data_9DB2
# 
_entry.id   9DB2 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   9DB2         pdb_00009db2 10.2210/pdb9db2/pdb 
WWPDB D_1000287765 ?            ?                   
EMDB  EMD-46711    ?            ?                   
# 
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 
1 'Structure model' 1 0 2024-11-06 
2 'Structure model' 1 1 2024-11-27 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Data collection' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            em_admin 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    2 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_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                        9DB2 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-23 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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           N 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'Class Ia ribonucleotide reductase with mechanism-based inhibitor N3CDP' 
_pdbx_database_related.db_id          EMD-46711 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              cdrennan@mit.edu 
_pdbx_contact_author.name_first         Catherine 
_pdbx_contact_author.name_last          Drennan 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5486-2755 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Westmoreland, D.E.' 1 0000-0002-5728-2446 
'Drennan, C.L.'      2 0000-0001-5486-2755 
# 
_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            121 
_citation.language                  ? 
_citation.page_first                e2417157121 
_citation.page_last                 e2417157121 
_citation.title                     
'2.6- angstrom resolution cryo-EM structure of a class Ia ribonucleotide reductase trapped with mechanism-based inhibitor N 3 CDP.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1073/pnas.2417157121 
_citation.pdbx_database_id_PubMed   39475643 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Westmoreland, D.E.' 1 ?                   
primary 'Feliciano, P.R.'    2 0000-0003-3853-115X 
primary 'Kang, G.'           3 ?                   
primary 'Cui, C.'            4 ?                   
primary 'Kim, A.'            5 ?                   
primary 'Stubbe, J.'         6 0000-0001-8076-4489 
primary 'Nocera, D.G.'       7 0000-0001-5055-320X 
primary 'Drennan, C.L.'      8 0000-0001-5486-2755 
# 
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 'Ribonucleoside-diphosphate reductase 1 subunit alpha' 85877.086 2   1.17.4.1 ? ? ? 
2 polymer     man 'Ribonucleoside-diphosphate reductase 1 subunit beta' 43558.055 2   1.17.4.1 ? ? ? 
3 non-polymer syn 
;2'-DEOXYADENOSINE 5'-TRIPHOSPHATE
;
491.182   2   ?        ? ? ? 
4 non-polymer syn 'MAGNESIUM ION' 24.305    4   ?        ? ? ? 
5 non-polymer syn "ADENOSINE-5'-TRIPHOSPHATE" 507.181   4   ?        ? ? ? 
6 non-polymer syn 'UNKNOWN LIGAND' 214.110   1   ?        ? ? ? 
7 non-polymer syn 
'4-amino-1-{(3xi)-3-C-amino-2-deoxy-5-O-[(S)-hydroxy(phosphonooxy)phosphoryl]-beta-D-threo-pentofuranosyl}pyrimidin-2(1H)-one' 
402.192   1   ?        ? ? ? 
8 non-polymer syn MU-OXO-DIIRON 127.689   2   ?        ? ? ? 
9 water       nat water 18.015    624 ?        ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Protein B1,Ribonucleoside-diphosphate reductase 1 R1 subunit,Ribonucleotide reductase 1' 
2 'Protein B2,Protein R2,Ribonucleotide reductase 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 
;MNQNLLVTKRDGSTERINLDKIHRVLDWAAEGLHNVSISQVELRSHIQFYDGIKTSDIHETIIKAAADLISRDAPDYQYL
AARLAIFHLRKKAYGQFEPPALYDHVVKMVEMGKYDNHLLEDYTEEEFKQMDTFIDHDRDMTFSYAAVKQLEGKYLVQNR
VTGEIYESAQFLYILVAACLFSNYPRETRLQYVKRFYDAVSTFKISLPTPIMSGVRTPTRQFSSCVLIECGDSLDSINAT
SSAIVKYVSQRAGIGINAGRIRALGSPIRGGEAFHTGCIPFYKHFQTAVKSCSQGGVRGGAATLFYPMWHLEVESLLVLK
NNRGVEGNRVRHMDYGVQINKLMYTRLLKGEDITLFSPSDVPGLYDAFFADQEEFERLYTKYEKDDSIRKQRVKAVELFS
LMMQERASTGRIYIQNVDHCNTHSPFDPAIAPVRQSNLCLEIALPTKPLNDVNDENGEIALCTLSAFNLGAINNLDELEE
LAILAVRALDALLDYQDYPIPAAKRGAMGRRTLGIGVINFAYYLAKHGKRYSDGSANNLTHKTFEAIQYYLLKASNELAK
EQGACPWFNETTYAKGILPIDTYKKDLDTIANEPLHYDWEALRESIKTHGLRNSTLSALMPSETSSQISNATNGIEPPRG
YVSIKASKDGILRQVVPDYEHLHDAYELLWEMPGNDGYLQLVGIMQKFIDQSISANTNYDPSRFPSGKVPMQQLLKDLLT
AYKFGVKTLYYQNTRDGAEDAQDDLVPSIQDDGCESGACKI
;
;MNQNLLVTKRDGSTERINLDKIHRVLDWAAEGLHNVSISQVELRSHIQFYDGIKTSDIHETIIKAAADLISRDAPDYQYL
AARLAIFHLRKKAYGQFEPPALYDHVVKMVEMGKYDNHLLEDYTEEEFKQMDTFIDHDRDMTFSYAAVKQLEGKYLVQNR
VTGEIYESAQFLYILVAACLFSNYPRETRLQYVKRFYDAVSTFKISLPTPIMSGVRTPTRQFSSCVLIECGDSLDSINAT
SSAIVKYVSQRAGIGINAGRIRALGSPIRGGEAFHTGCIPFYKHFQTAVKSCSQGGVRGGAATLFYPMWHLEVESLLVLK
NNRGVEGNRVRHMDYGVQINKLMYTRLLKGEDITLFSPSDVPGLYDAFFADQEEFERLYTKYEKDDSIRKQRVKAVELFS
LMMQERASTGRIYIQNVDHCNTHSPFDPAIAPVRQSNLCLEIALPTKPLNDVNDENGEIALCTLSAFNLGAINNLDELEE
LAILAVRALDALLDYQDYPIPAAKRGAMGRRTLGIGVINFAYYLAKHGKRYSDGSANNLTHKTFEAIQYYLLKASNELAK
EQGACPWFNETTYAKGILPIDTYKKDLDTIANEPLHYDWEALRESIKTHGLRNSTLSALMPSETSSQISNATNGIEPPRG
YVSIKASKDGILRQVVPDYEHLHDAYELLWEMPGNDGYLQLVGIMQKFIDQSISANTNYDPSRFPSGKVPMQQLLKDLLT
AYKFGVKTLYYQNTRDGAEDAQDDLVPSIQDDGCESGACKI
;
A,B ? 
2 'polypeptide(L)' no no 
;MAYTTFSQTKNDQLKEPMFFGQPVNVARYDQQKYDIFEKLIEKQLSFFWRPEEVDVSRDRIDYQALPEHEKHIFISNLKY
QTLLDSIQGRSPNVALLPLISIPELETWVETWAFSETIHSRSYTHIIRNIVNDPSVVFDDIVTNEQIQKRAEGISSYYDE
LIEMTSYWHLLGEGTHTVNGKTVTVSLRELKKKLYLCLMSVNALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEA
LHLTGTQHMLNLLRSGADDPEMAEIAEECKQECYDLFVQAAQQEKDWADYLFRDGSMIGLNKDILCQYVEYITNIRMQAV
GLDLPFQTRSNPIPWINTWLVSDNVQVAPQEVEVSSYLVGQIDSEVDTDDLSNFQL
;
;MAYTTFSQTKNDQLKEPMFFGQPVNVARYDQQKYDIFEKLIEKQLSFFWRPEEVDVSRDRIDYQALPEHEKHIFISNLKY
QTLLDSIQGRSPNVALLPLISIPELETWVETWAFSETIHSRSYTHIIRNIVNDPSVVFDDIVTNEQIQKRAEGISSYYDE
LIEMTSYWHLLGEGTHTVNGKTVTVSLRELKKKLYLCLMSVNALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEA
LHLTGTQHMLNLLRSGADDPEMAEIAEECKQECYDLFVQAAQQEKDWADYLFRDGSMIGLNKDILCQYVEYITNIRMQAV
GLDLPFQTRSNPIPWINTWLVSDNVQVAPQEVEVSSYLVGQIDSEVDTDDLSNFQL
;
C,D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 
;2'-DEOXYADENOSINE 5'-TRIPHOSPHATE
;
DTP   
4 'MAGNESIUM ION'                                                                                                                
MG    
5 "ADENOSINE-5'-TRIPHOSPHATE"                                                                                                    
ATP   
6 'UNKNOWN LIGAND'                                                                                                               
UNL   
7 '4-amino-1-{(3xi)-3-C-amino-2-deoxy-5-O-[(S)-hydroxy(phosphonooxy)phosphoryl]-beta-D-threo-pentofuranosyl}pyrimidin-2(1H)-one' 
A1A3L 
8 MU-OXO-DIIRON                                                                                                                  
FEO   
9 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   ASN n 
1 3   GLN n 
1 4   ASN n 
1 5   LEU n 
1 6   LEU n 
1 7   VAL n 
1 8   THR n 
1 9   LYS n 
1 10  ARG n 
1 11  ASP n 
1 12  GLY n 
1 13  SER n 
1 14  THR n 
1 15  GLU n 
1 16  ARG n 
1 17  ILE n 
1 18  ASN n 
1 19  LEU n 
1 20  ASP n 
1 21  LYS n 
1 22  ILE n 
1 23  HIS n 
1 24  ARG n 
1 25  VAL n 
1 26  LEU n 
1 27  ASP n 
1 28  TRP n 
1 29  ALA n 
1 30  ALA n 
1 31  GLU n 
1 32  GLY n 
1 33  LEU n 
1 34  HIS n 
1 35  ASN n 
1 36  VAL n 
1 37  SER n 
1 38  ILE n 
1 39  SER n 
1 40  GLN n 
1 41  VAL n 
1 42  GLU n 
1 43  LEU n 
1 44  ARG n 
1 45  SER n 
1 46  HIS n 
1 47  ILE n 
1 48  GLN n 
1 49  PHE n 
1 50  TYR n 
1 51  ASP n 
1 52  GLY n 
1 53  ILE n 
1 54  LYS n 
1 55  THR n 
1 56  SER n 
1 57  ASP n 
1 58  ILE n 
1 59  HIS n 
1 60  GLU n 
1 61  THR n 
1 62  ILE n 
1 63  ILE n 
1 64  LYS n 
1 65  ALA n 
1 66  ALA n 
1 67  ALA n 
1 68  ASP n 
1 69  LEU n 
1 70  ILE n 
1 71  SER n 
1 72  ARG n 
1 73  ASP n 
1 74  ALA n 
1 75  PRO n 
1 76  ASP n 
1 77  TYR n 
1 78  GLN n 
1 79  TYR n 
1 80  LEU n 
1 81  ALA n 
1 82  ALA n 
1 83  ARG n 
1 84  LEU n 
1 85  ALA n 
1 86  ILE n 
1 87  PHE n 
1 88  HIS n 
1 89  LEU n 
1 90  ARG n 
1 91  LYS n 
1 92  LYS n 
1 93  ALA n 
1 94  TYR n 
1 95  GLY n 
1 96  GLN n 
1 97  PHE n 
1 98  GLU n 
1 99  PRO n 
1 100 PRO n 
1 101 ALA n 
1 102 LEU n 
1 103 TYR n 
1 104 ASP n 
1 105 HIS n 
1 106 VAL n 
1 107 VAL n 
1 108 LYS n 
1 109 MET n 
1 110 VAL n 
1 111 GLU n 
1 112 MET n 
1 113 GLY n 
1 114 LYS n 
1 115 TYR n 
1 116 ASP n 
1 117 ASN n 
1 118 HIS n 
1 119 LEU n 
1 120 LEU n 
1 121 GLU n 
1 122 ASP n 
1 123 TYR n 
1 124 THR n 
1 125 GLU n 
1 126 GLU n 
1 127 GLU n 
1 128 PHE n 
1 129 LYS n 
1 130 GLN n 
1 131 MET n 
1 132 ASP n 
1 133 THR n 
1 134 PHE n 
1 135 ILE n 
1 136 ASP n 
1 137 HIS n 
1 138 ASP n 
1 139 ARG n 
1 140 ASP n 
1 141 MET n 
1 142 THR n 
1 143 PHE n 
1 144 SER n 
1 145 TYR n 
1 146 ALA n 
1 147 ALA n 
1 148 VAL n 
1 149 LYS n 
1 150 GLN n 
1 151 LEU n 
1 152 GLU n 
1 153 GLY n 
1 154 LYS n 
1 155 TYR n 
1 156 LEU n 
1 157 VAL n 
1 158 GLN n 
1 159 ASN n 
1 160 ARG n 
1 161 VAL n 
1 162 THR n 
1 163 GLY n 
1 164 GLU n 
1 165 ILE n 
1 166 TYR n 
1 167 GLU n 
1 168 SER n 
1 169 ALA n 
1 170 GLN n 
1 171 PHE n 
1 172 LEU n 
1 173 TYR n 
1 174 ILE n 
1 175 LEU n 
1 176 VAL n 
1 177 ALA n 
1 178 ALA n 
1 179 CYS n 
1 180 LEU n 
1 181 PHE n 
1 182 SER n 
1 183 ASN n 
1 184 TYR n 
1 185 PRO n 
1 186 ARG n 
1 187 GLU n 
1 188 THR n 
1 189 ARG n 
1 190 LEU n 
1 191 GLN n 
1 192 TYR n 
1 193 VAL n 
1 194 LYS n 
1 195 ARG n 
1 196 PHE n 
1 197 TYR n 
1 198 ASP n 
1 199 ALA n 
1 200 VAL n 
1 201 SER n 
1 202 THR n 
1 203 PHE n 
1 204 LYS n 
1 205 ILE n 
1 206 SER n 
1 207 LEU n 
1 208 PRO n 
1 209 THR n 
1 210 PRO n 
1 211 ILE n 
1 212 MET n 
1 213 SER n 
1 214 GLY n 
1 215 VAL n 
1 216 ARG n 
1 217 THR n 
1 218 PRO n 
1 219 THR n 
1 220 ARG n 
1 221 GLN n 
1 222 PHE n 
1 223 SER n 
1 224 SER n 
1 225 CYS n 
1 226 VAL n 
1 227 LEU n 
1 228 ILE n 
1 229 GLU n 
1 230 CYS n 
1 231 GLY n 
1 232 ASP n 
1 233 SER n 
1 234 LEU n 
1 235 ASP n 
1 236 SER n 
1 237 ILE n 
1 238 ASN n 
1 239 ALA n 
1 240 THR n 
1 241 SER n 
1 242 SER n 
1 243 ALA n 
1 244 ILE n 
1 245 VAL n 
1 246 LYS n 
1 247 TYR n 
1 248 VAL n 
1 249 SER n 
1 250 GLN n 
1 251 ARG n 
1 252 ALA n 
1 253 GLY n 
1 254 ILE n 
1 255 GLY n 
1 256 ILE n 
1 257 ASN n 
1 258 ALA n 
1 259 GLY n 
1 260 ARG n 
1 261 ILE n 
1 262 ARG n 
1 263 ALA n 
1 264 LEU n 
1 265 GLY n 
1 266 SER n 
1 267 PRO n 
1 268 ILE n 
1 269 ARG n 
1 270 GLY n 
1 271 GLY n 
1 272 GLU n 
1 273 ALA n 
1 274 PHE n 
1 275 HIS n 
1 276 THR n 
1 277 GLY n 
1 278 CYS n 
1 279 ILE n 
1 280 PRO n 
1 281 PHE n 
1 282 TYR n 
1 283 LYS n 
1 284 HIS n 
1 285 PHE n 
1 286 GLN n 
1 287 THR n 
1 288 ALA n 
1 289 VAL n 
1 290 LYS n 
1 291 SER n 
1 292 CYS n 
1 293 SER n 
1 294 GLN n 
1 295 GLY n 
1 296 GLY n 
1 297 VAL n 
1 298 ARG n 
1 299 GLY n 
1 300 GLY n 
1 301 ALA n 
1 302 ALA n 
1 303 THR n 
1 304 LEU n 
1 305 PHE n 
1 306 TYR n 
1 307 PRO n 
1 308 MET n 
1 309 TRP n 
1 310 HIS n 
1 311 LEU n 
1 312 GLU n 
1 313 VAL n 
1 314 GLU n 
1 315 SER n 
1 316 LEU n 
1 317 LEU n 
1 318 VAL n 
1 319 LEU n 
1 320 LYS n 
1 321 ASN n 
1 322 ASN n 
1 323 ARG n 
1 324 GLY n 
1 325 VAL n 
1 326 GLU n 
1 327 GLY n 
1 328 ASN n 
1 329 ARG n 
1 330 VAL n 
1 331 ARG n 
1 332 HIS n 
1 333 MET n 
1 334 ASP n 
1 335 TYR n 
1 336 GLY n 
1 337 VAL n 
1 338 GLN n 
1 339 ILE n 
1 340 ASN n 
1 341 LYS n 
1 342 LEU n 
1 343 MET n 
1 344 TYR n 
1 345 THR n 
1 346 ARG n 
1 347 LEU n 
1 348 LEU n 
1 349 LYS n 
1 350 GLY n 
1 351 GLU n 
1 352 ASP n 
1 353 ILE n 
1 354 THR n 
1 355 LEU n 
1 356 PHE n 
1 357 SER n 
1 358 PRO n 
1 359 SER n 
1 360 ASP n 
1 361 VAL n 
1 362 PRO n 
1 363 GLY n 
1 364 LEU n 
1 365 TYR n 
1 366 ASP n 
1 367 ALA n 
1 368 PHE n 
1 369 PHE n 
1 370 ALA n 
1 371 ASP n 
1 372 GLN n 
1 373 GLU n 
1 374 GLU n 
1 375 PHE n 
1 376 GLU n 
1 377 ARG n 
1 378 LEU n 
1 379 TYR n 
1 380 THR n 
1 381 LYS n 
1 382 TYR n 
1 383 GLU n 
1 384 LYS n 
1 385 ASP n 
1 386 ASP n 
1 387 SER n 
1 388 ILE n 
1 389 ARG n 
1 390 LYS n 
1 391 GLN n 
1 392 ARG n 
1 393 VAL n 
1 394 LYS n 
1 395 ALA n 
1 396 VAL n 
1 397 GLU n 
1 398 LEU n 
1 399 PHE n 
1 400 SER n 
1 401 LEU n 
1 402 MET n 
1 403 MET n 
1 404 GLN n 
1 405 GLU n 
1 406 ARG n 
1 407 ALA n 
1 408 SER n 
1 409 THR n 
1 410 GLY n 
1 411 ARG n 
1 412 ILE n 
1 413 TYR n 
1 414 ILE n 
1 415 GLN n 
1 416 ASN n 
1 417 VAL n 
1 418 ASP n 
1 419 HIS n 
1 420 CYS n 
1 421 ASN n 
1 422 THR n 
1 423 HIS n 
1 424 SER n 
1 425 PRO n 
1 426 PHE n 
1 427 ASP n 
1 428 PRO n 
1 429 ALA n 
1 430 ILE n 
1 431 ALA n 
1 432 PRO n 
1 433 VAL n 
1 434 ARG n 
1 435 GLN n 
1 436 SER n 
1 437 ASN n 
1 438 LEU n 
1 439 CYS n 
1 440 LEU n 
1 441 GLU n 
1 442 ILE n 
1 443 ALA n 
1 444 LEU n 
1 445 PRO n 
1 446 THR n 
1 447 LYS n 
1 448 PRO n 
1 449 LEU n 
1 450 ASN n 
1 451 ASP n 
1 452 VAL n 
1 453 ASN n 
1 454 ASP n 
1 455 GLU n 
1 456 ASN n 
1 457 GLY n 
1 458 GLU n 
1 459 ILE n 
1 460 ALA n 
1 461 LEU n 
1 462 CYS n 
1 463 THR n 
1 464 LEU n 
1 465 SER n 
1 466 ALA n 
1 467 PHE n 
1 468 ASN n 
1 469 LEU n 
1 470 GLY n 
1 471 ALA n 
1 472 ILE n 
1 473 ASN n 
1 474 ASN n 
1 475 LEU n 
1 476 ASP n 
1 477 GLU n 
1 478 LEU n 
1 479 GLU n 
1 480 GLU n 
1 481 LEU n 
1 482 ALA n 
1 483 ILE n 
1 484 LEU n 
1 485 ALA n 
1 486 VAL n 
1 487 ARG n 
1 488 ALA n 
1 489 LEU n 
1 490 ASP n 
1 491 ALA n 
1 492 LEU n 
1 493 LEU n 
1 494 ASP n 
1 495 TYR n 
1 496 GLN n 
1 497 ASP n 
1 498 TYR n 
1 499 PRO n 
1 500 ILE n 
1 501 PRO n 
1 502 ALA n 
1 503 ALA n 
1 504 LYS n 
1 505 ARG n 
1 506 GLY n 
1 507 ALA n 
1 508 MET n 
1 509 GLY n 
1 510 ARG n 
1 511 ARG n 
1 512 THR n 
1 513 LEU n 
1 514 GLY n 
1 515 ILE n 
1 516 GLY n 
1 517 VAL n 
1 518 ILE n 
1 519 ASN n 
1 520 PHE n 
1 521 ALA n 
1 522 TYR n 
1 523 TYR n 
1 524 LEU n 
1 525 ALA n 
1 526 LYS n 
1 527 HIS n 
1 528 GLY n 
1 529 LYS n 
1 530 ARG n 
1 531 TYR n 
1 532 SER n 
1 533 ASP n 
1 534 GLY n 
1 535 SER n 
1 536 ALA n 
1 537 ASN n 
1 538 ASN n 
1 539 LEU n 
1 540 THR n 
1 541 HIS n 
1 542 LYS n 
1 543 THR n 
1 544 PHE n 
1 545 GLU n 
1 546 ALA n 
1 547 ILE n 
1 548 GLN n 
1 549 TYR n 
1 550 TYR n 
1 551 LEU n 
1 552 LEU n 
1 553 LYS n 
1 554 ALA n 
1 555 SER n 
1 556 ASN n 
1 557 GLU n 
1 558 LEU n 
1 559 ALA n 
1 560 LYS n 
1 561 GLU n 
1 562 GLN n 
1 563 GLY n 
1 564 ALA n 
1 565 CYS n 
1 566 PRO n 
1 567 TRP n 
1 568 PHE n 
1 569 ASN n 
1 570 GLU n 
1 571 THR n 
1 572 THR n 
1 573 TYR n 
1 574 ALA n 
1 575 LYS n 
1 576 GLY n 
1 577 ILE n 
1 578 LEU n 
1 579 PRO n 
1 580 ILE n 
1 581 ASP n 
1 582 THR n 
1 583 TYR n 
1 584 LYS n 
1 585 LYS n 
1 586 ASP n 
1 587 LEU n 
1 588 ASP n 
1 589 THR n 
1 590 ILE n 
1 591 ALA n 
1 592 ASN n 
1 593 GLU n 
1 594 PRO n 
1 595 LEU n 
1 596 HIS n 
1 597 TYR n 
1 598 ASP n 
1 599 TRP n 
1 600 GLU n 
1 601 ALA n 
1 602 LEU n 
1 603 ARG n 
1 604 GLU n 
1 605 SER n 
1 606 ILE n 
1 607 LYS n 
1 608 THR n 
1 609 HIS n 
1 610 GLY n 
1 611 LEU n 
1 612 ARG n 
1 613 ASN n 
1 614 SER n 
1 615 THR n 
1 616 LEU n 
1 617 SER n 
1 618 ALA n 
1 619 LEU n 
1 620 MET n 
1 621 PRO n 
1 622 SER n 
1 623 GLU n 
1 624 THR n 
1 625 SER n 
1 626 SER n 
1 627 GLN n 
1 628 ILE n 
1 629 SER n 
1 630 ASN n 
1 631 ALA n 
1 632 THR n 
1 633 ASN n 
1 634 GLY n 
1 635 ILE n 
1 636 GLU n 
1 637 PRO n 
1 638 PRO n 
1 639 ARG n 
1 640 GLY n 
1 641 TYR n 
1 642 VAL n 
1 643 SER n 
1 644 ILE n 
1 645 LYS n 
1 646 ALA n 
1 647 SER n 
1 648 LYS n 
1 649 ASP n 
1 650 GLY n 
1 651 ILE n 
1 652 LEU n 
1 653 ARG n 
1 654 GLN n 
1 655 VAL n 
1 656 VAL n 
1 657 PRO n 
1 658 ASP n 
1 659 TYR n 
1 660 GLU n 
1 661 HIS n 
1 662 LEU n 
1 663 HIS n 
1 664 ASP n 
1 665 ALA n 
1 666 TYR n 
1 667 GLU n 
1 668 LEU n 
1 669 LEU n 
1 670 TRP n 
1 671 GLU n 
1 672 MET n 
1 673 PRO n 
1 674 GLY n 
1 675 ASN n 
1 676 ASP n 
1 677 GLY n 
1 678 TYR n 
1 679 LEU n 
1 680 GLN n 
1 681 LEU n 
1 682 VAL n 
1 683 GLY n 
1 684 ILE n 
1 685 MET n 
1 686 GLN n 
1 687 LYS n 
1 688 PHE n 
1 689 ILE n 
1 690 ASP n 
1 691 GLN n 
1 692 SER n 
1 693 ILE n 
1 694 SER n 
1 695 ALA n 
1 696 ASN n 
1 697 THR n 
1 698 ASN n 
1 699 TYR n 
1 700 ASP n 
1 701 PRO n 
1 702 SER n 
1 703 ARG n 
1 704 PHE n 
1 705 PRO n 
1 706 SER n 
1 707 GLY n 
1 708 LYS n 
1 709 VAL n 
1 710 PRO n 
1 711 MET n 
1 712 GLN n 
1 713 GLN n 
1 714 LEU n 
1 715 LEU n 
1 716 LYS n 
1 717 ASP n 
1 718 LEU n 
1 719 LEU n 
1 720 THR n 
1 721 ALA n 
1 722 TYR n 
1 723 LYS n 
1 724 PHE n 
1 725 GLY n 
1 726 VAL n 
1 727 LYS n 
1 728 THR n 
1 729 LEU n 
1 730 TYR n 
1 731 TYR n 
1 732 GLN n 
1 733 ASN n 
1 734 THR n 
1 735 ARG n 
1 736 ASP n 
1 737 GLY n 
1 738 ALA n 
1 739 GLU n 
1 740 ASP n 
1 741 ALA n 
1 742 GLN n 
1 743 ASP n 
1 744 ASP n 
1 745 LEU n 
1 746 VAL n 
1 747 PRO n 
1 748 SER n 
1 749 ILE n 
1 750 GLN n 
1 751 ASP n 
1 752 ASP n 
1 753 GLY n 
1 754 CYS n 
1 755 GLU n 
1 756 SER n 
1 757 GLY n 
1 758 ALA n 
1 759 CYS n 
1 760 LYS n 
1 761 ILE n 
2 1   MET n 
2 2   ALA n 
2 3   TYR n 
2 4   THR n 
2 5   THR n 
2 6   PHE n 
2 7   SER n 
2 8   GLN n 
2 9   THR n 
2 10  LYS n 
2 11  ASN n 
2 12  ASP n 
2 13  GLN n 
2 14  LEU n 
2 15  LYS n 
2 16  GLU n 
2 17  PRO n 
2 18  MET n 
2 19  PHE n 
2 20  PHE n 
2 21  GLY n 
2 22  GLN n 
2 23  PRO n 
2 24  VAL n 
2 25  ASN n 
2 26  VAL n 
2 27  ALA n 
2 28  ARG n 
2 29  TYR n 
2 30  ASP n 
2 31  GLN n 
2 32  GLN n 
2 33  LYS n 
2 34  TYR n 
2 35  ASP n 
2 36  ILE n 
2 37  PHE n 
2 38  GLU n 
2 39  LYS n 
2 40  LEU n 
2 41  ILE n 
2 42  GLU n 
2 43  LYS n 
2 44  GLN n 
2 45  LEU n 
2 46  SER n 
2 47  PHE n 
2 48  PHE n 
2 49  TRP n 
2 50  ARG n 
2 51  PRO n 
2 52  GLU n 
2 53  GLU n 
2 54  VAL n 
2 55  ASP n 
2 56  VAL n 
2 57  SER n 
2 58  ARG n 
2 59  ASP n 
2 60  ARG n 
2 61  ILE n 
2 62  ASP n 
2 63  TYR n 
2 64  GLN n 
2 65  ALA n 
2 66  LEU n 
2 67  PRO n 
2 68  GLU n 
2 69  HIS n 
2 70  GLU n 
2 71  LYS n 
2 72  HIS n 
2 73  ILE n 
2 74  PHE n 
2 75  ILE n 
2 76  SER n 
2 77  ASN n 
2 78  LEU n 
2 79  LYS n 
2 80  TYR n 
2 81  GLN n 
2 82  THR n 
2 83  LEU n 
2 84  LEU n 
2 85  ASP n 
2 86  SER n 
2 87  ILE n 
2 88  GLN n 
2 89  GLY n 
2 90  ARG n 
2 91  SER n 
2 92  PRO n 
2 93  ASN n 
2 94  VAL n 
2 95  ALA n 
2 96  LEU n 
2 97  LEU n 
2 98  PRO n 
2 99  LEU n 
2 100 ILE n 
2 101 SER n 
2 102 ILE n 
2 103 PRO n 
2 104 GLU n 
2 105 LEU n 
2 106 GLU n 
2 107 THR n 
2 108 TRP n 
2 109 VAL n 
2 110 GLU n 
2 111 THR n 
2 112 TRP n 
2 113 ALA n 
2 114 PHE n 
2 115 SER n 
2 116 GLU n 
2 117 THR n 
2 118 ILE n 
2 119 HIS n 
2 120 SER n 
2 121 ARG n 
2 122 SER n 
2 123 TYR n 
2 124 THR n 
2 125 HIS n 
2 126 ILE n 
2 127 ILE n 
2 128 ARG n 
2 129 ASN n 
2 130 ILE n 
2 131 VAL n 
2 132 ASN n 
2 133 ASP n 
2 134 PRO n 
2 135 SER n 
2 136 VAL n 
2 137 VAL n 
2 138 PHE n 
2 139 ASP n 
2 140 ASP n 
2 141 ILE n 
2 142 VAL n 
2 143 THR n 
2 144 ASN n 
2 145 GLU n 
2 146 GLN n 
2 147 ILE n 
2 148 GLN n 
2 149 LYS n 
2 150 ARG n 
2 151 ALA n 
2 152 GLU n 
2 153 GLY n 
2 154 ILE n 
2 155 SER n 
2 156 SER n 
2 157 TYR n 
2 158 TYR n 
2 159 ASP n 
2 160 GLU n 
2 161 LEU n 
2 162 ILE n 
2 163 GLU n 
2 164 MET n 
2 165 THR n 
2 166 SER n 
2 167 TYR n 
2 168 TRP n 
2 169 HIS n 
2 170 LEU n 
2 171 LEU n 
2 172 GLY n 
2 173 GLU n 
2 174 GLY n 
2 175 THR n 
2 176 HIS n 
2 177 THR n 
2 178 VAL n 
2 179 ASN n 
2 180 GLY n 
2 181 LYS n 
2 182 THR n 
2 183 VAL n 
2 184 THR n 
2 185 VAL n 
2 186 SER n 
2 187 LEU n 
2 188 ARG n 
2 189 GLU n 
2 190 LEU n 
2 191 LYS n 
2 192 LYS n 
2 193 LYS n 
2 194 LEU n 
2 195 TYR n 
2 196 LEU n 
2 197 CYS n 
2 198 LEU n 
2 199 MET n 
2 200 SER n 
2 201 VAL n 
2 202 ASN n 
2 203 ALA n 
2 204 LEU n 
2 205 GLU n 
2 206 ALA n 
2 207 ILE n 
2 208 ARG n 
2 209 PHE n 
2 210 TYR n 
2 211 VAL n 
2 212 SER n 
2 213 PHE n 
2 214 ALA n 
2 215 CYS n 
2 216 SER n 
2 217 PHE n 
2 218 ALA n 
2 219 PHE n 
2 220 ALA n 
2 221 GLU n 
2 222 ARG n 
2 223 GLU n 
2 224 LEU n 
2 225 MET n 
2 226 GLU n 
2 227 GLY n 
2 228 ASN n 
2 229 ALA n 
2 230 LYS n 
2 231 ILE n 
2 232 ILE n 
2 233 ARG n 
2 234 LEU n 
2 235 ILE n 
2 236 ALA n 
2 237 ARG n 
2 238 ASP n 
2 239 GLU n 
2 240 ALA n 
2 241 LEU n 
2 242 HIS n 
2 243 LEU n 
2 244 THR n 
2 245 GLY n 
2 246 THR n 
2 247 GLN n 
2 248 HIS n 
2 249 MET n 
2 250 LEU n 
2 251 ASN n 
2 252 LEU n 
2 253 LEU n 
2 254 ARG n 
2 255 SER n 
2 256 GLY n 
2 257 ALA n 
2 258 ASP n 
2 259 ASP n 
2 260 PRO n 
2 261 GLU n 
2 262 MET n 
2 263 ALA n 
2 264 GLU n 
2 265 ILE n 
2 266 ALA n 
2 267 GLU n 
2 268 GLU n 
2 269 CYS n 
2 270 LYS n 
2 271 GLN n 
2 272 GLU n 
2 273 CYS n 
2 274 TYR n 
2 275 ASP n 
2 276 LEU n 
2 277 PHE n 
2 278 VAL n 
2 279 GLN n 
2 280 ALA n 
2 281 ALA n 
2 282 GLN n 
2 283 GLN n 
2 284 GLU n 
2 285 LYS n 
2 286 ASP n 
2 287 TRP n 
2 288 ALA n 
2 289 ASP n 
2 290 TYR n 
2 291 LEU n 
2 292 PHE n 
2 293 ARG n 
2 294 ASP n 
2 295 GLY n 
2 296 SER n 
2 297 MET n 
2 298 ILE n 
2 299 GLY n 
2 300 LEU n 
2 301 ASN n 
2 302 LYS n 
2 303 ASP n 
2 304 ILE n 
2 305 LEU n 
2 306 CYS n 
2 307 GLN n 
2 308 TYR n 
2 309 VAL n 
2 310 GLU n 
2 311 TYR n 
2 312 ILE n 
2 313 THR n 
2 314 ASN n 
2 315 ILE n 
2 316 ARG n 
2 317 MET n 
2 318 GLN n 
2 319 ALA n 
2 320 VAL n 
2 321 GLY n 
2 322 LEU n 
2 323 ASP n 
2 324 LEU n 
2 325 PRO n 
2 326 PHE n 
2 327 GLN n 
2 328 THR n 
2 329 ARG n 
2 330 SER n 
2 331 ASN n 
2 332 PRO n 
2 333 ILE n 
2 334 PRO n 
2 335 TRP n 
2 336 ILE n 
2 337 ASN n 
2 338 THR n 
2 339 TRP n 
2 340 LEU n 
2 341 VAL n 
2 342 SER n 
2 343 ASP n 
2 344 ASN n 
2 345 VAL n 
2 346 GLN n 
2 347 VAL n 
2 348 ALA n 
2 349 PRO n 
2 350 GLN n 
2 351 GLU n 
2 352 VAL n 
2 353 GLU n 
2 354 VAL n 
2 355 SER n 
2 356 SER n 
2 357 TYR n 
2 358 LEU n 
2 359 VAL n 
2 360 GLY n 
2 361 GLN n 
2 362 ILE n 
2 363 ASP n 
2 364 SER n 
2 365 GLU n 
2 366 VAL n 
2 367 ASP n 
2 368 THR n 
2 369 ASP n 
2 370 ASP n 
2 371 LEU n 
2 372 SER n 
2 373 ASN n 
2 374 PHE n 
2 375 GLN n 
2 376 LEU 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' 1 761 ? ? 'nrdA, dnaF, b2234, JW2228' ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 376 ? ? 'nrdB, ftsB, b2235, JW2229' ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1A3L non-polymer         . 
'4-amino-1-{(3xi)-3-C-amino-2-deoxy-5-O-[(S)-hydroxy(phosphonooxy)phosphoryl]-beta-D-threo-pentofuranosyl}pyrimidin-2(1H)-one' ? 
'C9 H16 N4 O10 P2'  402.192 
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 
ATP   non-polymer         . "ADENOSINE-5'-TRIPHOSPHATE" ? 'C10 H16 N5 O13 P3' 507.181 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'      121.158 
DTP   non-polymer         . 
;2'-DEOXYADENOSINE 5'-TRIPHOSPHATE
;
? 'C10 H16 N5 O12 P3' 491.182 
FEO   non-polymer         . MU-OXO-DIIRON ? 'Fe2 O'             127.689 
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 
MG    non-polymer         . 'MAGNESIUM ION' ? 'Mg 2'              24.305  
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 
UNL   non-polymer         . 'UNKNOWN LIGAND' ? ?                   ?       
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'       117.146 
# 
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   1   ?   ?   ?   A . n 
A 1 2   ASN 2   2   ?   ?   ?   A . n 
A 1 3   GLN 3   3   ?   ?   ?   A . n 
A 1 4   ASN 4   4   ?   ?   ?   A . n 
A 1 5   LEU 5   5   ?   ?   ?   A . n 
A 1 6   LEU 6   6   ?   ?   ?   A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   THR 8   8   8   THR THR A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  ARG 10  10  10  ARG ARG A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  SER 13  13  13  SER SER A . n 
A 1 14  THR 14  14  14  THR THR A . n 
A 1 15  GLU 15  15  15  GLU GLU A . n 
A 1 16  ARG 16  16  16  ARG ARG A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  ASN 18  18  18  ASN ASN A . n 
A 1 19  LEU 19  19  19  LEU LEU A . n 
A 1 20  ASP 20  20  20  ASP ASP A . n 
A 1 21  LYS 21  21  21  LYS LYS A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  HIS 23  23  23  HIS HIS A . n 
A 1 24  ARG 24  24  24  ARG ARG A . n 
A 1 25  VAL 25  25  25  VAL VAL A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  ASP 27  27  27  ASP ASP A . n 
A 1 28  TRP 28  28  28  TRP TRP A . n 
A 1 29  ALA 29  29  29  ALA ALA A . n 
A 1 30  ALA 30  30  30  ALA ALA A . n 
A 1 31  GLU 31  31  31  GLU GLU A . n 
A 1 32  GLY 32  32  32  GLY GLY A . n 
A 1 33  LEU 33  33  33  LEU LEU A . n 
A 1 34  HIS 34  34  34  HIS HIS A . n 
A 1 35  ASN 35  35  35  ASN ASN A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  SER 37  37  37  SER SER A . n 
A 1 38  ILE 38  38  38  ILE ILE A . n 
A 1 39  SER 39  39  39  SER SER A . n 
A 1 40  GLN 40  40  40  GLN GLN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  GLU 42  42  42  GLU GLU A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  ARG 44  44  44  ARG ARG A . n 
A 1 45  SER 45  45  45  SER SER A . n 
A 1 46  HIS 46  46  46  HIS HIS A . n 
A 1 47  ILE 47  47  47  ILE ILE A . n 
A 1 48  GLN 48  48  48  GLN GLN A . n 
A 1 49  PHE 49  49  49  PHE PHE A . n 
A 1 50  TYR 50  50  50  TYR TYR A . n 
A 1 51  ASP 51  51  51  ASP ASP A . n 
A 1 52  GLY 52  52  52  GLY GLY A . n 
A 1 53  ILE 53  53  53  ILE ILE A . n 
A 1 54  LYS 54  54  54  LYS LYS A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  ASP 57  57  57  ASP ASP A . n 
A 1 58  ILE 58  58  58  ILE ILE A . n 
A 1 59  HIS 59  59  59  HIS HIS A . n 
A 1 60  GLU 60  60  60  GLU GLU A . n 
A 1 61  THR 61  61  61  THR THR A . n 
A 1 62  ILE 62  62  62  ILE ILE A . n 
A 1 63  ILE 63  63  63  ILE ILE A . n 
A 1 64  LYS 64  64  64  LYS LYS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  ALA 66  66  66  ALA ALA A . n 
A 1 67  ALA 67  67  67  ALA ALA A . n 
A 1 68  ASP 68  68  68  ASP ASP A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  ILE 70  70  70  ILE ILE A . n 
A 1 71  SER 71  71  71  SER SER A . n 
A 1 72  ARG 72  72  72  ARG ARG A . n 
A 1 73  ASP 73  73  73  ASP ASP A . n 
A 1 74  ALA 74  74  74  ALA ALA A . n 
A 1 75  PRO 75  75  75  PRO PRO A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  TYR 77  77  77  TYR TYR A . n 
A 1 78  GLN 78  78  78  GLN GLN A . n 
A 1 79  TYR 79  79  79  TYR TYR A . n 
A 1 80  LEU 80  80  80  LEU LEU A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  ARG 83  83  83  ARG ARG A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ALA 85  85  85  ALA ALA A . n 
A 1 86  ILE 86  86  86  ILE ILE A . n 
A 1 87  PHE 87  87  87  PHE PHE A . n 
A 1 88  HIS 88  88  88  HIS HIS A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  ARG 90  90  90  ARG ARG A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  LYS 92  92  92  LYS LYS A . n 
A 1 93  ALA 93  93  93  ALA ALA A . n 
A 1 94  TYR 94  94  94  TYR TYR A . n 
A 1 95  GLY 95  95  95  GLY GLY A . n 
A 1 96  GLN 96  96  96  GLN GLN A . n 
A 1 97  PHE 97  97  97  PHE PHE A . n 
A 1 98  GLU 98  98  98  GLU GLU A . n 
A 1 99  PRO 99  99  99  PRO PRO A . n 
A 1 100 PRO 100 100 100 PRO PRO A . n 
A 1 101 ALA 101 101 101 ALA ALA A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 TYR 103 103 103 TYR TYR A . n 
A 1 104 ASP 104 104 104 ASP ASP A . n 
A 1 105 HIS 105 105 105 HIS HIS A . n 
A 1 106 VAL 106 106 106 VAL VAL A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 LYS 108 108 108 LYS LYS A . n 
A 1 109 MET 109 109 109 MET MET A . n 
A 1 110 VAL 110 110 110 VAL VAL A . n 
A 1 111 GLU 111 111 111 GLU GLU A . n 
A 1 112 MET 112 112 112 MET MET A . n 
A 1 113 GLY 113 113 113 GLY GLY A . n 
A 1 114 LYS 114 114 114 LYS LYS A . n 
A 1 115 TYR 115 115 115 TYR TYR A . n 
A 1 116 ASP 116 116 116 ASP ASP A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 HIS 118 118 118 HIS HIS A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 ASP 122 122 122 ASP ASP A . n 
A 1 123 TYR 123 123 123 TYR TYR A . n 
A 1 124 THR 124 124 124 THR THR A . n 
A 1 125 GLU 125 125 125 GLU GLU A . n 
A 1 126 GLU 126 126 126 GLU GLU A . n 
A 1 127 GLU 127 127 127 GLU GLU A . n 
A 1 128 PHE 128 128 128 PHE PHE A . n 
A 1 129 LYS 129 129 129 LYS LYS A . n 
A 1 130 GLN 130 130 130 GLN GLN A . n 
A 1 131 MET 131 131 131 MET MET A . n 
A 1 132 ASP 132 132 132 ASP ASP A . n 
A 1 133 THR 133 133 133 THR THR A . n 
A 1 134 PHE 134 134 134 PHE PHE A . n 
A 1 135 ILE 135 135 135 ILE ILE A . n 
A 1 136 ASP 136 136 136 ASP ASP A . n 
A 1 137 HIS 137 137 137 HIS HIS A . n 
A 1 138 ASP 138 138 138 ASP ASP A . n 
A 1 139 ARG 139 139 139 ARG ARG A . n 
A 1 140 ASP 140 140 140 ASP ASP A . n 
A 1 141 MET 141 141 141 MET MET A . n 
A 1 142 THR 142 142 142 THR THR A . n 
A 1 143 PHE 143 143 143 PHE PHE A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 TYR 145 145 145 TYR TYR A . n 
A 1 146 ALA 146 146 146 ALA ALA A . n 
A 1 147 ALA 147 147 147 ALA ALA A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 LYS 149 149 149 LYS LYS A . n 
A 1 150 GLN 150 150 150 GLN GLN A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 GLU 152 152 152 GLU GLU A . n 
A 1 153 GLY 153 153 153 GLY GLY A . n 
A 1 154 LYS 154 154 154 LYS LYS A . n 
A 1 155 TYR 155 155 155 TYR TYR A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 GLN 158 158 158 GLN GLN A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 ARG 160 160 160 ARG ARG A . n 
A 1 161 VAL 161 161 161 VAL VAL A . n 
A 1 162 THR 162 162 162 THR THR A . n 
A 1 163 GLY 163 163 163 GLY GLY A . n 
A 1 164 GLU 164 164 164 GLU GLU A . n 
A 1 165 ILE 165 165 165 ILE ILE A . n 
A 1 166 TYR 166 166 166 TYR TYR A . n 
A 1 167 GLU 167 167 167 GLU GLU A . n 
A 1 168 SER 168 168 168 SER SER A . n 
A 1 169 ALA 169 169 169 ALA ALA A . n 
A 1 170 GLN 170 170 170 GLN GLN A . n 
A 1 171 PHE 171 171 171 PHE PHE A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 TYR 173 173 173 TYR TYR A . n 
A 1 174 ILE 174 174 174 ILE ILE A . n 
A 1 175 LEU 175 175 175 LEU LEU A . n 
A 1 176 VAL 176 176 176 VAL VAL A . n 
A 1 177 ALA 177 177 177 ALA ALA A . n 
A 1 178 ALA 178 178 178 ALA ALA A . n 
A 1 179 CYS 179 179 179 CYS CYS A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 SER 182 182 182 SER SER A . n 
A 1 183 ASN 183 183 183 ASN ASN A . n 
A 1 184 TYR 184 184 184 TYR TYR A . n 
A 1 185 PRO 185 185 185 PRO PRO A . n 
A 1 186 ARG 186 186 186 ARG ARG A . n 
A 1 187 GLU 187 187 187 GLU GLU A . n 
A 1 188 THR 188 188 188 THR THR A . n 
A 1 189 ARG 189 189 189 ARG ARG A . n 
A 1 190 LEU 190 190 190 LEU LEU A . n 
A 1 191 GLN 191 191 191 GLN GLN A . n 
A 1 192 TYR 192 192 192 TYR TYR A . n 
A 1 193 VAL 193 193 193 VAL VAL A . n 
A 1 194 LYS 194 194 194 LYS LYS A . n 
A 1 195 ARG 195 195 195 ARG ARG A . n 
A 1 196 PHE 196 196 196 PHE PHE A . n 
A 1 197 TYR 197 197 197 TYR TYR A . n 
A 1 198 ASP 198 198 198 ASP ASP A . n 
A 1 199 ALA 199 199 199 ALA ALA A . n 
A 1 200 VAL 200 200 200 VAL VAL A . n 
A 1 201 SER 201 201 201 SER SER A . n 
A 1 202 THR 202 202 202 THR THR A . n 
A 1 203 PHE 203 203 203 PHE PHE A . n 
A 1 204 LYS 204 204 204 LYS LYS A . n 
A 1 205 ILE 205 205 205 ILE ILE A . n 
A 1 206 SER 206 206 206 SER SER A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 PRO 208 208 208 PRO PRO A . n 
A 1 209 THR 209 209 209 THR THR A . n 
A 1 210 PRO 210 210 210 PRO PRO A . n 
A 1 211 ILE 211 211 211 ILE ILE A . n 
A 1 212 MET 212 212 212 MET MET A . n 
A 1 213 SER 213 213 213 SER SER A . n 
A 1 214 GLY 214 214 214 GLY GLY A . n 
A 1 215 VAL 215 215 215 VAL VAL A . n 
A 1 216 ARG 216 216 216 ARG ARG A . n 
A 1 217 THR 217 217 217 THR THR A . n 
A 1 218 PRO 218 218 218 PRO PRO A . n 
A 1 219 THR 219 219 219 THR THR A . n 
A 1 220 ARG 220 220 220 ARG ARG A . n 
A 1 221 GLN 221 221 221 GLN GLN A . n 
A 1 222 PHE 222 222 222 PHE PHE A . n 
A 1 223 SER 223 223 223 SER SER A . n 
A 1 224 SER 224 224 224 SER SER A . n 
A 1 225 CYS 225 225 225 CYS CYS A . n 
A 1 226 VAL 226 226 226 VAL VAL A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 ILE 228 228 228 ILE ILE A . n 
A 1 229 GLU 229 229 229 GLU GLU A . n 
A 1 230 CYS 230 230 230 CYS CYS A . n 
A 1 231 GLY 231 231 231 GLY GLY A . n 
A 1 232 ASP 232 232 232 ASP ASP A . n 
A 1 233 SER 233 233 233 SER SER A . n 
A 1 234 LEU 234 234 234 LEU LEU A . n 
A 1 235 ASP 235 235 235 ASP ASP A . n 
A 1 236 SER 236 236 236 SER SER A . n 
A 1 237 ILE 237 237 237 ILE ILE A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 ALA 239 239 239 ALA ALA A . n 
A 1 240 THR 240 240 240 THR THR A . n 
A 1 241 SER 241 241 241 SER SER A . n 
A 1 242 SER 242 242 242 SER SER A . n 
A 1 243 ALA 243 243 243 ALA ALA A . n 
A 1 244 ILE 244 244 244 ILE ILE A . n 
A 1 245 VAL 245 245 245 VAL VAL A . n 
A 1 246 LYS 246 246 246 LYS LYS A . n 
A 1 247 TYR 247 247 247 TYR TYR A . n 
A 1 248 VAL 248 248 248 VAL VAL A . n 
A 1 249 SER 249 249 249 SER SER A . n 
A 1 250 GLN 250 250 250 GLN GLN A . n 
A 1 251 ARG 251 251 251 ARG ARG A . n 
A 1 252 ALA 252 252 252 ALA ALA A . n 
A 1 253 GLY 253 253 253 GLY GLY A . n 
A 1 254 ILE 254 254 254 ILE ILE A . n 
A 1 255 GLY 255 255 255 GLY GLY A . n 
A 1 256 ILE 256 256 256 ILE ILE A . n 
A 1 257 ASN 257 257 257 ASN ASN A . n 
A 1 258 ALA 258 258 258 ALA ALA A . n 
A 1 259 GLY 259 259 259 GLY GLY A . n 
A 1 260 ARG 260 260 260 ARG ARG A . n 
A 1 261 ILE 261 261 261 ILE ILE A . n 
A 1 262 ARG 262 262 262 ARG ARG A . n 
A 1 263 ALA 263 263 263 ALA ALA A . n 
A 1 264 LEU 264 264 264 LEU LEU A . n 
A 1 265 GLY 265 265 265 GLY GLY A . n 
A 1 266 SER 266 266 266 SER SER A . n 
A 1 267 PRO 267 267 267 PRO PRO A . n 
A 1 268 ILE 268 268 268 ILE ILE A . n 
A 1 269 ARG 269 269 269 ARG ARG A . n 
A 1 270 GLY 270 270 270 GLY GLY A . n 
A 1 271 GLY 271 271 271 GLY GLY A . n 
A 1 272 GLU 272 272 272 GLU GLU A . n 
A 1 273 ALA 273 273 273 ALA ALA A . n 
A 1 274 PHE 274 274 274 PHE PHE A . n 
A 1 275 HIS 275 275 275 HIS HIS A . n 
A 1 276 THR 276 276 276 THR THR A . n 
A 1 277 GLY 277 277 277 GLY GLY A . n 
A 1 278 CYS 278 278 278 CYS CYS A . n 
A 1 279 ILE 279 279 279 ILE ILE A . n 
A 1 280 PRO 280 280 280 PRO PRO A . n 
A 1 281 PHE 281 281 281 PHE PHE A . n 
A 1 282 TYR 282 282 282 TYR TYR A . n 
A 1 283 LYS 283 283 283 LYS LYS A . n 
A 1 284 HIS 284 284 284 HIS HIS A . n 
A 1 285 PHE 285 285 285 PHE PHE A . n 
A 1 286 GLN 286 286 286 GLN GLN A . n 
A 1 287 THR 287 287 287 THR THR A . n 
A 1 288 ALA 288 288 288 ALA ALA A . n 
A 1 289 VAL 289 289 289 VAL VAL A . n 
A 1 290 LYS 290 290 290 LYS LYS A . n 
A 1 291 SER 291 291 291 SER SER A . n 
A 1 292 CYS 292 292 292 CYS CYS A . n 
A 1 293 SER 293 293 293 SER SER A . n 
A 1 294 GLN 294 294 294 GLN GLN A . n 
A 1 295 GLY 295 295 295 GLY GLY A . n 
A 1 296 GLY 296 296 296 GLY GLY A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 ARG 298 298 298 ARG ARG A . n 
A 1 299 GLY 299 299 299 GLY GLY A . n 
A 1 300 GLY 300 300 300 GLY GLY A . n 
A 1 301 ALA 301 301 301 ALA ALA A . n 
A 1 302 ALA 302 302 302 ALA ALA A . n 
A 1 303 THR 303 303 303 THR THR A . n 
A 1 304 LEU 304 304 304 LEU LEU A . n 
A 1 305 PHE 305 305 305 PHE PHE A . n 
A 1 306 TYR 306 306 306 TYR TYR A . n 
A 1 307 PRO 307 307 307 PRO PRO A . n 
A 1 308 MET 308 308 308 MET MET A . n 
A 1 309 TRP 309 309 309 TRP TRP A . n 
A 1 310 HIS 310 310 310 HIS HIS A . n 
A 1 311 LEU 311 311 311 LEU LEU A . n 
A 1 312 GLU 312 312 312 GLU GLU A . n 
A 1 313 VAL 313 313 313 VAL VAL A . n 
A 1 314 GLU 314 314 314 GLU GLU A . n 
A 1 315 SER 315 315 315 SER SER A . n 
A 1 316 LEU 316 316 316 LEU LEU A . n 
A 1 317 LEU 317 317 317 LEU LEU A . n 
A 1 318 VAL 318 318 318 VAL VAL A . n 
A 1 319 LEU 319 319 319 LEU LEU A . n 
A 1 320 LYS 320 320 320 LYS LYS A . n 
A 1 321 ASN 321 321 321 ASN ASN A . n 
A 1 322 ASN 322 322 322 ASN ASN A . n 
A 1 323 ARG 323 323 323 ARG ARG A . n 
A 1 324 GLY 324 324 324 GLY GLY A . n 
A 1 325 VAL 325 325 325 VAL VAL A . n 
A 1 326 GLU 326 326 326 GLU GLU A . n 
A 1 327 GLY 327 327 327 GLY GLY A . n 
A 1 328 ASN 328 328 328 ASN ASN A . n 
A 1 329 ARG 329 329 329 ARG ARG A . n 
A 1 330 VAL 330 330 330 VAL VAL A . n 
A 1 331 ARG 331 331 331 ARG ARG A . n 
A 1 332 HIS 332 332 332 HIS HIS A . n 
A 1 333 MET 333 333 333 MET MET A . n 
A 1 334 ASP 334 334 334 ASP ASP A . n 
A 1 335 TYR 335 335 335 TYR TYR A . n 
A 1 336 GLY 336 336 336 GLY GLY A . n 
A 1 337 VAL 337 337 337 VAL VAL A . n 
A 1 338 GLN 338 338 338 GLN GLN A . n 
A 1 339 ILE 339 339 339 ILE ILE A . n 
A 1 340 ASN 340 340 340 ASN ASN A . n 
A 1 341 LYS 341 341 341 LYS LYS A . n 
A 1 342 LEU 342 342 342 LEU LEU A . n 
A 1 343 MET 343 343 343 MET MET A . n 
A 1 344 TYR 344 344 344 TYR TYR A . n 
A 1 345 THR 345 345 345 THR THR A . n 
A 1 346 ARG 346 346 346 ARG ARG A . n 
A 1 347 LEU 347 347 347 LEU LEU A . n 
A 1 348 LEU 348 348 348 LEU LEU A . n 
A 1 349 LYS 349 349 349 LYS LYS A . n 
A 1 350 GLY 350 350 350 GLY GLY A . n 
A 1 351 GLU 351 351 351 GLU GLU A . n 
A 1 352 ASP 352 352 352 ASP ASP A . n 
A 1 353 ILE 353 353 353 ILE ILE A . n 
A 1 354 THR 354 354 354 THR THR A . n 
A 1 355 LEU 355 355 355 LEU LEU A . n 
A 1 356 PHE 356 356 356 PHE PHE A . n 
A 1 357 SER 357 357 357 SER SER A . n 
A 1 358 PRO 358 358 358 PRO PRO A . n 
A 1 359 SER 359 359 359 SER SER A . n 
A 1 360 ASP 360 360 360 ASP ASP A . n 
A 1 361 VAL 361 361 361 VAL VAL A . n 
A 1 362 PRO 362 362 362 PRO PRO A . n 
A 1 363 GLY 363 363 363 GLY GLY A . n 
A 1 364 LEU 364 364 364 LEU LEU A . n 
A 1 365 TYR 365 365 365 TYR TYR A . n 
A 1 366 ASP 366 366 366 ASP ASP A . n 
A 1 367 ALA 367 367 367 ALA ALA A . n 
A 1 368 PHE 368 368 368 PHE PHE A . n 
A 1 369 PHE 369 369 369 PHE PHE A . n 
A 1 370 ALA 370 370 370 ALA ALA A . n 
A 1 371 ASP 371 371 371 ASP ASP A . n 
A 1 372 GLN 372 372 372 GLN GLN A . n 
A 1 373 GLU 373 373 373 GLU GLU A . n 
A 1 374 GLU 374 374 374 GLU GLU A . n 
A 1 375 PHE 375 375 375 PHE PHE A . n 
A 1 376 GLU 376 376 376 GLU GLU A . n 
A 1 377 ARG 377 377 377 ARG ARG A . n 
A 1 378 LEU 378 378 378 LEU LEU A . n 
A 1 379 TYR 379 379 379 TYR TYR A . n 
A 1 380 THR 380 380 380 THR THR A . n 
A 1 381 LYS 381 381 381 LYS LYS A . n 
A 1 382 TYR 382 382 382 TYR TYR A . n 
A 1 383 GLU 383 383 383 GLU GLU A . n 
A 1 384 LYS 384 384 384 LYS LYS A . n 
A 1 385 ASP 385 385 385 ASP ASP A . n 
A 1 386 ASP 386 386 386 ASP ASP A . n 
A 1 387 SER 387 387 387 SER SER A . n 
A 1 388 ILE 388 388 388 ILE ILE A . n 
A 1 389 ARG 389 389 389 ARG ARG A . n 
A 1 390 LYS 390 390 390 LYS LYS A . n 
A 1 391 GLN 391 391 391 GLN GLN A . n 
A 1 392 ARG 392 392 392 ARG ARG A . n 
A 1 393 VAL 393 393 393 VAL VAL A . n 
A 1 394 LYS 394 394 394 LYS LYS A . n 
A 1 395 ALA 395 395 395 ALA ALA A . n 
A 1 396 VAL 396 396 396 VAL VAL A . n 
A 1 397 GLU 397 397 397 GLU GLU A . n 
A 1 398 LEU 398 398 398 LEU LEU A . n 
A 1 399 PHE 399 399 399 PHE PHE A . n 
A 1 400 SER 400 400 400 SER SER A . n 
A 1 401 LEU 401 401 401 LEU LEU A . n 
A 1 402 MET 402 402 402 MET MET A . n 
A 1 403 MET 403 403 403 MET MET A . n 
A 1 404 GLN 404 404 404 GLN GLN A . n 
A 1 405 GLU 405 405 405 GLU GLU A . n 
A 1 406 ARG 406 406 406 ARG ARG A . n 
A 1 407 ALA 407 407 407 ALA ALA A . n 
A 1 408 SER 408 408 408 SER SER A . n 
A 1 409 THR 409 409 409 THR THR A . n 
A 1 410 GLY 410 410 410 GLY GLY A . n 
A 1 411 ARG 411 411 411 ARG ARG A . n 
A 1 412 ILE 412 412 412 ILE ILE A . n 
A 1 413 TYR 413 413 413 TYR TYR A . n 
A 1 414 ILE 414 414 414 ILE ILE A . n 
A 1 415 GLN 415 415 415 GLN GLN A . n 
A 1 416 ASN 416 416 416 ASN ASN A . n 
A 1 417 VAL 417 417 417 VAL VAL A . n 
A 1 418 ASP 418 418 418 ASP ASP A . n 
A 1 419 HIS 419 419 419 HIS HIS A . n 
A 1 420 CYS 420 420 420 CYS CYS A . n 
A 1 421 ASN 421 421 421 ASN ASN A . n 
A 1 422 THR 422 422 422 THR THR A . n 
A 1 423 HIS 423 423 423 HIS HIS A . n 
A 1 424 SER 424 424 424 SER SER A . n 
A 1 425 PRO 425 425 425 PRO PRO A . n 
A 1 426 PHE 426 426 426 PHE PHE A . n 
A 1 427 ASP 427 427 427 ASP ASP A . n 
A 1 428 PRO 428 428 428 PRO PRO A . n 
A 1 429 ALA 429 429 429 ALA ALA A . n 
A 1 430 ILE 430 430 430 ILE ILE A . n 
A 1 431 ALA 431 431 431 ALA ALA A . n 
A 1 432 PRO 432 432 432 PRO PRO A . n 
A 1 433 VAL 433 433 433 VAL VAL A . n 
A 1 434 ARG 434 434 434 ARG ARG A . n 
A 1 435 GLN 435 435 435 GLN GLN A . n 
A 1 436 SER 436 436 436 SER SER A . n 
A 1 437 ASN 437 437 437 ASN ASN A . n 
A 1 438 LEU 438 438 438 LEU LEU A . n 
A 1 439 CYS 439 439 439 CYS CYS A . n 
A 1 440 LEU 440 440 440 LEU LEU A . n 
A 1 441 GLU 441 441 441 GLU GLU A . n 
A 1 442 ILE 442 442 442 ILE ILE A . n 
A 1 443 ALA 443 443 443 ALA ALA A . n 
A 1 444 LEU 444 444 444 LEU LEU A . n 
A 1 445 PRO 445 445 445 PRO PRO A . n 
A 1 446 THR 446 446 446 THR THR A . n 
A 1 447 LYS 447 447 447 LYS LYS A . n 
A 1 448 PRO 448 448 448 PRO PRO A . n 
A 1 449 LEU 449 449 449 LEU LEU A . n 
A 1 450 ASN 450 450 450 ASN ASN A . n 
A 1 451 ASP 451 451 451 ASP ASP A . n 
A 1 452 VAL 452 452 452 VAL VAL A . n 
A 1 453 ASN 453 453 453 ASN ASN A . n 
A 1 454 ASP 454 454 454 ASP ASP A . n 
A 1 455 GLU 455 455 455 GLU GLU A . n 
A 1 456 ASN 456 456 456 ASN ASN A . n 
A 1 457 GLY 457 457 457 GLY GLY A . n 
A 1 458 GLU 458 458 458 GLU GLU A . n 
A 1 459 ILE 459 459 459 ILE ILE A . n 
A 1 460 ALA 460 460 460 ALA ALA A . n 
A 1 461 LEU 461 461 461 LEU LEU A . n 
A 1 462 CYS 462 462 462 CYS CYS A . n 
A 1 463 THR 463 463 463 THR THR A . n 
A 1 464 LEU 464 464 464 LEU LEU A . n 
A 1 465 SER 465 465 465 SER SER A . n 
A 1 466 ALA 466 466 466 ALA ALA A . n 
A 1 467 PHE 467 467 467 PHE PHE A . n 
A 1 468 ASN 468 468 468 ASN ASN A . n 
A 1 469 LEU 469 469 469 LEU LEU A . n 
A 1 470 GLY 470 470 470 GLY GLY A . n 
A 1 471 ALA 471 471 471 ALA ALA A . n 
A 1 472 ILE 472 472 472 ILE ILE A . n 
A 1 473 ASN 473 473 473 ASN ASN A . n 
A 1 474 ASN 474 474 474 ASN ASN A . n 
A 1 475 LEU 475 475 475 LEU LEU A . n 
A 1 476 ASP 476 476 476 ASP ASP A . n 
A 1 477 GLU 477 477 477 GLU GLU A . n 
A 1 478 LEU 478 478 478 LEU LEU A . n 
A 1 479 GLU 479 479 479 GLU GLU A . n 
A 1 480 GLU 480 480 480 GLU GLU A . n 
A 1 481 LEU 481 481 481 LEU LEU A . n 
A 1 482 ALA 482 482 482 ALA ALA A . n 
A 1 483 ILE 483 483 483 ILE ILE A . n 
A 1 484 LEU 484 484 484 LEU LEU A . n 
A 1 485 ALA 485 485 485 ALA ALA A . n 
A 1 486 VAL 486 486 486 VAL VAL A . n 
A 1 487 ARG 487 487 487 ARG ARG A . n 
A 1 488 ALA 488 488 488 ALA ALA A . n 
A 1 489 LEU 489 489 489 LEU LEU A . n 
A 1 490 ASP 490 490 490 ASP ASP A . n 
A 1 491 ALA 491 491 491 ALA ALA A . n 
A 1 492 LEU 492 492 492 LEU LEU A . n 
A 1 493 LEU 493 493 493 LEU LEU A . n 
A 1 494 ASP 494 494 494 ASP ASP A . n 
A 1 495 TYR 495 495 495 TYR TYR A . n 
A 1 496 GLN 496 496 496 GLN GLN A . n 
A 1 497 ASP 497 497 497 ASP ASP A . n 
A 1 498 TYR 498 498 498 TYR TYR A . n 
A 1 499 PRO 499 499 499 PRO PRO A . n 
A 1 500 ILE 500 500 500 ILE ILE A . n 
A 1 501 PRO 501 501 501 PRO PRO A . n 
A 1 502 ALA 502 502 502 ALA ALA A . n 
A 1 503 ALA 503 503 503 ALA ALA A . n 
A 1 504 LYS 504 504 504 LYS LYS A . n 
A 1 505 ARG 505 505 505 ARG ARG A . n 
A 1 506 GLY 506 506 506 GLY GLY A . n 
A 1 507 ALA 507 507 507 ALA ALA A . n 
A 1 508 MET 508 508 508 MET MET A . n 
A 1 509 GLY 509 509 509 GLY GLY A . n 
A 1 510 ARG 510 510 510 ARG ARG A . n 
A 1 511 ARG 511 511 511 ARG ARG A . n 
A 1 512 THR 512 512 512 THR THR A . n 
A 1 513 LEU 513 513 513 LEU LEU A . n 
A 1 514 GLY 514 514 514 GLY GLY A . n 
A 1 515 ILE 515 515 515 ILE ILE A . n 
A 1 516 GLY 516 516 516 GLY GLY A . n 
A 1 517 VAL 517 517 517 VAL VAL A . n 
A 1 518 ILE 518 518 518 ILE ILE A . n 
A 1 519 ASN 519 519 519 ASN ASN A . n 
A 1 520 PHE 520 520 520 PHE PHE A . n 
A 1 521 ALA 521 521 521 ALA ALA A . n 
A 1 522 TYR 522 522 522 TYR TYR A . n 
A 1 523 TYR 523 523 523 TYR TYR A . n 
A 1 524 LEU 524 524 524 LEU LEU A . n 
A 1 525 ALA 525 525 525 ALA ALA A . n 
A 1 526 LYS 526 526 526 LYS LYS A . n 
A 1 527 HIS 527 527 527 HIS HIS A . n 
A 1 528 GLY 528 528 528 GLY GLY A . n 
A 1 529 LYS 529 529 529 LYS LYS A . n 
A 1 530 ARG 530 530 530 ARG ARG A . n 
A 1 531 TYR 531 531 531 TYR TYR A . n 
A 1 532 SER 532 532 532 SER SER A . n 
A 1 533 ASP 533 533 533 ASP ASP A . n 
A 1 534 GLY 534 534 534 GLY GLY A . n 
A 1 535 SER 535 535 535 SER SER A . n 
A 1 536 ALA 536 536 536 ALA ALA A . n 
A 1 537 ASN 537 537 537 ASN ASN A . n 
A 1 538 ASN 538 538 538 ASN ASN A . n 
A 1 539 LEU 539 539 539 LEU LEU A . n 
A 1 540 THR 540 540 540 THR THR A . n 
A 1 541 HIS 541 541 541 HIS HIS A . n 
A 1 542 LYS 542 542 542 LYS LYS A . n 
A 1 543 THR 543 543 543 THR THR A . n 
A 1 544 PHE 544 544 544 PHE PHE A . n 
A 1 545 GLU 545 545 545 GLU GLU A . n 
A 1 546 ALA 546 546 546 ALA ALA A . n 
A 1 547 ILE 547 547 547 ILE ILE A . n 
A 1 548 GLN 548 548 548 GLN GLN A . n 
A 1 549 TYR 549 549 549 TYR TYR A . n 
A 1 550 TYR 550 550 550 TYR TYR A . n 
A 1 551 LEU 551 551 551 LEU LEU A . n 
A 1 552 LEU 552 552 552 LEU LEU A . n 
A 1 553 LYS 553 553 553 LYS LYS A . n 
A 1 554 ALA 554 554 554 ALA ALA A . n 
A 1 555 SER 555 555 555 SER SER A . n 
A 1 556 ASN 556 556 556 ASN ASN A . n 
A 1 557 GLU 557 557 557 GLU GLU A . n 
A 1 558 LEU 558 558 558 LEU LEU A . n 
A 1 559 ALA 559 559 559 ALA ALA A . n 
A 1 560 LYS 560 560 560 LYS LYS A . n 
A 1 561 GLU 561 561 561 GLU GLU A . n 
A 1 562 GLN 562 562 562 GLN GLN A . n 
A 1 563 GLY 563 563 563 GLY GLY A . n 
A 1 564 ALA 564 564 564 ALA ALA A . n 
A 1 565 CYS 565 565 565 CYS CYS A . n 
A 1 566 PRO 566 566 566 PRO PRO A . n 
A 1 567 TRP 567 567 567 TRP TRP A . n 
A 1 568 PHE 568 568 568 PHE PHE A . n 
A 1 569 ASN 569 569 569 ASN ASN A . n 
A 1 570 GLU 570 570 570 GLU GLU A . n 
A 1 571 THR 571 571 571 THR THR A . n 
A 1 572 THR 572 572 572 THR THR A . n 
A 1 573 TYR 573 573 573 TYR TYR A . n 
A 1 574 ALA 574 574 574 ALA ALA A . n 
A 1 575 LYS 575 575 575 LYS LYS A . n 
A 1 576 GLY 576 576 576 GLY GLY A . n 
A 1 577 ILE 577 577 577 ILE ILE A . n 
A 1 578 LEU 578 578 578 LEU LEU A . n 
A 1 579 PRO 579 579 579 PRO PRO A . n 
A 1 580 ILE 580 580 580 ILE ILE A . n 
A 1 581 ASP 581 581 581 ASP ASP A . n 
A 1 582 THR 582 582 582 THR THR A . n 
A 1 583 TYR 583 583 583 TYR TYR A . n 
A 1 584 LYS 584 584 584 LYS LYS A . n 
A 1 585 LYS 585 585 585 LYS LYS A . n 
A 1 586 ASP 586 586 586 ASP ASP A . n 
A 1 587 LEU 587 587 587 LEU LEU A . n 
A 1 588 ASP 588 588 588 ASP ASP A . n 
A 1 589 THR 589 589 589 THR THR A . n 
A 1 590 ILE 590 590 590 ILE ILE A . n 
A 1 591 ALA 591 591 591 ALA ALA A . n 
A 1 592 ASN 592 592 592 ASN ASN A . n 
A 1 593 GLU 593 593 593 GLU GLU A . n 
A 1 594 PRO 594 594 594 PRO PRO A . n 
A 1 595 LEU 595 595 595 LEU LEU A . n 
A 1 596 HIS 596 596 596 HIS HIS A . n 
A 1 597 TYR 597 597 597 TYR TYR A . n 
A 1 598 ASP 598 598 598 ASP ASP A . n 
A 1 599 TRP 599 599 599 TRP TRP A . n 
A 1 600 GLU 600 600 600 GLU GLU A . n 
A 1 601 ALA 601 601 601 ALA ALA A . n 
A 1 602 LEU 602 602 602 LEU LEU A . n 
A 1 603 ARG 603 603 603 ARG ARG A . n 
A 1 604 GLU 604 604 604 GLU GLU A . n 
A 1 605 SER 605 605 605 SER SER A . n 
A 1 606 ILE 606 606 606 ILE ILE A . n 
A 1 607 LYS 607 607 607 LYS LYS A . n 
A 1 608 THR 608 608 608 THR THR A . n 
A 1 609 HIS 609 609 609 HIS HIS A . n 
A 1 610 GLY 610 610 610 GLY GLY A . n 
A 1 611 LEU 611 611 611 LEU LEU A . n 
A 1 612 ARG 612 612 612 ARG ARG A . n 
A 1 613 ASN 613 613 613 ASN ASN A . n 
A 1 614 SER 614 614 614 SER SER A . n 
A 1 615 THR 615 615 615 THR THR A . n 
A 1 616 LEU 616 616 616 LEU LEU A . n 
A 1 617 SER 617 617 617 SER SER A . n 
A 1 618 ALA 618 618 618 ALA ALA A . n 
A 1 619 LEU 619 619 619 LEU LEU A . n 
A 1 620 MET 620 620 620 MET MET A . n 
A 1 621 PRO 621 621 621 PRO PRO A . n 
A 1 622 SER 622 622 622 SER SER A . n 
A 1 623 GLU 623 623 623 GLU GLU A . n 
A 1 624 THR 624 624 624 THR THR A . n 
A 1 625 SER 625 625 625 SER SER A . n 
A 1 626 SER 626 626 626 SER SER A . n 
A 1 627 GLN 627 627 627 GLN GLN A . n 
A 1 628 ILE 628 628 628 ILE ILE A . n 
A 1 629 SER 629 629 629 SER SER A . n 
A 1 630 ASN 630 630 630 ASN ASN A . n 
A 1 631 ALA 631 631 631 ALA ALA A . n 
A 1 632 THR 632 632 632 THR THR A . n 
A 1 633 ASN 633 633 633 ASN ASN A . n 
A 1 634 GLY 634 634 634 GLY GLY A . n 
A 1 635 ILE 635 635 635 ILE ILE A . n 
A 1 636 GLU 636 636 636 GLU GLU A . n 
A 1 637 PRO 637 637 637 PRO PRO A . n 
A 1 638 PRO 638 638 638 PRO PRO A . n 
A 1 639 ARG 639 639 639 ARG ARG A . n 
A 1 640 GLY 640 640 640 GLY GLY A . n 
A 1 641 TYR 641 641 641 TYR TYR A . n 
A 1 642 VAL 642 642 642 VAL VAL A . n 
A 1 643 SER 643 643 643 SER SER A . n 
A 1 644 ILE 644 644 644 ILE ILE A . n 
A 1 645 LYS 645 645 645 LYS LYS A . n 
A 1 646 ALA 646 646 646 ALA ALA A . n 
A 1 647 SER 647 647 647 SER SER A . n 
A 1 648 LYS 648 648 648 LYS LYS A . n 
A 1 649 ASP 649 649 649 ASP ASP A . n 
A 1 650 GLY 650 650 650 GLY GLY A . n 
A 1 651 ILE 651 651 651 ILE ILE A . n 
A 1 652 LEU 652 652 652 LEU LEU A . n 
A 1 653 ARG 653 653 653 ARG ARG A . n 
A 1 654 GLN 654 654 654 GLN GLN A . n 
A 1 655 VAL 655 655 655 VAL VAL A . n 
A 1 656 VAL 656 656 656 VAL VAL A . n 
A 1 657 PRO 657 657 657 PRO PRO A . n 
A 1 658 ASP 658 658 658 ASP ASP A . n 
A 1 659 TYR 659 659 659 TYR TYR A . n 
A 1 660 GLU 660 660 660 GLU GLU A . n 
A 1 661 HIS 661 661 661 HIS HIS A . n 
A 1 662 LEU 662 662 662 LEU LEU A . n 
A 1 663 HIS 663 663 663 HIS HIS A . n 
A 1 664 ASP 664 664 664 ASP ASP A . n 
A 1 665 ALA 665 665 665 ALA ALA A . n 
A 1 666 TYR 666 666 666 TYR TYR A . n 
A 1 667 GLU 667 667 667 GLU GLU A . n 
A 1 668 LEU 668 668 668 LEU LEU A . n 
A 1 669 LEU 669 669 669 LEU LEU A . n 
A 1 670 TRP 670 670 670 TRP TRP A . n 
A 1 671 GLU 671 671 671 GLU GLU A . n 
A 1 672 MET 672 672 672 MET MET A . n 
A 1 673 PRO 673 673 673 PRO PRO A . n 
A 1 674 GLY 674 674 674 GLY GLY A . n 
A 1 675 ASN 675 675 675 ASN ASN A . n 
A 1 676 ASP 676 676 676 ASP ASP A . n 
A 1 677 GLY 677 677 677 GLY GLY A . n 
A 1 678 TYR 678 678 678 TYR TYR A . n 
A 1 679 LEU 679 679 679 LEU LEU A . n 
A 1 680 GLN 680 680 680 GLN GLN A . n 
A 1 681 LEU 681 681 681 LEU LEU A . n 
A 1 682 VAL 682 682 682 VAL VAL A . n 
A 1 683 GLY 683 683 683 GLY GLY A . n 
A 1 684 ILE 684 684 684 ILE ILE A . n 
A 1 685 MET 685 685 685 MET MET A . n 
A 1 686 GLN 686 686 686 GLN GLN A . n 
A 1 687 LYS 687 687 687 LYS LYS A . n 
A 1 688 PHE 688 688 688 PHE PHE A . n 
A 1 689 ILE 689 689 689 ILE ILE A . n 
A 1 690 ASP 690 690 690 ASP ASP A . n 
A 1 691 GLN 691 691 691 GLN GLN A . n 
A 1 692 SER 692 692 692 SER SER A . n 
A 1 693 ILE 693 693 693 ILE ILE A . n 
A 1 694 SER 694 694 694 SER SER A . n 
A 1 695 ALA 695 695 695 ALA ALA A . n 
A 1 696 ASN 696 696 696 ASN ASN A . n 
A 1 697 THR 697 697 697 THR THR A . n 
A 1 698 ASN 698 698 698 ASN ASN A . n 
A 1 699 TYR 699 699 699 TYR TYR A . n 
A 1 700 ASP 700 700 700 ASP ASP A . n 
A 1 701 PRO 701 701 701 PRO PRO A . n 
A 1 702 SER 702 702 702 SER SER A . n 
A 1 703 ARG 703 703 703 ARG ARG A . n 
A 1 704 PHE 704 704 704 PHE PHE A . n 
A 1 705 PRO 705 705 705 PRO PRO A . n 
A 1 706 SER 706 706 706 SER SER A . n 
A 1 707 GLY 707 707 707 GLY GLY A . n 
A 1 708 LYS 708 708 708 LYS LYS A . n 
A 1 709 VAL 709 709 709 VAL VAL A . n 
A 1 710 PRO 710 710 710 PRO PRO A . n 
A 1 711 MET 711 711 711 MET MET A . n 
A 1 712 GLN 712 712 712 GLN GLN A . n 
A 1 713 GLN 713 713 713 GLN GLN A . n 
A 1 714 LEU 714 714 714 LEU LEU A . n 
A 1 715 LEU 715 715 715 LEU LEU A . n 
A 1 716 LYS 716 716 716 LYS LYS A . n 
A 1 717 ASP 717 717 717 ASP ASP A . n 
A 1 718 LEU 718 718 718 LEU LEU A . n 
A 1 719 LEU 719 719 719 LEU LEU A . n 
A 1 720 THR 720 720 720 THR THR A . n 
A 1 721 ALA 721 721 721 ALA ALA A . n 
A 1 722 TYR 722 722 722 TYR TYR A . n 
A 1 723 LYS 723 723 723 LYS LYS A . n 
A 1 724 PHE 724 724 724 PHE PHE A . n 
A 1 725 GLY 725 725 725 GLY GLY A . n 
A 1 726 VAL 726 726 726 VAL VAL A . n 
A 1 727 LYS 727 727 727 LYS LYS A . n 
A 1 728 THR 728 728 728 THR THR A . n 
A 1 729 LEU 729 729 729 LEU LEU A . n 
A 1 730 TYR 730 730 730 TYR TYR A . n 
A 1 731 TYR 731 731 731 TYR TYR A . n 
A 1 732 GLN 732 732 732 GLN GLN A . n 
A 1 733 ASN 733 733 733 ASN ASN A . n 
A 1 734 THR 734 734 734 THR THR A . n 
A 1 735 ARG 735 735 735 ARG ARG A . n 
A 1 736 ASP 736 736 736 ASP ASP A . n 
A 1 737 GLY 737 737 737 GLY GLY A . n 
A 1 738 ALA 738 738 738 ALA ALA A . n 
A 1 739 GLU 739 739 739 GLU GLU A . n 
A 1 740 ASP 740 740 ?   ?   ?   A . n 
A 1 741 ALA 741 741 ?   ?   ?   A . n 
A 1 742 GLN 742 742 ?   ?   ?   A . n 
A 1 743 ASP 743 743 ?   ?   ?   A . n 
A 1 744 ASP 744 744 ?   ?   ?   A . n 
A 1 745 LEU 745 745 ?   ?   ?   A . n 
A 1 746 VAL 746 746 ?   ?   ?   A . n 
A 1 747 PRO 747 747 ?   ?   ?   A . n 
A 1 748 SER 748 748 ?   ?   ?   A . n 
A 1 749 ILE 749 749 ?   ?   ?   A . n 
A 1 750 GLN 750 750 ?   ?   ?   A . n 
A 1 751 ASP 751 751 ?   ?   ?   A . n 
A 1 752 ASP 752 752 ?   ?   ?   A . n 
A 1 753 GLY 753 753 ?   ?   ?   A . n 
A 1 754 CYS 754 754 ?   ?   ?   A . n 
A 1 755 GLU 755 755 ?   ?   ?   A . n 
A 1 756 SER 756 756 ?   ?   ?   A . n 
A 1 757 GLY 757 757 ?   ?   ?   A . n 
A 1 758 ALA 758 758 ?   ?   ?   A . n 
A 1 759 CYS 759 759 ?   ?   ?   A . n 
A 1 760 LYS 760 760 ?   ?   ?   A . n 
A 1 761 ILE 761 761 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   ASN 2   2   2   ASN ASN B . n 
B 1 3   GLN 3   3   3   GLN GLN B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   LEU 5   5   5   LEU LEU B . n 
B 1 6   LEU 6   6   6   LEU LEU B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   THR 8   8   8   THR THR B . n 
B 1 9   LYS 9   9   9   LYS LYS B . n 
B 1 10  ARG 10  10  10  ARG ARG B . n 
B 1 11  ASP 11  11  11  ASP ASP B . n 
B 1 12  GLY 12  12  12  GLY GLY B . n 
B 1 13  SER 13  13  13  SER SER B . n 
B 1 14  THR 14  14  14  THR THR B . n 
B 1 15  GLU 15  15  15  GLU GLU B . n 
B 1 16  ARG 16  16  16  ARG ARG B . n 
B 1 17  ILE 17  17  17  ILE ILE B . n 
B 1 18  ASN 18  18  18  ASN ASN B . n 
B 1 19  LEU 19  19  19  LEU LEU B . n 
B 1 20  ASP 20  20  20  ASP ASP B . n 
B 1 21  LYS 21  21  21  LYS LYS B . n 
B 1 22  ILE 22  22  22  ILE ILE B . n 
B 1 23  HIS 23  23  23  HIS HIS B . n 
B 1 24  ARG 24  24  24  ARG ARG B . n 
B 1 25  VAL 25  25  25  VAL VAL B . n 
B 1 26  LEU 26  26  26  LEU LEU B . n 
B 1 27  ASP 27  27  27  ASP ASP B . n 
B 1 28  TRP 28  28  28  TRP TRP B . n 
B 1 29  ALA 29  29  29  ALA ALA B . n 
B 1 30  ALA 30  30  30  ALA ALA B . n 
B 1 31  GLU 31  31  31  GLU GLU B . n 
B 1 32  GLY 32  32  32  GLY GLY B . n 
B 1 33  LEU 33  33  33  LEU LEU B . n 
B 1 34  HIS 34  34  34  HIS HIS B . n 
B 1 35  ASN 35  35  35  ASN ASN B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  SER 37  37  37  SER SER B . n 
B 1 38  ILE 38  38  38  ILE ILE B . n 
B 1 39  SER 39  39  39  SER SER B . n 
B 1 40  GLN 40  40  40  GLN GLN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  GLU 42  42  42  GLU GLU B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  ARG 44  44  44  ARG ARG B . n 
B 1 45  SER 45  45  45  SER SER B . n 
B 1 46  HIS 46  46  46  HIS HIS B . n 
B 1 47  ILE 47  47  47  ILE ILE B . n 
B 1 48  GLN 48  48  48  GLN GLN B . n 
B 1 49  PHE 49  49  49  PHE PHE B . n 
B 1 50  TYR 50  50  50  TYR TYR B . n 
B 1 51  ASP 51  51  51  ASP ASP B . n 
B 1 52  GLY 52  52  52  GLY GLY B . n 
B 1 53  ILE 53  53  53  ILE ILE B . n 
B 1 54  LYS 54  54  54  LYS LYS B . n 
B 1 55  THR 55  55  55  THR THR B . n 
B 1 56  SER 56  56  56  SER SER B . n 
B 1 57  ASP 57  57  57  ASP ASP B . n 
B 1 58  ILE 58  58  58  ILE ILE B . n 
B 1 59  HIS 59  59  59  HIS HIS B . n 
B 1 60  GLU 60  60  60  GLU GLU B . n 
B 1 61  THR 61  61  61  THR THR B . n 
B 1 62  ILE 62  62  62  ILE ILE B . n 
B 1 63  ILE 63  63  63  ILE ILE B . n 
B 1 64  LYS 64  64  64  LYS LYS B . n 
B 1 65  ALA 65  65  65  ALA ALA B . n 
B 1 66  ALA 66  66  66  ALA ALA B . n 
B 1 67  ALA 67  67  67  ALA ALA B . n 
B 1 68  ASP 68  68  68  ASP ASP B . n 
B 1 69  LEU 69  69  69  LEU LEU B . n 
B 1 70  ILE 70  70  70  ILE ILE B . n 
B 1 71  SER 71  71  71  SER SER B . n 
B 1 72  ARG 72  72  72  ARG ARG B . n 
B 1 73  ASP 73  73  73  ASP ASP B . n 
B 1 74  ALA 74  74  74  ALA ALA B . n 
B 1 75  PRO 75  75  75  PRO PRO B . n 
B 1 76  ASP 76  76  76  ASP ASP B . n 
B 1 77  TYR 77  77  77  TYR TYR B . n 
B 1 78  GLN 78  78  78  GLN GLN B . n 
B 1 79  TYR 79  79  79  TYR TYR B . n 
B 1 80  LEU 80  80  80  LEU LEU B . n 
B 1 81  ALA 81  81  81  ALA ALA B . n 
B 1 82  ALA 82  82  82  ALA ALA B . n 
B 1 83  ARG 83  83  83  ARG ARG B . n 
B 1 84  LEU 84  84  84  LEU LEU B . n 
B 1 85  ALA 85  85  85  ALA ALA B . n 
B 1 86  ILE 86  86  86  ILE ILE B . n 
B 1 87  PHE 87  87  87  PHE PHE B . n 
B 1 88  HIS 88  88  88  HIS HIS B . n 
B 1 89  LEU 89  89  89  LEU LEU B . n 
B 1 90  ARG 90  90  90  ARG ARG B . n 
B 1 91  LYS 91  91  91  LYS LYS B . n 
B 1 92  LYS 92  92  92  LYS LYS B . n 
B 1 93  ALA 93  93  93  ALA ALA B . n 
B 1 94  TYR 94  94  94  TYR TYR B . n 
B 1 95  GLY 95  95  95  GLY GLY B . n 
B 1 96  GLN 96  96  96  GLN GLN B . n 
B 1 97  PHE 97  97  97  PHE PHE B . n 
B 1 98  GLU 98  98  98  GLU GLU B . n 
B 1 99  PRO 99  99  99  PRO PRO B . n 
B 1 100 PRO 100 100 100 PRO PRO B . n 
B 1 101 ALA 101 101 101 ALA ALA B . n 
B 1 102 LEU 102 102 102 LEU LEU B . n 
B 1 103 TYR 103 103 103 TYR TYR B . n 
B 1 104 ASP 104 104 104 ASP ASP B . n 
B 1 105 HIS 105 105 105 HIS HIS B . n 
B 1 106 VAL 106 106 106 VAL VAL B . n 
B 1 107 VAL 107 107 107 VAL VAL B . n 
B 1 108 LYS 108 108 108 LYS LYS B . n 
B 1 109 MET 109 109 109 MET MET B . n 
B 1 110 VAL 110 110 110 VAL VAL B . n 
B 1 111 GLU 111 111 111 GLU GLU B . n 
B 1 112 MET 112 112 112 MET MET B . n 
B 1 113 GLY 113 113 113 GLY GLY B . n 
B 1 114 LYS 114 114 114 LYS LYS B . n 
B 1 115 TYR 115 115 115 TYR TYR B . n 
B 1 116 ASP 116 116 116 ASP ASP B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 HIS 118 118 118 HIS HIS B . n 
B 1 119 LEU 119 119 119 LEU LEU B . n 
B 1 120 LEU 120 120 120 LEU LEU B . n 
B 1 121 GLU 121 121 121 GLU GLU B . n 
B 1 122 ASP 122 122 122 ASP ASP B . n 
B 1 123 TYR 123 123 123 TYR TYR B . n 
B 1 124 THR 124 124 124 THR THR B . n 
B 1 125 GLU 125 125 125 GLU GLU B . n 
B 1 126 GLU 126 126 126 GLU GLU B . n 
B 1 127 GLU 127 127 127 GLU GLU B . n 
B 1 128 PHE 128 128 128 PHE PHE B . n 
B 1 129 LYS 129 129 129 LYS LYS B . n 
B 1 130 GLN 130 130 130 GLN GLN B . n 
B 1 131 MET 131 131 131 MET MET B . n 
B 1 132 ASP 132 132 132 ASP ASP B . n 
B 1 133 THR 133 133 133 THR THR B . n 
B 1 134 PHE 134 134 134 PHE PHE B . n 
B 1 135 ILE 135 135 135 ILE ILE B . n 
B 1 136 ASP 136 136 136 ASP ASP B . n 
B 1 137 HIS 137 137 137 HIS HIS B . n 
B 1 138 ASP 138 138 138 ASP ASP B . n 
B 1 139 ARG 139 139 139 ARG ARG B . n 
B 1 140 ASP 140 140 140 ASP ASP B . n 
B 1 141 MET 141 141 141 MET MET B . n 
B 1 142 THR 142 142 142 THR THR B . n 
B 1 143 PHE 143 143 143 PHE PHE B . n 
B 1 144 SER 144 144 144 SER SER B . n 
B 1 145 TYR 145 145 145 TYR TYR B . n 
B 1 146 ALA 146 146 146 ALA ALA B . n 
B 1 147 ALA 147 147 147 ALA ALA B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 LYS 149 149 149 LYS LYS B . n 
B 1 150 GLN 150 150 150 GLN GLN B . n 
B 1 151 LEU 151 151 151 LEU LEU B . n 
B 1 152 GLU 152 152 152 GLU GLU B . n 
B 1 153 GLY 153 153 153 GLY GLY B . n 
B 1 154 LYS 154 154 154 LYS LYS B . n 
B 1 155 TYR 155 155 155 TYR TYR B . n 
B 1 156 LEU 156 156 156 LEU LEU B . n 
B 1 157 VAL 157 157 157 VAL VAL B . n 
B 1 158 GLN 158 158 158 GLN GLN B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 ARG 160 160 160 ARG ARG B . n 
B 1 161 VAL 161 161 161 VAL VAL B . n 
B 1 162 THR 162 162 162 THR THR B . n 
B 1 163 GLY 163 163 163 GLY GLY B . n 
B 1 164 GLU 164 164 164 GLU GLU B . n 
B 1 165 ILE 165 165 165 ILE ILE B . n 
B 1 166 TYR 166 166 166 TYR TYR B . n 
B 1 167 GLU 167 167 167 GLU GLU B . n 
B 1 168 SER 168 168 168 SER SER B . n 
B 1 169 ALA 169 169 169 ALA ALA B . n 
B 1 170 GLN 170 170 170 GLN GLN B . n 
B 1 171 PHE 171 171 171 PHE PHE B . n 
B 1 172 LEU 172 172 172 LEU LEU B . n 
B 1 173 TYR 173 173 173 TYR TYR B . n 
B 1 174 ILE 174 174 174 ILE ILE B . n 
B 1 175 LEU 175 175 175 LEU LEU B . n 
B 1 176 VAL 176 176 176 VAL VAL B . n 
B 1 177 ALA 177 177 177 ALA ALA B . n 
B 1 178 ALA 178 178 178 ALA ALA B . n 
B 1 179 CYS 179 179 179 CYS CYS B . n 
B 1 180 LEU 180 180 180 LEU LEU B . n 
B 1 181 PHE 181 181 181 PHE PHE B . n 
B 1 182 SER 182 182 182 SER SER B . n 
B 1 183 ASN 183 183 183 ASN ASN B . n 
B 1 184 TYR 184 184 184 TYR TYR B . n 
B 1 185 PRO 185 185 185 PRO PRO B . n 
B 1 186 ARG 186 186 186 ARG ARG B . n 
B 1 187 GLU 187 187 187 GLU GLU B . n 
B 1 188 THR 188 188 188 THR THR B . n 
B 1 189 ARG 189 189 189 ARG ARG B . n 
B 1 190 LEU 190 190 190 LEU LEU B . n 
B 1 191 GLN 191 191 191 GLN GLN B . n 
B 1 192 TYR 192 192 192 TYR TYR B . n 
B 1 193 VAL 193 193 193 VAL VAL B . n 
B 1 194 LYS 194 194 194 LYS LYS B . n 
B 1 195 ARG 195 195 195 ARG ARG B . n 
B 1 196 PHE 196 196 196 PHE PHE B . n 
B 1 197 TYR 197 197 197 TYR TYR B . n 
B 1 198 ASP 198 198 198 ASP ASP B . n 
B 1 199 ALA 199 199 199 ALA ALA B . n 
B 1 200 VAL 200 200 200 VAL VAL B . n 
B 1 201 SER 201 201 201 SER SER B . n 
B 1 202 THR 202 202 202 THR THR B . n 
B 1 203 PHE 203 203 203 PHE PHE B . n 
B 1 204 LYS 204 204 204 LYS LYS B . n 
B 1 205 ILE 205 205 205 ILE ILE B . n 
B 1 206 SER 206 206 206 SER SER B . n 
B 1 207 LEU 207 207 207 LEU LEU B . n 
B 1 208 PRO 208 208 208 PRO PRO B . n 
B 1 209 THR 209 209 209 THR THR B . n 
B 1 210 PRO 210 210 210 PRO PRO B . n 
B 1 211 ILE 211 211 211 ILE ILE B . n 
B 1 212 MET 212 212 212 MET MET B . n 
B 1 213 SER 213 213 213 SER SER B . n 
B 1 214 GLY 214 214 214 GLY GLY B . n 
B 1 215 VAL 215 215 215 VAL VAL B . n 
B 1 216 ARG 216 216 216 ARG ARG B . n 
B 1 217 THR 217 217 217 THR THR B . n 
B 1 218 PRO 218 218 218 PRO PRO B . n 
B 1 219 THR 219 219 219 THR THR B . n 
B 1 220 ARG 220 220 220 ARG ARG B . n 
B 1 221 GLN 221 221 221 GLN GLN B . n 
B 1 222 PHE 222 222 222 PHE PHE B . n 
B 1 223 SER 223 223 223 SER SER B . n 
B 1 224 SER 224 224 224 SER SER B . n 
B 1 225 CYS 225 225 225 CYS CYS B . n 
B 1 226 VAL 226 226 226 VAL VAL B . n 
B 1 227 LEU 227 227 227 LEU LEU B . n 
B 1 228 ILE 228 228 228 ILE ILE B . n 
B 1 229 GLU 229 229 229 GLU GLU B . n 
B 1 230 CYS 230 230 230 CYS CYS B . n 
B 1 231 GLY 231 231 231 GLY GLY B . n 
B 1 232 ASP 232 232 232 ASP ASP B . n 
B 1 233 SER 233 233 233 SER SER B . n 
B 1 234 LEU 234 234 234 LEU LEU B . n 
B 1 235 ASP 235 235 235 ASP ASP B . n 
B 1 236 SER 236 236 236 SER SER B . n 
B 1 237 ILE 237 237 237 ILE ILE B . n 
B 1 238 ASN 238 238 238 ASN ASN B . n 
B 1 239 ALA 239 239 239 ALA ALA B . n 
B 1 240 THR 240 240 240 THR THR B . n 
B 1 241 SER 241 241 241 SER SER B . n 
B 1 242 SER 242 242 242 SER SER B . n 
B 1 243 ALA 243 243 243 ALA ALA B . n 
B 1 244 ILE 244 244 244 ILE ILE B . n 
B 1 245 VAL 245 245 245 VAL VAL B . n 
B 1 246 LYS 246 246 246 LYS LYS B . n 
B 1 247 TYR 247 247 247 TYR TYR B . n 
B 1 248 VAL 248 248 248 VAL VAL B . n 
B 1 249 SER 249 249 249 SER SER B . n 
B 1 250 GLN 250 250 250 GLN GLN B . n 
B 1 251 ARG 251 251 251 ARG ARG B . n 
B 1 252 ALA 252 252 252 ALA ALA B . n 
B 1 253 GLY 253 253 253 GLY GLY B . n 
B 1 254 ILE 254 254 254 ILE ILE B . n 
B 1 255 GLY 255 255 255 GLY GLY B . n 
B 1 256 ILE 256 256 256 ILE ILE B . n 
B 1 257 ASN 257 257 257 ASN ASN B . n 
B 1 258 ALA 258 258 258 ALA ALA B . n 
B 1 259 GLY 259 259 259 GLY GLY B . n 
B 1 260 ARG 260 260 260 ARG ARG B . n 
B 1 261 ILE 261 261 261 ILE ILE B . n 
B 1 262 ARG 262 262 262 ARG ARG B . n 
B 1 263 ALA 263 263 263 ALA ALA B . n 
B 1 264 LEU 264 264 264 LEU LEU B . n 
B 1 265 GLY 265 265 265 GLY GLY B . n 
B 1 266 SER 266 266 266 SER SER B . n 
B 1 267 PRO 267 267 267 PRO PRO B . n 
B 1 268 ILE 268 268 268 ILE ILE B . n 
B 1 269 ARG 269 269 269 ARG ARG B . n 
B 1 270 GLY 270 270 270 GLY GLY B . n 
B 1 271 GLY 271 271 271 GLY GLY B . n 
B 1 272 GLU 272 272 272 GLU GLU B . n 
B 1 273 ALA 273 273 273 ALA ALA B . n 
B 1 274 PHE 274 274 274 PHE PHE B . n 
B 1 275 HIS 275 275 275 HIS HIS B . n 
B 1 276 THR 276 276 276 THR THR B . n 
B 1 277 GLY 277 277 277 GLY GLY B . n 
B 1 278 CYS 278 278 278 CYS CYS B . n 
B 1 279 ILE 279 279 279 ILE ILE B . n 
B 1 280 PRO 280 280 280 PRO PRO B . n 
B 1 281 PHE 281 281 281 PHE PHE B . n 
B 1 282 TYR 282 282 282 TYR TYR B . n 
B 1 283 LYS 283 283 283 LYS LYS B . n 
B 1 284 HIS 284 284 284 HIS HIS B . n 
B 1 285 PHE 285 285 285 PHE PHE B . n 
B 1 286 GLN 286 286 286 GLN GLN B . n 
B 1 287 THR 287 287 287 THR THR B . n 
B 1 288 ALA 288 288 288 ALA ALA B . n 
B 1 289 VAL 289 289 289 VAL VAL B . n 
B 1 290 LYS 290 290 290 LYS LYS B . n 
B 1 291 SER 291 291 291 SER SER B . n 
B 1 292 CYS 292 292 292 CYS CYS B . n 
B 1 293 SER 293 293 293 SER SER B . n 
B 1 294 GLN 294 294 294 GLN GLN B . n 
B 1 295 GLY 295 295 295 GLY GLY B . n 
B 1 296 GLY 296 296 296 GLY GLY B . n 
B 1 297 VAL 297 297 297 VAL VAL B . n 
B 1 298 ARG 298 298 298 ARG ARG B . n 
B 1 299 GLY 299 299 299 GLY GLY B . n 
B 1 300 GLY 300 300 300 GLY GLY B . n 
B 1 301 ALA 301 301 301 ALA ALA B . n 
B 1 302 ALA 302 302 302 ALA ALA B . n 
B 1 303 THR 303 303 303 THR THR B . n 
B 1 304 LEU 304 304 304 LEU LEU B . n 
B 1 305 PHE 305 305 305 PHE PHE B . n 
B 1 306 TYR 306 306 306 TYR TYR B . n 
B 1 307 PRO 307 307 307 PRO PRO B . n 
B 1 308 MET 308 308 308 MET MET B . n 
B 1 309 TRP 309 309 309 TRP TRP B . n 
B 1 310 HIS 310 310 310 HIS HIS B . n 
B 1 311 LEU 311 311 311 LEU LEU B . n 
B 1 312 GLU 312 312 312 GLU GLU B . n 
B 1 313 VAL 313 313 313 VAL VAL B . n 
B 1 314 GLU 314 314 314 GLU GLU B . n 
B 1 315 SER 315 315 315 SER SER B . n 
B 1 316 LEU 316 316 316 LEU LEU B . n 
B 1 317 LEU 317 317 317 LEU LEU B . n 
B 1 318 VAL 318 318 318 VAL VAL B . n 
B 1 319 LEU 319 319 319 LEU LEU B . n 
B 1 320 LYS 320 320 320 LYS LYS B . n 
B 1 321 ASN 321 321 321 ASN ASN B . n 
B 1 322 ASN 322 322 322 ASN ASN B . n 
B 1 323 ARG 323 323 323 ARG ARG B . n 
B 1 324 GLY 324 324 324 GLY GLY B . n 
B 1 325 VAL 325 325 325 VAL VAL B . n 
B 1 326 GLU 326 326 326 GLU GLU B . n 
B 1 327 GLY 327 327 327 GLY GLY B . n 
B 1 328 ASN 328 328 328 ASN ASN B . n 
B 1 329 ARG 329 329 329 ARG ARG B . n 
B 1 330 VAL 330 330 330 VAL VAL B . n 
B 1 331 ARG 331 331 331 ARG ARG B . n 
B 1 332 HIS 332 332 332 HIS HIS B . n 
B 1 333 MET 333 333 333 MET MET B . n 
B 1 334 ASP 334 334 334 ASP ASP B . n 
B 1 335 TYR 335 335 335 TYR TYR B . n 
B 1 336 GLY 336 336 336 GLY GLY B . n 
B 1 337 VAL 337 337 337 VAL VAL B . n 
B 1 338 GLN 338 338 338 GLN GLN B . n 
B 1 339 ILE 339 339 339 ILE ILE B . n 
B 1 340 ASN 340 340 340 ASN ASN B . n 
B 1 341 LYS 341 341 341 LYS LYS B . n 
B 1 342 LEU 342 342 342 LEU LEU B . n 
B 1 343 MET 343 343 343 MET MET B . n 
B 1 344 TYR 344 344 344 TYR TYR B . n 
B 1 345 THR 345 345 345 THR THR B . n 
B 1 346 ARG 346 346 346 ARG ARG B . n 
B 1 347 LEU 347 347 347 LEU LEU B . n 
B 1 348 LEU 348 348 348 LEU LEU B . n 
B 1 349 LYS 349 349 349 LYS LYS B . n 
B 1 350 GLY 350 350 350 GLY GLY B . n 
B 1 351 GLU 351 351 351 GLU GLU B . n 
B 1 352 ASP 352 352 352 ASP ASP B . n 
B 1 353 ILE 353 353 353 ILE ILE B . n 
B 1 354 THR 354 354 354 THR THR B . n 
B 1 355 LEU 355 355 355 LEU LEU B . n 
B 1 356 PHE 356 356 356 PHE PHE B . n 
B 1 357 SER 357 357 357 SER SER B . n 
B 1 358 PRO 358 358 358 PRO PRO B . n 
B 1 359 SER 359 359 359 SER SER B . n 
B 1 360 ASP 360 360 360 ASP ASP B . n 
B 1 361 VAL 361 361 361 VAL VAL B . n 
B 1 362 PRO 362 362 362 PRO PRO B . n 
B 1 363 GLY 363 363 363 GLY GLY B . n 
B 1 364 LEU 364 364 364 LEU LEU B . n 
B 1 365 TYR 365 365 365 TYR TYR B . n 
B 1 366 ASP 366 366 366 ASP ASP B . n 
B 1 367 ALA 367 367 367 ALA ALA B . n 
B 1 368 PHE 368 368 368 PHE PHE B . n 
B 1 369 PHE 369 369 369 PHE PHE B . n 
B 1 370 ALA 370 370 370 ALA ALA B . n 
B 1 371 ASP 371 371 371 ASP ASP B . n 
B 1 372 GLN 372 372 372 GLN GLN B . n 
B 1 373 GLU 373 373 373 GLU GLU B . n 
B 1 374 GLU 374 374 374 GLU GLU B . n 
B 1 375 PHE 375 375 375 PHE PHE B . n 
B 1 376 GLU 376 376 376 GLU GLU B . n 
B 1 377 ARG 377 377 377 ARG ARG B . n 
B 1 378 LEU 378 378 378 LEU LEU B . n 
B 1 379 TYR 379 379 379 TYR TYR B . n 
B 1 380 THR 380 380 380 THR THR B . n 
B 1 381 LYS 381 381 381 LYS LYS B . n 
B 1 382 TYR 382 382 382 TYR TYR B . n 
B 1 383 GLU 383 383 383 GLU GLU B . n 
B 1 384 LYS 384 384 384 LYS LYS B . n 
B 1 385 ASP 385 385 385 ASP ASP B . n 
B 1 386 ASP 386 386 386 ASP ASP B . n 
B 1 387 SER 387 387 387 SER SER B . n 
B 1 388 ILE 388 388 388 ILE ILE B . n 
B 1 389 ARG 389 389 389 ARG ARG B . n 
B 1 390 LYS 390 390 390 LYS LYS B . n 
B 1 391 GLN 391 391 391 GLN GLN B . n 
B 1 392 ARG 392 392 392 ARG ARG B . n 
B 1 393 VAL 393 393 393 VAL VAL B . n 
B 1 394 LYS 394 394 394 LYS LYS B . n 
B 1 395 ALA 395 395 395 ALA ALA B . n 
B 1 396 VAL 396 396 396 VAL VAL B . n 
B 1 397 GLU 397 397 397 GLU GLU B . n 
B 1 398 LEU 398 398 398 LEU LEU B . n 
B 1 399 PHE 399 399 399 PHE PHE B . n 
B 1 400 SER 400 400 400 SER SER B . n 
B 1 401 LEU 401 401 401 LEU LEU B . n 
B 1 402 MET 402 402 402 MET MET B . n 
B 1 403 MET 403 403 403 MET MET B . n 
B 1 404 GLN 404 404 404 GLN GLN B . n 
B 1 405 GLU 405 405 405 GLU GLU B . n 
B 1 406 ARG 406 406 406 ARG ARG B . n 
B 1 407 ALA 407 407 407 ALA ALA B . n 
B 1 408 SER 408 408 408 SER SER B . n 
B 1 409 THR 409 409 409 THR THR B . n 
B 1 410 GLY 410 410 410 GLY GLY B . n 
B 1 411 ARG 411 411 411 ARG ARG B . n 
B 1 412 ILE 412 412 412 ILE ILE B . n 
B 1 413 TYR 413 413 413 TYR TYR B . n 
B 1 414 ILE 414 414 414 ILE ILE B . n 
B 1 415 GLN 415 415 415 GLN GLN B . n 
B 1 416 ASN 416 416 416 ASN ASN B . n 
B 1 417 VAL 417 417 417 VAL VAL B . n 
B 1 418 ASP 418 418 418 ASP ASP B . n 
B 1 419 HIS 419 419 419 HIS HIS B . n 
B 1 420 CYS 420 420 420 CYS CYS B . n 
B 1 421 ASN 421 421 421 ASN ASN B . n 
B 1 422 THR 422 422 422 THR THR B . n 
B 1 423 HIS 423 423 423 HIS HIS B . n 
B 1 424 SER 424 424 424 SER SER B . n 
B 1 425 PRO 425 425 425 PRO PRO B . n 
B 1 426 PHE 426 426 426 PHE PHE B . n 
B 1 427 ASP 427 427 427 ASP ASP B . n 
B 1 428 PRO 428 428 428 PRO PRO B . n 
B 1 429 ALA 429 429 429 ALA ALA B . n 
B 1 430 ILE 430 430 430 ILE ILE B . n 
B 1 431 ALA 431 431 431 ALA ALA B . n 
B 1 432 PRO 432 432 432 PRO PRO B . n 
B 1 433 VAL 433 433 433 VAL VAL B . n 
B 1 434 ARG 434 434 434 ARG ARG B . n 
B 1 435 GLN 435 435 435 GLN GLN B . n 
B 1 436 SER 436 436 436 SER SER B . n 
B 1 437 ASN 437 437 437 ASN ASN B . n 
B 1 438 LEU 438 438 438 LEU LEU B . n 
B 1 439 CYS 439 439 439 CYS CYS B . n 
B 1 440 LEU 440 440 440 LEU LEU B . n 
B 1 441 GLU 441 441 441 GLU GLU B . n 
B 1 442 ILE 442 442 442 ILE ILE B . n 
B 1 443 ALA 443 443 443 ALA ALA B . n 
B 1 444 LEU 444 444 444 LEU LEU B . n 
B 1 445 PRO 445 445 445 PRO PRO B . n 
B 1 446 THR 446 446 446 THR THR B . n 
B 1 447 LYS 447 447 447 LYS LYS B . n 
B 1 448 PRO 448 448 448 PRO PRO B . n 
B 1 449 LEU 449 449 449 LEU LEU B . n 
B 1 450 ASN 450 450 450 ASN ASN B . n 
B 1 451 ASP 451 451 451 ASP ASP B . n 
B 1 452 VAL 452 452 452 VAL VAL B . n 
B 1 453 ASN 453 453 453 ASN ASN B . n 
B 1 454 ASP 454 454 454 ASP ASP B . n 
B 1 455 GLU 455 455 455 GLU GLU B . n 
B 1 456 ASN 456 456 456 ASN ASN B . n 
B 1 457 GLY 457 457 457 GLY GLY B . n 
B 1 458 GLU 458 458 458 GLU GLU B . n 
B 1 459 ILE 459 459 459 ILE ILE B . n 
B 1 460 ALA 460 460 460 ALA ALA B . n 
B 1 461 LEU 461 461 461 LEU LEU B . n 
B 1 462 CYS 462 462 462 CYS CYS B . n 
B 1 463 THR 463 463 463 THR THR B . n 
B 1 464 LEU 464 464 464 LEU LEU B . n 
B 1 465 SER 465 465 465 SER SER B . n 
B 1 466 ALA 466 466 466 ALA ALA B . n 
B 1 467 PHE 467 467 467 PHE PHE B . n 
B 1 468 ASN 468 468 468 ASN ASN B . n 
B 1 469 LEU 469 469 469 LEU LEU B . n 
B 1 470 GLY 470 470 470 GLY GLY B . n 
B 1 471 ALA 471 471 471 ALA ALA B . n 
B 1 472 ILE 472 472 472 ILE ILE B . n 
B 1 473 ASN 473 473 473 ASN ASN B . n 
B 1 474 ASN 474 474 474 ASN ASN B . n 
B 1 475 LEU 475 475 475 LEU LEU B . n 
B 1 476 ASP 476 476 476 ASP ASP B . n 
B 1 477 GLU 477 477 477 GLU GLU B . n 
B 1 478 LEU 478 478 478 LEU LEU B . n 
B 1 479 GLU 479 479 479 GLU GLU B . n 
B 1 480 GLU 480 480 480 GLU GLU B . n 
B 1 481 LEU 481 481 481 LEU LEU B . n 
B 1 482 ALA 482 482 482 ALA ALA B . n 
B 1 483 ILE 483 483 483 ILE ILE B . n 
B 1 484 LEU 484 484 484 LEU LEU B . n 
B 1 485 ALA 485 485 485 ALA ALA B . n 
B 1 486 VAL 486 486 486 VAL VAL B . n 
B 1 487 ARG 487 487 487 ARG ARG B . n 
B 1 488 ALA 488 488 488 ALA ALA B . n 
B 1 489 LEU 489 489 489 LEU LEU B . n 
B 1 490 ASP 490 490 490 ASP ASP B . n 
B 1 491 ALA 491 491 491 ALA ALA B . n 
B 1 492 LEU 492 492 492 LEU LEU B . n 
B 1 493 LEU 493 493 493 LEU LEU B . n 
B 1 494 ASP 494 494 494 ASP ASP B . n 
B 1 495 TYR 495 495 495 TYR TYR B . n 
B 1 496 GLN 496 496 496 GLN GLN B . n 
B 1 497 ASP 497 497 497 ASP ASP B . n 
B 1 498 TYR 498 498 498 TYR TYR B . n 
B 1 499 PRO 499 499 499 PRO PRO B . n 
B 1 500 ILE 500 500 500 ILE ILE B . n 
B 1 501 PRO 501 501 501 PRO PRO B . n 
B 1 502 ALA 502 502 502 ALA ALA B . n 
B 1 503 ALA 503 503 503 ALA ALA B . n 
B 1 504 LYS 504 504 504 LYS LYS B . n 
B 1 505 ARG 505 505 505 ARG ARG B . n 
B 1 506 GLY 506 506 506 GLY GLY B . n 
B 1 507 ALA 507 507 507 ALA ALA B . n 
B 1 508 MET 508 508 508 MET MET B . n 
B 1 509 GLY 509 509 509 GLY GLY B . n 
B 1 510 ARG 510 510 510 ARG ARG B . n 
B 1 511 ARG 511 511 511 ARG ARG B . n 
B 1 512 THR 512 512 512 THR THR B . n 
B 1 513 LEU 513 513 513 LEU LEU B . n 
B 1 514 GLY 514 514 514 GLY GLY B . n 
B 1 515 ILE 515 515 515 ILE ILE B . n 
B 1 516 GLY 516 516 516 GLY GLY B . n 
B 1 517 VAL 517 517 517 VAL VAL B . n 
B 1 518 ILE 518 518 518 ILE ILE B . n 
B 1 519 ASN 519 519 519 ASN ASN B . n 
B 1 520 PHE 520 520 520 PHE PHE B . n 
B 1 521 ALA 521 521 521 ALA ALA B . n 
B 1 522 TYR 522 522 522 TYR TYR B . n 
B 1 523 TYR 523 523 523 TYR TYR B . n 
B 1 524 LEU 524 524 524 LEU LEU B . n 
B 1 525 ALA 525 525 525 ALA ALA B . n 
B 1 526 LYS 526 526 526 LYS LYS B . n 
B 1 527 HIS 527 527 527 HIS HIS B . n 
B 1 528 GLY 528 528 528 GLY GLY B . n 
B 1 529 LYS 529 529 529 LYS LYS B . n 
B 1 530 ARG 530 530 530 ARG ARG B . n 
B 1 531 TYR 531 531 531 TYR TYR B . n 
B 1 532 SER 532 532 532 SER SER B . n 
B 1 533 ASP 533 533 533 ASP ASP B . n 
B 1 534 GLY 534 534 534 GLY GLY B . n 
B 1 535 SER 535 535 535 SER SER B . n 
B 1 536 ALA 536 536 536 ALA ALA B . n 
B 1 537 ASN 537 537 537 ASN ASN B . n 
B 1 538 ASN 538 538 538 ASN ASN B . n 
B 1 539 LEU 539 539 539 LEU LEU B . n 
B 1 540 THR 540 540 540 THR THR B . n 
B 1 541 HIS 541 541 541 HIS HIS B . n 
B 1 542 LYS 542 542 542 LYS LYS B . n 
B 1 543 THR 543 543 543 THR THR B . n 
B 1 544 PHE 544 544 544 PHE PHE B . n 
B 1 545 GLU 545 545 545 GLU GLU B . n 
B 1 546 ALA 546 546 546 ALA ALA B . n 
B 1 547 ILE 547 547 547 ILE ILE B . n 
B 1 548 GLN 548 548 548 GLN GLN B . n 
B 1 549 TYR 549 549 549 TYR TYR B . n 
B 1 550 TYR 550 550 550 TYR TYR B . n 
B 1 551 LEU 551 551 551 LEU LEU B . n 
B 1 552 LEU 552 552 552 LEU LEU B . n 
B 1 553 LYS 553 553 553 LYS LYS B . n 
B 1 554 ALA 554 554 554 ALA ALA B . n 
B 1 555 SER 555 555 555 SER SER B . n 
B 1 556 ASN 556 556 556 ASN ASN B . n 
B 1 557 GLU 557 557 557 GLU GLU B . n 
B 1 558 LEU 558 558 558 LEU LEU B . n 
B 1 559 ALA 559 559 559 ALA ALA B . n 
B 1 560 LYS 560 560 560 LYS LYS B . n 
B 1 561 GLU 561 561 561 GLU GLU B . n 
B 1 562 GLN 562 562 562 GLN GLN B . n 
B 1 563 GLY 563 563 563 GLY GLY B . n 
B 1 564 ALA 564 564 564 ALA ALA B . n 
B 1 565 CYS 565 565 565 CYS CYS B . n 
B 1 566 PRO 566 566 566 PRO PRO B . n 
B 1 567 TRP 567 567 567 TRP TRP B . n 
B 1 568 PHE 568 568 568 PHE PHE B . n 
B 1 569 ASN 569 569 569 ASN ASN B . n 
B 1 570 GLU 570 570 570 GLU GLU B . n 
B 1 571 THR 571 571 571 THR THR B . n 
B 1 572 THR 572 572 572 THR THR B . n 
B 1 573 TYR 573 573 573 TYR TYR B . n 
B 1 574 ALA 574 574 574 ALA ALA B . n 
B 1 575 LYS 575 575 575 LYS LYS B . n 
B 1 576 GLY 576 576 576 GLY GLY B . n 
B 1 577 ILE 577 577 577 ILE ILE B . n 
B 1 578 LEU 578 578 578 LEU LEU B . n 
B 1 579 PRO 579 579 579 PRO PRO B . n 
B 1 580 ILE 580 580 580 ILE ILE B . n 
B 1 581 ASP 581 581 581 ASP ASP B . n 
B 1 582 THR 582 582 582 THR THR B . n 
B 1 583 TYR 583 583 583 TYR TYR B . n 
B 1 584 LYS 584 584 584 LYS LYS B . n 
B 1 585 LYS 585 585 585 LYS LYS B . n 
B 1 586 ASP 586 586 586 ASP ASP B . n 
B 1 587 LEU 587 587 587 LEU LEU B . n 
B 1 588 ASP 588 588 588 ASP ASP B . n 
B 1 589 THR 589 589 589 THR THR B . n 
B 1 590 ILE 590 590 590 ILE ILE B . n 
B 1 591 ALA 591 591 591 ALA ALA B . n 
B 1 592 ASN 592 592 592 ASN ASN B . n 
B 1 593 GLU 593 593 593 GLU GLU B . n 
B 1 594 PRO 594 594 594 PRO PRO B . n 
B 1 595 LEU 595 595 595 LEU LEU B . n 
B 1 596 HIS 596 596 596 HIS HIS B . n 
B 1 597 TYR 597 597 597 TYR TYR B . n 
B 1 598 ASP 598 598 598 ASP ASP B . n 
B 1 599 TRP 599 599 599 TRP TRP B . n 
B 1 600 GLU 600 600 600 GLU GLU B . n 
B 1 601 ALA 601 601 601 ALA ALA B . n 
B 1 602 LEU 602 602 602 LEU LEU B . n 
B 1 603 ARG 603 603 603 ARG ARG B . n 
B 1 604 GLU 604 604 604 GLU GLU B . n 
B 1 605 SER 605 605 605 SER SER B . n 
B 1 606 ILE 606 606 606 ILE ILE B . n 
B 1 607 LYS 607 607 607 LYS LYS B . n 
B 1 608 THR 608 608 608 THR THR B . n 
B 1 609 HIS 609 609 609 HIS HIS B . n 
B 1 610 GLY 610 610 610 GLY GLY B . n 
B 1 611 LEU 611 611 611 LEU LEU B . n 
B 1 612 ARG 612 612 612 ARG ARG B . n 
B 1 613 ASN 613 613 613 ASN ASN B . n 
B 1 614 SER 614 614 614 SER SER B . n 
B 1 615 THR 615 615 615 THR THR B . n 
B 1 616 LEU 616 616 616 LEU LEU B . n 
B 1 617 SER 617 617 617 SER SER B . n 
B 1 618 ALA 618 618 618 ALA ALA B . n 
B 1 619 LEU 619 619 619 LEU LEU B . n 
B 1 620 MET 620 620 620 MET MET B . n 
B 1 621 PRO 621 621 621 PRO PRO B . n 
B 1 622 SER 622 622 622 SER SER B . n 
B 1 623 GLU 623 623 623 GLU GLU B . n 
B 1 624 THR 624 624 624 THR THR B . n 
B 1 625 SER 625 625 625 SER SER B . n 
B 1 626 SER 626 626 626 SER SER B . n 
B 1 627 GLN 627 627 627 GLN GLN B . n 
B 1 628 ILE 628 628 628 ILE ILE B . n 
B 1 629 SER 629 629 629 SER SER B . n 
B 1 630 ASN 630 630 630 ASN ASN B . n 
B 1 631 ALA 631 631 631 ALA ALA B . n 
B 1 632 THR 632 632 632 THR THR B . n 
B 1 633 ASN 633 633 633 ASN ASN B . n 
B 1 634 GLY 634 634 634 GLY GLY B . n 
B 1 635 ILE 635 635 635 ILE ILE B . n 
B 1 636 GLU 636 636 636 GLU GLU B . n 
B 1 637 PRO 637 637 637 PRO PRO B . n 
B 1 638 PRO 638 638 638 PRO PRO B . n 
B 1 639 ARG 639 639 639 ARG ARG B . n 
B 1 640 GLY 640 640 640 GLY GLY B . n 
B 1 641 TYR 641 641 641 TYR TYR B . n 
B 1 642 VAL 642 642 642 VAL VAL B . n 
B 1 643 SER 643 643 643 SER SER B . n 
B 1 644 ILE 644 644 644 ILE ILE B . n 
B 1 645 LYS 645 645 645 LYS LYS B . n 
B 1 646 ALA 646 646 646 ALA ALA B . n 
B 1 647 SER 647 647 647 SER SER B . n 
B 1 648 LYS 648 648 648 LYS LYS B . n 
B 1 649 ASP 649 649 649 ASP ASP B . n 
B 1 650 GLY 650 650 650 GLY GLY B . n 
B 1 651 ILE 651 651 651 ILE ILE B . n 
B 1 652 LEU 652 652 652 LEU LEU B . n 
B 1 653 ARG 653 653 653 ARG ARG B . n 
B 1 654 GLN 654 654 654 GLN GLN B . n 
B 1 655 VAL 655 655 655 VAL VAL B . n 
B 1 656 VAL 656 656 656 VAL VAL B . n 
B 1 657 PRO 657 657 657 PRO PRO B . n 
B 1 658 ASP 658 658 658 ASP ASP B . n 
B 1 659 TYR 659 659 659 TYR TYR B . n 
B 1 660 GLU 660 660 660 GLU GLU B . n 
B 1 661 HIS 661 661 661 HIS HIS B . n 
B 1 662 LEU 662 662 662 LEU LEU B . n 
B 1 663 HIS 663 663 663 HIS HIS B . n 
B 1 664 ASP 664 664 664 ASP ASP B . n 
B 1 665 ALA 665 665 665 ALA ALA B . n 
B 1 666 TYR 666 666 666 TYR TYR B . n 
B 1 667 GLU 667 667 667 GLU GLU B . n 
B 1 668 LEU 668 668 668 LEU LEU B . n 
B 1 669 LEU 669 669 669 LEU LEU B . n 
B 1 670 TRP 670 670 670 TRP TRP B . n 
B 1 671 GLU 671 671 671 GLU GLU B . n 
B 1 672 MET 672 672 672 MET MET B . n 
B 1 673 PRO 673 673 673 PRO PRO B . n 
B 1 674 GLY 674 674 674 GLY GLY B . n 
B 1 675 ASN 675 675 675 ASN ASN B . n 
B 1 676 ASP 676 676 676 ASP ASP B . n 
B 1 677 GLY 677 677 677 GLY GLY B . n 
B 1 678 TYR 678 678 678 TYR TYR B . n 
B 1 679 LEU 679 679 679 LEU LEU B . n 
B 1 680 GLN 680 680 680 GLN GLN B . n 
B 1 681 LEU 681 681 681 LEU LEU B . n 
B 1 682 VAL 682 682 682 VAL VAL B . n 
B 1 683 GLY 683 683 683 GLY GLY B . n 
B 1 684 ILE 684 684 684 ILE ILE B . n 
B 1 685 MET 685 685 685 MET MET B . n 
B 1 686 GLN 686 686 686 GLN GLN B . n 
B 1 687 LYS 687 687 687 LYS LYS B . n 
B 1 688 PHE 688 688 688 PHE PHE B . n 
B 1 689 ILE 689 689 689 ILE ILE B . n 
B 1 690 ASP 690 690 690 ASP ASP B . n 
B 1 691 GLN 691 691 691 GLN GLN B . n 
B 1 692 SER 692 692 692 SER SER B . n 
B 1 693 ILE 693 693 693 ILE ILE B . n 
B 1 694 SER 694 694 694 SER SER B . n 
B 1 695 ALA 695 695 695 ALA ALA B . n 
B 1 696 ASN 696 696 696 ASN ASN B . n 
B 1 697 THR 697 697 697 THR THR B . n 
B 1 698 ASN 698 698 698 ASN ASN B . n 
B 1 699 TYR 699 699 699 TYR TYR B . n 
B 1 700 ASP 700 700 700 ASP ASP B . n 
B 1 701 PRO 701 701 701 PRO PRO B . n 
B 1 702 SER 702 702 702 SER SER B . n 
B 1 703 ARG 703 703 703 ARG ARG B . n 
B 1 704 PHE 704 704 704 PHE PHE B . n 
B 1 705 PRO 705 705 705 PRO PRO B . n 
B 1 706 SER 706 706 706 SER SER B . n 
B 1 707 GLY 707 707 707 GLY GLY B . n 
B 1 708 LYS 708 708 708 LYS LYS B . n 
B 1 709 VAL 709 709 709 VAL VAL B . n 
B 1 710 PRO 710 710 710 PRO PRO B . n 
B 1 711 MET 711 711 711 MET MET B . n 
B 1 712 GLN 712 712 712 GLN GLN B . n 
B 1 713 GLN 713 713 713 GLN GLN B . n 
B 1 714 LEU 714 714 714 LEU LEU B . n 
B 1 715 LEU 715 715 715 LEU LEU B . n 
B 1 716 LYS 716 716 716 LYS LYS B . n 
B 1 717 ASP 717 717 717 ASP ASP B . n 
B 1 718 LEU 718 718 718 LEU LEU B . n 
B 1 719 LEU 719 719 719 LEU LEU B . n 
B 1 720 THR 720 720 720 THR THR B . n 
B 1 721 ALA 721 721 721 ALA ALA B . n 
B 1 722 TYR 722 722 722 TYR TYR B . n 
B 1 723 LYS 723 723 723 LYS LYS B . n 
B 1 724 PHE 724 724 724 PHE PHE B . n 
B 1 725 GLY 725 725 725 GLY GLY B . n 
B 1 726 VAL 726 726 726 VAL VAL B . n 
B 1 727 LYS 727 727 727 LYS LYS B . n 
B 1 728 THR 728 728 728 THR THR B . n 
B 1 729 LEU 729 729 729 LEU LEU B . n 
B 1 730 TYR 730 730 730 TYR TYR B . n 
B 1 731 TYR 731 731 731 TYR TYR B . n 
B 1 732 GLN 732 732 732 GLN GLN B . n 
B 1 733 ASN 733 733 733 ASN ASN B . n 
B 1 734 THR 734 734 734 THR THR B . n 
B 1 735 ARG 735 735 735 ARG ARG B . n 
B 1 736 ASP 736 736 736 ASP ASP B . n 
B 1 737 GLY 737 737 737 GLY GLY B . n 
B 1 738 ALA 738 738 738 ALA ALA B . n 
B 1 739 GLU 739 739 739 GLU GLU B . n 
B 1 740 ASP 740 740 740 ASP ASP B . n 
B 1 741 ALA 741 741 741 ALA ALA B . n 
B 1 742 GLN 742 742 742 GLN GLN B . n 
B 1 743 ASP 743 743 743 ASP ASP B . n 
B 1 744 ASP 744 744 744 ASP ASP B . n 
B 1 745 LEU 745 745 745 LEU LEU B . n 
B 1 746 VAL 746 746 ?   ?   ?   B . n 
B 1 747 PRO 747 747 ?   ?   ?   B . n 
B 1 748 SER 748 748 ?   ?   ?   B . n 
B 1 749 ILE 749 749 ?   ?   ?   B . n 
B 1 750 GLN 750 750 ?   ?   ?   B . n 
B 1 751 ASP 751 751 ?   ?   ?   B . n 
B 1 752 ASP 752 752 ?   ?   ?   B . n 
B 1 753 GLY 753 753 ?   ?   ?   B . n 
B 1 754 CYS 754 754 ?   ?   ?   B . n 
B 1 755 GLU 755 755 ?   ?   ?   B . n 
B 1 756 SER 756 756 ?   ?   ?   B . n 
B 1 757 GLY 757 757 ?   ?   ?   B . n 
B 1 758 ALA 758 758 ?   ?   ?   B . n 
B 1 759 CYS 759 759 ?   ?   ?   B . n 
B 1 760 LYS 760 760 ?   ?   ?   B . n 
B 1 761 ILE 761 761 ?   ?   ?   B . n 
C 2 1   MET 1   0   ?   ?   ?   C . n 
C 2 2   ALA 2   1   1   ALA ALA C . n 
C 2 3   TYR 3   2   2   TYR TYR C . n 
C 2 4   THR 4   3   3   THR THR C . n 
C 2 5   THR 5   4   4   THR THR C . n 
C 2 6   PHE 6   5   5   PHE PHE C . n 
C 2 7   SER 7   6   6   SER SER C . n 
C 2 8   GLN 8   7   7   GLN GLN C . n 
C 2 9   THR 9   8   8   THR THR C . n 
C 2 10  LYS 10  9   9   LYS LYS C . n 
C 2 11  ASN 11  10  10  ASN ASN C . n 
C 2 12  ASP 12  11  11  ASP ASP C . n 
C 2 13  GLN 13  12  12  GLN GLN C . n 
C 2 14  LEU 14  13  13  LEU LEU C . n 
C 2 15  LYS 15  14  14  LYS LYS C . n 
C 2 16  GLU 16  15  15  GLU GLU C . n 
C 2 17  PRO 17  16  16  PRO PRO C . n 
C 2 18  MET 18  17  17  MET MET C . n 
C 2 19  PHE 19  18  18  PHE PHE C . n 
C 2 20  PHE 20  19  19  PHE PHE C . n 
C 2 21  GLY 21  20  20  GLY GLY C . n 
C 2 22  GLN 22  21  21  GLN GLN C . n 
C 2 23  PRO 23  22  22  PRO PRO C . n 
C 2 24  VAL 24  23  23  VAL VAL C . n 
C 2 25  ASN 25  24  24  ASN ASN C . n 
C 2 26  VAL 26  25  25  VAL VAL C . n 
C 2 27  ALA 27  26  26  ALA ALA C . n 
C 2 28  ARG 28  27  27  ARG ARG C . n 
C 2 29  TYR 29  28  28  TYR TYR C . n 
C 2 30  ASP 30  29  29  ASP ASP C . n 
C 2 31  GLN 31  30  30  GLN GLN C . n 
C 2 32  GLN 32  31  31  GLN GLN C . n 
C 2 33  LYS 33  32  32  LYS LYS C . n 
C 2 34  TYR 34  33  33  TYR TYR C . n 
C 2 35  ASP 35  34  34  ASP ASP C . n 
C 2 36  ILE 36  35  35  ILE ILE C . n 
C 2 37  PHE 37  36  36  PHE PHE C . n 
C 2 38  GLU 38  37  37  GLU GLU C . n 
C 2 39  LYS 39  38  38  LYS LYS C . n 
C 2 40  LEU 40  39  39  LEU LEU C . n 
C 2 41  ILE 41  40  40  ILE ILE C . n 
C 2 42  GLU 42  41  41  GLU GLU C . n 
C 2 43  LYS 43  42  42  LYS LYS C . n 
C 2 44  GLN 44  43  43  GLN GLN C . n 
C 2 45  LEU 45  44  44  LEU LEU C . n 
C 2 46  SER 46  45  45  SER SER C . n 
C 2 47  PHE 47  46  46  PHE PHE C . n 
C 2 48  PHE 48  47  47  PHE PHE C . n 
C 2 49  TRP 49  48  48  TRP TRP C . n 
C 2 50  ARG 50  49  49  ARG ARG C . n 
C 2 51  PRO 51  50  50  PRO PRO C . n 
C 2 52  GLU 52  51  51  GLU GLU C . n 
C 2 53  GLU 53  52  52  GLU GLU C . n 
C 2 54  VAL 54  53  53  VAL VAL C . n 
C 2 55  ASP 55  54  54  ASP ASP C . n 
C 2 56  VAL 56  55  55  VAL VAL C . n 
C 2 57  SER 57  56  56  SER SER C . n 
C 2 58  ARG 58  57  57  ARG ARG C . n 
C 2 59  ASP 59  58  58  ASP ASP C . n 
C 2 60  ARG 60  59  59  ARG ARG C . n 
C 2 61  ILE 61  60  60  ILE ILE C . n 
C 2 62  ASP 62  61  61  ASP ASP C . n 
C 2 63  TYR 63  62  62  TYR TYR C . n 
C 2 64  GLN 64  63  63  GLN GLN C . n 
C 2 65  ALA 65  64  64  ALA ALA C . n 
C 2 66  LEU 66  65  65  LEU LEU C . n 
C 2 67  PRO 67  66  66  PRO PRO C . n 
C 2 68  GLU 68  67  67  GLU GLU C . n 
C 2 69  HIS 69  68  68  HIS HIS C . n 
C 2 70  GLU 70  69  69  GLU GLU C . n 
C 2 71  LYS 71  70  70  LYS LYS C . n 
C 2 72  HIS 72  71  71  HIS HIS C . n 
C 2 73  ILE 73  72  72  ILE ILE C . n 
C 2 74  PHE 74  73  73  PHE PHE C . n 
C 2 75  ILE 75  74  74  ILE ILE C . n 
C 2 76  SER 76  75  75  SER SER C . n 
C 2 77  ASN 77  76  76  ASN ASN C . n 
C 2 78  LEU 78  77  77  LEU LEU C . n 
C 2 79  LYS 79  78  78  LYS LYS C . n 
C 2 80  TYR 80  79  79  TYR TYR C . n 
C 2 81  GLN 81  80  80  GLN GLN C . n 
C 2 82  THR 82  81  81  THR THR C . n 
C 2 83  LEU 83  82  82  LEU LEU C . n 
C 2 84  LEU 84  83  83  LEU LEU C . n 
C 2 85  ASP 85  84  84  ASP ASP C . n 
C 2 86  SER 86  85  85  SER SER C . n 
C 2 87  ILE 87  86  86  ILE ILE C . n 
C 2 88  GLN 88  87  87  GLN GLN C . n 
C 2 89  GLY 89  88  88  GLY GLY C . n 
C 2 90  ARG 90  89  89  ARG ARG C . n 
C 2 91  SER 91  90  90  SER SER C . n 
C 2 92  PRO 92  91  91  PRO PRO C . n 
C 2 93  ASN 93  92  92  ASN ASN C . n 
C 2 94  VAL 94  93  93  VAL VAL C . n 
C 2 95  ALA 95  94  94  ALA ALA C . n 
C 2 96  LEU 96  95  95  LEU LEU C . n 
C 2 97  LEU 97  96  96  LEU LEU C . n 
C 2 98  PRO 98  97  97  PRO PRO C . n 
C 2 99  LEU 99  98  98  LEU LEU C . n 
C 2 100 ILE 100 99  99  ILE ILE C . n 
C 2 101 SER 101 100 100 SER SER C . n 
C 2 102 ILE 102 101 101 ILE ILE C . n 
C 2 103 PRO 103 102 102 PRO PRO C . n 
C 2 104 GLU 104 103 103 GLU GLU C . n 
C 2 105 LEU 105 104 104 LEU LEU C . n 
C 2 106 GLU 106 105 105 GLU GLU C . n 
C 2 107 THR 107 106 106 THR THR C . n 
C 2 108 TRP 108 107 107 TRP TRP C . n 
C 2 109 VAL 109 108 108 VAL VAL C . n 
C 2 110 GLU 110 109 109 GLU GLU C . n 
C 2 111 THR 111 110 110 THR THR C . n 
C 2 112 TRP 112 111 111 TRP TRP C . n 
C 2 113 ALA 113 112 112 ALA ALA C . n 
C 2 114 PHE 114 113 113 PHE PHE C . n 
C 2 115 SER 115 114 114 SER SER C . n 
C 2 116 GLU 116 115 115 GLU GLU C . n 
C 2 117 THR 117 116 116 THR THR C . n 
C 2 118 ILE 118 117 117 ILE ILE C . n 
C 2 119 HIS 119 118 118 HIS HIS C . n 
C 2 120 SER 120 119 119 SER SER C . n 
C 2 121 ARG 121 120 120 ARG ARG C . n 
C 2 122 SER 122 121 121 SER SER C . n 
C 2 123 TYR 123 122 122 TYR TYR C . n 
C 2 124 THR 124 123 123 THR THR C . n 
C 2 125 HIS 125 124 124 HIS HIS C . n 
C 2 126 ILE 126 125 125 ILE ILE C . n 
C 2 127 ILE 127 126 126 ILE ILE C . n 
C 2 128 ARG 128 127 127 ARG ARG C . n 
C 2 129 ASN 129 128 128 ASN ASN C . n 
C 2 130 ILE 130 129 129 ILE ILE C . n 
C 2 131 VAL 131 130 130 VAL VAL C . n 
C 2 132 ASN 132 131 131 ASN ASN C . n 
C 2 133 ASP 133 132 132 ASP ASP C . n 
C 2 134 PRO 134 133 133 PRO PRO C . n 
C 2 135 SER 135 134 134 SER SER C . n 
C 2 136 VAL 136 135 135 VAL VAL C . n 
C 2 137 VAL 137 136 136 VAL VAL C . n 
C 2 138 PHE 138 137 137 PHE PHE C . n 
C 2 139 ASP 139 138 138 ASP ASP C . n 
C 2 140 ASP 140 139 139 ASP ASP C . n 
C 2 141 ILE 141 140 140 ILE ILE C . n 
C 2 142 VAL 142 141 141 VAL VAL C . n 
C 2 143 THR 143 142 142 THR THR C . n 
C 2 144 ASN 144 143 143 ASN ASN C . n 
C 2 145 GLU 145 144 144 GLU GLU C . n 
C 2 146 GLN 146 145 145 GLN GLN C . n 
C 2 147 ILE 147 146 146 ILE ILE C . n 
C 2 148 GLN 148 147 147 GLN GLN C . n 
C 2 149 LYS 149 148 148 LYS LYS C . n 
C 2 150 ARG 150 149 149 ARG ARG C . n 
C 2 151 ALA 151 150 150 ALA ALA C . n 
C 2 152 GLU 152 151 151 GLU GLU C . n 
C 2 153 GLY 153 152 152 GLY GLY C . n 
C 2 154 ILE 154 153 153 ILE ILE C . n 
C 2 155 SER 155 154 154 SER SER C . n 
C 2 156 SER 156 155 155 SER SER C . n 
C 2 157 TYR 157 156 156 TYR TYR C . n 
C 2 158 TYR 158 157 157 TYR TYR C . n 
C 2 159 ASP 159 158 158 ASP ASP C . n 
C 2 160 GLU 160 159 159 GLU GLU C . n 
C 2 161 LEU 161 160 160 LEU LEU C . n 
C 2 162 ILE 162 161 161 ILE ILE C . n 
C 2 163 GLU 163 162 162 GLU GLU C . n 
C 2 164 MET 164 163 163 MET MET C . n 
C 2 165 THR 165 164 164 THR THR C . n 
C 2 166 SER 166 165 165 SER SER C . n 
C 2 167 TYR 167 166 166 TYR TYR C . n 
C 2 168 TRP 168 167 167 TRP TRP C . n 
C 2 169 HIS 169 168 168 HIS HIS C . n 
C 2 170 LEU 170 169 169 LEU LEU C . n 
C 2 171 LEU 171 170 170 LEU LEU C . n 
C 2 172 GLY 172 171 171 GLY GLY C . n 
C 2 173 GLU 173 172 172 GLU GLU C . n 
C 2 174 GLY 174 173 173 GLY GLY C . n 
C 2 175 THR 175 174 174 THR THR C . n 
C 2 176 HIS 176 175 175 HIS HIS C . n 
C 2 177 THR 177 176 176 THR THR C . n 
C 2 178 VAL 178 177 177 VAL VAL C . n 
C 2 179 ASN 179 178 178 ASN ASN C . n 
C 2 180 GLY 180 179 179 GLY GLY C . n 
C 2 181 LYS 181 180 180 LYS LYS C . n 
C 2 182 THR 182 181 181 THR THR C . n 
C 2 183 VAL 183 182 182 VAL VAL C . n 
C 2 184 THR 184 183 183 THR THR C . n 
C 2 185 VAL 185 184 184 VAL VAL C . n 
C 2 186 SER 186 185 185 SER SER C . n 
C 2 187 LEU 187 186 186 LEU LEU C . n 
C 2 188 ARG 188 187 187 ARG ARG C . n 
C 2 189 GLU 189 188 188 GLU GLU C . n 
C 2 190 LEU 190 189 189 LEU LEU C . n 
C 2 191 LYS 191 190 190 LYS LYS C . n 
C 2 192 LYS 192 191 191 LYS LYS C . n 
C 2 193 LYS 193 192 192 LYS LYS C . n 
C 2 194 LEU 194 193 193 LEU LEU C . n 
C 2 195 TYR 195 194 194 TYR TYR C . n 
C 2 196 LEU 196 195 195 LEU LEU C . n 
C 2 197 CYS 197 196 196 CYS CYS C . n 
C 2 198 LEU 198 197 197 LEU LEU C . n 
C 2 199 MET 199 198 198 MET MET C . n 
C 2 200 SER 200 199 199 SER SER C . n 
C 2 201 VAL 201 200 200 VAL VAL C . n 
C 2 202 ASN 202 201 201 ASN ASN C . n 
C 2 203 ALA 203 202 202 ALA ALA C . n 
C 2 204 LEU 204 203 203 LEU LEU C . n 
C 2 205 GLU 205 204 204 GLU GLU C . n 
C 2 206 ALA 206 205 205 ALA ALA C . n 
C 2 207 ILE 207 206 206 ILE ILE C . n 
C 2 208 ARG 208 207 207 ARG ARG C . n 
C 2 209 PHE 209 208 208 PHE PHE C . n 
C 2 210 TYR 210 209 209 TYR TYR C . n 
C 2 211 VAL 211 210 210 VAL VAL C . n 
C 2 212 SER 212 211 211 SER SER C . n 
C 2 213 PHE 213 212 212 PHE PHE C . n 
C 2 214 ALA 214 213 213 ALA ALA C . n 
C 2 215 CYS 215 214 214 CYS CYS C . n 
C 2 216 SER 216 215 215 SER SER C . n 
C 2 217 PHE 217 216 216 PHE PHE C . n 
C 2 218 ALA 218 217 217 ALA ALA C . n 
C 2 219 PHE 219 218 218 PHE PHE C . n 
C 2 220 ALA 220 219 219 ALA ALA C . n 
C 2 221 GLU 221 220 220 GLU GLU C . n 
C 2 222 ARG 222 221 221 ARG ARG C . n 
C 2 223 GLU 223 222 222 GLU GLU C . n 
C 2 224 LEU 224 223 223 LEU LEU C . n 
C 2 225 MET 225 224 224 MET MET C . n 
C 2 226 GLU 226 225 225 GLU GLU C . n 
C 2 227 GLY 227 226 226 GLY GLY C . n 
C 2 228 ASN 228 227 227 ASN ASN C . n 
C 2 229 ALA 229 228 228 ALA ALA C . n 
C 2 230 LYS 230 229 229 LYS LYS C . n 
C 2 231 ILE 231 230 230 ILE ILE C . n 
C 2 232 ILE 232 231 231 ILE ILE C . n 
C 2 233 ARG 233 232 232 ARG ARG C . n 
C 2 234 LEU 234 233 233 LEU LEU C . n 
C 2 235 ILE 235 234 234 ILE ILE C . n 
C 2 236 ALA 236 235 235 ALA ALA C . n 
C 2 237 ARG 237 236 236 ARG ARG C . n 
C 2 238 ASP 238 237 237 ASP ASP C . n 
C 2 239 GLU 239 238 238 GLU GLU C . n 
C 2 240 ALA 240 239 239 ALA ALA C . n 
C 2 241 LEU 241 240 240 LEU LEU C . n 
C 2 242 HIS 242 241 241 HIS HIS C . n 
C 2 243 LEU 243 242 242 LEU LEU C . n 
C 2 244 THR 244 243 243 THR THR C . n 
C 2 245 GLY 245 244 244 GLY GLY C . n 
C 2 246 THR 246 245 245 THR THR C . n 
C 2 247 GLN 247 246 246 GLN GLN C . n 
C 2 248 HIS 248 247 247 HIS HIS C . n 
C 2 249 MET 249 248 248 MET MET C . n 
C 2 250 LEU 250 249 249 LEU LEU C . n 
C 2 251 ASN 251 250 250 ASN ASN C . n 
C 2 252 LEU 252 251 251 LEU LEU C . n 
C 2 253 LEU 253 252 252 LEU LEU C . n 
C 2 254 ARG 254 253 253 ARG ARG C . n 
C 2 255 SER 255 254 254 SER SER C . n 
C 2 256 GLY 256 255 255 GLY GLY C . n 
C 2 257 ALA 257 256 256 ALA ALA C . n 
C 2 258 ASP 258 257 257 ASP ASP C . n 
C 2 259 ASP 259 258 258 ASP ASP C . n 
C 2 260 PRO 260 259 259 PRO PRO C . n 
C 2 261 GLU 261 260 260 GLU GLU C . n 
C 2 262 MET 262 261 261 MET MET C . n 
C 2 263 ALA 263 262 262 ALA ALA C . n 
C 2 264 GLU 264 263 263 GLU GLU C . n 
C 2 265 ILE 265 264 264 ILE ILE C . n 
C 2 266 ALA 266 265 265 ALA ALA C . n 
C 2 267 GLU 267 266 266 GLU GLU C . n 
C 2 268 GLU 268 267 267 GLU GLU C . n 
C 2 269 CYS 269 268 268 CYS CYS C . n 
C 2 270 LYS 270 269 269 LYS LYS C . n 
C 2 271 GLN 271 270 270 GLN GLN C . n 
C 2 272 GLU 272 271 271 GLU GLU C . n 
C 2 273 CYS 273 272 272 CYS CYS C . n 
C 2 274 TYR 274 273 273 TYR TYR C . n 
C 2 275 ASP 275 274 274 ASP ASP C . n 
C 2 276 LEU 276 275 275 LEU LEU C . n 
C 2 277 PHE 277 276 276 PHE PHE C . n 
C 2 278 VAL 278 277 277 VAL VAL C . n 
C 2 279 GLN 279 278 278 GLN GLN C . n 
C 2 280 ALA 280 279 279 ALA ALA C . n 
C 2 281 ALA 281 280 280 ALA ALA C . n 
C 2 282 GLN 282 281 281 GLN GLN C . n 
C 2 283 GLN 283 282 282 GLN GLN C . n 
C 2 284 GLU 284 283 283 GLU GLU C . n 
C 2 285 LYS 285 284 284 LYS LYS C . n 
C 2 286 ASP 286 285 285 ASP ASP C . n 
C 2 287 TRP 287 286 286 TRP TRP C . n 
C 2 288 ALA 288 287 287 ALA ALA C . n 
C 2 289 ASP 289 288 288 ASP ASP C . n 
C 2 290 TYR 290 289 289 TYR TYR C . n 
C 2 291 LEU 291 290 290 LEU LEU C . n 
C 2 292 PHE 292 291 291 PHE PHE C . n 
C 2 293 ARG 293 292 292 ARG ARG C . n 
C 2 294 ASP 294 293 293 ASP ASP C . n 
C 2 295 GLY 295 294 294 GLY GLY C . n 
C 2 296 SER 296 295 295 SER SER C . n 
C 2 297 MET 297 296 296 MET MET C . n 
C 2 298 ILE 298 297 297 ILE ILE C . n 
C 2 299 GLY 299 298 298 GLY GLY C . n 
C 2 300 LEU 300 299 299 LEU LEU C . n 
C 2 301 ASN 301 300 300 ASN ASN C . n 
C 2 302 LYS 302 301 301 LYS LYS C . n 
C 2 303 ASP 303 302 302 ASP ASP C . n 
C 2 304 ILE 304 303 303 ILE ILE C . n 
C 2 305 LEU 305 304 304 LEU LEU C . n 
C 2 306 CYS 306 305 305 CYS CYS C . n 
C 2 307 GLN 307 306 306 GLN GLN C . n 
C 2 308 TYR 308 307 307 TYR TYR C . n 
C 2 309 VAL 309 308 308 VAL VAL C . n 
C 2 310 GLU 310 309 309 GLU GLU C . n 
C 2 311 TYR 311 310 310 TYR TYR C . n 
C 2 312 ILE 312 311 311 ILE ILE C . n 
C 2 313 THR 313 312 312 THR THR C . n 
C 2 314 ASN 314 313 313 ASN ASN C . n 
C 2 315 ILE 315 314 314 ILE ILE C . n 
C 2 316 ARG 316 315 315 ARG ARG C . n 
C 2 317 MET 317 316 316 MET MET C . n 
C 2 318 GLN 318 317 317 GLN GLN C . n 
C 2 319 ALA 319 318 318 ALA ALA C . n 
C 2 320 VAL 320 319 319 VAL VAL C . n 
C 2 321 GLY 321 320 320 GLY GLY C . n 
C 2 322 LEU 322 321 321 LEU LEU C . n 
C 2 323 ASP 323 322 322 ASP ASP C . n 
C 2 324 LEU 324 323 323 LEU LEU C . n 
C 2 325 PRO 325 324 324 PRO PRO C . n 
C 2 326 PHE 326 325 325 PHE PHE C . n 
C 2 327 GLN 327 326 326 GLN GLN C . n 
C 2 328 THR 328 327 327 THR THR C . n 
C 2 329 ARG 329 328 328 ARG ARG C . n 
C 2 330 SER 330 329 329 SER SER C . n 
C 2 331 ASN 331 330 330 ASN ASN C . n 
C 2 332 PRO 332 331 331 PRO PRO C . n 
C 2 333 ILE 333 332 332 ILE ILE C . n 
C 2 334 PRO 334 333 333 PRO PRO C . n 
C 2 335 TRP 335 334 334 TRP TRP C . n 
C 2 336 ILE 336 335 335 ILE ILE C . n 
C 2 337 ASN 337 336 336 ASN ASN C . n 
C 2 338 THR 338 337 337 THR THR C . n 
C 2 339 TRP 339 338 338 TRP TRP C . n 
C 2 340 LEU 340 339 339 LEU LEU C . n 
C 2 341 VAL 341 340 340 VAL VAL C . n 
C 2 342 SER 342 341 341 SER SER C . n 
C 2 343 ASP 343 342 342 ASP ASP C . n 
C 2 344 ASN 344 343 343 ASN ASN C . n 
C 2 345 VAL 345 344 344 VAL VAL C . n 
C 2 346 GLN 346 345 345 GLN GLN C . n 
C 2 347 VAL 347 346 346 VAL VAL C . n 
C 2 348 ALA 348 347 347 ALA ALA C . n 
C 2 349 PRO 349 348 348 PRO PRO C . n 
C 2 350 GLN 350 349 349 GLN GLN C . n 
C 2 351 GLU 351 350 350 GLU GLU C . n 
C 2 352 VAL 352 351 351 VAL VAL C . n 
C 2 353 GLU 353 352 352 GLU GLU C . n 
C 2 354 VAL 354 353 353 VAL VAL C . n 
C 2 355 SER 355 354 354 SER SER C . n 
C 2 356 SER 356 355 355 SER SER C . n 
C 2 357 TYR 357 356 356 TYR TYR C . n 
C 2 358 LEU 358 357 357 LEU LEU C . n 
C 2 359 VAL 359 358 358 VAL VAL C . n 
C 2 360 GLY 360 359 359 GLY GLY C . n 
C 2 361 GLN 361 360 360 GLN GLN C . n 
C 2 362 ILE 362 361 361 ILE ILE C . n 
C 2 363 ASP 363 362 362 ASP ASP C . n 
C 2 364 SER 364 363 363 SER SER C . n 
C 2 365 GLU 365 364 364 GLU GLU C . n 
C 2 366 VAL 366 365 365 VAL VAL C . n 
C 2 367 ASP 367 366 366 ASP ASP C . n 
C 2 368 THR 368 367 367 THR THR C . n 
C 2 369 ASP 369 368 368 ASP ASP C . n 
C 2 370 ASP 370 369 369 ASP ASP C . n 
C 2 371 LEU 371 370 370 LEU LEU C . n 
C 2 372 SER 372 371 371 SER SER C . n 
C 2 373 ASN 373 372 372 ASN ASN C . n 
C 2 374 PHE 374 373 373 PHE PHE C . n 
C 2 375 GLN 375 374 374 GLN GLN C . n 
C 2 376 LEU 376 375 375 LEU LEU C . n 
D 2 1   MET 1   0   ?   ?   ?   D . n 
D 2 2   ALA 2   1   1   ALA ALA D . n 
D 2 3   TYR 3   2   2   TYR TYR D . n 
D 2 4   THR 4   3   3   THR THR D . n 
D 2 5   THR 5   4   4   THR THR D . n 
D 2 6   PHE 6   5   5   PHE PHE D . n 
D 2 7   SER 7   6   6   SER SER D . n 
D 2 8   GLN 8   7   7   GLN GLN D . n 
D 2 9   THR 9   8   8   THR THR D . n 
D 2 10  LYS 10  9   9   LYS LYS D . n 
D 2 11  ASN 11  10  10  ASN ASN D . n 
D 2 12  ASP 12  11  11  ASP ASP D . n 
D 2 13  GLN 13  12  12  GLN GLN D . n 
D 2 14  LEU 14  13  13  LEU LEU D . n 
D 2 15  LYS 15  14  14  LYS LYS D . n 
D 2 16  GLU 16  15  15  GLU GLU D . n 
D 2 17  PRO 17  16  16  PRO PRO D . n 
D 2 18  MET 18  17  17  MET MET D . n 
D 2 19  PHE 19  18  18  PHE PHE D . n 
D 2 20  PHE 20  19  19  PHE PHE D . n 
D 2 21  GLY 21  20  20  GLY GLY D . n 
D 2 22  GLN 22  21  21  GLN GLN D . n 
D 2 23  PRO 23  22  22  PRO PRO D . n 
D 2 24  VAL 24  23  23  VAL VAL D . n 
D 2 25  ASN 25  24  24  ASN ASN D . n 
D 2 26  VAL 26  25  25  VAL VAL D . n 
D 2 27  ALA 27  26  26  ALA ALA D . n 
D 2 28  ARG 28  27  27  ARG ARG D . n 
D 2 29  TYR 29  28  28  TYR TYR D . n 
D 2 30  ASP 30  29  29  ASP ASP D . n 
D 2 31  GLN 31  30  30  GLN GLN D . n 
D 2 32  GLN 32  31  31  GLN GLN D . n 
D 2 33  LYS 33  32  32  LYS LYS D . n 
D 2 34  TYR 34  33  33  TYR TYR D . n 
D 2 35  ASP 35  34  34  ASP ASP D . n 
D 2 36  ILE 36  35  35  ILE ILE D . n 
D 2 37  PHE 37  36  36  PHE PHE D . n 
D 2 38  GLU 38  37  37  GLU GLU D . n 
D 2 39  LYS 39  38  38  LYS LYS D . n 
D 2 40  LEU 40  39  39  LEU LEU D . n 
D 2 41  ILE 41  40  40  ILE ILE D . n 
D 2 42  GLU 42  41  41  GLU GLU D . n 
D 2 43  LYS 43  42  42  LYS LYS D . n 
D 2 44  GLN 44  43  43  GLN GLN D . n 
D 2 45  LEU 45  44  44  LEU LEU D . n 
D 2 46  SER 46  45  45  SER SER D . n 
D 2 47  PHE 47  46  46  PHE PHE D . n 
D 2 48  PHE 48  47  47  PHE PHE D . n 
D 2 49  TRP 49  48  48  TRP TRP D . n 
D 2 50  ARG 50  49  49  ARG ARG D . n 
D 2 51  PRO 51  50  50  PRO PRO D . n 
D 2 52  GLU 52  51  51  GLU GLU D . n 
D 2 53  GLU 53  52  52  GLU GLU D . n 
D 2 54  VAL 54  53  53  VAL VAL D . n 
D 2 55  ASP 55  54  54  ASP ASP D . n 
D 2 56  VAL 56  55  55  VAL VAL D . n 
D 2 57  SER 57  56  56  SER SER D . n 
D 2 58  ARG 58  57  57  ARG ARG D . n 
D 2 59  ASP 59  58  58  ASP ASP D . n 
D 2 60  ARG 60  59  59  ARG ARG D . n 
D 2 61  ILE 61  60  60  ILE ILE D . n 
D 2 62  ASP 62  61  61  ASP ASP D . n 
D 2 63  TYR 63  62  62  TYR TYR D . n 
D 2 64  GLN 64  63  63  GLN GLN D . n 
D 2 65  ALA 65  64  64  ALA ALA D . n 
D 2 66  LEU 66  65  65  LEU LEU D . n 
D 2 67  PRO 67  66  66  PRO PRO D . n 
D 2 68  GLU 68  67  67  GLU GLU D . n 
D 2 69  HIS 69  68  68  HIS HIS D . n 
D 2 70  GLU 70  69  69  GLU GLU D . n 
D 2 71  LYS 71  70  70  LYS LYS D . n 
D 2 72  HIS 72  71  71  HIS HIS D . n 
D 2 73  ILE 73  72  72  ILE ILE D . n 
D 2 74  PHE 74  73  73  PHE PHE D . n 
D 2 75  ILE 75  74  74  ILE ILE D . n 
D 2 76  SER 76  75  75  SER SER D . n 
D 2 77  ASN 77  76  76  ASN ASN D . n 
D 2 78  LEU 78  77  77  LEU LEU D . n 
D 2 79  LYS 79  78  78  LYS LYS D . n 
D 2 80  TYR 80  79  79  TYR TYR D . n 
D 2 81  GLN 81  80  80  GLN GLN D . n 
D 2 82  THR 82  81  81  THR THR D . n 
D 2 83  LEU 83  82  82  LEU LEU D . n 
D 2 84  LEU 84  83  83  LEU LEU D . n 
D 2 85  ASP 85  84  84  ASP ASP D . n 
D 2 86  SER 86  85  85  SER SER D . n 
D 2 87  ILE 87  86  86  ILE ILE D . n 
D 2 88  GLN 88  87  87  GLN GLN D . n 
D 2 89  GLY 89  88  88  GLY GLY D . n 
D 2 90  ARG 90  89  89  ARG ARG D . n 
D 2 91  SER 91  90  90  SER SER D . n 
D 2 92  PRO 92  91  91  PRO PRO D . n 
D 2 93  ASN 93  92  92  ASN ASN D . n 
D 2 94  VAL 94  93  93  VAL VAL D . n 
D 2 95  ALA 95  94  94  ALA ALA D . n 
D 2 96  LEU 96  95  95  LEU LEU D . n 
D 2 97  LEU 97  96  96  LEU LEU D . n 
D 2 98  PRO 98  97  97  PRO PRO D . n 
D 2 99  LEU 99  98  98  LEU LEU D . n 
D 2 100 ILE 100 99  99  ILE ILE D . n 
D 2 101 SER 101 100 100 SER SER D . n 
D 2 102 ILE 102 101 101 ILE ILE D . n 
D 2 103 PRO 103 102 102 PRO PRO D . n 
D 2 104 GLU 104 103 103 GLU GLU D . n 
D 2 105 LEU 105 104 104 LEU LEU D . n 
D 2 106 GLU 106 105 105 GLU GLU D . n 
D 2 107 THR 107 106 106 THR THR D . n 
D 2 108 TRP 108 107 107 TRP TRP D . n 
D 2 109 VAL 109 108 108 VAL VAL D . n 
D 2 110 GLU 110 109 109 GLU GLU D . n 
D 2 111 THR 111 110 110 THR THR D . n 
D 2 112 TRP 112 111 111 TRP TRP D . n 
D 2 113 ALA 113 112 112 ALA ALA D . n 
D 2 114 PHE 114 113 113 PHE PHE D . n 
D 2 115 SER 115 114 114 SER SER D . n 
D 2 116 GLU 116 115 115 GLU GLU D . n 
D 2 117 THR 117 116 116 THR THR D . n 
D 2 118 ILE 118 117 117 ILE ILE D . n 
D 2 119 HIS 119 118 118 HIS HIS D . n 
D 2 120 SER 120 119 119 SER SER D . n 
D 2 121 ARG 121 120 120 ARG ARG D . n 
D 2 122 SER 122 121 121 SER SER D . n 
D 2 123 TYR 123 122 122 TYR TYR D . n 
D 2 124 THR 124 123 123 THR THR D . n 
D 2 125 HIS 125 124 124 HIS HIS D . n 
D 2 126 ILE 126 125 125 ILE ILE D . n 
D 2 127 ILE 127 126 126 ILE ILE D . n 
D 2 128 ARG 128 127 127 ARG ARG D . n 
D 2 129 ASN 129 128 128 ASN ASN D . n 
D 2 130 ILE 130 129 129 ILE ILE D . n 
D 2 131 VAL 131 130 130 VAL VAL D . n 
D 2 132 ASN 132 131 131 ASN ASN D . n 
D 2 133 ASP 133 132 132 ASP ASP D . n 
D 2 134 PRO 134 133 133 PRO PRO D . n 
D 2 135 SER 135 134 134 SER SER D . n 
D 2 136 VAL 136 135 135 VAL VAL D . n 
D 2 137 VAL 137 136 136 VAL VAL D . n 
D 2 138 PHE 138 137 137 PHE PHE D . n 
D 2 139 ASP 139 138 138 ASP ASP D . n 
D 2 140 ASP 140 139 139 ASP ASP D . n 
D 2 141 ILE 141 140 140 ILE ILE D . n 
D 2 142 VAL 142 141 141 VAL VAL D . n 
D 2 143 THR 143 142 142 THR THR D . n 
D 2 144 ASN 144 143 143 ASN ASN D . n 
D 2 145 GLU 145 144 144 GLU GLU D . n 
D 2 146 GLN 146 145 145 GLN GLN D . n 
D 2 147 ILE 147 146 146 ILE ILE D . n 
D 2 148 GLN 148 147 147 GLN GLN D . n 
D 2 149 LYS 149 148 148 LYS LYS D . n 
D 2 150 ARG 150 149 149 ARG ARG D . n 
D 2 151 ALA 151 150 150 ALA ALA D . n 
D 2 152 GLU 152 151 151 GLU GLU D . n 
D 2 153 GLY 153 152 152 GLY GLY D . n 
D 2 154 ILE 154 153 153 ILE ILE D . n 
D 2 155 SER 155 154 154 SER SER D . n 
D 2 156 SER 156 155 155 SER SER D . n 
D 2 157 TYR 157 156 156 TYR TYR D . n 
D 2 158 TYR 158 157 157 TYR TYR D . n 
D 2 159 ASP 159 158 158 ASP ASP D . n 
D 2 160 GLU 160 159 159 GLU GLU D . n 
D 2 161 LEU 161 160 160 LEU LEU D . n 
D 2 162 ILE 162 161 161 ILE ILE D . n 
D 2 163 GLU 163 162 162 GLU GLU D . n 
D 2 164 MET 164 163 163 MET MET D . n 
D 2 165 THR 165 164 164 THR THR D . n 
D 2 166 SER 166 165 165 SER SER D . n 
D 2 167 TYR 167 166 166 TYR TYR D . n 
D 2 168 TRP 168 167 167 TRP TRP D . n 
D 2 169 HIS 169 168 168 HIS HIS D . n 
D 2 170 LEU 170 169 169 LEU LEU D . n 
D 2 171 LEU 171 170 170 LEU LEU D . n 
D 2 172 GLY 172 171 171 GLY GLY D . n 
D 2 173 GLU 173 172 172 GLU GLU D . n 
D 2 174 GLY 174 173 173 GLY GLY D . n 
D 2 175 THR 175 174 174 THR THR D . n 
D 2 176 HIS 176 175 175 HIS HIS D . n 
D 2 177 THR 177 176 176 THR THR D . n 
D 2 178 VAL 178 177 177 VAL VAL D . n 
D 2 179 ASN 179 178 178 ASN ASN D . n 
D 2 180 GLY 180 179 179 GLY GLY D . n 
D 2 181 LYS 181 180 180 LYS LYS D . n 
D 2 182 THR 182 181 181 THR THR D . n 
D 2 183 VAL 183 182 182 VAL VAL D . n 
D 2 184 THR 184 183 183 THR THR D . n 
D 2 185 VAL 185 184 184 VAL VAL D . n 
D 2 186 SER 186 185 185 SER SER D . n 
D 2 187 LEU 187 186 186 LEU LEU D . n 
D 2 188 ARG 188 187 187 ARG ARG D . n 
D 2 189 GLU 189 188 188 GLU GLU D . n 
D 2 190 LEU 190 189 189 LEU LEU D . n 
D 2 191 LYS 191 190 190 LYS LYS D . n 
D 2 192 LYS 192 191 191 LYS LYS D . n 
D 2 193 LYS 193 192 192 LYS LYS D . n 
D 2 194 LEU 194 193 193 LEU LEU D . n 
D 2 195 TYR 195 194 194 TYR TYR D . n 
D 2 196 LEU 196 195 195 LEU LEU D . n 
D 2 197 CYS 197 196 196 CYS CYS D . n 
D 2 198 LEU 198 197 197 LEU LEU D . n 
D 2 199 MET 199 198 198 MET MET D . n 
D 2 200 SER 200 199 199 SER SER D . n 
D 2 201 VAL 201 200 200 VAL VAL D . n 
D 2 202 ASN 202 201 201 ASN ASN D . n 
D 2 203 ALA 203 202 202 ALA ALA D . n 
D 2 204 LEU 204 203 203 LEU LEU D . n 
D 2 205 GLU 205 204 204 GLU GLU D . n 
D 2 206 ALA 206 205 205 ALA ALA D . n 
D 2 207 ILE 207 206 206 ILE ILE D . n 
D 2 208 ARG 208 207 207 ARG ARG D . n 
D 2 209 PHE 209 208 208 PHE PHE D . n 
D 2 210 TYR 210 209 209 TYR TYR D . n 
D 2 211 VAL 211 210 210 VAL VAL D . n 
D 2 212 SER 212 211 211 SER SER D . n 
D 2 213 PHE 213 212 212 PHE PHE D . n 
D 2 214 ALA 214 213 213 ALA ALA D . n 
D 2 215 CYS 215 214 214 CYS CYS D . n 
D 2 216 SER 216 215 215 SER SER D . n 
D 2 217 PHE 217 216 216 PHE PHE D . n 
D 2 218 ALA 218 217 217 ALA ALA D . n 
D 2 219 PHE 219 218 218 PHE PHE D . n 
D 2 220 ALA 220 219 219 ALA ALA D . n 
D 2 221 GLU 221 220 220 GLU GLU D . n 
D 2 222 ARG 222 221 221 ARG ARG D . n 
D 2 223 GLU 223 222 222 GLU GLU D . n 
D 2 224 LEU 224 223 223 LEU LEU D . n 
D 2 225 MET 225 224 224 MET MET D . n 
D 2 226 GLU 226 225 225 GLU GLU D . n 
D 2 227 GLY 227 226 226 GLY GLY D . n 
D 2 228 ASN 228 227 227 ASN ASN D . n 
D 2 229 ALA 229 228 228 ALA ALA D . n 
D 2 230 LYS 230 229 229 LYS LYS D . n 
D 2 231 ILE 231 230 230 ILE ILE D . n 
D 2 232 ILE 232 231 231 ILE ILE D . n 
D 2 233 ARG 233 232 232 ARG ARG D . n 
D 2 234 LEU 234 233 233 LEU LEU D . n 
D 2 235 ILE 235 234 234 ILE ILE D . n 
D 2 236 ALA 236 235 235 ALA ALA D . n 
D 2 237 ARG 237 236 236 ARG ARG D . n 
D 2 238 ASP 238 237 237 ASP ASP D . n 
D 2 239 GLU 239 238 238 GLU GLU D . n 
D 2 240 ALA 240 239 239 ALA ALA D . n 
D 2 241 LEU 241 240 240 LEU LEU D . n 
D 2 242 HIS 242 241 241 HIS HIS D . n 
D 2 243 LEU 243 242 242 LEU LEU D . n 
D 2 244 THR 244 243 243 THR THR D . n 
D 2 245 GLY 245 244 244 GLY GLY D . n 
D 2 246 THR 246 245 245 THR THR D . n 
D 2 247 GLN 247 246 246 GLN GLN D . n 
D 2 248 HIS 248 247 247 HIS HIS D . n 
D 2 249 MET 249 248 248 MET MET D . n 
D 2 250 LEU 250 249 249 LEU LEU D . n 
D 2 251 ASN 251 250 250 ASN ASN D . n 
D 2 252 LEU 252 251 251 LEU LEU D . n 
D 2 253 LEU 253 252 252 LEU LEU D . n 
D 2 254 ARG 254 253 253 ARG ARG D . n 
D 2 255 SER 255 254 254 SER SER D . n 
D 2 256 GLY 256 255 255 GLY GLY D . n 
D 2 257 ALA 257 256 256 ALA ALA D . n 
D 2 258 ASP 258 257 257 ASP ASP D . n 
D 2 259 ASP 259 258 258 ASP ASP D . n 
D 2 260 PRO 260 259 259 PRO PRO D . n 
D 2 261 GLU 261 260 260 GLU GLU D . n 
D 2 262 MET 262 261 261 MET MET D . n 
D 2 263 ALA 263 262 262 ALA ALA D . n 
D 2 264 GLU 264 263 263 GLU GLU D . n 
D 2 265 ILE 265 264 264 ILE ILE D . n 
D 2 266 ALA 266 265 265 ALA ALA D . n 
D 2 267 GLU 267 266 266 GLU GLU D . n 
D 2 268 GLU 268 267 267 GLU GLU D . n 
D 2 269 CYS 269 268 268 CYS CYS D . n 
D 2 270 LYS 270 269 269 LYS LYS D . n 
D 2 271 GLN 271 270 270 GLN GLN D . n 
D 2 272 GLU 272 271 271 GLU GLU D . n 
D 2 273 CYS 273 272 272 CYS CYS D . n 
D 2 274 TYR 274 273 273 TYR TYR D . n 
D 2 275 ASP 275 274 274 ASP ASP D . n 
D 2 276 LEU 276 275 275 LEU LEU D . n 
D 2 277 PHE 277 276 276 PHE PHE D . n 
D 2 278 VAL 278 277 277 VAL VAL D . n 
D 2 279 GLN 279 278 278 GLN GLN D . n 
D 2 280 ALA 280 279 279 ALA ALA D . n 
D 2 281 ALA 281 280 280 ALA ALA D . n 
D 2 282 GLN 282 281 281 GLN GLN D . n 
D 2 283 GLN 283 282 282 GLN GLN D . n 
D 2 284 GLU 284 283 283 GLU GLU D . n 
D 2 285 LYS 285 284 284 LYS LYS D . n 
D 2 286 ASP 286 285 285 ASP ASP D . n 
D 2 287 TRP 287 286 286 TRP TRP D . n 
D 2 288 ALA 288 287 287 ALA ALA D . n 
D 2 289 ASP 289 288 288 ASP ASP D . n 
D 2 290 TYR 290 289 289 TYR TYR D . n 
D 2 291 LEU 291 290 290 LEU LEU D . n 
D 2 292 PHE 292 291 291 PHE PHE D . n 
D 2 293 ARG 293 292 292 ARG ARG D . n 
D 2 294 ASP 294 293 293 ASP ASP D . n 
D 2 295 GLY 295 294 294 GLY GLY D . n 
D 2 296 SER 296 295 295 SER SER D . n 
D 2 297 MET 297 296 296 MET MET D . n 
D 2 298 ILE 298 297 297 ILE ILE D . n 
D 2 299 GLY 299 298 298 GLY GLY D . n 
D 2 300 LEU 300 299 299 LEU LEU D . n 
D 2 301 ASN 301 300 300 ASN ASN D . n 
D 2 302 LYS 302 301 301 LYS LYS D . n 
D 2 303 ASP 303 302 302 ASP ASP D . n 
D 2 304 ILE 304 303 303 ILE ILE D . n 
D 2 305 LEU 305 304 304 LEU LEU D . n 
D 2 306 CYS 306 305 305 CYS CYS D . n 
D 2 307 GLN 307 306 306 GLN GLN D . n 
D 2 308 TYR 308 307 307 TYR TYR D . n 
D 2 309 VAL 309 308 308 VAL VAL D . n 
D 2 310 GLU 310 309 309 GLU GLU D . n 
D 2 311 TYR 311 310 310 TYR TYR D . n 
D 2 312 ILE 312 311 311 ILE ILE D . n 
D 2 313 THR 313 312 312 THR THR D . n 
D 2 314 ASN 314 313 313 ASN ASN D . n 
D 2 315 ILE 315 314 314 ILE ILE D . n 
D 2 316 ARG 316 315 315 ARG ARG D . n 
D 2 317 MET 317 316 316 MET MET D . n 
D 2 318 GLN 318 317 317 GLN GLN D . n 
D 2 319 ALA 319 318 318 ALA ALA D . n 
D 2 320 VAL 320 319 319 VAL VAL D . n 
D 2 321 GLY 321 320 320 GLY GLY D . n 
D 2 322 LEU 322 321 321 LEU LEU D . n 
D 2 323 ASP 323 322 322 ASP ASP D . n 
D 2 324 LEU 324 323 323 LEU LEU D . n 
D 2 325 PRO 325 324 324 PRO PRO D . n 
D 2 326 PHE 326 325 325 PHE PHE D . n 
D 2 327 GLN 327 326 326 GLN GLN D . n 
D 2 328 THR 328 327 327 THR THR D . n 
D 2 329 ARG 329 328 328 ARG ARG D . n 
D 2 330 SER 330 329 329 SER SER D . n 
D 2 331 ASN 331 330 330 ASN ASN D . n 
D 2 332 PRO 332 331 331 PRO PRO D . n 
D 2 333 ILE 333 332 332 ILE ILE D . n 
D 2 334 PRO 334 333 333 PRO PRO D . n 
D 2 335 TRP 335 334 334 TRP TRP D . n 
D 2 336 ILE 336 335 335 ILE ILE D . n 
D 2 337 ASN 337 336 336 ASN ASN D . n 
D 2 338 THR 338 337 337 THR THR D . n 
D 2 339 TRP 339 338 338 TRP TRP D . n 
D 2 340 LEU 340 339 339 LEU LEU D . n 
D 2 341 VAL 341 340 ?   ?   ?   D . n 
D 2 342 SER 342 341 ?   ?   ?   D . n 
D 2 343 ASP 343 342 ?   ?   ?   D . n 
D 2 344 ASN 344 343 ?   ?   ?   D . n 
D 2 345 VAL 345 344 ?   ?   ?   D . n 
D 2 346 GLN 346 345 ?   ?   ?   D . n 
D 2 347 VAL 347 346 ?   ?   ?   D . n 
D 2 348 ALA 348 347 ?   ?   ?   D . n 
D 2 349 PRO 349 348 ?   ?   ?   D . n 
D 2 350 GLN 350 349 ?   ?   ?   D . n 
D 2 351 GLU 351 350 ?   ?   ?   D . n 
D 2 352 VAL 352 351 ?   ?   ?   D . n 
D 2 353 GLU 353 352 ?   ?   ?   D . n 
D 2 354 VAL 354 353 ?   ?   ?   D . n 
D 2 355 SER 355 354 ?   ?   ?   D . n 
D 2 356 SER 356 355 ?   ?   ?   D . n 
D 2 357 TYR 357 356 ?   ?   ?   D . n 
D 2 358 LEU 358 357 ?   ?   ?   D . n 
D 2 359 VAL 359 358 ?   ?   ?   D . n 
D 2 360 GLY 360 359 ?   ?   ?   D . n 
D 2 361 GLN 361 360 360 GLN GLN D . n 
D 2 362 ILE 362 361 361 ILE ILE D . n 
D 2 363 ASP 363 362 362 ASP ASP D . n 
D 2 364 SER 364 363 363 SER SER D . n 
D 2 365 GLU 365 364 364 GLU GLU D . n 
D 2 366 VAL 366 365 365 VAL VAL D . n 
D 2 367 ASP 367 366 366 ASP ASP D . n 
D 2 368 THR 368 367 367 THR THR D . n 
D 2 369 ASP 369 368 368 ASP ASP D . n 
D 2 370 ASP 370 369 369 ASP ASP D . n 
D 2 371 LEU 371 370 370 LEU LEU D . n 
D 2 372 SER 372 371 371 SER SER D . n 
D 2 373 ASN 373 372 372 ASN ASN D . n 
D 2 374 PHE 374 373 373 PHE PHE D . n 
D 2 375 GLN 375 374 ?   ?   ?   D . n 
D 2 376 LEU 376 375 ?   ?   ?   D . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 ATP   ? ? ATP   ? ? 'SUBJECT OF INVESTIGATION' ? 
