data_9GH5
# 
_entry.id   9GH5 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9GH5         pdb_00009gh5 10.2210/pdb9gh5/pdb 
WWPDB D_1292140973 ?            ?                   
EMDB  EMD-51347    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1  'Structure model' 1 0 2025-04-02 ? 
2  'EM metadata'     1 0 2025-04-02 ? 
3  'Additional map'  1 0 2025-04-02 1 
4  FSC               1 0 2025-04-02 ? 
5  'Half map'        1 0 2025-04-02 1 
6  'Half map'        1 0 2025-04-02 2 
7  Image             1 0 2025-04-02 ? 
8  Mask              1 0 2025-04-02 1 
9  'Primary map'     1 0 2025-04-02 ? 
10 'Structure model' 1 1 2025-04-16 ? 
11 'Structure model' 1 2 2025-04-23 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1 1 'Structure model' repository 'Initial release' ? ? 
2 2 'EM metadata'     repository 'Initial release' ? ? 
3 3 'Additional map'  repository 'Initial release' ? ? 
4 4 FSC               repository 'Initial release' ? ? 
5 5 'Half map'        repository 'Initial release' ? ? 
6 6 'Half map'        repository 'Initial release' ? ? 
7 7 Image             repository 'Initial release' ? ? 
8 8 Mask              repository 'Initial release' ? ? 
9 9 'Primary map'     repository 'Initial release' ? ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 10 'Structure model' 'Data collection'     
2 10 'Structure model' 'Database references' 
3 11 'Structure model' 'Data collection'     
4 11 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 10 'Structure model' citation        
2 10 'Structure model' citation_author 
3 10 'Structure model' em_admin        
4 11 'Structure model' citation        
5 11 'Structure model' citation_author 
6 11 'Structure model' em_admin        
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  10 'Structure model' '_citation.country'                 
2  10 'Structure model' '_citation.journal_abbrev'          
3  10 'Structure model' '_citation.journal_id_ASTM'         
4  10 'Structure model' '_citation.journal_id_CSD'          
5  10 'Structure model' '_citation.journal_id_ISSN'         
6  10 'Structure model' '_citation.pdbx_database_id_DOI'    
7  10 'Structure model' '_citation.year'                    
8  10 'Structure model' '_em_admin.last_update'             
9  11 'Structure model' '_citation.journal_volume'          
10 11 'Structure model' '_citation.page_first'              
11 11 'Structure model' '_citation.page_last'               
12 11 'Structure model' '_citation.pdbx_database_id_PubMed' 
13 11 'Structure model' '_citation.title'                   
14 11 'Structure model' '_citation_author.identifier_ORCID' 
15 11 'Structure model' '_em_admin.last_update'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GH5 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-15 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
EMDB 'CbpF without CEACAM1'                                       EMD-51346 'other EM volume'      
EMDB 'Reconstruction focused on one CEACAM1'                      EMD-51348 'focused EM volume'    
EMDB 'Complex of Fusobacterium nucleatum CbpF with human CEACAM1' EMD-51347 'associated EM volume' 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              roderer@fmp-berlin.de 
_pdbx_contact_author.name_first         Daniel 
_pdbx_contact_author.name_last          Roderer 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7276-3467 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Marongiu, G.L.' 1 ? 
'Fink, U.'       2 ? 
'Roderer, D.'    3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Proc.Natl.Acad.Sci.USA 
_citation.journal_id_ASTM           PNASA6 
_citation.journal_id_CSD            0040 
_citation.journal_id_ISSN           1091-6490 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            122 
_citation.language                  ? 
_citation.page_first                e2418155122 
_citation.page_last                 e2418155122 
_citation.title                     
'Structural basis for immune cell binding of Fusobacterium nucleatum via the trimeric autotransporter adhesin CbpF.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1073/pnas.2418155122 
_citation.pdbx_database_id_PubMed   40198705 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Marongiu, G.L.'  1 ?                   
primary 'Fink, U.'        2 ?                   
primary 'Schopf, F.'      3 0000-0003-1929-6246 
primary 'Oder, A.'        4 ?                   
primary 'von Kries, J.P.' 5 ?                   
primary 'Roderer, D.'     6 0000-0002-7276-3467 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Cell surface protein'                                      51827.051 3  ? ? ? 
'full length protein, residues 25-274 are resolved'                     
2 polymer     man 'Carcinoembryonic antigen-related cell adhesion molecule 1' 44153.664 3  ? ? ? 
'CEACAM1 extracellular domain with C-terminal histag (Acro Biosystems)' 
3 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose                    221.208   18 ? ? ? ? 
4 water       nat water                                                       18.015    3  ? ? ? ? 
# 
_entity_name_com.entity_id   2 
_entity_name_com.name        'Biliary glycoprotein 1,BGP-1' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MKKTAIAIAVALAGFATVAQASAAPVIKAGTATDSTEAGVDNVANGVKSSAFGYDNKAIEKESSAFGTGNRATGEFSSAF
GFHNIASKIHSSAFGSNNAADGVNSSAFGFKNTVSGFNSSAFGSQYQVTGNFSGAFGMGEFNGQYQYKNEGNNSYMIGNK
NKIASGSDDNFILGNNVHIGGGINNSVALGNNSTVSASNTVSVGSSTLKRKIVNVGDGAISANSSDAVTGRQLYSGNGID
TAAWQNKLNVTRKNDYKDANDIDVNKWKAKLGVGSGGGGGAPVDAYTKSEADNKFANKTDLNDYTKKDDYKDANGIDVDK
WKAKLGTGAGTADIENLRNEVNEKIDDVKDEVRTVGSLSAALAGLHPMQYDPKAPVQVMAALGHYRDKQSVAVGASYYFN
DRFMMSTGIALSGEKRTKTMANVGFTLKLGKGSGVTYDETPQYVVQNEVKRLTVENQELKERVRNLEEKLNMLLKNKRSS
AWSHPQFEK
;
;MKKTAIAIAVALAGFATVAQASAAPVIKAGTATDSTEAGVDNVANGVKSSAFGYDNKAIEKESSAFGTGNRATGEFSSAF
GFHNIASKIHSSAFGSNNAADGVNSSAFGFKNTVSGFNSSAFGSQYQVTGNFSGAFGMGEFNGQYQYKNEGNNSYMIGNK
NKIASGSDDNFILGNNVHIGGGINNSVALGNNSTVSASNTVSVGSSTLKRKIVNVGDGAISANSSDAVTGRQLYSGNGID
TAAWQNKLNVTRKNDYKDANDIDVNKWKAKLGVGSGGGGGAPVDAYTKSEADNKFANKTDLNDYTKKDDYKDANGIDVDK
WKAKLGTGAGTADIENLRNEVNEKIDDVKDEVRTVGSLSAALAGLHPMQYDPKAPVQVMAALGHYRDKQSVAVGASYYFN
DRFMMSTGIALSGEKRTKTMANVGFTLKLGKGSGVTYDETPQYVVQNEVKRLTVENQELKERVRNLEEKLNMLLKNKRSS
AWSHPQFEK
;
A,B,C ? 
2 'polypeptide(L)' no no 
;QLTTESMPFNVAEGKEVLLLVHNLPQQLFGYSWYKGERVDGNRQIVGYAIGTQQATPGPANSGRETIYPNASLLIQNVTQ
NDTGFYTLQVIKSDLVNEEATGQFHVYPELPKPSISSNNSNPVEDKDAVAFTCEPETQDTTYLWWINNQSLPVSPRLQLS
NGNRTLTLLSVTRNDTGPYECEIQNPVSANRSDPVTLNVTYGPDTPTISPSDTYYRPGANLSLSCYAASNPPAQYSWLIN
GTFQQSTQELFIPNITVNNSGSYTCHANNSVTGCNRTTVKTIIVTELSPVVAKPQIKASKTTVTGDKDSVNLTCSTNDTG
ISIRWFFKNQSLPSSERMKLSQGNTTLSINPVKREDAGTYWCEVFNPISKNQSDPIMLNVNYNALPQENGLSPGHHHHHH
;
;QLTTESMPFNVAEGKEVLLLVHNLPQQLFGYSWYKGERVDGNRQIVGYAIGTQQATPGPANSGRETIYPNASLLIQNVTQ
NDTGFYTLQVIKSDLVNEEATGQFHVYPELPKPSISSNNSNPVEDKDAVAFTCEPETQDTTYLWWINNQSLPVSPRLQLS
NGNRTLTLLSVTRNDTGPYECEIQNPVSANRSDPVTLNVTYGPDTPTISPSDTYYRPGANLSLSCYAASNPPAQYSWLIN
GTFQQSTQELFIPNITVNNSGSYTCHANNSVTGCNRTTVKTIIVTELSPVVAKPQIKASKTTVTGDKDSVNLTCSTNDTG
ISIRWFFKNQSLPSSERMKLSQGNTTLSINPVKREDAGTYWCEVFNPISKNQSDPIMLNVNYNALPQENGLSPGHHHHHH
;
D,E,F ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 2-acetamido-2-deoxy-beta-D-glucopyranose NAG 
4 water                                    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   LYS n 
1 4   THR n 
1 5   ALA n 
1 6   ILE n 
1 7   ALA n 
1 8   ILE n 
1 9   ALA n 
1 10  VAL n 
1 11  ALA n 
1 12  LEU n 
1 13  ALA n 
1 14  GLY n 
1 15  PHE n 
1 16  ALA n 
1 17  THR n 
1 18  VAL n 
1 19  ALA n 
1 20  GLN n 
1 21  ALA n 
1 22  SER n 
1 23  ALA n 
1 24  ALA n 
1 25  PRO n 
1 26  VAL n 
1 27  ILE n 
1 28  LYS n 
1 29  ALA n 
1 30  GLY n 
1 31  THR n 
1 32  ALA n 
1 33  THR n 
1 34  ASP n 
1 35  SER n 
1 36  THR n 
1 37  GLU n 
1 38  ALA n 
1 39  GLY n 
1 40  VAL n 
1 41  ASP n 
1 42  ASN n 
1 43  VAL n 
1 44  ALA n 
1 45  ASN n 
1 46  GLY n 
1 47  VAL n 
1 48  LYS n 
1 49  SER n 
1 50  SER n 
1 51  ALA n 
1 52  PHE n 
1 53  GLY n 
1 54  TYR n 
1 55  ASP n 
1 56  ASN n 
1 57  LYS n 
1 58  ALA n 
1 59  ILE n 
1 60  GLU n 
1 61  LYS n 
1 62  GLU n 
1 63  SER n 
1 64  SER n 
1 65  ALA n 
1 66  PHE n 
1 67  GLY n 
1 68  THR n 
1 69  GLY n 
1 70  ASN n 
1 71  ARG n 
1 72  ALA n 
1 73  THR n 
1 74  GLY n 
1 75  GLU n 
1 76  PHE n 
1 77  SER n 
1 78  SER n 
1 79  ALA n 
1 80  PHE n 
1 81  GLY n 
1 82  PHE n 
1 83  HIS n 
1 84  ASN n 
1 85  ILE n 
1 86  ALA n 
1 87  SER n 
1 88  LYS n 
1 89  ILE n 
1 90  HIS n 
1 91  SER n 
1 92  SER n 
1 93  ALA n 
1 94  PHE n 
1 95  GLY n 
1 96  SER n 
1 97  ASN n 
1 98  ASN n 
1 99  ALA n 
1 100 ALA n 
1 101 ASP n 
1 102 GLY n 
1 103 VAL n 
1 104 ASN n 
1 105 SER n 
1 106 SER n 
1 107 ALA n 
1 108 PHE n 
1 109 GLY n 
1 110 PHE n 
1 111 LYS n 
1 112 ASN n 
1 113 THR n 
1 114 VAL n 
1 115 SER n 
1 116 GLY n 
1 117 PHE n 
1 118 ASN n 
1 119 SER n 
1 120 SER n 
1 121 ALA n 
1 122 PHE n 
1 123 GLY n 
1 124 SER n 
1 125 GLN n 
1 126 TYR n 
1 127 GLN n 
1 128 VAL n 
1 129 THR n 
1 130 GLY n 
1 131 ASN n 
1 132 PHE n 
1 133 SER n 
1 134 GLY n 
1 135 ALA n 
1 136 PHE n 
1 137 GLY n 
1 138 MET n 
1 139 GLY n 
1 140 GLU n 
1 141 PHE n 
1 142 ASN n 
1 143 GLY n 
1 144 GLN n 
1 145 TYR n 
1 146 GLN n 
1 147 TYR n 
1 148 LYS n 
1 149 ASN n 
1 150 GLU n 
1 151 GLY n 
1 152 ASN n 
1 153 ASN n 
1 154 SER n 
1 155 TYR n 
1 156 MET n 
1 157 ILE n 
1 158 GLY n 
1 159 ASN n 
1 160 LYS n 
1 161 ASN n 
1 162 LYS n 
1 163 ILE n 
1 164 ALA n 
1 165 SER n 
1 166 GLY n 
1 167 SER n 
1 168 ASP n 
1 169 ASP n 
1 170 ASN n 
1 171 PHE n 
1 172 ILE n 
1 173 LEU n 
1 174 GLY n 
1 175 ASN n 
1 176 ASN n 
1 177 VAL n 
1 178 HIS n 
1 179 ILE n 
1 180 GLY n 
1 181 GLY n 
1 182 GLY n 
1 183 ILE n 
1 184 ASN n 
1 185 ASN n 
1 186 SER n 
1 187 VAL n 
1 188 ALA n 
1 189 LEU n 
1 190 GLY n 
1 191 ASN n 
1 192 ASN n 
1 193 SER n 
1 194 THR n 
1 195 VAL n 
1 196 SER n 
1 197 ALA n 
1 198 SER n 
1 199 ASN n 
1 200 THR n 
1 201 VAL n 
1 202 SER n 
1 203 VAL n 
1 204 GLY n 
1 205 SER n 
1 206 SER n 
1 207 THR n 
1 208 LEU n 
1 209 LYS n 
1 210 ARG n 
1 211 LYS n 
1 212 ILE n 
1 213 VAL n 
1 214 ASN n 
1 215 VAL n 
1 216 GLY n 
1 217 ASP n 
1 218 GLY n 
1 219 ALA n 
1 220 ILE n 
1 221 SER n 
1 222 ALA n 
1 223 ASN n 
1 224 SER n 
1 225 SER n 
1 226 ASP n 
1 227 ALA n 
1 228 VAL n 
1 229 THR n 
1 230 GLY n 
1 231 ARG n 
1 232 GLN n 
1 233 LEU n 
1 234 TYR n 
1 235 SER n 
1 236 GLY n 
1 237 ASN n 
1 238 GLY n 
1 239 ILE n 
1 240 ASP n 
1 241 THR n 
1 242 ALA n 
1 243 ALA n 
1 244 TRP n 
1 245 GLN n 
1 246 ASN n 
1 247 LYS n 
1 248 LEU n 
1 249 ASN n 
1 250 VAL n 
1 251 THR n 
1 252 ARG n 
1 253 LYS n 
1 254 ASN n 
1 255 ASP n 
1 256 TYR n 
1 257 LYS n 
1 258 ASP n 
1 259 ALA n 
1 260 ASN n 
1 261 ASP n 
1 262 ILE n 
1 263 ASP n 
1 264 VAL n 
1 265 ASN n 
1 266 LYS n 
1 267 TRP n 
1 268 LYS n 
1 269 ALA n 
1 270 LYS n 
1 271 LEU n 
1 272 GLY n 
1 273 VAL n 
1 274 GLY n 
1 275 SER n 
1 276 GLY n 
1 277 GLY n 
1 278 GLY n 
1 279 GLY n 
1 280 GLY n 
1 281 ALA n 
1 282 PRO n 
1 283 VAL n 
1 284 ASP n 
1 285 ALA n 
1 286 TYR n 
1 287 THR n 
1 288 LYS n 
1 289 SER n 
1 290 GLU n 
1 291 ALA n 
1 292 ASP n 
1 293 ASN n 
1 294 LYS n 
1 295 PHE n 
1 296 ALA n 
1 297 ASN n 
1 298 LYS n 
1 299 THR n 
1 300 ASP n 
1 301 LEU n 
1 302 ASN n 
1 303 ASP n 
1 304 TYR n 
1 305 THR n 
1 306 LYS n 
1 307 LYS n 
1 308 ASP n 
1 309 ASP n 
1 310 TYR n 
1 311 LYS n 
1 312 ASP n 
1 313 ALA n 
1 314 ASN n 
1 315 GLY n 
1 316 ILE n 
1 317 ASP n 
1 318 VAL n 
1 319 ASP n 
1 320 LYS n 
1 321 TRP n 
1 322 LYS n 
1 323 ALA n 
1 324 LYS n 
1 325 LEU n 
1 326 GLY n 
1 327 THR n 
1 328 GLY n 
1 329 ALA n 
1 330 GLY n 
1 331 THR n 
1 332 ALA n 
1 333 ASP n 
1 334 ILE n 
1 335 GLU n 
1 336 ASN n 
1 337 LEU n 
1 338 ARG n 
1 339 ASN n 
1 340 GLU n 
1 341 VAL n 
1 342 ASN n 
1 343 GLU n 
1 344 LYS n 
1 345 ILE n 
1 346 ASP n 
1 347 ASP n 
1 348 VAL n 
1 349 LYS n 
1 350 ASP n 
1 351 GLU n 
1 352 VAL n 
1 353 ARG n 
1 354 THR n 
1 355 VAL n 
1 356 GLY n 
1 357 SER n 
1 358 LEU n 
1 359 SER n 
1 360 ALA n 
1 361 ALA n 
1 362 LEU n 
1 363 ALA n 
1 364 GLY n 
1 365 LEU n 
1 366 HIS n 
1 367 PRO n 
1 368 MET n 
1 369 GLN n 
1 370 TYR n 
1 371 ASP n 
1 372 PRO n 
1 373 LYS n 
1 374 ALA n 
1 375 PRO n 
1 376 VAL n 
1 377 GLN n 
1 378 VAL n 
1 379 MET n 
1 380 ALA n 
1 381 ALA n 
1 382 LEU n 
1 383 GLY n 
1 384 HIS n 
1 385 TYR n 
1 386 ARG n 
1 387 ASP n 
1 388 LYS n 
1 389 GLN n 
1 390 SER n 
1 391 VAL n 
1 392 ALA n 
1 393 VAL n 
1 394 GLY n 
1 395 ALA n 
1 396 SER n 
1 397 TYR n 
1 398 TYR n 
1 399 PHE n 
1 400 ASN n 
1 401 ASP n 
1 402 ARG n 
1 403 PHE n 
1 404 MET n 
1 405 MET n 
1 406 SER n 
1 407 THR n 
1 408 GLY n 
1 409 ILE n 
1 410 ALA n 
1 411 LEU n 
1 412 SER n 
1 413 GLY n 
1 414 GLU n 
1 415 LYS n 
1 416 ARG n 
1 417 THR n 
1 418 LYS n 
1 419 THR n 
1 420 MET n 
1 421 ALA n 
1 422 ASN n 
1 423 VAL n 
1 424 GLY n 
1 425 PHE n 
1 426 THR n 
1 427 LEU n 
1 428 LYS n 
1 429 LEU n 
1 430 GLY n 
1 431 LYS n 
1 432 GLY n 
1 433 SER n 
1 434 GLY n 
1 435 VAL n 
1 436 THR n 
1 437 TYR n 
1 438 ASP n 
1 439 GLU n 
1 440 THR n 
1 441 PRO n 
1 442 GLN n 
1 443 TYR n 
1 444 VAL n 
1 445 VAL n 
1 446 GLN n 
1 447 ASN n 
1 448 GLU n 
1 449 VAL n 
1 450 LYS n 
1 451 ARG n 
1 452 LEU n 
1 453 THR n 
1 454 VAL n 
1 455 GLU n 
1 456 ASN n 
1 457 GLN n 
1 458 GLU n 
1 459 LEU n 
1 460 LYS n 
1 461 GLU n 
1 462 ARG n 
1 463 VAL n 
1 464 ARG n 
1 465 ASN n 
1 466 LEU n 
1 467 GLU n 
1 468 GLU n 
1 469 LYS n 
1 470 LEU n 
1 471 ASN n 
1 472 MET n 
1 473 LEU n 
1 474 LEU n 
1 475 LYS n 
1 476 ASN n 
1 477 LYS n 
1 478 ARG n 
1 479 SER n 
1 480 SER n 
1 481 ALA n 
1 482 TRP n 
1 483 SER n 
1 484 HIS n 
1 485 PRO n 
1 486 GLN n 
1 487 PHE n 
1 488 GLU n 
1 489 LYS n 
2 1   GLN n 
2 2   LEU n 
2 3   THR n 
2 4   THR n 
2 5   GLU n 
2 6   SER n 
2 7   MET n 
2 8   PRO n 
2 9   PHE n 
2 10  ASN n 
2 11  VAL n 
2 12  ALA n 
2 13  GLU n 
2 14  GLY n 
2 15  LYS n 
2 16  GLU n 
2 17  VAL n 
2 18  LEU n 
2 19  LEU n 
2 20  LEU n 
2 21  VAL n 
2 22  HIS n 
2 23  ASN n 
2 24  LEU n 
2 25  PRO n 
2 26  GLN n 
2 27  GLN n 
2 28  LEU n 
2 29  PHE n 
2 30  GLY n 
2 31  TYR n 
2 32  SER n 
2 33  TRP n 
2 34  TYR n 
2 35  LYS n 
2 36  GLY n 
2 37  GLU n 
2 38  ARG n 
2 39  VAL n 
2 40  ASP n 
2 41  GLY n 
2 42  ASN n 
2 43  ARG n 
2 44  GLN n 
2 45  ILE n 
2 46  VAL n 
2 47  GLY n 
2 48  TYR n 
2 49  ALA n 
2 50  ILE n 
2 51  GLY n 
2 52  THR n 
2 53  GLN n 
2 54  GLN n 
2 55  ALA n 
2 56  THR n 
2 57  PRO n 
2 58  GLY n 
2 59  PRO n 
2 60  ALA n 
2 61  ASN n 
2 62  SER n 
2 63  GLY n 
2 64  ARG n 
2 65  GLU n 
2 66  THR n 
2 67  ILE n 
2 68  TYR n 
2 69  PRO n 
2 70  ASN n 
2 71  ALA n 
2 72  SER n 
2 73  LEU n 
2 74  LEU n 
2 75  ILE n 
2 76  GLN n 
2 77  ASN n 
2 78  VAL n 
2 79  THR n 
2 80  GLN n 
2 81  ASN n 
2 82  ASP n 
2 83  THR n 
2 84  GLY n 
2 85  PHE n 
2 86  TYR n 
2 87  THR n 
2 88  LEU n 
2 89  GLN n 
2 90  VAL n 
2 91  ILE n 
2 92  LYS n 
2 93  SER n 
2 94  ASP n 
2 95  LEU n 
2 96  VAL n 
2 97  ASN n 
2 98  GLU n 
2 99  GLU n 
2 100 ALA n 
2 101 THR n 
2 102 GLY n 
2 103 GLN n 
2 104 PHE n 
2 105 HIS n 
2 106 VAL n 
2 107 TYR n 
2 108 PRO n 
2 109 GLU n 
2 110 LEU n 
2 111 PRO n 
2 112 LYS n 
2 113 PRO n 
2 114 SER n 
2 115 ILE n 
2 116 SER n 
2 117 SER n 
2 118 ASN n 
2 119 ASN n 
2 120 SER n 
2 121 ASN n 
2 122 PRO n 
2 123 VAL n 
2 124 GLU n 
2 125 ASP n 
2 126 LYS n 
2 127 ASP n 
2 128 ALA n 
2 129 VAL n 
2 130 ALA n 
2 131 PHE n 
2 132 THR n 
2 133 CYS n 
2 134 GLU n 
2 135 PRO n 
2 136 GLU n 
2 137 THR n 
2 138 GLN n 
2 139 ASP n 
2 140 THR n 
2 141 THR n 
2 142 TYR n 
2 143 LEU n 
2 144 TRP n 
2 145 TRP n 
2 146 ILE n 
2 147 ASN n 
2 148 ASN n 
2 149 GLN n 
2 150 SER n 
2 151 LEU n 
2 152 PRO n 
2 153 VAL n 
2 154 SER n 
2 155 PRO n 
2 156 ARG n 
2 157 LEU n 
2 158 GLN n 
2 159 LEU n 
2 160 SER n 
2 161 ASN n 
2 162 GLY n 
2 163 ASN n 
2 164 ARG n 
2 165 THR n 
2 166 LEU n 
2 167 THR n 
2 168 LEU n 
2 169 LEU n 
2 170 SER n 
2 171 VAL n 
2 172 THR n 
2 173 ARG n 
2 174 ASN n 
2 175 ASP n 
2 176 THR n 
2 177 GLY n 
2 178 PRO n 
2 179 TYR n 
2 180 GLU n 
2 181 CYS n 
2 182 GLU n 
2 183 ILE n 
2 184 GLN n 
2 185 ASN n 
2 186 PRO n 
2 187 VAL n 
2 188 SER n 
2 189 ALA n 
2 190 ASN n 
2 191 ARG n 
2 192 SER n 
2 193 ASP n 
2 194 PRO n 
2 195 VAL n 
2 196 THR n 
2 197 LEU n 
2 198 ASN n 
2 199 VAL n 
2 200 THR n 
2 201 TYR n 
2 202 GLY n 
2 203 PRO n 
2 204 ASP n 
2 205 THR n 
2 206 PRO n 
2 207 THR n 
2 208 ILE n 
2 209 SER n 
2 210 PRO n 
2 211 SER n 
2 212 ASP n 
2 213 THR n 
2 214 TYR n 
2 215 TYR n 
2 216 ARG n 
2 217 PRO n 
2 218 GLY n 
2 219 ALA n 
2 220 ASN n 
2 221 LEU n 
2 222 SER n 
2 223 LEU n 
2 224 SER n 
2 225 CYS n 
2 226 TYR n 
2 227 ALA n 
2 228 ALA n 
2 229 SER n 
2 230 ASN n 
2 231 PRO n 
2 232 PRO n 
2 233 ALA n 
2 234 GLN n 
2 235 TYR n 
2 236 SER n 
2 237 TRP n 
2 238 LEU n 
2 239 ILE n 
2 240 ASN n 
2 241 GLY n 
2 242 THR n 
2 243 PHE n 
2 244 GLN n 
2 245 GLN n 
2 246 SER n 
2 247 THR n 
2 248 GLN n 
2 249 GLU n 
2 250 LEU n 
2 251 PHE n 
2 252 ILE n 
2 253 PRO n 
2 254 ASN n 
2 255 ILE n 
2 256 THR n 
2 257 VAL n 
2 258 ASN n 
2 259 ASN n 
2 260 SER n 
2 261 GLY n 
2 262 SER n 
2 263 TYR n 
2 264 THR n 
2 265 CYS n 
2 266 HIS n 
2 267 ALA n 
2 268 ASN n 
2 269 ASN n 
2 270 SER n 
2 271 VAL n 
2 272 THR n 
2 273 GLY n 
2 274 CYS n 
2 275 ASN n 
2 276 ARG n 
2 277 THR n 
2 278 THR n 
2 279 VAL n 
2 280 LYS n 
2 281 THR n 
2 282 ILE n 
2 283 ILE n 
2 284 VAL n 
2 285 THR n 
2 286 GLU n 
2 287 LEU n 
2 288 SER n 
2 289 PRO n 
2 290 VAL n 
2 291 VAL n 
2 292 ALA n 
2 293 LYS n 
2 294 PRO n 
2 295 GLN n 
2 296 ILE n 
2 297 LYS n 
2 298 ALA n 
2 299 SER n 
2 300 LYS n 
2 301 THR n 
2 302 THR n 
2 303 VAL n 
2 304 THR n 
2 305 GLY n 
2 306 ASP n 
2 307 LYS n 
2 308 ASP n 
2 309 SER n 
2 310 VAL n 
2 311 ASN n 
2 312 LEU n 
2 313 THR n 
2 314 CYS n 
2 315 SER n 
2 316 THR n 
2 317 ASN n 
2 318 ASP n 
2 319 THR n 
2 320 GLY n 
2 321 ILE n 
2 322 SER n 
2 323 ILE n 
2 324 ARG n 
2 325 TRP n 
2 326 PHE n 
2 327 PHE n 
2 328 LYS n 
2 329 ASN n 
2 330 GLN n 
2 331 SER n 
2 332 LEU n 
2 333 PRO n 
2 334 SER n 
2 335 SER n 
2 336 GLU n 
2 337 ARG n 
2 338 MET n 
2 339 LYS n 
2 340 LEU n 
2 341 SER n 
2 342 GLN n 
2 343 GLY n 
2 344 ASN n 
2 345 THR n 
2 346 THR n 
2 347 LEU n 
2 348 SER n 
2 349 ILE n 
2 350 ASN n 
2 351 PRO n 
2 352 VAL n 
2 353 LYS n 
2 354 ARG n 
2 355 GLU n 
2 356 ASP n 
2 357 ALA n 
2 358 GLY n 
2 359 THR n 
2 360 TYR n 
2 361 TRP n 
2 362 CYS n 
2 363 GLU n 
2 364 VAL n 
2 365 PHE n 
2 366 ASN n 
2 367 PRO n 
2 368 ILE n 
2 369 SER n 
2 370 LYS n 
2 371 ASN n 
2 372 GLN n 
2 373 SER n 
2 374 ASP n 
2 375 PRO n 
2 376 ILE n 
2 377 MET n 
2 378 LEU n 
2 379 ASN n 
2 380 VAL n 
2 381 ASN n 
2 382 TYR n 
2 383 ASN n 
2 384 ALA n 
2 385 LEU n 
2 386 PRO n 
2 387 GLN n 
2 388 GLU n 
2 389 ASN n 
2 390 GLY n 
2 391 LEU n 
2 392 SER n 
2 393 PRO n 
2 394 GLY n 
2 395 HIS n 
2 396 HIS n 
2 397 HIS n 
2 398 HIS n 
2 399 HIS n 
2 400 HIS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 489 ?     ? FN1499               ? ? ? ? ? ? 'Fusobacterium nucleatum' 851  ? ? ? ? ? ? ? ? 
'Escherichia coli' 562  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 400 human ? 'CEACAM1, BGP, BGP1' ? ? ? ? ? ? 'Homo sapiens'            9606 ? ? ? ? ? ? ? ? 
'Homo sapiens'     9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking'          y ALANINE                                  ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking'          y ARGININE                                 ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking'          y ASPARAGINE                               ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking'          y 'ASPARTIC ACID'                          ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking'          y CYSTEINE                                 ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking'          y GLUTAMINE                                ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking'          y 'GLUTAMIC ACID'                          ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'            y GLYCINE                                  ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking'          y HISTIDINE                                ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer                  . WATER                                    ? 'H2 O'           18.015  
ILE 'L-peptide linking'          y ISOLEUCINE                               ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking'          y LEUCINE                                  ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking'          y LYSINE                                   ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking'          y METHIONINE                               ? 'C5 H11 N O2 S'  149.211 
NAG 'D-saccharide, beta linking' . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
PHE 'L-peptide linking'          y PHENYLALANINE                            ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking'          y PROLINE                                  ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking'          y SERINE                                   ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking'          y THREONINE                                ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking'          y TRYPTOPHAN                               ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking'          y TYROSINE                                 ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking'          y VALINE                                   ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   3   ?   ?   ?   A . n 
A 1 2   LYS 2   4   ?   ?   ?   A . n 
A 1 3   LYS 3   5   ?   ?   ?   A . n 
A 1 4   THR 4   6   ?   ?   ?   A . n 
A 1 5   ALA 5   7   ?   ?   ?   A . n 
A 1 6   ILE 6   8   ?   ?   ?   A . n 
A 1 7   ALA 7   9   ?   ?   ?   A . n 
A 1 8   ILE 8   10  ?   ?   ?   A . n 
A 1 9   ALA 9   11  ?   ?   ?   A . n 
A 1 10  VAL 10  12  ?   ?   ?   A . n 
A 1 11  ALA 11  13  ?   ?   ?   A . n 
A 1 12  LEU 12  14  ?   ?   ?   A . n 
A 1 13  ALA 13  15  ?   ?   ?   A . n 
A 1 14  GLY 14  16  ?   ?   ?   A . n 
A 1 15  PHE 15  17  ?   ?   ?   A . n 
A 1 16  ALA 16  18  ?   ?   ?   A . n 
A 1 17  THR 17  19  ?   ?   ?   A . n 
A 1 18  VAL 18  20  ?   ?   ?   A . n 
A 1 19  ALA 19  21  ?   ?   ?   A . n 
A 1 20  GLN 20  22  ?   ?   ?   A . n 
A 1 21  ALA 21  23  ?   ?   ?   A . n 
A 1 22  SER 22  24  ?   ?   ?   A . n 
A 1 23  ALA 23  25  ?   ?   ?   A . n 
A 1 24  ALA 24  26  26  ALA ALA A . n 
A 1 25  PRO 25  27  27  PRO PRO A . n 
A 1 26  VAL 26  28  28  VAL VAL A . n 
A 1 27  ILE 27  29  29  ILE ILE A . n 
A 1 28  LYS 28  30  30  LYS LYS A . n 
A 1 29  ALA 29  31  31  ALA ALA A . n 
A 1 30  GLY 30  32  32  GLY GLY A . n 
A 1 31  THR 31  33  33  THR THR A . n 
A 1 32  ALA 32  34  34  ALA ALA A . n 
A 1 33  THR 33  35  35  THR THR A . n 
A 1 34  ASP 34  36  36  ASP ASP A . n 
A 1 35  SER 35  37  37  SER SER A . n 
A 1 36  THR 36  38  38  THR THR A . n 
A 1 37  GLU 37  39  39  GLU GLU A . n 
A 1 38  ALA 38  40  40  ALA ALA A . n 
A 1 39  GLY 39  41  41  GLY GLY A . n 
A 1 40  VAL 40  42  42  VAL VAL A . n 
A 1 41  ASP 41  43  43  ASP ASP A . n 
A 1 42  ASN 42  44  44  ASN ASN A . n 
A 1 43  VAL 43  45  45  VAL VAL A . n 
A 1 44  ALA 44  46  46  ALA ALA A . n 
A 1 45  ASN 45  47  47  ASN ASN A . n 
A 1 46  GLY 46  48  48  GLY GLY A . n 
A 1 47  VAL 47  49  49  VAL VAL A . n 
A 1 48  LYS 48  50  50  LYS LYS A . n 
A 1 49  SER 49  51  51  SER SER A . n 
A 1 50  SER 50  52  52  SER SER A . n 
A 1 51  ALA 51  53  53  ALA ALA A . n 
A 1 52  PHE 52  54  54  PHE PHE A . n 
A 1 53  GLY 53  55  55  GLY GLY A . n 
A 1 54  TYR 54  56  56  TYR TYR A . n 
A 1 55  ASP 55  57  57  ASP ASP A . n 
A 1 56  ASN 56  58  58  ASN ASN A . n 
A 1 57  LYS 57  59  59  LYS LYS A . n 
A 1 58  ALA 58  60  60  ALA ALA A . n 
A 1 59  ILE 59  61  61  ILE ILE A . n 
A 1 60  GLU 60  62  62  GLU GLU A . n 
A 1 61  LYS 61  63  63  LYS LYS A . n 
A 1 62  GLU 62  64  64  GLU GLU A . n 
A 1 63  SER 63  65  65  SER SER A . n 
A 1 64  SER 64  66  66  SER SER A . n 
A 1 65  ALA 65  67  67  ALA ALA A . n 
A 1 66  PHE 66  68  68  PHE PHE A . n 
A 1 67  GLY 67  69  69  GLY GLY A . n 
A 1 68  THR 68  70  70  THR THR A . n 
A 1 69  GLY 69  71  71  GLY GLY A . n 
A 1 70  ASN 70  72  72  ASN ASN A . n 
A 1 71  ARG 71  73  73  ARG ARG A . n 
A 1 72  ALA 72  74  74  ALA ALA A . n 
A 1 73  THR 73  75  75  THR THR A . n 
A 1 74  GLY 74  76  76  GLY GLY A . n 
A 1 75  GLU 75  77  77  GLU GLU A . n 
A 1 76  PHE 76  78  78  PHE PHE A . n 
A 1 77  SER 77  79  79  SER SER A . n 
A 1 78  SER 78  80  80  SER SER A . n 
A 1 79  ALA 79  81  81  ALA ALA A . n 
A 1 80  PHE 80  82  82  PHE PHE A . n 
A 1 81  GLY 81  83  83  GLY GLY A . n 
A 1 82  PHE 82  84  84  PHE PHE A . n 
A 1 83  HIS 83  85  85  HIS HIS A . n 
A 1 84  ASN 84  86  86  ASN ASN A . n 
A 1 85  ILE 85  87  87  ILE ILE A . n 
A 1 86  ALA 86  88  88  ALA ALA A . n 
A 1 87  SER 87  89  89  SER SER A . n 
A 1 88  LYS 88  90  90  LYS LYS A . n 
A 1 89  ILE 89  91  91  ILE ILE A . n 
A 1 90  HIS 90  92  92  HIS HIS A . n 
A 1 91  SER 91  93  93  SER SER A . n 
A 1 92  SER 92  94  94  SER SER A . n 
A 1 93  ALA 93  95  95  ALA ALA A . n 
A 1 94  PHE 94  96  96  PHE PHE A . n 
A 1 95  GLY 95  97  97  GLY GLY A . n 
A 1 96  SER 96  98  98  SER SER A . n 
A 1 97  ASN 97  99  99  ASN ASN A . n 
A 1 98  ASN 98  100 100 ASN ASN A . n 
A 1 99  ALA 99  101 101 ALA ALA A . n 
A 1 100 ALA 100 102 102 ALA ALA A . n 
A 1 101 ASP 101 103 103 ASP ASP A . n 
A 1 102 GLY 102 104 104 GLY GLY A . n 
A 1 103 VAL 103 105 105 VAL VAL A . n 
A 1 104 ASN 104 106 106 ASN ASN A . n 
A 1 105 SER 105 107 107 SER SER A . n 
A 1 106 SER 106 108 108 SER SER A . n 
A 1 107 ALA 107 109 109 ALA ALA A . n 
A 1 108 PHE 108 110 110 PHE PHE A . n 
A 1 109 GLY 109 111 111 GLY GLY A . n 
A 1 110 PHE 110 112 112 PHE PHE A . n 
A 1 111 LYS 111 113 113 LYS LYS A . n 
A 1 112 ASN 112 114 114 ASN ASN A . n 
A 1 113 THR 113 115 115 THR THR A . n 
A 1 114 VAL 114 116 116 VAL VAL A . n 
A 1 115 SER 115 117 117 SER SER A . n 
A 1 116 GLY 116 118 118 GLY GLY A . n 
A 1 117 PHE 117 119 119 PHE PHE A . n 
A 1 118 ASN 118 120 120 ASN ASN A . n 
A 1 119 SER 119 121 121 SER SER A . n 
A 1 120 SER 120 122 122 SER SER A . n 
A 1 121 ALA 121 123 123 ALA ALA A . n 
A 1 122 PHE 122 124 124 PHE PHE A . n 
A 1 123 GLY 123 125 125 GLY GLY A . n 
A 1 124 SER 124 126 126 SER SER A . n 
A 1 125 GLN 125 127 127 GLN GLN A . n 
A 1 126 TYR 126 128 128 TYR TYR A . n 
A 1 127 GLN 127 129 129 GLN GLN A . n 
A 1 128 VAL 128 130 130 VAL VAL A . n 
A 1 129 THR 129 131 131 THR THR A . n 
A 1 130 GLY 130 132 132 GLY GLY A . n 
A 1 131 ASN 131 133 133 ASN ASN A . n 
A 1 132 PHE 132 134 134 PHE PHE A . n 
A 1 133 SER 133 135 135 SER SER A . n 
A 1 134 GLY 134 136 136 GLY GLY A . n 
A 1 135 ALA 135 137 137 ALA ALA A . n 
A 1 136 PHE 136 138 138 PHE PHE A . n 
A 1 137 GLY 137 139 139 GLY GLY A . n 
A 1 138 MET 138 140 140 MET MET A . n 
A 1 139 GLY 139 141 141 GLY GLY A . n 
A 1 140 GLU 140 142 142 GLU GLU A . n 
A 1 141 PHE 141 143 143 PHE PHE A . n 
A 1 142 ASN 142 144 144 ASN ASN A . n 
A 1 143 GLY 143 145 145 GLY GLY A . n 
A 1 144 GLN 144 146 146 GLN GLN A . n 
A 1 145 TYR 145 147 147 TYR TYR A . n 
A 1 146 GLN 146 148 148 GLN GLN A . n 
A 1 147 TYR 147 149 149 TYR TYR A . n 
A 1 148 LYS 148 150 150 LYS LYS A . n 
A 1 149 ASN 149 151 151 ASN ASN A . n 
A 1 150 GLU 150 152 152 GLU GLU A . n 
A 1 151 GLY 151 153 153 GLY GLY A . n 
A 1 152 ASN 152 154 154 ASN ASN A . n 
A 1 153 ASN 153 155 155 ASN ASN A . n 
A 1 154 SER 154 156 156 SER SER A . n 
A 1 155 TYR 155 157 157 TYR TYR A . n 
A 1 156 MET 156 158 158 MET MET A . n 
A 1 157 ILE 157 159 159 ILE ILE A . n 
A 1 158 GLY 158 160 160 GLY GLY A . n 
A 1 159 ASN 159 161 161 ASN ASN A . n 
A 1 160 LYS 160 162 162 LYS LYS A . n 
A 1 161 ASN 161 163 163 ASN ASN A . n 
A 1 162 LYS 162 164 164 LYS LYS A . n 
A 1 163 ILE 163 165 165 ILE ILE A . n 
A 1 164 ALA 164 166 166 ALA ALA A . n 
A 1 165 SER 165 167 167 SER SER A . n 
A 1 166 GLY 166 168 168 GLY GLY A . n 
A 1 167 SER 167 169 169 SER SER A . n 
A 1 168 ASP 168 170 170 ASP ASP A . n 
A 1 169 ASP 169 171 171 ASP ASP A . n 
A 1 170 ASN 170 172 172 ASN ASN A . n 
A 1 171 PHE 171 173 173 PHE PHE A . n 
A 1 172 ILE 172 174 174 ILE ILE A . n 
A 1 173 LEU 173 175 175 LEU LEU A . n 
A 1 174 GLY 174 176 176 GLY GLY A . n 
A 1 175 ASN 175 177 177 ASN ASN A . n 
A 1 176 ASN 176 178 178 ASN ASN A . n 
A 1 177 VAL 177 179 179 VAL VAL A . n 
A 1 178 HIS 178 180 180 HIS HIS A . n 
A 1 179 ILE 179 181 181 ILE ILE A . n 
A 1 180 GLY 180 182 182 GLY GLY A . n 
A 1 181 GLY 181 183 183 GLY GLY A . n 
A 1 182 GLY 182 184 184 GLY GLY A . n 
A 1 183 ILE 183 185 185 ILE ILE A . n 
A 1 184 ASN 184 186 186 ASN ASN A . n 
A 1 185 ASN 185 187 187 ASN ASN A . n 
A 1 186 SER 186 188 188 SER SER A . n 
A 1 187 VAL 187 189 189 VAL VAL A . n 
A 1 188 ALA 188 190 190 ALA ALA A . n 
A 1 189 LEU 189 191 191 LEU LEU A . n 
A 1 190 GLY 190 192 192 GLY GLY A . n 
A 1 191 ASN 191 193 193 ASN ASN A . n 
A 1 192 ASN 192 194 194 ASN ASN A . n 
A 1 193 SER 193 195 195 SER SER A . n 
A 1 194 THR 194 196 196 THR THR A . n 
A 1 195 VAL 195 197 197 VAL VAL A . n 
A 1 196 SER 196 198 198 SER SER A . n 
A 1 197 ALA 197 199 199 ALA ALA A . n 
A 1 198 SER 198 200 200 SER SER A . n 
A 1 199 ASN 199 201 201 ASN ASN A . n 
A 1 200 THR 200 202 202 THR THR A . n 
A 1 201 VAL 201 203 203 VAL VAL A . n 
A 1 202 SER 202 204 204 SER SER A . n 
A 1 203 VAL 203 205 205 VAL VAL A . n 
A 1 204 GLY 204 206 206 GLY GLY A . n 
A 1 205 SER 205 207 207 SER SER A . n 
A 1 206 SER 206 208 208 SER SER A . n 
A 1 207 THR 207 209 209 THR THR A . n 
A 1 208 LEU 208 210 210 LEU LEU A . n 
A 1 209 LYS 209 211 211 LYS LYS A . n 
A 1 210 ARG 210 212 212 ARG ARG A . n 
A 1 211 LYS 211 213 213 LYS LYS A . n 
A 1 212 ILE 212 214 214 ILE ILE A . n 
A 1 213 VAL 213 215 215 VAL VAL A . n 
A 1 214 ASN 214 216 216 ASN ASN A . n 
A 1 215 VAL 215 217 217 VAL VAL A . n 
A 1 216 GLY 216 218 218 GLY GLY A . n 
A 1 217 ASP 217 219 219 ASP ASP A . n 
A 1 218 GLY 218 220 220 GLY GLY A . n 
A 1 219 ALA 219 221 221 ALA ALA A . n 
A 1 220 ILE 220 222 222 ILE ILE A . n 
A 1 221 SER 221 223 223 SER SER A . n 
A 1 222 ALA 222 224 224 ALA ALA A . n 
A 1 223 ASN 223 225 225 ASN ASN A . n 
A 1 224 SER 224 226 226 SER SER A . n 
A 1 225 SER 225 227 227 SER SER A . n 
A 1 226 ASP 226 228 228 ASP ASP A . n 
A 1 227 ALA 227 229 229 ALA ALA A . n 
A 1 228 VAL 228 230 230 VAL VAL A . n 
A 1 229 THR 229 231 231 THR THR A . n 
A 1 230 GLY 230 232 232 GLY GLY A . n 
A 1 231 ARG 231 233 233 ARG ARG A . n 
A 1 232 GLN 232 234 234 GLN GLN A . n 
A 1 233 LEU 233 235 235 LEU LEU A . n 
A 1 234 TYR 234 236 236 TYR TYR A . n 
A 1 235 SER 235 237 237 SER SER A . n 
A 1 236 GLY 236 238 238 GLY GLY A . n 
A 1 237 ASN 237 239 239 ASN ASN A . n 
A 1 238 GLY 238 240 240 GLY GLY A . n 
A 1 239 ILE 239 241 241 ILE ILE A . n 
A 1 240 ASP 240 242 242 ASP ASP A . n 
A 1 241 THR 241 243 243 THR THR A . n 
A 1 242 ALA 242 244 244 ALA ALA A . n 
A 1 243 ALA 243 245 245 ALA ALA A . n 
A 1 244 TRP 244 246 246 TRP TRP A . n 
A 1 245 GLN 245 247 247 GLN GLN A . n 
A 1 246 ASN 246 248 248 ASN ASN A . n 
A 1 247 LYS 247 249 249 LYS LYS A . n 
A 1 248 LEU 248 250 250 LEU LEU A . n 
A 1 249 ASN 249 251 251 ASN ASN A . n 
A 1 250 VAL 250 252 252 VAL VAL A . n 
A 1 251 THR 251 253 253 THR THR A . n 
A 1 252 ARG 252 254 254 ARG ARG A . n 
A 1 253 LYS 253 255 255 LYS LYS A . n 
A 1 254 ASN 254 256 256 ASN ASN A . n 
A 1 255 ASP 255 257 257 ASP ASP A . n 
A 1 256 TYR 256 258 258 TYR TYR A . n 
A 1 257 LYS 257 259 259 LYS LYS A . n 
A 1 258 ASP 258 260 260 ASP ASP A . n 
A 1 259 ALA 259 261 261 ALA ALA A . n 
A 1 260 ASN 260 262 262 ASN ASN A . n 
A 1 261 ASP 261 263 263 ASP ASP A . n 
A 1 262 ILE 262 264 264 ILE ILE A . n 
A 1 263 ASP 263 265 265 ASP ASP A . n 
A 1 264 VAL 264 266 266 VAL VAL A . n 
A 1 265 ASN 265 267 267 ASN ASN A . n 
A 1 266 LYS 266 268 268 LYS LYS A . n 
A 1 267 TRP 267 269 269 TRP TRP A . n 
A 1 268 LYS 268 270 270 LYS LYS A . n 
A 1 269 ALA 269 271 271 ALA ALA A . n 
A 1 270 LYS 270 272 272 LYS LYS A . n 
A 1 271 LEU 271 273 273 LEU LEU A . n 
A 1 272 GLY 272 274 274 GLY GLY A . n 
A 1 273 VAL 273 275 ?   ?   ?   A . n 
A 1 274 GLY 274 276 ?   ?   ?   A . n 
A 1 275 SER 275 277 ?   ?   ?   A . n 
A 1 276 GLY 276 278 ?   ?   ?   A . n 
A 1 277 GLY 277 279 ?   ?   ?   A . n 
A 1 278 GLY 278 280 ?   ?   ?   A . n 
A 1 279 GLY 279 281 ?   ?   ?   A . n 
A 1 280 GLY 280 282 ?   ?   ?   A . n 
A 1 281 ALA 281 283 ?   ?   ?   A . n 
A 1 282 PRO 282 284 ?   ?   ?   A . n 
A 1 283 VAL 283 285 ?   ?   ?   A . n 
A 1 284 ASP 284 286 ?   ?   ?   A . n 
A 1 285 ALA 285 287 ?   ?   ?   A . n 
A 1 286 TYR 286 288 ?   ?   ?   A . n 
A 1 287 THR 287 289 ?   ?   ?   A . n 
A 1 288 LYS 288 290 ?   ?   ?   A . n 
A 1 289 SER 289 291 ?   ?   ?   A . n 
A 1 290 GLU 290 292 ?   ?   ?   A . n 
A 1 291 ALA 291 293 ?   ?   ?   A . n 
A 1 292 ASP 292 294 ?   ?   ?   A . n 
A 1 293 ASN 293 295 ?   ?   ?   A . n 
A 1 294 LYS 294 296 ?   ?   ?   A . n 
A 1 295 PHE 295 297 ?   ?   ?   A . n 
A 1 296 ALA 296 298 ?   ?   ?   A . n 
A 1 297 ASN 297 299 ?   ?   ?   A . n 
A 1 298 LYS 298 300 ?   ?   ?   A . n 
A 1 299 THR 299 301 ?   ?   ?   A . n 
A 1 300 ASP 300 302 ?   ?   ?   A . n 
A 1 301 LEU 301 303 ?   ?   ?   A . n 
A 1 302 ASN 302 304 ?   ?   ?   A . n 
A 1 303 ASP 303 305 ?   ?   ?   A . n 
A 1 304 TYR 304 306 ?   ?   ?   A . n 
A 1 305 THR 305 307 ?   ?   ?   A . n 
A 1 306 LYS 306 308 ?   ?   ?   A . n 
A 1 307 LYS 307 309 ?   ?   ?   A . n 
A 1 308 ASP 308 310 ?   ?   ?   A . n 
A 1 309 ASP 309 311 ?   ?   ?   A . n 
A 1 310 TYR 310 312 ?   ?   ?   A . n 
A 1 311 LYS 311 313 ?   ?   ?   A . n 
A 1 312 ASP 312 314 ?   ?   ?   A . n 
A 1 313 ALA 313 315 ?   ?   ?   A . n 
A 1 314 ASN 314 316 ?   ?   ?   A . n 
A 1 315 GLY 315 317 ?   ?   ?   A . n 
A 1 316 ILE 316 318 ?   ?   ?   A . n 
A 1 317 ASP 317 319 ?   ?   ?   A . n 
A 1 318 VAL 318 320 ?   ?   ?   A . n 
A 1 319 ASP 319 321 ?   ?   ?   A . n 
A 1 320 LYS 320 322 ?   ?   ?   A . n 
A 1 321 TRP 321 323 ?   ?   ?   A . n 
A 1 322 LYS 322 324 ?   ?   ?   A . n 
A 1 323 ALA 323 325 ?   ?   ?   A . n 
A 1 324 LYS 324 326 ?   ?   ?   A . n 
A 1 325 LEU 325 327 ?   ?   ?   A . n 
A 1 326 GLY 326 328 ?   ?   ?   A . n 
A 1 327 THR 327 329 ?   ?   ?   A . n 
A 1 328 GLY 328 330 ?   ?   ?   A . n 
A 1 329 ALA 329 331 ?   ?   ?   A . n 
A 1 330 GLY 330 332 ?   ?   ?   A . n 
A 1 331 THR 331 333 ?   ?   ?   A . n 
A 1 332 ALA 332 334 ?   ?   ?   A . n 
A 1 333 ASP 333 335 ?   ?   ?   A . n 
A 1 334 ILE 334 336 ?   ?   ?   A . n 
A 1 335 GLU 335 337 ?   ?   ?   A . n 
A 1 336 ASN 336 338 ?   ?   ?   A . n 
A 1 337 LEU 337 339 ?   ?   ?   A . n 
A 1 338 ARG 338 340 ?   ?   ?   A . n 
A 1 339 ASN 339 341 ?   ?   ?   A . n 
A 1 340 GLU 340 342 ?   ?   ?   A . n 
A 1 341 VAL 341 343 ?   ?   ?   A . n 
A 1 342 ASN 342 344 ?   ?   ?   A . n 
A 1 343 GLU 343 345 ?   ?   ?   A . n 
A 1 344 LYS 344 346 ?   ?   ?   A . n 
A 1 345 ILE 345 347 ?   ?   ?   A . n 
A 1 346 ASP 346 348 ?   ?   ?   A . n 
A 1 347 ASP 347 349 ?   ?   ?   A . n 
A 1 348 VAL 348 350 ?   ?   ?   A . n 
A 1 349 LYS 349 351 ?   ?   ?   A . n 
A 1 350 ASP 350 352 ?   ?   ?   A . n 
A 1 351 GLU 351 353 ?   ?   ?   A . n 
A 1 352 VAL 352 354 ?   ?   ?   A . n 
A 1 353 ARG 353 355 ?   ?   ?   A . n 
A 1 354 THR 354 356 ?   ?   ?   A . n 
A 1 355 VAL 355 357 ?   ?   ?   A . n 
A 1 356 GLY 356 358 ?   ?   ?   A . n 
A 1 357 SER 357 359 ?   ?   ?   A . n 
A 1 358 LEU 358 360 ?   ?   ?   A . n 
A 1 359 SER 359 361 ?   ?   ?   A . n 
A 1 360 ALA 360 362 ?   ?   ?   A . n 
A 1 361 ALA 361 363 ?   ?   ?   A . n 
A 1 362 LEU 362 364 ?   ?   ?   A . n 
A 1 363 ALA 363 365 ?   ?   ?   A . n 
A 1 364 GLY 364 366 ?   ?   ?   A . n 
A 1 365 LEU 365 367 ?   ?   ?   A . n 
A 1 366 HIS 366 368 ?   ?   ?   A . n 
A 1 367 PRO 367 369 ?   ?   ?   A . n 
A 1 368 MET 368 370 ?   ?   ?   A . n 
A 1 369 GLN 369 371 ?   ?   ?   A . n 
A 1 370 TYR 370 372 ?   ?   ?   A . n 
A 1 371 ASP 371 373 ?   ?   ?   A . n 
A 1 372 PRO 372 374 ?   ?   ?   A . n 
A 1 373 LYS 373 375 ?   ?   ?   A . n 
A 1 374 ALA 374 376 ?   ?   ?   A . n 
A 1 375 PRO 375 377 ?   ?   ?   A . n 
A 1 376 VAL 376 378 ?   ?   ?   A . n 
A 1 377 GLN 377 379 ?   ?   ?   A . n 
A 1 378 VAL 378 380 ?   ?   ?   A . n 
A 1 379 MET 379 381 ?   ?   ?   A . n 
A 1 380 ALA 380 382 ?   ?   ?   A . n 
A 1 381 ALA 381 383 ?   ?   ?   A . n 
A 1 382 LEU 382 384 ?   ?   ?   A . n 
A 1 383 GLY 383 385 ?   ?   ?   A . n 
A 1 384 HIS 384 386 ?   ?   ?   A . n 
A 1 385 TYR 385 387 ?   ?   ?   A . n 
A 1 386 ARG 386 388 ?   ?   ?   A . n 
A 1 387 ASP 387 389 ?   ?   ?   A . n 
A 1 388 LYS 388 390 ?   ?   ?   A . n 
A 1 389 GLN 389 391 ?   ?   ?   A . n 
A 1 390 SER 390 392 ?   ?   ?   A . n 
A 1 391 VAL 391 393 ?   ?   ?   A . n 
A 1 392 ALA 392 394 ?   ?   ?   A . n 
A 1 393 VAL 393 395 ?   ?   ?   A . n 
A 1 394 GLY 394 396 ?   ?   ?   A . n 
A 1 395 ALA 395 397 ?   ?   ?   A . n 
A 1 396 SER 396 398 ?   ?   ?   A . n 
A 1 397 TYR 397 399 ?   ?   ?   A . n 
A 1 398 TYR 398 400 ?   ?   ?   A . n 
A 1 399 PHE 399 401 ?   ?   ?   A . n 
A 1 400 ASN 400 402 ?   ?   ?   A . n 
A 1 401 ASP 401 403 ?   ?   ?   A . n 
A 1 402 ARG 402 404 ?   ?   ?   A . n 
A 1 403 PHE 403 405 ?   ?   ?   A . n 
A 1 404 MET 404 406 ?   ?   ?   A . n 
A 1 405 MET 405 407 ?   ?   ?   A . n 
A 1 406 SER 406 408 ?   ?   ?   A . n 
A 1 407 THR 407 409 ?   ?   ?   A . n 
A 1 408 GLY 408 410 ?   ?   ?   A . n 
A 1 409 ILE 409 411 ?   ?   ?   A . n 
A 1 410 ALA 410 412 ?   ?   ?   A . n 
A 1 411 LEU 411 413 ?   ?   ?   A . n 
A 1 412 SER 412 414 ?   ?   ?   A . n 
A 1 413 GLY 413 415 ?   ?   ?   A . n 
A 1 414 GLU 414 416 ?   ?   ?   A . n 
A 1 415 LYS 415 417 ?   ?   ?   A . n 
A 1 416 ARG 416 418 ?   ?   ?   A . n 
A 1 417 THR 417 419 ?   ?   ?   A . n 
A 1 418 LYS 418 420 ?   ?   ?   A . n 
A 1 419 THR 419 421 ?   ?   ?   A . n 
A 1 420 MET 420 422 ?   ?   ?   A . n 
A 1 421 ALA 421 423 ?   ?   ?   A . n 
A 1 422 ASN 422 424 ?   ?   ?   A . n 
A 1 423 VAL 423 425 ?   ?   ?   A . n 
A 1 424 GLY 424 426 ?   ?   ?   A . n 
A 1 425 PHE 425 427 ?   ?   ?   A . n 
A 1 426 THR 426 428 ?   ?   ?   A . n 
A 1 427 LEU 427 429 ?   ?   ?   A . n 
A 1 428 LYS 428 430 ?   ?   ?   A . n 
A 1 429 LEU 429 431 ?   ?   ?   A . n 
A 1 430 GLY 430 432 ?   ?   ?   A . n 
A 1 431 LYS 431 433 ?   ?   ?   A . n 
A 1 432 GLY 432 434 ?   ?   ?   A . n 
A 1 433 SER 433 435 ?   ?   ?   A . n 
A 1 434 GLY 434 436 ?   ?   ?   A . n 
A 1 435 VAL 435 437 ?   ?   ?   A . n 
A 1 436 THR 436 438 ?   ?   ?   A . n 
A 1 437 TYR 437 439 ?   ?   ?   A . n 
A 1 438 ASP 438 440 ?   ?   ?   A . n 
A 1 439 GLU 439 441 ?   ?   ?   A . n 
A 1 440 THR 440 442 ?   ?   ?   A . n 
A 1 441 PRO 441 443 ?   ?   ?   A . n 
A 1 442 GLN 442 444 ?   ?   ?   A . n 
A 1 443 TYR 443 445 ?   ?   ?   A . n 
A 1 444 VAL 444 446 ?   ?   ?   A . n 
A 1 445 VAL 445 447 ?   ?   ?   A . n 
A 1 446 GLN 446 448 ?   ?   ?   A . n 
A 1 447 ASN 447 449 ?   ?   ?   A . n 
A 1 448 GLU 448 450 ?   ?   ?   A . n 
A 1 449 VAL 449 451 ?   ?   ?   A . n 
A 1 450 LYS 450 452 ?   ?   ?   A . n 
A 1 451 ARG 451 453 ?   ?   ?   A . n 
A 1 452 LEU 452 454 ?   ?   ?   A . n 
A 1 453 THR 453 455 ?   ?   ?   A . n 
A 1 454 VAL 454 456 ?   ?   ?   A . n 
A 1 455 GLU 455 457 ?   ?   ?   A . n 
A 1 456 ASN 456 458 ?   ?   ?   A . n 
A 1 457 GLN 457 459 ?   ?   ?   A . n 
A 1 458 GLU 458 460 ?   ?   ?   A . n 
A 1 459 LEU 459 461 ?   ?   ?   A . n 
A 1 460 LYS 460 462 ?   ?   ?   A . n 
A 1 461 GLU 461 463 ?   ?   ?   A . n 
A 1 462 ARG 462 464 ?   ?   ?   A . n 
A 1 463 VAL 463 465 ?   ?   ?   A . n 
A 1 464 ARG 464 466 ?   ?   ?   A . n 
A 1 465 ASN 465 467 ?   ?   ?   A . n 
A 1 466 LEU 466 468 ?   ?   ?   A . n 
A 1 467 GLU 467 469 ?   ?   ?   A . n 
A 1 468 GLU 468 470 ?   ?   ?   A . n 
A 1 469 LYS 469 471 ?   ?   ?   A . n 
A 1 470 LEU 470 472 ?   ?   ?   A . n 
A 1 471 ASN 471 473 ?   ?   ?   A . n 
A 1 472 MET 472 474 ?   ?   ?   A . n 
A 1 473 LEU 473 475 ?   ?   ?   A . n 
A 1 474 LEU 474 476 ?   ?   ?   A . n 
A 1 475 LYS 475 477 ?   ?   ?   A . n 
A 1 476 ASN 476 478 ?   ?   ?   A . n 
A 1 477 LYS 477 479 ?   ?   ?   A . n 
A 1 478 ARG 478 480 ?   ?   ?   A . n 
A 1 479 SER 479 481 ?   ?   ?   A . n 
A 1 480 SER 480 482 ?   ?   ?   A . n 
A 1 481 ALA 481 483 ?   ?   ?   A . n 
A 1 482 TRP 482 484 ?   ?   ?   A . n 
A 1 483 SER 483 485 ?   ?   ?   A . n 
A 1 484 HIS 484 486 ?   ?   ?   A . n 
A 1 485 PRO 485 487 ?   ?   ?   A . n 
A 1 486 GLN 486 488 ?   ?   ?   A . n 
A 1 487 PHE 487 489 ?   ?   ?   A . n 
A 1 488 GLU 488 490 ?   ?   ?   A . n 
A 1 489 LYS 489 491 ?   ?   ?   A . n 
B 1 1   MET 1   3   ?   ?   ?   B . n 
B 1 2   LYS 2   4   ?   ?   ?   B . n 
B 1 3   LYS 3   5   ?   ?   ?   B . n 
B 1 4   THR 4   6   ?   ?   ?   B . n 
B 1 5   ALA 5   7   ?   ?   ?   B . n 
B 1 6   ILE 6   8   ?   ?   ?   B . n 
B 1 7   ALA 7   9   ?   ?   ?   B . n 
B 1 8   ILE 8   10  ?   ?   ?   B . n 
B 1 9   ALA 9   11  ?   ?   ?   B . n 
B 1 10  VAL 10  12  ?   ?   ?   B . n 
B 1 11  ALA 11  13  ?   ?   ?   B . n 
B 1 12  LEU 12  14  ?   ?   ?   B . n 
B 1 13  ALA 13  15  ?   ?   ?   B . n 
B 1 14  GLY 14  16  ?   ?   ?   B . n 
B 1 15  PHE 15  17  ?   ?   ?   B . n 
B 1 16  ALA 16  18  ?   ?   ?   B . n 
B 1 17  THR 17  19  ?   ?   ?   B . n 
B 1 18  VAL 18  20  ?   ?   ?   B . n 
B 1 19  ALA 19  21  ?   ?   ?   B . n 
B 1 20  GLN 20  22  ?   ?   ?   B . n 
B 1 21  ALA 21  23  ?   ?   ?   B . n 
B 1 22  SER 22  24  ?   ?   ?   B . n 
B 1 23  ALA 23  25  ?   ?   ?   B . n 
B 1 24  ALA 24  26  26  ALA ALA B . n 
B 1 25  PRO 25  27  27  PRO PRO B . n 
B 1 26  VAL 26  28  28  VAL VAL B . n 
B 1 27  ILE 27  29  29  ILE ILE B . n 
B 1 28  LYS 28  30  30  LYS LYS B . n 
B 1 29  ALA 29  31  31  ALA ALA B . n 
B 1 30  GLY 30  32  32  GLY GLY B . n 
B 1 31  THR 31  33  33  THR THR B . n 
B 1 32  ALA 32  34  34  ALA ALA B . n 
B 1 33  THR 33  35  35  THR THR B . n 
B 1 34  ASP 34  36  36  ASP ASP B . n 
B 1 35  SER 35  37  37  SER SER B . n 
B 1 36  THR 36  38  38  THR THR B . n 
B 1 37  GLU 37  39  39  GLU GLU B . n 
B 1 38  ALA 38  40  40  ALA ALA B . n 
B 1 39  GLY 39  41  41  GLY GLY B . n 
B 1 40  VAL 40  42  42  VAL VAL B . n 
B 1 41  ASP 41  43  43  ASP ASP B . n 
B 1 42  ASN 42  44  44  ASN ASN B . n 
B 1 43  VAL 43  45  45  VAL VAL B . n 
B 1 44  ALA 44  46  46  ALA ALA B . n 
B 1 45  ASN 45  47  47  ASN ASN B . n 
B 1 46  GLY 46  48  48  GLY GLY B . n 
B 1 47  VAL 47  49  49  VAL VAL B . n 
B 1 48  LYS 48  50  50  LYS LYS B . n 
B 1 49  SER 49  51  51  SER SER B . n 
B 1 50  SER 50  52  52  SER SER B . n 
B 1 51  ALA 51  53  53  ALA ALA B . n 
B 1 52  PHE 52  54  54  PHE PHE B . n 
B 1 53  GLY 53  55  55  GLY GLY B . n 
B 1 54  TYR 54  56  56  TYR TYR B . n 
B 1 55  ASP 55  57  57  ASP ASP B . n 
B 1 56  ASN 56  58  58  ASN ASN B . n 
B 1 57  LYS 57  59  59  LYS LYS B . n 
B 1 58  ALA 58  60  60  ALA ALA B . n 
B 1 59  ILE 59  61  61  ILE ILE B . n 
B 1 60  GLU 60  62  62  GLU GLU B . n 
B 1 61  LYS 61  63  63  LYS LYS B . n 
B 1 62  GLU 62  64  64  GLU GLU B . n 
B 1 63  SER 63  65  65  SER SER B . n 
B 1 64  SER 64  66  66  SER SER B . n 
B 1 65  ALA 65  67  67  ALA ALA B . n 
B 1 66  PHE 66  68  68  PHE PHE B . n 
B 1 67  GLY 67  69  69  GLY GLY B . n 
B 1 68  THR 68  70  70  THR THR B . n 
B 1 69  GLY 69  71  71  GLY GLY B . n 
B 1 70  ASN 70  72  72  ASN ASN B . n 
B 1 71  ARG 71  73  73  ARG ARG B . n 
B 1 72  ALA 72  74  74  ALA ALA B . n 
B 1 73  THR 73  75  75  THR THR B . n 
B 1 74  GLY 74  76  76  GLY GLY B . n 
B 1 75  GLU 75  77  77  GLU GLU B . n 
B 1 76  PHE 76  78  78  PHE PHE B . n 
B 1 77  SER 77  79  79  SER SER B . n 
B 1 78  SER 78  80  80  SER SER B . n 
B 1 79  ALA 79  81  81  ALA ALA B . n 
B 1 80  PHE 80  82  82  PHE PHE B . n 
B 1 81  GLY 81  83  83  GLY GLY B . n 
B 1 82  PHE 82  84  84  PHE PHE B . n 
B 1 83  HIS 83  85  85  HIS HIS B . n 
B 1 84  ASN 84  86  86  ASN ASN B . n 
B 1 85  ILE 85  87  87  ILE ILE B . n 
B 1 86  ALA 86  88  88  ALA ALA B . n 
B 1 87  SER 87  89  89  SER SER B . n 
B 1 88  LYS 88  90  90  LYS LYS B . n 
B 1 89  ILE 89  91  91  ILE ILE B . n 
B 1 90  HIS 90  92  92  HIS HIS B . n 
B 1 91  SER 91  93  93  SER SER B . n 
B 1 92  SER 92  94  94  SER SER B . n 
B 1 93  ALA 93  95  95  ALA ALA B . n 
B 1 94  PHE 94  96  96  PHE PHE B . n 
B 1 95  GLY 95  97  97  GLY GLY B . n 
B 1 96  SER 96  98  98  SER SER B . n 
B 1 97  ASN 97  99  99  ASN ASN B . n 
B 1 98  ASN 98  100 100 ASN ASN B . n 
B 1 99  ALA 99  101 101 ALA ALA B . n 
B 1 100 ALA 100 102 102 ALA ALA B . n 
B 1 101 ASP 101 103 103 ASP ASP B . n 
B 1 102 GLY 102 104 104 GLY GLY B . n 
B 1 103 VAL 103 105 105 VAL VAL B . n 
B 1 104 ASN 104 106 106 ASN ASN B . n 
B 1 105 SER 105 107 107 SER SER B . n 
B 1 106 SER 106 108 108 SER SER B . n 
B 1 107 ALA 107 109 109 ALA ALA B . n 
B 1 108 PHE 108 110 110 PHE PHE B . n 
B 1 109 GLY 109 111 111 GLY GLY B . n 
B 1 110 PHE 110 112 112 PHE PHE B . n 
B 1 111 LYS 111 113 113 LYS LYS B . n 
B 1 112 ASN 112 114 114 ASN ASN B . n 
B 1 113 THR 113 115 115 THR THR B . n 
B 1 114 VAL 114 116 116 VAL VAL B . n 
B 1 115 SER 115 117 117 SER SER B . n 
B 1 116 GLY 116 118 118 GLY GLY B . n 
B 1 117 PHE 117 119 119 PHE PHE B . n 
B 1 118 ASN 118 120 120 ASN ASN B . n 
B 1 119 SER 119 121 121 SER SER B . n 
B 1 120 SER 120 122 122 SER SER B . n 
B 1 121 ALA 121 123 123 ALA ALA B . n 
B 1 122 PHE 122 124 124 PHE PHE B . n 
B 1 123 GLY 123 125 125 GLY GLY B . n 
B 1 124 SER 124 126 126 SER SER B . n 
B 1 125 GLN 125 127 127 GLN GLN B . n 
B 1 126 TYR 126 128 128 TYR TYR B . n 
B 1 127 GLN 127 129 129 GLN GLN B . n 
B 1 128 VAL 128 130 130 VAL VAL B . n 
B 1 129 THR 129 131 131 THR THR B . n 
B 1 130 GLY 130 132 132 GLY GLY B . n 
B 1 131 ASN 131 133 133 ASN ASN B . n 
B 1 132 PHE 132 134 134 PHE PHE B . n 
B 1 133 SER 133 135 135 SER SER B . n 
B 1 134 GLY 134 136 136 GLY GLY B . n 
B 1 135 ALA 135 137 137 ALA ALA B . n 
B 1 136 PHE 136 138 138 PHE PHE B . n 
B 1 137 GLY 137 139 139 GLY GLY B . n 
B 1 138 MET 138 140 140 MET MET B . n 
B 1 139 GLY 139 141 141 GLY GLY B . n 
B 1 140 GLU 140 142 142 GLU GLU B . n 
B 1 141 PHE 141 143 143 PHE PHE B . n 
B 1 142 ASN 142 144 144 ASN ASN B . n 
B 1 143 GLY 143 145 145 GLY GLY B . n 
B 1 144 GLN 144 146 146 GLN GLN B . n 
B 1 145 TYR 145 147 147 TYR TYR B . n 
B 1 146 GLN 146 148 148 GLN GLN B . n 
B 1 147 TYR 147 149 149 TYR TYR B . n 
B 1 148 LYS 148 150 150 LYS LYS B . n 
B 1 149 ASN 149 151 151 ASN ASN B . n 
B 1 150 GLU 150 152 152 GLU GLU B . n 
B 1 151 GLY 151 153 153 GLY GLY B . n 
B 1 152 ASN 152 154 154 ASN ASN B . n 
B 1 153 ASN 153 155 155 ASN ASN B . n 
B 1 154 SER 154 156 156 SER SER B . n 
B 1 155 TYR 155 157 157 TYR TYR B . n 
B 1 156 MET 156 158 158 MET MET B . n 
B 1 157 ILE 157 159 159 ILE ILE B . n 
B 1 158 GLY 158 160 160 GLY GLY B . n 
B 1 159 ASN 159 161 161 ASN ASN B . n 
B 1 160 LYS 160 162 162 LYS LYS B . n 
B 1 161 ASN 161 163 163 ASN ASN B . n 
B 1 162 LYS 162 164 164 LYS LYS B . n 
B 1 163 ILE 163 165 165 ILE ILE B . n 
B 1 164 ALA 164 166 166 ALA ALA B . n 
B 1 165 SER 165 167 167 SER SER B . n 
B 1 166 GLY 166 168 168 GLY GLY B . n 
B 1 167 SER 167 169 169 SER SER B . n 
B 1 168 ASP 168 170 170 ASP ASP B . n 
B 1 169 ASP 169 171 171 ASP ASP B . n 
B 1 170 ASN 170 172 172 ASN ASN B . n 
B 1 171 PHE 171 173 173 PHE PHE B . n 
B 1 172 ILE 172 174 174 ILE ILE B . n 
B 1 173 LEU 173 175 175 LEU LEU B . n 
B 1 174 GLY 174 176 176 GLY GLY B . n 
B 1 175 ASN 175 177 177 ASN ASN B . n 
B 1 176 ASN 176 178 178 ASN ASN B . n 
B 1 177 VAL 177 179 179 VAL VAL B . n 
B 1 178 HIS 178 180 180 HIS HIS B . n 
B 1 179 ILE 179 181 181 ILE ILE B . n 
B 1 180 GLY 180 182 182 GLY GLY B . n 
B 1 181 GLY 181 183 183 GLY GLY B . n 
B 1 182 GLY 182 184 184 GLY GLY B . n 
B 1 183 ILE 183 185 185 ILE ILE B . n 
B 1 184 ASN 184 186 186 ASN ASN B . n 
B 1 185 ASN 185 187 187 ASN ASN B . n 
B 1 186 SER 186 188 188 SER SER B . n 
B 1 187 VAL 187 189 189 VAL VAL B . n 
B 1 188 ALA 188 190 190 ALA ALA B . n 
B 1 189 LEU 189 191 191 LEU LEU B . n 
B 1 190 GLY 190 192 192 GLY GLY B . n 
B 1 191 ASN 191 193 193 ASN ASN B . n 
B 1 192 ASN 192 194 194 ASN ASN B . n 
B 1 193 SER 193 195 195 SER SER B . n 
B 1 194 THR 194 196 196 THR THR B . n 
B 1 195 VAL 195 197 197 VAL VAL B . n 
B 1 196 SER 196 198 198 SER SER B . n 
B 1 197 ALA 197 199 199 ALA ALA B . n 
B 1 198 SER 198 200 200 SER SER B . n 
B 1 199 ASN 199 201 201 ASN ASN B . n 
B 1 200 THR 200 202 202 THR THR B . n 
B 1 201 VAL 201 203 203 VAL VAL B . n 
B 1 202 SER 202 204 204 SER SER B . n 
B 1 203 VAL 203 205 205 VAL VAL B . n 
B 1 204 GLY 204 206 206 GLY GLY B . n 
B 1 205 SER 205 207 207 SER SER B . n 
B 1 206 SER 206 208 208 SER SER B . n 
B 1 207 THR 207 209 209 THR THR B . n 
B 1 208 LEU 208 210 210 LEU LEU B . n 
B 1 209 LYS 209 211 211 LYS LYS B . n 
B 1 210 ARG 210 212 212 ARG ARG B . n 
B 1 211 LYS 211 213 213 LYS LYS B . n 
B 1 212 ILE 212 214 214 ILE ILE B . n 
B 1 213 VAL 213 215 215 VAL VAL B . n 
B 1 214 ASN 214 216 216 ASN ASN B . n 
B 1 215 VAL 215 217 217 VAL VAL B . n 
B 1 216 GLY 216 218 218 GLY GLY B . n 
B 1 217 ASP 217 219 219 ASP ASP B . n 
B 1 218 GLY 218 220 220 GLY GLY B . n 
B 1 219 ALA 219 221 221 ALA ALA B . n 
B 1 220 ILE 220 222 222 ILE ILE B . n 
B 1 221 SER 221 223 223 SER SER B . n 
B 1 222 ALA 222 224 224 ALA ALA B . n 
B 1 223 ASN 223 225 225 ASN ASN B . n 
B 1 224 SER 224 226 226 SER SER B . n 
B 1 225 SER 225 227 227 SER SER B . n 
B 1 226 ASP 226 228 228 ASP ASP B . n 
B 1 227 ALA 227 229 229 ALA ALA B . n 
B 1 228 VAL 228 230 230 VAL VAL B . n 
B 1 229 THR 229 231 231 THR THR B . n 
B 1 230 GLY 230 232 232 GLY GLY B . n 
B 1 231 ARG 231 233 233 ARG ARG B . n 
B 1 232 GLN 232 234 234 GLN GLN B . n 
B 1 233 LEU 233 235 235 LEU LEU B . n 
B 1 234 TYR 234 236 236 TYR TYR B . n 
B 1 235 SER 235 237 237 SER SER B . n 
B 1 236 GLY 236 238 238 GLY GLY B . n 
B 1 237 ASN 237 239 239 ASN ASN B . n 
B 1 238 GLY 238 240 240 GLY GLY B . n 
B 1 239 ILE 239 241 241 ILE ILE B . n 
B 1 240 ASP 240 242 242 ASP ASP B . n 
B 1 241 THR 241 243 243 THR THR B . n 
B 1 242 ALA 242 244 244 ALA ALA B . n 
B 1 243 ALA 243 245 245 ALA ALA B . n 
B 1 244 TRP 244 246 246 TRP TRP B . n 
B 1 245 GLN 245 247 247 GLN GLN B . n 
B 1 246 ASN 246 248 248 ASN ASN B . n 
B 1 247 LYS 247 249 249 LYS LYS B . n 
B 1 248 LEU 248 250 250 LEU LEU B . n 
B 1 249 ASN 249 251 251 ASN ASN B . n 
B 1 250 VAL 250 252 252 VAL VAL B . n 
B 1 251 THR 251 253 253 THR THR B . n 
B 1 252 ARG 252 254 254 ARG ARG B . n 
B 1 253 LYS 253 255 255 LYS LYS B . n 
B 1 254 ASN 254 256 256 ASN ASN B . n 
B 1 255 ASP 255 257 257 ASP ASP B . n 
B 1 256 TYR 256 258 258 TYR TYR B . n 
B 1 257 LYS 257 259 259 LYS LYS B . n 
B 1 258 ASP 258 260 260 ASP ASP B . n 
B 1 259 ALA 259 261 261 ALA ALA B . n 
B 1 260 ASN 260 262 262 ASN ASN B . n 
B 1 261 ASP 261 263 263 ASP ASP B . n 
B 1 262 ILE 262 264 264 ILE ILE B . n 
B 1 263 ASP 263 265 265 ASP ASP B . n 
B 1 264 VAL 264 266 266 VAL VAL B . n 
B 1 265 ASN 265 267 267 ASN ASN B . n 
B 1 266 LYS 266 268 268 LYS LYS B . n 
B 1 267 TRP 267 269 269 TRP TRP B . n 
B 1 268 LYS 268 270 270 LYS LYS B . n 
B 1 269 ALA 269 271 271 ALA ALA B . n 
B 1 270 LYS 270 272 272 LYS LYS B . n 
B 1 271 LEU 271 273 273 LEU LEU B . n 
B 1 272 GLY 272 274 274 GLY GLY B . n 
B 1 273 VAL 273 275 ?   ?   ?   B . n 
B 1 274 GLY 274 276 ?   ?   ?   B . n 
B 1 275 SER 275 277 ?   ?   ?   B . n 
B 1 276 GLY 276 278 ?   ?   ?   B . n 
B 1 277 GLY 277 279 ?   ?   ?   B . n 
B 1 278 GLY 278 280 ?   ?   ?   B . n 
B 1 279 GLY 279 281 ?   ?   ?   B . n 
B 1 280 GLY 280 282 ?   ?   ?   B . n 
B 1 281 ALA 281 283 ?   ?   ?   B . n 
B 1 282 PRO 282 284 ?   ?   ?   B . n 
B 1 283 VAL 283 285 ?   ?   ?   B . n 
B 1 284 ASP 284 286 ?   ?   ?   B . n 
B 1 285 ALA 285 287 ?   ?   ?   B . n 
B 1 286 TYR 286 288 ?   ?   ?   B . n 
B 1 287 THR 287 289 ?   ?   ?   B . n 
B 1 288 LYS 288 290 ?   ?   ?   B . n 
B 1 289 SER 289 291 ?   ?   ?   B . n 
B 1 290 GLU 290 292 ?   ?   ?   B . n 
B 1 291 ALA 291 293 ?   ?   ?   B . n 
B 1 292 ASP 292 294 ?   ?   ?   B . n 
B 1 293 ASN 293 295 ?   ?   ?   B . n 
B 1 294 LYS 294 296 ?   ?   ?   B . n 
B 1 295 PHE 295 297 ?   ?   ?   B . n 
B 1 296 ALA 296 298 ?   ?   ?   B . n 
B 1 297 ASN 297 299 ?   ?   ?   B . n 
B 1 298 LYS 298 300 ?   ?   ?   B . n 
B 1 299 THR 299 301 ?   ?   ?   B . n 
B 1 300 ASP 300 302 ?   ?   ?   B . n 
B 1 301 LEU 301 303 ?   ?   ?   B . n 
B 1 302 ASN 302 304 ?   ?   ?   B . n 
B 1 303 ASP 303 305 ?   ?   ?   B . n 
B 1 304 TYR 304 306 ?   ?   ?   B . n 
B 1 305 THR 305 307 ?   ?   ?   B . n 
B 1 306 LYS 306 308 ?   ?   ?   B . n 
B 1 307 LYS 307 309 ?   ?   ?   B . n 
B 1 308 ASP 308 310 ?   ?   ?   B . n 
B 1 309 ASP 309 311 ?   ?   ?   B . n 
B 1 310 TYR 310 312 ?   ?   ?   B . n 
B 1 311 LYS 311 313 ?   ?   ?   B . n 
B 1 312 ASP 312 314 ?   ?   ?   B . n 
B 1 313 ALA 313 315 ?   ?   ?   B . n 
B 1 314 ASN 314 316 ?   ?   ?   B . n 
B 1 315 GLY 315 317 ?   ?   ?   B . n 
B 1 316 ILE 316 318 ?   ?   ?   B . n 
B 1 317 ASP 317 319 ?   ?   ?   B . n 
B 1 318 VAL 318 320 ?   ?   ?   B . n 
B 1 319 ASP 319 321 ?   ?   ?   B . n 
B 1 320 LYS 320 322 ?   ?   ?   B . n 
B 1 321 TRP 321 323 ?   ?   ?   B . n 
B 1 322 LYS 322 324 ?   ?   ?   B . n 
B 1 323 ALA 323 325 ?   ?   ?   B . n 
B 1 324 LYS 324 326 ?   ?   ?   B . n 
B 1 325 LEU 325 327 ?   ?   ?   B . n 
B 1 326 GLY 326 328 ?   ?   ?   B . n 
B 1 327 THR 327 329 ?   ?   ?   B . n 
B 1 328 GLY 328 330 ?   ?   ?   B . n 
B 1 329 ALA 329 331 ?   ?   ?   B . n 
B 1 330 GLY 330 332 ?   ?   ?   B . n 
B 1 331 THR 331 333 ?   ?   ?   B . n 
B 1 332 ALA 332 334 ?   ?   ?   B . n 
B 1 333 ASP 333 335 ?   ?   ?   B . n 
B 1 334 ILE 334 336 ?   ?   ?   B . n 
B 1 335 GLU 335 337 ?   ?   ?   B . n 
B 1 336 ASN 336 338 ?   ?   ?   B . n 
B 1 337 LEU 337 339 ?   ?   ?   B . n 
B 1 338 ARG 338 340 ?   ?   ?   B . n 
B 1 339 ASN 339 341 ?   ?   ?   B . n 
B 1 340 GLU 340 342 ?   ?   ?   B . n 
B 1 341 VAL 341 343 ?   ?   ?   B . n 
B 1 342 ASN 342 344 ?   ?   ?   B . n 
B 1 343 GLU 343 345 ?   ?   ?   B . n 
B 1 344 LYS 344 346 ?   ?   ?   B . n 
B 1 345 ILE 345 347 ?   ?   ?   B . n 
B 1 346 ASP 346 348 ?   ?   ?   B . n 
B 1 347 ASP 347 349 ?   ?   ?   B . n 
B 1 348 VAL 348 350 ?   ?   ?   B . n 
B 1 349 LYS 349 351 ?   ?   ?   B . n 
B 1 350 ASP 350 352 ?   ?   ?   B . n 
B 1 351 GLU 351 353 ?   ?   ?   B . n 
B 1 352 VAL 352 354 ?   ?   ?   B . n 
B 1 353 ARG 353 355 ?   ?   ?   B . n 
B 1 354 THR 354 356 ?   ?   ?   B . n 
B 1 355 VAL 355 357 ?   ?   ?   B . n 
B 1 356 GLY 356 358 ?   ?   ?   B . n 
B 1 357 SER 357 359 ?   ?   ?   B . n 
B 1 358 LEU 358 360 ?   ?   ?   B . n 
B 1 359 SER 359 361 ?   ?   ?   B . n 
B 1 360 ALA 360 362 ?   ?   ?   B . n 
B 1 361 ALA 361 363 ?   ?   ?   B . n 
B 1 362 LEU 362 364 ?   ?   ?   B . n 
B 1 363 ALA 363 365 ?   ?   ?   B . n 
B 1 364 GLY 364 366 ?   ?   ?   B . n 
B 1 365 LEU 365 367 ?   ?   ?   B . n 
B 1 366 HIS 366 368 ?   ?   ?   B . n 
B 1 367 PRO 367 369 ?   ?   ?   B . n 
B 1 368 MET 368 370 ?   ?   ?   B . n 
B 1 369 GLN 369 371 ?   ?   ?   B . n 
B 1 370 TYR 370 372 ?   ?   ?   B . n 
B 1 371 ASP 371 373 ?   ?   ?   B . n 
B 1 372 PRO 372 374 ?   ?   ?   B . n 
B 1 373 LYS 373 375 ?   ?   ?   B . n 
B 1 374 ALA 374 376 ?   ?   ?   B . n 
B 1 375 PRO 375 377 ?   ?   ?   B . n 
B 1 376 VAL 376 378 ?   ?   ?   B . n 
B 1 377 GLN 377 379 ?   ?   ?   B . n 
B 1 378 VAL 378 380 ?   ?   ?   B . n 
B 1 379 MET 379 381 ?   ?   ?   B . n 
B 1 380 ALA 380 382 ?   ?   ?   B . n 
B 1 381 ALA 381 383 ?   ?   ?   B . n 
B 1 382 LEU 382 384 ?   ?   ?   B . n 
B 1 383 GLY 383 385 ?   ?   ?   B . n 
B 1 384 HIS 384 386 ?   ?   ?   B . n 
B 1 385 TYR 385 387 ?   ?   ?   B . n 
B 1 386 ARG 386 388 ?   ?   ?   B . n 
B 1 387 ASP 387 389 ?   ?   ?   B . n 
B 1 388 LYS 388 390 ?   ?   ?   B . n 
B 1 389 GLN 389 391 ?   ?   ?   B . n 
B 1 390 SER 390 392 ?   ?   ?   B . n 
B 1 391 VAL 391 393 ?   ?   ?   B . n 
B 1 392 ALA 392 394 ?   ?   ?   B . n 
B 1 393 VAL 393 395 ?   ?   ?   B . n 
B 1 394 GLY 394 396 ?   ?   ?   B . n 
B 1 395 ALA 395 397 ?   ?   ?   B . n 
B 1 396 SER 396 398 ?   ?   ?   B . n 
B 1 397 TYR 397 399 ?   ?   ?   B . n 
B 1 398 TYR 398 400 ?   ?   ?   B . n 
B 1 399 PHE 399 401 ?   ?   ?   B . n 
B 1 400 ASN 400 402 ?   ?   ?   B . n 
B 1 401 ASP 401 403 ?   ?   ?   B . n 
B 1 402 ARG 402 404 ?   ?   ?   B . n 
B 1 403 PHE 403 405 ?   ?   ?   B . n 
B 1 404 MET 404 406 ?   ?   ?   B . n 
B 1 405 MET 405 407 ?   ?   ?   B . n 
B 1 406 SER 406 408 ?   ?   ?   B . n 
B 1 407 THR 407 409 ?   ?   ?   B . n 
B 1 408 GLY 408 410 ?   ?   ?   B . n 
B 1 409 ILE 409 411 ?   ?   ?   B . n 
B 1 410 ALA 410 412 ?   ?   ?   B . n 
B 1 411 LEU 411 413 ?   ?   ?   B . n 
B 1 412 SER 412 414 ?   ?   ?   B . n 
B 1 413 GLY 413 415 ?   ?   ?   B . n 
B 1 414 GLU 414 416 ?   ?   ?   B . n 
B 1 415 LYS 415 417 ?   ?   ?   B . n 
B 1 416 ARG 416 418 ?   ?   ?   B . n 
B 1 417 THR 417 419 ?   ?   ?   B . n 
B 1 418 LYS 418 420 ?   ?   ?   B . n 
B 1 419 THR 419 421 ?   ?   ?   B . n 
B 1 420 MET 420 422 ?   ?   ?   B . n 
B 1 421 ALA 421 423 ?   ?   ?   B . n 
B 1 422 ASN 422 424 ?   ?   ?   B . n 
B 1 423 VAL 423 425 ?   ?   ?   B . n 
B 1 424 GLY 424 426 ?   ?   ?   B . n 
B 1 425 PHE 425 427 ?   ?   ?   B . n 
B 1 426 THR 426 428 ?   ?   ?   B . n 
B 1 427 LEU 427 429 ?   ?   ?   B . n 
B 1 428 LYS 428 430 ?   ?   ?   B . n 
B 1 429 LEU 429 431 ?   ?   ?   B . n 
B 1 430 GLY 430 432 ?   ?   ?   B . n 
B 1 431 LYS 431 433 ?   ?   ?   B . n 
B 1 432 GLY 432 434 ?   ?   ?   B . n 
B 1 433 SER 433 435 ?   ?   ?   B . n 
B 1 434 GLY 434 436 ?   ?   ?   B . n 
B 1 435 VAL 435 437 ?   ?   ?   B . n 
B 1 436 THR 436 438 ?   ?   ?   B . n 
B 1 437 TYR 437 439 ?   ?   ?   B . n 
B 1 438 ASP 438 440 ?   ?   ?   B . n 
B 1 439 GLU 439 441 ?   ?   ?   B . n 
B 1 440 THR 440 442 ?   ?   ?   B . n 
B 1 441 PRO 441 443 ?   ?   ?   B . n 
B 1 442 GLN 442 444 ?   ?   ?   B . n 
B 1 443 TYR 443 445 ?   ?   ?   B . n 
B 1 444 VAL 444 446 ?   ?   ?   B . n 
B 1 445 VAL 445 447 ?   ?   ?   B . n 
B 1 446 GLN 446 448 ?   ?   ?   B . n 
B 1 447 ASN 447 449 ?   ?   ?   B . n 
B 1 448 GLU 448 450 ?   ?   ?   B . n 
B 1 449 VAL 449 451 ?   ?   ?   B . n 
B 1 450 LYS 450 452 ?   ?   ?   B . n 
B 1 451 ARG 451 453 ?   ?   ?   B . n 
B 1 452 LEU 452 454 ?   ?   ?   B . n 
B 1 453 THR 453 455 ?   ?   ?   B . n 
B 1 454 VAL 454 456 ?   ?   ?   B . n 
B 1 455 GLU 455 457 ?   ?   ?   B . n 
B 1 456 ASN 456 458 ?   ?   ?   B . n 
B 1 457 GLN 457 459 ?   ?   ?   B . n 
B 1 458 GLU 458 460 ?   ?   ?   B . n 
B 1 459 LEU 459 461 ?   ?   ?   B . n 
B 1 460 LYS 460 462 ?   ?   ?   B . n 
B 1 461 GLU 461 463 ?   ?   ?   B . n 
B 1 462 ARG 462 464 ?   ?   ?   B . n 
B 1 463 VAL 463 465 ?   ?   ?   B . n 
B 1 464 ARG 464 466 ?   ?   ?   B . n 
B 1 465 ASN 465 467 ?   ?   ?   B . n 
B 1 466 LEU 466 468 ?   ?   ?   B . n 
B 1 467 GLU 467 469 ?   ?   ?   B . n 
B 1 468 GLU 468 470 ?   ?   ?   B . n 
B 1 469 LYS 469 471 ?   ?   ?   B . n 
B 1 470 LEU 470 472 ?   ?   ?   B . n 
B 1 471 ASN 471 473 ?   ?   ?   B . n 
B 1 472 MET 472 474 ?   ?   ?   B . n 
B 1 473 LEU 473 475 ?   ?   ?   B . n 
B 1 474 LEU 474 476 ?   ?   ?   B . n 
B 1 475 LYS 475 477 ?   ?   ?   B . n 
B 1 476 ASN 476 478 ?   ?   ?   B . n 
B 1 477 LYS 477 479 ?   ?   ?   B . n 
B 1 478 ARG 478 480 ?   ?   ?   B . n 
B 1 479 SER 479 481 ?   ?   ?   B . n 
B 1 480 SER 480 482 ?   ?   ?   B . n 
B 1 481 ALA 481 483 ?   ?   ?   B . n 
B 1 482 TRP 482 484 ?   ?   ?   B . n 
B 1 483 SER 483 485 ?   ?   ?   B . n 
B 1 484 HIS 484 486 ?   ?   ?   B . n 
B 1 485 PRO 485 487 ?   ?   ?   B . n 
B 1 486 GLN 486 488 ?   ?   ?   B . n 
B 1 487 PHE 487 489 ?   ?   ?   B . n 
B 1 488 GLU 488 490 ?   ?   ?   B . n 
B 1 489 LYS 489 491 ?   ?   ?   B . n 
C 1 1   MET 1   3   ?   ?   ?   C . n 
C 1 2   LYS 2   4   ?   ?   ?   C . n 
C 1 3   LYS 3   5   ?   ?   ?   C . n 
C 1 4   THR 4   6   ?   ?   ?   C . n 
C 1 5   ALA 5   7   ?   ?   ?   C . n 
C 1 6   ILE 6   8   ?   ?   ?   C . n 
C 1 7   ALA 7   9   ?   ?   ?   C . n 
C 1 8   ILE 8   10  ?   ?   ?   C . n 
C 1 9   ALA 9   11  ?   ?   ?   C . n 
C 1 10  VAL 10  12  ?   ?   ?   C . n 
C 1 11  ALA 11  13  ?   ?   ?   C . n 
C 1 12  LEU 12  14  ?   ?   ?   C . n 
C 1 13  ALA 13  15  ?   ?   ?   C . n 
C 1 14  GLY 14  16  ?   ?   ?   C . n 
C 1 15  PHE 15  17  ?   ?   ?   C . n 
C 1 16  ALA 16  18  ?   ?   ?   C . n 
C 1 17  THR 17  19  ?   ?   ?   C . n 
C 1 18  VAL 18  20  ?   ?   ?   C . n 
C 1 19  ALA 19  21  ?   ?   ?   C . n 
C 1 20  GLN 20  22  ?   ?   ?   C . n 
C 1 21  ALA 21  23  ?   ?   ?   C . n 
C 1 22  SER 22  24  ?   ?   ?   C . n 
C 1 23  ALA 23  25  ?   ?   ?   C . n 
C 1 24  ALA 24  26  26  ALA ALA C . n 
C 1 25  PRO 25  27  27  PRO PRO C . n 
C 1 26  VAL 26  28  28  VAL VAL C . n 
C 1 27  ILE 27  29  29  ILE ILE C . n 
C 1 28  LYS 28  30  30  LYS LYS C . n 
C 1 29  ALA 29  31  31  ALA ALA C . n 
C 1 30  GLY 30  32  32  GLY GLY C . n 
C 1 31  THR 31  33  33  THR THR C . n 
C 1 32  ALA 32  34  34  ALA ALA C . n 
C 1 33  THR 33  35  35  THR THR C . n 
C 1 34  ASP 34  36  36  ASP ASP C . n 
C 1 35  SER 35  37  37  SER SER C . n 
C 1 36  THR 36  38  38  THR THR C . n 
C 1 37  GLU 37  39  39  GLU GLU C . n 
C 1 38  ALA 38  40  40  ALA ALA C . n 
C 1 39  GLY 39  41  41  GLY GLY C . n 
C 1 40  VAL 40  42  42  VAL VAL C . n 
C 1 41  ASP 41  43  43  ASP ASP C . n 
C 1 42  ASN 42  44  44  ASN ASN C . n 
C 1 43  VAL 43  45  45  VAL VAL C . n 
C 1 44  ALA 44  46  46  ALA ALA C . n 
C 1 45  ASN 45  47  47  ASN ASN C . n 
C 1 46  GLY 46  48  48  GLY GLY C . n 
C 1 47  VAL 47  49  49  VAL VAL C . n 
C 1 48  LYS 48  50  50  LYS LYS C . n 
C 1 49  SER 49  51  51  SER SER C . n 
C 1 50  SER 50  52  52  SER SER C . n 
C 1 51  ALA 51  53  53  ALA ALA C . n 
C 1 52  PHE 52  54  54  PHE PHE C . n 
C 1 53  GLY 53  55  55  GLY GLY C . n 
C 1 54  TYR 54  56  56  TYR TYR C . n 
C 1 55  ASP 55  57  57  ASP ASP C . n 
C 1 56  ASN 56  58  58  ASN ASN C . n 
C 1 57  LYS 57  59  59  LYS LYS C . n 
C 1 58  ALA 58  60  60  ALA ALA C . n 
C 1 59  ILE 59  61  61  ILE ILE C . n 
C 1 60  GLU 60  62  62  GLU GLU C . n 
C 1 61  LYS 61  63  63  LYS LYS C . n 
C 1 62  GLU 62  64  64  GLU GLU C . n 
C 1 63  SER 63  65  65  SER SER C . n 
C 1 64  SER 64  66  66  SER SER C . n 
C 1 65  ALA 65  67  67  ALA ALA C . n 
C 1 66  PHE 66  68  68  PHE PHE C . n 
C 1 67  GLY 67  69  69  GLY GLY C . n 
C 1 68  THR 68  70  70  THR THR C . n 
C 1 69  GLY 69  71  71  GLY GLY C . n 
C 1 70  ASN 70  72  72  ASN ASN C . n 
C 1 71  ARG 71  73  73  ARG ARG C . n 
C 1 72  ALA 72  74  74  ALA ALA C . n 
C 1 73  THR 73  75  75  THR THR C . n 
C 1 74  GLY 74  76  76  GLY GLY C . n 
C 1 75  GLU 75  77  77  GLU GLU C . n 
C 1 76  PHE 76  78  78  PHE PHE C . n 
C 1 77  SER 77  79  79  SER SER C . n 
C 1 78  SER 78  80  80  SER SER C . n 
C 1 79  ALA 79  81  81  ALA ALA C . n 
C 1 80  PHE 80  82  82  PHE PHE C . n 
C 1 81  GLY 81  83  83  GLY GLY C . n 
C 1 82  PHE 82  84  84  PHE PHE C . n 
C 1 83  HIS 83  85  85  HIS HIS C . n 
C 1 84  ASN 84  86  86  ASN ASN C . n 
C 1 85  ILE 85  87  87  ILE ILE C . n 
C 1 86  ALA 86  88  88  ALA ALA C . n 
C 1 87  SER 87  89  89  SER SER C . n 
C 1 88  LYS 88  90  90  LYS LYS C . n 
C 1 89  ILE 89  91  91  ILE ILE C . n 
C 1 90  HIS 90  92  92  HIS HIS C . n 
C 1 91  SER 91  93  93  SER SER C . n 
C 1 92  SER 92  94  94  SER SER C . n 
C 1 93  ALA 93  95  95  ALA ALA C . n 
C 1 94  PHE 94  96  96  PHE PHE C . n 
C 1 95  GLY 95  97  97  GLY GLY C . n 
C 1 96  SER 96  98  98  SER SER C . n 
C 1 97  ASN 97  99  99  ASN ASN C . n 
C 1 98  ASN 98  100 100 ASN ASN C . n 
C 1 99  ALA 99  101 101 ALA ALA C . n 
C 1 100 ALA 100 102 102 ALA ALA C . n 
C 1 101 ASP 101 103 103 ASP ASP C . n 
C 1 102 GLY 102 104 104 GLY GLY C . n 
C 1 103 VAL 103 105 105 VAL VAL C . n 
C 1 104 ASN 104 106 106 ASN ASN C . n 
C 1 105 SER 105 107 107 SER SER C . n 
C 1 106 SER 106 108 108 SER SER C . n 
C 1 107 ALA 107 109 109 ALA ALA C . n 
C 1 108 PHE 108 110 110 PHE PHE C . n 
C 1 109 GLY 109 111 111 GLY GLY C . n 
C 1 110 PHE 110 112 112 PHE PHE C . n 
C 1 111 LYS 111 113 113 LYS LYS C . n 
C 1 112 ASN 112 114 114 ASN ASN C . n 
C 1 113 THR 113 115 115 THR THR C . n 
C 1 114 VAL 114 116 116 VAL VAL C . n 
C 1 115 SER 115 117 117 SER SER C . n 
C 1 116 GLY 116 118 118 GLY GLY C . n 
C 1 117 PHE 117 119 119 PHE PHE C . n 
C 1 118 ASN 118 120 120 ASN ASN C . n 
C 1 119 SER 119 121 121 SER SER C . n 
C 1 120 SER 120 122 122 SER SER C . n 
C 1 121 ALA 121 123 123 ALA ALA C . n 
C 1 122 PHE 122 124 124 PHE PHE C . n 
C 1 123 GLY 123 125 125 GLY GLY C . n 
C 1 124 SER 124 126 126 SER SER C . n 
C 1 125 GLN 125 127 127 GLN GLN C . n 
C 1 126 TYR 126 128 128 TYR TYR C . n 
C 1 127 GLN 127 129 129 GLN GLN C . n 
C 1 128 VAL 128 130 130 VAL VAL C . n 
C 1 129 THR 129 131 131 THR THR C . n 
C 1 130 GLY 130 132 132 GLY GLY C . n 
C 1 131 ASN 131 133 133 ASN ASN C . n 
C 1 132 PHE 132 134 134 PHE PHE C . n 
C 1 133 SER 133 135 135 SER SER C . n 
C 1 134 GLY 134 136 136 GLY GLY C . n 
C 1 135 ALA 135 137 137 ALA ALA C . n 
C 1 136 PHE 136 138 138 PHE PHE C . n 
C 1 137 GLY 137 139 139 GLY GLY C . n 
C 1 138 MET 138 140 140 MET MET C . n 
C 1 139 GLY 139 141 141 GLY GLY C . n 
C 1 140 GLU 140 142 142 GLU GLU C . n 
C 1 141 PHE 141 143 143 PHE PHE C . n 
C 1 142 ASN 142 144 144 ASN ASN C . n 
C 1 143 GLY 143 145 145 GLY GLY C . n 
C 1 144 GLN 144 146 146 GLN GLN C . n 
C 1 145 TYR 145 147 147 TYR TYR C . n 
C 1 146 GLN 146 148 148 GLN GLN C . n 
C 1 147 TYR 147 149 149 TYR TYR C . n 
C 1 148 LYS 148 150 150 LYS LYS C . n 
C 1 149 ASN 149 151 151 ASN ASN C . n 
C 1 150 GLU 150 152 152 GLU GLU C . n 
C 1 151 GLY 151 153 153 GLY GLY C . n 
C 1 152 ASN 152 154 154 ASN ASN C . n 
C 1 153 ASN 153 155 155 ASN ASN C . n 
C 1 154 SER 154 156 156 SER SER C . n 
C 1 155 TYR 155 157 157 TYR TYR C . n 
C 1 156 MET 156 158 158 MET MET C . n 
C 1 157 ILE 157 159 159 ILE ILE C . n 
C 1 158 GLY 158 160 160 GLY GLY C . n 
C 1 159 ASN 159 161 161 ASN ASN C . n 
C 1 160 LYS 160 162 162 LYS LYS C . n 
C 1 161 ASN 161 163 163 ASN ASN C . n 
C 1 162 LYS 162 164 164 LYS LYS C . n 
C 1 163 ILE 163 165 165 ILE ILE C . n 
C 1 164 ALA 164 166 166 ALA ALA C . n 
C 1 165 SER 165 167 167 SER SER C . n 
C 1 166 GLY 166 168 168 GLY GLY C . n 
C 1 167 SER 167 169 169 SER SER C . n 
C 1 168 ASP 168 170 170 ASP ASP C . n 
C 1 169 ASP 169 171 171 ASP ASP C . n 
C 1 170 ASN 170 172 172 ASN ASN C . n 
C 1 171 PHE 171 173 173 PHE PHE C . n 
C 1 172 ILE 172 174 174 ILE ILE C . n 
C 1 173 LEU 173 175 175 LEU LEU C . n 
C 1 174 GLY 174 176 176 GLY GLY C . n 
C 1 175 ASN 175 177 177 ASN ASN C . n 
C 1 176 ASN 176 178 178 ASN ASN C . n 
C 1 177 VAL 177 179 179 VAL VAL C . n 
C 1 178 HIS 178 180 180 HIS HIS C . n 
C 1 179 ILE 179 181 181 ILE ILE C . n 
C 1 180 GLY 180 182 182 GLY GLY C . n 
C 1 181 GLY 181 183 183 GLY GLY C . n 
C 1 182 GLY 182 184 184 GLY GLY C . n 
C 1 183 ILE 183 185 185 ILE ILE C . n 
C 1 184 ASN 184 186 186 ASN ASN C . n 
C 1 185 ASN 185 187 187 ASN ASN C . n 
C 1 186 SER 186 188 188 SER SER C . n 
C 1 187 VAL 187 189 189 VAL VAL C . n 
C 1 188 ALA 188 190 190 ALA ALA C . n 
C 1 189 LEU 189 191 191 LEU LEU C . n 
C 1 190 GLY 190 192 192 GLY GLY C . n 
C 1 191 ASN 191 193 193 ASN ASN C . n 
C 1 192 ASN 192 194 194 ASN ASN C . n 
C 1 193 SER 193 195 195 SER SER C . n 
C 1 194 THR 194 196 196 THR THR C . n 
C 1 195 VAL 195 197 197 VAL VAL C . n 
C 1 196 SER 196 198 198 SER SER C . n 
C 1 197 ALA 197 199 199 ALA ALA C . n 
C 1 198 SER 198 200 200 SER SER C . n 
C 1 199 ASN 199 201 201 ASN ASN C . n 
C 1 200 THR 200 202 202 THR THR C . n 
C 1 201 VAL 201 203 203 VAL VAL C . n 
C 1 202 SER 202 204 204 SER SER C . n 
C 1 203 VAL 203 205 205 VAL VAL C . n 
C 1 204 GLY 204 206 206 GLY GLY C . n 
C 1 205 SER 205 207 207 SER SER C . n 
C 1 206 SER 206 208 208 SER SER C . n 
C 1 207 THR 207 209 209 THR THR C . n 
C 1 208 LEU 208 210 210 LEU LEU C . n 
C 1 209 LYS 209 211 211 LYS LYS C . n 
C 1 210 ARG 210 212 212 ARG ARG C . n 
C 1 211 LYS 211 213 213 LYS LYS C . n 
C 1 212 ILE 212 214 214 ILE ILE C . n 
C 1 213 VAL 213 215 215 VAL VAL C . n 
C 1 214 ASN 214 216 216 ASN ASN C . n 
C 1 215 VAL 215 217 217 VAL VAL C . n 
C 1 216 GLY 216 218 218 GLY GLY C . n 
C 1 217 ASP 217 219 219 ASP ASP C . n 
C 1 218 GLY 218 220 220 GLY GLY C . n 
C 1 219 ALA 219 221 221 ALA ALA C . n 
C 1 220 ILE 220 222 222 ILE ILE C . n 
C 1 221 SER 221 223 223 SER SER C . n 
C 1 222 ALA 222 224 224 ALA ALA C . n 
C 1 223 ASN 223 225 225 ASN ASN C . n 
C 1 224 SER 224 226 226 SER SER C . n 
C 1 225 SER 225 227 227 SER SER C . n 
C 1 226 ASP 226 228 228 ASP ASP C . n 
C 1 227 ALA 227 229 229 ALA ALA C . n 
C 1 228 VAL 228 230 230 VAL VAL C . n 
C 1 229 THR 229 231 231 THR THR C . n 
C 1 230 GLY 230 232 232 GLY GLY C . n 
C 1 231 ARG 231 233 233 ARG ARG C . n 
C 1 232 GLN 232 234 234 GLN GLN C . n 
C 1 233 LEU 233 235 235 LEU LEU C . n 
C 1 234 TYR 234 236 236 TYR TYR C . n 
C 1 235 SER 235 237 237 SER SER C . n 
C 1 236 GLY 236 238 238 GLY GLY C . n 
C 1 237 ASN 237 239 239 ASN ASN C . n 
C 1 238 GLY 238 240 240 GLY GLY C . n 
C 1 239 ILE 239 241 241 ILE ILE C . n 
C 1 240 ASP 240 242 242 ASP ASP C . n 
C 1 241 THR 241 243 243 THR THR C . n 
C 1 242 ALA 242 244 244 ALA ALA C . n 
C 1 243 ALA 243 245 245 ALA ALA C . n 
C 1 244 TRP 244 246 246 TRP TRP C . n 
C 1 245 GLN 245 247 247 GLN GLN C . n 
C 1 246 ASN 246 248 248 ASN ASN C . n 
C 1 247 LYS 247 249 249 LYS LYS C . n 
C 1 248 LEU 248 250 250 LEU LEU C . n 
C 1 249 ASN 249 251 251 ASN ASN C . n 
C 1 250 VAL 250 252 252 VAL VAL C . n 
C 1 251 THR 251 253 253 THR THR C . n 
C 1 252 ARG 252 254 254 ARG ARG C . n 
C 1 253 LYS 253 255 255 LYS LYS C . n 
C 1 254 ASN 254 256 256 ASN ASN C . n 
C 1 255 ASP 255 257 257 ASP ASP C . n 
C 1 256 TYR 256 258 258 TYR TYR C . n 
C 1 257 LYS 257 259 259 LYS LYS C . n 
C 1 258 ASP 258 260 260 ASP ASP C . n 
C 1 259 ALA 259 261 261 ALA ALA C . n 
C 1 260 ASN 260 262 262 ASN ASN C . n 
C 1 261 ASP 261 263 263 ASP ASP C . n 
C 1 262 ILE 262 264 264 ILE ILE C . n 
C 1 263 ASP 263 265 265 ASP ASP C . n 
C 1 264 VAL 264 266 266 VAL VAL C . n 
C 1 265 ASN 265 267 267 ASN ASN C . n 
C 1 266 LYS 266 268 268 LYS LYS C . n 
C 1 267 TRP 267 269 269 TRP TRP C . n 
C 1 268 LYS 268 270 270 LYS LYS C . n 
C 1 269 ALA 269 271 271 ALA ALA C . n 
C 1 270 LYS 270 272 272 LYS LYS C . n 
C 1 271 LEU 271 273 273 LEU LEU C . n 
C 1 272 GLY 272 274 274 GLY GLY C . n 
C 1 273 VAL 273 275 ?   ?   ?   C . n 
C 1 274 GLY 274 276 ?   ?   ?   C . n 
C 1 275 SER 275 277 ?   ?   ?   C . n 
C 1 276 GLY 276 278 ?   ?   ?   C . n 
C 1 277 GLY 277 279 ?   ?   ?   C . n 
C 1 278 GLY 278 280 ?   ?   ?   C . n 
C 1 279 GLY 279 281 ?   ?   ?   C . n 
C 1 280 GLY 280 282 ?   ?   ?   C . n 
C 1 281 ALA 281 283 ?   ?   ?   C . n 
C 1 282 PRO 282 284 ?   ?   ?   C . n 
C 1 283 VAL 283 285 ?   ?   ?   C . n 
C 1 284 ASP 284 286 ?   ?   ?   C . n 
C 1 285 ALA 285 287 ?   ?   ?   C . n 
C 1 286 TYR 286 288 ?   ?   ?   C . n 
C 1 287 THR 287 289 ?   ?   ?   C . n 
C 1 288 LYS 288 290 ?   ?   ?   C . n 
C 1 289 SER 289 291 ?   ?   ?   C . n 
C 1 290 GLU 290 292 ?   ?   ?   C . n 
C 1 291 ALA 291 293 ?   ?   ?   C . n 
C 1 292 ASP 292 294 ?   ?   ?   C . n 
C 1 293 ASN 293 295 ?   ?   ?   C . n 
C 1 294 LYS 294 296 ?   ?   ?   C . n 
C 1 295 PHE 295 297 ?   ?   ?   C . n 
C 1 296 ALA 296 298 ?   ?   ?   C . n 
C 1 297 ASN 297 299 ?   ?   ?   C . n 
C 1 298 LYS 298 300 ?   ?   ?   C . n 
C 1 299 THR 299 301 ?   ?   ?   C . n 
C 1 300 ASP 300 302 ?   ?   ?   C . n 
C 1 301 LEU 301 303 ?   ?   ?   C . n 
C 1 302 ASN 302 304 ?   ?   ?   C . n 
C 1 303 ASP 303 305 ?   ?   ?   C . n 
C 1 304 TYR 304 306 ?   ?   ?   C . n 
C 1 305 THR 305 307 ?   ?   ?   C . n 
C 1 306 LYS 306 308 ?   ?   ?   C . n 
C 1 307 LYS 307 309 ?   ?   ?   C . n 
C 1 308 ASP 308 310 ?   ?   ?   C . n 
C 1 309 ASP 309 311 ?   ?   ?   C . n 
C 1 310 TYR 310 312 ?   ?   ?   C . n 
C 1 311 LYS 311 313 ?   ?   ?   C . n 
C 1 312 ASP 312 314 ?   ?   ?   C . n 
C 1 313 ALA 313 315 ?   ?   ?   C . n 
C 1 314 ASN 314 316 ?   ?   ?   C . n 
C 1 315 GLY 315 317 ?   ?   ?   C . n 
C 1 316 ILE 316 318 ?   ?   ?   C . n 
C 1 317 ASP 317 319 ?   ?   ?   C . n 
C 1 318 VAL 318 320 ?   ?   ?   C . n 
C 1 319 ASP 319 321 ?   ?   ?   C . n 
C 1 320 LYS 320 322 ?   ?   ?   C . n 
C 1 321 TRP 321 323 ?   ?   ?   C . n 
C 1 322 LYS 322 324 ?   ?   ?   C . n 
C 1 323 ALA 323 325 ?   ?   ?   C . n 
C 1 324 LYS 324 326 ?   ?   ?   C . n 
C 1 325 LEU 325 327 ?   ?   ?   C . n 
C 1 326 GLY 326 328 ?   ?   ?   C . n 
C 1 327 THR 327 329 ?   ?   ?   C . n 
C 1 328 GLY 328 330 ?   ?   ?   C . n 
C 1 329 ALA 329 331 ?   ?   ?   C . n 
C 1 330 GLY 330 332 ?   ?   ?   C . n 
C 1 331 THR 331 333 ?   ?   ?   C . n 
C 1 332 ALA 332 334 ?   ?   ?   C . n 
C 1 333 ASP 333 335 ?   ?   ?   C . n 
C 1 334 ILE 334 336 ?   ?   ?   C . n 
C 1 335 GLU 335 337 ?   ?   ?   C . n 
C 1 336 ASN 336 338 ?   ?   ?   C . n 
C 1 337 LEU 337 339 ?   ?   ?   C . n 
C 1 338 ARG 338 340 ?   ?   ?   C . n 
C 1 339 ASN 339 341 ?   ?   ?   C . n 
C 1 340 GLU 340 342 ?   ?   ?   C . n 
C 1 341 VAL 341 343 ?   ?   ?   C . n 
C 1 342 ASN 342 344 ?   ?   ?   C . n 
C 1 343 GLU 343 345 ?   ?   ?   C . n 
C 1 344 LYS 344 346 ?   ?   ?   C . n 
C 1 345 ILE 345 347 ?   ?   ?   C . n 
C 1 346 ASP 346 348 ?   ?   ?   C . n 
C 1 347 ASP 347 349 ?   ?   ?   C . n 
C 1 348 VAL 348 350 ?   ?   ?   C . n 
C 1 349 LYS 349 351 ?   ?   ?   C . n 
C 1 350 ASP 350 352 ?   ?   ?   C . n 
C 1 351 GLU 351 353 ?   ?   ?   C . n 
C 1 352 VAL 352 354 ?   ?   ?   C . n 
C 1 353 ARG 353 355 ?   ?   ?   C . n 
C 1 354 THR 354 356 ?   ?   ?   C . n 
C 1 355 VAL 355 357 ?   ?   ?   C . n 
C 1 356 GLY 356 358 ?   ?   ?   C . n 
C 1 357 SER 357 359 ?   ?   ?   C . n 
C 1 358 LEU 358 360 ?   ?   ?   C . n 
C 1 359 SER 359 361 ?   ?   ?   C . n 
C 1 360 ALA 360 362 ?   ?   ?   C . n 
C 1 361 ALA 361 363 ?   ?   ?   C . n 
C 1 362 LEU 362 364 ?   ?   ?   C . n 
C 1 363 ALA 363 365 ?   ?   ?   C . n 
C 1 364 GLY 364 366 ?   ?   ?   C . n 
C 1 365 LEU 365 367 ?   ?   ?   C . n 
C 1 366 HIS 366 368 ?   ?   ?   C . n 
C 1 367 PRO 367 369 ?   ?   ?   C . n 
C 1 368 MET 368 370 ?   ?   ?   C . n 
C 1 369 GLN 369 371 ?   ?   ?   C . n 
C 1 370 TYR 370 372 ?   ?   ?   C . n 
C 1 371 ASP 371 373 ?   ?   ?   C . n 
C 1 372 PRO 372 374 ?   ?   ?   C . n 
C 1 373 LYS 373 375 ?   ?   ?   C . n 
C 1 374 ALA 374 376 ?   ?   ?   C . n 
C 1 375 PRO 375 377 ?   ?   ?   C . n 
C 1 376 VAL 376 378 ?   ?   ?   C . n 
C 1 377 GLN 377 379 ?   ?   ?   C . n 
C 1 378 VAL 378 380 ?   ?   ?   C . n 
C 1 379 MET 379 381 ?   ?   ?   C . n 
C 1 380 ALA 380 382 ?   ?   ?   C . n 
C 1 381 ALA 381 383 ?   ?   ?   C . n 
C 1 382 LEU 382 384 ?   ?   ?   C . n 
C 1 383 GLY 383 385 ?   ?   ?   C . n 
C 1 384 HIS 384 386 ?   ?   ?   C . n 
C 1 385 TYR 385 387 ?   ?   ?   C . n 
C 1 386 ARG 386 388 ?   ?   ?   C . n 
C 1 387 ASP 387 389 ?   ?   ?   C . n 
C 1 388 LYS 388 390 ?   ?   ?   C . n 
C 1 389 GLN 389 391 ?   ?   ?   C . n 
C 1 390 SER 390 392 ?   ?   ?   C . n 
C 1 391 VAL 391 393 ?   ?   ?   C . n 
C 1 392 ALA 392 394 ?   ?   ?   C . n 
C 1 393 VAL 393 395 ?   ?   ?   C . n 
C 1 394 GLY 394 396 ?   ?   ?   C . n 
C 1 395 ALA 395 397 ?   ?   ?   C . n 
C 1 396 SER 396 398 ?   ?   ?   C . n 
C 1 397 TYR 397 399 ?   ?   ?   C . n 
C 1 398 TYR 398 400 ?   ?   ?   C . n 
C 1 399 PHE 399 401 ?   ?   ?   C . n 
C 1 400 ASN 400 402 ?   ?   ?   C . n 
C 1 401 ASP 401 403 ?   ?   ?   C . n 
C 1 402 ARG 402 404 ?   ?   ?   C . n 
C 1 403 PHE 403 405 ?   ?   ?   C . n 
C 1 404 MET 404 406 ?   ?   ?   C . n 
C 1 405 MET 405 407 ?   ?   ?   C . n 
C 1 406 SER 406 408 ?   ?   ?   C . n 
C 1 407 THR 407 409 ?   ?   ?   C . n 
C 1 408 GLY 408 410 ?   ?   ?   C . n 
C 1 409 ILE 409 411 ?   ?   ?   C . n 
C 1 410 ALA 410 412 ?   ?   ?   C . n 
C 1 411 LEU 411 413 ?   ?   ?   C . n 
C 1 412 SER 412 414 ?   ?   ?   C . n 
C 1 413 GLY 413 415 ?   ?   ?   C . n 
C 1 414 GLU 414 416 ?   ?   ?   C . n 
C 1 415 LYS 415 417 ?   ?   ?   C . n 
C 1 416 ARG 416 418 ?   ?   ?   C . n 
C 1 417 THR 417 419 ?   ?   ?   C . n 
C 1 418 LYS 418 420 ?   ?   ?   C . n 
C 1 419 THR 419 421 ?   ?   ?   C . n 
C 1 420 MET 420 422 ?   ?   ?   C . n 
C 1 421 ALA 421 423 ?   ?   ?   C . n 
C 1 422 ASN 422 424 ?   ?   ?   C . n 
C 1 423 VAL 423 425 ?   ?   ?   C . n 
C 1 424 GLY 424 426 ?   ?   ?   C . n 
C 1 425 PHE 425 427 ?   ?   ?   C . n 
C 1 426 THR 426 428 ?   ?   ?   C . n 
C 1 427 LEU 427 429 ?   ?   ?   C . n 
C 1 428 LYS 428 430 ?   ?   ?   C . n 
C 1 429 LEU 429 431 ?   ?   ?   C . n 
C 1 430 GLY 430 432 ?   ?   ?   C . n 
C 1 431 LYS 431 433 ?   ?   ?   C . n 
C 1 432 GLY 432 434 ?   ?   ?   C . n 
C 1 433 SER 433 435 ?   ?   ?   C . n 
C 1 434 GLY 434 436 ?   ?   ?   C . n 
C 1 435 VAL 435 437 ?   ?   ?   C . n 
C 1 436 THR 436 438 ?   ?   ?   C . n 
C 1 437 TYR 437 439 ?   ?   ?   C . n 
C 1 438 ASP 438 440 ?   ?   ?   C . n 
C 1 439 GLU 439 441 ?   ?   ?   C . n 
C 1 440 THR 440 442 ?   ?   ?   C . n 
C 1 441 PRO 441 443 ?   ?   ?   C . n 
C 1 442 GLN 442 444 ?   ?   ?   C . n 
C 1 443 TYR 443 445 ?   ?   ?   C . n 
C 1 444 VAL 444 446 ?   ?   ?   C . n 
C 1 445 VAL 445 447 ?   ?   ?   C . n 
C 1 446 GLN 446 448 ?   ?   ?   C . n 
C 1 447 ASN 447 449 ?   ?   ?   C . n 
C 1 448 GLU 448 450 ?   ?   ?   C . n 
C 1 449 VAL 449 451 ?   ?   ?   C . n 
C 1 450 LYS 450 452 ?   ?   ?   C . n 
C 1 451 ARG 451 453 ?   ?   ?   C . n 
C 1 452 LEU 452 454 ?   ?   ?   C . n 
C 1 453 THR 453 455 ?   ?   ?   C . n 
C 1 454 VAL 454 456 ?   ?   ?   C . n 
C 1 455 GLU 455 457 ?   ?   ?   C . n 
C 1 456 ASN 456 458 ?   ?   ?   C . n 
C 1 457 GLN 457 459 ?   ?   ?   C . n 
C 1 458 GLU 458 460 ?   ?   ?   C . n 
C 1 459 LEU 459 461 ?   ?   ?   C . n 
C 1 460 LYS 460 462 ?   ?   ?   C . n 
C 1 461 GLU 461 463 ?   ?   ?   C . n 
C 1 462 ARG 462 464 ?   ?   ?   C . n 
C 1 463 VAL 463 465 ?   ?   ?   C . n 
C 1 464 ARG 464 466 ?   ?   ?   C . n 
C 1 465 ASN 465 467 ?   ?   ?   C . n 
C 1 466 LEU 466 468 ?   ?   ?   C . n 
C 1 467 GLU 467 469 ?   ?   ?   C . n 
C 1 468 GLU 468 470 ?   ?   ?   C . n 
C 1 469 LYS 469 471 ?   ?   ?   C . n 
C 1 470 LEU 470 472 ?   ?   ?   C . n 
C 1 471 ASN 471 473 ?   ?   ?   C . n 
C 1 472 MET 472 474 ?   ?   ?   C . n 
C 1 473 LEU 473 475 ?   ?   ?   C . n 
C 1 474 LEU 474 476 ?   ?   ?   C . n 
C 1 475 LYS 475 477 ?   ?   ?   C . n 
C 1 476 ASN 476 478 ?   ?   ?   C . n 
C 1 477 LYS 477 479 ?   ?   ?   C . n 
C 1 478 ARG 478 480 ?   ?   ?   C . n 
C 1 479 SER 479 481 ?   ?   ?   C . n 
C 1 480 SER 480 482 ?   ?   ?   C . n 
C 1 481 ALA 481 483 ?   ?   ?   C . n 
C 1 482 TRP 482 484 ?   ?   ?   C . n 
C 1 483 SER 483 485 ?   ?   ?   C . n 
C 1 484 HIS 484 486 ?   ?   ?   C . n 
C 1 485 PRO 485 487 ?   ?   ?   C . n 
C 1 486 GLN 486 488 ?   ?   ?   C . n 
C 1 487 PHE 487 489 ?   ?   ?   C . n 
C 1 488 GLU 488 490 ?   ?   ?   C . n 
C 1 489 LYS 489 491 ?   ?   ?   C . n 
D 2 1   GLN 1   35  35  GLN GLN D . n 
D 2 2   LEU 2   36  36  LEU LEU D . n 
D 2 3   THR 3   37  37  THR THR D . n 
D 2 4   THR 4   38  38  THR THR D . n 
D 2 5   GLU 5   39  39  GLU GLU D . n 
D 2 6   SER 6   40  40  SER SER D . n 
D 2 7   MET 7   41  41  MET MET D . n 
D 2 8   PRO 8   42  42  PRO PRO D . n 
D 2 9   PHE 9   43  43  PHE PHE D . n 
D 2 10  ASN 10  44  44  ASN ASN D . n 
D 2 11  VAL 11  45  45  VAL VAL D . n 
D 2 12  ALA 12  46  46  ALA ALA D . n 
D 2 13  GLU 13  47  47  GLU GLU D . n 
D 2 14  GLY 14  48  48  GLY GLY D . n 
D 2 15  LYS 15  49  49  LYS LYS D . n 
D 2 16  GLU 16  50  50  GLU GLU D . n 
D 2 17  VAL 17  51  51  VAL VAL D . n 
D 2 18  LEU 18  52  52  LEU LEU D . n 
D 2 19  LEU 19  53  53  LEU LEU D . n 
D 2 20  LEU 20  54  54  LEU LEU D . n 
D 2 21  VAL 21  55  55  VAL VAL D . n 
D 2 22  HIS 22  56  56  HIS HIS D . n 
D 2 23  ASN 23  57  57  ASN ASN D . n 
D 2 24  LEU 24  58  58  LEU LEU D . n 
D 2 25  PRO 25  59  59  PRO PRO D . n 
D 2 26  GLN 26  60  60  GLN GLN D . n 
D 2 27  GLN 27  61  61  GLN GLN D . n 
D 2 28  LEU 28  62  62  LEU LEU D . n 
D 2 29  PHE 29  63  63  PHE PHE D . n 
D 2 30  GLY 30  64  64  GLY GLY D . n 
D 2 31  TYR 31  65  65  TYR TYR D . n 
D 2 32  SER 32  66  66  SER SER D . n 
D 2 33  TRP 33  67  67  TRP TRP D . n 
D 2 34  TYR 34  68  68  TYR TYR D . n 
D 2 35  LYS 35  69  69  LYS LYS D . n 
D 2 36  GLY 36  70  70  GLY GLY D . n 
D 2 37  GLU 37  71  71  GLU GLU D . n 
D 2 38  ARG 38  72  72  ARG ARG D . n 
D 2 39  VAL 39  73  73  VAL VAL D . n 
D 2 40  ASP 40  74  74  ASP ASP D . n 
D 2 41  GLY 41  75  75  GLY GLY D . n 
D 2 42  ASN 42  76  76  ASN ASN D . n 
D 2 43  ARG 43  77  77  ARG ARG D . n 
D 2 44  GLN 44  78  78  GLN GLN D . n 
D 2 45  ILE 45  79  79  ILE ILE D . n 
D 2 46  VAL 46  80  80  VAL VAL D . n 
D 2 47  GLY 47  81  81  GLY GLY D . n 
D 2 48  TYR 48  82  82  TYR TYR D . n 
D 2 49  ALA 49  83  83  ALA ALA D . n 
D 2 50  ILE 50  84  84  ILE ILE D . n 
D 2 51  GLY 51  85  85  GLY GLY D . n 
D 2 52  THR 52  86  86  THR THR D . n 
D 2 53  GLN 53  87  87  GLN GLN D . n 
D 2 54  GLN 54  88  88  GLN GLN D . n 
D 2 55  ALA 55  89  89  ALA ALA D . n 
D 2 56  THR 56  90  90  THR THR D . n 
D 2 57  PRO 57  91  91  PRO PRO D . n 
D 2 58  GLY 58  92  92  GLY GLY D . n 
D 2 59  PRO 59  93  93  PRO PRO D . n 
D 2 60  ALA 60  94  94  ALA ALA D . n 
D 2 61  ASN 61  95  95  ASN ASN D . n 
D 2 62  SER 62  96  96  SER SER D . n 
D 2 63  GLY 63  97  97  GLY GLY D . n 
D 2 64  ARG 64  98  98  ARG ARG D . n 
D 2 65  GLU 65  99  99  GLU GLU D . n 
D 2 66  THR 66  100 100 THR THR D . n 
D 2 67  ILE 67  101 101 ILE ILE D . n 
D 2 68  TYR 68  102 102 TYR TYR D . n 
D 2 69  PRO 69  103 103 PRO PRO D . n 
D 2 70  ASN 70  104 104 ASN ASN D . n 
D 2 71  ALA 71  105 105 ALA ALA D . n 
D 2 72  SER 72  106 106 SER SER D . n 
D 2 73  LEU 73  107 107 LEU LEU D . n 
D 2 74  LEU 74  108 108 LEU LEU D . n 
D 2 75  ILE 75  109 109 ILE ILE D . n 
D 2 76  GLN 76  110 110 GLN GLN D . n 
D 2 77  ASN 77  111 111 ASN ASN D . n 
D 2 78  VAL 78  112 112 VAL VAL D . n 
D 2 79  THR 79  113 113 THR THR D . n 
D 2 80  GLN 80  114 114 GLN GLN D . n 
D 2 81  ASN 81  115 115 ASN ASN D . n 
D 2 82  ASP 82  116 116 ASP ASP D . n 
D 2 83  THR 83  117 117 THR THR D . n 
D 2 84  GLY 84  118 118 GLY GLY D . n 
D 2 85  PHE 85  119 119 PHE PHE D . n 
D 2 86  TYR 86  120 120 TYR TYR D . n 
D 2 87  THR 87  121 121 THR THR D . n 
D 2 88  LEU 88  122 122 LEU LEU D . n 
D 2 89  GLN 89  123 123 GLN GLN D . n 
D 2 90  VAL 90  124 124 VAL VAL D . n 
D 2 91  ILE 91  125 125 ILE ILE D . n 
D 2 92  LYS 92  126 126 LYS LYS D . n 
D 2 93  SER 93  127 127 SER SER D . n 
D 2 94  ASP 94  128 128 ASP ASP D . n 
D 2 95  LEU 95  129 129 LEU LEU D . n 
D 2 96  VAL 96  130 130 VAL VAL D . n 
D 2 97  ASN 97  131 131 ASN ASN D . n 
D 2 98  GLU 98  132 132 GLU GLU D . n 
D 2 99  GLU 99  133 133 GLU GLU D . n 
D 2 100 ALA 100 134 134 ALA ALA D . n 
D 2 101 THR 101 135 135 THR THR D . n 
D 2 102 GLY 102 136 136 GLY GLY D . n 
D 2 103 GLN 103 137 137 GLN GLN D . n 
D 2 104 PHE 104 138 138 PHE PHE D . n 
D 2 105 HIS 105 139 139 HIS HIS D . n 
D 2 106 VAL 106 140 140 VAL VAL D . n 
D 2 107 TYR 107 141 141 TYR TYR D . n 
D 2 108 PRO 108 142 142 PRO PRO D . n 
D 2 109 GLU 109 143 143 GLU GLU D . n 
D 2 110 LEU 110 144 144 LEU LEU D . n 
D 2 111 PRO 111 145 145 PRO PRO D . n 
D 2 112 LYS 112 146 146 LYS LYS D . n 
D 2 113 PRO 113 147 147 PRO PRO D . n 
D 2 114 SER 114 148 148 SER SER D . n 
D 2 115 ILE 115 149 149 ILE ILE D . n 
D 2 116 SER 116 150 150 SER SER D . n 
D 2 117 SER 117 151 151 SER SER D . n 
D 2 118 ASN 118 152 152 ASN ASN D . n 
D 2 119 ASN 119 153 153 ASN ASN D . n 
D 2 120 SER 120 154 154 SER SER D . n 
D 2 121 ASN 121 155 155 ASN ASN D . n 
D 2 122 PRO 122 156 156 PRO PRO D . n 
D 2 123 VAL 123 157 157 VAL VAL D . n 
D 2 124 GLU 124 158 158 GLU GLU D . n 
D 2 125 ASP 125 159 159 ASP ASP D . n 
D 2 126 LYS 126 160 160 LYS LYS D . n 
D 2 127 ASP 127 161 161 ASP ASP D . n 
D 2 128 ALA 128 162 162 ALA ALA D . n 
D 2 129 VAL 129 163 163 VAL VAL D . n 
D 2 130 ALA 130 164 164 ALA ALA D . n 
D 2 131 PHE 131 165 165 PHE PHE D . n 
D 2 132 THR 132 166 166 THR THR D . n 
D 2 133 CYS 133 167 167 CYS CYS D . n 
D 2 134 GLU 134 168 168 GLU GLU D . n 
D 2 135 PRO 135 169 169 PRO PRO D . n 
D 2 136 GLU 136 170 170 GLU GLU D . n 
D 2 137 THR 137 171 171 THR THR D . n 
D 2 138 GLN 138 172 172 GLN GLN D . n 
D 2 139 ASP 139 173 173 ASP ASP D . n 
D 2 140 THR 140 174 174 THR THR D . n 
D 2 141 THR 141 175 175 THR THR D . n 
D 2 142 TYR 142 176 176 TYR TYR D . n 
D 2 143 LEU 143 177 177 LEU LEU D . n 
D 2 144 TRP 144 178 178 TRP TRP D . n 
D 2 145 TRP 145 179 179 TRP TRP D . n 
D 2 146 ILE 146 180 180 ILE ILE D . n 
D 2 147 ASN 147 181 181 ASN ASN D . n 
D 2 148 ASN 148 182 182 ASN ASN D . n 
D 2 149 GLN 149 183 183 GLN GLN D . n 
D 2 150 SER 150 184 184 SER SER D . n 
D 2 151 LEU 151 185 185 LEU LEU D . n 
D 2 152 PRO 152 186 186 PRO PRO D . n 
D 2 153 VAL 153 187 187 VAL VAL D . n 
D 2 154 SER 154 188 188 SER SER D . n 
D 2 155 PRO 155 189 189 PRO PRO D . n 
D 2 156 ARG 156 190 190 ARG ARG D . n 
D 2 157 LEU 157 191 191 LEU LEU D . n 
D 2 158 GLN 158 192 192 GLN GLN D . n 
D 2 159 LEU 159 193 193 LEU LEU D . n 
D 2 160 SER 160 194 194 SER SER D . n 
D 2 161 ASN 161 195 195 ASN ASN D . n 
D 2 162 GLY 162 196 196 GLY GLY D . n 
D 2 163 ASN 163 197 197 ASN ASN D . n 
D 2 164 ARG 164 198 198 ARG ARG D . n 
D 2 165 THR 165 199 199 THR THR D . n 
D 2 166 LEU 166 200 200 LEU LEU D . n 
D 2 167 THR 167 201 201 THR THR D . n 
D 2 168 LEU 168 202 202 LEU LEU D . n 
D 2 169 LEU 169 203 203 LEU LEU D . n 
D 2 170 SER 170 204 204 SER SER D . n 
D 2 171 VAL 171 205 205 VAL VAL D . n 
D 2 172 THR 172 206 206 THR THR D . n 
D 2 173 ARG 173 207 207 ARG ARG D . n 
D 2 174 ASN 174 208 208 ASN ASN D . n 
D 2 175 ASP 175 209 209 ASP ASP D . n 
D 2 176 THR 176 210 210 THR THR D . n 
D 2 177 GLY 177 211 211 GLY GLY D . n 
D 2 178 PRO 178 212 212 PRO PRO D . n 
D 2 179 TYR 179 213 213 TYR TYR D . n 
D 2 180 GLU 180 214 214 GLU GLU D . n 
D 2 181 CYS 181 215 215 CYS CYS D . n 
D 2 182 GLU 182 216 216 GLU GLU D . n 
D 2 183 ILE 183 217 217 ILE ILE D . n 
D 2 184 GLN 184 218 218 GLN GLN D . n 
D 2 185 ASN 185 219 219 ASN ASN D . n 
D 2 186 PRO 186 220 220 PRO PRO D . n 
D 2 187 VAL 187 221 221 VAL VAL D . n 
D 2 188 SER 188 222 222 SER SER D . n 
D 2 189 ALA 189 223 223 ALA ALA D . n 
D 2 190 ASN 190 224 224 ASN ASN D . n 
D 2 191 ARG 191 225 225 ARG ARG D . n 
D 2 192 SER 192 226 226 SER SER D . n 
D 2 193 ASP 193 227 227 ASP ASP D . n 
D 2 194 PRO 194 228 228 PRO PRO D . n 
D 2 195 VAL 195 229 229 VAL VAL D . n 
D 2 196 THR 196 230 230 THR THR D . n 
D 2 197 LEU 197 231 231 LEU LEU D . n 
D 2 198 ASN 198 232 232 ASN ASN D . n 
D 2 199 VAL 199 233 233 VAL VAL D . n 
D 2 200 THR 200 234 234 THR THR D . n 
D 2 201 TYR 201 235 ?   ?   ?   D . n 
D 2 202 GLY 202 236 ?   ?   ?   D . n 
D 2 203 PRO 203 237 ?   ?   ?   D . n 
D 2 204 ASP 204 238 ?   ?   ?   D . n 
D 2 205 THR 205 239 ?   ?   ?   D . n 
D 2 206 PRO 206 240 ?   ?   ?   D . n 
D 2 207 THR 207 241 ?   ?   ?   D . n 
D 2 208 ILE 208 242 ?   ?   ?   D . n 
D 2 209 SER 209 243 ?   ?   ?   D . n 
D 2 210 PRO 210 244 ?   ?   ?   D . n 
D 2 211 SER 211 245 ?   ?   ?   D . n 
D 2 212 ASP 212 246 ?   ?   ?   D . n 
D 2 213 THR 213 247 ?   ?   ?   D . n 
D 2 214 TYR 214 248 ?   ?   ?   D . n 
D 2 215 TYR 215 249 ?   ?   ?   D . n 
D 2 216 ARG 216 250 ?   ?   ?   D . n 
D 2 217 PRO 217 251 ?   ?   ?   D . n 
D 2 218 GLY 218 252 ?   ?   ?   D . n 
D 2 219 ALA 219 253 ?   ?   ?   D . n 
D 2 220 ASN 220 254 ?   ?   ?   D . n 
D 2 221 LEU 221 255 ?   ?   ?   D . n 
D 2 222 SER 222 256 ?   ?   ?   D . n 
D 2 223 LEU 223 257 ?   ?   ?   D . n 
D 2 224 SER 224 258 ?   ?   ?   D . n 
D 2 225 CYS 225 259 ?   ?   ?   D . n 
D 2 226 TYR 226 260 ?   ?   ?   D . n 
D 2 227 ALA 227 261 ?   ?   ?   D . n 
D 2 228 ALA 228 262 ?   ?   ?   D . n 
D 2 229 SER 229 263 ?   ?   ?   D . n 
D 2 230 ASN 230 264 ?   ?   ?   D . n 
D 2 231 PRO 231 265 ?   ?   ?   D . n 
D 2 232 PRO 232 266 ?   ?   ?   D . n 
D 2 233 ALA 233 267 ?   ?   ?   D . n 
D 2 234 GLN 234 268 ?   ?   ?   D . n 
D 2 235 TYR 235 269 ?   ?   ?   D . n 
D 2 236 SER 236 270 ?   ?   ?   D . n 
D 2 237 TRP 237 271 ?   ?   ?   D . n 
D 2 238 LEU 238 272 ?   ?   ?   D . n 
D 2 239 ILE 239 273 ?   ?   ?   D . n 
D 2 240 ASN 240 274 ?   ?   ?   D . n 
D 2 241 GLY 241 275 ?   ?   ?   D . n 
D 2 242 THR 242 276 ?   ?   ?   D . n 
D 2 243 PHE 243 277 ?   ?   ?   D . n 
D 2 244 GLN 244 278 ?   ?   ?   D . n 
D 2 245 GLN 245 279 ?   ?   ?   D . n 
D 2 246 SER 246 280 ?   ?   ?   D . n 
D 2 247 THR 247 281 ?   ?   ?   D . n 
D 2 248 GLN 248 282 ?   ?   ?   D . n 
D 2 249 GLU 249 283 ?   ?   ?   D . n 
D 2 250 LEU 250 284 ?   ?   ?   D . n 
D 2 251 PHE 251 285 ?   ?   ?   D . n 
D 2 252 ILE 252 286 ?   ?   ?   D . n 
D 2 253 PRO 253 287 ?   ?   ?   D . n 
D 2 254 ASN 254 288 ?   ?   ?   D . n 
D 2 255 ILE 255 289 ?   ?   ?   D . n 
D 2 256 THR 256 290 ?   ?   ?   D . n 
D 2 257 VAL 257 291 ?   ?   ?   D . n 
D 2 258 ASN 258 292 ?   ?   ?   D . n 
D 2 259 ASN 259 293 ?   ?   ?   D . n 
D 2 260 SER 260 294 ?   ?   ?   D . n 
D 2 261 GLY 261 295 ?   ?   ?   D . n 
D 2 262 SER 262 296 ?   ?   ?   D . n 
D 2 263 TYR 263 297 ?   ?   ?   D . n 
D 2 264 THR 264 298 ?   ?   ?   D . n 
D 2 265 CYS 265 299 ?   ?   ?   D . n 
D 2 266 HIS 266 300 ?   ?   ?   D . n 
D 2 267 ALA 267 301 ?   ?   ?   D . n 
D 2 268 ASN 268 302 ?   ?   ?   D . n 
D 2 269 ASN 269 303 ?   ?   ?   D . n 
D 2 270 SER 270 304 ?   ?   ?   D . n 
D 2 271 VAL 271 305 ?   ?   ?   D . n 
D 2 272 THR 272 306 ?   ?   ?   D . n 
D 2 273 GLY 273 307 ?   ?   ?   D . n 
D 2 274 CYS 274 308 ?   ?   ?   D . n 
D 2 275 ASN 275 309 ?   ?   ?   D . n 
D 2 276 ARG 276 310 ?   ?   ?   D . n 
D 2 277 THR 277 311 ?   ?   ?   D . n 
D 2 278 THR 278 312 ?   ?   ?   D . n 
D 2 279 VAL 279 313 ?   ?   ?   D . n 
D 2 280 LYS 280 314 ?   ?   ?   D . n 
D 2 281 THR 281 315 ?   ?   ?   D . n 
D 2 282 ILE 282 316 ?   ?   ?   D . n 
D 2 283 ILE 283 317 ?   ?   ?   D . n 
D 2 284 VAL 284 318 ?   ?   ?   D . n 
D 2 285 THR 285 319 ?   ?   ?   D . n 
D 2 286 GLU 286 320 ?   ?   ?   D . n 
D 2 287 LEU 287 321 ?   ?   ?   D . n 
D 2 288 SER 288 322 ?   ?   ?   D . n 
D 2 289 PRO 289 323 ?   ?   ?   D . n 
D 2 290 VAL 290 324 ?   ?   ?   D . n 
D 2 291 VAL 291 325 ?   ?   ?   D . n 
D 2 292 ALA 292 326 ?   ?   ?   D . n 
D 2 293 LYS 293 327 ?   ?   ?   D . n 
D 2 294 PRO 294 328 ?   ?   ?   D . n 
D 2 295 GLN 295 329 ?   ?   ?   D . n 
D 2 296 ILE 296 330 ?   ?   ?   D . n 
D 2 297 LYS 297 331 ?   ?   ?   D . n 
D 2 298 ALA 298 332 ?   ?   ?   D . n 
D 2 299 SER 299 333 ?   ?   ?   D . n 
D 2 300 LYS 300 334 ?   ?   ?   D . n 
D 2 301 THR 301 335 ?   ?   ?   D . n 
D 2 302 THR 302 336 ?   ?   ?   D . n 
D 2 303 VAL 303 337 ?   ?   ?   D . n 
D 2 304 THR 304 338 ?   ?   ?   D . n 
D 2 305 GLY 305 339 ?   ?   ?   D . n 
D 2 306 ASP 306 340 ?   ?   ?   D . n 
D 2 307 LYS 307 341 ?   ?   ?   D . n 
D 2 308 ASP 308 342 ?   ?   ?   D . n 
D 2 309 SER 309 343 ?   ?   ?   D . n 
D 2 310 VAL 310 344 ?   ?   ?   D . n 
D 2 311 ASN 311 345 ?   ?   ?   D . n 
D 2 312 LEU 312 346 ?   ?   ?   D . n 
D 2 313 THR 313 347 ?   ?   ?   D . n 
D 2 314 CYS 314 348 ?   ?   ?   D . n 
D 2 315 SER 315 349 ?   ?   ?   D . n 
D 2 316 THR 316 350 ?   ?   ?   D . n 
D 2 317 ASN 317 351 ?   ?   ?   D . n 
D 2 318 ASP 318 352 ?   ?   ?   D . n 
D 2 319 THR 319 353 ?   ?   ?   D . n 
D 2 320 GLY 320 354 ?   ?   ?   D . n 
D 2 321 ILE 321 355 ?   ?   ?   D . n 
D 2 322 SER 322 356 ?   ?   ?   D . n 
D 2 323 ILE 323 357 ?   ?   ?   D . n 
D 2 324 ARG 324 358 ?   ?   ?   D . n 
D 2 325 TRP 325 359 ?   ?   ?   D . n 
D 2 326 PHE 326 360 ?   ?   ?   D . n 
D 2 327 PHE 327 361 ?   ?   ?   D . n 
D 2 328 LYS 328 362 ?   ?   ?   D . n 
D 2 329 ASN 329 363 ?   ?   ?   D . n 
D 2 330 GLN 330 364 ?   ?   ?   D . n 
D 2 331 SER 331 365 ?   ?   ?   D . n 
D 2 332 LEU 332 366 ?   ?   ?   D . n 
D 2 333 PRO 333 367 ?   ?   ?   D . n 
D 2 334 SER 334 368 ?   ?   ?   D . n 
D 2 335 SER 335 369 ?   ?   ?   D . n 
D 2 336 GLU 336 370 ?   ?   ?   D . n 
D 2 337 ARG 337 371 ?   ?   ?   D . n 
D 2 338 MET 338 372 ?   ?   ?   D . n 
D 2 339 LYS 339 373 ?   ?   ?   D . n 
D 2 340 LEU 340 374 ?   ?   ?   D . n 
D 2 341 SER 341 375 ?   ?   ?   D . n 
D 2 342 GLN 342 376 ?   ?   ?   D . n 
D 2 343 GLY 343 377 ?   ?   ?   D . n 
D 2 344 ASN 344 378 ?   ?   ?   D . n 
D 2 345 THR 345 379 ?   ?   ?   D . n 
D 2 346 THR 346 380 ?   ?   ?   D . n 
D 2 347 LEU 347 381 ?   ?   ?   D . n 
D 2 348 SER 348 382 ?   ?   ?   D . n 
D 2 349 ILE 349 383 ?   ?   ?   D . n 
D 2 350 ASN 350 384 ?   ?   ?   D . n 
D 2 351 PRO 351 385 ?   ?   ?   D . n 
D 2 352 VAL 352 386 ?   ?   ?   D . n 
D 2 353 LYS 353 387 ?   ?   ?   D . n 
D 2 354 ARG 354 388 ?   ?   ?   D . n 
D 2 355 GLU 355 389 ?   ?   ?   D . n 
D 2 356 ASP 356 390 ?   ?   ?   D . n 
D 2 357 ALA 357 391 ?   ?   ?   D . n 
D 2 358 GLY 358 392 ?   ?   ?   D . n 
D 2 359 THR 359 393 ?   ?   ?   D . n 
D 2 360 TYR 360 394 ?   ?   ?   D . n 
D 2 361 TRP 361 395 ?   ?   ?   D . n 
D 2 362 CYS 362 396 ?   ?   ?   D . n 
D 2 363 GLU 363 397 ?   ?   ?   D . n 
D 2 364 VAL 364 398 ?   ?   ?   D . n 
D 2 365 PHE 365 399 ?   ?   ?   D . n 
D 2 366 ASN 366 400 ?   ?   ?   D . n 
D 2 367 PRO 367 401 ?   ?   ?   D . n 
D 2 368 ILE 368 402 ?   ?   ?   D . n 
D 2 369 SER 369 403 ?   ?   ?   D . n 
D 2 370 LYS 370 404 ?   ?   ?   D . n 
D 2 371 ASN 371 405 ?   ?   ?   D . n 
D 2 372 GLN 372 406 ?   ?   ?   D . n 
D 2 373 SER 373 407 ?   ?   ?   D . n 
D 2 374 ASP 374 408 ?   ?   ?   D . n 
D 2 375 PRO 375 409 ?   ?   ?   D . n 
D 2 376 ILE 376 410 ?   ?   ?   D . n 
D 2 377 MET 377 411 ?   ?   ?   D . n 
D 2 378 LEU 378 412 ?   ?   ?   D . n 
D 2 379 ASN 379 413 ?   ?   ?   D . n 
D 2 380 VAL 380 414 ?   ?   ?   D . n 
D 2 381 ASN 381 415 ?   ?   ?   D . n 
D 2 382 TYR 382 416 ?   ?   ?   D . n 
D 2 383 ASN 383 417 ?   ?   ?   D . n 
D 2 384 ALA 384 418 ?   ?   ?   D . n 
D 2 385 LEU 385 419 ?   ?   ?   D . n 
D 2 386 PRO 386 420 ?   ?   ?   D . n 
D 2 387 GLN 387 421 ?   ?   ?   D . n 
D 2 388 GLU 388 422 ?   ?   ?   D . n 
D 2 389 ASN 389 423 ?   ?   ?   D . n 
D 2 390 GLY 390 424 ?   ?   ?   D . n 
D 2 391 LEU 391 425 ?   ?   ?   D . n 
D 2 392 SER 392 426 ?   ?   ?   D . n 
D 2 393 PRO 393 427 ?   ?   ?   D . n 
D 2 394 GLY 394 428 ?   ?   ?   D . n 
D 2 395 HIS 395 429 ?   ?   ?   D . n 
D 2 396 HIS 396 430 ?   ?   ?   D . n 
D 2 397 HIS 397 431 ?   ?   ?   D . n 
D 2 398 HIS 398 432 ?   ?   ?   D . n 
D 2 399 HIS 399 433 ?   ?   ?   D . n 
D 2 400 HIS 400 434 ?   ?   ?   D . n 
E 2 1   GLN 1   35  35  GLN GLN E . n 
E 2 2   LEU 2   36  36  LEU LEU E . n 
E 2 3   THR 3   37  37  THR THR E . n 
E 2 4   THR 4   38  38  THR THR E . n 
E 2 5   GLU 5   39  39  GLU GLU E . n 
E 2 6   SER 6   40  40  SER SER E . n 
E 2 7   MET 7   41  41  MET MET E . n 
E 2 8   PRO 8   42  42  PRO PRO E . n 
E 2 9   PHE 9   43  43  PHE PHE E . n 
E 2 10  ASN 10  44  44  ASN ASN E . n 
E 2 11  VAL 11  45  45  VAL VAL E . n 
E 2 12  ALA 12  46  46  ALA ALA E . n 
E 2 13  GLU 13  47  47  GLU GLU E . n 
E 2 14  GLY 14  48  48  GLY GLY E . n 
E 2 15  LYS 15  49  49  LYS LYS E . n 
E 2 16  GLU 16  50  50  GLU GLU E . n 
E 2 17  VAL 17  51  51  VAL VAL E . n 
E 2 18  LEU 18  52  52  LEU LEU E . n 
E 2 19  LEU 19  53  53  LEU LEU E . n 
E 2 20  LEU 20  54  54  LEU LEU E . n 
E 2 21  VAL 21  55  55  VAL VAL E . n 
E 2 22  HIS 22  56  56  HIS HIS E . n 
E 2 23  ASN 23  57  57  ASN ASN E . n 
E 2 24  LEU 24  58  58  LEU LEU E . n 
E 2 25  PRO 25  59  59  PRO PRO E . n 
E 2 26  GLN 26  60  60  GLN GLN E . n 
E 2 27  GLN 27  61  61  GLN GLN E . n 
E 2 28  LEU 28  62  62  LEU LEU E . n 
E 2 29  PHE 29  63  63  PHE PHE E . n 
E 2 30  GLY 30  64  64  GLY GLY E . n 
E 2 31  TYR 31  65  65  TYR TYR E . n 
E 2 32  SER 32  66  66  SER SER E . n 
E 2 33  TRP 33  67  67  TRP TRP E . n 
E 2 34  TYR 34  68  68  TYR TYR E . n 
E 2 35  LYS 35  69  69  LYS LYS E . n 
E 2 36  GLY 36  70  70  GLY GLY E . n 
E 2 37  GLU 37  71  71  GLU GLU E . n 
E 2 38  ARG 38  72  72  ARG ARG E . n 
E 2 39  VAL 39  73  73  VAL VAL E . n 
E 2 40  ASP 40  74  74  ASP ASP E . n 
E 2 41  GLY 41  75  75  GLY GLY E . n 
E 2 42  ASN 42  76  76  ASN ASN E . n 
E 2 43  ARG 43  77  77  ARG ARG E . n 
E 2 44  GLN 44  78  78  GLN GLN E . n 
E 2 45  ILE 45  79  79  ILE ILE E . n 
E 2 46  VAL 46  80  80  VAL VAL E . n 
E 2 47  GLY 47  81  81  GLY GLY E . n 
E 2 48  TYR 48  82  82  TYR TYR E . n 
E 2 49  ALA 49  83  83  ALA ALA E . n 
E 2 50  ILE 50  84  84  ILE ILE E . n 
E 2 51  GLY 51  85  85  GLY GLY E . n 
E 2 52  THR 52  86  86  THR THR E . n 
E 2 53  GLN 53  87  87  GLN GLN E . n 
E 2 54  GLN 54  88  88  GLN GLN E . n 
E 2 55  ALA 55  89  89  ALA ALA E . n 
E 2 56  THR 56  90  90  THR THR E . n 
E 2 57  PRO 57  91  91  PRO PRO E . n 
E 2 58  GLY 58  92  92  GLY GLY E . n 
E 2 59  PRO 59  93  93  PRO PRO E . n 
E 2 60  ALA 60  94  94  ALA ALA E . n 
E 2 61  ASN 61  95  95  ASN ASN E . n 
E 2 62  SER 62  96  96  SER SER E . n 
E 2 63  GLY 63  97  97  GLY GLY E . n 
E 2 64  ARG 64  98  98  ARG ARG E . n 
E 2 65  GLU 65  99  99  GLU GLU E . n 
E 2 66  THR 66  100 100 THR THR E . n 
E 2 67  ILE 67  101 101 ILE ILE E . n 
E 2 68  TYR 68  102 102 TYR TYR E . n 
E 2 69  PRO 69  103 103 PRO PRO E . n 
E 2 70  ASN 70  104 104 ASN ASN E . n 
E 2 71  ALA 71  105 105 ALA ALA E . n 
E 2 72  SER 72  106 106 SER SER E . n 
E 2 73  LEU 73  107 107 LEU LEU E . n 
E 2 74  LEU 74  108 108 LEU LEU E . n 
E 2 75  ILE 75  109 109 ILE ILE E . n 
E 2 76  GLN 76  110 110 GLN GLN E . n 
E 2 77  ASN 77  111 111 ASN ASN E . n 
E 2 78  VAL 78  112 112 VAL VAL E . n 
E 2 79  THR 79  113 113 THR THR E . n 
E 2 80  GLN 80  114 114 GLN GLN E . n 
E 2 81  ASN 81  115 115 ASN ASN E . n 
E 2 82  ASP 82  116 116 ASP ASP E . n 
E 2 83  THR 83  117 117 THR THR E . n 
E 2 84  GLY 84  118 118 GLY GLY E . n 
E 2 85  PHE 85  119 119 PHE PHE E . n 
E 2 86  TYR 86  120 120 TYR TYR E . n 
E 2 87  THR 87  121 121 THR THR E . n 
E 2 88  LEU 88  122 122 LEU LEU E . n 
E 2 89  GLN 89  123 123 GLN GLN E . n 
E 2 90  VAL 90  124 124 VAL VAL E . n 
E 2 91  ILE 91  125 125 ILE ILE E . n 
E 2 92  LYS 92  126 126 LYS LYS E . n 
E 2 93  SER 93  127 127 SER SER E . n 
E 2 94  ASP 94  128 128 ASP ASP E . n 
E 2 95  LEU 95  129 129 LEU LEU E . n 
E 2 96  VAL 96  130 130 VAL VAL E . n 
E 2 97  ASN 97  131 131 ASN ASN E . n 
E 2 98  GLU 98  132 132 GLU GLU E . n 
E 2 99  GLU 99  133 133 GLU GLU E . n 
E 2 100 ALA 100 134 134 ALA ALA E . n 
E 2 101 THR 101 135 135 THR THR E . n 
E 2 102 GLY 102 136 136 GLY GLY E . n 
E 2 103 GLN 103 137 137 GLN GLN E . n 
E 2 104 PHE 104 138 138 PHE PHE E . n 
E 2 105 HIS 105 139 139 HIS HIS E . n 
E 2 106 VAL 106 140 140 VAL VAL E . n 
E 2 107 TYR 107 141 141 TYR TYR E . n 
E 2 108 PRO 108 142 142 PRO PRO E . n 
E 2 109 GLU 109 143 143 GLU GLU E . n 
E 2 110 LEU 110 144 144 LEU LEU E . n 
E 2 111 PRO 111 145 145 PRO PRO E . n 
E 2 112 LYS 112 146 146 LYS LYS E . n 
E 2 113 PRO 113 147 147 PRO PRO E . n 
E 2 114 SER 114 148 148 SER SER E . n 
E 2 115 ILE 115 149 149 ILE ILE E . n 
E 2 116 SER 116 150 150 SER SER E . n 
E 2 117 SER 117 151 151 SER SER E . n 
E 2 118 ASN 118 152 152 ASN ASN E . n 
E 2 119 ASN 119 153 153 ASN ASN E . n 
E 2 120 SER 120 154 154 SER SER E . n 
E 2 121 ASN 121 155 155 ASN ASN E . n 
E 2 122 PRO 122 156 156 PRO PRO E . n 
E 2 123 VAL 123 157 157 VAL VAL E . n 
E 2 124 GLU 124 158 158 GLU GLU E . n 
E 2 125 ASP 125 159 159 ASP ASP E . n 
E 2 126 LYS 126 160 160 LYS LYS E . n 
E 2 127 ASP 127 161 161 ASP ASP E . n 
E 2 128 ALA 128 162 162 ALA ALA E . n 
E 2 129 VAL 129 163 163 VAL VAL E . n 
E 2 130 ALA 130 164 164 ALA ALA E . n 
E 2 131 PHE 131 165 165 PHE PHE E . n 
E 2 132 THR 132 166 166 THR THR E . n 
E 2 133 CYS 133 167 167 CYS CYS E . n 
E 2 134 GLU 134 168 168 GLU GLU E . n 
E 2 135 PRO 135 169 169 PRO PRO E . n 
E 2 136 GLU 136 170 170 GLU GLU E . n 
E 2 137 THR 137 171 171 THR THR E . n 
E 2 138 GLN 138 172 172 GLN GLN E . n 
E 2 139 ASP 139 173 173 ASP ASP E . n 
E 2 140 THR 140 174 174 THR THR E . n 
E 2 141 THR 141 175 175 THR THR E . n 
E 2 142 TYR 142 176 176 TYR TYR E . n 
E 2 143 LEU 143 177 177 LEU LEU E . n 
E 2 144 TRP 144 178 178 TRP TRP E . n 
E 2 145 TRP 145 179 179 TRP TRP E . n 
E 2 146 ILE 146 180 180 ILE ILE E . n 
E 2 147 ASN 147 181 181 ASN ASN E . n 
E 2 148 ASN 148 182 182 ASN ASN E . n 
E 2 149 GLN 149 183 183 GLN GLN E . n 
E 2 150 SER 150 184 184 SER SER E . n 
E 2 151 LEU 151 185 185 LEU LEU E . n 
E 2 152 PRO 152 186 186 PRO PRO E . n 
E 2 153 VAL 153 187 187 VAL VAL E . n 
E 2 154 SER 154 188 188 SER SER E . n 
E 2 155 PRO 155 189 189 PRO PRO E . n 
E 2 156 ARG 156 190 190 ARG ARG E . n 
E 2 157 LEU 157 191 191 LEU LEU E . n 
E 2 158 GLN 158 192 192 GLN GLN E . n 
E 2 159 LEU 159 193 193 LEU LEU E . n 
E 2 160 SER 160 194 194 SER SER E . n 
E 2 161 ASN 161 195 195 ASN ASN E . n 
E 2 162 GLY 162 196 196 GLY GLY E . n 
E 2 163 ASN 163 197 197 ASN ASN E . n 
E 2 164 ARG 164 198 198 ARG ARG E . n 
E 2 165 THR 165 199 199 THR THR E . n 
E 2 166 LEU 166 200 200 LEU LEU E . n 
E 2 167 THR 167 201 201 THR THR E . n 
E 2 168 LEU 168 202 202 LEU LEU E . n 
E 2 169 LEU 169 203 203 LEU LEU E . n 
E 2 170 SER 170 204 204 SER SER E . n 
E 2 171 VAL 171 205 205 VAL VAL E . n 
E 2 172 THR 172 206 206 THR THR E . n 
E 2 173 ARG 173 207 207 ARG ARG E . n 
E 2 174 ASN 174 208 208 ASN ASN E . n 
E 2 175 ASP 175 209 209 ASP ASP E . n 
E 2 176 THR 176 210 210 THR THR E . n 
E 2 177 GLY 177 211 211 GLY GLY E . n 
E 2 178 PRO 178 212 212 PRO PRO E . n 
E 2 179 TYR 179 213 213 TYR TYR E . n 
E 2 180 GLU 180 214 214 GLU GLU E . n 
E 2 181 CYS 181 215 215 CYS CYS E . n 
E 2 182 GLU 182 216 216 GLU GLU E . n 
E 2 183 ILE 183 217 217 ILE ILE E . n 
E 2 184 GLN 184 218 218 GLN GLN E . n 
E 2 185 ASN 185 219 219 ASN ASN E . n 
E 2 186 PRO 186 220 220 PRO PRO E . n 
E 2 187 VAL 187 221 221 VAL VAL E . n 
E 2 188 SER 188 222 222 SER SER E . n 
E 2 189 ALA 189 223 223 ALA ALA E . n 
E 2 190 ASN 190 224 224 ASN ASN E . n 
E 2 191 ARG 191 225 225 ARG ARG E . n 
E 2 192 SER 192 226 226 SER SER E . n 
E 2 193 ASP 193 227 227 ASP ASP E . n 
E 2 194 PRO 194 228 228 PRO PRO E . n 
E 2 195 VAL 195 229 229 VAL VAL E . n 
E 2 196 THR 196 230 230 THR THR E . n 
E 2 197 LEU 197 231 231 LEU LEU E . n 
E 2 198 ASN 198 232 232 ASN ASN E . n 
E 2 199 VAL 199 233 233 VAL VAL E . n 
E 2 200 THR 200 234 234 THR THR E . n 
E 2 201 TYR 201 235 ?   ?   ?   E . n 
E 2 202 GLY 202 236 ?   ?   ?   E . n 
E 2 203 PRO 203 237 ?   ?   ?   E . n 
E 2 204 ASP 204 238 ?   ?   ?   E . n 
E 2 205 THR 205 239 ?   ?   ?   E . n 
E 2 206 PRO 206 240 ?   ?   ?   E . n 
E 2 207 THR 207 241 ?   ?   ?   E . n 
E 2 208 ILE 208 242 ?   ?   ?   E . n 
E 2 209 SER 209 243 ?   ?   ?   E . n 
E 2 210 PRO 210 244 ?   ?   ?   E . n 
E 2 211 SER 211 245 ?   ?   ?   E . n 
E 2 212 ASP 212 246 ?   ?   ?   E . n 
E 2 213 THR 213 247 ?   ?   ?   E . n 
E 2 214 TYR 214 248 ?   ?   ?   E . n 
E 2 215 TYR 215 249 ?   ?   ?   E . n 
E 2 216 ARG 216 250 ?   ?   ?   E . n 
E 2 217 PRO 217 251 ?   ?   ?   E . n 
E 2 218 GLY 218 252 ?   ?   ?   E . n 
E 2 219 ALA 219 253 ?   ?   ?   E . n 
E 2 220 ASN 220 254 ?   ?   ?   E . n 
E 2 221 LEU 221 255 ?   ?   ?   E . n 
E 2 222 SER 222 256 ?   ?   ?   E . n 
E 2 223 LEU 223 257 ?   ?   ?   E . n 
E 2 224 SER 224 258 ?   ?   ?   E . n 
E 2 225 CYS 225 259 ?   ?   ?   E . n 
E 2 226 TYR 226 260 ?   ?   ?   E . n 
E 2 227 ALA 227 261 ?   ?   ?   E . n 
E 2 228 ALA 228 262 ?   ?   ?   E . n 
E 2 229 SER 229 263 ?   ?   ?   E . n 
E 2 230 ASN 230 264 ?   ?   ?   E . n 
E 2 231 PRO 231 265 ?   ?   ?   E . n 
E 2 232 PRO 232 266 ?   ?   ?   E . n 
E 2 233 ALA 233 267 ?   ?   ?   E . n 
E 2 234 GLN 234 268 ?   ?   ?   E . n 
E 2 235 TYR 235 269 ?   ?   ?   E . n 
E 2 236 SER 236 270 ?   ?   ?   E . n 
E 2 237 TRP 237 271 ?   ?   ?   E . n 
E 2 238 LEU 238 272 ?   ?   ?   E . n 
E 2 239 ILE 239 273 ?   ?   ?   E . n 
E 2 240 ASN 240 274 ?   ?   ?   E . n 
E 2 241 GLY 241 275 ?   ?   ?   E . n 
E 2 242 THR 242 276 ?   ?   ?   E . n 
E 2 243 PHE 243 277 ?   ?   ?   E . n 
E 2 244 GLN 244 278 ?   ?   ?   E . n 
E 2 245 GLN 245 279 ?   ?   ?   E . n 
E 2 246 SER 246 280 ?   ?   ?   E . n 
E 2 247 THR 247 281 ?   ?   ?   E . n 
E 2 248 GLN 248 282 ?   ?   ?   E . n 
E 2 249 GLU 249 283 ?   ?   ?   E . n 
E 2 250 LEU 250 284 ?   ?   ?   E . n 
E 2 251 PHE 251 285 ?   ?   ?   E . n 
E 2 252 ILE 252 286 ?   ?   ?   E . n 
E 2 253 PRO 253 287 ?   ?   ?   E . n 
E 2 254 ASN 254 288 ?   ?   ?   E . n 
E 2 255 ILE 255 289 ?   ?   ?   E . n 
E 2 256 THR 256 290 ?   ?   ?   E . n 
E 2 257 VAL 257 291 ?   ?   ?   E . n 
E 2 258 ASN 258 292 ?   ?   ?   E . n 
E 2 259 ASN 259 293 ?   ?   ?   E . n 
E 2 260 SER 260 294 ?   ?   ?   E . n 
E 2 261 GLY 261 295 ?   ?   ?   E . n 
E 2 262 SER 262 296 ?   ?   ?   E . n 
E 2 263 TYR 263 297 ?   ?   ?   E . n 
E 2 264 THR 264 298 ?   ?   ?   E . n 
E 2 265 CYS 265 299 ?   ?   ?   E . n 
E 2 266 HIS 266 300 ?   ?   ?   E . n 
E 2 267 ALA 267 301 ?   ?   ?   E . n 
E 2 268 ASN 268 302 ?   ?   ?   E . n 
E 2 269 ASN 269 303 ?   ?   ?   E . n 
E 2 270 SER 270 304 ?   ?   ?   E . n 
E 2 271 VAL 271 305 ?   ?   ?   E . n 
E 2 272 THR 272 306 ?   ?   ?   E . n 
E 2 273 GLY 273 307 ?   ?   ?   E . n 
E 2 274 CYS 274 308 ?   ?   ?   E . n 
E 2 275 ASN 275 309 ?   ?   ?   E . n 
E 2 276 ARG 276 310 ?   ?   ?   E . n 
E 2 277 THR 277 311 ?   ?   ?   E . n 
E 2 278 THR 278 312 ?   ?   ?   E . n 
E 2 279 VAL 279 313 ?   ?   ?   E . n 
E 2 280 LYS 280 314 ?   ?   ?   E . n 
E 2 281 THR 281 315 ?   ?   ?   E . n 
E 2 282 ILE 282 316 ?   ?   ?   E . n 
E 2 283 ILE 283 317 ?   ?   ?   E . n 
E 2 284 VAL 284 318 ?   ?   ?   E . n 
E 2 285 THR 285 319 ?   ?   ?   E . n 
E 2 286 GLU 286 320 ?   ?   ?   E . n 
E 2 287 LEU 287 321 ?   ?   ?   E . n 
E 2 288 SER 288 322 ?   ?   ?   E . n 
E 2 289 PRO 289 323 ?   ?   ?   E . n 
E 2 290 VAL 290 324 ?   ?   ?   E . n 
E 2 291 VAL 291 325 ?   ?   ?   E . n 
E 2 292 ALA 292 326 ?   ?   ?   E . n 
E 2 293 LYS 293 327 ?   ?   ?   E . n 
E 2 294 PRO 294 328 ?   ?   ?   E . n 
E 2 295 GLN 295 329 ?   ?   ?   E . n 
E 2 296 ILE 296 330 ?   ?   ?   E . n 
E 2 297 LYS 297 331 ?   ?   ?   E . n 
E 2 298 ALA 298 332 ?   ?   ?   E . n 
E 2 299 SER 299 333 ?   ?   ?   E . n 
E 2 300 LYS 300 334 ?   ?   ?   E . n 
E 2 301 THR 301 335 ?   ?   ?   E . n 
E 2 302 THR 302 336 ?   ?   ?   E . n 
E 2 303 VAL 303 337 ?   ?   ?   E . n 
E 2 304 THR 304 338 ?   ?   ?   E . n 
E 2 305 GLY 305 339 ?   ?   ?   E . n 
E 2 306 ASP 306 340 ?   ?   ?   E . n 
E 2 307 LYS 307 341 ?   ?   ?   E . n 
E 2 308 ASP 308 342 ?   ?   ?   E . n 
E 2 309 SER 309 343 ?   ?   ?   E . n 
E 2 310 VAL 310 344 ?   ?   ?   E . n 
E 2 311 ASN 311 345 ?   ?   ?   E . n 
E 2 312 LEU 312 346 ?   ?   ?   E . n 
E 2 313 THR 313 347 ?   ?   ?   E . n 
E 2 314 CYS 314 348 ?   ?   ?   E . n 
E 2 315 SER 315 349 ?   ?   ?   E . n 
E 2 316 THR 316 350 ?   ?   ?   E . n 
E 2 317 ASN 317 351 ?   ?   ?   E . n 
E 2 318 ASP 318 352 ?   ?   ?   E . n 
E 2 319 THR 319 353 ?   ?   ?   E . n 
E 2 320 GLY 320 354 ?   ?   ?   E . n 
E 2 321 ILE 321 355 ?   ?   ?   E . n 
E 2 322 SER 322 356 ?   ?   ?   E . n 
E 2 323 ILE 323 357 ?   ?   ?   E . n 
E 2 324 ARG 324 358 ?   ?   ?   E . n 
E 2 325 TRP 325 359 ?   ?   ?   E . n 
E 2 326 PHE 326 360 ?   ?   ?   E . n 
E 2 327 PHE 327 361 ?   ?   ?   E . n 
E 2 328 LYS 328 362 ?   ?   ?   E . n 
E 2 329 ASN 329 363 ?   ?   ?   E . n 
E 2 330 GLN 330 364 ?   ?   ?   E . n 
E 2 331 SER 331 365 ?   ?   ?   E . n 
E 2 332 LEU 332 366 ?   ?   ?   E . n 
E 2 333 PRO 333 367 ?   ?   ?   E . n 
E 2 334 SER 334 368 ?   ?   ?   E . n 
E 2 335 SER 335 369 ?   ?   ?   E . n 
E 2 336 GLU 336 370 ?   ?   ?   E . n 
E 2 337 ARG 337 371 ?   ?   ?   E . n 
E 2 338 MET 338 372 ?   ?   ?   E . n 
E 2 339 LYS 339 373 ?   ?   ?   E . n 
E 2 340 LEU 340 374 ?   ?   ?   E . n 
E 2 341 SER 341 375 ?   ?   ?   E . n 
E 2 342 GLN 342 376 ?   ?   ?   E . n 
E 2 343 GLY 343 377 ?   ?   ?   E . n 
E 2 344 ASN 344 378 ?   ?   ?   E . n 
E 2 345 THR 345 379 ?   ?   ?   E . n 
E 2 346 THR 346 380 ?   ?   ?   E . n 
E 2 347 LEU 347 381 ?   ?   ?   E . n 
E 2 348 SER 348 382 ?   ?   ?   E . n 
E 2 349 ILE 349 383 ?   ?   ?   E . n 
E 2 350 ASN 350 384 ?   ?   ?   E . n 
E 2 351 PRO 351 385 ?   ?   ?   E . n 
E 2 352 VAL 352 386 ?   ?   ?   E . n 
E 2 353 LYS 353 387 ?   ?   ?   E . n 
E 2 354 ARG 354 388 ?   ?   ?   E . n 
E 2 355 GLU 355 389 ?   ?   ?   E . n 
E 2 356 ASP 356 390 ?   ?   ?   E . n 
E 2 357 ALA 357 391 ?   ?   ?   E . n 
E 2 358 GLY 358 392 ?   ?   ?   E . n 
E 2 359 THR 359 393 ?   ?   ?   E . n 
E 2 360 TYR 360 394 ?   ?   ?   E . n 
E 2 361 TRP 361 395 ?   ?   ?   E . n 
E 2 362 CYS 362 396 ?   ?   ?   E . n 
E 2 363 GLU 363 397 ?   ?   ?   E . n 
E 2 364 VAL 364 398 ?   ?   ?   E . n 
E 2 365 PHE 365 399 ?   ?   ?   E . n 
E 2 366 ASN 366 400 ?   ?   ?   E . n 
E 2 367 PRO 367 401 ?   ?   ?   E . n 
E 2 368 ILE 368 402 ?   ?   ?   E . n 
E 2 369 SER 369 403 ?   ?   ?   E . n 
E 2 370 LYS 370 404 ?   ?   ?   E . n 
E 2 371 ASN 371 405 ?   ?   ?   E . n 
E 2 372 GLN 372 406 ?   ?   ?   E . n 
E 2 373 SER 373 407 ?   ?   ?   E . n 
E 2 374 ASP 374 408 ?   ?   ?   E . n 
E 2 375 PRO 375 409 ?   ?   ?   E . n 
E 2 376 ILE 376 410 ?   ?   ?   E . n 
E 2 377 MET 377 411 ?   ?   ?   E . n 
E 2 378 LEU 378 412 ?   ?   ?   E . n 
E 2 379 ASN 379 413 ?   ?   ?   E . n 
E 2 380 VAL 380 414 ?   ?   ?   E . n 
E 2 381 ASN 381 415 ?   ?   ?   E . n 
E 2 382 TYR 382 416 ?   ?   ?   E . n 
E 2 383 ASN 383 417 ?   ?   ?   E . n 
E 2 384 ALA 384 418 ?   ?   ?   E . n 
E 2 385 LEU 385 419 ?   ?   ?   E . n 
E 2 386 PRO 386 420 ?   ?   ?   E . n 
E 2 387 GLN 387 421 ?   ?   ?   E . n 
E 2 388 GLU 388 422 ?   ?   ?   E . n 
E 2 389 ASN 389 423 ?   ?   ?   E . n 
E 2 390 GLY 390 424 ?   ?   ?   E . n 
E 2 391 LEU 391 425 ?   ?   ?   E . n 
E 2 392 SER 392 426 ?   ?   ?   E . n 
E 2 393 PRO 393 427 ?   ?   ?   E . n 
E 2 394 GLY 394 428 ?   ?   ?   E . n 
E 2 395 HIS 395 429 ?   ?   ?   E . n 
E 2 396 HIS 396 430 ?   ?   ?   E . n 
E 2 397 HIS 397 431 ?   ?   ?   E . n 
E 2 398 HIS 398 432 ?   ?   ?   E . n 
E 2 399 HIS 399 433 ?   ?   ?   E . n 
E 2 400 HIS 400 434 ?   ?   ?   E . n 
F 2 1   GLN 1   35  35  GLN GLN F . n 
F 2 2   LEU 2   36  36  LEU LEU F . n 
F 2 3   THR 3   37  37  THR THR F . n 
F 2 4   THR 4   38  38  THR THR F . n 
F 2 5   GLU 5   39  39  GLU GLU F . n 
F 2 6   SER 6   40  40  SER SER F . n 
F 2 7   MET 7   41  41  MET MET F . n 
F 2 8   PRO 8   42  42  PRO PRO F . n 
F 2 9   PHE 9   43  43  PHE PHE F . n 
F 2 10  ASN 10  44  44  ASN ASN F . n 
F 2 11  VAL 11  45  45  VAL VAL F . n 
F 2 12  ALA 12  46  46  ALA ALA F . n 
F 2 13  GLU 13  47  47  GLU GLU F . n 
F 2 14  GLY 14  48  48  GLY GLY F . n 
F 2 15  LYS 15  49  49  LYS LYS F . n 
F 2 16  GLU 16  50  50  GLU GLU F . n 
F 2 17  VAL 17  51  51  VAL VAL F . n 
F 2 18  LEU 18  52  52  LEU LEU F . n 
F 2 19  LEU 19  53  53  LEU LEU F . n 
F 2 20  LEU 20  54  54  LEU LEU F . n 
F 2 21  VAL 21  55  55  VAL VAL F . n 
F 2 22  HIS 22  56  56  HIS HIS F . n 
F 2 23  ASN 23  57  57  ASN ASN F . n 
F 2 24  LEU 24  58  58  LEU LEU F . n 
F 2 25  PRO 25  59  59  PRO PRO F . n 
F 2 26  GLN 26  60  60  GLN GLN F . n 
F 2 27  GLN 27  61  61  GLN GLN F . n 
F 2 28  LEU 28  62  62  LEU LEU F . n 
F 2 29  PHE 29  63  63  PHE PHE F . n 
F 2 30  GLY 30  64  64  GLY GLY F . n 
F 2 31  TYR 31  65  65  TYR TYR F . n 
F 2 32  SER 32  66  66  SER SER F . n 
F 2 33  TRP 33  67  67  TRP TRP F . n 
F 2 34  TYR 34  68  68  TYR TYR F . n 
F 2 35  LYS 35  69  69  LYS LYS F . n 
F 2 36  GLY 36  70  70  GLY GLY F . n 
F 2 37  GLU 37  71  71  GLU GLU F . n 
F 2 38  ARG 38  72  72  ARG ARG F . n 
F 2 39  VAL 39  73  73  VAL VAL F . n 
F 2 40  ASP 40  74  74  ASP ASP F . n 
F 2 41  GLY 41  75  75  GLY GLY F . n 
F 2 42  ASN 42  76  76  ASN ASN F . n 
F 2 43  ARG 43  77  77  ARG ARG F . n 
F 2 44  GLN 44  78  78  GLN GLN F . n 
F 2 45  ILE 45  79  79  ILE ILE F . n 
F 2 46  VAL 46  80  80  VAL VAL F . n 
F 2 47  GLY 47  81  81  GLY GLY F . n 
F 2 48  TYR 48  82  82  TYR TYR F . n 
F 2 49  ALA 49  83  83  ALA ALA F . n 
F 2 50  ILE 50  84  84  ILE ILE F . n 
F 2 51  GLY 51  85  85  GLY GLY F . n 
F 2 52  THR 52  86  86  THR THR F . n 
F 2 53  GLN 53  87  87  GLN GLN F . n 
F 2 54  GLN 54  88  88  GLN GLN F . n 
F 2 55  ALA 55  89  89  ALA ALA F . n 
F 2 56  THR 56  90  90  THR THR F . n 
F 2 57  PRO 57  91  91  PRO PRO F . n 
F 2 58  GLY 58  92  92  GLY GLY F . n 
F 2 59  PRO 59  93  93  PRO PRO F . n 
F 2 60  ALA 60  94  94  ALA ALA F . n 
F 2 61  ASN 61  95  95  ASN ASN F . n 
F 2 62  SER 62  96  96  SER SER F . n 
F 2 63  GLY 63  97  97  GLY GLY F . n 
F 2 64  ARG 64  98  98  ARG ARG F . n 
F 2 65  GLU 65  99  99  GLU GLU F . n 
F 2 66  THR 66  100 100 THR THR F . n 
F 2 67  ILE 67  101 101 ILE ILE F . n 
F 2 68  TYR 68  102 102 TYR TYR F . n 
F 2 69  PRO 69  103 103 PRO PRO F . n 
F 2 70  ASN 70  104 104 ASN ASN F . n 
F 2 71  ALA 71  105 105 ALA ALA F . n 
F 2 72  SER 72  106 106 SER SER F . n 
F 2 73  LEU 73  107 107 LEU LEU F . n 
F 2 74  LEU 74  108 108 LEU LEU F . n 
F 2 75  ILE 75  109 109 ILE ILE F . n 
F 2 76  GLN 76  110 110 GLN GLN F . n 
F 2 77  ASN 77  111 111 ASN ASN F . n 
F 2 78  VAL 78  112 112 VAL VAL F . n 
F 2 79  THR 79  113 113 THR THR F . n 
F 2 80  GLN 80  114 114 GLN GLN F . n 
F 2 81  ASN 81  115 115 ASN ASN F . n 
F 2 82  ASP 82  116 116 ASP ASP F . n 
F 2 83  THR 83  117 117 THR THR F . n 
F 2 84  GLY 84  118 118 GLY GLY F . n 
F 2 85  PHE 85  119 119 PHE PHE F . n 
F 2 86  TYR 86  120 120 TYR TYR F . n 
F 2 87  THR 87  121 121 THR THR F . n 
F 2 88  LEU 88  122 122 LEU LEU F . n 
F 2 89  GLN 89  123 123 GLN GLN F . n 
F 2 90  VAL 90  124 124 VAL VAL F . n 
F 2 91  ILE 91  125 125 ILE ILE F . n 
F 2 92  LYS 92  126 126 LYS LYS F . n 
F 2 93  SER 93  127 127 SER SER F . n 
F 2 94  ASP 94  128 128 ASP ASP F . n 
F 2 95  LEU 95  129 129 LEU LEU F . n 
F 2 96  VAL 96  130 130 VAL VAL F . n 
F 2 97  ASN 97  131 131 ASN ASN F . n 
F 2 98  GLU 98  132 132 GLU GLU F . n 
F 2 99  GLU 99  133 133 GLU GLU F . n 
F 2 100 ALA 100 134 134 ALA ALA F . n 
F 2 101 THR 101 135 135 THR THR F . n 
F 2 102 GLY 102 136 136 GLY GLY F . n 
F 2 103 GLN 103 137 137 GLN GLN F . n 
F 2 104 PHE 104 138 138 PHE PHE F . n 
F 2 105 HIS 105 139 139 HIS HIS F . n 
F 2 106 VAL 106 140 140 VAL VAL F . n 
F 2 107 TYR 107 141 141 TYR TYR F . n 
F 2 108 PRO 108 142 142 PRO PRO F . n 
F 2 109 GLU 109 143 143 GLU GLU F . n 
F 2 110 LEU 110 144 144 LEU LEU F . n 
F 2 111 PRO 111 145 145 PRO PRO F . n 
F 2 112 LYS 112 146 146 LYS LYS F . n 
F 2 113 PRO 113 147 147 PRO PRO F . n 
F 2 114 SER 114 148 148 SER SER F . n 
F 2 115 ILE 115 149 149 ILE ILE F . n 
F 2 116 SER 116 150 150 SER SER F . n 
F 2 117 SER 117 151 151 SER SER F . n 
F 2 118 ASN 118 152 152 ASN ASN F . n 
F 2 119 ASN 119 153 153 ASN ASN F . n 
F 2 120 SER 120 154 154 SER SER F . n 
F 2 121 ASN 121 155 155 ASN ASN F . n 
F 2 122 PRO 122 156 156 PRO PRO F . n 
F 2 123 VAL 123 157 157 VAL VAL F . n 
F 2 124 GLU 124 158 158 GLU GLU F . n 
F 2 125 ASP 125 159 159 ASP ASP F . n 
F 2 126 LYS 126 160 160 LYS LYS F . n 
F 2 127 ASP 127 161 161 ASP ASP F . n 
F 2 128 ALA 128 162 162 ALA ALA F . n 
F 2 129 VAL 129 163 163 VAL VAL F . n 
F 2 130 ALA 130 164 164 ALA ALA F . n 
F 2 131 PHE 131 165 165 PHE PHE F . n 
F 2 132 THR 132 166 166 THR THR F . n 
F 2 133 CYS 133 167 167 CYS CYS F . n 
F 2 134 GLU 134 168 168 GLU GLU F . n 
F 2 135 PRO 135 169 169 PRO PRO F . n 
F 2 136 GLU 136 170 170 GLU GLU F . n 
F 2 137 THR 137 171 171 THR THR F . n 
F 2 138 GLN 138 172 172 GLN GLN F . n 
F 2 139 ASP 139 173 173 ASP ASP F . n 
F 2 140 THR 140 174 174 THR THR F . n 
F 2 141 THR 141 175 175 THR THR F . n 
F 2 142 TYR 142 176 176 TYR TYR F . n 
F 2 143 LEU 143 177 177 LEU LEU F . n 
F 2 144 TRP 144 178 178 TRP TRP F . n 
F 2 145 TRP 145 179 179 TRP TRP F . n 
F 2 146 ILE 146 180 180 ILE ILE F . n 
F 2 147 ASN 147 181 181 ASN ASN F . n 
F 2 148 ASN 148 182 182 ASN ASN F . n 
F 2 149 GLN 149 183 183 GLN GLN F . n 
F 2 150 SER 150 184 184 SER SER F . n 
F 2 151 LEU 151 185 185 LEU LEU F . n 
F 2 152 PRO 152 186 186 PRO PRO F . n 
F 2 153 VAL 153 187 187 VAL VAL F . n 
F 2 154 SER 154 188 188 SER SER F . n 
F 2 155 PRO 155 189 189 PRO PRO F . n 
F 2 156 ARG 156 190 190 ARG ARG F . n 
F 2 157 LEU 157 191 191 LEU LEU F . n 
F 2 158 GLN 158 192 192 GLN GLN F . n 
F 2 159 LEU 159 193 193 LEU LEU F . n 
F 2 160 SER 160 194 194 SER SER F . n 
F 2 161 ASN 161 195 195 ASN ASN F . n 
F 2 162 GLY 162 196 196 GLY GLY F . n 
F 2 163 ASN 163 197 197 ASN ASN F . n 
F 2 164 ARG 164 198 198 ARG ARG F . n 
F 2 165 THR 165 199 199 THR THR F . n 
F 2 166 LEU 166 200 200 LEU LEU F . n 
F 2 167 THR 167 201 201 THR THR F . n 
F 2 168 LEU 168 202 202 LEU LEU F . n 
F 2 169 LEU 169 203 203 LEU LEU F . n 
F 2 170 SER 170 204 204 SER SER F . n 
F 2 171 VAL 171 205 205 VAL VAL F . n 
F 2 172 THR 172 206 206 THR THR F . n 
F 2 173 ARG 173 207 207 ARG ARG F . n 
F 2 174 ASN 174 208 208 ASN ASN F . n 
F 2 175 ASP 175 209 209 ASP ASP F . n 
F 2 176 THR 176 210 210 THR THR F . n 
F 2 177 GLY 177 211 211 GLY GLY F . n 
F 2 178 PRO 178 212 212 PRO PRO F . n 
F 2 179 TYR 179 213 213 TYR TYR F . n 
F 2 180 GLU 180 214 214 GLU GLU F . n 
F 2 181 CYS 181 215 215 CYS CYS F . n 
F 2 182 GLU 182 216 216 GLU GLU F . n 
F 2 183 ILE 183 217 217 ILE ILE F . n 
F 2 184 GLN 184 218 218 GLN GLN F . n 
F 2 185 ASN 185 219 219 ASN ASN F . n 
F 2 186 PRO 186 220 220 PRO PRO F . n 
F 2 187 VAL 187 221 221 VAL VAL F . n 
F 2 188 SER 188 222 222 SER SER F . n 
F 2 189 ALA 189 223 223 ALA ALA F . n 
F 2 190 ASN 190 224 224 ASN ASN F . n 
F 2 191 ARG 191 225 225 ARG ARG F . n 
F 2 192 SER 192 226 226 SER SER F . n 
F 2 193 ASP 193 227 227 ASP ASP F . n 
F 2 194 PRO 194 228 228 PRO PRO F . n 
F 2 195 VAL 195 229 229 VAL VAL F . n 
F 2 196 THR 196 230 230 THR THR F . n 
F 2 197 LEU 197 231 231 LEU LEU F . n 
F 2 198 ASN 198 232 232 ASN ASN F . n 
F 2 199 VAL 199 233 233 VAL VAL F . n 
F 2 200 THR 200 234 234 THR THR F . n 
F 2 201 TYR 201 235 ?   ?   ?   F . n 
F 2 202 GLY 202 236 ?   ?   ?   F . n 
F 2 203 PRO 203 237 ?   ?   ?   F . n 
F 2 204 ASP 204 238 ?   ?   ?   F . n 
F 2 205 THR 205 239 ?   ?   ?   F . n 
F 2 206 PRO 206 240 ?   ?   ?   F . n 
F 2 207 THR 207 241 ?   ?   ?   F . n 
F 2 208 ILE 208 242 ?   ?   ?   F . n 
F 2 209 SER 209 243 ?   ?   ?   F . n 
F 2 210 PRO 210 244 ?   ?   ?   F . n 
F 2 211 SER 211 245 ?   ?   ?   F . n 
F 2 212 ASP 212 246 ?   ?   ?   F . n 
F 2 213 THR 213 247 ?   ?   ?   F . n 
F 2 214 TYR 214 248 ?   ?   ?   F . n 
F 2 215 TYR 215 249 ?   ?   ?   F . n 
F 2 216 ARG 216 250 ?   ?   ?   F . n 
F 2 217 PRO 217 251 ?   ?   ?   F . n 
F 2 218 GLY 218 252 ?   ?   ?   F . n 
F 2 219 ALA 219 253 ?   ?   ?   F . n 
F 2 220 ASN 220 254 ?   ?   ?   F . n 
F 2 221 LEU 221 255 ?   ?   ?   F . n 
F 2 222 SER 222 256 ?   ?   ?   F . n 
F 2 223 LEU 223 257 ?   ?   ?   F . n 
F 2 224 SER 224 258 ?   ?   ?   F . n 
F 2 225 CYS 225 259 ?   ?   ?   F . n 
F 2 226 TYR 226 260 ?   ?   ?   F . n 
F 2 227 ALA 227 261 ?   ?   ?   F . n 
F 2 228 ALA 228 262 ?   ?   ?   F . n 
F 2 229 SER 229 263 ?   ?   ?   F . n 
F 2 230 ASN 230 264 ?   ?   ?   F . n 
F 2 231 PRO 231 265 ?   ?   ?   F . n 
F 2 232 PRO 232 266 ?   ?   ?   F . n 
F 2 233 ALA 233 267 ?   ?   ?   F . n 
F 2 234 GLN 234 268 ?   ?   ?   F . n 
F 2 235 TYR 235 269 ?   ?   ?   F . n 
F 2 236 SER 236 270 ?   ?   ?   F . n 
F 2 237 TRP 237 271 ?   ?   ?   F . n 
F 2 238 LEU 238 272 ?   ?   ?   F . n 
F 2 239 ILE 239 273 ?   ?   ?   F . n 
F 2 240 ASN 240 274 ?   ?   ?   F . n 
F 2 241 GLY 241 275 ?   ?   ?   F . n 
F 2 242 THR 242 276 ?   ?   ?   F . n 
F 2 243 PHE 243 277 ?   ?   ?   F . n 
F 2 244 GLN 244 278 ?   ?   ?   F . n 
F 2 245 GLN 245 279 ?   ?   ?   F . n 
F 2 246 SER 246 280 ?   ?   ?   F . n 
F 2 247 THR 247 281 ?   ?   ?   F . n 
F 2 248 GLN 248 282 ?   ?   ?   F . n 
F 2 249 GLU 249 283 ?   ?   ?   F . n 
F 2 250 LEU 250 284 ?   ?   ?   F . n 
F 2 251 PHE 251 285 ?   ?   ?   F . n 
F 2 252 ILE 252 286 ?   ?   ?   F . n 
F 2 253 PRO 253 287 ?   ?   ?   F . n 
F 2 254 ASN 254 288 ?   ?   ?   F . n 
F 2 255 ILE 255 289 ?   ?   ?   F . n 
F 2 256 THR 256 290 ?   ?   ?   F . n 
F 2 257 VAL 257 291 ?   ?   ?   F . n 
F 2 258 ASN 258 292 ?   ?   ?   F . n 
F 2 259 ASN 259 293 ?   ?   ?   F . n 
F 2 260 SER 260 294 ?   ?   ?   F . n 
F 2 261 GLY 261 295 ?   ?   ?   F . n 
F 2 262 SER 262 296 ?   ?   ?   F . n 
F 2 263 TYR 263 297 ?   ?   ?   F . n 
F 2 264 THR 264 298 ?   ?   ?   F . n 
F 2 265 CYS 265 299 ?   ?   ?   F . n 
F 2 266 HIS 266 300 ?   ?   ?   F . n 
F 2 267 ALA 267 301 ?   ?   ?   F . n 
F 2 268 ASN 268 302 ?   ?   ?   F . n 
F 2 269 ASN 269 303 ?   ?   ?   F . n 
F 2 270 SER 270 304 ?   ?   ?   F . n 
F 2 271 VAL 271 305 ?   ?   ?   F . n 
F 2 272 THR 272 306 ?   ?   ?   F . n 
F 2 273 GLY 273 307 ?   ?   ?   F . n 
F 2 274 CYS 274 308 ?   ?   ?   F . n 
F 2 275 ASN 275 309 ?   ?   ?   F . n 
F 2 276 ARG 276 310 ?   ?   ?   F . n 
F 2 277 THR 277 311 ?   ?   ?   F . n 
F 2 278 THR 278 312 ?   ?   ?   F . n 
F 2 279 VAL 279 313 ?   ?   ?   F . n 
F 2 280 LYS 280 314 ?   ?   ?   F . n 
F 2 281 THR 281 315 ?   ?   ?   F . n 
F 2 282 ILE 282 316 ?   ?   ?   F . n 
F 2 283 ILE 283 317 ?   ?   ?   F . n 
F 2 284 VAL 284 318 ?   ?   ?   F . n 
F 2 285 THR 285 319 ?   ?   ?   F . n 
F 2 286 GLU 286 320 ?   ?   ?   F . n 
F 2 287 LEU 287 321 ?   ?   ?   F . n 
F 2 288 SER 288 322 ?   ?   ?   F . n 
F 2 289 PRO 289 323 ?   ?   ?   F . n 
F 2 290 VAL 290 324 ?   ?   ?   F . n 
F 2 291 VAL 291 325 ?   ?   ?   F . n 
F 2 292 ALA 292 326 ?   ?   ?   F . n 
F 2 293 LYS 293 327 ?   ?   ?   F . n 
F 2 294 PRO 294 328 ?   ?   ?   F . n 
F 2 295 GLN 295 329 ?   ?   ?   F . n 
F 2 296 ILE 296 330 ?   ?   ?   F . n 
F 2 297 LYS 297 331 ?   ?   ?   F . n 
F 2 298 ALA 298 332 ?   ?   ?   F . n 
F 2 299 SER 299 333 ?   ?   ?   F . n 
F 2 300 LYS 300 334 ?   ?   ?   F . n 
F 2 301 THR 301 335 ?   ?   ?   F . n 
F 2 302 THR 302 336 ?   ?   ?   F . n 
F 2 303 VAL 303 337 ?   ?   ?   F . n 
F 2 304 THR 304 338 ?   ?   ?   F . n 
F 2 305 GLY 305 339 ?   ?   ?   F . n 
F 2 306 ASP 306 340 ?   ?   ?   F . n 
F 2 307 LYS 307 341 ?   ?   ?   F . n 
F 2 308 ASP 308 342 ?   ?   ?   F . n 
F 2 309 SER 309 343 ?   ?   ?   F . n 
F 2 310 VAL 310 344 ?   ?   ?   F . n 
F 2 311 ASN 311 345 ?   ?   ?   F . n 
F 2 312 LEU 312 346 ?   ?   ?   F . n 
F 2 313 THR 313 347 ?   ?   ?   F . n 
F 2 314 CYS 314 348 ?   ?   ?   F . n 
F 2 315 SER 315 349 ?   ?   ?   F . n 
F 2 316 THR 316 350 ?   ?   ?   F . n 
F 2 317 ASN 317 351 ?   ?   ?   F . n 
F 2 318 ASP 318 352 ?   ?   ?   F . n 
F 2 319 THR 319 353 ?   ?   ?   F . n 
F 2 320 GLY 320 354 ?   ?   ?   F . n 
F 2 321 ILE 321 355 ?   ?   ?   F . n 
F 2 322 SER 322 356 ?   ?   ?   F . n 
F 2 323 ILE 323 357 ?   ?   ?   F . n 
F 2 324 ARG 324 358 ?   ?   ?   F . n 
F 2 325 TRP 325 359 ?   ?   ?   F . n 
F 2 326 PHE 326 360 ?   ?   ?   F . n 
F 2 327 PHE 327 361 ?   ?   ?   F . n 
F 2 328 LYS 328 362 ?   ?   ?   F . n 
F 2 329 ASN 329 363 ?   ?   ?   F . n 
F 2 330 GLN 330 364 ?   ?   ?   F . n 
F 2 331 SER 331 365 ?   ?   ?   F . n 
F 2 332 LEU 332 366 ?   ?   ?   F . n 
F 2 333 PRO 333 367 ?   ?   ?   F . n 
F 2 334 SER 334 368 ?   ?   ?   F . n 
F 2 335 SER 335 369 ?   ?   ?   F . n 
F 2 336 GLU 336 370 ?   ?   ?   F . n 
F 2 337 ARG 337 371 ?   ?   ?   F . n 
F 2 338 MET 338 372 ?   ?   ?   F . n 
F 2 339 LYS 339 373 ?   ?   ?   F . n 
F 2 340 LEU 340 374 ?   ?   ?   F . n 
F 2 341 SER 341 375 ?   ?   ?   F . n 
F 2 342 GLN 342 376 ?   ?   ?   F . n 
F 2 343 GLY 343 377 ?   ?   ?   F . n 
F 2 344 ASN 344 378 ?   ?   ?   F . n 
F 2 345 THR 345 379 ?   ?   ?   F . n 
F 2 346 THR 346 380 ?   ?   ?   F . n 
F 2 347 LEU 347 381 ?   ?   ?   F . n 
F 2 348 SER 348 382 ?   ?   ?   F . n 
F 2 349 ILE 349 383 ?   ?   ?   F . n 
F 2 350 ASN 350 384 ?   ?   ?   F . n 
F 2 351 PRO 351 385 ?   ?   ?   F . n 
F 2 352 VAL 352 386 ?   ?   ?   F . n 
F 2 353 LYS 353 387 ?   ?   ?   F . n 
F 2 354 ARG 354 388 ?   ?   ?   F . n 
F 2 355 GLU 355 389 ?   ?   ?   F . n 
F 2 356 ASP 356 390 ?   ?   ?   F . n 
F 2 357 ALA 357 391 ?   ?   ?   F . n 
F 2 358 GLY 358 392 ?   ?   ?   F . n 
F 2 359 THR 359 393 ?   ?   ?   F . n 
F 2 360 TYR 360 394 ?   ?   ?   F . n 
F 2 361 TRP 361 395 ?   ?   ?   F . n 
F 2 362 CYS 362 396 ?   ?   ?   F . n 
F 2 363 GLU 363 397 ?   ?   ?   F . n 
F 2 364 VAL 364 398 ?   ?   ?   F . n 
F 2 365 PHE 365 399 ?   ?   ?   F . n 
F 2 366 ASN 366 400 ?   ?   ?   F . n 
F 2 367 PRO 367 401 ?   ?   ?   F . n 
F 2 368 ILE 368 402 ?   ?   ?   F . n 
F 2 369 SER 369 403 ?   ?   ?   F . n 
F 2 370 LYS 370 404 ?   ?   ?   F . n 
F 2 371 ASN 371 405 ?   ?   ?   F . n 
F 2 372 GLN 372 406 ?   ?   ?   F . n 
F 2 373 SER 373 407 ?   ?   ?   F . n 
F 2 374 ASP 374 408 ?   ?   ?   F . n 
F 2 375 PRO 375 409 ?   ?   ?   F . n 
F 2 376 ILE 376 410 ?   ?   ?   F . n 
F 2 377 MET 377 411 ?   ?   ?   F . n 
F 2 378 LEU 378 412 ?   ?   ?   F . n 
F 2 379 ASN 379 413 ?   ?   ?   F . n 
F 2 380 VAL 380 414 ?   ?   ?   F . n 
F 2 381 ASN 381 415 ?   ?   ?   F . n 
F 2 382 TYR 382 416 ?   ?   ?   F . n 
F 2 383 ASN 383 417 ?   ?   ?   F . n 
F 2 384 ALA 384 418 ?   ?   ?   F . n 
F 2 385 LEU 385 419 ?   ?   ?   F . n 
F 2 386 PRO 386 420 ?   ?   ?   F . n 
F 2 387 GLN 387 421 ?   ?   ?   F . n 
F 2 388 GLU 388 422 ?   ?   ?   F . n 
F 2 389 ASN 389 423 ?   ?   ?   F . n 
F 2 390 GLY 390 424 ?   ?   ?   F . n 
F 2 391 LEU 391 425 ?   ?   ?   F . n 
F 2 392 SER 392 426 ?   ?   ?   F . n 
F 2 393 PRO 393 427 ?   ?   ?   F . n 
F 2 394 GLY 394 428 ?   ?   ?   F . n 
F 2 395 HIS 395 429 ?   ?   ?   F . n 
F 2 396 HIS 396 430 ?   ?   ?   F . n 
F 2 397 HIS 397 431 ?   ?   ?   F . n 
F 2 398 HIS 398 432 ?   ?   ?   F . n 
F 2 399 HIS 399 433 ?   ?   ?   F . n 
F 2 400 HIS 400 434 ?   ?   ?   F . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
G  3 NAG 1 501 501 NAG NAG D . 
H  3 NAG 1 502 503 NAG NAG D . 
I  3 NAG 1 503 504 NAG NAG D . 
J  3 NAG 1 504 505 NAG NAG D . 
K  3 NAG 1 505 506 NAG NAG D . 
L  3 NAG 1 506 507 NAG NAG D . 
M  3 NAG 1 501 501 NAG NAG E . 
N  3 NAG 1 502 503 NAG NAG E . 
O  3 NAG 1 503 504 NAG NAG E . 
P  3 NAG 1 504 505 NAG NAG E . 
Q  3 NAG 1 505 506 NAG NAG E . 
R  3 NAG 1 506 507 NAG NAG E . 
S  3 NAG 1 501 501 NAG NAG F . 
T  3 NAG 1 502 503 NAG NAG F . 
U  3 NAG 1 503 504 NAG NAG F . 
V  3 NAG 1 504 505 NAG NAG F . 
W  3 NAG 1 505 506 NAG NAG F . 
X  3 NAG 1 506 507 NAG NAG F . 
Y  4 HOH 1 501 1   HOH HOH A . 
Z  4 HOH 1 501 2   HOH HOH B . 
AA 4 HOH 1 501 3   HOH HOH C . 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GH5 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9GH5 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9GH5 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9GH5 
_refine.pdbx_diffrn_id                           ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            . 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'ELECTRON MICROSCOPY' ? 0.003  ? 10569 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.684  ? 14358 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 10.401 ? 1565  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.053  ? 1635  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.006  ? 1908  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9GH5 
_struct.title                        'Complex of Fusobacterium nucleatum CbpF with human CEACAM1' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9GH5 
_struct_keywords.text            'bacterial pathogenesis, adhesin, immunomodulation, host-pathogen interaction, CELL ADHESION' 
_struct_keywords.pdbx_keywords   'CELL ADHESION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 1 ? 
D  N N 2 ? 
E  N N 2 ? 
F  N N 2 ? 
G  N N 3 ? 
H  N N 3 ? 
I  N N 3 ? 
J  N N 3 ? 
K  N N 3 ? 
L  N N 3 ? 
M  N N 3 ? 
N  N N 3 ? 
O  N N 3 ? 
P  N N 3 ? 
Q  N N 3 ? 
R  N N 3 ? 
S  N N 3 ? 
T  N N 3 ? 
U  N N 3 ? 
V  N N 3 ? 
W  N N 3 ? 
X  N N 3 ? 
Y  N N 4 ? 
Z  N N 4 ? 
AA N N 4 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP Q8RIS0_FUSNN Q8RIS0 ? 1 
;SAAPVIKAGTATDSTEAGVDNVANGVKSSAFGYDNKAIEKESSAFGTGNRATGEFSSAFGFHNIASKIHSSAFGSNNAAD
GVNSSAFGFKNTVSGFNSSAFGSQYQVTGNFSGAFGMGEFNGQYQYKNEGNNSYMIGNKNKIASGSDDNFILGNNVHIGG
GINNSVALGNNSTVSASNTVSVGSSTLKRKIVNVGDGAISANSSDAVTGRQLYSGNGIDTAAWQNKLNVTRKNDYKDAND
IDVNKWKAKLGVGSGGGGGAPVDAYTKSEADNKFANKTDLNDYTKKDDYKDANGIDVDKWKAKLGTGAGTADIENLRNEV
NEKIDDVKDEVRTVGSLSAALAGLHPMQYDPKAPVQVMAALGHYRDKQSVAVGASYYFNDRFMMSTGIALSGEKRTKTMA
NVGFTLKLGKGSGVTYDETPQYVVQNEVKRLTVENQELKERVRNLEEKLNMLLKNK
;
24 
2 UNP CEAM1_HUMAN  P13688 ? 2 
;QLTTESMPFNVAEGKEVLLLVHNLPQQLFGYSWYKGERVDGNRQIVGYAIGTQQATPGPANSGRETIYPNASLLIQNVTQ
NDTGFYTLQVIKSDLVNEEATGQFHVYPELPKPSISSNNSNPVEDKDAVAFTCEPETQDTTYLWWINNQSLPVSPRLQLS
NGNRTLTLLSVTRNDTGPYECEIQNPVSANRSDPVTLNVTYGPDTPTISPSDTYYRPGANLSLSCYAASNPPAQYSWLIN
GTFQQSTQELFIPNITVNNSGSYTCHANNSVTGCNRTTVKTIIVTELSPVVAKPQIKASKTTVTGDKDSVNLTCSTNDTG
ISIRWFFKNQSLPSSERMKLSQGNTTLSINPVKREDAGTYWCEVFNPISKNQSDPIMLNVNYNALPQENGLSPG
;
35 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9GH5 A 22 ? 477 ? Q8RIS0 24 ? 479 ? 24 479 
2 1 9GH5 B 22 ? 477 ? Q8RIS0 24 ? 479 ? 24 479 
3 1 9GH5 C 22 ? 477 ? Q8RIS0 24 ? 479 ? 24 479 
4 2 9GH5 D 1  ? 394 ? P13688 35 ? 428 ? 35 428 
5 2 9GH5 E 1  ? 394 ? P13688 35 ? 428 ? 35 428 
6 2 9GH5 F 1  ? 394 ? P13688 35 ? 428 ? 35 428 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9GH5 MET A 1   ? UNP Q8RIS0 ? ? 'initiating methionine' 3   1   
1 9GH5 LYS A 2   ? UNP Q8RIS0 ? ? 'expression tag'        4   2   
1 9GH5 LYS A 3   ? UNP Q8RIS0 ? ? 'expression tag'        5   3   
1 9GH5 THR A 4   ? UNP Q8RIS0 ? ? 'expression tag'        6   4   
1 9GH5 ALA A 5   ? UNP Q8RIS0 ? ? 'expression tag'        7   5   
1 9GH5 ILE A 6   ? UNP Q8RIS0 ? ? 'expression tag'        8   6   
1 9GH5 ALA A 7   ? UNP Q8RIS0 ? ? 'expression tag'        9   7   
1 9GH5 ILE A 8   ? UNP Q8RIS0 ? ? 'expression tag'        10  8   
1 9GH5 ALA A 9   ? UNP Q8RIS0 ? ? 'expression tag'        11  9   
1 9GH5 VAL A 10  ? UNP Q8RIS0 ? ? 'expression tag'        12  10  
1 9GH5 ALA A 11  ? UNP Q8RIS0 ? ? 'expression tag'        13  11  
1 9GH5 LEU A 12  ? UNP Q8RIS0 ? ? 'expression tag'        14  12  
1 9GH5 ALA A 13  ? UNP Q8RIS0 ? ? 'expression tag'        15  13  
1 9GH5 GLY A 14  ? UNP Q8RIS0 ? ? 'expression tag'        16  14  
1 9GH5 PHE A 15  ? UNP Q8RIS0 ? ? 'expression tag'        17  15  
1 9GH5 ALA A 16  ? UNP Q8RIS0 ? ? 'expression tag'        18  16  
1 9GH5 THR A 17  ? UNP Q8RIS0 ? ? 'expression tag'        19  17  
1 9GH5 VAL A 18  ? UNP Q8RIS0 ? ? 'expression tag'        20  18  
1 9GH5 ALA A 19  ? UNP Q8RIS0 ? ? 'expression tag'        21  19  
1 9GH5 GLN A 20  ? UNP Q8RIS0 ? ? 'expression tag'        22  20  
1 9GH5 ALA A 21  ? UNP Q8RIS0 ? ? 'expression tag'        23  21  
1 9GH5 ARG A 478 ? UNP Q8RIS0 ? ? 'expression tag'        480 22  
1 9GH5 SER A 479 ? UNP Q8RIS0 ? ? 'expression tag'        481 23  
1 9GH5 SER A 480 ? UNP Q8RIS0 ? ? 'expression tag'        482 24  
1 9GH5 ALA A 481 ? UNP Q8RIS0 ? ? 'expression tag'        483 25  
1 9GH5 TRP A 482 ? UNP Q8RIS0 ? ? 'expression tag'        484 26  
1 9GH5 SER A 483 ? UNP Q8RIS0 ? ? 'expression tag'        485 27  
1 9GH5 HIS A 484 ? UNP Q8RIS0 ? ? 'expression tag'        486 28  
1 9GH5 PRO A 485 ? UNP Q8RIS0 ? ? 'expression tag'        487 29  
1 9GH5 GLN A 486 ? UNP Q8RIS0 ? ? 'expression tag'        488 30  
1 9GH5 PHE A 487 ? UNP Q8RIS0 ? ? 'expression tag'        489 31  
1 9GH5 GLU A 488 ? UNP Q8RIS0 ? ? 'expression tag'        490 32  
1 9GH5 LYS A 489 ? UNP Q8RIS0 ? ? 'expression tag'        491 33  
2 9GH5 MET B 1   ? UNP Q8RIS0 ? ? 'initiating methionine' 3   34  
2 9GH5 LYS B 2   ? UNP Q8RIS0 ? ? 'expression tag'        4   35  
2 9GH5 LYS B 3   ? UNP Q8RIS0 ? ? 'expression tag'        5   36  
2 9GH5 THR B 4   ? UNP Q8RIS0 ? ? 'expression tag'        6   37  
2 9GH5 ALA B 5   ? UNP Q8RIS0 ? ? 'expression tag'        7   38  
2 9GH5 ILE B 6   ? UNP Q8RIS0 ? ? 'expression tag'        8   39  
2 9GH5 ALA B 7   ? UNP Q8RIS0 ? ? 'expression tag'        9   40  
2 9GH5 ILE B 8   ? UNP Q8RIS0 ? ? 'expression tag'        10  41  
2 9GH5 ALA B 9   ? UNP Q8RIS0 ? ? 'expression tag'        11  42  
2 9GH5 VAL B 10  ? UNP Q8RIS0 ? ? 'expression tag'        12  43  
2 9GH5 ALA B 11  ? UNP Q8RIS0 ? ? 'expression tag'        13  44  
2 9GH5 LEU B 12  ? UNP Q8RIS0 ? ? 'expression tag'        14  45  
2 9GH5 ALA B 13  ? UNP Q8RIS0 ? ? 'expression tag'        15  46  
2 9GH5 GLY B 14  ? UNP Q8RIS0 ? ? 'expression tag'        16  47  
2 9GH5 PHE B 15  ? UNP Q8RIS0 ? ? 'expression tag'        17  48  
2 9GH5 ALA B 16  ? UNP Q8RIS0 ? ? 'expression tag'        18  49  
2 9GH5 THR B 17  ? UNP Q8RIS0 ? ? 'expression tag'        19  50  
2 9GH5 VAL B 18  ? UNP Q8RIS0 ? ? 'expression tag'        20  51  
2 9GH5 ALA B 19  ? UNP Q8RIS0 ? ? 'expression tag'        21  52  
2 9GH5 GLN B 20  ? UNP Q8RIS0 ? ? 'expression tag'        22  53  
2 9GH5 ALA B 21  ? UNP Q8RIS0 ? ? 'expression tag'        23  54  
2 9GH5 ARG B 478 ? UNP Q8RIS0 ? ? 'expression tag'        480 55  
2 9GH5 SER B 479 ? UNP Q8RIS0 ? ? 'expression tag'        481 56  
2 9GH5 SER B 480 ? UNP Q8RIS0 ? ? 'expression tag'        482 57  
2 9GH5 ALA B 481 ? UNP Q8RIS0 ? ? 'expression tag'        483 58  
2 9GH5 TRP B 482 ? UNP Q8RIS0 ? ? 'expression tag'        484 59  
2 9GH5 SER B 483 ? UNP Q8RIS0 ? ? 'expression tag'        485 60  
2 9GH5 HIS B 484 ? UNP Q8RIS0 ? ? 'expression tag'        486 61  
2 9GH5 PRO B 485 ? UNP Q8RIS0 ? ? 'expression tag'        487 62  
2 9GH5 GLN B 486 ? UNP Q8RIS0 ? ? 'expression tag'        488 63  
2 9GH5 PHE B 487 ? UNP Q8RIS0 ? ? 'expression tag'        489 64  
2 9GH5 GLU B 488 ? UNP Q8RIS0 ? ? 'expression tag'        490 65  
2 9GH5 LYS B 489 ? UNP Q8RIS0 ? ? 'expression tag'        491 66  
3 9GH5 MET C 1   ? UNP Q8RIS0 ? ? 'initiating methionine' 3   67  
3 9GH5 LYS C 2   ? UNP Q8RIS0 ? ? 'expression tag'        4   68  
3 9GH5 LYS C 3   ? UNP Q8RIS0 ? ? 'expression tag'        5   69  
3 9GH5 THR C 4   ? UNP Q8RIS0 ? ? 'expression tag'        6   70  
3 9GH5 ALA C 5   ? UNP Q8RIS0 ? ? 'expression tag'        7   71  
3 9GH5 ILE C 6   ? UNP Q8RIS0 ? ? 'expression tag'        8   72  
3 9GH5 ALA C 7   ? UNP Q8RIS0 ? ? 'expression tag'        9   73  
3 9GH5 ILE C 8   ? UNP Q8RIS0 ? ? 'expression tag'        10  74  
3 9GH5 ALA C 9   ? UNP Q8RIS0 ? ? 'expression tag'        11  75  
3 9GH5 VAL C 10  ? UNP Q8RIS0 ? ? 'expression tag'        12  76  
3 9GH5 ALA C 11  ? UNP Q8RIS0 ? ? 'expression tag'        13  77  
3 9GH5 LEU C 12  ? UNP Q8RIS0 ? ? 'expression tag'        14  78  
3 9GH5 ALA C 13  ? UNP Q8RIS0 ? ? 'expression tag'        15  79  
3 9GH5 GLY C 14  ? UNP Q8RIS0 ? ? 'expression tag'        16  80  
3 9GH5 PHE C 15  ? UNP Q8RIS0 ? ? 'expression tag'        17  81  
3 9GH5 ALA C 16  ? UNP Q8RIS0 ? ? 'expression tag'        18  82  
3 9GH5 THR C 17  ? UNP Q8RIS0 ? ? 'expression tag'        19  83  
3 9GH5 VAL C 18  ? UNP Q8RIS0 ? ? 'expression tag'        20  84  
3 9GH5 ALA C 19  ? UNP Q8RIS0 ? ? 'expression tag'        21  85  
3 9GH5 GLN C 20  ? UNP Q8RIS0 ? ? 'expression tag'        22  86  
3 9GH5 ALA C 21  ? UNP Q8RIS0 ? ? 'expression tag'        23  87  
3 9GH5 ARG C 478 ? UNP Q8RIS0 ? ? 'expression tag'        480 88  
3 9GH5 SER C 479 ? UNP Q8RIS0 ? ? 'expression tag'        481 89  
3 9GH5 SER C 480 ? UNP Q8RIS0 ? ? 'expression tag'        482 90  
3 9GH5 ALA C 481 ? UNP Q8RIS0 ? ? 'expression tag'        483 91  
3 9GH5 TRP C 482 ? UNP Q8RIS0 ? ? 'expression tag'        484 92  
3 9GH5 SER C 483 ? UNP Q8RIS0 ? ? 'expression tag'        485 93  
3 9GH5 HIS C 484 ? UNP Q8RIS0 ? ? 'expression tag'        486 94  
3 9GH5 PRO C 485 ? UNP Q8RIS0 ? ? 'expression tag'        487 95  
3 9GH5 GLN C 486 ? UNP Q8RIS0 ? ? 'expression tag'        488 96  
3 9GH5 PHE C 487 ? UNP Q8RIS0 ? ? 'expression tag'        489 97  
3 9GH5 GLU C 488 ? UNP Q8RIS0 ? ? 'expression tag'        490 98  
3 9GH5 LYS C 489 ? UNP Q8RIS0 ? ? 'expression tag'        491 99  
4 9GH5 HIS D 395 ? UNP P13688 ? ? 'expression tag'        429 100 
4 9GH5 HIS D 396 ? UNP P13688 ? ? 'expression tag'        430 101 
4 9GH5 HIS D 397 ? UNP P13688 ? ? 'expression tag'        431 102 
4 9GH5 HIS D 398 ? UNP P13688 ? ? 'expression tag'        432 103 
4 9GH5 HIS D 399 ? UNP P13688 ? ? 'expression tag'        433 104 
4 9GH5 HIS D 400 ? UNP P13688 ? ? 'expression tag'        434 105 
5 9GH5 HIS E 395 ? UNP P13688 ? ? 'expression tag'        429 106 
5 9GH5 HIS E 396 ? UNP P13688 ? ? 'expression tag'        430 107 
5 9GH5 HIS E 397 ? UNP P13688 ? ? 'expression tag'        431 108 
5 9GH5 HIS E 398 ? UNP P13688 ? ? 'expression tag'        432 109 
5 9GH5 HIS E 399 ? UNP P13688 ? ? 'expression tag'        433 110 
5 9GH5 HIS E 400 ? UNP P13688 ? ? 'expression tag'        434 111 
6 9GH5 HIS F 395 ? UNP P13688 ? ? 'expression tag'        429 112 
6 9GH5 HIS F 396 ? UNP P13688 ? ? 'expression tag'        430 113 
6 9GH5 HIS F 397 ? UNP P13688 ? ? 'expression tag'        431 114 
6 9GH5 HIS F 398 ? UNP P13688 ? ? 'expression tag'        432 115 
6 9GH5 HIS F 399 ? UNP P13688 ? ? 'expression tag'        433 116 
6 9GH5 HIS F 400 ? UNP P13688 ? ? 'expression tag'        434 117 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 229 ? GLY A 236 ? THR A 231 GLY A 238 1 ? 8 
HELX_P HELX_P2  AA2 ALA A 243 ? LEU A 248 ? ALA A 245 LEU A 250 1 ? 6 
HELX_P HELX_P3  AA3 ARG A 252 ? ALA A 259 ? ARG A 254 ALA A 261 1 ? 8 
HELX_P HELX_P4  AA4 LYS A 266 ? LEU A 271 ? LYS A 268 LEU A 273 1 ? 6 
HELX_P HELX_P5  AA5 THR B 229 ? GLY B 236 ? THR B 231 GLY B 238 1 ? 8 
HELX_P HELX_P6  AA6 ALA B 243 ? LEU B 248 ? ALA B 245 LEU B 250 1 ? 6 
HELX_P HELX_P7  AA7 ARG B 252 ? ALA B 259 ? ARG B 254 ALA B 261 1 ? 8 
HELX_P HELX_P8  AA8 ASP B 263 ? LEU B 271 ? ASP B 265 LEU B 273 1 ? 9 
HELX_P HELX_P9  AA9 THR C 229 ? GLY C 236 ? THR C 231 GLY C 238 1 ? 8 
HELX_P HELX_P10 AB1 ALA C 243 ? LEU C 248 ? ALA C 245 LEU C 250 1 ? 6 
HELX_P HELX_P11 AB2 ARG C 252 ? LYS C 257 ? ARG C 254 LYS C 259 1 ? 6 
HELX_P HELX_P12 AB3 LYS C 266 ? LEU C 271 ? LYS C 268 LEU C 273 1 ? 6 
HELX_P HELX_P13 AB4 ASP D 40  ? ASN D 42  ? ASP D 74  ASN D 76  5 ? 3 
HELX_P HELX_P14 AB5 THR D 79  ? THR D 83  ? THR D 113 THR D 117 5 ? 5 
HELX_P HELX_P15 AB6 THR D 172 ? THR D 176 ? THR D 206 THR D 210 5 ? 5 
HELX_P HELX_P16 AB7 ASP E 40  ? ASN E 42  ? ASP E 74  ASN E 76  5 ? 3 
HELX_P HELX_P17 AB8 THR E 79  ? THR E 83  ? THR E 113 THR E 117 5 ? 5 
HELX_P HELX_P18 AB9 THR E 172 ? THR E 176 ? THR E 206 THR E 210 5 ? 5 
HELX_P HELX_P19 AC1 ASP F 40  ? ASN F 42  ? ASP F 74  ASN F 76  5 ? 3 
HELX_P HELX_P20 AC2 THR F 79  ? THR F 83  ? THR F 113 THR F 117 5 ? 5 
HELX_P HELX_P21 AC3 THR F 172 ? THR F 176 ? THR F 206 THR F 210 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ?   ? D CYS 133 SG  ? ? ? 1_555 D CYS 181 SG ? ? D CYS 167 D CYS 215 1_555 ? ? ? ? ? ? ? 2.036 ? ?               
disulf2  disulf ?   ? E CYS 133 SG  ? ? ? 1_555 E CYS 181 SG ? ? E CYS 167 E CYS 215 1_555 ? ? ? ? ? ? ? 2.036 ? ?               
disulf3  disulf ?   ? F CYS 133 SG  ? ? ? 1_555 F CYS 181 SG ? ? F CYS 167 F CYS 215 1_555 ? ? ? ? ? ? ? 2.033 ? ?               
covale1  covale one ? D ASN 70  ND2 ? ? ? 1_555 G NAG .   C1 ? ? D ASN 104 D NAG 501 1_555 ? ? ? ? ? ? ? 1.448 ? N-Glycosylation 
covale2  covale one ? D ASN 77  ND2 ? ? ? 1_555 H NAG .   C1 ? ? D ASN 111 D NAG 502 1_555 ? ? ? ? ? ? ? 1.445 ? N-Glycosylation 
covale3  covale one ? D ASN 118 ND2 ? ? ? 1_555 K NAG .   C1 ? ? D ASN 152 D NAG 505 1_555 ? ? ? ? ? ? ? 1.451 ? N-Glycosylation 
covale4  covale one ? D ASN 148 ND2 ? ? ? 1_555 I NAG .   C1 ? ? D ASN 182 D NAG 503 1_555 ? ? ? ? ? ? ? 1.445 ? N-Glycosylation 
covale5  covale one ? D ASN 163 ND2 ? ? ? 1_555 J NAG .   C1 ? ? D ASN 197 D NAG 504 1_555 ? ? ? ? ? ? ? 1.442 ? N-Glycosylation 
covale6  covale one ? D ASN 190 ND2 ? ? ? 1_555 L NAG .   C1 ? ? D ASN 224 D NAG 506 1_555 ? ? ? ? ? ? ? 1.439 ? N-Glycosylation 
covale7  covale one ? E ASN 70  ND2 ? ? ? 1_555 M NAG .   C1 ? ? E ASN 104 E NAG 501 1_555 ? ? ? ? ? ? ? 1.443 ? N-Glycosylation 
covale8  covale one ? E ASN 77  ND2 ? ? ? 1_555 N NAG .   C1 ? ? E ASN 111 E NAG 502 1_555 ? ? ? ? ? ? ? 1.439 ? N-Glycosylation 
covale9  covale one ? E ASN 118 ND2 ? ? ? 1_555 Q NAG .   C1 ? ? E ASN 152 E NAG 505 1_555 ? ? ? ? ? ? ? 1.446 ? N-Glycosylation 
covale10 covale one ? E ASN 148 ND2 ? ? ? 1_555 O NAG .   C1 ? ? E ASN 182 E NAG 503 1_555 ? ? ? ? ? ? ? 1.459 ? N-Glycosylation 
covale11 covale one ? E ASN 163 ND2 ? ? ? 1_555 P NAG .   C1 ? ? E ASN 197 E NAG 504 1_555 ? ? ? ? ? ? ? 1.433 ? N-Glycosylation 
covale12 covale one ? E ASN 190 ND2 ? ? ? 1_555 R NAG .   C1 ? ? E ASN 224 E NAG 506 1_555 ? ? ? ? ? ? ? 1.435 ? N-Glycosylation 
covale13 covale one ? F ASN 70  ND2 ? ? ? 1_555 S NAG .   C1 ? ? F ASN 104 F NAG 501 1_555 ? ? ? ? ? ? ? 1.450 ? N-Glycosylation 
covale14 covale one ? F ASN 77  ND2 ? ? ? 1_555 T NAG .   C1 ? ? F ASN 111 F NAG 502 1_555 ? ? ? ? ? ? ? 1.441 ? N-Glycosylation 
covale15 covale one ? F ASN 118 ND2 ? ? ? 1_555 W NAG .   C1 ? ? F ASN 152 F NAG 505 1_555 ? ? ? ? ? ? ? 1.451 ? N-Glycosylation 
covale16 covale one ? F ASN 148 ND2 ? ? ? 1_555 U NAG .   C1 ? ? F ASN 182 F NAG 503 1_555 ? ? ? ? ? ? ? 1.456 ? N-Glycosylation 
covale17 covale one ? F ASN 163 ND2 ? ? ? 1_555 V NAG .   C1 ? ? F ASN 197 F NAG 504 1_555 ? ? ? ? ? ? ? 1.441 ? N-Glycosylation 
covale18 covale one ? F ASN 190 ND2 ? ? ? 1_555 X NAG .   C1 ? ? F ASN 224 F NAG 506 1_555 ? ? ? ? ? ? ? 1.449 ? N-Glycosylation 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  NAG G .   ? ASN D 70  ? NAG D 501 ? 1_555 ASN D 104 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2  NAG H .   ? ASN D 77  ? NAG D 502 ? 1_555 ASN D 111 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3  NAG I .   ? ASN D 148 ? NAG D 503 ? 1_555 ASN D 182 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4  NAG J .   ? ASN D 163 ? NAG D 504 ? 1_555 ASN D 197 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5  NAG K .   ? ASN D 118 ? NAG D 505 ? 1_555 ASN D 152 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
6  NAG L .   ? ASN D 190 ? NAG D 506 ? 1_555 ASN D 224 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
7  NAG M .   ? ASN E 70  ? NAG E 501 ? 1_555 ASN E 104 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
8  NAG N .   ? ASN E 77  ? NAG E 502 ? 1_555 ASN E 111 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
9  NAG O .   ? ASN E 148 ? NAG E 503 ? 1_555 ASN E 182 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
10 NAG P .   ? ASN E 163 ? NAG E 504 ? 1_555 ASN E 197 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
11 NAG Q .   ? ASN E 118 ? NAG E 505 ? 1_555 ASN E 152 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
12 NAG R .   ? ASN E 190 ? NAG E 506 ? 1_555 ASN E 224 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
13 NAG S .   ? ASN F 70  ? NAG F 501 ? 1_555 ASN F 104 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
14 NAG T .   ? ASN F 77  ? NAG F 502 ? 1_555 ASN F 111 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
15 NAG U .   ? ASN F 148 ? NAG F 503 ? 1_555 ASN F 182 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
16 NAG V .   ? ASN F 163 ? NAG F 504 ? 1_555 ASN F 197 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
17 NAG W .   ? ASN F 118 ? NAG F 505 ? 1_555 ASN F 152 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
18 NAG X .   ? ASN F 190 ? NAG F 506 ? 1_555 ASN F 224 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
19 CYS D 133 ? CYS D 181 ? CYS D 167 ? 1_555 CYS D 215 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
20 CYS E 133 ? CYS E 181 ? CYS E 167 ? 1_555 CYS E 215 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
21 CYS F 133 ? CYS F 181 ? CYS F 167 ? 1_555 CYS F 215 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 MET 7 D . ? MET 41 D PRO 8 D ? PRO 42 D 1 -2.52 
2 MET 7 E . ? MET 41 E PRO 8 E ? PRO 42 E 1 -3.13 
3 MET 7 F . ? MET 41 F PRO 8 F ? PRO 42 F 1 -2.63 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9  ? 
AA2 ? 13 ? 
AA3 ? 2  ? 
AA4 ? 13 ? 
AA5 ? 9  ? 
AA6 ? 9  ? 
AA7 ? 13 ? 
AA8 ? 2  ? 
AA9 ? 2  ? 
AB1 ? 4  ? 
AB2 ? 6  ? 
AB3 ? 4  ? 
AB4 ? 3  ? 
AB5 ? 4  ? 
AB6 ? 6  ? 
AB7 ? 4  ? 
AB8 ? 4  ? 
AB9 ? 4  ? 
AC1 ? 6  ? 
AC2 ? 4  ? 
AC3 ? 4  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1  2  ? anti-parallel 
AA1 2  3  ? parallel      
AA1 3  4  ? parallel      
AA1 4  5  ? parallel      
AA1 5  6  ? parallel      
AA1 6  7  ? parallel      
AA1 7  8  ? parallel      
AA1 8  9  ? parallel      
AA2 1  2  ? parallel      
AA2 2  3  ? parallel      
AA2 3  4  ? parallel      
AA2 4  5  ? parallel      
AA2 5  6  ? parallel      
AA2 6  7  ? parallel      
AA2 7  8  ? parallel      
AA2 8  9  ? parallel      
AA2 9  10 ? parallel      
AA2 10 11 ? parallel      
AA2 11 12 ? parallel      
AA2 12 13 ? parallel      
AA3 1  2  ? parallel      
AA4 1  2  ? parallel      
AA4 2  3  ? parallel      
AA4 3  4  ? parallel      
AA4 4  5  ? parallel      
AA4 5  6  ? parallel      
AA4 6  7  ? parallel      
AA4 7  8  ? parallel      
AA4 8  9  ? parallel      
AA4 9  10 ? parallel      
AA4 10 11 ? parallel      
AA4 11 12 ? parallel      
AA4 12 13 ? parallel      
AA5 1  2  ? anti-parallel 
AA5 2  3  ? parallel      
AA5 3  4  ? parallel      
AA5 4  5  ? parallel      
AA5 5  6  ? parallel      
AA5 6  7  ? parallel      
AA5 7  8  ? parallel      
AA5 8  9  ? parallel      
AA6 1  2  ? anti-parallel 
AA6 2  3  ? parallel      
AA6 3  4  ? parallel      
AA6 4  5  ? parallel      
AA6 5  6  ? parallel      
AA6 6  7  ? parallel      
AA6 7  8  ? parallel      
AA6 8  9  ? parallel      
AA7 1  2  ? parallel      
AA7 2  3  ? parallel      
AA7 3  4  ? parallel      
AA7 4  5  ? parallel      
AA7 5  6  ? parallel      
AA7 6  7  ? parallel      
AA7 7  8  ? parallel      
AA7 8  9  ? parallel      
AA7 9  10 ? parallel      
AA7 10 11 ? parallel      
AA7 11 12 ? parallel      
AA7 12 13 ? parallel      
AA8 1  2  ? parallel      
AA9 1  2  ? parallel      
AB1 1  2  ? anti-parallel 
AB1 2  3  ? anti-parallel 
AB1 3  4  ? anti-parallel 
AB2 1  2  ? parallel      
AB2 2  3  ? anti-parallel 
AB2 3  4  ? anti-parallel 
AB2 4  5  ? anti-parallel 
AB2 5  6  ? anti-parallel 
AB3 1  2  ? anti-parallel 
AB3 2  3  ? anti-parallel 
AB3 3  4  ? anti-parallel 
AB4 1  2  ? anti-parallel 
AB4 2  3  ? anti-parallel 
AB5 1  2  ? anti-parallel 
AB5 2  3  ? anti-parallel 
AB5 3  4  ? anti-parallel 
AB6 1  2  ? parallel      
AB6 2  3  ? anti-parallel 
AB6 3  4  ? anti-parallel 
AB6 4  5  ? anti-parallel 
AB6 5  6  ? anti-parallel 
AB7 1  2  ? anti-parallel 
AB7 2  3  ? anti-parallel 
AB7 3  4  ? anti-parallel 
AB8 1  2  ? anti-parallel 
AB8 2  3  ? anti-parallel 
AB8 3  4  ? anti-parallel 
AB9 1  2  ? anti-parallel 
AB9 2  3  ? anti-parallel 
AB9 3  4  ? anti-parallel 
AC1 1  2  ? parallel      
AC1 2  3  ? anti-parallel 
AC1 3  4  ? anti-parallel 
AC1 4  5  ? anti-parallel 
AC1 5  6  ? anti-parallel 
AC2 1  2  ? anti-parallel 
AC2 2  3  ? anti-parallel 
AC2 3  4  ? anti-parallel 
AC3 1  2  ? anti-parallel 
AC3 2  3  ? anti-parallel 
AC3 3  4  ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  VAL A 26  ? ALA A 29  ? VAL A 28  ALA A 31  
AA1 2  THR A 36  ? VAL A 40  ? THR A 38  VAL A 42  
AA1 3  SER A 50  ? TYR A 54  ? SER A 52  TYR A 56  
AA1 4  SER A 64  ? THR A 68  ? SER A 66  THR A 70  
AA1 5  SER A 78  ? PHE A 82  ? SER A 80  PHE A 84  
AA1 6  SER A 91  ? SER A 96  ? SER A 93  SER A 98  
AA1 7  SER A 105 ? VAL A 114 ? SER A 107 VAL A 116 
AA1 8  SER A 120 ? VAL A 128 ? SER A 122 VAL A 130 
AA1 9  LYS A 148 ? ASN A 149 ? LYS A 150 ASN A 151 
AA2 1  VAL A 43  ? ALA A 44  ? VAL A 45  ALA A 46  
AA2 2  LYS A 57  ? ALA A 58  ? LYS A 59  ALA A 60  
AA2 3  ARG A 71  ? ALA A 72  ? ARG A 73  ALA A 74  
AA2 4  ILE A 85  ? ALA A 86  ? ILE A 87  ALA A 88  
AA2 5  ALA A 99  ? ALA A 100 ? ALA A 101 ALA A 102 
AA2 6  SER A 105 ? VAL A 114 ? SER A 107 VAL A 116 
AA2 7  SER A 120 ? VAL A 128 ? SER A 122 VAL A 130 
AA2 8  GLY A 134 ? MET A 138 ? GLY A 136 MET A 140 
AA2 9  TYR A 155 ? ASN A 159 ? TYR A 157 ASN A 161 
AA2 10 ASN A 170 ? LEU A 173 ? ASN A 172 LEU A 175 
AA2 11 SER A 186 ? LEU A 189 ? SER A 188 LEU A 191 
AA2 12 THR A 200 ? SER A 202 ? THR A 202 SER A 204 
AA2 13 LYS B 211 ? VAL B 213 ? LYS B 213 VAL B 215 
AA3 1  LYS A 162 ? ILE A 163 ? LYS A 164 ILE A 165 
AA3 2  HIS A 178 ? ILE A 179 ? HIS A 180 ILE A 181 
AA4 1  LYS A 211 ? VAL A 213 ? LYS A 213 VAL A 215 
AA4 2  THR C 200 ? SER C 202 ? THR C 202 SER C 204 
AA4 3  SER C 186 ? LEU C 189 ? SER C 188 LEU C 191 
AA4 4  ASN C 170 ? LEU C 173 ? ASN C 172 LEU C 175 
AA4 5  TYR C 155 ? ASN C 159 ? TYR C 157 ASN C 161 
AA4 6  GLY C 134 ? MET C 138 ? GLY C 136 MET C 140 
AA4 7  SER C 120 ? VAL C 128 ? SER C 122 VAL C 130 
AA4 8  SER C 105 ? VAL C 114 ? SER C 107 VAL C 116 
AA4 9  ALA C 99  ? ALA C 100 ? ALA C 101 ALA C 102 
AA4 10 ILE C 85  ? ALA C 86  ? ILE C 87  ALA C 88  
AA4 11 ARG C 71  ? ALA C 72  ? ARG C 73  ALA C 74  
AA4 12 LYS C 57  ? ALA C 58  ? LYS C 59  ALA C 60  
AA4 13 VAL C 43  ? ALA C 44  ? VAL C 45  ALA C 46  
AA5 1  VAL C 26  ? ALA C 29  ? VAL C 28  ALA C 31  
AA5 2  THR C 36  ? VAL C 40  ? THR C 38  VAL C 42  
AA5 3  SER C 50  ? TYR C 54  ? SER C 52  TYR C 56  
AA5 4  SER C 64  ? THR C 68  ? SER C 66  THR C 70  
AA5 5  SER C 78  ? PHE C 82  ? SER C 80  PHE C 84  
AA5 6  SER C 91  ? SER C 96  ? SER C 93  SER C 98  
AA5 7  SER C 105 ? VAL C 114 ? SER C 107 VAL C 116 
AA5 8  SER C 120 ? VAL C 128 ? SER C 122 VAL C 130 
AA5 9  LYS C 148 ? ASN C 149 ? LYS C 150 ASN C 151 
AA6 1  VAL B 26  ? ALA B 29  ? VAL B 28  ALA B 31  
AA6 2  THR B 36  ? VAL B 40  ? THR B 38  VAL B 42  
AA6 3  SER B 50  ? TYR B 54  ? SER B 52  TYR B 56  
AA6 4  SER B 64  ? THR B 68  ? SER B 66  THR B 70  
AA6 5  SER B 78  ? PHE B 82  ? SER B 80  PHE B 84  
AA6 6  SER B 91  ? SER B 96  ? SER B 93  SER B 98  
AA6 7  SER B 105 ? VAL B 114 ? SER B 107 VAL B 116 
AA6 8  SER B 120 ? VAL B 128 ? SER B 122 VAL B 130 
AA6 9  LYS B 148 ? ASN B 149 ? LYS B 150 ASN B 151 
AA7 1  VAL B 43  ? ALA B 44  ? VAL B 45  ALA B 46  
AA7 2  LYS B 57  ? ALA B 58  ? LYS B 59  ALA B 60  
AA7 3  ARG B 71  ? ALA B 72  ? ARG B 73  ALA B 74  
AA7 4  ILE B 85  ? ALA B 86  ? ILE B 87  ALA B 88  
AA7 5  ALA B 99  ? ALA B 100 ? ALA B 101 ALA B 102 
AA7 6  SER B 105 ? VAL B 114 ? SER B 107 VAL B 116 
AA7 7  SER B 120 ? VAL B 128 ? SER B 122 VAL B 130 
AA7 8  GLY B 134 ? MET B 138 ? GLY B 136 MET B 140 
AA7 9  TYR B 155 ? ASN B 159 ? TYR B 157 ASN B 161 
AA7 10 ASN B 170 ? LEU B 173 ? ASN B 172 LEU B 175 
AA7 11 SER B 186 ? LEU B 189 ? SER B 188 LEU B 191 
AA7 12 THR B 200 ? SER B 202 ? THR B 202 SER B 204 
AA7 13 LYS C 211 ? VAL C 213 ? LYS C 213 VAL C 215 
AA8 1  LYS B 162 ? ILE B 163 ? LYS B 164 ILE B 165 
AA8 2  HIS B 178 ? ILE B 179 ? HIS B 180 ILE B 181 
AA9 1  LYS C 162 ? ILE C 163 ? LYS C 164 ILE C 165 
AA9 2  HIS C 178 ? ILE C 179 ? HIS C 180 ILE C 181 
AB1 1  THR D 3   ? MET D 7   ? THR D 37  MET D 41  
AB1 2  VAL D 17  ? HIS D 22  ? VAL D 51  HIS D 56  
AB1 3  LEU D 73  ? ILE D 75  ? LEU D 107 ILE D 109 
AB1 4  GLU D 65  ? ILE D 67  ? GLU D 99  ILE D 101 
AB2 1  ASN D 10  ? ALA D 12  ? ASN D 44  ALA D 46  
AB2 2  ASN D 97  ? TYR D 107 ? ASN D 131 TYR D 141 
AB2 3  GLY D 84  ? LYS D 92  ? GLY D 118 LYS D 126 
AB2 4  LEU D 28  ? LYS D 35  ? LEU D 62  LYS D 69  
AB2 5  GLN D 44  ? ALA D 49  ? GLN D 78  ALA D 83  
AB2 6  GLN D 54  ? PRO D 57  ? GLN D 88  PRO D 91  
AB3 1  ILE D 115 ? SER D 117 ? ILE D 149 SER D 151 
AB3 2  ALA D 130 ? CYS D 133 ? ALA D 164 CYS D 167 
AB3 3  THR D 165 ? LEU D 168 ? THR D 199 LEU D 202 
AB3 4  LEU D 157 ? SER D 160 ? LEU D 191 SER D 194 
AB4 1  GLN D 149 ? SER D 150 ? GLN D 183 SER D 184 
AB4 2  THR D 141 ? ILE D 146 ? THR D 175 ILE D 180 
AB4 3  GLU D 180 ? GLN D 184 ? GLU D 214 GLN D 218 
AB5 1  THR E 3   ? MET E 7   ? THR E 37  MET E 41  
AB5 2  VAL E 17  ? HIS E 22  ? VAL E 51  HIS E 56  
AB5 3  LEU E 73  ? ILE E 75  ? LEU E 107 ILE E 109 
AB5 4  GLU E 65  ? ILE E 67  ? GLU E 99  ILE E 101 
AB6 1  ASN E 10  ? ALA E 12  ? ASN E 44  ALA E 46  
AB6 2  ASN E 97  ? TYR E 107 ? ASN E 131 TYR E 141 
AB6 3  GLY E 84  ? LYS E 92  ? GLY E 118 LYS E 126 
AB6 4  LEU E 28  ? LYS E 35  ? LEU E 62  LYS E 69  
AB6 5  GLN E 44  ? ALA E 49  ? GLN E 78  ALA E 83  
AB6 6  GLN E 54  ? PRO E 57  ? GLN E 88  PRO E 91  
AB7 1  ILE E 115 ? SER E 117 ? ILE E 149 SER E 151 
AB7 2  ALA E 130 ? CYS E 133 ? ALA E 164 CYS E 167 
AB7 3  THR E 165 ? LEU E 168 ? THR E 199 LEU E 202 
AB7 4  LEU E 157 ? SER E 160 ? LEU E 191 SER E 194 
AB8 1  GLN E 149 ? SER E 150 ? GLN E 183 SER E 184 
AB8 2  THR E 141 ? ILE E 146 ? THR E 175 ILE E 180 
AB8 3  TYR E 179 ? GLN E 184 ? TYR E 213 GLN E 218 
AB8 4  ALA E 189 ? ARG E 191 ? ALA E 223 ARG E 225 
AB9 1  THR F 3   ? MET F 7   ? THR F 37  MET F 41  
AB9 2  VAL F 17  ? HIS F 22  ? VAL F 51  HIS F 56  
AB9 3  LEU F 73  ? ILE F 75  ? LEU F 107 ILE F 109 
AB9 4  GLU F 65  ? ILE F 67  ? GLU F 99  ILE F 101 
AC1 1  ASN F 10  ? ALA F 12  ? ASN F 44  ALA F 46  
AC1 2  ASN F 97  ? TYR F 107 ? ASN F 131 TYR F 141 
AC1 3  GLY F 84  ? LYS F 92  ? GLY F 118 LYS F 126 
AC1 4  LEU F 28  ? LYS F 35  ? LEU F 62  LYS F 69  
AC1 5  GLN F 44  ? ALA F 49  ? GLN F 78  ALA F 83  
AC1 6  GLN F 54  ? PRO F 57  ? GLN F 88  PRO F 91  
AC2 1  ILE F 115 ? SER F 117 ? ILE F 149 SER F 151 
AC2 2  ALA F 130 ? CYS F 133 ? ALA F 164 CYS F 167 
AC2 3  THR F 165 ? LEU F 168 ? THR F 199 LEU F 202 
AC2 4  LEU F 157 ? SER F 160 ? LEU F 191 SER F 194 
AC3 1  GLN F 149 ? SER F 150 ? GLN F 183 SER F 184 
AC3 2  THR F 141 ? ILE F 146 ? THR F 175 ILE F 180 
AC3 3  TYR F 179 ? GLN F 184 ? TYR F 213 GLN F 218 
AC3 4  ALA F 189 ? ARG F 191 ? ALA F 223 ARG F 225 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1  2  N LYS A 28  ? N LYS A 30  O GLU A 37  ? O GLU A 39  
AA1 2  3  N ALA A 38  ? N ALA A 40  O GLY A 53  ? O GLY A 55  
AA1 3  4  N PHE A 52  ? N PHE A 54  O GLY A 67  ? O GLY A 69  
AA1 4  5  N THR A 68  ? N THR A 70  O GLY A 81  ? O GLY A 83  
AA1 5  6  N SER A 78  ? N SER A 80  O SER A 91  ? O SER A 93  
AA1 6  7  N SER A 96  ? N SER A 98  O LYS A 111 ? O LYS A 113 
AA1 7  8  N PHE A 108 ? N PHE A 110 O ALA A 121 ? O ALA A 123 
AA1 8  9  N GLN A 127 ? N GLN A 129 O ASN A 149 ? O ASN A 151 
AA2 1  2  N VAL A 43  ? N VAL A 45  O ALA A 58  ? O ALA A 60  
AA2 2  3  N LYS A 57  ? N LYS A 59  O ALA A 72  ? O ALA A 74  
AA2 3  4  N ARG A 71  ? N ARG A 73  O ALA A 86  ? O ALA A 88  
AA2 4  5  N ILE A 85  ? N ILE A 87  O ALA A 100 ? O ALA A 102 
AA2 5  6  N ALA A 99  ? N ALA A 101 O ASN A 112 ? O ASN A 114 
AA2 6  7  N PHE A 108 ? N PHE A 110 O ALA A 121 ? O ALA A 123 
AA2 7  8  N PHE A 122 ? N PHE A 124 O ALA A 135 ? O ALA A 137 
AA2 8  9  N PHE A 136 ? N PHE A 138 O MET A 156 ? O MET A 158 
AA2 9  10 N ILE A 157 ? N ILE A 159 O ILE A 172 ? O ILE A 174 
AA2 10 11 N LEU A 173 ? N LEU A 175 O ALA A 188 ? O ALA A 190 
AA2 11 12 N VAL A 187 ? N VAL A 189 O SER A 202 ? O SER A 204 
AA2 12 13 N VAL A 201 ? N VAL A 203 O LYS B 211 ? O LYS B 213 
AA3 1  2  N LYS A 162 ? N LYS A 164 O ILE A 179 ? O ILE A 181 
AA4 1  2  N LYS A 211 ? N LYS A 213 O VAL C 201 ? O VAL C 203 
AA4 2  3  O SER C 202 ? O SER C 204 N VAL C 187 ? N VAL C 189 
AA4 3  4  O ALA C 188 ? O ALA C 190 N LEU C 173 ? N LEU C 175 
AA4 4  5  O ILE C 172 ? O ILE C 174 N TYR C 155 ? N TYR C 157 
AA4 5  6  O MET C 156 ? O MET C 158 N PHE C 136 ? N PHE C 138 
AA4 6  7  O ALA C 135 ? O ALA C 137 N PHE C 122 ? N PHE C 124 
AA4 7  8  O ALA C 121 ? O ALA C 123 N PHE C 108 ? N PHE C 110 
AA4 8  9  O ASN C 112 ? O ASN C 114 N ALA C 99  ? N ALA C 101 
AA4 9  10 O ALA C 100 ? O ALA C 102 N ILE C 85  ? N ILE C 87  
AA4 10 11 O ALA C 86  ? O ALA C 88  N ARG C 71  ? N ARG C 73  
AA4 11 12 O ALA C 72  ? O ALA C 74  N LYS C 57  ? N LYS C 59  
AA4 12 13 O ALA C 58  ? O ALA C 60  N VAL C 43  ? N VAL C 45  
AA5 1  2  N LYS C 28  ? N LYS C 30  O GLU C 37  ? O GLU C 39  
AA5 2  3  N ALA C 38  ? N ALA C 40  O ALA C 51  ? O ALA C 53  
AA5 3  4  N PHE C 52  ? N PHE C 54  O GLY C 67  ? O GLY C 69  
AA5 4  5  N PHE C 66  ? N PHE C 68  O GLY C 81  ? O GLY C 83  
AA5 5  6  N SER C 78  ? N SER C 80  O SER C 91  ? O SER C 93  
AA5 6  7  N SER C 96  ? N SER C 98  O LYS C 111 ? O LYS C 113 
AA5 7  8  N PHE C 108 ? N PHE C 110 O ALA C 121 ? O ALA C 123 
AA5 8  9  N GLN C 127 ? N GLN C 129 O ASN C 149 ? O ASN C 151 
AA6 1  2  N LYS B 28  ? N LYS B 30  O GLU B 37  ? O GLU B 39  
AA6 2  3  N ALA B 38  ? N ALA B 40  O ALA B 51  ? O ALA B 53  
AA6 3  4  N PHE B 52  ? N PHE B 54  O GLY B 67  ? O GLY B 69  
AA6 4  5  N THR B 68  ? N THR B 70  O GLY B 81  ? O GLY B 83  
AA6 5  6  N SER B 78  ? N SER B 80  O SER B 91  ? O SER B 93  
AA6 6  7  N SER B 96  ? N SER B 98  O LYS B 111 ? O LYS B 113 
AA6 7  8  N PHE B 108 ? N PHE B 110 O ALA B 121 ? O ALA B 123 
AA6 8  9  N GLN B 127 ? N GLN B 129 O ASN B 149 ? O ASN B 151 
AA7 1  2  N VAL B 43  ? N VAL B 45  O ALA B 58  ? O ALA B 60  
AA7 2  3  N LYS B 57  ? N LYS B 59  O ALA B 72  ? O ALA B 74  
AA7 3  4  N ARG B 71  ? N ARG B 73  O ALA B 86  ? O ALA B 88  
AA7 4  5  N ILE B 85  ? N ILE B 87  O ALA B 100 ? O ALA B 102 
AA7 5  6  N ALA B 99  ? N ALA B 101 O ASN B 112 ? O ASN B 114 
AA7 6  7  N PHE B 108 ? N PHE B 110 O ALA B 121 ? O ALA B 123 
AA7 7  8  N PHE B 122 ? N PHE B 124 O ALA B 135 ? O ALA B 137 
AA7 8  9  N PHE B 136 ? N PHE B 138 O MET B 156 ? O MET B 158 
AA7 9  10 N TYR B 155 ? N TYR B 157 O ILE B 172 ? O ILE B 174 
AA7 10 11 N LEU B 173 ? N LEU B 175 O ALA B 188 ? O ALA B 190 
AA7 11 12 N VAL B 187 ? N VAL B 189 O SER B 202 ? O SER B 204 
AA7 12 13 N VAL B 201 ? N VAL B 203 O LYS C 211 ? O LYS C 213 
AA8 1  2  N LYS B 162 ? N LYS B 164 O ILE B 179 ? O ILE B 181 
AA9 1  2  N LYS C 162 ? N LYS C 164 O ILE C 179 ? O ILE C 181 
AB1 1  2  N GLU D 5   ? N GLU D 39  O LEU D 20  ? O LEU D 54  
AB1 2  3  N LEU D 19  ? N LEU D 53  O LEU D 73  ? O LEU D 107 
AB1 3  4  O LEU D 74  ? O LEU D 108 N THR D 66  ? N THR D 100 
AB2 1  2  N VAL D 11  ? N VAL D 45  O HIS D 105 ? O HIS D 139 
AB2 2  3  O GLY D 102 ? O GLY D 136 N TYR D 86  ? N TYR D 120 
AB2 3  4  O ILE D 91  ? O ILE D 125 N PHE D 29  ? N PHE D 63  
AB2 4  5  N TRP D 33  ? N TRP D 67  O ILE D 45  ? O ILE D 79  
AB2 5  6  N ALA D 49  ? N ALA D 83  O GLN D 54  ? O GLN D 88  
AB3 1  2  N SER D 116 ? N SER D 150 O THR D 132 ? O THR D 166 
AB3 2  3  N PHE D 131 ? N PHE D 165 O LEU D 166 ? O LEU D 200 
AB3 3  4  O THR D 167 ? O THR D 201 N GLN D 158 ? N GLN D 192 
AB4 1  2  O GLN D 149 ? O GLN D 183 N ILE D 146 ? N ILE D 180 
AB4 2  3  N TRP D 145 ? N TRP D 179 O GLU D 180 ? O GLU D 214 
AB5 1  2  N GLU E 5   ? N GLU E 39  O LEU E 20  ? O LEU E 54  
AB5 2  3  N LEU E 19  ? N LEU E 53  O LEU E 73  ? O LEU E 107 
AB5 3  4  O LEU E 74  ? O LEU E 108 N THR E 66  ? N THR E 100 
AB6 1  2  N VAL E 11  ? N VAL E 45  O HIS E 105 ? O HIS E 139 
AB6 2  3  O GLY E 102 ? O GLY E 136 N TYR E 86  ? N TYR E 120 
AB6 3  4  O ILE E 91  ? O ILE E 125 N PHE E 29  ? N PHE E 63  
AB6 4  5  N TRP E 33  ? N TRP E 67  O ILE E 45  ? O ILE E 79  
AB6 5  6  N GLY E 47  ? N GLY E 81  O THR E 56  ? O THR E 90  
AB7 1  2  N SER E 116 ? N SER E 150 O THR E 132 ? O THR E 166 
AB7 2  3  N PHE E 131 ? N PHE E 165 O LEU E 166 ? O LEU E 200 
AB7 3  4  O THR E 167 ? O THR E 201 N GLN E 158 ? N GLN E 192 
AB8 1  2  O GLN E 149 ? O GLN E 183 N ILE E 146 ? N ILE E 180 
AB8 2  3  N TRP E 145 ? N TRP E 179 O GLU E 180 ? O GLU E 214 
AB8 3  4  N ILE E 183 ? N ILE E 217 O ASN E 190 ? O ASN E 224 
AB9 1  2  N GLU F 5   ? N GLU F 39  O LEU F 20  ? O LEU F 54  
AB9 2  3  N LEU F 19  ? N LEU F 53  O LEU F 73  ? O LEU F 107 
AB9 3  4  O LEU F 74  ? O LEU F 108 N THR F 66  ? N THR F 100 
AC1 1  2  N VAL F 11  ? N VAL F 45  O HIS F 105 ? O HIS F 139 
AC1 2  3  O GLY F 102 ? O GLY F 136 N TYR F 86  ? N TYR F 120 
AC1 3  4  O ILE F 91  ? O ILE F 125 N PHE F 29  ? N PHE F 63  
AC1 4  5  N TRP F 33  ? N TRP F 67  O ILE F 45  ? O ILE F 79  
AC1 5  6  N GLY F 47  ? N GLY F 81  O THR F 56  ? O THR F 90  
AC2 1  2  N SER F 116 ? N SER F 150 O THR F 132 ? O THR F 166 
AC2 2  3  N PHE F 131 ? N PHE F 165 O LEU F 166 ? O LEU F 200 
AC2 3  4  O THR F 165 ? O THR F 199 N SER F 160 ? N SER F 194 
AC3 1  2  O GLN F 149 ? O GLN F 183 N ILE F 146 ? N ILE F 180 
AC3 2  3  N THR F 141 ? N THR F 175 O GLN F 184 ? O GLN F 218 
AC3 3  4  N ILE F 183 ? N ILE F 217 O ASN F 190 ? O ASN F 224 
# 
_pdbx_entry_details.entry_id                   9GH5 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   F 
_pdbx_validate_close_contact.auth_comp_id_1   CYS 
_pdbx_validate_close_contact.auth_seq_id_1    167 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   NH1 
_pdbx_validate_close_contact.auth_asym_id_2   F 
_pdbx_validate_close_contact.auth_comp_id_2   ARG 
_pdbx_validate_close_contact.auth_seq_id_2    198 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.17 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 SER A 223 ? ? -171.32 -176.40 
2  1 ASP A 228 ? ? -127.72 -168.08 
3  1 SER B 223 ? ? -171.62 -176.76 
4  1 ASP B 228 ? ? -127.60 -168.48 
5  1 SER C 223 ? ? -170.82 -175.40 
6  1 ASP C 228 ? ? -127.71 -167.86 
7  1 ALA D 105 ? ? 76.50   -2.22   
8  1 ASN D 181 ? ? 35.80   42.10   
9  1 ASN D 197 ? ? -145.17 36.98   
10 1 ASN E 104 ? ? -83.57  44.55   
11 1 ALA E 105 ? ? 55.10   14.50   
12 1 ASN E 181 ? ? 37.69   40.56   
13 1 ASN E 182 ? ? 37.85   58.75   
14 1 ASN F 104 ? ? -89.81  31.89   
15 1 ALA F 105 ? ? 70.00   -3.41   
16 1 ASP F 173 ? ? 33.17   56.99   
17 1 ASN F 181 ? ? 33.70   46.33   
18 1 ASN F 197 ? ? -140.23 51.91   
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 ASN D 224 ? ? ARG D 225 ? ? -148.20 
2 1 ASN E 224 ? ? ARG E 225 ? ? -144.08 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9GH5 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         REAL 
_em_3d_fitting.ref_protocol      'FLEXIBLE FIT' 
# 
_em_3d_reconstruction.entry_id                    9GH5 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  2.7 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               211927 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          1 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            7.0 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'Hetero-hexameric complex of CbpF homotrimer with 3 CEACAM1 bound' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1,2 
# 
_em_imaging.entry_id                        9GH5 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             1200 
_em_imaging.nominal_defocus_max             2400 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           105000 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             'ZEMLIN TABLEAU' 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         NITROGEN 
# 
_em_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    COPPER 
_em_sample_support.grid_mesh_size   300 
_em_sample_support.grid_type        'Quantifoil R1.2/1.3' 
_em_sample_support.details          ? 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              9GH5 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9GH5 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
_em_single_particle_entity.entry_id              9GH5 
_em_single_particle_entity.id                    1 
_em_single_particle_entity.image_processing_id   1 
_em_single_particle_entity.point_symmetry        C3 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1    1 Y 1 A MET 3   ? A MET 1   
2    1 Y 1 A LYS 4   ? A LYS 2   
3    1 Y 1 A LYS 5   ? A LYS 3   
4    1 Y 1 A THR 6   ? A THR 4   
5    1 Y 1 A ALA 7   ? A ALA 5   
6    1 Y 1 A ILE 8   ? A ILE 6   
7    1 Y 1 A ALA 9   ? A ALA 7   
8    1 Y 1 A ILE 10  ? A ILE 8   
9    1 Y 1 A ALA 11  ? A ALA 9   
10   1 Y 1 A VAL 12  ? A VAL 10  
11   1 Y 1 A ALA 13  ? A ALA 11  
12   1 Y 1 A LEU 14  ? A LEU 12  
13   1 Y 1 A ALA 15  ? A ALA 13  
14   1 Y 1 A GLY 16  ? A GLY 14  
15   1 Y 1 A PHE 17  ? A PHE 15  
16   1 Y 1 A ALA 18  ? A ALA 16  
17   1 Y 1 A THR 19  ? A THR 17  
18   1 Y 1 A VAL 20  ? A VAL 18  
19   1 Y 1 A ALA 21  ? A ALA 19  
20   1 Y 1 A GLN 22  ? A GLN 20  
21   1 Y 1 A ALA 23  ? A ALA 21  
22   1 Y 1 A SER 24  ? A SER 22  
23   1 Y 1 A ALA 25  ? A ALA 23  
24   1 Y 1 A VAL 275 ? A VAL 273 
25   1 Y 1 A GLY 276 ? A GLY 274 
26   1 Y 1 A SER 277 ? A SER 275 
27   1 Y 1 A GLY 278 ? A GLY 276 
28   1 Y 1 A GLY 279 ? A GLY 277 
29   1 Y 1 A GLY 280 ? A GLY 278 
30   1 Y 1 A GLY 281 ? A GLY 279 
31   1 Y 1 A GLY 282 ? A GLY 280 
32   1 Y 1 A ALA 283 ? A ALA 281 
33   1 Y 1 A PRO 284 ? A PRO 282 
34   1 Y 1 A VAL 285 ? A VAL 283 
35   1 Y 1 A ASP 286 ? A ASP 284 
36   1 Y 1 A ALA 287 ? A ALA 285 
37   1 Y 1 A TYR 288 ? A TYR 286 
38   1 Y 1 A THR 289 ? A THR 287 
39   1 Y 1 A LYS 290 ? A LYS 288 
40   1 Y 1 A SER 291 ? A SER 289 
41   1 Y 1 A GLU 292 ? A GLU 290 
42   1 Y 1 A ALA 293 ? A ALA 291 
43   1 Y 1 A ASP 294 ? A ASP 292 
44   1 Y 1 A ASN 295 ? A ASN 293 
45   1 Y 1 A LYS 296 ? A LYS 294 
46   1 Y 1 A PHE 297 ? A PHE 295 
47   1 Y 1 A ALA 298 ? A ALA 296 
48   1 Y 1 A ASN 299 ? A ASN 297 
49   1 Y 1 A LYS 300 ? A LYS 298 
50   1 Y 1 A THR 301 ? A THR 299 
51   1 Y 1 A ASP 302 ? A ASP 300 
52   1 Y 1 A LEU 303 ? A LEU 301 
53   1 Y 1 A ASN 304 ? A ASN 302 
54   1 Y 1 A ASP 305 ? A ASP 303 
55   1 Y 1 A TYR 306 ? A TYR 304 
56   1 Y 1 A THR 307 ? A THR 305 
57   1 Y 1 A LYS 308 ? A LYS 306 
58   1 Y 1 A LYS 309 ? A LYS 307 
59   1 Y 1 A ASP 310 ? A ASP 308 
60   1 Y 1 A ASP 311 ? A ASP 309 
61   1 Y 1 A TYR 312 ? A TYR 310 
62   1 Y 1 A LYS 313 ? A LYS 311 
63   1 Y 1 A ASP 314 ? A ASP 312 
64   1 Y 1 A ALA 315 ? A ALA 313 
65   1 Y 1 A ASN 316 ? A ASN 314 
66   1 Y 1 A GLY 317 ? A GLY 315 
67   1 Y 1 A ILE 318 ? A ILE 316 
68   1 Y 1 A ASP 319 ? A ASP 317 
69   1 Y 1 A VAL 320 ? A VAL 318 
70   1 Y 1 A ASP 321 ? A ASP 319 
71   1 Y 1 A LYS 322 ? A LYS 320 
72   1 Y 1 A TRP 323 ? A TRP 321 
73   1 Y 1 A LYS 324 ? A LYS 322 
74   1 Y 1 A ALA 325 ? A ALA 323 
75   1 Y 1 A LYS 326 ? A LYS 324 
76   1 Y 1 A LEU 327 ? A LEU 325 
77   1 Y 1 A GLY 328 ? A GLY 326 
78   1 Y 1 A THR 329 ? A THR 327 
79   1 Y 1 A GLY 330 ? A GLY 328 
80   1 Y 1 A ALA 331 ? A ALA 329 
81   1 Y 1 A GLY 332 ? A GLY 330 
82   1 Y 1 A THR 333 ? A THR 331 
83   1 Y 1 A ALA 334 ? A ALA 332 
84   1 Y 1 A ASP 335 ? A ASP 333 
85   1 Y 1 A ILE 336 ? A ILE 334 
86   1 Y 1 A GLU 337 ? A GLU 335 
87   1 Y 1 A ASN 338 ? A ASN 336 
88   1 Y 1 A LEU 339 ? A LEU 337 
89   1 Y 1 A ARG 340 ? A ARG 338 
90   1 Y 1 A ASN 341 ? A ASN 339 
91   1 Y 1 A GLU 342 ? A GLU 340 
92   1 Y 1 A VAL 343 ? A VAL 341 
93   1 Y 1 A ASN 344 ? A ASN 342 
94   1 Y 1 A GLU 345 ? A GLU 343 
95   1 Y 1 A LYS 346 ? A LYS 344 
96   1 Y 1 A ILE 347 ? A ILE 345 
97   1 Y 1 A ASP 348 ? A ASP 346 
98   1 Y 1 A ASP 349 ? A ASP 347 
99   1 Y 1 A VAL 350 ? A VAL 348 
100  1 Y 1 A LYS 351 ? A LYS 349 
101  1 Y 1 A ASP 352 ? A ASP 350 
102  1 Y 1 A GLU 353 ? A GLU 351 
103  1 Y 1 A VAL 354 ? A VAL 352 
104  1 Y 1 A ARG 355 ? A ARG 353 
105  1 Y 1 A THR 356 ? A THR 354 
106  1 Y 1 A VAL 357 ? A VAL 355 
107  1 Y 1 A GLY 358 ? A GLY 356 
108  1 Y 1 A SER 359 ? A SER 357 
109  1 Y 1 A LEU 360 ? A LEU 358 
110  1 Y 1 A SER 361 ? A SER 359 
111  1 Y 1 A ALA 362 ? A ALA 360 
112  1 Y 1 A ALA 363 ? A ALA 361 
113  1 Y 1 A LEU 364 ? A LEU 362 
114  1 Y 1 A ALA 365 ? A ALA 363 
115  1 Y 1 A GLY 366 ? A GLY 364 
116  1 Y 1 A LEU 367 ? A LEU 365 
117  1 Y 1 A HIS 368 ? A HIS 366 
118  1 Y 1 A PRO 369 ? A PRO 367 
119  1 Y 1 A MET 370 ? A MET 368 
120  1 Y 1 A GLN 371 ? A GLN 369 
121  1 Y 1 A TYR 372 ? A TYR 370 
122  1 Y 1 A ASP 373 ? A ASP 371 
123  1 Y 1 A PRO 374 ? A PRO 372 
124  1 Y 1 A LYS 375 ? A LYS 373 
125  1 Y 1 A ALA 376 ? A ALA 374 
126  1 Y 1 A PRO 377 ? A PRO 375 
127  1 Y 1 A VAL 378 ? A VAL 376 
128  1 Y 1 A GLN 379 ? A GLN 377 
129  1 Y 1 A VAL 380 ? A VAL 378 
130  1 Y 1 A MET 381 ? A MET 379 
131  1 Y 1 A ALA 382 ? A ALA 380 
132  1 Y 1 A ALA 383 ? A ALA 381 
133  1 Y 1 A LEU 384 ? A LEU 382 
134  1 Y 1 A GLY 385 ? A GLY 383 
135  1 Y 1 A HIS 386 ? A HIS 384 
136  1 Y 1 A TYR 387 ? A TYR 385 
137  1 Y 1 A ARG 388 ? A ARG 386 
138  1 Y 1 A ASP 389 ? A ASP 387 
139  1 Y 1 A LYS 390 ? A LYS 388 
140  1 Y 1 A GLN 391 ? A GLN 389 
141  1 Y 1 A SER 392 ? A SER 390 
142  1 Y 1 A VAL 393 ? A VAL 391 
143  1 Y 1 A ALA 394 ? A ALA 392 
144  1 Y 1 A VAL 395 ? A VAL 393 
145  1 Y 1 A GLY 396 ? A GLY 394 
146  1 Y 1 A ALA 397 ? A ALA 395 
147  1 Y 1 A SER 398 ? A SER 396 
148  1 Y 1 A TYR 399 ? A TYR 397 
149  1 Y 1 A TYR 400 ? A TYR 398 
150  1 Y 1 A PHE 401 ? A PHE 399 
151  1 Y 1 A ASN 402 ? A ASN 400 
152  1 Y 1 A ASP 403 ? A ASP 401 
153  1 Y 1 A ARG 404 ? A ARG 402 
154  1 Y 1 A PHE 405 ? A PHE 403 
155  1 Y 1 A MET 406 ? A MET 404 
156  1 Y 1 A MET 407 ? A MET 405 
157  1 Y 1 A SER 408 ? A SER 406 
158  1 Y 1 A THR 409 ? A THR 407 
159  1 Y 1 A GLY 410 ? A GLY 408 
160  1 Y 1 A ILE 411 ? A ILE 409 
161  1 Y 1 A ALA 412 ? A ALA 410 
162  1 Y 1 A LEU 413 ? A LEU 411 
163  1 Y 1 A SER 414 ? A SER 412 
164  1 Y 1 A GLY 415 ? A GLY 413 
165  1 Y 1 A GLU 416 ? A GLU 414 
166  1 Y 1 A LYS 417 ? A LYS 415 
167  1 Y 1 A ARG 418 ? A ARG 416 
168  1 Y 1 A THR 419 ? A THR 417 
169  1 Y 1 A LYS 420 ? A LYS 418 
170  1 Y 1 A THR 421 ? A THR 419 
171  1 Y 1 A MET 422 ? A MET 420 
172  1 Y 1 A ALA 423 ? A ALA 421 
173  1 Y 1 A ASN 424 ? A ASN 422 
174  1 Y 1 A VAL 425 ? A VAL 423 
175  1 Y 1 A GLY 426 ? A GLY 424 
176  1 Y 1 A PHE 427 ? A PHE 425 
177  1 Y 1 A THR 428 ? A THR 426 
178  1 Y 1 A LEU 429 ? A LEU 427 
179  1 Y 1 A LYS 430 ? A LYS 428 
180  1 Y 1 A LEU 431 ? A LEU 429 
181  1 Y 1 A GLY 432 ? A GLY 430 
182  1 Y 1 A LYS 433 ? A LYS 431 
183  1 Y 1 A GLY 434 ? A GLY 432 
184  1 Y 1 A SER 435 ? A SER 433 
185  1 Y 1 A GLY 436 ? A GLY 434 
186  1 Y 1 A VAL 437 ? A VAL 435 
187  1 Y 1 A THR 438 ? A THR 436 
188  1 Y 1 A TYR 439 ? A TYR 437 
189  1 Y 1 A ASP 440 ? A ASP 438 
190  1 Y 1 A GLU 441 ? A GLU 439 
191  1 Y 1 A THR 442 ? A THR 440 
192  1 Y 1 A PRO 443 ? A PRO 441 
193  1 Y 1 A GLN 444 ? A GLN 442 
194  1 Y 1 A TYR 445 ? A TYR 443 
195  1 Y 1 A VAL 446 ? A VAL 444 
196  1 Y 1 A VAL 447 ? A VAL 445 
197  1 Y 1 A GLN 448 ? A GLN 446 
198  1 Y 1 A ASN 449 ? A ASN 447 
199  1 Y 1 A GLU 450 ? A GLU 448 
200  1 Y 1 A VAL 451 ? A VAL 449 
201  1 Y 1 A LYS 452 ? A LYS 450 
202  1 Y 1 A ARG 453 ? A ARG 451 
203  1 Y 1 A LEU 454 ? A LEU 452 
204  1 Y 1 A THR 455 ? A THR 453 
205  1 Y 1 A VAL 456 ? A VAL 454 
206  1 Y 1 A GLU 457 ? A GLU 455 
207  1 Y 1 A ASN 458 ? A ASN 456 
208  1 Y 1 A GLN 459 ? A GLN 457 
209  1 Y 1 A GLU 460 ? A GLU 458 
210  1 Y 1 A LEU 461 ? A LEU 459 
211  1 Y 1 A LYS 462 ? A LYS 460 
212  1 Y 1 A GLU 463 ? A GLU 461 
213  1 Y 1 A ARG 464 ? A ARG 462 
214  1 Y 1 A VAL 465 ? A VAL 463 
215  1 Y 1 A ARG 466 ? A ARG 464 
216  1 Y 1 A ASN 467 ? A ASN 465 
217  1 Y 1 A LEU 468 ? A LEU 466 
218  1 Y 1 A GLU 469 ? A GLU 467 
219  1 Y 1 A GLU 470 ? A GLU 468 
220  1 Y 1 A LYS 471 ? A LYS 469 
221  1 Y 1 A LEU 472 ? A LEU 470 
222  1 Y 1 A ASN 473 ? A ASN 471 
223  1 Y 1 A MET 474 ? A MET 472 
224  1 Y 1 A LEU 475 ? A LEU 473 
225  1 Y 1 A LEU 476 ? A LEU 474 
226  1 Y 1 A LYS 477 ? A LYS 475 
227  1 Y 1 A ASN 478 ? A ASN 476 
228  1 Y 1 A LYS 479 ? A LYS 477 
229  1 Y 1 A ARG 480 ? A ARG 478 
230  1 Y 1 A SER 481 ? A SER 479 
231  1 Y 1 A SER 482 ? A SER 480 
232  1 Y 1 A ALA 483 ? A ALA 481 
233  1 Y 1 A TRP 484 ? A TRP 482 
234  1 Y 1 A SER 485 ? A SER 483 
235  1 Y 1 A HIS 486 ? A HIS 484 
236  1 Y 1 A PRO 487 ? A PRO 485 
237  1 Y 1 A GLN 488 ? A GLN 486 
238  1 Y 1 A PHE 489 ? A PHE 487 
239  1 Y 1 A GLU 490 ? A GLU 488 
240  1 Y 1 A LYS 491 ? A LYS 489 
241  1 Y 1 B MET 3   ? B MET 1   
242  1 Y 1 B LYS 4   ? B LYS 2   
243  1 Y 1 B LYS 5   ? B LYS 3   
244  1 Y 1 B THR 6   ? B THR 4   
245  1 Y 1 B ALA 7   ? B ALA 5   
246  1 Y 1 B ILE 8   ? B ILE 6   
247  1 Y 1 B ALA 9   ? B ALA 7   
248  1 Y 1 B ILE 10  ? B ILE 8   
249  1 Y 1 B ALA 11  ? B ALA 9   
250  1 Y 1 B VAL 12  ? B VAL 10  
251  1 Y 1 B ALA 13  ? B ALA 11  
252  1 Y 1 B LEU 14  ? B LEU 12  
253  1 Y 1 B ALA 15  ? B ALA 13  
254  1 Y 1 B GLY 16  ? B GLY 14  
255  1 Y 1 B PHE 17  ? B PHE 15  
256  1 Y 1 B ALA 18  ? B ALA 16  
257  1 Y 1 B THR 19  ? B THR 17  
258  1 Y 1 B VAL 20  ? B VAL 18  
259  1 Y 1 B ALA 21  ? B ALA 19  
260  1 Y 1 B GLN 22  ? B GLN 20  
261  1 Y 1 B ALA 23  ? B ALA 21  
262  1 Y 1 B SER 24  ? B SER 22  
263  1 Y 1 B ALA 25  ? B ALA 23  
264  1 Y 1 B VAL 275 ? B VAL 273 
265  1 Y 1 B GLY 276 ? B GLY 274 
266  1 Y 1 B SER 277 ? B SER 275 
267  1 Y 1 B GLY 278 ? B GLY 276 
268  1 Y 1 B GLY 279 ? B GLY 277 
269  1 Y 1 B GLY 280 ? B GLY 278 
270  1 Y 1 B GLY 281 ? B GLY 279 
271  1 Y 1 B GLY 282 ? B GLY 280 
272  1 Y 1 B ALA 283 ? B ALA 281 
273  1 Y 1 B PRO 284 ? B PRO 282 
274  1 Y 1 B VAL 285 ? B VAL 283 
275  1 Y 1 B ASP 286 ? B ASP 284 
276  1 Y 1 B ALA 287 ? B ALA 285 
277  1 Y 1 B TYR 288 ? B TYR 286 
278  1 Y 1 B THR 289 ? B THR 287 
279  1 Y 1 B LYS 290 ? B LYS 288 
280  1 Y 1 B SER 291 ? B SER 289 
281  1 Y 1 B GLU 292 ? B GLU 290 
282  1 Y 1 B ALA 293 ? B ALA 291 
283  1 Y 1 B ASP 294 ? B ASP 292 
284  1 Y 1 B ASN 295 ? B ASN 293 
285  1 Y 1 B LYS 296 ? B LYS 294 
286  1 Y 1 B PHE 297 ? B PHE 295 
287  1 Y 1 B ALA 298 ? B ALA 296 
288  1 Y 1 B ASN 299 ? B ASN 297 
289  1 Y 1 B LYS 300 ? B LYS 298 
290  1 Y 1 B THR 301 ? B THR 299 
291  1 Y 1 B ASP 302 ? B ASP 300 
292  1 Y 1 B LEU 303 ? B LEU 301 
293  1 Y 1 B ASN 304 ? B ASN 302 
294  1 Y 1 B ASP 305 ? B ASP 303 
295  1 Y 1 B TYR 306 ? B TYR 304 
296  1 Y 1 B THR 307 ? B THR 305 
297  1 Y 1 B LYS 308 ? B LYS 306 
298  1 Y 1 B LYS 309 ? B LYS 307 
299  1 Y 1 B ASP 310 ? B ASP 308 
300  1 Y 1 B ASP 311 ? B ASP 309 
301  1 Y 1 B TYR 312 ? B TYR 310 
302  1 Y 1 B LYS 313 ? B LYS 311 
303  1 Y 1 B ASP 314 ? B ASP 312 
304  1 Y 1 B ALA 315 ? B ALA 313 
305  1 Y 1 B ASN 316 ? B ASN 314 
306  1 Y 1 B GLY 317 ? B GLY 315 
307  1 Y 1 B ILE 318 ? B ILE 316 
308  1 Y 1 B ASP 319 ? B ASP 317 
309  1 Y 1 B VAL 320 ? B VAL 318 
310  1 Y 1 B ASP 321 ? B ASP 319 
311  1 Y 1 B LYS 322 ? B LYS 320 
312  1 Y 1 B TRP 323 ? B TRP 321 
313  1 Y 1 B LYS 324 ? B LYS 322 
314  1 Y 1 B ALA 325 ? B ALA 323 
315  1 Y 1 B LYS 326 ? B LYS 324 
316  1 Y 1 B LEU 327 ? B LEU 325 
317  1 Y 1 B GLY 328 ? B GLY 326 
318  1 Y 1 B THR 329 ? B THR 327 
319  1 Y 1 B GLY 330 ? B GLY 328 
320  1 Y 1 B ALA 331 ? B ALA 329 
321  1 Y 1 B GLY 332 ? B GLY 330 
322  1 Y 1 B THR 333 ? B THR 331 
323  1 Y 1 B ALA 334 ? B ALA 332 
324  1 Y 1 B ASP 335 ? B ASP 333 
325  1 Y 1 B ILE 336 ? B ILE 334 
326  1 Y 1 B GLU 337 ? B GLU 335 
327  1 Y 1 B ASN 338 ? B ASN 336 
328  1 Y 1 B LEU 339 ? B LEU 337 
329  1 Y 1 B ARG 340 ? B ARG 338 
330  1 Y 1 B ASN 341 ? B ASN 339 
331  1 Y 1 B GLU 342 ? B GLU 340 
332  1 Y 1 B VAL 343 ? B VAL 341 
333  1 Y 1 B ASN 344 ? B ASN 342 
334  1 Y 1 B GLU 345 ? B GLU 343 
335  1 Y 1 B LYS 346 ? B LYS 344 
336  1 Y 1 B ILE 347 ? B ILE 345 
337  1 Y 1 B ASP 348 ? B ASP 346 
338  1 Y 1 B ASP 349 ? B ASP 347 
339  1 Y 1 B VAL 350 ? B VAL 348 
340  1 Y 1 B LYS 351 ? B LYS 349 
341  1 Y 1 B ASP 352 ? B ASP 350 
342  1 Y 1 B GLU 353 ? B GLU 351 
343  1 Y 1 B VAL 354 ? B VAL 352 
344  1 Y 1 B ARG 355 ? B ARG 353 
345  1 Y 1 B THR 356 ? B THR 354 
346  1 Y 1 B VAL 357 ? B VAL 355 
347  1 Y 1 B GLY 358 ? B GLY 356 
348  1 Y 1 B SER 359 ? B SER 357 
349  1 Y 1 B LEU 360 ? B LEU 358 
350  1 Y 1 B SER 361 ? B SER 359 
351  1 Y 1 B ALA 362 ? B ALA 360 
352  1 Y 1 B ALA 363 ? B ALA 361 
353  1 Y 1 B LEU 364 ? B LEU 362 
354  1 Y 1 B ALA 365 ? B ALA 363 
355  1 Y 1 B GLY 366 ? B GLY 364 
356  1 Y 1 B LEU 367 ? B LEU 365 
357  1 Y 1 B HIS 368 ? B HIS 366 
358  1 Y 1 B PRO 369 ? B PRO 367 
359  1 Y 1 B MET 370 ? B MET 368 
360  1 Y 1 B GLN 371 ? B GLN 369 
361  1 Y 1 B TYR 372 ? B TYR 370 
362  1 Y 1 B ASP 373 ? B ASP 371 
363  1 Y 1 B PRO 374 ? B PRO 372 
364  1 Y 1 B LYS 375 ? B LYS 373 
365  1 Y 1 B ALA 376 ? B ALA 374 
366  1 Y 1 B PRO 377 ? B PRO 375 
367  1 Y 1 B VAL 378 ? B VAL 376 
368  1 Y 1 B GLN 379 ? B GLN 377 
369  1 Y 1 B VAL 380 ? B VAL 378 
370  1 Y 1 B MET 381 ? B MET 379 
371  1 Y 1 B ALA 382 ? B ALA 380 
372  1 Y 1 B ALA 383 ? B ALA 381 
373  1 Y 1 B LEU 384 ? B LEU 382 
374  1 Y 1 B GLY 385 ? B GLY 383 
375  1 Y 1 B HIS 386 ? B HIS 384 
376  1 Y 1 B TYR 387 ? B TYR 385 
377  1 Y 1 B ARG 388 ? B ARG 386 
378  1 Y 1 B ASP 389 ? B ASP 387 
379  1 Y 1 B LYS 390 ? B LYS 388 
380  1 Y 1 B GLN 391 ? B GLN 389 
381  1 Y 1 B SER 392 ? B SER 390 
382  1 Y 1 B VAL 393 ? B VAL 391 
383  1 Y 1 B ALA 394 ? B ALA 392 
384  1 Y 1 B VAL 395 ? B VAL 393 
385  1 Y 1 B GLY 396 ? B GLY 394 
386  1 Y 1 B ALA 397 ? B ALA 395 
387  1 Y 1 B SER 398 ? B SER 396 
388  1 Y 1 B TYR 399 ? B TYR 397 
389  1 Y 1 B TYR 400 ? B TYR 398 
390  1 Y 1 B PHE 401 ? B PHE 399 
391  1 Y 1 B ASN 402 ? B ASN 400 
392  1 Y 1 B ASP 403 ? B ASP 401 
393  1 Y 1 B ARG 404 ? B ARG 402 
394  1 Y 1 B PHE 405 ? B PHE 403 
395  1 Y 1 B MET 406 ? B MET 404 
396  1 Y 1 B MET 407 ? B MET 405 
397  1 Y 1 B SER 408 ? B SER 406 
398  1 Y 1 B THR 409 ? B THR 407 
399  1 Y 1 B GLY 410 ? B GLY 408 
400  1 Y 1 B ILE 411 ? B ILE 409 
401  1 Y 1 B ALA 412 ? B ALA 410 
402  1 Y 1 B LEU 413 ? B LEU 411 
403  1 Y 1 B SER 414 ? B SER 412 
404  1 Y 1 B GLY 415 ? B GLY 413 
405  1 Y 1 B GLU 416 ? B GLU 414 
406  1 Y 1 B LYS 417 ? B LYS 415 
407  1 Y 1 B ARG 418 ? B ARG 416 
408  1 Y 1 B THR 419 ? B THR 417 
409  1 Y 1 B LYS 420 ? B LYS 418 
410  1 Y 1 B THR 421 ? B THR 419 
411  1 Y 1 B MET 422 ? B MET 420 
412  1 Y 1 B ALA 423 ? B ALA 421 
413  1 Y 1 B ASN 424 ? B ASN 422 
414  1 Y 1 B VAL 425 ? B VAL 423 
415  1 Y 1 B GLY 426 ? B GLY 424 
416  1 Y 1 B PHE 427 ? B PHE 425 
417  1 Y 1 B THR 428 ? B THR 426 
418  1 Y 1 B LEU 429 ? B LEU 427 
419  1 Y 1 B LYS 430 ? B LYS 428 
420  1 Y 1 B LEU 431 ? B LEU 429 
421  1 Y 1 B GLY 432 ? B GLY 430 
422  1 Y 1 B LYS 433 ? B LYS 431 
423  1 Y 1 B GLY 434 ? B GLY 432 
424  1 Y 1 B SER 435 ? B SER 433 
425  1 Y 1 B GLY 436 ? B GLY 434 
426  1 Y 1 B VAL 437 ? B VAL 435 
427  1 Y 1 B THR 438 ? B THR 436 
428  1 Y 1 B TYR 439 ? B TYR 437 
429  1 Y 1 B ASP 440 ? B ASP 438 
430  1 Y 1 B GLU 441 ? B GLU 439 
431  1 Y 1 B THR 442 ? B THR 440 
432  1 Y 1 B PRO 443 ? B PRO 441 
433  1 Y 1 B GLN 444 ? B GLN 442 
434  1 Y 1 B TYR 445 ? B TYR 443 
435  1 Y 1 B VAL 446 ? B VAL 444 
436  1 Y 1 B VAL 447 ? B VAL 445 
437  1 Y 1 B GLN 448 ? B GLN 446 
438  1 Y 1 B ASN 449 ? B ASN 447 
439  1 Y 1 B GLU 450 ? B GLU 448 
440  1 Y 1 B VAL 451 ? B VAL 449 
441  1 Y 1 B LYS 452 ? B LYS 450 
442  1 Y 1 B ARG 453 ? B ARG 451 
443  1 Y 1 B LEU 454 ? B LEU 452 
444  1 Y 1 B THR 455 ? B THR 453 
445  1 Y 1 B VAL 456 ? B VAL 454 
446  1 Y 1 B GLU 457 ? B GLU 455 
447  1 Y 1 B ASN 458 ? B ASN 456 
448  1 Y 1 B GLN 459 ? B GLN 457 
449  1 Y 1 B GLU 460 ? B GLU 458 
450  1 Y 1 B LEU 461 ? B LEU 459 
451  1 Y 1 B LYS 462 ? B LYS 460 
452  1 Y 1 B GLU 463 ? B GLU 461 
453  1 Y 1 B ARG 464 ? B ARG 462 
454  1 Y 1 B VAL 465 ? B VAL 463 
455  1 Y 1 B ARG 466 ? B ARG 464 
456  1 Y 1 B ASN 467 ? B ASN 465 
457  1 Y 1 B LEU 468 ? B LEU 466 
458  1 Y 1 B GLU 469 ? B GLU 467 
459  1 Y 1 B GLU 470 ? B GLU 468 
460  1 Y 1 B LYS 471 ? B LYS 469 
461  1 Y 1 B LEU 472 ? B LEU 470 
462  1 Y 1 B ASN 473 ? B ASN 471 
463  1 Y 1 B MET 474 ? B MET 472 
464  1 Y 1 B LEU 475 ? B LEU 473 
465  1 Y 1 B LEU 476 ? B LEU 474 
466  1 Y 1 B LYS 477 ? B LYS 475 
467  1 Y 1 B ASN 478 ? B ASN 476 
468  1 Y 1 B LYS 479 ? B LYS 477 
469  1 Y 1 B ARG 480 ? B ARG 478 
470  1 Y 1 B SER 481 ? B SER 479 
471  1 Y 1 B SER 482 ? B SER 480 
472  1 Y 1 B ALA 483 ? B ALA 481 
473  1 Y 1 B TRP 484 ? B TRP 482 
474  1 Y 1 B SER 485 ? B SER 483 
475  1 Y 1 B HIS 486 ? B HIS 484 
476  1 Y 1 B PRO 487 ? B PRO 485 
477  1 Y 1 B GLN 488 ? B GLN 486 
478  1 Y 1 B PHE 489 ? B PHE 487 
479  1 Y 1 B GLU 490 ? B GLU 488 
480  1 Y 1 B LYS 491 ? B LYS 489 
481  1 Y 1 C MET 3   ? C MET 1   
482  1 Y 1 C LYS 4   ? C LYS 2   
483  1 Y 1 C LYS 5   ? C LYS 3   
484  1 Y 1 C THR 6   ? C THR 4   
485  1 Y 1 C ALA 7   ? C ALA 5   
486  1 Y 1 C ILE 8   ? C ILE 6   
487  1 Y 1 C ALA 9   ? C ALA 7   
488  1 Y 1 C ILE 10  ? C ILE 8   
489  1 Y 1 C ALA 11  ? C ALA 9   
490  1 Y 1 C VAL 12  ? C VAL 10  
491  1 Y 1 C ALA 13  ? C ALA 11  
492  1 Y 1 C LEU 14  ? C LEU 12  
493  1 Y 1 C ALA 15  ? C ALA 13  
494  1 Y 1 C GLY 16  ? C GLY 14  
495  1 Y 1 C PHE 17  ? C PHE 15  
496  1 Y 1 C ALA 18  ? C ALA 16  
497  1 Y 1 C THR 19  ? C THR 17  
498  1 Y 1 C VAL 20  ? C VAL 18  
499  1 Y 1 C ALA 21  ? C ALA 19  
500  1 Y 1 C GLN 22  ? C GLN 20  
501  1 Y 1 C ALA 23  ? C ALA 21  
502  1 Y 1 C SER 24  ? C SER 22  
503  1 Y 1 C ALA 25  ? C ALA 23  
504  1 Y 1 C VAL 275 ? C VAL 273 
505  1 Y 1 C GLY 276 ? C GLY 274 
506  1 Y 1 C SER 277 ? C SER 275 
507  1 Y 1 C GLY 278 ? C GLY 276 
508  1 Y 1 C GLY 279 ? C GLY 277 
509  1 Y 1 C GLY 280 ? C GLY 278 
510  1 Y 1 C GLY 281 ? C GLY 279 
511  1 Y 1 C GLY 282 ? C GLY 280 
512  1 Y 1 C ALA 283 ? C ALA 281 
513  1 Y 1 C PRO 284 ? C PRO 282 
514  1 Y 1 C VAL 285 ? C VAL 283 
515  1 Y 1 C ASP 286 ? C ASP 284 
516  1 Y 1 C ALA 287 ? C ALA 285 
517  1 Y 1 C TYR 288 ? C TYR 286 
518  1 Y 1 C THR 289 ? C THR 287 
519  1 Y 1 C LYS 290 ? C LYS 288 
520  1 Y 1 C SER 291 ? C SER 289 
521  1 Y 1 C GLU 292 ? C GLU 290 
522  1 Y 1 C ALA 293 ? C ALA 291 
523  1 Y 1 C ASP 294 ? C ASP 292 
524  1 Y 1 C ASN 295 ? C ASN 293 
525  1 Y 1 C LYS 296 ? C LYS 294 
526  1 Y 1 C PHE 297 ? C PHE 295 
527  1 Y 1 C ALA 298 ? C ALA 296 
528  1 Y 1 C ASN 299 ? C ASN 297 
529  1 Y 1 C LYS 300 ? C LYS 298 
530  1 Y 1 C THR 301 ? C THR 299 
531  1 Y 1 C ASP 302 ? C ASP 300 
532  1 Y 1 C LEU 303 ? C LEU 301 
533  1 Y 1 C ASN 304 ? C ASN 302 
534  1 Y 1 C ASP 305 ? C ASP 303 
535  1 Y 1 C TYR 306 ? C TYR 304 
536  1 Y 1 C THR 307 ? C THR 305 
537  1 Y 1 C LYS 308 ? C LYS 306 
538  1 Y 1 C LYS 309 ? C LYS 307 
539  1 Y 1 C ASP 310 ? C ASP 308 
540  1 Y 1 C ASP 311 ? C ASP 309 
541  1 Y 1 C TYR 312 ? C TYR 310 
542  1 Y 1 C LYS 313 ? C LYS 311 
543  1 Y 1 C ASP 314 ? C ASP 312 
544  1 Y 1 C ALA 315 ? C ALA 313 
545  1 Y 1 C ASN 316 ? C ASN 314 
546  1 Y 1 C GLY 317 ? C GLY 315 
547  1 Y 1 C ILE 318 ? C ILE 316 
548  1 Y 1 C ASP 319 ? C ASP 317 
549  1 Y 1 C VAL 320 ? C VAL 318 
550  1 Y 1 C ASP 321 ? C ASP 319 
551  1 Y 1 C LYS 322 ? C LYS 320 
552  1 Y 1 C TRP 323 ? C TRP 321 
553  1 Y 1 C LYS 324 ? C LYS 322 
554  1 Y 1 C ALA 325 ? C ALA 323 
555  1 Y 1 C LYS 326 ? C LYS 324 
556  1 Y 1 C LEU 327 ? C LEU 325 
557  1 Y 1 C GLY 328 ? C GLY 326 
558  1 Y 1 C THR 329 ? C THR 327 
559  1 Y 1 C GLY 330 ? C GLY 328 
560  1 Y 1 C ALA 331 ? C ALA 329 
561  1 Y 1 C GLY 332 ? C GLY 330 
562  1 Y 1 C THR 333 ? C THR 331 
563  1 Y 1 C ALA 334 ? C ALA 332 
564  1 Y 1 C ASP 335 ? C ASP 333 
565  1 Y 1 C ILE 336 ? C ILE 334 
566  1 Y 1 C GLU 337 ? C GLU 335 
567  1 Y 1 C ASN 338 ? C ASN 336 
568  1 Y 1 C LEU 339 ? C LEU 337 
569  1 Y 1 C ARG 340 ? C ARG 338 
570  1 Y 1 C ASN 341 ? C ASN 339 
571  1 Y 1 C GLU 342 ? C GLU 340 
572  1 Y 1 C VAL 343 ? C VAL 341 
573  1 Y 1 C ASN 344 ? C ASN 342 
574  1 Y 1 C GLU 345 ? C GLU 343 
575  1 Y 1 C LYS 346 ? C LYS 344 
576  1 Y 1 C ILE 347 ? C ILE 345 
577  1 Y 1 C ASP 348 ? C ASP 346 
578  1 Y 1 C ASP 349 ? C ASP 347 
579  1 Y 1 C VAL 350 ? C VAL 348 
580  1 Y 1 C LYS 351 ? C LYS 349 
581  1 Y 1 C ASP 352 ? C ASP 350 
582  1 Y 1 C GLU 353 ? C GLU 351 
583  1 Y 1 C VAL 354 ? C VAL 352 
584  1 Y 1 C ARG 355 ? C ARG 353 
585  1 Y 1 C THR 356 ? C THR 354 
586  1 Y 1 C VAL 357 ? C VAL 355 
587  1 Y 1 C GLY 358 ? C GLY 356 
588  1 Y 1 C SER 359 ? C SER 357 
589  1 Y 1 C LEU 360 ? C LEU 358 
590  1 Y 1 C SER 361 ? C SER 359 
591  1 Y 1 C ALA 362 ? C ALA 360 
592  1 Y 1 C ALA 363 ? C ALA 361 
593  1 Y 1 C LEU 364 ? C LEU 362 
594  1 Y 1 C ALA 365 ? C ALA 363 
595  1 Y 1 C GLY 366 ? C GLY 364 
596  1 Y 1 C LEU 367 ? C LEU 365 
597  1 Y 1 C HIS 368 ? C HIS 366 
598  1 Y 1 C PRO 369 ? C PRO 367 
599  1 Y 1 C MET 370 ? C MET 368 
600  1 Y 1 C GLN 371 ? C GLN 369 
601  1 Y 1 C TYR 372 ? C TYR 370 
602  1 Y 1 C ASP 373 ? C ASP 371 
603  1 Y 1 C PRO 374 ? C PRO 372 
604  1 Y 1 C LYS 375 ? C LYS 373 
605  1 Y 1 C ALA 376 ? C ALA 374 
606  1 Y 1 C PRO 377 ? C PRO 375 
607  1 Y 1 C VAL 378 ? C VAL 376 
608  1 Y 1 C GLN 379 ? C GLN 377 
609  1 Y 1 C VAL 380 ? C VAL 378 
610  1 Y 1 C MET 381 ? C MET 379 
611  1 Y 1 C ALA 382 ? C ALA 380 
612  1 Y 1 C ALA 383 ? C ALA 381 
613  1 Y 1 C LEU 384 ? C LEU 382 
614  1 Y 1 C GLY 385 ? C GLY 383 
615  1 Y 1 C HIS 386 ? C HIS 384 
616  1 Y 1 C TYR 387 ? C TYR 385 
617  1 Y 1 C ARG 388 ? C ARG 386 
618  1 Y 1 C ASP 389 ? C ASP 387 
619  1 Y 1 C LYS 390 ? C LYS 388 
620  1 Y 1 C GLN 391 ? C GLN 389 
621  1 Y 1 C SER 392 ? C SER 390 
622  1 Y 1 C VAL 393 ? C VAL 391 
623  1 Y 1 C ALA 394 ? C ALA 392 
624  1 Y 1 C VAL 395 ? C VAL 393 
625  1 Y 1 C GLY 396 ? C GLY 394 
626  1 Y 1 C ALA 397 ? C ALA 395 
627  1 Y 1 C SER 398 ? C SER 396 
628  1 Y 1 C TYR 399 ? C TYR 397 
629  1 Y 1 C TYR 400 ? C TYR 398 
630  1 Y 1 C PHE 401 ? C PHE 399 
631  1 Y 1 C ASN 402 ? C ASN 400 
632  1 Y 1 C ASP 403 ? C ASP 401 
633  1 Y 1 C ARG 404 ? C ARG 402 
634  1 Y 1 C PHE 405 ? C PHE 403 
635  1 Y 1 C MET 406 ? C MET 404 
636  1 Y 1 C MET 407 ? C MET 405 
637  1 Y 1 C SER 408 ? C SER 406 
638  1 Y 1 C THR 409 ? C THR 407 
639  1 Y 1 C GLY 410 ? C GLY 408 
640  1 Y 1 C ILE 411 ? C ILE 409 
641  1 Y 1 C ALA 412 ? C ALA 410 
642  1 Y 1 C LEU 413 ? C LEU 411 
643  1 Y 1 C SER 414 ? C SER 412 
644  1 Y 1 C GLY 415 ? C GLY 413 
645  1 Y 1 C GLU 416 ? C GLU 414 
646  1 Y 1 C LYS 417 ? C LYS 415 
647  1 Y 1 C ARG 418 ? C ARG 416 
648  1 Y 1 C THR 419 ? C THR 417 
649  1 Y 1 C LYS 420 ? C LYS 418 
650  1 Y 1 C THR 421 ? C THR 419 
651  1 Y 1 C MET 422 ? C MET 420 
652  1 Y 1 C ALA 423 ? C ALA 421 
653  1 Y 1 C ASN 424 ? C ASN 422 
654  1 Y 1 C VAL 425 ? C VAL 423 
655  1 Y 1 C GLY 426 ? C GLY 424 
656  1 Y 1 C PHE 427 ? C PHE 425 
657  1 Y 1 C THR 428 ? C THR 426 
658  1 Y 1 C LEU 429 ? C LEU 427 
659  1 Y 1 C LYS 430 ? C LYS 428 
660  1 Y 1 C LEU 431 ? C LEU 429 
661  1 Y 1 C GLY 432 ? C GLY 430 
662  1 Y 1 C LYS 433 ? C LYS 431 
663  1 Y 1 C GLY 434 ? C GLY 432 
664  1 Y 1 C SER 435 ? C SER 433 
665  1 Y 1 C GLY 436 ? C GLY 434 
666  1 Y 1 C VAL 437 ? C VAL 435 
667  1 Y 1 C THR 438 ? C THR 436 
668  1 Y 1 C TYR 439 ? C TYR 437 
669  1 Y 1 C ASP 440 ? C ASP 438 
670  1 Y 1 C GLU 441 ? C GLU 439 
671  1 Y 1 C THR 442 ? C THR 440 
672  1 Y 1 C PRO 443 ? C PRO 441 
673  1 Y 1 C GLN 444 ? C GLN 442 
674  1 Y 1 C TYR 445 ? C TYR 443 
675  1 Y 1 C VAL 446 ? C VAL 444 
676  1 Y 1 C VAL 447 ? C VAL 445 
677  1 Y 1 C GLN 448 ? C GLN 446 
678  1 Y 1 C ASN 449 ? C ASN 447 
679  1 Y 1 C GLU 450 ? C GLU 448 
680  1 Y 1 C VAL 451 ? C VAL 449 
681  1 Y 1 C LYS 452 ? C LYS 450 
682  1 Y 1 C ARG 453 ? C ARG 451 
683  1 Y 1 C LEU 454 ? C LEU 452 
684  1 Y 1 C THR 455 ? C THR 453 
685  1 Y 1 C VAL 456 ? C VAL 454 
686  1 Y 1 C GLU 457 ? C GLU 455 
687  1 Y 1 C ASN 458 ? C ASN 456 
688  1 Y 1 C GLN 459 ? C GLN 457 
689  1 Y 1 C GLU 460 ? C GLU 458 
690  1 Y 1 C LEU 461 ? C LEU 459 
691  1 Y 1 C LYS 462 ? C LYS 460 
692  1 Y 1 C GLU 463 ? C GLU 461 
693  1 Y 1 C ARG 464 ? C ARG 462 
694  1 Y 1 C VAL 465 ? C VAL 463 
695  1 Y 1 C ARG 466 ? C ARG 464 
696  1 Y 1 C ASN 467 ? C ASN 465 
697  1 Y 1 C LEU 468 ? C LEU 466 
698  1 Y 1 C GLU 469 ? C GLU 467 
699  1 Y 1 C GLU 470 ? C GLU 468 
700  1 Y 1 C LYS 471 ? C LYS 469 
701  1 Y 1 C LEU 472 ? C LEU 470 
702  1 Y 1 C ASN 473 ? C ASN 471 
703  1 Y 1 C MET 474 ? C MET 472 
704  1 Y 1 C LEU 475 ? C LEU 473 
705  1 Y 1 C LEU 476 ? C LEU 474 
706  1 Y 1 C LYS 477 ? C LYS 475 
707  1 Y 1 C ASN 478 ? C ASN 476 
708  1 Y 1 C LYS 479 ? C LYS 477 
709  1 Y 1 C ARG 480 ? C ARG 478 
710  1 Y 1 C SER 481 ? C SER 479 
711  1 Y 1 C SER 482 ? C SER 480 
712  1 Y 1 C ALA 483 ? C ALA 481 
713  1 Y 1 C TRP 484 ? C TRP 482 
714  1 Y 1 C SER 485 ? C SER 483 
715  1 Y 1 C HIS 486 ? C HIS 484 
716  1 Y 1 C PRO 487 ? C PRO 485 
717  1 Y 1 C GLN 488 ? C GLN 486 
718  1 Y 1 C PHE 489 ? C PHE 487 
719  1 Y 1 C GLU 490 ? C GLU 488 
720  1 Y 1 C LYS 491 ? C LYS 489 
721  1 Y 1 D TYR 235 ? D TYR 201 
722  1 Y 1 D GLY 236 ? D GLY 202 
723  1 Y 1 D PRO 237 ? D PRO 203 
724  1 Y 1 D ASP 238 ? D ASP 204 
725  1 Y 1 D THR 239 ? D THR 205 
726  1 Y 1 D PRO 240 ? D PRO 206 
727  1 Y 1 D THR 241 ? D THR 207 
728  1 Y 1 D ILE 242 ? D ILE 208 
729  1 Y 1 D SER 243 ? D SER 209 
730  1 Y 1 D PRO 244 ? D PRO 210 
731  1 Y 1 D SER 245 ? D SER 211 
732  1 Y 1 D ASP 246 ? D ASP 212 
733  1 Y 1 D THR 247 ? D THR 213 
734  1 Y 1 D TYR 248 ? D TYR 214 
735  1 Y 1 D TYR 249 ? D TYR 215 
736  1 Y 1 D ARG 250 ? D ARG 216 
737  1 Y 1 D PRO 251 ? D PRO 217 
738  1 Y 1 D GLY 252 ? D GLY 218 
739  1 Y 1 D ALA 253 ? D ALA 219 
740  1 Y 1 D ASN 254 ? D ASN 220 
741  1 Y 1 D LEU 255 ? D LEU 221 
742  1 Y 1 D SER 256 ? D SER 222 
743  1 Y 1 D LEU 257 ? D LEU 223 
744  1 Y 1 D SER 258 ? D SER 224 
745  1 Y 1 D CYS 259 ? D CYS 225 
746  1 Y 1 D TYR 260 ? D TYR 226 
747  1 Y 1 D ALA 261 ? D ALA 227 
748  1 Y 1 D ALA 262 ? D ALA 228 
749  1 Y 1 D SER 263 ? D SER 229 
750  1 Y 1 D ASN 264 ? D ASN 230 
751  1 Y 1 D PRO 265 ? D PRO 231 
752  1 Y 1 D PRO 266 ? D PRO 232 
753  1 Y 1 D ALA 267 ? D ALA 233 
754  1 Y 1 D GLN 268 ? D GLN 234 
755  1 Y 1 D TYR 269 ? D TYR 235 
756  1 Y 1 D SER 270 ? D SER 236 
757  1 Y 1 D TRP 271 ? D TRP 237 
758  1 Y 1 D LEU 272 ? D LEU 238 
759  1 Y 1 D ILE 273 ? D ILE 239 
760  1 Y 1 D ASN 274 ? D ASN 240 
761  1 Y 1 D GLY 275 ? D GLY 241 
762  1 Y 1 D THR 276 ? D THR 242 
763  1 Y 1 D PHE 277 ? D PHE 243 
764  1 Y 1 D GLN 278 ? D GLN 244 
765  1 Y 1 D GLN 279 ? D GLN 245 
766  1 Y 1 D SER 280 ? D SER 246 
767  1 Y 1 D THR 281 ? D THR 247 
768  1 Y 1 D GLN 282 ? D GLN 248 
769  1 Y 1 D GLU 283 ? D GLU 249 
770  1 Y 1 D LEU 284 ? D LEU 250 
771  1 Y 1 D PHE 285 ? D PHE 251 
772  1 Y 1 D ILE 286 ? D ILE 252 
773  1 Y 1 D PRO 287 ? D PRO 253 
774  1 Y 1 D ASN 288 ? D ASN 254 
775  1 Y 1 D ILE 289 ? D ILE 255 
776  1 Y 1 D THR 290 ? D THR 256 
777  1 Y 1 D VAL 291 ? D VAL 257 
778  1 Y 1 D ASN 292 ? D ASN 258 
779  1 Y 1 D ASN 293 ? D ASN 259 
780  1 Y 1 D SER 294 ? D SER 260 
781  1 Y 1 D GLY 295 ? D GLY 261 
782  1 Y 1 D SER 296 ? D SER 262 
783  1 Y 1 D TYR 297 ? D TYR 263 
784  1 Y 1 D THR 298 ? D THR 264 
785  1 Y 1 D CYS 299 ? D CYS 265 
786  1 Y 1 D HIS 300 ? D HIS 266 
787  1 Y 1 D ALA 301 ? D ALA 267 
788  1 Y 1 D ASN 302 ? D ASN 268 
789  1 Y 1 D ASN 303 ? D ASN 269 
790  1 Y 1 D SER 304 ? D SER 270 
791  1 Y 1 D VAL 305 ? D VAL 271 
792  1 Y 1 D THR 306 ? D THR 272 
793  1 Y 1 D GLY 307 ? D GLY 273 
794  1 Y 1 D CYS 308 ? D CYS 274 
795  1 Y 1 D ASN 309 ? D ASN 275 
796  1 Y 1 D ARG 310 ? D ARG 276 
797  1 Y 1 D THR 311 ? D THR 277 
798  1 Y 1 D THR 312 ? D THR 278 
799  1 Y 1 D VAL 313 ? D VAL 279 
800  1 Y 1 D LYS 314 ? D LYS 280 
801  1 Y 1 D THR 315 ? D THR 281 
802  1 Y 1 D ILE 316 ? D ILE 282 
803  1 Y 1 D ILE 317 ? D ILE 283 
804  1 Y 1 D VAL 318 ? D VAL 284 
805  1 Y 1 D THR 319 ? D THR 285 
806  1 Y 1 D GLU 320 ? D GLU 286 
807  1 Y 1 D LEU 321 ? D LEU 287 
808  1 Y 1 D SER 322 ? D SER 288 
809  1 Y 1 D PRO 323 ? D PRO 289 
810  1 Y 1 D VAL 324 ? D VAL 290 
811  1 Y 1 D VAL 325 ? D VAL 291 
812  1 Y 1 D ALA 326 ? D ALA 292 
813  1 Y 1 D LYS 327 ? D LYS 293 
814  1 Y 1 D PRO 328 ? D PRO 294 
815  1 Y 1 D GLN 329 ? D GLN 295 
816  1 Y 1 D ILE 330 ? D ILE 296 
817  1 Y 1 D LYS 331 ? D LYS 297 
818  1 Y 1 D ALA 332 ? D ALA 298 
819  1 Y 1 D SER 333 ? D SER 299 
820  1 Y 1 D LYS 334 ? D LYS 300 
821  1 Y 1 D THR 335 ? D THR 301 
822  1 Y 1 D THR 336 ? D THR 302 
823  1 Y 1 D VAL 337 ? D VAL 303 
824  1 Y 1 D THR 338 ? D THR 304 
825  1 Y 1 D GLY 339 ? D GLY 305 
826  1 Y 1 D ASP 340 ? D ASP 306 
827  1 Y 1 D LYS 341 ? D LYS 307 
828  1 Y 1 D ASP 342 ? D ASP 308 
829  1 Y 1 D SER 343 ? D SER 309 
830  1 Y 1 D VAL 344 ? D VAL 310 
831  1 Y 1 D ASN 345 ? D ASN 311 
832  1 Y 1 D LEU 346 ? D LEU 312 
833  1 Y 1 D THR 347 ? D THR 313 
834  1 Y 1 D CYS 348 ? D CYS 314 
835  1 Y 1 D SER 349 ? D SER 315 
836  1 Y 1 D THR 350 ? D THR 316 
837  1 Y 1 D ASN 351 ? D ASN 317 
838  1 Y 1 D ASP 352 ? D ASP 318 
839  1 Y 1 D THR 353 ? D THR 319 
840  1 Y 1 D GLY 354 ? D GLY 320 
841  1 Y 1 D ILE 355 ? D ILE 321 
842  1 Y 1 D SER 356 ? D SER 322 
843  1 Y 1 D ILE 357 ? D ILE 323 
844  1 Y 1 D ARG 358 ? D ARG 324 
845  1 Y 1 D TRP 359 ? D TRP 325 
846  1 Y 1 D PHE 360 ? D PHE 326 
847  1 Y 1 D PHE 361 ? D PHE 327 
848  1 Y 1 D LYS 362 ? D LYS 328 
849  1 Y 1 D ASN 363 ? D ASN 329 
850  1 Y 1 D GLN 364 ? D GLN 330 
851  1 Y 1 D SER 365 ? D SER 331 
852  1 Y 1 D LEU 366 ? D LEU 332 
853  1 Y 1 D PRO 367 ? D PRO 333 
854  1 Y 1 D SER 368 ? D SER 334 
855  1 Y 1 D SER 369 ? D SER 335 
856  1 Y 1 D GLU 370 ? D GLU 336 
857  1 Y 1 D ARG 371 ? D ARG 337 
858  1 Y 1 D MET 372 ? D MET 338 
859  1 Y 1 D LYS 373 ? D LYS 339 
860  1 Y 1 D LEU 374 ? D LEU 340 
861  1 Y 1 D SER 375 ? D SER 341 
862  1 Y 1 D GLN 376 ? D GLN 342 
863  1 Y 1 D GLY 377 ? D GLY 343 
864  1 Y 1 D ASN 378 ? D ASN 344 
865  1 Y 1 D THR 379 ? D THR 345 
866  1 Y 1 D THR 380 ? D THR 346 
867  1 Y 1 D LEU 381 ? D LEU 347 
868  1 Y 1 D SER 382 ? D SER 348 
869  1 Y 1 D ILE 383 ? D ILE 349 
870  1 Y 1 D ASN 384 ? D ASN 350 
871  1 Y 1 D PRO 385 ? D PRO 351 
872  1 Y 1 D VAL 386 ? D VAL 352 
873  1 Y 1 D LYS 387 ? D LYS 353 
874  1 Y 1 D ARG 388 ? D ARG 354 
875  1 Y 1 D GLU 389 ? D GLU 355 
876  1 Y 1 D ASP 390 ? D ASP 356 
877  1 Y 1 D ALA 391 ? D ALA 357 
878  1 Y 1 D GLY 392 ? D GLY 358 
879  1 Y 1 D THR 393 ? D THR 359 
880  1 Y 1 D TYR 394 ? D TYR 360 
881  1 Y 1 D TRP 395 ? D TRP 361 
882  1 Y 1 D CYS 396 ? D CYS 362 
883  1 Y 1 D GLU 397 ? D GLU 363 
884  1 Y 1 D VAL 398 ? D VAL 364 
885  1 Y 1 D PHE 399 ? D PHE 365 
886  1 Y 1 D ASN 400 ? D ASN 366 
887  1 Y 1 D PRO 401 ? D PRO 367 
888  1 Y 1 D ILE 402 ? D ILE 368 
889  1 Y 1 D SER 403 ? D SER 369 
890  1 Y 1 D LYS 404 ? D LYS 370 
891  1 Y 1 D ASN 405 ? D ASN 371 
892  1 Y 1 D GLN 406 ? D GLN 372 
893  1 Y 1 D SER 407 ? D SER 373 
894  1 Y 1 D ASP 408 ? D ASP 374 
895  1 Y 1 D PRO 409 ? D PRO 375 
896  1 Y 1 D ILE 410 ? D ILE 376 
897  1 Y 1 D MET 411 ? D MET 377 
898  1 Y 1 D LEU 412 ? D LEU 378 
899  1 Y 1 D ASN 413 ? D ASN 379 
900  1 Y 1 D VAL 414 ? D VAL 380 
901  1 Y 1 D ASN 415 ? D ASN 381 
902  1 Y 1 D TYR 416 ? D TYR 382 
903  1 Y 1 D ASN 417 ? D ASN 383 
904  1 Y 1 D ALA 418 ? D ALA 384 
905  1 Y 1 D LEU 419 ? D LEU 385 
906  1 Y 1 D PRO 420 ? D PRO 386 
907  1 Y 1 D GLN 421 ? D GLN 387 
908  1 Y 1 D GLU 422 ? D GLU 388 
909  1 Y 1 D ASN 423 ? D ASN 389 
910  1 Y 1 D GLY 424 ? D GLY 390 
911  1 Y 1 D LEU 425 ? D LEU 391 
912  1 Y 1 D SER 426 ? D SER 392 
913  1 Y 1 D PRO 427 ? D PRO 393 
914  1 Y 1 D GLY 428 ? D GLY 394 
915  1 Y 1 D HIS 429 ? D HIS 395 
916  1 Y 1 D HIS 430 ? D HIS 396 
917  1 Y 1 D HIS 431 ? D HIS 397 
918  1 Y 1 D HIS 432 ? D HIS 398 
919  1 Y 1 D HIS 433 ? D HIS 399 
920  1 Y 1 D HIS 434 ? D HIS 400 
921  1 Y 1 E TYR 235 ? E TYR 201 
922  1 Y 1 E GLY 236 ? E GLY 202 
923  1 Y 1 E PRO 237 ? E PRO 203 
924  1 Y 1 E ASP 238 ? E ASP 204 
925  1 Y 1 E THR 239 ? E THR 205 
926  1 Y 1 E PRO 240 ? E PRO 206 
927  1 Y 1 E THR 241 ? E THR 207 
928  1 Y 1 E ILE 242 ? E ILE 208 
929  1 Y 1 E SER 243 ? E SER 209 
930  1 Y 1 E PRO 244 ? E PRO 210 
931  1 Y 1 E SER 245 ? E SER 211 
932  1 Y 1 E ASP 246 ? E ASP 212 
933  1 Y 1 E THR 247 ? E THR 213 
934  1 Y 1 E TYR 248 ? E TYR 214 
935  1 Y 1 E TYR 249 ? E TYR 215 
936  1 Y 1 E ARG 250 ? E ARG 216 
937  1 Y 1 E PRO 251 ? E PRO 217 
938  1 Y 1 E GLY 252 ? E GLY 218 
939  1 Y 1 E ALA 253 ? E ALA 219 
940  1 Y 1 E ASN 254 ? E ASN 220 
941  1 Y 1 E LEU 255 ? E LEU 221 
942  1 Y 1 E SER 256 ? E SER 222 
943  1 Y 1 E LEU 257 ? E LEU 223 
944  1 Y 1 E SER 258 ? E SER 224 
945  1 Y 1 E CYS 259 ? E CYS 225 
946  1 Y 1 E TYR 260 ? E TYR 226 
947  1 Y 1 E ALA 261 ? E ALA 227 
948  1 Y 1 E ALA 262 ? E ALA 228 
949  1 Y 1 E SER 263 ? E SER 229 
950  1 Y 1 E ASN 264 ? E ASN 230 
951  1 Y 1 E PRO 265 ? E PRO 231 
952  1 Y 1 E PRO 266 ? E PRO 232 
953  1 Y 1 E ALA 267 ? E ALA 233 
954  1 Y 1 E GLN 268 ? E GLN 234 
955  1 Y 1 E TYR 269 ? E TYR 235 
956  1 Y 1 E SER 270 ? E SER 236 
957  1 Y 1 E TRP 271 ? E TRP 237 
958  1 Y 1 E LEU 272 ? E LEU 238 
959  1 Y 1 E ILE 273 ? E ILE 239 
960  1 Y 1 E ASN 274 ? E ASN 240 
961  1 Y 1 E GLY 275 ? E GLY 241 
962  1 Y 1 E THR 276 ? E THR 242 
963  1 Y 1 E PHE 277 ? E PHE 243 
964  1 Y 1 E GLN 278 ? E GLN 244 
965  1 Y 1 E GLN 279 ? E GLN 245 
966  1 Y 1 E SER 280 ? E SER 246 
967  1 Y 1 E THR 281 ? E THR 247 
968  1 Y 1 E GLN 282 ? E GLN 248 
969  1 Y 1 E GLU 283 ? E GLU 249 
970  1 Y 1 E LEU 284 ? E LEU 250 
971  1 Y 1 E PHE 285 ? E PHE 251 
972  1 Y 1 E ILE 286 ? E ILE 252 
973  1 Y 1 E PRO 287 ? E PRO 253 
974  1 Y 1 E ASN 288 ? E ASN 254 
975  1 Y 1 E ILE 289 ? E ILE 255 
976  1 Y 1 E THR 290 ? E THR 256 
977  1 Y 1 E VAL 291 ? E VAL 257 
978  1 Y 1 E ASN 292 ? E ASN 258 
979  1 Y 1 E ASN 293 ? E ASN 259 
980  1 Y 1 E SER 294 ? E SER 260 
981  1 Y 1 E GLY 295 ? E GLY 261 
982  1 Y 1 E SER 296 ? E SER 262 
983  1 Y 1 E TYR 297 ? E TYR 263 
984  1 Y 1 E THR 298 ? E THR 264 
985  1 Y 1 E CYS 299 ? E CYS 265 
986  1 Y 1 E HIS 300 ? E HIS 266 
987  1 Y 1 E ALA 301 ? E ALA 267 
988  1 Y 1 E ASN 302 ? E ASN 268 
989  1 Y 1 E ASN 303 ? E ASN 269 
990  1 Y 1 E SER 304 ? E SER 270 
991  1 Y 1 E VAL 305 ? E VAL 271 
992  1 Y 1 E THR 306 ? E THR 272 
993  1 Y 1 E GLY 307 ? E GLY 273 
994  1 Y 1 E CYS 308 ? E CYS 274 
995  1 Y 1 E ASN 309 ? E ASN 275 
996  1 Y 1 E ARG 310 ? E ARG 276 
997  1 Y 1 E THR 311 ? E THR 277 
998  1 Y 1 E THR 312 ? E THR 278 
999  1 Y 1 E VAL 313 ? E VAL 279 
1000 1 Y 1 E LYS 314 ? E LYS 280 
1001 1 Y 1 E THR 315 ? E THR 281 
1002 1 Y 1 E ILE 316 ? E ILE 282 
1003 1 Y 1 E ILE 317 ? E ILE 283 
1004 1 Y 1 E VAL 318 ? E VAL 284 
1005 1 Y 1 E THR 319 ? E THR 285 
1006 1 Y 1 E GLU 320 ? E GLU 286 
1007 1 Y 1 E LEU 321 ? E LEU 287 
1008 1 Y 1 E SER 322 ? E SER 288 
1009 1 Y 1 E PRO 323 ? E PRO 289 
1010 1 Y 1 E VAL 324 ? E VAL 290 
1011 1 Y 1 E VAL 325 ? E VAL 291 
1012 1 Y 1 E ALA 326 ? E ALA 292 
1013 1 Y 1 E LYS 327 ? E LYS 293 
1014 1 Y 1 E PRO 328 ? E PRO 294 
1015 1 Y 1 E GLN 329 ? E GLN 295 
1016 1 Y 1 E ILE 330 ? E ILE 296 
1017 1 Y 1 E LYS 331 ? E LYS 297 
1018 1 Y 1 E ALA 332 ? E ALA 298 
1019 1 Y 1 E SER 333 ? E SER 299 
1020 1 Y 1 E LYS 334 ? E LYS 300 
1021 1 Y 1 E THR 335 ? E THR 301 
1022 1 Y 1 E THR 336 ? E THR 302 
1023 1 Y 1 E VAL 337 ? E VAL 303 
1024 1 Y 1 E THR 338 ? E THR 304 
1025 1 Y 1 E GLY 339 ? E GLY 305 
1026 1 Y 1 E ASP 340 ? E ASP 306 
1027 1 Y 1 E LYS 341 ? E LYS 307 
1028 1 Y 1 E ASP 342 ? E ASP 308 
1029 1 Y 1 E SER 343 ? E SER 309 
1030 1 Y 1 E VAL 344 ? E VAL 310 
1031 1 Y 1 E ASN 345 ? E ASN 311 
1032 1 Y 1 E LEU 346 ? E LEU 312 
1033 1 Y 1 E THR 347 ? E THR 313 
1034 1 Y 1 E CYS 348 ? E CYS 314 
1035 1 Y 1 E SER 349 ? E SER 315 
1036 1 Y 1 E THR 350 ? E THR 316 
1037 1 Y 1 E ASN 351 ? E ASN 317 
1038 1 Y 1 E ASP 352 ? E ASP 318 
1039 1 Y 1 E THR 353 ? E THR 319 
1040 1 Y 1 E GLY 354 ? E GLY 320 
1041 1 Y 1 E ILE 355 ? E ILE 321 
1042 1 Y 1 E SER 356 ? E SER 322 
1043 1 Y 1 E ILE 357 ? E ILE 323 
1044 1 Y 1 E ARG 358 ? E ARG 324 
1045 1 Y 1 E TRP 359 ? E TRP 325 
1046 1 Y 1 E PHE 360 ? E PHE 326 
1047 1 Y 1 E PHE 361 ? E PHE 327 
1048 1 Y 1 E LYS 362 ? E LYS 328 
1049 1 Y 1 E ASN 363 ? E ASN 329 
1050 1 Y 1 E GLN 364 ? E GLN 330 
1051 1 Y 1 E SER 365 ? E SER 331 
1052 1 Y 1 E LEU 366 ? E LEU 332 
1053 1 Y 1 E PRO 367 ? E PRO 333 
1054 1 Y 1 E SER 368 ? E SER 334 
1055 1 Y 1 E SER 369 ? E SER 335 
1056 1 Y 1 E GLU 370 ? E GLU 336 
1057 1 Y 1 E ARG 371 ? E ARG 337 
1058 1 Y 1 E MET 372 ? E MET 338 
1059 1 Y 1 E LYS 373 ? E LYS 339 
1060 1 Y 1 E LEU 374 ? E LEU 340 
1061 1 Y 1 E SER 375 ? E SER 341 
1062 1 Y 1 E GLN 376 ? E GLN 342 
1063 1 Y 1 E GLY 377 ? E GLY 343 
1064 1 Y 1 E ASN 378 ? E ASN 344 
1065 1 Y 1 E THR 379 ? E THR 345 
1066 1 Y 1 E THR 380 ? E THR 346 
1067 1 Y 1 E LEU 381 ? E LEU 347 
1068 1 Y 1 E SER 382 ? E SER 348 
1069 1 Y 1 E ILE 383 ? E ILE 349 
1070 1 Y 1 E ASN 384 ? E ASN 350 
1071 1 Y 1 E PRO 385 ? E PRO 351 
1072 1 Y 1 E VAL 386 ? E VAL 352 
1073 1 Y 1 E LYS 387 ? E LYS 353 
1074 1 Y 1 E ARG 388 ? E ARG 354 
1075 1 Y 1 E GLU 389 ? E GLU 355 
1076 1 Y 1 E ASP 390 ? E ASP 356 
1077 1 Y 1 E ALA 391 ? E ALA 357 
1078 1 Y 1 E GLY 392 ? E GLY 358 
1079 1 Y 1 E THR 393 ? E THR 359 
1080 1 Y 1 E TYR 394 ? E TYR 360 
1081 1 Y 1 E TRP 395 ? E TRP 361 
1082 1 Y 1 E CYS 396 ? E CYS 362 
1083 1 Y 1 E GLU 397 ? E GLU 363 
1084 1 Y 1 E VAL 398 ? E VAL 364 
1085 1 Y 1 E PHE 399 ? E PHE 365 
1086 1 Y 1 E ASN 400 ? E ASN 366 
1087 1 Y 1 E PRO 401 ? E PRO 367 
1088 1 Y 1 E ILE 402 ? E ILE 368 
1089 1 Y 1 E SER 403 ? E SER 369 
1090 1 Y 1 E LYS 404 ? E LYS 370 
1091 1 Y 1 E ASN 405 ? E ASN 371 
1092 1 Y 1 E GLN 406 ? E GLN 372 
1093 1 Y 1 E SER 407 ? E SER 373 
1094 1 Y 1 E ASP 408 ? E ASP 374 
1095 1 Y 1 E PRO 409 ? E PRO 375 
1096 1 Y 1 E ILE 410 ? E ILE 376 
1097 1 Y 1 E MET 411 ? E MET 377 
1098 1 Y 1 E LEU 412 ? E LEU 378 
1099 1 Y 1 E ASN 413 ? E ASN 379 
1100 1 Y 1 E VAL 414 ? E VAL 380 
1101 1 Y 1 E ASN 415 ? E ASN 381 
1102 1 Y 1 E TYR 416 ? E TYR 382 
1103 1 Y 1 E ASN 417 ? E ASN 383 
1104 1 Y 1 E ALA 418 ? E ALA 384 
1105 1 Y 1 E LEU 419 ? E LEU 385 
1106 1 Y 1 E PRO 420 ? E PRO 386 
1107 1 Y 1 E GLN 421 ? E GLN 387 
1108 1 Y 1 E GLU 422 ? E GLU 388 
1109 1 Y 1 E ASN 423 ? E ASN 389 
1110 1 Y 1 E GLY 424 ? E GLY 390 
1111 1 Y 1 E LEU 425 ? E LEU 391 
1112 1 Y 1 E SER 426 ? E SER 392 
1113 1 Y 1 E PRO 427 ? E PRO 393 
1114 1 Y 1 E GLY 428 ? E GLY 394 
1115 1 Y 1 E HIS 429 ? E HIS 395 
1116 1 Y 1 E HIS 430 ? E HIS 396 
1117 1 Y 1 E HIS 431 ? E HIS 397 
1118 1 Y 1 E HIS 432 ? E HIS 398 
1119 1 Y 1 E HIS 433 ? E HIS 399 
1120 1 Y 1 E HIS 434 ? E HIS 400 
1121 1 Y 1 F TYR 235 ? F TYR 201 
1122 1 Y 1 F GLY 236 ? F GLY 202 
1123 1 Y 1 F PRO 237 ? F PRO 203 
1124 1 Y 1 F ASP 238 ? F ASP 204 
1125 1 Y 1 F THR 239 ? F THR 205 
1126 1 Y 1 F PRO 240 ? F PRO 206 
1127 1 Y 1 F THR 241 ? F THR 207 
1128 1 Y 1 F ILE 242 ? F ILE 208 
1129 1 Y 1 F SER 243 ? F SER 209 
1130 1 Y 1 F PRO 244 ? F PRO 210 
1131 1 Y 1 F SER 245 ? F SER 211 
1132 1 Y 1 F ASP 246 ? F ASP 212 
1133 1 Y 1 F THR 247 ? F THR 213 
1134 1 Y 1 F TYR 248 ? F TYR 214 
1135 1 Y 1 F TYR 249 ? F TYR 215 
1136 1 Y 1 F ARG 250 ? F ARG 216 
1137 1 Y 1 F PRO 251 ? F PRO 217 
1138 1 Y 1 F GLY 252 ? F GLY 218 
1139 1 Y 1 F ALA 253 ? F ALA 219 
1140 1 Y 1 F ASN 254 ? F ASN 220 
1141 1 Y 1 F LEU 255 ? F LEU 221 
1142 1 Y 1 F SER 256 ? F SER 222 
1143 1 Y 1 F LEU 257 ? F LEU 223 
1144 1 Y 1 F SER 258 ? F SER 224 
1145 1 Y 1 F CYS 259 ? F CYS 225 
1146 1 Y 1 F TYR 260 ? F TYR 226 
1147 1 Y 1 F ALA 261 ? F ALA 227 
1148 1 Y 1 F ALA 262 ? F ALA 228 
1149 1 Y 1 F SER 263 ? F SER 229 
1150 1 Y 1 F ASN 264 ? F ASN 230 
1151 1 Y 1 F PRO 265 ? F PRO 231 
1152 1 Y 1 F PRO 266 ? F PRO 232 
1153 1 Y 1 F ALA 267 ? F ALA 233 
1154 1 Y 1 F GLN 268 ? F GLN 234 
1155 1 Y 1 F TYR 269 ? F TYR 235 
1156 1 Y 1 F SER 270 ? F SER 236 
1157 1 Y 1 F TRP 271 ? F TRP 237 
1158 1 Y 1 F LEU 272 ? F LEU 238 
1159 1 Y 1 F ILE 273 ? F ILE 239 
1160 1 Y 1 F ASN 274 ? F ASN 240 
1161 1 Y 1 F GLY 275 ? F GLY 241 
1162 1 Y 1 F THR 276 ? F THR 242 
1163 1 Y 1 F PHE 277 ? F PHE 243 
1164 1 Y 1 F GLN 278 ? F GLN 244 
1165 1 Y 1 F GLN 279 ? F GLN 245 
1166 1 Y 1 F SER 280 ? F SER 246 
1167 1 Y 1 F THR 281 ? F THR 247 
1168 1 Y 1 F GLN 282 ? F GLN 248 
1169 1 Y 1 F GLU 283 ? F GLU 249 
1170 1 Y 1 F LEU 284 ? F LEU 250 
1171 1 Y 1 F PHE 285 ? F PHE 251 
1172 1 Y 1 F ILE 286 ? F ILE 252 
1173 1 Y 1 F PRO 287 ? F PRO 253 
1174 1 Y 1 F ASN 288 ? F ASN 254 
1175 1 Y 1 F ILE 289 ? F ILE 255 
1176 1 Y 1 F THR 290 ? F THR 256 
1177 1 Y 1 F VAL 291 ? F VAL 257 
1178 1 Y 1 F ASN 292 ? F ASN 258 
1179 1 Y 1 F ASN 293 ? F ASN 259 
1180 1 Y 1 F SER 294 ? F SER 260 
1181 1 Y 1 F GLY 295 ? F GLY 261 
1182 1 Y 1 F SER 296 ? F SER 262 
1183 1 Y 1 F TYR 297 ? F TYR 263 
1184 1 Y 1 F THR 298 ? F THR 264 
1185 1 Y 1 F CYS 299 ? F CYS 265 
1186 1 Y 1 F HIS 300 ? F HIS 266 
1187 1 Y 1 F ALA 301 ? F ALA 267 
1188 1 Y 1 F ASN 302 ? F ASN 268 
1189 1 Y 1 F ASN 303 ? F ASN 269 
1190 1 Y 1 F SER 304 ? F SER 270 
1191 1 Y 1 F VAL 305 ? F VAL 271 
1192 1 Y 1 F THR 306 ? F THR 272 
1193 1 Y 1 F GLY 307 ? F GLY 273 
1194 1 Y 1 F CYS 308 ? F CYS 274 
1195 1 Y 1 F ASN 309 ? F ASN 275 
1196 1 Y 1 F ARG 310 ? F ARG 276 
1197 1 Y 1 F THR 311 ? F THR 277 
1198 1 Y 1 F THR 312 ? F THR 278 
1199 1 Y 1 F VAL 313 ? F VAL 279 
1200 1 Y 1 F LYS 314 ? F LYS 280 
1201 1 Y 1 F THR 315 ? F THR 281 
1202 1 Y 1 F ILE 316 ? F ILE 282 
1203 1 Y 1 F ILE 317 ? F ILE 283 
1204 1 Y 1 F VAL 318 ? F VAL 284 
1205 1 Y 1 F THR 319 ? F THR 285 
1206 1 Y 1 F GLU 320 ? F GLU 286 
1207 1 Y 1 F LEU 321 ? F LEU 287 
1208 1 Y 1 F SER 322 ? F SER 288 
1209 1 Y 1 F PRO 323 ? F PRO 289 
1210 1 Y 1 F VAL 324 ? F VAL 290 
1211 1 Y 1 F VAL 325 ? F VAL 291 
1212 1 Y 1 F ALA 326 ? F ALA 292 
1213 1 Y 1 F LYS 327 ? F LYS 293 
1214 1 Y 1 F PRO 328 ? F PRO 294 
1215 1 Y 1 F GLN 329 ? F GLN 295 
1216 1 Y 1 F ILE 330 ? F ILE 296 
1217 1 Y 1 F LYS 331 ? F LYS 297 
1218 1 Y 1 F ALA 332 ? F ALA 298 
1219 1 Y 1 F SER 333 ? F SER 299 
1220 1 Y 1 F LYS 334 ? F LYS 300 
1221 1 Y 1 F THR 335 ? F THR 301 
1222 1 Y 1 F THR 336 ? F THR 302 
1223 1 Y 1 F VAL 337 ? F VAL 303 
1224 1 Y 1 F THR 338 ? F THR 304 
1225 1 Y 1 F GLY 339 ? F GLY 305 
1226 1 Y 1 F ASP 340 ? F ASP 306 
1227 1 Y 1 F LYS 341 ? F LYS 307 
1228 1 Y 1 F ASP 342 ? F ASP 308 
1229 1 Y 1 F SER 343 ? F SER 309 
1230 1 Y 1 F VAL 344 ? F VAL 310 
1231 1 Y 1 F ASN 345 ? F ASN 311 
1232 1 Y 1 F LEU 346 ? F LEU 312 
1233 1 Y 1 F THR 347 ? F THR 313 
1234 1 Y 1 F CYS 348 ? F CYS 314 
1235 1 Y 1 F SER 349 ? F SER 315 
1236 1 Y 1 F THR 350 ? F THR 316 
1237 1 Y 1 F ASN 351 ? F ASN 317 
1238 1 Y 1 F ASP 352 ? F ASP 318 
1239 1 Y 1 F THR 353 ? F THR 319 
1240 1 Y 1 F GLY 354 ? F GLY 320 
1241 1 Y 1 F ILE 355 ? F ILE 321 
1242 1 Y 1 F SER 356 ? F SER 322 
1243 1 Y 1 F ILE 357 ? F ILE 323 
1244 1 Y 1 F ARG 358 ? F ARG 324 
1245 1 Y 1 F TRP 359 ? F TRP 325 
1246 1 Y 1 F PHE 360 ? F PHE 326 
1247 1 Y 1 F PHE 361 ? F PHE 327 
1248 1 Y 1 F LYS 362 ? F LYS 328 
1249 1 Y 1 F ASN 363 ? F ASN 329 
1250 1 Y 1 F GLN 364 ? F GLN 330 
1251 1 Y 1 F SER 365 ? F SER 331 
1252 1 Y 1 F LEU 366 ? F LEU 332 
1253 1 Y 1 F PRO 367 ? F PRO 333 
1254 1 Y 1 F SER 368 ? F SER 334 
1255 1 Y 1 F SER 369 ? F SER 335 
1256 1 Y 1 F GLU 370 ? F GLU 336 
1257 1 Y 1 F ARG 371 ? F ARG 337 
1258 1 Y 1 F MET 372 ? F MET 338 
1259 1 Y 1 F LYS 373 ? F LYS 339 
1260 1 Y 1 F LEU 374 ? F LEU 340 
1261 1 Y 1 F SER 375 ? F SER 341 
1262 1 Y 1 F GLN 376 ? F GLN 342 
1263 1 Y 1 F GLY 377 ? F GLY 343 
1264 1 Y 1 F ASN 378 ? F ASN 344 
1265 1 Y 1 F THR 379 ? F THR 345 
1266 1 Y 1 F THR 380 ? F THR 346 
1267 1 Y 1 F LEU 381 ? F LEU 347 
1268 1 Y 1 F SER 382 ? F SER 348 
1269 1 Y 1 F ILE 383 ? F ILE 349 
1270 1 Y 1 F ASN 384 ? F ASN 350 
1271 1 Y 1 F PRO 385 ? F PRO 351 
1272 1 Y 1 F VAL 386 ? F VAL 352 
1273 1 Y 1 F LYS 387 ? F LYS 353 
1274 1 Y 1 F ARG 388 ? F ARG 354 
1275 1 Y 1 F GLU 389 ? F GLU 355 
1276 1 Y 1 F ASP 390 ? F ASP 356 
1277 1 Y 1 F ALA 391 ? F ALA 357 
1278 1 Y 1 F GLY 392 ? F GLY 358 
1279 1 Y 1 F THR 393 ? F THR 359 
1280 1 Y 1 F TYR 394 ? F TYR 360 
1281 1 Y 1 F TRP 395 ? F TRP 361 
1282 1 Y 1 F CYS 396 ? F CYS 362 
1283 1 Y 1 F GLU 397 ? F GLU 363 
1284 1 Y 1 F VAL 398 ? F VAL 364 
1285 1 Y 1 F PHE 399 ? F PHE 365 
1286 1 Y 1 F ASN 400 ? F ASN 366 
1287 1 Y 1 F PRO 401 ? F PRO 367 
1288 1 Y 1 F ILE 402 ? F ILE 368 
1289 1 Y 1 F SER 403 ? F SER 369 
1290 1 Y 1 F LYS 404 ? F LYS 370 
1291 1 Y 1 F ASN 405 ? F ASN 371 
1292 1 Y 1 F GLN 406 ? F GLN 372 
1293 1 Y 1 F SER 407 ? F SER 373 
1294 1 Y 1 F ASP 408 ? F ASP 374 
1295 1 Y 1 F PRO 409 ? F PRO 375 
1296 1 Y 1 F ILE 410 ? F ILE 376 
1297 1 Y 1 F MET 411 ? F MET 377 
1298 1 Y 1 F LEU 412 ? F LEU 378 
1299 1 Y 1 F ASN 413 ? F ASN 379 
1300 1 Y 1 F VAL 414 ? F VAL 380 
1301 1 Y 1 F ASN 415 ? F ASN 381 
1302 1 Y 1 F TYR 416 ? F TYR 382 
1303 1 Y 1 F ASN 417 ? F ASN 383 
1304 1 Y 1 F ALA 418 ? F ALA 384 
1305 1 Y 1 F LEU 419 ? F LEU 385 
1306 1 Y 1 F PRO 420 ? F PRO 386 
1307 1 Y 1 F GLN 421 ? F GLN 387 
1308 1 Y 1 F GLU 422 ? F GLU 388 
1309 1 Y 1 F ASN 423 ? F ASN 389 
1310 1 Y 1 F GLY 424 ? F GLY 390 
1311 1 Y 1 F LEU 425 ? F LEU 391 
1312 1 Y 1 F SER 426 ? F SER 392 
1313 1 Y 1 F PRO 427 ? F PRO 393 
1314 1 Y 1 F GLY 428 ? F GLY 394 
1315 1 Y 1 F HIS 429 ? F HIS 395 
1316 1 Y 1 F HIS 430 ? F HIS 396 
1317 1 Y 1 F HIS 431 ? F HIS 397 
1318 1 Y 1 F HIS 432 ? F HIS 398 
1319 1 Y 1 F HIS 433 ? F HIS 399 
1320 1 Y 1 F HIS 434 ? F HIS 400 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
NAG C1   C N R 250 
NAG C2   C N R 251 
NAG C3   C N R 252 
NAG C4   C N S 253 
NAG C5   C N R 254 
NAG C6   C N N 255 
NAG C7   C N N 256 
NAG C8   C N N 257 
NAG N2   N N N 258 
NAG O1   O N N 259 
NAG O3   O N N 260 
NAG O4   O N N 261 
NAG O5   O N N 262 
NAG O6   O N N 263 
NAG O7   O N N 264 
NAG H1   H N N 265 
NAG H2   H N N 266 
NAG H3   H N N 267 
NAG H4   H N N 268 
NAG H5   H N N 269 
NAG H61  H N N 270 
NAG H62  H N N 271 
NAG H81  H N N 272 
NAG H82  H N N 273 
NAG H83  H N N 274 
NAG HN2  H N N 275 
NAG HO1  H N N 276 
NAG HO3  H N N 277 
NAG HO4  H N N 278 
NAG HO6  H N N 279 
PHE N    N N N 280 
PHE CA   C N S 281 
PHE C    C N N 282 
PHE O    O N N 283 
PHE CB   C N N 284 
PHE CG   C Y N 285 
PHE CD1  C Y N 286 
PHE CD2  C Y N 287 
PHE CE1  C Y N 288 
PHE CE2  C Y N 289 
PHE CZ   C Y N 290 
PHE OXT  O N N 291 
PHE H    H N N 292 
PHE H2   H N N 293 
PHE HA   H N N 294 
PHE HB2  H N N 295 
PHE HB3  H N N 296 
PHE HD1  H N N 297 
PHE HD2  H N N 298 
PHE HE1  H N N 299 
PHE HE2  H N N 300 
PHE HZ   H N N 301 
PHE HXT  H N N 302 
PRO N    N N N 303 
PRO CA   C N S 304 
PRO C    C N N 305 
PRO O    O N N 306 
PRO CB   C N N 307 
PRO CG   C N N 308 
PRO CD   C N N 309 
PRO OXT  O N N 310 
PRO H    H N N 311 
PRO HA   H N N 312 
PRO HB2  H N N 313 
PRO HB3  H N N 314 
PRO HG2  H N N 315 
PRO HG3  H N N 316 
PRO HD2  H N N 317 
PRO HD3  H N N 318 
PRO HXT  H N N 319 
SER N    N N N 320 
SER CA   C N S 321 
SER C    C N N 322 
SER O    O N N 323 
SER CB   C N N 324 
SER OG   O N N 325 
SER OXT  O N N 326 
SER H    H N N 327 
SER H2   H N N 328 
SER HA   H N N 329 
SER HB2  H N N 330 
SER HB3  H N N 331 
SER HG   H N N 332 
SER HXT  H N N 333 
THR N    N N N 334 
THR CA   C N S 335 
THR C    C N N 336 
THR O    O N N 337 
THR CB   C N R 338 
THR OG1  O N N 339 
THR CG2  C N N 340 
THR OXT  O N N 341 
THR H    H N N 342 
THR H2   H N N 343 
THR HA   H N N 344 
THR HB   H N N 345 
THR HG1  H N N 346 
THR HG21 H N N 347 
THR HG22 H N N 348 
THR HG23 H N N 349 
THR HXT  H N N 350 
TRP N    N N N 351 
TRP CA   C N S 352 
TRP C    C N N 353 
TRP O    O N N 354 
TRP CB   C N N 355 
TRP CG   C Y N 356 
TRP CD1  C Y N 357 
TRP CD2  C Y N 358 
TRP NE1  N Y N 359 
TRP CE2  C Y N 360 
TRP CE3  C Y N 361 
TRP CZ2  C Y N 362 
TRP CZ3  C Y N 363 
TRP CH2  C Y N 364 
TRP OXT  O N N 365 
TRP H    H N N 366 
TRP H2   H N N 367 
TRP HA   H N N 368 
TRP HB2  H N N 369 
TRP HB3  H N N 370 
TRP HD1  H N N 371 
TRP HE1  H N N 372 
TRP HE3  H N N 373 
TRP HZ2  H N N 374 
TRP HZ3  H N N 375 
TRP HH2  H N N 376 
TRP HXT  H N N 377 
TYR N    N N N 378 
TYR CA   C N S 379 
TYR C    C N N 380 
TYR O    O N N 381 
TYR CB   C N N 382 
TYR CG   C Y N 383 
TYR CD1  C Y N 384 
TYR CD2  C Y N 385 
TYR CE1  C Y N 386 
TYR CE2  C Y N 387 
TYR CZ   C Y N 388 
TYR OH   O N N 389 
TYR OXT  O N N 390 
TYR H    H N N 391 
TYR H2   H N N 392 
TYR HA   H N N 393 
TYR HB2  H N N 394 
TYR HB3  H N N 395 
TYR HD1  H N N 396 
TYR HD2  H N N 397 
TYR HE1  H N N 398 
TYR HE2  H N N 399 
TYR HH   H N N 400 
TYR HXT  H N N 401 
VAL N    N N N 402 
VAL CA   C N S 403 
VAL C    C N N 404 
VAL O    O N N 405 
VAL CB   C N N 406 
VAL CG1  C N N 407 
VAL CG2  C N N 408 
VAL OXT  O N N 409 
VAL H    H N N 410 
VAL H2   H N N 411 
VAL HA   H N N 412 
VAL HB   H N N 413 
VAL HG11 H N N 414 
VAL HG12 H N N 415 
VAL HG13 H N N 416 
VAL HG21 H N N 417 
VAL HG22 H N N 418 
VAL HG23 H N N 419 
VAL HXT  H N N 420 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
NAG C1  C2   sing N N 237 
NAG C1  O1   sing N N 238 
NAG C1  O5   sing N N 239 
NAG C1  H1   sing N N 240 
NAG C2  C3   sing N N 241 
NAG C2  N2   sing N N 242 
NAG C2  H2   sing N N 243 
NAG C3  C4   sing N N 244 
NAG C3  O3   sing N N 245 
NAG C3  H3   sing N N 246 
NAG C4  C5   sing N N 247 
NAG C4  O4   sing N N 248 
NAG C4  H4   sing N N 249 
NAG C5  C6   sing N N 250 
NAG C5  O5   sing N N 251 
NAG C5  H5   sing N N 252 
NAG C6  O6   sing N N 253 
NAG C6  H61  sing N N 254 
NAG C6  H62  sing N N 255 
NAG C7  C8   sing N N 256 
NAG C7  N2   sing N N 257 
NAG C7  O7   doub N N 258 
NAG C8  H81  sing N N 259 
NAG C8  H82  sing N N 260 
NAG C8  H83  sing N N 261 
NAG N2  HN2  sing N N 262 
NAG O1  HO1  sing N N 263 
NAG O3  HO3  sing N N 264 
NAG O4  HO4  sing N N 265 
NAG O6  HO6  sing N N 266 
PHE N   CA   sing N N 267 
PHE N   H    sing N N 268 
PHE N   H2   sing N N 269 
PHE CA  C    sing N N 270 
PHE CA  CB   sing N N 271 
PHE CA  HA   sing N N 272 
PHE C   O    doub N N 273 
PHE C   OXT  sing N N 274 
PHE CB  CG   sing N N 275 
PHE CB  HB2  sing N N 276 
PHE CB  HB3  sing N N 277 
PHE CG  CD1  doub Y N 278 
PHE CG  CD2  sing Y N 279 
PHE CD1 CE1  sing Y N 280 
PHE CD1 HD1  sing N N 281 
PHE CD2 CE2  doub Y N 282 
PHE CD2 HD2  sing N N 283 
PHE CE1 CZ   doub Y N 284 
PHE CE1 HE1  sing N N 285 
PHE CE2 CZ   sing Y N 286 
PHE CE2 HE2  sing N N 287 
PHE CZ  HZ   sing N N 288 
PHE OXT HXT  sing N N 289 
PRO N   CA   sing N N 290 
PRO N   CD   sing N N 291 
PRO N   H    sing N N 292 
PRO CA  C    sing N N 293 
PRO CA  CB   sing N N 294 
PRO CA  HA   sing N N 295 
PRO C   O    doub N N 296 
PRO C   OXT  sing N N 297 
PRO CB  CG   sing N N 298 
PRO CB  HB2  sing N N 299 
PRO CB  HB3  sing N N 300 
PRO CG  CD   sing N N 301 
PRO CG  HG2  sing N N 302 
PRO CG  HG3  sing N N 303 
PRO CD  HD2  sing N N 304 
PRO CD  HD3  sing N N 305 
PRO OXT HXT  sing N N 306 
SER N   CA   sing N N 307 
SER N   H    sing N N 308 
SER N   H2   sing N N 309 
SER CA  C    sing N N 310 
SER CA  CB   sing N N 311 
SER CA  HA   sing N N 312 
SER C   O    doub N N 313 
SER C   OXT  sing N N 314 
SER CB  OG   sing N N 315 
SER CB  HB2  sing N N 316 
SER CB  HB3  sing N N 317 
SER OG  HG   sing N N 318 
SER OXT HXT  sing N N 319 
THR N   CA   sing N N 320 
THR N   H    sing N N 321 
THR N   H2   sing N N 322 
THR CA  C    sing N N 323 
THR CA  CB   sing N N 324 
THR CA  HA   sing N N 325 
THR C   O    doub N N 326 
THR C   OXT  sing N N 327 
THR CB  OG1  sing N N 328 
THR CB  CG2  sing N N 329 
THR CB  HB   sing N N 330 
THR OG1 HG1  sing N N 331 
THR CG2 HG21 sing N N 332 
THR CG2 HG22 sing N N 333 
THR CG2 HG23 sing N N 334 
THR OXT HXT  sing N N 335 
TRP N   CA   sing N N 336 
TRP N   H    sing N N 337 
TRP N   H2   sing N N 338 
TRP CA  C    sing N N 339 
TRP CA  CB   sing N N 340 
TRP CA  HA   sing N N 341 
TRP C   O    doub N N 342 
TRP C   OXT  sing N N 343 
TRP CB  CG   sing N N 344 
TRP CB  HB2  sing N N 345 
TRP CB  HB3  sing N N 346 
TRP CG  CD1  doub Y N 347 
TRP CG  CD2  sing Y N 348 
TRP CD1 NE1  sing Y N 349 
TRP CD1 HD1  sing N N 350 
TRP CD2 CE2  doub Y N 351 
TRP CD2 CE3  sing Y N 352 
TRP NE1 CE2  sing Y N 353 
TRP NE1 HE1  sing N N 354 
TRP CE2 CZ2  sing Y N 355 
TRP CE3 CZ3  doub Y N 356 
TRP CE3 HE3  sing N N 357 
TRP CZ2 CH2  doub Y N 358 
TRP CZ2 HZ2  sing N N 359 
TRP CZ3 CH2  sing Y N 360 
TRP CZ3 HZ3  sing N N 361 
TRP CH2 HH2  sing N N 362 
TRP OXT HXT  sing N N 363 
TYR N   CA   sing N N 364 
TYR N   H    sing N N 365 
TYR N   H2   sing N N 366 
TYR CA  C    sing N N 367 
TYR CA  CB   sing N N 368 
TYR CA  HA   sing N N 369 
TYR C   O    doub N N 370 
TYR C   OXT  sing N N 371 
TYR CB  CG   sing N N 372 
TYR CB  HB2  sing N N 373 
TYR CB  HB3  sing N N 374 
TYR CG  CD1  doub Y N 375 
TYR CG  CD2  sing Y N 376 
TYR CD1 CE1  sing Y N 377 
TYR CD1 HD1  sing N N 378 
TYR CD2 CE2  doub Y N 379 
TYR CD2 HD2  sing N N 380 
TYR CE1 CZ   doub Y N 381 
TYR CE1 HE1  sing N N 382 
TYR CE2 CZ   sing Y N 383 
TYR CE2 HE2  sing N N 384 
TYR CZ  OH   sing N N 385 
TYR OH  HH   sing N N 386 
TYR OXT HXT  sing N N 387 
VAL N   CA   sing N N 388 
VAL N   H    sing N N 389 
VAL N   H2   sing N N 390 
VAL CA  C    sing N N 391 
VAL CA  CB   sing N N 392 
VAL CA  HA   sing N N 393 
VAL C   O    doub N N 394 
VAL C   OXT  sing N N 395 
VAL CB  CG1  sing N N 396 
VAL CB  CG2  sing N N 397 
VAL CB  HB   sing N N 398 
VAL CG1 HG11 sing N N 399 
VAL CG1 HG12 sing N N 400 
VAL CG1 HG13 sing N N 401 
VAL CG2 HG21 sing N N 402 
VAL CG2 HG22 sing N N 403 
VAL CG2 HG23 sing N N 404 
VAL OXT HXT  sing N N 405 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-08-15 
_em_admin.deposition_site    PDBE 
_em_admin.entry_id           9GH5 
_em_admin.last_update        2025-04-23 
_em_admin.map_release_date   2025-04-02 
_em_admin.title              'Complex of Fusobacterium nucleatum CbpF with human CEACAM1' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    NO 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                MEGADALTONS 
_em_entity_assembly_molwt.value                0.35 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          851 
_em_entity_assembly_naturalsource.organism             'Fusobacterium nucleatum' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          562 
_em_entity_assembly_recombinant.organism             'Escherichia coli' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         52.8 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 BIOQUANTUM (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    1 
_em_image_recording.num_real_images                     6334 
# 
_em_imaging_optics.chr_aberration_corrector   ? 
_em_imaging_optics.energyfilter_lower         ? 
_em_imaging_optics.energyfilter_slit_width    20 
_em_imaging_optics.energyfilter_name          'GIF Bioquantum' 
_em_imaging_optics.energyfilter_upper         ? 
_em_imaging_optics.id                         1 
_em_imaging_optics.imaging_id                 1 
_em_imaging_optics.phase_plate                ? 
_em_imaging_optics.sph_aberration_corrector   ? 
_em_imaging_optics.details                    ? 
# 
_em_particle_selection.details                  ? 
_em_particle_selection.id                       1 
_em_particle_selection.image_processing_id      1 
_em_particle_selection.method                   ? 
_em_particle_selection.num_particles_selected   1766853 
_em_particle_selection.reference_model          ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'       ? 1  1 ? ? cryoSPARC 4.4.0     
'IMAGE ACQUISITION'        ? 2  ? ? 1 EPU       2.12      
MASKING                    ? 3  ? ? ? ?         ?         
'CTF CORRECTION'           ? 4  1 ? ? cryoSPARC 4.4.0     
'LAYERLINE INDEXING'       ? 5  ? ? ? ?         ?         
'DIFFRACTION INDEXING'     ? 6  ? ? ? ?         ?         
'MODEL FITTING'            ? 7  ? 1 ? Coot      ?         
OTHER                      ? 8  ? ? ? ?         ?         
'INITIAL EULER ASSIGNMENT' ? 9  1 ? ? cryoSPARC 4.4.0     
'FINAL EULER ASSIGNMENT'   ? 10 1 ? ? cryoSPARC 4.4.0     
CLASSIFICATION             ? 11 1 ? ? cryoSPARC 4.4.0     
RECONSTRUCTION             ? 12 1 ? ? cryoSPARC 4.4.0     
'MODEL REFINEMENT'         ? 13 ? 1 ? PHENIX    1.21-5207 
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   'Leibniz Association' 
_pdbx_audit_support.country                Germany 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9GH5 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N N   . ALA A  1 24  ? 155.324 148.268 127.233 1.00 111.26 ? 26  ALA A N   1 
ATOM   2     C CA  . ALA A  1 24  ? 156.481 149.077 127.595 1.00 113.43 ? 26  ALA A CA  1 
ATOM   3     C C   . ALA A  1 24  ? 156.056 150.322 128.363 1.00 114.88 ? 26  ALA A C   1 
ATOM   4     O O   . ALA A  1 24  ? 154.984 150.872 128.113 1.00 115.50 ? 26  ALA A O   1 
ATOM   5     C CB  . ALA A  1 24  ? 157.269 149.462 126.352 1.00 108.63 ? 26  ALA A CB  1 
ATOM   6     N N   . PRO A  1 25  ? 156.890 150.756 129.306 1.00 110.48 ? 27  PRO A N   1 
ATOM   7     C CA  . PRO A  1 25  ? 156.580 151.976 130.059 1.00 107.81 ? 27  PRO A CA  1 
ATOM   8     C C   . PRO A  1 25  ? 156.473 153.179 129.136 1.00 108.83 ? 27  PRO A C   1 
ATOM   9     O O   . PRO A  1 25  ? 157.167 153.273 128.122 1.00 105.65 ? 27  PRO A O   1 
ATOM   10    C CB  . PRO A  1 25  ? 157.767 152.107 131.016 1.00 105.91 ? 27  PRO A CB  1 
ATOM   11    C CG  . PRO A  1 25  ? 158.245 150.711 131.198 1.00 105.69 ? 27  PRO A CG  1 
ATOM   12    C CD  . PRO A  1 25  ? 158.060 150.055 129.858 1.00 109.08 ? 27  PRO A CD  1 
ATOM   13    N N   . VAL A  1 26  ? 155.586 154.104 129.495 1.00 107.62 ? 28  VAL A N   1 
ATOM   14    C CA  . VAL A  1 26  ? 155.323 155.283 128.684 1.00 105.71 ? 28  VAL A CA  1 
ATOM   15    C C   . VAL A  1 26  ? 155.122 156.484 129.596 1.00 104.20 ? 28  VAL A C   1 
ATOM   16    O O   . VAL A  1 26  ? 154.755 156.348 130.767 1.00 103.24 ? 28  VAL A O   1 
ATOM   17    C CB  . VAL A  1 26  ? 154.097 155.072 127.765 1.00 101.90 ? 28  VAL A CB  1 
ATOM   18    C CG1 . VAL A  1 26  ? 152.805 155.202 128.556 1.00 93.89  ? 28  VAL A CG1 1 
ATOM   19    C CG2 . VAL A  1 26  ? 154.123 156.041 126.592 1.00 102.02 ? 28  VAL A CG2 1 
ATOM   20    N N   . ILE A  1 27  ? 155.382 157.669 129.050 1.00 101.00 ? 29  ILE A N   1 
ATOM   21    C CA  . ILE A  1 27  ? 155.073 158.939 129.696 1.00 97.15  ? 29  ILE A CA  1 
ATOM   22    C C   . ILE A  1 27  ? 153.931 159.585 128.921 1.00 100.17 ? 29  ILE A C   1 
ATOM   23    O O   . ILE A  1 27  ? 153.979 159.677 127.688 1.00 105.13 ? 29  ILE A O   1 
ATOM   24    C CB  . ILE A  1 27  ? 156.312 159.854 129.782 1.00 93.05  ? 29  ILE A CB  1 
ATOM   25    C CG1 . ILE A  1 27  ? 156.096 160.979 130.796 1.00 91.77  ? 29  ILE A CG1 1 
ATOM   26    C CG2 . ILE A  1 27  ? 156.737 160.393 128.420 1.00 95.70  ? 29  ILE A CG2 1 
ATOM   27    C CD1 . ILE A  1 27  ? 156.686 160.703 132.150 1.00 88.01  ? 29  ILE A CD1 1 
ATOM   28    N N   . LYS A  1 28  ? 152.878 159.972 129.634 1.00 95.73  ? 30  LYS A N   1 
ATOM   29    C CA  . LYS A  1 28  ? 151.689 160.488 128.973 1.00 94.28  ? 30  LYS A CA  1 
ATOM   30    C C   . LYS A  1 28  ? 150.877 161.303 129.966 1.00 99.79  ? 30  LYS A C   1 
ATOM   31    O O   . LYS A  1 28  ? 151.058 161.200 131.181 1.00 98.17  ? 30  LYS A O   1 
ATOM   32    C CB  . LYS A  1 28  ? 150.837 159.357 128.389 1.00 95.86  ? 30  LYS A CB  1 
ATOM   33    C CG  . LYS A  1 28  ? 150.150 158.501 129.437 1.00 103.26 ? 30  LYS A CG  1 
ATOM   34    C CD  . LYS A  1 28  ? 149.741 157.155 128.867 1.00 103.77 ? 30  LYS A CD  1 
ATOM   35    C CE  . LYS A  1 28  ? 148.390 157.235 128.181 1.00 109.50 ? 30  LYS A CE  1 
ATOM   36    N NZ  . LYS A  1 28  ? 147.485 158.206 128.852 1.00 113.12 ? 30  LYS A NZ  1 
ATOM   37    N N   . ALA A  1 29  ? 149.977 162.115 129.424 1.00 102.62 ? 31  ALA A N   1 
ATOM   38    C CA  . ALA A  1 29  ? 149.085 162.916 130.245 1.00 103.43 ? 31  ALA A CA  1 
ATOM   39    C C   . ALA A  1 29  ? 147.973 162.054 130.828 1.00 102.79 ? 31  ALA A C   1 
ATOM   40    O O   . ALA A  1 29  ? 147.545 161.063 130.231 1.00 105.24 ? 31  ALA A O   1 
ATOM   41    C CB  . ALA A  1 29  ? 148.482 164.059 129.429 1.00 100.66 ? 31  ALA A CB  1 
ATOM   42    N N   . GLY A  1 30  ? 147.507 162.444 132.010 1.00 101.90 ? 32  GLY A N   1 
ATOM   43    C CA  . GLY A  1 30  ? 146.387 161.768 132.632 1.00 103.27 ? 32  GLY A CA  1 
ATOM   44    C C   . GLY A  1 30  ? 145.064 162.221 132.052 1.00 107.78 ? 32  GLY A C   1 
ATOM   45    O O   . GLY A  1 30  ? 145.000 162.645 130.894 1.00 106.72 ? 32  GLY A O   1 
ATOM   46    N N   . THR A  1 31  ? 143.998 162.140 132.845 1.00 110.55 ? 33  THR A N   1 
ATOM   47    C CA  . THR A  1 31  ? 142.675 162.562 132.411 1.00 111.01 ? 33  THR A CA  1 
ATOM   48    C C   . THR A  1 31  ? 142.342 163.986 132.829 1.00 113.54 ? 33  THR A C   1 
ATOM   49    O O   . THR A  1 31  ? 141.217 164.439 132.592 1.00 115.65 ? 33  THR A O   1 
ATOM   50    C CB  . THR A  1 31  ? 141.609 161.605 132.953 1.00 109.91 ? 33  THR A CB  1 
ATOM   51    O OG1 . THR A  1 31  ? 141.931 161.244 134.302 1.00 110.61 ? 33  THR A OG1 1 
ATOM   52    C CG2 . THR A  1 31  ? 141.545 160.348 132.101 1.00 109.24 ? 33  THR A CG2 1 
ATOM   53    N N   . ALA A  1 32  ? 143.281 164.702 133.441 1.00 115.46 ? 34  ALA A N   1 
ATOM   54    C CA  . ALA A  1 32  ? 143.067 166.066 133.894 1.00 113.61 ? 34  ALA A CA  1 
ATOM   55    C C   . ALA A  1 32  ? 144.223 166.941 133.430 1.00 113.00 ? 34  ALA A C   1 
ATOM   56    O O   . ALA A  1 32  ? 145.259 166.452 132.973 1.00 116.12 ? 34  ALA A O   1 
ATOM   57    C CB  . ALA A  1 32  ? 142.922 166.136 135.419 1.00 105.82 ? 34  ALA A CB  1 
ATOM   58    N N   . THR A  1 33  ? 144.027 168.252 133.544 1.00 110.07 ? 35  THR A N   1 
ATOM   59    C CA  . THR A  1 33  ? 145.050 169.202 133.130 1.00 113.35 ? 35  THR A CA  1 
ATOM   60    C C   . THR A  1 33  ? 146.308 169.043 133.974 1.00 114.62 ? 35  THR A C   1 
ATOM   61    O O   . THR A  1 33  ? 146.239 168.962 135.204 1.00 114.37 ? 35  THR A O   1 
ATOM   62    C CB  . THR A  1 33  ? 144.518 170.630 133.243 1.00 114.65 ? 35  THR A CB  1 
ATOM   63    O OG1 . THR A  1 33  ? 143.229 170.711 132.624 1.00 119.39 ? 35  THR A OG1 1 
ATOM   64    C CG2 . THR A  1 33  ? 145.462 171.605 132.560 1.00 113.03 ? 35  THR A CG2 1 
ATOM   65    N N   . ASP A  1 34  ? 147.459 168.997 133.301 1.00 112.40 ? 36  ASP A N   1 
ATOM   66    C CA  . ASP A  1 34  ? 148.764 168.893 133.956 1.00 109.36 ? 36  ASP A CA  1 
ATOM   67    C C   . ASP A  1 34  ? 148.855 167.650 134.838 1.00 108.86 ? 36  ASP A C   1 
ATOM   68    O O   . ASP A  1 34  ? 149.466 167.668 135.908 1.00 109.80 ? 36  ASP A O   1 
ATOM   69    C CB  . ASP A  1 34  ? 149.079 170.155 134.762 1.00 113.37 ? 36  ASP A CB  1 
ATOM   70    C CG  . ASP A  1 34  ? 149.284 171.369 133.882 1.00 123.03 ? 36  ASP A CG  1 
ATOM   71    O OD1 . ASP A  1 34  ? 149.175 171.233 132.646 1.00 118.52 ? 36  ASP A OD1 1 
ATOM   72    O OD2 . ASP A  1 34  ? 149.550 172.461 134.426 1.00 129.71 ? 36  ASP A OD2 1 
ATOM   73    N N   . SER A  1 35  ? 148.253 166.557 134.383 1.00 105.68 ? 37  SER A N   1 
ATOM   74    C CA  . SER A  1 35  ? 148.316 165.280 135.080 1.00 99.52  ? 37  SER A CA  1 
ATOM   75    C C   . SER A  1 35  ? 149.272 164.357 134.337 1.00 101.07 ? 37  SER A C   1 
ATOM   76    O O   . SER A  1 35  ? 149.203 164.245 133.110 1.00 106.77 ? 37  SER A O   1 
ATOM   77    C CB  . SER A  1 35  ? 146.931 164.644 135.189 1.00 102.31 ? 37  SER A CB  1 
ATOM   78    O OG  . SER A  1 35  ? 146.264 164.662 133.941 1.00 115.30 ? 37  SER A OG  1 
ATOM   79    N N   . THR A  1 36  ? 150.157 163.701 135.081 1.00 98.19  ? 38  THR A N   1 
ATOM   80    C CA  . THR A  1 36  ? 151.246 162.920 134.509 1.00 96.71  ? 38  THR A CA  1 
ATOM   81    C C   . THR A  1 36  ? 151.118 161.461 134.918 1.00 99.49  ? 38  THR A C   1 
ATOM   82    O O   . THR A  1 36  ? 150.835 161.160 136.082 1.00 102.66 ? 38  THR A O   1 
ATOM   83    C CB  . THR A  1 36  ? 152.603 163.468 134.957 1.00 97.13  ? 38  THR A CB  1 
ATOM   84    O OG1 . THR A  1 36  ? 152.658 164.877 134.705 1.00 104.58 ? 38  THR A OG1 1 
ATOM   85    C CG2 . THR A  1 36  ? 153.734 162.776 134.216 1.00 97.88  ? 38  THR A CG2 1 
ATOM   86    N N   . GLU A  1 37  ? 151.328 160.562 133.960 1.00 96.25  ? 39  GLU A N   1 
ATOM   87    C CA  . GLU A  1 37  ? 151.414 159.130 134.214 1.00 93.54  ? 39  GLU A CA  1 
ATOM   88    C C   . GLU A  1 37  ? 152.749 158.633 133.684 1.00 98.69  ? 39  GLU A C   1 
ATOM   89    O O   . GLU A  1 37  ? 153.005 158.701 132.477 1.00 103.11 ? 39  GLU A O   1 
ATOM   90    C CB  . GLU A  1 37  ? 150.259 158.378 133.551 1.00 96.00  ? 39  GLU A CB  1 
ATOM   91    C CG  . GLU A  1 37  ? 148.929 158.530 134.261 1.00 102.82 ? 39  GLU A CG  1 
ATOM   92    C CD  . GLU A  1 37  ? 147.773 158.012 133.434 1.00 110.55 ? 39  GLU A CD  1 
ATOM   93    O OE1 . GLU A  1 37  ? 148.026 157.324 132.424 1.00 111.13 ? 39  GLU A OE1 1 
ATOM   94    O OE2 . GLU A  1 37  ? 146.610 158.294 133.791 1.00 108.14 ? 39  GLU A OE2 1 
ATOM   95    N N   . ALA A  1 38  ? 153.596 158.137 134.582 1.00 97.52  ? 40  ALA A N   1 
ATOM   96    C CA  . ALA A  1 38  ? 154.921 157.645 134.224 1.00 90.68  ? 40  ALA A CA  1 
ATOM   97    C C   . ALA A  1 38  ? 155.041 156.200 134.675 1.00 95.12  ? 40  ALA A C   1 
ATOM   98    O O   . ALA A  1 38  ? 154.896 155.905 135.865 1.00 98.51  ? 40  ALA A O   1 
ATOM   99    C CB  . ALA A  1 38  ? 156.020 158.496 134.861 1.00 87.07  ? 40  ALA A CB  1 
ATOM   100   N N   . GLY A  1 39  ? 155.308 155.306 133.730 1.00 92.47  ? 41  GLY A N   1 
ATOM   101   C CA  . GLY A  1 39  ? 155.417 153.900 134.052 1.00 96.25  ? 41  GLY A CA  1 
ATOM   102   C C   . GLY A  1 39  ? 154.426 153.052 133.287 1.00 103.19 ? 41  GLY A C   1 
ATOM   103   O O   . GLY A  1 39  ? 154.062 153.378 132.154 1.00 108.11 ? 41  GLY A O   1 
ATOM   104   N N   . VAL A  1 40  ? 153.977 151.962 133.901 1.00 103.09 ? 42  VAL A N   1 
ATOM   105   C CA  . VAL A  1 40  ? 153.065 151.015 133.273 1.00 106.49 ? 42  VAL A CA  1 
ATOM   106   C C   . VAL A  1 40  ? 151.819 150.893 134.137 1.00 107.59 ? 42  VAL A C   1 
ATOM   107   O O   . VAL A  1 40  ? 151.918 150.690 135.353 1.00 107.36 ? 42  VAL A O   1 
ATOM   108   C CB  . VAL A  1 40  ? 153.736 149.644 133.065 1.00 102.03 ? 42  VAL A CB  1 
ATOM   109   C CG1 . VAL A  1 40  ? 154.615 149.299 134.254 1.00 97.14  ? 42  VAL A CG1 1 
ATOM   110   C CG2 . VAL A  1 40  ? 152.693 148.565 132.840 1.00 105.52 ? 42  VAL A CG2 1 
ATOM   111   N N   . ASP A  1 41  ? 150.650 151.038 133.508 1.00 109.29 ? 43  ASP A N   1 
ATOM   112   C CA  . ASP A  1 41  ? 149.352 150.844 134.155 1.00 111.27 ? 43  ASP A CA  1 
ATOM   113   C C   . ASP A  1 41  ? 149.138 151.847 135.291 1.00 110.90 ? 43  ASP A C   1 
ATOM   114   O O   . ASP A  1 41  ? 148.794 151.488 136.417 1.00 108.95 ? 43  ASP A O   1 
ATOM   115   C CB  . ASP A  1 41  ? 149.204 149.404 134.658 1.00 118.34 ? 43  ASP A CB  1 
ATOM   116   C CG  . ASP A  1 41  ? 149.135 148.397 133.529 1.00 128.87 ? 43  ASP A CG  1 
ATOM   117   O OD1 . ASP A  1 41  ? 149.476 148.760 132.384 1.00 132.49 ? 43  ASP A OD1 1 
ATOM   118   O OD2 . ASP A  1 41  ? 148.747 147.238 133.788 1.00 125.47 ? 43  ASP A OD2 1 
ATOM   119   N N   . ASN A  1 42  ? 149.330 153.121 134.971 1.00 105.17 ? 44  ASN A N   1 
ATOM   120   C CA  . ASN A  1 42  ? 149.125 154.202 135.921 1.00 96.71  ? 44  ASN A CA  1 
ATOM   121   C C   . ASN A  1 42  ? 147.855 154.970 135.578 1.00 99.52  ? 44  ASN A C   1 
ATOM   122   O O   . ASN A  1 42  ? 147.430 155.013 134.420 1.00 107.60 ? 44  ASN A O   1 
ATOM   123   C CB  . ASN A  1 42  ? 150.318 155.160 135.940 1.00 95.23  ? 44  ASN A CB  1 
ATOM   124   C CG  . ASN A  1 42  ? 151.484 154.618 136.736 1.00 98.29  ? 44  ASN A CG  1 
ATOM   125   O OD1 . ASN A  1 42  ? 151.869 155.184 137.757 1.00 96.58  ? 44  ASN A OD1 1 
ATOM   126   N ND2 . ASN A  1 42  ? 152.057 153.517 136.269 1.00 104.54 ? 44  ASN A ND2 1 
ATOM   127   N N   . VAL A  1 43  ? 147.250 155.570 136.599 1.00 97.56  ? 45  VAL A N   1 
ATOM   128   C CA  . VAL A  1 43  ? 146.046 156.377 136.443 1.00 92.88  ? 45  VAL A CA  1 
ATOM   129   C C   . VAL A  1 43  ? 146.226 157.668 137.226 1.00 94.05  ? 45  VAL A C   1 
ATOM   130   O O   . VAL A  1 43  ? 146.523 157.635 138.425 1.00 95.61  ? 45  VAL A O   1 
ATOM   131   C CB  . VAL A  1 43  ? 144.787 155.629 136.919 1.00 90.64  ? 45  VAL A CB  1 
ATOM   132   C CG1 . VAL A  1 43  ? 143.621 156.591 137.060 1.00 91.05  ? 45  VAL A CG1 1 
ATOM   133   C CG2 . VAL A  1 43  ? 144.439 154.510 135.953 1.00 91.15  ? 45  VAL A CG2 1 
ATOM   134   N N   . ALA A  1 44  ? 146.047 158.801 136.550 1.00 95.87  ? 46  ALA A N   1 
ATOM   135   C CA  . ALA A  1 44  ? 146.083 160.113 137.184 1.00 97.61  ? 46  ALA A CA  1 
ATOM   136   C C   . ALA A  1 44  ? 144.843 160.880 136.758 1.00 103.62 ? 46  ALA A C   1 
ATOM   137   O O   . ALA A  1 44  ? 144.656 161.144 135.566 1.00 107.37 ? 46  ALA A O   1 
ATOM   138   C CB  . ALA A  1 44  ? 147.352 160.880 136.806 1.00 94.89  ? 46  ALA A CB  1 
ATOM   139   N N   . ASN A  1 45  ? 144.001 161.241 137.727 1.00 100.41 ? 47  ASN A N   1 
ATOM   140   C CA  . ASN A  1 45  ? 142.726 161.877 137.436 1.00 94.64  ? 47  ASN A CA  1 
ATOM   141   C C   . ASN A  1 45  ? 142.578 163.278 138.005 1.00 101.16 ? 47  ASN A C   1 
ATOM   142   O O   . ASN A  1 45  ? 141.722 164.027 137.523 1.00 107.45 ? 47  ASN A O   1 
ATOM   143   C CB  . ASN A  1 45  ? 141.568 161.014 137.959 1.00 91.14  ? 47  ASN A CB  1 
ATOM   144   C CG  . ASN A  1 45  ? 141.324 159.793 137.102 1.00 101.61 ? 47  ASN A CG  1 
ATOM   145   O OD1 . ASN A  1 45  ? 141.797 159.714 135.969 1.00 108.23 ? 47  ASN A OD1 1 
ATOM   146   N ND2 . ASN A  1 45  ? 140.586 158.830 137.638 1.00 107.10 ? 47  ASN A ND2 1 
ATOM   147   N N   . GLY A  1 46  ? 143.364 163.651 139.008 1.00 100.92 ? 48  GLY A N   1 
ATOM   148   C CA  . GLY A  1 46  ? 143.284 164.985 139.555 1.00 97.48  ? 48  GLY A CA  1 
ATOM   149   C C   . GLY A  1 46  ? 144.073 166.000 138.751 1.00 100.55 ? 48  GLY A C   1 
ATOM   150   O O   . GLY A  1 46  ? 145.004 165.662 138.024 1.00 105.06 ? 48  GLY A O   1 
ATOM   151   N N   . VAL A  1 47  ? 143.682 167.266 138.889 1.00 98.45  ? 49  VAL A N   1 
ATOM   152   C CA  . VAL A  1 47  ? 144.418 168.347 138.249 1.00 96.67  ? 49  VAL A CA  1 
ATOM   153   C C   . VAL A  1 47  ? 145.762 168.513 138.942 1.00 97.47  ? 49  VAL A C   1 
ATOM   154   O O   . VAL A  1 47  ? 145.844 168.516 140.177 1.00 102.81 ? 49  VAL A O   1 
ATOM   155   C CB  . VAL A  1 47  ? 143.607 169.650 138.284 1.00 92.22  ? 49  VAL A CB  1 
ATOM   156   C CG1 . VAL A  1 47  ? 144.093 170.600 137.206 1.00 96.86  ? 49  VAL A CG1 1 
ATOM   157   C CG2 . VAL A  1 47  ? 142.128 169.356 138.111 1.00 93.54  ? 49  VAL A CG2 1 
ATOM   158   N N   . LYS A  1 48  ? 146.824 168.645 138.146 1.00 95.38  ? 50  LYS A N   1 
ATOM   159   C CA  . LYS A  1 48  ? 148.192 168.758 138.653 1.00 93.27  ? 50  LYS A CA  1 
ATOM   160   C C   . LYS A  1 48  ? 148.582 167.554 139.505 1.00 97.68  ? 50  LYS A C   1 
ATOM   161   O O   . LYS A  1 48  ? 149.360 167.676 140.453 1.00 103.88 ? 50  LYS A O   1 
ATOM   162   C CB  . LYS A  1 48  ? 148.395 170.057 139.440 1.00 97.91  ? 50  LYS A CB  1 
ATOM   163   C CG  . LYS A  1 48  ? 147.774 171.281 138.794 1.00 102.45 ? 50  LYS A CG  1 
ATOM   164   C CD  . LYS A  1 48  ? 147.999 172.521 139.640 1.00 103.23 ? 50  LYS A CD  1 
ATOM   165   C CE  . LYS A  1 48  ? 147.876 173.787 138.811 1.00 102.02 ? 50  LYS A CE  1 
ATOM   166   N NZ  . LYS A  1 48  ? 147.560 173.490 137.387 1.00 110.36 ? 50  LYS A NZ  1 
ATOM   167   N N   . SER A  1 49  ? 148.048 166.385 139.173 1.00 96.08  ? 51  SER A N   1 
ATOM   168   C CA  . SER A  1 49  ? 148.372 165.146 139.861 1.00 89.56  ? 51  SER A CA  1 
ATOM   169   C C   . SER A  1 49  ? 149.379 164.346 139.045 1.00 93.30  ? 51  SER A C   1 
ATOM   170   O O   . SER A  1 49  ? 149.620 164.623 137.868 1.00 100.81 ? 51  SER A O   1 
ATOM   171   C CB  . SER A  1 49  ? 147.111 164.316 140.106 1.00 91.25  ? 51  SER A CB  1 
ATOM   172   O OG  . SER A  1 49  ? 146.469 163.998 138.885 1.00 98.06  ? 51  SER A OG  1 
ATOM   173   N N   . SER A  1 50  ? 149.976 163.346 139.687 1.00 91.92  ? 52  SER A N   1 
ATOM   174   C CA  . SER A  1 50  ? 150.993 162.541 139.029 1.00 91.75  ? 52  SER A CA  1 
ATOM   175   C C   . SER A  1 50  ? 151.060 161.165 139.672 1.00 90.73  ? 52  SER A C   1 
ATOM   176   O O   . SER A  1 50  ? 150.978 161.038 140.895 1.00 91.44  ? 52  SER A O   1 
ATOM   177   C CB  . SER A  1 50  ? 152.365 163.220 139.095 1.00 91.24  ? 52  SER A CB  1 
ATOM   178   O OG  . SER A  1 50  ? 152.708 163.539 140.430 1.00 96.89  ? 52  SER A OG  1 
ATOM   179   N N   . ALA A  1 51  ? 151.215 160.142 138.834 1.00 85.80  ? 53  ALA A N   1 
ATOM   180   C CA  . ALA A  1 51  ? 151.374 158.762 139.282 1.00 83.29  ? 53  ALA A CA  1 
ATOM   181   C C   . ALA A  1 51  ? 152.607 158.188 138.600 1.00 88.62  ? 53  ALA A C   1 
ATOM   182   O O   . ALA A  1 51  ? 152.611 157.994 137.381 1.00 92.63  ? 53  ALA A O   1 
ATOM   183   C CB  . ALA A  1 51  ? 150.134 157.929 138.964 1.00 89.10  ? 53  ALA A CB  1 
ATOM   184   N N   . PHE A  1 52  ? 153.649 157.919 139.382 1.00 87.24  ? 54  PHE A N   1 
ATOM   185   C CA  . PHE A  1 52  ? 154.923 157.436 138.868 1.00 83.09  ? 54  PHE A CA  1 
ATOM   186   C C   . PHE A  1 52  ? 155.203 156.056 139.441 1.00 86.72  ? 54  PHE A C   1 
ATOM   187   O O   . PHE A  1 52  ? 155.178 155.871 140.662 1.00 88.72  ? 54  PHE A O   1 
ATOM   188   C CB  . PHE A  1 52  ? 156.062 158.395 139.227 1.00 84.92  ? 54  PHE A CB  1 
ATOM   189   C CG  . PHE A  1 52  ? 156.132 159.620 138.357 1.00 85.39  ? 54  PHE A CG  1 
ATOM   190   C CD1 . PHE A  1 52  ? 155.028 160.437 138.188 1.00 88.32  ? 54  PHE A CD1 1 
ATOM   191   C CD2 . PHE A  1 52  ? 157.311 159.962 137.721 1.00 88.78  ? 54  PHE A CD2 1 
ATOM   192   C CE1 . PHE A  1 52  ? 155.095 161.561 137.393 1.00 88.22  ? 54  PHE A CE1 1 
ATOM   193   C CE2 . PHE A  1 52  ? 157.382 161.086 136.924 1.00 90.25  ? 54  PHE A CE2 1 
ATOM   194   C CZ  . PHE A  1 52  ? 156.273 161.886 136.761 1.00 85.95  ? 54  PHE A CZ  1 
ATOM   195   N N   . GLY A  1 53  ? 155.475 155.095 138.564 1.00 88.34  ? 55  GLY A N   1 
ATOM   196   C CA  . GLY A  1 53  ? 155.762 153.744 139.001 1.00 86.76  ? 55  GLY A CA  1 
ATOM   197   C C   . GLY A  1 53  ? 154.907 152.704 138.309 1.00 89.78  ? 55  GLY A C   1 
ATOM   198   O O   . GLY A  1 53  ? 154.699 152.773 137.095 1.00 90.84  ? 55  GLY A O   1 
ATOM   199   N N   . TYR A  1 54  ? 154.408 151.732 139.069 1.00 93.10  ? 56  TYR A N   1 
ATOM   200   C CA  . TYR A  1 54  ? 153.563 150.674 138.533 1.00 94.71  ? 56  TYR A CA  1 
ATOM   201   C C   . TYR A  1 54  ? 152.262 150.608 139.317 1.00 96.78  ? 56  TYR A C   1 
ATOM   202   O O   . TYR A  1 54  ? 152.282 150.513 140.548 1.00 97.06  ? 56  TYR A O   1 
ATOM   203   C CB  . TYR A  1 54  ? 154.271 149.317 138.580 1.00 88.95  ? 56  TYR A CB  1 
ATOM   204   C CG  . TYR A  1 54  ? 153.352 148.151 138.296 1.00 94.71  ? 56  TYR A CG  1 
ATOM   205   C CD1 . TYR A  1 54  ? 152.955 147.856 137.000 1.00 99.45  ? 56  TYR A CD1 1 
ATOM   206   C CD2 . TYR A  1 54  ? 152.881 147.346 139.323 1.00 96.47  ? 56  TYR A CD2 1 
ATOM   207   C CE1 . TYR A  1 54  ? 152.114 146.794 136.735 1.00 99.45  ? 56  TYR A CE1 1 
ATOM   208   C CE2 . TYR A  1 54  ? 152.039 146.282 139.067 1.00 95.69  ? 56  TYR A CE2 1 
ATOM   209   C CZ  . TYR A  1 54  ? 151.660 146.011 137.771 1.00 96.43  ? 56  TYR A CZ  1 
ATOM   210   O OH  . TYR A  1 54  ? 150.822 144.952 137.512 1.00 104.03 ? 56  TYR A OH  1 
ATOM   211   N N   . ASP A  1 55  ? 151.140 150.644 138.597 1.00 94.04  ? 57  ASP A N   1 
ATOM   212   C CA  . ASP A  1 55  ? 149.808 150.479 139.183 1.00 94.02  ? 57  ASP A CA  1 
ATOM   213   C C   . ASP A  1 55  ? 149.518 151.538 140.243 1.00 97.82  ? 57  ASP A C   1 
ATOM   214   O O   . ASP A  1 55  ? 148.987 151.240 141.314 1.00 97.20  ? 57  ASP A O   1 
ATOM   215   C CB  . ASP A  1 55  ? 149.633 149.074 139.759 1.00 102.44 ? 57  ASP A CB  1 
ATOM   216   C CG  . ASP A  1 55  ? 148.204 148.583 139.671 1.00 111.64 ? 57  ASP A CG  1 
ATOM   217   O OD1 . ASP A  1 55  ? 147.422 149.163 138.889 1.00 113.72 ? 57  ASP A OD1 1 
ATOM   218   O OD2 . ASP A  1 55  ? 147.863 147.617 140.384 1.00 116.06 ? 57  ASP A OD2 1 
ATOM   219   N N   . ASN A  1 56  ? 149.847 152.788 139.938 1.00 93.59  ? 58  ASN A N   1 
ATOM   220   C CA  . ASN A  1 56  ? 149.619 153.899 140.850 1.00 88.98  ? 58  ASN A CA  1 
ATOM   221   C C   . ASN A  1 56  ? 148.392 154.687 140.414 1.00 92.90  ? 58  ASN A C   1 
ATOM   222   O O   . ASN A  1 56  ? 148.157 154.879 139.218 1.00 98.85  ? 58  ASN A O   1 
ATOM   223   C CB  . ASN A  1 56  ? 150.839 154.818 140.903 1.00 86.73  ? 58  ASN A CB  1 
ATOM   224   C CG  . ASN A  1 56  ? 151.987 154.214 141.678 1.00 89.02  ? 58  ASN A CG  1 
ATOM   225   O OD1 . ASN A  1 56  ? 152.139 152.997 141.731 1.00 95.65  ? 58  ASN A OD1 1 
ATOM   226   N ND2 . ASN A  1 56  ? 152.808 155.062 142.280 1.00 93.62  ? 58  ASN A ND2 1 
ATOM   227   N N   . LYS A  1 57  ? 147.607 155.137 141.392 1.00 91.45  ? 59  LYS A N   1 
ATOM   228   C CA  . LYS A  1 57  ? 146.419 155.940 141.136 1.00 87.45  ? 59  LYS A CA  1 
ATOM   229   C C   . LYS A  1 57  ? 146.489 157.226 141.944 1.00 93.39  ? 59  LYS A C   1 
ATOM   230   O O   . LYS A  1 57  ? 146.647 157.188 143.168 1.00 97.12  ? 59  LYS A O   1 
ATOM   231   C CB  . LYS A  1 57  ? 145.136 155.176 141.483 1.00 84.43  ? 59  LYS A CB  1 
ATOM   232   C CG  . LYS A  1 57  ? 145.046 153.786 140.884 1.00 92.65  ? 59  LYS A CG  1 
ATOM   233   C CD  . LYS A  1 57  ? 143.659 153.198 141.083 1.00 101.46 ? 59  LYS A CD  1 
ATOM   234   C CE  . LYS A  1 57  ? 143.274 152.283 139.933 1.00 109.77 ? 59  LYS A CE  1 
ATOM   235   N NZ  . LYS A  1 57  ? 144.463 151.834 139.159 1.00 104.69 ? 59  LYS A NZ  1 
ATOM   236   N N   . ALA A  1 58  ? 146.371 158.358 141.255 1.00 93.03  ? 60  ALA A N   1 
ATOM   237   C CA  . ALA A  1 58  ? 146.270 159.674 141.877 1.00 90.28  ? 60  ALA A CA  1 
ATOM   238   C C   . ALA A  1 58  ? 145.000 160.323 141.346 1.00 95.44  ? 60  ALA A C   1 
ATOM   239   O O   . ALA A  1 58  ? 144.954 160.752 140.188 1.00 99.29  ? 60  ALA A O   1 
ATOM   240   C CB  . ALA A  1 58  ? 147.500 160.527 141.576 1.00 88.25  ? 60  ALA A CB  1 
ATOM   241   N N   . ILE A  1 59  ? 143.973 160.399 142.189 1.00 95.59  ? 61  ILE A N   1 
ATOM   242   C CA  . ILE A  1 59  ? 142.626 160.729 141.735 1.00 95.12  ? 61  ILE A CA  1 
ATOM   243   C C   . ILE A  1 59  ? 142.165 162.109 142.178 1.00 102.34 ? 61  ILE A C   1 
ATOM   244   O O   . ILE A  1 59  ? 141.096 162.558 141.733 1.00 105.69 ? 61  ILE A O   1 
ATOM   245   C CB  . ILE A  1 59  ? 141.611 159.660 142.194 1.00 92.93  ? 61  ILE A CB  1 
ATOM   246   C CG1 . ILE A  1 59  ? 142.281 158.288 142.215 1.00 91.06  ? 61  ILE A CG1 1 
ATOM   247   C CG2 . ILE A  1 59  ? 140.418 159.609 141.256 1.00 95.56  ? 61  ILE A CG2 1 
ATOM   248   C CD1 . ILE A  1 59  ? 141.389 157.180 142.709 1.00 94.69  ? 61  ILE A CD1 1 
ATOM   249   N N   . GLU A  1 60  ? 142.922 162.801 143.019 1.00 102.59 ? 62  GLU A N   1 
ATOM   250   C CA  . GLU A  1 60  ? 142.519 164.109 143.511 1.00 103.07 ? 62  GLU A CA  1 
ATOM   251   C C   . GLU A  1 60  ? 143.512 165.180 143.079 1.00 101.58 ? 62  GLU A C   1 
ATOM   252   O O   . GLU A  1 60  ? 144.608 164.894 142.591 1.00 104.01 ? 62  GLU A O   1 
ATOM   253   C CB  . GLU A  1 60  ? 142.375 164.095 145.037 1.00 99.39  ? 62  GLU A CB  1 
ATOM   254   C CG  . GLU A  1 60  ? 140.938 164.055 145.606 1.00 108.35 ? 62  GLU A CG  1 
ATOM   255   C CD  . GLU A  1 60  ? 139.933 165.040 144.992 1.00 122.63 ? 62  GLU A CD  1 
ATOM   256   O OE1 . GLU A  1 60  ? 138.811 165.122 145.535 1.00 131.47 ? 62  GLU A OE1 1 
ATOM   257   O OE2 . GLU A  1 60  ? 140.239 165.764 144.022 1.00 122.62 ? 62  GLU A OE2 1 
ATOM   258   N N   . LYS A  1 61  ? 143.097 166.432 143.264 1.00 98.63  ? 63  LYS A N   1 
ATOM   259   C CA  . LYS A  1 61  ? 143.899 167.572 142.844 1.00 93.47  ? 63  LYS A CA  1 
ATOM   260   C C   . LYS A  1 61  ? 145.223 167.615 143.596 1.00 95.30  ? 63  LYS A C   1 
ATOM   261   O O   . LYS A  1 61  ? 145.257 167.492 144.823 1.00 99.15  ? 63  LYS A O   1 
ATOM   262   C CB  . LYS A  1 61  ? 143.119 168.866 143.074 1.00 97.39  ? 63  LYS A CB  1 
ATOM   263   C CG  . LYS A  1 61  ? 143.699 170.083 142.381 1.00 105.64 ? 63  LYS A CG  1 
ATOM   264   C CD  . LYS A  1 61  ? 143.301 171.359 143.101 1.00 107.24 ? 63  LYS A CD  1 
ATOM   265   C CE  . LYS A  1 61  ? 142.294 172.155 142.293 1.00 112.18 ? 63  LYS A CE  1 
ATOM   266   N NZ  . LYS A  1 61  ? 142.724 173.569 142.130 1.00 112.32 ? 63  LYS A NZ  1 
ATOM   267   N N   . GLU A  1 62  ? 146.312 167.803 142.847 1.00 92.71  ? 64  GLU A N   1 
ATOM   268   C CA  . GLU A  1 62  ? 147.661 167.914 143.408 1.00 90.45  ? 64  GLU A CA  1 
ATOM   269   C C   . GLU A  1 62  ? 147.982 166.744 144.333 1.00 93.60  ? 64  GLU A C   1 
ATOM   270   O O   . GLU A  1 62  ? 148.564 166.912 145.406 1.00 97.97  ? 64  GLU A O   1 
ATOM   271   C CB  . GLU A  1 62  ? 147.855 169.248 144.129 1.00 96.31  ? 64  GLU A CB  1 
ATOM   272   C CG  . GLU A  1 62  ? 147.067 170.403 143.540 1.00 102.99 ? 64  GLU A CG  1 
ATOM   273   C CD  . GLU A  1 62  ? 147.807 171.719 143.634 1.00 115.05 ? 64  GLU A CD  1 
ATOM   274   O OE1 . GLU A  1 62  ? 147.142 172.775 143.654 1.00 116.26 ? 64  GLU A OE1 1 
ATOM   275   O OE2 . GLU A  1 62  ? 149.054 171.698 143.690 1.00 120.13 ? 64  GLU A OE2 1 
ATOM   276   N N   . SER A  1 63  ? 147.597 165.544 143.912 1.00 92.15  ? 65  SER A N   1 
ATOM   277   C CA  . SER A  1 63  ? 147.894 164.322 144.641 1.00 86.91  ? 65  SER A CA  1 
ATOM   278   C C   . SER A  1 63  ? 148.931 163.518 143.871 1.00 91.29  ? 65  SER A C   1 
ATOM   279   O O   . SER A  1 63  ? 148.862 163.415 142.643 1.00 97.77  ? 65  SER A O   1 
ATOM   280   C CB  . SER A  1 63  ? 146.632 163.485 144.855 1.00 86.82  ? 65  SER A CB  1 
ATOM   281   O OG  . SER A  1 63  ? 145.916 163.329 143.644 1.00 96.80  ? 65  SER A OG  1 
ATOM   282   N N   . SER A  1 64  ? 149.890 162.950 144.595 1.00 88.67  ? 66  SER A N   1 
ATOM   283   C CA  . SER A  1 64  ? 150.990 162.220 143.987 1.00 85.48  ? 66  SER A CA  1 
ATOM   284   C C   . SER A  1 64  ? 151.066 160.819 144.569 1.00 86.59  ? 66  SER A C   1 
ATOM   285   O O   . SER A  1 64  ? 150.945 160.632 145.782 1.00 87.81  ? 66  SER A O   1 
ATOM   286   C CB  . SER A  1 64  ? 152.320 162.945 144.201 1.00 88.92  ? 66  SER A CB  1 
ATOM   287   O OG  . SER A  1 64  ? 152.337 163.613 145.449 1.00 94.56  ? 66  SER A OG  1 
ATOM   288   N N   . ALA A  1 65  ? 151.270 159.837 143.695 1.00 84.81  ? 67  ALA A N   1 
ATOM   289   C CA  . ALA A  1 65  ? 151.446 158.445 144.090 1.00 80.83  ? 67  ALA A CA  1 
ATOM   290   C C   . ALA A  1 65  ? 152.692 157.921 143.393 1.00 85.31  ? 67  ALA A C   1 
ATOM   291   O O   . ALA A  1 65  ? 152.674 157.681 142.182 1.00 92.62  ? 67  ALA A O   1 
ATOM   292   C CB  . ALA A  1 65  ? 150.221 157.605 143.732 1.00 79.40  ? 67  ALA A CB  1 
ATOM   293   N N   . PHE A  1 66  ? 153.769 157.746 144.151 1.00 82.22  ? 68  PHE A N   1 
ATOM   294   C CA  . PHE A  1 66  ? 155.052 157.316 143.615 1.00 76.28  ? 68  PHE A CA  1 
ATOM   295   C C   . PHE A  1 66  ? 155.424 155.977 144.232 1.00 79.95  ? 68  PHE A C   1 
ATOM   296   O O   . PHE A  1 66  ? 155.422 155.834 145.458 1.00 81.96  ? 68  PHE A O   1 
ATOM   297   C CB  . PHE A  1 66  ? 156.145 158.350 143.901 1.00 78.56  ? 68  PHE A CB  1 
ATOM   298   C CG  . PHE A  1 66  ? 156.100 159.552 143.000 1.00 78.18  ? 68  PHE A CG  1 
ATOM   299   C CD1 . PHE A  1 66  ? 154.978 160.359 142.947 1.00 82.21  ? 68  PHE A CD1 1 
ATOM   300   C CD2 . PHE A  1 66  ? 157.189 159.881 142.214 1.00 80.09  ? 68  PHE A CD2 1 
ATOM   301   C CE1 . PHE A  1 66  ? 154.938 161.463 142.122 1.00 84.03  ? 68  PHE A CE1 1 
ATOM   302   C CE2 . PHE A  1 66  ? 157.154 160.986 141.388 1.00 85.57  ? 68  PHE A CE2 1 
ATOM   303   C CZ  . PHE A  1 66  ? 156.028 161.777 141.342 1.00 83.89  ? 68  PHE A CZ  1 
ATOM   304   N N   . GLY A  1 67  ? 155.748 155.005 143.386 1.00 80.55  ? 69  GLY A N   1 
ATOM   305   C CA  . GLY A  1 67  ? 156.114 153.690 143.871 1.00 79.64  ? 69  GLY A CA  1 
ATOM   306   C C   . GLY A  1 67  ? 155.380 152.568 143.170 1.00 81.72  ? 69  GLY A C   1 
ATOM   307   O O   . GLY A  1 67  ? 155.207 152.602 141.949 1.00 85.02  ? 69  GLY A O   1 
ATOM   308   N N   . THR A  1 68  ? 154.940 151.567 143.929 1.00 85.00  ? 70  THR A N   1 
ATOM   309   C CA  . THR A  1 68  ? 154.258 150.403 143.379 1.00 88.51  ? 70  THR A CA  1 
ATOM   310   C C   . THR A  1 68  ? 152.904 150.246 144.055 1.00 85.88  ? 70  THR A C   1 
ATOM   311   O O   . THR A  1 68  ? 152.834 150.040 145.271 1.00 88.20  ? 70  THR A O   1 
ATOM   312   C CB  . THR A  1 68  ? 155.097 149.138 143.565 1.00 87.19  ? 70  THR A CB  1 
ATOM   313   O OG1 . THR A  1 68  ? 156.269 149.216 142.744 1.00 93.12  ? 70  THR A OG1 1 
ATOM   314   C CG2 . THR A  1 68  ? 154.296 147.908 143.175 1.00 85.97  ? 70  THR A CG2 1 
ATOM   315   N N   . GLY A  1 69  ? 151.838 150.332 143.266 1.00 83.24  ? 71  GLY A N   1 
ATOM   316   C CA  . GLY A  1 69  ? 150.498 150.079 143.773 1.00 85.06  ? 71  GLY A CA  1 
ATOM   317   C C   . GLY A  1 69  ? 150.018 151.046 144.832 1.00 86.86  ? 71  GLY A C   1 
ATOM   318   O O   . GLY A  1 69  ? 149.315 150.639 145.764 1.00 85.92  ? 71  GLY A O   1 
ATOM   319   N N   . ASN A  1 70  ? 150.367 152.321 144.707 1.00 84.88  ? 72  ASN A N   1 
ATOM   320   C CA  . ASN A  1 70  ? 149.944 153.321 145.674 1.00 79.19  ? 72  ASN A CA  1 
ATOM   321   C C   . ASN A  1 70  ? 148.622 153.949 145.256 1.00 83.77  ? 72  ASN A C   1 
ATOM   322   O O   . ASN A  1 70  ? 148.263 153.963 144.076 1.00 89.81  ? 72  ASN A O   1 
ATOM   323   C CB  . ASN A  1 70  ? 151.007 154.407 145.832 1.00 78.00  ? 72  ASN A CB  1 
ATOM   324   C CG  . ASN A  1 70  ? 152.323 153.860 146.328 1.00 83.51  ? 72  ASN A CG  1 
ATOM   325   O OD1 . ASN A  1 70  ? 152.710 152.745 145.989 1.00 90.53  ? 72  ASN A OD1 1 
ATOM   326   N ND2 . ASN A  1 70  ? 153.019 154.641 147.142 1.00 85.69  ? 72  ASN A ND2 1 
ATOM   327   N N   . ARG A  1 71  ? 147.895 154.467 146.243 1.00 82.63  ? 73  ARG A N   1 
ATOM   328   C CA  . ARG A  1 71  ? 146.619 155.130 146.013 1.00 80.54  ? 73  ARG A CA  1 
ATOM   329   C C   . ARG A  1 71  ? 146.596 156.447 146.770 1.00 88.48  ? 73  ARG A C   1 
ATOM   330   O O   . ARG A  1 71  ? 146.806 156.471 147.986 1.00 92.80  ? 73  ARG A O   1 
ATOM   331   C CB  . ARG A  1 71  ? 145.450 154.246 146.453 1.00 82.55  ? 73  ARG A CB  1 
ATOM   332   C CG  . ARG A  1 71  ? 144.728 153.567 145.307 1.00 89.47  ? 73  ARG A CG  1 
ATOM   333   C CD  . ARG A  1 71  ? 145.279 152.173 145.076 1.00 93.08  ? 73  ARG A CD  1 
ATOM   334   N NE  . ARG A  1 71  ? 145.013 151.691 143.726 1.00 99.78  ? 73  ARG A NE  1 
ATOM   335   C CZ  . ARG A  1 71  ? 145.812 150.873 143.054 1.00 105.94 ? 73  ARG A CZ  1 
ATOM   336   N NH1 . ARG A  1 71  ? 146.942 150.428 143.576 1.00 104.94 ? 73  ARG A NH1 1 
ATOM   337   N NH2 . ARG A  1 71  ? 145.467 150.493 141.827 1.00 109.39 ? 73  ARG A NH2 1 
ATOM   338   N N   . ALA A  1 72  ? 146.338 157.536 146.052 1.00 87.33  ? 74  ALA A N   1 
ATOM   339   C CA  . ALA A  1 72  ? 146.214 158.868 146.637 1.00 84.05  ? 74  ALA A CA  1 
ATOM   340   C C   . ALA A  1 72  ? 144.837 159.400 146.260 1.00 90.72  ? 74  ALA A C   1 
ATOM   341   O O   . ALA A  1 72  ? 144.644 159.921 145.157 1.00 95.47  ? 74  ALA A O   1 
ATOM   342   C CB  . ALA A  1 72  ? 147.327 159.791 146.151 1.00 82.96  ? 74  ALA A CB  1 
ATOM   343   N N   . THR A  1 73  ? 143.880 159.271 147.179 1.00 89.73  ? 75  THR A N   1 
ATOM   344   C CA  . THR A  1 73  ? 142.487 159.606 146.916 1.00 90.90  ? 75  THR A CA  1 
ATOM   345   C C   . THR A  1 73  ? 142.048 160.878 147.631 1.00 93.92  ? 75  THR A C   1 
ATOM   346   O O   . THR A  1 73  ? 140.847 161.152 147.719 1.00 100.19 ? 75  THR A O   1 
ATOM   347   C CB  . THR A  1 73  ? 141.583 158.440 147.313 1.00 94.97  ? 75  THR A CB  1 
ATOM   348   O OG1 . THR A  1 73  ? 141.901 158.021 148.645 1.00 97.87  ? 75  THR A OG1 1 
ATOM   349   C CG2 . THR A  1 73  ? 141.783 157.271 146.366 1.00 92.21  ? 75  THR A CG2 1 
ATOM   350   N N   . GLY A  1 74  ? 142.990 161.657 148.143 1.00 89.89  ? 76  GLY A N   1 
ATOM   351   C CA  . GLY A  1 74  ? 142.668 162.908 148.796 1.00 88.52  ? 76  GLY A CA  1 
ATOM   352   C C   . GLY A  1 74  ? 143.468 164.047 148.202 1.00 93.54  ? 76  GLY A C   1 
ATOM   353   O O   . GLY A  1 74  ? 144.551 163.853 147.651 1.00 97.20  ? 76  GLY A O   1 
ATOM   354   N N   . GLU A  1 75  ? 142.905 165.248 148.308 1.00 95.15  ? 77  GLU A N   1 
ATOM   355   C CA  . GLU A  1 75  ? 143.594 166.434 147.823 1.00 94.40  ? 77  GLU A CA  1 
ATOM   356   C C   . GLU A  1 75  ? 144.914 166.609 148.560 1.00 92.01  ? 77  GLU A C   1 
ATOM   357   O O   . GLU A  1 75  ? 145.031 166.290 149.743 1.00 97.32  ? 77  GLU A O   1 
ATOM   358   C CB  . GLU A  1 75  ? 142.725 167.675 148.014 1.00 97.46  ? 77  GLU A CB  1 
ATOM   359   C CG  . GLU A  1 75  ? 141.258 167.468 147.697 1.00 112.40 ? 77  GLU A CG  1 
ATOM   360   C CD  . GLU A  1 75  ? 140.656 168.646 146.960 1.00 128.40 ? 77  GLU A CD  1 
ATOM   361   O OE1 . GLU A  1 75  ? 141.326 169.696 146.870 1.00 123.86 ? 77  GLU A OE1 1 
ATOM   362   O OE2 . GLU A  1 75  ? 139.514 168.523 146.471 1.00 138.83 ? 77  GLU A OE2 1 
ATOM   363   N N   . PHE A  1 76  ? 145.925 167.084 147.831 1.00 87.98  ? 78  PHE A N   1 
ATOM   364   C CA  . PHE A  1 76  ? 147.235 167.405 148.403 1.00 86.01  ? 78  PHE A CA  1 
ATOM   365   C C   . PHE A  1 76  ? 147.821 166.233 149.188 1.00 89.98  ? 78  PHE A C   1 
ATOM   366   O O   . PHE A  1 76  ? 148.646 166.420 150.085 1.00 98.34  ? 78  PHE A O   1 
ATOM   367   C CB  . PHE A  1 76  ? 147.156 168.649 149.290 1.00 90.28  ? 78  PHE A CB  1 
ATOM   368   C CG  . PHE A  1 76  ? 146.284 169.734 148.735 1.00 94.07  ? 78  PHE A CG  1 
ATOM   369   C CD1 . PHE A  1 76  ? 146.513 170.251 147.472 1.00 96.38  ? 78  PHE A CD1 1 
ATOM   370   C CD2 . PHE A  1 76  ? 145.231 170.236 149.476 1.00 96.14  ? 78  PHE A CD2 1 
ATOM   371   C CE1 . PHE A  1 76  ? 145.708 171.249 146.963 1.00 99.23  ? 78  PHE A CE1 1 
ATOM   372   C CE2 . PHE A  1 76  ? 144.423 171.233 148.972 1.00 96.85  ? 78  PHE A CE2 1 
ATOM   373   C CZ  . PHE A  1 76  ? 144.661 171.739 147.713 1.00 98.20  ? 78  PHE A CZ  1 
ATOM   374   N N   . SER A  1 77  ? 147.400 165.018 148.862 1.00 88.55  ? 79  SER A N   1 
ATOM   375   C CA  . SER A  1 77  ? 147.853 163.827 149.562 1.00 83.96  ? 79  SER A CA  1 
ATOM   376   C C   . SER A  1 77  ? 148.902 163.097 148.736 1.00 83.31  ? 79  SER A C   1 
ATOM   377   O O   . SER A  1 77  ? 148.867 163.090 147.504 1.00 91.03  ? 79  SER A O   1 
ATOM   378   C CB  . SER A  1 77  ? 146.680 162.894 149.867 1.00 84.51  ? 79  SER A CB  1 
ATOM   379   O OG  . SER A  1 77  ? 146.082 162.421 148.674 1.00 90.21  ? 79  SER A OG  1 
ATOM   380   N N   . SER A  1 78  ? 149.844 162.474 149.438 1.00 78.87  ? 80  SER A N   1 
ATOM   381   C CA  . SER A  1 78  ? 150.952 161.787 148.794 1.00 79.16  ? 80  SER A CA  1 
ATOM   382   C C   . SER A  1 78  ? 151.109 160.403 149.400 1.00 83.17  ? 80  SER A C   1 
ATOM   383   O O   . SER A  1 78  ? 151.061 160.247 150.623 1.00 87.21  ? 80  SER A O   1 
ATOM   384   C CB  . SER A  1 78  ? 152.254 162.580 148.943 1.00 83.47  ? 80  SER A CB  1 
ATOM   385   O OG  . SER A  1 78  ? 152.595 162.738 150.308 1.00 94.19  ? 80  SER A OG  1 
ATOM   386   N N   . ALA A  1 79  ? 151.295 159.406 148.539 1.00 79.34  ? 81  ALA A N   1 
ATOM   387   C CA  . ALA A  1 79  ? 151.544 158.031 148.956 1.00 74.51  ? 81  ALA A CA  1 
ATOM   388   C C   . ALA A  1 79  ? 152.804 157.557 148.249 1.00 78.37  ? 81  ALA A C   1 
ATOM   389   O O   . ALA A  1 79  ? 152.792 157.338 147.034 1.00 83.81  ? 81  ALA A O   1 
ATOM   390   C CB  . ALA A  1 79  ? 150.357 157.127 148.629 1.00 74.13  ? 81  ALA A CB  1 
ATOM   391   N N   . PHE A  1 80  ? 153.887 157.402 149.004 1.00 75.31  ? 82  PHE A N   1 
ATOM   392   C CA  . PHE A  1 80  ? 155.186 157.040 148.456 1.00 70.31  ? 82  PHE A CA  1 
ATOM   393   C C   . PHE A  1 80  ? 155.623 155.709 149.044 1.00 74.73  ? 82  PHE A C   1 
ATOM   394   O O   . PHE A  1 80  ? 155.670 155.553 150.268 1.00 82.28  ? 82  PHE A O   1 
ATOM   395   C CB  . PHE A  1 80  ? 156.230 158.117 148.761 1.00 73.29  ? 82  PHE A CB  1 
ATOM   396   C CG  . PHE A  1 80  ? 156.165 159.307 147.846 1.00 73.75  ? 82  PHE A CG  1 
ATOM   397   C CD1 . PHE A  1 80  ? 155.013 160.066 147.751 1.00 76.66  ? 82  PHE A CD1 1 
ATOM   398   C CD2 . PHE A  1 80  ? 157.262 159.671 147.087 1.00 78.21  ? 82  PHE A CD2 1 
ATOM   399   C CE1 . PHE A  1 80  ? 154.954 161.159 146.914 1.00 81.06  ? 82  PHE A CE1 1 
ATOM   400   C CE2 . PHE A  1 80  ? 157.207 160.765 146.248 1.00 83.35  ? 82  PHE A CE2 1 
ATOM   401   C CZ  . PHE A  1 80  ? 156.052 161.509 146.162 1.00 84.13  ? 82  PHE A CZ  1 
ATOM   402   N N   . GLY A  1 81  ? 155.946 154.755 148.177 1.00 71.73  ? 83  GLY A N   1 
ATOM   403   C CA  . GLY A  1 81  ? 156.417 153.467 148.643 1.00 73.54  ? 83  GLY A CA  1 
ATOM   404   C C   . GLY A  1 81  ? 155.746 152.284 147.978 1.00 75.87  ? 83  GLY A C   1 
ATOM   405   O O   . GLY A  1 81  ? 155.736 152.175 146.749 1.00 79.20  ? 83  GLY A O   1 
ATOM   406   N N   . PHE A  1 82  ? 155.180 151.389 148.785 1.00 77.70  ? 84  PHE A N   1 
ATOM   407   C CA  . PHE A  1 82  ? 154.590 150.150 148.294 1.00 77.93  ? 84  PHE A CA  1 
ATOM   408   C C   . PHE A  1 82  ? 153.206 149.977 148.898 1.00 80.96  ? 84  PHE A C   1 
ATOM   409   O O   . PHE A  1 82  ? 153.072 149.847 150.119 1.00 85.46  ? 84  PHE A O   1 
ATOM   410   C CB  . PHE A  1 82  ? 155.481 148.953 148.638 1.00 72.29  ? 84  PHE A CB  1 
ATOM   411   C CG  . PHE A  1 82  ? 154.869 147.625 148.305 1.00 78.88  ? 84  PHE A CG  1 
ATOM   412   C CD1 . PHE A  1 82  ? 154.801 147.186 146.996 1.00 82.64  ? 84  PHE A CD1 1 
ATOM   413   C CD2 . PHE A  1 82  ? 154.369 146.810 149.305 1.00 79.50  ? 84  PHE A CD2 1 
ATOM   414   C CE1 . PHE A  1 82  ? 154.241 145.963 146.690 1.00 79.89  ? 84  PHE A CE1 1 
ATOM   415   C CE2 . PHE A  1 82  ? 153.809 145.586 149.004 1.00 79.22  ? 84  PHE A CE2 1 
ATOM   416   C CZ  . PHE A  1 82  ? 153.744 145.163 147.695 1.00 78.12  ? 84  PHE A CZ  1 
ATOM   417   N N   . HIS A  1 83  ? 152.185 149.969 148.041 1.00 79.06  ? 85  HIS A N   1 
ATOM   418   C CA  . HIS A  1 83  ? 150.803 149.702 148.440 1.00 79.55  ? 85  HIS A CA  1 
ATOM   419   C C   . HIS A  1 83  ? 150.342 150.645 149.548 1.00 83.81  ? 85  HIS A C   1 
ATOM   420   O O   . HIS A  1 83  ? 149.746 150.233 150.544 1.00 87.39  ? 85  HIS A O   1 
ATOM   421   C CB  . HIS A  1 83  ? 150.632 148.242 148.861 1.00 80.04  ? 85  HIS A CB  1 
ATOM   422   C CG  . HIS A  1 83  ? 150.515 147.294 147.710 1.00 84.32  ? 85  HIS A CG  1 
ATOM   423   N ND1 . HIS A  1 83  ? 149.756 146.145 147.766 1.00 89.16  ? 85  HIS A ND1 1 
ATOM   424   C CD2 . HIS A  1 83  ? 151.061 147.323 146.472 1.00 88.95  ? 85  HIS A CD2 1 
ATOM   425   C CE1 . HIS A  1 83  ? 149.839 145.508 146.613 1.00 94.55  ? 85  HIS A CE1 1 
ATOM   426   N NE2 . HIS A  1 83  ? 150.626 146.201 145.810 1.00 90.90  ? 85  HIS A NE2 1 
ATOM   427   N N   . ASN A  1 84  ? 150.614 151.930 149.362 1.00 81.16  ? 86  ASN A N   1 
ATOM   428   C CA  . ASN A  1 84  ? 150.249 152.951 150.331 1.00 78.89  ? 86  ASN A CA  1 
ATOM   429   C C   . ASN A  1 84  ? 148.934 153.608 149.932 1.00 81.18  ? 86  ASN A C   1 
ATOM   430   O O   . ASN A  1 84  ? 148.594 153.690 148.749 1.00 89.74  ? 86  ASN A O   1 
ATOM   431   C CB  . ASN A  1 84  ? 151.350 154.005 150.441 1.00 76.17  ? 86  ASN A CB  1 
ATOM   432   C CG  . ASN A  1 84  ? 152.529 153.525 151.255 1.00 78.65  ? 86  ASN A CG  1 
ATOM   433   O OD1 . ASN A  1 84  ? 152.541 152.397 151.742 1.00 82.43  ? 86  ASN A OD1 1 
ATOM   434   N ND2 . ASN A  1 84  ? 153.536 154.374 151.396 1.00 87.66  ? 86  ASN A ND2 1 
ATOM   435   N N   . ILE A  1 85  ? 148.191 154.074 150.933 1.00 78.44  ? 87  ILE A N   1 
ATOM   436   C CA  . ILE A  1 85  ? 146.894 154.705 150.720 1.00 79.20  ? 87  ILE A CA  1 
ATOM   437   C C   . ILE A  1 85  ? 146.834 155.996 151.523 1.00 86.35  ? 87  ILE A C   1 
ATOM   438   O O   . ILE A  1 85  ? 147.046 155.986 152.740 1.00 91.03  ? 87  ILE A O   1 
ATOM   439   C CB  . ILE A  1 85  ? 145.732 153.772 151.111 1.00 77.39  ? 87  ILE A CB  1 
ATOM   440   C CG1 . ILE A  1 85  ? 145.555 152.674 150.061 1.00 82.13  ? 87  ILE A CG1 1 
ATOM   441   C CG2 . ILE A  1 85  ? 144.445 154.560 151.268 1.00 78.08  ? 87  ILE A CG2 1 
ATOM   442   C CD1 . ILE A  1 85  ? 145.278 151.310 150.648 1.00 84.49  ? 87  ILE A CD1 1 
ATOM   443   N N   . ALA A  1 86  ? 146.544 157.103 150.841 1.00 85.05  ? 88  ALA A N   1 
ATOM   444   C CA  . ALA A  1 86  ? 146.297 158.393 151.471 1.00 82.33  ? 88  ALA A CA  1 
ATOM   445   C C   . ALA A  1 86  ? 144.933 158.885 151.017 1.00 89.09  ? 88  ALA A C   1 
ATOM   446   O O   . ALA A  1 86  ? 144.637 158.872 149.818 1.00 94.02  ? 88  ALA A O   1 
ATOM   447   C CB  . ALA A  1 86  ? 147.383 159.407 151.110 1.00 79.66  ? 88  ALA A CB  1 
ATOM   448   N N   . SER A  1 87  ? 144.102 159.321 151.966 1.00 85.85  ? 89  SER A N   1 
ATOM   449   C CA  . SER A  1 87  ? 142.694 159.551 151.676 1.00 82.17  ? 89  SER A CA  1 
ATOM   450   C C   . SER A  1 87  ? 142.149 160.914 152.082 1.00 88.80  ? 89  SER A C   1 
ATOM   451   O O   . SER A  1 87  ? 140.957 161.154 151.868 1.00 95.21  ? 89  SER A O   1 
ATOM   452   C CB  . SER A  1 87  ? 141.833 158.473 152.350 1.00 84.17  ? 89  SER A CB  1 
ATOM   453   O OG  . SER A  1 87  ? 142.146 157.187 151.848 1.00 90.34  ? 89  SER A OG  1 
ATOM   454   N N   . LYS A  1 88  ? 142.954 161.808 152.656 1.00 88.44  ? 90  LYS A N   1 
ATOM   455   C CA  . LYS A  1 88  ? 142.385 163.059 153.145 1.00 87.44  ? 90  LYS A CA  1 
ATOM   456   C C   . LYS A  1 88  ? 143.135 164.290 152.646 1.00 91.13  ? 90  LYS A C   1 
ATOM   457   O O   . LYS A  1 88  ? 144.020 164.186 151.791 1.00 94.81  ? 90  LYS A O   1 
ATOM   458   C CB  . LYS A  1 88  ? 142.327 163.046 154.672 1.00 86.80  ? 90  LYS A CB  1 
ATOM   459   C CG  . LYS A  1 88  ? 141.361 162.008 155.218 1.00 87.02  ? 90  LYS A CG  1 
ATOM   460   C CD  . LYS A  1 88  ? 139.918 162.434 155.013 1.00 93.77  ? 90  LYS A CD  1 
ATOM   461   C CE  . LYS A  1 88  ? 138.959 161.499 155.731 1.00 97.65  ? 90  LYS A CE  1 
ATOM   462   N NZ  . LYS A  1 88  ? 139.466 160.100 155.755 1.00 96.16  ? 90  LYS A NZ  1 
ATOM   463   N N   . ILE A  1 89  ? 142.781 165.461 153.185 1.00 90.19  ? 91  ILE A N   1 
ATOM   464   C CA  . ILE A  1 89  ? 143.169 166.733 152.580 1.00 89.82  ? 91  ILE A CA  1 
ATOM   465   C C   . ILE A  1 89  ? 144.671 166.974 152.686 1.00 91.64  ? 91  ILE A C   1 
ATOM   466   O O   . ILE A  1 89  ? 145.242 167.722 151.884 1.00 98.62  ? 91  ILE A O   1 
ATOM   467   C CB  . ILE A  1 89  ? 142.360 167.879 153.217 1.00 90.81  ? 91  ILE A CB  1 
ATOM   468   C CG1 . ILE A  1 89  ? 142.660 169.212 152.531 1.00 96.44  ? 91  ILE A CG1 1 
ATOM   469   C CG2 . ILE A  1 89  ? 142.664 167.980 154.689 1.00 92.68  ? 91  ILE A CG2 1 
ATOM   470   C CD1 . ILE A  1 89  ? 141.985 169.369 151.192 1.00 101.69 ? 91  ILE A CD1 1 
ATOM   471   N N   . HIS A  1 90  ? 145.336 166.381 153.674 1.00 82.31  ? 92  HIS A N   1 
ATOM   472   C CA  . HIS A  1 90  ? 146.800 166.406 153.741 1.00 78.40  ? 92  HIS A CA  1 
ATOM   473   C C   . HIS A  1 90  ? 147.220 165.100 154.408 1.00 86.38  ? 92  HIS A C   1 
ATOM   474   O O   . HIS A  1 90  ? 147.298 165.014 155.634 1.00 97.37  ? 92  HIS A O   1 
ATOM   475   C CB  . HIS A  1 90  ? 147.309 167.622 154.504 1.00 84.53  ? 92  HIS A CB  1 
ATOM   476   C CG  . HIS A  1 90  ? 147.315 168.886 153.701 1.00 88.14  ? 92  HIS A CG  1 
ATOM   477   N ND1 . HIS A  1 90  ? 148.282 169.168 152.761 1.00 87.58  ? 92  HIS A ND1 1 
ATOM   478   C CD2 . HIS A  1 90  ? 146.471 169.945 153.701 1.00 89.90  ? 92  HIS A CD2 1 
ATOM   479   C CE1 . HIS A  1 90  ? 148.033 170.346 152.216 1.00 86.98  ? 92  HIS A CE1 1 
ATOM   480   N NE2 . HIS A  1 90  ? 146.940 170.838 152.769 1.00 86.88  ? 92  HIS A NE2 1 
ATOM   481   N N   . SER A  1 91  ? 147.508 164.090 153.598 1.00 81.49  ? 93  SER A N   1 
ATOM   482   C CA  . SER A  1 91  ? 147.822 162.768 154.114 1.00 79.98  ? 93  SER A CA  1 
ATOM   483   C C   . SER A  1 91  ? 149.128 162.278 153.515 1.00 86.53  ? 93  SER A C   1 
ATOM   484   O O   . SER A  1 91  ? 149.367 162.427 152.314 1.00 93.71  ? 93  SER A O   1 
ATOM   485   C CB  . SER A  1 91  ? 146.698 161.778 153.814 1.00 83.94  ? 93  SER A CB  1 
ATOM   486   O OG  . SER A  1 91  ? 145.436 162.414 153.895 1.00 83.89  ? 93  SER A OG  1 
ATOM   487   N N   . SER A  1 92  ? 149.969 161.692 154.361 1.00 82.92  ? 94  SER A N   1 
ATOM   488   C CA  . SER A  1 92  ? 151.249 161.144 153.938 1.00 81.28  ? 94  SER A CA  1 
ATOM   489   C C   . SER A  1 92  ? 151.317 159.692 154.375 1.00 83.71  ? 94  SER A C   1 
ATOM   490   O O   . SER A  1 92  ? 151.173 159.391 155.564 1.00 88.58  ? 94  SER A O   1 
ATOM   491   C CB  . SER A  1 92  ? 152.413 161.943 154.529 1.00 88.91  ? 94  SER A CB  1 
ATOM   492   O OG  . SER A  1 92  ? 152.397 163.280 154.062 1.00 89.46  ? 94  SER A OG  1 
ATOM   493   N N   . ALA A  1 93  ? 151.531 158.797 153.416 1.00 77.31  ? 95  ALA A N   1 
ATOM   494   C CA  . ALA A  1 93  ? 151.710 157.372 153.680 1.00 72.54  ? 95  ALA A CA  1 
ATOM   495   C C   . ALA A  1 93  ? 153.019 156.967 153.016 1.00 78.33  ? 95  ALA A C   1 
ATOM   496   O O   . ALA A  1 93  ? 153.046 156.654 151.822 1.00 88.64  ? 95  ALA A O   1 
ATOM   497   C CB  . ALA A  1 93  ? 150.535 156.555 153.156 1.00 73.62  ? 95  ALA A CB  1 
ATOM   498   N N   . PHE A  1 94  ? 154.102 156.977 153.785 1.00 74.78  ? 96  PHE A N   1 
ATOM   499   C CA  . PHE A  1 94  ? 155.436 156.700 153.273 1.00 72.48  ? 96  PHE A CA  1 
ATOM   500   C C   . PHE A  1 94  ? 155.930 155.396 153.883 1.00 75.05  ? 96  PHE A C   1 
ATOM   501   O O   . PHE A  1 94  ? 156.029 155.280 155.109 1.00 80.42  ? 96  PHE A O   1 
ATOM   502   C CB  . PHE A  1 94  ? 156.395 157.845 153.596 1.00 75.00  ? 96  PHE A CB  1 
ATOM   503   C CG  . PHE A  1 94  ? 156.197 159.068 152.741 1.00 76.21  ? 96  PHE A CG  1 
ATOM   504   C CD1 . PHE A  1 94  ? 155.007 159.774 152.779 1.00 77.77  ? 96  PHE A CD1 1 
ATOM   505   C CD2 . PHE A  1 94  ? 157.204 159.514 151.905 1.00 81.49  ? 96  PHE A CD2 1 
ATOM   506   C CE1 . PHE A  1 94  ? 154.825 160.896 151.997 1.00 81.03  ? 96  PHE A CE1 1 
ATOM   507   C CE2 . PHE A  1 94  ? 157.025 160.637 151.121 1.00 84.96  ? 96  PHE A CE2 1 
ATOM   508   C CZ  . PHE A  1 94  ? 155.834 161.327 151.168 1.00 84.13  ? 96  PHE A CZ  1 
ATOM   509   N N   . GLY A  1 95  ? 156.242 154.425 153.032 1.00 71.34  ? 97  GLY A N   1 
ATOM   510   C CA  . GLY A  1 95  ? 156.687 153.131 153.506 1.00 74.53  ? 97  GLY A CA  1 
ATOM   511   C C   . GLY A  1 95  ? 156.016 151.978 152.792 1.00 79.23  ? 97  GLY A C   1 
ATOM   512   O O   . GLY A  1 95  ? 155.905 151.983 151.563 1.00 82.10  ? 97  GLY A O   1 
ATOM   513   N N   . SER A  1 96  ? 155.560 150.983 153.549 1.00 79.43  ? 98  SER A N   1 
ATOM   514   C CA  . SER A  1 96  ? 154.932 149.792 152.991 1.00 78.28  ? 98  SER A CA  1 
ATOM   515   C C   . SER A  1 96  ? 153.568 149.588 153.634 1.00 80.09  ? 98  SER A C   1 
ATOM   516   O O   . SER A  1 96  ? 153.469 149.464 154.860 1.00 82.59  ? 98  SER A O   1 
ATOM   517   C CB  . SER A  1 96  ? 155.814 148.562 153.204 1.00 80.06  ? 98  SER A CB  1 
ATOM   518   O OG  . SER A  1 96  ? 155.411 147.496 152.364 1.00 88.73  ? 98  SER A OG  1 
ATOM   519   N N   . ASN A  1 97  ? 152.525 149.549 152.803 1.00 78.38  ? 99  ASN A N   1 
ATOM   520   C CA  . ASN A  1 97  ? 151.165 149.214 153.232 1.00 76.52  ? 99  ASN A CA  1 
ATOM   521   C C   . ASN A  1 97  ? 150.659 150.142 154.333 1.00 79.25  ? 99  ASN A C   1 
ATOM   522   O O   . ASN A  1 97  ? 149.933 149.722 155.235 1.00 85.11  ? 99  ASN A O   1 
ATOM   523   C CB  . ASN A  1 97  ? 151.074 147.754 153.678 1.00 79.49  ? 99  ASN A CB  1 
ATOM   524   C CG  . ASN A  1 97  ? 151.690 146.803 152.679 1.00 85.33  ? 99  ASN A CG  1 
ATOM   525   O OD1 . ASN A  1 97  ? 152.906 146.776 152.499 1.00 89.99  ? 99  ASN A OD1 1 
ATOM   526   N ND2 . ASN A  1 97  ? 150.851 146.018 152.016 1.00 85.03  ? 99  ASN A ND2 1 
ATOM   527   N N   . ASN A  1 98  ? 151.026 151.415 154.256 1.00 77.72  ? 100 ASN A N   1 
ATOM   528   C CA  . ASN A  1 98  ? 150.522 152.405 155.195 1.00 74.30  ? 100 ASN A CA  1 
ATOM   529   C C   . ASN A  1 98  ? 149.224 153.002 154.673 1.00 79.09  ? 100 ASN A C   1 
ATOM   530   O O   . ASN A  1 98  ? 149.079 153.254 153.474 1.00 88.02  ? 100 ASN A O   1 
ATOM   531   C CB  . ASN A  1 98  ? 151.549 153.511 155.430 1.00 73.71  ? 100 ASN A CB  1 
ATOM   532   C CG  . ASN A  1 98  ? 152.833 152.990 156.028 1.00 78.34  ? 100 ASN A CG  1 
ATOM   533   O OD1 . ASN A  1 98  ? 152.945 152.830 157.241 1.00 76.69  ? 100 ASN A OD1 1 
ATOM   534   N ND2 . ASN A  1 98  ? 153.814 152.724 155.179 1.00 82.63  ? 100 ASN A ND2 1 
ATOM   535   N N   . ALA A  1 99  ? 148.279 153.221 155.582 1.00 76.26  ? 101 ALA A N   1 
ATOM   536   C CA  . ALA A  1 99  ? 146.987 153.813 155.255 1.00 77.01  ? 101 ALA A CA  1 
ATOM   537   C C   . ALA A  1 99  ? 146.781 155.024 156.152 1.00 83.80  ? 101 ALA A C   1 
ATOM   538   O O   . ALA A  1 99  ? 146.503 154.877 157.346 1.00 87.03  ? 101 ALA A O   1 
ATOM   539   C CB  . ALA A  1 99  ? 145.857 152.801 155.428 1.00 76.28  ? 101 ALA A CB  1 
ATOM   540   N N   . ALA A  1 100 ? 146.914 156.216 155.581 1.00 87.22  ? 102 ALA A N   1 
ATOM   541   C CA  . ALA A  1 100 ? 146.728 157.464 156.318 1.00 84.34  ? 102 ALA A CA  1 
ATOM   542   C C   . ALA A  1 100 ? 145.376 158.037 155.913 1.00 90.99  ? 102 ALA A C   1 
ATOM   543   O O   . ALA A  1 100 ? 145.253 158.742 154.912 1.00 93.37  ? 102 ALA A O   1 
ATOM   544   C CB  . ALA A  1 100 ? 147.865 158.438 156.040 1.00 82.36  ? 102 ALA A CB  1 
ATOM   545   N N   . ASP A  1 101 ? 144.352 157.731 156.704 1.00 91.69  ? 103 ASP A N   1 
ATOM   546   C CA  . ASP A  1 101 ? 142.997 158.210 156.457 1.00 88.05  ? 103 ASP A CA  1 
ATOM   547   C C   . ASP A  1 101 ? 142.632 159.155 157.596 1.00 93.34  ? 103 ASP A C   1 
ATOM   548   O O   . ASP A  1 101 ? 141.976 158.778 158.565 1.00 94.59  ? 103 ASP A O   1 
ATOM   549   C CB  . ASP A  1 101 ? 142.023 157.043 156.351 1.00 95.44  ? 103 ASP A CB  1 
ATOM   550   C CG  . ASP A  1 101 ? 142.440 156.031 155.304 1.00 108.40 ? 103 ASP A CG  1 
ATOM   551   O OD1 . ASP A  1 101 ? 143.520 155.425 155.461 1.00 109.92 ? 103 ASP A OD1 1 
ATOM   552   O OD2 . ASP A  1 101 ? 141.690 155.840 154.324 1.00 119.19 ? 103 ASP A OD2 1 
ATOM   553   N N   . GLY A  1 102 ? 143.047 160.408 157.455 1.00 91.34  ? 104 GLY A N   1 
ATOM   554   C CA  . GLY A  1 102 ? 142.813 161.416 158.467 1.00 83.14  ? 104 GLY A CA  1 
ATOM   555   C C   . GLY A  1 102 ? 143.369 162.753 158.032 1.00 87.22  ? 104 GLY A C   1 
ATOM   556   O O   . GLY A  1 102 ? 144.398 162.808 157.353 1.00 90.53  ? 104 GLY A O   1 
ATOM   557   N N   . VAL A  1 103 ? 142.696 163.840 158.405 1.00 89.76  ? 105 VAL A N   1 
ATOM   558   C CA  . VAL A  1 103 ? 143.137 165.164 157.992 1.00 86.88  ? 105 VAL A CA  1 
ATOM   559   C C   . VAL A  1 103 ? 144.460 165.490 158.669 1.00 86.68  ? 105 VAL A C   1 
ATOM   560   O O   . VAL A  1 103 ? 144.596 165.361 159.893 1.00 91.67  ? 105 VAL A O   1 
ATOM   561   C CB  . VAL A  1 103 ? 142.066 166.213 158.321 1.00 82.58  ? 105 VAL A CB  1 
ATOM   562   C CG1 . VAL A  1 103 ? 142.632 167.610 158.163 1.00 84.07  ? 105 VAL A CG1 1 
ATOM   563   C CG2 . VAL A  1 103 ? 140.849 166.020 157.433 1.00 83.61  ? 105 VAL A CG2 1 
ATOM   564   N N   . ASN A  1 104 ? 145.442 165.912 157.871 1.00 78.99  ? 106 ASN A N   1 
ATOM   565   C CA  . ASN A  1 104 ? 146.775 166.256 158.365 1.00 78.39  ? 106 ASN A CA  1 
ATOM   566   C C   . ASN A  1 104 ? 147.388 165.103 159.155 1.00 86.58  ? 106 ASN A C   1 
ATOM   567   O O   . ASN A  1 104 ? 148.040 165.300 160.182 1.00 95.31  ? 106 ASN A O   1 
ATOM   568   C CB  . ASN A  1 104 ? 146.739 167.537 159.197 1.00 81.74  ? 106 ASN A CB  1 
ATOM   569   C CG  . ASN A  1 104 ? 146.019 168.666 158.492 1.00 86.87  ? 106 ASN A CG  1 
ATOM   570   O OD1 . ASN A  1 104 ? 146.104 168.808 157.274 1.00 92.03  ? 106 ASN A OD1 1 
ATOM   571   N ND2 . ASN A  1 104 ? 145.303 169.479 159.258 1.00 90.07  ? 106 ASN A ND2 1 
ATOM   572   N N   . SER A  1 105 ? 147.180 163.884 158.667 1.00 84.97  ? 107 SER A N   1 
ATOM   573   C CA  . SER A  1 105 ? 147.656 162.678 159.327 1.00 83.49  ? 107 SER A CA  1 
ATOM   574   C C   . SER A  1 105 ? 148.792 162.057 158.528 1.00 86.17  ? 107 SER A C   1 
ATOM   575   O O   . SER A  1 105 ? 148.789 162.094 157.294 1.00 91.44  ? 107 SER A O   1 
ATOM   576   C CB  . SER A  1 105 ? 146.526 161.662 159.499 1.00 83.85  ? 107 SER A CB  1 
ATOM   577   O OG  . SER A  1 105 ? 146.512 160.736 158.429 1.00 86.42  ? 107 SER A OG  1 
ATOM   578   N N   . SER A  1 106 ? 149.762 161.484 159.238 1.00 81.68  ? 108 SER A N   1 
ATOM   579   C CA  . SER A  1 106 ? 150.946 160.900 158.624 1.00 75.62  ? 108 SER A CA  1 
ATOM   580   C C   . SER A  1 106 ? 151.131 159.478 159.128 1.00 77.08  ? 108 SER A C   1 
ATOM   581   O O   . SER A  1 106 ? 151.076 159.232 160.337 1.00 82.05  ? 108 SER A O   1 
ATOM   582   C CB  . SER A  1 106 ? 152.192 161.734 158.933 1.00 80.39  ? 108 SER A CB  1 
ATOM   583   O OG  . SER A  1 106 ? 151.916 163.119 158.822 1.00 87.70  ? 108 SER A OG  1 
ATOM   584   N N   . ALA A  1 107 ? 151.351 158.548 158.203 1.00 75.11  ? 109 ALA A N   1 
ATOM   585   C CA  . ALA A  1 107 ? 151.626 157.151 158.523 1.00 71.28  ? 109 ALA A CA  1 
ATOM   586   C C   . ALA A  1 107 ? 152.943 156.772 157.862 1.00 74.51  ? 109 ALA A C   1 
ATOM   587   O O   . ALA A  1 107 ? 153.016 156.657 156.635 1.00 81.09  ? 109 ALA A O   1 
ATOM   588   C CB  . ALA A  1 107 ? 150.492 156.243 158.053 1.00 73.34  ? 109 ALA A CB  1 
ATOM   589   N N   . PHE A  1 108 ? 153.980 156.579 158.672 1.00 70.88  ? 110 PHE A N   1 
ATOM   590   C CA  . PHE A  1 108 ? 155.318 156.288 158.176 1.00 69.07  ? 110 PHE A CA  1 
ATOM   591   C C   . PHE A  1 108 ? 155.785 154.969 158.767 1.00 75.83  ? 110 PHE A C   1 
ATOM   592   O O   . PHE A  1 108 ? 155.625 154.734 159.968 1.00 83.62  ? 110 PHE A O   1 
ATOM   593   C CB  . PHE A  1 108 ? 156.298 157.410 158.539 1.00 74.08  ? 110 PHE A CB  1 
ATOM   594   C CG  . PHE A  1 108 ? 156.157 158.644 157.690 1.00 74.36  ? 110 PHE A CG  1 
ATOM   595   C CD1 . PHE A  1 108 ? 154.991 159.388 157.709 1.00 76.72  ? 110 PHE A CD1 1 
ATOM   596   C CD2 . PHE A  1 108 ? 157.195 159.063 156.879 1.00 76.55  ? 110 PHE A CD2 1 
ATOM   597   C CE1 . PHE A  1 108 ? 154.863 160.521 156.932 1.00 78.78  ? 110 PHE A CE1 1 
ATOM   598   C CE2 . PHE A  1 108 ? 157.070 160.196 156.101 1.00 79.07  ? 110 PHE A CE2 1 
ATOM   599   C CZ  . PHE A  1 108 ? 155.903 160.924 156.128 1.00 79.83  ? 110 PHE A CZ  1 
ATOM   600   N N   . GLY A  1 109 ? 156.361 154.108 157.926 1.00 72.83  ? 111 GLY A N   1 
ATOM   601   C CA  . GLY A  1 109 ? 156.866 152.819 158.357 1.00 74.36  ? 111 GLY A CA  1 
ATOM   602   C C   . GLY A  1 109 ? 156.218 151.683 157.580 1.00 77.74  ? 111 GLY A C   1 
ATOM   603   O O   . GLY A  1 109 ? 156.015 151.780 156.364 1.00 81.62  ? 111 GLY A O   1 
ATOM   604   N N   . PHE A  1 110 ? 155.894 150.608 158.292 1.00 76.42  ? 112 PHE A N   1 
ATOM   605   C CA  . PHE A  1 110 ? 155.324 149.406 157.698 1.00 75.05  ? 112 PHE A CA  1 
ATOM   606   C C   . PHE A  1 110 ? 153.948 149.145 158.293 1.00 79.66  ? 112 PHE A C   1 
ATOM   607   O O   . PHE A  1 110 ? 153.819 148.975 159.509 1.00 81.40  ? 112 PHE A O   1 
ATOM   608   C CB  . PHE A  1 110 ? 156.237 148.203 157.924 1.00 76.29  ? 112 PHE A CB  1 
ATOM   609   C CG  . PHE A  1 110 ? 155.588 146.887 157.620 1.00 80.46  ? 112 PHE A CG  1 
ATOM   610   C CD1 . PHE A  1 110 ? 155.185 146.580 156.334 1.00 84.07  ? 112 PHE A CD1 1 
ATOM   611   C CD2 . PHE A  1 110 ? 155.377 145.957 158.621 1.00 80.14  ? 112 PHE A CD2 1 
ATOM   612   C CE1 . PHE A  1 110 ? 154.586 145.370 156.052 1.00 82.32  ? 112 PHE A CE1 1 
ATOM   613   C CE2 . PHE A  1 110 ? 154.779 144.746 158.345 1.00 79.87  ? 112 PHE A CE2 1 
ATOM   614   C CZ  . PHE A  1 110 ? 154.383 144.452 157.058 1.00 83.04  ? 112 PHE A CZ  1 
ATOM   615   N N   . LYS A  1 111 ? 152.934 149.094 157.431 1.00 79.80  ? 113 LYS A N   1 
ATOM   616   C CA  . LYS A  1 111 ? 151.556 148.769 157.803 1.00 78.26  ? 113 LYS A CA  1 
ATOM   617   C C   . LYS A  1 111 ? 151.106 149.569 159.029 1.00 80.02  ? 113 LYS A C   1 
ATOM   618   O O   . LYS A  1 111 ? 150.822 149.035 160.099 1.00 84.06  ? 113 LYS A O   1 
ATOM   619   C CB  . LYS A  1 111 ? 151.397 147.262 158.030 1.00 77.82  ? 113 LYS A CB  1 
ATOM   620   C CG  . LYS A  1 111 ? 149.954 146.814 158.236 1.00 83.93  ? 113 LYS A CG  1 
ATOM   621   C CD  . LYS A  1 111 ? 149.373 146.184 156.988 1.00 87.11  ? 113 LYS A CD  1 
ATOM   622   C CE  . LYS A  1 111 ? 147.862 146.330 156.944 1.00 91.87  ? 113 LYS A CE  1 
ATOM   623   N NZ  . LYS A  1 111 ? 147.441 147.748 157.102 1.00 91.70  ? 113 LYS A NZ  1 
ATOM   624   N N   . ASN A  1 112 ? 151.062 150.881 158.844 1.00 77.17  ? 114 ASN A N   1 
ATOM   625   C CA  . ASN A  1 112 ? 150.548 151.792 159.855 1.00 77.02  ? 114 ASN A CA  1 
ATOM   626   C C   . ASN A  1 112 ? 149.255 152.410 159.349 1.00 81.19  ? 114 ASN A C   1 
ATOM   627   O O   . ASN A  1 112 ? 149.191 152.879 158.208 1.00 89.17  ? 114 ASN A O   1 
ATOM   628   C CB  . ASN A  1 112 ? 151.567 152.882 160.188 1.00 75.66  ? 114 ASN A CB  1 
ATOM   629   C CG  . ASN A  1 112 ? 152.658 152.391 161.111 1.00 79.60  ? 114 ASN A CG  1 
ATOM   630   O OD1 . ASN A  1 112 ? 152.389 151.938 162.223 1.00 79.72  ? 114 ASN A OD1 1 
ATOM   631   N ND2 . ASN A  1 112 ? 153.901 152.479 160.656 1.00 83.37  ? 114 ASN A ND2 1 
ATOM   632   N N   . THR A  1 113 ? 148.228 152.403 160.192 1.00 77.85  ? 115 THR A N   1 
ATOM   633   C CA  . THR A  1 113 ? 146.929 152.972 159.854 1.00 79.56  ? 115 THR A CA  1 
ATOM   634   C C   . THR A  1 113 ? 146.639 154.107 160.824 1.00 80.69  ? 115 THR A C   1 
ATOM   635   O O   . THR A  1 113 ? 146.591 153.894 162.039 1.00 85.80  ? 115 THR A O   1 
ATOM   636   C CB  . THR A  1 113 ? 145.831 151.912 159.906 1.00 83.25  ? 115 THR A CB  1 
ATOM   637   O OG1 . THR A  1 113 ? 146.088 150.908 158.917 1.00 92.29  ? 115 THR A OG1 1 
ATOM   638   C CG2 . THR A  1 113 ? 144.474 152.542 159.641 1.00 82.31  ? 115 THR A CG2 1 
ATOM   639   N N   . VAL A  1 114 ? 146.449 155.308 160.292 1.00 79.49  ? 116 VAL A N   1 
ATOM   640   C CA  . VAL A  1 114 ? 146.103 156.478 161.088 1.00 79.76  ? 116 VAL A CA  1 
ATOM   641   C C   . VAL A  1 114 ? 144.728 156.947 160.644 1.00 84.00  ? 116 VAL A C   1 
ATOM   642   O O   . VAL A  1 114 ? 144.541 157.338 159.485 1.00 87.37  ? 116 VAL A O   1 
ATOM   643   C CB  . VAL A  1 114 ? 147.147 157.593 160.943 1.00 80.26  ? 116 VAL A CB  1 
ATOM   644   C CG1 . VAL A  1 114 ? 146.934 158.650 162.003 1.00 81.49  ? 116 VAL A CG1 1 
ATOM   645   C CG2 . VAL A  1 114 ? 148.544 157.019 161.048 1.00 85.65  ? 116 VAL A CG2 1 
ATOM   646   N N   . SER A  1 115 ? 143.767 156.909 161.563 1.00 83.19  ? 117 SER A N   1 
ATOM   647   C CA  . SER A  1 115 ? 142.388 157.265 161.260 1.00 85.42  ? 117 SER A CA  1 
ATOM   648   C C   . SER A  1 115 ? 141.938 158.529 161.977 1.00 88.66  ? 117 SER A C   1 
ATOM   649   O O   . SER A  1 115 ? 140.760 158.894 161.886 1.00 99.89  ? 117 SER A O   1 
ATOM   650   C CB  . SER A  1 115 ? 141.451 156.105 161.612 1.00 91.98  ? 117 SER A CB  1 
ATOM   651   O OG  . SER A  1 115 ? 140.096 156.508 161.536 1.00 108.55 ? 117 SER A OG  1 
ATOM   652   N N   . GLY A  1 116 ? 142.840 159.209 162.684 1.00 84.94  ? 118 GLY A N   1 
ATOM   653   C CA  . GLY A  1 116 ? 142.486 160.363 163.476 1.00 86.98  ? 118 GLY A CA  1 
ATOM   654   C C   . GLY A  1 116 ? 142.825 161.682 162.797 1.00 89.26  ? 118 GLY A C   1 
ATOM   655   O O   . GLY A  1 116 ? 143.333 161.742 161.681 1.00 91.72  ? 118 GLY A O   1 
ATOM   656   N N   . PHE A  1 117 ? 142.529 162.758 163.518 1.00 89.15  ? 119 PHE A N   1 
ATOM   657   C CA  . PHE A  1 117 ? 142.738 164.117 163.035 1.00 86.81  ? 119 PHE A CA  1 
ATOM   658   C C   . PHE A  1 117 ? 144.069 164.638 163.564 1.00 86.41  ? 119 PHE A C   1 
ATOM   659   O O   . PHE A  1 117 ? 144.284 164.680 164.780 1.00 94.01  ? 119 PHE A O   1 
ATOM   660   C CB  . PHE A  1 117 ? 141.576 165.005 163.480 1.00 85.89  ? 119 PHE A CB  1 
ATOM   661   C CG  . PHE A  1 117 ? 141.714 166.445 163.084 1.00 88.31  ? 119 PHE A CG  1 
ATOM   662   C CD1 . PHE A  1 117 ? 142.180 166.800 161.834 1.00 89.72  ? 119 PHE A CD1 1 
ATOM   663   C CD2 . PHE A  1 117 ? 141.347 167.448 163.963 1.00 90.04  ? 119 PHE A CD2 1 
ATOM   664   C CE1 . PHE A  1 117 ? 142.295 168.130 161.479 1.00 89.79  ? 119 PHE A CE1 1 
ATOM   665   C CE2 . PHE A  1 117 ? 141.461 168.775 163.611 1.00 92.28  ? 119 PHE A CE2 1 
ATOM   666   C CZ  . PHE A  1 117 ? 141.934 169.116 162.366 1.00 88.02  ? 119 PHE A CZ  1 
ATOM   667   N N   . ASN A  1 118 ? 144.962 165.023 162.648 1.00 79.40  ? 120 ASN A N   1 
ATOM   668   C CA  . ASN A  1 118 ? 146.289 165.538 162.992 1.00 79.51  ? 120 ASN A CA  1 
ATOM   669   C C   . ASN A  1 118 ? 147.109 164.530 163.792 1.00 84.04  ? 120 ASN A C   1 
ATOM   670   O O   . ASN A  1 118 ? 147.940 164.912 164.619 1.00 90.76  ? 120 ASN A O   1 
ATOM   671   C CB  . ASN A  1 118 ? 146.198 166.864 163.753 1.00 81.19  ? 120 ASN A CB  1 
ATOM   672   C CG  . ASN A  1 118 ? 146.241 168.067 162.837 1.00 84.19  ? 120 ASN A CG  1 
ATOM   673   O OD1 . ASN A  1 118 ? 147.261 168.345 162.210 1.00 83.82  ? 120 ASN A OD1 1 
ATOM   674   N ND2 . ASN A  1 118 ? 145.134 168.793 162.761 1.00 84.37  ? 120 ASN A ND2 1 
ATOM   675   N N   . SER A  1 119 ? 146.894 163.242 163.554 1.00 83.72  ? 121 SER A N   1 
ATOM   676   C CA  . SER A  1 119 ? 147.598 162.193 164.276 1.00 80.59  ? 121 SER A CA  1 
ATOM   677   C C   . SER A  1 119 ? 148.682 161.578 163.401 1.00 83.50  ? 121 SER A C   1 
ATOM   678   O O   . SER A  1 119 ? 148.601 161.599 162.171 1.00 90.45  ? 121 SER A O   1 
ATOM   679   C CB  . SER A  1 119 ? 146.628 161.109 164.745 1.00 82.94  ? 121 SER A CB  1 
ATOM   680   O OG  . SER A  1 119 ? 145.586 160.927 163.807 1.00 90.96  ? 121 SER A OG  1 
ATOM   681   N N   . SER A  1 120 ? 149.698 161.020 164.053 1.00 81.07  ? 122 SER A N   1 
ATOM   682   C CA  . SER A  1 120 ? 150.862 160.477 163.372 1.00 75.87  ? 122 SER A CA  1 
ATOM   683   C C   . SER A  1 120 ? 151.178 159.093 163.919 1.00 75.78  ? 122 SER A C   1 
ATOM   684   O O   . SER A  1 120 ? 150.772 158.733 165.025 1.00 82.42  ? 122 SER A O   1 
ATOM   685   C CB  . SER A  1 120 ? 152.082 161.392 163.531 1.00 83.28  ? 122 SER A CB  1 
ATOM   686   O OG  . SER A  1 120 ? 151.827 162.678 162.997 1.00 87.11  ? 122 SER A OG  1 
ATOM   687   N N   . ALA A  1 121 ? 151.903 158.312 163.122 1.00 74.87  ? 123 ALA A N   1 
ATOM   688   C CA  . ALA A  1 121 ? 152.331 156.987 163.548 1.00 73.26  ? 123 ALA A CA  1 
ATOM   689   C C   . ALA A  1 121 ? 153.605 156.619 162.808 1.00 75.62  ? 123 ALA A C   1 
ATOM   690   O O   . ALA A  1 121 ? 153.672 156.755 161.583 1.00 83.07  ? 123 ALA A O   1 
ATOM   691   C CB  . ALA A  1 121 ? 151.242 155.942 163.289 1.00 71.59  ? 123 ALA A CB  1 
ATOM   692   N N   . PHE A  1 122 ? 154.609 156.161 163.551 1.00 69.00  ? 124 PHE A N   1 
ATOM   693   C CA  . PHE A  1 122 ? 155.864 155.699 162.978 1.00 67.28  ? 124 PHE A CA  1 
ATOM   694   C C   . PHE A  1 122 ? 156.215 154.358 163.598 1.00 75.05  ? 124 PHE A C   1 
ATOM   695   O O   . PHE A  1 122 ? 156.147 154.201 164.820 1.00 80.43  ? 124 PHE A O   1 
ATOM   696   C CB  . PHE A  1 122 ? 156.993 156.706 163.213 1.00 70.74  ? 124 PHE A CB  1 
ATOM   697   C CG  . PHE A  1 122 ? 158.288 156.323 162.560 1.00 79.18  ? 124 PHE A CG  1 
ATOM   698   C CD1 . PHE A  1 122 ? 158.348 156.083 161.200 1.00 83.40  ? 124 PHE A CD1 1 
ATOM   699   C CD2 . PHE A  1 122 ? 159.444 156.197 163.307 1.00 79.23  ? 124 PHE A CD2 1 
ATOM   700   C CE1 . PHE A  1 122 ? 159.539 155.729 160.597 1.00 87.96  ? 124 PHE A CE1 1 
ATOM   701   C CE2 . PHE A  1 122 ? 160.636 155.841 162.710 1.00 76.82  ? 124 PHE A CE2 1 
ATOM   702   C CZ  . PHE A  1 122 ? 160.683 155.607 161.354 1.00 85.58  ? 124 PHE A CZ  1 
ATOM   703   N N   . GLY A  1 123 ? 156.587 153.396 162.761 1.00 73.89  ? 125 GLY A N   1 
ATOM   704   C CA  . GLY A  1 123 ? 156.892 152.066 163.248 1.00 74.75  ? 125 GLY A CA  1 
ATOM   705   C C   . GLY A  1 123 ? 156.294 150.976 162.386 1.00 81.75  ? 125 GLY A C   1 
ATOM   706   O O   . GLY A  1 123 ? 156.223 151.119 161.162 1.00 90.19  ? 125 GLY A O   1 
ATOM   707   N N   . SER A  1 124 ? 155.859 149.881 163.006 1.00 78.77  ? 126 SER A N   1 
ATOM   708   C CA  . SER A  1 124 ? 155.304 148.757 162.266 1.00 80.14  ? 126 SER A CA  1 
ATOM   709   C C   . SER A  1 124 ? 154.032 148.263 162.936 1.00 80.83  ? 126 SER A C   1 
ATOM   710   O O   . SER A  1 124 ? 154.008 148.058 164.152 1.00 84.92  ? 126 SER A O   1 
ATOM   711   C CB  . SER A  1 124 ? 156.316 147.612 162.162 1.00 82.88  ? 126 SER A CB  1 
ATOM   712   O OG  . SER A  1 124 ? 156.447 146.938 163.399 1.00 89.38  ? 126 SER A OG  1 
ATOM   713   N N   . GLN A  1 125 ? 152.983 148.078 162.133 1.00 78.83  ? 127 GLN A N   1 
ATOM   714   C CA  . GLN A  1 125 ? 151.756 147.400 162.557 1.00 79.37  ? 127 GLN A CA  1 
ATOM   715   C C   . GLN A  1 125 ? 151.096 148.103 163.743 1.00 83.05  ? 127 GLN A C   1 
ATOM   716   O O   . GLN A  1 125 ? 150.743 147.480 164.745 1.00 88.65  ? 127 GLN A O   1 
ATOM   717   C CB  . GLN A  1 125 ? 152.036 145.930 162.874 1.00 82.96  ? 127 GLN A CB  1 
ATOM   718   C CG  . GLN A  1 125 ? 152.746 145.196 161.752 1.00 86.54  ? 127 GLN A CG  1 
ATOM   719   C CD  . GLN A  1 125 ? 153.321 143.870 162.196 1.00 90.32  ? 127 GLN A CD  1 
ATOM   720   O OE1 . GLN A  1 125 ? 152.655 142.838 162.129 1.00 95.22  ? 127 GLN A OE1 1 
ATOM   721   N NE2 . GLN A  1 125 ? 154.566 143.889 162.653 1.00 90.88  ? 127 GLN A NE2 1 
ATOM   722   N N   . TYR A  1 126 ? 150.913 149.414 163.616 1.00 82.39  ? 128 TYR A N   1 
ATOM   723   C CA  . TYR A  1 126 ? 150.271 150.213 164.649 1.00 79.29  ? 128 TYR A CA  1 
ATOM   724   C C   . TYR A  1 126 ? 149.106 150.985 164.052 1.00 80.49  ? 128 TYR A C   1 
ATOM   725   O O   . TYR A  1 126 ? 149.173 151.439 162.906 1.00 85.68  ? 128 TYR A O   1 
ATOM   726   C CB  . TYR A  1 126 ? 151.260 151.186 165.298 1.00 76.63  ? 128 TYR A CB  1 
ATOM   727   C CG  . TYR A  1 126 ? 151.585 150.863 166.737 1.00 78.70  ? 128 TYR A CG  1 
ATOM   728   C CD1 . TYR A  1 126 ? 150.673 150.196 167.542 1.00 74.75  ? 128 TYR A CD1 1 
ATOM   729   C CD2 . TYR A  1 126 ? 152.804 151.224 167.290 1.00 81.46  ? 128 TYR A CD2 1 
ATOM   730   C CE1 . TYR A  1 126 ? 150.967 149.899 168.857 1.00 78.29  ? 128 TYR A CE1 1 
ATOM   731   C CE2 . TYR A  1 126 ? 153.106 150.932 168.603 1.00 81.21  ? 128 TYR A CE2 1 
ATOM   732   C CZ  . TYR A  1 126 ? 152.185 150.270 169.382 1.00 83.26  ? 128 TYR A CZ  1 
ATOM   733   O OH  . TYR A  1 126 ? 152.487 149.979 170.691 1.00 88.58  ? 128 TYR A OH  1 
ATOM   734   N N   . GLN A  1 127 ? 148.038 151.130 164.832 1.00 76.96  ? 129 GLN A N   1 
ATOM   735   C CA  . GLN A  1 127 ? 146.864 151.886 164.425 1.00 76.19  ? 129 GLN A CA  1 
ATOM   736   C C   . GLN A  1 127 ? 146.583 152.986 165.437 1.00 80.61  ? 129 GLN A C   1 
ATOM   737   O O   . GLN A  1 127 ? 146.669 152.765 166.648 1.00 86.15  ? 129 GLN A O   1 
ATOM   738   C CB  . GLN A  1 127 ? 145.635 150.987 164.286 1.00 77.13  ? 129 GLN A CB  1 
ATOM   739   C CG  . GLN A  1 127 ? 144.611 151.519 163.300 1.00 82.84  ? 129 GLN A CG  1 
ATOM   740   C CD  . GLN A  1 127 ? 143.220 150.990 163.561 1.00 89.27  ? 129 GLN A CD  1 
ATOM   741   O OE1 . GLN A  1 127 ? 142.888 150.619 164.683 1.00 93.40  ? 129 GLN A OE1 1 
ATOM   742   N NE2 . GLN A  1 127 ? 142.395 150.955 162.522 1.00 89.54  ? 129 GLN A NE2 1 
ATOM   743   N N   . VAL A  1 128 ? 146.249 154.171 164.934 1.00 81.93  ? 130 VAL A N   1 
ATOM   744   C CA  . VAL A  1 128 ? 145.965 155.337 165.765 1.00 81.20  ? 130 VAL A CA  1 
ATOM   745   C C   . VAL A  1 128 ? 144.622 155.890 165.307 1.00 82.42  ? 130 VAL A C   1 
ATOM   746   O O   . VAL A  1 128 ? 144.544 156.582 164.286 1.00 85.18  ? 130 VAL A O   1 
ATOM   747   C CB  . VAL A  1 128 ? 147.060 156.403 165.673 1.00 74.02  ? 130 VAL A CB  1 
ATOM   748   C CG1 . VAL A  1 128 ? 146.721 157.582 166.564 1.00 80.18  ? 130 VAL A CG1 1 
ATOM   749   C CG2 . VAL A  1 128 ? 148.405 155.817 166.053 1.00 75.17  ? 130 VAL A CG2 1 
ATOM   750   N N   . THR A  1 129 ? 143.563 155.587 166.053 1.00 82.50  ? 131 THR A N   1 
ATOM   751   C CA  . THR A  1 129 ? 142.239 156.110 165.753 1.00 83.70  ? 131 THR A CA  1 
ATOM   752   C C   . THR A  1 129 ? 141.890 157.349 166.564 1.00 88.60  ? 131 THR A C   1 
ATOM   753   O O   . THR A  1 129 ? 140.836 157.947 166.327 1.00 94.01  ? 131 THR A O   1 
ATOM   754   C CB  . THR A  1 129 ? 141.176 155.034 165.994 1.00 90.59  ? 131 THR A CB  1 
ATOM   755   O OG1 . THR A  1 129 ? 141.212 154.623 167.365 1.00 94.86  ? 131 THR A OG1 1 
ATOM   756   C CG2 . THR A  1 129 ? 141.429 153.830 165.104 1.00 90.07  ? 131 THR A CG2 1 
ATOM   757   N N   . GLY A  1 130 ? 142.741 157.748 167.506 1.00 87.43  ? 132 GLY A N   1 
ATOM   758   C CA  . GLY A  1 130 ? 142.471 158.924 168.302 1.00 86.80  ? 132 GLY A CA  1 
ATOM   759   C C   . GLY A  1 130 ? 142.801 160.210 167.574 1.00 89.17  ? 132 GLY A C   1 
ATOM   760   O O   . GLY A  1 130 ? 143.441 160.224 166.524 1.00 90.82  ? 132 GLY A O   1 
ATOM   761   N N   . ASN A  1 131 ? 142.355 161.315 168.160 1.00 90.44  ? 133 ASN A N   1 
ATOM   762   C CA  . ASN A  1 131 ? 142.569 162.642 167.601 1.00 87.60  ? 133 ASN A CA  1 
ATOM   763   C C   . ASN A  1 131 ? 143.764 163.291 168.284 1.00 92.08  ? 133 ASN A C   1 
ATOM   764   O O   . ASN A  1 131 ? 143.868 163.268 169.514 1.00 94.81  ? 133 ASN A O   1 
ATOM   765   C CB  . ASN A  1 131 ? 141.323 163.510 167.772 1.00 88.46  ? 133 ASN A CB  1 
ATOM   766   C CG  . ASN A  1 131 ? 140.396 163.435 166.579 1.00 93.96  ? 133 ASN A CG  1 
ATOM   767   O OD1 . ASN A  1 131 ? 140.553 162.577 165.711 1.00 97.24  ? 133 ASN A OD1 1 
ATOM   768   N ND2 . ASN A  1 131 ? 139.420 164.332 166.531 1.00 100.89 ? 133 ASN A ND2 1 
ATOM   769   N N   . PHE A  1 132 ? 144.659 163.868 167.480 1.00 88.93  ? 134 PHE A N   1 
ATOM   770   C CA  . PHE A  1 132 ? 145.888 164.486 167.978 1.00 84.95  ? 134 PHE A CA  1 
ATOM   771   C C   . PHE A  1 132 ? 146.710 163.496 168.797 1.00 85.55  ? 134 PHE A C   1 
ATOM   772   O O   . PHE A  1 132 ? 147.299 163.846 169.821 1.00 89.30  ? 134 PHE A O   1 
ATOM   773   C CB  . PHE A  1 132 ? 145.591 165.743 168.797 1.00 86.85  ? 134 PHE A CB  1 
ATOM   774   C CG  . PHE A  1 132 ? 144.392 166.507 168.324 1.00 88.08  ? 134 PHE A CG  1 
ATOM   775   C CD1 . PHE A  1 132 ? 144.391 167.122 167.088 1.00 90.33  ? 134 PHE A CD1 1 
ATOM   776   C CD2 . PHE A  1 132 ? 143.266 166.613 169.119 1.00 90.07  ? 134 PHE A CD2 1 