2 DTP   ? ? DTP   ? ? 'SUBJECT OF INVESTIGATION' ? 
3 FEO   ? ? FEO   ? ? 'SUBJECT OF INVESTIGATION' ? 
4 UNL   ? ? UNL   ? ? 'SUBJECT OF INVESTIGATION' ? 
5 A1A3L ? ? A1A3L ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 
E 3 DTP   1   801  762 DTP   DTP A . 
F 4 MG    1   802  763 MG    MG  A . 
G 5 ATP   1   803  764 ATP   ATP A . 
H 5 ATP   1   804  765 ATP   ATP A . 
I 4 MG    1   805  766 MG    MG  A . 
J 6 UNL   1   806  772 UNL   N   A . 
K 5 ATP   1   801  762 ATP   ATP B . 
L 5 ATP   1   802  763 ATP   ATP B . 
M 3 DTP   1   803  764 DTP   DTP B . 
N 4 MG    1   804  765 MG    MG  B . 
O 4 MG    1   805  766 MG    MG  B . 
P 7 A1A3L 1   806  767 A1A3L NC1 B . 
Q 8 FEO   1   401  401 FEO   FEO C . 
R 8 FEO   1   401  401 FEO   FEO D . 
S 9 HOH   1   901  395 HOH   HOH A . 
S 9 HOH   2   902  463 HOH   HOH A . 
S 9 HOH   3   903  513 HOH   HOH A . 
S 9 HOH   4   904  438 HOH   HOH A . 
S 9 HOH   5   905  404 HOH   HOH A . 
S 9 HOH   6   906  466 HOH   HOH A . 
S 9 HOH   7   907  31  HOH   HOH A . 
S 9 HOH   8   908  530 HOH   HOH A . 
S 9 HOH   9   909  165 HOH   HOH A . 
S 9 HOH   10  910  527 HOH   HOH A . 
S 9 HOH   11  911  603 HOH   HOH A . 
S 9 HOH   12  912  457 HOH   HOH A . 
S 9 HOH   13  913  592 HOH   HOH A . 
S 9 HOH   14  914  501 HOH   HOH A . 
S 9 HOH   15  915  477 HOH   HOH A . 
S 9 HOH   16  916  138 HOH   HOH A . 
S 9 HOH   17  917  37  HOH   HOH A . 
S 9 HOH   18  918  525 HOH   HOH A . 
S 9 HOH   19  919  450 HOH   HOH A . 
S 9 HOH   20  920  440 HOH   HOH A . 
S 9 HOH   21  921  449 HOH   HOH A . 
S 9 HOH   22  922  28  HOH   HOH A . 
S 9 HOH   23  923  511 HOH   HOH A . 
S 9 HOH   24  924  465 HOH   HOH A . 
S 9 HOH   25  925  478 HOH   HOH A . 
S 9 HOH   26  926  572 HOH   HOH A . 
S 9 HOH   27  927  464 HOH   HOH A . 
S 9 HOH   28  928  30  HOH   HOH A . 
S 9 HOH   29  929  442 HOH   HOH A . 
S 9 HOH   30  930  509 HOH   HOH A . 
S 9 HOH   31  931  770 HOH   HOH A . 
S 9 HOH   32  932  484 HOH   HOH A . 
S 9 HOH   33  933  475 HOH   HOH A . 
S 9 HOH   34  934  508 HOH   HOH A . 
S 9 HOH   35  935  529 HOH   HOH A . 
S 9 HOH   36  936  499 HOH   HOH A . 
S 9 HOH   37  937  78  HOH   HOH A . 
S 9 HOH   38  938  447 HOH   HOH A . 
S 9 HOH   39  939  487 HOH   HOH A . 
S 9 HOH   40  940  91  HOH   HOH A . 
S 9 HOH   41  941  460 HOH   HOH A . 
S 9 HOH   42  942  512 HOH   HOH A . 
S 9 HOH   43  943  494 HOH   HOH A . 
S 9 HOH   44  944  771 HOH   HOH A . 
S 9 HOH   45  945  125 HOH   HOH A . 
S 9 HOH   46  946  451 HOH   HOH A . 
S 9 HOH   47  947  485 HOH   HOH A . 
S 9 HOH   48  948  467 HOH   HOH A . 
S 9 HOH   49  949  142 HOH   HOH A . 
S 9 HOH   50  950  459 HOH   HOH A . 
S 9 HOH   51  951  587 HOH   HOH A . 
S 9 HOH   52  952  437 HOH   HOH A . 
S 9 HOH   53  953  482 HOH   HOH A . 
S 9 HOH   54  954  575 HOH   HOH A . 
S 9 HOH   55  955  471 HOH   HOH A . 
S 9 HOH   56  956  503 HOH   HOH A . 
S 9 HOH   57  957  61  HOH   HOH A . 
S 9 HOH   58  958  579 HOH   HOH A . 
S 9 HOH   59  959  146 HOH   HOH A . 
S 9 HOH   60  960  443 HOH   HOH A . 
S 9 HOH   61  961  476 HOH   HOH A . 
S 9 HOH   62  962  111 HOH   HOH A . 
S 9 HOH   63  963  36  HOH   HOH A . 
S 9 HOH   64  964  455 HOH   HOH A . 
S 9 HOH   65  965  559 HOH   HOH A . 
S 9 HOH   66  966  117 HOH   HOH A . 
S 9 HOH   67  967  114 HOH   HOH A . 
S 9 HOH   68  968  93  HOH   HOH A . 
S 9 HOH   69  969  522 HOH   HOH A . 
S 9 HOH   70  970  23  HOH   HOH A . 
S 9 HOH   71  971  490 HOH   HOH A . 
S 9 HOH   72  972  441 HOH   HOH A . 
S 9 HOH   73  973  461 HOH   HOH A . 
S 9 HOH   74  974  302 HOH   HOH A . 
S 9 HOH   75  975  495 HOH   HOH A . 
S 9 HOH   76  976  33  HOH   HOH A . 
S 9 HOH   77  977  502 HOH   HOH A . 
S 9 HOH   78  978  108 HOH   HOH A . 
S 9 HOH   79  979  444 HOH   HOH A . 
S 9 HOH   80  980  448 HOH   HOH A . 
S 9 HOH   81  981  604 HOH   HOH A . 
S 9 HOH   82  982  1   HOH   HOH A . 
S 9 HOH   83  983  470 HOH   HOH A . 
S 9 HOH   84  984  769 HOH   HOH A . 
S 9 HOH   85  985  104 HOH   HOH A . 
S 9 HOH   86  986  500 HOH   HOH A . 
S 9 HOH   87  987  601 HOH   HOH A . 
S 9 HOH   88  988  11  HOH   HOH A . 
S 9 HOH   89  989  47  HOH   HOH A . 
S 9 HOH   90  990  187 HOH   HOH A . 
S 9 HOH   91  991  473 HOH   HOH A . 
S 9 HOH   92  992  436 HOH   HOH A . 
S 9 HOH   93  993  573 HOH   HOH A . 
S 9 HOH   94  994  458 HOH   HOH A . 
S 9 HOH   95  995  605 HOH   HOH A . 
S 9 HOH   96  996  492 HOH   HOH A . 
S 9 HOH   97  997  582 HOH   HOH A . 
S 9 HOH   98  998  64  HOH   HOH A . 
S 9 HOH   99  999  600 HOH   HOH A . 
S 9 HOH   100 1000 15  HOH   HOH A . 
S 9 HOH   101 1001 483 HOH   HOH A . 
S 9 HOH   102 1002 514 HOH   HOH A . 
S 9 HOH   103 1003 452 HOH   HOH A . 
S 9 HOH   104 1004 534 HOH   HOH A . 
S 9 HOH   105 1005 560 HOH   HOH A . 
S 9 HOH   106 1006 112 HOH   HOH A . 
S 9 HOH   107 1007 160 HOH   HOH A . 
S 9 HOH   108 1008 462 HOH   HOH A . 
S 9 HOH   109 1009 163 HOH   HOH A . 
S 9 HOH   110 1010 486 HOH   HOH A . 
S 9 HOH   111 1011 585 HOH   HOH A . 
S 9 HOH   112 1012 472 HOH   HOH A . 
S 9 HOH   113 1013 446 HOH   HOH A . 
S 9 HOH   114 1014 598 HOH   HOH A . 
S 9 HOH   115 1015 44  HOH   HOH A . 
S 9 HOH   116 1016 456 HOH   HOH A . 
S 9 HOH   117 1017 506 HOH   HOH A . 
S 9 HOH   118 1018 480 HOH   HOH A . 
S 9 HOH   119 1019 602 HOH   HOH A . 
S 9 HOH   120 1020 517 HOH   HOH A . 
S 9 HOH   121 1021 491 HOH   HOH A . 
S 9 HOH   122 1022 81  HOH   HOH A . 
S 9 HOH   123 1023 41  HOH   HOH A . 
S 9 HOH   124 1024 515 HOH   HOH A . 
S 9 HOH   125 1025 454 HOH   HOH A . 
S 9 HOH   126 1026 516 HOH   HOH A . 
S 9 HOH   127 1027 136 HOH   HOH A . 
S 9 HOH   128 1028 198 HOH   HOH A . 
S 9 HOH   129 1029 518 HOH   HOH A . 
S 9 HOH   130 1030 103 HOH   HOH A . 
S 9 HOH   131 1031 445 HOH   HOH A . 
S 9 HOH   132 1032 520 HOH   HOH A . 
S 9 HOH   133 1033 599 HOH   HOH A . 
S 9 HOH   134 1034 591 HOH   HOH A . 
S 9 HOH   135 1035 510 HOH   HOH A . 
S 9 HOH   136 1036 9   HOH   HOH A . 
S 9 HOH   137 1037 489 HOH   HOH A . 
S 9 HOH   138 1038 174 HOH   HOH A . 
S 9 HOH   139 1039 504 HOH   HOH A . 
S 9 HOH   140 1040 581 HOH   HOH A . 
S 9 HOH   141 1041 474 HOH   HOH A . 
S 9 HOH   142 1042 251 HOH   HOH A . 
S 9 HOH   143 1043 277 HOH   HOH A . 
S 9 HOH   144 1044 597 HOH   HOH A . 
S 9 HOH   145 1045 469 HOH   HOH A . 
S 9 HOH   146 1046 479 HOH   HOH A . 
S 9 HOH   147 1047 144 HOH   HOH A . 
S 9 HOH   148 1048 580 HOH   HOH A . 
S 9 HOH   149 1049 8   HOH   HOH A . 
S 9 HOH   150 1050 498 HOH   HOH A . 
T 9 HOH   1   901  328 HOH   HOH B . 
T 9 HOH   2   902  351 HOH   HOH B . 
T 9 HOH   3   903  321 HOH   HOH B . 
T 9 HOH   4   904  308 HOH   HOH B . 
T 9 HOH   5   905  617 HOH   HOH B . 
T 9 HOH   6   906  303 HOH   HOH B . 
T 9 HOH   7   907  332 HOH   HOH B . 
T 9 HOH   8   908  353 HOH   HOH B . 
T 9 HOH   9   909  311 HOH   HOH B . 
T 9 HOH   10  910  315 HOH   HOH B . 
T 9 HOH   11  911  285 HOH   HOH B . 
T 9 HOH   12  912  344 HOH   HOH B . 
T 9 HOH   13  913  173 HOH   HOH B . 
T 9 HOH   14  914  519 HOH   HOH B . 
T 9 HOH   15  915  538 HOH   HOH B . 
T 9 HOH   16  916  316 HOH   HOH B . 
T 9 HOH   17  917  338 HOH   HOH B . 
T 9 HOH   18  918  393 HOH   HOH B . 
T 9 HOH   19  919  143 HOH   HOH B . 
T 9 HOH   20  920  434 HOH   HOH B . 
T 9 HOH   21  921  83  HOH   HOH B . 
T 9 HOH   22  922  69  HOH   HOH B . 
T 9 HOH   23  923  354 HOH   HOH B . 
T 9 HOH   24  924  537 HOH   HOH B . 
T 9 HOH   25  925  90  HOH   HOH B . 
T 9 HOH   26  926  540 HOH   HOH B . 
T 9 HOH   27  927  92  HOH   HOH B . 
T 9 HOH   28  928  616 HOH   HOH B . 
T 9 HOH   29  929  370 HOH   HOH B . 
T 9 HOH   30  930  607 HOH   HOH B . 
T 9 HOH   31  931  288 HOH   HOH B . 
T 9 HOH   32  932  505 HOH   HOH B . 
T 9 HOH   33  933  128 HOH   HOH B . 
T 9 HOH   34  934  385 HOH   HOH B . 
T 9 HOH   35  935  335 HOH   HOH B . 
T 9 HOH   36  936  184 HOH   HOH B . 
T 9 HOH   37  937  96  HOH   HOH B . 
T 9 HOH   38  938  209 HOH   HOH B . 
T 9 HOH   39  939  371 HOH   HOH B . 
T 9 HOH   40  940  390 HOH   HOH B . 
T 9 HOH   41  941  343 HOH   HOH B . 
T 9 HOH   42  942  417 HOH   HOH B . 
T 9 HOH   43  943  359 HOH   HOH B . 
T 9 HOH   44  944  423 HOH   HOH B . 
T 9 HOH   45  945  429 HOH   HOH B . 
T 9 HOH   46  946  49  HOH   HOH B . 
T 9 HOH   47  947  58  HOH   HOH B . 
T 9 HOH   48  948  618 HOH   HOH B . 
T 9 HOH   49  949  323 HOH   HOH B . 
T 9 HOH   50  950  432 HOH   HOH B . 
T 9 HOH   51  951  574 HOH   HOH B . 
T 9 HOH   52  952  426 HOH   HOH B . 
T 9 HOH   53  953  413 HOH   HOH B . 
T 9 HOH   54  954  155 HOH   HOH B . 
T 9 HOH   55  955  67  HOH   HOH B . 
T 9 HOH   56  956  570 HOH   HOH B . 
T 9 HOH   57  957  387 HOH   HOH B . 
T 9 HOH   58  958  422 HOH   HOH B . 
T 9 HOH   59  959  411 HOH   HOH B . 
T 9 HOH   60  960  330 HOH   HOH B . 
T 9 HOH   61  961  297 HOH   HOH B . 
T 9 HOH   62  962  358 HOH   HOH B . 
T 9 HOH   63  963  102 HOH   HOH B . 
T 9 HOH   64  964  337 HOH   HOH B . 
T 9 HOH   65  965  488 HOH   HOH B . 
T 9 HOH   66  966  420 HOH   HOH B . 
T 9 HOH   67  967  152 HOH   HOH B . 
T 9 HOH   68  968  94  HOH   HOH B . 
T 9 HOH   69  969  356 HOH   HOH B . 
T 9 HOH   70  970  419 HOH   HOH B . 
T 9 HOH   71  971  333 HOH   HOH B . 
T 9 HOH   72  972  72  HOH   HOH B . 
T 9 HOH   73  973  384 HOH   HOH B . 
T 9 HOH   74  974  109 HOH   HOH B . 
T 9 HOH   75  975  276 HOH   HOH B . 
T 9 HOH   76  976  362 HOH   HOH B . 
T 9 HOH   77  977  610 HOH   HOH B . 
T 9 HOH   78  978  553 HOH   HOH B . 
T 9 HOH   79  979  407 HOH   HOH B . 
T 9 HOH   80  980  21  HOH   HOH B . 
T 9 HOH   81  981  578 HOH   HOH B . 
T 9 HOH   82  982  60  HOH   HOH B . 
T 9 HOH   83  983  307 HOH   HOH B . 
T 9 HOH   84  984  166 HOH   HOH B . 
T 9 HOH   85  985  324 HOH   HOH B . 
T 9 HOH   86  986  278 HOH   HOH B . 
T 9 HOH   87  987  172 HOH   HOH B . 
T 9 HOH   88  988  68  HOH   HOH B . 
T 9 HOH   89  989  318 HOH   HOH B . 
T 9 HOH   90  990  771 HOH   HOH B . 
T 9 HOH   91  991  107 HOH   HOH B . 
T 9 HOH   92  992  374 HOH   HOH B . 
T 9 HOH   93  993  327 HOH   HOH B . 
T 9 HOH   94  994  399 HOH   HOH B . 
T 9 HOH   95  995  62  HOH   HOH B . 
T 9 HOH   96  996  97  HOH   HOH B . 
T 9 HOH   97  997  571 HOH   HOH B . 
T 9 HOH   98  998  367 HOH   HOH B . 
T 9 HOH   99  999  133 HOH   HOH B . 
T 9 HOH   100 1000 368 HOH   HOH B . 
T 9 HOH   101 1001 365 HOH   HOH B . 
T 9 HOH   102 1002 366 HOH   HOH B . 
T 9 HOH   103 1003 350 HOH   HOH B . 
T 9 HOH   104 1004 170 HOH   HOH B . 
T 9 HOH   105 1005 392 HOH   HOH B . 
T 9 HOH   106 1006 124 HOH   HOH B . 
T 9 HOH   107 1007 134 HOH   HOH B . 
T 9 HOH   108 1008 584 HOH   HOH B . 
T 9 HOH   109 1009 287 HOH   HOH B . 
T 9 HOH   110 1010 322 HOH   HOH B . 
T 9 HOH   111 1011 334 HOH   HOH B . 
T 9 HOH   112 1012 408 HOH   HOH B . 
T 9 HOH   113 1013 289 HOH   HOH B . 
T 9 HOH   114 1014 115 HOH   HOH B . 
T 9 HOH   115 1015 43  HOH   HOH B . 
T 9 HOH   116 1016 569 HOH   HOH B . 
T 9 HOH   117 1017 360 HOH   HOH B . 
T 9 HOH   118 1018 565 HOH   HOH B . 
T 9 HOH   119 1019 355 HOH   HOH B . 
T 9 HOH   120 1020 381 HOH   HOH B . 
T 9 HOH   121 1021 402 HOH   HOH B . 
T 9 HOH   122 1022 396 HOH   HOH B . 
T 9 HOH   123 1023 19  HOH   HOH B . 
T 9 HOH   124 1024 17  HOH   HOH B . 
T 9 HOH   125 1025 154 HOH   HOH B . 
T 9 HOH   126 1026 12  HOH   HOH B . 
T 9 HOH   127 1027 87  HOH   HOH B . 
T 9 HOH   128 1028 352 HOH   HOH B . 
T 9 HOH   129 1029 95  HOH   HOH B . 
T 9 HOH   130 1030 382 HOH   HOH B . 
T 9 HOH   131 1031 378 HOH   HOH B . 
T 9 HOH   132 1032 35  HOH   HOH B . 
T 9 HOH   133 1033 291 HOH   HOH B . 
T 9 HOH   134 1034 80  HOH   HOH B . 
T 9 HOH   135 1035 54  HOH   HOH B . 
T 9 HOH   136 1036 189 HOH   HOH B . 
T 9 HOH   137 1037 63  HOH   HOH B . 
T 9 HOH   138 1038 150 HOH   HOH B . 
T 9 HOH   139 1039 293 HOH   HOH B . 
T 9 HOH   140 1040 409 HOH   HOH B . 
T 9 HOH   141 1041 363 HOH   HOH B . 
T 9 HOH   142 1042 590 HOH   HOH B . 
T 9 HOH   143 1043 84  HOH   HOH B . 
T 9 HOH   144 1044 177 HOH   HOH B . 
T 9 HOH   145 1045 349 HOH   HOH B . 
T 9 HOH   146 1046 74  HOH   HOH B . 
T 9 HOH   147 1047 292 HOH   HOH B . 
T 9 HOH   148 1048 110 HOH   HOH B . 
T 9 HOH   149 1049 383 HOH   HOH B . 
T 9 HOH   150 1050 51  HOH   HOH B . 
T 9 HOH   151 1051 317 HOH   HOH B . 
T 9 HOH   152 1052 536 HOH   HOH B . 
T 9 HOH   153 1053 424 HOH   HOH B . 
T 9 HOH   154 1054 314 HOH   HOH B . 
T 9 HOH   155 1055 468 HOH   HOH B . 
T 9 HOH   156 1056 400 HOH   HOH B . 
T 9 HOH   157 1057 126 HOH   HOH B . 
T 9 HOH   158 1058 6   HOH   HOH B . 
T 9 HOH   159 1059 329 HOH   HOH B . 
T 9 HOH   160 1060 611 HOH   HOH B . 
T 9 HOH   161 1061 180 HOH   HOH B . 
T 9 HOH   162 1062 310 HOH   HOH B . 
T 9 HOH   163 1063 341 HOH   HOH B . 
T 9 HOH   164 1064 99  HOH   HOH B . 
T 9 HOH   165 1065 98  HOH   HOH B . 
T 9 HOH   166 1066 312 HOH   HOH B . 
T 9 HOH   167 1067 325 HOH   HOH B . 
T 9 HOH   168 1068 331 HOH   HOH B . 
T 9 HOH   169 1069 526 HOH   HOH B . 
T 9 HOH   170 1070 550 HOH   HOH B . 
T 9 HOH   171 1071 609 HOH   HOH B . 
T 9 HOH   172 1072 50  HOH   HOH B . 
T 9 HOH   173 1073 230 HOH   HOH B . 
T 9 HOH   174 1074 75  HOH   HOH B . 
T 9 HOH   175 1075 345 HOH   HOH B . 
T 9 HOH   176 1076 14  HOH   HOH B . 
T 9 HOH   177 1077 158 HOH   HOH B . 
T 9 HOH   178 1078 295 HOH   HOH B . 
T 9 HOH   179 1079 281 HOH   HOH B . 
T 9 HOH   180 1080 48  HOH   HOH B . 
T 9 HOH   181 1081 29  HOH   HOH B . 
T 9 HOH   182 1082 305 HOH   HOH B . 
T 9 HOH   183 1083 568 HOH   HOH B . 
T 9 HOH   184 1084 613 HOH   HOH B . 
T 9 HOH   185 1085 309 HOH   HOH B . 
T 9 HOH   186 1086 100 HOH   HOH B . 
T 9 HOH   187 1087 772 HOH   HOH B . 
T 9 HOH   188 1088 547 HOH   HOH B . 
T 9 HOH   189 1089 336 HOH   HOH B . 
T 9 HOH   190 1090 773 HOH   HOH B . 
T 9 HOH   191 1091 122 HOH   HOH B . 
T 9 HOH   192 1092 5   HOH   HOH B . 
T 9 HOH   193 1093 70  HOH   HOH B . 
T 9 HOH   194 1094 428 HOH   HOH B . 
T 9 HOH   195 1095 79  HOH   HOH B . 
T 9 HOH   196 1096 319 HOH   HOH B . 
T 9 HOH   197 1097 4   HOH   HOH B . 
T 9 HOH   198 1098 389 HOH   HOH B . 
T 9 HOH   199 1099 89  HOH   HOH B . 
T 9 HOH   200 1100 175 HOH   HOH B . 
T 9 HOH   201 1101 282 HOH   HOH B . 
T 9 HOH   202 1102 46  HOH   HOH B . 
T 9 HOH   203 1103 615 HOH   HOH B . 
T 9 HOH   204 1104 372 HOH   HOH B . 
T 9 HOH   205 1105 121 HOH   HOH B . 
T 9 HOH   206 1106 347 HOH   HOH B . 
T 9 HOH   207 1107 380 HOH   HOH B . 
T 9 HOH   208 1108 283 HOH   HOH B . 
T 9 HOH   209 1109 59  HOH   HOH B . 
T 9 HOH   210 1110 406 HOH   HOH B . 
T 9 HOH   211 1111 3   HOH   HOH B . 
T 9 HOH   212 1112 286 HOH   HOH B . 
T 9 HOH   213 1113 294 HOH   HOH B . 
T 9 HOH   214 1114 549 HOH   HOH B . 
T 9 HOH   215 1115 169 HOH   HOH B . 
T 9 HOH   216 1116 77  HOH   HOH B . 
T 9 HOH   217 1117 280 HOH   HOH B . 
T 9 HOH   218 1118 300 HOH   HOH B . 
T 9 HOH   219 1119 481 HOH   HOH B . 
T 9 HOH   220 1120 306 HOH   HOH B . 
T 9 HOH   221 1121 20  HOH   HOH B . 
T 9 HOH   222 1122 105 HOH   HOH B . 
T 9 HOH   223 1123 376 HOH   HOH B . 
T 9 HOH   224 1124 18  HOH   HOH B . 
T 9 HOH   225 1125 405 HOH   HOH B . 
T 9 HOH   226 1126 379 HOH   HOH B . 
T 9 HOH   227 1127 348 HOH   HOH B . 
T 9 HOH   228 1128 435 HOH   HOH B . 
T 9 HOH   229 1129 394 HOH   HOH B . 
T 9 HOH   230 1130 418 HOH   HOH B . 
T 9 HOH   231 1131 377 HOH   HOH B . 
T 9 HOH   232 1132 129 HOH   HOH B . 
T 9 HOH   233 1133 168 HOH   HOH B . 
T 9 HOH   234 1134 548 HOH   HOH B . 
T 9 HOH   235 1135 414 HOH   HOH B . 
T 9 HOH   236 1136 13  HOH   HOH B . 
T 9 HOH   237 1137 279 HOH   HOH B . 
T 9 HOH   238 1138 55  HOH   HOH B . 
T 9 HOH   239 1139 401 HOH   HOH B . 
T 9 HOH   240 1140 56  HOH   HOH B . 
T 9 HOH   241 1141 539 HOH   HOH B . 
T 9 HOH   242 1142 583 HOH   HOH B . 
T 9 HOH   243 1143 346 HOH   HOH B . 
T 9 HOH   244 1144 301 HOH   HOH B . 
T 9 HOH   245 1145 313 HOH   HOH B . 
T 9 HOH   246 1146 339 HOH   HOH B . 
T 9 HOH   247 1147 612 HOH   HOH B . 
T 9 HOH   248 1148 66  HOH   HOH B . 
T 9 HOH   249 1149 40  HOH   HOH B . 
T 9 HOH   250 1150 546 HOH   HOH B . 
T 9 HOH   251 1151 290 HOH   HOH B . 
T 9 HOH   252 1152 364 HOH   HOH B . 
T 9 HOH   253 1153 186 HOH   HOH B . 
T 9 HOH   254 1154 340 HOH   HOH B . 
T 9 HOH   255 1155 398 HOH   HOH B . 
T 9 HOH   256 1156 188 HOH   HOH B . 
T 9 HOH   257 1157 357 HOH   HOH B . 
T 9 HOH   258 1158 45  HOH   HOH B . 
T 9 HOH   259 1159 369 HOH   HOH B . 
T 9 HOH   260 1160 523 HOH   HOH B . 
T 9 HOH   261 1161 101 HOH   HOH B . 
T 9 HOH   262 1162 614 HOH   HOH B . 
T 9 HOH   263 1163 427 HOH   HOH B . 
T 9 HOH   264 1164 543 HOH   HOH B . 
T 9 HOH   265 1165 161 HOH   HOH B . 
T 9 HOH   266 1166 137 HOH   HOH B . 
T 9 HOH   267 1167 388 HOH   HOH B . 
T 9 HOH   268 1168 532 HOH   HOH B . 
T 9 HOH   269 1169 524 HOH   HOH B . 
T 9 HOH   270 1170 57  HOH   HOH B . 
T 9 HOH   271 1171 433 HOH   HOH B . 
T 9 HOH   272 1172 375 HOH   HOH B . 
T 9 HOH   273 1173 421 HOH   HOH B . 
T 9 HOH   274 1174 299 HOH   HOH B . 
T 9 HOH   275 1175 298 HOH   HOH B . 
T 9 HOH   276 1176 320 HOH   HOH B . 
T 9 HOH   277 1177 167 HOH   HOH B . 
T 9 HOH   278 1178 127 HOH   HOH B . 
T 9 HOH   279 1179 296 HOH   HOH B . 
T 9 HOH   280 1180 425 HOH   HOH B . 
T 9 HOH   281 1181 439 HOH   HOH B . 
T 9 HOH   282 1182 415 HOH   HOH B . 
T 9 HOH   283 1183 373 HOH   HOH B . 
T 9 HOH   284 1184 326 HOH   HOH B . 
T 9 HOH   285 1185 208 HOH   HOH B . 
T 9 HOH   286 1186 391 HOH   HOH B . 
T 9 HOH   287 1187 561 HOH   HOH B . 
T 9 HOH   288 1188 342 HOH   HOH B . 
T 9 HOH   289 1189 586 HOH   HOH B . 
T 9 HOH   290 1190 589 HOH   HOH B . 
T 9 HOH   291 1191 533 HOH   HOH B . 
T 9 HOH   292 1192 430 HOH   HOH B . 
T 9 HOH   293 1193 595 HOH   HOH B . 
T 9 HOH   294 1194 410 HOH   HOH B . 
T 9 HOH   295 1195 113 HOH   HOH B . 
T 9 HOH   296 1196 528 HOH   HOH B . 
U 9 HOH   1   501  16  HOH   HOH C . 
U 9 HOH   2   502  412 HOH   HOH C . 
U 9 HOH   3   503  106 HOH   HOH C . 
U 9 HOH   4   504  200 HOH   HOH C . 
U 9 HOH   5   505  118 HOH   HOH C . 
U 9 HOH   6   506  496 HOH   HOH C . 
U 9 HOH   7   507  38  HOH   HOH C . 
U 9 HOH   8   508  22  HOH   HOH C . 
U 9 HOH   9   509  231 HOH   HOH C . 
U 9 HOH   10  510  145 HOH   HOH C . 
U 9 HOH   11  511  86  HOH   HOH C . 
U 9 HOH   12  512  139 HOH   HOH C . 
U 9 HOH   13  513  556 HOH   HOH C . 
U 9 HOH   14  514  606 HOH   HOH C . 
U 9 HOH   15  515  151 HOH   HOH C . 
U 9 HOH   16  516  566 HOH   HOH C . 
U 9 HOH   17  517  213 HOH   HOH C . 
U 9 HOH   18  518  577 HOH   HOH C . 
U 9 HOH   19  519  552 HOH   HOH C . 
U 9 HOH   20  520  541 HOH   HOH C . 
U 9 HOH   21  521  562 HOH   HOH C . 
U 9 HOH   22  522  42  HOH   HOH C . 
U 9 HOH   23  523  52  HOH   HOH C . 
U 9 HOH   24  524  229 HOH   HOH C . 
U 9 HOH   25  525  223 HOH   HOH C . 
U 9 HOH   26  526  493 HOH   HOH C . 
U 9 HOH   27  527  203 HOH   HOH C . 
U 9 HOH   28  528  201 HOH   HOH C . 
U 9 HOH   29  529  25  HOH   HOH C . 
U 9 HOH   30  530  119 HOH   HOH C . 
U 9 HOH   31  531  204 HOH   HOH C . 
U 9 HOH   32  532  120 HOH   HOH C . 
U 9 HOH   33  533  162 HOH   HOH C . 
U 9 HOH   34  534  224 HOH   HOH C . 
U 9 HOH   35  535  190 HOH   HOH C . 
U 9 HOH   36  536  32  HOH   HOH C . 
U 9 HOH   37  537  403 HOH   HOH C . 
U 9 HOH   38  538  218 HOH   HOH C . 
U 9 HOH   39  539  564 HOH   HOH C . 
U 9 HOH   40  540  576 HOH   HOH C . 
U 9 HOH   41  541  211 HOH   HOH C . 
U 9 HOH   42  542  159 HOH   HOH C . 
U 9 HOH   43  543  558 HOH   HOH C . 
U 9 HOH   44  544  185 HOH   HOH C . 
U 9 HOH   45  545  219 HOH   HOH C . 
U 9 HOH   46  546  26  HOH   HOH C . 
U 9 HOH   47  547  194 HOH   HOH C . 
U 9 HOH   48  548  176 HOH   HOH C . 
U 9 HOH   49  549  7   HOH   HOH C . 
U 9 HOH   50  550  225 HOH   HOH C . 
U 9 HOH   51  551  131 HOH   HOH C . 
U 9 HOH   52  552  130 HOH   HOH C . 
U 9 HOH   53  553  557 HOH   HOH C . 
U 9 HOH   54  554  196 HOH   HOH C . 
U 9 HOH   55  555  71  HOH   HOH C . 
U 9 HOH   56  556  2   HOH   HOH C . 
U 9 HOH   57  557  24  HOH   HOH C . 
U 9 HOH   58  558  361 HOH   HOH C . 
U 9 HOH   59  559  183 HOH   HOH C . 
U 9 HOH   60  560  199 HOH   HOH C . 
U 9 HOH   61  561  73  HOH   HOH C . 
U 9 HOH   62  562  246 HOH   HOH C . 
U 9 HOH   63  563  542 HOH   HOH C . 
U 9 HOH   64  564  164 HOH   HOH C . 
U 9 HOH   65  565  191 HOH   HOH C . 
U 9 HOH   66  566  215 HOH   HOH C . 
U 9 HOH   67  567  551 HOH   HOH C . 
U 9 HOH   68  568  226 HOH   HOH C . 
U 9 HOH   69  569  212 HOH   HOH C . 
U 9 HOH   70  570  563 HOH   HOH C . 
U 9 HOH   71  571  192 HOH   HOH C . 
U 9 HOH   72  572  76  HOH   HOH C . 
U 9 HOH   73  573  82  HOH   HOH C . 
U 9 HOH   74  574  214 HOH   HOH C . 
U 9 HOH   75  575  182 HOH   HOH C . 
U 9 HOH   76  576  227 HOH   HOH C . 
U 9 HOH   77  577  179 HOH   HOH C . 
U 9 HOH   78  578  608 HOH   HOH C . 
U 9 HOH   79  579  206 HOH   HOH C . 
U 9 HOH   80  580  431 HOH   HOH C . 
U 9 HOH   81  581  221 HOH   HOH C . 
U 9 HOH   82  582  123 HOH   HOH C . 
U 9 HOH   83  583  222 HOH   HOH C . 
U 9 HOH   84  584  416 HOH   HOH C . 
U 9 HOH   85  585  544 HOH   HOH C . 
U 9 HOH   86  586  567 HOH   HOH C . 
U 9 HOH   87  587  228 HOH   HOH C . 
U 9 HOH   88  588  217 HOH   HOH C . 
U 9 HOH   89  589  140 HOH   HOH C . 
U 9 HOH   90  590  193 HOH   HOH C . 
U 9 HOH   91  591  148 HOH   HOH C . 
U 9 HOH   92  592  594 HOH   HOH C . 
U 9 HOH   93  593  195 HOH   HOH C . 
U 9 HOH   94  594  153 HOH   HOH C . 
U 9 HOH   95  595  171 HOH   HOH C . 
U 9 HOH   96  596  593 HOH   HOH C . 
U 9 HOH   97  597  157 HOH   HOH C . 
U 9 HOH   98  598  216 HOH   HOH C . 
U 9 HOH   99  599  535 HOH   HOH C . 
U 9 HOH   100 600  555 HOH   HOH C . 
U 9 HOH   101 601  197 HOH   HOH C . 
U 9 HOH   102 602  554 HOH   HOH C . 
U 9 HOH   103 603  304 HOH   HOH C . 
U 9 HOH   104 604  397 HOH   HOH C . 
U 9 HOH   105 605  545 HOH   HOH C . 
U 9 HOH   106 606  220 HOH   HOH C . 
U 9 HOH   107 607  588 HOH   HOH C . 
U 9 HOH   108 608  453 HOH   HOH C . 
V 9 HOH   1   501  531 HOH   HOH D . 
V 9 HOH   2   502  242 HOH   HOH D . 
V 9 HOH   3   503  156 HOH   HOH D . 
V 9 HOH   4   504  241 HOH   HOH D . 
V 9 HOH   5   505  497 HOH   HOH D . 
V 9 HOH   6   506  205 HOH   HOH D . 
V 9 HOH   7   507  256 HOH   HOH D . 
V 9 HOH   8   508  263 HOH   HOH D . 
V 9 HOH   9   509  596 HOH   HOH D . 
V 9 HOH   10  510  149 HOH   HOH D . 
V 9 HOH   11  511  181 HOH   HOH D . 
V 9 HOH   12  512  237 HOH   HOH D . 
V 9 HOH   13  513  253 HOH   HOH D . 
V 9 HOH   14  514  260 HOH   HOH D . 
V 9 HOH   15  515  259 HOH   HOH D . 
V 9 HOH   16  516  270 HOH   HOH D . 
V 9 HOH   17  517  264 HOH   HOH D . 
V 9 HOH   18  518  248 HOH   HOH D . 
V 9 HOH   19  519  252 HOH   HOH D . 
V 9 HOH   20  520  275 HOH   HOH D . 
V 9 HOH   21  521  240 HOH   HOH D . 
V 9 HOH   22  522  27  HOH   HOH D . 
V 9 HOH   23  523  34  HOH   HOH D . 
V 9 HOH   24  524  258 HOH   HOH D . 
V 9 HOH   25  525  10  HOH   HOH D . 
V 9 HOH   26  526  245 HOH   HOH D . 
V 9 HOH   27  527  207 HOH   HOH D . 
V 9 HOH   28  528  235 HOH   HOH D . 
V 9 HOH   29  529  386 HOH   HOH D . 
V 9 HOH   30  530  85  HOH   HOH D . 
V 9 HOH   31  531  65  HOH   HOH D . 
V 9 HOH   32  532  254 HOH   HOH D . 
V 9 HOH   33  533  243 HOH   HOH D . 
V 9 HOH   34  534  236 HOH   HOH D . 
V 9 HOH   35  535  39  HOH   HOH D . 
V 9 HOH   36  536  132 HOH   HOH D . 
V 9 HOH   37  537  135 HOH   HOH D . 
V 9 HOH   38  538  257 HOH   HOH D . 
V 9 HOH   39  539  147 HOH   HOH D . 
V 9 HOH   40  540  202 HOH   HOH D . 
V 9 HOH   41  541  249 HOH   HOH D . 
V 9 HOH   42  542  266 HOH   HOH D . 
V 9 HOH   43  543  238 HOH   HOH D . 
V 9 HOH   44  544  267 HOH   HOH D . 
V 9 HOH   45  545  261 HOH   HOH D . 
V 9 HOH   46  546  53  HOH   HOH D . 
V 9 HOH   47  547  233 HOH   HOH D . 
V 9 HOH   48  548  244 HOH   HOH D . 
V 9 HOH   49  549  247 HOH   HOH D . 
V 9 HOH   50  550  507 HOH   HOH D . 
V 9 HOH   51  551  268 HOH   HOH D . 
V 9 HOH   52  552  262 HOH   HOH D . 
V 9 HOH   53  553  116 HOH   HOH D . 
V 9 HOH   54  554  255 HOH   HOH D . 
V 9 HOH   55  555  250 HOH   HOH D . 
V 9 HOH   56  556  141 HOH   HOH D . 
V 9 HOH   57  557  234 HOH   HOH D . 
V 9 HOH   58  558  88  HOH   HOH D . 
V 9 HOH   59  559  178 HOH   HOH D . 
V 9 HOH   60  560  239 HOH   HOH D . 
V 9 HOH   61  561  232 HOH   HOH D . 
V 9 HOH   62  562  269 HOH   HOH D . 
V 9 HOH   63  563  210 HOH   HOH D . 
V 9 HOH   64  564  521 HOH   HOH D . 
V 9 HOH   65  565  273 HOH   HOH D . 
V 9 HOH   66  566  271 HOH   HOH D . 
V 9 HOH   67  567  265 HOH   HOH D . 
V 9 HOH   68  568  284 HOH   HOH D . 
V 9 HOH   69  569  274 HOH   HOH D . 
V 9 HOH   70  570  272 HOH   HOH D . 
# 
_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                     9DB2 
_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                         9DB2 
_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                   9DB2 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9DB2 
_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' ? 0.004 ? 18433 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.714 ? 25040 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 5.816 ? 2537  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.051 ? 2739  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.006 ? 3215  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9DB2 
_struct.title                        'Class Ia ribonucleotide reductase with mechanism-based inhibitor N3CDP' 
_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        9DB2 
_struct_keywords.text            'ribonucleotide reductase, class Ia, mechanistic inhibition, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
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 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 5 ? 
I N N 4 ? 
J N N 6 ? 
K N N 5 ? 
L N N 5 ? 
M N N 3 ? 
N N N 4 ? 
O N N 4 ? 
P N N 7 ? 
Q N N 8 ? 
R N N 8 ? 
S N N 9 ? 
T N N 9 ? 
U N N 9 ? 
V N N 9 ? 
# 
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 RIR1_ECOLI P00452 ? 1 
;MNQNLLVTKRDGSTERINLDKIHRVLDWAAEGLHNVSISQVELRSHIQFYDGIKTSDIHETIIKAAADLISRDAPDYQYL
AARLAIFHLRKKAYGQFEPPALYDHVVKMVEMGKYDNHLLEDYTEEEFKQMDTFIDHDRDMTFSYAAVKQLEGKYLVQNR
VTGEIYESAQFLYILVAACLFSNYPRETRLQYVKRFYDAVSTFKISLPTPIMSGVRTPTRQFSSCVLIECGDSLDSINAT
SSAIVKYVSQRAGIGINAGRIRALGSPIRGGEAFHTGCIPFYKHFQTAVKSCSQGGVRGGAATLFYPMWHLEVESLLVLK
NNRGVEGNRVRHMDYGVQINKLMYTRLLKGEDITLFSPSDVPGLYDAFFADQEEFERLYTKYEKDDSIRKQRVKAVELFS
LMMQERASTGRIYIQNVDHCNTHSPFDPAIAPVRQSNLCLEIALPTKPLNDVNDENGEIALCTLSAFNLGAINNLDELEE
LAILAVRALDALLDYQDYPIPAAKRGAMGRRTLGIGVINFAYYLAKHGKRYSDGSANNLTHKTFEAIQYYLLKASNELAK
EQGACPWFNETTYAKGILPIDTYKKDLDTIANEPLHYDWEALRESIKTHGLRNSTLSALMPSETSSQISNATNGIEPPRG
YVSIKASKDGILRQVVPDYEHLHDAYELLWEMPGNDGYLQLVGIMQKFIDQSISANTNYDPSRFPSGKVPMQQLLKDLLT
AYKFGVKTLYYQNTRDGAEDAQDDLVPSIQDDGCESGACKI
;
1 
2 UNP RIR2_ECOLI P69924 ? 2 
;MAYTTFSQTKNDQLKEPMFFGQPVNVARYDQQKYDIFEKLIEKQLSFFWRPEEVDVSRDRIDYQALPEHEKHIFISNLKY
QTLLDSIQGRSPNVALLPLISIPELETWVETWAFSETIHSRSYTHIIRNIVNDPSVVFDDIVTNEQIQKRAEGISSYYDE
LIEMTSYWHLLGEGTHTVNGKTVTVSLRELKKKLYLCLMSVNALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEA
LHLTGTQHMLNLLRSGADDPEMAEIAEECKQECYDLFVQAAQQEKDWADYLFRDGSMIGLNKDILCQYVEYITNIRMQAV
GLDLPFQTRSNPIPWINTWLVSDNVQVAPQEVEVSSYLVGQIDSEVDTDDLSNFQL
;
1 
# 
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 9DB2 A 1 ? 761 ? P00452 1 ? 761 ? 1 761 
2 1 9DB2 B 1 ? 761 ? P00452 1 ? 761 ? 1 761 
3 2 9DB2 C 1 ? 376 ? P69924 1 ? 376 ? 0 375 
4 2 9DB2 D 1 ? 376 ? P69924 1 ? 376 ? 0 375 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_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 
# 
_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 ASN A 18  ? ALA A 30  ? ASN A 18  ALA A 30  1 ? 13 
HELX_P HELX_P2   AA2 SER A 37  ? ILE A 47  ? SER A 37  ILE A 47  1 ? 11 
HELX_P HELX_P3   AA3 LYS A 54  ? LEU A 69  ? LYS A 54  LEU A 69  1 ? 16 
HELX_P HELX_P4   AA4 ALA A 74  ? ASP A 76  ? ALA A 74  ASP A 76  5 ? 3  
HELX_P HELX_P5   AA5 TYR A 77  ? GLY A 95  ? TYR A 77  GLY A 95  1 ? 19 
HELX_P HELX_P6   AA6 ALA A 101 ? MET A 112 ? ALA A 101 MET A 112 1 ? 12 
HELX_P HELX_P7   AA7 ASN A 117 ? TYR A 123 ? ASN A 117 TYR A 123 1 ? 7  
HELX_P HELX_P8   AA8 THR A 124 ? ILE A 135 ? THR A 124 ILE A 135 1 ? 12 
HELX_P HELX_P9   AA9 ASP A 136 ? PHE A 143 ? ASP A 136 PHE A 143 5 ? 8  
HELX_P HELX_P10  AB1 SER A 144 ? TYR A 155 ? SER A 144 TYR A 155 1 ? 12 
HELX_P HELX_P11  AB2 SER A 168 ? PHE A 181 ? SER A 168 PHE A 181 1 ? 14 
HELX_P HELX_P12  AB3 THR A 188 ? THR A 202 ? THR A 188 THR A 202 1 ? 15 
HELX_P HELX_P13  AB4 PRO A 208 ? VAL A 215 ? PRO A 208 VAL A 215 1 ? 8  
HELX_P HELX_P14  AB5 SER A 233 ? SER A 249 ? SER A 233 SER A 249 1 ? 17 
HELX_P HELX_P15  AB6 GLY A 277 ? LYS A 290 ? GLY A 277 LYS A 290 1 ? 14 
HELX_P HELX_P16  AB7 GLU A 312 ? VAL A 318 ? GLU A 312 VAL A 318 1 ? 7  
HELX_P HELX_P17  AB8 VAL A 325 ? ARG A 329 ? VAL A 325 ARG A 329 5 ? 5  
HELX_P HELX_P18  AB9 ASN A 340 ? GLY A 350 ? ASN A 340 GLY A 350 1 ? 11 
HELX_P HELX_P19  AC1 GLY A 363 ? ALA A 370 ? GLY A 363 ALA A 370 1 ? 8  
HELX_P HELX_P20  AC2 ASP A 371 ? LYS A 384 ? ASP A 371 LYS A 384 1 ? 14 
HELX_P HELX_P21  AC3 ALA A 395 ? GLY A 410 ? ALA A 395 GLY A 410 1 ? 16 
HELX_P HELX_P22  AC4 VAL A 417 ? HIS A 423 ? VAL A 417 HIS A 423 1 ? 7  
HELX_P HELX_P23  AC5 GLU A 477 ? GLN A 496 ? GLU A 477 GLN A 496 1 ? 20 
HELX_P HELX_P24  AC6 ILE A 500 ? ARG A 511 ? ILE A 500 ARG A 511 1 ? 12 
HELX_P HELX_P25  AC7 ASN A 519 ? HIS A 527 ? ASN A 519 HIS A 527 1 ? 9  
HELX_P HELX_P26  AC8 ALA A 536 ? GLY A 563 ? ALA A 536 GLY A 563 1 ? 28 
HELX_P HELX_P27  AC9 TRP A 567 ? GLY A 576 ? TRP A 567 GLY A 576 5 ? 10 
HELX_P HELX_P28  AD1 LYS A 584 ? ILE A 590 ? LYS A 584 ILE A 590 5 ? 7  
HELX_P HELX_P29  AD2 ASP A 598 ? GLY A 610 ? ASP A 598 GLY A 610 1 ? 13 
HELX_P HELX_P30  AD3 SER A 622 ? SER A 629 ? SER A 622 SER A 629 1 ? 8  
HELX_P HELX_P31  AD4 ASP A 658 ? HIS A 663 ? ASP A 658 HIS A 663 1 ? 6  
HELX_P HELX_P32  AD5 LEU A 668 ? MET A 672 ? LEU A 668 MET A 672 5 ? 5  
HELX_P HELX_P33  AD6 ASP A 676 ? ILE A 689 ? ASP A 676 ILE A 689 1 ? 14 
HELX_P HELX_P34  AD7 ASP A 700 ? LYS A 708 ? ASP A 700 LYS A 708 5 ? 9  
HELX_P HELX_P35  AD8 MET A 711 ? PHE A 724 ? MET A 711 PHE A 724 1 ? 14 
HELX_P HELX_P36  AD9 ASN B 18  ? ALA B 30  ? ASN B 18  ALA B 30  1 ? 13 
HELX_P HELX_P37  AE1 SER B 37  ? ILE B 47  ? SER B 37  ILE B 47  1 ? 11 
HELX_P HELX_P38  AE2 THR B 55  ? ASP B 68  ? THR B 55  ASP B 68  1 ? 14 
HELX_P HELX_P39  AE3 ASP B 76  ? GLY B 95  ? ASP B 76  GLY B 95  1 ? 20 
HELX_P HELX_P40  AE4 ALA B 101 ? MET B 112 ? ALA B 101 MET B 112 1 ? 12 
HELX_P HELX_P41  AE5 ASN B 117 ? TYR B 123 ? ASN B 117 TYR B 123 1 ? 7  
HELX_P HELX_P42  AE6 THR B 124 ? ILE B 135 ? THR B 124 ILE B 135 1 ? 12 
HELX_P HELX_P43  AE7 ASP B 136 ? PHE B 143 ? ASP B 136 PHE B 143 5 ? 8  
HELX_P HELX_P44  AE8 SER B 144 ? LYS B 154 ? SER B 144 LYS B 154 1 ? 11 
HELX_P HELX_P45  AE9 SER B 168 ? PHE B 181 ? SER B 168 PHE B 181 1 ? 14 
HELX_P HELX_P46  AF1 THR B 188 ? THR B 202 ? THR B 188 THR B 202 1 ? 15 
HELX_P HELX_P47  AF2 PRO B 208 ? VAL B 215 ? PRO B 208 VAL B 215 1 ? 8  
HELX_P HELX_P48  AF3 SER B 233 ? SER B 249 ? SER B 233 SER B 249 1 ? 17 
HELX_P HELX_P49  AF4 CYS B 278 ? CYS B 292 ? CYS B 278 CYS B 292 1 ? 15 
HELX_P HELX_P50  AF5 GLU B 312 ? VAL B 318 ? GLU B 312 VAL B 318 1 ? 7  
HELX_P HELX_P51  AF6 ASN B 340 ? LYS B 349 ? ASN B 340 LYS B 349 1 ? 10 
HELX_P HELX_P52  AF7 PRO B 358 ? VAL B 361 ? PRO B 358 VAL B 361 5 ? 4  
HELX_P HELX_P53  AF8 GLY B 363 ? ALA B 370 ? GLY B 363 ALA B 370 1 ? 8  
HELX_P HELX_P54  AF9 ASP B 371 ? LYS B 384 ? ASP B 371 LYS B 384 1 ? 14 
HELX_P HELX_P55  AG1 ALA B 395 ? GLY B 410 ? ALA B 395 GLY B 410 1 ? 16 
HELX_P HELX_P56  AG2 VAL B 417 ? HIS B 423 ? VAL B 417 HIS B 423 1 ? 7  
HELX_P HELX_P57  AG3 ASN B 474 ? ASP B 476 ? ASN B 474 ASP B 476 5 ? 3  
HELX_P HELX_P58  AG4 GLU B 477 ? GLN B 496 ? GLU B 477 GLN B 496 1 ? 20 
HELX_P HELX_P59  AG5 ILE B 500 ? ARG B 511 ? ILE B 500 ARG B 511 1 ? 12 
HELX_P HELX_P60  AG6 ASN B 519 ? HIS B 527 ? ASN B 519 HIS B 527 1 ? 9  
HELX_P HELX_P61  AG7 ALA B 536 ? GLY B 563 ? ALA B 536 GLY B 563 1 ? 28 
HELX_P HELX_P62  AG8 TRP B 567 ? GLY B 576 ? TRP B 567 GLY B 576 5 ? 10 
HELX_P HELX_P63  AG9 LYS B 584 ? ILE B 590 ? LYS B 584 ILE B 590 5 ? 7  
HELX_P HELX_P64  AH1 ASP B 598 ? HIS B 609 ? ASP B 598 HIS B 609 1 ? 12 
HELX_P HELX_P65  AH2 THR B 624 ? SER B 629 ? THR B 624 SER B 629 1 ? 6  
HELX_P HELX_P66  AH3 ASP B 658 ? HIS B 663 ? ASP B 658 HIS B 663 1 ? 6  
HELX_P HELX_P67  AH4 LEU B 668 ? MET B 672 ? LEU B 668 MET B 672 5 ? 5  
HELX_P HELX_P68  AH5 ASN B 675 ? ILE B 689 ? ASN B 675 ILE B 689 1 ? 15 
HELX_P HELX_P69  AH6 ASP B 700 ? PHE B 704 ? ASP B 700 PHE B 704 5 ? 5  
HELX_P HELX_P70  AH7 PRO B 710 ? PHE B 724 ? PRO B 710 PHE B 724 1 ? 15 
HELX_P HELX_P71  AH8 TYR C 34  ? PHE C 47  ? TYR C 33  PHE C 46  1 ? 14 
HELX_P HELX_P72  AH9 ARG C 50  ? VAL C 54  ? ARG C 49  VAL C 53  5 ? 5  
HELX_P HELX_P73  AI1 VAL C 56  ? ALA C 65  ? VAL C 55  ALA C 64  1 ? 10 
HELX_P HELX_P74  AI2 PRO C 67  ? LEU C 96  ? PRO C 66  LEU C 95  1 ? 30 
HELX_P HELX_P75  AI3 ILE C 102 ? VAL C 131 ? ILE C 101 VAL C 130 1 ? 30 
HELX_P HELX_P76  AI4 PRO C 134 ? ASP C 139 ? PRO C 133 ASP C 138 1 ? 6  
HELX_P HELX_P77  AI5 ASN C 144 ? ARG C 150 ? ASN C 143 ARG C 149 1 ? 7  
HELX_P HELX_P78  AI6 ALA C 151 ? GLY C 172 ? ALA C 150 GLY C 171 1 ? 22 
HELX_P HELX_P79  AI7 SER C 186 ? ARG C 222 ? SER C 185 ARG C 221 1 ? 37 
HELX_P HELX_P80  AI8 MET C 225 ? SER C 255 ? MET C 224 SER C 254 1 ? 31 
HELX_P HELX_P81  AI9 ASP C 259 ? GLU C 268 ? ASP C 258 GLU C 267 1 ? 10 
HELX_P HELX_P82  AJ1 GLN C 271 ? PHE C 292 ? GLN C 270 PHE C 291 1 ? 22 
HELX_P HELX_P83  AJ2 ASN C 301 ? ALA C 319 ? ASN C 300 ALA C 318 1 ? 19 
HELX_P HELX_P84  AJ3 ILE C 333 ? TRP C 335 ? ILE C 332 TRP C 334 5 ? 3  
HELX_P HELX_P85  AJ4 ILE C 336 ? VAL C 341 ? ILE C 335 VAL C 340 1 ? 6  
HELX_P HELX_P86  AJ5 ASP C 367 ? ASN C 373 ? ASP C 366 ASN C 372 1 ? 7  
HELX_P HELX_P87  AJ6 TYR D 34  ? PHE D 47  ? TYR D 33  PHE D 46  1 ? 14 
HELX_P HELX_P88  AJ7 ARG D 50  ? VAL D 54  ? ARG D 49  VAL D 53  5 ? 5  
HELX_P HELX_P89  AJ8 VAL D 56  ? ALA D 65  ? VAL D 55  ALA D 64  1 ? 10 
HELX_P HELX_P90  AJ9 PRO D 67  ? LEU D 96  ? PRO D 66  LEU D 95  1 ? 30 
HELX_P HELX_P91  AK1 LEU D 97  ? ILE D 100 ? LEU D 96  ILE D 99  5 ? 4  
HELX_P HELX_P92  AK2 ILE D 102 ? VAL D 131 ? ILE D 101 VAL D 130 1 ? 30 
HELX_P HELX_P93  AK3 PRO D 134 ? ASN D 144 ? PRO D 133 ASN D 143 1 ? 11 
HELX_P HELX_P94  AK4 ASN D 144 ? GLY D 172 ? ASN D 143 GLY D 171 1 ? 29 
HELX_P HELX_P95  AK5 SER D 186 ? ILE D 207 ? SER D 185 ILE D 206 1 ? 22 
HELX_P HELX_P96  AK6 ILE D 207 ? ARG D 222 ? ILE D 206 ARG D 221 1 ? 16 
HELX_P HELX_P97  AK7 MET D 225 ? GLY D 256 ? MET D 224 GLY D 255 1 ? 32 
HELX_P HELX_P98  AK8 GLU D 261 ? CYS D 269 ? GLU D 260 CYS D 268 1 ? 9  
HELX_P HELX_P99  AK9 GLN D 271 ? PHE D 292 ? GLN D 270 PHE D 291 1 ? 22 
HELX_P HELX_P100 AL1 ASN D 301 ? ALA D 319 ? ASN D 300 ALA D 318 1 ? 19 
HELX_P HELX_P101 AL2 ILE D 333 ? TRP D 339 ? ILE D 332 TRP D 338 5 ? 7  
# 
_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 ?    ? A CYS 225 SG  A ? ? 1_555 A CYS   462 SG  ? ? A CYS 225 A CYS   462  1_555 ? ? ? ? ? ? ? 2.036 ? ? 
disulf2  disulf ?    ? C CYS 269 SG  ? ? ? 1_555 C CYS   273 SG  ? ? C CYS 268 C CYS   272  1_555 ? ? ? ? ? ? ? 2.039 ? ? 
disulf3  disulf ?    ? D CYS 269 SG  ? ? ? 1_555 D CYS   273 SG  ? ? D CYS 268 D CYS   272  1_555 ? ? ? ? ? ? ? 2.038 ? ? 
covale1  covale none ? A CYS 439 SG  ? ? ? 1_555 J UNL   .   N   ? ? A CYS 439 A UNL   806  1_555 ? ? ? ? ? ? ? 1.677 ? ? 
covale2  covale none ? B CYS 225 SG  ? ? ? 1_555 P A1A3L .   N01 ? ? B CYS 225 B A1A3L 806  1_555 ? ? ? ? ? ? ? 1.639 ? ? 
metalc1  metalc ?    ? E DTP .   O2G ? ? ? 1_555 F MG    .   MG  ? ? A DTP 801 A MG    802  1_555 ? ? ? ? ? ? ? 2.121 ? ? 
metalc2  metalc ?    ? E DTP .   O2B ? ? ? 1_555 F MG    .   MG  ? ? A DTP 801 A MG    802  1_555 ? ? ? ? ? ? ? 2.075 ? ? 
metalc3  metalc ?    ? E DTP .   O2A ? ? ? 1_555 F MG    .   MG  ? ? A DTP 801 A MG    802  1_555 ? ? ? ? ? ? ? 2.064 ? ? 
metalc4  metalc ?    ? F MG  .   MG  ? ? ? 1_555 S HOH   .   O   ? ? A MG  802 A HOH   931  1_555 ? ? ? ? ? ? ? 2.099 ? ? 
metalc5  metalc ?    ? F MG  .   MG  ? ? ? 1_555 S HOH   .   O   ? ? A MG  802 A HOH   944  1_555 ? ? ? ? ? ? ? 2.101 ? ? 
metalc6  metalc ?    ? F MG  .   MG  ? ? ? 1_555 S HOH   .   O   ? ? A MG  802 A HOH   984  1_555 ? ? ? ? ? ? ? 2.097 ? ? 
metalc7  metalc ?    ? G ATP .   O1G ? ? ? 1_555 I MG    .   MG  ? ? A ATP 803 A MG    805  1_555 ? ? ? ? ? ? ? 2.077 ? ? 
metalc8  metalc ?    ? G ATP .   O1B ? ? ? 1_555 I MG    .   MG  ? ? A ATP 803 A MG    805  1_555 ? ? ? ? ? ? ? 2.074 ? ? 
metalc9  metalc ?    ? G ATP .   O1A ? ? ? 1_555 I MG    .   MG  ? ? A ATP 803 A MG    805  1_555 ? ? ? ? ? ? ? 2.065 ? ? 
metalc10 metalc ?    ? H ATP .   O2G ? ? ? 1_555 I MG    .   MG  ? ? A ATP 804 A MG    805  1_555 ? ? ? ? ? ? ? 2.079 ? ? 
metalc11 metalc ?    ? H ATP .   O2B ? ? ? 1_555 I MG    .   MG  ? ? A ATP 804 A MG    805  1_555 ? ? ? ? ? ? ? 2.087 ? ? 
metalc12 metalc ?    ? H ATP .   O2A ? ? ? 1_555 I MG    .   MG  ? ? A ATP 804 A MG    805  1_555 ? ? ? ? ? ? ? 2.095 ? ? 
metalc13 metalc ?    ? K ATP .   O3G ? ? ? 1_555 O MG    .   MG  ? ? B ATP 801 B MG    805  1_555 ? ? ? ? ? ? ? 2.937 ? ? 
metalc14 metalc ?    ? K ATP .   O2A ? ? ? 1_555 O MG    .   MG  ? ? B ATP 801 B MG    805  1_555 ? ? ? ? ? ? ? 2.428 ? ? 
metalc15 metalc ?    ? L ATP .   O1B ? ? ? 1_555 O MG    .   MG  ? ? B ATP 802 B MG    805  1_555 ? ? ? ? ? ? ? 2.320 ? ? 
metalc16 metalc ?    ? L ATP .   O1A ? ? ? 1_555 O MG    .   MG  ? ? B ATP 802 B MG    805  1_555 ? ? ? ? ? ? ? 2.056 ? ? 
metalc17 metalc ?    ? M DTP .   O1G ? ? ? 1_555 N MG    .   MG  ? ? B DTP 803 B MG    804  1_555 ? ? ? ? ? ? ? 2.107 ? ? 
metalc18 metalc ?    ? M DTP .   O1B ? ? ? 1_555 N MG    .   MG  ? ? B DTP 803 B MG    804  1_555 ? ? ? ? ? ? ? 2.100 ? ? 
metalc19 metalc ?    ? M DTP .   O1A ? ? ? 1_555 N MG    .   MG  ? ? B DTP 803 B MG    804  1_555 ? ? ? ? ? ? ? 2.091 ? ? 
metalc20 metalc ?    ? N MG  .   MG  ? ? ? 1_555 T HOH   .   O   ? ? B MG  804 B HOH   990  1_555 ? ? ? ? ? ? ? 2.098 ? ? 
metalc21 metalc ?    ? N MG  .   MG  ? ? ? 1_555 T HOH   .   O   ? ? B MG  804 B HOH   1087 1_555 ? ? ? ? ? ? ? 2.100 ? ? 
metalc22 metalc ?    ? N MG  .   MG  ? ? ? 1_555 T HOH   .   O   ? ? B MG  804 B HOH   1090 1_555 ? ? ? ? ? ? ? 2.098 ? ? 
metalc23 metalc ?    ? C ASP 85  OD1 ? ? ? 1_555 Q FEO   .   FE1 ? ? C ASP 84  C FEO   401  1_555 ? ? ? ? ? ? ? 2.749 ? ? 
metalc24 metalc ?    ? C ASP 85  OD2 ? ? ? 1_555 Q FEO   .   FE1 ? ? C ASP 84  C FEO   401  1_555 ? ? ? ? ? ? ? 2.138 ? ? 
metalc25 metalc ?    ? C GLU 116 OE1 ? ? ? 1_555 Q FEO   .   FE1 ? ? C GLU 115 C FEO   401  1_555 ? ? ? ? ? ? ? 2.027 ? ? 
metalc26 metalc ?    ? C GLU 116 OE2 ? ? ? 1_555 Q FEO   .   FE2 ? ? C GLU 115 C FEO   401  1_555 ? ? ? ? ? ? ? 2.039 ? ? 
metalc27 metalc ?    ? C HIS 119 ND1 ? ? ? 1_555 Q FEO   .   FE1 ? ? C HIS 118 C FEO   401  1_555 ? ? ? ? ? ? ? 2.240 ? ? 
metalc28 metalc ?    ? C GLU 239 OE1 ? ? ? 1_555 Q FEO   .   FE2 ? ? C GLU 238 C FEO   401  1_555 ? ? ? ? ? ? ? 2.696 ? ? 
metalc29 metalc ?    ? C GLU 239 OE2 ? ? ? 1_555 Q FEO   .   FE2 ? ? C GLU 238 C FEO   401  1_555 ? ? ? ? ? ? ? 2.661 ? ? 
metalc30 metalc ?    ? C HIS 242 ND1 ? ? ? 1_555 Q FEO   .   FE2 ? ? C HIS 241 C FEO   401  1_555 ? ? ? ? ? ? ? 2.213 ? ? 
metalc31 metalc ?    ? Q FEO .   FE1 ? ? ? 1_555 U HOH   .   O   ? ? C FEO 401 C HOH   511  1_555 ? ? ? ? ? ? ? 1.969 ? ? 
metalc32 metalc ?    ? D ASP 85  OD1 ? ? ? 1_555 R FEO   .   FE1 ? ? D ASP 84  D FEO   401  1_555 ? ? ? ? ? ? ? 2.242 ? ? 
metalc33 metalc ?    ? D ASP 85  OD2 ? ? ? 1_555 R FEO   .   FE1 ? ? D ASP 84  D FEO   401  1_555 ? ? ? ? ? ? ? 2.154 ? ? 
metalc34 metalc ?    ? D GLU 116 OE1 ? ? ? 1_555 R FEO   .   FE1 ? ? D GLU 115 D FEO   401  1_555 ? ? ? ? ? ? ? 2.028 ? ? 
metalc35 metalc ?    ? D GLU 116 OE2 ? ? ? 1_555 R FEO   .   FE2 ? ? D GLU 115 D FEO   401  1_555 ? ? ? ? ? ? ? 2.021 ? ? 
metalc36 metalc ?    ? D HIS 119 ND1 ? ? ? 1_555 R FEO   .   FE1 ? ? D HIS 118 D FEO   401  1_555 ? ? ? ? ? ? ? 2.239 ? ? 
metalc37 metalc ?    ? D GLU 205 OE2 ? ? ? 1_555 R FEO   .   FE2 ? ? D GLU 204 D FEO   401  1_555 ? ? ? ? ? ? ? 2.096 ? ? 
metalc38 metalc ?    ? D GLU 239 OE2 ? ? ? 1_555 R FEO   .   FE2 ? ? D GLU 238 D FEO   401  1_555 ? ? ? ? ? ? ? 2.543 ? ? 
metalc39 metalc ?    ? D HIS 242 ND1 ? ? ? 1_555 R FEO   .   FE2 ? ? D HIS 241 D FEO   401  1_555 ? ? ? ? ? ? ? 2.229 ? ? 
metalc40 metalc ?    ? R FEO .   FE1 ? ? ? 1_555 V HOH   .   O   ? ? D FEO 401 D HOH   504  1_555 ? ? ? ? ? ? ? 2.098 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1   O2G ? E DTP .   ? A DTP 801  ? 1_555 MG  ? F MG  . ? A MG  802 ? 1_555 O2B ? E DTP .   ? A DTP 801  ? 1_555 90.3  ? 
2   O2G ? E DTP .   ? A DTP 801  ? 1_555 MG  ? F MG  . ? A MG  802 ? 1_555 O2A ? E DTP .   ? A DTP 801  ? 1_555 95.4  ? 
3   O2B ? E DTP .   ? A DTP 801  ? 1_555 MG  ? F MG  . ? A MG  802 ? 1_555 O2A ? E DTP .   ? A DTP 801  ? 1_555 106.0 ? 
4   O2G ? E DTP .   ? A DTP 801  ? 1_555 MG  ? F MG  . ? A MG  802 ? 1_555 O   ? S HOH .   ? A HOH 931  ? 1_555 88.6  ? 
5   O2B ? E DTP .   ? A DTP 801  ? 1_555 MG  ? F MG  . ? A MG  802 ? 1_555 O   ? S HOH .   ? A HOH 931  ? 1_555 93.9  ? 
6   O2A ? E DTP .   ? A DTP 801  ? 1_555 MG  ? F MG  . ? A MG  802 ? 1_555 O   ? S HOH .   ? A HOH 931  ? 1_555 159.7 ? 
7   O2G ? E DTP .   ? A DTP 801  ? 1_555 MG  ? F MG  . ? A MG  802 ? 1_555 O   ? S HOH .   ? A HOH 944  ? 1_555 89.6  ? 
8   O2B ? E DTP .   ? A DTP 801  ? 1_555 MG  ? F MG  . ? A MG  802 ? 1_555 O   ? S HOH .   ? A HOH 944  ? 1_555 179.9 ? 
9   O2A ? E DTP .   ? A DTP 801  ? 1_555 MG  ? F MG  . ? A MG  802 ? 1_555 O   ? S HOH .   ? A HOH 944  ? 1_555 74.1  ? 
10  O   ? S HOH .   ? A HOH 931  ? 1_555 MG  ? F MG  . ? A MG  802 ? 1_555 O   ? S HOH .   ? A HOH 944  ? 1_555 86.0  ? 
11  O2G ? E DTP .   ? A DTP 801  ? 1_555 MG  ? F MG  . ? A MG  802 ? 1_555 O   ? S HOH .   ? A HOH 984  ? 1_555 179.8 ? 
12  O2B ? E DTP .   ? A DTP 801  ? 1_555 MG  ? F MG  . ? A MG  802 ? 1_555 O   ? S HOH .   ? A HOH 984  ? 1_555 89.9  ? 
13  O2A ? E DTP .   ? A DTP 801  ? 1_555 MG  ? F MG  . ? A MG  802 ? 1_555 O   ? S HOH .   ? A HOH 984  ? 1_555 84.6  ? 
14  O   ? S HOH .   ? A HOH 931  ? 1_555 MG  ? F MG  . ? A MG  802 ? 1_555 O   ? S HOH .   ? A HOH 984  ? 1_555 91.3  ? 
15  O   ? S HOH .   ? A HOH 944  ? 1_555 MG  ? F MG  . ? A MG  802 ? 1_555 O   ? S HOH .   ? A HOH 984  ? 1_555 90.2  ? 
16  O1G ? G ATP .   ? A ATP 803  ? 1_555 MG  ? I MG  . ? A MG  805 ? 1_555 O1B ? G ATP .   ? A ATP 803  ? 1_555 83.4  ? 
17  O1G ? G ATP .   ? A ATP 803  ? 1_555 MG  ? I MG  . ? A MG  805 ? 1_555 O1A ? G ATP .   ? A ATP 803  ? 1_555 87.7  ? 
18  O1B ? G ATP .   ? A ATP 803  ? 1_555 MG  ? I MG  . ? A MG  805 ? 1_555 O1A ? G ATP .   ? A ATP 803  ? 1_555 90.5  ? 
19  O1G ? G ATP .   ? A ATP 803  ? 1_555 MG  ? I MG  . ? A MG  805 ? 1_555 O2G ? H ATP .   ? A ATP 804  ? 1_555 92.2  ? 
20  O1B ? G ATP .   ? A ATP 803  ? 1_555 MG  ? I MG  . ? A MG  805 ? 1_555 O2G ? H ATP .   ? A ATP 804  ? 1_555 174.3 ? 
21  O1A ? G ATP .   ? A ATP 803  ? 1_555 MG  ? I MG  . ? A MG  805 ? 1_555 O2G ? H ATP .   ? A ATP 804  ? 1_555 92.9  ? 
22  O1G ? G ATP .   ? A ATP 803  ? 1_555 MG  ? I MG  . ? A MG  805 ? 1_555 O2B ? H ATP .   ? A ATP 804  ? 1_555 89.8  ? 
23  O1B ? G ATP .   ? A ATP 803  ? 1_555 MG  ? I MG  . ? A MG  805 ? 1_555 O2B ? H ATP .   ? A ATP 804  ? 1_555 88.5  ? 
24  O1A ? G ATP .   ? A ATP 803  ? 1_555 MG  ? I MG  . ? A MG  805 ? 1_555 O2B ? H ATP .   ? A ATP 804  ? 1_555 177.3 ? 
25  O2G ? H ATP .   ? A ATP 804  ? 1_555 MG  ? I MG  . ? A MG  805 ? 1_555 O2B ? H ATP .   ? A ATP 804  ? 1_555 87.9  ? 
26  O1G ? G ATP .   ? A ATP 803  ? 1_555 MG  ? I MG  . ? A MG  805 ? 1_555 O2A ? H ATP .   ? A ATP 804  ? 1_555 179.4 ? 
27  O1B ? G ATP .   ? A ATP 803  ? 1_555 MG  ? I MG  . ? A MG  805 ? 1_555 O2A ? H ATP .   ? A ATP 804  ? 1_555 96.7  ? 
28  O1A ? G ATP .   ? A ATP 803  ? 1_555 MG  ? I MG  . ? A MG  805 ? 1_555 O2A ? H ATP .   ? A ATP 804  ? 1_555 93.0  ? 
29  O2G ? H ATP .   ? A ATP 804  ? 1_555 MG  ? I MG  . ? A MG  805 ? 1_555 O2A ? H ATP .   ? A ATP 804  ? 1_555 87.8  ? 
30  O2B ? H ATP .   ? A ATP 804  ? 1_555 MG  ? I MG  . ? A MG  805 ? 1_555 O2A ? H ATP .   ? A ATP 804  ? 1_555 89.6  ? 
31  O3G ? K ATP .   ? B ATP 801  ? 1_555 MG  ? O MG  . ? B MG  805 ? 1_555 O2A ? K ATP .   ? B ATP 801  ? 1_555 86.2  ? 
32  O3G ? K ATP .   ? B ATP 801  ? 1_555 MG  ? O MG  . ? B MG  805 ? 1_555 O1B ? L ATP .   ? B ATP 802  ? 1_555 86.5  ? 
33  O2A ? K ATP .   ? B ATP 801  ? 1_555 MG  ? O MG  . ? B MG  805 ? 1_555 O1B ? L ATP .   ? B ATP 802  ? 1_555 160.2 ? 
34  O3G ? K ATP .   ? B ATP 801  ? 1_555 MG  ? O MG  . ? B MG  805 ? 1_555 O1A ? L ATP .   ? B ATP 802  ? 1_555 165.6 ? 
35  O2A ? K ATP .   ? B ATP 801  ? 1_555 MG  ? O MG  . ? B MG  805 ? 1_555 O1A ? L ATP .   ? B ATP 802  ? 1_555 96.6  ? 
36  O1B ? L ATP .   ? B ATP 802  ? 1_555 MG  ? O MG  . ? B MG  805 ? 1_555 O1A ? L ATP .   ? B ATP 802  ? 1_555 86.1  ? 
37  O1G ? M DTP .   ? B DTP 803  ? 1_555 MG  ? N MG  . ? B MG  804 ? 1_555 O1B ? M DTP .   ? B DTP 803  ? 1_555 89.9  ? 
38  O1G ? M DTP .   ? B DTP 803  ? 1_555 MG  ? N MG  . ? B MG  804 ? 1_555 O1A ? M DTP .   ? B DTP 803  ? 1_555 90.1  ? 
39  O1B ? M DTP .   ? B DTP 803  ? 1_555 MG  ? N MG  . ? B MG  804 ? 1_555 O1A ? M DTP .   ? B DTP 803  ? 1_555 89.6  ? 
40  O1G ? M DTP .   ? B DTP 803  ? 1_555 MG  ? N MG  . ? B MG  804 ? 1_555 O   ? T HOH .   ? B HOH 990  ? 1_555 90.1  ? 
41  O1B ? M DTP .   ? B DTP 803  ? 1_555 MG  ? N MG  . ? B MG  804 ? 1_555 O   ? T HOH .   ? B HOH 990  ? 1_555 179.8 ? 
42  O1A ? M DTP .   ? B DTP 803  ? 1_555 MG  ? N MG  . ? B MG  804 ? 1_555 O   ? T HOH .   ? B HOH 990  ? 1_555 90.2  ? 
43  O1G ? M DTP .   ? B DTP 803  ? 1_555 MG  ? N MG  . ? B MG  804 ? 1_555 O   ? T HOH .   ? B HOH 1087 ? 1_555 179.9 ? 
44  O1B ? M DTP .   ? B DTP 803  ? 1_555 MG  ? N MG  . ? B MG  804 ? 1_555 O   ? T HOH .   ? B HOH 1087 ? 1_555 90.1  ? 
45  O1A ? M DTP .   ? B DTP 803  ? 1_555 MG  ? N MG  . ? B MG  804 ? 1_555 O   ? T HOH .   ? B HOH 1087 ? 1_555 89.9  ? 
46  O   ? T HOH .   ? B HOH 990  ? 1_555 MG  ? N MG  . ? B MG  804 ? 1_555 O   ? T HOH .   ? B HOH 1087 ? 1_555 89.9  ? 
47  O1G ? M DTP .   ? B DTP 803  ? 1_555 MG  ? N MG  . ? B MG  804 ? 1_555 O   ? T HOH .   ? B HOH 1090 ? 1_555 89.9  ? 
48  O1B ? M DTP .   ? B DTP 803  ? 1_555 MG  ? N MG  . ? B MG  804 ? 1_555 O   ? T HOH .   ? B HOH 1090 ? 1_555 90.5  ? 
49  O1A ? M DTP .   ? B DTP 803  ? 1_555 MG  ? N MG  . ? B MG  804 ? 1_555 O   ? T HOH .   ? B HOH 1090 ? 1_555 179.9 ? 
50  O   ? T HOH .   ? B HOH 990  ? 1_555 MG  ? N MG  . ? B MG  804 ? 1_555 O   ? T HOH .   ? B HOH 1090 ? 1_555 89.7  ? 
51  O   ? T HOH .   ? B HOH 1087 ? 1_555 MG  ? N MG  . ? B MG  804 ? 1_555 O   ? T HOH .   ? B HOH 1090 ? 1_555 90.1  ? 
52  OD1 ? C ASP 85  ? C ASP 84   ? 1_555 FE1 ? Q FEO . ? C FEO 401 ? 1_555 O   ? Q FEO .   ? C FEO 401  ? 1_555 80.8  ? 
53  OD1 ? C ASP 85  ? C ASP 84   ? 1_555 FE1 ? Q FEO . ? C FEO 401 ? 1_555 OD2 ? C ASP 85  ? C ASP 84   ? 1_555 51.3  ? 
54  O   ? Q FEO .   ? C FEO 401  ? 1_555 FE1 ? Q FEO . ? C FEO 401 ? 1_555 OD2 ? C ASP 85  ? C ASP 84   ? 1_555 121.2 ? 
55  OD1 ? C ASP 85  ? C ASP 84   ? 1_555 FE1 ? Q FEO . ? C FEO 401 ? 1_555 OE1 ? C GLU 116 ? C GLU 115  ? 1_555 66.9  ? 
56  O   ? Q FEO .   ? C FEO 401  ? 1_555 FE1 ? Q FEO . ? C FEO 401 ? 1_555 OE1 ? C GLU 116 ? C GLU 115  ? 1_555 79.6  ? 
57  OD2 ? C ASP 85  ? C ASP 84   ? 1_555 FE1 ? Q FEO . ? C FEO 401 ? 1_555 OE1 ? C GLU 116 ? C GLU 115  ? 1_555 104.8 ? 
58  OD1 ? C ASP 85  ? C ASP 84   ? 1_555 FE1 ? Q FEO . ? C FEO 401 ? 1_555 ND1 ? C HIS 119 ? C HIS 118  ? 1_555 158.5 ? 
59  O   ? Q FEO .   ? C FEO 401  ? 1_555 FE1 ? Q FEO . ? C FEO 401 ? 1_555 ND1 ? C HIS 119 ? C HIS 118  ? 1_555 118.6 ? 
60  OD2 ? C ASP 85  ? C ASP 84   ? 1_555 FE1 ? Q FEO . ? C FEO 401 ? 1_555 ND1 ? C HIS 119 ? C HIS 118  ? 1_555 116.2 ? 
61  OE1 ? C GLU 116 ? C GLU 115  ? 1_555 FE1 ? Q FEO . ? C FEO 401 ? 1_555 ND1 ? C HIS 119 ? C HIS 118  ? 1_555 105.6 ? 
62  OD1 ? C ASP 85  ? C ASP 84   ? 1_555 FE1 ? Q FEO . ? C FEO 401 ? 1_555 O   ? U HOH .   ? C HOH 511  ? 1_555 95.2  ? 
63  O   ? Q FEO .   ? C FEO 401  ? 1_555 FE1 ? Q FEO . ? C FEO 401 ? 1_555 O   ? U HOH .   ? C HOH 511  ? 1_555 74.5  ? 
64  OD2 ? C ASP 85  ? C ASP 84   ? 1_555 FE1 ? Q FEO . ? C FEO 401 ? 1_555 O   ? U HOH .   ? C HOH 511  ? 1_555 77.9  ? 
65  OE1 ? C GLU 116 ? C GLU 115  ? 1_555 FE1 ? Q FEO . ? C FEO 401 ? 1_555 O   ? U HOH .   ? C HOH 511  ? 1_555 150.7 ? 
66  ND1 ? C HIS 119 ? C HIS 118  ? 1_555 FE1 ? Q FEO . ? C FEO 401 ? 1_555 O   ? U HOH .   ? C HOH 511  ? 1_555 98.8  ? 
67  OE2 ? C GLU 116 ? C GLU 115  ? 1_555 FE2 ? Q FEO . ? C FEO 401 ? 1_555 O   ? Q FEO .   ? C FEO 401  ? 1_555 99.2  ? 
68  OE2 ? C GLU 116 ? C GLU 115  ? 1_555 FE2 ? Q FEO . ? C FEO 401 ? 1_555 OE1 ? C GLU 239 ? C GLU 238  ? 1_555 149.6 ? 
69  O   ? Q FEO .   ? C FEO 401  ? 1_555 FE2 ? Q FEO . ? C FEO 401 ? 1_555 OE1 ? C GLU 239 ? C GLU 238  ? 1_555 51.2  ? 
70  OE2 ? C GLU 116 ? C GLU 115  ? 1_555 FE2 ? Q FEO . ? C FEO 401 ? 1_555 OE2 ? C GLU 239 ? C GLU 238  ? 1_555 131.6 ? 
71  O   ? Q FEO .   ? C FEO 401  ? 1_555 FE2 ? Q FEO . ? C FEO 401 ? 1_555 OE2 ? C GLU 239 ? C GLU 238  ? 1_555 82.1  ? 
72  OE1 ? C GLU 239 ? C GLU 238  ? 1_555 FE2 ? Q FEO . ? C FEO 401 ? 1_555 OE2 ? C GLU 239 ? C GLU 238  ? 1_555 48.1  ? 
73  OE2 ? C GLU 116 ? C GLU 115  ? 1_555 FE2 ? Q FEO . ? C FEO 401 ? 1_555 ND1 ? C HIS 242 ? C HIS 241  ? 1_555 74.3  ? 
74  O   ? Q FEO .   ? C FEO 401  ? 1_555 FE2 ? Q FEO . ? C FEO 401 ? 1_555 ND1 ? C HIS 242 ? C HIS 241  ? 1_555 158.4 ? 
75  OE1 ? C GLU 239 ? C GLU 238  ? 1_555 FE2 ? Q FEO . ? C FEO 401 ? 1_555 ND1 ? C HIS 242 ? C HIS 241  ? 1_555 135.6 ? 
76  OE2 ? C GLU 239 ? C GLU 238  ? 1_555 FE2 ? Q FEO . ? C FEO 401 ? 1_555 ND1 ? C HIS 242 ? C HIS 241  ? 1_555 117.8 ? 
77  OD1 ? D ASP 85  ? D ASP 84   ? 1_555 FE1 ? R FEO . ? D FEO 401 ? 1_555 O   ? R FEO .   ? D FEO 401  ? 1_555 90.9  ? 
78  OD1 ? D ASP 85  ? D ASP 84   ? 1_555 FE1 ? R FEO . ? D FEO 401 ? 1_555 OD2 ? D ASP 85  ? D ASP 84   ? 1_555 59.6  ? 
79  O   ? R FEO .   ? D FEO 401  ? 1_555 FE1 ? R FEO . ? D FEO 401 ? 1_555 OD2 ? D ASP 85  ? D ASP 84   ? 1_555 134.1 ? 
80  OD1 ? D ASP 85  ? D ASP 84   ? 1_555 FE1 ? R FEO . ? D FEO 401 ? 1_555 OE1 ? D GLU 116 ? D GLU 115  ? 1_555 77.8  ? 
81  O   ? R FEO .   ? D FEO 401  ? 1_555 FE1 ? R FEO . ? D FEO 401 ? 1_555 OE1 ? D GLU 116 ? D GLU 115  ? 1_555 80.3  ? 
82  OD2 ? D ASP 85  ? D ASP 84   ? 1_555 FE1 ? R FEO . ? D FEO 401 ? 1_555 OE1 ? D GLU 116 ? D GLU 115  ? 1_555 120.8 ? 
83  OD1 ? D ASP 85  ? D ASP 84   ? 1_555 FE1 ? R FEO . ? D FEO 401 ? 1_555 ND1 ? D HIS 119 ? D HIS 118  ? 1_555 147.8 ? 
84  O   ? R FEO .   ? D FEO 401  ? 1_555 FE1 ? R FEO . ? D FEO 401 ? 1_555 ND1 ? D HIS 119 ? D HIS 118  ? 1_555 120.8 ? 
85  OD2 ? D ASP 85  ? D ASP 84   ? 1_555 FE1 ? R FEO . ? D FEO 401 ? 1_555 ND1 ? D HIS 119 ? D HIS 118  ? 1_555 96.6  ? 
86  OE1 ? D GLU 116 ? D GLU 115  ? 1_555 FE1 ? R FEO . ? D FEO 401 ? 1_555 ND1 ? D HIS 119 ? D HIS 118  ? 1_555 100.3 ? 
87  OD1 ? D ASP 85  ? D ASP 84   ? 1_555 FE1 ? R FEO . ? D FEO 401 ? 1_555 O   ? V HOH .   ? D HOH 504  ? 1_555 99.3  ? 
88  O   ? R FEO .   ? D FEO 401  ? 1_555 FE1 ? R FEO . ? D FEO 401 ? 1_555 O   ? V HOH .   ? D HOH 504  ? 1_555 80.7  ? 
89  OD2 ? D ASP 85  ? D ASP 84   ? 1_555 FE1 ? R FEO . ? D FEO 401 ? 1_555 O   ? V HOH .   ? D HOH 504  ? 1_555 71.7  ? 
90  OE1 ? D GLU 116 ? D GLU 115  ? 1_555 FE1 ? R FEO . ? D FEO 401 ? 1_555 O   ? V HOH .   ? D HOH 504  ? 1_555 160.7 ? 
91  ND1 ? D HIS 119 ? D HIS 118  ? 1_555 FE1 ? R FEO . ? D FEO 401 ? 1_555 O   ? V HOH .   ? D HOH 504  ? 1_555 92.2  ? 
92  OE2 ? D GLU 116 ? D GLU 115  ? 1_555 FE2 ? R FEO . ? D FEO 401 ? 1_555 O   ? R FEO .   ? D FEO 401  ? 1_555 100.0 ? 
93  OE2 ? D GLU 116 ? D GLU 115  ? 1_555 FE2 ? R FEO . ? D FEO 401 ? 1_555 OE2 ? D GLU 205 ? D GLU 204  ? 1_555 74.1  ? 
94  O   ? R FEO .   ? D FEO 401  ? 1_555 FE2 ? R FEO . ? D FEO 401 ? 1_555 OE2 ? D GLU 205 ? D GLU 204  ? 1_555 103.1 ? 
95  OE2 ? D GLU 116 ? D GLU 115  ? 1_555 FE2 ? R FEO . ? D FEO 401 ? 1_555 OE2 ? D GLU 239 ? D GLU 238  ? 1_555 127.5 ? 
96  O   ? R FEO .   ? D FEO 401  ? 1_555 FE2 ? R FEO . ? D FEO 401 ? 1_555 OE2 ? D GLU 239 ? D GLU 238  ? 1_555 61.3  ? 
97  OE2 ? D GLU 205 ? D GLU 204  ? 1_555 FE2 ? R FEO . ? D FEO 401 ? 1_555 OE2 ? D GLU 239 ? D GLU 238  ? 1_555 65.0  ? 
98  OE2 ? D GLU 116 ? D GLU 115  ? 1_555 FE2 ? R FEO . ? D FEO 401 ? 1_555 ND1 ? D HIS 242 ? D HIS 241  ? 1_555 89.8  ? 
99  O   ? R FEO .   ? D FEO 401  ? 1_555 FE2 ? R FEO . ? D FEO 401 ? 1_555 ND1 ? D HIS 242 ? D HIS 241  ? 1_555 162.5 ? 
100 OE2 ? D GLU 205 ? D GLU 204  ? 1_555 FE2 ? R FEO . ? D FEO 401 ? 1_555 ND1 ? D HIS 242 ? D HIS 241  ? 1_555 93.5  ? 
101 OE2 ? D GLU 239 ? D GLU 238  ? 1_555 FE2 ? R FEO . ? D FEO 401 ? 1_555 ND1 ? D HIS 242 ? D HIS 241  ? 1_555 123.0 ? 
# 
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 A1A3L P .   ? CYS B 225 ? A1A3L B 806 ? 1_555 CYS B 225 ? 1_555 N01 SG CYS 1 A1A3L None 'Covalent chemical modification' 
2 CYS   A 225 A CYS A 462 ? CYS   A 225 ? 1_555 CYS A 462 ? 1_555 SG  SG .   . .     None 'Disulfide bridge'               
3 CYS   C 269 ? CYS C 273 ? CYS   C 268 ? 1_555 CYS C 272 ? 1_555 SG  SG .   . .     None 'Disulfide bridge'               
4 CYS   D 269 ? CYS D 273 ? CYS   D 268 ? 1_555 CYS D 272 ? 1_555 SG  SG .   . .     None 'Disulfide bridge'               
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
AA7 ? 2 ? 
AA8 ? 3 ? 
AA9 ? 3 ? 
AB1 ? 8 ? 
AB2 ? 2 ? 
AB3 ? 2 ? 
AB4 ? 3 ? 
AB5 ? 2 ? 
AB6 ? 2 ? 
AB7 ? 2 ? 