ATOM   777   C CE1 . PHE A  1 132 ? 143.292 167.829 166.653 1.00 91.81  ? 134 PHE A CE1 1 
ATOM   778   C CE2 . PHE A  1 132 ? 142.162 167.317 168.688 1.00 92.53  ? 134 PHE A CE2 1 
ATOM   779   C CZ  . PHE A  1 132 ? 142.175 167.926 167.452 1.00 93.16  ? 134 PHE A CZ  1 
ATOM   780   N N   . SER A  1 133 ? 146.749 162.249 168.346 1.00 84.40  ? 135 SER A N   1 
ATOM   781   C CA  . SER A  1 133 ? 147.447 161.175 169.032 1.00 81.16  ? 135 SER A CA  1 
ATOM   782   C C   . SER A  1 133 ? 148.629 160.707 168.191 1.00 83.19  ? 135 SER A C   1 
ATOM   783   O O   . SER A  1 133 ? 148.829 161.142 167.055 1.00 91.47  ? 135 SER A O   1 
ATOM   784   C CB  . SER A  1 133 ? 146.490 160.021 169.333 1.00 85.36  ? 135 SER A CB  1 
ATOM   785   O OG  . SER A  1 133 ? 145.295 160.494 169.928 1.00 94.97  ? 135 SER A OG  1 
ATOM   786   N N   . GLY A  1 134 ? 149.424 159.810 168.764 1.00 79.24  ? 136 GLY A N   1 
ATOM   787   C CA  . GLY A  1 134 ? 150.586 159.300 168.064 1.00 73.45  ? 136 GLY A CA  1 
ATOM   788   C C   . GLY A  1 134 ? 151.060 157.994 168.652 1.00 75.27  ? 136 GLY A C   1 
ATOM   789   O O   . GLY A  1 134 ? 150.760 157.659 169.801 1.00 81.87  ? 136 GLY A O   1 
ATOM   790   N N   . ALA A  1 135 ? 151.812 157.254 167.842 1.00 73.06  ? 137 ALA A N   1 
ATOM   791   C CA  . ALA A  1 135 ? 152.378 155.980 168.253 1.00 70.66  ? 137 ALA A CA  1 
ATOM   792   C C   . ALA A  1 135 ? 153.728 155.795 167.583 1.00 75.21  ? 137 ALA A C   1 
ATOM   793   O O   . ALA A  1 135 ? 153.878 156.062 166.388 1.00 79.71  ? 137 ALA A O   1 
ATOM   794   C CB  . ALA A  1 135 ? 151.451 154.813 167.901 1.00 69.40  ? 137 ALA A CB  1 
ATOM   795   N N   . PHE A  1 136 ? 154.707 155.334 168.358 1.00 72.89  ? 138 PHE A N   1 
ATOM   796   C CA  . PHE A  1 136 ? 156.060 155.102 167.854 1.00 68.39  ? 138 PHE A CA  1 
ATOM   797   C C   . PHE A  1 136 ? 156.537 153.772 168.425 1.00 72.49  ? 138 PHE A C   1 
ATOM   798   O O   . PHE A  1 136 ? 156.930 153.695 169.592 1.00 77.55  ? 138 PHE A O   1 
ATOM   799   C CB  . PHE A  1 136 ? 156.998 156.242 168.231 1.00 69.95  ? 138 PHE A CB  1 
ATOM   800   C CG  . PHE A  1 136 ? 158.445 155.947 167.968 1.00 78.76  ? 138 PHE A CG  1 
ATOM   801   C CD1 . PHE A  1 136 ? 158.874 155.588 166.703 1.00 77.60  ? 138 PHE A CD1 1 
ATOM   802   C CD2 . PHE A  1 136 ? 159.377 156.030 168.985 1.00 82.50  ? 138 PHE A CD2 1 
ATOM   803   C CE1 . PHE A  1 136 ? 160.206 155.316 166.461 1.00 74.66  ? 138 PHE A CE1 1 
ATOM   804   C CE2 . PHE A  1 136 ? 160.709 155.760 168.747 1.00 81.11  ? 138 PHE A CE2 1 
ATOM   805   C CZ  . PHE A  1 136 ? 161.123 155.402 167.483 1.00 77.11  ? 138 PHE A CZ  1 
ATOM   806   N N   . GLY A  1 137 ? 156.502 152.735 167.603 1.00 70.95  ? 139 GLY A N   1 
ATOM   807   C CA  . GLY A  1 137 ? 156.883 151.407 168.052 1.00 74.23  ? 139 GLY A CA  1 
ATOM   808   C C   . GLY A  1 137 ? 156.300 150.350 167.131 1.00 81.52  ? 139 GLY A C   1 
ATOM   809   O O   . GLY A  1 137 ? 156.013 150.617 165.965 1.00 87.72  ? 139 GLY A O   1 
ATOM   810   N N   . MET A  1 138 ? 156.135 149.152 167.682 1.00 79.16  ? 140 MET A N   1 
ATOM   811   C CA  . MET A  1 138 ? 155.603 148.019 166.943 1.00 80.23  ? 140 MET A CA  1 
ATOM   812   C C   . MET A  1 138 ? 154.369 147.471 167.643 1.00 84.61  ? 140 MET A C   1 
ATOM   813   O O   . MET A  1 138 ? 154.374 147.266 168.860 1.00 88.30  ? 140 MET A O   1 
ATOM   814   C CB  . MET A  1 138 ? 156.648 146.911 166.798 1.00 82.44  ? 140 MET A CB  1 
ATOM   815   C CG  . MET A  1 138 ? 156.049 145.547 166.516 1.00 88.81  ? 140 MET A CG  1 
ATOM   816   S SD  . MET A  1 138 ? 157.242 144.208 166.636 1.00 109.13 ? 140 MET A SD  1 
ATOM   817   C CE  . MET A  1 138 ? 156.659 143.371 168.106 1.00 95.99  ? 140 MET A CE  1 
ATOM   818   N N   . GLY A  1 139 ? 153.316 147.236 166.868 1.00 80.83  ? 141 GLY A N   1 
ATOM   819   C CA  . GLY A  1 139 ? 152.126 146.593 167.385 1.00 81.35  ? 141 GLY A CA  1 
ATOM   820   C C   . GLY A  1 139 ? 151.997 145.177 166.866 1.00 90.36  ? 141 GLY A C   1 
ATOM   821   O O   . GLY A  1 139 ? 152.971 144.419 166.880 1.00 96.21  ? 141 GLY A O   1 
ATOM   822   N N   . GLU A  1 140 ? 150.807 144.804 166.404 1.00 93.48  ? 142 GLU A N   1 
ATOM   823   C CA  . GLU A  1 140 ? 150.600 143.479 165.842 1.00 92.68  ? 142 GLU A CA  1 
ATOM   824   C C   . GLU A  1 140 ? 149.408 143.515 164.899 1.00 93.32  ? 142 GLU A C   1 
ATOM   825   O O   . GLU A  1 140 ? 148.399 144.164 165.186 1.00 97.19  ? 142 GLU A O   1 
ATOM   826   C CB  . GLU A  1 140 ? 150.375 142.433 166.936 1.00 97.07  ? 142 GLU A CB  1 
ATOM   827   C CG  . GLU A  1 140 ? 150.242 141.018 166.407 1.00 106.41 ? 142 GLU A CG  1 
ATOM   828   C CD  . GLU A  1 140 ? 150.284 139.981 167.505 1.00 119.45 ? 142 GLU A CD  1 
ATOM   829   O OE1 . GLU A  1 140 ? 149.542 138.982 167.405 1.00 121.19 ? 142 GLU A OE1 1 
ATOM   830   O OE2 . GLU A  1 140 ? 151.056 140.164 168.468 1.00 119.96 ? 142 GLU A OE2 1 
ATOM   831   N N   . PHE A  1 141 ? 149.535 142.814 163.774 1.00 88.05  ? 143 PHE A N   1 
ATOM   832   C CA  . PHE A  1 141 ? 148.480 142.751 162.764 1.00 88.69  ? 143 PHE A CA  1 
ATOM   833   C C   . PHE A  1 141 ? 148.432 141.326 162.222 1.00 97.01  ? 143 PHE A C   1 
ATOM   834   O O   . PHE A  1 141 ? 149.180 140.982 161.304 1.00 104.57 ? 143 PHE A O   1 
ATOM   835   C CB  . PHE A  1 141 ? 148.726 143.762 161.650 1.00 83.31  ? 143 PHE A CB  1 
ATOM   836   C CG  . PHE A  1 141 ? 147.727 143.690 160.533 1.00 86.48  ? 143 PHE A CG  1 
ATOM   837   C CD1 . PHE A  1 141 ? 146.467 144.241 160.678 1.00 91.16  ? 143 PHE A CD1 1 
ATOM   838   C CD2 . PHE A  1 141 ? 148.051 143.080 159.335 1.00 85.26  ? 143 PHE A CD2 1 
ATOM   839   C CE1 . PHE A  1 141 ? 145.547 144.178 159.651 1.00 92.33  ? 143 PHE A CE1 1 
ATOM   840   C CE2 . PHE A  1 141 ? 147.136 143.014 158.306 1.00 87.94  ? 143 PHE A CE2 1 
ATOM   841   C CZ  . PHE A  1 141 ? 145.883 143.565 158.464 1.00 90.74  ? 143 PHE A CZ  1 
ATOM   842   N N   . ASN A  1 142 ? 147.558 140.499 162.798 1.00 94.28  ? 144 ASN A N   1 
ATOM   843   C CA  . ASN A  1 142 ? 147.356 139.157 162.263 1.00 94.47  ? 144 ASN A CA  1 
ATOM   844   C C   . ASN A  1 142 ? 146.399 139.190 161.077 1.00 94.19  ? 144 ASN A C   1 
ATOM   845   O O   . ASN A  1 142 ? 146.771 138.833 159.955 1.00 99.22  ? 144 ASN A O   1 
ATOM   846   C CB  . ASN A  1 142 ? 146.836 138.224 163.359 1.00 100.64 ? 144 ASN A CB  1 
ATOM   847   C CG  . ASN A  1 142 ? 145.805 138.885 164.246 1.00 104.26 ? 144 ASN A CG  1 
ATOM   848   O OD1 . ASN A  1 142 ? 145.063 139.762 163.807 1.00 102.27 ? 144 ASN A OD1 1 
ATOM   849   N ND2 . ASN A  1 142 ? 145.752 138.467 165.505 1.00 109.35 ? 144 ASN A ND2 1 
ATOM   850   N N   . GLY A  1 143 ? 145.159 139.605 161.314 1.00 95.09  ? 145 GLY A N   1 
ATOM   851   C CA  . GLY A  1 143 ? 144.244 139.950 160.245 1.00 96.28  ? 145 GLY A CA  1 
ATOM   852   C C   . GLY A  1 143 ? 143.584 141.280 160.539 1.00 97.82  ? 145 GLY A C   1 
ATOM   853   O O   . GLY A  1 143 ? 142.982 141.907 159.663 1.00 94.32  ? 145 GLY A O   1 
ATOM   854   N N   . GLN A  1 144 ? 143.702 141.712 161.793 1.00 99.56  ? 146 GLN A N   1 
ATOM   855   C CA  . GLN A  1 144 ? 143.220 143.004 162.252 1.00 92.95  ? 146 GLN A CA  1 
ATOM   856   C C   . GLN A  1 144 ? 144.245 143.583 163.212 1.00 89.55  ? 146 GLN A C   1 
ATOM   857   O O   . GLN A  1 144 ? 145.048 142.852 163.797 1.00 94.91  ? 146 GLN A O   1 
ATOM   858   C CB  . GLN A  1 144 ? 141.857 142.906 162.955 1.00 91.22  ? 146 GLN A CB  1 
ATOM   859   C CG  . GLN A  1 144 ? 140.832 142.037 162.251 1.00 98.75  ? 146 GLN A CG  1 
ATOM   860   C CD  . GLN A  1 144 ? 140.068 142.796 161.188 1.00 107.76 ? 146 GLN A CD  1 
ATOM   861   O OE1 . GLN A  1 144 ? 140.103 144.025 161.143 1.00 109.49 ? 146 GLN A OE1 1 
ATOM   862   N NE2 . GLN A  1 144 ? 139.371 142.068 160.326 1.00 108.41 ? 146 GLN A NE2 1 
ATOM   863   N N   . TYR A  1 145 ? 144.217 144.902 163.368 1.00 85.04  ? 147 TYR A N   1 
ATOM   864   C CA  . TYR A  1 145 ? 145.115 145.556 164.309 1.00 85.66  ? 147 TYR A CA  1 
ATOM   865   C C   . TYR A  1 145 ? 144.727 145.176 165.732 1.00 88.90  ? 147 TYR A C   1 
ATOM   866   O O   . TYR A  1 145 ? 143.629 145.503 166.193 1.00 94.45  ? 147 TYR A O   1 
ATOM   867   C CB  . TYR A  1 145 ? 145.070 147.069 164.120 1.00 83.31  ? 147 TYR A CB  1 
ATOM   868   C CG  . TYR A  1 145 ? 145.754 147.539 162.859 1.00 83.33  ? 147 TYR A CG  1 
ATOM   869   C CD1 . TYR A  1 145 ? 147.129 147.719 162.819 1.00 84.21  ? 147 TYR A CD1 1 
ATOM   870   C CD2 . TYR A  1 145 ? 145.027 147.797 161.707 1.00 85.94  ? 147 TYR A CD2 1 
ATOM   871   C CE1 . TYR A  1 145 ? 147.759 148.146 161.669 1.00 89.58  ? 147 TYR A CE1 1 
ATOM   872   C CE2 . TYR A  1 145 ? 145.648 148.224 160.552 1.00 88.77  ? 147 TYR A CE2 1 
ATOM   873   C CZ  . TYR A  1 145 ? 147.014 148.398 160.539 1.00 92.83  ? 147 TYR A CZ  1 
ATOM   874   O OH  . TYR A  1 145 ? 147.637 148.824 159.389 1.00 94.80  ? 147 TYR A OH  1 
ATOM   875   N N   . GLN A  1 146 ? 145.626 144.480 166.425 1.00 86.69  ? 148 GLN A N   1 
ATOM   876   C CA  . GLN A  1 146 ? 145.360 144.029 167.783 1.00 89.79  ? 148 GLN A CA  1 
ATOM   877   C C   . GLN A  1 146 ? 145.684 145.079 168.833 1.00 92.98  ? 148 GLN A C   1 
ATOM   878   O O   . GLN A  1 146 ? 145.088 145.056 169.916 1.00 93.04  ? 148 GLN A O   1 
ATOM   879   C CB  . GLN A  1 146 ? 146.154 142.754 168.079 1.00 92.98  ? 148 GLN A CB  1 
ATOM   880   C CG  . GLN A  1 146 ? 145.925 141.646 167.070 1.00 99.43  ? 148 GLN A CG  1 
ATOM   881   C CD  . GLN A  1 146 ? 144.504 141.127 167.099 1.00 103.17 ? 148 GLN A CD  1 
ATOM   882   O OE1 . GLN A  1 146 ? 143.905 140.989 168.164 1.00 102.58 ? 148 GLN A OE1 1 
ATOM   883   N NE2 . GLN A  1 146 ? 143.952 140.843 165.926 1.00 105.54 ? 148 GLN A NE2 1 
ATOM   884   N N   . TYR A  1 147 ? 146.606 145.993 168.545 1.00 92.34  ? 149 TYR A N   1 
ATOM   885   C CA  . TYR A  1 147 ? 146.992 147.044 169.477 1.00 94.89  ? 149 TYR A CA  1 
ATOM   886   C C   . TYR A  1 147 ? 146.820 148.384 168.782 1.00 92.14  ? 149 TYR A C   1 
ATOM   887   O O   . TYR A  1 147 ? 147.480 148.649 167.773 1.00 93.26  ? 149 TYR A O   1 
ATOM   888   C CB  . TYR A  1 147 ? 148.436 146.854 169.947 1.00 93.30  ? 149 TYR A CB  1 
ATOM   889   C CG  . TYR A  1 147 ? 148.688 145.499 170.562 1.00 91.56  ? 149 TYR A CG  1 
ATOM   890   C CD1 . TYR A  1 147 ? 148.228 145.196 171.835 1.00 91.35  ? 149 TYR A CD1 1 
ATOM   891   C CD2 . TYR A  1 147 ? 149.376 144.517 169.864 1.00 92.89  ? 149 TYR A CD2 1 
ATOM   892   C CE1 . TYR A  1 147 ? 148.452 143.957 172.398 1.00 94.36  ? 149 TYR A CE1 1 
ATOM   893   C CE2 . TYR A  1 147 ? 149.605 143.276 170.418 1.00 96.38  ? 149 TYR A CE2 1 
ATOM   894   C CZ  . TYR A  1 147 ? 149.141 143.001 171.685 1.00 98.52  ? 149 TYR A CZ  1 
ATOM   895   O OH  . TYR A  1 147 ? 149.368 141.764 172.240 1.00 101.89 ? 149 TYR A OH  1 
ATOM   896   N N   . LYS A  1 148 ? 145.940 149.224 169.320 1.00 86.74  ? 150 LYS A N   1 
ATOM   897   C CA  . LYS A  1 148 ? 145.616 150.496 168.695 1.00 86.75  ? 150 LYS A CA  1 
ATOM   898   C C   . LYS A  1 148 ? 145.547 151.587 169.751 1.00 90.05  ? 150 LYS A C   1 
ATOM   899   O O   . LYS A  1 148 ? 145.277 151.330 170.926 1.00 91.27  ? 150 LYS A O   1 
ATOM   900   C CB  . LYS A  1 148 ? 144.289 150.427 167.932 1.00 87.04  ? 150 LYS A CB  1 
ATOM   901   C CG  . LYS A  1 148 ? 143.409 149.260 168.333 1.00 88.42  ? 150 LYS A CG  1 
ATOM   902   C CD  . LYS A  1 148 ? 142.243 149.105 167.376 1.00 93.52  ? 150 LYS A CD  1 
ATOM   903   C CE  . LYS A  1 148 ? 141.564 147.760 167.545 1.00 105.57 ? 150 LYS A CE  1 
ATOM   904   N NZ  . LYS A  1 148 ? 140.555 147.524 166.477 1.00 107.04 ? 150 LYS A NZ  1 
ATOM   905   N N   . ASN A  1 149 ? 145.793 152.817 169.310 1.00 87.83  ? 151 ASN A N   1 
ATOM   906   C CA  . ASN A  1 149 ? 145.656 154.003 170.146 1.00 84.72  ? 151 ASN A CA  1 
ATOM   907   C C   . ASN A  1 149 ? 144.321 154.659 169.815 1.00 88.76  ? 151 ASN A C   1 
ATOM   908   O O   . ASN A  1 149 ? 144.167 155.264 168.750 1.00 91.62  ? 151 ASN A O   1 
ATOM   909   C CB  . ASN A  1 149 ? 146.816 154.968 169.913 1.00 80.83  ? 151 ASN A CB  1 
ATOM   910   C CG  . ASN A  1 149 ? 146.890 156.056 170.962 1.00 90.36  ? 151 ASN A CG  1 
ATOM   911   O OD1 . ASN A  1 149 ? 145.985 156.210 171.779 1.00 97.29  ? 151 ASN A OD1 1 
ATOM   912   N ND2 . ASN A  1 149 ? 147.971 156.824 170.939 1.00 91.52  ? 151 ASN A ND2 1 
ATOM   913   N N   . GLU A  1 150 ? 143.359 154.540 170.727 1.00 87.89  ? 152 GLU A N   1 
ATOM   914   C CA  . GLU A  1 150 ? 142.028 155.097 170.531 1.00 90.72  ? 152 GLU A CA  1 
ATOM   915   C C   . GLU A  1 150 ? 141.769 156.319 171.400 1.00 93.73  ? 152 GLU A C   1 
ATOM   916   O O   . GLU A  1 150 ? 140.641 156.819 171.429 1.00 102.68 ? 152 GLU A O   1 
ATOM   917   C CB  . GLU A  1 150 ? 140.964 154.031 170.799 1.00 96.68  ? 152 GLU A CB  1 
ATOM   918   C CG  . GLU A  1 150 ? 141.244 152.697 170.136 1.00 100.16 ? 152 GLU A CG  1 
ATOM   919   C CD  . GLU A  1 150 ? 140.038 151.782 170.143 1.00 114.46 ? 152 GLU A CD  1 
ATOM   920   O OE1 . GLU A  1 150 ? 139.895 150.992 171.099 1.00 119.34 ? 152 GLU A OE1 1 
ATOM   921   O OE2 . GLU A  1 150 ? 139.231 151.854 169.194 1.00 120.45 ? 152 GLU A OE2 1 
ATOM   922   N N   . GLY A  1 151 ? 142.780 156.811 172.106 1.00 87.88  ? 153 GLY A N   1 
ATOM   923   C CA  . GLY A  1 151 ? 142.630 157.961 172.973 1.00 93.13  ? 153 GLY A CA  1 
ATOM   924   C C   . GLY A  1 151 ? 143.041 159.250 172.287 1.00 95.88  ? 153 GLY A C   1 
ATOM   925   O O   . GLY A  1 151 ? 143.878 159.254 171.389 1.00 102.04 ? 153 GLY A O   1 
ATOM   926   N N   . ASN A  1 152 ? 142.435 160.349 172.724 1.00 94.00  ? 154 ASN A N   1 
ATOM   927   C CA  . ASN A  1 152 ? 142.754 161.665 172.195 1.00 89.64  ? 154 ASN A CA  1 
ATOM   928   C C   . ASN A  1 152 ? 143.906 162.276 172.979 1.00 92.92  ? 154 ASN A C   1 
ATOM   929   O O   . ASN A  1 152 ? 144.004 162.100 174.197 1.00 97.56  ? 154 ASN A O   1 
ATOM   930   C CB  . ASN A  1 152 ? 141.534 162.582 172.260 1.00 90.66  ? 154 ASN A CB  1 
ATOM   931   C CG  . ASN A  1 152 ? 140.373 162.060 171.446 1.00 99.54  ? 154 ASN A CG  1 
ATOM   932   O OD1 . ASN A  1 152 ? 140.542 161.197 170.587 1.00 103.03 ? 154 ASN A OD1 1 
ATOM   933   N ND2 . ASN A  1 152 ? 139.182 162.580 171.714 1.00 103.32 ? 154 ASN A ND2 1 
ATOM   934   N N   . ASN A  1 153 ? 144.774 162.997 172.269 1.00 88.20  ? 155 ASN A N   1 
ATOM   935   C CA  . ASN A  1 153 ? 145.918 163.678 172.876 1.00 85.38  ? 155 ASN A CA  1 
ATOM   936   C C   . ASN A  1 153 ? 146.783 162.707 173.675 1.00 88.21  ? 155 ASN A C   1 
ATOM   937   O O   . ASN A  1 153 ? 147.259 163.023 174.766 1.00 98.34  ? 155 ASN A O   1 
ATOM   938   C CB  . ASN A  1 153 ? 145.459 164.843 173.755 1.00 89.47  ? 155 ASN A CB  1 
ATOM   939   C CG  . ASN A  1 153 ? 144.658 165.872 172.986 1.00 95.67  ? 155 ASN A CG  1 
ATOM   940   O OD1 . ASN A  1 153 ? 145.219 166.722 172.297 1.00 100.80 ? 155 ASN A OD1 1 
ATOM   941   N ND2 . ASN A  1 153 ? 143.338 165.799 173.100 1.00 94.52  ? 155 ASN A ND2 1 
ATOM   942   N N   . SER A  1 154 ? 146.991 161.513 173.126 1.00 84.34  ? 156 SER A N   1 
ATOM   943   C CA  . SER A  1 154 ? 147.727 160.460 173.807 1.00 81.15  ? 156 SER A CA  1 
ATOM   944   C C   . SER A  1 154 ? 148.823 159.925 172.898 1.00 78.86  ? 156 SER A C   1 
ATOM   945   O O   . SER A  1 154 ? 148.668 159.873 171.676 1.00 83.10  ? 156 SER A O   1 
ATOM   946   C CB  . SER A  1 154 ? 146.797 159.321 174.236 1.00 86.93  ? 156 SER A CB  1 
ATOM   947   O OG  . SER A  1 154 ? 146.031 158.851 173.142 1.00 95.20  ? 156 SER A OG  1 
ATOM   948   N N   . TYR A  1 155 ? 149.935 159.520 173.507 1.00 78.48  ? 157 TYR A N   1 
ATOM   949   C CA  . TYR A  1 155 ? 151.097 159.062 172.761 1.00 74.36  ? 157 TYR A CA  1 
ATOM   950   C C   . TYR A  1 155 ? 151.661 157.807 173.406 1.00 75.90  ? 157 TYR A C   1 
ATOM   951   O O   . TYR A  1 155 ? 151.753 157.716 174.632 1.00 81.77  ? 157 TYR A O   1 
ATOM   952   C CB  . TYR A  1 155 ? 152.173 160.151 172.695 1.00 71.07  ? 157 TYR A CB  1 
ATOM   953   C CG  . TYR A  1 155 ? 151.847 161.247 171.709 1.00 75.42  ? 157 TYR A CG  1 
ATOM   954   C CD1 . TYR A  1 155 ? 151.047 162.318 172.076 1.00 76.25  ? 157 TYR A CD1 1 
ATOM   955   C CD2 . TYR A  1 155 ? 152.335 161.208 170.412 1.00 78.79  ? 157 TYR A CD2 1 
ATOM   956   C CE1 . TYR A  1 155 ? 150.741 163.318 171.180 1.00 83.36  ? 157 TYR A CE1 1 
ATOM   957   C CE2 . TYR A  1 155 ? 152.034 162.204 169.508 1.00 80.64  ? 157 TYR A CE2 1 
ATOM   958   C CZ  . TYR A  1 155 ? 151.236 163.256 169.898 1.00 84.91  ? 157 TYR A CZ  1 
ATOM   959   O OH  . TYR A  1 155 ? 150.932 164.254 169.003 1.00 88.20  ? 157 TYR A OH  1 
ATOM   960   N N   . MET A  1 156 ? 152.038 156.842 172.570 1.00 73.25  ? 158 MET A N   1 
ATOM   961   C CA  . MET A  1 156 ? 152.615 155.585 173.026 1.00 72.37  ? 158 MET A CA  1 
ATOM   962   C C   . MET A  1 156 ? 153.948 155.364 172.331 1.00 75.60  ? 158 MET A C   1 
ATOM   963   O O   . MET A  1 156 ? 154.031 155.442 171.102 1.00 80.66  ? 158 MET A O   1 
ATOM   964   C CB  . MET A  1 156 ? 151.680 154.406 172.742 1.00 72.51  ? 158 MET A CB  1 
ATOM   965   C CG  . MET A  1 156 ? 150.205 154.752 172.796 1.00 84.96  ? 158 MET A CG  1 
ATOM   966   S SD  . MET A  1 156 ? 149.157 153.361 172.339 1.00 117.80 ? 158 MET A SD  1 
ATOM   967   C CE  . MET A  1 156 ? 150.086 152.680 170.972 1.00 87.46  ? 158 MET A CE  1 
ATOM   968   N N   . ILE A  1 157 ? 154.986 155.089 173.116 1.00 75.18  ? 159 ILE A N   1 
ATOM   969   C CA  . ILE A  1 157 ? 156.295 154.715 172.596 1.00 71.36  ? 159 ILE A CA  1 
ATOM   970   C C   . ILE A  1 157 ? 156.650 153.373 173.218 1.00 76.83  ? 159 ILE A C   1 
ATOM   971   O O   . ILE A  1 157 ? 156.851 153.283 174.436 1.00 83.44  ? 159 ILE A O   1 
ATOM   972   C CB  . ILE A  1 157 ? 157.373 155.763 172.903 1.00 70.41  ? 159 ILE A CB  1 
ATOM   973   C CG1 . ILE A  1 157 ? 157.142 157.028 172.076 1.00 68.49  ? 159 ILE A CG1 1 
ATOM   974   C CG2 . ILE A  1 157 ? 158.753 155.201 172.614 1.00 71.78  ? 159 ILE A CG2 1 
ATOM   975   C CD1 . ILE A  1 157 ? 156.346 158.092 172.794 1.00 72.51  ? 159 ILE A CD1 1 
ATOM   976   N N   . GLY A  1 158 ? 156.727 152.340 172.398 1.00 69.47  ? 160 GLY A N   1 
ATOM   977   C CA  . GLY A  1 158 ? 157.006 151.007 172.884 1.00 75.02  ? 160 GLY A CA  1 
ATOM   978   C C   . GLY A  1 158 ? 156.350 149.973 171.994 1.00 79.94  ? 160 GLY A C   1 
ATOM   979   O O   . GLY A  1 158 ? 155.870 150.275 170.907 1.00 82.53  ? 160 GLY A O   1 
ATOM   980   N N   . ASN A  1 159 ? 156.335 148.739 172.488 1.00 82.08  ? 161 ASN A N   1 
ATOM   981   C CA  . ASN A  1 159 ? 155.846 147.593 171.736 1.00 81.51  ? 161 ASN A CA  1 
ATOM   982   C C   . ASN A  1 159 ? 154.551 147.080 172.346 1.00 85.09  ? 161 ASN A C   1 
ATOM   983   O O   . ASN A  1 159 ? 154.461 146.907 173.566 1.00 86.45  ? 161 ASN A O   1 
ATOM   984   C CB  . ASN A  1 159 ? 156.889 146.474 171.713 1.00 82.26  ? 161 ASN A CB  1 
ATOM   985   C CG  . ASN A  1 159 ? 158.069 146.798 170.828 1.00 91.76  ? 161 ASN A CG  1 
ATOM   986   O OD1 . ASN A  1 159 ? 157.965 147.606 169.906 1.00 97.75  ? 161 ASN A OD1 1 
ATOM   987   N ND2 . ASN A  1 159 ? 159.205 146.170 171.104 1.00 92.70  ? 161 ASN A ND2 1 
ATOM   988   N N   . LYS A  1 160 ? 153.556 146.833 171.492 1.00 84.45  ? 162 LYS A N   1 
ATOM   989   C CA  . LYS A  1 160 ? 152.308 146.178 171.881 1.00 87.29  ? 162 LYS A CA  1 
ATOM   990   C C   . LYS A  1 160 ? 151.617 146.931 173.020 1.00 89.19  ? 162 LYS A C   1 
ATOM   991   O O   . LYS A  1 160 ? 151.402 146.406 174.113 1.00 93.64  ? 162 LYS A O   1 
ATOM   992   C CB  . LYS A  1 160 ? 152.564 144.714 172.253 1.00 87.73  ? 162 LYS A CB  1 
ATOM   993   C CG  . LYS A  1 160 ? 153.595 144.030 171.370 1.00 88.97  ? 162 LYS A CG  1 
ATOM   994   C CD  . LYS A  1 160 ? 153.138 142.657 170.922 1.00 95.92  ? 162 LYS A CD  1 
ATOM   995   C CE  . LYS A  1 160 ? 153.534 141.596 171.932 1.00 100.87 ? 162 LYS A CE  1 
ATOM   996   N NZ  . LYS A  1 160 ? 153.444 140.226 171.356 1.00 112.03 ? 162 LYS A NZ  1 
ATOM   997   N N   . ASN A  1 161 ? 151.266 148.181 172.738 1.00 82.61  ? 163 ASN A N   1 
ATOM   998   C CA  . ASN A  1 161 ? 150.623 149.055 173.706 1.00 82.34  ? 163 ASN A CA  1 
ATOM   999   C C   . ASN A  1 161 ? 149.194 149.344 173.270 1.00 89.13  ? 163 ASN A C   1 
ATOM   1000  O O   . ASN A  1 161 ? 148.908 149.482 172.078 1.00 97.05  ? 163 ASN A O   1 
ATOM   1001  C CB  . ASN A  1 161 ? 151.396 150.366 173.861 1.00 82.92  ? 163 ASN A CB  1 
ATOM   1002  C CG  . ASN A  1 161 ? 152.671 150.196 174.654 1.00 88.68  ? 163 ASN A CG  1 
ATOM   1003  O OD1 . ASN A  1 161 ? 152.855 149.198 175.348 1.00 93.35  ? 163 ASN A OD1 1 
ATOM   1004  N ND2 . ASN A  1 161 ? 153.567 151.169 174.550 1.00 87.91  ? 163 ASN A ND2 1 
ATOM   1005  N N   . LYS A  1 162 ? 148.298 149.437 174.249 1.00 87.16  ? 164 LYS A N   1 
ATOM   1006  C CA  . LYS A  1 162 ? 146.882 149.646 173.992 1.00 84.36  ? 164 LYS A CA  1 
ATOM   1007  C C   . LYS A  1 162 ? 146.360 150.800 174.831 1.00 89.11  ? 164 LYS A C   1 
ATOM   1008  O O   . LYS A  1 162 ? 146.694 150.923 176.013 1.00 98.00  ? 164 LYS A O   1 
ATOM   1009  C CB  . LYS A  1 162 ? 146.071 148.384 174.300 1.00 85.89  ? 164 LYS A CB  1 
ATOM   1010  C CG  . LYS A  1 162 ? 145.795 147.510 173.095 1.00 91.02  ? 164 LYS A CG  1 
ATOM   1011  C CD  . LYS A  1 162 ? 144.600 146.606 173.343 1.00 92.57  ? 164 LYS A CD  1 
ATOM   1012  C CE  . LYS A  1 162 ? 144.891 145.603 174.444 1.00 91.64  ? 164 LYS A CE  1 
ATOM   1013  N NZ  . LYS A  1 162 ? 144.460 144.229 174.070 1.00 89.74  ? 164 LYS A NZ  1 
ATOM   1014  N N   . ILE A  1 163 ? 145.538 151.644 174.212 1.00 84.44  ? 165 ILE A N   1 
ATOM   1015  C CA  . ILE A  1 163 ? 144.810 152.698 174.906 1.00 89.67  ? 165 ILE A CA  1 
ATOM   1016  C C   . ILE A  1 163 ? 143.350 152.597 174.489 1.00 98.71  ? 165 ILE A C   1 
ATOM   1017  O O   . ILE A  1 163 ? 143.030 152.737 173.303 1.00 102.71 ? 165 ILE A O   1 
ATOM   1018  C CB  . ILE A  1 163 ? 145.367 154.097 174.595 1.00 87.02  ? 165 ILE A CB  1 
ATOM   1019  C CG1 . ILE A  1 163 ? 146.828 154.197 175.035 1.00 88.91  ? 165 ILE A CG1 1 
ATOM   1020  C CG2 . ILE A  1 163 ? 144.527 155.162 175.278 1.00 90.40  ? 165 ILE A CG2 1 
ATOM   1021  C CD1 . ILE A  1 163 ? 147.349 155.613 175.118 1.00 86.06  ? 165 ILE A CD1 1 
ATOM   1022  N N   . ALA A  1 164 ? 142.472 152.355 175.457 1.00 101.07 ? 166 ALA A N   1 
ATOM   1023  C CA  . ALA A  1 164 ? 141.062 152.177 175.157 1.00 103.46 ? 166 ALA A CA  1 
ATOM   1024  C C   . ALA A  1 164 ? 140.413 153.509 174.796 1.00 108.61 ? 166 ALA A C   1 
ATOM   1025  O O   . ALA A  1 164 ? 140.903 154.588 175.141 1.00 110.86 ? 166 ALA A O   1 
ATOM   1026  C CB  . ALA A  1 164 ? 140.336 151.546 176.344 1.00 103.55 ? 166 ALA A CB  1 
ATOM   1027  N N   . SER A  1 165 ? 139.295 153.421 174.082 1.00 111.36 ? 167 SER A N   1 
ATOM   1028  C CA  . SER A  1 165 ? 138.550 154.613 173.707 1.00 112.91 ? 167 SER A CA  1 
ATOM   1029  C C   . SER A  1 165 ? 137.960 155.279 174.943 1.00 116.63 ? 167 SER A C   1 
ATOM   1030  O O   . SER A  1 165 ? 137.468 154.609 175.855 1.00 116.39 ? 167 SER A O   1 
ATOM   1031  C CB  . SER A  1 165 ? 137.441 154.259 172.719 1.00 110.66 ? 167 SER A CB  1 
ATOM   1032  O OG  . SER A  1 165 ? 136.946 155.418 172.075 1.00 113.82 ? 167 SER A OG  1 
ATOM   1033  N N   . GLY A  1 166 ? 138.010 156.608 174.969 1.00 113.49 ? 168 GLY A N   1 
ATOM   1034  C CA  . GLY A  1 166 ? 137.557 157.379 176.104 1.00 111.66 ? 168 GLY A CA  1 
ATOM   1035  C C   . GLY A  1 166 ? 138.629 157.687 177.127 1.00 112.06 ? 168 GLY A C   1 
ATOM   1036  O O   . GLY A  1 166 ? 138.374 158.471 178.050 1.00 111.22 ? 168 GLY A O   1 
ATOM   1037  N N   . SER A  1 167 ? 139.814 157.096 176.995 1.00 110.78 ? 169 SER A N   1 
ATOM   1038  C CA  . SER A  1 167 ? 140.943 157.380 177.873 1.00 105.46 ? 169 SER A CA  1 
ATOM   1039  C C   . SER A  1 167 ? 141.876 158.335 177.138 1.00 107.14 ? 169 SER A C   1 
ATOM   1040  O O   . SER A  1 167 ? 142.550 157.941 176.182 1.00 109.63 ? 169 SER A O   1 
ATOM   1041  C CB  . SER A  1 167 ? 141.663 156.092 178.264 1.00 105.18 ? 169 SER A CB  1 
ATOM   1042  O OG  . SER A  1 167 ? 140.813 155.241 179.012 1.00 111.72 ? 169 SER A OG  1 
ATOM   1043  N N   . ASP A  1 168 ? 141.918 159.585 177.587 1.00 104.85 ? 170 ASP A N   1 
ATOM   1044  C CA  . ASP A  1 168 ? 142.612 160.649 176.880 1.00 104.54 ? 170 ASP A CA  1 
ATOM   1045  C C   . ASP A  1 168 ? 143.738 161.215 177.736 1.00 104.86 ? 170 ASP A C   1 
ATOM   1046  O O   . ASP A  1 168 ? 143.788 161.019 178.953 1.00 103.63 ? 170 ASP A O   1 
ATOM   1047  C CB  . ASP A  1 168 ? 141.636 161.762 176.482 1.00 107.84 ? 170 ASP A CB  1 
ATOM   1048  C CG  . ASP A  1 168 ? 140.398 161.230 175.794 1.00 114.00 ? 170 ASP A CG  1 
ATOM   1049  O OD1 . ASP A  1 168 ? 140.536 160.367 174.902 1.00 113.42 ? 170 ASP A OD1 1 
ATOM   1050  O OD2 . ASP A  1 168 ? 139.285 161.673 176.146 1.00 115.94 ? 170 ASP A OD2 1 
ATOM   1051  N N   . ASP A  1 169 ? 144.645 161.931 177.071 1.00 105.86 ? 171 ASP A N   1 
ATOM   1052  C CA  . ASP A  1 169 ? 145.796 162.570 177.711 1.00 103.14 ? 171 ASP A CA  1 
ATOM   1053  C C   . ASP A  1 169 ? 146.635 161.559 178.489 1.00 100.05 ? 171 ASP A C   1 
ATOM   1054  O O   . ASP A  1 169 ? 147.043 161.793 179.627 1.00 104.23 ? 171 ASP A O   1 
ATOM   1055  C CB  . ASP A  1 169 ? 145.355 163.724 178.614 1.00 110.30 ? 171 ASP A CB  1 
ATOM   1056  C CG  . ASP A  1 169 ? 144.381 164.661 177.931 1.00 119.88 ? 171 ASP A CG  1 
ATOM   1057  O OD1 . ASP A  1 169 ? 143.252 164.231 177.622 1.00 118.08 ? 171 ASP A OD1 1 
ATOM   1058  O OD2 . ASP A  1 169 ? 144.745 165.833 177.702 1.00 126.65 ? 171 ASP A OD2 1 
ATOM   1059  N N   . ASN A  1 170 ? 146.898 160.421 177.856 1.00 93.97  ? 172 ASN A N   1 
ATOM   1060  C CA  . ASN A  1 170 ? 147.700 159.359 178.446 1.00 87.17  ? 172 ASN A CA  1 
ATOM   1061  C C   . ASN A  1 170 ? 148.998 159.211 177.670 1.00 84.29  ? 172 ASN A C   1 
ATOM   1062  O O   . ASN A  1 170 ? 149.018 159.349 176.445 1.00 89.18  ? 172 ASN A O   1 
ATOM   1063  C CB  . ASN A  1 170 ? 146.941 158.033 178.452 1.00 86.91  ? 172 ASN A CB  1 
ATOM   1064  C CG  . ASN A  1 170 ? 145.699 158.080 179.312 1.00 98.47  ? 172 ASN A CG  1 
ATOM   1065  O OD1 . ASN A  1 170 ? 145.721 158.601 180.425 1.00 99.46  ? 172 ASN A OD1 1 
ATOM   1066  N ND2 . ASN A  1 170 ? 144.604 157.539 178.798 1.00 107.38 ? 172 ASN A ND2 1 
ATOM   1067  N N   . PHE A  1 171 ? 150.084 158.935 178.383 1.00 80.25  ? 173 PHE A N   1 
ATOM   1068  C CA  . PHE A  1 171 ? 151.384 158.755 177.757 1.00 74.43  ? 173 PHE A CA  1 
ATOM   1069  C C   . PHE A  1 171 ? 152.008 157.458 178.241 1.00 75.82  ? 173 PHE A C   1 
ATOM   1070  O O   . PHE A  1 171 ? 151.978 157.150 179.435 1.00 79.65  ? 173 PHE A O   1 
ATOM   1071  C CB  . PHE A  1 171 ? 152.305 159.940 178.046 1.00 72.19  ? 173 PHE A CB  1 
ATOM   1072  C CG  . PHE A  1 171 ? 151.918 161.187 177.311 1.00 79.36  ? 173 PHE A CG  1 
ATOM   1073  C CD1 . PHE A  1 171 ? 150.954 162.037 177.821 1.00 86.60  ? 173 PHE A CD1 1 
ATOM   1074  C CD2 . PHE A  1 171 ? 152.500 161.495 176.095 1.00 82.24  ? 173 PHE A CD2 1 
ATOM   1075  C CE1 . PHE A  1 171 ? 150.589 163.179 177.138 1.00 93.27  ? 173 PHE A CE1 1 
ATOM   1076  C CE2 . PHE A  1 171 ? 152.138 162.635 175.409 1.00 89.04  ? 173 PHE A CE2 1 
ATOM   1077  C CZ  . PHE A  1 171 ? 151.180 163.476 175.930 1.00 92.45  ? 173 PHE A CZ  1 
ATOM   1078  N N   . ILE A  1 172 ? 152.569 156.699 177.304 1.00 74.36  ? 174 ILE A N   1 
ATOM   1079  C CA  . ILE A  1 172 ? 153.135 155.387 177.583 1.00 74.23  ? 174 ILE A CA  1 
ATOM   1080  C C   . ILE A  1 172 ? 154.571 155.361 177.084 1.00 78.05  ? 174 ILE A C   1 
ATOM   1081  O O   . ILE A  1 172 ? 154.840 155.719 175.932 1.00 83.94  ? 174 ILE A O   1 
ATOM   1082  C CB  . ILE A  1 172 ? 152.321 154.259 176.923 1.00 73.30  ? 174 ILE A CB  1 
ATOM   1083  C CG1 . ILE A  1 172 ? 150.837 154.395 177.267 1.00 77.70  ? 174 ILE A CG1 1 
ATOM   1084  C CG2 . ILE A  1 172 ? 152.853 152.907 177.351 1.00 75.25  ? 174 ILE A CG2 1 
ATOM   1085  C CD1 . ILE A  1 172 ? 150.014 153.179 176.910 1.00 86.48  ? 174 ILE A CD1 1 
ATOM   1086  N N   . LEU A  1 173 ? 155.489 154.937 177.951 1.00 72.95  ? 175 LEU A N   1 
ATOM   1087  C CA  . LEU A  1 173 ? 156.883 154.687 177.587 1.00 73.15  ? 175 LEU A CA  1 
ATOM   1088  C C   . LEU A  1 173 ? 157.219 153.295 178.112 1.00 80.14  ? 175 LEU A C   1 
ATOM   1089  O O   . LEU A  1 173 ? 157.779 153.143 179.199 1.00 85.36  ? 175 LEU A O   1 
ATOM   1090  C CB  . LEU A  1 173 ? 157.807 155.760 178.155 1.00 77.15  ? 175 LEU A CB  1 
ATOM   1091  C CG  . LEU A  1 173 ? 159.246 155.774 177.637 1.00 79.45  ? 175 LEU A CG  1 
ATOM   1092  C CD1 . LEU A  1 173 ? 159.272 156.036 176.144 1.00 74.58  ? 175 LEU A CD1 1 
ATOM   1093  C CD2 . LEU A  1 173 ? 160.071 156.812 178.375 1.00 83.69  ? 175 LEU A CD2 1 
ATOM   1094  N N   . GLY A  1 174 ? 156.871 152.280 177.334 1.00 79.65  ? 176 GLY A N   1 
ATOM   1095  C CA  . GLY A  1 174 ? 157.066 150.912 177.764 1.00 84.90  ? 176 GLY A CA  1 
ATOM   1096  C C   . GLY A  1 174 ? 156.396 149.952 176.807 1.00 89.21  ? 176 GLY A C   1 
ATOM   1097  O O   . GLY A  1 174 ? 155.825 150.347 175.786 1.00 93.01  ? 176 GLY A O   1 
ATOM   1098  N N   . ASN A  1 175 ? 156.475 148.675 177.162 1.00 86.95  ? 177 ASN A N   1 
ATOM   1099  C CA  . ASN A  1 175 ? 155.893 147.604 176.370 1.00 84.04  ? 177 ASN A CA  1 
ATOM   1100  C C   . ASN A  1 175 ? 154.783 146.913 177.149 1.00 89.28  ? 177 ASN A C   1 
ATOM   1101  O O   . ASN A  1 175 ? 154.791 146.887 178.383 1.00 95.02  ? 177 ASN A O   1 
ATOM   1102  C CB  . ASN A  1 175 ? 156.949 146.572 175.967 1.00 84.36  ? 177 ASN A CB  1 
ATOM   1103  C CG  . ASN A  1 175 ? 158.193 147.205 175.391 1.00 87.74  ? 177 ASN A CG  1 
ATOM   1104  O OD1 . ASN A  1 175 ? 158.124 147.998 174.453 1.00 94.80  ? 177 ASN A OD1 1 
ATOM   1105  N ND2 . ASN A  1 175 ? 159.345 146.857 175.950 1.00 89.64  ? 177 ASN A ND2 1 
ATOM   1106  N N   . ASN A  1 176 ? 153.828 146.352 176.406 1.00 87.95  ? 178 ASN A N   1 
ATOM   1107  C CA  . ASN A  1 176 ? 152.741 145.553 176.974 1.00 90.88  ? 178 ASN A CA  1 
ATOM   1108  C C   . ASN A  1 176 ? 151.949 146.340 178.014 1.00 93.39  ? 178 ASN A C   1 
ATOM   1109  O O   . ASN A  1 176 ? 151.541 145.804 179.046 1.00 98.68  ? 178 ASN A O   1 
ATOM   1110  C CB  . ASN A  1 176 ? 153.273 144.250 177.572 1.00 90.67  ? 178 ASN A CB  1 
ATOM   1111  C CG  . ASN A  1 176 ? 154.090 143.451 176.583 1.00 92.73  ? 178 ASN A CG  1 
ATOM   1112  O OD1 . ASN A  1 176 ? 153.587 143.029 175.542 1.00 99.36  ? 178 ASN A OD1 1 
ATOM   1113  N ND2 . ASN A  1 176 ? 155.360 143.236 176.902 1.00 91.12  ? 178 ASN A ND2 1 
ATOM   1114  N N   . VAL A  1 177 ? 151.728 147.621 177.744 1.00 85.81  ? 179 VAL A N   1 
ATOM   1115  C CA  . VAL A  1 177 ? 150.965 148.488 178.632 1.00 86.62  ? 179 VAL A CA  1 
ATOM   1116  C C   . VAL A  1 177 ? 149.586 148.692 178.026 1.00 92.80  ? 179 VAL A C   1 
ATOM   1117  O O   . VAL A  1 177 ? 149.451 149.311 176.964 1.00 93.35  ? 179 VAL A O   1 
ATOM   1118  C CB  . VAL A  1 177 ? 151.675 149.831 178.854 1.00 85.81  ? 179 VAL A CB  1 
ATOM   1119  C CG1 . VAL A  1 177 ? 150.812 150.746 179.701 1.00 87.90  ? 179 VAL A CG1 1 
ATOM   1120  C CG2 . VAL A  1 177 ? 153.029 149.613 179.505 1.00 89.18  ? 179 VAL A CG2 1 
ATOM   1121  N N   . HIS A  1 178 ? 148.563 148.176 178.698 1.00 94.52  ? 180 HIS A N   1 
ATOM   1122  C CA  . HIS A  1 178 ? 147.182 148.313 178.261 1.00 91.86  ? 180 HIS A CA  1 
ATOM   1123  C C   . HIS A  1 178 ? 146.449 149.246 179.212 1.00 93.65  ? 180 HIS A C   1 
ATOM   1124  O O   . HIS A  1 178 ? 146.451 149.026 180.428 1.00 102.34 ? 180 HIS A O   1 
ATOM   1125  C CB  . HIS A  1 178 ? 146.483 146.953 178.210 1.00 94.75  ? 180 HIS A CB  1 
ATOM   1126  C CG  . HIS A  1 178 ? 147.278 145.892 177.515 1.00 98.26  ? 180 HIS A CG  1 
ATOM   1127  N ND1 . HIS A  1 178 ? 147.824 146.072 176.263 1.00 97.35  ? 180 HIS A ND1 1 
ATOM   1128  C CD2 . HIS A  1 178 ? 147.618 144.639 177.897 1.00 98.69  ? 180 HIS A CD2 1 
ATOM   1129  C CE1 . HIS A  1 178 ? 148.467 144.976 175.904 1.00 95.45  ? 180 HIS A CE1 1 
ATOM   1130  N NE2 . HIS A  1 178 ? 148.358 144.091 176.878 1.00 99.91  ? 180 HIS A NE2 1 
ATOM   1131  N N   . ILE A  1 179 ? 145.825 150.280 178.659 1.00 90.90  ? 181 ILE A N   1 
ATOM   1132  C CA  . ILE A  1 179 ? 145.076 151.261 179.435 1.00 94.94  ? 181 ILE A CA  1 
ATOM   1133  C C   . ILE A  1 179 ? 143.598 151.052 179.145 1.00 100.65 ? 181 ILE A C   1 
ATOM   1134  O O   . ILE A  1 179 ? 143.175 151.082 177.982 1.00 100.35 ? 181 ILE A O   1 
ATOM   1135  C CB  . ILE A  1 179 ? 145.509 152.697 179.105 1.00 88.47  ? 181 ILE A CB  1 
ATOM   1136  C CG1 . ILE A  1 179 ? 146.996 152.885 179.410 1.00 84.64  ? 181 ILE A CG1 1 
ATOM   1137  C CG2 . ILE A  1 179 ? 144.671 153.696 179.884 1.00 95.48  ? 181 ILE A CG2 1 
ATOM   1138  C CD1 . ILE A  1 179 ? 147.444 154.328 179.415 1.00 90.92  ? 181 ILE A CD1 1 
ATOM   1139  N N   . GLY A  1 180 ? 142.815 150.838 180.196 1.00 101.98 ? 182 GLY A N   1 
ATOM   1140  C CA  . GLY A  1 180 ? 141.394 150.603 180.058 1.00 104.20 ? 182 GLY A CA  1 
ATOM   1141  C C   . GLY A  1 180 ? 140.619 151.893 179.897 1.00 112.68 ? 182 GLY A C   1 
ATOM   1142  O O   . GLY A  1 180 ? 141.179 152.972 179.690 1.00 117.60 ? 182 GLY A O   1 
ATOM   1143  N N   . GLY A  1 181 ? 139.299 151.772 179.992 1.00 113.79 ? 183 GLY A N   1 
ATOM   1144  C CA  . GLY A  1 181 ? 138.426 152.916 179.848 1.00 113.05 ? 183 GLY A CA  1 
ATOM   1145  C C   . GLY A  1 181 ? 138.394 153.787 181.091 1.00 116.53 ? 183 GLY A C   1 
ATOM   1146  O O   . GLY A  1 181 ? 138.581 153.316 182.209 1.00 115.68 ? 183 GLY A O   1 
ATOM   1147  N N   . GLY A  1 182 ? 138.148 155.075 180.875 1.00 114.42 ? 184 GLY A N   1 
ATOM   1148  C CA  . GLY A  1 182 ? 138.043 156.015 181.981 1.00 111.42 ? 184 GLY A CA  1 
ATOM   1149  C C   . GLY A  1 182 ? 139.322 156.207 182.764 1.00 110.79 ? 184 GLY A C   1 
ATOM   1150  O O   . GLY A  1 182 ? 139.294 156.219 184.001 1.00 111.43 ? 184 GLY A O   1 
ATOM   1151  N N   . ILE A  1 183 ? 140.450 156.354 182.073 1.00 109.40 ? 185 ILE A N   1 
ATOM   1152  C CA  . ILE A  1 183 ? 141.745 156.593 182.703 1.00 105.10 ? 185 ILE A CA  1 
ATOM   1153  C C   . ILE A  1 183 ? 142.389 157.752 181.953 1.00 106.68 ? 185 ILE A C   1 
ATOM   1154  O O   . ILE A  1 183 ? 142.932 157.567 180.858 1.00 110.78 ? 185 ILE A O   1 
ATOM   1155  C CB  . ILE A  1 183 ? 142.645 155.353 182.687 1.00 102.05 ? 185 ILE A CB  1 
ATOM   1156  C CG1 . ILE A  1 183 ? 142.030 154.238 183.530 1.00 104.62 ? 185 ILE A CG1 1 
ATOM   1157  C CG2 . ILE A  1 183 ? 144.029 155.694 183.211 1.00 104.30 ? 185 ILE A CG2 1 
ATOM   1158  C CD1 . ILE A  1 183 ? 142.779 152.932 183.447 1.00 106.64 ? 185 ILE A CD1 1 
ATOM   1159  N N   . ASN A  1 184 ? 142.325 158.947 182.529 1.00 105.31 ? 186 ASN A N   1 
ATOM   1160  C CA  . ASN A  1 184 ? 142.864 160.149 181.915 1.00 101.50 ? 186 ASN A CA  1 
ATOM   1161  C C   . ASN A  1 184 ? 144.048 160.672 182.717 1.00 101.07 ? 186 ASN A C   1 
ATOM   1162  O O   . ASN A  1 184 ? 144.188 160.397 183.911 1.00 102.39 ? 186 ASN A O   1 
ATOM   1163  C CB  . ASN A  1 184 ? 141.795 161.244 181.807 1.00 104.38 ? 186 ASN A CB  1 
ATOM   1164  C CG  . ASN A  1 184 ? 140.510 160.752 181.173 1.00 111.28 ? 186 ASN A CG  1 
ATOM   1165  O OD1 . ASN A  1 184 ? 140.252 159.552 181.109 1.00 112.56 ? 186 ASN A OD1 1 
ATOM   1166  N ND2 . ASN A  1 184 ? 139.693 161.684 180.699 1.00 116.76 ? 186 ASN A ND2 1 
ATOM   1167  N N   . ASN A  1 185 ? 144.903 161.436 182.034 1.00 98.59  ? 187 ASN A N   1 
ATOM   1168  C CA  . ASN A  1 185 ? 146.029 162.128 182.663 1.00 96.17  ? 187 ASN A CA  1 
ATOM   1169  C C   . ASN A  1 185 ? 146.950 161.153 183.394 1.00 98.27  ? 187 ASN A C   1 
ATOM   1170  O O   . ASN A  1 185 ? 147.257 161.320 184.574 1.00 101.25 ? 187 ASN A O   1 
ATOM   1171  C CB  . ASN A  1 185 ? 145.534 163.221 183.613 1.00 94.47  ? 187 ASN A CB  1 
ATOM   1172  C CG  . ASN A  1 185 ? 145.235 164.518 182.901 1.00 105.19 ? 187 ASN A CG  1 
ATOM   1173  O OD1 . ASN A  1 185 ? 145.886 165.534 183.139 1.00 109.16 ? 187 ASN A OD1 1 
ATOM   1174  N ND2 . ASN A  1 185 ? 144.242 164.494 182.021 1.00 112.31 ? 187 ASN A ND2 1 
ATOM   1175  N N   . SER A  1 186 ? 147.405 160.130 182.678 1.00 92.77  ? 188 SER A N   1 
ATOM   1176  C CA  . SER A  1 186 ? 148.227 159.090 183.273 1.00 87.31  ? 188 SER A CA  1 
ATOM   1177  C C   . SER A  1 186 ? 149.477 158.866 182.438 1.00 86.20  ? 188 SER A C   1 
ATOM   1178  O O   . SER A  1 186 ? 149.471 159.044 181.218 1.00 92.99  ? 188 SER A O   1 
ATOM   1179  C CB  . SER A  1 186 ? 147.452 157.778 183.409 1.00 92.76  ? 188 SER A CB  1 
ATOM   1180  O OG  . SER A  1 186 ? 146.473 157.873 184.428 1.00 99.87  ? 188 SER A OG  1 
ATOM   1181  N N   . VAL A  1 187 ? 150.555 158.478 183.115 1.00 80.12  ? 189 VAL A N   1 
ATOM   1182  C CA  . VAL A  1 187 ? 151.833 158.182 182.480 1.00 76.17  ? 189 VAL A CA  1 
ATOM   1183  C C   . VAL A  1 187 ? 152.277 156.797 182.923 1.00 79.41  ? 189 VAL A C   1 
ATOM   1184  O O   . VAL A  1 187 ? 152.258 156.489 184.120 1.00 85.15  ? 189 VAL A O   1 
ATOM   1185  C CB  . VAL A  1 187 ? 152.909 159.227 182.829 1.00 69.45  ? 189 VAL A CB  1 
ATOM   1186  C CG1 . VAL A  1 187 ? 154.112 159.069 181.918 1.00 72.87  ? 189 VAL A CG1 1 
ATOM   1187  C CG2 . VAL A  1 187 ? 152.343 160.629 182.725 1.00 67.31  ? 189 VAL A CG2 1 
ATOM   1188  N N   . ALA A  1 188 ? 152.674 155.966 181.964 1.00 75.75  ? 190 ALA A N   1 
ATOM   1189  C CA  . ALA A  1 188 ? 153.185 154.631 182.236 1.00 76.32  ? 190 ALA A CA  1 
ATOM   1190  C C   . ALA A  1 188 ? 154.622 154.542 181.747 1.00 80.80  ? 190 ALA A C   1 
ATOM   1191  O O   . ALA A  1 188 ? 154.910 154.872 180.593 1.00 84.38  ? 190 ALA A O   1 
ATOM   1192  C CB  . ALA A  1 188 ? 152.330 153.561 181.559 1.00 76.10  ? 190 ALA A CB  1 
ATOM   1193  N N   . LEU A  1 189 ? 155.517 154.094 182.622 1.00 78.01  ? 191 LEU A N   1 
ATOM   1194  C CA  . LEU A  1 189 ? 156.938 154.008 182.320 1.00 76.23  ? 191 LEU A CA  1 
ATOM   1195  C C   . LEU A  1 189 ? 157.421 152.581 182.523 1.00 83.07  ? 191 LEU A C   1 
ATOM   1196  O O   . LEU A  1 189 ? 157.116 151.957 183.544 1.00 90.03  ? 191 LEU A O   1 
ATOM   1197  C CB  . LEU A  1 189 ? 157.745 154.962 183.204 1.00 77.16  ? 191 LEU A CB  1 
ATOM   1198  C CG  . LEU A  1 189 ? 157.415 156.450 183.102 1.00 72.28  ? 191 LEU A CG  1 
ATOM   1199  C CD1 . LEU A  1 189 ? 158.206 157.237 184.130 1.00 76.94  ? 191 LEU A CD1 1 
ATOM   1200  C CD2 . LEU A  1 189 ? 157.696 156.965 181.703 1.00 70.97  ? 191 LEU A CD2 1 
ATOM   1201  N N   . GLY A  1 190 ? 158.171 152.070 181.554 1.00 82.14  ? 192 GLY A N   1 
ATOM   1202  C CA  . GLY A  1 190 ? 158.878 150.816 181.704 1.00 87.38  ? 192 GLY A CA  1 
ATOM   1203  C C   . GLY A  1 190 ? 158.137 149.638 181.096 1.00 91.35  ? 192 GLY A C   1 
ATOM   1204  O O   . GLY A  1 190 ? 156.955 149.701 180.751 1.00 90.95  ? 192 GLY A O   1 
ATOM   1205  N N   . ASN A  1 191 ? 158.877 148.540 180.974 1.00 94.06  ? 193 ASN A N   1 
ATOM   1206  C CA  . ASN A  1 191 ? 158.327 147.295 180.459 1.00 93.95  ? 193 ASN A CA  1 
ATOM   1207  C C   . ASN A  1 191 ? 157.255 146.747 181.392 1.00 97.48  ? 193 ASN A C   1 
ATOM   1208  O O   . ASN A  1 191 ? 157.423 146.726 182.614 1.00 101.39 ? 193 ASN A O   1 
ATOM   1209  C CB  . ASN A  1 191 ? 159.445 146.266 180.290 1.00 94.82  ? 193 ASN A CB  1 
ATOM   1210  C CG  . ASN A  1 191 ? 159.025 145.079 179.454 1.00 99.45  ? 193 ASN A CG  1 
ATOM   1211  O OD1 . ASN A  1 191 ? 158.455 145.235 178.377 1.00 101.21 ? 193 ASN A OD1 1 
ATOM   1212  N ND2 . ASN A  1 191 ? 159.309 143.881 179.946 1.00 98.98  ? 193 ASN A ND2 1 
ATOM   1213  N N   . ASN A  1 192 ? 156.144 146.304 180.801 1.00 92.80  ? 194 ASN A N   1 
ATOM   1214  C CA  . ASN A  1 192 ? 155.071 145.621 181.525 1.00 95.35  ? 194 ASN A CA  1 
ATOM   1215  C C   . ASN A  1 192 ? 154.495 146.475 182.650 1.00 99.56  ? 194 ASN A C   1 
ATOM   1216  O O   . ASN A  1 192 ? 154.110 145.955 183.700 1.00 102.65 ? 194 ASN A O   1 
ATOM   1217  C CB  . ASN A  1 192 ? 155.547 144.274 182.074 1.00 96.57  ? 194 ASN A CB  1 
ATOM   1218  C CG  . ASN A  1 192 ? 155.826 143.266 180.981 1.00 100.93 ? 194 ASN A CG  1 
ATOM   1219  O OD1 . ASN A  1 192 ? 155.614 143.540 179.800 1.00 104.14 ? 194 ASN A OD1 1 
ATOM   1220  N ND2 . ASN A  1 192 ? 156.310 142.093 181.368 1.00 101.35 ? 194 ASN A ND2 1 
ATOM   1221  N N   . SER A  1 193 ? 154.431 147.787 182.449 1.00 99.19  ? 195 SER A N   1 
ATOM   1222  C CA  . SER A  1 193 ? 153.831 148.657 183.445 1.00 99.56  ? 195 SER A CA  1 
ATOM   1223  C C   . SER A  1 193 ? 152.310 148.538 183.408 1.00 103.44 ? 195 SER A C   1 
ATOM   1224  O O   . SER A  1 193 ? 151.724 148.021 182.453 1.00 104.25 ? 195 SER A O   1 
ATOM   1225  C CB  . SER A  1 193 ? 154.254 150.107 183.220 1.00 95.39  ? 195 SER A CB  1 
ATOM   1226  O OG  . SER A  1 193 ? 155.602 150.303 183.605 1.00 94.26  ? 195 SER A OG  1 
ATOM   1227  N N   . THR A  1 194 ? 151.670 149.027 184.467 1.00 104.06 ? 196 THR A N   1 
ATOM   1228  C CA  . THR A  1 194 ? 150.226 148.908 184.614 1.00 111.14 ? 196 THR A CA  1 
ATOM   1229  C C   . THR A  1 194 ? 149.655 150.211 185.147 1.00 111.09 ? 196 THR A C   1 
ATOM   1230  O O   . THR A  1 194 ? 150.153 150.747 186.140 1.00 118.40 ? 196 THR A O   1 
ATOM   1231  C CB  . THR A  1 194 ? 149.862 147.752 185.554 1.00 115.36 ? 196 THR A CB  1 
ATOM   1232  O OG1 . THR A  1 194 ? 150.214 146.506 184.942 1.00 116.54 ? 196 THR A OG1 1 
ATOM   1233  C CG2 . THR A  1 194 ? 148.373 147.757 185.860 1.00 116.29 ? 196 THR A CG2 1 
ATOM   1234  N N   . VAL A  1 195 ? 148.609 150.709 184.493 1.00 108.19 ? 197 VAL A N   1 
ATOM   1235  C CA  . VAL A  1 195 ? 147.893 151.905 184.922 1.00 109.24 ? 197 VAL A CA  1 
ATOM   1236  C C   . VAL A  1 195 ? 146.496 151.490 185.356 1.00 113.27 ? 197 VAL A C   1 
ATOM   1237  O O   . VAL A  1 195 ? 145.789 150.797 184.614 1.00 117.05 ? 197 VAL A O   1 
ATOM   1238  C CB  . VAL A  1 195 ? 147.825 152.960 183.806 1.00 102.27 ? 197 VAL A CB  1 
ATOM   1239  C CG1 . VAL A  1 195 ? 147.581 154.332 184.400 1.00 98.42  ? 197 VAL A CG1 1 
ATOM   1240  C CG2 . VAL A  1 195 ? 149.098 152.946 182.988 1.00 105.21 ? 197 VAL A CG2 1 
ATOM   1241  N N   . SER A  1 196 ? 146.097 151.914 186.555 1.00 110.07 ? 198 SER A N   1 
ATOM   1242  C CA  . SER A  1 196 ? 144.808 151.530 187.108 1.00 117.26 ? 198 SER A CA  1 
ATOM   1243  C C   . SER A  1 196 ? 143.959 152.705 187.571 1.00 118.29 ? 198 SER A C   1 
ATOM   1244  O O   . SER A  1 196 ? 142.846 152.481 188.059 1.00 124.23 ? 198 SER A O   1 
ATOM   1245  C CB  . SER A  1 196 ? 145.001 150.560 188.283 1.00 123.50 ? 198 SER A CB  1 
ATOM   1246  O OG  . SER A  1 196 ? 143.833 150.496 189.082 1.00 134.38 ? 198 SER A OG  1 
ATOM   1247  N N   . ALA A  1 197 ? 144.437 153.938 187.436 1.00 113.17 ? 199 ALA A N   1 
ATOM   1248  C CA  . ALA A  1 197 ? 143.686 155.094 187.903 1.00 109.01 ? 199 ALA A CA  1 
ATOM   1249  C C   . ALA A  1 197 ? 144.132 156.321 187.122 1.00 107.15 ? 199 ALA A C   1 
ATOM   1250  O O   . ALA A  1 197 ? 145.116 156.288 186.379 1.00 110.51 ? 199 ALA A O   1 
ATOM   1251  C CB  . ALA A  1 197 ? 143.865 155.307 189.408 1.00 105.40 ? 199 ALA A CB  1 
ATOM   1252  N N   . SER A  1 198 ? 143.389 157.406 187.300 1.00 103.66 ? 200 SER A N   1 
ATOM   1253  C CA  . SER A  1 198 ? 143.676 158.667 186.637 1.00 101.88 ? 200 SER A CA  1 
ATOM   1254  C C   . SER A  1 198 ? 144.594 159.531 187.495 1.00 103.03 ? 200 SER A C   1 
ATOM   1255  O O   . SER A  1 198 ? 144.696 159.356 188.712 1.00 105.21 ? 200 SER A O   1 
ATOM   1256  C CB  . SER A  1 198 ? 142.380 159.419 186.335 1.00 103.91 ? 200 SER A CB  1 
ATOM   1257  O OG  . SER A  1 198 ? 141.687 158.827 185.251 1.00 108.73 ? 200 SER A OG  1 
ATOM   1258  N N   . ASN A  1 199 ? 145.263 160.478 186.835 1.00 100.40 ? 201 ASN A N   1 
ATOM   1259  C CA  . ASN A  1 199 ? 146.162 161.426 187.495 1.00 97.98  ? 201 ASN A CA  1 
ATOM   1260  C C   . ASN A  1 199 ? 147.238 160.708 188.305 1.00 98.65  ? 201 ASN A C   1 
ATOM   1261  O O   . ASN A  1 199 ? 147.541 161.074 189.442 1.00 103.52 ? 201 ASN A O   1 
ATOM   1262  C CB  . ASN A  1 199 ? 145.381 162.403 188.372 1.00 98.49  ? 201 ASN A CB  1 
ATOM   1263  C CG  . ASN A  1 199 ? 144.088 162.854 187.729 1.00 104.73 ? 201 ASN A CG  1 
ATOM   1264  O OD1 . ASN A  1 199 ? 144.091 163.441 186.648 1.00 107.71 ? 201 ASN A OD1 1 
ATOM   1265  N ND2 . ASN A  1 199 ? 142.971 162.581 188.391 1.00 108.54 ? 201 ASN A ND2 1 
ATOM   1266  N N   . THR A  1 200 ? 147.823 159.669 187.712 1.00 94.21  ? 202 THR A N   1 
ATOM   1267  C CA  . THR A  1 200 ? 148.886 158.914 188.357 1.00 93.05  ? 202 THR A CA  1 
ATOM   1268  C C   . THR A  1 200 ? 150.004 158.659 187.358 1.00 87.31  ? 202 THR A C   1 
ATOM   1269  O O   . THR A  1 200 ? 149.786 158.616 186.146 1.00 87.85  ? 202 THR A O   1 
ATOM   1270  C CB  . THR A  1 200 ? 148.387 157.575 188.918 1.00 97.58  ? 202 THR A CB  1 
ATOM   1271  O OG1 . THR A  1 200 ? 147.768 156.816 187.872 1.00 101.82 ? 202 THR A OG1 1 
ATOM   1272  C CG2 . THR A  1 200 ? 147.388 157.796 190.043 1.00 99.52  ? 202 THR A CG2 1 
ATOM   1273  N N   . VAL A  1 201 ? 151.211 158.490 187.888 1.00 83.13  ? 203 VAL A N   1 
ATOM   1274  C CA  . VAL A  1 201 ? 152.367 158.062 187.112 1.00 78.16  ? 203 VAL A CA  1 
ATOM   1275  C C   . VAL A  1 201 ? 152.747 156.676 187.606 1.00 84.71  ? 203 VAL A C   1 
ATOM   1276  O O   . VAL A  1 201 ? 153.077 156.501 188.785 1.00 90.46  ? 203 VAL A O   1 
ATOM   1277  C CB  . VAL A  1 201 ? 153.547 159.036 187.245 1.00 73.79  ? 203 VAL A CB  1 
ATOM   1278  C CG1 . VAL A  1 201 ? 154.837 158.368 186.803 1.00 73.77  ? 203 VAL A CG1 1 
ATOM   1279  C CG2 . VAL A  1 201 ? 153.290 160.289 186.432 1.00 78.44  ? 203 VAL A CG2 1 
ATOM   1280  N N   . SER A  1 202 ? 152.697 155.694 186.714 1.00 83.58  ? 204 SER A N   1 
ATOM   1281  C CA  . SER A  1 202 ? 152.932 154.305 187.077 1.00 83.75  ? 204 SER A CA  1 
ATOM   1282  C C   . SER A  1 202 ? 154.327 153.891 186.634 1.00 88.44  ? 204 SER A C   1 
ATOM   1283  O O   . SER A  1 202 ? 154.719 154.133 185.488 1.00 89.50  ? 204 SER A O   1 
ATOM   1284  C CB  . SER A  1 202 ? 151.883 153.391 186.447 1.00 95.41  ? 204 SER A CB  1 
ATOM   1285  O OG  . SER A  1 202 ? 152.119 152.038 186.792 1.00 101.89 ? 204 SER A OG  1 
ATOM   1286  N N   . VAL A  1 203 ? 155.067 153.264 187.545 1.00 89.40  ? 205 VAL A N   1 
ATOM   1287  C CA  . VAL A  1 203 ? 156.438 152.845 187.306 1.00 85.33  ? 205 VAL A CA  1 
ATOM   1288  C C   . VAL A  1 203 ? 156.543 151.332 187.145 1.00 91.69  ? 205 VAL A C   1 
ATOM   1289  O O   . VAL A  1 203 ? 157.520 150.833 186.585 1.00 94.39  ? 205 VAL A O   1 
ATOM   1290  C CB  . VAL A  1 203 ? 157.360 153.357 188.432 1.00 81.68  ? 205 VAL A CB  1 
ATOM   1291  C CG1 . VAL A  1 203 ? 158.803 152.990 188.185 1.00 85.38  ? 205 VAL A CG1 1 
ATOM   1292  C CG2 . VAL A  1 203 ? 157.221 154.860 188.574 1.00 86.44  ? 205 VAL A CG2 1 
ATOM   1293  N N   . GLY A  1 204 ? 155.527 150.596 187.576 1.00 92.92  ? 206 GLY A N   1 
ATOM   1294  C CA  . GLY A  1 204 ? 155.525 149.157 187.425 1.00 94.44  ? 206 GLY A CA  1 
ATOM   1295  C C   . GLY A  1 204 ? 154.119 148.616 187.583 1.00 102.96 ? 206 GLY A C   1 
ATOM   1296  O O   . GLY A  1 204 ? 153.140 149.365 187.561 1.00 102.58 ? 206 GLY A O   1 
ATOM   1297  N N   . SER A  1 205 ? 154.040 147.301 187.735 1.00 107.40 ? 207 SER A N   1 
ATOM   1298  C CA  . SER A  1 205 ? 152.779 146.606 187.949 1.00 105.63 ? 207 SER A CA  1 
ATOM   1299  C C   . SER A  1 205 ? 152.731 146.071 189.376 1.00 108.82 ? 207 SER A C   1 
ATOM   1300  O O   . SER A  1 205 ? 153.647 146.279 190.174 1.00 112.34 ? 207 SER A O   1 
ATOM   1301  C CB  . SER A  1 205 ? 152.601 145.474 186.933 1.00 105.97 ? 207 SER A CB  1 
ATOM   1302  O OG  . SER A  1 205 ? 153.777 144.692 186.835 1.00 111.36 ? 207 SER A OG  1 
ATOM   1303  N N   . SER A  1 206 ? 151.639 145.374 189.695 1.00 111.70 ? 208 SER A N   1 
ATOM   1304  C CA  . SER A  1 206 ? 151.499 144.783 191.020 1.00 116.26 ? 208 SER A CA  1 
ATOM   1305  C C   . SER A  1 206 ? 152.495 143.657 191.259 1.00 119.51 ? 208 SER A C   1 
ATOM   1306  O O   . SER A  1 206 ? 152.772 143.327 192.417 1.00 120.59 ? 208 SER A O   1 
ATOM   1307  C CB  . SER A  1 206 ? 150.074 144.265 191.219 1.00 118.99 ? 208 SER A CB  1 
ATOM   1308  O OG  . SER A  1 206 ? 149.137 145.327 191.181 1.00 123.19 ? 208 SER A OG  1 
ATOM   1309  N N   . THR A  1 207 ? 153.038 143.064 190.198 1.00 118.63 ? 209 THR A N   1 
ATOM   1310  C CA  . THR A  1 207 ? 154.015 141.989 190.310 1.00 120.11 ? 209 THR A CA  1 
ATOM   1311  C C   . THR A  1 207 ? 155.450 142.502 190.300 1.00 122.72 ? 209 THR A C   1 
ATOM   1312  O O   . THR A  1 207 ? 156.265 142.078 191.123 1.00 121.31 ? 209 THR A O   1 
ATOM   1313  C CB  . THR A  1 207 ? 153.818 140.978 189.175 1.00 121.56 ? 209 THR A CB  1 
ATOM   1314  O OG1 . THR A  1 207 ? 154.414 141.482 187.974 1.00 124.45 ? 209 THR A OG1 1 
ATOM   1315  C CG2 . THR A  1 207 ? 152.338 140.734 188.935 1.00 114.44 ? 209 THR A CG2 1 
ATOM   1316  N N   . LEU A  1 208 ? 155.773 143.408 189.382 1.00 121.08 ? 210 LEU A N   1 
ATOM   1317  C CA  . LEU A  1 208 ? 157.103 143.993 189.280 1.00 115.68 ? 210 LEU A CA  1 
ATOM   1318  C C   . LEU A  1 208 ? 157.022 145.467 189.646 1.00 113.44 ? 210 LEU A C   1 
ATOM   1319  O O   . LEU A  1 208 ? 156.345 146.244 188.963 1.00 113.51 ? 210 LEU A O   1 
ATOM   1320  C CB  . LEU A  1 208 ? 157.674 143.820 187.873 1.00 114.94 ? 210 LEU A CB  1 
ATOM   1321  C CG  . LEU A  1 208 ? 159.075 144.392 187.656 1.00 117.22 ? 210 LEU A CG  1 
ATOM   1322  C CD1 . LEU A  1 208 ? 160.113 143.569 188.401 1.00 117.20 ? 210 LEU A CD1 1 
ATOM   1323  C CD2 . LEU A  1 208 ? 159.406 144.464 186.174 1.00 113.85 ? 210 LEU A CD2 1 
ATOM   1324  N N   . LYS A  1 209 ? 157.710 145.848 190.717 1.00 109.53 ? 211 LYS A N   1 
ATOM   1325  C CA  . LYS A  1 209 ? 157.753 147.225 191.183 1.00 105.12 ? 211 LYS A CA  1 
ATOM   1326  C C   . LYS A  1 209 ? 159.181 147.739 191.080 1.00 105.86 ? 211 LYS A C   1 
ATOM   1327  O O   . LYS A  1 209 ? 160.106 147.121 191.616 1.00 105.54 ? 211 LYS A O   1 
ATOM   1328  C CB  . LYS A  1 209 ? 157.248 147.327 192.622 1.00 96.30  ? 211 LYS A CB  1 
ATOM   1329  C CG  . LYS A  1 209 ? 155.815 146.861 192.791 1.00 102.56 ? 211 LYS A CG  1 
ATOM   1330  C CD  . LYS A  1 209 ? 155.382 146.902 194.242 1.00 102.81 ? 211 LYS A CD  1 
ATOM   1331  C CE  . LYS A  1 209 ? 153.872 146.988 194.352 1.00 105.26 ? 211 LYS A CE  1 
ATOM   1332  N NZ  . LYS A  1 209 ? 153.242 145.640 194.342 1.00 111.26 ? 211 LYS A NZ  1 
ATOM   1333  N N   . ARG A  1 210 ? 159.355 148.863 190.396 1.00 101.63 ? 212 ARG A N   1 
ATOM   1334  C CA  . ARG A  1 210 ? 160.677 149.420 190.160 1.00 91.75  ? 212 ARG A CA  1 
ATOM   1335  C C   . ARG A  1 210 ? 161.052 150.407 191.256 1.00 93.76  ? 212 ARG A C   1 
ATOM   1336  O O   . ARG A  1 210 ? 160.191 151.037 191.876 1.00 95.40  ? 212 ARG A O   1 
ATOM   1337  C CB  . ARG A  1 210 ? 160.733 150.125 188.806 1.00 79.33  ? 212 ARG A CB  1 
ATOM   1338  C CG  . ARG A  1 210 ? 160.824 149.206 187.609 1.00 71.65  ? 212 ARG A CG  1 
ATOM   1339  C CD  . ARG A  1 210 ? 160.790 150.010 186.323 1.00 76.00  ? 212 ARG A CD  1 
ATOM   1340  N NE  . ARG A  1 210 ? 160.907 149.162 185.145 1.00 80.26  ? 212 ARG A NE  1 
ATOM   1341  C CZ  . ARG A  1 210 ? 159.889 148.539 184.569 1.00 89.44  ? 212 ARG A CZ  1 
ATOM   1342  N NH1 . ARG A  1 210 ? 158.655 148.662 185.030 1.00 92.70  ? 212 ARG A NH1 1 
ATOM   1343  N NH2 . ARG A  1 210 ? 160.113 147.774 183.506 1.00 95.42  ? 212 ARG A NH2 1 
ATOM   1344  N N   . LYS A  1 211 ? 162.352 150.536 191.487 1.00 93.90  ? 213 LYS A N   1 
ATOM   1345  C CA  . LYS A  1 211 ? 162.882 151.563 192.367 1.00 90.03  ? 213 LYS A CA  1 
ATOM   1346  C C   . LYS A  1 211 ? 163.195 152.816 191.562 1.00 97.38  ? 213 LYS A C   1 
ATOM   1347  O O   . LYS A  1 211 ? 163.490 152.751 190.366 1.00 105.38 ? 213 LYS A O   1 
ATOM   1348  C CB  . LYS A  1 211 ? 164.146 151.079 193.076 1.00 86.99  ? 213 LYS A CB  1 
ATOM   1349  C CG  . LYS A  1 211 ? 163.913 150.001 194.114 1.00 92.13  ? 213 LYS A CG  1 
ATOM   1350  C CD  . LYS A  1 211 ? 165.230 149.397 194.568 1.00 96.16  ? 213 LYS A CD  1 
ATOM   1351  C CE  . LYS A  1 211 ? 166.129 150.450 195.190 1.00 98.40  ? 213 LYS A CE  1 
ATOM   1352  N NZ  . LYS A  1 211 ? 167.372 149.856 195.753 1.00 102.40 ? 213 LYS A NZ  1 
ATOM   1353  N N   . ILE A  1 212 ? 163.131 153.962 192.229 1.00 94.87  ? 214 ILE A N   1 
ATOM   1354  C CA  . ILE A  1 212 ? 163.516 155.236 191.635 1.00 96.63  ? 214 ILE A CA  1 
ATOM   1355  C C   . ILE A  1 212 ? 164.813 155.663 192.306 1.00 101.79 ? 214 ILE A C   1 
ATOM   1356  O O   . ILE A  1 212 ? 164.827 155.998 193.497 1.00 104.32 ? 214 ILE A O   1 
ATOM   1357  C CB  . ILE A  1 212 ? 162.423 156.299 191.788 1.00 88.43  ? 214 ILE A CB  1 
ATOM   1358  C CG1 . ILE A  1 212 ? 161.081 155.749 191.308 1.00 81.74  ? 214 ILE A CG1 1 
ATOM   1359  C CG2 . ILE A  1 212 ? 162.778 157.538 190.992 1.00 92.54  ? 214 ILE A CG2 1 
ATOM   1360  C CD1 . ILE A  1 212 ? 159.913 156.660 191.596 1.00 80.18  ? 214 ILE A CD1 1 
ATOM   1361  N N   . VAL A  1 213 ? 165.899 155.656 191.545 1.00 98.38  ? 215 VAL A N   1 
ATOM   1362  C CA  . VAL A  1 213 ? 167.221 155.891 192.082 1.00 98.15  ? 215 VAL A CA  1 
ATOM   1363  C C   . VAL A  1 213 ? 167.696 157.278 191.665 1.00 103.19 ? 215 VAL A C   1 
ATOM   1364  O O   . VAL A  1 213 ? 167.125 157.917 190.785 1.00 109.07 ? 215 VAL A O   1 
ATOM   1365  C CB  . VAL A  1 213 ? 168.224 154.802 191.630 1.00 98.14  ? 215 VAL A CB  1 
ATOM   1366  C CG1 . VAL A  1 213 ? 168.005 153.518 192.408 1.00 95.47  ? 215 VAL A CG1 1 
ATOM   1367  C CG2 . VAL A  1 213 ? 168.090 154.549 190.141 1.00 99.35  ? 215 VAL A CG2 1 
ATOM   1368  N N   . ASN A  1 214 ? 168.764 157.750 192.312 1.00 97.95  ? 216 ASN A N   1 
ATOM   1369  C CA  . ASN A  1 214 ? 169.397 159.027 191.979 1.00 102.15 ? 216 ASN A CA  1 
ATOM   1370  C C   . ASN A  1 214 ? 168.409 160.186 192.077 1.00 107.82 ? 216 ASN A C   1 
ATOM   1371  O O   . ASN A  1 214 ? 168.352 161.054 191.205 1.00 109.17 ? 216 ASN A O   1 
ATOM   1372  C CB  . ASN A  1 214 ? 170.040 158.974 190.592 1.00 103.06 ? 216 ASN A CB  1 
ATOM   1373  C CG  . ASN A  1 214 ? 171.179 157.981 190.519 1.00 105.74 ? 216 ASN A CG  1 
ATOM   1374  O OD1 . ASN A  1 214 ? 171.776 157.630 191.535 1.00 106.97 ? 216 ASN A OD1 1 
ATOM   1375  N ND2 . ASN A  1 214 ? 171.481 157.514 189.314 1.00 104.62 ? 216 ASN A ND2 1 
ATOM   1376  N N   . VAL A  1 215 ? 167.626 160.200 193.148 1.00 108.20 ? 217 VAL A N   1 
ATOM   1377  C CA  . VAL A  1 215 ? 166.654 161.259 193.389 1.00 108.16 ? 217 VAL A CA  1 
ATOM   1378  C C   . VAL A  1 215 ? 167.289 162.309 194.287 1.00 115.47 ? 217 VAL A C   1 
ATOM   1379  O O   . VAL A  1 215 ? 167.899 161.979 195.310 1.00 117.18 ? 217 VAL A O   1 
ATOM   1380  C CB  . VAL A  1 215 ? 165.372 160.698 194.024 1.00 102.35 ? 217 VAL A CB  1 
ATOM   1381  C CG1 . VAL A  1 215 ? 164.318 161.784 194.134 1.00 103.47 ? 217 VAL A CG1 1 
ATOM   1382  C CG2 . VAL A  1 215 ? 164.852 159.529 193.215 1.00 104.68 ? 217 VAL A CG2 1 
ATOM   1383  N N   . GLY A  1 216 ? 167.154 163.575 193.903 1.00 114.08 ? 218 GLY A N   1 
ATOM   1384  C CA  . GLY A  1 216 ? 167.642 164.647 194.739 1.00 115.06 ? 218 GLY A CA  1 
ATOM   1385  C C   . GLY A  1 216 ? 166.844 164.775 196.021 1.00 121.89 ? 218 GLY A C   1 
ATOM   1386  O O   . GLY A  1 216 ? 165.710 164.310 196.134 1.00 127.29 ? 218 GLY A O   1 
ATOM   1387  N N   . ASP A  1 217 ? 167.462 165.416 197.009 1.00 121.43 ? 219 ASP A N   1 
ATOM   1388  C CA  . ASP A  1 217 ? 166.821 165.572 198.307 1.00 119.91 ? 219 ASP A CA  1 
ATOM   1389  C C   . ASP A  1 217 ? 165.545 166.391 198.180 1.00 122.30 ? 219 ASP A C   1 
ATOM   1390  O O   . ASP A  1 217 ? 165.471 167.342 197.399 1.00 128.49 ? 219 ASP A O   1 
ATOM   1391  C CB  . ASP A  1 217 ? 167.776 166.239 199.295 1.00 121.87 ? 219 ASP A CB  1 
ATOM   1392  C CG  . ASP A  1 217 ? 168.807 165.279 199.845 1.00 125.99 ? 219 ASP A CG  1 
ATOM   1393  O OD1 . ASP A  1 217 ? 169.071 164.253 199.186 1.00 125.00 ? 219 ASP A OD1 1 
ATOM   1394  O OD2 . ASP A  1 217 ? 169.349 165.549 200.937 1.00 124.88 ? 219 ASP A OD2 1 
ATOM   1395  N N   . GLY A  1 218 ? 164.535 166.012 198.957 1.00 117.71 ? 220 GLY A N   1 
ATOM   1396  C CA  . GLY A  1 218 ? 163.267 166.710 198.929 1.00 115.92 ? 220 GLY A CA  1 
ATOM   1397  C C   . GLY A  1 218 ? 163.322 168.066 199.600 1.00 120.29 ? 220 GLY A C   1 
ATOM   1398  O O   . GLY A  1 218 ? 164.401 168.635 199.788 1.00 128.66 ? 220 GLY A O   1 
ATOM   1399  N N   . ALA A  1 219 ? 162.159 168.589 199.970 1.00 110.84 ? 221 ALA A N   1 
ATOM   1400  C CA  . ALA A  1 219 ? 162.017 169.931 200.521 1.00 109.85 ? 221 ALA A CA  1 
ATOM   1401  C C   . ALA A  1 219 ? 161.116 169.909 201.745 1.00 112.20 ? 221 ALA A C   1 
ATOM   1402  O O   . ALA A  1 219 ? 160.145 170.661 201.834 1.00 120.76 ? 221 ALA A O   1 
ATOM   1403  C CB  . ALA A  1 219 ? 161.478 170.899 199.474 1.00 113.21 ? 221 ALA A CB  1 
ATOM   1404  N N   . ILE A  1 220 ? 161.421 169.024 202.698 1.00 110.27 ? 222 ILE A N   1 
ATOM   1405  C CA  . ILE A  1 220 ? 160.551 168.752 203.841 1.00 111.42 ? 222 ILE A CA  1 
ATOM   1406  C C   . ILE A  1 220 ? 160.072 170.055 204.464 1.00 119.01 ? 222 ILE A C   1 
ATOM   1407  O O   . ILE A  1 220 ? 160.876 170.870 204.931 1.00 121.23 ? 222 ILE A O   1 
ATOM   1408  C CB  . ILE A  1 220 ? 161.274 167.891 204.894 1.00 102.02 ? 222 ILE A CB  1 
ATOM   1409  C CG1 . ILE A  1 220 ? 161.941 166.682 204.238 1.00 102.91 ? 222 ILE A CG1 1 
ATOM   1410  C CG2 . ILE A  1 220 ? 160.306 167.452 205.979 1.00 105.21 ? 222 ILE A CG2 1 
ATOM   1411  C CD1 . ILE A  1 220 ? 161.002 165.841 203.414 1.00 108.54 ? 222 ILE A CD1 1 
ATOM   1412  N N   . SER A  1 221 ? 158.758 170.247 204.482 1.00 120.28 ? 223 SER A N   1 
ATOM   1413  C CA  . SER A  1 221 ? 158.137 171.502 204.891 1.00 115.91 ? 223 SER A CA  1 
ATOM   1414  C C   . SER A  1 221 ? 156.634 171.267 204.987 1.00 118.44 ? 223 SER A C   1 
ATOM   1415  O O   . SER A  1 221 ? 156.147 170.150 204.788 1.00 122.13 ? 223 SER A O   1 
ATOM   1416  C CB  . SER A  1 221 ? 158.460 172.634 203.914 1.00 115.59 ? 223 SER A CB  1 
ATOM   1417  O OG  . SER A  1 221 ? 157.457 172.745 202.921 1.00 119.69 ? 223 SER A OG  1 
ATOM   1418  N N   . ALA A  1 222 ? 155.898 172.340 205.280 1.00 120.80 ? 224 ALA A N   1 
ATOM   1419  C CA  . ALA A  1 222 ? 154.464 172.211 205.513 1.00 121.77 ? 224 ALA A CA  1 
ATOM   1420  C C   . ALA A  1 222 ? 153.700 171.954 204.220 1.00 121.46 ? 224 ALA A C   1 
ATOM   1421  O O   . ALA A  1 222 ? 152.715 171.207 204.215 1.00 122.96 ? 224 ALA A O   1 
ATOM   1422  C CB  . ALA A  1 222 ? 153.932 173.464 206.208 1.00 120.93 ? 224 ALA A CB  1 
ATOM   1423  N N   . ASN A  1 223 ? 154.132 172.560 203.116 1.00 120.44 ? 225 ASN A N   1 
ATOM   1424  C CA  . ASN A  1 223 ? 153.362 172.540 201.881 1.00 121.94 ? 225 ASN A CA  1 
ATOM   1425  C C   . ASN A  1 223 ? 154.109 171.959 200.691 1.00 122.94 ? 225 ASN A C   1 
ATOM   1426  O O   . ASN A  1 223 ? 153.534 171.887 199.599 1.00 124.39 ? 225 ASN A O   1 
ATOM   1427  C CB  . ASN A  1 223 ? 152.894 173.959 201.533 1.00 130.56 ? 225 ASN A CB  1 
ATOM   1428  C CG  . ASN A  1 223 ? 154.029 174.843 201.055 1.00 138.87 ? 225 ASN A CG  1 
ATOM   1429  O OD1 . ASN A  1 223 ? 154.725 175.466 201.856 1.00 136.85 ? 225 ASN A OD1 1 
ATOM   1430  N ND2 . ASN A  1 223 ? 154.218 174.906 199.742 1.00 142.60 ? 225 ASN A ND2 1 
ATOM   1431  N N   . SER A  1 224 ? 155.363 171.550 200.857 1.00 120.02 ? 226 SER A N   1 
ATOM   1432  C CA  . SER A  1 224 ? 156.145 171.083 199.723 1.00 121.18 ? 226 SER A CA  1 
ATOM   1433  C C   . SER A  1 224 ? 155.593 169.774 199.178 1.00 123.52 ? 226 SER A C   1 
ATOM   1434  O O   . SER A  1 224 ? 155.210 168.877 199.934 1.00 128.58 ? 226 SER A O   1 
ATOM   1435  C CB  . SER A  1 224 ? 157.606 170.901 200.123 1.00 117.78 ? 226 SER A CB  1 
ATOM   1436  O OG  . SER A  1 224 ? 157.857 169.568 200.530 1.00 115.54 ? 226 SER A OG  1 
ATOM   1437  N N   . SER A  1 225 ? 155.556 169.668 197.853 1.00 117.46 ? 227 SER A N   1 
ATOM   1438  C CA  . SER A  1 225 ? 155.169 168.444 197.159 1.00 115.15 ? 227 SER A CA  1 
ATOM   1439  C C   . SER A  1 225 ? 156.403 167.958 196.408 1.00 115.80 ? 227 SER A C   1 
ATOM   1440  O O   . SER A  1 225 ? 156.595 168.272 195.231 1.00 118.87 ? 227 SER A O   1 
ATOM   1441  C CB  . SER A  1 225 ? 153.999 168.682 196.222 1.00 120.12 ? 227 SER A CB  1 
ATOM   1442  O OG  . SER A  1 225 ? 154.414 169.403 195.076 1.00 132.00 ? 227 SER A OG  1 
ATOM   1443  N N   . ASP A  1 226 ? 157.237 167.186 197.098 1.00 113.52 ? 228 ASP A N   1 
ATOM   1444  C CA  . ASP A  1 226 ? 158.464 166.659 196.520 1.00 109.95 ? 228 ASP A CA  1 
ATOM   1445  C C   . ASP A  1 226 ? 158.519 165.153 196.722 1.00 111.04 ? 228 ASP A C   1 
ATOM   1446  O O   . ASP A  1 226 ? 157.514 164.537 197.085 1.00 117.19 ? 228 ASP A O   1 
ATOM   1447  C CB  . ASP A  1 226 ? 159.685 167.335 197.144 1.00 113.00 ? 228 ASP A CB  1 
ATOM   1448  C CG  . ASP A  1 226 ? 160.252 168.429 196.267 1.00 120.18 ? 228 ASP A CG  1 
ATOM   1449  O OD1 . ASP A  1 226 ? 160.490 168.163 195.072 1.00 128.98 ? 228 ASP A OD1 1 
ATOM   1450  O OD2 . ASP A  1 226 ? 160.455 169.554 196.766 1.00 114.91 ? 228 ASP A OD2 1 
ATOM   1451  N N   . ALA A  1 227 ? 159.674 164.547 196.474 1.00 105.79 ? 229 ALA A N   1 
ATOM   1452  C CA  . ALA A  1 227 ? 159.877 163.123 196.716 1.00 96.27  ? 229 ALA A CA  1 
ATOM   1453  C C   . ALA A  1 227 ? 161.028 162.974 197.700 1.00 102.44 ? 229 ALA A C   1 
ATOM   1454  O O   . ALA A  1 227 ? 162.187 163.210 197.344 1.00 114.34 ? 229 ALA A O   1 
ATOM   1455  C CB  . ALA A  1 227 ? 160.161 162.377 195.414 1.00 93.01  ? 229 ALA A CB  1 
ATOM   1456  N N   . VAL A  1 228 ? 160.711 162.587 198.937 1.00 96.22  ? 230 VAL A N   1 
ATOM   1457  C CA  . VAL A  1 228 ? 161.762 162.398 199.924 1.00 100.18 ? 230 VAL A CA  1 
ATOM   1458  C C   . VAL A  1 228 ? 162.578 161.159 199.572 1.00 103.40 ? 230 VAL A C   1 
ATOM   1459  O O   . VAL A  1 228 ? 162.109 160.233 198.898 1.00 105.38 ? 230 VAL A O   1 
ATOM   1460  C CB  . VAL A  1 228 ? 161.180 162.305 201.345 1.00 93.67  ? 230 VAL A CB  1 
ATOM   1461  C CG1 . VAL A  1 228 ? 159.858 163.047 201.422 1.00 95.61  ? 230 VAL A CG1 1 
ATOM   1462  C CG2 . VAL A  1 228 ? 161.012 160.863 201.774 1.00 91.09  ? 230 VAL A CG2 1 
ATOM   1463  N N   . THR A  1 229 ? 163.827 161.151 200.019 1.00 105.20 ? 231 THR A N   1 
ATOM   1464  C CA  . THR A  1 229 ? 164.769 160.105 199.660 1.00 101.02 ? 231 THR A CA  1 
ATOM   1465  C C   . THR A  1 229 ? 165.051 159.213 200.863 1.00 99.37  ? 231 THR A C   1 
ATOM   1466  O O   . THR A  1 229 ? 164.518 159.411 201.958 1.00 100.19 ? 231 THR A O   1 
ATOM   1467  C CB  . THR A  1 229 ? 166.063 160.709 199.113 1.00 103.72 ? 231 THR A CB  1 
ATOM   1468  O OG1 . THR A  1 229 ? 166.540 161.714 200.013 1.00 110.44 ? 231 THR A OG1 1 
ATOM   1469  C CG2 . THR A  1 229 ? 165.817 161.338 197.754 1.00 105.62 ? 231 THR A CG2 1 
ATOM   1470  N N   . GLY A  1 230 ? 165.900 158.210 200.640 1.00 95.80  ? 232 GLY A N   1 
ATOM   1471  C CA  . GLY A  1 230 ? 166.244 157.294 201.713 1.00 96.59  ? 232 GLY A CA  1 
ATOM   1472  C C   . GLY A  1 230 ? 166.979 157.976 202.850 1.00 99.18  ? 232 GLY A C   1 
ATOM   1473  O O   . GLY A  1 230 ? 166.705 157.716 204.022 1.00 101.04 ? 232 GLY A O   1 
ATOM   1474  N N   . ARG A  1 231 ? 167.923 158.859 202.519 1.00 98.06  ? 233 ARG A N   1 
ATOM   1475  C CA  . ARG A  1 231 ? 168.670 159.563 203.556 1.00 99.19  ? 233 ARG A CA  1 
ATOM   1476  C C   . ARG A  1 231 ? 167.774 160.516 204.336 1.00 102.42 ? 233 ARG A C   1 
ATOM   1477  O O   . ARG A  1 231 ? 167.945 160.684 205.549 1.00 102.76 ? 233 ARG A O   1 
ATOM   1478  C CB  . ARG A  1 231 ? 169.842 160.320 202.934 1.00 99.81  ? 233 ARG A CB  1 
ATOM   1479  C CG  . ARG A  1 231 ? 169.478 161.095 201.683 1.00 101.76 ? 233 ARG A CG  1 
ATOM   1480  C CD  . ARG A  1 231 ? 170.064 162.495 201.716 1.00 108.99 ? 233 ARG A CD  1 
ATOM   1481  N NE  . ARG A  1 231 ? 171.521 162.484 201.728 1.00 112.93 ? 233 ARG A NE  1 
ATOM   1482  C CZ  . ARG A  1 231 ? 172.278 162.267 200.661 1.00 117.42 ? 233 ARG A CZ  1 
ATOM   1483  N NH1 . ARG A  1 231 ? 171.747 162.041 199.471 1.00 115.29 ? 233 ARG A NH1 1 
ATOM   1484  N NH2 . ARG A  1 231 ? 173.601 162.279 200.791 1.00 118.06 ? 233 ARG A NH2 1 
ATOM   1485  N N   . GLN A  1 232 ? 166.820 161.155 203.656 1.00 103.13 ? 234 GLN A N   1 
ATOM   1486  C CA  . GLN A  1 232 ? 165.921 162.088 204.328 1.00 98.27  ? 234 GLN A CA  1 
ATOM   1487  C C   . GLN A  1 232 ? 165.074 161.378 205.375 1.00 100.45 ? 234 GLN A C   1 
ATOM   1488  O O   . GLN A  1 232 ? 164.929 161.856 206.505 1.00 101.65 ? 234 GLN A O   1 
ATOM   1489  C CB  . GLN A  1 232 ? 165.032 162.780 203.299 1.00 92.72  ? 234 GLN A CB  1 
ATOM   1490  C CG  . GLN A  1 232 ? 165.781 163.690 202.353 1.00 100.52 ? 234 GLN A CG  1 
ATOM   1491  C CD  . GLN A  1 232 ? 164.980 164.912 201.980 1.00 108.86 ? 234 GLN A CD  1 
ATOM   1492  O OE1 . GLN A  1 232 ? 163.956 164.810 201.308 1.00 112.00 ? 234 GLN A OE1 1 
ATOM   1493  N NE2 . GLN A  1 232 ? 165.439 166.079 202.413 1.00 114.84 ? 234 GLN A NE2 1 
ATOM   1494  N N   . LEU A  1 233 ? 164.502 160.229 205.012 1.00 101.90 ? 235 LEU A N   1 
ATOM   1495  C CA  . LEU A  1 233 ? 163.712 159.462 205.967 1.00 102.03 ? 235 LEU A CA  1 
ATOM   1496  C C   . LEU A  1 233 ? 164.601 158.805 207.015 1.00 101.62 ? 235 LEU A C   1 
ATOM   1497  O O   . LEU A  1 233 ? 164.161 158.580 208.148 1.00 103.01 ? 235 LEU A O   1 
ATOM   1498  C CB  . LEU A  1 233 ? 162.868 158.429 205.215 1.00 101.18 ? 235 LEU A CB  1 
ATOM   1499  C CG  . LEU A  1 233 ? 161.897 157.475 205.921 1.00 99.57  ? 235 LEU A CG  1 
ATOM   1500  C CD1 . LEU A  1 233 ? 162.596 156.237 206.455 1.00 101.38 ? 235 LEU A CD1 1 
ATOM   1501  C CD2 . LEU A  1 233 ? 161.148 158.190 207.034 1.00 101.32 ? 235 LEU A CD2 1 
ATOM   1502  N N   . TYR A  1 234 ? 165.849 158.497 206.659 1.00 99.67  ? 236 TYR A N   1 
ATOM   1503  C CA  . TYR A  1 234 ? 166.776 157.901 207.614 1.00 99.88  ? 236 TYR A CA  1 
ATOM   1504  C C   . TYR A  1 234 ? 167.123 158.881 208.726 1.00 103.33 ? 236 TYR A C   1 
ATOM   1505  O O   . TYR A  1 234 ? 167.032 158.551 209.914 1.00 102.70 ? 236 TYR A O   1 
ATOM   1506  C CB  . TYR A  1 234 ? 168.043 157.454 206.887 1.00 97.97  ? 236 TYR A CB  1 
ATOM   1507  C CG  . TYR A  1 234 ? 169.091 156.839 207.782 1.00 101.57 ? 236 TYR A CG  1 
ATOM   1508  C CD1 . TYR A  1 234 ? 168.800 155.737 208.571 1.00 103.12 ? 236 TYR A CD1 1 
ATOM   1509  C CD2 . TYR A  1 234 ? 170.366 157.379 207.858 1.00 98.27  ? 236 TYR A CD2 1 
ATOM   1510  C CE1 . TYR A  1 234 ? 169.758 155.175 209.389 1.00 101.28 ? 236 TYR A CE1 1 
ATOM   1511  C CE2 . TYR A  1 234 ? 171.328 156.828 208.676 1.00 96.26  ? 236 TYR A CE2 1 
ATOM   1512  C CZ  . TYR A  1 234 ? 171.019 155.727 209.441 1.00 100.79 ? 236 TYR A CZ  1 
ATOM   1513  O OH  . TYR A  1 234 ? 171.976 155.174 210.259 1.00 105.73 ? 236 TYR A OH  1 
ATOM   1514  N N   . SER A  1 235 ? 167.526 160.096 208.358 1.00 103.80 ? 237 SER A N   1 
ATOM   1515  C CA  . SER A  1 235 ? 167.920 161.101 209.335 1.00 100.70 ? 237 SER A CA  1 
ATOM   1516  C C   . SER A  1 235 ? 166.725 161.854 209.902 1.00 104.58 ? 237 SER A C   1 
ATOM   1517  O O   . SER A  1 235 ? 166.709 162.182 211.093 1.00 105.82 ? 237 SER A O   1 
ATOM   1518  C CB  . SER A  1 235 ? 168.906 162.087 208.706 1.00 105.50 ? 237 SER A CB  1 
ATOM   1519  O OG  . SER A  1 235 ? 168.410 162.592 207.480 1.00 109.90 ? 237 SER A OG  1 
ATOM   1520  N N   . GLY A  1 236 ? 165.722 162.134 209.074 1.00 108.11 ? 238 GLY A N   1 
ATOM   1521  C CA  . GLY A  1 236 ? 164.545 162.834 209.547 1.00 109.49 ? 238 GLY A CA  1 
ATOM   1522  C C   . GLY A  1 236 ? 164.742 164.314 209.773 1.00 107.64 ? 238 GLY A C   1 
ATOM   1523  O O   . GLY A  1 236 ? 164.026 164.910 210.582 1.00 108.10 ? 238 GLY A O   1 
ATOM   1524  N N   . ASN A  1 237 ? 165.715 164.922 209.101 1.00 110.93 ? 239 ASN A N   1 
ATOM   1525  C CA  . ASN A  1 237 ? 165.955 166.348 209.270 1.00 112.17 ? 239 ASN A CA  1 
ATOM   1526  C C   . ASN A  1 237 ? 164.790 167.156 208.715 1.00 116.44 ? 239 ASN A C   1 
ATOM   1527  O O   . ASN A  1 237 ? 164.261 166.859 207.641 1.00 117.83 ? 239 ASN A O   1 
ATOM   1528  C CB  . ASN A  1 237 ? 167.252 166.757 208.576 1.00 111.09 ? 239 ASN A CB  1 
ATOM   1529  C CG  . ASN A  1 237 ? 168.445 165.955 209.050 1.00 112.18 ? 239 ASN A CG  1 
ATOM   1530  O OD1 . ASN A  1 237 ? 168.520 165.562 210.214 1.00 116.56 ? 239 ASN A OD1 1 
ATOM   1531  N ND2 . ASN A  1 237 ? 169.388 165.710 208.150 1.00 111.29 ? 239 ASN A ND2 1 
ATOM   1532  N N   . GLY A  1 238 ? 164.391 168.185 209.457 1.00 114.22 ? 240 GLY A N   1 
ATOM   1533  C CA  . GLY A  1 238 ? 163.345 169.084 209.022 1.00 116.14 ? 240 GLY A CA  1 
ATOM   1534  C C   . GLY A  1 238 ? 161.930 168.638 209.316 1.00 114.07 ? 240 GLY A C   1 
ATOM   1535  O O   . GLY A  1 238 ? 160.988 169.320 208.894 1.00 116.33 ? 240 GLY A O   1 
ATOM   1536  N N   . ILE A  1 239 ? 161.744 167.521 210.022 1.00 112.01 ? 241 ILE A N   1 
ATOM   1537  C CA  . ILE A  1 239 ? 160.394 167.093 210.370 1.00 106.65 ? 241 ILE A CA  1 
ATOM   1538  C C   . ILE A  1 239 ? 159.788 168.058 211.383 1.00 106.63 ? 241 ILE A C   1 
ATOM   1539  O O   . ILE A  1 239 ? 160.483 168.818 212.066 1.00 107.85 ? 241 ILE A O   1 
ATOM   1540  C CB  . ILE A  1 239 ? 160.390 165.656 210.914 1.00 99.72  ? 241 ILE A CB  1 
ATOM   1541  C CG1 . ILE A  1 239 ? 161.176 165.586 212.224 1.00 101.75 ? 241 ILE A CG1 1 
ATOM   1542  C CG2 . ILE A  1 239 ? 160.952 164.695 209.887 1.00 96.79  ? 241 ILE A CG2 1 
ATOM   1543  C CD1 . ILE A  1 239 ? 161.428 164.182 212.712 1.00 97.61  ? 241 ILE A CD1 1 
ATOM   1544  N N   . ASP A  1 240 ? 158.464 168.020 211.480 1.00 103.87 ? 242 ASP A N   1 
ATOM   1545  C CA  . ASP A  1 240 ? 157.752 168.814 212.476 1.00 107.90 ? 242 ASP A CA  1 
ATOM   1546  C C   . ASP A  1 240 ? 157.969 168.169 213.835 1.00 108.21 ? 242 ASP A C   1 
ATOM   1547  O O   . ASP A  1 240 ? 157.269 167.227 214.211 1.00 113.11 ? 242 ASP A O   1 
ATOM   1548  C CB  . ASP A  1 240 ? 156.270 168.902 212.131 1.00 112.50 ? 242 ASP A CB  1 
ATOM   1549  C CG  . ASP A  1 240 ? 155.559 170.006 212.888 1.00 118.16 ? 242 ASP A CG  1 
ATOM   1550  O OD1 . ASP A  1 240 ? 155.691 170.067 214.128 1.00 114.99 ? 242 ASP A OD1 1 
ATOM   1551  O OD2 . ASP A  1 240 ? 154.865 170.818 212.240 1.00 123.77 ? 242 ASP A OD2 1 
ATOM   1552  N N   . THR A  1 241 ? 158.950 168.678 214.582 1.00 105.53 ? 243 THR A N   1 
ATOM   1553  C CA  . THR A  1 241 ? 159.281 168.105 215.880 1.00 107.48 ? 243 THR A CA  1 
ATOM   1554  C C   . THR A  1 241 ? 158.159 168.253 216.896 1.00 110.26 ? 243 THR A C   1 
ATOM   1555  O O   . THR A  1 241 ? 158.190 167.570 217.922 1.00 110.06 ? 243 THR A O   1 
ATOM   1556  C CB  . THR A  1 241 ? 160.554 168.746 216.433 1.00 107.37 ? 243 THR A CB  1 
ATOM   1557  O OG1 . THR A  1 241 ? 160.258 170.063 216.913 1.00 114.69 ? 243 THR A OG1 1 
ATOM   1558  C CG2 . THR A  1 241 ? 161.620 168.832 215.352 1.00 106.84 ? 243 THR A CG2 1 
ATOM   1559  N N   . ALA A  1 242 ? 157.181 169.120 216.647 1.00 111.31 ? 244 ALA A N   1 
ATOM   1560  C CA  . ALA A  1 242 ? 156.045 169.283 217.545 1.00 110.47 ? 244 ALA A CA  1 
ATOM   1561  C C   . ALA A  1 242 ? 154.849 168.431 217.148 1.00 112.29 ? 244 ALA A C   1 
ATOM   1562  O O   . ALA A  1 242 ? 154.190 167.855 218.019 1.00 111.64 ? 244 ALA A O   1 
ATOM   1563  C CB  . ALA A  1 242 ? 155.624 170.753 217.607 1.00 109.11 ? 244 ALA A CB  1 
ATOM   1564  N N   . ALA A  1 243 ? 154.547 168.342 215.850 1.00 114.45 ? 245 ALA A N   1 
ATOM   1565  C CA  . ALA A  1 243 ? 153.448 167.491 215.405 1.00 115.13 ? 245 ALA A CA  1 
ATOM   1566  C C   . ALA A  1 243 ? 153.751 166.019 215.655 1.00 114.44 ? 245 ALA A C   1 
ATOM   1567  O O   . ALA A  1 243 ? 152.881 165.270 216.116 1.00 113.20 ? 245 ALA A O   1 
ATOM   1568  C CB  . ALA A  1 243 ? 153.159 167.735 213.925 1.00 113.25 ? 245 ALA A CB  1 
ATOM   1569  N N   . TRP A  1 244 ? 154.977 165.586 215.352 1.00 110.79 ? 246 TRP A N   1 
ATOM   1570  C CA  . TRP A  1 244 ? 155.358 164.197 215.577 1.00 100.16 ? 246 TRP A CA  1 
ATOM   1571  C C   . TRP A  1 244 ? 155.329 163.827 217.052 1.00 100.29 ? 246 TRP A C   1 
ATOM   1572  O O   . TRP A  1 244 ? 155.082 162.663 217.385 1.00 104.14 ? 246 TRP A O   1 
ATOM   1573  C CB  . TRP A  1 244 ? 156.750 163.939 215.004 1.00 90.21  ? 246 TRP A CB  1 
ATOM   1574  C CG  . TRP A  1 244 ? 156.753 163.661 213.538 1.00 87.01  ? 246 TRP A CG  1 
ATOM   1575  C CD1 . TRP A  1 244 ? 156.535 164.558 212.536 1.00 95.09  ? 246 TRP A CD1 1 
ATOM   1576  C CD2 . TRP A  1 244 ? 157.000 162.403 212.903 1.00 85.61  ? 246 TRP A CD2 1 
ATOM   1577  N NE1 . TRP A  1 244 ? 156.623 163.936 211.316 1.00 90.83  ? 246 TRP A NE1 1 
ATOM   1578  C CE2 . TRP A  1 244 ? 156.909 162.611 211.514 1.00 88.65  ? 246 TRP A CE2 1 
ATOM   1579  C CE3 . TRP A  1 244 ? 157.288 161.119 213.374 1.00 83.60  ? 246 TRP A CE3 1 
ATOM   1580  C CZ2 . TRP A  1 244 ? 157.096 161.585 210.592 1.00 82.91  ? 246 TRP A CZ2 1 
ATOM   1581  C CZ3 . TRP A  1 244 ? 157.473 160.103 212.457 1.00 85.95  ? 246 TRP A CZ3 1 
ATOM   1582  C CH2 . TRP A  1 244 ? 157.375 160.341 211.083 1.00 85.39  ? 246 TRP A CH2 1 
ATOM   1583  N N   . GLN A  1 245 ? 155.572 164.786 217.939 1.00 99.88  ? 247 GLN A N   1 
ATOM   1584  C CA  . GLN A  1 245 ? 155.547 164.551 219.374 1.00 102.52 ? 247 GLN A CA  1 
ATOM   1585  C C   . GLN A  1 245 ? 154.135 164.470 219.934 1.00 108.32 ? 247 GLN A C   1 
ATOM   1586  O O   . GLN A  1 245 ? 153.971 164.174 221.122 1.00 109.95 ? 247 GLN A O   1 
ATOM   1587  C CB  . GLN A  1 245 ? 156.334 165.647 220.095 1.00 102.04 ? 247 GLN A CB  1 
ATOM   1588  C CG  . GLN A  1 245 ? 157.834 165.435 220.055 1.00 106.74 ? 247 GLN A CG  1 
ATOM   1589  C CD  . GLN A  1 245 ? 158.588 166.480 220.843 1.00 112.15 ? 247 GLN A CD  1 
ATOM   1590  O OE1 . GLN A  1 245 ? 158.021 167.491 221.250 1.00 116.68 ? 247 GLN A OE1 1 
ATOM   1591  N NE2 . GLN A  1 245 ? 159.874 166.241 221.064 1.00 111.72 ? 247 GLN A NE2 1 
ATOM   1592  N N   . ASN A  1 246 ? 153.120 164.737 219.119 1.00 110.47 ? 248 ASN A N   1 
ATOM   1593  C CA  . ASN A  1 246 ? 151.729 164.525 219.498 1.00 111.75 ? 248 ASN A CA  1 
ATOM   1594  C C   . ASN A  1 246 ? 151.146 163.256 218.903 1.00 114.19 ? 248 ASN A C   1 
ATOM   1595  O O   . ASN A  1 246 ? 150.371 162.567 219.569 1.00 117.24 ? 248 ASN A O   1 
ATOM   1596  C CB  . ASN A  1 246 ? 150.875 165.723 219.073 1.00 114.90 ? 248 ASN A CB  1 
ATOM   1597  C CG  . ASN A  1 246 ? 150.750 166.763 220.167 1.00 123.86 ? 248 ASN A CG  1 
ATOM   1598  O OD1 . ASN A  1 246 ? 151.342 166.627 221.237 1.00 125.86 ? 248 ASN A OD1 1 
ATOM   1599  N ND2 . ASN A  1 246 ? 149.980 167.811 219.902 1.00 132.33 ? 248 ASN A ND2 1 
ATOM   1600  N N   . LYS A  1 247 ? 151.500 162.936 217.656 1.00 111.61 ? 249 LYS A N   1 
ATOM   1601  C CA  . LYS A  1 247 ? 151.104 161.657 217.077 1.00 110.97 ? 249 LYS A CA  1 
ATOM   1602  C C   . LYS A  1 247 ? 151.714 160.500 217.853 1.00 106.15 ? 249 LYS A C   1 
ATOM   1603  O O   . LYS A  1 247 ? 151.030 159.519 218.166 1.00 108.99 ? 249 LYS A O   1 
ATOM   1604  C CB  . LYS A  1 247 ? 151.524 161.605 215.611 1.00 104.54 ? 249 LYS A CB  1 
ATOM   1605  C CG  . LYS A  1 247 ? 150.747 160.623 214.769 1.00 107.24 ? 249 LYS A CG  1 
ATOM   1606  C CD  . LYS A  1 247 ? 150.868 161.003 213.311 1.00 119.24 ? 249 LYS A CD  1 
ATOM   1607  C CE  . LYS A  1 247 ? 150.448 162.450 213.103 1.00 124.60 ? 249 LYS A CE  1 
ATOM   1608  N NZ  . LYS A  1 247 ? 151.352 163.179 212.174 1.00 113.03 ? 249 LYS A NZ  1 
ATOM   1609  N N   . LEU A  1 248 ? 152.999 160.599 218.171 1.00 99.00  ? 250 LEU A N   1 
ATOM   1610  C CA  . LEU A  1 248 ? 153.657 159.694 219.100 1.00 96.68  ? 250 LEU A CA  1 
ATOM   1611  C C   . LEU A  1 248 ? 153.704 160.391 220.451 1.00 100.90 ? 250 LEU A C   1 
ATOM   1612  O O   . LEU A  1 248 ? 154.318 161.454 220.581 1.00 107.78 ? 250 LEU A O   1 
ATOM   1613  C CB  . LEU A  1 248 ? 155.070 159.338 218.636 1.00 92.51  ? 250 LEU A CB  1 
ATOM   1614  C CG  . LEU A  1 248 ? 155.316 158.420 217.434 1.00 91.65  ? 250 LEU A CG  1 
ATOM   1615  C CD1 . LEU A  1 248 ? 154.765 158.989 216.138 1.00 94.50  ? 250 LEU A CD1 1 
ATOM   1616  C CD2 . LEU A  1 248 ? 156.804 158.141 217.299 1.00 85.09  ? 250 LEU A CD2 1 
ATOM   1617  N N   . ASN A  1 249 ? 153.054 159.803 221.452 1.00 97.79  ? 251 ASN A N   1 
ATOM   1618  C CA  . ASN A  1 249 ? 153.001 160.417 222.777 1.00 103.07 ? 251 ASN A CA  1 
ATOM   1619  C C   . ASN A  1 249 ? 154.371 160.256 223.424 1.00 109.64 ? 251 ASN A C   1 
ATOM   1620  O O   . ASN A  1 249 ? 154.617 159.357 224.229 1.00 116.73 ? 251 ASN A O   1 
ATOM   1621  C CB  . ASN A  1 249 ? 151.906 159.787 223.627 1.00 101.86 ? 251 ASN A CB  1 
ATOM   1622  C CG  . ASN A  1 249 ? 150.622 159.575 222.858 1.00 115.30 ? 251 ASN A CG  1 
ATOM   1623  O OD1 . ASN A  1 249 ? 150.506 159.974 221.700 1.00 120.00 ? 251 ASN A OD1 1 
ATOM   1624  N ND2 . ASN A  1 249 ? 149.647 158.940 223.498 1.00 111.85 ? 251 ASN A ND2 1 
ATOM   1625  N N   . VAL A  1 250 ? 155.286 161.139 223.056 1.00 106.40 ? 252 VAL A N   1 
ATOM   1626  C CA  . VAL A  1 250 ? 156.628 161.095 223.611 1.00 96.83  ? 252 VAL A CA  1 
ATOM   1627  C C   . VAL A  1 250 ? 156.644 161.867 224.922 1.00 100.18 ? 252 VAL A C   1 
ATOM   1628  O O   . VAL A  1 250 ? 155.782 162.705 225.197 1.00 108.11 ? 252 VAL A O   1 
ATOM   1629  C CB  . VAL A  1 250 ? 157.684 161.648 222.635 1.00 87.33  ? 252 VAL A CB  1 
ATOM   1630  C CG1 . VAL A  1 250 ? 157.423 161.155 221.223 1.00 88.88  ? 252 VAL A CG1 1 
ATOM   1631  C CG2 . VAL A  1 250 ? 157.714 163.158 222.693 1.00 100.90 ? 252 VAL A CG2 1 
ATOM   1632  N N   . THR A  1 251 ? 157.639 161.572 225.744 1.00 99.70  ? 253 THR A N   1 
ATOM   1633  C CA  . THR A  1 251 ? 157.892 162.293 226.986 1.00 110.35 ? 253 THR A CA  1 
ATOM   1634  C C   . THR A  1 251 ? 159.229 163.002 226.824 1.00 127.10 ? 253 THR A C   1 
ATOM   1635  O O   . THR A  1 251 ? 160.287 162.372 226.900 1.00 136.31 ? 253 THR A O   1 
ATOM   1636  C CB  . THR A  1 251 ? 157.905 161.351 228.183 1.00 110.66 ? 253 THR A CB  1 
ATOM   1637  O OG1 . THR A  1 251 ? 156.662 160.641 228.251 1.00 111.29 ? 253 THR A OG1 1 
ATOM   1638  C CG2 . THR A  1 251 ? 158.126 162.131 229.462 1.00 116.13 ? 253 THR A CG2 1 
ATOM   1639  N N   . ARG A  1 252 ? 159.176 164.310 226.590 1.00 126.27 ? 254 ARG A N   1 
ATOM   1640  C CA  . ARG A  1 252 ? 160.397 165.067 226.363 1.00 127.86 ? 254 ARG A CA  1 
ATOM   1641  C C   . ARG A  1 252 ? 161.303 164.992 227.583 1.00 136.65 ? 254 ARG A C   1 
ATOM   1642  O O   . ARG A  1 252 ? 160.842 165.040 228.727 1.00 137.02 ? 254 ARG A O   1 
ATOM   1643  C CB  . ARG A  1 252 ? 160.067 166.519 226.024 1.00 134.62 ? 254 ARG A CB  1 
ATOM   1644  C CG  . ARG A  1 252 ? 159.152 167.202 227.018 1.00 141.49 ? 254 ARG A CG  1 
ATOM   1645  C CD  . ARG A  1 252 ? 158.548 168.509 226.492 1.00 139.89 ? 254 ARG A CD  1 
ATOM   1646  N NE  . ARG A  1 252 ? 157.560 168.315 225.435 1.00 134.46 ? 254 ARG A NE  1 
ATOM   1647  C CZ  . ARG A  1 252 ? 157.834 168.176 224.144 1.00 132.07 ? 254 ARG A CZ  1 
ATOM   1648  N NH1 . ARG A  1 252 ? 159.068 168.281 223.681 1.00 129.39 ? 254 ARG A NH1 1 
ATOM   1649  N NH2 . ARG A  1 252 ? 156.839 167.948 223.292 1.00 131.54 ? 254 ARG A NH2 1 
ATOM   1650  N N   . LYS A  1 253 ? 162.605 164.855 227.327 1.00 135.85 ? 255 LYS A N   1 
ATOM   1651  C CA  . LYS A  1 253 ? 163.573 164.714 228.407 1.00 139.60 ? 255 LYS A CA  1 
ATOM   1652  C C   . LYS A  1 253 ? 163.579 165.922 229.331 1.00 145.29 ? 255 LYS A C   1 
ATOM   1653  O O   . LYS A  1 253 ? 163.926 165.785 230.509 1.00 145.44 ? 255 LYS A O   1 
ATOM   1654  C CB  . LYS A  1 253 ? 164.967 164.486 227.823 1.00 131.11 ? 255 LYS A CB  1 
ATOM   1655  C CG  . LYS A  1 253 ? 165.431 163.041 227.874 1.00 131.33 ? 255 LYS A CG  1 
ATOM   1656  C CD  . LYS A  1 253 ? 166.652 162.825 226.995 1.00 129.67 ? 255 LYS A CD  1 
ATOM   1657  C CE  . LYS A  1 253 ? 167.571 161.762 227.569 1.00 130.92 ? 255 LYS A CE  1 
ATOM   1658  N NZ  . LYS A  1 253 ? 166.853 160.845 228.496 1.00 128.74 ? 255 LYS A NZ  1 
ATOM   1659  N N   . ASN A  1 254 ? 163.206 167.098 228.823 1.00 147.39 ? 256 ASN A N   1 
ATOM   1660  C CA  . ASN A  1 254 ? 163.112 168.278 229.675 1.00 146.04 ? 256 ASN A CA  1 
ATOM   1661  C C   . ASN A  1 254 ? 162.049 168.109 230.751 1.00 152.36 ? 256 ASN A C   1 
ATOM   1662  O O   . ASN A  1 254 ? 162.310 168.387 231.927 1.00 155.17 ? 256 ASN A O   1 
ATOM   1663  C CB  . ASN A  1 254 ? 162.813 169.511 228.825 1.00 143.16 ? 256 ASN A CB  1 
ATOM   1664  C CG  . ASN A  1 254 ? 163.372 169.399 227.421 1.00 144.80 ? 256 ASN A CG  1 
ATOM   1665  O OD1 . ASN A  1 254 ? 163.555 168.300 226.899 1.00 141.75 ? 256 ASN A OD1 1 
ATOM   1666  N ND2 . ASN A  1 254 ? 163.646 170.540 226.801 1.00 149.78 ? 256 ASN A ND2 1 
ATOM   1667  N N   . ASP A  1 255 ? 160.853 167.656 230.374 1.00 154.71 ? 257 ASP A N   1 
ATOM   1668  C CA  . ASP A  1 255 ? 159.795 167.388 231.341 1.00 158.66 ? 257 ASP A CA  1 
ATOM   1669  C C   . ASP A  1 255 ? 160.115 166.188 232.221 1.00 156.16 ? 257 ASP A C   1 
ATOM   1670  O O   . ASP A  1 255 ? 159.800 166.196 233.416 1.00 160.70 ? 257 ASP A O   1 
ATOM   1671  C CB  . ASP A  1 255 ? 158.464 167.161 230.622 1.00 159.72 ? 257 ASP A CB  1 
ATOM   1672  C CG  . ASP A  1 255 ? 157.956 168.408 229.930 1.00 166.00 ? 257 ASP A CG  1 
ATOM   1673  O OD1 . ASP A  1 255 ? 158.637 169.452 230.008 1.00 168.41 ? 257 ASP A OD1 1 
ATOM   1674  O OD2 . ASP A  1 255 ? 156.875 168.345 229.308 1.00 168.23 ? 257 ASP A OD2 1 
ATOM   1675  N N   . TYR A  1 256 ? 160.727 165.151 231.645 1.00 147.97 ? 258 TYR A N   1 
ATOM   1676  C CA  . TYR A  1 256 ? 161.107 163.983 232.431 1.00 147.84 ? 258 TYR A CA  1 
ATOM   1677  C C   . TYR A  1 256 ? 162.092 164.374 233.524 1.00 149.73 ? 258 TYR A C   1 
ATOM   1678  O O   . TYR A  1 256 ? 161.957 163.949 234.678 1.00 145.79 ? 258 TYR A O   1 
ATOM   1679  C CB  . TYR A  1 256 ? 161.716 162.925 231.510 1.00 144.35 ? 258 TYR A CB  1 
ATOM   1680  C CG  . TYR A  1 256 ? 162.387 161.758 232.204 1.00 147.78 ? 258 TYR A CG  1 
ATOM   1681  C CD1 . TYR A  1 256 ? 161.861 161.213 233.370 1.00 146.76 ? 258 TYR A CD1 1 
ATOM   1682  C CD2 . TYR A  1 256 ? 163.562 161.216 231.703 1.00 146.63 ? 258 TYR A CD2 1 
ATOM   1683  C CE1 . TYR A  1 256 ? 162.474 160.150 234.000 1.00 147.29 ? 258 TYR A CE1 1 
ATOM   1684  C CE2 . TYR A  1 256 ? 164.181 160.153 232.327 1.00 146.99 ? 258 TYR A CE2 1 
ATOM   1685  C CZ  . TYR A  1 256 ? 163.634 159.624 233.474 1.00 147.65 ? 258 TYR A CZ  1 
ATOM   1686  O OH  . TYR A  1 256 ? 164.252 158.567 234.099 1.00 147.70 ? 258 TYR A OH  1 
ATOM   1687  N N   . LYS A  1 257 ? 163.079 165.200 233.181 1.00 150.26 ? 259 LYS A N   1 
ATOM   1688  C CA  . LYS A  1 257 ? 164.079 165.658 234.134 1.00 150.87 ? 259 LYS A CA  1 
ATOM   1689  C C   . LYS A  1 257 ? 163.549 166.723 235.084 1.00 158.13 ? 259 LYS A C   1 
ATOM   1690  O O   . LYS A  1 257 ? 164.231 167.052 236.060 1.00 159.05 ? 259 LYS A O   1 
ATOM   1691  C CB  . LYS A  1 257 ? 165.296 166.202 233.380 1.00 146.19 ? 259 LYS A CB  1 
ATOM   1692  C CG  . LYS A  1 257 ? 166.593 166.208 234.171 1.00 139.66 ? 259 LYS A CG  1 
ATOM   1693  C CD  . LYS A  1 257 ? 167.676 167.031 233.476 1.00 138.42 ? 259 LYS A CD  1 
ATOM   1694  C CE  . LYS A  1 257 ? 168.010 166.502 232.086 1.00 136.93 ? 259 LYS A CE  1 
ATOM   1695  N NZ  . LYS A  1 257 ? 167.174 167.102 231.006 1.00 139.09 ? 259 LYS A NZ  1 
ATOM   1696  N N   . ASP A  1 258 ? 162.353 167.266 234.833 1.00 161.86 ? 260 ASP A N   1 
ATOM   1697  C CA  . ASP A  1 258 ? 161.819 168.348 235.653 1.00 165.23 ? 260 ASP A CA  1 
ATOM   1698  C C   . ASP A  1 258 ? 160.410 168.050 236.158 1.00 165.43 ? 260 ASP A C   1 
ATOM   1699  O O   . ASP A  1 258 ? 159.760 168.938 236.719 1.00 168.23 ? 260 ASP A O   1 
ATOM   1700  C CB  . ASP A  1 258 ? 161.844 169.669 234.883 1.00 166.99 ? 260 ASP A CB  1 
ATOM   1701  C CG  . ASP A  1 258 ? 163.183 170.373 234.987 1.00 166.90 ? 260 ASP A CG  1 
ATOM   1702  O OD1 . ASP A  1 258 ? 163.960 170.038 235.907 1.00 166.56 ? 260 ASP A OD1 1 
ATOM   1703  O OD2 . ASP A  1 258 ? 163.462 171.256 234.150 1.00 165.12 ? 260 ASP A OD2 1 
ATOM   1704  N N   . ALA A  1 259 ? 159.934 166.815 235.982 1.00 163.39 ? 261 ALA A N   1 
ATOM   1705  C CA  . ALA A  1 259 ? 158.658 166.352 236.533 1.00 164.20 ? 261 ALA A CA  1 
ATOM   1706  C C   . ALA A  1 259 ? 157.475 167.181 236.043 1.00 165.67 ? 261 ALA A C   1 
ATOM   1707  O O   . ALA A  1 259 ? 156.465 167.306 236.738 1.00 160.99 ? 261 ALA A O   1 
ATOM   1708  C CB  . ALA A  1 259 ? 158.681 166.327 238.064 1.00 155.58 ? 261 ALA A CB  1 
ATOM   1709  N N   . ASN A  1 260 ? 157.583 167.763 234.854 1.00 167.28 ? 262 ASN A N   1 
ATOM   1710  C CA  . ASN A  1 260 ? 156.435 168.432 234.263 1.00 168.42 ? 262 ASN A CA  1 
ATOM   1711  C C   . ASN A  1 260 ? 155.401 167.405 233.823 1.00 175.59 ? 262 ASN A C   1 
ATOM   1712  O O   . ASN A  1 260 ? 155.746 166.325 233.334 1.00 177.92 ? 262 ASN A O   1 
ATOM   1713  C CB  . ASN A  1 260 ? 156.863 169.290 233.074 1.00 170.97 ? 262 ASN A CB  1 
ATOM   1714  C CG  . ASN A  1 260 ? 158.115 170.095 233.354 1.00 170.95 ? 262 ASN A CG  1 
ATOM   1715  O OD1 . ASN A  1 260 ? 158.645 170.071 234.463 1.00 169.92 ? 262 ASN A OD1 1 
ATOM   1716  N ND2 . ASN A  1 260 ? 158.595 170.812 232.345 1.00 171.87 ? 262 ASN A ND2 1 
ATOM   1717  N N   . ASP A  1 261 ? 154.124 167.747 234.008 1.00 180.47 ? 263 ASP A N   1 
ATOM   1718  C CA  . ASP A  1 261 ? 152.996 166.935 233.551 1.00 183.43 ? 263 ASP A CA  1 
ATOM   1719  C C   . ASP A  1 261 ? 153.036 165.539 234.187 1.00 179.93 ? 263 ASP A C   1 
ATOM   1720  O O   . ASP A  1 261 ? 153.204 164.515 233.522 1.00 181.20 ? 263 ASP A O   1 
ATOM   1721  C CB  . ASP A  1 261 ? 152.982 166.861 232.017 1.00 188.37 ? 263 ASP A CB  1 
ATOM   1722  C CG  . ASP A  1 261 ? 151.805 166.069 231.471 1.00 194.03 ? 263 ASP A CG  1 
ATOM   1723  O OD1 . ASP A  1 261 ? 151.785 165.809 230.249 1.00 195.50 ? 263 ASP A OD1 1 
ATOM   1724  O OD2 . ASP A  1 261 ? 150.891 165.728 232.249 1.00 194.00 ? 263 ASP A OD2 1 
ATOM   1725  N N   . ILE A  1 262 ? 152.897 165.531 235.514 1.00 174.13 ? 264 ILE A N   1 
ATOM   1726  C CA  . ILE A  1 262 ? 152.780 164.297 236.279 1.00 168.20 ? 264 ILE A CA  1 
ATOM   1727  C C   . ILE A  1 262 ? 151.618 164.427 237.252 1.00 168.85 ? 264 ILE A C   1 
ATOM   1728  O O   . ILE A  1 262 ? 151.167 165.527 237.582 1.00 173.72 ? 264 ILE A O   1 
ATOM   1729  C CB  . ILE A  1 262 ? 154.070 163.934 237.053 1.00 166.56 ? 264 ILE A CB  1 
ATOM   1730  C CG1 . ILE A  1 262 ? 154.069 164.579 238.441 1.00 168.19 ? 264 ILE A CG1 1 
ATOM   1731  C CG2 . ILE A  1 262 ? 155.303 164.352 236.289 1.00 166.47 ? 264 ILE A CG2 1 
ATOM   1732  C CD1 . ILE A  1 262 ? 155.281 164.228 239.274 1.00 163.87 ? 264 ILE A CD1 1 
ATOM   1733  N N   . ASP A  1 263 ? 151.127 163.278 237.702 1.00 166.71 ? 265 ASP A N   1 
ATOM   1734  C CA  . ASP A  1 263 ? 150.203 163.224 238.822 1.00 169.78 ? 265 ASP A CA  1 
ATOM   1735  C C   . ASP A  1 263 ? 150.987 163.063 240.116 1.00 172.17 ? 265 ASP A C   1 
ATOM   1736  O O   . ASP A  1 263 ? 151.928 162.271 240.198 1.00 175.77 ? 265 ASP A O   1 
ATOM   1737  C CB  . ASP A  1 263 ? 149.214 162.068 238.661 1.00 167.51 ? 265 ASP A CB  1 
ATOM   1738  C CG  . ASP A  1 263 ? 148.277 162.263 237.488 1.00 171.96 ? 265 ASP A CG  1 
ATOM   1739  O OD1 . ASP A  1 263 ? 148.125 163.416 237.034 1.00 174.24 ? 265 ASP A OD1 1 
ATOM   1740  O OD2 . ASP A  1 263 ? 147.692 161.264 237.020 1.00 173.19 ? 265 ASP A OD2 1 
ATOM   1741  N N   . VAL A  1 264 ? 150.603 163.836 241.129 1.00 172.10 ? 266 VAL A N   1 
ATOM   1742  C CA  . VAL A  1 264 ? 151.281 163.795 242.412 1.00 173.95 ? 266 VAL A CA  1 
ATOM   1743  C C   . VAL A  1 264 ? 150.493 163.026 243.468 1.00 175.75 ? 266 VAL A C   1 
ATOM   1744  O O   . VAL A  1 264 ? 151.090 162.543 244.437 1.00 172.95 ? 266 VAL A O   1 
ATOM   1745  C CB  . VAL A  1 264 ? 151.610 165.220 242.908 1.00 171.67 ? 266 VAL A CB  1 
ATOM   1746  C CG1 . VAL A  1 264 ? 152.186 166.053 241.774 1.00 168.74 ? 266 VAL A CG1 1 
ATOM   1747  C CG2 . VAL A  1 264 ? 150.374 165.887 243.490 1.00 170.46 ? 266 VAL A CG2 1 
ATOM   1748  N N   . ASN A  1 265 ? 149.175 162.892 243.310 1.00 178.80 ? 267 ASN A N   1 
ATOM   1749  C CA  . ASN A  1 265 ? 148.373 162.200 244.310 1.00 181.58 ? 267 ASN A CA  1 
ATOM   1750  C C   . ASN A  1 265 ? 148.529 160.687 244.248 1.00 180.45 ? 267 ASN A C   1 
ATOM   1751  O O   . ASN A  1 265 ? 148.195 160.004 245.222 1.00 180.33 ? 267 ASN A O   1 
ATOM   1752  C CB  . ASN A  1 265 ? 146.899 162.577 244.150 1.00 181.23 ? 267 ASN A CB  1 
ATOM   1753  C CG  . ASN A  1 265 ? 146.234 161.856 242.992 1.00 184.87 ? 267 ASN A CG  1 
ATOM   1754  O OD1 . ASN A  1 265 ? 146.869 161.564 241.977 1.00 181.75 ? 267 ASN A OD1 1 
ATOM   1755  N ND2 . ASN A  1 265 ? 144.948 161.563 243.140 1.00 184.93 ? 267 ASN A ND2 1 
ATOM   1756  N N   . LYS A  1 266 ? 149.025 160.147 243.136 1.00 175.90 ? 268 LYS A N   1 
ATOM   1757  C CA  . LYS A  1 266 ? 149.073 158.699 242.973 1.00 174.45 ? 268 LYS A CA  1 
ATOM   1758  C C   . LYS A  1 266 ? 150.474 158.213 242.621 1.00 173.44 ? 268 LYS A C   1 
ATOM   1759  O O   . LYS A  1 266 ? 150.785 157.031 242.797 1.00 170.15 ? 268 LYS A O   1 
ATOM   1760  C CB  . LYS A  1 266 ? 148.054 158.257 241.923 1.00 173.14 ? 268 LYS A CB  1 
ATOM   1761  C CG  . LYS A  1 266 ? 148.411 158.597 240.494 1.00 165.76 ? 268 LYS A CG  1 
ATOM   1762  C CD  . LYS A  1 266 ? 147.630 157.705 239.551 1.00 162.92 ? 268 LYS A CD  1 
ATOM   1763  C CE  . LYS A  1 266 ? 147.770 158.149 238.113 1.00 156.27 ? 268 LYS A CE  1 
ATOM   1764  N NZ  . LYS A  1 266 ? 147.427 157.034 237.193 1.00 151.81 ? 268 LYS A NZ  1 
ATOM   1765  N N   . TRP A  1 267 ? 151.327 159.108 242.117 1.00 173.35 ? 269 TRP A N   1 
ATOM   1766  C CA  . TRP A  1 267 ? 152.751 158.794 242.077 1.00 168.23 ? 269 TRP A CA  1 
ATOM   1767  C C   . TRP A  1 267 ? 153.299 158.619 243.485 1.00 170.89 ? 269 TRP A C   1 
ATOM   1768  O O   . TRP A  1 267 ? 154.164 157.767 243.717 1.00 170.94 ? 269 TRP A O   1 
ATOM   1769  C CB  . TRP A  1 267 ? 153.522 159.885 241.336 1.00 164.13 ? 269 TRP A CB  1 
ATOM   1770  C CG  . TRP A  1 267 ? 153.811 159.565 239.899 1.00 160.63 ? 269 TRP A CG  1 
ATOM   1771  C CD1 . TRP A  1 267 ? 152.955 159.681 238.844 1.00 164.29 ? 269 TRP A CD1 1 
ATOM   1772  C CD2 . TRP A  1 267 ? 155.051 159.092 239.359 1.00 155.15 ? 269 TRP A CD2 1 
ATOM   1773  N NE1 . TRP A  1 267 ? 153.581 159.303 237.682 1.00 155.80 ? 269 TRP A NE1 1 
ATOM   1774  C CE2 . TRP A  1 267 ? 154.870 158.939 237.971 1.00 153.35 ? 269 TRP A CE2 1 
ATOM   1775  C CE3 . TRP A  1 267 ? 156.295 158.781 239.914 1.00 151.52 ? 269 TRP A CE3 1 
ATOM   1776  C CZ2 . TRP A  1 267 ? 155.884 158.485 237.132 1.00 146.73 ? 269 TRP A CZ2 1 
ATOM   1777  C CZ3 . TRP A  1 267 ? 157.301 158.333 239.079 1.00 146.51 ? 269 TRP A CZ3 1 
ATOM   1778  C CH2 . TRP A  1 267 ? 157.090 158.189 237.704 1.00 146.98 ? 269 TRP A CH2 1 
ATOM   1779  N N   . LYS A  1 268 ? 152.804 159.416 244.435 1.00 173.48 ? 270 LYS A N   1 
ATOM   1780  C CA  . LYS A  1 268 ? 153.123 159.232 245.844 1.00 171.26 ? 270 LYS A CA  1 
ATOM   1781  C C   . LYS A  1 268 ? 152.604 157.912 246.396 1.00 171.49 ? 270 LYS A C   1 
ATOM   1782  O O   . LYS A  1 268 ? 153.085 157.470 247.443 1.00 168.98 ? 270 LYS A O   1 
ATOM   1783  C CB  . LYS A  1 268 ? 152.544 160.384 246.667 1.00 167.39 ? 270 LYS A CB  1 
ATOM   1784  C CG  . LYS A  1 268 ? 153.321 161.685 246.579 1.00 162.88 ? 270 LYS A CG  1 
ATOM   1785  C CD  . LYS A  1 268 ? 153.594 162.249 247.964 1.00 156.29 ? 270 LYS A CD  1 
ATOM   1786  C CE  . LYS A  1 268 ? 154.575 163.406 247.907 1.00 147.26 ? 270 LYS A CE  1 
ATOM   1787  N NZ  . LYS A  1 268 ? 154.408 164.210 246.665 1.00 138.86 ? 270 LYS A NZ  1 
ATOM   1788  N N   . ALA A  1 269 ? 151.636 157.282 245.730 1.00 174.10 ? 271 ALA A N   1 
ATOM   1789  C CA  . ALA A  1 269 ? 151.099 156.015 246.216 1.00 172.99 ? 271 ALA A CA  1 
ATOM   1790  C C   . ALA A  1 269 ? 152.058 154.866 245.929 1.00 173.54 ? 271 ALA A C   1 
ATOM   1791  O O   . ALA A  1 269 ? 152.476 154.147 246.843 1.00 170.95 ? 271 ALA A O   1 
ATOM   1792  C CB  . ALA A  1 269 ? 149.729 155.748 245.587 1.00 168.63 ? 271 ALA A CB  1 
ATOM   1793  N N   . LYS A  1 270 ? 152.411 154.674 244.656 1.00 172.94 ? 272 LYS A N   1 
ATOM   1794  C CA  . LYS A  1 270 ? 153.334 153.602 244.298 1.00 167.97 ? 272 LYS A CA  1 
ATOM   1795  C C   . LYS A  1 270 ? 154.719 153.841 244.886 1.00 164.73 ? 272 LYS A C   1 
ATOM   1796  O O   . LYS A  1 270 ? 155.389 152.894 245.315 1.00 159.84 ? 272 LYS A O   1 
ATOM   1797  C CB  . LYS A  1 270 ? 153.412 153.461 242.778 1.00 160.49 ? 272 LYS A CB  1 
ATOM   1798  C CG  . LYS A  1 270 ? 152.080 153.140 242.119 1.00 157.37 ? 272 LYS A CG  1 
ATOM   1799  C CD  . LYS A  1 270 ? 152.227 152.070 241.047 1.00 153.25 ? 272 LYS A CD  1 
ATOM   1800  C CE  . LYS A  1 270 ? 153.453 152.306 240.182 1.00 148.75 ? 272 LYS A CE  1 
ATOM   1801  N NZ  . LYS A  1 270 ? 153.166 152.067 238.741 1.00 133.69 ? 272 LYS A NZ  1 
ATOM   1802  N N   . LEU A  1 271 ? 155.165 155.094 244.916 1.00 165.17 ? 273 LEU A N   1 
ATOM   1803  C CA  . LEU A  1 271 ? 156.494 155.432 245.404 1.00 164.64 ? 273 LEU A CA  1 
ATOM   1804  C C   . LEU A  1 271 ? 156.520 155.792 246.884 1.00 165.70 ? 273 LEU A C   1 
ATOM   1805  O O   . LEU A  1 271 ? 157.582 156.161 247.396 1.00 166.39 ? 273 LEU A O   1 
ATOM   1806  C CB  . LEU A  1 271 ? 157.082 156.586 244.585 1.00 166.16 ? 273 LEU A CB  1 
ATOM   1807  C CG  . LEU A  1 271 ? 157.842 156.188 243.319 1.00 162.74 ? 273 LEU A CG  1 
ATOM   1808  C CD1 . LEU A  1 271 ? 158.879 155.130 243.651 1.00 160.34 ? 273 LEU A CD1 1 
ATOM   1809  C CD2 . LEU A  1 271 ? 156.900 155.700 242.227 1.00 161.26 ? 273 LEU A CD2 1 
ATOM   1810  N N   . GLY A  1 272 ? 155.393 155.697 247.581 1.00 164.58 ? 274 GLY A N   1 
ATOM   1811  C CA  . GLY A  1 272 ? 155.354 156.002 248.999 1.00 157.97 ? 274 GLY A CA  1 
ATOM   1812  C C   . GLY A  1 272 ? 155.530 157.478 249.298 1.00 150.32 ? 274 GLY A C   1 
ATOM   1813  O O   . GLY A  1 272 ? 155.532 157.892 250.457 1.00 129.49 ? 274 GLY A O   1 
ATOM   1814  N N   . ALA B  1 24  ? 151.783 168.410 127.250 1.00 122.30 ? 26  ALA B N   1 
ATOM   1815  C CA  . ALA B  1 24  ? 151.904 167.002 127.604 1.00 124.59 ? 26  ALA B CA  1 
ATOM   1816  C C   . ALA B  1 24  ? 153.195 166.743 128.371 1.00 121.62 ? 26  ALA B C   1 
ATOM   1817  O O   . ALA B  1 24  ? 154.205 167.404 128.130 1.00 118.47 ? 26  ALA B O   1 
ATOM   1818  C CB  . ALA B  1 24  ? 151.844 166.134 126.356 1.00 117.21 ? 26  ALA B CB  1 
ATOM   1819  N N   . PRO B  1 25  ? 153.157 165.791 129.301 1.00 116.98 ? 27  PRO B N   1 
ATOM   1820  C CA  . PRO B  1 25  ? 154.369 165.445 130.050 1.00 113.46 ? 27  PRO B CA  1 
ATOM   1821  C C   . PRO B  1 25  ? 155.466 164.948 129.122 1.00 112.83 ? 27  PRO B C   1 
ATOM   1822  O O   . PRO B  1 25  ? 155.202 164.324 128.093 1.00 108.59 ? 27  PRO B O   1 
ATOM   1823  C CB  . PRO B  1 25  ? 153.892 164.341 130.996 1.00 111.71 ? 27  PRO B CB  1 
ATOM   1824  C CG  . PRO B  1 25  ? 152.446 164.625 131.186 1.00 111.37 ? 27  PRO B CG  1 
ATOM   1825  C CD  . PRO B  1 25  ? 151.964 165.129 129.854 1.00 116.99 ? 27  PRO B CD  1 
ATOM   1826  N N   . VAL B  1 26  ? 156.711 165.236 129.496 1.00 111.47 ? 28  VAL B N   1 
ATOM   1827  C CA  . VAL B  1 26  ? 157.865 164.886 128.682 1.00 108.13 ? 28  VAL B CA  1 
ATOM   1828  C C   . VAL B  1 26  ? 159.015 164.483 129.594 1.00 105.26 ? 28  VAL B C   1 
ATOM   1829  O O   . VAL B  1 26  ? 159.086 164.891 130.758 1.00 105.50 ? 28  VAL B O   1 
ATOM   1830  C CB  . VAL B  1 26  ? 158.276 166.054 127.754 1.00 103.95 ? 28  VAL B CB  1 
ATOM   1831  C CG1 . VAL B  1 26  ? 158.999 167.136 128.540 1.00 95.35  ? 28  VAL B CG1 1 
ATOM   1832  C CG2 . VAL B  1 26  ? 159.128 165.554 126.596 1.00 102.67 ? 28  VAL B CG2 1 
ATOM   1833  N N   . ILE B  1 27  ? 159.911 163.658 129.059 1.00 101.78 ? 29  ILE B N   1 
ATOM   1834  C CA  . ILE B  1 27  ? 161.167 163.305 129.708 1.00 98.37  ? 29  ILE B CA  1 
ATOM   1835  C C   . ILE B  1 27  ? 162.294 163.972 128.930 1.00 103.18 ? 29  ILE B C   1 
ATOM   1836  O O   . ILE B  1 27  ? 162.344 163.889 127.697 1.00 106.03 ? 29  ILE B O   1 
ATOM   1837  C CB  . ILE B  1 27  ? 161.348 161.776 129.805 1.00 94.47  ? 29  ILE B CB  1 
ATOM   1838  C CG1 . ILE B  1 27  ? 162.448 161.418 130.807 1.00 94.39  ? 29  ILE B CG1 1 
ATOM   1839  C CG2 . ILE B  1 27  ? 161.589 161.133 128.442 1.00 95.43  ? 29  ILE B CG2 1 
ATOM   1840  C CD1 . ILE B  1 27  ? 161.932 161.056 132.174 1.00 88.55  ? 29  ILE B CD1 1 
ATOM   1841  N N   . LYS B  1 28  ? 163.165 164.681 129.642 1.00 98.93  ? 30  LYS B N   1 
ATOM   1842  C CA  . LYS B  1 28  ? 164.202 165.459 128.981 1.00 98.00  ? 30  LYS B CA  1 
ATOM   1843  C C   . LYS B  1 28  ? 165.314 165.759 129.972 1.00 104.04 ? 30  LYS B C   1 
ATOM   1844  O O   . LYS B  1 28  ? 165.132 165.669 131.188 1.00 102.03 ? 30  LYS B O   1 
ATOM   1845  C CB  . LYS B  1 28  ? 163.640 166.761 128.401 1.00 97.19  ? 30  LYS B CB  1 
ATOM   1846  C CG  . LYS B  1 28  ? 163.228 167.774 129.453 1.00 102.27 ? 30  LYS B CG  1 
ATOM   1847  C CD  . LYS B  1 28  ? 162.250 168.789 128.889 1.00 101.97 ? 30  LYS B CD  1 
ATOM   1848  C CE  . LYS B  1 28  ? 162.975 169.932 128.204 1.00 109.74 ? 30  LYS B CE  1 
ATOM   1849  N NZ  . LYS B  1 28  ? 164.269 170.244 128.870 1.00 113.82 ? 30  LYS B NZ  1 
ATOM   1850  N N   . ALA B  1 29  ? 166.471 166.120 129.427 1.00 108.02 ? 31  ALA B N   1 
ATOM   1851  C CA  . ALA B  1 29  ? 167.611 166.497 130.245 1.00 108.27 ? 31  ALA B CA  1 
ATOM   1852  C C   . ALA B  1 29  ? 167.422 167.893 130.822 1.00 106.05 ? 31  ALA B C   1 
ATOM   1853  O O   . ALA B  1 29  ? 166.808 168.767 130.205 1.00 106.88 ? 31  ALA B O   1 
ATOM   1854  C CB  . ALA B  1 29  ? 168.901 166.445 129.428 1.00 105.53 ? 31  ALA B CB  1 
ATOM   1855  N N   . GLY B  1 30  ? 167.958 168.096 132.021 1.00 106.49 ? 32  GLY B N   1 
ATOM   1856  C CA  . GLY B  1 30  ? 167.928 169.404 132.641 1.00 109.21 ? 32  GLY B CA  1 
ATOM   1857  C C   . GLY B  1 30  ? 168.976 170.331 132.061 1.00 115.60 ? 32  GLY B C   1 
ATOM   1858  O O   . GLY B  1 30  ? 169.362 170.189 130.898 1.00 115.96 ? 32  GLY B O   1 
ATOM   1859  N N   . THR B  1 31  ? 169.447 171.285 132.860 1.00 116.81 ? 33  THR B N   1 
ATOM   1860  C CA  . THR B  1 31  ? 170.470 172.225 132.427 1.00 117.69 ? 33  THR B CA  1 
ATOM   1861  C C   . THR B  1 31  ? 171.873 171.803 132.835 1.00 120.67 ? 33  THR B C   1 
ATOM   1862  O O   . THR B  1 31  ? 172.826 172.548 132.583 1.00 125.16 ? 33  THR B O   1 
ATOM   1863  C CB  . THR B  1 31  ? 170.173 173.623 132.978 1.00 119.60 ? 33  THR B CB  1 
ATOM   1864  O OG1 . THR B  1 31  ? 169.695 173.516 134.323 1.00 120.04 ? 33  THR B OG1 1 
ATOM   1865  C CG2 . THR B  1 31  ? 169.120 174.314 132.127 1.00 119.52 ? 33  THR B CG2 1 
ATOM   1866  N N   . ALA B  1 32  ? 172.028 170.636 133.453 1.00 121.65 ? 34  ALA B N   1 
ATOM   1867  C CA  . ALA B  1 32  ? 173.321 170.141 133.895 1.00 120.41 ? 34  ALA B CA  1 
ATOM   1868  C C   . ALA B  1 32  ? 173.499 168.704 133.429 1.00 120.88 ? 34  ALA B C   1 
ATOM   1869  O O   . ALA B  1 32  ? 172.558 168.053 132.968 1.00 123.52 ? 34  ALA B O   1 
ATOM   1870  C CB  . ALA B  1 32  ? 173.466 170.231 135.419 1.00 110.64 ? 34  ALA B CB  1 
ATOM   1871  N N   . THR B  1 33  ? 174.731 168.214 133.546 1.00 117.76 ? 35  THR B N   1 
ATOM   1872  C CA  . THR B  1 33  ? 175.041 166.854 133.128 1.00 119.36 ? 35  THR B CA  1 
ATOM   1873  C C   . THR B  1 33  ? 174.277 165.843 133.973 1.00 121.06 ? 35  THR B C   1 
ATOM   1874  O O   . THR B  1 33  ? 174.245 165.941 135.203 1.00 121.26 ? 35  THR B O   1 
ATOM   1875  C CB  . THR B  1 33  ? 176.544 166.601 133.234 1.00 117.37 ? 35  THR B CB  1 
ATOM   1876  O OG1 . THR B  1 33  ? 177.255 167.676 132.610 1.00 120.56 ? 35  THR B OG1 1 
ATOM   1877  C CG2 . THR B  1 33  ? 176.912 165.295 132.549 1.00 117.38 ? 35  THR B CG2 1 
ATOM   1878  N N   . ASP B  1 34  ? 173.662 164.868 133.301 1.00 119.64 ? 36  ASP B N   1 
ATOM   1879  C CA  . ASP B  1 34  ? 172.924 163.787 133.956 1.00 117.89 ? 36  ASP B CA  1 
ATOM   1880  C C   . ASP B  1 34  ? 171.802 164.325 134.841 1.00 117.31 ? 36  ASP B C   1 
ATOM   1881  O O   . ASP B  1 34  ? 171.516 163.785 135.911 1.00 116.31 ? 36  ASP B O   1 
ATOM   1882  C CB  . ASP B  1 34  ? 173.863 162.885 134.759 1.00 119.32 ? 36  ASP B CB  1 
ATOM   1883  C CG  . ASP B  1 34  ? 174.810 162.100 133.875 1.00 127.28 ? 36  ASP B CG  1 
ATOM   1884  O OD1 . ASP B  1 34  ? 174.747 162.269 132.640 1.00 122.12 ? 36  ASP B OD1 1 
ATOM   1885  O OD2 . ASP B  1 34  ? 175.618 161.317 134.416 1.00 133.22 ? 36  ASP B OD2 1 
ATOM   1886  N N   . SER B  1 35  ? 171.153 165.393 134.388 1.00 113.45 ? 37  SER B N   1 
ATOM   1887  C CA  . SER B  1 35  ? 170.017 165.974 135.089 1.00 104.91 ? 37  SER B CA  1 
ATOM   1888  C C   . SER B  1 35  ? 168.738 165.610 134.347 1.00 106.59 ? 37  SER B C   1 
ATOM   1889  O O   . SER B  1 35  ? 168.675 165.726 133.120 1.00 110.89 ? 37  SER B O   1 
ATOM   1890  C CB  . SER B  1 35  ? 170.158 167.491 135.203 1.00 108.00 ? 37  SER B CB  1 
ATOM   1891  O OG  . SER B  1 35  ? 170.510 168.063 133.957 1.00 120.63 ? 37  SER B OG  1 
ATOM   1892  N N   . THR B  1 36  ? 167.727 165.173 135.091 1.00 104.40 ? 38  THR B N   1 
ATOM   1893  C CA  . THR B  1 36  ? 166.505 164.628 134.519 1.00 101.52 ? 38  THR B CA  1 
ATOM   1894  C C   . THR B  1 36  ? 165.302 165.464 134.927 1.00 100.84 ? 38  THR B C   1 
ATOM   1895  O O   . THR B  1 36  ? 165.174 165.863 136.089 1.00 103.87 ? 38  THR B O   1 
ATOM   1896  C CB  . THR B  1 36  ? 166.294 163.177 134.964 1.00 101.10 ? 38  THR B CB  1 
ATOM   1897  O OG1 . THR B  1 36  ? 167.488 162.423 134.720 1.00 108.39 ? 38  THR B OG1 1 
ATOM   1898  C CG2 . THR B  1 36  ? 165.135 162.546 134.214 1.00 98.21  ? 38  THR B CG2 1 
ATOM   1899  N N   . GLU B  1 37  ? 164.422 165.727 133.964 1.00 98.01  ? 39  GLU B N   1 
ATOM   1900  C CA  . GLU B  1 37  ? 163.137 166.366 134.214 1.00 95.45  ? 39  GLU B CA  1 
ATOM   1901  C C   . GLU B  1 37  ? 162.041 165.450 133.692 1.00 100.13 ? 39  GLU B C   1 
ATOM   1902  O O   . GLU B  1 37  ? 161.986 165.167 132.491 1.00 103.55 ? 39  GLU B O   1 
ATOM   1903  C CB  . GLU B  1 37  ? 163.058 167.738 133.543 1.00 99.23  ? 39  GLU B CB  1 
ATOM   1904  C CG  . GLU B  1 37  ? 163.843 168.823 134.253 1.00 106.30 ? 39  GLU B CG  1 
ATOM   1905  C CD  . GLU B  1 37  ? 163.975 170.079 133.419 1.00 114.06 ? 39  GLU B CD  1 
ATOM   1906  O OE1 . GLU B  1 37  ? 163.270 170.189 132.395 1.00 113.36 ? 39  GLU B OE1 1 
ATOM   1907  O OE2 . GLU B  1 37  ? 164.784 170.956 133.785 1.00 113.43 ? 39  GLU B OE2 1 
ATOM   1908  N N   . ALA B  1 38  ? 161.174 164.990 134.590 1.00 98.37  ? 40  ALA B N   1 
ATOM   1909  C CA  . ALA B  1 38  ? 160.077 164.098 134.240 1.00 92.66  ? 40  ALA B CA  1 
ATOM   1910  C C   . ALA B  1 38  ? 158.774 164.732 134.693 1.00 97.88  ? 40  ALA B C   1 
ATOM   1911  O O   . ALA B  1 38  ? 158.651 165.142 135.852 1.00 102.76 ? 40  ALA B O   1 
ATOM   1912  C CB  . ALA B  1 38  ? 160.254 162.720 134.878 1.00 89.56  ? 40  ALA B CB  1 
ATOM   1913  N N   . GLY B  1 39  ? 157.802 164.807 133.785 1.00 97.24  ? 41  GLY B N   1 
ATOM   1914  C CA  . GLY B  1 39  ? 156.537 165.450 134.061 1.00 99.48  ? 41  GLY B CA  1 
ATOM   1915  C C   . GLY B  1 39  ? 156.371 166.715 133.239 1.00 104.52 ? 41  GLY B C   1 
ATOM   1916  O O   . GLY B  1 39  ? 156.889 166.821 132.121 1.00 109.57 ? 41  GLY B O   1 
ATOM   1917  N N   . VAL B  1 40  ? 155.647 167.673 133.808 1.00 103.84 ? 42  VAL B N   1 
ATOM   1918  C CA  . VAL B  1 40  ? 155.371 168.945 133.155 1.00 109.47 ? 42  VAL B CA  1 
ATOM   1919  C C   . VAL B  1 40  ? 155.835 170.075 134.065 1.00 108.92 ? 42  VAL B C   1 
ATOM   1920  O O   . VAL B  1 40  ? 155.641 170.020 135.286 1.00 107.52 ? 42  VAL B O   1 
ATOM   1921  C CB  . VAL B  1 40  ? 153.881 169.081 132.782 1.00 108.25 ? 42  VAL B CB  1 
ATOM   1922  C CG1 . VAL B  1 40  ? 153.014 169.288 134.009 1.00 97.82  ? 42  VAL B CG1 1 
ATOM   1923  C CG2 . VAL B  1 40  ? 153.685 170.219 131.794 1.00 114.11 ? 42  VAL B CG2 1 
ATOM   1924  N N   . ASP B  1 41  ? 156.498 171.069 133.471 1.00 110.72 ? 43  ASP B N   1 
ATOM   1925  C CA  . ASP B  1 41  ? 156.940 172.280 134.164 1.00 110.09 ? 43  ASP B CA  1 
ATOM   1926  C C   . ASP B  1 41  ? 157.920 171.953 135.293 1.00 112.27 ? 43  ASP B C   1 
ATOM   1927  O O   . ASP B  1 41  ? 157.752 172.369 136.438 1.00 109.70 ? 43  ASP B O   1 
ATOM   1928  C CB  . ASP B  1 41  ? 155.740 173.072 134.693 1.00 115.21 ? 43  ASP B CB  1 
ATOM   1929  C CG  . ASP B  1 41  ? 154.898 173.665 133.583 1.00 128.64 ? 43  ASP B CG  1 
ATOM   1930  O OD1 . ASP B  1 41  ? 155.065 173.244 132.419 1.00 131.26 ? 43  ASP B OD1 1 
ATOM   1931  O OD2 . ASP B  1 41  ? 154.065 174.548 133.875 1.00 128.45 ? 43  ASP B OD2 1 
ATOM   1932  N N   . ASN B  1 42  ? 158.967 171.212 134.945 1.00 108.64 ? 44  ASN B N   1 
ATOM   1933  C CA  . ASN B  1 42  ? 160.005 170.843 135.894 1.00 100.29 ? 44  ASN B CA  1 
ATOM   1934  C C   . ASN B  1 42  ? 161.307 171.556 135.555 1.00 102.14 ? 44  ASN B C   1 
ATOM   1935  O O   . ASN B  1 42  ? 161.562 171.907 134.400 1.00 108.60 ? 44  ASN B O   1 
ATOM   1936  C CB  . ASN B  1 42  ? 160.235 169.330 135.907 1.00 95.55  ? 44  ASN B CB  1 
ATOM   1937  C CG  . ASN B  1 42  ? 159.185 168.590 136.702 1.00 99.36  ? 44  ASN B CG  1 
ATOM   1938  O OD1 . ASN B  1 42  ? 159.480 167.991 137.734 1.00 99.14  ? 44  ASN B OD1 1 
ATOM   1939  N ND2 . ASN B  1 42  ? 157.949 168.624 136.223 1.00 105.55 ? 44  ASN B ND2 1 
ATOM   1940  N N   . VAL B  1 43  ? 162.128 171.772 136.580 1.00 99.65  ? 45  VAL B N   1 
ATOM   1941  C CA  . VAL B  1 43  ? 163.433 172.405 136.432 1.00 95.97  ? 45  VAL B CA  1 
ATOM   1942  C C   . VAL B  1 43  ? 164.452 171.596 137.219 1.00 98.60  ? 45  VAL B C   1 
ATOM   1943  O O   . VAL B  1 43  ? 164.261 171.342 138.413 1.00 100.05 ? 45  VAL B O   1 
ATOM   1944  C CB  . VAL B  1 43  ? 163.419 173.868 136.913 1.00 93.35  ? 45  VAL B CB  1 
ATOM   1945  C CG1 . VAL B  1 43  ? 164.837 174.393 137.051 1.00 93.93  ? 45  VAL B CG1 1 
ATOM   1946  C CG2 . VAL B  1 43  ? 162.623 174.734 135.953 1.00 95.26  ? 45  VAL B CG2 1 
ATOM   1947  N N   . ALA B  1 44  ? 165.531 171.191 136.552 1.00 101.60 ? 46  ALA B N   1 
ATOM   1948  C CA  . ALA B  1 44  ? 166.638 170.484 137.187 1.00 102.06 ? 46  ALA B CA  1 
ATOM   1949  C C   . ALA B  1 44  ? 167.931 171.162 136.761 1.00 108.24 ? 46  ALA B C   1 
ATOM   1950  O O   . ALA B  1 44  ? 168.271 171.164 135.573 1.00 112.31 ? 46  ALA B O   1 
ATOM   1951  C CB  . ALA B  1 44  ? 166.644 169.004 136.809 1.00 99.37  ? 46  ALA B CB  1 
ATOM   1952  N N   . ASN B  1 45  ? 168.654 171.734 137.725 1.00 105.35 ? 47  ASN B N   1 
ATOM   1953  C CA  . ASN B  1 45  ? 169.842 172.520 137.430 1.00 100.80 ? 47  ASN B CA  1 
ATOM   1954  C C   . ASN B  1 45  ? 171.132 171.946 137.990 1.00 107.84 ? 47  ASN B C   1 
ATOM   1955  O O   . ASN B  1 45  ? 172.207 172.339 137.526 1.00 112.84 ? 47  ASN B O   1 
ATOM   1956  C CB  . ASN B  1 45  ? 169.678 173.954 137.956 1.00 97.87  ? 47  ASN B CB  1 
ATOM   1957  C CG  . ASN B  1 45  ? 168.741 174.779 137.105 1.00 110.32 ? 47  ASN B CG  1 
ATOM   1958  O OD1 . ASN B  1 45  ? 168.433 174.414 135.971 1.00 116.50 ? 47  ASN B OD1 1 
ATOM   1959  N ND2 . ASN B  1 45  ? 168.278 175.898 137.647 1.00 115.21 ? 47  ASN B ND2 1 
ATOM   1960  N N   . GLY B  1 46  ? 171.066 171.045 138.965 1.00 107.57 ? 48  GLY B N   1 
ATOM   1961  C CA  . GLY B  1 46  ? 172.267 170.463 139.517 1.00 102.65 ? 48  GLY B CA  1 
ATOM   1962  C C   . GLY B  1 46  ? 172.754 169.260 138.731 1.00 104.85 ? 48  GLY B C   1 
ATOM   1963  O O   . GLY B  1 46  ? 171.998 168.607 138.016 1.00 109.96 ? 48  GLY B O   1 
ATOM   1964  N N   . VAL B  1 47  ? 174.049 168.975 138.871 1.00 102.87 ? 49  VAL B N   1 
ATOM   1965  C CA  . VAL B  1 47  ? 174.625 167.795 138.240 1.00 101.61 ? 49  VAL B CA  1 
ATOM   1966  C C   . VAL B  1 47  ? 174.099 166.550 138.939 1.00 104.33 ? 49  VAL B C   1 
ATOM   1967  O O   . VAL B  1 47  ? 174.060 166.484 140.174 1.00 110.10 ? 49  VAL B O   1 
ATOM   1968  C CB  . VAL B  1 47  ? 176.158 167.852 138.281 1.00 97.36  ? 49  VAL B CB  1 
ATOM   1969  C CG1 . VAL B  1 47  ? 176.746 166.947 137.215 1.00 102.94 ? 49  VAL B CG1 1 
ATOM   1970  C CG2 . VAL B  1 47  ? 176.639 169.280 138.095 1.00 97.09  ? 49  VAL B CG2 1 
ATOM   1971  N N   . LYS B  1 48  ? 173.688 165.559 138.147 1.00 103.30 ? 50  LYS B N   1 
ATOM   1972  C CA  . LYS B  1 48  ? 173.108 164.316 138.659 1.00 100.03 ? 50  LYS B CA  1 
ATOM   1973  C C   . LYS B  1 48  ? 171.873 164.577 139.515 1.00 103.50 ? 50  LYS B C   1 
ATOM   1974  O O   . LYS B  1 48  ? 171.594 163.840 140.463 1.00 107.88 ? 50  LYS B O   1 
ATOM   1975  C CB  . LYS B  1 48  ? 174.138 163.498 139.443 1.00 104.13 ? 50  LYS B CB  1 
ATOM   1976  C CG  . LYS B  1 48  ? 175.504 163.420 138.788 1.00 110.59 ? 50  LYS B CG  1 
ATOM   1977  C CD  . LYS B  1 48  ? 176.466 162.595 139.624 1.00 113.22 ? 50  LYS B CD  1 
ATOM   1978  C CE  . LYS B  1 48  ? 177.618 162.071 138.785 1.00 114.45 ? 50  LYS B CE  1 
ATOM   1979  N NZ  . LYS B  1 48  ? 177.528 162.526 137.372 1.00 117.19 ? 50  LYS B NZ  1 
ATOM   1980  N N   . SER B  1 49  ? 171.125 165.624 139.190 1.00 102.63 ? 51  SER B N   1 
ATOM   1981  C CA  . SER B  1 49  ? 169.890 165.956 139.881 1.00 96.07  ? 51  SER B CA  1 
ATOM   1982  C C   . SER B  1 49  ? 168.694 165.491 139.061 1.00 99.41  ? 51  SER B C   1 
ATOM   1983  O O   . SER B  1 49  ? 168.818 165.124 137.891 1.00 106.16 ? 51  SER B O   1 
ATOM   1984  C CB  . SER B  1 49  ? 169.799 167.460 140.141 1.00 97.03  ? 51  SER B CB  1 
ATOM   1985  O OG  . SER B  1 49  ? 169.840 168.188 138.927 1.00 102.93 ? 51  SER B OG  1 
ATOM   1986  N N   . SER B  1 50  ? 167.523 165.503 139.693 1.00 97.54  ? 52  SER B N   1 
ATOM   1987  C CA  . SER B  1 50  ? 166.314 165.036 139.034 1.00 97.67  ? 52  SER B CA  1 
ATOM   1988  C C   . SER B  1 50  ? 165.095 165.673 139.680 1.00 95.70  ? 52  SER B C   1 
ATOM   1989  O O   . SER B  1 50  ? 165.049 165.848 140.900 1.00 94.49  ? 52  SER B O   1 
ATOM   1990  C CB  . SER B  1 50  ? 166.205 163.509 139.094 1.00 93.79  ? 52  SER B CB  1 
ATOM   1991  O OG  . SER B  1 50  ? 166.293 163.048 140.430 1.00 98.51  ? 52  SER B OG  1 
ATOM   1992  N N   . ALA B  1 51  ? 164.111 166.013 138.850 1.00 90.23  ? 53  ALA B N   1 
ATOM   1993  C CA  . ALA B  1 51  ? 162.844 166.577 139.302 1.00 87.19  ? 53  ALA B CA  1 
ATOM   1994  C C   . ALA B  1 51  ? 161.721 165.816 138.613 1.00 92.65  ? 53  ALA B C   1 
ATOM   1995  O O   . ALA B  1 51  ? 161.539 165.940 137.398 1.00 99.04  ? 53  ALA B O   1 
ATOM   1996  C CB  . ALA B  1 51  ? 162.762 168.072 138.998 1.00 93.78  ? 53  ALA B CB  1 
ATOM   1997  N N   . PHE B  1 52  ? 160.973 165.033 139.384 1.00 88.29  ? 54  PHE B N   1 
ATOM   1998  C CA  . PHE B  1 52  ? 159.917 164.178 138.860 1.00 84.16  ? 54  PHE B CA  1 
ATOM   1999  C C   . PHE B  1 52  ? 158.581 164.626 139.433 1.00 87.66  ? 54  PHE B C   1 
ATOM   2000  O O   . PHE B  1 52  ? 158.429 164.731 140.654 1.00 93.90  ? 54  PHE B O   1 
ATOM   2001  C CB  . PHE B  1 52  ? 160.172 162.709 139.211 1.00 88.02  ? 54  PHE B CB  1 
ATOM   2002  C CG  . PHE B  1 52  ? 161.197 162.037 138.338 1.00 90.59  ? 54  PHE B CG  1 
ATOM   2003  C CD1 . PHE B  1 52  ? 162.451 162.592 138.158 1.00 91.20  ? 54  PHE B CD1 1 
ATOM   2004  C CD2 . PHE B  1 52  ? 160.908 160.839 137.712 1.00 91.62  ? 54  PHE B CD2 1 
ATOM   2005  C CE1 . PHE B  1 52  ? 163.391 161.972 137.360 1.00 89.70  ? 54  PHE B CE1 1 
ATOM   2006  C CE2 . PHE B  1 52  ? 161.845 160.216 136.913 1.00 92.11  ? 54  PHE B CE2 1 
ATOM   2007  C CZ  . PHE B  1 52  ? 163.087 160.783 136.738 1.00 88.28  ? 54  PHE B CZ  1 
ATOM   2008  N N   . GLY B  1 53  ? 157.617 164.883 138.554 1.00 87.26  ? 55  GLY B N   1 
ATOM   2009  C CA  . GLY B  1 53  ? 156.302 165.306 138.988 1.00 87.99  ? 55  GLY B CA  1 
ATOM   2010  C C   . GLY B  1 53  ? 155.828 166.573 138.309 1.00 91.68  ? 55  GLY B C   1 
ATOM   2011  O O   . GLY B  1 53  ? 156.000 166.735 137.098 1.00 91.60  ? 55  GLY B O   1 
ATOM   2012  N N   . TYR B  1 54  ? 155.227 167.479 139.078 1.00 95.72  ? 56  TYR B N   1 
ATOM   2013  C CA  . TYR B  1 54  ? 154.726 168.742 138.554 1.00 95.89  ? 56  TYR B CA  1 
ATOM   2014  C C   . TYR B  1 54  ? 155.321 169.899 139.342 1.00 98.32  ? 56  TYR B C   1 
ATOM   2015  O O   . TYR B  1 54  ? 155.231 169.925 140.573 1.00 100.32 ? 56  TYR B O   1 
ATOM   2016  C CB  . TYR B  1 54  ? 153.196 168.804 138.615 1.00 89.05  ? 56  TYR B CB  1 
ATOM   2017  C CG  . TYR B  1 54  ? 152.641 170.190 138.378 1.00 97.06  ? 56  TYR B CG  1 
ATOM   2018  C CD1 . TYR B  1 54  ? 152.562 170.716 137.098 1.00 102.17 ? 56  TYR B CD1 1 
ATOM   2019  C CD2 . TYR B  1 54  ? 152.197 170.972 139.434 1.00 100.24 ? 56  TYR B CD2 1 
ATOM   2020  C CE1 . TYR B  1 54  ? 152.059 171.981 136.874 1.00 101.54 ? 56  TYR B CE1 1 
ATOM   2021  C CE2 . TYR B  1 54  ? 151.692 172.240 139.220 1.00 102.12 ? 56  TYR B CE2 1 
ATOM   2022  C CZ  . TYR B  1 54  ? 151.626 172.738 137.938 1.00 100.58 ? 56  TYR B CZ  1 
ATOM   2023  O OH  . TYR B  1 54  ? 151.123 173.999 137.718 1.00 102.18 ? 56  TYR B OH  1 
ATOM   2024  N N   . ASP B  1 55  ? 155.909 170.857 138.624 1.00 95.56  ? 57  ASP B N   1 
ATOM   2025  C CA  . ASP B  1 55  ? 156.430 172.092 139.213 1.00 95.71  ? 57  ASP B CA  1 
ATOM   2026  C C   . ASP B  1 55  ? 157.500 171.814 140.266 1.00 98.26  ? 57  ASP B C   1 
ATOM   2027  O O   . ASP B  1 55  ? 157.543 172.456 141.316 1.00 99.36  ? 57  ASP B O   1 
ATOM   2028  C CB  . ASP B  1 55  ? 155.299 172.939 139.799 1.00 105.39 ? 57  ASP B CB  1 
ATOM   2029  C CG  . ASP B  1 55  ? 155.579 174.423 139.712 1.00 117.65 ? 57  ASP B CG  1 
ATOM   2030  O OD1 . ASP B  1 55  ? 156.462 174.817 138.922 1.00 118.69 ? 57  ASP B OD1 1 
ATOM   2031  O OD2 . ASP B  1 55  ? 154.914 175.196 140.432 1.00 125.23 ? 57  ASP B OD2 1 
ATOM   2032  N N   . ASN B  1 56  ? 158.385 170.867 139.976 1.00 94.61  ? 58  ASN B N   1 
ATOM   2033  C CA  . ASN B  1 56  ? 159.467 170.508 140.880 1.00 91.94  ? 58  ASN B CA  1 
ATOM   2034  C C   . ASN B  1 56  ? 160.763 171.169 140.430 1.00 96.97  ? 58  ASN B C   1 
ATOM   2035  O O   . ASN B  1 56  ? 161.052 171.242 139.232 1.00 100.83 ? 58  ASN B O   1 
ATOM   2036  C CB  . ASN B  1 56  ? 159.647 168.991 140.937 1.00 88.64  ? 58  ASN B CB  1 
ATOM   2037  C CG  . ASN B  1 56  ? 158.546 168.306 141.713 1.00 89.89  ? 58  ASN B CG  1 
ATOM   2038  O OD1 . ASN B  1 56  ? 157.412 168.776 141.745 1.00 96.28  ? 58  ASN B OD1 1 
ATOM   2039  N ND2 . ASN B  1 56  ? 158.872 167.187 142.342 1.00 93.81  ? 58  ASN B ND2 1 
ATOM   2040  N N   . LYS B  1 57  ? 161.538 171.656 141.398 1.00 96.67  ? 59  LYS B N   1 
ATOM   2041  C CA  . LYS B  1 57  ? 162.823 172.291 141.131 1.00 92.18  ? 59  LYS B CA  1 
ATOM   2042  C C   . LYS B  1 57  ? 163.902 171.592 141.942 1.00 98.59  ? 59  LYS B C   1 
ATOM   2043  O O   . LYS B  1 57  ? 163.806 171.514 143.170 1.00 101.63 ? 59  LYS B O   1 
ATOM   2044  C CB  . LYS B  1 57  ? 162.789 173.785 141.468 1.00 87.44  ? 59  LYS B CB  1 
ATOM   2045  C CG  . LYS B  1 57  ? 161.601 174.533 140.896 1.00 95.83  ? 59  LYS B CG  1 
ATOM   2046  C CD  . LYS B  1 57  ? 161.741 176.031 141.115 1.00 105.16 ? 59  LYS B CD  1 
ATOM   2047  C CE  . LYS B  1 57  ? 161.098 176.819 139.987 1.00 112.54 ? 59  LYS B CE  1 
ATOM   2048  N NZ  . LYS B  1 57  ? 160.125 175.994 139.220 1.00 107.95 ? 59  LYS B NZ  1 
ATOM   2049  N N   . ALA B  1 58  ? 164.925 171.090 141.255 1.00 97.62  ? 60  ALA B N   1 
ATOM   2050  C CA  . ALA B  1 58  ? 166.115 170.523 141.882 1.00 95.40  ? 60  ALA B CA  1 
ATOM   2051  C C   . ALA B  1 58  ? 167.313 171.295 141.350 1.00 102.76 ? 60  ALA B C   1 
ATOM   2052  O O   . ALA B  1 58  ? 167.718 171.106 140.198 1.00 105.97 ? 60  ALA B O   1 
ATOM   2053  C CB  . ALA B  1 58  ? 166.240 169.029 141.588 1.00 91.88  ? 60  ALA B CB  1 
ATOM   2054  N N   . ILE B  1 59  ? 167.884 172.159 142.187 1.00 104.38 ? 61  ILE B N   1 
ATOM   2055  C CA  . ILE B  1 59  ? 168.839 173.162 141.727 1.00 101.95 ? 61  ILE B CA  1 
ATOM   2056  C C   . ILE B  1 59  ? 170.270 172.867 142.151 1.00 106.93 ? 61  ILE B C   1 
ATOM   2057  O O   . ILE B  1 59  ? 171.195 173.520 141.640 1.00 110.98 ? 61  ILE B O   1 
ATOM   2058  C CB  . ILE B  1 59  ? 168.430 174.573 142.198 1.00 101.23 ? 61  ILE B CB  1 
ATOM   2059  C CG1 . ILE B  1 59  ? 166.907 174.692 142.219 1.00 101.83 ? 61  ILE B CG1 1 
ATOM   2060  C CG2 . ILE B  1 59  ? 168.997 175.637 141.275 1.00 100.23 ? 61  ILE B CG2 1 
ATOM   2061  C CD1 . ILE B  1 59  ? 166.404 176.016 142.732 1.00 106.50 ? 61  ILE B CD1 1 
ATOM   2062  N N   . GLU B  1 60  ? 170.493 171.911 143.043 1.00 106.37 ? 62  GLU B N   1 
ATOM   2063  C CA  . GLU B  1 60  ? 171.828 171.625 143.542 1.00 107.86 ? 62  GLU B CA  1 
ATOM   2064  C C   . GLU B  1 60  ? 172.280 170.235 143.111 1.00 107.90 ? 62  GLU B C   1 
ATOM   2065  O O   . GLU B  1 60  ? 171.496 169.418 142.622 1.00 111.22 ? 62  GLU B O   1 
ATOM   2066  C CB  . GLU B  1 60  ? 171.877 171.756 145.069 1.00 107.01 ? 62  GLU B CB  1 
ATOM   2067  C CG  . GLU B  1 60  ? 172.538 173.030 145.639 1.00 114.78 ? 62  GLU B CG  1 
ATOM   2068  C CD  . GLU B  1 60  ? 173.890 173.422 145.027 1.00 125.29 ? 62  GLU B CD  1 
ATOM   2069  O OE1 . GLU B  1 60  ? 174.457 174.434 145.491 1.00 131.93 ? 62  GLU B OE1 1 
ATOM   2070  O OE2 . GLU B  1 60  ? 174.425 172.722 144.142 1.00 124.22 ? 62  GLU B OE2 1 
ATOM   2071  N N   . LYS B  1 61  ? 173.574 169.984 143.298 1.00 105.25 ? 63  LYS B N   1 
ATOM   2072  C CA  . LYS B  1 61  ? 174.176 168.726 142.876 1.00 97.54  ? 63  LYS B CA  1 
ATOM   2073  C C   . LYS B  1 61  ? 173.569 167.549 143.628 1.00 100.66 ? 63  LYS B C   1 
ATOM   2074  O O   . LYS B  1 61  ? 173.451 167.576 144.856 1.00 104.98 ? 63  LYS B O   1 
ATOM   2075  C CB  . LYS B  1 61  ? 175.686 168.774 143.103 1.00 99.39  ? 63  LYS B CB  1 
ATOM   2076  C CG  . LYS B  1 61  ? 176.450 167.627 142.472 1.00 108.97 ? 63  LYS B CG  1 
ATOM   2077  C CD  . LYS B  1 61  ? 177.801 167.439 143.139 1.00 113.65 ? 63  LYS B CD  1 
ATOM   2078  C CE  . LYS B  1 61  ? 178.930 167.857 142.217 1.00 115.59 ? 63  LYS B CE  1 
ATOM   2079  N NZ  . LYS B  1 61  ? 179.965 166.795 142.108 1.00 116.57 ? 63  LYS B NZ  1 
ATOM   2080  N N   . GLU B  1 62  ? 173.193 166.511 142.879 1.00 97.25  ? 64  GLU B N   1 
ATOM   2081  C CA  . GLU B  1 62  ? 172.627 165.284 143.441 1.00 95.23  ? 64  GLU B CA  1 
ATOM   2082  C C   . GLU B  1 62  ? 171.442 165.579 144.356 1.00 97.82  ? 64  GLU B C   1 
ATOM   2083  O O   . GLU B  1 62  ? 171.300 164.999 145.434 1.00 102.02 ? 64  GLU B O   1 
ATOM   2084  C CB  . GLU B  1 62  ? 173.692 164.471 144.176 1.00 100.87 ? 64  GLU B CB  1 
ATOM   2085  C CG  . GLU B  1 62  ? 174.437 163.490 143.289 1.00 110.54 ? 64  GLU B CG  1 
ATOM   2086  C CD  . GLU B  1 62  ? 175.918 163.435 143.596 1.00 123.15 ? 64  GLU B CD  1 
ATOM   2087  O OE1 . GLU B  1 62  ? 176.560 164.505 143.620 1.00 123.03 ? 64  GLU B OE1 1 
ATOM   2088  O OE2 . GLU B  1 62  ? 176.442 162.322 143.811 1.00 128.44 ? 64  GLU B OE2 1 
ATOM   2089  N N   . SER B  1 63  ? 170.579 166.490 143.920 1.00 96.42  ? 65  SER B N   1 
ATOM   2090  C CA  . SER B  1 63  ? 169.372 166.841 144.651 1.00 92.23  ? 65  SER B CA  1 
ATOM   2091  C C   . SER B  1 63  ? 168.159 166.285 143.919 1.00 94.40  ? 65  SER B C   1 
ATOM   2092  O O   . SER B  1 63  ? 168.111 166.290 142.686 1.00 97.92  ? 65  SER B O   1 
ATOM   2093  C CB  . SER B  1 63  ? 169.241 168.357 144.808 1.00 91.30  ? 65  SER B CB  1 
ATOM   2094  O OG  . SER B  1 63  ? 169.431 169.012 143.569 1.00 100.56 ? 65  SER B OG  1 
ATOM   2095  N N   . SER B  1 64  ? 167.184 165.804 144.683 1.00 92.33  ? 66  SER B N   1 
ATOM   2096  C CA  . SER B  1 64  ? 166.000 165.164 144.131 1.00 86.28  ? 66  SER B CA  1 
ATOM   2097  C C   . SER B  1 64  ? 164.747 165.856 144.644 1.00 88.13  ? 66  SER B C   1 
ATOM   2098  O O   . SER B  1 64  ? 164.651 166.191 145.828 1.00 93.32  ? 66  SER B O   1 
ATOM   2099  C CB  . SER B  1 64  ? 165.959 163.678 144.495 1.00 90.32  ? 66  SER B CB  1 
ATOM   2100  O OG  . SER B  1 64  ? 166.784 162.920 143.629 1.00 103.29 ? 66  SER B OG  1 
ATOM   2101  N N   . ALA B  1 65  ? 163.789 166.067 143.744 1.00 83.85  ? 67  ALA B N   1 
ATOM   2102  C CA  . ALA B  1 65  ? 162.503 166.668 144.092 1.00 82.82  ? 67  ALA B CA  1 
ATOM   2103  C C   . ALA B  1 65  ? 161.424 165.851 143.390 1.00 88.91  ? 67  ALA B C   1 
ATOM   2104  O O   . ALA B  1 65  ? 161.205 166.008 142.186 1.00 95.38  ? 67  ALA B O   1 
ATOM   2105  C CB  . ALA B  1 65  ? 162.445 168.136 143.688 1.00 84.11  ? 67  ALA B CB  1 
ATOM   2106  N N   . PHE B  1 66  ? 160.757 164.983 144.144 1.00 84.74  ? 68  PHE B N   1 
ATOM   2107  C CA  . PHE B  1 66  ? 159.746 164.083 143.607 1.00 76.87  ? 68  PHE B CA  1 
ATOM   2108  C C   . PHE B  1 66  ? 158.399 164.420 144.228 1.00 80.64  ? 68  PHE B C   1 
ATOM   2109  O O   . PHE B  1 66  ? 158.267 164.445 145.455 1.00 83.85  ? 68  PHE B O   1 
ATOM   2110  C CB  . PHE B  1 66  ? 160.104 162.621 143.888 1.00 77.60  ? 68  PHE B CB  1 
ATOM   2111  C CG  . PHE B  1 66  ? 161.166 162.067 142.981 1.00 78.34  ? 68  PHE B CG  1 
ATOM   2112  C CD1 . PHE B  1 66  ? 162.423 162.643 142.925 1.00 83.28  ? 68  PHE B CD1 1 
ATOM   2113  C CD2 . PHE B  1 66  ? 160.909 160.963 142.190 1.00 80.17  ? 68  PHE B CD2 1 
ATOM   2114  C CE1 . PHE B  1 66  ? 163.398 162.133 142.094 1.00 85.23  ? 68  PHE B CE1 1 
ATOM   2115  C CE2 . PHE B  1 66  ? 161.882 160.450 141.357 1.00 87.98  ? 68  PHE B CE2 1 
ATOM   2116  C CZ  . PHE B  1 66  ? 163.127 161.036 141.310 1.00 86.81  ? 68  PHE B CZ  1 
ATOM   2117  N N   . GLY B  1 67  ? 157.403 164.669 143.383 1.00 79.96  ? 69  GLY B N   1 
ATOM   2118  C CA  . GLY B  1 67  ? 156.079 164.994 143.872 1.00 78.15  ? 69  GLY B CA  1 
ATOM   2119  C C   . GLY B  1 67  ? 155.453 166.180 143.170 1.00 80.92  ? 69  GLY B C   1 
ATOM   2120  O O   . GLY B  1 67  ? 155.492 166.270 141.941 1.00 81.67  ? 69  GLY B O   1 
ATOM   2121  N N   . THR B  1 68  ? 154.871 167.098 143.939 1.00 86.20  ? 70  THR B N   1 
ATOM   2122  C CA  . THR B  1 68  ? 154.191 168.263 143.386 1.00 86.78  ? 70  THR B CA  1 
ATOM   2123  C C   . THR B  1 68  ? 154.721 169.521 144.058 1.00 86.51  ? 70  THR B C   1 
ATOM   2124  O O   . THR B  1 68  ? 154.558 169.695 145.270 1.00 90.36  ? 70  THR B O   1 
ATOM   2125  C CB  . THR B  1 68  ? 152.676 168.157 143.574 1.00 86.38  ? 70  THR B CB  1 
ATOM   2126  O OG1 . THR B  1 68  ? 152.167 167.094 142.760 1.00 94.24  ? 70  THR B OG1 1 
ATOM   2127  C CG2 . THR B  1 68  ? 152.001 169.458 143.176 1.00 89.15  ? 70  THR B CG2 1 
ATOM   2128  N N   . GLY B  1 69  ? 155.343 170.393 143.272 1.00 84.89  ? 71  GLY B N   1 
ATOM   2129  C CA  . GLY B  1 69  ? 155.779 171.686 143.774 1.00 86.48  ? 71  GLY B CA  1 
ATOM   2130  C C   . GLY B  1 69  ? 156.859 171.631 144.833 1.00 87.47  ? 71  GLY B C   1 
ATOM   2131  O O   . GLY B  1 69  ? 156.851 172.446 145.763 1.00 86.74  ? 71  GLY B O   1 
ATOM   2132  N N   . ASN B  1 70  ? 157.797 170.700 144.708 1.00 84.84  ? 72  ASN B N   1 
ATOM   2133  C CA  . ASN B  1 70  ? 158.880 170.581 145.671 1.00 79.87  ? 72  ASN B CA  1 
ATOM   2134  C C   . ASN B  1 70  ? 160.080 171.410 145.236 1.00 86.12  ? 72  ASN B C   1 
ATOM   2135  O O   . ASN B  1 70  ? 160.257 171.711 144.053 1.00 91.73  ? 72  ASN B O   1 
ATOM   2136  C CB  . ASN B  1 70  ? 159.294 169.120 145.843 1.00 78.94  ? 72  ASN B CB  1 
ATOM   2137  C CG  . ASN B  1 70  ? 158.157 168.249 146.318 1.00 82.73  ? 72  ASN B CG  1 
ATOM   2138  O OD1 . ASN B  1 70  ? 157.003 168.469 145.958 1.00 87.64  ? 72  ASN B OD1 1 
ATOM   2139  N ND2 . ASN B  1 70  ? 158.474 167.256 147.135 1.00 87.30  ? 72  ASN B ND2 1 
ATOM   2140  N N   . ARG B  1 71  ? 160.905 171.782 146.212 1.00 84.00  ? 73  ARG B N   1 
ATOM   2141  C CA  . ARG B  1 71  ? 162.125 172.541 145.965 1.00 82.36  ? 73  ARG B CA  1 
ATOM   2142  C C   . ARG B  1 71  ? 163.264 171.913 146.751 1.00 92.65  ? 73  ARG B C   1 
ATOM   2143  O O   . ARG B  1 71  ? 163.185 171.799 147.978 1.00 97.67  ? 73  ARG B O   1 
ATOM   2144  C CB  . ARG B  1 71  ? 161.950 174.011 146.354 1.00 83.33  ? 73  ARG B CB  1 
ATOM   2145  C CG  . ARG B  1 71  ? 161.591 174.918 145.192 1.00 93.80  ? 73  ARG B CG  1 
ATOM   2146  C CD  . ARG B  1 71  ? 160.176 175.450 145.320 1.00 99.19  ? 73  ARG B CD  1 
ATOM   2147  N NE  . ARG B  1 71  ? 159.671 175.961 144.051 1.00 105.86 ? 73  ARG B NE  1 
ATOM   2148  C CZ  . ARG B  1 71  ? 158.914 175.266 143.213 1.00 107.90 ? 73  ARG B CZ  1 
ATOM   2149  N NH1 . ARG B  1 71  ? 158.553 174.022 143.478 1.00 102.21 ? 73  ARG B NH1 1 
ATOM   2150  N NH2 . ARG B  1 71  ? 158.511 175.833 142.080 1.00 110.63 ? 73  ARG B NH2 1 
ATOM   2151  N N   . ALA B  1 72  ? 164.317 171.512 146.047 1.00 91.44  ? 74  ALA B N   1 
ATOM   2152  C CA  . ALA B  1 72  ? 165.529 170.970 146.656 1.00 89.41  ? 74  ALA B CA  1 
ATOM   2153  C C   . ALA B  1 72  ? 166.677 171.898 146.278 1.00 98.28  ? 74  ALA B C   1 
ATOM   2154  O O   . ALA B  1 72  ? 167.236 171.790 145.182 1.00 103.84 ? 74  ALA B O   1 
ATOM   2155  C CB  . ALA B  1 72  ? 165.786 169.538 146.198 1.00 88.72  ? 74  ALA B CB  1 
ATOM   2156  N N   . THR B  1 73  ? 167.026 172.809 147.185 1.00 99.05  ? 75  THR B N   1 
ATOM   2157  C CA  . THR B  1 73  ? 168.007 173.851 146.915 1.00 100.51 ? 75  THR B CA  1 
ATOM   2158  C C   . THR B  1 73  ? 169.343 173.586 147.600 1.00 102.44 ? 75  THR B C   1 
ATOM   2159  O O   . THR B  1 73  ? 170.209 174.466 147.622 1.00 109.79 ? 75  THR B O   1 
ATOM   2160  C CB  . THR B  1 73  ? 167.459 175.213 147.339 1.00 104.86 ? 75  THR B CB  1 
ATOM   2161  O OG1 . THR B  1 73  ? 166.937 175.124 148.670 1.00 103.77 ? 75  THR B OG1 1 
ATOM   2162  C CG2 . THR B  1 73  ? 166.349 175.650 146.401 1.00 102.02 ? 75  THR B CG2 1 
ATOM   2163  N N   . GLY B  1 74  ? 169.527 172.398 148.158 1.00 98.47  ? 76  GLY B N   1 
ATOM   2164  C CA  . GLY B  1 74  ? 170.778 172.046 148.795 1.00 96.86  ? 76  GLY B CA  1 
ATOM   2165  C C   . GLY B  1 74  ? 171.348 170.777 148.199 1.00 101.67 ? 76  GLY B C   1 
ATOM   2166  O O   . GLY B  1 74  ? 170.626 169.943 147.654 1.00 106.03 ? 76  GLY B O   1 
ATOM   2167  N N   . GLU B  1 75  ? 172.669 170.650 148.296 1.00 100.85 ? 77  GLU B N   1 
ATOM   2168  C CA  . GLU B  1 75  ? 173.336 169.455 147.803 1.00 100.17 ? 77  GLU B CA  1 
ATOM   2169  C C   . GLU B  1 75  ? 172.826 168.230 148.547 1.00 97.08  ? 77  GLU B C   1 
ATOM   2170  O O   . GLU B  1 75  ? 172.464 168.302 149.722 1.00 102.77 ? 77  GLU B O   1 
ATOM   2171  C CB  . GLU B  1 75  ? 174.849 169.573 147.976 1.00 103.54 ? 77  GLU B CB  1 
ATOM   2172  C CG  . GLU B  1 75  ? 175.403 170.960 147.724 1.00 118.43 ? 77  GLU B CG  1 
ATOM   2173  C CD  . GLU B  1 75  ? 176.779 170.924 147.091 1.00 136.56 ? 77  GLU B CD  1 
ATOM   2174  O OE1 . GLU B  1 75  ? 177.305 169.812 146.877 1.00 131.20 ? 77  GLU B OE1 1 
ATOM   2175  O OE2 . GLU B  1 75  ? 177.335 172.006 146.810 1.00 145.05 ? 77  GLU B OE2 1 
ATOM   2176  N N   . PHE B  1 76  ? 172.758 167.105 147.833 1.00 91.05  ? 78  PHE B N   1 
ATOM   2177  C CA  . PHE B  1 76  ? 172.382 165.814 148.416 1.00 90.87  ? 78  PHE B CA  1 
ATOM   2178  C C   . PHE B  1 76  ? 171.078 165.898 149.206 1.00 95.25  ? 78  PHE B C   1 
ATOM   2179  O O   . PHE B  1 76  ? 170.849 165.122 150.135 1.00 102.42 ? 78  PHE B O   1 
ATOM   2180  C CB  . PHE B  1 76  ? 173.502 165.264 149.301 1.00 94.53  ? 78  PHE B CB  1 
ATOM   2181  C CG  . PHE B  1 76  ? 174.877 165.472 148.740 1.00 97.72  ? 78  PHE B CG  1 
ATOM   2182  C CD1 . PHE B  1 76  ? 175.202 165.020 147.474 1.00 102.25 ? 78  PHE B CD1 1 
ATOM   2183  C CD2 . PHE B  1 76  ? 175.847 166.120 149.483 1.00 98.80  ? 78  PHE B CD2 1 
ATOM   2184  C CE1 . PHE B  1 76  ? 176.468 165.213 146.960 1.00 104.37 ? 78  PHE B CE1 1 
ATOM   2185  C CE2 . PHE B  1 76  ? 177.113 166.315 148.974 1.00 101.43 ? 78  PHE B CE2 1 
ATOM   2186  C CZ  . PHE B  1 76  ? 177.424 165.862 147.711 1.00 101.46 ? 78  PHE B CZ  1 
ATOM   2187  N N   . SER B  1 77  ? 170.216 166.840 148.847 1.00 93.93  ? 79  SER B N   1 
ATOM   2188  C CA  . SER B  1 77  ? 168.963 167.053 149.553 1.00 88.77  ? 79  SER B CA  1 
ATOM   2189  C C   . SER B  1 77  ? 167.797 166.531 148.727 1.00 87.69  ? 79  SER B C   1 
ATOM   2190  O O   . SER B  1 77  ? 167.803 166.578 147.495 1.00 94.35  ? 79  SER B O   1 
ATOM   2191  C CB  . SER B  1 77  ? 168.762 168.536 149.872 1.00 89.99  ? 79  SER B CB  1 
ATOM   2192  O OG  . SER B  1 77  ? 168.629 169.297 148.686 1.00 99.70  ? 79  SER B OG  1 
ATOM   2193  N N   . SER B  1 78  ? 166.784 166.030 149.428 1.00 82.78  ? 80  SER B N   1 
ATOM   2194  C CA  . SER B  1 78  ? 165.635 165.415 148.784 1.00 82.48  ? 80  SER B CA  1 
ATOM   2195  C C   . SER B  1 78  ? 164.357 165.953 149.402 1.00 85.24  ? 80  SER B C   1 
ATOM   2196  O O   . SER B  1 78  ? 164.233 166.014 150.628 1.00 88.87  ? 80  SER B O   1 
ATOM   2197  C CB  . SER B  1 78  ? 165.683 163.890 148.914 1.00 85.93  ? 80  SER B CB  1 
ATOM   2198  O OG  . SER B  1 78  ? 165.680 163.500 150.275 1.00 94.79  ? 80  SER B OG  1 
ATOM   2199  N N   . ALA B  1 79  ? 163.413 166.340 148.549 1.00 81.13  ? 81  ALA B N   1 
ATOM   2200  C CA  . ALA B  1 79  ? 162.091 166.790 148.968 1.00 78.28  ? 81  ALA B CA  1 
ATOM   2201  C C   . ALA B  1 79  ? 161.063 165.924 148.254 1.00 82.62  ? 81  ALA B C   1 
ATOM   2202  O O   . ALA B  1 79  ? 160.881 166.046 147.039 1.00 87.92  ? 81  ALA B O   1 
ATOM   2203  C CB  . ALA B  1 79  ? 161.885 168.269 148.650 1.00 79.08  ? 81  ALA B CB  1 
ATOM   2204  N N   . PHE B  1 80  ? 160.397 165.053 149.005 1.00 79.16  ? 82  PHE B N   1 
ATOM   2205  C CA  . PHE B  1 80  ? 159.443 164.100 148.452 1.00 73.18  ? 82  PHE B CA  1 
ATOM   2206  C C   . PHE B  1 80  ? 158.071 164.384 149.040 1.00 76.52  ? 82  PHE B C   1 
ATOM   2207  O O   . PHE B  1 80  ? 157.905 164.375 150.264 1.00 81.38  ? 82  PHE B O   1 
ATOM   2208  C CB  . PHE B  1 80  ? 159.867 162.661 148.753 1.00 76.36  ? 82  PHE B CB  1 
ATOM   2209  C CG  . PHE B  1 80  ? 160.936 162.135 147.838 1.00 74.39  ? 82  PHE B CG  1 
ATOM   2210  C CD1 . PHE B  1 80  ? 162.163 162.766 147.746 1.00 77.45  ? 82  PHE B CD1 1 
ATOM   2211  C CD2 . PHE B  1 80  ? 160.715 161.004 147.075 1.00 77.81  ? 82  PHE B CD2 1 
ATOM   2212  C CE1 . PHE B  1 80  ? 163.146 162.282 146.909 1.00 83.01  ? 82  PHE B CE1 1 
ATOM   2213  C CE2 . PHE B  1 80  ? 161.695 160.515 146.236 1.00 83.34  ? 82  PHE B CE2 1 
ATOM   2214  C CZ  . PHE B  1 80  ? 162.911 161.156 146.153 1.00 86.16  ? 82  PHE B CZ  1 
ATOM   2215  N N   . GLY B  1 81  ? 157.092 164.629 148.176 1.00 73.77  ? 83  GLY B N   1 
ATOM   2216  C CA  . GLY B  1 81  ? 155.743 164.872 148.641 1.00 75.05  ? 83  GLY B CA  1 
ATOM   2217  C C   . GLY B  1 81  ? 155.060 166.047 147.976 1.00 78.25  ? 83  GLY B C   1 
ATOM   2218  O O   . GLY B  1 81  ? 155.004 166.129 146.746 1.00 80.42  ? 83  GLY B O   1 
ATOM   2219  N N   . PHE B  1 82  ? 154.536 166.967 148.783 1.00 81.74  ? 84  PHE B N   1 
ATOM   2220  C CA  . PHE B  1 82  ? 153.758 168.097 148.291 1.00 81.87  ? 84  PHE B CA  1 
ATOM   2221  C C   . PHE B  1 82  ? 154.301 169.383 148.892 1.00 83.33  ? 84  PHE B C   1 
ATOM   2222  O O   . PHE B  1 82  ? 154.252 169.567 150.112 1.00 86.51  ? 84  PHE B O   1 
ATOM   2223  C CB  . PHE B  1 82  ? 152.276 167.924 148.635 1.00 77.13  ? 84  PHE B CB  1 
ATOM   2224  C CG  . PHE B  1 82  ? 151.432 169.119 148.306 1.00 83.13  ? 84  PHE B CG  1 
ATOM   2225  C CD1 . PHE B  1 82  ? 151.063 169.385 147.001 1.00 87.82  ? 84  PHE B CD1 1 
ATOM   2226  C CD2 . PHE B  1 82  ? 151.000 169.972 149.305 1.00 83.11  ? 84  PHE B CD2 1 
ATOM   2227  C CE1 . PHE B  1 82  ? 150.283 170.482 146.697 1.00 86.45  ? 84  PHE B CE1 1 
ATOM   2228  C CE2 . PHE B  1 82  ? 150.221 171.071 149.008 1.00 85.62  ? 84  PHE B CE2 1 
ATOM   2229  C CZ  . PHE B  1 82  ? 149.863 171.326 147.702 1.00 87.43  ? 84  PHE B CZ  1 
ATOM   2230  N N   . HIS B  1 83  ? 154.810 170.267 148.034 1.00 81.47  ? 85  HIS B N   1 
ATOM   2231  C CA  . HIS B  1 83  ? 155.271 171.598 148.432 1.00 82.27  ? 85  HIS B CA  1 
ATOM   2232  C C   . HIS B  1 83  ? 156.311 171.525 149.547 1.00 85.37  ? 85  HIS B C   1 
ATOM   2233  O O   . HIS B  1 83  ? 156.222 172.218 150.562 1.00 89.58  ? 85  HIS B O   1 
ATOM   2234  C CB  . HIS B  1 83  ? 154.093 172.481 148.843 1.00 84.61  ? 85  HIS B CB  1 
ATOM   2235  C CG  . HIS B  1 83  ? 153.335 173.052 147.687 1.00 91.48  ? 85  HIS B CG  1 
ATOM   2236  N ND1 . HIS B  1 83  ? 152.726 174.287 147.735 1.00 95.07  ? 85  HIS B ND1 1 
ATOM   2237  C CD2 . HIS B  1 83  ? 153.088 172.558 146.452 1.00 94.54  ? 85  HIS B CD2 1 
ATOM   2238  C CE1 . HIS B  1 83  ? 152.136 174.529 146.578 1.00 98.25  ? 85  HIS B CE1 1 
ATOM   2239  N NE2 . HIS B  1 83  ? 152.340 173.495 145.782 1.00 94.57  ? 85  HIS B NE2 1 
ATOM   2240  N N   . ASN B  1 84  ? 157.316 170.682 149.347 1.00 82.51  ? 86  ASN B N   1 
ATOM   2241  C CA  . ASN B  1 84  ? 158.370 170.480 150.329 1.00 80.07  ? 86  ASN B CA  1 
ATOM   2242  C C   . ASN B  1 84  ? 159.609 171.270 149.934 1.00 82.73  ? 86  ASN B C   1 
ATOM   2243  O O   . ASN B  1 84  ? 159.869 171.481 148.746 1.00 87.87  ? 86  ASN B O   1 
ATOM   2244  C CB  . ASN B  1 84  ? 158.710 168.996 150.456 1.00 77.60  ? 86  ASN B CB  1 
ATOM   2245  C CG  . ASN B  1 84  ? 157.691 168.239 151.275 1.00 79.99  ? 86  ASN B CG  1 
ATOM   2246  O OD1 . ASN B  1 84  ? 156.698 168.806 151.727 1.00 83.96  ? 86  ASN B OD1 1 
ATOM   2247  N ND2 . ASN B  1 84  ? 157.923 166.948 151.462 1.00 88.62  ? 86  ASN B ND2 1 
ATOM   2248  N N   . ILE B  1 85  ? 160.370 171.709 150.934 1.00 82.26  ? 87  ILE B N   1 
ATOM   2249  C CA  . ILE B  1 85  ? 161.570 172.506 150.716 1.00 82.41  ? 87  ILE B CA  1 
ATOM   2250  C C   . ILE B  1 85  ? 162.714 171.907 151.522 1.00 90.89  ? 87  ILE B C   1 
ATOM   2251  O O   . ILE B  1 85  ? 162.597 171.736 152.740 1.00 96.23  ? 87  ILE B O   1 
ATOM   2252  C CB  . ILE B  1 85  ? 161.354 173.981 151.100 1.00 80.10  ? 87  ILE B CB  1 
ATOM   2253  C CG1 . ILE B  1 85  ? 160.488 174.682 150.053 1.00 88.77  ? 87  ILE B CG1 1 
ATOM   2254  C CG2 . ILE B  1 85  ? 162.685 174.695 151.244 1.00 79.47  ? 87  ILE B CG2 1 
ATOM   2255  C CD1 . ILE B  1 85  ? 159.448 175.607 150.642 1.00 91.81  ? 87  ILE B CD1 1 
ATOM   2256  N N   . ALA B  1 86  ? 163.814 171.591 150.842 1.00 88.04  ? 88  ALA B N   1 
ATOM   2257  C CA  . ALA B  1 86  ? 165.052 171.156 151.474 1.00 86.34  ? 88  ALA B CA  1 
ATOM   2258  C C   . ALA B  1 86  ? 166.164 172.083 151.014 1.00 93.27  ? 88  ALA B C   1 
ATOM   2259  O O   . ALA B  1 86  ? 166.303 172.337 149.813 1.00 99.00  ? 88  ALA B O   1 
ATOM   2260  C CB  . ALA B  1 86  ? 165.380 169.704 151.119 1.00 84.91  ? 88  ALA B CB  1 
ATOM   2261  N N   . SER B  1 87  ? 166.958 172.589 151.960 1.00 91.23  ? 89  SER B N   1 
ATOM   2262  C CA  . SER B  1 87  ? 167.853 173.699 151.667 1.00 90.46  ? 89  SER B CA  1 
ATOM   2263  C C   . SER B  1 87  ? 169.308 173.503 152.068 1.00 95.81  ? 89  SER B C   1 
ATOM   2264  O O   . SER B  1 87  ? 170.108 174.412 151.825 1.00 101.36 ? 89  SER B O   1 
ATOM   2265  C CB  . SER B  1 87  ? 167.341 174.981 152.341 1.00 92.45  ? 89  SER B CB  1 
ATOM   2266  O OG  . SER B  1 87  ? 166.058 175.331 151.857 1.00 102.10 ? 89  SER B OG  1 
ATOM   2267  N N   . LYS B  1 88  ? 169.687 172.378 152.664 1.00 96.06  ? 90  LYS B N   1 
ATOM   2268  C CA  . LYS B  1 88  ? 171.044 172.244 153.179 1.00 93.67  ? 90  LYS B CA  1 
ATOM   2269  C C   . LYS B  1 88  ? 171.705 170.964 152.658 1.00 95.40  ? 90  LYS B C   1 
ATOM   2270  O O   . LYS B  1 88  ? 171.162 170.258 151.805 1.00 98.58  ? 90  LYS B O   1 
ATOM   2271  C CB  . LYS B  1 88  ? 171.034 172.310 154.706 1.00 89.18  ? 90  LYS B CB  1 
ATOM   2272  C CG  . LYS B  1 88  ? 170.634 173.677 155.236 1.00 90.31  ? 90  LYS B CG  1 
ATOM   2273  C CD  . LYS B  1 88  ? 171.752 174.690 155.056 1.00 96.43  ? 90  LYS B CD  1 
ATOM   2274  C CE  . LYS B  1 88  ? 171.429 175.998 155.758 1.00 101.92 ? 90  LYS B CE  1 
ATOM   2275  N NZ  . LYS B  1 88  ? 169.969 176.285 155.745 1.00 101.08 ? 90  LYS B NZ  1 
ATOM   2276  N N   . ILE B  1 89  ? 172.894 170.676 153.195 1.00 92.23  ? 91  ILE B N   1 
ATOM   2277  C CA  . ILE B  1 89  ? 173.799 169.705 152.583 1.00 90.18  ? 91  ILE B CA  1 
ATOM   2278  C C   . ILE B  1 89  ? 173.258 168.282 152.683 1.00 92.63  ? 91  ILE B C   1 
ATOM   2279  O O   . ILE B  1 89  ? 173.583 167.430 151.849 1.00 100.94 ? 91  ILE B O   1 
ATOM   2280  C CB  . ILE B  1 89  ? 175.199 169.830 153.212 1.00 90.22  ? 91  ILE B CB  1 
ATOM   2281  C CG1 . ILE B  1 89  ? 176.191 168.880 152.540 1.00 95.15  ? 91  ILE B CG1 1 
ATOM   2282  C CG2 . ILE B  1 89  ? 175.139 169.551 154.693 1.00 91.10  ? 91  ILE B CG2 1 
ATOM   2283  C CD1 . ILE B  1 89  ? 176.671 169.359 151.192 1.00 100.02 ? 91  ILE B CD1 1 
ATOM   2284  N N   . HIS B  1 90  ? 172.472 167.976 153.711 1.00 84.60  ? 92  HIS B N   1 
ATOM   2285  C CA  . HIS B  1 90  ? 171.756 166.699 153.766 1.00 82.14  ? 92  HIS B CA  1 
ATOM   2286  C C   . HIS B  1 90  ? 170.407 166.978 154.421 1.00 89.36  ? 92  HIS B C   1 
ATOM   2287  O O   . HIS B  1 90  ? 170.273 166.906 155.643 1.00 98.88  ? 92  HIS B O   1 
ATOM   2288  C CB  . HIS B  1 90  ? 172.552 165.646 154.525 1.00 88.76  ? 92  HIS B CB  1 
ATOM   2289  C CG  . HIS B  1 90  ? 173.630 164.999 153.712 1.00 89.20  ? 92  HIS B CG  1 
ATOM   2290  N ND1 . HIS B  1 90  ? 173.375 164.019 152.778 1.00 89.34  ? 92  HIS B ND1 1 
ATOM   2291  C CD2 . HIS B  1 90  ? 174.970 165.194 153.695 1.00 89.90  ? 92  HIS B CD2 1 
ATOM   2292  C CE1 . HIS B  1 90  ? 174.510 163.637 152.221 1.00 89.28  ? 92  HIS B CE1 1 
ATOM   2293  N NE2 . HIS B  1 90  ? 175.493 164.336 152.759 1.00 85.44  ? 92  HIS B NE2 1 
ATOM   2294  N N   . SER B  1 91  ? 169.404 167.276 153.604 1.00 83.73  ? 93  SER B N   1 
ATOM   2295  C CA  . SER B  1 91  ? 168.097 167.654 154.114 1.00 82.70  ? 93  SER B CA  1 
ATOM   2296  C C   . SER B  1 91  ? 167.028 166.762 153.507 1.00 88.43  ? 93  SER B C   1 
ATOM   2297  O O   . SER B  1 91  ? 167.054 166.472 152.308 1.00 95.47  ? 93  SER B O   1 
ATOM   2298  C CB  . SER B  1 91  ? 167.792 169.122 153.815 1.00 87.30  ? 93  SER B CB  1 
ATOM   2299  O OG  . SER B  1 91  ? 168.966 169.906 153.904 1.00 88.92  ? 93  SER B OG  1 
ATOM   2300  N N   . SER B  1 92  ? 166.089 166.333 154.344 1.00 84.22  ? 94  SER B N   1 
ATOM   2301  C CA  . SER B  1 92  ? 164.985 165.486 153.917 1.00 82.23  ? 94  SER B CA  1 
ATOM   2302  C C   . SER B  1 92  ? 163.685 166.125 154.373 1.00 86.32  ? 94  SER B C   1 
ATOM   2303  O O   . SER B  1 92  ? 163.480 166.330 155.573 1.00 91.93  ? 94  SER B O   1 
ATOM   2304  C CB  . SER B  1 92  ? 165.122 164.072 154.485 1.00 88.19  ? 94  SER B CB  1 
ATOM   2305  O OG  . SER B  1 92  ? 166.298 163.445 154.005 1.00 93.42  ? 94  SER B OG  1 
ATOM   2306  N N   . ALA B  1 93  ? 162.818 166.442 153.419 1.00 78.49  ? 95  ALA B N   1 
ATOM   2307  C CA  . ALA B  1 93  ? 161.494 166.991 153.695 1.00 73.37  ? 95  ALA B CA  1 
ATOM   2308  C C   . ALA B  1 93  ? 160.485 166.068 153.025 1.00 79.43  ? 95  ALA B C   1 
ATOM   2309  O O   . ALA B  1 93  ? 160.187 166.220 151.837 1.00 88.30  ? 95  ALA B O   1 
ATOM   2310  C CB  . ALA B  1 93  ? 161.372 168.424 153.189 1.00 76.45  ? 95  ALA B CB  1 
ATOM   2311  N N   . PHE B  1 94  ? 159.962 165.112 153.785 1.00 76.83  ? 96  PHE B N   1 
ATOM   2312  C CA  . PHE B  1 94  ? 159.048 164.104 153.269 1.00 74.23  ? 96  PHE B CA  1 
ATOM   2313  C C   . PHE B  1 94  ? 157.674 164.335 153.881 1.00 75.37  ? 96  PHE B C   1 
ATOM   2314  O O   . PHE B  1 94  ? 157.535 164.359 155.108 1.00 80.12  ? 96  PHE B O   1 
ATOM   2315  C CB  . PHE B  1 94  ? 159.551 162.695 153.584 1.00 76.21  ? 96  PHE B CB  1 
ATOM   2316  C CG  . PHE B  1 94  ? 160.708 162.253 152.730 1.00 75.02  ? 96  PHE B CG  1 
ATOM   2317  C CD1 . PHE B  1 94  ? 161.910 162.939 152.754 1.00 77.48  ? 96  PHE B CD1 1 
ATOM   2318  C CD2 . PHE B  1 94  ? 160.596 161.146 151.909 1.00 79.05  ? 96  PHE B CD2 1 
ATOM   2319  C CE1 . PHE B  1 94  ? 162.972 162.535 151.973 1.00 80.77  ? 96  PHE B CE1 1 
ATOM   2320  C CE2 . PHE B  1 94  ? 161.657 160.737 151.126 1.00 84.52  ? 96  PHE B CE2 1 
ATOM   2321  C CZ  . PHE B  1 94  ? 162.846 161.433 151.158 1.00 84.48  ? 96  PHE B CZ  1 
ATOM   2322  N N   . GLY B  1 95  ? 156.666 164.497 153.030 1.00 71.72  ? 97  GLY B N   1 
ATOM   2323  C CA  . GLY B  1 95  ? 155.325 164.770 153.504 1.00 75.12  ? 97  GLY B CA  1 
ATOM   2324  C C   . GLY B  1 95  ? 154.671 165.932 152.788 1.00 79.22  ? 97  GLY B C   1 
ATOM   2325  O O   . GLY B  1 95  ? 154.758 166.039 151.562 1.00 82.07  ? 97  GLY B O   1 
ATOM   2326  N N   . SER B  1 96  ? 154.016 166.812 153.540 1.00 78.99  ? 98  SER B N   1 
ATOM   2327  C CA  . SER B  1 96  ? 153.297 167.949 152.978 1.00 78.75  ? 98  SER B CA  1 
ATOM   2328  C C   . SER B  1 96  ? 153.789 169.233 153.628 1.00 80.58  ? 98  SER B C   1 
ATOM   2329  O O   . SER B  1 96  ? 153.735 169.371 154.855 1.00 82.11  ? 98  SER B O   1 
ATOM   2330  C CB  . SER B  1 96  ? 151.789 167.791 153.177 1.00 80.93  ? 98  SER B CB  1 
ATOM   2331  O OG  . SER B  1 96  ? 151.071 168.664 152.325 1.00 88.79  ? 98  SER B OG  1 
ATOM   2332  N N   . ASN B  1 97  ? 154.263 170.167 152.802 1.00 80.12  ? 99  ASN B N   1 
ATOM   2333  C CA  . ASN B  1 97  ? 154.651 171.510 153.238 1.00 77.29  ? 99  ASN B CA  1 
ATOM   2334  C C   . ASN B  1 97  ? 155.717 171.490 154.328 1.00 79.11  ? 99  ASN B C   1 
ATOM   2335  O O   . ASN B  1 97  ? 155.728 172.348 155.212 1.00 86.90  ? 99  ASN B O   1 
ATOM   2336  C CB  . ASN B  1 97  ? 153.435 172.314 153.705 1.00 82.44  ? 99  ASN B CB  1 
ATOM   2337  C CG  . ASN B  1 97  ? 152.307 172.295 152.701 1.00 90.50  ? 99  ASN B CG  1 
ATOM   2338  O OD1 . ASN B  1 97  ? 151.665 171.268 152.490 1.00 94.31  ? 99  ASN B OD1 1 
ATOM   2339  N ND2 . ASN B  1 97  ? 152.062 173.434 152.067 1.00 88.31  ? 99  ASN B ND2 1 
ATOM   2340  N N   . ASN B  1 98  ? 156.632 170.529 154.273 1.00 77.26  ? 100 ASN B N   1 
ATOM   2341  C CA  . ASN B  1 98  ? 157.742 170.486 155.211 1.00 73.90  ? 100 ASN B CA  1 
ATOM   2342  C C   . ASN B  1 98  ? 158.901 171.318 154.683 1.00 81.66  ? 100 ASN B C   1 
ATOM   2343  O O   . ASN B  1 98  ? 159.176 171.332 153.481 1.00 90.96  ? 100 ASN B O   1 
ATOM   2344  C CB  . ASN B  1 98  ? 158.200 169.048 155.453 1.00 74.01  ? 100 ASN B CB  1 
ATOM   2345  C CG  . ASN B  1 98  ? 157.106 168.182 156.028 1.00 79.18  ? 100 ASN B CG  1 
ATOM   2346  O OD1 . ASN B  1 98  ? 156.888 168.160 157.238 1.00 79.15  ? 100 ASN B OD1 1 
ATOM   2347  N ND2 . ASN B  1 98  ? 156.410 167.458 155.164 1.00 83.39  ? 100 ASN B ND2 1 
ATOM   2348  N N   . ALA B  1 99  ? 159.575 172.017 155.592 1.00 79.26  ? 101 ALA B N   1 
ATOM   2349  C CA  . ALA B  1 99  ? 160.730 172.841 155.255 1.00 81.17  ? 101 ALA B CA  1 
ATOM   2350  C C   . ALA B  1 99  ? 161.884 172.427 156.154 1.00 88.90  ? 101 ALA B C   1 
ATOM   2351  O O   . ALA B  1 99  ? 161.887 172.740 157.348 1.00 91.55  ? 101 ALA B O   1 
ATOM   2352  C CB  . ALA B  1 99  ? 160.417 174.328 155.415 1.00 82.09  ? 101 ALA B CB  1 
ATOM   2353  N N   . ALA B  1 100 ? 162.859 171.729 155.586 1.00 91.02  ? 102 ALA B N   1 
ATOM   2354  C CA  . ALA B  1 100 ? 164.029 171.260 156.322 1.00 89.77  ? 102 ALA B CA  1 
ATOM   2355  C C   . ALA B  1 100 ? 165.207 172.141 155.919 1.00 96.64  ? 102 ALA B C   1 
ATOM   2356  O O   . ALA B  1 100 ? 165.899 171.868 154.938 1.00 99.42  ? 102 ALA B O   1 
ATOM   2357  C CB  . ALA B  1 100 ? 164.304 169.789 156.040 1.00 86.36  ? 102 ALA B CB  1 
ATOM   2358  N N   . ASP B  1 101 ? 165.431 173.203 156.687 1.00 99.38  ? 103 ASP B N   1 
ATOM   2359  C CA  . ASP B  1 101 ? 166.528 174.133 156.443 1.00 98.48  ? 103 ASP B CA  1 
ATOM   2360  C C   . ASP B  1 101 ? 167.524 173.973 157.586 1.00 100.62 ? 103 ASP B C   1 
ATOM   2361  O O   . ASP B  1 101 ? 167.525 174.731 158.555 1.00 98.83  ? 103 ASP B O   1 
ATOM   2362  C CB  . ASP B  1 101 ? 166.010 175.564 156.337 1.00 106.46 ? 103 ASP B CB  1 
ATOM   2363  C CG  . ASP B  1 101 ? 164.937 175.716 155.277 1.00 116.21 ? 103 ASP B CG  1 
ATOM   2364  O OD1 . ASP B  1 101 ? 163.866 175.092 155.423 1.00 115.02 ? 103 ASP B OD1 1 
ATOM   2365  O OD2 . ASP B  1 101 ? 165.164 176.459 154.300 1.00 126.73 ? 103 ASP B OD2 1 
ATOM   2366  N N   . GLY B  1 102 ? 168.397 172.982 157.450 1.00 98.89  ? 104 GLY B N   1 
ATOM   2367  C CA  . GLY B  1 102 ? 169.376 172.675 158.469 1.00 90.10  ? 104 GLY B CA  1 
ATOM   2368  C C   . GLY B  1 102 ? 170.263 171.528 158.039 1.00 94.30  ? 104 GLY B C   1 
ATOM   2369  O O   . GLY B  1 102 ? 169.800 170.602 157.367 1.00 99.90  ? 104 GLY B O   1 
ATOM   2370  N N   . VAL B  1 103 ? 171.541 171.580 158.407 1.00 96.17  ? 105 VAL B N   1 
ATOM   2371  C CA  . VAL B  1 103 ? 172.476 170.541 157.996 1.00 92.08  ? 105 VAL B CA  1 
ATOM   2372  C C   . VAL B  1 103 ? 172.102 169.230 158.671 1.00 93.71  ? 105 VAL B C   1 
ATOM   2373  O O   . VAL B  1 103 ? 171.914 169.175 159.893 1.00 98.82  ? 105 VAL B O   1 
ATOM   2374  C CB  . VAL B  1 103 ? 173.916 170.953 158.330 1.00 86.46  ? 105 VAL B CB  1 
ATOM   2375  C CG1 . VAL B  1 103 ? 174.851 169.771 158.172 1.00 87.10  ? 105 VAL B CG1 1 
ATOM   2376  C CG2 . VAL B  1 103 ? 174.352 172.108 157.447 1.00 83.35  ? 105 VAL B CG2 1 
ATOM   2377  N N   . ASN B  1 104 ? 171.990 168.167 157.872 1.00 85.53  ? 106 ASN B N   1 
ATOM   2378  C CA  . ASN B  1 104 ? 171.634 166.835 158.362 1.00 87.12  ? 106 ASN B CA  1 
ATOM   2379  C C   . ASN B  1 104 ? 170.318 166.858 159.136 1.00 93.83  ? 106 ASN B C   1 
ATOM   2380  O O   . ASN B  1 104 ? 170.150 166.157 160.135 1.00 101.46 ? 106 ASN B O   1 
ATOM   2381  C CB  . ASN B  1 104 ? 172.758 166.239 159.210 1.00 90.96  ? 106 ASN B CB  1 
ATOM   2382  C CG  . ASN B  1 104 ? 174.095 166.263 158.502 1.00 95.00  ? 106 ASN B CG  1 
ATOM   2383  O OD1 . ASN B  1 104 ? 174.173 166.059 157.292 1.00 99.79  ? 106 ASN B OD1 1 
ATOM   2384  N ND2 . ASN B  1 104 ? 175.159 166.511 159.254 1.00 95.39  ? 106 ASN B ND2 1 
ATOM   2385  N N   . SER B  1 105 ? 169.372 167.666 158.667 1.00 90.17  ? 107 SER B N   1 
ATOM   2386  C CA  . SER B  1 105 ? 168.081 167.826 159.317 1.00 88.43  ? 107 SER B CA  1 
ATOM   2387  C C   . SER B  1 105 ? 166.995 167.123 158.515 1.00 90.28  ? 107 SER B C   1 
ATOM   2388  O O   . SER B  1 105 ? 167.079 167.008 157.289 1.00 94.59  ? 107 SER B O   1 
ATOM   2389  C CB  . SER B  1 105 ? 167.726 169.306 159.482 1.00 88.21  ? 107 SER B CB  1 
ATOM   2390  O OG  . SER B  1 105 ? 166.924 169.756 158.406 1.00 93.42  ? 107 SER B OG  1 
ATOM   2391  N N   . SER B  1 106 ? 165.968 166.657 159.221 1.00 86.43  ? 108 SER B N   1 
ATOM   2392  C CA  . SER B  1 106 ? 164.876 165.906 158.616 1.00 81.48  ? 108 SER B CA  1 
ATOM   2393  C C   . SER B  1 106 ? 163.547 166.439 159.125 1.00 82.80  ? 108 SER B C   1 
ATOM   2394  O O   . SER B  1 106 ? 163.355 166.584 160.336 1.00 87.73  ? 108 SER B O   1 
ATOM   2395  C CB  . SER B  1 106 ? 164.999 164.413 158.928 1.00 86.12  ? 108 SER B CB  1 
ATOM   2396  O OG  . SER B  1 106 ? 166.343 163.980 158.824 1.00 92.26  ? 108 SER B OG  1 
ATOM   2397  N N   . ALA B  1 107 ? 162.635 166.728 158.201 1.00 76.55  ? 109 ALA B N   1 
ATOM   2398  C CA  . ALA B  1 107 ? 161.283 167.173 158.523 1.00 71.11  ? 109 ALA B CA  1 
ATOM   2399  C C   . ALA B  1 107 ? 160.305 166.214 157.862 1.00 79.50  ? 109 ALA B C   1 
ATOM   2400  O O   . ALA B  1 107 ? 160.174 166.202 156.634 1.00 86.36  ? 109 ALA B O   1 
ATOM   2401  C CB  . ALA B  1 107 ? 161.049 168.608 158.056 1.00 73.37  ? 109 ALA B CB  1 
ATOM   2402  N N   . PHE B  1 108 ? 159.622 165.410 158.672 1.00 77.50  ? 110 PHE B N   1 
ATOM   2403  C CA  . PHE B  1 108 ? 158.703 164.395 158.177 1.00 75.34  ? 110 PHE B CA  1 
ATOM   2404  C C   . PHE B  1 108 ? 157.327 164.650 158.768 1.00 79.94  ? 110 PHE B C   1 
ATOM   2405  O O   . PHE B  1 108 ? 157.208 164.938 159.963 1.00 87.74  ? 110 PHE B O   1 
ATOM   2406  C CB  . PHE B  1 108 ? 159.187 162.987 158.540 1.00 78.42  ? 110 PHE B CB  1 
ATOM   2407  C CG  . PHE B  1 108 ? 160.331 162.496 157.696 1.00 76.46  ? 110 PHE B CG  1 
ATOM   2408  C CD1 . PHE B  1 108 ? 161.558 163.135 157.722 1.00 78.47  ? 110 PHE B CD1 1 
ATOM   2409  C CD2 . PHE B  1 108 ? 160.181 161.389 156.882 1.00 79.58  ? 110 PHE B CD2 1 
ATOM   2410  C CE1 . PHE B  1 108 ? 162.608 162.683 156.950 1.00 79.09  ? 110 PHE B CE1 1 
ATOM   2411  C CE2 . PHE B  1 108 ? 161.230 160.934 156.108 1.00 82.25  ? 110 PHE B CE2 1 
ATOM   2412  C CZ  . PHE B  1 108 ? 162.443 161.582 156.143 1.00 80.68  ? 110 PHE B CZ  1 
ATOM   2413  N N   . GLY B  1 109 ? 156.290 164.549 157.935 1.00 74.98  ? 111 GLY B N   1 
ATOM   2414  C CA  . GLY B  1 109 ? 154.923 164.764 158.366 1.00 76.05  ? 111 GLY B CA  1 
ATOM   2415  C C   . GLY B  1 109 ? 154.269 165.895 157.585 1.00 78.70  ? 111 GLY B C   1 
ATOM   2416  O O   . GLY B  1 109 ? 154.440 166.009 156.369 1.00 81.48  ? 111 GLY B O   1 
ATOM   2417  N N   . PHE B  1 110 ? 153.518 166.730 158.302 1.00 78.03  ? 112 PHE B N   1 
ATOM   2418  C CA  . PHE B  1 110 ? 152.760 167.822 157.704 1.00 74.34  ? 112 PHE B CA  1 
ATOM   2419  C C   . PHE B  1 110 ? 153.226 169.145 158.293 1.00 80.67  ? 112 PHE B C   1 
ATOM   2420  O O   . PHE B  1 110 ? 153.152 169.344 159.510 1.00 83.62  ? 112 PHE B O   1 
ATOM   2421  C CB  . PHE B  1 110 ? 151.261 167.636 157.939 1.00 76.07  ? 112 PHE B CB  1 
ATOM   2422  C CG  . PHE B  1 110 ? 150.445 168.854 157.625 1.00 80.47  ? 112 PHE B CG  1 
ATOM   2423  C CD1 . PHE B  1 110 ? 150.385 169.349 156.335 1.00 85.48  ? 112 PHE B CD1 1 
ATOM   2424  C CD2 . PHE B  1 110 ? 149.742 169.506 158.620 1.00 78.99  ? 112 PHE B CD2 1 
ATOM   2425  C CE1 . PHE B  1 110 ? 149.636 170.469 156.045 1.00 83.97  ? 112 PHE B CE1 1 
ATOM   2426  C CE2 . PHE B  1 110 ? 148.992 170.628 158.335 1.00 78.16  ? 112 PHE B CE2 1 
ATOM   2427  C CZ  . PHE B  1 110 ? 148.939 171.110 157.046 1.00 81.70  ? 112 PHE B CZ  1 
ATOM   2428  N N   . LYS B  1 111 ? 153.681 170.047 157.426 1.00 80.94  ? 113 LYS B N   1 
ATOM   2429  C CA  . LYS B  1 111 ? 154.091 171.402 157.797 1.00 79.10  ? 113 LYS B CA  1 
ATOM   2430  C C   . LYS B  1 111 ? 155.019 171.395 159.012 1.00 81.81  ? 113 LYS B C   1 
ATOM   2431  O O   . LYS B  1 111 ? 154.698 171.901 160.086 1.00 86.77  ? 113 LYS B O   1 
ATOM   2432  C CB  . LYS B  1 111 ? 152.870 172.296 158.037 1.00 79.42  ? 113 LYS B CB  1 
ATOM   2433  C CG  . LYS B  1 111 ? 153.211 173.770 158.221 1.00 89.61  ? 113 LYS B CG  1 
ATOM   2434  C CD  . LYS B  1 111 ? 152.946 174.571 156.965 1.00 88.16  ? 113 LYS B CD  1 
ATOM   2435  C CE  . LYS B  1 111 ? 153.769 175.847 156.937 1.00 92.79  ? 113 LYS B CE  1 
ATOM   2436  N NZ  . LYS B  1 111 ? 155.220 175.571 157.110 1.00 91.71  ? 113 LYS B NZ  1 
ATOM   2437  N N   . ASN B  1 112 ? 156.187 170.794 158.827 1.00 77.16  ? 114 ASN B N   1 
ATOM   2438  C CA  . ASN B  1 112 ? 157.229 170.791 159.842 1.00 77.29  ? 114 ASN B CA  1 
ATOM   2439  C C   . ASN B  1 112 ? 158.410 171.606 159.340 1.00 83.74  ? 114 ASN B C   1 
ATOM   2440  O O   . ASN B  1 112 ? 158.862 171.417 158.207 1.00 91.51  ? 114 ASN B O   1 
ATOM   2441  C CB  . ASN B  1 112 ? 157.668 169.366 160.178 1.00 75.96  ? 114 ASN B CB  1 
ATOM   2442  C CG  . ASN B  1 112 ? 156.714 168.675 161.126 1.00 79.21  ? 114 ASN B CG  1 
ATOM   2443  O OD1 . ASN B  1 112 ? 156.521 169.113 162.258 1.00 81.16  ? 114 ASN B OD1 1 
ATOM   2444  N ND2 . ASN B  1 112 ? 156.110 167.588 160.667 1.00 81.97  ? 114 ASN B ND2 1 
ATOM   2445  N N   . THR B  1 113 ? 158.900 172.512 160.179 1.00 80.88  ? 115 THR B N   1 
ATOM   2446  C CA  . THR B  1 113 ? 160.046 173.346 159.848 1.00 82.87  ? 115 THR B CA  1 
ATOM   2447  C C   . THR B  1 113 ? 161.170 173.032 160.821 1.00 83.81  ? 115 THR B C   1 
ATOM   2448  O O   . THR B  1 113 ? 161.009 173.193 162.034 1.00 87.06  ? 115 THR B O   1 
ATOM   2449  C CB  . THR B  1 113 ? 159.687 174.831 159.902 1.00 88.07  ? 115 THR B CB  1 
ATOM   2450  O OG1 . THR B  1 113 ? 158.686 175.118 158.919 1.00 97.58  ? 115 THR B OG1 1 
ATOM   2451  C CG2 . THR B  1 113 ? 160.915 175.684 159.631 1.00 84.65  ? 115 THR B CG2 1 
ATOM   2452  N N   . VAL B  1 114 ? 162.303 172.584 160.291 1.00 81.26  ? 116 VAL B N   1 
ATOM   2453  C CA  . VAL B  1 114 ? 163.483 172.286 161.091 1.00 81.84  ? 116 VAL B CA  1 
ATOM   2454  C C   . VAL B  1 114 ? 164.587 173.233 160.651 1.00 87.21  ? 116 VAL B C   1 
ATOM   2455  O O   . VAL B  1 114 ? 165.020 173.200 159.493 1.00 93.20  ? 116 VAL B O   1 
ATOM   2456  C CB  . VAL B  1 114 ? 163.914 170.820 160.944 1.00 85.10  ? 116 VAL B CB  1 
ATOM   2457  C CG1 . VAL B  1 114 ? 164.932 170.466 162.004 1.00 84.76  ? 116 VAL B CG1 1 
ATOM   2458  C CG2 . VAL B  1 114 ? 162.709 169.908 161.045 1.00 89.12  ? 116 VAL B CG2 1 
ATOM   2459  N N   . SER B  1 115 ? 165.042 174.076 161.575 1.00 88.10  ? 117 SER B N   1 
ATOM   2460  C CA  . SER B  1 115 ? 166.048 175.080 161.276 1.00 93.11  ? 117 SER B CA  1 
ATOM   2461  C C   . SER B  1 115 ? 167.370 174.834 161.984 1.00 94.85  ? 117 SER B C   1 
ATOM   2462  O O   . SER B  1 115 ? 168.290 175.648 161.845 1.00 103.66 ? 117 SER B O   1 
ATOM   2463  C CB  . SER B  1 115 ? 165.529 176.477 161.640 1.00 96.96  ? 117 SER B CB  1 
ATOM   2464  O OG  . SER B  1 115 ? 166.566 177.439 161.565 1.00 114.79 ? 117 SER B OG  1 
ATOM   2465  N N   . GLY B  1 116 ? 167.497 173.740 162.734 1.00 89.17  ? 118 GLY B N   1 
ATOM   2466  C CA  . GLY B  1 116 ? 168.686 173.470 163.508 1.00 89.43  ? 118 GLY B CA  1 
ATOM   2467  C C   . GLY B  1 116 ? 169.653 172.528 162.806 1.00 95.47  ? 118 GLY B C   1 
ATOM   2468  O O   . GLY B  1 116 ? 169.450 172.089 161.677 1.00 100.76 ? 118 GLY B O   1 
ATOM   2469  N N   . PHE B  1 117 ? 170.730 172.219 163.520 1.00 94.79  ? 119 PHE B N   1 
ATOM   2470  C CA  . PHE B  1 117 ? 171.799 171.362 163.028 1.00 90.89  ? 119 PHE B CA  1 
ATOM   2471  C C   . PHE B  1 117 ? 171.588 169.950 163.561 1.00 91.40  ? 119 PHE B C   1 
ATOM   2472  O O   . PHE B  1 117 ? 171.527 169.747 164.779 1.00 98.92  ? 119 PHE B O   1 
ATOM   2473  C CB  . PHE B  1 117 ? 173.155 171.920 163.459 1.00 90.01  ? 119 PHE B CB  1 
ATOM   2474  C CG  . PHE B  1 117 ? 174.327 171.069 163.067 1.00 91.02  ? 119 PHE B CG  1 
ATOM   2475  C CD1 . PHE B  1 117 ? 174.375 170.441 161.838 1.00 92.71  ? 119 PHE B CD1 1 
ATOM   2476  C CD2 . PHE B  1 117 ? 175.397 170.918 163.929 1.00 91.08  ? 119 PHE B CD2 1 
ATOM   2477  C CE1 . PHE B  1 117 ? 175.463 169.666 161.488 1.00 93.52  ? 119 PHE B CE1 1 
ATOM   2478  C CE2 . PHE B  1 117 ? 176.483 170.145 163.582 1.00 95.17  ? 119 PHE B CE2 1 
ATOM   2479  C CZ  . PHE B  1 117 ? 176.516 169.519 162.360 1.00 93.98  ? 119 PHE B CZ  1 
ATOM   2480  N N   . ASN B  1 118 ? 171.465 168.983 162.648 1.00 83.59  ? 120 ASN B N   1 
ATOM   2481  C CA  . ASN B  1 118 ? 171.237 167.578 162.996 1.00 85.64  ? 120 ASN B CA  1 
ATOM   2482  C C   . ASN B  1 118 ? 169.955 167.385 163.800 1.00 89.61  ? 120 ASN B C   1 
ATOM   2483  O O   . ASN B  1 118 ? 169.864 166.480 164.631 1.00 96.56  ? 120 ASN B O   1 
ATOM   2484  C CB  . ASN B  1 118 ? 172.428 166.985 163.754 1.00 87.54  ? 120 ASN B CB  1 
ATOM   2485  C CG  . ASN B  1 118 ? 173.430 166.320 162.838 1.00 89.86  ? 120 ASN B CG  1 
ATOM   2486  O OD1 . ASN B  1 118 ? 173.134 165.306 162.210 1.00 90.88  ? 120 ASN B OD1 1 
ATOM   2487  N ND2 . ASN B  1 118 ? 174.629 166.883 162.764 1.00 88.44  ? 120 ASN B ND2 1 
ATOM   2488  N N   . SER B  1 119 ? 168.952 168.223 163.561 1.00 89.15  ? 121 SER B N   1 
ATOM   2489  C CA  . SER B  1 119 ? 167.691 168.144 164.280 1.00 88.22  ? 121 SER B CA  1 
ATOM   2490  C C   . SER B  1 119 ? 166.614 167.520 163.402 1.00 88.43  ? 121 SER B C   1 
ATOM   2491  O O   . SER B  1 119 ? 166.670 167.591 162.173 1.00 93.38  ? 121 SER B O   1 
ATOM   2492  C CB  . SER B  1 119 ? 167.242 169.528 164.748 1.00 90.15  ? 121 SER B CB  1 
ATOM   2493  O OG  . SER B  1 119 ? 167.594 170.517 163.802 1.00 97.17  ? 121 SER B OG  1 
ATOM   2494  N N   . SER B  1 120 ? 165.626 166.909 164.050 1.00 86.71  ? 122 SER B N   1 
ATOM   2495  C CA  . SER B  1 120 ? 164.573 166.179 163.365 1.00 81.93  ? 122 SER B CA  1 
ATOM   2496  C C   . SER B  1 120 ? 163.218 166.583 163.926 1.00 80.54  ? 122 SER B C   1 
ATOM   2497  O O   . SER B  1 120 ? 163.112 167.090 165.044 1.00 87.90  ? 122 SER B O   1 
ATOM   2498  C CB  . SER B  1 120 ? 164.764 164.664 163.501 1.00 90.65  ? 122 SER B CB  1 
ATOM   2499  O OG  . SER B  1 120 ? 166.009 164.258 162.961 1.00 95.17  ? 122 SER B OG  1 
ATOM   2500  N N   . ALA B  1 121 ? 162.176 166.360 163.129 1.00 79.48  ? 123 ALA B N   1 
ATOM   2501  C CA  . ALA B  1 121 ? 160.816 166.643 163.565 1.00 78.32  ? 123 ALA B CA  1 
ATOM   2502  C C   . ALA B  1 121 ? 159.859 165.736 162.811 1.00 81.76  ? 123 ALA B C   1 
ATOM   2503  O O   . ALA B  1 121 ? 159.933 165.640 161.583 1.00 87.09  ? 123 ALA B O   1 
ATOM   2504  C CB  . ALA B  1 121 ? 160.453 168.113 163.334 1.00 74.64  ? 123 ALA B CB  1 
ATOM   2505  N N   . PHE B  1 122 ? 158.969 165.074 163.546 1.00 75.58  ? 124 PHE B N   1 
ATOM   2506  C CA  . PHE B  1 122 ? 157.946 164.220 162.961 1.00 75.31  ? 124 PHE B CA  1 
ATOM   2507  C C   . PHE B  1 122 ? 156.606 164.563 163.590 1.00 81.92  ? 124 PHE B C   1 
ATOM   2508  O O   . PHE B  1 122 ? 156.497 164.639 164.816 1.00 87.61  ? 124 PHE B O   1 
ATOM   2509  C CB  . PHE B  1 122 ? 158.265 162.738 163.168 1.00 77.16  ? 124 PHE B CB  1 
ATOM   2510  C CG  . PHE B  1 122 ? 157.271 161.812 162.533 1.00 81.51  ? 124 PHE B CG  1 
ATOM   2511  C CD1 . PHE B  1 122 ? 157.019 161.872 161.175 1.00 85.88  ? 124 PHE B CD1 1 
ATOM   2512  C CD2 . PHE B  1 122 ? 156.582 160.888 163.295 1.00 82.20  ? 124 PHE B CD2 1 
ATOM   2513  C CE1 . PHE B  1 122 ? 156.102 161.022 160.589 1.00 90.18  ? 124 PHE B CE1 1 
ATOM   2514  C CE2 . PHE B  1 122 ? 155.663 160.038 162.715 1.00 82.17  ? 124 PHE B CE2 1 
ATOM   2515  C CZ  . PHE B  1 122 ? 155.423 160.105 161.360 1.00 89.98  ? 124 PHE B CZ  1 
ATOM   2516  N N   . GLY B  1 123 ? 155.593 164.766 162.755 1.00 78.13  ? 125 GLY B N   1 
ATOM   2517  C CA  . GLY B  1 123 ? 154.285 165.139 163.252 1.00 77.75  ? 125 GLY B CA  1 
ATOM   2518  C C   . GLY B  1 123 ? 153.604 166.177 162.387 1.00 84.96  ? 125 GLY B C   1 
ATOM   2519  O O   . GLY B  1 123 ? 153.697 166.122 161.158 1.00 90.86  ? 125 GLY B O   1 
ATOM   2520  N N   . SER B  1 124 ? 152.915 167.129 163.012 1.00 82.39  ? 126 SER B N   1 
ATOM   2521  C CA  . SER B  1 124 ? 152.200 168.161 162.275 1.00 79.12  ? 126 SER B CA  1 
ATOM   2522  C C   . SER B  1 124 ? 152.407 169.514 162.935 1.00 83.23  ? 126 SER B C   1 
ATOM   2523  O O   . SER B  1 124 ? 152.239 169.646 164.150 1.00 88.50  ? 126 SER B O   1 
ATOM   2524  C CB  . SER B  1 124 ? 150.704 167.843 162.192 1.00 80.76  ? 126 SER B CB  1 
ATOM   2525  O OG  . SER B  1 124 ? 150.070 168.063 163.438 1.00 89.25  ? 126 SER B OG  1 
ATOM   2526  N N   . GLN B  1 125 ? 152.770 170.511 162.126 1.00 81.68  ? 127 GLN B N   1 
ATOM   2527  C CA  . GLN B  1 125 ? 152.806 171.912 162.547 1.00 82.00  ? 127 GLN B CA  1 
ATOM   2528  C C   . GLN B  1 125 ? 153.742 172.127 163.735 1.00 85.95  ? 127 GLN B C   1 
ATOM   2529  O O   . GLN B  1 125 ? 153.366 172.707 164.755 1.00 93.32  ? 127 GLN B O   1 
ATOM   2530  C CB  . GLN B  1 125 ? 151.396 172.416 162.859 1.00 85.36  ? 127 GLN B CB  1 
ATOM   2531  C CG  . GLN B  1 125 ? 150.400 172.158 161.745 1.00 88.06  ? 127 GLN B CG  1 
ATOM   2532  C CD  . GLN B  1 125 ? 148.969 172.374 162.181 1.00 92.47  ? 127 GLN B CD  1 
ATOM   2533  O OE1 . GLN B  1 125 ? 148.441 173.481 162.088 1.00 100.09 ? 127 GLN B OE1 1 
ATOM   2534  N NE2 . GLN B  1 125 ? 148.332 171.315 162.662 1.00 94.24  ? 127 GLN B NE2 1 
ATOM   2535  N N   . TYR B  1 126 ? 154.981 171.666 163.593 1.00 81.33  ? 128 TYR B N   1 
ATOM   2536  C CA  . TYR B  1 126 ? 155.992 171.817 164.628 1.00 79.90  ? 128 TYR B CA  1 
ATOM   2537  C C   . TYR B  1 126 ? 157.244 172.446 164.038 1.00 82.27  ? 128 TYR B C   1 
ATOM   2538  O O   . TYR B  1 126 ? 157.621 172.148 162.901 1.00 87.70  ? 128 TYR B O   1 
ATOM   2539  C CB  . TYR B  1 126 ? 156.340 170.472 165.270 1.00 77.69  ? 128 TYR B CB  1 
ATOM   2540  C CG  . TYR B  1 126 ? 155.917 170.355 166.715 1.00 84.40  ? 128 TYR B CG  1 
ATOM   2541  C CD1 . TYR B  1 126 ? 155.846 171.475 167.531 1.00 80.74  ? 128 TYR B CD1 1 
ATOM   2542  C CD2 . TYR B  1 126 ? 155.586 169.124 167.263 1.00 85.92  ? 128 TYR B CD2 1 
ATOM   2543  C CE1 . TYR B  1 126 ? 155.459 171.371 168.852 1.00 81.15  ? 128 TYR B CE1 1 
ATOM   2544  C CE2 . TYR B  1 126 ? 155.199 169.011 168.581 1.00 85.39  ? 128 TYR B CE2 1 
ATOM   2545  C CZ  . TYR B  1 126 ? 155.137 170.136 169.370 1.00 85.36  ? 128 TYR B CZ  1 
ATOM   2546  O OH  . TYR B  1 126 ? 154.750 170.023 170.684 1.00 91.34  ? 128 TYR B OH  1 
ATOM   2547  N N   . GLN B  1 127 ? 157.885 173.314 164.815 1.00 80.30  ? 129 GLN B N   1 
ATOM   2548  C CA  . GLN B  1 127 ? 159.129 173.955 164.418 1.00 78.21  ? 129 GLN B CA  1 
ATOM   2549  C C   . GLN B  1 127 ? 160.219 173.629 165.427 1.00 85.38  ? 129 GLN B C   1 
ATOM   2550  O O   . GLN B  1 127 ? 159.986 173.657 166.638 1.00 91.34  ? 129 GLN B O   1 
ATOM   2551  C CB  . GLN B  1 127 ? 158.971 175.471 164.299 1.00 82.81  ? 129 GLN B CB  1 
ATOM   2552  C CG  . GLN B  1 127 ? 159.919 176.097 163.293 1.00 89.05  ? 129 GLN B CG  1 
ATOM   2553  C CD  . GLN B  1 127 ? 160.185 177.558 163.572 1.00 96.52  ? 129 GLN B CD  1 
ATOM   2554  O OE1 . GLN B  1 127 ? 160.107 178.005 164.713 1.00 99.87  ? 129 GLN B OE1 1 
ATOM   2555  N NE2 . GLN B  1 127 ? 160.503 178.312 162.528 1.00 92.85  ? 129 GLN B NE2 1 
ATOM   2556  N N   . VAL B  1 128 ? 161.409 173.317 164.922 1.00 87.62  ? 130 VAL B N   1 
ATOM   2557  C CA  . VAL B  1 128 ? 162.559 172.969 165.750 1.00 84.05  ? 130 VAL B CA  1 
ATOM   2558  C C   . VAL B  1 128 ? 163.714 173.850 165.295 1.00 87.39  ? 130 VAL B C   1 
ATOM   2559  O O   . VAL B  1 128 ? 164.347 173.573 164.270 1.00 91.61  ? 130 VAL B O   1 
ATOM   2560  C CB  . VAL B  1 128 ? 162.925 171.486 165.653 1.00 75.12  ? 130 VAL B CB  1 
ATOM   2561  C CG1 . VAL B  1 128 ? 164.114 171.179 166.542 1.00 82.90  ? 130 VAL B CG1 1 
ATOM   2562  C CG2 . VAL B  1 128 ? 161.739 170.620 166.033 1.00 77.96  ? 130 VAL B CG2 1 
ATOM   2563  N N   . THR B  1 129 ? 163.991 174.912 166.047 1.00 86.83  ? 131 THR B N   1 
ATOM   2564  C CA  . THR B  1 129 ? 165.102 175.802 165.748 1.00 90.16  ? 131 THR B CA  1 
ATOM   2565  C C   . THR B  1 129 ? 166.349 175.496 166.565 1.00 93.00  ? 131 THR B C   1 
ATOM   2566  O O   . THR B  1 129 ? 167.392 176.112 166.324 1.00 94.47  ? 131 THR B O   1 
ATOM   2567  C CB  . THR B  1 129 ? 164.694 177.261 165.980 1.00 95.94  ? 131 THR B CB  1 
ATOM   2568  O OG1 . THR B  1 129 ? 164.331 177.444 167.354 1.00 99.65  ? 131 THR B OG1 1 
ATOM   2569  C CG2 . THR B  1 129 ? 163.514 177.628 165.099 1.00 94.67  ? 131 THR B CG2 1 
ATOM   2570  N N   . GLY B  1 130 ? 166.270 174.569 167.515 1.00 90.91  ? 132 GLY B N   1 
ATOM   2571  C CA  . GLY B  1 130 ? 167.425 174.220 168.311 1.00 90.67  ? 132 GLY B CA  1 
ATOM   2572  C C   . GLY B  1 130 ? 168.369 173.283 167.587 1.00 94.52  ? 132 GLY B C   1 
ATOM   2573  O O   . GLY B  1 130 ? 168.054 172.708 166.547 1.00 96.47  ? 132 GLY B O   1 
ATOM   2574  N N   . ASN B  1 131 ? 169.554 173.125 168.166 1.00 97.87  ? 133 ASN B N   1 
ATOM   2575  C CA  . ASN B  1 131 ? 170.594 172.275 167.606 1.00 91.05  ? 133 ASN B CA  1 
ATOM   2576  C C   . ASN B  1 131 ? 170.554 170.913 168.283 1.00 96.35  ? 133 ASN B C   1 
ATOM   2577  O O   . ASN B  1 131 ? 170.471 170.830 169.513 1.00 101.82 ? 133 ASN B O   1 
ATOM   2578  C CB  . ASN B  1 131 ? 171.971 172.915 167.781 1.00 91.56  ? 133 ASN B CB  1 
ATOM   2579  C CG  . ASN B  1 131 ? 172.371 173.761 166.593 1.00 95.94  ? 133 ASN B CG  1 
ATOM   2580  O OD1 . ASN B  1 131 ? 171.552 174.058 165.725 1.00 96.08  ? 133 ASN B OD1 1 
ATOM   2581  N ND2 . ASN B  1 131 ? 173.636 174.158 166.549 1.00 105.48 ? 133 ASN B ND2 1 
ATOM   2582  N N   . PHE B  1 132 ? 170.612 169.853 167.476 1.00 92.39  ? 134 PHE B N   1 
ATOM   2583  C CA  . PHE B  1 132 ? 170.531 168.476 167.967 1.00 92.44  ? 134 PHE B CA  1 
ATOM   2584  C C   . PHE B  1 132 ? 169.265 168.257 168.789 1.00 92.92  ? 134 PHE B C   1 
ATOM   2585  O O   . PHE B  1 132 ? 169.281 167.582 169.820 1.00 96.08  ? 134 PHE B O   1 
ATOM   2586  C CB  . PHE B  1 132 ? 171.770 168.098 168.781 1.00 92.07  ? 134 PHE B CB  1 
ATOM   2587  C CG  . PHE B  1 132 ? 173.029 168.769 168.321 1.00 93.04  ? 134 PHE B CG  1 
ATOM   2588  C CD1 . PHE B  1 132 ? 173.563 168.491 167.077 1.00 95.97  ? 134 PHE B CD1 1 
ATOM   2589  C CD2 . PHE B  1 132 ? 173.682 169.674 169.136 1.00 93.15  ? 134 PHE B CD2 1 
ATOM   2590  C CE1 . PHE B  1 132 ? 174.723 169.102 166.656 1.00 95.34  ? 134 PHE B CE1 1 
ATOM   2591  C CE2 . PHE B  1 132 ? 174.842 170.291 168.718 1.00 93.42  ? 134 PHE B CE2 1 
ATOM   2592  C CZ  . PHE B  1 132 ? 175.362 170.004 167.476 1.00 93.71  ? 134 PHE B CZ  1 
ATOM   2593  N N   . SER B  1 133 ? 168.159 168.831 168.332 1.00 88.04  ? 135 SER B N   1 
ATOM   2594  C CA  . SER B  1 133 ? 166.882 168.750 169.022 1.00 87.42  ? 135 SER B CA  1 
ATOM   2595  C C   . SER B  1 133 ? 165.886 167.956 168.189 1.00 89.53  ? 135 SER B C   1 
ATOM   2596  O O   . SER B  1 133 ? 166.154 167.575 167.048 1.00 96.40  ? 135 SER B O   1 
ATOM   2597  C CB  . SER B  1 133 ? 166.337 170.150 169.320 1.00 91.67  ? 135 SER B CB  1 
ATOM   2598  O OG  . SER B  1 133 ? 167.335 170.971 169.898 1.00 99.14  ? 135 SER B OG  1 
ATOM   2599  N N   . GLY B  1 134 ? 164.722 167.703 168.777 1.00 85.82  ? 136 GLY B N   1 
ATOM   2600  C CA  . GLY B  1 134 ? 163.698 166.945 168.087 1.00 78.73  ? 136 GLY B CA  1 
ATOM   2601  C C   . GLY B  1 134 ? 162.327 167.213 168.657 1.00 78.47  ? 136 GLY B C   1 
ATOM   2602  O O   . GLY B  1 134 ? 162.181 167.678 169.792 1.00 85.72  ? 136 GLY B O   1 
ATOM   2603  N N   . ALA B  1 135 ? 161.315 166.910 167.850 1.00 78.19  ? 137 ALA B N   1 
ATOM   2604  C CA  . ALA B  1 135 ? 159.928 167.070 168.257 1.00 74.26  ? 137 ALA B CA  1 
ATOM   2605  C C   . ALA B  1 135 ? 159.096 165.986 167.593 1.00 80.75  ? 137 ALA B C   1 
ATOM   2606  O O   . ALA B  1 135 ? 159.282 165.689 166.410 1.00 86.60  ? 137 ALA B O   1 
ATOM   2607  C CB  . ALA B  1 135 ? 159.388 168.455 167.888 1.00 72.04  ? 137 ALA B CB  1 
ATOM   2608  N N   . PHE B  1 136 ? 158.177 165.403 168.359 1.00 77.40  ? 138 PHE B N   1 
ATOM   2609  C CA  . PHE B  1 136 ? 157.302 164.342 167.860 1.00 74.12  ? 138 PHE B CA  1 
ATOM   2610  C C   . PHE B  1 136 ? 155.909 164.596 168.424 1.00 78.08  ? 138 PHE B C   1 
ATOM   2611  O O   . PHE B  1 136 ? 155.631 164.269 169.581 1.00 83.96  ? 138 PHE B O   1 
ATOM   2612  C CB  . PHE B  1 136 ? 157.821 162.964 168.250 1.00 72.64  ? 138 PHE B CB  1 
ATOM   2613  C CG  . PHE B  1 136 ? 156.851 161.853 167.981 1.00 78.80  ? 138 PHE B CG  1 
ATOM   2614  C CD1 . PHE B  1 136 ? 156.372 161.627 166.704 1.00 80.28  ? 138 PHE B CD1 1 
ATOM   2615  C CD2 . PHE B  1 136 ? 156.418 161.033 169.006 1.00 84.92  ? 138 PHE B CD2 1 
ATOM   2616  C CE1 . PHE B  1 136 ? 155.478 160.605 166.456 1.00 77.68  ? 138 PHE B CE1 1 
ATOM   2617  C CE2 . PHE B  1 136 ? 155.524 160.009 168.762 1.00 88.04  ? 138 PHE B CE2 1 
ATOM   2618  C CZ  . PHE B  1 136 ? 155.055 159.796 167.485 1.00 81.86  ? 138 PHE B CZ  1 
ATOM   2619  N N   . GLY B  1 137 ? 155.041 165.176 167.607 1.00 76.69  ? 139 GLY B N   1 
ATOM   2620  C CA  . GLY B  1 137 ? 153.702 165.510 168.051 1.00 77.05  ? 139 GLY B CA  1 
ATOM   2621  C C   . GLY B  1 137 ? 153.083 166.542 167.127 1.00 83.06  ? 139 GLY B C   1 
ATOM   2622  O O   . GLY B  1 137 ? 153.463 166.659 165.965 1.00 89.81  ? 139 GLY B O   1 
ATOM   2623  N N   . MET B  1 138 ? 152.124 167.282 167.675 1.00 81.05  ? 140 MET B N   1 
ATOM   2624  C CA  . MET B  1 138 ? 151.403 168.306 166.934 1.00 82.58  ? 140 MET B CA  1 
ATOM   2625  C C   . MET B  1 138 ? 151.541 169.645 167.641 1.00 87.87  ? 140 MET B C   1 
ATOM   2626  O O   . MET B  1 138 ? 151.368 169.728 168.861 1.00 91.98  ? 140 MET B O   1 
ATOM   2627  C CB  . MET B  1 138 ? 149.924 167.944 166.787 1.00 85.71  ? 140 MET B CB  1 
ATOM   2628  C CG  . MET B  1 138 ? 149.038 169.140 166.492 1.00 95.32  ? 140 MET B CG  1 
ATOM   2629  S SD  . MET B  1 138 ? 147.284 168.780 166.635 1.00 117.62 ? 140 MET B SD  1 
ATOM   2630  C CE  . MET B  1 138 ? 146.864 169.735 168.088 1.00 96.22  ? 140 MET B CE  1 
ATOM   2631  N N   . GLY B  1 139 ? 151.851 170.686 166.874 1.00 84.38  ? 141 GLY B N   1 
ATOM   2632  C CA  . GLY B  1 139 ? 151.870 172.035 167.401 1.00 85.11  ? 141 GLY B CA  1 
ATOM   2633  C C   . GLY B  1 139 ? 150.715 172.854 166.866 1.00 93.15  ? 141 GLY B C   1 
ATOM   2634  O O   . GLY B  1 139 ? 149.575 172.383 166.842 1.00 99.71  ? 141 GLY B O   1 
ATOM   2635  N N   . GLU B  1 140 ? 150.991 174.082 166.433 1.00 95.17  ? 142 GLU B N   1 
ATOM   2636  C CA  . GLU B  1 140 ? 149.957 174.933 165.865 1.00 97.36  ? 142 GLU B CA  1 
ATOM   2637  C C   . GLU B  1 140 ? 150.596 175.923 164.904 1.00 99.02  ? 142 GLU B C   1 
ATOM   2638  O O   . GLU B  1 140 ? 151.678 176.454 165.166 1.00 102.12 ? 142 GLU B O   1 
ATOM   2639  C CB  . GLU B  1 140 ? 149.174 175.668 166.960 1.00 98.81  ? 142 GLU B CB  1 
ATOM   2640  C CG  . GLU B  1 140 ? 148.541 176.973 166.511 1.00 109.78 ? 142 GLU B CG  1 
ATOM   2641  C CD  . GLU B  1 140 ? 147.182 177.204 167.136 1.00 121.75 ? 142 GLU B CD  1 
ATOM   2642  O OE1 . GLU B  1 140 ? 146.648 176.264 167.760 1.00 122.76 ? 142 GLU B OE1 1 
ATOM   2643  O OE2 . GLU B  1 140 ? 146.647 178.324 167.000 1.00 122.67 ? 142 GLU B OE2 1 
ATOM   2644  N N   . PHE B  1 141 ? 149.912 176.166 163.786 1.00 93.44  ? 143 PHE B N   1 
ATOM   2645  C CA  . PHE B  1 141 ? 150.399 177.102 162.775 1.00 91.90  ? 143 PHE B CA  1 
ATOM   2646  C C   . PHE B  1 141 ? 149.197 177.873 162.238 1.00 99.67  ? 143 PHE B C   1 
ATOM   2647  O O   . PHE B  1 141 ? 148.514 177.401 161.324 1.00 105.17 ? 143 PHE B O   1 
ATOM   2648  C CB  . PHE B  1 141 ? 151.136 176.370 161.662 1.00 87.09  ? 143 PHE B CB  1 
ATOM   2649  C CG  . PHE B  1 141 ? 151.583 177.263 160.542 1.00 91.97  ? 143 PHE B CG  1 
ATOM   2650  C CD1 . PHE B  1 141 ? 152.694 178.074 160.686 1.00 94.88  ? 143 PHE B CD1 1 
ATOM   2651  C CD2 . PHE B  1 141 ? 150.895 177.288 159.343 1.00 92.81  ? 143 PHE B CD2 1 
ATOM   2652  C CE1 . PHE B  1 141 ? 153.107 178.895 159.656 1.00 96.04  ? 143 PHE B CE1 1 
ATOM   2653  C CE2 . PHE B  1 141 ? 151.302 178.108 158.311 1.00 92.36  ? 143 PHE B CE2 1 
ATOM   2654  C CZ  . PHE B  1 141 ? 152.410 178.912 158.468 1.00 93.94  ? 143 PHE B CZ  1 
ATOM   2655  N N   . ASN B  1 142 ? 148.940 179.049 162.811 1.00 97.75  ? 144 ASN B N   1 
ATOM   2656  C CA  . ASN B  1 142 ? 147.893 179.914 162.277 1.00 96.17  ? 144 ASN B CA  1 
ATOM   2657  C C   . ASN B  1 142 ? 148.412 180.710 161.085 1.00 97.13  ? 144 ASN B C   1 
ATOM   2658  O O   . ASN B  1 142 ? 147.910 180.571 159.966 1.00 101.80 ? 144 ASN B O   1 
ATOM   2659  C CB  . ASN B  1 142 ? 147.367 180.847 163.369 1.00 102.74 ? 144 ASN B CB  1 
ATOM   2660  C CG  . ASN B  1 142 ? 148.463 181.351 164.280 1.00 108.47 ? 144 ASN B CG  1 
ATOM   2661  O OD1 . ASN B  1 142 ? 149.615 181.486 163.868 1.00 109.09 ? 144 ASN B OD1 1 
ATOM   2662  N ND2 . ASN B  1 142 ? 148.112 181.635 165.528 1.00 113.30 ? 144 ASN B ND2 1 
ATOM   2663  N N   . GLY B  1 143 ? 149.409 181.559 161.314 1.00 99.08  ? 145 GLY B N   1 
ATOM   2664  C CA  . GLY B  1 143 ? 150.173 182.153 160.235 1.00 99.51  ? 145 GLY B CA  1 
ATOM   2665  C C   . GLY B  1 143 ? 151.655 182.036 160.518 1.00 101.63 ? 145 GLY B C   1 
ATOM   2666  O O   . GLY B  1 143 ? 152.494 182.204 159.628 1.00 101.54 ? 145 GLY B O   1 
ATOM   2667  N N   . GLN B  1 144 ? 151.978 181.744 161.776 1.00 102.03 ? 146 GLN B N   1 
ATOM   2668  C CA  . GLN B  1 144 ? 153.335 181.467 162.219 1.00 97.64  ? 146 GLN B CA  1 
ATOM   2669  C C   . GLN B  1 144 ? 153.290 180.329 163.226 1.00 94.82  ? 146 GLN B C   1 
ATOM   2670  O O   . GLN B  1 144 ? 152.255 180.057 163.837 1.00 100.07 ? 146 GLN B O   1 
ATOM   2671  C CB  . GLN B  1 144 ? 154.013 182.693 162.852 1.00 98.49  ? 146 GLN B CB  1 
ATOM   2672  C CG  . GLN B  1 144 ? 153.639 184.026 162.240 1.00 104.79 ? 146 GLN B CG  1 
ATOM   2673  C CD  . GLN B  1 144 ? 154.623 184.456 161.174 1.00 111.41 ? 146 GLN B CD  1 
ATOM   2674  O OE1 . GLN B  1 144 ? 155.769 184.009 161.157 1.00 109.26 ? 146 GLN B OE1 1 
ATOM   2675  N NE2 . GLN B  1 144 ? 154.181 185.323 160.274 1.00 113.41 ? 146 GLN B NE2 1 
ATOM   2676  N N   . TYR B  1 145 ? 154.427 179.662 163.390 1.00 90.21  ? 147 TYR B N   1 
ATOM   2677  C CA  . TYR B  1 145 ? 154.519 178.572 164.350 1.00 90.51  ? 147 TYR B CA  1 
ATOM   2678  C C   . TYR B  1 145 ? 154.393 179.125 165.764 1.00 95.15  ? 147 TYR B C   1 
ATOM   2679  O O   . TYR B  1 145 ? 155.239 179.906 166.211 1.00 103.36 ? 147 TYR B O   1 
ATOM   2680  C CB  . TYR B  1 145 ? 155.837 177.825 164.176 1.00 87.09  ? 147 TYR B CB  1 
ATOM   2681  C CG  . TYR B  1 145 ? 155.911 177.031 162.895 1.00 88.68  ? 147 TYR B CG  1 
ATOM   2682  C CD1 . TYR B  1 145 ? 155.330 175.775 162.800 1.00 88.83  ? 147 TYR B CD1 1 
ATOM   2683  C CD2 . TYR B  1 145 ? 156.557 177.539 161.779 1.00 89.02  ? 147 TYR B CD2 1 
ATOM   2684  C CE1 . TYR B  1 145 ? 155.392 175.047 161.631 1.00 91.12  ? 147 TYR B CE1 1 
ATOM   2685  C CE2 . TYR B  1 145 ? 156.625 176.819 160.605 1.00 90.62  ? 147 TYR B CE2 1 
ATOM   2686  C CZ  . TYR B  1 145 ? 156.042 175.573 160.537 1.00 95.35  ? 147 TYR B CZ  1 
ATOM   2687  O OH  . TYR B  1 145 ? 156.109 174.852 159.368 1.00 99.22  ? 147 TYR B OH  1 
ATOM   2688  N N   . GLN B  1 146 ? 153.334 178.725 166.463 1.00 94.35  ? 148 GLN B N   1 
ATOM   2689  C CA  . GLN B  1 146 ? 153.097 179.191 167.821 1.00 94.66  ? 148 GLN B CA  1 
ATOM   2690  C C   . GLN B  1 146 ? 153.833 178.371 168.868 1.00 97.09  ? 148 GLN B C   1 
ATOM   2691  O O   . GLN B  1 146 ? 154.094 178.881 169.963 1.00 96.21  ? 148 GLN B O   1 
ATOM   2692  C CB  . GLN B  1 146 ? 151.597 179.180 168.126 1.00 97.14  ? 148 GLN B CB  1 
ATOM   2693  C CG  . GLN B  1 146 ? 150.761 179.898 167.086 1.00 104.27 ? 148 GLN B CG  1 
ATOM   2694  C CD  . GLN B  1 146 ? 150.980 181.396 167.109 1.00 111.49 ? 148 GLN B CD  1 
ATOM   2695  O OE1 . GLN B  1 146 ? 151.076 182.003 168.175 1.00 111.34 ? 148 GLN B OE1 1 
ATOM   2696  N NE2 . GLN B  1 146 ? 151.070 182.000 165.931 1.00 114.74 ? 148 GLN B NE2 1 
ATOM   2697  N N   . TYR B  1 147 ? 154.172 177.121 168.562 1.00 97.27  ? 149 TYR B N   1 
ATOM   2698  C CA  . TYR B  1 147 ? 154.891 176.251 169.483 1.00 101.02 ? 149 TYR B CA  1 
ATOM   2699  C C   . TYR B  1 147 ? 156.131 175.732 168.773 1.00 99.65  ? 149 TYR B C   1 
ATOM   2700  O O   . TYR B  1 147 ? 156.021 175.074 167.734 1.00 99.50  ? 149 TYR B O   1 
ATOM   2701  C CB  . TYR B  1 147 ? 154.002 175.095 169.946 1.00 98.74  ? 149 TYR B CB  1 
ATOM   2702  C CG  . TYR B  1 147 ? 152.703 175.553 170.567 1.00 96.34  ? 149 TYR B CG  1 
ATOM   2703  C CD1 . TYR B  1 147 ? 152.676 176.112 171.835 1.00 95.99  ? 149 TYR B CD1 1 
ATOM   2704  C CD2 . TYR B  1 147 ? 151.506 175.440 169.876 1.00 95.60  ? 149 TYR B CD2 1 
ATOM   2705  C CE1 . TYR B  1 147 ? 151.491 176.537 172.402 1.00 101.27 ? 149 TYR B CE1 1 
ATOM   2706  C CE2 . TYR B  1 147 ? 150.318 175.861 170.433 1.00 99.02  ? 149 TYR B CE2 1 
ATOM   2707  C CZ  . TYR B  1 147 ? 150.316 176.409 171.696 1.00 104.08 ? 149 TYR B CZ  1 
ATOM   2708  O OH  . TYR B  1 147 ? 149.133 176.831 172.255 1.00 107.11 ? 149 TYR B OH  1 
ATOM   2709  N N   . LYS B  1 148 ? 157.304 176.025 169.330 1.00 95.68  ? 150 LYS B N   1 
ATOM   2710  C CA  . LYS B  1 148 ? 158.561 175.679 168.686 1.00 94.95  ? 150 LYS B CA  1 
ATOM   2711  C C   . LYS B  1 148 ? 159.554 175.171 169.720 1.00 96.65  ? 150 LYS B C   1 
ATOM   2712  O O   . LYS B  1 148 ? 159.449 175.460 170.913 1.00 97.74  ? 150 LYS B O   1 
ATOM   2713  C CB  . LYS B  1 148 ? 159.163 176.875 167.940 1.00 95.57  ? 150 LYS B CB  1 
ATOM   2714  C CG  . LYS B  1 148 ? 158.577 178.215 168.336 1.00 93.53  ? 150 LYS B CG  1 
ATOM   2715  C CD  . LYS B  1 148 ? 159.029 179.303 167.383 1.00 98.17  ? 150 LYS B CD  1 
ATOM   2716  C CE  . LYS B  1 148 ? 158.202 180.563 167.544 1.00 111.04 ? 150 LYS B CE  1 
ATOM   2717  N NZ  . LYS B  1 148 ? 158.515 181.555 166.481 1.00 111.12 ? 150 LYS B NZ  1 
ATOM   2718  N N   . ASN B  1 149 ? 160.528 174.402 169.237 1.00 93.73  ? 151 ASN B N   1 
ATOM   2719  C CA  . ASN B  1 149 ? 161.633 173.908 170.054 1.00 88.36  ? 151 ASN B CA  1 
ATOM   2720  C C   . ASN B  1 149 ? 162.844 174.784 169.764 1.00 93.11  ? 151 ASN B C   1 
ATOM   2721  O O   . ASN B  1 149 ? 163.465 174.672 168.704 1.00 97.93  ? 151 ASN B O   1 
ATOM   2722  C CB  . ASN B  1 149 ? 161.926 172.444 169.747 1.00 88.93  ? 151 ASN B CB  1 
ATOM   2723  C CG  . ASN B  1 149 ? 162.850 171.809 170.765 1.00 93.46  ? 151 ASN B CG  1 
ATOM   2724  O OD1 . ASN B  1 149 ? 163.459 172.495 171.585 1.00 100.63 ? 151 ASN B OD1 1 
ATOM   2725  N ND2 . ASN B  1 149 ? 162.957 170.487 170.720 1.00 92.25  ? 151 ASN B ND2 1 
ATOM   2726  N N   . GLU B  1 150 ? 163.183 175.656 170.709 1.00 92.40  ? 152 GLU B N   1 
ATOM   2727  C CA  . GLU B  1 150 ? 164.307 176.566 170.557 1.00 97.44  ? 152 GLU B CA  1 
ATOM   2728  C C   . GLU B  1 150 ? 165.503 176.168 171.410 1.00 99.06  ? 152 GLU B C   1 
ATOM   2729  O O   . GLU B  1 150 ? 166.507 176.887 171.425 1.00 106.16 ? 152 GLU B O   1 
ATOM   2730  C CB  . GLU B  1 150 ? 163.873 177.992 170.892 1.00 102.30 ? 152 GLU B CB  1 
ATOM   2731  C CG  . GLU B  1 150 ? 162.698 178.480 170.066 1.00 105.22 ? 152 GLU B CG  1 
ATOM   2732  C CD  . GLU B  1 150 ? 162.563 179.987 170.080 1.00 119.56 ? 152 GLU B CD  1 
ATOM   2733  O OE1 . GLU B  1 150 ? 161.842 180.512 170.954 1.00 121.00 ? 152 GLU B OE1 1 
ATOM   2734  O OE2 . GLU B  1 150 ? 163.176 180.648 169.217 1.00 130.65 ? 152 GLU B OE2 1 
ATOM   2735  N N   . GLY B  1 151 ? 165.422 175.046 172.115 1.00 94.75  ? 153 GLY B N   1 
ATOM   2736  C CA  . GLY B  1 151 ? 166.496 174.591 172.973 1.00 97.92  ? 153 GLY B CA  1 
ATOM   2737  C C   . GLY B  1 151 ? 167.396 173.585 172.281 1.00 101.11 ? 153 GLY B C   1 
ATOM   2738  O O   . GLY B  1 151 ? 166.984 172.892 171.355 1.00 108.12 ? 153 GLY B O   1 
ATOM   2739  N N   . ASN B  1 152 ? 168.640 173.516 172.744 1.00 100.60 ? 154 ASN B N   1 
ATOM   2740  C CA  . ASN B  1 152 ? 169.614 172.581 172.204 1.00 94.95  ? 154 ASN B CA  1 
ATOM   2741  C C   . ASN B  1 152 ? 169.582 171.278 172.989 1.00 98.91  ? 154 ASN B C   1 
ATOM   2742  O O   . ASN B  1 152 ? 169.387 171.279 174.207 1.00 104.99 ? 154 ASN B O   1 
ATOM   2743  C CB  . ASN B  1 152 ? 171.018 173.180 172.249 1.00 96.16  ? 154 ASN B CB  1 
ATOM   2744  C CG  . ASN B  1 152 ? 171.138 174.436 171.418 1.00 104.70 ? 154 ASN B CG  1 
ATOM   2745  O OD1 . ASN B  1 152 ? 170.303 174.702 170.555 1.00 106.81 ? 154 ASN B OD1 1 
ATOM   2746  N ND2 . ASN B  1 152 ? 172.177 175.218 171.674 1.00 112.18 ? 154 ASN B ND2 1 
ATOM   2747  N N   . ASN B  1 153 ? 169.775 170.167 172.277 1.00 93.99  ? 155 ASN B N   1 
ATOM   2748  C CA  . ASN B  1 153 ? 169.806 168.838 172.887 1.00 93.55  ? 155 ASN B CA  1 
ATOM   2749  C C   . ASN B  1 153 ? 168.535 168.569 173.688 1.00 95.14  ? 155 ASN B C   1 
ATOM   2750  O O   . ASN B  1 153 ? 168.569 167.984 174.772 1.00 101.60 ? 155 ASN B O   1 
ATOM   2751  C CB  . ASN B  1 153 ? 171.047 168.670 173.764 1.00 95.58  ? 155 ASN B CB  1 
ATOM   2752  C CG  . ASN B  1 153 ? 172.335 168.846 172.989 1.00 101.35 ? 155 ASN B CG  1 
ATOM   2753  O OD1 . ASN B  1 153 ? 172.794 167.931 172.309 1.00 104.69 ? 155 ASN B OD1 1 
ATOM   2754  N ND2 . ASN B  1 153 ? 172.924 170.032 173.085 1.00 101.67 ? 155 ASN B ND2 1 
ATOM   2755  N N   . SER B  1 154 ? 167.399 169.000 173.147 1.00 90.11  ? 156 SER B N   1 
ATOM   2756  C CA  . SER B  1 154 ? 166.121 168.899 173.832 1.00 87.88  ? 156 SER B CA  1 
ATOM   2757  C C   . SER B  1 154 ? 165.103 168.223 172.927 1.00 86.50  ? 156 SER B C   1 
ATOM   2758  O O   . SER B  1 154 ? 165.118 168.403 171.708 1.00 89.27  ? 156 SER B O   1 
ATOM   2759  C CB  . SER B  1 154 ? 165.611 170.281 174.259 1.00 93.41  ? 156 SER B CB  1 
ATOM   2760  O OG  . SER B  1 154 ? 165.596 171.178 173.165 1.00 104.80 ? 156 SER B OG  1 
ATOM   2761  N N   . TYR B  1 155 ? 164.213 167.441 173.536 1.00 82.29  ? 157 TYR B N   1 
ATOM   2762  C CA  . TYR B  1 155 ? 163.238 166.662 172.786 1.00 76.27  ? 157 TYR B CA  1 
ATOM   2763  C C   . TYR B  1 155 ? 161.858 166.800 173.409 1.00 76.85  ? 157 TYR B C   1 
ATOM   2764  O O   . TYR B  1 155 ? 161.717 166.841 174.634 1.00 85.33  ? 157 TYR B O   1 
ATOM   2765  C CB  . TYR B  1 155 ? 163.641 165.186 172.720 1.00 76.37  ? 157 TYR B CB  1 
ATOM   2766  C CG  . TYR B  1 155 ? 164.753 164.923 171.734 1.00 78.33  ? 157 TYR B CG  1 
ATOM   2767  C CD1 . TYR B  1 155 ? 166.077 165.140 172.081 1.00 77.80  ? 157 TYR B CD1 1 
ATOM   2768  C CD2 . TYR B  1 155 ? 164.476 164.466 170.455 1.00 79.91  ? 157 TYR B CD2 1 
ATOM   2769  C CE1 . TYR B  1 155 ? 167.094 164.908 171.182 1.00 86.61  ? 157 TYR B CE1 1 
ATOM   2770  C CE2 . TYR B  1 155 ? 165.488 164.231 169.549 1.00 84.40  ? 157 TYR B CE2 1 
ATOM   2771  C CZ  . TYR B  1 155 ? 166.795 164.453 169.919 1.00 91.18  ? 157 TYR B CZ  1 
ATOM   2772  O OH  . TYR B  1 155 ? 167.808 164.221 169.021 1.00 97.10  ? 157 TYR B OH  1 
ATOM   2773  N N   . MET B  1 156 ? 160.846 166.871 172.549 1.00 76.92  ? 158 MET B N   1 
ATOM   2774  C CA  . MET B  1 156 ? 159.456 167.027 172.949 1.00 76.51  ? 158 MET B CA  1 
ATOM   2775  C C   . MET B  1 156 ? 158.618 165.943 172.295 1.00 79.08  ? 158 MET B C   1 
ATOM   2776  O O   . MET B  1 156 ? 158.716 165.727 171.083 1.00 82.30  ? 158 MET B O   1 
ATOM   2777  C CB  . MET B  1 156 ? 158.927 168.404 172.548 1.00 75.78  ? 158 MET B CB  1 
ATOM   2778  C CG  . MET B  1 156 ? 159.941 169.519 172.684 1.00 89.02  ? 158 MET B CG  1 
ATOM   2779  S SD  . MET B  1 156 ? 159.582 170.914 171.609 1.00 123.48 ? 158 MET B SD  1 
ATOM   2780  C CE  . MET B  1 156 ? 157.805 170.878 171.560 1.00 97.50  ? 158 MET B CE  1 
ATOM   2781  N N   . ILE B  1 157 ? 157.798 165.264 173.092 1.00 77.51  ? 159 ILE B N   1 
ATOM   2782  C CA  . ILE B  1 157 ? 156.831 164.296 172.591 1.00 75.15  ? 159 ILE B CA  1 
ATOM   2783  C C   . ILE B  1 157 ? 155.489 164.656 173.210 1.00 82.73  ? 159 ILE B C   1 
ATOM   2784  O O   . ILE B  1 157 ? 155.290 164.472 174.417 1.00 87.74  ? 159 ILE B O   1 
ATOM   2785  C CB  . ILE B  1 157 ? 157.221 162.849 172.923 1.00 72.80  ? 159 ILE B CB  1 
ATOM   2786  C CG1 . ILE B  1 157 ? 158.437 162.420 172.101 1.00 70.31  ? 159 ILE B CG1 1 
ATOM   2787  C CG2 . ILE B  1 157 ? 156.054 161.911 172.658 1.00 75.09  ? 159 ILE B CG2 1 
ATOM   2788  C CD1 . ILE B  1 157 ? 159.758 162.613 172.815 1.00 70.65  ? 159 ILE B CD1 1 
ATOM   2789  N N   . GLY B  1 158 ? 154.581 165.174 172.401 1.00 77.99  ? 160 GLY B N   1 
ATOM   2790  C CA  . GLY B  1 158 ? 153.286 165.595 172.888 1.00 80.06  ? 160 GLY B CA  1 
ATOM   2791  C C   . GLY B  1 158 ? 152.711 166.677 171.998 1.00 83.85  ? 160 GLY B C   1 
ATOM   2792  O O   . GLY B  1 158 ? 153.198 166.932 170.902 1.00 87.15  ? 160 GLY B O   1 
ATOM   2793  N N   . ASN B  1 159 ? 151.659 167.315 172.503 1.00 86.23  ? 161 ASN B N   1 
ATOM   2794  C CA  . ASN B  1 159 ? 150.907 168.312 171.756 1.00 86.41  ? 161 ASN B CA  1 
ATOM   2795  C C   . ASN B  1 159 ? 151.108 169.689 172.371 1.00 90.57  ? 161 ASN B C   1 
ATOM   2796  O O   . ASN B  1 159 ? 151.011 169.846 173.592 1.00 94.94  ? 161 ASN B O   1 
ATOM   2797  C CB  . ASN B  1 159 ? 149.418 167.966 171.732 1.00 87.15  ? 161 ASN B CB  1 
ATOM   2798  C CG  . ASN B  1 159 ? 149.108 166.795 170.829 1.00 96.43  ? 161 ASN B CG  1 
ATOM   2799  O OD1 . ASN B  1 159 ? 149.844 166.512 169.886 1.00 101.86 ? 161 ASN B OD1 1 
ATOM   2800  N ND2 . ASN B  1 159 ? 148.011 166.104 171.113 1.00 100.05 ? 161 ASN B ND2 1 
ATOM   2801  N N   . LYS B  1 160 ? 151.383 170.677 171.522 1.00 87.74  ? 162 LYS B N   1 
ATOM   2802  C CA  . LYS B  1 160 ? 151.427 172.085 171.911 1.00 90.22  ? 162 LYS B CA  1 
ATOM   2803  C C   . LYS B  1 160 ? 152.401 172.315 173.066 1.00 93.05  ? 162 LYS B C   1 
ATOM   2804  O O   . LYS B  1 160 ? 152.036 172.779 174.146 1.00 98.19  ? 162 LYS B O   1 
ATOM   2805  C CB  . LYS B  1 160 ? 150.025 172.589 172.264 1.00 90.76  ? 162 LYS B CB  1 
ATOM   2806  C CG  . LYS B  1 160 ? 148.922 172.013 171.390 1.00 90.58  ? 162 LYS B CG  1 
ATOM   2807  C CD  . LYS B  1 160 ? 147.977 173.092 170.899 1.00 96.49  ? 162 LYS B CD  1 
ATOM   2808  C CE  . LYS B  1 160 ? 146.861 173.334 171.899 1.00 99.63  ? 162 LYS B CE  1 
ATOM   2809  N NZ  . LYS B  1 160 ? 145.734 174.095 171.295 1.00 107.88 ? 162 LYS B NZ  1 
ATOM   2810  N N   . ASN B  1 161 ? 153.663 171.985 172.816 1.00 86.86  ? 163 ASN B N   1 
ATOM   2811  C CA  . ASN B  1 161 ? 154.717 172.118 173.807 1.00 87.21  ? 163 ASN B CA  1 
ATOM   2812  C C   . ASN B  1 161 ? 155.703 173.188 173.358 1.00 93.82  ? 163 ASN B C   1 
ATOM   2813  O O   . ASN B  1 161 ? 155.946 173.366 172.162 1.00 100.13 ? 163 ASN B O   1 
ATOM   2814  C CB  . ASN B  1 161 ? 155.442 170.789 174.022 1.00 86.80  ? 163 ASN B CB  1 
ATOM   2815  C CG  . ASN B  1 161 ? 154.628 169.804 174.827 1.00 93.08  ? 163 ASN B CG  1 
ATOM   2816  O OD1 . ASN B  1 161 ? 153.657 170.173 175.485 1.00 98.84  ? 163 ASN B OD1 1 
ATOM   2817  N ND2 . ASN B  1 161 ? 155.011 168.536 174.767 1.00 93.16  ? 163 ASN B ND2 1 
ATOM   2818  N N   . LYS B  1 162 ? 156.258 173.913 174.325 1.00 95.26  ? 164 LYS B N   1 
ATOM   2819  C CA  . LYS B  1 162 ? 157.160 175.020 174.043 1.00 91.21  ? 164 LYS B CA  1 
ATOM   2820  C C   . LYS B  1 162 ? 158.431 174.895 174.868 1.00 93.23  ? 164 LYS B C   1 
ATOM   2821  O O   . LYS B  1 162 ? 158.385 174.543 176.050 1.00 99.05  ? 164 LYS B O   1 
ATOM   2822  C CB  . LYS B  1 162 ? 156.490 176.365 174.336 1.00 92.62  ? 164 LYS B CB  1 
ATOM   2823  C CG  . LYS B  1 162 ? 155.874 177.028 173.121 1.00 94.92  ? 164 LYS B CG  1 
ATOM   2824  C CD  . LYS B  1 162 ? 155.688 178.516 173.348 1.00 94.24  ? 164 LYS B CD  1 
ATOM   2825  C CE  . LYS B  1 162 ? 154.672 178.777 174.446 1.00 98.27  ? 164 LYS B CE  1 
ATOM   2826  N NZ  . LYS B  1 162 ? 153.693 179.829 174.061 1.00 99.09  ? 164 LYS B NZ  1 
ATOM   2827  N N   . ILE B  1 163 ? 159.566 175.184 174.235 1.00 88.75  ? 165 ILE B N   1 
ATOM   2828  C CA  . ILE B  1 163 ? 160.852 175.291 174.913 1.00 93.51  ? 165 ILE B CA  1 
ATOM   2829  C C   . ILE B  1 163 ? 161.490 176.604 174.486 1.00 102.24 ? 165 ILE B C   1 
ATOM   2830  O O   . ILE B  1 163 ? 161.761 176.808 173.297 1.00 107.47 ? 165 ILE B O   1 
ATOM   2831  C CB  . ILE B  1 163 ? 161.781 174.109 174.595 1.00 90.50  ? 165 ILE B CB  1 
ATOM   2832  C CG1 . ILE B  1 163 ? 161.136 172.791 175.027 1.00 92.23  ? 165 ILE B CG1 1 
ATOM   2833  C CG2 . ILE B  1 163 ? 163.125 174.298 175.276 1.00 93.11  ? 165 ILE B CG2 1 
ATOM   2834  C CD1 . ILE B  1 163 ? 162.103 171.632 175.107 1.00 90.48  ? 165 ILE B CD1 1 
ATOM   2835  N N   . ALA B  1 164 ? 161.729 177.489 175.449 1.00 105.61 ? 166 ALA B N   1 
ATOM   2836  C CA  . ALA B  1 164 ? 162.276 178.799 175.143 1.00 107.81 ? 166 ALA B CA  1 
ATOM   2837  C C   . ALA B  1 164 ? 163.756 178.699 174.785 1.00 111.54 ? 166 ALA B C   1 
ATOM   2838  O O   . ALA B  1 164 ? 164.448 177.740 175.134 1.00 114.59 ? 166 ALA B O   1 
ATOM   2839  C CB  . ALA B  1 164 ? 162.087 179.750 176.324 1.00 107.48 ? 166 ALA B CB  1 
ATOM   2840  N N   . SER B  1 165 ? 164.235 179.713 174.070 1.00 112.84 ? 167 SER B N   1 
ATOM   2841  C CA  . SER B  1 165 ? 165.641 179.768 173.698 1.00 116.56 ? 167 SER B CA  1 
ATOM   2842  C C   . SER B  1 165 ? 166.511 179.956 174.934 1.00 120.63 ? 167 SER B C   1 
ATOM   2843  O O   . SER B  1 165 ? 166.172 180.718 175.843 1.00 120.89 ? 167 SER B O   1 
ATOM   2844  C CB  . SER B  1 165 ? 165.884 180.903 172.705 1.00 117.17 ? 167 SER B CB  1 
ATOM   2845  O OG  . SER B  1 165 ? 167.138 180.756 172.063 1.00 120.79 ? 167 SER B OG  1 
ATOM   2846  N N   . GLY B  1 166 ? 167.642 179.256 174.962 1.00 118.02 ? 168 GLY B N   1 
ATOM   2847  C CA  . GLY B  1 166 ? 168.537 179.272 176.097 1.00 119.39 ? 168 GLY B CA  1 
ATOM   2848  C C   . GLY B  1 166 ? 168.272 178.196 177.127 1.00 118.86 ? 168 GLY B C   1 
ATOM   2849  O O   . GLY B  1 166 ? 169.072 178.042 178.057 1.00 116.86 ? 168 GLY B O   1 
ATOM   2850  N N   . SER B  1 167 ? 167.177 177.452 176.992 1.00 116.20 ? 169 SER B N   1 
ATOM   2851  C CA  . SER B  1 167 ? 166.865 176.333 177.872 1.00 109.32 ? 169 SER B CA  1 
ATOM   2852  C C   . SER B  1 167 ? 167.219 175.047 177.134 1.00 111.53 ? 169 SER B C   1 
ATOM   2853  O O   . SER B  1 167 ? 166.545 174.675 176.169 1.00 117.40 ? 169 SER B O   1 
ATOM   2854  C CB  . SER B  1 167 ? 165.394 176.354 178.277 1.00 108.00 ? 169 SER B CB  1 
ATOM   2855  O OG  . SER B  1 167 ? 165.090 177.516 179.027 1.00 113.85 ? 169 SER B OG  1 
ATOM   2856  N N   . ASP B  1 168 ? 168.266 174.370 177.590 1.00 108.45 ? 170 ASP B N   1 
ATOM   2857  C CA  . ASP B  1 168 ? 168.833 173.235 176.880 1.00 108.55 ? 170 ASP B CA  1 
ATOM   2858  C C   . ASP B  1 168 ? 168.756 171.975 177.735 1.00 108.79 ? 170 ASP B C   1 
ATOM   2859  O O   . ASP B  1 168 ? 168.555 172.029 178.950 1.00 108.86 ? 170 ASP B O   1 
ATOM   2860  C CB  . ASP B  1 168 ? 170.286 173.517 176.479 1.00 114.85 ? 170 ASP B CB  1 
ATOM   2861  C CG  . ASP B  1 168 ? 170.448 174.854 175.788 1.00 120.99 ? 170 ASP B CG  1 
ATOM   2862  O OD1 . ASP B  1 168 ? 169.632 175.165 174.895 1.00 120.72 ? 170 ASP B OD1 1 
ATOM   2863  O OD2 . ASP B  1 168 ? 171.390 175.595 176.138 1.00 124.46 ? 170 ASP B OD2 1 
ATOM   2864  N N   . ASP B  1 169 ? 168.926 170.832 177.069 1.00 109.11 ? 171 ASP B N   1 
ATOM   2865  C CA  . ASP B  1 169 ? 168.892 169.515 177.707 1.00 107.70 ? 171 ASP B CA  1 
ATOM   2866  C C   . ASP B  1 169 ? 167.597 169.305 178.488 1.00 104.65 ? 171 ASP B C   1 
ATOM   2867  O O   . ASP B  1 169 ? 167.596 168.848 179.632 1.00 108.62 ? 171 ASP B O   1 
ATOM   2868  C CB  . ASP B  1 169 ? 170.111 169.304 178.606 1.00 116.52 ? 171 ASP B CB  1 
ATOM   2869  C CG  . ASP B  1 169 ? 171.410 169.700 177.935 1.00 125.43 ? 171 ASP B CG  1 
ATOM   2870  O OD1 . ASP B  1 169 ? 171.587 170.896 177.628 1.00 124.78 ? 171 ASP B OD1 1 
ATOM   2871  O OD2 . ASP B  1 169 ? 172.258 168.812 177.712 1.00 130.71 ? 171 ASP B OD2 1 
ATOM   2872  N N   . ASN B  1 170 ? 166.479 169.639 177.852 1.00 97.85  ? 172 ASN B N   1 
ATOM   2873  C CA  . ASN B  1 170 ? 165.161 169.482 178.448 1.00 92.34  ? 172 ASN B CA  1 
ATOM   2874  C C   . ASN B  1 170 ? 164.373 168.440 177.670 1.00 89.36  ? 172 ASN B C   1 
ATOM   2875  O O   . ASN B  1 170 ? 164.446 168.384 176.441 1.00 93.04  ? 172 ASN B O   1 
ATOM   2876  C CB  . ASN B  1 170 ? 164.401 170.808 178.463 1.00 91.58  ? 172 ASN B CB  1 
ATOM   2877  C CG  . ASN B  1 170 ? 165.088 171.858 179.304 1.00 101.96 ? 172 ASN B CG  1 
ATOM   2878  O OD1 . ASN B  1 170 ? 165.553 171.579 180.407 1.00 103.62 ? 172 ASN B OD1 1 
ATOM   2879  N ND2 . ASN B  1 170 ? 165.162 173.076 178.784 1.00 109.96 ? 172 ASN B ND2 1 
ATOM   2880  N N   . PHE B  1 171 ? 163.620 167.612 178.387 1.00 83.26  ? 173 PHE B N   1 
ATOM   2881  C CA  . PHE B  1 171 ? 162.826 166.564 177.764 1.00 77.64  ? 173 PHE B CA  1 
ATOM   2882  C C   . PHE B  1 171 ? 161.389 166.667 178.241 1.00 80.56  ? 173 PHE B C   1 
ATOM   2883  O O   . PHE B  1 171 ? 161.136 166.798 179.443 1.00 83.40  ? 173 PHE B O   1 
ATOM   2884  C CB  . PHE B  1 171 ? 163.406 165.182 178.068 1.00 75.83  ? 173 PHE B CB  1 
ATOM   2885  C CG  . PHE B  1 171 ? 164.665 164.888 177.312 1.00 82.33  ? 173 PHE B CG  1 
ATOM   2886  C CD1 . PHE B  1 171 ? 165.892 165.299 177.798 1.00 87.64  ? 173 PHE B CD1 1 
ATOM   2887  C CD2 . PHE B  1 171 ? 164.618 164.226 176.099 1.00 86.31  ? 173 PHE B CD2 1 
ATOM   2888  C CE1 . PHE B  1 171 ? 167.050 165.040 177.096 1.00 94.31  ? 173 PHE B CE1 1 
ATOM   2889  C CE2 . PHE B  1 171 ? 165.772 163.965 175.394 1.00 91.73  ? 173 PHE B CE2 1 
ATOM   2890  C CZ  . PHE B  1 171 ? 166.989 164.374 175.891 1.00 94.19  ? 173 PHE B CZ  1 
ATOM   2891  N N   . ILE B  1 172 ? 160.453 166.614 177.299 1.00 79.22  ? 174 ILE B N   1 
ATOM   2892  C CA  . ILE B  1 172 ? 159.033 166.770 177.579 1.00 79.01  ? 174 ILE B CA  1 
ATOM   2893  C C   . ILE B  1 172 ? 158.301 165.538 177.073 1.00 83.37  ? 174 ILE B C   1 
ATOM   2894  O O   . ILE B  1 172 ? 158.481 165.132 175.919 1.00 87.04  ? 174 ILE B O   1 
ATOM   2895  C CB  . ILE B  1 172 ? 158.463 168.041 176.927 1.00 79.77  ? 174 ILE B CB  1 
ATOM   2896  C CG1 . ILE B  1 172 ? 159.316 169.258 177.286 1.00 80.24  ? 174 ILE B CG1 1 
ATOM   2897  C CG2 . ILE B  1 172 ? 157.027 168.248 177.357 1.00 81.67  ? 174 ILE B CG2 1 
ATOM   2898  C CD1 . ILE B  1 172 ? 158.670 170.580 176.941 1.00 89.57  ? 174 ILE B CD1 1 
ATOM   2899  N N   . LEU B  1 173 ? 157.479 164.945 177.937 1.00 81.12  ? 175 LEU B N   1 
ATOM   2900  C CA  . LEU B  1 173 ? 156.572 163.858 177.568 1.00 82.86  ? 175 LEU B CA  1 
ATOM   2901  C C   . LEU B  1 173 ? 155.195 164.249 178.095 1.00 87.85  ? 175 LEU B C   1 
ATOM   2902  O O   . LEU B  1 173 ? 154.786 163.833 179.180 1.00 92.65  ? 175 LEU B O   1 
ATOM   2903  C CB  . LEU B  1 173 ? 157.047 162.521 178.128 1.00 83.23  ? 175 LEU B CB  1 
ATOM   2904  C CG  . LEU B  1 173 ? 156.349 161.276 177.582 1.00 80.59  ? 175 LEU B CG  1 
ATOM   2905  C CD1 . LEU B  1 173 ? 156.788 161.002 176.157 1.00 78.53  ? 175 LEU B CD1 1 
ATOM   2906  C CD2 . LEU B  1 173 ? 156.629 160.074 178.466 1.00 86.42  ? 175 LEU B CD2 1 
ATOM   2907  N N   . GLY B  1 174 ? 154.483 165.053 177.317 1.00 85.05  ? 176 GLY B N   1 
ATOM   2908  C CA  . GLY B  1 174 ? 153.195 165.556 177.744 1.00 87.98  ? 176 GLY B CA  1 
ATOM   2909  C C   . GLY B  1 174 ? 152.711 166.636 176.803 1.00 92.82  ? 176 GLY B C   1 
ATOM   2910  O O   . GLY B  1 174 ? 153.353 166.957 175.799 1.00 98.38  ? 176 GLY B O   1 
ATOM   2911  N N   . ASN B  1 175 ? 151.558 167.197 177.153 1.00 89.31  ? 177 ASN B N   1 
ATOM   2912  C CA  . ASN B  1 175 ? 150.933 168.249 176.370 1.00 85.97  ? 177 ASN B CA  1 
ATOM   2913  C C   . ASN B  1 175 ? 150.904 169.550 177.158 1.00 91.92  ? 177 ASN B C   1 
ATOM   2914  O O   . ASN B  1 175 ? 150.895 169.549 178.392 1.00 97.86  ? 177 ASN B O   1 
ATOM   2915  C CB  . ASN B  1 175 ? 149.506 167.869 175.966 1.00 84.70  ? 177 ASN B CB  1 
ATOM   2916  C CG  . ASN B  1 175 ? 149.414 166.475 175.392 1.00 89.09  ? 177 ASN B CG  1 
ATOM   2917  O OD1 . ASN B  1 175 ? 150.131 166.128 174.455 1.00 99.07  ? 177 ASN B OD1 1 
ATOM   2918  N ND2 . ASN B  1 175 ? 148.526 165.663 175.952 1.00 89.40  ? 177 ASN B ND2 1 
ATOM   2919  N N   . ASN B  1 176 ? 150.887 170.662 176.422 1.00 90.41  ? 178 ASN B N   1 
ATOM   2920  C CA  . ASN B  1 176 ? 150.738 171.999 176.998 1.00 95.22  ? 178 ASN B CA  1 
ATOM   2921  C C   . ASN B  1 176 ? 151.817 172.290 178.037 1.00 95.01  ? 178 ASN B C   1 
ATOM   2922  O O   . ASN B  1 176 ? 151.558 172.905 179.073 1.00 99.68  ? 178 ASN B O   1 
ATOM   2923  C CB  . ASN B  1 176 ? 149.345 172.184 177.600 1.00 94.72  ? 178 ASN B CB  1 
ATOM   2924  C CG  . ASN B  1 176 ? 148.242 171.887 176.609 1.00 95.43  ? 178 ASN B CG  1 
ATOM   2925  O OD1 . ASN B  1 176 ? 148.131 172.541 175.573 1.00 100.77 ? 178 ASN B OD1 1 
ATOM   2926  N ND2 . ASN B  1 176 ? 147.417 170.897 176.922 1.00 93.61  ? 178 ASN B ND2 1 
ATOM   2927  N N   . VAL B  1 177 ? 153.038 171.846 177.761 1.00 87.87  ? 179 VAL B N   1 
ATOM   2928  C CA  . VAL B  1 177 ? 154.172 172.078 178.645 1.00 88.52  ? 179 VAL B CA  1 
ATOM   2929  C C   . VAL B  1 177 ? 155.035 173.169 178.031 1.00 94.60  ? 179 VAL B C   1 
ATOM   2930  O O   . VAL B  1 177 ? 155.638 172.972 176.969 1.00 96.28  ? 179 VAL B O   1 
ATOM   2931  C CB  . VAL B  1 177 ? 154.983 170.794 178.870 1.00 86.67  ? 179 VAL B CB  1 
ATOM   2932  C CG1 . VAL B  1 177 ? 156.196 171.085 179.734 1.00 89.63  ? 179 VAL B CG1 1 
ATOM   2933  C CG2 . VAL B  1 177 ? 154.115 169.723 179.503 1.00 89.67  ? 179 VAL B CG2 1 
ATOM   2934  N N   . HIS B  1 178 ? 155.097 174.318 178.696 1.00 97.63  ? 180 HIS B N   1 
ATOM   2935  C CA  . HIS B  1 178 ? 155.907 175.443 178.254 1.00 97.08  ? 180 HIS B CA  1 
ATOM   2936  C C   . HIS B  1 178 ? 157.077 175.618 179.209 1.00 98.79  ? 180 HIS B C   1 
ATOM   2937  O O   . HIS B  1 178 ? 156.880 175.736 180.423 1.00 105.16 ? 180 HIS B O   1 
ATOM   2938  C CB  . HIS B  1 178 ? 155.078 176.727 178.190 1.00 99.49  ? 180 HIS B CB  1 
ATOM   2939  C CG  . HIS B  1 178 ? 153.754 176.558 177.513 1.00 102.70 ? 180 HIS B CG  1 
ATOM   2940  N ND1 . HIS B  1 178 ? 153.624 176.001 176.260 1.00 102.77 ? 180 HIS B ND1 1 
ATOM   2941  C CD2 . HIS B  1 178 ? 152.500 176.874 177.915 1.00 102.06 ? 180 HIS B CD2 1 
ATOM   2942  C CE1 . HIS B  1 178 ? 152.348 175.980 175.919 1.00 100.47 ? 180 HIS B CE1 1 
ATOM   2943  N NE2 . HIS B  1 178 ? 151.645 176.504 176.906 1.00 105.19 ? 180 HIS B NE2 1 
ATOM   2944  N N   . ILE B  1 179 ? 158.287 175.639 178.661 1.00 96.84  ? 181 ILE B N   1 
ATOM   2945  C CA  . ILE B  1 179 ? 159.508 175.799 179.440 1.00 98.22  ? 181 ILE B CA  1 
ATOM   2946  C C   . ILE B  1 179 ? 160.061 177.186 179.152 1.00 103.46 ? 181 ILE B C   1 
ATOM   2947  O O   . ILE B  1 179 ? 160.317 177.533 177.993 1.00 104.26 ? 181 ILE B O   1 
ATOM   2948  C CB  . ILE B  1 179 ? 160.539 174.711 179.110 1.00 89.03  ? 181 ILE B CB  1 
ATOM   2949  C CG1 . ILE B  1 179 ? 159.965 173.327 179.416 1.00 88.52  ? 181 ILE B CG1 1 
ATOM   2950  C CG2 . ILE B  1 179 ? 161.822 174.943 179.889 1.00 94.99  ? 181 ILE B CG2 1 
ATOM   2951  C CD1 . ILE B  1 179 ? 160.995 172.221 179.419 1.00 89.16  ? 181 ILE B CD1 1 
ATOM   2952  N N   . GLY B  1 180 ? 160.244 177.978 180.203 1.00 104.84 ? 182 GLY B N   1 
ATOM   2953  C CA  . GLY B  1 180 ? 160.739 179.330 180.066 1.00 106.23 ? 182 GLY B CA  1 
ATOM   2954  C C   . GLY B  1 180 ? 162.242 179.368 179.886 1.00 112.73 ? 182 GLY B C   1 
ATOM   2955  O O   . GLY B  1 180 ? 162.894 178.358 179.609 1.00 118.96 ? 182 GLY B O   1 
ATOM   2956  N N   . GLY B  1 181 ? 162.798 180.564 180.047 1.00 112.58 ? 183 GLY B N   1 
ATOM   2957  C CA  . GLY B  1 181 ? 164.223 180.758 179.890 1.00 115.92 ? 183 GLY B CA  1 
ATOM   2958  C C   . GLY B  1 181 ? 165.010 180.325 181.115 1.00 121.55 ? 183 GLY B C   1 
ATOM   2959  O O   . GLY B  1 181 ? 164.525 180.381 182.241 1.00 119.41 ? 183 GLY B O   1 
ATOM   2960  N N   . GLY B  1 182 ? 166.242 179.892 180.873 1.00 122.18 ? 184 GLY B N   1 
ATOM   2961  C CA  . GLY B  1 182 ? 167.131 179.494 181.951 1.00 119.30 ? 184 GLY B CA  1 
ATOM   2962  C C   . GLY B  1 182 ? 166.681 178.283 182.738 1.00 115.88 ? 184 GLY B C   1 
ATOM   2963  O O   . GLY B  1 182 ? 166.765 178.287 183.972 1.00 115.10 ? 184 GLY B O   1 
ATOM   2964  N N   . ILE B  1 183 ? 166.203 177.244 182.058 1.00 111.73 ? 185 ILE B N   1 
ATOM   2965  C CA  . ILE B  1 183 ? 165.775 176.003 182.696 1.00 107.78 ? 185 ILE B CA  1 
ATOM   2966  C C   . ILE B  1 183 ? 166.461 174.867 181.947 1.00 110.82 ? 185 ILE B C   1 
ATOM   2967  O O   . ILE B  1 183 ? 166.046 174.504 180.841 1.00 116.27 ? 185 ILE B O   1 
ATOM   2968  C CB  . ILE B  1 183 ? 164.253 175.832 182.689 1.00 105.99 ? 185 ILE B CB  1 
ATOM   2969  C CG1 . ILE B  1 183 ? 163.592 176.916 183.539 1.00 107.45 ? 185 ILE B CG1 1 
ATOM   2970  C CG2 . ILE B  1 183 ? 163.870 174.458 183.210 1.00 107.39 ? 185 ILE B CG2 1 
ATOM   2971  C CD1 . ILE B  1 183 ? 162.085 176.904 183.471 1.00 105.95 ? 185 ILE B CD1 1 
ATOM   2972  N N   . ASN B  1 184 ? 167.512 174.310 182.538 1.00 109.88 ? 186 ASN B N   1 
ATOM   2973  C CA  . ASN B  1 184 ? 168.291 173.247 181.923 1.00 105.93 ? 186 ASN B CA  1 
ATOM   2974  C C   . ASN B  1 184 ? 168.156 171.958 182.722 1.00 104.59 ? 186 ASN B C   1 
ATOM   2975  O O   . ASN B  1 184 ? 167.842 171.970 183.915 1.00 105.40 ? 186 ASN B O   1 
ATOM   2976  C CB  . ASN B  1 184 ? 169.772 173.631 181.821 1.00 110.17 ? 186 ASN B CB  1 
ATOM   2977  C CG  . ASN B  1 184 ? 169.987 174.988 181.179 1.00 116.42 ? 186 ASN B CG  1 
ATOM   2978  O OD1 . ASN B  1 184 ? 169.077 175.811 181.112 1.00 115.59 ? 186 ASN B OD1 1 
ATOM   2979  N ND2 . ASN B  1 184 ? 171.201 175.227 180.701 1.00 121.08 ? 186 ASN B ND2 1 
ATOM   2980  N N   . ASN B  1 185 ? 168.399 170.838 182.039 1.00 102.71 ? 187 ASN B N   1 
ATOM   2981  C CA  . ASN B  1 185 ? 168.444 169.516 182.664 1.00 99.80  ? 187 ASN B CA  1 
ATOM   2982  C C   . ASN B  1 185 ? 167.140 169.194 183.392 1.00 101.19 ? 187 ASN B C   1 
ATOM   2983  O O   . ASN B  1 185 ? 167.133 168.801 184.558 1.00 105.15 ? 187 ASN B O   1 
ATOM   2984  C CB  . ASN B  1 185 ? 169.637 169.405 183.617 1.00 97.13  ? 187 ASN B CB  1 
ATOM   2985  C CG  . ASN B  1 185 ? 170.911 169.012 182.908 1.00 107.24 ? 187 ASN B CG  1 
ATOM   2986  O OD1 . ASN B  1 185 ? 171.470 167.945 183.157 1.00 109.46 ? 187 ASN B OD1 1 
ATOM   2987  N ND2 . ASN B  1 185 ? 171.383 169.877 182.020 1.00 114.79 ? 187 ASN B ND2 1 
ATOM   2988  N N   . SER B  1 186 ? 166.023 169.352 182.688 1.00 94.61  ? 188 SER B N   1 
ATOM   2989  C CA  . SER B  1 186 ? 164.712 169.157 183.283 1.00 90.58  ? 188 SER B CA  1 
ATOM   2990  C C   . SER B  1 186 ? 163.893 168.186 182.446 1.00 90.23  ? 188 SER B C   1 
ATOM   2991  O O   . SER B  1 186 ? 164.051 168.104 181.226 1.00 97.95  ? 188 SER B O   1 
ATOM   2992  C CB  . SER B  1 186 ? 163.962 170.482 183.422 1.00 96.27  ? 188 SER B CB  1 
ATOM   2993  O OG  . SER B  1 186 ? 164.525 171.277 184.450 1.00 103.80 ? 188 SER B OG  1 
ATOM   2994  N N   . VAL B  1 187 ? 163.018 167.445 183.122 1.00 83.86  ? 189 VAL B N   1 
ATOM   2995  C CA  . VAL B  1 187 ? 162.125 166.486 182.484 1.00 80.78  ? 189 VAL B CA  1 
ATOM   2996  C C   . VAL B  1 187 ? 160.703 166.784 182.931 1.00 84.62  ? 189 VAL B C   1 
ATOM   2997  O O   . VAL B  1 187 ? 160.447 166.951 184.128 1.00 90.58  ? 189 VAL B O   1 
ATOM   2998  C CB  . VAL B  1 187 ? 162.499 165.031 182.826 1.00 75.40  ? 189 VAL B CB  1 
ATOM   2999  C CG1 . VAL B  1 187 ? 161.758 164.069 181.916 1.00 77.13  ? 189 VAL B CG1 1 
ATOM   3000  C CG2 . VAL B  1 187 ? 163.995 164.826 182.713 1.00 69.30  ? 189 VAL B CG2 1 
ATOM   3001  N N   . ALA B  1 188 ? 159.782 166.851 181.974 1.00 81.44  ? 190 ALA B N   1 
ATOM   3002  C CA  . ALA B  1 188 ? 158.369 167.071 182.249 1.00 81.14  ? 190 ALA B CA  1 
ATOM   3003  C C   . ALA B  1 188 ? 157.574 165.874 181.753 1.00 86.26  ? 190 ALA B C   1 
ATOM   3004  O O   . ALA B  1 188 ? 157.721 165.463 180.598 1.00 89.51  ? 190 ALA B O   1 
ATOM   3005  C CB  . ALA B  1 188 ? 157.867 168.351 181.582 1.00 80.83  ? 190 ALA B CB  1 
ATOM   3006  N N   . LEU B  1 189 ? 156.734 165.322 182.623 1.00 84.86  ? 191 LEU B N   1 
ATOM   3007  C CA  . LEU B  1 189 ? 155.944 164.142 182.310 1.00 82.11  ? 191 LEU B CA  1 
ATOM   3008  C C   . LEU B  1 189 ? 154.464 164.433 182.506 1.00 86.22  ? 191 LEU B C   1 
ATOM   3009  O O   . LEU B  1 189 ? 154.064 165.011 183.521 1.00 89.85  ? 191 LEU B O   1 
ATOM   3010  C CB  . LEU B  1 189 ? 156.353 162.956 183.187 1.00 83.49  ? 191 LEU B CB  1 
ATOM   3011  C CG  . LEU B  1 189 ? 157.811 162.504 183.102 1.00 79.22  ? 191 LEU B CG  1 
ATOM   3012  C CD1 . LEU B  1 189 ? 158.093 161.435 184.142 1.00 83.14  ? 191 LEU B CD1 1 
ATOM   3013  C CD2 . LEU B  1 189 ? 158.133 161.995 181.710 1.00 78.37  ? 191 LEU B CD2 1 
ATOM   3014  N N   . GLY B  1 190 ? 153.656 164.029 181.531 1.00 85.60  ? 192 GLY B N   1 
ATOM   3015  C CA  . GLY B  1 190 ? 152.217 164.052 181.671 1.00 89.78  ? 192 GLY B CA  1 
ATOM   3016  C C   . GLY B  1 190 ? 151.559 165.284 181.078 1.00 94.22  ? 192 GLY B C   1 
ATOM   3017  O O   . GLY B  1 190 ? 152.198 166.283 180.738 1.00 94.21  ? 192 GLY B O   1 
ATOM   3018  N N   . ASN B  1 191 ? 150.238 165.193 180.959 1.00 94.36  ? 193 ASN B N   1 
ATOM   3019  C CA  . ASN B  1 191 ? 149.434 166.293 180.450 1.00 93.31  ? 193 ASN B CA  1 
ATOM   3020  C C   . ASN B  1 191 ? 149.491 167.491 181.390 1.00 97.35  ? 193 ASN B C   1 
ATOM   3021  O O   . ASN B  1 191 ? 149.392 167.347 182.612 1.00 102.79 ? 193 ASN B O   1 
ATOM   3022  C CB  . ASN B  1 191 ? 147.985 165.839 180.273 1.00 95.08  ? 193 ASN B CB  1 
ATOM   3023  C CG  . ASN B  1 191 ? 147.168 166.803 179.444 1.00 103.32 ? 193 ASN B CG  1 
ATOM   3024  O OD1 . ASN B  1 191 ? 147.586 167.224 178.369 1.00 106.40 ? 193 ASN B OD1 1 
ATOM   3025  N ND2 . ASN B  1 191 ? 145.990 167.159 179.943 1.00 103.58 ? 193 ASN B ND2 1 
ATOM   3026  N N   . ASN B  1 192 ? 149.655 168.679 180.806 1.00 92.07  ? 194 ASN B N   1 
ATOM   3027  C CA  . ASN B  1 192 ? 149.590 169.946 181.536 1.00 95.86  ? 194 ASN B CA  1 
ATOM   3028  C C   . ASN B  1 192 ? 150.622 170.022 182.658 1.00 98.37  ? 194 ASN B C   1 
ATOM   3029  O O   . ASN B  1 192 ? 150.373 170.629 183.702 1.00 101.25 ? 194 ASN B O   1 
ATOM   3030  C CB  . ASN B  1 192 ? 148.185 170.190 182.093 1.00 97.58  ? 194 ASN B CB  1 
ATOM   3031  C CG  . ASN B  1 192 ? 147.169 170.463 181.005 1.00 101.07 ? 194 ASN B CG  1 
ATOM   3032  O OD1 . ASN B  1 192 ? 147.511 170.538 179.826 1.00 104.03 ? 194 ASN B OD1 1 
ATOM   3033  N ND2 . ASN B  1 192 ? 145.910 170.608 181.396 1.00 101.40 ? 194 ASN B ND2 1 
ATOM   3034  N N   . SER B  1 193 ? 151.784 169.409 182.460 1.00 96.38  ? 195 SER B N   1 
ATOM   3035  C CA  . SER B  1 193 ? 152.843 169.496 183.450 1.00 97.46  ? 195 SER B CA  1 
ATOM   3036  C C   . SER B  1 193 ? 153.504 170.870 183.403 1.00 103.07 ? 195 SER B C   1 
ATOM   3037  O O   . SER B  1 193 ? 153.338 171.637 182.452 1.00 106.88 ? 195 SER B O   1 
ATOM   3038  C CB  . SER B  1 193 ? 153.883 168.400 183.226 1.00 94.85  ? 195 SER B CB  1 
ATOM   3039  O OG  . SER B  1 193 ? 153.381 167.139 183.627 1.00 95.80  ? 195 SER B OG  1 
ATOM   3040  N N   . THR B  1 194 ? 154.265 171.177 184.451 1.00 101.59 ? 196 THR B N   1 
ATOM   3041  C CA  . THR B  1 194 ? 154.886 172.487 184.591 1.00 109.05 ? 196 THR B CA  1 
ATOM   3042  C C   . THR B  1 194 ? 156.298 172.329 185.131 1.00 112.69 ? 196 THR B C   1 
ATOM   3043  O O   . THR B  1 194 ? 156.511 171.623 186.120 1.00 120.42 ? 196 THR B O   1 
ATOM   3044  C CB  . THR B  1 194 ? 154.066 173.389 185.521 1.00 115.28 ? 196 THR B CB  1 
ATOM   3045  O OG1 . THR B  1 194 ? 152.818 173.712 184.897 1.00 117.87 ? 196 THR B OG1 1 
ATOM   3046  C CG2 . THR B  1 194 ? 154.819 174.673 185.829 1.00 113.79 ? 196 THR B CG2 1 
ATOM   3047  N N   . VAL B  1 195 ? 157.254 172.992 184.484 1.00 111.19 ? 197 VAL B N   1 
ATOM   3048  C CA  . VAL B  1 195 ? 158.645 173.017 184.920 1.00 109.50 ? 197 VAL B CA  1 
ATOM   3049  C C   . VAL B  1 195 ? 158.979 174.435 185.355 1.00 111.96 ? 197 VAL B C   1 
ATOM   3050  O O   . VAL B  1 195 ? 158.733 175.392 184.612 1.00 116.01 ? 197 VAL B O   1 
ATOM   3051  C CB  . VAL B  1 195 ? 159.599 172.550 183.808 1.00 104.50 ? 197 VAL B CB  1 
ATOM   3052  C CG1 . VAL B  1 195 ? 160.904 172.067 184.408 1.00 100.17 ? 197 VAL B CG1 1 
ATOM   3053  C CG2 . VAL B  1 195 ? 158.951 171.463 182.978 1.00 105.83 ? 197 VAL B CG2 1 
ATOM   3054  N N   . SER B  1 196 ? 159.540 174.571 186.555 1.00 110.58 ? 198 SER B N   1 
ATOM   3055  C CA  . SER B  1 196 ? 159.844 175.878 187.116 1.00 118.21 ? 198 SER B CA  1 
ATOM   3056  C C   . SER B  1 196 ? 161.285 176.027 187.580 1.00 117.10 ? 198 SER B C   1 
ATOM   3057  O O   . SER B  1 196 ? 161.648 177.101 188.074 1.00 119.50 ? 198 SER B O   1 
ATOM   3058  C CB  . SER B  1 196 ? 158.903 176.180 188.290 1.00 124.58 ? 198 SER B CB  1 
ATOM   3059  O OG  . SER B  1 196 ? 159.421 177.221 189.098 1.00 134.42 ? 198 SER B OG  1 
ATOM   3060  N N   . ALA B  1 197 ? 162.115 174.998 187.438 1.00 113.34 ? 199 ALA B N   1 
ATOM   3061  C CA  . ALA B  1 197 ? 163.493 175.071 187.904 1.00 108.97 ? 199 ALA B CA  1 
ATOM   3062  C C   . ALA B  1 197 ? 164.332 174.077 187.116 1.00 108.05 ? 199 ALA B C   1 
ATOM   3063  O O   . ALA B  1 197 ? 163.813 173.243 186.372 1.00 112.83 ? 199 ALA B O   1 
ATOM   3064  C CB  . ALA B  1 197 ? 163.589 174.801 189.408 1.00 107.45 ? 199 ALA B CB  1 
ATOM   3065  N N   . SER B  1 198 ? 165.644 174.181 187.292 1.00 104.82 ? 200 SER B N   1 
ATOM   3066  C CA  . SER B  1 198 ? 166.591 173.303 186.626 1.00 104.81 ? 200 SER B CA  1 
ATOM   3067  C C   . SER B  1 198 ? 166.879 172.073 187.481 1.00 106.38 ? 200 SER B C   1 
ATOM   3068  O O   . SER B  1 198 ? 166.683 172.072 188.699 1.00 109.43 ? 200 SER B O   1 
ATOM   3069  C CB  . SER B  1 198 ? 167.891 174.048 186.325 1.00 106.48 ? 200 SER B CB  1 
ATOM   3070  O OG  . SER B  1 198 ? 167.725 174.948 185.244 1.00 111.46 ? 200 SER B OG  1 
ATOM   3071  N N   . ASN B  1 199 ? 167.357 171.019 186.817 1.00 103.12 ? 201 ASN B N   1 
ATOM   3072  C CA  . ASN B  1 199 ? 167.731 169.764 187.475 1.00 101.16 ? 201 ASN B CA  1 
ATOM   3073  C C   . ASN B  1 199 ? 166.572 169.183 188.281 1.00 102.92 ? 201 ASN B C   1 
ATOM   3074  O O   . ASN B  1 199 ? 166.744 168.739 189.418 1.00 107.71 ? 201 ASN B O   1 
ATOM   3075  C CB  . ASN B  1 199 ? 168.967 169.950 188.356 1.00 99.38  ? 201 ASN B CB  1 
ATOM   3076  C CG  . ASN B  1 199 ? 169.997 170.863 187.726 1.00 105.77 ? 201 ASN B CG  1 
ATOM   3077  O OD1 . ASN B  1 199 ? 170.510 170.584 186.643 1.00 108.40 ? 201 ASN B OD1 1 
ATOM   3078  N ND2 . ASN B  1 199 ? 170.307 171.961 188.403 1.00 109.22 ? 201 ASN B ND2 1 
ATOM   3079  N N   . THR B  1 200 ? 165.379 169.186 187.691 1.00 97.82  ? 202 THR B N   1 
ATOM   3080  C CA  . THR B  1 200 ? 164.196 168.646 188.343 1.00 97.99  ? 202 THR B CA  1 
ATOM   3081  C C   . THR B  1 200 ? 163.410 167.798 187.355 1.00 92.41  ? 202 THR B C   1 
ATOM   3082  O O   . THR B  1 200 ? 163.521 167.959 186.137 1.00 93.78  ? 202 THR B O   1 
ATOM   3083  C CB  . THR B  1 200 ? 163.287 169.752 188.900 1.00 104.12 ? 202 THR B CB  1 
ATOM   3084  O OG1 . THR B  1 200 ? 162.928 170.655 187.848 1.00 108.10 ? 202 THR B OG1 1 
ATOM   3085  C CG2 . THR B  1 200 ? 163.985 170.520 190.012 1.00 104.65 ? 202 THR B CG2 1 
ATOM   3086  N N   . VAL B  1 201 ? 162.613 166.885 187.900 1.00 88.63  ? 203 VAL B N   1 
ATOM   3087  C CA  . VAL B  1 201 ? 161.664 166.090 187.129 1.00 84.45  ? 203 VAL B CA  1 
ATOM   3088  C C   . VAL B  1 201 ? 160.276 166.413 187.660 1.00 91.50  ? 203 VAL B C   1 
ATOM   3089  O O   . VAL B  1 201 ? 160.009 166.242 188.855 1.00 100.32 ? 203 VAL B O   1 
ATOM   3090  C CB  . VAL B  1 201 ? 161.956 164.586 187.230 1.00 80.83  ? 203 VAL B CB  1 
ATOM   3091  C CG1 . VAL B  1 201 ? 160.746 163.781 186.789 1.00 79.57  ? 203 VAL B CG1 1 
ATOM   3092  C CG2 . VAL B  1 201 ? 163.171 164.227 186.399 1.00 86.07  ? 203 VAL B CG2 1 
ATOM   3093  N N   . SER B  1 202 ? 159.397 166.880 186.781 1.00 86.00  ? 204 SER B N   1 
ATOM   3094  C CA  . SER B  1 202 ? 158.072 167.333 187.178 1.00 84.27  ? 204 SER B CA  1 
ATOM   3095  C C   . SER B  1 202 ? 157.016 166.372 186.653 1.00 89.50  ? 204 SER B C   1 
ATOM   3096  O O   . SER B  1 202 ? 157.037 166.000 185.475 1.00 93.30  ? 204 SER B O   1 
ATOM   3097  C CB  . SER B  1 202 ? 157.804 168.746 186.661 1.00 93.00  ? 204 SER B CB  1 
ATOM   3098  O OG  . SER B  1 202 ? 156.501 169.175 187.011 1.00 97.20  ? 204 SER B OG  1 
ATOM   3099  N N   . VAL B  1 203 ? 156.096 165.976 187.528 1.00 88.68  ? 205 VAL B N   1 
ATOM   3100  C CA  . VAL B  1 203 ? 155.003 165.084 187.172 1.00 85.17  ? 205 VAL B CA  1 
ATOM   3101  C C   . VAL B  1 203 ? 153.650 165.774 187.328 1.00 90.68  ? 205 VAL B C   1 
ATOM   3102  O O   . VAL B  1 203 ? 152.642 165.118 187.548 1.00 95.50  ? 205 VAL B O   1 
ATOM   3103  C CB  . VAL B  1 203 ? 155.061 163.782 187.992 1.00 79.21  ? 205 VAL B CB  1 
ATOM   3104  C CG1 . VAL B  1 203 ? 156.224 162.922 187.535 1.00 75.78  ? 205 VAL B CG1 1 
ATOM   3105  C CG2 . VAL B  1 203 ? 155.178 164.094 189.472 1.00 83.10  ? 205 VAL B CG2 1 
ATOM   3106  N N   . GLY B  1 204 ? 153.621 167.093 187.216 1.00 88.58  ? 206 GLY B N   1 
ATOM   3107  C CA  . GLY B  1 204 ? 152.383 167.829 187.350 1.00 91.88  ? 206 GLY B CA  1 
ATOM   3108  C C   . GLY B  1 204 ? 152.661 169.306 187.550 1.00 101.62 ? 206 GLY B C   1 
ATOM   3109  O O   . GLY B  1 204 ? 153.805 169.756 187.512 1.00 102.48 ? 206 GLY B O   1 
ATOM   3110  N N   . SER B  1 205 ? 151.580 170.046 187.763 1.00 104.24 ? 207 SER B N   1 
ATOM   3111  C CA  . SER B  1 205 ? 151.634 171.481 188.001 1.00 104.52 ? 207 SER B CA  1 
ATOM   3112  C C   . SER B  1 205 ? 151.162 171.773 189.424 1.00 110.29 ? 207 SER B C   1 
ATOM   3113  O O   . SER B  1 205 ? 150.867 170.864 190.203 1.00 114.53 ? 207 SER B O   1 
ATOM   3114  C CB  . SER B  1 205 ? 150.797 172.228 186.962 1.00 105.17 ? 207 SER B CB  1 
ATOM   3115  O OG  . SER B  1 205 ? 149.523 171.629 186.812 1.00 110.87 ? 207 SER B OG  1 
ATOM   3116  N N   . SER B  1 206 ? 151.095 173.063 189.761 1.00 113.03 ? 208 SER B N   1 
ATOM   3117  C CA  . SER B  1 206 ? 150.632 173.460 191.085 1.00 117.37 ? 208 SER B CA  1 
ATOM   3118  C C   . SER B  1 206 ? 149.156 173.156 191.298 1.00 122.53 ? 208 SER B C   1 
ATOM   3119  O O   . SER B  1 206 ? 148.717 173.058 192.449 1.00 127.02 ? 208 SER B O   1 
ATOM   3120  C CB  . SER B  1 206 ? 150.893 174.949 191.310 1.00 120.27 ? 208 SER B CB  1 
ATOM   3121  O OG  . SER B  1 206 ? 152.281 175.233 191.284 1.00 124.39 ? 208 SER B OG  1 
ATOM   3122  N N   . THR B  1 207 ? 148.384 173.005 190.223 1.00 119.40 ? 209 THR B N   1 
ATOM   3123  C CA  . THR B  1 207 ? 146.961 172.701 190.314 1.00 120.88 ? 209 THR B CA  1 
ATOM   3124  C C   . THR B  1 207 ? 146.684 171.204 190.311 1.00 122.16 ? 209 THR B C   1 
ATOM   3125  O O   . THR B  1 207 ? 145.897 170.717 191.128 1.00 120.66 ? 209 THR B O   1 
ATOM   3126  C CB  . THR B  1 207 ? 146.206 173.370 189.160 1.00 120.35 ? 209 THR B CB  1 
ATOM   3127  O OG1 . THR B  1 207 ? 146.363 172.589 187.968 1.00 121.43 ? 209 THR B OG1 1 
ATOM   3128  C CG2 . THR B  1 207 ? 146.744 174.769 188.915 1.00 112.57 ? 209 THR B CG2 1 
ATOM   3129  N N   . LEU B  1 208 ? 147.317 170.461 189.408 1.00 120.01 ? 210 LEU B N   1 
ATOM   3130  C CA  . LEU B  1 208 ? 147.155 169.017 189.314 1.00 114.37 ? 210 LEU B CA  1 
ATOM   3131  C C   . LEU B  1 208 ? 148.477 168.351 189.664 1.00 109.34 ? 210 LEU B C   1 
ATOM   3132  O O   . LEU B  1 208 ? 149.491 168.587 188.998 1.00 109.87 ? 210 LEU B O   1 
ATOM   3133  C CB  . LEU B  1 208 ? 146.699 168.604 187.915 1.00 113.69 ? 210 LEU B CB  1 
ATOM   3134  C CG  . LEU B  1 208 ? 146.602 167.099 187.666 1.00 112.57 ? 210 LEU B CG  1 
ATOM   3135  C CD1 . LEU B  1 208 ? 145.248 166.568 188.105 1.00 110.04 ? 210 LEU B CD1 1 
ATOM   3136  C CD2 . LEU B  1 208 ? 146.860 166.777 186.203 1.00 106.98 ? 210 LEU B CD2 1 
ATOM   3137  N N   . LYS B  1 209 ? 148.464 167.521 190.703 1.00 105.56 ? 211 LYS B N   1 
ATOM   3138  C CA  . LYS B  1 209 ? 149.646 166.810 191.164 1.00 104.72 ? 211 LYS B CA  1 
ATOM   3139  C C   . LYS B  1 209 ? 149.399 165.315 191.043 1.00 105.89 ? 211 LYS B C   1 
ATOM   3140  O O   . LYS B  1 209 ? 148.385 164.808 191.534 1.00 108.56 ? 211 LYS B O   1 
ATOM   3141  C CB  . LYS B  1 209 ? 149.980 167.186 192.607 1.00 99.95  ? 211 LYS B CB  1 
ATOM   3142  C CG  . LYS B  1 209 ? 150.278 168.661 192.790 1.00 105.33 ? 211 LYS B CG  1 
ATOM   3143  C CD  . LYS B  1 209 ? 150.555 169.000 194.240 1.00 109.15 ? 211 LYS B CD  1 
ATOM   3144  C CE  . LYS B  1 209 ? 151.373 170.273 194.349 1.00 112.00 ? 211 LYS B CE  1 
ATOM   3145  N NZ  . LYS B  1 209 ? 150.509 171.482 194.370 1.00 117.92 ? 211 LYS B NZ  1 
ATOM   3146  N N   . ARG B  1 210 ? 150.322 164.615 190.395 1.00 101.88 ? 212 ARG B N   1 
ATOM   3147  C CA  . ARG B  1 210 ? 150.167 163.193 190.137 1.00 93.33  ? 212 ARG B CA  1 
ATOM   3148  C C   . ARG B  1 210 ? 150.824 162.368 191.234 1.00 98.06  ? 212 ARG B C   1 
ATOM   3149  O O   . ARG B  1 210 ? 151.810 162.783 191.848 1.00 98.97  ? 212 ARG B O   1 
ATOM   3150  C CB  . ARG B  1 210 ? 150.775 162.819 188.786 1.00 82.31  ? 212 ARG B CB  1 
ATOM   3151  C CG  . ARG B  1 210 ? 149.923 163.193 187.591 1.00 74.40  ? 212 ARG B CG  1 
ATOM   3152  C CD  . ARG B  1 210 ? 150.622 162.828 186.296 1.00 79.28  ? 212 ARG B CD  1 
ATOM   3153  N NE  . ARG B  1 210 ? 149.810 163.149 185.131 1.00 84.91  ? 212 ARG B NE  1 
ATOM   3154  C CZ  . ARG B  1 210 ? 149.760 164.346 184.564 1.00 90.95  ? 212 ARG B CZ  1 
ATOM   3155  N NH1 . ARG B  1 210 ? 150.477 165.358 185.022 1.00 91.72  ? 212 ARG B NH1 1 
ATOM   3156  N NH2 . ARG B  1 210 ? 148.969 164.532 183.511 1.00 97.69  ? 212 ARG B NH2 1 
ATOM   3157  N N   . LYS B  1 211 ? 150.263 161.189 191.473 1.00 97.81  ? 213 LYS B N   1 
ATOM   3158  C CA  . LYS B  1 211 ? 150.875 160.211 192.356 1.00 94.49  ? 213 LYS B CA  1 
ATOM   3159  C C   . LYS B  1 211 ? 151.797 159.304 191.556 1.00 100.26 ? 213 LYS B C   1 
ATOM   3160  O O   . LYS B  1 211 ? 151.586 159.068 190.364 1.00 104.12 ? 213 LYS B O   1 
ATOM   3161  C CB  . LYS B  1 211 ? 149.813 159.368 193.062 1.00 88.51  ? 213 LYS B CB  1 
ATOM   3162  C CG  . LYS B  1 211 ? 148.993 160.118 194.091 1.00 97.20  ? 213 LYS B CG  1 
ATOM   3163  C CD  . LYS B  1 211 ? 147.805 159.288 194.540 1.00 102.44 ? 213 LYS B CD  1 
ATOM   3164  C CE  . LYS B  1 211 ? 148.257 157.980 195.164 1.00 102.99 ? 213 LYS B CE  1 
ATOM   3165  N NZ  . LYS B  1 211 ? 147.114 157.205 195.719 1.00 104.67 ? 213 LYS B NZ  1 
ATOM   3166  N N   . ILE B  1 212 ? 152.827 158.795 192.222 1.00 98.53  ? 214 ILE B N   1 
ATOM   3167  C CA  . ILE B  1 212 ? 153.741 157.827 191.632 1.00 98.65  ? 214 ILE B CA  1 
ATOM   3168  C C   . ILE B  1 212 ? 153.459 156.489 192.297 1.00 101.38 ? 214 ILE B C   1 
ATOM   3169  O O   . ILE B  1 212 ? 153.770 156.292 193.478 1.00 103.14 ? 214 ILE B O   1 
ATOM   3170  C CB  . ILE B  1 212 ? 155.207 158.245 191.800 1.00 92.90  ? 214 ILE B CB  1 
ATOM   3171  C CG1 . ILE B  1 212 ? 155.402 159.684 191.322 1.00 89.17  ? 214 ILE B CG1 1 
ATOM   3172  C CG2 . ILE B  1 212 ? 156.111 157.320 191.015 1.00 93.12  ? 214 ILE B CG2 1 
ATOM   3173  C CD1 . ILE B  1 212 ? 156.768 160.246 191.629 1.00 86.20  ? 214 ILE B CD1 1 
ATOM   3174  N N   . VAL B  1 213 ? 152.873 155.569 191.542 1.00 97.70  ? 215 VAL B N   1 
ATOM   3175  C CA  . VAL B  1 213 ? 152.420 154.304 192.077 1.00 99.58  ? 215 VAL B CA  1 
ATOM   3176  C C   . VAL B  1 213 ? 153.387 153.204 191.659 1.00 105.16 ? 215 VAL B C   1 
ATOM   3177  O O   . VAL B  1 213 ? 154.217 153.378 190.770 1.00 109.80 ? 215 VAL B O   1 
ATOM   3178  C CB  . VAL B  1 213 ? 150.977 153.977 191.624 1.00 100.01 ? 215 VAL B CB  1 
ATOM   3179  C CG1 . VAL B  1 213 ? 149.972 154.807 192.400 1.00 98.47  ? 215 VAL B CG1 1 
ATOM   3180  C CG2 . VAL B  1 213 ? 150.826 154.215 190.134 1.00 100.12 ? 215 VAL B CG2 1 
ATOM   3181  N N   . ASN B  1 214 ? 153.278 152.047 192.315 1.00 100.89 ? 216 ASN B N   1 
ATOM   3182  C CA  . ASN B  1 214 ? 154.074 150.865 191.986 1.00 104.56 ? 216 ASN B CA  1 
ATOM   3183  C C   . ASN B  1 214 ? 155.570 151.155 192.071 1.00 108.72 ? 216 ASN B C   1 
ATOM   3184  O O   . ASN B  1 214 ? 156.338 150.836 191.162 1.00 109.24 ? 216 ASN B O   1 
ATOM   3185  C CB  . ASN B  1 214 ? 153.702 150.320 190.606 1.00 107.15 ? 216 ASN B CB  1 
ATOM   3186  C CG  . ASN B  1 214 ? 152.278 149.812 190.549 1.00 109.30 ? 216 ASN B CG  1 
ATOM   3187  O OD1 . ASN B  1 214 ? 151.695 149.453 191.571 1.00 111.02 ? 216 ASN B OD1 1 
ATOM   3188  N ND2 . ASN B  1 214 ? 151.705 149.788 189.353 1.00 108.31 ? 216 ASN B ND2 1 
ATOM   3189  N N   . VAL B  1 215 ? 155.986 151.770 193.171 1.00 110.18 ? 217 VAL B N   1 
ATOM   3190  C CA  . VAL B  1 215 ? 157.391 152.074 193.410 1.00 110.43 ? 217 VAL B CA  1 
ATOM   3191  C C   . VAL B  1 215 ? 157.974 150.999 194.313 1.00 116.87 ? 217 VAL B C   1 
ATOM   3192  O O   . VAL B  1 215 ? 157.376 150.639 195.334 1.00 119.13 ? 217 VAL B O   1 
ATOM   3193  C CB  . VAL B  1 215 ? 157.554 153.467 194.039 1.00 103.60 ? 217 VAL B CB  1 
ATOM   3194  C CG1 . VAL B  1 215 ? 159.024 153.831 194.142 1.00 104.34 ? 217 VAL B CG1 1 
ATOM   3195  C CG2 . VAL B  1 215 ? 156.804 154.502 193.228 1.00 103.56 ? 217 VAL B CG2 1 
ATOM   3196  N N   . GLY B  1 216 ? 159.138 150.478 193.936 1.00 115.10 ? 218 GLY B N   1 
ATOM   3197  C CA  . GLY B  1 216 ? 159.817 149.523 194.782 1.00 117.62 ? 218 GLY B CA  1 
ATOM   3198  C C   . GLY B  1 216 ? 160.325 150.158 196.060 1.00 122.60 ? 218 GLY B C   1 
ATOM   3199  O O   . GLY B  1 216 ? 160.491 151.374 196.165 1.00 126.70 ? 218 GLY B O   1 
ATOM   3200  N N   . ASP B  1 217 ? 160.567 149.309 197.055 1.00 122.15 ? 219 ASP B N   1 
ATOM   3201  C CA  . ASP B  1 217 ? 161.021 149.795 198.350 1.00 124.21 ? 219 ASP B CA  1 
ATOM   3202  C C   . ASP B  1 217 ? 162.370 150.489 198.218 1.00 125.11 ? 219 ASP B C   1 
ATOM   3203  O O   . ASP B  1 217 ? 163.232 150.069 197.443 1.00 127.83 ? 219 ASP B O   1 
ATOM   3204  C CB  . ASP B  1 217 ? 161.121 148.642 199.347 1.00 126.70 ? 219 ASP B CB  1 
ATOM   3205  C CG  . ASP B  1 217 ? 159.775 148.250 199.918 1.00 129.57 ? 219 ASP B CG  1 
ATOM   3206  O OD1 . ASP B  1 217 ? 158.747 148.550 199.276 1.00 129.12 ? 219 ASP B OD1 1 
ATOM   3207  O OD2 . ASP B  1 217 ? 159.745 147.647 201.010 1.00 127.77 ? 219 ASP B OD2 1 
ATOM   3208  N N   . GLY B  1 218 ? 162.546 151.562 198.983 1.00 122.30 ? 220 GLY B N   1 
ATOM   3209  C CA  . GLY B  1 218 ? 163.783 152.313 198.953 1.00 118.97 ? 220 GLY B CA  1 
ATOM   3210  C C   . GLY B  1 218 ? 164.937 151.589 199.613 1.00 123.56 ? 220 GLY B C   1 
ATOM   3211  O O   . GLY B  1 218 ? 164.901 150.368 199.788 1.00 130.40 ? 220 GLY B O   1 
ATOM   3212  N N   . ALA B  1 219 ? 165.966 152.339 199.989 1.00 115.46 ? 221 ALA B N   1 
ATOM   3213  C CA  . ALA B  1 219 ? 167.209 151.796 200.522 1.00 115.39 ? 221 ALA B CA  1 
ATOM   3214  C C   . ALA B  1 219 ? 167.642 152.570 201.756 1.00 117.58 ? 221 ALA B C   1 
ATOM   3215  O O   . ALA B  1 219 ? 168.774 153.049 201.841 1.00 127.21 ? 221 ALA B O   1 
ATOM   3216  C CB  . ALA B  1 219 ? 168.309 151.808 199.466 1.00 119.11 ? 221 ALA B CB  1 
ATOM   3217  N N   . ILE B  1 220 ? 166.731 152.719 202.722 1.00 113.75 ? 222 ILE B N   1 
ATOM   3218  C CA  . ILE B  1 220 ? 166.932 153.593 203.877 1.00 114.67 ? 222 ILE B CA  1 
ATOM   3219  C C   . ILE B  1 220 ? 168.312 153.368 204.477 1.00 123.09 ? 222 ILE B C   1 
ATOM   3220  O O   . ILE B  1 220 ? 168.636 152.264 204.929 1.00 126.95 ? 222 ILE B O   1 
ATOM   3221  C CB  . ILE B  1 220 ? 165.844 153.360 204.942 1.00 105.67 ? 222 ILE B CB  1 
ATOM   3222  C CG1 . ILE B  1 220 ? 164.454 153.375 204.308 1.00 108.18 ? 222 ILE B CG1 1 
ATOM   3223  C CG2 . ILE B  1 220 ? 165.943 154.404 206.041 1.00 107.67 ? 222 ILE B CG2 1 
ATOM   3224  C CD1 . ILE B  1 220 ? 164.175 154.607 203.497 1.00 111.42 ? 222 ILE B CD1 1 
ATOM   3225  N N   . SER B  1 221 ? 169.122 154.420 204.494 1.00 122.54 ? 223 SER B N   1 
ATOM   3226  C CA  . SER B  1 221 ? 170.527 154.341 204.881 1.00 119.15 ? 223 SER B CA  1 
ATOM   3227  C C   . SER B  1 221 ? 171.063 155.764 204.978 1.00 123.11 ? 223 SER B C   1 
ATOM   3228  O O   . SER B  1 221 ? 170.329 156.739 204.790 1.00 126.36 ? 223 SER B O   1 
ATOM   3229  C CB  . SER B  1 221 ? 171.338 153.509 203.886 1.00 119.27 ? 223 SER B CB  1 
ATOM   3230  O OG  . SER B  1 221 ? 171.910 154.336 202.888 1.00 123.00 ? 223 SER B OG  1 
ATOM   3231  N N   . ALA B  1 222 ? 172.362 155.874 205.259 1.00 124.72 ? 224 ALA B N   1 
ATOM   3232  C CA  . ALA B  1 222 ? 172.960 157.184 205.492 1.00 124.06 ? 224 ALA B CA  1 
ATOM   3233  C C   . ALA B  1 222 ? 173.099 157.982 204.202 1.00 123.98 ? 224 ALA B C   1 
ATOM   3234  O O   . ALA B  1 222 ? 172.907 159.203 204.200 1.00 126.98 ? 224 ALA B O   1 
ATOM   3235  C CB  . ALA B  1 222 ? 174.320 157.024 206.170 1.00 120.98 ? 224 ALA B CB  1 
ATOM   3236  N N   . ASN B  1 223 ? 173.431 157.318 203.096 1.00 124.13 ? 225 ASN B N   1 
ATOM   3237  C CA  . ASN B  1 223 ? 173.777 158.011 201.864 1.00 125.28 ? 225 ASN B CA  1 
ATOM   3238  C C   . ASN B  1 223 ? 172.913 157.628 200.672 1.00 122.92 ? 225 ASN B C   1 
ATOM   3239  O O   . ASN B  1 223 ? 173.153 158.134 199.570 1.00 124.03 ? 225 ASN B O   1 
ATOM   3240  C CB  . ASN B  1 223 ? 175.248 157.753 201.513 1.00 134.67 ? 225 ASN B CB  1 
ATOM   3241  C CG  . ASN B  1 223 ? 175.656 156.313 201.750 1.00 139.45 ? 225 ASN B CG  1 
ATOM   3242  O OD1 . ASN B  1 223 ? 175.039 155.386 201.224 1.00 138.32 ? 225 ASN B OD1 1 
ATOM   3243  N ND2 . ASN B  1 223 ? 176.701 156.117 202.546 1.00 137.95 ? 225 ASN B ND2 1 
ATOM   3244  N N   . SER B  1 224 ? 171.927 156.755 200.849 1.00 120.33 ? 226 SER B N   1 
ATOM   3245  C CA  . SER B  1 224 ? 171.130 156.302 199.719 1.00 122.13 ? 226 SER B CA  1 
ATOM   3246  C C   . SER B  1 224 ? 170.267 157.430 199.171 1.00 122.67 ? 226 SER B C   1 
ATOM   3247  O O   . SER B  1 224 ? 169.678 158.209 199.925 1.00 125.64 ? 226 SER B O   1 
ATOM   3248  C CB  . SER B  1 224 ? 170.247 155.128 200.128 1.00 120.89 ? 226 SER B CB  1 
ATOM   3249  O OG  . SER B  1 224 ? 168.968 155.574 200.542 1.00 119.78 ? 226 SER B OG  1 
ATOM   3250  N N   . SER B  1 225 ? 170.195 157.512 197.846 1.00 116.90 ? 227 SER B N   1 
ATOM   3251  C CA  . SER B  1 225 ? 169.325 158.455 197.150 1.00 114.51 ? 227 SER B CA  1 
ATOM   3252  C C   . SER B  1 225 ? 168.291 157.623 196.401 1.00 116.99 ? 227 SER B C   1 
ATOM   3253  O O   . SER B  1 225 ? 168.467 157.299 195.225 1.00 120.38 ? 227 SER B O   1 
ATOM   3254  C CB  . SER B  1 225 ? 170.113 159.349 196.212 1.00 118.95 ? 227 SER B CB  1 
ATOM   3255  O OG  . SER B  1 225 ? 170.527 158.628 195.065 1.00 128.68 ? 227 SER B OG  1 
ATOM   3256  N N   . ASP B  1 226 ? 167.207 157.285 197.093 1.00 116.57 ? 228 ASP B N   1 
ATOM   3257  C CA  . ASP B  1 226 ? 166.137 156.484 196.516 1.00 114.00 ? 228 ASP B CA  1 
ATOM   3258  C C   . ASP B  1 226 ? 164.806 157.189 196.718 1.00 116.20 ? 228 ASP B C   1 
ATOM   3259  O O   . ASP B  1 226 ? 164.775 158.364 197.089 1.00 121.59 ? 228 ASP B O   1 
ATOM   3260  C CB  . ASP B  1 226 ? 166.113 155.089 197.141 1.00 118.84 ? 228 ASP B CB  1 
ATOM   3261  C CG  . ASP B  1 226 ? 166.757 154.046 196.255 1.00 126.27 ? 228 ASP B CG  1 
ATOM   3262  O OD1 . ASP B  1 226 ? 166.374 153.961 195.072 1.00 131.00 ? 228 ASP B OD1 1 
ATOM   3263  O OD2 . ASP B  1 226 ? 167.649 153.317 196.735 1.00 123.59 ? 228 ASP B OD2 1 
ATOM   3264  N N   . ALA B  1 227 ? 163.704 156.495 196.464 1.00 112.44 ? 229 ALA B N   1 
ATOM   3265  C CA  . ALA B  1 227 ? 162.370 157.031 196.709 1.00 104.12 ? 229 ALA B CA  1 
ATOM   3266  C C   . ALA B  1 227 ? 161.666 156.105 197.689 1.00 108.89 ? 229 ALA B C   1 
ATOM   3267  O O   . ALA B  1 227 ? 161.365 154.955 197.354 1.00 119.87 ? 229 ALA B O   1 
ATOM   3268  C CB  . ALA B  1 227 ? 161.581 157.165 195.409 1.00 99.30  ? 229 ALA B CB  1 
ATOM   3269  N N   . VAL B  1 228 ? 161.408 156.602 198.901 1.00 100.57 ? 230 VAL B N   1 
ATOM   3270  C CA  . VAL B  1 228 ? 160.712 155.784 199.881 1.00 105.57 ? 230 VAL B CA  1 
ATOM   3271  C C   . VAL B  1 228 ? 159.254 155.622 199.465 1.00 109.08 ? 230 VAL B C   1 
ATOM   3272  O O   . VAL B  1 228 ? 158.707 156.402 198.678 1.00 113.02 ? 230 VAL B O   1 
ATOM   3273  C CB  . VAL B  1 228 ? 160.823 156.391 201.289 1.00 98.16  ? 230 VAL B CB  1 
ATOM   3274  C CG1 . VAL B  1 228 ? 162.241 156.859 201.552 1.00 97.50  ? 230 VAL B CG1 1 
ATOM   3275  C CG2 . VAL B  1 228 ? 159.837 157.522 201.459 1.00 97.23  ? 230 VAL B CG2 1 
ATOM   3276  N N   . THR B  1 229 ? 158.619 154.589 200.000 1.00 107.74 ? 231 THR B N   1 
ATOM   3277  C CA  . THR B  1 229 ? 157.240 154.278 199.662 1.00 105.26 ? 231 THR B CA  1 
ATOM   3278  C C   . THR B  1 229 ? 156.349 154.466 200.884 1.00 103.52 ? 231 THR B C   1 
ATOM   3279  O O   . THR B  1 229 ? 156.812 154.792 201.981 1.00 102.88 ? 231 THR B O   1 
ATOM   3280  C CB  . THR B  1 229 ? 157.124 152.857 199.111 1.00 105.52 ? 231 THR B CB  1 
ATOM   3281  O OG1 . THR B  1 229 ? 157.743 151.939 200.016 1.00 112.36 ? 231 THR B OG1 1 
ATOM   3282  C CG2 . THR B  1 229 ? 157.812 152.758 197.762 1.00 105.69 ? 231 THR B CG2 1 
ATOM   3283  N N   . GLY B  1 230 ? 155.049 154.260 200.677 1.00 100.85 ? 232 GLY B N   1 
ATOM   3284  C CA  . GLY B  1 230 ? 154.105 154.414 201.770 1.00 102.22 ? 232 GLY B CA  1 
ATOM   3285  C C   . GLY B  1 230 ? 154.355 153.437 202.900 1.00 104.64 ? 232 GLY B C   1 
ATOM   3286  O O   . GLY B  1 230 ? 154.311 153.808 204.075 1.00 105.76 ? 232 GLY B O   1 
ATOM   3287  N N   . ARG B  1 231 ? 154.627 152.175 202.562 1.00 101.86 ? 233 ARG B N   1 
ATOM   3288  C CA  . ARG B  1 231 ? 154.888 151.177 203.593 1.00 104.09 ? 233 ARG B CA  1 
ATOM   3289  C C   . ARG B  1 231 ? 156.180 151.478 204.342 1.00 106.84 ? 233 ARG B C   1 
ATOM   3290  O O   . ARG B  1 231 ? 156.281 151.213 205.546 1.00 107.62 ? 233 ARG B O   1 
ATOM   3291  C CB  . ARG B  1 231 ? 154.938 149.782 202.973 1.00 106.66 ? 233 ARG B CB  1 
ATOM   3292  C CG  . ARG B  1 231 ? 155.958 149.632 201.859 1.00 109.71 ? 233 ARG B CG  1 
ATOM   3293  C CD  . ARG B  1 231 ? 156.727 148.327 201.988 1.00 117.35 ? 233 ARG B CD  1 
ATOM   3294  N NE  . ARG B  1 231 ? 155.925 147.167 201.616 1.00 123.65 ? 233 ARG B NE  1 
ATOM   3295  C CZ  . ARG B  1 231 ? 155.553 146.874 200.378 1.00 127.22 ? 233 ARG B CZ  1 
ATOM   3296  N NH1 . ARG B  1 231 ? 155.907 147.628 199.350 1.00 125.09 ? 233 ARG B NH1 1 
ATOM   3297  N NH2 . ARG B  1 231 ? 154.809 145.792 200.164 1.00 124.92 ? 233 ARG B NH2 1 
ATOM   3298  N N   . GLN B  1 232 ? 157.178 152.030 203.648 1.00 107.61 ? 234 GLN B N   1 
ATOM   3299  C CA  . GLN B  1 232 ? 158.456 152.321 204.287 1.00 100.53 ? 234 GLN B CA  1 
ATOM   3300  C C   . GLN B  1 232 ? 158.299 153.354 205.393 1.00 102.71 ? 234 GLN B C   1 
ATOM   3301  O O   . GLN B  1 232 ? 158.820 153.178 206.499 1.00 105.85 ? 234 GLN B O   1 
ATOM   3302  C CB  . GLN B  1 232 ? 159.463 152.801 203.245 1.00 97.31  ? 234 GLN B CB  1 
ATOM   3303  C CG  . GLN B  1 232 ? 159.886 151.732 202.266 1.00 104.82 ? 234 GLN B CG  1 
ATOM   3304  C CD  . GLN B  1 232 ? 161.357 151.803 201.944 1.00 111.12 ? 234 GLN B CD  1 
ATOM   3305  O OE1 . GLN B  1 232 ? 161.819 152.761 201.330 1.00 115.77 ? 234 GLN B OE1 1 
ATOM   3306  N NE2 . GLN B  1 232 ? 162.106 150.790 202.360 1.00 113.82 ? 234 GLN B NE2 1 
ATOM   3307  N N   . LEU B  1 233 ? 157.583 154.443 205.115 1.00 103.69 ? 235 LEU B N   1 
ATOM   3308  C CA  . LEU B  1 233 ? 157.366 155.451 206.144 1.00 103.80 ? 235 LEU B CA  1 
ATOM   3309  C C   . LEU B  1 233 ? 156.327 154.994 207.161 1.00 104.02 ? 235 LEU B C   1 
ATOM   3310  O O   . LEU B  1 233 ? 156.397 155.384 208.331 1.00 104.99 ? 235 LEU B O   1 
ATOM   3311  C CB  . LEU B  1 233 ? 156.957 156.779 205.501 1.00 102.22 ? 235 LEU B CB  1 
ATOM   3312  C CG  . LEU B  1 233 ? 156.076 157.754 206.283 1.00 103.65 ? 235 LEU B CG  1 
ATOM   3313  C CD1 . LEU B  1 233 ? 156.876 158.422 207.388 1.00 103.25 ? 235 LEU B CD1 1 
ATOM   3314  C CD2 . LEU B  1 233 ? 155.489 158.799 205.356 1.00 107.35 ? 235 LEU B CD2 1 
ATOM   3315  N N   . TYR B  1 234 ? 155.373 154.160 206.740 1.00 102.34 ? 236 TYR B N   1 
ATOM   3316  C CA  . TYR B  1 234 ? 154.389 153.622 207.672 1.00 103.50 ? 236 TYR B CA  1 
ATOM   3317  C C   . TYR B  1 234 ? 155.063 152.792 208.757 1.00 108.99 ? 236 TYR B C   1 
ATOM   3318  O O   . TYR B  1 234 ? 154.806 152.980 209.951 1.00 111.64 ? 236 TYR B O   1 
ATOM   3319  C CB  . TYR B  1 234 ? 153.366 152.778 206.915 1.00 100.85 ? 236 TYR B CB  1 
ATOM   3320  C CG  . TYR B  1 234 ? 152.297 152.171 207.792 1.00 103.21 ? 236 TYR B CG  1 
ATOM   3321  C CD1 . TYR B  1 234 ? 151.476 152.968 208.574 1.00 104.79 ? 236 TYR B CD1 1 
ATOM   3322  C CD2 . TYR B  1 234 ? 152.129 150.796 207.858 1.00 100.81 ? 236 TYR B CD2 1 
ATOM   3323  C CE1 . TYR B  1 234 ? 150.500 152.413 209.377 1.00 106.69 ? 236 TYR B CE1 1 
ATOM   3324  C CE2 . TYR B  1 234 ? 151.160 150.232 208.661 1.00 101.95 ? 236 TYR B CE2 1 
ATOM   3325  C CZ  . TYR B  1 234 ? 150.350 151.045 209.419 1.00 106.33 ? 236 TYR B CZ  1 
ATOM   3326  O OH  . TYR B  1 234 ? 149.383 150.486 210.222 1.00 106.92 ? 236 TYR B OH  1 
ATOM   3327  N N   . SER B  1 235 ? 155.939 151.872 208.357 1.00 108.78 ? 237 SER B N   1 
ATOM   3328  C CA  . SER B  1 235 ? 156.652 151.034 209.311 1.00 107.04 ? 237 SER B CA  1 
ATOM   3329  C C   . SER B  1 235 ? 157.922 151.689 209.829 1.00 111.18 ? 237 SER B C   1 
ATOM   3330  O O   . SER B  1 235 ? 158.274 151.502 210.999 1.00 107.83 ? 237 SER B O   1 
ATOM   3331  C CB  . SER B  1 235 ? 156.991 149.683 208.676 1.00 111.48 ? 237 SER B CB  1 
ATOM   3332  O OG  . SER B  1 235 ? 157.623 149.852 207.419 1.00 116.32 ? 237 SER B OG  1 
ATOM   3333  N N   . GLY B  1 236 ? 158.616 152.451 208.987 1.00 115.82 ? 238 GLY B N   1 
ATOM   3334  C CA  . GLY B  1 236 ? 159.817 153.131 209.424 1.00 117.42 ? 238 GLY B CA  1 
ATOM   3335  C C   . GLY B  1 236 ? 161.012 152.236 209.637 1.00 115.16 ? 238 GLY B C   1 
ATOM   3336  O O   . GLY B  1 236 ? 161.892 152.577 210.428 1.00 116.90 ? 238 GLY B O   1 
ATOM   3337  N N   . ASN B  1 237 ? 161.059 151.083 208.977 1.00 116.83 ? 239 ASN B N   1 
ATOM   3338  C CA  . ASN B  1 237 ? 162.161 150.155 209.187 1.00 117.46 ? 239 ASN B CA  1 
ATOM   3339  C C   . ASN B  1 237 ? 163.461 150.731 208.645 1.00 118.65 ? 239 ASN B C   1 
ATOM   3340  O O   . ASN B  1 237 ? 163.503 151.295 207.548 1.00 118.95 ? 239 ASN B O   1 
ATOM   3341  C CB  . ASN B  1 237 ? 161.857 148.813 208.525 1.00 118.83 ? 239 ASN B CB  1 
ATOM   3342  C CG  . ASN B  1 237 ? 160.535 148.228 208.978 1.00 121.54 ? 239 ASN B CG  1 
ATOM   3343  O OD1 . ASN B  1 237 ? 160.122 148.408 210.123 1.00 122.93 ? 239 ASN B OD1 1 
ATOM   3344  N ND2 . ASN B  1 237 ? 159.861 147.524 208.077 1.00 121.48 ? 239 ASN B ND2 1 
ATOM   3345  N N   . GLY B  1 238 ? 164.529 150.584 209.425 1.00 114.91 ? 240 GLY B N   1 
ATOM   3346  C CA  . GLY B  1 238 ? 165.843 151.036 209.026 1.00 116.78 ? 240 GLY B CA  1 
ATOM   3347  C C   . GLY B  1 238 ? 166.158 152.486 209.320 1.00 117.60 ? 240 GLY B C   1 
ATOM   3348  O O   . GLY B  1 238 ? 167.214 152.967 208.891 1.00 121.48 ? 240 GLY B O   1 
ATOM   3349  N N   . ILE B  1 239 ? 165.286 153.202 210.033 1.00 115.40 ? 241 ILE B N   1 
ATOM   3350  C CA  . ILE B  1 239 ? 165.588 154.587 210.377 1.00 110.88 ? 241 ILE B CA  1 
ATOM   3351  C C   . ILE B  1 239 ? 166.711 154.635 211.406 1.00 111.33 ? 241 ILE B C   1 
ATOM   3352  O O   . ILE B  1 239 ? 167.009 153.657 212.101 1.00 111.29 ? 241 ILE B O   1 
ATOM   3353  C CB  . ILE B  1 239 ? 164.341 155.319 210.895 1.00 103.70 ? 241 ILE B CB  1 
ATOM   3354  C CG1 . ILE B  1 239 ? 163.836 154.659 212.179 1.00 104.24 ? 241 ILE B CG1 1 
ATOM   3355  C CG2 . ILE B  1 239 ? 163.262 155.351 209.834 1.00 100.54 ? 241 ILE B CG2 1 
ATOM   3356  C CD1 . ILE B  1 239 ? 162.485 155.150 212.629 1.00 97.27  ? 241 ILE B CD1 1 
ATOM   3357  N N   . ASP B  1 240 ? 167.342 155.800 211.505 1.00 108.75 ? 242 ASP B N   1 
ATOM   3358  C CA  . ASP B  1 240 ? 168.369 156.029 212.516 1.00 110.63 ? 242 ASP B CA  1 
ATOM   3359  C C   . ASP B  1 240 ? 167.680 156.189 213.862 1.00 112.07 ? 242 ASP B C   1 
ATOM   3360  O O   . ASP B  1 240 ? 167.214 157.275 214.212 1.00 116.60 ? 242 ASP B O   1 
ATOM   3361  C CB  . ASP B  1 240 ? 169.198 157.260 212.166 1.00 115.22 ? 242 ASP B CB  1 
ATOM   3362  C CG  . ASP B  1 240 ? 170.490 157.339 212.957 1.00 123.56 ? 242 ASP B CG  1 
ATOM   3363  O OD1 . ASP B  1 240 ? 170.443 157.220 214.199 1.00 121.41 ? 242 ASP B OD1 1 
ATOM   3364  O OD2 . ASP B  1 240 ? 171.556 157.523 212.333 1.00 131.19 ? 242 ASP B OD2 1 
ATOM   3365  N N   . THR B  1 241 ? 167.613 155.099 214.628 1.00 110.88 ? 243 THR B N   1 
ATOM   3366  C CA  . THR B  1 241 ? 166.935 155.128 215.918 1.00 113.71 ? 243 THR B CA  1 
ATOM   3367  C C   . THR B  1 241 ? 167.604 156.061 216.917 1.00 114.47 ? 243 THR B C   1 
ATOM   3368  O O   . THR B  1 241 ? 166.959 156.450 217.895 1.00 112.52 ? 243 THR B O   1 
ATOM   3369  C CB  . THR B  1 241 ? 166.860 153.720 216.509 1.00 116.27 ? 243 THR B CB  1 
ATOM   3370  O OG1 . THR B  1 241 ? 168.146 153.344 217.016 1.00 120.89 ? 243 THR B OG1 1 
ATOM   3371  C CG2 . THR B  1 241 ? 166.426 152.720 215.449 1.00 112.86 ? 243 THR B CG2 1 
ATOM   3372  N N   . ALA B  1 242 ? 168.865 156.426 216.703 1.00 115.28 ? 244 ALA B N   1 
ATOM   3373  C CA  . ALA B  1 242 ? 169.570 157.339 217.593 1.00 114.87 ? 244 ALA B CA  1 
ATOM   3374  C C   . ALA B  1 242 ? 169.434 158.796 217.176 1.00 117.97 ? 244 ALA B C   1 
ATOM   3375  O O   . ALA B  1 242 ? 169.268 159.666 218.035 1.00 117.75 ? 244 ALA B O   1 
ATOM   3376  C CB  . ALA B  1 242 ? 171.053 156.968 217.667 1.00 112.36 ? 244 ALA B CB  1 
ATOM   3377  N N   . ALA B  1 243 ? 169.511 159.085 215.875 1.00 120.20 ? 245 ALA B N   1 
ATOM   3378  C CA  . ALA B  1 243 ? 169.317 160.455 215.412 1.00 119.96 ? 245 ALA B CA  1 
ATOM   3379  C C   . ALA B  1 243 ? 167.890 160.926 215.658 1.00 117.82 ? 245 ALA B C   1 
ATOM   3380  O O   . ALA B  1 243 ? 167.671 162.065 216.087 1.00 114.74 ? 245 ALA B O   1 
ATOM   3381  C CB  . ALA B  1 243 ? 169.670 160.565 213.929 1.00 118.45 ? 245 ALA B CB  1 
ATOM   3382  N N   . TRP B  1 244 ? 166.906 160.065 215.390 1.00 113.64 ? 246 TRP B N   1 
ATOM   3383  C CA  . TRP B  1 244 ? 165.512 160.426 215.617 1.00 102.34 ? 246 TRP B CA  1 
ATOM   3384  C C   . TRP B  1 244 ? 165.208 160.639 217.092 1.00 105.11 ? 246 TRP B C   1 
ATOM   3385  O O   . TRP B  1 244 ? 164.294 161.402 217.423 1.00 109.47 ? 246 TRP B O   1 
ATOM   3386  C CB  . TRP B  1 244 ? 164.594 159.345 215.048 1.00 93.16  ? 246 TRP B CB  1 
ATOM   3387  C CG  . TRP B  1 244 ? 164.375 159.455 213.574 1.00 89.93  ? 246 TRP B CG  1 
ATOM   3388  C CD1 . TRP B  1 244 ? 165.265 159.143 212.591 1.00 97.77  ? 246 TRP B CD1 1 
ATOM   3389  C CD2 . TRP B  1 244 ? 163.183 159.892 212.912 1.00 87.10  ? 246 TRP B CD2 1 
ATOM   3390  N NE1 . TRP B  1 244 ? 164.706 159.366 211.358 1.00 92.06  ? 246 TRP B NE1 1 
ATOM   3391  C CE2 . TRP B  1 244 ? 163.427 159.825 211.527 1.00 89.29  ? 246 TRP B CE2 1 
ATOM   3392  C CE3 . TRP B  1 244 ? 161.935 160.336 213.355 1.00 83.48  ? 246 TRP B CE3 1 
ATOM   3393  C CZ2 . TRP B  1 244 ? 162.470 160.185 210.583 1.00 84.39  ? 246 TRP B CZ2 1 
ATOM   3394  C CZ3 . TRP B  1 244 ? 160.987 160.692 212.416 1.00 86.15  ? 246 TRP B CZ3 1 
ATOM   3395  C CH2 . TRP B  1 244 ? 161.259 160.616 211.047 1.00 85.97  ? 246 TRP B CH2 1 
ATOM   3396  N N   . GLN B  1 245 ? 165.951 159.988 217.981 1.00 106.03 ? 247 GLN B N   1 
ATOM   3397  C CA  . GLN B  1 245 ? 165.759 160.127 219.417 1.00 108.58 ? 247 GLN B CA  1 
ATOM   3398  C C   . GLN B  1 245 ? 166.399 161.387 219.981 1.00 113.20 ? 247 GLN B C   1 
ATOM   3399  O O   . GLN B  1 245 ? 166.248 161.661 221.176 1.00 115.32 ? 247 GLN B O   1 
ATOM   3400  C CB  . GLN B  1 245 ? 166.308 158.894 220.138 1.00 106.77 ? 247 GLN B CB  1 
ATOM   3401  C CG  . GLN B  1 245 ? 165.319 157.746 220.210 1.00 109.34 ? 247 GLN B CG  1 
ATOM   3402  C CD  . GLN B  1 245 ? 165.891 156.530 220.902 1.00 113.68 ? 247 GLN B CD  1 
ATOM   3403  O OE1 . GLN B  1 245 ? 167.083 156.474 221.195 1.00 120.19 ? 247 GLN B OE1 1 
ATOM   3404  N NE2 . GLN B  1 245 ? 165.042 155.546 221.166 1.00 113.49 ? 247 GLN B NE2 1 
ATOM   3405  N N   . ASN B  1 246 ? 167.116 162.150 219.161 1.00 115.32 ? 248 ASN B N   1 
ATOM   3406  C CA  . ASN B  1 246 ? 167.630 163.455 219.555 1.00 116.63 ? 248 ASN B CA  1 
ATOM   3407  C C   . ASN B  1 246 ? 166.803 164.598 218.988 1.00 119.18 ? 248 ASN B C   1 
ATOM   3408  O O   . ASN B  1 246 ? 166.581 165.599 219.676 1.00 121.07 ? 248 ASN B O   1 
ATOM   3409  C CB  . ASN B  1 246 ? 169.086 163.608 219.105 1.00 119.74 ? 248 ASN B CB  1 
ATOM   3410  C CG  . ASN B  1 246 ? 170.071 163.162 220.164 1.00 127.77 ? 248 ASN B CG  1 
ATOM   3411  O OD1 . ASN B  1 246 ? 169.680 162.667 221.221 1.00 130.49 ? 248 ASN B OD1 1 
ATOM   3412  N ND2 . ASN B  1 246 ? 171.357 163.332 219.885 1.00 134.67 ? 248 ASN B ND2 1 
ATOM   3413  N N   . LYS B  1 247 ? 166.345 164.464 217.742 1.00 116.99 ? 249 LYS B N   1 
ATOM   3414  C CA  . LYS B  1 247 ? 165.456 165.463 217.158 1.00 116.13 ? 249 LYS B CA  1 
ATOM   3415  C C   . LYS B  1 247 ? 164.138 165.528 217.915 1.00 112.52 ? 249 LYS B C   1 
ATOM   3416  O O   . LYS B  1 247 ? 163.622 166.617 218.191 1.00 113.76 ? 249 LYS B O   1 
ATOM   3417  C CB  . LYS B  1 247 ? 165.234 165.137 215.685 1.00 108.81 ? 249 LYS B CB  1 
ATOM   3418  C CG  . LYS B  1 247 ? 165.159 166.339 214.768 1.00 113.35 ? 249 LYS B CG  1 
ATOM   3419  C CD  . LYS B  1 247 ? 165.381 165.904 213.331 1.00 119.26 ? 249 LYS B CD  1 
ATOM   3420  C CE  . LYS B  1 247 ? 166.410 164.777 213.285 1.00 121.95 ? 249 LYS B CE  1 
ATOM   3421  N NZ  . LYS B  1 247 ? 166.768 164.336 211.917 1.00 108.97 ? 249 LYS B NZ  1 
ATOM   3422  N N   . LEU B  1 248 ? 163.583 164.373 218.259 1.00 106.62 ? 250 LEU B N   1 
ATOM   3423  C CA  . LEU B  1 248 ? 162.489 164.276 219.213 1.00 103.17 ? 250 LEU B CA  1 
ATOM   3424  C C   . LEU B  1 248 ? 163.095 163.902 220.557 1.00 107.07 ? 250 LEU B C   1 
ATOM   3425  O O   . LEU B  1 248 ? 163.776 162.877 220.666 1.00 111.51 ? 250 LEU B O   1 
ATOM   3426  C CB  . LEU B  1 248 ? 161.456 163.231 218.786 1.00 99.25  ? 250 LEU B CB  1 
ATOM   3427  C CG  . LEU B  1 248 ? 160.672 163.373 217.478 1.00 101.49 ? 250 LEU B CG  1 
ATOM   3428  C CD1 . LEU B  1 248 ? 161.524 163.059 216.259 1.00 100.89 ? 250 LEU B CD1 1 
ATOM   3429  C CD2 . LEU B  1 248 ? 159.449 162.474 217.510 1.00 99.68  ? 250 LEU B CD2 1 
ATOM   3430  N N   . ASN B  1 249 ? 162.858 164.725 221.575 1.00 105.15 ? 251 ASN B N   1 
ATOM   3431  C CA  . ASN B  1 249 ? 163.415 164.412 222.883 1.00 108.40 ? 251 ASN B CA  1 
ATOM   3432  C C   . ASN B  1 249 ? 162.673 163.215 223.452 1.00 113.42 ? 251 ASN B C   1 
ATOM   3433  O O   . ASN B  1 249 ? 161.629 163.366 224.091 1.00 121.73 ? 251 ASN B O   1 
ATOM   3434  C CB  . ASN B  1 249 ? 163.320 165.612 223.825 1.00 107.40 ? 251 ASN B CB  1 
ATOM   3435  C CG  . ASN B  1 249 ? 163.780 166.899 223.176 1.00 118.94 ? 251 ASN B CG  1 
ATOM   3436  O OD1 . ASN B  1 249 ? 164.174 166.912 222.010 1.00 123.37 ? 251 ASN B OD1 1 
ATOM   3437  N ND2 . ASN B  1 249 ? 163.737 167.990 223.930 1.00 115.38 ? 251 ASN B ND2 1 
ATOM   3438  N N   . VAL B  1 250 ? 163.200 162.020 223.211 1.00 110.37 ? 252 VAL B N   1 
ATOM   3439  C CA  . VAL B  1 250 ? 162.532 160.778 223.571 1.00 103.18 ? 252 VAL B CA  1 
ATOM   3440  C C   . VAL B  1 250 ? 163.108 160.271 224.882 1.00 108.46 ? 252 VAL B C   1 
ATOM   3441  O O   . VAL B  1 250 ? 164.326 160.088 225.007 1.00 119.95 ? 252 VAL B O   1 
ATOM   3442  C CB  . VAL B  1 250 ? 162.684 159.724 222.463 1.00 95.96  ? 252 VAL B CB  1 
ATOM   3443  C CG1 . VAL B  1 250 ? 162.107 158.399 222.916 1.00 105.77 ? 252 VAL B CG1 1 
ATOM   3444  C CG2 . VAL B  1 250 ? 162.005 160.195 221.190 1.00 94.20  ? 252 VAL B CG2 1 
ATOM   3445  N N   . THR B  1 251 ? 162.236 160.042 225.859 1.00 108.79 ? 253 THR B N   1 
ATOM   3446  C CA  . THR B  1 251 ? 162.617 159.382 227.104 1.00 118.04 ? 253 THR B CA  1 
ATOM   3447  C C   . THR B  1 251 ? 162.557 157.882 226.856 1.00 133.02 ? 253 THR B C   1 
ATOM   3448  O O   . THR B  1 251 ? 161.477 157.286 226.849 1.00 139.49 ? 253 THR B O   1 
ATOM   3449  C CB  . THR B  1 251 ? 161.700 159.793 228.248 1.00 120.60 ? 253 THR B CB  1 
ATOM   3450  O OG1 . THR B  1 251 ? 161.778 161.211 228.444 1.00 121.89 ? 253 THR B OG1 1 
ATOM   3451  C CG2 . THR B  1 251 ? 162.089 159.072 229.525 1.00 122.88 ? 253 THR B CG2 1 
ATOM   3452  N N   . ARG B  1 252 ? 163.719 157.273 226.642 1.00 134.80 ? 254 ARG B N   1 
ATOM   3453  C CA  . ARG B  1 252 ? 163.764 155.854 226.327 1.00 135.06 ? 254 ARG B CA  1 
ATOM   3454  C C   . ARG B  1 252 ? 163.224 155.034 227.491 1.00 141.80 ? 254 ARG B C   1 
ATOM   3455  O O   . ARG B  1 252 ? 163.450 155.357 228.660 1.00 141.53 ? 254 ARG B O   1 
ATOM   3456  C CB  . ARG B  1 252 ? 165.191 155.432 225.988 1.00 139.64 ? 254 ARG B CB  1 
ATOM   3457  C CG  . ARG B  1 252 ? 166.233 155.918 226.973 1.00 145.14 ? 254 ARG B CG  1 
ATOM   3458  C CD  . ARG B  1 252 ? 167.704 155.677 226.565 1.00 143.59 ? 254 ARG B CD  1 
ATOM   3459  N NE  . ARG B  1 252 ? 168.164 156.386 225.371 1.00 140.81 ? 254 ARG B NE  1 
ATOM   3460  C CZ  . ARG B  1 252 ? 167.841 156.106 224.113 1.00 140.29 ? 254 ARG B CZ  1 
ATOM   3461  N NH1 . ARG B  1 252 ? 167.170 155.012 223.792 1.00 141.02 ? 254 ARG B NH1 1 
ATOM   3462  N NH2 . ARG B  1 252 ? 168.247 156.922 223.145 1.00 139.96 ? 254 ARG B NH2 1 
ATOM   3463  N N   . LYS B  1 253 ? 162.489 153.969 227.158 1.00 141.94 ? 255 LYS B N   1 
ATOM   3464  C CA  . LYS B  1 253 ? 161.866 153.148 228.191 1.00 143.79 ? 255 LYS B CA  1 
ATOM   3465  C C   . LYS B  1 253 ? 162.901 152.509 229.104 1.00 147.22 ? 255 LYS B C   1 
ATOM   3466  O O   . LYS B  1 253 ? 162.604 152.219 230.267 1.00 148.14 ? 255 LYS B O   1 
ATOM   3467  C CB  . LYS B  1 253 ? 160.983 152.077 227.552 1.00 136.68 ? 255 LYS B CB  1 
ATOM   3468  C CG  . LYS B  1 253 ? 159.495 152.332 227.715 1.00 138.60 ? 255 LYS B CG  1 
ATOM   3469  C CD  . LYS B  1 253 ? 158.680 151.503 226.740 1.00 140.02 ? 255 LYS B CD  1 
ATOM   3470  C CE  . LYS B  1 253 ? 157.566 150.755 227.452 1.00 143.05 ? 255 LYS B CE  1 
ATOM   3471  N NZ  . LYS B  1 253 ? 156.756 151.657 228.317 1.00 133.24 ? 255 LYS B NZ  1 
ATOM   3472  N N   . ASN B  1 254 ? 164.116 152.278 228.601 1.00 148.37 ? 256 ASN B N   1 
ATOM   3473  C CA  . ASN B  1 254 ? 165.176 151.757 229.457 1.00 147.60 ? 256 ASN B CA  1 
ATOM   3474  C C   . ASN B  1 254 ? 165.527 152.734 230.571 1.00 154.93 ? 256 ASN B C   1 
ATOM   3475  O O   . ASN B  1 254 ? 165.659 152.329 231.732 1.00 157.80 ? 256 ASN B O   1 
ATOM   3476  C CB  . ASN B  1 254 ? 166.413 151.434 228.621 1.00 145.73 ? 256 ASN B CB  1 
ATOM   3477  C CG  . ASN B  1 254 ? 166.065 151.047 227.198 1.00 146.41 ? 256 ASN B CG  1 
ATOM   3478  O OD1 . ASN B  1 254 ? 166.111 151.874 226.288 1.00 147.21 ? 256 ASN B OD1 1 
ATOM   3479  N ND2 . ASN B  1 254 ? 165.711 149.783 227.000 1.00 144.05 ? 256 ASN B ND2 1 
ATOM   3480  N N   . ASP B  1 255 ? 165.677 154.020 230.246 1.00 157.16 ? 257 ASP B N   1 
ATOM   3481  C CA  . ASP B  1 255 ? 165.919 155.021 231.279 1.00 160.73 ? 257 ASP B CA  1 
ATOM   3482  C C   . ASP B  1 255 ? 164.691 155.224 232.156 1.00 159.06 ? 257 ASP B C   1 
ATOM   3483  O O   . ASP B  1 255 ? 164.816 155.396 233.373 1.00 161.76 ? 257 ASP B O   1 
ATOM   3484  C CB  . ASP B  1 255 ? 166.346 156.344 230.645 1.00 162.25 ? 257 ASP B CB  1 
ATOM   3485  C CG  . ASP B  1 255 ? 167.723 156.271 230.020 1.00 166.83 ? 257 ASP B CG  1 
ATOM   3486  O OD1 . ASP B  1 255 ? 168.350 155.193 230.087 1.00 169.55 ? 257 ASP B OD1 1 
ATOM   3487  O OD2 . ASP B  1 255 ? 168.177 157.290 229.460 1.00 167.73 ? 257 ASP B OD2 1 
ATOM   3488  N N   . TYR B  1 256 ? 163.499 155.210 231.555 1.00 152.80 ? 258 TYR B N   1 
ATOM   3489  C CA  . TYR B  1 256 ? 162.263 155.318 232.317 1.00 151.58 ? 258 TYR B CA  1 
ATOM   3490  C C   . TYR B  1 256 ? 162.083 154.132 233.257 1.00 153.66 ? 258 TYR B C   1 
ATOM   3491  O O   . TYR B  1 256 ? 161.282 154.206 234.193 1.00 151.82 ? 258 TYR B O   1 
ATOM   3492  C CB  . TYR B  1 256 ? 161.074 155.410 231.355 1.00 150.29 ? 258 TYR B CB  1 
ATOM   3493  C CG  . TYR B  1 256 ? 159.708 155.372 232.006 1.00 153.41 ? 258 TYR B CG  1 
ATOM   3494  C CD1 . TYR B  1 256 ? 159.431 156.144 233.128 1.00 149.97 ? 258 TYR B CD1 1 
ATOM   3495  C CD2 . TYR B  1 256 ? 158.714 154.529 231.531 1.00 154.17 ? 258 TYR B CD2 1 
ATOM   3496  C CE1 . TYR B  1 256 ? 158.192 156.110 233.729 1.00 151.49 ? 258 TYR B CE1 1 
ATOM   3497  C CE2 . TYR B  1 256 ? 157.470 154.486 232.130 1.00 156.98 ? 258 TYR B CE2 1 
ATOM   3498  C CZ  . TYR B  1 256 ? 157.216 155.277 233.229 1.00 156.48 ? 258 TYR B CZ  1 
ATOM   3499  O OH  . TYR B  1 256 ? 155.980 155.234 233.832 1.00 155.02 ? 258 TYR B OH  1 
ATOM   3500  N N   . LYS B  1 257 ? 162.801 153.037 233.017 1.00 154.52 ? 259 LYS B N   1 
ATOM   3501  C CA  . LYS B  1 257 ? 162.787 151.879 233.894 1.00 156.01 ? 259 LYS B CA  1 
ATOM   3502  C C   . LYS B  1 257 ? 163.929 151.881 234.900 1.00 161.55 ? 259 LYS B C   1 
ATOM   3503  O O   . LYS B  1 257 ? 163.766 151.341 235.999 1.00 160.19 ? 259 LYS B O   1 
ATOM   3504  C CB  . LYS B  1 257 ? 162.853 150.593 233.056 1.00 152.34 ? 259 LYS B CB  1 
ATOM   3505  C CG  . LYS B  1 257 ? 162.741 149.296 233.844 1.00 151.69 ? 259 LYS B CG  1 
ATOM   3506  C CD  . LYS B  1 257 ? 161.543 149.300 234.776 1.00 147.86 ? 259 LYS B CD  1 
ATOM   3507  C CE  . LYS B  1 257 ? 160.245 149.427 234.003 1.00 145.10 ? 259 LYS B CE  1 
ATOM   3508  N NZ  . LYS B  1 257 ? 159.154 148.617 234.611 1.00 139.04 ? 259 LYS B NZ  1 
ATOM   3509  N N   . ASP B  1 258 ? 165.066 152.490 234.561 1.00 166.26 ? 260 ASP B N   1 
ATOM   3510  C CA  . ASP B  1 258 ? 166.255 152.439 235.402 1.00 170.50 ? 260 ASP B CA  1 
ATOM   3511  C C   . ASP B  1 258 ? 166.573 153.770 236.076 1.00 170.19 ? 260 ASP B C   1 
ATOM   3512  O O   . ASP B  1 258 ? 167.634 153.895 236.699 1.00 173.50 ? 260 ASP B O   1 
ATOM   3513  C CB  . ASP B  1 258 ? 167.458 151.961 234.585 1.00 174.85 ? 260 ASP B CB  1 
ATOM   3514  C CG  . ASP B  1 258 ? 167.501 150.452 234.445 1.00 174.71 ? 260 ASP B CG  1 
ATOM   3515  O OD1 . ASP B  1 258 ? 166.841 149.760 235.250 1.00 175.80 ? 260 ASP B OD1 1 
ATOM   3516  O OD2 . ASP B  1 258 ? 168.192 149.957 233.530 1.00 172.30 ? 260 ASP B OD2 1 
ATOM   3517  N N   . ALA B  1 259 ? 165.685 154.761 235.970 1.00 164.66 ? 261 ALA B N   1 
ATOM   3518  C CA  . ALA B  1 259 ? 165.827 156.048 236.658 1.00 163.69 ? 261 ALA B CA  1 
ATOM   3519  C C   . ALA B  1 259 ? 167.088 156.796 236.238 1.00 164.42 ? 261 ALA B C   1 
ATOM   3520  O O   . ALA B  1 259 ? 167.656 157.563 237.020 1.00 159.20 ? 261 ALA B O   1 
ATOM   3521  C CB  . ALA B  1 259 ? 165.794 155.874 238.180 1.00 153.84 ? 261 ALA B CB  1 
ATOM   3522  N N   . ASN B  1 260 ? 167.537 156.585 235.005 1.00 165.21 ? 262 ASN B N   1 
ATOM   3523  C CA  . ASN B  1 260 ? 168.690 157.316 234.502 1.00 164.76 ? 262 ASN B CA  1 
ATOM   3524  C C   . ASN B  1 260 ? 168.312 158.749 234.149 1.00 170.40 ? 262 ASN B C   1 
ATOM   3525  O O   . ASN B  1 260 ? 167.219 159.014 233.640 1.00 172.81 ? 262 ASN B O   1 
ATOM   3526  C CB  . ASN B  1 260 ? 169.273 156.615 233.275 1.00 167.52 ? 262 ASN B CB  1 
ATOM   3527  C CG  . ASN B  1 260 ? 169.287 155.110 233.417 1.00 170.00 ? 262 ASN B CG  1 
ATOM   3528  O OD1 . ASN B  1 260 ? 169.224 154.581 234.525 1.00 171.16 ? 262 ASN B OD1 1 
ATOM   3529  N ND2 . ASN B  1 260 ? 169.368 154.409 232.292 1.00 172.14 ? 262 ASN B ND2 1 
ATOM   3530  N N   . ASP B  1 261 ? 169.234 159.673 234.424 1.00 173.52 ? 263 ASP B N   1 
ATOM   3531  C CA  . ASP B  1 261 ? 169.158 161.062 233.971 1.00 177.22 ? 263 ASP B CA  1 
ATOM   3532  C C   . ASP B  1 261 ? 167.873 161.718 234.500 1.00 174.84 ? 263 ASP B C   1 
ATOM   3533  O O   . ASP B  1 261 ? 166.910 161.985 233.778 1.00 175.60 ? 263 ASP B O   1 
ATOM   3534  C CB  . ASP B  1 261 ? 169.295 161.108 232.436 1.00 181.01 ? 263 ASP B CB  1 
ATOM   3535  C CG  . ASP B  1 261 ? 168.743 162.383 231.797 1.00 184.24 ? 263 ASP B CG  1 
ATOM   3536  O OD1 . ASP B  1 261 ? 168.681 163.438 232.462 1.00 183.00 ? 263 ASP B OD1 1 
ATOM   3537  O OD2 . ASP B  1 261 ? 168.361 162.321 230.610 1.00 181.18 ? 263 ASP B OD2 1 
ATOM   3538  N N   . ILE B  1 262 ? 167.849 161.878 235.823 1.00 170.11 ? 264 ILE B N   1 
ATOM   3539  C CA  . ILE B  1 262 ? 166.832 162.678 236.493 1.00 164.55 ? 264 ILE B CA  1 
ATOM   3540  C C   . ILE B  1 262 ? 167.513 163.552 237.535 1.00 165.02 ? 264 ILE B C   1 
ATOM   3541  O O   . ILE B  1 262 ? 168.623 163.261 237.991 1.00 169.35 ? 264 ILE B O   1 
ATOM   3542  C CB  . ILE B  1 262 ? 165.727 161.827 237.163 1.00 164.99 ? 264 ILE B CB  1 
ATOM   3543  C CG1 . ILE B  1 262 ? 166.238 161.195 238.457 1.00 164.76 ? 264 ILE B CG1 1 
ATOM   3544  C CG2 . ILE B  1 262 ? 165.213 160.758 236.223 1.00 165.64 ? 264 ILE B CG2 1 
ATOM   3545  C CD1 . ILE B  1 262 ? 165.324 160.123 239.003 1.00 159.94 ? 264 ILE B CD1 1 
ATOM   3546  N N   . ASP B  1 263 ? 166.842 164.639 237.903 1.00 163.75 ? 265 ASP B N   1 
ATOM   3547  C CA  . ASP B  1 263 ? 167.301 165.451 239.019 1.00 166.80 ? 265 ASP B CA  1 
ATOM   3548  C C   . ASP B  1 263 ? 166.857 164.830 240.338 1.00 168.59 ? 265 ASP B C   1 
ATOM   3549  O O   . ASP B  1 263 ? 165.758 164.285 240.455 1.00 171.37 ? 265 ASP B O   1 
ATOM   3550  C CB  . ASP B  1 263 ? 166.761 166.876 238.905 1.00 167.02 ? 265 ASP B CB  1 
ATOM   3551  C CG  . ASP B  1 263 ? 167.304 167.611 237.697 1.00 172.40 ? 265 ASP B CG  1 
ATOM   3552  O OD1 . ASP B  1 263 ? 168.360 167.199 237.174 1.00 175.02 ? 265 ASP B OD1 1 
ATOM   3553  O OD2 . ASP B  1 263 ? 166.675 168.603 237.271 1.00 174.53 ? 265 ASP B OD2 1 
ATOM   3554  N N   . VAL B  1 264 ? 167.728 164.911 241.341 1.00 168.82 ? 266 VAL B N   1 
ATOM   3555  C CA  . VAL B  1 264 ? 167.397 164.430 242.670 1.00 170.48 ? 266 VAL B CA  1 
ATOM   3556  C C   . VAL B  1 264 ? 167.006 165.560 243.617 1.00 174.39 ? 266 VAL B C   1 
ATOM   3557  O O   . VAL B  1 264 ? 166.213 165.332 244.538 1.00 170.15 ? 266 VAL B O   1 
ATOM   3558  C CB  . VAL B  1 264 ? 168.548 163.590 243.264 1.00 168.49 ? 266 VAL B CB  1 
ATOM   3559  C CG1 . VAL B  1 264 ? 169.026 162.561 242.252 1.00 163.31 ? 266 VAL B CG1 1 
ATOM   3560  C CG2 . VAL B  1 264 ? 169.701 164.478 243.705 1.00 169.64 ? 266 VAL B CG2 1 
ATOM   3561  N N   . ASN B  1 265 ? 167.527 166.771 243.418 1.00 179.33 ? 267 ASN B N   1 
ATOM   3562  C CA  . ASN B  1 265 ? 167.120 167.913 244.223 1.00 181.75 ? 267 ASN B CA  1 
ATOM   3563  C C   . ASN B  1 265 ? 165.782 168.489 243.785 1.00 178.01 ? 267 ASN B C   1 
ATOM   3564  O O   . ASN B  1 265 ? 165.223 169.329 244.498 1.00 179.02 ? 267 ASN B O   1 
ATOM   3565  C CB  . ASN B  1 265 ? 168.194 169.002 244.168 1.00 183.26 ? 267 ASN B CB  1 
ATOM   3566  C CG  . ASN B  1 265 ? 169.277 168.801 245.208 1.00 186.01 ? 267 ASN B CG  1 
ATOM   3567  O OD1 . ASN B  1 265 ? 169.080 168.097 246.197 1.00 185.73 ? 267 ASN B OD1 1 
ATOM   3568  N ND2 . ASN B  1 265 ? 170.432 169.417 244.985 1.00 188.87 ? 267 ASN B ND2 1 
ATOM   3569  N N   . LYS B  1 266 ? 165.262 168.059 242.638 1.00 172.60 ? 268 LYS B N   1 
ATOM   3570  C CA  . LYS B  1 266 ? 163.993 168.536 242.107 1.00 172.84 ? 268 LYS B CA  1 
ATOM   3571  C C   . LYS B  1 266 ? 162.884 167.501 242.230 1.00 174.22 ? 268 LYS B C   1 
ATOM   3572  O O   . LYS B  1 266 ? 161.762 167.844 242.616 1.00 171.48 ? 268 LYS B O   1 
ATOM   3573  C CB  . LYS B  1 266 ? 164.180 168.958 240.639 1.00 169.73 ? 268 LYS B CB  1 
ATOM   3574  C CG  . LYS B  1 266 ? 162.986 169.650 239.980 1.00 167.65 ? 268 LYS B CG  1 
ATOM   3575  C CD  . LYS B  1 266 ? 162.011 168.645 239.382 1.00 171.60 ? 268 LYS B CD  1 
ATOM   3576  C CE  . LYS B  1 266 ? 162.754 167.419 238.873 1.00 172.12 ? 268 LYS B CE  1 
ATOM   3577  N NZ  . LYS B  1 266 ? 161.844 166.418 238.272 1.00 163.20 ? 268 LYS B NZ  1 
ATOM   3578  N N   . TRP B  1 267 ? 163.164 166.238 241.895 1.00 174.44 ? 269 TRP B N   1 
ATOM   3579  C CA  . TRP B  1 267 ? 162.155 165.195 242.058 1.00 168.58 ? 269 TRP B CA  1 
ATOM   3580  C C   . TRP B  1 267 ? 161.766 165.041 243.521 1.00 171.06 ? 269 TRP B C   1 
ATOM   3581  O O   . TRP B  1 267 ? 160.592 164.822 243.841 1.00 171.08 ? 269 TRP B O   1 
ATOM   3582  C CB  . TRP B  1 267 ? 162.663 163.864 241.499 1.00 164.31 ? 269 TRP B CB  1 
ATOM   3583  C CG  . TRP B  1 267 ? 162.403 163.657 240.031 1.00 162.64 ? 269 TRP B CG  1 
ATOM   3584  C CD1 . TRP B  1 267 ? 163.258 163.920 239.002 1.00 166.97 ? 269 TRP B CD1 1 
ATOM   3585  C CD2 . TRP B  1 267 ? 161.207 163.140 239.435 1.00 155.58 ? 269 TRP B CD2 1 
ATOM   3586  N NE1 . TRP B  1 267 ? 162.670 163.601 237.803 1.00 161.33 ? 269 TRP B NE1 1 
ATOM   3587  C CE2 . TRP B  1 267 ? 161.410 163.120 238.041 1.00 154.52 ? 269 TRP B CE2 1 
ATOM   3588  C CE3 . TRP B  1 267 ? 159.985 162.693 239.944 1.00 152.54 ? 269 TRP B CE3 1 
ATOM   3589  C CZ2 . TRP B  1 267 ? 160.438 162.671 237.152 1.00 146.67 ? 269 TRP B CZ2 1 
ATOM   3590  C CZ3 . TRP B  1 267 ? 159.021 162.248 239.059 1.00 151.04 ? 269 TRP B CZ3 1 
ATOM   3591  C CH2 . TRP B  1 267 ? 159.253 162.240 237.679 1.00 148.62 ? 269 TRP B CH2 1 
ATOM   3592  N N   . LYS B  1 268 ? 162.742 165.153 244.425 1.00 173.56 ? 270 LYS B N   1 
ATOM   3593  C CA  . LYS B  1 268 ? 162.458 165.083 245.853 1.00 171.61 ? 270 LYS B CA  1 
ATOM   3594  C C   . LYS B  1 268 ? 161.545 166.208 246.318 1.00 172.42 ? 270 LYS B C   1 
ATOM   3595  O O   . LYS B  1 268 ? 160.902 166.075 247.364 1.00 168.92 ? 270 LYS B O   1 
ATOM   3596  C CB  . LYS B  1 268 ? 163.762 165.120 246.651 1.00 165.70 ? 270 LYS B CB  1 
ATOM   3597  C CG  . LYS B  1 268 ? 164.168 163.789 247.261 1.00 157.42 ? 270 LYS B CG  1 
ATOM   3598  C CD  . LYS B  1 268 ? 164.993 162.966 246.288 1.00 158.48 ? 270 LYS B CD  1 
ATOM   3599  C CE  . LYS B  1 268 ? 165.544 161.717 246.950 1.00 148.10 ? 270 LYS B CE  1 
ATOM   3600  N NZ  . LYS B  1 268 ? 166.592 161.066 246.117 1.00 138.84 ? 270 LYS B NZ  1 
ATOM   3601  N N   . ALA B  1 269 ? 161.478 167.314 245.576 1.00 175.25 ? 271 ALA B N   1 
ATOM   3602  C CA  . ALA B  1 269 ? 160.630 168.430 245.979 1.00 174.19 ? 271 ALA B CA  1 
ATOM   3603  C C   . ALA B  1 269 ? 159.153 168.102 245.787 1.00 174.98 ? 271 ALA B C   1 
ATOM   3604  O O   . ALA B  1 269 ? 158.371 168.121 246.743 1.00 173.07 ? 271 ALA B O   1 
ATOM   3605  C CB  . ALA B  1 269 ? 161.010 169.689 245.195 1.00 168.57 ? 271 ALA B CB  1 
ATOM   3606  N N   . LYS B  1 270 ? 158.755 167.801 244.549 1.00 173.94 ? 272 LYS B N   1 
ATOM   3607  C CA  . LYS B  1 270 ? 157.349 167.525 244.274 1.00 170.13 ? 272 LYS B CA  1 
ATOM   3608  C C   . LYS B  1 270 ? 156.909 166.199 244.883 1.00 166.85 ? 272 LYS B C   1 
ATOM   3609  O O   . LYS B  1 270 ? 155.757 166.059 245.310 1.00 161.81 ? 272 LYS B O   1 
ATOM   3610  C CB  . LYS B  1 270 ? 157.098 167.535 242.766 1.00 163.79 ? 272 LYS B CB  1 
ATOM   3611  C CG  . LYS B  1 270 ? 157.032 168.931 242.164 1.00 160.15 ? 272 LYS B CG  1 
ATOM   3612  C CD  . LYS B  1 270 ? 156.044 169.008 241.009 1.00 157.71 ? 272 LYS B CD  1 
ATOM   3613  C CE  . LYS B  1 270 ? 156.002 167.716 240.211 1.00 156.14 ? 272 LYS B CE  1 
ATOM   3614  N NZ  . LYS B  1 270 ? 155.662 167.962 238.784 1.00 138.57 ? 272 LYS B NZ  1 
ATOM   3615  N N   . LEU B  1 271 ? 157.805 165.217 244.932 1.00 167.50 ? 273 LEU B N   1 
ATOM   3616  C CA  . LEU B  1 271 ? 157.477 163.890 245.433 1.00 167.48 ? 273 LEU B CA  1 
ATOM   3617  C C   . LEU B  1 271 ? 157.854 163.694 246.897 1.00 169.38 ? 273 LEU B C   1 
ATOM   3618  O O   . LEU B  1 271 ? 157.733 162.577 247.409 1.00 171.80 ? 273 LEU B O   1 
ATOM   3619  C CB  . LEU B  1 271 ? 158.150 162.812 244.576 1.00 168.80 ? 273 LEU B CB  1 
ATOM   3620  C CG  . LEU B  1 271 ? 157.496 162.418 243.246 1.00 165.79 ? 273 LEU B CG  1 
ATOM   3621  C CD1 . LEU B  1 271 ? 156.128 161.798 243.493 1.00 161.66 ? 273 LEU B CD1 1 
ATOM   3622  C CD2 . LEU B  1 271 ? 157.394 163.583 242.268 1.00 162.93 ? 273 LEU B CD2 1 
ATOM   3623  N N   . GLY B  1 272 ? 158.305 164.742 247.577 1.00 166.79 ? 274 GLY B N   1 
ATOM   3624  C CA  . GLY B  1 272 ? 158.647 164.639 248.984 1.00 159.90 ? 274 GLY B CA  1 
ATOM   3625  C C   . GLY B  1 272 ? 159.904 163.830 249.238 1.00 153.00 ? 274 GLY B C   1 
ATOM   3626  O O   . GLY B  1 272 ? 160.072 163.246 250.308 1.00 132.43 ? 274 GLY B O   1 
ATOM   3627  N N   . ALA C  1 24  ? 170.975 161.424 127.230 1.00 113.26 ? 26  ALA C N   1 
ATOM   3628  C CA  . ALA C  1 24  ? 169.695 162.019 127.591 1.00 112.38 ? 26  ALA C CA  1 
ATOM   3629  C C   . ALA C  1 24  ? 168.833 161.028 128.364 1.00 112.91 ? 26  ALA C C   1 
ATOM   3630  O O   . ALA C  1 24  ? 168.900 159.823 128.123 1.00 113.30 ? 26  ALA C O   1 
ATOM   3631  C CB  . ALA C  1 24  ? 168.964 162.499 126.346 1.00 108.13 ? 26  ALA C CB  1 
ATOM   3632  N N   . PRO C  1 25  ? 168.035 161.536 129.302 1.00 109.86 ? 27  PRO C N   1 
ATOM   3633  C CA  . PRO C  1 25  ? 167.135 160.658 130.057 1.00 107.05 ? 27  PRO C CA  1 
ATOM   3634  C C   . PRO C  1 25  ? 166.154 159.953 129.135 1.00 108.60 ? 27  PRO C C   1 
ATOM   3635  O O   . PRO C  1 25  ? 165.726 160.499 128.116 1.00 105.23 ? 27  PRO C O   1 
ATOM   3636  C CB  . PRO C  1 25  ? 166.420 161.623 131.005 1.00 105.15 ? 27  PRO C CB  1 
ATOM   3637  C CG  . PRO C  1 25  ? 167.387 162.739 131.186 1.00 106.05 ? 27  PRO C CG  1 
ATOM   3638  C CD  . PRO C  1 25  ? 168.052 162.903 129.848 1.00 110.69 ? 27  PRO C CD  1 
ATOM   3639  N N   . VAL C  1 26  ? 165.802 158.723 129.501 1.00 107.94 ? 28  VAL C N   1 
ATOM   3640  C CA  . VAL C  1 26  ? 164.924 157.894 128.688 1.00 104.27 ? 28  VAL C CA  1 
ATOM   3641  C C   . VAL C  1 26  ? 163.977 157.125 129.599 1.00 102.26 ? 28  VAL C C   1 
ATOM   3642  O O   . VAL C  1 26  ? 164.267 156.888 130.775 1.00 101.28 ? 28  VAL C O   1 
ATOM   3643  C CB  . VAL C  1 26  ? 165.736 156.930 127.790 1.00 99.20  ? 28  VAL C CB  1 
ATOM   3644  C CG1 . VAL C  1 26  ? 166.280 155.768 128.605 1.00 92.52  ? 28  VAL C CG1 1 
ATOM   3645  C CG2 . VAL C  1 26  ? 164.895 156.437 126.620 1.00 101.45 ? 28  VAL C CG2 1 
ATOM   3646  N N   . ILE C  1 27  ? 162.827 156.749 129.045 1.00 98.21  ? 29  ILE C N   1 
ATOM   3647  C CA  . ILE C  1 27  ? 161.873 155.859 129.695 1.00 95.45  ? 29  ILE C CA  1 
ATOM   3648  C C   . ILE C  1 27  ? 161.882 154.546 128.921 1.00 98.69  ? 29  ILE C C   1 
ATOM   3649  O O   . ILE C  1 27  ? 161.805 154.544 127.685 1.00 102.72 ? 29  ILE C O   1 
ATOM   3650  C CB  . ILE C  1 27  ? 160.463 156.479 129.776 1.00 91.18  ? 29  ILE C CB  1 
ATOM   3651  C CG1 . ILE C  1 27  ? 159.619 155.789 130.850 1.00 89.99  ? 29  ILE C CG1 1 
ATOM   3652  C CG2 . ILE C  1 27  ? 159.749 156.496 128.429 1.00 93.69  ? 29  ILE C CG2 1 
ATOM   3653  C CD1 . ILE C  1 27  ? 159.614 156.502 132.172 1.00 87.15  ? 29  ILE C CD1 1 
ATOM   3654  N N   . LYS C  1 28  ? 162.051 153.438 129.636 1.00 94.81  ? 30  LYS C N   1 
ATOM   3655  C CA  . LYS C  1 28  ? 162.191 152.149 128.976 1.00 93.53  ? 30  LYS C CA  1 
ATOM   3656  C C   . LYS C  1 28  ? 161.884 151.040 129.969 1.00 102.04 ? 30  LYS C C   1 
ATOM   3657  O O   . LYS C  1 28  ? 161.855 151.255 131.183 1.00 100.87 ? 30  LYS C O   1 
ATOM   3658  C CB  . LYS C  1 28  ? 163.595 151.968 128.392 1.00 94.38  ? 30  LYS C CB  1 
ATOM   3659  C CG  . LYS C  1 28  ? 164.684 151.822 129.439 1.00 101.79 ? 30  LYS C CG  1 
ATOM   3660  C CD  . LYS C  1 28  ? 166.049 152.145 128.860 1.00 102.09 ? 30  LYS C CD  1 
ATOM   3661  C CE  . LYS C  1 28  ? 166.667 150.929 128.195 1.00 107.38 ? 30  LYS C CE  1 
ATOM   3662  N NZ  . LYS C  1 28  ? 166.293 149.669 128.891 1.00 111.18 ? 30  LYS C NZ  1 
ATOM   3663  N N   . ALA C  1 29  ? 161.658 149.848 129.428 1.00 104.13 ? 31  ALA C N   1 
ATOM   3664  C CA  . ALA C  1 29  ? 161.415 148.674 130.248 1.00 103.11 ? 31  ALA C CA  1 
ATOM   3665  C C   . ALA C  1 29  ? 162.720 148.141 130.823 1.00 101.57 ? 31  ALA C C   1 
ATOM   3666  O O   . ALA C  1 29  ? 163.786 148.252 130.212 1.00 103.65 ? 31  ALA C O   1 
ATOM   3667  C CB  . ALA C  1 29  ? 160.721 147.583 129.434 1.00 99.66  ? 31  ALA C CB  1 
ATOM   3668  N N   . GLY C  1 30  ? 162.627 147.558 132.014 1.00 102.05 ? 32  GLY C N   1 
ATOM   3669  C CA  . GLY C  1 30  ? 163.778 146.930 132.629 1.00 103.93 ? 32  GLY C CA  1 
ATOM   3670  C C   . GLY C  1 30  ? 164.049 145.557 132.051 1.00 109.20 ? 32  GLY C C   1 
ATOM   3671  O O   . GLY C  1 30  ? 163.726 145.292 130.890 1.00 108.50 ? 32  GLY C O   1 
ATOM   3672  N N   . THR C  1 31  ? 164.641 144.673 132.850 1.00 112.19 ? 33  THR C N   1 
ATOM   3673  C CA  . THR C  1 31  ? 164.942 143.316 132.416 1.00 111.74 ? 33  THR C CA  1 
ATOM   3674  C C   . THR C  1 31  ? 163.878 142.312 132.833 1.00 113.74 ? 33  THR C C   1 
ATOM   3675  O O   . THR C  1 31  ? 164.054 141.112 132.597 1.00 115.79 ? 33  THR C O   1 
ATOM   3676  C CB  . THR C  1 31  ? 166.305 142.876 132.959 1.00 112.05 ? 33  THR C CB  1 
ATOM   3677  O OG1 . THR C  1 31  ? 166.456 143.339 134.306 1.00 112.01 ? 33  THR C OG1 1 
ATOM   3678  C CG2 . THR C  1 31  ? 167.425 143.448 132.106 1.00 112.57 ? 33  THR C CG2 1 
ATOM   3679  N N   . ALA C  1 32  ? 162.786 142.764 133.441 1.00 115.82 ? 34  ALA C N   1 
ATOM   3680  C CA  . ALA C  1 32  ? 161.713 141.891 133.890 1.00 114.30 ? 34  ALA C CA  1 
ATOM   3681  C C   . ALA C  1 32  ? 160.377 142.448 133.422 1.00 115.17 ? 34  ALA C C   1 
ATOM   3682  O O   . ALA C  1 32  ? 160.281 143.584 132.949 1.00 117.32 ? 34  ALA C O   1 
ATOM   3683  C CB  . ALA C  1 32  ? 161.721 141.731 135.415 1.00 105.61 ? 34  ALA C CB  1 
ATOM   3684  N N   . THR C  1 33  ? 159.339 141.626 133.551 1.00 113.47 ? 35  THR C N   1 
ATOM   3685  C CA  . THR C  1 33  ? 158.004 142.033 133.136 1.00 114.89 ? 35  THR C CA  1 
ATOM   3686  C C   . THR C  1 33  ? 157.514 143.205 133.978 1.00 115.51 ? 35  THR C C   1 
ATOM   3687  O O   . THR C  1 33  ? 157.627 143.192 135.207 1.00 114.89 ? 35  THR C O   1 
ATOM   3688  C CB  . THR C  1 33  ? 157.034 140.859 133.256 1.00 114.64 ? 35  THR C CB  1 
ATOM   3689  O OG1 . THR C  1 33  ? 157.611 139.698 132.644 1.00 120.03 ? 35  THR C OG1 1 
ATOM   3690  C CG2 . THR C  1 33  ? 155.718 141.183 132.568 1.00 112.53 ? 35  THR C CG2 1 
ATOM   3691  N N   . ASP C  1 34  ? 156.969 144.219 133.303 1.00 114.60 ? 36  ASP C N   1 
ATOM   3692  C CA  . ASP C  1 34  ? 156.407 145.403 133.957 1.00 111.74 ? 36  ASP C CA  1 
ATOM   3693  C C   . ASP C  1 34  ? 157.440 146.106 134.834 1.00 110.51 ? 36  ASP C C   1 
ATOM   3694  O O   . ASP C  1 34  ? 157.119 146.636 135.899 1.00 112.22 ? 36  ASP C O   1 
ATOM   3695  C CB  . ASP C  1 34  ? 155.159 145.046 134.766 1.00 113.63 ? 36  ASP C CB  1 
ATOM   3696  C CG  . ASP C  1 34  ? 154.012 144.586 133.891 1.00 123.10 ? 36  ASP C CG  1 
ATOM   3697  O OD1 . ASP C  1 34  ? 154.196 144.512 132.659 1.00 122.53 ? 36  ASP C OD1 1 
ATOM   3698  O OD2 . ASP C  1 34  ? 152.927 144.296 134.437 1.00 127.58 ? 36  ASP C OD2 1 
ATOM   3699  N N   . SER C  1 35  ? 158.689 146.119 134.381 1.00 107.00 ? 37  SER C N   1 
ATOM   3700  C CA  . SER C  1 35  ? 159.765 146.814 135.073 1.00 102.07 ? 37  SER C CA  1 
ATOM   3701  C C   . SER C  1 35  ? 160.077 148.107 134.334 1.00 102.97 ? 37  SER C C   1 
ATOM   3702  O O   . SER C  1 35  ? 160.195 148.110 133.105 1.00 108.35 ? 37  SER C O   1 
ATOM   3703  C CB  . SER C  1 35  ? 161.013 145.937 135.171 1.00 105.17 ? 37  SER C CB  1 
ATOM   3704  O OG  . SER C  1 35  ? 161.325 145.357 133.918 1.00 118.40 ? 37  SER C OG  1 
ATOM   3705  N N   . THR C  1 36  ? 160.209 149.199 135.081 1.00 99.70  ? 38  THR C N   1 
ATOM   3706  C CA  . THR C  1 36  ? 160.343 150.533 134.513 1.00 98.58  ? 38  THR C CA  1 
ATOM   3707  C C   . THR C  1 36  ? 161.671 151.149 134.924 1.00 100.60 ? 38  THR C C   1 
ATOM   3708  O O   . THR C  1 36  ? 162.078 151.042 136.085 1.00 103.65 ? 38  THR C O   1 
ATOM   3709  C CB  . THR C  1 36  ? 159.190 151.435 134.964 1.00 97.99  ? 38  THR C CB  1 
ATOM   3710  O OG1 . THR C  1 36  ? 157.942 150.780 134.708 1.00 105.83 ? 38  THR C OG1 1 
ATOM   3711  C CG2 . THR C  1 36  ? 159.226 152.762 134.226 1.00 97.08  ? 38  THR C CG2 1 
ATOM   3712  N N   . GLU C  1 37  ? 162.340 151.791 133.970 1.00 96.76  ? 39  GLU C N   1 
ATOM   3713  C CA  . GLU C  1 37  ? 163.541 152.576 134.226 1.00 94.06  ? 39  GLU C CA  1 
ATOM   3714  C C   . GLU C  1 37  ? 163.306 153.986 133.707 1.00 97.93  ? 39  GLU C C   1 
ATOM   3715  O O   . GLU C  1 37  ? 163.102 154.180 132.504 1.00 101.10 ? 39  GLU C O   1 
ATOM   3716  C CB  . GLU C  1 37  ? 164.766 151.954 133.556 1.00 96.91  ? 39  GLU C CB  1 
ATOM   3717  C CG  . GLU C  1 37  ? 165.298 150.719 134.253 1.00 103.96 ? 39  GLU C CG  1 
ATOM   3718  C CD  . GLU C  1 37  ? 166.332 149.991 133.424 1.00 110.96 ? 39  GLU C CD  1 
ATOM   3719  O OE1 . GLU C  1 37  ? 166.801 150.567 132.420 1.00 110.81 ? 39  GLU C OE1 1 
ATOM   3720  O OE2 . GLU C  1 37  ? 166.676 148.843 133.773 1.00 109.50 ? 39  GLU C OE2 1 
ATOM   3721  N N   . ALA C  1 38  ? 163.335 154.964 134.609 1.00 96.72  ? 40  ALA C N   1 
ATOM   3722  C CA  . ALA C  1 38  ? 163.110 156.361 134.261 1.00 90.00  ? 40  ALA C CA  1 
ATOM   3723  C C   . ALA C  1 38  ? 164.314 157.174 134.702 1.00 94.28  ? 40  ALA C C   1 
ATOM   3724  O O   . ALA C  1 38  ? 164.718 157.106 135.867 1.00 97.13  ? 40  ALA C O   1 
ATOM   3725  C CB  . ALA C  1 38  ? 161.836 156.897 134.914 1.00 85.84  ? 40  ALA C CB  1 
ATOM   3726  N N   . GLY C  1 39  ? 164.883 157.943 133.775 1.00 93.08  ? 41  GLY C N   1 
ATOM   3727  C CA  . GLY C  1 39  ? 166.055 158.743 134.053 1.00 96.19  ? 41  GLY C CA  1 
ATOM   3728  C C   . GLY C  1 39  ? 167.249 158.274 133.242 1.00 102.67 ? 41  GLY C C   1 
ATOM   3729  O O   . GLY C  1 39  ? 167.102 157.771 132.123 1.00 107.38 ? 41  GLY C O   1 
ATOM   3730  N N   . VAL C  1 40  ? 168.431 158.439 133.826 1.00 101.61 ? 42  VAL C N   1 
ATOM   3731  C CA  . VAL C  1 40  ? 169.687 158.082 133.181 1.00 106.03 ? 42  VAL C CA  1 
ATOM   3732  C C   . VAL C  1 40  ? 170.434 157.097 134.072 1.00 106.09 ? 42  VAL C C   1 
ATOM   3733  O O   . VAL C  1 40  ? 170.509 157.285 135.292 1.00 105.76 ? 42  VAL C O   1 
ATOM   3734  C CB  . VAL C  1 40  ? 170.538 159.330 132.874 1.00 103.25 ? 42  VAL C CB  1 
ATOM   3735  C CG1 . VAL C  1 40  ? 170.873 160.092 134.142 1.00 94.16  ? 42  VAL C CG1 1 
ATOM   3736  C CG2 . VAL C  1 40  ? 171.806 158.940 132.134 1.00 107.58 ? 42  VAL C CG2 1 
ATOM   3737  N N   . ASP C  1 41  ? 170.946 156.028 133.460 1.00 107.59 ? 43  ASP C N   1 
ATOM   3738  C CA  . ASP C  1 41  ? 171.764 155.020 134.135 1.00 107.84 ? 43  ASP C CA  1 
ATOM   3739  C C   . ASP C  1 41  ? 170.993 154.343 135.270 1.00 109.68 ? 43  ASP C C   1 
ATOM   3740  O O   . ASP C  1 41  ? 171.419 154.328 136.424 1.00 108.70 ? 43  ASP C O   1 
ATOM   3741  C CB  . ASP C  1 41  ? 173.070 155.636 134.651 1.00 112.29 ? 43  ASP C CB  1 
ATOM   3742  C CG  . ASP C  1 41  ? 173.996 156.061 133.531 1.00 124.09 ? 43  ASP C CG  1 
ATOM   3743  O OD1 . ASP C  1 41  ? 173.533 156.149 132.375 1.00 130.01 ? 43  ASP C OD1 1 
ATOM   3744  O OD2 . ASP C  1 41  ? 175.188 156.313 133.808 1.00 122.95 ? 43  ASP C OD2 1 
ATOM   3745  N N   . ASN C  1 42  ? 169.853 153.760 134.918 1.00 103.83 ? 44  ASN C N   1 
ATOM   3746  C CA  . ASN C  1 42  ? 169.016 153.052 135.875 1.00 94.84  ? 44  ASN C CA  1 
ATOM   3747  C C   . ASN C  1 42  ? 168.980 151.566 135.549 1.00 98.12  ? 44  ASN C C   1 
ATOM   3748  O O   . ASN C  1 42  ? 169.183 151.158 134.401 1.00 105.94 ? 44  ASN C O   1 
ATOM   3749  C CB  . ASN C  1 42  ? 167.592 153.611 135.887 1.00 90.88  ? 44  ASN C CB  1 
ATOM   3750  C CG  . ASN C  1 42  ? 167.478 154.894 136.678 1.00 95.37  ? 44  ASN C CG  1 
ATOM   3751  O OD1 . ASN C  1 42  ? 166.804 154.945 137.705 1.00 93.81  ? 44  ASN C OD1 1 
ATOM   3752  N ND2 . ASN C  1 42  ? 168.136 155.942 136.202 1.00 102.47 ? 44  ASN C ND2 1 
ATOM   3753  N N   . VAL C  1 43  ? 168.727 150.757 136.575 1.00 96.50  ? 45  VAL C N   1 
ATOM   3754  C CA  . VAL C  1 43  ? 168.621 149.309 136.433 1.00 93.82  ? 45  VAL C CA  1 
ATOM   3755  C C   . VAL C  1 43  ? 167.405 148.836 137.214 1.00 94.44  ? 45  VAL C C   1 
ATOM   3756  O O   . VAL C  1 43  ? 167.270 149.137 138.404 1.00 95.00  ? 45  VAL C O   1 
ATOM   3757  C CB  . VAL C  1 43  ? 169.891 148.587 136.923 1.00 91.80  ? 45  VAL C CB  1 
ATOM   3758  C CG1 . VAL C  1 43  ? 169.627 147.100 137.080 1.00 93.34  ? 45  VAL C CG1 1 
ATOM   3759  C CG2 . VAL C  1 43  ? 171.041 148.824 135.961 1.00 91.59  ? 45  VAL C CG2 1 
ATOM   3760  N N   . ALA C  1 44  ? 166.520 148.098 136.547 1.00 97.60  ? 46  ALA C N   1 
ATOM   3761  C CA  . ALA C  1 44  ? 165.354 147.493 137.181 1.00 99.02  ? 46  ALA C CA  1 
ATOM   3762  C C   . ALA C  1 44  ? 165.296 146.033 136.756 1.00 104.19 ? 46  ALA C C   1 
ATOM   3763  O O   . ALA C  1 44  ? 165.131 145.737 135.569 1.00 107.71 ? 46  ALA C O   1 
ATOM   3764  C CB  . ALA C  1 44  ? 164.069 148.227 136.801 1.00 96.73  ? 46  ALA C CB  1 
ATOM   3765  N N   . ASN C  1 45  ? 165.428 145.122 137.722 1.00 101.48 ? 47  ASN C N   1 
ATOM   3766  C CA  . ASN C  1 45  ? 165.513 143.700 137.428 1.00 96.05  ? 47  ASN C CA  1 
ATOM   3767  C C   . ASN C  1 45  ? 164.372 142.871 137.994 1.00 102.98 ? 47  ASN C C   1 
ATOM   3768  O O   . ASN C  1 45  ? 164.157 141.753 137.515 1.00 109.19 ? 47  ASN C O   1 
ATOM   3769  C CB  . ASN C  1 45  ? 166.838 143.126 137.951 1.00 92.24  ? 47  ASN C CB  1 
ATOM   3770  C CG  . ASN C  1 45  ? 168.020 143.534 137.102 1.00 102.33 ? 47  ASN C CG  1 
ATOM   3771  O OD1 . ASN C  1 45  ? 167.857 143.984 135.969 1.00 108.57 ? 47  ASN C OD1 1 
ATOM   3772  N ND2 . ASN C  1 45  ? 169.221 143.384 137.647 1.00 105.77 ? 47  ASN C ND2 1 
ATOM   3773  N N   . GLY C  1 46  ? 163.647 143.369 138.989 1.00 103.98 ? 48  GLY C N   1 
ATOM   3774  C CA  . GLY C  1 46  ? 162.539 142.626 139.541 1.00 100.29 ? 48  GLY C CA  1 
ATOM   3775  C C   . GLY C  1 46  ? 161.258 142.802 138.749 1.00 101.76 ? 48  GLY C C   1 
ATOM   3776  O O   . GLY C  1 46  ? 161.075 143.781 138.029 1.00 105.85 ? 48  GLY C O   1 
ATOM   3777  N N   . VAL C  1 47  ? 160.362 141.826 138.888 1.00 98.77  ? 49  VAL C N   1 
ATOM   3778  C CA  . VAL C  1 47  ? 159.056 141.915 138.250 1.00 97.93  ? 49  VAL C CA  1 
ATOM   3779  C C   . VAL C  1 47  ? 158.235 142.992 138.943 1.00 100.08 ? 49  VAL C C   1 
ATOM   3780  O O   . VAL C  1 47  ? 158.184 143.056 140.178 1.00 104.56 ? 49  VAL C O   1 
ATOM   3781  C CB  . VAL C  1 47  ? 158.340 140.558 138.286 1.00 91.77  ? 49  VAL C CB  1 
ATOM   3782  C CG1 . VAL C  1 47  ? 157.274 140.497 137.208 1.00 96.08  ? 49  VAL C CG1 1 
ATOM   3783  C CG2 . VAL C  1 47  ? 159.340 139.429 138.114 1.00 91.47  ? 49  VAL C CG2 1 
ATOM   3784  N N   . LYS C  1 48  ? 157.594 143.849 138.147 1.00 98.23  ? 50  LYS C N   1 
ATOM   3785  C CA  . LYS C  1 48  ? 156.805 144.973 138.654 1.00 94.16  ? 50  LYS C CA  1 
ATOM   3786  C C   . LYS C  1 48  ? 157.646 145.915 139.511 1.00 97.72  ? 50  LYS C C   1 
ATOM   3787  O O   . LYS C  1 48  ? 157.139 146.543 140.442 1.00 101.56 ? 50  LYS C O   1 
ATOM   3788  C CB  . LYS C  1 48  ? 155.579 144.494 139.436 1.00 99.99  ? 50  LYS C CB  1 
ATOM   3789  C CG  . LYS C  1 48  ? 154.819 143.360 138.772 1.00 107.10 ? 50  LYS C CG  1 
ATOM   3790  C CD  . LYS C  1 48  ? 153.629 142.934 139.614 1.00 109.99 ? 50  LYS C CD  1 
ATOM   3791  C CE  . LYS C  1 48  ? 152.588 142.213 138.776 1.00 109.95 ? 50  LYS C CE  1 
ATOM   3792  N NZ  . LYS C  1 48  ? 153.007 142.090 137.353 1.00 115.60 ? 50  LYS C NZ  1 
ATOM   3793  N N   . SER C  1 49  ? 158.933 146.020 139.203 1.00 98.41  ? 51  SER C N   1 
ATOM   3794  C CA  . SER C  1 49  ? 159.837 146.926 139.894 1.00 92.71  ? 51  SER C CA  1 
ATOM   3795  C C   . SER C  1 49  ? 160.043 148.187 139.067 1.00 96.43  ? 51  SER C C   1 
ATOM   3796  O O   . SER C  1 49  ? 159.727 148.236 137.877 1.00 102.74 ? 51  SER C O   1 
ATOM   3797  C CB  . SER C  1 49  ? 161.181 146.248 140.169 1.00 92.45  ? 51  SER C CB  1 
ATOM   3798  O OG  . SER C  1 49  ? 161.809 145.861 138.960 1.00 98.72  ? 51  SER C OG  1 
ATOM   3799  N N   . SER C  1 50  ? 160.575 149.220 139.714 1.00 94.78  ? 52  SER C N   1 
ATOM   3800  C CA  . SER C  1 50  ? 160.775 150.496 139.045 1.00 94.01  ? 52  SER C CA  1 
ATOM   3801  C C   . SER C  1 50  ? 161.937 151.236 139.686 1.00 91.90  ? 52  SER C C   1 
ATOM   3802  O O   . SER C  1 50  ? 162.113 151.196 140.906 1.00 92.23  ? 52  SER C O   1 
ATOM   3803  C CB  . SER C  1 50  ? 159.508 151.354 139.100 1.00 92.28  ? 52  SER C CB  1 
ATOM   3804  O OG  . SER C  1 50  ? 159.068 151.521 140.435 1.00 98.89  ? 52  SER C OG  1 
ATOM   3805  N N   . ALA C  1 51  ? 162.724 151.913 138.852 1.00 85.65  ? 53  ALA C N   1 
ATOM   3806  C CA  . ALA C  1 51  ? 163.847 152.729 139.300 1.00 81.77  ? 53  ALA C CA  1 
ATOM   3807  C C   . ALA C  1 51  ? 163.748 154.082 138.611 1.00 86.01  ? 53  ALA C C   1 
ATOM   3808  O O   . ALA C  1 51  ? 163.921 154.175 137.391 1.00 91.01  ? 53  ALA C O   1 
ATOM   3809  C CB  . ALA C  1 51  ? 165.182 152.053 138.990 1.00 88.64  ? 53  ALA C CB  1 
ATOM   3810  N N   . PHE C  1 52  ? 163.471 155.125 139.387 1.00 84.10  ? 54  PHE C N   1 
ATOM   3811  C CA  . PHE C  1 52  ? 163.263 156.469 138.867 1.00 80.42  ? 54  PHE C CA  1 
ATOM   3812  C C   . PHE C  1 52  ? 164.328 157.395 139.433 1.00 85.42  ? 54  PHE C C   1 
ATOM   3813  O O   . PHE C  1 52  ? 164.509 157.465 140.653 1.00 89.27  ? 54  PHE C O   1 
ATOM   3814  C CB  . PHE C  1 52  ? 161.869 156.991 139.229 1.00 82.90  ? 54  PHE C CB  1 
ATOM   3815  C CG  . PHE C  1 52  ? 160.765 156.445 138.366 1.00 82.57  ? 54  PHE C CG  1 
ATOM   3816  C CD1 . PHE C  1 52  ? 160.591 155.081 138.210 1.00 86.30  ? 54  PHE C CD1 1 
ATOM   3817  C CD2 . PHE C  1 52  ? 159.886 157.300 137.726 1.00 85.41  ? 54  PHE C CD2 1 
ATOM   3818  C CE1 . PHE C  1 52  ? 159.574 154.583 137.421 1.00 87.41  ? 54  PHE C CE1 1 
ATOM   3819  C CE2 . PHE C  1 52  ? 158.868 156.806 136.936 1.00 87.83  ? 54  PHE C CE2 1 
ATOM   3820  C CZ  . PHE C  1 52  ? 158.712 155.446 136.785 1.00 85.60  ? 54  PHE C CZ  1 
ATOM   3821  N N   . GLY C  1 53  ? 165.023 158.107 138.551 1.00 85.69  ? 55  GLY C N   1 
ATOM   3822  C CA  . GLY C  1 53  ? 166.056 159.028 138.982 1.00 85.19  ? 55  GLY C CA  1 
ATOM   3823  C C   . GLY C  1 53  ? 167.389 158.787 138.307 1.00 89.89  ? 55  GLY C C   1 
ATOM   3824  O O   . GLY C  1 53  ? 167.442 158.517 137.104 1.00 92.06  ? 55  GLY C O   1 
ATOM   3825  N N   . TYR C  1 54  ? 168.476 158.885 139.070 1.00 93.45  ? 56  TYR C N   1 
ATOM   3826  C CA  . TYR C  1 54  ? 169.821 158.679 138.549 1.00 95.24  ? 56  TYR C CA  1 
ATOM   3827  C C   . TYR C  1 54  ? 170.518 157.585 139.343 1.00 96.92  ? 56  TYR C C   1 
ATOM   3828  O O   . TYR C  1 54  ? 170.578 157.652 140.575 1.00 98.07  ? 56  TYR C O   1 
ATOM   3829  C CB  . TYR C  1 54  ? 170.644 159.970 138.605 1.00 89.47  ? 56  TYR C CB  1 
ATOM   3830  C CG  . TYR C  1 54  ? 172.120 159.755 138.353 1.00 94.73  ? 56  TYR C CG  1 
ATOM   3831  C CD1 . TYR C  1 54  ? 172.601 159.557 137.069 1.00 99.78  ? 56  TYR C CD1 1 
ATOM   3832  C CD2 . TYR C  1 54  ? 173.031 159.753 139.400 1.00 96.89  ? 56  TYR C CD2 1 
ATOM   3833  C CE1 . TYR C  1 54  ? 173.945 159.359 136.831 1.00 99.70  ? 56  TYR C CE1 1 
ATOM   3834  C CE2 . TYR C  1 54  ? 174.378 159.556 139.172 1.00 98.24  ? 56  TYR C CE2 1 
ATOM   3835  C CZ  . TYR C  1 54  ? 174.829 159.360 137.885 1.00 99.39  ? 56  TYR C CZ  1 
ATOM   3836  O OH  . TYR C  1 54  ? 176.170 159.163 137.652 1.00 106.39 ? 56  TYR C OH  1 
ATOM   3837  N N   . ASP C  1 55  ? 171.051 156.592 138.630 1.00 94.44  ? 57  ASP C N   1 
ATOM   3838  C CA  . ASP C  1 55  ? 171.858 155.525 139.225 1.00 93.97  ? 57  ASP C CA  1 
ATOM   3839  C C   . ASP C  1 55  ? 171.075 154.737 140.272 1.00 98.00  ? 57  ASP C C   1 
ATOM   3840  O O   . ASP C  1 55  ? 171.596 154.397 141.335 1.00 98.62  ? 57  ASP C O   1 
ATOM   3841  C CB  . ASP C  1 55  ? 173.152 156.081 139.820 1.00 102.62 ? 57  ASP C CB  1 
ATOM   3842  C CG  . ASP C  1 55  ? 174.302 155.102 139.726 1.00 113.11 ? 57  ASP C CG  1 
ATOM   3843  O OD1 . ASP C  1 55  ? 174.206 154.145 138.930 1.00 113.53 ? 57  ASP C OD1 1 
ATOM   3844  O OD2 . ASP C  1 55  ? 175.304 155.291 140.447 1.00 121.57 ? 57  ASP C OD2 1 
ATOM   3845  N N   . ASN C  1 56  ? 169.823 154.423 139.963 1.00 93.99  ? 58  ASN C N   1 
ATOM   3846  C CA  . ASN C  1 56  ? 168.962 153.674 140.866 1.00 88.08  ? 58  ASN C CA  1 
ATOM   3847  C C   . ASN C  1 56  ? 168.875 152.221 140.419 1.00 92.01  ? 58  ASN C C   1 
ATOM   3848  O O   . ASN C  1 56  ? 168.789 151.933 139.221 1.00 97.75  ? 58  ASN C O   1 
ATOM   3849  C CB  . ASN C  1 56  ? 167.565 154.290 140.919 1.00 85.52  ? 58  ASN C CB  1 
ATOM   3850  C CG  . ASN C  1 56  ? 167.530 155.578 141.710 1.00 89.94  ? 58  ASN C CG  1 
ATOM   3851  O OD1 . ASN C  1 56  ? 168.522 156.297 141.785 1.00 97.23  ? 58  ASN C OD1 1 
ATOM   3852  N ND2 . ASN C  1 56  ? 166.383 155.880 142.300 1.00 93.55  ? 58  ASN C ND2 1 
ATOM   3853  N N   . LYS C  1 57  ? 168.905 151.309 141.387 1.00 91.01  ? 59  LYS C N   1 
ATOM   3854  C CA  . LYS C  1 57  ? 168.814 149.877 141.127 1.00 86.47  ? 59  LYS C CA  1 
ATOM   3855  C C   . LYS C  1 57  ? 167.666 149.293 141.936 1.00 93.62  ? 59  LYS C C   1 
ATOM   3856  O O   . LYS C  1 57  ? 167.641 149.419 143.165 1.00 96.03  ? 59  LYS C O   1 
ATOM   3857  C CB  . LYS C  1 57  ? 170.124 149.166 141.471 1.00 83.84  ? 59  LYS C CB  1 
ATOM   3858  C CG  . LYS C  1 57  ? 171.366 149.829 140.905 1.00 92.54  ? 59  LYS C CG  1 
ATOM   3859  C CD  . LYS C  1 57  ? 172.597 148.967 141.129 1.00 98.99  ? 59  LYS C CD  1 
ATOM   3860  C CE  . LYS C  1 57  ? 173.605 149.139 140.005 1.00 107.53 ? 59  LYS C CE  1 
ATOM   3861  N NZ  . LYS C  1 57  ? 173.374 150.395 139.241 1.00 101.96 ? 59  LYS C NZ  1 
ATOM   3862  N N   . ALA C  1 58  ? 166.724 148.655 141.246 1.00 94.35  ? 60  ALA C N   1 
ATOM   3863  C CA  . ALA C  1 58  ? 165.633 147.912 141.870 1.00 89.88  ? 60  ALA C CA  1 
ATOM   3864  C C   . ALA C  1 58  ? 165.708 146.484 141.348 1.00 95.52  ? 60  ALA C C   1 
ATOM   3865  O O   . ALA C  1 58  ? 165.326 146.217 140.204 1.00 99.44  ? 60  ALA C O   1 
ATOM   3866  C CB  . ALA C  1 58  ? 164.280 148.548 141.562 1.00 88.15  ? 60  ALA C CB  1 
ATOM   3867  N N   . ILE C  1 59  ? 166.192 145.570 142.185 1.00 97.93  ? 61  ILE C N   1 
ATOM   3868  C CA  . ILE C  1 59  ? 166.588 144.241 141.731 1.00 97.74  ? 61  ILE C CA  1 
ATOM   3869  C C   . ILE C  1 59  ? 165.624 143.147 142.164 1.00 102.96 ? 61  ILE C C   1 
ATOM   3870  O O   . ILE C  1 59  ? 165.734 142.016 141.664 1.00 104.94 ? 61  ILE C O   1 
ATOM   3871  C CB  . ILE C  1 59  ? 168.019 143.900 142.199 1.00 94.93  ? 61  ILE C CB  1 
ATOM   3872  C CG1 . ILE C  1 59  ? 168.875 145.165 142.215 1.00 91.93  ? 61  ILE C CG1 1 
ATOM   3873  C CG2 . ILE C  1 59  ? 168.660 142.880 141.276 1.00 94.00  ? 61  ILE C CG2 1 
ATOM   3874  C CD1 . ILE C  1 59  ? 170.277 144.948 142.722 1.00 93.42  ? 61  ILE C CD1 1 
ATOM   3875  N N   . GLU C  1 60  ? 164.684 143.434 143.056 1.00 104.35 ? 62  GLU C N   1 
ATOM   3876  C CA  . GLU C  1 60  ? 163.762 142.424 143.550 1.00 104.62 ? 62  GLU C CA  1 
ATOM   3877  C C   . GLU C  1 60  ? 162.335 142.741 143.119 1.00 103.70 ? 62  GLU C C   1 
ATOM   3878  O O   . GLU C  1 60  ? 162.030 143.832 142.632 1.00 105.86 ? 62  GLU C O   1 
ATOM   3879  C CB  . GLU C  1 60  ? 163.849 142.310 145.076 1.00 101.16 ? 62  GLU C CB  1 
ATOM   3880  C CG  . GLU C  1 60  ? 164.612 141.094 145.653 1.00 107.59 ? 62  GLU C CG  1 
ATOM   3881  C CD  . GLU C  1 60  ? 164.275 139.723 145.047 1.00 121.56 ? 62  GLU C CD  1 
ATOM   3882  O OE1 . GLU C  1 60  ? 164.774 138.719 145.596 1.00 130.67 ? 62  GLU C OE1 1 
ATOM   3883  O OE2 . GLU C  1 60  ? 163.500 139.614 144.074 1.00 121.69 ? 62  GLU C OE2 1 
ATOM   3884  N N   . LYS C  1 61  ? 161.462 141.753 143.303 1.00 100.15 ? 63  LYS C N   1 
ATOM   3885  C CA  . LYS C  1 61  ? 160.074 141.874 142.875 1.00 94.34  ? 63  LYS C CA  1 
ATOM   3886  C C   . LYS C  1 61  ? 159.367 142.995 143.625 1.00 96.55  ? 63  LYS C C   1 
ATOM   3887  O O   . LYS C  1 61  ? 159.456 143.089 144.853 1.00 101.01 ? 63  LYS C O   1 
ATOM   3888  C CB  . LYS C  1 61  ? 159.344 140.551 143.096 1.00 94.27  ? 63  LYS C CB  1 
ATOM   3889  C CG  . LYS C  1 61  ? 157.999 140.461 142.403 1.00 102.02 ? 63  LYS C CG  1 
ATOM   3890  C CD  . LYS C  1 61  ? 157.068 139.512 143.136 1.00 103.76 ? 63  LYS C CD  1 
ATOM   3891  C CE  . LYS C  1 61  ? 156.865 138.229 142.353 1.00 106.61 ? 63  LYS C CE  1 
ATOM   3892  N NZ  . LYS C  1 61  ? 155.422 137.909 142.192 1.00 102.38 ? 63  LYS C NZ  1 
ATOM   3893  N N   . GLU C  1 62  ? 158.650 143.834 142.876 1.00 93.68  ? 64  GLU C N   1 
ATOM   3894  C CA  . GLU C  1 62  ? 157.869 144.940 143.435 1.00 90.68  ? 64  GLU C CA  1 
ATOM   3895  C C   . GLU C  1 62  ? 158.716 145.817 144.352 1.00 93.56  ? 64  GLU C C   1 
ATOM   3896  O O   . GLU C  1 62  ? 158.281 146.230 145.429 1.00 97.02  ? 64  GLU C O   1 
ATOM   3897  C CB  . GLU C  1 62  ? 156.628 144.428 144.166 1.00 96.70  ? 64  GLU C CB  1 
ATOM   3898  C CG  . GLU C  1 62  ? 155.997 143.199 143.542 1.00 105.22 ? 64  GLU C CG  1 
ATOM   3899  C CD  . GLU C  1 62  ? 154.486 143.225 143.605 1.00 117.05 ? 64  GLU C CD  1 
ATOM   3900  O OE1 . GLU C  1 62  ? 153.909 144.332 143.609 1.00 119.84 ? 64  GLU C OE1 1 
ATOM   3901  O OE2 . GLU C  1 62  ? 153.874 142.138 143.650 1.00 119.09 ? 64  GLU C OE2 1 
ATOM   3902  N N   . SER C  1 63  ? 159.938 146.106 143.920 1.00 93.03  ? 65  SER C N   1 
ATOM   3903  C CA  . SER C  1 63  ? 160.849 146.969 144.654 1.00 88.10  ? 65  SER C CA  1 
ATOM   3904  C C   . SER C  1 63  ? 160.987 148.296 143.924 1.00 90.57  ? 65  SER C C   1 
ATOM   3905  O O   . SER C  1 63  ? 161.063 148.332 142.692 1.00 96.12  ? 65  SER C O   1 
ATOM   3906  C CB  . SER C  1 63  ? 162.221 146.314 144.817 1.00 87.49  ? 65  SER C CB  1 
ATOM   3907  O OG  . SER C  1 63  ? 162.693 145.814 143.580 1.00 97.91  ? 65  SER C OG  1 
ATOM   3908  N N   . SER C  1 64  ? 161.017 149.384 144.687 1.00 87.22  ? 66  SER C N   1 
ATOM   3909  C CA  . SER C  1 64  ? 161.063 150.729 144.134 1.00 84.68  ? 66  SER C CA  1 
ATOM   3910  C C   . SER C  1 64  ? 162.295 151.458 144.645 1.00 86.80  ? 66  SER C C   1 
ATOM   3911  O O   . SER C  1 64  ? 162.628 151.383 145.831 1.00 89.79  ? 66  SER C O   1 
ATOM   3912  C CB  . SER C  1 64  ? 159.804 151.517 144.501 1.00 89.77  ? 66  SER C CB  1 
ATOM   3913  O OG  . SER C  1 64  ? 158.730 151.189 143.637 1.00 100.38 ? 66  SER C OG  1 
ATOM   3914  N N   . ALA C  1 65  ? 162.970 152.165 143.740 1.00 82.38  ? 67  ALA C N   1 
ATOM   3915  C CA  . ALA C  1 65  ? 164.138 152.973 144.085 1.00 78.08  ? 67  ALA C CA  1 
ATOM   3916  C C   . ALA C  1 65  ? 163.973 154.318 143.387 1.00 83.36  ? 67  ALA C C   1 
ATOM   3917  O O   . ALA C  1 65  ? 164.213 154.430 142.182 1.00 90.48  ? 67  ALA C O   1 
ATOM   3918  C CB  . ALA C  1 65  ? 165.434 152.285 143.676 1.00 78.41  ? 67  ALA C CB  1 
ATOM   3919  N N   . PHE C  1 66  ? 163.563 155.331 144.144 1.00 81.64  ? 68  PHE C N   1 
ATOM   3920  C CA  . PHE C  1 66  ? 163.296 156.659 143.612 1.00 76.24  ? 68  PHE C CA  1 
ATOM   3921  C C   . PHE C  1 66  ? 164.267 157.651 144.233 1.00 81.28  ? 68  PHE C C   1 
ATOM   3922  O O   . PHE C  1 66  ? 164.376 157.730 145.460 1.00 83.09  ? 68  PHE C O   1 
ATOM   3923  C CB  . PHE C  1 66  ? 161.853 157.087 143.897 1.00 78.96  ? 68  PHE C CB  1 
ATOM   3924  C CG  . PHE C  1 66  ? 160.835 156.441 142.999 1.00 79.03  ? 68  PHE C CG  1 
ATOM   3925  C CD1 . PHE C  1 66  ? 160.693 155.065 142.962 1.00 81.88  ? 68  PHE C CD1 1 
ATOM   3926  C CD2 . PHE C  1 66  ? 160.013 157.213 142.200 1.00 81.24  ? 68  PHE C CD2 1 
ATOM   3927  C CE1 . PHE C  1 66  ? 159.757 154.473 142.141 1.00 83.60  ? 68  PHE C CE1 1 
ATOM   3928  C CE2 . PHE C  1 66  ? 159.076 156.625 141.376 1.00 85.39  ? 68  PHE C CE2 1 
ATOM   3929  C CZ  . PHE C  1 66  ? 158.948 155.254 141.347 1.00 83.06  ? 68  PHE C CZ  1 
ATOM   3930  N N   . GLY C  1 67  ? 164.962 158.407 143.390 1.00 82.47  ? 69  GLY C N   1 
ATOM   3931  C CA  . GLY C  1 67  ? 165.902 159.394 143.880 1.00 80.88  ? 69  GLY C CA  1 
ATOM   3932  C C   . GLY C  1 67  ? 167.240 159.357 143.175 1.00 83.42  ? 69  GLY C C   1 
ATOM   3933  O O   . GLY C  1 67  ? 167.297 159.320 141.943 1.00 85.55  ? 69  GLY C O   1 
ATOM   3934  N N   . THR C  1 68  ? 168.327 159.366 143.943 1.00 85.88  ? 70  THR C N   1 
ATOM   3935  C CA  . THR C  1 68  ? 169.676 159.372 143.391 1.00 87.62  ? 70  THR C CA  1 
ATOM   3936  C C   . THR C  1 68  ? 170.500 158.289 144.069 1.00 84.87  ? 70  THR C C   1 
ATOM   3937  O O   . THR C  1 68  ? 170.737 158.352 145.279 1.00 86.99  ? 70  THR C O   1 
ATOM   3938  C CB  . THR C  1 68  ? 170.340 160.739 143.574 1.00 85.61  ? 70  THR C CB  1 
ATOM   3939  O OG1 . THR C  1 68  ? 169.668 161.709 142.762 1.00 92.34  ? 70  THR C OG1 1 
ATOM   3940  C CG2 . THR C  1 68  ? 171.802 160.676 143.170 1.00 85.03  ? 70  THR C CG2 1 
ATOM   3941  N N   . GLY C  1 69  ? 170.940 157.307 143.289 1.00 82.47  ? 71  GLY C N   1 
ATOM   3942  C CA  . GLY C  1 69  ? 171.824 156.273 143.805 1.00 83.86  ? 71  GLY C CA  1 
ATOM   3943  C C   . GLY C  1 69  ? 171.212 155.377 144.858 1.00 86.79  ? 71  GLY C C   1 
ATOM   3944  O O   . GLY C  1 69  ? 171.907 154.957 145.791 1.00 85.02  ? 71  GLY C O   1 
ATOM   3945  N N   . ASN C  1 70  ? 169.929 155.059 144.726 1.00 85.89  ? 72  ASN C N   1 
ATOM   3946  C CA  . ASN C  1 70  ? 169.259 154.192 145.682 1.00 79.67  ? 72  ASN C CA  1 
ATOM   3947  C C   . ASN C  1 70  ? 169.338 152.738 145.237 1.00 84.10  ? 72  ASN C C   1 
ATOM   3948  O O   . ASN C  1 70  ? 169.399 152.435 144.042 1.00 90.77  ? 72  ASN C O   1 
ATOM   3949  C CB  . ASN C  1 70  ? 167.798 154.602 145.855 1.00 79.38  ? 72  ASN C CB  1 
ATOM   3950  C CG  . ASN C  1 70  ? 167.650 156.025 146.338 1.00 83.13  ? 72  ASN C CG  1 
ATOM   3951  O OD1 . ASN C  1 70  ? 168.439 156.896 145.983 1.00 88.72  ? 72  ASN C OD1 1 
ATOM   3952  N ND2 . ASN C  1 70  ? 166.637 156.268 147.157 1.00 86.02  ? 72  ASN C ND2 1 
ATOM   3953  N N   . ARG C  1 71  ? 169.341 151.837 146.215 1.00 81.93  ? 73  ARG C N   1 
ATOM   3954  C CA  . ARG C  1 71  ? 169.369 150.403 145.962 1.00 79.91  ? 73  ARG C CA  1 
ATOM   3955  C C   . ARG C  1 71  ? 168.256 149.732 146.749 1.00 87.73  ? 73  ARG C C   1 
ATOM   3956  O O   . ARG C  1 71  ? 168.174 149.887 147.971 1.00 91.54  ? 73  ARG C O   1 
ATOM   3957  C CB  . ARG C  1 71  ? 170.724 149.799 146.340 1.00 80.42  ? 73  ARG C CB  1 
ATOM   3958  C CG  . ARG C  1 71  ? 171.685 149.661 145.174 1.00 88.43  ? 73  ARG C CG  1 
ATOM   3959  C CD  . ARG C  1 71  ? 172.863 150.607 145.312 1.00 92.40  ? 73  ARG C CD  1 
ATOM   3960  N NE  . ARG C  1 71  ? 173.566 150.788 144.047 1.00 99.98  ? 73  ARG C NE  1 
ATOM   3961  C CZ  . ARG C  1 71  ? 173.364 151.802 143.218 1.00 105.34 ? 73  ARG C CZ  1 
ATOM   3962  N NH1 . ARG C  1 71  ? 172.483 152.751 143.488 1.00 101.94 ? 73  ARG C NH1 1 
ATOM   3963  N NH2 . ARG C  1 71  ? 174.063 151.866 142.089 1.00 109.00 ? 73  ARG C NH2 1 
ATOM   3964  N N   . ALA C  1 72  ? 167.406 148.987 146.049 1.00 86.86  ? 74  ALA C N   1 
ATOM   3965  C CA  . ALA C  1 72  ? 166.326 148.214 146.659 1.00 82.08  ? 74  ALA C CA  1 
ATOM   3966  C C   . ALA C  1 72  ? 166.550 146.754 146.285 1.00 89.84  ? 74  ALA C C   1 
ATOM   3967  O O   . ALA C  1 72  ? 166.148 146.314 145.204 1.00 96.20  ? 74  ALA C O   1 
ATOM   3968  C CB  . ALA C  1 72  ? 164.961 148.712 146.197 1.00 81.35  ? 74  ALA C CB  1 
ATOM   3969  N N   . THR C  1 73  ? 167.191 146.004 147.181 1.00 89.33  ? 75  THR C N   1 
ATOM   3970  C CA  . THR C  1 73  ? 167.601 144.633 146.910 1.00 90.81  ? 75  THR C CA  1 
ATOM   3971  C C   . THR C  1 73  ? 166.702 143.608 147.593 1.00 94.52  ? 75  THR C C   1 
ATOM   3972  O O   . THR C  1 73  ? 167.030 142.418 147.612 1.00 100.47 ? 75  THR C O   1 
ATOM   3973  C CB  . THR C  1 73  ? 169.053 144.424 147.336 1.00 93.90  ? 75  THR C CB  1 
ATOM   3974  O OG1 . THR C  1 73  ? 169.238 144.926 148.665 1.00 95.07  ? 75  THR C OG1 1 
ATOM   3975  C CG2 . THR C  1 73  ? 169.989 145.161 146.395 1.00 91.87  ? 75  THR C CG2 1 
ATOM   3976  N N   . GLY C  1 74  ? 165.575 144.044 148.154 1.00 90.11  ? 76  GLY C N   1 
ATOM   3977  C CA  . GLY C  1 74  ? 164.649 143.137 148.790 1.00 87.47  ? 76  GLY C CA  1 
ATOM   3978  C C   . GLY C  1 74  ? 163.262 143.281 148.197 1.00 93.63  ? 76  GLY C C   1 