# 
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      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? parallel      
AA7 1 2 ? parallel      
AA8 1 2 ? anti-parallel 
AA8 2 3 ? parallel      
AA9 1 2 ? anti-parallel 
AA9 2 3 ? parallel      
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? parallel      
AB1 4 5 ? parallel      
AB1 5 6 ? parallel      
AB1 6 7 ? parallel      
AB1 7 8 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? parallel      
AB5 1 2 ? parallel      
AB6 1 2 ? anti-parallel 
AB7 1 2 ? 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 ILE A 205 ? SER A 206 ? ILE A 205 SER A 206 
AA1 2 LEU A 464 ? ASN A 468 ? LEU A 464 ASN A 468 
AA1 3 GLY A 514 ? ILE A 518 ? GLY A 514 ILE A 518 
AA2 1 ALA A 460 ? LEU A 461 ? ALA A 460 LEU A 461 
AA2 2 CYS A 225 ? GLU A 229 ? CYS A 225 GLU A 229 
AA2 3 GLY A 253 ? ASN A 257 ? GLY A 253 ASN A 257 
AA2 4 ALA A 302 ? PRO A 307 ? ALA A 302 PRO A 307 
AA2 5 ASP A 334 ? ILE A 339 ? ASP A 334 ILE A 339 
AA2 6 ILE A 412 ? ASN A 416 ? ILE A 412 ASN A 416 
AA2 7 THR A 728 ? LEU A 729 ? THR A 728 LEU A 729 
AA3 1 PRO A 267 ? ILE A 268 ? PRO A 267 ILE A 268 
AA3 2 ALA A 273 ? PHE A 274 ? ALA A 273 PHE A 274 
AA4 1 ASP A 352 ? PHE A 356 ? ASP A 352 PHE A 356 
AA4 2 LYS A 390 ? LYS A 394 ? LYS A 390 LYS A 394 
AA5 1 VAL A 642 ? LYS A 645 ? VAL A 642 LYS A 645 
AA5 2 LEU A 652 ? VAL A 655 ? LEU A 652 VAL A 655 
AA6 1 THR A 697 ? TYR A 699 ? THR A 697 TYR A 699 
AA6 2 GLN A 732 ? THR A 734 ? GLN A 732 THR A 734 
AA7 1 VAL A 709 ? PRO A 710 ? VAL A 709 PRO A 710 
AA7 2 ILE D 362 ? ASP D 363 ? ILE D 361 ASP D 362 
AA8 1 THR B 14  ? ARG B 16  ? THR B 14  ARG B 16  
AA8 2 LEU B 6   ? THR B 8   ? LEU B 6   THR B 8   
AA8 3 ILE B 53  ? LYS B 54  ? ILE B 53  LYS B 54  
AA9 1 ILE B 205 ? SER B 206 ? ILE B 205 SER B 206 
AA9 2 ALA B 460 ? ASN B 468 ? ALA B 460 ASN B 468 
AA9 3 LEU B 513 ? ILE B 518 ? LEU B 513 ILE B 518 
AB1 1 ILE B 205 ? SER B 206 ? ILE B 205 SER B 206 
AB1 2 ALA B 460 ? ASN B 468 ? ALA B 460 ASN B 468 
AB1 3 CYS B 225 ? GLU B 229 ? CYS B 225 GLU B 229 
AB1 4 GLY B 253 ? ASN B 257 ? GLY B 253 ASN B 257 
AB1 5 ALA B 302 ? PRO B 307 ? ALA B 302 PRO B 307 
AB1 6 ASP B 334 ? ILE B 339 ? ASP B 334 ILE B 339 
AB1 7 ILE B 412 ? ASN B 416 ? ILE B 412 ASN B 416 
AB1 8 THR B 728 ? LEU B 729 ? THR B 728 LEU B 729 
AB2 1 PRO B 267 ? ILE B 268 ? PRO B 267 ILE B 268 
AB2 2 ALA B 273 ? PHE B 274 ? ALA B 273 PHE B 274 
AB3 1 ASP B 352 ? PHE B 356 ? ASP B 352 PHE B 356 
AB3 2 LYS B 390 ? LYS B 394 ? LYS B 390 LYS B 394 
AB4 1 GLY B 650 ? VAL B 655 ? GLY B 650 VAL B 655 
AB4 2 VAL B 642 ? SER B 647 ? VAL B 642 SER B 647 
AB4 3 VAL C 345 ? VAL C 347 ? VAL C 344 VAL C 346 
AB5 1 THR B 697 ? TYR B 699 ? THR B 697 TYR B 699 
AB5 2 GLN B 732 ? THR B 734 ? GLN B 732 THR B 734 
AB6 1 GLY C 174 ? VAL C 178 ? GLY C 173 VAL C 177 
AB6 2 LYS C 181 ? VAL C 185 ? LYS C 180 VAL C 184 
AB7 1 GLY D 174 ? VAL D 178 ? GLY D 173 VAL D 177 
AB7 2 LYS D 181 ? VAL D 185 ? LYS D 180 VAL D 184 
# 
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 SER A 206 ? N SER A 206 O ALA A 466 ? O ALA A 466 
AA1 2 3 N SER A 465 ? N SER A 465 O GLY A 516 ? O GLY A 516 
AA2 1 2 O ALA A 460 ? O ALA A 460 N LEU A 227 ? N LEU A 227 
AA2 2 3 N ILE A 228 ? N ILE A 228 O GLY A 255 ? O GLY A 255 
AA2 3 4 N ILE A 256 ? N ILE A 256 O THR A 303 ? O THR A 303 
AA2 4 5 N LEU A 304 ? N LEU A 304 O ASP A 334 ? O ASP A 334 
AA2 5 6 N TYR A 335 ? N TYR A 335 O TYR A 413 ? O TYR A 413 
AA2 6 7 N ILE A 414 ? N ILE A 414 O LEU A 729 ? O LEU A 729 
AA3 1 2 N ILE A 268 ? N ILE A 268 O ALA A 273 ? O ALA A 273 
AA4 1 2 N LEU A 355 ? N LEU A 355 O GLN A 391 ? O GLN A 391 
AA5 1 2 N LYS A 645 ? N LYS A 645 O LEU A 652 ? O LEU A 652 
AA6 1 2 N TYR A 699 ? N TYR A 699 O ASN A 733 ? O ASN A 733 
AA7 1 2 N VAL A 709 ? N VAL A 709 O ASP D 363 ? O ASP D 362 
AA8 1 2 O GLU B 15  ? O GLU B 15  N VAL B 7   ? N VAL B 7   
AA8 2 3 N THR B 8   ? N THR B 8   O ILE B 53  ? O ILE B 53  
AA9 1 2 N SER B 206 ? N SER B 206 O ALA B 466 ? O ALA B 466 
AA9 2 3 N THR B 463 ? N THR B 463 O GLY B 514 ? O GLY B 514 
AB1 1 2 N SER B 206 ? N SER B 206 O ALA B 466 ? O ALA B 466 
AB1 2 3 O ALA B 460 ? O ALA B 460 N LEU B 227 ? N LEU B 227 
AB1 3 4 N VAL B 226 ? N VAL B 226 O GLY B 255 ? O GLY B 255 
AB1 4 5 N ILE B 256 ? N ILE B 256 O PHE B 305 ? O PHE B 305 
AB1 5 6 N LEU B 304 ? N LEU B 304 O GLY B 336 ? O GLY B 336 
AB1 6 7 N VAL B 337 ? N VAL B 337 O TYR B 413 ? O TYR B 413 
AB1 7 8 N ILE B 414 ? N ILE B 414 O LEU B 729 ? O LEU B 729 
AB2 1 2 N ILE B 268 ? N ILE B 268 O ALA B 273 ? O ALA B 273 
AB3 1 2 N LEU B 355 ? N LEU B 355 O GLN B 391 ? O GLN B 391 
AB4 1 2 O LEU B 652 ? O LEU B 652 N LYS B 645 ? N LYS B 645 
AB4 2 3 N ILE B 644 ? N ILE B 644 O GLN C 346 ? O GLN C 345 
AB5 1 2 N TYR B 699 ? N TYR B 699 O ASN B 733 ? O ASN B 733 
AB6 1 2 N GLY C 174 ? N GLY C 173 O VAL C 185 ? O VAL C 184 
AB7 1 2 N VAL D 178 ? N VAL D 177 O LYS D 181 ? O LYS D 180 
# 
_pdbx_entry_details.entry_id                   9DB2 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O1G B ATP 802  ? ? MG B MG  805  ? ? 1.30 
2  1 O   A HOH 994  ? ? O  A HOH 1011 ? ? 1.43 
3  1 O1B B ATP 801  ? ? MG B MG  805  ? ? 1.66 
4  1 O   B HOH 953  ? ? O  B HOH 1026 ? ? 1.94 
5  1 NE2 A GLN 294  ? ? O  A HOH 901  ? ? 2.04 
6  1 O   B VAL 215  ? ? O  B HOH 901  ? ? 2.06 
7  1 O   D HOH 528  ? ? O  D HOH 530  ? ? 2.08 
8  1 O   B HOH 1109 ? ? O  C HOH 580  ? ? 2.10 
9  1 OE1 C GLU 238  ? ? O  C FEO 401  ? ? 2.10 
10 1 O   B HOH 1002 ? ? O  B HOH 1176 ? ? 2.11 
11 1 NE2 B GLN 654  ? ? O  B HOH 902  ? ? 2.13 
12 1 OG1 B THR 446  ? ? O  B HOH 903  ? ? 2.13 
13 1 OG  B SER 359  ? ? O  B HOH 904  ? ? 2.14 
14 1 O   A HOH 982  ? ? O  B HOH 1008 ? ? 2.15 
15 1 O   A CYS 230  ? ? O  A HOH 902  ? ? 2.15 
16 1 O   A HOH 938  ? ? O  B HOH 1170 ? ? 2.15 
17 1 O   B ALA 741  ? ? O  B HOH 905  ? ? 2.15 
18 1 O   B HOH 1104 ? ? O  B HOH 1115 ? ? 2.16 
19 1 OD1 B ASN 257  ? ? O  B HOH 906  ? ? 2.16 
20 1 O   D HOH 567  ? ? O  D HOH 569  ? ? 2.16 
21 1 O   A HOH 932  ? ? O  A HOH 1030 ? ? 2.18 
22 1 N   A LYS 585  ? ? O  A HOH 903  ? ? 2.18 
23 1 OH  A TYR 344  ? ? O  A HOH 904  ? ? 2.19 
24 1 NH1 A ARG 298  ? ? O  A HOH 905  ? ? 2.19 
25 1 O   B HOH 1113 ? ? O  B HOH 1149 ? ? 2.19 
26 1 O   B VAL 517  ? ? O  B HOH 907  ? ? 2.19 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            C 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            ILE 
_pdbx_validate_rmsd_bond.auth_seq_id_1             47 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            N 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            GLN 
_pdbx_validate_rmsd_bond.auth_seq_id_2             48 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.591 
_pdbx_validate_rmsd_bond.bond_target_value         1.336 
_pdbx_validate_rmsd_bond.bond_deviation            0.255 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.023 
_pdbx_validate_rmsd_bond.linker_flag               Y 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CA A GLN 48  ? ? C  A GLN 48  ? ? N  A PHE 49  ? ? 133.24 117.20 16.04  2.20 Y 
2 1 O  A GLN 48  ? ? C  A GLN 48  ? ? N  A PHE 49  ? ? 101.99 122.70 -20.71 1.60 Y 
3 1 CB A CYS 462 ? ? CA A CYS 462 ? ? C  A CYS 462 ? ? 94.78  110.40 -15.62 2.00 N 
4 1 N  A CYS 462 ? ? CA A CYS 462 ? ? C  A CYS 462 ? ? 81.04  111.00 -29.96 2.70 N 
5 1 N  A THR 463 ? ? CA A THR 463 ? ? CB A THR 463 ? ? 89.47  110.30 -20.83 1.90 N 
6 1 CB A GLU 636 ? ? CA A GLU 636 ? ? C  A GLU 636 ? ? 98.22  110.40 -12.18 2.00 N 
# 
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 PHE A 49  ? ? -118.12 77.31   
2  1 VAL A 161 ? ? -103.76 -61.24  
3  1 ASN A 183 ? ? -89.54  46.97   
4  1 PHE A 203 ? ? 70.29   43.33   
5  1 ARG A 216 ? ? 79.48   -7.46   
6  1 PHE A 222 ? ? -108.25 76.08   
7  1 PHE A 222 ? ? -111.61 76.08   
8  1 SER A 223 ? ? -64.67  -169.75 
9  1 SER A 224 ? ? 169.19  -112.08 
10 1 ARG A 298 ? ? -130.07 -67.70  
11 1 TYR A 731 ? ? -19.89  140.66  
12 1 TYR A 731 ? ? -20.80  141.22  
13 1 ARG B 220 ? ? -103.00 65.93   
14 1 ARG B 220 ? ? -109.34 73.91   
15 1 GLN B 691 ? ? -110.94 -167.98 
16 1 TYR B 730 ? ? -90.86  -158.87 
17 1 ASP C 139 ? ? -96.60  56.90   
18 1 ILE C 140 ? ? -125.39 -55.65  
19 1 ILE C 206 ? ? -126.03 -51.91  
20 1 ARG C 328 ? ? -119.76 -164.57 
21 1 GLN C 360 ? ? -94.04  32.25   
22 1 SER C 363 ? ? 72.58   -1.35   
23 1 ILE D 206 ? ? -120.39 -52.51  
24 1 ASP D 293 ? ? -94.21  51.78   
25 1 ASN D 372 ? ? -79.91  -106.16 
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             GLN 
_pdbx_validate_main_chain_plane.auth_asym_id             A 
_pdbx_validate_main_chain_plane.auth_seq_id              48 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   -17.42 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9DB2 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_reconstruction.entry_id                    9DB2 
_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                  2.6 
_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               440549 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_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            7.6 
# 
_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                 
'Active state of class Ia ribonucleotide reductase trapped with mechanism-based inhibitor N3CDP' 
_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                        9DB2 
_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           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               OTHER 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             1000 
_em_imaging.nominal_defocus_max             2300 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_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             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_vitrification.entry_id              9DB2 
_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                9DB2 
_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              9DB2 
_em_single_particle_entity.id                    1 
_em_single_particle_entity.image_processing_id   1 
_em_single_particle_entity.point_symmetry        C1 
# 
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 1   ? A MET 1   
2  1 Y 1 A ASN 2   ? A ASN 2   
3  1 Y 1 A GLN 3   ? A GLN 3   
4  1 Y 1 A ASN 4   ? A ASN 4   
5  1 Y 1 A LEU 5   ? A LEU 5   
6  1 Y 1 A LEU 6   ? A LEU 6   
7  1 Y 1 A ASP 740 ? A ASP 740 
8  1 Y 1 A ALA 741 ? A ALA 741 
9  1 Y 1 A GLN 742 ? A GLN 742 
10 1 Y 1 A ASP 743 ? A ASP 743 
11 1 Y 1 A ASP 744 ? A ASP 744 
12 1 Y 1 A LEU 745 ? A LEU 745 
13 1 Y 1 A VAL 746 ? A VAL 746 
14 1 Y 1 A PRO 747 ? A PRO 747 
15 1 Y 1 A SER 748 ? A SER 748 
16 1 Y 1 A ILE 749 ? A ILE 749 
17 1 Y 1 A GLN 750 ? A GLN 750 
18 1 Y 1 A ASP 751 ? A ASP 751 
19 1 Y 1 A ASP 752 ? A ASP 752 
20 1 Y 1 A GLY 753 ? A GLY 753 
21 1 Y 1 A CYS 754 ? A CYS 754 
22 1 Y 1 A GLU 755 ? A GLU 755 
23 1 Y 1 A SER 756 ? A SER 756 
24 1 Y 1 A GLY 757 ? A GLY 757 
25 1 Y 1 A ALA 758 ? A ALA 758 
26 1 Y 1 A CYS 759 ? A CYS 759 
27 1 Y 1 A LYS 760 ? A LYS 760 
28 1 Y 1 A ILE 761 ? A ILE 761 
29 1 Y 1 B MET 1   ? B MET 1   
30 1 Y 1 B VAL 746 ? B VAL 746 
31 1 Y 1 B PRO 747 ? B PRO 747 
32 1 Y 1 B SER 748 ? B SER 748 
33 1 Y 1 B ILE 749 ? B ILE 749 
34 1 Y 1 B GLN 750 ? B GLN 750 
35 1 Y 1 B ASP 751 ? B ASP 751 
36 1 Y 1 B ASP 752 ? B ASP 752 
37 1 Y 1 B GLY 753 ? B GLY 753 
38 1 Y 1 B CYS 754 ? B CYS 754 
39 1 Y 1 B GLU 755 ? B GLU 755 
40 1 Y 1 B SER 756 ? B SER 756 
41 1 Y 1 B GLY 757 ? B GLY 757 
42 1 Y 1 B ALA 758 ? B ALA 758 
43 1 Y 1 B CYS 759 ? B CYS 759 
44 1 Y 1 B LYS 760 ? B LYS 760 
45 1 Y 1 B ILE 761 ? B ILE 761 
46 1 Y 1 C MET 0   ? C MET 1   
47 1 Y 1 D MET 0   ? D MET 1   
48 1 Y 1 D VAL 340 ? D VAL 341 
49 1 Y 1 D SER 341 ? D SER 342 
50 1 Y 1 D ASP 342 ? D ASP 343 
51 1 Y 1 D ASN 343 ? D ASN 344 
52 1 Y 1 D VAL 344 ? D VAL 345 
53 1 Y 1 D GLN 345 ? D GLN 346 
54 1 Y 1 D VAL 346 ? D VAL 347 
55 1 Y 1 D ALA 347 ? D ALA 348 
56 1 Y 1 D PRO 348 ? D PRO 349 
57 1 Y 1 D GLN 349 ? D GLN 350 
58 1 Y 1 D GLU 350 ? D GLU 351 
59 1 Y 1 D VAL 351 ? D VAL 352 
60 1 Y 1 D GLU 352 ? D GLU 353 
61 1 Y 1 D VAL 353 ? D VAL 354 
62 1 Y 1 D SER 354 ? D SER 355 
63 1 Y 1 D SER 355 ? D SER 356 
64 1 Y 1 D TYR 356 ? D TYR 357 
65 1 Y 1 D LEU 357 ? D LEU 358 
66 1 Y 1 D VAL 358 ? D VAL 359 
67 1 Y 1 D GLY 359 ? D GLY 360 
68 1 Y 1 D GLN 374 ? D GLN 375 
69 1 Y 1 D LEU 375 ? D LEU 376 
# 
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 
A1A3L C2     C  N N 1   
A1A3L N3     N  N N 2   
A1A3L C4     C  N N 3   
A1A3L C5     C  N N 4   
A1A3L C6     C  N N 5   
A1A3L "C1'"  C  N R 6   
A1A3L "C2'"  C  N N 7   
A1A3L "C3'"  C  N R 8   
A1A3L "C4'"  C  N R 9   
A1A3L "C5'"  C  N N 10  
A1A3L N01    N  N N 11  
A1A3L N1     N  N N 12  
A1A3L N4     N  N N 13  
A1A3L O01    O  N N 14  
A1A3L O1A    O  N N 15  
A1A3L O1B    O  N N 16  
A1A3L O2     O  N N 17  
A1A3L O2A    O  N N 18  
A1A3L O2B    O  N N 19  
A1A3L O3A    O  N N 20  
A1A3L O3B    O  N N 21  
A1A3L "O4'"  O  N N 22  
A1A3L "O5'"  O  N N 23  
A1A3L PA     P  N N 24  
A1A3L PB     P  N N 25  
A1A3L H1     H  N N 26  
A1A3L H2     H  N N 27  
A1A3L H3     H  N N 28  
A1A3L H4     H  N N 29  
A1A3L H5     H  N N 30  
A1A3L H6     H  N N 31  
A1A3L H7     H  N N 32  
A1A3L H8     H  N N 33  
A1A3L H9     H  N N 34  
A1A3L H10    H  N N 35  
A1A3L H12    H  N N 36  
A1A3L H13    H  N N 37  
A1A3L H14    H  N N 38  
A1A3L H15    H  N N 39  
A1A3L H16    H  N N 40  
A1A3L H17    H  N N 41  
ALA   N      N  N N 42  
ALA   CA     C  N S 43  
ALA   C      C  N N 44  
ALA   O      O  N N 45  
ALA   CB     C  N N 46  
ALA   OXT    O  N N 47  
ALA   H      H  N N 48  
ALA   H2     H  N N 49  
ALA   HA     H  N N 50  
ALA   HB1    H  N N 51  
ALA   HB2    H  N N 52  
ALA   HB3    H  N N 53  
ALA   HXT    H  N N 54  
ARG   N      N  N N 55  
ARG   CA     C  N S 56  
ARG   C      C  N N 57  
ARG   O      O  N N 58  
ARG   CB     C  N N 59  
ARG   CG     C  N N 60  
ARG   CD     C  N N 61  
ARG   NE     N  N N 62  
ARG   CZ     C  N N 63  
ARG   NH1    N  N N 64  
ARG   NH2    N  N N 65  
ARG   OXT    O  N N 66  
ARG   H      H  N N 67  
ARG   H2     H  N N 68  
ARG   HA     H  N N 69  
ARG   HB2    H  N N 70  
ARG   HB3    H  N N 71  
ARG   HG2    H  N N 72  
ARG   HG3    H  N N 73  
ARG   HD2    H  N N 74  
ARG   HD3    H  N N 75  
ARG   HE     H  N N 76  
ARG   HH11   H  N N 77  
ARG   HH12   H  N N 78  
ARG   HH21   H  N N 79  
ARG   HH22   H  N N 80  
ARG   HXT    H  N N 81  
ASN   N      N  N N 82  
ASN   CA     C  N S 83  
ASN   C      C  N N 84  
ASN   O      O  N N 85  
ASN   CB     C  N N 86  
ASN   CG     C  N N 87  
ASN   OD1    O  N N 88  
ASN   ND2    N  N N 89  
ASN   OXT    O  N N 90  
ASN   H      H  N N 91  
ASN   H2     H  N N 92  
ASN   HA     H  N N 93  
ASN   HB2    H  N N 94  
ASN   HB3    H  N N 95  
ASN   HD21   H  N N 96  
ASN   HD22   H  N N 97  
ASN   HXT    H  N N 98  
ASP   N      N  N N 99  
ASP   CA     C  N S 100 
ASP   C      C  N N 101 
ASP   O      O  N N 102 
ASP   CB     C  N N 103 
ASP   CG     C  N N 104 
ASP   OD1    O  N N 105 
ASP   OD2    O  N N 106 
ASP   OXT    O  N N 107 
ASP   H      H  N N 108 
ASP   H2     H  N N 109 
ASP   HA     H  N N 110 
ASP   HB2    H  N N 111 
ASP   HB3    H  N N 112 
ASP   HD2    H  N N 113 
ASP   HXT    H  N N 114 
ATP   PG     P  N N 115 
ATP   O1G    O  N N 116 
ATP   O2G    O  N N 117 
ATP   O3G    O  N N 118 
ATP   PB     P  N R 119 
ATP   O1B    O  N N 120 
ATP   O2B    O  N N 121 
ATP   O3B    O  N N 122 
ATP   PA     P  N R 123 
ATP   O1A    O  N N 124 
ATP   O2A    O  N N 125 
ATP   O3A    O  N N 126 
ATP   "O5'"  O  N N 127 
ATP   "C5'"  C  N N 128 
ATP   "C4'"  C  N R 129 
ATP   "O4'"  O  N N 130 
ATP   "C3'"  C  N S 131 
ATP   "O3'"  O  N N 132 
ATP   "C2'"  C  N R 133 
ATP   "O2'"  O  N N 134 
ATP   "C1'"  C  N R 135 
ATP   N9     N  Y N 136 
ATP   C8     C  Y N 137 
ATP   N7     N  Y N 138 
ATP   C5     C  Y N 139 
ATP   C6     C  Y N 140 
ATP   N6     N  N N 141 
ATP   N1     N  Y N 142 
ATP   C2     C  Y N 143 
ATP   N3     N  Y N 144 
ATP   C4     C  Y N 145 
ATP   HOG2   H  N N 146 
ATP   HOG3   H  N N 147 
ATP   HOB2   H  N N 148 
ATP   HOA2   H  N N 149 
ATP   "H5'1" H  N N 150 
ATP   "H5'2" H  N N 151 
ATP   "H4'"  H  N N 152 
ATP   "H3'"  H  N N 153 
ATP   "HO3'" H  N N 154 
ATP   "H2'"  H  N N 155 
ATP   "HO2'" H  N N 156 
ATP   "H1'"  H  N N 157 
ATP   H8     H  N N 158 
ATP   HN61   H  N N 159 
ATP   HN62   H  N N 160 
ATP   H2     H  N N 161 
CYS   N      N  N N 162 
CYS   CA     C  N R 163 
CYS   C      C  N N 164 
CYS   O      O  N N 165 
CYS   CB     C  N N 166 
CYS   SG     S  N N 167 
CYS   OXT    O  N N 168 
CYS   H      H  N N 169 
CYS   H2     H  N N 170 
CYS   HA     H  N N 171 
CYS   HB2    H  N N 172 
CYS   HB3    H  N N 173 
CYS   HG     H  N N 174 
CYS   HXT    H  N N 175 
DTP   PG     P  N N 176 
DTP   O1G    O  N N 177 
DTP   O2G    O  N N 178 
DTP   O3G    O  N N 179 
DTP   PB     P  N S 180 
DTP   O1B    O  N N 181 
DTP   O2B    O  N N 182 
DTP   O3B    O  N N 183 
DTP   PA     P  N S 184 
DTP   O1A    O  N N 185 
DTP   O2A    O  N N 186 
DTP   O3A    O  N N 187 
DTP   "O5'"  O  N N 188 
DTP   "C5'"  C  N N 189 
DTP   "C4'"  C  N R 190 
DTP   "O4'"  O  N N 191 
DTP   "C3'"  C  N S 192 
DTP   "O3'"  O  N N 193 
DTP   "C2'"  C  N N 194 
DTP   "C1'"  C  N R 195 
DTP   N9     N  Y N 196 
DTP   C8     C  Y N 197 
DTP   N7     N  Y N 198 
DTP   C5     C  Y N 199 
DTP   C6     C  Y N 200 
DTP   N6     N  N N 201 
DTP   N1     N  Y N 202 
DTP   C2     C  Y N 203 
DTP   N3     N  Y N 204 
DTP   C4     C  Y N 205 
DTP   HOG2   H  N N 206 
DTP   HOG3   H  N N 207 
DTP   HOB2   H  N N 208 
DTP   HOA2   H  N N 209 
DTP   "H5'1" H  N N 210 
DTP   "H5'2" H  N N 211 
DTP   "H4'"  H  N N 212 
DTP   "H3'"  H  N N 213 
DTP   "HO3'" H  N N 214 
DTP   "H2'1" H  N N 215 
DTP   "H2'2" H  N N 216 
DTP   "H1'"  H  N N 217 
DTP   H8     H  N N 218 
DTP   HN61   H  N N 219 
DTP   HN62   H  N N 220 
DTP   H2     H  N N 221 
FEO   FE1    FE N N 222 
FEO   FE2    FE N N 223 
FEO   O      O  N N 224 
GLN   N      N  N N 225 
GLN   CA     C  N S 226 
GLN   C      C  N N 227 
GLN   O      O  N N 228 
GLN   CB     C  N N 229 
GLN   CG     C  N N 230 
GLN   CD     C  N N 231 
GLN   OE1    O  N N 232 
GLN   NE2    N  N N 233 
GLN   OXT    O  N N 234 
GLN   H      H  N N 235 
GLN   H2     H  N N 236 
GLN   HA     H  N N 237 
GLN   HB2    H  N N 238 
GLN   HB3    H  N N 239 
GLN   HG2    H  N N 240 
GLN   HG3    H  N N 241 
GLN   HE21   H  N N 242 
GLN   HE22   H  N N 243 
GLN   HXT    H  N N 244 
GLU   N      N  N N 245 
GLU   CA     C  N S 246 
GLU   C      C  N N 247 
GLU   O      O  N N 248 
GLU   CB     C  N N 249 
GLU   CG     C  N N 250 
GLU   CD     C  N N 251 
GLU   OE1    O  N N 252 
GLU   OE2    O  N N 253 
GLU   OXT    O  N N 254 
GLU   H      H  N N 255 
GLU   H2     H  N N 256 
GLU   HA     H  N N 257 
GLU   HB2    H  N N 258 
GLU   HB3    H  N N 259 
GLU   HG2    H  N N 260 
GLU   HG3    H  N N 261 
GLU   HE2    H  N N 262 
GLU   HXT    H  N N 263 
GLY   N      N  N N 264 
GLY   CA     C  N N 265 
GLY   C      C  N N 266 
GLY   O      O  N N 267 
GLY   OXT    O  N N 268 
GLY   H      H  N N 269 
GLY   H2     H  N N 270 
GLY   HA2    H  N N 271 
GLY   HA3    H  N N 272 
GLY   HXT    H  N N 273 
HIS   N      N  N N 274 
HIS   CA     C  N S 275 
HIS   C      C  N N 276 
HIS   O      O  N N 277 
HIS   CB     C  N N 278 
HIS   CG     C  Y N 279 
HIS   ND1    N  Y N 280 
HIS   CD2    C  Y N 281 
HIS   CE1    C  Y N 282 
HIS   NE2    N  Y N 283 
HIS   OXT    O  N N 284 
HIS   H      H  N N 285 
HIS   H2     H  N N 286 
HIS   HA     H  N N 287 
HIS   HB2    H  N N 288 
HIS   HB3    H  N N 289 
HIS   HD1    H  N N 290 
HIS   HD2    H  N N 291 
HIS   HE1    H  N N 292 
HIS   HE2    H  N N 293 
HIS   HXT    H  N N 294 
HOH   O      O  N N 295 
HOH   H1     H  N N 296 
HOH   H2     H  N N 297 
ILE   N      N  N N 298 
ILE   CA     C  N S 299 
ILE   C      C  N N 300 
ILE   O      O  N N 301 
ILE   CB     C  N S 302 
ILE   CG1    C  N N 303 
ILE   CG2    C  N N 304 
ILE   CD1    C  N N 305 
ILE   OXT    O  N N 306 
ILE   H      H  N N 307 
ILE   H2     H  N N 308 
ILE   HA     H  N N 309 
ILE   HB     H  N N 310 
ILE   HG12   H  N N 311 
ILE   HG13   H  N N 312 
ILE   HG21   H  N N 313 
ILE   HG22   H  N N 314 
ILE   HG23   H  N N 315 
ILE   HD11   H  N N 316 
ILE   HD12   H  N N 317 
ILE   HD13   H  N N 318 
ILE   HXT    H  N N 319 
LEU   N      N  N N 320 
LEU   CA     C  N S 321 
LEU   C      C  N N 322 
LEU   O      O  N N 323 
LEU   CB     C  N N 324 
LEU   CG     C  N N 325 
LEU   CD1    C  N N 326 
LEU   CD2    C  N N 327 
LEU   OXT    O  N N 328 
LEU   H      H  N N 329 
LEU   H2     H  N N 330 
LEU   HA     H  N N 331 
LEU   HB2    H  N N 332 
LEU   HB3    H  N N 333 
LEU   HG     H  N N 334 
LEU   HD11   H  N N 335 
LEU   HD12   H  N N 336 
LEU   HD13   H  N N 337 
LEU   HD21   H  N N 338 
LEU   HD22   H  N N 339 
LEU   HD23   H  N N 340 
LEU   HXT    H  N N 341 
LYS   N      N  N N 342 
LYS   CA     C  N S 343 
LYS   C      C  N N 344 
LYS   O      O  N N 345 
LYS   CB     C  N N 346 
LYS   CG     C  N N 347 
LYS   CD     C  N N 348 
LYS   CE     C  N N 349 
LYS   NZ     N  N N 350 
LYS   OXT    O  N N 351 
LYS   H      H  N N 352 
LYS   H2     H  N N 353 
LYS   HA     H  N N 354 
LYS   HB2    H  N N 355 
LYS   HB3    H  N N 356 
LYS   HG2    H  N N 357 
LYS   HG3    H  N N 358 
LYS   HD2    H  N N 359 
LYS   HD3    H  N N 360 
LYS   HE2    H  N N 361 
LYS   HE3    H  N N 362 
LYS   HZ1    H  N N 363 
LYS   HZ2    H  N N 364 
LYS   HZ3    H  N N 365 
LYS   HXT    H  N N 366 
MET   N      N  N N 367 
MET   CA     C  N S 368 
MET   C      C  N N 369 
MET   O      O  N N 370 
MET   CB     C  N N 371 
MET   CG     C  N N 372 
MET   SD     S  N N 373 
MET   CE     C  N N 374 
MET   OXT    O  N N 375 
MET   H      H  N N 376 
MET   H2     H  N N 377 
MET   HA     H  N N 378 
MET   HB2    H  N N 379 
MET   HB3    H  N N 380 
MET   HG2    H  N N 381 
MET   HG3    H  N N 382 
MET   HE1    H  N N 383 
MET   HE2    H  N N 384 
MET   HE3    H  N N 385 
MET   HXT    H  N N 386 
MG    MG     MG N N 387 
PHE   N      N  N N 388 
PHE   CA     C  N S 389 
PHE   C      C  N N 390 
PHE   O      O  N N 391 
PHE   CB     C  N N 392 
PHE   CG     C  Y N 393 
PHE   CD1    C  Y N 394 
PHE   CD2    C  Y N 395 
PHE   CE1    C  Y N 396 
PHE   CE2    C  Y N 397 
PHE   CZ     C  Y N 398 
PHE   OXT    O  N N 399 
PHE   H      H  N N 400 
PHE   H2     H  N N 401 
PHE   HA     H  N N 402 
PHE   HB2    H  N N 403 
PHE   HB3    H  N N 404 
PHE   HD1    H  N N 405 
PHE   HD2    H  N N 406 
PHE   HE1    H  N N 407 
PHE   HE2    H  N N 408 
PHE   HZ     H  N N 409 
PHE   HXT    H  N N 410 
PRO   N      N  N N 411 
PRO   CA     C  N S 412 
PRO   C      C  N N 413 
PRO   O      O  N N 414 
PRO   CB     C  N N 415 
PRO   CG     C  N N 416 
PRO   CD     C  N N 417 
PRO   OXT    O  N N 418 
PRO   H      H  N N 419 
PRO   HA     H  N N 420 
PRO   HB2    H  N N 421 
PRO   HB3    H  N N 422 
PRO   HG2    H  N N 423 
PRO   HG3    H  N N 424 
PRO   HD2    H  N N 425 
PRO   HD3    H  N N 426 
PRO   HXT    H  N N 427 
SER   N      N  N N 428 
SER   CA     C  N S 429 
SER   C      C  N N 430 
SER   O      O  N N 431 
SER   CB     C  N N 432 
SER   OG     O  N N 433 
SER   OXT    O  N N 434 
SER   H      H  N N 435 
SER   H2     H  N N 436 
SER   HA     H  N N 437 
SER   HB2    H  N N 438 
SER   HB3    H  N N 439 
SER   HG     H  N N 440 
SER   HXT    H  N N 441 
THR   N      N  N N 442 
THR   CA     C  N S 443 
THR   C      C  N N 444 
THR   O      O  N N 445 
THR   CB     C  N R 446 
THR   OG1    O  N N 447 
THR   CG2    C  N N 448 
THR   OXT    O  N N 449 
THR   H      H  N N 450 
THR   H2     H  N N 451 
THR   HA     H  N N 452 
THR   HB     H  N N 453 
THR   HG1    H  N N 454 
THR   HG21   H  N N 455 
THR   HG22   H  N N 456 
THR   HG23   H  N N 457 
THR   HXT    H  N N 458 
TRP   N      N  N N 459 
TRP   CA     C  N S 460 
TRP   C      C  N N 461 
TRP   O      O  N N 462 
TRP   CB     C  N N 463 
TRP   CG     C  Y N 464 
TRP   CD1    C  Y N 465 
TRP   CD2    C  Y N 466 
TRP   NE1    N  Y N 467 
TRP   CE2    C  Y N 468 
TRP   CE3    C  Y N 469 
TRP   CZ2    C  Y N 470 
TRP   CZ3    C  Y N 471 
TRP   CH2    C  Y N 472 
TRP   OXT    O  N N 473 
TRP   H      H  N N 474 
TRP   H2     H  N N 475 
TRP   HA     H  N N 476 
TRP   HB2    H  N N 477 
TRP   HB3    H  N N 478 
TRP   HD1    H  N N 479 
TRP   HE1    H  N N 480 
TRP   HE3    H  N N 481 
TRP   HZ2    H  N N 482 
TRP   HZ3    H  N N 483 
TRP   HH2    H  N N 484 
TRP   HXT    H  N N 485 
TYR   N      N  N N 486 
TYR   CA     C  N S 487 
TYR   C      C  N N 488 
TYR   O      O  N N 489 
TYR   CB     C  N N 490 
TYR   CG     C  Y N 491 
TYR   CD1    C  Y N 492 
TYR   CD2    C  Y N 493 
TYR   CE1    C  Y N 494 
TYR   CE2    C  Y N 495 
TYR   CZ     C  Y N 496 
TYR   OH     O  N N 497 
TYR   OXT    O  N N 498 
TYR   H      H  N N 499 
TYR   H2     H  N N 500 
TYR   HA     H  N N 501 
TYR   HB2    H  N N 502 
TYR   HB3    H  N N 503 
TYR   HD1    H  N N 504 
TYR   HD2    H  N N 505 
TYR   HE1    H  N N 506 
TYR   HE2    H  N N 507 
TYR   HH     H  N N 508 
TYR   HXT    H  N N 509 
VAL   N      N  N N 510 
VAL   CA     C  N S 511 
VAL   C      C  N N 512 
VAL   O      O  N N 513 
VAL   CB     C  N N 514 
VAL   CG1    C  N N 515 
VAL   CG2    C  N N 516 
VAL   OXT    O  N N 517 
VAL   H      H  N N 518 
VAL   H2     H  N N 519 
VAL   HA     H  N N 520 
VAL   HB     H  N N 521 
VAL   HG11   H  N N 522 
VAL   HG12   H  N N 523 
VAL   HG13   H  N N 524 
VAL   HG21   H  N N 525 
VAL   HG22   H  N N 526 
VAL   HG23   H  N N 527 
VAL   HXT    H  N N 528 
# 
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 
A1A3L N4    C4     sing N N 1   
A1A3L C4    N3     doub N N 2   
A1A3L C4    C5     sing N N 3   
A1A3L N3    C2     sing N N 4   
A1A3L C5    C6     doub N N 5   
A1A3L C2    O2     doub N N 6   
A1A3L C2    N1     sing N N 7   
A1A3L C6    N1     sing N N 8   
A1A3L N1    "C1'"  sing N N 9   
A1A3L O2B   PB     doub N N 10  
A1A3L O1B   PB     sing N N 11  
A1A3L O1A   PA     doub N N 12  
A1A3L PB    O3B    sing N N 13  
A1A3L PB    O3A    sing N N 14  
A1A3L "C1'" "C2'"  sing N N 15  
A1A3L "C1'" "O4'"  sing N N 16  
A1A3L "C2'" "C3'"  sing N N 17  
A1A3L PA    O2A    sing N N 18  
A1A3L PA    O3A    sing N N 19  
A1A3L PA    "O5'"  sing N N 20  
A1A3L "C5'" "O5'"  sing N N 21  
A1A3L "C5'" "C4'"  sing N N 22  
A1A3L "O4'" "C4'"  sing N N 23  
A1A3L O01   "C3'"  sing N N 24  
A1A3L "C3'" "C4'"  sing N N 25  
A1A3L "C3'" N01    sing N N 26  
A1A3L C5    H1     sing N N 27  
A1A3L C6    H2     sing N N 28  
A1A3L "C1'" H3     sing N N 29  
A1A3L "C2'" H4     sing N N 30  
A1A3L "C2'" H5     sing N N 31  
A1A3L "C4'" H6     sing N N 32  
A1A3L "C5'" H7     sing N N 33  
A1A3L "C5'" H8     sing N N 34  
A1A3L N01   H9     sing N N 35  
A1A3L N01   H10    sing N N 36  
A1A3L N4    H12    sing N N 37  
A1A3L N4    H13    sing N N 38  
A1A3L O01   H14    sing N N 39  
A1A3L O1B   H15    sing N N 40  
A1A3L O2A   H16    sing N N 41  
A1A3L O3B   H17    sing N N 42  
ALA   N     CA     sing N N 43  
ALA   N     H      sing N N 44  
ALA   N     H2     sing N N 45  
ALA   CA    C      sing N N 46  
ALA   CA    CB     sing N N 47  
ALA   CA    HA     sing N N 48  
ALA   C     O      doub N N 49  
ALA   C     OXT    sing N N 50  
ALA   CB    HB1    sing N N 51  
ALA   CB    HB2    sing N N 52  
ALA   CB    HB3    sing N N 53  
ALA   OXT   HXT    sing N N 54  
ARG   N     CA     sing N N 55  
ARG   N     H      sing N N 56  
ARG   N     H2     sing N N 57  
ARG   CA    C      sing N N 58  
ARG   CA    CB     sing N N 59  
ARG   CA    HA     sing N N 60  
ARG   C     O      doub N N 61  
ARG   C     OXT    sing N N 62  
ARG   CB    CG     sing N N 63  
ARG   CB    HB2    sing N N 64  
ARG   CB    HB3    sing N N 65  
ARG   CG    CD     sing N N 66  
ARG   CG    HG2    sing N N 67  
ARG   CG    HG3    sing N N 68  
ARG   CD    NE     sing N N 69  
ARG   CD    HD2    sing N N 70  
ARG   CD    HD3    sing N N 71  
ARG   NE    CZ     sing N N 72  
ARG   NE    HE     sing N N 73  
ARG   CZ    NH1    sing N N 74  
ARG   CZ    NH2    doub N N 75  
ARG   NH1   HH11   sing N N 76  
ARG   NH1   HH12   sing N N 77  
ARG   NH2   HH21   sing N N 78  
ARG   NH2   HH22   sing N N 79  
ARG   OXT   HXT    sing N N 80  
ASN   N     CA     sing N N 81  
ASN   N     H      sing N N 82  
ASN   N     H2     sing N N 83  
ASN   CA    C      sing N N 84  
ASN   CA    CB     sing N N 85  
ASN   CA    HA     sing N N 86  
ASN   C     O      doub N N 87  
ASN   C     OXT    sing N N 88  
ASN   CB    CG     sing N N 89  
ASN   CB    HB2    sing N N 90  
ASN   CB    HB3    sing N N 91  
ASN   CG    OD1    doub N N 92  
ASN   CG    ND2    sing N N 93  
ASN   ND2   HD21   sing N N 94  
ASN   ND2   HD22   sing N N 95  
ASN   OXT   HXT    sing N N 96  
ASP   N     CA     sing N N 97  
ASP   N     H      sing N N 98  
ASP   N     H2     sing N N 99  
ASP   CA    C      sing N N 100 
ASP   CA    CB     sing N N 101 
ASP   CA    HA     sing N N 102 
ASP   C     O      doub N N 103 
ASP   C     OXT    sing N N 104 
ASP   CB    CG     sing N N 105 
ASP   CB    HB2    sing N N 106 
ASP   CB    HB3    sing N N 107 
ASP   CG    OD1    doub N N 108 
ASP   CG    OD2    sing N N 109 
ASP   OD2   HD2    sing N N 110 
ASP   OXT   HXT    sing N N 111 
ATP   PG    O1G    doub N N 112 
ATP   PG    O2G    sing N N 113 
ATP   PG    O3G    sing N N 114 
ATP   PG    O3B    sing N N 115 
ATP   O2G   HOG2   sing N N 116 
ATP   O3G   HOG3   sing N N 117 
ATP   PB    O1B    doub N N 118 
ATP   PB    O2B    sing N N 119 
ATP   PB    O3B    sing N N 120 
ATP   PB    O3A    sing N N 121 
ATP   O2B   HOB2   sing N N 122 
ATP   PA    O1A    doub N N 123 
ATP   PA    O2A    sing N N 124 
ATP   PA    O3A    sing N N 125 
ATP   PA    "O5'"  sing N N 126 
ATP   O2A   HOA2   sing N N 127 
ATP   "O5'" "C5'"  sing N N 128 
ATP   "C5'" "C4'"  sing N N 129 
ATP   "C5'" "H5'1" sing N N 130 
ATP   "C5'" "H5'2" sing N N 131 
ATP   "C4'" "O4'"  sing N N 132 
ATP   "C4'" "C3'"  sing N N 133 
ATP   "C4'" "H4'"  sing N N 134 
ATP   "O4'" "C1'"  sing N N 135 
ATP   "C3'" "O3'"  sing N N 136 
ATP   "C3'" "C2'"  sing N N 137 
ATP   "C3'" "H3'"  sing N N 138 
ATP   "O3'" "HO3'" sing N N 139 
ATP   "C2'" "O2'"  sing N N 140 
ATP   "C2'" "C1'"  sing N N 141 
ATP   "C2'" "H2'"  sing N N 142 
ATP   "O2'" "HO2'" sing N N 143 
ATP   "C1'" N9     sing N N 144 
ATP   "C1'" "H1'"  sing N N 145 
ATP   N9    C8     sing Y N 146 
ATP   N9    C4     sing Y N 147 
ATP   C8    N7     doub Y N 148 
ATP   C8    H8     sing N N 149 
ATP   N7    C5     sing Y N 150 
ATP   C5    C6     sing Y N 151 
ATP   C5    C4     doub Y N 152 
ATP   C6    N6     sing N N 153 
ATP   C6    N1     doub Y N 154 
ATP   N6    HN61   sing N N 155 
ATP   N6    HN62   sing N N 156 
ATP   N1    C2     sing Y N 157 
ATP   C2    N3     doub Y N 158 
ATP   C2    H2     sing N N 159 
ATP   N3    C4     sing Y N 160 
CYS   N     CA     sing N N 161 
CYS   N     H      sing N N 162 
CYS   N     H2     sing N N 163 
CYS   CA    C      sing N N 164 
CYS   CA    CB     sing N N 165 
CYS   CA    HA     sing N N 166 
CYS   C     O      doub N N 167 
CYS   C     OXT    sing N N 168 
CYS   CB    SG     sing N N 169 
CYS   CB    HB2    sing N N 170 
CYS   CB    HB3    sing N N 171 
CYS   SG    HG     sing N N 172 
CYS   OXT   HXT    sing N N 173 
DTP   PG    O1G    doub N N 174 
DTP   PG    O2G    sing N N 175 
DTP   PG    O3G    sing N N 176 
DTP   PG    O3B    sing N N 177 
DTP   O2G   HOG2   sing N N 178 
DTP   O3G   HOG3   sing N N 179 
DTP   PB    O1B    doub N N 180 
DTP   PB    O2B    sing N N 181 
DTP   PB    O3B    sing N N 182 
DTP   PB    O3A    sing N N 183 
DTP   O2B   HOB2   sing N N 184 
DTP   PA    O1A    doub N N 185 
DTP   PA    O2A    sing N N 186 
DTP   PA    O3A    sing N N 187 
DTP   PA    "O5'"  sing N N 188 
DTP   O2A   HOA2   sing N N 189 
DTP   "O5'" "C5'"  sing N N 190 
DTP   "C5'" "C4'"  sing N N 191 
DTP   "C5'" "H5'1" sing N N 192 
DTP   "C5'" "H5'2" sing N N 193 
DTP   "C4'" "O4'"  sing N N 194 
DTP   "C4'" "C3'"  sing N N 195 
DTP   "C4'" "H4'"  sing N N 196 
DTP   "O4'" "C1'"  sing N N 197 
DTP   "C3'" "O3'"  sing N N 198 
DTP   "C3'" "C2'"  sing N N 199 
DTP   "C3'" "H3'"  sing N N 200 
DTP   "O3'" "HO3'" sing N N 201 
DTP   "C2'" "C1'"  sing N N 202 
DTP   "C2'" "H2'1" sing N N 203 
DTP   "C2'" "H2'2" sing N N 204 
DTP   "C1'" N9     sing N N 205 
DTP   "C1'" "H1'"  sing N N 206 
DTP   N9    C8     sing Y N 207 
DTP   N9    C4     sing Y N 208 
DTP   C8    N7     doub Y N 209 
DTP   C8    H8     sing N N 210 
DTP   N7    C5     sing Y N 211 
DTP   C5    C6     sing Y N 212 
DTP   C5    C4     doub Y N 213 
DTP   C6    N6     sing N N 214 
DTP   C6    N1     doub Y N 215 
DTP   N6    HN61   sing N N 216 
DTP   N6    HN62   sing N N 217 
DTP   N1    C2     sing Y N 218 
DTP   C2    N3     doub Y N 219 
DTP   C2    H2     sing N N 220 
DTP   N3    C4     sing Y N 221 
FEO   FE1   O      sing N N 222 
FEO   FE2   O      sing N N 223 
GLN   N     CA     sing N N 224 
GLN   N     H      sing N N 225 
GLN   N     H2     sing N N 226 
GLN   CA    C      sing N N 227 
GLN   CA    CB     sing N N 228 
GLN   CA    HA     sing N N 229 
GLN   C     O      doub N N 230 
GLN   C     OXT    sing N N 231 
GLN   CB    CG     sing N N 232 
GLN   CB    HB2    sing N N 233 
GLN   CB    HB3    sing N N 234 
GLN   CG    CD     sing N N 235 
GLN   CG    HG2    sing N N 236 
GLN   CG    HG3    sing N N 237 
GLN   CD    OE1    doub N N 238 
GLN   CD    NE2    sing N N 239 
GLN   NE2   HE21   sing N N 240 
GLN   NE2   HE22   sing N N 241 
GLN   OXT   HXT    sing N N 242 
GLU   N     CA     sing N N 243 
GLU   N     H      sing N N 244 
GLU   N     H2     sing N N 245 
GLU   CA    C      sing N N 246 
GLU   CA    CB     sing N N 247 
GLU   CA    HA     sing N N 248 
GLU   C     O      doub N N 249 
GLU   C     OXT    sing N N 250 
GLU   CB    CG     sing N N 251 
GLU   CB    HB2    sing N N 252 
GLU   CB    HB3    sing N N 253 
GLU   CG    CD     sing N N 254 
GLU   CG    HG2    sing N N 255 
GLU   CG    HG3    sing N N 256 
GLU   CD    OE1    doub N N 257 
GLU   CD    OE2    sing N N 258 
GLU   OE2   HE2    sing N N 259 
GLU   OXT   HXT    sing N N 260 
GLY   N     CA     sing N N 261 
GLY   N     H      sing N N 262 
GLY   N     H2     sing N N 263 
GLY   CA    C      sing N N 264 
GLY   CA    HA2    sing N N 265 
GLY   CA    HA3    sing N N 266 
GLY   C     O      doub N N 267 
GLY   C     OXT    sing N N 268 
GLY   OXT   HXT    sing N N 269 
HIS   N     CA     sing N N 270 
HIS   N     H      sing N N 271 
HIS   N     H2     sing N N 272 
HIS   CA    C      sing N N 273 
HIS   CA    CB     sing N N 274 
HIS   CA    HA     sing N N 275 
HIS   C     O      doub N N 276 
HIS   C     OXT    sing N N 277 
HIS   CB    CG     sing N N 278 
HIS   CB    HB2    sing N N 279 
HIS   CB    HB3    sing N N 280 
HIS   CG    ND1    sing Y N 281 
HIS   CG    CD2    doub Y N 282 
HIS   ND1   CE1    doub Y N 283 
HIS   ND1   HD1    sing N N 284 
HIS   CD2   NE2    sing Y N 285 
HIS   CD2   HD2    sing N N 286 
HIS   CE1   NE2    sing Y N 287 
HIS   CE1   HE1    sing N N 288 
HIS   NE2   HE2    sing N N 289 
HIS   OXT   HXT    sing N N 290 
HOH   O     H1     sing N N 291 
HOH   O     H2     sing N N 292 
ILE   N     CA     sing N N 293 
ILE   N     H      sing N N 294 
ILE   N     H2     sing N N 295 
ILE   CA    C      sing N N 296 
ILE   CA    CB     sing N N 297 
ILE   CA    HA     sing N N 298 
ILE   C     O      doub N N 299 
ILE   C     OXT    sing N N 300 
ILE   CB    CG1    sing N N 301 
ILE   CB    CG2    sing N N 302 
ILE   CB    HB     sing N N 303 
ILE   CG1   CD1    sing N N 304 
ILE   CG1   HG12   sing N N 305 
ILE   CG1   HG13   sing N N 306 
ILE   CG2   HG21   sing N N 307 
ILE   CG2   HG22   sing N N 308 
ILE   CG2   HG23   sing N N 309 
ILE   CD1   HD11   sing N N 310 
ILE   CD1   HD12   sing N N 311 
ILE   CD1   HD13   sing N N 312 
ILE   OXT   HXT    sing N N 313 
LEU   N     CA     sing N N 314 
LEU   N     H      sing N N 315 
LEU   N     H2     sing N N 316 
LEU   CA    C      sing N N 317 
LEU   CA    CB     sing N N 318 
LEU   CA    HA     sing N N 319 
LEU   C     O      doub N N 320 
LEU   C     OXT    sing N N 321 
LEU   CB    CG     sing N N 322 
LEU   CB    HB2    sing N N 323 
LEU   CB    HB3    sing N N 324 
LEU   CG    CD1    sing N N 325 
LEU   CG    CD2    sing N N 326 
LEU   CG    HG     sing N N 327 
LEU   CD1   HD11   sing N N 328 
LEU   CD1   HD12   sing N N 329 
LEU   CD1   HD13   sing N N 330 
LEU   CD2   HD21   sing N N 331 
LEU   CD2   HD22   sing N N 332 
LEU   CD2   HD23   sing N N 333 
LEU   OXT   HXT    sing N N 334 
LYS   N     CA     sing N N 335 
LYS   N     H      sing N N 336 
LYS   N     H2     sing N N 337 
LYS   CA    C      sing N N 338 
LYS   CA    CB     sing N N 339 
LYS   CA    HA     sing N N 340 
LYS   C     O      doub N N 341 
LYS   C     OXT    sing N N 342 
LYS   CB    CG     sing N N 343 
LYS   CB    HB2    sing N N 344 
LYS   CB    HB3    sing N N 345 
LYS   CG    CD     sing N N 346 
LYS   CG    HG2    sing N N 347 
LYS   CG    HG3    sing N N 348 
LYS   CD    CE     sing N N 349 
LYS   CD    HD2    sing N N 350 
LYS   CD    HD3    sing N N 351 
LYS   CE    NZ     sing N N 352 
LYS   CE    HE2    sing N N 353 
LYS   CE    HE3    sing N N 354 
LYS   NZ    HZ1    sing N N 355 
LYS   NZ    HZ2    sing N N 356 
LYS   NZ    HZ3    sing N N 357 
LYS   OXT   HXT    sing N N 358 
MET   N     CA     sing N N 359 
MET   N     H      sing N N 360 
MET   N     H2     sing N N 361 
MET   CA    C      sing N N 362 
MET   CA    CB     sing N N 363 
MET   CA    HA     sing N N 364 
MET   C     O      doub N N 365 
MET   C     OXT    sing N N 366 
MET   CB    CG     sing N N 367 
MET   CB    HB2    sing N N 368 
MET   CB    HB3    sing N N 369 
MET   CG    SD     sing N N 370 
MET   CG    HG2    sing N N 371 
MET   CG    HG3    sing N N 372 
MET   SD    CE     sing N N 373 
MET   CE    HE1    sing N N 374 
MET   CE    HE2    sing N N 375 
MET   CE    HE3    sing N N 376 
MET   OXT   HXT    sing N N 377 
PHE   N     CA     sing N N 378 
PHE   N     H      sing N N 379 
PHE   N     H2     sing N N 380 
PHE   CA    C      sing N N 381 
PHE   CA    CB     sing N N 382 
PHE   CA    HA     sing N N 383 
PHE   C     O      doub N N 384 
PHE   C     OXT    sing N N 385 
PHE   CB    CG     sing N N 386 
PHE   CB    HB2    sing N N 387 
PHE   CB    HB3    sing N N 388 
PHE   CG    CD1    doub Y N 389 
PHE   CG    CD2    sing Y N 390 
PHE   CD1   CE1    sing Y N 391 
PHE   CD1   HD1    sing N N 392 
PHE   CD2   CE2    doub Y N 393 
PHE   CD2   HD2    sing N N 394 
PHE   CE1   CZ     doub Y N 395 
PHE   CE1   HE1    sing N N 396 
PHE   CE2   CZ     sing Y N 397 
PHE   CE2   HE2    sing N N 398 
PHE   CZ    HZ     sing N N 399 
PHE   OXT   HXT    sing N N 400 
PRO   N     CA     sing N N 401 
PRO   N     CD     sing N N 402 
PRO   N     H      sing N N 403 
PRO   CA    C      sing N N 404 
PRO   CA    CB     sing N N 405 
PRO   CA    HA     sing N N 406 
PRO   C     O      doub N N 407 
PRO   C     OXT    sing N N 408 
PRO   CB    CG     sing N N 409 
PRO   CB    HB2    sing N N 410 
PRO   CB    HB3    sing N N 411 
PRO   CG    CD     sing N N 412 
PRO   CG    HG2    sing N N 413 
PRO   CG    HG3    sing N N 414 
PRO   CD    HD2    sing N N 415 
PRO   CD    HD3    sing N N 416 
PRO   OXT   HXT    sing N N 417 
SER   N     CA     sing N N 418 
SER   N     H      sing N N 419 
SER   N     H2     sing N N 420 
SER   CA    C      sing N N 421 
SER   CA    CB     sing N N 422 
SER   CA    HA     sing N N 423 
SER   C     O      doub N N 424 
SER   C     OXT    sing N N 425 
SER   CB    OG     sing N N 426 
SER   CB    HB2    sing N N 427 
SER   CB    HB3    sing N N 428 
SER   OG    HG     sing N N 429 
SER   OXT   HXT    sing N N 430 
THR   N     CA     sing N N 431 
THR   N     H      sing N N 432 
THR   N     H2     sing N N 433 
THR   CA    C      sing N N 434 
THR   CA    CB     sing N N 435 
THR   CA    HA     sing N N 436 
THR   C     O      doub N N 437 
THR   C     OXT    sing N N 438 
THR   CB    OG1    sing N N 439 
THR   CB    CG2    sing N N 440 
THR   CB    HB     sing N N 441 
THR   OG1   HG1    sing N N 442 
THR   CG2   HG21   sing N N 443 
THR   CG2   HG22   sing N N 444 
THR   CG2   HG23   sing N N 445 
THR   OXT   HXT    sing N N 446 
TRP   N     CA     sing N N 447 
TRP   N     H      sing N N 448 
TRP   N     H2     sing N N 449 
TRP   CA    C      sing N N 450 
TRP   CA    CB     sing N N 451 
TRP   CA    HA     sing N N 452 
TRP   C     O      doub N N 453 
TRP   C     OXT    sing N N 454 
TRP   CB    CG     sing N N 455 
TRP   CB    HB2    sing N N 456 
TRP   CB    HB3    sing N N 457 
TRP   CG    CD1    doub Y N 458 
TRP   CG    CD2    sing Y N 459 
TRP   CD1   NE1    sing Y N 460 
TRP   CD1   HD1    sing N N 461 
TRP   CD2   CE2    doub Y N 462 
TRP   CD2   CE3    sing Y N 463 
TRP   NE1   CE2    sing Y N 464 
TRP   NE1   HE1    sing N N 465 
TRP   CE2   CZ2    sing Y N 466 
TRP   CE3   CZ3    doub Y N 467 
TRP   CE3   HE3    sing N N 468 
TRP   CZ2   CH2    doub Y N 469 
TRP   CZ2   HZ2    sing N N 470 
TRP   CZ3   CH2    sing Y N 471 
TRP   CZ3   HZ3    sing N N 472 
TRP   CH2   HH2    sing N N 473 
TRP   OXT   HXT    sing N N 474 
TYR   N     CA     sing N N 475 
TYR   N     H      sing N N 476 
TYR   N     H2     sing N N 477 
TYR   CA    C      sing N N 478 
TYR   CA    CB     sing N N 479 
TYR   CA    HA     sing N N 480 
TYR   C     O      doub N N 481 
TYR   C     OXT    sing N N 482 
TYR   CB    CG     sing N N 483 
TYR   CB    HB2    sing N N 484 
TYR   CB    HB3    sing N N 485 
TYR   CG    CD1    doub Y N 486 
TYR   CG    CD2    sing Y N 487 
TYR   CD1   CE1    sing Y N 488 
TYR   CD1   HD1    sing N N 489 
TYR   CD2   CE2    doub Y N 490 
TYR   CD2   HD2    sing N N 491 
TYR   CE1   CZ     doub Y N 492 
TYR   CE1   HE1    sing N N 493 
TYR   CE2   CZ     sing Y N 494 
TYR   CE2   HE2    sing N N 495 
TYR   CZ    OH     sing N N 496 
TYR   OH    HH     sing N N 497 
TYR   OXT   HXT    sing N N 498 
VAL   N     CA     sing N N 499 
VAL   N     H      sing N N 500 
VAL   N     H2     sing N N 501 
VAL   CA    C      sing N N 502 
VAL   CA    CB     sing N N 503 
VAL   CA    HA     sing N N 504 
VAL   C     O      doub N N 505 
VAL   C     OXT    sing N N 506 
VAL   CB    CG1    sing N N 507 
VAL   CB    CG2    sing N N 508 
VAL   CB    HB     sing N N 509 
VAL   CG1   HG11   sing N N 510 
VAL   CG1   HG12   sing N N 511 
VAL   CG1   HG13   sing N N 512 
VAL   CG2   HG21   sing N N 513 
VAL   CG2   HG22   sing N N 514 
VAL   CG2   HG23   sing N N 515 
VAL   OXT   HXT    sing N N 516 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-08-23 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9DB2 
_em_admin.last_update        2024-11-27 
_em_admin.map_release_date   2024-11-06 
_em_admin.title              'Class Ia ribonucleotide reductase with mechanism-based inhibitor N3CDP' 
# 
_em_ctf_correction.details                  
;CTF correction using RELION's implementation of CTFFIND
;
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     NONE 
# 
_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                0.26069 
# 
_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          562 
_em_entity_assembly_naturalsource.organism             'Escherichia coli' 
_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         50.946 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K2 SUMMIT (4k 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                    ? 
_em_image_recording.num_real_images                     ? 
# 
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 
'MODEL REFINEMENT'              ? 1  ? ? ? PHENIX 1.20.1_4487: 
'IMAGE ACQUISITION'             ? 2  1 1 1 ?      ?            
'PARTICLE SELECTION'            ? 3  1 1 1 ?      ?            
'VOLUME SELECTION'              ? 4  1 1 1 ?      ?            
CLASSIFICATION                  ? 5  1 1 1 ?      ?            
MASKING                         ? 6  1 1 1 ?      ?            
RECONSTRUCTION                  ? 7  1 1 1 ?      ?            
'INITIAL EULER ASSIGNMENT'      ? 8  1 1 1 ?      ?            
'FINAL EULER ASSIGNMENT'        ? 9  1 1 1 ?      ?            
'CTF CORRECTION'                ? 10 1 1 1 ?      ?            
'LAYERLINE INDEXING'            ? 11 1 1 1 ?      ?            
'DIFFRACTION INDEXING'          ? 12 1 1 1 ?      ?            
'MODEL FITTING'                 ? 13 1 1 1 ?      ?            
'SERIES ALIGNMENT'              ? 14 1 1 1 ?      ?            
'MOLECULAR REPLACEMENT'         ? 15 1 1 1 ?      ?            
'LATTICE DISTORTION CORRECTION' ? 16 1 1 1 ?      ?            
'SYMMETRY DETERMINATION'        ? 17 1 1 1 ?      ?            
'CRYSTALLOGRAPHY MERGING'       ? 18 1 1 1 ?      ?            
OTHER                           ? 19 1 1 1 ?      ?            
# 
_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 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' 1R35GM126982-01 1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' GM047274        2 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' GM29595         3 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' 1F32GM145072-01 4 
# 
_atom_sites.entry_id                    9DB2 
_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  
FE 
MG 
N  
O  
P  
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     . VAL   A 1 7   ? 147.134 171.328 113.036 1.00 69.68  ?  7    VAL   A N     1 
ATOM   2     C  CA    . VAL   A 1 7   ? 147.036 170.060 113.746 1.00 67.24  ?  7    VAL   A CA    1 
ATOM   3     C  C     . VAL   A 1 7   ? 146.599 170.324 115.180 1.00 68.95  ?  7    VAL   A C     1 
ATOM   4     O  O     . VAL   A 1 7   ? 146.849 171.394 115.730 1.00 71.33  ?  7    VAL   A O     1 
ATOM   5     C  CB    . VAL   A 1 7   ? 148.378 169.280 113.753 1.00 63.97  ?  7    VAL   A CB    1 
ATOM   6     C  CG1   . VAL   A 1 7   ? 148.868 169.028 112.333 1.00 62.51  ?  7    VAL   A CG1   1 
ATOM   7     C  CG2   . VAL   A 1 7   ? 149.429 170.028 114.552 1.00 64.74  ?  7    VAL   A CG2   1 
ATOM   8     N  N     . THR   A 1 8   ? 145.923 169.352 115.774 1.00 67.99  ?  8    THR   A N     1 
ATOM   9     C  CA    . THR   A 1 8   ? 145.513 169.454 117.162 1.00 69.46  ?  8    THR   A CA    1 
ATOM   10    C  C     . THR   A 1 8   ? 146.438 168.655 118.063 1.00 66.87  ?  8    THR   A C     1 
ATOM   11    O  O     . THR   A 1 8   ? 146.556 167.446 117.912 1.00 64.10  ?  8    THR   A O     1 
ATOM   12    C  CB    . THR   A 1 8   ? 144.089 168.941 117.366 1.00 70.62  ?  8    THR   A CB    1 
ATOM   13    O  OG1   . THR   A 1 8   ? 143.240 169.457 116.338 1.00 72.64  ?  8    THR   A OG1   1 
ATOM   14    C  CG2   . THR   A 1 8   ? 143.564 169.349 118.733 1.00 73.15  ?  8    THR   A CG2   1 
ATOM   15    N  N     . LYS   A 1 9   ? 147.066 169.325 119.022 1.00 69.98  ?  9    LYS   A N     1 
ATOM   16    C  CA    . LYS   A 1 9   ? 147.958 168.656 119.962 1.00 65.99  ?  9    LYS   A CA    1 
ATOM   17    C  C     . LYS   A 1 9   ? 147.125 167.896 120.988 1.00 66.01  ?  9    LYS   A C     1 
ATOM   18    O  O     . LYS   A 1 9   ? 145.901 167.980 120.980 1.00 67.87  ?  9    LYS   A O     1 
ATOM   19    C  CB    . LYS   A 1 9   ? 148.878 169.662 120.654 1.00 67.62  ?  9    LYS   A CB    1 
ATOM   20    C  CG    . LYS   A 1 9   ? 149.547 170.647 119.708 1.00 68.60  ?  9    LYS   A CG    1 
ATOM   21    C  CD    . LYS   A 1 9   ? 150.679 170.011 118.937 1.00 65.56  ?  9    LYS   A CD    1 
ATOM   22    C  CE    . LYS   A 1 9   ? 151.976 170.120 119.701 1.00 65.17  ?  9    LYS   A CE    1 
ATOM   23    N  NZ    . LYS   A 1 9   ? 153.072 169.424 118.986 1.00 62.41  1  9    LYS   A NZ    1 
ATOM   24    N  N     . ARG   A 1 10  ? 147.783 167.122 121.844 1.00 67.87  ?  10   ARG   A N     1 
ATOM   25    C  CA    . ARG   A 1 10  ? 147.086 166.303 122.837 1.00 63.92  ?  10   ARG   A CA    1 
ATOM   26    C  C     . ARG   A 1 10  ? 146.297 167.127 123.853 1.00 67.46  ?  10   ARG   A C     1 
ATOM   27    O  O     . ARG   A 1 10  ? 145.245 166.694 124.312 1.00 68.43  ?  10   ARG   A O     1 
ATOM   28    C  CB    . ARG   A 1 10  ? 148.080 165.401 123.565 1.00 61.34  ?  10   ARG   A CB    1 
ATOM   29    C  CG    . ARG   A 1 10  ? 148.715 164.354 122.673 1.00 61.07  ?  10   ARG   A CG    1 
ATOM   30    C  CD    . ARG   A 1 10  ? 149.636 163.440 123.455 1.00 62.91  ?  10   ARG   A CD    1 
ATOM   31    N  NE    . ARG   A 1 10  ? 150.267 162.445 122.598 1.00 67.19  ?  10   ARG   A NE    1 
ATOM   32    C  CZ    . ARG   A 1 10  ? 149.693 161.304 122.235 1.00 64.35  ?  10   ARG   A CZ    1 
ATOM   33    N  NH1   . ARG   A 1 10  ? 148.469 161.010 122.660 1.00 63.22  1  10   ARG   A NH1   1 
ATOM   34    N  NH2   . ARG   A 1 10  ? 150.342 160.454 121.451 1.00 60.07  ?  10   ARG   A NH2   1 
ATOM   35    N  N     . ASP   A 1 11  ? 146.827 168.288 124.231 1.00 71.62  ?  11   ASP   A N     1 
ATOM   36    C  CA    . ASP   A 1 11  ? 146.153 169.182 125.181 1.00 75.66  ?  11   ASP   A CA    1 
ATOM   37    C  C     . ASP   A 1 11  ? 144.947 169.918 124.584 1.00 78.69  ?  11   ASP   A C     1 
ATOM   38    O  O     . ASP   A 1 11  ? 144.167 170.526 125.306 1.00 84.77  ?  11   ASP   A O     1 
ATOM   39    C  CB    . ASP   A 1 11  ? 147.137 170.206 125.748 1.00 76.39  ?  11   ASP   A CB    1 
ATOM   40    C  CG    . ASP   A 1 11  ? 147.739 171.094 124.684 1.00 84.42  ?  11   ASP   A CG    1 
ATOM   41    O  OD1   . ASP   A 1 11  ? 147.457 170.877 123.488 1.00 90.51  ?  11   ASP   A OD1   1 
ATOM   42    O  OD2   . ASP   A 1 11  ? 148.499 172.012 125.047 1.00 87.90  -1 11   ASP   A OD2   1 
ATOM   43    N  N     . GLY   A 1 12  ? 144.813 169.870 123.266 1.00 75.48  ?  12   GLY   A N     1 
ATOM   44    C  CA    . GLY   A 1 12  ? 143.737 170.561 122.586 1.00 78.38  ?  12   GLY   A CA    1 
ATOM   45    C  C     . GLY   A 1 12  ? 144.194 171.846 121.932 1.00 80.32  ?  12   GLY   A C     1 
ATOM   46    O  O     . GLY   A 1 12  ? 143.434 172.499 121.230 1.00 82.73  ?  12   GLY   A O     1 
ATOM   47    N  N     . SER   A 1 13  ? 145.458 172.190 122.131 1.00 79.37  ?  13   SER   A N     1 
ATOM   48    C  CA    . SER   A 1 13  ? 146.045 173.326 121.443 1.00 80.94  ?  13   SER   A CA    1 
ATOM   49    C  C     . SER   A 1 13  ? 146.142 173.014 119.953 1.00 78.84  ?  13   SER   A C     1 
ATOM   50    O  O     . SER   A 1 13  ? 146.005 171.869 119.541 1.00 75.83  ?  13   SER   A O     1 
ATOM   51    C  CB    . SER   A 1 13  ? 147.414 173.658 122.033 1.00 80.43  ?  13   SER   A CB    1 
ATOM   52    O  OG    . SER   A 1 13  ? 148.242 174.303 121.084 1.00 82.11  ?  13   SER   A OG    1 
ATOM   53    N  N     . THR   A 1 14  ? 146.338 174.043 119.139 1.00 80.71  ?  14   THR   A N     1 
ATOM   54    C  CA    . THR   A 1 14  ? 146.483 173.850 117.700 1.00 79.03  ?  14   THR   A CA    1 
ATOM   55    C  C     . THR   A 1 14  ? 147.794 174.462 117.251 1.00 78.67  ?  14   THR   A C     1 
ATOM   56    O  O     . THR   A 1 14  ? 148.272 175.431 117.827 1.00 81.10  ?  14   THR   A O     1 
ATOM   57    C  CB    . THR   A 1 14  ? 145.323 174.444 116.904 1.00 81.77  ?  14   THR   A CB    1 
ATOM   58    O  OG1   . THR   A 1 14  ? 145.267 175.864 117.100 1.00 85.87  ?  14   THR   A OG1   1 
ATOM   59    C  CG2   . THR   A 1 14  ? 144.021 173.803 117.355 1.00 82.39  ?  14   THR   A CG2   1 
ATOM   60    N  N     . GLU   A 1 15  ? 148.391 173.860 116.235 1.00 75.78  ?  15   GLU   A N     1 
ATOM   61    C  CA    . GLU   A 1 15  ? 149.695 174.289 115.767 1.00 79.20  ?  15   GLU   A CA    1 
ATOM   62    C  C     . GLU   A 1 15  ? 149.747 174.208 114.261 1.00 77.18  ?  15   GLU   A C     1 
ATOM   63    O  O     . GLU   A 1 15  ? 149.040 173.403 113.662 1.00 77.41  ?  15   GLU   A O     1 
ATOM   64    C  CB    . GLU   A 1 15  ? 150.768 173.386 116.382 1.00 80.76  ?  15   GLU   A CB    1 
ATOM   65    C  CG    . GLU   A 1 15  ? 152.116 174.013 116.647 1.00 87.24  ?  15   GLU   A CG    1 
ATOM   66    C  CD    . GLU   A 1 15  ? 153.027 173.069 117.419 1.00 86.15  ?  15   GLU   A CD    1 
ATOM   67    O  OE1   . GLU   A 1 15  ? 153.655 173.513 118.404 1.00 93.09  ?  15   GLU   A OE1   1 
ATOM   68    O  OE2   . GLU   A 1 15  ? 153.116 171.879 117.041 1.00 75.74  -1 15   GLU   A OE2   1 
ATOM   69    N  N     . ARG   A 1 16  ? 150.600 175.022 113.650 1.00 76.41  ?  16   ARG   A N     1 
ATOM   70    C  CA    . ARG   A 1 16  ? 150.757 174.972 112.208 1.00 78.59  ?  16   ARG   A CA    1 
ATOM   71    C  C     . ARG   A 1 16  ? 151.306 173.591 111.889 1.00 71.55  ?  16   ARG   A C     1 
ATOM   72    O  O     . ARG   A 1 16  ? 152.163 173.086 112.608 1.00 68.73  ?  16   ARG   A O     1 
ATOM   73    C  CB    . ARG   A 1 16  ? 151.696 176.068 111.699 1.00 85.55  ?  16   ARG   A CB    1 
ATOM   74    C  CG    . ARG   A 1 16  ? 151.526 177.418 112.383 1.00 101.59 ?  16   ARG   A CG    1 
ATOM   75    C  CD    . ARG   A 1 16  ? 152.775 178.289 112.231 1.00 110.60 ?  16   ARG   A CD    1 
ATOM   76    N  NE    . ARG   A 1 16  ? 153.939 177.738 112.923 1.00 113.70 ?  16   ARG   A NE    1 
ATOM   77    C  CZ    . ARG   A 1 16  ? 155.121 178.345 113.004 1.00 117.15 ?  16   ARG   A CZ    1 
ATOM   78    N  NH1   . ARG   A 1 16  ? 155.302 179.532 112.440 1.00 122.67 1  16   ARG   A NH1   1 
ATOM   79    N  NH2   . ARG   A 1 16  ? 156.124 177.769 113.655 1.00 112.82 ?  16   ARG   A NH2   1 
ATOM   80    N  N     . ILE   A 1 17  ? 150.796 172.962 110.841 1.00 69.28  ?  17   ILE   A N     1 
ATOM   81    C  CA    . ILE   A 1 17  ? 151.257 171.628 110.506 1.00 66.05  ?  17   ILE   A CA    1 
ATOM   82    C  C     . ILE   A 1 17  ? 152.753 171.673 110.203 1.00 65.60  ?  17   ILE   A C     1 
ATOM   83    O  O     . ILE   A 1 17  ? 153.240 172.571 109.517 1.00 70.34  ?  17   ILE   A O     1 
ATOM   84    C  CB    . ILE   A 1 17  ? 150.471 171.037 109.319 1.00 64.58  ?  17   ILE   A CB    1 
ATOM   85    C  CG1   . ILE   A 1 17  ? 150.848 169.576 109.104 1.00 61.20  ?  17   ILE   A CG1   1 
ATOM   86    C  CG2   . ILE   A 1 17  ? 150.676 171.854 108.055 1.00 66.00  ?  17   ILE   A CG2   1 
ATOM   87    C  CD1   . ILE   A 1 17  ? 149.841 168.831 108.281 1.00 60.55  ?  17   ILE   A CD1   1 
ATOM   88    N  N     . ASN   A 1 18  ? 153.488 170.727 110.767 1.00 65.21  ?  18   ASN   A N     1 
ATOM   89    C  CA    . ASN   A 1 18  ? 154.927 170.696 110.574 1.00 61.29  ?  18   ASN   A CA    1 
ATOM   90    C  C     . ASN   A 1 18  ? 155.383 169.318 110.144 1.00 58.24  ?  18   ASN   A C     1 
ATOM   91    O  O     . ASN   A 1 18  ? 155.577 168.428 110.964 1.00 56.54  ?  18   ASN   A O     1 
ATOM   92    C  CB    . ASN   A 1 18  ? 155.647 171.116 111.847 1.00 62.20  ?  18   ASN   A CB    1 
ATOM   93    C  CG    . ASN   A 1 18  ? 157.083 171.504 111.593 1.00 65.98  ?  18   ASN   A CG    1 
ATOM   94    O  OD1   . ASN   A 1 18  ? 157.686 171.087 110.607 1.00 69.47  ?  18   ASN   A OD1   1 
ATOM   95    N  ND2   . ASN   A 1 18  ? 157.643 172.309 112.486 1.00 67.42  ?  18   ASN   A ND2   1 
ATOM   96    N  N     . LEU   A 1 19  ? 155.551 169.149 108.843 1.00 57.76  ?  19   LEU   A N     1 
ATOM   97    C  CA    . LEU   A 1 19  ? 155.922 167.867 108.277 1.00 55.25  ?  19   LEU   A CA    1 
ATOM   98    C  C     . LEU   A 1 19  ? 157.328 167.456 108.713 1.00 54.28  ?  19   LEU   A C     1 
ATOM   99    O  O     . LEU   A 1 19  ? 157.676 166.280 108.684 1.00 52.24  ?  19   LEU   A O     1 
ATOM   100   C  CB    . LEU   A 1 19  ? 155.805 167.918 106.756 1.00 55.45  ?  19   LEU   A CB    1 
ATOM   101   C  CG    . LEU   A 1 19  ? 154.393 168.271 106.268 1.00 56.57  ?  19   LEU   A CG    1 
ATOM   102   C  CD1   . LEU   A 1 19  ? 154.278 168.175 104.756 1.00 56.63  ?  19   LEU   A CD1   1 
ATOM   103   C  CD2   . LEU   A 1 19  ? 153.346 167.396 106.932 1.00 55.44  ?  19   LEU   A CD2   1 
ATOM   104   N  N     . ASP   A 1 20  ? 158.138 168.430 109.109 1.00 56.02  ?  20   ASP   A N     1 
ATOM   105   C  CA    . ASP   A 1 20  ? 159.476 168.134 109.603 1.00 59.05  ?  20   ASP   A CA    1 
ATOM   106   C  C     . ASP   A 1 20  ? 159.440 167.388 110.933 1.00 58.59  ?  20   ASP   A C     1 
ATOM   107   O  O     . ASP   A 1 20  ? 160.305 166.560 111.206 1.00 65.53  ?  20   ASP   A O     1 
ATOM   108   C  CB    . ASP   A 1 20  ? 160.287 169.416 109.742 1.00 64.31  ?  20   ASP   A CB    1 
ATOM   109   C  CG    . ASP   A 1 20  ? 160.593 170.051 108.405 1.00 73.51  ?  20   ASP   A CG    1 
ATOM   110   O  OD1   . ASP   A 1 20  ? 160.612 169.327 107.386 1.00 76.16  ?  20   ASP   A OD1   1 
ATOM   111   O  OD2   . ASP   A 1 20  ? 160.814 171.276 108.373 1.00 81.44  -1 20   ASP   A OD2   1 
ATOM   112   N  N     . LYS   A 1 21  ? 158.452 167.689 111.766 1.00 54.82  ?  21   LYS   A N     1 
ATOM   113   C  CA    . LYS   A 1 21  ? 158.287 166.977 113.026 1.00 53.68  ?  21   LYS   A CA    1 
ATOM   114   C  C     . LYS   A 1 21  ? 158.003 165.500 112.780 1.00 51.05  ?  21   LYS   A C     1 
ATOM   115   O  O     . LYS   A 1 21  ? 158.545 164.626 113.453 1.00 49.68  ?  21   LYS   A O     1 
ATOM   116   C  CB    . LYS   A 1 21  ? 157.167 167.599 113.849 1.00 55.09  ?  21   LYS   A CB    1 
ATOM   117   C  CG    . LYS   A 1 21  ? 157.519 168.954 114.407 1.00 57.87  ?  21   LYS   A CG    1 
ATOM   118   C  CD    . LYS   A 1 21  ? 156.542 169.394 115.471 1.00 59.29  ?  21   LYS   A CD    1 
ATOM   119   C  CE    . LYS   A 1 21  ? 156.929 170.756 116.023 1.00 62.40  ?  21   LYS   A CE    1 
ATOM   120   N  NZ    . LYS   A 1 21  ? 156.142 171.130 117.228 1.00 66.30  1  21   LYS   A NZ    1 
ATOM   121   N  N     . ILE   A 1 22  ? 157.133 165.230 111.818 1.00 50.58  ?  22   ILE   A N     1 
ATOM   122   C  CA    . ILE   A 1 22  ? 156.803 163.865 111.454 1.00 48.46  ?  22   ILE   A CA    1 
ATOM   123   C  C     . ILE   A 1 22  ? 158.025 163.196 110.853 1.00 47.39  ?  22   ILE   A C     1 
ATOM   124   O  O     . ILE   A 1 22  ? 158.307 162.032 111.110 1.00 46.34  ?  22   ILE   A O     1 
ATOM   125   C  CB    . ILE   A 1 22  ? 155.634 163.822 110.455 1.00 48.65  ?  22   ILE   A CB    1 
ATOM   126   C  CG1   . ILE   A 1 22  ? 154.362 164.360 111.103 1.00 49.91  ?  22   ILE   A CG1   1 
ATOM   127   C  CG2   . ILE   A 1 22  ? 155.396 162.417 109.958 1.00 46.75  ?  22   ILE   A CG2   1 
ATOM   128   C  CD1   . ILE   A 1 22  ? 153.254 164.605 110.118 1.00 50.80  ?  22   ILE   A CD1   1 
ATOM   129   N  N     . HIS   A 1 23  ? 158.763 163.960 110.061 1.00 51.50  ?  23   HIS   A N     1 
ATOM   130   C  CA    . HIS   A 1 23  ? 159.959 163.448 109.422 1.00 48.03  ?  23   HIS   A CA    1 
ATOM   131   C  C     . HIS   A 1 23  ? 160.985 163.022 110.455 1.00 47.62  ?  23   HIS   A C     1 
ATOM   132   O  O     . HIS   A 1 23  ? 161.621 161.981 110.324 1.00 46.46  ?  23   HIS   A O     1 
ATOM   133   C  CB    . HIS   A 1 23  ? 160.556 164.499 108.500 1.00 49.80  ?  23   HIS   A CB    1 
ATOM   134   C  CG    . HIS   A 1 23  ? 161.690 163.996 107.674 1.00 49.60  ?  23   HIS   A CG    1 
ATOM   135   N  ND1   . HIS   A 1 23  ? 161.494 163.300 106.499 1.00 48.83  ?  23   HIS   A ND1   1 
ATOM   136   C  CD2   . HIS   A 1 23  ? 163.026 164.083 107.842 1.00 50.34  ?  23   HIS   A CD2   1 
ATOM   137   C  CE1   . HIS   A 1 23  ? 162.669 162.978 105.982 1.00 49.14  ?  23   HIS   A CE1   1 
ATOM   138   N  NE2   . HIS   A 1 23  ? 163.613 163.442 106.782 1.00 50.56  ?  23   HIS   A NE2   1 
ATOM   139   N  N     . ARG   A 1 24  ? 161.112 163.819 111.506 1.00 48.76  ?  24   ARG   A N     1 
ATOM   140   C  CA    . ARG   A 1 24  ? 162.073 163.548 112.565 1.00 49.86  ?  24   ARG   A CA    1 
ATOM   141   C  C     . ARG   A 1 24  ? 161.751 162.233 113.270 1.00 48.20  ?  24   ARG   A C     1 
ATOM   142   O  O     . ARG   A 1 24  ? 162.645 161.440 113.560 1.00 46.05  ?  24   ARG   A O     1 
ATOM   143   C  CB    . ARG   A 1 24  ? 162.101 164.715 113.548 1.00 53.45  ?  24   ARG   A CB    1 
ATOM   144   C  CG    . ARG   A 1 24  ? 163.248 164.679 114.536 1.00 61.03  ?  24   ARG   A CG    1 
ATOM   145   C  CD    . ARG   A 1 24  ? 163.391 166.024 115.236 1.00 69.95  ?  24   ARG   A CD    1 
ATOM   146   N  NE    . ARG   A 1 24  ? 162.297 166.308 116.156 1.00 79.77  ?  24   ARG   A NE    1 
ATOM   147   C  CZ    . ARG   A 1 24  ? 162.383 166.178 117.475 1.00 90.78  ?  24   ARG   A CZ    1 
ATOM   148   N  NH1   . ARG   A 1 24  ? 163.522 165.794 118.032 1.00 93.05  1  24   ARG   A NH1   1 
ATOM   149   N  NH2   . ARG   A 1 24  ? 161.336 166.452 118.241 1.00 94.90  ?  24   ARG   A NH2   1 
ATOM   150   N  N     . VAL   A 1 25  ? 160.470 162.007 113.533 1.00 46.02  ?  25   VAL   A N     1 
ATOM   151   C  CA    . VAL   A 1 25  ? 160.002 160.772 114.147 1.00 44.31  ?  25   VAL   A CA    1 
ATOM   152   C  C     . VAL   A 1 25  ? 160.260 159.576 113.234 1.00 42.92  ?  25   VAL   A C     1 
ATOM   153   O  O     . VAL   A 1 25  ? 160.664 158.508 113.694 1.00 41.83  ?  25   VAL   A O     1 
ATOM   154   C  CB    . VAL   A 1 25  ? 158.504 160.855 114.492 1.00 44.28  ?  25   VAL   A CB    1 
ATOM   155   C  CG1   . VAL   A 1 25  ? 157.979 159.522 114.948 1.00 42.66  ?  25   VAL   A CG1   1 
ATOM   156   C  CG2   . VAL   A 1 25  ? 158.280 161.913 115.551 1.00 45.84  ?  25   VAL   A CG2   1 
ATOM   157   N  N     . LEU   A 1 26  ? 160.032 159.760 111.939 1.00 44.56  ?  26   LEU   A N     1 
ATOM   158   C  CA    . LEU   A 1 26  ? 160.271 158.699 110.976 1.00 42.18  ?  26   LEU   A CA    1 
ATOM   159   C  C     . LEU   A 1 26  ? 161.752 158.358 110.899 1.00 42.36  ?  26   LEU   A C     1 
ATOM   160   O  O     . LEU   A 1 26  ? 162.112 157.201 110.717 1.00 43.18  ?  26   LEU   A O     1 
ATOM   161   C  CB    . LEU   A 1 26  ? 159.748 159.085 109.601 1.00 42.70  ?  26   LEU   A CB    1 
ATOM   162   C  CG    . LEU   A 1 26  ? 158.230 159.086 109.450 1.00 42.55  ?  26   LEU   A CG    1 
ATOM   163   C  CD1   . LEU   A 1 26  ? 157.851 159.641 108.103 1.00 43.40  ?  26   LEU   A CD1   1 
ATOM   164   C  CD2   . LEU   A 1 26  ? 157.694 157.684 109.621 1.00 41.18  ?  26   LEU   A CD2   1 
ATOM   165   N  N     . ASP   A 1 27  ? 162.503 159.409 111.123 1.00 150.00 ?  27   ASP   A N     1 
ATOM   166   C  CA    . ASP   A 1 27  ? 163.931 159.154 111.045 1.00 150.77 ?  27   ASP   A CA    1 
ATOM   167   C  C     . ASP   A 1 27  ? 164.429 158.330 112.220 1.00 152.08 ?  27   ASP   A C     1 
ATOM   168   O  O     . ASP   A 1 27  ? 165.412 157.594 112.075 1.00 151.88 ?  27   ASP   A O     1 
ATOM   169   C  CB    . ASP   A 1 27  ? 164.704 160.476 110.975 1.00 151.34 ?  27   ASP   A CB    1 
ATOM   170   C  CG    . ASP   A 1 27  ? 166.166 160.278 110.626 1.00 152.56 ?  27   ASP   A CG    1 
ATOM   171   O  OD1   . ASP   A 1 27  ? 166.515 159.196 110.107 1.00 152.18 ?  27   ASP   A OD1   1 
ATOM   172   O  OD2   . ASP   A 1 27  ? 166.968 161.204 110.871 1.00 152.84 ?  27   ASP   A OD2   1 
ATOM   173   N  N     . TRP   A 1 28  ? 163.793 158.464 113.389 1.00 150.71 ?  28   TRP   A N     1 
ATOM   174   C  CA    . TRP   A 1 28  ? 164.131 157.557 114.495 1.00 149.55 ?  28   TRP   A CA    1 
ATOM   175   C  C     . TRP   A 1 28  ? 163.702 156.123 114.198 1.00 148.76 ?  28   TRP   A C     1 
ATOM   176   O  O     . TRP   A 1 28  ? 164.449 155.168 114.452 1.00 146.85 ?  28   TRP   A O     1 
ATOM   177   C  CB    . TRP   A 1 28  ? 163.483 158.023 115.793 1.00 149.86 ?  28   TRP   A CB    1 
ATOM   178   C  CG    . TRP   A 1 28  ? 164.040 159.291 116.340 1.00 149.87 ?  28   TRP   A CG    1 
ATOM   179   C  CD1   . TRP   A 1 28  ? 165.351 159.662 116.383 1.00 147.50 ?  28   TRP   A CD1   1 
ATOM   180   C  CD2   . TRP   A 1 28  ? 163.300 160.357 116.943 1.00 150.49 ?  28   TRP   A CD2   1 
ATOM   181   N  NE1   . TRP   A 1 28  ? 165.472 160.900 116.967 1.00 147.29 ?  28   TRP   A NE1   1 
ATOM   182   C  CE2   . TRP   A 1 28  ? 164.226 161.347 117.319 1.00 148.81 ?  28   TRP   A CE2   1 
ATOM   183   C  CE3   . TRP   A 1 28  ? 161.944 160.573 117.198 1.00 150.39 ?  28   TRP   A CE3   1 
ATOM   184   C  CZ2   . TRP   A 1 28  ? 163.840 162.534 117.935 1.00 149.19 ?  28   TRP   A CZ2   1 
ATOM   185   C  CZ3   . TRP   A 1 28  ? 161.563 161.753 117.805 1.00 148.73 ?  28   TRP   A CZ3   1 
ATOM   186   C  CH2   . TRP   A 1 28  ? 162.506 162.716 118.169 1.00 149.04 ?  28   TRP   A CH2   1 
ATOM   187   N  N     . ALA   A 1 29  ? 162.480 155.958 113.693 1.00 142.56 ?  29   ALA   A N     1 
ATOM   188   C  CA    . ALA   A 1 29  ? 162.021 154.630 113.322 1.00 141.45 ?  29   ALA   A CA    1 
ATOM   189   C  C     . ALA   A 1 29  ? 162.874 154.040 112.210 1.00 142.08 ?  29   ALA   A C     1 
ATOM   190   O  O     . ALA   A 1 29  ? 162.840 152.827 111.993 1.00 142.36 ?  29   ALA   A O     1 
ATOM   191   C  CB    . ALA   A 1 29  ? 160.552 154.674 112.891 1.00 140.80 ?  29   ALA   A CB    1 
ATOM   192   N  N     . ALA   A 1 30  ? 163.579 154.859 111.425 1.00 141.25 ?  30   ALA   A N     1 
ATOM   193   C  CA    . ALA   A 1 30  ? 164.273 154.240 110.303 1.00 138.27 ?  30   ALA   A CA    1 
ATOM   194   C  C     . ALA   A 1 30  ? 165.778 154.082 110.504 1.00 137.45 ?  30   ALA   A C     1 
ATOM   195   O  O     . ALA   A 1 30  ? 166.496 153.828 109.527 1.00 136.58 ?  30   ALA   A O     1 
ATOM   196   C  CB    . ALA   A 1 30  ? 163.989 155.029 109.034 1.00 138.58 ?  30   ALA   A CB    1 
ATOM   197   N  N     . GLU   A 1 31  ? 166.275 154.202 111.734 1.00 144.09 ?  31   GLU   A N     1 
ATOM   198   C  CA    . GLU   A 1 31  ? 167.721 154.175 111.951 1.00 145.71 ?  31   GLU   A CA    1 
ATOM   199   C  C     . GLU   A 1 31  ? 168.212 152.732 111.916 1.00 146.78 ?  31   GLU   A C     1 
ATOM   200   O  O     . GLU   A 1 31  ? 167.852 151.944 112.793 1.00 146.89 ?  31   GLU   A O     1 
ATOM   201   C  CB    . GLU   A 1 31  ? 168.082 154.834 113.281 1.00 145.16 ?  31   GLU   A CB    1 
ATOM   202   C  CG    . GLU   A 1 31  ? 169.532 155.296 113.364 1.00 146.68 ?  31   GLU   A CG    1 
ATOM   203   C  CD    . GLU   A 1 31  ? 170.547 154.170 113.459 1.00 148.33 ?  31   GLU   A CD    1 
ATOM   204   O  OE1   . GLU   A 1 31  ? 170.203 153.096 113.991 1.00 149.42 ?  31   GLU   A OE1   1 
ATOM   205   O  OE2   . GLU   A 1 31  ? 171.691 154.371 112.999 1.00 148.21 ?  31   GLU   A OE2   1 
ATOM   206   N  N     . GLY   A 1 32  ? 169.045 152.376 110.919 1.00 136.88 ?  32   GLY   A N     1 
ATOM   207   C  CA    . GLY   A 1 32  ? 169.651 151.057 110.850 1.00 135.12 ?  32   GLY   A CA    1 
ATOM   208   C  C     . GLY   A 1 32  ? 169.015 150.111 109.851 1.00 136.09 ?  32   GLY   A C     1 
ATOM   209   O  O     . GLY   A 1 32  ? 169.684 149.173 109.400 1.00 136.34 ?  32   GLY   A O     1 
ATOM   210   N  N     . LEU   A 1 33  ? 167.755 150.339 109.480 1.00 134.03 ?  33   LEU   A N     1 
ATOM   211   C  CA    . LEU   A 1 33  ? 167.024 149.455 108.576 1.00 133.46 ?  33   LEU   A CA    1 
ATOM   212   C  C     . LEU   A 1 33  ? 167.610 149.584 107.172 1.00 133.84 ?  33   LEU   A C     1 
ATOM   213   O  O     . LEU   A 1 33  ? 168.399 150.494 106.918 1.00 133.81 ?  33   LEU   A O     1 
ATOM   214   C  CB    . LEU   A 1 33  ? 165.541 149.819 108.595 1.00 132.88 ?  33   LEU   A CB    1 
ATOM   215   C  CG    . LEU   A 1 33  ? 164.799 149.562 109.909 1.00 132.00 ?  33   LEU   A CG    1 
ATOM   216   C  CD1   . LEU   A 1 33  ? 165.221 150.552 110.984 1.00 133.28 ?  33   LEU   A CD1   1 
ATOM   217   C  CD2   . LEU   A 1 33  ? 163.297 149.633 109.698 1.00 134.46 ?  33   LEU   A CD2   1 
ATOM   218   N  N     . HIS   A 1 34  ? 167.245 148.669 106.251 1.00 140.60 ?  34   HIS   A N     1 
ATOM   219   C  CA    . HIS   A 1 34  ? 167.699 148.755 104.865 1.00 140.53 ?  34   HIS   A CA    1 
ATOM   220   C  C     . HIS   A 1 34  ? 166.521 148.568 103.920 1.00 141.73 ?  34   HIS   A C     1 
ATOM   221   O  O     . HIS   A 1 34  ? 165.606 147.788 104.202 1.00 142.31 ?  34   HIS   A O     1 
ATOM   222   C  CB    . HIS   A 1 34  ? 168.793 147.723 104.562 1.00 138.64 ?  34   HIS   A CB    1 
ATOM   223   C  CG    . HIS   A 1 34  ? 170.059 147.944 105.331 1.00 140.36 ?  34   HIS   A CG    1 
ATOM   224   N  ND1   . HIS   A 1 34  ? 170.613 146.980 106.145 1.00 141.59 ?  34   HIS   A ND1   1 
ATOM   225   C  CD2   . HIS   A 1 34  ? 170.873 149.023 105.419 1.00 140.65 ?  34   HIS   A CD2   1 
ATOM   226   C  CE1   . HIS   A 1 34  ? 171.715 147.454 106.699 1.00 141.17 ?  34   HIS   A CE1   1 
ATOM   227   N  NE2   . HIS   A 1 34  ? 171.895 148.692 106.275 1.00 140.25 ?  34   HIS   A NE2   1 
ATOM   228   N  N     . ASN   A 1 35  ? 166.545 149.311 102.809 1.00 140.98 ?  35   ASN   A N     1 
ATOM   229   C  CA    . ASN   A 1 35  ? 165.501 149.269 101.779 1.00 139.74 ?  35   ASN   A CA    1 
ATOM   230   C  C     . ASN   A 1 35  ? 164.169 149.811 102.305 1.00 140.70 ?  35   ASN   A C     1 
ATOM   231   O  O     . ASN   A 1 35  ? 163.110 149.225 102.082 1.00 140.31 ?  35   ASN   A O     1 
ATOM   232   C  CB    . ASN   A 1 35  ? 165.331 147.854 101.217 1.00 139.39 ?  35   ASN   A CB    1 
ATOM   233   C  CG    . ASN   A 1 35  ? 164.753 147.848 99.816  1.00 140.53 ?  35   ASN   A CG    1 
ATOM   234   O  OD1   . ASN   A 1 35  ? 163.928 148.692 99.470  1.00 141.19 ?  35   ASN   A OD1   1 
ATOM   235   N  ND2   . ASN   A 1 35  ? 165.185 146.892 99.001  1.00 140.43 ?  35   ASN   A ND2   1 
ATOM   236   N  N     . VAL   A 1 36  ? 164.228 150.948 102.997 1.00 145.91 ?  36   VAL   A N     1 
ATOM   237   C  CA    . VAL   A 1 36  ? 163.041 151.621 103.514 1.00 146.37 ?  36   VAL   A CA    1 
ATOM   238   C  C     . VAL   A 1 36  ? 163.054 153.064 103.030 1.00 146.61 ?  36   VAL   A C     1 
ATOM   239   O  O     . VAL   A 1 36  ? 164.055 153.770 103.196 1.00 146.58 ?  36   VAL   A O     1 
ATOM   240   C  CB    . VAL   A 1 36  ? 162.973 151.565 105.053 1.00 145.69 ?  36   VAL   A CB    1 
ATOM   241   C  CG1   . VAL   A 1 36  ? 161.997 152.601 105.585 1.00 144.14 ?  36   VAL   A CG1   1 
ATOM   242   C  CG2   . VAL   A 1 36  ? 162.570 150.176 105.509 1.00 146.15 ?  36   VAL   A CG2   1 
ATOM   243   N  N     . SER   A 1 37  ? 161.944 153.499 102.435 1.00 150.96 ?  37   SER   A N     1 
ATOM   244   C  CA    . SER   A 1 37  ? 161.789 154.867 101.946 1.00 150.58 ?  37   SER   A CA    1 
ATOM   245   C  C     . SER   A 1 37  ? 160.942 155.653 102.949 1.00 150.74 ?  37   SER   A C     1 
ATOM   246   O  O     . SER   A 1 37  ? 159.698 155.528 102.995 1.00 150.43 ?  37   SER   A O     1 
ATOM   247   C  CB    . SER   A 1 37  ? 161.168 154.881 100.554 1.00 149.92 ?  37   SER   A CB    1 
ATOM   248   O  OG    . SER   A 1 37  ? 160.894 156.206 100.130 1.00 150.26 ?  37   SER   A OG    1 
ATOM   249   N  N     . ILE   A 1 38  ? 161.624 156.482 103.746 1.00 148.16 ?  38   ILE   A N     1 
ATOM   250   C  CA    . ILE   A 1 38  ? 160.921 157.396 104.641 1.00 148.91 ?  38   ILE   A CA    1 
ATOM   251   C  C     . ILE   A 1 38  ? 159.997 158.295 103.833 1.00 149.92 ?  38   ILE   A C     1 
ATOM   252   O  O     . ILE   A 1 38  ? 158.837 158.529 104.206 1.00 150.20 ?  38   ILE   A O     1 
ATOM   253   C  CB    . ILE   A 1 38  ? 161.928 158.220 105.471 1.00 148.36 ?  38   ILE   A CB    1 
ATOM   254   C  CG1   . ILE   A 1 38  ? 162.720 157.326 106.436 1.00 148.60 ?  38   ILE   A CG1   1 
ATOM   255   C  CG2   . ILE   A 1 38  ? 161.217 159.332 106.233 1.00 148.15 ?  38   ILE   A CG2   1 
ATOM   256   C  CD1   . ILE   A 1 38  ? 163.911 158.011 107.099 1.00 147.33 ?  38   ILE   A CD1   1 
ATOM   257   N  N     . SER   A 1 39  ? 160.495 158.787 102.696 1.00 155.84 ?  39   SER   A N     1 
ATOM   258   C  CA    . SER   A 1 39  ? 159.718 159.686 101.854 1.00 155.89 ?  39   SER   A CA    1 
ATOM   259   C  C     . SER   A 1 39  ? 158.424 159.036 101.386 1.00 157.32 ?  39   SER   A C     1 
ATOM   260   O  O     . SER   A 1 39  ? 157.396 159.706 101.287 1.00 156.59 ?  39   SER   A O     1 
ATOM   261   C  CB    . SER   A 1 39  ? 160.557 160.129 100.656 1.00 155.27 ?  39   SER   A CB    1 
ATOM   262   O  OG    . SER   A 1 39  ? 160.940 159.018 99.863  1.00 155.32 ?  39   SER   A OG    1 
ATOM   263   N  N     . GLN   A 1 40  ? 158.436 157.720 101.170 1.00 154.43 ?  40   GLN   A N     1 
ATOM   264   C  CA    . GLN   A 1 40  ? 157.218 157.098 100.597 1.00 152.75 ?  40   GLN   A CA    1 
ATOM   265   C  C     . GLN   A 1 40  ? 156.154 157.010 101.675 1.00 153.17 ?  40   GLN   A C     1 
ATOM   266   O  O     . GLN   A 1 40  ? 154.983 157.300 101.382 1.00 152.49 ?  40   GLN   A O     1 
ATOM   267   C  CB    . GLN   A 1 40  ? 157.537 155.747 99.990  1.00 151.14 ?  40   GLN   A CB    1 
ATOM   268   C  CG    . GLN   A 1 40  ? 156.332 155.106 99.312  1.00 150.67 ?  40   GLN   A CG    1 
ATOM   269   C  CD    . GLN   A 1 40  ? 156.702 154.252 98.122  1.00 152.39 ?  40   GLN   A CD    1 
ATOM   270   O  OE1   . GLN   A 1 40  ? 157.871 153.915 97.911  1.00 152.19 ?  40   GLN   A OE1   1 
ATOM   271   N  NE2   . GLN   A 1 40  ? 155.702 153.902 97.328  1.00 152.48 ?  40   GLN   A NE2   1 
ATOM   272   N  N     . VAL   A 1 41  ? 156.555 156.627 102.879 1.00 159.64 ?  41   VAL   A N     1 
ATOM   273   C  CA    . VAL   A 1 41  ? 155.581 156.655 103.975 1.00 160.32 ?  41   VAL   A CA    1 
ATOM   274   C  C     . VAL   A 1 41  ? 155.022 158.062 104.156 1.00 159.32 ?  41   VAL   A C     1 
ATOM   275   O  O     . VAL   A 1 41  ? 153.814 158.253 104.371 1.00 158.44 ?  41   VAL   A O     1 
ATOM   276   C  CB    . VAL   A 1 41  ? 156.223 156.139 105.273 1.00 159.53 ?  41   VAL   A CB    1 
ATOM   277   C  CG1   . VAL   A 1 41  ? 155.174 155.954 106.357 1.00 158.63 ?  41   VAL   A CG1   1 
ATOM   278   C  CG2   . VAL   A 1 41  ? 156.972 154.848 105.008 1.00 158.54 ?  41   VAL   A CG2   1 
ATOM   279   N  N     . GLU   A 1 42  ? 155.896 159.066 104.081 1.00 159.75 ?  42   GLU   A N     1 
ATOM   280   C  CA    . GLU   A 1 42  ? 155.436 160.449 104.134 1.00 159.73 ?  42   GLU   A CA    1 
ATOM   281   C  C     . GLU   A 1 42  ? 154.400 160.719 103.050 1.00 161.10 ?  42   GLU   A C     1 
ATOM   282   O  O     . GLU   A 1 42  ? 153.309 161.240 103.326 1.00 162.23 ?  42   GLU   A O     1 
ATOM   283   C  CB    . GLU   A 1 42  ? 156.630 161.392 103.993 1.00 159.70 ?  42   GLU   A CB    1 
ATOM   284   C  CG    . GLU   A 1 42  ? 157.654 161.251 105.101 1.00 160.03 ?  42   GLU   A CG    1 
ATOM   285   C  CD    . GLU   A 1 42  ? 158.564 162.452 105.210 1.00 159.78 ?  42   GLU   A CD    1 
ATOM   286   O  OE1   . GLU   A 1 42  ? 158.242 163.499 104.612 1.00 159.46 ?  42   GLU   A OE1   1 
ATOM   287   O  OE2   . GLU   A 1 42  ? 159.604 162.348 105.891 1.00 159.97 ?  42   GLU   A OE2   1 
ATOM   288   N  N     . LEU   A 1 43  ? 154.726 160.348 101.812 1.00 161.56 ?  43   LEU   A N     1 
ATOM   289   C  CA    . LEU   A 1 43  ? 153.824 160.550 100.690 1.00 162.01 ?  43   LEU   A CA    1 
ATOM   290   C  C     . LEU   A 1 43  ? 152.438 160.025 101.017 1.00 161.90 ?  43   LEU   A C     1 
ATOM   291   O  O     . LEU   A 1 43  ? 151.450 160.761 100.920 1.00 161.26 ?  43   LEU   A O     1 
ATOM   292   C  CB    . LEU   A 1 43  ? 154.388 159.853 99.451  1.00 161.66 ?  43   LEU   A CB    1 
ATOM   293   C  CG    . LEU   A 1 43  ? 153.449 159.754 98.250  1.00 161.29 ?  43   LEU   A CG    1 
ATOM   294   C  CD1   . LEU   A 1 43  ? 152.961 161.132 97.836  1.00 159.92 ?  43   LEU   A CD1   1 
ATOM   295   C  CD2   . LEU   A 1 43  ? 154.130 159.053 97.086  1.00 159.96 ?  43   LEU   A CD2   1 
ATOM   296   N  N     . ARG   A 1 44  ? 152.356 158.754 101.440 1.00 158.78 ?  44   ARG   A N     1 
ATOM   297   C  CA    . ARG   A 1 44  ? 151.048 158.150 101.693 1.00 157.93 ?  44   ARG   A CA    1 
ATOM   298   C  C     . ARG   A 1 44  ? 150.334 158.816 102.863 1.00 158.58 ?  44   ARG   A C     1 
ATOM   299   O  O     . ARG   A 1 44  ? 149.105 158.948 102.841 1.00 158.38 ?  44   ARG   A O     1 
ATOM   300   C  CB    . ARG   A 1 44  ? 151.180 156.647 101.942 1.00 157.01 ?  44   ARG   A CB    1 
ATOM   301   C  CG    . ARG   A 1 44  ? 151.447 155.838 100.689 1.00 156.49 ?  44   ARG   A CG    1 
ATOM   302   C  CD    . ARG   A 1 44  ? 151.093 154.375 100.894 1.00 157.00 ?  44   ARG   A CD    1 
ATOM   303   N  NE    . ARG   A 1 44  ? 151.061 153.665 99.622  1.00 158.30 ?  44   ARG   A NE    1 
ATOM   304   C  CZ    . ARG   A 1 44  ? 152.097 153.023 99.102  1.00 159.28 ?  44   ARG   A CZ    1 
ATOM   305   N  NH1   . ARG   A 1 44  ? 153.237 152.908 99.760  1.00 159.83 ?  44   ARG   A NH1   1 
ATOM   306   N  NH2   . ARG   A 1 44  ? 151.987 152.486 97.890  1.00 158.04 ?  44   ARG   A NH2   1 
ATOM   307   N  N     . SER   A 1 45  ? 151.076 159.248 103.885 1.00 163.31 ?  45   SER   A N     1 
ATOM   308   C  CA    . SER   A 1 45  ? 150.428 159.809 105.067 1.00 163.53 ?  45   SER   A CA    1 
ATOM   309   C  C     . SER   A 1 45  ? 149.825 161.184 104.793 1.00 165.92 ?  45   SER   A C     1 
ATOM   310   O  O     . SER   A 1 45  ? 148.723 161.486 105.265 1.00 165.99 ?  45   SER   A O     1 
ATOM   311   C  CB    . SER   A 1 45  ? 151.427 159.890 106.219 1.00 162.52 ?  45   SER   A CB    1 
ATOM   312   O  OG    . SER   A 1 45  ? 152.675 160.387 105.774 1.00 162.66 ?  45   SER   A OG    1 
ATOM   313   N  N     . HIS   A 1 46  ? 150.538 162.015 104.030 1.00 165.36 ?  46   HIS   A N     1 
ATOM   314   C  CA    . HIS   A 1 46  ? 150.134 163.423 103.776 1.00 162.68 ?  46   HIS   A CA    1 
ATOM   315   C  C     . HIS   A 1 46  ? 148.795 163.499 103.038 1.00 161.25 ?  46   HIS   A C     1 
ATOM   316   O  O     . HIS   A 1 46  ? 148.052 164.464 103.302 1.00 161.47 ?  46   HIS   A O     1 
ATOM   317   C  CB    . HIS   A 1 46  ? 151.264 164.120 103.021 1.00 162.67 ?  46   HIS   A CB    1 
ATOM   318   C  CG    . HIS   A 1 46  ? 152.502 164.300 103.838 1.00 163.83 ?  46   HIS   A CG    1 
ATOM   319   N  ND1   . HIS   A 1 46  ? 153.490 165.197 103.495 1.00 165.02 ?  46   HIS   A ND1   1 
ATOM   320   C  CD2   . HIS   A 1 46  ? 152.935 163.683 104.945 1.00 163.36 ?  46   HIS   A CD2   1 
ATOM   321   C  CE1   . HIS   A 1 46  ? 154.470 165.128 104.383 1.00 164.21 ?  46   HIS   A CE1   1 
ATOM   322   N  NE2   . HIS   A 1 46  ? 154.152 164.216 105.273 1.00 163.80 ?  46   HIS   A NE2   1 
ATOM   323   N  N     . ILE   A 1 47  ? 148.473 162.530 102.176 1.00 162.22 ?  47   ILE   A N     1 
ATOM   324   C  CA    . ILE   A 1 47  ? 147.214 162.566 101.377 1.00 163.96 ?  47   ILE   A CA    1 
ATOM   325   C  C     . ILE   A 1 47  ? 146.008 162.232 102.276 1.00 164.11 ?  47   ILE   A C     1 
ATOM   326   O  O     . ILE   A 1 47  ? 144.910 162.041 101.727 1.00 163.58 ?  47   ILE   A O     1 
ATOM   327   C  CB    . ILE   A 1 47  ? 147.310 161.655 100.143 1.00 163.98 ?  47   ILE   A CB    1 
ATOM   328   C  CG1   . ILE   A 1 47  ? 148.484 162.029 99.264  1.00 163.49 ?  47   ILE   A CG1   1 
ATOM   329   C  CG2   . ILE   A 1 47  ? 146.003 161.672 99.351  1.00 162.70 ?  47   ILE   A CG2   1 
ATOM   330   C  CD1   . ILE   A 1 47  ? 148.439 163.456 98.753  1.00 162.35 ?  47   ILE   A CD1   1 
ATOM   331   N  N     . GLN   A 1 48  ? 146.279 162.063 103.835 1.00 54.11  ?  48   GLN   A N     1 
ATOM   332   C  CA    . GLN   A 1 48  ? 145.163 161.794 104.732 1.00 55.00  ?  48   GLN   A CA    1 
ATOM   333   C  C     . GLN   A 1 48  ? 144.955 162.863 105.791 1.00 56.43  ?  48   GLN   A C     1 
ATOM   334   O  O     . GLN   A 1 48  ? 144.066 162.737 106.627 1.00 57.44  ?  48   GLN   A O     1 
ATOM   335   C  CB    . GLN   A 1 48  ? 145.350 160.453 105.430 1.00 53.05  ?  48   GLN   A CB    1 
ATOM   336   C  CG    . GLN   A 1 48  ? 145.647 159.324 104.504 1.00 51.74  ?  48   GLN   A CG    1 
ATOM   337   C  CD    . GLN   A 1 48  ? 145.661 158.005 105.221 1.00 50.30  ?  48   GLN   A CD    1 
ATOM   338   O  OE1   . GLN   A 1 48  ? 144.775 157.718 106.016 1.00 51.26  ?  48   GLN   A OE1   1 
ATOM   339   N  NE2   . GLN   A 1 48  ? 146.668 157.191 104.949 1.00 48.49  ?  48   GLN   A NE2   1 
ATOM   340   N  N     . PHE   A 1 49  ? 145.163 164.101 105.816 1.00 169.55 ?  49   PHE   A N     1 
ATOM   341   C  CA    . PHE   A 1 49  ? 145.341 164.922 107.046 1.00 171.32 ?  49   PHE   A CA    1 
ATOM   342   C  C     . PHE   A 1 49  ? 144.225 165.965 107.117 1.00 172.16 ?  49   PHE   A C     1 
ATOM   343   O  O     . PHE   A 1 49  ? 144.486 167.144 106.813 1.00 172.32 ?  49   PHE   A O     1 
ATOM   344   C  CB    . PHE   A 1 49  ? 146.756 165.510 107.050 1.00 171.19 ?  49   PHE   A CB    1 
ATOM   345   C  CG    . PHE   A 1 49  ? 147.868 164.605 107.567 1.00 170.73 ?  49   PHE   A CG    1 
ATOM   346   C  CD1   . PHE   A 1 49  ? 147.649 163.695 108.596 1.00 171.08 ?  49   PHE   A CD1   1 
ATOM   347   C  CD2   . PHE   A 1 49  ? 149.146 164.684 107.027 1.00 170.25 ?  49   PHE   A CD2   1 
ATOM   348   C  CE1   . PHE   A 1 49  ? 148.673 162.885 109.057 1.00 171.27 ?  49   PHE   A CE1   1 
ATOM   349   C  CE2   . PHE   A 1 49  ? 150.166 163.871 107.493 1.00 170.39 ?  49   PHE   A CE2   1 
ATOM   350   C  CZ    . PHE   A 1 49  ? 149.928 162.974 108.505 1.00 170.60 ?  49   PHE   A CZ    1 
ATOM   351   N  N     . TYR   A 1 50  ? 143.014 165.562 107.513 1.00 186.41 ?  50   TYR   A N     1 
ATOM   352   C  CA    . TYR   A 1 50  ? 141.882 166.484 107.682 1.00 186.78 ?  50   TYR   A CA    1 
ATOM   353   C  C     . TYR   A 1 50  ? 142.153 167.476 108.811 1.00 187.57 ?  50   TYR   A C     1 
ATOM   354   O  O     . TYR   A 1 50  ? 142.837 167.139 109.778 1.00 187.90 ?  50   TYR   A O     1 
ATOM   355   C  CB    . TYR   A 1 50  ? 140.613 165.695 108.016 1.00 186.35 ?  50   TYR   A CB    1 
ATOM   356   C  CG    . TYR   A 1 50  ? 140.730 164.912 109.305 1.00 187.16 ?  50   TYR   A CG    1 
ATOM   357   C  CD1   . TYR   A 1 50  ? 141.230 163.627 109.305 1.00 186.03 ?  50   TYR   A CD1   1 
ATOM   358   C  CD2   . TYR   A 1 50  ? 140.339 165.462 110.517 1.00 187.12 ?  50   TYR   A CD2   1 
ATOM   359   C  CE1   . TYR   A 1 50  ? 141.324 162.893 110.491 1.00 185.89 ?  50   TYR   A CE1   1 
ATOM   360   C  CE2   . TYR   A 1 50  ? 140.456 164.756 111.701 1.00 186.63 ?  50   TYR   A CE2   1 
ATOM   361   C  CZ    . TYR   A 1 50  ? 140.967 163.477 111.686 1.00 186.63 ?  50   TYR   A CZ    1 
ATOM   362   O  OH    . TYR   A 1 50  ? 141.089 162.768 112.854 1.00 186.94 ?  50   TYR   A OH    1 
ATOM   363   N  N     . ASP   A 1 51  ? 141.605 168.705 108.697 1.00 188.48 ?  51   ASP   A N     1 
ATOM   364   C  CA    . ASP   A 1 51  ? 141.752 169.697 109.768 1.00 188.55 ?  51   ASP   A CA    1 
ATOM   365   C  C     . ASP   A 1 51  ? 141.148 169.126 111.046 1.00 188.36 ?  51   ASP   A C     1 
ATOM   366   O  O     . ASP   A 1 51  ? 140.082 168.510 111.003 1.00 187.92 ?  51   ASP   A O     1 
ATOM   367   C  CB    . ASP   A 1 51  ? 141.076 171.030 109.388 1.00 187.49 ?  51   ASP   A CB    1 
ATOM   368   C  CG    . ASP   A 1 51  ? 141.906 171.851 108.415 1.00 187.42 ?  51   ASP   A CG    1 
ATOM   369   O  OD1   . ASP   A 1 51  ? 142.959 171.352 107.978 1.00 187.98 ?  51   ASP   A OD1   1 
ATOM   370   O  OD2   . ASP   A 1 51  ? 141.496 172.988 108.099 1.00 187.38 ?  51   ASP   A OD2   1 
ATOM   371   N  N     . GLY   A 1 52  ? 141.833 169.308 112.190 1.00 188.45 ?  52   GLY   A N     1 
ATOM   372   C  CA    . GLY   A 1 52  ? 141.428 168.677 113.432 1.00 188.04 ?  52   GLY   A CA    1 
ATOM   373   C  C     . GLY   A 1 52  ? 142.191 167.406 113.717 1.00 188.78 ?  52   GLY   A C     1 
ATOM   374   O  O     . GLY   A 1 52  ? 142.107 166.888 114.839 1.00 188.90 ?  52   GLY   A O     1 
ATOM   375   N  N     . ILE   A 1 53  ? 142.943 166.901 112.728 1.00 181.31 ?  53   ILE   A N     1 
ATOM   376   C  CA    . ILE   A 1 53  ? 143.792 165.718 112.872 1.00 180.14 ?  53   ILE   A CA    1 
ATOM   377   C  C     . ILE   A 1 53  ? 144.500 165.820 114.221 1.00 180.03 ?  53   ILE   A C     1 
ATOM   378   O  O     . ILE   A 1 53  ? 144.992 166.902 114.558 1.00 180.07 ?  53   ILE   A O     1 
ATOM   379   C  CB    . ILE   A 1 53  ? 144.783 165.654 111.684 1.00 179.66 ?  53   ILE   A CB    1 
ATOM   380   C  CG1   . ILE   A 1 53  ? 145.524 164.317 111.608 1.00 179.41 ?  53   ILE   A CG1   1 
ATOM   381   C  CG2   . ILE   A 1 53  ? 145.736 166.837 111.675 1.00 179.23 ?  53   ILE   A CG2   1 
ATOM   382   C  CD1   . ILE   A 1 53  ? 144.700 163.192 111.314 1.00 178.97 ?  53   ILE   A CD1   1 
ATOM   383   N  N     . LYS   A 1 54  ? 144.520 164.758 115.038 1.00 168.05 ?  54   LYS   A N     1 
ATOM   384   C  CA    . LYS   A 1 54  ? 145.097 164.900 116.372 1.00 167.27 ?  54   LYS   A CA    1 
ATOM   385   C  C     . LYS   A 1 54  ? 146.420 164.152 116.400 1.00 166.95 ?  54   LYS   A C     1 
ATOM   386   O  O     . LYS   A 1 54  ? 146.598 163.203 115.636 1.00 167.78 ?  54   LYS   A O     1 
ATOM   387   C  CB    . LYS   A 1 54  ? 144.150 164.390 117.470 1.00 166.94 ?  54   LYS   A CB    1 
ATOM   388   C  CG    . LYS   A 1 54  ? 142.908 165.251 117.691 1.00 167.16 ?  54   LYS   A CG    1 
ATOM   389   C  CD    . LYS   A 1 54  ? 142.245 164.982 119.034 1.00 166.64 ?  54   LYS   A CD    1 
ATOM   390   C  CE    . LYS   A 1 54  ? 143.227 165.061 120.187 1.00 167.15 ?  54   LYS   A CE    1 
ATOM   391   N  NZ    . LYS   A 1 54  ? 143.965 166.348 120.199 1.00 167.93 ?  54   LYS   A NZ    1 
ATOM   392   N  N     . THR   A 1 55  ? 147.363 164.587 117.257 1.00 170.74 ?  55   THR   A N     1 
ATOM   393   C  CA    . THR   A 1 55  ? 148.684 163.954 117.254 1.00 171.71 ?  55   THR   A CA    1 
ATOM   394   C  C     . THR   A 1 55  ? 148.556 162.432 117.343 1.00 171.86 ?  55   THR   A C     1 
ATOM   395   O  O     . THR   A 1 55  ? 149.373 161.698 116.761 1.00 171.39 ?  55   THR   A O     1 
ATOM   396   C  CB    . THR   A 1 55  ? 149.564 164.515 118.382 1.00 172.35 ?  55   THR   A CB    1 
ATOM   397   O  OG1   . THR   A 1 55  ? 148.822 164.560 119.602 1.00 172.83 ?  55   THR   A OG1   1 
ATOM   398   C  CG2   . THR   A 1 55  ? 150.063 165.919 118.040 1.00 171.00 ?  55   THR   A CG2   1 
ATOM   399   N  N     . SER   A 1 56  ? 147.486 161.943 117.988 1.00 166.27 ?  56   SER   A N     1 
ATOM   400   C  CA    . SER   A 1 56  ? 147.209 160.510 118.001 1.00 166.14 ?  56   SER   A CA    1 
ATOM   401   C  C     . SER   A 1 56  ? 146.736 160.025 116.637 1.00 166.70 ?  56   SER   A C     1 
ATOM   402   O  O     . SER   A 1 56  ? 147.154 158.958 116.174 1.00 168.05 ?  56   SER   A O     1 
ATOM   403   C  CB    . SER   A 1 56  ? 146.174 160.180 119.079 1.00 165.18 ?  56   SER   A CB    1 
ATOM   404   O  OG    . SER   A 1 56  ? 146.795 160.006 120.341 1.00 165.67 ?  56   SER   A OG    1 
ATOM   405   N  N     . ASP   A 1 57  ? 145.869 160.796 115.975 1.00 158.20 ?  57   ASP   A N     1 
ATOM   406   C  CA    . ASP   A 1 57  ? 145.402 160.411 114.646 1.00 156.32 ?  57   ASP   A CA    1 
ATOM   407   C  C     . ASP   A 1 57  ? 146.531 160.460 113.622 1.00 155.68 ?  57   ASP   A C     1 
ATOM   408   O  O     . ASP   A 1 57  ? 146.607 159.597 112.740 1.00 155.37 ?  57   ASP   A O     1 
ATOM   409   C  CB    . ASP   A 1 57  ? 144.241 161.306 114.214 1.00 157.46 ?  57   ASP   A CB    1 
ATOM   410   C  CG    . ASP   A 1 57  ? 142.962 161.003 114.968 1.00 157.72 ?  57   ASP   A CG    1 
ATOM   411   O  OD1   . ASP   A 1 57  ? 142.596 159.813 115.066 1.00 157.36 ?  57   ASP   A OD1   1 
ATOM   412   O  OD2   . ASP   A 1 57  ? 142.322 161.954 115.463 1.00 157.79 ?  57   ASP   A OD2   1 
ATOM   413   N  N     . ILE   A 1 58  ? 147.414 161.458 113.718 1.00 160.08 ?  58   ILE   A N     1 
ATOM   414   C  CA    . ILE   A 1 58  ? 148.566 161.514 112.821 1.00 160.13 ?  58   ILE   A CA    1 
ATOM   415   C  C     . ILE   A 1 58  ? 149.432 160.271 112.998 1.00 161.58 ?  58   ILE   A C     1 
ATOM   416   O  O     . ILE   A 1 58  ? 149.842 159.639 112.015 1.00 162.52 ?  58   ILE   A O     1 
ATOM   417   C  CB    . ILE   A 1 58  ? 149.381 162.798 113.056 1.00 161.58 ?  58   ILE   A CB    1 
ATOM   418   C  CG1   . ILE   A 1 58  ? 148.558 164.041 112.740 1.00 162.51 ?  58   ILE   A CG1   1 
ATOM   419   C  CG2   . ILE   A 1 58  ? 150.658 162.776 112.233 1.00 161.31 ?  58   ILE   A CG2   1 
ATOM   420   C  CD1   . ILE   A 1 58  ? 148.696 165.120 113.789 1.00 162.27 ?  58   ILE   A CD1   1 
ATOM   421   N  N     . HIS   A 1 59  ? 149.732 159.929 114.265 1.00 156.48 ?  59   HIS   A N     1 
ATOM   422   C  CA    . HIS   A 1 59  ? 150.594 158.747 114.575 1.00 155.07 ?  59   HIS   A CA    1 
ATOM   423   C  C     . HIS   A 1 59  ? 149.894 157.477 114.050 1.00 155.94 ?  59   HIS   A C     1 
ATOM   424   O  O     . HIS   A 1 59  ? 150.581 156.683 113.401 1.00 155.95 ?  59   HIS   A O     1 
ATOM   425   C  CB    . HIS   A 1 59  ? 151.025 158.751 116.072 1.00 153.17 ?  59   HIS   A CB    1 
ATOM   426   C  CG    . HIS   A 1 59  ? 152.369 158.144 116.368 1.00 155.07 ?  59   HIS   A CG    1 
ATOM   427   N  ND1   . HIS   A 1 59  ? 153.138 158.395 117.542 1.00 155.67 ?  59   HIS   A ND1   1 
ATOM   428   C  CD2   . HIS   A 1 59  ? 153.089 157.269 115.636 1.00 156.24 ?  59   HIS   A CD2   1 
ATOM   429   C  CE1   . HIS   A 1 59  ? 154.250 157.682 117.455 1.00 156.55 ?  59   HIS   A CE1   1 
ATOM   430   N  NE2   . HIS   A 1 59  ? 154.242 156.995 116.312 1.00 157.27 ?  59   HIS   A NE2   1 
ATOM   431   N  N     . GLU   A 1 60  ? 148.572 157.334 114.238 1.00 157.26 ?  60   GLU   A N     1 
ATOM   432   C  CA    . GLU   A 1 60  ? 147.842 156.159 113.781 1.00 156.07 ?  60   GLU   A CA    1 
ATOM   433   C  C     . GLU   A 1 60  ? 147.882 156.050 112.262 1.00 156.86 ?  60   GLU   A C     1 
ATOM   434   O  O     . GLU   A 1 60  ? 148.147 154.974 111.713 1.00 158.35 ?  60   GLU   A O     1 
ATOM   435   C  CB    . GLU   A 1 60  ? 146.402 156.202 114.283 1.00 155.44 ?  60   GLU   A CB    1 
ATOM   436   C  CG    . GLU   A 1 60  ? 145.654 154.890 114.136 1.00 157.09 ?  60   GLU   A CG    1 
ATOM   437   C  CD    . GLU   A 1 60  ? 144.554 154.963 113.097 1.00 158.20 ?  60   GLU   A CD    1 
ATOM   438   O  OE1   . GLU   A 1 60  ? 144.619 155.853 112.223 1.00 157.63 ?  60   GLU   A OE1   1 
ATOM   439   O  OE2   . GLU   A 1 60  ? 143.624 154.131 113.154 1.00 158.56 ?  60   GLU   A OE2   1 
ATOM   440   N  N     . THR   A 1 61  ? 147.646 157.163 111.564 1.00 151.50 ?  61   THR   A N     1 
ATOM   441   C  CA    . THR   A 1 61  ? 147.668 157.142 110.106 1.00 150.55 ?  61   THR   A CA    1 
ATOM   442   C  C     . THR   A 1 61  ? 149.052 156.782 109.580 1.00 149.51 ?  61   THR   A C     1 
ATOM   443   O  O     . THR   A 1 61  ? 149.183 155.976 108.649 1.00 150.38 ?  61   THR   A O     1 
ATOM   444   C  CB    . THR   A 1 61  ? 147.216 158.498 109.561 1.00 151.67 ?  61   THR   A CB    1 
ATOM   445   O  OG1   . THR   A 1 61  ? 145.784 158.563 109.563 1.00 151.92 ?  61   THR   A OG1   1 
ATOM   446   C  CG2   . THR   A 1 61  ? 147.722 158.709 108.142 1.00 151.18 ?  61   THR   A CG2   1 
ATOM   447   N  N     . ILE   A 1 62  ? 150.103 157.360 110.165 1.00 139.54 ?  62   ILE   A N     1 
ATOM   448   C  CA    . ILE   A 1 62  ? 151.480 157.129 109.632 1.00 139.21 ?  62   ILE   A CA    1 
ATOM   449   C  C     . ILE   A 1 62  ? 151.925 155.696 109.932 1.00 141.73 ?  62   ILE   A C     1 
ATOM   450   O  O     . ILE   A 1 62  ? 152.605 155.109 109.073 1.00 141.13 ?  62   ILE   A O     1 
ATOM   451   C  CB    . ILE   A 1 62  ? 152.494 158.157 110.174 1.00 138.73 ?  62   ILE   A CB    1 
ATOM   452   C  CG1   . ILE   A 1 62  ? 152.785 157.951 111.662 1.00 140.26 ?  62   ILE   A CG1   1 
ATOM   453   C  CG2   . ILE   A 1 62  ? 152.030 159.575 109.882 1.00 137.92 ?  62   ILE   A CG2   1 
ATOM   454   C  CD1   . ILE   A 1 62  ? 153.933 158.780 112.186 1.00 141.98 ?  62   ILE   A CD1   1 
ATOM   455   N  N     . ILE   A 1 63  ? 151.597 155.173 111.110 1.00 147.23 ?  63   ILE   A N     1 
ATOM   456   C  CA    . ILE   A 1 63  ? 151.930 153.745 111.360 1.00 144.79 ?  63   ILE   A CA    1 
ATOM   457   C  C     . ILE   A 1 63  ? 151.160 152.930 110.322 1.00 145.26 ?  63   ILE   A C     1 
ATOM   458   O  O     . ILE   A 1 63  ? 151.789 152.099 109.651 1.00 147.19 ?  63   ILE   A O     1 
ATOM   459   C  CB    . ILE   A 1 63  ? 151.585 153.327 112.803 1.00 144.33 ?  63   ILE   A CB    1 
ATOM   460   C  CG1   . ILE   A 1 63  ? 152.527 153.971 113.822 1.00 145.91 ?  63   ILE   A CG1   1 
ATOM   461   C  CG2   . ILE   A 1 63  ? 151.564 151.813 112.936 1.00 144.35 ?  63   ILE   A CG2   1 
ATOM   462   C  CD1   . ILE   A 1 63  ? 151.942 154.069 115.208 1.00 145.30 ?  63   ILE   A CD1   1 
ATOM   463   N  N     . LYS   A 1 64  ? 149.855 153.179 110.184 1.00 141.85 ?  64   LYS   A N     1 
ATOM   464   C  CA    . LYS   A 1 64  ? 149.071 152.365 109.263 1.00 141.17 ?  64   LYS   A CA    1 
ATOM   465   C  C     . LYS   A 1 64  ? 149.691 152.357 107.872 1.00 141.22 ?  64   LYS   A C     1 
ATOM   466   O  O     . LYS   A 1 64  ? 149.745 151.312 107.215 1.00 141.89 ?  64   LYS   A O     1 
ATOM   467   C  CB    . LYS   A 1 64  ? 147.632 152.876 109.207 1.00 140.72 ?  64   LYS   A CB    1 
ATOM   468   C  CG    . LYS   A 1 64  ? 146.645 151.883 108.622 1.00 140.88 ?  64   LYS   A CG    1 
ATOM   469   C  CD    . LYS   A 1 64  ? 145.226 152.195 109.059 1.00 141.56 ?  64   LYS   A CD    1 
ATOM   470   C  CE    . LYS   A 1 64  ? 144.231 151.875 107.957 1.00 140.98 ?  64   LYS   A CE    1 
ATOM   471   N  NZ    . LYS   A 1 64  ? 144.852 151.066 106.872 1.00 140.85 ?  64   LYS   A NZ    1 
ATOM   472   N  N     . ALA   A 1 65  ? 150.161 153.516 107.406 1.00 141.02 ?  65   ALA   A N     1 
ATOM   473   C  CA    . ALA   A 1 65  ? 150.828 153.571 106.108 1.00 139.62 ?  65   ALA   A CA    1 
ATOM   474   C  C     . ALA   A 1 65  ? 152.104 152.735 106.107 1.00 139.31 ?  65   ALA   A C     1 
ATOM   475   O  O     . ALA   A 1 65  ? 152.358 151.971 105.165 1.00 140.71 ?  65   ALA   A O     1 
ATOM   476   C  CB    . ALA   A 1 65  ? 151.135 155.021 105.736 1.00 140.58 ?  65   ALA   A CB    1 
ATOM   477   N  N     . ALA   A 1 66  ? 152.911 152.855 107.165 1.00 138.69 ?  66   ALA   A N     1 
ATOM   478   C  CA    . ALA   A 1 66  ? 154.142 152.073 107.242 1.00 139.52 ?  66   ALA   A CA    1 
ATOM   479   C  C     . ALA   A 1 66  ? 153.846 150.578 107.271 1.00 139.97 ?  66   ALA   A C     1 
ATOM   480   O  O     . ALA   A 1 66  ? 154.565 149.783 106.654 1.00 139.69 ?  66   ALA   A O     1 
ATOM   481   C  CB    . ALA   A 1 66  ? 154.952 152.489 108.469 1.00 138.45 ?  66   ALA   A CB    1 
ATOM   482   N  N     . ALA   A 1 67  ? 152.795 150.176 107.989 1.00 135.08 ?  67   ALA   A N     1 
ATOM   483   C  CA    . ALA   A 1 67  ? 152.398 148.772 108.012 1.00 132.75 ?  67   ALA   A CA    1 
ATOM   484   C  C     . ALA   A 1 67  ? 151.928 148.304 106.641 1.00 134.04 ?  67   ALA   A C     1 
ATOM   485   O  O     . ALA   A 1 67  ? 152.267 147.198 106.206 1.00 135.09 ?  67   ALA   A O     1 
ATOM   486   C  CB    . ALA   A 1 67  ? 151.304 148.555 109.055 1.00 130.68 ?  67   ALA   A CB    1 
ATOM   487   N  N     . ASP   A 1 68  ? 151.143 149.130 105.946 1.00 140.19 ?  68   ASP   A N     1 
ATOM   488   C  CA    . ASP   A 1 68  ? 150.675 148.769 104.614 1.00 139.49 ?  68   ASP   A CA    1 
ATOM   489   C  C     . ASP   A 1 68  ? 151.802 148.753 103.592 1.00 138.09 ?  68   ASP   A C     1 
ATOM   490   O  O     . ASP   A 1 68  ? 151.629 148.191 102.506 1.00 137.50 ?  68   ASP   A O     1 
ATOM   491   C  CB    . ASP   A 1 68  ? 149.574 149.730 104.163 1.00 139.87 ?  68   ASP   A CB    1 
ATOM   492   C  CG    . ASP   A 1 68  ? 148.255 149.471 104.862 1.00 141.29 ?  68   ASP   A CG    1 
ATOM   493   O  OD1   . ASP   A 1 68  ? 148.277 149.017 106.026 1.00 140.52 ?  68   ASP   A OD1   1 
ATOM   494   O  OD2   . ASP   A 1 68  ? 147.195 149.720 104.249 1.00 142.12 ?  68   ASP   A OD2   1 
ATOM   495   N  N     . LEU   A 1 69  ? 152.950 149.350 103.914 1.00 137.89 ?  69   LEU   A N     1 
ATOM   496   C  CA    . LEU   A 1 69  ? 154.114 149.311 103.040 1.00 136.51 ?  69   LEU   A CA    1 
ATOM   497   C  C     . LEU   A 1 69  ? 154.974 148.065 103.250 1.00 138.25 ?  69   LEU   A C     1 
ATOM   498   O  O     . LEU   A 1 69  ? 156.167 148.087 102.928 1.00 139.41 ?  69   LEU   A O     1 
ATOM   499   C  CB    . LEU   A 1 69  ? 154.962 150.569 103.236 1.00 136.97 ?  69   LEU   A CB    1 
ATOM   500   C  CG    . LEU   A 1 69  ? 155.084 151.484 102.017 1.00 138.55 ?  69   LEU   A CG    1 
ATOM   501   C  CD1   . LEU   A 1 69  ? 156.030 152.637 102.296 1.00 138.85 ?  69   LEU   A CD1   1 
ATOM   502   C  CD2   . LEU   A 1 69  ? 155.541 150.697 100.797 1.00 138.23 ?  69   LEU   A CD2   1 
ATOM   503   N  N     . ILE   A 1 70  ? 154.399 146.985 103.776 1.00 138.89 ?  70   ILE   A N     1 
ATOM   504   C  CA    . ILE   A 1 70  ? 155.126 145.749 104.050 1.00 138.03 ?  70   ILE   A CA    1 
ATOM   505   C  C     . ILE   A 1 70  ? 154.808 144.741 102.955 1.00 136.30 ?  70   ILE   A C     1 
ATOM   506   O  O     . ILE   A 1 70  ? 153.637 144.530 102.616 1.00 136.59 ?  70   ILE   A O     1 
ATOM   507   C  CB    . ILE   A 1 70  ? 154.763 145.185 105.435 1.00 138.74 ?  70   ILE   A CB    1 
ATOM   508   C  CG1   . ILE   A 1 70  ? 155.349 146.058 106.544 1.00 138.44 ?  70   ILE   A CG1   1 
ATOM   509   C  CG2   . ILE   A 1 70  ? 155.254 143.752 105.578 1.00 135.12 ?  70   ILE   A CG2   1 
ATOM   510   C  CD1   . ILE   A 1 70  ? 154.682 145.857 107.888 1.00 136.36 ?  70   ILE   A CD1   1 
ATOM   511   N  N     . SER   A 1 71  ? 155.845 144.120 102.399 1.00 132.14 ?  71   SER   A N     1 
ATOM   512   C  CA    . SER   A 1 71  ? 155.676 143.110 101.363 1.00 132.38 ?  71   SER   A CA    1 
ATOM   513   C  C     . SER   A 1 71  ? 156.931 142.246 101.321 1.00 132.38 ?  71   SER   A C     1 
ATOM   514   O  O     . SER   A 1 71  ? 157.886 142.465 102.071 1.00 132.00 ?  71   SER   A O     1 
ATOM   515   C  CB    . SER   A 1 71  ? 155.393 143.753 100.002 1.00 133.32 ?  71   SER   A CB    1 
ATOM   516   O  OG    . SER   A 1 71  ? 155.275 142.769 98.990  1.00 133.73 ?  71   SER   A OG    1 
ATOM   517   N  N     . ARG   A 1 72  ? 156.915 141.248 100.434 1.00 128.86 ?  72   ARG   A N     1 
ATOM   518   C  CA    . ARG   A 1 72  ? 158.080 140.384 100.271 1.00 128.35 ?  72   ARG   A CA    1 
ATOM   519   C  C     . ARG   A 1 72  ? 159.272 141.162 99.730  1.00 130.84 ?  72   ARG   A C     1 
ATOM   520   O  O     . ARG   A 1 72  ? 160.417 140.902 100.117 1.00 131.15 ?  72   ARG   A O     1 
ATOM   521   C  CB    . ARG   A 1 72  ? 157.744 139.213 99.348  1.00 126.86 ?  72   ARG   A CB    1 
ATOM   522   C  CG    . ARG   A 1 72  ? 156.372 138.606 99.578  1.00 126.85 ?  72   ARG   A CG    1 
ATOM   523   C  CD    . ARG   A 1 72  ? 156.299 137.190 99.029  1.00 128.00 ?  72   ARG   A CD    1 
ATOM   524   N  NE    . ARG   A 1 72  ? 157.256 136.972 97.952  1.00 129.59 ?  72   ARG   A NE    1 
ATOM   525   C  CZ    . ARG   A 1 72  ? 157.160 136.007 97.048  1.00 129.64 ?  72   ARG   A CZ    1 
ATOM   526   N  NH1   . ARG   A 1 72  ? 156.157 135.145 97.062  1.00 127.90 ?  72   ARG   A NH1   1 
ATOM   527   N  NH2   . ARG   A 1 72  ? 158.095 135.902 96.108  1.00 128.82 ?  72   ARG   A NH2   1 
ATOM   528   N  N     . ASP   A 1 73  ? 159.023 142.118 98.831  1.00 145.89 ?  73   ASP   A N     1 
ATOM   529   C  CA    . ASP   A 1 73  ? 160.112 142.899 98.254  1.00 145.77 ?  73   ASP   A CA    1 
ATOM   530   C  C     . ASP   A 1 73  ? 160.861 143.681 99.325  1.00 145.08 ?  73   ASP   A C     1 
ATOM   531   O  O     . ASP   A 1 73  ? 162.096 143.755 99.303  1.00 143.93 ?  73   ASP   A O     1 
ATOM   532   C  CB    . ASP   A 1 73  ? 159.568 143.845 97.184  1.00 144.45 ?  73   ASP   A CB    1 
ATOM   533   C  CG    . ASP   A 1 73  ? 159.592 143.233 95.798  1.00 145.67 ?  73   ASP   A CG    1 
ATOM   534   O  OD1   . ASP   A 1 73  ? 160.355 142.267 95.586  1.00 145.38 ?  73   ASP   A OD1   1 