ATOM   3979  O O   . GLY C  1 74  ? 162.900 144.320 147.647 1.00 99.29  ? 76  GLY C O   1 
ATOM   3980  N N   . GLU C  1 75  ? 162.490 142.202 148.307 1.00 93.61  ? 77  GLU C N   1 
ATOM   3981  C CA  . GLU C  1 75  ? 161.119 142.219 147.820 1.00 93.52  ? 77  GLU C CA  1 
ATOM   3982  C C   . GLU C  1 75  ? 160.318 143.284 148.553 1.00 90.80  ? 77  GLU C C   1 
ATOM   3983  O O   . GLU C  1 75  ? 160.568 143.577 149.723 1.00 96.30  ? 77  GLU C O   1 
ATOM   3984  C CB  . GLU C  1 75  ? 160.462 140.853 148.013 1.00 97.75  ? 77  GLU C CB  1 
ATOM   3985  C CG  . GLU C  1 75  ? 161.360 139.674 147.702 1.00 112.19 ? 77  GLU C CG  1 
ATOM   3986  C CD  . GLU C  1 75  ? 160.598 138.514 147.096 1.00 127.20 ? 77  GLU C CD  1 
ATOM   3987  O OE1 . GLU C  1 75  ? 161.222 137.467 146.825 1.00 134.09 ? 77  GLU C OE1 1 
ATOM   3988  O OE2 . GLU C  1 75  ? 159.373 138.649 146.895 1.00 124.56 ? 77  GLU C OE2 1 
ATOM   3989  N N   . PHE C  1 76  ? 159.377 143.898 147.835 1.00 87.55  ? 78  PHE C N   1 
ATOM   3990  C CA  . PHE C  1 76  ? 158.444 144.872 148.409 1.00 86.07  ? 78  PHE C CA  1 
ATOM   3991  C C   . PHE C  1 76  ? 159.164 145.963 149.198 1.00 88.09  ? 78  PHE C C   1 
ATOM   3992  O O   . PHE C  1 76  ? 158.597 146.562 150.114 1.00 95.26  ? 78  PHE C O   1 
ATOM   3993  C CB  . PHE C  1 76  ? 157.405 144.179 149.293 1.00 87.92  ? 78  PHE C CB  1 
ATOM   3994  C CG  . PHE C  1 76  ? 156.912 142.875 148.740 1.00 90.81  ? 78  PHE C CG  1 
ATOM   3995  C CD1 . PHE C  1 76  ? 156.371 142.803 147.469 1.00 95.91  ? 78  PHE C CD1 1 
ATOM   3996  C CD2 . PHE C  1 76  ? 156.991 141.718 149.494 1.00 92.72  ? 78  PHE C CD2 1 
ATOM   3997  C CE1 . PHE C  1 76  ? 155.919 141.602 146.962 1.00 100.46 ? 78  PHE C CE1 1 
ATOM   3998  C CE2 . PHE C  1 76  ? 156.542 140.516 148.991 1.00 94.60  ? 78  PHE C CE2 1 
ATOM   3999  C CZ  . PHE C  1 76  ? 156.006 140.457 147.724 1.00 96.79  ? 78  PHE C CZ  1 
ATOM   4000  N N   . SER C  1 77  ? 160.417 146.229 148.853 1.00 85.39  ? 79  SER C N   1 
ATOM   4001  C CA  . SER C  1 77  ? 161.223 147.212 149.556 1.00 82.81  ? 79  SER C CA  1 
ATOM   4002  C C   . SER C  1 77  ? 161.335 148.488 148.734 1.00 84.24  ? 79  SER C C   1 
ATOM   4003  O O   . SER C  1 77  ? 161.336 148.466 147.502 1.00 92.56  ? 79  SER C O   1 
ATOM   4004  C CB  . SER C  1 77  ? 162.616 146.658 149.861 1.00 84.59  ? 79  SER C CB  1 
ATOM   4005  O OG  . SER C  1 77  ? 163.326 146.380 148.667 1.00 93.15  ? 79  SER C OG  1 
ATOM   4006  N N   . SER C  1 78  ? 161.432 149.611 149.439 1.00 79.42  ? 80  SER C N   1 
ATOM   4007  C CA  . SER C  1 78  ? 161.470 150.916 148.800 1.00 79.47  ? 80  SER C CA  1 
ATOM   4008  C C   . SER C  1 78  ? 162.587 151.747 149.407 1.00 82.91  ? 80  SER C C   1 
ATOM   4009  O O   . SER C  1 78  ? 162.712 151.824 150.633 1.00 86.37  ? 80  SER C O   1 
ATOM   4010  C CB  . SER C  1 78  ? 160.130 151.642 148.950 1.00 84.41  ? 80  SER C CB  1 
ATOM   4011  O OG  . SER C  1 78  ? 159.817 151.845 150.316 1.00 94.73  ? 80  SER C OG  1 
ATOM   4012  N N   . ALA C  1 79  ? 163.390 152.365 148.547 1.00 79.43  ? 81  ALA C N   1 
ATOM   4013  C CA  . ALA C  1 79  ? 164.453 153.276 148.955 1.00 74.86  ? 81  ALA C CA  1 
ATOM   4014  C C   . ALA C  1 79  ? 164.219 154.601 148.246 1.00 78.83  ? 81  ALA C C   1 
ATOM   4015  O O   . ALA C  1 79  ? 164.394 154.697 147.027 1.00 83.43  ? 81  ALA C O   1 
ATOM   4016  C CB  . ALA C  1 79  ? 165.828 152.704 148.621 1.00 73.59  ? 81  ALA C CB  1 
ATOM   4017  N N   . PHE C  1 80  ? 163.822 155.619 149.005 1.00 76.40  ? 82  PHE C N   1 
ATOM   4018  C CA  . PHE C  1 80  ? 163.468 156.921 148.457 1.00 71.69  ? 82  PHE C CA  1 
ATOM   4019  C C   . PHE C  1 80  ? 164.400 157.969 149.044 1.00 75.79  ? 82  PHE C C   1 
ATOM   4020  O O   . PHE C  1 80  ? 164.493 158.103 150.268 1.00 81.18  ? 82  PHE C O   1 
ATOM   4021  C CB  . PHE C  1 80  ? 162.011 157.270 148.764 1.00 75.66  ? 82  PHE C CB  1 
ATOM   4022  C CG  . PHE C  1 80  ? 161.019 156.604 147.852 1.00 75.19  ? 82  PHE C CG  1 
ATOM   4023  C CD1 . PHE C  1 80  ? 160.954 155.226 147.760 1.00 78.77  ? 82  PHE C CD1 1 
ATOM   4024  C CD2 . PHE C  1 80  ? 160.147 157.360 147.091 1.00 78.03  ? 82  PHE C CD2 1 
ATOM   4025  C CE1 . PHE C  1 80  ? 160.043 154.616 146.925 1.00 83.47  ? 82  PHE C CE1 1 
ATOM   4026  C CE2 . PHE C  1 80  ? 159.233 156.754 146.255 1.00 81.69  ? 82  PHE C CE2 1 
ATOM   4027  C CZ  . PHE C  1 80  ? 159.182 155.380 146.172 1.00 85.01  ? 82  PHE C CZ  1 
ATOM   4028  N N   . GLY C  1 81  ? 165.081 158.711 148.177 1.00 74.50  ? 83  GLY C N   1 
ATOM   4029  C CA  . GLY C  1 81  ? 165.961 159.764 148.640 1.00 75.01  ? 83  GLY C CA  1 
ATOM   4030  C C   . GLY C  1 81  ? 167.323 159.768 147.980 1.00 76.56  ? 83  GLY C C   1 
ATOM   4031  O O   . GLY C  1 81  ? 167.427 159.808 146.751 1.00 80.86  ? 83  GLY C O   1 
ATOM   4032  N N   . PHE C  1 82  ? 168.378 159.726 148.790 1.00 77.88  ? 84  PHE C N   1 
ATOM   4033  C CA  . PHE C  1 82  ? 169.748 159.837 148.305 1.00 79.49  ? 84  PHE C CA  1 
ATOM   4034  C C   . PHE C  1 82  ? 170.586 158.721 148.907 1.00 81.23  ? 84  PHE C C   1 
ATOM   4035  O O   . PHE C  1 82  ? 170.782 158.678 150.125 1.00 83.91  ? 84  PHE C O   1 
ATOM   4036  C CB  . PHE C  1 82  ? 170.339 161.205 148.659 1.00 75.25  ? 84  PHE C CB  1 
ATOM   4037  C CG  . PHE C  1 82  ? 171.791 161.347 148.313 1.00 80.82  ? 84  PHE C CG  1 
ATOM   4038  C CD1 . PHE C  1 82  ? 172.190 161.529 147.001 1.00 84.39  ? 84  PHE C CD1 1 
ATOM   4039  C CD2 . PHE C  1 82  ? 172.758 161.309 149.301 1.00 81.11  ? 84  PHE C CD2 1 
ATOM   4040  C CE1 . PHE C  1 82  ? 173.525 161.663 146.682 1.00 82.35  ? 84  PHE C CE1 1 
ATOM   4041  C CE2 . PHE C  1 82  ? 174.094 161.442 148.987 1.00 79.59  ? 84  PHE C CE2 1 
ATOM   4042  C CZ  . PHE C  1 82  ? 174.477 161.619 147.676 1.00 78.77  ? 84  PHE C CZ  1 
ATOM   4043  N N   . HIS C  1 83  ? 171.083 157.827 148.049 1.00 79.88  ? 85  HIS C N   1 
ATOM   4044  C CA  . HIS C  1 83  ? 171.992 156.751 148.450 1.00 80.51  ? 85  HIS C CA  1 
ATOM   4045  C C   . HIS C  1 83  ? 171.394 155.889 149.560 1.00 82.52  ? 85  HIS C C   1 
ATOM   4046  O O   . HIS C  1 83  ? 172.039 155.596 150.568 1.00 85.72  ? 85  HIS C O   1 
ATOM   4047  C CB  . HIS C  1 83  ? 173.352 157.313 148.868 1.00 82.38  ? 85  HIS C CB  1 
ATOM   4048  C CG  . HIS C  1 83  ? 174.222 157.707 147.717 1.00 87.16  ? 85  HIS C CG  1 
ATOM   4049  N ND1 . HIS C  1 83  ? 175.596 157.611 147.757 1.00 91.27  ? 85  HIS C ND1 1 
ATOM   4050  C CD2 . HIS C  1 83  ? 173.914 158.200 146.495 1.00 91.04  ? 85  HIS C CD2 1 
ATOM   4051  C CE1 . HIS C  1 83  ? 176.097 158.027 146.607 1.00 94.37  ? 85  HIS C CE1 1 
ATOM   4052  N NE2 . HIS C  1 83  ? 175.098 158.390 145.824 1.00 90.84  ? 85  HIS C NE2 1 
ATOM   4053  N N   . ASN C  1 84  ? 170.149 155.471 149.364 1.00 79.48  ? 86  ASN C N   1 
ATOM   4054  C CA  . ASN C  1 84  ? 169.436 154.661 150.339 1.00 77.88  ? 86  ASN C CA  1 
ATOM   4055  C C   . ASN C  1 84  ? 169.500 153.192 149.942 1.00 82.05  ? 86  ASN C C   1 
ATOM   4056  O O   . ASN C  1 84  ? 169.546 152.862 148.754 1.00 90.57  ? 86  ASN C O   1 
ATOM   4057  C CB  . ASN C  1 84  ? 167.981 155.112 150.451 1.00 75.61  ? 86  ASN C CB  1 
ATOM   4058  C CG  . ASN C  1 84  ? 167.827 156.363 151.284 1.00 77.65  ? 86  ASN C CG  1 
ATOM   4059  O OD1 . ASN C  1 84  ? 168.807 156.913 151.782 1.00 82.27  ? 86  ASN C OD1 1 
ATOM   4060  N ND2 . ASN C  1 84  ? 166.596 156.829 151.430 1.00 86.19  ? 86  ASN C ND2 1 
ATOM   4061  N N   . ILE C  1 85  ? 169.508 152.313 150.942 1.00 79.16  ? 87  ILE C N   1 
ATOM   4062  C CA  . ILE C  1 85  ? 169.607 150.875 150.723 1.00 78.31  ? 87  ILE C CA  1 
ATOM   4063  C C   . ILE C  1 85  ? 168.522 150.176 151.530 1.00 86.58  ? 87  ILE C C   1 
ATOM   4064  O O   . ILE C  1 85  ? 168.425 150.370 152.747 1.00 92.05  ? 87  ILE C O   1 
ATOM   4065  C CB  . ILE C  1 85  ? 170.997 150.334 151.106 1.00 75.39  ? 87  ILE C CB  1 
ATOM   4066  C CG1 . ILE C  1 85  ? 172.036 150.749 150.064 1.00 82.30  ? 87  ILE C CG1 1 
ATOM   4067  C CG2 . ILE C  1 85  ? 170.963 148.823 151.240 1.00 75.59  ? 87  ILE C CG2 1 
ATOM   4068  C CD1 . ILE C  1 85  ? 173.352 151.193 150.659 1.00 85.33  ? 87  ILE C CD1 1 
ATOM   4069  N N   . ALA C  1 86  ? 167.712 149.366 150.852 1.00 83.61  ? 88  ALA C N   1 
ATOM   4070  C CA  . ALA C  1 86  ? 166.720 148.506 151.485 1.00 80.89  ? 88  ALA C CA  1 
ATOM   4071  C C   . ALA C  1 86  ? 166.965 147.081 151.018 1.00 86.79  ? 88  ALA C C   1 
ATOM   4072  O O   . ALA C  1 86  ? 167.112 146.840 149.816 1.00 91.83  ? 88  ALA C O   1 
ATOM   4073  C CB  . ALA C  1 86  ? 165.297 148.949 151.141 1.00 79.36  ? 88  ALA C CB  1 
ATOM   4074  N N   . SER C  1 87  ? 167.007 146.136 151.959 1.00 83.84  ? 89  SER C N   1 
ATOM   4075  C CA  . SER C  1 87  ? 167.523 144.808 151.663 1.00 81.15  ? 89  SER C CA  1 
ATOM   4076  C C   . SER C  1 87  ? 166.623 143.647 152.062 1.00 88.31  ? 89  SER C C   1 
ATOM   4077  O O   . SER C  1 87  ? 167.003 142.497 151.819 1.00 94.11  ? 89  SER C O   1 
ATOM   4078  C CB  . SER C  1 87  ? 168.888 144.612 152.341 1.00 81.81  ? 89  SER C CB  1 
ATOM   4079  O OG  . SER C  1 87  ? 169.835 145.543 151.851 1.00 87.29  ? 89  SER C OG  1 
ATOM   4080  N N   . LYS C  1 88  ? 165.461 143.886 152.660 1.00 87.54  ? 90  LYS C N   1 
ATOM   4081  C CA  . LYS C  1 88  ? 164.662 142.781 153.176 1.00 85.44  ? 90  LYS C CA  1 
ATOM   4082  C C   . LYS C  1 88  ? 163.224 142.852 152.655 1.00 89.81  ? 90  LYS C C   1 
ATOM   4083  O O   . LYS C  1 88  ? 162.887 143.672 151.797 1.00 93.42  ? 90  LYS C O   1 
ATOM   4084  C CB  . LYS C  1 88  ? 164.724 142.759 154.704 1.00 82.51  ? 90  LYS C CB  1 
ATOM   4085  C CG  . LYS C  1 88  ? 166.111 142.441 155.235 1.00 82.27  ? 90  LYS C CG  1 
ATOM   4086  C CD  . LYS C  1 88  ? 166.455 140.974 155.044 1.00 90.88  ? 90  LYS C CD  1 
ATOM   4087  C CE  . LYS C  1 88  ? 167.747 140.613 155.757 1.00 94.31  ? 90  LYS C CE  1 
ATOM   4088  N NZ  . LYS C  1 88  ? 168.704 141.753 155.775 1.00 92.67  ? 90  LYS C NZ  1 
ATOM   4089  N N   . ILE C  1 89  ? 162.376 141.972 153.195 1.00 88.41  ? 91  ILE C N   1 
ATOM   4090  C CA  . ILE C  1 89  ? 161.083 141.675 152.582 1.00 87.54  ? 91  ILE C CA  1 
ATOM   4091  C C   . ILE C  1 89  ? 160.124 142.858 152.675 1.00 91.01  ? 91  ILE C C   1 
ATOM   4092  O O   . ILE C  1 89  ? 159.233 143.007 151.832 1.00 97.21  ? 91  ILE C O   1 
ATOM   4093  C CB  . ILE C  1 89  ? 160.486 140.404 153.216 1.00 83.62  ? 91  ILE C CB  1 
ATOM   4094  C CG1 . ILE C  1 89  ? 159.165 140.025 152.544 1.00 88.33  ? 91  ILE C CG1 1 
ATOM   4095  C CG2 . ILE C  1 89  ? 160.276 140.600 154.696 1.00 87.25  ? 91  ILE C CG2 1 
ATOM   4096  C CD1 . ILE C  1 89  ? 159.337 139.359 151.202 1.00 96.47  ? 91  ILE C CD1 1 
ATOM   4097  N N   . HIS C  1 90  ? 160.246 143.690 153.705 1.00 81.79  ? 92  HIS C N   1 
ATOM   4098  C CA  . HIS C  1 90  ? 159.497 144.949 153.756 1.00 76.91  ? 92  HIS C CA  1 
ATOM   4099  C C   . HIS C  1 90  ? 160.412 145.977 154.415 1.00 84.82  ? 92  HIS C C   1 
ATOM   4100  O O   . HIS C  1 90  ? 160.411 146.130 155.636 1.00 95.86  ? 92  HIS C O   1 
ATOM   4101  C CB  . HIS C  1 90  ? 158.185 144.786 154.511 1.00 85.07  ? 92  HIS C CB  1 
ATOM   4102  C CG  . HIS C  1 90  ? 157.095 144.154 153.703 1.00 87.42  ? 92  HIS C CG  1 
ATOM   4103  N ND1 . HIS C  1 90  ? 156.364 144.848 152.763 1.00 86.33  ? 92  HIS C ND1 1 
ATOM   4104  C CD2 . HIS C  1 90  ? 156.613 142.889 153.694 1.00 88.35  ? 92  HIS C CD2 1 
ATOM   4105  C CE1 . HIS C  1 90  ? 155.478 144.039 152.211 1.00 86.85  ? 92  HIS C CE1 1 
ATOM   4106  N NE2 . HIS C  1 90  ? 155.609 142.844 152.758 1.00 85.73  ? 92  HIS C NE2 1 
ATOM   4107  N N   . SER C  1 91  ? 161.176 146.694 153.601 1.00 80.25  ? 93  SER C N   1 
ATOM   4108  C CA  . SER C  1 91  ? 162.161 147.631 154.116 1.00 77.80  ? 93  SER C CA  1 
ATOM   4109  C C   . SER C  1 91  ? 161.935 149.004 153.508 1.00 86.34  ? 93  SER C C   1 
ATOM   4110  O O   . SER C  1 91  ? 161.700 149.130 152.303 1.00 94.98  ? 93  SER C O   1 
ATOM   4111  C CB  . SER C  1 91  ? 163.583 147.152 153.823 1.00 81.07  ? 93  SER C CB  1 
ATOM   4112  O OG  . SER C  1 91  ? 163.664 145.742 153.913 1.00 81.94  ? 93  SER C OG  1 
ATOM   4113  N N   . SER C  1 92  ? 162.010 150.029 154.350 1.00 82.45  ? 94  SER C N   1 
ATOM   4114  C CA  . SER C  1 92  ? 161.840 151.410 153.920 1.00 79.90  ? 94  SER C CA  1 
ATOM   4115  C C   . SER C  1 92  ? 163.055 152.204 154.368 1.00 82.75  ? 94  SER C C   1 
ATOM   4116  O O   . SER C  1 92  ? 163.376 152.232 155.560 1.00 88.06  ? 94  SER C O   1 
ATOM   4117  C CB  . SER C  1 92  ? 160.557 152.012 154.495 1.00 86.95  ? 94  SER C CB  1 
ATOM   4118  O OG  . SER C  1 92  ? 159.416 151.312 154.031 1.00 90.17  ? 94  SER C OG  1 
ATOM   4119  N N   . ALA C  1 93  ? 163.727 152.842 153.414 1.00 77.00  ? 95  ALA C N   1 
ATOM   4120  C CA  . ALA C  1 93  ? 164.866 153.712 153.690 1.00 72.10  ? 95  ALA C CA  1 
ATOM   4121  C C   . ALA C  1 93  ? 164.573 155.049 153.021 1.00 78.89  ? 95  ALA C C   1 
ATOM   4122  O O   . ALA C  1 93  ? 164.854 155.230 151.833 1.00 88.91  ? 95  ALA C O   1 
ATOM   4123  C CB  . ALA C  1 93  ? 166.168 153.104 153.183 1.00 73.26  ? 95  ALA C CB  1 
ATOM   4124  N N   . PHE C  1 94  ? 164.006 155.979 153.780 1.00 75.41  ? 96  PHE C N   1 
ATOM   4125  C CA  . PHE C  1 94  ? 163.594 157.277 153.263 1.00 73.99  ? 96  PHE C CA  1 
ATOM   4126  C C   . PHE C  1 94  ? 164.483 158.348 153.878 1.00 75.43  ? 96  PHE C C   1 
ATOM   4127  O O   . PHE C  1 94  ? 164.544 158.479 155.104 1.00 80.59  ? 96  PHE C O   1 
ATOM   4128  C CB  . PHE C  1 94  ? 162.123 157.550 153.578 1.00 77.23  ? 96  PHE C CB  1 
ATOM   4129  C CG  . PHE C  1 94  ? 161.159 156.771 152.723 1.00 76.98  ? 96  PHE C CG  1 
ATOM   4130  C CD1 . PHE C  1 94  ? 161.137 155.388 152.760 1.00 77.69  ? 96  PHE C CD1 1 
ATOM   4131  C CD2 . PHE C  1 94  ? 160.270 157.424 151.890 1.00 81.98  ? 96  PHE C CD2 1 
ATOM   4132  C CE1 . PHE C  1 94  ? 160.253 154.673 151.978 1.00 81.84  ? 96  PHE C CE1 1 
ATOM   4133  C CE2 . PHE C  1 94  ? 159.382 156.713 151.107 1.00 86.21  ? 96  PHE C CE2 1 
ATOM   4134  C CZ  . PHE C  1 94  ? 159.375 155.336 151.152 1.00 86.67  ? 96  PHE C CZ  1 
ATOM   4135  N N   . GLY C  1 95  ? 165.162 159.113 153.029 1.00 71.58  ? 97  GLY C N   1 
ATOM   4136  C CA  . GLY C  1 95  ? 166.056 160.147 153.507 1.00 72.87  ? 97  GLY C CA  1 
ATOM   4137  C C   . GLY C  1 95  ? 167.390 160.158 152.792 1.00 76.90  ? 97  GLY C C   1 
ATOM   4138  O O   . GLY C  1 95  ? 167.439 160.086 151.561 1.00 80.99  ? 97  GLY C O   1 
ATOM   4139  N N   . SER C  1 96  ? 168.481 160.243 153.550 1.00 77.18  ? 98  SER C N   1 
ATOM   4140  C CA  . SER C  1 96  ? 169.823 160.314 152.986 1.00 77.07  ? 98  SER C CA  1 
ATOM   4141  C C   . SER C  1 96  ? 170.698 159.248 153.626 1.00 78.75  ? 98  SER C C   1 
ATOM   4142  O O   . SER C  1 96  ? 170.851 159.222 154.852 1.00 81.18  ? 98  SER C O   1 
ATOM   4143  C CB  . SER C  1 96  ? 170.433 161.702 153.195 1.00 79.44  ? 98  SER C CB  1 
ATOM   4144  O OG  . SER C  1 96  ? 171.551 161.898 152.350 1.00 87.62  ? 98  SER C OG  1 
ATOM   4145  N N   . ASN C  1 97  ? 171.269 158.376 152.794 1.00 78.37  ? 99  ASN C N   1 
ATOM   4146  C CA  . ASN C  1 97  ? 172.237 157.364 153.223 1.00 76.97  ? 99  ASN C CA  1 
ATOM   4147  C C   . ASN C  1 97  ? 171.690 156.456 154.319 1.00 79.03  ? 99  ASN C C   1 
ATOM   4148  O O   . ASN C  1 97  ? 172.429 156.031 155.209 1.00 86.13  ? 99  ASN C O   1 
ATOM   4149  C CB  . ASN C  1 97  ? 173.547 158.009 153.681 1.00 80.56  ? 99  ASN C CB  1 
ATOM   4150  C CG  . ASN C  1 97  ? 174.082 159.007 152.681 1.00 86.84  ? 99  ASN C CG  1 
ATOM   4151  O OD1 . ASN C  1 97  ? 173.517 160.084 152.498 1.00 89.63  ? 99  ASN C OD1 1 
ATOM   4152  N ND2 . ASN C  1 97  ? 175.176 158.651 152.020 1.00 87.35  ? 99  ASN C ND2 1 
ATOM   4153  N N   . ASN C  1 98  ? 170.404 156.133 154.263 1.00 77.59  ? 100 ASN C N   1 
ATOM   4154  C CA  . ASN C  1 98  ? 169.820 155.188 155.202 1.00 73.35  ? 100 ASN C CA  1 
ATOM   4155  C C   . ASN C  1 98  ? 169.994 153.769 154.682 1.00 78.62  ? 100 ASN C C   1 
ATOM   4156  O O   . ASN C  1 98  ? 169.974 153.531 153.472 1.00 87.33  ? 100 ASN C O   1 
ATOM   4157  C CB  . ASN C  1 98  ? 168.339 155.485 155.428 1.00 72.36  ? 100 ASN C CB  1 
ATOM   4158  C CG  . ASN C  1 98  ? 168.106 156.855 156.018 1.00 78.87  ? 100 ASN C CG  1 
ATOM   4159  O OD1 . ASN C  1 98  ? 168.186 157.042 157.229 1.00 78.63  ? 100 ASN C OD1 1 
ATOM   4160  N ND2 . ASN C  1 98  ? 167.813 157.824 155.163 1.00 82.78  ? 100 ASN C ND2 1 
ATOM   4161  N N   . ALA C  1 99  ? 170.170 152.829 155.606 1.00 76.24  ? 101 ALA C N   1 
ATOM   4162  C CA  . ALA C  1 99  ? 170.338 151.416 155.274 1.00 76.44  ? 101 ALA C CA  1 
ATOM   4163  C C   . ALA C  1 99  ? 169.401 150.613 156.167 1.00 82.38  ? 101 ALA C C   1 
ATOM   4164  O O   . ALA C  1 99  ? 169.693 150.392 157.345 1.00 85.98  ? 101 ALA C O   1 
ATOM   4165  C CB  . ALA C  1 99  ? 171.787 150.975 155.448 1.00 75.47  ? 101 ALA C CB  1 
ATOM   4166  N N   . ALA C  1 100 ? 168.278 150.175 155.607 1.00 83.49  ? 102 ALA C N   1 
ATOM   4167  C CA  . ALA C  1 100 ? 167.295 149.381 156.339 1.00 82.16  ? 102 ALA C CA  1 
ATOM   4168  C C   . ALA C  1 100 ? 167.479 147.926 155.925 1.00 88.25  ? 102 ALA C C   1 
ATOM   4169  O O   . ALA C  1 100 ? 166.909 147.464 154.937 1.00 91.13  ? 102 ALA C O   1 
ATOM   4170  C CB  . ALA C  1 100 ? 165.880 149.874 156.063 1.00 81.48  ? 102 ALA C CB  1 
ATOM   4171  N N   . ASP C  1 101 ? 168.285 147.200 156.693 1.00 89.00  ? 103 ASP C N   1 
ATOM   4172  C CA  . ASP C  1 101 ? 168.549 145.787 156.443 1.00 85.49  ? 103 ASP C CA  1 
ATOM   4173  C C   . ASP C  1 101 ? 167.920 144.995 157.584 1.00 89.86  ? 103 ASP C C   1 
ATOM   4174  O O   . ASP C  1 101 ? 168.581 144.614 158.548 1.00 92.77  ? 103 ASP C O   1 
ATOM   4175  C CB  . ASP C  1 101 ? 170.047 145.528 156.329 1.00 92.74  ? 103 ASP C CB  1 
ATOM   4176  C CG  . ASP C  1 101 ? 170.709 146.396 155.278 1.00 104.62 ? 103 ASP C CG  1 
ATOM   4177  O OD1 . ASP C  1 101 ? 170.704 147.634 155.440 1.00 105.19 ? 103 ASP C OD1 1 
ATOM   4178  O OD2 . ASP C  1 101 ? 171.233 145.842 154.290 1.00 114.96 ? 103 ASP C OD2 1 
ATOM   4179  N N   . GLY C  1 102 ? 166.627 144.729 157.451 1.00 88.26  ? 104 GLY C N   1 
ATOM   4180  C CA  . GLY C  1 102 ? 165.879 144.017 158.465 1.00 81.27  ? 104 GLY C CA  1 
ATOM   4181  C C   . GLY C  1 102 ? 164.444 143.818 158.035 1.00 84.43  ? 104 GLY C C   1 
ATOM   4182  O O   . GLY C  1 102 ? 163.873 144.679 157.360 1.00 88.51  ? 104 GLY C O   1 
ATOM   4183  N N   . VAL C  1 103 ? 163.850 142.686 158.407 1.00 86.78  ? 105 VAL C N   1 
ATOM   4184  C CA  . VAL C  1 103 ? 162.484 142.396 157.996 1.00 84.51  ? 105 VAL C CA  1 
ATOM   4185  C C   . VAL C  1 103 ? 161.535 143.374 158.672 1.00 85.56  ? 105 VAL C C   1 
ATOM   4186  O O   . VAL C  1 103 ? 161.579 143.561 159.895 1.00 89.82  ? 105 VAL C O   1 
ATOM   4187  C CB  . VAL C  1 103 ? 162.120 140.942 158.329 1.00 80.02  ? 105 VAL C CB  1 
ATOM   4188  C CG1 . VAL C  1 103 ? 160.629 140.724 158.175 1.00 79.87  ? 105 VAL C CG1 1 
ATOM   4189  C CG2 . VAL C  1 103 ? 162.899 139.988 157.441 1.00 78.67  ? 105 VAL C CG2 1 
ATOM   4190  N N   . ASN C  1 104 ? 160.674 144.007 157.873 1.00 79.00  ? 106 ASN C N   1 
ATOM   4191  C CA  . ASN C  1 104 ? 159.704 144.987 158.364 1.00 78.83  ? 106 ASN C CA  1 
ATOM   4192  C C   . ASN C  1 104 ? 160.390 146.108 159.142 1.00 84.97  ? 106 ASN C C   1 
ATOM   4193  O O   . ASN C  1 104 ? 159.876 146.594 160.151 1.00 94.59  ? 106 ASN C O   1 
ATOM   4194  C CB  . ASN C  1 104 ? 158.619 144.317 159.208 1.00 83.10  ? 106 ASN C CB  1 
ATOM   4195  C CG  . ASN C  1 104 ? 157.976 143.144 158.501 1.00 86.30  ? 106 ASN C CG  1 
ATOM   4196  O OD1 . ASN C  1 104 ? 157.773 143.171 157.288 1.00 90.80  ? 106 ASN C OD1 1 
ATOM   4197  N ND2 . ASN C  1 104 ? 157.650 142.105 159.257 1.00 87.63  ? 106 ASN C ND2 1 
ATOM   4198  N N   . SER C  1 105 ? 161.558 146.527 158.666 1.00 82.82  ? 107 SER C N   1 
ATOM   4199  C CA  . SER C  1 105 ? 162.347 147.560 159.316 1.00 82.53  ? 107 SER C CA  1 
ATOM   4200  C C   . SER C  1 105 ? 162.288 148.853 158.514 1.00 85.65  ? 107 SER C C   1 
ATOM   4201  O O   . SER C  1 105 ? 162.186 148.837 157.284 1.00 91.33  ? 107 SER C O   1 
ATOM   4202  C CB  . SER C  1 105 ? 163.804 147.121 159.481 1.00 84.44  ? 107 SER C CB  1 
ATOM   4203  O OG  . SER C  1 105 ? 164.597 147.584 158.404 1.00 85.75  ? 107 SER C OG  1 
ATOM   4204  N N   . SER C  1 106 ? 162.358 149.976 159.225 1.00 81.52  ? 108 SER C N   1 
ATOM   4205  C CA  . SER C  1 106 ? 162.255 151.296 158.619 1.00 77.24  ? 108 SER C CA  1 
ATOM   4206  C C   . SER C  1 106 ? 163.381 152.181 159.129 1.00 79.57  ? 108 SER C C   1 
ATOM   4207  O O   . SER C  1 106 ? 163.604 152.270 160.340 1.00 83.80  ? 108 SER C O   1 
ATOM   4208  C CB  . SER C  1 106 ? 160.900 151.938 158.928 1.00 82.57  ? 108 SER C CB  1 
ATOM   4209  O OG  . SER C  1 106 ? 159.851 150.996 158.796 1.00 89.52  ? 108 SER C OG  1 
ATOM   4210  N N   . ALA C  1 107 ? 164.083 152.833 158.206 1.00 77.65  ? 109 ALA C N   1 
ATOM   4211  C CA  . ALA C  1 107 ? 165.149 153.775 158.531 1.00 71.02  ? 109 ALA C CA  1 
ATOM   4212  C C   . ALA C  1 107 ? 164.818 155.103 157.868 1.00 74.51  ? 109 ALA C C   1 
ATOM   4213  O O   . ALA C  1 107 ? 164.887 155.224 156.641 1.00 81.07  ? 109 ALA C O   1 
ATOM   4214  C CB  . ALA C  1 107 ? 166.507 153.252 158.067 1.00 73.34  ? 109 ALA C CB  1 
ATOM   4215  N N   . PHE C  1 108 ? 164.457 156.097 158.675 1.00 70.97  ? 110 PHE C N   1 
ATOM   4216  C CA  . PHE C  1 108 ? 164.038 157.399 158.177 1.00 69.83  ? 110 PHE C CA  1 
ATOM   4217  C C   . PHE C  1 108 ? 164.945 158.466 158.766 1.00 76.38  ? 110 PHE C C   1 
ATOM   4218  O O   . PHE C  1 108 ? 165.225 158.450 159.968 1.00 84.70  ? 110 PHE C O   1 
ATOM   4219  C CB  . PHE C  1 108 ? 162.576 157.685 158.539 1.00 74.47  ? 110 PHE C CB  1 
ATOM   4220  C CG  . PHE C  1 108 ? 161.580 156.939 157.695 1.00 75.17  ? 110 PHE C CG  1 
ATOM   4221  C CD1 . PHE C  1 108 ? 161.521 155.557 157.721 1.00 77.68  ? 110 PHE C CD1 1 
ATOM   4222  C CD2 . PHE C  1 108 ? 160.695 157.621 156.881 1.00 76.50  ? 110 PHE C CD2 1 
ATOM   4223  C CE1 . PHE C  1 108 ? 160.607 154.873 156.949 1.00 78.75  ? 110 PHE C CE1 1 
ATOM   4224  C CE2 . PHE C  1 108 ? 159.778 156.940 156.107 1.00 78.62  ? 110 PHE C CE2 1 
ATOM   4225  C CZ  . PHE C  1 108 ? 159.735 155.565 156.142 1.00 79.74  ? 110 PHE C CZ  1 
ATOM   4226  N N   . GLY C  1 109 ? 165.406 159.390 157.922 1.00 71.91  ? 111 GLY C N   1 
ATOM   4227  C CA  . GLY C  1 109 ? 166.274 160.470 158.349 1.00 73.52  ? 111 GLY C CA  1 
ATOM   4228  C C   . GLY C  1 109 ? 167.585 160.463 157.574 1.00 77.62  ? 111 GLY C C   1 
ATOM   4229  O O   . GLY C  1 109 ? 167.609 160.196 156.370 1.00 81.28  ? 111 GLY C O   1 
ATOM   4230  N N   . PHE C  1 110 ? 168.672 160.758 158.282 1.00 76.00  ? 112 PHE C N   1 
ATOM   4231  C CA  . PHE C  1 110 ? 169.999 160.856 157.688 1.00 74.82  ? 112 PHE C CA  1 
ATOM   4232  C C   . PHE C  1 110 ? 170.906 159.790 158.287 1.00 80.22  ? 112 PHE C C   1 
ATOM   4233  O O   . PHE C  1 110 ? 171.120 159.768 159.503 1.00 83.15  ? 112 PHE C O   1 
ATOM   4234  C CB  . PHE C  1 110 ? 170.592 162.245 157.912 1.00 76.23  ? 112 PHE C CB  1 
ATOM   4235  C CG  . PHE C  1 110 ? 172.058 162.332 157.610 1.00 80.45  ? 112 PHE C CG  1 
ATOM   4236  C CD1 . PHE C  1 110 ? 172.530 162.090 156.334 1.00 83.82  ? 112 PHE C CD1 1 
ATOM   4237  C CD2 . PHE C  1 110 ? 172.963 162.654 158.604 1.00 79.98  ? 112 PHE C CD2 1 
ATOM   4238  C CE1 . PHE C  1 110 ? 173.878 162.168 156.055 1.00 83.18  ? 112 PHE C CE1 1 
ATOM   4239  C CE2 . PHE C  1 110 ? 174.312 162.733 158.330 1.00 79.14  ? 112 PHE C CE2 1 
ATOM   4240  C CZ  . PHE C  1 110 ? 174.770 162.490 157.054 1.00 81.40  ? 112 PHE C CZ  1 
ATOM   4241  N N   . LYS C  1 111 ? 171.449 158.929 157.428 1.00 80.32  ? 113 LYS C N   1 
ATOM   4242  C CA  . LYS C  1 111 ? 172.410 157.890 157.804 1.00 78.30  ? 113 LYS C CA  1 
ATOM   4243  C C   . LYS C  1 111 ? 171.938 157.108 159.034 1.00 80.85  ? 113 LYS C C   1 
ATOM   4244  O O   . LYS C  1 111 ? 172.545 157.130 160.102 1.00 84.01  ? 113 LYS C O   1 
ATOM   4245  C CB  . LYS C  1 111 ? 173.801 158.490 158.030 1.00 76.53  ? 113 LYS C CB  1 
ATOM   4246  C CG  . LYS C  1 111 ? 174.897 157.444 158.176 1.00 83.97  ? 113 LYS C CG  1 
ATOM   4247  C CD  . LYS C  1 111 ? 175.741 157.335 156.926 1.00 89.11  ? 113 LYS C CD  1 
ATOM   4248  C CE  . LYS C  1 111 ? 176.521 156.034 156.897 1.00 94.80  ? 113 LYS C CE  1 
ATOM   4249  N NZ  . LYS C  1 111 ? 175.628 154.854 157.047 1.00 92.23  ? 113 LYS C NZ  1 
ATOM   4250  N N   . ASN C  1 112 ? 170.821 156.417 158.851 1.00 77.82  ? 114 ASN C N   1 
ATOM   4251  C CA  . ASN C  1 112 ? 170.291 155.516 159.862 1.00 76.41  ? 114 ASN C CA  1 
ATOM   4252  C C   . ASN C  1 112 ? 170.403 154.087 159.356 1.00 80.39  ? 114 ASN C C   1 
ATOM   4253  O O   . ASN C  1 112 ? 170.000 153.791 158.226 1.00 88.84  ? 114 ASN C O   1 
ATOM   4254  C CB  . ASN C  1 112 ? 168.838 155.852 160.195 1.00 75.97  ? 114 ASN C CB  1 
ATOM   4255  C CG  . ASN C  1 112 ? 168.718 157.012 161.157 1.00 79.34  ? 114 ASN C CG  1 
ATOM   4256  O OD1 . ASN C  1 112 ? 169.208 156.952 162.283 1.00 79.49  ? 114 ASN C OD1 1 
ATOM   4257  N ND2 . ASN C  1 112 ? 168.066 158.079 160.717 1.00 82.56  ? 114 ASN C ND2 1 
ATOM   4258  N N   . THR C  1 113 ? 170.955 153.208 160.187 1.00 76.10  ? 115 THR C N   1 
ATOM   4259  C CA  . THR C  1 113 ? 171.109 151.798 159.849 1.00 78.01  ? 115 THR C CA  1 
ATOM   4260  C C   . THR C  1 113 ? 170.271 150.983 160.822 1.00 80.58  ? 115 THR C C   1 
ATOM   4261  O O   . THR C  1 113 ? 170.482 151.047 162.036 1.00 84.55  ? 115 THR C O   1 
ATOM   4262  C CB  . THR C  1 113 ? 172.575 151.374 159.901 1.00 82.51  ? 115 THR C CB  1 
ATOM   4263  O OG1 . THR C  1 113 ? 173.321 152.111 158.925 1.00 92.30  ? 115 THR C OG1 1 
ATOM   4264  C CG2 . THR C  1 113 ? 172.706 149.887 159.616 1.00 81.24  ? 115 THR C CG2 1 
ATOM   4265  N N   . VAL C  1 114 ? 169.321 150.221 160.292 1.00 79.82  ? 116 VAL C N   1 
ATOM   4266  C CA  . VAL C  1 114 ? 168.477 149.343 161.090 1.00 79.64  ? 116 VAL C CA  1 
ATOM   4267  C C   . VAL C  1 114 ? 168.746 147.915 160.645 1.00 83.25  ? 116 VAL C C   1 
ATOM   4268  O O   . VAL C  1 114 ? 168.482 147.556 159.491 1.00 87.06  ? 116 VAL C O   1 
ATOM   4269  C CB  . VAL C  1 114 ? 166.991 149.700 160.949 1.00 80.37  ? 116 VAL C CB  1 
ATOM   4270  C CG1 . VAL C  1 114 ? 166.180 148.988 162.008 1.00 81.02  ? 116 VAL C CG1 1 
ATOM   4271  C CG2 . VAL C  1 114 ? 166.801 151.197 161.062 1.00 84.74  ? 116 VAL C CG2 1 
ATOM   4272  N N   . SER C  1 115 ? 169.274 147.103 161.557 1.00 84.42  ? 117 SER C N   1 
ATOM   4273  C CA  . SER C  1 115 ? 169.648 145.729 161.256 1.00 86.76  ? 117 SER C CA  1 
ATOM   4274  C C   . SER C  1 115 ? 168.774 144.714 161.977 1.00 88.59  ? 117 SER C C   1 
ATOM   4275  O O   . SER C  1 115 ? 169.011 143.508 161.853 1.00 96.43  ? 117 SER C O   1 
ATOM   4276  C CB  . SER C  1 115 ? 171.118 145.495 161.606 1.00 91.87  ? 117 SER C CB  1 
ATOM   4277  O OG  . SER C  1 115 ? 171.442 144.118 161.542 1.00 107.10 ? 117 SER C OG  1 
ATOM   4278  N N   . GLY C  1 116 ? 167.768 145.168 162.723 1.00 85.16  ? 118 GLY C N   1 
ATOM   4279  C CA  . GLY C  1 116 ? 166.935 144.290 163.510 1.00 86.05  ? 118 GLY C CA  1 
ATOM   4280  C C   . GLY C  1 116 ? 165.635 143.917 162.812 1.00 88.14  ? 118 GLY C C   1 
ATOM   4281  O O   . GLY C  1 116 ? 165.344 144.324 161.691 1.00 90.94  ? 118 GLY C O   1 
ATOM   4282  N N   . PHE C  1 117 ? 164.843 143.121 163.522 1.00 88.69  ? 119 PHE C N   1 
ATOM   4283  C CA  . PHE C  1 117 ? 163.568 142.616 163.032 1.00 87.05  ? 119 PHE C CA  1 
ATOM   4284  C C   . PHE C  1 117 ? 162.447 143.501 163.562 1.00 86.24  ? 119 PHE C C   1 
ATOM   4285  O O   . PHE C  1 117 ? 162.301 143.657 164.779 1.00 92.98  ? 119 PHE C O   1 
ATOM   4286  C CB  . PHE C  1 117 ? 163.382 141.162 163.467 1.00 87.40  ? 119 PHE C CB  1 
ATOM   4287  C CG  . PHE C  1 117 ? 162.061 140.565 163.079 1.00 89.39  ? 119 PHE C CG  1 
ATOM   4288  C CD1 . PHE C  1 117 ? 161.497 140.820 161.845 1.00 90.58  ? 119 PHE C CD1 1 
ATOM   4289  C CD2 . PHE C  1 117 ? 161.394 139.724 163.950 1.00 90.78  ? 119 PHE C CD2 1 
ATOM   4290  C CE1 . PHE C  1 117 ? 160.285 140.259 161.497 1.00 91.14  ? 119 PHE C CE1 1 
ATOM   4291  C CE2 . PHE C  1 117 ? 160.183 139.163 163.606 1.00 90.96  ? 119 PHE C CE2 1 
ATOM   4292  C CZ  . PHE C  1 117 ? 159.629 139.430 162.377 1.00 87.60  ? 119 PHE C CZ  1 
ATOM   4293  N N   . ASN C  1 118 ? 161.670 144.086 162.648 1.00 79.97  ? 120 ASN C N   1 
ATOM   4294  C CA  . ASN C  1 118 ? 160.556 144.973 162.992 1.00 79.62  ? 120 ASN C CA  1 
ATOM   4295  C C   . ASN C  1 118 ? 161.012 146.190 163.790 1.00 84.42  ? 120 ASN C C   1 
ATOM   4296  O O   . ASN C  1 118 ? 160.252 146.737 164.591 1.00 92.34  ? 120 ASN C O   1 
ATOM   4297  C CB  . ASN C  1 118 ? 159.456 144.227 163.754 1.00 80.14  ? 120 ASN C CB  1 
ATOM   4298  C CG  . ASN C  1 118 ? 158.384 143.677 162.841 1.00 83.92  ? 120 ASN C CG  1 
ATOM   4299  O OD1 . ASN C  1 118 ? 157.642 144.431 162.215 1.00 86.20  ? 120 ASN C OD1 1 
ATOM   4300  N ND2 . ASN C  1 118 ? 158.287 142.357 162.770 1.00 84.37  ? 120 ASN C ND2 1 
ATOM   4301  N N   . SER C  1 119 ? 162.246 146.632 163.580 1.00 83.53  ? 121 SER C N   1 
ATOM   4302  C CA  . SER C  1 119 ? 162.787 147.779 164.292 1.00 80.65  ? 121 SER C CA  1 
ATOM   4303  C C   . SER C  1 119 ? 162.766 149.019 163.408 1.00 84.86  ? 121 SER C C   1 
ATOM   4304  O O   . SER C  1 119 ? 162.752 148.938 162.178 1.00 91.53  ? 121 SER C O   1 
ATOM   4305  C CB  . SER C  1 119 ? 164.213 147.498 164.769 1.00 83.80  ? 121 SER C CB  1 
ATOM   4306  O OG  . SER C  1 119 ? 164.904 146.688 163.839 1.00 92.27  ? 121 SER C OG  1 
ATOM   4307  N N   . SER C  1 120 ? 162.772 150.180 164.057 1.00 82.18  ? 122 SER C N   1 
ATOM   4308  C CA  . SER C  1 120 ? 162.654 151.459 163.376 1.00 76.90  ? 122 SER C CA  1 
ATOM   4309  C C   . SER C  1 120 ? 163.690 152.430 163.922 1.00 75.39  ? 122 SER C C   1 
ATOM   4310  O O   . SER C  1 120 ? 164.224 152.250 165.018 1.00 80.87  ? 122 SER C O   1 
ATOM   4311  C CB  . SER C  1 120 ? 161.249 152.051 163.536 1.00 82.63  ? 122 SER C CB  1 
ATOM   4312  O OG  . SER C  1 120 ? 160.266 151.172 163.019 1.00 87.81  ? 122 SER C OG  1 
ATOM   4313  N N   . ALA C  1 121 ? 163.979 153.464 163.136 1.00 75.03  ? 123 ALA C N   1 
ATOM   4314  C CA  . ALA C  1 121 ? 164.911 154.500 163.559 1.00 74.19  ? 123 ALA C CA  1 
ATOM   4315  C C   . ALA C  1 121 ? 164.592 155.784 162.813 1.00 77.21  ? 123 ALA C C   1 
ATOM   4316  O O   . ALA C  1 121 ? 164.450 155.771 161.587 1.00 83.84  ? 123 ALA C O   1 
ATOM   4317  C CB  . ALA C  1 121 ? 166.362 154.081 163.305 1.00 72.45  ? 123 ALA C CB  1 
ATOM   4318  N N   . PHE C  1 122 ? 164.476 156.884 163.552 1.00 71.41  ? 124 PHE C N   1 
ATOM   4319  C CA  . PHE C  1 122 ? 164.252 158.200 162.972 1.00 67.78  ? 124 PHE C CA  1 
ATOM   4320  C C   . PHE C  1 122 ? 165.226 159.182 163.600 1.00 75.64  ? 124 PHE C C   1 
ATOM   4321  O O   . PHE C  1 122 ? 165.354 159.232 164.826 1.00 80.29  ? 124 PHE C O   1 
ATOM   4322  C CB  . PHE C  1 122 ? 162.812 158.671 163.186 1.00 70.76  ? 124 PHE C CB  1 
ATOM   4323  C CG  . PHE C  1 122 ? 162.506 159.987 162.535 1.00 77.23  ? 124 PHE C CG  1 
ATOM   4324  C CD1 . PHE C  1 122 ? 162.694 160.162 161.176 1.00 82.38  ? 124 PHE C CD1 1 
ATOM   4325  C CD2 . PHE C  1 122 ? 162.040 161.052 163.282 1.00 77.80  ? 124 PHE C CD2 1 
ATOM   4326  C CE1 . PHE C  1 122 ? 162.415 161.373 160.575 1.00 87.56  ? 124 PHE C CE1 1 
ATOM   4327  C CE2 . PHE C  1 122 ? 161.763 162.265 162.687 1.00 75.91  ? 124 PHE C CE2 1 
ATOM   4328  C CZ  . PHE C  1 122 ? 161.950 162.425 161.332 1.00 85.20  ? 124 PHE C CZ  1 
ATOM   4329  N N   . GLY C  1 123 ? 165.907 159.960 162.765 1.00 73.66  ? 125 GLY C N   1 
ATOM   4330  C CA  . GLY C  1 123 ? 166.885 160.905 163.262 1.00 75.25  ? 125 GLY C CA  1 
ATOM   4331  C C   . GLY C  1 123 ? 168.121 160.982 162.394 1.00 80.89  ? 125 GLY C C   1 
ATOM   4332  O O   . GLY C  1 123 ? 168.018 161.019 161.165 1.00 87.77  ? 125 GLY C O   1 
ATOM   4333  N N   . SER C  1 124 ? 169.299 161.008 163.015 1.00 78.79  ? 126 SER C N   1 
ATOM   4334  C CA  . SER C  1 124 ? 170.548 161.110 162.275 1.00 81.13  ? 126 SER C CA  1 
ATOM   4335  C C   . SER C  1 124 ? 171.624 160.270 162.942 1.00 82.77  ? 126 SER C C   1 
ATOM   4336  O O   . SER C  1 124 ? 171.806 160.344 164.160 1.00 85.31  ? 126 SER C O   1 
ATOM   4337  C CB  . SER C  1 124 ? 171.011 162.567 162.174 1.00 83.54  ? 126 SER C CB  1 
ATOM   4338  O OG  . SER C  1 124 ? 171.525 163.020 163.412 1.00 87.72  ? 126 SER C OG  1 
ATOM   4339  N N   . GLN C  1 125 ? 172.331 159.475 162.136 1.00 80.93  ? 127 GLN C N   1 
ATOM   4340  C CA  . GLN C  1 125 ? 173.533 158.761 162.567 1.00 79.92  ? 127 GLN C CA  1 
ATOM   4341  C C   . GLN C  1 125 ? 173.256 157.839 163.753 1.00 82.88  ? 127 GLN C C   1 
ATOM   4342  O O   . GLN C  1 125 ? 173.978 157.839 164.751 1.00 88.84  ? 127 GLN C O   1 
ATOM   4343  C CB  . GLN C  1 125 ? 174.658 159.747 162.886 1.00 84.14  ? 127 GLN C CB  1 
ATOM   4344  C CG  . GLN C  1 125 ? 174.946 160.721 161.760 1.00 87.53  ? 127 GLN C CG  1 
ATOM   4345  C CD  . GLN C  1 125 ? 175.814 161.879 162.197 1.00 91.94  ? 127 GLN C CD  1 
ATOM   4346  O OE1 . GLN C  1 125 ? 177.040 161.808 162.134 1.00 96.20  ? 127 GLN C OE1 1 
ATOM   4347  N NE2 . GLN C  1 125 ? 175.182 162.955 162.645 1.00 92.91  ? 127 GLN C NE2 1 
ATOM   4348  N N   . TYR C  1 126 ? 172.202 157.037 163.634 1.00 82.13  ? 128 TYR C N   1 
ATOM   4349  C CA  . TYR C  1 126 ? 171.829 156.080 164.665 1.00 79.39  ? 128 TYR C CA  1 
ATOM   4350  C C   . TYR C  1 126 ? 171.737 154.688 164.061 1.00 80.19  ? 128 TYR C C   1 
ATOM   4351  O O   . TYR C  1 126 ? 171.271 154.523 162.930 1.00 85.61  ? 128 TYR C O   1 
ATOM   4352  C CB  . TYR C  1 126 ? 170.495 156.453 165.317 1.00 77.53  ? 128 TYR C CB  1 
ATOM   4353  C CG  . TYR C  1 126 ? 170.616 156.881 166.761 1.00 79.39  ? 128 TYR C CG  1 
ATOM   4354  C CD1 . TYR C  1 126 ? 171.631 156.390 167.569 1.00 75.67  ? 128 TYR C CD1 1 
ATOM   4355  C CD2 . TYR C  1 126 ? 169.715 157.778 167.315 1.00 80.19  ? 128 TYR C CD2 1 
ATOM   4356  C CE1 . TYR C  1 126 ? 171.743 156.779 168.889 1.00 78.80  ? 128 TYR C CE1 1 
ATOM   4357  C CE2 . TYR C  1 126 ? 169.820 158.173 168.632 1.00 80.99  ? 128 TYR C CE2 1 
ATOM   4358  C CZ  . TYR C  1 126 ? 170.834 157.671 169.413 1.00 84.00  ? 128 TYR C CZ  1 
ATOM   4359  O OH  . TYR C  1 126 ? 170.939 158.065 170.726 1.00 89.96  ? 128 TYR C OH  1 
ATOM   4360  N N   . GLN C  1 127 ? 172.181 153.690 164.820 1.00 76.99  ? 129 GLN C N   1 
ATOM   4361  C CA  . GLN C  1 127 ? 172.111 152.298 164.404 1.00 76.06  ? 129 GLN C CA  1 
ATOM   4362  C C   . GLN C  1 127 ? 171.293 151.501 165.408 1.00 79.89  ? 129 GLN C C   1 
ATOM   4363  O O   . GLN C  1 127 ? 171.472 151.642 166.621 1.00 85.38  ? 129 GLN C O   1 
ATOM   4364  C CB  . GLN C  1 127 ? 173.502 151.679 164.266 1.00 77.68  ? 129 GLN C CB  1 
ATOM   4365  C CG  . GLN C  1 127 ? 173.548 150.517 163.291 1.00 84.13  ? 129 GLN C CG  1 
ATOM   4366  C CD  . GLN C  1 127 ? 174.696 149.573 163.560 1.00 91.41  ? 129 GLN C CD  1 
ATOM   4367  O OE1 . GLN C  1 127 ? 175.180 149.474 164.685 1.00 92.70  ? 129 GLN C OE1 1 
ATOM   4368  N NE2 . GLN C  1 127 ? 175.139 148.868 162.527 1.00 93.22  ? 129 GLN C NE2 1 
ATOM   4369  N N   . VAL C  1 128 ? 170.394 150.666 164.897 1.00 81.39  ? 130 VAL C N   1 
ATOM   4370  C CA  . VAL C  1 128 ? 169.539 149.818 165.719 1.00 81.95  ? 130 VAL C CA  1 
ATOM   4371  C C   . VAL C  1 128 ? 169.733 148.390 165.229 1.00 84.73  ? 130 VAL C C   1 
ATOM   4372  O O   . VAL C  1 128 ? 169.266 148.030 164.143 1.00 88.45  ? 130 VAL C O   1 
ATOM   4373  C CB  . VAL C  1 128 ? 168.065 150.228 165.651 1.00 74.91  ? 130 VAL C CB  1 
ATOM   4374  C CG1 . VAL C  1 128 ? 167.225 149.313 166.519 1.00 80.07  ? 130 VAL C CG1 1 
ATOM   4375  C CG2 . VAL C  1 128 ? 167.899 151.672 166.080 1.00 76.69  ? 130 VAL C CG2 1 
ATOM   4376  N N   . THR C  1 129 ? 170.421 147.573 166.021 1.00 83.07  ? 131 THR C N   1 
ATOM   4377  C CA  . THR C  1 129 ? 170.637 146.172 165.694 1.00 84.07  ? 131 THR C CA  1 
ATOM   4378  C C   . THR C  1 129 ? 169.796 145.233 166.545 1.00 88.11  ? 131 THR C C   1 
ATOM   4379  O O   . THR C  1 129 ? 169.811 144.022 166.306 1.00 93.54  ? 131 THR C O   1 
ATOM   4380  C CB  . THR C  1 129 ? 172.117 145.814 165.847 1.00 91.09  ? 131 THR C CB  1 
ATOM   4381  O OG1 . THR C  1 129 ? 172.520 146.021 167.205 1.00 96.79  ? 131 THR C OG1 1 
ATOM   4382  C CG2 . THR C  1 129 ? 172.969 146.680 164.936 1.00 91.76  ? 131 THR C CG2 1 
ATOM   4383  N N   . GLY C  1 130 ? 169.065 145.757 167.525 1.00 87.21  ? 132 GLY C N   1 
ATOM   4384  C CA  . GLY C  1 130 ? 168.193 144.928 168.325 1.00 89.47  ? 132 GLY C CA  1 
ATOM   4385  C C   . GLY C  1 130 ? 166.906 144.587 167.605 1.00 90.17  ? 132 GLY C C   1 
ATOM   4386  O O   . GLY C  1 130 ? 166.561 145.159 166.572 1.00 92.68  ? 132 GLY C O   1 
ATOM   4387  N N   . ASN C  1 131 ? 166.179 143.634 168.176 1.00 89.47  ? 133 ASN C N   1 
ATOM   4388  C CA  . ASN C  1 131 ? 164.923 143.164 167.611 1.00 86.06  ? 133 ASN C CA  1 
ATOM   4389  C C   . ASN C  1 131 ? 163.764 143.877 168.292 1.00 89.87  ? 133 ASN C C   1 
ATOM   4390  O O   . ASN C  1 131 ? 163.730 143.978 169.523 1.00 93.72  ? 133 ASN C O   1 
ATOM   4391  C CB  . ASN C  1 131 ? 164.788 141.650 167.774 1.00 87.83  ? 133 ASN C CB  1 
ATOM   4392  C CG  . ASN C  1 131 ? 165.322 140.890 166.581 1.00 94.42  ? 133 ASN C CG  1 
ATOM   4393  O OD1 . ASN C  1 131 ? 165.988 141.458 165.717 1.00 98.00  ? 133 ASN C OD1 1 
ATOM   4394  N ND2 . ASN C  1 131 ? 165.034 139.596 166.527 1.00 99.97  ? 133 ASN C ND2 1 
ATOM   4395  N N   . PHE C  1 132 ? 162.821 144.368 167.487 1.00 87.01  ? 134 PHE C N   1 
ATOM   4396  C CA  . PHE C  1 132 ? 161.669 145.123 167.982 1.00 83.84  ? 134 PHE C CA  1 
ATOM   4397  C C   . PHE C  1 132 ? 162.112 146.331 168.802 1.00 85.70  ? 134 PHE C C   1 
ATOM   4398  O O   . PHE C  1 132 ? 161.516 146.660 169.828 1.00 89.29  ? 134 PHE C O   1 
ATOM   4399  C CB  . PHE C  1 132 ? 160.728 144.236 168.799 1.00 86.00  ? 134 PHE C CB  1 
ATOM   4400  C CG  . PHE C  1 132 ? 160.656 142.820 168.317 1.00 87.19  ? 134 PHE C CG  1 
ATOM   4401  C CD1 . PHE C  1 132 ? 160.134 142.523 167.073 1.00 89.47  ? 134 PHE C CD1 1 
ATOM   4402  C CD2 . PHE C  1 132 ? 161.107 141.782 169.112 1.00 88.18  ? 134 PHE C CD2 1 
ATOM   4403  C CE1 . PHE C  1 132 ? 160.062 141.221 166.631 1.00 89.51  ? 134 PHE C CE1 1 
ATOM   4404  C CE2 . PHE C  1 132 ? 161.040 140.477 168.673 1.00 88.93  ? 134 PHE C CE2 1 
ATOM   4405  C CZ  . PHE C  1 132 ? 160.517 140.196 167.430 1.00 89.25  ? 134 PHE C CZ  1 
ATOM   4406  N N   . SER C  1 133 ? 163.166 146.997 168.348 1.00 84.34  ? 135 SER C N   1 
ATOM   4407  C CA  . SER C  1 133 ? 163.739 148.142 169.035 1.00 80.58  ? 135 SER C CA  1 
ATOM   4408  C C   . SER C  1 133 ? 163.529 149.403 168.205 1.00 84.23  ? 135 SER C C   1 
ATOM   4409  O O   . SER C  1 133 ? 162.996 149.365 167.094 1.00 92.99  ? 135 SER C O   1 
ATOM   4410  C CB  . SER C  1 133 ? 165.224 147.908 169.319 1.00 83.22  ? 135 SER C CB  1 
ATOM   4411  O OG  . SER C  1 133 ? 165.435 146.632 169.898 1.00 93.62  ? 135 SER C OG  1 
ATOM   4412  N N   . GLY C  1 134 ? 163.953 150.534 168.758 1.00 80.17  ? 136 GLY C N   1 
ATOM   4413  C CA  . GLY C  1 134 ? 163.799 151.799 168.068 1.00 75.66  ? 136 GLY C CA  1 
ATOM   4414  C C   . GLY C  1 134 ? 164.697 152.862 168.651 1.00 76.08  ? 136 GLY C C   1 
ATOM   4415  O O   . GLY C  1 134 ? 165.149 152.765 169.796 1.00 83.33  ? 136 GLY C O   1 
ATOM   4416  N N   . ALA C  1 135 ? 164.951 153.888 167.844 1.00 73.02  ? 137 ALA C N   1 
ATOM   4417  C CA  . ALA C  1 135 ? 165.769 155.014 168.264 1.00 70.43  ? 137 ALA C CA  1 
ATOM   4418  C C   . ALA C  1 135 ? 165.251 156.275 167.593 1.00 75.00  ? 137 ALA C C   1 
ATOM   4419  O O   . ALA C  1 135 ? 164.953 156.271 166.396 1.00 79.96  ? 137 ALA C O   1 
ATOM   4420  C CB  . ALA C  1 135 ? 167.245 154.797 167.919 1.00 69.69  ? 137 ALA C CB  1 
ATOM   4421  N N   . PHE C  1 136 ? 165.151 157.351 168.369 1.00 73.01  ? 138 PHE C N   1 
ATOM   4422  C CA  . PHE C  1 136 ? 164.673 158.639 167.865 1.00 69.29  ? 138 PHE C CA  1 
ATOM   4423  C C   . PHE C  1 136 ? 165.589 159.721 168.426 1.00 74.72  ? 138 PHE C C   1 
ATOM   4424  O O   . PHE C  1 136 ? 165.443 160.128 169.581 1.00 80.56  ? 138 PHE C O   1 
ATOM   4425  C CB  . PHE C  1 136 ? 163.219 158.882 168.251 1.00 69.89  ? 138 PHE C CB  1 
ATOM   4426  C CG  . PHE C  1 136 ? 162.748 160.280 167.982 1.00 78.34  ? 138 PHE C CG  1 
ATOM   4427  C CD1 . PHE C  1 136 ? 162.787 160.805 166.704 1.00 75.94  ? 138 PHE C CD1 1 
ATOM   4428  C CD2 . PHE C  1 136 ? 162.263 161.069 169.009 1.00 82.98  ? 138 PHE C CD2 1 
ATOM   4429  C CE1 . PHE C  1 136 ? 162.353 162.093 166.457 1.00 73.37  ? 138 PHE C CE1 1 
ATOM   4430  C CE2 . PHE C  1 136 ? 161.828 162.356 168.765 1.00 81.74  ? 138 PHE C CE2 1 
ATOM   4431  C CZ  . PHE C  1 136 ? 161.873 162.867 167.488 1.00 75.80  ? 138 PHE C CZ  1 
ATOM   4432  N N   . GLY C  1 137 ? 166.522 160.181 167.608 1.00 71.80  ? 139 GLY C N   1 
ATOM   4433  C CA  . GLY C  1 137 ? 167.482 161.178 168.050 1.00 73.09  ? 139 GLY C CA  1 
ATOM   4434  C C   . GLY C  1 137 ? 168.686 161.199 167.124 1.00 80.98  ? 139 GLY C C   1 
ATOM   4435  O O   . GLY C  1 137 ? 168.592 160.817 165.959 1.00 88.05  ? 139 GLY C O   1 
ATOM   4436  N N   . MET C  1 138 ? 169.809 161.650 167.671 1.00 76.77  ? 140 MET C N   1 
ATOM   4437  C CA  . MET C  1 138 ? 171.054 161.747 166.926 1.00 79.96  ? 140 MET C CA  1 
ATOM   4438  C C   . MET C  1 138 ? 172.149 160.968 167.639 1.00 85.19  ? 140 MET C C   1 
ATOM   4439  O O   . MET C  1 138 ? 172.285 161.046 168.864 1.00 87.37  ? 140 MET C O   1 
ATOM   4440  C CB  . MET C  1 138 ? 171.483 163.207 166.749 1.00 84.09  ? 140 MET C CB  1 
ATOM   4441  C CG  . MET C  1 138 ? 172.984 163.420 166.823 1.00 93.55  ? 140 MET C CG  1 
ATOM   4442  S SD  . MET C  1 138 ? 173.460 165.151 166.794 1.00 112.37 ? 140 MET C SD  1 
ATOM   4443  C CE  . MET C  1 138 ? 174.838 165.139 167.936 1.00 97.49  ? 140 MET C CE  1 
ATOM   4444  N N   . GLY C  1 139 ? 172.922 160.211 166.867 1.00 81.91  ? 141 GLY C N   1 
ATOM   4445  C CA  . GLY C  1 139 ? 174.082 159.525 167.397 1.00 81.07  ? 141 GLY C CA  1 
ATOM   4446  C C   . GLY C  1 139 ? 175.368 160.118 166.863 1.00 89.39  ? 141 GLY C C   1 
ATOM   4447  O O   . GLY C  1 139 ? 175.527 161.341 166.836 1.00 93.54  ? 141 GLY C O   1 
ATOM   4448  N N   . GLU C  1 140 ? 176.295 159.266 166.434 1.00 92.52  ? 142 GLU C N   1 
ATOM   4449  C CA  . GLU C  1 140 ? 177.541 159.739 165.852 1.00 92.07  ? 142 GLU C CA  1 
ATOM   4450  C C   . GLU C  1 140 ? 178.075 158.684 164.896 1.00 92.71  ? 142 GLU C C   1 
ATOM   4451  O O   . GLU C  1 140 ? 177.972 157.482 165.154 1.00 95.66  ? 142 GLU C O   1 
ATOM   4452  C CB  . GLU C  1 140 ? 178.577 160.064 166.935 1.00 95.17  ? 142 GLU C CB  1 
ATOM   4453  C CG  . GLU C  1 140 ? 180.016 160.034 166.456 1.00 105.08 ? 142 GLU C CG  1 
ATOM   4454  C CD  . GLU C  1 140 ? 180.863 161.115 167.091 1.00 121.93 ? 142 GLU C CD  1 
ATOM   4455  O OE1 . GLU C  1 140 ? 182.104 161.042 166.976 1.00 126.27 ? 142 GLU C OE1 1 
ATOM   4456  O OE2 . GLU C  1 140 ? 180.287 162.039 167.702 1.00 122.00 ? 142 GLU C OE2 1 
ATOM   4457  N N   . PHE C  1 141 ? 178.648 159.149 163.786 1.00 88.09  ? 143 PHE C N   1 
ATOM   4458  C CA  . PHE C  1 141 ? 179.213 158.253 162.780 1.00 88.60  ? 143 PHE C CA  1 
ATOM   4459  C C   . PHE C  1 141 ? 180.476 158.912 162.232 1.00 95.56  ? 143 PHE C C   1 
ATOM   4460  O O   . PHE C  1 141 ? 180.398 159.741 161.320 1.00 101.03 ? 143 PHE C O   1 
ATOM   4461  C CB  . PHE C  1 141 ? 178.206 157.967 161.675 1.00 83.50  ? 143 PHE C CB  1 
ATOM   4462  C CG  . PHE C  1 141 ? 178.755 157.132 160.555 1.00 86.25  ? 143 PHE C CG  1 
ATOM   4463  C CD1 . PHE C  1 141 ? 178.883 155.762 160.694 1.00 89.80  ? 143 PHE C CD1 1 
ATOM   4464  C CD2 . PHE C  1 141 ? 179.140 157.716 159.362 1.00 86.46  ? 143 PHE C CD2 1 
ATOM   4465  C CE1 . PHE C  1 141 ? 179.387 154.992 159.666 1.00 90.80  ? 143 PHE C CE1 1 
ATOM   4466  C CE2 . PHE C  1 141 ? 179.645 156.951 158.332 1.00 88.94  ? 143 PHE C CE2 1 
ATOM   4467  C CZ  . PHE C  1 141 ? 179.768 155.588 158.484 1.00 89.43  ? 143 PHE C CZ  1 
ATOM   4468  N N   . ASN C  1 142 ? 181.628 158.548 162.795 1.00 94.50  ? 144 ASN C N   1 
ATOM   4469  C CA  . ASN C  1 142 ? 182.896 159.026 162.253 1.00 94.63  ? 144 ASN C CA  1 
ATOM   4470  C C   . ASN C  1 142 ? 183.325 158.176 161.063 1.00 96.60  ? 144 ASN C C   1 
ATOM   4471  O O   . ASN C  1 142 ? 183.441 158.674 159.940 1.00 101.19 ? 144 ASN C O   1 
ATOM   4472  C CB  . ASN C  1 142 ? 183.971 159.022 163.341 1.00 98.33  ? 144 ASN C CB  1 
ATOM   4473  C CG  . ASN C  1 142 ? 183.859 157.830 164.264 1.00 103.79 ? 144 ASN C CG  1 
ATOM   4474  O OD1 . ASN C  1 142 ? 183.409 156.759 163.859 1.00 104.11 ? 144 ASN C OD1 1 
ATOM   4475  N ND2 . ASN C  1 142 ? 184.269 158.008 165.513 1.00 109.87 ? 144 ASN C ND2 1 
ATOM   4476  N N   . GLY C  1 143 ? 183.574 156.892 161.299 1.00 96.69  ? 145 GLY C N   1 
ATOM   4477  C CA  . GLY C  1 143 ? 183.707 155.923 160.230 1.00 96.17  ? 145 GLY C CA  1 
ATOM   4478  C C   . GLY C  1 143 ? 182.878 154.696 160.539 1.00 98.16  ? 145 GLY C C   1 
ATOM   4479  O O   . GLY C  1 143 ? 182.609 153.865 159.667 1.00 97.89  ? 145 GLY C O   1 
ATOM   4480  N N   . GLN C  1 144 ? 182.469 154.585 161.801 1.00 98.72  ? 146 GLN C N   1 
ATOM   4481  C CA  . GLN C  1 144 ? 181.581 153.534 162.272 1.00 93.17  ? 146 GLN C CA  1 
ATOM   4482  C C   . GLN C  1 144 ? 180.578 154.151 163.233 1.00 90.47  ? 146 GLN C C   1 
ATOM   4483  O O   . GLN C  1 144 ? 180.809 155.225 163.795 1.00 94.03  ? 146 GLN C O   1 
ATOM   4484  C CB  . GLN C  1 144 ? 182.340 152.397 162.972 1.00 89.00  ? 146 GLN C CB  1 
ATOM   4485  C CG  . GLN C  1 144 ? 183.634 151.977 162.300 1.00 96.57  ? 146 GLN C CG  1 
ATOM   4486  C CD  . GLN C  1 144 ? 183.408 150.967 161.197 1.00 105.80 ? 146 GLN C CD  1 
ATOM   4487  O OE1 . GLN C  1 144 ? 182.419 150.236 161.202 1.00 105.81 ? 146 GLN C OE1 1 
ATOM   4488  N NE2 . GLN C  1 144 ? 184.327 150.918 160.241 1.00 109.06 ? 146 GLN C NE2 1 
ATOM   4489  N N   . TYR C  1 145 ? 179.457 153.464 163.417 1.00 86.78  ? 147 TYR C N   1 
ATOM   4490  C CA  . TYR C  1 145 ? 178.447 153.930 164.357 1.00 84.91  ? 147 TYR C CA  1 
ATOM   4491  C C   . TYR C  1 145 ? 178.966 153.782 165.781 1.00 87.78  ? 147 TYR C C   1 
ATOM   4492  O O   . TYR C  1 145 ? 179.188 152.664 166.256 1.00 94.71  ? 147 TYR C O   1 
ATOM   4493  C CB  . TYR C  1 145 ? 177.149 153.153 164.170 1.00 83.44  ? 147 TYR C CB  1 
ATOM   4494  C CG  . TYR C  1 145 ? 176.421 153.493 162.892 1.00 83.23  ? 147 TYR C CG  1 
ATOM   4495  C CD1 . TYR C  1 145 ? 175.594 154.604 162.818 1.00 83.77  ? 147 TYR C CD1 1 
ATOM   4496  C CD2 . TYR C  1 145 ? 176.562 152.706 161.759 1.00 85.36  ? 147 TYR C CD2 1 
ATOM   4497  C CE1 . TYR C  1 145 ? 174.928 154.921 161.652 1.00 90.28  ? 147 TYR C CE1 1 
ATOM   4498  C CE2 . TYR C  1 145 ? 175.900 153.014 160.590 1.00 88.73  ? 147 TYR C CE2 1 
ATOM   4499  C CZ  . TYR C  1 145 ? 175.084 154.122 160.542 1.00 93.68  ? 147 TYR C CZ  1 
ATOM   4500  O OH  . TYR C  1 145 ? 174.422 154.432 159.377 1.00 95.38  ? 147 TYR C OH  1 
ATOM   4501  N N   . GLN C  1 146 ? 179.165 154.910 166.459 1.00 84.83  ? 148 GLN C N   1 
ATOM   4502  C CA  . GLN C  1 146 ? 179.669 154.903 167.824 1.00 89.22  ? 148 GLN C CA  1 
ATOM   4503  C C   . GLN C  1 146 ? 178.585 154.646 168.859 1.00 93.99  ? 148 GLN C C   1 
ATOM   4504  O O   . GLN C  1 146 ? 178.894 154.145 169.946 1.00 94.21  ? 148 GLN C O   1 
ATOM   4505  C CB  . GLN C  1 146 ? 180.364 156.231 168.135 1.00 92.59  ? 148 GLN C CB  1 
ATOM   4506  C CG  . GLN C  1 146 ? 181.421 156.615 167.118 1.00 99.11  ? 148 GLN C CG  1 
ATOM   4507  C CD  . GLN C  1 146 ? 182.580 155.641 167.100 1.00 102.22 ? 148 GLN C CD  1 
ATOM   4508  O OE1 . GLN C  1 146 ? 183.057 155.210 168.148 1.00 101.03 ? 148 GLN C OE1 1 
ATOM   4509  N NE2 . GLN C  1 146 ? 183.032 155.281 165.906 1.00 106.35 ? 148 GLN C NE2 1 
ATOM   4510  N N   . TYR C  1 147 ? 177.333 154.974 168.553 1.00 94.62  ? 149 TYR C N   1 
ATOM   4511  C CA  . TYR C  1 147 ? 176.221 154.784 169.476 1.00 96.39  ? 149 TYR C CA  1 
ATOM   4512  C C   . TYR C  1 147 ? 175.151 153.968 168.770 1.00 92.41  ? 149 TYR C C   1 
ATOM   4513  O O   . TYR C  1 147 ? 174.619 154.399 167.743 1.00 92.65  ? 149 TYR C O   1 
ATOM   4514  C CB  . TYR C  1 147 ? 175.663 156.131 169.941 1.00 94.06  ? 149 TYR C CB  1 
ATOM   4515  C CG  . TYR C  1 147 ? 176.710 157.027 170.560 1.00 92.02  ? 149 TYR C CG  1 
ATOM   4516  C CD1 . TYR C  1 147 ? 177.215 156.770 171.825 1.00 91.93  ? 149 TYR C CD1 1 
ATOM   4517  C CD2 . TYR C  1 147 ? 177.204 158.125 169.870 1.00 92.95  ? 149 TYR C CD2 1 
ATOM   4518  C CE1 . TYR C  1 147 ? 178.175 157.584 172.389 1.00 95.16  ? 149 TYR C CE1 1 
ATOM   4519  C CE2 . TYR C  1 147 ? 178.163 158.944 170.425 1.00 95.72  ? 149 TYR C CE2 1 
ATOM   4520  C CZ  . TYR C  1 147 ? 178.645 158.670 171.685 1.00 98.17  ? 149 TYR C CZ  1 
ATOM   4521  O OH  . TYR C  1 147 ? 179.602 159.485 172.241 1.00 102.76 ? 149 TYR C OH  1 
ATOM   4522  N N   . LYS C  1 148 ? 174.834 152.797 169.319 1.00 87.42  ? 150 LYS C N   1 
ATOM   4523  C CA  . LYS C  1 148 ? 173.905 151.880 168.678 1.00 87.30  ? 150 LYS C CA  1 
ATOM   4524  C C   . LYS C  1 148 ? 172.976 151.269 169.715 1.00 89.04  ? 150 LYS C C   1 
ATOM   4525  O O   . LYS C  1 148 ? 173.289 151.210 170.906 1.00 91.56  ? 150 LYS C O   1 
ATOM   4526  C CB  . LYS C  1 148 ? 174.640 150.767 167.923 1.00 87.73  ? 150 LYS C CB  1 
ATOM   4527  C CG  . LYS C  1 148 ? 176.087 150.590 168.336 1.00 87.98  ? 150 LYS C CG  1 
ATOM   4528  C CD  . LYS C  1 148 ? 176.811 149.661 167.383 1.00 94.75  ? 150 LYS C CD  1 
ATOM   4529  C CE  . LYS C  1 148 ? 178.314 149.740 167.563 1.00 106.81 ? 150 LYS C CE  1 
ATOM   4530  N NZ  . LYS C  1 148 ? 179.029 148.988 166.497 1.00 106.76 ? 150 LYS C NZ  1 
ATOM   4531  N N   . ASN C  1 149 ? 171.821 150.810 169.238 1.00 85.12  ? 151 ASN C N   1 
ATOM   4532  C CA  . ASN C  1 149 ? 170.841 150.106 170.061 1.00 83.36  ? 151 ASN C CA  1 
ATOM   4533  C C   . ASN C  1 149 ? 171.004 148.614 169.798 1.00 90.69  ? 151 ASN C C   1 
ATOM   4534  O O   . ASN C  1 149 ? 170.570 148.104 168.763 1.00 93.36  ? 151 ASN C O   1 
ATOM   4535  C CB  . ASN C  1 149 ? 169.426 150.571 169.739 1.00 81.81  ? 151 ASN C CB  1 
ATOM   4536  C CG  . ASN C  1 149 ? 168.420 150.140 170.785 1.00 89.82  ? 151 ASN C CG  1 
ATOM   4537  O OD1 . ASN C  1 149 ? 168.718 149.319 171.650 1.00 96.60  ? 151 ASN C OD1 1 
ATOM   4538  N ND2 . ASN C  1 149 ? 167.218 150.696 170.711 1.00 89.99  ? 151 ASN C ND2 1 
ATOM   4539  N N   . GLU C  1 150 ? 171.628 147.912 170.740 1.00 91.30  ? 152 GLU C N   1 
ATOM   4540  C CA  . GLU C  1 150 ? 171.872 146.484 170.610 1.00 94.76  ? 152 GLU C CA  1 
ATOM   4541  C C   . GLU C  1 150 ? 170.899 145.645 171.427 1.00 97.98  ? 152 GLU C C   1 
ATOM   4542  O O   . GLU C  1 150 ? 171.024 144.417 171.448 1.00 105.62 ? 152 GLU C O   1 
ATOM   4543  C CB  . GLU C  1 150 ? 173.310 146.160 171.015 1.00 102.45 ? 152 GLU C CB  1 
ATOM   4544  C CG  . GLU C  1 150 ? 174.271 146.044 169.847 1.00 107.38 ? 152 GLU C CG  1 
ATOM   4545  C CD  . GLU C  1 150 ? 175.674 146.487 170.205 1.00 116.31 ? 152 GLU C CD  1 
ATOM   4546  O OE1 . GLU C  1 150 ? 175.824 147.265 171.170 1.00 117.71 ? 152 GLU C OE1 1 
ATOM   4547  O OE2 . GLU C  1 150 ? 176.627 146.059 169.521 1.00 122.21 ? 152 GLU C OE2 1 
ATOM   4548  N N   . GLY C  1 151 ? 169.937 146.272 172.093 1.00 92.01  ? 153 GLY C N   1 
ATOM   4549  C CA  . GLY C  1 151 ? 169.004 145.569 172.948 1.00 94.93  ? 153 GLY C CA  1 
ATOM   4550  C C   . GLY C  1 151 ? 167.683 145.284 172.259 1.00 95.56  ? 153 GLY C C   1 
ATOM   4551  O O   . GLY C  1 151 ? 167.277 145.991 171.340 1.00 101.06 ? 153 GLY C O   1 
ATOM   4552  N N   . ASN C  1 152 ? 167.013 144.232 172.720 1.00 95.30  ? 154 ASN C N   1 
ATOM   4553  C CA  . ASN C  1 152 ? 165.714 143.849 172.191 1.00 91.25  ? 154 ASN C CA  1 
ATOM   4554  C C   . ASN C  1 152 ? 164.605 144.533 172.977 1.00 93.50  ? 154 ASN C C   1 
ATOM   4555  O O   . ASN C  1 152 ? 164.708 144.703 174.195 1.00 99.12  ? 154 ASN C O   1 
ATOM   4556  C CB  . ASN C  1 152 ? 165.533 142.333 172.250 1.00 91.26  ? 154 ASN C CB  1 
ATOM   4557  C CG  . ASN C  1 152 ? 166.545 141.596 171.404 1.00 99.73  ? 154 ASN C CG  1 
ATOM   4558  O OD1 . ASN C  1 152 ? 167.166 142.175 170.515 1.00 102.31 ? 154 ASN C OD1 1 
ATOM   4559  N ND2 . ASN C  1 152 ? 166.719 140.309 171.678 1.00 104.20 ? 154 ASN C ND2 1 
ATOM   4560  N N   . ASN C  1 153 ? 163.543 144.918 172.269 1.00 87.04  ? 155 ASN C N   1 
ATOM   4561  C CA  . ASN C  1 153 ? 162.376 145.557 172.879 1.00 85.27  ? 155 ASN C CA  1 
ATOM   4562  C C   . ASN C  1 153 ? 162.775 146.791 173.683 1.00 88.04  ? 155 ASN C C   1 
ATOM   4563  O O   . ASN C  1 153 ? 162.257 147.039 174.772 1.00 97.99  ? 155 ASN C O   1 
ATOM   4564  C CB  . ASN C  1 153 ? 161.604 144.568 173.754 1.00 88.89  ? 155 ASN C CB  1 
ATOM   4565  C CG  . ASN C  1 153 ? 161.091 143.377 172.973 1.00 94.32  ? 155 ASN C CG  1 
ATOM   4566  O OD1 . ASN C  1 153 ? 160.062 143.457 172.303 1.00 100.16 ? 155 ASN C OD1 1 
ATOM   4567  N ND2 . ASN C  1 153 ? 161.809 142.264 173.052 1.00 94.29  ? 155 ASN C ND2 1 
ATOM   4568  N N   . SER C  1 154 ? 163.703 147.575 173.140 1.00 84.37  ? 156 SER C N   1 
ATOM   4569  C CA  . SER C  1 154 ? 164.236 148.741 173.825 1.00 81.79  ? 156 SER C CA  1 
ATOM   4570  C C   . SER C  1 154 ? 164.153 149.956 172.914 1.00 80.17  ? 156 SER C C   1 
ATOM   4571  O O   . SER C  1 154 ? 164.311 149.849 171.696 1.00 84.14  ? 156 SER C O   1 
ATOM   4572  C CB  . SER C  1 154 ? 165.685 148.512 174.267 1.00 86.93  ? 156 SER C CB  1 
ATOM   4573  O OG  . SER C  1 154 ? 166.485 148.079 173.182 1.00 95.42  ? 156 SER C OG  1 
ATOM   4574  N N   . TYR C  1 155 ? 163.909 151.118 173.516 1.00 79.19  ? 157 TYR C N   1 
ATOM   4575  C CA  . TYR C  1 155 ? 163.713 152.351 172.767 1.00 74.76  ? 157 TYR C CA  1 
ATOM   4576  C C   . TYR C  1 155 ? 164.524 153.481 173.379 1.00 76.05  ? 157 TYR C C   1 
ATOM   4577  O O   . TYR C  1 155 ? 164.624 153.600 174.603 1.00 80.87  ? 157 TYR C O   1 
ATOM   4578  C CB  . TYR C  1 155 ? 162.232 152.731 172.712 1.00 72.30  ? 157 TYR C CB  1 
ATOM   4579  C CG  . TYR C  1 155 ? 161.454 151.900 171.724 1.00 75.80  ? 157 TYR C CG  1 
ATOM   4580  C CD1 . TYR C  1 155 ? 160.953 150.656 172.077 1.00 76.60  ? 157 TYR C CD1 1 
ATOM   4581  C CD2 . TYR C  1 155 ? 161.230 152.353 170.433 1.00 79.26  ? 157 TYR C CD2 1 
ATOM   4582  C CE1 . TYR C  1 155 ? 160.249 149.890 171.175 1.00 84.32  ? 157 TYR C CE1 1 
ATOM   4583  C CE2 . TYR C  1 155 ? 160.527 151.594 169.524 1.00 81.68  ? 157 TYR C CE2 1 
ATOM   4584  C CZ  . TYR C  1 155 ? 160.039 150.363 169.900 1.00 86.16  ? 157 TYR C CZ  1 
ATOM   4585  O OH  . TYR C  1 155 ? 159.337 149.601 168.999 1.00 90.57  ? 157 TYR C OH  1 
ATOM   4586  N N   . MET C  1 156 ? 165.103 154.305 172.510 1.00 74.83  ? 158 MET C N   1 
ATOM   4587  C CA  . MET C  1 156 ? 165.955 155.419 172.897 1.00 72.64  ? 158 MET C CA  1 
ATOM   4588  C C   . MET C  1 156 ? 165.434 156.697 172.262 1.00 75.49  ? 158 MET C C   1 
ATOM   4589  O O   . MET C  1 156 ? 165.181 156.733 171.054 1.00 79.36  ? 158 MET C O   1 
ATOM   4590  C CB  . MET C  1 156 ? 167.398 155.171 172.456 1.00 73.02  ? 158 MET C CB  1 
ATOM   4591  C CG  . MET C  1 156 ? 167.836 153.727 172.573 1.00 85.47  ? 158 MET C CG  1 
ATOM   4592  S SD  . MET C  1 156 ? 169.347 153.374 171.663 1.00 118.80 ? 158 MET C SD  1 
ATOM   4593  C CE  . MET C  1 156 ? 170.127 154.974 171.645 1.00 95.85  ? 158 MET C CE  1 
ATOM   4594  N N   . ILE C  1 157 ? 165.275 157.740 173.071 1.00 74.57  ? 159 ILE C N   1 
ATOM   4595  C CA  . ILE C  1 157 ? 164.943 159.073 172.584 1.00 71.38  ? 159 ILE C CA  1 
ATOM   4596  C C   . ILE C  1 157 ? 165.941 160.033 173.213 1.00 77.51  ? 159 ILE C C   1 
ATOM   4597  O O   . ILE C  1 157 ? 165.924 160.240 174.432 1.00 83.62  ? 159 ILE C O   1 
ATOM   4598  C CB  . ILE C  1 157 ? 163.503 159.481 172.918 1.00 70.45  ? 159 ILE C CB  1 
ATOM   4599  C CG1 . ILE C  1 157 ? 162.508 158.659 172.098 1.00 65.23  ? 159 ILE C CG1 1 
ATOM   4600  C CG2 . ILE C  1 157 ? 163.299 160.961 172.644 1.00 74.35  ? 159 ILE C CG2 1 
ATOM   4601  C CD1 . ILE C  1 157 ? 161.974 157.444 172.823 1.00 66.08  ? 159 ILE C CD1 1 
ATOM   4602  N N   . GLY C  1 158 ? 166.805 160.611 172.397 1.00 69.71  ? 160 GLY C N   1 
ATOM   4603  C CA  . GLY C  1 158 ? 167.820 161.517 172.888 1.00 75.74  ? 160 GLY C CA  1 
ATOM   4604  C C   . GLY C  1 158 ? 169.040 161.483 171.993 1.00 80.50  ? 160 GLY C C   1 
ATOM   4605  O O   . GLY C  1 158 ? 169.010 160.949 170.888 1.00 83.30  ? 160 GLY C O   1 
ATOM   4606  N N   . ASN C  1 159 ? 170.123 162.063 172.501 1.00 82.62  ? 161 ASN C N   1 
ATOM   4607  C CA  . ASN C  1 159 ? 171.363 162.213 171.754 1.00 82.37  ? 161 ASN C CA  1 
ATOM   4608  C C   . ASN C  1 159 ? 172.453 161.348 172.368 1.00 85.50  ? 161 ASN C C   1 
ATOM   4609  O O   . ASN C  1 159 ? 172.636 161.350 173.590 1.00 88.62  ? 161 ASN C O   1 
ATOM   4610  C CB  . ASN C  1 159 ? 171.811 163.675 171.731 1.00 82.24  ? 161 ASN C CB  1 
ATOM   4611  C CG  . ASN C  1 159 ? 170.931 164.539 170.859 1.00 90.47  ? 161 ASN C CG  1 
ATOM   4612  O OD1 . ASN C  1 159 ? 170.266 164.048 169.948 1.00 97.71  ? 161 ASN C OD1 1 
ATOM   4613  N ND2 . ASN C  1 159 ? 170.921 165.837 171.132 1.00 88.31  ? 161 ASN C ND2 1 
ATOM   4614  N N   . LYS C  1 160 ? 173.174 160.618 171.516 1.00 84.27  ? 162 LYS C N   1 
ATOM   4615  C CA  . LYS C  1 160 ? 174.378 159.884 171.904 1.00 87.58  ? 162 LYS C CA  1 
ATOM   4616  C C   . LYS C  1 160 ? 174.101 158.932 173.070 1.00 90.75  ? 162 LYS C C   1 
ATOM   4617  O O   . LYS C  1 160 ? 174.705 159.019 174.140 1.00 94.82  ? 162 LYS C O   1 
ATOM   4618  C CB  . LYS C  1 160 ? 175.514 160.855 172.242 1.00 88.09  ? 162 LYS C CB  1 
ATOM   4619  C CG  . LYS C  1 160 ? 175.557 162.086 171.351 1.00 88.44  ? 162 LYS C CG  1 
ATOM   4620  C CD  . LYS C  1 160 ? 176.961 162.377 170.865 1.00 95.06  ? 162 LYS C CD  1 
ATOM   4621  C CE  . LYS C  1 160 ? 177.711 163.246 171.858 1.00 98.18  ? 162 LYS C CE  1 
ATOM   4622  N NZ  . LYS C  1 160 ? 178.930 163.849 171.253 1.00 105.89 ? 162 LYS C NZ  1 
ATOM   4623  N N   . ASN C  1 161 ? 173.176 158.008 172.839 1.00 86.18  ? 163 ASN C N   1 
ATOM   4624  C CA  . ASN C  1 161 ? 172.783 157.029 173.839 1.00 86.33  ? 163 ASN C CA  1 
ATOM   4625  C C   . ASN C  1 161 ? 173.198 155.640 173.376 1.00 91.79  ? 163 ASN C C   1 
ATOM   4626  O O   . ASN C  1 161 ? 173.243 155.357 172.176 1.00 99.02  ? 163 ASN C O   1 
ATOM   4627  C CB  . ASN C  1 161 ? 171.274 157.074 174.090 1.00 85.64  ? 163 ASN C CB  1 
ATOM   4628  C CG  . ASN C  1 161 ? 170.852 158.288 174.883 1.00 92.40  ? 163 ASN C CG  1 
ATOM   4629  O OD1 . ASN C  1 161 ? 171.672 158.941 175.525 1.00 96.32  ? 163 ASN C OD1 1 
ATOM   4630  N ND2 . ASN C  1 161 ? 169.566 158.606 174.832 1.00 92.00  ? 163 ASN C ND2 1 
ATOM   4631  N N   . LYS C  1 162 ? 173.514 154.775 174.337 1.00 90.75  ? 164 LYS C N   1 
ATOM   4632  C CA  . LYS C  1 162 ? 174.018 153.442 174.044 1.00 86.54  ? 164 LYS C CA  1 
ATOM   4633  C C   . LYS C  1 162 ? 173.281 152.401 174.871 1.00 90.55  ? 164 LYS C C   1 
ATOM   4634  O O   . LYS C  1 162 ? 173.008 152.614 176.055 1.00 100.71 ? 164 LYS C O   1 
ATOM   4635  C CB  . LYS C  1 162 ? 175.520 153.346 174.322 1.00 88.25  ? 164 LYS C CB  1 
ATOM   4636  C CG  . LYS C  1 162 ? 176.393 153.547 173.101 1.00 94.11  ? 164 LYS C CG  1 
ATOM   4637  C CD  . LYS C  1 162 ? 177.757 152.912 173.294 1.00 95.87  ? 164 LYS C CD  1 
ATOM   4638  C CE  . LYS C  1 162 ? 178.534 153.610 174.396 1.00 93.54  ? 164 LYS C CE  1 
ATOM   4639  N NZ  . LYS C  1 162 ? 179.935 153.902 173.991 1.00 91.17  ? 164 LYS C NZ  1 
ATOM   4640  N N   . ILE C  1 163 ? 172.962 151.275 174.238 1.00 85.55  ? 165 ILE C N   1 
ATOM   4641  C CA  . ILE C  1 163 ? 172.412 150.107 174.916 1.00 92.26  ? 165 ILE C CA  1 
ATOM   4642  C C   . ILE C  1 163 ? 173.233 148.900 174.490 1.00 102.17 ? 165 ILE C C   1 
ATOM   4643  O O   . ILE C  1 163 ? 173.278 148.565 173.301 1.00 106.39 ? 165 ILE C O   1 
ATOM   4644  C CB  . ILE C  1 163 ? 170.924 149.892 174.596 1.00 89.94  ? 165 ILE C CB  1 
ATOM   4645  C CG1 . ILE C  1 163 ? 170.102 151.101 175.044 1.00 91.49  ? 165 ILE C CG1 1 
ATOM   4646  C CG2 . ILE C  1 163 ? 170.420 148.624 175.261 1.00 92.03  ? 165 ILE C CG2 1 
ATOM   4647  C CD1 . ILE C  1 163 ? 168.614 150.842 175.111 1.00 89.08  ? 165 ILE C CD1 1 
ATOM   4648  N N   . ALA C  1 164 ? 173.878 148.250 175.454 1.00 103.33 ? 166 ALA C N   1 
ATOM   4649  C CA  . ALA C  1 164 ? 174.736 147.118 175.148 1.00 105.50 ? 166 ALA C CA  1 
ATOM   4650  C C   . ALA C  1 164 ? 173.907 145.889 174.791 1.00 111.36 ? 166 ALA C C   1 
ATOM   4651  O O   . ALA C  1 164 ? 172.726 145.778 175.133 1.00 113.76 ? 166 ALA C O   1 
ATOM   4652  C CB  . ALA C  1 164 ? 175.654 146.805 176.329 1.00 105.08 ? 166 ALA C CB  1 
ATOM   4653  N N   . SER C  1 165 ? 174.545 144.958 174.088 1.00 113.90 ? 167 SER C N   1 
ATOM   4654  C CA  . SER C  1 165 ? 173.883 143.717 173.715 1.00 115.74 ? 167 SER C CA  1 
ATOM   4655  C C   . SER C  1 165 ? 173.613 142.868 174.950 1.00 120.65 ? 167 SER C C   1 
ATOM   4656  O O   . SER C  1 165 ? 174.439 142.790 175.863 1.00 120.39 ? 167 SER C O   1 
ATOM   4657  C CB  . SER C  1 165 ? 174.736 142.938 172.716 1.00 113.72 ? 167 SER C CB  1 
ATOM   4658  O OG  . SER C  1 165 ? 173.975 141.929 172.077 1.00 116.76 ? 167 SER C OG  1 
ATOM   4659  N N   . GLY C  1 166 ? 172.448 142.227 174.973 1.00 116.43 ? 168 GLY C N   1 
ATOM   4660  C CA  . GLY C  1 166 ? 172.016 141.444 176.108 1.00 113.39 ? 168 GLY C CA  1 
ATOM   4661  C C   . GLY C  1 166 ? 171.206 142.209 177.132 1.00 113.69 ? 168 GLY C C   1 
ATOM   4662  O O   . GLY C  1 166 ? 170.657 141.590 178.051 1.00 114.10 ? 168 GLY C O   1 
ATOM   4663  N N   . SER C  1 167 ? 171.116 143.530 177.002 1.00 111.54 ? 169 SER C N   1 
ATOM   4664  C CA  . SER C  1 167 ? 170.297 144.360 177.877 1.00 104.97 ? 169 SER C CA  1 
ATOM   4665  C C   . SER C  1 167 ? 169.010 144.691 177.133 1.00 106.53 ? 169 SER C C   1 
ATOM   4666  O O   . SER C  1 167 ? 169.028 145.446 176.157 1.00 111.77 ? 169 SER C O   1 
ATOM   4667  C CB  . SER C  1 167 ? 171.046 145.627 178.282 1.00 104.24 ? 169 SER C CB  1 
ATOM   4668  O OG  . SER C  1 167 ? 172.203 145.314 179.037 1.00 109.95 ? 169 SER C OG  1 
ATOM   4669  N N   . ASP C  1 168 ? 167.897 144.134 177.596 1.00 104.28 ? 170 ASP C N   1 
ATOM   4670  C CA  . ASP C  1 168 ? 166.631 144.206 176.884 1.00 105.74 ? 170 ASP C CA  1 
ATOM   4671  C C   . ASP C  1 168 ? 165.575 144.894 177.740 1.00 104.81 ? 170 ASP C C   1 
ATOM   4672  O O   . ASP C  1 168 ? 165.715 145.028 178.958 1.00 104.83 ? 170 ASP C O   1 
ATOM   4673  C CB  . ASP C  1 168 ? 166.157 142.807 176.476 1.00 109.75 ? 170 ASP C CB  1 
ATOM   4674  C CG  . ASP C  1 168 ? 167.240 142.005 175.785 1.00 115.75 ? 170 ASP C CG  1 
ATOM   4675  O OD1 . ASP C  1 168 ? 167.916 142.562 174.895 1.00 115.11 ? 170 ASP C OD1 1 
ATOM   4676  O OD2 . ASP C  1 168 ? 167.417 140.819 176.134 1.00 117.93 ? 170 ASP C OD2 1 
ATOM   4677  N N   . ASP C  1 169 ? 164.504 145.325 177.073 1.00 104.24 ? 171 ASP C N   1 
ATOM   4678  C CA  . ASP C  1 169 ? 163.377 146.006 177.712 1.00 101.46 ? 171 ASP C CA  1 
ATOM   4679  C C   . ASP C  1 169 ? 163.837 147.235 178.492 1.00 99.28  ? 171 ASP C C   1 
ATOM   4680  O O   . ASP C  1 169 ? 163.455 147.455 179.642 1.00 104.71 ? 171 ASP C O   1 
ATOM   4681  C CB  . ASP C  1 169 ? 162.593 145.050 178.613 1.00 110.19 ? 171 ASP C CB  1 
ATOM   4682  C CG  . ASP C  1 169 ? 162.269 143.736 177.931 1.00 118.53 ? 171 ASP C CG  1 
ATOM   4683  O OD1 . ASP C  1 169 ? 163.209 142.993 177.585 1.00 118.76 ? 171 ASP C OD1 1 
ATOM   4684  O OD2 . ASP C  1 169 ? 161.071 143.445 177.741 1.00 120.66 ? 171 ASP C OD2 1 
ATOM   4685  N N   . ASN C  1 170 ? 164.665 148.051 177.847 1.00 92.55  ? 172 ASN C N   1 
ATOM   4686  C CA  . ASN C  1 170 ? 165.169 149.279 178.439 1.00 87.96  ? 172 ASN C CA  1 
ATOM   4687  C C   . ASN C  1 170 ? 164.635 150.476 177.666 1.00 86.74  ? 172 ASN C C   1 
ATOM   4688  O O   . ASN C  1 170 ? 164.450 150.417 176.449 1.00 91.75  ? 172 ASN C O   1 
ATOM   4689  C CB  . ASN C  1 170 ? 166.699 149.306 178.447 1.00 87.42  ? 172 ASN C CB  1 
ATOM   4690  C CG  . ASN C  1 170 ? 167.294 148.195 179.282 1.00 99.82  ? 172 ASN C CG  1 
ATOM   4691  O OD1 . ASN C  1 170 ? 166.824 147.910 180.382 1.00 101.84 ? 172 ASN C OD1 1 
ATOM   4692  N ND2 . ASN C  1 170 ? 168.332 147.555 178.761 1.00 107.11 ? 172 ASN C ND2 1 
ATOM   4693  N N   . PHE C  1 171 ? 164.380 151.565 178.381 1.00 80.94  ? 173 PHE C N   1 
ATOM   4694  C CA  . PHE C  1 171 ? 163.875 152.782 177.766 1.00 74.77  ? 173 PHE C CA  1 
ATOM   4695  C C   . PHE C  1 171 ? 164.686 153.972 178.246 1.00 76.51  ? 173 PHE C C   1 
ATOM   4696  O O   . PHE C  1 171 ? 164.955 154.112 179.442 1.00 80.02  ? 173 PHE C O   1 
ATOM   4697  C CB  . PHE C  1 171 ? 162.390 152.978 178.072 1.00 73.60  ? 173 PHE C CB  1 
ATOM   4698  C CG  . PHE C  1 171 ? 161.501 152.034 177.322 1.00 81.85  ? 173 PHE C CG  1 
ATOM   4699  C CD1 . PHE C  1 171 ? 161.217 150.779 177.829 1.00 87.89  ? 173 PHE C CD1 1 
ATOM   4700  C CD2 . PHE C  1 171 ? 160.970 152.392 176.097 1.00 85.63  ? 173 PHE C CD2 1 
ATOM   4701  C CE1 . PHE C  1 171 ? 160.408 149.905 177.133 1.00 94.10  ? 173 PHE C CE1 1 
ATOM   4702  C CE2 . PHE C  1 171 ? 160.160 151.522 175.398 1.00 90.84  ? 173 PHE C CE2 1 
ATOM   4703  C CZ  . PHE C  1 171 ? 159.881 150.277 175.916 1.00 94.09  ? 173 PHE C CZ  1 
ATOM   4704  N N   . ILE C  1 172 ? 165.078 154.825 177.305 1.00 74.70  ? 174 ILE C N   1 
ATOM   4705  C CA  . ILE C  1 172 ? 165.933 155.970 177.583 1.00 75.73  ? 174 ILE C CA  1 
ATOM   4706  C C   . ILE C  1 172 ? 165.236 157.229 177.094 1.00 80.23  ? 174 ILE C C   1 
ATOM   4707  O O   . ILE C  1 172 ? 164.783 157.288 175.946 1.00 84.06  ? 174 ILE C O   1 
ATOM   4708  C CB  . ILE C  1 172 ? 167.313 155.830 176.916 1.00 74.34  ? 174 ILE C CB  1 
ATOM   4709  C CG1 . ILE C  1 172 ? 167.934 154.473 177.250 1.00 76.88  ? 174 ILE C CG1 1 
ATOM   4710  C CG2 . ILE C  1 172 ? 168.222 156.958 177.355 1.00 76.71  ? 174 ILE C CG2 1 
ATOM   4711  C CD1 . ILE C  1 172 ? 169.399 154.368 176.898 1.00 86.66  ? 174 ILE C CD1 1 
ATOM   4712  N N   . LEU C  1 173 ? 165.152 158.233 177.965 1.00 75.72  ? 175 LEU C N   1 
ATOM   4713  C CA  . LEU C  1 173 ? 164.659 159.565 177.615 1.00 75.45  ? 175 LEU C CA  1 
ATOM   4714  C C   . LEU C  1 173 ? 165.698 160.556 178.132 1.00 80.35  ? 175 LEU C C   1 
ATOM   4715  O O   . LEU C  1 173 ? 165.564 161.104 179.228 1.00 85.87  ? 175 LEU C O   1 
ATOM   4716  C CB  . LEU C  1 173 ? 163.274 159.819 178.203 1.00 77.76  ? 175 LEU C CB  1 
ATOM   4717  C CG  . LEU C  1 173 ? 162.523 161.048 177.690 1.00 76.76  ? 175 LEU C CG  1 
ATOM   4718  C CD1 . LEU C  1 173 ? 162.484 161.055 176.177 1.00 74.84  ? 175 LEU C CD1 1 
ATOM   4719  C CD2 . LEU C  1 173 ? 161.116 161.094 178.260 1.00 78.88  ? 175 LEU C CD2 1 
ATOM   4720  N N   . GLY C  1 174 ? 166.733 160.783 177.336 1.00 78.22  ? 176 GLY C N   1 
ATOM   4721  C CA  . GLY C  1 174 ? 167.823 161.638 177.757 1.00 84.70  ? 176 GLY C CA  1 
ATOM   4722  C C   . GLY C  1 174 ? 168.995 161.511 176.811 1.00 88.83  ? 176 GLY C C   1 
ATOM   4723  O O   . GLY C  1 174 ? 168.940 160.801 175.803 1.00 92.89  ? 176 GLY C O   1 
ATOM   4724  N N   . ASN C  1 175 ? 170.065 162.216 177.161 1.00 85.68  ? 177 ASN C N   1 
ATOM   4725  C CA  . ASN C  1 175 ? 171.284 162.233 176.370 1.00 83.85  ? 177 ASN C CA  1 
ATOM   4726  C C   . ASN C  1 175 ? 172.433 161.616 177.155 1.00 89.53  ? 177 ASN C C   1 
ATOM   4727  O O   . ASN C  1 175 ? 172.447 161.636 178.389 1.00 93.58  ? 177 ASN C O   1 
ATOM   4728  C CB  . ASN C  1 175 ? 171.661 163.658 175.958 1.00 83.13  ? 177 ASN C CB  1 
ATOM   4729  C CG  . ASN C  1 175 ? 170.494 164.428 175.386 1.00 85.05  ? 177 ASN C CG  1 
ATOM   4730  O OD1 . ASN C  1 175 ? 169.837 163.977 174.449 1.00 91.17  ? 177 ASN C OD1 1 
ATOM   4731  N ND2 . ASN C  1 175 ? 170.228 165.600 175.947 1.00 86.89  ? 177 ASN C ND2 1 
ATOM   4732  N N   . ASN C  1 176 ? 173.397 161.065 176.416 1.00 89.68  ? 178 ASN C N   1 
ATOM   4733  C CA  . ASN C  1 176 ? 174.632 160.527 176.988 1.00 92.55  ? 178 ASN C CA  1 
ATOM   4734  C C   . ASN C  1 176 ? 174.347 159.446 178.026 1.00 93.71  ? 178 ASN C C   1 
ATOM   4735  O O   . ASN C  1 176 ? 175.021 159.352 179.053 1.00 98.56  ? 178 ASN C O   1 
ATOM   4736  C CB  . ASN C  1 176 ? 175.489 161.641 177.589 1.00 92.52  ? 178 ASN C CB  1 
ATOM   4737  C CG  . ASN C  1 176 ? 175.772 162.750 176.601 1.00 95.39  ? 178 ASN C CG  1 
ATOM   4738  O OD1 . ASN C  1 176 ? 176.394 162.529 175.564 1.00 100.48 ? 178 ASN C OD1 1 
ATOM   4739  N ND2 . ASN C  1 176 ? 175.315 163.955 176.918 1.00 94.83  ? 178 ASN C ND2 1 
ATOM   4740  N N   . VAL C  1 177 ? 173.341 158.621 177.760 1.00 86.42  ? 179 VAL C N   1 
ATOM   4741  C CA  . VAL C  1 177 ? 172.974 157.523 178.644 1.00 87.16  ? 179 VAL C CA  1 
ATOM   4742  C C   . VAL C  1 177 ? 173.478 156.229 178.025 1.00 93.18  ? 179 VAL C C   1 
ATOM   4743  O O   . VAL C  1 177 ? 172.998 155.809 176.965 1.00 94.06  ? 179 VAL C O   1 
ATOM   4744  C CB  . VAL C  1 177 ? 171.458 157.469 178.877 1.00 84.78  ? 179 VAL C CB  1 
ATOM   4745  C CG1 . VAL C  1 177 ? 171.099 156.256 179.713 1.00 86.61  ? 179 VAL C CG1 1 
ATOM   4746  C CG2 . VAL C  1 177 ? 170.979 158.745 179.544 1.00 88.42  ? 179 VAL C CG2 1 
ATOM   4747  N N   . HIS C  1 178 ? 174.442 155.595 178.683 1.00 95.19  ? 180 HIS C N   1 
ATOM   4748  C CA  . HIS C  1 178 ? 175.003 154.329 178.236 1.00 91.37  ? 180 HIS C CA  1 
ATOM   4749  C C   . HIS C  1 178 ? 174.575 153.229 179.195 1.00 91.64  ? 180 HIS C C   1 
ATOM   4750  O O   . HIS C  1 178 ? 174.783 153.342 180.407 1.00 98.82  ? 180 HIS C O   1 
ATOM   4751  C CB  . HIS C  1 178 ? 176.529 154.400 178.158 1.00 94.68  ? 180 HIS C CB  1 
ATOM   4752  C CG  . HIS C  1 178 ? 177.044 155.644 177.505 1.00 99.71  ? 180 HIS C CG  1 
ATOM   4753  N ND1 . HIS C  1 178 ? 176.852 155.918 176.169 1.00 98.46  ? 180 HIS C ND1 1 
ATOM   4754  C CD2 . HIS C  1 178 ? 177.747 156.687 178.005 1.00 100.62 ? 180 HIS C CD2 1 
ATOM   4755  C CE1 . HIS C  1 178 ? 177.412 157.077 175.873 1.00 97.17  ? 180 HIS C CE1 1 
ATOM   4756  N NE2 . HIS C  1 178 ? 177.962 157.564 176.970 1.00 101.48 ? 180 HIS C NE2 1 
ATOM   4757  N N   . ILE C  1 179 ? 173.983 152.172 178.651 1.00 90.94  ? 181 ILE C N   1 
ATOM   4758  C CA  . ILE C  1 179 ? 173.513 151.037 179.435 1.00 95.23  ? 181 ILE C CA  1 
ATOM   4759  C C   . ILE C  1 179 ? 174.430 149.859 179.143 1.00 100.59 ? 181 ILE C C   1 
ATOM   4760  O O   . ILE C  1 179 ? 174.590 149.460 177.984 1.00 100.75 ? 181 ILE C O   1 
ATOM   4761  C CB  . ILE C  1 179 ? 172.050 150.693 179.116 1.00 88.72  ? 181 ILE C CB  1 
ATOM   4762  C CG1 . ILE C  1 179 ? 171.147 151.888 179.423 1.00 86.58  ? 181 ILE C CG1 1 
ATOM   4763  C CG2 . ILE C  1 179 ? 171.609 149.471 179.903 1.00 94.44  ? 181 ILE C CG2 1 
ATOM   4764  C CD1 . ILE C  1 179 ? 169.672 151.559 179.426 1.00 89.42  ? 181 ILE C CD1 1 
ATOM   4765  N N   . GLY C  1 180 ? 175.031 149.306 180.191 1.00 101.13 ? 182 GLY C N   1 
ATOM   4766  C CA  . GLY C  1 180 ? 175.947 148.196 180.050 1.00 103.64 ? 182 GLY C CA  1 
ATOM   4767  C C   . GLY C  1 180 ? 175.221 146.878 179.884 1.00 112.09 ? 182 GLY C C   1 
ATOM   4768  O O   . GLY C  1 180 ? 174.012 146.822 179.646 1.00 118.98 ? 182 GLY C O   1 
ATOM   4769  N N   . GLY C  1 181 ? 175.982 145.796 180.012 1.00 111.37 ? 183 GLY C N   1 
ATOM   4770  C CA  . GLY C  1 181 ? 175.431 144.467 179.862 1.00 112.24 ? 183 GLY C CA  1 
ATOM   4771  C C   . GLY C  1 181 ? 174.687 143.999 181.100 1.00 116.07 ? 183 GLY C C   1 
ATOM   4772  O O   . GLY C  1 181 ? 174.996 144.392 182.221 1.00 113.09 ? 183 GLY C O   1 
ATOM   4773  N N   . GLY C  1 182 ? 173.696 143.144 180.877 1.00 115.28 ? 184 GLY C N   1 
ATOM   4774  C CA  . GLY C  1 182 ? 172.922 142.577 181.968 1.00 111.97 ? 184 GLY C CA  1 
ATOM   4775  C C   . GLY C  1 182 ? 172.101 143.576 182.754 1.00 111.08 ? 184 GLY C C   1 
ATOM   4776  O O   . GLY C  1 182 ? 172.071 143.510 183.989 1.00 112.68 ? 184 GLY C O   1 
ATOM   4777  N N   . ILE C  1 183 ? 171.434 144.503 182.071 1.00 108.50 ? 185 ILE C N   1 
ATOM   4778  C CA  . ILE C  1 183 ? 170.572 145.495 182.708 1.00 104.82 ? 185 ILE C CA  1 
ATOM   4779  C C   . ILE C  1 183 ? 169.248 145.468 181.955 1.00 106.24 ? 185 ILE C C   1 
ATOM   4780  O O   . ILE C  1 183 ? 169.140 146.019 180.854 1.00 110.48 ? 185 ILE C O   1 
ATOM   4781  C CB  . ILE C  1 183 ? 171.185 146.898 182.701 1.00 103.58 ? 185 ILE C CB  1 
ATOM   4782  C CG1 . ILE C  1 183 ? 172.460 146.925 183.542 1.00 105.58 ? 185 ILE C CG1 1 
ATOM   4783  C CG2 . ILE C  1 183 ? 170.191 147.914 183.234 1.00 104.60 ? 185 ILE C CG2 1 
ATOM   4784  C CD1 . ILE C  1 183 ? 173.209 148.233 183.466 1.00 106.33 ? 185 ILE C CD1 1 
ATOM   4785  N N   . ASN C  1 184 ? 168.240 144.827 182.538 1.00 105.26 ? 186 ASN C N   1 
ATOM   4786  C CA  . ASN C  1 184 ? 166.934 144.680 181.916 1.00 102.15 ? 186 ASN C CA  1 
ATOM   4787  C C   . ASN C  1 184 ? 165.879 145.436 182.712 1.00 100.92 ? 186 ASN C C   1 
ATOM   4788  O O   . ASN C  1 184 ? 166.044 145.688 183.908 1.00 100.98 ? 186 ASN C O   1 
ATOM   4789  C CB  . ASN C  1 184 ? 166.529 143.206 181.809 1.00 103.97 ? 186 ASN C CB  1 
ATOM   4790  C CG  . ASN C  1 184 ? 167.607 142.342 181.184 1.00 110.82 ? 186 ASN C CG  1 
ATOM   4791  O OD1 . ASN C  1 184 ? 168.773 142.725 181.122 1.00 113.06 ? 186 ASN C OD1 1 
ATOM   4792  N ND2 . ASN C  1 184 ? 167.217 141.164 180.716 1.00 116.46 ? 186 ASN C ND2 1 
ATOM   4793  N N   . ASN C  1 185 ? 164.791 145.793 182.029 1.00 99.78  ? 187 ASN C N   1 
ATOM   4794  C CA  . ASN C  1 185 ? 163.624 146.416 182.656 1.00 97.14  ? 187 ASN C CA  1 
ATOM   4795  C C   . ASN C  1 185 ? 164.003 147.701 183.391 1.00 98.54  ? 187 ASN C C   1 
ATOM   4796  O O   . ASN C  1 185 ? 163.693 147.884 184.568 1.00 102.55 ? 187 ASN C O   1 
ATOM   4797  C CB  . ASN C  1 185 ? 162.927 145.436 183.602 1.00 97.45  ? 187 ASN C CB  1 
ATOM   4798  C CG  . ASN C  1 185 ? 161.970 144.515 182.883 1.00 106.76 ? 187 ASN C CG  1 
ATOM   4799  O OD1 . ASN C  1 185 ? 160.763 144.551 183.114 1.00 109.39 ? 187 ASN C OD1 1 
ATOM   4800  N ND2 . ASN C  1 185 ? 162.505 143.678 182.004 1.00 111.78 ? 187 ASN C ND2 1 
ATOM   4801  N N   . SER C  1 186 ? 164.667 148.607 182.680 1.00 92.85  ? 188 SER C N   1 
ATOM   4802  C CA  . SER C  1 186 ? 165.155 149.839 183.278 1.00 88.84  ? 188 SER C CA  1 
ATOM   4803  C C   . SER C  1 186 ? 164.735 151.033 182.437 1.00 86.53  ? 188 SER C C   1 
ATOM   4804  O O   . SER C  1 186 ? 164.590 150.935 181.216 1.00 91.79  ? 188 SER C O   1 
ATOM   4805  C CB  . SER C  1 186 ? 166.677 149.820 183.428 1.00 94.84  ? 188 SER C CB  1 
ATOM   4806  O OG  . SER C  1 186 ? 167.073 148.927 184.453 1.00 102.55 ? 188 SER C OG  1 
ATOM   4807  N N   . VAL C  1 187 ? 164.533 152.165 183.108 1.00 79.23  ? 189 VAL C N   1 
ATOM   4808  C CA  . VAL C  1 187 ? 164.163 153.418 182.464 1.00 75.22  ? 189 VAL C CA  1 
ATOM   4809  C C   . VAL C  1 187 ? 165.136 154.495 182.917 1.00 79.59  ? 189 VAL C C   1 
ATOM   4810  O O   . VAL C  1 187 ? 165.405 154.630 184.115 1.00 84.48  ? 189 VAL C O   1 
ATOM   4811  C CB  . VAL C  1 187 ? 162.716 153.833 182.792 1.00 69.94  ? 189 VAL C CB  1 
ATOM   4812  C CG1 . VAL C  1 187 ? 162.270 154.958 181.877 1.00 72.95  ? 189 VAL C CG1 1 
ATOM   4813  C CG2 . VAL C  1 187 ? 161.783 152.647 182.672 1.00 68.00  ? 189 VAL C CG2 1 
ATOM   4814  N N   . ALA C  1 188 ? 165.663 155.257 181.963 1.00 76.72  ? 190 ALA C N   1 
ATOM   4815  C CA  . ALA C  1 188 ? 166.556 156.372 182.243 1.00 76.74  ? 190 ALA C CA  1 
ATOM   4816  C C   . ALA C  1 188 ? 165.912 157.658 181.750 1.00 81.38  ? 190 ALA C C   1 
ATOM   4817  O O   . ALA C  1 188 ? 165.484 157.737 180.594 1.00 84.70  ? 190 ALA C O   1 
ATOM   4818  C CB  . ALA C  1 188 ? 167.916 156.174 181.577 1.00 76.44  ? 190 ALA C CB  1 
ATOM   4819  N N   . LEU C  1 189 ? 165.848 158.659 182.623 1.00 78.10  ? 191 LEU C N   1 
ATOM   4820  C CA  . LEU C  1 189 ? 165.211 159.931 182.315 1.00 77.24  ? 191 LEU C CA  1 
ATOM   4821  C C   . LEU C  1 189 ? 166.204 161.064 182.519 1.00 83.62  ? 191 LEU C C   1 
ATOM   4822  O O   . LEU C  1 189 ? 166.890 161.116 183.544 1.00 89.93  ? 191 LEU C O   1 
ATOM   4823  C CB  . LEU C  1 189 ? 163.978 160.153 183.193 1.00 77.19  ? 191 LEU C CB  1 
ATOM   4824  C CG  . LEU C  1 189 ? 162.854 159.122 183.084 1.00 71.69  ? 191 LEU C CG  1 
ATOM   4825  C CD1 . LEU C  1 189 ? 161.783 159.397 184.123 1.00 73.74  ? 191 LEU C CD1 1 
ATOM   4826  C CD2 . LEU C  1 189 ? 162.259 159.124 181.689 1.00 72.34  ? 191 LEU C CD2 1 
ATOM   4827  N N   . GLY C  1 190 ? 166.276 161.966 181.547 1.00 81.81  ? 192 GLY C N   1 
ATOM   4828  C CA  . GLY C  1 190 ? 167.006 163.206 181.697 1.00 86.67  ? 192 GLY C CA  1 
ATOM   4829  C C   . GLY C  1 190 ? 168.399 163.155 181.093 1.00 89.58  ? 192 GLY C C   1 
ATOM   4830  O O   . GLY C  1 190 ? 168.941 162.099 180.758 1.00 88.76  ? 192 GLY C O   1 
ATOM   4831  N N   . ASN C  1 191 ? 168.974 164.347 180.961 1.00 91.00  ? 193 ASN C N   1 
ATOM   4832  C CA  . ASN C  1 191 ? 170.329 164.495 180.451 1.00 91.85  ? 193 ASN C CA  1 
ATOM   4833  C C   . ASN C  1 191 ? 171.338 163.844 181.388 1.00 95.58  ? 193 ASN C C   1 
ATOM   4834  O O   . ASN C  1 191 ? 171.266 163.999 182.610 1.00 98.28  ? 193 ASN C O   1 
ATOM   4835  C CB  . ASN C  1 191 ? 170.660 165.977 180.281 1.00 92.96  ? 193 ASN C CB  1 
ATOM   4836  C CG  . ASN C  1 191 ? 171.895 166.208 179.441 1.00 98.90  ? 193 ASN C CG  1 
ATOM   4837  O OD1 . ASN C  1 191 ? 172.034 165.650 178.356 1.00 101.56 ? 193 ASN C OD1 1 
ATOM   4838  N ND2 . ASN C  1 191 ? 172.803 167.036 179.942 1.00 96.45  ? 193 ASN C ND2 1 
ATOM   4839  N N   . ASN C  1 192 ? 172.284 163.108 180.802 1.00 91.03  ? 194 ASN C N   1 
ATOM   4840  C CA  . ASN C  1 192 ? 173.413 162.528 181.530 1.00 91.83  ? 194 ASN C CA  1 
ATOM   4841  C C   . ASN C  1 192 ? 172.963 161.596 182.651 1.00 95.68  ? 194 ASN C C   1 
ATOM   4842  O O   . ASN C  1 192 ? 173.613 161.508 183.695 1.00 97.58  ? 194 ASN C O   1 
ATOM   4843  C CB  . ASN C  1 192 ? 174.330 163.620 182.087 1.00 93.75  ? 194 ASN C CB  1 
ATOM   4844  C CG  . ASN C  1 192 ? 175.084 164.355 181.001 1.00 99.12  ? 194 ASN C CG  1 
ATOM   4845  O OD1 . ASN C  1 192 ? 174.985 164.015 179.823 1.00 102.34 ? 194 ASN C OD1 1 
ATOM   4846  N ND2 . ASN C  1 192 ? 175.839 165.373 181.391 1.00 100.93 ? 194 ASN C ND2 1 
ATOM   4847  N N   . SER C  1 193 ? 171.851 160.895 182.453 1.00 96.29  ? 195 SER C N   1 
ATOM   4848  C CA  . SER C  1 193 ? 171.396 159.936 183.445 1.00 96.32  ? 195 SER C CA  1 
ATOM   4849  C C   . SER C  1 193 ? 172.261 158.680 183.402 1.00 99.90  ? 195 SER C C   1 
ATOM   4850  O O   . SER C  1 193 ? 173.009 158.439 182.452 1.00 102.86 ? 195 SER C O   1 
ATOM   4851  C CB  . SER C  1 193 ? 169.930 159.578 183.217 1.00 91.97  ? 195 SER C CB  1 
ATOM   4852  O OG  . SER C  1 193 ? 169.084 160.643 183.612 1.00 92.11  ? 195 SER C OG  1 
ATOM   4853  N N   . THR C  1 194 ? 172.149 157.871 184.454 1.00 99.02  ? 196 THR C N   1 
ATOM   4854  C CA  . THR C  1 194 ? 172.977 156.681 184.598 1.00 106.07 ? 196 THR C CA  1 
ATOM   4855  C C   . THR C  1 194 ? 172.139 155.535 185.139 1.00 106.58 ? 196 THR C C   1 
ATOM   4856  O O   . THR C  1 194 ? 171.433 155.699 186.137 1.00 112.26 ? 196 THR C O   1 
ATOM   4857  C CB  . THR C  1 194 ? 174.166 156.948 185.530 1.00 110.30 ? 196 THR C CB  1 
ATOM   4858  O OG1 . THR C  1 194 ? 175.072 157.862 184.901 1.00 111.43 ? 196 THR C OG1 1 
ATOM   4859  C CG2 . THR C  1 194 ? 174.900 155.655 185.849 1.00 110.08 ? 196 THR C CG2 1 
ATOM   4860  N N   . VAL C  1 195 ? 172.229 154.379 184.486 1.00 103.98 ? 197 VAL C N   1 
ATOM   4861  C CA  . VAL C  1 195 ? 171.551 153.162 184.917 1.00 104.86 ? 197 VAL C CA  1 
ATOM   4862  C C   . VAL C  1 195 ? 172.608 152.160 185.353 1.00 107.61 ? 197 VAL C C   1 
ATOM   4863  O O   . VAL C  1 195 ? 173.566 151.900 184.615 1.00 108.43 ? 197 VAL C O   1 
ATOM   4864  C CB  . VAL C  1 195 ? 170.673 152.575 183.800 1.00 97.36  ? 197 VAL C CB  1 
ATOM   4865  C CG1 . VAL C  1 195 ? 169.600 151.682 184.393 1.00 94.16  ? 197 VAL C CG1 1 
ATOM   4866  C CG2 . VAL C  1 195 ? 170.056 153.683 182.975 1.00 101.05 ? 197 VAL C CG2 1 
ATOM   4867  N N   . SER C  1 196 ? 172.434 151.597 186.548 1.00 107.32 ? 198 SER C N   1 
ATOM   4868  C CA  . SER C  1 196 ? 173.411 150.675 187.103 1.00 114.57 ? 198 SER C CA  1 
ATOM   4869  C C   . SER C  1 196 ? 172.820 149.354 187.573 1.00 116.56 ? 198 SER C C   1 
ATOM   4870  O O   . SER C  1 196 ? 173.570 148.505 188.066 1.00 121.05 ? 198 SER C O   1 
ATOM   4871  C CB  . SER C  1 196 ? 174.158 151.331 188.274 1.00 118.85 ? 198 SER C CB  1 
ATOM   4872  O OG  . SER C  1 196 ? 174.801 150.356 189.074 1.00 132.41 ? 198 SER C OG  1 
ATOM   4873  N N   . ALA C  1 197 ? 171.512 149.151 187.439 1.00 112.04 ? 199 ALA C N   1 
ATOM   4874  C CA  . ALA C  1 197 ? 170.888 147.920 187.903 1.00 108.16 ? 199 ALA C CA  1 
ATOM   4875  C C   . ALA C  1 197 ? 169.602 147.694 187.123 1.00 106.46 ? 199 ALA C C   1 
ATOM   4876  O O   . ALA C  1 197 ? 169.129 148.569 186.395 1.00 110.08 ? 199 ALA C O   1 
ATOM   4877  C CB  . ALA C  1 197 ? 170.616 147.965 189.409 1.00 105.44 ? 199 ALA C CB  1 
ATOM   4878  N N   . SER C  1 198 ? 169.045 146.500 187.286 1.00 101.41 ? 200 SER C N   1 
ATOM   4879  C CA  . SER C  1 198 ? 167.805 146.123 186.629 1.00 102.00 ? 200 SER C CA  1 
ATOM   4880  C C   . SER C  1 198 ? 166.603 146.501 187.489 1.00 103.92 ? 200 SER C C   1 
ATOM   4881  O O   . SER C  1 198 ? 166.710 146.684 188.704 1.00 106.86 ? 200 SER C O   1 
ATOM   4882  C CB  . SER C  1 198 ? 167.789 144.622 186.337 1.00 103.95 ? 200 SER C CB  1 
ATOM   4883  O OG  . SER C  1 198 ? 168.632 144.305 185.245 1.00 109.01 ? 200 SER C OG  1 
ATOM   4884  N N   . ASN C  1 199 ? 165.447 146.612 186.832 1.00 100.24 ? 201 ASN C N   1 
ATOM   4885  C CA  . ASN C  1 199 ? 164.180 146.929 187.495 1.00 97.08  ? 201 ASN C CA  1 
ATOM   4886  C C   . ASN C  1 199 ? 164.272 148.224 188.297 1.00 99.67  ? 201 ASN C C   1 
ATOM   4887  O O   . ASN C  1 199 ? 163.810 148.304 189.437 1.00 105.16 ? 201 ASN C O   1 
ATOM   4888  C CB  . ASN C  1 199 ? 163.717 145.771 188.380 1.00 97.14  ? 201 ASN C CB  1 
ATOM   4889  C CG  . ASN C  1 199 ? 163.979 144.419 187.752 1.00 103.42 ? 201 ASN C CG  1 
ATOM   4890  O OD1 . ASN C  1 199 ? 163.481 144.119 186.668 1.00 106.93 ? 201 ASN C OD1 1 
ATOM   4891  N ND2 . ASN C  1 199 ? 164.766 143.594 188.431 1.00 107.25 ? 201 ASN C ND2 1 
ATOM   4892  N N   . THR C  1 200 ? 164.878 149.248 187.701 1.00 95.99  ? 202 THR C N   1 
ATOM   4893  C CA  . THR C  1 200 ? 165.014 150.545 188.345 1.00 95.88  ? 202 THR C CA  1 
ATOM   4894  C C   . THR C  1 200 ? 164.679 151.646 187.351 1.00 89.30  ? 202 THR C C   1 
ATOM   4895  O O   . THR C  1 200 ? 164.757 151.460 186.134 1.00 88.87  ? 202 THR C O   1 
ATOM   4896  C CB  . THR C  1 200 ? 166.430 150.772 188.897 1.00 100.65 ? 202 THR C CB  1 
ATOM   4897  O OG1 . THR C  1 200 ? 167.387 150.614 187.842 1.00 105.51 ? 202 THR C OG1 1 
ATOM   4898  C CG2 . THR C  1 200 ? 166.741 149.789 190.014 1.00 101.70 ? 202 THR C CG2 1 
ATOM   4899  N N   . VAL C  1 201 ? 164.297 152.800 187.889 1.00 83.22  ? 203 VAL C N   1 
ATOM   4900  C CA  . VAL C  1 201 ? 164.097 154.016 187.111 1.00 77.52  ? 203 VAL C CA  1 
ATOM   4901  C C   . VAL C  1 201 ? 165.059 155.061 187.653 1.00 84.68  ? 203 VAL C C   1 
ATOM   4902  O O   . VAL C  1 201 ? 165.016 155.393 188.843 1.00 92.99  ? 203 VAL C O   1 
ATOM   4903  C CB  . VAL C  1 201 ? 162.646 154.513 187.181 1.00 71.64  ? 203 VAL C CB  1 
ATOM   4904  C CG1 . VAL C  1 201 ? 162.563 155.964 186.746 1.00 73.23  ? 203 VAL C CG1 1 
ATOM   4905  C CG2 . VAL C  1 201 ? 161.760 153.649 186.311 1.00 75.25  ? 203 VAL C CG2 1 
ATOM   4906  N N   . SER C  1 202 ? 165.925 155.574 186.788 1.00 80.49  ? 204 SER C N   1 
ATOM   4907  C CA  . SER C  1 202 ? 166.968 156.504 187.193 1.00 79.48  ? 204 SER C CA  1 
ATOM   4908  C C   . SER C  1 202 ? 166.652 157.896 186.669 1.00 85.52  ? 204 SER C C   1 
ATOM   4909  O O   . SER C  1 202 ? 166.344 158.064 185.485 1.00 87.25  ? 204 SER C O   1 
ATOM   4910  C CB  . SER C  1 202 ? 168.333 156.044 186.683 1.00 87.23  ? 204 SER C CB  1 
ATOM   4911  O OG  . SER C  1 202 ? 169.347 156.962 187.049 1.00 95.32  ? 204 SER C OG  1 
ATOM   4912  N N   . VAL C  1 203 ? 166.732 158.888 187.552 1.00 86.15  ? 205 VAL C N   1 
ATOM   4913  C CA  . VAL C  1 203 ? 166.496 160.278 187.195 1.00 82.32  ? 205 VAL C CA  1 
ATOM   4914  C C   . VAL C  1 203 ? 167.771 161.108 187.326 1.00 88.86  ? 205 VAL C C   1 
ATOM   4915  O O   . VAL C  1 203 ? 167.709 162.313 187.520 1.00 94.01  ? 205 VAL C O   1 
ATOM   4916  C CB  . VAL C  1 203 ? 165.353 160.880 188.035 1.00 76.85  ? 205 VAL C CB  1 
ATOM   4917  C CG1 . VAL C  1 203 ? 164.014 160.347 187.562 1.00 72.56  ? 205 VAL C CG1 1 
ATOM   4918  C CG2 . VAL C  1 203 ? 165.562 160.576 189.507 1.00 79.86  ? 205 VAL C CG2 1 
ATOM   4919  N N   . GLY C  1 204 ? 168.926 160.468 187.223 1.00 87.50  ? 206 GLY C N   1 
ATOM   4920  C CA  . GLY C  1 204 ? 170.185 161.172 187.336 1.00 91.17  ? 206 GLY C CA  1 
ATOM   4921  C C   . GLY C  1 204 ? 171.324 160.193 187.542 1.00 99.29  ? 206 GLY C C   1 
ATOM   4922  O O   . GLY C  1 204 ? 171.142 158.978 187.500 1.00 99.94  ? 206 GLY C O   1 
ATOM   4923  N N   . SER C  1 205 ? 172.504 160.758 187.764 1.00 104.20 ? 207 SER C N   1 
ATOM   4924  C CA  . SER C  1 205 ? 173.720 159.997 188.006 1.00 102.39 ? 207 SER C CA  1 
ATOM   4925  C C   . SER C  1 205 ? 174.209 160.256 189.427 1.00 106.48 ? 207 SER C C   1 
ATOM   4926  O O   . SER C  1 205 ? 173.573 160.967 190.208 1.00 110.57 ? 207 SER C O   1 
ATOM   4927  C CB  . SER C  1 205 ? 174.799 160.356 186.982 1.00 101.49 ? 207 SER C CB  1 
ATOM   4928  O OG  . SER C  1 205 ? 174.912 161.760 186.836 1.00 108.27 ? 207 SER C OG  1 
ATOM   4929  N N   . SER C  1 206 ? 175.357 159.663 189.759 1.00 109.40 ? 208 SER C N   1 
ATOM   4930  C CA  . SER C  1 206 ? 175.938 159.860 191.081 1.00 115.21 ? 208 SER C CA  1 
ATOM   4931  C C   . SER C  1 206 ? 176.427 161.286 191.293 1.00 119.39 ? 208 SER C C   1 
ATOM   4932  O O   . SER C  1 206 ? 176.605 161.701 192.443 1.00 120.73 ? 208 SER C O   1 
ATOM   4933  C CB  . SER C  1 206 ? 177.089 158.879 191.302 1.00 118.50 ? 208 SER C CB  1 
ATOM   4934  O OG  . SER C  1 206 ? 176.628 157.539 191.277 1.00 121.14 ? 208 SER C OG  1 
ATOM   4935  N N   . THR C  1 207 ? 176.647 162.041 190.219 1.00 117.46 ? 209 THR C N   1 
ATOM   4936  C CA  . THR C  1 207 ? 177.101 163.423 190.309 1.00 119.00 ? 209 THR C CA  1 
ATOM   4937  C C   . THR C  1 207 ? 175.945 164.416 190.325 1.00 120.83 ? 209 THR C C   1 
ATOM   4938  O O   . THR C  1 207 ? 175.915 165.318 191.165 1.00 119.79 ? 209 THR C O   1 
ATOM   4939  C CB  . THR C  1 207 ? 178.045 163.745 189.145 1.00 120.58 ? 209 THR C CB  1 
ATOM   4940  O OG1 . THR C  1 207 ? 177.277 164.002 187.963 1.00 123.89 ? 209 THR C OG1 1 
ATOM   4941  C CG2 . THR C  1 207 ? 178.984 162.580 188.888 1.00 111.90 ? 209 THR C CG2 1 
ATOM   4942  N N   . LEU C  1 208 ? 174.992 164.266 189.410 1.00 118.21 ? 210 LEU C N   1 
ATOM   4943  C CA  . LEU C  1 208 ? 173.818 165.126 189.340 1.00 114.45 ? 210 LEU C CA  1 
ATOM   4944  C C   . LEU C  1 208 ? 172.585 164.304 189.683 1.00 112.52 ? 210 LEU C C   1 
ATOM   4945  O O   . LEU C  1 208 ? 172.296 163.303 189.019 1.00 111.01 ? 210 LEU C O   1 
ATOM   4946  C CB  . LEU C  1 208 ? 173.677 165.752 187.953 1.00 114.23 ? 210 LEU C CB  1 
ATOM   4947  C CG  . LEU C  1 208 ? 172.628 166.858 187.834 1.00 117.39 ? 210 LEU C CG  1 
ATOM   4948  C CD1 . LEU C  1 208 ? 173.283 168.229 187.865 1.00 120.23 ? 210 LEU C CD1 1 
ATOM   4949  C CD2 . LEU C  1 208 ? 171.806 166.682 186.568 1.00 106.03 ? 210 LEU C CD2 1 
ATOM   4950  N N   . LYS C  1 209 ? 171.862 164.729 190.715 1.00 109.92 ? 211 LYS C N   1 
ATOM   4951  C CA  . LYS C  1 209 ? 170.652 164.058 191.166 1.00 106.09 ? 211 LYS C CA  1 
ATOM   4952  C C   . LYS C  1 209 ? 169.483 165.023 191.048 1.00 107.18 ? 211 LYS C C   1 
ATOM   4953  O O   . LYS C  1 209 ? 169.558 166.156 191.534 1.00 109.26 ? 211 LYS C O   1 
ATOM   4954  C CB  . LYS C  1 209 ? 170.806 163.570 192.606 1.00 100.34 ? 211 LYS C CB  1 
ATOM   4955  C CG  . LYS C  1 209 ? 171.933 162.571 192.783 1.00 105.38 ? 211 LYS C CG  1 
ATOM   4956  C CD  . LYS C  1 209 ? 172.083 162.145 194.228 1.00 104.12 ? 211 LYS C CD  1 
ATOM   4957  C CE  . LYS C  1 209 ? 172.793 160.808 194.323 1.00 102.64 ? 211 LYS C CE  1 
ATOM   4958  N NZ  . LYS C  1 209 ? 174.271 160.971 194.354 1.00 107.77 ? 211 LYS C NZ  1 
ATOM   4959  N N   . ARG C  1 210 ? 168.411 164.574 190.407 1.00 101.48 ? 212 ARG C N   1 
ATOM   4960  C CA  . ARG C  1 210 ? 167.255 165.414 190.139 1.00 93.37  ? 212 ARG C CA  1 
ATOM   4961  C C   . ARG C  1 210 ? 166.200 165.245 191.223 1.00 94.78  ? 212 ARG C C   1 
ATOM   4962  O O   . ARG C  1 210 ? 166.024 164.161 191.783 1.00 97.11  ? 212 ARG C O   1 
ATOM   4963  C CB  . ARG C  1 210 ? 166.643 165.081 188.778 1.00 82.77  ? 212 ARG C CB  1 
ATOM   4964  C CG  . ARG C  1 210 ? 167.411 165.626 187.592 1.00 76.24  ? 212 ARG C CG  1 
ATOM   4965  C CD  . ARG C  1 210 ? 166.767 165.190 186.289 1.00 77.95  ? 212 ARG C CD  1 
ATOM   4966  N NE  . ARG C  1 210 ? 167.455 165.742 185.130 1.00 80.49  ? 212 ARG C NE  1 
ATOM   4967  C CZ  . ARG C  1 210 ? 168.514 165.188 184.557 1.00 88.71  ? 212 ARG C CZ  1 
ATOM   4968  N NH1 . ARG C  1 210 ? 169.025 164.053 185.003 1.00 91.14  ? 212 ARG C NH1 1 
ATOM   4969  N NH2 . ARG C  1 210 ? 169.073 165.788 183.511 1.00 94.18  ? 212 ARG C NH2 1 
ATOM   4970  N N   . LYS C  1 211 ? 165.500 166.335 191.512 1.00 92.35  ? 213 LYS C N   1 
ATOM   4971  C CA  . LYS C  1 211 ? 164.341 166.297 192.387 1.00 89.01  ? 213 LYS C CA  1 
ATOM   4972  C C   . LYS C  1 211 ? 163.100 165.948 191.578 1.00 94.87  ? 213 LYS C C   1 
ATOM   4973  O O   . LYS C  1 211 ? 163.017 166.231 190.380 1.00 101.96 ? 213 LYS C O   1 
ATOM   4974  C CB  . LYS C  1 211 ? 164.137 167.642 193.084 1.00 86.55  ? 213 LYS C CB  1 
ATOM   4975  C CG  . LYS C  1 211 ? 165.179 167.978 194.129 1.00 92.20  ? 213 LYS C CG  1 
ATOM   4976  C CD  . LYS C  1 211 ? 165.047 169.423 194.573 1.00 96.70  ? 213 LYS C CD  1 
ATOM   4977  C CE  . LYS C  1 211 ? 163.681 169.685 195.182 1.00 100.37 ? 213 LYS C CE  1 
ATOM   4978  N NZ  . LYS C  1 211 ? 163.575 171.061 195.737 1.00 104.13 ? 213 LYS C NZ  1 
ATOM   4979  N N   . ILE C  1 212 ? 162.132 165.329 192.244 1.00 91.43  ? 214 ILE C N   1 
ATOM   4980  C CA  . ILE C  1 212 ? 160.840 165.028 191.643 1.00 93.98  ? 214 ILE C CA  1 
ATOM   4981  C C   . ILE C  1 212 ? 159.818 165.940 192.305 1.00 99.06  ? 214 ILE C C   1 
ATOM   4982  O O   . ILE C  1 212 ? 159.493 165.772 193.487 1.00 102.28 ? 214 ILE C O   1 
ATOM   4983  C CB  . ILE C  1 212 ? 160.463 163.550 191.797 1.00 90.08  ? 214 ILE C CB  1 
ATOM   4984  C CG1 . ILE C  1 212 ? 161.613 162.661 191.325 1.00 83.91  ? 214 ILE C CG1 1 
ATOM   4985  C CG2 . ILE C  1 212 ? 159.218 163.239 190.992 1.00 92.56  ? 214 ILE C CG2 1 
ATOM   4986  C CD1 . ILE C  1 212 ? 161.405 161.195 191.611 1.00 80.68  ? 214 ILE C CD1 1 
ATOM   4987  N N   . VAL C  1 213 ? 159.311 166.903 191.547 1.00 96.46  ? 215 VAL C N   1 
ATOM   4988  C CA  . VAL C  1 213 ? 158.442 167.930 192.078 1.00 97.95  ? 215 VAL C CA  1 
ATOM   4989  C C   . VAL C  1 213 ? 157.005 167.641 191.659 1.00 103.98 ? 215 VAL C C   1 
ATOM   4990  O O   . VAL C  1 213 ? 156.742 166.830 190.774 1.00 107.63 ? 215 VAL C O   1 
ATOM   4991  C CB  . VAL C  1 213 ? 158.880 169.341 191.621 1.00 96.74  ? 215 VAL C CB  1 
ATOM   4992  C CG1 . VAL C  1 213 ? 160.099 169.801 192.399 1.00 92.75  ? 215 VAL C CG1 1 
ATOM   4993  C CG2 . VAL C  1 213 ? 159.167 169.346 190.132 1.00 96.95  ? 215 VAL C CG2 1 
ATOM   4994  N N   . ASN C  1 214 ? 156.058 168.321 192.308 1.00 100.20 ? 216 ASN C N   1 
ATOM   4995  C CA  . ASN C  1 214 ? 154.636 168.228 191.975 1.00 102.75 ? 216 ASN C CA  1 
ATOM   4996  C C   . ASN C  1 214 ? 154.135 166.788 192.066 1.00 107.88 ? 216 ASN C C   1 
ATOM   4997  O O   . ASN C  1 214 ? 153.442 166.287 191.179 1.00 110.15 ? 216 ASN C O   1 
ATOM   4998  C CB  . ASN C  1 214 ? 154.361 168.821 190.592 1.00 103.43 ? 216 ASN C CB  1 
ATOM   4999  C CG  . ASN C  1 214 ? 154.649 170.305 190.530 1.00 105.55 ? 216 ASN C CG  1 
ATOM   5000  O OD1 . ASN C  1 214 ? 154.646 170.991 191.550 1.00 105.99 ? 216 ASN C OD1 1 
ATOM   5001  N ND2 . ASN C  1 214 ? 154.909 170.807 189.330 1.00 105.03 ? 216 ASN C ND2 1 
ATOM   5002  N N   . VAL C  1 215 ? 154.492 166.121 193.156 1.00 108.22 ? 217 VAL C N   1 
ATOM   5003  C CA  . VAL C  1 215 ? 154.070 164.748 193.402 1.00 108.68 ? 217 VAL C CA  1 
ATOM   5004  C C   . VAL C  1 215 ? 152.845 164.768 194.303 1.00 116.32 ? 217 VAL C C   1 
ATOM   5005  O O   . VAL C  1 215 ? 152.830 165.454 195.331 1.00 119.80 ? 217 VAL C O   1 
ATOM   5006  C CB  . VAL C  1 215 ? 155.204 163.927 194.037 1.00 105.53 ? 217 VAL C CB  1 
ATOM   5007  C CG1 . VAL C  1 215 ? 154.799 162.469 194.154 1.00 105.22 ? 217 VAL C CG1 1 
ATOM   5008  C CG2 . VAL C  1 215 ? 156.472 164.064 193.222 1.00 107.52 ? 217 VAL C CG2 1 
ATOM   5009  N N   . GLY C  1 216 ? 151.815 164.024 193.915 1.00 113.64 ? 218 GLY C N   1 
ATOM   5010  C CA  . GLY C  1 216 ? 150.642 163.908 194.751 1.00 115.14 ? 218 GLY C CA  1 
ATOM   5011  C C   . GLY C  1 216 ? 150.928 163.146 196.028 1.00 122.48 ? 218 GLY C C   1 
ATOM   5012  O O   . GLY C  1 216 ? 151.900 162.397 196.140 1.00 127.32 ? 218 GLY C O   1 
ATOM   5013  N N   . ASP C  1 217 ? 150.061 163.352 197.016 1.00 121.14 ? 219 ASP C N   1 
ATOM   5014  C CA  . ASP C  1 217 ? 150.243 162.710 198.310 1.00 120.44 ? 219 ASP C CA  1 
ATOM   5015  C C   . ASP C  1 217 ? 150.176 161.196 198.171 1.00 125.14 ? 219 ASP C C   1 
ATOM   5016  O O   . ASP C  1 217 ? 149.395 160.660 197.382 1.00 130.16 ? 219 ASP C O   1 
ATOM   5017  C CB  . ASP C  1 217 ? 149.181 163.193 199.297 1.00 122.33 ? 219 ASP C CB  1 
ATOM   5018  C CG  . ASP C  1 217 ? 149.494 164.560 199.862 1.00 125.85 ? 219 ASP C CG  1 
ATOM   5019  O OD1 . ASP C  1 217 ? 150.264 165.305 199.221 1.00 126.64 ? 219 ASP C OD1 1 
ATOM   5020  O OD2 . ASP C  1 217 ? 148.973 164.890 200.948 1.00 124.99 ? 219 ASP C OD2 1 
ATOM   5021  N N   . GLY C  1 218 ? 151.006 160.507 198.947 1.00 122.57 ? 220 GLY C N   1 
ATOM   5022  C CA  . GLY C  1 218 ? 151.032 159.059 198.918 1.00 119.20 ? 220 GLY C CA  1 
ATOM   5023  C C   . GLY C  1 218 ? 149.825 158.437 199.585 1.00 121.39 ? 220 GLY C C   1 
ATOM   5024  O O   . GLY C  1 218 ? 148.800 159.096 199.781 1.00 129.24 ? 220 GLY C O   1 
ATOM   5025  N N   . ALA C  1 219 ? 149.938 157.164 199.943 1.00 111.87 ? 221 ALA C N   1 
ATOM   5026  C CA  . ALA C  1 219 ? 148.840 156.381 200.497 1.00 113.22 ? 221 ALA C CA  1 
ATOM   5027  C C   . ALA C  1 219 ? 149.307 155.607 201.718 1.00 114.51 ? 221 ALA C C   1 
ATOM   5028  O O   . ALA C  1 219 ? 149.120 154.393 201.815 1.00 121.95 ? 221 ALA C O   1 
ATOM   5029  C CB  . ALA C  1 219 ? 148.257 155.437 199.451 1.00 117.52 ? 221 ALA C CB  1 
ATOM   5030  N N   . ILE C  1 220 ? 149.940 156.309 202.663 1.00 111.64 ? 222 ILE C N   1 
ATOM   5031  C CA  . ILE C  1 220 ? 150.626 155.691 203.796 1.00 112.24 ? 222 ILE C CA  1 
ATOM   5032  C C   . ILE C  1 220 ? 149.740 154.631 204.437 1.00 118.51 ? 222 ILE C C   1 
ATOM   5033  O O   . ILE C  1 220 ? 148.643 154.929 204.923 1.00 121.03 ? 222 ILE C O   1 
ATOM   5034  C CB  . ILE C  1 220 ? 151.037 156.748 204.838 1.00 105.50 ? 222 ILE C CB  1 
ATOM   5035  C CG1 . ILE C  1 220 ? 151.714 157.944 204.164 1.00 108.11 ? 222 ILE C CG1 1 
ATOM   5036  C CG2 . ILE C  1 220 ? 151.944 156.136 205.890 1.00 106.92 ? 222 ILE C CG2 1 
ATOM   5037  C CD1 . ILE C  1 220 ? 152.830 157.569 203.217 1.00 110.79 ? 222 ILE C CD1 1 
ATOM   5038  N N   . SER C  1 221 ? 150.223 153.394 204.450 1.00 119.88 ? 223 SER C N   1 
ATOM   5039  C CA  . SER C  1 221 ? 149.442 152.235 204.867 1.00 116.01 ? 223 SER C CA  1 
ATOM   5040  C C   . SER C  1 221 ? 150.392 151.047 204.966 1.00 118.60 ? 223 SER C C   1 
ATOM   5041  O O   . SER C  1 221 ? 151.605 151.180 204.783 1.00 122.13 ? 223 SER C O   1 
ATOM   5042  C CB  . SER C  1 221 ? 148.295 151.950 203.897 1.00 117.79 ? 223 SER C CB  1 
ATOM   5043  O OG  . SER C  1 221 ? 148.692 151.017 202.908 1.00 120.21 ? 223 SER C OG  1 
ATOM   5044  N N   . ALA C  1 222 ? 149.822 149.874 205.246 1.00 121.43 ? 224 ALA C N   1 
ATOM   5045  C CA  . ALA C  1 222 ? 150.643 148.691 205.482 1.00 122.58 ? 224 ALA C CA  1 
ATOM   5046  C C   . ALA C  1 222 ? 151.273 148.171 204.195 1.00 122.26 ? 224 ALA C C   1 
ATOM   5047  O O   . ALA C  1 222 ? 152.422 147.714 204.204 1.00 122.01 ? 224 ALA C O   1 
ATOM   5048  C CB  . ALA C  1 222 ? 149.807 147.598 206.146 1.00 120.99 ? 224 ALA C CB  1 
ATOM   5049  N N   . ASN C  1 223 ? 150.545 148.230 203.082 1.00 122.18 ? 225 ASN C N   1 
ATOM   5050  C CA  . ASN C  1 223 ? 150.978 147.586 201.851 1.00 121.94 ? 225 ASN C CA  1 
ATOM   5051  C C   . ASN C  1 223 ? 151.071 148.526 200.659 1.00 120.35 ? 225 ASN C C   1 
ATOM   5052  O O   . ASN C  1 223 ? 151.385 148.065 199.556 1.00 119.50 ? 225 ASN C O   1 
ATOM   5053  C CB  . ASN C  1 223 ? 150.030 146.432 201.501 1.00 129.91 ? 225 ASN C CB  1 
ATOM   5054  C CG  . ASN C  1 223 ? 148.578 146.778 201.758 1.00 136.28 ? 225 ASN C CG  1 
ATOM   5055  O OD1 . ASN C  1 223 ? 148.065 147.774 201.246 1.00 136.65 ? 225 ASN C OD1 1 
ATOM   5056  N ND2 . ASN C  1 223 ? 147.906 145.958 202.556 1.00 136.64 ? 225 ASN C ND2 1 
ATOM   5057  N N   . SER C  1 224 ? 150.806 149.816 200.837 1.00 117.69 ? 226 SER C N   1 
ATOM   5058  C CA  . SER C  1 224 ? 150.810 150.733 199.708 1.00 119.96 ? 226 SER C CA  1 
ATOM   5059  C C   . SER C  1 224 ? 152.217 150.913 199.156 1.00 122.23 ? 226 SER C C   1 
ATOM   5060  O O   . SER C  1 224 ? 153.188 151.034 199.908 1.00 126.76 ? 226 SER C O   1 
ATOM   5061  C CB  . SER C  1 224 ? 150.239 152.086 200.120 1.00 117.65 ? 226 SER C CB  1 
ATOM   5062  O OG  . SER C  1 224 ? 151.269 152.968 200.531 1.00 117.67 ? 226 SER C OG  1 
ATOM   5063  N N   . SER C  1 225 ? 152.321 150.933 197.831 1.00 116.72 ? 227 SER C N   1 
ATOM   5064  C CA  . SER C  1 225 ? 153.573 151.206 197.133 1.00 114.57 ? 227 SER C CA  1 
ATOM   5065  C C   . SER C  1 225 ? 153.379 152.519 196.385 1.00 116.85 ? 227 SER C C   1 
ATOM   5066  O O   . SER C  1 225 ? 153.009 152.534 195.210 1.00 118.91 ? 227 SER C O   1 
ATOM   5067  C CB  . SER C  1 225 ? 153.943 150.073 196.193 1.00 118.67 ? 227 SER C CB  1 
ATOM   5068  O OG  . SER C  1 225 ? 153.108 150.077 195.049 1.00 126.89 ? 227 SER C OG  1 
ATOM   5069  N N   . ASP C  1 226 ? 153.638 153.624 197.079 1.00 115.57 ? 228 ASP C N   1 
ATOM   5070  C CA  . ASP C  1 226 ? 153.486 154.954 196.509 1.00 113.04 ? 228 ASP C CA  1 
ATOM   5071  C C   . ASP C  1 226 ? 154.769 155.744 196.713 1.00 111.51 ? 228 ASP C C   1 
ATOM   5072  O O   . ASP C  1 226 ? 155.803 155.171 197.064 1.00 116.39 ? 228 ASP C O   1 
ATOM   5073  C CB  . ASP C  1 226 ? 152.297 155.678 197.139 1.00 116.66 ? 228 ASP C CB  1 
ATOM   5074  C CG  . ASP C  1 226 ? 151.063 155.636 196.265 1.00 124.12 ? 228 ASP C CG  1 
ATOM   5075  O OD1 . ASP C  1 226 ? 151.171 155.995 195.076 1.00 130.02 ? 228 ASP C OD1 1 
ATOM   5076  O OD2 . ASP C  1 226 ? 149.989 155.240 196.761 1.00 121.57 ? 228 ASP C OD2 1 
ATOM   5077  N N   . ALA C  1 227 ? 154.725 157.050 196.478 1.00 105.04 ? 229 ALA C N   1 
ATOM   5078  C CA  . ALA C  1 227 ? 155.860 157.928 196.735 1.00 98.12  ? 229 ALA C CA  1 
ATOM   5079  C C   . ALA C  1 227 ? 155.413 158.994 197.724 1.00 105.93 ? 229 ALA C C   1 
ATOM   5080  O O   . ALA C  1 227 ? 154.594 159.854 197.385 1.00 115.92 ? 229 ALA C O   1 
ATOM   5081  C CB  . ALA C  1 227 ? 156.377 158.555 195.442 1.00 93.34  ? 229 ALA C CB  1 
ATOM   5082  N N   . VAL C  1 228 ? 155.944 158.936 198.947 1.00 100.50 ? 230 VAL C N   1 
ATOM   5083  C CA  . VAL C  1 228 ? 155.587 159.946 199.933 1.00 102.59 ? 230 VAL C CA  1 
ATOM   5084  C C   . VAL C  1 228 ? 156.201 161.284 199.537 1.00 105.40 ? 230 VAL C C   1 
ATOM   5085  O O   . VAL C  1 228 ? 157.189 161.359 198.796 1.00 106.95 ? 230 VAL C O   1 
ATOM   5086  C CB  . VAL C  1 228 ? 156.024 159.525 201.346 1.00 97.10  ? 230 VAL C CB  1 
ATOM   5087  C CG1 . VAL C  1 228 ? 156.034 158.011 201.470 1.00 98.30  ? 230 VAL C CG1 1 
ATOM   5088  C CG2 . VAL C  1 228 ? 157.381 160.109 201.693 1.00 96.85  ? 230 VAL C CG2 1 
ATOM   5089  N N   . THR C  1 229 ? 155.596 162.356 200.027 1.00 105.98 ? 231 THR C N   1 
ATOM   5090  C CA  . THR C  1 229 ? 156.009 163.703 199.672 1.00 101.46 ? 231 THR C CA  1 
ATOM   5091  C C   . THR C  1 229 ? 156.623 164.398 200.881 1.00 98.26  ? 231 THR C C   1 
ATOM   5092  O O   . THR C  1 229 ? 156.704 163.841 201.979 1.00 98.41  ? 231 THR C O   1 
ATOM   5093  C CB  . THR C  1 229 ? 154.828 164.502 199.121 1.00 103.76 ? 231 THR C CB  1 
ATOM   5094  O OG1 . THR C  1 229 ? 153.721 164.404 200.023 1.00 110.21 ? 231 THR C OG1 1 
ATOM   5095  C CG2 . THR C  1 229 ? 154.411 163.958 197.767 1.00 105.23 ? 231 THR C CG2 1 
ATOM   5096  N N   . GLY C  1 230 ? 157.064 165.637 200.662 1.00 93.78  ? 232 GLY C N   1 
ATOM   5097  C CA  . GLY C  1 230 ? 157.678 166.392 201.739 1.00 95.13  ? 232 GLY C CA  1 
ATOM   5098  C C   . GLY C  1 230 ? 156.718 166.672 202.878 1.00 100.87 ? 232 GLY C C   1 
ATOM   5099  O O   . GLY C  1 230 ? 157.082 166.564 204.049 1.00 103.66 ? 232 GLY C O   1 
ATOM   5100  N N   . ARG C  1 231 ? 155.476 167.033 202.549 1.00 99.52  ? 233 ARG C N   1 
ATOM   5101  C CA  . ARG C  1 231 ? 154.491 167.314 203.589 1.00 100.20 ? 233 ARG C CA  1 
ATOM   5102  C C   . ARG C  1 231 ? 154.121 166.053 204.360 1.00 103.10 ? 233 ARG C C   1 
ATOM   5103  O O   . ARG C  1 231 ? 153.888 166.108 205.573 1.00 103.34 ? 233 ARG C O   1 
ATOM   5104  C CB  . ARG C  1 231 ? 153.247 167.950 202.971 1.00 99.04  ? 233 ARG C CB  1 
ATOM   5105  C CG  . ARG C  1 231 ? 152.742 167.239 201.731 1.00 102.85 ? 233 ARG C CG  1 
ATOM   5106  C CD  . ARG C  1 231 ? 151.236 167.059 201.778 1.00 109.12 ? 233 ARG C CD  1 
ATOM   5107  N NE  . ARG C  1 231 ? 150.528 168.329 201.689 1.00 110.37 ? 233 ARG C NE  1 
ATOM   5108  C CZ  . ARG C  1 231 ? 150.374 169.026 200.571 1.00 114.20 ? 233 ARG C CZ  1 
ATOM   5109  N NH1 . ARG C  1 231 ? 150.863 168.601 199.418 1.00 112.50 ? 233 ARG C NH1 1 
ATOM   5110  N NH2 . ARG C  1 231 ? 149.710 170.177 200.611 1.00 113.95 ? 233 ARG C NH2 1 
ATOM   5111  N N   . GLN C  1 232 ? 154.053 164.911 203.673 1.00 103.92 ? 234 GLN C N   1 
ATOM   5112  C CA  . GLN C  1 232 ? 153.704 163.659 204.338 1.00 98.35  ? 234 GLN C CA  1 
ATOM   5113  C C   . GLN C  1 232 ? 154.744 163.284 205.383 1.00 100.81 ? 234 GLN C C   1 
ATOM   5114  O O   . GLN C  1 232 ? 154.404 162.887 206.503 1.00 105.29 ? 234 GLN C O   1 
ATOM   5115  C CB  . GLN C  1 232 ? 153.560 162.547 203.302 1.00 96.49  ? 234 GLN C CB  1 
ATOM   5116  C CG  . GLN C  1 232 ? 152.401 162.736 202.351 1.00 104.42 ? 234 GLN C CG  1 
ATOM   5117  C CD  . GLN C  1 232 ? 151.773 161.426 201.948 1.00 110.54 ? 234 GLN C CD  1 
ATOM   5118  O OE1 . GLN C  1 232 ? 152.393 160.619 201.261 1.00 113.24 ? 234 GLN C OE1 1 
ATOM   5119  N NE2 . GLN C  1 232 ? 150.536 161.205 202.372 1.00 116.09 ? 234 GLN C NE2 1 
ATOM   5120  N N   . LEU C  1 233 ? 156.025 163.401 205.031 1.00 100.53 ? 235 LEU C N   1 
ATOM   5121  C CA  . LEU C  1 233 ? 157.083 163.099 205.986 1.00 100.34 ? 235 LEU C CA  1 
ATOM   5122  C C   . LEU C  1 233 ? 157.206 164.195 207.037 1.00 100.98 ? 235 LEU C C   1 
ATOM   5123  O O   . LEU C  1 233 ? 157.625 163.926 208.168 1.00 102.78 ? 235 LEU C O   1 
ATOM   5124  C CB  . LEU C  1 233 ? 158.401 162.889 205.235 1.00 97.53  ? 235 LEU C CB  1 
ATOM   5125  C CG  . LEU C  1 233 ? 159.704 162.502 205.945 1.00 96.57  ? 235 LEU C CG  1 
ATOM   5126  C CD1 . LEU C  1 233 ? 160.437 163.713 206.496 1.00 101.27 ? 235 LEU C CD1 1 
ATOM   5127  C CD2 . LEU C  1 233 ? 159.435 161.490 207.047 1.00 99.89  ? 235 LEU C CD2 1 
ATOM   5128  N N   . TYR C  1 234 ? 156.842 165.429 206.685 1.00 99.66  ? 236 TYR C N   1 
ATOM   5129  C CA  . TYR C  1 234 ? 156.891 166.530 207.640 1.00 101.01 ? 236 TYR C CA  1 
ATOM   5130  C C   . TYR C  1 234 ? 155.868 166.342 208.751 1.00 104.32 ? 236 TYR C C   1 
ATOM   5131  O O   . TYR C  1 234 ? 156.200 166.430 209.938 1.00 104.66 ? 236 TYR C O   1 
ATOM   5132  C CB  . TYR C  1 234 ? 156.648 167.850 206.912 1.00 99.21  ? 236 TYR C CB  1 
ATOM   5133  C CG  . TYR C  1 234 ? 156.674 169.067 207.804 1.00 103.25 ? 236 TYR C CG  1 
ATOM   5134  C CD1 . TYR C  1 234 ? 157.786 169.364 208.575 1.00 106.62 ? 236 TYR C CD1 1 
ATOM   5135  C CD2 . TYR C  1 234 ? 155.573 169.905 207.894 1.00 99.87  ? 236 TYR C CD2 1 
ATOM   5136  C CE1 . TYR C  1 234 ? 157.811 170.477 209.390 1.00 107.30 ? 236 TYR C CE1 1 
ATOM   5137  C CE2 . TYR C  1 234 ? 155.585 171.015 208.709 1.00 100.44 ? 236 TYR C CE2 1 
ATOM   5138  C CZ  . TYR C  1 234 ? 156.706 171.296 209.457 1.00 106.15 ? 236 TYR C CZ  1 
ATOM   5139  O OH  . TYR C  1 234 ? 156.722 172.403 210.272 1.00 106.33 ? 236 TYR C OH  1 
ATOM   5140  N N   . SER C  1 235 ? 154.614 166.081 208.383 1.00 104.40 ? 237 SER C N   1 
ATOM   5141  C CA  . SER C  1 235 ? 153.546 165.935 209.362 1.00 102.61 ? 237 SER C CA  1 
ATOM   5142  C C   . SER C  1 235 ? 153.466 164.530 209.937 1.00 105.84 ? 237 SER C C   1 
ATOM   5143  O O   . SER C  1 235 ? 153.115 164.369 211.111 1.00 105.12 ? 237 SER C O   1 
ATOM   5144  C CB  . SER C  1 235 ? 152.201 166.306 208.734 1.00 107.66 ? 237 SER C CB  1 
ATOM   5145  O OG  . SER C  1 235 ? 152.000 165.615 207.514 1.00 110.75 ? 237 SER C OG  1 
ATOM   5146  N N   . GLY C  1 236 ? 153.780 163.514 209.139 1.00 109.62 ? 238 GLY C N   1 
ATOM   5147  C CA  . GLY C  1 236 ? 153.762 162.151 209.628 1.00 110.25 ? 238 GLY C CA  1 
ATOM   5148  C C   . GLY C  1 236 ? 152.388 161.560 209.820 1.00 108.12 ? 238 GLY C C   1 
ATOM   5149  O O   . GLY C  1 236 ? 152.246 160.581 210.554 1.00 111.73 ? 238 GLY C O   1 
ATOM   5150  N N   . ASN C  1 237 ? 151.366 162.129 209.187 1.00 109.33 ? 239 ASN C N   1 
ATOM   5151  C CA  . ASN C  1 237 ? 150.013 161.615 209.343 1.00 110.48 ? 239 ASN C CA  1 
ATOM   5152  C C   . ASN C  1 237 ? 149.896 160.217 208.751 1.00 112.68 ? 239 ASN C C   1 
ATOM   5153  O O   . ASN C  1 237 ? 150.422 159.934 207.671 1.00 113.56 ? 239 ASN C O   1 
ATOM   5154  C CB  . ASN C  1 237 ? 149.009 162.551 208.672 1.00 110.17 ? 239 ASN C CB  1 
ATOM   5155  C CG  . ASN C  1 237 ? 149.123 163.977 209.164 1.00 113.89 ? 239 ASN C CG  1 
ATOM   5156  O OD1 . ASN C  1 237 ? 149.446 164.222 210.326 1.00 117.78 ? 239 ASN C OD1 1 
ATOM   5157  N ND2 . ASN C  1 237 ? 148.857 164.931 208.280 1.00 114.72 ? 239 ASN C ND2 1 
ATOM   5158  N N   . GLY C  1 238 ? 149.200 159.339 209.469 1.00 111.96 ? 240 GLY C N   1 
ATOM   5159  C CA  . GLY C  1 238 ? 148.930 158.000 208.993 1.00 115.81 ? 240 GLY C CA  1 
ATOM   5160  C C   . GLY C  1 238 ? 150.000 156.971 209.280 1.00 114.89 ? 240 GLY C C   1 
ATOM   5161  O O   . GLY C  1 238 ? 149.849 155.816 208.860 1.00 118.46 ? 240 GLY C O   1 
ATOM   5162  N N   . ILE C  1 239 ? 151.076 157.341 209.977 1.00 113.70 ? 241 ILE C N   1 
ATOM   5163  C CA  . ILE C  1 239 ? 152.109 156.365 210.300 1.00 109.72 ? 241 ILE C CA  1 
ATOM   5164  C C   . ILE C  1 239 ? 151.593 155.388 211.351 1.00 109.13 ? 241 ILE C C   1 
ATOM   5165  O O   . ILE C  1 239 ? 150.603 155.634 212.049 1.00 111.81 ? 241 ILE C O   1 
ATOM   5166  C CB  . ILE C  1 239 ? 153.394 157.058 210.779 1.00 103.56 ? 241 ILE C CB  1 
ATOM   5167  C CG1 . ILE C  1 239 ? 153.126 157.819 212.079 1.00 102.40 ? 241 ILE C CG1 1 
ATOM   5168  C CG2 . ILE C  1 239 ? 153.936 157.979 209.701 1.00 101.91 ? 241 ILE C CG2 1 
ATOM   5169  C CD1 . ILE C  1 239 ? 154.250 158.728 212.498 1.00 98.84  ? 241 ILE C CD1 1 
ATOM   5170  N N   . ASP C  1 240 ? 152.284 154.258 211.463 1.00 105.09 ? 242 ASP C N   1 
ATOM   5171  C CA  . ASP C  1 240 ? 151.958 153.258 212.475 1.00 107.15 ? 242 ASP C CA  1 
ATOM   5172  C C   . ASP C  1 240 ? 152.425 153.779 213.826 1.00 107.57 ? 242 ASP C C   1 
ATOM   5173  O O   . ASP C  1 240 ? 153.595 153.646 214.188 1.00 111.93 ? 242 ASP C O   1 
ATOM   5174  C CB  . ASP C  1 240 ? 152.613 151.924 212.137 1.00 109.49 ? 242 ASP C CB  1 
ATOM   5175  C CG  . ASP C  1 240 ? 152.019 150.767 212.917 1.00 116.29 ? 242 ASP C CG  1 
ATOM   5176  O OD1 . ASP C  1 240 ? 151.912 150.869 214.157 1.00 113.57 ? 242 ASP C OD1 1 
ATOM   5177  O OD2 . ASP C  1 240 ? 151.658 149.751 212.287 1.00 122.42 ? 242 ASP C OD2 1 
ATOM   5178  N N   . THR C  1 241 ? 151.503 154.376 214.582 1.00 106.97 ? 243 THR C N   1 
ATOM   5179  C CA  . THR C  1 241 ? 151.847 154.952 215.875 1.00 108.02 ? 243 THR C CA  1 
ATOM   5180  C C   . THR C  1 241 ? 152.291 153.908 216.889 1.00 109.49 ? 243 THR C C   1 
ATOM   5181  O O   . THR C  1 241 ? 152.889 154.278 217.903 1.00 107.71 ? 243 THR C O   1 
ATOM   5182  C CB  . THR C  1 241 ? 150.661 155.735 216.439 1.00 108.84 ? 243 THR C CB  1 
ATOM   5183  O OG1 . THR C  1 241 ? 149.679 154.821 216.941 1.00 114.13 ? 243 THR C OG1 1 
ATOM   5184  C CG2 . THR C  1 241 ? 150.035 156.603 215.359 1.00 109.81 ? 243 THR C CG2 1 
ATOM   5185  N N   . ALA C  1 242 ? 152.016 152.628 216.652 1.00 111.23 ? 244 ALA C N   1 
ATOM   5186  C CA  . ALA C  1 242 ? 152.439 151.566 217.555 1.00 110.01 ? 244 ALA C CA  1 
ATOM   5187  C C   . ALA C  1 242 ? 153.769 150.943 217.157 1.00 112.53 ? 244 ALA C C   1 
ATOM   5188  O O   . ALA C  1 242 ? 154.596 150.656 218.027 1.00 110.26 ? 244 ALA C O   1 
ATOM   5189  C CB  . ALA C  1 242 ? 151.368 150.474 217.628 1.00 105.96 ? 244 ALA C CB  1 
ATOM   5190  N N   . ALA C  1 243 ? 153.992 150.719 215.860 1.00 115.19 ? 245 ALA C N   1 
ATOM   5191  C CA  . ALA C  1 243 ? 155.274 150.181 215.415 1.00 113.57 ? 245 ALA C CA  1 
ATOM   5192  C C   . ALA C  1 243 ? 156.405 151.168 215.672 1.00 112.65 ? 245 ALA C C   1 
ATOM   5193  O O   . ALA C  1 243 ? 157.495 150.777 216.105 1.00 110.01 ? 245 ALA C O   1 
ATOM   5194  C CB  . ALA C  1 243 ? 155.206 149.818 213.932 1.00 109.68 ? 245 ALA C CB  1 
ATOM   5195  N N   . TRP C  1 244 ? 156.165 152.454 215.406 1.00 109.67 ? 246 TRP C N   1 
ATOM   5196  C CA  . TRP C  1 244 ? 157.184 153.470 215.635 1.00 98.58  ? 246 TRP C CA  1 
ATOM   5197  C C   . TRP C  1 244 ? 157.519 153.624 217.111 1.00 100.68 ? 246 TRP C C   1 
ATOM   5198  O O   . TRP C  1 244 ? 158.641 154.021 217.444 1.00 104.83 ? 246 TRP C O   1 
ATOM   5199  C CB  . TRP C  1 244 ? 156.720 154.809 215.060 1.00 89.28  ? 246 TRP C CB  1 
ATOM   5200  C CG  . TRP C  1 244 ? 156.924 154.935 213.583 1.00 87.34  ? 246 TRP C CG  1 
ATOM   5201  C CD1 . TRP C  1 244 ? 156.213 154.308 212.604 1.00 97.06  ? 246 TRP C CD1 1 
ATOM   5202  C CD2 . TRP C  1 244 ? 157.889 155.754 212.914 1.00 86.30  ? 246 TRP C CD2 1 
ATOM   5203  N NE1 . TRP C  1 244 ? 156.681 154.677 211.368 1.00 93.78  ? 246 TRP C NE1 1 
ATOM   5204  C CE2 . TRP C  1 244 ? 157.710 155.566 211.531 1.00 90.18  ? 246 TRP C CE2 1 
ATOM   5205  C CE3 . TRP C  1 244 ? 158.890 156.625 213.351 1.00 84.55  ? 246 TRP C CE3 1 
ATOM   5206  C CZ2 . TRP C  1 244 ? 158.494 156.215 210.581 1.00 86.29  ? 246 TRP C CZ2 1 
ATOM   5207  C CZ3 . TRP C  1 244 ? 159.667 157.269 212.407 1.00 88.29  ? 246 TRP C CZ3 1 
ATOM   5208  C CH2 . TRP C  1 244 ? 159.465 157.060 211.038 1.00 88.55  ? 246 TRP C CH2 1 
ATOM   5209  N N   . GLN C  1 245 ? 156.578 153.320 218.000 1.00 101.93 ? 247 GLN C N   1 
ATOM   5210  C CA  . GLN C  1 245 ? 156.783 153.444 219.437 1.00 104.80 ? 247 GLN C CA  1 
ATOM   5211  C C   . GLN C  1 245 ? 157.548 152.272 220.034 1.00 109.41 ? 247 GLN C C   1 
ATOM   5212  O O   . GLN C  1 245 ? 157.825 152.280 221.237 1.00 111.72 ? 247 GLN C O   1 
ATOM   5213  C CB  . GLN C  1 245 ? 155.437 153.595 220.147 1.00 104.34 ? 247 GLN C CB  1 
ATOM   5214  C CG  . GLN C  1 245 ? 154.887 155.004 220.109 1.00 108.93 ? 247 GLN C CG  1 
ATOM   5215  C CD  . GLN C  1 245 ? 153.586 155.132 220.864 1.00 112.67 ? 247 GLN C CD  1 
ATOM   5216  O OE1 . GLN C  1 245 ? 152.956 154.134 221.206 1.00 116.25 ? 247 GLN C OE1 1 
ATOM   5217  N NE2 . GLN C  1 245 ? 153.174 156.365 221.130 1.00 112.88 ? 247 GLN C NE2 1 
ATOM   5218  N N   . ASN C  1 246 ? 157.884 151.266 219.233 1.00 109.94 ? 248 ASN C N   1 
ATOM   5219  C CA  . ASN C  1 246 ? 158.750 150.178 219.667 1.00 110.21 ? 248 ASN C CA  1 
ATOM   5220  C C   . ASN C  1 246 ? 160.172 150.342 219.155 1.00 111.45 ? 248 ASN C C   1 
ATOM   5221  O O   . ASN C  1 246 ? 161.130 150.091 219.892 1.00 112.39 ? 248 ASN C O   1 
ATOM   5222  C CB  . ASN C  1 246 ? 158.189 148.837 219.188 1.00 112.77 ? 248 ASN C CB  1 
ATOM   5223  C CG  . ASN C  1 246 ? 157.257 148.203 220.196 1.00 117.95 ? 248 ASN C CG  1 
ATOM   5224  O OD1 . ASN C  1 246 ? 156.982 148.774 221.251 1.00 118.98 ? 248 ASN C OD1 1 
ATOM   5225  N ND2 . ASN C  1 246 ? 156.756 147.017 219.872 1.00 122.97 ? 248 ASN C ND2 1 
ATOM   5226  N N   . LYS C  1 247 ? 160.314 150.761 217.898 1.00 109.49 ? 249 LYS C N   1 
ATOM   5227  C CA  . LYS C  1 247 ? 161.628 151.044 217.333 1.00 109.10 ? 249 LYS C CA  1 
ATOM   5228  C C   . LYS C  1 247 ? 162.297 152.203 218.057 1.00 106.77 ? 249 LYS C C   1 
ATOM   5229  O O   . LYS C  1 247 ? 163.491 152.145 218.373 1.00 109.10 ? 249 LYS C O   1 
ATOM   5230  C CB  . LYS C  1 247 ? 161.459 151.333 215.848 1.00 101.14 ? 249 LYS C CB  1 
ATOM   5231  C CG  . LYS C  1 247 ? 162.658 151.097 214.966 1.00 102.54 ? 249 LYS C CG  1 
ATOM   5232  C CD  . LYS C  1 247 ? 162.262 151.490 213.565 1.00 111.50 ? 249 LYS C CD  1 
ATOM   5233  C CE  . LYS C  1 247 ? 160.864 150.925 213.311 1.00 116.95 ? 249 LYS C CE  1 
ATOM   5234  N NZ  . LYS C  1 247 ? 160.577 150.509 211.928 1.00 103.40 ? 249 LYS C NZ  1 
ATOM   5235  N N   . LEU C  1 248 ? 161.545 153.263 218.324 1.00 100.58 ? 250 LEU C N   1 
ATOM   5236  C CA  . LEU C  1 248 ? 161.941 154.296 219.269 1.00 99.05  ? 250 LEU C CA  1 
ATOM   5237  C C   . LEU C  1 248 ? 161.272 153.966 220.595 1.00 103.42 ? 250 LEU C C   1 
ATOM   5238  O O   . LEU C  1 248 ? 160.042 153.899 220.669 1.00 109.50 ? 250 LEU C O   1 
ATOM   5239  C CB  . LEU C  1 248 ? 161.527 155.689 218.791 1.00 95.52  ? 250 LEU C CB  1 
ATOM   5240  C CG  . LEU C  1 248 ? 162.156 156.333 217.552 1.00 93.91  ? 250 LEU C CG  1 
ATOM   5241  C CD1 . LEU C  1 248 ? 161.740 155.646 216.260 1.00 96.21  ? 250 LEU C CD1 1 
ATOM   5242  C CD2 . LEU C  1 248 ? 161.797 157.808 217.506 1.00 91.45  ? 250 LEU C CD2 1 
ATOM   5243  N N   . ASN C  1 249 ? 162.075 153.750 221.635 1.00 96.98  ? 251 ASN C N   1 
ATOM   5244  C CA  . ASN C  1 249 ? 161.549 153.283 222.918 1.00 101.46 ? 251 ASN C CA  1 
ATOM   5245  C C   . ASN C  1 249 ? 160.911 154.453 223.668 1.00 108.85 ? 251 ASN C C   1 
ATOM   5246  O O   . ASN C  1 249 ? 161.319 154.834 224.766 1.00 113.27 ? 251 ASN C O   1 
ATOM   5247  C CB  . ASN C  1 249 ? 162.651 152.633 223.742 1.00 100.22 ? 251 ASN C CB  1 
ATOM   5248  C CG  . ASN C  1 249 ? 163.547 151.741 222.913 1.00 109.90 ? 251 ASN C CG  1 
ATOM   5249  O OD1 . ASN C  1 249 ? 163.266 151.470 221.746 1.00 113.08 ? 251 ASN C OD1 1 
ATOM   5250  N ND2 . ASN C  1 249 ? 164.638 151.279 223.512 1.00 108.19 ? 251 ASN C ND2 1 
ATOM   5251  N N   . VAL C  1 250 ? 159.871 155.018 223.056 1.00 107.40 ? 252 VAL C N   1 
ATOM   5252  C CA  . VAL C  1 250 ? 159.229 156.192 223.630 1.00 101.12 ? 252 VAL C CA  1 
ATOM   5253  C C   . VAL C  1 250 ? 158.530 155.818 224.933 1.00 104.83 ? 252 VAL C C   1 
ATOM   5254  O O   . VAL C  1 250 ? 158.155 154.667 225.170 1.00 109.50 ? 252 VAL C O   1 
ATOM   5255  C CB  . VAL C  1 250 ? 158.247 156.842 222.639 1.00 90.34  ? 252 VAL C CB  1 
ATOM   5256  C CG1 . VAL C  1 250 ? 158.778 156.757 221.218 1.00 92.70  ? 252 VAL C CG1 1 
ATOM   5257  C CG2 . VAL C  1 250 ? 156.875 156.209 222.753 1.00 99.24  ? 252 VAL C CG2 1 
ATOM   5258  N N   . THR C  1 251 ? 158.372 156.813 225.794 1.00 108.96 ? 253 THR C N   1 
ATOM   5259  C CA  . THR C  1 251 ? 157.641 156.682 227.049 1.00 117.16 ? 253 THR C CA  1 
ATOM   5260  C C   . THR C  1 251 ? 156.356 157.487 226.908 1.00 131.07 ? 253 THR C C   1 
ATOM   5261  O O   . THR C  1 251 ? 156.376 158.719 226.971 1.00 137.74 ? 253 THR C O   1 
ATOM   5262  C CB  . THR C  1 251 ? 158.473 157.170 228.228 1.00 116.87 ? 253 THR C CB  1 
ATOM   5263  O OG1 . THR C  1 251 ? 159.689 156.416 228.306 1.00 114.74 ? 253 THR C OG1 1 
ATOM   5264  C CG2 . THR C  1 251 ? 157.691 157.037 229.518 1.00 120.36 ? 253 THR C CG2 1 
ATOM   5265  N N   . ARG C  1 252 ? 155.242 156.787 226.713 1.00 131.52 ? 254 ARG C N   1 
ATOM   5266  C CA  . ARG C  1 252 ? 153.978 157.467 226.481 1.00 133.35 ? 254 ARG C CA  1 
ATOM   5267  C C   . ARG C  1 252 ? 153.562 158.270 227.706 1.00 143.03 ? 254 ARG C C   1 
ATOM   5268  O O   . ARG C  1 252 ? 153.716 157.825 228.846 1.00 143.59 ? 254 ARG C O   1 
ATOM   5269  C CB  . ARG C  1 252 ? 152.895 156.458 226.103 1.00 138.16 ? 254 ARG C CB  1 
ATOM   5270  C CG  . ARG C  1 252 ? 152.733 155.311 227.078 1.00 145.00 ? 254 ARG C CG  1 
ATOM   5271  C CD  . ARG C  1 252 ? 151.865 154.209 226.491 1.00 141.69 ? 254 ARG C CD  1 
ATOM   5272  N NE  . ARG C  1 252 ? 152.558 153.467 225.445 1.00 135.30 ? 254 ARG C NE  1 
ATOM   5273  C CZ  . ARG C  1 252 ? 152.423 153.693 224.145 1.00 133.54 ? 254 ARG C CZ  1 
ATOM   5274  N NH1 . ARG C  1 252 ? 151.617 154.636 223.687 1.00 134.10 ? 254 ARG C NH1 1 
ATOM   5275  N NH2 . ARG C  1 252 ? 153.114 152.953 223.283 1.00 131.12 ? 254 ARG C NH2 1 
ATOM   5276  N N   . LYS C  1 253 ? 153.043 159.476 227.457 1.00 143.74 ? 255 LYS C N   1 
ATOM   5277  C CA  . LYS C  1 253 ? 152.572 160.320 228.549 1.00 145.84 ? 255 LYS C CA  1 
ATOM   5278  C C   . LYS C  1 253 ? 151.441 159.653 229.317 1.00 150.01 ? 255 LYS C C   1 
ATOM   5279  O O   . LYS C  1 253 ? 151.252 159.926 230.507 1.00 147.74 ? 255 LYS C O   1 
ATOM   5280  C CB  . LYS C  1 253 ? 152.120 161.676 228.009 1.00 138.66 ? 255 LYS C CB  1 
ATOM   5281  C CG  . LYS C  1 253 ? 153.217 162.725 227.961 1.00 136.96 ? 255 LYS C CG  1 
ATOM   5282  C CD  . LYS C  1 253 ? 152.752 163.972 227.229 1.00 133.76 ? 255 LYS C CD  1 
ATOM   5283  C CE  . LYS C  1 253 ? 153.641 165.164 227.544 1.00 133.40 ? 255 LYS C CE  1 
ATOM   5284  N NZ  . LYS C  1 253 ? 153.944 165.261 228.997 1.00 130.94 ? 255 LYS C NZ  1 
ATOM   5285  N N   . ASN C  1 254 ? 150.680 158.780 228.654 1.00 153.73 ? 256 ASN C N   1 
ATOM   5286  C CA  . ASN C  1 254 ? 149.638 158.024 229.336 1.00 153.96 ? 256 ASN C CA  1 
ATOM   5287  C C   . ASN C  1 254 ? 150.203 157.125 230.426 1.00 159.01 ? 256 ASN C C   1 
ATOM   5288  O O   . ASN C  1 254 ? 149.494 156.820 231.390 1.00 162.90 ? 256 ASN C O   1 
ATOM   5289  C CB  . ASN C  1 254 ? 148.854 157.190 228.324 1.00 150.95 ? 256 ASN C CB  1 
ATOM   5290  C CG  . ASN C  1 254 ? 148.616 157.929 227.023 1.00 151.64 ? 256 ASN C CG  1 
ATOM   5291  O OD1 . ASN C  1 254 ? 149.535 158.518 226.453 1.00 147.27 ? 256 ASN C OD1 1 
ATOM   5292  N ND2 . ASN C  1 254 ? 147.378 157.904 226.546 1.00 157.62 ? 256 ASN C ND2 1 
ATOM   5293  N N   . ASP C  1 255 ? 151.455 156.689 230.293 1.00 158.37 ? 257 ASP C N   1 
ATOM   5294  C CA  . ASP C  1 255 ? 152.130 155.903 231.319 1.00 160.45 ? 257 ASP C CA  1 
ATOM   5295  C C   . ASP C  1 255 ? 153.011 156.748 232.226 1.00 156.55 ? 257 ASP C C   1 
ATOM   5296  O O   . ASP C  1 255 ? 153.052 156.511 233.437 1.00 159.81 ? 257 ASP C O   1 
ATOM   5297  C CB  . ASP C  1 255 ? 152.979 154.803 230.675 1.00 161.48 ? 257 ASP C CB  1 
ATOM   5298  C CG  . ASP C  1 255 ? 152.139 153.717 230.038 1.00 164.80 ? 257 ASP C CG  1 
ATOM   5299  O OD1 . ASP C  1 255 ? 150.895 153.813 230.097 1.00 167.99 ? 257 ASP C OD1 1 
ATOM   5300  O OD2 . ASP C  1 255 ? 152.723 152.769 229.472 1.00 164.26 ? 257 ASP C OD2 1 
ATOM   5301  N N   . TYR C  1 256 ? 153.726 157.724 231.661 1.00 148.57 ? 258 TYR C N   1 
ATOM   5302  C CA  . TYR C  1 256 ? 154.612 158.561 232.464 1.00 149.56 ? 258 TYR C CA  1 
ATOM   5303  C C   . TYR C  1 256 ? 153.823 159.334 233.512 1.00 152.32 ? 258 TYR C C   1 
ATOM   5304  O O   . TYR C  1 256 ? 154.219 159.395 234.681 1.00 149.95 ? 258 TYR C O   1 
ATOM   5305  C CB  . TYR C  1 256 ? 155.377 159.517 231.550 1.00 148.27 ? 258 TYR C CB  1 
ATOM   5306  C CG  . TYR C  1 256 ? 155.922 160.762 232.217 1.00 152.43 ? 258 TYR C CG  1 
ATOM   5307  C CD1 . TYR C  1 256 ? 156.727 160.678 233.347 1.00 152.91 ? 258 TYR C CD1 1 
ATOM   5308  C CD2 . TYR C  1 256 ? 155.617 162.022 231.725 1.00 152.61 ? 258 TYR C CD2 1 
ATOM   5309  C CE1 . TYR C  1 256 ? 157.228 161.814 233.952 1.00 153.49 ? 258 TYR C CE1 1 
ATOM   5310  C CE2 . TYR C  1 256 ? 156.112 163.162 232.324 1.00 153.77 ? 258 TYR C CE2 1 
ATOM   5311  C CZ  . TYR C  1 256 ? 156.914 163.053 233.437 1.00 155.39 ? 258 TYR C CZ  1 
ATOM   5312  O OH  . TYR C  1 256 ? 157.408 164.189 234.034 1.00 154.47 ? 258 TYR C OH  1 
ATOM   5313  N N   . LYS C  1 257 ? 152.698 159.927 233.110 1.00 153.28 ? 259 LYS C N   1 
ATOM   5314  C CA  . LYS C  1 257 ? 151.827 160.609 234.056 1.00 153.82 ? 259 LYS C CA  1 
ATOM   5315  C C   . LYS C  1 257 ? 151.167 159.640 235.026 1.00 158.17 ? 259 LYS C C   1 
ATOM   5316  O O   . LYS C  1 257 ? 150.876 160.021 236.165 1.00 156.81 ? 259 LYS C O   1 
ATOM   5317  C CB  . LYS C  1 257 ? 150.758 161.398 233.299 1.00 148.08 ? 259 LYS C CB  1 
ATOM   5318  C CG  . LYS C  1 257 ? 149.858 162.258 234.168 1.00 142.53 ? 259 LYS C CG  1 
ATOM   5319  C CD  . LYS C  1 257 ? 148.562 162.627 233.450 1.00 144.08 ? 259 LYS C CD  1 
ATOM   5320  C CE  . LYS C  1 257 ? 148.813 163.331 232.121 1.00 144.42 ? 259 LYS C CE  1 
ATOM   5321  N NZ  . LYS C  1 257 ? 148.865 162.395 230.961 1.00 148.17 ? 259 LYS C NZ  1 
ATOM   5322  N N   . ASP C  1 258 ? 150.933 158.399 234.604 1.00 160.64 ? 260 ASP C N   1 
ATOM   5323  C CA  . ASP C  1 258 ? 150.203 157.422 235.401 1.00 164.24 ? 260 ASP C CA  1 
ATOM   5324  C C   . ASP C  1 258 ? 151.122 156.453 236.135 1.00 164.88 ? 260 ASP C C   1 
ATOM   5325  O O   . ASP C  1 258 ? 150.631 155.528 236.790 1.00 166.81 ? 260 ASP C O   1 
ATOM   5326  C CB  . ASP C  1 258 ? 149.230 156.650 234.509 1.00 167.96 ? 260 ASP C CB  1 
ATOM   5327  C CG  . ASP C  1 258 ? 147.983 157.448 234.180 1.00 167.52 ? 260 ASP C CG  1 
ATOM   5328  O OD1 . ASP C  1 258 ? 147.709 158.442 234.885 1.00 165.55 ? 260 ASP C OD1 1 
ATOM   5329  O OD2 . ASP C  1 258 ? 147.279 157.085 233.215 1.00 166.69 ? 260 ASP C OD2 1 
ATOM   5330  N N   . ALA C  1 259 ? 152.439 156.640 236.036 1.00 162.90 ? 261 ALA C N   1 
ATOM   5331  C CA  . ALA C  1 259 ? 153.438 155.816 236.717 1.00 164.45 ? 261 ALA C CA  1 
ATOM   5332  C C   . ALA C  1 259 ? 153.383 154.351 236.297 1.00 167.15 ? 261 ALA C C   1 
ATOM   5333  O O   . ALA C  1 259 ? 153.821 153.473 237.045 1.00 162.33 ? 261 ALA C O   1 
ATOM   5334  C CB  . ALA C  1 259 ? 153.310 155.926 238.242 1.00 156.52 ? 261 ALA C CB  1 
ATOM   5335  N N   . ASN C  1 260 ? 152.855 154.059 235.111 1.00 167.66 ? 262 ASN C N   1 
ATOM   5336  C CA  . ASN C  1 260 ? 152.820 152.682 234.640 1.00 165.06 ? 262 ASN C CA  1 
ATOM   5337  C C   . ASN C  1 260 ? 154.214 152.209 234.250 1.00 172.00 ? 262 ASN C C   1 
ATOM   5338  O O   . ASN C  1 260 ? 155.041 152.989 233.770 1.00 175.24 ? 262 ASN C O   1 
ATOM   5339  C CB  . ASN C  1 260 ? 151.875 152.548 233.445 1.00 166.24 ? 262 ASN C CB  1 
ATOM   5340  C CG  . ASN C  1 260 ? 150.554 153.251 233.664 1.00 168.76 ? 262 ASN C CG  1 
ATOM   5341  O OD1 . ASN C  1 260 ? 150.219 153.630 234.785 1.00 169.83 ? 262 ASN C OD1 1 
ATOM   5342  N ND2 . ASN C  1 260 ? 149.794 153.431 232.590 1.00 169.28 ? 262 ASN C ND2 1 
ATOM   5343  N N   . ASP C  1 261 ? 154.467 150.916 234.463 1.00 176.27 ? 263 ASP C N   1 
ATOM   5344  C CA  . ASP C  1 261 ? 155.653 150.225 233.954 1.00 180.55 ? 263 ASP C CA  1 
ATOM   5345  C C   . ASP C  1 261 ? 156.929 150.894 234.488 1.00 178.31 ? 263 ASP C C   1 
ATOM   5346  O O   . ASP C  1 261 ? 157.692 151.548 233.774 1.00 179.32 ? 263 ASP C O   1 
ATOM   5347  C CB  . ASP C  1 261 ? 155.588 150.166 232.417 1.00 184.77 ? 263 ASP C CB  1 
ATOM   5348  C CG  . ASP C  1 261 ? 156.929 149.891 231.760 1.00 188.56 ? 263 ASP C CG  1 
ATOM   5349  O OD1 . ASP C  1 261 ? 157.198 150.480 230.692 1.00 184.18 ? 263 ASP C OD1 1 
ATOM   5350  O OD2 . ASP C  1 261 ? 157.696 149.060 232.287 1.00 191.16 ? 263 ASP C OD2 1 
ATOM   5351  N N   . ILE C  1 262 ? 157.104 150.763 235.803 1.00 174.39 ? 264 ILE C N   1 
ATOM   5352  C CA  . ILE C  1 262 ? 158.287 151.269 236.492 1.00 169.27 ? 264 ILE C CA  1 
ATOM   5353  C C   . ILE C  1 262 ? 158.744 150.239 237.513 1.00 169.48 ? 264 ILE C C   1 
ATOM   5354  O O   . ILE C  1 262 ? 157.932 149.481 238.054 1.00 174.78 ? 264 ILE C O   1 
ATOM   5355  C CB  . ILE C  1 262 ? 158.026 152.619 237.195 1.00 168.48 ? 264 ILE C CB  1 
ATOM   5356  C CG1 . ILE C  1 262 ? 156.863 152.501 238.181 1.00 169.69 ? 264 ILE C CG1 1 
ATOM   5357  C CG2 . ILE C  1 262 ? 157.754 153.711 236.187 1.00 170.22 ? 264 ILE C CG2 1 
ATOM   5358  C CD1 . ILE C  1 262 ? 156.486 153.814 238.831 1.00 163.32 ? 264 ILE C CD1 1 
ATOM   5359  N N   . ASP C  1 263 ? 160.049 150.206 237.770 1.00 165.31 ? 265 ASP C N   1 
ATOM   5360  C CA  . ASP C  1 263 ? 160.554 149.485 238.928 1.00 169.24 ? 265 ASP C CA  1 
ATOM   5361  C C   . ASP C  1 263 ? 160.226 150.254 240.202 1.00 171.60 ? 265 ASP C C   1 
ATOM   5362  O O   . ASP C  1 263 ? 160.162 151.486 240.213 1.00 173.06 ? 265 ASP C O   1 
ATOM   5363  C CB  . ASP C  1 263 ? 162.064 149.274 238.821 1.00 169.20 ? 265 ASP C CB  1 
ATOM   5364  C CG  . ASP C  1 263 ? 162.434 148.197 237.823 1.00 171.24 ? 265 ASP C CG  1 
ATOM   5365  O OD1 . ASP C  1 263 ? 161.572 147.347 237.517 1.00 171.34 ? 265 ASP C OD1 1 
ATOM   5366  O OD2 . ASP C  1 263 ? 163.586 148.201 237.341 1.00 173.83 ? 265 ASP C OD2 1 
ATOM   5367  N N   . VAL C  1 264 ? 160.013 149.513 241.286 1.00 172.12 ? 266 VAL C N   1 
ATOM   5368  C CA  . VAL C  1 264 ? 159.710 150.099 242.581 1.00 174.73 ? 266 VAL C CA  1 
ATOM   5369  C C   . VAL C  1 264 ? 160.855 149.910 243.569 1.00 177.35 ? 266 VAL C C   1 
ATOM   5370  O O   . VAL C  1 264 ? 161.158 150.816 244.347 1.00 174.79 ? 266 VAL C O   1 
ATOM   5371  C CB  . VAL C  1 264 ? 158.384 149.542 243.148 1.00 174.77 ? 266 VAL C CB  1 
ATOM   5372  C CG1 . VAL C  1 264 ? 157.243 149.831 242.188 1.00 171.79 ? 266 VAL C CG1 1 
ATOM   5373  C CG2 . VAL C  1 264 ? 158.481 148.045 243.405 1.00 174.63 ? 266 VAL C CG2 1 
ATOM   5374  N N   . ASN C  1 265 ? 161.513 148.749 243.548 1.00 182.27 ? 267 ASN C N   1 
ATOM   5375  C CA  . ASN C  1 265 ? 162.649 148.514 244.429 1.00 184.37 ? 267 ASN C CA  1 
ATOM   5376  C C   . ASN C  1 265 ? 163.843 149.397 244.098 1.00 182.83 ? 267 ASN C C   1 
ATOM   5377  O O   . ASN C  1 265 ? 164.711 149.585 244.958 1.00 181.59 ? 267 ASN C O   1 
ATOM   5378  C CB  . ASN C  1 265 ? 163.062 147.043 244.369 1.00 184.57 ? 267 ASN C CB  1 
ATOM   5379  C CG  . ASN C  1 265 ? 163.782 146.691 243.079 1.00 188.31 ? 267 ASN C CG  1 
ATOM   5380  O OD1 . ASN C  1 265 ? 163.557 147.309 242.038 1.00 185.08 ? 267 ASN C OD1 1 
ATOM   5381  N ND2 . ASN C  1 265 ? 164.657 145.695 243.145 1.00 187.83 ? 267 ASN C ND2 1 
ATOM   5382  N N   . LYS C  1 266 ? 163.906 149.938 242.886 1.00 178.63 ? 268 LYS C N   1 
ATOM   5383  C CA  . LYS C  1 266 ? 165.026 150.751 242.430 1.00 175.62 ? 268 LYS C CA  1 
ATOM   5384  C C   . LYS C  1 266 ? 164.719 152.238 242.392 1.00 173.10 ? 268 LYS C C   1 
ATOM   5385  O O   . LYS C  1 266 ? 165.602 153.050 242.680 1.00 170.36 ? 268 LYS C O   1 
ATOM   5386  C CB  . LYS C  1 266 ? 165.471 150.282 241.043 1.00 173.01 ? 268 LYS C CB  1 
ATOM   5387  C CG  . LYS C  1 266 ? 166.830 150.795 240.606 1.00 170.42 ? 268 LYS C CG  1 
ATOM   5388  C CD  . LYS C  1 266 ? 167.061 150.506 239.132 1.00 162.91 ? 268 LYS C CD  1 
ATOM   5389  C CE  . LYS C  1 266 ? 165.755 150.562 238.355 1.00 159.38 ? 268 LYS C CE  1 
ATOM   5390  N NZ  . LYS C  1 266 ? 165.159 151.929 238.352 1.00 156.84 ? 268 LYS C NZ  1 
ATOM   5391  N N   . TRP C  1 267 ? 163.492 152.624 242.033 1.00 172.69 ? 269 TRP C N   1 
ATOM   5392  C CA  . TRP C  1 267 ? 163.089 154.018 242.191 1.00 168.24 ? 269 TRP C CA  1 
ATOM   5393  C C   . TRP C  1 267 ? 163.136 154.441 243.652 1.00 172.60 ? 269 TRP C C   1 
ATOM   5394  O O   . TRP C  1 267 ? 163.628 155.528 243.975 1.00 171.27 ? 269 TRP C O   1 
ATOM   5395  C CB  . TRP C  1 267 ? 161.691 154.239 241.618 1.00 161.43 ? 269 TRP C CB  1 
ATOM   5396  C CG  . TRP C  1 267 ? 161.635 155.281 240.547 1.00 152.29 ? 269 TRP C CG  1 
ATOM   5397  C CD1 . TRP C  1 267 ? 161.229 156.575 240.692 1.00 151.42 ? 269 TRP C CD1 1 
ATOM   5398  C CD2 . TRP C  1 267 ? 161.990 155.125 239.169 1.00 149.26 ? 269 TRP C CD2 1 
ATOM   5399  N NE1 . TRP C  1 267 ? 161.311 157.236 239.493 1.00 142.78 ? 269 TRP C NE1 1 
ATOM   5400  C CE2 . TRP C  1 267 ? 161.775 156.368 238.541 1.00 144.40 ? 269 TRP C CE2 1 
ATOM   5401  C CE3 . TRP C  1 267 ? 162.469 154.058 238.406 1.00 152.38 ? 269 TRP C CE3 1 
ATOM   5402  C CZ2 . TRP C  1 267 ? 162.021 156.572 237.190 1.00 140.55 ? 269 TRP C CZ2 1 
ATOM   5403  C CZ3 . TRP C  1 267 ? 162.711 154.263 237.065 1.00 143.62 ? 269 TRP C CZ3 1 
ATOM   5404  C CH2 . TRP C  1 267 ? 162.488 155.511 236.471 1.00 136.85 ? 269 TRP C CH2 1 
ATOM   5405  N N   . LYS C  1 268 ? 162.632 153.593 244.552 1.00 175.22 ? 270 LYS C N   1 
ATOM   5406  C CA  . LYS C  1 268 ? 162.682 153.906 245.975 1.00 173.18 ? 270 LYS C CA  1 
ATOM   5407  C C   . LYS C  1 268 ? 164.110 153.999 246.493 1.00 174.39 ? 270 LYS C C   1 
ATOM   5408  O O   . LYS C  1 268 ? 164.335 154.594 247.551 1.00 172.60 ? 270 LYS C O   1 
ATOM   5409  C CB  . LYS C  1 268 ? 161.907 152.859 246.775 1.00 169.43 ? 270 LYS C CB  1 
ATOM   5410  C CG  . LYS C  1 268 ? 160.403 152.891 246.559 1.00 164.35 ? 270 LYS C CG  1 
ATOM   5411  C CD  . LYS C  1 268 ? 159.694 153.638 247.674 1.00 156.28 ? 270 LYS C CD  1 
ATOM   5412  C CE  . LYS C  1 268 ? 158.475 152.868 248.155 1.00 148.28 ? 270 LYS C CE  1 
ATOM   5413  N NZ  . LYS C  1 268 ? 157.435 152.746 247.098 1.00 137.26 ? 270 LYS C NZ  1 
ATOM   5414  N N   . ALA C  1 269 ? 165.076 153.417 245.781 1.00 176.80 ? 271 ALA C N   1 
ATOM   5415  C CA  . ALA C  1 269 ? 166.470 153.516 246.197 1.00 177.06 ? 271 ALA C CA  1 
ATOM   5416  C C   . ALA C  1 269 ? 167.017 154.920 245.963 1.00 177.24 ? 271 ALA C C   1 
ATOM   5417  O O   . ALA C  1 269 ? 167.455 155.594 246.902 1.00 175.96 ? 271 ALA C O   1 
ATOM   5418  C CB  . ALA C  1 269 ? 167.314 152.476 245.456 1.00 175.06 ? 271 ALA C CB  1 
ATOM   5419  N N   . LYS C  1 270 ? 166.999 155.376 244.709 1.00 176.03 ? 272 LYS C N   1 
ATOM   5420  C CA  . LYS C  1 270 ? 167.544 156.694 244.396 1.00 172.70 ? 272 LYS C CA  1 
ATOM   5421  C C   . LYS C  1 270 ? 166.647 157.807 244.929 1.00 168.61 ? 272 LYS C C   1 
ATOM   5422  O O   . LYS C  1 270 ? 167.143 158.825 245.426 1.00 164.10 ? 272 LYS C O   1 
ATOM   5423  C CB  . LYS C  1 270 ? 167.749 156.827 242.886 1.00 167.68 ? 272 LYS C CB  1 
ATOM   5424  C CG  . LYS C  1 270 ? 167.542 158.226 242.337 1.00 166.09 ? 272 LYS C CG  1 
ATOM   5425  C CD  . LYS C  1 270 ? 167.759 158.273 240.833 1.00 166.30 ? 272 LYS C CD  1 
ATOM   5426  C CE  . LYS C  1 270 ? 168.989 157.485 240.413 1.00 161.42 ? 272 LYS C CE  1 
ATOM   5427  N NZ  . LYS C  1 270 ? 169.120 157.421 238.931 1.00 149.19 ? 272 LYS C NZ  1 
ATOM   5428  N N   . LEU C  1 271 ? 165.327 157.630 244.847 1.00 166.66 ? 273 LEU C N   1 
ATOM   5429  C CA  . LEU C  1 271 ? 164.395 158.641 245.332 1.00 164.11 ? 273 LEU C CA  1 
ATOM   5430  C C   . LEU C  1 271 ? 164.114 158.533 246.825 1.00 164.55 ? 273 LEU C C   1 
ATOM   5431  O O   . LEU C  1 271 ? 163.364 159.360 247.355 1.00 162.92 ? 273 LEU C O   1 
ATOM   5432  C CB  . LEU C  1 271 ? 163.069 158.566 244.567 1.00 164.16 ? 273 LEU C CB  1 
ATOM   5433  C CG  . LEU C  1 271 ? 162.897 159.353 243.264 1.00 161.09 ? 273 LEU C CG  1 
ATOM   5434  C CD1 . LEU C  1 271 ? 162.469 160.780 243.569 1.00 155.28 ? 273 LEU C CD1 1 
ATOM   5435  C CD2 . LEU C  1 271 ? 164.154 159.345 242.412 1.00 157.69 ? 273 LEU C CD2 1 
ATOM   5436  N N   . GLY C  1 272 ? 164.683 157.548 247.510 1.00 165.32 ? 274 GLY C N   1 
ATOM   5437  C CA  . GLY C  1 272 ? 164.453 157.391 248.935 1.00 161.27 ? 274 GLY C CA  1 
ATOM   5438  C C   . GLY C  1 272 ? 163.064 156.875 249.254 1.00 155.82 ? 274 GLY C C   1 
ATOM   5439  O O   . GLY C  1 272 ? 162.645 156.861 250.411 1.00 139.25 ? 274 GLY C O   1 
ATOM   5440  N N   . GLN D  2 1   ? 143.682 127.805 144.576 1.00 133.58 ? 35  GLN D N   1 
ATOM   5441  C CA  . GLN D  2 1   ? 142.431 128.173 145.230 1.00 137.22 ? 35  GLN D CA  1 
ATOM   5442  C C   . GLN D  2 1   ? 142.359 127.687 146.682 1.00 129.92 ? 35  GLN D C   1 
ATOM   5443  O O   . GLN D  2 1   ? 142.751 126.569 147.004 1.00 127.99 ? 35  GLN D O   1 
ATOM   5444  C CB  . GLN D  2 1   ? 141.236 127.655 144.408 1.00 140.59 ? 35  GLN D CB  1 
ATOM   5445  C CG  . GLN D  2 1   ? 140.655 126.274 144.765 1.00 138.57 ? 35  GLN D CG  1 
ATOM   5446  C CD  . GLN D  2 1   ? 141.650 125.112 144.677 1.00 143.24 ? 35  GLN D CD  1 
ATOM   5447  O OE1 . GLN D  2 1   ? 142.866 125.296 144.640 1.00 143.16 ? 35  GLN D OE1 1 
ATOM   5448  N NE2 . GLN D  2 1   ? 141.116 123.897 144.641 1.00 144.34 ? 35  GLN D NE2 1 
ATOM   5449  N N   . LEU D  2 2   ? 141.877 128.560 147.562 1.00 122.36 ? 36  LEU D N   1 
ATOM   5450  C CA  . LEU D  2 2   ? 141.823 128.232 148.979 1.00 113.94 ? 36  LEU D CA  1 
ATOM   5451  C C   . LEU D  2 2   ? 140.471 127.629 149.339 1.00 119.22 ? 36  LEU D C   1 
ATOM   5452  O O   . LEU D  2 2   ? 139.420 128.233 149.108 1.00 127.77 ? 36  LEU D O   1 
ATOM   5453  C CB  . LEU D  2 2   ? 142.087 129.482 149.819 1.00 106.07 ? 36  LEU D CB  1 
ATOM   5454  C CG  . LEU D  2 2   ? 142.500 129.251 151.271 1.00 98.09  ? 36  LEU D CG  1 
ATOM   5455  C CD1 . LEU D  2 2   ? 143.959 128.844 151.349 1.00 109.69 ? 36  LEU D CD1 1 
ATOM   5456  C CD2 . LEU D  2 2   ? 142.254 130.503 152.088 1.00 96.61  ? 36  LEU D CD2 1 
ATOM   5457  N N   . THR D  2 3   ? 140.504 126.427 149.908 1.00 112.97 ? 37  THR D N   1 
ATOM   5458  C CA  . THR D  2 3   ? 139.295 125.722 150.302 1.00 112.37 ? 37  THR D CA  1 
ATOM   5459  C C   . THR D  2 3   ? 139.433 125.239 151.737 1.00 112.00 ? 37  THR D C   1 
ATOM   5460  O O   . THR D  2 3   ? 140.510 124.818 152.166 1.00 114.68 ? 37  THR D O   1 
ATOM   5461  C CB  . THR D  2 3   ? 139.003 124.525 149.384 1.00 117.24 ? 37  THR D CB  1 
ATOM   5462  O OG1 . THR D  2 3   ? 140.101 123.606 149.432 1.00 123.74 ? 37  THR D OG1 1 
ATOM   5463  C CG2 . THR D  2 3   ? 138.794 124.986 147.951 1.00 121.16 ? 37  THR D CG2 1 
ATOM   5464  N N   . THR D  2 4   ? 138.328 125.304 152.474 1.00 110.81 ? 38  THR D N   1 
ATOM   5465  C CA  . THR D  2 4   ? 138.263 124.810 153.841 1.00 110.78 ? 38  THR D CA  1 
ATOM   5466  C C   . THR D  2 4   ? 137.255 123.675 153.910 1.00 113.27 ? 38  THR D C   1 
ATOM   5467  O O   . THR D  2 4   ? 136.269 123.663 153.167 1.00 115.96 ? 38  THR D O   1 
ATOM   5468  C CB  . THR D  2 4   ? 137.869 125.913 154.829 1.00 104.92 ? 38  THR D CB  1 
ATOM   5469  O OG1 . THR D  2 4   ? 136.449 126.094 154.803 1.00 108.16 ? 38  THR D OG1 1 
ATOM   5470  C CG2 . THR D  2 4   ? 138.550 127.221 154.467 1.00 107.19 ? 38  THR D CG2 1 
ATOM   5471  N N   . GLU D  2 5   ? 137.506 122.723 154.803 1.00 112.54 ? 39  GLU D N   1 
ATOM   5472  C CA  . GLU D  2 5   ? 136.671 121.539 154.937 1.00 115.34 ? 39  GLU D CA  1 
ATOM   5473  C C   . GLU D  2 5   ? 136.453 121.240 156.410 1.00 117.15 ? 39  GLU D C   1 
ATOM   5474  O O   . GLU D  2 5   ? 137.418 121.074 157.163 1.00 121.39 ? 39  GLU D O   1 
ATOM   5475  C CB  . GLU D  2 5   ? 137.313 120.335 154.243 1.00 119.42 ? 39  GLU D CB  1 
ATOM   5476  C CG  . GLU D  2 5   ? 136.524 119.046 154.372 1.00 128.44 ? 39  GLU D CG  1 
ATOM   5477  C CD  . GLU D  2 5   ? 137.119 117.921 153.553 1.00 147.06 ? 39  GLU D CD  1 
ATOM   5478  O OE1 . GLU D  2 5   ? 138.361 117.793 153.534 1.00 148.63 ? 39  GLU D OE1 1 
ATOM   5479  O OE2 . GLU D  2 5   ? 136.348 117.165 152.925 1.00 159.15 ? 39  GLU D OE2 1 
ATOM   5480  N N   . SER D  2 6   ? 135.189 121.174 156.818 1.00 114.57 ? 40  SER D N   1 
ATOM   5481  C CA  . SER D  2 6   ? 134.822 120.813 158.180 1.00 111.17 ? 40  SER D CA  1 
ATOM   5482  C C   . SER D  2 6   ? 135.068 119.322 158.369 1.00 116.61 ? 40  SER D C   1 
ATOM   5483  O O   . SER D  2 6   ? 135.030 118.556 157.401 1.00 122.50 ? 40  SER D O   1 
ATOM   5484  C CB  . SER D  2 6   ? 133.362 121.162 158.463 1.00 111.12 ? 40  SER D CB  1 
ATOM   5485  O OG  . SER D  2 6   ? 132.491 120.401 157.646 1.00 121.45 ? 40  SER D OG  1 
ATOM   5486  N N   . MET D  2 7   ? 135.318 118.916 159.607 1.00 111.83 ? 41  MET D N   1 
ATOM   5487  C CA  . MET D  2 7   ? 135.635 117.523 159.918 1.00 112.03 ? 41  MET D CA  1 
ATOM   5488  C C   . MET D  2 7   ? 135.216 117.199 161.343 1.00 107.99 ? 41  MET D C   1 
ATOM   5489  O O   . MET D  2 7   ? 135.949 117.538 162.292 1.00 105.65 ? 41  MET D O   1 
ATOM   5490  C CB  . MET D  2 7   ? 137.129 117.259 159.730 1.00 115.08 ? 41  MET D CB  1 
ATOM   5491  C CG  . MET D  2 7   ? 137.469 115.816 159.405 1.00 121.42 ? 41  MET D CG  1 
ATOM   5492  S SD  . MET D  2 7   ? 136.915 115.333 157.760 1.00 143.60 ? 41  MET D SD  1 
ATOM   5493  C CE  . MET D  2 7   ? 136.107 113.776 158.117 1.00 133.10 ? 41  MET D CE  1 
ATOM   5494  N N   . PRO D  2 8   ? 134.064 116.556 161.557 1.00 106.22 ? 42  PRO D N   1 
ATOM   5495  C CA  . PRO D  2 8   ? 133.071 116.139 160.560 1.00 108.05 ? 42  PRO D CA  1 
ATOM   5496  C C   . PRO D  2 8   ? 132.127 117.274 160.183 1.00 112.53 ? 42  PRO D C   1 
ATOM   5497  O O   . PRO D  2 8   ? 132.126 118.322 160.822 1.00 115.62 ? 42  PRO D O   1 
ATOM   5498  C CB  . PRO D  2 8   ? 132.344 114.993 161.269 1.00 104.12 ? 42  PRO D CB  1 
ATOM   5499  C CG  . PRO D  2 8   ? 132.397 115.364 162.725 1.00 102.09 ? 42  PRO D CG  1 
ATOM   5500  C CD  . PRO D  2 8   ? 133.663 116.172 162.922 1.00 102.20 ? 42  PRO D CD  1 
ATOM   5501  N N   . PHE D  2 9   ? 131.315 117.093 159.139 1.00 115.43 ? 43  PHE D N   1 
ATOM   5502  C CA  . PHE D  2 9   ? 130.374 118.138 158.745 1.00 114.07 ? 43  PHE D CA  1 
ATOM   5503  C C   . PHE D  2 9   ? 129.273 118.310 159.783 1.00 114.07 ? 43  PHE D C   1 
ATOM   5504  O O   . PHE D  2 9   ? 128.858 119.437 160.078 1.00 111.50 ? 43  PHE D O   1 
ATOM   5505  C CB  . PHE D  2 9   ? 129.778 117.818 157.375 1.00 114.90 ? 43  PHE D CB  1 
ATOM   5506  C CG  . PHE D  2 9   ? 129.009 118.956 156.768 1.00 117.90 ? 43  PHE D CG  1 
ATOM   5507  C CD1 . PHE D  2 9   ? 127.660 119.120 157.034 1.00 117.50 ? 43  PHE D CD1 1 
ATOM   5508  C CD2 . PHE D  2 9   ? 129.638 119.866 155.936 1.00 121.58 ? 43  PHE D CD2 1 
ATOM   5509  C CE1 . PHE D  2 9   ? 126.952 120.168 156.478 1.00 120.22 ? 43  PHE D CE1 1 
ATOM   5510  C CE2 . PHE D  2 9   ? 128.935 120.916 155.377 1.00 121.07 ? 43  PHE D CE2 1 
ATOM   5511  C CZ  . PHE D  2 9   ? 127.591 121.067 155.649 1.00 121.51 ? 43  PHE D CZ  1 
ATOM   5512  N N   . ASN D  2 10  ? 128.785 117.209 160.345 1.00 116.17 ? 44  ASN D N   1 
ATOM   5513  C CA  . ASN D  2 10  ? 127.758 117.238 161.375 1.00 114.37 ? 44  ASN D CA  1 
ATOM   5514  C C   . ASN D  2 10  ? 128.355 116.776 162.696 1.00 116.46 ? 44  ASN D C   1 
ATOM   5515  O O   . ASN D  2 10  ? 128.912 115.678 162.785 1.00 123.93 ? 44  ASN D O   1 
ATOM   5516  C CB  . ASN D  2 10  ? 126.571 116.352 160.993 1.00 118.30 ? 44  ASN D CB  1 
ATOM   5517  C CG  . ASN D  2 10  ? 126.015 116.685 159.625 1.00 122.85 ? 44  ASN D CG  1 
ATOM   5518  O OD1 . ASN D  2 10  ? 125.381 117.722 159.435 1.00 126.30 ? 44  ASN D OD1 1 
ATOM   5519  N ND2 . ASN D  2 10  ? 126.251 115.805 158.660 1.00 124.31 ? 44  ASN D ND2 1 
ATOM   5520  N N   . VAL D  2 11  ? 128.233 117.616 163.719 1.00 110.58 ? 45  VAL D N   1 
ATOM   5521  C CA  . VAL D  2 11  ? 128.854 117.369 165.013 1.00 109.44 ? 45  VAL D CA  1 
ATOM   5522  C C   . VAL D  2 11  ? 127.770 117.259 166.073 1.00 120.87 ? 45  VAL D C   1 
ATOM   5523  O O   . VAL D  2 11  ? 126.840 118.071 166.114 1.00 130.50 ? 45  VAL D O   1 
ATOM   5524  C CB  . VAL D  2 11  ? 129.861 118.476 165.384 1.00 106.36 ? 45  VAL D CB  1 
ATOM   5525  C CG1 . VAL D  2 11  ? 131.196 118.219 164.716 1.00 114.52 ? 45  VAL D CG1 1 
ATOM   5526  C CG2 . VAL D  2 11  ? 129.321 119.838 164.989 1.00 109.47 ? 45  VAL D CG2 1 
ATOM   5527  N N   . ALA D  2 12  ? 127.888 116.247 166.924 1.00 126.79 ? 46  ALA D N   1 
ATOM   5528  C CA  . ALA D  2 12  ? 127.032 116.138 168.093 1.00 144.82 ? 46  ALA D CA  1 
ATOM   5529  C C   . ALA D  2 12  ? 127.341 117.263 169.073 1.00 150.19 ? 46  ALA D C   1 
ATOM   5530  O O   . ALA D  2 12  ? 128.476 117.738 169.165 1.00 151.42 ? 46  ALA D O   1 
ATOM   5531  C CB  . ALA D  2 12  ? 127.221 114.783 168.772 1.00 149.69 ? 46  ALA D CB  1 
ATOM   5532  N N   . GLU D  2 13  ? 126.314 117.696 169.801 1.00 146.62 ? 47  GLU D N   1 
ATOM   5533  C CA  . GLU D  2 13  ? 126.496 118.761 170.778 1.00 139.71 ? 47  GLU D CA  1 
ATOM   5534  C C   . GLU D  2 13  ? 127.489 118.338 171.853 1.00 146.52 ? 47  GLU D C   1 
ATOM   5535  O O   . GLU D  2 13  ? 127.459 117.206 172.342 1.00 153.77 ? 47  GLU D O   1 
ATOM   5536  C CB  . GLU D  2 13  ? 125.159 119.136 171.416 1.00 145.80 ? 47  GLU D CB  1 
ATOM   5537  C CG  . GLU D  2 13  ? 124.564 120.429 170.887 1.00 149.65 ? 47  GLU D CG  1 
ATOM   5538  C CD  . GLU D  2 13  ? 123.484 120.986 171.793 1.00 154.89 ? 47  GLU D CD  1 
ATOM   5539  O OE1 . GLU D  2 13  ? 122.337 120.497 171.724 1.00 156.62 ? 47  GLU D OE1 1 
ATOM   5540  O OE2 . GLU D  2 13  ? 123.784 121.911 172.577 1.00 152.88 ? 47  GLU D OE2 1 
ATOM   5541  N N   . GLY D  2 14  ? 128.376 119.262 172.219 1.00 142.96 ? 48  GLY D N   1 
ATOM   5542  C CA  . GLY D  2 14  ? 129.394 119.010 173.210 1.00 142.07 ? 48  GLY D CA  1 
ATOM   5543  C C   . GLY D  2 14  ? 130.653 118.356 172.681 1.00 137.91 ? 48  GLY D C   1 
ATOM   5544  O O   . GLY D  2 14  ? 131.612 118.187 173.441 1.00 139.85 ? 48  GLY D O   1 
ATOM   5545  N N   . LYS D  2 15  ? 130.679 117.985 171.405 1.00 133.76 ? 49  LYS D N   1 
ATOM   5546  C CA  . LYS D  2 15  ? 131.864 117.409 170.790 1.00 130.60 ? 49  LYS D CA  1 
ATOM   5547  C C   . LYS D  2 15  ? 132.723 118.530 170.207 1.00 131.50 ? 49  LYS D C   1 
ATOM   5548  O O   . LYS D  2 15  ? 132.495 119.715 170.464 1.00 135.86 ? 49  LYS D O   1 
ATOM   5549  C CB  . LYS D  2 15  ? 131.466 116.379 169.736 1.00 129.02 ? 49  LYS D CB  1 
ATOM   5550  C CG  . LYS D  2 15  ? 131.054 115.034 170.311 1.00 133.46 ? 49  LYS D CG  1 
ATOM   5551  C CD  . LYS D  2 15  ? 131.964 114.618 171.455 1.00 137.93 ? 49  LYS D CD  1 
ATOM   5552  C CE  . LYS D  2 15  ? 131.190 113.874 172.529 1.00 139.80 ? 49  LYS D CE  1 
ATOM   5553  N NZ  . LYS D  2 15  ? 130.234 112.896 171.943 1.00 142.82 ? 49  LYS D NZ  1 
ATOM   5554  N N   . GLU D  2 16  ? 133.726 118.167 169.412 1.00 124.89 ? 50  GLU D N   1 
ATOM   5555  C CA  . GLU D  2 16  ? 134.609 119.139 168.791 1.00 121.44 ? 50  GLU D CA  1 
ATOM   5556  C C   . GLU D  2 16  ? 134.570 118.994 167.276 1.00 117.13 ? 50  GLU D C   1 
ATOM   5557  O O   . GLU D  2 16  ? 134.253 117.925 166.744 1.00 120.40 ? 50  GLU D O   1 
ATOM   5558  C CB  . GLU D  2 16  ? 136.054 118.990 169.284 1.00 124.86 ? 50  GLU D CB  1 
ATOM   5559  C CG  . GLU D  2 16  ? 136.772 117.759 168.759 1.00 134.41 ? 50  GLU D CG  1 
ATOM   5560  C CD  . GLU D  2 16  ? 137.943 117.354 169.631 1.00 142.84 ? 50  GLU D CD  1 
ATOM   5561  O OE1 . GLU D  2 16  ? 138.443 118.211 170.389 1.00 143.02 ? 50  GLU D OE1 1 
ATOM   5562  O OE2 . GLU D  2 16  ? 138.366 116.182 169.555 1.00 146.00 ? 50  GLU D OE2 1 
ATOM   5563  N N   . VAL D  2 17  ? 134.890 120.086 166.589 1.00 112.62 ? 51  VAL D N   1 
ATOM   5564  C CA  . VAL D  2 17  ? 134.942 120.126 165.134 1.00 109.47 ? 51  VAL D CA  1 
ATOM   5565  C C   . VAL D  2 17  ? 136.259 120.766 164.720 1.00 106.95 ? 51  VAL D C   1 
ATOM   5566  O O   . VAL D  2 17  ? 136.732 121.709 165.363 1.00 108.85 ? 51  VAL D O   1 
ATOM   5567  C CB  . VAL D  2 17  ? 133.737 120.890 164.541 1.00 109.61 ? 51  VAL D CB  1 
ATOM   5568  C CG1 . VAL D  2 17  ? 133.706 122.328 165.038 1.00 111.87 ? 51  VAL D CG1 1 
ATOM   5569  C CG2 . VAL D  2 17  ? 133.763 120.843 163.021 1.00 110.85 ? 51  VAL D CG2 1 
ATOM   5570  N N   . LEU D  2 18  ? 136.863 120.238 163.660 1.00 103.21 ? 52  LEU D N   1 
ATOM   5571  C CA  . LEU D  2 18  ? 138.137 120.726 163.154 1.00 104.40 ? 52  LEU D CA  1 
ATOM   5572  C C   . LEU D  2 18  ? 137.981 121.122 161.693 1.00 108.41 ? 52  LEU D C   1 
ATOM   5573  O O   . LEU D  2 18  ? 137.536 120.315 160.871 1.00 111.90 ? 52  LEU D O   1 
ATOM   5574  C CB  . LEU D  2 18  ? 139.226 119.661 163.304 1.00 107.21 ? 52  LEU D CB  1 
ATOM   5575  C CG  . LEU D  2 18  ? 140.606 120.002 162.741 1.00 108.69 ? 52  LEU D CG  1 
ATOM   5576  C CD1 . LEU D  2 18  ? 141.213 121.176 163.488 1.00 106.65 ? 52  LEU D CD1 1 
ATOM   5577  C CD2 . LEU D  2 18  ? 141.522 118.791 162.810 1.00 110.93 ? 52  LEU D CD2 1 
ATOM   5578  N N   . LEU D  2 19  ? 138.346 122.361 161.376 1.00 102.97 ? 53  LEU D N   1 
ATOM   5579  C CA  . LEU D  2 19  ? 138.259 122.883 160.019 1.00 105.28 ? 53  LEU D CA  1 