ATOM   535   O  OD2   . ASP   A 1 73  ? 158.849 143.719 94.920  1.00 145.88 ?  73   ASP   A OD2   1 
ATOM   536   N  N     . ALA   A 1 74  ? 160.135 144.268 100.274 1.00 137.71 ?  74   ALA   A N     1 
ATOM   537   C  CA    . ALA   A 1 74  ? 160.723 145.055 101.356 1.00 136.78 ?  74   ALA   A CA    1 
ATOM   538   C  C     . ALA   A 1 74  ? 160.192 144.533 102.684 1.00 137.61 ?  74   ALA   A C     1 
ATOM   539   O  O     . ALA   A 1 74  ? 159.327 145.158 103.312 1.00 136.28 ?  74   ALA   A O     1 
ATOM   540   C  CB    . ALA   A 1 74  ? 160.423 146.544 101.184 1.00 137.08 ?  74   ALA   A CB    1 
ATOM   541   N  N     . PRO   A 1 75  ? 160.688 143.380 103.142 1.00 142.13 ?  75   PRO   A N     1 
ATOM   542   C  CA    . PRO   A 1 75  ? 160.235 142.865 104.443 1.00 142.29 ?  75   PRO   A CA    1 
ATOM   543   C  C     . PRO   A 1 75  ? 160.712 143.709 105.608 1.00 139.81 ?  75   PRO   A C     1 
ATOM   544   O  O     . PRO   A 1 75  ? 160.043 143.752 106.648 1.00 140.58 ?  75   PRO   A O     1 
ATOM   545   C  CB    . PRO   A 1 75  ? 160.823 141.446 104.497 1.00 141.45 ?  75   PRO   A CB    1 
ATOM   546   C  CG    . PRO   A 1 75  ? 161.714 141.302 103.287 1.00 139.31 ?  75   PRO   A CG    1 
ATOM   547   C  CD    . PRO   A 1 75  ? 161.829 142.623 102.605 1.00 139.68 ?  75   PRO   A CD    1 
ATOM   548   N  N     . ASP   A 1 76  ? 161.844 144.399 105.453 1.00 138.38 ?  76   ASP   A N     1 
ATOM   549   C  CA    . ASP   A 1 76  ? 162.407 145.199 106.532 1.00 138.28 ?  76   ASP   A CA    1 
ATOM   550   C  C     . ASP   A 1 76  ? 161.471 146.318 106.972 1.00 139.43 ?  76   ASP   A C     1 
ATOM   551   O  O     . ASP   A 1 76  ? 161.620 146.837 108.085 1.00 141.18 ?  76   ASP   A O     1 
ATOM   552   C  CB    . ASP   A 1 76  ? 163.757 145.763 106.089 1.00 139.69 ?  76   ASP   A CB    1 
ATOM   553   C  CG    . ASP   A 1 76  ? 164.411 146.609 107.151 1.00 141.32 ?  76   ASP   A CG    1 
ATOM   554   O  OD1   . ASP   A 1 76  ? 164.114 147.815 107.187 1.00 141.62 ?  76   ASP   A OD1   1 
ATOM   555   O  OD2   . ASP   A 1 76  ? 165.212 146.071 107.943 1.00 142.27 ?  76   ASP   A OD2   1 
ATOM   556   N  N     . TYR   A 1 77  ? 160.498 146.686 106.133 1.00 140.49 ?  77   TYR   A N     1 
ATOM   557   C  CA    . TYR   A 1 77  ? 159.497 147.669 106.534 1.00 140.75 ?  77   TYR   A CA    1 
ATOM   558   C  C     . TYR   A 1 77  ? 158.757 147.233 107.791 1.00 140.58 ?  77   TYR   A C     1 
ATOM   559   O  O     . TYR   A 1 77  ? 158.278 148.081 108.554 1.00 139.15 ?  77   TYR   A O     1 
ATOM   560   C  CB    . TYR   A 1 77  ? 158.505 147.900 105.393 1.00 140.77 ?  77   TYR   A CB    1 
ATOM   561   C  CG    . TYR   A 1 77  ? 158.765 149.151 104.586 1.00 141.47 ?  77   TYR   A CG    1 
ATOM   562   C  CD1   . TYR   A 1 77  ? 158.646 150.408 105.161 1.00 141.11 ?  77   TYR   A CD1   1 
ATOM   563   C  CD2   . TYR   A 1 77  ? 159.126 149.074 103.249 1.00 141.15 ?  77   TYR   A CD2   1 
ATOM   564   C  CE1   . TYR   A 1 77  ? 158.879 151.553 104.425 1.00 141.39 ?  77   TYR   A CE1   1 
ATOM   565   C  CE2   . TYR   A 1 77  ? 159.363 150.213 102.506 1.00 140.49 ?  77   TYR   A CE2   1 
ATOM   566   C  CZ    . TYR   A 1 77  ? 159.239 151.450 103.099 1.00 142.08 ?  77   TYR   A CZ    1 
ATOM   567   O  OH    . TYR   A 1 77  ? 159.474 152.587 102.361 1.00 144.56 ?  77   TYR   A OH    1 
ATOM   568   N  N     . GLN   A 1 78  ? 158.658 145.922 108.029 1.00 134.60 ?  78   GLN   A N     1 
ATOM   569   C  CA    . GLN   A 1 78  ? 157.994 145.434 109.231 1.00 132.81 ?  78   GLN   A CA    1 
ATOM   570   C  C     . GLN   A 1 78  ? 158.711 145.867 110.503 1.00 132.56 ?  78   GLN   A C     1 
ATOM   571   O  O     . GLN   A 1 78  ? 158.086 145.909 111.568 1.00 133.71 ?  78   GLN   A O     1 
ATOM   572   C  CB    . GLN   A 1 78  ? 157.870 143.909 109.182 1.00 131.65 ?  78   GLN   A CB    1 
ATOM   573   C  CG    . GLN   A 1 78  ? 159.082 143.155 109.702 1.00 131.35 ?  78   GLN   A CG    1 
ATOM   574   C  CD    . GLN   A 1 78  ? 159.083 141.700 109.281 1.00 131.64 ?  78   GLN   A CD    1 
ATOM   575   O  OE1   . GLN   A 1 78  ? 158.041 141.045 109.270 1.00 132.42 ?  78   GLN   A OE1   1 
ATOM   576   N  NE2   . GLN   A 1 78  ? 160.255 141.186 108.930 1.00 130.23 ?  78   GLN   A NE2   1 
ATOM   577   N  N     . TYR   A 1 79  ? 159.999 146.195 110.418 1.00 131.58 ?  79   TYR   A N     1 
ATOM   578   C  CA    . TYR   A 1 79  ? 160.733 146.705 111.566 1.00 130.76 ?  79   TYR   A CA    1 
ATOM   579   C  C     . TYR   A 1 79  ? 160.608 148.214 111.725 1.00 131.42 ?  79   TYR   A C     1 
ATOM   580   O  O     . TYR   A 1 79  ? 161.082 148.756 112.729 1.00 132.47 ?  79   TYR   A O     1 
ATOM   581   C  CB    . TYR   A 1 79  ? 162.212 146.321 111.462 1.00 129.12 ?  79   TYR   A CB    1 
ATOM   582   C  CG    . TYR   A 1 79  ? 162.466 144.844 111.648 1.00 130.63 ?  79   TYR   A CG    1 
ATOM   583   C  CD1   . TYR   A 1 79  ? 162.643 144.304 112.914 1.00 130.07 ?  79   TYR   A CD1   1 
ATOM   584   C  CD2   . TYR   A 1 79  ? 162.524 143.988 110.557 1.00 130.59 ?  79   TYR   A CD2   1 
ATOM   585   C  CE1   . TYR   A 1 79  ? 162.872 142.953 113.089 1.00 131.74 ?  79   TYR   A CE1   1 
ATOM   586   C  CE2   . TYR   A 1 79  ? 162.753 142.636 110.722 1.00 131.87 ?  79   TYR   A CE2   1 
ATOM   587   C  CZ    . TYR   A 1 79  ? 162.926 142.124 111.990 1.00 134.60 ?  79   TYR   A CZ    1 
ATOM   588   O  OH    . TYR   A 1 79  ? 163.154 140.778 112.158 1.00 135.35 ?  79   TYR   A OH    1 
ATOM   589   N  N     . LEU   A 1 80  ? 159.983 148.900 110.768 1.00 133.39 ?  80   LEU   A N     1 
ATOM   590   C  CA    . LEU   A 1 80  ? 159.799 150.346 110.849 1.00 134.30 ?  80   LEU   A CA    1 
ATOM   591   C  C     . LEU   A 1 80  ? 158.516 150.701 111.592 1.00 135.27 ?  80   LEU   A C     1 
ATOM   592   O  O     . LEU   A 1 80  ? 158.554 151.400 112.610 1.00 135.87 ?  80   LEU   A O     1 
ATOM   593   C  CB    . LEU   A 1 80  ? 159.790 150.953 109.441 1.00 135.24 ?  80   LEU   A CB    1 
ATOM   594   C  CG    . LEU   A 1 80  ? 159.329 152.406 109.322 1.00 135.18 ?  80   LEU   A CG    1 
ATOM   595   C  CD1   . LEU   A 1 80  ? 160.487 153.359 109.539 1.00 133.89 ?  80   LEU   A CD1   1 
ATOM   596   C  CD2   . LEU   A 1 80  ? 158.673 152.658 107.975 1.00 133.91 ?  80   LEU   A CD2   1 
ATOM   597   N  N     . ALA   A 1 81  ? 157.378 150.205 111.099 1.00 130.43 ?  81   ALA   A N     1 
ATOM   598   C  CA    . ALA   A 1 81  ? 156.092 150.539 111.701 1.00 129.17 ?  81   ALA   A CA    1 
ATOM   599   C  C     . ALA   A 1 81  ? 156.059 150.167 113.175 1.00 129.33 ?  81   ALA   A C     1 
ATOM   600   O  O     . ALA   A 1 81  ? 155.574 150.944 114.008 1.00 133.59 ?  81   ALA   A O     1 
ATOM   601   C  CB    . ALA   A 1 81  ? 154.964 149.838 110.946 1.00 129.84 ?  81   ALA   A CB    1 
ATOM   602   N  N     . ALA   A 1 82  ? 156.582 148.987 113.517 1.00 122.24 ?  82   ALA   A N     1 
ATOM   603   C  CA    . ALA   A 1 82  ? 156.682 148.589 114.917 1.00 122.43 ?  82   ALA   A CA    1 
ATOM   604   C  C     . ALA   A 1 82  ? 157.402 149.651 115.734 1.00 124.13 ?  82   ALA   A C     1 
ATOM   605   O  O     . ALA   A 1 82  ? 156.916 150.079 116.788 1.00 126.20 ?  82   ALA   A O     1 
ATOM   606   C  CB    . ALA   A 1 82  ? 157.411 147.251 115.025 1.00 122.33 ?  82   ALA   A CB    1 
ATOM   607   N  N     . ARG   A 1 83  ? 158.557 150.106 115.240 1.00 119.25 ?  83   ARG   A N     1 
ATOM   608   C  CA    . ARG   A 1 83  ? 159.300 151.149 115.936 1.00 118.58 ?  83   ARG   A CA    1 
ATOM   609   C  C     . ARG   A 1 83  ? 158.449 152.397 116.114 1.00 120.34 ?  83   ARG   A C     1 
ATOM   610   O  O     . ARG   A 1 83  ? 158.528 153.069 117.148 1.00 123.45 ?  83   ARG   A O     1 
ATOM   611   C  CB    . ARG   A 1 83  ? 160.583 151.469 115.175 1.00 118.61 ?  83   ARG   A CB    1 
ATOM   612   C  CG    . ARG   A 1 83  ? 161.728 150.536 115.507 1.00 116.73 ?  83   ARG   A CG    1 
ATOM   613   C  CD    . ARG   A 1 83  ? 163.069 151.191 115.231 1.00 117.84 ?  83   ARG   A CD    1 
ATOM   614   N  NE    . ARG   A 1 83  ? 164.174 150.240 115.271 1.00 118.95 ?  83   ARG   A NE    1 
ATOM   615   C  CZ    . ARG   A 1 83  ? 164.352 149.252 114.404 1.00 118.61 ?  83   ARG   A CZ    1 
ATOM   616   N  NH1   . ARG   A 1 83  ? 163.494 149.026 113.423 1.00 120.85 ?  83   ARG   A NH1   1 
ATOM   617   N  NH2   . ARG   A 1 83  ? 165.420 148.469 114.524 1.00 118.08 ?  83   ARG   A NH2   1 
ATOM   618   N  N     . LEU   A 1 84  ? 157.620 152.717 115.120 1.00 129.22 ?  84   LEU   A N     1 
ATOM   619   C  CA    . LEU   A 1 84  ? 156.658 153.799 115.288 1.00 129.20 ?  84   LEU   A CA    1 
ATOM   620   C  C     . LEU   A 1 84  ? 155.594 153.425 116.312 1.00 128.95 ?  84   LEU   A C     1 
ATOM   621   O  O     . LEU   A 1 84  ? 155.307 154.198 117.234 1.00 129.65 ?  84   LEU   A O     1 
ATOM   622   C  CB    . LEU   A 1 84  ? 156.019 154.139 113.944 1.00 129.77 ?  84   LEU   A CB    1 
ATOM   623   C  CG    . LEU   A 1 84  ? 156.957 154.658 112.860 1.00 129.74 ?  84   LEU   A CG    1 
ATOM   624   C  CD1   . LEU   A 1 84  ? 156.354 154.463 111.478 1.00 128.31 ?  84   LEU   A CD1   1 
ATOM   625   C  CD2   . LEU   A 1 84  ? 157.260 156.119 113.123 1.00 131.10 ?  84   LEU   A CD2   1 
ATOM   626   N  N     . ALA   A 1 85  ? 155.018 152.226 116.180 1.00 126.59 ?  85   ALA   A N     1 
ATOM   627   C  CA    . ALA   A 1 85  ? 153.934 151.825 117.070 1.00 125.06 ?  85   ALA   A CA    1 
ATOM   628   C  C     . ALA   A 1 85  ? 154.399 151.795 118.518 1.00 125.00 ?  85   ALA   A C     1 
ATOM   629   O  O     . ALA   A 1 85  ? 153.686 152.260 119.417 1.00 127.55 ?  85   ALA   A O     1 
ATOM   630   C  CB    . ALA   A 1 85  ? 153.385 150.462 116.650 1.00 123.21 ?  85   ALA   A CB    1 
ATOM   631   N  N     . ILE   A 1 86  ? 155.618 151.291 118.719 1.00 126.37 ?  86   ILE   A N     1 
ATOM   632   C  CA    . ILE   A 1 86  ? 156.213 151.270 120.082 1.00 127.63 ?  86   ILE   A CA    1 
ATOM   633   C  C     . ILE   A 1 86  ? 156.155 152.693 120.625 1.00 129.24 ?  86   ILE   A C     1 
ATOM   634   O  O     . ILE   A 1 86  ? 155.709 152.868 121.765 1.00 132.09 ?  86   ILE   A O     1 
ATOM   635   C  CB    . ILE   A 1 86  ? 157.659 150.745 120.034 1.00 126.45 ?  86   ILE   A CB    1 
ATOM   636   C  CG1   . ILE   A 1 86  ? 157.705 149.231 119.814 1.00 125.76 ?  86   ILE   A CG1   1 
ATOM   637   C  CG2   . ILE   A 1 86  ? 158.422 151.151 121.284 1.00 125.51 ?  86   ILE   A CG2   1 
ATOM   638   C  CD1   . ILE   A 1 86  ? 157.979 148.438 121.068 1.00 127.00 ?  86   ILE   A CD1   1 
ATOM   639   N  N     . PHE   A 1 87  ? 156.579 153.670 119.823 1.00 136.08 ?  87   PHE   A N     1 
ATOM   640   C  CA    . PHE   A 1 87  ? 156.565 155.061 120.257 1.00 134.67 ?  87   PHE   A CA    1 
ATOM   641   C  C     . PHE   A 1 87  ? 155.165 155.486 120.677 1.00 134.91 ?  87   PHE   A C     1 
ATOM   642   O  O     . PHE   A 1 87  ? 154.988 156.113 121.729 1.00 137.23 ?  87   PHE   A O     1 
ATOM   643   C  CB    . PHE   A 1 87  ? 157.091 155.962 119.141 1.00 135.05 ?  87   PHE   A CB    1 
ATOM   644   C  CG    . PHE   A 1 87  ? 158.518 155.688 118.761 1.00 137.27 ?  87   PHE   A CG    1 
ATOM   645   C  CD1   . PHE   A 1 87  ? 159.377 155.054 119.644 1.00 137.21 ?  87   PHE   A CD1   1 
ATOM   646   C  CD2   . PHE   A 1 87  ? 159.002 156.068 117.520 1.00 136.88 ?  87   PHE   A CD2   1 
ATOM   647   C  CE1   . PHE   A 1 87  ? 160.689 154.801 119.295 1.00 137.15 ?  87   PHE   A CE1   1 
ATOM   648   C  CE2   . PHE   A 1 87  ? 160.315 155.817 117.166 1.00 136.72 ?  87   PHE   A CE2   1 
ATOM   649   C  CZ    . PHE   A 1 87  ? 161.159 155.182 118.055 1.00 136.53 ?  87   PHE   A CZ    1 
ATOM   650   N  N     . HIS   A 1 88  ? 154.152 155.123 119.884 1.00 124.59 ?  88   HIS   A N     1 
ATOM   651   C  CA    . HIS   A 1 88  ? 152.779 155.434 120.263 1.00 124.13 ?  88   HIS   A CA    1 
ATOM   652   C  C     . HIS   A 1 88  ? 152.408 154.772 121.581 1.00 126.54 ?  88   HIS   A C     1 
ATOM   653   O  O     . HIS   A 1 88  ? 151.596 155.311 122.341 1.00 126.77 ?  88   HIS   A O     1 
ATOM   654   C  CB    . HIS   A 1 88  ? 151.813 155.003 119.161 1.00 125.20 ?  88   HIS   A CB    1 
ATOM   655   C  CG    . HIS   A 1 88  ? 150.477 155.674 119.233 1.00 126.95 ?  88   HIS   A CG    1 
ATOM   656   N  ND1   . HIS   A 1 88  ? 150.269 156.845 119.929 1.00 127.45 ?  88   HIS   A ND1   1 
ATOM   657   C  CD2   . HIS   A 1 88  ? 149.281 155.339 118.694 1.00 127.31 ?  88   HIS   A CD2   1 
ATOM   658   C  CE1   . HIS   A 1 88  ? 149.002 157.202 119.817 1.00 127.03 ?  88   HIS   A CE1   1 
ATOM   659   N  NE2   . HIS   A 1 88  ? 148.381 156.305 119.073 1.00 128.65 ?  88   HIS   A NE2   1 
ATOM   660   N  N     . LEU   A 1 89  ? 152.991 153.607 121.869 1.00 129.90 ?  89   LEU   A N     1 
ATOM   661   C  CA    . LEU   A 1 89  ? 152.779 152.973 123.162 1.00 126.96 ?  89   LEU   A CA    1 
ATOM   662   C  C     . LEU   A 1 89  ? 153.587 153.647 124.262 1.00 127.02 ?  89   LEU   A C     1 
ATOM   663   O  O     . LEU   A 1 89  ? 153.148 153.676 125.417 1.00 128.86 ?  89   LEU   A O     1 
ATOM   664   C  CB    . LEU   A 1 89  ? 153.133 151.488 123.084 1.00 124.05 ?  89   LEU   A CB    1 
ATOM   665   C  CG    . LEU   A 1 89  ? 152.411 150.679 122.005 1.00 125.05 ?  89   LEU   A CG    1 
ATOM   666   C  CD1   . LEU   A 1 89  ? 152.782 149.208 122.101 1.00 126.63 ?  89   LEU   A CD1   1 
ATOM   667   C  CD2   . LEU   A 1 89  ? 150.906 150.864 122.113 1.00 125.03 ?  89   LEU   A CD2   1 
ATOM   668   N  N     . ARG   A 1 90  ? 154.761 154.190 123.929 1.00 123.96 ?  90   ARG   A N     1 
ATOM   669   C  CA    . ARG   A 1 90  ? 155.610 154.786 124.955 1.00 121.26 ?  90   ARG   A CA    1 
ATOM   670   C  C     . ARG   A 1 90  ? 155.000 156.069 125.505 1.00 124.08 ?  90   ARG   A C     1 
ATOM   671   O  O     . ARG   A 1 90  ? 155.027 156.305 126.718 1.00 125.01 ?  90   ARG   A O     1 
ATOM   672   C  CB    . ARG   A 1 90  ? 157.006 155.049 124.392 1.00 119.54 ?  90   ARG   A CB    1 
ATOM   673   C  CG    . ARG   A 1 90  ? 157.884 153.811 124.324 1.00 120.41 ?  90   ARG   A CG    1 
ATOM   674   C  CD    . ARG   A 1 90  ? 159.113 153.954 125.205 1.00 121.10 ?  90   ARG   A CD    1 
ATOM   675   N  NE    . ARG   A 1 90  ? 160.133 152.963 124.887 1.00 123.40 ?  90   ARG   A NE    1 
ATOM   676   C  CZ    . ARG   A 1 90  ? 161.438 153.167 125.005 1.00 124.10 ?  90   ARG   A CZ    1 
ATOM   677   N  NH1   . ARG   A 1 90  ? 161.921 154.321 125.436 1.00 124.40 ?  90   ARG   A NH1   1 
ATOM   678   N  NH2   . ARG   A 1 90  ? 162.280 152.189 124.684 1.00 122.57 ?  90   ARG   A NH2   1 
ATOM   679   N  N     . LYS   A 1 91  ? 154.444 156.909 124.630 1.00 134.19 ?  91   LYS   A N     1 
ATOM   680   C  CA    . LYS   A 1 91  ? 153.846 158.160 125.081 1.00 134.39 ?  91   LYS   A CA    1 
ATOM   681   C  C     . LYS   A 1 91  ? 152.483 157.934 125.724 1.00 134.09 ?  91   LYS   A C     1 
ATOM   682   O  O     . LYS   A 1 91  ? 152.124 158.629 126.681 1.00 134.92 ?  91   LYS   A O     1 
ATOM   683   C  CB    . LYS   A 1 91  ? 153.729 159.136 123.910 1.00 134.36 ?  91   LYS   A CB    1 
ATOM   684   C  CG    . LYS   A 1 91  ? 153.352 160.551 124.318 1.00 134.77 ?  91   LYS   A CG    1 
ATOM   685   C  CD    . LYS   A 1 91  ? 154.579 161.360 124.701 1.00 133.48 ?  91   LYS   A CD    1 
ATOM   686   C  CE    . LYS   A 1 91  ? 154.283 162.850 124.689 1.00 134.96 ?  91   LYS   A CE    1 
ATOM   687   N  NZ    . LYS   A 1 91  ? 155.411 163.644 125.252 1.00 135.47 ?  91   LYS   A NZ    1 
ATOM   688   N  N     . LYS   A 1 92  ? 151.712 156.970 125.214 1.00 121.87 ?  92   LYS   A N     1 
ATOM   689   C  CA    . LYS   A 1 92  ? 150.379 156.720 125.749 1.00 122.22 ?  92   LYS   A CA    1 
ATOM   690   C  C     . LYS   A 1 92  ? 150.411 156.157 127.164 1.00 123.74 ?  92   LYS   A C     1 
ATOM   691   O  O     . LYS   A 1 92  ? 149.413 156.270 127.883 1.00 123.71 ?  92   LYS   A O     1 
ATOM   692   C  CB    . LYS   A 1 92  ? 149.614 155.766 124.832 1.00 123.60 ?  92   LYS   A CB    1 
ATOM   693   C  CG    . LYS   A 1 92  ? 148.603 156.450 123.927 1.00 123.76 ?  92   LYS   A CG    1 
ATOM   694   C  CD    . LYS   A 1 92  ? 148.233 155.574 122.738 1.00 124.13 ?  92   LYS   A CD    1 
ATOM   695   C  CE    . LYS   A 1 92  ? 148.025 154.126 123.151 1.00 125.25 ?  92   LYS   A CE    1 
ATOM   696   N  NZ    . LYS   A 1 92  ? 146.851 153.967 124.053 1.00 125.87 ?  92   LYS   A NZ    1 
ATOM   697   N  N     . ALA   A 1 93  ? 151.525 155.557 127.579 1.00 124.78 ?  93   ALA   A N     1 
ATOM   698   C  CA    . ALA   A 1 93  ? 151.629 154.962 128.904 1.00 124.10 ?  93   ALA   A CA    1 
ATOM   699   C  C     . ALA   A 1 93  ? 152.382 155.829 129.900 1.00 123.28 ?  93   ALA   A C     1 
ATOM   700   O  O     . ALA   A 1 93  ? 152.069 155.791 131.094 1.00 124.01 ?  93   ALA   A O     1 
ATOM   701   C  CB    . ALA   A 1 93  ? 152.313 153.593 128.818 1.00 122.77 ?  93   ALA   A CB    1 
ATOM   702   N  N     . TYR   A 1 94  ? 153.364 156.608 129.443 1.00 125.07 ?  94   TYR   A N     1 
ATOM   703   C  CA    . TYR   A 1 94  ? 154.181 157.417 130.335 1.00 125.87 ?  94   TYR   A CA    1 
ATOM   704   C  C     . TYR   A 1 94  ? 154.004 158.915 130.147 1.00 127.30 ?  94   TYR   A C     1 
ATOM   705   O  O     . TYR   A 1 94  ? 154.309 159.673 131.073 1.00 128.74 ?  94   TYR   A O     1 
ATOM   706   C  CB    . TYR   A 1 94  ? 155.668 157.075 130.153 1.00 123.57 ?  94   TYR   A CB    1 
ATOM   707   C  CG    . TYR   A 1 94  ? 155.983 155.601 130.266 1.00 125.79 ?  94   TYR   A CG    1 
ATOM   708   C  CD1   . TYR   A 1 94  ? 155.321 154.798 131.185 1.00 127.58 ?  94   TYR   A CD1   1 
ATOM   709   C  CD2   . TYR   A 1 94  ? 156.941 155.012 129.453 1.00 126.61 ?  94   TYR   A CD2   1 
ATOM   710   C  CE1   . TYR   A 1 94  ? 155.605 153.452 131.291 1.00 126.37 ?  94   TYR   A CE1   1 
ATOM   711   C  CE2   . TYR   A 1 94  ? 157.231 153.666 129.552 1.00 126.42 ?  94   TYR   A CE2   1 
ATOM   712   C  CZ    . TYR   A 1 94  ? 156.561 152.891 130.473 1.00 125.93 ?  94   TYR   A CZ    1 
ATOM   713   O  OH    . TYR   A 1 94  ? 156.846 151.550 130.576 1.00 123.68 ?  94   TYR   A OH    1 
ATOM   714   N  N     . GLY   A 1 95  ? 153.520 159.359 128.990 1.00 138.17 ?  95   GLY   A N     1 
ATOM   715   C  CA    . GLY   A 1 95  ? 153.494 160.771 128.678 1.00 138.43 ?  95   GLY   A CA    1 
ATOM   716   C  C     . GLY   A 1 95  ? 154.803 161.319 128.174 1.00 140.05 ?  95   GLY   A C     1 
ATOM   717   O  O     . GLY   A 1 95  ? 154.898 162.524 127.903 1.00 140.79 ?  95   GLY   A O     1 
ATOM   718   N  N     . GLN   A 1 96  ? 155.811 160.476 128.011 1.00 136.80 ?  96   GLN   A N     1 
ATOM   719   C  CA    . GLN   A 1 96  ? 157.048 160.916 127.387 1.00 135.46 ?  96   GLN   A CA    1 
ATOM   720   C  C     . GLN   A 1 96  ? 157.594 159.746 126.609 1.00 136.61 ?  96   GLN   A C     1 
ATOM   721   O  O     . GLN   A 1 96  ? 156.916 158.731 126.449 1.00 136.86 ?  96   GLN   A O     1 
ATOM   722   C  CB    . GLN   A 1 96  ? 158.083 161.397 128.401 1.00 133.61 ?  96   GLN   A CB    1 
ATOM   723   C  CG    . GLN   A 1 96  ? 157.910 160.831 129.783 1.00 134.40 ?  96   GLN   A CG    1 
ATOM   724   C  CD    . GLN   A 1 96  ? 158.973 161.356 130.704 1.00 135.81 ?  96   GLN   A CD    1 
ATOM   725   O  OE1   . GLN   A 1 96  ? 160.147 161.020 130.575 1.00 136.43 ?  96   GLN   A OE1   1 
ATOM   726   N  NE2   . GLN   A 1 96  ? 158.569 162.186 131.649 1.00 135.41 ?  96   GLN   A NE2   1 
ATOM   727   N  N     . PHE   A 1 97  ? 158.823 159.887 126.125 1.00 142.01 ?  97   PHE   A N     1 
ATOM   728   C  CA    . PHE   A 1 97  ? 159.478 158.774 125.459 1.00 141.65 ?  97   PHE   A CA    1 
ATOM   729   C  C     . PHE   A 1 97  ? 160.284 157.929 126.440 1.00 142.40 ?  97   PHE   A C     1 
ATOM   730   O  O     . PHE   A 1 97  ? 160.132 156.704 126.480 1.00 143.46 ?  97   PHE   A O     1 
ATOM   731   C  CB    . PHE   A 1 97  ? 160.380 159.282 124.334 1.00 142.86 ?  97   PHE   A CB    1 
ATOM   732   C  CG    . PHE   A 1 97  ? 161.331 158.244 123.807 1.00 144.23 ?  97   PHE   A CG    1 
ATOM   733   C  CD1   . PHE   A 1 97  ? 160.894 157.264 122.930 1.00 144.79 ?  97   PHE   A CD1   1 
ATOM   734   C  CD2   . PHE   A 1 97  ? 162.661 158.245 124.191 1.00 142.93 ?  97   PHE   A CD2   1 
ATOM   735   C  CE1   . PHE   A 1 97  ? 161.769 156.308 122.445 1.00 143.93 ?  97   PHE   A CE1   1 
ATOM   736   C  CE2   . PHE   A 1 97  ? 163.537 157.292 123.712 1.00 142.20 ?  97   PHE   A CE2   1 
ATOM   737   C  CZ    . PHE   A 1 97  ? 163.091 156.323 122.837 1.00 142.72 ?  97   PHE   A CZ    1 
ATOM   738   N  N     . GLU   A 1 98  ? 161.136 158.559 127.237 1.00 142.99 ?  98   GLU   A N     1 
ATOM   739   C  CA    . GLU   A 1 98  ? 162.002 157.798 128.131 1.00 142.88 ?  98   GLU   A CA    1 
ATOM   740   C  C     . GLU   A 1 98  ? 161.192 157.256 129.305 1.00 144.54 ?  98   GLU   A C     1 
ATOM   741   O  O     . GLU   A 1 98  ? 160.489 158.020 129.978 1.00 145.88 ?  98   GLU   A O     1 
ATOM   742   C  CB    . GLU   A 1 98  ? 163.183 158.647 128.622 1.00 142.80 ?  98   GLU   A CB    1 
ATOM   743   C  CG    . GLU   A 1 98  ? 164.201 157.940 129.509 1.00 144.58 ?  98   GLU   A CG    1 
ATOM   744   C  CD    . GLU   A 1 98  ? 165.357 158.835 129.909 1.00 145.83 ?  98   GLU   A CD    1 
ATOM   745   O  OE1   . GLU   A 1 98  ? 165.353 160.021 129.529 1.00 145.26 ?  98   GLU   A OE1   1 
ATOM   746   O  OE2   . GLU   A 1 98  ? 166.273 158.351 130.602 1.00 145.40 ?  98   GLU   A OE2   1 
ATOM   747   N  N     . PRO   A 1 99  ? 161.232 155.946 129.557 1.00 127.41 ?  99   PRO   A N     1 
ATOM   748   C  CA    . PRO   A 1 99  ? 160.483 155.400 130.684 1.00 125.72 ?  99   PRO   A CA    1 
ATOM   749   C  C     . PRO   A 1 99  ? 161.058 155.887 132.001 1.00 126.17 ?  99   PRO   A C     1 
ATOM   750   O  O     . PRO   A 1 99  ? 162.265 156.166 132.103 1.00 123.34 ?  99   PRO   A O     1 
ATOM   751   C  CB    . PRO   A 1 99  ? 160.660 153.879 130.522 1.00 124.72 ?  99   PRO   A CB    1 
ATOM   752   C  CG    . PRO   A 1 99  ? 161.033 153.691 129.084 1.00 124.04 ?  99   PRO   A CG    1 
ATOM   753   C  CD    . PRO   A 1 99  ? 161.857 154.890 128.746 1.00 124.59 ?  99   PRO   A CD    1 
ATOM   754   N  N     . PRO   A 1 100 ? 160.232 156.001 133.042 1.00 125.18 ?  100  PRO   A N     1 
ATOM   755   C  CA    . PRO   A 1 100 ? 160.739 156.469 134.338 1.00 124.61 ?  100  PRO   A CA    1 
ATOM   756   C  C     . PRO   A 1 100 ? 161.552 155.407 135.059 1.00 124.12 ?  100  PRO   A C     1 
ATOM   757   O  O     . PRO   A 1 100 ? 161.809 154.331 134.510 1.00 125.29 ?  100  PRO   A O     1 
ATOM   758   C  CB    . PRO   A 1 100 ? 159.459 156.813 135.106 1.00 123.17 ?  100  PRO   A CB    1 
ATOM   759   C  CG    . PRO   A 1 100 ? 158.435 155.891 134.534 1.00 121.54 ?  100  PRO   A CG    1 
ATOM   760   C  CD    . PRO   A 1 100 ? 158.786 155.721 133.078 1.00 121.40 ?  100  PRO   A CD    1 
ATOM   761   N  N     . ALA   A 1 101 ? 161.965 155.703 136.288 1.00 121.95 ?  101  ALA   A N     1 
ATOM   762   C  CA    . ALA   A 1 101 ? 162.684 154.726 137.090 1.00 120.54 ?  101  ALA   A CA    1 
ATOM   763   C  C     . ALA   A 1 101 ? 161.783 153.539 137.411 1.00 121.92 ?  101  ALA   A C     1 
ATOM   764   O  O     . ALA   A 1 101 ? 160.561 153.669 137.525 1.00 121.22 ?  101  ALA   A O     1 
ATOM   765   C  CB    . ALA   A 1 101 ? 163.195 155.363 138.381 1.00 119.75 ?  101  ALA   A CB    1 
ATOM   766   N  N     . LEU   A 1 102 ? 162.404 152.364 137.547 1.00 125.13 ?  102  LEU   A N     1 
ATOM   767   C  CA    . LEU   A 1 102 ? 161.634 151.141 137.748 1.00 125.52 ?  102  LEU   A CA    1 
ATOM   768   C  C     . LEU   A 1 102 ? 160.856 151.176 139.058 1.00 125.47 ?  102  LEU   A C     1 
ATOM   769   O  O     . LEU   A 1 102 ? 159.698 150.747 139.109 1.00 127.00 ?  102  LEU   A O     1 
ATOM   770   C  CB    . LEU   A 1 102 ? 162.557 149.924 137.705 1.00 124.05 ?  102  LEU   A CB    1 
ATOM   771   C  CG    . LEU   A 1 102 ? 161.869 148.558 137.750 1.00 123.69 ?  102  LEU   A CG    1 
ATOM   772   C  CD1   . LEU   A 1 102 ? 160.675 148.517 136.809 1.00 122.98 ?  102  LEU   A CD1   1 
ATOM   773   C  CD2   . LEU   A 1 102 ? 162.851 147.457 137.409 1.00 123.31 ?  102  LEU   A CD2   1 
ATOM   774   N  N     . TYR   A 1 103 ? 161.475 151.678 140.130 1.00 120.03 ?  103  TYR   A N     1 
ATOM   775   C  CA    . TYR   A 1 103 ? 160.804 151.681 141.427 1.00 119.77 ?  103  TYR   A CA    1 
ATOM   776   C  C     . TYR   A 1 103 ? 159.570 152.575 141.416 1.00 120.23 ?  103  TYR   A C     1 
ATOM   777   O  O     . TYR   A 1 103 ? 158.524 152.205 141.964 1.00 121.25 ?  103  TYR   A O     1 
ATOM   778   C  CB    . TYR   A 1 103 ? 161.771 152.123 142.526 1.00 119.11 ?  103  TYR   A CB    1 
ATOM   779   C  CG    . TYR   A 1 103 ? 161.168 152.068 143.913 1.00 121.80 ?  103  TYR   A CG    1 
ATOM   780   C  CD1   . TYR   A 1 103 ? 161.026 150.860 144.581 1.00 122.55 ?  103  TYR   A CD1   1 
ATOM   781   C  CD2   . TYR   A 1 103 ? 160.738 153.224 144.551 1.00 120.89 ?  103  TYR   A CD2   1 
ATOM   782   C  CE1   . TYR   A 1 103 ? 160.472 150.804 145.845 1.00 121.56 ?  103  TYR   A CE1   1 
ATOM   783   C  CE2   . TYR   A 1 103 ? 160.181 153.177 145.814 1.00 121.55 ?  103  TYR   A CE2   1 
ATOM   784   C  CZ    . TYR   A 1 103 ? 160.052 151.964 146.457 1.00 121.76 ?  103  TYR   A CZ    1 
ATOM   785   O  OH    . TYR   A 1 103 ? 159.501 151.913 147.716 1.00 121.44 ?  103  TYR   A OH    1 
ATOM   786   N  N     . ASP   A 1 104 ? 159.675 153.762 140.816 1.00 122.66 ?  104  ASP   A N     1 
ATOM   787   C  CA    . ASP   A 1 104 ? 158.530 154.665 140.765 1.00 124.07 ?  104  ASP   A CA    1 
ATOM   788   C  C     . ASP   A 1 104 ? 157.383 154.057 139.964 1.00 125.39 ?  104  ASP   A C     1 
ATOM   789   O  O     . ASP   A 1 104 ? 156.224 154.110 140.386 1.00 125.45 ?  104  ASP   A O     1 
ATOM   790   C  CB    . ASP   A 1 104 ? 158.948 156.011 140.175 1.00 124.54 ?  104  ASP   A CB    1 
ATOM   791   C  CG    . ASP   A 1 104 ? 160.134 156.619 140.897 1.00 126.55 ?  104  ASP   A CG    1 
ATOM   792   O  OD1   . ASP   A 1 104 ? 161.206 155.980 140.923 1.00 125.32 ?  104  ASP   A OD1   1 
ATOM   793   O  OD2   . ASP   A 1 104 ? 159.994 157.734 141.440 1.00 126.64 ?  104  ASP   A OD2   1 
ATOM   794   N  N     . HIS   A 1 105 ? 157.690 153.474 138.796 1.00 123.45 ?  105  HIS   A N     1 
ATOM   795   C  CA    . HIS   A 1 105 ? 156.685 152.761 138.001 1.00 121.75 ?  105  HIS   A CA    1 
ATOM   796   C  C     . HIS   A 1 105 ? 156.045 151.629 138.778 1.00 119.70 ?  105  HIS   A C     1 
ATOM   797   O  O     . HIS   A 1 105 ? 154.830 151.447 138.715 1.00 119.64 ?  105  HIS   A O     1 
ATOM   798   C  CB    . HIS   A 1 105 ? 157.300 152.191 136.725 1.00 118.70 ?  105  HIS   A CB    1 
ATOM   799   C  CG    . HIS   A 1 105 ? 156.355 151.366 135.920 1.00 120.82 ?  105  HIS   A CG    1 
ATOM   800   N  ND1   . HIS   A 1 105 ? 155.502 151.922 134.997 1.00 122.30 ?  105  HIS   A ND1   1 
ATOM   801   C  CD2   . HIS   A 1 105 ? 156.133 150.032 135.888 1.00 121.35 ?  105  HIS   A CD2   1 
ATOM   802   C  CE1   . HIS   A 1 105 ? 154.789 150.967 134.432 1.00 121.72 ?  105  HIS   A CE1   1 
ATOM   803   N  NE2   . HIS   A 1 105 ? 155.149 149.811 134.958 1.00 120.75 ?  105  HIS   A NE2   1 
ATOM   804   N  N     . VAL   A 1 106 ? 156.840 150.861 139.519 1.00 111.28 ?  106  VAL   A N     1 
ATOM   805   C  CA    . VAL   A 1 106 ? 156.309 149.720 140.255 1.00 110.51 ?  106  VAL   A CA    1 
ATOM   806   C  C     . VAL   A 1 106 ? 155.371 150.185 141.361 1.00 114.49 ?  106  VAL   A C     1 
ATOM   807   O  O     . VAL   A 1 106 ? 154.256 149.670 141.507 1.00 115.49 ?  106  VAL   A O     1 
ATOM   808   C  CB    . VAL   A 1 106 ? 157.461 148.866 140.814 1.00 110.95 ?  106  VAL   A CB    1 
ATOM   809   C  CG1   . VAL   A 1 106 ? 156.972 147.994 141.959 1.00 112.86 ?  106  VAL   A CG1   1 
ATOM   810   C  CG2   . VAL   A 1 106 ? 158.065 148.012 139.714 1.00 112.20 ?  106  VAL   A CG2   1 
ATOM   811   N  N     . VAL   A 1 107 ? 155.807 151.166 142.158 1.00 121.05 ?  107  VAL   A N     1 
ATOM   812   C  CA    . VAL   A 1 107 ? 154.958 151.643 143.247 1.00 120.07 ?  107  VAL   A CA    1 
ATOM   813   C  C     . VAL   A 1 107 ? 153.704 152.303 142.695 1.00 117.61 ?  107  VAL   A C     1 
ATOM   814   O  O     . VAL   A 1 107 ? 152.623 152.180 143.282 1.00 117.04 ?  107  VAL   A O     1 
ATOM   815   C  CB    . VAL   A 1 107 ? 155.734 152.582 144.191 1.00 118.07 ?  107  VAL   A CB    1 
ATOM   816   C  CG1   . VAL   A 1 107 ? 156.963 151.882 144.726 1.00 117.02 ?  107  VAL   A CG1   1 
ATOM   817   C  CG2   . VAL   A 1 107 ? 156.110 153.880 143.500 1.00 118.14 ?  107  VAL   A CG2   1 
ATOM   818   N  N     . LYS   A 1 108 ? 153.807 152.987 141.554 1.00 116.14 ?  108  LYS   A N     1 
ATOM   819   C  CA    . LYS   A 1 108 ? 152.616 153.502 140.898 1.00 117.76 ?  108  LYS   A CA    1 
ATOM   820   C  C     . LYS   A 1 108 ? 151.644 152.368 140.596 1.00 119.93 ?  108  LYS   A C     1 
ATOM   821   O  O     . LYS   A 1 108 ? 150.549 152.295 141.174 1.00 121.74 ?  108  LYS   A O     1 
ATOM   822   C  CB    . LYS   A 1 108 ? 153.022 154.252 139.625 1.00 118.44 ?  108  LYS   A CB    1 
ATOM   823   C  CG    . LYS   A 1 108 ? 151.958 155.165 139.043 1.00 118.36 ?  108  LYS   A CG    1 
ATOM   824   C  CD    . LYS   A 1 108 ? 152.367 155.703 137.677 1.00 118.08 ?  108  LYS   A CD    1 
ATOM   825   C  CE    . LYS   A 1 108 ? 151.210 156.432 137.007 1.00 117.25 ?  108  LYS   A CE    1 
ATOM   826   N  NZ    . LYS   A 1 108 ? 151.603 157.056 135.713 1.00 117.59 ?  108  LYS   A NZ    1 
ATOM   827   N  N     . MET   A 1 109 ? 152.054 151.434 139.727 1.00 122.23 ?  109  MET   A N     1 
ATOM   828   C  CA    . MET   A 1 109 ? 151.148 150.369 139.300 1.00 120.87 ?  109  MET   A CA    1 
ATOM   829   C  C     . MET   A 1 109 ? 150.618 149.562 140.478 1.00 120.40 ?  109  MET   A C     1 
ATOM   830   O  O     . MET   A 1 109 ? 149.536 148.972 140.387 1.00 121.10 ?  109  MET   A O     1 
ATOM   831   C  CB    . MET   A 1 109 ? 151.836 149.452 138.290 1.00 119.91 ?  109  MET   A CB    1 
ATOM   832   C  CG    . MET   A 1 109 ? 152.661 150.166 137.230 1.00 121.50 ?  109  MET   A CG    1 
ATOM   833   S  SD    . MET   A 1 109 ? 151.720 151.060 135.977 1.00 128.32 ?  109  MET   A SD    1 
ATOM   834   C  CE    . MET   A 1 109 ? 150.153 150.197 136.012 1.00 122.10 ?  109  MET   A CE    1 
ATOM   835   N  N     . VAL   A 1 110 ? 151.356 149.523 141.587 1.00 113.31 ?  110  VAL   A N     1 
ATOM   836   C  CA    . VAL   A 1 110 ? 150.803 148.952 142.809 1.00 112.24 ?  110  VAL   A CA    1 
ATOM   837   C  C     . VAL   A 1 110 ? 149.709 149.854 143.369 1.00 115.64 ?  110  VAL   A C     1 
ATOM   838   O  O     . VAL   A 1 110 ? 148.688 149.372 143.875 1.00 114.95 ?  110  VAL   A O     1 
ATOM   839   C  CB    . VAL   A 1 110 ? 151.925 148.702 143.831 1.00 112.21 ?  110  VAL   A CB    1 
ATOM   840   C  CG1   . VAL   A 1 110 ? 151.345 148.414 145.203 1.00 112.83 ?  110  VAL   A CG1   1 
ATOM   841   C  CG2   . VAL   A 1 110 ? 152.798 147.551 143.367 1.00 112.65 ?  110  VAL   A CG2   1 
ATOM   842   N  N     . GLU   A 1 111 ? 149.898 151.175 143.281 1.00 127.81 ?  111  GLU   A N     1 
ATOM   843   C  CA    . GLU   A 1 111 ? 148.867 152.097 143.750 1.00 125.60 ?  111  GLU   A CA    1 
ATOM   844   C  C     . GLU   A 1 111 ? 147.552 151.885 143.005 1.00 127.04 ?  111  GLU   A C     1 
ATOM   845   O  O     . GLU   A 1 111 ? 146.497 151.759 143.634 1.00 127.24 ?  111  GLU   A O     1 
ATOM   846   C  CB    . GLU   A 1 111 ? 149.332 153.550 143.622 1.00 125.36 ?  111  GLU   A CB    1 
ATOM   847   C  CG    . GLU   A 1 111 ? 148.216 154.582 143.792 1.00 128.27 ?  111  GLU   A CG    1 
ATOM   848   C  CD    . GLU   A 1 111 ? 147.554 154.532 145.160 1.00 131.33 ?  111  GLU   A CD    1 
ATOM   849   O  OE1   . GLU   A 1 111 ? 148.177 154.028 146.119 1.00 130.89 ?  111  GLU   A OE1   1 
ATOM   850   O  OE2   . GLU   A 1 111 ? 146.404 155.005 145.276 1.00 131.21 ?  111  GLU   A OE2   1 
ATOM   851   N  N     . MET   A 1 112 ? 147.586 151.795 141.679 1.00 125.80 ?  112  MET   A N     1 
ATOM   852   C  CA    . MET   A 1 112 ? 146.311 151.456 140.988 1.00 125.99 ?  112  MET   A CA    1 
ATOM   853   C  C     . MET   A 1 112 ? 146.008 149.970 141.103 1.00 125.67 ?  112  MET   A C     1 
ATOM   854   O  O     . MET   A 1 112 ? 144.881 149.578 140.805 1.00 126.13 ?  112  MET   A O     1 
ATOM   855   C  CB    . MET   A 1 112 ? 146.340 151.772 139.500 1.00 125.39 ?  112  MET   A CB    1 
ATOM   856   C  CG    . MET   A 1 112 ? 147.363 152.803 139.112 1.00 126.59 ?  112  MET   A CG    1 
ATOM   857   S  SD    . MET   A 1 112 ? 147.415 153.047 137.326 1.00 131.36 ?  112  MET   A SD    1 
ATOM   858   C  CE    . MET   A 1 112 ? 149.008 153.861 137.170 1.00 125.90 ?  112  MET   A CE    1 
ATOM   859   N  N     . GLY   A 1 113 ? 146.973 149.171 141.512 1.00 117.87 ?  113  GLY   A N     1 
ATOM   860   C  CA    . GLY   A 1 113 ? 146.744 147.757 141.698 1.00 117.84 ?  113  GLY   A CA    1 
ATOM   861   C  C     . GLY   A 1 113 ? 146.844 146.900 140.457 1.00 118.26 ?  113  GLY   A C     1 
ATOM   862   O  O     . GLY   A 1 113 ? 146.406 145.745 140.493 1.00 118.50 ?  113  GLY   A O     1 
ATOM   863   N  N     . LYS   A 1 114 ? 147.388 147.423 139.356 1.00 110.90 ?  114  LYS   A N     1 
ATOM   864   C  CA    . LYS   A 1 114 ? 147.629 146.576 138.193 1.00 107.63 ?  114  LYS   A CA    1 
ATOM   865   C  C     . LYS   A 1 114 ? 148.779 145.605 138.423 1.00 105.13 ?  114  LYS   A C     1 
ATOM   866   O  O     . LYS   A 1 114 ? 148.904 144.623 137.684 1.00 107.66 ?  114  LYS   A O     1 
ATOM   867   C  CB    . LYS   A 1 114 ? 147.907 147.430 136.957 1.00 109.67 ?  114  LYS   A CB    1 
ATOM   868   C  CG    . LYS   A 1 114 ? 146.866 148.502 136.691 1.00 108.84 ?  114  LYS   A CG    1 
ATOM   869   C  CD    . LYS   A 1 114 ? 145.473 147.906 136.592 1.00 108.01 ?  114  LYS   A CD    1 
ATOM   870   C  CE    . LYS   A 1 114 ? 145.288 147.158 135.282 1.00 107.99 ?  114  LYS   A CE    1 
ATOM   871   N  NZ    . LYS   A 1 114 ? 144.130 147.678 134.507 1.00 109.50 ?  114  LYS   A NZ    1 
ATOM   872   N  N     . TYR   A 1 115 ? 149.616 145.859 139.423 1.00 100.14 ?  115  TYR   A N     1 
ATOM   873   C  CA    . TYR   A 1 115 ? 150.688 144.960 139.817 1.00 100.56 ?  115  TYR   A CA    1 
ATOM   874   C  C     . TYR   A 1 115 ? 150.399 144.397 141.201 1.00 103.83 ?  115  TYR   A C     1 
ATOM   875   O  O     . TYR   A 1 115 ? 149.766 145.050 142.035 1.00 106.30 ?  115  TYR   A O     1 
ATOM   876   C  CB    . TYR   A 1 115 ? 152.042 145.675 139.837 1.00 100.95 ?  115  TYR   A CB    1 
ATOM   877   C  CG    . TYR   A 1 115 ? 152.628 145.960 138.476 1.00 100.40 ?  115  TYR   A CG    1 
ATOM   878   C  CD1   . TYR   A 1 115 ? 152.009 145.508 137.320 1.00 102.18 ?  115  TYR   A CD1   1 
ATOM   879   C  CD2   . TYR   A 1 115 ? 153.804 146.682 138.349 1.00 101.09 ?  115  TYR   A CD2   1 
ATOM   880   C  CE1   . TYR   A 1 115 ? 152.546 145.771 136.075 1.00 101.80 ?  115  TYR   A CE1   1 
ATOM   881   C  CE2   . TYR   A 1 115 ? 154.342 146.955 137.113 1.00 102.36 ?  115  TYR   A CE2   1 
ATOM   882   C  CZ    . TYR   A 1 115 ? 153.713 146.494 135.978 1.00 103.83 ?  115  TYR   A CZ    1 
ATOM   883   O  OH    . TYR   A 1 115 ? 154.254 146.761 134.742 1.00 108.02 ?  115  TYR   A OH    1 
ATOM   884   N  N     . ASP   A 1 116 ? 150.864 143.175 141.438 1.00 105.04 ?  116  ASP   A N     1 
ATOM   885   C  CA    . ASP   A 1 116 ? 150.756 142.594 142.767 1.00 103.81 ?  116  ASP   A CA    1 
ATOM   886   C  C     . ASP   A 1 116 ? 151.686 143.332 143.720 1.00 105.22 ?  116  ASP   A C     1 
ATOM   887   O  O     . ASP   A 1 116 ? 152.875 143.505 143.433 1.00 107.27 ?  116  ASP   A O     1 
ATOM   888   C  CB    . ASP   A 1 116 ? 151.099 141.106 142.730 1.00 103.92 ?  116  ASP   A CB    1 
ATOM   889   C  CG    . ASP   A 1 116 ? 150.500 140.341 143.893 1.00 107.90 ?  116  ASP   A CG    1 
ATOM   890   O  OD1   . ASP   A 1 116 ? 150.841 140.655 145.052 1.00 108.67 ?  116  ASP   A OD1   1 
ATOM   891   O  OD2   . ASP   A 1 116 ? 149.689 139.424 143.649 1.00 107.87 ?  116  ASP   A OD2   1 
ATOM   892   N  N     . ASN   A 1 117 ? 151.143 143.771 144.858 1.00 108.49 ?  117  ASN   A N     1 
ATOM   893   C  CA    A ASN   A 1 117 ? 151.948 144.502 145.829 0.50 110.47 ?  117  ASN   A CA    1 
ATOM   894   C  CA    B ASN   A 1 117 ? 152.048 144.502 145.829 0.50 110.47 ?  117  ASN   A CA    1 
ATOM   895   C  C     . ASN   A 1 117 ? 153.025 143.630 146.457 1.00 108.70 ?  117  ASN   A C     1 
ATOM   896   O  O     . ASN   A 1 117 ? 153.988 144.165 147.019 1.00 108.07 ?  117  ASN   A O     1 
ATOM   897   C  CB    A ASN   A 1 117 ? 151.052 145.092 146.919 0.50 109.13 ?  117  ASN   A CB    1 
ATOM   898   C  CB    B ASN   A 1 117 ? 151.152 145.092 146.919 0.50 109.13 ?  117  ASN   A CB    1 
ATOM   899   C  CG    A ASN   A 1 117 ? 150.579 144.050 147.913 0.50 111.05 ?  117  ASN   A CG    1 
ATOM   900   C  CG    B ASN   A 1 117 ? 151.914 145.977 147.885 0.50 111.05 ?  117  ASN   A CG    1 
ATOM   901   O  OD1   A ASN   A 1 117 ? 151.375 143.288 148.460 0.50 114.65 ?  117  ASN   A OD1   1 
ATOM   902   O  OD1   B ASN   A 1 117 ? 153.136 145.889 147.997 0.50 114.65 ?  117  ASN   A OD1   1 
ATOM   903   N  ND2   A ASN   A 1 117 ? 149.275 144.013 148.155 0.50 108.22 ?  117  ASN   A ND2   1 
ATOM   904   N  ND2   B ASN   A 1 117 ? 151.194 146.841 148.589 0.50 108.22 ?  117  ASN   A ND2   1 
ATOM   905   N  N     . HIS   A 1 118 ? 152.887 142.302 146.360 1.00 102.26 ?  118  HIS   A N     1 
ATOM   906   C  CA    . HIS   A 1 118 ? 153.846 141.400 146.988 1.00 103.39 ?  118  HIS   A CA    1 
ATOM   907   C  C     . HIS   A 1 118 ? 155.268 141.688 146.534 1.00 103.03 ?  118  HIS   A C     1 
ATOM   908   O  O     . HIS   A 1 118 ? 156.208 141.486 147.305 1.00 107.01 ?  118  HIS   A O     1 
ATOM   909   C  CB    . HIS   A 1 118 ? 153.475 139.945 146.692 1.00 103.29 ?  118  HIS   A CB    1 
ATOM   910   C  CG    . HIS   A 1 118 ? 154.259 139.334 145.572 1.00 105.81 ?  118  HIS   A CG    1 
ATOM   911   N  ND1   . HIS   A 1 118 ? 153.883 139.449 144.251 1.00 106.61 ?  118  HIS   A ND1   1 
ATOM   912   C  CD2   . HIS   A 1 118 ? 155.395 138.597 145.576 1.00 104.97 ?  118  HIS   A CD2   1 
ATOM   913   C  CE1   . HIS   A 1 118 ? 154.755 138.813 143.490 1.00 103.11 ?  118  HIS   A CE1   1 
ATOM   914   N  NE2   . HIS   A 1 118 ? 155.683 138.288 144.269 1.00 103.38 ?  118  HIS   A NE2   1 
ATOM   915   N  N     . LEU   A 1 119 ? 155.437 142.179 145.303 1.00 99.33  ?  119  LEU   A N     1 
ATOM   916   C  CA    . LEU   A 1 119 ? 156.764 142.522 144.801 1.00 100.64 ?  119  LEU   A CA    1 
ATOM   917   C  C     . LEU   A 1 119 ? 157.493 143.451 145.762 1.00 103.97 ?  119  LEU   A C     1 
ATOM   918   O  O     . LEU   A 1 119 ? 158.659 143.221 146.107 1.00 104.79 ?  119  LEU   A O     1 
ATOM   919   C  CB    . LEU   A 1 119 ? 156.645 143.170 143.420 1.00 99.91  ?  119  LEU   A CB    1 
ATOM   920   C  CG    . LEU   A 1 119 ? 156.796 142.272 142.192 1.00 101.90 ?  119  LEU   A CG    1 
ATOM   921   C  CD1   . LEU   A 1 119 ? 156.192 142.941 140.970 1.00 99.49  ?  119  LEU   A CD1   1 
ATOM   922   C  CD2   . LEU   A 1 119 ? 158.259 141.936 141.953 1.00 103.61 ?  119  LEU   A CD2   1 
ATOM   923   N  N     . LEU   A 1 120 ? 156.804 144.494 146.235 1.00 106.73 ?  120  LEU   A N     1 
ATOM   924   C  CA    . LEU   A 1 120 ? 157.446 145.468 147.109 1.00 103.61 ?  120  LEU   A CA    1 
ATOM   925   C  C     . LEU   A 1 120 ? 157.887 144.857 148.431 1.00 104.15 ?  120  LEU   A C     1 
ATOM   926   O  O     . LEU   A 1 120 ? 158.712 145.454 149.132 1.00 103.69 ?  120  LEU   A O     1 
ATOM   927   C  CB    . LEU   A 1 120 ? 156.506 146.645 147.363 1.00 102.46 ?  120  LEU   A CB    1 
ATOM   928   C  CG    . LEU   A 1 120 ? 156.086 147.423 146.117 1.00 102.42 ?  120  LEU   A CG    1 
ATOM   929   C  CD1   . LEU   A 1 120 ? 154.795 148.178 146.370 1.00 103.48 ?  120  LEU   A CD1   1 
ATOM   930   C  CD2   . LEU   A 1 120 ? 157.192 148.368 145.683 1.00 102.21 ?  120  LEU   A CD2   1 
ATOM   931   N  N     . GLU   A 1 121 ? 157.362 143.687 148.786 1.00 111.58 ?  121  GLU   A N     1 
ATOM   932   C  CA    . GLU   A 1 121 ? 157.768 143.002 150.003 1.00 111.05 ?  121  GLU   A CA    1 
ATOM   933   C  C     . GLU   A 1 121 ? 159.000 142.123 149.822 1.00 112.97 ?  121  GLU   A C     1 
ATOM   934   O  O     . GLU   A 1 121 ? 159.579 141.693 150.825 1.00 113.50 ?  121  GLU   A O     1 
ATOM   935   C  CB    . GLU   A 1 121 ? 156.613 142.153 150.544 1.00 110.83 ?  121  GLU   A CB    1 
ATOM   936   C  CG    . GLU   A 1 121 ? 155.233 142.722 150.264 1.00 111.64 ?  121  GLU   A CG    1 
ATOM   937   C  CD    . GLU   A 1 121 ? 154.124 141.739 150.588 1.00 115.84 ?  121  GLU   A CD    1 
ATOM   938   O  OE1   . GLU   A 1 121 ? 154.415 140.700 151.216 1.00 117.77 ?  121  GLU   A OE1   1 
ATOM   939   O  OE2   . GLU   A 1 121 ? 152.962 142.004 150.216 1.00 113.48 ?  121  GLU   A OE2   1 
ATOM   940   N  N     . ASP   A 1 122 ? 159.424 141.843 148.585 1.00 110.09 ?  122  ASP   A N     1 
ATOM   941   C  CA    . ASP   A 1 122 ? 160.643 141.070 148.381 1.00 109.07 ?  122  ASP   A CA    1 
ATOM   942   C  C     . ASP   A 1 122 ? 161.817 141.890 147.872 1.00 107.85 ?  122  ASP   A C     1 
ATOM   943   O  O     . ASP   A 1 122 ? 162.957 141.430 147.981 1.00 107.99 ?  122  ASP   A O     1 
ATOM   944   C  CB    . ASP   A 1 122 ? 160.409 139.910 147.399 1.00 107.69 ?  122  ASP   A CB    1 
ATOM   945   C  CG    . ASP   A 1 122 ? 159.058 139.257 147.574 1.00 108.79 ?  122  ASP   A CG    1 
ATOM   946   O  OD1   . ASP   A 1 122 ? 158.035 139.914 147.310 1.00 108.17 ?  122  ASP   A OD1   1 
ATOM   947   O  OD2   . ASP   A 1 122 ? 159.023 138.084 147.989 1.00 110.08 ?  122  ASP   A OD2   1 
ATOM   948   N  N     . TYR   A 1 123 ? 161.580 143.079 147.324 1.00 102.35 ?  123  TYR   A N     1 
ATOM   949   C  CA    . TYR   A 1 123 ? 162.652 143.890 146.766 1.00 104.61 ?  123  TYR   A CA    1 
ATOM   950   C  C     . TYR   A 1 123 ? 162.618 145.285 147.370 1.00 107.01 ?  123  TYR   A C     1 
ATOM   951   O  O     . TYR   A 1 123 ? 161.554 145.907 147.453 1.00 105.35 ?  123  TYR   A O     1 
ATOM   952   C  CB    . TYR   A 1 123 ? 162.554 143.962 145.240 1.00 102.63 ?  123  TYR   A CB    1 
ATOM   953   C  CG    . TYR   A 1 123 ? 162.610 142.605 144.576 1.00 102.78 ?  123  TYR   A CG    1 
ATOM   954   C  CD1   . TYR   A 1 123 ? 163.824 142.018 144.251 1.00 101.88 ?  123  TYR   A CD1   1 
ATOM   955   C  CD2   . TYR   A 1 123 ? 161.448 141.902 144.290 1.00 102.85 ?  123  TYR   A CD2   1 
ATOM   956   C  CE1   . TYR   A 1 123 ? 163.879 140.776 143.651 1.00 101.20 ?  123  TYR   A CE1   1 
ATOM   957   C  CE2   . TYR   A 1 123 ? 161.494 140.660 143.690 1.00 104.04 ?  123  TYR   A CE2   1 
ATOM   958   C  CZ    . TYR   A 1 123 ? 162.713 140.103 143.372 1.00 102.86 ?  123  TYR   A CZ    1 
ATOM   959   O  OH    . TYR   A 1 123 ? 162.770 138.866 142.773 1.00 102.29 ?  123  TYR   A OH    1 
ATOM   960   N  N     . THR   A 1 124 ? 163.786 145.768 147.787 1.00 118.77 ?  124  THR   A N     1 
ATOM   961   C  CA    . THR   A 1 124 ? 163.929 147.088 148.380 1.00 118.35 ?  124  THR   A CA    1 
ATOM   962   C  C     . THR   A 1 124 ? 164.279 148.106 147.294 1.00 120.73 ?  124  THR   A C     1 
ATOM   963   O  O     . THR   A 1 124 ? 164.196 147.825 146.096 1.00 122.20 ?  124  THR   A O     1 
ATOM   964   C  CB    . THR   A 1 124 ? 164.981 147.058 149.487 1.00 119.40 ?  124  THR   A CB    1 
ATOM   965   O  OG1   . THR   A 1 124 ? 166.288 147.154 148.908 1.00 120.21 ?  124  THR   A OG1   1 
ATOM   966   C  CG2   . THR   A 1 124 ? 164.880 145.767 150.283 1.00 117.66 ?  124  THR   A CG2   1 
ATOM   967   N  N     . GLU   A 1 125 ? 164.674 149.310 147.713 1.00 128.87 ?  125  GLU   A N     1 
ATOM   968   C  CA    . GLU   A 1 125 ? 165.023 150.358 146.758 1.00 129.29 ?  125  GLU   A CA    1 
ATOM   969   C  C     . GLU   A 1 125 ? 166.254 149.980 145.942 1.00 130.40 ?  125  GLU   A C     1 
ATOM   970   O  O     . GLU   A 1 125 ? 166.255 150.094 144.710 1.00 129.84 ?  125  GLU   A O     1 
ATOM   971   C  CB    . GLU   A 1 125 ? 165.258 151.676 147.497 1.00 129.69 ?  125  GLU   A CB    1 
ATOM   972   C  CG    . GLU   A 1 125 ? 165.222 152.907 146.608 1.00 130.96 ?  125  GLU   A CG    1 
ATOM   973   C  CD    . GLU   A 1 125 ? 163.828 153.218 146.111 1.00 129.70 ?  125  GLU   A CD    1 
ATOM   974   O  OE1   . GLU   A 1 125 ? 162.864 152.927 146.846 1.00 129.10 ?  125  GLU   A OE1   1 
ATOM   975   O  OE2   . GLU   A 1 125 ? 163.697 153.749 144.988 1.00 129.13 ?  125  GLU   A OE2   1 
ATOM   976   N  N     . GLU   A 1 126 ? 167.312 149.523 146.617 1.00 132.60 ?  126  GLU   A N     1 
ATOM   977   C  CA    . GLU   A 1 126 ? 168.578 149.262 145.936 1.00 135.64 ?  126  GLU   A CA    1 
ATOM   978   C  C     . GLU   A 1 126 ? 168.438 148.157 144.897 1.00 137.38 ?  126  GLU   A C     1 
ATOM   979   O  O     . GLU   A 1 126 ? 169.026 148.236 143.812 1.00 136.07 ?  126  GLU   A O     1 
ATOM   980   C  CB    . GLU   A 1 126 ? 169.655 148.901 146.958 1.00 133.95 ?  126  GLU   A CB    1 
ATOM   981   C  CG    . GLU   A 1 126 ? 171.071 148.971 146.413 1.00 134.25 ?  126  GLU   A CG    1 
ATOM   982   C  CD    . GLU   A 1 126 ? 172.018 149.701 147.343 1.00 134.62 ?  126  GLU   A CD    1 
ATOM   983   O  OE1   . GLU   A 1 126 ? 171.882 150.935 147.483 1.00 133.74 ?  126  GLU   A OE1   1 
ATOM   984   O  OE2   . GLU   A 1 126 ? 172.899 149.042 147.934 1.00 135.54 ?  126  GLU   A OE2   1 
ATOM   985   N  N     . GLU   A 1 127 ? 167.673 147.112 145.214 1.00 127.19 ?  127  GLU   A N     1 
ATOM   986   C  CA    . GLU   A 1 127 ? 167.477 146.025 144.261 1.00 123.88 ?  127  GLU   A CA    1 
ATOM   987   C  C     . GLU   A 1 127 ? 166.711 146.500 143.030 1.00 124.28 ?  127  GLU   A C     1 
ATOM   988   O  O     . GLU   A 1 127 ? 167.022 146.098 141.900 1.00 127.55 ?  127  GLU   A O     1 
ATOM   989   C  CB    . GLU   A 1 127 ? 166.765 144.864 144.952 1.00 122.83 ?  127  GLU   A CB    1 
ATOM   990   C  CG    . GLU   A 1 127 ? 167.662 144.132 145.944 1.00 125.43 ?  127  GLU   A CG    1 
ATOM   991   C  CD    . GLU   A 1 127 ? 166.891 143.340 146.978 1.00 125.73 ?  127  GLU   A CD    1 
ATOM   992   O  OE1   . GLU   A 1 127 ? 165.689 143.609 147.157 1.00 124.58 ?  127  GLU   A OE1   1 
ATOM   993   O  OE2   . GLU   A 1 127 ? 167.489 142.447 147.615 1.00 124.83 ?  127  GLU   A OE2   1 
ATOM   994   N  N     . PHE   A 1 128 ? 165.718 147.370 143.223 1.00 111.05 ?  128  PHE   A N     1 
ATOM   995   C  CA    . PHE   A 1 128 ? 165.002 147.926 142.079 1.00 111.70 ?  128  PHE   A CA    1 
ATOM   996   C  C     . PHE   A 1 128 ? 165.904 148.829 141.245 1.00 114.53 ?  128  PHE   A C     1 
ATOM   997   O  O     . PHE   A 1 128 ? 165.796 148.851 140.015 1.00 116.56 ?  128  PHE   A O     1 
ATOM   998   C  CB    . PHE   A 1 128 ? 163.758 148.677 142.548 1.00 112.68 ?  128  PHE   A CB    1 
ATOM   999   C  CG    . PHE   A 1 128 ? 162.533 147.813 142.641 1.00 112.34 ?  128  PHE   A CG    1 
ATOM   1000  C  CD1   . PHE   A 1 128 ? 161.978 147.252 141.504 1.00 110.46 ?  128  PHE   A CD1   1 
ATOM   1001  C  CD2   . PHE   A 1 128 ? 161.940 147.558 143.865 1.00 115.97 ?  128  PHE   A CD2   1 
ATOM   1002  C  CE1   . PHE   A 1 128 ? 160.854 146.453 141.584 1.00 110.32 ?  128  PHE   A CE1   1 
ATOM   1003  C  CE2   . PHE   A 1 128 ? 160.813 146.761 143.951 1.00 115.35 ?  128  PHE   A CE2   1 
ATOM   1004  C  CZ    . PHE   A 1 128 ? 160.271 146.208 142.809 1.00 112.00 ?  128  PHE   A CZ    1 
ATOM   1005  N  N     . LYS   A 1 129 ? 166.802 149.581 141.888 1.00 116.17 ?  129  LYS   A N     1 
ATOM   1006  C  CA    . LYS   A 1 129 ? 167.765 150.375 141.126 1.00 118.58 ?  129  LYS   A CA    1 
ATOM   1007  C  C     . LYS   A 1 129 ? 168.717 149.480 140.337 1.00 120.49 ?  129  LYS   A C     1 
ATOM   1008  O  O     . LYS   A 1 129 ? 169.102 149.809 139.206 1.00 123.50 ?  129  LYS   A O     1 
ATOM   1009  C  CB    . LYS   A 1 129 ? 168.546 151.300 142.059 1.00 115.96 ?  129  LYS   A CB    1 
ATOM   1010  C  CG    . LYS   A 1 129 ? 167.673 152.194 142.922 1.00 116.91 ?  129  LYS   A CG    1 
ATOM   1011  C  CD    . LYS   A 1 129 ? 167.313 153.483 142.205 1.00 118.51 ?  129  LYS   A CD    1 
ATOM   1012  C  CE    . LYS   A 1 129 ? 167.283 154.655 143.170 1.00 117.19 ?  129  LYS   A CE    1 
ATOM   1013  N  NZ    . LYS   A 1 129 ? 168.403 154.592 144.149 1.00 118.09 ?  129  LYS   A NZ    1 
ATOM   1014  N  N     . GLN   A 1 130 ? 169.117 148.351 140.926 1.00 115.97 ?  130  GLN   A N     1 
ATOM   1015  C  CA    . GLN   A 1 130 ? 169.956 147.395 140.212 1.00 115.28 ?  130  GLN   A CA    1 
ATOM   1016  C  C     . GLN   A 1 130 ? 169.231 146.831 138.996 1.00 116.24 ?  130  GLN   A C     1 
ATOM   1017  O  O     . GLN   A 1 130 ? 169.829 146.661 137.927 1.00 119.16 ?  130  GLN   A O     1 
ATOM   1018  C  CB    . GLN   A 1 130 ? 170.385 146.270 141.152 1.00 114.78 ?  130  GLN   A CB    1 
ATOM   1019  C  CG    . GLN   A 1 130 ? 171.855 145.906 141.055 1.00 114.79 ?  130  GLN   A CG    1 
ATOM   1020  C  CD    . GLN   A 1 130 ? 172.436 145.486 142.390 1.00 118.67 ?  130  GLN   A CD    1 
ATOM   1021  O  OE1   . GLN   A 1 130 ? 172.130 146.075 143.426 1.00 119.59 ?  130  GLN   A OE1   1 
ATOM   1022  N  NE2   . GLN   A 1 130 ? 173.279 144.461 142.372 1.00 118.28 ?  130  GLN   A NE2   1 
ATOM   1023  N  N     . MET   A 1 131 ? 167.940 146.532 139.139 1.00 113.45 ?  131  MET   A N     1 
ATOM   1024  C  CA    . MET   A 1 131 ? 167.159 146.114 137.978 1.00 114.21 ?  131  MET   A CA    1 
ATOM   1025  C  C     . MET   A 1 131 ? 167.062 147.231 136.945 1.00 116.41 ?  131  MET   A C     1 
ATOM   1026  O  O     . MET   A 1 131 ? 167.111 146.975 135.736 1.00 120.34 ?  131  MET   A O     1 
ATOM   1027  C  CB    . MET   A 1 131 ? 165.766 145.666 138.407 1.00 115.19 ?  131  MET   A CB    1 
ATOM   1028  C  CG    . MET   A 1 131 ? 165.751 144.362 139.155 1.00 115.57 ?  131  MET   A CG    1 
ATOM   1029  S  SD    . MET   A 1 131 ? 164.134 144.008 139.850 1.00 119.71 ?  131  MET   A SD    1 
ATOM   1030  C  CE    . MET   A 1 131 ? 164.599 142.753 141.025 1.00 114.41 ?  131  MET   A CE    1 
ATOM   1031  N  N     . ASP   A 1 132 ? 166.908 148.476 137.403 1.00 119.10 ?  132  ASP   A N     1 
ATOM   1032  C  CA    . ASP   A 1 132 ? 166.806 149.600 136.479 1.00 119.28 ?  132  ASP   A CA    1 
ATOM   1033  C  C     . ASP   A 1 132 ? 168.072 149.744 135.645 1.00 119.69 ?  132  ASP   A C     1 
ATOM   1034  O  O     . ASP   A 1 132 ? 168.002 149.987 134.434 1.00 119.85 ?  132  ASP   A O     1 
ATOM   1035  C  CB    . ASP   A 1 132 ? 166.521 150.890 137.249 1.00 120.60 ?  132  ASP   A CB    1 
ATOM   1036  C  CG    . ASP   A 1 132 ? 166.005 152.001 136.355 1.00 123.70 ?  132  ASP   A CG    1 
ATOM   1037  O  OD1   . ASP   A 1 132 ? 164.954 151.806 135.709 1.00 123.72 ?  132  ASP   A OD1   1 
ATOM   1038  O  OD2   . ASP   A 1 132 ? 166.651 153.068 136.297 1.00 124.37 ?  132  ASP   A OD2   1 
ATOM   1039  N  N     . THR   A 1 133 ? 169.240 149.601 136.272 1.00 114.26 ?  133  THR   A N     1 
ATOM   1040  C  CA    . THR   A 1 133 ? 170.476 149.627 135.497 1.00 115.82 ?  133  THR   A CA    1 
ATOM   1041  C  C     . THR   A 1 133 ? 170.715 148.328 134.737 1.00 116.09 ?  133  THR   A C     1 
ATOM   1042  O  O     . THR   A 1 133 ? 171.560 148.303 133.835 1.00 116.39 ?  133  THR   A O     1 
ATOM   1043  C  CB    . THR   A 1 133 ? 171.686 149.939 136.387 1.00 114.77 ?  133  THR   A CB    1 
ATOM   1044  O  OG1   . THR   A 1 133 ? 172.885 149.855 135.607 1.00 115.77 ?  133  THR   A OG1   1 
ATOM   1045  C  CG2   . THR   A 1 133 ? 171.787 148.965 137.535 1.00 113.23 ?  133  THR   A CG2   1 
ATOM   1046  N  N     . PHE   A 1 134 ? 169.930 147.280 135.009 1.00 112.70 ?  134  PHE   A N     1 
ATOM   1047  C  CA    . PHE   A 1 134 ? 170.031 146.035 134.201 1.00 110.06 ?  134  PHE   A CA    1 
ATOM   1048  C  C     . PHE   A 1 134 ? 169.166 146.187 132.959 1.00 109.88 ?  134  PHE   A C     1 
ATOM   1049  O  O     . PHE   A 1 134 ? 169.424 145.504 131.961 1.00 109.18 ?  134  PHE   A O     1 
ATOM   1050  C  CB    . PHE   A 1 134 ? 169.421 144.830 134.918 1.00 108.14 ?  134  PHE   A CB    1 
ATOM   1051  C  CG    . PHE   A 1 134 ? 170.226 144.225 136.037 1.00 110.12 ?  134  PHE   A CG    1 
ATOM   1052  C  CD1   . PHE   A 1 134 ? 171.554 144.562 136.224 1.00 112.60 ?  134  PHE   A CD1   1 
ATOM   1053  C  CD2   . PHE   A 1 134 ? 169.646 143.315 136.904 1.00 108.27 ?  134  PHE   A CD2   1 
ATOM   1054  C  CE1   . PHE   A 1 134 ? 172.286 144.002 137.258 1.00 112.50 ?  134  PHE   A CE1   1 
ATOM   1055  C  CE2   . PHE   A 1 134 ? 170.379 142.756 137.937 1.00 111.59 ?  134  PHE   A CE2   1 
ATOM   1056  C  CZ    . PHE   A 1 134 ? 171.697 143.099 138.111 1.00 112.65 ?  134  PHE   A CZ    1 
ATOM   1057  N  N     . ILE   A 1 135 ? 168.169 147.069 133.020 1.00 111.41 ?  135  ILE   A N     1 
ATOM   1058  C  CA    . ILE   A 1 135 ? 167.225 147.183 131.915 1.00 110.11 ?  135  ILE   A CA    1 
ATOM   1059  C  C     . ILE   A 1 135 ? 167.895 147.840 130.717 1.00 112.65 ?  135  ILE   A C     1 
ATOM   1060  O  O     . ILE   A 1 135 ? 168.646 148.815 130.857 1.00 115.44 ?  135  ILE   A O     1 
ATOM   1061  C  CB    . ILE   A 1 135 ? 165.986 147.979 132.363 1.00 112.51 ?  135  ILE   A CB    1 
ATOM   1062  C  CG1   . ILE   A 1 135 ? 164.984 147.070 133.069 1.00 112.58 ?  135  ILE   A CG1   1 
ATOM   1063  C  CG2   . ILE   A 1 135 ? 165.314 148.655 131.182 1.00 112.23 ?  135  ILE   A CG2   1 
ATOM   1064  C  CD1   . ILE   A 1 135 ? 163.695 147.774 133.418 1.00 112.89 ?  135  ILE   A CD1   1 
ATOM   1065  N  N     . ASP   A 1 136 ? 167.630 147.302 129.528 1.00 124.93 ?  136  ASP   A N     1 
ATOM   1066  C  CA    . ASP   A 1 136 ? 168.047 147.908 128.265 1.00 127.84 ?  136  ASP   A CA    1 
ATOM   1067  C  C     . ASP   A 1 136 ? 166.792 148.133 127.426 1.00 126.61 ?  136  ASP   A C     1 
ATOM   1068  O  O     . ASP   A 1 136 ? 166.253 147.190 126.839 1.00 128.92 ?  136  ASP   A O     1 
ATOM   1069  C  CB    . ASP   A 1 136 ? 169.056 147.028 127.535 1.00 126.82 ?  136  ASP   A CB    1 
ATOM   1070  C  CG    . ASP   A 1 136 ? 169.391 147.553 126.152 1.00 127.66 ?  136  ASP   A CG    1 
ATOM   1071  O  OD1   . ASP   A 1 136 ? 169.440 148.789 125.979 1.00 127.79 ?  136  ASP   A OD1   1 
ATOM   1072  O  OD2   . ASP   A 1 136 ? 169.606 146.730 125.238 1.00 127.77 ?  136  ASP   A OD2   1 
ATOM   1073  N  N     . HIS   A 1 137 ? 166.336 149.390 127.283 1.00 110.51 ?  137  HIS   A N     1 
ATOM   1074  C  CA    . HIS   A 1 137 ? 165.078 149.739 126.581 1.00 111.94 ?  137  HIS   A CA    1 
ATOM   1075  C  C     . HIS   A 1 137 ? 165.323 149.818 125.085 1.00 114.24 ?  137  HIS   A C     1 
ATOM   1076  O  O     . HIS   A 1 137 ? 164.357 149.932 124.341 1.00 113.98 ?  137  HIS   A O     1 
ATOM   1077  C  CB    . HIS   A 1 137 ? 164.502 151.046 127.101 1.00 111.93 ?  137  HIS   A CB    1 
ATOM   1078  C  CG    . HIS   A 1 137 ? 163.649 150.961 128.320 1.00 115.22 ?  137  HIS   A CG    1 
ATOM   1079  N  ND1   . HIS   A 1 137 ? 164.158 151.096 129.590 1.00 114.06 ?  137  HIS   A ND1   1 
ATOM   1080  C  CD2   . HIS   A 1 137 ? 162.318 150.814 128.465 1.00 115.43 ?  137  HIS   A CD2   1 
ATOM   1081  C  CE1   . HIS   A 1 137 ? 163.180 151.018 130.463 1.00 114.20 ?  137  HIS   A CE1   1 
ATOM   1082  N  NE2   . HIS   A 1 137 ? 162.048 150.836 129.801 1.00 114.56 ?  137  HIS   A NE2   1 
ATOM   1083  N  N     . ASP   A 1 138 ? 166.576 149.737 124.662 1.00 128.96 ?  138  ASP   A N     1 
ATOM   1084  C  CA    . ASP   A 1 138 ? 166.849 149.687 123.229 1.00 130.49 ?  138  ASP   A CA    1 
ATOM   1085  C  C     . ASP   A 1 138 ? 166.307 148.411 122.599 1.00 129.90 ?  138  ASP   A C     1 
ATOM   1086  O  O     . ASP   A 1 138 ? 165.985 148.395 121.405 1.00 129.68 ?  138  ASP   A O     1 
ATOM   1087  C  CB    . ASP   A 1 138 ? 168.353 149.808 122.982 1.00 131.11 ?  138  ASP   A CB    1 
ATOM   1088  C  CG    . ASP   A 1 138 ? 168.703 149.840 121.508 1.00 134.38 ?  138  ASP   A CG    1 
ATOM   1089  O  OD1   . ASP   A 1 138 ? 167.940 150.445 120.726 1.00 135.66 ?  138  ASP   A OD1   1 
ATOM   1090  O  OD2   . ASP   A 1 138 ? 169.742 149.259 121.130 1.00 132.37 ?  138  ASP   A OD2   1 
ATOM   1091  N  N     . ARG   A 1 139 ? 166.184 147.340 123.387 1.00 109.84 ?  139  ARG   A N     1 
ATOM   1092  C  CA    . ARG   A 1 139 ? 165.639 146.089 122.877 1.00 107.55 ?  139  ARG   A CA    1 
ATOM   1093  C  C     . ARG   A 1 139 ? 164.205 146.244 122.389 1.00 107.55 ?  139  ARG   A C     1 
ATOM   1094  O  O     . ARG   A 1 139 ? 163.746 145.429 121.579 1.00 111.46 ?  139  ARG   A O     1 
ATOM   1095  C  CB    . ARG   A 1 139 ? 165.728 145.012 123.958 1.00 103.41 ?  139  ARG   A CB    1 
ATOM   1096  C  CG    . ARG   A 1 139 ? 167.162 144.652 124.312 1.00 102.89 ?  139  ARG   A CG    1 
ATOM   1097  C  CD    . ARG   A 1 139 ? 167.255 143.739 125.519 1.00 103.83 ?  139  ARG   A CD    1 
ATOM   1098  N  NE    . ARG   A 1 139 ? 168.634 143.333 125.763 1.00 105.09 ?  139  ARG   A NE    1 
ATOM   1099  C  CZ    . ARG   A 1 139 ? 169.039 142.637 126.816 1.00 106.90 ?  139  ARG   A CZ    1 
ATOM   1100  N  NH1   . ARG   A 1 139 ? 168.191 142.238 127.748 1.00 106.34 ?  139  ARG   A NH1   1 
ATOM   1101  N  NH2   . ARG   A 1 139 ? 170.328 142.333 126.936 1.00 107.42 ?  139  ARG   A NH2   1 
ATOM   1102  N  N     . ASP   A 1 140 ? 163.502 147.291 122.832 1.00 111.07 ?  140  ASP   A N     1 
ATOM   1103  C  CA    . ASP   A 1 140 ? 162.162 147.559 122.323 1.00 112.96 ?  140  ASP   A CA    1 
ATOM   1104  C  C     . ASP   A 1 140 ? 162.162 147.814 120.824 1.00 115.54 ?  140  ASP   A C     1 
ATOM   1105  O  O     . ASP   A 1 140 ? 161.107 147.719 120.188 1.00 113.87 ?  140  ASP   A O     1 
ATOM   1106  C  CB    . ASP   A 1 140 ? 161.552 148.759 123.047 1.00 114.28 ?  140  ASP   A CB    1 
ATOM   1107  C  CG    . ASP   A 1 140 ? 160.663 148.353 124.199 1.00 116.04 ?  140  ASP   A CG    1 
ATOM   1108  O  OD1   . ASP   A 1 140 ? 159.607 147.737 123.946 1.00 116.86 ?  140  ASP   A OD1   1 
ATOM   1109  O  OD2   . ASP   A 1 140 ? 161.016 148.652 125.358 1.00 117.16 ?  140  ASP   A OD2   1 
ATOM   1110  N  N     . MET   A 1 141 ? 163.335 147.971 120.278 1.00 121.57 ?  141  MET   A N     1 
ATOM   1111  C  CA    . MET   A 1 141 ? 163.399 148.328 118.856 1.00 119.55 ?  141  MET   A CA    1 
ATOM   1112  C  C     . MET   A 1 141 ? 163.793 147.095 118.067 1.00 121.10 ?  141  MET   A C     1 
ATOM   1113  O  O     . MET   A 1 141 ? 164.132 147.240 116.899 1.00 124.04 ?  141  MET   A O     1 
ATOM   1114  C  CB    . MET   A 1 141 ? 164.410 149.462 118.731 1.00 120.47 ?  141  MET   A CB    1 
ATOM   1115  C  CG    . MET   A 1 141 ? 164.236 150.549 119.761 1.00 122.25 ?  141  MET   A CG    1 
ATOM   1116  S  SD    . MET   A 1 141 ? 163.043 151.735 119.124 1.00 129.92 ?  141  MET   A SD    1 
ATOM   1117  C  CE    . MET   A 1 141 ? 161.524 151.127 119.866 1.00 123.36 ?  141  MET   A CE    1 
ATOM   1118  N  N     . THR   A 1 142 ? 163.703 145.936 118.690 1.00 107.47 ?  142  THR   A N     1 
ATOM   1119  C  CA    . THR   A 1 142 ? 163.931 144.667 118.014 1.00 106.31 ?  142  THR   A CA    1 
ATOM   1120  C  C     . THR   A 1 142 ? 162.642 143.936 117.651 1.00 105.56 ?  142  THR   A C     1 
ATOM   1121  O  O     . THR   A 1 142 ? 162.699 142.927 116.939 1.00 107.33 ?  142  THR   A O     1 
ATOM   1122  C  CB    . THR   A 1 142 ? 164.813 143.764 118.887 1.00 106.66 ?  142  THR   A CB    1 
ATOM   1123  O  OG1   . THR   A 1 142 ? 165.758 144.573 119.599 1.00 104.46 ?  142  THR   A OG1   1 
ATOM   1124  C  CG2   . THR   A 1 142 ? 165.575 142.765 118.033 1.00 106.60 ?  142  THR   A CG2   1 
ATOM   1125  N  N     . PHE   A 1 143 ? 161.489 144.422 118.102 1.00 103.37 ?  143  PHE   A N     1 
ATOM   1126  C  CA    . PHE   A 1 143 ? 160.220 143.788 117.784 1.00 101.55 ?  143  PHE   A CA    1 
ATOM   1127  C  C     . PHE   A 1 143 ? 159.809 144.087 116.343 1.00 104.11 ?  143  PHE   A C     1 
ATOM   1128  O  O     . PHE   A 1 143 ? 160.338 144.990 115.689 1.00 106.20 ?  143  PHE   A O     1 
ATOM   1129  C  CB    . PHE   A 1 143 ? 159.124 144.260 118.740 1.00 102.27 ?  143  PHE   A CB    1 
ATOM   1130  C  CG    . PHE   A 1 143 ? 159.348 143.865 120.173 1.00 105.04 ?  143  PHE   A CG    1 
ATOM   1131  C  CD1   . PHE   A 1 143 ? 160.152 144.631 121.000 1.00 107.72 ?  143  PHE   A CD1   1 
ATOM   1132  C  CD2   . PHE   A 1 143 ? 158.741 142.738 120.697 1.00 105.25 ?  143  PHE   A CD2   1 
ATOM   1133  C  CE1   . PHE   A 1 143 ? 160.355 144.272 122.318 1.00 106.53 ?  143  PHE   A CE1   1 
ATOM   1134  C  CE2   . PHE   A 1 143 ? 158.938 142.376 122.015 1.00 106.77 ?  143  PHE   A CE2   1 
ATOM   1135  C  CZ    . PHE   A 1 143 ? 159.747 143.143 122.825 1.00 106.49 ?  143  PHE   A CZ    1 
ATOM   1136  N  N     . SER   A 1 144 ? 158.850 143.308 115.853 1.00 111.56 ?  144  SER   A N     1 
ATOM   1137  C  CA    . SER   A 1 144 ? 158.242 143.508 114.546 1.00 110.34 ?  144  SER   A CA    1 
ATOM   1138  C  C     . SER   A 1 144 ? 156.806 143.992 114.721 1.00 111.51 ?  144  SER   A C     1 
ATOM   1139  O  O     . SER   A 1 144 ? 156.269 144.022 115.831 1.00 114.54 ?  144  SER   A O     1 
ATOM   1140  C  CB    . SER   A 1 144 ? 158.290 142.217 113.720 1.00 110.00 ?  144  SER   A CB    1 
ATOM   1141  O  OG    . SER   A 1 144 ? 157.236 141.342 114.074 1.00 111.69 ?  144  SER   A OG    1 
ATOM   1142  N  N     . TYR   A 1 145 ? 156.187 144.393 113.607 1.00 105.87 ?  145  TYR   A N     1 
ATOM   1143  C  CA    . TYR   A 1 145 ? 154.867 145.016 113.685 1.00 105.76 ?  145  TYR   A CA    1 
ATOM   1144  C  C     . TYR   A 1 145 ? 153.821 144.050 114.230 1.00 105.02 ?  145  TYR   A C     1 
ATOM   1145  O  O     . TYR   A 1 145 ? 153.012 144.418 115.088 1.00 106.57 ?  145  TYR   A O     1 
ATOM   1146  C  CB    . TYR   A 1 145 ? 154.441 145.546 112.318 1.00 103.45 ?  145  TYR   A CB    1 
ATOM   1147  C  CG    . TYR   A 1 145 ? 153.154 146.335 112.380 1.00 102.43 ?  145  TYR   A CG    1 
ATOM   1148  C  CD1   . TYR   A 1 145 ? 153.107 147.571 113.008 1.00 105.39 ?  145  TYR   A CD1   1 
ATOM   1149  C  CD2   . TYR   A 1 145 ? 151.982 145.836 111.832 1.00 101.52 ?  145  TYR   A CD2   1 
ATOM   1150  C  CE1   . TYR   A 1 145 ? 151.933 148.294 113.076 1.00 106.57 ?  145  TYR   A CE1   1 
ATOM   1151  C  CE2   . TYR   A 1 145 ? 150.804 146.552 111.896 1.00 103.78 ?  145  TYR   A CE2   1 
ATOM   1152  C  CZ    . TYR   A 1 145 ? 150.785 147.780 112.518 1.00 106.11 ?  145  TYR   A CZ    1 
ATOM   1153  O  OH    . TYR   A 1 145 ? 149.612 148.495 112.583 1.00 107.13 ?  145  TYR   A OH    1 
ATOM   1154  N  N     . ALA   A 1 146 ? 153.813 142.810 113.735 1.00 99.99  ?  146  ALA   A N     1 
ATOM   1155  C  CA    . ALA   A 1 146 ? 152.902 141.812 114.286 1.00 98.73  ?  146  ALA   A CA    1 
ATOM   1156  C  C     . ALA   A 1 146 ? 153.224 141.536 115.748 1.00 99.82  ?  146  ALA   A C     1 
ATOM   1157  O  O     . ALA   A 1 146 ? 152.317 141.360 116.573 1.00 100.99 ?  146  ALA   A O     1 
ATOM   1158  C  CB    . ALA   A 1 146 ? 152.969 140.524 113.465 1.00 99.84  ?  146  ALA   A CB    1 
ATOM   1159  N  N     . ALA   A 1 147 ? 154.515 141.503 116.085 1.00 96.24  ?  147  ALA   A N     1 
ATOM   1160  C  CA    . ALA   A 1 147 ? 154.924 141.314 117.471 1.00 95.31  ?  147  ALA   A CA    1 
ATOM   1161  C  C     . ALA   A 1 147 ? 154.399 142.436 118.356 1.00 97.13  ?  147  ALA   A C     1 
ATOM   1162  O  O     . ALA   A 1 147 ? 153.873 142.184 119.445 1.00 98.32  ?  147  ALA   A O     1 
ATOM   1163  C  CB    . ALA   A 1 147 ? 156.448 141.234 117.555 1.00 94.90  ?  147  ALA   A CB    1 
ATOM   1164  N  N     . VAL   A 1 148 ? 154.521 143.683 117.897 1.00 101.42 ?  148  VAL   A N     1 
ATOM   1165  C  CA    . VAL   A 1 148 ? 154.058 144.819 118.688 1.00 99.88  ?  148  VAL   A CA    1 
ATOM   1166  C  C     . VAL   A 1 148 ? 152.540 144.802 118.817 1.00 99.89  ?  148  VAL   A C     1 
ATOM   1167  O  O     . VAL   A 1 148 ? 151.989 145.113 119.881 1.00 105.07 ?  148  VAL   A O     1 
ATOM   1168  C  CB    . VAL   A 1 148 ? 154.566 146.136 118.072 1.00 97.99  ?  148  VAL   A CB    1 
ATOM   1169  C  CG1   . VAL   A 1 148 ? 153.860 147.330 118.693 1.00 99.23  ?  148  VAL   A CG1   1 
ATOM   1170  C  CG2   . VAL   A 1 148 ? 156.068 146.252 118.251 1.00 99.28  ?  148  VAL   A CG2   1 
ATOM   1171  N  N     . LYS   A 1 149 ? 151.839 144.443 117.739 1.00 97.75  ?  149  LYS   A N     1 
ATOM   1172  C  CA    . LYS   A 1 149 ? 150.383 144.374 117.801 1.00 96.84  ?  149  LYS   A CA    1 
ATOM   1173  C  C     . LYS   A 1 149 ? 149.923 143.318 118.797 1.00 99.86  ?  149  LYS   A C     1 
ATOM   1174  O  O     . LYS   A 1 149 ? 149.012 143.565 119.595 1.00 103.71 ?  149  LYS   A O     1 
ATOM   1175  C  CB    . LYS   A 1 149 ? 149.810 144.095 116.412 1.00 101.38 ?  149  LYS   A CB    1 
ATOM   1176  C  CG    . LYS   A 1 149 ? 149.904 145.276 115.459 1.00 102.91 ?  149  LYS   A CG    1 
ATOM   1177  C  CD    . LYS   A 1 149 ? 149.267 146.520 116.055 1.00 101.87 ?  149  LYS   A CD    1 
ATOM   1178  C  CE    . LYS   A 1 149 ? 147.961 146.861 115.357 1.00 103.52 ?  149  LYS   A CE    1 
ATOM   1179  N  NZ    . LYS   A 1 149 ? 146.948 147.398 116.307 1.00 101.09 ?  149  LYS   A NZ    1 
ATOM   1180  N  N     . GLN   A 1 150 ? 150.550 142.139 118.778 1.00 100.86 ?  150  GLN   A N     1 
ATOM   1181  C  CA    . GLN   A 1 150 ? 150.211 141.110 119.757 1.00 100.22 ?  150  GLN   A CA    1 
ATOM   1182  C  C     . GLN   A 1 150 ? 150.561 141.561 121.171 1.00 98.95  ?  150  GLN   A C     1 
ATOM   1183  O  O     . GLN   A 1 150 ? 149.806 141.307 122.120 1.00 103.26 ?  150  GLN   A O     1 
ATOM   1184  C  CB    . GLN   A 1 150 ? 150.928 139.804 119.415 1.00 102.34 ?  150  GLN   A CB    1 
ATOM   1185  C  CG    . GLN   A 1 150 ? 150.472 139.164 118.114 1.00 103.48 ?  150  GLN   A CG    1 
ATOM   1186  C  CD    . GLN   A 1 150 ? 148.998 138.818 118.119 1.00 105.31 ?  150  GLN   A CD    1 
ATOM   1187  O  OE1   . GLN   A 1 150 ? 148.460 138.352 119.122 1.00 105.44 ?  150  GLN   A OE1   1 
ATOM   1188  N  NE2   . GLN   A 1 150 ? 148.333 139.048 116.993 1.00 105.41 ?  150  GLN   A NE2   1 
ATOM   1189  N  N     . LEU   A 1 151 ? 151.708 142.230 121.325 1.00 96.47  ?  151  LEU   A N     1 
ATOM   1190  C  CA    . LEU   A 1 151 ? 152.132 142.737 122.626 1.00 97.33  ?  151  LEU   A CA    1 
ATOM   1191  C  C     . LEU   A 1 151 ? 151.085 143.673 123.210 1.00 99.31  ?  151  LEU   A C     1 
ATOM   1192  O  O     . LEU   A 1 151 ? 150.710 143.559 124.383 1.00 103.08 ?  151  LEU   A O     1 
ATOM   1193  C  CB    . LEU   A 1 151 ? 153.473 143.465 122.481 1.00 96.30  ?  151  LEU   A CB    1 
ATOM   1194  C  CG    . LEU   A 1 151 ? 154.794 142.885 122.999 1.00 98.06  ?  151  LEU   A CG    1 
ATOM   1195  C  CD1   . LEU   A 1 151 ? 155.800 143.990 123.260 1.00 98.53  ?  151  LEU   A CD1   1 
ATOM   1196  C  CD2   . LEU   A 1 151 ? 154.599 142.095 124.256 1.00 100.78 ?  151  LEU   A CD2   1 
ATOM   1197  N  N     . GLU   A 1 152 ? 150.601 144.610 122.394 1.00 116.97 ?  152  GLU   A N     1 
ATOM   1198  C  CA    . GLU   A 1 152 ? 149.560 145.527 122.843 1.00 117.41 ?  152  GLU   A CA    1 
ATOM   1199  C  C     . GLU   A 1 152 ? 148.253 144.791 123.106 1.00 119.56 ?  152  GLU   A C     1 
ATOM   1200  O  O     . GLU   A 1 152 ? 147.546 145.096 124.073 1.00 122.74 ?  152  GLU   A O     1 
ATOM   1201  C  CB    . GLU   A 1 152 ? 149.362 146.636 121.808 1.00 119.22 ?  152  GLU   A CB    1 
ATOM   1202  C  CG    . GLU   A 1 152 ? 147.986 147.290 121.827 1.00 121.50 ?  152  GLU   A CG    1 
ATOM   1203  C  CD    . GLU   A 1 152 ? 147.046 146.709 120.787 1.00 124.18 ?  152  GLU   A CD    1 
ATOM   1204  O  OE1   . GLU   A 1 152 ? 147.372 146.779 119.584 1.00 122.84 ?  152  GLU   A OE1   1 
ATOM   1205  O  OE2   . GLU   A 1 152 ? 145.982 146.182 121.175 1.00 125.14 ?  152  GLU   A OE2   1 
ATOM   1206  N  N     . GLY   A 1 153 ? 147.918 143.816 122.258 1.00 111.59 ?  153  GLY   A N     1 
ATOM   1207  C  CA    . GLY   A 1 153 ? 146.636 143.145 122.386 1.00 110.05 ?  153  GLY   A CA    1 
ATOM   1208  C  C     . GLY   A 1 153 ? 146.502 142.313 123.648 1.00 111.51 ?  153  GLY   A C     1 
ATOM   1209  O  O     . GLY   A 1 153 ? 145.471 142.366 124.325 1.00 115.28 ?  153  GLY   A O     1 
ATOM   1210  N  N     . LYS   A 1 154 ? 147.532 141.534 123.987 1.00 106.96 ?  154  LYS   A N     1 
ATOM   1211  C  CA    . LYS   A 1 154 ? 147.380 140.551 125.053 1.00 109.44 ?  154  LYS   A CA    1 
ATOM   1212  C  C     . LYS   A 1 154 ? 148.494 140.516 126.090 1.00 110.24 ?  154  LYS   A C     1 
ATOM   1213  O  O     . LYS   A 1 154 ? 148.342 139.805 127.088 1.00 114.67 ?  154  LYS   A O     1 
ATOM   1214  C  CB    . LYS   A 1 154 ? 147.233 139.141 124.458 1.00 109.13 ?  154  LYS   A CB    1 
ATOM   1215  C  CG    . LYS   A 1 154 ? 148.012 138.917 123.177 1.00 110.50 ?  154  LYS   A CG    1 
ATOM   1216  C  CD    . LYS   A 1 154 ? 147.486 137.709 122.421 1.00 111.05 ?  154  LYS   A CD    1 
ATOM   1217  C  CE    . LYS   A 1 154 ? 146.055 137.927 121.959 1.00 111.57 ?  154  LYS   A CE    1 
ATOM   1218  N  NZ    . LYS   A 1 154 ? 145.663 136.964 120.892 1.00 110.64 ?  154  LYS   A NZ    1 
ATOM   1219  N  N     . TYR   A 1 155 ? 149.596 141.237 125.903 1.00 105.27 ?  155  TYR   A N     1 
ATOM   1220  C  CA    . TYR   A 1 155 ? 150.743 141.100 126.794 1.00 105.48 ?  155  TYR   A CA    1 
ATOM   1221  C  C     . TYR   A 1 155 ? 150.836 142.231 127.814 1.00 106.09 ?  155  TYR   A C     1 
ATOM   1222  O  O     . TYR   A 1 155 ? 150.854 141.979 129.021 1.00 107.32 ?  155  TYR   A O     1 
ATOM   1223  C  CB    . TYR   A 1 155 ? 152.028 141.031 125.973 1.00 108.02 ?  155  TYR   A CB    1 
ATOM   1224  C  CG    . TYR   A 1 155 ? 152.538 139.639 125.671 1.00 107.15 ?  155  TYR   A CG    1 
ATOM   1225  C  CD1   . TYR   A 1 155 ? 151.693 138.654 125.177 1.00 105.49 ?  155  TYR   A CD1   1 
ATOM   1226  C  CD2   . TYR   A 1 155 ? 153.875 139.320 125.857 1.00 106.75 ?  155  TYR   A CD2   1 
ATOM   1227  C  CE1   . TYR   A 1 155 ? 152.167 137.387 124.891 1.00 108.76 ?  155  TYR   A CE1   1 
ATOM   1228  C  CE2   . TYR   A 1 155 ? 154.356 138.068 125.566 1.00 107.53 ?  155  TYR   A CE2   1 
ATOM   1229  C  CZ    . TYR   A 1 155 ? 153.499 137.100 125.093 1.00 110.67 ?  155  TYR   A CZ    1 
ATOM   1230  O  OH    . TYR   A 1 155 ? 153.982 135.844 124.809 1.00 110.40 ?  155  TYR   A OH    1 
ATOM   1231  N  N     . LEU   A 1 156 ? 150.908 143.475 127.348 1.00 114.23 ?  156  LEU   A N     1 
ATOM   1232  C  CA    . LEU   A 1 156 ? 151.072 144.601 128.257 1.00 112.32 ?  156  LEU   A CA    1 
ATOM   1233  C  C     . LEU   A 1 156 ? 149.803 144.822 129.069 1.00 112.86 ?  156  LEU   A C     1 
ATOM   1234  O  O     . LEU   A 1 156 ? 148.688 144.662 128.564 1.00 114.94 ?  156  LEU   A O     1 
ATOM   1235  C  CB    . LEU   A 1 156 ? 151.423 145.869 127.480 1.00 112.74 ?  156  LEU   A CB    1 
ATOM   1236  C  CG    . LEU   A 1 156 ? 152.528 145.751 126.430 1.00 114.11 ?  156  LEU   A CG    1 
ATOM   1237  C  CD1   . LEU   A 1 156 ? 152.427 146.877 125.415 1.00 112.64 ?  156  LEU   A CD1   1 
ATOM   1238  C  CD2   . LEU   A 1 156 ? 153.897 145.741 127.092 1.00 111.45 ?  156  LEU   A CD2   1 
ATOM   1239  N  N     . VAL   A 1 157 ? 149.977 145.185 130.341 1.00 115.33 ?  157  VAL   A N     1 
ATOM   1240  C  CA    . VAL   A 1 157 ? 148.830 145.498 131.182 1.00 117.90 ?  157  VAL   A CA    1 
ATOM   1241  C  C     . VAL   A 1 157 ? 148.172 146.775 130.677 1.00 118.82 ?  157  VAL   A C     1 
ATOM   1242  O  O     . VAL   A 1 157 ? 148.843 147.703 130.202 1.00 119.80 ?  157  VAL   A O     1 
ATOM   1243  C  CB    . VAL   A 1 157 ? 149.240 145.616 132.662 1.00 115.68 ?  157  VAL   A CB    1 
ATOM   1244  C  CG1   . VAL   A 1 157 ? 150.196 144.499 133.039 1.00 113.71 ?  157  VAL   A CG1   1 
ATOM   1245  C  CG2   . VAL   A 1 157 ? 149.858 146.974 132.961 1.00 118.11 ?  157  VAL   A CG2   1 
ATOM   1246  N  N     . GLN   A 1 158 ? 146.846 146.815 130.751 1.00 128.14 ?  158  GLN   A N     1 
ATOM   1247  C  CA    . GLN   A 1 158 ? 146.089 147.931 130.204 1.00 128.51 ?  158  GLN   A CA    1 
ATOM   1248  C  C     . GLN   A 1 158 ? 144.704 147.930 130.831 1.00 130.57 ?  158  GLN   A C     1 
ATOM   1249  O  O     . GLN   A 1 158 ? 144.283 146.956 131.459 1.00 132.70 ?  158  GLN   A O     1 
ATOM   1250  C  CB    . GLN   A 1 158 ? 145.996 147.843 128.678 1.00 129.00 ?  158  GLN   A CB    1 
ATOM   1251  C  CG    . GLN   A 1 158 ? 145.537 146.486 128.172 1.00 128.79 ?  158  GLN   A CG    1 
ATOM   1252  C  CD    . GLN   A 1 158 ? 145.845 146.273 126.705 1.00 130.82 ?  158  GLN   A CD    1 
ATOM   1253  O  OE1   . GLN   A 1 158 ? 145.155 146.798 125.831 1.00 131.42 ?  158  GLN   A OE1   1 
ATOM   1254  N  NE2   . GLN   A 1 158 ? 146.886 145.499 126.425 1.00 130.80 ?  158  GLN   A NE2   1 
ATOM   1255  N  N     . ASN   A 1 159 ? 144.000 149.042 130.652 1.00 141.56 ?  159  ASN   A N     1 
ATOM   1256  C  CA    . ASN   A 1 159 ? 142.611 149.152 131.072 1.00 141.52 ?  159  ASN   A CA    1 
ATOM   1257  C  C     . ASN   A 1 159 ? 141.720 148.608 129.965 1.00 143.31 ?  159  ASN   A C     1 
ATOM   1258  O  O     . ASN   A 1 159 ? 141.803 149.047 128.818 1.00 144.07 ?  159  ASN   A O     1 
ATOM   1259  C  CB    . ASN   A 1 159 ? 142.251 150.605 131.383 1.00 140.91 ?  159  ASN   A CB    1 
ATOM   1260  C  CG    . ASN   A 1 159 ? 141.437 150.743 132.652 1.00 140.59 ?  159  ASN   A CG    1 
ATOM   1261  O  OD1   . ASN   A 1 159 ? 140.301 150.276 132.728 1.00 140.97 ?  159  ASN   A OD1   1 
ATOM   1262  N  ND2   . ASN   A 1 159 ? 142.016 151.388 133.658 1.00 140.49 ?  159  ASN   A ND2   1 
ATOM   1263  N  N     . ARG   A 1 160 ? 140.857 147.653 130.298 1.00 146.52 ?  160  ARG   A N     1 
ATOM   1264  C  CA    . ARG   A 1 160 ? 140.041 147.012 129.236 1.00 146.95 ?  160  ARG   A CA    1 
ATOM   1265  C  C     . ARG   A 1 160 ? 138.809 147.864 128.905 1.00 147.55 ?  160  ARG   A C     1 
ATOM   1266  O  O     . ARG   A 1 160 ? 138.044 147.446 128.018 1.00 146.89 ?  160  ARG   A O     1 
ATOM   1267  C  CB    . ARG   A 1 160 ? 139.684 145.589 129.670 1.00 146.37 ?  160  ARG   A CB    1 
ATOM   1268  C  CG    . ARG   A 1 160 ? 140.862 144.628 129.595 1.00 146.52 ?  160  ARG   A CG    1 
ATOM   1269  C  CD    . ARG   A 1 160 ? 141.536 144.725 128.239 1.00 147.09 ?  160  ARG   A CD    1 
ATOM   1270  N  NE    . ARG   A 1 160 ? 142.690 143.847 128.108 1.00 147.46 ?  160  ARG   A NE    1 
ATOM   1271  C  CZ    . ARG   A 1 160 ? 143.433 143.744 127.013 1.00 146.98 ?  160  ARG   A CZ    1 
ATOM   1272  N  NH1   . ARG   A 1 160 ? 143.138 144.462 125.945 1.00 145.99 ?  160  ARG   A NH1   1 
ATOM   1273  N  NH2   . ARG   A 1 160 ? 144.469 142.923 126.990 1.00 145.89 ?  160  ARG   A NH2   1 
ATOM   1274  N  N     . VAL   A 1 161 ? 138.621 149.008 129.568 1.00 151.76 ?  161  VAL   A N     1 
ATOM   1275  C  CA    . VAL   A 1 161 ? 137.507 149.892 129.234 1.00 151.72 ?  161  VAL   A CA    1 
ATOM   1276  C  C     . VAL   A 1 161 ? 138.019 151.086 128.439 1.00 151.83 ?  161  VAL   A C     1 
ATOM   1277  O  O     . VAL   A 1 161 ? 137.622 151.294 127.287 1.00 151.74 ?  161  VAL   A O     1 
ATOM   1278  C  CB    . VAL   A 1 161 ? 136.761 150.352 130.499 1.00 150.13 ?  161  VAL   A CB    1 
ATOM   1279  C  CG1   . VAL   A 1 161 ? 135.464 151.051 130.124 1.00 149.59 ?  161  VAL   A CG1   1 
ATOM   1280  C  CG2   . VAL   A 1 161 ? 136.492 149.168 131.415 1.00 149.45 ?  161  VAL   A CG2   1 
ATOM   1281  N  N     . THR   A 1 162 ? 138.907 151.878 129.046 1.00 152.98 ?  162  THR   A N     1 
ATOM   1282  C  CA    . THR   A 1 162 ? 139.437 153.053 128.364 1.00 152.74 ?  162  THR   A CA    1 
ATOM   1283  C  C     . THR   A 1 162 ? 140.418 152.689 127.257 1.00 152.82 ?  162  THR   A C     1 
ATOM   1284  O  O     . THR   A 1 162 ? 140.668 153.515 126.373 1.00 152.57 ?  162  THR   A O     1 
ATOM   1285  C  CB    . THR   A 1 162 ? 140.113 153.992 129.366 1.00 151.88 ?  162  THR   A CB    1 
ATOM   1286  O  OG1   . THR   A 1 162 ? 140.800 153.222 130.359 1.00 152.09 ?  162  THR   A OG1   1 
ATOM   1287  C  CG2   . THR   A 1 162 ? 139.079 154.877 130.047 1.00 151.33 ?  162  THR   A CG2   1 
ATOM   1288  N  N     . GLY   A 1 163 ? 140.976 151.481 127.284 1.00 151.69 ?  163  GLY   A N     1 
ATOM   1289  C  CA    . GLY   A 1 163 ? 141.855 151.045 126.219 1.00 151.62 ?  163  GLY   A CA    1 
ATOM   1290  C  C     . GLY   A 1 163 ? 143.235 151.660 126.225 1.00 151.29 ?  163  GLY   A C     1 
ATOM   1291  O  O     . GLY   A 1 163 ? 143.898 151.674 125.185 1.00 150.72 ?  163  GLY   A O     1 
ATOM   1292  N  N     . GLU   A 1 164 ? 143.692 152.172 127.364 1.00 147.17 ?  164  GLU   A N     1 
ATOM   1293  C  CA    . GLU   A 1 164 ? 145.022 152.754 127.475 1.00 147.50 ?  164  GLU   A CA    1 
ATOM   1294  C  C     . GLU   A 1 164 ? 145.961 151.771 128.163 1.00 148.97 ?  164  GLU   A C     1 
ATOM   1295  O  O     . GLU   A 1 164 ? 145.553 151.027 129.060 1.00 149.36 ?  164  GLU   A O     1 
ATOM   1296  C  CB    . GLU   A 1 164 ? 144.980 154.083 128.236 1.00 146.51 ?  164  GLU   A CB    1 
ATOM   1297  C  CG    . GLU   A 1 164 ? 145.258 153.986 129.728 1.00 147.90 ?  164  GLU   A CG    1 
ATOM   1298  C  CD    . GLU   A 1 164 ? 144.818 155.224 130.483 1.00 149.84 ?  164  GLU   A CD    1 
ATOM   1299  O  OE1   . GLU   A 1 164 ? 145.682 155.892 131.088 1.00 149.52 ?  164  GLU   A OE1   1 
ATOM   1300  O  OE2   . GLU   A 1 164 ? 143.606 155.530 130.471 1.00 150.47 ?  164  GLU   A OE2   1 
ATOM   1301  N  N     . ILE   A 1 165 ? 147.213 151.754 127.718 1.00 137.64 ?  165  ILE   A N     1 
ATOM   1302  C  CA    . ILE   A 1 165 ? 148.213 150.847 128.253 1.00 136.70 ?  165  ILE   A CA    1 
ATOM   1303  C  C     . ILE   A 1 165 ? 149.035 151.584 129.301 1.00 134.94 ?  165  ILE   A C     1 
ATOM   1304  O  O     . ILE   A 1 165 ? 149.058 152.816 129.363 1.00 135.24 ?  165  ILE   A O     1 
ATOM   1305  C  CB    . ILE   A 1 165 ? 149.117 150.264 127.144 1.00 136.50 ?  165  ILE   A CB    1 
ATOM   1306  C  CG1   . ILE   A 1 165 ? 149.877 151.381 126.431 1.00 136.02 ?  165  ILE   A CG1   1 
ATOM   1307  C  CG2   . ILE   A 1 165 ? 148.292 149.462 126.152 1.00 134.61 ?  165  ILE   A CG2   1 
ATOM   1308  C  CD1   . ILE   A 1 165 ? 151.343 151.078 126.231 1.00 136.42 ?  165  ILE   A CD1   1 
ATOM   1309  N  N     . TYR   A 1 166 ? 149.728 150.814 130.141 1.00 126.65 ?  166  TYR   A N     1 
ATOM   1310  C  CA    . TYR   A 1 166 ? 150.462 151.372 131.266 1.00 126.15 ?  166  TYR   A CA    1 
ATOM   1311  C  C     . TYR   A 1 166 ? 151.940 151.010 131.308 1.00 126.69 ?  166  TYR   A C     1 
ATOM   1312  O  O     . TYR   A 1 166 ? 152.695 151.692 132.008 1.00 127.19 ?  166  TYR   A O     1 
ATOM   1313  C  CB    . TYR   A 1 166 ? 149.826 150.929 132.593 1.00 126.60 ?  166  TYR   A CB    1 
ATOM   1314  C  CG    . TYR   A 1 166 ? 148.378 151.326 132.761 1.00 127.12 ?  166  TYR   A CG    1 
ATOM   1315  C  CD1   . TYR   A 1 166 ? 148.006 152.660 132.841 1.00 126.65 ?  166  TYR   A CD1   1 
ATOM   1316  C  CD2   . TYR   A 1 166 ? 147.383 150.363 132.849 1.00 127.50 ?  166  TYR   A CD2   1 
ATOM   1317  C  CE1   . TYR   A 1 166 ? 146.682 153.024 132.998 1.00 127.18 ?  166  TYR   A CE1   1 
ATOM   1318  C  CE2   . TYR   A 1 166 ? 146.057 150.716 133.005 1.00 128.59 ?  166  TYR   A CE2   1 
ATOM   1319  C  CZ    . TYR   A 1 166 ? 145.712 152.048 133.079 1.00 129.07 ?  166  TYR   A CZ    1 
ATOM   1320  O  OH    . TYR   A 1 166 ? 144.392 152.404 133.235 1.00 129.88 ?  166  TYR   A OH    1 
ATOM   1321  N  N     . GLU   A 1 167 ? 152.376 149.974 130.596 1.00 119.75 ?  167  GLU   A N     1 
ATOM   1322  C  CA    . GLU   A 1 167 ? 153.740 149.482 130.729 1.00 118.84 ?  167  GLU   A CA    1 
ATOM   1323  C  C     . GLU   A 1 167 ? 154.335 149.213 129.355 1.00 118.62 ?  167  GLU   A C     1 
ATOM   1324  O  O     . GLU   A 1 167 ? 153.619 149.022 128.370 1.00 116.79 ?  167  GLU   A O     1 
ATOM   1325  C  CB    . GLU   A 1 167 ? 153.793 148.206 131.580 1.00 116.82 ?  167  GLU   A CB    1 
ATOM   1326  C  CG    . GLU   A 1 167 ? 153.028 147.044 130.975 1.00 118.05 ?  167  GLU   A CG    1 
ATOM   1327  C  CD    . GLU   A 1 167 ? 153.313 145.732 131.673 1.00 118.36 ?  167  GLU   A CD    1 
ATOM   1328  O  OE1   . GLU   A 1 167 ? 154.148 145.719 132.601 1.00 118.71 ?  167  GLU   A OE1   1 
ATOM   1329  O  OE2   . GLU   A 1 167 ? 152.707 144.710 131.289 1.00 119.04 ?  167  GLU   A OE2   1 
ATOM   1330  N  N     . SER   A 1 168 ? 155.663 149.200 129.305 1.00 112.94 ?  168  SER   A N     1 
ATOM   1331  C  CA    . SER   A 1 168 ? 156.409 148.870 128.101 1.00 112.85 ?  168  SER   A CA    1 
ATOM   1332  C  C     . SER   A 1 168 ? 156.874 147.417 128.150 1.00 114.04 ?  168  SER   A C     1 
ATOM   1333  O  O     . SER   A 1 168 ? 156.710 146.717 129.151 1.00 117.13 ?  168  SER   A O     1 
ATOM   1334  C  CB    . SER   A 1 168 ? 157.602 149.815 127.931 1.00 112.48 ?  168  SER   A CB    1 
ATOM   1335  O  OG    . SER   A 1 168 ? 158.532 149.659 128.988 1.00 111.07 ?  168  SER   A OG    1 
ATOM   1336  N  N     . ALA   A 1 169 ? 157.462 146.966 127.040 1.00 102.06 ?  169  ALA   A N     1 
ATOM   1337  C  CA    . ALA   A 1 169 ? 157.871 145.568 126.936 1.00 101.63 ?  169  ALA   A CA    1 
ATOM   1338  C  C     . ALA   A 1 169 ? 159.009 145.246 127.892 1.00 101.45 ?  169  ALA   A C     1 
ATOM   1339  O  O     . ALA   A 1 169 ? 159.023 144.176 128.515 1.00 106.09 ?  169  ALA   A O     1 
ATOM   1340  C  CB    . ALA   A 1 169 ? 158.265 145.241 125.498 1.00 102.46 ?  169  ALA   A CB    1 
ATOM   1341  N  N     . GLN   A 1 170 ? 159.968 146.163 128.011 1.00 95.11  ?  170  GLN   A N     1 
ATOM   1342  C  CA    . GLN   A 1 170 ? 161.144 145.897 128.875 1.00 94.86  ?  170  GLN   A CA    1 
ATOM   1343  C  C     . GLN   A 1 170 ? 160.674 145.775 130.323 1.00 98.92  ?  170  GLN   A C     1 
ATOM   1344  O  O     . GLN   A 1 170 ? 161.119 144.846 131.009 1.00 101.41 ?  170  GLN   A O     1 
ATOM   1345  C  CB    . GLN   A 1 170 ? 162.211 146.972 128.694 1.00 95.65  ?  170  GLN   A CB    1 
ATOM   1346  C  CG    . GLN   A 1 170 ? 162.888 146.939 127.334 1.00 99.22  ?  170  GLN   A CG    1 
ATOM   1347  C  CD    . GLN   A 1 170 ? 163.080 145.532 126.827 1.00 100.60 ?  170  GLN   A CD    1 
ATOM   1348  O  OE1   . GLN   A 1 170 ? 162.407 145.089 125.902 1.00 101.67 ?  170  GLN   A OE1   1 
ATOM   1349  N  NE2   . GLN   A 1 170 ? 164.013 144.818 127.433 1.00 98.51  ?  170  GLN   A NE2   1 
ATOM   1350  N  N     . PHE   A 1 171 ? 159.776 146.652 130.757 1.00 103.61 ?  171  PHE   A N     1 
ATOM   1351  C  CA    . PHE   A 1 171 ? 159.236 146.538 132.105 1.00 100.80 ?  171  PHE   A CA    1 
ATOM   1352  C  C     . PHE   A 1 171 ? 158.534 145.202 132.300 1.00 98.64  ?  171  PHE   A C     1 
ATOM   1353  O  O     . PHE   A 1 171 ? 158.695 144.553 133.339 1.00 103.58 ?  171  PHE   A O     1 
ATOM   1354  C  CB    . PHE   A 1 171 ? 158.279 147.695 132.381 1.00 102.39 ?  171  PHE   A CB    1 
ATOM   1355  C  CG    . PHE   A 1 171 ? 158.962 148.949 132.845 1.00 104.59 ?  171  PHE   A CG    1 
ATOM   1356  C  CD1   . PHE   A 1 171 ? 160.310 148.945 133.158 1.00 101.94 ?  171  PHE   A CD1   1 
ATOM   1357  C  CD2   . PHE   A 1 171 ? 158.256 150.132 132.969 1.00 104.76 ?  171  PHE   A CD2   1 
ATOM   1358  C  CE1   . PHE   A 1 171 ? 160.940 150.098 133.584 1.00 100.75 ?  171  PHE   A CE1   1 
ATOM   1359  C  CE2   . PHE   A 1 171 ? 158.880 151.288 133.395 1.00 104.06 ?  171  PHE   A CE2   1 
ATOM   1360  C  CZ    . PHE   A 1 171 ? 160.224 151.270 133.703 1.00 101.72 ?  171  PHE   A CZ    1 
ATOM   1361  N  N     . LEU   A 1 172 ? 157.760 144.770 131.302 1.00 85.80  ?  172  LEU   A N     1 
ATOM   1362  C  CA    . LEU   A 1 172 ? 157.088 143.477 131.379 1.00 84.64  ?  172  LEU   A CA    1 
ATOM   1363  C  C     . LEU   A 1 172 ? 158.094 142.351 131.586 1.00 85.23  ?  172  LEU   A C     1 
ATOM   1364  O  O     . LEU   A 1 172 ? 157.927 141.508 132.475 1.00 87.23  ?  172  LEU   A O     1 
ATOM   1365  C  CB    . LEU   A 1 172 ? 156.269 143.247 130.106 1.00 82.13  ?  172  LEU   A CB    1 
ATOM   1366  C  CG    . LEU   A 1 172 ? 155.457 141.959 129.949 1.00 84.81  ?  172  LEU   A CG    1 
ATOM   1367  C  CD1   . LEU   A 1 172 ? 154.149 142.255 129.241 1.00 90.08  ?  172  LEU   A CD1   1 
ATOM   1368  C  CD2   . LEU   A 1 172 ? 156.237 140.907 129.180 1.00 85.79  ?  172  LEU   A CD2   1 
ATOM   1369  N  N     . TYR   A 1 173 ? 159.158 142.334 130.780 1.00 83.65  ?  173  TYR   A N     1 
ATOM   1370  C  CA    . TYR   A 1 173 ? 160.143 141.260 130.870 1.00 80.91  ?  173  TYR   A CA    1 
ATOM   1371  C  C     . TYR   A 1 173 ? 160.866 141.280 132.212 1.00 84.05  ?  173  TYR   A C     1 
ATOM   1372  O  O     . TYR   A 1 173 ? 161.009 140.240 132.871 1.00 89.23  ?  173  TYR   A O     1 
ATOM   1373  C  CB    . TYR   A 1 173 ? 161.143 141.371 129.720 1.00 81.08  ?  173  TYR   A CB    1 
ATOM   1374  C  CG    . TYR   A 1 173 ? 160.568 141.002 128.373 1.00 83.21  ?  173  TYR   A CG    1 
ATOM   1375  C  CD1   . TYR   A 1 173 ? 159.535 140.084 128.268 1.00 82.58  ?  173  TYR   A CD1   1 
ATOM   1376  C  CD2   . TYR   A 1 173 ? 161.059 141.570 127.207 1.00 84.16  ?  173  TYR   A CD2   1 
ATOM   1377  C  CE1   . TYR   A 1 173 ? 159.006 139.741 127.040 1.00 82.83  ?  173  TYR   A CE1   1 
ATOM   1378  C  CE2   . TYR   A 1 173 ? 160.536 141.235 125.974 1.00 85.45  ?  173  TYR   A CE2   1 
ATOM   1379  C  CZ    . TYR   A 1 173 ? 159.510 140.320 125.896 1.00 86.63  ?  173  TYR   A CZ    1 
ATOM   1380  O  OH    . TYR   A 1 173 ? 158.985 139.981 124.671 1.00 90.62  ?  173  TYR   A OH    1 
ATOM   1381  N  N     . ILE   A 1 174 ? 161.323 142.459 132.640 1.00 81.92  ?  174  ILE   A N     1 
ATOM   1382  C  CA    . ILE   A 1 174 ? 162.094 142.541 133.877 1.00 82.21  ?  174  ILE   A CA    1 
ATOM   1383  C  C     . ILE   A 1 174 ? 161.222 142.188 135.075 1.00 82.53  ?  174  ILE   A C     1 
ATOM   1384  O  O     . ILE   A 1 174 ? 161.685 141.549 136.026 1.00 85.10  ?  174  ILE   A O     1 
ATOM   1385  C  CB    . ILE   A 1 174 ? 162.744 143.930 134.026 1.00 83.53  ?  174  ILE   A CB    1 
ATOM   1386  C  CG1   . ILE   A 1 174 ? 163.784 143.914 135.148 1.00 82.59  ?  174  ILE   A CG1   1 
ATOM   1387  C  CG2   . ILE   A 1 174 ? 161.703 144.998 134.302 1.00 84.41  ?  174  ILE   A CG2   1 
ATOM   1388  C  CD1   . ILE   A 1 174 ? 164.913 142.936 134.923 1.00 84.46  ?  174  ILE   A CD1   1 
ATOM   1389  N  N     . LEU   A 1 175 ? 159.941 142.564 135.043 1.00 86.08  ?  175  LEU   A N     1 
ATOM   1390  C  CA    . LEU   A 1 175 ? 159.068 142.259 136.166 1.00 84.85  ?  175  LEU   A CA    1 
ATOM   1391  C  C     . LEU   A 1 175 ? 158.648 140.798 136.179 1.00 87.48  ?  175  LEU   A C     1 
ATOM   1392  O  O     . LEU   A 1 175 ? 158.490 140.222 137.258 1.00 91.13  ?  175  LEU   A O     1 
ATOM   1393  C  CB    . LEU   A 1 175 ? 157.850 143.179 136.143 1.00 88.84  ?  175  LEU   A CB    1 
ATOM   1394  C  CG    . LEU   A 1 175 ? 158.205 144.599 136.585 1.00 87.95  ?  175  LEU   A CG    1 
ATOM   1395  C  CD1   . LEU   A 1 175 ? 157.244 145.610 135.997 1.00 87.25  ?  175  LEU   A CD1   1 
ATOM   1396  C  CD2   . LEU   A 1 175 ? 158.235 144.693 138.102 1.00 88.86  ?  175  LEU   A CD2   1 
ATOM   1397  N  N     . VAL   A 1 176 ? 158.484 140.177 135.008 1.00 83.85  ?  176  VAL   A N     1 
ATOM   1398  C  CA    . VAL   A 1 176 ? 158.271 138.734 134.973 1.00 80.02  ?  176  VAL   A CA    1 
ATOM   1399  C  C     . VAL   A 1 176 ? 159.474 138.014 135.567 1.00 80.95  ?  176  VAL   A C     1 
ATOM   1400  O  O     . VAL   A 1 176 ? 159.328 137.090 136.378 1.00 84.22  ?  176  VAL   A O     1 
ATOM   1401  C  CB    . VAL   A 1 176 ? 157.980 138.268 133.534 1.00 76.68  ?  176  VAL   A CB    1 
ATOM   1402  C  CG1   . VAL   A 1 176 ? 158.180 136.766 133.408 1.00 79.81  ?  176  VAL   A CG1   1 
ATOM   1403  C  CG2   . VAL   A 1 176 ? 156.567 138.652 133.129 1.00 78.05  ?  176  VAL   A CG2   1 
ATOM   1404  N  N     . ALA   A 1 177 ? 160.683 138.441 135.190 1.00 79.48  ?  177  ALA   A N     1 
ATOM   1405  C  CA    . ALA   A 1 177 ? 161.888 137.831 135.743 1.00 78.94  ?  177  ALA   A CA    1 
ATOM   1406  C  C     . ALA   A 1 177 ? 161.968 138.021 137.254 1.00 83.91  ?  177  ALA   A C     1 
ATOM   1407  O  O     . ALA   A 1 177 ? 162.305 137.085 137.988 1.00 86.50  ?  177  ALA   A O     1 
ATOM   1408  C  CB    . ALA   A 1 177 ? 163.129 138.411 135.065 1.00 75.60  ?  177  ALA   A CB    1 
ATOM   1409  N  N     . ALA   A 1 178 ? 161.663 139.228 137.736 1.00 90.06  ?  178  ALA   A N     1 
ATOM   1410  C  CA    . ALA   A 1 178 ? 161.733 139.499 139.169 1.00 88.21  ?  178  ALA   A CA    1 
ATOM   1411  C  C     . ALA   A 1 178 ? 160.698 138.692 139.944 1.00 89.14  ?  178  ALA   A C     1 
ATOM   1412  O  O     . ALA   A 1 178 ? 161.002 138.148 141.012 1.00 89.66  ?  178  ALA   A O     1 
ATOM   1413  C  CB    . ALA   A 1 178 ? 161.551 140.994 139.428 1.00 86.41  ?  178  ALA   A CB    1 
ATOM   1414  N  N     . CYS   A 1 179 ? 159.470 138.608 139.428 1.00 83.65  ?  179  CYS   A N     1 
ATOM   1415  C  CA    . CYS   A 1 179 ? 158.420 137.879 140.130 1.00 84.32  ?  179  CYS   A CA    1 
ATOM   1416  C  C     . CYS   A 1 179 ? 158.686 136.380 140.128 1.00 86.73  ?  179  CYS   A C     1 
ATOM   1417  O  O     . CYS   A 1 179 ? 158.401 135.695 141.117 1.00 92.12  ?  179  CYS   A O     1 
ATOM   1418  C  CB    . CYS   A 1 179 ? 157.061 138.185 139.501 1.00 86.45  ?  179  CYS   A CB    1 
ATOM   1419  S  SG    . CYS   A 1 179 ? 155.657 137.471 140.382 1.00 94.86  ?  179  CYS   A SG    1 
ATOM   1420  N  N     . LEU   A 1 180 ? 159.221 135.849 139.026 1.00 73.90  ?  180  LEU   A N     1 
ATOM   1421  C  CA    . LEU   A 1 180 ? 159.502 134.418 138.968 1.00 72.89  ?  180  LEU   A CA    1 
ATOM   1422  C  C     . LEU   A 1 180 ? 160.565 134.020 139.985 1.00 76.10  ?  180  LEU   A C     1 
ATOM   1423  O  O     . LEU   A 1 180 ? 160.419 133.010 140.681 1.00 81.26  ?  180  LEU   A O     1 
ATOM   1424  C  CB    . LEU   A 1 180 ? 159.931 134.023 137.556 1.00 75.87  ?  180  LEU   A CB    1 
ATOM   1425  C  CG    . LEU   A 1 180 ? 158.801 133.868 136.537 1.00 77.25  ?  180  LEU   A CG    1 
ATOM   1426  C  CD1   . LEU   A 1 180 ? 159.341 133.398 135.198 1.00 77.67  ?  180  LEU   A CD1   1 
ATOM   1427  C  CD2   . LEU   A 1 180 ? 157.737 132.915 137.057 1.00 72.83  ?  180  LEU   A CD2   1 
ATOM   1428  N  N     . PHE   A 1 181 ? 161.631 134.810 140.101 1.00 82.48  ?  181  PHE   A N     1 
ATOM   1429  C  CA    . PHE   A 1 181 ? 162.735 134.500 140.998 1.00 83.48  ?  181  PHE   A CA    1 
ATOM   1430  C  C     . PHE   A 1 181 ? 162.617 135.214 142.340 1.00 89.62  ?  181  PHE   A C     1 
ATOM   1431  O  O     . PHE   A 1 181 ? 163.632 135.431 143.009 1.00 93.24  ?  181  PHE   A O     1 
ATOM   1432  C  CB    . PHE   A 1 181 ? 164.066 134.844 140.329 1.00 81.75  ?  181  PHE   A CB    1 
ATOM   1433  C  CG    . PHE   A 1 181 ? 164.397 133.966 139.159 1.00 85.93  ?  181  PHE   A CG    1 
ATOM   1434  C  CD1   . PHE   A 1 181 ? 165.099 132.787 139.338 1.00 86.46  ?  181  PHE   A CD1   1 
ATOM   1435  C  CD2   . PHE   A 1 181 ? 164.000 134.315 137.880 1.00 87.27  ?  181  PHE   A CD2   1 
ATOM   1436  C  CE1   . PHE   A 1 181 ? 165.402 131.974 138.264 1.00 85.97  ?  181  PHE   A CE1   1 
ATOM   1437  C  CE2   . PHE   A 1 181 ? 164.300 133.506 136.803 1.00 85.54  ?  181  PHE   A CE2   1 
ATOM   1438  C  CZ    . PHE   A 1 181 ? 165.002 132.335 136.995 1.00 84.11  ?  181  PHE   A CZ    1 
ATOM   1439  N  N     . SER   A 1 182 ? 161.399 135.578 142.746 1.00 94.28  ?  182  SER   A N     1 
ATOM   1440  C  CA    . SER   A 1 182 ? 161.221 136.300 144.001 1.00 90.73  ?  182  SER   A CA    1 
ATOM   1441  C  C     . SER   A 1 182 ? 161.630 135.458 145.213 1.00 93.07  ?  182  SER   A C     1 
ATOM   1442  O  O     . SER   A 1 182 ? 162.267 135.969 146.134 1.00 96.30  ?  182  SER   A O     1 
ATOM   1443  C  CB    . SER   A 1 182 ? 159.772 136.768 144.135 1.00 91.20  ?  182  SER   A CB    1 
ATOM   1444  O  OG    . SER   A 1 182 ? 159.003 135.829 144.865 1.00 97.32  ?  182  SER   A OG    1 
ATOM   1445  N  N     . ASN   A 1 183 ? 161.265 134.178 145.260 1.00 93.72  ?  183  ASN   A N     1 
ATOM   1446  C  CA    . ASN   A 1 183 ? 161.555 133.390 146.467 1.00 92.40  ?  183  ASN   A CA    1 
ATOM   1447  C  C     . ASN   A 1 183 ? 162.915 132.716 146.403 1.00 95.15  ?  183  ASN   A C     1 
ATOM   1448  O  O     . ASN   A 1 183 ? 163.018 131.605 146.856 1.00 99.81  ?  183  ASN   A O     1 
ATOM   1449  C  CB    . ASN   A 1 183 ? 160.447 132.359 146.718 1.00 94.31  ?  183  ASN   A CB    1 
ATOM   1450  C  CG    . ASN   A 1 183 ? 159.098 133.010 146.909 1.00 99.72  ?  183  ASN   A CG    1 
ATOM   1451  O  OD1   . ASN   A 1 183 ? 158.667 133.806 146.080 1.00 104.48 ?  183  ASN   A OD1   1 
ATOM   1452  N  ND2   . ASN   A 1 183 ? 158.428 132.685 148.003 1.00 99.00  ?  183  ASN   A ND2   1 
ATOM   1453  N  N     . TYR   A 1 184 ? 163.966 133.421 146.021 1.00 94.20  ?  184  TYR   A N     1 
ATOM   1454  C  CA    . TYR   A 1 184 ? 165.321 132.940 145.822 1.00 95.42  ?  184  TYR   A CA    1 
ATOM   1455  C  C     . TYR   A 1 184 ? 166.247 133.552 146.863 1.00 99.29  ?  184  TYR   A C     1 
ATOM   1456  O  O     . TYR   A 1 184 ? 165.965 134.633 147.390 1.00 101.26 ?  184  TYR   A O     1 
ATOM   1457  C  CB    . TYR   A 1 184 ? 165.831 133.293 144.418 1.00 93.39  ?  184  TYR   A CB    1 
ATOM   1458  C  CG    . TYR   A 1 184 ? 165.886 132.114 143.472 1.00 92.40  ?  184  TYR   A CG    1 
ATOM   1459  C  CD1   . TYR   A 1 184 ? 164.727 131.466 143.072 1.00 94.99  ?  184  TYR   A CD1   1 
ATOM   1460  C  CD2   . TYR   A 1 184 ? 167.098 131.647 142.984 1.00 91.58  ?  184  TYR   A CD2   1 
ATOM   1461  C  CE1   . TYR   A 1 184 ? 164.772 130.387 142.211 1.00 97.18  ?  184  TYR   A CE1   1 
ATOM   1462  C  CE2   . TYR   A 1 184 ? 167.152 130.568 142.122 1.00 93.90  ?  184  TYR   A CE2   1 
ATOM   1463  C  CZ    . TYR   A 1 184 ? 165.986 129.943 141.740 1.00 97.52  ?  184  TYR   A CZ    1 
ATOM   1464  O  OH    . TYR   A 1 184 ? 166.036 128.868 140.882 1.00 95.10  ?  184  TYR   A OH    1 
ATOM   1465  N  N     . PRO   A 1 185 ? 167.346 132.876 147.198 1.00 109.03 ?  185  PRO   A N     1 
ATOM   1466  C  CA    . PRO   A 1 185 ? 168.316 133.471 148.122 1.00 106.22 ?  185  PRO   A CA    1 
ATOM   1467  C  C     . PRO   A 1 185 ? 168.860 134.780 147.572 1.00 110.20 ?  185  PRO   A C     1 
ATOM   1468  O  O     . PRO   A 1 185 ? 169.110 134.917 146.373 1.00 113.60 ?  185  PRO   A O     1 
ATOM   1469  C  CB    . PRO   A 1 185 ? 169.412 132.404 148.231 1.00 106.63 ?  185  PRO   A CB    1 
ATOM   1470  C  CG    . PRO   A 1 185 ? 169.203 131.502 147.059 1.00 108.57 ?  185  PRO   A CG    1 
ATOM   1471  C  CD    . PRO   A 1 185 ? 167.735 131.516 146.793 1.00 109.88 ?  185  PRO   A CD    1 
ATOM   1472  N  N     . ARG   A 1 186 ? 169.053 135.751 148.469 1.00 121.43 ?  186  ARG   A N     1 
ATOM   1473  C  CA    . ARG   A 1 186 ? 169.440 137.112 148.018 1.00 122.68 ?  186  ARG   A CA    1 
ATOM   1474  C  C     . ARG   A 1 186 ? 170.926 137.191 147.661 1.00 122.98 ?  186  ARG   A C     1 
ATOM   1475  O  O     . ARG   A 1 186 ? 171.372 138.295 147.310 1.00 124.30 ?  186  ARG   A O     1 
ATOM   1476  C  CB    . ARG   A 1 186 ? 168.984 138.091 149.102 1.00 120.91 ?  186  ARG   A CB    1 
ATOM   1477  C  CG    . ARG   A 1 186 ? 167.504 137.911 149.398 1.00 121.28 ?  186  ARG   A CG    1 
ATOM   1478  C  CD    . ARG   A 1 186 ? 166.815 139.200 149.792 1.00 123.34 ?  186  ARG   A CD    1 
ATOM   1479  N  NE    . ARG   A 1 186 ? 165.363 138.999 149.845 1.00 124.99 ?  186  ARG   A NE    1 
ATOM   1480  C  CZ    . ARG   A 1 186 ? 164.464 139.927 150.140 1.00 125.62 ?  186  ARG   A CZ    1 
ATOM   1481  N  NH1   . ARG   A 1 186 ? 164.814 141.196 150.251 1.00 125.28 ?  186  ARG   A NH1   1 
ATOM   1482  N  NH2   . ARG   A 1 186 ? 163.200 139.582 150.303 1.00 122.82 ?  186  ARG   A NH2   1 
ATOM   1483  N  N     . GLU   A 1 187 ? 171.679 136.110 147.803 1.00 123.63 ?  187  GLU   A N     1 
ATOM   1484  C  CA    . GLU   A 1 187 ? 173.047 136.098 147.298 1.00 123.43 ?  187  GLU   A CA    1 
ATOM   1485  C  C     . GLU   A 1 187 ? 173.080 135.993 145.778 1.00 124.26 ?  187  GLU   A C     1 
ATOM   1486  O  O     . GLU   A 1 187 ? 173.909 136.636 145.124 1.00 124.67 ?  187  GLU   A O     1 
ATOM   1487  C  CB    . GLU   A 1 187 ? 173.828 134.950 147.935 1.00 123.99 ?  187  GLU   A CB    1 
ATOM   1488  C  CG    . GLU   A 1 187 ? 173.286 133.570 147.599 1.00 126.25 ?  187  GLU   A CG    1 
ATOM   1489  C  CD    . GLU   A 1 187 ? 174.007 132.462 148.342 1.00 127.56 ?  187  GLU   A CD    1 
ATOM   1490  O  OE1   . GLU   A 1 187 ? 175.124 132.709 148.843 1.00 126.93 ?  187  GLU   A OE1   1 
ATOM   1491  O  OE2   . GLU   A 1 187 ? 173.458 131.343 148.422 1.00 128.02 ?  187  GLU   A OE2   1 
ATOM   1492  N  N     . THR   A 1 188 ? 172.186 135.192 145.196 1.00 115.22 ?  188  THR   A N     1 
ATOM   1493  C  CA    . THR   A 1 188 ? 172.200 134.925 143.762 1.00 113.94 ?  188  THR   A CA    1 
ATOM   1494  C  C     . THR   A 1 188 ? 170.902 135.315 143.064 1.00 114.75 ?  188  THR   A C     1 
ATOM   1495  O  O     . THR   A 1 188 ? 170.727 134.984 141.886 1.00 116.05 ?  188  THR   A O     1 
ATOM   1496  C  CB    . THR   A 1 188 ? 172.491 133.443 143.501 1.00 115.13 ?  188  THR   A CB    1 
ATOM   1497  O  OG1   . THR   A 1 188 ? 171.412 132.647 144.005 1.00 114.37 ?  188  THR   A OG1   1 
ATOM   1498  C  CG2   . THR   A 1 188 ? 173.783 133.022 144.184 1.00 114.16 ?  188  THR   A CG2   1 
ATOM   1499  N  N     . ARG   A 1 189 ? 169.998 135.997 143.764 1.00 103.18 ?  189  ARG   A N     1 
ATOM   1500  C  CA    . ARG   A 1 189 ? 168.682 136.313 143.164 1.00 101.09 ?  189  ARG   A CA    1 
ATOM   1501  C  C     . ARG   A 1 189 ? 168.866 137.343 142.055 1.00 101.56 ?  189  ARG   A C     1 
ATOM   1502  O  O     . ARG   A 1 189 ? 168.238 137.152 141.035 1.00 102.68 ?  189  ARG   A O     1 
ATOM   1503  C  CB    . ARG   A 1 189 ? 167.663 136.912 144.131 1.00 99.44  ?  189  ARG   A CB    1 
ATOM   1504  C  CG    . ARG   A 1 189 ? 166.246 136.985 143.588 1.00 100.92 ?  189  ARG   A CG    1 
ATOM   1505  C  CD    . ARG   A 1 189 ? 165.260 137.371 144.672 1.00 99.79  ?  189  ARG   A CD    1 
ATOM   1506  N  NE    . ARG   A 1 189 ? 165.585 138.679 145.245 1.00 103.93 ?  189  ARG   A NE    1 
ATOM   1507  C  CZ    . ARG   A 1 189 ? 164.876 139.309 146.166 1.00 105.10 ?  189  ARG   A CZ    1 
ATOM   1508  N  NH1   . ARG   A 1 189 ? 163.635 138.945 146.427 1.00 102.59 ?  189  ARG   A NH1   1 
ATOM   1509  N  NH2   . ARG   A 1 189 ? 165.405 140.332 146.805 1.00 105.26 ?  189  ARG   A NH2   1 
ATOM   1510  N  N     . LEU   A 1 190 ? 169.650 138.401 142.257 1.00 104.27 ?  190  LEU   A N     1 
ATOM   1511  C  CA    . LEU   A 1 190 ? 169.766 139.476 141.277 1.00 104.38 ?  190  LEU   A CA    1 
ATOM   1512  C  C     . LEU   A 1 190 ? 170.425 138.992 139.992 1.00 105.39 ?  190  LEU   A C     1 
ATOM   1513  O  O     . LEU   A 1 190 ? 169.998 139.364 138.892 1.00 104.31 ?  190  LEU   A O     1 
ATOM   1514  C  CB    . LEU   A 1 190 ? 170.542 140.649 141.874 1.00 103.55 ?  190  LEU   A CB    1 
ATOM   1515  C  CG    . LEU   A 1 190 ? 169.690 141.862 142.250 1.00 105.46 ?  190  LEU   A CG    1 
ATOM   1516  C  CD1   . LEU   A 1 190 ? 169.028 142.451 141.014 1.00 105.60 ?  190  LEU   A CD1   1 
ATOM   1517  C  CD2   . LEU   A 1 190 ? 168.647 141.483 143.287 1.00 107.48 ?  190  LEU   A CD2   1 
ATOM   1518  N  N     . GLN   A 1 191 ? 171.468 138.167 140.106 1.00 107.70 ?  191  GLN   A N     1 
ATOM   1519  C  CA    A GLN   A 1 191 ? 172.120 137.649 138.908 0.50 105.91 ?  191  GLN   A CA    1 