ATOM   5580  C C   . LEU D  2 19  ? 139.635 122.807 159.371 1.00 109.97 ? 53  LEU D C   1 
ATOM   5581  O O   . LEU D  2 19  ? 140.567 123.491 159.804 1.00 107.45 ? 53  LEU D O   1 
ATOM   5582  C CB  . LEU D  2 19  ? 137.748 124.324 160.019 1.00 96.40  ? 53  LEU D CB  1 
ATOM   5583  C CG  . LEU D  2 19  ? 136.470 124.619 160.805 1.00 89.54  ? 53  LEU D CG  1 
ATOM   5584  C CD1 . LEU D  2 19  ? 136.109 126.089 160.695 1.00 86.73  ? 53  LEU D CD1 1 
ATOM   5585  C CD2 . LEU D  2 19  ? 135.325 123.754 160.314 1.00 97.48  ? 53  LEU D CD2 1 
ATOM   5586  N N   . LEU D  2 20  ? 139.758 121.984 158.335 1.00 112.74 ? 54  LEU D N   1 
ATOM   5587  C CA  . LEU D  2 20  ? 141.005 121.824 157.605 1.00 104.13 ? 54  LEU D CA  1 
ATOM   5588  C C   . LEU D  2 20  ? 141.133 122.895 156.529 1.00 105.50 ? 54  LEU D C   1 
ATOM   5589  O O   . LEU D  2 20  ? 140.142 123.435 156.033 1.00 110.13 ? 54  LEU D O   1 
ATOM   5590  C CB  . LEU D  2 20  ? 141.090 120.433 156.972 1.00 105.52 ? 54  LEU D CB  1 
ATOM   5591  C CG  . LEU D  2 20  ? 140.943 119.247 157.924 1.00 106.67 ? 54  LEU D CG  1 
ATOM   5592  C CD1 . LEU D  2 20  ? 141.152 117.937 157.184 1.00 113.73 ? 54  LEU D CD1 1 
ATOM   5593  C CD2 . LEU D  2 20  ? 141.919 119.372 159.082 1.00 109.67 ? 54  LEU D CD2 1 
ATOM   5594  N N   . VAL D  2 21  ? 142.378 123.199 156.174 1.00 103.48 ? 55  VAL D N   1 
ATOM   5595  C CA  . VAL D  2 21  ? 142.691 124.176 155.139 1.00 104.40 ? 55  VAL D CA  1 
ATOM   5596  C C   . VAL D  2 21  ? 143.567 123.503 154.093 1.00 111.81 ? 55  VAL D C   1 
ATOM   5597  O O   . VAL D  2 21  ? 144.556 122.843 154.430 1.00 116.14 ? 55  VAL D O   1 
ATOM   5598  C CB  . VAL D  2 21  ? 143.394 125.421 155.718 1.00 98.39  ? 55  VAL D CB  1 
ATOM   5599  C CG1 . VAL D  2 21  ? 143.629 126.453 154.630 1.00 100.67 ? 55  VAL D CG1 1 
ATOM   5600  C CG2 . VAL D  2 21  ? 142.577 126.014 156.852 1.00 97.81  ? 55  VAL D CG2 1 
ATOM   5601  N N   . HIS D  2 22  ? 143.204 123.669 152.824 1.00 113.49 ? 56  HIS D N   1 
ATOM   5602  C CA  . HIS D  2 22  ? 143.926 123.058 151.720 1.00 114.37 ? 56  HIS D CA  1 
ATOM   5603  C C   . HIS D  2 22  ? 144.436 124.135 150.773 1.00 118.69 ? 56  HIS D C   1 
ATOM   5604  O O   . HIS D  2 22  ? 143.881 125.234 150.692 1.00 120.58 ? 56  HIS D O   1 
ATOM   5605  C CB  . HIS D  2 22  ? 143.047 122.064 150.950 1.00 113.11 ? 56  HIS D CB  1 
ATOM   5606  C CG  . HIS D  2 22  ? 142.666 120.854 151.742 1.00 112.06 ? 56  HIS D CG  1 
ATOM   5607  N ND1 . HIS D  2 22  ? 143.515 119.783 151.920 1.00 115.29 ? 56  HIS D ND1 1 
ATOM   5608  C CD2 . HIS D  2 22  ? 141.525 120.543 152.402 1.00 113.59 ? 56  HIS D CD2 1 
ATOM   5609  C CE1 . HIS D  2 22  ? 142.915 118.866 152.656 1.00 120.68 ? 56  HIS D CE1 1 
ATOM   5610  N NE2 . HIS D  2 22  ? 141.706 119.302 152.962 1.00 122.61 ? 56  HIS D NE2 1 
ATOM   5611  N N   . ASN D  2 23  ? 145.506 123.793 150.053 1.00 118.08 ? 57  ASN D N   1 
ATOM   5612  C CA  . ASN D  2 23  ? 146.111 124.675 149.053 1.00 120.60 ? 57  ASN D CA  1 
ATOM   5613  C C   . ASN D  2 23  ? 146.488 126.026 149.654 1.00 115.88 ? 57  ASN D C   1 
ATOM   5614  O O   . ASN D  2 23  ? 146.276 127.078 149.048 1.00 113.37 ? 57  ASN D O   1 
ATOM   5615  C CB  . ASN D  2 23  ? 145.188 124.856 147.848 1.00 124.29 ? 57  ASN D CB  1 
ATOM   5616  C CG  . ASN D  2 23  ? 144.617 123.545 147.350 1.00 128.73 ? 57  ASN D CG  1 
ATOM   5617  O OD1 . ASN D  2 23  ? 145.280 122.510 147.391 1.00 130.31 ? 57  ASN D OD1 1 
ATOM   5618  N ND2 . ASN D  2 23  ? 143.375 123.582 146.881 1.00 128.80 ? 57  ASN D ND2 1 
ATOM   5619  N N   . LEU D  2 24  ? 147.041 125.997 150.858 1.00 112.24 ? 58  LEU D N   1 
ATOM   5620  C CA  . LEU D  2 24  ? 147.468 127.225 151.513 1.00 111.61 ? 58  LEU D CA  1 
ATOM   5621  C C   . LEU D  2 24  ? 148.620 127.847 150.730 1.00 120.44 ? 58  LEU D C   1 
ATOM   5622  O O   . LEU D  2 24  ? 149.566 127.139 150.365 1.00 129.03 ? 58  LEU D O   1 
ATOM   5623  C CB  . LEU D  2 24  ? 147.884 126.930 152.952 1.00 106.30 ? 58  LEU D CB  1 
ATOM   5624  C CG  . LEU D  2 24  ? 147.992 128.102 153.925 1.00 108.89 ? 58  LEU D CG  1 
ATOM   5625  C CD1 . LEU D  2 24  ? 146.619 128.689 154.193 1.00 109.18 ? 58  LEU D CD1 1 
ATOM   5626  C CD2 . LEU D  2 24  ? 148.629 127.637 155.221 1.00 112.52 ? 58  LEU D CD2 1 
ATOM   5627  N N   . PRO D  2 25  ? 148.570 129.154 150.433 1.00 118.03 ? 59  PRO D N   1 
ATOM   5628  C CA  . PRO D  2 25  ? 149.624 129.778 149.616 1.00 118.04 ? 59  PRO D CA  1 
ATOM   5629  C C   . PRO D  2 25  ? 151.024 129.595 150.183 1.00 124.16 ? 59  PRO D C   1 
ATOM   5630  O O   . PRO D  2 25  ? 151.196 129.353 151.381 1.00 122.77 ? 59  PRO D O   1 
ATOM   5631  C CB  . PRO D  2 25  ? 149.226 131.258 149.601 1.00 116.28 ? 59  PRO D CB  1 
ATOM   5632  C CG  . PRO D  2 25  ? 147.759 131.271 149.836 1.00 116.04 ? 59  PRO D CG  1 
ATOM   5633  C CD  . PRO D  2 25  ? 147.387 130.019 150.582 1.00 118.07 ? 59  PRO D CD  1 
ATOM   5634  N N   . GLN D  2 26  ? 152.032 129.703 149.313 1.00 127.38 ? 60  GLN D N   1 
ATOM   5635  C CA  . GLN D  2 26  ? 153.411 129.460 149.727 1.00 131.58 ? 60  GLN D CA  1 
ATOM   5636  C C   . GLN D  2 26  ? 153.875 130.470 150.771 1.00 130.67 ? 60  GLN D C   1 
ATOM   5637  O O   . GLN D  2 26  ? 154.184 130.097 151.908 1.00 127.53 ? 60  GLN D O   1 
ATOM   5638  C CB  . GLN D  2 26  ? 154.334 129.493 148.506 1.00 133.26 ? 60  GLN D CB  1 
ATOM   5639  C CG  . GLN D  2 26  ? 154.628 128.136 147.852 1.00 138.82 ? 60  GLN D CG  1 
ATOM   5640  C CD  . GLN D  2 26  ? 155.225 127.088 148.789 1.00 147.87 ? 60  GLN D CD  1 
ATOM   5641  O OE1 . GLN D  2 26  ? 155.469 127.338 149.970 1.00 145.04 ? 60  GLN D OE1 1 
ATOM   5642  N NE2 . GLN D  2 26  ? 155.462 125.898 148.251 1.00 156.43 ? 60  GLN D NE2 1 
ATOM   5643  N N   . GLN D  2 27  ? 153.931 131.747 150.406 1.00 130.13 ? 61  GLN D N   1 
ATOM   5644  C CA  . GLN D  2 27  ? 154.420 132.801 151.284 1.00 124.35 ? 61  GLN D CA  1 
ATOM   5645  C C   . GLN D  2 27  ? 153.240 133.467 151.977 1.00 120.53 ? 61  GLN D C   1 
ATOM   5646  O O   . GLN D  2 27  ? 152.326 133.965 151.311 1.00 126.19 ? 61  GLN D O   1 
ATOM   5647  C CB  . GLN D  2 27  ? 155.229 133.834 150.498 1.00 129.43 ? 61  GLN D CB  1 
ATOM   5648  C CG  . GLN D  2 27  ? 156.335 133.238 149.641 1.00 136.27 ? 61  GLN D CG  1 
ATOM   5649  C CD  . GLN D  2 27  ? 157.456 132.639 150.466 1.00 142.65 ? 61  GLN D CD  1 
ATOM   5650  O OE1 . GLN D  2 27  ? 158.400 133.331 150.847 1.00 148.78 ? 61  GLN D OE1 1 
ATOM   5651  N NE2 . GLN D  2 27  ? 157.361 131.344 150.742 1.00 142.02 ? 61  GLN D NE2 1 
ATOM   5652  N N   . LEU D  2 28  ? 153.264 133.479 153.307 1.00 109.92 ? 62  LEU D N   1 
ATOM   5653  C CA  . LEU D  2 28  ? 152.140 133.956 154.096 1.00 106.53 ? 62  LEU D CA  1 
ATOM   5654  C C   . LEU D  2 28  ? 152.616 134.935 155.158 1.00 105.50 ? 62  LEU D C   1 
ATOM   5655  O O   . LEU D  2 28  ? 153.765 134.899 155.604 1.00 105.49 ? 62  LEU D O   1 
ATOM   5656  C CB  . LEU D  2 28  ? 151.397 132.797 154.768 1.00 108.11 ? 62  LEU D CB  1 
ATOM   5657  C CG  . LEU D  2 28  ? 151.114 131.572 153.902 1.00 112.20 ? 62  LEU D CG  1 
ATOM   5658  C CD1 . LEU D  2 28  ? 151.000 130.330 154.765 1.00 117.80 ? 62  LEU D CD1 1 
ATOM   5659  C CD2 . LEU D  2 28  ? 149.853 131.784 153.095 1.00 109.38 ? 62  LEU D CD2 1 
ATOM   5660  N N   . PHE D  2 29  ? 151.702 135.813 155.562 1.00 104.45 ? 63  PHE D N   1 
ATOM   5661  C CA  . PHE D  2 29  ? 151.929 136.753 156.648 1.00 102.93 ? 63  PHE D CA  1 
ATOM   5662  C C   . PHE D  2 29  ? 151.117 136.445 157.895 1.00 102.77 ? 63  PHE D C   1 
ATOM   5663  O O   . PHE D  2 29  ? 151.524 136.838 158.990 1.00 105.75 ? 63  PHE D O   1 
ATOM   5664  C CB  . PHE D  2 29  ? 151.609 138.185 156.190 1.00 105.68 ? 63  PHE D CB  1 
ATOM   5665  C CG  . PHE D  2 29  ? 151.997 139.241 157.184 1.00 105.09 ? 63  PHE D CG  1 
ATOM   5666  C CD1 . PHE D  2 29  ? 153.315 139.642 157.312 1.00 107.14 ? 63  PHE D CD1 1 
ATOM   5667  C CD2 . PHE D  2 29  ? 151.040 139.833 157.991 1.00 104.18 ? 63  PHE D CD2 1 
ATOM   5668  C CE1 . PHE D  2 29  ? 153.671 140.613 158.226 1.00 108.44 ? 63  PHE D CE1 1 
ATOM   5669  C CE2 . PHE D  2 29  ? 151.391 140.803 158.906 1.00 105.88 ? 63  PHE D CE2 1 
ATOM   5670  C CZ  . PHE D  2 29  ? 152.707 141.194 159.024 1.00 108.72 ? 63  PHE D CZ  1 
ATOM   5671  N N   . GLY D  2 30  ? 149.993 135.752 157.764 1.00 99.30  ? 64  GLY D N   1 
ATOM   5672  C CA  . GLY D  2 30  ? 149.181 135.415 158.919 1.00 97.45  ? 64  GLY D CA  1 
ATOM   5673  C C   . GLY D  2 30  ? 147.790 135.013 158.482 1.00 94.71  ? 64  GLY D C   1 
ATOM   5674  O O   . GLY D  2 30  ? 147.402 135.182 157.321 1.00 95.01  ? 64  GLY D O   1 
ATOM   5675  N N   . TYR D  2 31  ? 147.040 134.474 159.439 1.00 94.39  ? 65  TYR D N   1 
ATOM   5676  C CA  . TYR D  2 31  ? 145.683 134.007 159.205 1.00 93.36  ? 65  TYR D CA  1 
ATOM   5677  C C   . TYR D  2 31  ? 144.722 134.700 160.161 1.00 94.32  ? 65  TYR D C   1 
ATOM   5678  O O   . TYR D  2 31  ? 145.132 135.396 161.094 1.00 103.96 ? 65  TYR D O   1 
ATOM   5679  C CB  . TYR D  2 31  ? 145.560 132.487 159.389 1.00 95.50  ? 65  TYR D CB  1 
ATOM   5680  C CG  . TYR D  2 31  ? 146.824 131.705 159.124 1.00 96.14  ? 65  TYR D CG  1 
ATOM   5681  C CD1 . TYR D  2 31  ? 147.349 130.862 160.093 1.00 96.34  ? 65  TYR D CD1 1 
ATOM   5682  C CD2 . TYR D  2 31  ? 147.476 131.785 157.902 1.00 102.29 ? 65  TYR D CD2 1 
ATOM   5683  C CE1 . TYR D  2 31  ? 148.499 130.139 159.862 1.00 107.06 ? 65  TYR D CE1 1 
ATOM   5684  C CE2 . TYR D  2 31  ? 148.628 131.065 157.661 1.00 108.09 ? 65  TYR D CE2 1 
ATOM   5685  C CZ  . TYR D  2 31  ? 149.134 130.242 158.645 1.00 113.76 ? 65  TYR D CZ  1 
ATOM   5686  O OH  . TYR D  2 31  ? 150.280 129.519 158.411 1.00 119.71 ? 65  TYR D OH  1 
ATOM   5687  N N   . SER D  2 32  ? 143.430 134.493 159.916 1.00 86.37  ? 66  SER D N   1 
ATOM   5688  C CA  . SER D  2 32  ? 142.386 134.987 160.805 1.00 89.08  ? 66  SER D CA  1 
ATOM   5689  C C   . SER D  2 32  ? 141.092 134.263 160.477 1.00 89.53  ? 66  SER D C   1 
ATOM   5690  O O   . SER D  2 32  ? 140.773 134.066 159.301 1.00 94.18  ? 66  SER D O   1 
ATOM   5691  C CB  . SER D  2 32  ? 142.205 136.501 160.663 1.00 93.10  ? 66  SER D CB  1 
ATOM   5692  O OG  . SER D  2 32  ? 143.123 137.198 161.485 1.00 96.13  ? 66  SER D OG  1 
ATOM   5693  N N   . TRP D  2 33  ? 140.353 133.874 161.511 1.00 85.88  ? 67  TRP D N   1 
ATOM   5694  C CA  . TRP D  2 33  ? 139.078 133.188 161.356 1.00 83.57  ? 67  TRP D CA  1 
ATOM   5695  C C   . TRP D  2 33  ? 137.960 134.092 161.854 1.00 92.37  ? 67  TRP D C   1 
ATOM   5696  O O   . TRP D  2 33  ? 138.012 134.583 162.986 1.00 99.55  ? 67  TRP D O   1 
ATOM   5697  C CB  . TRP D  2 33  ? 139.071 131.862 162.118 1.00 82.22  ? 67  TRP D CB  1 
ATOM   5698  C CG  . TRP D  2 33  ? 139.724 130.738 161.375 1.00 79.05  ? 67  TRP D CG  1 
ATOM   5699  C CD1 . TRP D  2 33  ? 141.016 130.321 161.494 1.00 84.40  ? 67  TRP D CD1 1 
ATOM   5700  C CD2 . TRP D  2 33  ? 139.116 129.886 160.398 1.00 80.44  ? 67  TRP D CD2 1 
ATOM   5701  N NE1 . TRP D  2 33  ? 141.251 129.262 160.652 1.00 85.89  ? 67  TRP D NE1 1 
ATOM   5702  C CE2 . TRP D  2 33  ? 140.099 128.976 159.968 1.00 80.33  ? 67  TRP D CE2 1 
ATOM   5703  C CE3 . TRP D  2 33  ? 137.835 129.805 159.845 1.00 88.45  ? 67  TRP D CE3 1 
ATOM   5704  C CZ2 . TRP D  2 33  ? 139.843 127.997 159.012 1.00 77.72  ? 67  TRP D CZ2 1 
ATOM   5705  C CZ3 . TRP D  2 33  ? 137.583 128.833 158.896 1.00 84.74  ? 67  TRP D CZ3 1 
ATOM   5706  C CH2 . TRP D  2 33  ? 138.581 127.942 158.490 1.00 75.50  ? 67  TRP D CH2 1 
ATOM   5707  N N   . TYR D  2 34  ? 136.956 134.307 161.010 1.00 92.64  ? 68  TYR D N   1 
ATOM   5708  C CA  . TYR D  2 34  ? 135.836 135.181 161.321 1.00 93.66  ? 68  TYR D CA  1 
ATOM   5709  C C   . TYR D  2 34  ? 134.545 134.378 161.331 1.00 97.82  ? 68  TYR D C   1 
ATOM   5710  O O   . TYR D  2 34  ? 134.352 133.484 160.502 1.00 102.90 ? 68  TYR D O   1 
ATOM   5711  C CB  . TYR D  2 34  ? 135.726 136.321 160.306 1.00 93.93  ? 68  TYR D CB  1 
ATOM   5712  C CG  . TYR D  2 34  ? 136.949 137.202 160.237 1.00 94.35  ? 68  TYR D CG  1 
ATOM   5713  C CD1 . TYR D  2 34  ? 138.004 136.892 159.393 1.00 95.88  ? 68  TYR D CD1 1 
ATOM   5714  C CD2 . TYR D  2 34  ? 137.044 138.349 161.010 1.00 101.18 ? 68  TYR D CD2 1 
ATOM   5715  C CE1 . TYR D  2 34  ? 139.123 137.694 159.327 1.00 100.97 ? 68  TYR D CE1 1 
ATOM   5716  C CE2 . TYR D  2 34  ? 138.159 139.158 160.950 1.00 103.51 ? 68  TYR D CE2 1 
ATOM   5717  C CZ  . TYR D  2 34  ? 139.194 138.827 160.106 1.00 104.24 ? 68  TYR D CZ  1 
ATOM   5718  O OH  . TYR D  2 34  ? 140.308 139.630 160.040 1.00 112.20 ? 68  TYR D OH  1 
ATOM   5719  N N   . LYS D  2 35  ? 133.664 134.700 162.273 1.00 92.96  ? 69  LYS D N   1 
ATOM   5720  C CA  . LYS D  2 35  ? 132.351 134.072 162.336 1.00 96.44  ? 69  LYS D CA  1 
ATOM   5721  C C   . LYS D  2 35  ? 131.424 134.753 161.337 1.00 107.70 ? 69  LYS D C   1 
ATOM   5722  O O   . LYS D  2 35  ? 131.350 135.986 161.291 1.00 115.58 ? 69  LYS D O   1 
ATOM   5723  C CB  . LYS D  2 35  ? 131.783 134.160 163.751 1.00 103.72 ? 69  LYS D CB  1 
ATOM   5724  C CG  . LYS D  2 35  ? 130.316 133.781 163.853 1.00 111.13 ? 69  LYS D CG  1 
ATOM   5725  C CD  . LYS D  2 35  ? 130.123 132.542 164.709 1.00 114.71 ? 69  LYS D CD  1 
ATOM   5726  C CE  . LYS D  2 35  ? 128.665 132.361 165.092 1.00 116.69 ? 69  LYS D CE  1 
ATOM   5727  N NZ  . LYS D  2 35  ? 127.792 132.236 163.893 1.00 116.11 ? 69  LYS D NZ  1 
ATOM   5728  N N   . GLY D  2 36  ? 130.724 133.959 160.542 1.00 107.07 ? 70  GLY D N   1 
ATOM   5729  C CA  . GLY D  2 36  ? 129.841 134.468 159.513 1.00 106.86 ? 70  GLY D CA  1 
ATOM   5730  C C   . GLY D  2 36  ? 130.531 134.549 158.161 1.00 104.25 ? 70  GLY D C   1 
ATOM   5731  O O   . GLY D  2 36  ? 131.732 134.322 158.018 1.00 106.83 ? 70  GLY D O   1 
ATOM   5732  N N   . GLU D  2 37  ? 129.727 134.888 157.153 1.00 104.41 ? 71  GLU D N   1 
ATOM   5733  C CA  . GLU D  2 37  ? 130.212 134.966 155.782 1.00 109.82 ? 71  GLU D CA  1 
ATOM   5734  C C   . GLU D  2 37  ? 131.041 136.212 155.511 1.00 110.87 ? 71  GLU D C   1 
ATOM   5735  O O   . GLU D  2 37  ? 131.668 136.299 154.450 1.00 111.61 ? 71  GLU D O   1 
ATOM   5736  C CB  . GLU D  2 37  ? 129.035 134.924 154.806 1.00 112.20 ? 71  GLU D CB  1 
ATOM   5737  C CG  . GLU D  2 37  ? 128.686 133.535 154.308 1.00 120.38 ? 71  GLU D CG  1 
ATOM   5738  C CD  . GLU D  2 37  ? 127.194 133.341 154.143 1.00 132.28 ? 71  GLU D CD  1 
ATOM   5739  O OE1 . GLU D  2 37  ? 126.459 134.350 154.143 1.00 141.46 ? 71  GLU D OE1 1 
ATOM   5740  O OE2 . GLU D  2 37  ? 126.755 132.180 154.010 1.00 133.71 ? 71  GLU D OE2 1 
ATOM   5741  N N   . ARG D  2 38  ? 131.061 137.168 156.432 1.00 112.66 ? 72  ARG D N   1 
ATOM   5742  C CA  . ARG D  2 38  ? 131.755 138.432 156.246 1.00 117.92 ? 72  ARG D CA  1 
ATOM   5743  C C   . ARG D  2 38  ? 133.072 138.425 157.006 1.00 115.39 ? 72  ARG D C   1 
ATOM   5744  O O   . ARG D  2 38  ? 133.257 137.641 157.942 1.00 115.17 ? 72  ARG D O   1 
ATOM   5745  C CB  . ARG D  2 38  ? 130.897 139.604 156.725 1.00 129.16 ? 72  ARG D CB  1 
ATOM   5746  C CG  . ARG D  2 38  ? 129.790 140.009 155.773 1.00 135.50 ? 72  ARG D CG  1 
ATOM   5747  C CD  . ARG D  2 38  ? 130.162 141.285 155.027 1.00 139.94 ? 72  ARG D CD  1 
ATOM   5748  N NE  . ARG D  2 38  ? 130.422 142.420 155.910 1.00 149.06 ? 72  ARG D NE  1 
ATOM   5749  C CZ  . ARG D  2 38  ? 129.600 142.881 156.846 1.00 151.15 ? 72  ARG D CZ  1 
ATOM   5750  N NH1 . ARG D  2 38  ? 129.985 143.816 157.700 1.00 150.33 ? 72  ARG D NH1 1 
ATOM   5751  N NH2 . ARG D  2 38  ? 128.354 142.420 156.909 1.00 147.46 ? 72  ARG D NH2 1 
ATOM   5752  N N   . VAL D  2 39  ? 133.983 139.303 156.597 1.00 116.99 ? 73  VAL D N   1 
ATOM   5753  C CA  . VAL D  2 39  ? 135.216 139.536 157.339 1.00 113.34 ? 73  VAL D CA  1 
ATOM   5754  C C   . VAL D  2 39  ? 135.090 140.896 158.016 1.00 119.19 ? 73  VAL D C   1 
ATOM   5755  O O   . VAL D  2 39  ? 135.288 141.939 157.388 1.00 123.96 ? 73  VAL D O   1 
ATOM   5756  C CB  . VAL D  2 39  ? 136.446 139.466 156.429 1.00 108.54 ? 73  VAL D CB  1 
ATOM   5757  C CG1 . VAL D  2 39  ? 137.673 140.031 157.131 1.00 104.82 ? 73  VAL D CG1 1 
ATOM   5758  C CG2 . VAL D  2 39  ? 136.692 138.028 156.015 1.00 112.49 ? 73  VAL D CG2 1 
ATOM   5759  N N   . ASP D  2 40  ? 134.725 140.885 159.295 1.00 119.52 ? 74  ASP D N   1 
ATOM   5760  C CA  . ASP D  2 40  ? 134.537 142.101 160.068 1.00 121.49 ? 74  ASP D CA  1 
ATOM   5761  C C   . ASP D  2 40  ? 135.352 141.987 161.346 1.00 122.87 ? 74  ASP D C   1 
ATOM   5762  O O   . ASP D  2 40  ? 135.453 140.910 161.940 1.00 121.83 ? 74  ASP D O   1 
ATOM   5763  C CB  . ASP D  2 40  ? 133.052 142.335 160.388 1.00 123.41 ? 74  ASP D CB  1 
ATOM   5764  C CG  . ASP D  2 40  ? 132.823 143.558 161.256 1.00 133.89 ? 74  ASP D CG  1 
ATOM   5765  O OD1 . ASP D  2 40  ? 131.739 143.654 161.868 1.00 135.70 ? 74  ASP D OD1 1 
ATOM   5766  O OD2 . ASP D  2 40  ? 133.713 144.432 161.313 1.00 138.11 ? 74  ASP D OD2 1 
ATOM   5767  N N   . GLY D  2 41  ? 135.933 143.112 161.766 1.00 124.55 ? 75  GLY D N   1 
ATOM   5768  C CA  . GLY D  2 41  ? 136.808 143.088 162.927 1.00 120.52 ? 75  GLY D CA  1 
ATOM   5769  C C   . GLY D  2 41  ? 136.087 142.686 164.199 1.00 120.56 ? 75  GLY D C   1 
ATOM   5770  O O   . GLY D  2 41  ? 136.704 142.183 165.141 1.00 120.93 ? 75  GLY D O   1 
ATOM   5771  N N   . ASN D  2 42  ? 134.771 142.899 164.245 1.00 121.81 ? 76  ASN D N   1 
ATOM   5772  C CA  . ASN D  2 42  ? 133.997 142.511 165.417 1.00 120.97 ? 76  ASN D CA  1 
ATOM   5773  C C   . ASN D  2 42  ? 133.740 141.012 165.468 1.00 116.10 ? 76  ASN D C   1 
ATOM   5774  O O   . ASN D  2 42  ? 133.426 140.484 166.541 1.00 113.97 ? 76  ASN D O   1 
ATOM   5775  C CB  . ASN D  2 42  ? 132.669 143.267 165.438 1.00 129.48 ? 76  ASN D CB  1 
ATOM   5776  C CG  . ASN D  2 42  ? 132.852 144.760 165.607 1.00 139.87 ? 76  ASN D CG  1 
ATOM   5777  O OD1 . ASN D  2 42  ? 133.819 145.213 166.219 1.00 144.93 ? 76  ASN D OD1 1 
ATOM   5778  N ND2 . ASN D  2 42  ? 131.924 145.536 165.059 1.00 140.11 ? 76  ASN D ND2 1 
ATOM   5779  N N   . ARG D  2 43  ? 133.863 140.317 164.341 1.00 115.24 ? 77  ARG D N   1 
ATOM   5780  C CA  . ARG D  2 43  ? 133.596 138.887 164.270 1.00 112.76 ? 77  ARG D CA  1 
ATOM   5781  C C   . ARG D  2 43  ? 134.856 138.033 164.315 1.00 110.00 ? 77  ARG D C   1 
ATOM   5782  O O   . ARG D  2 43  ? 134.758 136.813 164.153 1.00 110.36 ? 77  ARG D O   1 
ATOM   5783  C CB  . ARG D  2 43  ? 132.813 138.557 162.996 1.00 113.93 ? 77  ARG D CB  1 
ATOM   5784  C CG  . ARG D  2 43  ? 131.705 139.536 162.661 1.00 117.42 ? 77  ARG D CG  1 
ATOM   5785  C CD  . ARG D  2 43  ? 130.689 139.614 163.786 1.00 122.83 ? 77  ARG D CD  1 
ATOM   5786  N NE  . ARG D  2 43  ? 129.868 138.411 163.860 1.00 128.21 ? 77  ARG D NE  1 
ATOM   5787  C CZ  . ARG D  2 43  ? 128.889 138.114 163.016 1.00 129.90 ? 77  ARG D CZ  1 
ATOM   5788  N NH1 . ARG D  2 43  ? 128.575 138.915 162.011 1.00 132.82 ? 77  ARG D NH1 1 
ATOM   5789  N NH2 . ARG D  2 43  ? 128.208 136.984 163.184 1.00 126.12 ? 77  ARG D NH2 1 
ATOM   5790  N N   . GLN D  2 44  ? 136.027 138.630 164.518 1.00 107.15 ? 78  GLN D N   1 
ATOM   5791  C CA  . GLN D  2 44  ? 137.257 137.849 164.516 1.00 101.16 ? 78  GLN D CA  1 
ATOM   5792  C C   . GLN D  2 44  ? 137.289 136.901 165.704 1.00 103.74 ? 78  GLN D C   1 
ATOM   5793  O O   . GLN D  2 44  ? 137.170 137.323 166.858 1.00 109.89 ? 78  GLN D O   1 
ATOM   5794  C CB  . GLN D  2 44  ? 138.477 138.767 164.542 1.00 101.02 ? 78  GLN D CB  1 
ATOM   5795  C CG  . GLN D  2 44  ? 139.783 138.033 164.285 1.00 99.66  ? 78  GLN D CG  1 
ATOM   5796  C CD  . GLN D  2 44  ? 140.999 138.918 164.454 1.00 108.11 ? 78  GLN D CD  1 
ATOM   5797  O OE1 . GLN D  2 44  ? 141.046 139.766 165.343 1.00 119.34 ? 78  GLN D OE1 1 
ATOM   5798  N NE2 . GLN D  2 44  ? 141.996 138.720 163.600 1.00 106.65 ? 78  GLN D NE2 1 
ATOM   5799  N N   . ILE D  2 45  ? 137.456 135.616 165.417 1.00 96.19  ? 79  ILE D N   1 
ATOM   5800  C CA  . ILE D  2 45  ? 137.554 134.588 166.444 1.00 93.61  ? 79  ILE D CA  1 
ATOM   5801  C C   . ILE D  2 45  ? 138.975 134.465 166.968 1.00 97.52  ? 79  ILE D C   1 
ATOM   5802  O O   . ILE D  2 45  ? 139.210 134.522 168.174 1.00 105.52 ? 79  ILE D O   1 
ATOM   5803  C CB  . ILE D  2 45  ? 137.046 133.236 165.897 1.00 87.71  ? 79  ILE D CB  1 
ATOM   5804  C CG1 . ILE D  2 45  ? 135.591 133.355 165.445 1.00 96.89  ? 79  ILE D CG1 1 
ATOM   5805  C CG2 . ILE D  2 45  ? 137.194 132.152 166.944 1.00 94.47  ? 79  ILE D CG2 1 
ATOM   5806  C CD1 . ILE D  2 45  ? 135.146 132.230 164.545 1.00 94.83  ? 79  ILE D CD1 1 
ATOM   5807  N N   . VAL D  2 46  ? 139.939 134.297 166.064 1.00 95.33  ? 80  VAL D N   1 
ATOM   5808  C CA  . VAL D  2 46  ? 141.336 134.123 166.440 1.00 97.54  ? 80  VAL D CA  1 
ATOM   5809  C C   . VAL D  2 46  ? 142.187 134.527 165.248 1.00 96.71  ? 80  VAL D C   1 
ATOM   5810  O O   . VAL D  2 46  ? 141.719 134.547 164.109 1.00 99.74  ? 80  VAL D O   1 
ATOM   5811  C CB  . VAL D  2 46  ? 141.614 132.663 166.881 1.00 94.16  ? 80  VAL D CB  1 
ATOM   5812  C CG1 . VAL D  2 46  ? 141.714 131.756 165.671 1.00 89.37  ? 80  VAL D CG1 1 
ATOM   5813  C CG2 . VAL D  2 46  ? 142.875 132.586 167.729 1.00 100.53 ? 80  VAL D CG2 1 
ATOM   5814  N N   . GLY D  2 47  ? 143.442 134.861 165.511 1.00 92.05  ? 81  GLY D N   1 
ATOM   5815  C CA  . GLY D  2 47  ? 144.354 135.257 164.456 1.00 90.63  ? 81  GLY D CA  1 
ATOM   5816  C C   . GLY D  2 47  ? 145.762 134.806 164.771 1.00 92.89  ? 81  GLY D C   1 
ATOM   5817  O O   . GLY D  2 47  ? 146.184 134.774 165.929 1.00 101.78 ? 81  GLY D O   1 
ATOM   5818  N N   . TYR D  2 48  ? 146.491 134.453 163.717 1.00 89.04  ? 82  TYR D N   1 
ATOM   5819  C CA  . TYR D  2 48  ? 147.862 133.986 163.843 1.00 93.42  ? 82  TYR D CA  1 
ATOM   5820  C C   . TYR D  2 48  ? 148.770 134.899 163.038 1.00 98.21  ? 82  TYR D C   1 
ATOM   5821  O O   . TYR D  2 48  ? 148.400 135.351 161.951 1.00 101.89 ? 82  TYR D O   1 
ATOM   5822  C CB  . TYR D  2 48  ? 148.006 132.538 163.360 1.00 96.02  ? 82  TYR D CB  1 
ATOM   5823  C CG  . TYR D  2 48  ? 149.318 131.890 163.736 1.00 97.63  ? 82  TYR D CG  1 
ATOM   5824  C CD1 . TYR D  2 48  ? 149.653 131.678 165.065 1.00 100.25 ? 82  TYR D CD1 1 
ATOM   5825  C CD2 . TYR D  2 48  ? 150.220 131.488 162.761 1.00 101.45 ? 82  TYR D CD2 1 
ATOM   5826  C CE1 . TYR D  2 48  ? 150.849 131.085 165.414 1.00 103.97 ? 82  TYR D CE1 1 
ATOM   5827  C CE2 . TYR D  2 48  ? 151.419 130.895 163.100 1.00 104.40 ? 82  TYR D CE2 1 
ATOM   5828  C CZ  . TYR D  2 48  ? 151.728 130.696 164.428 1.00 108.58 ? 82  TYR D CZ  1 
ATOM   5829  O OH  . TYR D  2 48  ? 152.922 130.105 164.770 1.00 119.67 ? 82  TYR D OH  1 
ATOM   5830  N N   . ALA D  2 49  ? 149.953 135.173 163.579 1.00 101.72 ? 83  ALA D N   1 
ATOM   5831  C CA  . ALA D  2 49  ? 150.958 135.999 162.919 1.00 103.79 ? 83  ALA D CA  1 
ATOM   5832  C C   . ALA D  2 49  ? 152.237 135.181 162.815 1.00 108.17 ? 83  ALA D C   1 
ATOM   5833  O O   . ALA D  2 49  ? 152.946 135.003 163.810 1.00 114.66 ? 83  ALA D O   1 
ATOM   5834  C CB  . ALA D  2 49  ? 151.193 137.300 163.683 1.00 106.74 ? 83  ALA D CB  1 
ATOM   5835  N N   . ILE D  2 50  ? 152.528 134.686 161.609 1.00 103.99 ? 84  ILE D N   1 
ATOM   5836  C CA  . ILE D  2 50  ? 153.659 133.783 161.415 1.00 105.28 ? 84  ILE D CA  1 
ATOM   5837  C C   . ILE D  2 50  ? 154.975 134.454 161.781 1.00 112.42 ? 84  ILE D C   1 
ATOM   5838  O O   . ILE D  2 50  ? 155.875 133.809 162.333 1.00 115.65 ? 84  ILE D O   1 
ATOM   5839  C CB  . ILE D  2 50  ? 153.669 133.261 159.965 1.00 102.32 ? 84  ILE D CB  1 
ATOM   5840  C CG1 . ILE D  2 50  ? 152.399 132.456 159.694 1.00 104.64 ? 84  ILE D CG1 1 
ATOM   5841  C CG2 . ILE D  2 50  ? 154.898 132.407 159.705 1.00 104.49 ? 84  ILE D CG2 1 
ATOM   5842  C CD1 . ILE D  2 50  ? 152.046 132.353 158.239 1.00 105.52 ? 84  ILE D CD1 1 
ATOM   5843  N N   . GLY D  2 51  ? 155.114 135.744 161.481 1.00 115.66 ? 85  GLY D N   1 
ATOM   5844  C CA  . GLY D  2 51  ? 156.321 136.486 161.794 1.00 119.97 ? 85  GLY D CA  1 
ATOM   5845  C C   . GLY D  2 51  ? 156.787 136.336 163.228 1.00 117.66 ? 85  GLY D C   1 
ATOM   5846  O O   . GLY D  2 51  ? 157.875 135.810 163.481 1.00 117.13 ? 85  GLY D O   1 
ATOM   5847  N N   . THR D  2 52  ? 155.973 136.791 164.177 1.00 115.07 ? 86  THR D N   1 
ATOM   5848  C CA  . THR D  2 52  ? 156.295 136.660 165.591 1.00 117.75 ? 86  THR D CA  1 
ATOM   5849  C C   . THR D  2 52  ? 155.787 135.361 166.202 1.00 121.79 ? 86  THR D C   1 
ATOM   5850  O O   . THR D  2 52  ? 156.088 135.088 167.369 1.00 123.60 ? 86  THR D O   1 
ATOM   5851  C CB  . THR D  2 52  ? 155.727 137.846 166.378 1.00 122.40 ? 86  THR D CB  1 
ATOM   5852  O OG1 . THR D  2 52  ? 154.296 137.828 166.308 1.00 123.56 ? 86  THR D OG1 1 
ATOM   5853  C CG2 . THR D  2 52  ? 156.240 139.157 165.806 1.00 126.06 ? 86  THR D CG2 1 
ATOM   5854  N N   . GLN D  2 53  ? 155.028 134.563 165.448 1.00 121.43 ? 87  GLN D N   1 
ATOM   5855  C CA  . GLN D  2 53  ? 154.499 133.278 165.909 1.00 115.97 ? 87  GLN D CA  1 
ATOM   5856  C C   . GLN D  2 53  ? 153.641 133.455 167.164 1.00 114.24 ? 87  GLN D C   1 
ATOM   5857  O O   . GLN D  2 53  ? 153.874 132.842 168.207 1.00 114.24 ? 87  GLN D O   1 
ATOM   5858  C CB  . GLN D  2 53  ? 155.631 132.272 166.138 1.00 114.52 ? 87  GLN D CB  1 
ATOM   5859  C CG  . GLN D  2 53  ? 156.232 131.738 164.850 1.00 118.24 ? 87  GLN D CG  1 
ATOM   5860  C CD  . GLN D  2 53  ? 157.395 130.800 165.092 1.00 130.71 ? 87  GLN D CD  1 
ATOM   5861  O OE1 . GLN D  2 53  ? 157.751 130.514 166.234 1.00 139.76 ? 87  GLN D OE1 1 
ATOM   5862  N NE2 . GLN D  2 53  ? 157.997 130.316 164.012 1.00 132.95 ? 87  GLN D NE2 1 
ATOM   5863  N N   . GLN D  2 54  ? 152.632 134.314 167.037 1.00 111.87 ? 88  GLN D N   1 
ATOM   5864  C CA  . GLN D  2 54  ? 151.706 134.612 168.121 1.00 112.11 ? 88  GLN D CA  1 
ATOM   5865  C C   . GLN D  2 54  ? 150.288 134.301 167.669 1.00 109.71 ? 88  GLN D C   1 
ATOM   5866  O O   . GLN D  2 54  ? 149.938 134.535 166.508 1.00 110.59 ? 88  GLN D O   1 
ATOM   5867  C CB  . GLN D  2 54  ? 151.814 136.077 168.555 1.00 116.90 ? 88  GLN D CB  1 
ATOM   5868  C CG  . GLN D  2 54  ? 152.519 136.300 169.887 1.00 124.02 ? 88  GLN D CG  1 
ATOM   5869  C CD  . GLN D  2 54  ? 151.899 135.514 171.030 1.00 131.10 ? 88  GLN D CD  1 
ATOM   5870  O OE1 . GLN D  2 54  ? 152.163 134.323 171.200 1.00 135.97 ? 88  GLN D OE1 1 
ATOM   5871  N NE2 . GLN D  2 54  ? 151.066 136.181 171.820 1.00 132.54 ? 88  GLN D NE2 1 
ATOM   5872  N N   . ALA D  2 55  ? 149.479 133.777 168.585 1.00 108.68 ? 89  ALA D N   1 
ATOM   5873  C CA  . ALA D  2 55  ? 148.077 133.456 168.324 1.00 105.85 ? 89  ALA D CA  1 
ATOM   5874  C C   . ALA D  2 55  ? 147.226 134.269 169.293 1.00 107.05 ? 89  ALA D C   1 
ATOM   5875  O O   . ALA D  2 55  ? 147.086 133.909 170.465 1.00 112.67 ? 89  ALA D O   1 
ATOM   5876  C CB  . ALA D  2 55  ? 147.823 131.960 168.471 1.00 109.19 ? 89  ALA D CB  1 
ATOM   5877  N N   . THR D  2 56  ? 146.655 135.366 168.799 1.00 105.64 ? 90  THR D N   1 
ATOM   5878  C CA  . THR D  2 56  ? 145.895 136.282 169.640 1.00 112.64 ? 90  THR D CA  1 
ATOM   5879  C C   . THR D  2 56  ? 144.404 136.067 169.450 1.00 110.82 ? 90  THR D C   1 
ATOM   5880  O O   . THR D  2 56  ? 143.906 136.188 168.321 1.00 110.16 ? 90  THR D O   1 
ATOM   5881  C CB  . THR D  2 56  ? 146.249 137.729 169.315 1.00 116.90 ? 90  THR D CB  1 
ATOM   5882  O OG1 . THR D  2 56  ? 146.192 137.930 167.898 1.00 116.61 ? 90  THR D OG1 1 
ATOM   5883  C CG2 . THR D  2 56  ? 147.645 138.058 169.817 1.00 114.51 ? 90  THR D CG2 1 
ATOM   5884  N N   . PRO D  2 57  ? 143.668 135.744 170.510 1.00 110.42 ? 91  PRO D N   1 
ATOM   5885  C CA  . PRO D  2 57  ? 142.212 135.623 170.389 1.00 108.39 ? 91  PRO D CA  1 
ATOM   5886  C C   . PRO D  2 57  ? 141.572 136.952 170.023 1.00 105.33 ? 91  PRO D C   1 
ATOM   5887  O O   . PRO D  2 57  ? 142.080 138.027 170.347 1.00 108.54 ? 91  PRO D O   1 
ATOM   5888  C CB  . PRO D  2 57  ? 141.780 135.164 171.788 1.00 109.78 ? 91  PRO D CB  1 
ATOM   5889  C CG  . PRO D  2 57  ? 142.896 135.619 172.683 1.00 111.26 ? 91  PRO D CG  1 
ATOM   5890  C CD  . PRO D  2 57  ? 144.128 135.396 171.864 1.00 111.73 ? 91  PRO D CD  1 
ATOM   5891  N N   . GLY D  2 58  ? 140.439 136.864 169.332 1.00 102.67 ? 92  GLY D N   1 
ATOM   5892  C CA  . GLY D  2 58  ? 139.725 138.038 168.892 1.00 105.39 ? 92  GLY D CA  1 
ATOM   5893  C C   . GLY D  2 58  ? 138.535 138.355 169.773 1.00 112.23 ? 92  GLY D C   1 
ATOM   5894  O O   . GLY D  2 58  ? 138.247 137.652 170.746 1.00 115.71 ? 92  GLY D O   1 
ATOM   5895  N N   . PRO D  2 59  ? 137.825 139.439 169.451 1.00 112.10 ? 93  PRO D N   1 
ATOM   5896  C CA  . PRO D  2 59  ? 136.644 139.806 170.250 1.00 110.85 ? 93  PRO D CA  1 
ATOM   5897  C C   . PRO D  2 59  ? 135.567 138.736 170.273 1.00 109.83 ? 93  PRO D C   1 
ATOM   5898  O O   . PRO D  2 59  ? 134.848 138.618 171.273 1.00 112.48 ? 93  PRO D O   1 
ATOM   5899  C CB  . PRO D  2 59  ? 136.154 141.090 169.564 1.00 113.58 ? 93  PRO D CB  1 
ATOM   5900  C CG  . PRO D  2 59  ? 136.732 141.009 168.176 1.00 115.00 ? 93  PRO D CG  1 
ATOM   5901  C CD  . PRO D  2 59  ? 138.091 140.434 168.402 1.00 111.08 ? 93  PRO D CD  1 
ATOM   5902  N N   . ALA D  2 60  ? 135.430 137.955 169.205 1.00 108.10 ? 94  ALA D N   1 
ATOM   5903  C CA  . ALA D  2 60  ? 134.422 136.907 169.135 1.00 106.21 ? 94  ALA D CA  1 
ATOM   5904  C C   . ALA D  2 60  ? 134.864 135.612 169.804 1.00 108.47 ? 94  ALA D C   1 
ATOM   5905  O O   . ALA D  2 60  ? 134.082 134.657 169.848 1.00 109.72 ? 94  ALA D O   1 
ATOM   5906  C CB  . ALA D  2 60  ? 134.048 136.630 167.676 1.00 103.45 ? 94  ALA D CB  1 
ATOM   5907  N N   . ASN D  2 61  ? 136.092 135.554 170.315 1.00 112.07 ? 95  ASN D N   1 
ATOM   5908  C CA  . ASN D  2 61  ? 136.575 134.345 170.966 1.00 116.37 ? 95  ASN D CA  1 
ATOM   5909  C C   . ASN D  2 61  ? 135.792 134.069 172.243 1.00 117.69 ? 95  ASN D C   1 
ATOM   5910  O O   . ASN D  2 61  ? 135.359 134.991 172.939 1.00 118.21 ? 95  ASN D O   1 
ATOM   5911  C CB  . ASN D  2 61  ? 138.065 134.473 171.282 1.00 117.30 ? 95  ASN D CB  1 
ATOM   5912  C CG  . ASN D  2 61  ? 138.707 133.140 171.607 1.00 118.38 ? 95  ASN D CG  1 
ATOM   5913  O OD1 . ASN D  2 61  ? 138.598 132.642 172.727 1.00 123.04 ? 95  ASN D OD1 1 
ATOM   5914  N ND2 . ASN D  2 61  ? 139.385 132.555 170.627 1.00 111.75 ? 95  ASN D ND2 1 
ATOM   5915  N N   . SER D  2 62  ? 135.611 132.785 172.547 1.00 123.21 ? 96  SER D N   1 
ATOM   5916  C CA  . SER D  2 62  ? 134.928 132.356 173.761 1.00 126.97 ? 96  SER D CA  1 
ATOM   5917  C C   . SER D  2 62  ? 135.755 131.368 174.573 1.00 127.26 ? 96  SER D C   1 
ATOM   5918  O O   . SER D  2 62  ? 135.225 130.747 175.502 1.00 126.13 ? 96  SER D O   1 
ATOM   5919  C CB  . SER D  2 62  ? 133.567 131.744 173.418 1.00 123.90 ? 96  SER D CB  1 
ATOM   5920  O OG  . SER D  2 62  ? 133.721 130.483 172.790 1.00 123.75 ? 96  SER D OG  1 
ATOM   5921  N N   . GLY D  2 63  ? 137.037 131.203 174.248 1.00 125.07 ? 97  GLY D N   1 
ATOM   5922  C CA  . GLY D  2 63  ? 137.900 130.284 174.954 1.00 123.42 ? 97  GLY D CA  1 
ATOM   5923  C C   . GLY D  2 63  ? 137.868 128.857 174.456 1.00 125.47 ? 97  GLY D C   1 
ATOM   5924  O O   . GLY D  2 63  ? 138.663 128.036 174.930 1.00 131.48 ? 97  GLY D O   1 
ATOM   5925  N N   . ARG D  2 64  ? 136.981 128.531 173.520 1.00 124.64 ? 98  ARG D N   1 
ATOM   5926  C CA  . ARG D  2 64  ? 136.863 127.182 172.986 1.00 124.00 ? 98  ARG D CA  1 
ATOM   5927  C C   . ARG D  2 64  ? 137.558 127.009 171.643 1.00 118.91 ? 98  ARG D C   1 
ATOM   5928  O O   . ARG D  2 64  ? 137.506 125.915 171.073 1.00 113.68 ? 98  ARG D O   1 
ATOM   5929  C CB  . ARG D  2 64  ? 135.387 126.807 172.838 1.00 122.92 ? 98  ARG D CB  1 
ATOM   5930  C CG  . ARG D  2 64  ? 134.576 126.908 174.115 1.00 120.44 ? 98  ARG D CG  1 
ATOM   5931  C CD  . ARG D  2 64  ? 133.106 126.681 173.820 1.00 125.21 ? 98  ARG D CD  1 
ATOM   5932  N NE  . ARG D  2 64  ? 132.611 127.636 172.836 1.00 124.09 ? 98  ARG D NE  1 
ATOM   5933  C CZ  . ARG D  2 64  ? 131.712 127.355 171.903 1.00 126.27 ? 98  ARG D CZ  1 
ATOM   5934  N NH1 . ARG D  2 64  ? 131.183 126.147 171.794 1.00 132.88 ? 98  ARG D NH1 1 
ATOM   5935  N NH2 . ARG D  2 64  ? 131.337 128.308 171.055 1.00 124.68 ? 98  ARG D NH2 1 
ATOM   5936  N N   . GLU D  2 65  ? 138.204 128.050 171.126 1.00 119.41 ? 99  GLU D N   1 
ATOM   5937  C CA  . GLU D  2 65  ? 138.755 128.045 169.779 1.00 116.52 ? 99  GLU D CA  1 
ATOM   5938  C C   . GLU D  2 65  ? 140.269 128.193 169.836 1.00 119.93 ? 99  GLU D C   1 
ATOM   5939  O O   . GLU D  2 65  ? 140.785 129.080 170.523 1.00 123.06 ? 99  GLU D O   1 
ATOM   5940  C CB  . GLU D  2 65  ? 138.146 129.170 168.940 1.00 112.47 ? 99  GLU D CB  1 
ATOM   5941  C CG  . GLU D  2 65  ? 136.644 129.338 169.117 1.00 114.84 ? 99  GLU D CG  1 
ATOM   5942  C CD  . GLU D  2 65  ? 136.289 130.288 170.247 1.00 127.00 ? 99  GLU D CD  1 
ATOM   5943  O OE1 . GLU D  2 65  ? 137.091 130.414 171.196 1.00 127.95 ? 99  GLU D OE1 1 
ATOM   5944  O OE2 . GLU D  2 65  ? 135.208 130.910 170.185 1.00 129.47 ? 99  GLU D OE2 1 
ATOM   5945  N N   . THR D  2 66  ? 140.971 127.324 169.113 1.00 115.92 ? 100 THR D N   1 
ATOM   5946  C CA  . THR D  2 66  ? 142.420 127.372 169.004 1.00 112.02 ? 100 THR D CA  1 
ATOM   5947  C C   . THR D  2 66  ? 142.818 127.329 167.537 1.00 109.15 ? 100 THR D C   1 
ATOM   5948  O O   . THR D  2 66  ? 142.256 126.563 166.749 1.00 107.10 ? 100 THR D O   1 
ATOM   5949  C CB  . THR D  2 66  ? 143.089 126.207 169.750 1.00 114.41 ? 100 THR D CB  1 
ATOM   5950  O OG1 . THR D  2 66  ? 142.630 124.964 169.206 1.00 112.86 ? 100 THR D OG1 1 
ATOM   5951  C CG2 . THR D  2 66  ? 142.759 126.257 171.232 1.00 114.86 ? 100 THR D CG2 1 
ATOM   5952  N N   . ILE D  2 67  ? 143.794 128.157 167.175 1.00 107.64 ? 101 ILE D N   1 
ATOM   5953  C CA  . ILE D  2 67  ? 144.346 128.190 165.826 1.00 105.24 ? 101 ILE D CA  1 
ATOM   5954  C C   . ILE D  2 67  ? 145.637 127.384 165.825 1.00 107.55 ? 101 ILE D C   1 
ATOM   5955  O O   . ILE D  2 67  ? 146.316 127.281 166.854 1.00 110.32 ? 101 ILE D O   1 
ATOM   5956  C CB  . ILE D  2 67  ? 144.580 129.632 165.339 1.00 102.84 ? 101 ILE D CB  1 
ATOM   5957  C CG1 . ILE D  2 67  ? 144.393 129.721 163.822 1.00 103.23 ? 101 ILE D CG1 1 
ATOM   5958  C CG2 . ILE D  2 67  ? 145.954 130.140 165.746 1.00 102.26 ? 101 ILE D CG2 1 
ATOM   5959  C CD1 . ILE D  2 67  ? 144.433 131.134 163.279 1.00 101.13 ? 101 ILE D CD1 1 
ATOM   5960  N N   . TYR D  2 68  ? 145.956 126.788 164.683 1.00 107.69 ? 102 TYR D N   1 
ATOM   5961  C CA  . TYR D  2 68  ? 147.141 125.966 164.502 1.00 109.77 ? 102 TYR D CA  1 
ATOM   5962  C C   . TYR D  2 68  ? 148.066 126.565 163.454 1.00 113.01 ? 102 TYR D C   1 
ATOM   5963  O O   . TYR D  2 68  ? 147.627 127.310 162.572 1.00 114.90 ? 102 TYR D O   1 
ATOM   5964  C CB  . TYR D  2 68  ? 146.740 124.549 164.093 1.00 107.31 ? 102 TYR D CB  1 
ATOM   5965  C CG  . TYR D  2 68  ? 146.108 123.726 165.193 1.00 110.13 ? 102 TYR D CG  1 
ATOM   5966  C CD1 . TYR D  2 68  ? 145.690 122.430 164.949 1.00 116.88 ? 102 TYR D CD1 1 
ATOM   5967  C CD2 . TYR D  2 68  ? 145.975 124.220 166.483 1.00 111.40 ? 102 TYR D CD2 1 
ATOM   5968  C CE1 . TYR D  2 68  ? 145.126 121.658 165.941 1.00 119.63 ? 102 TYR D CE1 1 
ATOM   5969  C CE2 . TYR D  2 68  ? 145.411 123.454 167.487 1.00 116.43 ? 102 TYR D CE2 1 
ATOM   5970  C CZ  . TYR D  2 68  ? 144.989 122.172 167.209 1.00 123.12 ? 102 TYR D CZ  1 
ATOM   5971  O OH  . TYR D  2 68  ? 144.428 121.398 168.198 1.00 132.63 ? 102 TYR D OH  1 
ATOM   5972  N N   . PRO D  2 69  ? 149.364 126.255 163.527 1.00 115.19 ? 103 PRO D N   1 
ATOM   5973  C CA  . PRO D  2 69  ? 150.303 126.788 162.527 1.00 113.53 ? 103 PRO D CA  1 
ATOM   5974  C C   . PRO D  2 69  ? 149.956 126.417 161.096 1.00 111.43 ? 103 PRO D C   1 
ATOM   5975  O O   . PRO D  2 69  ? 150.232 127.210 160.189 1.00 110.32 ? 103 PRO D O   1 
ATOM   5976  C CB  . PRO D  2 69  ? 151.648 126.182 162.956 1.00 119.54 ? 103 PRO D CB  1 
ATOM   5977  C CG  . PRO D  2 69  ? 151.274 124.999 163.808 1.00 119.06 ? 103 PRO D CG  1 
ATOM   5978  C CD  . PRO D  2 69  ? 150.073 125.480 164.558 1.00 118.15 ? 103 PRO D CD  1 
ATOM   5979  N N   . ASN D  2 70  ? 149.353 125.253 160.855 1.00 108.51 ? 104 ASN D N   1 
ATOM   5980  C CA  . ASN D  2 70  ? 148.869 124.925 159.524 1.00 107.67 ? 104 ASN D CA  1 
ATOM   5981  C C   . ASN D  2 70  ? 147.420 125.373 159.292 1.00 110.36 ? 104 ASN D C   1 
ATOM   5982  O O   . ASN D  2 70  ? 146.729 124.820 158.428 1.00 114.54 ? 104 ASN D O   1 
ATOM   5983  C CB  . ASN D  2 70  ? 149.097 123.434 159.223 1.00 109.86 ? 104 ASN D CB  1 
ATOM   5984  C CG  . ASN D  2 70  ? 147.913 122.530 159.549 1.00 108.96 ? 104 ASN D CG  1 
ATOM   5985  O OD1 . ASN D  2 70  ? 147.116 122.222 158.668 1.00 110.71 ? 104 ASN D OD1 1 
ATOM   5986  N ND2 . ASN D  2 70  ? 147.858 122.026 160.782 1.00 110.24 ? 104 ASN D ND2 1 
ATOM   5987  N N   . ALA D  2 71  ? 146.972 126.396 160.022 1.00 108.77 ? 105 ALA D N   1 
ATOM   5988  C CA  . ALA D  2 71  ? 145.783 127.208 159.766 1.00 99.61  ? 105 ALA D CA  1 
ATOM   5989  C C   . ALA D  2 71  ? 144.474 126.524 160.132 1.00 99.42  ? 105 ALA D C   1 
ATOM   5990  O O   . ALA D  2 71  ? 143.413 127.143 159.985 1.00 99.95  ? 105 ALA D O   1 
ATOM   5991  C CB  . ALA D  2 71  ? 145.691 127.676 158.304 1.00 97.31  ? 105 ALA D CB  1 
ATOM   5992  N N   . SER D  2 72  ? 144.499 125.279 160.593 1.00 104.32 ? 106 SER D N   1 
ATOM   5993  C CA  . SER D  2 72  ? 143.271 124.624 161.014 1.00 100.58 ? 106 SER D CA  1 
ATOM   5994  C C   . SER D  2 72  ? 142.725 125.286 162.272 1.00 105.09 ? 106 SER D C   1 
ATOM   5995  O O   . SER D  2 72  ? 143.487 125.752 163.125 1.00 108.88 ? 106 SER D O   1 
ATOM   5996  C CB  . SER D  2 72  ? 143.515 123.139 161.262 1.00 106.72 ? 106 SER D CB  1 
ATOM   5997  O OG  . SER D  2 72  ? 144.197 122.549 160.171 1.00 114.81 ? 106 SER D OG  1 
ATOM   5998  N N   . LEU D  2 73  ? 141.401 125.340 162.378 1.00 105.10 ? 107 LEU D N   1 
ATOM   5999  C CA  . LEU D  2 73  ? 140.725 125.873 163.553 1.00 100.01 ? 107 LEU D CA  1 
ATOM   6000  C C   . LEU D  2 73  ? 140.010 124.741 164.274 1.00 102.97 ? 107 LEU D C   1 
ATOM   6001  O O   . LEU D  2 73  ? 139.268 123.974 163.653 1.00 105.75 ? 107 LEU D O   1 
ATOM   6002  C CB  . LEU D  2 73  ? 139.729 126.967 163.163 1.00 92.97  ? 107 LEU D CB  1 
ATOM   6003  C CG  . LEU D  2 73  ? 138.927 127.574 164.315 1.00 93.91  ? 107 LEU D CG  1 
ATOM   6004  C CD1 . LEU D  2 73  ? 139.820 128.400 165.222 1.00 99.38  ? 107 LEU D CD1 1 
ATOM   6005  C CD2 . LEU D  2 73  ? 137.780 128.415 163.782 1.00 92.52  ? 107 LEU D CD2 1 
ATOM   6006  N N   . LEU D  2 74  ? 140.239 124.636 165.580 1.00 100.63 ? 108 LEU D N   1 
ATOM   6007  C CA  . LEU D  2 74  ? 139.629 123.606 166.408 1.00 100.50 ? 108 LEU D CA  1 
ATOM   6008  C C   . LEU D  2 74  ? 138.666 124.264 167.383 1.00 108.69 ? 108 LEU D C   1 
ATOM   6009  O O   . LEU D  2 74  ? 139.059 125.160 168.137 1.00 116.00 ? 108 LEU D O   1 
ATOM   6010  C CB  . LEU D  2 74  ? 140.690 122.807 167.171 1.00 104.21 ? 108 LEU D CB  1 
ATOM   6011  C CG  . LEU D  2 74  ? 140.162 121.830 168.224 1.00 107.15 ? 108 LEU D CG  1 
ATOM   6012  C CD1 . LEU D  2 74  ? 139.268 120.779 167.582 1.00 108.77 ? 108 LEU D CD1 1 
ATOM   6013  C CD2 . LEU D  2 74  ? 141.298 121.176 168.994 1.00 111.37 ? 108 LEU D CD2 1 
ATOM   6014  N N   . ILE D  2 75  ? 137.412 123.824 167.365 1.00 109.19 ? 109 ILE D N   1 
ATOM   6015  C CA  . ILE D  2 75  ? 136.381 124.329 168.265 1.00 105.39 ? 109 ILE D CA  1 
ATOM   6016  C C   . ILE D  2 75  ? 135.921 123.177 169.146 1.00 113.84 ? 109 ILE D C   1 
ATOM   6017  O O   . ILE D  2 75  ? 135.344 122.202 168.649 1.00 116.97 ? 109 ILE D O   1 
ATOM   6018  C CB  . ILE D  2 75  ? 135.198 124.936 167.495 1.00 98.37  ? 109 ILE D CB  1 
ATOM   6019  C CG1 . ILE D  2 75  ? 135.621 126.226 166.791 1.00 99.28  ? 109 ILE D CG1 1 
ATOM   6020  C CG2 . ILE D  2 75  ? 134.033 125.200 168.432 1.00 114.51 ? 109 ILE D CG2 1 
ATOM   6021  C CD1 . ILE D  2 75  ? 134.678 126.657 165.701 1.00 96.33  ? 109 ILE D CD1 1 
ATOM   6022  N N   . GLN D  2 76  ? 136.163 123.296 170.446 1.00 114.96 ? 110 GLN D N   1 
ATOM   6023  C CA  . GLN D  2 76  ? 135.744 122.315 171.434 1.00 120.35 ? 110 GLN D CA  1 
ATOM   6024  C C   . GLN D  2 76  ? 134.484 122.809 172.132 1.00 130.03 ? 110 GLN D C   1 
ATOM   6025  O O   . GLN D  2 76  ? 134.147 123.997 172.073 1.00 133.20 ? 110 GLN D O   1 
ATOM   6026  C CB  . GLN D  2 76  ? 136.851 122.071 172.463 1.00 119.00 ? 110 GLN D CB  1 
ATOM   6027  C CG  . GLN D  2 76  ? 138.207 121.764 171.855 1.00 123.49 ? 110 GLN D CG  1 
ATOM   6028  C CD  . GLN D  2 76  ? 139.352 122.005 172.824 1.00 133.18 ? 110 GLN D CD  1 
ATOM   6029  O OE1 . GLN D  2 76  ? 139.170 122.595 173.889 1.00 134.56 ? 110 GLN D OE1 1 
ATOM   6030  N NE2 . GLN D  2 76  ? 140.540 121.548 172.456 1.00 137.81 ? 110 GLN D NE2 1 
ATOM   6031  N N   . ASN D  2 77  ? 133.791 121.888 172.803 1.00 132.70 ? 111 ASN D N   1 
ATOM   6032  C CA  . ASN D  2 77  ? 132.562 122.216 173.522 1.00 133.72 ? 111 ASN D CA  1 
ATOM   6033  C C   . ASN D  2 77  ? 131.559 122.899 172.597 1.00 135.51 ? 111 ASN D C   1 
ATOM   6034  O O   . ASN D  2 77  ? 130.991 123.946 172.916 1.00 141.08 ? 111 ASN D O   1 
ATOM   6035  C CB  . ASN D  2 77  ? 132.867 123.096 174.737 1.00 144.32 ? 111 ASN D CB  1 
ATOM   6036  C CG  . ASN D  2 77  ? 131.802 123.016 175.819 1.00 164.90 ? 111 ASN D CG  1 
ATOM   6037  O OD1 . ASN D  2 77  ? 130.793 123.715 175.755 1.00 167.29 ? 111 ASN D OD1 1 
ATOM   6038  N ND2 . ASN D  2 77  ? 132.037 122.175 176.820 1.00 176.29 ? 111 ASN D ND2 1 
ATOM   6039  N N   . VAL D  2 78  ? 131.350 122.297 171.425 1.00 131.12 ? 112 VAL D N   1 
ATOM   6040  C CA  . VAL D  2 78  ? 130.473 122.917 170.443 1.00 128.88 ? 112 VAL D CA  1 
ATOM   6041  C C   . VAL D  2 78  ? 129.028 122.887 170.943 1.00 133.58 ? 112 VAL D C   1 
ATOM   6042  O O   . VAL D  2 78  ? 128.588 121.954 171.628 1.00 139.09 ? 112 VAL D O   1 
ATOM   6043  C CB  . VAL D  2 78  ? 130.607 122.232 169.073 1.00 126.88 ? 112 VAL D CB  1 
ATOM   6044  C CG1 . VAL D  2 78  ? 129.773 120.957 169.005 1.00 133.61 ? 112 VAL D CG1 1 
ATOM   6045  C CG2 . VAL D  2 78  ? 130.209 123.187 167.952 1.00 127.45 ? 112 VAL D CG2 1 
ATOM   6046  N N   . THR D  2 79  ? 128.291 123.941 170.605 1.00 130.78 ? 113 THR D N   1 
ATOM   6047  C CA  . THR D  2 79  ? 126.905 124.097 171.013 1.00 131.81 ? 113 THR D CA  1 
ATOM   6048  C C   . THR D  2 79  ? 126.068 124.385 169.778 1.00 131.37 ? 113 THR D C   1 
ATOM   6049  O O   . THR D  2 79  ? 126.594 124.666 168.698 1.00 131.94 ? 113 THR D O   1 
ATOM   6050  C CB  . THR D  2 79  ? 126.734 125.214 172.050 1.00 131.93 ? 113 THR D CB  1 
ATOM   6051  O OG1 . THR D  2 79  ? 127.189 126.452 171.493 1.00 133.42 ? 113 THR D OG1 1 
ATOM   6052  C CG2 . THR D  2 79  ? 127.530 124.900 173.308 1.00 132.84 ? 113 THR D CG2 1 
ATOM   6053  N N   . GLN D  2 80  ? 124.748 124.302 169.945 1.00 130.29 ? 114 GLN D N   1 
ATOM   6054  C CA  . GLN D  2 80  ? 123.848 124.479 168.811 1.00 128.53 ? 114 GLN D CA  1 
ATOM   6055  C C   . GLN D  2 80  ? 123.883 125.912 168.293 1.00 128.14 ? 114 GLN D C   1 
ATOM   6056  O O   . GLN D  2 80  ? 123.441 126.186 167.171 1.00 131.52 ? 114 GLN D O   1 
ATOM   6057  C CB  . GLN D  2 80  ? 122.429 124.078 169.207 1.00 127.26 ? 114 GLN D CB  1 
ATOM   6058  C CG  . GLN D  2 80  ? 121.529 123.757 168.028 1.00 127.89 ? 114 GLN D CG  1 
ATOM   6059  C CD  . GLN D  2 80  ? 120.243 123.066 168.442 1.00 136.96 ? 114 GLN D CD  1 
ATOM   6060  O OE1 . GLN D  2 80  ? 119.744 123.267 169.548 1.00 143.73 ? 114 GLN D OE1 1 
ATOM   6061  N NE2 . GLN D  2 80  ? 119.708 122.233 167.555 1.00 138.17 ? 114 GLN D NE2 1 
ATOM   6062  N N   . ASN D  2 81  ? 124.405 126.843 169.096 1.00 126.61 ? 115 ASN D N   1 
ATOM   6063  C CA  . ASN D  2 81  ? 124.509 128.231 168.660 1.00 129.35 ? 115 ASN D CA  1 
ATOM   6064  C C   . ASN D  2 81  ? 125.644 128.443 167.667 1.00 129.94 ? 115 ASN D C   1 
ATOM   6065  O O   . ASN D  2 81  ? 125.665 129.467 166.976 1.00 132.83 ? 115 ASN D O   1 
ATOM   6066  C CB  . ASN D  2 81  ? 124.697 129.146 169.873 1.00 131.43 ? 115 ASN D CB  1 
ATOM   6067  C CG  . ASN D  2 81  ? 124.516 130.613 169.532 1.00 141.26 ? 115 ASN D CG  1 
ATOM   6068  O OD1 . ASN D  2 81  ? 125.476 131.383 169.524 1.00 146.52 ? 115 ASN D OD1 1 
ATOM   6069  N ND2 . ASN D  2 81  ? 123.281 131.006 169.248 1.00 138.69 ? 115 ASN D ND2 1 
ATOM   6070  N N   . ASP D  2 82  ? 126.584 127.502 167.574 1.00 125.33 ? 116 ASP D N   1 
ATOM   6071  C CA  . ASP D  2 82  ? 127.735 127.653 166.694 1.00 117.98 ? 116 ASP D CA  1 
ATOM   6072  C C   . ASP D  2 82  ? 127.427 127.341 165.235 1.00 115.83 ? 116 ASP D C   1 
ATOM   6073  O O   . ASP D  2 82  ? 128.268 127.622 164.374 1.00 115.14 ? 116 ASP D O   1 
ATOM   6074  C CB  . ASP D  2 82  ? 128.883 126.759 167.168 1.00 119.61 ? 116 ASP D CB  1 
ATOM   6075  C CG  . ASP D  2 82  ? 129.422 127.171 168.522 1.00 129.53 ? 116 ASP D CG  1 
ATOM   6076  O OD1 . ASP D  2 82  ? 130.220 128.129 168.577 1.00 130.58 ? 116 ASP D OD1 1 
ATOM   6077  O OD2 . ASP D  2 82  ? 129.051 126.535 169.531 1.00 134.41 ? 116 ASP D OD2 1 
ATOM   6078  N N   . THR D  2 83  ? 126.263 126.767 164.939 1.00 115.79 ? 117 THR D N   1 
ATOM   6079  C CA  . THR D  2 83  ? 125.924 126.410 163.566 1.00 111.98 ? 117 THR D CA  1 
ATOM   6080  C C   . THR D  2 83  ? 125.894 127.649 162.683 1.00 111.84 ? 117 THR D C   1 
ATOM   6081  O O   . THR D  2 83  ? 125.079 128.553 162.894 1.00 122.56 ? 117 THR D O   1 
ATOM   6082  C CB  . THR D  2 83  ? 124.572 125.701 163.526 1.00 114.83 ? 117 THR D CB  1 
ATOM   6083  O OG1 . THR D  2 83  ? 124.590 124.580 164.418 1.00 119.35 ? 117 THR D OG1 1 
ATOM   6084  C CG2 . THR D  2 83  ? 124.267 125.217 162.117 1.00 113.41 ? 117 THR D CG2 1 
ATOM   6085  N N   . GLY D  2 84  ? 126.780 127.691 161.696 1.00 104.58 ? 118 GLY D N   1 
ATOM   6086  C CA  . GLY D  2 84  ? 126.836 128.827 160.802 1.00 108.54 ? 118 GLY D CA  1 
ATOM   6087  C C   . GLY D  2 84  ? 128.044 128.737 159.892 1.00 107.81 ? 118 GLY D C   1 
ATOM   6088  O O   . GLY D  2 84  ? 128.737 127.719 159.842 1.00 108.61 ? 118 GLY D O   1 
ATOM   6089  N N   . PHE D  2 85  ? 128.276 129.828 159.171 1.00 103.42 ? 119 PHE D N   1 
ATOM   6090  C CA  . PHE D  2 85  ? 129.394 129.927 158.248 1.00 99.62  ? 119 PHE D CA  1 
ATOM   6091  C C   . PHE D  2 85  ? 130.608 130.532 158.941 1.00 99.27  ? 119 PHE D C   1 
ATOM   6092  O O   . PHE D  2 85  ? 130.485 131.387 159.821 1.00 99.79  ? 119 PHE D O   1 
ATOM   6093  C CB  . PHE D  2 85  ? 129.018 130.773 157.031 1.00 101.68 ? 119 PHE D CB  1 
ATOM   6094  C CG  . PHE D  2 85  ? 127.982 130.141 156.148 1.00 106.82 ? 119 PHE D CG  1 
ATOM   6095  C CD1 . PHE D  2 85  ? 126.635 130.240 156.455 1.00 110.06 ? 119 PHE D CD1 1 
ATOM   6096  C CD2 . PHE D  2 85  ? 128.354 129.450 155.008 1.00 111.86 ? 119 PHE D CD2 1 
ATOM   6097  C CE1 . PHE D  2 85  ? 125.681 129.660 155.643 1.00 116.05 ? 119 PHE D CE1 1 
ATOM   6098  C CE2 . PHE D  2 85  ? 127.404 128.868 154.193 1.00 118.04 ? 119 PHE D CE2 1 
ATOM   6099  C CZ  . PHE D  2 85  ? 126.066 128.973 154.511 1.00 118.79 ? 119 PHE D CZ  1 
ATOM   6100  N N   . TYR D  2 86  ? 131.788 130.067 158.541 1.00 99.60  ? 120 TYR D N   1 
ATOM   6101  C CA  . TYR D  2 86  ? 133.051 130.603 159.026 1.00 94.18  ? 120 TYR D CA  1 
ATOM   6102  C C   . TYR D  2 86  ? 133.945 130.925 157.840 1.00 94.38  ? 120 TYR D C   1 
ATOM   6103  O O   . TYR D  2 86  ? 134.057 130.129 156.904 1.00 99.63  ? 120 TYR D O   1 
ATOM   6104  C CB  . TYR D  2 86  ? 133.762 129.621 159.966 1.00 88.71  ? 120 TYR D CB  1 
ATOM   6105  C CG  . TYR D  2 86  ? 133.016 129.342 161.250 1.00 94.00  ? 120 TYR D CG  1 
ATOM   6106  C CD1 . TYR D  2 86  ? 131.900 128.519 161.266 1.00 97.45  ? 120 TYR D CD1 1 
ATOM   6107  C CD2 . TYR D  2 86  ? 133.431 129.904 162.448 1.00 95.59  ? 120 TYR D CD2 1 
ATOM   6108  C CE1 . TYR D  2 86  ? 131.218 128.266 162.437 1.00 100.80 ? 120 TYR D CE1 1 
ATOM   6109  C CE2 . TYR D  2 86  ? 132.756 129.656 163.624 1.00 98.65  ? 120 TYR D CE2 1 
ATOM   6110  C CZ  . TYR D  2 86  ? 131.650 128.836 163.613 1.00 101.18 ? 120 TYR D CZ  1 
ATOM   6111  O OH  . TYR D  2 86  ? 130.973 128.585 164.784 1.00 110.48 ? 120 TYR D OH  1 
ATOM   6112  N N   . THR D  2 87  ? 134.582 132.090 157.887 1.00 89.22  ? 121 THR D N   1 
ATOM   6113  C CA  . THR D  2 87  ? 135.454 132.549 156.817 1.00 93.30  ? 121 THR D CA  1 
ATOM   6114  C C   . THR D  2 87  ? 136.887 132.631 157.319 1.00 90.60  ? 121 THR D C   1 
ATOM   6115  O O   . THR D  2 87  ? 137.140 133.099 158.433 1.00 94.54  ? 121 THR D O   1 
ATOM   6116  C CB  . THR D  2 87  ? 135.019 133.916 156.284 1.00 99.79  ? 121 THR D CB  1 
ATOM   6117  O OG1 . THR D  2 87  ? 134.837 134.822 157.379 1.00 103.73 ? 121 THR D OG1 1 
ATOM   6118  C CG2 . THR D  2 87  ? 133.721 133.794 155.506 1.00 105.20 ? 121 THR D CG2 1 
ATOM   6119  N N   . LEU D  2 88  ? 137.818 132.172 156.491 1.00 86.43  ? 122 LEU D N   1 
ATOM   6120  C CA  . LEU D  2 88  ? 139.241 132.232 156.789 1.00 84.75  ? 122 LEU D CA  1 
ATOM   6121  C C   . LEU D  2 88  ? 139.883 133.305 155.925 1.00 89.62  ? 122 LEU D C   1 
ATOM   6122  O O   . LEU D  2 88  ? 139.723 133.299 154.700 1.00 97.40  ? 122 LEU D O   1 
ATOM   6123  C CB  . LEU D  2 88  ? 139.913 130.880 156.540 1.00 86.25  ? 122 LEU D CB  1 
ATOM   6124  C CG  . LEU D  2 88  ? 141.435 130.900 156.380 1.00 84.10  ? 122 LEU D CG  1 
ATOM   6125  C CD1 . LEU D  2 88  ? 142.112 131.305 157.679 1.00 84.63  ? 122 LEU D CD1 1 
ATOM   6126  C CD2 . LEU D  2 88  ? 141.945 129.551 155.907 1.00 91.44  ? 122 LEU D CD2 1 
ATOM   6127  N N   . GLN D  2 89  ? 140.601 134.223 156.562 1.00 88.68  ? 123 GLN D N   1 
ATOM   6128  C CA  . GLN D  2 89  ? 141.359 135.253 155.867 1.00 92.87  ? 123 GLN D CA  1 
ATOM   6129  C C   . GLN D  2 89  ? 142.829 134.867 155.887 1.00 94.41  ? 123 GLN D C   1 
ATOM   6130  O O   . GLN D  2 89  ? 143.399 134.639 156.958 1.00 101.21 ? 123 GLN D O   1 
ATOM   6131  C CB  . GLN D  2 89  ? 141.162 136.624 156.510 1.00 94.02  ? 123 GLN D CB  1 
ATOM   6132  C CG  . GLN D  2 89  ? 141.893 137.737 155.779 1.00 98.29  ? 123 GLN D CG  1 
ATOM   6133  C CD  . GLN D  2 89  ? 141.414 139.114 156.176 1.00 110.66 ? 123 GLN D CD  1 
ATOM   6134  O OE1 . GLN D  2 89  ? 140.932 139.880 155.342 1.00 117.17 ? 123 GLN D OE1 1 
ATOM   6135  N NE2 . GLN D  2 89  ? 141.550 139.443 157.455 1.00 110.10 ? 123 GLN D NE2 1 
ATOM   6136  N N   . VAL D  2 90  ? 143.435 134.796 154.708 1.00 89.29  ? 124 VAL D N   1 
ATOM   6137  C CA  . VAL D  2 90  ? 144.852 134.493 154.564 1.00 86.71  ? 124 VAL D CA  1 
ATOM   6138  C C   . VAL D  2 90  ? 145.536 135.710 153.965 1.00 94.82  ? 124 VAL D C   1 
ATOM   6139  O O   . VAL D  2 90  ? 145.152 136.177 152.887 1.00 102.41 ? 124 VAL D O   1 
ATOM   6140  C CB  . VAL D  2 90  ? 145.081 133.247 153.692 1.00 85.72  ? 124 VAL D CB  1 
ATOM   6141  C CG1 . VAL D  2 90  ? 146.550 133.100 153.366 1.00 93.07  ? 124 VAL D CG1 1 
ATOM   6142  C CG2 . VAL D  2 90  ? 144.576 132.010 154.408 1.00 87.94  ? 124 VAL D CG2 1 
ATOM   6143  N N   . ILE D  2 91  ? 146.542 136.222 154.665 1.00 91.60  ? 125 ILE D N   1 
ATOM   6144  C CA  . ILE D  2 91  ? 147.303 137.380 154.218 1.00 92.67  ? 125 ILE D CA  1 
ATOM   6145  C C   . ILE D  2 91  ? 148.652 136.894 153.713 1.00 95.96  ? 125 ILE D C   1 
ATOM   6146  O O   . ILE D  2 91  ? 149.456 136.353 154.481 1.00 104.70 ? 125 ILE D O   1 
ATOM   6147  C CB  . ILE D  2 91  ? 147.464 138.415 155.342 1.00 90.07  ? 125 ILE D CB  1 
ATOM   6148  C CG1 . ILE D  2 91  ? 146.093 138.925 155.783 1.00 97.85  ? 125 ILE D CG1 1 
ATOM   6149  C CG2 . ILE D  2 91  ? 148.343 139.562 154.890 1.00 97.18  ? 125 ILE D CG2 1 
ATOM   6150  C CD1 . ILE D  2 91  ? 146.127 139.750 157.038 1.00 105.31 ? 125 ILE D CD1 1 
ATOM   6151  N N   . LYS D  2 92  ? 148.897 137.086 152.422 1.00 93.20  ? 126 LYS D N   1 
ATOM   6152  C CA  . LYS D  2 92  ? 150.118 136.619 151.793 1.00 100.78 ? 126 LYS D CA  1 
ATOM   6153  C C   . LYS D  2 92  ? 151.284 137.541 152.146 1.00 105.41 ? 126 LYS D C   1 
ATOM   6154  O O   . LYS D  2 92  ? 151.142 138.514 152.891 1.00 106.29 ? 126 LYS D O   1 
ATOM   6155  C CB  . LYS D  2 92  ? 149.925 136.526 150.281 1.00 103.57 ? 126 LYS D CB  1 
ATOM   6156  C CG  . LYS D  2 92  ? 148.575 135.937 149.889 1.00 106.55 ? 126 LYS D CG  1 
ATOM   6157  C CD  . LYS D  2 92  ? 148.239 136.185 148.427 1.00 108.28 ? 126 LYS D CD  1 
ATOM   6158  C CE  . LYS D  2 92  ? 149.434 135.940 147.525 1.00 118.64 ? 126 LYS D CE  1 
ATOM   6159  N NZ  . LYS D  2 92  ? 149.905 134.530 147.607 1.00 124.85 ? 126 LYS D NZ  1 
ATOM   6160  N N   . SER D  2 93  ? 152.460 137.213 151.603 1.00 107.78 ? 127 SER D N   1 
ATOM   6161  C CA  . SER D  2 93  ? 153.662 137.981 151.917 1.00 105.54 ? 127 SER D CA  1 
ATOM   6162  C C   . SER D  2 93  ? 153.537 139.432 151.475 1.00 106.26 ? 127 SER D C   1 
ATOM   6163  O O   . SER D  2 93  ? 153.937 140.341 152.212 1.00 101.80 ? 127 SER D O   1 
ATOM   6164  C CB  . SER D  2 93  ? 154.883 137.334 151.266 1.00 109.74 ? 127 SER D CB  1 
ATOM   6165  O OG  . SER D  2 93  ? 154.629 137.023 149.908 1.00 115.86 ? 127 SER D OG  1 
ATOM   6166  N N   . ASP D  2 94  ? 152.986 139.673 150.288 1.00 104.22 ? 128 ASP D N   1 
ATOM   6167  C CA  . ASP D  2 94  ? 152.742 141.024 149.804 1.00 101.50 ? 128 ASP D CA  1 
ATOM   6168  C C   . ASP D  2 94  ? 151.535 141.676 150.465 1.00 101.82 ? 128 ASP D C   1 
ATOM   6169  O O   . ASP D  2 94  ? 151.129 142.766 150.050 1.00 103.42 ? 128 ASP D O   1 
ATOM   6170  C CB  . ASP D  2 94  ? 152.579 141.018 148.279 1.00 103.92 ? 128 ASP D CB  1 
ATOM   6171  C CG  . ASP D  2 94  ? 151.478 140.086 147.803 1.00 112.50 ? 128 ASP D CG  1 
ATOM   6172  O OD1 . ASP D  2 94  ? 150.473 139.902 148.520 1.00 114.89 ? 128 ASP D OD1 1 
ATOM   6173  O OD2 . ASP D  2 94  ? 151.620 139.531 146.694 1.00 115.60 ? 128 ASP D OD2 1 
ATOM   6174  N N   . LEU D  2 95  ? 150.951 141.023 151.469 1.00 101.15 ? 129 LEU D N   1 
ATOM   6175  C CA  . LEU D  2 95  ? 149.847 141.525 152.279 1.00 100.07 ? 129 LEU D CA  1 
ATOM   6176  C C   . LEU D  2 95  ? 148.561 141.706 151.486 1.00 101.22 ? 129 LEU D C   1 
ATOM   6177  O O   . LEU D  2 95  ? 147.730 142.547 151.850 1.00 101.70 ? 129 LEU D O   1 
ATOM   6178  C CB  . LEU D  2 95  ? 150.221 142.834 152.982 1.00 96.06  ? 129 LEU D CB  1 
ATOM   6179  C CG  . LEU D  2 95  ? 150.662 142.677 154.437 1.00 100.64 ? 129 LEU D CG  1 
ATOM   6180  C CD1 . LEU D  2 95  ? 151.763 141.641 154.559 1.00 107.16 ? 129 LEU D CD1 1 
ATOM   6181  C CD2 . LEU D  2 95  ? 151.151 144.001 154.965 1.00 103.45 ? 129 LEU D CD2 1 
ATOM   6182  N N   . VAL D  2 96  ? 148.370 140.941 150.416 1.00 101.19 ? 130 VAL D N   1 
ATOM   6183  C CA  . VAL D  2 96  ? 147.094 140.911 149.711 1.00 101.76 ? 130 VAL D CA  1 
ATOM   6184  C C   . VAL D  2 96  ? 146.255 139.776 150.280 1.00 105.37 ? 130 VAL D C   1 
ATOM   6185  O O   . VAL D  2 96  ? 146.686 138.618 150.302 1.00 107.19 ? 130 VAL D O   1 
ATOM   6186  C CB  . VAL D  2 96  ? 147.308 140.744 148.199 1.00 100.76 ? 130 VAL D CB  1 
ATOM   6187  C CG1 . VAL D  2 96  ? 145.979 140.518 147.498 1.00 102.58 ? 130 VAL D CG1 1 
ATOM   6188  C CG2 . VAL D  2 96  ? 148.015 141.963 147.630 1.00 102.53 ? 130 VAL D CG2 1 
ATOM   6189  N N   . ASN D  2 97  ? 145.053 140.106 150.742 1.00 104.51 ? 131 ASN D N   1 
ATOM   6190  C CA  . ASN D  2 97  ? 144.220 139.141 151.443 1.00 99.92  ? 131 ASN D CA  1 
ATOM   6191  C C   . ASN D  2 97  ? 143.641 138.109 150.484 1.00 102.35 ? 131 ASN D C   1 
ATOM   6192  O O   . ASN D  2 97  ? 143.307 138.419 149.337 1.00 108.08 ? 131 ASN D O   1 
ATOM   6193  C CB  . ASN D  2 97  ? 143.089 139.858 152.179 1.00 104.11 ? 131 ASN D CB  1 
ATOM   6194  C CG  . ASN D  2 97  ? 143.595 140.961 153.087 1.00 109.66 ? 131 ASN D CG  1 
ATOM   6195  O OD1 . ASN D  2 97  ? 144.467 141.741 152.706 1.00 110.33 ? 131 ASN D OD1 1 
ATOM   6196  N ND2 . ASN D  2 97  ? 143.048 141.032 154.294 1.00 109.81 ? 131 ASN D ND2 1 
ATOM   6197  N N   . GLU D  2 98  ? 143.525 136.875 150.967 1.00 100.94 ? 132 GLU D N   1 
ATOM   6198  C CA  . GLU D  2 98  ? 142.841 135.799 150.262 1.00 101.76 ? 132 GLU D CA  1 
ATOM   6199  C C   . GLU D  2 98  ? 141.791 135.223 151.197 1.00 105.18 ? 132 GLU D C   1 
ATOM   6200  O O   . GLU D  2 98  ? 142.027 135.116 152.405 1.00 109.66 ? 132 GLU D O   1 
ATOM   6201  C CB  . GLU D  2 98  ? 143.816 134.710 149.808 1.00 103.24 ? 132 GLU D CB  1 
ATOM   6202  C CG  . GLU D  2 98  ? 143.351 133.946 148.582 1.00 115.44 ? 132 GLU D CG  1 
ATOM   6203  C CD  . GLU D  2 98  ? 144.496 133.300 147.830 1.00 125.51 ? 132 GLU D CD  1 
ATOM   6204  O OE1 . GLU D  2 98  ? 145.661 133.664 148.092 1.00 120.67 ? 132 GLU D OE1 1 
ATOM   6205  O OE2 . GLU D  2 98  ? 144.231 132.426 146.978 1.00 128.85 ? 132 GLU D OE2 1 
ATOM   6206  N N   . GLU D  2 99  ? 140.639 134.854 150.647 1.00 103.66 ? 133 GLU D N   1 
ATOM   6207  C CA  . GLU D  2 99  ? 139.479 134.530 151.460 1.00 105.50 ? 133 GLU D CA  1 
ATOM   6208  C C   . GLU D  2 99  ? 138.920 133.163 151.086 1.00 109.82 ? 133 GLU D C   1 
ATOM   6209  O O   . GLU D  2 99  ? 138.954 132.746 149.925 1.00 117.27 ? 133 GLU D O   1 
ATOM   6210  C CB  . GLU D  2 99  ? 138.391 135.596 151.299 1.00 108.74 ? 133 GLU D CB  1 
ATOM   6211  C CG  . GLU D  2 99  ? 138.851 136.990 151.685 1.00 120.71 ? 133 GLU D CG  1 
ATOM   6212  C CD  . GLU D  2 99  ? 137.928 137.670 152.669 1.00 135.64 ? 133 GLU D CD  1 
ATOM   6213  O OE1 . GLU D  2 99  ? 138.430 138.468 153.487 1.00 133.90 ? 133 GLU D OE1 1 
ATOM   6214  O OE2 . GLU D  2 99  ? 136.708 137.405 152.629 1.00 145.37 ? 133 GLU D OE2 1 
ATOM   6215  N N   . ALA D  2 100 ? 138.399 132.472 152.096 1.00 105.46 ? 134 ALA D N   1 
ATOM   6216  C CA  . ALA D  2 100 ? 137.715 131.202 151.907 1.00 103.13 ? 134 ALA D CA  1 
ATOM   6217  C C   . ALA D  2 100 ? 136.559 131.134 152.893 1.00 101.34 ? 134 ALA D C   1 
ATOM   6218  O O   . ALA D  2 100 ? 136.319 132.067 153.663 1.00 107.48 ? 134 ALA D O   1 
ATOM   6219  C CB  . ALA D  2 100 ? 138.664 130.015 152.088 1.00 106.02 ? 134 ALA D CB  1 
ATOM   6220  N N   . THR D  2 101 ? 135.839 130.015 152.867 1.00 97.87  ? 135 THR D N   1 
ATOM   6221  C CA  . THR D  2 101 ? 134.678 129.847 153.727 1.00 97.80  ? 135 THR D CA  1 
ATOM   6222  C C   . THR D  2 101 ? 134.485 128.375 154.060 1.00 98.11  ? 135 THR D C   1 
ATOM   6223  O O   . THR D  2 101 ? 134.999 127.485 153.378 1.00 105.03 ? 135 THR D O   1 
ATOM   6224  C CB  . THR D  2 101 ? 133.406 130.409 153.078 1.00 104.49 ? 135 THR D CB  1 
ATOM   6225  O OG1 . THR D  2 101 ? 132.356 130.464 154.051 1.00 106.21 ? 135 THR D OG1 1 
ATOM   6226  C CG2 . THR D  2 101 ? 132.968 129.534 151.915 1.00 105.78 ? 135 THR D CG2 1 
ATOM   6227  N N   . GLY D  2 102 ? 133.733 128.136 155.130 1.00 93.29  ? 136 GLY D N   1 
ATOM   6228  C CA  . GLY D  2 102 ? 133.410 126.789 155.558 1.00 93.52  ? 136 GLY D CA  1 
ATOM   6229  C C   . GLY D  2 102 ? 132.287 126.824 156.566 1.00 97.49  ? 136 GLY D C   1 
ATOM   6230  O O   . GLY D  2 102 ? 132.038 127.848 157.211 1.00 102.92 ? 136 GLY D O   1 
ATOM   6231  N N   . GLN D  2 103 ? 131.606 125.689 156.700 1.00 96.00  ? 137 GLN D N   1 
ATOM   6232  C CA  . GLN D  2 103 ? 130.433 125.624 157.558 1.00 102.22 ? 137 GLN D CA  1 
ATOM   6233  C C   . GLN D  2 103 ? 130.278 124.218 158.112 1.00 106.90 ? 137 GLN D C   1 
ATOM   6234  O O   . GLN D  2 103 ? 130.824 123.250 157.577 1.00 108.81 ? 137 GLN D O   1 
ATOM   6235  C CB  . GLN D  2 103 ? 129.163 126.030 156.803 1.00 107.27 ? 137 GLN D CB  1 
ATOM   6236  C CG  . GLN D  2 103 ? 128.702 125.000 155.786 1.00 111.42 ? 137 GLN D CG  1 
ATOM   6237  C CD  . GLN D  2 103 ? 127.635 125.535 154.854 1.00 122.67 ? 137 GLN D CD  1 
ATOM   6238  O OE1 . GLN D  2 103 ? 127.879 125.738 153.665 1.00 126.50 ? 137 GLN D OE1 1 
ATOM   6239  N NE2 . GLN D  2 103 ? 126.443 125.768 155.390 1.00 123.44 ? 137 GLN D NE2 1 
ATOM   6240  N N   . PHE D  2 104 ? 129.518 124.121 159.200 1.00 105.70 ? 138 PHE D N   1 
ATOM   6241  C CA  . PHE D  2 104 ? 129.161 122.839 159.788 1.00 107.97 ? 138 PHE D CA  1 
ATOM   6242  C C   . PHE D  2 104 ? 127.855 123.006 160.546 1.00 110.26 ? 138 PHE D C   1 
ATOM   6243  O O   . PHE D  2 104 ? 127.484 124.113 160.944 1.00 114.30 ? 138 PHE D O   1 
ATOM   6244  C CB  . PHE D  2 104 ? 130.269 122.305 160.705 1.00 106.52 ? 138 PHE D CB  1 
ATOM   6245  C CG  . PHE D  2 104 ? 130.604 123.214 161.853 1.00 102.30 ? 138 PHE D CG  1 
ATOM   6246  C CD1 . PHE D  2 104 ? 129.916 123.127 163.051 1.00 104.14 ? 138 PHE D CD1 1 
ATOM   6247  C CD2 . PHE D  2 104 ? 131.619 124.147 161.738 1.00 102.43 ? 138 PHE D CD2 1 
ATOM   6248  C CE1 . PHE D  2 104 ? 130.228 123.959 164.107 1.00 105.85 ? 138 PHE D CE1 1 
ATOM   6249  C CE2 . PHE D  2 104 ? 131.936 124.980 162.791 1.00 99.31  ? 138 PHE D CE2 1 
ATOM   6250  C CZ  . PHE D  2 104 ? 131.239 124.887 163.976 1.00 102.77 ? 138 PHE D CZ  1 
ATOM   6251  N N   . HIS D  2 105 ? 127.161 121.890 160.741 1.00 111.75 ? 139 HIS D N   1 
ATOM   6252  C CA  . HIS D  2 105 ? 125.882 121.870 161.434 1.00 113.60 ? 139 HIS D CA  1 
ATOM   6253  C C   . HIS D  2 105 ? 126.021 121.132 162.757 1.00 117.51 ? 139 HIS D C   1 
ATOM   6254  O O   . HIS D  2 105 ? 126.680 120.091 162.833 1.00 123.03 ? 139 HIS D O   1 
ATOM   6255  C CB  . HIS D  2 105 ? 124.800 121.203 160.580 1.00 116.40 ? 139 HIS D CB  1 
ATOM   6256  C CG  . HIS D  2 105 ? 124.169 122.120 159.580 1.00 122.82 ? 139 HIS D CG  1 
ATOM   6257  N ND1 . HIS D  2 105 ? 124.737 122.389 158.353 1.00 127.05 ? 139 HIS D ND1 1 
ATOM   6258  C CD2 . HIS D  2 105 ? 123.015 122.828 159.624 1.00 123.90 ? 139 HIS D CD2 1 
ATOM   6259  C CE1 . HIS D  2 105 ? 123.961 123.224 157.685 1.00 129.05 ? 139 HIS D CE1 1 
ATOM   6260  N NE2 . HIS D  2 105 ? 122.911 123.507 158.434 1.00 134.52 ? 139 HIS D NE2 1 
ATOM   6261  N N   . VAL D  2 106 ? 125.398 121.679 163.797 1.00 113.97 ? 140 VAL D N   1 
ATOM   6262  C CA  . VAL D  2 106 ? 125.399 121.087 165.129 1.00 114.44 ? 140 VAL D CA  1 
ATOM   6263  C C   . VAL D  2 106 ? 124.009 120.535 165.398 1.00 119.03 ? 140 VAL D C   1 
ATOM   6264  O O   . VAL D  2 106 ? 123.006 121.228 165.185 1.00 126.00 ? 140 VAL D O   1 
ATOM   6265  C CB  . VAL D  2 106 ? 125.804 122.110 166.203 1.00 116.39 ? 140 VAL D CB  1 
ATOM   6266  C CG1 . VAL D  2 106 ? 126.016 121.417 167.538 1.00 126.32 ? 140 VAL D CG1 1 
ATOM   6267  C CG2 . VAL D  2 106 ? 127.058 122.853 165.778 1.00 116.29 ? 140 VAL D CG2 1 
ATOM   6268  N N   . TYR D  2 107 ? 123.948 119.294 165.864 1.00 123.02 ? 141 TYR D N   1 
ATOM   6269  C CA  . TYR D  2 107 ? 122.684 118.624 166.109 1.00 134.66 ? 141 TYR D CA  1 
ATOM   6270  C C   . TYR D  2 107 ? 122.670 118.052 167.518 1.00 143.74 ? 141 TYR D C   1 
ATOM   6271  O O   . TYR D  2 107 ? 123.723 117.699 168.058 1.00 143.73 ? 141 TYR D O   1 
ATOM   6272  C CB  . TYR D  2 107 ? 122.456 117.505 165.082 1.00 137.94 ? 141 TYR D CB  1 
ATOM   6273  C CG  . TYR D  2 107 ? 122.201 118.025 163.687 1.00 135.58 ? 141 TYR D CG  1 
ATOM   6274  C CD1 . TYR D  2 107 ? 121.065 118.769 163.399 1.00 143.36 ? 141 TYR D CD1 1 
ATOM   6275  C CD2 . TYR D  2 107 ? 123.103 117.786 162.660 1.00 132.71 ? 141 TYR D CD2 1 
ATOM   6276  C CE1 . TYR D  2 107 ? 120.831 119.252 162.126 1.00 143.46 ? 141 TYR D CE1 1 
ATOM   6277  C CE2 . TYR D  2 107 ? 122.876 118.264 161.384 1.00 130.07 ? 141 TYR D CE2 1 
ATOM   6278  C CZ  . TYR D  2 107 ? 121.740 118.997 161.123 1.00 134.18 ? 141 TYR D CZ  1 
ATOM   6279  O OH  . TYR D  2 107 ? 121.511 119.476 159.854 1.00 133.42 ? 141 TYR D OH  1 
ATOM   6280  N N   . PRO D  2 108 ? 121.497 117.950 168.137 1.00 147.74 ? 142 PRO D N   1 
ATOM   6281  C CA  . PRO D  2 108 ? 121.440 117.512 169.532 1.00 155.13 ? 142 PRO D CA  1 
ATOM   6282  C C   . PRO D  2 108 ? 121.477 115.998 169.659 1.00 164.76 ? 142 PRO D C   1 
ATOM   6283  O O   . PRO D  2 108 ? 121.277 115.252 168.697 1.00 167.25 ? 142 PRO D O   1 
ATOM   6284  C CB  . PRO D  2 108 ? 120.105 118.078 170.015 1.00 155.71 ? 142 PRO D CB  1 
ATOM   6285  C CG  . PRO D  2 108 ? 119.241 118.005 168.801 1.00 155.80 ? 142 PRO D CG  1 
ATOM   6286  C CD  . PRO D  2 108 ? 120.152 118.241 167.606 1.00 149.74 ? 142 PRO D CD  1 
ATOM   6287  N N   . GLU D  2 109 ? 121.738 115.550 170.885 1.00 171.69 ? 143 GLU D N   1 
ATOM   6288  C CA  . GLU D  2 109 ? 121.779 114.126 171.213 1.00 184.11 ? 143 GLU D CA  1 
ATOM   6289  C C   . GLU D  2 109 ? 120.342 113.639 171.329 1.00 194.61 ? 143 GLU D C   1 
ATOM   6290  O O   . GLU D  2 109 ? 119.703 113.792 172.373 1.00 201.92 ? 143 GLU D O   1 
ATOM   6291  C CB  . GLU D  2 109 ? 122.556 113.887 172.503 1.00 189.61 ? 143 GLU D CB  1 
ATOM   6292  C CG  . GLU D  2 109 ? 123.909 114.598 172.615 1.00 184.72 ? 143 GLU D CG  1 
ATOM   6293  C CD  . GLU D  2 109 ? 124.655 114.748 171.297 1.00 175.73 ? 143 GLU D CD  1 
ATOM   6294  O OE1 . GLU D  2 109 ? 125.290 115.805 171.105 1.00 171.86 ? 143 GLU D OE1 1 
ATOM   6295  O OE2 . GLU D  2 109 ? 124.661 113.801 170.482 1.00 176.79 ? 143 GLU D OE2 1 
ATOM   6296  N N   . LEU D  2 110 ? 119.834 113.052 170.252 1.00 197.15 ? 144 LEU D N   1 
ATOM   6297  C CA  . LEU D  2 110 ? 118.444 112.636 170.212 1.00 205.85 ? 144 LEU D CA  1 
ATOM   6298  C C   . LEU D  2 110 ? 118.187 111.494 171.196 1.00 217.85 ? 144 LEU D C   1 
ATOM   6299  O O   . LEU D  2 110 ? 118.905 110.490 171.201 1.00 222.32 ? 144 LEU D O   1 
ATOM   6300  C CB  . LEU D  2 110 ? 118.065 112.221 168.798 1.00 204.11 ? 144 LEU D CB  1 
ATOM   6301  C CG  . LEU D  2 110 ? 117.977 113.399 167.824 1.00 197.91 ? 144 LEU D CG  1 
ATOM   6302  C CD1 . LEU D  2 110 ? 117.398 112.973 166.488 1.00 203.89 ? 144 LEU D CD1 1 
ATOM   6303  C CD2 . LEU D  2 110 ? 117.173 114.546 168.421 1.00 199.29 ? 144 LEU D CD2 1 
ATOM   6304  N N   . PRO D  2 111 ? 117.166 111.628 172.036 1.00 220.45 ? 145 PRO D N   1 
ATOM   6305  C CA  . PRO D  2 111 ? 116.976 110.713 173.164 1.00 228.97 ? 145 PRO D CA  1 
ATOM   6306  C C   . PRO D  2 111 ? 116.085 109.513 172.855 1.00 236.11 ? 145 PRO D C   1 
ATOM   6307  O O   . PRO D  2 111 ? 115.702 109.252 171.713 1.00 237.04 ? 145 PRO D O   1 
ATOM   6308  C CB  . PRO D  2 111 ? 116.309 111.614 174.212 1.00 225.68 ? 145 PRO D CB  1 
ATOM   6309  C CG  . PRO D  2 111 ? 115.503 112.564 173.393 1.00 219.89 ? 145 PRO D CG  1 
ATOM   6310  C CD  . PRO D  2 111 ? 116.295 112.813 172.134 1.00 214.58 ? 145 PRO D CD  1 
ATOM   6311  N N   . LYS D  2 112 ? 115.777 108.778 173.920 1.00 240.41 ? 146 LYS D N   1 
ATOM   6312  C CA  . LYS D  2 112 ? 114.847 107.659 173.861 1.00 246.57 ? 146 LYS D CA  1 
ATOM   6313  C C   . LYS D  2 112 ? 113.464 108.161 173.455 1.00 249.59 ? 146 LYS D C   1 
ATOM   6314  O O   . LYS D  2 112 ? 112.889 109.005 174.154 1.00 246.97 ? 146 LYS D O   1 
ATOM   6315  C CB  . LYS D  2 112 ? 114.788 107.002 175.244 1.00 248.94 ? 146 LYS D CB  1 
ATOM   6316  C CG  . LYS D  2 112 ? 114.034 105.678 175.423 1.00 254.73 ? 146 LYS D CG  1 
ATOM   6317  C CD  . LYS D  2 112 ? 113.813 104.870 174.167 1.00 260.24 ? 146 LYS D CD  1 
ATOM   6318  C CE  . LYS D  2 112 ? 113.165 103.541 174.525 1.00 266.91 ? 146 LYS D CE  1 
ATOM   6319  N NZ  . LYS D  2 112 ? 111.693 103.668 174.705 1.00 270.75 ? 146 LYS D NZ  1 
ATOM   6320  N N   . PRO D  2 113 ? 112.893 107.670 172.352 1.00 255.17 ? 147 PRO D N   1 
ATOM   6321  C CA  . PRO D  2 113 ? 111.528 108.079 172.004 1.00 259.11 ? 147 PRO D CA  1 
ATOM   6322  C C   . PRO D  2 113 ? 110.471 107.166 172.609 1.00 264.12 ? 147 PRO D C   1 
ATOM   6323  O O   . PRO D  2 113 ? 110.797 106.141 173.215 1.00 264.54 ? 147 PRO D O   1 
ATOM   6324  C CB  . PRO D  2 113 ? 111.527 108.015 170.472 1.00 260.09 ? 147 PRO D CB  1 
ATOM   6325  C CG  . PRO D  2 113 ? 112.591 107.010 170.118 1.00 257.82 ? 147 PRO D CG  1 
ATOM   6326  C CD  . PRO D  2 113 ? 113.483 106.795 171.323 1.00 254.43 ? 147 PRO D CD  1 
ATOM   6327  N N   . SER D  2 114 ? 109.200 107.528 172.443 1.00 269.06 ? 148 SER D N   1 
ATOM   6328  C CA  . SER D  2 114 ? 108.092 106.747 172.974 1.00 279.56 ? 148 SER D CA  1 
ATOM   6329  C C   . SER D  2 114 ? 106.894 106.880 172.044 1.00 287.10 ? 148 SER D C   1 
ATOM   6330  O O   . SER D  2 114 ? 106.786 107.835 171.273 1.00 287.20 ? 148 SER D O   1 
ATOM   6331  C CB  . SER D  2 114 ? 107.725 107.183 174.399 1.00 283.67 ? 148 SER D CB  1 
ATOM   6332  O OG  . SER D  2 114 ? 107.425 108.565 174.449 1.00 285.15 ? 148 SER D OG  1 
ATOM   6333  N N   . ILE D  2 115 ? 105.985 105.911 172.135 1.00 291.25 ? 149 ILE D N   1 
ATOM   6334  C CA  . ILE D  2 115 ? 104.893 105.749 171.182 1.00 296.08 ? 149 ILE D CA  1 
ATOM   6335  C C   . ILE D  2 115 ? 103.571 105.767 171.937 1.00 300.57 ? 149 ILE D C   1 
ATOM   6336  O O   . ILE D  2 115 ? 103.522 105.448 173.130 1.00 300.08 ? 149 ILE D O   1 
ATOM   6337  C CB  . ILE D  2 115 ? 105.039 104.444 170.367 1.00 293.86 ? 149 ILE D CB  1 
ATOM   6338  C CG1 . ILE D  2 115 ? 106.507 104.179 170.021 1.00 289.49 ? 149 ILE D CG1 1 
ATOM   6339  C CG2 . ILE D  2 115 ? 104.210 104.504 169.093 1.00 299.23 ? 149 ILE D CG2 1 
ATOM   6340  C CD1 . ILE D  2 115 ? 107.214 103.246 170.982 1.00 285.66 ? 149 ILE D CD1 1 
ATOM   6341  N N   . SER D  2 116 ? 102.499 106.141 171.238 1.00 304.73 ? 150 SER D N   1 
ATOM   6342  C CA  . SER D  2 116 ? 101.169 106.223 171.822 1.00 308.75 ? 150 SER D CA  1 
ATOM   6343  C C   . SER D  2 116 ? 100.117 105.815 170.799 1.00 313.17 ? 150 SER D C   1 
ATOM   6344  O O   . SER D  2 116 ? 100.323 105.927 169.588 1.00 312.79 ? 150 SER D O   1 
ATOM   6345  C CB  . SER D  2 116 ? 100.869 107.638 172.335 1.00 308.11 ? 150 SER D CB  1 
ATOM   6346  O OG  . SER D  2 116 ? 101.324 108.618 171.419 1.00 304.07 ? 150 SER D OG  1 
ATOM   6347  N N   . SER D  2 117 ? 98.986  105.334 171.309 1.00 316.67 ? 151 SER D N   1 
ATOM   6348  C CA  . SER D  2 117 ? 97.834  104.945 170.508 1.00 322.99 ? 151 SER D CA  1 
ATOM   6349  C C   . SER D  2 117 ? 96.573  105.507 171.149 1.00 329.59 ? 151 SER D C   1 
ATOM   6350  O O   . SER D  2 117 ? 96.457  105.523 172.378 1.00 329.91 ? 151 SER D O   1 
ATOM   6351  C CB  . SER D  2 117 ? 97.733  103.423 170.404 1.00 323.47 ? 151 SER D CB  1 
ATOM   6352  O OG  . SER D  2 117 ? 96.488  103.033 169.862 1.00 328.59 ? 151 SER D OG  1 
ATOM   6353  N N   . ASN D  2 118 ? 95.622  105.969 170.332 1.00 333.27 ? 152 ASN D N   1 
ATOM   6354  C CA  . ASN D  2 118 ? 94.441  106.543 170.966 1.00 335.59 ? 152 ASN D CA  1 
ATOM   6355  C C   . ASN D  2 118 ? 93.360  105.497 171.205 1.00 338.07 ? 152 ASN D C   1 
ATOM   6356  O O   . ASN D  2 118 ? 92.319  105.825 171.783 1.00 338.86 ? 152 ASN D O   1 
ATOM   6357  C CB  . ASN D  2 118 ? 93.856  107.706 170.150 1.00 336.51 ? 152 ASN D CB  1 
ATOM   6358  C CG  . ASN D  2 118 ? 92.823  107.271 169.115 1.00 338.90 ? 152 ASN D CG  1 
ATOM   6359  O OD1 . ASN D  2 118 ? 91.627  107.408 169.374 1.00 339.24 ? 152 ASN D OD1 1 
ATOM   6360  N ND2 . ASN D  2 118 ? 93.243  106.784 167.956 1.00 339.73 ? 152 ASN D ND2 1 
ATOM   6361  N N   . ASN D  2 119 ? 93.586  104.256 170.776 1.00 339.17 ? 153 ASN D N   1 
ATOM   6362  C CA  . ASN D  2 119 ? 92.691  103.143 171.060 1.00 340.89 ? 153 ASN D CA  1 
ATOM   6363  C C   . ASN D  2 119 ? 93.519  101.996 171.615 1.00 341.38 ? 153 ASN D C   1 
ATOM   6364  O O   . ASN D  2 119 ? 94.340  101.417 170.897 1.00 339.96 ? 153 ASN D O   1 
ATOM   6365  C CB  . ASN D  2 119 ? 91.933  102.697 169.803 1.00 341.80 ? 153 ASN D CB  1 
ATOM   6366  C CG  . ASN D  2 119 ? 90.946  101.577 170.082 1.00 343.64 ? 153 ASN D CG  1 
ATOM   6367  O OD1 . ASN D  2 119 ? 90.652  101.262 171.235 1.00 344.07 ? 153 ASN D OD1 1 
ATOM   6368  N ND2 . ASN D  2 119 ? 90.428  100.970 169.022 1.00 345.50 ? 153 ASN D ND2 1 
ATOM   6369  N N   . SER D  2 120 ? 93.302  101.673 172.890 1.00 343.44 ? 154 SER D N   1 
ATOM   6370  C CA  . SER D  2 120 ? 94.075  100.642 173.569 1.00 342.97 ? 154 SER D CA  1 
ATOM   6371  C C   . SER D  2 120 ? 93.679  99.226  173.178 1.00 343.04 ? 154 SER D C   1 
ATOM   6372  O O   . SER D  2 120 ? 94.535  98.334  173.199 1.00 339.52 ? 154 SER D O   1 
ATOM   6373  C CB  . SER D  2 120 ? 93.942  100.795 175.090 1.00 343.07 ? 154 SER D CB  1 
ATOM   6374  O OG  . SER D  2 120 ? 92.586  100.955 175.468 1.00 344.54 ? 154 SER D OG  1 
ATOM   6375  N N   . ASN D  2 121 ? 92.417  98.996  172.821 1.00 345.14 ? 155 ASN D N   1 
ATOM   6376  C CA  . ASN D  2 121 ? 91.915  97.667  172.470 1.00 343.93 ? 155 ASN D CA  1 
ATOM   6377  C C   . ASN D  2 121 ? 91.317  97.721  171.072 1.00 345.45 ? 155 ASN D C   1 
ATOM   6378  O O   . ASN D  2 121 ? 90.113  97.962  170.907 1.00 346.34 ? 155 ASN D O   1 
ATOM   6379  C CB  . ASN D  2 121 ? 90.889  97.177  173.493 1.00 342.17 ? 155 ASN D CB  1 
ATOM   6380  C CG  . ASN D  2 121 ? 91.270  95.845  174.107 1.00 337.65 ? 155 ASN D CG  1 
ATOM   6381  O OD1 . ASN D  2 121 ? 91.599  94.894  173.399 1.00 336.63 ? 155 ASN D OD1 1 
ATOM   6382  N ND2 . ASN D  2 121 ? 91.229  95.771  175.433 1.00 336.24 ? 155 ASN D ND2 1 
ATOM   6383  N N   . PRO D  2 122 ? 92.136  97.523  170.038 1.00 345.56 ? 156 PRO D N   1 
ATOM   6384  C CA  . PRO D  2 122 ? 91.605  97.506  168.671 1.00 347.59 ? 156 PRO D CA  1 
ATOM   6385  C C   . PRO D  2 122 ? 90.533  96.440  168.498 1.00 348.53 ? 156 PRO D C   1 
ATOM   6386  O O   . PRO D  2 122 ? 90.628  95.341  169.047 1.00 345.89 ? 156 PRO D O   1 
ATOM   6387  C CB  . PRO D  2 122 ? 92.838  97.193  167.818 1.00 345.79 ? 156 PRO D CB  1 
ATOM   6388  C CG  . PRO D  2 122 ? 93.991  97.686  168.611 1.00 341.41 ? 156 PRO D CG  1 
ATOM   6389  C CD  . PRO D  2 122 ? 93.598  97.707  170.066 1.00 342.06 ? 156 PRO D CD  1 
ATOM   6390  N N   . VAL D  2 123 ? 89.507  96.779  167.726 1.00 350.74 ? 157 VAL D N   1 
ATOM   6391  C CA  . VAL D  2 123 ? 88.453  95.826  167.399 1.00 350.20 ? 157 VAL D CA  1 
ATOM   6392  C C   . VAL D  2 123 ? 88.999  94.833  166.383 1.00 350.79 ? 157 VAL D C   1 
ATOM   6393  O O   . VAL D  2 123 ? 89.604  95.225  165.377 1.00 353.19 ? 157 VAL D O   1 
ATOM   6394  C CB  . VAL D  2 123 ? 87.207  96.551  166.869 1.00 350.96 ? 157 VAL D CB  1 
ATOM   6395  C CG1 . VAL D  2 123 ? 86.100  95.554  166.575 1.00 351.67 ? 157 VAL D CG1 1 
ATOM   6396  C CG2 . VAL D  2 123 ? 86.739  97.600  167.867 1.00 348.65 ? 157 VAL D CG2 1 
ATOM   6397  N N   . GLU D  2 124 ? 88.795  93.540  166.650 1.00 347.02 ? 158 GLU D N   1 
ATOM   6398  C CA  . GLU D  2 124 ? 89.472  92.501  165.879 1.00 344.98 ? 158 GLU D CA  1 
ATOM   6399  C C   . GLU D  2 124 ? 89.065  92.521  164.410 1.00 351.81 ? 158 GLU D C   1 
ATOM   6400  O O   . GLU D  2 124 ? 89.917  92.382  163.524 1.00 352.70 ? 158 GLU D O   1 
ATOM   6401  C CB  . GLU D  2 124 ? 89.191  91.131  166.496 1.00 335.44 ? 158 GLU D CB  1 
ATOM   6402  C CG  . GLU D  2 124 ? 89.537  91.041  167.972 1.00 328.57 ? 158 GLU D CG  1 
ATOM   6403  C CD  . GLU D  2 124 ? 89.189  89.695  168.574 1.00 319.34 ? 158 GLU D CD  1 
ATOM   6404  O OE1 . GLU D  2 124 ? 89.093  88.709  167.813 1.00 317.61 ? 158 GLU D OE1 1 
ATOM   6405  O OE2 . GLU D  2 124 ? 89.007  89.625  169.807 1.00 315.89 ? 158 GLU D OE2 1 
ATOM   6406  N N   . ASP D  2 125 ? 87.770  92.683  164.128 1.00 354.09 ? 159 ASP D N   1 
ATOM   6407  C CA  . ASP D  2 125 ? 87.314  92.617  162.741 1.00 356.50 ? 159 ASP D CA  1 
ATOM   6408  C C   . ASP D  2 125 ? 87.847  93.785  161.916 1.00 358.94 ? 159 ASP D C   1 
ATOM   6409  O O   . ASP D  2 125 ? 88.275  93.595  160.771 1.00 360.41 ? 159 ASP D O   1 
ATOM   6410  C CB  . ASP D  2 125 ? 85.783  92.541  162.689 1.00 357.03 ? 159 ASP D CB  1 
ATOM   6411  C CG  . ASP D  2 125 ? 85.104  93.873  162.974 1.00 357.65 ? 159 ASP D CG  1 
ATOM   6412  O OD1 . ASP D  2 125 ? 85.742  94.773  163.558 1.00 357.58 ? 159 ASP D OD1 1 
ATOM   6413  O OD2 . ASP D  2 125 ? 83.919  94.019  162.609 1.00 357.29 ? 159 ASP D OD2 1 
ATOM   6414  N N   . LYS D  2 126 ? 87.842  94.991  162.480 1.00 359.14 ? 160 LYS D N   1 
ATOM   6415  C CA  . LYS D  2 126 ? 88.329  96.179  161.791 1.00 359.19 ? 160 LYS D CA  1 
ATOM   6416  C C   . LYS D  2 126 ? 88.443  97.316  162.795 1.00 358.08 ? 160 LYS D C   1 
ATOM   6417  O O   . LYS D  2 126 ? 87.655  97.403  163.741 1.00 357.06 ? 160 LYS D O   1 
ATOM   6418  C CB  . LYS D  2 126 ? 87.406  96.577  160.627 1.00 358.96 ? 160 LYS D CB  1 
ATOM   6419  C CG  . LYS D  2 126 ? 85.943  96.805  161.004 1.00 356.19 ? 160 LYS D CG  1 
ATOM   6420  C CD  . LYS D  2 126 ? 85.656  98.263  161.347 1.00 351.37 ? 160 LYS D CD  1 
ATOM   6421  C CE  . LYS D  2 126 ? 84.340  98.407  162.094 1.00 345.99 ? 160 LYS D CE  1 
ATOM   6422  N NZ  . LYS D  2 126 ? 84.289  99.668  162.885 1.00 336.59 ? 160 LYS D NZ  1 
ATOM   6423  N N   . ASP D  2 127 ? 89.430  98.180  162.578 1.00 358.95 ? 161 ASP D N   1 
ATOM   6424  C CA  . ASP D  2 127 ? 89.611  99.372  163.396 1.00 358.05 ? 161 ASP D CA  1 
ATOM   6425  C C   . ASP D  2 127 ? 90.519  100.327 162.632 1.00 357.40 ? 161 ASP D C   1 
ATOM   6426  O O   . ASP D  2 127 ? 91.193  99.938  161.675 1.00 358.16 ? 161 ASP D O   1 
ATOM   6427  C CB  . ASP D  2 127 ? 90.194  99.035  164.770 1.00 356.51 ? 161 ASP D CB  1 
ATOM   6428  C CG  . ASP D  2 127 ? 89.683  99.953  165.859 1.00 354.38 ? 161 ASP D CG  1 
ATOM   6429  O OD1 . ASP D  2 127 ? 88.678  100.654 165.621 1.00 354.31 ? 161 ASP D OD1 1 
ATOM   6430  O OD2 . ASP D  2 127 ? 90.286  99.974  166.952 1.00 352.20 ? 161 ASP D OD2 1 
ATOM   6431  N N   . ALA D  2 128 ? 90.535  101.582 163.072 1.00 355.71 ? 162 ALA D N   1 
ATOM   6432  C CA  . ALA D  2 128 ? 91.313  102.637 162.433 1.00 353.00 ? 162 ALA D CA  1 
ATOM   6433  C C   . ALA D  2 128 ? 92.349  103.212 163.391 1.00 350.53 ? 162 ALA D C   1 
ATOM   6434  O O   . ALA D  2 128 ? 92.588  104.421 163.426 1.00 348.93 ? 162 ALA D O   1 
ATOM   6435  C CB  . ALA D  2 128 ? 90.400  103.738 161.899 1.00 350.15 ? 162 ALA D CB  1 
ATOM   6436  N N   . VAL D  2 129 ? 92.995  102.338 164.168 1.00 350.60 ? 163 VAL D N   1 
ATOM   6437  C CA  . VAL D  2 129 ? 93.859  102.792 165.249 1.00 345.62 ? 163 VAL D CA  1 
ATOM   6438  C C   . VAL D  2 129 ? 95.073  103.538 164.692 1.00 342.77 ? 163 VAL D C   1 
ATOM   6439  O O   . VAL D  2 129 ? 95.593  103.221 163.615 1.00 343.29 ? 163 VAL D O   1 
ATOM   6440  C CB  . VAL D  2 129 ? 94.286  101.597 166.121 1.00 343.42 ? 163 VAL D CB  1 
ATOM   6441  C CG1 . VAL D  2 129 ? 95.144  100.624 165.327 1.00 342.69 ? 163 VAL D CG1 1 
ATOM   6442  C CG2 . VAL D  2 129 ? 95.003  102.065 167.367 1.00 338.40 ? 163 VAL D CG2 1 
ATOM   6443  N N   . ALA D  2 130 ? 95.517  104.556 165.432 1.00 338.85 ? 164 ALA D N   1 
ATOM   6444  C CA  . ALA D  2 130 ? 96.623  105.410 165.024 1.00 333.31 ? 164 ALA D CA  1 
ATOM   6445  C C   . ALA D  2 130 ? 97.781  105.276 166.002 1.00 325.47 ? 164 ALA D C   1 
ATOM   6446  O O   . ALA D  2 130 ? 97.573  105.125 167.210 1.00 325.39 ? 164 ALA D O   1 
ATOM   6447  C CB  . ALA D  2 130 ? 96.186  106.878 164.932 1.00 332.57 ? 164 ALA D CB  1 
ATOM   6448  N N   . PHE D  2 131 ? 99.000  105.336 165.470 1.00 321.36 ? 165 PHE D N   1 
ATOM   6449  C CA  . PHE D  2 131 ? 100.226 105.251 166.249 1.00 315.64 ? 165 PHE D CA  1 
ATOM   6450  C C   . PHE D  2 131 ? 101.059 106.506 166.020 1.00 311.66 ? 165 PHE D C   1 
ATOM   6451  O O   . PHE D  2 131 ? 101.183 106.986 164.890 1.00 311.76 ? 165 PHE D O   1 
ATOM   6452  C CB  . PHE D  2 131 ? 101.036 104.007 165.862 1.00 312.95 ? 165 PHE D CB  1 
ATOM   6453  C CG  . PHE D  2 131 ? 100.792 102.820 166.749 1.00 311.12 ? 165 PHE D CG  1 
ATOM   6454  C CD1 . PHE D  2 131 ? 100.704 101.547 166.211 1.00 307.56 ? 165 PHE D CD1 1 
ATOM   6455  C CD2 . PHE D  2 131 ? 100.667 102.972 168.119 1.00 312.47 ? 165 PHE D CD2 1 
ATOM   6456  C CE1 . PHE D  2 131 ? 100.481 100.450 167.021 1.00 304.06 ? 165 PHE D CE1 1 
ATOM   6457  C CE2 . PHE D  2 131 ? 100.449 101.877 168.934 1.00 309.81 ? 165 PHE D CE2 1 
ATOM   6458  C CZ  . PHE D  2 131 ? 100.355 100.615 168.384 1.00 305.81 ? 165 PHE D CZ  1 
ATOM   6459  N N   . THR D  2 132 ? 101.630 107.038 167.100 1.00 308.77 ? 166 THR D N   1 
ATOM   6460  C CA  . THR D  2 132 ? 102.368 108.292 167.024 1.00 304.65 ? 166 THR D CA  1 
ATOM   6461  C C   . THR D  2 132 ? 103.495 108.286 168.046 1.00 301.69 ? 166 THR D C   1 
ATOM   6462  O O   . THR D  2 132 ? 103.321 107.801 169.167 1.00 301.94 ? 166 THR D O   1 
ATOM   6463  C CB  . THR D  2 132 ? 101.447 109.495 167.273 1.00 303.68 ? 166 THR D CB  1 
ATOM   6464  O OG1 . THR D  2 132 ? 100.336 109.445 166.370 1.00 307.13 ? 166 THR D OG1 1 
ATOM   6465  C CG2 . THR D  2 132 ? 102.197 110.804 167.065 1.00 299.15 ? 166 THR D CG2 1 
ATOM   6466  N N   . CYS D  2 133 ? 104.648 108.826 167.651 1.00 299.25 ? 167 CYS D N   1 
ATOM   6467  C CA  . CYS D  2 133 ? 105.763 109.043 168.568 1.00 295.34 ? 167 CYS D CA  1 
ATOM   6468  C C   . CYS D  2 133 ? 105.661 110.466 169.111 1.00 290.20 ? 167 CYS D C   1 
ATOM   6469  O O   . CYS D  2 133 ? 105.842 111.436 168.370 1.00 288.06 ? 167 CYS D O   1 
ATOM   6470  C CB  . CYS D  2 133 ? 107.100 108.802 167.870 1.00 294.35 ? 167 CYS D CB  1 
ATOM   6471  S SG  . CYS D  2 133 ? 107.079 107.453 166.659 1.00 301.01 ? 167 CYS D SG  1 
ATOM   6472  N N   . GLU D  2 134 ? 105.356 110.586 170.403 1.00 290.37 ? 168 GLU D N   1 
ATOM   6473  C CA  . GLU D  2 134 ? 105.102 111.853 171.088 1.00 288.16 ? 168 GLU D CA  1 
ATOM   6474  C C   . GLU D  2 134 ? 106.272 112.841 171.158 1.00 282.19 ? 168 GLU D C   1 
ATOM   6475  O O   . GLU D  2 134 ? 106.051 114.039 170.939 1.00 280.26 ? 168 GLU D O   1 
ATOM   6476  C CB  . GLU D  2 134 ? 104.587 111.578 172.505 1.00 291.88 ? 168 GLU D CB  1 
ATOM   6477  C CG  . GLU D  2 134 ? 105.196 110.368 173.190 1.00 292.15 ? 168 GLU D CG  1 
ATOM   6478  C CD  . GLU D  2 134 ? 104.434 109.085 172.905 1.00 296.82 ? 168 GLU D CD  1 
ATOM   6479  O OE1 . GLU D  2 134 ? 103.986 108.899 171.754 1.00 297.82 ? 168 GLU D OE1 1 
ATOM   6480  O OE2 . GLU D  2 134 ? 104.287 108.262 173.832 1.00 299.58 ? 168 GLU D OE2 1 
ATOM   6481  N N   . PRO D  2 135 ? 107.529 112.419 171.455 1.00 279.30 ? 169 PRO D N   1 
ATOM   6482  C CA  . PRO D  2 135 ? 108.550 113.420 171.810 1.00 275.13 ? 169 PRO D CA  1 
ATOM   6483  C C   . PRO D  2 135 ? 109.020 114.253 170.626 1.00 272.26 ? 169 PRO D C   1 
ATOM   6484  O O   . PRO D  2 135 ? 110.019 113.927 169.977 1.00 269.50 ? 169 PRO D O   1 
ATOM   6485  C CB  . PRO D  2 135 ? 109.691 112.572 172.383 1.00 269.79 ? 169 PRO D CB  1 
ATOM   6486  C CG  . PRO D  2 135 ? 109.555 111.260 171.729 1.00 269.77 ? 169 PRO D CG  1 
ATOM   6487  C CD  . PRO D  2 135 ? 108.110 111.065 171.366 1.00 277.28 ? 169 PRO D CD  1 
ATOM   6488  N N   . GLU D  2 136 ? 108.295 115.334 170.341 1.00 272.09 ? 170 GLU D N   1 
ATOM   6489  C CA  . GLU D  2 136 ? 108.573 116.136 169.157 1.00 269.04 ? 170 GLU D CA  1 
ATOM   6490  C C   . GLU D  2 136 ? 109.855 116.946 169.312 1.00 265.19 ? 170 GLU D C   1 
ATOM   6491  O O   . GLU D  2 136 ? 110.008 117.733 170.250 1.00 264.66 ? 170 GLU D O   1 
ATOM   6492  C CB  . GLU D  2 136 ? 107.398 117.071 168.867 1.00 268.83 ? 170 GLU D CB  1 
ATOM   6493  C CG  . GLU D  2 136 ? 107.474 117.830 167.538 1.00 266.08 ? 170 GLU D CG  1 
ATOM   6494  C CD  . GLU D  2 136 ? 107.686 116.932 166.326 1.00 268.77 ? 170 GLU D CD  1 
ATOM   6495  O OE1 . GLU D  2 136 ? 108.796 116.383 166.152 1.00 267.88 ? 170 GLU D OE1 1 
ATOM   6496  O OE2 . GLU D  2 136 ? 106.729 116.771 165.540 1.00 273.19 ? 170 GLU D OE2 1 
ATOM   6497  N N   . THR D  2 137 ? 110.781 116.745 168.373 1.00 261.06 ? 171 THR D N   1 
ATOM   6498  C CA  . THR D  2 137 ? 111.979 117.563 168.246 1.00 254.95 ? 171 THR D CA  1 
ATOM   6499  C C   . THR D  2 137 ? 112.165 117.915 166.776 1.00 248.56 ? 171 THR D C   1 
ATOM   6500  O O   . THR D  2 137 ? 111.553 117.304 165.896 1.00 247.36 ? 171 THR D O   1 
ATOM   6501  C CB  . THR D  2 137 ? 113.242 116.864 168.786 1.00 254.82 ? 171 THR D CB  1 
ATOM   6502  O OG1 . THR D  2 137 ? 113.851 116.093 167.747 1.00 252.44 ? 171 THR D OG1 1 
ATOM   6503  C CG2 . THR D  2 137 ? 112.914 115.951 169.961 1.00 259.10 ? 171 THR D CG2 1 
ATOM   6504  N N   . GLN D  2 138 ? 113.016 118.904 166.517 1.00 244.11 ? 172 GLN D N   1 
ATOM   6505  C CA  . GLN D  2 138 ? 113.109 119.489 165.189 1.00 236.43 ? 172 GLN D CA  1 
ATOM   6506  C C   . GLN D  2 138 ? 114.066 118.707 164.290 1.00 230.28 ? 172 GLN D C   1 
ATOM   6507  O O   . GLN D  2 138 ? 114.924 117.953 164.753 1.00 227.81 ? 172 GLN D O   1 
ATOM   6508  C CB  . GLN D  2 138 ? 113.558 120.948 165.277 1.00 234.50 ? 172 GLN D CB  1 
ATOM   6509  C CG  . GLN D  2 138 ? 112.424 121.966 165.381 1.00 236.96 ? 172 GLN D CG  1 
ATOM   6510  C CD  . GLN D  2 138 ? 111.217 121.608 164.531 1.00 241.88 ? 172 GLN D CD  1 
ATOM   6511  O OE1 . GLN D  2 138 ? 111.140 121.978 163.359 1.00 243.32 ? 172 GLN D OE1 1 
ATOM   6512  N NE2 . GLN D  2 138 ? 110.254 120.912 165.127 1.00 244.68 ? 172 GLN D NE2 1 
ATOM   6513  N N   . ASP D  2 139 ? 113.876 118.893 162.979 1.00 227.32 ? 173 ASP D N   1 
ATOM   6514  C CA  . ASP D  2 139 ? 114.718 118.409 161.883 1.00 221.72 ? 173 ASP D CA  1 
ATOM   6515  C C   . ASP D  2 139 ? 115.182 116.960 162.019 1.00 219.40 ? 173 ASP D C   1 
ATOM   6516  O O   . ASP D  2 139 ? 116.330 116.639 161.695 1.00 215.72 ? 173 ASP D O   1 
ATOM   6517  C CB  . ASP D  2 139 ? 115.916 119.359 161.675 1.00 216.64 ? 173 ASP D CB  1 
ATOM   6518  C CG  . ASP D  2 139 ? 116.891 119.406 162.856 1.00 211.42 ? 173 ASP D CG  1 
ATOM   6519  O OD1 . ASP D  2 139 ? 117.480 120.486 163.070 1.00 205.32 ? 173 ASP D OD1 1 
ATOM   6520  O OD2 . ASP D  2 139 ? 117.131 118.386 163.531 1.00 211.55 ? 173 ASP D OD2 1 
ATOM   6521  N N   . THR D  2 140 ? 114.293 116.071 162.453 1.00 220.80 ? 174 THR D N   1 
ATOM   6522  C CA  . THR D  2 140 ? 114.592 114.649 162.525 1.00 224.64 ? 174 THR D CA  1 
ATOM   6523  C C   . THR D  2 140 ? 114.023 113.927 161.312 1.00 227.02 ? 174 THR D C   1 
ATOM   6524  O O   . THR D  2 140 ? 113.393 114.533 160.440 1.00 227.21 ? 174 THR D O   1 
ATOM   6525  C CB  . THR D  2 140 ? 114.014 114.009 163.789 1.00 231.19 ? 174 THR D CB  1 
ATOM   6526  O OG1 . THR D  2 140 ? 112.729 113.452 163.492 1.00 239.21 ? 174 THR D OG1 1 
ATOM   6527  C CG2 . THR D  2 140 ? 113.848 115.040 164.871 1.00 233.38 ? 174 THR D CG2 1 
ATOM   6528  N N   . THR D  2 141 ? 114.257 112.619 161.268 1.00 228.24 ? 175 THR D N   1 
ATOM   6529  C CA  . THR D  2 141 ? 113.642 111.727 160.296 1.00 233.63 ? 175 THR D CA  1 
ATOM   6530  C C   . THR D  2 141 ? 112.968 110.586 161.046 1.00 238.35 ? 175 THR D C   1 
ATOM   6531  O O   . THR D  2 141 ? 113.544 110.038 161.992 1.00 236.91 ? 175 THR D O   1 
ATOM   6532  C CB  . THR D  2 141 ? 114.678 111.178 159.312 1.00 231.89 ? 175 THR D CB  1 
ATOM   6533  O OG1 . THR D  2 141 ? 115.469 112.257 158.798 1.00 231.60 ? 175 THR D OG1 1 
ATOM   6534  C CG2 . THR D  2 141 ? 113.992 110.465 158.157 1.00 238.88 ? 175 THR D CG2 1 
ATOM   6535  N N   . TYR D  2 142 ? 111.757 110.232 160.628 1.00 245.40 ? 176 TYR D N   1 
ATOM   6536  C CA  . TYR D  2 142 ? 110.980 109.195 161.293 1.00 251.52 ? 176 TYR D CA  1 
ATOM   6537  C C   . TYR D  2 142 ? 110.808 107.999 160.369 1.00 257.15 ? 176 TYR D C   1 
ATOM   6538  O O   . TYR D  2 142 ? 110.646 108.161 159.154 1.00 261.66 ? 176 TYR D O   1 
ATOM   6539  C CB  . TYR D  2 142 ? 109.605 109.711 161.724 1.00 258.63 ? 176 TYR D CB  1 
ATOM   6540  C CG  . TYR D  2 142 ? 109.634 110.952 162.583 1.00 259.85 ? 176 TYR D CG  1 
ATOM   6541  C CD1 . TYR D  2 142 ? 109.447 110.869 163.954 1.00 261.62 ? 176 TYR D CD1 1 
ATOM   6542  C CD2 . TYR D  2 142 ? 109.795 112.211 162.019 1.00 257.02 ? 176 TYR D CD2 1 
ATOM   6543  C CE1 . TYR D  2 142 ? 109.462 111.994 164.743 1.00 264.27 ? 176 TYR D CE1 1 
ATOM   6544  C CE2 . TYR D  2 142 ? 109.802 113.348 162.802 1.00 257.04 ? 176 TYR D CE2 1 
ATOM   6545  C CZ  . TYR D  2 142 ? 109.636 113.234 164.165 1.00 262.90 ? 176 TYR D CZ  1 
ATOM   6546  O OH  . TYR D  2 142 ? 109.644 114.362 164.953 1.00 264.31 ? 176 TYR D OH  1 
ATOM   6547  N N   . LEU D  2 143 ? 110.841 106.804 160.949 1.00 257.78 ? 177 LEU D N   1 
ATOM   6548  C CA  . LEU D  2 143 ? 110.575 105.564 160.234 1.00 264.85 ? 177 LEU D CA  1 
ATOM   6549  C C   . LEU D  2 143 ? 110.032 104.536 161.217 1.00 269.91 ? 177 LEU D C   1 
ATOM   6550  O O   . LEU D  2 143 ? 110.360 104.574 162.408 1.00 268.84 ? 177 LEU D O   1 
ATOM   6551  C CB  . LEU D  2 143 ? 111.836 105.066 159.504 1.00 264.87 ? 177 LEU D CB  1 
ATOM   6552  C CG  . LEU D  2 143 ? 113.187 104.714 160.150 1.00 263.21 ? 177 LEU D CG  1 
ATOM   6553  C CD1 . LEU D  2 143 ? 113.121 103.610 161.193 1.00 265.76 ? 177 LEU D CD1 1 
ATOM   6554  C CD2 . LEU D  2 143 ? 114.202 104.358 159.067 1.00 263.80 ? 177 LEU D CD2 1 
ATOM   6555  N N   . TRP D  2 144 ? 109.191 103.635 160.720 1.00 276.69 ? 178 TRP D N   1 
ATOM   6556  C CA  . TRP D  2 144 ? 108.477 102.676 161.550 1.00 281.88 ? 178 TRP D CA  1 
ATOM   6557  C C   . TRP D  2 144 ? 109.027 101.275 161.325 1.00 284.17 ? 178 TRP D C   1 
ATOM   6558  O O   . TRP D  2 144 ? 109.498 100.954 160.229 1.00 285.58 ? 178 TRP D O   1 
ATOM   6559  C CB  . TRP D  2 144 ? 106.981 102.713 161.242 1.00 288.14 ? 178 TRP D CB  1 
ATOM   6560  C CG  . TRP D  2 144 ? 106.340 104.015 161.590 1.00 290.51 ? 178 TRP D CG  1 
ATOM   6561  C CD1 . TRP D  2 144 ? 106.125 105.073 160.757 1.00 292.92 ? 178 TRP D CD1 1 
ATOM   6562  C CD2 . TRP D  2 144 ? 105.794 104.385 162.860 1.00 291.81 ? 178 TRP D CD2 1 
ATOM   6563  N NE1 . TRP D  2 144 ? 105.497 106.088 161.436 1.00 296.45 ? 178 TRP D NE1 1 
ATOM   6564  C CE2 . TRP D  2 144 ? 105.281 105.689 162.729 1.00 296.63 ? 178 TRP D CE2 1 
ATOM   6565  C CE3 . TRP D  2 144 ? 105.694 103.743 164.097 1.00 291.49 ? 178 TRP D CE3 1 
ATOM   6566  C CZ2 . TRP D  2 144 ? 104.677 106.361 163.786 1.00 299.97 ? 178 TRP D CZ2 1 
ATOM   6567  C CZ3 . TRP D  2 144 ? 105.095 104.414 165.147 1.00 296.17 ? 178 TRP D CZ3 1 
ATOM   6568  C CH2 . TRP D  2 144 ? 104.595 105.710 164.984 1.00 299.99 ? 178 TRP D CH2 1 
ATOM   6569  N N   . TRP D  2 145 ? 108.974 100.450 162.367 1.00 285.26 ? 179 TRP D N   1 
ATOM   6570  C CA  . TRP D  2 145 ? 109.434 99.071  162.309 1.00 289.22 ? 179 TRP D CA  1 
ATOM   6571  C C   . TRP D  2 145 ? 108.349 98.164  162.867 1.00 294.96 ? 179 TRP D C   1 
ATOM   6572  O O   . TRP D  2 145 ? 107.942 98.313  164.024 1.00 295.95 ? 179 TRP D O   1 
ATOM   6573  C CB  . TRP D  2 145 ? 110.737 98.906  163.095 1.00 284.56 ? 179 TRP D CB  1 
ATOM   6574  C CG  . TRP D  2 145 ? 111.962 99.140  162.262 1.00 283.70 ? 179 TRP D CG  1 
ATOM   6575  C CD1 . TRP D  2 145 ? 112.467 100.346 161.876 1.00 279.15 ? 179 TRP D CD1 1 
ATOM   6576  C CD2 . TRP D  2 145 ? 112.866 98.150  161.758 1.00 286.38 ? 179 TRP D CD2 1 
ATOM   6577  N NE1 . TRP D  2 145 ? 113.609 100.169 161.136 1.00 279.40 ? 179 TRP D NE1 1 
ATOM   6578  C CE2 . TRP D  2 145 ? 113.878 98.829  161.052 1.00 284.61 ? 179 TRP D CE2 1 
ATOM   6579  C CE3 . TRP D  2 145 ? 112.912 96.757  161.827 1.00 290.84 ? 179 TRP D CE3 1 
ATOM   6580  C CZ2 . TRP D  2 145 ? 114.922 98.161  160.418 1.00 287.73 ? 179 TRP D CZ2 1 
ATOM   6581  C CZ3 . TRP D  2 145 ? 113.949 96.095  161.194 1.00 292.06 ? 179 TRP D CZ3 1 
ATOM   6582  C CH2 . TRP D  2 145 ? 114.939 96.797  160.499 1.00 291.34 ? 179 TRP D CH2 1 
ATOM   6583  N N   . ILE D  2 146 ? 107.888 97.226  162.046 1.00 299.90 ? 180 ILE D N   1 
ATOM   6584  C CA  . ILE D  2 146 ? 106.890 96.243  162.441 1.00 302.89 ? 180 ILE D CA  1 
ATOM   6585  C C   . ILE D  2 146 ? 107.526 94.869  162.322 1.00 305.22 ? 180 ILE D C   1 
ATOM   6586  O O   . ILE D  2 146 ? 108.442 94.673  161.517 1.00 306.05 ? 180 ILE D O   1 
ATOM   6587  C CB  . ILE D  2 146 ? 105.607 96.348  161.583 1.00 303.74 ? 180 ILE D CB  1 
ATOM   6588  C CG1 . ILE D  2 146 ? 104.451 95.588  162.240 1.00 303.92 ? 180 ILE D CG1 1 
ATOM   6589  C CG2 . ILE D  2 146 ? 105.859 95.848  160.165 1.00 305.30 ? 180 ILE D CG2 1 
ATOM   6590  C CD1 . ILE D  2 146 ? 104.333 95.826  163.724 1.00 304.07 ? 180 ILE D CD1 1 
ATOM   6591  N N   . ASN D  2 147 ? 107.092 93.945  163.184 1.00 305.73 ? 181 ASN D N   1 
ATOM   6592  C CA  . ASN D  2 147 ? 107.576 92.566  163.286 1.00 307.25 ? 181 ASN D CA  1 
ATOM   6593  C C   . ASN D  2 147 ? 109.075 92.464  163.015 1.00 307.04 ? 181 ASN D C   1 
ATOM   6594  O O   . ASN D  2 147 ? 109.539 91.533  162.351 1.00 308.64 ? 181 ASN D O   1 
ATOM   6595  C CB  . ASN D  2 147 ? 106.741 91.611  162.402 1.00 310.45 ? 181 ASN D CB  1 
ATOM   6596  C CG  . ASN D  2 147 ? 107.064 91.676  160.906 1.00 311.09 ? 181 ASN D CG  1 
ATOM   6597  O OD1 . ASN D  2 147 ? 107.764 92.555  160.430 1.00 310.85 ? 181 ASN D OD1 1 
ATOM   6598  N ND2 . ASN D  2 147 ? 106.528 90.714  160.158 1.00 311.12 ? 181 ASN D ND2 1 
ATOM   6599  N N   . ASN D  2 148 ? 109.834 93.416  163.564 1.00 303.88 ? 182 ASN D N   1 
ATOM   6600  C CA  . ASN D  2 148 ? 111.278 93.515  163.388 1.00 301.69 ? 182 ASN D CA  1 
ATOM   6601  C C   . ASN D  2 148 ? 111.624 93.538  161.892 1.00 300.65 ? 182 ASN D C   1 
ATOM   6602  O O   . ASN D  2 148 ? 112.377 92.704  161.384 1.00 298.63 ? 182 ASN D O   1 
ATOM   6603  C CB  . ASN D  2 148 ? 111.947 92.368  164.167 1.00 300.19 ? 182 ASN D CB  1 
ATOM   6604  C CG  . ASN D  2 148 ? 113.439 92.181  163.909 1.00 297.15 ? 182 ASN D CG  1 
ATOM   6605  O OD1 . ASN D  2 148 ? 113.859 91.443  163.022 1.00 296.11 ? 182 ASN D OD1 1 
ATOM   6606  N ND2 . ASN D  2 148 ? 114.238 92.813  164.755 1.00 295.48 ? 182 ASN D ND2 1 
ATOM   6607  N N   . GLN D  2 149 ? 111.027 94.487  161.166 1.00 300.87 ? 183 GLN D N   1 
ATOM   6608  C CA  . GLN D  2 149 ? 111.177 94.616  159.720 1.00 301.72 ? 183 GLN D CA  1 
ATOM   6609  C C   . GLN D  2 149 ? 110.571 95.950  159.295 1.00 301.15 ? 183 GLN D C   1 
ATOM   6610  O O   . GLN D  2 149 ? 109.562 96.398  159.846 1.00 301.57 ? 183 GLN D O   1 
ATOM   6611  C CB  . GLN D  2 149 ? 110.533 93.429  158.982 1.00 304.08 ? 183 GLN D CB  1 
ATOM   6612  C CG  . GLN D  2 149 ? 110.212 93.659  157.509 1.00 304.31 ? 183 GLN D CG  1 
ATOM   6613  C CD  . GLN D  2 149 ? 108.767 94.048  157.271 1.00 306.08 ? 183 GLN D CD  1 
ATOM   6614  O OE1 . GLN D  2 149 ? 108.095 94.569  158.159 1.00 307.29 ? 183 GLN D OE1 1 
ATOM   6615  N NE2 . GLN D  2 149 ? 108.286 93.811  156.061 1.00 305.01 ? 183 GLN D NE2 1 
ATOM   6616  N N   . SER D  2 150 ? 111.212 96.592  158.319 1.00 300.59 ? 184 SER D N   1 
ATOM   6617  C CA  . SER D  2 150 ? 110.758 97.899  157.858 1.00 300.58 ? 184 SER D CA  1 
ATOM   6618  C C   . SER D  2 150 ? 109.343 97.813  157.293 1.00 304.26 ? 184 SER D C   1 
ATOM   6619  O O   . SER D  2 150 ? 108.983 96.854  156.606 1.00 306.04 ? 184 SER D O   1 
ATOM   6620  C CB  . SER D  2 150 ? 111.715 98.456  156.803 1.00 300.63 ? 184 SER D CB  1 
ATOM   6621  O OG  . SER D  2 150 ? 111.903 97.537  155.740 1.00 301.02 ? 184 SER D OG  1 
ATOM   6622  N N   . LEU D  2 151 ? 108.545 98.838  157.583 1.00 303.15 ? 185 LEU D N   1 
ATOM   6623  C CA  . LEU D  2 151 ? 107.118 98.792  157.284 1.00 304.64 ? 185 LEU D CA  1 
ATOM   6624  C C   . LEU D  2 151 ? 106.885 98.596  155.788 1.00 306.84 ? 185 LEU D C   1 
ATOM   6625  O O   . LEU D  2 151 ? 107.559 99.237  154.968 1.00 307.16 ? 185 LEU D O   1 
ATOM   6626  C CB  . LEU D  2 151 ? 106.423 100.069 157.770 1.00 302.50 ? 185 LEU D CB  1 
ATOM   6627  C CG  . LEU D  2 151 ? 106.468 101.364 156.950 1.00 299.64 ? 185 LEU D CG  1 
ATOM   6628  C CD1 . LEU D  2 151 ? 105.512 102.392 157.539 1.00 298.02 ? 185 LEU D CD1 1 
ATOM   6629  C CD2 . LEU D  2 151 ? 107.878 101.929 156.873 1.00 295.31 ? 185 LEU D CD2 1 
ATOM   6630  N N   . PRO D  2 152 ? 105.975 97.703  155.392 1.00 308.17 ? 186 PRO D N   1 
ATOM   6631  C CA  . PRO D  2 152 ? 105.678 97.497  153.968 1.00 311.62 ? 186 PRO D CA  1 
ATOM   6632  C C   . PRO D  2 152 ? 104.792 98.612  153.434 1.00 317.25 ? 186 PRO D C   1 
ATOM   6633  O O   . PRO D  2 152 ? 103.703 98.868  153.958 1.00 317.33 ? 186 PRO D O   1 
ATOM   6634  C CB  . PRO D  2 152 ? 104.964 96.138  153.957 1.00 309.16 ? 186 PRO D CB  1 
ATOM   6635  C CG  . PRO D  2 152 ? 104.326 96.043  155.300 1.00 306.87 ? 186 PRO D CG  1 
ATOM   6636  C CD  . PRO D  2 152 ? 105.228 96.774  156.260 1.00 307.02 ? 186 PRO D CD  1 
ATOM   6637  N N   . VAL D  2 153 ? 105.262 99.284  152.381 1.00 321.10 ? 187 VAL D N   1 
ATOM   6638  C CA  . VAL D  2 153 ? 104.532 100.421 151.834 1.00 324.30 ? 187 VAL D CA  1 
ATOM   6639  C C   . VAL D  2 153 ? 103.196 99.954  151.278 1.00 328.58 ? 187 VAL D C   1 
ATOM   6640  O O   . VAL D  2 153 ? 103.129 99.020  150.469 1.00 329.99 ? 187 VAL D O   1 
ATOM   6641  C CB  . VAL D  2 153 ? 105.371 101.128 150.760 1.00 324.15 ? 187 VAL D CB  1 
ATOM   6642  C CG1 . VAL D  2 153 ? 104.627 102.340 150.219 1.00 323.96 ? 187 VAL D CG1 1 
ATOM   6643  C CG2 . VAL D  2 153 ? 106.722 101.533 151.326 1.00 322.33 ? 187 VAL D CG2 1 
ATOM   6644  N N   . SER D  2 154 ? 102.122 100.611 151.711 1.00 331.20 ? 188 SER D N   1 
ATOM   6645  C CA  . SER D  2 154 ? 100.770 100.267 151.295 1.00 335.38 ? 188 SER D CA  1 
ATOM   6646  C C   . SER D  2 154 ? 99.856  101.431 151.638 1.00 339.44 ? 188 SER D C   1 
ATOM   6647  O O   . SER D  2 154 ? 100.107 102.137 152.622 1.00 339.43 ? 188 SER D O   1 
ATOM   6648  C CB  . SER D  2 154 ? 100.287 98.983  151.986 1.00 335.55 ? 188 SER D CB  1 
ATOM   6649  O OG  . SER D  2 154 ? 98.897  98.783  151.797 1.00 339.32 ? 188 SER D OG  1 
ATOM   6650  N N   . PRO D  2 155 ? 98.800  101.665 150.854 1.00 341.71 ? 189 PRO D N   1 
ATOM   6651  C CA  . PRO D  2 155 ? 97.821  102.692 151.246 1.00 342.47 ? 189 PRO D CA  1 
ATOM   6652  C C   . PRO D  2 155 ? 97.140  102.381 152.564 1.00 342.71 ? 189 PRO D C   1 
ATOM   6653  O O   . PRO D  2 155 ? 96.624  103.294 153.222 1.00 342.85 ? 189 PRO D O   1 
ATOM   6654  C CB  . PRO D  2 155 ? 96.829  102.688 150.074 1.00 341.65 ? 189 PRO D CB  1 
ATOM   6655  C CG  . PRO D  2 155 ? 96.969  101.318 149.478 1.00 341.44 ? 189 PRO D CG  1 
ATOM   6656  C CD  . PRO D  2 155 ? 98.437  101.024 149.579 1.00 341.15 ? 189 PRO D CD  1 
ATOM   6657  N N   . ARG D  2 156 ? 97.123  101.108 152.964 1.00 342.69 ? 190 ARG D N   1 
ATOM   6658  C CA  . ARG D  2 156 ? 96.589  100.716 154.262 1.00 341.82 ? 190 ARG D CA  1 
ATOM   6659  C C   . ARG D  2 156 ? 97.340  101.372 155.416 1.00 341.06 ? 190 ARG D C   1 
ATOM   6660  O O   . ARG D  2 156 ? 96.740  101.628 156.467 1.00 342.29 ? 190 ARG D O   1 
ATOM   6661  C CB  . ARG D  2 156 ? 96.629  99.189  154.371 1.00 341.87 ? 190 ARG D CB  1 
ATOM   6662  C CG  . ARG D  2 156 ? 96.440  98.618  155.760 1.00 342.77 ? 190 ARG D CG  1 
ATOM   6663  C CD  . ARG D  2 156 ? 97.296  97.372  155.946 1.00 342.70 ? 190 ARG D CD  1 
ATOM   6664  N NE  . ARG D  2 156 ? 97.210  96.851  157.304 1.00 344.25 ? 190 ARG D NE  1 
ATOM   6665  C CZ  . ARG D  2 156 ? 96.148  96.235  157.805 1.00 347.26 ? 190 ARG D CZ  1 
ATOM   6666  N NH1 . ARG D  2 156 ? 95.073  95.999  157.070 1.00 348.48 ? 190 ARG D NH1 1 
ATOM   6667  N NH2 . ARG D  2 156 ? 96.161  95.853  159.078 1.00 349.82 ? 190 ARG D NH2 1 
ATOM   6668  N N   . LEU D  2 157 ? 98.629  101.669 155.240 1.00 338.56 ? 191 LEU D N   1 
ATOM   6669  C CA  . LEU D  2 157 ? 99.423  102.354 156.261 1.00 334.85 ? 191 LEU D CA  1 
ATOM   6670  C C   . LEU D  2 157 ? 99.401  103.852 155.966 1.00 333.62 ? 191 LEU D C   1 
ATOM   6671  O O   . LEU D  2 157 ? 100.160 104.369 155.147 1.00 331.97 ? 191 LEU D O   1 
ATOM   6672  C CB  . LEU D  2 157 ? 100.847 101.805 156.298 1.00 329.52 ? 191 LEU D CB  1 
ATOM   6673  C CG  . LEU D  2 157 ? 101.023 100.298 156.489 1.00 328.17 ? 191 LEU D CG  1 
ATOM   6674  C CD1 . LEU D  2 157 ? 102.490 99.961  156.699 1.00 316.74 ? 191 LEU D CD1 1 
ATOM   6675  C CD2 . LEU D  2 157 ? 100.190 99.802  157.656 1.00 331.29 ? 191 LEU D CD2 1 
ATOM   6676  N N   . GLN D  2 158 ? 98.506  104.554 156.656 1.00 334.59 ? 192 GLN D N   1 
ATOM   6677  C CA  . GLN D  2 158 ? 98.380  105.993 156.487 1.00 332.37 ? 192 GLN D CA  1 
ATOM   6678  C C   . GLN D  2 158 ? 99.363  106.726 157.392 1.00 328.58 ? 192 GLN D C   1 
ATOM   6679  O O   . GLN D  2 158 ? 99.649  106.298 158.514 1.00 328.44 ? 192 GLN D O   1 
ATOM   6680  C CB  . GLN D  2 158 ? 96.948  106.445 156.788 1.00 334.72 ? 192 GLN D CB  1 
ATOM   6681  C CG  . GLN D  2 158 ? 96.682  107.933 156.573 1.00 332.11 ? 192 GLN D CG  1 
ATOM   6682  C CD  . GLN D  2 158 ? 96.652  108.728 157.868 1.00 330.66 ? 192 GLN D CD  1 
ATOM   6683  O OE1 . GLN D  2 158 ? 97.548  108.617 158.705 1.00 331.30 ? 192 GLN D OE1 1 
ATOM   6684  N NE2 . GLN D  2 158 ? 95.613  109.537 158.038 1.00 330.45 ? 192 GLN D NE2 1 
ATOM   6685  N N   . LEU D  2 159 ? 99.879  107.846 156.891 1.00 325.45 ? 193 LEU D N   1 
ATOM   6686  C CA  . LEU D  2 159 ? 100.812 108.678 157.634 1.00 319.90 ? 193 LEU D CA  1 
ATOM   6687  C C   . LEU D  2 159 ? 100.323 110.120 157.640 1.00 319.48 ? 193 LEU D C   1 
ATOM   6688  O O   . LEU D  2 159 ? 99.875  110.645 156.617 1.00 320.65 ? 193 LEU D O   1 
ATOM   6689  C CB  . LEU D  2 159 ? 102.223 108.595 157.039 1.00 314.16 ? 193 LEU D CB  1 
ATOM   6690  C CG  . LEU D  2 159 ? 102.886 107.216 157.113 1.00 310.84 ? 193 LEU D CG  1 
ATOM   6691  C CD1 . LEU D  2 159 ? 103.992 107.084 156.078 1.00 303.10 ? 193 LEU D CD1 1 
ATOM   6692  C CD2 . LEU D  2 159 ? 103.423 106.943 158.514 1.00 307.98 ? 193 LEU D CD2 1 
ATOM   6693  N N   . SER D  2 160 ? 100.421 110.755 158.806 1.00 316.50 ? 194 SER D N   1 
ATOM   6694  C CA  . SER D  2 160 ? 99.958  112.124 158.986 1.00 315.25 ? 194 SER D CA  1 
ATOM   6695  C C   . SER D  2 160 ? 100.943 112.862 159.882 1.00 310.78 ? 194 SER D C   1 
ATOM   6696  O O   . SER D  2 160 ? 101.782 112.251 160.551 1.00 308.40 ? 194 SER D O   1 
ATOM   6697  C CB  . SER D  2 160 ? 98.540  112.166 159.566 1.00 316.90 ? 194 SER D CB  1 
ATOM   6698  O OG  . SER D  2 160 ? 98.428  111.341 160.712 1.00 316.92 ? 194 SER D OG  1 
ATOM   6699  N N   . ASN D  2 161 ? 100.828 114.191 159.889 1.00 311.17 ? 195 ASN D N   1 
ATOM   6700  C CA  . ASN D  2 161 ? 101.791 115.075 160.545 1.00 309.77 ? 195 ASN D CA  1 
ATOM   6701  C C   . ASN D  2 161 ? 103.187 114.760 160.008 1.00 307.44 ? 195 ASN D C   1 
ATOM   6702  O O   . ASN D  2 161 ? 104.089 114.303 160.714 1.00 304.43 ? 195 ASN D O   1 
ATOM   6703  C CB  . ASN D  2 161 ? 101.694 114.959 162.074 1.00 309.11 ? 195 ASN D CB  1 
ATOM   6704  C CG  . ASN D  2 161 ? 102.808 115.696 162.804 1.00 304.54 ? 195 ASN D CG  1 
ATOM   6705  O OD1 . ASN D  2 161 ? 103.729 115.079 163.339 1.00 299.69 ? 195 ASN D OD1 1 
ATOM   6706  N ND2 . ASN D  2 161 ? 102.724 117.021 162.831 1.00 304.53 ? 195 ASN D ND2 1 
ATOM   6707  N N   . GLY D  2 162 ? 103.328 114.974 158.704 1.00 307.35 ? 196 GLY D N   1 
ATOM   6708  C CA  . GLY D  2 162 ? 104.436 114.393 157.981 1.00 304.94 ? 196 GLY D CA  1 
ATOM   6709  C C   . GLY D  2 162 ? 104.249 112.891 157.969 1.00 305.09 ? 196 GLY D C   1 
ATOM   6710  O O   . GLY D  2 162 ? 103.316 112.387 157.341 1.00 308.38 ? 196 GLY D O   1 
ATOM   6711  N N   . ASN D  2 163 ? 105.122 112.162 158.655 1.00 301.29 ? 197 ASN D N   1 
ATOM   6712  C CA  . ASN D  2 163 ? 104.933 110.734 158.872 1.00 300.70 ? 197 ASN D CA  1 
ATOM   6713  C C   . ASN D  2 163 ? 105.454 110.309 160.242 1.00 296.36 ? 197 ASN D C   1 
ATOM   6714  O O   . ASN D  2 163 ? 106.023 109.223 160.391 1.00 293.84 ? 197 ASN D O   1 
ATOM   6715  C CB  . ASN D  2 163 ? 105.533 109.944 157.698 1.00 297.65 ? 197 ASN D CB  1 
ATOM   6716  C CG  . ASN D  2 163 ? 106.885 110.480 157.247 1.00 293.16 ? 197 ASN D CG  1 
ATOM   6717  O OD1 . ASN D  2 163 ? 107.081 111.689 157.221 1.00 294.86 ? 197 ASN D OD1 1 
ATOM   6718  N ND2 . ASN D  2 163 ? 107.782 109.591 156.833 1.00 289.28 ? 197 ASN D ND2 1 
ATOM   6719  N N   . ARG D  2 164 ? 105.269 111.176 161.245 1.00 293.91 ? 198 ARG D N   1 
ATOM   6720  C CA  . ARG D  2 164 ? 105.423 110.801 162.646 1.00 291.79 ? 198 ARG D CA  1 
ATOM   6721  C C   . ARG D  2 164 ? 104.215 110.032 163.176 1.00 299.12 ? 198 ARG D C   1 
ATOM   6722  O O   . ARG D  2 164 ? 104.357 109.247 164.120 1.00 299.77 ? 198 ARG D O   1 
ATOM   6723  C CB  . ARG D  2 164 ? 105.672 112.063 163.486 1.00 285.51 ? 198 ARG D CB  1 
ATOM   6724  C CG  . ARG D  2 164 ? 105.335 111.952 164.962 1.00 285.84 ? 198 ARG D CG  1 
ATOM   6725  C CD  . ARG D  2 164 ? 105.555 113.274 165.670 1.00 281.50 ? 198 ARG D CD  1 
ATOM   6726  N NE  . ARG D  2 164 ? 106.976 113.460 165.934 1.00 276.26 ? 198 ARG D NE  1 
ATOM   6727  C CZ  . ARG D  2 164 ? 107.519 113.561 167.138 1.00 275.70 ? 198 ARG D CZ  1 
ATOM   6728  N NH1 . ARG D  2 164 ? 106.780 113.544 168.235 1.00 277.25 ? 198 ARG D NH1 1 
ATOM   6729  N NH2 . ARG D  2 164 ? 108.839 113.668 167.244 1.00 272.21 ? 198 ARG D NH2 1 
ATOM   6730  N N   . THR D  2 165 ? 103.038 110.225 162.588 1.00 302.40 ? 199 THR D N   1 
ATOM   6731  C CA  . THR D  2 165 ? 101.824 109.538 163.010 1.00 305.89 ? 199 THR D CA  1 
ATOM   6732  C C   . THR D  2 165 ? 101.508 108.420 162.025 1.00 310.06 ? 199 THR D C   1 
ATOM   6733  O O   . THR D  2 165 ? 101.370 108.669 160.823 1.00 312.36 ? 199 THR D O   1 
ATOM   6734  C CB  . THR D  2 165 ? 100.640 110.505 163.100 1.00 307.29 ? 199 THR D CB  1 
ATOM   6735  O OG1 . THR D  2 165 ? 100.856 111.448 164.158 1.00 303.61 ? 199 THR D OG1 1 
ATOM   6736  C CG2 . THR D  2 165 ? 99.346  109.738 163.362 1.00 310.87 ? 199 THR D CG2 1 
ATOM   6737  N N   . LEU D  2 166 ? 101.385 107.197 162.537 1.00 312.42 ? 200 LEU D N   1 
ATOM   6738  C CA  . LEU D  2 166 ? 101.060 106.029 161.727 1.00 316.67 ? 200 LEU D CA  1 
ATOM   6739  C C   . LEU D  2 166 ? 99.642  105.587 162.058 1.00 324.94 ? 200 LEU D C   1 
ATOM   6740  O O   . LEU D  2 166 ? 99.374  105.138 163.177 1.00 325.29 ? 200 LEU D O   1 
ATOM   6741  C CB  . LEU D  2 166 ? 102.048 104.890 161.982 1.00 310.32 ? 200 LEU D CB  1 
ATOM   6742  C CG  . LEU D  2 166 ? 101.882 103.608 161.161 1.00 311.26 ? 200 LEU D CG  1 
ATOM   6743  C CD1 . LEU D  2 166 ? 101.482 103.915 159.722 1.00 319.17 ? 200 LEU D CD1 1 
ATOM   6744  C CD2 . LEU D  2 166 ? 103.148 102.766 161.200 1.00 303.46 ? 200 LEU D CD2 1 
ATOM   6745  N N   . THR D  2 167 ? 98.744  105.699 161.084 1.00 331.13 ? 201 THR D N   1 
ATOM   6746  C CA  . THR D  2 167 ? 97.350  105.309 161.250 1.00 336.18 ? 201 THR D CA  1 
ATOM   6747  C C   . THR D  2 167 ? 97.103  104.040 160.450 1.00 340.58 ? 201 THR D C   1 
ATOM   6748  O O   . THR D  2 167 ? 97.441  103.975 159.263 1.00 340.13 ? 201 THR D O   1 
ATOM   6749  C CB  . THR D  2 167 ? 96.404  106.423 160.796 1.00 337.48 ? 201 THR D CB  1 
ATOM   6750  O OG1 . THR D  2 167 ? 96.844  107.676 161.335 1.00 333.28 ? 201 THR D OG1 1 
ATOM   6751  C CG2 . THR D  2 167 ? 94.985  106.144 161.269 1.00 340.51 ? 201 THR D CG2 1 
ATOM   6752  N N   . LEU D  2 168 ? 96.515  103.040 161.098 1.00 344.68 ? 202 LEU D N   1 
ATOM   6753  C CA  . LEU D  2 168 ? 96.189  101.773 160.453 1.00 346.63 ? 202 LEU D CA  1 
ATOM   6754  C C   . LEU D  2 168 ? 94.718  101.807 160.057 1.00 349.47 ? 202 LEU D C   1 
ATOM   6755  O O   . LEU D  2 168 ? 93.838  101.765 160.920 1.00 351.45 ? 202 LEU D O   1 
ATOM   6756  C CB  . LEU D  2 168 ? 96.489  100.604 161.387 1.00 345.74 ? 202 LEU D CB  1 
ATOM   6757  C CG  . LEU D  2 168 ? 96.465  99.216  160.749 1.00 345.91 ? 202 LEU D CG  1 
ATOM   6758  C CD1 . LEU D  2 168 ? 97.045  99.284  159.354 1.00 344.12 ? 202 LEU D CD1 1 
ATOM   6759  C CD2 . LEU D  2 168 ? 97.231  98.218  161.603 1.00 343.86 ? 202 LEU D CD2 1 
ATOM   6760  N N   . LEU D  2 169 ? 94.453  101.878 158.750 1.00 350.29 ? 203 LEU D N   1 
ATOM   6761  C CA  . LEU D  2 169 ? 93.089  102.102 158.277 1.00 351.31 ? 203 LEU D CA  1 
ATOM   6762  C C   . LEU D  2 169 ? 92.158  100.957 158.658 1.00 354.40 ? 203 LEU D C   1 
ATOM   6763  O O   . LEU D  2 169 ? 91.024  101.190 159.092 1.00 355.24 ? 203 LEU D O   1 
ATOM   6764  C CB  . LEU D  2 169 ? 93.089  102.312 156.763 1.00 349.44 ? 203 LEU D CB  1 
ATOM   6765  C CG  . LEU D  2 169 ? 93.992  103.431 156.241 1.00 345.88 ? 203 LEU D CG  1 
ATOM   6766  C CD1 . LEU D  2 169 ? 93.726  103.691 154.767 1.00 344.39 ? 203 LEU D CD1 1 
ATOM   6767  C CD2 . LEU D  2 169 ? 93.787  104.700 157.054 1.00 344.28 ? 203 LEU D CD2 1 
ATOM   6768  N N   . SER D  2 170 ? 92.612  99.715  158.505 1.00 354.53 ? 204 SER D N   1 
ATOM   6769  C CA  . SER D  2 170 ? 91.777  98.547  158.778 1.00 355.66 ? 204 SER D CA  1 
ATOM   6770  C C   . SER D  2 170 ? 92.648  97.470  159.407 1.00 355.72 ? 204 SER D C   1 
ATOM   6771  O O   . SER D  2 170 ? 93.397  96.787  158.702 1.00 354.68 ? 204 SER D O   1 
ATOM   6772  C CB  . SER D  2 170 ? 91.111  98.033  157.502 1.00 354.65 ? 204 SER D CB  1 
ATOM   6773  O OG  . SER D  2 170 ? 90.041  98.876  157.111 1.00 353.51 ? 204 SER D OG  1 
ATOM   6774  N N   . VAL D  2 171 ? 92.542  97.308  160.722 1.00 356.58 ? 205 VAL D N   1 
ATOM   6775  C CA  . VAL D  2 171 ? 93.381  96.357  161.439 1.00 355.80 ? 205 VAL D CA  1 
ATOM   6776  C C   . VAL D  2 171 ? 92.797  94.957  161.312 1.00 355.77 ? 205 VAL D C   1 
ATOM   6777  O O   . VAL D  2 171 ? 91.601  94.772  161.062 1.00 356.85 ? 205 VAL D O   1 
ATOM   6778  C CB  . VAL D  2 171 ? 93.530  96.767  162.918 1.00 355.06 ? 205 VAL D CB  1 
ATOM   6779  C CG1 . VAL D  2 171 ? 93.798  98.255  163.029 1.00 354.05 ? 205 VAL D CG1 1 
ATOM   6780  C CG2 . VAL D  2 171 ? 92.297  96.369  163.713 1.00 355.84 ? 205 VAL D CG2 1 
ATOM   6781  N N   . THR D  2 172 ? 93.661  93.958  161.478 1.00 354.66 ? 206 THR D N   1 
ATOM   6782  C CA  . THR D  2 172 ? 93.256  92.561  161.531 1.00 352.18 ? 206 THR D CA  1 
ATOM   6783  C C   . THR D  2 172 ? 94.013  91.882  162.661 1.00 349.34 ? 206 THR D C   1 
ATOM   6784  O O   . THR D  2 172 ? 95.048  92.374  163.118 1.00 349.49 ? 206 THR D O   1 
ATOM   6785  C CB  . THR D  2 172 ? 93.525  91.818  160.210 1.00 351.82 ? 206 THR D CB  1 
ATOM   6786  O OG1 . THR D  2 172 ? 94.935  91.784  159.954 1.00 352.56 ? 206 THR D OG1 1 
ATOM   6787  C CG2 . THR D  2 172 ? 92.812  92.492  159.044 1.00 352.96 ? 206 THR D CG2 1 
ATOM   6788  N N   . ARG D  2 173 ? 93.481  90.744  163.116 1.00 345.77 ? 207 ARG D N   1 
ATOM   6789  C CA  . ARG D  2 173 ? 94.153  89.994  164.172 1.00 341.53 ? 207 ARG D CA  1 
ATOM   6790  C C   . ARG D  2 173 ? 95.499  89.454  163.705 1.00 342.71 ? 207 ARG D C   1 
ATOM   6791  O O   . ARG D  2 173 ? 96.382  89.191  164.530 1.00 342.26 ? 207 ARG D O   1 
ATOM   6792  C CB  . ARG D  2 173 ? 93.259  88.853  164.658 1.00 333.96 ? 207 ARG D CB  1 
ATOM   6793  C CG  . ARG D  2 173 ? 92.769  87.929  163.557 1.00 328.72 ? 207 ARG D CG  1 
ATOM   6794  C CD  . ARG D  2 173 ? 92.186  86.652  164.139 1.00 321.50 ? 207 ARG D CD  1 
ATOM   6795  N NE  . ARG D  2 173 ? 91.285  86.925  165.252 1.00 317.19 ? 207 ARG D NE  1 
ATOM   6796  C CZ  . ARG D  2 173 ? 90.775  85.995  166.048 1.00 312.37 ? 207 ARG D CZ  1 
ATOM   6797  N NH1 . ARG D  2 173 ? 91.056  84.713  165.883 1.00 309.25 ? 207 ARG D NH1 1 
ATOM   6798  N NH2 . ARG D  2 173 ? 89.962  86.361  167.036 1.00 312.18 ? 207 ARG D NH2 1 
ATOM   6799  N N   . ASN D  2 174 ? 95.676  89.284  162.393 1.00 343.78 ? 208 ASN D N   1 
ATOM   6800  C CA  . ASN D  2 174 ? 96.944  88.813  161.850 1.00 342.25 ? 208 ASN D CA  1 
ATOM   6801  C C   . ASN D  2 174 ? 98.037  89.872  161.891 1.00 342.73 ? 208 ASN D C   1 
ATOM   6802  O O   . ASN D  2 174 ? 99.201  89.544  161.641 1.00 341.01 ? 208 ASN D O   1 
ATOM   6803  C CB  . ASN D  2 174 ? 96.750  88.332  160.411 1.00 339.45 ? 208 ASN D CB  1 
ATOM   6804  C CG  . ASN D  2 174 ? 96.430  86.854  160.329 1.00 335.48 ? 208 ASN D CG  1 
ATOM   6805  O OD1 . ASN D  2 174 ? 96.500  86.136  161.327 1.00 335.20 ? 208 ASN D OD1 1 
ATOM   6806  N ND2 . ASN D  2 174 ? 96.075  86.390  159.137 1.00 332.09 ? 208 ASN D ND2 1 
ATOM   6807  N N   . ASP D  2 175 ? 97.698  91.123  162.197 1.00 344.42 ? 209 ASP D N   1 
ATOM   6808  C CA  . ASP D  2 175 ? 98.678  92.201  162.241 1.00 341.55 ? 209 ASP D CA  1 
ATOM   6809  C C   . ASP D  2 175 ? 99.349  92.341  163.600 1.00 336.75 ? 209 ASP D C   1 
ATOM   6810  O O   . ASP D  2 175 ? 100.152 93.263  163.779 1.00 331.31 ? 209 ASP D O   1 
ATOM   6811  C CB  . ASP D  2 175 ? 98.019  93.528  161.861 1.00 344.88 ? 209 ASP D CB  1 
ATOM   6812  C CG  . ASP D  2 175 ? 97.471  93.521  160.452 1.00 349.54 ? 209 ASP D CG  1 
ATOM   6813  O OD1 . ASP D  2 175 ? 98.271  93.405  159.501 1.00 349.39 ? 209 ASP D OD1 1 
ATOM   6814  O OD2 . ASP D  2 175 ? 96.238  93.642  160.293 1.00 352.99 ? 209 ASP D OD2 1 
ATOM   6815  N N   . THR D  2 176 ? 99.038  91.463  164.552 1.00 336.33 ? 210 THR D N   1 
ATOM   6816  C CA  . THR D  2 176 ? 99.615  91.562  165.885 1.00 331.61 ? 210 THR D CA  1 
ATOM   6817  C C   . THR D  2 176 ? 101.131 91.428  165.825 1.00 326.61 ? 210 THR D C   1 
ATOM   6818  O O   . THR D  2 176 ? 101.662 90.435  165.321 1.00 326.86 ? 210 THR D O   1 
ATOM   6819  C CB  . THR D  2 176 ? 99.028  90.483  166.795 1.00 333.45 ? 210 THR D CB  1 
ATOM   6820  O OG1 . THR D  2 176 ? 97.598  90.544  166.746 1.00 335.81 ? 210 THR D OG1 1 
ATOM   6821  C CG2 . THR D  2 176 ? 99.490  90.688  168.230 1.00 329.64 ? 210 THR D CG2 1 
ATOM   6822  N N   . GLY D  2 177 ? 101.825 92.438  166.342 1.00 320.45 ? 211 GLY D N   1 
ATOM   6823  C CA  . GLY D  2 177 ? 103.267 92.451  166.346 1.00 315.93 ? 211 GLY D CA  1 
ATOM   6824  C C   . GLY D  2 177 ? 103.824 93.605  167.153 1.00 311.74 ? 211 GLY D C   1 
ATOM   6825  O O   . GLY D  2 177 ? 103.083 94.430  167.697 1.00 310.55 ? 211 GLY D O   1 
ATOM   6826  N N   . PRO D  2 178 ? 105.152 93.684  167.248 1.00 309.28 ? 212 PRO D N   1 
ATOM   6827  C CA  . PRO D  2 178 ? 105.776 94.768  168.018 1.00 306.03 ? 212 PRO D CA  1 
ATOM   6828  C C   . PRO D  2 178 ? 105.913 96.029  167.175 1.00 303.15 ? 212 PRO D C   1 
ATOM   6829  O O   . PRO D  2 178 ? 106.564 96.025  166.127 1.00 302.77 ? 212 PRO D O   1 
ATOM   6830  C CB  . PRO D  2 178 ? 107.147 94.194  168.394 1.00 303.14 ? 212 PRO D CB  1 
ATOM   6831  C CG  . PRO D  2 178 ? 107.429 93.135  167.355 1.00 303.00 ? 212 PRO D CG  1 
ATOM   6832  C CD  . PRO D  2 178 ? 106.148 92.791  166.633 1.00 306.08 ? 212 PRO D CD  1 
ATOM   6833  N N   . TYR D  2 179 ? 105.296 97.112  167.640 1.00 301.23 ? 213 TYR D N   1 
ATOM   6834  C CA  . TYR D  2 179 ? 105.365 98.410  166.981 1.00 298.45 ? 213 TYR D CA  1 
ATOM   6835  C C   . TYR D  2 179 ? 106.422 99.255  167.677 1.00 294.04 ? 213 TYR D C   1 
ATOM   6836  O O   . TYR D  2 179 ? 106.430 99.360  168.908 1.00 294.26 ? 213 TYR D O   1 
ATOM   6837  C CB  . TYR D  2 179 ? 104.008 99.110  166.988 1.00 299.71 ? 213 TYR D CB  1 
ATOM   6838  C CG  . TYR D  2 179 ? 103.011 98.468  166.054 1.00 300.89 ? 213 TYR D CG  1 
ATOM   6839  C CD1 . TYR D  2 179 ? 102.382 97.278  166.390 1.00 303.87 ? 213 TYR D CD1 1 
ATOM   6840  C CD2 . TYR D  2 179 ? 102.715 99.042  164.825 1.00 301.69 ? 213 TYR D CD2 1 
ATOM   6841  C CE1 . TYR D  2 179 ? 101.478 96.685  165.535 1.00 307.01 ? 213 TYR D CE1 1 
ATOM   6842  C CE2 . TYR D  2 179 ? 101.810 98.457  163.964 1.00 303.73 ? 213 TYR D CE2 1 
ATOM   6843  C CZ  . TYR D  2 179 ? 101.194 97.278  164.323 1.00 308.13 ? 213 TYR D CZ  1 
ATOM   6844  O OH  . TYR D  2 179 ? 100.293 96.691  163.465 1.00 314.74 ? 213 TYR D OH  1 
ATOM   6845  N N   . GLU D  2 180 ? 107.305 99.854  166.885 1.00 288.64 ? 214 GLU D N   1 
ATOM   6846  C CA  . GLU D  2 180 ? 108.527 100.458 167.387 1.00 283.22 ? 214 GLU D CA  1 
ATOM   6847  C C   . GLU D  2 180 ? 109.007 101.488 166.374 1.00 279.87 ? 214 GLU D C   1 
ATOM   6848  O O   . GLU D  2 180 ? 109.124 101.190 165.182 1.00 279.94 ? 214 GLU D O   1 
ATOM   6849  C CB  . GLU D  2 180 ? 109.572 99.360  167.630 1.00 284.23 ? 214 GLU D CB  1 
ATOM   6850  C CG  . GLU D  2 180 ? 110.987 99.813  167.857 1.00 279.97 ? 214 GLU D CG  1 
ATOM   6851  C CD  . GLU D  2 180 ? 111.922 98.643  168.102 1.00 280.83 ? 214 GLU D CD  1 
ATOM   6852  O OE1 . GLU D  2 180 ? 111.752 97.945  169.121 1.00 284.14 ? 214 GLU D OE1 1 
ATOM   6853  O OE2 . GLU D  2 180 ? 112.817 98.407  167.263 1.00 278.46 ? 214 GLU D OE2 1 
ATOM   6854  N N   . CYS D  2 181 ? 109.286 102.703 166.846 1.00 277.86 ? 215 CYS D N   1 
ATOM   6855  C CA  . CYS D  2 181 ? 109.576 103.817 165.951 1.00 276.49 ? 215 CYS D CA  1 
ATOM   6856  C C   . CYS D  2 181 ? 110.901 104.476 166.304 1.00 270.56 ? 215 CYS D C   1 
ATOM   6857  O O   . CYS D  2 181 ? 111.359 104.412 167.450 1.00 268.37 ? 215 CYS D O   1 
ATOM   6858  C CB  . CYS D  2 181 ? 108.449 104.861 165.966 1.00 282.26 ? 215 CYS D CB  1 
ATOM   6859  S SG  . CYS D  2 181 ? 108.465 106.101 167.290 1.00 288.53 ? 215 CYS D SG  1 
ATOM   6860  N N   . GLU D  2 182 ? 111.505 105.112 165.301 1.00 265.57 ? 216 GLU D N   1 
ATOM   6861  C CA  . GLU D  2 182 ? 112.832 105.699 165.390 1.00 257.87 ? 216 GLU D CA  1 
ATOM   6862  C C   . GLU D  2 182 ? 112.756 107.185 165.079 1.00 251.05 ? 216 GLU D C   1 
ATOM   6863  O O   . GLU D  2 182 ? 111.985 107.617 164.218 1.00 253.39 ? 216 GLU D O   1 
ATOM   6864  C CB  . GLU D  2 182 ? 113.802 105.031 164.400 1.00 257.14 ? 216 GLU D CB  1 
ATOM   6865  C CG  . GLU D  2 182 ? 115.252 105.507 164.461 1.00 248.83 ? 216 GLU D CG  1 
ATOM   6866  C CD  . GLU D  2 182 ? 115.829 105.500 165.857 1.00 245.23 ? 216 GLU D CD  1 
ATOM   6867  O OE1 . GLU D  2 182 ? 116.305 106.555 166.318 1.00 238.45 ? 216 GLU D OE1 1 
ATOM   6868  O OE2 . GLU D  2 182 ? 115.845 104.426 166.481 1.00 248.27 ? 216 GLU D OE2 1 
ATOM   6869  N N   . ILE D  2 183 ? 113.565 107.963 165.792 1.00 242.81 ? 217 ILE D N   1 
ATOM   6870  C CA  . ILE D  2 183 ? 113.760 109.380 165.513 1.00 238.44 ? 217 ILE D CA  1 
ATOM   6871  C C   . ILE D  2 183 ? 115.259 109.616 165.350 1.00 231.12 ? 217 ILE D C   1 
ATOM   6872  O O   . ILE D  2 183 ? 116.060 109.187 166.188 1.00 231.10 ? 217 ILE D O   1 
ATOM   6873  C CB  . ILE D  2 183 ? 113.070 110.260 166.586 1.00 242.11 ? 217 ILE D CB  1 
ATOM   6874  C CG1 . ILE D  2 183 ? 113.763 110.294 167.959 1.00 238.58 ? 217 ILE D CG1 1 
ATOM   6875  C CG2 . ILE D  2 183 ? 111.609 109.845 166.761 1.00 251.38 ? 217 ILE D CG2 1 
ATOM   6876  C CD1 . ILE D  2 183 ? 114.916 111.209 168.102 1.00 226.72 ? 217 ILE D CD1 1 
ATOM   6877  N N   . GLN D  2 184 ? 115.637 110.238 164.232 1.00 222.99 ? 218 GLN D N   1 
ATOM   6878  C CA  . GLN D  2 184 ? 116.964 110.065 163.652 1.00 211.36 ? 218 GLN D CA  1 
ATOM   6879  C C   . GLN D  2 184 ? 117.436 111.377 163.039 1.00 204.84 ? 218 GLN D C   1 
ATOM   6880  O O   . GLN D  2 184 ? 116.699 112.002 162.271 1.00 209.66 ? 218 GLN D O   1 
ATOM   6881  C CB  . GLN D  2 184 ? 116.904 108.933 162.603 1.00 211.42 ? 218 GLN D CB  1 
ATOM   6882  C CG  . GLN D  2 184 ? 117.780 109.003 161.334 1.00 204.85 ? 218 GLN D CG  1 
ATOM   6883  C CD  . GLN D  2 184 ? 119.229 109.386 161.568 1.00 202.02 ? 218 GLN D CD  1 
ATOM   6884  O OE1 . GLN D  2 184 ? 119.747 109.264 162.675 1.00 201.26 ? 218 GLN D OE1 1 
ATOM   6885  N NE2 . GLN D  2 184 ? 119.891 109.857 160.517 1.00 199.10 ? 218 GLN D NE2 1 
ATOM   6886  N N   . ASN D  2 185 ? 118.652 111.790 163.376 1.00 192.30 ? 219 ASN D N   1 
ATOM   6887  C CA  . ASN D  2 185 ? 119.303 112.955 162.798 1.00 181.28 ? 219 ASN D CA  1 
ATOM   6888  C C   . ASN D  2 185 ? 120.645 112.580 162.174 1.00 173.92 ? 219 ASN D C   1 
ATOM   6889  O O   . ASN D  2 185 ? 121.164 111.482 162.397 1.00 177.08 ? 219 ASN D O   1 
ATOM   6890  C CB  . ASN D  2 185 ? 119.498 114.050 163.860 1.00 179.00 ? 219 ASN D CB  1 
ATOM   6891  C CG  . ASN D  2 185 ? 120.410 113.626 165.000 1.00 181.67 ? 219 ASN D CG  1 
ATOM   6892  O OD1 . ASN D  2 185 ? 121.112 112.620 164.924 1.00 184.50 ? 219 ASN D OD1 1 
ATOM   6893  N ND2 . ASN D  2 185 ? 120.429 114.427 166.056 1.00 176.75 ? 219 ASN D ND2 1 
ATOM   6894  N N   . PRO D  2 186 ? 121.244 113.479 161.384 1.00 166.77 ? 220 PRO D N   1 
ATOM   6895  C CA  . PRO D  2 186 ? 122.544 113.171 160.763 1.00 167.04 ? 220 PRO D CA  1 
ATOM   6896  C C   . PRO D  2 186 ? 123.635 112.700 161.721 1.00 165.61 ? 220 PRO D C   1 
ATOM   6897  O O   . PRO D  2 186 ? 124.676 112.236 161.238 1.00 163.77 ? 220 PRO D O   1 
ATOM   6898  C CB  . PRO D  2 186 ? 122.933 114.501 160.111 1.00 155.78 ? 220 PRO D CB  1 
ATOM   6899  C CG  . PRO D  2 186 ? 121.633 115.081 159.710 1.00 152.47 ? 220 PRO D CG  1 
ATOM   6900  C CD  . PRO D  2 186 ? 120.649 114.695 160.794 1.00 159.07 ? 220 PRO D CD  1 
ATOM   6901  N N   . VAL D  2 187 ? 123.457 112.803 163.039 1.00 167.15 ? 221 VAL D N   1 
ATOM   6902  C CA  . VAL D  2 187 ? 124.558 112.489 163.945 1.00 167.88 ? 221 VAL D CA  1 
ATOM   6903  C C   . VAL D  2 187 ? 124.276 111.248 164.790 1.00 173.60 ? 221 VAL D C   1 
ATOM   6904  O O   . VAL D  2 187 ? 125.210 110.537 165.177 1.00 175.34 ? 221 VAL D O   1 
ATOM   6905  C CB  . VAL D  2 187 ? 124.899 113.699 164.840 1.00 157.70 ? 221 VAL D CB  1 
ATOM   6906  C CG1 . VAL D  2 187 ? 123.810 113.952 165.862 1.00 167.20 ? 221 VAL D CG1 1 
ATOM   6907  C CG2 . VAL D  2 187 ? 126.246 113.497 165.519 1.00 145.45 ? 221 VAL D CG2 1 
ATOM   6908  N N   . SER D  2 188 ? 123.006 110.958 165.080 1.00 177.36 ? 222 SER D N   1 
ATOM   6909  C CA  . SER D  2 188 ? 122.720 109.858 165.995 1.00 186.32 ? 222 SER D CA  1 
ATOM   6910  C C   . SER D  2 188 ? 121.295 109.356 165.812 1.00 191.46 ? 222 SER D C   1 
ATOM   6911  O O   . SER D  2 188 ? 120.434 110.046 165.261 1.00 192.93 ? 222 SER D O   1 
ATOM   6912  C CB  . SER D  2 188 ? 122.944 110.277 167.453 1.00 192.76 ? 222 SER D CB  1 
ATOM   6913  O OG  . SER D  2 188 ? 122.323 111.520 167.731 1.00 194.20 ? 222 SER D OG  1 
ATOM   6914  N N   . ALA D  2 189 ? 121.065 108.132 166.293 1.00 199.84 ? 223 ALA D N   1 
ATOM   6915  C CA  . ALA D  2 189 ? 119.745 107.516 166.334 1.00 212.71 ? 223 ALA D CA  1 
ATOM   6916  C C   . ALA D  2 189 ? 119.805 106.257 167.187 1.00 226.48 ? 223 ALA D C   1 
ATOM   6917  O O   . ALA D  2 189 ? 120.737 105.459 167.057 1.00 227.61 ? 223 ALA D O   1 
ATOM   6918  C CB  . ALA D  2 189 ? 119.236 107.167 164.928 1.00 213.14 ? 223 ALA D CB  1 
ATOM   6919  N N   . ASN D  2 190 ? 118.809 106.086 168.050 1.00 234.02 ? 224 ASN D N   1 
ATOM   6920  C CA  . ASN D  2 190 ? 118.630 104.838 168.781 1.00 241.03 ? 224 ASN D CA  1 
ATOM   6921  C C   . ASN D  2 190 ? 117.162 104.696 169.165 1.00 244.63 ? 224 ASN D C   1 
ATOM   6922  O O   . ASN D  2 190 ? 116.404 105.669 169.190 1.00 241.35 ? 224 ASN D O   1 
ATOM   6923  C CB  . ASN D  2 190 ? 119.615 104.727 169.958 1.00 245.27 ? 224 ASN D CB  1 
ATOM   6924  C CG  . ASN D  2 190 ? 119.305 105.661 171.123 1.00 248.16 ? 224 ASN D CG  1 
ATOM   6925  O OD1 . ASN D  2 190 ? 118.203 106.188 171.283 1.00 245.21 ? 224 ASN D OD1 1 
ATOM   6926  N ND2 . ASN D  2 190 ? 120.323 105.851 171.959 1.00 250.70 ? 224 ASN D ND2 1 
ATOM   6927  N N   . ARG D  2 191 ? 116.772 103.460 169.459 1.00 249.62 ? 225 ARG D N   1 
ATOM   6928  C CA  . ARG D  2 191 ? 115.425 102.975 169.196 1.00 255.55 ? 225 ARG D CA  1 
ATOM   6929  C C   . ARG D  2 191 ? 114.526 103.131 170.424 1.00 259.72 ? 225 ARG D C   1 
ATOM   6930  O O   . ARG D  2 191 ? 114.990 103.331 171.548 1.00 257.97 ? 225 ARG D O   1 
ATOM   6931  C CB  . ARG D  2 191 ? 115.486 101.515 168.741 1.00 260.47 ? 225 ARG D CB  1 
ATOM   6932  C CG  . ARG D  2 191 ? 114.317 101.089 167.884 1.00 266.04 ? 225 ARG D CG  1 
ATOM   6933  C CD  . ARG D  2 191 ? 113.781 102.297 167.138 1.00 265.39 ? 225 ARG D CD  1 
ATOM   6934  N NE  . ARG D  2 191 ? 112.591 102.030 166.347 1.00 271.17 ? 225 ARG D NE  1 
ATOM   6935  C CZ  . ARG D  2 191 ? 112.599 101.815 165.041 1.00 272.33 ? 225 ARG D CZ  1 
ATOM   6936  N NH1 . ARG D  2 191 ? 113.731 101.751 164.358 1.00 269.48 ? 225 ARG D NH1 1 
ATOM   6937  N NH2 . ARG D  2 191 ? 111.444 101.656 164.404 1.00 275.98 ? 225 ARG D NH2 1 
ATOM   6938  N N   . SER D  2 192 ? 113.217 103.028 170.187 1.00 264.49 ? 226 SER D N   1 
ATOM   6939  C CA  . SER D  2 192 ? 112.183 103.114 171.207 1.00 270.13 ? 226 SER D CA  1 
ATOM   6940  C C   . SER D  2 192 ? 111.836 101.719 171.724 1.00 275.69 ? 226 SER D C   1 
ATOM   6941  O O   . SER D  2 192 ? 112.513 100.732 171.427 1.00 275.89 ? 226 SER D O   1 
ATOM   6942  C CB  . SER D  2 192 ? 110.942 103.818 170.658 1.00 271.72 ? 226 SER D CB  1 
ATOM   6943  O OG  . SER D  2 192 ? 110.283 103.012 169.696 1.00 276.18 ? 226 SER D OG  1 
ATOM   6944  N N   . ASP D  2 193 ? 110.759 101.652 172.499 1.00 279.29 ? 227 ASP D N   1 
ATOM   6945  C CA  . ASP D  2 193 ? 110.338 100.392 173.096 1.00 283.11 ? 227 ASP D CA  1 
ATOM   6946  C C   . ASP D  2 193 ? 109.256 99.743  172.240 1.00 287.11 ? 227 ASP D C   1 
ATOM   6947  O O   . ASP D  2 193 ? 108.299 100.417 171.845 1.00 288.17 ? 227 ASP D O   1 
ATOM   6948  C CB  . ASP D  2 193 ? 109.820 100.617 174.514 1.00 283.30 ? 227 ASP D CB  1 
ATOM   6949  C CG  . ASP D  2 193 ? 108.986 101.882 174.634 1.00 282.03 ? 227 ASP D CG  1 
ATOM   6950  O OD1 . ASP D  2 193 ? 109.458 102.954 174.199 1.00 278.81 ? 227 ASP D OD1 1 
ATOM   6951  O OD2 . ASP D  2 193 ? 107.856 101.798 175.164 1.00 285.41 ? 227 ASP D OD2 1 
ATOM   6952  N N   . PRO D  2 194 ? 109.376 98.453  171.921 1.00 288.54 ? 228 PRO D N   1 
ATOM   6953  C CA  . PRO D  2 194 ? 108.354 97.793  171.094 1.00 291.09 ? 228 PRO D CA  1 
ATOM   6954  C C   . PRO D  2 194 ? 106.978 97.878  171.741 1.00 293.68 ? 228 PRO D C   1 
ATOM   6955  O O   . PRO D  2 194 ? 106.834 97.705  172.955 1.00 291.84 ? 228 PRO D O   1 
ATOM   6956  C CB  . PRO D  2 194 ? 108.838 96.338  171.011 1.00 290.40 ? 228 PRO D CB  1 
ATOM   6957  C CG  . PRO D  2 194 ? 110.111 96.259  171.815 1.00 288.05 ? 228 PRO D CG  1 
ATOM   6958  C CD  . PRO D  2 194 ? 110.604 97.650  172.029 1.00 286.63 ? 228 PRO D CD  1 
ATOM   6959  N N   . VAL D  2 195 ? 105.964 98.138  170.919 1.00 296.85 ? 229 VAL D N   1 
ATOM   6960  C CA  . VAL D  2 195 ? 104.580 98.205  171.372 1.00 300.41 ? 229 VAL D CA  1 
ATOM   6961  C C   . VAL D  2 195 ? 103.775 97.131  170.654 1.00 304.88 ? 229 VAL D C   1 
ATOM   6962  O O   . VAL D  2 195 ? 103.830 96.998  169.428 1.00 304.46 ? 229 VAL D O   1 
ATOM   6963  C CB  . VAL D  2 195 ? 103.985 99.610  171.137 1.00 298.96 ? 229 VAL D CB  1 
ATOM   6964  C CG1 . VAL D  2 195 ? 102.508 99.629  171.500 1.00 300.61 ? 229 VAL D CG1 1 
ATOM   6965  C CG2 . VAL D  2 195 ? 104.747 100.650 171.940 1.00 293.59 ? 229 VAL D CG2 1 
ATOM   6966  N N   . THR D  2 196 ? 103.017 96.356  171.422 1.00 308.68 ? 230 THR D N   1 
ATOM   6967  C CA  . THR D  2 196 ? 102.258 95.232  170.897 1.00 311.73 ? 230 THR D CA  1 
ATOM   6968  C C   . THR D  2 196 ? 100.815 95.634  170.616 1.00 314.02 ? 230 THR D C   1 
ATOM   6969  O O   . THR D  2 196 ? 100.335 96.678  171.066 1.00 312.72 ? 230 THR D O   1 
ATOM   6970  C CB  . THR D  2 196 ? 102.282 94.050  171.872 1.00 312.69 ? 230 THR D CB  1 
ATOM   6971  O OG1 . THR D  2 196 ? 101.685 92.904  171.254 1.00 314.35 ? 230 THR D OG1 1 
ATOM   6972  C CG2 . THR D  2 196 ? 101.517 94.393  173.143 1.00 312.26 ? 230 THR D CG2 1 
ATOM   6973  N N   . LEU D  2 197 ? 100.129 94.784  169.856 1.00 317.16 ? 231 LEU D N   1 
ATOM   6974  C CA  . LEU D  2 197 ? 98.702  94.916  169.600 1.00 320.56 ? 231 LEU D CA  1 
ATOM   6975  C C   . LEU D  2 197 ? 97.950  93.958  170.512 1.00 324.11 ? 231 LEU D C   1 
ATOM   6976  O O   . LEU D  2 197 ? 98.419  92.844  170.767 1.00 325.10 ? 231 LEU D O   1 
ATOM   6977  C CB  . LEU D  2 197 ? 98.359  94.613  168.140 1.00 321.52 ? 231 LEU D CB  1 
ATOM   6978  C CG  . LEU D  2 197 ? 98.360  95.755  167.123 1.00 318.47 ? 231 LEU D CG  1 
ATOM   6979  C CD1 . LEU D  2 197 ? 98.437  95.192  165.714 1.00 322.02 ? 231 LEU D CD1 1 
ATOM   6980  C CD2 . LEU D  2 197 ? 97.137  96.635  167.284 1.00 321.37 ? 231 LEU D CD2 1 
ATOM   6981  N N   . ASN D  2 198 ? 96.792  94.390  171.001 1.00 326.77 ? 232 ASN D N   1 
ATOM   6982  C CA  . ASN D  2 198 ? 95.964  93.572  171.877 1.00 328.02 ? 232 ASN D CA  1 
ATOM   6983  C C   . ASN D  2 198 ? 94.730  93.114  171.109 1.00 329.22 ? 232 ASN D C   1 
ATOM   6984  O O   . ASN D  2 198 ? 93.875  93.932  170.753 1.00 332.43 ? 232 ASN D O   1 
ATOM   6985  C CB  . ASN D  2 198 ? 95.567  94.348  173.132 1.00 328.33 ? 232 ASN D CB  1 
ATOM   6986  C CG  . ASN D  2 198 ? 94.658  93.552  174.053 1.00 327.75 ? 232 ASN D CG  1 
ATOM   6987  O OD1 . ASN D  2 198 ? 94.659  92.321  174.028 1.00 326.50 ? 232 ASN D OD1 1 
ATOM   6988  N ND2 . ASN D  2 198 ? 93.861  94.251  174.855 1.00 328.58 ? 232 ASN D ND2 1 
ATOM   6989  N N   . VAL D  2 199 ? 94.643  91.808  170.857 1.00 328.19 ? 233 VAL D N   1 
ATOM   6990  C CA  . VAL D  2 199 ? 93.483  91.182  170.234 1.00 326.17 ? 233 VAL D CA  1 
ATOM   6991  C C   . VAL D  2 199 ? 93.205  89.879  170.974 1.00 322.89 ? 233 VAL D C   1 
ATOM   6992  O O   . VAL D  2 199 ? 93.989  89.439  171.817 1.00 321.81 ? 233 VAL D O   1 
ATOM   6993  C CB  . VAL D  2 199 ? 93.690  90.910  168.726 1.00 326.67 ? 233 VAL D CB  1 
ATOM   6994  C CG1 . VAL D  2 199 ? 93.734  92.216  167.943 1.00 328.27 ? 233 VAL D CG1 1 
ATOM   6995  C CG2 . VAL D  2 199 ? 94.954  90.098  168.503 1.00 327.53 ? 233 VAL D CG2 1 
ATOM   6996  N N   . THR D  2 200 ? 92.077  89.254  170.652 1.00 320.78 ? 234 THR D N   1 
ATOM   6997  C CA  . THR D  2 200 ? 91.699  87.999  171.291 1.00 317.14 ? 234 THR D CA  1 
ATOM   6998  C C   . THR D  2 200 ? 90.763  87.186  170.402 1.00 313.41 ? 234 THR D C   1 
ATOM   6999  O O   . THR D  2 200 ? 91.097  86.079  169.981 1.00 310.39 ? 234 THR D O   1 
ATOM   7000  C CB  . THR D  2 200 ? 91.021  88.242  172.653 1.00 314.50 ? 234 THR D CB  1 
ATOM   7001  O OG1 . THR D  2 200 ? 92.005  88.647  173.613 1.00 315.00 ? 234 THR D OG1 1 
ATOM   7002  C CG2 . THR D  2 200 ? 90.337  86.975  173.143 1.00 311.40 ? 234 THR D CG2 1 
ATOM   7003  N N   . GLN E  2 1   ? 139.934 188.739 144.611 1.00 133.20 ? 35  GLN E N   1 
ATOM   7004  C CA  . GLN E  2 1   ? 140.820 189.696 145.266 1.00 136.66 ? 35  GLN E CA  1 
ATOM   7005  C C   . GLN E  2 1   ? 140.439 189.999 146.723 1.00 131.98 ? 35  GLN E C   1 
ATOM   7006  O O   . GLN E  2 1   ? 139.279 190.213 147.060 1.00 131.13 ? 35  GLN E O   1 
ATOM   7007  C CB  . GLN E  2 1   ? 140.912 190.982 144.415 1.00 139.83 ? 35  GLN E CB  1 
ATOM   7008  C CG  . GLN E  2 1   ? 140.037 192.198 144.785 1.00 138.50 ? 35  GLN E CG  1 
ATOM   7009  C CD  . GLN E  2 1   ? 138.532 191.919 144.863 1.00 142.97 ? 35  GLN E CD  1 
ATOM   7010  O OE1 . GLN E  2 1   ? 138.078 190.776 144.796 1.00 142.78 ? 35  GLN E OE1 1 
ATOM   7011  N NE2 . GLN E  2 1   ? 137.754 192.985 145.004 1.00 143.20 ? 35  GLN E NE2 1 
ATOM   7012  N N   . LEU E  2 2   ? 141.443 189.967 147.596 1.00 124.80 ? 36  LEU E N   1 
ATOM   7013  C CA  . LEU E  2 2   ? 141.197 190.163 149.017 1.00 117.05 ? 36  LEU E CA  1 
ATOM   7014  C C   . LEU E  2 2   ? 141.344 191.633 149.386 1.00 121.08 ? 36  LEU E C   1 
ATOM   7015  O O   . LEU E  2 2   ? 142.403 192.237 149.197 1.00 128.75 ? 36  LEU E O   1 
ATOM   7016  C CB  . LEU E  2 2   ? 142.162 189.310 149.840 1.00 109.80 ? 36  LEU E CB  1 
ATOM   7017  C CG  . LEU E  2 2   ? 141.773 189.027 151.290 1.00 101.22 ? 36  LEU E CG  1 
ATOM   7018  C CD1 . LEU E  2 2   ? 140.669 187.988 151.348 1.00 111.44 ? 36  LEU E CD1 1 
ATOM   7019  C CD2 . LEU E  2 2   ? 142.985 188.561 152.068 1.00 98.56  ? 36  LEU E CD2 1 
ATOM   7020  N N   . THR E  2 3   ? 140.268 192.209 149.917 1.00 115.36 ? 37  THR E N   1 
ATOM   7021  C CA  . THR E  2 3   ? 140.254 193.608 150.314 1.00 114.88 ? 37  THR E CA  1 
ATOM   7022  C C   . THR E  2 3   ? 139.768 193.723 151.750 1.00 115.09 ? 37  THR E C   1 
ATOM   7023  O O   . THR E  2 3   ? 138.881 192.984 152.184 1.00 116.74 ? 37  THR E O   1 
ATOM   7024  C CB  . THR E  2 3   ? 139.358 194.454 149.399 1.00 119.80 ? 37  THR E CB  1 
ATOM   7025  O OG1 . THR E  2 3   ? 138.014 193.958 149.453 1.00 125.40 ? 37  THR E OG1 1 
ATOM   7026  C CG2 . THR E  2 3   ? 139.857 194.403 147.963 1.00 123.08 ? 37  THR E CG2 1 
ATOM   7027  N N   . THR E  2 4   ? 140.362 194.661 152.483 1.00 114.99 ? 38  THR E N   1 
ATOM   7028  C CA  . THR E  2 4   ? 139.970 194.959 153.852 1.00 113.75 ? 38  THR E CA  1 
ATOM   7029  C C   . THR E  2 4   ? 139.498 196.401 153.928 1.00 115.48 ? 38  THR E C   1 
ATOM   7030  O O   . THR E  2 4   ? 139.988 197.263 153.192 1.00 118.14 ? 38  THR E O   1 
ATOM   7031  C CB  . THR E  2 4   ? 141.123 194.738 154.838 1.00 107.92 ? 38  THR E CB  1 
ATOM   7032  O OG1 . THR E  2 4   ? 141.998 195.871 154.813 1.00 109.86 ? 38  THR E OG1 1 
ATOM   7033  C CG2 . THR E  2 4   ? 141.907 193.490 154.473 1.00 109.15 ? 38  THR E CG2 1 
ATOM   7034  N N   . GLU E  2 5   ? 138.546 196.659 154.819 1.00 114.25 ? 39  GLU E N   1 
ATOM   7035  C CA  . GLU E  2 5   ? 137.939 197.975 154.951 1.00 118.42 ? 39  GLU E CA  1 
ATOM   7036  C C   . GLU E  2 5   ? 137.782 198.313 156.424 1.00 120.92 ? 39  GLU E C   1 
ATOM   7037  O O   . GLU E  2 5   ? 137.115 197.583 157.164 1.00 125.41 ? 39  GLU E O   1 
ATOM   7038  C CB  . GLU E  2 5   ? 136.580 198.023 154.249 1.00 124.60 ? 39  GLU E CB  1 
ATOM   7039  C CG  . GLU E  2 5   ? 135.856 199.349 154.380 1.00 133.86 ? 39  GLU E CG  1 
ATOM   7040  C CD  . GLU E  2 5   ? 134.595 199.402 153.544 1.00 153.47 ? 39  GLU E CD  1 
ATOM   7041  O OE1 . GLU E  2 5   ? 133.860 198.393 153.514 1.00 154.71 ? 39  GLU E OE1 1 
ATOM   7042  O OE2 . GLU E  2 5   ? 134.338 200.450 152.915 1.00 165.33 ? 39  GLU E OE2 1 
ATOM   7043  N N   . SER E  2 6   ? 138.395 199.415 156.845 1.00 117.42 ? 40  SER E N   1 
ATOM   7044  C CA  . SER E  2 6   ? 138.273 199.910 158.209 1.00 114.01 ? 40  SER E CA  1 
ATOM   7045  C C   . SER E  2 6   ? 136.875 200.485 158.394 1.00 119.71 ? 40  SER E C   1 
ATOM   7046  O O   . SER E  2 6   ? 136.290 201.021 157.446 1.00 124.55 ? 40  SER E O   1 
ATOM   7047  C CB  . SER E  2 6   ? 139.337 200.966 158.505 1.00 113.16 ? 40  SER E CB  1 
ATOM   7048  O OG  . SER E  2 6   ? 139.158 202.107 157.686 1.00 122.40 ? 40  SER E OG  1 
ATOM   7049  N N   . MET E  2 7   ? 136.345 200.375 159.605 1.00 116.00 ? 41  MET E N   1 
ATOM   7050  C CA  . MET E  2 7   ? 134.991 200.838 159.906 1.00 116.63 ? 41  MET E CA  1 
ATOM   7051  C C   . MET E  2 7   ? 134.928 201.369 161.330 1.00 112.12 ? 41  MET E C   1 
ATOM   7052  O O   . MET E  2 7   ? 134.862 200.568 162.282 1.00 108.95 ? 41  MET E O   1 
ATOM   7053  C CB  . MET E  2 7   ? 133.982 199.706 159.715 1.00 119.67 ? 41  MET E CB  1 
ATOM   7054  C CG  . MET E  2 7   ? 132.577 200.174 159.381 1.00 124.43 ? 41  MET E CG  1 
ATOM   7055  S SD  . MET E  2 7   ? 132.462 200.896 157.734 1.00 149.33 ? 41  MET E SD  1 
ATOM   7056  C CE  . MET E  2 7   ? 131.981 202.574 158.132 1.00 130.60 ? 41  MET E CE  1 
ATOM   7057  N N   . PRO E  2 8   ? 134.945 202.690 161.538 1.00 109.62 ? 42  PRO E N   1 
ATOM   7058  C CA  . PRO E  2 8   ? 135.083 203.754 160.538 1.00 111.97 ? 42  PRO E CA  1 
ATOM   7059  C C   . PRO E  2 8   ? 136.541 204.012 160.174 1.00 115.86 ? 42  PRO E C   1 
ATOM   7060  O O   . PRO E  2 8   ? 137.447 203.505 160.828 1.00 117.68 ? 42  PRO E O   1 
ATOM   7061  C CB  . PRO E  2 8   ? 134.437 204.954 161.235 1.00 108.80 ? 42  PRO E CB  1 
ATOM   7062  C CG  . PRO E  2 8   ? 134.719 204.733 162.698 1.00 105.33 ? 42  PRO E CG  1 
ATOM   7063  C CD  . PRO E  2 8   ? 134.840 203.235 162.903 1.00 105.55 ? 42  PRO E CD  1 
ATOM   7064  N N   . PHE E  2 9   ? 136.793 204.795 159.122 1.00 118.37 ? 43  PHE E N   1 
ATOM   7065  C CA  . PHE E  2 9   ? 138.169 205.096 158.738 1.00 116.49 ? 43  PHE E CA  1 
ATOM   7066  C C   . PHE E  2 9   ? 138.859 205.963 159.783 1.00 116.65 ? 43  PHE E C   1 
ATOM   7067  O O   . PHE E  2 9   ? 140.041 205.761 160.086 1.00 113.23 ? 43  PHE E O   1 
ATOM   7068  C CB  . PHE E  2 9   ? 138.194 205.778 157.371 1.00 116.41 ? 43  PHE E CB  1 
ATOM   7069  C CG  . PHE E  2 9   ? 139.566 205.877 156.768 1.00 119.60 ? 43  PHE E CG  1 
ATOM   7070  C CD1 . PHE E  2 9   ? 140.379 206.965 157.035 1.00 120.13 ? 43  PHE E CD1 1 
ATOM   7071  C CD2 . PHE E  2 9   ? 140.044 204.878 155.938 1.00 123.39 ? 43  PHE E CD2 1 
ATOM   7072  C CE1 . PHE E  2 9   ? 141.642 207.057 156.484 1.00 122.84 ? 43  PHE E CE1 1 
ATOM   7073  C CE2 . PHE E  2 9   ? 141.306 204.964 155.384 1.00 124.43 ? 43  PHE E CE2 1 
ATOM   7074  C CZ  . PHE E  2 9   ? 142.106 206.054 155.657 1.00 124.79 ? 43  PHE E CZ  1 
ATOM   7075  N N   . ASN E  2 10  ? 138.143 206.933 160.341 1.00 119.36 ? 44  ASN E N   1 
ATOM   7076  C CA  . ASN E  2 10  ? 138.673 207.811 161.373 1.00 117.48 ? 44  ASN E CA  1 
ATOM   7077  C C   . ASN E  2 10  ? 137.969 207.526 162.692 1.00 119.33 ? 44  ASN E C   1 
ATOM   7078  O O   . ASN E  2 10  ? 136.737 207.574 162.772 1.00 125.97 ? 44  ASN E O   1 
ATOM   7079  C CB  . ASN E  2 10  ? 138.498 209.281 160.989 1.00 119.69 ? 44  ASN E CB  1 
ATOM   7080  C CG  . ASN E  2 10  ? 139.076 209.598 159.626 1.00 123.65 ? 44  ASN E CG  1 
ATOM   7081  O OD1 . ASN E  2 10  ? 140.293 209.635 159.449 1.00 126.66 ? 44  ASN E OD1 1 
ATOM   7082  N ND2 . ASN E  2 10  ? 138.204 209.827 158.653 1.00 124.14 ? 44  ASN E ND2 1 
ATOM   7083  N N   . VAL E  2 11  ? 138.754 207.231 163.723 1.00 114.19 ? 45  VAL E N   1 
ATOM   7084  C CA  . VAL E  2 11  ? 138.226 206.821 165.018 1.00 112.99 ? 45  VAL E CA  1 
ATOM   7085  C C   . VAL E  2 11  ? 138.677 207.813 166.077 1.00 123.19 ? 45  VAL E C   1 
ATOM   7086  O O   . VAL E  2 11  ? 139.847 208.207 166.119 1.00 131.84 ? 45  VAL E O   1 
ATOM   7087  C CB  . VAL E  2 11  ? 138.676 205.393 165.391 1.00 110.18 ? 45  VAL E CB  1 
ATOM   7088  C CG1 . VAL E  2 11  ? 137.792 204.368 164.714 1.00 117.81 ? 45  VAL E CG1 1 
ATOM   7089  C CG2 . VAL E  2 11  ? 140.130 205.179 165.008 1.00 111.54 ? 45  VAL E CG2 1 
ATOM   7090  N N   . ALA E  2 12  ? 137.741 208.225 166.925 1.00 128.37 ? 46  ALA E N   1 
ATOM   7091  C CA  . ALA E  2 12  ? 138.077 209.024 168.091 1.00 145.16 ? 46  ALA E CA  1 
ATOM   7092  C C   . ALA E  2 12  ? 138.893 208.194 169.074 1.00 149.35 ? 46  ALA E C   1 
ATOM   7093  O O   . ALA E  2 12  ? 138.737 206.973 169.167 1.00 149.79 ? 46  ALA E O   1 
ATOM   7094  C CB  . ALA E  2 12  ? 136.810 209.545 168.768 1.00 149.05 ? 46  ALA E CB  1 
ATOM   7095  N N   . GLU E  2 13  ? 139.781 208.867 169.803 1.00 145.30 ? 47  GLU E N   1 
ATOM   7096  C CA  . GLU E  2 13  ? 140.619 208.175 170.773 1.00 137.29 ? 47  GLU E CA  1 
ATOM   7097  C C   . GLU E  2 13  ? 139.765 207.515 171.848 1.00 142.60 ? 47  GLU E C   1 
ATOM   7098  O O   . GLU E  2 13  ? 138.794 208.096 172.340 1.00 148.75 ? 47  GLU E O   1 
ATOM   7099  C CB  . GLU E  2 13  ? 141.610 209.147 171.413 1.00 144.57 ? 47  GLU E CB  1 
ATOM   7100  C CG  . GLU E  2 13  ? 143.028 209.017 170.884 1.00 150.44 ? 47  GLU E CG  1 
ATOM   7101  C CD  . GLU E  2 13  ? 144.051 209.669 171.793 1.00 157.54 ? 47  GLU E CD  1 
ATOM   7102  O OE1 . GLU E  2 13  ? 144.202 210.907 171.729 1.00 160.23 ? 47  GLU E OE1 1 
ATOM   7103  O OE2 . GLU E  2 13  ? 144.702 208.943 172.572 1.00 155.70 ? 47  GLU E OE2 1 
ATOM   7104  N N   . GLY E  2 14  ? 140.135 206.289 172.211 1.00 139.12 ? 48  GLY E N   1 
ATOM   7105  C CA  . GLY E  2 14  ? 139.424 205.526 173.210 1.00 139.07 ? 48  GLY E CA  1 
ATOM   7106  C C   . GLY E  2 14  ? 138.233 204.746 172.693 1.00 135.54 ? 48  GLY E C   1 
ATOM   7107  O O   . GLY E  2 14  ? 137.619 204.001 173.464 1.00 138.65 ? 48  GLY E O   1 
ATOM   7108  N N   . LYS E  2 15  ? 137.891 204.892 171.418 1.00 132.58 ? 49  LYS E N   1 
ATOM   7109  C CA  . LYS E  2 15  ? 136.797 204.143 170.820 1.00 132.09 ? 49  LYS E CA  1 
ATOM   7110  C C   . LYS E  2 15  ? 137.343 202.853 170.211 1.00 133.15 ? 49  LYS E C   1 
ATOM   7111  O O   . LYS E  2 15  ? 138.496 202.474 170.436 1.00 134.71 ? 49  LYS E O   1 
ATOM   7112  C CB  . LYS E  2 15  ? 136.066 205.003 169.792 1.00 131.34 ? 49  LYS E CB  1 
ATOM   7113  C CG  . LYS E  2 15  ? 135.213 206.112 170.395 1.00 135.22 ? 49  LYS E CG  1 
ATOM   7114  C CD  . LYS E  2 15  ? 134.691 205.735 171.775 1.00 136.42 ? 49  LYS E CD  1 
ATOM   7115  C CE  . LYS E  2 15  ? 133.490 206.580 172.161 1.00 145.03 ? 49  LYS E CE  1 
ATOM   7116  N NZ  . LYS E  2 15  ? 133.506 207.904 171.482 1.00 147.52 ? 49  LYS E NZ  1 
ATOM   7117  N N   . GLU E  2 16  ? 136.518 202.160 169.432 1.00 127.95 ? 50  GLU E N   1 
ATOM   7118  C CA  . GLU E  2 16  ? 136.915 200.914 168.799 1.00 123.77 ? 50  GLU E CA  1 
ATOM   7119  C C   . GLU E  2 16  ? 136.809 201.034 167.286 1.00 118.90 ? 50  GLU E C   1 
ATOM   7120  O O   . GLU E  2 16  ? 136.054 201.857 166.760 1.00 120.67 ? 50  GLU E O   1 
ATOM   7121  C CB  . GLU E  2 16  ? 136.059 199.736 169.281 1.00 125.58 ? 50  GLU E CB  1 
ATOM   7122  C CG  . GLU E  2 16  ? 134.633 199.745 168.759 1.00 131.98 ? 50  GLU E CG  1 
ATOM   7123  C CD  . GLU E  2 16  ? 133.690 198.942 169.631 1.00 140.34 ? 50  GLU E CD  1 
ATOM   7124  O OE1 . GLU E  2 16  ? 134.174 198.074 170.388 1.00 142.29 ? 50  GLU E OE1 1 
ATOM   7125  O OE2 . GLU E  2 16  ? 132.466 199.175 169.557 1.00 144.11 ? 50  GLU E OE2 1 
ATOM   7126  N N   . VAL E  2 17  ? 137.581 200.203 166.591 1.00 114.50 ? 51  VAL E N   1 
ATOM   7127  C CA  . VAL E  2 17  ? 137.578 200.143 165.136 1.00 111.79 ? 51  VAL E CA  1 
ATOM   7128  C C   . VAL E  2 17  ? 137.481 198.682 164.719 1.00 110.14 ? 51  VAL E C   1 
ATOM   7129  O O   . VAL E  2 17  ? 138.080 197.804 165.351 1.00 111.54 ? 51  VAL E O   1 
ATOM   7130  C CB  . VAL E  2 17  ? 138.831 200.816 164.533 1.00 112.18 ? 51  VAL E CB  1 
ATOM   7131  C CG1 . VAL E  2 17  ? 140.102 200.131 165.014 1.00 113.73 ? 51  VAL E CG1 1 
ATOM   7132  C CG2 . VAL E  2 17  ? 138.762 200.822 163.014 1.00 114.50 ? 51  VAL E CG2 1 
ATOM   7133  N N   . LEU E  2 18  ? 136.707 198.419 163.672 1.00 107.06 ? 52  LEU E N   1 
ATOM   7134  C CA  . LEU E  2 18  ? 136.493 197.070 163.169 1.00 107.71 ? 52  LEU E CA  1 
ATOM   7135  C C   . LEU E  2 18  ? 136.927 196.998 161.712 1.00 112.24 ? 52  LEU E C   1 
ATOM   7136  O O   . LEU E  2 18  ? 136.457 197.783 160.881 1.00 114.81 ? 52  LEU E O   1 
ATOM   7137  C CB  . LEU E  2 18  ? 135.025 196.663 163.308 1.00 111.09 ? 52  LEU E CB  1 
ATOM   7138  C CG  . LEU E  2 18  ? 134.633 195.297 162.743 1.00 113.91 ? 52  LEU E CG  1 
ATOM   7139  C CD1 . LEU E  2 18  ? 135.339 194.184 163.497 1.00 111.09 ? 52  LEU E CD1 1 
ATOM   7140  C CD2 . LEU E  2 18  ? 133.126 195.111 162.799 1.00 117.45 ? 52  LEU E CD2 1 
ATOM   7141  N N   . LEU E  2 19  ? 137.818 196.059 161.408 1.00 108.69 ? 53  LEU E N   1 
ATOM   7142  C CA  . LEU E  2 19  ? 138.315 195.855 160.054 1.00 110.29 ? 53  LEU E CA  1 
ATOM   7143  C C   . LEU E  2 19  ? 137.543 194.711 159.410 1.00 114.78 ? 53  LEU E C   1 
ATOM   7144  O O   . LEU E  2 19  ? 137.625 193.566 159.868 1.00 111.06 ? 53  LEU E O   1 
ATOM   7145  C CB  . LEU E  2 19  ? 139.813 195.555 160.060 1.00 100.85 ? 53  LEU E CB  1 
ATOM   7146  C CG  . LEU E  2 19  ? 140.716 196.516 160.834 1.00 91.74  ? 53  LEU E CG  1 
ATOM   7147  C CD1 . LEU E  2 19  ? 142.165 196.080 160.735 1.00 88.80  ? 53  LEU E CD1 1 
ATOM   7148  C CD2 . LEU E  2 19  ? 140.553 197.934 160.320 1.00 99.10  ? 53  LEU E CD2 1 
ATOM   7149  N N   . LEU E  2 20  ? 136.801 195.020 158.353 1.00 116.14 ? 54  LEU E N   1 
ATOM   7150  C CA  . LEU E  2 20  ? 136.035 194.031 157.613 1.00 108.85 ? 54  LEU E CA  1 
ATOM   7151  C C   . LEU E  2 20  ? 136.899 193.391 156.533 1.00 110.50 ? 54  LEU E C   1 
ATOM   7152  O O   . LEU E  2 20  ? 137.878 193.972 156.061 1.00 114.54 ? 54  LEU E O   1 
ATOM   7153  C CB  . LEU E  2 20  ? 134.794 194.667 156.982 1.00 110.66 ? 54  LEU E CB  1 
ATOM   7154  C CG  . LEU E  2 20  ? 133.841 195.391 157.934 1.00 114.06 ? 54  LEU E CG  1 
ATOM   7155  C CD1 . LEU E  2 20  ? 132.606 195.875 157.193 1.00 122.14 ? 54  LEU E CD1 1 
ATOM   7156  C CD2 . LEU E  2 20  ? 133.455 194.485 159.090 1.00 117.42 ? 54  LEU E CD2 1 
ATOM   7157  N N   . VAL E  2 21  ? 136.522 192.175 156.149 1.00 107.84 ? 55  VAL E N   1 
ATOM   7158  C CA  . VAL E  2 21  ? 137.204 191.430 155.099 1.00 108.53 ? 55  VAL E CA  1 
ATOM   7159  C C   . VAL E  2 21  ? 136.172 191.002 154.067 1.00 114.52 ? 55  VAL E C   1 
ATOM   7160  O O   . VAL E  2 21  ? 135.103 190.490 154.420 1.00 118.96 ? 55  VAL E O   1 
ATOM   7161  C CB  . VAL E  2 21  ? 137.956 190.205 155.659 1.00 101.63 ? 55  VAL E CB  1 
ATOM   7162  C CG1 . VAL E  2 21  ? 138.695 189.479 154.548 1.00 105.42 ? 55  VAL E CG1 1 
ATOM   7163  C CG2 . VAL E  2 21  ? 138.921 190.632 156.748 1.00 100.90 ? 55  VAL E CG2 1 
ATOM   7164  N N   . HIS E  2 22  ? 136.491 191.212 152.793 1.00 115.36 ? 56  HIS E N   1 
ATOM   7165  C CA  . HIS E  2 22  ? 135.593 190.884 151.697 1.00 116.48 ? 56  HIS E CA  1 
ATOM   7166  C C   . HIS E  2 22  ? 136.271 189.904 150.752 1.00 121.04 ? 56  HIS E C   1 
ATOM   7167  O O   . HIS E  2 22  ? 137.502 189.835 150.682 1.00 122.58 ? 56  HIS E O   1 
ATOM   7168  C CB  . HIS E  2 22  ? 135.170 192.138 150.920 1.00 116.72 ? 56  HIS E CB  1 
ATOM   7169  C CG  . HIS E  2 22  ? 134.333 193.090 151.716 1.00 116.84 ? 56  HIS E CG  1 
ATOM   7170  N ND1 . HIS E  2 22  ? 132.985 192.898 151.927 1.00 119.31 ? 56  HIS E ND1 1 
ATOM   7171  C CD2 . HIS E  2 22  ? 134.653 194.243 152.349 1.00 118.59 ? 56  HIS E CD2 1 
ATOM   7172  C CE1 . HIS E  2 22  ? 132.510 193.891 152.657 1.00 124.25 ? 56  HIS E CE1 1 
ATOM   7173  N NE2 . HIS E  2 22  ? 133.502 194.721 152.927 1.00 125.50 ? 56  HIS E NE2 1 
ATOM   7174  N N   . ASN E  2 23  ? 135.447 189.144 150.028 1.00 119.94 ? 57  ASN E N   1 
ATOM   7175  C CA  . ASN E  2 23  ? 135.918 188.199 149.013 1.00 122.05 ? 57  ASN E CA  1 
ATOM   7176  C C   . ASN E  2 23  ? 136.895 187.186 149.604 1.00 118.04 ? 57  ASN E C   1 
ATOM   7177  O O   . ASN E  2 23  ? 137.901 186.829 148.986 1.00 116.20 ? 57  ASN E O   1 
ATOM   7178  C CB  . ASN E  2 23  ? 136.548 188.935 147.831 1.00 126.55 ? 57  ASN E CB  1 
ATOM   7179  C CG  . ASN E  2 23  ? 135.711 190.105 147.363 1.00 130.93 ? 57  ASN E CG  1 
ATOM   7180  O OD1 . ASN E  2 23  ? 136.237 191.164 147.023 1.00 131.32 ? 57  ASN E OD1 1 
ATOM   7181  N ND2 . ASN E  2 23  ? 134.397 189.916 147.328 1.00 131.48 ? 57  ASN E ND2 1 
ATOM   7182  N N   . LEU E  2 24  ? 136.599 186.724 150.810 1.00 115.22 ? 58  LEU E N   1 
ATOM   7183  C CA  . LEU E  2 24  ? 137.452 185.743 151.465 1.00 115.05 ? 58  LEU E CA  1 
ATOM   7184  C C   . LEU E  2 24  ? 137.404 184.426 150.697 1.00 123.56 ? 58  LEU E C   1 
ATOM   7185  O O   . LEU E  2 24  ? 136.315 183.971 150.329 1.00 131.49 ? 58  LEU E O   1 
ATOM   7186  C CB  . LEU E  2 24  ? 137.002 185.545 152.910 1.00 110.13 ? 58  LEU E CB  1 
ATOM   7187  C CG  . LEU E  2 24  ? 137.969 184.883 153.889 1.00 113.75 ? 58  LEU E CG  1 
ATOM   7188  C CD1 . LEU E  2 24  ? 139.181 185.766 154.115 1.00 113.43 ? 58  LEU E CD1 1 
ATOM   7189  C CD2 . LEU E  2 24  ? 137.263 184.608 155.205 1.00 117.89 ? 58  LEU E CD2 1 
ATOM   7190  N N   . PRO E  2 25  ? 138.554 183.798 150.416 1.00 121.34 ? 59  PRO E N   1 
ATOM   7191  C CA  . PRO E  2 25  ? 138.552 182.538 149.656 1.00 120.90 ? 59  PRO E CA  1 
ATOM   7192  C C   . PRO E  2 25  ? 137.697 181.455 150.297 1.00 128.01 ? 59  PRO E C   1 
ATOM   7193  O O   . PRO E  2 25  ? 137.479 181.460 151.512 1.00 126.32 ? 59  PRO E O   1 
ATOM   7194  C CB  . PRO E  2 25  ? 140.031 182.140 149.640 1.00 119.16 ? 59  PRO E CB  1 
ATOM   7195  C CG  . PRO E  2 25  ? 140.769 183.427 149.739 1.00 116.56 ? 59  PRO E CG  1 
ATOM   7196  C CD  . PRO E  2 25  ? 139.902 184.384 150.519 1.00 120.40 ? 59  PRO E CD  1 
ATOM   7197  N N   . GLN E  2 26  ? 137.195 180.527 149.478 1.00 131.50 ? 60  GLN E N   1 
ATOM   7198  C CA  . GLN E  2 26  ? 136.275 179.512 149.983 1.00 136.54 ? 60  GLN E CA  1 
ATOM   7199  C C   . GLN E  2 26  ? 136.974 178.530 150.916 1.00 135.78 ? 60  GLN E C   1 
ATOM   7200  O O   . GLN E  2 26  ? 136.480 178.255 152.016 1.00 132.88 ? 60  GLN E O   1 
ATOM   7201  C CB  . GLN E  2 26  ? 135.627 178.770 148.814 1.00 136.54 ? 60  GLN E CB  1 
ATOM   7202  C CG  . GLN E  2 26  ? 134.839 179.663 147.868 1.00 143.31 ? 60  GLN E CG  1 
ATOM   7203  C CD  . GLN E  2 26  ? 133.659 180.339 148.540 1.00 149.62 ? 60  GLN E CD  1 
ATOM   7204  O OE1 . GLN E  2 26  ? 133.152 179.867 149.558 1.00 149.58 ? 60  GLN E OE1 1 
ATOM   7205  N NE2 . GLN E  2 26  ? 133.216 181.455 147.972 1.00 153.40 ? 60  GLN E NE2 1 
ATOM   7206  N N   . GLN E  2 27  ? 138.118 177.996 150.502 1.00 134.59 ? 61  GLN E N   1 
ATOM   7207  C CA  . GLN E  2 27  ? 138.847 176.997 151.272 1.00 128.34 ? 61  GLN E CA  1 
ATOM   7208  C C   . GLN E  2 27  ? 140.007 177.668 151.993 1.00 123.67 ? 61  GLN E C   1 
ATOM   7209  O O   . GLN E  2 27  ? 140.912 178.209 151.350 1.00 129.40 ? 61  GLN E O   1 
ATOM   7210  C CB  . GLN E  2 27  ? 139.358 175.877 150.364 1.00 133.02 ? 61  GLN E CB  1 
ATOM   7211  C CG  . GLN E  2 27  ? 138.265 175.170 149.578 1.00 138.81 ? 61  GLN E CG  1 
ATOM   7212  C CD  . GLN E  2 27  ? 137.402 174.277 150.447 1.00 146.00 ? 61  GLN E CD  1 
ATOM   7213  O OE1 . GLN E  2 27  ? 137.697 173.096 150.630 1.00 150.24 ? 61  GLN E OE1 1 
ATOM   7214  N NE2 . GLN E  2 27  ? 136.325 174.837 150.985 1.00 144.74 ? 61  GLN E NE2 1 
ATOM   7215  N N   . LEU E  2 28  ? 139.981 177.626 153.323 1.00 113.06 ? 62  LEU E N   1 
ATOM   7216  C CA  . LEU E  2 28  ? 140.941 178.354 154.137 1.00 109.54 ? 62  LEU E CA  1 
ATOM   7217  C C   . LEU E  2 28  ? 141.565 177.437 155.177 1.00 107.78 ? 62  LEU E C   1 
ATOM   7218  O O   . LEU E  2 28  ? 140.972 176.443 155.603 1.00 108.23 ? 62  LEU E O   1 
ATOM   7219  C CB  . LEU E  2 28  ? 140.286 179.549 154.838 1.00 112.39 ? 62  LEU E CB  1 
ATOM   7220  C CG  . LEU E  2 28  ? 139.395 180.433 153.970 1.00 116.11 ? 62  LEU E CG  1 
ATOM   7221  C CD1 . LEU E  2 28  ? 138.386 181.177 154.826 1.00 122.69 ? 62  LEU E CD1 1 
ATOM   7222  C CD2 . LEU E  2 28  ? 140.243 181.399 153.172 1.00 112.43 ? 62  LEU E CD2 1 
ATOM   7223  N N   . PHE E  2 29  ? 142.779 177.796 155.584 1.00 106.97 ? 63  PHE E N   1 
ATOM   7224  C CA  . PHE E  2 29  ? 143.486 177.126 156.664 1.00 104.49 ? 63  PHE E CA  1 
ATOM   7225  C C   . PHE E  2 29  ? 143.634 177.979 157.913 1.00 104.99 ? 63  PHE E C   1 
ATOM   7226  O O   . PHE E  2 29  ? 143.717 177.427 159.011 1.00 109.36 ? 63  PHE E O   1 
ATOM   7227  C CB  . PHE E  2 29  ? 144.883 176.687 156.196 1.00 107.17 ? 63  PHE E CB  1 
ATOM   7228  C CG  . PHE E  2 29  ? 145.612 175.827 157.187 1.00 106.09 ? 63  PHE E CG  1 
ATOM   7229  C CD1 . PHE E  2 29  ? 145.316 174.481 157.308 1.00 106.83 ? 63  PHE E CD1 1 
ATOM   7230  C CD2 . PHE E  2 29  ? 146.594 176.368 157.999 1.00 106.23 ? 63  PHE E CD2 1 
ATOM   7231  C CE1 . PHE E  2 29  ? 145.987 173.691 158.220 1.00 107.27 ? 63  PHE E CE1 1 
ATOM   7232  C CE2 . PHE E  2 29  ? 147.266 175.583 158.912 1.00 106.84 ? 63  PHE E CE2 1 
ATOM   7233  C CZ  . PHE E  2 29  ? 146.963 174.243 159.023 1.00 107.94 ? 63  PHE E CZ  1 
ATOM   7234  N N   . GLY E  2 30  ? 143.665 179.299 157.779 1.00 100.79 ? 64  GLY E N   1 
ATOM   7235  C CA  . GLY E  2 30  ? 143.790 180.167 158.935 1.00 101.32 ? 64  GLY E CA  1 
ATOM   7236  C C   . GLY E  2 30  ? 144.108 181.580 158.501 1.00 97.63  ? 64  GLY E C   1 
ATOM   7237  O O   . GLY E  2 30  ? 144.441 181.841 157.340 1.00 97.26  ? 64  GLY E O   1 
ATOM   7238  N N   . TYR E  2 31  ? 143.999 182.495 159.461 1.00 97.53  ? 65  TYR E N   1 
ATOM   7239  C CA  . TYR E  2 31  ? 144.260 183.908 159.238 1.00 95.84  ? 65  TYR E CA  1 
ATOM   7240  C C   . TYR E  2 31  ? 145.362 184.387 160.172 1.00 97.24  ? 65  TYR E C   1 
ATOM   7241  O O   . TYR E  2 31  ? 145.783 183.677 161.089 1.00 103.67 ? 65  TYR E O   1 
ATOM   7242  C CB  . TYR E  2 31  ? 143.007 184.770 159.464 1.00 97.12  ? 65  TYR E CB  1 
ATOM   7243  C CG  . TYR E  2 31  ? 141.687 184.092 159.176 1.00 98.14  ? 65  TYR E CG  1 
ATOM   7244  C CD1 . TYR E  2 31  ? 141.466 183.427 157.978 1.00 102.74 ? 65  TYR E CD1 1 
ATOM   7245  C CD2 . TYR E  2 31  ? 140.662 184.116 160.111 1.00 99.38  ? 65  TYR E CD2 1 
ATOM   7246  C CE1 . TYR E  2 31  ? 140.261 182.809 157.719 1.00 108.95 ? 65  TYR E CE1 1 
ATOM   7247  C CE2 . TYR E  2 31  ? 139.455 183.500 159.861 1.00 109.67 ? 65  TYR E CE2 1 
ATOM   7248  C CZ  . TYR E  2 31  ? 139.259 182.847 158.664 1.00 115.85 ? 65  TYR E CZ  1 
ATOM   7249  O OH  . TYR E  2 31  ? 138.055 182.232 158.412 1.00 120.27 ? 65  TYR E OH  1 
ATOM   7250  N N   . SER E  2 32  ? 145.821 185.612 159.926 1.00 91.46  ? 66  SER E N   1 
ATOM   7251  C CA  . SER E  2 32  ? 146.791 186.264 160.796 1.00 91.86  ? 66  SER E CA  1 
ATOM   7252  C C   . SER E  2 32  ? 146.807 187.748 160.472 1.00 91.46  ? 66  SER E C   1 
ATOM   7253  O O   . SER E  2 32  ? 146.809 188.126 159.297 1.00 96.54  ? 66  SER E O   1 
ATOM   7254  C CB  . SER E  2 32  ? 148.189 185.662 160.623 1.00 95.86  ? 66  SER E CB  1 
ATOM   7255  O OG  . SER E  2 32  ? 148.348 184.514 161.436 1.00 99.33  ? 66  SER E OG  1 
ATOM   7256  N N   . TRP E  2 33  ? 146.823 188.580 161.508 1.00 88.45  ? 67  TRP E N   1 
ATOM   7257  C CA  . TRP E  2 33  ? 146.861 190.027 161.358 1.00 87.51  ? 67  TRP E CA  1 
ATOM   7258  C C   . TRP E  2 33  ? 148.199 190.546 161.862 1.00 96.45  ? 67  TRP E C   1 
ATOM   7259  O O   . TRP E  2 33  ? 148.613 190.221 162.980 1.00 102.41 ? 67  TRP E O   1 
ATOM   7260  C CB  . TRP E  2 33  ? 145.712 190.691 162.118 1.00 84.16  ? 67  TRP E CB  1 
ATOM   7261  C CG  . TRP E  2 33  ? 144.415 190.689 161.371 1.00 81.49  ? 67  TRP E CG  1 
ATOM   7262  C CD1 . TRP E  2 33  ? 143.406 189.781 161.485 1.00 86.95  ? 67  TRP E CD1 1 
ATOM   7263  C CD2 . TRP E  2 33  ? 143.987 191.643 160.392 1.00 84.10  ? 67  TRP E CD2 1 
ATOM   7264  N NE1 . TRP E  2 33  ? 142.375 190.110 160.639 1.00 88.32  ? 67  TRP E NE1 1 
ATOM   7265  C CE2 . TRP E  2 33  ? 142.708 191.250 159.957 1.00 80.11  ? 67  TRP E CE2 1 
ATOM   7266  C CE3 . TRP E  2 33  ? 144.561 192.792 159.842 1.00 90.73  ? 67  TRP E CE3 1 
ATOM   7267  C CZ2 . TRP E  2 33  ? 141.994 191.963 158.998 1.00 77.78  ? 67  TRP E CZ2 1 
ATOM   7268  C CZ3 . TRP E  2 33  ? 143.850 193.498 158.891 1.00 86.94  ? 67  TRP E CZ3 1 
ATOM   7269  C CH2 . TRP E  2 33  ? 142.581 193.082 158.479 1.00 77.29  ? 67  TRP E CH2 1 
ATOM   7270  N N   . TYR E  2 34  ? 148.869 191.347 161.041 1.00 96.49  ? 68  TYR E N   1 
ATOM   7271  C CA  . TYR E  2 34  ? 150.180 191.887 161.362 1.00 97.65  ? 68  TYR E CA  1 
ATOM   7272  C C   . TYR E  2 34  ? 150.122 193.406 161.386 1.00 100.92 ? 68  TYR E C   1 
ATOM   7273  O O   . TYR E  2 34  ? 149.411 194.022 160.587 1.00 106.37 ? 68  TYR E O   1 
ATOM   7274  C CB  . TYR E  2 34  ? 151.232 191.429 160.349 1.00 97.75  ? 68  TYR E CB  1 
ATOM   7275  C CG  . TYR E  2 34  ? 151.378 189.931 160.250 1.00 97.35  ? 68  TYR E CG  1 
ATOM   7276  C CD1 . TYR E  2 34  ? 150.584 189.192 159.387 1.00 98.69  ? 68  TYR E CD1 1 
ATOM   7277  C CD2 . TYR E  2 34  ? 152.312 189.256 161.020 1.00 103.47 ? 68  TYR E CD2 1 
ATOM   7278  C CE1 . TYR E  2 34  ? 150.715 187.824 159.294 1.00 103.08 ? 68  TYR E CE1 1 
ATOM   7279  C CE2 . TYR E  2 34  ? 152.450 187.888 160.934 1.00 104.66 ? 68  TYR E CE2 1 
ATOM   7280  C CZ  . TYR E  2 34  ? 151.649 187.177 160.069 1.00 104.89 ? 68  TYR E CZ  1 
ATOM   7281  O OH  . TYR E  2 34  ? 151.784 185.812 159.979 1.00 111.04 ? 68  TYR E OH  1 
ATOM   7282  N N   . LYS E  2 35  ? 150.873 194.004 162.305 1.00 94.28  ? 69  LYS E N   1 
ATOM   7283  C CA  . LYS E  2 35  ? 150.991 195.454 162.369 1.00 98.02  ? 69  LYS E CA  1 
ATOM   7284  C C   . LYS E  2 35  ? 152.048 195.909 161.371 1.00 108.71 ? 69  LYS E C   1 
ATOM   7285  O O   . LYS E  2 35  ? 153.153 195.358 161.336 1.00 116.83 ? 69  LYS E O   1 
ATOM   7286  C CB  . LYS E  2 35  ? 151.349 195.899 163.784 1.00 106.35 ? 69  LYS E CB  1 
ATOM   7287  C CG  . LYS E  2 35  ? 151.806 197.343 163.884 1.00 113.38 ? 69  LYS E CG  1 
ATOM   7288  C CD  . LYS E  2 35  ? 150.786 198.194 164.620 1.00 115.01 ? 69  LYS E CD  1 
ATOM   7289  C CE  . LYS E  2 35  ? 151.344 199.571 164.937 1.00 117.45 ? 69  LYS E CE  1 
ATOM   7290  N NZ  . LYS E  2 35  ? 151.629 200.347 163.699 1.00 116.05 ? 69  LYS E NZ  1 
ATOM   7291  N N   . GLY E  2 36  ? 151.714 196.906 160.567 1.00 107.96 ? 70  GLY E N   1 
ATOM   7292  C CA  . GLY E  2 36  ? 152.597 197.400 159.531 1.00 108.08 ? 70  GLY E CA  1 
ATOM   7293  C C   . GLY E  2 36  ? 152.307 196.760 158.184 1.00 106.18 ? 70  GLY E C   1 
ATOM   7294  O O   . GLY E  2 36  ? 151.487 195.852 158.047 1.00 107.76 ? 70  GLY E O   1 
ATOM   7295  N N   . GLU E  2 37  ? 153.017 197.261 157.174 1.00 107.98 ? 71  GLU E N   1 
ATOM   7296  C CA  . GLU E  2 37  ? 152.824 196.809 155.802 1.00 113.33 ? 71  GLU E CA  1 
ATOM   7297  C C   . GLU E  2 37  ? 153.474 195.463 155.520 1.00 116.40 ? 71  GLU E C   1 
ATOM   7298  O O   . GLU E  2 37  ? 153.211 194.877 154.464 1.00 118.18 ? 71  GLU E O   1 
ATOM   7299  C CB  . GLU E  2 37  ? 153.375 197.850 154.826 1.00 115.79 ? 71  GLU E CB  1 
ATOM   7300  C CG  . GLU E  2 37  ? 152.343 198.843 154.328 1.00 123.53 ? 71  GLU E CG  1 
ATOM   7301  C CD  . GLU E  2 37  ? 152.919 200.233 154.153 1.00 135.41 ? 71  GLU E CD  1 
ATOM   7302  O OE1 . GLU E  2 37  ? 154.160 200.364 154.134 1.00 141.66 ? 71  GLU E OE1 1 
ATOM   7303  O OE2 . GLU E  2 37  ? 152.131 201.193 154.033 1.00 138.91 ? 71  GLU E OE2 1 
ATOM   7304  N N   . ARG E  2 38  ? 154.307 194.964 156.425 1.00 118.33 ? 72  ARG E N   1 
ATOM   7305  C CA  . ARG E  2 38  ? 155.044 193.726 156.227 1.00 122.99 ? 72  ARG E CA  1 
ATOM   7306  C C   . ARG E  2 38  ? 154.378 192.589 156.986 1.00 119.48 ? 72  ARG E C   1 
ATOM   7307  O O   . ARG E  2 38  ? 153.600 192.821 157.917 1.00 118.15 ? 72  ARG E O   1 
ATOM   7308  C CB  . ARG E  2 38  ? 156.492 193.874 156.698 1.00 131.79 ? 72  ARG E CB  1 
ATOM   7309  C CG  . ARG E  2 38  ? 157.427 194.505 155.687 1.00 137.00 ? 72  ARG E CG  1 
ATOM   7310  C CD  . ARG E  2 38  ? 158.308 193.447 155.033 1.00 140.87 ? 72  ARG E CD  1 
ATOM   7311  N NE  . ARG E  2 38  ? 159.160 192.726 155.975 1.00 150.10 ? 72  ARG E NE  1 
ATOM   7312  C CZ  . ARG E  2 38  ? 159.966 193.275 156.878 1.00 150.32 ? 72  ARG E CZ  1 
ATOM   7313  N NH1 . ARG E  2 38  ? 160.565 192.542 157.803 1.00 148.36 ? 72  ARG E NH1 1 
ATOM   7314  N NH2 . ARG E  2 38  ? 160.207 194.583 156.833 1.00 144.43 ? 72  ARG E NH2 1 
ATOM   7315  N N   . VAL E  2 39  ? 154.687 191.360 156.582 1.00 120.71 ? 73  VAL E N   1 
ATOM   7316  C CA  . VAL E  2 39  ? 154.301 190.179 157.345 1.00 116.73 ? 73  VAL E CA  1 
ATOM   7317  C C   . VAL E  2 39  ? 155.556 189.654 158.034 1.00 123.15 ? 73  VAL E C   1 
ATOM   7318  O O   . VAL E  2 39  ? 156.431 189.064 157.395 1.00 129.17 ? 73  VAL E O   1 
ATOM   7319  C CB  . VAL E  2 39  ? 153.657 189.110 156.455 1.00 110.84 ? 73  VAL E CB  1 
ATOM   7320  C CG1 . VAL E  2 39  ? 153.650 187.758 157.155 1.00 107.40 ? 73  VAL E CG1 1 
ATOM   7321  C CG2 . VAL E  2 39  ? 152.244 189.521 156.098 1.00 112.98 ? 73  VAL E CG2 1 
ATOM   7322  N N   . ASP E  2 40  ? 155.660 189.900 159.337 1.00 122.26 ? 74  ASP E N   1 
ATOM   7323  C CA  . ASP E  2 40  ? 156.813 189.489 160.119 1.00 123.37 ? 74  ASP E CA  1 
ATOM   7324  C C   . ASP E  2 40  ? 156.318 188.828 161.395 1.00 125.10 ? 74  ASP E C   1 
ATOM   7325  O O   . ASP E  2 40  ? 155.311 189.242 161.974 1.00 125.16 ? 74  ASP E O   1 
ATOM   7326  C CB  . ASP E  2 40  ? 157.723 190.684 160.444 1.00 124.70 ? 74  ASP E CB  1 
ATOM   7327  C CG  . ASP E  2 40  ? 158.956 190.288 161.234 1.00 132.96 ? 74  ASP E CG  1 
ATOM   7328  O OD1 . ASP E  2 40  ? 159.656 191.195 161.732 1.00 135.05 ? 74  ASP E OD1 1 
ATOM   7329  O OD2 . ASP E  2 40  ? 159.240 189.077 161.345 1.00 136.35 ? 74  ASP E OD2 1 
ATOM   7330  N N   . GLY E  2 41  ? 157.038 187.792 161.828 1.00 125.63 ? 75  GLY E N   1 
ATOM   7331  C CA  . GLY E  2 41  ? 156.614 187.053 163.005 1.00 121.76 ? 75  GLY E CA  1 
ATOM   7332  C C   . GLY E  2 41  ? 156.579 187.909 164.256 1.00 122.95 ? 75  GLY E C   1 
ATOM   7333  O O   . GLY E  2 41  ? 155.774 187.674 165.159 1.00 123.38 ? 75  GLY E O   1 
ATOM   7334  N N   . ASN E  2 42  ? 157.451 188.917 164.325 1.00 124.14 ? 76  ASN E N   1 
ATOM   7335  C CA  . ASN E  2 42  ? 157.481 189.798 165.485 1.00 123.42 ? 76  ASN E CA  1 
ATOM   7336  C C   . ASN E  2 42  ? 156.294 190.751 165.517 1.00 119.81 ? 76  ASN E C   1 
ATOM   7337  O O   . ASN E  2 42  ? 155.965 191.276 166.586 1.00 117.59 ? 76  ASN E O   1 
ATOM   7338  C CB  . ASN E  2 42  ? 158.785 190.594 165.501 1.00 130.01 ? 76  ASN E CB  1 
ATOM   7339  C CG  . ASN E  2 42  ? 159.984 189.754 165.110 1.00 136.13 ? 76  ASN E CG  1 
ATOM   7340  O OD1 . ASN E  2 42  ? 160.120 188.609 165.539 1.00 140.42 ? 76  ASN E OD1 1 
ATOM   7341  N ND2 . ASN E  2 42  ? 160.859 190.319 164.287 1.00 134.53 ? 76  ASN E ND2 1 
ATOM   7342  N N   . ARG E  2 43  ? 155.649 190.988 164.378 1.00 118.59 ? 77  ARG E N   1 
ATOM   7343  C CA  . ARG E  2 43  ? 154.540 191.929 164.289 1.00 115.72 ? 77  ARG E CA  1 
ATOM   7344  C C   . ARG E  2 43  ? 153.173 191.262 164.320 1.00 113.35 ? 77  ARG E C   1 
ATOM   7345  O O   . ARG E  2 43  ? 152.165 191.951 164.129 1.00 113.50 ? 77  ARG E O   1 
ATOM   7346  C CB  . ARG E  2 43  ? 154.659 192.770 163.014 1.00 115.26 ? 77  ARG E CB  1 
ATOM   7347  C CG  . ARG E  2 43  ? 156.063 193.245 162.695 1.00 119.55 ? 77  ARG E CG  1 
ATOM   7348  C CD  . ARG E  2 43  ? 156.624 194.085 163.830 1.00 126.44 ? 77  ARG E CD  1 
ATOM   7349  N NE  . ARG E  2 43  ? 155.989 195.396 163.902 1.00 132.43 ? 77  ARG E NE  1 
ATOM   7350  C CZ  . ARG E  2 43  ? 156.207 196.388 163.049 1.00 133.47 ? 77  ARG E CZ  1 
ATOM   7351  N NH1 . ARG E  2 43  ? 157.049 196.258 162.037 1.00 133.97 ? 77  ARG E NH1 1 
ATOM   7352  N NH2 . ARG E  2 43  ? 155.565 197.540 163.217 1.00 130.30 ? 77  ARG E NH2 1 
ATOM   7353  N N   . GLN E  2 44  ? 153.102 189.952 164.542 1.00 110.61 ? 78  GLN E N   1 
ATOM   7354  C CA  . GLN E  2 44  ? 151.812 189.276 164.529 1.00 105.18 ? 78  GLN E CA  1 
ATOM   7355  C C   . GLN E  2 44  ? 150.963 189.723 165.710 1.00 106.91 ? 78  GLN E C   1 
ATOM   7356  O O   . GLN E  2 44  ? 151.391 189.646 166.865 1.00 112.38 ? 78  GLN E O   1 
ATOM   7357  C CB  . GLN E  2 44  ? 151.999 187.761 164.559 1.00 104.08 ? 78  GLN E CB  1 
ATOM   7358  C CG  . GLN E  2 44  ? 150.715 186.992 164.292 1.00 102.60 ? 78  GLN E CG  1 
ATOM   7359  C CD  . GLN E  2 44  ? 150.876 185.498 164.470 1.00 109.94 ? 78  GLN E CD  1 
ATOM   7360  O OE1 . GLN E  2 44  ? 151.583 185.041 165.366 1.00 121.63 ? 78  GLN E OE1 1 
ATOM   7361  N NE2 . GLN E  2 44  ? 150.214 184.728 163.616 1.00 107.83 ? 78  GLN E NE2 1 
ATOM   7362  N N   . ILE E  2 45  ? 149.755 190.186 165.415 1.00 99.73  ? 79  ILE E N   1 
ATOM   7363  C CA  . ILE E  2 45  ? 148.810 190.622 166.435 1.00 95.96  ? 79  ILE E CA  1 
ATOM   7364  C C   . ILE E  2 45  ? 147.985 189.458 166.957 1.00 99.36  ? 79  ILE E C   1 
ATOM   7365  O O   . ILE E  2 45  ? 147.891 189.243 168.165 1.00 106.96 ? 79  ILE E O   1 
ATOM   7366  C CB  . ILE E  2 45  ? 147.901 191.741 165.878 1.00 91.20  ? 79  ILE E CB  1 
ATOM   7367  C CG1 . ILE E  2 45  ? 148.738 192.940 165.438 1.00 100.25 ? 79  ILE E CG1 1 
ATOM   7368  C CG2 . ILE E  2 45  ? 146.876 192.156 166.915 1.00 95.59  ? 79  ILE E CG2 1 
ATOM   7369  C CD1 . ILE E  2 45  ? 147.999 193.889 164.527 1.00 100.47 ? 79  ILE E CD1 1 
ATOM   7370  N N   . VAL E  2 46  ? 147.379 188.692 166.051 1.00 98.81  ? 80  VAL E N   1 
ATOM   7371  C CA  . VAL E  2 46  ? 146.520 187.576 166.426 1.00 99.52  ? 80  VAL E CA  1 
ATOM   7372  C C   . VAL E  2 46  ? 146.455 186.627 165.241 1.00 99.69  ? 80  VAL E C   1 
ATOM   7373  O O   . VAL E  2 46  ? 146.715 187.015 164.101 1.00 102.61 ? 80  VAL E O   1 
ATOM   7374  C CB  . VAL E  2 46  ? 145.113 188.074 166.844 1.00 95.88  ? 80  VAL E CB  1 
ATOM   7375  C CG1 . VAL E  2 46  ? 144.303 188.457 165.620 1.00 92.79  ? 80  VAL E CG1 1 
ATOM   7376  C CG2 . VAL E  2 46  ? 144.391 187.023 167.674 1.00 101.79 ? 80  VAL E CG2 1 
ATOM   7377  N N   . GLY E  2 47  ? 146.117 185.376 165.511 1.00 95.49  ? 81  GLY E N   1 
ATOM   7378  C CA  . GLY E  2 47  ? 145.998 184.383 164.462 1.00 93.87  ? 81  GLY E CA  1 
ATOM   7379  C C   . GLY E  2 47  ? 144.891 183.403 164.780 1.00 96.52  ? 81  GLY E C   1 
ATOM   7380  O O   . GLY E  2 47  ? 144.648 183.061 165.939 1.00 104.35 ? 81  GLY E O   1 
ATOM   7381  N N   . TYR E  2 48  ? 144.217 182.951 163.727 1.00 92.87  ? 82  TYR E N   1 
ATOM   7382  C CA  . TYR E  2 48  ? 143.123 182.002 163.857 1.00 95.23  ? 82  TYR E CA  1 
ATOM   7383  C C   . TYR E  2 48  ? 143.453 180.757 163.050 1.00 99.66  ? 82  TYR E C   1 
ATOM   7384  O O   . TYR E  2 48  ? 144.068 180.846 161.985 1.00 103.37 ? 82  TYR E O   1 
ATOM   7385  C CB  . TYR E  2 48  ? 141.797 182.604 163.378 1.00 97.39  ? 82  TYR E CB  1 
ATOM   7386  C CG  . TYR E  2 48  ? 140.580 181.791 163.750 1.00 99.60  ? 82  TYR E CG  1 
ATOM   7387  C CD1 . TYR E  2 48  ? 140.247 181.575 165.080 1.00 100.93 ? 82  TYR E CD1 1 
ATOM   7388  C CD2 . TYR E  2 48  ? 139.763 181.242 162.773 1.00 103.78 ? 82  TYR E CD2 1 
ATOM   7389  C CE1 . TYR E  2 48  ? 139.136 180.834 165.425 1.00 104.43 ? 82  TYR E CE1 1 
ATOM   7390  C CE2 . TYR E  2 48  ? 138.649 180.499 163.109 1.00 105.71 ? 82  TYR E CE2 1 
ATOM   7391  C CZ  . TYR E  2 48  ? 138.341 180.298 164.437 1.00 109.48 ? 82  TYR E CZ  1 
ATOM   7392  O OH  . TYR E  2 48  ? 137.232 179.559 164.776 1.00 119.56 ? 82  TYR E OH  1 
ATOM   7393  N N   . ALA E  2 49  ? 143.047 179.601 163.566 1.00 102.57 ? 83  ALA E N   1 
ATOM   7394  C CA  . ALA E  2 49  ? 143.243 178.319 162.898 1.00 104.14 ? 83  ALA E CA  1 
ATOM   7395  C C   . ALA E  2 49  ? 141.881 177.653 162.759 1.00 109.50 ? 83  ALA E C   1 
ATOM   7396  O O   . ALA E  2 49  ? 141.306 177.198 163.752 1.00 115.37 ? 83  ALA E O   1 
ATOM   7397  C CB  . ALA E  2 49  ? 144.216 177.434 163.673 1.00 106.40 ? 83  ALA E CB  1 
ATOM   7398  N N   . ILE E  2 50  ? 141.369 177.599 161.528 1.00 105.53 ? 84  ILE E N   1 
ATOM   7399  C CA  . ILE E  2 50  ? 140.028 177.068 161.296 1.00 106.58 ? 84  ILE E CA  1 
ATOM   7400  C C   . ILE E  2 50  ? 139.955 175.597 161.686 1.00 113.54 ? 84  ILE E C   1 
ATOM   7401  O O   . ILE E  2 50  ? 138.932 175.127 162.201 1.00 116.18 ? 84  ILE E O   1 
ATOM   7402  C CB  . ILE E  2 50  ? 139.615 177.291 159.829 1.00 106.97 ? 84  ILE E CB  1 
ATOM   7403  C CG1 . ILE E  2 50  ? 139.418 178.782 159.557 1.00 108.10 ? 84  ILE E CG1 1 
ATOM   7404  C CG2 . ILE E  2 50  ? 138.343 176.529 159.498 1.00 106.78 ? 84  ILE E CG2 1 
ATOM   7405  C CD1 . ILE E  2 50  ? 140.289 179.314 158.453 1.00 108.45 ? 84  ILE E CD1 1 
ATOM   7406  N N   . GLY E  2 51  ? 141.036 174.850 161.448 1.00 117.11 ? 85  GLY E N   1 
ATOM   7407  C CA  . GLY E  2 51  ? 141.020 173.422 161.734 1.00 120.91 ? 85  GLY E CA  1 
ATOM   7408  C C   . GLY E  2 51  ? 140.633 173.108 163.166 1.00 120.29 ? 85  GLY E C   1 
ATOM   7409  O O   . GLY E  2 51  ? 139.644 172.415 163.418 1.00 123.30 ? 85  GLY E O   1 
ATOM   7410  N N   . THR E  2 52  ? 141.404 173.615 164.125 1.00 115.63 ? 86  THR E N   1 
ATOM   7411  C CA  . THR E  2 52  ? 141.136 173.388 165.538 1.00 118.91 ? 86  THR E CA  1 
ATOM   7412  C C   . THR E  2 52  ? 140.242 174.460 166.150 1.00 122.00 ? 86  THR E C   1 
ATOM   7413  O O   . THR E  2 52  ? 139.867 174.340 167.321 1.00 124.32 ? 86  THR E O   1 
ATOM   7414  C CB  . THR E  2 52  ? 142.450 173.300 166.317 1.00 123.17 ? 86  THR E CB  1 
ATOM   7415  O OG1 . THR E  2 52  ? 143.139 174.554 166.241 1.00 124.05 ? 86  THR E OG1 1 
ATOM   7416  C CG2 . THR E  2 52  ? 143.336 172.207 165.741 1.00 126.16 ? 86  THR E CG2 1 
ATOM   7417  N N   . GLN E  2 53  ? 139.890 175.493 165.387 1.00 120.25 ? 87  GLN E N   1 
ATOM   7418  C CA  . GLN E  2 53  ? 139.048 176.594 165.857 1.00 115.73 ? 87  GLN E CA  1 
ATOM   7419  C C   . GLN E  2 53  ? 139.629 177.227 167.122 1.00 112.78 ? 87  GLN E C   1 
ATOM   7420  O O   . GLN E  2 53  ? 139.008 177.252 168.186 1.00 112.54 ? 87  GLN E O   1 
ATOM   7421  C CB  . GLN E  2 53  ? 137.609 176.126 166.081 1.00 114.74 ? 87  GLN E CB  1 
ATOM   7422  C CG  . GLN E  2 53  ? 136.767 176.106 164.819 1.00 119.86 ? 87  GLN E CG  1 
ATOM   7423  C CD  . GLN E  2 53  ? 136.057 174.784 164.615 1.00 132.16 ? 87  GLN E CD  1 
ATOM   7424  O OE1 . GLN E  2 53  ? 136.231 173.847 165.393 1.00 137.13 ? 87  GLN E OE1 1 
ATOM   7425  N NE2 . GLN E  2 53  ? 135.251 174.702 163.563 1.00 137.64 ? 87  GLN E NE2 1 
ATOM   7426  N N   . GLN E  2 54  ? 140.847 177.743 166.984 1.00 110.82 ? 88  GLN E N   1 
ATOM   7427  C CA  . GLN E  2 54  ? 141.564 178.362 168.088 1.00 110.63 ? 88  GLN E CA  1 
ATOM   7428  C C   . GLN E  2 54  ? 142.130 179.703 167.648 1.00 109.10 ? 88  GLN E C   1 
ATOM   7429  O O   . GLN E  2 54  ? 142.678 179.826 166.549 1.00 111.05 ? 88  GLN E O   1 
ATOM   7430  C CB  . GLN E  2 54  ? 142.697 177.459 168.591 1.00 113.42 ? 88  GLN E CB  1 
ATOM   7431  C CG  . GLN E  2 54  ? 142.441 176.847 169.958 1.00 121.03 ? 88  GLN E CG  1 
ATOM   7432  C CD  . GLN E  2 54  ? 142.826 177.773 171.095 1.00 128.00 ? 88  GLN E CD  1 
ATOM   7433  O OE1 . GLN E  2 54  ? 143.112 178.951 170.883 1.00 126.05 ? 88  GLN E OE1 1 
ATOM   7434  N NE2 . GLN E  2 54  ? 142.834 177.243 172.312 1.00 140.86 ? 88  GLN E NE2 1 
ATOM   7435  N N   . ALA E  2 55  ? 141.995 180.705 168.514 1.00 107.88 ? 89  ALA E N   1 
ATOM   7436  C CA  . ALA E  2 55  ? 142.539 182.039 168.282 1.00 106.64 ? 89  ALA E CA  1 
ATOM   7437  C C   . ALA E  2 55  ? 143.664 182.267 169.282 1.00 107.55 ? 89  ALA E C   1 
ATOM   7438  O O   . ALA E  2 55  ? 143.437 182.230 170.496 1.00 115.44 ? 89  ALA E O   1 
ATOM   7439  C CB  . ALA E  2 55  ? 141.456 183.107 168.415 1.00 107.91 ? 89  ALA E CB  1 
ATOM   7440  N N   . THR E  2 56  ? 144.870 182.505 168.775 1.00 105.48 ? 90  THR E N   1 
ATOM   7441  C CA  . THR E  2 56  ? 146.058 182.633 169.610 1.00 112.25 ? 90  THR E CA  1 
ATOM   7442  C C   . THR E  2 56  ? 146.650 184.027 169.460 1.00 112.74 ? 90  THR E C   1 
ATOM   7443  O O   . THR E  2 56  ? 147.023 184.418 168.340 1.00 112.72 ? 90  THR E O   1 
ATOM   7444  C CB  . THR E  2 56  ? 147.098 181.573 169.241 1.00 115.59 ? 90  THR E CB  1 
ATOM   7445  O OG1 . THR E  2 56  ? 147.224 181.502 167.816 1.00 117.08 ? 90  THR E OG1 1 
ATOM   7446  C CG2 . THR E  2 56  ? 146.682 180.213 169.775 1.00 112.50 ? 90  THR E CG2 1 
ATOM   7447  N N   . PRO E  2 57  ? 146.751 184.808 170.533 1.00 112.71 ? 91  PRO E N   1 
ATOM   7448  C CA  . PRO E  2 57  ? 147.389 186.123 170.431 1.00 109.95 ? 91  PRO E CA  1 
ATOM   7449  C C   . PRO E  2 57  ? 148.856 186.005 170.054 1.00 108.14 ? 91  PRO E C   1 
ATOM   7450  O O   . PRO E  2 57  ? 149.533 185.028 170.383 1.00 111.44 ? 91  PRO E O   1 
ATOM   7451  C CB  . PRO E  2 57  ? 147.223 186.705 171.840 1.00 110.48 ? 91  PRO E CB  1 
ATOM   7452  C CG  . PRO E  2 57  ? 147.039 185.499 172.716 1.00 113.62 ? 91  PRO E CG  1 
ATOM   7453  C CD  . PRO E  2 57  ? 146.216 184.570 171.882 1.00 113.62 ? 91  PRO E CD  1 
ATOM   7454  N N   . GLY E  2 58  ? 149.343 187.021 169.347 1.00 107.03 ? 92  GLY E N   1 
ATOM   7455  C CA  . GLY E  2 58  ? 150.717 187.050 168.908 1.00 108.86 ? 92  GLY E CA  1 
ATOM   7456  C C   . GLY E  2 58  ? 151.585 187.922 169.791 1.00 114.35 ? 92  GLY E C   1 
ATOM   7457  O O   . GLY E  2 58  ? 151.119 188.517 170.768 1.00 117.27 ? 92  GLY E O   1 
ATOM   7458  N N   . PRO E  2 59  ? 152.877 188.004 169.466 1.00 112.69 ? 93  PRO E N   1 
ATOM   7459  C CA  . PRO E  2 59  ? 153.781 188.848 170.263 1.00 110.22 ? 93  PRO E CA  1 
ATOM   7460  C C   . PRO E  2 59  ? 153.386 190.314 170.286 1.00 110.86 ? 93  PRO E C   1 
ATOM   7461  O O   . PRO E  2 59  ? 153.630 190.995 171.290 1.00 113.86 ? 93  PRO E O   1 
ATOM   7462  C CB  . PRO E  2 59  ? 155.139 188.637 169.577 1.00 113.10 ? 93  PRO E CB  1 
ATOM   7463  C CG  . PRO E  2 59  ? 154.781 188.177 168.190 1.00 116.47 ? 93  PRO E CG  1 
ATOM   7464  C CD  . PRO E  2 59  ? 153.609 187.281 168.415 1.00 112.16 ? 93  PRO E CD  1 
ATOM   7465  N N   . ALA E  2 60  ? 152.787 190.823 169.214 1.00 110.87 ? 94  ALA E N   1 
ATOM   7466  C CA  . ALA E  2 60  ? 152.379 192.219 169.141 1.00 110.81 ? 94  ALA E CA  1 
ATOM   7467  C C   . ALA E  2 60  ? 151.037 192.481 169.812 1.00 114.27 ? 94  ALA E C   1 
ATOM   7468  O O   . ALA E  2 60  ? 150.601 193.636 169.858 1.00 117.56 ? 94  ALA E O   1 
ATOM   7469  C CB  . ALA E  2 60  ? 152.322 192.678 167.681 1.00 107.04 ? 94  ALA E CB  1 
ATOM   7470  N N   . ASN E  2 61  ? 150.375 191.446 170.322 1.00 115.72 ? 95  ASN E N   1 
ATOM   7471  C CA  . ASN E  2 61  ? 149.086 191.630 170.974 1.00 119.41 ? 95  ASN E CA  1 
ATOM   7472  C C   . ASN E  2 61  ? 149.239 192.448 172.250 1.00 121.11 ? 95  ASN E C   1 
ATOM   7473  O O   . ASN E  2 61  ? 150.254 192.363 172.947 1.00 121.67 ? 95  ASN E O   1 
ATOM   7474  C CB  . ASN E  2 61  ? 148.456 190.275 171.294 1.00 120.40 ? 95  ASN E CB  1 
ATOM   7475  C CG  . ASN E  2 61  ? 146.980 190.381 171.619 1.00 119.37 ? 95  ASN E CG  1 
ATOM   7476  O OD1 . ASN E  2 61  ? 146.603 190.724 172.739 1.00 122.49 ? 95  ASN E OD1 1 
ATOM   7477  N ND2 . ASN E  2 61  ? 146.136 190.085 170.639 1.00 113.65 ? 95  ASN E ND2 1 
ATOM   7478  N N   . SER E  2 62  ? 148.218 193.249 172.552 1.00 126.64 ? 96  SER E N   1 
ATOM   7479  C CA  . SER E  2 62  ? 148.189 194.057 173.765 1.00 129.78 ? 96  SER E CA  1 
ATOM   7480  C C   . SER E  2 62  ? 146.923 193.831 174.581 1.00 128.51 ? 96  SER E C   1 
ATOM   7481  O O   . SER E  2 62  ? 146.648 194.603 175.507 1.00 125.85 ? 96  SER E O   1 
ATOM   7482  C CB  . SER E  2 62  ? 148.331 195.542 173.418 1.00 127.38 ? 96  SER E CB  1 
ATOM   7483  O OG  . SER E  2 62  ? 147.157 196.034 172.796 1.00 126.50 ? 96  SER E OG  1 
ATOM   7484  N N   . GLY E  2 63  ? 146.144 192.798 174.261 1.00 125.84 ? 97  GLY E N   1 
ATOM   7485  C CA  . GLY E  2 63  ? 144.918 192.509 174.969 1.00 122.43 ? 97  GLY E CA  1 
ATOM   7486  C C   . GLY E  2 63  ? 143.699 193.247 174.468 1.00 123.72 ? 97  GLY E C   1 
ATOM   7487  O O   . GLY E  2 63  ? 142.587 192.952 174.924 1.00 126.98 ? 97  GLY E O   1 
ATOM   7488  N N   . ARG E  2 64  ? 143.863 194.194 173.550 1.00 124.64 ? 98  ARG E N   1 
ATOM   7489  C CA  . ARG E  2 64  ? 142.754 194.969 173.016 1.00 124.66 ? 98  ARG E CA  1 
ATOM   7490  C C   . ARG E  2 64  ? 142.260 194.454 171.671 1.00 118.10 ? 98  ARG E C   1 
ATOM   7491  O O   . ARG E  2 64  ? 141.336 195.044 171.102 1.00 111.73 ? 98  ARG E O   1 
ATOM   7492  C CB  . ARG E  2 64  ? 143.163 196.435 172.869 1.00 122.43 ? 98  ARG E CB  1 
ATOM   7493  C CG  . ARG E  2 64  ? 143.669 197.088 174.139 1.00 118.52 ? 98  ARG E CG  1 
ATOM   7494  C CD  . ARG E  2 64  ? 144.217 198.469 173.832 1.00 123.58 ? 98  ARG E CD  1 
ATOM   7495  N NE  . ARG E  2 64  ? 145.283 198.412 172.840 1.00 125.95 ? 98  ARG E NE  1 
ATOM   7496  C CZ  . ARG E  2 64  ? 145.484 199.326 171.901 1.00 126.64 ? 98  ARG E CZ  1 
ATOM   7497  N NH1 . ARG E  2 64  ? 144.703 200.388 171.793 1.00 131.98 ? 98  ARG E NH1 1 
ATOM   7498  N NH2 . ARG E  2 64  ? 146.490 199.169 171.046 1.00 124.53 ? 98  ARG E NH2 1 
ATOM   7499  N N   . GLU E  2 65  ? 142.844 193.379 171.153 1.00 118.04 ? 99  GLU E N   1 
ATOM   7500  C CA  . GLU E  2 65  ? 142.560 192.902 169.808 1.00 116.06 ? 99  GLU E CA  1 
ATOM   7501  C C   . GLU E  2 65  ? 141.925 191.521 169.871 1.00 119.99 ? 99  GLU E C   1 
ATOM   7502  O O   . GLU E  2 65  ? 142.456 190.616 170.523 1.00 123.51 ? 99  GLU E O   1 
ATOM   7503  C CB  . GLU E  2 65  ? 143.838 192.859 168.967 1.00 112.67 ? 99  GLU E CB  1 
ATOM   7504  C CG  . GLU E  2 65  ? 144.736 194.076 169.132 1.00 115.83 ? 99  GLU E CG  1 
ATOM   7505  C CD  . GLU E  2 65  ? 145.738 193.919 170.261 1.00 128.42 ? 99  GLU E CD  1 
ATOM   7506  O OE1 . GLU E  2 65  ? 145.447 193.172 171.219 1.00 128.66 ? 99  GLU E OE1 1 
ATOM   7507  O OE2 . GLU E  2 65  ? 146.817 194.543 170.189 1.00 131.94 ? 99  GLU E OE2 1 
ATOM   7508  N N   . THR E  2 66  ? 140.792 191.367 169.192 1.00 117.08 ? 100 THR E N   1 
ATOM   7509  C CA  . THR E  2 66  ? 140.104 190.092 169.083 1.00 113.90 ? 100 THR E CA  1 
ATOM   7510  C C   . THR E  2 66  ? 139.829 189.797 167.617 1.00 112.16 ? 100 THR E C   1 
ATOM   7511  O O   . THR E  2 66  ? 139.426 190.680 166.856 1.00 110.05 ? 100 THR E O   1 
ATOM   7512  C CB  . THR E  2 66  ? 138.782 190.083 169.863 1.00 117.23 ? 100 THR E CB  1 
ATOM   7513  O OG1 . THR E  2 66  ? 137.914 191.102 169.350 1.00 116.15 ? 100 THR E OG1 1 
ATOM   7514  C CG2 . THR E  2 66  ? 139.030 190.331 171.341 1.00 117.60 ? 100 THR E CG2 1 
ATOM   7515  N N   . ILE E  2 67  ? 140.052 188.546 167.226 1.00 111.67 ? 101 ILE E N   1 
ATOM   7516  C CA  . ILE E  2 67  ? 139.804 188.090 165.864 1.00 108.44 ? 101 ILE E CA  1 
ATOM   7517  C C   . ILE E  2 67  ? 138.473 187.350 165.850 1.00 108.39 ? 101 ILE E C   1 
ATOM   7518  O O   . ILE E  2 67  ? 138.060 186.779 166.867 1.00 110.23 ? 101 ILE E O   1 
ATOM   7519  C CB  . ILE E  2 67  ? 140.953 187.207 165.343 1.00 104.65 ? 101 ILE E CB  1 
ATOM   7520  C CG1 . ILE E  2 67  ? 141.024 187.268 163.815 1.00 105.23 ? 101 ILE E CG1 1 
ATOM   7521  C CG2 . ILE E  2 67  ? 140.808 185.773 165.821 1.00 102.71 ? 101 ILE E CG2 1 
ATOM   7522  C CD1 . ILE E  2 67  ? 141.993 186.276 163.205 1.00 103.75 ? 101 ILE E CD1 1 
ATOM   7523  N N   . TYR E  2 68  ? 137.790 187.391 164.712 1.00 109.01 ? 102 TYR E N   1 
ATOM   7524  C CA  . TYR E  2 68  ? 136.501 186.748 164.518 1.00 111.69 ? 102 TYR E CA  1 
ATOM   7525  C C   . TYR E  2 68  ? 136.588 185.654 163.466 1.00 115.44 ? 102 TYR E C   1 
ATOM   7526  O O   . TYR E  2 68  ? 137.491 185.654 162.623 1.00 117.42 ? 102 TYR E O   1 
ATOM   7527  C CB  . TYR E  2 68  ? 135.453 187.782 164.112 1.00 111.62 ? 102 TYR E CB  1 
ATOM   7528  C CG  . TYR E  2 68  ? 135.059 188.728 165.218 1.00 113.66 ? 102 TYR E CG  1 
ATOM   7529  C CD1 . TYR E  2 68  ? 135.274 188.399 166.549 1.00 112.87 ? 102 TYR E CD1 1 
ATOM   7530  C CD2 . TYR E  2 68  ? 134.443 189.937 164.935 1.00 118.33 ? 102 TYR E CD2 1 
ATOM   7531  C CE1 . TYR E  2 68  ? 134.904 189.256 167.566 1.00 117.29 ? 102 TYR E CE1 1 
ATOM   7532  C CE2 . TYR E  2 68  ? 134.067 190.801 165.945 1.00 120.77 ? 102 TYR E CE2 1 
ATOM   7533  C CZ  . TYR E  2 68  ? 134.300 190.455 167.259 1.00 124.11 ? 102 TYR E CZ  1 
ATOM   7534  O OH  . TYR E  2 68  ? 133.929 191.310 168.271 1.00 130.94 ? 102 TYR E OH  1 
ATOM   7535  N N   . PRO E  2 69  ? 135.662 184.692 163.498 1.00 116.14 ? 103 PRO E N   1 
ATOM   7536  C CA  . PRO E  2 69  ? 135.669 183.633 162.477 1.00 112.89 ? 103 PRO E CA  1 
ATOM   7537  C C   . PRO E  2 69  ? 135.583 184.147 161.045 1.00 112.15 ? 103 PRO E C   1 
ATOM   7538  O O   . PRO E  2 69  ? 136.219 183.554 160.167 1.00 111.63 ? 103 PRO E O   1 
ATOM   7539  C CB  . PRO E  2 69  ? 134.447 182.782 162.854 1.00 118.54 ? 103 PRO E CB  1 
ATOM   7540  C CG  . PRO E  2 69  ? 133.593 183.700 163.703 1.00 118.41 ? 103 PRO E CG  1 
ATOM   7541  C CD  . PRO E  2 69  ? 134.603 184.466 164.495 1.00 117.96 ? 103 PRO E CD  1 
ATOM   7542  N N   . ASN E  2 70  ? 134.846 185.228 160.771 1.00 111.01 ? 104 ASN E N   1 
ATOM   7543  C CA  . ASN E  2 70  ? 134.889 185.831 159.446 1.00 111.57 ? 104 ASN E CA  1 
ATOM   7544  C C   . ASN E  2 70  ? 136.075 186.796 159.272 1.00 115.54 ? 104 ASN E C   1 
ATOM   7545  O O   . ASN E  2 70  ? 135.950 187.835 158.617 1.00 123.38 ? 104 ASN E O   1 
ATOM   7546  C CB  . ASN E  2 70  ? 133.523 186.479 159.136 1.00 113.00 ? 104 ASN E CB  1 
ATOM   7547  C CG  . ASN E  2 70  ? 133.330 187.885 159.729 1.00 115.94 ? 104 ASN E CG  1 
ATOM   7548  O OD1 . ASN E  2 70  ? 133.873 188.867 159.232 1.00 124.05 ? 104 ASN E OD1 1 
ATOM   7549  N ND2 . ASN E  2 70  ? 132.504 187.981 160.762 1.00 117.38 ? 104 ASN E ND2 1 
ATOM   7550  N N   . ALA E  2 71  ? 137.261 186.394 159.724 1.00 112.02 ? 105 ALA E N   1 
ATOM   7551  C CA  . ALA E  2 71  ? 138.538 187.064 159.502 1.00 105.37 ? 105 ALA E CA  1 
ATOM   7552  C C   . ALA E  2 71  ? 138.558 188.527 159.936 1.00 104.97 ? 105 ALA E C   1 
ATOM   7553  O O   . ALA E  2 71  ? 139.494 189.245 159.570 1.00 109.60 ? 105 ALA E O   1 
ATOM   7554  C CB  . ALA E  2 71  ? 138.977 186.990 158.031 1.00 104.49 ? 105 ALA E CB  1 
ATOM   7555  N N   . SER E  2 72  ? 137.587 188.990 160.715 1.00 107.29 ? 106 SER E N   1 
ATOM   7556  C CA  . SER E  2 72  ? 137.545 190.396 161.092 1.00 102.65 ? 106 SER E CA  1 
ATOM   7557  C C   . SER E  2 72  ? 138.364 190.632 162.354 1.00 107.17 ? 106 SER E C   1 
ATOM   7558  O O   . SER E  2 72  ? 138.451 189.760 163.225 1.00 112.89 ? 106 SER E O   1 
ATOM   7559  C CB  . SER E  2 72  ? 136.105 190.846 161.309 1.00 110.74 ? 106 SER E CB  1 
ATOM   7560  O OG  . SER E  2 72  ? 135.280 190.441 160.232 1.00 124.98 ? 106 SER E OG  1 
ATOM   7561  N N   . LEU E  2 73  ? 138.968 191.812 162.448 1.00 107.48 ? 107 LEU E N   1 
ATOM   7562  C CA  . LEU E  2 73  ? 139.758 192.203 163.608 1.00 101.75 ? 107 LEU E CA  1 
ATOM   7563  C C   . LEU E  2 73  ? 139.097 193.388 164.296 1.00 105.32 ? 107 LEU E C   1 
ATOM   7564  O O   . LEU E  2 73  ? 138.773 194.388 163.646 1.00 107.61 ? 107 LEU E O   1 
ATOM   7565  C CB  . LEU E  2 73  ? 141.187 192.558 163.198 1.00 91.70  ? 107 LEU E CB  1 
ATOM   7566  C CG  . LEU E  2 73  ? 142.112 192.998 164.332 1.00 93.15  ? 107 LEU E CG  1 
ATOM   7567  C CD1 . LEU E  2 73  ? 142.425 191.828 165.248 1.00 99.54  ? 107 LEU E CD1 1 
ATOM   7568  C CD2 . LEU E  2 73  ? 143.389 193.605 163.778 1.00 94.97  ? 107 LEU E CD2 1 
ATOM   7569  N N   . LEU E  2 74  ? 138.899 193.272 165.605 1.00 102.59 ? 108 LEU E N   1 
ATOM   7570  C CA  . LEU E  2 74  ? 138.308 194.326 166.416 1.00 103.10 ? 108 LEU E CA  1 
ATOM   7571  C C   . LEU E  2 74  ? 139.347 194.837 167.401 1.00 110.55 ? 108 LEU E C   1 
ATOM   7572  O O   . LEU E  2 74  ? 139.935 194.051 168.150 1.00 117.23 ? 108 LEU E O   1 
ATOM   7573  C CB  . LEU E  2 74  ? 137.071 193.823 167.165 1.00 106.06 ? 108 LEU E CB  1 
ATOM   7574  C CG  . LEU E  2 74  ? 136.467 194.798 168.178 1.00 108.10 ? 108 LEU E CG  1 
ATOM   7575  C CD1 . LEU E  2 74  ? 136.010 196.072 167.487 1.00 110.73 ? 108 LEU E CD1 1 
ATOM   7576  C CD2 . LEU E  2 74  ? 135.318 194.154 168.936 1.00 112.62 ? 108 LEU E CD2 1 
ATOM   7577  N N   . ILE E  2 75  ? 139.571 196.148 167.396 1.00 110.07 ? 109 ILE E N   1 
ATOM   7578  C CA  . ILE E  2 75  ? 140.533 196.793 168.282 1.00 105.92 ? 109 ILE E CA  1 
ATOM   7579  C C   . ILE E  2 75  ? 139.771 197.750 169.185 1.00 114.77 ? 109 ILE E C   1 
ATOM   7580  O O   . ILE E  2 75  ? 139.181 198.725 168.705 1.00 117.46 ? 109 ILE E O   1 
ATOM   7581  C CB  . ILE E  2 75  ? 141.622 197.537 167.496 1.00 98.93  ? 109 ILE E CB  1 
ATOM   7582  C CG1 . ILE E  2 75  ? 142.529 196.545 166.770 1.00 100.69 ? 109 ILE E CG1 1 
ATOM   7583  C CG2 . ILE E  2 75  ? 142.439 198.417 168.425 1.00 113.63 ? 109 ILE E CG2 1 
ATOM   7584  C CD1 . ILE E  2 75  ? 143.394 197.182 165.712 1.00 100.19 ? 109 ILE E CD1 1 
ATOM   7585  N N   . GLN E  2 76  ? 139.794 197.479 170.485 1.00 117.48 ? 110 GLN E N   1 
ATOM   7586  C CA  . GLN E  2 76  ? 139.157 198.310 171.495 1.00 120.30 ? 110 GLN E CA  1 
ATOM   7587  C C   . GLN E  2 76  ? 140.216 199.149 172.197 1.00 129.83 ? 110 GLN E C   1 
ATOM   7588  O O   . GLN E  2 76  ? 141.407 198.829 172.157 1.00 133.08 ? 110 GLN E O   1 
ATOM   7589  C CB  . GLN E  2 76  ? 138.408 197.446 172.511 1.00 118.24 ? 110 GLN E CB  1 
ATOM   7590  C CG  . GLN E  2 76  ? 137.349 196.550 171.893 1.00 122.79 ? 110 GLN E CG  1 
ATOM   7591  C CD  . GLN E  2 76  ? 136.460 195.894 172.929 1.00 134.13 ? 110 GLN E CD  1 
ATOM   7592  O OE1 . GLN E  2 76  ? 136.927 195.113 173.758 1.00 140.79 ? 110 GLN E OE1 1 
ATOM   7593  N NE2 . GLN E  2 76  ? 135.169 196.201 172.881 1.00 138.16 ? 110 GLN E NE2 1 
ATOM   7594  N N   . ASN E  2 77  ? 139.777 200.231 172.841 1.00 132.27 ? 111 ASN E N   1 
ATOM   7595  C CA  . ASN E  2 77  ? 140.702 201.194 173.441 1.00 133.65 ? 111 ASN E CA  1 
ATOM   7596  C C   . ASN E  2 77  ? 141.755 201.663 172.443 1.00 134.86 ? 111 ASN E C   1 
ATOM   7597  O O   . ASN E  2 77  ? 142.958 201.617 172.708 1.00 138.84 ? 111 ASN E O   1 
ATOM   7598  C CB  . ASN E  2 77  ? 141.379 200.632 174.691 1.00 140.80 ? 111 ASN E CB  1 
ATOM   7599  C CG  . ASN E  2 77  ? 141.450 201.641 175.815 1.00 159.16 ? 111 ASN E CG  1 
ATOM   7600  O OD1 . ASN E  2 77  ? 141.939 202.750 175.604 1.00 159.91 ? 111 ASN E OD1 1 
ATOM   7601  N ND2 . ASN E  2 77  ? 141.016 201.262 177.014 1.00 170.17 ? 111 ASN E ND2 1 
ATOM   7602  N N   . VAL E  2 78  ? 141.296 202.118 171.275 1.00 130.43 ? 112 VAL E N   1 
ATOM   7603  C CA  . VAL E  2 78  ? 142.247 202.621 170.297 1.00 130.00 ? 112 VAL E CA  1 
ATOM   7604  C C   . VAL E  2 78  ? 142.936 203.873 170.847 1.00 135.16 ? 112 VAL E C   1 
ATOM   7605  O O   . VAL E  2 78  ? 142.341 204.694 171.558 1.00 138.82 ? 112 VAL E O   1 
ATOM   7606  C CB  . VAL E  2 78  ? 141.575 202.896 168.941 1.00 129.57 ? 112 VAL E CB  1 
ATOM   7607  C CG1 . VAL E  2 78  ? 140.837 204.230 168.942 1.00 135.33 ? 112 VAL E CG1 1 
ATOM   7608  C CG2 . VAL E  2 78  ? 142.606 202.846 167.821 1.00 129.82 ? 112 VAL E CG2 1 
ATOM   7609  N N   . THR E  2 79  ? 144.226 203.987 170.546 1.00 133.65 ? 113 THR E N   1 
ATOM   7610  C CA  . THR E  2 79  ? 145.036 205.116 170.973 1.00 134.85 ? 113 THR E CA  1 
ATOM   7611  C C   . THR E  2 79  ? 145.725 205.703 169.752 1.00 135.06 ? 113 THR E C   1 
ATOM   7612  O O   . THR E  2 79  ? 145.742 205.104 168.673 1.00 135.94 ? 113 THR E O   1 
ATOM   7613  C CB  . THR E  2 79  ? 146.072 204.712 172.032 1.00 134.32 ? 113 THR E CB  1 
ATOM   7614  O OG1 . THR E  2 79  ? 146.949 203.716 171.491 1.00 135.07 ? 113 THR E OG1 1 
ATOM   7615  C CG2 . THR E  2 79  ? 145.386 204.165 173.276 1.00 133.15 ? 113 THR E CG2 1 
ATOM   7616  N N   . GLN E  2 80  ? 146.304 206.892 169.932 1.00 133.28 ? 114 GLN E N   1 
ATOM   7617  C CA  . GLN E  2 80  ? 146.915 207.590 168.806 1.00 131.89 ? 114 GLN E CA  1 
ATOM   7618  C C   . GLN E  2 80  ? 148.148 206.852 168.299 1.00 131.68 ? 114 GLN E C   1 
ATOM   7619  O O   . GLN E  2 80  ? 148.620 207.106 167.185 1.00 135.67 ? 114 GLN E O   1 
ATOM   7620  C CB  . GLN E  2 80  ? 147.266 209.022 169.209 1.00 131.34 ? 114 GLN E CB  1 
ATOM   7621  C CG  . GLN E  2 80  ? 147.445 209.968 168.034 1.00 132.59 ? 114 GLN E CG  1 
ATOM   7622  C CD  . GLN E  2 80  ? 147.492 211.423 168.457 1.00 143.48 ? 114 GLN E CD  1 
ATOM   7623  O OE1 . GLN E  2 80  ? 147.923 211.748 169.563 1.00 150.63 ? 114 GLN E OE1 1 
ATOM   7624  N NE2 . GLN E  2 80  ? 147.039 212.308 167.577 1.00 143.46 ? 114 GLN E NE2 1 
ATOM   7625  N N   . ASN E  2 81  ? 148.686 205.933 169.104 1.00 129.83 ? 115 ASN E N   1 
ATOM   7626  C CA  . ASN E  2 81  ? 149.837 205.149 168.674 1.00 133.61 ? 115 ASN E CA  1 
ATOM   7627  C C   . ASN E  2 81  ? 149.456 204.059 167.680 1.00 133.66 ? 115 ASN E C   1 
ATOM   7628  O O   . ASN E  2 81  ? 150.335 203.530 166.991 1.00 136.72 ? 115 ASN E O   1 
ATOM   7629  C CB  . ASN E  2 81  ? 150.529 204.529 169.890 1.00 134.65 ? 115 ASN E CB  1 
ATOM   7630  C CG  . ASN E  2 81  ? 151.889 203.950 169.556 1.00 143.04 ? 115 ASN E CG  1 
ATOM   7631  O OD1 . ASN E  2 81  ? 152.073 202.733 169.548 1.00 147.84 ? 115 ASN E OD1 1 
ATOM   7632  N ND2 . ASN E  2 81  ? 152.851 204.822 169.278 1.00 139.14 ? 115 ASN E ND2 1 
ATOM   7633  N N   . ASP E  2 82  ? 148.172 203.713 167.586 1.00 128.13 ? 116 ASP E N   1 
ATOM   7634  C CA  . ASP E  2 82  ? 147.731 202.637 166.707 1.00 121.82 ? 116 ASP E CA  1 
ATOM   7635  C C   . ASP E  2 82  ? 147.614 203.056 165.248 1.00 118.67 ? 116 ASP E C   1 
ATOM   7636  O O   . ASP E  2 82  ? 147.442 202.185 164.389 1.00 117.71 ? 116 ASP E O   1 
ATOM   7637  C CB  . ASP E  2 82  ? 146.384 202.086 167.182 1.00 123.95 ? 116 ASP E CB  1 
ATOM   7638  C CG  . ASP E  2 82  ? 146.474 201.417 168.537 1.00 134.00 ? 116 ASP E CG  1 
ATOM   7639  O OD1 . ASP E  2 82  ? 146.915 200.250 168.595 1.00 133.98 ? 116 ASP E OD1 1 
ATOM   7640  O OD2 . ASP E  2 82  ? 146.098 202.053 169.544 1.00 139.51 ? 116 ASP E OD2 1 
ATOM   7641  N N   . THR E  2 83  ? 147.691 204.351 164.948 1.00 118.12 ? 117 THR E N   1 
ATOM   7642  C CA  . THR E  2 83  ? 147.545 204.820 163.575 1.00 116.86 ? 117 THR E CA  1 
ATOM   7643  C C   . THR E  2 83  ? 148.634 204.230 162.690 1.00 116.34 ? 117 THR E C   1 
ATOM   7644  O O   . THR E  2 83  ? 149.823 204.492 162.896 1.00 126.75 ? 117 THR E O   1 
ATOM   7645  C CB  . THR E  2 83  ? 147.599 206.346 163.532 1.00 119.66 ? 117 THR E CB  1 
ATOM   7646  O OG1 . THR E  2 83  ? 146.616 206.886 164.424 1.00 122.90 ? 117 THR E OG1 1 
ATOM   7647  C CG2 . THR E  2 83  ? 147.329 206.847 162.122 1.00 119.43 ? 117 THR E CG2 1 
ATOM   7648  N N   . GLY E  2 84  ? 148.228 203.436 161.707 1.00 109.04 ? 118 GLY E N   1 
ATOM   7649  C CA  . GLY E  2 84  ? 149.184 202.820 160.813 1.00 111.57 ? 118 GLY E CA  1 
ATOM   7650  C C   . GLY E  2 84  ? 148.504 201.814 159.907 1.00 111.35 ? 118 GLY E C   1 
ATOM   7651  O O   . GLY E  2 84  ? 147.275 201.719 159.861 1.00 111.29 ? 118 GLY E O   1 
ATOM   7652  N N   . PHE E  2 85  ? 149.333 201.069 159.185 1.00 107.02 ? 119 PHE E N   1 
ATOM   7653  C CA  . PHE E  2 85  ? 148.860 200.049 158.264 1.00 101.88 ? 119 PHE E CA  1 
ATOM   7654  C C   . PHE E  2 85  ? 148.781 198.695 158.957 1.00 101.95 ? 119 PHE E C   1 
ATOM   7655  O O   . PHE E  2 85  ? 149.590 198.373 159.831 1.00 103.97 ? 119 PHE E O   1 
ATOM   7656  C CB  . PHE E  2 85  ? 149.779 199.952 157.045 1.00 103.50 ? 119 PHE E CB  1 
ATOM   7657  C CG  . PHE E  2 85  ? 149.749 201.168 156.165 1.00 109.54 ? 119 PHE E CG  1 
ATOM   7658  C CD1 . PHE E  2 85  ? 150.509 202.283 156.473 1.00 111.26 ? 119 PHE E CD1 1 
ATOM   7659  C CD2 . PHE E  2 85  ? 148.966 201.192 155.024 1.00 115.99 ? 119 PHE E CD2 1 
ATOM   7660  C CE1 . PHE E  2 85  ? 150.484 203.402 155.663 1.00 116.58 ? 119 PHE E CE1 1 
ATOM   7661  C CE2 . PHE E  2 85  ? 148.938 202.307 154.210 1.00 122.07 ? 119 PHE E CE2 1 
ATOM   7662  C CZ  . PHE E  2 85  ? 149.697 203.413 154.530 1.00 121.51 ? 119 PHE E CZ  1 
ATOM   7663  N N   . TYR E  2 86  ? 147.786 197.906 158.563 1.00 101.45 ? 120 TYR E N   1 
ATOM   7664  C CA  . TYR E  2 86  ? 147.622 196.543 159.047 1.00 95.99  ? 120 TYR E CA  1 
ATOM   7665  C C   . TYR E  2 86  ? 147.453 195.610 157.860 1.00 96.45  ? 120 TYR E C   1 
ATOM   7666  O O   . TYR E  2 86  ? 146.716 195.917 156.919 1.00 101.93 ? 120 TYR E O   1 
ATOM   7667  C CB  . TYR E  2 86  ? 146.420 196.415 159.990 1.00 91.58  ? 120 TYR E CB  1 
ATOM   7668  C CG  . TYR E  2 86  ? 146.552 197.204 161.272 1.00 97.69  ? 120 TYR E CG  1 
ATOM   7669  C CD1 . TYR E  2 86  ? 146.380 198.580 161.287 1.00 100.87 ? 120 TYR E CD1 1 
ATOM   7670  C CD2 . TYR E  2 86  ? 146.850 196.569 162.468 1.00 100.07 ? 120 TYR E CD2 1 
ATOM   7671  C CE1 . TYR E  2 86  ? 146.504 199.301 162.456 1.00 103.99 ? 120 TYR E CE1 1 
ATOM   7672  C CE2 . TYR E  2 86  ? 146.973 197.281 163.643 1.00 103.11 ? 120 TYR E CE2 1 
ATOM   7673  C CZ  . TYR E  2 86  ? 146.799 198.647 163.631 1.00 104.88 ? 120 TYR E CZ  1 
ATOM   7674  O OH  . TYR E  2 86  ? 146.921 199.363 164.798 1.00 114.74 ? 120 TYR E OH  1 
ATOM   7675  N N   . THR E  2 87  ? 148.134 194.469 157.910 1.00 91.69  ? 121 THR E N   1 
ATOM   7676  C CA  . THR E  2 87  ? 148.099 193.490 156.836 1.00 96.28  ? 121 THR E CA  1 
ATOM   7677  C C   . THR E  2 87  ? 147.465 192.200 157.332 1.00 93.61  ? 121 THR E C   1 
ATOM   7678  O O   . THR E  2 87  ? 147.751 191.743 158.443 1.00 95.77  ? 121 THR E O   1 
ATOM   7679  C CB  . THR E  2 87  ? 149.501 193.198 156.296 1.00 103.27 ? 121 THR E CB  1 
ATOM   7680  O OG1 . THR E  2 87  ? 150.382 192.898 157.385 1.00 106.54 ? 121 THR E OG1 1 
ATOM   7681  C CG2 . THR E  2 87  ? 150.034 194.394 155.527 1.00 108.10 ? 121 THR E CG2 1 
ATOM   7682  N N   . LEU E  2 88  ? 146.605 191.621 156.503 1.00 89.02  ? 122 LEU E N   1 
ATOM   7683  C CA  . LEU E  2 88  ? 145.947 190.358 156.799 1.00 87.73  ? 122 LEU E CA  1 
ATOM   7684  C C   . LEU E  2 88  ? 146.557 189.266 155.934 1.00 90.97  ? 122 LEU E C   1 
ATOM   7685  O O   . LEU E  2 88  ? 146.634 189.409 154.709 1.00 97.68  ? 122 LEU E O   1 
ATOM   7686  C CB  . LEU E  2 88  ? 144.441 190.451 156.548 1.00 88.04  ? 122 LEU E CB  1 
ATOM   7687  C CG  . LEU E  2 88  ? 143.698 189.124 156.378 1.00 85.03  ? 122 LEU E CG  1 
ATOM   7688  C CD1 . LEU E  2 88  ? 143.704 188.328 157.673 1.00 86.68  ? 122 LEU E CD1 1 
ATOM   7689  C CD2 . LEU E  2 88  ? 142.276 189.358 155.899 1.00 93.75  ? 122 LEU E CD2 1 
ATOM   7690  N N   . GLN E  2 89  ? 146.990 188.183 156.570 1.00 90.83  ? 123 GLN E N   1 
ATOM   7691  C CA  . GLN E  2 89  ? 147.497 187.010 155.873 1.00 93.91  ? 123 GLN E CA  1 
ATOM   7692  C C   . GLN E  2 89  ? 146.427 185.932 155.896 1.00 95.85  ? 123 GLN E C   1 
ATOM   7693  O O   . GLN E  2 89  ? 145.952 185.547 156.970 1.00 101.23 ? 123 GLN E O   1 
ATOM   7694  C CB  . GLN E  2 89  ? 148.785 186.492 156.510 1.00 95.59  ? 123 GLN E CB  1 
ATOM   7695  C CG  . GLN E  2 89  ? 149.396 185.325 155.754 1.00 101.16 ? 123 GLN E CG  1 
ATOM   7696  C CD  . GLN E  2 89  ? 150.823 185.040 156.165 1.00 113.05 ? 123 GLN E CD  1 
ATOM   7697  O OE1 . GLN E  2 89  ? 151.742 185.122 155.351 1.00 117.59 ? 123 GLN E OE1 1 
ATOM   7698  N NE2 . GLN E  2 89  ? 151.016 184.695 157.432 1.00 111.66 ? 123 GLN E NE2 1 
ATOM   7699  N N   . VAL E  2 90  ? 146.051 185.450 154.718 1.00 92.22  ? 124 VAL E N   1 
ATOM   7700  C CA  . VAL E  2 90  ? 145.081 184.373 154.575 1.00 88.17  ? 124 VAL E CA  1 
ATOM   7701  C C   . VAL E  2 90  ? 145.794 183.173 153.977 1.00 95.13  ? 124 VAL E C   1 
ATOM   7702  O O   . VAL E  2 90  ? 146.395 183.273 152.901 1.00 101.27 ? 124 VAL E O   1 
ATOM   7703  C CB  . VAL E  2 90  ? 143.886 184.796 153.704 1.00 86.50  ? 124 VAL E CB  1 
ATOM   7704  C CG1 . VAL E  2 90  ? 143.037 183.593 153.362 1.00 93.23  ? 124 VAL E CG1 1 
ATOM   7705  C CG2 . VAL E  2 90  ? 143.054 185.835 154.430 1.00 90.01  ? 124 VAL E CG2 1 
ATOM   7706  N N   . ILE E  2 91  ? 145.733 182.045 154.675 1.00 93.88  ? 125 ILE E N   1 
ATOM   7707  C CA  . ILE E  2 91  ? 146.350 180.805 154.224 1.00 95.60  ? 125 ILE E CA  1 
ATOM   7708  C C   . ILE E  2 91  ? 145.251 179.888 153.712 1.00 98.51  ? 125 ILE E C   1 
ATOM   7709  O O   . ILE E  2 91  ? 144.377 179.463 154.475 1.00 107.52 ? 125 ILE E O   1 
ATOM   7710  C CB  . ILE E  2 91  ? 147.160 180.139 155.345 1.00 94.58  ? 125 ILE E CB  1 
ATOM   7711  C CG1 . ILE E  2 91  ? 148.295 181.060 155.788 1.00 99.69  ? 125 ILE E CG1 1 
ATOM   7712  C CG2 . ILE E  2 91  ? 147.704 178.802 154.889 1.00 100.83 ? 125 ILE E CG2 1 
ATOM   7713  C CD1 . ILE E  2 91  ? 148.988 180.611 157.043 1.00 108.77 ? 125 ILE E CD1 1 
ATOM   7714  N N   . LYS E  2 92  ? 145.297 179.585 152.419 1.00 94.43  ? 126 LYS E N   1 
ATOM   7715  C CA  . LYS E  2 92  ? 144.282 178.767 151.784 1.00 103.88 ? 126 LYS E CA  1 
ATOM   7716  C C   . LYS E  2 92  ? 144.489 177.295 152.136 1.00 108.79 ? 126 LYS E C   1 
ATOM   7717  O O   . LYS E  2 92  ? 145.395 176.927 152.888 1.00 109.06 ? 126 LYS E O   1 
ATOM   7718  C CB  . LYS E  2 92  ? 144.307 178.983 150.272 1.00 106.34 ? 126 LYS E CB  1 
ATOM   7719  C CG  . LYS E  2 92  ? 144.480 180.446 149.883 1.00 108.87 ? 126 LYS E CG  1 
ATOM   7720  C CD  . LYS E  2 92  ? 144.882 180.615 148.426 1.00 109.59 ? 126 LYS E CD  1 
ATOM   7721  C CE  . LYS E  2 92  ? 144.080 179.707 147.512 1.00 118.71 ? 126 LYS E CE  1 
ATOM   7722  N NZ  . LYS E  2 92  ? 142.623 180.009 147.577 1.00 123.49 ? 126 LYS E NZ  1 
ATOM   7723  N N   . SER E  2 93  ? 143.619 176.444 151.583 1.00 111.53 ? 127 SER E N   1 
ATOM   7724  C CA  . SER E  2 93  ? 143.674 175.020 151.898 1.00 108.05 ? 127 SER E CA  1 
ATOM   7725  C C   . SER E  2 93  ? 144.991 174.395 151.460 1.00 108.68 ? 127 SER E C   1 
ATOM   7726  O O   . SER E  2 93  ? 145.568 173.586 152.196 1.00 105.54 ? 127 SER E O   1 
ATOM   7727  C CB  . SER E  2 93  ? 142.501 174.292 151.245 1.00 114.84 ? 127 SER E CB  1 
ATOM   7728  O OG  . SER E  2 93  ? 142.366 174.666 149.886 1.00 122.40 ? 127 SER E OG  1 
ATOM   7729  N N   . ASP E  2 94  ? 145.484 174.754 150.278 1.00 107.18 ? 128 ASP E N   1 
ATOM   7730  C CA  . ASP E  2 94  ? 146.775 174.285 149.796 1.00 105.16 ? 128 ASP E CA  1 
ATOM   7731  C C   . ASP E  2 94  ? 147.944 174.995 150.463 1.00 104.88 ? 128 ASP E C   1 
ATOM   7732  O O   . ASP E  2 94  ? 149.094 174.780 150.065 1.00 105.63 ? 128 ASP E O   1 
ATOM   7733  C CB  . ASP E  2 94  ? 146.856 174.433 148.273 1.00 108.87 ? 128 ASP E CB  1 
ATOM   7734  C CG  . ASP E  2 94  ? 146.615 175.858 147.800 1.00 116.97 ? 128 ASP E CG  1 
ATOM   7735  O OD1 . ASP E  2 94  ? 146.966 176.814 148.522 1.00 117.23 ? 128 ASP E OD1 1 
ATOM   7736  O OD2 . ASP E  2 94  ? 146.070 176.021 146.689 1.00 122.80 ? 128 ASP E OD2 1 
ATOM   7737  N N   . LEU E  2 95  ? 147.670 175.847 151.451 1.00 104.84 ? 129 LEU E N   1 
ATOM   7738  C CA  . LEU E  2 95  ? 148.655 176.549 152.266 1.00 103.75 ? 129 LEU E CA  1 
ATOM   7739  C C   . LEU E  2 95  ? 149.455 177.577 151.479 1.00 104.78 ? 129 LEU E C   1 
ATOM   7740  O O   . LEU E  2 95  ? 150.602 177.868 151.840 1.00 103.70 ? 129 LEU E O   1 
ATOM   7741  C CB  . LEU E  2 95  ? 149.604 175.570 152.967 1.00 100.37 ? 129 LEU E CB  1 
ATOM   7742  C CG  . LEU E  2 95  ? 149.248 175.261 154.421 1.00 104.92 ? 129 LEU E CG  1 
ATOM   7743  C CD1 . LEU E  2 95  ? 147.800 174.825 154.542 1.00 109.80 ? 129 LEU E CD1 1 
ATOM   7744  C CD2 . LEU E  2 95  ? 150.152 174.173 154.945 1.00 108.04 ? 129 LEU E CD2 1 
ATOM   7745  N N   . VAL E  2 96  ? 148.886 178.136 150.416 1.00 105.71 ? 130 VAL E N   1 
ATOM   7746  C CA  . VAL E  2 96  ? 149.502 179.258 149.717 1.00 105.55 ? 130 VAL E CA  1 
ATOM   7747  C C   . VAL E  2 96  ? 148.952 180.553 150.298 1.00 107.62 ? 130 VAL E C   1 
ATOM   7748  O O   . VAL E  2 96  ? 147.734 180.765 150.331 1.00 108.09 ? 130 VAL E O   1 
ATOM   7749  C CB  . VAL E  2 96  ? 149.243 179.169 148.206 1.00 103.17 ? 130 VAL E CB  1 
ATOM   7750  C CG1 . VAL E  2 96  ? 149.718 180.435 147.512 1.00 105.38 ? 130 VAL E CG1 1 
ATOM   7751  C CG2 . VAL E  2 96  ? 149.935 177.947 147.624 1.00 103.37 ? 130 VAL E CG2 1 
ATOM   7752  N N   . ASN E  2 97  ? 149.847 181.420 150.759 1.00 106.23 ? 131 ASN E N   1 
ATOM   7753  C CA  . ASN E  2 97  ? 149.442 182.628 151.463 1.00 101.71 ? 131 ASN E CA  1 
ATOM   7754  C C   . ASN E  2 97  ? 148.833 183.646 150.508 1.00 102.49 ? 131 ASN E C   1 
ATOM   7755  O O   . ASN E  2 97  ? 149.238 183.756 149.348 1.00 106.44 ? 131 ASN E O   1 
ATOM   7756  C CB  . ASN E  2 97  ? 150.640 183.244 152.183 1.00 105.68 ? 131 ASN E CB  1 
ATOM   7757  C CG  . ASN E  2 97  ? 151.253 182.304 153.200 1.00 110.43 ? 131 ASN E CG  1 
ATOM   7758  O OD1 . ASN E  2 97  ? 151.099 181.087 153.107 1.00 108.99 ? 131 ASN E OD1 1 
ATOM   7759  N ND2 . ASN E  2 97  ? 151.957 182.864 154.176 1.00 108.93 ? 131 ASN E ND2 1 
ATOM   7760  N N   . GLU E  2 98  ? 147.850 184.390 151.009 1.00 100.64 ? 132 GLU E N   1 
ATOM   7761  C CA  . GLU E  2 98  ? 147.254 185.511 150.295 1.00 101.23 ? 132 GLU E CA  1 
ATOM   7762  C C   . GLU E  2 98  ? 147.276 186.722 151.212 1.00 105.43 ? 132 GLU E C   1 
ATOM   7763  O O   . GLU E  2 98  ? 147.041 186.593 152.418 1.00 110.37 ? 132 GLU E O   1 
ATOM   7764  C CB  . GLU E  2 98  ? 145.823 185.199 149.849 1.00 101.99 ? 132 GLU E CB  1 
ATOM   7765  C CG  . GLU E  2 98  ? 145.383 185.972 148.618 1.00 114.14 ? 132 GLU E CG  1 
ATOM   7766  C CD  . GLU E  2 98  ? 144.253 185.292 147.875 1.00 124.36 ? 132 GLU E CD  1 
ATOM   7767  O OE1 . GLU E  2 98  ? 143.996 184.100 148.142 1.00 119.27 ? 132 GLU E OE1 1 
ATOM   7768  O OE2 . GLU E  2 98  ? 143.620 185.950 147.022 1.00 127.21 ? 132 GLU E OE2 1 
ATOM   7769  N N   . GLU E  2 99  ? 147.557 187.892 150.647 1.00 106.33 ? 133 GLU E N   1 
ATOM   7770  C CA  . GLU E  2 99  ? 147.830 189.083 151.434 1.00 106.85 ? 133 GLU E CA  1 
ATOM   7771  C C   . GLU E  2 99  ? 146.859 190.204 151.089 1.00 111.09 ? 133 GLU E C   1 
ATOM   7772  O O   . GLU E  2 99  ? 146.376 190.320 149.960 1.00 117.49 ? 133 GLU E O   1 
ATOM   7773  C CB  . GLU E  2 99  ? 149.269 189.562 151.216 1.00 108.27 ? 133 GLU E CB  1 
ATOM   7774  C CG  . GLU E  2 99  ? 150.318 188.520 151.550 1.00 120.81 ? 133 GLU E CG  1 
ATOM   7775  C CD  . GLU E  2 99  ? 151.135 188.893 152.766 1.00 133.25 ? 133 GLU E CD  1 
ATOM   7776  O OE1 . GLU E  2 99  ? 151.866 188.022 153.282 1.00 137.73 ? 133 GLU E OE1 1 
ATOM   7777  O OE2 . GLU E  2 99  ? 151.047 190.060 153.201 1.00 137.29 ? 133 GLU E OE2 1 
ATOM   7778  N N   . ALA E  2 100 ? 146.585 191.034 152.093 1.00 106.72 ? 134 ALA E N   1 
ATOM   7779  C CA  . ALA E  2 100 ? 145.784 192.237 151.929 1.00 103.24 ? 134 ALA E CA  1 
ATOM   7780  C C   . ALA E  2 100 ? 146.272 193.266 152.938 1.00 103.28 ? 134 ALA E C   1 
ATOM   7781  O O   . ALA E  2 100 ? 147.132 192.982 153.774 1.00 109.17 ? 134 ALA E O   1 
ATOM   7782  C CB  . ALA E  2 100 ? 144.290 191.954 152.106 1.00 106.48 ? 134 ALA E CB  1 
ATOM   7783  N N   . THR E  2 101 ? 145.714 194.471 152.857 1.00 101.16 ? 135 THR E N   1 
ATOM   7784  C CA  . THR E  2 101 ? 146.143 195.557 153.724 1.00 101.28 ? 135 THR E CA  1 
ATOM   7785  C C   . THR E  2 101 ? 144.964 196.461 154.053 1.00 101.30 ? 135 THR E C   1 
ATOM   7786  O O   . THR E  2 101 ? 143.950 196.482 153.352 1.00 107.03 ? 135 THR E O   1 
ATOM   7787  C CB  . THR E  2 101 ? 147.273 196.378 153.087 1.00 105.91 ? 135 THR E CB  1 
ATOM   7788  O OG1 . THR E  2 101 ? 147.838 197.257 154.068 1.00 107.80 ? 135 THR E OG1 1 
ATOM   7789  C CG2 . THR E  2 101 ? 146.747 197.198 151.920 1.00 106.83 ? 135 THR E CG2 1 
ATOM   7790  N N   . GLY E  2 102 ? 145.116 197.206 155.144 1.00 97.31  ? 136 GLY E N   1 
ATOM   7791  C CA  . GLY E  2 102 ? 144.113 198.162 155.571 1.00 98.57  ? 136 GLY E CA  1 
ATOM   7792  C C   . GLY E  2 102 ? 144.705 199.112 156.583 1.00 103.46 ? 136 GLY E C   1 
ATOM   7793  O O   . GLY E  2 102 ? 145.711 198.809 157.232 1.00 108.29 ? 136 GLY E O   1 
ATOM   7794  N N   . GLN E  2 103 ? 144.067 200.272 156.719 1.00 101.22 ? 137 GLN E N   1 
ATOM   7795  C CA  . GLN E  2 103 ? 144.599 201.315 157.581 1.00 106.02 ? 137 GLN E CA  1 
ATOM   7796  C C   . GLN E  2 103 ? 143.461 202.159 158.132 1.00 110.08 ? 137 GLN E C   1 
ATOM   7797  O O   . GLN E  2 103 ? 142.352 202.174 157.594 1.00 113.11 ? 137 GLN E O   1 
ATOM   7798  C CB  . GLN E  2 103 ? 145.595 202.207 156.831 1.00 111.71 ? 137 GLN E CB  1 
ATOM   7799  C CG  . GLN E  2 103 ? 144.944 203.124 155.810 1.00 114.38 ? 137 GLN E CG  1 
ATOM   7800  C CD  . GLN E  2 103 ? 145.949 203.774 154.883 1.00 125.74 ? 137 GLN E CD  1 
ATOM   7801  O OE1 . GLN E  2 103 ? 146.010 203.458 153.695 1.00 129.34 ? 137 GLN E OE1 1 
ATOM   7802  N NE2 . GLN E  2 103 ? 146.747 204.687 155.422 1.00 127.07 ? 137 GLN E NE2 1 
ATOM   7803  N N   . PHE E  2 104 ? 143.758 202.864 159.221 1.00 108.85 ? 138 PHE E N   1 
ATOM   7804  C CA  . PHE E  2 104 ? 142.825 203.811 159.811 1.00 111.41 ? 138 PHE E CA  1 
ATOM   7805  C C   . PHE E  2 104 ? 143.621 204.863 160.568 1.00 114.43 ? 138 PHE E C   1 
ATOM   7806  O O   . PHE E  2 104 ? 144.767 204.634 160.962 1.00 117.82 ? 138 PHE E O   1 
ATOM   7807  C CB  . PHE E  2 104 ? 141.814 203.116 160.731 1.00 108.61 ? 138 PHE E CB  1 
ATOM   7808  C CG  . PHE E  2 104 ? 142.440 202.362 161.870 1.00 103.40 ? 138 PHE E CG  1 
ATOM   7809  C CD1 . PHE E  2 104 ? 142.728 202.995 163.067 1.00 105.47 ? 138 PHE E CD1 1 
ATOM   7810  C CD2 . PHE E  2 104 ? 142.729 201.015 161.746 1.00 103.03 ? 138 PHE E CD2 1 
ATOM   7811  C CE1 . PHE E  2 104 ? 143.299 202.300 164.114 1.00 107.62 ? 138 PHE E CE1 1 
ATOM   7812  C CE2 . PHE E  2 104 ? 143.298 200.316 162.791 1.00 100.80 ? 138 PHE E CE2 1 
ATOM   7813  C CZ  . PHE E  2 104 ? 143.584 200.959 163.975 1.00 104.90 ? 138 PHE E CZ  1 
ATOM   7814  N N   . HIS E  2 105 ? 142.997 206.019 160.765 1.00 115.85 ? 139 HIS E N   1 
ATOM   7815  C CA  . HIS E  2 105 ? 143.616 207.140 161.456 1.00 117.71 ? 139 HIS E CA  1 
ATOM   7816  C C   . HIS E  2 105 ? 142.905 207.395 162.777 1.00 121.14 ? 139 HIS E C   1 
ATOM   7817  O O   . HIS E  2 105 ? 141.674 207.339 162.851 1.00 126.56 ? 139 HIS E O   1 
ATOM   7818  C CB  . HIS E  2 105 ? 143.584 208.406 160.596 1.00 122.44 ? 139 HIS E CB  1 
ATOM   7819  C CG  . HIS E  2 105 ? 144.703 208.494 159.607 1.00 129.20 ? 139 HIS E CG  1 
ATOM   7820  N ND1 . HIS E  2 105 ? 144.668 207.860 158.383 1.00 131.74 ? 139 HIS E ND1 1 
ATOM   7821  C CD2 . HIS E  2 105 ? 145.890 209.144 159.659 1.00 131.02 ? 139 HIS E CD2 1 
ATOM   7822  C CE1 . HIS E  2 105 ? 145.784 208.115 157.725 1.00 134.55 ? 139 HIS E CE1 1 
ATOM   7823  N NE2 . HIS E  2 105 ? 146.543 208.892 158.477 1.00 140.99 ? 139 HIS E NE2 1 
ATOM   7824  N N   . VAL E  2 106 ? 143.688 207.674 163.815 1.00 117.66 ? 140 VAL E N   1 
ATOM   7825  C CA  . VAL E  2 106 ? 143.174 207.969 165.146 1.00 118.84 ? 140 VAL E CA  1 
ATOM   7826  C C   . VAL E  2 106 ? 143.393 209.449 165.418 1.00 122.92 ? 140 VAL E C   1 
ATOM   7827  O O   . VAL E  2 106 ? 144.490 209.972 165.190 1.00 128.81 ? 140 VAL E O   1 
ATOM   7828  C CB  . VAL E  2 106 ? 143.858 207.105 166.219 1.00 120.24 ? 140 VAL E CB  1 
ATOM   7829  C CG1 . VAL E  2 106 ? 143.157 207.268 167.556 1.00 128.99 ? 140 VAL E CG1 1 
ATOM   7830  C CG2 . VAL E  2 106 ? 143.874 205.649 165.791 1.00 119.95 ? 140 VAL E CG2 1 
ATOM   7831  N N   . TYR E  2 107 ? 142.354 210.121 165.901 1.00 125.87 ? 141 TYR E N   1 
ATOM   7832  C CA  . TYR E  2 107 ? 142.408 211.553 166.132 1.00 137.27 ? 141 TYR E CA  1 
ATOM   7833  C C   . TYR E  2 107 ? 141.922 211.872 167.538 1.00 146.02 ? 141 TYR E C   1 
ATOM   7834  O O   . TYR E  2 107 ? 141.100 211.139 168.096 1.00 144.98 ? 141 TYR E O   1 
ATOM   7835  C CB  . TYR E  2 107 ? 141.556 212.302 165.098 1.00 140.71 ? 141 TYR E CB  1 
ATOM   7836  C CG  . TYR E  2 107 ? 142.137 212.250 163.703 1.00 138.14 ? 141 TYR E CG  1 
ATOM   7837  C CD1 . TYR E  2 107 ? 143.349 212.861 163.412 1.00 145.22 ? 141 TYR E CD1 1 
ATOM   7838  C CD2 . TYR E  2 107 ? 141.480 211.581 162.680 1.00 136.60 ? 141 TYR E CD2 1 
ATOM   7839  C CE1 . TYR E  2 107 ? 143.886 212.813 162.140 1.00 145.60 ? 141 TYR E CE1 1 
ATOM   7840  C CE2 . TYR E  2 107 ? 142.010 211.528 161.405 1.00 133.32 ? 141 TYR E CE2 1 
ATOM   7841  C CZ  . TYR E  2 107 ? 143.212 212.145 161.141 1.00 135.67 ? 141 TYR E CZ  1 
ATOM   7842  O OH  . TYR E  2 107 ? 143.744 212.095 159.873 1.00 135.42 ? 141 TYR E OH  1 
ATOM   7843  N N   . PRO E  2 108 ? 142.414 212.955 168.135 1.00 150.56 ? 142 PRO E N   1 
ATOM   7844  C CA  . PRO E  2 108 ? 142.065 213.251 169.526 1.00 156.27 ? 142 PRO E CA  1 
ATOM   7845  C C   . PRO E  2 108 ? 140.760 214.022 169.641 1.00 166.95 ? 142 PRO E C   1 
ATOM   7846  O O   . PRO E  2 108 ? 140.205 214.526 168.662 1.00 170.95 ? 142 PRO E O   1 
ATOM   7847  C CB  . PRO E  2 108 ? 143.248 214.091 170.005 1.00 154.85 ? 142 PRO E CB  1 
ATOM   7848  C CG  . PRO E  2 108 ? 143.645 214.852 168.782 1.00 156.02 ? 142 PRO E CG  1 
ATOM   7849  C CD  . PRO E  2 108 ? 143.369 213.941 167.596 1.00 150.86 ? 142 PRO E CD  1 
ATOM   7850  N N   . GLU E  2 109 ? 140.276 214.111 170.879 1.00 173.69 ? 143 GLU E N   1 
ATOM   7851  C CA  . GLU E  2 109 ? 139.018 214.786 171.196 1.00 188.88 ? 143 GLU E CA  1 
ATOM   7852  C C   . GLU E  2 109 ? 139.301 216.271 171.386 1.00 202.47 ? 143 GLU E C   1 
ATOM   7853  O O   . GLU E  2 109 ? 139.728 216.702 172.460 1.00 212.62 ? 143 GLU E O   1 
ATOM   7854  C CB  . GLU E  2 109 ? 138.380 214.179 172.441 1.00 196.99 ? 143 GLU E CB  1 
ATOM   7855  C CG  . GLU E  2 109 ? 138.303 212.648 172.488 1.00 188.05 ? 143 GLU E CG  1 
ATOM   7856  C CD  . GLU E  2 109 ? 138.103 211.978 171.133 1.00 177.20 ? 143 GLU E CD  1 
ATOM   7857  O OE1 . GLU E  2 109 ? 138.695 210.897 170.926 1.00 171.41 ? 143 GLU E OE1 1 
ATOM   7858  O OE2 . GLU E  2 109 ? 137.319 212.486 170.302 1.00 180.13 ? 143 GLU E OE2 1 
ATOM   7859  N N   . LEU E  2 110 ? 139.063 217.056 170.339 1.00 203.58 ? 144 LEU E N   1 
ATOM   7860  C CA  . LEU E  2 110 ? 139.348 218.480 170.390 1.00 213.24 ? 144 LEU E CA  1 
ATOM   7861  C C   . LEU E  2 110 ? 138.363 219.199 171.315 1.00 226.25 ? 144 LEU E C   1 
ATOM   7862  O O   . LEU E  2 110 ? 137.147 219.039 171.187 1.00 230.59 ? 144 LEU E O   1 
ATOM   7863  C CB  . LEU E  2 110 ? 139.288 219.083 168.990 1.00 210.85 ? 144 LEU E CB  1 
ATOM   7864  C CG  . LEU E  2 110 ? 140.390 218.653 168.017 1.00 205.20 ? 144 LEU E CG  1 
ATOM   7865  C CD1 . LEU E  2 110 ? 140.350 219.494 166.753 1.00 209.84 ? 144 LEU E CD1 1 
ATOM   7866  C CD2 . LEU E  2 110 ? 141.759 218.733 168.677 1.00 209.07 ? 144 LEU E CD2 1 
ATOM   7867  N N   . PRO E  2 111 ? 138.866 219.998 172.252 1.00 230.49 ? 145 PRO E N   1 
ATOM   7868  C CA  . PRO E  2 111 ? 138.004 220.675 173.224 1.00 237.23 ? 145 PRO E CA  1 
ATOM   7869  C C   . PRO E  2 111 ? 137.415 221.975 172.682 1.00 243.33 ? 145 PRO E C   1 
ATOM   7870  O O   . PRO E  2 111 ? 137.531 222.292 171.496 1.00 243.05 ? 145 PRO E O   1 
ATOM   7871  C CB  . PRO E  2 111 ? 138.971 220.957 174.380 1.00 235.36 ? 145 PRO E CB  1 
ATOM   7872  C CG  . PRO E  2 111 ? 140.285 221.166 173.700 1.00 230.29 ? 145 PRO E CG  1 
ATOM   7873  C CD  . PRO E  2 111 ? 140.296 220.230 172.519 1.00 224.52 ? 145 PRO E CD  1 
ATOM   7874  N N   . LYS E  2 112 ? 136.755 222.721 173.578 1.00 246.45 ? 146 LYS E N   1 
ATOM   7875  C CA  . LYS E  2 112 ? 136.506 224.129 173.285 1.00 250.77 ? 146 LYS E CA  1 
ATOM   7876  C C   . LYS E  2 112 ? 137.832 224.822 172.995 1.00 251.79 ? 146 LYS E C   1 
ATOM   7877  O O   . LYS E  2 112 ? 138.797 224.644 173.751 1.00 248.75 ? 146 LYS E O   1 
ATOM   7878  C CB  . LYS E  2 112 ? 135.813 224.907 174.418 1.00 252.30 ? 146 LYS E CB  1 
ATOM   7879  C CG  . LYS E  2 112 ? 134.602 224.394 175.220 1.00 251.17 ? 146 LYS E CG  1 
ATOM   7880  C CD  . LYS E  2 112 ? 133.592 223.541 174.483 1.00 251.13 ? 146 LYS E CD  1 
ATOM   7881  C CE  . LYS E  2 112 ? 133.487 222.173 175.091 1.00 249.30 ? 146 LYS E CE  1 
ATOM   7882  N NZ  . LYS E  2 112 ? 132.241 221.486 174.659 1.00 248.06 ? 146 LYS E NZ  1 
ATOM   7883  N N   . PRO E  2 113 ? 137.926 225.600 171.926 1.00 257.10 ? 147 PRO E N   1 
ATOM   7884  C CA  . PRO E  2 113 ? 139.059 226.517 171.789 1.00 262.26 ? 147 PRO E CA  1 
ATOM   7885  C C   . PRO E  2 113 ? 138.783 227.821 172.518 1.00 268.36 ? 147 PRO E C   1 
ATOM   7886  O O   . PRO E  2 113 ? 137.759 227.951 173.194 1.00 267.42 ? 147 PRO E O   1 
ATOM   7887  C CB  . PRO E  2 113 ? 139.176 226.711 170.273 1.00 262.67 ? 147 PRO E CB  1 
ATOM   7888  C CG  . PRO E  2 113 ? 137.793 226.428 169.734 1.00 259.90 ? 147 PRO E CG  1 
ATOM   7889  C CD  . PRO E  2 113 ? 136.993 225.698 170.791 1.00 257.94 ? 147 PRO E CD  1 
ATOM   7890  N N   . SER E  2 114 ? 139.693 228.783 172.408 1.00 274.84 ? 148 SER E N   1 
ATOM   7891  C CA  . SER E  2 114 ? 139.492 230.104 172.982 1.00 284.67 ? 148 SER E CA  1 
ATOM   7892  C C   . SER E  2 114 ? 140.209 231.118 172.105 1.00 291.67 ? 148 SER E C   1 
ATOM   7893  O O   . SER E  2 114 ? 141.140 230.780 171.371 1.00 292.16 ? 148 SER E O   1 
ATOM   7894  C CB  . SER E  2 114 ? 139.989 230.181 174.433 1.00 287.11 ? 148 SER E CB  1 
ATOM   7895  O OG  . SER E  2 114 ? 141.357 229.832 174.530 1.00 288.28 ? 148 SER E OG  1 
ATOM   7896  N N   . ILE E  2 115 ? 139.768 232.369 172.191 1.00 295.97 ? 149 ILE E N   1 
ATOM   7897  C CA  . ILE E  2 115 ? 140.199 233.423 171.282 1.00 300.86 ? 149 ILE E CA  1 
ATOM   7898  C C   . ILE E  2 115 ? 140.846 234.537 172.091 1.00 305.52 ? 149 ILE E C   1 
ATOM   7899  O O   . ILE E  2 115 ? 140.513 234.743 173.263 1.00 305.49 ? 149 ILE E O   1 
ATOM   7900  C CB  . ILE E  2 115 ? 139.026 233.973 170.441 1.00 299.62 ? 149 ILE E CB  1 
ATOM   7901  C CG1 . ILE E  2 115 ? 138.077 232.848 170.021 1.00 294.15 ? 149 ILE E CG1 1 
ATOM   7902  C CG2 . ILE E  2 115 ? 139.538 234.702 169.210 1.00 305.39 ? 149 ILE E CG2 1 
ATOM   7903  C CD1 . ILE E  2 115 ? 136.890 232.667 170.938 1.00 289.12 ? 149 ILE E CD1 1 
ATOM   7904  N N   . SER E  2 116 ? 141.772 235.254 171.457 1.00 309.47 ? 150 SER E N   1 
ATOM   7905  C CA  . SER E  2 116 ? 142.471 236.370 172.075 1.00 313.74 ? 150 SER E CA  1 
ATOM   7906  C C   . SER E  2 116 ? 142.589 237.514 171.078 1.00 319.49 ? 150 SER E C   1 
ATOM   7907  O O   . SER E  2 116 ? 142.626 237.301 169.863 1.00 318.97 ? 150 SER E O   1 
ATOM   7908  C CB  . SER E  2 116 ? 143.866 235.957 172.562 1.00 311.95 ? 150 SER E CB  1 
ATOM   7909  O OG  . SER E  2 116 ? 144.511 235.124 171.613 1.00 308.02 ? 150 SER E OG  1 
ATOM   7910  N N   . SER E  2 117 ? 142.643 238.732 171.608 1.00 324.57 ? 151 SER E N   1 
ATOM   7911  C CA  . SER E  2 117 ? 142.805 239.943 170.817 1.00 331.23 ? 151 SER E CA  1 
ATOM   7912  C C   . SER E  2 117 ? 144.024 240.705 171.313 1.00 336.76 ? 151 SER E C   1 
ATOM   7913  O O   . SER E  2 117 ? 144.245 240.811 172.523 1.00 336.33 ? 151 SER E O   1 
ATOM   7914  C CB  . SER E  2 117 ? 141.562 240.833 170.908 1.00 332.95 ? 151 SER E CB  1 
ATOM   7915  O OG  . SER E  2 117 ? 141.803 242.107 170.338 1.00 337.96 ? 151 SER E OG  1 
ATOM   7916  N N   . ASN E  2 118 ? 144.818 241.236 170.382 1.00 341.35 ? 152 ASN E N   1 
ATOM   7917  C CA  . ASN E  2 118 ? 145.990 241.989 170.807 1.00 343.14 ? 152 ASN E CA  1 
ATOM   7918  C C   . ASN E  2 118 ? 145.682 243.468 170.991 1.00 345.42 ? 152 ASN E C   1 
ATOM   7919  O O   . ASN E  2 118 ? 146.586 244.237 171.337 1.00 345.48 ? 152 ASN E O   1 
ATOM   7920  C CB  . ASN E  2 118 ? 147.144 241.806 169.814 1.00 344.75 ? 152 ASN E CB  1 
ATOM   7921  C CG  . ASN E  2 118 ? 146.991 242.637 168.553 1.00 347.52 ? 152 ASN E CG  1 
ATOM   7922  O OD1 . ASN E  2 118 ? 146.234 242.299 167.642 1.00 348.42 ? 152 ASN E OD1 1 
ATOM   7923  N ND2 . ASN E  2 118 ? 147.751 243.729 168.495 1.00 349.04 ? 152 ASN E ND2 1 
ATOM   7924  N N   . ASN E  2 119 ? 144.435 243.877 170.766 1.00 346.80 ? 153 ASN E N   1 
ATOM   7925  C CA  . ASN E  2 119 ? 143.967 245.222 171.072 1.00 348.22 ? 153 ASN E CA  1 
ATOM   7926  C C   . ASN E  2 119 ? 142.566 245.115 171.655 1.00 348.46 ? 153 ASN E C   1 
ATOM   7927  O O   . ASN E  2 119 ? 141.627 244.734 170.950 1.00 347.52 ? 153 ASN E O   1 
ATOM   7928  C CB  . ASN E  2 119 ? 143.961 246.114 169.825 1.00 349.72 ? 153 ASN E CB  1 
ATOM   7929  C CG  . ASN E  2 119 ? 143.544 247.542 170.130 1.00 351.51 ? 153 ASN E CG  1 
ATOM   7930  O OD1 . ASN E  2 119 ? 143.472 247.947 171.290 1.00 351.71 ? 153 ASN E OD1 1 
ATOM   7931  N ND2 . ASN E  2 119 ? 143.268 248.311 169.085 1.00 353.40 ? 153 ASN E ND2 1 
ATOM   7932  N N   . SER E  2 120 ? 142.431 245.450 172.938 1.00 349.97 ? 154 SER E N   1 
ATOM   7933  C CA  . SER E  2 120 ? 141.163 245.313 173.641 1.00 349.63 ? 154 SER E CA  1 
ATOM   7934  C C   . SER E  2 120 ? 140.136 246.371 173.262 1.00 350.47 ? 154 SER E C   1 
ATOM   7935  O O   . SER E  2 120 ? 138.935 246.083 173.298 1.00 346.82 ? 154 SER E O   1 
ATOM   7936  C CB  . SER E  2 120 ? 141.389 245.359 175.158 1.00 349.80 ? 154 SER E CB  1 
ATOM   7937  O OG  . SER E  2 120 ? 142.225 246.445 175.516 1.00 351.19 ? 154 SER E OG  1 
ATOM   7938  N N   . ASN E  2 121 ? 140.571 247.576 172.899 1.00 352.91 ? 155 ASN E N   1 
ATOM   7939  C CA  . ASN E  2 121 ? 139.672 248.679 172.561 1.00 352.15 ? 155 ASN E CA  1 
ATOM   7940  C C   . ASN E  2 121 ? 140.011 249.176 171.162 1.00 354.29 ? 155 ASN E C   1 
ATOM   7941  O O   . ASN E  2 121 ? 140.817 250.102 170.997 1.00 355.43 ? 155 ASN E O   1 
ATOM   7942  C CB  . ASN E  2 121 ? 139.772 249.808 173.588 1.00 351.64 ? 155 ASN E CB  1 
ATOM   7943  C CG  . ASN E  2 121 ? 139.811 249.295 175.014 1.00 351.16 ? 155 ASN E CG  1 
ATOM   7944  O OD1 . ASN E  2 121 ? 140.879 249.004 175.553 1.00 353.34 ? 155 ASN E OD1 1 
ATOM   7945  N ND2 . ASN E  2 121 ? 138.642 249.180 175.634 1.00 347.69 ? 155 ASN E ND2 1 
ATOM   7946  N N   . PRO E  2 122 ? 139.429 248.566 170.129 1.00 354.94 ? 156 PRO E N   1 
ATOM   7947  C CA  . PRO E  2 122 ? 139.682 249.031 168.761 1.00 356.54 ? 156 PRO E CA  1 
ATOM   7948  C C   . PRO E  2 122 ? 139.299 250.493 168.584 1.00 356.51 ? 156 PRO E C   1 
ATOM   7949  O O   . PRO E  2 122 ? 138.304 250.967 169.137 1.00 353.25 ? 156 PRO E O   1 
ATOM   7950  C CB  . PRO E  2 122 ? 138.794 248.121 167.909 1.00 355.68 ? 156 PRO E CB  1 
ATOM   7951  C CG  . PRO E  2 122 ? 138.642 246.877 168.703 1.00 351.97 ? 156 PRO E CG  1 
ATOM   7952  C CD  . PRO E  2 122 ? 138.854 247.209 170.158 1.00 351.72 ? 156 PRO E CD  1 
ATOM   7953  N N   . VAL E  2 123 ? 140.103 251.206 167.803 1.00 358.72 ? 157 VAL E N   1 
ATOM   7954  C CA  . VAL E  2 123 ? 139.810 252.596 167.475 1.00 357.67 ? 157 VAL E CA  1 
ATOM   7955  C C   . VAL E  2 123 ? 138.681 252.622 166.453 1.00 357.48 ? 157 VAL E C   1 
ATOM   7956  O O   . VAL E  2 123 ? 138.721 251.904 165.446 1.00 359.60 ? 157 VAL E O   1 
ATOM   7957  C CB  . VAL E  2 123 ? 141.064 253.309 166.949 1.00 357.86 ? 157 VAL E CB  1 
ATOM   7958  C CG1 . VAL E  2 123 ? 140.761 254.769 166.658 1.00 356.49 ? 157 VAL E CG1 1 
ATOM   7959  C CG2 . VAL E  2 123 ? 142.204 253.183 167.949 1.00 356.63 ? 157 VAL E CG2 1 
ATOM   7960  N N   . GLU E  2 124 ? 137.663 253.447 166.717 1.00 352.99 ? 158 GLU E N   1 
ATOM   7961  C CA  . GLU E  2 124 ? 136.426 253.380 165.943 1.00 350.11 ? 158 GLU E CA  1 
ATOM   7962  C C   . GLU E  2 124 ? 136.651 253.724 164.475 1.00 356.70 ? 158 GLU E C   1 
ATOM   7963  O O   . GLU E  2 124 ? 136.107 253.056 163.587 1.00 358.98 ? 158 GLU E O   1 
ATOM   7964  C CB  . GLU E  2 124 ? 135.380 254.309 166.558 1.00 341.17 ? 158 GLU E CB  1 
ATOM   7965  C CG  . GLU E  2 124 ? 135.126 254.053 168.034 1.00 334.02 ? 158 GLU E CG  1 
ATOM   7966  C CD  . GLU E  2 124 ? 134.134 255.027 168.635 1.00 326.06 ? 158 GLU E CD  1 
ATOM   7967  O OE1 . GLU E  2 124 ? 133.330 255.605 167.874 1.00 324.92 ? 158 GLU E OE1 1 
ATOM   7968  O OE2 . GLU E  2 124 ? 134.161 255.217 169.869 1.00 322.96 ? 158 GLU E OE2 1 
ATOM   7969  N N   . ASP E  2 125 ? 137.440 254.765 164.195 1.00 358.62 ? 159 ASP E N   1 
ATOM   7970  C CA  . ASP E  2 125 ? 137.614 255.194 162.809 1.00 360.48 ? 159 ASP E CA  1 
ATOM   7971  C C   . ASP E  2 125 ? 138.362 254.148 161.986 1.00 362.29 ? 159 ASP E C   1 
ATOM   7972  O O   . ASP E  2 125 ? 137.983 253.867 160.842 1.00 363.52 ? 159 ASP E O   1 
ATOM   7973  C CB  . ASP E  2 125 ? 138.313 256.558 162.760 1.00 359.39 ? 159 ASP E CB  1 
ATOM   7974  C CG  . ASP E  2 125 ? 139.805 256.481 163.051 1.00 358.71 ? 159 ASP E CG  1 
ATOM   7975  O OD1 . ASP E  2 125 ? 140.264 255.478 163.637 1.00 358.91 ? 159 ASP E OD1 1 
ATOM   7976  O OD2 . ASP E  2 125 ? 140.525 257.435 162.690 1.00 357.58 ? 159 ASP E OD2 1 
ATOM   7977  N N   . LYS E  2 126 ? 139.413 253.556 162.550 1.00 362.20 ? 160 LYS E N   1 
ATOM   7978  C CA  . LYS E  2 126 ? 140.201 252.540 161.865 1.00 362.96 ? 160 LYS E CA  1 
ATOM   7979  C C   . LYS E  2 126 ? 141.122 251.874 162.875 1.00 363.13 ? 160 LYS E C   1 
ATOM   7980  O O   . LYS E  2 126 ? 141.586 252.514 163.823 1.00 361.86 ? 160 LYS E O   1 
ATOM   7981  C CB  . LYS E  2 126 ? 141.013 253.138 160.704 1.00 361.61 ? 160 LYS E CB  1 
ATOM   7982  C CG  . LYS E  2 126 ? 141.944 254.288 161.085 1.00 359.39 ? 160 LYS E CG  1 
ATOM   7983  C CD  . LYS E  2 126 ? 143.346 253.804 161.434 1.00 357.26 ? 160 LYS E CD  1 
ATOM   7984  C CE  . LYS E  2 126 ? 144.130 254.868 162.184 1.00 354.72 ? 160 LYS E CE  1 
ATOM   7985  N NZ  . LYS E  2 126 ? 145.243 254.279 162.978 1.00 351.99 ? 160 LYS E NZ  1 
ATOM   7986  N N   . ASP E  2 127 ? 141.379 250.587 162.661 1.00 365.80 ? 161 ASP E N   1 
ATOM   7987  C CA  . ASP E  2 127 ? 142.315 249.838 163.490 1.00 365.98 ? 161 ASP E CA  1 
ATOM   7988  C C   . ASP E  2 127 ? 142.696 248.571 162.738 1.00 367.15 ? 161 ASP E C   1 
ATOM   7989  O O   . ASP E  2 127 ? 142.040 248.181 161.769 1.00 368.79 ? 161 ASP E O   1 
ATOM   7990  C CB  . ASP E  2 127 ? 141.720 249.506 164.861 1.00 364.22 ? 161 ASP E CB  1 
ATOM   7991  C CG  . ASP E  2 127 ? 142.763 249.492 165.957 1.00 362.76 ? 161 ASP E CG  1 
ATOM   7992  O OD1 . ASP E  2 127 ? 143.874 250.011 165.724 1.00 363.42 ? 161 ASP E OD1 1 
ATOM   7993  O OD2 . ASP E  2 127 ? 142.473 248.961 167.048 1.00 360.35 ? 161 ASP E OD2 1 
ATOM   7994  N N   . ALA E  2 128 ? 143.766 247.928 163.199 1.00 365.83 ? 162 ALA E N   1 
ATOM   7995  C CA  . ALA E  2 128 ? 144.287 246.715 162.581 1.00 364.09 ? 162 ALA E CA  1 
ATOM   7996  C C   . ALA E  2 128 ? 144.321 245.560 163.577 1.00 361.75 ? 162 ALA E C   1 
ATOM   7997  O O   . ALA E  2 128 ? 145.271 244.775 163.614 1.00 360.12 ? 162 ALA E O   1 
ATOM   7998  C CB  . ALA E  2 128 ? 145.674 246.958 161.990 1.00 361.32 ? 162 ALA E CB  1 
ATOM   7999  N N   . VAL E  2 129 ? 143.266 245.436 164.386 1.00 361.60 ? 163 VAL E N   1 
ATOM   8000  C CA  . VAL E  2 129 ? 143.248 244.430 165.440 1.00 357.26 ? 163 VAL E CA  1 
ATOM   8001  C C   . VAL E  2 129 ? 143.259 243.025 164.836 1.00 354.35 ? 163 VAL E C   1 
ATOM   8002  O O   . VAL E  2 129 ? 142.685 242.772 163.768 1.00 355.00 ? 163 VAL E O   1 
ATOM   8003  C CB  . VAL E  2 129 ? 142.029 244.636 166.356 1.00 355.64 ? 163 VAL E CB  1 
ATOM   8004  C CG1 . VAL E  2 129 ? 140.730 244.430 165.587 1.00 355.93 ? 163 VAL E CG1 1 
ATOM   8005  C CG2 . VAL E  2 129 ? 142.098 243.719 167.569 1.00 351.24 ? 163 VAL E CG2 1 
ATOM   8006  N N   . ALA E  2 130 ? 143.940 242.106 165.520 1.00 350.24 ? 164 ALA E N   1 
ATOM   8007  C CA  . ALA E  2 130 ? 144.080 240.728 165.072 1.00 344.50 ? 164 ALA E CA  1 
ATOM   8008  C C   . ALA E  2 130 ? 143.394 239.790 166.054 1.00 336.48 ? 164 ALA E C   1 
ATOM   8009  O O   . ALA E  2 130 ? 143.433 240.009 167.269 1.00 336.95 ? 164 ALA E O   1 
ATOM   8010  C CB  . ALA E  2 130 ? 145.555 240.338 164.921 1.00 342.68 ? 164 ALA E CB  1 
ATOM   8011  N N   . PHE E  2 131 ? 142.769 238.744 165.519 1.00 330.65 ? 165 PHE E N   1 
ATOM   8012  C CA  . PHE E  2 131 ? 142.082 237.731 166.304 1.00 323.46 ? 165 PHE E CA  1 
ATOM   8013  C C   . PHE E  2 131 ? 142.755 236.381 166.093 1.00 318.42 ? 165 PHE E C   1 
ATOM   8014  O O   . PHE E  2 131 ? 143.075 236.001 164.964 1.00 318.10 ? 165 PHE E O   1 
ATOM   8015  C CB  . PHE E  2 131 ? 140.601 237.645 165.916 1.00 322.17 ? 165 PHE E CB  1 
ATOM   8016  C CG  . PHE E  2 131 ? 139.697 238.474 166.782 1.00 321.29 ? 165 PHE E CG  1 
ATOM   8017  C CD1 . PHE E  2 131 ? 138.533 239.017 166.268 1.00 318.57 ? 165 PHE E CD1 1 
ATOM   8018  C CD2 . PHE E  2 131 ? 140.002 238.696 168.113 1.00 322.83 ? 165 PHE E CD2 1 
ATOM   8019  C CE1 . PHE E  2 131 ? 137.698 239.779 167.062 1.00 315.60 ? 165 PHE E CE1 1 
ATOM   8020  C CE2 . PHE E  2 131 ? 139.166 239.453 168.912 1.00 321.00 ? 165 PHE E CE2 1 
ATOM   8021  C CZ  . PHE E  2 131 ? 138.014 239.995 168.385 1.00 316.97 ? 165 PHE E CZ  1 
ATOM   8022  N N   . THR E  2 132 ? 142.966 235.657 167.190 1.00 313.98 ? 166 THR E N   1 
ATOM   8023  C CA  . THR E  2 132 ? 143.679 234.389 167.136 1.00 308.99 ? 166 THR E CA  1 
ATOM   8024  C C   . THR E  2 132 ? 143.077 233.420 168.142 1.00 305.87 ? 166 THR E C   1 
ATOM   8025  O O   . THR E  2 132 ? 142.762 233.804 169.271 1.00 306.27 ? 166 THR E O   1 
ATOM   8026  C CB  . THR E  2 132 ? 145.174 234.576 167.430 1.00 307.72 ? 166 THR E CB  1 
ATOM   8027  O OG1 . THR E  2 132 ? 145.721 235.553 166.537 1.00 310.81 ? 166 THR E OG1 1 
ATOM   8028  C CG2 . THR E  2 132 ? 145.926 233.263 167.259 1.00 303.77 ? 166 THR E CG2 1 
ATOM   8029  N N   . CYS E  2 133 ? 142.918 232.165 167.723 1.00 303.70 ? 167 CYS E N   1 
ATOM   8030  C CA  . CYS E  2 133 ? 142.538 231.084 168.627 1.00 299.99 ? 167 CYS E CA  1 
ATOM   8031  C C   . CYS E  2 133 ? 143.817 230.440 169.155 1.00 295.73 ? 167 CYS E C   1 
ATOM   8032  O O   . CYS E  2 133 ? 144.560 229.810 168.399 1.00 294.58 ? 167 CYS E O   1 
ATOM   8033  C CB  . CYS E  2 133 ? 141.644 230.068 167.919 1.00 299.24 ? 167 CYS E CB  1 
ATOM   8034  S SG  . CYS E  2 133 ? 140.504 230.787 166.706 1.00 307.11 ? 167 CYS E SG  1 
ATOM   8035  N N   . GLU E  2 134 ? 144.079 230.616 170.450 1.00 295.37 ? 168 GLU E N   1 
ATOM   8036  C CA  . GLU E  2 134 ? 145.314 230.189 171.107 1.00 293.04 ? 168 GLU E CA  1 
ATOM   8037  C C   . GLU E  2 134 ? 145.584 228.680 171.150 1.00 287.75 ? 168 GLU E C   1 
ATOM   8038  O O   . GLU E  2 134 ? 146.723 228.274 170.887 1.00 286.74 ? 168 GLU E O   1 
ATOM   8039  C CB  . GLU E  2 134 ? 145.361 230.751 172.533 1.00 295.92 ? 168 GLU E CB  1 
ATOM   8040  C CG  . GLU E  2 134 ? 144.022 230.838 173.242 1.00 296.06 ? 168 GLU E CG  1 
ATOM   8041  C CD  . GLU E  2 134 ? 143.307 232.154 172.988 1.00 300.45 ? 168 GLU E CD  1 
ATOM   8042  O OE1 . GLU E  2 134 ? 143.355 232.649 171.842 1.00 302.20 ? 168 GLU E OE1 1 
ATOM   8043  O OE2 . GLU E  2 134 ? 142.695 232.692 173.935 1.00 304.10 ? 168 GLU E OE2 1 
ATOM   8044  N N   . PRO E  2 135 ? 144.600 227.803 171.469 1.00 283.93 ? 169 PRO E N   1 
ATOM   8045  C CA  . PRO E  2 135 ? 144.964 226.417 171.812 1.00 279.69 ? 169 PRO E CA  1 
ATOM   8046  C C   . PRO E  2 135 ? 145.415 225.592 170.616 1.00 277.13 ? 169 PRO E C   1 
ATOM   8047  O O   . PRO E  2 135 ? 144.611 224.898 169.984 1.00 274.78 ? 169 PRO E O   1 
ATOM   8048  C CB  . PRO E  2 135 ? 143.676 225.856 172.424 1.00 275.34 ? 169 PRO E CB  1 
ATOM   8049  C CG  . PRO E  2 135 ? 142.595 226.629 171.800 1.00 274.15 ? 169 PRO E CG  1 
ATOM   8050  C CD  . PRO E  2 135 ? 143.135 227.975 171.412 1.00 281.59 ? 169 PRO E CD  1 
ATOM   8051  N N   . GLU E  2 136 ? 146.707 225.669 170.301 1.00 277.48 ? 170 GLU E N   1 
ATOM   8052  C CA  . GLU E  2 136 ? 147.233 225.023 169.105 1.00 275.62 ? 170 GLU E CA  1 
ATOM   8053  C C   . GLU E  2 136 ? 147.175 223.505 169.214 1.00 270.59 ? 170 GLU E C   1 
ATOM   8054  O O   . GLU E  2 136 ? 147.633 222.912 170.195 1.00 269.60 ? 170 GLU E O   1 
ATOM   8055  C CB  . GLU E  2 136 ? 148.672 225.475 168.853 1.00 277.22 ? 170 GLU E CB  1 
ATOM   8056  C CG  . GLU E  2 136 ? 149.297 224.960 167.556 1.00 276.04 ? 170 GLU E CG  1 
ATOM   8057  C CD  . GLU E  2 136 ? 148.525 225.363 166.306 1.00 277.87 ? 170 GLU E CD  1 
ATOM   8058  O OE1 . GLU E  2 136 ? 147.424 224.822 166.064 1.00 275.40 ? 170 GLU E OE1 1 
ATOM   8059  O OE2 . GLU E  2 136 ? 149.024 226.232 165.561 1.00 282.06 ? 170 GLU E OE2 1 
ATOM   8060  N N   . THR E  2 137 ? 146.604 222.877 168.186 1.00 265.73 ? 171 THR E N   1 
ATOM   8061  C CA  . THR E  2 137 ? 146.601 221.430 168.035 1.00 258.47 ? 171 THR E CA  1 
ATOM   8062  C C   . THR E  2 137 ? 147.015 221.095 166.610 1.00 251.29 ? 171 THR E C   1 
ATOM   8063  O O   . THR E  2 137 ? 146.907 221.927 165.706 1.00 251.88 ? 171 THR E O   1 
ATOM   8064  C CB  . THR E  2 137 ? 145.228 220.803 168.334 1.00 257.13 ? 171 THR E CB  1 
ATOM   8065  O OG1 . THR E  2 137 ? 144.445 220.768 167.134 1.00 251.32 ? 171 THR E OG1 1 
ATOM   8066  C CG2 . THR E  2 137 ? 144.479 221.594 169.398 1.00 262.85 ? 171 THR E CG2 1 
ATOM   8067  N N   . GLN E  2 138 ? 147.496 219.871 166.418 1.00 245.64 ? 172 GLN E N   1 
ATOM   8068  C CA  . GLN E  2 138 ? 147.962 219.453 165.107 1.00 239.76 ? 172 GLN E CA  1 
ATOM   8069  C C   . GLN E  2 138 ? 146.793 219.025 164.222 1.00 233.44 ? 172 GLN E C   1 
ATOM   8070  O O   . GLN E  2 138 ? 145.673 218.809 164.689 1.00 230.65 ? 172 GLN E O   1 
ATOM   8071  C CB  . GLN E  2 138 ? 148.971 218.311 165.232 1.00 237.62 ? 172 GLN E CB  1 
ATOM   8072  C CG  . GLN E  2 138 ? 150.325 218.742 165.768 1.00 240.42 ? 172 GLN E CG  1 
ATOM   8073  C CD  . GLN E  2 138 ? 150.977 219.808 164.909 1.00 244.09 ? 172 GLN E CD  1 
ATOM   8074  O OE1 . GLN E  2 138 ? 151.366 220.867 165.401 1.00 246.47 ? 172 GLN E OE1 1 
ATOM   8075  N NE2 . GLN E  2 138 ? 151.098 219.533 163.615 1.00 244.24 ? 172 GLN E NE2 1 
ATOM   8076  N N   . ASP E  2 139 ? 147.072 218.965 162.915 1.00 231.41 ? 173 ASP E N   1 
ATOM   8077  C CA  . ASP E  2 139 ? 146.212 218.421 161.862 1.00 225.41 ? 173 ASP E CA  1 
ATOM   8078  C C   . ASP E  2 139 ? 144.739 218.800 162.001 1.00 222.74 ? 173 ASP E C   1 
ATOM   8079  O O   . ASP E  2 139 ? 143.855 218.014 161.646 1.00 218.62 ? 173 ASP E O   1 
ATOM   8080  C CB  . ASP E  2 139 ? 146.391 216.893 161.761 1.00 218.72 ? 173 ASP E CB  1 
ATOM   8081  C CG  . ASP E  2 139 ? 145.915 216.127 162.998 1.00 213.25 ? 173 ASP E CG  1 
ATOM   8082  O OD1 . ASP E  2 139 ? 146.467 215.034 163.242 1.00 207.00 ? 173 ASP E OD1 1 
ATOM   8083  O OD2 . ASP E  2 139 ? 144.971 216.553 163.691 1.00 211.78 ? 173 ASP E OD2 1 
ATOM   8084  N N   . THR E  2 140 ? 144.467 220.003 162.494 1.00 225.34 ? 174 THR E N   1 
ATOM   8085  C CA  . THR E  2 140 ? 143.109 220.495 162.662 1.00 225.97 ? 174 THR E CA  1 
ATOM   8086  C C   . THR E  2 140 ? 142.775 221.505 161.572 1.00 226.60 ? 174 THR E C   1 
ATOM   8087  O O   . THR E  2 140 ? 143.659 222.002 160.868 1.00 227.65 ? 174 THR E O   1 
ATOM   8088  C CB  . THR E  2 140 ? 142.921 221.148 164.033 1.00 233.36 ? 174 THR E CB  1 
ATOM   8089  O OG1 . THR E  2 140 ? 141.657 221.824 164.071 1.00 233.16 ? 174 THR E OG1 1 
ATOM   8090  C CG2 . THR E  2 140 ? 144.025 222.157 164.287 1.00 241.26 ? 174 THR E CG2 1 
ATOM   8091  N N   . THR E  2 141 ? 141.486 221.803 161.442 1.00 226.15 ? 175 THR E N   1 
ATOM   8092  C CA  . THR E  2 141 ? 140.993 222.806 160.508 1.00 229.60 ? 175 THR E CA  1 
ATOM   8093  C C   . THR E  2 141 ? 140.241 223.881 161.280 1.00 235.36 ? 175 THR E C   1 
ATOM   8094  O O   . THR E  2 141 ? 139.388 223.567 162.118 1.00 235.75 ? 175 THR E O   1 
ATOM   8095  C CB  . THR E  2 141 ? 140.080 222.178 159.452 1.00 226.00 ? 175 THR E CB  1 
ATOM   8096  O OG1 . THR E  2 141 ? 140.683 220.980 158.947 1.00 223.52 ? 175 THR E OG1 1 
ATOM   8097  C CG2 . THR E  2 141 ? 139.850 223.147 158.303 1.00 229.20 ? 175 THR E CG2 1 
ATOM   8098  N N   . TYR E  2 142 ? 140.559 225.140 160.998 1.00 242.84 ? 176 TYR E N   1 
ATOM   8099  C CA  . TYR E  2 142 ? 139.948 226.278 161.671 1.00 249.83 ? 176 TYR E CA  1 
ATOM   8100  C C   . TYR E  2 142 ? 138.976 226.964 160.722 1.00 253.80 ? 176 TYR E C   1 
ATOM   8101  O O   . TYR E  2 142 ? 139.143 226.896 159.500 1.00 256.40 ? 176 TYR E O   1 
ATOM   8102  C CB  . TYR E  2 142 ? 141.003 227.282 162.144 1.00 258.77 ? 176 TYR E CB  1 
ATOM   8103  C CG  . TYR E  2 142 ? 142.238 226.680 162.784 1.00 261.48 ? 176 TYR E CG  1 
ATOM   8104  C CD1 . TYR E  2 142 ? 143.233 226.087 162.014 1.00 260.39 ? 176 TYR E CD1 1 
ATOM   8105  C CD2 . TYR E  2 142 ? 142.410 226.709 164.160 1.00 262.22 ? 176 TYR E CD2 1 
ATOM   8106  C CE1 . TYR E  2 142 ? 144.360 225.541 162.597 1.00 261.61 ? 176 TYR E CE1 1 
ATOM   8107  C CE2 . TYR E  2 142 ? 143.530 226.163 164.750 1.00 266.64 ? 176 TYR E CE2 1 
ATOM   8108  C CZ  . TYR E  2 142 ? 144.503 225.582 163.966 1.00 266.34 ? 176 TYR E CZ  1 
ATOM   8109  O OH  . TYR E  2 142 ? 145.622 225.039 164.556 1.00 269.84 ? 176 TYR E OH  1 
ATOM   8110  N N   . LEU E  2 143 ? 137.967 227.627 161.285 1.00 258.02 ? 177 LEU E N   1 
ATOM   8111  C CA  . LEU E  2 143 ? 137.041 228.451 160.520 1.00 265.39 ? 177 LEU E CA  1 
ATOM   8112  C C   . LEU E  2 143 ? 136.377 229.454 161.455 1.00 270.89 ? 177 LEU E C   1 
ATOM   8113  O O   . LEU E  2 143 ? 136.125 229.148 162.625 1.00 270.20 ? 177 LEU E O   1 
ATOM   8114  C CB  . LEU E  2 143 ? 136.015 227.583 159.767 1.00 265.08 ? 177 LEU E CB  1 
ATOM   8115  C CG  . LEU E  2 143 ? 135.010 226.584 160.365 1.00 262.22 ? 177 LEU E CG  1 
ATOM   8116  C CD1 . LEU E  2 143 ? 134.030 227.193 161.350 1.00 267.23 ? 177 LEU E CD1 1 
ATOM   8117  C CD2 . LEU E  2 143 ? 134.264 225.860 159.251 1.00 259.44 ? 177 LEU E CD2 1 
ATOM   8118  N N   . TRP E  2 144 ? 136.121 230.654 160.941 1.00 277.20 ? 178 TRP E N   1 
ATOM   8119  C CA  . TRP E  2 144 ? 135.657 231.777 161.744 1.00 282.13 ? 178 TRP E CA  1 
ATOM   8120  C C   . TRP E  2 144 ? 134.183 232.037 161.471 1.00 283.20 ? 178 TRP E C   1 
ATOM   8121  O O   . TRP E  2 144 ? 133.715 231.859 160.341 1.00 284.64 ? 178 TRP E O   1 
ATOM   8122  C CB  . TRP E  2 144 ? 136.481 233.028 161.440 1.00 288.89 ? 178 TRP E CB  1 
ATOM   8123  C CG  . TRP E  2 144 ? 137.943 232.847 161.698 1.00 292.21 ? 178 TRP E CG  1 
ATOM   8124  C CD1 . TRP E  2 144 ? 138.850 232.239 160.880 1.00 292.91 ? 178 TRP E CD1 1 
ATOM   8125  C CD2 . TRP E  2 144 ? 138.672 233.279 162.853 1.00 295.37 ? 178 TRP E CD2 1 
ATOM   8126  N NE1 . TRP E  2 144 ? 140.097 232.263 161.454 1.00 297.88 ? 178 TRP E NE1 1 
ATOM   8127  C CE2 . TRP E  2 144 ? 140.015 232.898 162.665 1.00 300.26 ? 178 TRP E CE2 1 
ATOM   8128  C CE3 . TRP E  2 144 ? 138.319 233.952 164.026 1.00 297.85 ? 178 TRP E CE3 1 
ATOM   8129  C CZ2 . TRP E  2 144 ? 141.004 233.166 163.606 1.00 304.66 ? 178 TRP E CZ2 1 
ATOM   8130  C CZ3 . TRP E  2 144 ? 139.305 234.218 164.960 1.00 304.04 ? 178 TRP E CZ3 1 
ATOM   8131  C CH2 . TRP E  2 144 ? 140.631 233.825 164.744 1.00 306.08 ? 178 TRP E CH2 1 
ATOM   8132  N N   . TRP E  2 145 ? 133.455 232.450 162.506 1.00 283.46 ? 179 TRP E N   1 
ATOM   8133  C CA  . TRP E  2 145 ? 132.025 232.704 162.411 1.00 285.91 ? 179 TRP E CA  1 
ATOM   8134  C C   . TRP E  2 145 ? 131.760 234.101 162.957 1.00 291.49 ? 179 TRP E C   1 
ATOM   8135  O O   . TRP E  2 145 ? 132.081 234.385 164.115 1.00 294.09 ? 179 TRP E O   1 
ATOM   8136  C CB  . TRP E  2 145 ? 131.251 231.650 163.208 1.00 283.81 ? 179 TRP E CB  1 
ATOM   8137  C CG  . TRP E  2 145 ? 130.841 230.456 162.390 1.00 283.27 ? 179 TRP E CG  1 
ATOM   8138  C CD1 . TRP E  2 145 ? 131.596 229.346 162.155 1.00 280.56 ? 179 TRP E CD1 1 
ATOM   8139  C CD2 . TRP E  2 145 ? 129.584 230.226 161.742 1.00 286.69 ? 179 TRP E CD2 1 
ATOM   8140  N NE1 . TRP E  2 145 ? 130.903 228.451 161.381 1.00 281.22 ? 179 TRP E NE1 1 
ATOM   8141  C CE2 . TRP E  2 145 ? 129.662 228.965 161.115 1.00 285.77 ? 179 TRP E CE2 1 
ATOM   8142  C CE3 . TRP E  2 145 ? 128.406 230.962 161.622 1.00 290.27 ? 179 TRP E CE3 1 
ATOM   8143  C CZ2 . TRP E  2 145 ? 128.609 228.429 160.379 1.00 288.42 ? 179 TRP E CZ2 1 
ATOM   8144  C CZ3 . TRP E  2 145 ? 127.360 230.426 160.889 1.00 290.90 ? 179 TRP E CZ3 1 
ATOM   8145  C CH2 . TRP E  2 145 ? 127.470 229.174 160.277 1.00 290.13 ? 179 TRP E CH2 1 
ATOM   8146  N N   . ILE E  2 146 ? 131.175 234.968 162.132 1.00 295.62 ? 180 ILE E N   1 
ATOM   8147  C CA  . ILE E  2 146 ? 130.935 236.361 162.499 1.00 300.05 ? 180 ILE E CA  1 
ATOM   8148  C C   . ILE E  2 146 ? 129.453 236.663 162.333 1.00 302.19 ? 180 ILE E C   1 
ATOM   8149  O O   . ILE E  2 146 ? 128.806 236.144 161.416 1.00 302.75 ? 180 ILE E O   1 
ATOM   8150  C CB  . ILE E  2 146 ? 131.803 237.333 161.670 1.00 301.86 ? 180 ILE E CB  1 
ATOM   8151  C CG1 . ILE E  2 146 ? 131.760 238.736 162.278 1.00 304.31 ? 180 ILE E CG1 1 
ATOM   8152  C CG2 . ILE E  2 146 ? 131.375 237.350 160.208 1.00 302.81 ? 180 ILE E CG2 1 
ATOM   8153  C CD1 . ILE E  2 146 ? 131.924 238.752 163.780 1.00 306.08 ? 180 ILE E CD1 1 
ATOM   8154  N N   . ASN E  2 147 ? 128.911 237.478 163.249 1.00 303.62 ? 181 ASN E N   1 
ATOM   8155  C CA  . ASN E  2 147 ? 127.472 237.671 163.439 1.00 304.22 ? 181 ASN E CA  1 
ATOM   8156  C C   . ASN E  2 147 ? 126.748 236.343 163.244 1.00 303.29 ? 181 ASN E C   1 
ATOM   8157  O O   . ASN E  2 147 ? 125.654 236.280 162.673 1.00 304.12 ? 181 ASN E O   1 
ATOM   8158  C CB  . ASN E  2 147 ? 126.922 238.795 162.541 1.00 305.39 ? 181 ASN E CB  1 
ATOM   8159  C CG  . ASN E  2 147 ? 126.904 238.442 161.067 1.00 305.74 ? 181 ASN E CG  1 
ATOM   8160  O OD1 . ASN E  2 147 ? 127.945 238.406 160.412 1.00 305.05 ? 181 ASN E OD1 1 
ATOM   8161  N ND2 . ASN E  2 147 ? 125.714 238.189 160.535 1.00 306.67 ? 181 ASN E ND2 1 
ATOM   8162  N N   . ASN E  2 148 ? 127.372 235.288 163.774 1.00 300.59 ? 182 ASN E N   1 
ATOM   8163  C CA  . ASN E  2 148 ? 127.044 233.886 163.535 1.00 297.87 ? 182 ASN E CA  1 
ATOM   8164  C C   . ASN E  2 148 ? 126.637 233.664 162.071 1.00 297.92 ? 182 ASN E C   1 
ATOM   8165  O O   . ASN E  2 148 ? 125.506 233.284 161.760 1.00 295.72 ? 182 ASN E O   1 
ATOM   8166  C CB  . ASN E  2 148 ? 125.999 233.389 164.556 1.00 296.74 ? 182 ASN E CB  1 
ATOM   8167  C CG  . ASN E  2 148 ? 125.310 232.090 164.158 1.00 294.96 ? 182 ASN E CG  1 
ATOM   8168  O OD1 . ASN E  2 148 ? 125.917 231.232 163.516 1.00 294.17 ? 182 ASN E OD1 1 
ATOM   8169  N ND2 . ASN E  2 148 ? 124.050 231.929 164.592 1.00 293.59 ? 182 ASN E ND2 1 
ATOM   8170  N N   . GLN E  2 149 ? 127.551 233.999 161.159 1.00 297.95 ? 183 GLN E N   1 
ATOM   8171  C CA  . GLN E  2 149 ? 127.470 233.622 159.755 1.00 297.66 ? 183 GLN E CA  1 
ATOM   8172  C C   . GLN E  2 149 ? 128.896 233.518 159.233 1.00 297.30 ? 183 GLN E C   1 
ATOM   8173  O O   . GLN E  2 149 ? 129.803 234.199 159.720 1.00 298.01 ? 183 GLN E O   1 
ATOM   8174  C CB  . GLN E  2 149 ? 126.617 234.607 158.936 1.00 299.11 ? 183 GLN E CB  1 
ATOM   8175  C CG  . GLN E  2 149 ? 127.247 235.961 158.640 1.00 300.97 ? 183 GLN E CG  1 
ATOM   8176  C CD  . GLN E  2 149 ? 128.127 235.959 157.407 1.00 300.66 ? 183 GLN E CD  1 
ATOM   8177  O OE1 . GLN E  2 149 ? 127.695 235.572 156.321 1.00 297.92 ? 183 GLN E OE1 1 
ATOM   8178  N NE2 . GLN E  2 149 ? 129.371 236.397 157.567 1.00 304.04 ? 183 GLN E NE2 1 
ATOM   8179  N N   . SER E  2 150 ? 129.092 232.641 158.250 1.00 296.94 ? 184 SER E N   1 
ATOM   8180  C CA  . SER E  2 150 ? 130.437 232.350 157.770 1.00 299.58 ? 184 SER E CA  1 
ATOM   8181  C C   . SER E  2 150 ? 131.105 233.613 157.239 1.00 305.01 ? 184 SER E C   1 
ATOM   8182  O O   . SER E  2 150 ? 130.473 234.454 156.595 1.00 306.33 ? 184 SER E O   1 
ATOM   8183  C CB  . SER E  2 150 ? 130.395 231.275 156.684 1.00 298.84 ? 184 SER E CB  1 
ATOM   8184  O OG  . SER E  2 150 ? 129.580 231.678 155.599 1.00 297.40 ? 184 SER E OG  1 
ATOM   8185  N N   . LEU E  2 151 ? 132.401 233.734 157.511 1.00 306.57 ? 185 LEU E N   1 
ATOM   8186  C CA  . LEU E  2 151 ? 133.106 234.984 157.260 1.00 309.90 ? 185 LEU E CA  1 
ATOM   8187  C C   . LEU E  2 151 ? 133.066 235.331 155.774 1.00 314.33 ? 185 LEU E C   1 
ATOM   8188  O O   . LEU E  2 151 ? 133.301 234.457 154.928 1.00 315.16 ? 185 LEU E O   1 
ATOM   8189  C CB  . LEU E  2 151 ? 134.553 234.896 157.755 1.00 307.57 ? 185 LEU E CB  1 
ATOM   8190  C CG  . LEU E  2 151 ? 135.640 234.202 156.927 1.00 305.49 ? 185 LEU E CG  1 
ATOM   8191  C CD1 . LEU E  2 151 ? 137.014 234.484 157.517 1.00 303.83 ? 185 LEU E CD1 1 
ATOM   8192  C CD2 . LEU E  2 151 ? 135.398 232.703 156.834 1.00 301.08 ? 185 LEU E CD2 1 
ATOM   8193  N N   . PRO E  2 152 ? 132.740 236.573 155.415 1.00 317.08 ? 186 PRO E N   1 
ATOM   8194  C CA  . PRO E  2 152 ? 132.703 236.972 154.002 1.00 321.64 ? 186 PRO E CA  1 
ATOM   8195  C C   . PRO E  2 152 ? 134.113 237.157 153.456 1.00 327.75 ? 186 PRO E C   1 
ATOM   8196  O O   . PRO E  2 152 ? 134.883 237.983 153.949 1.00 328.20 ? 186 PRO E O   1 
ATOM   8197  C CB  . PRO E  2 152 ? 131.921 238.292 154.036 1.00 319.92 ? 186 PRO E CB  1 
ATOM   8198  C CG  . PRO E  2 152 ? 132.186 238.846 155.395 1.00 317.24 ? 186 PRO E CG  1 
ATOM   8199  C CD  . PRO E  2 152 ? 132.332 237.665 156.317 1.00 315.32 ? 186 PRO E CD  1 
ATOM   8200  N N   . VAL E  2 153 ? 134.450 236.372 152.430 1.00 332.63 ? 187 VAL E N   1 
ATOM   8201  C CA  . VAL E  2 153 ? 135.796 236.413 151.871 1.00 336.12 ? 187 VAL E CA  1 
ATOM   8202  C C   . VAL E  2 153 ? 136.075 237.795 151.303 1.00 339.70 ? 187 VAL E C   1 
ATOM   8203  O O   . VAL E  2 153 ? 135.327 238.306 150.459 1.00 341.00 ? 187 VAL E O   1 
ATOM   8204  C CB  . VAL E  2 153 ? 135.964 235.323 150.802 1.00 337.23 ? 187 VAL E CB  1 
ATOM   8205  C CG1 . VAL E  2 153 ? 137.380 235.340 150.249 1.00 338.20 ? 187 VAL E CG1 1 
ATOM   8206  C CG2 . VAL E  2 153 ? 135.626 233.958 151.382 1.00 335.85 ? 187 VAL E CG2 1 
ATOM   8207  N N   . SER E  2 154 ? 137.161 238.409 151.768 1.00 342.02 ? 188 SER E N   1 
ATOM   8208  C CA  . SER E  2 154 ? 137.547 239.747 151.346 1.00 344.93 ? 188 SER E CA  1 
ATOM   8209  C C   . SER E  2 154 ? 139.010 239.952 151.696 1.00 348.23 ? 188 SER E C   1 
ATOM   8210  O O   . SER E  2 154 ? 139.490 239.380 152.681 1.00 348.22 ? 188 SER E O   1 
ATOM   8211  C CB  . SER E  2 154 ? 136.676 240.814 152.027 1.00 345.14 ? 188 SER E CB  1 
ATOM   8212  O OG  . SER E  2 154 ? 137.199 242.116 151.829 1.00 347.62 ? 188 SER E OG  1 
ATOM   8213  N N   . PRO E  2 155 ? 139.746 240.748 150.915 1.00 348.72 ? 189 PRO E N   1 
ATOM   8214  C CA  . PRO E  2 155 ? 141.123 241.080 151.314 1.00 350.20 ? 189 PRO E CA  1 
ATOM   8215  C C   . PRO E  2 155 ? 141.189 241.818 152.637 1.00 351.97 ? 189 PRO E C   1 
ATOM   8216  O O   . PRO E  2 155 ? 142.230 241.793 153.306 1.00 352.36 ? 189 PRO E O   1 
ATOM   8217  C CB  . PRO E  2 155 ? 141.621 241.947 150.149 1.00 349.65 ? 189 PRO E CB  1 
ATOM   8218  C CG  . PRO E  2 155 ? 140.368 242.510 149.546 1.00 347.49 ? 189 PRO E CG  1 
ATOM   8219  C CD  . PRO E  2 155 ? 139.381 241.384 149.639 1.00 347.59 ? 189 PRO E CD  1 
ATOM   8220  N N   . ARG E  2 156 ? 140.099 242.482 153.028 1.00 352.68 ? 190 ARG E N   1 
ATOM   8221  C CA  . ARG E  2 156 ? 140.020 243.133 154.328 1.00 353.31 ? 190 ARG E CA  1 
ATOM   8222  C C   . ARG E  2 156 ? 140.198 242.149 155.480 1.00 353.18 ? 190 ARG E C   1 
ATOM   8223  O O   . ARG E  2 156 ? 140.718 242.531 156.534 1.00 355.06 ? 190 ARG E O   1 
ATOM   8224  C CB  . ARG E  2 156 ? 138.681 243.870 154.432 1.00 353.58 ? 190 ARG E CB  1 
ATOM   8225  C CG  . ARG E  2 156 ? 138.275 244.312 155.821 1.00 356.08 ? 190 ARG E CG  1 
ATOM   8226  C CD  . ARG E  2 156 ? 136.767 244.199 155.998 1.00 357.00 ? 190 ARG E CD  1 
ATOM   8227  N NE  . ARG E  2 156 ? 136.352 244.527 157.355 1.00 360.08 ? 190 ARG E NE  1 
ATOM   8228  C CZ  . ARG E  2 156 ? 136.353 245.751 157.865 1.00 362.80 ? 190 ARG E CZ  1 
ATOM   8229  N NH1 . ARG E  2 156 ? 136.695 246.803 157.139 1.00 362.86 ? 190 ARG E NH1 1 
ATOM   8230  N NH2 . ARG E  2 156 ? 136.009 245.924 159.137 1.00 365.03 ? 190 ARG E NH2 1 
ATOM   8231  N N   . LEU E  2 157 ? 139.799 240.889 155.298 1.00 350.55 ? 191 LEU E N   1 
ATOM   8232  C CA  . LEU E  2 157 ? 139.985 239.854 156.314 1.00 347.50 ? 191 LEU E CA  1 
ATOM   8233  C C   . LEU E  2 157 ? 141.294 239.124 156.025 1.00 346.79 ? 191 LEU E C   1 
ATOM   8234  O O   . LEU E  2 157 ? 141.365 238.206 155.207 1.00 344.73 ? 191 LEU E O   1 
ATOM   8235  C CB  . LEU E  2 157 ? 138.797 238.896 156.340 1.00 343.06 ? 191 LEU E CB  1 
ATOM   8236  C CG  . LEU E  2 157 ? 137.404 239.498 156.531 1.00 342.23 ? 191 LEU E CG  1 
ATOM   8237  C CD1 . LEU E  2 157 ? 136.377 238.396 156.731 1.00 328.37 ? 191 LEU E CD1 1 
ATOM   8238  C CD2 . LEU E  2 157 ? 137.389 240.460 157.704 1.00 346.37 ? 191 LEU E CD2 1 
ATOM   8239  N N   . GLN E  2 158 ? 142.348 239.548 156.716 1.00 348.10 ? 192 GLN E N   1 
ATOM   8240  C CA  . GLN E  2 158 ? 143.657 238.935 156.557 1.00 345.27 ? 192 GLN E CA  1 
ATOM   8241  C C   . GLN E  2 158 ? 143.791 237.717 157.463 1.00 340.63 ? 192 GLN E C   1 
ATOM   8242  O O   . GLN E  2 158 ? 143.296 237.697 158.593 1.00 340.77 ? 192 GLN E O   1 
ATOM   8243  C CB  . GLN E  2 158 ? 144.764 239.945 156.865 1.00 347.09 ? 192 GLN E CB  1 
ATOM   8244  C CG  . GLN E  2 158 ? 146.185 239.426 156.662 1.00 344.06 ? 192 GLN E CG  1 
ATOM   8245  C CD  . GLN E  2 158 ? 146.879 239.060 157.963 1.00 341.80 ? 192 GLN E CD  1 
ATOM   8246  O OE1 . GLN E  2 158 ? 146.329 238.343 158.799 1.00 341.82 ? 192 GLN E OE1 1 
ATOM   8247  N NE2 . GLN E  2 158 ? 148.097 239.558 158.140 1.00 341.21 ? 192 GLN E NE2 1 
ATOM   8248  N N   . LEU E  2 159 ? 144.469 236.693 156.951 1.00 336.72 ? 193 LEU E N   1 
ATOM   8249  C CA  . LEU E  2 159 ? 144.728 235.475 157.702 1.00 330.28 ? 193 LEU E CA  1 
ATOM   8250  C C   . LEU E  2 159 ? 146.223 235.191 157.719 1.00 328.20 ? 193 LEU E C   1 
ATOM   8251  O O   . LEU E  2 159 ? 146.889 235.218 156.681 1.00 330.65 ? 193 LEU E O   1 
ATOM   8252  C CB  . LEU E  2 159 ? 143.970 234.280 157.109 1.00 323.65 ? 193 LEU E CB  1 
ATOM   8253  C CG  . LEU E  2 159 ? 142.443 234.401 157.102 1.00 320.78 ? 193 LEU E CG  1 
ATOM   8254  C CD1 . LEU E  2 159 ? 141.835 233.515 156.026 1.00 312.31 ? 193 LEU E CD1 1 
ATOM   8255  C CD2 . LEU E  2 159 ? 141.861 234.071 158.471 1.00 316.57 ? 193 LEU E CD2 1 
ATOM   8256  N N   . SER E  2 160 ? 146.742 234.914 158.913 1.00 324.57 ? 194 SER E N   1 
ATOM   8257  C CA  . SER E  2 160 ? 148.158 234.627 159.094 1.00 321.65 ? 194 SER E CA  1 
ATOM   8258  C C   . SER E  2 160 ? 148.299 233.381 159.956 1.00 316.01 ? 194 SER E C   1 
ATOM   8259  O O   . SER E  2 160 ? 147.362 232.973 160.649 1.00 314.08 ? 194 SER E O   1 
ATOM   8260  C CB  . SER E  2 160 ? 148.898 235.818 159.715 1.00 323.81 ? 194 SER E CB  1 
ATOM   8261  O OG  . SER E  2 160 ? 148.327 236.187 160.957 1.00 322.76 ? 194 SER E OG  1 
ATOM   8262  N N   . ASN E  2 161 ? 149.490 232.784 159.907 1.00 315.10 ? 195 ASN E N   1 
ATOM   8263  C CA  . ASN E  2 161 ? 149.772 231.509 160.564 1.00 313.30 ? 195 ASN E CA  1 
ATOM   8264  C C   . ASN E  2 161 ? 148.754 230.468 160.087 1.00 311.21 ? 195 ASN E C   1 
ATOM   8265  O O   . ASN E  2 161 ? 147.902 229.977 160.830 1.00 309.47 ? 195 ASN E O   1 
ATOM   8266  C CB  . ASN E  2 161 ? 149.796 231.671 162.089 1.00 312.56 ? 195 ASN E CB  1 
ATOM   8267  C CG  . ASN E  2 161 ? 149.859 230.347 162.833 1.00 309.84 ? 195 ASN E CG  1 
ATOM   8268  O OD1 . ASN E  2 161 ? 148.874 229.911 163.430 1.00 306.67 ? 195 ASN E OD1 1 
ATOM   8269  N ND2 . ASN E  2 161 ? 151.018 229.704 162.803 1.00 310.39 ? 195 ASN E ND2 1 
ATOM   8270  N N   . GLY E  2 162 ? 148.834 230.178 158.788 1.00 311.50 ? 196 GLY E N   1 
ATOM   8271  C CA  . GLY E  2 162 ? 147.762 229.501 158.099 1.00 309.18 ? 196 GLY E CA  1 
ATOM   8272  C C   . GLY E  2 162 ? 146.551 230.408 158.088 1.00 309.94 ? 196 GLY E C   1 
ATOM   8273  O O   . GLY E  2 162 ? 146.584 231.481 157.471 1.00 313.24 ? 196 GLY E O   1 
ATOM   8274  N N   . ASN E  2 163 ? 145.479 230.001 158.762 1.00 305.71 ? 197 ASN E N   1 
ATOM   8275  C CA  . ASN E  2 163 ? 144.372 230.911 159.028 1.00 306.52 ? 197 ASN E CA  1 
ATOM   8276  C C   . ASN E  2 163 ? 143.872 230.766 160.459 1.00 302.17 ? 197 ASN E C   1 
ATOM   8277  O O   . ASN E  2 163 ? 142.688 230.989 160.737 1.00 302.01 ? 197 ASN E O   1 
ATOM   8278  C CB  . ASN E  2 163 ? 143.231 230.702 158.030 1.00 302.13 ? 197 ASN E CB  1 
ATOM   8279  C CG  . ASN E  2 163 ? 143.072 229.261 157.622 1.00 296.76 ? 197 ASN E CG  1 
ATOM   8280  O OD1 . ASN E  2 163 ? 143.698 228.364 158.182 1.00 295.46 ? 197 ASN E OD1 1 
ATOM   8281  N ND2 . ASN E  2 163 ? 142.209 229.033 156.636 1.00 293.25 ? 197 ASN E ND2 1 
ATOM   8282  N N   . ARG E  2 164 ? 144.768 230.410 161.381 1.00 300.59 ? 198 ARG E N   1 
ATOM   8283  C CA  . ARG E  2 164 ? 144.443 230.420 162.806 1.00 296.55 ? 198 ARG E CA  1 
ATOM   8284  C C   . ARG E  2 164 ? 144.372 231.836 163.366 1.00 304.05 ? 198 ARG E C   1 
ATOM   8285  O O   . ARG E  2 164 ? 143.684 232.065 164.366 1.00 303.81 ? 198 ARG E O   1 
ATOM   8286  C CB  . ARG E  2 164 ? 145.463 229.573 163.570 1.00 292.79 ? 198 ARG E CB  1 
ATOM   8287  C CG  . ARG E  2 164 ? 145.916 230.137 164.907 1.00 293.47 ? 198 ARG E CG  1 
ATOM   8288  C CD  . ARG E  2 164 ? 146.724 229.115 165.679 1.00 289.51 ? 198 ARG E CD  1 
ATOM   8289  N NE  . ARG E  2 164 ? 145.895 227.968 166.024 1.00 284.95 ? 198 ARG E NE  1 
ATOM   8290  C CZ  . ARG E  2 164 ? 145.775 227.480 167.250 1.00 282.97 ? 198 ARG E CZ  1 
ATOM   8291  N NH1 . ARG E  2 164 ? 146.436 228.005 168.268 1.00 284.08 ? 198 ARG E NH1 1 
ATOM   8292  N NH2 . ARG E  2 164 ? 144.952 226.457 167.464 1.00 279.32 ? 198 ARG E NH2 1 
ATOM   8293  N N   . THR E  2 165 ? 145.049 232.790 162.733 1.00 307.86 ? 199 THR E N   1 
ATOM   8294  C CA  . THR E  2 165 ? 145.011 234.190 163.134 1.00 311.66 ? 199 THR E CA  1 
ATOM   8295  C C   . THR E  2 165 ? 144.215 234.982 162.105 1.00 316.37 ? 199 THR E C   1 
ATOM   8296  O O   . THR E  2 165 ? 144.514 234.927 160.908 1.00 319.05 ? 199 THR E O   1 
ATOM   8297  C CB  . THR E  2 165 ? 146.421 234.771 163.267 1.00 312.39 ? 199 THR E CB  1 
ATOM   8298  O OG1 . THR E  2 165 ? 147.103 234.150 164.362 1.00 308.59 ? 199 THR E OG1 1 
ATOM   8299  C CG2 . THR E  2 165 ? 146.358 236.277 163.503 1.00 317.31 ? 199 THR E CG2 1 
ATOM   8300  N N   . LEU E  2 166 ? 143.208 235.714 162.574 1.00 319.16 ? 200 LEU E N   1 
ATOM   8301  C CA  . LEU E  2 166 ? 142.390 236.570 161.726 1.00 325.08 ? 200 LEU E CA  1 
ATOM   8302  C C   . LEU E  2 166 ? 142.694 238.017 162.084 1.00 333.51 ? 200 LEU E C   1 
ATOM   8303  O O   . LEU E  2 166 ? 142.451 238.442 163.218 1.00 333.51 ? 200 LEU E O   1 
ATOM   8304  C CB  . LEU E  2 166 ? 140.899 236.253 161.902 1.00 318.48 ? 200 LEU E CB  1 
ATOM   8305  C CG  . LEU E  2 166 ? 139.799 237.096 161.237 1.00 320.23 ? 200 LEU E CG  1 
ATOM   8306  C CD1 . LEU E  2 166 ? 139.439 238.357 162.030 1.00 325.17 ? 200 LEU E CD1 1 
ATOM   8307  C CD2 . LEU E  2 166 ? 140.178 237.450 159.802 1.00 330.63 ? 200 LEU E CD2 1 
ATOM   8308  N N   . THR E  2 167 ? 143.227 238.766 161.123 1.00 340.48 ? 201 THR E N   1 
ATOM   8309  C CA  . THR E  2 167 ? 143.579 240.167 161.319 1.00 346.32 ? 201 THR E CA  1 
ATOM   8310  C C   . THR E  2 167 ? 142.618 241.030 160.516 1.00 351.21 ? 201 THR E C   1 
ATOM   8311  O O   . THR E  2 167 ? 142.421 240.796 159.318 1.00 351.22 ? 201 THR E O   1 
ATOM   8312  C CB  . THR E  2 167 ? 145.025 240.440 160.901 1.00 348.09 ? 201 THR E CB  1 
ATOM   8313  O OG1 . THR E  2 167 ? 145.881 239.427 161.445 1.00 343.49 ? 201 THR E OG1 1 
ATOM   8314  C CG2 . THR E  2 167 ? 145.478 241.804 161.404 1.00 351.59 ? 201 THR E CG2 1 
ATOM   8315  N N   . LEU E  2 168 ? 142.025 242.022 161.174 1.00 355.78 ? 202 LEU E N   1 
ATOM   8316  C CA  . LEU E  2 168 ? 141.098 242.944 160.528 1.00 360.12 ? 202 LEU E CA  1 
ATOM   8317  C C   . LEU E  2 168 ? 141.870 244.199 160.136 1.00 363.55 ? 202 LEU E C   1 
ATOM   8318  O O   . LEU E  2 168 ? 142.273 244.981 161.002 1.00 364.92 ? 202 LEU E O   1 
ATOM   8319  C CB  . LEU E  2 168 ? 139.934 243.273 161.459 1.00 358.88 ? 202 LEU E CB  1 
ATOM   8320  C CG  . LEU E  2 168 ? 138.747 243.984 160.812 1.00 360.73 ? 202 LEU E CG  1 
ATOM   8321  C CD1 . LEU E  2 168 ? 138.519 243.434 159.421 1.00 360.18 ? 202 LEU E CD1 1 
ATOM   8322  C CD2 . LEU E  2 168 ? 137.498 243.831 161.664 1.00 358.96 ? 202 LEU E CD2 1 
ATOM   8323  N N   . LEU E  2 169 ? 142.070 244.392 158.829 1.00 364.47 ? 203 LEU E N   1 
ATOM   8324  C CA  . LEU E  2 169 ? 142.948 245.461 158.359 1.00 365.53 ? 203 LEU E CA  1 
ATOM   8325  C C   . LEU E  2 169 ? 142.421 246.841 158.740 1.00 368.64 ? 203 LEU E C   1 
ATOM   8326  O O   . LEU E  2 169 ? 143.191 247.707 159.171 1.00 369.20 ? 203 LEU E O   1 
ATOM   8327  C CB  . LEU E  2 169 ? 143.132 245.358 156.845 1.00 363.49 ? 203 LEU E CB  1 
ATOM   8328  C CG  . LEU E  2 169 ? 143.652 244.018 156.320 1.00 359.41 ? 203 LEU E CG  1 
ATOM   8329  C CD1 . LEU E  2 169 ? 144.008 244.121 154.847 1.00 357.64 ? 203 LEU E CD1 1 
ATOM   8330  C CD2 . LEU E  2 169 ? 144.855 243.562 157.131 1.00 358.29 ? 203 LEU E CD2 1 
ATOM   8331  N N   . SER E  2 170 ? 141.118 247.068 158.587 1.00 368.58 ? 204 SER E N   1 
ATOM   8332  C CA  . SER E  2 170 ? 140.524 248.375 158.858 1.00 369.02 ? 204 SER E CA  1 
ATOM   8333  C C   . SER E  2 170 ? 139.155 248.161 159.487 1.00 368.12 ? 204 SER E C   1 
ATOM   8334  O O   . SER E  2 170 ? 138.185 247.876 158.779 1.00 367.08 ? 204 SER E O   1 
ATOM   8335  C CB  . SER E  2 170 ? 140.413 249.208 157.581 1.00 370.09 ? 204 SER E CB  1 
ATOM   8336  O OG  . SER E  2 170 ? 141.679 249.711 157.189 1.00 370.39 ? 204 SER E OG  1 
ATOM   8337  N N   . VAL E  2 171 ? 139.073 248.310 160.805 1.00 368.27 ? 205 VAL E N   1 
ATOM   8338  C CA  . VAL E  2 171 ? 137.827 248.060 161.520 1.00 368.26 ? 205 VAL E CA  1 
ATOM   8339  C C   . VAL E  2 171 ? 136.910 249.268 161.391 1.00 368.79 ? 205 VAL E C   1 
ATOM   8340  O O   . VAL E  2 171 ? 137.351 250.397 161.143 1.00 368.23 ? 205 VAL E O   1 
ATOM   8341  C CB  . VAL E  2 171 ? 138.103 247.726 163.000 1.00 366.72 ? 205 VAL E CB  1 
ATOM   8342  C CG1 . VAL E  2 171 ? 139.257 246.745 163.121 1.00 365.71 ? 205 VAL E CG1 1 
ATOM   8343  C CG2 . VAL E  2 171 ? 138.372 248.993 163.796 1.00 365.82 ? 205 VAL E CG2 1 
ATOM   8344  N N   . THR E  2 172 ? 135.611 249.023 161.549 1.00 369.19 ? 206 THR E N   1 
ATOM   8345  C CA  . THR E  2 172 ? 134.605 250.073 161.595 1.00 368.28 ? 206 THR E CA  1 
ATOM   8346  C C   . THR E  2 172 ? 133.629 249.759 162.719 1.00 366.94 ? 206 THR E C   1 
ATOM   8347  O O   . THR E  2 172 ? 133.527 248.614 163.167 1.00 366.76 ? 206 THR E O   1 
ATOM   8348  C CB  . THR E  2 172 ? 133.835 250.215 160.270 1.00 368.57 ? 206 THR E CB  1 
ATOM   8349  O OG1 . THR E  2 172 ? 133.100 249.013 160.008 1.00 369.40 ? 206 THR E OG1 1 
ATOM   8350  C CG2 . THR E  2 172 ? 134.783 250.494 159.110 1.00 368.06 ? 206 THR E CG2 1 
ATOM   8351  N N   . ARG E  2 173 ? 132.916 250.791 163.177 1.00 364.62 ? 207 ARG E N   1 
ATOM   8352  C CA  . ARG E  2 173 ? 131.925 250.585 164.228 1.00 361.18 ? 207 ARG E CA  1 
ATOM   8353  C C   . ARG E  2 173 ? 130.784 249.693 163.755 1.00 363.90 ? 207 ARG E C   1 
ATOM   8354  O O   . ARG E  2 173 ? 130.113 249.057 164.576 1.00 363.02 ? 207 ARG E O   1 
ATOM   8355  C CB  . ARG E  2 173 ? 131.383 251.930 164.714 1.00 354.53 ? 207 ARG E CB  1 
ATOM   8356  C CG  . ARG E  2 173 ? 130.836 252.820 163.611 1.00 352.49 ? 207 ARG E CG  1 
ATOM   8357  C CD  . ARG E  2 173 ? 130.023 253.966 164.190 1.00 344.15 ? 207 ARG E CD  1 
ATOM   8358  N NE  . ARG E  2 173 ? 130.704 254.607 165.308 1.00 336.19 ? 207 ARG E NE  1 
ATOM   8359  C CZ  . ARG E  2 173 ? 130.152 255.514 166.102 1.00 330.35 ? 207 ARG E CZ  1 
ATOM   8360  N NH1 . ARG E  2 173 ? 128.903 255.914 165.930 1.00 329.74 ? 207 ARG E NH1 1 
ATOM   8361  N NH2 . ARG E  2 173 ? 130.871 256.033 167.094 1.00 327.08 ? 207 ARG E NH2 1 
ATOM   8362  N N   . ASN E  2 174 ? 130.551 249.629 162.442 1.00 365.87 ? 208 ASN E N   1 
ATOM   8363  C CA  . ASN E  2 174 ? 129.511 248.768 161.894 1.00 365.42 ? 208 ASN E CA  1 
ATOM   8364  C C   . ASN E  2 174 ? 129.883 247.292 161.932 1.00 364.19 ? 208 ASN E C   1 
ATOM   8365  O O   . ASN E  2 174 ? 129.017 246.448 161.679 1.00 362.68 ? 208 ASN E O   1 
ATOM   8366  C CB  . ASN E  2 174 ? 129.194 249.181 160.456 1.00 366.06 ? 208 ASN E CB  1 
ATOM   8367  C CG  . ASN E  2 174 ? 128.075 250.198 160.375 1.00 365.66 ? 208 ASN E CG  1 
ATOM   8368  O OD1 . ASN E  2 174 ? 127.417 250.495 161.373 1.00 364.93 ? 208 ASN E OD1 1 
ATOM   8369  N ND2 . ASN E  2 174 ? 127.852 250.740 159.183 1.00 366.70 ? 208 ASN E ND2 1 
ATOM   8370  N N   . ASP E  2 175 ? 131.136 246.961 162.238 1.00 364.28 ? 209 ASP E N   1 
ATOM   8371  C CA  . ASP E  2 175 ? 131.577 245.573 162.286 1.00 360.51 ? 209 ASP E CA  1 
ATOM   8372  C C   . ASP E  2 175 ? 131.359 244.925 163.645 1.00 354.10 ? 209 ASP E C   1 
ATOM   8373  O O   . ASP E  2 175 ? 131.752 243.767 163.828 1.00 348.63 ? 209 ASP E O   1 
ATOM   8374  C CB  . ASP E  2 175 ? 133.057 245.477 161.910 1.00 363.18 ? 209 ASP E CB  1 
ATOM   8375  C CG  . ASP E  2 175 ? 133.330 245.952 160.501 1.00 367.77 ? 209 ASP E CG  1 
ATOM   8376  O OD1 . ASP E  2 175 ? 132.832 245.316 159.549 1.00 369.01 ? 209 ASP E OD1 1 
ATOM   8377  O OD2 . ASP E  2 175 ? 134.051 246.959 160.342 1.00 369.67 ? 209 ASP E OD2 1 
ATOM   8378  N N   . THR E  2 176 ? 130.755 245.636 164.595 1.00 352.38 ? 210 THR E N   1 
ATOM   8379  C CA  . THR E  2 176 ? 130.545 245.088 165.928 1.00 344.91 ? 210 THR E CA  1 
ATOM   8380  C C   . THR E  2 176 ? 129.663 243.848 165.865 1.00 339.04 ? 210 THR E C   1 
ATOM   8381  O O   . THR E  2 176 ? 128.545 243.889 165.342 1.00 340.41 ? 210 THR E O   1 
ATOM   8382  C CB  . THR E  2 176 ? 129.909 246.140 166.836 1.00 344.36 ? 210 THR E CB  1 
ATOM   8383  O OG1 . THR E  2 176 ? 130.687 247.342 166.790 1.00 346.93 ? 210 THR E OG1 1 
ATOM   8384  C CG2 . THR E  2 176 ? 129.846 245.636 168.270 1.00 337.55 ? 210 THR E CG2 1 
ATOM   8385  N N   . GLY E  2 177 ? 130.173 242.743 166.400 1.00 330.07 ? 211 GLY E N   1 
ATOM   8386  C CA  . GLY E  2 177 ? 129.451 241.496 166.412 1.00 322.57 ? 211 GLY E CA  1 
ATOM   8387  C C   . GLY E  2 177 ? 130.170 240.432 167.214 1.00 316.08 ? 211 GLY E C   1 
ATOM   8388  O O   . GLY E  2 177 ? 131.265 240.651 167.742 1.00 315.88 ? 211 GLY E O   1 
ATOM   8389  N N   . PRO E  2 178 ? 129.563 239.249 167.322 1.00 312.15 ? 212 PRO E N   1 
ATOM   8390  C CA  . PRO E  2 178 ? 130.195 238.159 168.075 1.00 309.03 ? 212 PRO E CA  1 
ATOM   8391  C C   . PRO E  2 178 ? 131.200 237.407 167.212 1.00 307.21 ? 212 PRO E C   1 
ATOM   8392  O O   . PRO E  2 178 ? 130.843 236.813 166.192 1.00 305.64 ? 212 PRO E O   1 
ATOM   8393  C CB  . PRO E  2 178 ? 129.012 237.266 168.469 1.00 306.73 ? 212 PRO E CB  1 
ATOM   8394  C CG  . PRO E  2 178 ? 127.940 237.561 167.448 1.00 305.94 ? 212 PRO E CG  1 
ATOM   8395  C CD  . PRO E  2 178 ? 128.280 238.843 166.725 1.00 308.56 ? 212 PRO E CD  1 
ATOM   8396  N N   . TYR E  2 179 ? 132.462 237.433 167.633 1.00 306.34 ? 213 TYR E N   1 
ATOM   8397  C CA  . TYR E  2 179 ? 133.541 236.724 166.958 1.00 303.79 ? 213 TYR E CA  1 
ATOM   8398  C C   . TYR E  2 179 ? 133.750 235.393 167.662 1.00 298.58 ? 213 TYR E C   1 
ATOM   8399  O O   . TYR E  2 179 ? 133.822 235.341 168.894 1.00 298.35 ? 213 TYR E O   1 
ATOM   8400  C CB  . TYR E  2 179 ? 134.826 237.549 166.950 1.00 305.92 ? 213 TYR E CB  1 
ATOM   8401  C CG  . TYR E  2 179 ? 134.764 238.734 166.017 1.00 308.88 ? 213 TYR E CG  1 
ATOM   8402  C CD1 . TYR E  2 179 ? 134.066 239.880 166.369 1.00 311.96 ? 213 TYR E CD1 1 
ATOM   8403  C CD2 . TYR E  2 179 ? 135.393 238.703 164.780 1.00 310.91 ? 213 TYR E CD2 1 
ATOM   8404  C CE1 . TYR E  2 179 ? 134.000 240.961 165.520 1.00 316.00 ? 213 TYR E CE1 1 
ATOM   8405  C CE2 . TYR E  2 179 ? 135.335 239.784 163.922 1.00 313.51 ? 213 TYR E CE2 1 
ATOM   8406  C CZ  . TYR E  2 179 ? 134.636 240.911 164.298 1.00 318.29 ? 213 TYR E CZ  1 
ATOM   8407  O OH  . TYR E  2 179 ? 134.573 241.991 163.448 1.00 326.37 ? 213 TYR E OH  1 
ATOM   8408  N N   . GLU E  2 180 ? 133.849 234.324 166.879 1.00 293.30 ? 214 GLU E N   1 
ATOM   8409  C CA  . GLU E  2 180 ? 133.749 232.972 167.400 1.00 287.22 ? 214 GLU E CA  1 
ATOM   8410  C C   . GLU E  2 180 ? 134.377 232.015 166.396 1.00 283.90 ? 214 GLU E C   1 
ATOM   8411  O O   . GLU E  2 180 ? 134.012 232.012 165.217 1.00 283.55 ? 214 GLU E O   1 
ATOM   8412  C CB  . GLU E  2 180 ? 132.275 232.630 167.659 1.00 287.10 ? 214 GLU E CB  1 
ATOM   8413  C CG  . GLU E  2 180 ? 131.968 231.177 167.893 1.00 282.20 ? 214 GLU E CG  1 
ATOM   8414  C CD  . GLU E  2 180 ? 130.496 230.935 168.166 1.00 280.97 ? 214 GLU E CD  1 
ATOM   8415  O OE1 . GLU E  2 180 ? 129.990 231.425 169.195 1.00 282.89 ? 214 GLU E OE1 1 
ATOM   8416  O OE2 . GLU E  2 180 ? 129.843 230.257 167.345 1.00 279.30 ? 214 GLU E OE2 1 
ATOM   8417  N N   . CYS E  2 181 ? 135.324 231.200 166.863 1.00 281.46 ? 215 CYS E N   1 
ATOM   8418  C CA  . CYS E  2 181 ? 136.105 230.345 165.977 1.00 278.65 ? 215 CYS E CA  1 
ATOM   8419  C C   . CYS E  2 181 ? 135.989 228.880 166.380 1.00 271.60 ? 215 CYS E C   1 
ATOM   8420  O O   . CYS E  2 181 ? 135.729 228.558 167.544 1.00 269.72 ? 215 CYS E O   1 
ATOM   8421  C CB  . CYS E  2 181 ? 137.582 230.777 165.943 1.00 284.74 ? 215 CYS E CB  1 
ATOM   8422  S SG  . CYS E  2 181 ? 138.642 230.221 167.304 1.00 291.27 ? 215 CYS E SG  1 
ATOM   8423  N N   . GLU E  2 182 ? 136.190 228.003 165.395 1.00 265.80 ? 216 GLU E N   1 
ATOM   8424  C CA  . GLU E  2 182 ? 136.003 226.563 165.507 1.00 257.95 ? 216 GLU E CA  1 
ATOM   8425  C C   . GLU E  2 182 ? 137.306 225.841 165.202 1.00 249.98 ? 216 GLU E C   1 
ATOM   8426  O O   . GLU E  2 182 ? 138.168 226.352 164.482 1.00 252.34 ? 216 GLU E O   1 
ATOM   8427  C CB  . GLU E  2 182 ? 134.910 226.075 164.530 1.00 257.69 ? 216 GLU E CB  1 
ATOM   8428  C CG  . GLU E  2 182 ? 134.521 224.584 164.568 1.00 250.34 ? 216 GLU E CG  1 
ATOM   8429  C CD  . GLU E  2 182 ? 134.168 224.052 165.940 1.00 247.43 ? 216 GLU E CD  1 
ATOM   8430  O OE1 . GLU E  2 182 ? 134.564 222.919 166.269 1.00 239.34 ? 216 GLU E OE1 1 
ATOM   8431  O OE2 . GLU E  2 182 ? 133.455 224.737 166.681 1.00 252.32 ? 216 GLU E OE2 1 
ATOM   8432  N N   . ILE E  2 183 ? 137.440 224.644 165.765 1.00 243.51 ? 217 ILE E N   1 
ATOM   8433  C CA  . ILE E  2 183 ? 138.464 223.686 165.369 1.00 236.50 ? 217 ILE E CA  1 
ATOM   8434  C C   . ILE E  2 183 ? 137.786 222.369 165.007 1.00 230.40 ? 217 ILE E C   1 
ATOM   8435  O O   . ILE E  2 183 ? 136.871 221.920 165.704 1.00 230.73 ? 217 ILE E O   1 
ATOM   8436  C CB  . ILE E  2 183 ? 139.566 223.539 166.445 1.00 237.81 ? 217 ILE E CB  1 
ATOM   8437  C CG1 . ILE E  2 183 ? 139.055 223.416 167.902 1.00 239.59 ? 217 ILE E CG1 1 
ATOM   8438  C CG2 . ILE E  2 183 ? 140.548 224.695 166.351 1.00 245.35 ? 217 ILE E CG2 1 
ATOM   8439  C CD1 . ILE E  2 183 ? 138.074 222.336 168.265 1.00 237.87 ? 217 ILE E CD1 1 
ATOM   8440  N N   . GLN E  2 184 ? 138.175 221.792 163.875 1.00 223.89 ? 218 GLN E N   1 
ATOM   8441  C CA  . GLN E  2 184 ? 137.513 220.582 163.408 1.00 210.97 ? 218 GLN E CA  1 
ATOM   8442  C C   . GLN E  2 184 ? 138.530 219.615 162.828 1.00 202.92 ? 218 GLN E C   1 
ATOM   8443  O O   . GLN E  2 184 ? 139.355 219.991 161.991 1.00 208.33 ? 218 GLN E O   1 
ATOM   8444  C CB  . GLN E  2 184 ? 136.423 220.902 162.374 1.00 211.97 ? 218 GLN E CB  1 
ATOM   8445  C CG  . GLN E  2 184 ? 136.884 221.666 161.149 1.00 221.12 ? 218 GLN E CG  1 
ATOM   8446  C CD  . GLN E  2 184 ? 135.809 221.744 160.082 1.00 227.62 ? 218 GLN E CD  1 
ATOM   8447  O OE1 . GLN E  2 184 ? 136.010 221.309 158.948 1.00 230.59 ? 218 GLN E OE1 1 
ATOM   8448  N NE2 . GLN E  2 184 ? 134.656 222.296 160.443 1.00 230.16 ? 218 GLN E NE2 1 
ATOM   8449  N N   . ASN E  2 185 ? 138.468 218.380 163.292 1.00 187.93 ? 219 ASN E N   1 
ATOM   8450  C CA  . ASN E  2 185 ? 139.204 217.253 162.761 1.00 176.85 ? 219 ASN E CA  1 
ATOM   8451  C C   . ASN E  2 185 ? 138.230 216.265 162.127 1.00 168.98 ? 219 ASN E C   1 
ATOM   8452  O O   . ASN E  2 185 ? 137.010 216.407 162.261 1.00 170.13 ? 219 ASN E O   1 
ATOM   8453  C CB  . ASN E  2 185 ? 140.035 216.594 163.877 1.00 177.82 ? 219 ASN E CB  1 
ATOM   8454  C CG  . ASN E  2 185 ? 139.187 216.054 165.020 1.00 181.22 ? 219 ASN E CG  1 
ATOM   8455  O OD1 . ASN E  2 185 ? 137.979 215.870 164.892 1.00 184.15 ? 219 ASN E OD1 1 
ATOM   8456  N ND2 . ASN E  2 185 ? 139.832 215.794 166.152 1.00 178.55 ? 219 ASN E ND2 1 
ATOM   8457  N N   . PRO E  2 186 ? 138.732 215.264 161.397 1.00 162.99 ? 220 PRO E N   1 
ATOM   8458  C CA  . PRO E  2 186 ? 137.829 214.281 160.776 1.00 162.90 ? 220 PRO E CA  1 
ATOM   8459  C C   . PRO E  2 186 ? 136.831 213.625 161.725 1.00 164.95 ? 220 PRO E C   1 
ATOM   8460  O O   . PRO E  2 186 ? 135.887 212.993 161.237 1.00 164.39 ? 220 PRO E O   1 
ATOM   8461  C CB  . PRO E  2 186 ? 138.799 213.246 160.200 1.00 154.80 ? 220 PRO E CB  1 
ATOM   8462  C CG  . PRO E  2 186 ? 139.969 214.062 159.800 1.00 152.24 ? 220 PRO E CG  1 
ATOM   8463  C CD  . PRO E  2 186 ? 140.096 215.157 160.842 1.00 158.22 ? 220 PRO E CD  1 
ATOM   8464  N N   . VAL E  2 187 ? 136.992 213.742 163.044 1.00 166.71 ? 221 VAL E N   1 
ATOM   8465  C CA  . VAL E  2 187 ? 136.166 212.948 163.949 1.00 168.06 ? 221 VAL E CA  1 
ATOM   8466  C C   . VAL E  2 187 ? 135.239 213.808 164.807 1.00 174.63 ? 221 VAL E C   1 
ATOM   8467  O O   . VAL E  2 187 ? 134.176 213.339 165.233 1.00 177.41 ? 221 VAL E O   1 
ATOM   8468  C CB  . VAL E  2 187 ? 137.047 212.042 164.831 1.00 156.86 ? 221 VAL E CB  1 
ATOM   8469  C CG1 . VAL E  2 187 ? 137.794 212.853 165.868 1.00 166.52 ? 221 VAL E CG1 1 
ATOM   8470  C CG2 . VAL E  2 187 ? 136.209 210.954 165.486 1.00 145.31 ? 221 VAL E CG2 1 
ATOM   8471  N N   . SER E  2 188 ? 135.609 215.061 165.072 1.00 178.08 ? 222 SER E N   1 
ATOM   8472  C CA  . SER E  2 188 ? 134.807 215.863 165.991 1.00 189.25 ? 222 SER E CA  1 
ATOM   8473  C C   . SER E  2 188 ? 135.033 217.349 165.744 1.00 195.03 ? 222 SER E C   1 
ATOM   8474  O O   . SER E  2 188 ? 136.001 217.752 165.093 1.00 193.78 ? 222 SER E O   1 
ATOM   8475  C CB  . SER E  2 188 ? 135.122 215.515 167.449 1.00 196.32 ? 222 SER E CB  1 
ATOM   8476  O OG  . SER E  2 188 ? 136.519 215.510 167.676 1.00 198.13 ? 222 SER E OG  1 
ATOM   8477  N N   . ALA E  2 189 ? 134.111 218.158 166.276 1.00 204.74 ? 223 ALA E N   1 
ATOM   8478  C CA  . ALA E  2 189 ? 134.170 219.613 166.186 1.00 216.65 ? 223 ALA E CA  1 
ATOM   8479  C C   . ALA E  2 189 ? 133.147 220.229 167.135 1.00 228.70 ? 223 ALA E C   1 
ATOM   8480  O O   . ALA E  2 189 ? 131.991 219.799 167.169 1.00 228.73 ? 223 ALA E O   1 
ATOM   8481  C CB  . ALA E  2 189 ? 133.909 220.092 164.752 1.00 218.07 ? 223 ALA E CB  1 
ATOM   8482  N N   . ASN E  2 190 ? 133.576 221.249 167.877 1.00 236.34 ? 224 ASN E N   1 
ATOM   8483  C CA  . ASN E  2 190 ? 132.733 221.936 168.851 1.00 242.74 ? 224 ASN E CA  1 
ATOM   8484  C C   . ASN E  2 190 ? 133.414 223.228 169.297 1.00 246.78 ? 224 ASN E C   1 
ATOM   8485  O O   . ASN E  2 190 ? 134.621 223.415 169.121 1.00 245.03 ? 224 ASN E O   1 
ATOM   8486  C CB  . ASN E  2 190 ? 132.312 220.953 169.958 1.00 244.01 ? 224 ASN E CB  1 
ATOM   8487  C CG  . ASN E  2 190 ? 133.353 220.738 171.057 1.00 246.74 ? 224 ASN E CG  1 
ATOM   8488  O OD1 . ASN E  2 190 ? 134.376 221.421 171.176 1.00 245.29 ? 224 ASN E OD1 1 
ATOM   8489  N ND2 . ASN E  2 190 ? 133.068 219.715 171.854 1.00 248.60 ? 224 ASN E ND2 1 
ATOM   8490  N N   . ARG E  2 191 ? 132.611 224.130 169.865 1.00 251.36 ? 225 ARG E N   1 
ATOM   8491  C CA  . ARG E  2 191 ? 132.787 225.565 169.671 1.00 256.03 ? 225 ARG E CA  1 
ATOM   8492  C C   . ARG E  2 191 ? 133.472 226.228 170.865 1.00 259.97 ? 225 ARG E C   1 
ATOM   8493  O O   . ARG E  2 191 ? 133.555 225.675 171.964 1.00 258.20 ? 225 ARG E O   1 
ATOM   8494  C CB  . ARG E  2 191 ? 131.432 226.229 169.408 1.00 258.78 ? 225 ARG E CB  1 
ATOM   8495  C CG  . ARG E  2 191 ? 131.518 227.506 168.576 1.00 263.92 ? 225 ARG E CG  1 
ATOM   8496  C CD  . ARG E  2 191 ? 132.645 227.349 167.575 1.00 264.87 ? 225 ARG E CD  1 
ATOM   8497  N NE  . ARG E  2 191 ? 132.958 228.532 166.790 1.00 271.83 ? 225 ARG E NE  1 
ATOM   8498  C CZ  . ARG E  2 191 ? 132.700 228.656 165.496 1.00 274.31 ? 225 ARG E CZ  1 
ATOM   8499  N NH1 . ARG E  2 191 ? 132.083 227.702 164.819 1.00 272.81 ? 225 ARG E NH1 1 
ATOM   8500  N NH2 . ARG E  2 191 ? 133.079 229.760 164.863 1.00 278.33 ? 225 ARG E NH2 1 
ATOM   8501  N N   . SER E  2 192 ? 133.965 227.443 170.625 1.00 265.14 ? 226 SER E N   1 
ATOM   8502  C CA  . SER E  2 192 ? 134.516 228.346 171.626 1.00 271.06 ? 226 SER E CA  1 
ATOM   8503  C C   . SER E  2 192 ? 133.443 229.319 172.112 1.00 276.66 ? 226 SER E C   1 
ATOM   8504  O O   . SER E  2 192 ? 132.248 229.157 171.849 1.00 275.44 ? 226 SER E O   1 
ATOM   8505  C CB  . SER E  2 192 ? 135.718 229.099 171.056 1.00 273.81 ? 226 SER E CB  1 
ATOM   8506  O OG  . SER E  2 192 ? 135.320 229.975 170.015 1.00 276.91 ? 226 SER E OG  1 
ATOM   8507  N N   . ASP E  2 193 ? 133.889 230.346 172.828 1.00 281.21 ? 227 ASP E N   1 
ATOM   8508  C CA  . ASP E  2 193 ? 132.970 231.348 173.357 1.00 285.86 ? 227 ASP E CA  1 
ATOM   8509  C C   . ASP E  2 193 ? 132.927 232.564 172.435 1.00 289.32 ? 227 ASP E C   1 
ATOM   8510  O O   . ASP E  2 193 ? 133.983 233.063 172.028 1.00 289.84 ? 227 ASP E O   1 
ATOM   8511  C CB  . ASP E  2 193 ? 133.393 231.771 174.762 1.00 287.13 ? 227 ASP E CB  1 
ATOM   8512  C CG  . ASP E  2 193 ? 134.895 231.909 174.900 1.00 287.30 ? 227 ASP E CG  1 
ATOM   8513  O OD1 . ASP E  2 193 ? 135.627 231.066 174.343 1.00 284.87 ? 227 ASP E OD1 1 
ATOM   8514  O OD2 . ASP E  2 193 ? 135.343 232.868 175.562 1.00 291.38 ? 227 ASP E OD2 1 
ATOM   8515  N N   . PRO E  2 194 ? 131.742 233.061 172.076 1.00 291.24 ? 228 PRO E N   1 
ATOM   8516  C CA  . PRO E  2 194 ? 131.662 234.254 171.217 1.00 293.82 ? 228 PRO E CA  1 
ATOM   8517  C C   . PRO E  2 194 ? 132.374 235.447 171.845 1.00 296.61 ? 228 PRO E C   1 
ATOM   8518  O O   . PRO E  2 194 ? 132.296 235.667 173.056 1.00 295.33 ? 228 PRO E O   1 
ATOM   8519  C CB  . PRO E  2 194 ? 130.153 234.511 171.092 1.00 292.49 ? 228 PRO E CB  1 
ATOM   8520  C CG  . PRO E  2 194 ? 129.467 233.442 171.908 1.00 289.54 ? 228 PRO E CG  1 
ATOM   8521  C CD  . PRO E  2 194 ? 130.453 232.359 172.168 1.00 288.84 ? 228 PRO E CD  1 
ATOM   8522  N N   . VAL E  2 195 ? 133.068 236.221 171.006 1.00 300.40 ? 229 VAL E N   1 
ATOM   8523  C CA  . VAL E  2 195 ? 133.794 237.408 171.443 1.00 305.14 ? 229 VAL E CA  1 
ATOM   8524  C C   . VAL E  2 195 ? 133.250 238.630 170.714 1.00 310.22 ? 229 VAL E C   1 
ATOM   8525  O O   . VAL E  2 195 ? 133.094 238.633 169.489 1.00 310.33 ? 229 VAL E O   1 
ATOM   8526  C CB  . VAL E  2 195 ? 135.311 237.241 171.211 1.00 303.87 ? 229 VAL E CB  1 
ATOM   8527  C CG1 . VAL E  2 195 ? 136.048 238.529 171.543 1.00 307.27 ? 229 VAL E CG1 1 
ATOM   8528  C CG2 . VAL E  2 195 ? 135.848 236.084 172.036 1.00 298.09 ? 229 VAL E CG2 1 
ATOM   8529  N N   . THR E  2 196 ? 132.965 239.686 171.470 1.00 313.78 ? 230 THR E N   1 
ATOM   8530  C CA  . THR E  2 196 ? 132.381 240.906 170.934 1.00 316.70 ? 230 THR E CA  1 
ATOM   8531  C C   . THR E  2 196 ? 133.456 241.954 170.667 1.00 319.19 ? 230 THR E C   1 
ATOM   8532  O O   . THR E  2 196 ? 134.596 241.844 171.126 1.00 318.86 ? 230 THR E O   1 
ATOM   8533  C CB  . THR E  2 196 ? 131.333 241.480 171.894 1.00 317.70 ? 230 THR E CB  1 
ATOM   8534  O OG1 . THR E  2 196 ? 130.651 242.572 171.266 1.00 319.56 ? 230 THR E OG1 1 
ATOM   8535  C CG2 . THR E  2 196 ? 131.998 241.972 173.172 1.00 316.68 ? 230 THR E CG2 1 
ATOM   8536  N N   . LEU E  2 197 ? 133.072 242.978 169.908 1.00 321.87 ? 231 LEU E N   1 
ATOM   8537  C CA  . LEU E  2 197 ? 133.903 244.151 169.670 1.00 325.08 ? 231 LEU E CA  1 
ATOM   8538  C C   . LEU E  2 197 ? 133.454 245.270 170.599 1.00 327.36 ? 231 LEU E C   1 
ATOM   8539  O O   . LEU E  2 197 ? 132.259 245.397 170.889 1.00 327.88 ? 231 LEU E O   1 
ATOM   8540  C CB  . LEU E  2 197 ? 133.814 244.626 168.218 1.00 328.46 ? 231 LEU E CB  1 
ATOM   8541  C CG  . LEU E  2 197 ? 134.796 244.072 167.185 1.00 326.97 ? 231 LEU E CG  1 
ATOM   8542  C CD1 . LEU E  2 197 ? 134.266 244.320 165.783 1.00 332.54 ? 231 LEU E CD1 1 
ATOM   8543  C CD2 . LEU E  2 197 ? 136.173 244.681 167.355 1.00 329.28 ? 231 LEU E CD2 1 
ATOM   8544  N N   . ASN E  2 198 ? 134.405 246.076 171.060 1.00 329.52 ? 232 ASN E N   1 
ATOM   8545  C CA  . ASN E  2 198 ? 134.112 247.210 171.927 1.00 330.41 ? 232 ASN E CA  1 
ATOM   8546  C C   . ASN E  2 198 ? 134.327 248.505 171.152 1.00 332.01 ? 232 ASN E C   1 
ATOM   8547  O O   . ASN E  2 198 ? 135.461 248.836 170.788 1.00 335.60 ? 232 ASN E O   1 
ATOM   8548  C CB  . ASN E  2 198 ? 134.989 247.181 173.179 1.00 330.56 ? 232 ASN E CB  1 
ATOM   8549  C CG  . ASN E  2 198 ? 134.754 248.377 174.082 1.00 329.36 ? 232 ASN E CG  1 
ATOM   8550  O OD1 . ASN E  2 198 ? 135.625 248.760 174.865 1.00 330.32 ? 232 ASN E OD1 1 
ATOM   8551  N ND2 . ASN E  2 198 ? 133.574 248.974 173.977 1.00 328.23 ? 232 ASN E ND2 1 
ATOM   8552  N N   . VAL E  2 199 ? 133.238 249.232 170.905 1.00 331.48 ? 233 VAL E N   1 
ATOM   8553  C CA  . VAL E  2 199 ? 133.275 250.554 170.289 1.00 329.65 ? 233 VAL E CA  1 
ATOM   8554  C C   . VAL E  2 199 ? 132.294 251.446 171.040 1.00 327.26 ? 233 VAL E C   1 
ATOM   8555  O O   . VAL E  2 199 ? 131.543 250.990 171.905 1.00 327.14 ? 233 VAL E O   1 
ATOM   8556  C CB  . VAL E  2 199 ? 132.925 250.519 168.783 1.00 330.90 ? 233 VAL E CB  1 
ATOM   8557  C CG1 . VAL E  2 199 ? 134.026 249.830 167.989 1.00 333.22 ? 233 VAL E CG1 1 
ATOM   8558  C CG2 . VAL E  2 199 ? 131.586 249.836 168.566 1.00 333.17 ? 233 VAL E CG2 1 
ATOM   8559  N N   . THR E  2 200 ? 132.299 252.731 170.704 1.00 324.85 ? 234 THR E N   1 
ATOM   8560  C CA  . THR E  2 200 ? 131.402 253.686 171.345 1.00 321.40 ? 234 THR E CA  1 
ATOM   8561  C C   . THR E  2 200 ? 131.166 254.903 170.456 1.00 319.87 ? 234 THR E C   1 
ATOM   8562  O O   . THR E  2 200 ? 130.038 255.173 170.043 1.00 318.06 ? 234 THR E O   1 
ATOM   8563  C CB  . THR E  2 200 ? 131.954 254.152 172.706 1.00 317.03 ? 234 THR E CB  1 
ATOM   8564  O OG1 . THR E  2 200 ? 131.818 253.096 173.665 1.00 316.96 ? 234 THR E OG1 1 
ATOM   8565  C CG2 . THR E  2 200 ? 131.196 255.375 173.199 1.00 312.38 ? 234 THR E CG2 1 
ATOM   8566  N N   . GLN F  2 1   ? 194.489 161.495 144.658 1.00 129.86 ? 35  GLN F N   1 
ATOM   8567  C CA  . GLN F  2 1   ? 194.840 160.221 145.274 1.00 134.44 ? 35  GLN F CA  1 
ATOM   8568  C C   . GLN F  2 1   ? 195.294 160.386 146.727 1.00 127.80 ? 35  GLN F C   1 
ATOM   8569  O O   . GLN F  2 1   ? 196.112 161.245 147.052 1.00 125.94 ? 35  GLN F O   1 
ATOM   8570  C CB  . GLN F  2 1   ? 195.913 159.506 144.432 1.00 137.85 ? 35  GLN F CB  1 
ATOM   8571  C CG  . GLN F  2 1   ? 197.390 159.879 144.672 1.00 135.94 ? 35  GLN F CG  1 
ATOM   8572  C CD  . GLN F  2 1   ? 197.725 161.363 144.485 1.00 139.69 ? 35  GLN F CD  1 
ATOM   8573  O OE1 . GLN F  2 1   ? 198.853 161.745 144.172 1.00 142.50 ? 35  GLN F OE1 1 
ATOM   8574  N NE2 . GLN F  2 1   ? 196.721 162.209 144.684 1.00 137.35 ? 35  GLN F NE2 1 
ATOM   8575  N N   . LEU F  2 2   ? 194.730 159.564 147.607 1.00 120.41 ? 36  LEU F N   1 
ATOM   8576  C CA  . LEU F  2 2   ? 195.041 159.668 149.025 1.00 111.46 ? 36  LEU F CA  1 
ATOM   8577  C C   . LEU F  2 2   ? 196.249 158.808 149.372 1.00 116.53 ? 36  LEU F C   1 
ATOM   8578  O O   . LEU F  2 2   ? 196.252 157.593 149.159 1.00 123.74 ? 36  LEU F O   1 
ATOM   8579  C CB  . LEU F  2 2   ? 193.833 159.247 149.861 1.00 103.33 ? 36  LEU F CB  1 
ATOM   8580  C CG  . LEU F  2 2   ? 193.801 159.737 151.307 1.00 94.70  ? 36  LEU F CG  1 
ATOM   8581  C CD1 . LEU F  2 2   ? 193.442 161.210 151.360 1.00 106.08 ? 36  LEU F CD1 1 
ATOM   8582  C CD2 . LEU F  2 2   ? 192.810 158.919 152.110 1.00 93.75  ? 36  LEU F CD2 1 
ATOM   8583  N N   . THR F  2 3   ? 197.284 159.450 149.910 1.00 111.77 ? 37  THR F N   1 
ATOM   8584  C CA  . THR F  2 3   ? 198.504 158.761 150.300 1.00 111.34 ? 37  THR F CA  1 
ATOM   8585  C C   . THR F  2 3   ? 198.857 159.129 151.732 1.00 110.35 ? 37  THR F C   1 
ATOM   8586  O O   . THR F  2 3   ? 198.660 160.267 152.165 1.00 111.92 ? 37  THR F O   1 
ATOM   8587  C CB  . THR F  2 3   ? 199.680 159.109 149.375 1.00 115.79 ? 37  THR F CB  1 
ATOM   8588  O OG1 . THR F  2 3   ? 199.926 160.520 149.422 1.00 122.53 ? 37  THR F OG1 1 
ATOM   8589  C CG2 . THR F  2 3   ? 199.377 158.697 147.944 1.00 120.05 ? 37  THR F CG2 1 
ATOM   8590  N N   . THR F  2 4   ? 199.383 158.150 152.464 1.00 109.38 ? 38  THR F N   1 
ATOM   8591  C CA  . THR F  2 4   ? 199.832 158.344 153.834 1.00 109.40 ? 38  THR F CA  1 
ATOM   8592  C C   . THR F  2 4   ? 201.320 158.044 153.914 1.00 111.43 ? 38  THR F C   1 
ATOM   8593  O O   . THR F  2 4   ? 201.830 157.192 153.181 1.00 114.67 ? 38  THR F O   1 
ATOM   8594  C CB  . THR F  2 4   ? 199.068 157.449 154.816 1.00 105.03 ? 38  THR F CB  1 
ATOM   8595  O OG1 . THR F  2 4   ? 199.631 156.133 154.801 1.00 107.44 ? 38  THR F OG1 1 
ATOM   8596  C CG2 . THR F  2 4   ? 197.599 157.371 154.435 1.00 105.82 ? 38  THR F CG2 1 
ATOM   8597  N N   . GLU F  2 5   ? 202.012 158.747 154.805 1.00 109.67 ? 39  GLU F N   1 
ATOM   8598  C CA  . GLU F  2 5   ? 203.457 158.626 154.941 1.00 111.96 ? 39  GLU F CA  1 
ATOM   8599  C C   . GLU F  2 5   ? 203.826 158.601 156.415 1.00 113.50 ? 39  GLU F C   1 
ATOM   8600  O O   . GLU F  2 5   ? 203.491 159.529 157.157 1.00 117.84 ? 39  GLU F O   1 
ATOM   8601  C CB  . GLU F  2 5   ? 204.170 159.783 154.236 1.00 116.42 ? 39  GLU F CB  1 
ATOM   8602  C CG  . GLU F  2 5   ? 205.679 159.770 154.387 1.00 126.12 ? 39  GLU F CG  1 
ATOM   8603  C CD  . GLU F  2 5   ? 206.349 160.846 153.557 1.00 145.65 ? 39  GLU F CD  1 
ATOM   8604  O OE1 . GLU F  2 5   ? 205.834 161.983 153.531 1.00 148.06 ? 39  GLU F OE1 1 
ATOM   8605  O OE2 . GLU F  2 5   ? 207.389 160.555 152.929 1.00 155.32 ? 39  GLU F OE2 1 
ATOM   8606  N N   . SER F  2 6   ? 204.511 157.541 156.833 1.00 111.41 ? 40  SER F N   1 
ATOM   8607  C CA  . SER F  2 6   ? 204.996 157.407 158.199 1.00 109.89 ? 40  SER F CA  1 
ATOM   8608  C C   . SER F  2 6   ? 206.195 158.327 158.385 1.00 114.71 ? 40  SER F C   1 
ATOM   8609  O O   . SER F  2 6   ? 206.976 158.532 157.450 1.00 118.77 ? 40  SER F O   1 
ATOM   8610  C CB  . SER F  2 6   ? 205.374 155.959 158.505 1.00 109.60 ? 40  SER F CB  1 
ATOM   8611  O OG  . SER F  2 6   ? 206.424 155.519 157.662 1.00 118.78 ? 40  SER F OG  1 
ATOM   8612  N N   . MET F  2 7   ? 206.339 158.876 159.585 1.00 111.52 ? 41  MET F N   1 
ATOM   8613  C CA  . MET F  2 7   ? 207.429 159.802 159.891 1.00 112.05 ? 41  MET F CA  1 
ATOM   8614  C C   . MET F  2 7   ? 207.888 159.604 161.327 1.00 107.05 ? 41  MET F C   1 
ATOM   8615  O O   . MET F  2 7   ? 207.210 160.073 162.261 1.00 105.15 ? 41  MET F O   1 
ATOM   8616  C CB  . MET F  2 7   ? 206.986 161.247 159.669 1.00 114.55 ? 41  MET F CB  1 
ATOM   8617  C CG  . MET F  2 7   ? 207.499 161.863 158.379 1.00 120.17 ? 41  MET F CG  1 
ATOM   8618  S SD  . MET F  2 7   ? 209.289 161.740 158.215 1.00 139.07 ? 41  MET F SD  1 
ATOM   8619  C CE  . MET F  2 7   ? 209.777 163.429 158.555 1.00 134.17 ? 41  MET F CE  1 
ATOM   8620  N N   . PRO F  2 8   ? 209.016 158.925 161.566 1.00 105.31 ? 42  PRO F N   1 
ATOM   8621  C CA  . PRO F  2 8   ? 209.891 158.268 160.591 1.00 108.33 ? 42  PRO F CA  1 
ATOM   8622  C C   . PRO F  2 8   ? 209.394 156.875 160.221 1.00 112.58 ? 42  PRO F C   1 
ATOM   8623  O O   . PRO F  2 8   ? 208.481 156.350 160.850 1.00 115.41 ? 42  PRO F O   1 
ATOM   8624  C CB  . PRO F  2 8   ? 211.237 158.230 161.321 1.00 105.52 ? 42  PRO F CB  1 
ATOM   8625  C CG  . PRO F  2 8   ? 210.869 158.105 162.777 1.00 102.56 ? 42  PRO F CG  1 
ATOM   8626  C CD  . PRO F  2 8   ? 209.497 158.730 162.946 1.00 101.13 ? 42  PRO F CD  1 
ATOM   8627  N N   . PHE F  2 9   ? 209.978 156.256 159.192 1.00 114.98 ? 43  PHE F N   1 
ATOM   8628  C CA  . PHE F  2 9   ? 209.556 154.915 158.800 1.00 113.50 ? 43  PHE F CA  1 
ATOM   8629  C C   . PHE F  2 9   ? 209.957 153.881 159.844 1.00 114.60 ? 43  PHE F C   1 
ATOM   8630  O O   . PHE F  2 9   ? 209.194 152.953 160.135 1.00 112.00 ? 43  PHE F O   1 
ATOM   8631  C CB  . PHE F  2 9   ? 210.144 154.560 157.435 1.00 113.62 ? 43  PHE F CB  1 
ATOM   8632  C CG  . PHE F  2 9   ? 209.549 153.325 156.823 1.00 118.20 ? 43  PHE F CG  1 
ATOM   8633  C CD1 . PHE F  2 9   ? 210.083 152.075 157.089 1.00 118.75 ? 43  PHE F CD1 1 
ATOM   8634  C CD2 . PHE F  2 9   ? 208.453 153.413 155.983 1.00 122.68 ? 43  PHE F CD2 1 
ATOM   8635  C CE1 . PHE F  2 9   ? 209.537 150.938 156.527 1.00 121.69 ? 43  PHE F CE1 1 
ATOM   8636  C CE2 . PHE F  2 9   ? 207.902 152.279 155.418 1.00 122.42 ? 43  PHE F CE2 1 
ATOM   8637  C CZ  . PHE F  2 9   ? 208.444 151.041 155.691 1.00 122.19 ? 43  PHE F CZ  1 
ATOM   8638  N N   . ASN F  2 10  ? 211.149 154.020 160.414 1.00 117.22 ? 44  ASN F N   1 
ATOM   8639  C CA  . ASN F  2 10  ? 211.643 153.118 161.444 1.00 115.21 ? 44  ASN F CA  1 
ATOM   8640  C C   . ASN F  2 10  ? 211.739 153.863 162.767 1.00 117.39 ? 44  ASN F C   1 
ATOM   8641  O O   . ASN F  2 10  ? 212.382 154.914 162.854 1.00 124.04 ? 44  ASN F O   1 
ATOM   8642  C CB  . ASN F  2 10  ? 213.008 152.543 161.063 1.00 119.07 ? 44  ASN F CB  1 
ATOM   8643  C CG  . ASN F  2 10  ? 213.005 151.900 159.693 1.00 123.23 ? 44  ASN F CG  1 
ATOM   8644  O OD1 . ASN F  2 10  ? 212.442 150.822 159.502 1.00 126.18 ? 44  ASN F OD1 1 
ATOM   8645  N ND2 . ASN F  2 10  ? 213.633 152.560 158.728 1.00 124.77 ? 44  ASN F ND2 1 
ATOM   8646  N N   . VAL F  2 11  ? 211.099 153.315 163.796 1.00 110.34 ? 45  VAL F N   1 
ATOM   8647  C CA  . VAL F  2 11  ? 210.994 153.971 165.093 1.00 109.91 ? 45  VAL F CA  1 
ATOM   8648  C C   . VAL F  2 11  ? 211.606 153.074 166.157 1.00 119.41 ? 45  VAL F C   1 
ATOM   8649  O O   . VAL F  2 11  ? 211.358 151.865 166.186 1.00 128.56 ? 45  VAL F O   1 
ATOM   8650  C CB  . VAL F  2 11  ? 209.530 154.303 165.446 1.00 107.82 ? 45  VAL F CB  1 
ATOM   8651  C CG1 . VAL F  2 11  ? 209.101 155.585 164.766 1.00 114.27 ? 45  VAL F CG1 1 
ATOM   8652  C CG2 . VAL F  2 11  ? 208.616 153.158 165.049 1.00 106.82 ? 45  VAL F CG2 1 
ATOM   8653  N N   . ALA F  2 12  ? 212.417 153.670 167.025 1.00 123.31 ? 46  ALA F N   1 
ATOM   8654  C CA  . ALA F  2 12  ? 212.909 152.971 168.200 1.00 140.33 ? 46  ALA F CA  1 
ATOM   8655  C C   . ALA F  2 12  ? 211.767 152.734 169.180 1.00 144.31 ? 46  ALA F C   1 
ATOM   8656  O O   . ALA F  2 12  ? 210.791 153.488 169.221 1.00 145.89 ? 46  ALA F O   1 
ATOM   8657  C CB  . ALA F  2 12  ? 214.025 153.768 168.874 1.00 144.95 ? 46  ALA F CB  1 
ATOM   8658  N N   . GLU F  2 13  ? 211.891 151.668 169.966 1.00 139.68 ? 47  GLU F N   1 
ATOM   8659  C CA  . GLU F  2 13  ? 210.843 151.323 170.917 1.00 133.67 ? 47  GLU F CA  1 
ATOM   8660  C C   . GLU F  2 13  ? 210.669 152.427 171.954 1.00 139.91 ? 47  GLU F C   1 
ATOM   8661  O O   . GLU F  2 13  ? 211.642 153.000 172.448 1.00 145.67 ? 47  GLU F O   1 
ATOM   8662  C CB  . GLU F  2 13  ? 211.168 149.999 171.608 1.00 139.01 ? 47  GLU F CB  1 
ATOM   8663  C CG  . GLU F  2 13  ? 210.432 148.805 171.028 1.00 144.84 ? 47  GLU F CG  1 
ATOM   8664  C CD  . GLU F  2 13  ? 210.490 147.591 171.933 1.00 153.60 ? 47  GLU F CD  1 
ATOM   8665  O OE1 . GLU F  2 13  ? 211.525 146.893 171.929 1.00 156.69 ? 47  GLU F OE1 1 
ATOM   8666  O OE2 . GLU F  2 13  ? 209.499 147.336 172.649 1.00 152.23 ? 47  GLU F OE2 1 
ATOM   8667  N N   . GLY F  2 14  ? 209.413 152.724 172.280 1.00 135.56 ? 48  GLY F N   1 
ATOM   8668  C CA  . GLY F  2 14  ? 209.086 153.741 173.251 1.00 133.84 ? 48  GLY F CA  1 
ATOM   8669  C C   . GLY F  2 14  ? 209.063 155.156 172.713 1.00 131.51 ? 48  GLY F C   1 
ATOM   8670  O O   . GLY F  2 14  ? 208.723 156.080 173.459 1.00 135.59 ? 48  GLY F O   1 
ATOM   8671  N N   . LYS F  2 15  ? 209.413 155.354 171.447 1.00 127.51 ? 49  LYS F N   1 
ATOM   8672  C CA  . LYS F  2 15  ? 209.337 156.665 170.823 1.00 126.36 ? 49  LYS F CA  1 
ATOM   8673  C C   . LYS F  2 15  ? 207.953 156.842 170.201 1.00 126.71 ? 49  LYS F C   1 
ATOM   8674  O O   . LYS F  2 15  ? 207.040 156.043 170.427 1.00 130.65 ? 49  LYS F O   1 
ATOM   8675  C CB  . LYS F  2 15  ? 210.458 156.831 169.799 1.00 125.65 ? 49  LYS F CB  1 
ATOM   8676  C CG  . LYS F  2 15  ? 211.854 156.889 170.402 1.00 130.06 ? 49  LYS F CG  1 
ATOM   8677  C CD  . LYS F  2 15  ? 211.855 157.601 171.747 1.00 131.69 ? 49  LYS F CD  1 
ATOM   8678  C CE  . LYS F  2 15  ? 213.257 157.681 172.328 1.00 135.69 ? 49  LYS F CE  1 
ATOM   8679  N NZ  . LYS F  2 15  ? 214.302 157.570 171.273 1.00 140.14 ? 49  LYS F NZ  1 
ATOM   8680  N N   . GLU F  2 16  ? 207.779 157.894 169.408 1.00 120.23 ? 50  GLU F N   1 
ATOM   8681  C CA  . GLU F  2 16  ? 206.506 158.176 168.766 1.00 117.60 ? 50  GLU F CA  1 
ATOM   8682  C C   . GLU F  2 16  ? 206.670 158.192 167.254 1.00 113.45 ? 50  GLU F C   1 
ATOM   8683  O O   . GLU F  2 16  ? 207.750 158.480 166.730 1.00 117.81 ? 50  GLU F O   1 
ATOM   8684  C CB  . GLU F  2 16  ? 205.920 159.514 169.236 1.00 122.10 ? 50  GLU F CB  1 
ATOM   8685  C CG  . GLU F  2 16  ? 206.659 160.737 168.721 1.00 130.85 ? 50  GLU F CG  1 
ATOM   8686  C CD  . GLU F  2 16  ? 206.438 161.957 169.591 1.00 139.65 ? 50  GLU F CD  1 
ATOM   8687  O OE1 . GLU F  2 16  ? 205.429 161.989 170.326 1.00 138.93 ? 50  GLU F OE1 1 
ATOM   8688  O OE2 . GLU F  2 16  ? 207.271 162.887 169.537 1.00 145.75 ? 50  GLU F OE2 1 
ATOM   8689  N N   . VAL F  2 17  ? 205.584 157.868 166.558 1.00 108.92 ? 51  VAL F N   1 
ATOM   8690  C CA  . VAL F  2 17  ? 205.535 157.890 165.103 1.00 106.31 ? 51  VAL F CA  1 
ATOM   8691  C C   . VAL F  2 17  ? 204.312 158.692 164.680 1.00 105.03 ? 51  VAL F C   1 
ATOM   8692  O O   . VAL F  2 17  ? 203.246 158.591 165.298 1.00 108.09 ? 51  VAL F O   1 
ATOM   8693  C CB  . VAL F  2 17  ? 205.503 156.464 164.509 1.00 107.97 ? 51  VAL F CB  1 
ATOM   8694  C CG1 . VAL F  2 17  ? 204.288 155.693 165.005 1.00 110.08 ? 51  VAL F CG1 1 
ATOM   8695  C CG2 . VAL F  2 17  ? 205.528 156.514 162.989 1.00 111.07 ? 51  VAL F CG2 1 
ATOM   8696  N N   . LEU F  2 18  ? 204.473 159.509 163.644 1.00 100.73 ? 52  LEU F N   1 
ATOM   8697  C CA  . LEU F  2 18  ? 203.405 160.360 163.140 1.00 101.69 ? 52  LEU F CA  1 
ATOM   8698  C C   . LEU F  2 18  ? 203.135 160.020 161.682 1.00 107.04 ? 52  LEU F C   1 
ATOM   8699  O O   . LEU F  2 18  ? 204.051 160.051 160.853 1.00 109.78 ? 52  LEU F O   1 
ATOM   8700  C CB  . LEU F  2 18  ? 203.772 161.838 163.285 1.00 104.32 ? 52  LEU F CB  1 
ATOM   8701  C CG  . LEU F  2 18  ? 202.772 162.851 162.728 1.00 107.37 ? 52  LEU F CG  1 
ATOM   8702  C CD1 . LEU F  2 18  ? 201.459 162.778 163.487 1.00 105.60 ? 52  LEU F CD1 1 
ATOM   8703  C CD2 . LEU F  2 18  ? 203.348 164.256 162.788 1.00 111.58 ? 52  LEU F CD2 1 
ATOM   8704  N N   . LEU F  2 19  ? 201.882 159.701 161.374 1.00 104.27 ? 53  LEU F N   1 
ATOM   8705  C CA  . LEU F  2 19  ? 201.465 159.361 160.021 1.00 105.90 ? 53  LEU F CA  1 
ATOM   8706  C C   . LEU F  2 19  ? 200.851 160.593 159.369 1.00 110.63 ? 53  LEU F C   1 
ATOM   8707  O O   . LEU F  2 19  ? 199.819 161.092 159.829 1.00 108.48 ? 53  LEU F O   1 
ATOM   8708  C CB  . LEU F  2 19  ? 200.465 158.205 160.031 1.00 94.72  ? 53  LEU F CB  1 
ATOM   8709  C CG  . LEU F  2 19  ? 200.848 156.954 160.823 1.00 84.04  ? 53  LEU F CG  1 
ATOM   8710  C CD1 . LEU F  2 19  ? 199.753 155.909 160.725 1.00 82.62  ? 53  LEU F CD1 1 
ATOM   8711  C CD2 . LEU F  2 19  ? 202.165 156.390 160.327 1.00 92.71  ? 53  LEU F CD2 1 
ATOM   8712  N N   . LEU F  2 20  ? 201.478 161.073 158.302 1.00 110.89 ? 54  LEU F N   1 
ATOM   8713  C CA  . LEU F  2 20  ? 201.000 162.235 157.570 1.00 102.28 ? 54  LEU F CA  1 
ATOM   8714  C C   . LEU F  2 20  ? 200.011 161.813 156.490 1.00 103.98 ? 54  LEU F C   1 
ATOM   8715  O O   . LEU F  2 20  ? 200.040 160.685 155.994 1.00 107.49 ? 54  LEU F O   1 
ATOM   8716  C CB  . LEU F  2 20  ? 202.167 162.999 156.941 1.00 104.27 ? 54  LEU F CB  1 
ATOM   8717  C CG  . LEU F  2 20  ? 203.269 163.458 157.896 1.00 106.26 ? 54  LEU F CG  1 
ATOM   8718  C CD1 . LEU F  2 20  ? 204.306 164.289 157.159 1.00 113.87 ? 54  LEU F CD1 1 
ATOM   8719  C CD2 . LEU F  2 20  ? 202.675 164.243 159.054 1.00 108.52 ? 54  LEU F CD2 1 
ATOM   8720  N N   . VAL F  2 21  ? 199.127 162.740 156.133 1.00 101.72 ? 55  VAL F N   1 
ATOM   8721  C CA  . VAL F  2 21  ? 198.124 162.521 155.100 1.00 103.09 ? 55  VAL F CA  1 
ATOM   8722  C C   . VAL F  2 21  ? 198.271 163.612 154.050 1.00 109.62 ? 55  VAL F C   1 
ATOM   8723  O O   . VAL F  2 21  ? 198.375 164.798 154.384 1.00 113.65 ? 55  VAL F O   1 
ATOM   8724  C CB  . VAL F  2 21  ? 196.695 162.512 155.681 1.00 96.80  ? 55  VAL F CB  1 
ATOM   8725  C CG1 . VAL F  2 21  ? 195.683 162.186 154.597 1.00 99.60  ? 55  VAL F CG1 1 
ATOM   8726  C CG2 . VAL F  2 21  ? 196.592 161.520 156.826 1.00 96.29  ? 55  VAL F CG2 1 
ATOM   8727  N N   . HIS F  2 22  ? 198.278 163.213 152.780 1.00 111.43 ? 56  HIS F N   1 
ATOM   8728  C CA  . HIS F  2 22  ? 198.450 164.138 151.672 1.00 113.04 ? 56  HIS F CA  1 
ATOM   8729  C C   . HIS F  2 22  ? 197.269 164.034 150.720 1.00 116.85 ? 56  HIS F C   1 
ATOM   8730  O O   . HIS F  2 22  ? 196.595 163.003 150.651 1.00 118.72 ? 56  HIS F O   1 
ATOM   8731  C CB  . HIS F  2 22  ? 199.752 163.865 150.908 1.00 114.20 ? 56  HIS F CB  1 
ATOM   8732  C CG  . HIS F  2 22  ? 200.989 164.144 151.703 1.00 113.96 ? 56  HIS F CG  1 
ATOM   8733  N ND1 . HIS F  2 22  ? 201.488 165.417 151.879 1.00 116.21 ? 56  HIS F ND1 1 
ATOM   8734  C CD2 . HIS F  2 22  ? 201.828 163.315 152.366 1.00 115.47 ? 56  HIS F CD2 1 
ATOM   8735  C CE1 . HIS F  2 22  ? 202.581 165.359 152.619 1.00 121.17 ? 56  HIS F CE1 1 
ATOM   8736  N NE2 . HIS F  2 22  ? 202.809 164.096 152.927 1.00 122.88 ? 56  HIS F NE2 1 
ATOM   8737  N N   . ASN F  2 23  ? 197.031 165.122 149.983 1.00 115.27 ? 57  ASN F N   1 
ATOM   8738  C CA  . ASN F  2 23  ? 195.973 165.186 148.974 1.00 117.47 ? 57  ASN F CA  1 
ATOM   8739  C C   . ASN F  2 23  ? 194.609 164.859 149.575 1.00 113.45 ? 57  ASN F C   1 
ATOM   8740  O O   . ASN F  2 23  ? 193.793 164.160 148.971 1.00 112.48 ? 57  ASN F O   1 
ATOM   8741  C CB  . ASN F  2 23  ? 196.281 164.264 147.794 1.00 122.43 ? 57  ASN F CB  1 
ATOM   8742  C CG  . ASN F  2 23  ? 197.711 164.393 147.313 1.00 125.49 ? 57  ASN F CG  1 
ATOM   8743  O OD1 . ASN F  2 23  ? 198.340 163.409 146.928 1.00 126.69 ? 57  ASN F OD1 1 
ATOM   8744  N ND2 . ASN F  2 23  ? 198.230 165.615 147.324 1.00 124.18 ? 57  ASN F ND2 1 
ATOM   8745  N N   . LEU F  2 24  ? 194.365 165.362 150.776 1.00 109.73 ? 58  LEU F N   1 
ATOM   8746  C CA  . LEU F  2 24  ? 193.094 165.119 151.444 1.00 109.54 ? 58  LEU F CA  1 
ATOM   8747  C C   . LEU F  2 24  ? 191.969 165.807 150.676 1.00 118.35 ? 58  LEU F C   1 
ATOM   8748  O O   . LEU F  2 24  ? 192.108 166.978 150.305 1.00 127.77 ? 58  LEU F O   1 
ATOM   8749  C CB  . LEU F  2 24  ? 193.156 165.624 152.883 1.00 104.77 ? 58  LEU F CB  1 
ATOM   8750  C CG  . LEU F  2 24  ? 192.105 165.115 153.868 1.00 106.49 ? 58  LEU F CG  1 
ATOM   8751  C CD1 . LEU F  2 24  ? 192.276 163.626 154.098 1.00 105.80 ? 58  LEU F CD1 1 
ATOM   8752  C CD2 . LEU F  2 24  ? 192.220 165.869 155.180 1.00 109.63 ? 58  LEU F CD2 1 
ATOM   8753  N N   . PRO F  2 25  ? 190.856 165.113 150.400 1.00 115.48 ? 59  PRO F N   1 
ATOM   8754  C CA  . PRO F  2 25  ? 189.760 165.730 149.636 1.00 116.28 ? 59  PRO F CA  1 
ATOM   8755  C C   . PRO F  2 25  ? 189.236 167.012 150.266 1.00 123.13 ? 59  PRO F C   1 
ATOM   8756  O O   . PRO F  2 25  ? 189.354 167.214 151.478 1.00 121.66 ? 59  PRO F O   1 
ATOM   8757  C CB  . PRO F  2 25  ? 188.686 164.638 149.626 1.00 114.03 ? 59  PRO F CB  1 
ATOM   8758  C CG  . PRO F  2 25  ? 189.443 163.364 149.735 1.00 112.73 ? 59  PRO F CG  1 
ATOM   8759  C CD  . PRO F  2 25  ? 190.702 163.652 150.514 1.00 114.73 ? 59  PRO F CD  1 
ATOM   8760  N N   . GLN F  2 26  ? 188.664 167.892 149.440 1.00 125.93 ? 60  GLN F N   1 
ATOM   8761  C CA  . GLN F  2 26  ? 188.228 169.196 149.930 1.00 131.15 ? 60  GLN F CA  1 
ATOM   8762  C C   . GLN F  2 26  ? 187.036 169.077 150.872 1.00 129.77 ? 60  GLN F C   1 
ATOM   8763  O O   . GLN F  2 26  ? 187.043 169.653 151.966 1.00 127.49 ? 60  GLN F O   1 
ATOM   8764  C CB  . GLN F  2 26  ? 187.887 170.107 148.752 1.00 133.21 ? 60  GLN F CB  1 
ATOM   8765  C CG  . GLN F  2 26  ? 189.040 170.341 147.789 1.00 140.42 ? 60  GLN F CG  1 
ATOM   8766  C CD  . GLN F  2 26  ? 190.218 171.043 148.437 1.00 147.81 ? 60  GLN F CD  1 
ATOM   8767  O OE1 . GLN F  2 26  ? 190.069 171.731 149.447 1.00 148.57 ? 60  GLN F OE1 1 
ATOM   8768  N NE2 . GLN F  2 26  ? 191.400 170.870 147.857 1.00 153.28 ? 60  GLN F NE2 1 
ATOM   8769  N N   . GLN F  2 27  ? 186.009 168.335 150.472 1.00 128.81 ? 61  GLN F N   1 
ATOM   8770  C CA  . GLN F  2 27  ? 184.780 168.205 151.243 1.00 123.34 ? 61  GLN F CA  1 
ATOM   8771  C C   . GLN F  2 27  ? 184.789 166.876 151.983 1.00 118.56 ? 61  GLN F C   1 
ATOM   8772  O O   . GLN F  2 27  ? 184.778 165.812 151.355 1.00 124.60 ? 61  GLN F O   1 
ATOM   8773  C CB  . GLN F  2 27  ? 183.555 168.300 150.332 1.00 129.10 ? 61  GLN F CB  1 
ATOM   8774  C CG  . GLN F  2 27  ? 183.480 169.584 149.521 1.00 134.69 ? 61  GLN F CG  1 
ATOM   8775  C CD  . GLN F  2 27  ? 183.122 170.790 150.367 1.00 140.35 ? 61  GLN F CD  1 
ATOM   8776  O OE1 . GLN F  2 27  ? 181.947 171.116 150.537 1.00 146.12 ? 61  GLN F OE1 1 
ATOM   8777  N NE2 . GLN F  2 27  ? 184.136 171.462 150.899 1.00 137.68 ? 61  GLN F NE2 1 
ATOM   8778  N N   . LEU F  2 28  ? 184.803 166.938 153.312 1.00 107.48 ? 62  LEU F N   1 
ATOM   8779  C CA  . LEU F  2 28  ? 184.958 165.752 154.139 1.00 105.67 ? 62  LEU F CA  1 
ATOM   8780  C C   . LEU F  2 28  ? 183.862 165.686 155.191 1.00 103.80 ? 62  LEU F C   1 
ATOM   8781  O O   . LEU F  2 28  ? 183.320 166.705 155.627 1.00 104.48 ? 62  LEU F O   1 
ATOM   8782  C CB  . LEU F  2 28  ? 186.327 165.725 154.826 1.00 108.14 ? 62  LEU F CB  1 