ATOM   1520  C  CA    B GLN   A 1 191 ? 172.220 137.649 138.908 0.50 105.91 ?  191  GLN   A CA    1 
ATOM   1521  C  C     . GLN   A 1 191 ? 171.184 136.736 138.122 1.00 108.92 ?  191  GLN   A C     1 
ATOM   1522  O  O     . GLN   A 1 191 ? 171.169 136.775 136.887 1.00 113.30 ?  191  GLN   A O     1 
ATOM   1523  C  CB    A GLN   A 1 191 ? 173.420 136.930 139.280 0.50 103.30 ?  191  GLN   A CB    1 
ATOM   1524  C  CB    B GLN   A 1 191 ? 173.520 136.930 139.280 0.50 103.30 ?  191  GLN   A CB    1 
ATOM   1525  C  CG    A GLN   A 1 191 ? 173.250 135.632 140.051 0.50 107.37 ?  191  GLN   A CG    1 
ATOM   1526  C  CG    B GLN   A 1 191 ? 174.604 137.810 139.878 0.50 107.37 ?  191  GLN   A CG    1 
ATOM   1527  C  CD    A GLN   A 1 191 ? 173.782 134.431 139.294 0.50 112.51 ?  191  GLN   A CD    1 
ATOM   1528  C  CD    B GLN   A 1 191 ? 175.833 137.023 140.289 0.50 112.51 ?  191  GLN   A CD    1 
ATOM   1529  O  OE1   A GLN   A 1 191 ? 174.000 134.494 138.084 0.50 114.07 ?  191  GLN   A OE1   1 
ATOM   1530  O  OE1   B GLN   A 1 191 ? 175.752 135.826 140.566 0.50 114.07 ?  191  GLN   A OE1   1 
ATOM   1531  N  NE2   A GLN   A 1 191 ? 173.993 133.329 140.003 0.50 110.26 ?  191  GLN   A NE2   1 
ATOM   1532  N  NE2   B GLN   A 1 191 ? 176.979 137.691 140.332 0.50 110.26 ?  191  GLN   A NE2   1 
ATOM   1533  N  N     . TYR   A 1 192 ? 170.387 135.919 138.817 1.00 96.77  ?  192  TYR   A N     1 
ATOM   1534  C  CA    . TYR   A 1 192 ? 169.420 135.071 138.128 1.00 95.83  ?  192  TYR   A CA    1 
ATOM   1535  C  C     . TYR   A 1 192 ? 168.366 135.908 137.416 1.00 95.19  ?  192  TYR   A C     1 
ATOM   1536  O  O     . TYR   A 1 192 ? 167.982 135.602 136.280 1.00 98.65  ?  192  TYR   A O     1 
ATOM   1537  C  CB    . TYR   A 1 192 ? 168.761 134.111 139.117 1.00 92.43  ?  192  TYR   A CB    1 
ATOM   1538  C  CG    . TYR   A 1 192 ? 169.462 132.778 139.236 1.00 95.34  ?  192  TYR   A CG    1 
ATOM   1539  C  CD1   . TYR   A 1 192 ? 169.860 132.079 138.106 1.00 93.11  ?  192  TYR   A CD1   1 
ATOM   1540  C  CD2   . TYR   A 1 192 ? 169.726 132.220 140.478 1.00 96.87  ?  192  TYR   A CD2   1 
ATOM   1541  C  CE1   . TYR   A 1 192 ? 170.502 130.861 138.210 1.00 93.73  ?  192  TYR   A CE1   1 
ATOM   1542  C  CE2   . TYR   A 1 192 ? 170.367 131.002 140.592 1.00 94.56  ?  192  TYR   A CE2   1 
ATOM   1543  C  CZ    . TYR   A 1 192 ? 170.753 130.327 139.455 1.00 94.42  ?  192  TYR   A CZ    1 
ATOM   1544  O  OH    . TYR   A 1 192 ? 171.392 129.114 139.563 1.00 95.73  ?  192  TYR   A OH    1 
ATOM   1545  N  N     . VAL   A 1 193 ? 167.889 136.970 138.068 1.00 86.03  ?  193  VAL   A N     1 
ATOM   1546  C  CA    . VAL   A 1 193 ? 166.907 137.852 137.443 1.00 84.97  ?  193  VAL   A CA    1 
ATOM   1547  C  C     . VAL   A 1 193 ? 167.500 138.509 136.205 1.00 84.33  ?  193  VAL   A C     1 
ATOM   1548  O  O     . VAL   A 1 193 ? 166.852 138.585 135.154 1.00 87.21  ?  193  VAL   A O     1 
ATOM   1549  C  CB    . VAL   A 1 193 ? 166.407 138.898 138.458 1.00 85.65  ?  193  VAL   A CB    1 
ATOM   1550  C  CG1   . VAL   A 1 193 ? 165.691 140.035 137.747 1.00 84.96  ?  193  VAL   A CG1   1 
ATOM   1551  C  CG2   . VAL   A 1 193 ? 165.493 138.247 139.482 1.00 87.50  ?  193  VAL   A CG2   1 
ATOM   1552  N  N     . LYS   A 1 194 ? 168.744 138.982 136.305 1.00 87.82  ?  194  LYS   A N     1 
ATOM   1553  C  CA    . LYS   A 1 194 ? 169.397 139.610 135.161 1.00 88.93  ?  194  LYS   A CA    1 
ATOM   1554  C  C     . LYS   A 1 194 ? 169.562 138.629 134.007 1.00 90.21  ?  194  LYS   A C     1 
ATOM   1555  O  O     . LYS   A 1 194 ? 169.288 138.969 132.850 1.00 91.37  ?  194  LYS   A O     1 
ATOM   1556  C  CB    . LYS   A 1 194 ? 170.753 140.176 135.584 1.00 87.34  ?  194  LYS   A CB    1 
ATOM   1557  C  CG    . LYS   A 1 194 ? 171.768 140.282 134.461 1.00 88.85  ?  194  LYS   A CG    1 
ATOM   1558  C  CD    . LYS   A 1 194 ? 172.813 141.342 134.763 1.00 91.67  ?  194  LYS   A CD    1 
ATOM   1559  C  CE    . LYS   A 1 194 ? 173.496 141.821 133.494 1.00 91.79  ?  194  LYS   A CE    1 
ATOM   1560  N  NZ    . LYS   A 1 194 ? 174.710 141.018 133.184 1.00 92.60  ?  194  LYS   A NZ    1 
ATOM   1561  N  N     . ARG   A 1 195 ? 170.005 137.405 134.303 1.00 87.84  ?  195  ARG   A N     1 
ATOM   1562  C  CA    . ARG   A 1 195 ? 170.207 136.417 133.248 1.00 84.51  ?  195  ARG   A CA    1 
ATOM   1563  C  C     . ARG   A 1 195 ? 168.890 136.030 132.587 1.00 86.67  ?  195  ARG   A C     1 
ATOM   1564  O  O     . ARG   A 1 195 ? 168.819 135.915 131.357 1.00 91.61  ?  195  ARG   A O     1 
ATOM   1565  C  CB    . ARG   A 1 195 ? 170.917 135.186 133.811 1.00 83.30  ?  195  ARG   A CB    1 
ATOM   1566  C  CG    . ARG   A 1 195 ? 172.334 135.468 134.282 1.00 87.09  ?  195  ARG   A CG    1 
ATOM   1567  C  CD    . ARG   A 1 195 ? 173.235 134.256 134.141 1.00 89.11  ?  195  ARG   A CD    1 
ATOM   1568  N  NE    . ARG   A 1 195 ? 172.510 133.003 134.305 1.00 93.59  ?  195  ARG   A NE    1 
ATOM   1569  C  CZ    . ARG   A 1 195 ? 172.705 132.152 135.303 1.00 94.42  ?  195  ARG   A CZ    1 
ATOM   1570  N  NH1   . ARG   A 1 195 ? 173.587 132.397 136.258 1.00 89.87  ?  195  ARG   A NH1   1 
ATOM   1571  N  NH2   . ARG   A 1 195 ? 171.996 131.027 135.344 1.00 92.86  ?  195  ARG   A NH2   1 
ATOM   1572  N  N     . PHE   A 1 196 ? 167.832 135.832 133.378 1.00 77.12  ?  196  PHE   A N     1 
ATOM   1573  C  CA    . PHE   A 1 196 ? 166.541 135.489 132.792 1.00 75.16  ?  196  PHE   A CA    1 
ATOM   1574  C  C     . PHE   A 1 196 ? 165.984 136.640 131.964 1.00 83.00  ?  196  PHE   A C     1 
ATOM   1575  O  O     . PHE   A 1 196 ? 165.396 136.417 130.898 1.00 91.22  ?  196  PHE   A O     1 
ATOM   1576  C  CB    . PHE   A 1 196 ? 165.549 135.084 133.880 1.00 75.65  ?  196  PHE   A CB    1 
ATOM   1577  C  CG    . PHE   A 1 196 ? 164.257 134.543 133.341 1.00 73.74  ?  196  PHE   A CG    1 
ATOM   1578  C  CD1   . PHE   A 1 196 ? 164.220 133.321 132.695 1.00 80.39  ?  196  PHE   A CD1   1 
ATOM   1579  C  CD2   . PHE   A 1 196 ? 163.082 135.260 133.472 1.00 78.38  ?  196  PHE   A CD2   1 
ATOM   1580  C  CE1   . PHE   A 1 196 ? 163.035 132.823 132.192 1.00 82.21  ?  196  PHE   A CE1   1 
ATOM   1581  C  CE2   . PHE   A 1 196 ? 161.893 134.766 132.974 1.00 79.36  ?  196  PHE   A CE2   1 
ATOM   1582  C  CZ    . PHE   A 1 196 ? 161.869 133.545 132.334 1.00 79.47  ?  196  PHE   A CZ    1 
ATOM   1583  N  N     . TYR   A 1 197 ? 166.149 137.878 132.438 1.00 88.15  ?  197  TYR   A N     1 
ATOM   1584  C  CA    . TYR   A 1 197 ? 165.694 139.026 131.663 1.00 86.88  ?  197  TYR   A CA    1 
ATOM   1585  C  C     . TYR   A 1 197 ? 166.451 139.132 130.347 1.00 88.13  ?  197  TYR   A C     1 
ATOM   1586  O  O     . TYR   A 1 197 ? 165.858 139.433 129.306 1.00 92.30  ?  197  TYR   A O     1 
ATOM   1587  C  CB    . TYR   A 1 197 ? 165.853 140.313 132.472 1.00 87.28  ?  197  TYR   A CB    1 
ATOM   1588  C  CG    . TYR   A 1 197 ? 165.902 141.551 131.609 1.00 86.32  ?  197  TYR   A CG    1 
ATOM   1589  C  CD1   . TYR   A 1 197 ? 164.736 142.142 131.145 1.00 86.33  ?  197  TYR   A CD1   1 
ATOM   1590  C  CD2   . TYR   A 1 197 ? 167.113 142.122 131.246 1.00 87.87  ?  197  TYR   A CD2   1 
ATOM   1591  C  CE1   . TYR   A 1 197 ? 164.773 143.267 130.351 1.00 86.96  ?  197  TYR   A CE1   1 
ATOM   1592  C  CE2   . TYR   A 1 197 ? 167.160 143.249 130.451 1.00 89.93  ?  197  TYR   A CE2   1 
ATOM   1593  C  CZ    . TYR   A 1 197 ? 165.987 143.817 130.006 1.00 92.01  ?  197  TYR   A CZ    1 
ATOM   1594  O  OH    . TYR   A 1 197 ? 166.026 144.941 129.213 1.00 95.84  ?  197  TYR   A OH    1 
ATOM   1595  N  N     . ASP   A 1 198 ? 167.765 138.903 130.377 1.00 91.97  ?  198  ASP   A N     1 
ATOM   1596  C  CA    . ASP   A 1 198 ? 168.543 138.927 129.143 1.00 94.69  ?  198  ASP   A CA    1 
ATOM   1597  C  C     . ASP   A 1 198 ? 168.094 137.827 128.191 1.00 97.01  ?  198  ASP   A C     1 
ATOM   1598  O  O     . ASP   A 1 198 ? 167.997 138.047 126.979 1.00 100.28 ?  198  ASP   A O     1 
ATOM   1599  C  CB    . ASP   A 1 198 ? 170.032 138.791 129.456 1.00 94.60  ?  198  ASP   A CB    1 
ATOM   1600  C  CG    . ASP   A 1 198 ? 170.626 140.063 130.023 1.00 99.93  ?  198  ASP   A CG    1 
ATOM   1601  O  OD1   . ASP   A 1 198 ? 169.980 141.125 129.906 1.00 100.45 ?  198  ASP   A OD1   1 
ATOM   1602  O  OD2   . ASP   A 1 198 ? 171.740 140.003 130.583 1.00 102.40 ?  198  ASP   A OD2   1 
ATOM   1603  N  N     . ALA   A 1 199 ? 167.817 136.635 128.722 1.00 84.99  ?  199  ALA   A N     1 
ATOM   1604  C  CA    . ALA   A 1 199 ? 167.376 135.533 127.874 1.00 82.05  ?  199  ALA   A CA    1 
ATOM   1605  C  C     . ALA   A 1 199 ? 166.026 135.827 127.230 1.00 81.24  ?  199  ALA   A C     1 
ATOM   1606  O  O     . ALA   A 1 199 ? 165.826 135.558 126.040 1.00 88.33  ?  199  ALA   A O     1 
ATOM   1607  C  CB    . ALA   A 1 199 ? 167.309 134.243 128.689 1.00 81.65  ?  199  ALA   A CB    1 
ATOM   1608  N  N     . VAL   A 1 200 ? 165.086 136.376 128.000 1.00 76.65  ?  200  VAL   A N     1 
ATOM   1609  C  CA    . VAL   A 1 200 ? 163.734 136.583 127.487 1.00 79.99  ?  200  VAL   A CA    1 
ATOM   1610  C  C     . VAL   A 1 200 ? 163.676 137.787 126.553 1.00 82.23  ?  200  VAL   A C     1 
ATOM   1611  O  O     . VAL   A 1 200 ? 163.059 137.727 125.484 1.00 87.30  ?  200  VAL   A O     1 
ATOM   1612  C  CB    . VAL   A 1 200 ? 162.742 136.720 128.656 1.00 78.92  ?  200  VAL   A CB    1 
ATOM   1613  C  CG1   . VAL   A 1 200 ? 161.383 137.158 128.148 1.00 81.33  ?  200  VAL   A CG1   1 
ATOM   1614  C  CG2   . VAL   A 1 200 ? 162.626 135.405 129.404 1.00 79.83  ?  200  VAL   A CG2   1 
ATOM   1615  N  N     . SER   A 1 201 ? 164.311 138.897 126.938 1.00 87.44  ?  201  SER   A N     1 
ATOM   1616  C  CA    . SER   A 1 201 ? 164.239 140.115 126.138 1.00 90.23  ?  201  SER   A CA    1 
ATOM   1617  C  C     . SER   A 1 201 ? 164.948 139.962 124.798 1.00 92.75  ?  201  SER   A C     1 
ATOM   1618  O  O     . SER   A 1 201 ? 164.604 140.654 123.834 1.00 93.32  ?  201  SER   A O     1 
ATOM   1619  C  CB    . SER   A 1 201 ? 164.831 141.287 126.920 1.00 88.21  ?  201  SER   A CB    1 
ATOM   1620  O  OG    . SER   A 1 201 ? 166.168 141.021 127.304 1.00 91.50  ?  201  SER   A OG    1 
ATOM   1621  N  N     . THR   A 1 202 ? 165.940 139.077 124.719 1.00 82.43  ?  202  THR   A N     1 
ATOM   1622  C  CA    . THR   A 1 202 ? 166.659 138.822 123.478 1.00 80.67  ?  202  THR   A CA    1 
ATOM   1623  C  C     . THR   A 1 202 ? 165.902 137.858 122.564 1.00 83.06  ?  202  THR   A C     1 
ATOM   1624  O  O     . THR   A 1 202 ? 166.283 137.695 121.398 1.00 87.88  ?  202  THR   A O     1 
ATOM   1625  C  CB    . THR   A 1 202 ? 168.076 138.324 123.834 1.00 81.58  ?  202  THR   A CB    1 
ATOM   1626  O  OG1   . THR   A 1 202 ? 168.854 139.430 124.306 1.00 85.09  ?  202  THR   A OG1   1 
ATOM   1627  C  CG2   . THR   A 1 202 ? 168.815 137.699 122.661 1.00 81.50  ?  202  THR   A CG2   1 
ATOM   1628  N  N     . PHE   A 1 203 ? 164.791 137.293 123.048 1.00 86.58  ?  203  PHE   A N     1 
ATOM   1629  C  CA    . PHE   A 1 203 ? 163.971 136.319 122.318 1.00 85.19  ?  203  PHE   A CA    1 
ATOM   1630  C  C     . PHE   A 1 203 ? 164.689 134.980 122.179 1.00 91.01  ?  203  PHE   A C     1 
ATOM   1631  O  O     . PHE   A 1 203 ? 164.682 134.369 121.112 1.00 98.27  ?  203  PHE   A O     1 
ATOM   1632  C  CB    . PHE   A 1 203 ? 163.534 136.832 120.941 1.00 88.33  ?  203  PHE   A CB    1 
ATOM   1633  C  CG    . PHE   A 1 203 ? 162.960 138.215 120.957 1.00 91.87  ?  203  PHE   A CG    1 
ATOM   1634  C  CD1   . PHE   A 1 203 ? 162.104 138.616 121.967 1.00 91.65  ?  203  PHE   A CD1   1 
ATOM   1635  C  CD2   . PHE   A 1 203 ? 163.272 139.114 119.953 1.00 92.13  ?  203  PHE   A CD2   1 
ATOM   1636  C  CE1   . PHE   A 1 203 ? 161.575 139.890 121.976 1.00 92.62  ?  203  PHE   A CE1   1 
ATOM   1637  C  CE2   . PHE   A 1 203 ? 162.746 140.388 119.956 1.00 91.71  ?  203  PHE   A CE2   1 
ATOM   1638  C  CZ    . PHE   A 1 203 ? 161.898 140.776 120.969 1.00 91.39  ?  203  PHE   A CZ    1 
ATOM   1639  N  N     . LYS   A 1 204 ? 165.319 134.525 123.259 1.00 81.78  ?  204  LYS   A N     1 
ATOM   1640  C  CA    . LYS   A 1 204 ? 165.921 133.199 123.305 1.00 77.76  ?  204  LYS   A CA    1 
ATOM   1641  C  C     . LYS   A 1 204 ? 165.044 132.183 124.020 1.00 78.33  ?  204  LYS   A C     1 
ATOM   1642  O  O     . LYS   A 1 204 ? 165.000 131.016 123.620 1.00 82.95  ?  204  LYS   A O     1 
ATOM   1643  C  CB    . LYS   A 1 204 ? 167.290 133.262 123.985 1.00 74.31  ?  204  LYS   A CB    1 
ATOM   1644  C  CG    . LYS   A 1 204 ? 168.309 134.076 123.216 1.00 80.23  ?  204  LYS   A CG    1 
ATOM   1645  C  CD    . LYS   A 1 204 ? 169.556 134.318 124.038 1.00 79.26  ?  204  LYS   A CD    1 
ATOM   1646  C  CE    . LYS   A 1 204 ? 170.753 134.561 123.141 1.00 80.25  ?  204  LYS   A CE    1 
ATOM   1647  N  NZ    . LYS   A 1 204 ? 171.917 135.082 123.906 1.00 82.32  ?  204  LYS   A NZ    1 
ATOM   1648  N  N     . ILE   A 1 205 ? 164.345 132.603 125.070 1.00 71.16  ?  205  ILE   A N     1 
ATOM   1649  C  CA    . ILE   A 1 205 ? 163.391 131.765 125.782 1.00 65.37  ?  205  ILE   A CA    1 
ATOM   1650  C  C     . ILE   A 1 205 ? 162.023 132.417 125.666 1.00 67.21  ?  205  ILE   A C     1 
ATOM   1651  O  O     . ILE   A 1 205 ? 161.862 133.595 126.004 1.00 79.88  ?  205  ILE   A O     1 
ATOM   1652  C  CB    . ILE   A 1 205 ? 163.782 131.579 127.259 1.00 67.87  ?  205  ILE   A CB    1 
ATOM   1653  C  CG1   . ILE   A 1 205 ? 165.011 130.678 127.378 1.00 74.07  ?  205  ILE   A CG1   1 
ATOM   1654  C  CG2   . ILE   A 1 205 ? 162.620 131.001 128.051 1.00 66.11  ?  205  ILE   A CG2   1 
ATOM   1655  C  CD1   . ILE   A 1 205 ? 165.720 130.804 128.702 1.00 77.30  ?  205  ILE   A CD1   1 
ATOM   1656  N  N     . SER   A 1 206 ? 161.046 131.659 125.184 1.00 76.04  ?  206  SER   A N     1 
ATOM   1657  C  CA    . SER   A 1 206 ? 159.682 132.139 125.038 1.00 78.68  ?  206  SER   A CA    1 
ATOM   1658  C  C     . SER   A 1 206 ? 158.777 131.416 126.023 1.00 80.81  ?  206  SER   A C     1 
ATOM   1659  O  O     . SER   A 1 206 ? 158.925 130.212 126.248 1.00 89.43  ?  206  SER   A O     1 
ATOM   1660  C  CB    . SER   A 1 206 ? 159.173 131.931 123.611 1.00 80.02  ?  206  SER   A CB    1 
ATOM   1661  O  OG    . SER   A 1 206 ? 157.772 131.733 123.604 1.00 85.32  ?  206  SER   A OG    1 
ATOM   1662  N  N     . LEU   A 1 207 ? 157.846 132.158 126.610 1.00 85.78  ?  207  LEU   A N     1 
ATOM   1663  C  CA    . LEU   A 1 207 ? 156.908 131.641 127.589 1.00 88.92  ?  207  LEU   A CA    1 
ATOM   1664  C  C     . LEU   A 1 207 ? 155.492 132.046 127.201 1.00 88.31  ?  207  LEU   A C     1 
ATOM   1665  O  O     . LEU   A 1 207 ? 155.294 133.079 126.553 1.00 90.15  ?  207  LEU   A O     1 
ATOM   1666  C  CB    . LEU   A 1 207 ? 157.257 132.156 128.996 1.00 87.86  ?  207  LEU   A CB    1 
ATOM   1667  C  CG    . LEU   A 1 207 ? 158.754 132.198 129.353 1.00 90.53  ?  207  LEU   A CG    1 
ATOM   1668  C  CD1   . LEU   A 1 207 ? 159.423 133.540 129.069 1.00 90.33  ?  207  LEU   A CD1   1 
ATOM   1669  C  CD2   . LEU   A 1 207 ? 158.963 131.813 130.802 1.00 90.41  ?  207  LEU   A CD2   1 
ATOM   1670  N  N     . PRO   A 1 208 ? 154.491 131.252 127.580 1.00 80.69  ?  208  PRO   A N     1 
ATOM   1671  C  CA    . PRO   A 1 208 ? 153.153 131.412 127.000 1.00 81.65  ?  208  PRO   A CA    1 
ATOM   1672  C  C     . PRO   A 1 208 ? 152.503 132.739 127.362 1.00 84.64  ?  208  PRO   A C     1 
ATOM   1673  O  O     . PRO   A 1 208 ? 152.930 133.457 128.268 1.00 88.94  ?  208  PRO   A O     1 
ATOM   1674  C  CB    . PRO   A 1 208 ? 152.365 130.235 127.591 1.00 84.17  ?  208  PRO   A CB    1 
ATOM   1675  C  CG    . PRO   A 1 208 ? 153.403 129.258 128.031 1.00 83.45  ?  208  PRO   A CG    1 
ATOM   1676  C  CD    . PRO   A 1 208 ? 154.558 130.089 128.479 1.00 80.06  ?  208  PRO   A CD    1 
ATOM   1677  N  N     . THR   A 1 209 ? 151.450 133.058 126.610 1.00 95.10  ?  209  THR   A N     1 
ATOM   1678  C  CA    . THR   A 1 209 ? 150.713 134.298 126.837 1.00 97.49  ?  209  THR   A CA    1 
ATOM   1679  C  C     . THR   A 1 209 ? 150.138 134.423 128.246 1.00 100.44 ?  209  THR   A C     1 
ATOM   1680  O  O     . THR   A 1 209 ? 150.222 135.527 128.813 1.00 104.17 ?  209  THR   A O     1 
ATOM   1681  C  CB    . THR   A 1 209 ? 149.604 134.437 125.784 1.00 99.06  ?  209  THR   A CB    1 
ATOM   1682  O  OG1   . THR   A 1 209 ? 150.166 134.294 124.474 1.00 100.90 ?  209  THR   A OG1   1 
ATOM   1683  C  CG2   . THR   A 1 209 ? 148.929 135.795 125.891 1.00 99.39  ?  209  THR   A CG2   1 
ATOM   1684  N  N     . PRO   A 1 210 ? 149.535 133.392 128.853 1.00 88.26  ?  210  PRO   A N     1 
ATOM   1685  C  CA    . PRO   A 1 210 ? 149.052 133.559 130.235 1.00 83.67  ?  210  PRO   A CA    1 
ATOM   1686  C  C     . PRO   A 1 210 ? 150.143 133.938 131.221 1.00 84.86  ?  210  PRO   A C     1 
ATOM   1687  O  O     . PRO   A 1 210 ? 149.872 134.695 132.160 1.00 87.89  ?  210  PRO   A O     1 
ATOM   1688  C  CB    . PRO   A 1 210 ? 148.441 132.189 130.568 1.00 86.78  ?  210  PRO   A CB    1 
ATOM   1689  C  CG    . PRO   A 1 210 ? 148.956 131.257 129.525 1.00 86.86  ?  210  PRO   A CG    1 
ATOM   1690  C  CD    . PRO   A 1 210 ? 149.128 132.087 128.304 1.00 85.77  ?  210  PRO   A CD    1 
ATOM   1691  N  N     . ILE   A 1 211 ? 151.368 133.438 131.040 1.00 87.70  ?  211  ILE   A N     1 
ATOM   1692  C  CA    . ILE   A 1 211 ? 152.462 133.816 131.933 1.00 86.57  ?  211  ILE   A CA    1 
ATOM   1693  C  C     . ILE   A 1 211 ? 152.751 135.307 131.811 1.00 85.60  ?  211  ILE   A C     1 
ATOM   1694  O  O     . ILE   A 1 211 ? 152.934 136.006 132.815 1.00 92.74  ?  211  ILE   A O     1 
ATOM   1695  C  CB    . ILE   A 1 211 ? 153.715 132.966 131.640 1.00 85.60  ?  211  ILE   A CB    1 
ATOM   1696  C  CG1   . ILE   A 1 211 ? 153.759 131.720 132.530 1.00 83.63  ?  211  ILE   A CG1   1 
ATOM   1697  C  CG2   . ILE   A 1 211 ? 154.986 133.781 131.849 1.00 85.87  ?  211  ILE   A CG2   1 
ATOM   1698  C  CD1   . ILE   A 1 211 ? 152.495 130.891 132.525 1.00 87.40  ?  211  ILE   A CD1   1 
ATOM   1699  N  N     . MET   A 1 212 ? 152.776 135.820 130.580 1.00 90.48  ?  212  MET   A N     1 
ATOM   1700  C  CA    . MET   A 1 212 ? 153.096 137.226 130.364 1.00 93.11  ?  212  MET   A CA    1 
ATOM   1701  C  C     . MET   A 1 212 ? 151.958 138.146 130.783 1.00 97.85  ?  212  MET   A C     1 
ATOM   1702  O  O     . MET   A 1 212 ? 152.204 139.292 131.174 1.00 101.66 ?  212  MET   A O     1 
ATOM   1703  C  CB    . MET   A 1 212 ? 153.445 137.448 128.900 1.00 94.61  ?  212  MET   A CB    1 
ATOM   1704  C  CG    . MET   A 1 212 ? 154.565 136.562 128.445 1.00 99.05  ?  212  MET   A CG    1 
ATOM   1705  S  SD    . MET   A 1 212 ? 156.119 137.270 128.986 1.00 113.33 ?  212  MET   A SD    1 
ATOM   1706  C  CE    . MET   A 1 212 ? 157.124 135.814 129.011 1.00 98.84  ?  212  MET   A CE    1 
ATOM   1707  N  N     . SER   A 1 213 ? 150.716 137.677 130.702 1.00 96.61  ?  213  SER   A N     1 
ATOM   1708  C  CA    . SER   A 1 213 ? 149.583 138.499 131.099 1.00 94.22  ?  213  SER   A CA    1 
ATOM   1709  C  C     . SER   A 1 213 ? 149.266 138.405 132.585 1.00 96.52  ?  213  SER   A C     1 
ATOM   1710  O  O     . SER   A 1 213 ? 148.593 139.296 133.116 1.00 101.40 ?  213  SER   A O     1 
ATOM   1711  C  CB    . SER   A 1 213 ? 148.343 138.114 130.287 1.00 95.24  ?  213  SER   A CB    1 
ATOM   1712  O  OG    . SER   A 1 213 ? 147.974 136.767 130.524 1.00 99.29  ?  213  SER   A OG    1 
ATOM   1713  N  N     . GLY   A 1 214 ? 149.729 137.359 133.268 1.00 92.75  ?  214  GLY   A N     1 
ATOM   1714  C  CA    . GLY   A 1 214 ? 149.396 137.180 134.667 1.00 94.74  ?  214  GLY   A CA    1 
ATOM   1715  C  C     . GLY   A 1 214 ? 150.523 137.424 135.649 1.00 95.81  ?  214  GLY   A C     1 
ATOM   1716  O  O     . GLY   A 1 214 ? 150.301 138.013 136.711 1.00 101.41 ?  214  GLY   A O     1 
ATOM   1717  N  N     . VAL   A 1 215 ? 151.734 136.972 135.322 1.00 91.20  ?  215  VAL   A N     1 
ATOM   1718  C  CA    . VAL   A 1 215 ? 152.865 137.174 136.218 1.00 92.22  ?  215  VAL   A CA    1 
ATOM   1719  C  C     . VAL   A 1 215 ? 153.200 138.658 136.265 1.00 94.21  ?  215  VAL   A C     1 
ATOM   1720  O  O     . VAL   A 1 215 ? 153.193 139.341 135.233 1.00 99.32  ?  215  VAL   A O     1 
ATOM   1721  C  CB    . VAL   A 1 215 ? 154.070 136.328 135.770 1.00 91.82  ?  215  VAL   A CB    1 
ATOM   1722  C  CG1   . VAL   A 1 215 ? 155.297 136.640 136.612 1.00 90.44  ?  215  VAL   A CG1   1 
ATOM   1723  C  CG2   . VAL   A 1 215 ? 153.732 134.847 135.852 1.00 90.77  ?  215  VAL   A CG2   1 
ATOM   1724  N  N     . ARG   A 1 216 ? 153.506 139.152 137.468 1.00 91.03  ?  216  ARG   A N     1 
ATOM   1725  C  CA    . ARG   A 1 216 ? 153.636 140.541 137.905 1.00 89.80  ?  216  ARG   A CA    1 
ATOM   1726  C  C     . ARG   A 1 216 ? 152.277 141.188 138.173 1.00 90.54  ?  216  ARG   A C     1 
ATOM   1727  O  O     . ARG   A 1 216 ? 152.237 142.291 138.719 1.00 98.21  ?  216  ARG   A O     1 
ATOM   1728  C  CB    . ARG   A 1 216 ? 154.421 141.431 136.918 1.00 89.27  ?  216  ARG   A CB    1 
ATOM   1729  C  CG    . ARG   A 1 216 ? 153.536 142.227 135.965 1.00 91.29  ?  216  ARG   A CG    1 
ATOM   1730  C  CD    . ARG   A 1 216 ? 154.280 142.692 134.733 1.00 92.11  ?  216  ARG   A CD    1 
ATOM   1731  N  NE    . ARG   A 1 216 ? 153.372 142.839 133.602 1.00 93.96  ?  216  ARG   A NE    1 
ATOM   1732  C  CZ    . ARG   A 1 216 ? 153.013 141.846 132.800 1.00 90.85  ?  216  ARG   A CZ    1 
ATOM   1733  N  NH1   . ARG   A 1 216 ? 153.490 140.623 132.959 1.00 92.01  ?  216  ARG   A NH1   1 
ATOM   1734  N  NH2   . ARG   A 1 216 ? 152.150 142.086 131.817 1.00 94.28  ?  216  ARG   A NH2   1 
ATOM   1735  N  N     . THR   A 1 217 ? 151.170 140.533 137.857 1.00 88.43  ?  217  THR   A N     1 
ATOM   1736  C  CA    . THR   A 1 217 ? 149.843 141.062 138.119 1.00 89.93  ?  217  THR   A CA    1 
ATOM   1737  C  C     . THR   A 1 217 ? 149.207 140.331 139.296 1.00 94.25  ?  217  THR   A C     1 
ATOM   1738  O  O     . THR   A 1 217 ? 149.629 139.226 139.652 1.00 96.52  ?  217  THR   A O     1 
ATOM   1739  C  CB    . THR   A 1 217 ? 148.953 140.932 136.874 1.00 91.09  ?  217  THR   A CB    1 
ATOM   1740  O  OG1   . THR   A 1 217 ? 148.296 139.660 136.880 1.00 93.40  ?  217  THR   A OG1   1 
ATOM   1741  C  CG2   . THR   A 1 217 ? 149.785 141.071 135.608 1.00 91.12  ?  217  THR   A CG2   1 
ATOM   1742  N  N     . PRO   A 1 218 ? 148.198 140.926 139.940 1.00 99.23  ?  218  PRO   A N     1 
ATOM   1743  C  CA    . PRO   A 1 218 ? 147.626 140.297 141.143 1.00 97.31  ?  218  PRO   A CA    1 
ATOM   1744  C  C     . PRO   A 1 218 ? 147.039 138.915 140.912 1.00 98.24  ?  218  PRO   A C     1 
ATOM   1745  O  O     . PRO   A 1 218 ? 146.895 138.156 141.879 1.00 99.40  ?  218  PRO   A O     1 
ATOM   1746  C  CB    . PRO   A 1 218 ? 146.542 141.293 141.575 1.00 95.44  ?  218  PRO   A CB    1 
ATOM   1747  C  CG    . PRO   A 1 218 ? 147.001 142.596 141.040 1.00 96.42  ?  218  PRO   A CG    1 
ATOM   1748  C  CD    . PRO   A 1 218 ? 147.674 142.289 139.736 1.00 97.21  ?  218  PRO   A CD    1 
ATOM   1749  N  N     . THR   A 1 219 ? 146.694 138.560 139.678 1.00 93.83  ?  219  THR   A N     1 
ATOM   1750  C  CA    . THR   A 1 219 ? 146.100 137.257 139.424 1.00 93.10  ?  219  THR   A CA    1 
ATOM   1751  C  C     . THR   A 1 219 ? 147.123 136.142 139.635 1.00 94.68  ?  219  THR   A C     1 
ATOM   1752  O  O     . THR   A 1 219 ? 148.338 136.360 139.633 1.00 97.24  ?  219  THR   A O     1 
ATOM   1753  C  CB    . THR   A 1 219 ? 145.535 137.187 138.004 1.00 91.58  ?  219  THR   A CB    1 
ATOM   1754  O  OG1   . THR   A 1 219 ? 144.523 136.174 137.942 1.00 91.97  ?  219  THR   A OG1   1 
ATOM   1755  C  CG2   . THR   A 1 219 ? 146.630 136.857 137.002 1.00 88.73  ?  219  THR   A CG2   1 
ATOM   1756  N  N     . ARG   A 1 220 ? 146.605 134.929 139.838 1.00 85.17  ?  220  ARG   A N     1 
ATOM   1757  C  CA    . ARG   A 1 220 ? 147.435 133.742 139.998 1.00 82.79  ?  220  ARG   A CA    1 
ATOM   1758  C  C     . ARG   A 1 220 ? 147.003 132.607 139.078 1.00 87.63  ?  220  ARG   A C     1 
ATOM   1759  O  O     . ARG   A 1 220 ? 147.426 131.464 139.286 1.00 85.40  ?  220  ARG   A O     1 
ATOM   1760  C  CB    . ARG   A 1 220 ? 147.416 133.259 141.452 1.00 79.85  ?  220  ARG   A CB    1 
ATOM   1761  C  CG    . ARG   A 1 220 ? 148.168 134.153 142.418 1.00 81.74  ?  220  ARG   A CG    1 
ATOM   1762  C  CD    . ARG   A 1 220 ? 149.639 134.247 142.052 1.00 81.35  ?  220  ARG   A CD    1 
ATOM   1763  N  NE    . ARG   A 1 220 ? 150.399 135.011 143.034 1.00 82.42  ?  220  ARG   A NE    1 
ATOM   1764  C  CZ    . ARG   A 1 220 ? 150.339 136.329 143.172 1.00 86.31  ?  220  ARG   A CZ    1 
ATOM   1765  N  NH1   . ARG   A 1 220 ? 149.570 137.072 142.393 1.00 85.75  ?  220  ARG   A NH1   1 
ATOM   1766  N  NH2   . ARG   A 1 220 ? 151.072 136.916 144.113 1.00 86.01  ?  220  ARG   A NH2   1 
ATOM   1767  N  N     A GLN   A 1 221 ? 146.180 132.887 138.072 0.50 93.82  ?  221  GLN   A N     1 
ATOM   1768  N  N     B GLN   A 1 221 ? 146.280 132.887 138.072 0.50 93.82  ?  221  GLN   A N     1 
ATOM   1769  C  CA    A GLN   A 1 221 ? 145.661 131.863 137.169 0.50 90.13  ?  221  GLN   A CA    1 
ATOM   1770  C  CA    B GLN   A 1 221 ? 145.761 131.863 137.169 0.50 90.13  ?  221  GLN   A CA    1 
ATOM   1771  C  C     A GLN   A 1 221 ? 146.506 131.862 135.901 0.50 92.14  ?  221  GLN   A C     1 
ATOM   1772  C  C     B GLN   A 1 221 ? 146.606 131.862 135.901 0.50 92.14  ?  221  GLN   A C     1 
ATOM   1773  O  O     A GLN   A 1 221 ? 146.353 132.729 135.037 0.50 97.23  ?  221  GLN   A O     1 
ATOM   1774  O  O     B GLN   A 1 221 ? 146.453 132.729 135.037 0.50 97.23  ?  221  GLN   A O     1 
ATOM   1775  C  CB    A GLN   A 1 221 ? 144.190 132.115 136.855 0.50 93.89  ?  221  GLN   A CB    1 
ATOM   1776  C  CB    B GLN   A 1 221 ? 144.290 132.115 136.855 0.50 93.89  ?  221  GLN   A CB    1 
ATOM   1777  C  CG    A GLN   A 1 221 ? 143.243 131.081 137.440 0.50 96.90  ?  221  GLN   A CG    1 
ATOM   1778  C  CG    B GLN   A 1 221 ? 143.362 131.944 138.045 0.50 96.90  ?  221  GLN   A CG    1 
ATOM   1779  C  CD    A GLN   A 1 221 ? 143.370 130.963 138.945 0.50 99.71  ?  221  GLN   A CD    1 
ATOM   1780  C  CD    B GLN   A 1 221 ? 141.921 132.273 137.710 0.50 99.71  ?  221  GLN   A CD    1 
ATOM   1781  O  OE1   A GLN   A 1 221 ? 142.913 131.832 139.689 0.50 98.72  ?  221  GLN   A OE1   1 
ATOM   1782  O  OE1   B GLN   A 1 221 ? 141.645 133.039 136.786 0.50 98.72  ?  221  GLN   A OE1   1 
ATOM   1783  N  NE2   A GLN   A 1 221 ? 143.994 129.885 139.403 0.50 97.48  ?  221  GLN   A NE2   1 
ATOM   1784  N  NE2   B GLN   A 1 221 ? 140.993 131.696 138.462 0.50 97.48  ?  221  GLN   A NE2   1 
ATOM   1785  N  N     . PHE   A 1 222 ? 147.420 130.948 135.881 1.00 84.68  ?  222  PHE   A N     1 
ATOM   1786  C  CA    . PHE   A 1 222 ? 148.283 130.874 134.709 1.00 85.68  ?  222  PHE   A CA    1 
ATOM   1787  C  C     . PHE   A 1 222 ? 147.819 129.616 134.008 1.00 89.60  ?  222  PHE   A C     1 
ATOM   1788  O  O     . PHE   A 1 222 ? 148.463 128.604 134.059 1.00 95.43  ?  222  PHE   A O     1 
ATOM   1789  C  CB    . PHE   A 1 222 ? 149.744 130.988 135.125 1.00 87.15  ?  222  PHE   A CB    1 
ATOM   1790  C  CG    . PHE   A 1 222 ? 149.990 132.122 136.069 1.00 86.81  ?  222  PHE   A CG    1 
ATOM   1791  C  CD1   . PHE   A 1 222 ? 149.884 133.423 135.631 1.00 86.75  ?  222  PHE   A CD1   1 
ATOM   1792  C  CD2   . PHE   A 1 222 ? 150.284 131.884 137.391 1.00 86.37  ?  222  PHE   A CD2   1 
ATOM   1793  C  CE1   . PHE   A 1 222 ? 150.091 134.471 136.503 1.00 87.57  ?  222  PHE   A CE1   1 
ATOM   1794  C  CE2   . PHE   A 1 222 ? 150.496 132.935 138.260 1.00 88.91  ?  222  PHE   A CE2   1 
ATOM   1795  C  CZ    . PHE   A 1 222 ? 150.399 134.225 137.814 1.00 88.94  ?  222  PHE   A CZ    1 
ATOM   1796  N  N     . SER   A 1 223 ? 146.687 129.715 133.347 1.00 101.86 ?  223  SER   A N     1 
ATOM   1797  C  CA    . SER   A 1 223 ? 146.047 128.572 132.629 1.00 103.05 ?  223  SER   A CA    1 
ATOM   1798  C  C     . SER   A 1 223 ? 146.822 128.005 131.450 1.00 98.94  ?  223  SER   A C     1 
ATOM   1799  O  O     . SER   A 1 223 ? 147.846 128.548 131.096 1.00 95.67  ?  223  SER   A O     1 
ATOM   1800  C  CB    . SER   A 1 223 ? 144.744 129.037 132.079 1.00 105.27 ?  223  SER   A CB    1 
ATOM   1801  O  OG    . SER   A 1 223 ? 143.763 129.075 133.101 1.00 102.18 ?  223  SER   A OG    1 
ATOM   1802  N  N     . SER   A 1 224 ? 146.149 127.138 130.696 1.00 77.89  ?  224  SER   A N     1 
ATOM   1803  C  CA    . SER   A 1 224 ? 146.871 126.444 129.632 1.00 80.95  ?  224  SER   A CA    1 
ATOM   1804  C  C     . SER   A 1 224 ? 145.974 125.345 129.116 1.00 80.04  ?  224  SER   A C     1 
ATOM   1805  O  O     . SER   A 1 224 ? 144.935 125.667 128.616 1.00 80.71  ?  224  SER   A O     1 
ATOM   1806  C  CB    . SER   A 1 224 ? 148.082 125.899 130.182 1.00 85.60  ?  224  SER   A CB    1 
ATOM   1807  O  OG    . SER   A 1 224 ? 147.771 124.923 131.157 1.00 91.63  ?  224  SER   A OG    1 
ATOM   1808  N  N     . CYS   A 1 225 ? 146.340 124.103 129.349 1.00 73.87  ?  225  CYS   A N     1 
ATOM   1809  C  CA    A CYS   A 1 225 ? 145.656 122.862 129.029 0.26 72.13  ?  225  CYS   A CA    1 
ATOM   1810  C  CA    B CYS   A 1 225 ? 145.628 122.876 129.040 0.74 69.33  ?  225  CYS   A CA    1 
ATOM   1811  C  C     . CYS   A 1 225 ? 145.638 121.980 130.268 1.00 67.81  ?  225  CYS   A C     1 
ATOM   1812  O  O     . CYS   A 1 225 ? 146.605 121.959 131.033 1.00 73.80  ?  225  CYS   A O     1 
ATOM   1813  C  CB    A CYS   A 1 225 ? 146.349 122.129 127.872 0.26 73.66  ?  225  CYS   A CB    1 
ATOM   1814  C  CB    B CYS   A 1 225 ? 146.252 122.130 127.853 0.74 73.48  ?  225  CYS   A CB    1 
ATOM   1815  S  SG    A CYS   A 1 225 ? 147.770 123.012 127.168 0.26 74.46  ?  225  CYS   A SG    1 
ATOM   1816  S  SG    B CYS   A 1 225 ? 146.254 123.026 126.285 0.74 84.69  ?  225  CYS   A SG    1 
ATOM   1817  N  N     . VAL   A 1 226 ? 144.548 121.243 130.454 1.00 55.65  ?  226  VAL   A N     1 
ATOM   1818  C  CA    . VAL   A 1 226 ? 144.414 120.329 131.581 1.00 50.77  ?  226  VAL   A CA    1 
ATOM   1819  C  C     . VAL   A 1 226 ? 144.034 118.951 131.061 1.00 59.99  ?  226  VAL   A C     1 
ATOM   1820  O  O     . VAL   A 1 226 ? 143.232 118.823 130.129 1.00 66.05  ?  226  VAL   A O     1 
ATOM   1821  C  CB    . VAL   A 1 226 ? 143.385 120.829 132.618 1.00 50.37  ?  226  VAL   A CB    1 
ATOM   1822  C  CG1   . VAL   A 1 226 ? 143.865 122.123 133.247 1.00 61.42  ?  226  VAL   A CG1   1 
ATOM   1823  C  CG2   . VAL   A 1 226 ? 142.020 121.018 131.983 1.00 63.39  ?  226  VAL   A CG2   1 
ATOM   1824  N  N     . LEU   A 1 227 ? 144.631 117.923 131.653 1.00 55.94  ?  227  LEU   A N     1 
ATOM   1825  C  CA    . LEU   A 1 227 ? 144.338 116.534 131.332 1.00 44.48  ?  227  LEU   A CA    1 
ATOM   1826  C  C     . LEU   A 1 227 ? 143.507 115.953 132.465 1.00 52.08  ?  227  LEU   A C     1 
ATOM   1827  O  O     . LEU   A 1 227 ? 143.961 115.914 133.614 1.00 67.94  ?  227  LEU   A O     1 
ATOM   1828  C  CB    . LEU   A 1 227 ? 145.623 115.730 131.138 1.00 48.29  ?  227  LEU   A CB    1 
ATOM   1829  C  CG    . LEU   A 1 227 ? 146.414 115.988 129.855 1.00 52.24  ?  227  LEU   A CG    1 
ATOM   1830  C  CD1   . LEU   A 1 227 ? 147.300 117.214 129.994 1.00 52.25  ?  227  LEU   A CD1   1 
ATOM   1831  C  CD2   . LEU   A 1 227 ? 147.239 114.767 129.483 1.00 59.33  ?  227  LEU   A CD2   1 
ATOM   1832  N  N     . ILE   A 1 228 ? 142.295 115.513 132.145 1.00 47.44  ?  228  ILE   A N     1 
ATOM   1833  C  CA    . ILE   A 1 228 ? 141.377 114.941 133.120 1.00 49.61  ?  228  ILE   A CA    1 
ATOM   1834  C  C     . ILE   A 1 228 ? 140.986 113.552 132.644 1.00 59.20  ?  228  ILE   A C     1 
ATOM   1835  O  O     . ILE   A 1 228 ? 140.578 113.380 131.490 1.00 68.15  ?  228  ILE   A O     1 
ATOM   1836  C  CB    . ILE   A 1 228 ? 140.129 115.822 133.314 1.00 47.36  ?  228  ILE   A CB    1 
ATOM   1837  C  CG1   . ILE   A 1 228 ? 140.533 117.253 133.673 1.00 57.70  ?  228  ILE   A CG1   1 
ATOM   1838  C  CG2   . ILE   A 1 228 ? 139.234 115.243 134.393 1.00 50.98  ?  228  ILE   A CG2   1 
ATOM   1839  C  CD1   . ILE   A 1 228 ? 139.613 118.307 133.102 1.00 58.12  ?  228  ILE   A CD1   1 
ATOM   1840  N  N     . GLU   A 1 229 ? 141.116 112.567 133.524 1.00 77.35  ?  229  GLU   A N     1 
ATOM   1841  C  CA    . GLU   A 1 229 ? 140.694 111.205 133.236 1.00 72.09  ?  229  GLU   A CA    1 
ATOM   1842  C  C     . GLU   A 1 229 ? 139.355 110.942 133.908 1.00 78.08  ?  229  GLU   A C     1 
ATOM   1843  O  O     . GLU   A 1 229 ? 139.164 111.285 135.079 1.00 86.62  ?  229  GLU   A O     1 
ATOM   1844  C  CB    . GLU   A 1 229 ? 141.732 110.188 133.712 1.00 71.39  ?  229  GLU   A CB    1 
ATOM   1845  C  CG    . GLU   A 1 229 ? 141.303 108.746 133.499 1.00 78.85  ?  229  GLU   A CG    1 
ATOM   1846  C  CD    . GLU   A 1 229 ? 142.467 107.779 133.491 1.00 90.00  ?  229  GLU   A CD    1 
ATOM   1847  O  OE1   . GLU   A 1 229 ? 143.575 108.177 133.902 1.00 89.14  ?  229  GLU   A OE1   1 
ATOM   1848  O  OE2   . GLU   A 1 229 ? 142.272 106.619 133.072 1.00 89.78  ?  229  GLU   A OE2   1 
ATOM   1849  N  N     . CYS   A 1 230 ? 138.435 110.338 133.165 1.00 69.54  ?  230  CYS   A N     1 
ATOM   1850  C  CA    . CYS   A 1 230 ? 137.108 110.010 133.662 1.00 70.18  ?  230  CYS   A CA    1 
ATOM   1851  C  C     . CYS   A 1 230 ? 136.984 108.500 133.798 1.00 77.87  ?  230  CYS   A C     1 
ATOM   1852  O  O     . CYS   A 1 230 ? 137.227 107.764 132.836 1.00 84.07  ?  230  CYS   A O     1 
ATOM   1853  C  CB    . CYS   A 1 230 ? 136.026 110.551 132.727 1.00 71.82  ?  230  CYS   A CB    1 
ATOM   1854  S  SG    . CYS   A 1 230 ? 134.360 109.988 133.113 1.00 87.15  ?  230  CYS   A SG    1 
ATOM   1855  N  N     . GLY   A 1 231 ? 136.613 108.044 134.992 1.00 73.94  ?  231  GLY   A N     1 
ATOM   1856  C  CA    . GLY   A 1 231 ? 136.408 106.634 135.233 1.00 71.90  ?  231  GLY   A CA    1 
ATOM   1857  C  C     . GLY   A 1 231 ? 135.024 106.175 134.821 1.00 73.76  ?  231  GLY   A C     1 
ATOM   1858  O  O     . GLY   A 1 231 ? 134.171 106.951 134.391 1.00 79.56  ?  231  GLY   A O     1 
ATOM   1859  N  N     . ASP   A 1 232 ? 134.803 104.872 134.959 1.00 73.60  ?  232  ASP   A N     1 
ATOM   1860  C  CA    . ASP   A 1 232 ? 133.517 104.265 134.618 1.00 71.89  ?  232  ASP   A CA    1 
ATOM   1861  C  C     . ASP   A 1 232 ? 132.550 104.315 135.797 1.00 70.94  ?  232  ASP   A C     1 
ATOM   1862  O  O     . ASP   A 1 232 ? 132.001 103.303 136.228 1.00 72.87  ?  232  ASP   A O     1 
ATOM   1863  C  CB    . ASP   A 1 232 ? 133.730 102.833 134.142 1.00 71.71  ?  232  ASP   A CB    1 
ATOM   1864  C  CG    . ASP   A 1 232 ? 132.525 102.278 133.412 1.00 76.62  ?  232  ASP   A CG    1 
ATOM   1865  O  OD1   . ASP   A 1 232 ? 131.779 103.072 132.805 1.00 79.68  ?  232  ASP   A OD1   1 
ATOM   1866  O  OD2   . ASP   A 1 232 ? 132.322 101.047 133.447 1.00 78.38  ?  232  ASP   A OD2   1 
ATOM   1867  N  N     . SER   A 1 233 ? 132.340 105.515 136.331 1.00 69.55  ?  233  SER   A N     1 
ATOM   1868  C  CA    . SER   A 1 233 ? 131.467 105.715 137.475 1.00 64.43  ?  233  SER   A CA    1 
ATOM   1869  C  C     . SER   A 1 233 ? 130.713 107.025 137.310 1.00 66.99  ?  233  SER   A C     1 
ATOM   1870  O  O     . SER   A 1 233 ? 131.187 107.954 136.653 1.00 73.16  ?  233  SER   A O     1 
ATOM   1871  C  CB    . SER   A 1 233 ? 132.256 105.728 138.790 1.00 63.40  ?  233  SER   A CB    1 
ATOM   1872  O  OG    . SER   A 1 233 ? 131.405 105.512 139.901 1.00 73.72  ?  233  SER   A OG    1 
ATOM   1873  N  N     . LEU   A 1 234 ? 129.524 107.086 137.912 1.00 63.05  ?  234  LEU   A N     1 
ATOM   1874  C  CA    . LEU   A 1 234 ? 128.756 108.325 137.894 1.00 60.68  ?  234  LEU   A CA    1 
ATOM   1875  C  C     . LEU   A 1 234 ? 129.443 109.410 138.712 1.00 64.12  ?  234  LEU   A C     1 
ATOM   1876  O  O     . LEU   A 1 234 ? 129.435 110.585 138.326 1.00 67.37  ?  234  LEU   A O     1 
ATOM   1877  C  CB    . LEU   A 1 234 ? 127.341 108.074 138.408 1.00 59.71  ?  234  LEU   A CB    1 
ATOM   1878  C  CG    . LEU   A 1 234 ? 126.294 107.794 137.331 1.00 61.27  ?  234  LEU   A CG    1 
ATOM   1879  C  CD1   . LEU   A 1 234 ? 124.913 107.999 137.898 1.00 61.01  ?  234  LEU   A CD1   1 
ATOM   1880  C  CD2   . LEU   A 1 234 ? 126.513 108.676 136.112 1.00 60.35  ?  234  LEU   A CD2   1 
ATOM   1881  N  N     . ASP   A 1 235 ? 130.038 109.035 139.847 1.00 70.59  ?  235  ASP   A N     1 
ATOM   1882  C  CA    . ASP   A 1 235 ? 130.816 109.993 140.625 1.00 67.82  ?  235  ASP   A CA    1 
ATOM   1883  C  C     . ASP   A 1 235 ? 131.991 110.525 139.817 1.00 69.49  ?  235  ASP   A C     1 
ATOM   1884  O  O     . ASP   A 1 235 ? 132.281 111.727 139.844 1.00 75.78  ?  235  ASP   A O     1 
ATOM   1885  C  CB    . ASP   A 1 235 ? 131.309 109.342 141.917 1.00 73.63  ?  235  ASP   A CB    1 
ATOM   1886  C  CG    . ASP   A 1 235 ? 130.187 109.063 142.895 1.00 82.90  ?  235  ASP   A CG    1 
ATOM   1887  O  OD1   . ASP   A 1 235 ? 129.291 109.920 143.037 1.00 85.59  ?  235  ASP   A OD1   1 
ATOM   1888  O  OD2   . ASP   A 1 235 ? 130.201 107.985 143.525 1.00 85.44  ?  235  ASP   A OD2   1 
ATOM   1889  N  N     . SER   A 1 236 ? 132.678 109.642 139.089 1.00 62.16  ?  236  SER   A N     1 
ATOM   1890  C  CA    . SER   A 1 236 ? 133.794 110.074 138.256 1.00 56.92  ?  236  SER   A CA    1 
ATOM   1891  C  C     . SER   A 1 236 ? 133.328 111.000 137.141 1.00 61.73  ?  236  SER   A C     1 
ATOM   1892  O  O     . SER   A 1 236 ? 133.993 111.995 136.834 1.00 66.34  ?  236  SER   A O     1 
ATOM   1893  C  CB    . SER   A 1 236 ? 134.519 108.859 137.678 1.00 61.04  ?  236  SER   A CB    1 
ATOM   1894  O  OG    . SER   A 1 236 ? 135.809 109.214 137.213 1.00 71.31  ?  236  SER   A OG    1 
ATOM   1895  N  N     . ILE   A 1 237 ? 132.188 110.687 136.521 1.00 56.44  ?  237  ILE   A N     1 
ATOM   1896  C  CA    . ILE   A 1 237 ? 131.658 111.539 135.460 1.00 51.81  ?  237  ILE   A CA    1 
ATOM   1897  C  C     . ILE   A 1 237 ? 131.301 112.915 136.009 1.00 57.95  ?  237  ILE   A C     1 
ATOM   1898  O  O     . ILE   A 1 237 ? 131.597 113.944 135.389 1.00 59.07  ?  237  ILE   A O     1 
ATOM   1899  C  CB    . ILE   A 1 237 ? 130.450 110.861 134.786 1.00 50.98  ?  237  ILE   A CB    1 
ATOM   1900  C  CG1   . ILE   A 1 237 ? 130.919 109.712 133.892 1.00 50.33  ?  237  ILE   A CG1   1 
ATOM   1901  C  CG2   . ILE   A 1 237 ? 129.646 111.866 133.980 1.00 57.16  ?  237  ILE   A CG2   1 
ATOM   1902  C  CD1   . ILE   A 1 237 ? 129.839 108.712 133.560 1.00 58.66  ?  237  ILE   A CD1   1 
ATOM   1903  N  N     . ASN   A 1 238 ? 130.664 112.955 137.182 1.00 55.76  ?  238  ASN   A N     1 
ATOM   1904  C  CA    . ASN   A 1 238 ? 130.316 114.233 137.795 1.00 43.02  ?  238  ASN   A CA    1 
ATOM   1905  C  C     . ASN   A 1 238 ? 131.560 115.041 138.140 1.00 54.08  ?  238  ASN   A C     1 
ATOM   1906  O  O     . ASN   A 1 238 ? 131.606 116.255 137.905 1.00 68.17  ?  238  ASN   A O     1 
ATOM   1907  C  CB    . ASN   A 1 238 ? 129.466 114.000 139.043 1.00 51.25  ?  238  ASN   A CB    1 
ATOM   1908  C  CG    . ASN   A 1 238 ? 128.021 113.702 138.713 1.00 57.67  ?  238  ASN   A CG    1 
ATOM   1909  O  OD1   . ASN   A 1 238 ? 127.531 114.070 137.648 1.00 61.94  ?  238  ASN   A OD1   1 
ATOM   1910  N  ND2   . ASN   A 1 238 ? 127.330 113.032 139.625 1.00 63.61  ?  238  ASN   A ND2   1 
ATOM   1911  N  N     . ALA   A 1 239 ? 132.580 114.386 138.702 1.00 53.69  ?  239  ALA   A N     1 
ATOM   1912  C  CA    . ALA   A 1 239 ? 133.815 115.088 139.033 1.00 49.80  ?  239  ALA   A CA    1 
ATOM   1913  C  C     . ALA   A 1 239 ? 134.498 115.624 137.782 1.00 53.78  ?  239  ALA   A C     1 
ATOM   1914  O  O     . ALA   A 1 239 ? 134.999 116.755 137.773 1.00 60.83  ?  239  ALA   A O     1 
ATOM   1915  C  CB    . ALA   A 1 239 ? 134.755 114.162 139.804 1.00 54.09  ?  239  ALA   A CB    1 
ATOM   1916  N  N     . THR   A 1 240 ? 134.523 114.825 136.713 1.00 55.68  ?  240  THR   A N     1 
ATOM   1917  C  CA    . THR   A 1 240 ? 135.121 115.272 135.461 1.00 51.54  ?  240  THR   A CA    1 
ATOM   1918  C  C     . THR   A 1 240 ? 134.373 116.469 134.891 1.00 53.03  ?  240  THR   A C     1 
ATOM   1919  O  O     . THR   A 1 240 ? 134.993 117.434 134.434 1.00 64.61  ?  240  THR   A O     1 
ATOM   1920  C  CB    . THR   A 1 240 ? 135.140 114.125 134.450 1.00 51.31  ?  240  THR   A CB    1 
ATOM   1921  O  OG1   . THR   A 1 240 ? 135.809 112.994 135.020 1.00 67.32  ?  240  THR   A OG1   1 
ATOM   1922  C  CG2   . THR   A 1 240 ? 135.857 114.543 133.176 1.00 49.56  ?  240  THR   A CG2   1 
ATOM   1923  N  N     . SER   A 1 241 ? 133.039 116.426 134.913 1.00 50.47  ?  241  SER   A N     1 
ATOM   1924  C  CA    . SER   A 1 241 ? 132.257 117.543 134.393 1.00 49.60  ?  241  SER   A CA    1 
ATOM   1925  C  C     . SER   A 1 241 ? 132.477 118.804 135.220 1.00 51.45  ?  241  SER   A C     1 
ATOM   1926  O  O     . SER   A 1 241 ? 132.604 119.904 134.668 1.00 62.50  ?  241  SER   A O     1 
ATOM   1927  C  CB    . SER   A 1 241 ? 130.775 117.171 134.357 1.00 51.08  ?  241  SER   A CB    1 
ATOM   1928  O  OG    . SER   A 1 241 ? 129.971 118.308 134.098 1.00 69.12  ?  241  SER   A OG    1 
ATOM   1929  N  N     . SER   A 1 242 ? 132.530 118.663 136.547 1.00 46.91  ?  242  SER   A N     1 
ATOM   1930  C  CA    . SER   A 1 242 ? 132.778 119.819 137.402 1.00 46.35  ?  242  SER   A CA    1 
ATOM   1931  C  C     . SER   A 1 242 ? 134.157 120.413 137.144 1.00 53.47  ?  242  SER   A C     1 
ATOM   1932  O  O     . SER   A 1 242 ? 134.309 121.638 137.072 1.00 65.70  ?  242  SER   A O     1 
ATOM   1933  C  CB    . SER   A 1 242 ? 132.627 119.428 138.871 1.00 54.37  ?  242  SER   A CB    1 
ATOM   1934  O  OG    . SER   A 1 242 ? 131.410 118.740 139.093 1.00 62.59  ?  242  SER   A OG    1 
ATOM   1935  N  N     . ALA   A 1 243 ? 135.176 119.562 137.000 1.00 53.43  ?  243  ALA   A N     1 
ATOM   1936  C  CA    . ALA   A 1 243 ? 136.517 120.059 136.709 1.00 50.53  ?  243  ALA   A CA    1 
ATOM   1937  C  C     . ALA   A 1 243 ? 136.568 120.744 135.349 1.00 51.89  ?  243  ALA   A C     1 
ATOM   1938  O  O     . ALA   A 1 243 ? 137.232 121.776 135.190 1.00 61.06  ?  243  ALA   A O     1 
ATOM   1939  C  CB    . ALA   A 1 243 ? 137.528 118.915 136.776 1.00 47.85  ?  243  ALA   A CB    1 
ATOM   1940  N  N     . ILE   A 1 244 ? 135.873 120.185 134.357 1.00 45.96  ?  244  ILE   A N     1 
ATOM   1941  C  CA    . ILE   A 1 244 ? 135.826 120.804 133.035 1.00 43.16  ?  244  ILE   A CA    1 
ATOM   1942  C  C     . ILE   A 1 244 ? 135.191 122.185 133.121 1.00 53.82  ?  244  ILE   A C     1 
ATOM   1943  O  O     . ILE   A 1 244 ? 135.695 123.155 132.546 1.00 62.90  ?  244  ILE   A O     1 
ATOM   1944  C  CB    . ILE   A 1 244 ? 135.072 119.903 132.042 1.00 47.79  ?  244  ILE   A CB    1 
ATOM   1945  C  CG1   . ILE   A 1 244 ? 135.910 118.680 131.675 1.00 44.91  ?  244  ILE   A CG1   1 
ATOM   1946  C  CG2   . ILE   A 1 244 ? 134.710 120.682 130.793 1.00 44.53  ?  244  ILE   A CG2   1 
ATOM   1947  C  CD1   . ILE   A 1 244 ? 135.114 117.589 131.000 1.00 48.10  ?  244  ILE   A CD1   1 
ATOM   1948  N  N     . VAL   A 1 245 ? 134.076 122.294 133.847 1.00 56.20  ?  245  VAL   A N     1 
ATOM   1949  C  CA    . VAL   A 1 245 ? 133.414 123.589 133.994 1.00 47.16  ?  245  VAL   A CA    1 
ATOM   1950  C  C     . VAL   A 1 245 ? 134.333 124.582 134.697 1.00 49.37  ?  245  VAL   A C     1 
ATOM   1951  O  O     . VAL   A 1 245 ? 134.433 125.747 134.297 1.00 65.24  ?  245  VAL   A O     1 
ATOM   1952  C  CB    . VAL   A 1 245 ? 132.074 123.425 134.736 1.00 47.51  ?  245  VAL   A CB    1 
ATOM   1953  C  CG1   . VAL   A 1 245 ? 131.538 124.777 135.172 1.00 47.60  ?  245  VAL   A CG1   1 
ATOM   1954  C  CG2   . VAL   A 1 245 ? 131.061 122.711 133.859 1.00 48.14  ?  245  VAL   A CG2   1 
ATOM   1955  N  N     . LYS   A 1 246 ? 135.036 124.128 135.741 1.00 53.66  ?  246  LYS   A N     1 
ATOM   1956  C  CA    A LYS   A 1 246 ? 135.919 125.005 136.506 0.49 56.85  ?  246  LYS   A CA    1 
ATOM   1957  C  CA    B LYS   A 1 246 ? 135.912 125.012 136.505 0.51 57.14  ?  246  LYS   A CA    1 
ATOM   1958  C  C     . LYS   A 1 246 ? 137.141 125.438 135.708 1.00 55.59  ?  246  LYS   A C     1 
ATOM   1959  O  O     . LYS   A 1 246 ? 137.720 126.495 135.986 1.00 69.38  ?  246  LYS   A O     1 
ATOM   1960  C  CB    A LYS   A 1 246 ? 136.365 124.301 137.783 0.49 58.58  ?  246  LYS   A CB    1 
ATOM   1961  C  CB    B LYS   A 1 246 ? 136.322 124.319 137.808 0.51 58.72  ?  246  LYS   A CB    1 
ATOM   1962  C  CG    A LYS   A 1 246 ? 135.890 124.953 139.060 0.49 60.50  ?  246  LYS   A CG    1 
ATOM   1963  C  CG    B LYS   A 1 246 ? 137.202 125.152 138.729 0.51 60.23  ?  246  LYS   A CG    1 
ATOM   1964  C  CD    A LYS   A 1 246 ? 135.919 123.964 140.214 0.49 61.52  ?  246  LYS   A CD    1 
ATOM   1965  C  CD    B LYS   A 1 246 ? 136.549 126.478 139.085 0.51 58.79  ?  246  LYS   A CD    1 
ATOM   1966  C  CE    A LYS   A 1 246 ? 136.097 124.673 141.546 0.49 62.24  ?  246  LYS   A CE    1 
ATOM   1967  C  CE    B LYS   A 1 246 ? 137.461 127.348 139.936 0.51 59.75  ?  246  LYS   A CE    1 
ATOM   1968  N  NZ    A LYS   A 1 246 ? 135.976 123.733 142.693 0.49 61.93  ?  246  LYS   A NZ    1 
ATOM   1969  N  NZ    B LYS   A 1 246 ? 136.817 128.646 140.266 0.51 59.02  ?  246  LYS   A NZ    1 
ATOM   1970  N  N     . TYR   A 1 247 ? 137.566 124.641 134.734 1.00 55.81  ?  247  TYR   A N     1 
ATOM   1971  C  CA    . TYR   A 1 247 ? 138.750 125.005 133.967 1.00 48.68  ?  247  TYR   A CA    1 
ATOM   1972  C  C     . TYR   A 1 247 ? 138.444 125.740 132.668 1.00 58.47  ?  247  TYR   A C     1 
ATOM   1973  O  O     . TYR   A 1 247 ? 139.278 126.529 132.216 1.00 67.93  ?  247  TYR   A O     1 
ATOM   1974  C  CB    . TYR   A 1 247 ? 139.588 123.761 133.668 1.00 54.25  ?  247  TYR   A CB    1 
ATOM   1975  C  CG    . TYR   A 1 247 ? 140.674 123.537 134.691 1.00 55.43  ?  247  TYR   A CG    1 
ATOM   1976  C  CD1   . TYR   A 1 247 ? 141.693 124.461 134.857 1.00 54.83  ?  247  TYR   A CD1   1 
ATOM   1977  C  CD2   . TYR   A 1 247 ? 140.673 122.411 135.501 1.00 61.02  ?  247  TYR   A CD2   1 
ATOM   1978  C  CE1   . TYR   A 1 247 ? 142.686 124.268 135.793 1.00 61.36  ?  247  TYR   A CE1   1 
ATOM   1979  C  CE2   . TYR   A 1 247 ? 141.664 122.208 136.440 1.00 56.65  ?  247  TYR   A CE2   1 
ATOM   1980  C  CZ    . TYR   A 1 247 ? 142.668 123.140 136.581 1.00 63.24  ?  247  TYR   A CZ    1 
ATOM   1981  O  OH    . TYR   A 1 247 ? 143.658 122.947 137.514 1.00 69.16  ?  247  TYR   A OH    1 
ATOM   1982  N  N     . VAL   A 1 248 ? 137.283 125.509 132.048 1.00 55.01  ?  248  VAL   A N     1 
ATOM   1983  C  CA    . VAL   A 1 248 ? 136.945 126.274 130.849 1.00 50.82  ?  248  VAL   A CA    1 
ATOM   1984  C  C     . VAL   A 1 248 ? 136.663 127.727 131.204 1.00 58.80  ?  248  VAL   A C     1 
ATOM   1985  O  O     . VAL   A 1 248 ? 136.910 128.629 130.394 1.00 67.94  ?  248  VAL   A O     1 
ATOM   1986  C  CB    . VAL   A 1 248 ? 135.759 125.642 130.094 1.00 55.18  ?  248  VAL   A CB    1 
ATOM   1987  C  CG1   . VAL   A 1 248 ? 136.125 124.259 129.580 1.00 55.82  ?  248  VAL   A CG1   1 
ATOM   1988  C  CG2   . VAL   A 1 248 ? 134.514 125.597 130.967 1.00 59.30  ?  248  VAL   A CG2   1 
ATOM   1989  N  N     . SER   A 1 249 ? 136.144 127.983 132.407 1.00 63.40  ?  249  SER   A N     1 
ATOM   1990  C  CA    . SER   A 1 249 ? 135.915 129.354 132.845 1.00 63.93  ?  249  SER   A CA    1 
ATOM   1991  C  C     . SER   A 1 249 ? 137.214 130.131 132.989 1.00 70.25  ?  249  SER   A C     1 
ATOM   1992  O  O     . SER   A 1 249 ? 137.188 131.366 132.998 1.00 77.97  ?  249  SER   A O     1 
ATOM   1993  C  CB    . SER   A 1 249 ? 135.155 129.363 134.167 1.00 62.97  ?  249  SER   A CB    1 
ATOM   1994  O  OG    . SER   A 1 249 ? 135.998 128.986 135.241 1.00 68.09  ?  249  SER   A OG    1 
ATOM   1995  N  N     . GLN   A 1 250 ? 138.343 129.437 133.105 1.00 68.71  ?  250  GLN   A N     1 
ATOM   1996  C  CA    . GLN   A 1 250 ? 139.657 130.059 133.087 1.00 68.27  ?  250  GLN   A CA    1 
ATOM   1997  C  C     . GLN   A 1 250 ? 140.287 130.018 131.703 1.00 72.91  ?  250  GLN   A C     1 
ATOM   1998  O  O     . GLN   A 1 250 ? 141.486 130.281 131.570 1.00 80.62  ?  250  GLN   A O     1 
ATOM   1999  C  CB    . GLN   A 1 250 ? 140.574 129.386 134.108 1.00 71.40  ?  250  GLN   A CB    1 
ATOM   2000  C  CG    . GLN   A 1 250 ? 140.353 129.863 135.532 1.00 74.27  ?  250  GLN   A CG    1 
ATOM   2001  C  CD    . GLN   A 1 250 ? 140.490 128.750 136.548 1.00 80.89  ?  250  GLN   A CD    1 
ATOM   2002  O  OE1   . GLN   A 1 250 ? 141.282 127.826 136.370 1.00 81.98  ?  250  GLN   A OE1   1 
ATOM   2003  N  NE2   . GLN   A 1 250 ? 139.713 128.830 137.621 1.00 80.60  ?  250  GLN   A NE2   1 
ATOM   2004  N  N     . ARG   A 1 251 ? 139.501 129.685 130.676 1.00 79.79  ?  251  ARG   A N     1 
ATOM   2005  C  CA    . ARG   A 1 251 ? 139.958 129.657 129.287 1.00 74.35  ?  251  ARG   A CA    1 
ATOM   2006  C  C     . ARG   A 1 251 ? 141.124 128.687 129.107 1.00 80.08  ?  251  ARG   A C     1 
ATOM   2007  O  O     . ARG   A 1 251 ? 142.146 129.008 128.498 1.00 91.22  ?  251  ARG   A O     1 
ATOM   2008  C  CB    . ARG   A 1 251 ? 140.324 131.062 128.804 1.00 80.75  ?  251  ARG   A CB    1 
ATOM   2009  C  CG    . ARG   A 1 251 ? 139.209 132.067 128.996 1.00 84.04  ?  251  ARG   A CG    1 
ATOM   2010  C  CD    . ARG   A 1 251 ? 139.712 133.506 129.004 1.00 85.67  ?  251  ARG   A CD    1 
ATOM   2011  N  NE    . ARG   A 1 251 ? 140.018 134.041 127.678 1.00 92.53  ?  251  ARG   A NE    1 
ATOM   2012  C  CZ    . ARG   A 1 251 ? 139.213 134.006 126.621 1.00 93.01  ?  251  ARG   A CZ    1 
ATOM   2013  N  NH1   . ARG   A 1 251 ? 137.996 133.489 126.683 1.00 90.63  ?  251  ARG   A NH1   1 
ATOM   2014  N  NH2   . ARG   A 1 251 ? 139.641 134.506 125.466 1.00 89.14  ?  251  ARG   A NH2   1 
ATOM   2015  N  N     . ALA   A 1 252 ? 140.957 127.484 129.645 1.00 55.44  ?  252  ALA   A N     1 
ATOM   2016  C  CA    . ALA   A 1 252 ? 141.958 126.433 129.559 1.00 55.75  ?  252  ALA   A CA    1 
ATOM   2017  C  C     . ALA   A 1 252 ? 141.444 125.297 128.687 1.00 60.65  ?  252  ALA   A C     1 
ATOM   2018  O  O     . ALA   A 1 252 ? 140.289 124.879 128.813 1.00 67.11  ?  252  ALA   A O     1 
ATOM   2019  C  CB    . ALA   A 1 252 ? 142.318 125.902 130.949 1.00 56.47  ?  252  ALA   A CB    1 
ATOM   2020  N  N     . GLY   A 1 253 ? 142.302 124.810 127.795 1.00 62.81  ?  253  GLY   A N     1 
ATOM   2021  C  CA    . GLY   A 1 253 ? 141.946 123.661 126.988 1.00 51.47  ?  253  GLY   A CA    1 
ATOM   2022  C  C     . GLY   A 1 253 ? 141.804 122.408 127.829 1.00 58.19  ?  253  GLY   A C     1 
ATOM   2023  O  O     . GLY   A 1 253 ? 142.411 122.267 128.890 1.00 68.08  ?  253  GLY   A O     1 
ATOM   2024  N  N     . ILE   A 1 254 ? 140.981 121.481 127.347 1.00 53.27  ?  254  ILE   A N     1 
ATOM   2025  C  CA    . ILE   A 1 254 ? 140.626 120.282 128.095 1.00 52.32  ?  254  ILE   A CA    1 
ATOM   2026  C  C     . ILE   A 1 254 ? 141.031 119.054 127.294 1.00 58.03  ?  254  ILE   A C     1 
ATOM   2027  O  O     . ILE   A 1 254 ? 140.735 118.958 126.097 1.00 65.26  ?  254  ILE   A O     1 
ATOM   2028  C  CB    . ILE   A 1 254 ? 139.124 120.238 128.425 1.00 54.48  ?  254  ILE   A CB    1 
ATOM   2029  C  CG1   . ILE   A 1 254 ? 138.625 121.621 128.846 1.00 55.79  ?  254  ILE   A CG1   1 
ATOM   2030  C  CG2   . ILE   A 1 254 ? 138.853 119.219 129.514 1.00 54.20  ?  254  ILE   A CG2   1 
ATOM   2031  C  CD1   . ILE   A 1 254 ? 138.994 122.003 130.258 1.00 49.59  ?  254  ILE   A CD1   1 
ATOM   2032  N  N     . GLY   A 1 255 ? 141.719 118.127 127.953 1.00 57.79  ?  255  GLY   A N     1 
ATOM   2033  C  CA    . GLY   A 1 255 ? 141.943 116.805 127.407 1.00 47.11  ?  255  GLY   A CA    1 
ATOM   2034  C  C     . GLY   A 1 255 ? 141.283 115.755 128.275 1.00 55.39  ?  255  GLY   A C     1 
ATOM   2035  O  O     . GLY   A 1 255 ? 141.727 115.507 129.399 1.00 67.87  ?  255  GLY   A O     1 
ATOM   2036  N  N     . ILE   A 1 256 ? 140.222 115.132 127.772 1.00 57.07  ?  256  ILE   A N     1 
ATOM   2037  C  CA    . ILE   A 1 256 ? 139.434 114.165 128.524 1.00 52.09  ?  256  ILE   A CA    1 
ATOM   2038  C  C     . ILE   A 1 256 ? 139.753 112.769 128.014 1.00 55.15  ?  256  ILE   A C     1 
ATOM   2039  O  O     . ILE   A 1 256 ? 139.860 112.549 126.803 1.00 60.64  ?  256  ILE   A O     1 
ATOM   2040  C  CB    . ILE   A 1 256 ? 137.924 114.450 128.410 1.00 51.27  ?  256  ILE   A CB    1 
ATOM   2041  C  CG1   . ILE   A 1 256 ? 137.637 115.931 128.650 1.00 51.50  ?  256  ILE   A CG1   1 
ATOM   2042  C  CG2   . ILE   A 1 256 ? 137.142 113.591 129.388 1.00 48.44  ?  256  ILE   A CG2   1 
ATOM   2043  C  CD1   . ILE   A 1 256 ? 136.541 116.489 127.773 1.00 56.91  ?  256  ILE   A CD1   1 
ATOM   2044  N  N     . ASN   A 1 257 ? 139.922 111.834 128.941 1.00 56.22  ?  257  ASN   A N     1 
ATOM   2045  C  CA    . ASN   A 1 257 ? 140.067 110.417 128.624 1.00 53.59  ?  257  ASN   A CA    1 
ATOM   2046  C  C     . ASN   A 1 257 ? 138.790 109.726 129.093 1.00 61.38  ?  257  ASN   A C     1 
ATOM   2047  O  O     . ASN   A 1 257 ? 138.688 109.285 130.238 1.00 69.07  ?  257  ASN   A O     1 
ATOM   2048  C  CB    . ASN   A 1 257 ? 141.304 109.820 129.283 1.00 54.12  ?  257  ASN   A CB    1 
ATOM   2049  C  CG    . ASN   A 1 257 ? 141.427 108.329 129.043 1.00 59.56  ?  257  ASN   A CG    1 
ATOM   2050  O  OD1   . ASN   A 1 257 ? 141.004 107.820 128.007 1.00 64.58  ?  257  ASN   A OD1   1 
ATOM   2051  N  ND2   . ASN   A 1 257 ? 142.003 107.620 130.005 1.00 58.66  ?  257  ASN   A ND2   1 
ATOM   2052  N  N     . ALA   A 1 258 ? 137.810 109.638 128.195 1.00 59.12  ?  258  ALA   A N     1 
ATOM   2053  C  CA    . ALA   A 1 258 ? 136.535 109.000 128.485 1.00 63.85  ?  258  ALA   A CA    1 
ATOM   2054  C  C     . ALA   A 1 258 ? 136.431 107.609 127.873 1.00 66.27  ?  258  ALA   A C     1 
ATOM   2055  O  O     . ALA   A 1 258 ? 135.324 107.080 127.734 1.00 75.48  ?  258  ALA   A O     1 
ATOM   2056  C  CB    . ALA   A 1 258 ? 135.383 109.880 128.000 1.00 64.80  ?  258  ALA   A CB    1 
ATOM   2057  N  N     . GLY   A 1 259 ? 137.561 107.005 127.509 1.00 53.53  ?  259  GLY   A N     1 
ATOM   2058  C  CA    . GLY   A 1 259 ? 137.546 105.698 126.882 1.00 55.28  ?  259  GLY   A CA    1 
ATOM   2059  C  C     . GLY   A 1 259 ? 137.233 104.551 127.817 1.00 59.52  ?  259  GLY   A C     1 
ATOM   2060  O  O     . GLY   A 1 259 ? 136.999 103.436 127.339 1.00 70.31  ?  259  GLY   A O     1 
ATOM   2061  N  N     . ARG   A 1 260 ? 137.225 104.790 129.126 1.00 66.14  ?  260  ARG   A N     1 
ATOM   2062  C  CA    . ARG   A 1 260 ? 136.919 103.745 130.092 1.00 68.02  ?  260  ARG   A CA    1 
ATOM   2063  C  C     . ARG   A 1 260 ? 135.426 103.601 130.360 1.00 69.92  ?  260  ARG   A C     1 
ATOM   2064  O  O     . ARG   A 1 260 ? 135.024 102.654 131.043 1.00 73.17  ?  260  ARG   A O     1 
ATOM   2065  C  CB    . ARG   A 1 260 ? 137.656 104.012 131.409 1.00 66.52  ?  260  ARG   A CB    1 
ATOM   2066  C  CG    . ARG   A 1 260 ? 137.926 102.766 132.238 1.00 67.25  ?  260  ARG   A CG    1 
ATOM   2067  C  CD    . ARG   A 1 260 ? 138.221 103.118 133.685 1.00 73.68  ?  260  ARG   A CD    1 
ATOM   2068  N  NE    . ARG   A 1 260 ? 139.415 103.945 133.808 1.00 74.43  ?  260  ARG   A NE    1 
ATOM   2069  C  CZ    . ARG   A 1 260 ? 140.640 103.469 133.981 1.00 78.22  ?  260  ARG   A CZ    1 
ATOM   2070  N  NH1   . ARG   A 1 260 ? 140.873 102.169 134.053 1.00 77.95  ?  260  ARG   A NH1   1 
ATOM   2071  N  NH2   . ARG   A 1 260 ? 141.658 104.319 134.081 1.00 73.51  ?  260  ARG   A NH2   1 
ATOM   2072  N  N     . ILE   A 1 261 ? 134.599 104.507 129.838 1.00 56.14  ?  261  ILE   A N     1 
ATOM   2073  C  CA    . ILE   A 1 261 ? 133.156 104.387 130.000 1.00 48.50  ?  261  ILE   A CA    1 
ATOM   2074  C  C     . ILE   A 1 261 ? 132.666 103.175 129.221 1.00 55.83  ?  261  ILE   A C     1 
ATOM   2075  O  O     . ILE   A 1 261 ? 133.002 102.997 128.043 1.00 65.12  ?  261  ILE   A O     1 
ATOM   2076  C  CB    . ILE   A 1 261 ? 132.452 105.671 129.538 1.00 53.43  ?  261  ILE   A CB    1 
ATOM   2077  C  CG1   . ILE   A 1 261 ? 133.025 106.886 130.272 1.00 56.35  ?  261  ILE   A CG1   1 
ATOM   2078  C  CG2   . ILE   A 1 261 ? 130.953 105.569 129.763 1.00 55.26  ?  261  ILE   A CG2   1 
ATOM   2079  C  CD1   . ILE   A 1 261 ? 132.321 108.184 129.951 1.00 54.03  ?  261  ILE   A CD1   1 
ATOM   2080  N  N     . ARG   A 1 262 ? 131.870 102.335 129.876 1.00 57.57  ?  262  ARG   A N     1 
ATOM   2081  C  CA    . ARG   A 1 262 ? 131.419 101.098 129.261 1.00 53.96  ?  262  ARG   A CA    1 
ATOM   2082  C  C     . ARG   A 1 262 ? 130.486 101.385 128.087 1.00 57.71  ?  262  ARG   A C     1 
ATOM   2083  O  O     . ARG   A 1 262 ? 129.847 102.436 128.003 1.00 68.72  ?  262  ARG   A O     1 
ATOM   2084  C  CB    . ARG   A 1 262 ? 130.727 100.206 130.292 1.00 49.55  ?  262  ARG   A CB    1 
ATOM   2085  C  CG    . ARG   A 1 262 ? 129.345 100.666 130.696 1.00 57.27  ?  262  ARG   A CG    1 
ATOM   2086  C  CD    . ARG   A 1 262 ? 128.881 99.950  131.950 1.00 58.51  ?  262  ARG   A CD    1 
ATOM   2087  N  NE    . ARG   A 1 262 ? 129.835 100.096 133.042 1.00 58.19  ?  262  ARG   A NE    1 
ATOM   2088  C  CZ    . ARG   A 1 262 ? 129.598 99.739  134.296 1.00 57.75  ?  262  ARG   A CZ    1 
ATOM   2089  N  NH1   . ARG   A 1 262 ? 128.449 99.189  134.653 1.00 55.77  ?  262  ARG   A NH1   1 
ATOM   2090  N  NH2   . ARG   A 1 262 ? 130.537 99.940  135.216 1.00 55.12  ?  262  ARG   A NH2   1 
ATOM   2091  N  N     . ALA   A 1 263 ? 130.424 100.427 127.168 1.00 58.88  ?  263  ALA   A N     1 
ATOM   2092  C  CA    . ALA   A 1 263 ? 129.733 100.617 125.905 1.00 59.40  ?  263  ALA   A CA    1 
ATOM   2093  C  C     . ALA   A 1 263 ? 128.219 100.531 126.084 1.00 63.94  ?  263  ALA   A C     1 
ATOM   2094  O  O     . ALA   A 1 263 ? 127.704 100.072 127.106 1.00 64.09  ?  263  ALA   A O     1 
ATOM   2095  C  CB    . ALA   A 1 263 ? 130.202 99.587  124.882 1.00 61.99  ?  263  ALA   A CB    1 
ATOM   2096  N  N     . LEU   A 1 264 ? 127.507 100.991 125.057 1.00 67.62  ?  264  LEU   A N     1 
ATOM   2097  C  CA    . LEU   A 1 264 ? 126.052 100.937 125.053 1.00 63.72  ?  264  LEU   A CA    1 
ATOM   2098  C  C     . LEU   A 1 264 ? 125.568 99.495  125.125 1.00 65.63  ?  264  LEU   A C     1 
ATOM   2099  O  O     . LEU   A 1 264 ? 126.082 98.613  124.431 1.00 69.91  ?  264  LEU   A O     1 
ATOM   2100  C  CB    . LEU   A 1 264 ? 125.510 101.617 123.795 1.00 62.39  ?  264  LEU   A CB    1 
ATOM   2101  C  CG    . LEU   A 1 264 ? 124.116 101.217 123.312 1.00 61.73  ?  264  LEU   A CG    1 
ATOM   2102  C  CD1   . LEU   A 1 264 ? 123.053 101.976 124.078 1.00 66.78  ?  264  LEU   A CD1   1 
ATOM   2103  C  CD2   . LEU   A 1 264 ? 123.984 101.462 121.819 1.00 60.39  ?  264  LEU   A CD2   1 
ATOM   2104  N  N     . GLY   A 1 265 ? 124.570 99.258  125.974 1.00 58.48  ?  265  GLY   A N     1 
ATOM   2105  C  CA    . GLY   A 1 265 ? 124.038 97.932  126.184 1.00 56.99  ?  265  GLY   A CA    1 
ATOM   2106  C  C     . GLY   A 1 265 ? 124.689 97.149  127.302 1.00 63.25  ?  265  GLY   A C     1 
ATOM   2107  O  O     . GLY   A 1 265 ? 124.215 96.052  127.624 1.00 69.63  ?  265  GLY   A O     1 
ATOM   2108  N  N     . SER   A 1 266 ? 125.755 97.670  127.900 1.00 66.71  ?  266  SER   A N     1 
ATOM   2109  C  CA    . SER   A 1 266 ? 126.397 96.975  129.004 1.00 62.08  ?  266  SER   A CA    1 
ATOM   2110  C  C     . SER   A 1 266 ? 125.486 96.983  130.229 1.00 67.15  ?  266  SER   A C     1 
ATOM   2111  O  O     . SER   A 1 266 ? 124.793 97.972  130.482 1.00 71.15  ?  266  SER   A O     1 
ATOM   2112  C  CB    . SER   A 1 266 ? 127.735 97.629  129.344 1.00 64.39  ?  266  SER   A CB    1 
ATOM   2113  O  OG    . SER   A 1 266 ? 128.473 97.925  128.172 1.00 72.78  ?  266  SER   A OG    1 
ATOM   2114  N  N     . PRO   A 1 267 ? 125.455 95.899  130.998 1.00 60.86  ?  267  PRO   A N     1 
ATOM   2115  C  CA    . PRO   A 1 267 ? 124.636 95.886  132.212 1.00 54.57  ?  267  PRO   A CA    1 
ATOM   2116  C  C     . PRO   A 1 267 ? 125.164 96.851  133.260 1.00 59.10  ?  267  PRO   A C     1 
ATOM   2117  O  O     . PRO   A 1 267 ? 126.365 97.112  133.355 1.00 70.37  ?  267  PRO   A O     1 
ATOM   2118  C  CB    . PRO   A 1 267 ? 124.737 94.434  132.693 1.00 49.14  ?  267  PRO   A CB    1 
ATOM   2119  C  CG    . PRO   A 1 267 ? 126.003 93.928  132.100 1.00 54.48  ?  267  PRO   A CG    1 
ATOM   2120  C  CD    . PRO   A 1 267 ? 126.143 94.616  130.778 1.00 52.73  ?  267  PRO   A CD    1 
ATOM   2121  N  N     . ILE   A 1 268 ? 124.240 97.386  134.052 1.00 60.04  ?  268  ILE   A N     1 
ATOM   2122  C  CA    . ILE   A 1 268 ? 124.558 98.253  135.180 1.00 58.76  ?  268  ILE   A CA    1 
ATOM   2123  C  C     . ILE   A 1 268 ? 123.998 97.604  136.436 1.00 65.54  ?  268  ILE   A C     1 
ATOM   2124  O  O     . ILE   A 1 268 ? 122.811 97.262  136.482 1.00 74.55  ?  268  ILE   A O     1 
ATOM   2125  C  CB    . ILE   A 1 268 ? 123.984 99.669  134.995 1.00 60.34  ?  268  ILE   A CB    1 
ATOM   2126  C  CG1   . ILE   A 1 268 ? 124.757 100.420 133.913 1.00 61.38  ?  268  ILE   A CG1   1 
ATOM   2127  C  CG2   . ILE   A 1 268 ? 124.024 100.438 136.304 1.00 56.99  ?  268  ILE   A CG2   1 
ATOM   2128  C  CD1   . ILE   A 1 268 ? 124.001 101.585 133.338 1.00 57.77  ?  268  ILE   A CD1   1 
ATOM   2129  N  N     . ARG   A 1 269 ? 124.853 97.436  137.447 1.00 60.24  ?  269  ARG   A N     1 
ATOM   2130  C  CA    . ARG   A 1 269 ? 124.473 96.781  138.699 1.00 57.80  ?  269  ARG   A CA    1 
ATOM   2131  C  C     . ARG   A 1 269 ? 123.911 95.384  138.442 1.00 68.90  ?  269  ARG   A C     1 
ATOM   2132  O  O     . ARG   A 1 269 ? 122.928 94.967  139.057 1.00 73.06  ?  269  ARG   A O     1 
ATOM   2133  C  CB    . ARG   A 1 269 ? 123.477 97.632  139.489 1.00 58.77  ?  269  ARG   A CB    1 
ATOM   2134  C  CG    . ARG   A 1 269 ? 124.107 98.506  140.554 1.00 63.54  ?  269  ARG   A CG    1 
ATOM   2135  C  CD    . ARG   A 1 269 ? 123.109 99.516  141.088 1.00 62.66  ?  269  ARG   A CD    1 
ATOM   2136  N  NE    . ARG   A 1 269 ? 123.323 100.841 140.522 1.00 65.37  ?  269  ARG   A NE    1 
ATOM   2137  C  CZ    . ARG   A 1 269 ? 122.422 101.507 139.815 1.00 69.57  ?  269  ARG   A CZ    1 
ATOM   2138  N  NH1   . ARG   A 1 269 ? 121.226 101.000 139.567 1.00 66.98  ?  269  ARG   A NH1   1 
ATOM   2139  N  NH2   . ARG   A 1 269 ? 122.729 102.712 139.343 1.00 69.32  ?  269  ARG   A NH2   1 
ATOM   2140  N  N     . GLY   A 1 270 ? 124.538 94.659  137.522 1.00 67.24  ?  270  GLY   A N     1 
ATOM   2141  C  CA    . GLY   A 1 270 ? 124.100 93.313  137.195 1.00 67.72  ?  270  GLY   A CA    1 
ATOM   2142  C  C     . GLY   A 1 270 ? 122.731 93.233  136.556 1.00 69.40  ?  270  GLY   A C     1 
ATOM   2143  O  O     . GLY   A 1 270 ? 121.930 92.365  136.926 1.00 77.75  ?  270  GLY   A O     1 
ATOM   2144  N  N     . GLY   A 1 271 ? 122.439 94.117  135.605 1.00 64.18  ?  271  GLY   A N     1 
ATOM   2145  C  CA    . GLY   A 1 271 ? 121.167 94.110  134.919 1.00 65.52  ?  271  GLY   A CA    1 
ATOM   2146  C  C     . GLY   A 1 271 ? 120.100 94.999  135.517 1.00 66.82  ?  271  GLY   A C     1 
ATOM   2147  O  O     . GLY   A 1 271 ? 118.969 95.000  135.016 1.00 72.57  ?  271  GLY   A O     1 
ATOM   2148  N  N     . GLU   A 1 272 ? 120.416 95.752  136.573 1.00 74.79  ?  272  GLU   A N     1 
ATOM   2149  C  CA    . GLU   A 1 272 ? 119.429 96.655  137.156 1.00 73.08  ?  272  GLU   A CA    1 
ATOM   2150  C  C     . GLU   A 1 272 ? 119.080 97.793  136.207 1.00 74.69  ?  272  GLU   A C     1 
ATOM   2151  O  O     . GLU   A 1 272 ? 117.972 98.337  136.277 1.00 79.10  ?  272  GLU   A O     1 
ATOM   2152  C  CB    . GLU   A 1 272 ? 119.943 97.212  138.482 1.00 71.09  ?  272  GLU   A CB    1 
ATOM   2153  C  CG    . GLU   A 1 272 ? 119.865 96.234  139.639 1.00 80.20  ?  272  GLU   A CG    1 
ATOM   2154  C  CD    . GLU   A 1 272 ? 120.011 96.912  140.986 1.00 86.34  ?  272  GLU   A CD    1 
ATOM   2155  O  OE1   . GLU   A 1 272 ? 119.399 97.982  141.183 1.00 87.76  ?  272  GLU   A OE1   1 
ATOM   2156  O  OE2   . GLU   A 1 272 ? 120.738 96.376  141.848 1.00 82.85  ?  272  GLU   A OE2   1 
ATOM   2157  N  N     . ALA   A 1 273 ? 120.000 98.163  135.321 1.00 61.64  ?  273  ALA   A N     1 
ATOM   2158  C  CA    . ALA   A 1 273 ? 119.768 99.237  134.370 1.00 57.85  ?  273  ALA   A CA    1 
ATOM   2159  C  C     . ALA   A 1 273 ? 120.458 98.906  133.055 1.00 61.76  ?  273  ALA   A C     1 
ATOM   2160  O  O     . ALA   A 1 273 ? 121.383 98.093  133.000 1.00 65.41  ?  273  ALA   A O     1 
ATOM   2161  C  CB    . ALA   A 1 273 ? 120.263 100.586 134.905 1.00 62.06  ?  273  ALA   A CB    1 
ATOM   2162  N  N     . PHE   A 1 274 ? 119.988 99.551  131.993 1.00 63.27  ?  274  PHE   A N     1 
ATOM   2163  C  CA    . PHE   A 1 274 ? 120.533 99.386  130.653 1.00 53.92  ?  274  PHE   A CA    1 
ATOM   2164  C  C     . PHE   A 1 274 ? 121.369 100.616 130.322 1.00 65.07  ?  274  PHE   A C     1 
ATOM   2165  O  O     . PHE   A 1 274 ? 120.856 101.740 130.340 1.00 81.04  ?  274  PHE   A O     1 
ATOM   2166  C  CB    . PHE   A 1 274 ? 119.403 99.200  129.640 1.00 54.09  ?  274  PHE   A CB    1 
ATOM   2167  C  CG    . PHE   A 1 274 ? 119.866 98.999  128.224 1.00 55.65  ?  274  PHE   A CG    1 
ATOM   2168  C  CD1   . PHE   A 1 274 ? 120.084 100.082 127.389 1.00 60.24  ?  274  PHE   A CD1   1 
ATOM   2169  C  CD2   . PHE   A 1 274 ? 120.055 97.725  127.720 1.00 60.01  ?  274  PHE   A CD2   1 
ATOM   2170  C  CE1   . PHE   A 1 274 ? 120.502 99.898  126.086 1.00 63.80  ?  274  PHE   A CE1   1 
ATOM   2171  C  CE2   . PHE   A 1 274 ? 120.471 97.536  126.417 1.00 60.81  ?  274  PHE   A CE2   1 
ATOM   2172  C  CZ    . PHE   A 1 274 ? 120.693 98.624  125.599 1.00 63.80  ?  274  PHE   A CZ    1 
ATOM   2173  N  N     . HIS   A 1 275 ? 122.650 100.406 130.029 1.00 55.15  ?  275  HIS   A N     1 
ATOM   2174  C  CA    . HIS   A 1 275 ? 123.535 101.525 129.734 1.00 46.37  ?  275  HIS   A CA    1 
ATOM   2175  C  C     . HIS   A 1 275 ? 123.163 102.152 128.395 1.00 60.81  ?  275  HIS   A C     1 
ATOM   2176  O  O     . HIS   A 1 275 ? 122.999 101.451 127.395 1.00 71.42  ?  275  HIS   A O     1 
ATOM   2177  C  CB    . HIS   A 1 275 ? 124.991 101.065 129.715 1.00 51.88  ?  275  HIS   A CB    1 
ATOM   2178  C  CG    . HIS   A 1 275 ? 125.973 102.163 129.982 1.00 56.16  ?  275  HIS   A CG    1 
ATOM   2179  N  ND1   . HIS   A 1 275 ? 126.449 102.994 128.992 1.00 64.96  ?  275  HIS   A ND1   1 
ATOM   2180  C  CD2   . HIS   A 1 275 ? 126.565 102.570 131.129 1.00 56.97  ?  275  HIS   A CD2   1 
ATOM   2181  C  CE1   . HIS   A 1 275 ? 127.293 103.864 129.516 1.00 58.70  ?  275  HIS   A CE1   1 
ATOM   2182  N  NE2   . HIS   A 1 275 ? 127.381 103.628 130.812 1.00 56.15  ?  275  HIS   A NE2   1 
ATOM   2183  N  N     . THR   A 1 276 ? 123.072 103.480 128.346 1.00 66.91  ?  276  THR   A N     1 
ATOM   2184  C  CA    . THR   A 1 276 ? 122.612 104.111 127.116 1.00 66.46  ?  276  THR   A CA    1 
ATOM   2185  C  C     . THR   A 1 276 ? 123.787 104.576 126.265 1.00 66.21  ?  276  THR   A C     1 
ATOM   2186  O  O     . THR   A 1 276 ? 123.580 105.173 125.210 1.00 72.29  ?  276  THR   A O     1 
ATOM   2187  C  CB    . THR   A 1 276 ? 121.579 105.212 127.446 1.00 67.51  ?  276  THR   A CB    1 
ATOM   2188  O  OG1   . THR   A 1 276 ? 122.083 106.003 128.515 1.00 75.98  ?  276  THR   A OG1   1 
ATOM   2189  C  CG2   . THR   A 1 276 ? 120.244 104.609 127.871 1.00 66.04  ?  276  THR   A CG2   1 
ATOM   2190  N  N     . GLY   A 1 277 ? 125.014 104.263 126.687 1.00 57.45  ?  277  GLY   A N     1 
ATOM   2191  C  CA    . GLY   A 1 277 ? 126.173 104.494 125.854 1.00 57.27  ?  277  GLY   A CA    1 
ATOM   2192  C  C     . GLY   A 1 277 ? 126.971 105.707 126.284 1.00 64.42  ?  277  GLY   A C     1 
ATOM   2193  O  O     . GLY   A 1 277 ? 126.627 106.433 127.221 1.00 74.44  ?  277  GLY   A O     1 
ATOM   2194  N  N     . CYS   A 1 278 ? 128.073 105.915 125.564 1.00 70.39  ?  278  CYS   A N     1 
ATOM   2195  C  CA    . CYS   A 1 278 ? 128.975 107.022 125.848 1.00 72.72  ?  278  CYS   A CA    1 
ATOM   2196  C  C     . CYS   A 1 278 ? 128.489 108.346 125.276 1.00 72.82  ?  278  CYS   A C     1 
ATOM   2197  O  O     . CYS   A 1 278 ? 128.893 109.401 125.774 1.00 80.93  ?  278  CYS   A O     1 
ATOM   2198  C  CB    . CYS   A 1 278 ? 130.369 106.712 125.299 1.00 71.37  ?  278  CYS   A CB    1 
ATOM   2199  S  SG    . CYS   A 1 278 ? 131.113 105.202 125.955 1.00 98.05  ?  278  CYS   A SG    1 
ATOM   2200  N  N     . ILE   A 1 279 ? 127.635 108.314 124.250 1.00 60.79  ?  279  ILE   A N     1 
ATOM   2201  C  CA    . ILE   A 1 279 ? 127.239 109.552 123.573 1.00 54.59  ?  279  ILE   A CA    1 
ATOM   2202  C  C     . ILE   A 1 279 ? 126.534 110.533 124.505 1.00 59.29  ?  279  ILE   A C     1 
ATOM   2203  O  O     . ILE   A 1 279 ? 126.856 111.731 124.458 1.00 70.77  ?  279  ILE   A O     1 
ATOM   2204  C  CB    . ILE   A 1 279 ? 126.413 109.225 122.316 1.00 61.27  ?  279  ILE   A CB    1 
ATOM   2205  C  CG1   . ILE   A 1 279 ? 127.328 108.738 121.193 1.00 64.48  ?  279  ILE   A CG1   1 
ATOM   2206  C  CG2   . ILE   A 1 279 ? 125.626 110.441 121.855 1.00 60.73  ?  279  ILE   A CG2   1 
ATOM   2207  C  CD1   . ILE   A 1 279 ? 126.626 107.888 120.167 1.00 65.33  ?  279  ILE   A CD1   1 
ATOM   2208  N  N     . PRO   A 1 280 ? 125.567 110.124 125.341 1.00 55.71  ?  280  PRO   A N     1 
ATOM   2209  C  CA    . PRO   A 1 280 ? 124.982 111.103 126.278 1.00 57.19  ?  280  PRO   A CA    1 
ATOM   2210  C  C     . PRO   A 1 280 ? 126.003 111.733 127.212 1.00 59.07  ?  280  PRO   A C     1 
ATOM   2211  O  O     . PRO   A 1 280 ? 125.940 112.941 127.480 1.00 64.19  ?  280  PRO   A O     1 
ATOM   2212  C  CB    . PRO   A 1 280 ? 123.943 110.272 127.042 1.00 53.51  ?  280  PRO   A CB    1 
ATOM   2213  C  CG    . PRO   A 1 280 ? 123.586 109.177 126.111 1.00 55.45  ?  280  PRO   A CG    1 
ATOM   2214  C  CD    . PRO   A 1 280 ? 124.853 108.835 125.396 1.00 51.82  ?  280  PRO   A CD    1 
ATOM   2215  N  N     . PHE   A 1 281 ? 126.968 110.950 127.698 1.00 49.48  ?  281  PHE   A N     1 
ATOM   2216  C  CA    . PHE   A 1 281 ? 128.001 111.514 128.559 1.00 46.95  ?  281  PHE   A CA    1 
ATOM   2217  C  C     . PHE   A 1 281 ? 128.951 112.411 127.777 1.00 53.28  ?  281  PHE   A C     1 
ATOM   2218  O  O     . PHE   A 1 281 ? 129.447 113.405 128.316 1.00 64.42  ?  281  PHE   A O     1 
ATOM   2219  C  CB    . PHE   A 1 281 ? 128.761 110.393 129.263 1.00 48.14  ?  281  PHE   A CB    1 
ATOM   2220  C  CG    . PHE   A 1 281 ? 127.907 109.587 130.194 1.00 52.74  ?  281  PHE   A CG    1 
ATOM   2221  C  CD1   . PHE   A 1 281 ? 127.258 110.193 131.255 1.00 46.76  ?  281  PHE   A CD1   1 
ATOM   2222  C  CD2   . PHE   A 1 281 ? 127.737 108.228 130.001 1.00 53.69  ?  281  PHE   A CD2   1 
ATOM   2223  C  CE1   . PHE   A 1 281 ? 126.466 109.459 132.112 1.00 43.81  ?  281  PHE   A CE1   1 
ATOM   2224  C  CE2   . PHE   A 1 281 ? 126.945 107.489 130.857 1.00 53.08  ?  281  PHE   A CE2   1 
ATOM   2225  C  CZ    . PHE   A 1 281 ? 126.308 108.106 131.912 1.00 49.85  ?  281  PHE   A CZ    1 
ATOM   2226  N  N     . TYR   A 1 282 ? 129.205 112.089 126.508 1.00 48.79  ?  282  TYR   A N     1 
ATOM   2227  C  CA    . TYR   A 1 282 ? 130.000 112.981 125.671 1.00 46.01  ?  282  TYR   A CA    1 
ATOM   2228  C  C     . TYR   A 1 282 ? 129.281 114.306 125.456 1.00 53.38  ?  282  TYR   A C     1 
ATOM   2229  O  O     . TYR   A 1 282 ? 129.910 115.369 125.443 1.00 60.59  ?  282  TYR   A O     1 
ATOM   2230  C  CB    . TYR   A 1 282 ? 130.315 112.313 124.331 1.00 48.03  ?  282  TYR   A CB    1 
ATOM   2231  C  CG    . TYR   A 1 282 ? 131.323 111.183 124.406 1.00 54.27  ?  282  TYR   A CG    1 
ATOM   2232  C  CD1   . TYR   A 1 282 ? 131.701 110.634 125.623 1.00 55.23  ?  282  TYR   A CD1   1 
ATOM   2233  C  CD2   . TYR   A 1 282 ? 131.895 110.666 123.253 1.00 58.07  ?  282  TYR   A CD2   1 
ATOM   2234  C  CE1   . TYR   A 1 282 ? 132.614 109.603 125.690 1.00 56.70  ?  282  TYR   A CE1   1 
ATOM   2235  C  CE2   . TYR   A 1 282 ? 132.813 109.636 123.312 1.00 58.25  ?  282  TYR   A CE2   1 
ATOM   2236  C  CZ    . TYR   A 1 282 ? 133.165 109.107 124.532 1.00 61.28  ?  282  TYR   A CZ    1 
ATOM   2237  O  OH    . TYR   A 1 282 ? 134.080 108.081 124.595 1.00 67.38  ?  282  TYR   A OH    1 
ATOM   2238  N  N     . LYS   A 1 283 ? 127.958 114.261 125.284 1.00 45.99  ?  283  LYS   A N     1 
ATOM   2239  C  CA    . LYS   A 1 283 ? 127.176 115.488 125.168 1.00 49.90  ?  283  LYS   A CA    1 
ATOM   2240  C  C     . LYS   A 1 283 ? 127.218 116.292 126.461 1.00 54.32  ?  283  LYS   A C     1 
ATOM   2241  O  O     . LYS   A 1 283 ? 127.292 117.527 126.433 1.00 61.23  ?  283  LYS   A O     1 
ATOM   2242  C  CB    . LYS   A 1 283 ? 125.733 115.154 124.793 1.00 50.53  ?  283  LYS   A CB    1 
ATOM   2243  C  CG    . LYS   A 1 283 ? 125.556 114.709 123.356 1.00 51.32  ?  283  LYS   A CG    1 
ATOM   2244  C  CD    . LYS   A 1 283 ? 124.116 114.326 123.071 1.00 54.98  ?  283  LYS   A CD    1 
ATOM   2245  C  CE    . LYS   A 1 283 ? 123.827 114.371 121.583 1.00 59.57  ?  283  LYS   A CE    1 
ATOM   2246  N  NZ    . LYS   A 1 283 ? 124.000 115.740 121.028 1.00 64.02  ?  283  LYS   A NZ    1 
ATOM   2247  N  N     . HIS   A 1 284 ? 127.156 115.608 127.606 1.00 48.91  ?  284  HIS   A N     1 
ATOM   2248  C  CA    . HIS   A 1 284 ? 127.293 116.299 128.885 1.00 43.72  ?  284  HIS   A CA    1 
ATOM   2249  C  C     . HIS   A 1 284 ? 128.654 116.976 129.002 1.00 48.87  ?  284  HIS   A C     1 
ATOM   2250  O  O     . HIS   A 1 284 ? 128.750 118.128 129.443 1.00 59.95  ?  284  HIS   A O     1 
ATOM   2251  C  CB    . HIS   A 1 284 ? 127.080 115.318 130.037 1.00 42.88  ?  284  HIS   A CB    1 
ATOM   2252  C  CG    . HIS   A 1 284 ? 126.876 115.981 131.363 1.00 47.05  ?  284  HIS   A CG    1 
ATOM   2253  N  ND1   . HIS   A 1 284 ? 126.050 117.071 131.532 1.00 56.34  ?  284  HIS   A ND1   1 
ATOM   2254  C  CD2   . HIS   A 1 284 ? 127.390 115.707 132.585 1.00 45.05  ?  284  HIS   A CD2   1 
ATOM   2255  C  CE1   . HIS   A 1 284 ? 126.065 117.439 132.799 1.00 50.46  ?  284  HIS   A CE1   1 
ATOM   2256  N  NE2   . HIS   A 1 284 ? 126.871 116.629 133.459 1.00 54.33  ?  284  HIS   A NE2   1 
ATOM   2257  N  N     . PHE   A 1 285 ? 129.717 116.279 128.597 1.00 50.53  ?  285  PHE   A N     1 
ATOM   2258  C  CA    . PHE   A 1 285 ? 131.048 116.879 128.609 1.00 41.87  ?  285  PHE   A CA    1 
ATOM   2259  C  C     . PHE   A 1 285 ? 131.119 118.081 127.677 1.00 45.68  ?  285  PHE   A C     1 
ATOM   2260  O  O     . PHE   A 1 285 ? 131.743 119.095 128.006 1.00 58.86  ?  285  PHE   A O     1 
ATOM   2261  C  CB    . PHE   A 1 285 ? 132.100 115.842 128.214 1.00 41.61  ?  285  PHE   A CB    1 
ATOM   2262  C  CG    . PHE   A 1 285 ? 132.341 114.790 129.257 1.00 45.55  ?  285  PHE   A CG    1 
ATOM   2263  C  CD1   . PHE   A 1 285 ? 132.029 115.025 130.584 1.00 49.66  ?  285  PHE   A CD1   1 
ATOM   2264  C  CD2   . PHE   A 1 285 ? 132.887 113.566 128.909 1.00 49.98  ?  285  PHE   A CD2   1 
ATOM   2265  C  CE1   . PHE   A 1 285 ? 132.252 114.057 131.542 1.00 53.83  ?  285  PHE   A CE1   1 
ATOM   2266  C  CE2   . PHE   A 1 285 ? 133.111 112.596 129.863 1.00 51.16  ?  285  PHE   A CE2   1 
ATOM   2267  C  CZ    . PHE   A 1 285 ? 132.794 112.843 131.181 1.00 48.60  ?  285  PHE   A CZ    1 
ATOM   2268  N  N     . GLN   A 1 286 ? 130.496 117.978 126.502 1.00 43.72  ?  286  GLN   A N     1 
ATOM   2269  C  CA    . GLN   A 1 286 ? 130.503 119.088 125.555 1.00 46.90  ?  286  GLN   A CA    1 
ATOM   2270  C  C     . GLN   A 1 286 ? 129.786 120.307 126.122 1.00 53.68  ?  286  GLN   A C     1 
ATOM   2271  O  O     . GLN   A 1 286 ? 130.264 121.438 125.978 1.00 65.65  ?  286  GLN   A O     1 
ATOM   2272  C  CB    . GLN   A 1 286 ? 129.863 118.655 124.238 1.00 47.51  ?  286  GLN   A CB    1 
ATOM   2273  C  CG    . GLN   A 1 286 ? 129.873 119.725 123.164 1.00 55.37  ?  286  GLN   A CG    1 
ATOM   2274  C  CD    . GLN   A 1 286 ? 129.011 119.356 121.977 1.00 63.46  ?  286  GLN   A CD    1 
ATOM   2275  O  OE1   . GLN   A 1 286 ? 129.471 119.364 120.837 1.00 68.57  ?  286  GLN   A OE1   1 
ATOM   2276  N  NE2   . GLN   A 1 286 ? 127.754 119.023 122.239 1.00 65.96  ?  286  GLN   A NE2   1 
ATOM   2277  N  N     . THR   A 1 287 ? 128.636 120.100 126.767 1.00 53.93  ?  287  THR   A N     1 
ATOM   2278  C  CA    . THR   A 1 287 ? 127.944 121.226 127.388 1.00 50.41  ?  287  THR   A CA    1 
ATOM   2279  C  C     . THR   A 1 287 ? 128.740 121.794 128.555 1.00 53.20  ?  287  THR   A C     1 
ATOM   2280  O  O     . THR   A 1 287 ? 128.671 122.999 128.821 1.00 60.97  ?  287  THR   A O     1 
ATOM   2281  C  CB    . THR   A 1 287 ? 126.547 120.817 127.854 1.00 50.68  ?  287  THR   A CB    1 
ATOM   2282  O  OG1   . THR   A 1 287 ? 126.577 119.479 128.362 1.00 60.29  ?  287  THR   A OG1   1 
ATOM   2283  C  CG2   . THR   A 1 287 ? 125.560 120.905 126.704 1.00 51.91  ?  287  THR   A CG2   1 
ATOM   2284  N  N     . ALA   A 1 288 ? 129.493 120.949 129.261 1.00 52.98  ?  288  ALA   A N     1 
ATOM   2285  C  CA    . ALA   A 1 288 ? 130.403 121.455 130.283 1.00 42.40  ?  288  ALA   A CA    1 
ATOM   2286  C  C     . ALA   A 1 288 ? 131.484 122.334 129.666 1.00 48.51  ?  288  ALA   A C     1 
ATOM   2287  O  O     . ALA   A 1 288 ? 131.854 123.369 130.233 1.00 61.39  ?  288  ALA   A O     1 
ATOM   2288  C  CB    . ALA   A 1 288 ? 131.028 120.292 131.052 1.00 41.69  ?  288  ALA   A CB    1 
ATOM   2289  N  N     . VAL   A 1 289 ? 132.003 121.937 128.503 1.00 52.97  ?  289  VAL   A N     1 
ATOM   2290  C  CA    . VAL   A 1 289 ? 133.034 122.721 127.830 1.00 47.76  ?  289  VAL   A CA    1 
ATOM   2291  C  C     . VAL   A 1 289 ? 132.470 124.053 127.351 1.00 51.04  ?  289  VAL   A C     1 
ATOM   2292  O  O     . VAL   A 1 289 ? 133.148 125.086 127.405 1.00 69.33  ?  289  VAL   A O     1 
ATOM   2293  C  CB    . VAL   A 1 289 ? 133.643 121.911 126.670 1.00 41.85  ?  289  VAL   A CB    1 
ATOM   2294  C  CG1   . VAL   A 1 289 ? 134.590 122.769 125.850 1.00 45.38  ?  289  VAL   A CG1   1 
ATOM   2295  C  CG2   . VAL   A 1 289 ? 134.362 120.688 127.201 1.00 47.50  ?  289  VAL   A CG2   1 
ATOM   2296  N  N     . LYS   A 1 290 ? 131.223 124.056 126.886 1.00 53.11  ?  290  LYS   A N     1 
ATOM   2297  C  CA    . LYS   A 1 290 ? 130.593 125.245 126.330 1.00 51.17  ?  290  LYS   A CA    1 
ATOM   2298  C  C     . LYS   A 1 290 ? 129.755 126.005 127.350 1.00 54.09  ?  290  LYS   A C     1 
ATOM   2299  O  O     . LYS   A 1 290 ? 128.998 126.903 126.967 1.00 65.06  ?  290  LYS   A O     1 
ATOM   2300  C  CB    . LYS   A 1 290 ? 129.728 124.864 125.127 1.00 51.62  ?  290  LYS   A CB    1 
ATOM   2301  C  CG    . LYS   A 1 290 ? 130.478 124.130 124.032 1.00 52.53  ?  290  LYS   A CG    1 
ATOM   2302  C  CD    . LYS   A 1 290 ? 131.541 125.017 123.410 1.00 59.16  ?  290  LYS   A CD    1 
ATOM   2303  C  CE    . LYS   A 1 290 ? 132.175 124.355 122.202 1.00 61.24  ?  290  LYS   A CE    1 
ATOM   2304  N  NZ    . LYS   A 1 290 ? 133.029 125.302 121.439 1.00 63.27  ?  290  LYS   A NZ    1 
ATOM   2305  N  N     . SER   A 1 291 ? 129.869 125.667 128.637 1.00 55.47  ?  291  SER   A N     1 
ATOM   2306  C  CA    . SER   A 1 291 ? 129.039 126.310 129.651 1.00 54.89  ?  291  SER   A CA    1 
ATOM   2307  C  C     . SER   A 1 291 ? 129.352 127.797 129.771 1.00 59.89  ?  291  SER   A C     1 
ATOM   2308  O  O     . SER   A 1 291 ? 128.451 128.612 129.999 1.00 69.31  ?  291  SER   A O     1 
ATOM   2309  C  CB    . SER   A 1 291 ? 129.222 125.613 130.998 1.00 56.22  ?  291  SER   A CB    1 
ATOM   2310  O  OG    . SER   A 1 291 ? 130.595 125.458 131.310 1.00 68.92  ?  291  SER   A OG    1 
ATOM   2311  N  N     . CYS   A 1 292 ? 130.623 128.170 129.629 1.00 67.24  ?  292  CYS   A N     1 
ATOM   2312  C  CA    . CYS   A 1 292 ? 131.050 129.560 129.724 1.00 62.35  ?  292  CYS   A CA    1 
ATOM   2313  C  C     . CYS   A 1 292 ? 131.374 130.152 128.356 1.00 63.23  ?  292  CYS   A C     1 
ATOM   2314  O  O     . CYS   A 1 292 ? 132.227 131.035 128.240 1.00 69.58  ?  292  CYS   A O     1 
ATOM   2315  C  CB    . CYS   A 1 292 ? 132.253 129.684 130.657 1.00 64.52  ?  292  CYS   A CB    1 
ATOM   2316  S  SG    . CYS   A 1 292 ? 131.992 128.999 132.306 1.00 70.25  ?  292  CYS   A SG    1 
ATOM   2317  N  N     . SER   A 1 293 ? 130.700 129.678 127.314 1.00 77.29  ?  293  SER   A N     1 
ATOM   2318  C  CA    . SER   A 1 293 ? 130.953 130.112 125.947 1.00 76.14  ?  293  SER   A CA    1 
ATOM   2319  C  C     . SER   A 1 293 ? 129.863 131.077 125.501 1.00 84.84  ?  293  SER   A C     1 
ATOM   2320  O  O     . SER   A 1 293 ? 128.673 130.807 125.691 1.00 88.02  ?  293  SER   A O     1 
ATOM   2321  C  CB    . SER   A 1 293 ? 131.014 128.913 125.001 1.00 80.82  ?  293  SER   A CB    1 
ATOM   2322  O  OG    . SER   A 1 293 ? 132.307 128.337 124.993 1.00 88.58  ?  293  SER   A OG    1 
ATOM   2323  N  N     . GLN   A 1 294 ? 130.277 132.179 124.890 1.00 100.33 ?  294  GLN   A N     1 
ATOM   2324  C  CA    . GLN   A 1 294 ? 129.323 133.200 124.409 1.00 99.23  ?  294  GLN   A CA    1 
ATOM   2325  C  C     . GLN   A 1 294 ? 128.549 132.600 123.250 1.00 98.85  ?  294  GLN   A C     1 
ATOM   2326  O  O     . GLN   A 1 294 ? 129.151 131.893 122.437 1.00 103.08 ?  294  GLN   A O     1 
ATOM   2327  C  CB    . GLN   A 1 294 ? 130.054 134.464 123.962 1.00 99.94  ?  294  GLN   A CB    1 
ATOM   2328  C  CG    . GLN   A 1 294 ? 129.143 135.604 123.515 1.00 102.09 ?  294  GLN   A CG    1 
ATOM   2329  C  CD    . GLN   A 1 294 ? 128.277 136.163 124.623 1.00 102.23 ?  294  GLN   A CD    1 
ATOM   2330  O  OE1   . GLN   A 1 294 ? 127.093 135.831 124.737 1.00 102.48 ?  294  GLN   A OE1   1 
ATOM   2331  N  NE2   . GLN   A 1 294 ? 128.858 137.001 125.468 1.00 100.34 ?  294  GLN   A NE2   1 
ATOM   2332  N  N     . GLY   A 1 295 ? 127.257 132.863 123.186 1.00 103.71 ?  295  GLY   A N     1 
ATOM   2333  C  CA    . GLY   A 1 295 ? 126.445 132.390 122.087 1.00 107.22 ?  295  GLY   A CA    1 
ATOM   2334  C  C     . GLY   A 1 295 ? 126.243 130.896 122.064 1.00 107.65 ?  295  GLY   A C     1 
ATOM   2335  O  O     . GLY   A 1 295 ? 125.883 130.344 121.021 1.00 108.45 ?  295  GLY   A O     1 
ATOM   2336  N  N     . GLY   A 1 296 ? 126.461 130.223 123.189 1.00 102.22 ?  296  GLY   A N     1 
ATOM   2337  C  CA    . GLY   A 1 296 ? 126.353 128.781 123.240 1.00 102.56 ?  296  GLY   A CA    1 
ATOM   2338  C  C     . GLY   A 1 296 ? 127.645 128.059 122.989 1.00 101.30 ?  296  GLY   A C     1 
ATOM   2339  O  O     . GLY   A 1 296 ? 128.156 127.375 123.879 1.00 99.62  ?  296  GLY   A O     1 
ATOM   2340  N  N     . VAL   A 1 297 ? 128.191 128.203 121.784 1.00 106.19 ?  297  VAL   A N     1 
ATOM   2341  C  CA    . VAL   A 1 297 ? 129.394 127.478 121.375 1.00 106.23 ?  297  VAL   A CA    1 
ATOM   2342  C  C     . VAL   A 1 297 ? 130.385 128.490 120.802 1.00 106.12 ?  297  VAL   A C     1 
ATOM   2343  O  O     . VAL   A 1 297 ? 130.339 128.825 119.605 1.00 110.15 ?  297  VAL   A O     1 
ATOM   2344  C  CB    . VAL   A 1 297 ? 129.087 126.345 120.387 1.00 107.96 ?  297  VAL   A CB    1 
ATOM   2345  C  CG1   . VAL   A 1 297 ? 128.293 125.257 121.090 1.00 104.35 ?  297  VAL   A CG1   1 
ATOM   2346  C  CG2   . VAL   A 1 297 ? 128.275 126.836 119.197 1.00 106.18 ?  297  VAL   A CG2   1 
ATOM   2347  N  N     . ARG   A 1 298 ? 131.278 129.035 121.676 1.00 114.98 ?  298  ARG   A N     1 
ATOM   2348  C  CA    . ARG   A 1 298 ? 132.342 129.797 121.019 1.00 117.10 ?  298  ARG   A CA    1 
ATOM   2349  C  C     . ARG   A 1 298 ? 133.833 129.568 121.352 1.00 115.28 ?  298  ARG   A C     1 
ATOM   2350  O  O     . ARG   A 1 298 ? 134.462 128.977 120.452 1.00 115.83 ?  298  ARG   A O     1 
ATOM   2351  C  CB    . ARG   A 1 298 ? 131.875 131.271 120.857 1.00 114.61 ?  298  ARG   A CB    1 
ATOM   2352  C  CG    . ARG   A 1 298 ? 132.333 131.766 119.463 1.00 111.73 ?  298  ARG   A CG    1 
ATOM   2353  C  CD    . ARG   A 1 298 ? 132.033 133.241 119.278 1.00 114.45 ?  298  ARG   A CD    1 
ATOM   2354  N  NE    . ARG   A 1 298 ? 130.712 133.596 119.783 1.00 120.11 ?  298  ARG   A NE    1 
ATOM   2355  C  CZ    . ARG   A 1 298 ? 129.575 133.356 119.143 1.00 119.70 ?  298  ARG   A CZ    1 
ATOM   2356  N  NH1   . ARG   A 1 298 ? 129.557 132.753 117.966 1.00 116.58 ?  298  ARG   A NH1   1 
ATOM   2357  N  NH2   . ARG   A 1 298 ? 128.427 133.732 119.699 1.00 115.44 ?  298  ARG   A NH2   1 
ATOM   2358  N  N     . GLY   A 1 299 ? 134.389 129.870 122.519 1.00 100.79 ?  299  GLY   A N     1 
ATOM   2359  C  CA    . GLY   A 1 299 ? 135.767 129.549 122.842 1.00 102.82 ?  299  GLY   A CA    1 
ATOM   2360  C  C     . GLY   A 1 299 ? 136.063 128.296 123.646 1.00 100.28 ?  299  GLY   A C     1 
ATOM   2361  O  O     . GLY   A 1 299 ? 137.185 128.165 124.152 1.00 101.94 ?  299  GLY   A O     1 
ATOM   2362  N  N     . GLY   A 1 300 ? 135.114 127.377 123.780 1.00 69.02  ?  300  GLY   A N     1 
ATOM   2363  C  CA    . GLY   A 1 300 ? 135.370 126.141 124.491 1.00 66.36  ?  300  GLY   A CA    1 
ATOM   2364  C  C     . GLY   A 1 300 ? 136.041 125.101 123.618 1.00 74.38  ?  300  GLY   A C     1 
ATOM   2365  O  O     . GLY   A 1 300 ? 135.512 124.735 122.564 1.00 84.76  ?  300  GLY   A O     1 
ATOM   2366  N  N     . ALA   A 1 301 ? 137.207 124.619 124.037 1.00 54.25  ?  301  ALA   A N     1 
ATOM   2367  C  CA    . ALA   A 1 301 ? 137.979 123.653 123.268 1.00 51.05  ?  301  ALA   A CA    1 
ATOM   2368  C  C     . ALA   A 1 301 ? 138.262 122.430 124.125 1.00 55.39  ?  301  ALA   A C     1 
ATOM   2369  O  O     . ALA   A 1 301 ? 138.714 122.559 125.267 1.00 58.79  ?  301  ALA   A O     1 
ATOM   2370  C  CB    . ALA   A 1 301 ? 139.290 124.264 122.771 1.00 54.20  ?  301  ALA   A CB    1 
ATOM   2371  N  N     . ALA   A 1 302 ? 138.001 121.248 123.572 1.00 55.11  ?  302  ALA   A N     1 
ATOM   2372  C  CA    . ALA   A 1 302 ? 138.254 120.002 124.277 1.00 41.49  ?  302  ALA   A CA    1 
ATOM   2373  C  C     . ALA   A 1 302 ? 138.607 118.915 123.275 1.00 49.04  ?  302  ALA   A C     1 
ATOM   2374  O  O     . ALA   A 1 302 ? 138.198 118.962 122.113 1.00 55.94  ?  302  ALA   A O     1 
ATOM   2375  C  CB    . ALA   A 1 302 ? 137.047 119.570 125.115 1.00 49.75  ?  302  ALA   A CB    1 
ATOM   2376  N  N     . THR   A 1 303 ? 139.377 117.936 123.743 1.00 50.64  ?  303  THR   A N     1 
ATOM   2377  C  CA    . THR   A 1 303 ? 139.725 116.760 122.957 1.00 44.34  ?  303  THR   A CA    1 
ATOM   2378  C  C     . THR   A 1 303 ? 139.469 115.519 123.797 1.00 50.21  ?  303  THR   A C     1 
ATOM   2379  O  O     . THR   A 1 303 ? 139.987 115.406 124.911 1.00 64.85  ?  303  THR   A O     1 
ATOM   2380  C  CB    . THR   A 1 303 ? 141.188 116.796 122.504 1.00 48.78  ?  303  THR   A CB    1 
ATOM   2381  O  OG1   . THR   A 1 303 ? 141.406 117.943 121.674 1.00 68.55  ?  303  THR   A OG1   1 
ATOM   2382  C  CG2   . THR   A 1 303 ? 141.532 115.542 121.719 1.00 40.46  ?  303  THR   A CG2   1 
ATOM   2383  N  N     . LEU   A 1 304 ? 138.688 114.589 123.257 1.00 47.23  ?  304  LEU   A N     1 
ATOM   2384  C  CA    . LEU   A 1 304 ? 138.284 113.385 123.967 1.00 42.23  ?  304  LEU   A CA    1 
ATOM   2385  C  C     . LEU   A 1 304 ? 138.977 112.169 123.365 1.00 50.15  ?  304  LEU   A C     1 
ATOM   2386  O  O     . LEU   A 1 304 ? 139.066 112.036 122.142 1.00 59.03  ?  304  LEU   A O     1 
ATOM   2387  C  CB    . LEU   A 1 304 ? 136.764 113.212 123.914 1.00 53.10  ?  304  LEU   A CB    1 
ATOM   2388  C  CG    . LEU   A 1 304 ? 136.111 112.342 124.985 1.00 55.98  ?  304  LEU   A CG    1 
ATOM   2389  C  CD1   . LEU   A 1 304 ? 134.732 112.873 125.325 1.00 52.32  ?  304  LEU   A CD1   1 
ATOM   2390  C  CD2   . LEU   A 1 304 ? 136.031 110.902 124.516 1.00 58.04  ?  304  LEU   A CD2   1 
ATOM   2391  N  N     . PHE   A 1 305 ? 139.462 111.280 124.228 1.00 49.09  ?  305  PHE   A N     1 
ATOM   2392  C  CA    . PHE   A 1 305 ? 140.250 110.129 123.810 1.00 41.79  ?  305  PHE   A CA    1 
ATOM   2393  C  C     . PHE   A 1 305 ? 139.527 108.836 124.156 1.00 49.67  ?  305  PHE   A C     1 
ATOM   2394  O  O     . PHE   A 1 305 ? 138.931 108.715 125.230 1.00 66.45  ?  305  PHE   A O     1 
ATOM   2395  C  CB    . PHE   A 1 305 ? 141.632 110.139 124.468 1.00 39.83  ?  305  PHE   A CB    1 
ATOM   2396  C  CG    . PHE   A 1 305 ? 142.491 111.296 124.052 1.00 51.89  ?  305  PHE   A CG    1 
ATOM   2397  C  CD1   . PHE   A 1 305 ? 142.390 112.517 124.696 1.00 48.18  ?  305  PHE   A CD1   1 
ATOM   2398  C  CD2   . PHE   A 1 305 ? 143.396 111.166 123.015 1.00 48.62  ?  305  PHE   A CD2   1 
ATOM   2399  C  CE1   . PHE   A 1 305 ? 143.176 113.582 124.314 1.00 51.45  ?  305  PHE   A CE1   1 
ATOM   2400  C  CE2   . PHE   A 1 305 ? 144.184 112.229 122.630 1.00 52.07  ?  305  PHE   A CE2   1 
ATOM   2401  C  CZ    . PHE   A 1 305 ? 144.074 113.438 123.280 1.00 54.75  ?  305  PHE   A CZ    1 
ATOM   2402  N  N     . TYR   A 1 306 ? 139.584 107.873 123.239 1.00 50.80  ?  306  TYR   A N     1 
ATOM   2403  C  CA    . TYR   A 1 306 ? 139.014 106.550 123.446 1.00 45.47  ?  306  TYR   A CA    1 
ATOM   2404  C  C     . TYR   A 1 306 ? 139.847 105.541 122.673 1.00 48.61  ?  306  TYR   A C     1 
ATOM   2405  O  O     . TYR   A 1 306 ? 140.440 105.891 121.647 1.00 57.37  ?  306  TYR   A O     1 
ATOM   2406  C  CB    . TYR   A 1 306 ? 137.547 106.486 122.994 1.00 41.73  ?  306  TYR   A CB    1 
ATOM   2407  C  CG    . TYR   A 1 306 ? 137.313 106.989 121.588 1.00 48.61  ?  306  TYR   A CG    1 
ATOM   2408  C  CD1   . TYR   A 1 306 ? 137.057 108.330 121.343 1.00 51.65  ?  306  TYR   A CD1   1 
ATOM   2409  C  CD2   . TYR   A 1 306 ? 137.349 106.123 120.505 1.00 48.84  ?  306  TYR   A CD2   1 
ATOM   2410  C  CE1   . TYR   A 1 306 ? 136.845 108.794 120.062 1.00 52.85  ?  306  TYR   A CE1   1 
ATOM   2411  C  CE2   . TYR   A 1 306 ? 137.137 106.579 119.219 1.00 50.78  ?  306  TYR   A CE2   1 
ATOM   2412  C  CZ    . TYR   A 1 306 ? 136.886 107.915 119.004 1.00 57.44  ?  306  TYR   A CZ    1 
ATOM   2413  O  OH    . TYR   A 1 306 ? 136.673 108.374 117.726 1.00 62.33  ?  306  TYR   A OH    1 
ATOM   2414  N  N     . PRO   A 1 307 ? 139.920 104.295 123.136 1.00 49.55  ?  307  PRO   A N     1 
ATOM   2415  C  CA    . PRO   A 1 307 ? 140.671 103.279 122.393 1.00 44.51  ?  307  PRO   A CA    1 
ATOM   2416  C  C     . PRO   A 1 307 ? 139.966 102.885 121.105 1.00 47.49  ?  307  PRO   A C     1 
ATOM   2417  O  O     . PRO   A 1 307 ? 138.746 103.002 120.972 1.00 61.60  ?  307  PRO   A O     1 
ATOM   2418  C  CB    . PRO   A 1 307 ? 140.739 102.102 123.372 1.00 45.79  ?  307  PRO   A CB    1 
ATOM   2419  C  CG    . PRO   A 1 307 ? 139.557 102.282 124.251 1.00 55.03  ?  307  PRO   A CG    1 
ATOM   2420  C  CD    . PRO   A 1 307 ? 139.362 103.763 124.390 1.00 51.65  ?  307  PRO   A CD    1 
ATOM   2421  N  N     . MET   A 1 308 ? 140.763 102.408 120.146 1.00 63.05  ?  308  MET   A N     1 
ATOM   2422  C  CA    . MET   A 1 308 ? 140.215 102.004 118.854 1.00 61.49  ?  308  MET   A CA    1 
ATOM   2423  C  C     . MET   A 1 308 ? 139.321 100.776 118.986 1.00 63.41  ?  308  MET   A C     1 
ATOM   2424  O  O     . MET   A 1 308 ? 138.312 100.659 118.282 1.00 71.69  ?  308  MET   A O     1 
ATOM   2425  C  CB    . MET   A 1 308 ? 141.353 101.745 117.864 1.00 61.91  ?  308  MET   A CB    1 
ATOM   2426  C  CG    . MET   A 1 308 ? 141.019 100.761 116.755 1.00 69.90  ?  308  MET   A CG    1 
ATOM   2427  S  SD    . MET   A 1 308 ? 142.003 101.009 115.266 1.00 92.61  ?  308  MET   A SD    1 
ATOM   2428  C  CE    . MET   A 1 308 ? 141.058 102.288 114.445 1.00 69.05  ?  308  MET   A CE    1 
ATOM   2429  N  N     . TRP   A 1 309 ? 139.666 99.858  119.885 1.00 56.68  ?  309  TRP   A N     1 
ATOM   2430  C  CA    . TRP   A 1 309 ? 138.922 98.616  120.045 1.00 53.37  ?  309  TRP   A CA    1 
ATOM   2431  C  C     . TRP   A 1 309 ? 137.660 98.774  120.886 1.00 52.99  ?  309  TRP   A C     1 
ATOM   2432  O  O     . TRP   A 1 309 ? 137.071 97.763  121.280 1.00 56.19  ?  309  TRP   A O     1 
ATOM   2433  C  CB    . TRP   A 1 309 ? 139.821 97.541  120.662 1.00 52.70  ?  309  TRP   A CB    1 
ATOM   2434  C  CG    . TRP   A 1 309 ? 140.512 97.981  121.912 1.00 50.98  ?  309  TRP   A CG    1 
ATOM   2435  C  CD1   . TRP   A 1 309 ? 141.745 98.550  122.006 1.00 52.48  ?  309  TRP   A CD1   1 
ATOM   2436  C  CD2   . TRP   A 1 309 ? 140.011 97.885  123.251 1.00 51.60  ?  309  TRP   A CD2   1 
ATOM   2437  N  NE1   . TRP   A 1 309 ? 142.043 98.819  123.319 1.00 57.42  ?  309  TRP   A NE1   1 
ATOM   2438  C  CE2   . TRP   A 1 309 ? 140.996 98.417  124.104 1.00 56.14  ?  309  TRP   A CE2   1 
ATOM   2439  C  CE3   . TRP   A 1 309 ? 138.827 97.400  123.811 1.00 48.29  ?  309  TRP   A CE3   1 
ATOM   2440  C  CZ2   . TRP   A 1 309 ? 140.832 98.481  125.484 1.00 56.45  ?  309  TRP   A CZ2   1 
ATOM   2441  C  CZ3   . TRP   A 1 309 ? 138.667 97.465  125.181 1.00 49.28  ?  309  TRP   A CZ3   1 
ATOM   2442  C  CH2   . TRP   A 1 309 ? 139.663 98.000  126.002 1.00 52.76  ?  309  TRP   A CH2   1 
ATOM   2443  N  N     . HIS   A 1 310 ? 137.236 100.002 121.176 1.00 57.85  ?  310  HIS   A N     1 
ATOM   2444  C  CA    . HIS   A 1 310 ? 136.001 100.205 121.922 1.00 49.38  ?  310  HIS   A CA    1 
ATOM   2445  C  C     . HIS   A 1 310 ? 134.813 99.682  121.125 1.00 60.54  ?  310  HIS   A C     1 
ATOM   2446  O  O     . HIS   A 1 310 ? 134.768 99.799  119.898 1.00 73.26  ?  310  HIS   A O     1 
ATOM   2447  C  CB    . HIS   A 1 310 ? 135.815 101.688 122.243 1.00 53.00  ?  310  HIS   A CB    1 
ATOM   2448  C  CG    . HIS   A 1 310 ? 134.888 101.947 123.389 1.00 59.59  ?  310  HIS   A CG    1 
ATOM   2449  N  ND1   . HIS   A 1 310 ? 133.517 101.933 123.255 1.00 64.10  ?  310  HIS   A ND1   1 
ATOM   2450  C  CD2   . HIS   A 1 310 ? 135.136 102.225 124.690 1.00 58.13  ?  310  HIS   A CD2   1 
ATOM   2451  C  CE1   . HIS   A 1 310 ? 132.960 102.191 124.424 1.00 61.46  ?  310  HIS   A CE1   1 
ATOM   2452  N  NE2   . HIS   A 1 310 ? 133.920 102.373 125.312 1.00 55.99  ?  310  HIS   A NE2   1 
ATOM   2453  N  N     . LEU   A 1 311 ? 133.845 99.094  121.832 1.00 53.02  ?  311  LEU   A N     1 
ATOM   2454  C  CA    . LEU   A 1 311 ? 132.693 98.498  121.165 1.00 54.55  ?  311  LEU   A CA    1 
ATOM   2455  C  C     . LEU   A 1 311 ? 131.855 99.527  120.419 1.00 61.59  ?  311  LEU   A C     1 
ATOM   2456  O  O     . LEU   A 1 311 ? 131.150 99.167  119.469 1.00 70.13  ?  311  LEU   A O     1 
ATOM   2457  C  CB    . LEU   A 1 311 ? 131.827 97.755  122.183 1.00 55.03  ?  311  LEU   A CB    1 
ATOM   2458  C  CG    . LEU   A 1 311 ? 130.683 96.903  121.632 1.00 59.98  ?  311  LEU   A CG    1 
ATOM   2459  C  CD1   . LEU   A 1 311 ? 131.176 95.519  121.261 1.00 57.17  ?  311  LEU   A CD1   1 
ATOM   2460  C  CD2   . LEU   A 1 311 ? 129.545 96.814  122.630 1.00 60.60  ?  311  LEU   A CD2   1 
ATOM   2461  N  N     . GLU   A 1 312 ? 131.924 100.797 120.813 1.00 71.31  ?  312  GLU   A N     1 
ATOM   2462  C  CA    . GLU   A 1 312 ? 131.151 101.860 120.186 1.00 68.23  ?  312  GLU   A CA    1 
ATOM   2463  C  C     . GLU   A 1 312 ? 131.978 102.687 119.208 1.00 72.60  ?  312  GLU   A C     1 
ATOM   2464  O  O     . GLU   A 1 312 ? 131.544 103.771 118.808 1.00 80.44  ?  312  GLU   A O     1 
ATOM   2465  C  CB    . GLU   A 1 312 ? 130.543 102.767 121.257 1.00 69.64  ?  312  GLU   A CB    1 
ATOM   2466  C  CG    . GLU   A 1 312 ? 129.207 102.291 121.797 1.00 74.47  ?  312  GLU   A CG    1 
ATOM   2467  C  CD    . GLU   A 1 312 ? 128.588 103.279 122.766 1.00 80.34  ?  312  GLU   A CD    1 
ATOM   2468  O  OE1   . GLU   A 1 312 ? 127.998 104.278 122.304 1.00 78.24  ?  312  GLU   A OE1   1 
ATOM   2469  O  OE2   . GLU   A 1 312 ? 128.692 103.059 123.990 1.00 82.26  ?  312  GLU   A OE2   1 
ATOM   2470  N  N     . VAL   A 1 313 ? 133.148 102.186 118.799 1.00 62.80  ?  313  VAL   A N     1 
ATOM   2471  C  CA    . VAL   A 1 313 ? 134.088 102.997 118.026 1.00 60.95  ?  313  VAL   A CA    1 
ATOM   2472  C  C     . VAL   A 1 313 ? 133.485 103.417 116.690 1.00 67.67  ?  313  VAL   A C     1 
ATOM   2473  O  O     . VAL   A 1 313 ? 133.750 104.520 116.197 1.00 70.56  ?  313  VAL   A O     1 
ATOM   2474  C  CB    . VAL   A 1 313 ? 135.421 102.246 117.839 1.00 53.94  ?  313  VAL   A CB    1 
ATOM   2475  C  CG1   . VAL   A 1 313 ? 135.233 100.992 116.996 1.00 58.52  ?  313  VAL   A CG1   1 
ATOM   2476  C  CG2   . VAL   A 1 313 ? 136.465 103.161 117.217 1.00 58.17  ?  313  VAL   A CG2   1 
ATOM   2477  N  N     . GLU   A 1 314 ? 132.674 102.552 116.077 1.00 75.79  ?  314  GLU   A N     1 
ATOM   2478  C  CA    . GLU   A 1 314 ? 132.059 102.905 114.801 1.00 70.57  ?  314  GLU   A CA    1 
ATOM   2479  C  C     . GLU   A 1 314 ? 131.096 104.074 114.961 1.00 73.77  ?  314  GLU   A C     1 
ATOM   2480  O  O     . GLU   A 1 314 ? 131.012 104.944 114.086 1.00 75.04  ?  314  GLU   A O     1 
ATOM   2481  C  CB    . GLU   A 1 314 ? 131.344 101.693 114.206 1.00 73.21  ?  314  GLU   A CB    1 
ATOM   2482  C  CG    . GLU   A 1 314 ? 132.239 100.811 113.356 1.00 77.72  ?  314  GLU   A CG    1 
ATOM   2483  C  CD    . GLU   A 1 314 ? 131.674 99.419  113.167 1.00 87.23  ?  314  GLU   A CD    1 
ATOM   2484  O  OE1   . GLU   A 1 314 ? 131.177 98.839  114.155 1.00 88.11  ?  314  GLU   A OE1   1 
ATOM   2485  O  OE2   . GLU   A 1 314 ? 131.729 98.903  112.031 1.00 86.58  ?  314  GLU   A OE2   1 
ATOM   2486  N  N     . SER   A 1 315 ? 130.361 104.111 116.071 1.00 74.13  ?  315  SER   A N     1 
ATOM   2487  C  CA    . SER   A 1 315 ? 129.458 105.217 116.354 1.00 69.06  ?  315  SER   A CA    1 
ATOM   2488  C  C     . SER   A 1 315 ? 130.165 106.430 116.946 1.00 71.73  ?  315  SER   A C     1 
ATOM   2489  O  O     . SER   A 1 315 ? 129.576 107.515 116.971 1.00 76.95  ?  315  SER   A O     1 
ATOM   2490  C  CB    . SER   A 1 315 ? 128.349 104.754 117.300 1.00 68.13  ?  315  SER   A CB    1 
ATOM   2491  O  OG    . SER   A 1 315 ? 127.911 105.814 118.128 1.00 84.47  ?  315  SER   A OG    1 
ATOM   2492  N  N     . LEU   A 1 316 ? 131.403 106.278 117.418 1.00 63.39  ?  316  LEU   A N     1 
ATOM   2493  C  CA    . LEU   A 1 316 ? 132.158 107.404 117.953 1.00 56.60  ?  316  LEU   A CA    1 
ATOM   2494  C  C     . LEU   A 1 316 ? 133.001 108.101 116.896 1.00 64.58  ?  316  LEU   A C     1 
ATOM   2495  O  O     . LEU   A 1 316 ? 133.264 109.302 117.019 1.00 77.65  ?  316  LEU   A O     1 
ATOM   2496  C  CB    . LEU   A 1 316 ? 133.069 106.944 119.095 1.00 52.46  ?  316  LEU   A CB    1 
ATOM   2497  C  CG    . LEU   A 1 316 ? 132.408 106.356 120.342 1.00 60.98  ?  316  LEU   A CG    1 
ATOM   2498  C  CD1   . LEU   A 1 316 ? 133.461 105.902 121.339 1.00 57.82  ?  316  LEU   A CD1   1 
ATOM   2499  C  CD2   . LEU   A 1 316 ? 131.455 107.354 120.975 1.00 68.35  ?  316  LEU   A CD2   1 
ATOM   2500  N  N     . LEU   A 1 317 ? 133.434 107.375 115.863 1.00 58.78  ?  317  LEU   A N     1 
ATOM   2501  C  CA    . LEU   A 1 317 ? 134.266 107.978 114.828 1.00 58.74  ?  317  LEU   A CA    1 
ATOM   2502  C  C     . LEU   A 1 317 ? 133.491 108.991 113.997 1.00 62.79  ?  317  LEU   A C     1 
ATOM   2503  O  O     . LEU   A 1 317 ? 134.078 109.951 113.486 1.00 66.75  ?  317  LEU   A O     1 