ATOM   8783  C CG  . LEU F  2 28  ? 187.528 166.057 153.945 1.00 111.19 ? 62  LEU F CG  1 
ATOM   8784  C CD1 . LEU F  2 28  ? 188.680 166.569 154.787 1.00 116.78 ? 62  LEU F CD1 1 
ATOM   8785  C CD2 . LEU F  2 28  ? 187.940 164.837 153.150 1.00 108.40 ? 62  LEU F CD2 1 
ATOM   8786  N N   . PHE F  2 29  ? 183.549 164.460 155.597 1.00 103.55 ? 63  PHE F N   1 
ATOM   8787  C CA  . PHE F  2 29  ? 182.621 164.193 156.685 1.00 101.47 ? 63  PHE F CA  1 
ATOM   8788  C C   . PHE F  2 29  ? 183.295 163.644 157.932 1.00 100.87 ? 63  PHE F C   1 
ATOM   8789  O O   . PHE F  2 29  ? 182.749 163.795 159.026 1.00 103.19 ? 63  PHE F O   1 
ATOM   8790  C CB  . PHE F  2 29  ? 181.536 163.204 156.229 1.00 104.01 ? 63  PHE F CB  1 
ATOM   8791  C CG  . PHE F  2 29  ? 180.435 163.007 157.231 1.00 102.37 ? 63  PHE F CG  1 
ATOM   8792  C CD1 . PHE F  2 29  ? 179.428 163.945 157.368 1.00 103.12 ? 63  PHE F CD1 1 
ATOM   8793  C CD2 . PHE F  2 29  ? 180.408 161.879 158.034 1.00 101.48 ? 63  PHE F CD2 1 
ATOM   8794  C CE1 . PHE F  2 29  ? 178.416 163.762 158.289 1.00 103.39 ? 63  PHE F CE1 1 
ATOM   8795  C CE2 . PHE F  2 29  ? 179.400 161.693 158.956 1.00 102.64 ? 63  PHE F CE2 1 
ATOM   8796  C CZ  . PHE F  2 29  ? 178.402 162.635 159.084 1.00 103.78 ? 63  PHE F CZ  1 
ATOM   8797  N N   . GLY F  2 30  ? 184.461 163.024 157.800 1.00 98.51  ? 64  GLY F N   1 
ATOM   8798  C CA  . GLY F  2 30  ? 185.162 162.489 158.952 1.00 97.33  ? 64  GLY F CA  1 
ATOM   8799  C C   . GLY F  2 30  ? 186.213 161.496 158.510 1.00 94.33  ? 64  GLY F C   1 
ATOM   8800  O O   . GLY F  2 30  ? 186.269 161.089 157.345 1.00 94.49  ? 64  GLY F O   1 
ATOM   8801  N N   . TYR F  2 31  ? 187.052 161.108 159.468 1.00 93.11  ? 65  TYR F N   1 
ATOM   8802  C CA  . TYR F  2 31  ? 188.132 160.165 159.230 1.00 91.72  ? 65  TYR F CA  1 
ATOM   8803  C C   . TYR F  2 31  ? 188.005 158.975 160.170 1.00 92.98  ? 65  TYR F C   1 
ATOM   8804  O O   . TYR F  2 31  ? 187.175 158.960 161.083 1.00 102.76 ? 65  TYR F O   1 
ATOM   8805  C CB  . TYR F  2 31  ? 189.513 160.807 159.429 1.00 93.37  ? 65  TYR F CB  1 
ATOM   8806  C CG  . TYR F  2 31  ? 189.582 162.292 159.164 1.00 93.86  ? 65  TYR F CG  1 
ATOM   8807  C CD1 . TYR F  2 31  ? 190.094 163.157 160.120 1.00 94.89  ? 65  TYR F CD1 1 
ATOM   8808  C CD2 . TYR F  2 31  ? 189.170 162.826 157.951 1.00 99.40  ? 65  TYR F CD2 1 
ATOM   8809  C CE1 . TYR F  2 31  ? 190.170 164.512 159.888 1.00 105.08 ? 65  TYR F CE1 1 
ATOM   8810  C CE2 . TYR F  2 31  ? 189.242 164.183 157.710 1.00 105.22 ? 65  TYR F CE2 1 
ATOM   8811  C CZ  . TYR F  2 31  ? 189.744 165.021 158.681 1.00 110.97 ? 65  TYR F CZ  1 
ATOM   8812  O OH  . TYR F  2 31  ? 189.822 166.373 158.447 1.00 116.40 ? 65  TYR F OH  1 
ATOM   8813  N N   . SER F  2 32  ? 188.851 157.974 159.933 1.00 84.73  ? 66  SER F N   1 
ATOM   8814  C CA  . SER F  2 32  ? 188.948 156.815 160.810 1.00 85.51  ? 66  SER F CA  1 
ATOM   8815  C C   . SER F  2 32  ? 190.235 156.076 160.486 1.00 87.06  ? 66  SER F C   1 
ATOM   8816  O O   . SER F  2 32  ? 190.593 155.942 159.312 1.00 90.63  ? 66  SER F O   1 
ATOM   8817  C CB  . SER F  2 32  ? 187.741 155.888 160.645 1.00 90.20  ? 66  SER F CB  1 
ATOM   8818  O OG  . SER F  2 32  ? 186.668 156.305 161.468 1.00 94.09  ? 66  SER F OG  1 
ATOM   8819  N N   . TRP F  2 33  ? 190.922 155.599 161.518 1.00 83.40  ? 67  TRP F N   1 
ATOM   8820  C CA  . TRP F  2 33  ? 192.156 154.843 161.363 1.00 81.95  ? 67  TRP F CA  1 
ATOM   8821  C C   . TRP F  2 33  ? 191.937 153.422 161.861 1.00 90.42  ? 67  TRP F C   1 
ATOM   8822  O O   . TRP F  2 33  ? 191.457 153.219 162.980 1.00 97.50  ? 67  TRP F O   1 
ATOM   8823  C CB  . TRP F  2 33  ? 193.307 155.502 162.124 1.00 81.50  ? 67  TRP F CB  1 
ATOM   8824  C CG  . TRP F  2 33  ? 193.952 156.631 161.380 1.00 78.93  ? 67  TRP F CG  1 
ATOM   8825  C CD1 . TRP F  2 33  ? 193.664 157.958 161.496 1.00 83.73  ? 67  TRP F CD1 1 
ATOM   8826  C CD2 . TRP F  2 33  ? 194.994 156.531 160.402 1.00 79.64  ? 67  TRP F CD2 1 
ATOM   8827  N NE1 . TRP F  2 33  ? 194.463 158.691 160.653 1.00 84.14  ? 67  TRP F NE1 1 
ATOM   8828  C CE2 . TRP F  2 33  ? 195.288 157.837 159.970 1.00 77.25  ? 67  TRP F CE2 1 
ATOM   8829  C CE3 . TRP F  2 33  ? 195.706 155.463 159.851 1.00 88.81  ? 67  TRP F CE3 1 
ATOM   8830  C CZ2 . TRP F  2 33  ? 196.263 158.104 159.013 1.00 76.66  ? 67  TRP F CZ2 1 
ATOM   8831  C CZ3 . TRP F  2 33  ? 196.673 155.731 158.901 1.00 85.59  ? 67  TRP F CZ3 1 
ATOM   8832  C CH2 . TRP F  2 33  ? 196.943 157.040 158.492 1.00 75.96  ? 67  TRP F CH2 1 
ATOM   8833  N N   . TYR F  2 34  ? 192.291 152.446 161.031 1.00 91.15  ? 68  TYR F N   1 
ATOM   8834  C CA  . TYR F  2 34  ? 192.104 151.038 161.342 1.00 92.98  ? 68  TYR F CA  1 
ATOM   8835  C C   . TYR F  2 34  ? 193.450 150.330 161.350 1.00 97.34  ? 68  TYR F C   1 
ATOM   8836  O O   . TYR F  2 34  ? 194.315 150.612 160.516 1.00 103.23 ? 68  TYR F O   1 
ATOM   8837  C CB  . TYR F  2 34  ? 191.176 150.365 160.328 1.00 93.19  ? 68  TYR F CB  1 
ATOM   8838  C CG  . TYR F  2 34  ? 189.802 150.983 160.245 1.00 93.20  ? 68  TYR F CG  1 
ATOM   8839  C CD1 . TYR F  2 34  ? 189.548 152.044 159.388 1.00 94.71  ? 68  TYR F CD1 1 
ATOM   8840  C CD2 . TYR F  2 34  ? 188.756 150.503 161.017 1.00 99.87  ? 68  TYR F CD2 1 
ATOM   8841  C CE1 . TYR F  2 34  ? 188.294 152.610 159.307 1.00 99.82  ? 68  TYR F CE1 1 
ATOM   8842  C CE2 . TYR F  2 34  ? 187.498 151.063 160.943 1.00 102.63 ? 68  TYR F CE2 1 
ATOM   8843  C CZ  . TYR F  2 34  ? 187.273 152.116 160.086 1.00 102.37 ? 68  TYR F CZ  1 
ATOM   8844  O OH  . TYR F  2 34  ? 186.022 152.679 160.007 1.00 109.65 ? 68  TYR F OH  1 
ATOM   8845  N N   . LYS F  2 35  ? 193.621 149.410 162.295 1.00 92.13  ? 69  LYS F N   1 
ATOM   8846  C CA  . LYS F  2 35  ? 194.827 148.596 162.355 1.00 95.63  ? 69  LYS F CA  1 
ATOM   8847  C C   . LYS F  2 35  ? 194.705 147.452 161.356 1.00 105.91 ? 69  LYS F C   1 
ATOM   8848  O O   . LYS F  2 35  ? 193.669 146.783 161.295 1.00 114.14 ? 69  LYS F O   1 
ATOM   8849  C CB  . LYS F  2 35  ? 195.042 148.062 163.769 1.00 102.87 ? 69  LYS F CB  1 
ATOM   8850  C CG  . LYS F  2 35  ? 196.100 146.977 163.867 1.00 110.60 ? 69  LYS F CG  1 
ATOM   8851  C CD  . LYS F  2 35  ? 197.249 147.403 164.764 1.00 113.04 ? 69  LYS F CD  1 
ATOM   8852  C CE  . LYS F  2 35  ? 198.121 146.218 165.141 1.00 116.05 ? 69  LYS F CE  1 
ATOM   8853  N NZ  . LYS F  2 35  ? 198.577 145.467 163.939 1.00 116.00 ? 69  LYS F NZ  1 
ATOM   8854  N N   . GLY F  2 36  ? 195.754 147.229 160.579 1.00 105.59 ? 70  GLY F N   1 
ATOM   8855  C CA  . GLY F  2 36  ? 195.761 146.206 159.555 1.00 107.25 ? 70  GLY F CA  1 
ATOM   8856  C C   . GLY F  2 36  ? 195.328 146.751 158.204 1.00 105.13 ? 70  GLY F C   1 
ATOM   8857  O O   . GLY F  2 36  ? 194.849 147.877 158.068 1.00 105.11 ? 70  GLY F O   1 
ATOM   8858  N N   . GLU F  2 37  ? 195.509 145.907 157.188 1.00 108.11 ? 71  GLU F N   1 
ATOM   8859  C CA  . GLU F  2 37  ? 195.193 146.279 155.815 1.00 111.82 ? 71  GLU F CA  1 
ATOM   8860  C C   . GLU F  2 37  ? 193.698 146.366 155.547 1.00 111.21 ? 71  GLU F C   1 
ATOM   8861  O O   . GLU F  2 37  ? 193.304 146.887 154.498 1.00 110.74 ? 71  GLU F O   1 
ATOM   8862  C CB  . GLU F  2 37  ? 195.818 145.276 154.843 1.00 115.48 ? 71  GLU F CB  1 
ATOM   8863  C CG  . GLU F  2 37  ? 197.190 145.670 154.333 1.00 122.72 ? 71  GLU F CG  1 
ATOM   8864  C CD  . GLU F  2 37  ? 198.113 144.478 154.182 1.00 135.09 ? 71  GLU F CD  1 
ATOM   8865  O OE1 . GLU F  2 37  ? 197.612 143.334 154.184 1.00 143.59 ? 71  GLU F OE1 1 
ATOM   8866  O OE2 . GLU F  2 37  ? 199.338 144.684 154.056 1.00 137.65 ? 71  GLU F OE2 1 
ATOM   8867  N N   . ARG F  2 38  ? 192.865 145.876 156.457 1.00 113.08 ? 72  ARG F N   1 
ATOM   8868  C CA  . ARG F  2 38  ? 191.426 145.817 156.261 1.00 118.33 ? 72  ARG F CA  1 
ATOM   8869  C C   . ARG F  2 38  ? 190.751 146.987 156.961 1.00 114.04 ? 72  ARG F C   1 
ATOM   8870  O O   . ARG F  2 38  ? 191.350 147.640 157.821 1.00 114.23 ? 72  ARG F O   1 
ATOM   8871  C CB  . ARG F  2 38  ? 190.859 144.500 156.796 1.00 129.38 ? 72  ARG F CB  1 
ATOM   8872  C CG  . ARG F  2 38  ? 190.901 143.351 155.807 1.00 135.27 ? 72  ARG F CG  1 
ATOM   8873  C CD  . ARG F  2 38  ? 189.635 143.315 154.958 1.00 137.17 ? 72  ARG F CD  1 
ATOM   8874  N NE  . ARG F  2 38  ? 188.402 143.216 155.737 1.00 143.47 ? 72  ARG F NE  1 
ATOM   8875  C CZ  . ARG F  2 38  ? 188.152 142.329 156.695 1.00 148.35 ? 72  ARG F CZ  1 
ATOM   8876  N NH1 . ARG F  2 38  ? 187.077 142.427 157.460 1.00 146.77 ? 72  ARG F NH1 1 
ATOM   8877  N NH2 . ARG F  2 38  ? 188.977 141.300 156.867 1.00 145.52 ? 72  ARG F NH2 1 
ATOM   8878  N N   . VAL F  2 39  ? 189.502 147.246 156.586 1.00 116.80 ? 73  VAL F N   1 
ATOM   8879  C CA  . VAL F  2 39  ? 188.677 148.233 157.272 1.00 112.83 ? 73  VAL F CA  1 
ATOM   8880  C C   . VAL F  2 39  ? 187.568 147.475 157.995 1.00 119.75 ? 73  VAL F C   1 
ATOM   8881  O O   . VAL F  2 39  ? 186.539 147.141 157.403 1.00 125.10 ? 73  VAL F O   1 
ATOM   8882  C CB  . VAL F  2 39  ? 188.108 149.271 156.299 1.00 106.59 ? 73  VAL F CB  1 
ATOM   8883  C CG1 . VAL F  2 39  ? 187.083 150.158 156.994 1.00 100.95 ? 73  VAL F CG1 1 
ATOM   8884  C CG2 . VAL F  2 39  ? 189.233 150.110 155.718 1.00 109.57 ? 73  VAL F CG2 1 
ATOM   8885  N N   . ASP F  2 40  ? 187.790 147.179 159.272 1.00 119.60 ? 74  ASP F N   1 
ATOM   8886  C CA  . ASP F  2 40  ? 186.850 146.412 160.071 1.00 121.21 ? 74  ASP F CA  1 
ATOM   8887  C C   . ASP F  2 40  ? 186.509 147.199 161.326 1.00 120.83 ? 74  ASP F C   1 
ATOM   8888  O O   . ASP F  2 40  ? 187.365 147.875 161.903 1.00 120.39 ? 74  ASP F O   1 
ATOM   8889  C CB  . ASP F  2 40  ? 187.421 145.037 160.443 1.00 124.33 ? 74  ASP F CB  1 
ATOM   8890  C CG  . ASP F  2 40  ? 186.386 144.122 161.064 1.00 132.89 ? 74  ASP F CG  1 
ATOM   8891  O OD1 . ASP F  2 40  ? 185.190 144.480 161.058 1.00 134.40 ? 74  ASP F OD1 1 
ATOM   8892  O OD2 . ASP F  2 40  ? 186.769 143.040 161.558 1.00 136.38 ? 74  ASP F OD2 1 
ATOM   8893  N N   . GLY F  2 41  ? 185.248 147.099 161.748 1.00 121.49 ? 75  GLY F N   1 
ATOM   8894  C CA  . GLY F  2 41  ? 184.806 147.866 162.902 1.00 118.16 ? 75  GLY F CA  1 
ATOM   8895  C C   . GLY F  2 41  ? 185.509 147.458 164.182 1.00 119.10 ? 75  GLY F C   1 
ATOM   8896  O O   . GLY F  2 41  ? 185.644 148.259 165.109 1.00 119.31 ? 75  GLY F O   1 
ATOM   8897  N N   . ASN F  2 42  ? 185.969 146.208 164.249 1.00 120.44 ? 76  ASN F N   1 
ATOM   8898  C CA  . ASN F  2 42  ? 186.692 145.745 165.427 1.00 120.54 ? 76  ASN F CA  1 
ATOM   8899  C C   . ASN F  2 42  ? 188.116 146.280 165.475 1.00 115.87 ? 76  ASN F C   1 
ATOM   8900  O O   . ASN F  2 42  ? 188.729 146.286 166.548 1.00 115.12 ? 76  ASN F O   1 
ATOM   8901  C CB  . ASN F  2 42  ? 186.710 144.218 165.462 1.00 128.76 ? 76  ASN F CB  1 
ATOM   8902  C CG  . ASN F  2 42  ? 185.330 143.624 165.645 1.00 137.73 ? 76  ASN F CG  1 
ATOM   8903  O OD1 . ASN F  2 42  ? 184.451 144.240 166.247 1.00 141.01 ? 76  ASN F OD1 1 
ATOM   8904  N ND2 . ASN F  2 42  ? 185.129 142.420 165.120 1.00 139.35 ? 76  ASN F ND2 1 
ATOM   8905  N N   . ARG F  2 43  ? 188.655 146.726 164.343 1.00 113.71 ? 77  ARG F N   1 
ATOM   8906  C CA  . ARG F  2 43  ? 190.023 147.219 164.268 1.00 111.23 ? 77  ARG F CA  1 
ATOM   8907  C C   . ARG F  2 43  ? 190.121 148.738 164.298 1.00 108.58 ? 77  ARG F C   1 
ATOM   8908  O O   . ARG F  2 43  ? 191.219 149.271 164.112 1.00 109.89 ? 77  ARG F O   1 
ATOM   8909  C CB  . ARG F  2 43  ? 190.705 146.697 163.000 1.00 111.71 ? 77  ARG F CB  1 
ATOM   8910  C CG  . ARG F  2 43  ? 190.435 145.238 162.690 1.00 115.57 ? 77  ARG F CG  1 
ATOM   8911  C CD  . ARG F  2 43  ? 190.887 144.346 163.833 1.00 121.34 ? 77  ARG F CD  1 
ATOM   8912  N NE  . ARG F  2 43  ? 192.340 144.266 163.917 1.00 126.75 ? 77  ARG F NE  1 
ATOM   8913  C CZ  . ARG F  2 43  ? 193.104 143.566 163.088 1.00 129.96 ? 77  ARG F CZ  1 
ATOM   8914  N NH1 . ARG F  2 43  ? 192.586 142.867 162.092 1.00 133.59 ? 77  ARG F NH1 1 
ATOM   8915  N NH2 . ARG F  2 43  ? 194.423 143.569 163.264 1.00 127.09 ? 77  ARG F NH2 1 
ATOM   8916  N N   . GLN F  2 44  ? 189.016 149.447 164.515 1.00 105.25 ? 78  GLN F N   1 
ATOM   8917  C CA  . GLN F  2 44  ? 189.069 150.902 164.509 1.00 99.87  ? 78  GLN F CA  1 
ATOM   8918  C C   . GLN F  2 44  ? 189.875 151.411 165.694 1.00 101.93 ? 78  GLN F C   1 
ATOM   8919  O O   . GLN F  2 44  ? 189.588 151.079 166.847 1.00 107.83 ? 78  GLN F O   1 
ATOM   8920  C CB  . GLN F  2 44  ? 187.660 151.491 164.540 1.00 98.69  ? 78  GLN F CB  1 
ATOM   8921  C CG  . GLN F  2 44  ? 187.632 152.992 164.301 1.00 95.33  ? 78  GLN F CG  1 
ATOM   8922  C CD  . GLN F  2 44  ? 186.254 153.592 164.479 1.00 102.80 ? 78  GLN F CD  1 
ATOM   8923  O OE1 . GLN F  2 44  ? 185.496 153.184 165.357 1.00 113.61 ? 78  GLN F OE1 1 
ATOM   8924  N NE2 . GLN F  2 44  ? 185.924 154.571 163.646 1.00 103.24 ? 78  GLN F NE2 1 
ATOM   8925  N N   . ILE F  2 45  ? 190.883 152.225 165.405 1.00 94.71  ? 79  ILE F N   1 
ATOM   8926  C CA  . ILE F  2 45  ? 191.728 152.823 166.429 1.00 90.97  ? 79  ILE F CA  1 
ATOM   8927  C C   . ILE F  2 45  ? 191.122 154.110 166.961 1.00 95.10  ? 79  ILE F C   1 
ATOM   8928  O O   . ILE F  2 45  ? 190.976 154.285 168.170 1.00 104.25 ? 79  ILE F O   1 
ATOM   8929  C CB  . ILE F  2 45  ? 193.149 153.065 165.875 1.00 85.61  ? 79  ILE F CB  1 
ATOM   8930  C CG1 . ILE F  2 45  ? 193.780 151.747 165.429 1.00 96.30  ? 79  ILE F CG1 1 
ATOM   8931  C CG2 . ILE F  2 45  ? 194.014 153.747 166.915 1.00 90.47  ? 79  ILE F CG2 1 
ATOM   8932  C CD1 . ILE F  2 45  ? 194.979 151.926 164.534 1.00 95.11  ? 79  ILE F CD1 1 
ATOM   8933  N N   . VAL F  2 46  ? 190.758 155.024 166.063 1.00 94.36  ? 80  VAL F N   1 
ATOM   8934  C CA  . VAL F  2 46  ? 190.199 156.312 166.450 1.00 96.35  ? 80  VAL F CA  1 
ATOM   8935  C C   . VAL F  2 46  ? 189.432 156.859 165.257 1.00 95.74  ? 80  VAL F C   1 
ATOM   8936  O O   . VAL F  2 46  ? 189.667 156.464 164.114 1.00 98.24  ? 80  VAL F O   1 
ATOM   8937  C CB  . VAL F  2 46  ? 191.313 157.285 166.915 1.00 92.27  ? 80  VAL F CB  1 
ATOM   8938  C CG1 . VAL F  2 46  ? 192.055 157.852 165.719 1.00 87.48  ? 80  VAL F CG1 1 
ATOM   8939  C CG2 . VAL F  2 46  ? 190.734 158.389 167.784 1.00 99.07  ? 80  VAL F CG2 1 
ATOM   8940  N N   . GLY F  2 47  ? 188.504 157.765 165.523 1.00 91.93  ? 81  GLY F N   1 
ATOM   8941  C CA  . GLY F  2 47  ? 187.716 158.371 164.468 1.00 89.13  ? 81  GLY F CA  1 
ATOM   8942  C C   . GLY F  2 47  ? 187.431 159.823 164.780 1.00 91.71  ? 81  GLY F C   1 
ATOM   8943  O O   . GLY F  2 47  ? 187.265 160.212 165.938 1.00 99.88  ? 81  GLY F O   1 
ATOM   8944  N N   . TYR F  2 48  ? 187.378 160.627 163.723 1.00 89.40  ? 82  TYR F N   1 
ATOM   8945  C CA  . TYR F  2 48  ? 187.104 162.050 163.843 1.00 93.30  ? 82  TYR F CA  1 
ATOM   8946  C C   . TYR F  2 48  ? 185.849 162.377 163.053 1.00 96.73  ? 82  TYR F C   1 
ATOM   8947  O O   . TYR F  2 48  ? 185.621 161.816 161.979 1.00 101.29 ? 82  TYR F O   1 
ATOM   8948  C CB  . TYR F  2 48  ? 188.283 162.891 163.338 1.00 95.93  ? 82  TYR F CB  1 
ATOM   8949  C CG  . TYR F  2 48  ? 188.193 164.356 163.696 1.00 96.44  ? 82  TYR F CG  1 
ATOM   8950  C CD1 . TYR F  2 48  ? 188.240 164.769 165.019 1.00 97.64  ? 82  TYR F CD1 1 
ATOM   8951  C CD2 . TYR F  2 48  ? 188.063 165.325 162.711 1.00 100.15 ? 82  TYR F CD2 1 
ATOM   8952  C CE1 . TYR F  2 48  ? 188.160 166.106 165.352 1.00 100.05 ? 82  TYR F CE1 1 
ATOM   8953  C CE2 . TYR F  2 48  ? 187.981 166.664 163.035 1.00 102.06 ? 82  TYR F CE2 1 
ATOM   8954  C CZ  . TYR F  2 48  ? 188.031 167.048 164.357 1.00 104.44 ? 82  TYR F CZ  1 
ATOM   8955  O OH  . TYR F  2 48  ? 187.950 168.381 164.685 1.00 114.26 ? 82  TYR F OH  1 
ATOM   8956  N N   . ALA F  2 49  ? 185.035 163.280 163.593 1.00 99.21  ? 83  ALA F N   1 
ATOM   8957  C CA  . ALA F  2 49  ? 183.804 163.727 162.950 1.00 100.64 ? 83  ALA F CA  1 
ATOM   8958  C C   . ALA F  2 49  ? 183.875 165.240 162.806 1.00 103.00 ? 83  ALA F C   1 
ATOM   8959  O O   . ALA F  2 49  ? 183.710 165.968 163.790 1.00 108.85 ? 83  ALA F O   1 
ATOM   8960  C CB  . ALA F  2 49  ? 182.576 163.304 163.754 1.00 103.75 ? 83  ALA F CB  1 
ATOM   8961  N N   . ILE F  2 50  ? 184.121 165.709 161.581 1.00 100.02 ? 84  ILE F N   1 
ATOM   8962  C CA  . ILE F  2 50  ? 184.340 167.135 161.348 1.00 101.20 ? 84  ILE F CA  1 
ATOM   8963  C C   . ILE F  2 50  ? 183.107 167.944 161.733 1.00 106.73 ? 84  ILE F C   1 
ATOM   8964  O O   . ILE F  2 50  ? 183.220 169.051 162.273 1.00 109.23 ? 84  ILE F O   1 
ATOM   8965  C CB  . ILE F  2 50  ? 184.748 167.373 159.882 1.00 101.45 ? 84  ILE F CB  1 
ATOM   8966  C CG1 . ILE F  2 50  ? 186.220 167.014 159.685 1.00 102.82 ? 84  ILE F CG1 1 
ATOM   8967  C CG2 . ILE F  2 50  ? 184.498 168.815 159.469 1.00 103.34 ? 84  ILE F CG2 1 
ATOM   8968  C CD1 . ILE F  2 50  ? 186.588 166.737 158.254 1.00 103.83 ? 84  ILE F CD1 1 
ATOM   8969  N N   . GLY F  2 51  ? 181.915 167.405 161.464 1.00 110.79 ? 85  GLY F N   1 
ATOM   8970  C CA  . GLY F  2 51  ? 180.693 168.139 161.756 1.00 114.18 ? 85  GLY F CA  1 
ATOM   8971  C C   . GLY F  2 51  ? 180.604 168.606 163.197 1.00 111.82 ? 85  GLY F C   1 
ATOM   8972  O O   . GLY F  2 51  ? 180.557 169.808 163.467 1.00 111.82 ? 85  GLY F O   1 
ATOM   8973  N N   . THR F  2 52  ? 180.584 167.667 164.140 1.00 110.42 ? 86  THR F N   1 
ATOM   8974  C CA  . THR F  2 52  ? 180.527 167.994 165.557 1.00 113.19 ? 86  THR F CA  1 
ATOM   8975  C C   . THR F  2 52  ? 181.903 168.208 166.174 1.00 117.38 ? 86  THR F C   1 
ATOM   8976  O O   . THR F  2 52  ? 181.985 168.605 167.341 1.00 119.80 ? 86  THR F O   1 
ATOM   8977  C CB  . THR F  2 52  ? 179.783 166.897 166.327 1.00 117.53 ? 86  THR F CB  1 
ATOM   8978  O OG1 . THR F  2 52  ? 180.474 165.651 166.178 1.00 119.72 ? 86  THR F OG1 1 
ATOM   8979  C CG2 . THR F  2 52  ? 178.364 166.750 165.802 1.00 120.46 ? 86  THR F CG2 1 
ATOM   8980  N N   . GLN F  2 53  ? 182.978 167.955 165.425 1.00 116.55 ? 87  GLN F N   1 
ATOM   8981  C CA  . GLN F  2 53  ? 184.351 168.168 165.884 1.00 111.40 ? 87  GLN F CA  1 
ATOM   8982  C C   . GLN F  2 53  ? 184.643 167.348 167.143 1.00 110.28 ? 87  GLN F C   1 
ATOM   8983  O O   . GLN F  2 53  ? 185.080 167.864 168.173 1.00 111.07 ? 87  GLN F O   1 
ATOM   8984  C CB  . GLN F  2 53  ? 184.628 169.658 166.105 1.00 109.14 ? 87  GLN F CB  1 
ATOM   8985  C CG  . GLN F  2 53  ? 184.887 170.419 164.817 1.00 113.27 ? 87  GLN F CG  1 
ATOM   8986  C CD  . GLN F  2 53  ? 185.025 171.910 165.035 1.00 125.96 ? 87  GLN F CD  1 
ATOM   8987  O OE1 . GLN F  2 53  ? 184.934 172.395 166.162 1.00 133.34 ? 87  GLN F OE1 1 
ATOM   8988  N NE2 . GLN F  2 53  ? 185.243 172.647 163.953 1.00 128.40 ? 87  GLN F NE2 1 
ATOM   8989  N N   . GLN F  2 54  ? 184.392 166.045 167.035 1.00 108.12 ? 88  GLN F N   1 
ATOM   8990  C CA  . GLN F  2 54  ? 184.613 165.106 168.125 1.00 108.43 ? 88  GLN F CA  1 
ATOM   8991  C C   . GLN F  2 54  ? 185.583 164.022 167.683 1.00 106.92 ? 88  GLN F C   1 
ATOM   8992  O O   . GLN F  2 54  ? 185.508 163.532 166.553 1.00 107.39 ? 88  GLN F O   1 
ATOM   8993  C CB  . GLN F  2 54  ? 183.299 164.469 168.589 1.00 113.06 ? 88  GLN F CB  1 
ATOM   8994  C CG  . GLN F  2 54  ? 182.765 165.036 169.891 1.00 121.02 ? 88  GLN F CG  1 
ATOM   8995  C CD  . GLN F  2 54  ? 183.556 164.564 171.095 1.00 128.12 ? 88  GLN F CD  1 
ATOM   8996  O OE1 . GLN F  2 54  ? 184.568 165.161 171.460 1.00 131.05 ? 88  GLN F OE1 1 
ATOM   8997  N NE2 . GLN F  2 54  ? 183.099 163.483 171.716 1.00 131.30 ? 88  GLN F NE2 1 
ATOM   8998  N N   . ALA F  2 55  ? 186.492 163.653 168.580 1.00 106.61 ? 89  ALA F N   1 
ATOM   8999  C CA  . ALA F  2 55  ? 187.466 162.592 168.344 1.00 103.60 ? 89  ALA F CA  1 
ATOM   9000  C C   . ALA F  2 55  ? 187.155 161.456 169.313 1.00 103.50 ? 89  ALA F C   1 
ATOM   9001  O O   . ALA F  2 55  ? 187.421 161.561 170.513 1.00 110.29 ? 89  ALA F O   1 
ATOM   9002  C CB  . ALA F  2 55  ? 188.890 163.109 168.522 1.00 106.38 ? 89  ALA F CB  1 
ATOM   9003  N N   . THR F  2 56  ? 186.595 160.368 168.788 1.00 101.67 ? 90  THR F N   1 
ATOM   9004  C CA  . THR F  2 56  ? 186.146 159.258 169.611 1.00 108.10 ? 90  THR F CA  1 
ATOM   9005  C C   . THR F  2 56  ? 187.058 158.056 169.434 1.00 107.25 ? 90  THR F C   1 
ATOM   9006  O O   . THR F  2 56  ? 187.232 157.578 168.305 1.00 107.41 ? 90  THR F O   1 
ATOM   9007  C CB  . THR F  2 56  ? 184.707 158.870 169.256 1.00 111.97 ? 90  THR F CB  1 
ATOM   9008  O OG1 . THR F  2 56  ? 184.630 158.533 167.866 1.00 112.65 ? 90  THR F OG1 1 
ATOM   9009  C CG2 . THR F  2 56  ? 183.761 160.021 169.549 1.00 110.36 ? 90  THR F CG2 1 
ATOM   9010  N N   . PRO F  2 57  ? 187.655 157.549 170.509 1.00 107.89 ? 91  PRO F N   1 
ATOM   9011  C CA  . PRO F  2 57  ? 188.479 156.343 170.395 1.00 106.35 ? 91  PRO F CA  1 
ATOM   9012  C C   . PRO F  2 57  ? 187.647 155.133 170.004 1.00 103.58 ? 91  PRO F C   1 
ATOM   9013  O O   . PRO F  2 57  ? 186.443 155.065 170.260 1.00 106.60 ? 91  PRO F O   1 
ATOM   9014  C CB  . PRO F  2 57  ? 189.064 156.182 171.804 1.00 108.35 ? 91  PRO F CB  1 
ATOM   9015  C CG  . PRO F  2 57  ? 188.100 156.921 172.686 1.00 111.07 ? 91  PRO F CG  1 
ATOM   9016  C CD  . PRO F  2 57  ? 187.699 158.108 171.869 1.00 109.48 ? 91  PRO F CD  1 
ATOM   9017  N N   . GLY F  2 58  ? 188.310 154.170 169.371 1.00 101.33 ? 92  GLY F N   1 
ATOM   9018  C CA  . GLY F  2 58  ? 187.656 152.965 168.923 1.00 103.04 ? 92  GLY F CA  1 
ATOM   9019  C C   . GLY F  2 58  ? 187.990 151.771 169.794 1.00 108.89 ? 92  GLY F C   1 
ATOM   9020  O O   . GLY F  2 58  ? 188.744 151.873 170.765 1.00 113.29 ? 92  GLY F O   1 
ATOM   9021  N N   . PRO F  2 59  ? 187.416 150.612 169.465 1.00 108.04 ? 93  PRO F N   1 
ATOM   9022  C CA  . PRO F  2 59  ? 187.698 149.404 170.258 1.00 107.37 ? 93  PRO F CA  1 
ATOM   9023  C C   . PRO F  2 59  ? 189.166 149.019 170.284 1.00 106.70 ? 93  PRO F C   1 
ATOM   9024  O O   . PRO F  2 59  ? 189.631 148.460 171.285 1.00 110.04 ? 93  PRO F O   1 
ATOM   9025  C CB  . PRO F  2 59  ? 186.843 148.333 169.564 1.00 111.02 ? 93  PRO F CB  1 
ATOM   9026  C CG  . PRO F  2 59  ? 186.623 148.879 168.178 1.00 112.58 ? 93  PRO F CG  1 
ATOM   9027  C CD  . PRO F  2 59  ? 186.427 150.340 168.411 1.00 107.96 ? 93  PRO F CD  1 
ATOM   9028  N N   . ALA F  2 60  ? 189.911 149.297 169.217 1.00 104.50 ? 94  ALA F N   1 
ATOM   9029  C CA  . ALA F  2 60  ? 191.326 148.961 169.151 1.00 103.79 ? 94  ALA F CA  1 
ATOM   9030  C C   . ALA F  2 60  ? 192.216 150.002 169.816 1.00 107.01 ? 94  ALA F C   1 
ATOM   9031  O O   . ALA F  2 60  ? 193.435 149.813 169.862 1.00 110.14 ? 94  ALA F O   1 
ATOM   9032  C CB  . ALA F  2 60  ? 191.757 148.772 167.693 1.00 100.93 ? 94  ALA F CB  1 
ATOM   9033  N N   . ASN F  2 61  ? 191.642 151.091 170.323 1.00 109.07 ? 95  ASN F N   1 
ATOM   9034  C CA  . ASN F  2 61  ? 192.437 152.124 170.970 1.00 114.14 ? 95  ASN F CA  1 
ATOM   9035  C C   . ASN F  2 61  ? 193.069 151.595 172.251 1.00 115.30 ? 95  ASN F C   1 
ATOM   9036  O O   . ASN F  2 61  ? 192.495 150.754 172.948 1.00 115.62 ? 95  ASN F O   1 
ATOM   9037  C CB  . ASN F  2 61  ? 191.571 153.344 171.279 1.00 115.28 ? 95  ASN F CB  1 
ATOM   9038  C CG  . ASN F  2 61  ? 192.393 154.574 171.605 1.00 116.65 ? 95  ASN F CG  1 
ATOM   9039  O OD1 . ASN F  2 61  ? 192.869 154.737 172.728 1.00 120.39 ? 95  ASN F OD1 1 
ATOM   9040  N ND2 . ASN F  2 61  ? 192.563 155.449 170.621 1.00 111.58 ? 95  ASN F ND2 1 
ATOM   9041  N N   . SER F  2 62  ? 194.265 152.096 172.557 1.00 121.19 ? 96  SER F N   1 
ATOM   9042  C CA  . SER F  2 62  ? 194.978 151.732 173.775 1.00 124.89 ? 96  SER F CA  1 
ATOM   9043  C C   . SER F  2 62  ? 195.396 152.950 174.588 1.00 124.74 ? 96  SER F C   1 
ATOM   9044  O O   . SER F  2 62  ? 196.205 152.817 175.514 1.00 122.02 ? 96  SER F O   1 
ATOM   9045  C CB  . SER F  2 62  ? 196.206 150.880 173.438 1.00 121.83 ? 96  SER F CB  1 
ATOM   9046  O OG  . SER F  2 62  ? 197.209 151.661 172.813 1.00 121.12 ? 96  SER F OG  1 
ATOM   9047  N N   . GLY F  2 63  ? 194.871 154.132 174.267 1.00 123.61 ? 97  GLY F N   1 
ATOM   9048  C CA  . GLY F  2 63  ? 195.222 155.347 174.968 1.00 121.64 ? 97  GLY F CA  1 
ATOM   9049  C C   . GLY F  2 63  ? 196.469 156.040 174.470 1.00 122.93 ? 97  GLY F C   1 
ATOM   9050  O O   . GLY F  2 63  ? 196.785 157.133 174.956 1.00 127.31 ? 97  GLY F O   1 
ATOM   9051  N N   . ARG F  2 64  ? 197.189 155.448 173.521 1.00 122.76 ? 98  ARG F N   1 
ATOM   9052  C CA  . ARG F  2 64  ? 198.420 156.019 172.995 1.00 122.04 ? 98  ARG F CA  1 
ATOM   9053  C C   . ARG F  2 64  ? 198.236 156.701 171.647 1.00 116.82 ? 98  ARG F C   1 
ATOM   9054  O O   . ARG F  2 64  ? 199.220 157.183 171.075 1.00 111.31 ? 98  ARG F O   1 
ATOM   9055  C CB  . ARG F  2 64  ? 199.486 154.930 172.862 1.00 120.87 ? 98  ARG F CB  1 
ATOM   9056  C CG  . ARG F  2 64  ? 199.796 154.188 174.146 1.00 118.33 ? 98  ARG F CG  1 
ATOM   9057  C CD  . ARG F  2 64  ? 200.724 153.021 173.865 1.00 118.38 ? 98  ARG F CD  1 
ATOM   9058  N NE  . ARG F  2 64  ? 200.144 152.107 172.889 1.00 118.86 ? 98  ARG F NE  1 
ATOM   9059  C CZ  . ARG F  2 64  ? 200.837 151.461 171.961 1.00 120.97 ? 98  ARG F CZ  1 
ATOM   9060  N NH1 . ARG F  2 64  ? 202.147 151.604 171.852 1.00 126.99 ? 98  ARG F NH1 1 
ATOM   9061  N NH2 . ARG F  2 64  ? 200.198 150.653 171.120 1.00 119.10 ? 98  ARG F NH2 1 
ATOM   9062  N N   . GLU F  2 65  ? 197.015 156.756 171.125 1.00 118.06 ? 99  GLU F N   1 
ATOM   9063  C CA  . GLU F  2 65  ? 196.760 157.228 169.772 1.00 116.52 ? 99  GLU F CA  1 
ATOM   9064  C C   . GLU F  2 65  ? 195.880 158.469 169.810 1.00 120.15 ? 99  GLU F C   1 
ATOM   9065  O O   . GLU F  2 65  ? 194.857 158.491 170.502 1.00 123.11 ? 99  GLU F O   1 
ATOM   9066  C CB  . GLU F  2 65  ? 196.096 156.135 168.932 1.00 111.52 ? 99  GLU F CB  1 
ATOM   9067  C CG  . GLU F  2 65  ? 196.702 154.752 169.123 1.00 113.67 ? 99  GLU F CG  1 
ATOM   9068  C CD  . GLU F  2 65  ? 196.055 153.976 170.254 1.00 124.97 ? 99  GLU F CD  1 
ATOM   9069  O OE1 . GLU F  2 65  ? 195.543 154.613 171.199 1.00 125.91 ? 99  GLU F OE1 1 
ATOM   9070  O OE2 . GLU F  2 65  ? 196.061 152.729 170.200 1.00 127.97 ? 99  GLU F OE2 1 
ATOM   9071  N N   . THR F  2 66  ? 196.283 159.496 169.064 1.00 116.45 ? 100 THR F N   1 
ATOM   9072  C CA  . THR F  2 66  ? 195.524 160.730 168.940 1.00 112.32 ? 100 THR F CA  1 
ATOM   9073  C C   . THR F  2 66  ? 195.347 161.068 167.468 1.00 110.02 ? 100 THR F C   1 
ATOM   9074  O O   . THR F  2 66  ? 196.252 160.863 166.655 1.00 108.68 ? 100 THR F O   1 
ATOM   9075  C CB  . THR F  2 66  ? 196.216 161.899 169.659 1.00 115.78 ? 100 THR F CB  1 
ATOM   9076  O OG1 . THR F  2 66  ? 197.517 162.104 169.096 1.00 116.21 ? 100 THR F OG1 1 
ATOM   9077  C CG2 . THR F  2 66  ? 196.350 161.612 171.147 1.00 116.72 ? 100 THR F CG2 1 
ATOM   9078  N N   . ILE F  2 67  ? 194.172 161.591 167.131 1.00 109.15 ? 101 ILE F N   1 
ATOM   9079  C CA  . ILE F  2 67  ? 193.835 161.975 165.765 1.00 105.80 ? 101 ILE F CA  1 
ATOM   9080  C C   . ILE F  2 67  ? 193.823 163.496 165.694 1.00 107.03 ? 101 ILE F C   1 
ATOM   9081  O O   . ILE F  2 67  ? 193.220 164.162 166.545 1.00 107.38 ? 101 ILE F O   1 
ATOM   9082  C CB  . ILE F  2 67  ? 192.488 161.382 165.321 1.00 101.70 ? 101 ILE F CB  1 
ATOM   9083  C CG1 . ILE F  2 67  ? 192.085 161.918 163.946 1.00 101.49 ? 101 ILE F CG1 1 
ATOM   9084  C CG2 . ILE F  2 67  ? 191.408 161.653 166.354 1.00 103.82 ? 101 ILE F CG2 1 
ATOM   9085  C CD1 . ILE F  2 67  ? 193.062 161.569 162.846 1.00 101.97 ? 101 ILE F CD1 1 
ATOM   9086  N N   . TYR F  2 68  ? 194.496 164.040 164.703 1.00 107.53 ? 102 TYR F N   1 
ATOM   9087  C CA  . TYR F  2 68  ? 194.564 165.481 164.549 1.00 107.69 ? 102 TYR F CA  1 
ATOM   9088  C C   . TYR F  2 68  ? 193.500 165.956 163.569 1.00 109.46 ? 102 TYR F C   1 
ATOM   9089  O O   . TYR F  2 68  ? 193.004 165.175 162.752 1.00 110.86 ? 102 TYR F O   1 
ATOM   9090  C CB  . TYR F  2 68  ? 195.956 165.881 164.072 1.00 107.87 ? 102 TYR F CB  1 
ATOM   9091  C CG  . TYR F  2 68  ? 196.984 165.835 165.175 1.00 111.20 ? 102 TYR F CG  1 
ATOM   9092  C CD1 . TYR F  2 68  ? 197.041 166.830 166.138 1.00 118.88 ? 102 TYR F CD1 1 
ATOM   9093  C CD2 . TYR F  2 68  ? 197.882 164.781 165.267 1.00 110.20 ? 102 TYR F CD2 1 
ATOM   9094  C CE1 . TYR F  2 68  ? 197.973 166.788 167.150 1.00 121.75 ? 102 TYR F CE1 1 
ATOM   9095  C CE2 . TYR F  2 68  ? 198.816 164.729 166.276 1.00 113.00 ? 102 TYR F CE2 1 
ATOM   9096  C CZ  . TYR F  2 68  ? 198.857 165.735 167.216 1.00 119.13 ? 102 TYR F CZ  1 
ATOM   9097  O OH  . TYR F  2 68  ? 199.787 165.690 168.226 1.00 126.05 ? 102 TYR F OH  1 
ATOM   9098  N N   . PRO F  2 69  ? 193.112 167.234 163.631 1.00 110.28 ? 103 PRO F N   1 
ATOM   9099  C CA  . PRO F  2 69  ? 192.085 167.733 162.699 1.00 108.61 ? 103 PRO F CA  1 
ATOM   9100  C C   . PRO F  2 69  ? 192.452 167.559 161.234 1.00 109.41 ? 103 PRO F C   1 
ATOM   9101  O O   . PRO F  2 69  ? 191.553 167.374 160.406 1.00 109.25 ? 103 PRO F O   1 
ATOM   9102  C CB  . PRO F  2 69  ? 191.963 169.217 163.081 1.00 113.25 ? 103 PRO F CB  1 
ATOM   9103  C CG  . PRO F  2 69  ? 193.249 169.522 163.832 1.00 113.44 ? 103 PRO F CG  1 
ATOM   9104  C CD  . PRO F  2 69  ? 193.495 168.270 164.605 1.00 113.27 ? 103 PRO F CD  1 
ATOM   9105  N N   . ASN F  2 70  ? 193.739 167.600 160.893 1.00 109.68 ? 104 ASN F N   1 
ATOM   9106  C CA  . ASN F  2 70  ? 194.228 167.318 159.551 1.00 107.07 ? 104 ASN F CA  1 
ATOM   9107  C C   . ASN F  2 70  ? 194.555 165.841 159.336 1.00 108.47 ? 104 ASN F C   1 
ATOM   9108  O O   . ASN F  2 70  ? 195.485 165.522 158.587 1.00 112.67 ? 104 ASN F O   1 
ATOM   9109  C CB  . ASN F  2 70  ? 195.426 168.219 159.233 1.00 109.66 ? 104 ASN F CB  1 
ATOM   9110  C CG  . ASN F  2 70  ? 196.432 168.283 160.365 1.00 114.47 ? 104 ASN F CG  1 
ATOM   9111  O OD1 . ASN F  2 70  ? 196.217 169.007 161.334 1.00 123.60 ? 104 ASN F OD1 1 
ATOM   9112  N ND2 . ASN F  2 70  ? 197.528 167.547 160.250 1.00 110.80 ? 104 ASN F ND2 1 
ATOM   9113  N N   . ALA F  2 71  ? 193.825 164.945 160.003 1.00 106.19 ? 105 ALA F N   1 
ATOM   9114  C CA  . ALA F  2 71  ? 193.752 163.507 159.753 1.00 97.26  ? 105 ALA F CA  1 
ATOM   9115  C C   . ALA F  2 71  ? 195.022 162.751 160.114 1.00 96.68  ? 105 ALA F C   1 
ATOM   9116  O O   . ALA F  2 71  ? 195.038 161.520 160.005 1.00 98.66  ? 105 ALA F O   1 
ATOM   9117  C CB  . ALA F  2 71  ? 193.392 163.185 158.295 1.00 95.66  ? 105 ALA F CB  1 
ATOM   9118  N N   . SER F  2 72  ? 196.080 163.431 160.543 1.00 101.67 ? 106 SER F N   1 
ATOM   9119  C CA  . SER F  2 72  ? 197.296 162.738 160.936 1.00 97.76  ? 106 SER F CA  1 
ATOM   9120  C C   . SER F  2 72  ? 197.062 161.957 162.221 1.00 102.15 ? 106 SER F C   1 
ATOM   9121  O O   . SER F  2 72  ? 196.307 162.392 163.096 1.00 107.17 ? 106 SER F O   1 
ATOM   9122  C CB  . SER F  2 72  ? 198.438 163.732 161.116 1.00 104.72 ? 106 SER F CB  1 
ATOM   9123  O OG  . SER F  2 72  ? 198.521 164.605 160.004 1.00 115.24 ? 106 SER F OG  1 
ATOM   9124  N N   . LEU F  2 73  ? 197.707 160.800 162.331 1.00 102.78 ? 107 LEU F N   1 
ATOM   9125  C CA  . LEU F  2 73  ? 197.611 159.953 163.510 1.00 98.56  ? 107 LEU F CA  1 
ATOM   9126  C C   . LEU F  2 73  ? 198.949 159.944 164.231 1.00 102.07 ? 107 LEU F C   1 
ATOM   9127  O O   . LEU F  2 73  ? 199.992 159.714 163.611 1.00 105.11 ? 107 LEU F O   1 
ATOM   9128  C CB  . LEU F  2 73  ? 197.211 158.527 163.132 1.00 90.25  ? 107 LEU F CB  1 
ATOM   9129  C CG  . LEU F  2 73  ? 197.131 157.533 164.292 1.00 91.08  ? 107 LEU F CG  1 
ATOM   9130  C CD1 . LEU F  2 73  ? 195.969 157.877 165.208 1.00 98.11  ? 107 LEU F CD1 1 
ATOM   9131  C CD2 . LEU F  2 73  ? 197.015 156.108 163.768 1.00 90.10  ? 107 LEU F CD2 1 
ATOM   9132  N N   . LEU F  2 74  ? 198.917 160.191 165.534 1.00 100.14 ? 108 LEU F N   1 
ATOM   9133  C CA  . LEU F  2 74  ? 200.111 160.178 166.363 1.00 100.34 ? 108 LEU F CA  1 
ATOM   9134  C C   . LEU F  2 74  ? 200.020 159.018 167.340 1.00 107.78 ? 108 LEU F C   1 
ATOM   9135  O O   . LEU F  2 74  ? 199.031 158.893 168.068 1.00 115.80 ? 108 LEU F O   1 
ATOM   9136  C CB  . LEU F  2 74  ? 200.274 161.499 167.119 1.00 104.60 ? 108 LEU F CB  1 
ATOM   9137  C CG  . LEU F  2 74  ? 201.378 161.531 168.178 1.00 107.26 ? 108 LEU F CG  1 
ATOM   9138  C CD1 . LEU F  2 74  ? 202.738 161.258 167.560 1.00 108.64 ? 108 LEU F CD1 1 
ATOM   9139  C CD2 . LEU F  2 74  ? 201.380 162.861 168.917 1.00 111.57 ? 108 LEU F CD2 1 
ATOM   9140  N N   . ILE F  2 75  ? 201.052 158.181 167.357 1.00 107.41 ? 109 ILE F N   1 
ATOM   9141  C CA  . ILE F  2 75  ? 201.124 157.030 168.249 1.00 104.03 ? 109 ILE F CA  1 
ATOM   9142  C C   . ILE F  2 75  ? 202.343 157.220 169.139 1.00 112.43 ? 109 ILE F C   1 
ATOM   9143  O O   . ILE F  2 75  ? 203.480 157.204 168.651 1.00 115.12 ? 109 ILE F O   1 
ATOM   9144  C CB  . ILE F  2 75  ? 201.214 155.709 167.469 1.00 97.74  ? 109 ILE F CB  1 
ATOM   9145  C CG1 . ILE F  2 75  ? 199.892 155.411 166.757 1.00 99.56  ? 109 ILE F CG1 1 
ATOM   9146  C CG2 . ILE F  2 75  ? 201.584 154.568 168.402 1.00 110.18 ? 109 ILE F CG2 1 
ATOM   9147  C CD1 . ILE F  2 75  ? 200.005 154.341 165.700 1.00 96.36  ? 109 ILE F CD1 1 
ATOM   9148  N N   . GLN F  2 76  ? 202.110 157.400 170.436 1.00 115.05 ? 110 GLN F N   1 
ATOM   9149  C CA  . GLN F  2 76  ? 203.185 157.579 171.400 1.00 118.89 ? 110 GLN F CA  1 
ATOM   9150  C C   . GLN F  2 76  ? 203.497 156.260 172.091 1.00 126.74 ? 110 GLN F C   1 
ATOM   9151  O O   . GLN F  2 76  ? 202.675 155.339 172.121 1.00 128.93 ? 110 GLN F O   1 
ATOM   9152  C CB  . GLN F  2 76  ? 202.831 158.640 172.453 1.00 119.14 ? 110 GLN F CB  1 
ATOM   9153  C CG  . GLN F  2 76  ? 202.483 160.006 171.888 1.00 125.33 ? 110 GLN F CG  1 
ATOM   9154  C CD  . GLN F  2 76  ? 201.661 160.835 172.849 1.00 136.53 ? 110 GLN F CD  1 
ATOM   9155  O OE1 . GLN F  2 76  ? 200.430 160.788 172.837 1.00 140.52 ? 110 GLN F OE1 1 
ATOM   9156  N NE2 . GLN F  2 76  ? 202.339 161.591 173.700 1.00 140.67 ? 110 GLN F NE2 1 
ATOM   9157  N N   . ASN F  2 77  ? 204.707 156.181 172.635 1.00 130.75 ? 111 ASN F N   1 
ATOM   9158  C CA  . ASN F  2 77  ? 205.156 155.017 173.392 1.00 132.14 ? 111 ASN F CA  1 
ATOM   9159  C C   . ASN F  2 77  ? 205.006 153.739 172.565 1.00 130.71 ? 111 ASN F C   1 
ATOM   9160  O O   . ASN F  2 77  ? 204.367 152.768 172.975 1.00 131.47 ? 111 ASN F O   1 
ATOM   9161  C CB  . ASN F  2 77  ? 204.399 154.917 174.714 1.00 138.93 ? 111 ASN F CB  1 
ATOM   9162  C CG  . ASN F  2 77  ? 205.262 154.412 175.840 1.00 152.72 ? 111 ASN F CG  1 
ATOM   9163  O OD1 . ASN F  2 77  ? 206.485 154.405 175.735 1.00 153.09 ? 111 ASN F OD1 1 
ATOM   9164  N ND2 . ASN F  2 77  ? 204.628 153.988 176.923 1.00 163.20 ? 111 ASN F ND2 1 
ATOM   9165  N N   . VAL F  2 78  ? 205.589 153.762 171.364 1.00 128.29 ? 112 VAL F N   1 
ATOM   9166  C CA  . VAL F  2 78  ? 205.412 152.651 170.441 1.00 125.63 ? 112 VAL F CA  1 
ATOM   9167  C C   . VAL F  2 78  ? 206.132 151.407 170.960 1.00 129.83 ? 112 VAL F C   1 
ATOM   9168  O O   . VAL F  2 78  ? 207.144 151.482 171.668 1.00 133.85 ? 112 VAL F O   1 
ATOM   9169  C CB  . VAL F  2 78  ? 205.888 153.024 169.028 1.00 124.36 ? 112 VAL F CB  1 
ATOM   9170  C CG1 . VAL F  2 78  ? 207.411 152.954 168.926 1.00 131.31 ? 112 VAL F CG1 1 
ATOM   9171  C CG2 . VAL F  2 78  ? 205.236 152.114 167.997 1.00 123.98 ? 112 VAL F CG2 1 
ATOM   9172  N N   . THR F  2 79  ? 205.576 150.246 170.620 1.00 129.04 ? 113 THR F N   1 
ATOM   9173  C CA  . THR F  2 79  ? 206.136 148.967 171.031 1.00 130.46 ? 113 THR F CA  1 
ATOM   9174  C C   . THR F  2 79  ? 206.318 148.083 169.804 1.00 129.61 ? 113 THR F C   1 
ATOM   9175  O O   . THR F  2 79  ? 205.797 148.365 168.721 1.00 130.18 ? 113 THR F O   1 
ATOM   9176  C CB  . THR F  2 79  ? 205.250 148.264 172.070 1.00 130.11 ? 113 THR F CB  1 
ATOM   9177  O OG1 . THR F  2 79  ? 203.951 148.024 171.515 1.00 130.67 ? 113 THR F OG1 1 
ATOM   9178  C CG2 . THR F  2 79  ? 205.107 149.120 173.323 1.00 131.32 ? 113 THR F CG2 1 
ATOM   9179  N N   . GLN F  2 80  ? 207.074 146.997 169.983 1.00 128.82 ? 114 GLN F N   1 
ATOM   9180  C CA  . GLN F  2 80  ? 207.372 146.112 168.861 1.00 127.44 ? 114 GLN F CA  1 
ATOM   9181  C C   . GLN F  2 80  ? 206.119 145.408 168.356 1.00 127.38 ? 114 GLN F C   1 
ATOM   9182  O O   . GLN F  2 80  ? 206.100 144.884 167.236 1.00 131.84 ? 114 GLN F O   1 
ATOM   9183  C CB  . GLN F  2 80  ? 208.440 145.098 169.268 1.00 126.41 ? 114 GLN F CB  1 
ATOM   9184  C CG  . GLN F  2 80  ? 209.165 144.444 168.107 1.00 125.02 ? 114 GLN F CG  1 
ATOM   9185  C CD  . GLN F  2 80  ? 210.410 143.712 168.555 1.00 134.89 ? 114 GLN F CD  1 
ATOM   9186  O OE1 . GLN F  2 80  ? 210.483 143.226 169.684 1.00 142.80 ? 114 GLN F OE1 1 
ATOM   9187  N NE2 . GLN F  2 80  ? 211.393 143.615 167.669 1.00 134.91 ? 114 GLN F NE2 1 
ATOM   9188  N N   . ASN F  2 81  ? 205.060 145.386 169.165 1.00 125.40 ? 115 ASN F N   1 
ATOM   9189  C CA  . ASN F  2 81  ? 203.814 144.770 168.727 1.00 128.29 ? 115 ASN F CA  1 
ATOM   9190  C C   . ASN F  2 81  ? 203.063 145.637 167.724 1.00 128.55 ? 115 ASN F C   1 
ATOM   9191  O O   . ASN F  2 81  ? 202.180 145.130 167.024 1.00 131.35 ? 115 ASN F O   1 
ATOM   9192  C CB  . ASN F  2 81  ? 202.923 144.477 169.933 1.00 129.55 ? 115 ASN F CB  1 
ATOM   9193  C CG  . ASN F  2 81  ? 201.764 143.567 169.590 1.00 138.67 ? 115 ASN F CG  1 
ATOM   9194  O OD1 . ASN F  2 81  ? 200.611 143.997 169.559 1.00 144.48 ? 115 ASN F OD1 1 
ATOM   9195  N ND2 . ASN F  2 81  ? 202.063 142.300 169.330 1.00 135.25 ? 115 ASN F ND2 1 
ATOM   9196  N N   . ASP F  2 82  ? 203.394 146.925 167.634 1.00 123.97 ? 116 ASP F N   1 
ATOM   9197  C CA  . ASP F  2 82  ? 202.687 147.841 166.747 1.00 116.92 ? 116 ASP F CA  1 
ATOM   9198  C C   . ASP F  2 82  ? 203.111 147.720 165.289 1.00 112.94 ? 116 ASP F C   1 
ATOM   9199  O O   . ASP F  2 82  ? 202.450 148.305 164.424 1.00 112.31 ? 116 ASP F O   1 
ATOM   9200  C CB  . ASP F  2 82  ? 202.889 149.284 167.215 1.00 118.82 ? 116 ASP F CB  1 
ATOM   9201  C CG  . ASP F  2 82  ? 202.263 149.549 168.569 1.00 129.08 ? 116 ASP F CG  1 
ATOM   9202  O OD1 . ASP F  2 82  ? 201.031 149.751 168.626 1.00 130.72 ? 116 ASP F OD1 1 
ATOM   9203  O OD2 . ASP F  2 82  ? 203.001 149.555 169.576 1.00 134.03 ? 116 ASP F OD2 1 
ATOM   9204  N N   . THR F  2 83  ? 204.190 146.997 164.997 1.00 112.03 ? 117 THR F N   1 
ATOM   9205  C CA  . THR F  2 83  ? 204.670 146.872 163.626 1.00 110.65 ? 117 THR F CA  1 
ATOM   9206  C C   . THR F  2 83  ? 203.610 146.226 162.746 1.00 110.95 ? 117 THR F C   1 
ATOM   9207  O O   . THR F  2 83  ? 203.228 145.072 162.964 1.00 120.78 ? 117 THR F O   1 
ATOM   9208  C CB  . THR F  2 83  ? 205.956 146.049 163.590 1.00 115.09 ? 117 THR F CB  1 
ATOM   9209  O OG1 . THR F  2 83  ? 206.920 146.624 164.479 1.00 118.60 ? 117 THR F OG1 1 
ATOM   9210  C CG2 . THR F  2 83  ? 206.528 146.021 162.181 1.00 114.76 ? 117 THR F CG2 1 
ATOM   9211  N N   . GLY F  2 84  ? 203.136 146.968 161.754 1.00 103.99 ? 118 GLY F N   1 
ATOM   9212  C CA  . GLY F  2 84  ? 202.125 146.448 160.859 1.00 107.68 ? 118 GLY F CA  1 
ATOM   9213  C C   . GLY F  2 84  ? 201.601 147.538 159.947 1.00 107.86 ? 118 GLY F C   1 
ATOM   9214  O O   . GLY F  2 84  ? 202.134 148.648 159.900 1.00 107.58 ? 118 GLY F O   1 
ATOM   9215  N N   . PHE F  2 85  ? 200.543 147.191 159.223 1.00 105.08 ? 119 PHE F N   1 
ATOM   9216  C CA  . PHE F  2 85  ? 199.897 148.109 158.300 1.00 99.98  ? 119 PHE F CA  1 
ATOM   9217  C C   . PHE F  2 85  ? 198.762 148.852 158.991 1.00 98.73  ? 119 PHE F C   1 
ATOM   9218  O O   . PHE F  2 85  ? 198.093 148.319 159.880 1.00 100.39 ? 119 PHE F O   1 
ATOM   9219  C CB  . PHE F  2 85  ? 199.358 147.360 157.081 1.00 103.20 ? 119 PHE F CB  1 
ATOM   9220  C CG  . PHE F  2 85  ? 200.428 146.784 156.200 1.00 109.02 ? 119 PHE F CG  1 
ATOM   9221  C CD1 . PHE F  2 85  ? 201.031 145.578 156.514 1.00 111.72 ? 119 PHE F CD1 1 
ATOM   9222  C CD2 . PHE F  2 85  ? 200.826 147.447 155.052 1.00 113.95 ? 119 PHE F CD2 1 
ATOM   9223  C CE1 . PHE F  2 85  ? 202.014 145.047 155.702 1.00 117.02 ? 119 PHE F CE1 1 
ATOM   9224  C CE2 . PHE F  2 85  ? 201.808 146.920 154.236 1.00 119.10 ? 119 PHE F CE2 1 
ATOM   9225  C CZ  . PHE F  2 85  ? 202.403 145.719 154.562 1.00 119.42 ? 119 PHE F CZ  1 
ATOM   9226  N N   . TYR F  2 86  ? 198.558 150.100 158.579 1.00 98.43  ? 120 TYR F N   1 
ATOM   9227  C CA  . TYR F  2 86  ? 197.454 150.917 159.060 1.00 93.36  ? 120 TYR F CA  1 
ATOM   9228  C C   . TYR F  2 86  ? 196.724 151.518 157.871 1.00 93.64  ? 120 TYR F C   1 
ATOM   9229  O O   . TYR F  2 86  ? 197.353 151.982 156.916 1.00 98.76  ? 120 TYR F O   1 
ATOM   9230  C CB  . TYR F  2 86  ? 197.938 152.030 159.998 1.00 86.68  ? 120 TYR F CB  1 
ATOM   9231  C CG  . TYR F  2 86  ? 198.551 151.528 161.284 1.00 91.96  ? 120 TYR F CG  1 
ATOM   9232  C CD1 . TYR F  2 86  ? 199.831 150.994 161.308 1.00 97.17  ? 120 TYR F CD1 1 
ATOM   9233  C CD2 . TYR F  2 86  ? 197.845 151.587 162.477 1.00 94.08  ? 120 TYR F CD2 1 
ATOM   9234  C CE1 . TYR F  2 86  ? 200.388 150.532 162.481 1.00 100.87 ? 120 TYR F CE1 1 
ATOM   9235  C CE2 . TYR F  2 86  ? 198.395 151.129 163.655 1.00 98.45  ? 120 TYR F CE2 1 
ATOM   9236  C CZ  . TYR F  2 86  ? 199.667 150.603 163.652 1.00 101.14 ? 120 TYR F CZ  1 
ATOM   9237  O OH  . TYR F  2 86  ? 200.221 150.145 164.824 1.00 109.69 ? 120 TYR F OH  1 
ATOM   9238  N N   . THR F  2 87  ? 195.397 151.512 157.935 1.00 89.27  ? 121 THR F N   1 
ATOM   9239  C CA  . THR F  2 87  ? 194.560 152.028 156.864 1.00 92.39  ? 121 THR F CA  1 
ATOM   9240  C C   . THR F  2 87  ? 193.781 153.237 157.356 1.00 88.41  ? 121 THR F C   1 
ATOM   9241  O O   . THR F  2 87  ? 193.276 153.248 158.482 1.00 91.23  ? 121 THR F O   1 
ATOM   9242  C CB  . THR F  2 87  ? 193.587 150.965 156.348 1.00 99.12  ? 121 THR F CB  1 
ATOM   9243  O OG1 . THR F  2 87  ? 192.897 150.368 157.452 1.00 102.91 ? 121 THR F OG1 1 
ATOM   9244  C CG2 . THR F  2 87  ? 194.335 149.891 155.576 1.00 104.26 ? 121 THR F CG2 1 
ATOM   9245  N N   . LEU F  2 88  ? 193.688 154.252 156.504 1.00 84.71  ? 122 LEU F N   1 
ATOM   9246  C CA  . LEU F  2 88  ? 192.946 155.468 156.799 1.00 83.14  ? 122 LEU F CA  1 
ATOM   9247  C C   . LEU F  2 88  ? 191.674 155.489 155.966 1.00 86.14  ? 122 LEU F C   1 
ATOM   9248  O O   . LEU F  2 88  ? 191.725 155.312 154.745 1.00 91.30  ? 122 LEU F O   1 
ATOM   9249  C CB  . LEU F  2 88  ? 193.787 156.713 156.510 1.00 83.34  ? 122 LEU F CB  1 
ATOM   9250  C CG  . LEU F  2 88  ? 193.014 158.024 156.347 1.00 79.19  ? 122 LEU F CG  1 
ATOM   9251  C CD1 . LEU F  2 88  ? 192.358 158.433 157.656 1.00 79.47  ? 122 LEU F CD1 1 
ATOM   9252  C CD2 . LEU F  2 88  ? 193.924 159.125 155.837 1.00 89.17  ? 122 LEU F CD2 1 
ATOM   9253  N N   . GLN F  2 89  ? 190.542 155.699 156.627 1.00 85.21  ? 123 GLN F N   1 
ATOM   9254  C CA  . GLN F  2 89  ? 189.251 155.815 155.966 1.00 87.46  ? 123 GLN F CA  1 
ATOM   9255  C C   . GLN F  2 89  ? 188.845 157.280 155.955 1.00 90.69  ? 123 GLN F C   1 
ATOM   9256  O O   . GLN F  2 89  ? 188.769 157.914 157.013 1.00 97.90  ? 123 GLN F O   1 
ATOM   9257  C CB  . GLN F  2 89  ? 188.191 154.974 156.673 1.00 88.98  ? 123 GLN F CB  1 
ATOM   9258  C CG  . GLN F  2 89  ? 186.838 155.003 155.994 1.00 93.53  ? 123 GLN F CG  1 
ATOM   9259  C CD  . GLN F  2 89  ? 185.966 153.833 156.390 1.00 107.49 ? 123 GLN F CD  1 
ATOM   9260  O OE1 . GLN F  2 89  ? 185.575 153.024 155.549 1.00 113.34 ? 123 GLN F OE1 1 
ATOM   9261  N NE2 . GLN F  2 89  ? 185.648 153.740 157.675 1.00 109.79 ? 123 GLN F NE2 1 
ATOM   9262  N N   . VAL F  2 90  ? 188.585 157.812 154.766 1.00 86.54  ? 124 VAL F N   1 
ATOM   9263  C CA  . VAL F  2 90  ? 188.140 159.188 154.596 1.00 85.35  ? 124 VAL F CA  1 
ATOM   9264  C C   . VAL F  2 90  ? 186.747 159.164 153.991 1.00 93.43  ? 124 VAL F C   1 
ATOM   9265  O O   . VAL F  2 90  ? 186.538 158.579 152.922 1.00 100.00 ? 124 VAL F O   1 
ATOM   9266  C CB  . VAL F  2 90  ? 189.110 159.994 153.715 1.00 84.38  ? 124 VAL F CB  1 
ATOM   9267  C CG1 . VAL F  2 90  ? 188.492 161.321 153.336 1.00 91.47  ? 124 VAL F CG1 1 
ATOM   9268  C CG2 . VAL F  2 90  ? 190.417 160.217 154.452 1.00 85.28  ? 124 VAL F CG2 1 
ATOM   9269  N N   . ILE F  2 91  ? 185.799 159.794 154.674 1.00 91.21  ? 125 ILE F N   1 
ATOM   9270  C CA  . ILE F  2 91  ? 184.418 159.870 154.219 1.00 92.03  ? 125 ILE F CA  1 
ATOM   9271  C C   . ILE F  2 91  ? 184.163 161.278 153.706 1.00 93.69  ? 125 ILE F C   1 
ATOM   9272  O O   . ILE F  2 91  ? 184.216 162.249 154.471 1.00 101.98 ? 125 ILE F O   1 
ATOM   9273  C CB  . ILE F  2 91  ? 183.435 159.494 155.338 1.00 90.04  ? 125 ILE F CB  1 
ATOM   9274  C CG1 . ILE F  2 91  ? 183.681 158.054 155.786 1.00 98.51  ? 125 ILE F CG1 1 
ATOM   9275  C CG2 . ILE F  2 91  ? 182.005 159.677 154.877 1.00 95.83  ? 125 ILE F CG2 1 
ATOM   9276  C CD1 . ILE F  2 91  ? 182.939 157.672 157.034 1.00 108.05 ? 125 ILE F CD1 1 
ATOM   9277  N N   . LYS F  2 92  ? 183.886 161.387 152.412 1.00 91.77  ? 126 LYS F N   1 
ATOM   9278  C CA  . LYS F  2 92  ? 183.666 162.672 151.773 1.00 99.32  ? 126 LYS F CA  1 
ATOM   9279  C C   . LYS F  2 92  ? 182.280 163.210 152.124 1.00 104.53 ? 126 LYS F C   1 
ATOM   9280  O O   . LYS F  2 92  ? 181.514 162.595 152.869 1.00 105.74 ? 126 LYS F O   1 
ATOM   9281  C CB  . LYS F  2 92  ? 183.846 162.538 150.262 1.00 100.72 ? 126 LYS F CB  1 
ATOM   9282  C CG  . LYS F  2 92  ? 185.046 161.677 149.883 1.00 104.17 ? 126 LYS F CG  1 
ATOM   9283  C CD  . LYS F  2 92  ? 184.996 161.213 148.435 1.00 106.26 ? 126 LYS F CD  1 
ATOM   9284  C CE  . LYS F  2 92  ? 184.578 162.330 147.499 1.00 113.37 ? 126 LYS F CE  1 
ATOM   9285  N NZ  . LYS F  2 92  ? 185.542 163.464 147.535 1.00 118.42 ? 126 LYS F NZ  1 
ATOM   9286  N N   . SER F  2 93  ? 181.966 164.390 151.580 1.00 106.58 ? 127 SER F N   1 
ATOM   9287  C CA  . SER F  2 93  ? 180.696 165.037 151.898 1.00 103.92 ? 127 SER F CA  1 
ATOM   9288  C C   . SER F  2 93  ? 179.507 164.200 151.448 1.00 105.56 ? 127 SER F C   1 
ATOM   9289  O O   . SER F  2 93  ? 178.522 164.076 152.184 1.00 102.10 ? 127 SER F O   1 
ATOM   9290  C CB  . SER F  2 93  ? 180.636 166.422 151.257 1.00 108.49 ? 127 SER F CB  1 
ATOM   9291  O OG  . SER F  2 93  ? 181.015 166.365 149.894 1.00 117.20 ? 127 SER F OG  1 
ATOM   9292  N N   . ASP F  2 94  ? 179.577 163.618 150.254 1.00 103.96 ? 128 ASP F N   1 
ATOM   9293  C CA  . ASP F  2 94  ? 178.541 162.724 149.759 1.00 101.24 ? 128 ASP F CA  1 
ATOM   9294  C C   . ASP F  2 94  ? 178.578 161.356 150.427 1.00 101.49 ? 128 ASP F C   1 
ATOM   9295  O O   . ASP F  2 94  ? 177.789 160.479 150.061 1.00 102.27 ? 128 ASP F O   1 
ATOM   9296  C CB  . ASP F  2 94  ? 178.649 162.582 148.236 1.00 103.97 ? 128 ASP F CB  1 
ATOM   9297  C CG  . ASP F  2 94  ? 180.008 162.073 147.781 1.00 112.77 ? 128 ASP F CG  1 
ATOM   9298  O OD1 . ASP F  2 94  ? 180.653 161.295 148.512 1.00 114.15 ? 128 ASP F OD1 1 
ATOM   9299  O OD2 . ASP F  2 94  ? 180.433 162.457 146.672 1.00 116.34 ? 128 ASP F OD2 1 
ATOM   9300  N N   . LEU F  2 95  ? 179.491 161.158 151.378 1.00 101.58 ? 129 LEU F N   1 
ATOM   9301  C CA  . LEU F  2 95  ? 179.625 159.957 152.195 1.00 100.10 ? 129 LEU F CA  1 
ATOM   9302  C C   . LEU F  2 95  ? 180.116 158.753 151.403 1.00 101.50 ? 129 LEU F C   1 
ATOM   9303  O O   . LEU F  2 95  ? 179.814 157.612 151.773 1.00 101.95 ? 129 LEU F O   1 
ATOM   9304  C CB  . LEU F  2 95  ? 178.315 159.616 152.914 1.00 95.82  ? 129 LEU F CB  1 
ATOM   9305  C CG  . LEU F  2 95  ? 178.229 160.096 154.364 1.00 96.91  ? 129 LEU F CG  1 
ATOM   9306  C CD1 . LEU F  2 95  ? 178.625 161.555 154.479 1.00 103.42 ? 129 LEU F CD1 1 
ATOM   9307  C CD2 . LEU F  2 95  ? 176.822 159.912 154.875 1.00 98.71  ? 129 LEU F CD2 1 
ATOM   9308  N N   . VAL F  2 96  ? 180.866 158.973 150.328 1.00 100.78 ? 130 VAL F N   1 
ATOM   9309  C CA  . VAL F  2 96  ? 181.534 157.885 149.623 1.00 101.58 ? 130 VAL F CA  1 
ATOM   9310  C C   . VAL F  2 96  ? 182.914 157.687 150.233 1.00 103.63 ? 130 VAL F C   1 
ATOM   9311  O O   . VAL F  2 96  ? 183.711 158.629 150.317 1.00 103.76 ? 130 VAL F O   1 
ATOM   9312  C CB  . VAL F  2 96  ? 181.624 158.182 148.118 1.00 100.49 ? 130 VAL F CB  1 
ATOM   9313  C CG1 . VAL F  2 96  ? 182.468 157.129 147.422 1.00 103.56 ? 130 VAL F CG1 1 
ATOM   9314  C CG2 . VAL F  2 96  ? 180.233 158.241 147.508 1.00 101.98 ? 130 VAL F CG2 1 
ATOM   9315  N N   . ASN F  2 97  ? 183.197 156.463 150.663 1.00 103.78 ? 131 ASN F N   1 
ATOM   9316  C CA  . ASN F  2 97  ? 184.412 156.178 151.411 1.00 99.12  ? 131 ASN F CA  1 
ATOM   9317  C C   . ASN F  2 97  ? 185.635 156.198 150.504 1.00 100.43 ? 131 ASN F C   1 
ATOM   9318  O O   . ASN F  2 97  ? 185.571 155.801 149.338 1.00 105.41 ? 131 ASN F O   1 
ATOM   9319  C CB  . ASN F  2 97  ? 184.291 154.820 152.100 1.00 103.97 ? 131 ASN F CB  1 
ATOM   9320  C CG  . ASN F  2 97  ? 183.312 154.842 153.255 1.00 110.39 ? 131 ASN F CG  1 
ATOM   9321  O OD1 . ASN F  2 97  ? 182.190 155.328 153.120 1.00 110.65 ? 131 ASN F OD1 1 
ATOM   9322  N ND2 . ASN F  2 97  ? 183.728 154.307 154.394 1.00 112.71 ? 131 ASN F ND2 1 
ATOM   9323  N N   . GLU F  2 98  ? 186.756 156.666 151.051 1.00 97.56  ? 132 GLU F N   1 
ATOM   9324  C CA  . GLU F  2 98  ? 188.042 156.649 150.368 1.00 97.15  ? 132 GLU F CA  1 
ATOM   9325  C C   . GLU F  2 98  ? 189.084 156.068 151.310 1.00 100.10 ? 132 GLU F C   1 
ATOM   9326  O O   . GLU F  2 98  ? 189.162 156.470 152.475 1.00 103.99 ? 132 GLU F O   1 
ATOM   9327  C CB  . GLU F  2 98  ? 188.456 158.050 149.911 1.00 97.32  ? 132 GLU F CB  1 
ATOM   9328  C CG  . GLU F  2 98  ? 189.416 158.049 148.735 1.00 108.31 ? 132 GLU F CG  1 
ATOM   9329  C CD  . GLU F  2 98  ? 189.366 159.334 147.937 1.00 119.80 ? 132 GLU F CD  1 
ATOM   9330  O OE1 . GLU F  2 98  ? 188.393 160.100 148.101 1.00 114.68 ? 132 GLU F OE1 1 
ATOM   9331  O OE2 . GLU F  2 98  ? 190.299 159.579 147.144 1.00 125.80 ? 132 GLU F OE2 1 
ATOM   9332  N N   . GLU F  2 99  ? 189.882 155.130 150.807 1.00 99.18  ? 133 GLU F N   1 
ATOM   9333  C CA  . GLU F  2 99  ? 190.805 154.370 151.632 1.00 99.74  ? 133 GLU F CA  1 
ATOM   9334  C C   . GLU F  2 99  ? 192.245 154.623 151.206 1.00 104.40 ? 133 GLU F C   1 
ATOM   9335  O O   . GLU F  2 99  ? 192.537 154.884 150.036 1.00 110.77 ? 133 GLU F O   1 
ATOM   9336  C CB  . GLU F  2 99  ? 190.499 152.869 151.555 1.00 99.40  ? 133 GLU F CB  1 
ATOM   9337  C CG  . GLU F  2 99  ? 189.013 152.546 151.531 1.00 111.62 ? 133 GLU F CG  1 
ATOM   9338  C CD  . GLU F  2 99  ? 188.423 152.366 152.915 1.00 115.95 ? 133 GLU F CD  1 
ATOM   9339  O OE1 . GLU F  2 99  ? 187.786 151.319 153.154 1.00 126.43 ? 133 GLU F OE1 1 
ATOM   9340  O OE2 . GLU F  2 99  ? 188.593 153.267 153.763 1.00 109.15 ? 133 GLU F OE2 1 
ATOM   9341  N N   . ALA F  2 100 ? 193.145 154.538 152.183 1.00 101.19 ? 134 ALA F N   1 
ATOM   9342  C CA  . ALA F  2 100 ? 194.578 154.634 151.947 1.00 99.48  ? 134 ALA F CA  1 
ATOM   9343  C C   . ALA F  2 100 ? 195.288 153.861 153.047 1.00 96.93  ? 134 ALA F C   1 
ATOM   9344  O O   . ALA F  2 100 ? 194.720 153.591 154.107 1.00 99.23  ? 134 ALA F O   1 
ATOM   9345  C CB  . ALA F  2 100 ? 195.051 156.089 151.901 1.00 103.75 ? 134 ALA F CB  1 
ATOM   9346  N N   . THR F  2 101 ? 196.547 153.511 152.791 1.00 96.98  ? 135 THR F N   1 
ATOM   9347  C CA  . THR F  2 101 ? 197.283 152.636 153.689 1.00 97.46  ? 135 THR F CA  1 
ATOM   9348  C C   . THR F  2 101 ? 198.643 153.237 154.015 1.00 97.34  ? 135 THR F C   1 
ATOM   9349  O O   . THR F  2 101 ? 199.149 154.112 153.309 1.00 102.69 ? 135 THR F O   1 
ATOM   9350  C CB  . THR F  2 101 ? 197.463 151.234 153.091 1.00 104.20 ? 135 THR F CB  1 
ATOM   9351  O OG1 . THR F  2 101 ? 197.929 150.336 154.106 1.00 106.20 ? 135 THR F OG1 1 
ATOM   9352  C CG2 . THR F  2 101 ? 198.467 151.265 151.949 1.00 106.04 ? 135 THR F CG2 1 
ATOM   9353  N N   . GLY F  2 102 ? 199.222 152.750 155.109 1.00 93.70  ? 136 GLY F N   1 
ATOM   9354  C CA  . GLY F  2 102 ? 200.547 153.161 155.532 1.00 94.49  ? 136 GLY F CA  1 
ATOM   9355  C C   . GLY F  2 102 ? 201.076 152.193 156.562 1.00 97.68  ? 136 GLY F C   1 
ATOM   9356  O O   . GLY F  2 102 ? 200.313 151.480 157.222 1.00 102.70 ? 136 GLY F O   1 
ATOM   9357  N N   . GLN F  2 103 ? 202.400 152.173 156.700 1.00 96.29  ? 137 GLN F N   1 
ATOM   9358  C CA  . GLN F  2 103 ? 203.039 151.197 157.568 1.00 101.81 ? 137 GLN F CA  1 
ATOM   9359  C C   . GLN F  2 103 ? 204.332 151.769 158.126 1.00 107.28 ? 137 GLN F C   1 
ATOM   9360  O O   . GLN F  2 103 ? 204.897 152.727 157.591 1.00 109.05 ? 137 GLN F O   1 
ATOM   9361  C CB  . GLN F  2 103 ? 203.328 149.889 156.824 1.00 107.06 ? 137 GLN F CB  1 
ATOM   9362  C CG  . GLN F  2 103 ? 204.464 149.997 155.821 1.00 112.33 ? 137 GLN F CG  1 
ATOM   9363  C CD  . GLN F  2 103 ? 204.547 148.797 154.901 1.00 126.72 ? 137 GLN F CD  1 
ATOM   9364  O OE1 . GLN F  2 103 ? 204.259 148.894 153.708 1.00 133.33 ? 137 GLN F OE1 1 
ATOM   9365  N NE2 . GLN F  2 103 ? 204.943 147.656 155.451 1.00 126.17 ? 137 GLN F NE2 1 
ATOM   9366  N N   . PHE F  2 104 ? 204.794 151.161 159.216 1.00 106.74 ? 138 PHE F N   1 
ATOM   9367  C CA  . PHE F  2 104 ? 206.081 151.494 159.806 1.00 108.95 ? 138 PHE F CA  1 
ATOM   9368  C C   . PHE F  2 104 ? 206.591 150.278 160.563 1.00 110.32 ? 138 PHE F C   1 
ATOM   9369  O O   . PHE F  2 104 ? 205.821 149.392 160.940 1.00 113.81 ? 138 PHE F O   1 
ATOM   9370  C CB  . PHE F  2 104 ? 205.986 152.718 160.725 1.00 106.93 ? 138 PHE F CB  1 
ATOM   9371  C CG  . PHE F  2 104 ? 205.036 152.547 161.876 1.00 102.03 ? 138 PHE F CG  1 
ATOM   9372  C CD1 . PHE F  2 104 ? 205.460 151.989 163.070 1.00 103.67 ? 138 PHE F CD1 1 
ATOM   9373  C CD2 . PHE F  2 104 ? 203.720 152.959 161.768 1.00 101.80 ? 138 PHE F CD2 1 
ATOM   9374  C CE1 . PHE F  2 104 ? 204.587 151.837 164.128 1.00 105.85 ? 138 PHE F CE1 1 
ATOM   9375  C CE2 . PHE F  2 104 ? 202.844 152.812 162.823 1.00 98.01  ? 138 PHE F CE2 1 
ATOM   9376  C CZ  . PHE F  2 104 ? 203.277 152.249 164.004 1.00 102.46 ? 138 PHE F CZ  1 
ATOM   9377  N N   . HIS F  2 105 ? 207.902 150.248 160.779 1.00 111.80 ? 139 HIS F N   1 
ATOM   9378  C CA  . HIS F  2 105 ? 208.560 149.153 161.474 1.00 114.79 ? 139 HIS F CA  1 
ATOM   9379  C C   . HIS F  2 105 ? 209.120 149.644 162.801 1.00 119.07 ? 139 HIS F C   1 
ATOM   9380  O O   . HIS F  2 105 ? 209.692 150.735 162.880 1.00 124.54 ? 139 HIS F O   1 
ATOM   9381  C CB  . HIS F  2 105 ? 209.686 148.557 160.625 1.00 118.67 ? 139 HIS F CB  1 
ATOM   9382  C CG  . HIS F  2 105 ? 209.222 147.532 159.639 1.00 125.31 ? 139 HIS F CG  1 
ATOM   9383  N ND1 . HIS F  2 105 ? 208.694 147.866 158.411 1.00 128.83 ? 139 HIS F ND1 1 
ATOM   9384  C CD2 . HIS F  2 105 ? 209.211 146.179 159.698 1.00 126.65 ? 139 HIS F CD2 1 
ATOM   9385  C CE1 . HIS F  2 105 ? 208.376 146.763 157.756 1.00 130.71 ? 139 HIS F CE1 1 
ATOM   9386  N NE2 . HIS F  2 105 ? 208.679 145.726 158.516 1.00 134.96 ? 139 HIS F NE2 1 
ATOM   9387  N N   . VAL F  2 106 ? 208.952 148.832 163.841 1.00 114.63 ? 140 VAL F N   1 
ATOM   9388  C CA  . VAL F  2 106 ? 209.462 149.127 165.174 1.00 115.02 ? 140 VAL F CA  1 
ATOM   9389  C C   . VAL F  2 106 ? 210.654 148.219 165.433 1.00 118.64 ? 140 VAL F C   1 
ATOM   9390  O O   . VAL F  2 106 ? 210.576 147.004 165.212 1.00 124.89 ? 140 VAL F O   1 
ATOM   9391  C CB  . VAL F  2 106 ? 208.380 148.937 166.250 1.00 116.46 ? 140 VAL F CB  1 
ATOM   9392  C CG1 . VAL F  2 106 ? 208.866 149.469 167.587 1.00 124.80 ? 140 VAL F CG1 1 
ATOM   9393  C CG2 . VAL F  2 106 ? 207.094 149.628 165.832 1.00 116.88 ? 140 VAL F CG2 1 
ATOM   9394  N N   . TYR F  2 107 ? 211.752 148.804 165.898 1.00 122.19 ? 141 TYR F N   1 
ATOM   9395  C CA  . TYR F  2 107 ? 212.981 148.066 166.125 1.00 131.38 ? 141 TYR F CA  1 
ATOM   9396  C C   . TYR F  2 107 ? 213.506 148.351 167.524 1.00 139.89 ? 141 TYR F C   1 
ATOM   9397  O O   . TYR F  2 107 ? 213.275 149.435 168.070 1.00 138.83 ? 141 TYR F O   1 
ATOM   9398  C CB  . TYR F  2 107 ? 214.044 148.443 165.084 1.00 135.60 ? 141 TYR F CB  1 
ATOM   9399  C CG  . TYR F  2 107 ? 213.751 147.905 163.702 1.00 133.80 ? 141 TYR F CG  1 
ATOM   9400  C CD1 . TYR F  2 107 ? 213.787 146.542 163.444 1.00 144.11 ? 141 TYR F CD1 1 
ATOM   9401  C CD2 . TYR F  2 107 ? 213.431 148.760 162.657 1.00 132.79 ? 141 TYR F CD2 1 
ATOM   9402  C CE1 . TYR F  2 107 ? 213.517 146.047 162.183 1.00 145.88 ? 141 TYR F CE1 1 
ATOM   9403  C CE2 . TYR F  2 107 ? 213.160 148.274 161.393 1.00 131.19 ? 141 TYR F CE2 1 
ATOM   9404  C CZ  . TYR F  2 107 ? 213.204 146.917 161.162 1.00 135.57 ? 141 TYR F CZ  1 
ATOM   9405  O OH  . TYR F  2 107 ? 212.934 146.429 159.905 1.00 135.34 ? 141 TYR F OH  1 
ATOM   9406  N N   . PRO F  2 108 ? 214.210 147.398 168.129 1.00 144.59 ? 142 PRO F N   1 
ATOM   9407  C CA  . PRO F  2 108 ? 214.718 147.610 169.485 1.00 150.93 ? 142 PRO F CA  1 
ATOM   9408  C C   . PRO F  2 108 ? 216.061 148.323 169.482 1.00 162.56 ? 142 PRO F C   1 
ATOM   9409  O O   . PRO F  2 108 ? 216.824 148.282 168.514 1.00 167.85 ? 142 PRO F O   1 
ATOM   9410  C CB  . PRO F  2 108 ? 214.848 146.187 170.031 1.00 151.04 ? 142 PRO F CB  1 
ATOM   9411  C CG  . PRO F  2 108 ? 215.208 145.384 168.822 1.00 151.65 ? 142 PRO F CG  1 
ATOM   9412  C CD  . PRO F  2 108 ? 214.528 146.046 167.634 1.00 145.39 ? 142 PRO F CD  1 
ATOM   9413  N N   . GLU F  2 109 ? 216.342 148.987 170.600 1.00 168.36 ? 143 GLU F N   1 
ATOM   9414  C CA  . GLU F  2 109 ? 217.595 149.717 170.783 1.00 181.61 ? 143 GLU F CA  1 
ATOM   9415  C C   . GLU F  2 109 ? 218.667 148.728 171.223 1.00 193.74 ? 143 GLU F C   1 
ATOM   9416  O O   . GLU F  2 109 ? 218.676 148.269 172.368 1.00 200.53 ? 143 GLU F O   1 
ATOM   9417  C CB  . GLU F  2 109 ? 217.424 150.844 171.794 1.00 184.35 ? 143 GLU F CB  1 
ATOM   9418  C CG  . GLU F  2 109 ? 216.510 151.981 171.353 1.00 178.60 ? 143 GLU F CG  1 
ATOM   9419  C CD  . GLU F  2 109 ? 215.029 151.649 171.440 1.00 171.62 ? 143 GLU F CD  1 
ATOM   9420  O OE1 . GLU F  2 109 ? 214.622 150.539 171.042 1.00 168.18 ? 143 GLU F OE1 1 
ATOM   9421  O OE2 . GLU F  2 109 ? 214.265 152.513 171.915 1.00 170.85 ? 143 GLU F OE2 1 
ATOM   9422  N N   . LEU F  2 110 ? 219.575 148.402 170.309 1.00 199.37 ? 144 LEU F N   1 
ATOM   9423  C CA  . LEU F  2 110 ? 220.576 147.383 170.568 1.00 209.46 ? 144 LEU F CA  1 
ATOM   9424  C C   . LEU F  2 110 ? 221.702 147.934 171.446 1.00 226.35 ? 144 LEU F C   1 
ATOM   9425  O O   . LEU F  2 110 ? 222.119 149.084 171.287 1.00 232.07 ? 144 LEU F O   1 
ATOM   9426  C CB  . LEU F  2 110 ? 221.129 146.861 169.247 1.00 208.38 ? 144 LEU F CB  1 
ATOM   9427  C CG  . LEU F  2 110 ? 220.012 146.275 168.376 1.00 200.94 ? 144 LEU F CG  1 
ATOM   9428  C CD1 . LEU F  2 110 ? 220.467 146.014 166.952 1.00 205.08 ? 144 LEU F CD1 1 
ATOM   9429  C CD2 . LEU F  2 110 ? 219.464 145.004 169.011 1.00 203.66 ? 144 LEU F CD2 1 
ATOM   9430  N N   . PRO F  2 111 ? 222.210 147.131 172.376 1.00 230.44 ? 145 PRO F N   1 
ATOM   9431  C CA  . PRO F  2 111 ? 223.212 147.605 173.336 1.00 239.61 ? 145 PRO F CA  1 
ATOM   9432  C C   . PRO F  2 111 ? 224.643 147.526 172.809 1.00 245.34 ? 145 PRO F C   1 
ATOM   9433  O O   . PRO F  2 111 ? 224.889 147.279 171.627 1.00 244.77 ? 145 PRO F O   1 
ATOM   9434  C CB  . PRO F  2 111 ? 223.024 146.640 174.514 1.00 237.71 ? 145 PRO F CB  1 
ATOM   9435  C CG  . PRO F  2 111 ? 222.596 145.359 173.860 1.00 229.02 ? 145 PRO F CG  1 
ATOM   9436  C CD  . PRO F  2 111 ? 221.756 145.760 172.675 1.00 222.37 ? 145 PRO F CD  1 
ATOM   9437  N N   . LYS F  2 112 ? 225.590 147.758 173.723 1.00 248.66 ? 146 LYS F N   1 
ATOM   9438  C CA  . LYS F  2 112 ? 226.956 147.300 173.495 1.00 251.87 ? 146 LYS F CA  1 
ATOM   9439  C C   . LYS F  2 112 ? 226.939 145.811 173.178 1.00 251.93 ? 146 LYS F C   1 
ATOM   9440  O O   . LYS F  2 112 ? 226.349 145.027 173.935 1.00 247.04 ? 146 LYS F O   1 
ATOM   9441  C CB  . LYS F  2 112 ? 227.868 147.530 174.712 1.00 253.82 ? 146 LYS F CB  1 
ATOM   9442  C CG  . LYS F  2 112 ? 227.872 148.859 175.492 1.00 254.67 ? 146 LYS F CG  1 
ATOM   9443  C CD  . LYS F  2 112 ? 228.034 150.106 174.629 1.00 256.64 ? 146 LYS F CD  1 
ATOM   9444  C CE  . LYS F  2 112 ? 226.745 150.707 174.177 1.00 255.54 ? 146 LYS F CE  1 
ATOM   9445  N NZ  . LYS F  2 112 ? 226.919 152.136 173.801 1.00 255.78 ? 146 LYS F NZ  1 
ATOM   9446  N N   . PRO F  2 113 ? 227.558 145.381 172.086 1.00 258.18 ? 147 PRO F N   1 
ATOM   9447  C CA  . PRO F  2 113 ? 227.803 143.949 171.907 1.00 261.99 ? 147 PRO F CA  1 
ATOM   9448  C C   . PRO F  2 113 ? 229.066 143.524 172.634 1.00 266.24 ? 147 PRO F C   1 
ATOM   9449  O O   . PRO F  2 113 ? 229.693 144.336 173.322 1.00 267.04 ? 147 PRO F O   1 
ATOM   9450  C CB  . PRO F  2 113 ? 227.932 143.799 170.387 1.00 263.69 ? 147 PRO F CB  1 
ATOM   9451  C CG  . PRO F  2 113 ? 228.353 145.160 169.889 1.00 262.37 ? 147 PRO F CG  1 
ATOM   9452  C CD  . PRO F  2 113 ? 228.111 146.181 170.980 1.00 259.75 ? 147 PRO F CD  1 
ATOM   9453  N N   . SER F  2 114 ? 229.440 142.256 172.505 1.00 270.40 ? 148 SER F N   1 
ATOM   9454  C CA  . SER F  2 114 ? 230.670 141.754 173.094 1.00 279.44 ? 148 SER F CA  1 
ATOM   9455  C C   . SER F  2 114 ? 231.220 140.655 172.199 1.00 285.93 ? 148 SER F C   1 
ATOM   9456  O O   . SER F  2 114 ? 230.493 140.045 171.412 1.00 285.83 ? 148 SER F O   1 
ATOM   9457  C CB  . SER F  2 114 ? 230.448 141.249 174.526 1.00 281.61 ? 148 SER F CB  1 
ATOM   9458  O OG  . SER F  2 114 ? 229.475 140.223 174.567 1.00 281.46 ? 148 SER F OG  1 
ATOM   9459  N N   . ILE F  2 115 ? 232.521 140.411 172.328 1.00 290.58 ? 149 ILE F N   1 
ATOM   9460  C CA  . ILE F  2 115 ? 233.261 139.551 171.414 1.00 295.50 ? 149 ILE F CA  1 
ATOM   9461  C C   . ILE F  2 115 ? 233.873 138.405 172.204 1.00 300.57 ? 149 ILE F C   1 
ATOM   9462  O O   . ILE F  2 115 ? 234.209 138.558 173.383 1.00 300.36 ? 149 ILE F O   1 
ATOM   9463  C CB  . ILE F  2 115 ? 234.354 140.333 170.653 1.00 294.76 ? 149 ILE F CB  1 
ATOM   9464  C CG1 . ILE F  2 115 ? 233.864 141.735 170.283 1.00 290.08 ? 149 ILE F CG1 1 
ATOM   9465  C CG2 . ILE F  2 115 ? 234.787 139.578 169.407 1.00 299.77 ? 149 ILE F CG2 1 
ATOM   9466  C CD1 . ILE F  2 115 ? 234.274 142.808 171.264 1.00 288.93 ? 149 ILE F CD1 1 
ATOM   9467  N N   . SER F  2 116 ? 234.014 137.255 171.548 1.00 304.63 ? 150 SER F N   1 
ATOM   9468  C CA  . SER F  2 116 ? 234.598 136.069 172.152 1.00 309.13 ? 150 SER F CA  1 
ATOM   9469  C C   . SER F  2 116 ? 235.551 135.407 171.168 1.00 314.61 ? 150 SER F C   1 
ATOM   9470  O O   . SER F  2 116 ? 235.383 135.507 169.949 1.00 313.46 ? 150 SER F O   1 
ATOM   9471  C CB  . SER F  2 116 ? 233.516 135.071 172.583 1.00 307.97 ? 150 SER F CB  1 
ATOM   9472  O OG  . SER F  2 116 ? 232.489 134.988 171.611 1.00 302.86 ? 150 SER F OG  1 
ATOM   9473  N N   . SER F  2 117 ? 236.558 134.733 171.714 1.00 320.24 ? 151 SER F N   1 
ATOM   9474  C CA  . SER F  2 117 ? 237.549 133.998 170.942 1.00 326.88 ? 151 SER F CA  1 
ATOM   9475  C C   . SER F  2 117 ? 237.711 132.609 171.539 1.00 333.28 ? 151 SER F C   1 
ATOM   9476  O O   . SER F  2 117 ? 237.697 132.452 172.764 1.00 332.94 ? 151 SER F O   1 
ATOM   9477  C CB  . SER F  2 117 ? 238.894 134.730 170.944 1.00 329.47 ? 151 SER F CB  1 
ATOM   9478  O OG  . SER F  2 117 ? 239.918 133.925 170.392 1.00 334.89 ? 151 SER F OG  1 
ATOM   9479  N N   . ASN F  2 118 ? 237.865 131.592 170.686 1.00 336.95 ? 152 ASN F N   1 
ATOM   9480  C CA  . ASN F  2 118 ? 238.032 130.260 171.251 1.00 338.74 ? 152 ASN F CA  1 
ATOM   9481  C C   . ASN F  2 118 ? 239.460 130.001 171.716 1.00 341.25 ? 152 ASN F C   1 
ATOM   9482  O O   . ASN F  2 118 ? 239.691 129.037 172.452 1.00 341.25 ? 152 ASN F O   1 
ATOM   9483  C CB  . ASN F  2 118 ? 237.574 129.161 170.263 1.00 339.72 ? 152 ASN F CB  1 
ATOM   9484  C CG  . ASN F  2 118 ? 238.630 128.767 169.206 1.00 342.33 ? 152 ASN F CG  1 
ATOM   9485  O OD1 . ASN F  2 118 ? 239.798 129.146 169.266 1.00 343.27 ? 152 ASN F OD1 1 
ATOM   9486  N ND2 . ASN F  2 118 ? 238.200 127.937 168.254 1.00 343.68 ? 152 ASN F ND2 1 
ATOM   9487  N N   . ASN F  2 119 ? 240.413 130.834 171.300 1.00 343.71 ? 153 ASN F N   1 
ATOM   9488  C CA  . ASN F  2 119 ? 241.823 130.645 171.609 1.00 346.74 ? 153 ASN F CA  1 
ATOM   9489  C C   . ASN F  2 119 ? 242.382 131.947 172.156 1.00 347.74 ? 153 ASN F C   1 
ATOM   9490  O O   . ASN F  2 119 ? 242.462 132.944 171.432 1.00 346.79 ? 153 ASN F O   1 
ATOM   9491  C CB  . ASN F  2 119 ? 242.609 130.208 170.366 1.00 348.31 ? 153 ASN F CB  1 
ATOM   9492  C CG  . ASN F  2 119 ? 244.066 129.914 170.666 1.00 350.76 ? 153 ASN F CG  1 
ATOM   9493  O OD1 . ASN F  2 119 ? 244.472 129.834 171.826 1.00 352.05 ? 153 ASN F OD1 1 
ATOM   9494  N ND2 . ASN F  2 119 ? 244.864 129.753 169.617 1.00 352.17 ? 153 ASN F ND2 1 
ATOM   9495  N N   . SER F  2 120 ? 242.767 131.933 173.431 1.00 350.12 ? 154 SER F N   1 
ATOM   9496  C CA  . SER F  2 120 ? 243.303 133.115 174.092 1.00 349.92 ? 154 SER F CA  1 
ATOM   9497  C C   . SER F  2 120 ? 244.727 133.452 173.673 1.00 349.96 ? 154 SER F C   1 
ATOM   9498  O O   . SER F  2 120 ? 245.106 134.627 173.721 1.00 346.18 ? 154 SER F O   1 
ATOM   9499  C CB  . SER F  2 120 ? 243.259 132.935 175.614 1.00 349.88 ? 154 SER F CB  1 
ATOM   9500  O OG  . SER F  2 120 ? 243.781 131.672 175.991 1.00 350.69 ? 154 SER F OG  1 
ATOM   9501  N N   . ASN F  2 121 ? 245.519 132.462 173.265 1.00 351.70 ? 155 ASN F N   1 
ATOM   9502  C CA  . ASN F  2 121 ? 246.920 132.661 172.895 1.00 350.54 ? 155 ASN F CA  1 
ATOM   9503  C C   . ASN F  2 121 ? 247.144 132.112 171.493 1.00 352.13 ? 155 ASN F C   1 
ATOM   9504  O O   . ASN F  2 121 ? 247.532 130.948 171.324 1.00 354.02 ? 155 ASN F O   1 
ATOM   9505  C CB  . ASN F  2 121 ? 247.856 131.994 173.903 1.00 350.31 ? 155 ASN F CB  1 
ATOM   9506  C CG  . ASN F  2 121 ? 247.415 132.209 175.338 1.00 349.72 ? 155 ASN F CG  1 
ATOM   9507  O OD1 . ASN F  2 121 ? 246.629 131.433 175.880 1.00 350.90 ? 155 ASN F OD1 1 
ATOM   9508  N ND2 . ASN F  2 121 ? 247.920 133.268 175.960 1.00 346.42 ? 155 ASN F ND2 1 
ATOM   9509  N N   . PRO F  2 122 ? 246.886 132.917 170.461 1.00 351.46 ? 156 PRO F N   1 
ATOM   9510  C CA  . PRO F  2 122 ? 247.157 132.467 169.091 1.00 353.11 ? 156 PRO F CA  1 
ATOM   9511  C C   . PRO F  2 122 ? 248.618 132.079 168.912 1.00 354.43 ? 156 PRO F C   1 
ATOM   9512  O O   . PRO F  2 122 ? 249.522 132.719 169.453 1.00 352.09 ? 156 PRO F O   1 
ATOM   9513  C CB  . PRO F  2 122 ? 246.802 133.689 168.240 1.00 350.55 ? 156 PRO F CB  1 
ATOM   9514  C CG  . PRO F  2 122 ? 245.799 134.441 169.039 1.00 345.11 ? 156 PRO F CG  1 
ATOM   9515  C CD  . PRO F  2 122 ? 245.990 134.087 170.495 1.00 347.97 ? 156 PRO F CD  1 
ATOM   9516  N N   . VAL F  2 123 ? 248.842 131.019 168.142 1.00 356.17 ? 157 VAL F N   1 
ATOM   9517  C CA  . VAL F  2 123 ? 250.196 130.583 167.825 1.00 355.51 ? 157 VAL F CA  1 
ATOM   9518  C C   . VAL F  2 123 ? 250.782 131.538 166.794 1.00 356.18 ? 157 VAL F C   1 
ATOM   9519  O O   . VAL F  2 123 ? 250.145 131.841 165.777 1.00 358.35 ? 157 VAL F O   1 
ATOM   9520  C CB  . VAL F  2 123 ? 250.198 129.133 167.318 1.00 355.55 ? 157 VAL F CB  1 
ATOM   9521  C CG1 . VAL F  2 123 ? 251.618 128.672 167.037 1.00 355.65 ? 157 VAL F CG1 1 
ATOM   9522  C CG2 . VAL F  2 123 ? 249.523 128.217 168.328 1.00 353.19 ? 157 VAL F CG2 1 
ATOM   9523  N N   . GLU F  2 124 ? 251.998 132.021 167.059 1.00 352.76 ? 158 GLU F N   1 
ATOM   9524  C CA  . GLU F  2 124 ? 252.550 133.127 166.281 1.00 350.46 ? 158 GLU F CA  1 
ATOM   9525  C C   . GLU F  2 124 ? 252.753 132.750 164.817 1.00 356.88 ? 158 GLU F C   1 
ATOM   9526  O O   . GLU F  2 124 ? 252.445 133.544 163.920 1.00 356.84 ? 158 GLU F O   1 
ATOM   9527  C CB  . GLU F  2 124 ? 253.865 133.594 166.903 1.00 341.72 ? 158 GLU F CB  1 
ATOM   9528  C CG  . GLU F  2 124 ? 253.749 133.956 168.375 1.00 334.70 ? 158 GLU F CG  1 
ATOM   9529  C CD  . GLU F  2 124 ? 255.077 134.351 168.986 1.00 325.90 ? 158 GLU F CD  1 
ATOM   9530  O OE1 . GLU F  2 124 ? 255.984 134.761 168.231 1.00 324.49 ? 158 GLU F OE1 1 
ATOM   9531  O OE2 . GLU F  2 124 ? 255.215 134.248 170.223 1.00 322.81 ? 158 GLU F OE2 1 
ATOM   9532  N N   . ASP F  2 125 ? 253.277 131.551 164.552 1.00 359.21 ? 159 ASP F N   1 
ATOM   9533  C CA  . ASP F  2 125 ? 253.566 131.174 163.171 1.00 361.49 ? 159 ASP F CA  1 
ATOM   9534  C C   . ASP F  2 125 ? 252.287 131.018 162.351 1.00 362.78 ? 159 ASP F C   1 
ATOM   9535  O O   . ASP F  2 125 ? 252.224 131.472 161.203 1.00 363.40 ? 159 ASP F O   1 
ATOM   9536  C CB  . ASP F  2 125 ? 254.418 129.900 163.135 1.00 361.92 ? 159 ASP F CB  1 
ATOM   9537  C CG  . ASP F  2 125 ? 253.627 128.636 163.441 1.00 361.78 ? 159 ASP F CG  1 
ATOM   9538  O OD1 . ASP F  2 125 ? 252.529 128.729 164.027 1.00 361.53 ? 159 ASP F OD1 1 
ATOM   9539  O OD2 . ASP F  2 125 ? 254.110 127.540 163.089 1.00 360.97 ? 159 ASP F OD2 1 
ATOM   9540  N N   . LYS F  2 126 ? 251.259 130.396 162.926 1.00 362.95 ? 160 LYS F N   1 
ATOM   9541  C CA  . LYS F  2 126 ? 249.987 130.192 162.246 1.00 363.42 ? 160 LYS F CA  1 
ATOM   9542  C C   . LYS F  2 126 ? 248.964 129.694 163.256 1.00 362.80 ? 160 LYS F C   1 
ATOM   9543  O O   . LYS F  2 126 ? 249.305 128.970 164.195 1.00 361.61 ? 160 LYS F O   1 
ATOM   9544  C CB  . LYS F  2 126 ? 250.120 129.200 161.078 1.00 362.80 ? 160 LYS F CB  1 
ATOM   9545  C CG  . LYS F  2 126 ? 250.677 127.826 161.450 1.00 360.41 ? 160 LYS F CG  1 
ATOM   9546  C CD  . LYS F  2 126 ? 249.574 126.829 161.787 1.00 357.03 ? 160 LYS F CD  1 
ATOM   9547  C CE  . LYS F  2 126 ? 250.124 125.625 162.533 1.00 352.45 ? 160 LYS F CE  1 
ATOM   9548  N NZ  . LYS F  2 126 ? 249.066 124.932 163.319 1.00 346.98 ? 160 LYS F NZ  1 
ATOM   9549  N N   . ASP F  2 127 ? 247.712 130.092 163.051 1.00 364.29 ? 161 ASP F N   1 
ATOM   9550  C CA  . ASP F  2 127 ? 246.597 129.626 163.866 1.00 363.42 ? 161 ASP F CA  1 
ATOM   9551  C C   . ASP F  2 127 ? 245.310 129.942 163.116 1.00 363.99 ? 161 ASP F C   1 
ATOM   9552  O O   . ASP F  2 127 ? 245.293 130.761 162.195 1.00 365.59 ? 161 ASP F O   1 
ATOM   9553  C CB  . ASP F  2 127 ? 246.596 130.271 165.255 1.00 361.51 ? 161 ASP F CB  1 
ATOM   9554  C CG  . ASP F  2 127 ? 246.002 129.369 166.316 1.00 359.53 ? 161 ASP F CG  1 
ATOM   9555  O OD1 . ASP F  2 127 ? 245.844 128.160 166.048 1.00 359.55 ? 161 ASP F OD1 1 
ATOM   9556  O OD2 . ASP F  2 127 ? 245.692 129.870 167.417 1.00 357.44 ? 161 ASP F OD2 1 
ATOM   9557  N N   . ALA F  2 128 ? 244.228 129.289 163.530 1.00 362.49 ? 162 ALA F N   1 
ATOM   9558  C CA  . ALA F  2 128 ? 242.923 129.446 162.902 1.00 360.82 ? 162 ALA F CA  1 
ATOM   9559  C C   . ALA F  2 128 ? 241.900 129.989 163.894 1.00 358.70 ? 162 ALA F C   1 
ATOM   9560  O O   . ALA F  2 128 ? 240.758 129.531 163.952 1.00 356.72 ? 162 ALA F O   1 
ATOM   9561  C CB  . ALA F  2 128 ? 242.447 128.127 162.298 1.00 357.88 ? 162 ALA F CB  1 
ATOM   9562  N N   . VAL F  2 129 ? 242.308 130.985 164.685 1.00 358.58 ? 163 VAL F N   1 
ATOM   9563  C CA  . VAL F  2 129 ? 241.443 131.512 165.731 1.00 353.70 ? 163 VAL F CA  1 
ATOM   9564  C C   . VAL F  2 129 ? 240.199 132.155 165.115 1.00 351.16 ? 163 VAL F C   1 
ATOM   9565  O O   . VAL F  2 129 ? 240.240 132.724 164.016 1.00 351.98 ? 163 VAL F O   1 
ATOM   9566  C CB  . VAL F  2 129 ? 242.215 132.512 166.610 1.00 351.52 ? 163 VAL F CB  1 
ATOM   9567  C CG1 . VAL F  2 129 ? 242.607 133.748 165.812 1.00 350.42 ? 163 VAL F CG1 1 
ATOM   9568  C CG2 . VAL F  2 129 ? 241.408 132.889 167.839 1.00 345.72 ? 163 VAL F CG2 1 
ATOM   9569  N N   . ALA F  2 130 ? 239.077 132.046 165.826 1.00 346.32 ? 164 ALA F N   1 
ATOM   9570  C CA  . ALA F  2 130 ? 237.797 132.554 165.357 1.00 339.60 ? 164 ALA F CA  1 
ATOM   9571  C C   . ALA F  2 130 ? 237.239 133.566 166.347 1.00 331.00 ? 164 ALA F C   1 
ATOM   9572  O O   . ALA F  2 130 ? 237.266 133.343 167.561 1.00 329.96 ? 164 ALA F O   1 
ATOM   9573  C CB  . ALA F  2 130 ? 236.789 131.417 165.151 1.00 337.26 ? 164 ALA F CB  1 
ATOM   9574  N N   . PHE F  2 131 ? 236.732 134.678 165.818 1.00 326.01 ? 165 PHE F N   1 
ATOM   9575  C CA  . PHE F  2 131 ? 236.076 135.710 166.604 1.00 318.87 ? 165 PHE F CA  1 
ATOM   9576  C C   . PHE F  2 131 ? 234.576 135.667 166.352 1.00 313.99 ? 165 PHE F C   1 
ATOM   9577  O O   . PHE F  2 131 ? 234.128 135.411 165.231 1.00 314.36 ? 165 PHE F O   1 
ATOM   9578  C CB  . PHE F  2 131 ? 236.609 137.106 166.261 1.00 318.01 ? 165 PHE F CB  1 
ATOM   9579  C CG  . PHE F  2 131 ? 237.946 137.413 166.866 1.00 317.77 ? 165 PHE F CG  1 
ATOM   9580  C CD1 . PHE F  2 131 ? 238.493 136.585 167.830 1.00 320.73 ? 165 PHE F CD1 1 
ATOM   9581  C CD2 . PHE F  2 131 ? 238.653 138.537 166.475 1.00 313.96 ? 165 PHE F CD2 1 
ATOM   9582  C CE1 . PHE F  2 131 ? 239.723 136.870 168.387 1.00 319.54 ? 165 PHE F CE1 1 
ATOM   9583  C CE2 . PHE F  2 131 ? 239.881 138.825 167.030 1.00 312.42 ? 165 PHE F CE2 1 
ATOM   9584  C CZ  . PHE F  2 131 ? 240.415 137.991 167.988 1.00 314.10 ? 165 PHE F CZ  1 
ATOM   9585  N N   . THR F  2 132 ? 233.800 135.920 167.403 1.00 309.00 ? 166 THR F N   1 
ATOM   9586  C CA  . THR F  2 132 ? 232.349 135.895 167.299 1.00 303.66 ? 166 THR F CA  1 
ATOM   9587  C C   . THR F  2 132 ? 231.759 136.918 168.257 1.00 300.65 ? 166 THR F C   1 
ATOM   9588  O O   . THR F  2 132 ? 232.207 137.038 169.399 1.00 301.14 ? 166 THR F O   1 
ATOM   9589  C CB  . THR F  2 132 ? 231.789 134.500 167.608 1.00 302.18 ? 166 THR F CB  1 
ATOM   9590  O OG1 . THR F  2 132 ? 232.422 133.529 166.765 1.00 305.26 ? 166 THR F OG1 1 
ATOM   9591  C CG2 . THR F  2 132 ? 230.286 134.459 167.373 1.00 296.72 ? 166 THR F CG2 1 
ATOM   9592  N N   . CYS F  2 133 ? 230.758 137.657 167.780 1.00 298.29 ? 167 CYS F N   1 
ATOM   9593  C CA  . CYS F  2 133 ? 230.003 138.584 168.615 1.00 293.54 ? 167 CYS F CA  1 
ATOM   9594  C C   . CYS F  2 133 ? 228.808 137.834 169.194 1.00 288.36 ? 167 CYS F C   1 
ATOM   9595  O O   . CYS F  2 133 ? 227.821 137.594 168.494 1.00 285.04 ? 167 CYS F O   1 
ATOM   9596  C CB  . CYS F  2 133 ? 229.562 139.805 167.809 1.00 293.27 ? 167 CYS F CB  1 
ATOM   9597  S SG  . CYS F  2 133 ? 230.795 140.407 166.625 1.00 301.07 ? 167 CYS F SG  1 
ATOM   9598  N N   . GLU F  2 134 ? 228.898 137.467 170.473 1.00 288.44 ? 168 GLU F N   1 
ATOM   9599  C CA  . GLU F  2 134 ? 227.928 136.604 171.145 1.00 284.83 ? 168 GLU F CA  1 
ATOM   9600  C C   . GLU F  2 134 ? 226.489 137.126 171.209 1.00 277.43 ? 168 GLU F C   1 
ATOM   9601  O O   . GLU F  2 134 ? 225.564 136.342 170.960 1.00 273.63 ? 168 GLU F O   1 
ATOM   9602  C CB  . GLU F  2 134 ? 228.411 136.279 172.564 1.00 288.38 ? 168 GLU F CB  1 
ATOM   9603  C CG  . GLU F  2 134 ? 229.094 137.417 173.300 1.00 289.35 ? 168 GLU F CG  1 
ATOM   9604  C CD  . GLU F  2 134 ? 230.591 137.458 173.061 1.00 294.63 ? 168 GLU F CD  1 
ATOM   9605  O OE1 . GLU F  2 134 ? 231.020 137.195 171.919 1.00 296.56 ? 168 GLU F OE1 1 
ATOM   9606  O OE2 . GLU F  2 134 ? 231.338 137.759 174.016 1.00 297.80 ? 168 GLU F OE2 1 
ATOM   9607  N N   . PRO F  2 135 ? 226.224 138.418 171.534 1.00 274.76 ? 169 PRO F N   1 
ATOM   9608  C CA  . PRO F  2 135 ? 224.837 138.797 171.851 1.00 269.43 ? 169 PRO F CA  1 
ATOM   9609  C C   . PRO F  2 135 ? 223.925 138.781 170.635 1.00 266.79 ? 169 PRO F C   1 
ATOM   9610  O O   . PRO F  2 135 ? 223.680 139.816 170.006 1.00 265.03 ? 169 PRO F O   1 
ATOM   9611  C CB  . PRO F  2 135 ? 224.979 140.208 172.431 1.00 265.06 ? 169 PRO F CB  1 
ATOM   9612  C CG  . PRO F  2 135 ? 226.194 140.751 171.813 1.00 266.83 ? 169 PRO F CG  1 
ATOM   9613  C CD  . PRO F  2 135 ? 227.101 139.604 171.472 1.00 274.11 ? 169 PRO F CD  1 
ATOM   9614  N N   . GLU F  2 136 ? 223.425 137.592 170.301 1.00 265.88 ? 170 GLU F N   1 
ATOM   9615  C CA  . GLU F  2 136 ? 222.620 137.414 169.100 1.00 262.83 ? 170 GLU F CA  1 
ATOM   9616  C C   . GLU F  2 136 ? 221.313 138.192 169.183 1.00 259.29 ? 170 GLU F C   1 
ATOM   9617  O O   . GLU F  2 136 ? 220.617 138.169 170.202 1.00 258.91 ? 170 GLU F O   1 
ATOM   9618  C CB  . GLU F  2 136 ? 222.332 135.927 168.880 1.00 263.47 ? 170 GLU F CB  1 
ATOM   9619  C CG  . GLU F  2 136 ? 221.567 135.578 167.598 1.00 261.24 ? 170 GLU F CG  1 
ATOM   9620  C CD  . GLU F  2 136 ? 222.180 136.166 166.333 1.00 264.20 ? 170 GLU F CD  1 
ATOM   9621  O OE1 . GLU F  2 136 ? 222.086 137.393 166.117 1.00 262.18 ? 170 GLU F OE1 1 
ATOM   9622  O OE2 . GLU F  2 136 ? 222.767 135.390 165.550 1.00 268.27 ? 170 GLU F OE2 1 
ATOM   9623  N N   . THR F  2 137 ? 220.980 138.878 168.090 1.00 255.18 ? 171 THR F N   1 
ATOM   9624  C CA  . THR F  2 137 ? 219.733 139.617 167.961 1.00 249.22 ? 171 THR F CA  1 
ATOM   9625  C C   . THR F  2 137 ? 219.210 139.463 166.541 1.00 243.02 ? 171 THR F C   1 
ATOM   9626  O O   . THR F  2 137 ? 219.970 139.184 165.610 1.00 243.28 ? 171 THR F O   1 
ATOM   9627  C CB  . THR F  2 137 ? 219.907 141.108 168.293 1.00 249.07 ? 171 THR F CB  1 
ATOM   9628  O OG1 . THR F  2 137 ? 221.047 141.627 167.597 1.00 246.40 ? 171 THR F OG1 1 
ATOM   9629  C CG2 . THR F  2 137 ? 220.086 141.318 169.791 1.00 252.93 ? 171 THR F CG2 1 
ATOM   9630  N N   . GLN F  2 138 ? 217.902 139.645 166.383 1.00 237.41 ? 172 GLN F N   1 
ATOM   9631  C CA  . GLN F  2 138 ? 217.269 139.481 165.085 1.00 230.51 ? 172 GLN F CA  1 
ATOM   9632  C C   . GLN F  2 138 ? 217.430 140.739 164.234 1.00 222.60 ? 172 GLN F C   1 
ATOM   9633  O O   . GLN F  2 138 ? 217.832 141.800 164.718 1.00 220.92 ? 172 GLN F O   1 
ATOM   9634  C CB  . GLN F  2 138 ? 215.787 139.145 165.248 1.00 229.42 ? 172 GLN F CB  1 
ATOM   9635  C CG  . GLN F  2 138 ? 215.523 137.815 165.935 1.00 232.66 ? 172 GLN F CG  1 
ATOM   9636  C CD  . GLN F  2 138 ? 216.208 136.654 165.241 1.00 236.29 ? 172 GLN F CD  1 
ATOM   9637  O OE1 . GLN F  2 138 ? 216.906 135.862 165.874 1.00 238.90 ? 172 GLN F OE1 1 
ATOM   9638  N NE2 . GLN F  2 138 ? 216.010 136.546 163.932 1.00 236.43 ? 172 GLN F NE2 1 
ATOM   9639  N N   . ASP F  2 139 ? 217.142 140.581 162.936 1.00 219.40 ? 173 ASP F N   1 
ATOM   9640  C CA  . ASP F  2 139 ? 217.074 141.616 161.899 1.00 215.03 ? 173 ASP F CA  1 
ATOM   9641  C C   . ASP F  2 139 ? 218.065 142.755 162.112 1.00 214.22 ? 173 ASP F C   1 
ATOM   9642  O O   . ASP F  2 139 ? 217.668 143.921 162.197 1.00 210.20 ? 173 ASP F O   1 
ATOM   9643  C CB  . ASP F  2 139 ? 215.646 142.179 161.725 1.00 210.24 ? 173 ASP F CB  1 
ATOM   9644  C CG  . ASP F  2 139 ? 214.914 142.450 163.035 1.00 206.05 ? 173 ASP F CG  1 
ATOM   9645  O OD1 . ASP F  2 139 ? 213.666 142.455 163.006 1.00 200.80 ? 173 ASP F OD1 1 
ATOM   9646  O OD2 . ASP F  2 139 ? 215.544 142.764 164.059 1.00 205.05 ? 173 ASP F OD2 1 
ATOM   9647  N N   . THR F  2 140 ? 219.351 142.431 162.199 1.00 216.15 ? 174 THR F N   1 
ATOM   9648  C CA  . THR F  2 140 ? 220.402 143.419 162.386 1.00 220.17 ? 174 THR F CA  1 
ATOM   9649  C C   . THR F  2 140 ? 221.593 143.116 161.484 1.00 224.57 ? 174 THR F C   1 
ATOM   9650  O O   . THR F  2 140 ? 221.727 142.011 160.951 1.00 224.68 ? 174 THR F O   1 
ATOM   9651  C CB  . THR F  2 140 ? 220.848 143.474 163.850 1.00 223.80 ? 174 THR F CB  1 
ATOM   9652  O OG1 . THR F  2 140 ? 222.114 144.138 163.947 1.00 226.36 ? 174 THR F OG1 1 
ATOM   9653  C CG2 . THR F  2 140 ? 220.946 142.077 164.432 1.00 229.64 ? 174 THR F CG2 1 
ATOM   9654  N N   . THR F  2 141 ? 222.461 144.113 161.323 1.00 226.48 ? 175 THR F N   1 
ATOM   9655  C CA  . THR F  2 141 ? 223.605 144.038 160.423 1.00 232.01 ? 175 THR F CA  1 
ATOM   9656  C C   . THR F  2 141 ? 224.897 144.056 161.230 1.00 237.67 ? 175 THR F C   1 
ATOM   9657  O O   . THR F  2 141 ? 225.039 144.845 162.170 1.00 237.55 ? 175 THR F O   1 
ATOM   9658  C CB  . THR F  2 141 ? 223.592 145.192 159.418 1.00 230.97 ? 175 THR F CB  1 
ATOM   9659  O OG1 . THR F  2 141 ? 222.327 145.228 158.747 1.00 229.07 ? 175 THR F OG1 1 
ATOM   9660  C CG2 . THR F  2 141 ? 224.699 145.018 158.388 1.00 236.47 ? 175 THR F CG2 1 
ATOM   9661  N N   . TYR F  2 142 ? 225.828 143.181 160.859 1.00 245.62 ? 176 TYR F N   1 
ATOM   9662  C CA  . TYR F  2 142 ? 227.050 142.929 161.614 1.00 252.29 ? 176 TYR F CA  1 
ATOM   9663  C C   . TYR F  2 142 ? 228.250 143.485 160.858 1.00 258.48 ? 176 TYR F C   1 
ATOM   9664  O O   . TYR F  2 142 ? 228.396 143.244 159.655 1.00 263.10 ? 176 TYR F O   1 
ATOM   9665  C CB  . TYR F  2 142 ? 227.226 141.428 161.865 1.00 258.67 ? 176 TYR F CB  1 
ATOM   9666  C CG  . TYR F  2 142 ? 226.077 140.744 162.593 1.00 259.01 ? 176 TYR F CG  1 
ATOM   9667  C CD1 . TYR F  2 142 ? 224.961 141.449 163.017 1.00 250.76 ? 176 TYR F CD1 1 
ATOM   9668  C CD2 . TYR F  2 142 ? 226.086 139.377 162.797 1.00 267.22 ? 176 TYR F CD2 1 
ATOM   9669  C CE1 . TYR F  2 142 ? 223.922 140.824 163.663 1.00 250.93 ? 176 TYR F CE1 1 
ATOM   9670  C CE2 . TYR F  2 142 ? 225.039 138.739 163.440 1.00 267.03 ? 176 TYR F CE2 1 
ATOM   9671  C CZ  . TYR F  2 142 ? 223.961 139.469 163.871 1.00 259.48 ? 176 TYR F CZ  1 
ATOM   9672  O OH  . TYR F  2 142 ? 222.915 138.844 164.511 1.00 259.13 ? 176 TYR F OH  1 
ATOM   9673  N N   . LEU F  2 143 ? 229.105 144.223 161.563 1.00 261.31 ? 177 LEU F N   1 
ATOM   9674  C CA  . LEU F  2 143 ? 230.237 144.913 160.960 1.00 266.74 ? 177 LEU F CA  1 
ATOM   9675  C C   . LEU F  2 143 ? 231.461 144.761 161.854 1.00 272.47 ? 177 LEU F C   1 
ATOM   9676  O O   . LEU F  2 143 ? 231.371 144.948 163.072 1.00 272.32 ? 177 LEU F O   1 
ATOM   9677  C CB  . LEU F  2 143 ? 229.896 146.390 160.735 1.00 266.41 ? 177 LEU F CB  1 
ATOM   9678  C CG  . LEU F  2 143 ? 230.976 147.471 160.762 1.00 272.06 ? 177 LEU F CG  1 
ATOM   9679  C CD1 . LEU F  2 143 ? 231.958 147.294 159.614 1.00 276.56 ? 177 LEU F CD1 1 
ATOM   9680  C CD2 . LEU F  2 143 ? 230.326 148.846 160.708 1.00 269.75 ? 177 LEU F CD2 1 
ATOM   9681  N N   . TRP F  2 144 ? 232.598 144.426 161.247 1.00 277.74 ? 178 TRP F N   1 
ATOM   9682  C CA  . TRP F  2 144 ? 233.846 144.199 161.967 1.00 282.03 ? 178 TRP F CA  1 
ATOM   9683  C C   . TRP F  2 144 ? 234.813 145.349 161.715 1.00 283.44 ? 178 TRP F C   1 
ATOM   9684  O O   . TRP F  2 144 ? 234.718 146.033 160.691 1.00 283.61 ? 178 TRP F O   1 
ATOM   9685  C CB  . TRP F  2 144 ? 234.485 142.874 161.551 1.00 287.84 ? 178 TRP F CB  1 
ATOM   9686  C CG  . TRP F  2 144 ? 233.589 141.698 161.742 1.00 289.64 ? 178 TRP F CG  1 
ATOM   9687  C CD1 . TRP F  2 144 ? 232.581 141.290 160.919 1.00 288.62 ? 178 TRP F CD1 1 
ATOM   9688  C CD2 . TRP F  2 144 ? 233.615 140.774 162.834 1.00 292.88 ? 178 TRP F CD2 1 
ATOM   9689  N NE1 . TRP F  2 144 ? 231.979 140.167 161.430 1.00 292.53 ? 178 TRP F NE1 1 
ATOM   9690  C CE2 . TRP F  2 144 ? 232.596 139.830 162.606 1.00 296.91 ? 178 TRP F CE2 1 
ATOM   9691  C CE3 . TRP F  2 144 ? 234.402 140.652 163.983 1.00 295.33 ? 178 TRP F CE3 1 
ATOM   9692  C CZ2 . TRP F  2 144 ? 232.345 138.780 163.481 1.00 301.95 ? 178 TRP F CZ2 1 
ATOM   9693  C CZ3 . TRP F  2 144 ? 234.150 139.608 164.852 1.00 302.24 ? 178 TRP F CZ3 1 
ATOM   9694  C CH2 . TRP F  2 144 ? 233.130 138.686 164.597 1.00 303.79 ? 178 TRP F CH2 1 
ATOM   9695  N N   . TRP F  2 145 ? 235.744 145.552 162.645 1.00 284.75 ? 179 TRP F N   1 
ATOM   9696  C CA  . TRP F  2 145 ? 236.653 146.689 162.614 1.00 288.15 ? 179 TRP F CA  1 
ATOM   9697  C C   . TRP F  2 145 ? 238.017 146.248 163.130 1.00 294.08 ? 179 TRP F C   1 
ATOM   9698  O O   . TRP F  2 145 ? 238.124 145.738 164.251 1.00 296.73 ? 179 TRP F O   1 
ATOM   9699  C CB  . TRP F  2 145 ? 236.084 147.829 163.464 1.00 285.24 ? 179 TRP F CB  1 
ATOM   9700  C CG  . TRP F  2 145 ? 235.135 148.714 162.708 1.00 282.41 ? 179 TRP F CG  1 
ATOM   9701  C CD1 . TRP F  2 145 ? 233.774 148.693 162.787 1.00 279.97 ? 179 TRP F CD1 1 
ATOM   9702  C CD2 . TRP F  2 145 ? 235.465 149.781 161.807 1.00 286.35 ? 179 TRP F CD2 1 
ATOM   9703  N NE1 . TRP F  2 145 ? 233.235 149.649 161.965 1.00 280.52 ? 179 TRP F NE1 1 
ATOM   9704  C CE2 . TRP F  2 145 ? 234.250 150.337 161.358 1.00 283.98 ? 179 TRP F CE2 1 
ATOM   9705  C CE3 . TRP F  2 145 ? 236.664 150.312 161.329 1.00 291.47 ? 179 TRP F CE3 1 
ATOM   9706  C CZ2 . TRP F  2 145 ? 234.201 151.396 160.455 1.00 286.86 ? 179 TRP F CZ2 1 
ATOM   9707  C CZ3 . TRP F  2 145 ? 236.610 151.367 160.430 1.00 293.81 ? 179 TRP F CZ3 1 
ATOM   9708  C CH2 . TRP F  2 145 ? 235.388 151.895 160.004 1.00 291.49 ? 179 TRP F CH2 1 
ATOM   9709  N N   . ILE F  2 146 ? 239.054 146.450 162.319 1.00 298.19 ? 180 ILE F N   1 
ATOM   9710  C CA  . ILE F  2 146 ? 240.419 146.053 162.651 1.00 303.16 ? 180 ILE F CA  1 
ATOM   9711  C C   . ILE F  2 146 ? 241.308 147.283 162.538 1.00 307.01 ? 180 ILE F C   1 
ATOM   9712  O O   . ILE F  2 146 ? 241.109 148.110 161.643 1.00 307.63 ? 180 ILE F O   1 
ATOM   9713  C CB  . ILE F  2 146 ? 240.920 144.915 161.734 1.00 304.07 ? 180 ILE F CB  1 
ATOM   9714  C CG1 . ILE F  2 146 ? 242.430 144.706 161.884 1.00 307.00 ? 180 ILE F CG1 1 
ATOM   9715  C CG2 . ILE F  2 146 ? 240.558 145.198 160.284 1.00 305.09 ? 180 ILE F CG2 1 
ATOM   9716  C CD1 . ILE F  2 146 ? 242.862 144.275 163.271 1.00 310.99 ? 180 ILE F CD1 1 
ATOM   9717  N N   . ASN F  2 147 ? 242.243 147.425 163.489 1.00 309.71 ? 181 ASN F N   1 
ATOM   9718  C CA  . ASN F  2 147 ? 243.140 148.570 163.680 1.00 311.79 ? 181 ASN F CA  1 
ATOM   9719  C C   . ASN F  2 147 ? 242.435 149.865 163.285 1.00 310.77 ? 181 ASN F C   1 
ATOM   9720  O O   . ASN F  2 147 ? 242.999 150.729 162.606 1.00 312.65 ? 181 ASN F O   1 
ATOM   9721  C CB  . ASN F  2 147 ? 244.503 148.365 162.979 1.00 314.45 ? 181 ASN F CB  1 
ATOM   9722  C CG  . ASN F  2 147 ? 244.452 148.429 161.457 1.00 315.29 ? 181 ASN F CG  1 
ATOM   9723  O OD1 . ASN F  2 147 ? 243.406 148.568 160.849 1.00 314.29 ? 181 ASN F OD1 1 
ATOM   9724  N ND2 . ASN F  2 147 ? 245.622 148.320 160.838 1.00 317.33 ? 181 ASN F ND2 1 
ATOM   9725  N N   . ASN F  2 148 ? 241.198 149.992 163.768 1.00 307.31 ? 182 ASN F N   1 
ATOM   9726  C CA  . ASN F  2 148 ? 240.258 151.059 163.437 1.00 304.85 ? 182 ASN F CA  1 
ATOM   9727  C C   . ASN F  2 148 ? 240.273 151.383 161.940 1.00 304.81 ? 182 ASN F C   1 
ATOM   9728  O O   . ASN F  2 148 ? 240.520 152.523 161.537 1.00 303.72 ? 182 ASN F O   1 
ATOM   9729  C CB  . ASN F  2 148 ? 240.520 152.305 164.294 1.00 304.89 ? 182 ASN F CB  1 
ATOM   9730  C CG  . ASN F  2 148 ? 239.520 153.424 164.042 1.00 305.82 ? 182 ASN F CG  1 
ATOM   9731  O OD1 . ASN F  2 148 ? 238.539 153.240 163.321 1.00 304.72 ? 182 ASN F OD1 1 
ATOM   9732  N ND2 . ASN F  2 148 ? 239.759 154.581 164.678 1.00 306.99 ? 182 ASN F ND2 1 
ATOM   9733  N N   . GLN F  2 149 ? 240.049 150.366 161.109 1.00 304.60 ? 183 GLN F N   1 
ATOM   9734  C CA  . GLN F  2 149 ? 239.778 150.547 159.690 1.00 303.56 ? 183 GLN F CA  1 
ATOM   9735  C C   . GLN F  2 149 ? 239.018 149.317 159.213 1.00 302.90 ? 183 GLN F C   1 
ATOM   9736  O O   . GLN F  2 149 ? 239.224 148.208 159.711 1.00 302.86 ? 183 GLN F O   1 
ATOM   9737  C CB  . GLN F  2 149 ? 241.064 150.801 158.883 1.00 306.23 ? 183 GLN F CB  1 
ATOM   9738  C CG  . GLN F  2 149 ? 241.867 149.578 158.455 1.00 308.40 ? 183 GLN F CG  1 
ATOM   9739  C CD  . GLN F  2 149 ? 241.353 148.932 157.186 1.00 308.09 ? 183 GLN F CD  1 
ATOM   9740  O OE1 . GLN F  2 149 ? 240.999 149.616 156.226 1.00 306.62 ? 183 GLN F OE1 1 
ATOM   9741  N NE2 . GLN F  2 149 ? 241.315 147.604 157.172 1.00 310.52 ? 183 GLN F NE2 1 
ATOM   9742  N N   . SER F  2 150 ? 238.116 149.530 158.256 1.00 301.93 ? 184 SER F N   1 
ATOM   9743  C CA  . SER F  2 150 ? 237.196 148.474 157.853 1.00 303.29 ? 184 SER F CA  1 
ATOM   9744  C C   . SER F  2 150 ? 237.961 147.263 157.332 1.00 309.79 ? 184 SER F C   1 
ATOM   9745  O O   . SER F  2 150 ? 238.985 147.390 156.658 1.00 312.60 ? 184 SER F O   1 
ATOM   9746  C CB  . SER F  2 150 ? 236.227 148.987 156.787 1.00 302.22 ? 184 SER F CB  1 
ATOM   9747  O OG  . SER F  2 150 ? 236.925 149.465 155.651 1.00 300.80 ? 184 SER F OG  1 
ATOM   9748  N N   . LEU F  2 151 ? 237.446 146.079 157.652 1.00 310.42 ? 185 LEU F N   1 
ATOM   9749  C CA  . LEU F  2 151 ? 238.183 144.850 157.392 1.00 313.99 ? 185 LEU F CA  1 
ATOM   9750  C C   . LEU F  2 151 ? 238.477 144.713 155.900 1.00 318.63 ? 185 LEU F C   1 
ATOM   9751  O O   . LEU F  2 151 ? 237.569 144.877 155.073 1.00 319.38 ? 185 LEU F O   1 
ATOM   9752  C CB  . LEU F  2 151 ? 237.404 143.635 157.908 1.00 310.49 ? 185 LEU F CB  1 
ATOM   9753  C CG  . LEU F  2 151 ? 236.232 143.034 157.125 1.00 306.82 ? 185 LEU F CG  1 
ATOM   9754  C CD1 . LEU F  2 151 ? 235.847 141.682 157.703 1.00 305.70 ? 185 LEU F CD1 1 
ATOM   9755  C CD2 . LEU F  2 151 ? 235.032 143.970 157.116 1.00 301.65 ? 185 LEU F CD2 1 
ATOM   9756  N N   . PRO F  2 152 ? 239.728 144.456 155.516 1.00 321.46 ? 186 PRO F N   1 
ATOM   9757  C CA  . PRO F  2 152 ? 240.072 144.319 154.094 1.00 324.41 ? 186 PRO F CA  1 
ATOM   9758  C C   . PRO F  2 152 ? 239.596 142.980 153.556 1.00 327.82 ? 186 PRO F C   1 
ATOM   9759  O O   . PRO F  2 152 ? 240.012 141.918 154.030 1.00 328.24 ? 186 PRO F O   1 
ATOM   9760  C CB  . PRO F  2 152 ? 241.605 144.431 154.091 1.00 323.80 ? 186 PRO F CB  1 
ATOM   9761  C CG  . PRO F  2 152 ? 242.054 144.345 155.516 1.00 322.27 ? 186 PRO F CG  1 
ATOM   9762  C CD  . PRO F  2 152 ? 240.871 144.217 156.412 1.00 320.62 ? 186 PRO F CD  1 
ATOM   9763  N N   . VAL F  2 153 ? 238.713 143.029 152.555 1.00 330.37 ? 187 VAL F N   1 
ATOM   9764  C CA  . VAL F  2 153 ? 238.096 141.814 152.036 1.00 332.17 ? 187 VAL F CA  1 
ATOM   9765  C C   . VAL F  2 153 ? 239.165 140.889 151.477 1.00 335.00 ? 187 VAL F C   1 
ATOM   9766  O O   . VAL F  2 153 ? 240.008 141.296 150.667 1.00 335.21 ? 187 VAL F O   1 
ATOM   9767  C CB  . VAL F  2 153 ? 237.044 142.162 150.974 1.00 331.17 ? 187 VAL F CB  1 
ATOM   9768  C CG1 . VAL F  2 153 ? 236.356 140.900 150.476 1.00 330.22 ? 187 VAL F CG1 1 
ATOM   9769  C CG2 . VAL F  2 153 ? 236.028 143.142 151.539 1.00 329.90 ? 187 VAL F CG2 1 
ATOM   9770  N N   . SER F  2 154 ? 239.131 139.631 151.912 1.00 336.77 ? 188 SER F N   1 
ATOM   9771  C CA  . SER F  2 154 ? 240.109 138.630 151.514 1.00 340.33 ? 188 SER F CA  1 
ATOM   9772  C C   . SER F  2 154 ? 239.561 137.262 151.881 1.00 344.28 ? 188 SER F C   1 
ATOM   9773  O O   . SER F  2 154 ? 238.806 137.146 152.853 1.00 344.29 ? 188 SER F O   1 
ATOM   9774  C CB  . SER F  2 154 ? 241.460 138.873 152.206 1.00 340.44 ? 188 SER F CB  1 
ATOM   9775  O OG  . SER F  2 154 ? 242.339 137.776 152.033 1.00 343.17 ? 188 SER F OG  1 
ATOM   9776  N N   . PRO F  2 155 ? 239.908 136.213 151.129 1.00 346.10 ? 189 PRO F N   1 
ATOM   9777  C CA  . PRO F  2 155 ? 239.523 134.857 151.556 1.00 346.55 ? 189 PRO F CA  1 
ATOM   9778  C C   . PRO F  2 155 ? 240.122 134.483 152.896 1.00 346.35 ? 189 PRO F C   1 
ATOM   9779  O O   . PRO F  2 155 ? 239.616 133.578 153.572 1.00 345.25 ? 189 PRO F O   1 
ATOM   9780  C CB  . PRO F  2 155 ? 240.057 133.971 150.422 1.00 345.34 ? 189 PRO F CB  1 
ATOM   9781  C CG  . PRO F  2 155 ? 241.171 134.779 149.821 1.00 344.68 ? 189 PRO F CG  1 
ATOM   9782  C CD  . PRO F  2 155 ? 240.664 136.190 149.866 1.00 345.15 ? 189 PRO F CD  1 
ATOM   9783  N N   . ARG F  2 156 ? 241.203 135.160 153.286 1.00 347.05 ? 190 ARG F N   1 
ATOM   9784  C CA  . ARG F  2 156 ? 241.780 135.022 154.615 1.00 346.86 ? 190 ARG F CA  1 
ATOM   9785  C C   . ARG F  2 156 ? 240.750 135.295 155.707 1.00 347.04 ? 190 ARG F C   1 
ATOM   9786  O O   . ARG F  2 156 ? 240.742 134.599 156.728 1.00 348.41 ? 190 ARG F O   1 
ATOM   9787  C CB  . ARG F  2 156 ? 242.959 135.995 154.721 1.00 347.20 ? 190 ARG F CB  1 
ATOM   9788  C CG  . ARG F  2 156 ? 243.588 136.229 156.085 1.00 348.82 ? 190 ARG F CG  1 
ATOM   9789  C CD  . ARG F  2 156 ? 243.710 134.999 156.965 1.00 353.33 ? 190 ARG F CD  1 
ATOM   9790  N NE  . ARG F  2 156 ? 244.478 135.340 158.153 1.00 356.24 ? 190 ARG F NE  1 
ATOM   9791  C CZ  . ARG F  2 156 ? 245.787 135.545 158.164 1.00 357.11 ? 190 ARG F CZ  1 
ATOM   9792  N NH1 . ARG F  2 156 ? 246.524 135.375 157.079 1.00 355.93 ? 190 ARG F NH1 1 
ATOM   9793  N NH2 . ARG F  2 156 ? 246.372 135.937 159.292 1.00 358.16 ? 190 ARG F NH2 1 
ATOM   9794  N N   . LEU F  2 157 ? 239.862 136.269 155.505 1.00 345.12 ? 191 LEU F N   1 
ATOM   9795  C CA  . LEU F  2 157 ? 238.866 136.633 156.513 1.00 342.98 ? 191 LEU F CA  1 
ATOM   9796  C C   . LEU F  2 157 ? 237.602 135.815 156.268 1.00 341.38 ? 191 LEU F C   1 
ATOM   9797  O O   . LEU F  2 157 ? 236.696 136.210 155.534 1.00 338.31 ? 191 LEU F O   1 
ATOM   9798  C CB  . LEU F  2 157 ? 238.586 138.133 156.483 1.00 339.29 ? 191 LEU F CB  1 
ATOM   9799  C CG  . LEU F  2 157 ? 239.782 139.081 156.584 1.00 336.83 ? 191 LEU F CG  1 
ATOM   9800  C CD1 . LEU F  2 157 ? 239.303 140.508 156.786 1.00 327.65 ? 191 LEU F CD1 1 
ATOM   9801  C CD2 . LEU F  2 157 ? 240.705 138.663 157.715 1.00 339.68 ? 191 LEU F CD2 1 
ATOM   9802  N N   . GLN F  2 158 ? 237.552 134.650 156.906 1.00 341.89 ? 192 GLN F N   1 
ATOM   9803  C CA  . GLN F  2 158 ? 236.390 133.780 156.817 1.00 338.58 ? 192 GLN F CA  1 
ATOM   9804  C C   . GLN F  2 158 ? 235.265 134.304 157.702 1.00 334.07 ? 192 GLN F C   1 
ATOM   9805  O O   . GLN F  2 158 ? 235.500 134.884 158.767 1.00 333.86 ? 192 GLN F O   1 
ATOM   9806  C CB  . GLN F  2 158 ? 236.762 132.351 157.219 1.00 340.45 ? 192 GLN F CB  1 
ATOM   9807  C CG  . GLN F  2 158 ? 235.656 131.319 157.030 1.00 337.75 ? 192 GLN F CG  1 
ATOM   9808  C CD  . GLN F  2 158 ? 234.959 130.948 158.328 1.00 336.21 ? 192 GLN F CD  1 
ATOM   9809  O OE1 . GLN F  2 158 ? 234.559 131.814 159.105 1.00 335.93 ? 192 GLN F OE1 1 
ATOM   9810  N NE2 . GLN F  2 158 ? 234.814 129.650 158.568 1.00 336.07 ? 192 GLN F NE2 1 
ATOM   9811  N N   . LEU F  2 159 ? 234.031 134.095 157.249 1.00 329.93 ? 193 LEU F N   1 
ATOM   9812  C CA  . LEU F  2 159 ? 232.845 134.497 157.989 1.00 323.17 ? 193 LEU F CA  1 
ATOM   9813  C C   . LEU F  2 159 ? 231.887 133.317 158.099 1.00 322.10 ? 193 LEU F C   1 
ATOM   9814  O O   . LEU F  2 159 ? 231.671 132.581 157.133 1.00 323.97 ? 193 LEU F O   1 
ATOM   9815  C CB  . LEU F  2 159 ? 232.154 135.693 157.320 1.00 316.67 ? 193 LEU F CB  1 
ATOM   9816  C CG  . LEU F  2 159 ? 232.986 136.979 157.287 1.00 314.97 ? 193 LEU F CG  1 
ATOM   9817  C CD1 . LEU F  2 159 ? 232.458 137.945 156.236 1.00 308.93 ? 193 LEU F CD1 1 
ATOM   9818  C CD2 . LEU F  2 159 ? 233.033 137.638 158.661 1.00 310.36 ? 193 LEU F CD2 1 
ATOM   9819  N N   . SER F  2 160 ? 231.312 133.147 159.289 1.00 317.81 ? 194 SER F N   1 
ATOM   9820  C CA  . SER F  2 160 ? 230.435 132.018 159.571 1.00 314.96 ? 194 SER F CA  1 
ATOM   9821  C C   . SER F  2 160 ? 229.221 132.515 160.345 1.00 308.58 ? 194 SER F C   1 
ATOM   9822  O O   . SER F  2 160 ? 229.242 133.593 160.945 1.00 306.02 ? 194 SER F O   1 
ATOM   9823  C CB  . SER F  2 160 ? 231.173 130.919 160.344 1.00 317.83 ? 194 SER F CB  1 
ATOM   9824  O OG  . SER F  2 160 ? 230.604 129.647 160.088 1.00 318.91 ? 194 SER F OG  1 
ATOM   9825  N N   . ASN F  2 161 ? 228.158 131.709 160.326 1.00 306.23 ? 195 ASN F N   1 
ATOM   9826  C CA  . ASN F  2 161 ? 226.856 132.085 160.881 1.00 302.92 ? 195 ASN F CA  1 
ATOM   9827  C C   . ASN F  2 161 ? 226.426 133.423 160.280 1.00 301.13 ? 195 ASN F C   1 
ATOM   9828  O O   . ASN F  2 161 ? 226.276 134.437 160.965 1.00 297.48 ? 195 ASN F O   1 
ATOM   9829  C CB  . ASN F  2 161 ? 226.901 132.134 162.415 1.00 300.28 ? 195 ASN F CB  1 
ATOM   9830  C CG  . ASN F  2 161 ? 225.520 132.286 163.053 1.00 295.10 ? 195 ASN F CG  1 
ATOM   9831  O OD1 . ASN F  2 161 ? 224.705 133.117 162.650 1.00 293.16 ? 195 ASN F OD1 1 
ATOM   9832  N ND2 . ASN F  2 161 ? 225.265 131.478 164.074 1.00 292.98 ? 195 ASN F ND2 1 
ATOM   9833  N N   . GLY F  2 162 ? 226.265 133.410 158.960 1.00 302.50 ? 196 GLY F N   1 
ATOM   9834  C CA  . GLY F  2 162 ? 226.204 134.656 158.229 1.00 301.80 ? 196 GLY F CA  1 
ATOM   9835  C C   . GLY F  2 162 ? 227.575 135.293 158.304 1.00 303.08 ? 196 GLY F C   1 
ATOM   9836  O O   . GLY F  2 162 ? 228.539 134.746 157.766 1.00 306.29 ? 196 GLY F O   1 
ATOM   9837  N N   . ASN F  2 163 ? 227.688 136.434 158.971 1.00 300.34 ? 197 ASN F N   1 
ATOM   9838  C CA  . ASN F  2 163 ? 228.987 137.009 159.296 1.00 301.20 ? 197 ASN F CA  1 
ATOM   9839  C C   . ASN F  2 163 ? 229.000 137.608 160.697 1.00 296.13 ? 197 ASN F C   1 
ATOM   9840  O O   . ASN F  2 163 ? 229.358 138.775 160.883 1.00 292.06 ? 197 ASN F O   1 
ATOM   9841  C CB  . ASN F  2 163 ? 229.441 137.970 158.187 1.00 300.65 ? 197 ASN F CB  1 
ATOM   9842  C CG  . ASN F  2 163 ? 228.297 138.758 157.559 1.00 297.88 ? 197 ASN F CG  1 
ATOM   9843  O OD1 . ASN F  2 163 ? 227.304 138.164 157.155 1.00 297.12 ? 197 ASN F OD1 1 
ATOM   9844  N ND2 . ASN F  2 163 ? 228.462 140.066 157.412 1.00 295.64 ? 197 ASN F ND2 1 
ATOM   9845  N N   . ARG F  2 164 ? 228.576 136.807 161.684 1.00 295.63 ? 198 ARG F N   1 
ATOM   9846  C CA  . ARG F  2 164 ? 228.810 137.103 163.092 1.00 294.35 ? 198 ARG F CA  1 
ATOM   9847  C C   . ARG F  2 164 ? 230.037 136.388 163.635 1.00 301.23 ? 198 ARG F C   1 
ATOM   9848  O O   . ARG F  2 164 ? 230.537 136.766 164.700 1.00 301.30 ? 198 ARG F O   1 
ATOM   9849  C CB  . ARG F  2 164 ? 227.602 136.706 163.936 1.00 289.01 ? 198 ARG F CB  1 
ATOM   9850  C CG  . ARG F  2 164 ? 227.407 135.215 164.163 1.00 288.83 ? 198 ARG F CG  1 
ATOM   9851  C CD  . ARG F  2 164 ? 226.684 135.013 165.483 1.00 283.89 ? 198 ARG F CD  1 
ATOM   9852  N NE  . ARG F  2 164 ? 225.729 136.097 165.679 1.00 277.50 ? 198 ARG F NE  1 
ATOM   9853  C CZ  . ARG F  2 164 ? 225.536 136.748 166.818 1.00 273.61 ? 198 ARG F CZ  1 
ATOM   9854  N NH1 . ARG F  2 164 ? 226.116 136.363 167.944 1.00 275.46 ? 198 ARG F NH1 1 
ATOM   9855  N NH2 . ARG F  2 164 ? 224.747 137.818 166.827 1.00 269.75 ? 198 ARG F NH2 1 
ATOM   9856  N N   . THR F  2 165 ? 230.508 135.353 162.950 1.00 304.29 ? 199 THR F N   1 
ATOM   9857  C CA  . THR F  2 165 ? 231.695 134.612 163.352 1.00 308.25 ? 199 THR F CA  1 
ATOM   9858  C C   . THR F  2 165 ? 232.815 134.901 162.364 1.00 313.89 ? 199 THR F C   1 
ATOM   9859  O O   . THR F  2 165 ? 232.704 134.569 161.179 1.00 316.52 ? 199 THR F O   1 
ATOM   9860  C CB  . THR F  2 165 ? 231.421 133.105 163.411 1.00 307.40 ? 199 THR F CB  1 
ATOM   9861  O OG1 . THR F  2 165 ? 230.529 132.812 164.495 1.00 303.02 ? 199 THR F OG1 1 
ATOM   9862  C CG2 . THR F  2 165 ? 232.722 132.332 163.610 1.00 312.73 ? 199 THR F CG2 1 
ATOM   9863  N N   . LEU F  2 166 ? 233.892 135.512 162.850 1.00 316.14 ? 200 LEU F N   1 
ATOM   9864  C CA  . LEU F  2 166 ? 235.038 135.861 162.020 1.00 320.73 ? 200 LEU F CA  1 
ATOM   9865  C C   . LEU F  2 166 ? 236.178 134.914 162.361 1.00 328.98 ? 200 LEU F C   1 
ATOM   9866  O O   . LEU F  2 166 ? 236.665 134.909 163.496 1.00 329.04 ? 200 LEU F O   1 
ATOM   9867  C CB  . LEU F  2 166 ? 235.445 137.324 162.231 1.00 314.35 ? 200 LEU F CB  1 
ATOM   9868  C CG  . LEU F  2 166 ? 236.794 137.844 161.722 1.00 314.68 ? 200 LEU F CG  1 
ATOM   9869  C CD1 . LEU F  2 166 ? 236.647 139.291 161.282 1.00 304.67 ? 200 LEU F CD1 1 
ATOM   9870  C CD2 . LEU F  2 166 ? 237.885 137.739 162.781 1.00 317.67 ? 200 LEU F CD2 1 
ATOM   9871  N N   . THR F  2 167 ? 236.594 134.112 161.385 1.00 335.87 ? 201 THR F N   1 
ATOM   9872  C CA  . THR F  2 167 ? 237.644 133.118 161.571 1.00 341.70 ? 201 THR F CA  1 
ATOM   9873  C C   . THR F  2 167 ? 238.887 133.575 160.823 1.00 346.79 ? 201 THR F C   1 
ATOM   9874  O O   . THR F  2 167 ? 238.822 133.865 159.624 1.00 346.89 ? 201 THR F O   1 
ATOM   9875  C CB  . THR F  2 167 ? 237.192 131.741 161.081 1.00 343.12 ? 201 THR F CB  1 
ATOM   9876  O OG1 . THR F  2 167 ? 235.901 131.439 161.625 1.00 338.43 ? 201 THR F OG1 1 
ATOM   9877  C CG2 . THR F  2 167 ? 238.180 130.668 161.516 1.00 346.66 ? 201 THR F CG2 1 
ATOM   9878  N N   . LEU F  2 168 ? 240.012 133.634 161.530 1.00 351.43 ? 202 LEU F N   1 
ATOM   9879  C CA  . LEU F  2 168 ? 241.276 134.084 160.958 1.00 354.72 ? 202 LEU F CA  1 
ATOM   9880  C C   . LEU F  2 168 ? 242.078 132.843 160.576 1.00 357.90 ? 202 LEU F C   1 
ATOM   9881  O O   . LEU F  2 168 ? 242.579 132.131 161.450 1.00 360.79 ? 202 LEU F O   1 
ATOM   9882  C CB  . LEU F  2 168 ? 242.030 134.950 161.963 1.00 354.67 ? 202 LEU F CB  1 
ATOM   9883  C CG  . LEU F  2 168 ? 243.060 135.945 161.431 1.00 354.30 ? 202 LEU F CG  1 
ATOM   9884  C CD1 . LEU F  2 168 ? 242.502 136.653 160.210 1.00 352.71 ? 202 LEU F CD1 1 
ATOM   9885  C CD2 . LEU F  2 168 ? 243.440 136.946 162.507 1.00 349.32 ? 202 LEU F CD2 1 
ATOM   9886  N N   . LEU F  2 169 ? 242.210 132.590 159.269 1.00 357.70 ? 203 LEU F N   1 
ATOM   9887  C CA  . LEU F  2 169 ? 242.657 131.277 158.804 1.00 358.29 ? 203 LEU F CA  1 
ATOM   9888  C C   . LEU F  2 169 ? 244.087 130.961 159.234 1.00 361.51 ? 203 LEU F C   1 
ATOM   9889  O O   . LEU F  2 169 ? 244.356 129.866 159.743 1.00 362.32 ? 203 LEU F O   1 
ATOM   9890  C CB  . LEU F  2 169 ? 242.521 131.182 157.284 1.00 355.18 ? 203 LEU F CB  1 
ATOM   9891  C CG  . LEU F  2 169 ? 241.130 131.457 156.706 1.00 350.35 ? 203 LEU F CG  1 
ATOM   9892  C CD1 . LEU F  2 169 ? 241.074 131.107 155.226 1.00 345.90 ? 203 LEU F CD1 1 
ATOM   9893  C CD2 . LEU F  2 169 ? 240.065 130.691 157.478 1.00 349.09 ? 203 LEU F CD2 1 
ATOM   9894  N N   . SER F  2 170 ? 245.021 131.891 159.037 1.00 362.34 ? 204 SER F N   1 
ATOM   9895  C CA  . SER F  2 170 ? 246.431 131.632 159.329 1.00 363.35 ? 204 SER F CA  1 
ATOM   9896  C C   . SER F  2 170 ? 247.048 132.885 159.934 1.00 363.91 ? 204 SER F C   1 
ATOM   9897  O O   . SER F  2 170 ? 247.659 133.683 159.216 1.00 363.35 ? 204 SER F O   1 
ATOM   9898  C CB  . SER F  2 170 ? 247.185 131.213 158.066 1.00 363.06 ? 204 SER F CB  1 
ATOM   9899  O OG  . SER F  2 170 ? 246.878 129.878 157.703 1.00 362.44 ? 204 SER F OG  1 
ATOM   9900  N N   . VAL F  2 171 ? 246.945 133.027 161.254 1.00 364.65 ? 205 VAL F N   1 
ATOM   9901  C CA  . VAL F  2 171 ? 247.305 134.275 161.918 1.00 362.59 ? 205 VAL F CA  1 
ATOM   9902  C C   . VAL F  2 171 ? 248.810 134.496 161.852 1.00 361.34 ? 205 VAL F C   1 
ATOM   9903  O O   . VAL F  2 171 ? 249.603 133.555 161.729 1.00 362.01 ? 205 VAL F O   1 
ATOM   9904  C CB  . VAL F  2 171 ? 246.805 134.285 163.377 1.00 361.73 ? 205 VAL F CB  1 
ATOM   9905  C CG1 . VAL F  2 171 ? 245.369 133.790 163.453 1.00 361.54 ? 205 VAL F CG1 1 
ATOM   9906  C CG2 . VAL F  2 171 ? 247.719 133.459 164.264 1.00 361.65 ? 205 VAL F CG2 1 
ATOM   9907  N N   . THR F  2 172 ? 249.201 135.767 161.923 1.00 358.83 ? 206 THR F N   1 
ATOM   9908  C CA  . THR F  2 172 ? 250.597 136.174 161.961 1.00 356.03 ? 206 THR F CA  1 
ATOM   9909  C C   . THR F  2 172 ? 250.771 137.215 163.056 1.00 353.33 ? 206 THR F C   1 
ATOM   9910  O O   . THR F  2 172 ? 249.803 137.842 163.495 1.00 352.90 ? 206 THR F O   1 
ATOM   9911  C CB  . THR F  2 172 ? 251.074 136.757 160.620 1.00 354.76 ? 206 THR F CB  1 
ATOM   9912  O OG1 . THR F  2 172 ? 250.347 137.959 160.333 1.00 353.52 ? 206 THR F OG1 1 
ATOM   9913  C CG2 . THR F  2 172 ? 250.872 135.759 159.489 1.00 355.74 ? 206 THR F CG2 1 
ATOM   9914  N N   . ARG F  2 173 ? 252.019 137.394 163.497 1.00 350.74 ? 207 ARG F N   1 
ATOM   9915  C CA  . ARG F  2 173 ? 252.294 138.383 164.535 1.00 346.93 ? 207 ARG F CA  1 
ATOM   9916  C C   . ARG F  2 173 ? 252.030 139.801 164.045 1.00 348.49 ? 207 ARG F C   1 
ATOM   9917  O O   . ARG F  2 173 ? 251.808 140.706 164.857 1.00 347.74 ? 207 ARG F O   1 
ATOM   9918  C CB  . ARG F  2 173 ? 253.736 138.245 165.024 1.00 341.22 ? 207 ARG F CB  1 
ATOM   9919  C CG  . ARG F  2 173 ? 254.779 138.291 163.922 1.00 338.04 ? 207 ARG F CG  1 
ATOM   9920  C CD  . ARG F  2 173 ? 256.174 138.456 164.502 1.00 331.19 ? 207 ARG F CD  1 
ATOM   9921  N NE  . ARG F  2 173 ? 256.403 137.551 165.622 1.00 327.00 ? 207 ARG F NE  1 
ATOM   9922  C CZ  . ARG F  2 173 ? 257.459 137.599 166.422 1.00 323.39 ? 207 ARG F CZ  1 
ATOM   9923  N NH1 . ARG F  2 173 ? 258.414 138.499 166.253 1.00 321.49 ? 207 ARG F NH1 1 
ATOM   9924  N NH2 . ARG F  2 173 ? 257.561 136.722 167.417 1.00 323.34 ? 207 ARG F NH2 1 
ATOM   9925  N N   . ASN F  2 174 ? 252.048 140.014 162.727 1.00 349.35 ? 208 ASN F N   1 
ATOM   9926  C CA  . ASN F  2 174 ? 251.753 141.327 162.167 1.00 348.52 ? 208 ASN F CA  1 
ATOM   9927  C C   . ASN F  2 174 ? 250.267 141.661 162.190 1.00 348.71 ? 208 ASN F C   1 
ATOM   9928  O O   . ASN F  2 174 ? 249.905 142.808 161.909 1.00 348.00 ? 208 ASN F O   1 
ATOM   9929  C CB  . ASN F  2 174 ? 252.279 141.416 160.734 1.00 347.01 ? 208 ASN F CB  1 
ATOM   9930  C CG  . ASN F  2 174 ? 253.695 141.954 160.665 1.00 344.44 ? 208 ASN F CG  1 
ATOM   9931  O OD1 . ASN F  2 174 ? 254.247 142.411 161.665 1.00 344.89 ? 208 ASN F OD1 1 
ATOM   9932  N ND2 . ASN F  2 174 ? 254.290 141.901 159.479 1.00 340.92 ? 208 ASN F ND2 1 
ATOM   9933  N N   . ASP F  2 175 ? 249.406 140.697 162.512 1.00 349.50 ? 209 ASP F N   1 
ATOM   9934  C CA  . ASP F  2 175 ? 247.968 140.929 162.568 1.00 348.00 ? 209 ASP F CA  1 
ATOM   9935  C C   . ASP F  2 175 ? 247.512 141.513 163.898 1.00 344.49 ? 209 ASP F C   1 
ATOM   9936  O O   . ASP F  2 175 ? 246.312 141.756 164.067 1.00 340.26 ? 209 ASP F O   1 
ATOM   9937  C CB  . ASP F  2 175 ? 247.213 139.624 162.297 1.00 348.69 ? 209 ASP F CB  1 
ATOM   9938  C CG  . ASP F  2 175 ? 247.435 139.101 160.892 1.00 351.77 ? 209 ASP F CG  1 
ATOM   9939  O OD1 . ASP F  2 175 ? 247.007 139.774 159.931 1.00 351.41 ? 209 ASP F OD1 1 
ATOM   9940  O OD2 . ASP F  2 175 ? 248.034 138.015 160.748 1.00 353.94 ? 209 ASP F OD2 1 
ATOM   9941  N N   . THR F  2 176 ? 248.428 141.734 164.838 1.00 344.67 ? 210 THR F N   1 
ATOM   9942  C CA  . THR F  2 176 ? 248.058 142.245 166.151 1.00 340.18 ? 210 THR F CA  1 
ATOM   9943  C C   . THR F  2 176 ? 247.450 143.638 166.040 1.00 337.44 ? 210 THR F C   1 
ATOM   9944  O O   . THR F  2 176 ? 247.972 144.505 165.332 1.00 339.86 ? 210 THR F O   1 
ATOM   9945  C CB  . THR F  2 176 ? 249.282 142.277 167.067 1.00 340.83 ? 210 THR F CB  1 
ATOM   9946  O OG1 . THR F  2 176 ? 249.905 140.987 167.076 1.00 341.09 ? 210 THR F OG1 1 
ATOM   9947  C CG2 . THR F  2 176 ? 248.879 142.648 168.487 1.00 337.00 ? 210 THR F CG2 1 
ATOM   9948  N N   . GLY F  2 177 ? 246.340 143.847 166.744 1.00 331.63 ? 211 GLY F N   1 
ATOM   9949  C CA  . GLY F  2 177 ? 245.674 145.126 166.763 1.00 326.93 ? 211 GLY F CA  1 
ATOM   9950  C C   . GLY F  2 177 ? 244.393 145.082 167.571 1.00 322.16 ? 211 GLY F C   1 
ATOM   9951  O O   . GLY F  2 177 ? 244.096 144.099 168.255 1.00 321.61 ? 211 GLY F O   1 
ATOM   9952  N N   . PRO F  2 178 ? 243.612 146.162 167.517 1.00 319.64 ? 212 PRO F N   1 
ATOM   9953  C CA  . PRO F  2 178 ? 242.302 146.162 168.181 1.00 316.88 ? 212 PRO F CA  1 
ATOM   9954  C C   . PRO F  2 178 ? 241.232 145.562 167.278 1.00 313.58 ? 212 PRO F C   1 
ATOM   9955  O O   . PRO F  2 178 ? 241.103 145.934 166.109 1.00 311.40 ? 212 PRO F O   1 
ATOM   9956  C CB  . PRO F  2 178 ? 242.040 147.647 168.454 1.00 315.15 ? 212 PRO F CB  1 
ATOM   9957  C CG  . PRO F  2 178 ? 242.854 148.382 167.431 1.00 314.37 ? 212 PRO F CG  1 
ATOM   9958  C CD  . PRO F  2 178 ? 243.924 147.459 166.895 1.00 316.97 ? 212 PRO F CD  1 
ATOM   9959  N N   . TYR F  2 179 ? 240.467 144.626 167.830 1.00 311.40 ? 213 TYR F N   1 
ATOM   9960  C CA  . TYR F  2 179 ? 239.361 143.978 167.135 1.00 306.87 ? 213 TYR F CA  1 
ATOM   9961  C C   . TYR F  2 179 ? 238.061 144.381 167.814 1.00 301.92 ? 213 TYR F C   1 
ATOM   9962  O O   . TYR F  2 179 ? 237.924 144.249 169.035 1.00 301.55 ? 213 TYR F O   1 
ATOM   9963  C CB  . TYR F  2 179 ? 239.534 142.460 167.121 1.00 307.25 ? 213 TYR F CB  1 
ATOM   9964  C CG  . TYR F  2 179 ? 240.818 142.018 166.461 1.00 309.86 ? 213 TYR F CG  1 
ATOM   9965  C CD1 . TYR F  2 179 ? 242.020 142.028 167.152 1.00 313.23 ? 213 TYR F CD1 1 
ATOM   9966  C CD2 . TYR F  2 179 ? 240.825 141.578 165.144 1.00 309.91 ? 213 TYR F CD2 1 
ATOM   9967  C CE1 . TYR F  2 179 ? 243.192 141.634 166.547 1.00 316.61 ? 213 TYR F CE1 1 
ATOM   9968  C CE2 . TYR F  2 179 ? 241.992 141.169 164.534 1.00 313.62 ? 213 TYR F CE2 1 
ATOM   9969  C CZ  . TYR F  2 179 ? 243.174 141.199 165.241 1.00 317.67 ? 213 TYR F CZ  1 
ATOM   9970  O OH  . TYR F  2 179 ? 244.343 140.795 164.640 1.00 325.14 ? 213 TYR F OH  1 
ATOM   9971  N N   . GLU F  2 180 ? 237.112 144.865 167.018 1.00 295.43 ? 214 GLU F N   1 
ATOM   9972  C CA  . GLU F  2 180 ? 235.938 145.548 167.533 1.00 288.85 ? 214 GLU F CA  1 
ATOM   9973  C C   . GLU F  2 180 ? 234.743 145.211 166.654 1.00 282.68 ? 214 GLU F C   1 
ATOM   9974  O O   . GLU F  2 180 ? 234.852 145.160 165.426 1.00 281.28 ? 214 GLU F O   1 
ATOM   9975  C CB  . GLU F  2 180 ? 236.199 147.059 167.584 1.00 290.13 ? 214 GLU F CB  1 
ATOM   9976  C CG  . GLU F  2 180 ? 235.065 147.910 168.092 1.00 285.86 ? 214 GLU F CG  1 
ATOM   9977  C CD  . GLU F  2 180 ? 235.509 149.336 168.363 1.00 288.88 ? 214 GLU F CD  1 
ATOM   9978  O OE1 . GLU F  2 180 ? 236.378 149.530 169.239 1.00 293.05 ? 214 GLU F OE1 1 
ATOM   9979  O OE2 . GLU F  2 180 ? 235.009 150.262 167.691 1.00 286.07 ? 214 GLU F OE2 1 
ATOM   9980  N N   . CYS F  2 181 ? 233.598 144.981 167.294 1.00 279.49 ? 215 CYS F N   1 
ATOM   9981  C CA  . CYS F  2 181 ? 232.411 144.469 166.625 1.00 276.67 ? 215 CYS F CA  1 
ATOM   9982  C C   . CYS F  2 181 ? 231.286 145.493 166.697 1.00 269.70 ? 215 CYS F C   1 
ATOM   9983  O O   . CYS F  2 181 ? 231.095 146.151 167.724 1.00 268.04 ? 215 CYS F O   1 
ATOM   9984  C CB  . CYS F  2 181 ? 231.963 143.142 167.253 1.00 280.67 ? 215 CYS F CB  1 
ATOM   9985  S SG  . CYS F  2 181 ? 230.481 142.413 166.522 1.00 285.70 ? 215 CYS F SG  1 
ATOM   9986  N N   . GLU F  2 182 ? 230.545 145.621 165.597 1.00 266.14 ? 216 GLU F N   1 
ATOM   9987  C CA  . GLU F  2 182 ? 229.474 146.597 165.471 1.00 260.82 ? 216 GLU F CA  1 
ATOM   9988  C C   . GLU F  2 182 ? 228.169 145.897 165.119 1.00 254.24 ? 216 GLU F C   1 
ATOM   9989  O O   . GLU F  2 182 ? 228.077 145.190 164.112 1.00 254.74 ? 216 GLU F O   1 
ATOM   9990  C CB  . GLU F  2 182 ? 229.813 147.650 164.400 1.00 263.45 ? 216 GLU F CB  1 
ATOM   9991  C CG  . GLU F  2 182 ? 228.772 148.749 164.175 1.00 257.03 ? 216 GLU F CG  1 
ATOM   9992  C CD  . GLU F  2 182 ? 228.013 149.153 165.427 1.00 249.17 ? 216 GLU F CD  1 
ATOM   9993  O OE1 . GLU F  2 182 ? 226.769 149.198 165.370 1.00 240.41 ? 216 GLU F OE1 1 
ATOM   9994  O OE2 . GLU F  2 182 ? 228.650 149.444 166.459 1.00 252.31 ? 216 GLU F OE2 1 
ATOM   9995  N N   . ILE F  2 183 ? 227.160 146.103 165.961 1.00 247.03 ? 217 ILE F N   1 
ATOM   9996  C CA  . ILE F  2 183 ? 225.812 145.592 165.736 1.00 238.01 ? 217 ILE F CA  1 
ATOM   9997  C C   . ILE F  2 183 ? 224.913 146.785 165.443 1.00 232.64 ? 217 ILE F C   1 
ATOM   9998  O O   . ILE F  2 183 ? 224.749 147.669 166.293 1.00 232.28 ? 217 ILE F O   1 
ATOM   9999  C CB  . ILE F  2 183 ? 225.293 144.779 166.940 1.00 236.64 ? 217 ILE F CB  1 
ATOM   10000 C CG1 . ILE F  2 183 ? 225.641 143.290 166.817 1.00 245.03 ? 217 ILE F CG1 1 
ATOM   10001 C CG2 . ILE F  2 183 ? 223.789 144.894 167.070 1.00 227.54 ? 217 ILE F CG2 1 
ATOM   10002 C CD1 . ILE F  2 183 ? 227.043 142.980 166.373 1.00 254.66 ? 217 ILE F CD1 1 
ATOM   10003 N N   . GLN F  2 184 ? 224.354 146.824 164.235 1.00 225.90 ? 218 GLN F N   1 
ATOM   10004 C CA  . GLN F  2 184 ? 223.574 147.972 163.793 1.00 215.23 ? 218 GLN F CA  1 
ATOM   10005 C C   . GLN F  2 184 ? 222.232 147.513 163.245 1.00 206.45 ? 218 GLN F C   1 
ATOM   10006 O O   . GLN F  2 184 ? 222.132 146.436 162.648 1.00 210.54 ? 218 GLN F O   1 
ATOM   10007 C CB  . GLN F  2 184 ? 224.336 148.784 162.735 1.00 215.37 ? 218 GLN F CB  1 
ATOM   10008 C CG  . GLN F  2 184 ? 224.274 148.231 161.323 1.00 219.18 ? 218 GLN F CG  1 
ATOM   10009 C CD  . GLN F  2 184 ? 224.823 149.201 160.296 1.00 226.36 ? 218 GLN F CD  1 
ATOM   10010 O OE1 . GLN F  2 184 ? 226.037 149.355 160.158 1.00 232.80 ? 218 GLN F OE1 1 
ATOM   10011 N NE2 . GLN F  2 184 ? 223.930 149.861 159.568 1.00 228.68 ? 218 GLN F NE2 1 
ATOM   10012 N N   . ASN F  2 185 ? 221.209 148.321 163.471 1.00 193.44 ? 219 ASN F N   1 
ATOM   10013 C CA  . ASN F  2 185 ? 219.875 148.140 162.932 1.00 182.46 ? 219 ASN F CA  1 
ATOM   10014 C C   . ASN F  2 185 ? 219.417 149.423 162.243 1.00 172.15 ? 219 ASN F C   1 
ATOM   10015 O O   . ASN F  2 185 ? 220.093 150.455 162.316 1.00 175.11 ? 219 ASN F O   1 
ATOM   10016 C CB  . ASN F  2 185 ? 218.902 147.722 164.050 1.00 183.43 ? 219 ASN F CB  1 
ATOM   10017 C CG  . ASN F  2 185 ? 218.714 148.788 165.123 1.00 183.43 ? 219 ASN F CG  1 
ATOM   10018 O OD1 . ASN F  2 185 ? 219.004 149.964 164.924 1.00 183.77 ? 219 ASN F OD1 1 
ATOM   10019 N ND2 . ASN F  2 185 ? 218.215 148.365 166.279 1.00 182.01 ? 219 ASN F ND2 1 
ATOM   10020 N N   . PRO F  2 186 ? 218.278 149.392 161.542 1.00 165.94 ? 220 PRO F N   1 
ATOM   10021 C CA  . PRO F  2 186 ? 217.790 150.617 160.887 1.00 165.17 ? 220 PRO F CA  1 
ATOM   10022 C C   . PRO F  2 186 ? 217.616 151.818 161.810 1.00 163.15 ? 220 PRO F C   1 
ATOM   10023 O O   . PRO F  2 186 ? 217.529 152.943 161.301 1.00 161.98 ? 220 PRO F O   1 
ATOM   10024 C CB  . PRO F  2 186 ? 216.445 150.178 160.298 1.00 155.48 ? 220 PRO F CB  1 
ATOM   10025 C CG  . PRO F  2 186 ? 216.662 148.753 159.965 1.00 154.28 ? 220 PRO F CG  1 
ATOM   10026 C CD  . PRO F  2 186 ? 217.550 148.203 161.057 1.00 160.51 ? 220 PRO F CD  1 
ATOM   10027 N N   . VAL F  2 187 ? 217.559 151.637 163.130 1.00 164.94 ? 221 VAL F N   1 
ATOM   10028 C CA  . VAL F  2 187 ? 217.204 152.749 164.007 1.00 164.58 ? 221 VAL F CA  1 
ATOM   10029 C C   . VAL F  2 187 ? 218.373 153.192 164.883 1.00 171.63 ? 221 VAL F C   1 
ATOM   10030 O O   . VAL F  2 187 ? 218.432 154.354 165.302 1.00 173.96 ? 221 VAL F O   1 
ATOM   10031 C CB  . VAL F  2 187 ? 215.977 152.393 164.869 1.00 152.17 ? 221 VAL F CB  1 
ATOM   10032 C CG1 . VAL F  2 187 ? 216.343 151.393 165.955 1.00 163.49 ? 221 VAL F CG1 1 
ATOM   10033 C CG2 . VAL F  2 187 ? 215.364 153.650 165.466 1.00 139.09 ? 221 VAL F CG2 1 
ATOM   10034 N N   . SER F  2 188 ? 219.316 152.295 165.163 1.00 176.49 ? 222 SER F N   1 
ATOM   10035 C CA  . SER F  2 188 ? 220.382 152.642 166.095 1.00 188.96 ? 222 SER F CA  1 
ATOM   10036 C C   . SER F  2 188 ? 221.606 151.777 165.839 1.00 194.49 ? 222 SER F C   1 
ATOM   10037 O O   . SER F  2 188 ? 221.542 150.765 165.137 1.00 192.72 ? 222 SER F O   1 
ATOM   10038 C CB  . SER F  2 188 ? 219.921 152.490 167.549 1.00 195.79 ? 222 SER F CB  1 
ATOM   10039 O OG  . SER F  2 188 ? 219.292 151.237 167.756 1.00 195.38 ? 222 SER F OG  1 
ATOM   10040 N N   . ALA F  2 189 ? 222.727 152.197 166.425 1.00 206.41 ? 223 ALA F N   1 
ATOM   10041 C CA  . ALA F  2 189 ? 223.982 151.464 166.329 1.00 218.86 ? 223 ALA F CA  1 
ATOM   10042 C C   . ALA F  2 189 ? 224.971 152.031 167.335 1.00 231.85 ? 223 ALA F C   1 
ATOM   10043 O O   . ALA F  2 189 ? 225.171 153.247 167.390 1.00 233.50 ? 223 ALA F O   1 
ATOM   10044 C CB  . ALA F  2 189 ? 224.571 151.553 164.915 1.00 217.99 ? 223 ALA F CB  1 
ATOM   10045 N N   . ASN F  2 190 ? 225.586 151.150 168.122 1.00 238.58 ? 224 ASN F N   1 
ATOM   10046 C CA  . ASN F  2 190 ? 226.730 151.532 168.941 1.00 245.51 ? 224 ASN F CA  1 
ATOM   10047 C C   . ASN F  2 190 ? 227.569 150.293 169.224 1.00 247.63 ? 224 ASN F C   1 
ATOM   10048 O O   . ASN F  2 190 ? 227.104 149.158 169.102 1.00 243.41 ? 224 ASN F O   1 
ATOM   10049 C CB  . ASN F  2 190 ? 226.304 152.281 170.215 1.00 249.72 ? 224 ASN F CB  1 
ATOM   10050 C CG  . ASN F  2 190 ? 225.184 151.603 170.984 1.00 251.19 ? 224 ASN F CG  1 
ATOM   10051 O OD1 . ASN F  2 190 ? 224.721 150.512 170.648 1.00 249.23 ? 224 ASN F OD1 1 
ATOM   10052 N ND2 . ASN F  2 190 ? 224.726 152.295 172.027 1.00 253.57 ? 224 ASN F ND2 1 
ATOM   10053 N N   . ARG F  2 191 ? 228.823 150.536 169.601 1.00 252.90 ? 225 ARG F N   1 
ATOM   10054 C CA  . ARG F  2 191 ? 229.920 149.597 169.407 1.00 258.44 ? 225 ARG F CA  1 
ATOM   10055 C C   . ARG F  2 191 ? 230.270 148.865 170.702 1.00 261.96 ? 225 ARG F C   1 
ATOM   10056 O O   . ARG F  2 191 ? 229.753 149.159 171.784 1.00 259.79 ? 225 ARG F O   1 
ATOM   10057 C CB  . ARG F  2 191 ? 231.143 150.335 168.859 1.00 263.80 ? 225 ARG F CB  1 
ATOM   10058 C CG  . ARG F  2 191 ? 231.997 149.504 167.924 1.00 268.65 ? 225 ARG F CG  1 
ATOM   10059 C CD  . ARG F  2 191 ? 231.728 149.879 166.482 1.00 268.59 ? 225 ARG F CD  1 
ATOM   10060 N NE  . ARG F  2 191 ? 232.669 150.876 165.988 1.00 273.12 ? 225 ARG F NE  1 
ATOM   10061 C CZ  . ARG F  2 191 ? 232.651 151.373 164.759 1.00 274.77 ? 225 ARG F CZ  1 
ATOM   10062 N NH1 . ARG F  2 191 ? 231.706 151.040 163.895 1.00 274.21 ? 225 ARG F NH1 1 
ATOM   10063 N NH2 . ARG F  2 191 ? 233.596 152.234 164.393 1.00 277.31 ? 225 ARG F NH2 1 
ATOM   10064 N N   . SER F  2 192 ? 231.170 147.892 170.569 1.00 267.95 ? 226 SER F N   1 
ATOM   10065 C CA  . SER F  2 192 ? 231.665 147.054 171.652 1.00 274.96 ? 226 SER F CA  1 
ATOM   10066 C C   . SER F  2 192 ? 233.045 147.529 172.104 1.00 282.39 ? 226 SER F C   1 
ATOM   10067 O O   . SER F  2 192 ? 233.551 148.567 171.669 1.00 283.49 ? 226 SER F O   1 
ATOM   10068 C CB  . SER F  2 192 ? 231.710 145.592 171.208 1.00 276.19 ? 226 SER F CB  1 
ATOM   10069 O OG  . SER F  2 192 ? 232.735 145.389 170.251 1.00 279.39 ? 226 SER F OG  1 
ATOM   10070 N N   . ASP F  2 193 ? 233.653 146.746 172.990 1.00 287.10 ? 227 ASP F N   1 
ATOM   10071 C CA  . ASP F  2 193 ? 234.979 147.077 173.504 1.00 292.64 ? 227 ASP F CA  1 
ATOM   10072 C C   . ASP F  2 193 ? 236.056 146.418 172.646 1.00 295.63 ? 227 ASP F C   1 
ATOM   10073 O O   . ASP F  2 193 ? 235.966 145.218 172.363 1.00 295.63 ? 227 ASP F O   1 
ATOM   10074 C CB  . ASP F  2 193 ? 235.111 146.632 174.959 1.00 294.62 ? 227 ASP F CB  1 
ATOM   10075 C CG  . ASP F  2 193 ? 234.670 145.197 175.174 1.00 294.40 ? 227 ASP F CG  1 
ATOM   10076 O OD1 . ASP F  2 193 ? 234.973 144.637 176.247 1.00 300.09 ? 227 ASP F OD1 1 
ATOM   10077 O OD2 . ASP F  2 193 ? 234.012 144.632 174.275 1.00 290.72 ? 227 ASP F OD2 1 
ATOM   10078 N N   . PRO F  2 194 ? 237.071 147.162 172.203 1.00 298.03 ? 228 PRO F N   1 
ATOM   10079 C CA  . PRO F  2 194 ? 238.112 146.572 171.344 1.00 300.06 ? 228 PRO F CA  1 
ATOM   10080 C C   . PRO F  2 194 ? 238.813 145.400 172.021 1.00 302.63 ? 228 PRO F C   1 
ATOM   10081 O O   . PRO F  2 194 ? 239.087 145.430 173.223 1.00 301.41 ? 228 PRO F O   1 
ATOM   10082 C CB  . PRO F  2 194 ? 239.083 147.736 171.098 1.00 301.09 ? 228 PRO F CB  1 
ATOM   10083 C CG  . PRO F  2 194 ? 238.610 148.872 171.966 1.00 298.86 ? 228 PRO F CG  1 
ATOM   10084 C CD  . PRO F  2 194 ? 237.182 148.625 172.293 1.00 297.43 ? 228 PRO F CD  1 
ATOM   10085 N N   . VAL F  2 195 ? 239.101 144.363 171.231 1.00 305.86 ? 229 VAL F N   1 
ATOM   10086 C CA  . VAL F  2 195 ? 239.810 143.173 171.691 1.00 308.98 ? 229 VAL F CA  1 
ATOM   10087 C C   . VAL F  2 195 ? 241.134 143.074 170.944 1.00 314.00 ? 229 VAL F C   1 
ATOM   10088 O O   . VAL F  2 195 ? 241.239 143.455 169.775 1.00 313.99 ? 229 VAL F O   1 
ATOM   10089 C CB  . VAL F  2 195 ? 238.940 141.912 171.493 1.00 305.97 ? 229 VAL F CB  1 
ATOM   10090 C CG1 . VAL F  2 195 ? 239.700 140.650 171.877 1.00 308.63 ? 229 VAL F CG1 1 
ATOM   10091 C CG2 . VAL F  2 195 ? 237.658 142.025 172.300 1.00 300.56 ? 229 VAL F CG2 1 
ATOM   10092 N N   . THR F  2 196 ? 242.160 142.566 171.623 1.00 318.41 ? 230 THR F N   1 
ATOM   10093 C CA  . THR F  2 196 ? 243.496 142.444 171.060 1.00 321.77 ? 230 THR F CA  1 
ATOM   10094 C C   . THR F  2 196 ? 243.961 140.992 171.072 1.00 323.30 ? 230 THR F C   1 
ATOM   10095 O O   . THR F  2 196 ? 243.368 140.128 171.724 1.00 322.82 ? 230 THR F O   1 
ATOM   10096 C CB  . THR F  2 196 ? 244.497 143.311 171.833 1.00 324.34 ? 230 THR F CB  1 
ATOM   10097 O OG1 . THR F  2 196 ? 245.767 143.286 171.171 1.00 326.55 ? 230 THR F OG1 1 
ATOM   10098 C CG2 . THR F  2 196 ? 244.661 142.794 173.255 1.00 324.50 ? 230 THR F CG2 1 
ATOM   10099 N N   . LEU F  2 197 ? 245.038 140.734 170.332 1.00 325.24 ? 231 LEU F N   1 
ATOM   10100 C CA  . LEU F  2 197 ? 245.686 139.428 170.289 1.00 327.36 ? 231 LEU F CA  1 
ATOM   10101 C C   . LEU F  2 197 ? 246.894 139.424 171.213 1.00 330.46 ? 231 LEU F C   1 
ATOM   10102 O O   . LEU F  2 197 ? 247.466 140.480 171.502 1.00 331.52 ? 231 LEU F O   1 
ATOM   10103 C CB  . LEU F  2 197 ? 246.127 139.060 168.869 1.00 326.84 ? 231 LEU F CB  1 
ATOM   10104 C CG  . LEU F  2 197 ? 245.119 139.096 167.723 1.00 322.67 ? 231 LEU F CG  1 
ATOM   10105 C CD1 . LEU F  2 197 ? 245.577 138.195 166.591 1.00 326.22 ? 231 LEU F CD1 1 
ATOM   10106 C CD2 . LEU F  2 197 ? 243.761 138.649 168.220 1.00 319.42 ? 231 LEU F CD2 1 
ATOM   10107 N N   . ASN F  2 198 ? 247.277 138.235 171.669 1.00 332.29 ? 232 ASN F N   1 
ATOM   10108 C CA  . ASN F  2 198 ? 248.456 138.053 172.505 1.00 331.99 ? 232 ASN F CA  1 
ATOM   10109 C C   . ASN F  2 198 ? 249.496 137.265 171.717 1.00 331.50 ? 232 ASN F C   1 
ATOM   10110 O O   . ASN F  2 198 ? 249.293 136.082 171.422 1.00 334.33 ? 232 ASN F O   1 
ATOM   10111 C CB  . ASN F  2 198 ? 248.094 137.328 173.802 1.00 332.16 ? 232 ASN F CB  1 
ATOM   10112 C CG  . ASN F  2 198 ? 249.306 137.035 174.671 1.00 330.21 ? 232 ASN F CG  1 
ATOM   10113 O OD1 . ASN F  2 198 ? 249.288 136.111 175.484 1.00 330.29 ? 232 ASN F OD1 1 
ATOM   10114 N ND2 . ASN F  2 198 ? 250.355 137.837 174.523 1.00 329.17 ? 232 ASN F ND2 1 
ATOM   10115 N N   . VAL F  2 199 ? 250.603 137.923 171.376 1.00 330.47 ? 233 VAL F N   1 
ATOM   10116 C CA  . VAL F  2 199 ? 251.728 137.299 170.689 1.00 329.03 ? 233 VAL F CA  1 
ATOM   10117 C C   . VAL F  2 199 ? 253.011 137.764 171.368 1.00 328.10 ? 233 VAL F C   1 
ATOM   10118 O O   . VAL F  2 199 ? 253.026 138.751 172.106 1.00 327.57 ? 233 VAL F O   1 
ATOM   10119 C CB  . VAL F  2 199 ? 251.763 137.636 169.181 1.00 328.67 ? 233 VAL F CB  1 
ATOM   10120 C CG1 . VAL F  2 199 ? 250.606 136.966 168.454 1.00 328.68 ? 233 VAL F CG1 1 
ATOM   10121 C CG2 . VAL F  2 199 ? 251.738 139.141 168.975 1.00 330.82 ? 233 VAL F CG2 1 
ATOM   10122 N N   . THR F  2 200 ? 254.098 137.043 171.114 1.00 327.14 ? 234 THR F N   1 
ATOM   10123 C CA  . THR F  2 200 ? 255.387 137.380 171.708 1.00 323.98 ? 234 THR F CA  1 
ATOM   10124 C C   . THR F  2 200 ? 256.539 136.939 170.812 1.00 322.19 ? 234 THR F C   1 
ATOM   10125 O O   . THR F  2 200 ? 257.317 137.764 170.332 1.00 320.88 ? 234 THR F O   1 
ATOM   10126 C CB  . THR F  2 200 ? 255.551 136.738 173.098 1.00 321.60 ? 234 THR F CB  1 
ATOM   10127 O OG1 . THR F  2 200 ? 254.706 137.411 174.040 1.00 322.03 ? 234 THR F OG1 1 
ATOM   10128 C CG2 . THR F  2 200 ? 256.996 136.834 173.563 1.00 319.00 ? 234 THR F CG2 1 
HETATM 10129 C C1  . NAG G  3 .   ? 146.858 121.109 161.287 1.00 117.00 ? 501 NAG D C1  1 
HETATM 10130 C C2  . NAG G  3 .   ? 146.649 119.854 160.436 1.00 115.93 ? 501 NAG D C2  1 
HETATM 10131 C C3  . NAG G  3 .   ? 145.800 118.836 161.102 1.00 117.51 ? 501 NAG D C3  1 
HETATM 10132 C C4  . NAG G  3 .   ? 146.379 118.412 162.421 1.00 124.34 ? 501 NAG D C4  1 
HETATM 10133 C C5  . NAG G  3 .   ? 146.590 119.596 163.343 1.00 131.11 ? 501 NAG D C5  1 
HETATM 10134 C C6  . NAG G  3 .   ? 147.460 119.118 164.515 1.00 135.13 ? 501 NAG D C6  1 
HETATM 10135 C C7  . NAG G  3 .   ? 146.462 119.529 157.856 1.00 122.42 ? 501 NAG D C7  1 
HETATM 10136 C C8  . NAG G  3 .   ? 145.799 119.877 156.480 1.00 111.51 ? 501 NAG D C8  1 
HETATM 10137 N N2  . NAG G  3 .   ? 146.017 120.198 159.084 1.00 121.15 ? 501 NAG D N2  1 
HETATM 10138 O O3  . NAG G  3 .   ? 145.731 117.667 160.217 1.00 116.27 ? 501 NAG D O3  1 
HETATM 10139 O O4  . NAG G  3 .   ? 145.509 117.478 163.061 1.00 121.78 ? 501 NAG D O4  1 
HETATM 10140 O O5  . NAG G  3 .   ? 147.252 120.762 162.709 1.00 128.14 ? 501 NAG D O5  1 
HETATM 10141 O O6  . NAG G  3 .   ? 148.795 118.939 164.051 1.00 134.99 ? 501 NAG D O6  1 
HETATM 10142 O O7  . NAG G  3 .   ? 147.335 118.708 157.909 1.00 127.90 ? 501 NAG D O7  1 
HETATM 10143 C C1  . NAG H  3 .   ? 131.178 121.958 177.961 1.00 185.48 ? 502 NAG D C1  1 
HETATM 10144 C C2  . NAG H  3 .   ? 132.005 122.058 179.230 1.00 185.74 ? 502 NAG D C2  1 
HETATM 10145 C C3  . NAG H  3 .   ? 131.170 121.948 180.445 1.00 189.62 ? 502 NAG D C3  1 
HETATM 10146 C C4  . NAG H  3 .   ? 130.128 123.029 180.502 1.00 192.68 ? 502 NAG D C4  1 
HETATM 10147 C C5  . NAG H  3 .   ? 129.224 122.949 179.287 1.00 193.57 ? 502 NAG D C5  1 
HETATM 10148 C C6  . NAG H  3 .   ? 128.342 124.205 179.233 1.00 191.06 ? 502 NAG D C6  1 
HETATM 10149 C C7  . NAG H  3 .   ? 134.446 121.232 178.891 1.00 175.89 ? 502 NAG D C7  1 
HETATM 10150 C C8  . NAG H  3 .   ? 135.512 120.081 178.888 1.00 177.35 ? 502 NAG D C8  1 
HETATM 10151 N N2  . NAG H  3 .   ? 133.050 120.940 179.227 1.00 180.74 ? 502 NAG D N2  1 
HETATM 10152 O O3  . NAG H  3 .   ? 132.051 122.053 181.607 1.00 188.35 ? 502 NAG D O3  1 
HETATM 10153 O O4  . NAG H  3 .   ? 129.333 122.853 181.676 1.00 194.61 ? 502 NAG D O4  1 
HETATM 10154 O O5  . NAG H  3 .   ? 129.970 122.869 178.011 1.00 189.30 ? 502 NAG D O5  1 
HETATM 10155 O O6  . NAG H  3 .   ? 129.157 125.359 179.401 1.00 184.69 ? 502 NAG D O6  1 
HETATM 10156 O O7  . NAG H  3 .   ? 134.772 122.357 178.624 1.00 170.87 ? 502 NAG D O7  1 
HETATM 10157 C C1  . NAG I  3 .   ? 115.681 92.750  164.796 1.00 294.96 ? 503 NAG D C1  1 
HETATM 10158 C C2  . NAG I  3 .   ? 116.419 93.691  163.857 1.00 296.30 ? 503 NAG D C2  1 
HETATM 10159 C C3  . NAG I  3 .   ? 117.793 94.019  164.307 1.00 295.87 ? 503 NAG D C3  1 
HETATM 10160 C C4  . NAG I  3 .   ? 117.796 94.521  165.722 1.00 293.49 ? 503 NAG D C4  1 
HETATM 10161 C C5  . NAG I  3 .   ? 117.320 93.449  166.675 1.00 291.72 ? 503 NAG D C5  1 
HETATM 10162 C C6  . NAG I  3 .   ? 117.161 94.077  168.069 1.00 288.25 ? 503 NAG D C6  1 
HETATM 10163 C C7  . NAG I  3 .   ? 116.927 93.622  161.291 1.00 296.11 ? 503 NAG D C7  1 
HETATM 10164 C C8  . NAG I  3 .   ? 117.008 92.823  159.948 1.00 294.07 ? 503 NAG D C8  1 
HETATM 10165 N N2  . NAG I  3 .   ? 116.519 92.948  162.524 1.00 295.99 ? 503 NAG D N2  1 
HETATM 10166 O O3  . NAG I  3 .   ? 118.379 95.053  163.447 1.00 297.53 ? 503 NAG D O3  1 
HETATM 10167 O O4  . NAG I  3 .   ? 119.126 94.891  166.076 1.00 291.10 ? 503 NAG D O4  1 
HETATM 10168 O O5  . NAG I  3 .   ? 116.029 92.862  166.271 1.00 292.32 ? 503 NAG D O5  1 
HETATM 10169 O O6  . NAG I  3 .   ? 116.299 93.253  168.842 1.00 283.69 ? 503 NAG D O6  1 
HETATM 10170 O O7  . NAG I  3 .   ? 117.199 94.789  161.312 1.00 297.28 ? 503 NAG D O7  1 
HETATM 10171 C C1  . NAG J  3 .   ? 109.094 109.896 156.319 1.00 287.13 ? 504 NAG D C1  1 
HETATM 10172 C C2  . NAG J  3 .   ? 109.159 109.274 154.938 1.00 286.99 ? 504 NAG D C2  1 
HETATM 10173 C C3  . NAG J  3 .   ? 110.392 109.624 154.208 1.00 287.69 ? 504 NAG D C3  1 
HETATM 10174 C C4  . NAG J  3 .   ? 110.449 111.106 153.999 1.00 288.95 ? 504 NAG D C4  1 
HETATM 10175 C C5  . NAG J  3 .   ? 110.438 111.838 155.326 1.00 287.63 ? 504 NAG D C5  1 
HETATM 10176 C C6  . NAG J  3 .   ? 110.197 113.325 155.027 1.00 287.43 ? 504 NAG D C6  1 
HETATM 10177 C C7  . NAG J  3 .   ? 107.808 107.070 154.644 1.00 285.73 ? 504 NAG D C7  1 
HETATM 10178 C C8  . NAG J  3 .   ? 107.690 105.513 154.776 1.00 285.59 ? 504 NAG D C8  1 
HETATM 10179 N N2  . NAG J  3 .   ? 109.029 107.757 155.072 1.00 286.28 ? 504 NAG D N2  1 
HETATM 10180 O O3  . NAG J  3 .   ? 110.346 108.956 152.906 1.00 284.09 ? 504 NAG D O3  1 
HETATM 10181 O O4  . NAG J  3 .   ? 111.652 111.451 153.315 1.00 289.80 ? 504 NAG D O4  1 
HETATM 10182 O O5  . NAG J  3 .   ? 109.393 111.374 156.266 1.00 288.44 ? 504 NAG D O5  1 
HETATM 10183 O O6  . NAG J  3 .   ? 111.194 113.801 154.134 1.00 285.99 ? 504 NAG D O6  1 
HETATM 10184 O O7  . NAG J  3 .   ? 106.897 107.702 154.184 1.00 285.37 ? 504 NAG D O7  1 
HETATM 10185 C C1  . NAG K  3 .   ? 92.122  106.456 167.095 1.00 342.04 ? 505 NAG D C1  1 
HETATM 10186 C C2  . NAG K  3 .   ? 91.980  107.354 165.878 1.00 342.53 ? 505 NAG D C2  1 
HETATM 10187 C C3  . NAG K  3 .   ? 90.672  107.159 165.198 1.00 342.44 ? 505 NAG D C3  1 
HETATM 10188 C C4  . NAG K  3 .   ? 90.258  105.714 165.041 1.00 343.95 ? 505 NAG D C4  1 
HETATM 10189 C C5  . NAG K  3 .   ? 90.539  104.865 166.273 1.00 345.15 ? 505 NAG D C5  1 
HETATM 10190 C C6  . NAG K  3 .   ? 90.221  103.394 165.977 1.00 347.64 ? 505 NAG D C6  1 
HETATM 10191 C C7  . NAG K  3 .   ? 93.046  109.728 165.864 1.00 340.19 ? 505 NAG D C7  1 
HETATM 10192 C C8  . NAG K  3 .   ? 93.063  111.205 166.383 1.00 338.75 ? 505 NAG D C8  1 
HETATM 10193 N N2  . NAG K  3 .   ? 92.029  108.800 166.359 1.00 341.00 ? 505 NAG D N2  1 
HETATM 10194 O O3  . NAG K  3 .   ? 90.737  107.776 163.870 1.00 340.50 ? 505 NAG D O3  1 
HETATM 10195 O O4  . NAG K  3 .   ? 88.858  105.670 164.764 1.00 341.23 ? 505 NAG D O4  1 
HETATM 10196 O O5  . NAG K  3 .   ? 91.939  105.008 166.723 1.00 343.61 ? 505 NAG D O5  1 
HETATM 10197 O O6  . NAG K  3 .   ? 88.902  103.292 165.456 1.00 347.77 ? 505 NAG D O6  1 
HETATM 10198 O O7  . NAG K  3 .   ? 93.860  109.359 165.066 1.00 340.32 ? 505 NAG D O7  1 
HETATM 10199 C C1  . NAG L  3 .   ? 120.385 106.675 173.137 1.00 253.05 ? 506 NAG D C1  1 
HETATM 10200 C C2  . NAG L  3 .   ? 120.913 108.057 172.806 1.00 253.92 ? 506 NAG D C2  1 
HETATM 10201 C C3  . NAG L  3 .   ? 121.139 108.860 174.030 1.00 253.88 ? 506 NAG D C3  1 
HETATM 10202 C C4  . NAG L  3 .   ? 119.964 108.862 174.977 1.00 251.29 ? 506 NAG D C4  1 
HETATM 10203 C C5  . NAG L  3 .   ? 119.424 107.461 175.220 1.00 250.11 ? 506 NAG D C5  1 
HETATM 10204 C C6  . NAG L  3 .   ? 118.165 107.535 176.094 1.00 246.71 ? 506 NAG D C6  1 
HETATM 10205 C C7  . NAG L  3 .   ? 122.319 107.936 170.625 1.00 245.48 ? 506 NAG D C7  1 
HETATM 10206 C C8  . NAG L  3 .   ? 123.698 107.748 169.906 1.00 236.86 ? 506 NAG D C8  1 
HETATM 10207 N N2  . NAG L  3 .   ? 122.247 107.881 172.086 1.00 254.29 ? 506 NAG D N2  1 
HETATM 10208 O O3  . NAG L  3 .   ? 121.437 110.236 173.627 1.00 246.62 ? 506 NAG D O3  1 
HETATM 10209 O O4  . NAG L  3 .   ? 120.397 109.391 176.229 1.00 252.11 ? 506 NAG D O4  1 
HETATM 10210 O O5  . NAG L  3 .   ? 119.125 106.760 173.953 1.00 250.83 ? 506 NAG D O5  1 
HETATM 10211 O O6  . NAG L  3 .   ? 117.438 108.709 175.759 1.00 245.39 ? 506 NAG D O6  1 
HETATM 10212 O O7  . NAG L  3 .   ? 121.324 108.124 169.981 1.00 242.37 ? 506 NAG D O7  1 
HETATM 10213 C C1  . NAG M  3 .   ? 132.226 189.252 161.386 1.00 122.88 ? 501 NAG E C1  1 
HETATM 10214 C C2  . NAG M  3 .   ? 131.321 190.143 160.539 1.00 121.93 ? 501 NAG E C2  1 
HETATM 10215 C C3  . NAG M  3 .   ? 130.908 191.388 161.232 1.00 125.78 ? 501 NAG E C3  1 
HETATM 10216 C C4  . NAG M  3 .   ? 130.308 191.125 162.585 1.00 134.19 ? 501 NAG E C4  1 
HETATM 10217 C C5  . NAG M  3 .   ? 131.206 190.256 163.447 1.00 138.90 ? 501 NAG E C5  1 
HETATM 10218 C C6  . NAG M  3 .   ? 130.406 189.864 164.695 1.00 143.10 ? 501 NAG E C6  1 
HETATM 10219 C C7  . NAG M  3 .   ? 131.314 190.318 157.955 1.00 126.54 ? 501 NAG E C7  1 
HETATM 10220 C C8  . NAG M  3 .   ? 132.008 190.709 156.609 1.00 116.13 ? 501 NAG E C8  1 
HETATM 10221 N N2  . NAG M  3 .   ? 132.007 190.521 159.228 1.00 124.08 ? 501 NAG E N2  1 
HETATM 10222 O O3  . NAG M  3 .   ? 129.894 192.058 160.407 1.00 125.51 ? 501 NAG E O3  1 
HETATM 10223 O O4  . NAG M  3 .   ? 130.069 192.366 163.251 1.00 131.14 ? 501 NAG E O4  1 
HETATM 10224 O O5  . NAG M  3 .   ? 131.646 189.022 162.760 1.00 134.94 ? 501 NAG E O5  1 
HETATM 10225 O O6  . NAG M  3 .   ? 129.601 188.737 164.370 1.00 142.80 ? 501 NAG E O6  1 
HETATM 10226 O O7  . NAG M  3 .   ? 130.207 189.861 157.950 1.00 134.25 ? 501 NAG E O7  1 
HETATM 10227 C C1  . NAG N  3 .   ? 141.121 202.195 178.105 1.00 178.34 ? 502 NAG E C1  1 
HETATM 10228 C C2  . NAG N  3 .   ? 140.731 201.591 179.440 1.00 179.44 ? 502 NAG E C2  1 
HETATM 10229 C C3  . NAG N  3 .   ? 141.049 202.501 180.566 1.00 183.31 ? 502 NAG E C3  1 
HETATM 10230 C C4  . NAG N  3 .   ? 142.501 202.888 180.611 1.00 186.29 ? 502 NAG E C4  1 
HETATM 10231 C C5  . NAG N  3 .   ? 142.906 203.537 179.307 1.00 184.10 ? 502 NAG E C5  1 
HETATM 10232 C C6  . NAG N  3 .   ? 144.430 203.718 179.293 1.00 180.42 ? 502 NAG E C6  1 
HETATM 10233 C C7  . NAG N  3 .   ? 138.693 200.056 179.027 1.00 171.71 ? 502 NAG E C7  1 
HETATM 10234 C C8  . NAG N  3 .   ? 137.150 199.790 179.054 1.00 171.47 ? 502 NAG E C8  1 
HETATM 10235 N N2  . NAG N  3 .   ? 139.225 201.343 179.467 1.00 175.64 ? 502 NAG E N2  1 
HETATM 10236 O O3  . NAG N  3 .   ? 140.692 201.843 181.823 1.00 183.10 ? 502 NAG E O3  1 
HETATM 10237 O O4  . NAG N  3 .   ? 142.704 203.821 181.672 1.00 186.28 ? 502 NAG E O4  1 
HETATM 10238 O O5  . NAG N  3 .   ? 142.541 202.705 178.145 1.00 181.12 ? 502 NAG E O5  1 
HETATM 10239 O O6  . NAG N  3 .   ? 145.058 202.446 179.405 1.00 172.88 ? 502 NAG E O6  1 
HETATM 10240 O O7  . NAG N  3 .   ? 139.445 199.203 178.648 1.00 166.78 ? 502 NAG E O7  1 
HETATM 10241 C C1  . NAG O  3 .   ? 123.103 230.830 164.441 1.00 291.76 ? 503 NAG E C1  1 
HETATM 10242 C C2  . NAG O  3 .   ? 123.568 229.594 163.676 1.00 292.68 ? 503 NAG E C2  1 
HETATM 10243 C C3  . NAG O  3 .   ? 123.095 228.327 164.274 1.00 292.15 ? 503 NAG E C3  1 
HETATM 10244 C C4  . NAG O  3 .   ? 123.597 228.241 165.681 1.00 290.47 ? 503 NAG E C4  1 
HETATM 10245 C C5  . NAG O  3 .   ? 122.947 229.307 166.542 1.00 289.09 ? 503 NAG E C5  1 
HETATM 10246 C C6  . NAG O  3 .   ? 123.941 229.723 167.637 1.00 286.51 ? 503 NAG E C6  1 
HETATM 10247 C C7  . NAG O  3 .   ? 123.804 229.001 161.169 1.00 290.28 ? 503 NAG E C7  1 
HETATM 10248 C C8  . NAG O  3 .   ? 123.316 229.110 159.686 1.00 283.56 ? 503 NAG E C8  1 
HETATM 10249 N N2  . NAG O  3 .   ? 123.085 229.703 162.232 1.00 291.03 ? 503 NAG E N2  1 
HETATM 10250 O O3  . NAG O  3 .   ? 123.623 227.191 163.516 1.00 293.81 ? 503 NAG E O3  1 
HETATM 10251 O O4  . NAG O  3 .   ? 123.280 226.953 166.208 1.00 288.37 ? 503 NAG E O4  1 
HETATM 10252 O O5  . NAG O  3 .   ? 122.495 230.514 165.800 1.00 289.51 ? 503 NAG E O5  1 
HETATM 10253 O O6  . NAG O  3 .   ? 123.229 230.234 168.756 1.00 283.02 ? 503 NAG E O6  1 
HETATM 10254 O O7  . NAG O  3 .   ? 124.763 228.334 161.438 1.00 292.34 ? 503 NAG E O7  1 
HETATM 10255 C C1  . NAG P  3 .   ? 141.873 227.754 156.084 1.00 290.31 ? 504 NAG E C1  1 
HETATM 10256 C C2  . NAG P  3 .   ? 141.180 227.955 154.749 1.00 290.52 ? 504 NAG E C2  1 
HETATM 10257 C C3  . NAG P  3 .   ? 140.860 226.675 154.081 1.00 289.87 ? 504 NAG E C3  1 
HETATM 10258 C C4  . NAG P  3 .   ? 142.095 225.839 153.907 1.00 290.28 ? 504 NAG E C4  1 
HETATM 10259 C C5  . NAG P  3 .   ? 142.803 225.622 155.232 1.00 288.90 ? 504 NAG E C5  1 
HETATM 10260 C C6  . NAG P  3 .   ? 144.136 224.918 154.960 1.00 288.44 ? 504 NAG E C6  1 
HETATM 10261 C C7  . NAG P  3 .   ? 139.892 230.202 154.649 1.00 292.57 ? 504 NAG E C7  1 
HETATM 10262 C C8  . NAG P  3 .   ? 138.588 231.042 154.850 1.00 294.12 ? 504 NAG E C8  1 
HETATM 10263 N N2  . NAG P  3 .   ? 139.904 228.769 154.960 1.00 290.76 ? 504 NAG E N2  1 
HETATM 10264 O O3  . NAG P  3 .   ? 140.281 226.959 152.765 1.00 287.09 ? 504 NAG E O3  1 
HETATM 10265 O O4  . NAG P  3 .   ? 141.723 224.567 153.378 1.00 291.45 ? 504 NAG E O4  1 
HETATM 10266 O O5  . NAG P  3 .   ? 143.086 226.879 155.946 1.00 290.36 ? 504 NAG E O5  1 
HETATM 10267 O O6  . NAG P  3 .   ? 143.907 223.787 154.132 1.00 287.48 ? 504 NAG E O6  1 
HETATM 10268 O O7  . NAG P  3 .   ? 140.877 230.738 154.224 1.00 292.73 ? 504 NAG E O7  1 
HETATM 10269 C C1  . NAG Q  3 .   ? 147.841 244.698 167.426 1.00 351.74 ? 505 NAG E C1  1 
HETATM 10270 C C2  . NAG Q  3 .   ? 148.394 244.149 166.124 1.00 352.79 ? 505 NAG E C2  1 
HETATM 10271 C C3  . NAG Q  3 .   ? 148.739 245.256 165.197 1.00 353.22 ? 505 NAG E C3  1 
HETATM 10272 C C4  . NAG Q  3 .   ? 147.628 246.266 165.032 1.00 354.94 ? 505 NAG E C4  1 
HETATM 10273 C C5  . NAG Q  3 .   ? 146.953 246.662 166.339 1.00 355.68 ? 505 NAG E C5  1 
HETATM 10274 C C6  . NAG Q  3 .   ? 145.692 247.478 166.031 1.00 358.62 ? 505 NAG E C6  1 
HETATM 10275 C C7  . NAG Q  3 .   ? 149.759 241.948 166.008 1.00 351.68 ? 505 NAG E C7  1 
HETATM 10276 C C8  . NAG Q  3 .   ? 151.063 241.139 166.317 1.00 351.87 ? 505 NAG E C8  1 
HETATM 10277 N N2  . NAG Q  3 .   ? 149.659 243.349 166.419 1.00 352.32 ? 505 NAG E N2  1 
HETATM 10278 O O3  . NAG Q  3 .   ? 149.062 244.690 163.884 1.00 352.21 ? 505 NAG E O3  1 
HETATM 10279 O O4  . NAG Q  3 .   ? 148.168 247.440 164.423 1.00 351.68 ? 505 NAG E O4  1 
HETATM 10280 O O5  . NAG Q  3 .   ? 146.589 245.492 167.163 1.00 353.49 ? 505 NAG E O5  1 
HETATM 10281 O O6  . NAG Q  3 .   ? 146.057 248.676 165.359 1.00 359.89 ? 505 NAG E O6  1 
HETATM 10282 O O7  . NAG Q  3 .   ? 148.847 241.421 165.437 1.00 350.85 ? 505 NAG E O7  1 
HETATM 10283 C C1  . NAG R  3 .   ? 133.752 219.095 172.952 1.00 250.27 ? 506 NAG E C1  1 
HETATM 10284 C C2  . NAG R  3 .   ? 134.406 217.858 172.375 1.00 251.29 ? 506 NAG E C2  1 
HETATM 10285 C C3  . NAG R  3 .   ? 135.016 216.998 173.411 1.00 248.84 ? 506 NAG E C3  1 
HETATM 10286 C C4  . NAG R  3 .   ? 135.851 217.748 174.415 1.00 249.46 ? 506 NAG E C4  1 
HETATM 10287 C C5  . NAG R  3 .   ? 135.121 218.985 174.911 1.00 249.94 ? 506 NAG E C5  1 
HETATM 10288 C C6  . NAG R  3 .   ? 135.956 219.663 176.018 1.00 248.29 ? 506 NAG E C6  1 
HETATM 10289 C C7  . NAG R  3 .   ? 133.267 217.204 170.132 1.00 240.94 ? 506 NAG E C7  1 
HETATM 10290 C C8  . NAG R  3 .   ? 132.187 216.391 169.343 1.00 232.74 ? 506 NAG E C8  1 
HETATM 10291 N N2  . NAG R  3 .   ? 133.358 217.069 171.591 1.00 250.56 ? 506 NAG E N2  1 
HETATM 10292 O O3  . NAG R  3 .   ? 135.862 216.034 172.709 1.00 236.87 ? 506 NAG E O3  1 
HETATM 10293 O O4  . NAG R  3 .   ? 136.078 216.898 175.535 1.00 253.15 ? 506 NAG E O4  1 
HETATM 10294 O O5  . NAG R  3 .   ? 134.754 219.866 173.771 1.00 250.01 ? 506 NAG E O5  1 
HETATM 10295 O O6  . NAG R  3 .   ? 136.193 221.038 175.749 1.00 247.83 ? 506 NAG E O6  1 
HETATM 10296 O O7  . NAG R  3 .   ? 134.012 217.936 169.538 1.00 240.06 ? 506 NAG E O7  1 
HETATM 10297 C C1  . NAG S  3 .   ? 198.580 167.510 161.247 1.00 118.72 ? 501 NAG F C1  1 
HETATM 10298 C C2  . NAG S  3 .   ? 199.847 168.109 160.693 1.00 117.59 ? 501 NAG F C2  1 
HETATM 10299 C C3  . NAG S  3 .   ? 200.963 167.924 161.639 1.00 118.43 ? 501 NAG F C3  1 
HETATM 10300 C C4  . NAG S  3 .   ? 200.717 168.636 162.940 1.00 128.87 ? 501 NAG F C4  1 
HETATM 10301 C C5  . NAG S  3 .   ? 199.394 168.220 163.560 1.00 132.48 ? 501 NAG F C5  1 
HETATM 10302 C C6  . NAG S  3 .   ? 199.018 169.250 164.638 1.00 133.27 ? 501 NAG F C6  1 
HETATM 10303 C C7  . NAG S  3 .   ? 200.270 168.213 158.168 1.00 125.56 ? 501 NAG F C7  1 
HETATM 10304 C C8  . NAG S  3 .   ? 200.637 167.537 156.804 1.00 117.99 ? 501 NAG F C8  1 
HETATM 10305 N N2  . NAG S  3 .   ? 200.205 167.412 159.386 1.00 121.46 ? 501 NAG F N2  1 
HETATM 10306 O O3  . NAG S  3 .   ? 202.163 168.484 161.026 1.00 112.37 ? 501 NAG F O3  1 
HETATM 10307 O O4  . NAG S  3 .   ? 201.766 168.337 163.867 1.00 126.96 ? 501 NAG F O4  1 
HETATM 10308 O O5  . NAG S  3 .   ? 198.267 168.133 162.594 1.00 128.11 ? 501 NAG F O5  1 
HETATM 10309 O O6  . NAG S  3 .   ? 199.386 170.555 164.203 1.00 133.64 ? 501 NAG F O6  1 
HETATM 10310 O O7  . NAG S  3 .   ? 200.037 169.391 158.218 1.00 130.47 ? 501 NAG F O7  1 
HETATM 10311 C C1  . NAG T  3 .   ? 205.333 153.469 178.067 1.00 171.20 ? 502 NAG F C1  1 
HETATM 10312 C C2  . NAG T  3 .   ? 205.121 154.344 179.293 1.00 172.58 ? 502 NAG F C2  1 
HETATM 10313 C C3  . NAG T  3 .   ? 205.735 153.778 180.520 1.00 175.91 ? 502 NAG F C3  1 
HETATM 10314 C C4  . NAG T  3 .   ? 205.366 152.334 180.737 1.00 179.07 ? 502 NAG F C4  1 
HETATM 10315 C C5  . NAG T  3 .   ? 205.630 151.486 179.508 1.00 178.16 ? 502 NAG F C5  1 
HETATM 10316 C C6  . NAG T  3 .   ? 205.102 150.075 179.772 1.00 178.15 ? 502 NAG F C6  1 
HETATM 10317 C C7  . NAG T  3 .   ? 204.788 156.872 178.831 1.00 163.04 ? 502 NAG F C7  1 
HETATM 10318 C C8  . NAG T  3 .   ? 205.389 158.295 178.571 1.00 163.23 ? 502 NAG F C8  1 
HETATM 10319 N N2  . NAG T  3 .   ? 205.692 155.736 179.030 1.00 167.47 ? 502 NAG F N2  1 
HETATM 10320 O O3  . NAG T  3 .   ? 205.274 154.566 181.674 1.00 177.28 ? 502 NAG F O3  1 
HETATM 10321 O O4  . NAG T  3 .   ? 206.135 151.820 181.824 1.00 178.66 ? 502 NAG F O4  1 
HETATM 10322 O O5  . NAG T  3 .   ? 204.963 152.025 178.312 1.00 174.07 ? 502 NAG F O5  1 
HETATM 10323 O O6  . NAG T  3 .   ? 203.699 150.047 179.541 1.00 175.73 ? 502 NAG F O6  1 
HETATM 10324 O O7  . NAG T  3 .   ? 203.599 156.709 178.871 1.00 160.13 ? 502 NAG F O7  1 
HETATM 10325 C C1  . NAG U  3 .   ? 239.037 155.845 164.722 1.00 310.02 ? 503 NAG F C1  1 
HETATM 10326 C C2  . NAG U  3 .   ? 237.735 155.926 163.931 1.00 311.61 ? 503 NAG F C2  1 
HETATM 10327 C C3  . NAG U  3 .   ? 236.780 156.924 164.453 1.00 313.03 ? 503 NAG F C3  1 
HETATM 10328 C C4  . NAG U  3 .   ? 236.429 156.556 165.859 1.00 312.95 ? 503 NAG F C4  1 
HETATM 10329 C C5  . NAG U  3 .   ? 237.640 156.713 166.757 1.00 312.26 ? 503 NAG F C5  1 
HETATM 10330 C C6  . NAG U  3 .   ? 237.368 155.944 168.059 1.00 310.25 ? 503 NAG F C6  1 
HETATM 10331 C C7  . NAG U  3 .   ? 237.384 155.524 161.404 1.00 306.36 ? 503 NAG F C7  1 
HETATM 10332 C C8  . NAG U  3 .   ? 237.703 155.858 159.908 1.00 302.90 ? 503 NAG F C8  1 
HETATM 10333 N N2  . NAG U  3 .   ? 238.054 156.261 162.477 1.00 309.37 ? 503 NAG F N2  1 
HETATM 10334 O O3  . NAG U  3 .   ? 235.570 156.908 163.629 1.00 313.93 ? 503 NAG F O3  1 
HETATM 10335 O O4  . NAG U  3 .   ? 235.389 157.416 166.322 1.00 312.79 ? 503 NAG F O4  1 
HETATM 10336 O O5  . NAG U  3 .   ? 238.923 156.229 166.190 1.00 311.52 ? 503 NAG F O5  1 
HETATM 10337 O O6  . NAG U  3 .   ? 238.543 155.921 168.858 1.00 306.42 ? 503 NAG F O6  1 
HETATM 10338 O O7  . NAG U  3 .   ? 236.590 154.668 161.672 1.00 305.51 ? 503 NAG F O7  1 
HETATM 10339 C C1  . NAG V  3 .   ? 227.498 140.923 156.769 1.00 294.61 ? 504 NAG F C1  1 
HETATM 10340 C C2  . NAG V  3 .   ? 228.026 141.141 155.365 1.00 296.37 ? 504 NAG F C2  1 
HETATM 10341 C C3  . NAG V  3 .   ? 227.115 141.936 154.522 1.00 297.06 ? 504 NAG F C3  1 
HETATM 10342 C C4  . NAG V  3 .   ? 225.830 141.190 154.348 1.00 296.45 ? 504 NAG F C4  1 
HETATM 10343 C C5  . NAG V  3 .   ? 225.172 140.955 155.692 1.00 295.16 ? 504 NAG F C5  1 
HETATM 10344 C C6  . NAG V  3 .   ? 224.013 139.977 155.450 1.00 293.92 ? 504 NAG F C6  1 
HETATM 10345 C C7  . NAG V  3 .   ? 230.579 141.112 154.925 1.00 297.69 ? 504 NAG F C7  1 
HETATM 10346 C C8  . NAG V  3 .   ? 231.986 141.799 154.997 1.00 298.79 ? 504 NAG F C8  1 
HETATM 10347 N N2  . NAG V  3 .   ? 229.399 141.806 155.444 1.00 297.60 ? 504 NAG F N2  1 
HETATM 10348 O O3  . NAG V  3 .   ? 227.751 142.094 153.214 1.00 294.62 ? 504 NAG F O3  1 
HETATM 10349 O O4  . NAG V  3 .   ? 224.934 141.955 153.547 1.00 296.37 ? 504 NAG F O4  1 
HETATM 10350 O O5  . NAG V  3 .   ? 226.079 140.400 156.732 1.00 295.13 ? 504 NAG F O5  1 
HETATM 10351 O O6  . NAG V  3 .   ? 223.216 140.448 154.374 1.00 292.05 ? 504 NAG F O6  1 
HETATM 10352 O O7  . NAG V  3 .   ? 230.462 140.019 154.441 1.00 297.47 ? 504 NAG F O7  1 
HETATM 10353 C C1  . NAG W  3 .   ? 239.048 127.390 167.211 1.00 346.57 ? 505 NAG F C1  1 
HETATM 10354 C C2  . NAG W  3 .   ? 238.374 127.077 165.889 1.00 346.20 ? 505 NAG F C2  1 
HETATM 10355 C C3  . NAG W  3 .   ? 239.233 126.167 165.084 1.00 346.29 ? 505 NAG F C3  1 
HETATM 10356 C C4  . NAG W  3 .   ? 240.696 126.559 165.032 1.00 349.47 ? 505 NAG F C4  1 
HETATM 10357 C C5  . NAG W  3 .   ? 241.251 127.070 166.355 1.00 350.82 ? 505 NAG F C5  1 
HETATM 10358 C C6  . NAG W  3 .   ? 242.655 127.657 166.157 1.00 353.92 ? 505 NAG F C6  1 
HETATM 10359 C C7  . NAG W  3 .   ? 235.799 127.105 166.181 1.00 343.43 ? 505 NAG F C7  1 
HETATM 10360 C C8  . NAG W  3 .   ? 234.457 126.355 166.472 1.00 342.58 ? 505 NAG F C8  1 
HETATM 10361 N N2  . NAG W  3 .   ? 237.059 126.361 166.171 1.00 344.26 ? 505 NAG F N2  1 
HETATM 10362 O O3  . NAG W  3 .   ? 238.713 126.114 163.715 1.00 342.62 ? 505 NAG F O3  1 
HETATM 10363 O O4  . NAG W  3 .   ? 241.458 125.418 164.638 1.00 346.94 ? 505 NAG F O4  1 
HETATM 10364 O O5  . NAG W  3 .   ? 240.361 128.082 166.953 1.00 349.36 ? 505 NAG F O5  1 
HETATM 10365 O O6  . NAG W  3 .   ? 243.517 126.660 165.626 1.00 354.44 ? 505 NAG F O6  1 
HETATM 10366 O O7  . NAG W  3 .   ? 235.797 128.285 165.968 1.00 343.36 ? 505 NAG F O7  1 
HETATM 10367 C C1  . NAG X  3 .   ? 223.677 151.997 172.981 1.00 256.02 ? 506 NAG F C1  1 
HETATM 10368 C C2  . NAG X  3 .   ? 222.261 152.101 172.458 1.00 256.77 ? 506 NAG F C2  1 
HETATM 10369 C C3  . NAG X  3 .   ? 221.330 152.154 173.617 1.00 254.31 ? 506 NAG F C3  1 
HETATM 10370 C C4  . NAG X  3 .   ? 221.567 151.104 174.678 1.00 258.54 ? 506 NAG F C4  1 
HETATM 10371 C C5  . NAG X  3 .   ? 223.035 150.958 175.029 1.00 256.02 ? 506 NAG F C5  1 
HETATM 10372 C C6  . NAG X  3 .   ? 223.223 149.846 176.074 1.00 253.20 ? 506 NAG F C6  1 
HETATM 10373 C C7  . NAG X  3 .   ? 222.305 153.414 170.209 1.00 243.90 ? 506 NAG F C7  1 
HETATM 10374 C C8  . NAG X  3 .   ? 222.172 154.762 169.421 1.00 234.76 ? 506 NAG F C8  1 
HETATM 10375 N N2  . NAG X  3 .   ? 222.127 153.398 171.663 1.00 255.66 ? 506 NAG F N2  1 
HETATM 10376 O O3  . NAG X  3 .   ? 219.962 152.003 173.131 1.00 243.68 ? 506 NAG F O3  1 
HETATM 10377 O O4  . NAG X  3 .   ? 220.866 151.485 175.860 1.00 265.81 ? 506 NAG F O4  1 
HETATM 10378 O O5  . NAG X  3 .   ? 223.825 150.737 173.799 1.00 255.61 ? 506 NAG F O5  1 
HETATM 10379 O O6  . NAG X  3 .   ? 224.502 149.257 175.908 1.00 251.01 ? 506 NAG F O6  1 
HETATM 10380 O O7  . NAG X  3 .   ? 222.552 152.401 169.619 1.00 242.90 ? 506 NAG F O7  1 
HETATM 10381 O O   . HOH Y  4 .   ? 144.694 143.666 177.959 1.00 79.46  ? 501 HOH A O   1 
HETATM 10382 O O   . HOH Z  4 .   ? 153.099 179.896 177.995 1.00 82.83  ? 501 HOH B O   1 
HETATM 10383 O O   . HOH AA 4 .   ? 180.084 154.667 177.958 1.00 77.35  ? 501 HOH C O   1 
# 