ATOM   2504  C  CB    . LEU   A 1 317 ? 134.848 106.892 113.925 1.00 57.53  ?  317  LEU   A CB    1 
ATOM   2505  C  CG    . LEU   A 1 317 ? 136.049 106.117 114.466 1.00 57.58  ?  317  LEU   A CG    1 
ATOM   2506  C  CD1   . LEU   A 1 317 ? 136.311 104.882 113.622 1.00 58.23  ?  317  LEU   A CD1   1 
ATOM   2507  C  CD2   . LEU   A 1 317 ? 137.277 107.007 114.513 1.00 57.97  ?  317  LEU   A CD2   1 
ATOM   2508  N  N     . VAL   A 1 318 ? 132.184 108.800 113.855 1.00 65.43  ?  318  VAL   A N     1 
ATOM   2509  C  CA    . VAL   A 1 318 ? 131.358 109.660 113.023 1.00 59.55  ?  318  VAL   A CA    1 
ATOM   2510  C  C     . VAL   A 1 318 ? 130.692 110.765 113.844 1.00 61.29  ?  318  VAL   A C     1 
ATOM   2511  O  O     . VAL   A 1 318 ? 129.752 111.400 113.373 1.00 74.80  ?  318  VAL   A O     1 
ATOM   2512  C  CB    . VAL   A 1 318 ? 130.315 108.848 112.241 1.00 58.74  ?  318  VAL   A CB    1 
ATOM   2513  C  CG1   . VAL   A 1 318 ? 131.001 107.876 111.298 1.00 62.09  ?  318  VAL   A CG1   1 
ATOM   2514  C  CG2   . VAL   A 1 318 ? 129.395 108.110 113.198 1.00 58.07  ?  318  VAL   A CG2   1 
ATOM   2515  N  N     . LEU   A 1 319 ? 131.176 111.014 115.062 1.00 57.76  ?  319  LEU   A N     1 
ATOM   2516  C  CA    . LEU   A 1 319 ? 130.543 111.982 115.949 1.00 54.59  ?  319  LEU   A CA    1 
ATOM   2517  C  C     . LEU   A 1 319 ? 130.679 113.420 115.467 1.00 58.89  ?  319  LEU   A C     1 
ATOM   2518  O  O     . LEU   A 1 319 ? 130.001 114.298 116.010 1.00 65.65  ?  319  LEU   A O     1 
ATOM   2519  C  CB    . LEU   A 1 319 ? 131.131 111.866 117.356 1.00 46.89  ?  319  LEU   A CB    1 
ATOM   2520  C  CG    . LEU   A 1 319 ? 130.522 110.820 118.291 1.00 52.88  ?  319  LEU   A CG    1 
ATOM   2521  C  CD1   . LEU   A 1 319 ? 131.180 110.885 119.657 1.00 55.79  ?  319  LEU   A CD1   1 
ATOM   2522  C  CD2   . LEU   A 1 319 ? 129.019 111.008 118.408 1.00 55.40  ?  319  LEU   A CD2   1 
ATOM   2523  N  N     . LYS   A 1 320 ? 131.523 113.688 114.471 1.00 60.34  ?  320  LYS   A N     1 
ATOM   2524  C  CA    . LYS   A 1 320 ? 131.809 115.056 114.068 1.00 58.89  ?  320  LYS   A CA    1 
ATOM   2525  C  C     . LYS   A 1 320 ? 131.302 115.423 112.680 1.00 66.04  ?  320  LYS   A C     1 
ATOM   2526  O  O     . LYS   A 1 320 ? 131.326 116.608 112.332 1.00 71.29  ?  320  LYS   A O     1 
ATOM   2527  C  CB    . LYS   A 1 320 ? 133.320 115.321 114.135 1.00 56.02  ?  320  LYS   A CB    1 
ATOM   2528  C  CG    . LYS   A 1 320 ? 133.689 116.514 114.998 1.00 59.41  ?  320  LYS   A CG    1 
ATOM   2529  C  CD    . LYS   A 1 320 ? 135.179 116.788 114.974 1.00 56.25  ?  320  LYS   A CD    1 
ATOM   2530  C  CE    . LYS   A 1 320 ? 135.500 118.091 115.684 1.00 58.40  ?  320  LYS   A CE    1 
ATOM   2531  N  NZ    . LYS   A 1 320 ? 134.973 119.271 114.951 1.00 64.10  ?  320  LYS   A NZ    1 
ATOM   2532  N  N     . ASN   A 1 321 ? 130.849 114.463 111.879 1.00 59.40  ?  321  ASN   A N     1 
ATOM   2533  C  CA    . ASN   A 1 321 ? 130.356 114.797 110.551 1.00 58.67  ?  321  ASN   A CA    1 
ATOM   2534  C  C     . ASN   A 1 321 ? 128.886 115.215 110.608 1.00 66.30  ?  321  ASN   A C     1 
ATOM   2535  O  O     . ASN   A 1 321 ? 128.189 114.999 111.601 1.00 70.52  ?  321  ASN   A O     1 
ATOM   2536  C  CB    . ASN   A 1 321 ? 130.559 113.631 109.577 1.00 61.97  ?  321  ASN   A CB    1 
ATOM   2537  C  CG    . ASN   A 1 321 ? 129.845 112.361 110.003 1.00 62.91  ?  321  ASN   A CG    1 
ATOM   2538  O  OD1   . ASN   A 1 321 ? 128.651 112.365 110.298 1.00 62.93  ?  321  ASN   A OD1   1 
ATOM   2539  N  ND2   . ASN   A 1 321 ? 130.578 111.257 110.013 1.00 69.49  ?  321  ASN   A ND2   1 
ATOM   2540  N  N     . ASN   A 1 322 ? 128.401 115.818 109.518 1.00 80.51  ?  322  ASN   A N     1 
ATOM   2541  C  CA    . ASN   A 1 322 ? 127.038 116.354 109.511 1.00 78.70  ?  322  ASN   A CA    1 
ATOM   2542  C  C     . ASN   A 1 322 ? 126.009 115.357 109.002 1.00 78.94  ?  322  ASN   A C     1 
ATOM   2543  O  O     . ASN   A 1 322 ? 124.820 115.685 108.950 1.00 81.06  ?  322  ASN   A O     1 
ATOM   2544  C  CB    . ASN   A 1 322 ? 126.973 117.663 108.710 1.00 76.49  ?  322  ASN   A CB    1 
ATOM   2545  C  CG    . ASN   A 1 322 ? 127.126 118.878 109.597 1.00 83.63  ?  322  ASN   A CG    1 
ATOM   2546  O  OD1   . ASN   A 1 322 ? 128.237 119.237 109.980 1.00 87.33  ?  322  ASN   A OD1   1 
ATOM   2547  N  ND2   . ASN   A 1 322 ? 126.014 119.506 109.943 1.00 85.53  ?  322  ASN   A ND2   1 
ATOM   2548  N  N     . ARG   A 1 323 ? 126.434 114.143 108.657 1.00 75.26  ?  323  ARG   A N     1 
ATOM   2549  C  CA    . ARG   A 1 323 ? 125.501 113.166 108.121 1.00 73.30  ?  323  ARG   A CA    1 
ATOM   2550  C  C     . ARG   A 1 323 ? 124.507 112.663 109.158 1.00 73.25  ?  323  ARG   A C     1 
ATOM   2551  O  O     . ARG   A 1 323 ? 123.567 111.952 108.789 1.00 80.10  ?  323  ARG   A O     1 
ATOM   2552  C  CB    . ARG   A 1 323 ? 126.262 111.985 107.522 1.00 74.63  ?  323  ARG   A CB    1 
ATOM   2553  C  CG    . ARG   A 1 323 ? 127.251 112.375 106.442 1.00 75.36  ?  323  ARG   A CG    1 
ATOM   2554  C  CD    . ARG   A 1 323 ? 127.644 111.178 105.596 1.00 79.20  ?  323  ARG   A CD    1 
ATOM   2555  N  NE    . ARG   A 1 323 ? 127.089 111.258 104.250 1.00 81.86  ?  323  ARG   A NE    1 
ATOM   2556  C  CZ    . ARG   A 1 323 ? 127.592 112.003 103.276 1.00 84.74  ?  323  ARG   A CZ    1 
ATOM   2557  N  NH1   . ARG   A 1 323 ? 128.670 112.748 103.461 1.00 83.44  ?  323  ARG   A NH1   1 
ATOM   2558  N  NH2   . ARG   A 1 323 ? 127.000 112.000 102.085 1.00 81.44  ?  323  ARG   A NH2   1 
ATOM   2559  N  N     . GLY   A 1 324 ? 124.687 113.001 110.434 1.00 66.98  ?  324  GLY   A N     1 
ATOM   2560  C  CA    . GLY   A 1 324 ? 123.809 112.553 111.489 1.00 60.25  ?  324  GLY   A CA    1 
ATOM   2561  C  C     . GLY   A 1 324 ? 122.979 113.684 112.078 1.00 59.88  ?  324  GLY   A C     1 
ATOM   2562  O  O     . GLY   A 1 324 ? 123.180 114.864 111.799 1.00 67.19  ?  324  GLY   A O     1 
ATOM   2563  N  N     . VAL   A 1 325 ? 122.018 113.286 112.910 1.00 66.88  ?  325  VAL   A N     1 
ATOM   2564  C  CA    . VAL   A 1 325 ? 121.139 114.220 113.605 1.00 67.25  ?  325  VAL   A CA    1 
ATOM   2565  C  C     . VAL   A 1 325 ? 121.827 114.735 114.863 1.00 70.57  ?  325  VAL   A C     1 
ATOM   2566  O  O     . VAL   A 1 325 ? 122.883 114.231 115.257 1.00 77.95  ?  325  VAL   A O     1 
ATOM   2567  C  CB    . VAL   A 1 325 ? 119.788 113.567 113.944 1.00 67.22  ?  325  VAL   A CB    1 
ATOM   2568  C  CG1   . VAL   A 1 325 ? 119.152 112.992 112.691 1.00 68.12  ?  325  VAL   A CG1   1 
ATOM   2569  C  CG2   . VAL   A 1 325 ? 119.967 112.490 115.000 1.00 67.59  ?  325  VAL   A CG2   1 
ATOM   2570  N  N     . GLU   A 1 326 ? 121.238 115.755 115.491 1.00 84.05  ?  326  GLU   A N     1 
ATOM   2571  C  CA    . GLU   A 1 326 ? 121.812 116.311 116.713 1.00 85.38  ?  326  GLU   A CA    1 
ATOM   2572  C  C     . GLU   A 1 326 ? 121.874 115.284 117.837 1.00 82.51  ?  326  GLU   A C     1 
ATOM   2573  O  O     . GLU   A 1 326 ? 122.749 115.370 118.706 1.00 81.99  ?  326  GLU   A O     1 
ATOM   2574  C  CB    . GLU   A 1 326 ? 121.004 117.530 117.159 1.00 86.89  ?  326  GLU   A CB    1 
ATOM   2575  C  CG    . GLU   A 1 326 ? 121.780 118.523 118.011 1.00 89.59  ?  326  GLU   A CG    1 
ATOM   2576  C  CD    . GLU   A 1 326 ? 122.800 119.318 117.215 1.00 96.85  ?  326  GLU   A CD    1 
ATOM   2577  O  OE1   . GLU   A 1 326 ? 122.807 119.215 115.970 1.00 95.09  ?  326  GLU   A OE1   1 
ATOM   2578  O  OE2   . GLU   A 1 326 ? 123.599 120.048 117.838 1.00 97.28  ?  326  GLU   A OE2   1 
ATOM   2579  N  N     . GLY   A 1 327 ? 120.966 114.307 117.838 1.00 75.99  ?  327  GLY   A N     1 
ATOM   2580  C  CA    . GLY   A 1 327 ? 120.898 113.353 118.933 1.00 74.55  ?  327  GLY   A CA    1 
ATOM   2581  C  C     . GLY   A 1 327 ? 122.053 112.377 118.989 1.00 77.05  ?  327  GLY   A C     1 
ATOM   2582  O  O     . GLY   A 1 327 ? 122.308 111.801 120.050 1.00 82.42  ?  327  GLY   A O     1 
ATOM   2583  N  N     . ASN   A 1 328 ? 122.811 112.264 117.901 1.00 62.51  ?  328  ASN   A N     1 
ATOM   2584  C  CA    . ASN   A 1 328 ? 123.846 111.265 117.718 1.00 59.49  ?  328  ASN   A CA    1 
ATOM   2585  C  C     . ASN   A 1 328 ? 125.096 111.917 117.208 1.00 62.80  ?  328  ASN   A C     1 
ATOM   2586  O  O     . ASN   A 1 328 ? 125.965 111.239 116.725 1.00 68.20  ?  328  ASN   A O     1 
ATOM   2587  C  CB    . ASN   A 1 328 ? 123.391 110.123 116.788 1.00 59.26  ?  328  ASN   A CB    1 
ATOM   2588  C  CG    . ASN   A 1 328 ? 123.139 110.526 115.341 1.00 63.93  ?  328  ASN   A CG    1 
ATOM   2589  O  OD1   . ASN   A 1 328 ? 123.063 111.681 115.011 1.00 72.54  ?  328  ASN   A OD1   1 
ATOM   2590  N  ND2   . ASN   A 1 328 ? 123.004 109.535 114.477 1.00 57.93  ?  328  ASN   A ND2   1 
ATOM   2591  N  N     . ARG   A 1 329 ? 125.244 113.202 117.438 1.00 57.78  ?  329  ARG   A N     1 
ATOM   2592  C  CA    . ARG   A 1 329 ? 126.409 113.924 116.972 1.00 52.17  ?  329  ARG   A CA    1 
ATOM   2593  C  C     . ARG   A 1 329 ? 126.900 114.852 118.070 1.00 59.95  ?  329  ARG   A C     1 
ATOM   2594  O  O     . ARG   A 1 329 ? 126.104 115.563 118.690 1.00 72.92  ?  329  ARG   A O     1 
ATOM   2595  C  CB    . ARG   A 1 329 ? 126.086 114.723 115.706 1.00 54.95  ?  329  ARG   A CB    1 
ATOM   2596  C  CG    . ARG   A 1 329 ? 125.962 113.876 114.453 1.00 52.89  ?  329  ARG   A CG    1 
ATOM   2597  C  CD    . ARG   A 1 329 ? 127.256 113.149 114.159 1.00 52.18  ?  329  ARG   A CD    1 
ATOM   2598  N  NE    . ARG   A 1 329 ? 127.177 112.341 112.948 1.00 50.47  ?  329  ARG   A NE    1 
ATOM   2599  C  CZ    . ARG   A 1 329 ? 126.698 111.106 112.900 1.00 54.66  ?  329  ARG   A CZ    1 
ATOM   2600  N  NH1   . ARG   A 1 329 ? 126.222 110.507 113.978 1.00 60.78  ?  329  ARG   A NH1   1 
ATOM   2601  N  NH2   . ARG   A 1 329 ? 126.693 110.457 111.740 1.00 53.02  ?  329  ARG   A NH2   1 
ATOM   2602  N  N     . VAL   A 1 330 ? 128.208 114.833 118.310 1.00 53.52  ?  330  VAL   A N     1 
ATOM   2603  C  CA    . VAL   A 1 330 ? 128.864 115.756 119.236 1.00 49.86  ?  330  VAL   A CA    1 
ATOM   2604  C  C     . VAL   A 1 330 ? 129.979 116.419 118.431 1.00 54.68  ?  330  VAL   A C     1 
ATOM   2605  O  O     . VAL   A 1 330 ? 131.106 115.918 118.370 1.00 63.36  ?  330  VAL   A O     1 
ATOM   2606  C  CB    . VAL   A 1 330 ? 129.413 115.054 120.481 1.00 47.48  ?  330  VAL   A CB    1 
ATOM   2607  C  CG1   . VAL   A 1 330 ? 129.902 116.068 121.500 1.00 59.50  ?  330  VAL   A CG1   1 
ATOM   2608  C  CG2   . VAL   A 1 330 ? 128.362 114.135 121.089 1.00 53.81  ?  330  VAL   A CG2   1 
ATOM   2609  N  N     . ARG   A 1 331 ? 129.672 117.558 117.813 1.00 63.91  ?  331  ARG   A N     1 
ATOM   2610  C  CA    . ARG   A 1 331 ? 130.514 118.129 116.772 1.00 67.89  ?  331  ARG   A CA    1 
ATOM   2611  C  C     . ARG   A 1 331 ? 131.489 119.189 117.267 1.00 70.30  ?  331  ARG   A C     1 
ATOM   2612  O  O     . ARG   A 1 331 ? 132.411 119.546 116.527 1.00 74.21  ?  331  ARG   A O     1 
ATOM   2613  C  CB    . ARG   A 1 331 ? 129.641 118.736 115.667 1.00 71.36  ?  331  ARG   A CB    1 
ATOM   2614  C  CG    . ARG   A 1 331 ? 128.968 117.711 114.776 1.00 71.73  ?  331  ARG   A CG    1 
ATOM   2615  C  CD    . ARG   A 1 331 ? 128.020 118.365 113.809 1.00 72.53  ?  331  ARG   A CD    1 
ATOM   2616  N  NE    . ARG   A 1 331 ? 126.698 118.570 114.336 1.00 80.29  ?  331  ARG   A NE    1 
ATOM   2617  C  CZ    . ARG   A 1 331 ? 125.635 117.872 113.970 1.00 85.78  ?  331  ARG   A CZ    1 
ATOM   2618  N  NH1   . ARG   A 1 331 ? 125.706 116.937 113.037 1.00 81.85  ?  331  ARG   A NH1   1 
ATOM   2619  N  NH2   . ARG   A 1 331 ? 124.468 118.119 114.558 1.00 77.46  ?  331  ARG   A NH2   1 
ATOM   2620  N  N     . HIS   A 1 332 ? 131.321 119.699 118.484 1.00 71.22  ?  332  HIS   A N     1 
ATOM   2621  C  CA    . HIS   A 1 332 ? 132.138 120.800 118.972 1.00 71.14  ?  332  HIS   A CA    1 
ATOM   2622  C  C     . HIS   A 1 332 ? 133.290 120.337 119.853 1.00 72.66  ?  332  HIS   A C     1 
ATOM   2623  O  O     . HIS   A 1 332 ? 133.938 121.167 120.498 1.00 78.08  ?  332  HIS   A O     1 
ATOM   2624  C  CB    . HIS   A 1 332 ? 131.264 121.807 119.719 1.00 72.36  ?  332  HIS   A CB    1 
ATOM   2625  C  CG    . HIS   A 1 332 ? 130.147 122.356 118.889 1.00 80.80  ?  332  HIS   A CG    1 
ATOM   2626  N  ND1   . HIS   A 1 332 ? 128.820 122.151 119.196 1.00 83.63  ?  332  HIS   A ND1   1 
ATOM   2627  C  CD2   . HIS   A 1 332 ? 130.161 123.088 117.750 1.00 79.31  ?  332  HIS   A CD2   1 
ATOM   2628  C  CE1   . HIS   A 1 332 ? 128.064 122.742 118.288 1.00 80.64  ?  332  HIS   A CE1   1 
ATOM   2629  N  NE2   . HIS   A 1 332 ? 128.853 123.317 117.399 1.00 81.37  ?  332  HIS   A NE2   1 
ATOM   2630  N  N     . MET   A 1 333 ? 133.561 119.038 119.891 1.00 67.35  ?  333  MET   A N     1 
ATOM   2631  C  CA    . MET   A 1 333 ? 134.693 118.486 120.617 1.00 63.00  ?  333  MET   A CA    1 
ATOM   2632  C  C     . MET   A 1 333 ? 135.537 117.649 119.669 1.00 68.47  ?  333  MET   A C     1 
ATOM   2633  O  O     . MET   A 1 333 ? 135.003 116.923 118.826 1.00 77.88  ?  333  MET   A O     1 
ATOM   2634  C  CB    . MET   A 1 333 ? 134.231 117.636 121.804 1.00 61.37  ?  333  MET   A CB    1 
ATOM   2635  C  CG    . MET   A 1 333 ? 134.041 118.424 123.088 1.00 67.87  ?  333  MET   A CG    1 
ATOM   2636  S  SD    . MET   A 1 333 ? 134.046 117.379 124.554 1.00 89.54  ?  333  MET   A SD    1 
ATOM   2637  C  CE    . MET   A 1 333 ? 132.839 116.144 124.089 1.00 75.76  ?  333  MET   A CE    1 
ATOM   2638  N  N     . ASP   A 1 334 ? 136.854 117.766 119.797 1.00 60.47  ?  334  ASP   A N     1 
ATOM   2639  C  CA    . ASP   A 1 334 ? 137.759 116.955 119.001 1.00 48.58  ?  334  ASP   A CA    1 
ATOM   2640  C  C     . ASP   A 1 334 ? 137.934 115.580 119.638 1.00 59.93  ?  334  ASP   A C     1 
ATOM   2641  O  O     . ASP   A 1 334 ? 137.646 115.373 120.819 1.00 72.01  ?  334  ASP   A O     1 
ATOM   2642  C  CB    . ASP   A 1 334 ? 139.109 117.650 118.851 1.00 55.18  ?  334  ASP   A CB    1 
ATOM   2643  C  CG    . ASP   A 1 334 ? 139.002 118.977 118.129 1.00 72.20  ?  334  ASP   A CG    1 
ATOM   2644  O  OD1   . ASP   A 1 334 ? 138.025 119.169 117.378 1.00 73.34  ?  334  ASP   A OD1   1 
ATOM   2645  O  OD2   . ASP   A 1 334 ? 139.895 119.829 118.311 1.00 77.16  ?  334  ASP   A OD2   1 
ATOM   2646  N  N     . TYR   A 1 335 ? 138.411 114.631 118.837 1.00 52.96  ?  335  TYR   A N     1 
ATOM   2647  C  CA    . TYR   A 1 335 ? 138.516 113.247 119.271 1.00 48.11  ?  335  TYR   A CA    1 
ATOM   2648  C  C     . TYR   A 1 335 ? 139.883 112.681 118.930 1.00 52.84  ?  335  TYR   A C     1 
ATOM   2649  O  O     . TYR   A 1 335 ? 140.461 113.010 117.891 1.00 63.01  ?  335  TYR   A O     1 
ATOM   2650  C  CB    . TYR   A 1 335 ? 137.423 112.389 118.638 1.00 51.31  ?  335  TYR   A CB    1 
ATOM   2651  C  CG    . TYR   A 1 335 ? 136.046 112.801 119.078 1.00 59.17  ?  335  TYR   A CG    1 
ATOM   2652  C  CD1   . TYR   A 1 335 ? 135.543 112.396 120.303 1.00 58.05  ?  335  TYR   A CD1   1 
ATOM   2653  C  CD2   . TYR   A 1 335 ? 135.257 113.616 118.281 1.00 53.41  ?  335  TYR   A CD2   1 
ATOM   2654  C  CE1   . TYR   A 1 335 ? 134.291 112.779 120.717 1.00 58.83  ?  335  TYR   A CE1   1 
ATOM   2655  C  CE2   . TYR   A 1 335 ? 134.002 114.002 118.688 1.00 53.14  ?  335  TYR   A CE2   1 
ATOM   2656  C  CZ    . TYR   A 1 335 ? 133.526 113.582 119.906 1.00 60.54  ?  335  TYR   A CZ    1 
ATOM   2657  O  OH    . TYR   A 1 335 ? 132.277 113.962 120.319 1.00 68.31  ?  335  TYR   A OH    1 
ATOM   2658  N  N     . GLY   A 1 336 ? 140.390 111.827 119.814 1.00 53.05  ?  336  GLY   A N     1 
ATOM   2659  C  CA    . GLY   A 1 336 ? 141.645 111.141 119.591 1.00 46.03  ?  336  GLY   A CA    1 
ATOM   2660  C  C     . GLY   A 1 336 ? 141.504 109.640 119.727 1.00 51.91  ?  336  GLY   A C     1 
ATOM   2661  O  O     . GLY   A 1 336 ? 141.171 109.135 120.803 1.00 63.38  ?  336  GLY   A O     1 
ATOM   2662  N  N     . VAL   A 1 337 ? 141.746 108.917 118.640 1.00 40.73  ?  337  VAL   A N     1 
ATOM   2663  C  CA    . VAL   A 1 337 ? 141.667 107.462 118.633 1.00 40.83  ?  337  VAL   A CA    1 
ATOM   2664  C  C     . VAL   A 1 337 ? 143.006 106.900 119.086 1.00 46.75  ?  337  VAL   A C     1 
ATOM   2665  O  O     . VAL   A 1 337 ? 144.063 107.306 118.588 1.00 59.75  ?  337  VAL   A O     1 
ATOM   2666  C  CB    . VAL   A 1 337 ? 141.291 106.939 117.238 1.00 41.85  ?  337  VAL   A CB    1 
ATOM   2667  C  CG1   . VAL   A 1 337 ? 140.856 105.487 117.317 1.00 48.01  ?  337  VAL   A CG1   1 
ATOM   2668  C  CG2   . VAL   A 1 337 ? 140.195 107.799 116.633 1.00 46.39  ?  337  VAL   A CG2   1 
ATOM   2669  N  N     . GLN   A 1 338 ? 142.963 105.969 120.032 1.00 45.33  ?  338  GLN   A N     1 
ATOM   2670  C  CA    . GLN   A 1 338 ? 144.162 105.376 120.605 1.00 39.02  ?  338  GLN   A CA    1 
ATOM   2671  C  C     . GLN   A 1 338 ? 144.393 104.006 119.978 1.00 47.59  ?  338  GLN   A C     1 
ATOM   2672  O  O     . GLN   A 1 338 ? 143.520 103.134 120.036 1.00 59.92  ?  338  GLN   A O     1 
ATOM   2673  C  CB    . GLN   A 1 338 ? 144.039 105.278 122.124 1.00 45.42  ?  338  GLN   A CB    1 
ATOM   2674  C  CG    . GLN   A 1 338 ? 144.000 106.638 122.804 1.00 44.83  ?  338  GLN   A CG    1 
ATOM   2675  C  CD    . GLN   A 1 338 ? 143.590 106.562 124.256 1.00 51.11  ?  338  GLN   A CD    1 
ATOM   2676  O  OE1   . GLN   A 1 338 ? 142.684 105.816 124.620 1.00 58.36  ?  338  GLN   A OE1   1 
ATOM   2677  N  NE2   . GLN   A 1 338 ? 144.251 107.346 125.096 1.00 50.90  ?  338  GLN   A NE2   1 
ATOM   2678  N  N     . ILE   A 1 339 ? 145.569 103.827 119.381 1.00 52.42  ?  339  ILE   A N     1 
ATOM   2679  C  CA    . ILE   A 1 339 ? 145.917 102.628 118.631 1.00 48.37  ?  339  ILE   A CA    1 
ATOM   2680  C  C     . ILE   A 1 339 ? 147.237 102.090 119.165 1.00 58.22  ?  339  ILE   A C     1 
ATOM   2681  O  O     . ILE   A 1 339 ? 148.051 102.835 119.720 1.00 70.72  ?  339  ILE   A O     1 
ATOM   2682  C  CB    . ILE   A 1 339 ? 146.016 102.921 117.114 1.00 49.12  ?  339  ILE   A CB    1 
ATOM   2683  C  CG1   . ILE   A 1 339 ? 144.869 103.825 116.662 1.00 51.08  ?  339  ILE   A CG1   1 
ATOM   2684  C  CG2   . ILE   A 1 339 ? 146.006 101.644 116.306 1.00 49.91  ?  339  ILE   A CG2   1 
ATOM   2685  C  CD1   . ILE   A 1 339 ? 144.991 104.294 115.233 1.00 56.06  ?  339  ILE   A CD1   1 
ATOM   2686  N  N     . ASN   A 1 340 ? 147.448 100.786 119.001 1.00 61.69  ?  340  ASN   A N     1 
ATOM   2687  C  CA    . ASN   A 1 340 ? 148.693 100.151 119.413 1.00 57.86  ?  340  ASN   A CA    1 
ATOM   2688  C  C     . ASN   A 1 340 ? 149.128 99.183  118.317 1.00 60.78  ?  340  ASN   A C     1 
ATOM   2689  O  O     . ASN   A 1 340 ? 148.593 99.189  117.204 1.00 67.31  ?  340  ASN   A O     1 
ATOM   2690  C  CB    . ASN   A 1 340 ? 148.539 99.470  120.780 1.00 59.04  ?  340  ASN   A CB    1 
ATOM   2691  C  CG    . ASN   A 1 340 ? 147.674 98.228  120.726 1.00 59.66  ?  340  ASN   A CG    1 
ATOM   2692  O  OD1   . ASN   A 1 340 ? 146.840 98.072  119.837 1.00 61.85  ?  340  ASN   A OD1   1 
ATOM   2693  N  ND2   . ASN   A 1 340 ? 147.867 97.338  121.688 1.00 59.64  ?  340  ASN   A ND2   1 
ATOM   2694  N  N     . LYS   A 1 341 ? 150.115 98.344  118.643 1.00 70.48  ?  341  LYS   A N     1 
ATOM   2695  C  CA    . LYS   A 1 341 ? 150.740 97.488  117.638 1.00 67.56  ?  341  LYS   A CA    1 
ATOM   2696  C  C     . LYS   A 1 341 ? 149.760 96.469  117.069 1.00 68.94  ?  341  LYS   A C     1 
ATOM   2697  O  O     . LYS   A 1 341 ? 149.790 96.175  115.867 1.00 76.68  ?  341  LYS   A O     1 
ATOM   2698  C  CB    . LYS   A 1 341 ? 151.953 96.781  118.243 1.00 75.25  ?  341  LYS   A CB    1 
ATOM   2699  C  CG    . LYS   A 1 341 ? 152.454 95.593  117.440 1.00 73.19  ?  341  LYS   A CG    1 
ATOM   2700  C  CD    . LYS   A 1 341 ? 153.403 96.036  116.342 1.00 73.84  ?  341  LYS   A CD    1 
ATOM   2701  C  CE    . LYS   A 1 341 ? 154.847 95.987  116.806 1.00 76.23  ?  341  LYS   A CE    1 
ATOM   2702  N  NZ    . LYS   A 1 341 ? 155.781 95.701  115.683 1.00 77.87  ?  341  LYS   A NZ    1 
ATOM   2703  N  N     . LEU   A 1 342 ? 148.899 95.901  117.917 1.00 70.53  ?  342  LEU   A N     1 
ATOM   2704  C  CA    . LEU   A 1 342 ? 148.026 94.820  117.468 1.00 69.81  ?  342  LEU   A CA    1 
ATOM   2705  C  C     . LEU   A 1 342 ? 147.064 95.299  116.391 1.00 72.14  ?  342  LEU   A C     1 
ATOM   2706  O  O     . LEU   A 1 342 ? 146.828 94.596  115.402 1.00 80.83  ?  342  LEU   A O     1 
ATOM   2707  C  CB    . LEU   A 1 342 ? 147.260 94.231  118.654 1.00 69.65  ?  342  LEU   A CB    1 
ATOM   2708  C  CG    . LEU   A 1 342 ? 146.564 92.885  118.427 1.00 72.07  ?  342  LEU   A CG    1 
ATOM   2709  C  CD1   . LEU   A 1 342 ? 146.595 92.055  119.695 1.00 74.20  ?  342  LEU   A CD1   1 
ATOM   2710  C  CD2   . LEU   A 1 342 ? 145.130 93.052  117.943 1.00 75.89  ?  342  LEU   A CD2   1 
ATOM   2711  N  N     . MET   A 1 343 ? 146.500 96.496  116.564 1.00 66.01  ?  343  MET   A N     1 
ATOM   2712  C  CA    . MET   A 1 343 ? 145.577 97.028  115.568 1.00 67.08  ?  343  MET   A CA    1 
ATOM   2713  C  C     . MET   A 1 343 ? 146.275 97.236  114.233 1.00 67.61  ?  343  MET   A C     1 
ATOM   2714  O  O     . MET   A 1 343 ? 145.712 96.930  113.174 1.00 75.91  ?  343  MET   A O     1 
ATOM   2715  C  CB    . MET   A 1 343 ? 144.969 98.342  116.052 1.00 73.36  ?  343  MET   A CB    1 
ATOM   2716  C  CG    . MET   A 1 343 ? 144.550 98.352  117.505 1.00 73.81  ?  343  MET   A CG    1 
ATOM   2717  S  SD    . MET   A 1 343 ? 143.193 97.223  117.856 1.00 88.92  ?  343  MET   A SD    1 
ATOM   2718  C  CE    . MET   A 1 343 ? 144.008 96.037  118.913 1.00 78.04  ?  343  MET   A CE    1 
ATOM   2719  N  N     . TYR   A 1 344 ? 147.507 97.753  114.270 1.00 63.94  ?  344  TYR   A N     1 
ATOM   2720  C  CA    . TYR   A 1 344 ? 148.273 97.983  113.049 1.00 60.94  ?  344  TYR   A CA    1 
ATOM   2721  C  C     . TYR   A 1 344 ? 148.614 96.675  112.348 1.00 66.21  ?  344  TYR   A C     1 
ATOM   2722  O  O     . TYR   A 1 344 ? 148.506 96.578  111.121 1.00 73.21  ?  344  TYR   A O     1 
ATOM   2723  C  CB    . TYR   A 1 344 ? 149.548 98.765  113.370 1.00 61.06  ?  344  TYR   A CB    1 
ATOM   2724  C  CG    . TYR   A 1 344 ? 149.327 100.248 113.551 1.00 64.28  ?  344  TYR   A CG    1 
ATOM   2725  C  CD1   . TYR   A 1 344 ? 148.853 101.030 112.510 1.00 63.60  ?  344  TYR   A CD1   1 
ATOM   2726  C  CD2   . TYR   A 1 344 ? 149.590 100.865 114.765 1.00 64.56  ?  344  TYR   A CD2   1 
ATOM   2727  C  CE1   . TYR   A 1 344 ? 148.648 102.385 112.672 1.00 68.01  ?  344  TYR   A CE1   1 
ATOM   2728  C  CE2   . TYR   A 1 344 ? 149.385 102.218 114.937 1.00 60.01  ?  344  TYR   A CE2   1 
ATOM   2729  C  CZ    . TYR   A 1 344 ? 148.916 102.974 113.888 1.00 65.04  ?  344  TYR   A CZ    1 
ATOM   2730  O  OH    . TYR   A 1 344 ? 148.713 104.324 114.056 1.00 66.48  ?  344  TYR   A OH    1 
ATOM   2731  N  N     . THR   A 1 345 ? 149.028 95.655  113.103 1.00 73.57  ?  345  THR   A N     1 
ATOM   2732  C  CA    . THR   A 1 345 ? 149.387 94.394  112.461 1.00 70.42  ?  345  THR   A CA    1 
ATOM   2733  C  C     . THR   A 1 345 ? 148.158 93.661  111.937 1.00 71.52  ?  345  THR   A C     1 
ATOM   2734  O  O     . THR   A 1 345 ? 148.247 92.959  110.922 1.00 79.62  ?  345  THR   A O     1 
ATOM   2735  C  CB    . THR   A 1 345 ? 150.194 93.507  113.417 1.00 69.69  ?  345  THR   A CB    1 
ATOM   2736  O  OG1   . THR   A 1 345 ? 150.722 92.387  112.696 1.00 78.86  ?  345  THR   A OG1   1 
ATOM   2737  C  CG2   . THR   A 1 345 ? 149.342 92.996  114.561 1.00 69.63  ?  345  THR   A CG2   1 
ATOM   2738  N  N     . ARG   A 1 346 ? 147.004 93.818  112.593 1.00 63.20  ?  346  ARG   A N     1 
ATOM   2739  C  CA    . ARG   A 1 346 ? 145.774 93.251  112.049 1.00 63.12  ?  346  ARG   A CA    1 
ATOM   2740  C  C     . ARG   A 1 346 ? 145.367 93.961  110.767 1.00 67.45  ?  346  ARG   A C     1 
ATOM   2741  O  O     . ARG   A 1 346 ? 144.858 93.327  109.835 1.00 75.29  ?  346  ARG   A O     1 
ATOM   2742  C  CB    . ARG   A 1 346 ? 144.654 93.323  113.084 1.00 60.61  ?  346  ARG   A CB    1 
ATOM   2743  C  CG    . ARG   A 1 346 ? 144.892 92.452  114.300 1.00 65.03  ?  346  ARG   A CG    1 
ATOM   2744  C  CD    . ARG   A 1 346 ? 143.896 91.316  114.383 1.00 64.35  ?  346  ARG   A CD    1 
ATOM   2745  N  NE    . ARG   A 1 346 ? 144.180 90.445  115.516 1.00 63.16  ?  346  ARG   A NE    1 
ATOM   2746  C  CZ    . ARG   A 1 346 ? 143.260 89.965  116.340 1.00 70.47  ?  346  ARG   A CZ    1 
ATOM   2747  N  NH1   . ARG   A 1 346 ? 141.978 90.249  116.183 1.00 72.48  ?  346  ARG   A NH1   1 
ATOM   2748  N  NH2   . ARG   A 1 346 ? 143.636 89.181  117.346 1.00 71.07  ?  346  ARG   A NH2   1 
ATOM   2749  N  N     . LEU   A 1 347 ? 145.574 95.280  110.703 1.00 66.38  ?  347  LEU   A N     1 
ATOM   2750  C  CA    . LEU   A 1 347 ? 145.333 95.999  109.456 1.00 68.08  ?  347  LEU   A CA    1 
ATOM   2751  C  C     . LEU   A 1 347 ? 146.279 95.527  108.357 1.00 65.67  ?  347  LEU   A C     1 
ATOM   2752  O  O     . LEU   A 1 347 ? 145.870 95.363  107.201 1.00 68.11  ?  347  LEU   A O     1 
ATOM   2753  C  CB    . LEU   A 1 347 ? 145.477 97.503  109.684 1.00 69.37  ?  347  LEU   A CB    1 
ATOM   2754  C  CG    . LEU   A 1 347 ? 145.789 98.368  108.462 1.00 64.36  ?  347  LEU   A CG    1 
ATOM   2755  C  CD1   . LEU   A 1 347 ? 144.549 98.550  107.604 1.00 64.18  ?  347  LEU   A CD1   1 
ATOM   2756  C  CD2   . LEU   A 1 347 ? 146.351 99.713  108.886 1.00 61.04  ?  347  LEU   A CD2   1 
ATOM   2757  N  N     . LEU   A 1 348 ? 147.550 95.308  108.699 1.00 80.92  ?  348  LEU   A N     1 
ATOM   2758  C  CA    . LEU   A 1 348 ? 148.522 94.850  107.710 1.00 81.75  ?  348  LEU   A CA    1 
ATOM   2759  C  C     . LEU   A 1 348 ? 148.174 93.463  107.185 1.00 82.21  ?  348  LEU   A C     1 
ATOM   2760  O  O     . LEU   A 1 348 ? 148.252 93.210  105.977 1.00 86.90  ?  348  LEU   A O     1 
ATOM   2761  C  CB    . LEU   A 1 348 ? 149.926 94.851  108.313 1.00 80.80  ?  348  LEU   A CB    1 
ATOM   2762  C  CG    . LEU   A 1 348 ? 150.521 96.213  108.664 1.00 85.47  ?  348  LEU   A CG    1 
ATOM   2763  C  CD1   . LEU   A 1 348 ? 151.918 96.047  109.226 1.00 87.62  ?  348  LEU   A CD1   1 
ATOM   2764  C  CD2   . LEU   A 1 348 ? 150.534 97.116  107.447 1.00 85.03  ?  348  LEU   A CD2   1 
ATOM   2765  N  N     . LYS   A 1 349 ? 147.788 92.549  108.076 1.00 81.21  ?  349  LYS   A N     1 
ATOM   2766  C  CA    . LYS   A 1 349 ? 147.474 91.185  107.670 1.00 79.23  ?  349  LYS   A CA    1 
ATOM   2767  C  C     . LYS   A 1 349 ? 146.071 91.040  107.098 1.00 81.79  ?  349  LYS   A C     1 
ATOM   2768  O  O     . LYS   A 1 349 ? 145.735 89.961  106.597 1.00 85.21  ?  349  LYS   A O     1 
ATOM   2769  C  CB    . LYS   A 1 349 ? 147.642 90.233  108.856 1.00 78.85  ?  349  LYS   A CB    1 
ATOM   2770  C  CG    . LYS   A 1 349 ? 149.084 89.999  109.267 1.00 79.65  ?  349  LYS   A CG    1 
ATOM   2771  C  CD    . LYS   A 1 349 ? 149.162 89.254  110.589 1.00 82.76  ?  349  LYS   A CD    1 
ATOM   2772  C  CE    . LYS   A 1 349 ? 150.243 88.187  110.560 1.00 84.18  ?  349  LYS   A CE    1 
ATOM   2773  N  NZ    . LYS   A 1 349 ? 151.586 88.752  110.867 1.00 87.33  ?  349  LYS   A NZ    1 
ATOM   2774  N  N     . GLY   A 1 350 ? 145.251 92.086  107.157 1.00 80.96  ?  350  GLY   A N     1 
ATOM   2775  C  CA    . GLY   A 1 350 ? 143.901 92.000  106.639 1.00 80.30  ?  350  GLY   A CA    1 
ATOM   2776  C  C     . GLY   A 1 350 ? 142.947 91.190  107.484 1.00 81.96  ?  350  GLY   A C     1 
ATOM   2777  O  O     . GLY   A 1 350 ? 141.921 90.732  106.976 1.00 83.95  ?  350  GLY   A O     1 
ATOM   2778  N  N     . GLU   A 1 351 ? 143.252 91.000  108.765 1.00 83.41  ?  351  GLU   A N     1 
ATOM   2779  C  CA    . GLU   A 1 351 ? 142.404 90.216  109.651 1.00 84.28  ?  351  GLU   A CA    1 
ATOM   2780  C  C     . GLU   A 1 351 ? 141.271 91.090  110.187 1.00 86.32  ?  351  GLU   A C     1 
ATOM   2781  O  O     . GLU   A 1 351 ? 141.035 92.206  109.718 1.00 85.20  ?  351  GLU   A O     1 
ATOM   2782  C  CB    . GLU   A 1 351 ? 143.236 89.605  110.774 1.00 84.25  ?  351  GLU   A CB    1 
ATOM   2783  C  CG    . GLU   A 1 351 ? 144.443 88.822  110.293 1.00 84.07  ?  351  GLU   A CG    1 
ATOM   2784  C  CD    . GLU   A 1 351 ? 144.830 87.710  111.247 1.00 91.34  ?  351  GLU   A CD    1 
ATOM   2785  O  OE1   . GLU   A 1 351 ? 145.131 86.595  110.772 1.00 92.63  ?  351  GLU   A OE1   1 
ATOM   2786  O  OE2   . GLU   A 1 351 ? 144.835 87.952  112.472 1.00 91.01  ?  351  GLU   A OE2   1 
ATOM   2787  N  N     . ASP   A 1 352 ? 140.550 90.582  111.183 1.00 92.32  ?  352  ASP   A N     1 
ATOM   2788  C  CA    . ASP   A 1 352 ? 139.415 91.277  111.774 1.00 88.73  ?  352  ASP   A CA    1 
ATOM   2789  C  C     . ASP   A 1 352 ? 139.783 91.790  113.159 1.00 92.60  ?  352  ASP   A C     1 
ATOM   2790  O  O     . ASP   A 1 352 ? 140.382 91.063  113.958 1.00 96.75  ?  352  ASP   A O     1 
ATOM   2791  C  CB    . ASP   A 1 352 ? 138.195 90.358  111.864 1.00 92.32  ?  352  ASP   A CB    1 
ATOM   2792  C  CG    . ASP   A 1 352 ? 137.466 90.228  110.544 1.00 100.03 ?  352  ASP   A CG    1 
ATOM   2793  O  OD1   . ASP   A 1 352 ? 137.973 90.751  109.530 1.00 101.85 ?  352  ASP   A OD1   1 
ATOM   2794  O  OD2   . ASP   A 1 352 ? 136.383 89.606  110.519 1.00 99.12  ?  352  ASP   A OD2   1 
ATOM   2795  N  N     . ILE   A 1 353 ? 139.425 93.039  113.433 1.00 77.18  ?  353  ILE   A N     1 
ATOM   2796  C  CA    . ILE   A 1 353 ? 139.583 93.636  114.752 1.00 73.29  ?  353  ILE   A CA    1 
ATOM   2797  C  C     . ILE   A 1 353 ? 138.322 93.357  115.558 1.00 72.87  ?  353  ILE   A C     1 
ATOM   2798  O  O     . ILE   A 1 353 ? 137.201 93.566  115.075 1.00 79.32  ?  353  ILE   A O     1 
ATOM   2799  C  CB    . ILE   A 1 353 ? 139.846 95.147  114.643 1.00 69.75  ?  353  ILE   A CB    1 
ATOM   2800  C  CG1   . ILE   A 1 353 ? 141.269 95.410  114.153 1.00 72.58  ?  353  ILE   A CG1   1 
ATOM   2801  C  CG2   . ILE   A 1 353 ? 139.607 95.835  115.977 1.00 71.61  ?  353  ILE   A CG2   1 
ATOM   2802  C  CD1   . ILE   A 1 353 ? 141.548 96.865  113.854 1.00 75.26  ?  353  ILE   A CD1   1 
ATOM   2803  N  N     . THR   A 1 354 ? 138.501 92.873  116.781 1.00 69.43  ?  354  THR   A N     1 
ATOM   2804  C  CA    . THR   A 1 354 ? 137.394 92.608  117.686 1.00 64.67  ?  354  THR   A CA    1 
ATOM   2805  C  C     . THR   A 1 354 ? 137.256 93.764  118.666 1.00 65.93  ?  354  THR   A C     1 
ATOM   2806  O  O     . THR   A 1 354 ? 138.249 94.217  119.245 1.00 75.34  ?  354  THR   A O     1 
ATOM   2807  C  CB    . THR   A 1 354 ? 137.603 91.297  118.442 1.00 65.98  ?  354  THR   A CB    1 
ATOM   2808  O  OG1   . THR   A 1 354 ? 138.045 90.285  117.529 1.00 76.30  ?  354  THR   A OG1   1 
ATOM   2809  C  CG2   . THR   A 1 354 ? 136.308 90.852  119.085 1.00 68.40  ?  354  THR   A CG2   1 
ATOM   2810  N  N     . LEU   A 1 355 ? 136.029 94.241  118.839 1.00 53.39  ?  355  LEU   A N     1 
ATOM   2811  C  CA    . LEU   A 1 355 ? 135.715 95.344  119.732 1.00 55.01  ?  355  LEU   A CA    1 
ATOM   2812  C  C     . LEU   A 1 355 ? 134.952 94.811  120.934 1.00 56.48  ?  355  LEU   A C     1 
ATOM   2813  O  O     . LEU   A 1 355 ? 133.992 94.047  120.775 1.00 64.38  ?  355  LEU   A O     1 
ATOM   2814  C  CB    . LEU   A 1 355 ? 134.888 96.413  119.015 1.00 54.55  ?  355  LEU   A CB    1 
ATOM   2815  C  CG    . LEU   A 1 355 ? 135.185 96.647  117.535 1.00 58.39  ?  355  LEU   A CG    1 
ATOM   2816  C  CD1   . LEU   A 1 355 ? 134.021 97.355  116.867 1.00 57.40  ?  355  LEU   A CD1   1 
ATOM   2817  C  CD2   . LEU   A 1 355 ? 136.468 97.442  117.366 1.00 58.70  ?  355  LEU   A CD2   1 
ATOM   2818  N  N     . PHE   A 1 356 ? 135.390 95.211  122.125 1.00 61.08  ?  356  PHE   A N     1 
ATOM   2819  C  CA    . PHE   A 1 356 ? 134.759 94.853  123.383 1.00 60.87  ?  356  PHE   A CA    1 
ATOM   2820  C  C     . PHE   A 1 356 ? 134.377 96.115  124.141 1.00 64.64  ?  356  PHE   A C     1 
ATOM   2821  O  O     . PHE   A 1 356 ? 134.937 97.192  123.921 1.00 72.42  ?  356  PHE   A O     1 
ATOM   2822  C  CB    . PHE   A 1 356 ? 135.684 94.015  124.278 1.00 56.94  ?  356  PHE   A CB    1 
ATOM   2823  C  CG    . PHE   A 1 356 ? 136.412 92.917  123.564 1.00 55.30  ?  356  PHE   A CG    1 
ATOM   2824  C  CD1   . PHE   A 1 356 ? 137.633 93.157  122.959 1.00 58.58  ?  356  PHE   A CD1   1 
ATOM   2825  C  CD2   . PHE   A 1 356 ? 135.894 91.636  123.531 1.00 62.03  ?  356  PHE   A CD2   1 
ATOM   2826  C  CE1   . PHE   A 1 356 ? 138.310 92.145  122.313 1.00 63.83  ?  356  PHE   A CE1   1 
ATOM   2827  C  CE2   . PHE   A 1 356 ? 136.569 90.620  122.887 1.00 67.98  ?  356  PHE   A CE2   1 
ATOM   2828  C  CZ    . PHE   A 1 356 ? 137.780 90.876  122.278 1.00 64.66  ?  356  PHE   A CZ    1 
ATOM   2829  N  N     . SER   A 1 357 ? 133.417 95.972  125.040 1.00 69.16  ?  357  SER   A N     1 
ATOM   2830  C  CA    . SER   A 1 357 ? 133.198 97.000  126.044 1.00 63.52  ?  357  SER   A CA    1 
ATOM   2831  C  C     . SER   A 1 357 ? 134.338 96.946  127.055 1.00 67.50  ?  357  SER   A C     1 
ATOM   2832  O  O     . SER   A 1 357 ? 134.697 95.856  127.513 1.00 76.10  ?  357  SER   A O     1 
ATOM   2833  C  CB    . SER   A 1 357 ? 131.856 96.799  126.742 1.00 64.43  ?  357  SER   A CB    1 
ATOM   2834  O  OG    . SER   A 1 357 ? 131.780 97.565  127.930 1.00 67.07  ?  357  SER   A OG    1 
ATOM   2835  N  N     . PRO   A 1 358 ? 134.938 98.082  127.416 1.00 66.37  ?  358  PRO   A N     1 
ATOM   2836  C  CA    . PRO   A 1 358 ? 136.075 98.043  128.351 1.00 66.26  ?  358  PRO   A CA    1 
ATOM   2837  C  C     . PRO   A 1 358 ? 135.727 97.466  129.711 1.00 68.60  ?  358  PRO   A C     1 
ATOM   2838  O  O     . PRO   A 1 358 ? 136.629 97.000  130.418 1.00 71.77  ?  358  PRO   A O     1 
ATOM   2839  C  CB    . PRO   A 1 358 ? 136.496 99.516  128.457 1.00 63.53  ?  358  PRO   A CB    1 
ATOM   2840  C  CG    . PRO   A 1 358 ? 135.307 100.294 128.000 1.00 66.48  ?  358  PRO   A CG    1 
ATOM   2841  C  CD    . PRO   A 1 358 ? 134.633 99.450  126.969 1.00 66.62  ?  358  PRO   A CD    1 
ATOM   2842  N  N     . SER   A 1 359 ? 134.452 97.479  130.102 1.00 70.18  ?  359  SER   A N     1 
ATOM   2843  C  CA    . SER   A 1 359 ? 134.048 96.904  131.378 1.00 71.11  ?  359  SER   A CA    1 
ATOM   2844  C  C     . SER   A 1 359 ? 133.904 95.389  131.329 1.00 74.38  ?  359  SER   A C     1 
ATOM   2845  O  O     . SER   A 1 359 ? 133.877 94.750  132.386 1.00 80.96  ?  359  SER   A O     1 
ATOM   2846  C  CB    . SER   A 1 359 ? 132.726 97.522  131.835 1.00 76.73  ?  359  SER   A CB    1 
ATOM   2847  O  OG    . SER   A 1 359 ? 131.653 97.084  131.019 1.00 78.05  ?  359  SER   A OG    1 
ATOM   2848  N  N     . ASP   A 1 360 ? 133.811 94.801  130.137 1.00 85.15  ?  360  ASP   A N     1 
ATOM   2849  C  CA    . ASP   A 1 360 ? 133.597 93.367  129.998 1.00 83.93  ?  360  ASP   A CA    1 
ATOM   2850  C  C     . ASP   A 1 360 ? 134.890 92.575  129.872 1.00 87.09  ?  360  ASP   A C     1 
ATOM   2851  O  O     . ASP   A 1 360 ? 134.844 91.340  129.893 1.00 87.97  ?  360  ASP   A O     1 
ATOM   2852  C  CB    . ASP   A 1 360 ? 132.715 93.084  128.778 1.00 85.87  ?  360  ASP   A CB    1 
ATOM   2853  C  CG    . ASP   A 1 360 ? 131.247 92.994  129.130 1.00 96.29  ?  360  ASP   A CG    1 
ATOM   2854  O  OD1   . ASP   A 1 360 ? 130.925 92.958  130.336 1.00 98.14  ?  360  ASP   A OD1   1 
ATOM   2855  O  OD2   . ASP   A 1 360 ? 130.412 92.961  128.202 1.00 98.04  ?  360  ASP   A OD2   1 
ATOM   2856  N  N     . VAL   A 1 361 ? 136.029 93.242  129.751 1.00 80.93  ?  361  VAL   A N     1 
ATOM   2857  C  CA    . VAL   A 1 361 ? 137.313 92.591  129.538 1.00 75.23  ?  361  VAL   A CA    1 
ATOM   2858  C  C     . VAL   A 1 361 ? 138.235 92.950  130.700 1.00 76.98  ?  361  VAL   A C     1 
ATOM   2859  O  O     . VAL   A 1 361 ? 138.868 94.006  130.706 1.00 78.84  ?  361  VAL   A O     1 
ATOM   2860  C  CB    . VAL   A 1 361 ? 137.923 92.988  128.181 1.00 72.87  ?  361  VAL   A CB    1 
ATOM   2861  C  CG1   . VAL   A 1 361 ? 137.177 92.284  127.068 1.00 74.05  ?  361  VAL   A CG1   1 
ATOM   2862  C  CG2   . VAL   A 1 361 ? 137.830 94.488  127.961 1.00 78.66  ?  361  VAL   A CG2   1 
ATOM   2863  N  N     . PRO   A 1 362 ? 138.327 92.090  131.716 1.00 80.16  ?  362  PRO   A N     1 
ATOM   2864  C  CA    . PRO   A 1 362 ? 139.131 92.411  132.906 1.00 77.72  ?  362  PRO   A CA    1 
ATOM   2865  C  C     . PRO   A 1 362 ? 140.610 92.516  132.563 1.00 75.83  ?  362  PRO   A C     1 
ATOM   2866  O  O     . PRO   A 1 362 ? 141.226 91.550  132.109 1.00 75.55  ?  362  PRO   A O     1 
ATOM   2867  C  CB    . PRO   A 1 362 ? 138.852 91.235  133.851 1.00 77.51  ?  362  PRO   A CB    1 
ATOM   2868  C  CG    . PRO   A 1 362 ? 137.581 90.624  133.344 1.00 79.22  ?  362  PRO   A CG    1 
ATOM   2869  C  CD    . PRO   A 1 362 ? 137.606 90.817  131.864 1.00 80.11  ?  362  PRO   A CD    1 
ATOM   2870  N  N     . GLY   A 1 363 ? 141.174 93.704  132.778 1.00 63.80  ?  363  GLY   A N     1 
ATOM   2871  C  CA    . GLY   A 1 363 ? 142.588 93.937  132.592 1.00 61.20  ?  363  GLY   A CA    1 
ATOM   2872  C  C     . GLY   A 1 363 ? 143.006 94.318  131.189 1.00 61.80  ?  363  GLY   A C     1 
ATOM   2873  O  O     . GLY   A 1 363 ? 144.167 94.697  130.991 1.00 68.38  ?  363  GLY   A O     1 
ATOM   2874  N  N     . LEU   A 1 364 ? 142.104 94.235  130.209 1.00 62.39  ?  364  LEU   A N     1 
ATOM   2875  C  CA    . LEU   A 1 364 ? 142.482 94.566  128.839 1.00 56.93  ?  364  LEU   A CA    1 
ATOM   2876  C  C     . LEU   A 1 364 ? 142.755 96.056  128.681 1.00 61.56  ?  364  LEU   A C     1 
ATOM   2877  O  O     . LEU   A 1 364 ? 143.702 96.446  127.989 1.00 70.17  ?  364  LEU   A O     1 
ATOM   2878  C  CB    . LEU   A 1 364 ? 141.395 94.114  127.865 1.00 55.98  ?  364  LEU   A CB    1 
ATOM   2879  C  CG    . LEU   A 1 364 ? 141.774 94.170  126.384 1.00 60.90  ?  364  LEU   A CG    1 
ATOM   2880  C  CD1   . LEU   A 1 364 ? 142.667 92.999  126.018 1.00 64.38  ?  364  LEU   A CD1   1 
ATOM   2881  C  CD2   . LEU   A 1 364 ? 140.535 94.196  125.505 1.00 60.83  ?  364  LEU   A CD2   1 
ATOM   2882  N  N     . TYR   A 1 365 ? 141.936 96.904  129.306 1.00 61.95  ?  365  TYR   A N     1 
ATOM   2883  C  CA    . TYR   A 1 365 ? 142.151 98.344  129.197 1.00 56.75  ?  365  TYR   A CA    1 
ATOM   2884  C  C     . TYR   A 1 365 ? 143.473 98.755  129.832 1.00 62.41  ?  365  TYR   A C     1 
ATOM   2885  O  O     . TYR   A 1 365 ? 144.199 99.592  129.283 1.00 76.06  ?  365  TYR   A O     1 
ATOM   2886  C  CB    . TYR   A 1 365 ? 140.993 99.107  129.838 1.00 62.88  ?  365  TYR   A CB    1 
ATOM   2887  C  CG    . TYR   A 1 365 ? 141.074 100.600 129.618 1.00 62.35  ?  365  TYR   A CG    1 
ATOM   2888  C  CD1   . TYR   A 1 365 ? 140.642 101.169 128.429 1.00 59.47  ?  365  TYR   A CD1   1 
ATOM   2889  C  CD2   . TYR   A 1 365 ? 141.594 101.438 130.593 1.00 61.77  ?  365  TYR   A CD2   1 
ATOM   2890  C  CE1   . TYR   A 1 365 ? 140.720 102.531 128.220 1.00 63.60  ?  365  TYR   A CE1   1 
ATOM   2891  C  CE2   . TYR   A 1 365 ? 141.677 102.802 130.393 1.00 61.06  ?  365  TYR   A CE2   1 
ATOM   2892  C  CZ    . TYR   A 1 365 ? 141.237 103.342 129.205 1.00 66.20  ?  365  TYR   A CZ    1 
ATOM   2893  O  OH    . TYR   A 1 365 ? 141.317 104.699 129.001 1.00 69.43  ?  365  TYR   A OH    1 
ATOM   2894  N  N     . ASP   A 1 366 ? 143.799 98.184  130.993 1.00 71.40  ?  366  ASP   A N     1 
ATOM   2895  C  CA    . ASP   A 1 366 ? 145.072 98.495  131.635 1.00 74.41  ?  366  ASP   A CA    1 
ATOM   2896  C  C     . ASP   A 1 366 ? 146.248 98.009  130.797 1.00 76.16  ?  366  ASP   A C     1 
ATOM   2897  O  O     . ASP   A 1 366 ? 147.254 98.714  130.662 1.00 78.46  ?  366  ASP   A O     1 
ATOM   2898  C  CB    . ASP   A 1 366 ? 145.118 97.881  133.033 1.00 77.90  ?  366  ASP   A CB    1 
ATOM   2899  C  CG    . ASP   A 1 366 ? 144.194 98.583  134.007 1.00 88.54  ?  366  ASP   A CG    1 
ATOM   2900  O  OD1   . ASP   A 1 366 ? 143.737 99.702  133.694 1.00 92.94  ?  366  ASP   A OD1   1 
ATOM   2901  O  OD2   . ASP   A 1 366 ? 143.924 98.016  135.086 1.00 88.64  ?  366  ASP   A OD2   1 
ATOM   2902  N  N     . ALA   A 1 367 ? 146.138 96.809  130.223 1.00 62.46  ?  367  ALA   A N     1 
ATOM   2903  C  CA    . ALA   A 1 367 ? 147.218 96.270  129.406 1.00 60.11  ?  367  ALA   A CA    1 
ATOM   2904  C  C     . ALA   A 1 367 ? 147.354 96.992  128.073 1.00 61.82  ?  367  ALA   A C     1 
ATOM   2905  O  O     . ALA   A 1 367 ? 148.425 96.937  127.461 1.00 69.26  ?  367  ALA   A O     1 
ATOM   2906  C  CB    . ALA   A 1 367 ? 147.001 94.776  129.169 1.00 64.29  ?  367  ALA   A CB    1 
ATOM   2907  N  N     . PHE   A 1 368 ? 146.297 97.666  127.613 1.00 55.54  ?  368  PHE   A N     1 
ATOM   2908  C  CA    . PHE   A 1 368 ? 146.364 98.386  126.346 1.00 49.69  ?  368  PHE   A CA    1 
ATOM   2909  C  C     . PHE   A 1 368 ? 147.430 99.473  126.373 1.00 55.70  ?  368  PHE   A C     1 
ATOM   2910  O  O     . PHE   A 1 368 ? 147.998 99.811  125.329 1.00 64.34  ?  368  PHE   A O     1 
ATOM   2911  C  CB    . PHE   A 1 368 ? 144.997 98.985  126.020 1.00 51.38  ?  368  PHE   A CB    1 
ATOM   2912  C  CG    . PHE   A 1 368 ? 144.946 99.711  124.708 1.00 53.83  ?  368  PHE   A CG    1 
ATOM   2913  C  CD1   . PHE   A 1 368 ? 145.168 99.040  123.520 1.00 51.51  ?  368  PHE   A CD1   1 
ATOM   2914  C  CD2   . PHE   A 1 368 ? 144.664 101.065 124.663 1.00 53.11  ?  368  PHE   A CD2   1 
ATOM   2915  C  CE1   . PHE   A 1 368 ? 145.114 99.706  122.313 1.00 54.05  ?  368  PHE   A CE1   1 
ATOM   2916  C  CE2   . PHE   A 1 368 ? 144.611 101.736 123.458 1.00 49.68  ?  368  PHE   A CE2   1 
ATOM   2917  C  CZ    . PHE   A 1 368 ? 144.838 101.055 122.282 1.00 52.88  ?  368  PHE   A CZ    1 
ATOM   2918  N  N     . PHE   A 1 369 ? 147.718 100.024 127.549 1.00 61.14  ?  369  PHE   A N     1 
ATOM   2919  C  CA    . PHE   A 1 369 ? 148.735 101.055 127.701 1.00 58.90  ?  369  PHE   A CA    1 
ATOM   2920  C  C     . PHE   A 1 369 ? 150.022 100.536 128.327 1.00 60.84  ?  369  PHE   A C     1 
ATOM   2921  O  O     . PHE   A 1 369 ? 151.111 100.935 127.907 1.00 66.18  ?  369  PHE   A O     1 
ATOM   2922  C  CB    . PHE   A 1 369 ? 148.195 102.212 128.550 1.00 53.64  ?  369  PHE   A CB    1 
ATOM   2923  C  CG    . PHE   A 1 369 ? 146.883 102.763 128.066 1.00 50.18  ?  369  PHE   A CG    1 
ATOM   2924  C  CD1   . PHE   A 1 369 ? 146.845 103.764 127.113 1.00 52.00  ?  369  PHE   A CD1   1 
ATOM   2925  C  CD2   . PHE   A 1 369 ? 145.687 102.286 128.574 1.00 48.51  ?  369  PHE   A CD2   1 
ATOM   2926  C  CE1   . PHE   A 1 369 ? 145.639 104.274 126.672 1.00 53.51  ?  369  PHE   A CE1   1 
ATOM   2927  C  CE2   . PHE   A 1 369 ? 144.480 102.792 128.133 1.00 52.31  ?  369  PHE   A CE2   1 
ATOM   2928  C  CZ    . PHE   A 1 369 ? 144.457 103.786 127.181 1.00 53.48  ?  369  PHE   A CZ    1 
ATOM   2929  N  N     . ALA   A 1 370 ? 149.927 99.643  129.313 1.00 68.15  ?  370  ALA   A N     1 
ATOM   2930  C  CA    . ALA   A 1 370 ? 151.101 99.273  130.097 1.00 64.88  ?  370  ALA   A CA    1 
ATOM   2931  C  C     . ALA   A 1 370 ? 151.954 98.218  129.397 1.00 70.59  ?  370  ALA   A C     1 
ATOM   2932  O  O     . ALA   A 1 370 ? 153.111 98.473  129.047 1.00 76.28  ?  370  ALA   A O     1 
ATOM   2933  C  CB    . ALA   A 1 370 ? 150.668 98.779  131.480 1.00 68.39  ?  370  ALA   A CB    1 
ATOM   2934  N  N     . ASP   A 1 371 ? 151.413 97.012  129.222 1.00 90.90  ?  371  ASP   A N     1 
ATOM   2935  C  CA    . ASP   A 1 371 ? 152.196 95.844  128.740 1.00 93.28  ?  371  ASP   A CA    1 
ATOM   2936  C  C     . ASP   A 1 371 ? 151.621 95.339  127.421 1.00 91.38  ?  371  ASP   A C     1 
ATOM   2937  O  O     . ASP   A 1 371 ? 150.466 94.948  127.442 1.00 98.69  ?  371  ASP   A O     1 
ATOM   2938  C  CB    . ASP   A 1 371 ? 152.149 94.832  129.871 1.00 92.18  ?  371  ASP   A CB    1 
ATOM   2939  C  CG    . ASP   A 1 371 ? 152.954 93.551  129.738 1.00 98.47  ?  371  ASP   A CG    1 
ATOM   2940  O  OD1   . ASP   A 1 371 ? 153.517 93.320  128.665 1.00 99.15  ?  371  ASP   A OD1   1 
ATOM   2941  O  OD2   . ASP   A 1 371 ? 153.012 92.796  130.729 1.00 100.55 ?  371  ASP   A OD2   1 
ATOM   2942  N  N     . GLN   A 1 372 ? 152.361 95.402  126.318 1.00 73.98  ?  372  GLN   A N     1 
ATOM   2943  C  CA    . GLN   A 1 372 ? 151.863 94.994  125.009 1.00 75.52  ?  372  GLN   A CA    1 
ATOM   2944  C  C     . GLN   A 1 372 ? 151.728 93.480  124.896 1.00 84.34  ?  372  GLN   A C     1 
ATOM   2945  O  O     . GLN   A 1 372 ? 150.772 92.987  124.287 1.00 85.93  ?  372  GLN   A O     1 
ATOM   2946  C  CB    . GLN   A 1 372 ? 152.775 95.536  123.911 1.00 73.46  ?  372  GLN   A CB    1 
ATOM   2947  C  CG    . GLN   A 1 372 ? 152.807 97.053  123.843 1.00 78.30  ?  372  GLN   A CG    1 
ATOM   2948  C  CD    . GLN   A 1 372 ? 151.419 97.665  123.841 1.00 83.31  ?  372  GLN   A CD    1 
ATOM   2949  O  OE1   . GLN   A 1 372 ? 150.535 97.225  123.106 1.00 88.25  ?  372  GLN   A OE1   1 
ATOM   2950  N  NE2   . GLN   A 1 372 ? 151.220 98.683  124.669 1.00 80.60  ?  372  GLN   A NE2   1 
ATOM   2951  N  N     . GLU   A 1 373 ? 152.672 92.726  125.465 1.00 90.67  ?  373  GLU   A N     1 
ATOM   2952  C  CA    . GLU   A 1 373 ? 152.560 91.270  125.445 1.00 88.69  ?  373  GLU   A CA    1 
ATOM   2953  C  C     . GLU   A 1 373 ? 151.347 90.803  126.239 1.00 90.68  ?  373  GLU   A C     1 
ATOM   2954  O  O     . GLU   A 1 373 ? 150.606 89.913  125.799 1.00 93.02  ?  373  GLU   A O     1 
ATOM   2955  C  CB    . GLU   A 1 373 ? 153.839 90.639  125.994 1.00 88.26  ?  373  GLU   A CB    1 
ATOM   2956  C  CG    . GLU   A 1 373 ? 153.961 89.149  125.728 1.00 93.57  ?  373  GLU   A CG    1 
ATOM   2957  C  CD    . GLU   A 1 373 ? 155.004 88.484  126.605 1.00 97.46  ?  373  GLU   A CD    1 
ATOM   2958  O  OE1   . GLU   A 1 373 ? 155.218 87.263  126.455 1.00 95.26  ?  373  GLU   A OE1   1 
ATOM   2959  O  OE2   . GLU   A 1 373 ? 155.611 89.182  127.444 1.00 98.28  ?  373  GLU   A OE2   1 
ATOM   2960  N  N     . GLU   A 1 374 ? 151.125 91.399  127.413 1.00 83.84  ?  374  GLU   A N     1 
ATOM   2961  C  CA    . GLU   A 1 374 ? 149.942 91.068  128.199 1.00 81.42  ?  374  GLU   A CA    1 
ATOM   2962  C  C     . GLU   A 1 374 ? 148.668 91.452  127.461 1.00 82.08  ?  374  GLU   A C     1 
ATOM   2963  O  O     . GLU   A 1 374 ? 147.672 90.721  127.509 1.00 83.67  ?  374  GLU   A O     1 
ATOM   2964  C  CB    . GLU   A 1 374 ? 150.004 91.756  129.562 1.00 80.65  ?  374  GLU   A CB    1 
ATOM   2965  C  CG    . GLU   A 1 374 ? 148.755 91.574  130.418 1.00 83.09  ?  374  GLU   A CG    1 
ATOM   2966  C  CD    . GLU   A 1 374 ? 148.595 90.162  130.956 1.00 88.96  ?  374  GLU   A CD    1 
ATOM   2967  O  OE1   . GLU   A 1 374 ? 149.473 89.310  130.706 1.00 90.12  ?  374  GLU   A OE1   1 
ATOM   2968  O  OE2   . GLU   A 1 374 ? 147.580 89.902  131.635 1.00 90.59  ?  374  GLU   A OE2   1 
ATOM   2969  N  N     . PHE   A 1 375 ? 148.675 92.601  126.779 1.00 69.88  ?  375  PHE   A N     1 
ATOM   2970  C  CA    . PHE   A 1 375 ? 147.502 92.989  126.005 1.00 66.02  ?  375  PHE   A CA    1 
ATOM   2971  C  C     . PHE   A 1 375 ? 147.227 91.991  124.892 1.00 71.93  ?  375  PHE   A C     1 
ATOM   2972  O  O     . PHE   A 1 375 ? 146.072 91.641  124.641 1.00 80.91  ?  375  PHE   A O     1 
ATOM   2973  C  CB    . PHE   A 1 375 ? 147.668 94.389  125.419 1.00 65.97  ?  375  PHE   A CB    1 
ATOM   2974  C  CG    . PHE   A 1 375 ? 146.576 94.764  124.455 1.00 66.09  ?  375  PHE   A CG    1 
ATOM   2975  C  CD1   . PHE   A 1 375 ? 145.343 95.188  124.919 1.00 64.79  ?  375  PHE   A CD1   1 
ATOM   2976  C  CD2   . PHE   A 1 375 ? 146.772 94.669  123.088 1.00 67.06  ?  375  PHE   A CD2   1 
ATOM   2977  C  CE1   . PHE   A 1 375 ? 144.333 95.524  124.040 1.00 65.93  ?  375  PHE   A CE1   1 
ATOM   2978  C  CE2   . PHE   A 1 375 ? 145.763 95.002  122.204 1.00 68.05  ?  375  PHE   A CE2   1 
ATOM   2979  C  CZ    . PHE   A 1 375 ? 144.543 95.431  122.682 1.00 68.57  ?  375  PHE   A CZ    1 
ATOM   2980  N  N     . GLU   A 1 376 ? 148.274 91.535  124.201 1.00 79.26  ?  376  GLU   A N     1 
ATOM   2981  C  CA    . GLU   A 1 376 ? 148.081 90.547  123.145 1.00 77.67  ?  376  GLU   A CA    1 
ATOM   2982  C  C     . GLU   A 1 376 ? 147.520 89.248  123.707 1.00 79.94  ?  376  GLU   A C     1 
ATOM   2983  O  O     . GLU   A 1 376 ? 146.600 88.658  123.127 1.00 85.58  ?  376  GLU   A O     1 
ATOM   2984  C  CB    . GLU   A 1 376 ? 149.399 90.292  122.416 1.00 79.80  ?  376  GLU   A CB    1 
ATOM   2985  C  CG    . GLU   A 1 376 ? 149.277 89.348  121.233 1.00 85.54  ?  376  GLU   A CG    1 
ATOM   2986  C  CD    . GLU   A 1 376 ? 149.868 89.927  119.963 1.00 91.56  ?  376  GLU   A CD    1 
ATOM   2987  O  OE1   . GLU   A 1 376 ? 150.253 91.114  119.973 1.00 93.56  ?  376  GLU   A OE1   1 
ATOM   2988  O  OE2   . GLU   A 1 376 ? 149.946 89.194  118.954 1.00 92.15  ?  376  GLU   A OE2   1 
ATOM   2989  N  N     . ARG   A 1 377 ? 148.053 88.794  124.843 1.00 73.20  ?  377  ARG   A N     1 
ATOM   2990  C  CA    . ARG   A 1 377 ? 147.552 87.567  125.456 1.00 73.55  ?  377  ARG   A CA    1 
ATOM   2991  C  C     . ARG   A 1 377 ? 146.083 87.704  125.841 1.00 74.82  ?  377  ARG   A C     1 
ATOM   2992  O  O     . ARG   A 1 377 ? 145.264 86.826  125.540 1.00 78.73  ?  377  ARG   A O     1 
ATOM   2993  C  CB    . ARG   A 1 377 ? 148.397 87.210  126.679 1.00 73.93  ?  377  ARG   A CB    1 
ATOM   2994  C  CG    . ARG   A 1 377 ? 147.990 85.908  127.347 1.00 75.84  ?  377  ARG   A CG    1 
ATOM   2995  C  CD    . ARG   A 1 377 ? 148.679 85.727  128.689 1.00 76.88  ?  377  ARG   A CD    1 
ATOM   2996  N  NE    . ARG   A 1 377 ? 148.126 86.604  129.714 1.00 78.62  ?  377  ARG   A NE    1 
ATOM   2997  C  CZ    . ARG   A 1 377 ? 146.981 86.391  130.347 1.00 81.07  ?  377  ARG   A CZ    1 
ATOM   2998  N  NH1   . ARG   A 1 377 ? 146.224 85.341  130.073 1.00 80.21  ?  377  ARG   A NH1   1 
ATOM   2999  N  NH2   . ARG   A 1 377 ? 146.585 87.252  131.279 1.00 77.99  ?  377  ARG   A NH2   1 
ATOM   3000  N  N     . LEU   A 1 378 ? 145.730 88.808  126.504 1.00 70.94  ?  378  LEU   A N     1 
ATOM   3001  C  CA    . LEU   A 1 378 ? 144.350 89.012  126.933 1.00 66.83  ?  378  LEU   A CA    1 
ATOM   3002  C  C     . LEU   A 1 378 ? 143.412 89.161  125.742 1.00 71.55  ?  378  LEU   A C     1 
ATOM   3003  O  O     . LEU   A 1 378 ? 142.292 88.641  125.760 1.00 78.98  ?  378  LEU   A O     1 
ATOM   3004  C  CB    . LEU   A 1 378 ? 144.262 90.235  127.843 1.00 70.63  ?  378  LEU   A CB    1 
ATOM   3005  C  CG    . LEU   A 1 378 ? 144.829 90.057  129.251 1.00 70.77  ?  378  LEU   A CG    1 
ATOM   3006  C  CD1   . LEU   A 1 378 ? 144.826 91.376  130.002 1.00 68.15  ?  378  LEU   A CD1   1 
ATOM   3007  C  CD2   . LEU   A 1 378 ? 144.034 89.007  130.006 1.00 72.79  ?  378  LEU   A CD2   1 
ATOM   3008  N  N     . TYR   A 1 379 ? 143.847 89.878  124.704 1.00 70.50  ?  379  TYR   A N     1 
ATOM   3009  C  CA    . TYR   A 1 379 ? 143.033 90.047  123.507 1.00 69.31  ?  379  TYR   A CA    1 
ATOM   3010  C  C     . TYR   A 1 379 ? 142.775 88.712  122.825 1.00 76.45  ?  379  TYR   A C     1 
ATOM   3011  O  O     . TYR   A 1 379 ? 141.643 88.420  122.421 1.00 80.00  ?  379  TYR   A O     1 
ATOM   3012  C  CB    . TYR   A 1 379 ? 143.731 91.016  122.553 1.00 66.92  ?  379  TYR   A CB    1 
ATOM   3013  C  CG    . TYR   A 1 379 ? 142.834 91.647  121.517 1.00 68.94  ?  379  TYR   A CG    1 
ATOM   3014  C  CD1   . TYR   A 1 379 ? 142.047 92.745  121.829 1.00 73.33  ?  379  TYR   A CD1   1 
ATOM   3015  C  CD2   . TYR   A 1 379 ? 142.790 91.157  120.221 1.00 68.20  ?  379  TYR   A CD2   1 
ATOM   3016  C  CE1   . TYR   A 1 379 ? 141.232 93.329  120.882 1.00 76.14  ?  379  TYR   A CE1   1 
ATOM   3017  C  CE2   . TYR   A 1 379 ? 141.978 91.736  119.268 1.00 66.37  ?  379  TYR   A CE2   1 
ATOM   3018  C  CZ    . TYR   A 1 379 ? 141.201 92.820  119.604 1.00 73.47  ?  379  TYR   A CZ    1 
ATOM   3019  O  OH    . TYR   A 1 379 ? 140.392 93.399  118.657 1.00 81.63  ?  379  TYR   A OH    1 
ATOM   3020  N  N     . THR   A 1 380 ? 143.814 87.883  122.695 1.00 78.15  ?  380  THR   A N     1 
ATOM   3021  C  CA    . THR   A 1 380 ? 143.636 86.565  122.098 1.00 74.47  ?  380  THR   A CA    1 
ATOM   3022  C  C     . THR   A 1 380 ? 142.706 85.702  122.941 1.00 80.94  ?  380  THR   A C     1 
ATOM   3023  O  O     . THR   A 1 380 ? 141.845 84.996  122.403 1.00 85.04  ?  380  THR   A O     1 
ATOM   3024  C  CB    . THR   A 1 380 ? 144.993 85.885  121.919 1.00 79.17  ?  380  THR   A CB    1 
ATOM   3025  O  OG1   . THR   A 1 380 ? 145.655 86.435  120.773 1.00 80.89  ?  380  THR   A OG1   1 
ATOM   3026  C  CG2   . THR   A 1 380 ? 144.823 84.387  121.724 1.00 83.43  ?  380  THR   A CG2   1 
ATOM   3027  N  N     . LYS   A 1 381 ? 142.859 85.749  124.268 1.00 75.07  ?  381  LYS   A N     1 
ATOM   3028  C  CA    . LYS   A 1 381 ? 142.004 84.944  125.135 1.00 70.33  ?  381  LYS   A CA    1 
ATOM   3029  C  C     . LYS   A 1 381 ? 140.546 85.379  125.044 1.00 73.96  ?  381  LYS   A C     1 
ATOM   3030  O  O     . LYS   A 1 381 ? 139.643 84.538  124.973 1.00 79.74  ?  381  LYS   A O     1 
ATOM   3031  C  CB    . LYS   A 1 381 ? 142.496 85.025  126.579 1.00 72.17  ?  381  LYS   A CB    1 
ATOM   3032  C  CG    . LYS   A 1 381 ? 141.647 84.242  127.565 1.00 73.62  ?  381  LYS   A CG    1 
ATOM   3033  C  CD    . LYS   A 1 381 ? 141.460 85.006  128.862 1.00 72.17  ?  381  LYS   A CD    1 
ATOM   3034  C  CE    . LYS   A 1 381 ? 142.722 84.976  129.704 1.00 77.36  ?  381  LYS   A CE    1 
ATOM   3035  N  NZ    . LYS   A 1 381 ? 142.698 83.866  130.696 1.00 79.04  ?  381  LYS   A NZ    1 
ATOM   3036  N  N     . TYR   A 1 382 ? 140.296 86.689  125.044 1.00 72.38  ?  382  TYR   A N     1 
ATOM   3037  C  CA    . TYR   A 1 382 ? 138.927 87.189  125.027 1.00 67.00  ?  382  TYR   A CA    1 
ATOM   3038  C  C     . TYR   A 1 382 ? 138.284 87.062  123.653 1.00 72.18  ?  382  TYR   A C     1 
ATOM   3039  O  O     . TYR   A 1 382 ? 137.054 86.997  123.556 1.00 78.43  ?  382  TYR   A O     1 
ATOM   3040  C  CB    . TYR   A 1 382 ? 138.894 88.646  125.491 1.00 68.55  ?  382  TYR   A CB    1 
ATOM   3041  C  CG    . TYR   A 1 382 ? 139.282 88.829  126.941 1.00 72.93  ?  382  TYR   A CG    1 
ATOM   3042  C  CD1   . TYR   A 1 382 ? 138.942 87.879  127.893 1.00 71.94  ?  382  TYR   A CD1   1 
ATOM   3043  C  CD2   . TYR   A 1 382 ? 139.989 89.948  127.357 1.00 74.97  ?  382  TYR   A CD2   1 
ATOM   3044  C  CE1   . TYR   A 1 382 ? 139.293 88.039  129.218 1.00 72.59  ?  382  TYR   A CE1   1 
ATOM   3045  C  CE2   . TYR   A 1 382 ? 140.346 90.115  128.680 1.00 70.48  ?  382  TYR   A CE2   1 
ATOM   3046  C  CZ    . TYR   A 1 382 ? 139.996 89.158  129.606 1.00 69.10  ?  382  TYR   A CZ    1 
ATOM   3047  O  OH    . TYR   A 1 382 ? 140.349 89.321  130.925 1.00 74.42  ?  382  TYR   A OH    1 
ATOM   3048  N  N     . GLU   A 1 383 ? 139.087 87.033  122.587 1.00 80.63  ?  383  GLU   A N     1 
ATOM   3049  C  CA    . GLU   A 1 383 ? 138.526 86.852  121.253 1.00 78.70  ?  383  GLU   A CA    1 
ATOM   3050  C  C     . GLU   A 1 383 ? 137.925 85.464  121.078 1.00 84.83  ?  383  GLU   A C     1 
ATOM   3051  O  O     . GLU   A 1 383 ? 136.956 85.300  120.328 1.00 87.50  ?  383  GLU   A O     1 
ATOM   3052  C  CB    . GLU   A 1 383 ? 139.597 87.101  120.193 1.00 79.34  ?  383  GLU   A CB    1 
ATOM   3053  C  CG    . GLU   A 1 383 ? 139.678 88.539  119.726 1.00 80.46  ?  383  GLU   A CG    1 
ATOM   3054  C  CD    . GLU   A 1 383 ? 140.607 88.712  118.544 1.00 87.93  ?  383  GLU   A CD    1 
ATOM   3055  O  OE1   . GLU   A 1 383 ? 141.759 88.237  118.618 1.00 89.98  ?  383  GLU   A OE1   1 
ATOM   3056  O  OE2   . GLU   A 1 383 ? 140.186 89.322  117.539 1.00 88.84  ?  383  GLU   A OE2   1 
ATOM   3057  N  N     . LYS   A 1 384 ? 138.481 84.461  121.752 1.00 84.59  ?  384  LYS   A N     1 
ATOM   3058  C  CA    . LYS   A 1 384 ? 137.981 83.096  121.674 1.00 83.64  ?  384  LYS   A CA    1 
ATOM   3059  C  C     . LYS   A 1 384 ? 136.899 82.798  122.704 1.00 88.73  ?  384  LYS   A C     1 
ATOM   3060  O  O     . LYS   A 1 384 ? 136.332 81.701  122.683 1.00 92.96  ?  384  LYS   A O     1 
ATOM   3061  C  CB    . LYS   A 1 384 ? 139.135 82.102  121.845 1.00 84.94  ?  384  LYS   A CB    1 
ATOM   3062  C  CG    . LYS   A 1 384 ? 140.164 82.147  120.730 1.00 87.65  ?  384  LYS   A CG    1 
ATOM   3063  C  CD    . LYS   A 1 384 ? 141.275 81.138  120.966 1.00 88.80  ?  384  LYS   A CD    1 
ATOM   3064  C  CE    . LYS   A 1 384 ? 142.332 81.215  119.877 1.00 90.16  ?  384  LYS   A CE    1 
ATOM   3065  N  NZ    . LYS   A 1 384 ? 141.781 80.869  118.538 1.00 90.80  ?  384  LYS   A NZ    1 
ATOM   3066  N  N     . ASP   A 1 385 ? 136.599 83.737  123.597 1.00 93.95  ?  385  ASP   A N     1 
ATOM   3067  C  CA    . ASP   A 1 385 ? 135.599 83.528  124.636 1.00 93.82  ?  385  ASP   A CA    1 
ATOM   3068  C  C     . ASP   A 1 385 ? 134.226 83.903  124.094 1.00 96.09  ?  385  ASP   A C     1 
ATOM   3069  O  O     . ASP   A 1 385 ? 133.994 85.058  123.720 1.00 99.16  ?  385  ASP   A O     1 
ATOM   3070  C  CB    . ASP   A 1 385 ? 135.934 84.350  125.879 1.00 92.59  ?  385  ASP   A CB    1 
ATOM   3071  C  CG    . ASP   A 1 385 ? 135.234 83.838  127.122 1.00 97.71  ?  385  ASP   A CG    1 
ATOM   3072  O  OD1   . ASP   A 1 385 ? 134.403 82.914  127.000 1.00 100.79 ?  385  ASP   A OD1   1 
ATOM   3073  O  OD2   . ASP   A 1 385 ? 135.517 84.356  128.222 1.00 98.18  ?  385  ASP   A OD2   1 
ATOM   3074  N  N     . ASP   A 1 386 ? 133.317 82.929  124.057 1.00 95.04  ?  386  ASP   A N     1 
ATOM   3075  C  CA    . ASP   A 1 386 ? 131.979 83.153  123.526 1.00 94.43  ?  386  ASP   A CA    1 
ATOM   3076  C  C     . ASP   A 1 386 ? 131.017 83.732  124.554 1.00 94.61  ?  386  ASP   A C     1 
ATOM   3077  O  O     . ASP   A 1 386 ? 129.878 84.054  124.198 1.00 95.50  ?  386  ASP   A O     1 
ATOM   3078  C  CB    . ASP   A 1 386 ? 131.411 81.844  122.972 1.00 97.29  ?  386  ASP   A CB    1 
ATOM   3079  C  CG    . ASP   A 1 386 ? 132.114 81.393  121.708 1.00 99.61  ?  386  ASP   A CG    1 
ATOM   3080  O  OD1   . ASP   A 1 386 ? 133.100 82.048  121.310 1.00 99.80  ?  386  ASP   A OD1   1 
ATOM   3081  O  OD2   . ASP   A 1 386 ? 131.682 80.384  121.112 1.00 98.86  ?  386  ASP   A OD2   1 
ATOM   3082  N  N     . SER   A 1 387 ? 131.438 83.869  125.809 1.00 96.53  ?  387  SER   A N     1 
ATOM   3083  C  CA    . SER   A 1 387 ? 130.601 84.440  126.854 1.00 97.34  ?  387  SER   A CA    1 
ATOM   3084  C  C     . SER   A 1 387 ? 130.771 85.946  126.990 1.00 98.53  ?  387  SER   A C     1 
ATOM   3085  O  O     . SER   A 1 387 ? 130.134 86.551  127.858 1.00 101.25 ?  387  SER   A O     1 
ATOM   3086  C  CB    . SER   A 1 387 ? 130.902 83.768  128.197 1.00 97.58  ?  387  SER   A CB    1 
ATOM   3087  O  OG    . SER   A 1 387 ? 132.289 83.513  128.337 1.00 98.30  ?  387  SER   A OG    1 
ATOM   3088  N  N     . ILE   A 1 388 ? 131.607 86.562  126.160 1.00 79.12  ?  388  ILE   A N     1 
ATOM   3089  C  CA    . ILE   A 1 388 ? 131.894 87.989  126.228 1.00 77.17  ?  388  ILE   A CA    1 
ATOM   3090  C  C     . ILE   A 1 388 ? 131.295 88.658  125.001 1.00 78.59  ?  388  ILE   A C     1 
ATOM   3091  O  O     . ILE   A 1 388 ? 131.562 88.242  123.868 1.00 80.12  ?  388  ILE   A O     1 
ATOM   3092  C  CB    . ILE   A 1 388 ? 133.406 88.254  126.316 1.00 78.35  ?  388  ILE   A CB    1 
ATOM   3093  C  CG1   . ILE   A 1 388 ? 133.951 87.775  127.662 1.00 78.93  ?  388  ILE   A CG1   1 
ATOM   3094  C  CG2   . ILE   A 1 388 ? 133.706 89.729  126.108 1.00 78.99  ?  388  ILE   A CG2   1 
ATOM   3095  C  CD1   . ILE   A 1 388 ? 135.449 87.623  127.691 1.00 77.96  ?  388  ILE   A CD1   1 
ATOM   3096  N  N     . ARG   A 1 389 ? 130.480 89.686  125.228 1.00 78.88  ?  389  ARG   A N     1 
ATOM   3097  C  CA    A ARG   A 1 389 ? 129.913 90.444  124.122 0.50 78.92  ?  389  ARG   A CA    1 
ATOM   3098  C  CA    B ARG   A 1 389 ? 130.013 90.444  124.122 0.50 78.92  ?  389  ARG   A CA    1 
ATOM   3099  C  C     . ARG   A 1 389 ? 131.022 91.131  123.338 1.00 77.79  ?  389  ARG   A C     1 
ATOM   3100  O  O     . ARG   A 1 389 ? 131.911 91.762  123.917 1.00 84.97  ?  389  ARG   A O     1 
ATOM   3101  C  CB    A ARG   A 1 389 ? 128.914 91.476  124.644 0.50 71.78  ?  389  ARG   A CB    1 
ATOM   3102  C  CB    B ARG   A 1 389 ? 129.014 91.476  124.644 0.50 71.78  ?  389  ARG   A CB    1 
ATOM   3103  C  CG    A ARG   A 1 389 ? 128.193 92.244  123.552 0.50 72.69  ?  389  ARG   A CG    1 
ATOM   3104  C  CG    B ARG   A 1 389 ? 128.408 92.350  123.562 0.50 72.69  ?  389  ARG   A CG    1 
ATOM   3105  C  CD    A ARG   A 1 389 ? 127.004 93.009  124.103 0.50 76.64  ?  389  ARG   A CD    1 
ATOM   3106  C  CD    B ARG   A 1 389 ? 127.373 93.302  124.132 0.50 76.64  ?  389  ARG   A CD    1 
ATOM   3107  N  NE    A ARG   A 1 389 ? 127.416 94.197  124.841 0.50 80.54  ?  389  ARG   A NE    1 
ATOM   3108  N  NE    B ARG   A 1 389 ? 126.768 94.131  123.096 0.50 80.54  ?  389  ARG   A NE    1 
ATOM   3109  C  CZ    A ARG   A 1 389 ? 127.022 95.430  124.554 0.50 79.52  ?  389  ARG   A CZ    1 
ATOM   3110  C  CZ    B ARG   A 1 389 ? 125.710 94.908  123.283 0.50 79.52  ?  389  ARG   A CZ    1 
ATOM   3111  N  NH1   A ARG   A 1 389 ? 126.203 95.676  123.545 0.50 77.16  ?  389  ARG   A NH1   1 
ATOM   3112  N  NH1   B ARG   A 1 389 ? 125.109 94.986  124.459 0.50 77.16  ?  389  ARG   A NH1   1 
ATOM   3113  N  NH2   A ARG   A 1 389 ? 127.465 96.441  125.295 0.50 74.80  ?  389  ARG   A NH2   1 
ATOM   3114  N  NH2   B ARG   A 1 389 ? 125.240 95.620  122.263 0.50 74.80  ?  389  ARG   A NH2   1 
ATOM   3115  N  N     . LYS   A 1 390 ? 130.969 91.005  122.015 1.00 63.00  ?  390  LYS   A N     1 
ATOM   3116  C  CA    . LYS   A 1 390 ? 132.007 91.563  121.161 1.00 62.43  ?  390  LYS   A CA    1 
ATOM   3117  C  C     . LYS   A 1 390 ? 131.435 91.781  119.771 1.00 68.60  ?  390  LYS   A C     1 
ATOM   3118  O  O     . LYS   A 1 390 ? 130.394 91.225  119.414 1.00 77.50  ?  390  LYS   A O     1 
ATOM   3119  C  CB    . LYS   A 1 390 ? 133.229 90.644  121.092 1.00 64.58  ?  390  LYS   A CB    1 
ATOM   3120  C  CG    . LYS   A 1 390 ? 132.906 89.241  120.608 1.00 66.37  ?  390  LYS   A CG    1 
ATOM   3121  C  CD    . LYS   A 1 390 ? 134.150 88.377  120.539 1.00 67.43  ?  390  LYS   A CD    1 
ATOM   3122  C  CE    . LYS   A 1 390 ? 134.327 87.574  121.810 1.00 71.98  ?  390  LYS   A CE    1 
ATOM   3123  N  NZ    . LYS   A 1 390 ? 133.148 86.708  122.081 1.00 73.81  ?  390  LYS   A NZ    1 
ATOM   3124  N  N     . GLN   A 1 391 ? 132.131 92.605  118.991 1.00 68.75  ?  391  GLN   A N     1 
ATOM   3125  C  CA    A GLN   A 1 391 ? 131.758 92.879  117.609 0.58 68.97  ?  391  GLN   A CA    1 
ATOM   3126  C  CA    B GLN   A 1 391 ? 131.755 92.852  117.606 0.42 70.31  ?  391  GLN   A CA    1 
ATOM   3127  C  C     . GLN   A 1 391 ? 132.989 92.757  116.724 1.00 72.60  ?  391  GLN   A C     1 
ATOM   3128  O  O     . GLN   A 1 391 ? 134.025 93.352  117.025 1.00 76.01  ?  391  GLN   A O     1 
ATOM   3129  C  CB    A GLN   A 1 391 ? 131.147 94.276  117.472 0.58 72.87  ?  391  GLN   A CB    1 
ATOM   3130  C  CB    B GLN   A 1 391 ? 131.081 94.218  117.442 0.42 72.67  ?  391  GLN   A CB    1 
ATOM   3131  C  CG    A GLN   A 1 391 ? 130.032 94.377  116.451 0.58 71.97  ?  391  GLN   A CG    1 
ATOM   3132  C  CG    B GLN   A 1 391 ? 129.729 94.318  118.129 0.42 71.85  ?  391  GLN   A CG    1 
ATOM   3133  C  CD    A GLN   A 1 391 ? 129.955 95.751  115.818 0.58 75.62  ?  391  GLN   A CD    1 
ATOM   3134  C  CD    B GLN   A 1 391 ? 129.111 95.694  118.008 0.42 73.25  ?  391  GLN   A CD    1 
ATOM   3135  O  OE1   A GLN   A 1 391 ? 129.907 96.766  116.513 0.58 79.39  ?  391  GLN   A OE1   1 
ATOM   3136  O  OE1   B GLN   A 1 391 ? 129.548 96.514  117.202 0.42 75.91  ?  391  GLN   A OE1   1 
ATOM   3137  N  NE2   A GLN   A 1 391 ? 129.949 95.792  114.491 0.58 72.53  ?  391  GLN   A NE2   1 
ATOM   3138  N  NE2   B GLN   A 1 391 ? 128.085 95.955  118.811 0.42 72.44  ?  391  GLN   A NE2   1 
ATOM   3139  N  N     . ARG   A 1 392 ? 132.875 92.007  115.636 1.00 85.22  ?  392  ARG   A N     1 
ATOM   3140  C  CA    A ARG   A 1 392 ? 133.976 91.831  114.700 0.50 83.92  ?  392  ARG   A CA    1 
ATOM   3141  C  CA    B ARG   A 1 392 ? 134.076 91.831  114.700 0.50 83.92  ?  392  ARG   A CA    1 
ATOM   3142  C  C     . ARG   A 1 392 ? 133.829 92.821  113.553 1.00 82.45  ?  392  ARG   A C     1 
ATOM   3143  O  O     . ARG   A 1 392 ? 132.750 92.939  112.965 1.00 89.23  ?  392  ARG   A O     1 
ATOM   3144  C  CB    A ARG   A 1 392 ? 134.013 90.399  114.168 0.50 85.43  ?  392  ARG   A CB    1 
ATOM   3145  C  CB    B ARG   A 1 392 ? 134.113 90.399  114.168 0.50 85.43  ?  392  ARG   A CB    1 
ATOM   3146  C  CG    A ARG   A 1 392 ? 134.242 89.358  115.243 0.50 84.48  ?  392  ARG   A CG    1 
ATOM   3147  C  CG    B ARG   A 1 392 ? 134.451 89.368  115.224 0.50 84.48  ?  392  ARG   A CG    1 
ATOM   3148  C  CD    A ARG   A 1 392 ? 135.522 88.570  114.998 0.50 89.28  ?  392  ARG   A CD    1 
ATOM   3149  C  CD    B ARG   A 1 392 ? 134.403 87.953  114.662 0.50 89.28  ?  392  ARG   A CD    1 
ATOM   3150  N  NE    A ARG   A 1 392 ? 136.089 88.012  116.222 0.50 94.14  ?  392  ARG   A NE    1 
ATOM   3151  N  NE    B ARG   A 1 392 ? 135.406 87.718  113.627 0.50 94.14  ?  392  ARG   A NE    1 
ATOM   3152  C  CZ    A ARG   A 1 392 ? 135.475 87.145  117.019 0.50 93.00  ?  392  ARG   A CZ    1 
ATOM   3153  C  CZ    B ARG   A 1 392 ? 136.670 87.380  113.855 0.50 93.00  ?  392  ARG   A CZ    1 
ATOM   3154  N  NH1   A ARG   A 1 392 ? 134.261 86.691  116.750 0.50 91.25  ?  392  ARG   A NH1   1 
ATOM   3155  N  NH1   B ARG   A 1 392 ? 137.134 87.208  115.082 0.50 91.25  ?  392  ARG   A NH1   1 
ATOM   3156  N  NH2   A ARG   A 1 392 ? 136.096 86.720  118.115 0.50 90.11  ?  392  ARG   A NH2   1 
ATOM   3157  N  NH2   B ARG   A 1 392 ? 137.490 87.206  112.823 0.50 90.11  ?  392  ARG   A NH2   1 
ATOM   3158  N  N     . VAL   A 1 393 ? 134.908 93.536  113.243 1.00 71.89  ?  393  VAL   A N     1 
ATOM   3159  C  CA    . VAL   A 1 393 ? 134.913 94.516  112.166 1.00 69.71  ?  393  VAL   A CA    1 
ATOM   3160  C  C     . VAL   A 1 393 ? 136.182 94.321  111.352 1.00 73.62  ?  393  VAL   A C     1 
ATOM   3161  O  O     . VAL   A 1 393 ? 137.263 94.129  111.915 1.00 82.51  ?  393  VAL   A O     1 
ATOM   3162  C  CB    . VAL   A 1 393 ? 134.825 95.958  112.713 1.00 69.71  ?  393  VAL   A CB    1 
ATOM   3163  C  CG1   . VAL   A 1 393 ? 135.110 96.973  111.617 1.00 73.60  ?  393  VAL   A CG1   1 
ATOM   3164  C  CG2   . VAL   A 1 393 ? 133.459 96.212  113.332 1.00 76.83  ?  393  VAL   A CG2   1 
ATOM   3165  N  N     . LYS   A 1 394 ? 136.054 94.362  110.028 1.00 81.96  ?  394  LYS   A N     1 
ATOM   3166  C  CA    . LYS   A 1 394 ? 137.233 94.282  109.176 1.00 81.53  ?  394  LYS   A CA    1 
ATOM   3167  C  C     . LYS   A 1 394 ? 138.207 95.398  109.533 1.00 81.50  ?  394  LYS   A C     1 
ATOM   3168  O  O     . LYS   A 1 394 ? 137.827 96.570  109.605 1.00 81.53  ?  394  LYS   A O     1 
ATOM   3169  C  CB    . LYS   A 1 394 ? 136.830 94.374  107.705 1.00 82.57  ?  394  LYS   A CB    1 
ATOM   3170  C  CG    . LYS   A 1 394 ? 137.460 93.312  106.823 1.00 82.46  ?  394  LYS   A CG    1 
ATOM   3171  C  CD    . LYS   A 1 394 ? 136.654 92.026  106.847 1.00 83.94  ?  394  LYS   A CD    1 
ATOM   3172  C  CE    . LYS   A 1 394 ? 137.417 90.884  106.195 1.00 85.55  ?  394  LYS   A CE    1 
ATOM   3173  N  NZ    . LYS   A 1 394 ? 138.553 90.424  107.042 1.00 83.75  ?  394  LYS   A NZ    1 
ATOM   3174  N  N     . ALA   A 1 395 ? 139.468 95.025  109.765 1.00 75.02  ?  395  ALA   A N     1 
ATOM   3175  C  CA    . ALA   A 1 395 ? 140.457 95.997  110.219 1.00 72.60  ?  395  ALA   A CA    1 
ATOM   3176  C  C     . ALA   A 1 395 ? 140.665 97.096  109.189 1.00 76.07  ?  395  ALA   A C     1 
ATOM   3177  O  O     . ALA   A 1 395 ? 140.745 98.281  109.539 1.00 81.20  ?  395  ALA   A O     1 
ATOM   3178  C  CB    . ALA   A 1 395 ? 141.779 95.296  110.528 1.00 70.98  ?  395  ALA   A CB    1 
ATOM   3179  N  N     . VAL   A 1 396 ? 140.748 96.724  107.912 1.00 80.11  ?  396  VAL   A N     1 
ATOM   3180  C  CA    . VAL   A 1 396 ? 140.918 97.725  106.867 1.00 80.09  ?  396  VAL   A CA    1 
ATOM   3181  C  C     . VAL   A 1 396 ? 139.692 98.626  106.788 1.00 79.74  ?  396  VAL   A C     1 
ATOM   3182  O  O     . VAL   A 1 396 ? 139.813 99.832  106.556 1.00 84.36  ?  396  VAL   A O     1 
ATOM   3183  C  CB    . VAL   A 1 396 ? 141.234 97.050  105.517 1.00 75.99  ?  396  VAL   A CB    1 
ATOM   3184  C  CG1   . VAL   A 1 396 ? 140.029 96.294  104.975 1.00 74.65  ?  396  VAL   A CG1   1 
ATOM   3185  C  CG2   . VAL   A 1 396 ? 141.720 98.081  104.517 1.00 80.23  ?  396  VAL   A CG2   1 
ATOM   3186  N  N     . GLU   A 1 397 ? 138.499 98.070  107.016 1.00 84.31  ?  397  GLU   A N     1 
ATOM   3187  C  CA    . GLU   A 1 397 ? 137.284 98.879  106.981 1.00 83.88  ?  397  GLU   A CA    1 
ATOM   3188  C  C     . GLU   A 1 397 ? 137.263 99.893  108.119 1.00 86.70  ?  397  GLU   A C     1 
ATOM   3189  O  O     . GLU   A 1 397 ? 136.939 101.069 107.911 1.00 88.21  ?  397  GLU   A O     1 
ATOM   3190  C  CB    . GLU   A 1 397 ? 136.054 97.973  107.041 1.00 84.32  ?  397  GLU   A CB    1 
ATOM   3191  C  CG    . GLU   A 1 397 ? 134.734 98.718  107.076 1.00 90.63  ?  397  GLU   A CG    1 
ATOM   3192  C  CD    . GLU   A 1 397 ? 133.684 98.001  107.901 1.00 97.31  ?  397  GLU   A CD    1 
ATOM   3193  O  OE1   . GLU   A 1 397 ? 133.680 96.752  107.904 1.00 98.12  ?  397  GLU   A OE1   1 
ATOM   3194  O  OE2   . GLU   A 1 397 ? 132.863 98.686  108.548 1.00 95.81  ?  397  GLU   A OE2   1 
ATOM   3195  N  N     . LEU   A 1 398 ? 137.612 99.456  109.332 1.00 72.34  ?  398  LEU   A N     1 
ATOM   3196  C  CA    . LEU   A 1 398 ? 137.638 100.369 110.470 1.00 68.84  ?  398  LEU   A CA    1 
ATOM   3197  C  C     . LEU   A 1 398 ? 138.692 101.453 110.287 1.00 67.58  ?  398  LEU   A C     1 
ATOM   3198  O  O     . LEU   A 1 398 ? 138.435 102.635 110.555 1.00 74.73  ?  398  LEU   A O     1 
ATOM   3199  C  CB    . LEU   A 1 398 ? 137.890 99.588  111.759 1.00 67.63  ?  398  LEU   A CB    1 
ATOM   3200  C  CG    . LEU   A 1 398 ? 137.904 100.388 113.061 1.00 66.76  ?  398  LEU   A CG    1 
ATOM   3201  C  CD1   . LEU   A 1 398 ? 136.526 100.953 113.357 1.00 67.05  ?  398  LEU   A CD1   1 
ATOM   3202  C  CD2   . LEU   A 1 398 ? 138.392 99.525  114.211 1.00 65.57  ?  398  LEU   A CD2   1 
ATOM   3203  N  N     . PHE   A 1 399 ? 139.886 101.070 109.827 1.00 65.91  ?  399  PHE   A N     1 
ATOM   3204  C  CA    . PHE   A 1 399 ? 140.937 102.056 109.606 1.00 63.69  ?  399  PHE   A CA    1 
ATOM   3205  C  C     . PHE   A 1 399 ? 140.550 103.036 108.506 1.00 66.83  ?  399  PHE   A C     1 
ATOM   3206  O  O     . PHE   A 1 399 ? 140.831 104.235 108.609 1.00 72.55  ?  399  PHE   A O     1 
ATOM   3207  C  CB    . PHE   A 1 399 ? 142.253 101.356 109.271 1.00 65.66  ?  399  PHE   A CB    1 
ATOM   3208  C  CG    . PHE   A 1 399 ? 143.123 101.103 110.468 1.00 68.73  ?  399  PHE   A CG    1 
ATOM   3209  C  CD1   . PHE   A 1 399 ? 143.001 99.933  111.195 1.00 63.63  ?  399  PHE   A CD1   1 
ATOM   3210  C  CD2   . PHE   A 1 399 ? 144.061 102.038 110.868 1.00 65.50  ?  399  PHE   A CD2   1 
ATOM   3211  C  CE1   . PHE   A 1 399 ? 143.800 99.699  112.296 1.00 63.59  ?  399  PHE   A CE1   1 
ATOM   3212  C  CE2   . PHE   A 1 399 ? 144.862 101.811 111.970 1.00 61.91  ?  399  PHE   A CE2   1 
ATOM   3213  C  CZ    . PHE   A 1 399 ? 144.731 100.639 112.684 1.00 64.03  ?  399  PHE   A CZ    1 
ATOM   3214  N  N     . SER   A 1 400 ? 139.903 102.546 107.446 1.00 71.62  ?  400  SER   A N     1 
ATOM   3215  C  CA    . SER   A 1 400 ? 139.452 103.425 106.375 1.00 67.11  ?  400  SER   A CA    1 
ATOM   3216  C  C     . SER   A 1 400 ? 138.388 104.394 106.867 1.00 71.49  ?  400  SER   A C     1 
ATOM   3217  O  O     . SER   A 1 400 ? 138.403 105.571 106.498 1.00 80.36  ?  400  SER   A O     1 
ATOM   3218  C  CB    . SER   A 1 400 ? 138.924 102.595 105.206 1.00 70.13  ?  400  SER   A CB    1 
ATOM   3219  O  OG    . SER   A 1 400 ? 139.811 101.535 104.896 1.00 80.89  ?  400  SER   A OG    1 
ATOM   3220  N  N     . LEU   A 1 401 ? 137.455 103.923 107.698 1.00 62.51  ?  401  LEU   A N     1 
ATOM   3221  C  CA    . LEU   A 1 401 ? 136.447 104.822 108.252 1.00 66.55  ?  401  LEU   A CA    1 
ATOM   3222  C  C     . LEU   A 1 401 ? 137.088 105.896 109.123 1.00 68.92  ?  401  LEU   A C     1 
ATOM   3223  O  O     . LEU   A 1 401 ? 136.746 107.083 109.017 1.00 73.73  ?  401  LEU   A O     1 
ATOM   3224  C  CB    . LEU   A 1 401 ? 135.417 104.027 109.054 1.00 65.97  ?  401  LEU   A CB    1 
ATOM   3225  C  CG    . LEU   A 1 401 ? 134.501 104.839 109.973 1.00 65.87  ?  401  LEU   A CG    1 
ATOM   3226  C  CD1   . LEU   A 1 401 ? 133.580 105.732 109.160 1.00 66.54  ?  401  LEU   A CD1   1 
ATOM   3227  C  CD2   . LEU   A 1 401 ? 133.701 103.925 110.884 1.00 65.79  ?  401  LEU   A CD2   1 
ATOM   3228  N  N     . MET   A 1 402 ? 138.030 105.499 109.983 1.00 73.25  ?  402  MET   A N     1 
ATOM   3229  C  CA    . MET   A 1 402 ? 138.701 106.470 110.841 1.00 66.61  ?  402  MET   A CA    1 
ATOM   3230  C  C     . MET   A 1 402 ? 139.475 107.493 110.019 1.00 71.03  ?  402  MET   A C     1 
ATOM   3231  O  O     . MET   A 1 402 ? 139.398 108.699 110.283 1.00 80.69  ?  402  MET   A O     1 
ATOM   3232  C  CB    . MET   A 1 402 ? 139.630 105.752 111.819 1.00 66.89  ?  402  MET   A CB    1 
ATOM   3233  C  CG    . MET   A 1 402 ? 140.816 106.581 112.272 1.00 68.15  ?  402  MET   A CG    1 
ATOM   3234  S  SD    . MET   A 1 402 ? 141.943 105.651 113.324 1.00 89.19  ?  402  MET   A SD    1 
ATOM   3235  C  CE    . MET   A 1 402 ? 143.082 105.007 112.104 1.00 78.39  ?  402  MET   A CE    1 
ATOM   3236  N  N     . MET   A 1 403 ? 140.213 107.034 109.005 1.00 72.00  ?  403  MET   A N     1 
ATOM   3237  C  CA    . MET   A 1 403 ? 140.994 107.955 108.189 1.00 69.55  ?  403  MET   A CA    1 
ATOM   3238  C  C     . MET   A 1 403 ? 140.103 108.844 107.333 1.00 73.13  ?  403  MET   A C     1 
ATOM   3239  O  O     . MET   A 1 403 ? 140.450 110.000 107.082 1.00 74.01  ?  403  MET   A O     1 
ATOM   3240  C  CB    . MET   A 1 403 ? 141.980 107.182 107.315 1.00 66.15  ?  403  MET   A CB    1 
ATOM   3241  C  CG    . MET   A 1 403 ? 143.189 106.654 108.068 1.00 73.47  ?  403  MET   A CG    1 
ATOM   3242  S  SD    . MET   A 1 403 ? 143.964 107.894 109.126 1.00 86.97  ?  403  MET   A SD    1 
ATOM   3243  C  CE    . MET   A 1 403 ? 144.889 108.846 107.927 1.00 80.45  ?  403  MET   A CE    1 
ATOM   3244  N  N     . GLN   A 1 404 ? 138.950 108.310 106.931 1.00 74.02  ?  404  GLN   A N     1 
ATOM   3245  C  CA    A GLN   A 1 404 ? 138.019 109.164 106.134 0.50 73.93  ?  404  GLN   A CA    1 
ATOM   3246  C  CA    B GLN   A 1 404 ? 137.951 109.124 106.174 0.50 73.93  ?  404  GLN   A CA    1 
ATOM   3247  C  C     . GLN   A 1 404 ? 137.357 110.282 107.008 1.00 76.34  ?  404  GLN   A C     1 
ATOM   3248  O  O     . GLN   A 1 404 ? 137.128 111.491 106.639 1.00 80.16  ?  404  GLN   A O     1 
ATOM   3249  C  CB    A GLN   A 1 404 ? 136.911 108.294 105.541 0.50 73.88  ?  404  GLN   A CB    1 
ATOM   3250  C  CB    B GLN   A 1 404 ? 136.777 108.247 105.751 0.50 73.88  ?  404  GLN   A CB    1 
ATOM   3251  C  CG    A GLN   A 1 404 ? 135.724 109.070 105.004 0.50 82.44  ?  404  GLN   A CG    1 
ATOM   3252  C  CG    B GLN   A 1 404 ? 136.823 107.800 104.300 0.50 82.44  ?  404  GLN   A CG    1 
ATOM   3253  C  CD    A GLN   A 1 404 ? 134.451 108.250 105.000 0.50 90.15  ?  404  GLN   A CD    1 
ATOM   3254  C  CD    B GLN   A 1 404 ? 136.420 106.354 104.148 0.50 90.15  ?  404  GLN   A CD    1 
ATOM   3255  O  OE1   A GLN   A 1 404 ? 134.492 107.020 104.999 0.50 89.74  ?  404  GLN   A OE1   1 
ATOM   3256  O  OE1   B GLN   A 1 404 ? 135.826 105.758 105.044 0.50 89.74  ?  404  GLN   A OE1   1 
ATOM   3257  N  NE2   A GLN   A 1 404 ? 133.309 108.928 104.998 0.50 87.34  ?  404  GLN   A NE2   1 
ATOM   3258  N  NE2   B GLN   A 1 404 ? 136.741 105.775 103.003 0.50 87.34  ?  404  GLN   A NE2   1 
ATOM   3259  N  N     . GLU   A 1 405 ? 137.054 109.920 108.247 1.00 74.61  ?  405  GLU   A N     1 
ATOM   3260  C  CA    . GLU   A 1 405 ? 136.570 110.943 109.170 1.00 70.35  ?  405  GLU   A CA    1 
ATOM   3261  C  C     . GLU   A 1 405 ? 137.659 111.964 109.477 1.00 67.42  ?  405  GLU   A C     1 
ATOM   3262  O  O     . GLU   A 1 405 ? 137.389 113.170 109.555 1.00 70.56  ?  405  GLU   A O     1 
ATOM   3263  C  CB    . GLU   A 1 405 ? 136.058 110.293 110.454 1.00 65.60  ?  405  GLU   A CB    1 
ATOM   3264  C  CG    . GLU   A 1 405 ? 134.699 109.636 110.308 1.00 71.23  ?  405  GLU   A CG    1 
ATOM   3265  C  CD    . GLU   A 1 405 ? 133.692 110.535 109.620 1.00 83.17  ?  405  GLU   A CD    1 
ATOM   3266  O  OE1   . GLU   A 1 405 ? 133.492 111.675 110.088 1.00 83.57  ?  405  GLU   A OE1   1 
ATOM   3267  O  OE2   . GLU   A 1 405 ? 133.101 110.104 108.608 1.00 82.79  ?  405  GLU   A OE2   1 
ATOM   3268  N  N     . ARG   A 1 406 ? 138.897 111.497 109.654 1.00 56.86  ?  406  ARG   A N     1 
ATOM   3269  C  CA    . ARG   A 1 406 ? 140.010 112.405 109.910 1.00 53.78  ?  406  ARG   A CA    1 
ATOM   3270  C  C     . ARG   A 1 406 ? 140.254 113.335 108.727 1.00 57.23  ?  406  ARG   A C     1 
ATOM   3271  O  O     . ARG   A 1 406 ? 140.514 114.528 108.911 1.00 60.85  ?  406  ARG   A O     1 
ATOM   3272  C  CB    . ARG   A 1 406 ? 141.269 111.600 110.235 1.00 56.06  ?  406  ARG   A CB    1 
ATOM   3273  C  CG    . ARG   A 1 406 ? 142.568 112.357 110.044 1.00 52.01  ?  406  ARG   A CG    1 
ATOM   3274  C  CD    . ARG   A 1 406 ? 143.743 111.580 110.610 1.00 50.20  ?  406  ARG   A CD    1 
ATOM   3275  N  NE    . ARG   A 1 406 ? 144.997 112.306 110.455 1.00 53.67  ?  406  ARG   A NE    1 
ATOM   3276  C  CZ    . ARG   A 1 406 ? 145.532 113.082 111.386 1.00 54.27  ?  406  ARG   A CZ    1 
ATOM   3277  N  NH1   . ARG   A 1 406 ? 144.953 113.248 112.563 1.00 59.34  ?  406  ARG   A NH1   1 
ATOM   3278  N  NH2   . ARG   A 1 406 ? 146.677 113.708 111.130 1.00 57.83  ?  406  ARG   A NH2   1 
ATOM   3279  N  N     . ALA   A 1 407 ? 140.181 112.807 107.505 1.00 60.10  ?  407  ALA   A N     1 
ATOM   3280  C  CA    . ALA   A 1 407 ? 140.394 113.638 106.325 1.00 55.18  ?  407  ALA   A CA    1 
ATOM   3281  C  C     . ALA   A 1 407 ? 139.255 114.630 106.134 1.00 62.23  ?  407  ALA   A C     1 
ATOM   3282  O  O     . ALA   A 1 407 ? 139.478 115.761 105.687 1.00 69.15  ?  407  ALA   A O     1 
ATOM   3283  C  CB    . ALA   A 1 407 ? 140.557 112.760 105.086 1.00 53.77  ?  407  ALA   A CB    1 
ATOM   3284  N  N     . SER   A 1 408 ? 138.029 114.226 106.467 1.00 66.51  ?  408  SER   A N     1 
ATOM   3285  C  CA    . SER   A 1 408 ? 136.886 115.117 106.306 1.00 63.30  ?  408  SER   A CA    1 
ATOM   3286  C  C     . SER   A 1 408 ? 136.919 116.245 107.330 1.00 66.56  ?  408  SER   A C     1 
ATOM   3287  O  O     . SER   A 1 408 ? 136.994 117.425 106.971 1.00 66.87  ?  408  SER   A O     1 
ATOM   3288  C  CB    . SER   A 1 408 ? 135.585 114.320 106.418 1.00 65.14  ?  408  SER   A CB    1 
ATOM   3289  O  OG    . SER   A 1 408 ? 134.561 115.095 107.015 1.00 74.72  ?  408  SER   A OG    1 
ATOM   3290  N  N     . THR   A 1 409 ? 136.867 115.900 108.618 1.00 70.31  ?  409  THR   A N     1 
ATOM   3291  C  CA    . THR   A 1 409 ? 136.817 116.933 109.647 1.00 65.34  ?  409  THR   A CA    1 
ATOM   3292  C  C     . THR   A 1 409 ? 138.179 117.578 109.874 1.00 66.30  ?  409  THR   A C     1 
ATOM   3293  O  O     . THR   A 1 409 ? 138.263 118.786 110.120 1.00 67.21  ?  409  THR   A O     1 
ATOM   3294  C  CB    . THR   A 1 409 ? 136.287 116.351 110.958 1.00 63.33  ?  409  THR   A CB    1 
ATOM   3295  O  OG1   . THR   A 1 409 ? 137.274 115.485 111.531 1.00 75.49  ?  409  THR   A OG1   1 
ATOM   3296  C  CG2   . THR   A 1 409 ? 135.009 115.565 110.714 1.00 63.57  ?  409  THR   A CG2   1 
ATOM   3297  N  N     . GLY   A 1 410 ? 139.253 116.796 109.795 1.00 67.07  ?  410  GLY   A N     1 
ATOM   3298  C  CA    . GLY   A 1 410 ? 140.568 117.282 110.147 1.00 60.61  ?  410  GLY   A CA    1 
ATOM   3299  C  C     . GLY   A 1 410 ? 140.859 117.289 111.629 1.00 71.44  ?  410  GLY   A C     1 
ATOM   3300  O  O     . GLY   A 1 410 ? 141.959 117.689 112.025 1.00 74.38  ?  410  GLY   A O     1 
ATOM   3301  N  N     . ARG   A 1 411 ? 139.912 116.849 112.461 1.00 69.65  ?  411  ARG   A N     1 
ATOM   3302  C  CA    . ARG   A 1 411 ? 140.028 116.948 113.910 1.00 62.03  ?  411  ARG   A CA    1 
ATOM   3303  C  C     . ARG   A 1 411 ? 139.974 115.586 114.591 1.00 64.92  ?  411  ARG   A C     1 
ATOM   3304  O  O     . ARG   A 1 411 ? 139.729 115.511 115.798 1.00 72.16  ?  411  ARG   A O     1 
ATOM   3305  C  CB    . ARG   A 1 411 ? 138.936 117.862 114.466 1.00 64.59  ?  411  ARG   A CB    1 
ATOM   3306  C  CG    . ARG   A 1 411 ? 138.875 119.222 113.798 1.00 66.21  ?  411  ARG   A CG    1 
ATOM   3307  C  CD    . ARG   A 1 411 ? 140.165 119.989 114.002 1.00 64.94  ?  411  ARG   A CD    1 
ATOM   3308  N  NE    . ARG   A 1 411 ? 140.056 120.955 115.088 1.00 73.26  ?  411  ARG   A NE    1 
ATOM   3309  C  CZ    . ARG   A 1 411 ? 140.437 122.222 115.004 1.00 79.87  ?  411  ARG   A CZ    1 
ATOM   3310  N  NH1   . ARG   A 1 411 ? 140.965 122.713 113.895 1.00 77.73  ?  411  ARG   A NH1   1 
ATOM   3311  N  NH2   . ARG   A 1 411 ? 140.290 123.016 116.061 1.00 76.82  ?  411  ARG   A NH2   1 
ATOM   3312  N  N     . ILE   A 1 412 ? 140.186 114.508 113.846 1.00 51.95  ?  412  ILE   A N     1 
ATOM   3313  C  CA    . ILE   A 1 412 ? 140.324 113.174 114.417 1.00 48.19  ?  412  ILE   A CA    1 
ATOM   3314  C  C     . ILE   A 1 412 ? 141.814 112.879 114.495 1.00 52.85  ?  412  ILE   A C     1 
ATOM   3315  O  O     . ILE   A 1 412 ? 142.491 112.768 113.468 1.00 63.17  ?  412  ILE   A O     1 
ATOM   3316  C  CB    . ILE   A 1 412 ? 139.584 112.115 113.590 1.00 50.68  ?  412  ILE   A CB    1 
ATOM   3317  C  CG1   . ILE   A 1 412 ? 138.126 112.524 113.377 1.00 55.96  ?  412  ILE   A CG1   1 
ATOM   3318  C  CG2   . ILE   A 1 412 ? 139.664 110.759 114.270 1.00 44.93  ?  412  ILE   A CG2   1 
ATOM   3319  C  CD1   . ILE   A 1 412 ? 137.284 112.464 114.630 1.00 56.37  ?  412  ILE   A CD1   1 
ATOM   3320  N  N     . TYR   A 1 413 ? 142.330 112.754 115.710 1.00 51.87  ?  413  TYR   A N     1 
ATOM   3321  C  CA    . TYR   A 1 413 ? 143.753 112.576 115.943 1.00 41.14  ?  413  TYR   A CA    1 
ATOM   3322  C  C     . TYR   A 1 413 ? 144.065 111.122 116.268 1.00 47.53  ?  413  TYR   A C     1 
ATOM   3323  O  O     . TYR   A 1 413 ? 143.184 110.321 116.581 1.00 59.74  ?  413  TYR   A O     1 
ATOM   3324  C  CB    . TYR   A 1 413 ? 144.226 113.484 117.077 1.00 41.23  ?  413  TYR   A CB    1 
ATOM   3325  C  CG    . TYR   A 1 413 ? 143.609 114.858 117.067 1.00 53.48  ?  413  TYR   A CG    1 
ATOM   3326  C  CD1   . TYR   A 1 413 ? 143.790 115.717 115.994 1.00 51.64  ?  413  TYR   A CD1   1 
ATOM   3327  C  CD2   . TYR   A 1 413 ? 142.843 115.297 118.133 1.00 61.74  ?  413  TYR   A CD2   1 
ATOM   3328  C  CE1   . TYR   A 1 413 ? 143.223 116.975 115.988 1.00 49.54  ?  413  TYR   A CE1   1 
ATOM   3329  C  CE2   . TYR   A 1 413 ? 142.280 116.548 118.137 1.00 60.18  ?  413  TYR   A CE2   1 
ATOM   3330  C  CZ    . TYR   A 1 413 ? 142.469 117.383 117.064 1.00 52.00  ?  413  TYR   A CZ    1 
ATOM   3331  O  OH    . TYR   A 1 413 ? 141.896 118.631 117.078 1.00 61.12  ?  413  TYR   A OH    1 
ATOM   3332  N  N     . ILE   A 1 414 ? 145.350 110.793 116.203 1.00 50.70  ?  414  ILE   A N     1 
ATOM   3333  C  CA    . ILE   A 1 414 ? 145.845 109.452 116.480 1.00 45.62  ?  414  ILE   A CA    1 
ATOM   3334  C  C     . ILE   A 1 414 ? 146.793 109.527 117.666 1.00 48.58  ?  414  ILE   A C     1 
ATOM   3335  O  O     . ILE   A 1 414 ? 147.591 110.463 117.773 1.00 56.62  ?  414  ILE   A O     1 
ATOM   3336  C  CB    . ILE   A 1 414 ? 146.556 108.847 115.252 1.00 44.25  ?  414  ILE   A CB    1 
ATOM   3337  C  CG1   . ILE   A 1 414 ? 145.688 108.999 114.002 1.00 46.10  ?  414  ILE   A CG1   1 
ATOM   3338  C  CG2   . ILE   A 1 414 ? 146.901 107.389 115.497 1.00 43.34  ?  414  ILE   A CG2   1 
ATOM   3339  C  CD1   . ILE   A 1 414 ? 144.356 108.299 114.097 1.00 50.80  ?  414  ILE   A CD1   1 
ATOM   3340  N  N     . GLN   A 1 415 ? 146.692 108.552 118.566 1.00 56.50  ?  415  GLN   A N     1 
ATOM   3341  C  CA    . GLN   A 1 415 ? 147.635 108.409 119.671 1.00 53.31  ?  415  GLN   A CA    1 
ATOM   3342  C  C     . GLN   A 1 415 ? 148.110 106.964 119.712 1.00 57.30  ?  415  GLN   A C     1 
ATOM   3343  O  O     . GLN   A 1 415 ? 147.319 106.055 119.979 1.00 67.88  ?  415  GLN   A O     1 
ATOM   3344  C  CB    . GLN   A 1 415 ? 147.006 108.814 121.004 1.00 55.55  ?  415  GLN   A CB    1 
ATOM   3345  C  CG    . GLN   A 1 415 ? 148.023 108.974 122.124 1.00 61.43  ?  415  GLN   A CG    1 
ATOM   3346  C  CD    . GLN   A 1 415 ? 147.390 109.000 123.499 1.00 70.21  ?  415  GLN   A CD    1 
ATOM   3347  O  OE1   . GLN   A 1 415 ? 146.169 109.000 123.633 1.00 76.32  ?  415  GLN   A OE1   1 
ATOM   3348  N  NE2   . GLN   A 1 415 ? 148.223 109.017 124.531 1.00 62.30  ?  415  GLN   A NE2   1 
ATOM   3349  N  N     . ASN   A 1 416 ? 149.397 106.755 119.448 1.00 57.01  ?  416  ASN   A N     1 
ATOM   3350  C  CA    . ASN   A 1 416 ? 150.002 105.427 119.517 1.00 47.38  ?  416  ASN   A CA    1 
ATOM   3351  C  C     . ASN   A 1 416 ? 150.402 105.176 120.964 1.00 52.38  ?  416  ASN   A C     1 
ATOM   3352  O  O     . ASN   A 1 416 ? 151.461 105.617 121.415 1.00 62.08  ?  416  ASN   A O     1 
ATOM   3353  C  CB    . ASN   A 1 416 ? 151.194 105.330 118.574 1.00 48.42  ?  416  ASN   A CB    1 
ATOM   3354  C  CG    . ASN   A 1 416 ? 150.812 105.566 117.126 1.00 52.02  ?  416  ASN   A CG    1 
ATOM   3355  O  OD1   . ASN   A 1 416 ? 149.838 105.003 116.630 1.00 61.34  ?  416  ASN   A OD1   1 
ATOM   3356  N  ND2   . ASN   A 1 416 ? 151.577 106.404 116.441 1.00 50.61  ?  416  ASN   A ND2   1 
ATOM   3357  N  N     . VAL   A 1 417 ? 149.541 104.471 121.700 1.00 53.41  ?  417  VAL   A N     1 
ATOM   3358  C  CA    . VAL   A 1 417 ? 149.740 104.308 123.137 1.00 62.51  ?  417  VAL   A CA    1 
ATOM   3359  C  C     . VAL   A 1 417 ? 150.976 103.468 123.430 1.00 61.95  ?  417  VAL   A C     1 
ATOM   3360  O  O     . VAL   A 1 417 ? 151.671 103.701 124.429 1.00 73.81  ?  417  VAL   A O     1 
ATOM   3361  C  CB    . VAL   A 1 417 ? 148.473 103.715 123.780 1.00 61.31  ?  417  VAL   A CB    1 
ATOM   3362  C  CG1   . VAL   A 1 417 ? 147.324 104.697 123.655 1.00 55.67  ?  417  VAL   A CG1   1 
ATOM   3363  C  CG2   . VAL   A 1 417 ? 148.109 102.392 123.128 1.00 64.51  ?  417  VAL   A CG2   1 
ATOM   3364  N  N     . ASP   A 1 418 ? 151.271 102.482 122.580 1.00 59.72  ?  418  ASP   A N     1 
ATOM   3365  C  CA    . ASP   A 1 418 ? 152.460 101.662 122.784 1.00 63.74  ?  418  ASP   A CA    1 
ATOM   3366  C  C     . ASP   A 1 418 ? 153.725 102.506 122.725 1.00 68.43  ?  418  ASP   A C     1 
ATOM   3367  O  O     . ASP   A 1 418 ? 154.621 102.357 123.563 1.00 77.48  ?  418  ASP   A O     1 
ATOM   3368  C  CB    . ASP   A 1 418 ? 152.508 100.543 121.745 1.00 65.94  ?  418  ASP   A CB    1 
ATOM   3369  C  CG    . ASP   A 1 418 ? 152.258 101.043 120.337 1.00 74.92  ?  418  ASP   A CG    1 
ATOM   3370  O  OD1   . ASP   A 1 418 ? 152.022 102.257 120.167 1.00 78.72  ?  418  ASP   A OD1   1 
ATOM   3371  O  OD2   . ASP   A 1 418 ? 152.299 100.221 119.399 1.00 75.01  ?  418  ASP   A OD2   1 
ATOM   3372  N  N     . HIS   A 1 419 ? 153.813 103.405 121.743 1.00 68.11  ?  419  HIS   A N     1 
ATOM   3373  C  CA    . HIS   A 1 419 ? 154.951 104.313 121.675 1.00 62.81  ?  419  HIS   A CA    1 
ATOM   3374  C  C     . HIS   A 1 419 ? 154.919 105.318 122.818 1.00 60.03  ?  419  HIS   A C     1 
ATOM   3375  O  O     . HIS   A 1 419 ? 155.969 105.707 123.341 1.00 68.55  ?  419  HIS   A O     1 
ATOM   3376  C  CB    . HIS   A 1 419 ? 154.969 105.033 120.328 1.00 63.59  ?  419  HIS   A CB    1 
ATOM   3377  C  CG    . HIS   A 1 419 ? 155.277 104.139 119.169 1.00 68.78  ?  419  HIS   A CG    1 
ATOM   3378  N  ND1   . HIS   A 1 419 ? 155.944 102.942 119.310 1.00 68.12  ?  419  HIS   A ND1   1 
ATOM   3379  C  CD2   . HIS   A 1 419 ? 155.012 104.269 117.848 1.00 65.99  ?  419  HIS   A CD2   1 
ATOM   3380  C  CE1   . HIS   A 1 419 ? 156.075 102.371 118.127 1.00 70.10  ?  419  HIS   A CE1   1 
ATOM   3381  N  NE2   . HIS   A 1 419 ? 155.520 103.157 117.222 1.00 72.15  ?  419  HIS   A NE2   1 
ATOM   3382  N  N     . CYS   A 1 420 ? 153.721 105.750 123.217 1.00 63.52  ?  420  CYS   A N     1 
ATOM   3383  C  CA    . CYS   A 1 420 ? 153.590 106.708 124.307 1.00 67.51  ?  420  CYS   A CA    1 
ATOM   3384  C  C     . CYS   A 1 420 ? 154.024 106.131 125.646 1.00 71.57  ?  420  CYS   A C     1 
ATOM   3385  O  O     . CYS   A 1 420 ? 154.376 106.896 126.549 1.00 77.88  ?  420  CYS   A O     1 
ATOM   3386  C  CB    . CYS   A 1 420 ? 152.146 107.202 124.405 1.00 62.00  ?  420  CYS   A CB    1 
ATOM   3387  S  SG    . CYS   A 1 420 ? 151.711 108.495 123.225 1.00 76.50  ?  420  CYS   A SG    1 
ATOM   3388  N  N     . ASN   A 1 421 ? 154.006 104.808 125.801 1.00 64.35  ?  421  ASN   A N     1 
ATOM   3389  C  CA    . ASN   A 1 421 ? 154.355 104.188 127.072 1.00 59.52  ?  421  ASN   A CA    1 
ATOM   3390  C  C     . ASN   A 1 421 ? 155.715 103.506 127.082 1.00 62.35  ?  421  ASN   A C     1 
ATOM   3391  O  O     . ASN   A 1 421 ? 156.382 103.518 128.118 1.00 76.04  ?  421  ASN   A O     1 
ATOM   3392  C  CB    . ASN   A 1 421 ? 153.285 103.170 127.477 1.00 53.53  ?  421  ASN   A CB    1 
ATOM   3393  C  CG    . ASN   A 1 421 ? 152.053 103.828 128.064 1.00 61.07  ?  421  ASN   A CG    1 
ATOM   3394  O  OD1   . ASN   A 1 421 ? 151.955 104.018 129.275 1.00 69.10  ?  421  ASN   A OD1   1 
ATOM   3395  N  ND2   . ASN   A 1 421 ? 151.104 104.180 127.207 1.00 60.88  ?  421  ASN   A ND2   1 
ATOM   3396  N  N     . THR   A 1 422 ? 156.144 102.907 125.970 1.00 62.65  ?  422  THR   A N     1 
ATOM   3397  C  CA    . THR   A 1 422 ? 157.462 102.278 125.945 1.00 65.31  ?  422  THR   A CA    1 
ATOM   3398  C  C     . THR   A 1 422 ? 158.572 103.322 125.929 1.00 67.04  ?  422  THR   A C     1 
ATOM   3399  O  O     . THR   A 1 422 ? 159.563 103.194 126.657 1.00 66.74  ?  422  THR   A O     1 
ATOM   3400  C  CB    . THR   A 1 422 ? 157.584 101.347 124.739 1.00 65.16  ?  422  THR   A CB    1 
ATOM   3401  O  OG1   . THR   A 1 422 ? 157.254 102.064 123.543 1.00 72.25  ?  422  THR   A OG1   1 
ATOM   3402  C  CG2   . THR   A 1 422 ? 156.648 100.159 124.887 1.00 61.90  ?  422  THR   A CG2   1 
ATOM   3403  N  N     . HIS   A 1 423 ? 158.428 104.356 125.103 1.00 66.65  ?  423  HIS   A N     1 
ATOM   3404  C  CA    . HIS   A 1 423 ? 159.390 105.455 125.056 1.00 63.76  ?  423  HIS   A CA    1 
ATOM   3405  C  C     . HIS   A 1 423 ? 158.869 106.623 125.892 1.00 64.01  ?  423  HIS   A C     1 
ATOM   3406  O  O     . HIS   A 1 423 ? 158.541 107.699 125.393 1.00 71.32  ?  423  HIS   A O     1 
ATOM   3407  C  CB    . HIS   A 1 423 ? 159.654 105.866 123.611 1.00 69.24  ?  423  HIS   A CB    1 
ATOM   3408  C  CG    . HIS   A 1 423 ? 160.680 106.946 123.467 1.00 69.34  ?  423  HIS   A CG    1 
ATOM   3409  N  ND1   . HIS   A 1 423 ? 161.883 106.924 124.138 1.00 69.71  ?  423  HIS   A ND1   1 
ATOM   3410  C  CD2   . HIS   A 1 423 ? 160.680 108.082 122.732 1.00 66.61  ?  423  HIS   A CD2   1 
ATOM   3411  C  CE1   . HIS   A 1 423 ? 162.581 107.999 123.821 1.00 72.49  ?  423  HIS   A CE1   1 
ATOM   3412  N  NE2   . HIS   A 1 423 ? 161.873 108.719 122.970 1.00 70.21  ?  423  HIS   A NE2   1 
ATOM   3413  N  N     . SER   A 1 424 ? 158.795 106.386 127.196 1.00 68.41  ?  424  SER   A N     1 
ATOM   3414  C  CA    . SER   A 1 424 ? 158.250 107.367 128.117 1.00 70.67  ?  424  SER   A CA    1 
ATOM   3415  C  C     . SER   A 1 424 ? 159.164 107.526 129.320 1.00 72.18  ?  424  SER   A C     1 
ATOM   3416  O  O     . SER   A 1 424 ? 159.835 106.573 129.728 1.00 77.09  ?  424  SER   A O     1 
ATOM   3417  C  CB    . SER   A 1 424 ? 156.849 106.954 128.590 1.00 67.16  ?  424  SER   A CB    1 
ATOM   3418  O  OG    . SER   A 1 424 ? 156.386 107.792 129.633 1.00 72.73  ?  424  SER   A OG    1 
ATOM   3419  N  N     . PRO   A 1 425 ? 159.215 108.726 129.906 1.00 70.91  ?  425  PRO   A N     1 
ATOM   3420  C  CA    . PRO   A 1 425 ? 159.963 108.899 131.159 1.00 71.67  ?  425  PRO   A CA    1 
ATOM   3421  C  C     . PRO   A 1 425 ? 159.314 108.221 132.351 1.00 77.08  ?  425  PRO   A C     1 
ATOM   3422  O  O     . PRO   A 1 425 ? 159.961 108.107 133.399 1.00 80.37  ?  425  PRO   A O     1 
ATOM   3423  C  CB    . PRO   A 1 425 ? 159.998 110.421 131.340 1.00 65.28  ?  425  PRO   A CB    1 
ATOM   3424  C  CG    . PRO   A 1 425 ? 158.822 110.918 130.579 1.00 67.17  ?  425  PRO   A CG    1 
ATOM   3425  C  CD    . PRO   A 1 425 ? 158.678 110.001 129.402 1.00 73.33  ?  425  PRO   A CD    1 
ATOM   3426  N  N     . PHE   A 1 426 ? 158.072 107.767 132.228 1.00 69.29  ?  426  PHE   A N     1 
ATOM   3427  C  CA    . PHE   A 1 426 ? 157.343 107.148 133.323 1.00 61.88  ?  426  PHE   A CA    1 
ATOM   3428  C  C     . PHE   A 1 426 ? 157.308 105.634 133.166 1.00 69.21  ?  426  PHE   A C     1 
ATOM   3429  O  O     . PHE   A 1 426 ? 157.421 105.093 132.064 1.00 78.82  ?  426  PHE   A O     1 
ATOM   3430  C  CB    . PHE   A 1 426 ? 155.916 107.693 133.398 1.00 62.94  ?  426  PHE   A CB    1 
ATOM   3431  C  CG    . PHE   A 1 426 ? 155.846 109.175 133.594 1.00 68.08  ?  426  PHE   A CG    1 
ATOM   3432  C  CD1   . PHE   A 1 426 ? 156.058 109.732 134.842 1.00 68.23  ?  426  PHE   A CD1   1 
ATOM   3433  C  CD2   . PHE   A 1 426 ? 155.571 110.013 132.529 1.00 65.81  ?  426  PHE   A CD2   1 
ATOM   3434  C  CE1   . PHE   A 1 426 ? 155.997 111.095 135.024 1.00 68.45  ?  426  PHE   A CE1   1 
ATOM   3435  C  CE2   . PHE   A 1 426 ? 155.507 111.376 132.706 1.00 68.01  ?  426  PHE   A CE2   1 
ATOM   3436  C  CZ    . PHE   A 1 426 ? 155.721 111.919 133.956 1.00 67.47  ?  426  PHE   A CZ    1 
ATOM   3437  N  N     . ASP   A 1 427 ? 157.147 104.952 134.297 1.00 83.69  ?  427  ASP   A N     1 
ATOM   3438  C  CA    . ASP   A 1 427 ? 157.012 103.504 134.304 1.00 84.02  ?  427  ASP   A CA    1 
ATOM   3439  C  C     . ASP   A 1 427 ? 155.555 103.134 134.063 1.00 85.84  ?  427  ASP   A C     1 
ATOM   3440  O  O     . ASP   A 1 427 ? 154.693 103.512 134.868 1.00 81.64  ?  427  ASP   A O     1 
ATOM   3441  C  CB    . ASP   A 1 427 ? 157.488 102.929 135.627 1.00 87.25  ?  427  ASP   A CB    1 
ATOM   3442  C  CG    . ASP   A 1 427 ? 157.308 101.428 135.709 1.00 92.10  ?  427  ASP   A CG    1 
ATOM   3443  O  OD1   . ASP   A 1 427 ? 157.480 100.750 134.675 1.00 92.50  ?  427  ASP   A OD1   1 
ATOM   3444  O  OD2   . ASP   A 1 427 ? 156.996 100.925 136.809 1.00 91.14  ?  427  ASP   A OD2   1 
ATOM   3445  N  N     . PRO   A 1 428 ? 155.234 102.412 132.986 1.00 73.21  ?  428  PRO   A N     1 
ATOM   3446  C  CA    . PRO   A 1 428 ? 153.823 102.103 132.700 1.00 71.90  ?  428  PRO   A CA    1 
ATOM   3447  C  C     . PRO   A 1 428 ? 153.149 101.257 133.764 1.00 75.72  ?  428  PRO   A C     1 
ATOM   3448  O  O     . PRO   A 1 428 ? 151.915 101.258 133.842 1.00 76.93  ?  428  PRO   A O     1 
ATOM   3449  C  CB    . PRO   A 1 428 ? 153.892 101.361 131.358 1.00 70.43  ?  428  PRO   A CB    1 
ATOM   3450  C  CG    . PRO   A 1 428 ? 155.208 101.751 130.767 1.00 70.39  ?  428  PRO   A CG    1 
ATOM   3451  C  CD    . PRO   A 1 428 ? 156.133 101.929 131.926 1.00 69.73  ?  428  PRO   A CD    1 
ATOM   3452  N  N     . ALA   A 1 429 ? 153.914 100.529 134.579 1.00 84.16  ?  429  ALA   A N     1 
ATOM   3453  C  CA    . ALA   A 1 429 ? 153.310 99.692  135.608 1.00 80.33  ?  429  ALA   A CA    1 
ATOM   3454  C  C     . ALA   A 1 429 ? 152.620 100.522 136.681 1.00 85.09  ?  429  ALA   A C     1 
ATOM   3455  O  O     . ALA   A 1 429 ? 151.589 100.101 137.218 1.00 86.53  ?  429  ALA   A O     1 
ATOM   3456  C  CB    . ALA   A 1 429 ? 154.369 98.790  136.240 1.00 76.91  ?  429  ALA   A CB    1 
ATOM   3457  N  N     . ILE   A 1 430 ? 153.172 101.705 136.982 1.00 85.69  ?  430  ILE   A N     1 
ATOM   3458  C  CA    . ILE   A 1 430 ? 152.656 102.551 138.099 1.00 85.20  ?  430  ILE   A CA    1 
ATOM   3459  C  C     . ILE   A 1 430 ? 152.006 103.821 137.553 1.00 85.74  ?  430  ILE   A C     1 
ATOM   3460  O  O     . ILE   A 1 430 ? 150.939 104.191 138.060 1.00 87.94  ?  430  ILE   A O     1 
ATOM   3461  C  CB    . ILE   A 1 430 ? 153.831 102.928 139.021 1.00 83.10  ?  430  ILE   A CB    1 
ATOM   3462  C  CG1   . ILE   A 1 430 ? 154.898 101.833 139.073 1.00 86.90  ?  430  ILE   A CG1   1 
ATOM   3463  C  CG2   . ILE   A 1 430 ? 153.332 103.299 140.407 1.00 81.30  ?  430  ILE   A CG2   1 
ATOM   3464  C  CD1   . ILE   A 1 430 ? 156.181 102.269 139.740 1.00 85.07  ?  430  ILE   A CD1   1 
ATOM   3465  N  N     . ALA   A 1 431 ? 152.625 104.457 136.567 1.00 70.51  ?  431  ALA   A N     1 
ATOM   3466  C  CA    . ALA   A 1 431 ? 152.172 105.742 136.034 1.00 67.61  ?  431  ALA   A CA    1 
ATOM   3467  C  C     . ALA   A 1 431 ? 152.099 105.669 134.514 1.00 70.61  ?  431  ALA   A C     1 
ATOM   3468  O  O     . ALA   A 1 431 ? 152.953 106.216 133.808 1.00 74.86  ?  431  ALA   A O     1 
ATOM   3469  C  CB    . ALA   A 1 431 ? 153.102 106.871 136.481 1.00 63.97  ?  431  ALA   A CB    1 
ATOM   3470  N  N     . PRO   A 1 432 ? 151.085 104.998 133.976 1.00 67.29  ?  432  PRO   A N     1 
ATOM   3471  C  CA    . PRO   A 1 432 ? 150.943 104.916 132.521 1.00 63.01  ?  432  PRO   A CA    1 
ATOM   3472  C  C     . PRO   A 1 432 ? 150.378 106.197 131.928 1.00 63.04  ?  432  PRO   A C     1 
ATOM   3473  O  O     . PRO   A 1 432 ? 149.645 106.946 132.576 1.00 72.41  ?  432  PRO   A O     1 
ATOM   3474  C  CB    . PRO   A 1 432 ? 149.968 103.749 132.334 1.00 60.65  ?  432  PRO   A CB    1 
ATOM   3475  C  CG    . PRO   A 1 432 ? 149.120 103.796 133.554 1.00 62.32  ?  432  PRO   A CG    1 
ATOM   3476  C  CD    . PRO   A 1 432 ? 150.003 104.284 134.677 1.00 64.50  ?  432  PRO   A CD    1 
ATOM   3477  N  N     . VAL   A 1 433 ? 150.734 106.438 130.670 1.00 60.45  ?  433  VAL   A N     1 
ATOM   3478  C  CA    . VAL   A 1 433 ? 150.200 107.562 129.909 1.00 56.01  ?  433  VAL   A CA    1 
ATOM   3479  C  C     . VAL   A 1 433 ? 148.992 107.051 129.131 1.00 60.64  ?  433  VAL   A C     1 
ATOM   3480  O  O     . VAL   A 1 433 ? 149.135 106.285 128.175 1.00 70.79  ?  433  VAL   A O     1 
ATOM   3481  C  CB    . VAL   A 1 433 ? 151.257 108.162 128.975 1.00 59.33  ?  433  VAL   A CB    1 
ATOM   3482  C  CG1   . VAL   A 1 433 ? 150.622 109.164 128.026 1.00 63.32  ?  433  VAL   A CG1   1 
ATOM   3483  C  CG2   . VAL   A 1 433 ? 152.366 108.816 129.783 1.00 62.24  ?  433  VAL   A CG2   1 
ATOM   3484  N  N     . ARG   A 1 434 ? 147.799 107.470 129.546 1.00 57.14  ?  434  ARG   A N     1 
ATOM   3485  C  CA    . ARG   A 1 434 ? 146.556 106.949 128.997 1.00 52.82  ?  434  ARG   A CA    1 
ATOM   3486  C  C     . ARG   A 1 434 ? 145.808 107.957 128.136 1.00 60.38  ?  434  ARG   A C     1 
ATOM   3487  O  O     . ARG   A 1 434 ? 144.696 107.661 127.687 1.00 71.72  ?  434  ARG   A O     1 
ATOM   3488  C  CB    . ARG   A 1 434 ? 145.648 106.461 130.127 1.00 57.82  ?  434  ARG   A CB    1 
ATOM   3489  C  CG    . ARG   A 1 434 ? 146.149 105.219 130.837 1.00 63.43  ?  434  ARG   A CG    1 
ATOM   3490  C  CD    . ARG   A 1 434 ? 144.997 104.405 131.388 1.00 65.30  ?  434  ARG   A CD    1 
ATOM   3491  N  NE    . ARG   A 1 434 ? 145.315 103.815 132.682 1.00 62.33  ?  434  ARG   A NE    1 
ATOM   3492  C  CZ    . ARG   A 1 434 ? 145.257 104.465 133.835 1.00 69.63  ?  434  ARG   A CZ    1 
ATOM   3493  N  NH1   . ARG   A 1 434 ? 144.899 105.737 133.893 1.00 67.49  ?  434  ARG   A NH1   1 
ATOM   3494  N  NH2   . ARG   A 1 434 ? 145.567 103.825 134.958 1.00 71.98  ?  434  ARG   A NH2   1 
ATOM   3495  N  N     . GLN   A 1 435 ? 146.380 109.129 127.890 1.00 57.53  ?  435  GLN   A N     1 
ATOM   3496  C  CA    . GLN   A 1 435 ? 145.702 110.168 127.122 1.00 55.28  ?  435  GLN   A CA    1 
ATOM   3497  C  C     . GLN   A 1 435 ? 146.727 111.227 126.741 1.00 58.74  ?  435  GLN   A C     1 
ATOM   3498  O  O     . GLN   A 1 435 ? 147.926 111.087 127.001 1.00 68.54  ?  435  GLN   A O     1 
ATOM   3499  C  CB    . GLN   A 1 435 ? 144.547 110.785 127.912 1.00 56.07  ?  435  GLN   A CB    1 
ATOM   3500  C  CG    . GLN   A 1 435 ? 144.998 111.639 129.085 1.00 56.02  ?  435  GLN   A CG    1 
ATOM   3501  C  CD    . GLN   A 1 435 ? 143.857 112.394 129.728 1.00 61.40  ?  435  GLN   A CD    1 
ATOM   3502  O  OE1   . GLN   A 1 435 ? 143.304 111.963 130.738 1.00 67.16  ?  435  GLN   A OE1   1 
ATOM   3503  N  NE2   . GLN   A 1 435 ? 143.496 113.529 129.145 1.00 61.08  ?  435  GLN   A NE2   1 
ATOM   3504  N  N     . SER   A 1 436 ? 146.236 112.297 126.119 1.00 52.74  ?  436  SER   A N     1 
ATOM   3505  C  CA    . SER   A 1 436 ? 147.045 113.455 125.781 1.00 54.42  ?  436  SER   A CA    1 
ATOM   3506  C  C     . SER   A 1 436 ? 146.234 114.709 126.079 1.00 57.12  ?  436  SER   A C     1 
ATOM   3507  O  O     . SER   A 1 436 ? 145.114 114.640 126.595 1.00 68.21  ?  436  SER   A O     1 
ATOM   3508  C  CB    . SER   A 1 436 ? 147.495 113.410 124.317 1.00 59.24  ?  436  SER   A CB    1 
ATOM   3509  O  OG    . SER   A 1 436 ? 148.595 114.273 124.101 1.00 67.88  ?  436  SER   A OG    1 
ATOM   3510  N  N     . ASN   A 1 437 ? 146.807 115.864 125.761 1.00 51.50  ?  437  ASN   A N     1 
ATOM   3511  C  CA    . ASN   A 1 437 ? 146.145 117.135 126.008 1.00 53.52  ?  437  ASN   A CA    1 
ATOM   3512  C  C     . ASN   A 1 437 ? 145.337 117.544 124.777 1.00 61.90  ?  437  ASN   A C     1 
ATOM   3513  O  O     . ASN   A 1 437 ? 145.132 116.758 123.849 1.00 63.59  ?  437  ASN   A O     1 
ATOM   3514  C  CB    . ASN   A 1 437 ? 147.167 118.197 126.405 1.00 59.62  ?  437  ASN   A CB    1 
ATOM   3515  C  CG    . ASN   A 1 437 ? 148.001 118.671 125.235 1.00 65.85  ?  437  ASN   A CG    1 
ATOM   3516  O  OD1   . ASN   A 1 437 ? 148.642 117.875 124.552 1.00 73.39  ?  437  ASN   A OD1   1 
ATOM   3517  N  ND2   . ASN   A 1 437 ? 148.000 119.976 124.999 1.00 66.47  ?  437  ASN   A ND2   1 
ATOM   3518  N  N     . LEU   A 1 438 ? 144.861 118.791 124.767 1.00 62.38  ?  438  LEU   A N     1 
ATOM   3519  C  CA    . LEU   A 1 438 ? 144.057 119.274 123.650 1.00 52.46  ?  438  LEU   A CA    1 
ATOM   3520  C  C     . LEU   A 1 438 ? 144.866 119.322 122.359 1.00 56.20  ?  438  LEU   A C     1 
ATOM   3521  O  O     . LEU   A 1 438 ? 144.356 118.982 121.285 1.00 65.07  ?  438  LEU   A O     1 
ATOM   3522  C  CB    . LEU   A 1 438 ? 143.486 120.652 123.982 1.00 55.26  ?  438  LEU   A CB    1 
ATOM   3523  C  CG    . LEU   A 1 438 ? 142.885 121.462 122.833 1.00 59.43  ?  438  LEU   A CG    1 
ATOM   3524  C  CD1   . LEU   A 1 438 ? 141.416 121.132 122.661 1.00 58.71  ?  438  LEU   A CD1   1 
ATOM   3525  C  CD2   . LEU   A 1 438 ? 143.078 122.949 123.073 1.00 58.52  ?  438  LEU   A CD2   1 
ATOM   3526  N  N     . CYS   A 1 439 ? 146.126 119.741 122.442 1.00 66.69  ?  439  CYS   A N     1 
ATOM   3527  C  CA    . CYS   A 1 439 ? 146.987 119.859 121.273 1.00 62.23  ?  439  CYS   A CA    1 
ATOM   3528  C  C     . CYS   A 1 439 ? 147.851 118.628 121.037 1.00 65.27  ?  439  CYS   A C     1 
ATOM   3529  O  O     . CYS   A 1 439 ? 148.672 118.635 120.114 1.00 69.79  ?  439  CYS   A O     1 
ATOM   3530  C  CB    . CYS   A 1 439 ? 147.863 121.086 121.397 1.00 70.44  ?  439  CYS   A CB    1 
ATOM   3531  S  SG    . CYS   A 1 439 ? 146.926 122.552 121.957 1.00 93.75  ?  439  CYS   A SG    1 
ATOM   3532  N  N     . LEU   A 1 440 ? 147.686 117.583 121.849 1.00 61.92  ?  440  LEU   A N     1 
ATOM   3533  C  CA    . LEU   A 1 440 ? 148.345 116.291 121.646 1.00 58.98  ?  440  LEU   A CA    1 
ATOM   3534  C  C     . LEU   A 1 440 ? 149.867 116.406 121.677 1.00 57.99  ?  440  LEU   A C     1 
ATOM   3535  O  O     . LEU   A 1 440 ? 150.572 115.784 120.880 1.00 62.83  ?  440  LEU   A O     1 
ATOM   3536  C  CB    . LEU   A 1 440 ? 147.876 115.632 120.350 1.00 57.62  ?  440  LEU   A CB    1 
ATOM   3537  C  CG    . LEU   A 1 440 ? 146.661 114.731 120.559 1.00 64.45  ?  440  LEU   A CG    1 
ATOM   3538  C  CD1   . LEU   A 1 440 ? 145.387 115.531 120.399 1.00 65.78  ?  440  LEU   A CD1   1 
ATOM   3539  C  CD2   . LEU   A 1 440 ? 146.689 113.556 119.604 1.00 64.58  ?  440  LEU   A CD2   1 
ATOM   3540  N  N     . GLU   A 1 441 ? 150.379 117.204 122.611 1.00 68.02  ?  441  GLU   A N     1 
ATOM   3541  C  CA    . GLU   A 1 441 ? 151.807 117.270 122.872 1.00 64.61  ?  441  GLU   A CA    1 
ATOM   3542  C  C     . GLU   A 1 441 ? 152.176 116.865 124.290 1.00 72.43  ?  441  GLU   A C     1 
ATOM   3543  O  O     . GLU   A 1 441 ? 153.355 116.603 124.552 1.00 81.21  ?  441  GLU   A O     1 
ATOM   3544  C  CB    . GLU   A 1 441 ? 152.340 118.685 122.595 1.00 62.20  ?  441  GLU   A CB    1 
ATOM   3545  C  CG    . GLU   A 1 441 ? 152.399 119.590 123.812 1.00 69.44  ?  441  GLU   A CG    1 
ATOM   3546  C  CD    . GLU   A 1 441 ? 151.198 120.501 123.915 1.00 85.12  ?  441  GLU   A CD    1 
ATOM   3547  O  OE1   . GLU   A 1 441 ? 151.063 121.195 124.943 1.00 87.20  ?  441  GLU   A OE1   1 
ATOM   3548  O  OE2   . GLU   A 1 441 ? 150.385 120.521 122.969 1.00 86.85  ?  441  GLU   A OE2   1 
ATOM   3549  N  N     . ILE   A 1 442 ? 151.211 116.788 125.200 1.00 62.16  ?  442  ILE   A N     1 
ATOM   3550  C  CA    . ILE   A 1 442 ? 151.458 116.464 126.599 1.00 60.97  ?  442  ILE   A CA    1 
ATOM   3551  C  C     . ILE   A 1 442 ? 151.106 115.002 126.828 1.00 66.11  ?  442  ILE   A C     1 
ATOM   3552  O  O     . ILE   A 1 442 ? 149.998 114.563 126.497 1.00 74.13  ?  442  ILE   A O     1 
ATOM   3553  C  CB    . ILE   A 1 442 ? 150.647 117.381 127.529 1.00 62.89  ?  442  ILE   A CB    1 
ATOM   3554  C  CG1   . ILE   A 1 442 ? 151.075 118.836 127.345 1.00 63.45  ?  442  ILE   A CG1   1 
ATOM   3555  C  CG2   . ILE   A 1 442 ? 150.812 116.960 128.972 1.00 64.17  ?  442  ILE   A CG2   1 
ATOM   3556  C  CD1   . ILE   A 1 442 ? 152.531 119.089 127.660 1.00 63.72  ?  442  ILE   A CD1   1 
ATOM   3557  N  N     . ALA   A 1 443 ? 152.050 114.247 127.389 1.00 63.27  ?  443  ALA   A N     1 
ATOM   3558  C  CA    . ALA   A 1 443 ? 151.871 112.825 127.684 1.00 60.90  ?  443  ALA   A CA    1 
ATOM   3559  C  C     . ALA   A 1 443 ? 152.212 112.619 129.157 1.00 64.63  ?  443  ALA   A C     1 
ATOM   3560  O  O     . ALA   A 1 443 ? 153.368 112.365 129.505 1.00 71.53  ?  443  ALA   A O     1 
ATOM   3561  C  CB    . ALA   A 1 443 ? 152.736 111.963 126.773 1.00 57.88  ?  443  ALA   A CB    1 
ATOM   3562  N  N     . LEU   A 1 444 ? 151.205 112.725 130.018 1.00 62.42  ?  444  LEU   A N     1 
ATOM   3563  C  CA    . LEU   A 1 444 ? 151.410 112.662 131.455 1.00 58.74  ?  444  LEU   A CA    1 
ATOM   3564  C  C     . LEU   A 1 444 ? 150.431 111.693 132.095 1.00 60.51  ?  444  LEU   A C     1 
ATOM   3565  O  O     . LEU   A 1 444 ? 149.322 111.495 131.589 1.00 66.14  ?  444  LEU   A O     1 
ATOM   3566  C  CB    . LEU   A 1 444 ? 151.242 114.047 132.094 1.00 54.40  ?  444  LEU   A CB    1 
ATOM   3567  C  CG    . LEU   A 1 444 ? 152.286 115.085 131.692 1.00 54.57  ?  444  LEU   A CG    1 
ATOM   3568  C  CD1   . LEU   A 1 444 ? 152.029 116.402 132.399 1.00 63.50  ?  444  LEU   A CD1   1 
ATOM   3569  C  CD2   . LEU   A 1 444 ? 153.682 114.570 131.984 1.00 57.38  ?  444  LEU   A CD2   1 
ATOM   3570  N  N     . PRO   A 1 445 ? 150.817 111.070 133.206 1.00 61.46  ?  445  PRO   A N     1 
ATOM   3571  C  CA    . PRO   A 1 445 ? 149.881 110.200 133.922 1.00 57.83  ?  445  PRO   A CA    1 
ATOM   3572  C  C     . PRO   A 1 445 ? 148.749 110.996 134.548 1.00 62.84  ?  445  PRO   A C     1 
ATOM   3573  O  O     . PRO   A 1 445 ? 148.923 112.134 134.990 1.00 71.21  ?  445  PRO   A O     1 
ATOM   3574  C  CB    . PRO   A 1 445 ? 150.754 109.539 134.998 1.00 54.82  ?  445  PRO   A CB    1 
ATOM   3575  C  CG    . PRO   A 1 445 ? 152.167 109.798 134.580 1.00 58.94  ?  445  PRO   A CG    1 
ATOM   3576  C  CD    . PRO   A 1 445 ? 152.148 111.082 133.831 1.00 59.71  ?  445  PRO   A CD    1 
ATOM   3577  N  N     . THR   A 1 446 ? 147.575 110.372 134.586 1.00 70.04  ?  446  THR   A N     1 
ATOM   3578  C  CA    . THR   A 1 446 ? 146.404 110.947 135.227 1.00 69.28  ?  446  THR   A CA    1 
ATOM   3579  C  C     . THR   A 1 446 ? 145.675 109.845 135.978 1.00 70.60  ?  446  THR   A C     1 
ATOM   3580  O  O     . THR   A 1 446 ? 145.802 108.661 135.659 1.00 80.51  ?  446  THR   A O     1 
ATOM   3581  C  CB    . THR   A 1 446 ? 145.457 111.611 134.215 1.00 71.90  ?  446  THR   A CB    1 
ATOM   3582  O  OG1   . THR   A 1 446 ? 145.331 110.779 133.056 1.00 80.58  ?  446  THR   A OG1   1 
ATOM   3583  C  CG2   . THR   A 1 446 ? 145.983 112.976 133.800 1.00 64.39  ?  446  THR   A CG2   1 
ATOM   3584  N  N     . LYS   A 1 447 ? 144.914 110.246 136.991 1.00 73.20  ?  447  LYS   A N     1 
ATOM   3585  C  CA    . LYS   A 1 447 ? 144.109 109.302 137.744 1.00 70.56  ?  447  LYS   A CA    1 
ATOM   3586  C  C     . LYS   A 1 447 ? 142.694 109.844 137.893 1.00 76.67  ?  447  LYS   A C     1 
ATOM   3587  O  O     . LYS   A 1 447 ? 142.507 111.045 138.123 1.00 82.13  ?  447  LYS   A O     1 
ATOM   3588  C  CB    . LYS   A 1 447 ? 144.723 109.028 139.124 1.00 69.89  ?  447  LYS   A CB    1 
ATOM   3589  C  CG    . LYS   A 1 447 ? 146.062 108.312 139.057 1.00 76.71  ?  447  LYS   A CG    1 
ATOM   3590  C  CD    . LYS   A 1 447 ? 146.537 107.879 140.430 1.00 80.07  ?  447  LYS   A CD    1 
ATOM   3591  C  CE    . LYS   A 1 447 ? 146.894 109.078 141.287 1.00 85.39  ?  447  LYS   A CE    1 
ATOM   3592  N  NZ    . LYS   A 1 447 ? 148.093 109.794 140.769 1.00 85.65  ?  447  LYS   A NZ    1 
ATOM   3593  N  N     . PRO   A 1 448 ? 141.683 108.988 137.757 1.00 73.31  ?  448  PRO   A N     1 
ATOM   3594  C  CA    . PRO   A 1 448 ? 140.298 109.470 137.794 1.00 70.04  ?  448  PRO   A CA    1 
ATOM   3595  C  C     . PRO   A 1 448 ? 139.937 110.058 139.149 1.00 76.29  ?  448  PRO   A C     1 
ATOM   3596  O  O     . PRO   A 1 448 ? 140.466 109.663 140.189 1.00 80.56  ?  448  PRO   A O     1 
ATOM   3597  C  CB    . PRO   A 1 448 ? 139.474 108.213 137.491 1.00 66.47  ?  448  PRO   A CB    1 
ATOM   3598  C  CG    . PRO   A 1 448 ? 140.382 107.071 137.809 1.00 74.95  ?  448  PRO   A CG    1 
ATOM   3599  C  CD    . PRO   A 1 448 ? 141.760 107.545 137.483 1.00 71.96  ?  448  PRO   A CD    1 
ATOM   3600  N  N     . LEU   A 1 449 ? 139.021 111.021 139.119 1.00 81.93  ?  449  LEU   A N     1 
ATOM   3601  C  CA    . LEU   A 1 449 ? 138.548 111.705 140.313 1.00 77.56  ?  449  LEU   A CA    1 
ATOM   3602  C  C     . LEU   A 1 449 ? 137.162 111.190 140.673 1.00 80.35  ?  449  LEU   A C     1 
ATOM   3603  O  O     . LEU   A 1 449 ? 136.255 111.210 139.837 1.00 87.15  ?  449  LEU   A O     1 
ATOM   3604  C  CB    . LEU   A 1 449 ? 138.495 113.216 140.085 1.00 76.06  ?  449  LEU   A CB    1 
ATOM   3605  C  CG    . LEU   A 1 449 ? 139.776 114.037 140.225 1.00 78.67  ?  449  LEU   A CG    1 
ATOM   3606  C  CD1   . LEU   A 1 449 ? 140.621 113.933 138.969 1.00 82.42  ?  449  LEU   A CD1   1 
ATOM   3607  C  CD2   . LEU   A 1 449 ? 139.431 115.487 140.516 1.00 78.37  ?  449  LEU   A CD2   1 
ATOM   3608  N  N     . ASN   A 1 450 ? 137.001 110.728 141.911 1.00 90.54  ?  450  ASN   A N     1 
ATOM   3609  C  CA    A ASN   A 1 450 ? 135.680 110.372 142.410 0.50 92.66  ?  450  ASN   A CA    1 
ATOM   3610  C  CA    B ASN   A 1 450 ? 135.780 110.372 142.410 0.50 92.66  ?  450  ASN   A CA    1 
ATOM   3611  C  C     . ASN   A 1 450 ? 134.941 111.565 142.999 1.00 94.44  ?  450  ASN   A C     1 
ATOM   3612  O  O     . ASN   A 1 450 ? 133.761 111.438 143.341 1.00 92.72  ?  450  ASN   A O     1 
ATOM   3613  C  CB    A ASN   A 1 450 ? 135.783 109.257 143.458 0.50 93.92  ?  450  ASN   A CB    1 
ATOM   3614  C  CB    B ASN   A 1 450 ? 135.883 109.257 143.458 0.50 93.92  ?  450  ASN   A CB    1 
ATOM   3615  C  CG    A ASN   A 1 450 ? 136.141 109.779 144.833 0.50 100.87 ?  450  ASN   A CG    1 
ATOM   3616  C  CG    B ASN   A 1 450 ? 136.249 107.919 142.853 0.50 100.87 ?  450  ASN   A CG    1 
ATOM   3617  O  OD1   A ASN   A 1 450 ? 137.312 109.979 145.145 0.50 98.24  ?  450  ASN   A OD1   1 
ATOM   3618  O  OD1   B ASN   A 1 450 ? 136.029 107.682 141.668 0.50 98.24  ?  450  ASN   A OD1   1 
ATOM   3619  N  ND2   A ASN   A 1 450 ? 135.130 110.001 145.665 0.50 101.06 ?  450  ASN   A ND2   1 
ATOM   3620  N  ND2   B ASN   A 1 450 ? 136.810 107.033 143.668 0.50 101.06 ?  450  ASN   A ND2   1 
ATOM   3621  N  N     . ASP   A 1 451 ? 135.607 112.710 143.123 1.00 95.80  ?  451  ASP   A N     1 
ATOM   3622  C  CA    . ASP   A 1 451 ? 134.984 113.949 143.563 1.00 93.58  ?  451  ASP   A CA    1 
ATOM   3623  C  C     . ASP   A 1 451 ? 135.834 115.103 143.056 1.00 97.22  ?  451  ASP   A C     1 
ATOM   3624  O  O     . ASP   A 1 451 ? 137.033 114.950 142.814 1.00 103.69 ?  451  ASP   A O     1 
ATOM   3625  C  CB    . ASP   A 1 451 ? 134.846 114.005 145.087 1.00 95.78  ?  451  ASP   A CB    1 
ATOM   3626  C  CG    . ASP   A 1 451 ? 133.740 114.936 145.537 1.00 103.43 ?  451  ASP   A CG    1 
ATOM   3627  O  OD1   . ASP   A 1 451 ? 132.555 114.593 145.338 1.00 106.31 ?  451  ASP   A OD1   1 
ATOM   3628  O  OD2   . ASP   A 1 451 ? 134.052 116.012 146.089 1.00 101.21 ?  451  ASP   A OD2   1 
ATOM   3629  N  N     . VAL   A 1 452 ? 135.198 116.267 142.898 1.00 80.90  ?  452  VAL   A N     1 
ATOM   3630  C  CA    . VAL   A 1 452 ? 135.921 117.431 142.397 1.00 79.78  ?  452  VAL   A CA    1 
ATOM   3631  C  C     . VAL   A 1 452 ? 136.945 117.932 143.408 1.00 82.18  ?  452  VAL   A C     1 
ATOM   3632  O  O     . VAL   A 1 452 ? 137.895 118.627 143.031 1.00 86.35  ?  452  VAL   A O     1 
ATOM   3633  C  CB    . VAL   A 1 452 ? 134.938 118.550 141.999 1.00 81.08  ?  452  VAL   A CB    1 
ATOM   3634  C  CG1   . VAL   A 1 452 ? 134.448 119.304 143.225 1.00 81.91  ?  452  VAL   A CG1   1 
ATOM   3635  C  CG2   . VAL   A 1 452 ? 135.587 119.497 141.000 1.00 79.82  ?  452  VAL   A CG2   1 
ATOM   3636  N  N     . ASN   A 1 453 ? 136.783 117.590 144.687 1.00 85.81  ?  453  ASN   A N     1 
ATOM   3637  C  CA    . ASN   A 1 453 ? 137.745 117.936 145.724 1.00 86.68  ?  453  ASN   A CA    1 
ATOM   3638  C  C     . ASN   A 1 453 ? 138.485 116.710 146.248 1.00 89.10  ?  453  ASN   A C     1 
ATOM   3639  O  O     . ASN   A 1 453 ? 139.032 116.744 147.355 1.00 92.78  ?  453  ASN   A O     1 
ATOM   3640  C  CB    . ASN   A 1 453 ? 137.048 118.670 146.870 1.00 86.20  ?  453  ASN   A CB    1 
ATOM   3641  C  CG    . ASN   A 1 453 ? 136.458 119.996 146.437 1.00 88.58  ?  453  ASN   A CG    1 
ATOM   3642  O  OD1   . ASN   A 1 453 ? 135.255 120.223 146.558 1.00 94.93  ?  453  ASN   A OD1   1 
ATOM   3643  N  ND2   . ASN   A 1 453 ? 137.305 120.882 145.926 1.00 84.68  ?  453  ASN   A ND2   1 
ATOM   3644  N  N     . ASP   A 1 454 ? 138.506 115.629 145.474 1.00 101.04 ?  454  ASP   A N     1 
ATOM   3645  C  CA    . ASP   A 1 454 ? 139.187 114.412 145.890 1.00 99.46  ?  454  ASP   A CA    1 
ATOM   3646  C  C     . ASP   A 1 454 ? 140.691 114.637 145.963 1.00 103.91 ?  454  ASP   A C     1 
ATOM   3647  O  O     . ASP   A 1 454 ? 141.277 115.320 145.119 1.00 105.67 ?  454  ASP   A O     1 
ATOM   3648  C  CB    . ASP   A 1 454 ? 138.872 113.274 144.919 1.00 99.66  ?  454  ASP   A CB    1 
ATOM   3649  C  CG    . ASP   A 1 454 ? 139.658 112.011 145.219 1.00 105.34 ?  454  ASP   A CG    1 
ATOM   3650  O  OD1   . ASP   A 1 454 ? 140.029 111.796 146.392 1.00 105.42 ?  454  ASP   A OD1   1 
ATOM   3651  O  OD2   . ASP   A 1 454 ? 139.900 111.228 144.277 1.00 105.34 ?  454  ASP   A OD2   1 
ATOM   3652  N  N     . GLU   A 1 455 ? 141.317 114.052 146.982 1.00 104.32 ?  455  GLU   A N     1 
ATOM   3653  C  CA    . GLU   A 1 455 ? 142.757 114.137 147.172 1.00 102.53 ?  455  GLU   A CA    1 
ATOM   3654  C  C     . GLU   A 1 455 ? 143.488 112.905 146.657 1.00 102.48 ?  455  GLU   A C     1 
ATOM   3655  O  O     . GLU   A 1 455 ? 144.681 112.745 146.930 1.00 105.24 ?  455  GLU   A O     1 
ATOM   3656  C  CB    . GLU   A 1 455 ? 143.081 114.361 148.650 1.00 103.17 ?  455  GLU   A CB    1 
ATOM   3657  C  CG    . GLU   A 1 455 ? 142.456 115.615 149.236 1.00 106.00 ?  455  GLU   A CG    1 
ATOM   3658  C  CD    . GLU   A 1 455 ? 143.305 116.851 149.009 1.00 109.65 ?  455  GLU   A CD    1 
ATOM   3659  O  OE1   . GLU   A 1 455 ? 144.414 116.718 148.450 1.00 110.88 ?  455  GLU   A OE1   1 
ATOM   3660  O  OE2   . GLU   A 1 455 ? 142.862 117.955 149.389 1.00 109.08 ?  455  GLU   A OE2   1 
ATOM   3661  N  N     . ASN   A 1 456 ? 142.797 112.025 145.929 1.00 94.62  ?  456  ASN   A N     1 
ATOM   3662  C  CA    . ASN   A 1 456 ? 143.420 110.848 145.343 1.00 93.89  ?  456  ASN   A CA    1 
ATOM   3663  C  C     . ASN   A 1 456 ? 143.557 110.920 143.830 1.00 94.81  ?  456  ASN   A C     1 
ATOM   3664  O  O     . ASN   A 1 456 ? 144.421 110.235 143.274 1.00 96.95  ?  456  ASN   A O     1 
ATOM   3665  C  CB    . ASN   A 1 456 ? 142.626 109.586 145.709 1.00 95.81  ?  456  ASN   A CB    1 
ATOM   3666  C  CG    . ASN   A 1 456 ? 143.172 108.893 146.940 1.00 100.14 ?  456  ASN   A CG    1 
ATOM   3667  O  OD1   . ASN   A 1 456 ? 144.005 109.445 147.659 1.00 100.09 ?  456  ASN   A OD1   1 
ATOM   3668  N  ND2   . ASN   A 1 456 ? 142.704 107.676 147.191 1.00 98.36  ?  456  ASN   A ND2   1 
ATOM   3669  N  N     . GLY   A 1 457 ? 142.733 111.721 143.155 1.00 85.40  ?  457  GLY   A N     1 
ATOM   3670  C  CA    . GLY   A 1 457 ? 142.871 111.881 141.726 1.00 80.35  ?  457  GLY   A CA    1 
ATOM   3671  C  C     . GLY   A 1 457 ? 144.049 112.759 141.354 1.00 81.30  ?  457  GLY   A C     1 
ATOM   3672  O  O     . GLY   A 1 457 ? 144.613 113.478 142.177 1.00 86.12  ?  457  GLY   A O     1 
ATOM   3673  N  N     . GLU   A 1 458 ? 144.428 112.691 140.081 1.00 78.76  ?  458  GLU   A N     1 
ATOM   3674  C  CA    . GLU   A 1 458 ? 145.537 113.476 139.557 1.00 76.50  ?  458  GLU   A CA    1 
ATOM   3675  C  C     . GLU   A 1 458 ? 145.120 114.131 138.251 1.00 77.84  ?  458  GLU   A C     1 
ATOM   3676  O  O     . GLU   A 1 458 ? 144.602 113.461 137.353 1.00 82.02  ?  458  GLU   A O     1 
ATOM   3677  C  CB    . GLU   A 1 458 ? 146.780 112.606 139.343 1.00 76.73  ?  458  GLU   A CB    1 
ATOM   3678  C  CG    . GLU   A 1 458 ? 147.980 113.369 138.810 1.00 82.20  ?  458  GLU   A CG    1 
ATOM   3679  C  CD    . GLU   A 1 458 ? 149.112 112.456 138.386 1.00 89.75  ?  458  GLU   A CD    1 
ATOM   3680  O  OE1   . GLU   A 1 458 ? 149.046 111.247 138.688 1.00 89.01  ?  458  GLU   A OE1   1 
ATOM   3681  O  OE2   . GLU   A 1 458 ? 150.068 112.948 137.751 1.00 90.19  ?  458  GLU   A OE2   1 
ATOM   3682  N  N     . ILE   A 1 459 ? 145.346 115.438 138.151 1.00 63.43  ?  459  ILE   A N     1 
ATOM   3683  C  CA    . ILE   A 1 459 ? 145.086 116.205 136.940 1.00 57.16  ?  459  ILE   A CA    1 
ATOM   3684  C  C     . ILE   A 1 459 ? 146.405 116.808 136.482 1.00 66.58  ?  459  ILE   A C     1 
ATOM   3685  O  O     . ILE   A 1 459 ? 147.097 117.466 137.267 1.00 76.93  ?  459  ILE   A O     1 
ATOM   3686  C  CB    . ILE   A 1 459 ? 144.028 117.300 137.174 1.00 57.12  ?  459  ILE   A CB    1 
ATOM   3687  C  CG1   . ILE   A 1 459 ? 142.629 116.686 137.217 1.00 60.81  ?  459  ILE   A CG1   1 
ATOM   3688  C  CG2   . ILE   A 1 459 ? 144.106 118.364 136.093 1.00 58.87  ?  459  ILE   A CG2   1 
ATOM   3689  C  CD1   . ILE   A 1 459 ? 141.581 117.594 137.814 1.00 64.52  ?  459  ILE   A CD1   1 
ATOM   3690  N  N     . ALA   A 1 460 ? 146.753 116.581 135.219 1.00 55.80  ?  460  ALA   A N     1 
ATOM   3691  C  CA    . ALA   A 1 460 ? 148.037 117.010 134.683 1.00 53.95  ?  460  ALA   A CA    1 
ATOM   3692  C  C     . ALA   A 1 460 ? 147.923 118.406 134.086 1.00 59.93  ?  460  ALA   A C     1 
ATOM   3693  O  O     . ALA   A 1 460 ? 146.979 118.697 133.345 1.00 68.27  ?  460  ALA   A O     1 
ATOM   3694  C  CB    . ALA   A 1 460 ? 148.531 116.022 133.627 1.00 52.81  ?  460  ALA   A CB    1 
ATOM   3695  N  N     . LEU   A 1 461 ? 148.887 119.262 134.409 1.00 64.83  ?  461  LEU   A N     1 
ATOM   3696  C  CA    . LEU   A 1 461 ? 148.944 120.610 133.869 1.00 60.20  ?  461  LEU   A CA    1 
ATOM   3697  C  C     . LEU   A 1 461 ? 149.821 120.637 132.619 1.00 65.05  ?  461  LEU   A C     1 
ATOM   3698  O  O     . LEU   A 1 461 ? 150.543 119.687 132.314 1.00 68.19  ?  461  LEU   A O     1 
ATOM   3699  C  CB    . LEU   A 1 461 ? 149.457 121.591 134.924 1.00 62.18  ?  461  LEU   A CB    1 
ATOM   3700  C  CG    . LEU   A 1 461 ? 148.466 121.962 136.031 1.00 66.48  ?  461  LEU   A CG    1 
ATOM   3701  C  CD1   . LEU   A 1 461 ? 147.060 122.115 135.474 1.00 62.66  ?  461  LEU   A CD1   1 
ATOM   3702  C  CD2   . LEU   A 1 461 ? 148.493 120.937 137.156 1.00 74.19  ?  461  LEU   A CD2   1 
ATOM   3703  N  N     . CYS   A 1 462 ? 149.751 121.750 131.889 1.00 82.74  ?  462  CYS   A N     1 
ATOM   3704  C  CA    . CYS   A 1 462 ? 150.410 121.869 130.590 1.00 85.29  ?  462  CYS   A CA    1 
ATOM   3705  C  C     . CYS   A 1 462 ? 151.030 123.084 131.284 1.00 86.98  ?  462  CYS   A C     1 
ATOM   3706  O  O     . CYS   A 1 462 ? 150.313 123.969 131.758 1.00 95.48  ?  462  CYS   A O     1 
ATOM   3707  C  CB    . CYS   A 1 462 ? 149.527 122.697 129.647 1.00 86.24  ?  462  CYS   A CB    1 
ATOM   3708  S  SG    . CYS   A 1 462 ? 149.402 122.078 127.948 1.00 86.21  ?  462  CYS   A SG    1 
ATOM   3709  N  N     . THR   A 1 463 ? 152.363 123.126 131.359 1.00 76.62  ?  463  THR   A N     1 
ATOM   3710  C  CA    . THR   A 1 463 ? 153.133 124.334 131.700 1.00 76.06  ?  463  THR   A CA    1 
ATOM   3711  C  C     . THR   A 1 463 ? 154.269 124.296 130.668 1.00 76.29  ?  463  THR   A C     1 
ATOM   3712  O  O     . THR   A 1 463 ? 155.257 123.580 130.821 1.00 74.82  ?  463  THR   A O     1 
ATOM   3713  C  CB    . THR   A 1 463 ? 153.579 123.664 133.005 1.00 75.46  ?  463  THR   A CB    1 
ATOM   3714  O  OG1   . THR   A 1 463 ? 154.252 124.620 133.835 1.00 78.49  ?  463  THR   A OG1   1 
ATOM   3715  C  CG2   . THR   A 1 463 ? 154.514 122.497 132.720 1.00 72.05  ?  463  THR   A CG2   1 
ATOM   3716  N  N     . LEU   A 1 464 ? 154.115 125.081 129.605 1.00 79.89  ?  464  LEU   A N     1 
ATOM   3717  C  CA    . LEU   A 1 464 ? 155.071 125.046 128.504 1.00 78.69  ?  464  LEU   A CA    1 
ATOM   3718  C  C     . LEU   A 1 464 ? 156.062 126.201 128.545 1.00 77.75  ?  464  LEU   A C     1 
ATOM   3719  O  O     . LEU   A 1 464 ? 155.872 127.211 129.225 1.00 81.68  ?  464  LEU   A O     1 
ATOM   3720  C  CB    . LEU   A 1 464 ? 154.377 125.082 127.140 1.00 77.83  ?  464  LEU   A CB    1 
ATOM   3721  C  CG    . LEU   A 1 464 ? 153.384 124.017 126.701 1.00 83.52  ?  464  LEU   A CG    1 
ATOM   3722  C  CD1   . LEU   A 1 464 ? 153.962 122.608 126.788 1.00 81.65  ?  464  LEU   A CD1   1 
ATOM   3723  C  CD2   . LEU   A 1 464 ? 152.141 124.175 127.523 1.00 83.05  ?  464  LEU   A CD2   1 
ATOM   3724  N  N     . SER   A 1 465 ? 157.131 126.022 127.773 1.00 77.43  ?  465  SER   A N     1 
ATOM   3725  C  CA    . SER   A 1 465 ? 158.056 127.073 127.381 1.00 75.41  ?  465  SER   A CA    1 
ATOM   3726  C  C     . SER   A 1 465 ? 158.663 126.655 126.047 1.00 74.91  ?  465  SER   A C     1 
ATOM   3727  O  O     . SER   A 1 465 ? 158.351 125.586 125.515 1.00 86.14  ?  465  SER   A O     1 
ATOM   3728  C  CB    . SER   A 1 465 ? 159.122 127.313 128.451 1.00 77.07  ?  465  SER   A CB    1 
ATOM   3729  O  OG    . SER   A 1 465 ? 159.825 128.519 128.206 1.00 80.30  ?  465  SER   A OG    1 
ATOM   3730  N  N     . ALA   A 1 466 ? 159.533 127.498 125.497 1.00 59.99  ?  466  ALA   A N     1 
ATOM   3731  C  CA    . ALA   A 1 466 ? 160.096 127.204 124.188 1.00 64.10  ?  466  ALA   A CA    1 
ATOM   3732  C  C     . ALA   A 1 466 ? 161.477 127.826 124.054 1.00 66.72  ?  466  ALA   A C     1 
ATOM   3733  O  O     . ALA   A 1 466 ? 161.743 128.910 124.579 1.00 70.84  ?  466  ALA   A O     1 
ATOM   3734  C  CB    . ALA   A 1 466 ? 159.186 127.706 123.061 1.00 67.10  ?  466  ALA   A CB    1 
ATOM   3735  N  N     . PHE   A 1 467 ? 162.348 127.125 123.335 1.00 75.68  ?  467  PHE   A N     1 
ATOM   3736  C  CA    . PHE   A 1 467 ? 163.652 127.640 122.943 1.00 68.73  ?  467  PHE   A CA    1 
ATOM   3737  C  C     . PHE   A 1 467 ? 163.557 128.196 121.530 1.00 71.99  ?  467  PHE   A C     1 
ATOM   3738  O  O     . PHE   A 1 467 ? 162.994 127.549 120.641 1.00 75.66  ?  467  PHE   A O     1 
ATOM   3739  C  CB    . PHE   A 1 467 ? 164.721 126.549 123.000 1.00 64.30  ?  467  PHE   A CB    1 
ATOM   3740  C  CG    . PHE   A 1 467 ? 165.127 126.166 124.389 1.00 68.97  ?  467  PHE   A CG    1 
ATOM   3741  C  CD1   . PHE   A 1 467 ? 165.504 127.130 125.306 1.00 76.36  ?  467  PHE   A CD1   1 
ATOM   3742  C  CD2   . PHE   A 1 467 ? 165.143 124.838 124.776 1.00 70.29  ?  467  PHE   A CD2   1 
ATOM   3743  C  CE1   . PHE   A 1 467 ? 165.882 126.777 126.585 1.00 78.79  ?  467  PHE   A CE1   1 
ATOM   3744  C  CE2   . PHE   A 1 467 ? 165.520 124.479 126.052 1.00 73.60  ?  467  PHE   A CE2   1 
ATOM   3745  C  CZ    . PHE   A 1 467 ? 165.889 125.449 126.958 1.00 75.10  ?  467  PHE   A CZ    1 
ATOM   3746  N  N     . ASN   A 1 468 ? 164.100 129.390 121.329 1.00 75.72  ?  468  ASN   A N     1 
ATOM   3747  C  CA    . ASN   A 1 468 ? 164.149 130.004 120.015 1.00 75.10  ?  468  ASN   A CA    1 
ATOM   3748  C  C     . ASN   A 1 468 ? 165.402 129.545 119.309 1.00 79.49  ?  468  ASN   A C     1 
ATOM   3749  O  O     . ASN   A 1 468 ? 166.487 130.076 119.552 1.00 82.86  ?  468  ASN   A O     1 
ATOM   3750  C  CB    . ASN   A 1 468 ? 164.104 131.536 120.141 1.00 75.31  ?  468  ASN   A CB    1 
ATOM   3751  C  CG    . ASN   A 1 468 ? 163.994 132.235 118.775 1.00 80.03  ?  468  ASN   A CG    1 
ATOM   3752  O  OD1   . ASN   A 1 468 ? 163.975 131.582 117.731 1.00 85.00  ?  468  ASN   A OD1   1 
ATOM   3753  N  ND2   . ASN   A 1 468 ? 163.891 133.548 118.802 1.00 80.76  ?  468  ASN   A ND2   1 
ATOM   3754  N  N     . LEU   A 1 469 ? 165.263 128.540 118.442 1.00 78.53  ?  469  LEU   A N     1 
ATOM   3755  C  CA    . LEU   A 1 469 ? 166.422 128.016 117.729 1.00 77.04  ?  469  LEU   A CA    1 
ATOM   3756  C  C     . LEU   A 1 469 ? 166.994 129.037 116.756 1.00 82.97  ?  469  LEU   A C     1 
ATOM   3757  O  O     . LEU   A 1 469 ? 168.184 128.977 116.427 1.00 82.89  ?  469  LEU   A O     1 
ATOM   3758  C  CB    . LEU   A 1 469 ? 166.049 126.732 116.990 1.00 80.00  ?  469  LEU   A CB    1 
ATOM   3759  C  CG    . LEU   A 1 469 ? 166.136 125.434 117.794 1.00 79.93  ?  469  LEU   A CG    1 
ATOM   3760  C  CD1   . LEU   A 1 469 ? 165.972 124.234 116.878 1.00 82.10  ?  469  LEU   A CD1   1 
ATOM   3761  C  CD2   . LEU   A 1 469 ? 167.448 125.357 118.556 1.00 79.25  ?  469  LEU   A CD2   1 
ATOM   3762  N  N     . GLY   A 1 470 ? 166.172 129.974 116.287 1.00 85.35  ?  470  GLY   A N     1 
ATOM   3763  C  CA    . GLY   A 1 470 ? 166.647 130.997 115.378 1.00 85.51  ?  470  GLY   A CA    1 
ATOM   3764  C  C     . GLY   A 1 470 ? 167.402 132.135 116.025 1.00 86.52  ?  470  GLY   A C     1 
ATOM   3765  O  O     . GLY   A 1 470 ? 168.026 132.929 115.315 1.00 91.64  ?  470  GLY   A O     1 
ATOM   3766  N  N     . ALA   A 1 471 ? 167.361 132.237 117.353 1.00 89.44  ?  471  ALA   A N     1 
ATOM   3767  C  CA    . ALA   A 1 471 ? 168.084 133.279 118.067 1.00 88.21  ?  471  ALA   A CA    1 
ATOM   3768  C  C     . ALA   A 1 471 ? 169.408 132.805 118.644 1.00 92.82  ?  471  ALA   A C     1 
ATOM   3769  O  O     . ALA   A 1 471 ? 170.236 133.643 119.019 1.00 97.17  ?  471  ALA   A O     1 
ATOM   3770  C  CB    . ALA   A 1 471 ? 167.221 133.848 119.198 1.00 87.42  ?  471  ALA   A CB    1 
ATOM   3771  N  N     . ILE   A 1 472 ? 169.626 131.501 118.726 1.00 96.59  ?  472  ILE   A N     1 
ATOM   3772  C  CA    . ILE   A 1 472 ? 170.878 130.949 119.226 1.00 96.08  ?  472  ILE   A CA    1 
ATOM   3773  C  C     . ILE   A 1 472 ? 171.807 130.689 118.050 1.00 98.78  ?  472  ILE   A C     1 
ATOM   3774  O  O     . ILE   A 1 472 ? 171.367 130.301 116.961 1.00 99.35  ?  472  ILE   A O     1 
ATOM   3775  C  CB    . ILE   A 1 472 ? 170.630 129.667 120.043 1.00 94.44  ?  472  ILE   A CB    1 
ATOM   3776  C  CG1   . ILE   A 1 472 ? 170.003 128.579 119.169 1.00 95.27  ?  472  ILE   A CG1   1 
ATOM   3777  C  CG2   . ILE   A 1 472 ? 169.743 129.963 121.241 1.00 94.04  ?  472  ILE   A CG2   1 
ATOM   3778  C  CD1   . ILE   A 1 472 ? 170.567 127.198 119.416 1.00 94.58  ?  472  ILE   A CD1   1 
ATOM   3779  N  N     . ASN   A 1 473 ? 173.101 130.924 118.264 1.00 106.06 ?  473  ASN   A N     1 
ATOM   3780  C  CA    . ASN   A 1 473 ? 174.105 130.688 117.238 1.00 104.58 ?  473  ASN   A CA    1 
ATOM   3781  C  C     . ASN   A 1 473 ? 174.896 129.408 117.459 1.00 104.73 ?  473  ASN   A C     1 
ATOM   3782  O  O     . ASN   A 1 473 ? 175.474 128.882 116.501 1.00 106.42 ?  473  ASN   A O     1 
ATOM   3783  C  CB    . ASN   A 1 473 ? 175.077 131.872 117.165 1.00 103.46 ?  473  ASN   A CB    1 
ATOM   3784  C  CG    . ASN   A 1 473 ? 175.629 132.256 118.524 1.00 107.88 ?  473  ASN   A CG    1 
ATOM   3785  O  OD1   . ASN   A 1 473 ? 175.324 131.620 119.533 1.00 109.58 ?  473  ASN   A OD1   1 
ATOM   3786  N  ND2   . ASN   A 1 473 ? 176.446 133.301 118.557 1.00 109.21 ?  473  ASN   A ND2   1 
ATOM   3787  N  N     . ASN   A 1 474 ? 174.935 128.899 118.688 1.00 95.58  ?  474  ASN   A N     1 
ATOM   3788  C  CA    . ASN   A 1 474 ? 175.662 127.681 119.006 1.00 94.81  ?  474  ASN   A CA    1 
ATOM   3789  C  C     . ASN   A 1 474 ? 174.792 126.803 119.894 1.00 93.34  ?  474  ASN   A C     1 
ATOM   3790  O  O     . ASN   A 1 474 ? 174.008 127.299 120.707 1.00 94.24  ?  474  ASN   A O     1 
ATOM   3791  C  CB    . ASN   A 1 474 ? 176.997 127.994 119.698 1.00 96.50  ?  474  ASN   A CB    1 
ATOM   3792  C  CG    . ASN   A 1 474 ? 177.833 126.756 119.938 1.00 100.24 ?  474  ASN   A CG    1 
ATOM   3793  O  OD1   . ASN   A 1 474 ? 177.881 125.855 119.103 1.00 101.71 ?  474  ASN   A OD1   1 
ATOM   3794  N  ND2   . ASN   A 1 474 ? 178.497 126.705 121.086 1.00 99.81  ?  474  ASN   A ND2   1 
ATOM   3795  N  N     . LEU   A 1 475 ? 174.934 125.486 119.724 1.00 88.98  ?  475  LEU   A N     1 
ATOM   3796  C  CA    . LEU   A 1 475 ? 174.124 124.551 120.498 1.00 90.71  ?  475  LEU   A CA    1 
ATOM   3797  C  C     . LEU   A 1 475 ? 174.514 124.544 121.970 1.00 95.29  ?  475  LEU   A C     1 
ATOM   3798  O  O     . LEU   A 1 475 ? 173.650 124.358 122.836 1.00 94.66  ?  475  LEU   A O     1 
ATOM   3799  C  CB    . LEU   A 1 475 ? 174.240 123.144 119.912 1.00 92.44  ?  475  LEU   A CB    1 
ATOM   3800  C  CG    . LEU   A 1 475 ? 173.348 122.827 118.710 1.00 91.41  ?  475  LEU   A CG    1 
ATOM   3801  C  CD1   . LEU   A 1 475 ? 173.372 121.339 118.401 1.00 88.95  ?  475  LEU   A CD1   1 
ATOM   3802  C  CD2   . LEU   A 1 475 ? 171.925 123.304 118.946 1.00 86.38  ?  475  LEU   A CD2   1 
ATOM   3803  N  N     . ASP   A 1 476 ? 175.801 124.739 122.273 1.00 101.46 ?  476  ASP   A N     1 
ATOM   3804  C  CA    . ASP   A 1 476 ? 176.242 124.734 123.663 1.00 99.92  ?  476  ASP   A CA    1 
ATOM   3805  C  C     . ASP   A 1 476 ? 175.611 125.865 124.456 1.00 99.88  ?  476  ASP   A C     1 
ATOM   3806  O  O     . ASP   A 1 476 ? 175.435 125.739 125.668 1.00 101.59 ?  476  ASP   A O     1 
ATOM   3807  C  CB    . ASP   A 1 476 ? 177.763 124.834 123.740 1.00 100.36 ?  476  ASP   A CB    1 
ATOM   3808  C  CG    . ASP   A 1 476 ? 178.457 123.647 123.107 1.00 104.68 ?  476  ASP   A CG    1 
ATOM   3809  O  OD1   . ASP   A 1 476 ? 177.776 122.637 122.833 1.00 102.51 ?  476  ASP   A OD1   1 
ATOM   3810  O  OD2   . ASP   A 1 476 ? 179.682 123.724 122.882 1.00 106.28 ?  476  ASP   A OD2   1 
ATOM   3811  N  N     . GLU   A 1 477 ? 175.268 126.972 123.794 1.00 96.92  ?  477  GLU   A N     1 
ATOM   3812  C  CA    . GLU   A 1 477 ? 174.579 128.064 124.468 1.00 97.56  ?  477  GLU   A CA    1 
ATOM   3813  C  C     . GLU   A 1 477 ? 173.246 127.606 125.051 1.00 98.34  ?  477  GLU   A C     1 
ATOM   3814  O  O     . GLU   A 1 477 ? 172.716 128.254 125.960 1.00 96.72  ?  477  GLU   A O     1 
ATOM   3815  C  CB    . GLU   A 1 477 ? 174.417 129.234 123.489 1.00 97.09  ?  477  GLU   A CB    1 
ATOM   3816  C  CG    . GLU   A 1 477 ? 173.120 130.010 123.575 1.00 102.45 ?  477  GLU   A CG    1 
ATOM   3817  C  CD    . GLU   A 1 477 ? 173.143 131.262 122.726 1.00 104.27 ?  477  GLU   A CD    1 
ATOM   3818  O  OE1   . GLU   A 1 477 ? 173.319 131.143 121.496 1.00 103.54 ?  477  GLU   A OE1   1 
ATOM   3819  O  OE2   . GLU   A 1 477 ? 172.993 132.365 123.290 1.00 102.58 ?  477  GLU   A OE2   1 
ATOM   3820  N  N     . LEU   A 1 478 ? 172.732 126.461 124.608 1.00 94.75  ?  478  LEU   A N     1 
ATOM   3821  C  CA    . LEU   A 1 478 ? 171.551 125.895 125.241 1.00 91.63  ?  478  LEU   A CA    1 
ATOM   3822  C  C     . LEU   A 1 478 ? 171.841 125.301 126.610 1.00 95.05  ?  478  LEU   A C     1 
ATOM   3823  O  O     . LEU   A 1 478 ? 170.894 124.908 127.300 1.00 95.66  ?  478  LEU   A O     1 
ATOM   3824  C  CB    . LEU   A 1 478 ? 170.923 124.839 124.332 1.00 85.08  ?  478  LEU   A CB    1 
ATOM   3825  C  CG    . LEU   A 1 478 ? 170.153 125.353 123.114 1.00 91.66  ?  478  LEU   A CG    1 
ATOM   3826  C  CD1   . LEU   A 1 478 ? 169.736 124.197 122.221 1.00 91.61  ?  478  LEU   A CD1   1 
ATOM   3827  C  CD2   . LEU   A 1 478 ? 168.942 126.160 123.546 1.00 94.14  ?  478  LEU   A CD2   1 
ATOM   3828  N  N     . GLU   A 1 479 ? 173.097 125.244 127.059 1.00 98.68  ?  479  GLU   A N     1 
ATOM   3829  C  CA    . GLU   A 1 479 ? 173.318 124.751 128.413 1.00 97.03  ?  479  GLU   A CA    1 
ATOM   3830  C  C     . GLU   A 1 479 ? 172.687 125.698 129.416 1.00 99.13  ?  479  GLU   A C     1 
ATOM   3831  O  O     . GLU   A 1 479 ? 171.909 125.269 130.274 1.00 100.18 ?  479  GLU   A O     1 
ATOM   3832  C  CB    . GLU   A 1 479 ? 174.805 124.533 128.722 1.00 95.11  ?  479  GLU   A CB    1 
ATOM   3833  C  CG    . GLU   A 1 479 ? 175.066 124.109 130.156 1.00 97.02  ?  479  GLU   A CG    1 
ATOM   3834  C  CD    . GLU   A 1 479 ? 176.419 123.461 130.360 1.00 101.86 ?  479  GLU   A CD    1 
ATOM   3835  O  OE1   . GLU   A 1 479 ? 177.094 123.169 129.354 1.00 105.21 ?  479  GLU   A OE1   1 
ATOM   3836  O  OE2   . GLU   A 1 479 ? 176.801 123.250 131.528 1.00 100.49 ?  479  GLU   A OE2   1 
ATOM   3837  N  N     . GLU   A 1 480 ? 172.941 127.011 129.256 1.00 99.15  ?  480  GLU   A N     1 
ATOM   3838  C  CA    A GLU   A 1 480 ? 172.434 128.039 130.166 0.50 95.66  ?  480  GLU   A CA    1 
ATOM   3839  C  CA    B GLU   A 1 480 ? 172.534 128.039 130.166 0.50 95.66  ?  480  GLU   A CA    1 
ATOM   3840  C  C     . GLU   A 1 480 ? 170.942 128.236 130.013 1.00 97.14  ?  480  GLU   A C     1 
ATOM   3841  O  O     . GLU   A 1 480 ? 170.194 128.030 130.964 1.00 97.17  ?  480  GLU   A O     1 
ATOM   3842  C  CB    A GLU   A 1 480 ? 173.149 129.362 129.916 0.50 97.30  ?  480  GLU   A CB    1 
ATOM   3843  C  CB    B GLU   A 1 480 ? 173.249 129.362 129.916 0.50 97.30  ?  480  GLU   A CB    1 
ATOM   3844  C  CG    A GLU   A 1 480 ? 174.618 129.347 130.299 0.50 101.70 ?  480  GLU   A CG    1 
ATOM   3845  C  CG    B GLU   A 1 480 ? 172.890 130.451 130.912 0.50 101.70 ?  480  GLU   A CG    1 
ATOM   3846  C  CD    A GLU   A 1 480 ? 175.406 128.138 129.817 0.50 105.74 ?  480  GLU   A CD    1 
ATOM   3847  C  CD    B GLU   A 1 480 ? 173.619 131.773 130.724 0.50 105.74 ?  480  GLU   A CD    1 
ATOM   3848  O  OE1   A GLU   A 1 480 ? 174.924 127.432 128.912 0.50 105.00 ?  480  GLU   A OE1   1 
ATOM   3849  O  OE1   B GLU   A 1 480 ? 174.412 131.889 129.771 0.50 105.00 ?  480  GLU   A OE1   1 
ATOM   3850  O  OE2   A GLU   A 1 480 ? 176.501 127.895 130.363 0.50 105.15 ?  480  GLU   A OE2   1 
ATOM   3851  O  OE2   B GLU   A 1 480 ? 173.403 132.685 131.547 0.50 105.15 ?  480  GLU   A OE2   1 
ATOM   3852  N  N     . LEU   A 1 481 ? 170.489 128.666 128.822 1.00 82.63  ?  481  LEU   A N     1 
ATOM   3853  C  CA    . LEU   A 1 481 ? 169.069 128.859 128.553 1.00 78.54  ?  481  LEU   A CA    1 
ATOM   3854  C  C     . LEU   A 1 481 ? 168.261 127.749 129.221 1.00 78.07  ?  481  LEU   A C     1 
ATOM   3855  O  O     . LEU   A 1 481 ? 167.254 128.037 129.877 1.00 75.20  ?  481  LEU   A O     1 
ATOM   3856  C  CB    . LEU   A 1 481 ? 168.834 128.896 127.042 1.00 77.63  ?  481  LEU   A CB    1 
ATOM   3857  C  CG    . LEU   A 1 481 ? 169.453 130.078 126.301 1.00 79.73  ?  481  LEU   A CG    1 
ATOM   3858  C  CD1   . LEU   A 1 481 ? 169.024 130.066 124.847 1.00 81.30  ?  481  LEU   A CD1   1 
ATOM   3859  C  CD2   . LEU   A 1 481 ? 169.055 131.384 126.964 1.00 78.05  ?  481  LEU   A CD2   1 
ATOM   3860  N  N     . ALA   A 1 482 ? 168.741 126.494 129.126 1.00 84.67  ?  482  ALA   A N     1 
ATOM   3861  C  CA    . ALA   A 1 482 ? 168.075 125.368 129.770 1.00 79.39  ?  482  ALA   A CA    1 
ATOM   3862  C  C     . ALA   A 1 482 ? 167.891 125.611 131.245 1.00 82.95  ?  482  ALA   A C     1 
ATOM   3863  O  O     . ALA   A 1 482 ? 166.777 125.499 131.763 1.00 88.86  ?  482  ALA   A O     1 
ATOM   3864  C  CB    . ALA   A 1 482 ? 168.878 124.101 129.565 1.00 80.75  ?  482  ALA   A CB    1 
ATOM   3865  N  N     . ILE   A 1 483 ? 168.984 125.948 131.941 1.00 80.59  ?  483  ILE   A N     1 
ATOM   3866  C  CA    . ILE   A 1 483 ? 168.947 126.196 133.376 1.00 77.94  ?  483  ILE   A CA    1 
ATOM   3867  C  C     . ILE   A 1 483 ? 167.872 127.220 133.692 1.00 80.69  ?  483  ILE   A C     1 
ATOM   3868  O  O     . ILE   A 1 483 ? 166.875 126.914 134.361 1.00 86.61  ?  483  ILE   A O     1 
ATOM   3869  C  CB    . ILE   A 1 483 ? 170.325 126.650 133.886 1.00 73.89  ?  483  ILE   A CB    1 
ATOM   3870  C  CG1   . ILE   A 1 483 ? 171.314 125.484 133.871 1.00 77.56  ?  483  ILE   A CG1   1 
ATOM   3871  C  CG2   . ILE   A 1 483 ? 170.206 127.223 135.288 1.00 73.36  ?  483  ILE   A CG2   1 
ATOM   3872  C  CD1   . ILE   A 1 483 ? 172.761 125.913 133.968 1.00 76.55  ?  483  ILE   A CD1   1 
ATOM   3873  N  N     . LEU   A 1 484 ? 168.009 128.420 133.113 1.00 69.58  ?  484  LEU   A N     1 
ATOM   3874  C  CA    . LEU   A 1 484 ? 167.055 129.484 133.400 1.00 71.33  ?  484  LEU   A CA    1 
ATOM   3875  C  C     . LEU   A 1 484 ? 165.641 128.992 133.160 1.00 73.57  ?  484  LEU   A C     1 
ATOM   3876  O  O     . LEU   A 1 484 ? 164.801 129.015 134.070 1.00 81.51  ?  484  LEU   A O     1 
ATOM   3877  C  CB    . LEU   A 1 484 ? 167.350 130.707 132.532 1.00 74.03  ?  484  LEU   A CB    1 
ATOM   3878  C  CG    . LEU   A 1 484 ? 168.689 131.413 132.734 1.00 77.85  ?  484  LEU   A CG    1 
ATOM   3879  C  CD1   . LEU   A 1 484 ? 168.902 132.442 131.639 1.00 77.93  ?  484  LEU   A CD1   1 
ATOM   3880  C  CD2   . LEU   A 1 484 ? 168.753 132.060 134.106 1.00 77.43  ?  484  LEU   A CD2   1 
ATOM   3881  N  N     . ALA   A 1 485 ? 165.399 128.427 131.969 1.00 71.45  ?  485  ALA   A N     1 
ATOM   3882  C  CA    . ALA   A 1 485 ? 164.052 127.991 131.633 1.00 72.27  ?  485  ALA   A CA    1 
ATOM   3883  C  C     . ALA   A 1 485 ? 163.530 127.061 132.710 1.00 75.33  ?  485  ALA   A C     1 
ATOM   3884  O  O     . ALA   A 1 485 ? 162.499 127.337 133.339 1.00 77.00  ?  485  ALA   A O     1 
ATOM   3885  C  CB    . ALA   A 1 485 ? 164.044 127.304 130.267 1.00 69.07  ?  485  ALA   A CB    1 
ATOM   3886  N  N     . VAL   A 1 486 ? 164.309 126.023 133.030 1.00 71.70  ?  486  VAL   A N     1 
ATOM   3887  C  CA    . VAL   A 1 486 ? 163.852 125.049 134.011 1.00 67.99  ?  486  VAL   A CA    1 
ATOM   3888  C  C     . VAL   A 1 486 ? 163.521 125.758 135.310 1.00 73.54  ?  486  VAL   A C     1 
ATOM   3889  O  O     . VAL   A 1 486 ? 162.386 125.689 135.805 1.00 79.75  ?  486  VAL   A O     1 
ATOM   3890  C  CB    . VAL   A 1 486 ? 164.912 123.952 134.216 1.00 68.15  ?  486  VAL   A CB    1 
ATOM   3891  C  CG1   . VAL   A 1 486 ? 164.518 123.042 135.367 1.00 71.33  ?  486  VAL   A CG1   1 
ATOM   3892  C  CG2   . VAL   A 1 486 ? 165.100 123.152 132.938 1.00 72.73  ?  486  VAL   A CG2   1 
ATOM   3893  N  N     . ARG   A 1 487 ? 164.463 126.566 135.801 1.00 72.74  ?  487  ARG   A N     1 
ATOM   3894  C  CA    . ARG   A 1 487 ? 164.248 127.240 137.071 1.00 73.75  ?  487  ARG   A CA    1 
ATOM   3895  C  C     . ARG   A 1 487 ? 162.999 128.099 137.000 1.00 77.33  ?  487  ARG   A C     1 
ATOM   3896  O  O     . ARG   A 1 487 ? 162.111 127.993 137.857 1.00 83.46  ?  487  ARG   A O     1 
ATOM   3897  C  CB    . ARG   A 1 487 ? 165.475 128.072 137.441 1.00 72.43  ?  487  ARG   A CB    1 
ATOM   3898  C  CG    . ARG   A 1 487 ? 166.631 127.232 137.956 1.00 73.54  ?  487  ARG   A CG    1 
ATOM   3899  C  CD    . ARG   A 1 487 ? 167.898 128.049 138.127 1.00 81.40  ?  487  ARG   A CD    1 
ATOM   3900  N  NE    . ARG   A 1 487 ? 169.012 127.218 138.568 1.00 83.77  ?  487  ARG   A NE    1 
ATOM   3901  C  CZ    . ARG   A 1 487 ? 169.213 126.836 139.822 1.00 82.99  ?  487  ARG   A CZ    1 
ATOM   3902  N  NH1   . ARG   A 1 487 ? 168.397 127.204 140.796 1.00 80.69  ?  487  ARG   A NH1   1 
ATOM   3903  N  NH2   . ARG   A 1 487 ? 170.257 126.063 140.105 1.00 81.01  ?  487  ARG   A NH2   1 
ATOM   3904  N  N     . ALA   A 1 488 ? 162.866 128.878 135.922 1.00 61.47  ?  488  ALA   A N     1 
ATOM   3905  C  CA    . ALA   A 1 488 ? 161.691 129.724 135.782 1.00 62.09  ?  488  ALA   A CA    1 
ATOM   3906  C  C     . ALA   A 1 488 ? 160.429 128.886 135.878 1.00 68.54  ?  488  ALA   A C     1 
ATOM   3907  O  O     . ALA   A 1 488 ? 159.563 129.140 136.726 1.00 67.26  ?  488  ALA   A O     1 
ATOM   3908  C  CB    . ALA   A 1 488 ? 161.742 130.484 134.458 1.00 66.94  ?  488  ALA   A CB    1 
ATOM   3909  N  N     . LEU   A 1 489 ? 160.357 127.817 135.081 1.00 75.71  ?  489  LEU   A N     1 
ATOM   3910  C  CA    . LEU   A 1 489 ? 159.164 126.986 135.107 1.00 68.52  ?  489  LEU   A CA    1 
ATOM   3911  C  C     . LEU   A 1 489 ? 158.968 126.389 136.489 1.00 71.97  ?  489  LEU   A C     1 
ATOM   3912  O  O     . LEU   A 1 489 ? 157.852 126.402 137.026 1.00 77.16  ?  489  LEU   A O     1 
ATOM   3913  C  CB    . LEU   A 1 489 ? 159.255 125.900 134.039 1.00 73.47  ?  489  LEU   A CB    1 
ATOM   3914  C  CG    . LEU   A 1 489 ? 159.008 126.361 132.601 1.00 72.95  ?  489  LEU   A CG    1 
ATOM   3915  C  CD1   . LEU   A 1 489 ? 158.536 125.204 131.739 1.00 77.69  ?  489  LEU   A CD1   1 
ATOM   3916  C  CD2   . LEU   A 1 489 ? 158.007 127.507 132.559 1.00 72.78  ?  489  LEU   A CD2   1 
ATOM   3917  N  N     . ASP   A 1 490 ? 160.059 125.931 137.111 1.00 74.06  ?  490  ASP   A N     1 
ATOM   3918  C  CA    . ASP   A 1 490 ? 159.948 125.385 138.456 1.00 71.86  ?  490  ASP   A CA    1 
ATOM   3919  C  C     . ASP   A 1 490 ? 159.356 126.420 139.397 1.00 74.94  ?  490  ASP   A C     1 
ATOM   3920  O  O     . ASP   A 1 490 ? 158.419 126.124 140.150 1.00 76.11  ?  490  ASP   A O     1 
ATOM   3921  C  CB    . ASP   A 1 490 ? 161.317 124.919 138.949 1.00 78.81  ?  490  ASP   A CB    1 
ATOM   3922  C  CG    . ASP   A 1 490 ? 161.220 123.779 139.940 1.00 86.00  ?  490  ASP   A CG    1 
ATOM   3923  O  OD1   . ASP   A 1 490 ? 160.345 122.907 139.760 1.00 87.64  ?  490  ASP   A OD1   1 
ATOM   3924  O  OD2   . ASP   A 1 490 ? 162.018 123.754 140.900 1.00 86.33  ?  490  ASP   A OD2   1 
ATOM   3925  N  N     . ALA   A 1 491 ? 159.838 127.662 139.308 1.00 74.00  ?  491  ALA   A N     1 
ATOM   3926  C  CA    . ALA   A 1 491 ? 159.298 128.713 140.158 1.00 73.64  ?  491  ALA   A CA    1 
ATOM   3927  C  C     . ALA   A 1 491 ? 157.813 128.903 139.898 1.00 74.49  ?  491  ALA   A C     1 
ATOM   3928  O  O     . ALA   A 1 491 ? 157.021 129.032 140.840 1.00 78.96  ?  491  ALA   A O     1 
ATOM   3929  C  CB    . ALA   A 1 491 ? 160.062 130.014 139.931 1.00 72.53  ?  491  ALA   A CB    1 
ATOM   3930  N  N     . LEU   A 1 492 ? 157.411 128.875 138.624 1.00 71.63  ?  492  LEU   A N     1 
ATOM   3931  C  CA    . LEU   A 1 492 ? 155.999 129.035 138.304 1.00 65.07  ?  492  LEU   A CA    1 
ATOM   3932  C  C     . LEU   A 1 492 ? 155.170 127.943 138.960 1.00 69.35  ?  492  LEU   A C     1 
ATOM   3933  O  O     . LEU   A 1 492 ? 154.049 128.195 139.425 1.00 73.82  ?  492  LEU   A O     1 
ATOM   3934  C  CB    . LEU   A 1 492 ? 155.796 129.035 136.790 1.00 64.74  ?  492  LEU   A CB    1 
ATOM   3935  C  CG    . LEU   A 1 492 ? 154.359 129.267 136.320 1.00 70.43  ?  492  LEU   A CG    1 
ATOM   3936  C  CD1   . LEU   A 1 492 ? 154.064 130.754 136.214 1.00 68.34  ?  492  LEU   A CD1   1 
ATOM   3937  C  CD2   . LEU   A 1 492 ? 154.106 128.571 134.994 1.00 74.02  ?  492  LEU   A CD2   1 
ATOM   3938  N  N     . LEU   A 1 493 ? 155.726 126.731 139.055 1.00 75.71  ?  493  LEU   A N     1 
ATOM   3939  C  CA    . LEU   A 1 493 ? 154.983 125.639 139.665 1.00 73.33  ?  493  LEU   A CA    1 
ATOM   3940  C  C     . LEU   A 1 493 ? 154.653 125.930 141.124 1.00 74.96  ?  493  LEU   A C     1 
ATOM   3941  O  O     . LEU   A 1 493 ? 153.629 125.464 141.625 1.00 80.01  ?  493  LEU   A O     1 
ATOM   3942  C  CB    . LEU   A 1 493 ? 155.763 124.332 139.524 1.00 75.46  ?  493  LEU   A CB    1 
ATOM   3943  C  CG    . LEU   A 1 493 ? 155.734 123.733 138.118 1.00 72.82  ?  493  LEU   A CG    1 
ATOM   3944  C  CD1   . LEU   A 1 493 ? 156.545 122.455 138.065 1.00 70.12  ?  493  LEU   A CD1   1 
ATOM   3945  C  CD2   . LEU   A 1 493 ? 154.302 123.485 137.672 1.00 72.82  ?  493  LEU   A CD2   1 
ATOM   3946  N  N     . ASP   A 1 494 ? 155.393 126.802 141.793 1.00 87.73  ?  494  ASP   A N     1 
ATOM   3947  C  CA    . ASP   A 1 494 ? 155.108 126.998 143.209 1.00 86.41  ?  494  ASP   A CA    1 
ATOM   3948  C  C     . ASP   A 1 494 ? 154.289 128.254 143.458 1.00 86.27  ?  494  ASP   A C     1 
ATOM   3949  O  O     . ASP   A 1 494 ? 153.840 128.467 144.584 1.00 91.08  ?  494  ASP   A O     1 
ATOM   3950  C  CB    . ASP   A 1 494 ? 156.416 127.005 144.020 1.00 85.86  ?  494  ASP   A CB    1 
ATOM   3951  C  CG    . ASP   A 1 494 ? 157.125 125.666 143.986 1.00 91.11  ?  494  ASP   A CG    1 
ATOM   3952  O  OD1   . ASP   A 1 494 ? 156.429 124.632 144.002 1.00 91.91  ?  494  ASP   A OD1   1 
ATOM   3953  O  OD2   . ASP   A 1 494 ? 158.371 125.663 143.942 1.00 95.69  ?  494  ASP   A OD2   1 
ATOM   3954  N  N     . TYR   A 1 495 ? 154.050 129.064 142.421 1.00 78.79  ?  495  TYR   A N     1 
ATOM   3955  C  CA    . TYR   A 1 495 ? 153.362 130.336 142.542 1.00 77.77  ?  495  TYR   A CA    1 
ATOM   3956  C  C     . TYR   A 1 495 ? 151.951 130.238 141.992 1.00 81.83  ?  495  TYR   A C     1 
ATOM   3957  O  O     . TYR   A 1 495 ? 151.062 130.970 142.432 1.00 87.03  ?  495  TYR   A O     1 
ATOM   3958  C  CB    . TYR   A 1 495 ? 154.216 131.370 141.798 1.00 77.84  ?  495  TYR   A CB    1 
ATOM   3959  C  CG    . TYR   A 1 495 ? 153.759 132.788 141.611 1.00 82.12  ?  495  TYR   A CG    1 
ATOM   3960  C  CD1   . TYR   A 1 495 ? 154.000 133.751 142.575 1.00 84.34  ?  495  TYR   A CD1   1 
ATOM   3961  C  CD2   . TYR   A 1 495 ? 153.197 133.195 140.414 1.00 81.10  ?  495  TYR   A CD2   1 
ATOM   3962  C  CE1   . TYR   A 1 495 ? 153.630 135.071 142.380 1.00 86.01  ?  495  TYR   A CE1   1 
ATOM   3963  C  CE2   . TYR   A 1 495 ? 152.822 134.510 140.204 1.00 80.76  ?  495  TYR   A CE2   1 
ATOM   3964  C  CZ    . TYR   A 1 495 ? 153.036 135.448 141.192 1.00 86.27  ?  495  TYR   A CZ    1 
ATOM   3965  O  OH    . TYR   A 1 495 ? 152.663 136.756 140.991 1.00 88.72  ?  495  TYR   A OH    1 
ATOM   3966  N  N     . GLN   A 1 496 ? 151.728 129.302 141.060 1.00 77.39  ?  496  GLN   A N     1 
ATOM   3967  C  CA    . GLN   A 1 496 ? 150.423 129.144 140.420 1.00 76.36  ?  496  GLN   A CA    1 
ATOM   3968  C  C     . GLN   A 1 496 ? 149.408 128.746 141.458 1.00 81.94  ?  496  GLN   A C     1 
ATOM   3969  O  O     . GLN   A 1 496 ? 149.757 128.042 142.402 1.00 85.45  ?  496  GLN   A O     1 
ATOM   3970  C  CB    . GLN   A 1 496 ? 150.448 128.006 139.415 1.00 77.33  ?  496  GLN   A CB    1 
ATOM   3971  C  CG    . GLN   A 1 496 ? 150.989 128.336 138.051 1.00 80.01  ?  496  GLN   A CG    1 
ATOM   3972  C  CD    . GLN   A 1 496 ? 151.046 127.080 137.221 1.00 80.96  ?  496  GLN   A CD    1 
ATOM   3973  O  OE1   . GLN   A 1 496 ? 151.116 125.976 137.758 1.00 83.40  ?  496  GLN   A OE1   1 
ATOM   3974  N  NE2   . GLN   A 1 496 ? 150.997 127.234 135.911 1.00 84.00  ?  496  GLN   A NE2   1 
ATOM   3975  N  N     . ASP   A 1 497 ? 148.153 129.165 141.291 1.00 91.21  ?  497  ASP   A N     1 
ATOM   3976  C  CA    . ASP   A 1 497 ? 147.095 128.645 142.142 1.00 91.16  ?  497  ASP   A CA    1 
ATOM   3977  C  C     . ASP   A 1 497 ? 146.321 127.571 141.391 1.00 92.78  ?  497  ASP   A C     1 
ATOM   3978  O  O     . ASP   A 1 497 ? 146.036 127.718 140.199 1.00 93.78  ?  497  ASP   A O     1 
ATOM   3979  C  CB    . ASP   A 1 497 ? 146.152 129.755 142.600 1.00 95.18  ?  497  ASP   A CB    1 
ATOM   3980  C  CG    . ASP   A 1 497 ? 146.402 130.178 144.033 1.00 100.86 ?  497  ASP   A CG    1 
ATOM   3981  O  OD1   . ASP   A 1 497 ? 146.912 129.353 144.818 1.00 97.63  ?  497  ASP   A OD1   1 
ATOM   3982  O  OD2   . ASP   A 1 497 ? 146.089 131.338 144.374 1.00 101.12 ?  497  ASP   A OD2   1 
ATOM   3983  N  N     . TYR   A 1 498 ? 145.986 126.493 142.092 1.00 75.54  ?  498  TYR   A N     1 
ATOM   3984  C  CA    . TYR   A 1 498 ? 145.292 125.364 141.484 1.00 73.49  ?  498  TYR   A CA    1 
ATOM   3985  C  C     . TYR   A 1 498 ? 143.863 125.291 142.001 1.00 74.86  ?  498  TYR   A C     1 
ATOM   3986  O  O     . TYR   A 1 498 ? 143.655 124.994 143.188 1.00 75.45  ?  498  TYR   A O     1 
ATOM   3987  C  CB    . TYR   A 1 498 ? 146.037 124.062 141.777 1.00 72.01  ?  498  TYR   A CB    1 
ATOM   3988  C  CG    . TYR   A 1 498 ? 147.499 124.107 141.394 1.00 73.08  ?  498  TYR   A CG    1 
ATOM   3989  C  CD1   . TYR   A 1 498 ? 147.905 123.818 140.099 1.00 73.12  ?  498  TYR   A CD1   1 
ATOM   3990  C  CD2   . TYR   A 1 498 ? 148.470 124.449 142.323 1.00 73.53  ?  498  TYR   A CD2   1 
ATOM   3991  C  CE1   . TYR   A 1 498 ? 149.239 123.862 139.743 1.00 72.48  ?  498  TYR   A CE1   1 
ATOM   3992  C  CE2   . TYR   A 1 498 ? 149.806 124.496 141.975 1.00 73.31  ?  498  TYR   A CE2   1 
ATOM   3993  C  CZ    . TYR   A 1 498 ? 150.184 124.201 140.685 1.00 75.60  ?  498  TYR   A CZ    1 
ATOM   3994  O  OH    . TYR   A 1 498 ? 151.513 124.247 140.334 1.00 78.51  ?  498  TYR   A OH    1 
ATOM   3995  N  N     . PRO   A 1 499 ? 142.857 125.563 141.167 1.00 79.62  ?  499  PRO   A N     1 
ATOM   3996  C  CA    . PRO   A 1 499 ? 141.467 125.484 141.646 1.00 79.58  ?  499  PRO   A CA    1 
ATOM   3997  C  C     . PRO   A 1 499 ? 141.062 124.099 142.120 1.00 78.51  ?  499  PRO   A C     1 
ATOM   3998  O  O     . PRO   A 1 499 ? 140.249 123.986 143.046 1.00 79.75  ?  499  PRO   A O     1 
ATOM   3999  C  CB    . PRO   A 1 499 ? 140.652 125.925 140.423 1.00 76.35  ?  499  PRO   A CB    1 
ATOM   4000  C  CG    . PRO   A 1 499 ? 141.546 125.676 139.254 1.00 73.96  ?  499  PRO   A CG    1 
ATOM   4001  C  CD    . PRO   A 1 499 ? 142.937 125.928 139.744 1.00 77.65  ?  499  PRO   A CD    1 
ATOM   4002  N  N     . ILE   A 1 500 ? 141.597 123.048 141.518 1.00 80.04  ?  500  ILE   A N     1 
ATOM   4003  C  CA    . ILE   A 1 500 ? 141.251 121.671 141.862 1.00 75.91  ?  500  ILE   A CA    1 
ATOM   4004  C  C     . ILE   A 1 500 ? 142.397 121.074 142.670 1.00 79.00  ?  500  ILE   A C     1 
ATOM   4005  O  O     . ILE   A 1 500 ? 143.559 121.211 142.262 1.00 84.42  ?  500  ILE   A O     1 
ATOM   4006  C  CB    . ILE   A 1 500 ? 140.975 120.827 140.604 1.00 73.84  ?  500  ILE   A CB    1 
ATOM   4007  C  CG1   . ILE   A 1 500 ? 140.082 121.598 139.629 1.00 73.67  ?  500  ILE   A CG1   1 
ATOM   4008  C  CG2   . ILE   A 1 500 ? 140.348 119.494 140.980 1.00 73.33  ?  500  ILE   A CG2   1 
ATOM   4009  C  CD1   . ILE   A 1 500 ? 138.609 121.513 139.947 1.00 75.99  ?  500  ILE   A CD1   1 
ATOM   4010  N  N     . PRO   A 1 501 ? 142.125 120.428 143.807 1.00 75.62  ?  501  PRO   A N     1 
ATOM   4011  C  CA    . PRO   A 1 501 ? 143.216 119.803 144.573 1.00 72.28  ?  501  PRO   A CA    1 
ATOM   4012  C  C     . PRO   A 1 501 ? 143.980 118.745 143.796 1.00 71.84  ?  501  PRO   A C     1 
ATOM   4013  O  O     . PRO   A 1 501 ? 145.180 118.565 144.035 1.00 74.72  ?  501  PRO   A O     1 
ATOM   4014  C  CB    . PRO   A 1 501 ? 142.489 119.200 145.783 1.00 71.59  ?  501  PRO   A CB    1 
ATOM   4015  C  CG    . PRO   A 1 501 ? 141.240 120.001 145.912 1.00 74.08  ?  501  PRO   A CG    1 
ATOM   4016  C  CD    . PRO   A 1 501 ? 140.835 120.349 144.512 1.00 76.03  ?  501  PRO   A CD    1 
ATOM   4017  N  N     . ALA   A 1 502 ? 143.321 118.031 142.880 1.00 72.13  ?  502  ALA   A N     1 
ATOM   4018  C  CA    . ALA   A 1 502 ? 144.009 117.001 142.107 1.00 70.91  ?  502  ALA   A CA    1 
ATOM   4019  C  C     . ALA   A 1 502 ? 145.089 117.603 141.217 1.00 75.48  ?  502  ALA   A C     1 
ATOM   4020  O  O     . ALA   A 1 502 ? 146.173 117.024 141.063 1.00 80.74  ?  502  ALA   A O     1 
ATOM   4021  C  CB    . ALA   A 1 502 ? 143.001 116.212 141.271 1.00 69.41  ?  502  ALA   A CB    1 
ATOM   4022  N  N     . ALA   A 1 503 ? 144.809 118.761 140.615 1.00 70.28  ?  503  ALA   A N     1 
ATOM   4023  C  CA    . ALA   A 1 503 ? 145.809 119.423 139.786 1.00 67.38  ?  503  ALA   A CA    1 
ATOM   4024  C  C     . ALA   A 1 503 ? 147.025 119.830 140.607 1.00 71.92  ?  503  ALA   A C     1 
ATOM   4025  O  O     . ALA   A 1 503 ? 148.168 119.643 140.172 1.00 80.64  ?  503  ALA   A O     1 
ATOM   4026  C  CB    . ALA   A 1 503 ? 145.195 120.640 139.097 1.00 64.89  ?  503  ALA   A CB    1 
ATOM   4027  N  N     . LYS   A 1 504 ? 146.798 120.386 141.800 1.00 66.82  ?  504  LYS   A N     1 
ATOM   4028  C  CA    . LYS   A 1 504 ? 147.913 120.741 142.671 1.00 70.38  ?  504  LYS   A CA    1 
ATOM   4029  C  C     . LYS   A 1 504 ? 148.699 119.507 143.083 1.00 65.31  ?  504  LYS   A C     1 
ATOM   4030  O  O     . LYS   A 1 504 ? 149.933 119.537 143.134 1.00 71.76  ?  504  LYS   A O     1 
ATOM   4031  C  CB    . LYS   A 1 504 ? 147.408 121.483 143.908 1.00 70.21  ?  504  LYS   A CB    1 
ATOM   4032  C  CG    . LYS   A 1 504 ? 148.520 121.936 144.840 1.00 65.48  ?  504  LYS   A CG    1 
ATOM   4033  C  CD    . LYS   A 1 504 ? 147.980 122.739 146.008 1.00 71.69  ?  504  LYS   A CD    1 
ATOM   4034  C  CE    . LYS   A 1 504 ? 148.997 122.818 147.134 1.00 70.36  ?  504  LYS   A CE    1 
ATOM   4035  N  NZ    . LYS   A 1 504 ? 150.185 123.626 146.747 1.00 73.42  ?  504  LYS   A NZ    1 
ATOM   4036  N  N     . ARG   A 1 505 ? 148.000 118.414 143.390 1.00 69.19  ?  505  ARG   A N     1 
ATOM   4037  C  CA    . ARG   A 1 505 ? 148.679 117.182 143.773 1.00 69.87  ?  505  ARG   A CA    1 
ATOM   4038  C  C     . ARG   A 1 505 ? 149.577 116.685 142.649 1.00 72.95  ?  505  ARG   A C     1 
ATOM   4039  O  O     . ARG   A 1 505 ? 150.741 116.336 142.877 1.00 75.72  ?  505  ARG   A O     1 
ATOM   4040  C  CB    . ARG   A 1 505 ? 147.652 116.117 144.153 1.00 69.89  ?  505  ARG   A CB    1 
ATOM   4041  C  CG    . ARG   A 1 505 ? 148.217 114.981 144.980 1.00 78.44  ?  505  ARG   A CG    1 
ATOM   4042  C  CD    . ARG   A 1 505 ? 147.137 113.984 145.346 1.00 78.40  ?  505  ARG   A CD    1 
ATOM   4043  N  NE    . ARG   A 1 505 ? 147.184 112.795 144.505 1.00 79.22  ?  505  ARG   A NE    1 
ATOM   4044  C  CZ    . ARG   A 1 505 ? 147.834 111.684 144.820 1.00 81.50  ?  505  ARG   A CZ    1 
ATOM   4045  N  NH1   . ARG   A 1 505 ? 148.507 111.575 145.954 1.00 78.18  ?  505  ARG   A NH1   1 
ATOM   4046  N  NH2   . ARG   A 1 505 ? 147.808 110.656 143.978 1.00 74.66  ?  505  ARG   A NH2   1 
ATOM   4047  N  N     . GLY   A 1 506 ? 149.055 116.663 141.422 1.00 74.65  ?  506  GLY   A N     1 
ATOM   4048  C  CA    . GLY   A 1 506 ? 149.864 116.222 140.296 1.00 72.97  ?  506  GLY   A CA    1 
ATOM   4049  C  C     . GLY   A 1 506 ? 151.058 117.125 140.050 1.00 72.94  ?  506  GLY   A C     1 
ATOM   4050  O  O     . GLY   A 1 506 ? 152.183 116.652 139.855 1.00 78.94  ?  506  GLY   A O     1 
ATOM   4051  N  N     . ALA   A 1 507 ? 150.831 118.442 140.072 1.00 71.67  ?  507  ALA   A N     1 
ATOM   4052  C  CA    . ALA   A 1 507 ? 151.912 119.387 139.814 1.00 72.13  ?  507  ALA   A CA    1 
ATOM   4053  C  C     . ALA   A 1 507 ? 153.000 119.295 140.876 1.00 74.90  ?  507  ALA   A C     1 
ATOM   4054  O  O     . ALA   A 1 507 ? 154.193 119.357 140.559 1.00 77.90  ?  507  ALA   A O     1 
ATOM   4055  C  CB    . ALA   A 1 507 ? 151.358 120.808 139.734 1.00 69.82  ?  507  ALA   A CB    1 
ATOM   4056  N  N     . MET   A 1 508 ? 152.612 119.154 142.145 1.00 81.36  ?  508  MET   A N     1 
ATOM   4057  C  CA    . MET   A 1 508 ? 153.603 119.062 143.210 1.00 76.25  ?  508  MET   A CA    1 
ATOM   4058  C  C     . MET   A 1 508 ? 154.346 117.734 143.164 1.00 79.15  ?  508  MET   A C     1 
ATOM   4059  O  O     . MET   A 1 508 ? 155.569 117.697 143.336 1.00 84.47  ?  508  MET   A O     1 
ATOM   4060  C  CB    . MET   A 1 508 ? 152.932 119.254 144.569 1.00 80.63  ?  508  MET   A CB    1 
ATOM   4061  C  CG    . MET   A 1 508 ? 152.736 120.706 144.965 1.00 84.35  ?  508  MET   A CG    1 
ATOM   4062  S  SD    . MET   A 1 508 ? 153.990 121.791 144.262 1.00 99.44  ?  508  MET   A SD    1 
ATOM   4063  C  CE    . MET   A 1 508 ? 153.000 122.733 143.108 1.00 80.03  ?  508  MET   A CE    1 
ATOM   4064  N  N     . GLY   A 1 509 ? 153.628 116.632 142.938 1.00 74.10  ?  509  GLY   A N     1 
ATOM   4065  C  CA    . GLY   A 1 509 ? 154.274 115.332 142.927 1.00 74.04  ?  509  GLY   A CA    1 
ATOM   4066  C  C     . GLY   A 1 509 ? 155.233 115.151 141.767 1.00 76.96  ?  509  GLY   A C     1 
ATOM   4067  O  O     . GLY   A 1 509 ? 156.337 114.629 141.943 1.00 78.97  ?  509  GLY   A O     1 
ATOM   4068  N  N     . ARG   A 1 510 ? 154.834 115.577 140.569 1.00 74.41  ?  510  ARG   A N     1 
ATOM   4069  C  CA    . ARG   A 1 510 ? 155.626 115.285 139.381 1.00 70.06  ?  510  ARG   A CA    1 
ATOM   4070  C  C     . ARG   A 1 510 ? 156.437 116.468 138.875 1.00 71.30  ?  510  ARG   A C     1 
ATOM   4071  O  O     . ARG   A 1 510 ? 157.537 116.262 138.352 1.00 75.48  ?  510  ARG   A O     1 
ATOM   4072  C  CB    . ARG   A 1 510 ? 154.718 114.768 138.261 1.00 69.02  ?  510  ARG   A CB    1 
ATOM   4073  C  CG    . ARG   A 1 510 ? 154.491 113.270 138.333 1.00 69.27  ?  510  ARG   A CG    1 
ATOM   4074  C  CD    . ARG   A 1 510 ? 153.454 112.796 137.334 1.00 70.34  ?  510  ARG   A CD    1 
ATOM   4075  N  NE    . ARG   A 1 510 ? 152.525 111.845 137.933 1.00 71.49  ?  510  ARG   A NE    1 
ATOM   4076  C  CZ    . ARG   A 1 510 ? 152.824 110.589 138.238 1.00 73.12  ?  510  ARG   A CZ    1 
ATOM   4077  N  NH1   . ARG   A 1 510 ? 154.027 110.089 138.010 1.00 72.83  ?  510  ARG   A NH1   1 
ATOM   4078  N  NH2   . ARG   A 1 510 ? 151.892 109.816 138.787 1.00 73.54  ?  510  ARG   A NH2   1 
ATOM   4079  N  N     . ARG   A 1 511 ? 155.930 117.694 139.022 1.00 72.42  ?  511  ARG   A N     1 
ATOM   4080  C  CA    . ARG   A 1 511 ? 156.636 118.902 138.587 1.00 68.75  ?  511  ARG   A CA    1 
ATOM   4081  C  C     . ARG   A 1 511 ? 157.020 118.827 137.111 1.00 68.36  ?  511  ARG   A C     1 
ATOM   4082  O  O     . ARG   A 1 511 ? 158.118 119.221 136.715 1.00 75.34  ?  511  ARG   A O     1 
ATOM   4083  C  CB    . ARG   A 1 511 ? 157.869 119.167 139.455 1.00 67.78  ?  511  ARG   A CB    1 
ATOM   4084  C  CG    . ARG   A 1 511 ? 157.625 119.025 140.947 1.00 70.27  ?  511  ARG   A CG    1 
ATOM   4085  C  CD    . ARG   A 1 511 ? 158.776 119.603 141.753 1.00 70.10  ?  511  ARG   A CD    1 
ATOM   4086  N  NE    . ARG   A 1 511 ? 158.920 121.040 141.553 1.00 72.03  ?  511  ARG   A NE    1 
ATOM   4087  C  CZ    . ARG   A 1 511 ? 158.263 121.962 142.243 1.00 72.46  ?  511  ARG   A CZ    1 
ATOM   4088  N  NH1   . ARG   A 1 511 ? 157.399 121.632 143.189 1.00 69.00  ?  511  ARG   A NH1   1 
ATOM   4089  N  NH2   . ARG   A 1 511 ? 158.479 123.247 141.978 1.00 71.60  ?  511  ARG   A NH2   1 
ATOM   4090  N  N     . THR   A 1 512 ? 156.108 118.319 136.287 1.00 68.58  ?  512  THR   A N     1 
ATOM   4091  C  CA    . THR   A 1 512 ? 156.405 118.108 134.873 1.00 70.21  ?  512  THR   A CA    1 
ATOM   4092  C  C     . THR   A 1 512 ? 156.463 119.450 134.120 1.00 68.85  ?  512  THR   A C     1 
ATOM   4093  O  O     . THR   A 1 512 ? 155.665 120.339 134.369 1.00 71.81  ?  512  THR   A O     1 
ATOM   4094  C  CB    . THR   A 1 512 ? 155.344 117.197 134.256 1.00 73.43  ?  512  THR   A CB    1 
ATOM   4095  O  OG1   . THR   A 1 512 ? 154.041 117.734 134.520 1.00 76.50  ?  512  THR   A OG1   1 
ATOM   4096  C  CG2   . THR   A 1 512 ? 155.436 115.803 134.849 1.00 73.85  ?  512  THR   A CG2   1 
ATOM   4097  N  N     . LEU   A 1 513 ? 157.430 119.629 133.218 1.00 67.64  ?  513  LEU   A N     1 
ATOM   4098  C  CA    . LEU   A 1 513 ? 157.624 120.875 132.464 1.00 68.24  ?  513  LEU   A CA    1 
ATOM   4099  C  C     . LEU   A 1 513 ? 157.602 120.500 130.999 1.00 72.42  ?  513  LEU   A C     1 
ATOM   4100  O  O     . LEU   A 1 513 ? 158.074 119.437 130.668 1.00 74.65  ?  513  LEU   A O     1 
ATOM   4101  C  CB    . LEU   A 1 513 ? 158.971 121.525 132.799 1.00 64.36  ?  513  LEU   A CB    1 
ATOM   4102  C  CG    . LEU   A 1 513 ? 159.223 121.862 134.259 1.00 66.97  ?  513  LEU   A CG    1 
ATOM   4103  C  CD1   . LEU   A 1 513 ? 160.537 122.593 134.380 1.00 68.42  ?  513  LEU   A CD1   1 
ATOM   4104  C  CD2   . LEU   A 1 513 ? 158.089 122.692 134.814 1.00 68.08  ?  513  LEU   A CD2   1 
ATOM   4105  N  N     . GLY   A 1 514 ? 157.008 121.295 130.122 1.00 73.06  ?  514  GLY   A N     1 
ATOM   4106  C  CA    . GLY   A 1 514 ? 157.095 120.963 128.710 1.00 67.24  ?  514  GLY   A CA    1 
ATOM   4107  C  C     . GLY   A 1 514 ? 157.846 122.019 127.974 1.00 66.29  ?  514  GLY   A C     1 
ATOM   4108  O  O     . GLY   A 1 514 ? 157.210 122.858 127.371 1.00 73.11  ?  514  GLY   A O     1 
ATOM   4109  N  N     . ILE   A 1 515 ? 159.153 121.977 127.931 1.00 64.74  ?  515  ILE   A N     1 
ATOM   4110  C  CA    . ILE   A 1 515 ? 159.882 123.052 127.281 1.00 65.92  ?  515  ILE   A CA    1 
ATOM   4111  C  C     . ILE   A 1 515 ? 160.067 122.623 125.854 1.00 71.78  ?  515  ILE   A C     1 
ATOM   4112  O  O     . ILE   A 1 515 ? 160.507 121.517 125.593 1.00 74.39  ?  515  ILE   A O     1 
ATOM   4113  C  CB    . ILE   A 1 515 ? 161.221 123.362 127.975 1.00 61.95  ?  515  ILE   A CB    1 
ATOM   4114  C  CG1   . ILE   A 1 515 ? 160.971 124.124 129.277 1.00 64.65  ?  515  ILE   A CG1   1 
ATOM   4115  C  CG2   . ILE   A 1 515 ? 162.128 124.138 127.046 1.00 59.94  ?  515  ILE   A CG2   1 
ATOM   4116  C  CD1   . ILE   A 1 515 ? 162.066 123.943 130.276 1.00 70.19  ?  515  ILE   A CD1   1 
ATOM   4117  N  N     . GLY   A 1 516 ? 159.664 123.454 124.933 1.00 75.09  ?  516  GLY   A N     1 
ATOM   4118  C  CA    . GLY   A 1 516 ? 159.686 123.052 123.549 1.00 68.33  ?  516  GLY   A CA    1 
ATOM   4119  C  C     . GLY   A 1 516 ? 160.612 123.878 122.686 1.00 69.89  ?  516  GLY   A C     1 
ATOM   4120  O  O     . GLY   A 1 516 ? 161.601 124.433 123.173 1.00 81.63  ?  516  GLY   A O     1 
ATOM   4121  N  N     . VAL   A 1 517 ? 160.301 123.961 121.395 1.00 66.93  ?  517  VAL   A N     1 
ATOM   4122  C  CA    . VAL   A 1 517 ? 161.155 124.618 120.413 1.00 64.49  ?  517  VAL   A CA    1 
ATOM   4123  C  C     . VAL   A 1 517 ? 160.282 125.416 119.455 1.00 70.64  ?  517  VAL   A C     1 
ATOM   4124  O  O     . VAL   A 1 517 ? 159.205 124.963 119.056 1.00 80.95  ?  517  VAL   A O     1 
ATOM   4125  C  CB    . VAL   A 1 517 ? 162.017 123.592 119.644 1.00 64.25  ?  517  VAL   A CB    1 
ATOM   4126  C  CG1   . VAL   A 1 517 ? 162.710 124.242 118.462 1.00 68.50  ?  517  VAL   A CG1   1 
ATOM   4127  C  CG2   . VAL   A 1 517 ? 163.039 122.955 120.568 1.00 69.14  ?  517  VAL   A CG2   1 
ATOM   4128  N  N     . ILE   A 1 518 ? 160.745 126.614 119.095 1.00 73.49  ?  518  ILE   A N     1 
ATOM   4129  C  CA    . ILE   A 1 518 ? 160.141 127.412 118.038 1.00 73.68  ?  518  ILE   A CA    1 
ATOM   4130  C  C     . ILE   A 1 518 ? 161.233 127.787 117.044 1.00 74.89  ?  518  ILE   A C     1 
ATOM   4131  O  O     . ILE   A 1 518 ? 162.424 127.600 117.296 1.00 79.75  ?  518  ILE   A O     1 
ATOM   4132  C  CB    . ILE   A 1 518 ? 159.436 128.675 118.575 1.00 75.78  ?  518  ILE   A CB    1 
ATOM   4133  C  CG1   . ILE   A 1 518 ? 160.387 129.500 119.423 1.00 71.80  ?  518  ILE   A CG1   1 
ATOM   4134  C  CG2   . ILE   A 1 518 ? 158.201 128.299 119.376 1.00 78.37  ?  518  ILE   A CG2   1 
ATOM   4135  C  CD1   . ILE   A 1 518 ? 160.247 130.994 119.167 1.00 71.78  ?  518  ILE   A CD1   1 
ATOM   4136  N  N     . ASN   A 1 519 ? 160.804 128.316 115.896 1.00 76.42  ?  519  ASN   A N     1 
ATOM   4137  C  CA    . ASN   A 1 519 ? 161.711 128.777 114.843 1.00 79.33  ?  519  ASN   A CA    1 
ATOM   4138  C  C     . ASN   A 1 519 ? 162.581 127.642 114.306 1.00 79.25  ?  519  ASN   A C     1 
ATOM   4139  O  O     . ASN   A 1 519 ? 163.757 127.834 113.993 1.00 78.90  ?  519  ASN   A O     1 
ATOM   4140  C  CB    . ASN   A 1 519 ? 162.584 129.935 115.331 1.00 80.56  ?  519  ASN   A CB    1 
ATOM   4141  C  CG    . ASN   A 1 519 ? 162.689 131.052 114.318 1.00 83.49  ?  519  ASN   A CG    1 
ATOM   4142  O  OD1   . ASN   A 1 519 ? 162.003 131.046 113.297 1.00 85.17  ?  519  ASN   A OD1   1 
ATOM   4143  N  ND2   . ASN   A 1 519 ? 163.542 132.028 114.601 1.00 82.86  ?  519  ASN   A ND2   1 
ATOM   4144  N  N     . PHE   A 1 520 ? 162.000 126.447 114.194 1.00 76.31  ?  520  PHE   A N     1 
ATOM   4145  C  CA    . PHE   A 1 520 ? 162.760 125.318 113.670 1.00 71.86  ?  520  PHE   A CA    1 
ATOM   4146  C  C     . PHE   A 1 520 ? 162.928 125.401 112.158 1.00 75.36  ?  520  PHE   A C     1 
ATOM   4147  O  O     . PHE   A 1 520 ? 163.968 124.998 111.626 1.00 83.56  ?  520  PHE   A O     1 
ATOM   4148  C  CB    . PHE   A 1 520 ? 162.091 124.000 114.052 1.00 76.69  ?  520  PHE   A CB    1 
ATOM   4149  C  CG    . PHE   A 1 520 ? 162.887 122.788 113.665 1.00 78.22  ?  520  PHE   A CG    1 
ATOM   4150  C  CD1   . PHE   A 1 520 ? 164.135 122.560 114.217 1.00 74.75  ?  520  PHE   A CD1   1 
ATOM   4151  C  CD2   . PHE   A 1 520 ? 162.393 121.882 112.743 1.00 78.57  ?  520  PHE   A CD2   1 
ATOM   4152  C  CE1   . PHE   A 1 520 ? 164.872 121.449 113.862 1.00 74.85  ?  520  PHE   A CE1   1 
ATOM   4153  C  CE2   . PHE   A 1 520 ? 163.127 120.769 112.384 1.00 74.88  ?  520  PHE   A CE2   1 
ATOM   4154  C  CZ    . PHE   A 1 520 ? 164.367 120.553 112.945 1.00 73.00  ?  520  PHE   A CZ    1 
ATOM   4155  N  N     . ALA   A 1 521 ? 161.915 125.906 111.449 1.00 76.65  ?  521  ALA   A N     1 
ATOM   4156  C  CA    . ALA   A 1 521 ? 162.027 126.040 110.000 1.00 77.62  ?  521  ALA   A CA    1 
ATOM   4157  C  C     . ALA   A 1 521 ? 163.134 127.016 109.622 1.00 81.85  ?  521  ALA   A C     1 
ATOM   4158  O  O     . ALA   A 1 521 ? 163.920 126.753 108.704 1.00 84.19  ?  521  ALA   A O     1 
ATOM   4159  C  CB    . ALA   A 1 521 ? 160.691 126.485 109.409 1.00 81.08  ?  521  ALA   A CB    1 
ATOM   4160  N  N     . TYR   A 1 522 ? 163.215 128.148 110.324 1.00 82.06  ?  522  TYR   A N     1 
ATOM   4161  C  CA    . TYR   A 1 522 ? 164.296 129.097 110.078 1.00 79.10  ?  522  TYR   A CA    1 
ATOM   4162  C  C     . TYR   A 1 522 ? 165.644 128.504 110.466 1.00 79.93  ?  522  TYR   A C     1 
ATOM   4163  O  O     . TYR   A 1 522 ? 166.658 128.769 109.810 1.00 82.16  ?  522  TYR   A O     1 
ATOM   4164  C  CB    . TYR   A 1 522 ? 164.030 130.395 110.840 1.00 78.95  ?  522  TYR   A CB    1 
ATOM   4165  C  CG    . TYR   A 1 522 ? 165.212 131.335 110.913 1.00 82.42  ?  522  TYR   A CG    1 
ATOM   4166  C  CD1   . TYR   A 1 522 ? 165.844 131.782 109.761 1.00 87.91  ?  522  TYR   A CD1   1 
ATOM   4167  C  CD2   . TYR   A 1 522 ? 165.688 131.785 112.134 1.00 84.17  ?  522  TYR   A CD2   1 
ATOM   4168  C  CE1   . TYR   A 1 522 ? 166.922 132.642 109.827 1.00 91.29  ?  522  TYR   A CE1   1 
ATOM   4169  C  CE2   . TYR   A 1 522 ? 166.764 132.646 112.208 1.00 84.44  ?  522  TYR   A CE2   1 
ATOM   4170  C  CZ    . TYR   A 1 522 ? 167.377 133.071 111.053 1.00 90.17  ?  522  TYR   A CZ    1 
ATOM   4171  O  OH    . TYR   A 1 522 ? 168.449 133.929 111.125 1.00 92.85  ?  522  TYR   A OH    1 
ATOM   4172  N  N     . TYR   A 1 523 ? 165.673 127.697 111.529 1.00 82.28  ?  523  TYR   A N     1 
ATOM   4173  C  CA    . TYR   A 1 523 ? 166.909 127.032 111.926 1.00 80.96  ?  523  TYR   A CA    1 
ATOM   4174  C  C     . TYR   A 1 523 ? 167.395 126.080 110.839 1.00 80.27  ?  523  TYR   A C     1 
ATOM   4175  O  O     . TYR   A 1 523 ? 168.597 126.005 110.560 1.00 87.66  ?  523  TYR   A O     1 
ATOM   4176  C  CB    . TYR   A 1 523 ? 166.693 126.288 113.244 1.00 79.76  ?  523  TYR   A CB    1 
ATOM   4177  C  CG    . TYR   A 1 523 ? 167.903 125.536 113.747 1.00 81.12  ?  523  TYR   A CG    1 
ATOM   4178  C  CD1   . TYR   A 1 523 ? 168.971 126.205 114.325 1.00 80.98  ?  523  TYR   A CD1   1 
ATOM   4179  C  CD2   . TYR   A 1 523 ? 167.971 124.154 113.654 1.00 81.53  ?  523  TYR   A CD2   1 
ATOM   4180  C  CE1   . TYR   A 1 523 ? 170.075 125.519 114.790 1.00 80.96  ?  523  TYR   A CE1   1 
ATOM   4181  C  CE2   . TYR   A 1 523 ? 169.070 123.461 114.115 1.00 80.28  ?  523  TYR   A CE2   1 
ATOM   4182  C  CZ    . TYR   A 1 523 ? 170.119 124.148 114.683 1.00 80.93  ?  523  TYR   A CZ    1 
ATOM   4183  O  OH    . TYR   A 1 523 ? 171.217 123.460 115.144 1.00 84.43  ?  523  TYR   A OH    1 
ATOM   4184  N  N     . LEU   A 1 524 ? 166.473 125.339 110.221 1.00 72.69  ?  524  LEU   A N     1 
ATOM   4185  C  CA    . LEU   A 1 524 ? 166.842 124.468 109.110 1.00 72.80  ?  524  LEU   A CA    1 
ATOM   4186  C  C     . LEU   A 1 524 ? 167.286 125.273 107.895 1.00 79.13  ?  524  LEU   A C     1 
ATOM   4187  O  O     . LEU   A 1 524 ? 168.270 124.918 107.235 1.00 82.33  ?  524  LEU   A O     1 
ATOM   4188  C  CB    . LEU   A 1 524 ? 165.669 123.559 108.744 1.00 73.59  ?  524  LEU   A CB    1 
ATOM   4189  C  CG    . LEU   A 1 524 ? 165.348 122.411 109.699 1.00 77.20  ?  524  LEU   A CG    1 
ATOM   4190  C  CD1   . LEU   A 1 524 ? 164.344 121.463 109.065 1.00 77.94  ?  524  LEU   A CD1   1 
ATOM   4191  C  CD2   . LEU   A 1 524 ? 166.614 121.671 110.091 1.00 79.15  ?  524  LEU   A CD2   1 
ATOM   4192  N  N     . ALA   A 1 525 ? 166.570 126.355 107.581 1.00 83.92  ?  525  ALA   A N     1 
ATOM   4193  C  CA    . ALA   A 1 525 ? 166.893 127.145 106.397 1.00 85.02  ?  525  ALA   A CA    1 
ATOM   4194  C  C     . ALA   A 1 525 ? 168.261 127.805 106.520 1.00 91.32  ?  525  ALA   A C     1 
ATOM   4195  O  O     . ALA   A 1 525 ? 169.007 127.886 105.537 1.00 94.25  ?  525  ALA   A O     1 
ATOM   4196  C  CB    . ALA   A 1 525 ? 165.809 128.195 106.155 1.00 87.83  ?  525  ALA   A CB    1 
ATOM   4197  N  N     . LYS   A 1 526 ? 168.604 128.290 107.716 1.00 89.76  ?  526  LYS   A N     1 
ATOM   4198  C  CA    . LYS   A 1 526 ? 169.901 128.930 107.910 1.00 86.86  ?  526  LYS   A CA    1 
ATOM   4199  C  C     . LYS   A 1 526 ? 171.046 127.947 107.705 1.00 85.96  ?  526  LYS   A C     1 
ATOM   4200  O  O     . LYS   A 1 526 ? 172.139 128.345 107.286 1.00 90.16  ?  526  LYS   A O     1 
ATOM   4201  C  CB    . LYS   A 1 526 ? 169.970 129.554 109.305 1.00 87.38  ?  526  LYS   A CB    1 
ATOM   4202  C  CG    . LYS   A 1 526 ? 171.285 130.245 109.625 1.00 90.68  ?  526  LYS   A CG    1 
ATOM   4203  C  CD    . LYS   A 1 526 ? 171.174 131.089 110.885 1.00 90.28  ?  526  LYS   A CD    1 
ATOM   4204  C  CE    . LYS   A 1 526 ? 170.590 130.287 112.036 1.00 90.91  ?  526  LYS   A CE    1 
ATOM   4205  N  NZ    . LYS   A 1 526 ? 169.585 131.071 112.802 1.00 89.55  ?  526  LYS   A NZ    1 
ATOM   4206  N  N     . HIS   A 1 527 ? 170.816 126.667 107.980 1.00 85.13  ?  527  HIS   A N     1 
ATOM   4207  C  CA    . HIS   A 1 527 ? 171.827 125.635 107.811 1.00 86.61  ?  527  HIS   A CA    1 
ATOM   4208  C  C     . HIS   A 1 527 ? 171.769 124.964 106.445 1.00 87.53  ?  527  HIS   A C     1 
ATOM   4209  O  O     . HIS   A 1 527 ? 172.513 124.007 106.208 1.00 88.52  ?  527  HIS   A O     1 
ATOM   4210  C  CB    . HIS   A 1 527 ? 171.689 124.579 108.911 1.00 88.97  ?  527  HIS   A CB    1 
ATOM   4211  C  CG    . HIS   A 1 527 ? 172.403 124.931 110.178 1.00 90.01  ?  527  HIS   A CG    1 
ATOM   4212  N  ND1   . HIS   A 1 527 ? 171.781 125.564 111.232 1.00 88.06  ?  527  HIS   A ND1   1 
ATOM   4213  C  CD2   . HIS   A 1 527 ? 173.688 124.740 110.560 1.00 88.20  ?  527  HIS   A CD2   1 
ATOM   4214  C  CE1   . HIS   A 1 527 ? 172.651 125.748 112.208 1.00 91.12  ?  527  HIS   A CE1   1 
ATOM   4215  N  NE2   . HIS   A 1 527 ? 173.816 125.256 111.826 1.00 91.64  ?  527  HIS   A NE2   1 
ATOM   4216  N  N     . GLY   A 1 528 ? 170.910 125.438 105.548 1.00 81.72  ?  528  GLY   A N     1 
ATOM   4217  C  CA    . GLY   A 1 528 ? 170.794 124.849 104.225 1.00 82.43  ?  528  GLY   A CA    1 
ATOM   4218  C  C     . GLY   A 1 528 ? 170.242 123.440 104.212 1.00 84.50  ?  528  GLY   A C     1 
ATOM   4219  O  O     . GLY   A 1 528 ? 170.756 122.584 103.481 1.00 86.25  ?  528  GLY   A O     1 
ATOM   4220  N  N     . LYS   A 1 529 ? 169.205 123.176 105.002 1.00 83.91  ?  529  LYS   A N     1 
ATOM   4221  C  CA    . LYS   A 1 529 ? 168.571 121.869 105.058 1.00 82.69  ?  529  LYS   A CA    1 
ATOM   4222  C  C     . LYS   A 1 529 ? 167.091 122.000 104.729 1.00 81.63  ?  529  LYS   A C     1 
ATOM   4223  O  O     . LYS   A 1 529 ? 166.487 123.060 104.917 1.00 84.51  ?  529  LYS   A O     1 
ATOM   4224  C  CB    . LYS   A 1 529 ? 168.746 121.221 106.436 1.00 84.36  ?  529  LYS   A CB    1 
ATOM   4225  C  CG    . LYS   A 1 529 ? 170.164 121.287 106.971 1.00 86.94  ?  529  LYS   A CG    1 
ATOM   4226  C  CD    . LYS   A 1 529 ? 170.932 120.017 106.656 1.00 82.59  ?  529  LYS   A CD    1 
ATOM   4227  C  CE    . LYS   A 1 529 ? 172.411 120.300 106.463 1.00 82.89  ?  529  LYS   A CE    1 
ATOM   4228  N  NZ    . LYS   A 1 529 ? 173.131 119.129 105.892 1.00 85.46  ?  529  LYS   A NZ    1 
ATOM   4229  N  N     . ARG   A 1 530 ? 166.512 120.911 104.232 1.00 98.10  ?  530  ARG   A N     1 
ATOM   4230  C  CA    . ARG   A 1 530 ? 165.132 120.895 103.774 1.00 98.59  ?  530  ARG   A CA    1 
ATOM   4231  C  C     . ARG   A 1 530 ? 164.341 119.821 104.511 1.00 96.64  ?  530  ARG   A C     1 
ATOM   4232  O  O     . ARG   A 1 530 ? 164.901 118.864 105.053 1.00 100.40 ?  530  ARG   A O     1 
ATOM   4233  C  CB    . ARG   A 1 530 ? 165.057 120.663 102.260 1.00 96.02  ?  530  ARG   A CB    1 
ATOM   4234  C  CG    . ARG   A 1 530 ? 166.224 121.253 101.484 1.00 98.08  ?  530  ARG   A CG    1 
ATOM   4235  C  CD    . ARG   A 1 530 ? 165.845 121.543 100.042 1.00 96.22  ?  530  ARG   A CD    1 
ATOM   4236  N  NE    . ARG   A 1 530 ? 164.796 122.550 99.947  1.00 98.40  ?  530  ARG   A NE    1 
ATOM   4237  C  CZ    . ARG   A 1 530 ? 165.014 123.858 99.930  1.00 100.87 ?  530  ARG   A CZ    1 
ATOM   4238  N  NH1   . ARG   A 1 530 ? 166.238 124.355 100.000 1.00 99.93  ?  530  ARG   A NH1   1 
ATOM   4239  N  NH2   . ARG   A 1 530 ? 163.979 124.687 99.839  1.00 100.17 ?  530  ARG   A NH2   1 
ATOM   4240  N  N     . TYR   A 1 531 ? 163.018 119.997 104.520 1.00 89.84  ?  531  TYR   A N     1 
ATOM   4241  C  CA    . TYR   A 1 531 ? 162.148 119.098 105.272 1.00 91.11  ?  531  TYR   A CA    1 
ATOM   4242  C  C     . TYR   A 1 531 ? 162.000 117.745 104.587 1.00 98.94  ?  531  TYR   A C     1 
ATOM   4243  O  O     . TYR   A 1 531 ? 162.003 116.703 105.253 1.00 100.84 ?  531  TYR   A O     1 
ATOM   4244  C  CB    . TYR   A 1 531 ? 160.773 119.739 105.459 1.00 92.61  ?  531  TYR   A CB    1 
ATOM   4245  C  CG    . TYR   A 1 531 ? 160.623 120.554 106.721 1.00 96.39  ?  531  TYR   A CG    1 
ATOM   4246  C  CD1   . TYR   A 1 531 ? 160.935 121.906 106.740 1.00 97.56  ?  531  TYR   A CD1   1 
ATOM   4247  C  CD2   . TYR   A 1 531 ? 160.153 119.975 107.891 1.00 96.93  ?  531  TYR   A CD2   1 
ATOM   4248  C  CE1   . TYR   A 1 531 ? 160.793 122.655 107.890 1.00 96.14  ?  531  TYR   A CE1   1 
ATOM   4249  C  CE2   . TYR   A 1 531 ? 160.007 120.717 109.046 1.00 96.65  ?  531  TYR   A CE2   1 
ATOM   4250  C  CZ    . TYR   A 1 531 ? 160.328 122.056 109.040 1.00 97.46  ?  531  TYR   A CZ    1 
ATOM   4251  O  OH    . TYR   A 1 531 ? 160.185 122.798 110.189 1.00 103.51 ?  531  TYR   A OH    1 
ATOM   4252  N  N     . SER   A 1 532 ? 161.865 117.737 103.261 1.00 108.01 ?  532  SER   A N     1 
ATOM   4253  C  CA    . SER   A 1 532 ? 161.384 116.557 102.551 1.00 103.81 ?  532  SER   A CA    1 
ATOM   4254  C  C     . SER   A 1 532 ? 162.488 115.572 102.181 1.00 104.80 ?  532  SER   A C     1 
ATOM   4255  O  O     . SER   A 1 532 ? 162.310 114.361 102.348 1.00 108.15 ?  532  SER   A O     1 
ATOM   4256  C  CB    . SER   A 1 532 ? 160.633 116.983 101.288 1.00 103.76 ?  532  SER   A CB    1 
ATOM   4257  O  OG    . SER   A 1 532 ? 161.308 118.037 100.624 1.00 105.18 ?  532  SER   A OG    1 
ATOM   4258  N  N     . ASP   A 1 533 ? 163.624 116.058 101.678 1.00 109.63 ?  533  ASP   A N     1 
ATOM   4259  C  CA    . ASP   A 1 533 ? 164.651 115.161 101.159 1.00 109.77 ?  533  ASP   A CA    1 
ATOM   4260  C  C     . ASP   A 1 533 ? 165.348 114.349 102.243 1.00 111.13 ?  533  ASP   A C     1 
ATOM   4261  O  O     . ASP   A 1 533 ? 166.077 113.408 101.911 1.00 110.81 ?  533  ASP   A O     1 
ATOM   4262  C  CB    . ASP   A 1 533 ? 165.694 115.953 100.371 1.00 111.91 ?  533  ASP   A CB    1 
ATOM   4263  C  CG    . ASP   A 1 533 ? 166.001 117.295 100.996 1.00 115.67 ?  533  ASP   A CG    1 
ATOM   4264  O  OD1   . ASP   A 1 533 ? 166.244 117.343 102.220 1.00 115.57 ?  533  ASP   A OD1   1 
ATOM   4265  O  OD2   . ASP   A 1 533 ? 166.004 118.302 100.261 1.00 116.11 ?  533  ASP   A OD2   1 
ATOM   4266  N  N     . GLY   A 1 534 ? 165.149 114.681 103.516 1.00 103.82 ?  534  GLY   A N     1 
ATOM   4267  C  CA    . GLY   A 1 534 ? 165.830 113.979 104.582 1.00 103.18 ?  534  GLY   A CA    1 
ATOM   4268  C  C     . GLY   A 1 534 ? 167.235 114.454 104.864 1.00 102.77 ?  534  GLY   A C     1 
ATOM   4269  O  O     . GLY   A 1 534 ? 167.965 113.777 105.597 1.00 105.73 ?  534  GLY   A O     1 
ATOM   4270  N  N     . SER   A 1 535 ? 167.644 115.592 104.300 1.00 91.18  ?  535  SER   A N     1 
ATOM   4271  C  CA    . SER   A 1 535 ? 168.978 116.119 104.559 1.00 89.14  ?  535  SER   A CA    1 
ATOM   4272  C  C     . SER   A 1 535 ? 169.113 116.692 105.963 1.00 92.85  ?  535  SER   A C     1 
ATOM   4273  O  O     . SER   A 1 535 ? 170.239 116.883 106.434 1.00 98.82  ?  535  SER   A O     1 
ATOM   4274  C  CB    . SER   A 1 535 ? 169.328 117.191 103.528 1.00 92.54  ?  535  SER   A CB    1 
ATOM   4275  O  OG    . SER   A 1 535 ? 168.357 118.223 103.516 1.00 92.40  ?  535  SER   A OG    1 
ATOM   4276  N  N     . ALA   A 1 536 ? 168.000 116.964 106.638 1.00 85.30  ?  536  ALA   A N     1 
ATOM   4277  C  CA    . ALA   A 1 536 ? 168.010 117.562 107.964 1.00 84.34  ?  536  ALA   A CA    1 
ATOM   4278  C  C     . ALA   A 1 536 ? 167.977 116.530 109.083 1.00 85.94  ?  536  ALA   A C     1 
ATOM   4279  O  O     . ALA   A 1 536 ? 167.878 116.910 110.253 1.00 94.89  ?  536  ALA   A O     1 
ATOM   4280  C  CB    . ALA   A 1 536 ? 166.829 118.524 108.115 1.00 81.53  ?  536  ALA   A CB    1 
ATOM   4281  N  N     . ASN   A 1 537 ? 168.054 115.239 108.752 1.00 78.22  ?  537  ASN   A N     1 
ATOM   4282  C  CA    . ASN   A 1 537 ? 167.945 114.199 109.771 1.00 77.00  ?  537  ASN   A CA    1 
ATOM   4283  C  C     . ASN   A 1 537 ? 169.074 114.297 110.791 1.00 82.01  ?  537  ASN   A C     1 
ATOM   4284  O  O     . ASN   A 1 537 ? 168.835 114.269 112.004 1.00 85.38  ?  537  ASN   A O     1 
ATOM   4285  C  CB    . ASN   A 1 537 ? 167.935 112.822 109.107 1.00 74.33  ?  537  ASN   A CB    1 
ATOM   4286  C  CG    . ASN   A 1 537 ? 166.653 112.551 108.345 1.00 78.75  ?  537  ASN   A CG    1 
ATOM   4287  O  OD1   . ASN   A 1 537 ? 166.033 113.467 107.808 1.00 82.27  ?  537  ASN   A OD1   1 
ATOM   4288  N  ND2   . ASN   A 1 537 ? 166.251 111.288 108.291 1.00 82.89  ?  537  ASN   A ND2   1 
ATOM   4289  N  N     . ASN   A 1 538 ? 170.315 114.422 110.316 1.00 79.02  ?  538  ASN   A N     1 
ATOM   4290  C  CA    . ASN   A 1 538 ? 171.453 114.482 111.228 1.00 77.38  ?  538  ASN   A CA    1 
ATOM   4291  C  C     . ASN   A 1 538 ? 171.454 115.774 112.036 1.00 79.66  ?  538  ASN   A C     1 
ATOM   4292  O  O     . ASN   A 1 538 ? 171.745 115.761 113.239 1.00 86.99  ?  538  ASN   A O     1 
ATOM   4293  C  CB    . ASN   A 1 538 ? 172.756 114.332 110.444 1.00 77.07  ?  538  ASN   A CB    1 
ATOM   4294  C  CG    . ASN   A 1 538 ? 173.001 112.906 109.994 1.00 80.10  ?  538  ASN   A CG    1 
ATOM   4295  O  OD1   . ASN   A 1 538 ? 172.208 112.009 110.276 1.00 80.26  ?  538  ASN   A OD1   1 
ATOM   4296  N  ND2   . ASN   A 1 538 ? 174.105 112.689 109.292 1.00 82.04  ?  538  ASN   A ND2   1 
ATOM   4297  N  N     . LEU   A 1 539 ? 171.135 116.900 111.393 1.00 72.99  ?  539  LEU   A N     1 
ATOM   4298  C  CA    . LEU   A 1 539 ? 171.088 118.169 112.111 1.00 76.99  ?  539  LEU   A CA    1 
ATOM   4299  C  C     . LEU   A 1 539 ? 169.993 118.163 113.170 1.00 78.54  ?  539  LEU   A C     1 
ATOM   4300  O  O     . LEU   A 1 539 ? 170.204 118.634 114.294 1.00 83.73  ?  539  LEU   A O     1 
ATOM   4301  C  CB    . LEU   A 1 539 ? 170.881 119.321 111.128 1.00 73.88  ?  539  LEU   A CB    1 
ATOM   4302  C  CG    . LEU   A 1 539 ? 170.774 120.712 111.752 1.00 76.13  ?  539  LEU   A CG    1 
ATOM   4303  C  CD1   . LEU   A 1 539 ? 172.115 121.146 112.313 1.00 75.72  ?  539  LEU   A CD1   1 
ATOM   4304  C  CD2   . LEU   A 1 539 ? 170.267 121.715 110.733 1.00 78.76  ?  539  LEU   A CD2   1 
ATOM   4305  N  N     . THR   A 1 540 ? 168.816 117.632 112.829 1.00 69.68  ?  540  THR   A N     1 
ATOM   4306  C  CA    . THR   A 1 540 ? 167.740 117.522 113.808 1.00 68.72  ?  540  THR   A CA    1 
ATOM   4307  C  C     . THR   A 1 540 ? 168.142 116.615 114.962 1.00 74.72  ?  540  THR   A C     1 
ATOM   4308  O  O     . THR   A 1 540 ? 167.884 116.931 116.132 1.00 82.38  ?  540  THR   A O     1 
ATOM   4309  C  CB    . THR   A 1 540 ? 166.470 116.999 113.135 1.00 70.92  ?  540  THR   A CB    1 
ATOM   4310  O  OG1   . THR   A 1 540 ? 166.094 117.879 112.069 1.00 84.06  ?  540  THR   A OG1   1 
ATOM   4311  C  CG2   . THR   A 1 540 ? 165.332 116.907 114.132 1.00 72.10  ?  540  THR   A CG2   1 
ATOM   4312  N  N     . HIS   A 1 541 ? 168.783 115.486 114.649 1.00 69.19  ?  541  HIS   A N     1 
ATOM   4313  C  CA    . HIS   A 1 541 ? 169.257 114.580 115.688 1.00 68.57  ?  541  HIS   A CA    1 
ATOM   4314  C  C     . HIS   A 1 541 ? 170.195 115.296 116.649 1.00 71.67  ?  541  HIS   A C     1 
ATOM   4315  O  O     . HIS   A 1 541 ? 170.009 115.243 117.870 1.00 80.90  ?  541  HIS   A O     1 
ATOM   4316  C  CB    . HIS   A 1 541 ? 169.955 113.379 115.047 1.00 69.27  ?  541  HIS   A CB    1 
ATOM   4317  C  CG    . HIS   A 1 541 ? 170.181 112.235 115.985 1.00 74.67  ?  541  HIS   A CG    1 
ATOM   4318  N  ND1   . HIS   A 1 541 ? 171.334 112.098 116.727 1.00 74.63  ?  541  HIS   A ND1   1 
ATOM   4319  C  CD2   . HIS   A 1 541 ? 169.406 111.169 116.295 1.00 74.46  ?  541  HIS   A CD2   1 
ATOM   4320  C  CE1   . HIS   A 1 541 ? 171.257 111.000 117.458 1.00 74.22  ?  541  HIS   A CE1   1 
ATOM   4321  N  NE2   . HIS   A 1 541 ? 170.097 110.418 117.214 1.00 73.42  ?  541  HIS   A NE2   1 
ATOM   4322  N  N     . LYS   A 1 542 ? 171.199 115.991 116.110 1.00 74.81  ?  542  LYS   A N     1 
ATOM   4323  C  CA    . LYS   A 1 542 ? 172.169 116.681 116.956 1.00 75.71  ?  542  LYS   A CA    1 
ATOM   4324  C  C     . LYS   A 1 542 ? 171.501 117.765 117.794 1.00 75.73  ?  542  LYS   A C     1 
ATOM   4325  O  O     . LYS   A 1 542 ? 171.746 117.873 119.003 1.00 82.52  ?  542  LYS   A O     1 
ATOM   4326  C  CB    . LYS   A 1 542 ? 173.280 117.277 116.091 1.00 76.82  ?  542  LYS   A CB    1 
ATOM   4327  C  CG    . LYS   A 1 542 ? 174.529 117.665 116.861 1.00 83.52  ?  542  LYS   A CG    1 
ATOM   4328  C  CD    . LYS   A 1 542 ? 175.601 118.205 115.932 1.00 84.33  ?  542  LYS   A CD    1 
ATOM   4329  C  CE    . LYS   A 1 542 ? 175.358 119.667 115.601 1.00 86.38  ?  542  LYS   A CE    1 
ATOM   4330  N  NZ    . LYS   A 1 542 ? 176.429 120.545 116.147 1.00 83.01  ?  542  LYS   A NZ    1 
ATOM   4331  N  N     . THR   A 1 543 ? 170.640 118.571 117.168 1.00 70.92  ?  543  THR   A N     1 
ATOM   4332  C  CA    . THR   A 1 543 ? 170.012 119.684 117.872 1.00 69.59  ?  543  THR   A CA    1 
ATOM   4333  C  C     . THR   A 1 543 ? 169.144 119.190 119.022 1.00 70.99  ?  543  THR   A C     1 
ATOM   4334  O  O     . THR   A 1 543 ? 169.237 119.694 120.149 1.00 77.85  ?  543  THR   A O     1 
ATOM   4335  C  CB    . THR   A 1 543 ? 169.181 120.516 116.895 1.00 69.73  ?  543  THR   A CB    1 
ATOM   4336  O  OG1   . THR   A 1 543 ? 170.050 121.167 115.961 1.00 79.48  ?  543  THR   A OG1   1 
ATOM   4337  C  CG2   . THR   A 1 543 ? 168.367 121.561 117.639 1.00 70.41  ?  543  THR   A CG2   1 
ATOM   4338  N  N     . PHE   A 1 544 ? 168.302 118.190 118.764 1.00 64.42  ?  544  PHE   A N     1 
ATOM   4339  C  CA    . PHE   A 1 544 ? 167.394 117.748 119.811 1.00 61.81  ?  544  PHE   A CA    1 
ATOM   4340  C  C     . PHE   A 1 544 ? 168.101 116.898 120.859 1.00 64.79  ?  544  PHE   A C     1 
ATOM   4341  O  O     . PHE   A 1 544 ? 167.694 116.908 122.027 1.00 74.84  ?  544  PHE   A O     1 
ATOM   4342  C  CB    . PHE   A 1 544 ? 166.205 117.021 119.190 1.00 62.57  ?  544  PHE   A CB    1 
ATOM   4343  C  CG    . PHE   A 1 544 ? 165.193 117.956 118.592 1.00 68.84  ?  544  PHE   A CG    1 
ATOM   4344  C  CD1   . PHE   A 1 544 ? 165.397 118.509 117.341 1.00 68.75  ?  544  PHE   A CD1   1 
ATOM   4345  C  CD2   . PHE   A 1 544 ? 164.063 118.318 119.298 1.00 69.38  ?  544  PHE   A CD2   1 
ATOM   4346  C  CE1   . PHE   A 1 544 ? 164.478 119.383 116.796 1.00 66.03  ?  544  PHE   A CE1   1 
ATOM   4347  C  CE2   . PHE   A 1 544 ? 163.140 119.191 118.760 1.00 67.32  ?  544  PHE   A CE2   1 
ATOM   4348  C  CZ    . PHE   A 1 544 ? 163.350 119.726 117.508 1.00 66.01  ?  544  PHE   A CZ    1 
ATOM   4349  N  N     . GLU   A 1 545 ? 169.182 116.202 120.489 1.00 72.01  ?  545  GLU   A N     1 
ATOM   4350  C  CA    . GLU   A 1 545 ? 170.010 115.563 121.504 1.00 72.63  ?  545  GLU   A CA    1 
ATOM   4351  C  C     . GLU   A 1 545 ? 170.617 116.597 122.439 1.00 74.66  ?  545  GLU   A C     1 
ATOM   4352  O  O     . GLU   A 1 545 ? 170.614 116.414 123.662 1.00 78.02  ?  545  GLU   A O     1 
ATOM   4353  C  CB    . GLU   A 1 545 ? 171.112 114.732 120.848 1.00 72.82  ?  545  GLU   A CB    1 
ATOM   4354  C  CG    . GLU   A 1 545 ? 171.899 113.881 121.831 1.00 74.62  ?  545  GLU   A CG    1 
ATOM   4355  C  CD    . GLU   A 1 545 ? 173.391 113.925 121.581 1.00 81.06  ?  545  GLU   A CD    1 
ATOM   4356  O  OE1   . GLU   A 1 545 ? 173.807 114.488 120.549 1.00 84.34  ?  545  GLU   A OE1   1 
ATOM   4357  O  OE2   . GLU   A 1 545 ? 174.150 113.395 122.419 1.00 81.91  ?  545  GLU   A OE2   1 
ATOM   4358  N  N     . ALA   A 1 546 ? 171.137 117.695 121.883 1.00 69.60  ?  546  ALA   A N     1 
ATOM   4359  C  CA    . ALA   A 1 546 ? 171.685 118.753 122.724 1.00 63.18  ?  546  ALA   A CA    1 
ATOM   4360  C  C     . ALA   A 1 546 ? 170.614 119.346 123.628 1.00 66.83  ?  546  ALA   A C     1 
ATOM   4361  O  O     . ALA   A 1 546 ? 170.853 119.577 124.821 1.00 75.05  ?  546  ALA   A O     1 
ATOM   4362  C  CB    . ALA   A 1 546 ? 172.317 119.841 121.856 1.00 65.77  ?  546  ALA   A CB    1 
ATOM   4363  N  N     . ILE   A 1 547 ? 169.421 119.587 123.078 1.00 65.48  ?  547  ILE   A N     1 
ATOM   4364  C  CA    . ILE   A 1 547 ? 168.337 120.167 123.868 1.00 63.76  ?  547  ILE   A CA    1 
ATOM   4365  C  C     . ILE   A 1 547 ? 167.979 119.255 125.035 1.00 59.79  ?  547  ILE   A C     1 
ATOM   4366  O  O     . ILE   A 1 547 ? 167.900 119.696 126.189 1.00 66.32  ?  547  ILE   A O     1 
ATOM   4367  C  CB    . ILE   A 1 547 ? 167.112 120.444 122.977 1.00 61.21  ?  547  ILE   A CB    1 
ATOM   4368  C  CG1   . ILE   A 1 547 ? 167.387 121.619 122.040 1.00 62.47  ?  547  ILE   A CG1   1 
ATOM   4369  C  CG2   . ILE   A 1 547 ? 165.882 120.717 123.830 1.00 57.57  ?  547  ILE   A CG2   1 
ATOM   4370  C  CD1   . ILE   A 1 547 ? 166.424 121.711 120.883 1.00 62.65  ?  547  ILE   A CD1   1 
ATOM   4371  N  N     . GLN   A 1 548 ? 167.760 117.968 124.753 1.00 60.12  ?  548  GLN   A N     1 
ATOM   4372  C  CA    . GLN   A 1 548 ? 167.366 117.042 125.809 1.00 61.58  ?  548  GLN   A CA    1 
ATOM   4373  C  C     . GLN   A 1 548 ? 168.471 116.876 126.844 1.00 67.89  ?  548  GLN   A C     1 
ATOM   4374  O  O     . GLN   A 1 548 ? 168.198 116.839 128.050 1.00 70.55  ?  548  GLN   A O     1 
ATOM   4375  C  CB    . GLN   A 1 548 ? 166.984 115.688 125.212 1.00 60.75  ?  548  GLN   A CB    1 
ATOM   4376  C  CG    . GLN   A 1 548 ? 166.402 114.715 126.224 1.00 57.43  ?  548  GLN   A CG    1 
ATOM   4377  C  CD    . GLN   A 1 548 ? 165.103 115.207 126.831 1.00 64.35  ?  548  GLN   A CD    1 
ATOM   4378  O  OE1   . GLN   A 1 548 ? 164.369 115.978 126.215 1.00 68.65  ?  548  GLN   A OE1   1 
ATOM   4379  N  NE2   . GLN   A 1 548 ? 164.813 114.763 128.047 1.00 64.35  ?  548  GLN   A NE2   1 
ATOM   4380  N  N     . TYR   A 1 549 ? 169.726 116.782 126.395 1.00 69.24  ?  549  TYR   A N     1 
ATOM   4381  C  CA    . TYR   A 1 549 ? 170.834 116.622 127.329 1.00 64.05  ?  549  TYR   A CA    1 
ATOM   4382  C  C     . TYR   A 1 549 ? 170.949 117.822 128.258 1.00 68.09  ?  549  TYR   A C     1 
ATOM   4383  O  O     . TYR   A 1 549 ? 171.119 117.662 129.472 1.00 73.89  ?  549  TYR   A O     1 
ATOM   4384  C  CB    . TYR   A 1 549 ? 172.139 116.411 126.561 1.00 69.43  ?  549  TYR   A CB    1 
ATOM   4385  C  CG    . TYR   A 1 549 ? 173.376 116.427 127.430 1.00 68.95  ?  549  TYR   A CG    1 
ATOM   4386  C  CD1   . TYR   A 1 549 ? 173.791 115.285 128.098 1.00 70.75  ?  549  TYR   A CD1   1 
ATOM   4387  C  CD2   . TYR   A 1 549 ? 174.132 117.582 127.578 1.00 68.40  ?  549  TYR   A CD2   1 
ATOM   4388  C  CE1   . TYR   A 1 549 ? 174.920 115.293 128.893 1.00 74.00  ?  549  TYR   A CE1   1 
ATOM   4389  C  CE2   . TYR   A 1 549 ? 175.261 117.599 128.371 1.00 66.81  ?  549  TYR   A CE2   1 
ATOM   4390  C  CZ    . TYR   A 1 549 ? 175.651 116.452 129.025 1.00 71.62  ?  549  TYR   A CZ    1 
ATOM   4391  O  OH    . TYR   A 1 549 ? 176.777 116.463 129.816 1.00 76.12  ?  549  TYR   A OH    1 
ATOM   4392  N  N     . TYR   A 1 550 ? 170.848 119.035 127.710 1.00 69.99  ?  550  TYR   A N     1 
ATOM   4393  C  CA    . TYR   A 1 550 ? 171.000 120.219 128.547 1.00 64.83  ?  550  TYR   A CA    1 
ATOM   4394  C  C     . TYR   A 1 550 ? 169.807 120.400 129.477 1.00 70.80  ?  550  TYR   A C     1 
ATOM   4395  O  O     . TYR   A 1 550 ? 169.972 120.824 130.627 1.00 78.11  ?  550  TYR   A O     1 
ATOM   4396  C  CB    . TYR   A 1 550 ? 171.216 121.450 127.672 1.00 69.72  ?  550  TYR   A CB    1 
ATOM   4397  C  CG    . TYR   A 1 550 ? 172.622 121.530 127.128 1.00 74.88  ?  550  TYR   A CG    1 
ATOM   4398  C  CD1   . TYR   A 1 550 ? 173.705 121.137 127.902 1.00 70.95  ?  550  TYR   A CD1   1 
ATOM   4399  C  CD2   . TYR   A 1 550 ? 172.868 121.985 125.841 1.00 74.75  ?  550  TYR   A CD2   1 
ATOM   4400  C  CE1   . TYR   A 1 550 ? 174.993 121.200 127.412 1.00 71.99  ?  550  TYR   A CE1   1 
ATOM   4401  C  CE2   . TYR   A 1 550 ? 174.156 122.051 125.342 1.00 77.82  ?  550  TYR   A CE2   1 
ATOM   4402  C  CZ    . TYR   A 1 550 ? 175.214 121.659 126.133 1.00 77.82  ?  550  TYR   A CZ    1 
ATOM   4403  O  OH    . TYR   A 1 550 ? 176.497 121.723 125.643 1.00 77.69  ?  550  TYR   A OH    1 
ATOM   4404  N  N     . LEU   A 1 551 ? 168.599 120.066 129.012 1.00 63.22  ?  551  LEU   A N     1 
ATOM   4405  C  CA    . LEU   A 1 551 ? 167.439 120.119 129.896 1.00 59.39  ?  551  LEU   A CA    1 
ATOM   4406  C  C     . LEU   A 1 551 ? 167.582 119.132 131.048 1.00 60.56  ?  551  LEU   A C     1 
ATOM   4407  O  O     . LEU   A 1 551 ? 167.302 119.470 132.206 1.00 65.45  ?  551  LEU   A O     1 
ATOM   4408  C  CB    . LEU   A 1 551 ? 166.162 119.838 129.106 1.00 60.96  ?  551  LEU   A CB    1 
ATOM   4409  C  CG    . LEU   A 1 551 ? 165.613 120.982 128.252 1.00 66.17  ?  551  LEU   A CG    1 
ATOM   4410  C  CD1   . LEU   A 1 551 ? 164.309 120.572 127.591 1.00 66.65  ?  551  LEU   A CD1   1 
ATOM   4411  C  CD2   . LEU   A 1 551 ? 165.421 122.236 129.089 1.00 63.70  ?  551  LEU   A CD2   1 
ATOM   4412  N  N     . LEU   A 1 552 ? 168.031 117.910 130.751 1.00 66.04  ?  552  LEU   A N     1 
ATOM   4413  C  CA    . LEU   A 1 552 ? 168.219 116.915 131.800 1.00 66.96  ?  552  LEU   A CA    1 
ATOM   4414  C  C     . LEU   A 1 552 ? 169.303 117.342 132.779 1.00 68.42  ?  552  LEU   A C     1 
ATOM   4415  O  O     . LEU   A 1 552 ? 169.162 117.151 133.991 1.00 73.82  ?  552  LEU   A O     1 
ATOM   4416  C  CB    . LEU   A 1 552 ? 168.556 115.558 131.182 1.00 69.53  ?  552  LEU   A CB    1 
ATOM   4417  C  CG    . LEU   A 1 552 ? 167.378 114.766 130.613 1.00 68.88  ?  552  LEU   A CG    1 
ATOM   4418  C  CD1   . LEU   A 1 552 ? 167.865 113.495 129.941 1.00 72.08  ?  552  LEU   A CD1   1 
ATOM   4419  C  CD2   . LEU   A 1 552 ? 166.371 114.446 131.704 1.00 66.01  ?  552  LEU   A CD2   1 
ATOM   4420  N  N     . LYS   A 1 553 ? 170.397 117.918 132.274 1.00 71.26  ?  553  LYS   A N     1 
ATOM   4421  C  CA    . LYS   A 1 553 ? 171.460 118.375 133.164 1.00 67.32  ?  553  LYS   A CA    1 
ATOM   4422  C  C     . LYS   A 1 553 ? 170.985 119.513 134.059 1.00 72.82  ?  553  LYS   A C     1 
ATOM   4423  O  O     . LYS   A 1 553 ? 171.305 119.545 135.253 1.00 79.69  ?  553  LYS   A O     1 
ATOM   4424  C  CB    . LYS   A 1 553 ? 172.682 118.804 132.352 1.00 68.51  ?  553  LYS   A CB    1 
ATOM   4425  C  CG    . LYS   A 1 553 ? 174.002 118.382 132.973 1.00 73.36  ?  553  LYS   A CG    1 
ATOM   4426  C  CD    . LYS   A 1 553 ? 175.161 118.593 132.017 1.00 72.90  ?  553  LYS   A CD    1 
ATOM   4427  C  CE    . LYS   A 1 553 ? 175.395 120.069 131.761 1.00 73.30  ?  553  LYS   A CE    1 
ATOM   4428  N  NZ    . LYS   A 1 553 ? 176.219 120.691 132.833 1.00 76.53  ?  553  LYS   A NZ    1 
ATOM   4429  N  N     . ALA   A 1 554 ? 170.221 120.457 133.502 1.00 71.41  ?  554  ALA   A N     1 
ATOM   4430  C  CA    . ALA   A 1 554 ? 169.682 121.541 134.316 1.00 70.45  ?  554  ALA   A CA    1 
ATOM   4431  C  C     . ALA   A 1 554 ? 168.743 121.007 135.389 1.00 77.96  ?  554  ALA   A C     1 
ATOM   4432  O  O     . ALA   A 1 554 ? 168.798 121.442 136.547 1.00 81.04  ?  554  ALA   A O     1 
ATOM   4433  C  CB    . ALA   A 1 554 ? 168.963 122.555 133.429 1.00 69.66  ?  554  ALA   A CB    1 
ATOM   4434  N  N     . SER   A 1 555 ? 167.880 120.055 135.026 1.00 71.46  ?  555  SER   A N     1 
ATOM   4435  C  CA    . SER   A 1 555 ? 166.977 119.468 136.010 1.00 63.21  ?  555  SER   A CA    1 
ATOM   4436  C  C     . SER   A 1 555 ? 167.747 118.720 137.091 1.00 73.62  ?  555  SER   A C     1 
ATOM   4437  O  O     . SER   A 1 555 ? 167.380 118.767 138.268 1.00 80.76  ?  555  SER   A O     1 
ATOM   4438  C  CB    . SER   A 1 555 ? 165.979 118.540 135.319 1.00 68.62  ?  555  SER   A CB    1 
ATOM   4439  O  OG    . SER   A 1 555 ? 164.772 118.453 136.054 1.00 69.11  ?  555  SER   A OG    1 
ATOM   4440  N  N     . ASN   A 1 556 ? 168.819 118.021 136.710 1.00 70.47  ?  556  ASN   A N     1 
ATOM   4441  C  CA    . ASN   A 1 556 ? 169.622 117.294 137.689 1.00 67.63  ?  556  ASN   A CA    1 
ATOM   4442  C  C     . ASN   A 1 556 ? 170.327 118.244 138.650 1.00 69.21  ?  556  ASN   A C     1 
ATOM   4443  O  O     . ASN   A 1 556 ? 170.394 117.979 139.857 1.00 75.75  ?  556  ASN   A O     1 
ATOM   4444  C  CB    . ASN   A 1 556 ? 170.635 116.403 136.970 1.00 68.49  ?  556  ASN   A CB    1 
ATOM   4445  C  CG    . ASN   A 1 556 ? 171.560 115.683 137.927 1.00 72.55  ?  556  ASN   A CG    1 
ATOM   4446  O  OD1   . ASN   A 1 556 ? 172.763 115.938 137.956 1.00 77.78  ?  556  ASN   A OD1   1 
ATOM   4447  N  ND2   . ASN   A 1 556 ? 171.002 114.776 138.718 1.00 72.10  ?  556  ASN   A ND2   1 
ATOM   4448  N  N     . GLU   A 1 557 ? 170.869 119.351 138.135 1.00 72.14  ?  557  GLU   A N     1 
ATOM   4449  C  CA    . GLU   A 1 557 ? 171.477 120.343 139.015 1.00 74.20  ?  557  GLU   A CA    1 
ATOM   4450  C  C     . GLU   A 1 557 ? 170.447 120.951 139.954 1.00 80.80  ?  557  GLU   A C     1 
ATOM   4451  O  O     . GLU   A 1 557 ? 170.713 121.137 141.149 1.00 83.56  ?  557  GLU   A O     1 
ATOM   4452  C  CB    . GLU   A 1 557 ? 172.170 121.432 138.193 1.00 73.56  ?  557  GLU   A CB    1 
ATOM   4453  C  CG    . GLU   A 1 557 ? 173.231 120.930 137.219 1.00 81.06  ?  557  GLU   A CG    1 
ATOM   4454  C  CD    . GLU   A 1 557 ? 174.126 119.852 137.806 1.00 88.90  ?  557  GLU   A CD    1 
ATOM   4455  O  OE1   . GLU   A 1 557 ? 174.887 119.216 137.044 1.00 89.07  ?  557  GLU   A OE1   1 
ATOM   4456  O  OE2   . GLU   A 1 557 ? 174.072 119.636 139.034 1.00 88.21  ?  557  GLU   A OE2   1 
ATOM   4457  N  N     . LEU   A 1 558 ? 169.258 121.260 139.434 1.00 79.10  ?  558  LEU   A N     1 
ATOM   4458  C  CA    . LEU   A 1 558 ? 168.202 121.799 140.284 1.00 72.72  ?  558  LEU   A CA    1 
ATOM   4459  C  C     . LEU   A 1 558 ? 167.785 120.792 141.349 1.00 73.04  ?  558  LEU   A C     1 
ATOM   4460  O  O     . LEU   A 1 558 ? 167.451 121.172 142.475 1.00 77.90  ?  558  LEU   A O     1 
ATOM   4461  C  CB    . LEU   A 1 558 ? 167.004 122.212 139.431 1.00 70.73  ?  558  LEU   A CB    1 
ATOM   4462  C  CG    . LEU   A 1 558 ? 165.946 123.076 140.115 1.00 72.29  ?  558  LEU   A CG    1 
ATOM   4463  C  CD1   . LEU   A 1 558 ? 166.588 124.272 140.794 1.00 70.46  ?  558  LEU   A CD1   1 
ATOM   4464  C  CD2   . LEU   A 1 558 ? 164.901 123.526 139.109 1.00 75.96  ?  558  LEU   A CD2   1 
ATOM   4465  N  N     . ALA   A 1 559 ? 167.792 119.501 141.009 1.00 76.82  ?  559  ALA   A N     1 
ATOM   4466  C  CA    . ALA   A 1 559 ? 167.453 118.473 141.987 1.00 74.65  ?  559  ALA   A CA    1 
ATOM   4467  C  C     . ALA   A 1 559 ? 168.517 118.363 143.070 1.00 79.94  ?  559  ALA   A C     1 
ATOM   4468  O  O     . ALA   A 1 559 ? 168.193 118.254 144.257 1.00 82.71  ?  559  ALA   A O     1 
ATOM   4469  C  CB    . ALA   A 1 559 ? 167.263 117.127 141.291 1.00 75.11  ?  559  ALA   A CB    1 
ATOM   4470  N  N     . LYS   A 1 560 ? 169.793 118.385 142.685 1.00 87.31  ?  560  LYS   A N     1 
ATOM   4471  C  CA    . LYS   A 1 560 ? 170.851 118.314 143.686 1.00 86.78  ?  560  LYS   A CA    1 
ATOM   4472  C  C     . LYS   A 1 560 ? 170.949 119.593 144.505 1.00 87.79  ?  560  LYS   A C     1 
ATOM   4473  O  O     . LYS   A 1 560 ? 171.563 119.583 145.577 1.00 89.56  ?  560  LYS   A O     1 
ATOM   4474  C  CB    . LYS   A 1 560 ? 172.195 118.002 143.023 1.00 86.02  ?  560  LYS   A CB    1 
ATOM   4475  C  CG    . LYS   A 1 560 ? 172.916 119.208 142.451 1.00 87.47  ?  560  LYS   A CG    1 
ATOM   4476  C  CD    . LYS   A 1 560 ? 174.403 118.934 142.300 1.00 88.91  ?  560  LYS   A CD    1 
ATOM   4477  C  CE    . LYS   A 1 560 ? 174.654 117.639 141.543 1.00 89.25  ?  560  LYS   A CE    1 
ATOM   4478  N  NZ    . LYS   A 1 560 ? 173.965 117.619 140.224 1.00 90.11  ?  560  LYS   A NZ    1 
ATOM   4479  N  N     . GLU   A 1 561 ? 170.362 120.690 144.026 1.00 90.25  ?  561  GLU   A N     1 
ATOM   4480  C  CA    . GLU   A 1 561 ? 170.338 121.929 144.794 1.00 87.41  ?  561  GLU   A CA    1 
ATOM   4481  C  C     . GLU   A 1 561 ? 169.106 122.065 145.682 1.00 88.15  ?  561  GLU   A C     1 
ATOM   4482  O  O     . GLU   A 1 561 ? 169.185 122.703 146.738 1.00 89.68  ?  561  GLU   A O     1 
ATOM   4483  C  CB    . GLU   A 1 561 ? 170.415 123.130 143.847 1.00 88.70  ?  561  GLU   A CB    1 
ATOM   4484  C  CG    . GLU   A 1 561 ? 170.787 124.438 144.522 1.00 89.63  ?  561  GLU   A CG    1 
ATOM   4485  C  CD    . GLU   A 1 561 ? 170.122 125.635 143.873 1.00 94.57  ?  561  GLU   A CD    1 
ATOM   4486  O  OE1   . GLU   A 1 561 ? 168.876 125.689 143.859 1.00 93.80  ?  561  GLU   A OE1   1 
ATOM   4487  O  OE2   . GLU   A 1 561 ? 170.846 126.521 143.373 1.00 92.72  ?  561  GLU   A OE2   1 
ATOM   4488  N  N     . GLN   A 1 562 ? 167.971 121.481 145.288 1.00 86.32  ?  562  GLN   A N     1 
ATOM   4489  C  CA    . GLN   A 1 562 ? 166.717 121.673 146.004 1.00 80.16  ?  562  GLN   A CA    1 
ATOM   4490  C  C     . GLN   A 1 562 ? 165.970 120.384 146.316 1.00 83.29  ?  562  GLN   A C     1 
ATOM   4491  O  O     . GLN   A 1 562 ? 164.902 120.447 146.934 1.00 82.30  ?  562  GLN   A O     1 
ATOM   4492  C  CB    . GLN   A 1 562 ? 165.783 122.599 145.209 1.00 77.82  ?  562  GLN   A CB    1 
ATOM   4493  C  CG    . GLN   A 1 562 ? 166.353 123.978 144.930 1.00 83.19  ?  562  GLN   A CG    1 
ATOM   4494  C  CD    . GLN   A 1 562 ? 165.297 124.961 144.470 1.00 87.25  ?  562  GLN   A CD    1 
ATOM   4495  O  OE1   . GLN   A 1 562 ? 164.101 124.681 144.536 1.00 87.62  ?  562  GLN   A OE1   1 
ATOM   4496  N  NE2   . GLN   A 1 562 ? 165.735 126.122 143.999 1.00 87.97  ?  562  GLN   A NE2   1 
ATOM   4497  N  N     . GLY   A 1 563 ? 166.486 119.227 145.913 1.00 89.20  ?  563  GLY   A N     1 
ATOM   4498  C  CA    . GLY   A 1 563 ? 165.788 117.978 146.150 1.00 85.18  ?  563  GLY   A CA    1 
ATOM   4499  C  C     . GLY   A 1 563 ? 164.977 117.529 144.952 1.00 85.51  ?  563  GLY   A C     1 
ATOM   4500  O  O     . GLY   A 1 563 ? 164.362 118.352 144.269 1.00 90.95  ?  563  GLY   A O     1 
ATOM   4501  N  N     . ALA   A 1 564 ? 164.967 116.226 144.688 1.00 76.82  ?  564  ALA   A N     1 
ATOM   4502  C  CA    . ALA   A 1 564 ? 164.222 115.698 143.558 1.00 75.31  ?  564  ALA   A CA    1 
ATOM   4503  C  C     . ALA   A 1 564 ? 162.720 115.788 143.820 1.00 81.60  ?  564  ALA   A C     1 
ATOM   4504  O  O     . ALA   A 1 564 ? 162.266 116.000 144.948 1.00 83.93  ?  564  ALA   A O     1 
ATOM   4505  C  CB    . ALA   A 1 564 ? 164.631 114.254 143.275 1.00 77.36  ?  564  ALA   A CB    1 
ATOM   4506  N  N     . CYS   A 1 565 ? 161.944 115.627 142.752 1.00 85.22  ?  565  CYS   A N     1 
ATOM   4507  C  CA    . CYS   A 1 565 ? 160.498 115.694 142.870 1.00 81.68  ?  565  CYS   A CA    1 
ATOM   4508  C  C     . CYS   A 1 565 ? 159.981 114.535 143.723 1.00 81.06  ?  565  CYS   A C     1 
ATOM   4509  O  O     . CYS   A 1 565 ? 160.580 113.457 143.747 1.00 82.75  ?  565  CYS   A O     1 
ATOM   4510  C  CB    . CYS   A 1 565 ? 159.846 115.670 141.489 1.00 80.49  ?  565  CYS   A CB    1 
ATOM   4511  S  SG    . CYS   A 1 565 ? 159.929 114.091 140.624 1.00 97.24  ?  565  CYS   A SG    1 
ATOM   4512  N  N     . PRO   A 1 566 ? 158.878 114.743 144.448 1.00 75.64  ?  566  PRO   A N     1 
ATOM   4513  C  CA    . PRO   A 1 566 ? 158.408 113.707 145.385 1.00 75.94  ?  566  PRO   A CA    1 
ATOM   4514  C  C     . PRO   A 1 566 ? 158.095 112.371 144.733 1.00 78.99  ?  566  PRO   A C     1 
ATOM   4515  O  O     . PRO   A 1 566 ? 158.257 111.329 145.379 1.00 82.24  ?  566  PRO   A O     1 
ATOM   4516  C  CB    . PRO   A 1 566 ? 157.152 114.338 146.000 1.00 74.02  ?  566  PRO   A CB    1 
ATOM   4517  C  CG    . PRO   A 1 566 ? 157.340 115.804 145.834 1.00 77.14  ?  566  PRO   A CG    1 
ATOM   4518  C  CD    . PRO   A 1 566 ? 158.100 115.988 144.558 1.00 77.79  ?  566  PRO   A CD    1 
ATOM   4519  N  N     . TRP   A 1 567 ? 157.650 112.362 143.477 1.00 76.19  ?  567  TRP   A N     1 
ATOM   4520  C  CA    . TRP   A 1 567 ? 157.271 111.132 142.793 1.00 73.47  ?  567  TRP   A CA    1 
ATOM   4521  C  C     . TRP   A 1 567 ? 158.302 110.717 141.748 1.00 76.45  ?  567  TRP   A C     1 
ATOM   4522  O  O     . TRP   A 1 567 ? 157.951 110.144 140.714 1.00 85.83  ?  567  TRP   A O     1 
ATOM   4523  C  CB    . TRP   A 1 567 ? 155.892 111.279 142.153 1.00 76.27  ?  567  TRP   A CB    1 
ATOM   4524  C  CG    . TRP   A 1 567 ? 154.793 111.515 143.142 1.00 75.44  ?  567  TRP   A CG    1 
ATOM   4525  C  CD1   . TRP   A 1 567 ? 154.891 111.476 144.501 1.00 76.05  ?  567  TRP   A CD1   1 
ATOM   4526  C  CD2   . TRP   A 1 567 ? 153.426 111.825 142.847 1.00 79.72  ?  567  TRP   A CD2   1 
ATOM   4527  N  NE1   . TRP   A 1 567 ? 153.672 111.745 145.072 1.00 73.63  ?  567  TRP   A NE1   1 
ATOM   4528  C  CE2   . TRP   A 1 567 ? 152.755 111.962 144.077 1.00 79.09  ?  567  TRP   A CE2   1 
ATOM   4529  C  CE3   . TRP   A 1 567 ? 152.706 112.000 141.663 1.00 81.49  ?  567  TRP   A CE3   1 
ATOM   4530  C  CZ2   . TRP   A 1 567 ? 151.399 112.266 144.157 1.00 83.15  ?  567  TRP   A CZ2   1 
ATOM   4531  C  CZ3   . TRP   A 1 567 ? 151.360 112.301 141.744 1.00 77.10  ?  567  TRP   A CZ3   1 
ATOM   4532  C  CH2   . TRP   A 1 567 ? 150.721 112.431 142.981 1.00 80.02  ?  567  TRP   A CH2   1 
ATOM   4533  N  N     . PHE   A 1 568 ? 159.581 110.995 142.009 1.00 75.82  ?  568  PHE   A N     1 
ATOM   4534  C  CA    . PHE   A 1 568 ? 160.633 110.619 141.070 1.00 71.38  ?  568  PHE   A CA    1 
ATOM   4535  C  C     . PHE   A 1 568 ? 160.798 109.108 140.970 1.00 73.61  ?  568  PHE   A C     1 
ATOM   4536  O  O     . PHE   A 1 568 ? 161.273 108.609 139.944 1.00 81.36  ?  568  PHE   A O     1 
ATOM   4537  C  CB    . PHE   A 1 568 ? 161.957 111.261 141.479 1.00 71.53  ?  568  PHE   A CB    1 
ATOM   4538  C  CG    . PHE   A 1 568 ? 163.071 111.016 140.506 1.00 75.38  ?  568  PHE   A CG    1 
ATOM   4539  C  CD1   . PHE   A 1 568 ? 163.037 111.574 139.240 1.00 74.62  ?  568  PHE   A CD1   1 
ATOM   4540  C  CD2   . PHE   A 1 568 ? 164.150 110.223 140.854 1.00 77.14  ?  568  PHE   A CD2   1 
ATOM   4541  C  CE1   . PHE   A 1 568 ? 164.059 111.349 138.341 1.00 75.87  ?  568  PHE   A CE1   1 
ATOM   4542  C  CE2   . PHE   A 1 568 ? 165.175 109.995 139.959 1.00 76.22  ?  568  PHE   A CE2   1 
ATOM   4543  C  CZ    . PHE   A 1 568 ? 165.130 110.559 138.701 1.00 76.26  ?  568  PHE   A CZ    1 
ATOM   4544  N  N     . ASN   A 1 569 ? 160.418 108.367 142.013 1.00 84.37  ?  569  ASN   A N     1 
ATOM   4545  C  CA    A ASN   A 1 569 ? 160.571 106.916 141.998 0.50 83.90  ?  569  ASN   A CA    1 
ATOM   4546  C  CA    B ASN   A 1 569 ? 160.671 106.916 141.998 0.50 83.90  ?  569  ASN   A CA    1 
ATOM   4547  C  C     . ASN   A 1 569 ? 159.669 106.242 140.972 1.00 89.45  ?  569  ASN   A C     1 
ATOM   4548  O  O     . ASN   A 1 569 ? 159.904 105.078 140.631 1.00 95.82  ?  569  ASN   A O     1 
ATOM   4549  C  CB    A ASN   A 1 569 ? 160.297 106.339 143.389 0.50 87.57  ?  569  ASN   A CB    1 
ATOM   4550  C  CB    B ASN   A 1 569 ? 160.397 106.339 143.389 0.50 87.57  ?  569  ASN   A CB    1 
ATOM   4551  C  CG    A ASN   A 1 569 ? 159.009 106.861 143.999 0.50 93.99  ?  569  ASN   A CG    1 
ATOM   4552  C  CG    B ASN   A 1 569 ? 161.441 106.749 144.412 0.50 93.99  ?  569  ASN   A CG    1 
ATOM   4553  O  OD1   A ASN   A 1 569 ? 158.959 107.981 144.507 0.50 97.29  ?  569  ASN   A OD1   1 
ATOM   4554  O  OD1   B ASN   A 1 569 ? 162.569 107.094 144.060 0.50 97.29  ?  569  ASN   A OD1   1 
ATOM   4555  N  ND2   A ASN   A 1 569 ? 157.955 106.055 143.940 0.50 90.94  ?  569  ASN   A ND2   1 
ATOM   4556  N  ND2   B ASN   A 1 569 ? 161.065 106.726 145.685 0.50 90.94  ?  569  ASN   A ND2   1 
ATOM   4557  N  N     . GLU   A 1 570 ? 158.649 106.937 140.477 1.00 83.18  ?  570  GLU   A N     1 
ATOM   4558  C  CA    . GLU   A 1 570 ? 157.747 106.384 139.477 1.00 84.72  ?  570  GLU   A CA    1 
ATOM   4559  C  C     . GLU   A 1 570 ? 158.243 106.587 138.052 1.00 85.37  ?  570  GLU   A C     1 
ATOM   4560  O  O     . GLU   A 1 570 ? 157.597 106.108 137.114 1.00 90.23  ?  570  GLU   A O     1 
ATOM   4561  C  CB    . GLU   A 1 570 ? 156.353 107.000 139.626 1.00 86.51  ?  570  GLU   A CB    1 
ATOM   4562  C  CG    . GLU   A 1 570 ? 155.881 107.126 141.061 1.00 87.88  ?  570  GLU   A CG    1 
ATOM   4563  C  CD    . GLU   A 1 570 ? 154.372 107.203 141.172 1.00 94.22  ?  570  GLU   A CD    1 
ATOM   4564  O  OE1   . GLU   A 1 570 ? 153.710 107.442 140.141 1.00 95.17  ?  570  GLU   A OE1   1 
ATOM   4565  O  OE2   . GLU   A 1 570 ? 153.847 107.025 142.291 1.00 95.27  ?  570  GLU   A OE2   1 
ATOM   4566  N  N     . THR   A 1 571 ? 159.363 107.275 137.866 1.00 74.34  ?  571  THR   A N     1 
ATOM   4567  C  CA    . THR   A 1 571 ? 159.913 107.537 136.546 1.00 70.38  ?  571  THR   A CA    1 
ATOM   4568  C  C     . THR   A 1 571 ? 160.967 106.496 136.187 1.00 75.03  ?  571  THR   A C     1 
ATOM   4569  O  O     . THR   A 1 571 ? 161.586 105.875 137.055 1.00 80.54  ?  571  THR   A O     1 
ATOM   4570  C  CB    . THR   A 1 571 ? 160.525 108.939 136.477 1.00 73.74  ?  571  THR   A CB    1 
ATOM   4571  O  OG1   . THR   A 1 571 ? 161.678 109.000 137.324 1.00 83.35  ?  571  THR   A OG1   1 
ATOM   4572  C  CG2   . THR   A 1 571 ? 159.517 109.983 136.926 1.00 77.10  ?  571  THR   A CG2   1 
ATOM   4573  N  N     . THR   A 1 572 ? 161.163 106.310 134.880 1.00 79.28  ?  572  THR   A N     1 
ATOM   4574  C  CA    . THR   A 1 572 ? 162.208 105.410 134.408 1.00 78.26  ?  572  THR   A CA    1 
ATOM   4575  C  C     . THR   A 1 572 ? 163.599 105.995 134.603 1.00 80.35  ?  572  THR   A C     1 
ATOM   4576  O  O     . THR   A 1 572 ? 164.583 105.249 134.559 1.00 85.74  ?  572  THR   A O     1 
ATOM   4577  C  CB    . THR   A 1 572 ? 161.992 105.069 132.933 1.00 79.26  ?  572  THR   A CB    1 
ATOM   4578  O  OG1   . THR   A 1 572 ? 161.992 106.273 132.157 1.00 79.99  ?  572  THR   A OG1   1 
ATOM   4579  C  CG2   . THR   A 1 572 ? 160.667 104.349 132.741 1.00 76.56  ?  572  THR   A CG2   1 
ATOM   4580  N  N     . TYR   A 1 573 ? 163.703 107.310 134.813 1.00 77.23  ?  573  TYR   A N     1 
ATOM   4581  C  CA    . TYR   A 1 573 ? 165.001 107.918 135.085 1.00 72.37  ?  573  TYR   A CA    1 
ATOM   4582  C  C     . TYR   A 1 573 ? 165.592 107.390 136.384 1.00 75.14  ?  573  TYR   A C     1 
ATOM   4583  O  O     . TYR   A 1 573 ? 166.810 107.204 136.492 1.00 78.93  ?  573  TYR   A O     1 
ATOM   4584  C  CB    . TYR   A 1 573 ? 164.868 109.439 135.140 1.00 70.39  ?  573  TYR   A CB    1 
ATOM   4585  C  CG    . TYR   A 1 573 ? 164.658 110.093 133.795 1.00 71.13  ?  573  TYR   A CG    1 
ATOM   4586  C  CD1   . TYR   A 1 573 ? 165.661 110.093 132.837 1.00 75.01  ?  573  TYR   A CD1   1 
ATOM   4587  C  CD2   . TYR   A 1 573 ? 163.459 110.719 133.487 1.00 72.88  ?  573  TYR   A CD2   1 
ATOM   4588  C  CE1   . TYR   A 1 573 ? 165.472 110.694 131.607 1.00 76.52  ?  573  TYR   A CE1   1 
ATOM   4589  C  CE2   . TYR   A 1 573 ? 163.262 111.322 132.261 1.00 76.69  ?  573  TYR   A CE2   1 
ATOM   4590  C  CZ    . TYR   A 1 573 ? 164.271 111.306 131.325 1.00 78.56  ?  573  TYR   A CZ    1 
ATOM   4591  O  OH    . TYR   A 1 573 ? 164.076 111.906 130.103 1.00 77.50  ?  573  TYR   A OH    1 
ATOM   4592  N  N     . ALA   A 1 574 ? 164.743 107.147 137.385 1.00 79.96  ?  574  ALA   A N     1 
ATOM   4593  C  CA    . ALA   A 1 574 ? 165.212 106.616 138.659 1.00 82.43  ?  574  ALA   A CA    1 
ATOM   4594  C  C     . ALA   A 1 574 ? 165.825 105.230 138.519 1.00 87.67  ?  574  ALA   A C     1 
ATOM   4595  O  O     . ALA   A 1 574 ? 166.628 104.831 139.369 1.00 90.49  ?  574  ALA   A O     1 
ATOM   4596  C  CB    . ALA   A 1 574 ? 164.061 106.576 139.665 1.00 82.16  ?  574  ALA   A CB    1 
ATOM   4597  N  N     . LYS   A 1 575 ? 165.469 104.490 137.471 1.00 83.12  ?  575  LYS   A N     1 
ATOM   4598  C  CA    . LYS   A 1 575 ? 166.009 103.162 137.225 1.00 77.00  ?  575  LYS   A CA    1 
ATOM   4599  C  C     . LYS   A 1 575 ? 167.195 103.181 136.269 1.00 79.14  ?  575  LYS   A C     1 
ATOM   4600  O  O     . LYS   A 1 575 ? 167.651 102.116 135.843 1.00 83.32  ?  575  LYS   A O     1 
ATOM   4601  C  CB    . LYS   A 1 575 ? 164.915 102.241 136.683 1.00 76.61  ?  575  LYS   A CB    1 
ATOM   4602  C  CG    . LYS   A 1 575 ? 163.731 102.071 137.619 1.00 80.38  ?  575  LYS   A CG    1 
ATOM   4603  C  CD    . LYS   A 1 575 ? 162.679 101.154 137.018 1.00 83.98  ?  575  LYS   A CD    1 
ATOM   4604  C  CE    . LYS   A 1 575 ? 161.379 101.215 137.804 1.00 87.28  ?  575  LYS   A CE    1 
ATOM   4605  N  NZ    . LYS   A 1 575 ? 161.209 102.523 138.496 1.00 87.09  ?  575  LYS   A NZ    1 
ATOM   4606  N  N     . GLY   A 1 576 ? 167.702 104.362 135.924 1.00 77.94  ?  576  GLY   A N     1 
ATOM   4607  C  CA    . GLY   A 1 576 ? 168.819 104.467 135.010 1.00 76.70  ?  576  GLY   A CA    1 
ATOM   4608  C  C     . GLY   A 1 576 ? 168.459 104.413 133.544 1.00 80.67  ?  576  GLY   A C     1 
ATOM   4609  O  O     . GLY   A 1 576 ? 169.360 104.288 132.707 1.00 84.58  ?  576  GLY   A O     1 
ATOM   4610  N  N     . ILE   A 1 577 ? 167.178 104.500 133.205 1.00 83.91  ?  577  ILE   A N     1 
ATOM   4611  C  CA    . ILE   A 1 577 ? 166.732 104.460 131.818 1.00 79.18  ?  577  ILE   A CA    1 
ATOM   4612  C  C     . ILE   A 1 577 ? 166.752 105.875 131.257 1.00 82.10  ?  577  ILE   A C     1 
ATOM   4613  O  O     . ILE   A 1 577 ? 166.232 106.808 131.880 1.00 86.14  ?  577  ILE   A O     1 
ATOM   4614  C  CB    . ILE   A 1 577 ? 165.329 103.839 131.707 1.00 77.86  ?  577  ILE   A CB    1 
ATOM   4615  C  CG1   . ILE   A 1 577 ? 165.345 102.372 132.151 1.00 77.94  ?  577  ILE   A CG1   1 
ATOM   4616  C  CG2   . ILE   A 1 577 ? 164.802 103.955 130.287 1.00 80.49  ?  577  ILE   A CG2   1 
ATOM   4617  C  CD1   . ILE   A 1 577 ? 166.684 101.678 131.980 1.00 77.70  ?  577  ILE   A CD1   1 
ATOM   4618  N  N     . LEU   A 1 578 ? 167.353 106.035 130.086 1.00 80.03  ?  578  LEU   A N     1 
ATOM   4619  C  CA    . LEU   A 1 578 ? 167.489 107.313 129.410 1.00 78.44  ?  578  LEU   A CA    1 
ATOM   4620  C  C     . LEU   A 1 578 ? 166.725 107.288 128.092 1.00 81.76  ?  578  LEU   A C     1 
ATOM   4621  O  O     . LEU   A 1 578 ? 166.439 106.213 127.552 1.00 82.69  ?  578  LEU   A O     1 
ATOM   4622  C  CB    . LEU   A 1 578 ? 168.969 107.633 129.152 1.00 78.40  ?  578  LEU   A CB    1 
ATOM   4623  C  CG    . LEU   A 1 578 ? 169.735 108.242 130.328 1.00 77.81  ?  578  LEU   A CG    1 
ATOM   4624  C  CD1   . LEU   A 1 578 ? 171.169 108.553 129.932 1.00 79.14  ?  578  LEU   A CD1   1 
ATOM   4625  C  CD2   . LEU   A 1 578 ? 169.033 109.489 130.838 1.00 76.55  ?  578  LEU   A CD2   1 
ATOM   4626  N  N     . PRO   A 1 579 ? 166.365 108.456 127.550 1.00 79.87  ?  579  PRO   A N     1 
ATOM   4627  C  CA    . PRO   A 1 579 ? 165.644 108.475 126.266 1.00 76.09  ?  579  PRO   A CA    1 
ATOM   4628  C  C     . PRO   A 1 579 ? 166.421 107.851 125.121 1.00 75.80  ?  579  PRO   A C     1 
ATOM   4629  O  O     . PRO   A 1 579 ? 165.806 107.422 124.138 1.00 79.07  ?  579  PRO   A O     1 
ATOM   4630  C  CB    . PRO   A 1 579 ? 165.395 109.970 126.022 1.00 72.54  ?  579  PRO   A CB    1 
ATOM   4631  C  CG    . PRO   A 1 579 ? 165.463 110.591 127.371 1.00 75.28  ?  579  PRO   A CG    1 
ATOM   4632  C  CD    . PRO   A 1 579 ? 166.479 109.803 128.136 1.00 76.85  ?  579  PRO   A CD    1 
ATOM   4633  N  N     . ILE   A 1 580 ? 167.753 107.783 125.215 1.00 82.79  ?  580  ILE   A N     1 
ATOM   4634  C  CA    . ILE   A 1 580 ? 168.559 107.143 124.177 1.00 84.41  ?  580  ILE   A CA    1 
ATOM   4635  C  C     . ILE   A 1 580 ? 168.513 105.627 124.248 1.00 88.44  ?  580  ILE   A C     1 
ATOM   4636  O  O     . ILE   A 1 580 ? 169.181 104.960 123.447 1.00 87.43  ?  580  ILE   A O     1 
ATOM   4637  C  CB    . ILE   A 1 580 ? 170.028 107.601 124.260 1.00 84.80  ?  580  ILE   A CB    1 
ATOM   4638  C  CG1   . ILE   A 1 580 ? 170.688 107.027 125.515 1.00 84.22  ?  580  ILE   A CG1   1 
ATOM   4639  C  CG2   . ILE   A 1 580 ? 170.112 109.118 124.251 1.00 81.96  ?  580  ILE   A CG2   1 
ATOM   4640  C  CD1   . ILE   A 1 580 ? 172.071 107.566 125.781 1.00 86.26  ?  580  ILE   A CD1   1 
ATOM   4641  N  N     . ASP   A 1 581 ? 167.749 105.058 125.183 1.00 91.64  ?  581  ASP   A N     1 
ATOM   4642  C  CA    . ASP   A 1 581 ? 167.651 103.614 125.334 1.00 86.85  ?  581  ASP   A CA    1 
ATOM   4643  C  C     . ASP   A 1 581 ? 166.304 103.040 124.920 1.00 88.19  ?  581  ASP   A C     1 
ATOM   4644  O  O     . ASP   A 1 581 ? 166.240 101.858 124.570 1.00 93.08  ?  581  ASP   A O     1 
ATOM   4645  C  CB    . ASP   A 1 581 ? 167.928 103.211 126.790 1.00 89.42  ?  581  ASP   A CB    1 
ATOM   4646  C  CG    . ASP   A 1 581 ? 169.266 103.714 127.290 1.00 96.14  ?  581  ASP   A CG    1 
ATOM   4647  O  OD1   . ASP   A 1 581 ? 170.204 103.824 126.474 1.00 96.23  ?  581  ASP   A OD1   1 
ATOM   4648  O  OD2   . ASP   A 1 581 ? 169.381 104.000 128.500 1.00 94.98  ?  581  ASP   A OD2   1 
ATOM   4649  N  N     . THR   A 1 582 ? 165.236 103.836 124.951 1.00 79.89  ?  582  THR   A N     1 
ATOM   4650  C  CA    . THR   A 1 582 ? 163.893 103.354 124.656 1.00 80.50  ?  582  THR   A CA    1 
ATOM   4651  C  C     . THR   A 1 582 ? 163.359 103.864 123.323 1.00 82.39  ?  582  THR   A C     1 
ATOM   4652  O  O     . THR   A 1 582 ? 162.168 103.696 123.041 1.00 82.43  ?  582  THR   A O     1 
ATOM   4653  C  CB    . THR   A 1 582 ? 162.934 103.742 125.783 1.00 82.64  ?  582  THR   A CB    1 
ATOM   4654  O  OG1   . THR   A 1 582 ? 163.067 105.141 126.066 1.00 83.58  ?  582  THR   A OG1   1 
ATOM   4655  C  CG2   . THR   A 1 582 ? 163.245 102.947 127.040 1.00 78.77  ?  582  THR   A CG2   1 
ATOM   4656  N  N     . TYR   A 1 583 ? 164.201 104.482 122.501 1.00 84.46  ?  583  TYR   A N     1 
ATOM   4657  C  CA    . TYR   A 1 583 ? 163.747 104.989 121.217 1.00 84.20  ?  583  TYR   A CA    1 
ATOM   4658  C  C     . TYR   A 1 583 ? 163.470 103.839 120.251 1.00 87.05  ?  583  TYR   A C     1 
ATOM   4659  O  O     . TYR   A 1 583 ? 164.010 102.737 120.379 1.00 92.37  ?  583  TYR   A O     1 
ATOM   4660  C  CB    . TYR   A 1 583 ? 164.782 105.942 120.619 1.00 87.29  ?  583  TYR   A CB    1 
ATOM   4661  C  CG    . TYR   A 1 583 ? 166.019 105.256 120.087 1.00 90.54  ?  583  TYR   A CG    1 
ATOM   4662  C  CD1   . TYR   A 1 583 ? 167.029 104.841 120.942 1.00 87.19  ?  583  TYR   A CD1   1 
ATOM   4663  C  CD2   . TYR   A 1 583 ? 166.181 105.029 118.728 1.00 88.73  ?  583  TYR   A CD2   1 
ATOM   4664  C  CE1   . TYR   A 1 583 ? 168.161 104.215 120.460 1.00 87.00  ?  583  TYR   A CE1   1 
ATOM   4665  C  CE2   . TYR   A 1 583 ? 167.308 104.404 118.237 1.00 87.96  ?  583  TYR   A CE2   1 
ATOM   4666  C  CZ    . TYR   A 1 583 ? 168.296 104.000 119.106 1.00 89.16  ?  583  TYR   A CZ    1 
ATOM   4667  O  OH    . TYR   A 1 583 ? 169.422 103.377 118.621 1.00 92.62  ?  583  TYR   A OH    1 
ATOM   4668  N  N     . LYS   A 1 584 ? 162.607 104.111 119.274 1.00 86.85  ?  584  LYS   A N     1 
ATOM   4669  C  CA    . LYS   A 1 584 ? 162.289 103.119 118.256 1.00 88.90  ?  584  LYS   A CA    1 
ATOM   4670  C  C     . LYS   A 1 584 ? 163.511 102.862 117.383 1.00 90.57  ?  584  LYS   A C     1 
ATOM   4671  O  O     . LYS   A 1 584 ? 164.096 103.795 116.826 1.00 93.13  ?  584  LYS   A O     1 
ATOM   4672  C  CB    . LYS   A 1 584 ? 161.114 103.597 117.404 1.00 87.65  ?  584  LYS   A CB    1 
ATOM   4673  C  CG    . LYS   A 1 584 ? 160.593 102.564 116.423 1.00 85.76  ?  584  LYS   A CG    1 
ATOM   4674  C  CD    . LYS   A 1 584 ? 159.517 101.697 117.052 1.00 85.21  ?  584  LYS   A CD    1 
ATOM   4675  C  CE    . LYS   A 1 584 ? 158.532 101.199 116.009 1.00 86.65  ?  584  LYS   A CE    1 
ATOM   4676  N  NZ    . LYS   A 1 584 ? 159.207 100.866 114.727 1.00 91.41  ?  584  LYS   A NZ    1 
ATOM   4677  N  N     . LYS   A 1 585 ? 163.889 101.587 117.255 1.00 93.64  ?  585  LYS   A N     1 
ATOM   4678  C  CA    . LYS   A 1 585 ? 165.125 101.237 116.565 1.00 92.45  ?  585  LYS   A CA    1 
ATOM   4679  C  C     . LYS   A 1 585 ? 165.076 101.541 115.073 1.00 91.39  ?  585  LYS   A C     1 
ATOM   4680  O  O     . LYS   A 1 585 ? 166.135 101.646 114.444 1.00 94.19  ?  585  LYS   A O     1 
ATOM   4681  C  CB    . LYS   A 1 585 ? 165.449 99.760  116.785 1.00 94.45  ?  585  LYS   A CB    1 
ATOM   4682  C  CG    . LYS   A 1 585 ? 165.880 99.429  118.204 1.00 95.57  ?  585  LYS   A CG    1 
ATOM   4683  C  CD    . LYS   A 1 585 ? 166.893 100.437 118.724 1.00 94.28  ?  585  LYS   A CD    1 
ATOM   4684  C  CE    . LYS   A 1 585 ? 167.077 100.310 120.227 1.00 96.05  ?  585  LYS   A CE    1 
ATOM   4685  N  NZ    . LYS   A 1 585 ? 165.882 100.787 120.976 1.00 92.78  ?  585  LYS   A NZ    1 
ATOM   4686  N  N     . ASP   A 1 586 ? 163.880 101.691 114.496 1.00 89.63  ?  586  ASP   A N     1 
ATOM   4687  C  CA    . ASP   A 1 586 ? 163.780 102.028 113.080 1.00 89.70  ?  586  ASP   A CA    1 
ATOM   4688  C  C     . ASP   A 1 586 ? 164.469 103.350 112.769 1.00 90.26  ?  586  ASP   A C     1 
ATOM   4689  O  O     . ASP   A 1 586 ? 164.973 103.542 111.655 1.00 93.50  ?  586  ASP   A O     1 
ATOM   4690  C  CB    . ASP   A 1 586 ? 162.313 102.082 112.655 1.00 93.56  ?  586  ASP   A CB    1 
ATOM   4691  C  CG    . ASP   A 1 586 ? 161.793 100.738 112.186 1.00 97.38  ?  586  ASP   A CG    1 
ATOM   4692  O  OD1   . ASP   A 1 586 ? 162.239 100.265 111.120 1.00 96.77  ?  586  ASP   A OD1   1 
ATOM   4693  O  OD2   . ASP   A 1 586 ? 160.937 100.154 112.883 1.00 96.82  ?  586  ASP   A OD2   1 
ATOM   4694  N  N     . LEU   A 1 587 ? 164.520 104.262 113.744 1.00 83.03  ?  587  LEU   A N     1 
ATOM   4695  C  CA    . LEU   A 1 587 ? 165.200 105.536 113.549 1.00 83.81  ?  587  LEU   A CA    1 
ATOM   4696  C  C     . LEU   A 1 587 ? 166.683 105.359 113.257 1.00 84.64  ?  587  LEU   A C     1 
ATOM   4697  O  O     . LEU   A 1 587 ? 167.314 106.281 112.729 1.00 86.70  ?  587  LEU   A O     1 
ATOM   4698  C  CB    . LEU   A 1 587 ? 165.017 106.422 114.780 1.00 85.11  ?  587  LEU   A CB    1 
ATOM   4699  C  CG    . LEU   A 1 587 ? 163.579 106.809 115.126 1.00 81.59  ?  587  LEU   A CG    1 
ATOM   4700  C  CD1   . LEU   A 1 587 ? 163.497 107.334 116.548 1.00 81.33  ?  587  LEU   A CD1   1 
ATOM   4701  C  CD2   . LEU   A 1 587 ? 163.051 107.836 114.140 1.00 81.90  ?  587  LEU   A CD2   1 
ATOM   4702  N  N     . ASP   A 1 588 ? 167.257 104.201 113.594 1.00 92.99  ?  588  ASP   A N     1 
ATOM   4703  C  CA    . ASP   A 1 588 ? 168.650 103.941 113.258 1.00 93.05  ?  588  ASP   A CA    1 
ATOM   4704  C  C     . ASP   A 1 588 ? 168.870 103.828 111.756 1.00 93.97  ?  588  ASP   A C     1 
ATOM   4705  O  O     . ASP   A 1 588 ? 170.003 104.000 111.295 1.00 92.36  ?  588  ASP   A O     1 
ATOM   4706  C  CB    . ASP   A 1 588 ? 169.129 102.665 113.951 1.00 94.05  ?  588  ASP   A CB    1 
ATOM   4707  C  CG    . ASP   A 1 588 ? 169.199 102.812 115.457 1.00 97.69  ?  588  ASP   A CG    1 
ATOM   4708  O  OD1   . ASP   A 1 588 ? 169.455 103.937 115.933 1.00 100.12 ?  588  ASP   A OD1   1 
ATOM   4709  O  OD2   . ASP   A 1 588 ? 169.000 101.803 116.164 1.00 97.74  ?  588  ASP   A OD2   1 
ATOM   4710  N  N     . THR   A 1 589 ? 167.820 103.548 110.986 1.00 95.15  ?  589  THR   A N     1 
ATOM   4711  C  CA    . THR   A 1 589 ? 167.944 103.402 109.543 1.00 92.13  ?  589  THR   A CA    1 
ATOM   4712  C  C     . THR   A 1 589 ? 167.813 104.720 108.792 1.00 92.27  ?  589  THR   A C     1 
ATOM   4713  O  O     . THR   A 1 589 ? 167.999 104.738 107.571 1.00 94.51  ?  589  THR   A O     1 
ATOM   4714  C  CB    . THR   A 1 589 ? 166.895 102.417 109.017 1.00 93.20  ?  589  THR   A CB    1 
ATOM   4715  O  OG1   . THR   A 1 589 ? 165.609 103.050 108.997 1.00 94.91  ?  589  THR   A OG1   1 
ATOM   4716  C  CG2   . THR   A 1 589 ? 166.831 101.185 109.905 1.00 91.68  ?  589  THR   A CG2   1 
ATOM   4717  N  N     . ILE   A 1 590 ? 167.503 105.817 109.482 1.00 81.27  ?  590  ILE   A N     1 
ATOM   4718  C  CA    . ILE   A 1 590 ? 167.319 107.116 108.849 1.00 79.43  ?  590  ILE   A CA    1 
ATOM   4719  C  C     . ILE   A 1 590 ? 168.219 108.190 109.437 1.00 80.40  ?  590  ILE   A C     1 
ATOM   4720  O  O     . ILE   A 1 590 ? 168.198 109.327 108.956 1.00 82.59  ?  590  ILE   A O     1 
ATOM   4721  C  CB    . ILE   A 1 590 ? 165.845 107.567 108.912 1.00 78.10  ?  590  ILE   A CB    1 
ATOM   4722  C  CG1   . ILE   A 1 590 ? 165.306 107.428 110.336 1.00 77.48  ?  590  ILE   A CG1   1 
ATOM   4723  C  CG2   . ILE   A 1 590 ? 165.000 106.762 107.940 1.00 79.70  ?  590  ILE   A CG2   1 
ATOM   4724  C  CD1   . ILE   A 1 590 ? 164.152 108.354 110.642 1.00 81.38  ?  590  ILE   A CD1   1 
ATOM   4725  N  N     . ALA   A 1 591 ? 169.007 107.870 110.460 1.00 89.11  ?  591  ALA   A N     1 
ATOM   4726  C  CA    . ALA   A 1 591 ? 169.906 108.844 111.070 1.00 90.09  ?  591  ALA   A CA    1 
ATOM   4727  C  C     . ALA   A 1 591 ? 171.105 108.107 111.644 1.00 93.68  ?  591  ALA   A C     1 
ATOM   4728  O  O     . ALA   A 1 591 ? 170.939 107.212 112.479 1.00 93.31  ?  591  ALA   A O     1 
ATOM   4729  C  CB    . ALA   A 1 591 ? 169.193 109.648 112.158 1.00 89.44  ?  591  ALA   A CB    1 
ATOM   4730  N  N     . ASN   A 1 592 ? 172.304 108.482 111.199 1.00 106.17 ?  592  ASN   A N     1 
ATOM   4731  C  CA    . ASN   A 1 592 ? 173.539 107.875 111.677 1.00 106.51 ?  592  ASN   A CA    1 
ATOM   4732  C  C     . ASN   A 1 592 ? 174.384 108.833 112.510 1.00 106.82 ?  592  ASN   A C     1 
ATOM   4733  O  O     . ASN   A 1 592 ? 175.556 108.542 112.774 1.00 107.51 ?  592  ASN   A O     1 
ATOM   4734  C  CB    . ASN   A 1 592 ? 174.352 107.323 110.499 1.00 105.72 ?  592  ASN   A CB    1 
ATOM   4735  C  CG    . ASN   A 1 592 ? 174.738 108.391 109.480 1.00 105.91 ?  592  ASN   A CG    1 
ATOM   4736  O  OD1   . ASN   A 1 592 ? 174.703 109.589 109.757 1.00 107.16 ?  592  ASN   A OD1   1 
ATOM   4737  N  ND2   . ASN   A 1 592 ? 175.126 107.946 108.291 1.00 104.60 ?  592  ASN   A ND2   1 
ATOM   4738  N  N     . GLU   A 1 593 ? 173.824 109.962 112.925 1.00 102.23 ?  593  GLU   A N     1 
ATOM   4739  C  CA    . GLU   A 1 593 ? 174.572 110.910 113.740 1.00 100.12 ?  593  GLU   A CA    1 
ATOM   4740  C  C     . GLU   A 1 593 ? 174.846 110.308 115.114 1.00 103.38 ?  593  GLU   A C     1 
ATOM   4741  O  O     . GLU   A 1 593 ? 173.911 109.851 115.782 1.00 103.32 ?  593  GLU   A O     1 
ATOM   4742  C  CB    . GLU   A 1 593 ? 173.799 112.219 113.882 1.00 99.84  ?  593  GLU   A CB    1 
ATOM   4743  C  CG    . GLU   A 1 593 ? 174.509 113.275 114.709 1.00 101.16 ?  593  GLU   A CG    1 
ATOM   4744  C  CD    . GLU   A 1 593 ? 175.373 114.189 113.864 1.00 105.50 ?  593  GLU   A CD    1 
ATOM   4745  O  OE1   . GLU   A 1 593 ? 174.955 114.535 112.741 1.00 105.85 ?  593  GLU   A OE1   1 
ATOM   4746  O  OE2   . GLU   A 1 593 ? 176.472 114.563 114.318 1.00 105.50 ?  593  GLU   A OE2   1 
ATOM   4747  N  N     . PRO   A 1 594 ? 176.095 110.277 115.564 1.00 100.79 ?  594  PRO   A N     1 
ATOM   4748  C  CA    . PRO   A 1 594 ? 176.388 109.762 116.902 1.00 98.20  ?  594  PRO   A CA    1 
ATOM   4749  C  C     . PRO   A 1 594 ? 176.099 110.797 117.979 1.00 101.42 ?  594  PRO   A C     1 
ATOM   4750  O  O     . PRO   A 1 594 ? 175.960 111.993 117.717 1.00 106.40 ?  594  PRO   A O     1 
ATOM   4751  C  CB    . PRO   A 1 594 ? 177.885 109.444 116.833 1.00 97.91  ?  594  PRO   A CB    1 
ATOM   4752  C  CG    . PRO   A 1 594 ? 178.412 110.434 115.853 1.00 98.03  ?  594  PRO   A CG    1 
ATOM   4753  C  CD    . PRO   A 1 594 ? 177.320 110.652 114.835 1.00 97.84  ?  594  PRO   A CD    1 
ATOM   4754  N  N     . LEU   A 1 595 ? 176.010 110.308 119.213 1.00 91.85  ?  595  LEU   A N     1 
ATOM   4755  C  CA    . LEU   A 1 595 ? 175.818 111.194 120.353 1.00 88.76  ?  595  LEU   A CA    1 
ATOM   4756  C  C     . LEU   A 1 595 ? 177.102 111.961 120.644 1.00 90.67  ?  595  LEU   A C     1 
ATOM   4757  O  O     . LEU   A 1 595 ? 178.195 111.387 120.657 1.00 92.56  ?  595  LEU   A O     1 
ATOM   4758  C  CB    . LEU   A 1 595 ? 175.385 110.396 121.581 1.00 84.15  ?  595  LEU   A CB    1 
ATOM   4759  C  CG    . LEU   A 1 595 ? 174.173 109.483 121.398 1.00 86.44  ?  595  LEU   A CG    1 
ATOM   4760  C  CD1   . LEU   A 1 595 ? 173.901 108.695 122.668 1.00 87.41  ?  595  LEU   A CD1   1 
ATOM   4761  C  CD2   . LEU   A 1 595 ? 172.952 110.288 120.992 1.00 88.30  ?  595  LEU   A CD2   1 
ATOM   4762  N  N     . HIS   A 1 596 ? 176.967 113.265 120.878 1.00 92.64  ?  596  HIS   A N     1 
ATOM   4763  C  CA    . HIS   A 1 596 ? 178.107 114.140 121.117 1.00 92.53  ?  596  HIS   A CA    1 
ATOM   4764  C  C     . HIS   A 1 596 ? 178.254 114.540 122.579 1.00 93.64  ?  596  HIS   A C     1 
ATOM   4765  O  O     . HIS   A 1 596 ? 179.099 115.384 122.895 1.00 97.30  ?  596  HIS   A O     1 
ATOM   4766  C  CB    . HIS   A 1 596 ? 177.999 115.393 120.247 1.00 94.20  ?  596  HIS   A CB    1 
ATOM   4767  C  CG    . HIS   A 1 596 ? 177.714 115.103 118.808 1.00 95.23  ?  596  HIS   A CG    1 
ATOM   4768  N  ND1   . HIS   A 1 596 ? 178.709 114.853 117.889 1.00 96.78  ?  596  HIS   A ND1   1 
ATOM   4769  C  CD2   . HIS   A 1 596 ? 176.546 115.021 118.129 1.00 94.63  ?  596  HIS   A CD2   1 
ATOM   4770  C  CE1   . HIS   A 1 596 ? 178.167 114.630 116.706 1.00 95.98  ?  596  HIS   A CE1   1 
ATOM   4771  N  NE2   . HIS   A 1 596 ? 176.855 114.727 116.824 1.00 96.71  ?  596  HIS   A NE2   1 
ATOM   4772  N  N     . TYR   A 1 597 ? 177.464 113.960 123.476 1.00 84.97  ?  597  TYR   A N     1 
ATOM   4773  C  CA    . TYR   A 1 597 ? 177.498 114.327 124.882 1.00 84.99  ?  597  TYR   A CA    1 
ATOM   4774  C  C     . TYR   A 1 597 ? 177.641 113.080 125.740 1.00 86.77  ?  597  TYR   A C     1 
ATOM   4775  O  O     . TYR   A 1 597 ? 177.224 111.985 125.352 1.00 90.05  ?  597  TYR   A O     1 
ATOM   4776  C  CB    . TYR   A 1 597 ? 176.241 115.109 125.282 1.00 84.24  ?  597  TYR   A CB    1 
ATOM   4777  C  CG    . TYR   A 1 597 ? 176.152 116.465 124.620 1.00 84.90  ?  597  TYR   A CG    1 
ATOM   4778  C  CD1   . TYR   A 1 597 ? 176.997 117.499 124.999 1.00 83.38  ?  597  TYR   A CD1   1 
ATOM   4779  C  CD2   . TYR   A 1 597 ? 175.232 116.708 123.611 1.00 83.16  ?  597  TYR   A CD2   1 
ATOM   4780  C  CE1   . TYR   A 1 597 ? 176.923 118.738 124.394 1.00 83.73  ?  597  TYR   A CE1   1 
ATOM   4781  C  CE2   . TYR   A 1 597 ? 175.153 117.944 123.000 1.00 84.00  ?  597  TYR   A CE2   1 
ATOM   4782  C  CZ    . TYR   A 1 597 ? 176.000 118.955 123.396 1.00 85.76  ?  597  TYR   A CZ    1 
ATOM   4783  O  OH    . TYR   A 1 597 ? 175.923 120.188 122.792 1.00 84.71  ?  597  TYR   A OH    1 
ATOM   4784  N  N     . ASP   A 1 598 ? 178.243 113.260 126.916 1.00 101.23 ?  598  ASP   A N     1 
ATOM   4785  C  CA    . ASP   A 1 598 ? 178.509 112.155 127.836 1.00 101.06 ?  598  ASP   A CA    1 
ATOM   4786  C  C     . ASP   A 1 598 ? 177.218 111.809 128.570 1.00 101.92 ?  598  ASP   A C     1 
ATOM   4787  O  O     . ASP   A 1 598 ? 176.947 112.265 129.683 1.00 103.53 ?  598  ASP   A O     1 
ATOM   4788  C  CB    . ASP   A 1 598 ? 179.627 112.519 128.803 1.00 103.20 ?  598  ASP   A CB    1 
ATOM   4789  C  CG    . ASP   A 1 598 ? 180.311 111.300 129.387 1.00 108.15 ?  598  ASP   A CG    1 
ATOM   4790  O  OD1   . ASP   A 1 598 ? 179.842 110.173 129.126 1.00 106.00 ?  598  ASP   A OD1   1 
ATOM   4791  O  OD2   . ASP   A 1 598 ? 181.317 111.468 130.107 1.00 110.53 ?  598  ASP   A OD2   1 
ATOM   4792  N  N     . TRP   A 1 599 ? 176.404 110.974 127.922 1.00 86.63  ?  599  TRP   A N     1 
ATOM   4793  C  CA    . TRP   A 1 599 ? 175.149 110.546 128.524 1.00 84.04  ?  599  TRP   A CA    1 
ATOM   4794  C  C     . TRP   A 1 599 ? 175.360 109.586 129.686 1.00 88.14  ?  599  TRP   A C     1 
ATOM   4795  O  O     . TRP   A 1 599 ? 174.457 109.430 130.511 1.00 92.86  ?  599  TRP   A O     1 
ATOM   4796  C  CB    . TRP   A 1 599 ? 174.252 109.898 127.470 1.00 83.16  ?  599  TRP   A CB    1 
ATOM   4797  C  CG    . TRP   A 1 599 ? 173.621 110.881 126.535 1.00 81.08  ?  599  TRP   A CG    1 
ATOM   4798  C  CD1   . TRP   A 1 599 ? 174.183 111.425 125.420 1.00 85.03  ?  599  TRP   A CD1   1 
ATOM   4799  C  CD2   . TRP   A 1 599 ? 172.307 111.441 126.636 1.00 82.64  ?  599  TRP   A CD2   1 
ATOM   4800  N  NE1   . TRP   A 1 599 ? 173.301 112.288 124.818 1.00 86.13  ?  599  TRP   A NE1   1 
ATOM   4801  C  CE2   . TRP   A 1 599 ? 172.141 112.315 125.546 1.00 85.56  ?  599  TRP   A CE2   1 
ATOM   4802  C  CE3   . TRP   A 1 599 ? 171.254 111.286 127.542 1.00 83.97  ?  599  TRP   A CE3   1 
ATOM   4803  C  CZ2   . TRP   A 1 599 ? 170.967 113.033 125.337 1.00 84.91  ?  599  TRP   A CZ2   1 
ATOM   4804  C  CZ3   . TRP   A 1 599 ? 170.089 112.000 127.332 1.00 84.36  ?  599  TRP   A CZ3   1 
ATOM   4805  C  CH2   . TRP   A 1 599 ? 169.955 112.862 126.239 1.00 85.16  ?  599  TRP   A CH2   1 
ATOM   4806  N  N     . GLU   A 1 600 ? 176.527 108.943 129.774 1.00 97.09  ?  600  GLU   A N     1 
ATOM   4807  C  CA    . GLU   A 1 600 ? 176.778 108.025 130.881 1.00 98.60  ?  600  GLU   A CA    1 
ATOM   4808  C  C     . GLU   A 1 600 ? 177.001 108.778 132.187 1.00 100.39 ?  600  GLU   A C     1 
ATOM   4809  O  O     . GLU   A 1 600 ? 176.498 108.369 133.242 1.00 103.04 ?  600  GLU   A O     1 
ATOM   4810  C  CB    . GLU   A 1 600 ? 177.974 107.132 130.558 1.00 98.65  ?  600  GLU   A CB    1 
ATOM   4811  C  CG    . GLU   A 1 600 ? 177.788 106.292 129.307 1.00 102.21 ?  600  GLU   A CG    1 
ATOM   4812  C  CD    . GLU   A 1 600 ? 176.574 105.388 129.387 1.00 104.77 ?  600  GLU   A CD    1 
ATOM   4813  O  OE1   . GLU   A 1 600 ? 176.300 104.851 130.481 1.00 104.31 ?  600  GLU   A OE1   1 
ATOM   4814  O  OE2   . GLU   A 1 600 ? 175.891 105.214 128.357 1.00 103.98 ?  600  GLU   A OE2   1 
ATOM   4815  N  N     . ALA   A 1 601 ? 177.751 109.881 132.138 1.00 85.97  ?  601  ALA   A N     1 
ATOM   4816  C  CA    . ALA   A 1 601 ? 177.917 110.710 133.327 1.00 87.06  ?  601  ALA   A CA    1 
ATOM   4817  C  C     . ALA   A 1 601 ? 176.582 111.286 133.777 1.00 91.48  ?  601  ALA   A C     1 
ATOM   4818  O  O     . ALA   A 1 601 ? 176.288 111.334 134.978 1.00 93.37  ?  601  ALA   A O     1 
ATOM   4819  C  CB    . ALA   A 1 601 ? 178.923 111.827 133.053 1.00 86.78  ?  601  ALA   A CB    1 
ATOM   4820  N  N     . LEU   A 1 602 ? 175.757 111.724 132.823 1.00 87.22  ?  602  LEU   A N     1 
ATOM   4821  C  CA    . LEU   A 1 602 ? 174.426 112.216 133.160 1.00 82.53  ?  602  LEU   A CA    1 
ATOM   4822  C  C     . LEU   A 1 602 ? 173.568 111.113 133.766 1.00 80.89  ?  602  LEU   A C     1 
ATOM   4823  O  O     . LEU   A 1 602 ? 172.806 111.358 134.706 1.00 82.98  ?  602  LEU   A O     1 
ATOM   4824  C  CB    . LEU   A 1 602 ? 173.752 112.801 131.920 1.00 79.98  ?  602  LEU   A CB    1 
ATOM   4825  C  CG    . LEU   A 1 602 ? 172.422 113.517 132.158 1.00 81.30  ?  602  LEU   A CG    1 
ATOM   4826  C  CD1   . LEU   A 1 602 ? 172.558 114.549 133.264 1.00 81.55  ?  602  LEU   A CD1   1 
ATOM   4827  C  CD2   . LEU   A 1 602 ? 171.927 114.160 130.877 1.00 81.01  ?  602  LEU   A CD2   1 
ATOM   4828  N  N     . ARG   A 1 603 ? 173.672 109.892 133.236 1.00 82.06  ?  603  ARG   A N     1 
ATOM   4829  C  CA    . ARG   A 1 603 ? 172.916 108.776 133.794 1.00 83.12  ?  603  ARG   A CA    1 
ATOM   4830  C  C     . ARG   A 1 603 ? 173.331 108.494 135.231 1.00 89.47  ?  603  ARG   A C     1 
ATOM   4831  O  O     . ARG   A 1 603 ? 172.480 108.265 136.099 1.00 93.18  ?  603  ARG   A O     1 
ATOM   4832  C  CB    . ARG   A 1 603 ? 173.106 107.530 132.928 1.00 83.36  ?  603  ARG   A CB    1 
ATOM   4833  C  CG    . ARG   A 1 603 ? 172.224 106.358 133.321 1.00 88.35  ?  603  ARG   A CG    1 
ATOM   4834  C  CD    . ARG   A 1 603 ? 172.765 105.050 132.768 1.00 86.20  ?  603  ARG   A CD    1 
ATOM   4835  N  NE    . ARG   A 1 603 ? 173.125 105.160 131.360 1.00 86.31  ?  603  ARG   A NE    1 
ATOM   4836  C  CZ    . ARG   A 1 603 ? 172.310 104.877 130.354 1.00 88.73  ?  603  ARG   A CZ    1 
ATOM   4837  N  NH1   . ARG   A 1 603 ? 171.071 104.463 130.564 1.00 89.45  ?  603  ARG   A NH1   1 
ATOM   4838  N  NH2   . ARG   A 1 603 ? 172.748 105.012 129.106 1.00 85.89  ?  603  ARG   A NH2   1 
ATOM   4839  N  N     . GLU   A 1 604 ? 174.639 108.507 135.501 1.00 95.54  ?  604  GLU   A N     1 
ATOM   4840  C  CA    . GLU   A 1 604 ? 175.111 108.302 136.868 1.00 93.79  ?  604  GLU   A CA    1 
ATOM   4841  C  C     . GLU   A 1 604 ? 174.632 109.417 137.791 1.00 95.63  ?  604  GLU   A C     1 
ATOM   4842  O  O     . GLU   A 1 604 ? 174.187 109.156 138.916 1.00 97.94  ?  604  GLU   A O     1 
ATOM   4843  C  CB    . GLU   A 1 604 ? 176.636 108.205 136.888 1.00 93.09  ?  604  GLU   A CB    1 
ATOM   4844  C  CG    . GLU   A 1 604 ? 177.183 106.957 136.219 1.00 100.34 ?  604  GLU   A CG    1 
ATOM   4845  C  CD    . GLU   A 1 604 ? 176.401 105.711 136.585 1.00 102.51 ?  604  GLU   A CD    1 
ATOM   4846  O  OE1   . GLU   A 1 604 ? 176.513 105.255 137.742 1.00 103.12 ?  604  GLU   A OE1   1 
ATOM   4847  O  OE2   . GLU   A 1 604 ? 175.674 105.188 135.715 1.00 99.05  ?  604  GLU   A OE2   1 
ATOM   4848  N  N     . SER   A 1 605 ? 174.704 110.667 137.326 1.00 84.79  ?  605  SER   A N     1 
ATOM   4849  C  CA    . SER   A 1 605 ? 174.258 111.789 138.145 1.00 81.48  ?  605  SER   A CA    1 
ATOM   4850  C  C     . SER   A 1 605 ? 172.765 111.704 138.437 1.00 84.54  ?  605  SER   A C     1 
ATOM   4851  O  O     . SER   A 1 605 ? 172.322 112.032 139.543 1.00 87.69  ?  605  SER   A O     1 
ATOM   4852  C  CB    . SER   A 1 605 ? 174.596 113.109 137.453 1.00 82.44  ?  605  SER   A CB    1 
ATOM   4853  O  OG    . SER   A 1 605 ? 174.472 114.200 138.348 1.00 87.08  ?  605  SER   A OG    1 
ATOM   4854  N  N     . ILE   A 1 606 ? 171.971 111.277 137.453 1.00 76.65  ?  606  ILE   A N     1 
ATOM   4855  C  CA    . ILE   A 1 606 ? 170.533 111.141 137.660 1.00 74.32  ?  606  ILE   A CA    1 
ATOM   4856  C  C     . ILE   A 1 606 ? 170.237 110.002 138.627 1.00 78.24  ?  606  ILE   A C     1 
ATOM   4857  O  O     . ILE   A 1 606 ? 169.374 110.123 139.503 1.00 80.94  ?  606  ILE   A O     1 
ATOM   4858  C  CB    . ILE   A 1 606 ? 169.818 110.946 136.310 1.00 74.14  ?  606  ILE   A CB    1 
ATOM   4859  C  CG1   . ILE   A 1 606 ? 169.850 112.243 135.500 1.00 77.15  ?  606  ILE   A CG1   1 
ATOM   4860  C  CG2   . ILE   A 1 606 ? 168.384 110.492 136.520 1.00 76.64  ?  606  ILE   A CG2   1 
ATOM   4861  C  CD1   . ILE   A 1 606 ? 169.506 112.058 134.041 1.00 77.59  ?  606  ILE   A CD1   1 
ATOM   4862  N  N     . LYS   A 1 607 ? 170.947 108.879 138.491 1.00 87.55  ?  607  LYS   A N     1 
ATOM   4863  C  CA    . LYS   A 1 607 ? 170.745 107.772 139.418 1.00 90.28  ?  607  LYS   A CA    1 
ATOM   4864  C  C     . LYS   A 1 607 ? 171.163 108.142 140.835 1.00 90.36  ?  607  LYS   A C     1 
ATOM   4865  O  O     . LYS   A 1 607 ? 170.626 107.590 141.802 1.00 90.49  ?  607  LYS   A O     1 
ATOM   4866  C  CB    . LYS   A 1 607 ? 171.511 106.538 138.941 1.00 90.13  ?  607  LYS   A CB    1 
ATOM   4867  C  CG    . LYS   A 1 607 ? 170.730 105.662 137.976 1.00 92.54  ?  607  LYS   A CG    1 
ATOM   4868  C  CD    . LYS   A 1 607 ? 171.022 104.189 138.203 1.00 92.04  ?  607  LYS   A CD    1 
ATOM   4869  C  CE    . LYS   A 1 607 ? 172.400 103.814 137.686 1.00 92.30  ?  607  LYS   A CE    1 
ATOM   4870  N  NZ    . LYS   A 1 607 ? 172.343 102.660 136.748 1.00 95.54  ?  607  LYS   A NZ    1 
ATOM   4871  N  N     . THR   A 1 608 ? 172.110 109.070 140.979 1.00 90.41  ?  608  THR   A N     1 
ATOM   4872  C  CA    . THR   A 1 608 ? 172.559 109.467 142.310 1.00 91.10  ?  608  THR   A CA    1 
ATOM   4873  C  C     . THR   A 1 608 ? 171.629 110.503 142.936 1.00 91.27  ?  608  THR   A C     1 
ATOM   4874  O  O     . THR   A 1 608 ? 171.085 110.287 144.024 1.00 92.31  ?  608  THR   A O     1 
ATOM   4875  C  CB    . THR   A 1 608 ? 173.991 110.005 142.242 1.00 91.66  ?  608  THR   A CB    1 
ATOM   4876  O  OG1   . THR   A 1 608 ? 174.893 108.933 141.940 1.00 96.68  ?  608  THR   A OG1   1 
ATOM   4877  C  CG2   . THR   A 1 608 ? 174.388 110.633 143.568 1.00 87.09  ?  608  THR   A CG2   1 
ATOM   4878  N  N     . HIS   A 1 609 ? 171.431 111.637 142.260 1.00 88.81  ?  609  HIS   A N     1 
ATOM   4879  C  CA    . HIS   A 1 609 ? 170.706 112.761 142.839 1.00 84.39  ?  609  HIS   A CA    1 
ATOM   4880  C  C     . HIS   A 1 609 ? 169.281 112.911 142.324 1.00 87.93  ?  609  HIS   A C     1 
ATOM   4881  O  O     . HIS   A 1 609 ? 168.473 113.577 142.981 1.00 89.17  ?  609  HIS   A O     1 
ATOM   4882  C  CB    . HIS   A 1 609 ? 171.464 114.068 142.580 1.00 82.72  ?  609  HIS   A CB    1 
ATOM   4883  C  CG    . HIS   A 1 609 ? 172.867 114.064 143.099 1.00 91.05  ?  609  HIS   A CG    1 
ATOM   4884  N  ND1   . HIS   A 1 609 ? 173.967 114.106 142.270 1.00 94.14  ?  609  HIS   A ND1   1 
ATOM   4885  C  CD2   . HIS   A 1 609 ? 173.351 114.022 144.363 1.00 91.14  ?  609  HIS   A CD2   1 
ATOM   4886  C  CE1   . HIS   A 1 609 ? 175.068 114.091 143.000 1.00 93.73  ?  609  HIS   A CE1   1 
ATOM   4887  N  NE2   . HIS   A 1 609 ? 174.722 114.040 144.273 1.00 95.41  ?  609  HIS   A NE2   1 
ATOM   4888  N  N     . GLY   A 1 610 ? 168.951 112.321 141.183 1.00 80.98  ?  610  GLY   A N     1 
ATOM   4889  C  CA    . GLY   A 1 610 ? 167.612 112.435 140.643 1.00 76.95  ?  610  GLY   A CA    1 
ATOM   4890  C  C     . GLY   A 1 610 ? 167.408 113.684 139.811 1.00 77.58  ?  610  GLY   A C     1 
ATOM   4891  O  O     . GLY   A 1 610 ? 168.329 114.454 139.523 1.00 78.17  ?  610  GLY   A O     1 
ATOM   4892  N  N     . LEU   A 1 611 ? 166.153 113.879 139.416 1.00 74.84  ?  611  LEU   A N     1 
ATOM   4893  C  CA    . LEU   A 1 611 ? 165.744 115.013 138.602 1.00 71.84  ?  611  LEU   A CA    1 
ATOM   4894  C  C     . LEU   A 1 611 ? 164.688 115.820 139.340 1.00 71.27  ?  611  LEU   A C     1 
ATOM   4895  O  O     . LEU   A 1 611 ? 163.836 115.258 140.035 1.00 76.04  ?  611  LEU   A O     1 
ATOM   4896  C  CB    . LEU   A 1 611 ? 165.190 114.558 137.248 1.00 70.65  ?  611  LEU   A CB    1 
ATOM   4897  C  CG    . LEU   A 1 611 ? 166.186 113.960 136.256 1.00 71.46  ?  611  LEU   A CG    1 
ATOM   4898  C  CD1   . LEU   A 1 611 ? 165.450 113.288 135.113 1.00 71.83  ?  611  LEU   A CD1   1 
ATOM   4899  C  CD2   . LEU   A 1 611 ? 167.130 115.030 135.735 1.00 73.57  ?  611  LEU   A CD2   1 
ATOM   4900  N  N     . ARG   A 1 612 ? 164.751 117.144 139.189 1.00 67.33  ?  612  ARG   A N     1 
ATOM   4901  C  CA    . ARG   A 1 612 ? 163.749 118.002 139.809 1.00 72.69  ?  612  ARG   A CA    1 
ATOM   4902  C  C     . ARG   A 1 612 ? 162.397 117.869 139.121 1.00 80.02  ?  612  ARG   A C     1 
ATOM   4903  O  O     . ARG   A 1 612 ? 161.355 118.003 139.772 1.00 84.11  ?  612  ARG   A O     1 
ATOM   4904  C  CB    . ARG   A 1 612 ? 164.221 119.456 139.788 1.00 71.33  ?  612  ARG   A CB    1 
ATOM   4905  C  CG    . ARG   A 1 612 ? 163.277 120.429 140.470 1.00 66.75  ?  612  ARG   A CG    1 
ATOM   4906  C  CD    . ARG   A 1 612 ? 163.576 120.541 141.953 1.00 70.57  ?  612  ARG   A CD    1 
ATOM   4907  N  NE    . ARG   A 1 612 ? 162.706 121.508 142.610 1.00 75.51  ?  612  ARG   A NE    1 
ATOM   4908  C  CZ    . ARG   A 1 612 ? 161.966 121.244 143.678 1.00 78.31  ?  612  ARG   A CZ    1 
ATOM   4909  N  NH1   . ARG   A 1 612 ? 161.969 120.048 144.243 1.00 79.84  ?  612  ARG   A NH1   1 
ATOM   4910  N  NH2   . ARG   A 1 612 ? 161.202 122.204 144.191 1.00 74.87  ?  612  ARG   A NH2   1 
ATOM   4911  N  N     . ASN   A 1 613 ? 162.393 117.595 137.820 1.00 70.00  ?  613  ASN   A N     1 
ATOM   4912  C  CA    . ASN   A 1 613 ? 161.174 117.498 137.032 1.00 63.05  ?  613  ASN   A CA    1 
ATOM   4913  C  C     . ASN   A 1 613 ? 161.098 116.133 136.362 1.00 68.61  ?  613  ASN   A C     1 
ATOM   4914  O  O     . ASN   A 1 613 ? 162.098 115.632 135.839 1.00 80.06  ?  613  ASN   A O     1 
ATOM   4915  C  CB    . ASN   A 1 613 ? 161.119 118.606 135.979 1.00 66.28  ?  613  ASN   A CB    1 
ATOM   4916  C  CG    . ASN   A 1 613 ? 161.439 119.970 136.555 1.00 69.82  ?  613  ASN   A CG    1 
ATOM   4917  O  OD1   . ASN   A 1 613 ? 162.568 120.448 136.460 1.00 75.31  ?  613  ASN   A OD1   1 
ATOM   4918  N  ND2   . ASN   A 1 613 ? 160.444 120.604 137.161 1.00 72.49  ?  613  ASN   A ND2   1 
ATOM   4919  N  N     . SER   A 1 614 ? 159.906 115.531 136.389 1.00 70.87  ?  614  SER   A N     1 
ATOM   4920  C  CA    . SER   A 1 614 ? 159.720 114.230 135.753 1.00 71.15  ?  614  SER   A CA    1 
ATOM   4921  C  C     . SER   A 1 614 ? 159.903 114.318 134.243 1.00 73.84  ?  614  SER   A C     1 
ATOM   4922  O  O     . SER   A 1 614 ? 160.549 113.455 133.639 1.00 81.31  ?  614  SER   A O     1 
ATOM   4923  C  CB    . SER   A 1 614 ? 158.339 113.673 136.095 1.00 71.43  ?  614  SER   A CB    1 
ATOM   4924  O  OG    . SER   A 1 614 ? 158.245 113.351 137.471 1.00 79.95  ?  614  SER   A OG    1 
ATOM   4925  N  N     . THR   A 1 615 ? 159.343 115.351 133.616 1.00 69.43  ?  615  THR   A N     1 
ATOM   4926  C  CA    . THR   A 1 615 ? 159.480 115.575 132.185 1.00 68.82  ?  615  THR   A CA    1 
ATOM   4927  C  C     . THR   A 1 615 ? 159.998 116.983 131.943 1.00 73.73  ?  615  THR   A C     1 
ATOM   4928  O  O     . THR   A 1 615 ? 159.814 117.880 132.769 1.00 80.45  ?  615  THR   A O     1 
ATOM   4929  C  CB    . THR   A 1 615 ? 158.151 115.394 131.435 1.00 77.20  ?  615  THR   A CB    1 
ATOM   4930  O  OG1   . THR   A 1 615 ? 157.296 116.514 131.697 1.00 76.90  ?  615  THR   A OG1   1 
ATOM   4931  C  CG2   . THR   A 1 615 ? 157.456 114.124 131.870 1.00 78.11  ?  615  THR   A CG2   1 
ATOM   4932  N  N     . LEU   A 1 616 ? 160.656 117.167 130.799 1.00 74.68  ?  616  LEU   A N     1 
ATOM   4933  C  CA    . LEU   A 1 616 ? 161.203 118.472 130.453 1.00 73.63  ?  616  LEU   A CA    1 
ATOM   4934  C  C     . LEU   A 1 616 ? 160.966 118.895 129.013 1.00 72.05  ?  616  LEU   A C     1 
ATOM   4935  O  O     . LEU   A 1 616 ? 161.195 120.067 128.703 1.00 81.12  ?  616  LEU   A O     1 
ATOM   4936  C  CB    . LEU   A 1 616 ? 162.712 118.503 130.730 1.00 68.02  ?  616  LEU   A CB    1 
ATOM   4937  C  CG    . LEU   A 1 616 ? 163.123 118.391 132.197 1.00 66.30  ?  616  LEU   A CG    1 
ATOM   4938  C  CD1   . LEU   A 1 616 ? 164.225 117.362 132.359 1.00 69.83  ?  616  LEU   A CD1   1 
ATOM   4939  C  CD2   . LEU   A 1 616 ? 163.558 119.743 132.734 1.00 71.29  ?  616  LEU   A CD2   1 
ATOM   4940  N  N     . SER   A 1 617 ? 160.517 118.009 128.128 1.00 64.28  ?  617  SER   A N     1 
ATOM   4941  C  CA    . SER   A 1 617 ? 160.449 118.304 126.704 1.00 62.35  ?  617  SER   A CA    1 
ATOM   4942  C  C     . SER   A 1 617 ? 159.050 118.031 126.175 1.00 72.24  ?  617  SER   A C     1 
ATOM   4943  O  O     . SER   A 1 617 ? 158.471 116.977 126.455 1.00 79.20  ?  617  SER   A O     1 
ATOM   4944  C  CB    . SER   A 1 617 ? 161.477 117.474 125.931 1.00 66.45  ?  617  SER   A CB    1 
ATOM   4945  O  OG    . SER   A 1 617 ? 162.743 118.110 125.925 1.00 74.53  ?  617  SER   A OG    1 
ATOM   4946  N  N     . ALA   A 1 618 ? 158.517 118.982 125.410 1.00 70.26  ?  618  ALA   A N     1 
ATOM   4947  C  CA    . ALA   A 1 618 ? 157.231 118.818 124.736 1.00 67.44  ?  618  ALA   A CA    1 
ATOM   4948  C  C     . ALA   A 1 618 ? 157.140 119.870 123.644 1.00 72.70  ?  618  ALA   A C     1 
ATOM   4949  O  O     . ALA   A 1 618 ? 157.224 121.067 123.935 1.00 81.47  ?  618  ALA   A O     1 
ATOM   4950  C  CB    . ALA   A 1 618 ? 156.068 118.954 125.718 1.00 68.80  ?  618  ALA   A CB    1 
ATOM   4951  N  N     . LEU   A 1 619 ? 156.965 119.437 122.398 1.00 67.25  ?  619  LEU   A N     1 
ATOM   4952  C  CA    . LEU   A 1 619 ? 156.943 120.366 121.271 1.00 69.84  ?  619  LEU   A CA    1 
ATOM   4953  C  C     . LEU   A 1 619 ? 155.534 120.941 121.104 1.00 76.64  ?  619  LEU   A C     1 
ATOM   4954  O  O     . LEU   A 1 619 ? 154.568 120.204 120.991 1.00 80.12  ?  619  LEU   A O     1 
ATOM   4955  C  CB    . LEU   A 1 619 ? 157.390 119.655 119.996 1.00 68.84  ?  619  LEU   A CB    1 
ATOM   4956  C  CG    . LEU   A 1 619 ? 158.840 119.168 119.998 1.00 70.48  ?  619  LEU   A CG    1 
ATOM   4957  C  CD1   . LEU   A 1 619 ? 159.311 118.898 118.584 1.00 75.55  ?  619  LEU   A CD1   1 
ATOM   4958  C  CD2   . LEU   A 1 619 ? 159.751 120.176 120.682 1.00 67.46  ?  619  LEU   A CD2   1 
ATOM   4959  N  N     . MET   A 1 620 ? 155.366 122.244 121.133 1.00 92.19  ?  620  MET   A N     1 
ATOM   4960  C  CA    . MET   A 1 620 ? 153.997 122.670 120.901 1.00 84.82  ?  620  MET   A CA    1 
ATOM   4961  C  C     . MET   A 1 620 ? 154.050 123.876 120.013 1.00 89.24  ?  620  MET   A C     1 
ATOM   4962  O  O     . MET   A 1 620 ? 154.951 124.714 120.140 1.00 95.84  ?  620  MET   A O     1 
ATOM   4963  C  CB    . MET   A 1 620 ? 153.186 123.032 122.140 1.00 87.45  ?  620  MET   A CB    1 
ATOM   4964  C  CG    . MET   A 1 620 ? 151.760 123.470 121.830 1.00 92.00  ?  620  MET   A CG    1 
ATOM   4965  S  SD    . MET   A 1 620 ? 150.638 123.681 123.237 1.00 102.80 ?  620  MET   A SD    1 
ATOM   4966  C  CE    . MET   A 1 620 ? 149.250 124.332 122.448 1.00 88.24  ?  620  MET   A CE    1 
ATOM   4967  N  N     . PRO   A 1 621 ? 153.157 123.879 119.050 1.00 92.85  ?  621  PRO   A N     1 
ATOM   4968  C  CA    . PRO   A 1 621 ? 152.964 125.014 118.180 1.00 93.77  ?  621  PRO   A CA    1 
ATOM   4969  C  C     . PRO   A 1 621 ? 152.470 126.155 119.015 1.00 96.79  ?  621  PRO   A C     1 
ATOM   4970  O  O     . PRO   A 1 621 ? 151.481 125.981 119.691 1.00 99.46  ?  621  PRO   A O     1 
ATOM   4971  C  CB    . PRO   A 1 621 ? 151.819 124.526 117.312 1.00 94.05  ?  621  PRO   A CB    1 
ATOM   4972  C  CG    . PRO   A 1 621 ? 151.050 123.582 118.185 1.00 94.25  ?  621  PRO   A CG    1 
ATOM   4973  C  CD    . PRO   A 1 621 ? 152.207 122.804 118.705 1.00 94.73  ?  621  PRO   A CD    1 
ATOM   4974  N  N     . SER   A 1 622 ? 153.111 127.306 118.973 1.00 105.85 ?  622  SER   A N     1 
ATOM   4975  C  CA    . SER   A 1 622 ? 152.646 128.507 119.666 1.00 107.97 ?  622  SER   A CA    1 
ATOM   4976  C  C     . SER   A 1 622 ? 152.595 129.643 118.651 1.00 108.10 ?  622  SER   A C     1 
ATOM   4977  O  O     . SER   A 1 622 ? 153.639 130.167 118.248 1.00 109.91 ?  622  SER   A O     1 
ATOM   4978  C  CB    . SER   A 1 622 ? 153.571 128.852 120.831 1.00 106.69 ?  622  SER   A CB    1 
ATOM   4979  O  OG    . SER   A 1 622 ? 154.927 128.863 120.418 1.00 107.49 ?  622  SER   A OG    1 
ATOM   4980  N  N     . GLU   A 1 623 ? 151.384 130.015 118.234 1.00 113.67 ?  623  GLU   A N     1 
ATOM   4981  C  CA    . GLU   A 1 623 ? 151.233 131.079 117.247 1.00 113.93 ?  623  GLU   A CA    1 
ATOM   4982  C  C     . GLU   A 1 623 ? 151.668 132.426 117.811 1.00 115.29 ?  623  GLU   A C     1 
ATOM   4983  O  O     . GLU   A 1 623 ? 152.462 133.141 117.191 1.00 117.99 ?  623  GLU   A O     1 
ATOM   4984  C  CB    . GLU   A 1 623 ? 149.784 131.140 116.764 1.00 114.68 ?  623  GLU   A CB    1 
ATOM   4985  C  CG    . GLU   A 1 623 ? 149.591 131.923 115.475 1.00 117.64 ?  623  GLU   A CG    1 
ATOM   4986  C  CD    . GLU   A 1 623 ? 150.460 131.409 114.344 1.00 121.23 ?  623  GLU   A CD    1 
ATOM   4987  O  OE1   . GLU   A 1 623 ? 150.083 130.397 113.716 1.00 120.17 ?  623  GLU   A OE1   1 
ATOM   4988  O  OE2   . GLU   A 1 623 ? 151.519 132.016 114.081 1.00 121.87 ?  623  GLU   A OE2   1 
ATOM   4989  N  N     . THR   A 1 624 ? 151.160 132.788 118.992 1.00 106.44 ?  624  THR   A N     1 
ATOM   4990  C  CA    . THR   A 1 624 ? 151.470 134.095 119.564 1.00 105.28 ?  624  THR   A CA    1 
ATOM   4991  C  C     . THR   A 1 624 ? 152.934 134.196 119.974 1.00 105.65 ?  624  THR   A C     1 
ATOM   4992  O  O     . THR   A 1 624 ? 153.581 135.226 119.740 1.00 110.06 ?  624  THR   A O     1 
ATOM   4993  C  CB    . THR   A 1 624 ? 150.562 134.371 120.763 1.00 106.10 ?  624  THR   A CB    1 
ATOM   4994  O  OG1   . THR   A 1 624 ? 149.197 134.141 120.394 1.00 108.60 ?  624  THR   A OG1   1 
ATOM   4995  C  CG2   . THR   A 1 624 ? 150.721 135.809 121.232 1.00 106.33 ?  624  THR   A CG2   1 
ATOM   4996  N  N     . SER   A 1 625 ? 153.472 133.142 120.591 1.00 103.85 ?  625  SER   A N     1 
ATOM   4997  C  CA    . SER   A 1 625 ? 154.861 133.173 121.037 1.00 105.92 ?  625  SER   A CA    1 
ATOM   4998  C  C     . SER   A 1 625 ? 155.818 133.303 119.859 1.00 106.32 ?  625  SER   A C     1 
ATOM   4999  O  O     . SER   A 1 625 ? 156.810 134.038 119.934 1.00 109.74 ?  625  SER   A O     1 
ATOM   5000  C  CB    . SER   A 1 625 ? 155.175 131.921 121.854 1.00 107.15 ?  625  SER   A CB    1 
ATOM   5001  O  OG    . SER   A 1 625 ? 154.053 131.518 122.619 1.00 109.20 ?  625  SER   A OG    1 
ATOM   5002  N  N     . SER   A 1 626 ? 155.543 132.590 118.765 1.00 100.91 ?  626  SER   A N     1 
ATOM   5003  C  CA    . SER   A 1 626 ? 156.379 132.718 117.578 1.00 100.92 ?  626  SER   A CA    1 
ATOM   5004  C  C     . SER   A 1 626 ? 156.178 134.066 116.900 1.00 103.89 ?  626  SER   A C     1 
ATOM   5005  O  O     . SER   A 1 626 ? 157.128 134.639 116.355 1.00 107.39 ?  626  SER   A O     1 
ATOM   5006  C  CB    . SER   A 1 626 ? 156.089 131.580 116.602 1.00 102.68 ?  626  SER   A CB    1 
ATOM   5007  O  OG    . SER   A 1 626 ? 154.795 131.708 116.039 1.00 106.10 ?  626  SER   A OG    1 
ATOM   5008  N  N     . GLN   A 1 627 ? 154.949 134.585 116.870 1.00 107.51 ?  627  GLN   A N     1 
ATOM   5009  C  CA    . GLN   A 1 627 ? 154.805 135.909 116.273 1.00 106.95 ?  627  GLN   A CA    1 
ATOM   5010  C  C     . GLN   A 1 627 ? 155.594 136.932 117.053 1.00 107.47 ?  627  GLN   A C     1 
ATOM   5011  O  O     . GLN   A 1 627 ? 156.390 137.649 116.475 1.00 111.57 ?  627  GLN   A O     1 
ATOM   5012  C  CB    . GLN   A 1 627 ? 153.360 136.378 116.152 1.00 106.87 ?  627  GLN   A CB    1 
ATOM   5013  C  CG    . GLN   A 1 627 ? 152.735 136.108 114.808 1.00 108.56 ?  627  GLN   A CG    1 
ATOM   5014  C  CD    . GLN   A 1 627 ? 151.237 136.110 114.895 1.00 112.59 ?  627  GLN   A CD    1 
ATOM   5015  O  OE1   . GLN   A 1 627 ? 150.666 136.113 115.986 1.00 109.47 ?  627  GLN   A OE1   1 
ATOM   5016  N  NE2   . GLN   A 1 627 ? 150.583 136.107 113.750 1.00 113.71 ?  627  GLN   A NE2   1 
ATOM   5017  N  N     . ILE   A 1 628 ? 155.454 136.982 118.369 1.00 95.83  ?  628  ILE   A N     1 
ATOM   5018  C  CA    . ILE   A 1 628 ? 156.148 138.035 119.106 1.00 94.87  ?  628  ILE   A CA    1 
ATOM   5019  C  C     . ILE   A 1 628 ? 157.659 137.924 118.920 1.00 95.32  ?  628  ILE   A C     1 
ATOM   5020  O  O     . ILE   A 1 628 ? 158.362 138.936 118.807 1.00 99.44  ?  628  ILE   A O     1 
ATOM   5021  C  CB    . ILE   A 1 628 ? 155.737 137.996 120.586 1.00 92.67  ?  628  ILE   A CB    1 
ATOM   5022  C  CG1   . ILE   A 1 628 ? 154.450 138.799 120.778 1.00 96.50  ?  628  ILE   A CG1   1 
ATOM   5023  C  CG2   . ILE   A 1 628 ? 156.845 138.532 121.480 1.00 92.87  ?  628  ILE   A CG2   1 
ATOM   5024  C  CD1   . ILE   A 1 628 ? 153.948 138.825 122.188 1.00 96.72  ?  628  ILE   A CD1   1 
ATOM   5025  N  N     . SER   A 1 629 ? 158.177 136.702 118.857 1.00 101.72 ?  629  SER   A N     1 
ATOM   5026  C  CA    . SER   A 1 629 ? 159.604 136.491 118.660 1.00 102.95 ?  629  SER   A CA    1 
ATOM   5027  C  C     . SER   A 1 629 ? 160.027 136.613 117.202 1.00 103.45 ?  629  SER   A C     1 
ATOM   5028  O  O     . SER   A 1 629 ? 161.220 136.470 116.911 1.00 103.38 ?  629  SER   A O     1 
ATOM   5029  C  CB    . SER   A 1 629 ? 160.010 135.116 119.197 1.00 104.26 ?  629  SER   A CB    1 
ATOM   5030  O  OG    . SER   A 1 629 ? 159.641 134.971 120.558 1.00 106.48 ?  629  SER   A OG    1 
ATOM   5031  N  N     . ASN   A 1 630 ? 159.089 136.878 116.292 1.00 102.66 ?  630  ASN   A N     1 
ATOM   5032  C  CA    . ASN   A 1 630 ? 159.347 136.890 114.853 1.00 100.78 ?  630  ASN   A CA    1 
ATOM   5033  C  C     . ASN   A 1 630 ? 159.967 135.564 114.417 1.00 104.80 ?  630  ASN   A C     1 
ATOM   5034  O  O     . ASN   A 1 630 ? 161.089 135.496 113.912 1.00 107.50 ?  630  ASN   A O     1 
ATOM   5035  C  CB    . ASN   A 1 630 ? 160.229 138.076 114.455 1.00 104.66 ?  630  ASN   A CB    1 
ATOM   5036  C  CG    . ASN   A 1 630 ? 160.262 138.299 112.955 1.00 107.78 ?  630  ASN   A CG    1 
ATOM   5037  O  OD1   . ASN   A 1 630 ? 159.394 137.820 112.225 1.00 105.04 ?  630  ASN   A OD1   1 
ATOM   5038  N  ND2   . ASN   A 1 630 ? 161.267 139.030 112.488 1.00 107.64 ?  630  ASN   A ND2   1 
ATOM   5039  N  N     . ALA   A 1 631 ? 159.204 134.497 114.634 1.00 95.77  ?  631  ALA   A N     1 
ATOM   5040  C  CA    . ALA   A 1 631 ? 159.689 133.142 114.438 1.00 93.21  ?  631  ALA   A CA    1 
ATOM   5041  C  C     . ALA   A 1 631 ? 158.626 132.318 113.730 1.00 95.96  ?  631  ALA   A C     1 
ATOM   5042  O  O     . ALA   A 1 631 ? 157.432 132.618 113.794 1.00 96.48  ?  631  ALA   A O     1 
ATOM   5043  C  CB    . ALA   A 1 631 ? 160.059 132.489 115.775 1.00 91.77  ?  631  ALA   A CB    1 
ATOM   5044  N  N     . THR   A 1 632 ? 159.077 131.273 113.043 1.00 99.80  ?  632  THR   A N     1 
ATOM   5045  C  CA    . THR   A 1 632 ? 158.152 130.314 112.460 1.00 101.00 ?  632  THR   A CA    1 
ATOM   5046  C  C     . THR   A 1 632 ? 157.460 129.520 113.562 1.00 99.71  ?  632  THR   A C     1 
ATOM   5047  O  O     . THR   A 1 632 ? 158.037 129.245 114.617 1.00 99.25  ?  632  THR   A O     1 
ATOM   5048  C  CB    . THR   A 1 632 ? 158.881 129.370 111.504 1.00 98.18  ?  632  THR   A CB    1 
ATOM   5049  O  OG1   . THR   A 1 632 ? 160.192 129.092 112.008 1.00 99.50  ?  632  THR   A OG1   1 
ATOM   5050  C  CG2   . THR   A 1 632 ? 159.000 129.998 110.124 1.00 94.70  ?  632  THR   A CG2   1 
ATOM   5051  N  N     . ASN   A 1 633 ? 156.207 129.154 113.307 1.00 98.59  ?  633  ASN   A N     1 
ATOM   5052  C  CA    . ASN   A 1 633 ? 155.371 128.523 114.324 1.00 97.26  ?  633  ASN   A CA    1 
ATOM   5053  C  C     . ASN   A 1 633 ? 155.898 127.129 114.642 1.00 102.51 ?  633  ASN   A C     1 
ATOM   5054  O  O     . ASN   A 1 633 ? 155.725 126.196 113.851 1.00 104.60 ?  633  ASN   A O     1 
ATOM   5055  C  CB    . ASN   A 1 633 ? 153.924 128.462 113.847 1.00 99.02  ?  633  ASN   A CB    1 
ATOM   5056  C  CG    . ASN   A 1 633 ? 152.953 128.155 114.969 1.00 104.63 ?  633  ASN   A CG    1 
ATOM   5057  O  OD1   . ASN   A 1 633 ? 153.304 128.229 116.145 1.00 107.48 ?  633  ASN   A OD1   1 
ATOM   5058  N  ND2   . ASN   A 1 633 ? 151.724 127.806 114.609 1.00 103.31 ?  633  ASN   A ND2   1 
ATOM   5059  N  N     . GLY   A 1 634 ? 156.531 126.987 115.804 1.00 89.25  ?  634  GLY   A N     1 
ATOM   5060  C  CA    . GLY   A 1 634 ? 156.964 125.677 116.266 1.00 84.85  ?  634  GLY   A CA    1 
ATOM   5061  C  C     . GLY   A 1 634 ? 157.948 125.028 115.315 1.00 85.69  ?  634  GLY   A C     1 
ATOM   5062  O  O     . GLY   A 1 634 ? 158.936 125.637 114.889 1.00 89.02  ?  634  GLY   A O     1 
ATOM   5063  N  N     . ILE   A 1 635 ? 157.682 123.767 114.976 1.00 86.87  ?  635  ILE   A N     1 
ATOM   5064  C  CA    . ILE   A 1 635 ? 158.532 123.004 114.069 1.00 87.39  ?  635  ILE   A CA    1 
ATOM   5065  C  C     . ILE   A 1 635 ? 157.923 122.848 112.692 1.00 87.69  ?  635  ILE   A C     1 
ATOM   5066  O  O     . ILE   A 1 635 ? 158.586 122.307 111.789 1.00 90.80  ?  635  ILE   A O     1 
ATOM   5067  C  CB    . ILE   A 1 635 ? 158.883 121.622 114.654 1.00 82.67  ?  635  ILE   A CB    1 
ATOM   5068  C  CG1   . ILE   A 1 635 ? 157.620 120.893 115.115 1.00 86.90  ?  635  ILE   A CG1   1 
ATOM   5069  C  CG2   . ILE   A 1 635 ? 159.855 121.764 115.814 1.00 81.80  ?  635  ILE   A CG2   1 
ATOM   5070  C  CD1   . ILE   A 1 635 ? 157.096 119.883 114.124 1.00 85.69  ?  635  ILE   A CD1   1 
ATOM   5071  N  N     . GLU   A 1 636 ? 156.730 123.312 112.481 1.00 102.42 ?  636  GLU   A N     1 
ATOM   5072  C  CA    . GLU   A 1 636 ? 156.052 123.168 111.191 1.00 102.69 ?  636  GLU   A CA    1 
ATOM   5073  C  C     . GLU   A 1 636 ? 156.674 124.110 110.210 1.00 104.66 ?  636  GLU   A C     1 
ATOM   5074  O  O     . GLU   A 1 636 ? 156.991 125.205 110.618 1.00 104.87 ?  636  GLU   A O     1 
ATOM   5075  C  CB    . GLU   A 1 636 ? 154.685 123.804 111.264 1.00 101.27 ?  636  GLU   A CB    1 
ATOM   5076  C  CG    . GLU   A 1 636 ? 153.747 123.122 112.223 1.00 103.49 ?  636  GLU   A CG    1 
ATOM   5077  C  CD    . GLU   A 1 636 ? 153.547 121.657 111.876 1.00 109.78 ?  636  GLU   A CD    1 
ATOM   5078  O  OE1   . GLU   A 1 636 ? 153.445 121.353 110.674 1.00 109.81 ?  636  GLU   A OE1   1 
ATOM   5079  O  OE2   . GLU   A 1 636 ? 153.492 120.825 112.805 1.00 110.05 ?  636  GLU   A OE2   1 
ATOM   5080  N  N     . PRO   A 1 637 ? 156.790 123.765 108.926 1.00 97.74  ?  637  PRO   A N     1 
ATOM   5081  C  CA    . PRO   A 1 637 ? 157.242 124.743 107.927 1.00 95.23  ?  637  PRO   A CA    1 
ATOM   5082  C  C     . PRO   A 1 637 ? 156.190 125.815 107.709 1.00 96.40  ?  637  PRO   A C     1 
ATOM   5083  O  O     . PRO   A 1 637 ? 154.982 125.554 107.840 1.00 94.67  ?  637  PRO   A O     1 
ATOM   5084  C  CB    . PRO   A 1 637 ? 157.440 123.889 106.660 1.00 94.88  ?  637  PRO   A CB    1 
ATOM   5085  C  CG    . PRO   A 1 637 ? 156.576 122.695 106.870 1.00 97.70  ?  637  PRO   A CG    1 
ATOM   5086  C  CD    . PRO   A 1 637 ? 156.589 122.432 108.344 1.00 97.43  ?  637  PRO   A CD    1 
ATOM   5087  N  N     . PRO   A 1 638 ? 156.600 127.042 107.389 1.00 91.46  ?  638  PRO   A N     1 
ATOM   5088  C  CA    . PRO   A 1 638 ? 155.617 128.108 107.166 1.00 91.64  ?  638  PRO   A CA    1 
ATOM   5089  C  C     . PRO   A 1 638 ? 154.750 127.822 105.950 1.00 94.10  ?  638  PRO   A C     1 
ATOM   5090  O  O     . PRO   A 1 638 ? 155.214 127.281 104.944 1.00 93.16  ?  638  PRO   A O     1 
ATOM   5091  C  CB    . PRO   A 1 638 ? 156.483 129.355 106.957 1.00 90.58  ?  638  PRO   A CB    1 
ATOM   5092  C  CG    . PRO   A 1 638 ? 157.799 128.829 106.500 1.00 88.48  ?  638  PRO   A CG    1 
ATOM   5093  C  CD    . PRO   A 1 638 ? 157.982 127.508 107.183 1.00 89.47  ?  638  PRO   A CD    1 
ATOM   5094  N  N     . ARG   A 1 639 ? 153.487 128.202 105.987 1.00 104.64 ?  639  ARG   A N     1 
ATOM   5095  C  CA    . ARG   A 1 639 ? 152.591 127.960 104.834 1.00 102.87 ?  639  ARG   A CA    1 
ATOM   5096  C  C     . ARG   A 1 639 ? 152.961 128.914 103.704 1.00 105.59 ?  639  ARG   A C     1 
ATOM   5097  O  O     . ARG   A 1 639 ? 152.934 128.502 102.557 1.00 105.95 ?  639  ARG   A O     1 
ATOM   5098  C  CB    . ARG   A 1 639 ? 151.102 128.167 105.095 1.00 103.15 ?  639  ARG   A CB    1 
ATOM   5099  C  CG    . ARG   A 1 639 ? 150.481 127.168 106.055 1.00 107.19 ?  639  ARG   A CG    1 
ATOM   5100  C  CD    . ARG   A 1 639 ? 149.012 127.422 106.336 1.00 107.71 ?  639  ARG   A CD    1 
ATOM   5101  N  NE    . ARG   A 1 639 ? 148.471 126.421 107.242 1.00 108.91 ?  639  ARG   A NE    1 
ATOM   5102  C  CZ    . ARG   A 1 639 ? 148.582 126.468 108.565 1.00 110.66 ?  639  ARG   A CZ    1 
ATOM   5103  N  NH1   . ARG   A 1 639 ? 149.227 127.469 109.137 1.00 108.69 ?  639  ARG   A NH1   1 
ATOM   5104  N  NH2   . ARG   A 1 639 ? 148.048 125.518 109.313 1.00 108.10 ?  639  ARG   A NH2   1 
ATOM   5105  N  N     . GLY   A 1 640 ? 153.308 130.137 104.028 1.00 107.47 ?  640  GLY   A N     1 
ATOM   5106  C  CA    . GLY   A 1 640 ? 153.712 131.047 102.980 1.00 107.54 ?  640  GLY   A CA    1 
ATOM   5107  C  C     . GLY   A 1 640 ? 154.850 131.933 103.445 1.00 106.25 ?  640  GLY   A C     1 
ATOM   5108  O  O     . GLY   A 1 640 ? 155.192 131.972 104.629 1.00 106.98 ?  640  GLY   A O     1 
ATOM   5109  N  N     . TYR   A 1 641 ? 155.438 132.646 102.481 1.00 103.95 ?  641  TYR   A N     1 
ATOM   5110  C  CA    . TYR   A 1 641 ? 156.531 133.557 102.803 1.00 102.77 ?  641  TYR   A CA    1 
ATOM   5111  C  C     . TYR   A 1 641 ? 156.062 134.700 103.691 1.00 103.98 ?  641  TYR   A C     1 
ATOM   5112  O  O     . TYR   A 1 641 ? 156.825 135.185 104.535 1.00 102.71 ?  641  TYR   A O     1 
ATOM   5113  C  CB    . TYR   A 1 641 ? 157.158 134.101 101.520 1.00 104.48 ?  641  TYR   A CB    1 
ATOM   5114  C  CG    . TYR   A 1 641 ? 158.099 133.132 100.846 1.00 105.46 ?  641  TYR   A CG    1 
ATOM   5115  C  CD1   . TYR   A 1 641 ? 159.273 132.731 101.466 1.00 104.62 ?  641  TYR   A CD1   1 
ATOM   5116  C  CD2   . TYR   A 1 641 ? 157.813 132.616 99.590  1.00 104.98 ?  641  TYR   A CD2   1 
ATOM   5117  C  CE1   . TYR   A 1 641 ? 160.136 131.843 100.855 1.00 103.46 ?  641  TYR   A CE1   1 
ATOM   5118  C  CE2   . TYR   A 1 641 ? 158.670 131.728 98.971  1.00 103.81 ?  641  TYR   A CE2   1 
ATOM   5119  C  CZ    . TYR   A 1 641 ? 159.830 131.345 99.608  1.00 104.49 ?  641  TYR   A CZ    1 
ATOM   5120  O  OH    . TYR   A 1 641 ? 160.688 130.461 98.995  1.00 107.02 ?  641  TYR   A OH    1 
ATOM   5121  N  N     . VAL   A 1 642 ? 154.820 135.145 103.516 1.00 108.46 ?  642  VAL   A N     1 
ATOM   5122  C  CA    . VAL   A 1 642 ? 154.231 136.190 104.342 1.00 107.55 ?  642  VAL   A CA    1 
ATOM   5123  C  C     . VAL   A 1 642 ? 152.911 135.679 104.905 1.00 109.23 ?  642  VAL   A C     1 
ATOM   5124  O  O     . VAL   A 1 642 ? 152.152 134.987 104.217 1.00 109.64 ?  642  VAL   A O     1 
ATOM   5125  C  CB    . VAL   A 1 642 ? 154.028 137.505 103.555 1.00 106.89 ?  642  VAL   A CB    1 
ATOM   5126  C  CG1   . VAL   A 1 642 ? 155.353 137.999 103.002 1.00 109.53 ?  642  VAL   A CG1   1 
ATOM   5127  C  CG2   . VAL   A 1 642 ? 153.023 137.321 102.430 1.00 107.93 ?  642  VAL   A CG2   1 
ATOM   5128  N  N     . SER   A 1 643 ? 152.657 135.994 106.170 1.00 116.26 ?  643  SER   A N     1 
ATOM   5129  C  CA    . SER   A 1 643 ? 151.415 135.648 106.844 1.00 115.54 ?  643  SER   A CA    1 
ATOM   5130  C  C     . SER   A 1 643 ? 150.606 136.917 107.061 1.00 117.70 ?  643  SER   A C     1 
ATOM   5131  O  O     . SER   A 1 643 ? 151.133 137.914 107.569 1.00 121.07 ?  643  SER   A O     1 
ATOM   5132  C  CB    . SER   A 1 643 ? 151.687 134.954 108.180 1.00 115.28 ?  643  SER   A CB    1 
ATOM   5133  O  OG    . SER   A 1 643 ? 152.298 135.842 109.100 1.00 117.56 ?  643  SER   A OG    1 
ATOM   5134  N  N     . ILE   A 1 644 ? 149.334 136.878 106.670 1.00 128.64 ?  644  ILE   A N     1 
ATOM   5135  C  CA    . ILE   A 1 644 ? 148.446 138.031 106.751 1.00 129.87 ?  644  ILE   A CA    1 
ATOM   5136  C  C     . ILE   A 1 644 ? 147.265 137.670 107.645 1.00 131.02 ?  644  ILE   A C     1 
ATOM   5137  O  O     . ILE   A 1 644 ? 146.685 136.585 107.514 1.00 133.25 ?  644  ILE   A O     1 
ATOM   5138  C  CB    . ILE   A 1 644 ? 147.997 138.511 105.351 1.00 129.63 ?  644  ILE   A CB    1 
ATOM   5139  C  CG1   . ILE   A 1 644 ? 146.909 137.619 104.738 1.00 129.23 ?  644  ILE   A CG1   1 
ATOM   5140  C  CG2   . ILE   A 1 644 ? 149.197 138.582 104.409 1.00 127.71 ?  644  ILE   A CG2   1 
ATOM   5141  C  CD1   . ILE   A 1 644 ? 145.479 137.986 105.139 1.00 129.44 ?  644  ILE   A CD1   1 
ATOM   5142  N  N     . LYS   A 1 645 ? 146.949 138.559 108.586 1.00 133.99 ?  645  LYS   A N     1 
ATOM   5143  C  CA    . LYS   A 1 645 ? 145.811 138.400 109.480 1.00 133.62 ?  645  LYS   A CA    1 
ATOM   5144  C  C     . LYS   A 1 645 ? 145.102 139.738 109.622 1.00 134.48 ?  645  LYS   A C     1 
ATOM   5145  O  O     . LYS   A 1 645 ? 145.749 140.775 109.787 1.00 137.52 ?  645  LYS   A O     1 
ATOM   5146  C  CB    . LYS   A 1 645 ? 146.238 137.888 110.864 1.00 133.08 ?  645  LYS   A CB    1 
ATOM   5147  C  CG    . LYS   A 1 645 ? 147.133 136.658 110.841 1.00 133.68 ?  645  LYS   A CG    1 
ATOM   5148  C  CD    . LYS   A 1 645 ? 147.124 135.945 112.183 1.00 133.51 ?  645  LYS   A CD    1 
ATOM   5149  C  CE    . LYS   A 1 645 ? 147.416 134.462 112.019 1.00 133.94 ?  645  LYS   A CE    1 
ATOM   5150  N  NZ    . LYS   A 1 645 ? 148.876 134.182 111.947 1.00 133.26 ?  645  LYS   A NZ    1 
ATOM   5151  N  N     . ALA   A 1 646 ? 143.774 139.709 109.567 1.00 135.69 ?  646  ALA   A N     1 
ATOM   5152  C  CA    . ALA   A 1 646 ? 142.985 140.928 109.655 1.00 136.06 ?  646  ALA   A CA    1 
ATOM   5153  C  C     . ALA   A 1 646 ? 142.858 141.394 111.101 1.00 137.76 ?  646  ALA   A C     1 
ATOM   5154  O  O     . ALA   A 1 646 ? 142.923 140.598 112.042 1.00 138.29 ?  646  ALA   A O     1 
ATOM   5155  C  CB    . ALA   A 1 646 ? 141.596 140.711 109.053 1.00 135.94 ?  646  ALA   A CB    1 
ATOM   5156  N  N     . SER   A 1 647 ? 142.674 142.702 111.268 1.00 154.24 ?  647  SER   A N     1 
ATOM   5157  C  CA    . SER   A 1 647 ? 142.486 143.299 112.583 1.00 155.90 ?  647  SER   A CA    1 
ATOM   5158  C  C     . SER   A 1 647 ? 141.641 144.558 112.433 1.00 155.97 ?  647  SER   A C     1 
ATOM   5159  O  O     . SER   A 1 647 ? 141.222 144.923 111.330 1.00 154.63 ?  647  SER   A O     1 
ATOM   5160  C  CB    . SER   A 1 647 ? 143.829 143.607 113.251 1.00 154.98 ?  647  SER   A CB    1 
ATOM   5161  O  OG    . SER   A 1 647 ? 143.663 143.866 114.634 1.00 154.90 ?  647  SER   A OG    1 
ATOM   5162  N  N     . LYS   A 1 648 ? 141.384 145.221 113.563 1.00 161.30 ?  648  LYS   A N     1 
ATOM   5163  C  CA    . LYS   A 1 648 ? 140.570 146.433 113.546 1.00 160.97 ?  648  LYS   A CA    1 
ATOM   5164  C  C     . LYS   A 1 648 ? 141.280 147.568 112.818 1.00 161.54 ?  648  LYS   A C     1 
ATOM   5165  O  O     . LYS   A 1 648 ? 140.703 148.207 111.931 1.00 161.42 ?  648  LYS   A O     1 
ATOM   5166  C  CB    . LYS   A 1 648 ? 140.218 146.847 114.975 1.00 160.06 ?  648  LYS   A CB    1 
ATOM   5167  C  CG    . LYS   A 1 648 ? 139.822 145.692 115.879 1.00 161.27 ?  648  LYS   A CG    1 
ATOM   5168  C  CD    . LYS   A 1 648 ? 139.662 146.152 117.318 1.00 161.90 ?  648  LYS   A CD    1 
ATOM   5169  C  CE    . LYS   A 1 648 ? 139.358 144.985 118.242 1.00 161.05 ?  648  LYS   A CE    1 
ATOM   5170  N  NZ    . LYS   A 1 648 ? 139.202 145.425 119.655 1.00 159.65 ?  648  LYS   A NZ    1 
ATOM   5171  N  N     . ASP   A 1 649 ? 142.536 147.837 113.186 1.00 166.27 ?  649  ASP   A N     1 
ATOM   5172  C  CA    . ASP   A 1 649 ? 143.294 148.890 112.516 1.00 166.61 ?  649  ASP   A CA    1 
ATOM   5173  C  C     . ASP   A 1 649 ? 143.526 148.547 111.053 1.00 165.06 ?  649  ASP   A C     1 
ATOM   5174  O  O     . ASP   A 1 649 ? 143.427 149.414 110.176 1.00 165.63 ?  649  ASP   A O     1 
ATOM   5175  C  CB    . ASP   A 1 649 ? 144.629 149.112 113.228 1.00 165.63 ?  649  ASP   A CB    1 
ATOM   5176  C  CG    . ASP   A 1 649 ? 145.453 150.212 112.593 1.00 165.50 ?  649  ASP   A CG    1 
ATOM   5177  O  OD1   . ASP   A 1 649 ? 145.013 151.381 112.626 1.00 165.58 ?  649  ASP   A OD1   1 
ATOM   5178  O  OD2   . ASP   A 1 649 ? 146.543 149.909 112.063 1.00 164.77 ?  649  ASP   A OD2   1 
ATOM   5179  N  N     . GLY   A 1 650 ? 143.834 147.290 110.775 1.00 144.57 ?  650  GLY   A N     1 
ATOM   5180  C  CA    . GLY   A 1 650 ? 144.089 146.844 109.423 1.00 142.79 ?  650  GLY   A CA    1 
ATOM   5181  C  C     . GLY   A 1 650 ? 144.657 145.449 109.463 1.00 144.93 ?  650  GLY   A C     1 
ATOM   5182  O  O     . GLY   A 1 650 ? 144.969 144.904 110.526 1.00 146.39 ?  650  GLY   A O     1 
ATOM   5183  N  N     . ILE   A 1 651 ? 144.783 144.865 108.275 1.00 136.47 ?  651  ILE   A N     1 
ATOM   5184  C  CA    . ILE   A 1 651 ? 145.304 143.511 108.197 1.00 136.11 ?  651  ILE   A CA    1 
ATOM   5185  C  C     . ILE   A 1 651 ? 146.789 143.524 108.554 1.00 135.00 ?  651  ILE   A C     1 
ATOM   5186  O  O     . ILE   A 1 651 ? 147.504 144.504 108.305 1.00 134.20 ?  651  ILE   A O     1 
ATOM   5187  C  CB    . ILE   A 1 651 ? 145.037 142.909 106.804 1.00 133.29 ?  651  ILE   A CB    1 
ATOM   5188  C  CG1   . ILE   A 1 651 ? 145.952 143.518 105.747 1.00 131.04 ?  651  ILE   A CG1   1 
ATOM   5189  C  CG2   . ILE   A 1 651 ? 143.583 143.122 106.401 1.00 132.99 ?  651  ILE   A CG2   1 
ATOM   5190  C  CD1   . ILE   A 1 651 ? 147.216 142.746 105.564 1.00 131.77 ?  651  ILE   A CD1   1 
ATOM   5191  N  N     . LEU   A 1 652 ? 147.257 142.435 109.153 1.00 132.26 ?  652  LEU   A N     1 
ATOM   5192  C  CA    . LEU   A 1 652 ? 148.655 142.313 109.539 1.00 129.68 ?  652  LEU   A CA    1 
ATOM   5193  C  C     . LEU   A 1 652 ? 149.472 141.686 108.412 1.00 128.49 ?  652  LEU   A C     1 
ATOM   5194  O  O     . LEU   A 1 652 ? 148.939 141.051 107.502 1.00 131.34 ?  652  LEU   A O     1 
ATOM   5195  C  CB    . LEU   A 1 652 ? 148.798 141.473 110.810 1.00 130.02 ?  652  LEU   A CB    1 
ATOM   5196  C  CG    . LEU   A 1 652 ? 148.526 142.129 112.166 1.00 129.96 ?  652  LEU   A CG    1 
ATOM   5197  C  CD1   . LEU   A 1 652 ? 149.249 143.459 112.281 1.00 129.15 ?  652  LEU   A CD1   1 
ATOM   5198  C  CD2   . LEU   A 1 652 ? 147.035 142.301 112.408 1.00 129.58 ?  652  LEU   A CD2   1 
ATOM   5199  N  N     . ARG   A 1 653 ? 150.787 141.876 108.484 1.00 118.22 ?  653  ARG   A N     1 
ATOM   5200  C  CA    . ARG   A 1 653 ? 151.704 141.236 107.545 1.00 120.63 ?  653  ARG   A CA    1 
ATOM   5201  C  C     . ARG   A 1 653 ? 152.993 140.917 108.284 1.00 121.61 ?  653  ARG   A C     1 
ATOM   5202  O  O     . ARG   A 1 653 ? 153.629 141.820 108.837 1.00 121.97 ?  653  ARG   A O     1 
ATOM   5203  C  CB    . ARG   A 1 653 ? 151.989 142.133 106.335 1.00 122.66 ?  653  ARG   A CB    1 
ATOM   5204  C  CG    . ARG   A 1 653 ? 150.796 142.402 105.422 1.00 122.08 ?  653  ARG   A CG    1 
ATOM   5205  C  CD    . ARG   A 1 653 ? 151.219 143.244 104.214 1.00 121.08 ?  653  ARG   A CD    1 
ATOM   5206  N  NE    . ARG   A 1 653 ? 150.130 143.569 103.296 1.00 122.11 ?  653  ARG   A NE    1 
ATOM   5207  C  CZ    . ARG   A 1 653 ? 149.684 142.766 102.339 1.00 123.43 ?  653  ARG   A CZ    1 
ATOM   5208  N  NH1   . ARG   A 1 653 ? 150.157 141.539 102.189 1.00 121.31 ?  653  ARG   A NH1   1 
ATOM   5209  N  NH2   . ARG   A 1 653 ? 148.715 143.192 101.533 1.00 123.69 ?  653  ARG   A NH2   1 
ATOM   5210  N  N     . GLN   A 1 654 ? 153.377 139.643 108.296 1.00 109.85 ?  654  GLN   A N     1 
ATOM   5211  C  CA    . GLN   A 1 654 ? 154.627 139.217 108.912 1.00 104.91 ?  654  GLN   A CA    1 
ATOM   5212  C  C     . GLN   A 1 654 ? 155.407 138.358 107.930 1.00 105.51 ?  654  GLN   A C     1 
ATOM   5213  O  O     . GLN   A 1 654 ? 154.865 137.400 107.373 1.00 109.83 ?  654  GLN   A O     1 
ATOM   5214  C  CB    . GLN   A 1 654 ? 154.380 138.442 110.209 1.00 106.29 ?  654  GLN   A CB    1 
ATOM   5215  C  CG    . GLN   A 1 654 ? 155.617 137.731 110.736 1.00 110.25 ?  654  GLN   A CG    1 
ATOM   5216  C  CD    . GLN   A 1 654 ? 155.658 137.671 112.245 1.00 112.20 ?  654  GLN   A CD    1 
ATOM   5217  O  OE1   . GLN   A 1 654 ? 156.556 138.225 112.878 1.00 111.11 ?  654  GLN   A OE1   1 
ATOM   5218  N  NE2   . GLN   A 1 654 ? 154.685 136.995 112.831 1.00 110.87 ?  654  GLN   A NE2   1 
ATOM   5219  N  N     . VAL   A 1 655 ? 156.675 138.695 107.728 1.00 104.19 ?  655  VAL   A N     1 
ATOM   5220  C  CA    . VAL   A 1 655 ? 157.539 137.962 106.821 1.00 107.22 ?  655  VAL   A CA    1 
ATOM   5221  C  C     . VAL   A 1 655 ? 158.437 137.043 107.640 1.00 106.83 ?  655  VAL   A C     1 
ATOM   5222  O  O     . VAL   A 1 655 ? 158.652 137.243 108.838 1.00 107.64 ?  655  VAL   A O     1 
ATOM   5223  C  CB    . VAL   A 1 655 ? 158.370 138.917 105.931 1.00 107.86 ?  655  VAL   A CB    1 
ATOM   5224  C  CG1   . VAL   A 1 655 ? 158.884 138.197 104.692 1.00 107.72 ?  655  VAL   A CG1   1 
ATOM   5225  C  CG2   . VAL   A 1 655 ? 157.539 140.128 105.540 1.00 107.85 ?  655  VAL   A CG2   1 
ATOM   5226  N  N     . VAL   A 1 656 ? 158.968 136.016 106.983 1.00 106.55 ?  656  VAL   A N     1 
ATOM   5227  C  CA    . VAL   A 1 656 ? 159.861 135.052 107.621 1.00 105.67 ?  656  VAL   A CA    1 
ATOM   5228  C  C     . VAL   A 1 656 ? 161.125 135.783 108.064 1.00 107.62 ?  656  VAL   A C     1 
ATOM   5229  O  O     . VAL   A 1 656 ? 161.473 136.818 107.478 1.00 112.31 ?  656  VAL   A O     1 
ATOM   5230  C  CB    . VAL   A 1 656 ? 160.176 133.877 106.680 1.00 106.81 ?  656  VAL   A CB    1 
ATOM   5231  C  CG1   . VAL   A 1 656 ? 158.915 133.073 106.400 1.00 106.09 ?  656  VAL   A CG1   1 
ATOM   5232  C  CG2   . VAL   A 1 656 ? 160.786 134.377 105.387 1.00 107.15 ?  656  VAL   A CG2   1 
ATOM   5233  N  N     . PRO   A 1 657 ? 161.827 135.295 109.094 1.00 110.09 ?  657  PRO   A N     1 
ATOM   5234  C  CA    . PRO   A 1 657 ? 162.904 136.103 109.697 1.00 115.16 ?  657  PRO   A CA    1 
ATOM   5235  C  C     . PRO   A 1 657 ? 163.991 136.552 108.731 1.00 114.30 ?  657  PRO   A C     1 
ATOM   5236  O  O     . PRO   A 1 657 ? 164.497 137.673 108.868 1.00 116.46 ?  657  PRO   A O     1 
ATOM   5237  C  CB    . PRO   A 1 657 ? 163.467 135.169 110.776 1.00 111.83 ?  657  PRO   A CB    1 
ATOM   5238  C  CG    . PRO   A 1 657 ? 162.334 134.287 111.139 1.00 110.75 ?  657  PRO   A CG    1 
ATOM   5239  C  CD    . PRO   A 1 657 ? 161.508 134.103 109.900 1.00 108.66 ?  657  PRO   A CD    1 
ATOM   5240  N  N     . ASP   A 1 658 ? 164.370 135.725 107.762 1.00 104.27 ?  658  ASP   A N     1 
ATOM   5241  C  CA    . ASP   A 1 658 ? 165.511 136.017 106.897 1.00 104.72 ?  658  ASP   A CA    1 
ATOM   5242  C  C     . ASP   A 1 658 ? 165.151 135.799 105.433 1.00 107.23 ?  658  ASP   A C     1 
ATOM   5243  O  O     . ASP   A 1 658 ? 165.856 135.115 104.688 1.00 108.99 ?  658  ASP   A O     1 
ATOM   5244  C  CB    . ASP   A 1 658 ? 166.721 135.175 107.288 1.00 107.51 ?  658  ASP   A CB    1 
ATOM   5245  C  CG    . ASP   A 1 658 ? 168.027 135.928 107.131 1.00 109.77 ?  658  ASP   A CG    1 
ATOM   5246  O  OD1   . ASP   A 1 658 ? 167.996 137.177 107.118 1.00 111.54 ?  658  ASP   A OD1   1 
ATOM   5247  O  OD2   . ASP   A 1 658 ? 169.085 135.274 107.021 1.00 109.85 ?  658  ASP   A OD2   1 
ATOM   5248  N  N     . TYR   A 1 659 ? 164.029 136.384 105.005 1.00 115.53 ?  659  TYR   A N     1 
ATOM   5249  C  CA    . TYR   A 1 659 ? 163.588 136.226 103.622 1.00 117.18 ?  659  TYR   A CA    1 
ATOM   5250  C  C     . TYR   A 1 659 ? 164.619 136.750 102.631 1.00 118.34 ?  659  TYR   A C     1 
ATOM   5251  O  O     . TYR   A 1 659 ? 164.729 136.224 101.518 1.00 119.06 ?  659  TYR   A O     1 
ATOM   5252  C  CB    . TYR   A 1 659 ? 162.252 136.941 103.414 1.00 115.49 ?  659  TYR   A CB    1 
ATOM   5253  C  CG    . TYR   A 1 659 ? 161.774 136.945 101.980 1.00 118.65 ?  659  TYR   A CG    1 
ATOM   5254  C  CD1   . TYR   A 1 659 ? 161.451 135.761 101.333 1.00 119.18 ?  659  TYR   A CD1   1 
ATOM   5255  C  CD2   . TYR   A 1 659 ? 161.645 138.133 101.273 1.00 119.20 ?  659  TYR   A CD2   1 
ATOM   5256  C  CE1   . TYR   A 1 659 ? 161.015 135.759 100.023 1.00 119.54 ?  659  TYR   A CE1   1 
ATOM   5257  C  CE2   . TYR   A 1 659 ? 161.211 138.138 99.962  1.00 119.03 ?  659  TYR   A CE2   1 
ATOM   5258  C  CZ    . TYR   A 1 659 ? 160.896 136.950 99.342  1.00 119.58 ?  659  TYR   A CZ    1 
ATOM   5259  O  OH    . TYR   A 1 659 ? 160.462 136.952 98.037  1.00 120.24 ?  659  TYR   A OH    1 
ATOM   5260  N  N     . GLU   A 1 660 ? 165.378 137.781 103.011 1.00 123.03 ?  660  GLU   A N     1 
ATOM   5261  C  CA    . GLU   A 1 660 ? 166.324 138.391 102.081 1.00 123.00 ?  660  GLU   A CA    1 
ATOM   5262  C  C     . GLU   A 1 660 ? 167.409 137.407 101.661 1.00 122.42 ?  660  GLU   A C     1 
ATOM   5263  O  O     . GLU   A 1 660 ? 167.724 137.282 100.472 1.00 122.13 ?  660  GLU   A O     1 
ATOM   5264  C  CB    . GLU   A 1 660 ? 166.946 139.637 102.712 1.00 122.62 ?  660  GLU   A CB    1 
ATOM   5265  C  CG    . GLU   A 1 660 ? 167.045 140.825 101.771 1.00 123.25 ?  660  GLU   A CG    1 
ATOM   5266  C  CD    . GLU   A 1 660 ? 165.690 141.295 101.283 1.00 125.31 ?  660  GLU   A CD    1 
ATOM   5267  O  OE1   . GLU   A 1 660 ? 165.363 141.045 100.104 1.00 123.75 ?  660  GLU   A OE1   1 
ATOM   5268  O  OE2   . GLU   A 1 660 ? 164.953 141.916 102.077 1.00 126.46 ?  660  GLU   A OE2   1 
ATOM   5269  N  N     . HIS   A 1 661 ? 167.976 136.674 102.617 1.00 115.27 ?  661  HIS   A N     1 
ATOM   5270  C  CA    . HIS   A 1 661 ? 169.119 135.800 102.242 1.00 114.75 ?  661  HIS   A CA    1 
ATOM   5271  C  C     . HIS   A 1 661 ? 168.718 134.323 102.210 1.00 115.39 ?  661  HIS   A C     1 
ATOM   5272  O  O     . HIS   A 1 661 ? 169.582 133.497 101.880 1.00 114.59 ?  661  HIS   A O     1 
ATOM   5273  C  CB    . HIS   A 1 661 ? 170.298 136.032 103.191 1.00 112.33 ?  661  HIS   A CB    1 
ATOM   5274  C  CG    . HIS   A 1 661 ? 170.653 137.466 103.392 1.00 115.55 ?  661  HIS   A CG    1 
ATOM   5275  N  ND1   . HIS   A 1 661 ? 171.643 137.859 104.269 1.00 117.30 ?  661  HIS   A ND1   1 
ATOM   5276  C  CD2   . HIS   A 1 661 ? 170.167 138.597 102.839 1.00 115.96 ?  661  HIS   A CD2   1 
ATOM   5277  C  CE1   . HIS   A 1 661 ? 171.750 139.171 104.250 1.00 115.35 ?  661  HIS   A CE1   1 
ATOM   5278  N  NE2   . HIS   A 1 661 ? 170.854 139.647 103.380 1.00 116.24 ?  661  HIS   A NE2   1 
ATOM   5279  N  N     . LEU   A 1 662 ? 167.475 133.999 102.564 1.00 104.76 ?  662  LEU   A N     1 
ATOM   5280  C  CA    . LEU   A 1 662 ? 167.072 132.599 102.620 1.00 103.65 ?  662  LEU   A CA    1 
ATOM   5281  C  C     . LEU   A 1 662 ? 165.750 132.359 101.902 1.00 105.48 ?  662  LEU   A C     1 
ATOM   5282  O  O     . LEU   A 1 662 ? 165.016 131.427 102.248 1.00 110.46 ?  662  LEU   A O     1 
ATOM   5283  C  CB    . LEU   A 1 662 ? 166.962 132.114 104.068 1.00 103.28 ?  662  LEU   A CB    1 
ATOM   5284  C  CG    . LEU   A 1 662 ? 168.230 132.137 104.923 1.00 100.97 ?  662  LEU   A CG    1 
ATOM   5285  C  CD1   . LEU   A 1 662 ? 167.899 131.816 106.369 1.00 99.22  ?  662  LEU   A CD1   1 
ATOM   5286  C  CD2   . LEU   A 1 662 ? 169.263 131.165 104.378 1.00 102.52 ?  662  LEU   A CD2   1 
ATOM   5287  N  N     . HIS   A 1 663 ? 165.428 133.181 100.899 1.00 114.49 ?  663  HIS   A N     1 
ATOM   5288  C  CA    . HIS   A 1 663 ? 164.166 133.004 100.187 1.00 115.54 ?  663  HIS   A CA    1 
ATOM   5289  C  C     . HIS   A 1 663 ? 164.110 131.662 99.468  1.00 117.03 ?  663  HIS   A C     1 
ATOM   5290  O  O     . HIS   A 1 663 ? 163.039 131.051 99.379  1.00 118.10 ?  663  HIS   A O     1 
ATOM   5291  C  CB    . HIS   A 1 663 ? 163.947 134.155 99.202  1.00 112.58 ?  663  HIS   A CB    1 
ATOM   5292  C  CG    . HIS   A 1 663 ? 165.015 134.279 98.160  1.00 116.52 ?  663  HIS   A CG    1 
ATOM   5293  N  ND1   . HIS   A 1 663 ? 166.265 134.789 98.431  1.00 115.96 ?  663  HIS   A ND1   1 
ATOM   5294  C  CD2   . HIS   A 1 663 ? 165.012 133.973 96.840  1.00 118.01 ?  663  HIS   A CD2   1 
ATOM   5295  C  CE1   . HIS   A 1 663 ? 166.990 134.784 97.327  1.00 116.62 ?  663  HIS   A CE1   1 
ATOM   5296  N  NE2   . HIS   A 1 663 ? 166.254 134.293 96.348  1.00 117.65 ?  663  HIS   A NE2   1 
ATOM   5297  N  N     . ASP   A 1 664 ? 165.244 131.187 98.957  1.00 113.40 ?  664  ASP   A N     1 
ATOM   5298  C  CA    . ASP   A 1 664 ? 165.304 129.902 98.276  1.00 112.83 ?  664  ASP   A CA    1 
ATOM   5299  C  C     . ASP   A 1 664 ? 165.582 128.739 99.218  1.00 113.88 ?  664  ASP   A C     1 
ATOM   5300  O  O     . ASP   A 1 664 ? 165.524 127.584 98.783  1.00 113.04 ?  664  ASP   A O     1 
ATOM   5301  C  CB    . ASP   A 1 664 ? 166.373 129.936 97.179  1.00 114.21 ?  664  ASP   A CB    1 
ATOM   5302  C  CG    . ASP   A 1 664 ? 167.761 130.205 97.726  1.00 116.50 ?  664  ASP   A CG    1 
ATOM   5303  O  OD1   . ASP   A 1 664 ? 167.883 130.441 98.947  1.00 115.98 ?  664  ASP   A OD1   1 
ATOM   5304  O  OD2   . ASP   A 1 664 ? 168.729 130.182 96.937  1.00 115.68 ?  664  ASP   A OD2   1 
ATOM   5305  N  N     . ALA   A 1 665 ? 165.883 129.011 100.487 1.00 107.56 ?  665  ALA   A N     1 
ATOM   5306  C  CA    . ALA   A 1 665 ? 166.114 127.954 101.462 1.00 102.83 ?  665  ALA   A CA    1 
ATOM   5307  C  C     . ALA   A 1 665 ? 164.864 127.592 102.249 1.00 104.72 ?  665  ALA   A C     1 
ATOM   5308  O  O     . ALA   A 1 665 ? 164.813 126.507 102.840 1.00 105.89 ?  665  ALA   A O     1 
ATOM   5309  C  CB    . ALA   A 1 665 ? 167.225 128.363 102.433 1.00 99.75  ?  665  ALA   A CB    1 
ATOM   5310  N  N     . TYR   A 1 666 ? 163.862 128.467 102.268 1.00 104.87 ?  666  TYR   A N     1 
ATOM   5311  C  CA    . TYR   A 1 666 ? 162.615 128.203 102.976 1.00 101.57 ?  666  TYR   A CA    1 
ATOM   5312  C  C     . TYR   A 1 666 ? 161.754 127.277 102.129 1.00 104.16 ?  666  TYR   A C     1 
ATOM   5313  O  O     . TYR   A 1 666 ? 161.200 127.696 101.108 1.00 108.81 ?  666  TYR   A O     1 
ATOM   5314  C  CB    . TYR   A 1 666 ? 161.876 129.506 103.263 1.00 101.55 ?  666  TYR   A CB    1 
ATOM   5315  C  CG    . TYR   A 1 666 ? 162.231 130.156 104.578 1.00 102.20 ?  666  TYR   A CG    1 
ATOM   5316  C  CD1   . TYR   A 1 666 ? 161.683 129.704 105.770 1.00 102.86 ?  666  TYR   A CD1   1 
ATOM   5317  C  CD2   . TYR   A 1 666 ? 163.102 131.233 104.626 1.00 101.55 ?  666  TYR   A CD2   1 
ATOM   5318  C  CE1   . TYR   A 1 666 ? 162.003 130.302 106.972 1.00 104.39 ?  666  TYR   A CE1   1 
ATOM   5319  C  CE2   . TYR   A 1 666 ? 163.427 131.835 105.821 1.00 102.33 ?  666  TYR   A CE2   1 
ATOM   5320  C  CZ    . TYR   A 1 666 ? 162.876 131.367 106.990 1.00 105.53 ?  666  TYR   A CZ    1 
ATOM   5321  O  OH    . TYR   A 1 666 ? 163.200 131.969 108.181 1.00 110.57 ?  666  TYR   A OH    1 
ATOM   5322  N  N     . GLU   A 1 667 ? 161.633 126.022 102.545 1.00 104.39 ?  667  GLU   A N     1 
ATOM   5323  C  CA    . GLU   A 1 667 ? 160.734 125.084 101.884 1.00 103.17 ?  667  GLU   A CA    1 
ATOM   5324  C  C     . GLU   A 1 667 ? 159.344 125.264 102.482 1.00 103.98 ?  667  GLU   A C     1 
ATOM   5325  O  O     . GLU   A 1 667 ? 159.104 124.893 103.635 1.00 108.95 ?  667  GLU   A O     1 
ATOM   5326  C  CB    . GLU   A 1 667 ? 161.227 123.650 102.043 1.00 103.33 ?  667  GLU   A CB    1 
ATOM   5327  C  CG    . GLU   A 1 667 ? 160.205 122.601 101.639 1.00 109.47 ?  667  GLU   A CG    1 
ATOM   5328  C  CD    . GLU   A 1 667 ? 160.838 121.258 101.342 1.00 112.79 ?  667  GLU   A CD    1 
ATOM   5329  O  OE1   . GLU   A 1 667 ? 162.072 121.142 101.478 1.00 112.55 ?  667  GLU   A OE1   1 
ATOM   5330  O  OE2   . GLU   A 1 667 ? 160.106 120.319 100.968 1.00 111.21 ?  667  GLU   A OE2   1 
ATOM   5331  N  N     . LEU   A 1 668 ? 158.432 125.840 101.704 1.00 96.85  ?  668  LEU   A N     1 
ATOM   5332  C  CA    . LEU   A 1 668 ? 157.094 126.106 102.203 1.00 99.37  ?  668  LEU   A CA    1 
ATOM   5333  C  C     . LEU   A 1 668 ? 156.334 124.797 102.413 1.00 101.00 ?  668  LEU   A C     1 
ATOM   5334  O  O     . LEU   A 1 668 ? 156.763 123.717 101.998 1.00 100.47 ?  668  LEU   A O     1 
ATOM   5335  C  CB    . LEU   A 1 668 ? 156.335 127.024 101.245 1.00 98.32  ?  668  LEU   A CB    1 
ATOM   5336  C  CG    . LEU   A 1 668 ? 156.915 128.426 101.052 1.00 96.81  ?  668  LEU   A CG    1 
ATOM   5337  C  CD1   . LEU   A 1 668 ? 155.994 129.272 100.188 1.00 98.10  ?  668  LEU   A CD1   1 
ATOM   5338  C  CD2   . LEU   A 1 668 ? 157.160 129.095 102.394 1.00 94.80  ?  668  LEU   A CD2   1 
ATOM   5339  N  N     . LEU   A 1 669 ? 155.186 124.910 103.083 1.00 98.02  ?  669  LEU   A N     1 
ATOM   5340  C  CA    . LEU   A 1 669 ? 154.437 123.723 103.481 1.00 96.53  ?  669  LEU   A CA    1 
ATOM   5341  C  C     . LEU   A 1 669 ? 153.948 122.933 102.273 1.00 97.44  ?  669  LEU   A C     1 
ATOM   5342  O  O     . LEU   A 1 669 ? 154.026 121.699 102.258 1.00 100.53 ?  669  LEU   A O     1 
ATOM   5343  C  CB    . LEU   A 1 669 ? 153.262 124.125 104.371 1.00 97.94  ?  669  LEU   A CB    1 
ATOM   5344  C  CG    . LEU   A 1 669 ? 152.299 123.007 104.764 1.00 97.44  ?  669  LEU   A CG    1 
ATOM   5345  C  CD1   . LEU   A 1 669 ? 152.805 122.293 106.002 1.00 98.45  ?  669  LEU   A CD1   1 
ATOM   5346  C  CD2   . LEU   A 1 669 ? 150.904 123.561 104.993 1.00 97.01  ?  669  LEU   A CD2   1 
ATOM   5347  N  N     . TRP   A 1 670 ? 153.445 123.620 101.252 1.00 94.44  ?  670  TRP   A N     1 
ATOM   5348  C  CA    . TRP   A 1 670 ? 152.805 122.957 100.123 1.00 94.55  ?  670  TRP   A CA    1 
ATOM   5349  C  C     . TRP   A 1 670 ? 153.771 122.588 99.005  1.00 97.45  ?  670  TRP   A C     1 
ATOM   5350  O  O     . TRP   A 1 670 ? 153.354 121.938 98.041  1.00 100.21 ?  670  TRP   A O     1 
ATOM   5351  C  CB    . TRP   A 1 670 ? 151.681 123.836 99.572  1.00 94.05  ?  670  TRP   A CB    1 
ATOM   5352  C  CG    . TRP   A 1 670 ? 150.596 124.082 100.573 1.00 94.82  ?  670  TRP   A CG    1 
ATOM   5353  C  CD1   . TRP   A 1 670 ? 150.161 125.290 101.029 1.00 96.52  ?  670  TRP   A CD1   1 
ATOM   5354  C  CD2   . TRP   A 1 670 ? 149.813 123.091 101.250 1.00 94.60  ?  670  TRP   A CD2   1 
ATOM   5355  N  NE1   . TRP   A 1 670 ? 149.152 125.115 101.944 1.00 94.52  ?  670  TRP   A NE1   1 
ATOM   5356  C  CE2   . TRP   A 1 670 ? 148.920 123.774 102.097 1.00 95.38  ?  670  TRP   A CE2   1 
ATOM   5357  C  CE3   . TRP   A 1 670 ? 149.777 121.694 101.220 1.00 92.87  ?  670  TRP   A CE3   1 
ATOM   5358  C  CZ2   . TRP   A 1 670 ? 148.004 123.109 102.905 1.00 94.75  ?  670  TRP   A CZ2   1 
ATOM   5359  C  CZ3   . TRP   A 1 670 ? 148.868 121.036 102.025 1.00 91.65  ?  670  TRP   A CZ3   1 
ATOM   5360  C  CH2   . TRP   A 1 670 ? 147.995 121.744 102.856 1.00 94.60  ?  670  TRP   A CH2   1 
ATOM   5361  N  N     . GLU   A 1 671 ? 155.041 122.978 99.103  1.00 103.00 ?  671  GLU   A N     1 
ATOM   5362  C  CA    . GLU   A 1 671 ? 156.037 122.508 98.150  1.00 103.67 ?  671  GLU   A CA    1 
ATOM   5363  C  C     . GLU   A 1 671 ? 156.552 121.115 98.483  1.00 107.25 ?  671  GLU   A C     1 
ATOM   5364  O  O     . GLU   A 1 671 ? 157.247 120.515 97.656  1.00 110.46 ?  671  GLU   A O     1 
ATOM   5365  C  CB    . GLU   A 1 671 ? 157.211 123.485 98.083  1.00 102.81 ?  671  GLU   A CB    1 
ATOM   5366  C  CG    . GLU   A 1 671 ? 156.864 124.893 98.512  1.00 106.27 ?  671  GLU   A CG    1 
ATOM   5367  C  CD    . GLU   A 1 671 ? 158.019 125.859 98.337  1.00 111.31 ?  671  GLU   A CD    1 
ATOM   5368  O  OE1   . GLU   A 1 671 ? 159.077 125.642 98.965  1.00 112.15 ?  671  GLU   A OE1   1 
ATOM   5369  O  OE2   . GLU   A 1 671 ? 157.868 126.835 97.573  1.00 109.86 ?  671  GLU   A OE2   1 
ATOM   5370  N  N     . MET   A 1 672 ? 156.234 120.598 99.662  1.00 102.98 ?  672  MET   A N     1 
ATOM   5371  C  CA    . MET   A 1 672 ? 156.661 119.256 100.033 1.00 105.15 ?  672  MET   A CA    1 
ATOM   5372  C  C     . MET   A 1 672 ? 155.959 118.228 99.154  1.00 108.19 ?  672  MET   A C     1 
ATOM   5373  O  O     . MET   A 1 672 ? 154.742 118.322 98.952  1.00 108.13 ?  672  MET   A O     1 
ATOM   5374  C  CB    . MET   A 1 672 ? 156.354 118.992 101.506 1.00 104.39 ?  672  MET   A CB    1 
ATOM   5375  C  CG    . MET   A 1 672 ? 157.482 119.362 102.454 1.00 104.51 ?  672  MET   A CG    1 
ATOM   5376  S  SD    . MET   A 1 672 ? 156.896 119.943 104.057 1.00 110.85 ?  672  MET   A SD    1 
ATOM   5377  C  CE    . MET   A 1 672 ? 155.401 118.974 104.244 1.00 106.27 ?  672  MET   A CE    1 
ATOM   5378  N  N     . PRO   A 1 673 ? 156.681 117.249 98.602  1.00 106.55 ?  673  PRO   A N     1 
ATOM   5379  C  CA    . PRO   A 1 673 ? 156.004 116.200 97.820  1.00 104.67 ?  673  PRO   A CA    1 
ATOM   5380  C  C     . PRO   A 1 673 ? 154.972 115.439 98.630  1.00 105.00 ?  673  PRO   A C     1 
ATOM   5381  O  O     . PRO   A 1 673 ? 153.931 115.040 98.092  1.00 108.34 ?  673  PRO   A O     1 
ATOM   5382  C  CB    . PRO   A 1 673 ? 157.156 115.287 97.372  1.00 105.00 ?  673  PRO   A CB    1 
ATOM   5383  C  CG    . PRO   A 1 673 ? 158.409 116.066 97.598  1.00 107.51 ?  673  PRO   A CG    1 
ATOM   5384  C  CD    . PRO   A 1 673 ? 158.136 117.047 98.687  1.00 105.88 ?  673  PRO   A CD    1 
ATOM   5385  N  N     . GLY   A 1 674 ? 155.232 115.234 99.908  1.00 99.18  ?  674  GLY   A N     1 
ATOM   5386  C  CA    . GLY   A 1 674 ? 154.291 114.595 100.794 1.00 97.71  ?  674  GLY   A CA    1 
ATOM   5387  C  C     . GLY   A 1 674 ? 154.638 114.920 102.224 1.00 99.93  ?  674  GLY   A C     1 
ATOM   5388  O  O     . GLY   A 1 674 ? 155.269 115.937 102.514 1.00 103.65 ?  674  GLY   A O     1 
ATOM   5389  N  N     . ASN   A 1 675 ? 154.220 114.039 103.129 1.00 88.83  ?  675  ASN   A N     1 
ATOM   5390  C  CA    . ASN   A 1 675 ? 154.576 114.202 104.532 1.00 88.96  ?  675  ASN   A CA    1 
ATOM   5391  C  C     . ASN   A 1 675 ? 155.351 112.987 105.025 1.00 86.93  ?  675  ASN   A C     1 
ATOM   5392  O  O     . ASN   A 1 675 ? 155.070 112.459 106.105 1.00 91.84  ?  675  ASN   A O     1 
ATOM   5393  C  CB    . ASN   A 1 675 ? 153.329 114.442 105.387 1.00 88.27  ?  675  ASN   A CB    1 
ATOM   5394  C  CG    . ASN   A 1 675 ? 152.204 113.488 105.061 1.00 87.49  ?  675  ASN   A CG    1 
ATOM   5395  O  OD1   . ASN   A 1 675 ? 152.233 112.323 105.451 1.00 91.49  ?  675  ASN   A OD1   1 
ATOM   5396  N  ND2   . ASN   A 1 675 ? 151.199 113.980 104.348 1.00 86.60  ?  675  ASN   A ND2   1 
ATOM   5397  N  N     . ASP   A 1 676 ? 156.324 112.535 104.235 1.00 89.89  ?  676  ASP   A N     1 
ATOM   5398  C  CA    . ASP   A 1 676 ? 157.176 111.416 104.618 1.00 89.56  ?  676  ASP   A CA    1 
ATOM   5399  C  C     . ASP   A 1 676 ? 158.451 111.886 105.310 1.00 89.30  ?  676  ASP   A C     1 
ATOM   5400  O  O     . ASP   A 1 676 ? 158.815 111.363 106.367 1.00 92.40  ?  676  ASP   A O     1 
ATOM   5401  C  CB    . ASP   A 1 676 ? 157.518 110.571 103.387 1.00 93.01  ?  676  ASP   A CB    1 
ATOM   5402  C  CG    . ASP   A 1 676 ? 158.763 109.729 103.585 1.00 97.32  ?  676  ASP   A CG    1 
ATOM   5403  O  OD1   . ASP   A 1 676 ? 158.810 108.952 104.562 1.00 99.40  ?  676  ASP   A OD1   1 
ATOM   5404  O  OD2   . ASP   A 1 676 ? 159.696 109.844 102.764 1.00 96.47  ?  676  ASP   A OD2   1 
ATOM   5405  N  N     . GLY   A 1 677 ? 159.144 112.864 104.723 1.00 80.98  ?  677  GLY   A N     1 
ATOM   5406  C  CA    . GLY   A 1 677 ? 160.327 113.408 105.370 1.00 81.02  ?  677  GLY   A CA    1 
ATOM   5407  C  C     . GLY   A 1 677 ? 159.998 114.153 106.649 1.00 86.60  ?  677  GLY   A C     1 
ATOM   5408  O  O     . GLY   A 1 677 ? 160.752 114.095 107.626 1.00 88.60  ?  677  GLY   A O     1 
ATOM   5409  N  N     . TYR   A 1 678 ? 158.870 114.867 106.659 1.00 84.24  ?  678  TYR   A N     1 
ATOM   5410  C  CA    . TYR   A 1 678 ? 158.437 115.559 107.868 1.00 79.73  ?  678  TYR   A CA    1 
ATOM   5411  C  C     . TYR   A 1 678 ? 158.151 114.572 108.992 1.00 81.24  ?  678  TYR   A C     1 
ATOM   5412  O  O     . TYR   A 1 678 ? 158.498 114.823 110.152 1.00 85.85  ?  678  TYR   A O     1 
ATOM   5413  C  CB    . TYR   A 1 678 ? 157.204 116.409 107.565 1.00 76.29  ?  678  TYR   A CB    1 
ATOM   5414  C  CG    . TYR   A 1 678 ? 156.587 117.065 108.777 1.00 80.79  ?  678  TYR   A CG    1 
ATOM   5415  C  CD1   . TYR   A 1 678 ? 157.139 118.212 109.327 1.00 80.75  ?  678  TYR   A CD1   1 
ATOM   5416  C  CD2   . TYR   A 1 678 ? 155.448 116.539 109.366 1.00 81.18  ?  678  TYR   A CD2   1 
ATOM   5417  C  CE1   . TYR   A 1 678 ? 156.574 118.815 110.434 1.00 81.90  ?  678  TYR   A CE1   1 
ATOM   5418  C  CE2   . TYR   A 1 678 ? 154.879 117.133 110.471 1.00 79.33  ?  678  TYR   A CE2   1 
ATOM   5419  C  CZ    . TYR   A 1 678 ? 155.442 118.270 111.001 1.00 84.38  ?  678  TYR   A CZ    1 
ATOM   5420  O  OH    . TYR   A 1 678 ? 154.869 118.860 112.102 1.00 88.95  ?  678  TYR   A OH    1 
ATOM   5421  N  N     . LEU   A 1 679 ? 157.521 113.441 108.669 1.00 74.51  ?  679  LEU   A N     1 
ATOM   5422  C  CA    . LEU   A 1 679 ? 157.276 112.418 109.680 1.00 72.43  ?  679  LEU   A CA    1 
ATOM   5423  C  C     . LEU   A 1 679 ? 158.582 111.817 110.187 1.00 74.42  ?  679  LEU   A C     1 
ATOM   5424  O  O     . LEU   A 1 679 ? 158.703 111.494 111.374 1.00 81.95  ?  679  LEU   A O     1 
ATOM   5425  C  CB    . LEU   A 1 679 ? 156.360 111.333 109.118 1.00 74.16  ?  679  LEU   A CB    1 
ATOM   5426  C  CG    . LEU   A 1 679 ? 154.865 111.655 109.174 1.00 73.39  ?  679  LEU   A CG    1 
ATOM   5427  C  CD1   . LEU   A 1 679 ? 154.044 110.514 108.596 1.00 74.32  ?  679  LEU   A CD1   1 
ATOM   5428  C  CD2   . LEU   A 1 679 ? 154.434 111.963 110.598 1.00 73.81  ?  679  LEU   A CD2   1 
ATOM   5429  N  N     . GLN   A 1 680 ? 159.570 111.655 109.304 1.00 75.71  ?  680  GLN   A N     1 
ATOM   5430  C  CA    . GLN   A 1 680 ? 160.878 111.176 109.741 1.00 74.59  ?  680  GLN   A CA    1 
ATOM   5431  C  C     . GLN   A 1 680 ? 161.533 112.161 110.701 1.00 74.69  ?  680  GLN   A C     1 
ATOM   5432  O  O     . GLN   A 1 680 ? 162.111 111.760 111.720 1.00 81.12  ?  680  GLN   A O     1 
ATOM   5433  C  CB    . GLN   A 1 680 ? 161.776 110.929 108.530 1.00 73.96  ?  680  GLN   A CB    1 
ATOM   5434  C  CG    . GLN   A 1 680 ? 161.770 109.493 108.042 1.00 76.16  ?  680  GLN   A CG    1 
ATOM   5435  C  CD    . GLN   A 1 680 ? 162.134 109.373 106.578 1.00 81.94  ?  680  GLN   A CD    1 
ATOM   5436  O  OE1   . GLN   A 1 680 ? 161.501 108.630 105.829 1.00 86.02  ?  680  GLN   A OE1   1 
ATOM   5437  N  NE2   . GLN   A 1 680 ? 163.160 110.103 106.162 1.00 79.25  ?  680  GLN   A NE2   1 
ATOM   5438  N  N     . LEU   A 1 681 ? 161.451 113.458 110.394 1.00 61.75  ?  681  LEU   A N     1 
ATOM   5439  C  CA    . LEU   A 1 681 ? 161.985 114.465 111.305 1.00 61.95  ?  681  LEU   A CA    1 
ATOM   5440  C  C     . LEU   A 1 681 ? 161.250 114.441 112.639 1.00 65.98  ?  681  LEU   A C     1 
ATOM   5441  O  O     . LEU   A 1 681 ? 161.868 114.592 113.700 1.00 68.44  ?  681  LEU   A O     1 
ATOM   5442  C  CB    . LEU   A 1 681 ? 161.896 115.852 110.669 1.00 60.31  ?  681  LEU   A CB    1 
ATOM   5443  C  CG    . LEU   A 1 681 ? 162.959 116.203 109.628 1.00 66.18  ?  681  LEU   A CG    1 
ATOM   5444  C  CD1   . LEU   A 1 681 ? 162.892 117.680 109.277 1.00 66.15  ?  681  LEU   A CD1   1 
ATOM   5445  C  CD2   . LEU   A 1 681 ? 164.345 115.830 110.125 1.00 69.17  ?  681  LEU   A CD2   1 
ATOM   5446  N  N     . VAL   A 1 682 ? 159.929 114.255 112.604 1.00 63.14  ?  682  VAL   A N     1 
ATOM   5447  C  CA    . VAL   A 1 682 ? 159.149 114.186 113.837 1.00 56.24  ?  682  VAL   A CA    1 
ATOM   5448  C  C     . VAL   A 1 682 ? 159.576 112.986 114.671 1.00 63.26  ?  682  VAL   A C     1 
ATOM   5449  O  O     . VAL   A 1 682 ? 159.697 113.077 115.897 1.00 74.67  ?  682  VAL   A O     1 
ATOM   5450  C  CB    . VAL   A 1 682 ? 157.643 114.154 113.517 1.00 59.78  ?  682  VAL   A CB    1 
ATOM   5451  C  CG1   . VAL   A 1 682 ? 156.844 113.726 114.736 1.00 60.66  ?  682  VAL   A CG1   1 
ATOM   5452  C  CG2   . VAL   A 1 682 ? 157.180 115.518 113.030 1.00 60.44  ?  682  VAL   A CG2   1 
ATOM   5453  N  N     . GLY   A 1 683 ? 159.811 111.844 114.025 1.00 65.67  ?  683  GLY   A N     1 
ATOM   5454  C  CA    . GLY   A 1 683 ? 160.290 110.680 114.755 1.00 55.39  ?  683  GLY   A CA    1 
ATOM   5455  C  C     . GLY   A 1 683 ? 161.664 110.895 115.362 1.00 59.81  ?  683  GLY   A C     1 
ATOM   5456  O  O     . GLY   A 1 683 ? 161.925 110.487 116.499 1.00 68.22  ?  683  GLY   A O     1 
ATOM   5457  N  N     . ILE   A 1 684 ? 162.560 111.542 114.614 1.00 62.01  ?  684  ILE   A N     1 
ATOM   5458  C  CA    . ILE   A 1 684 ? 163.891 111.838 115.139 1.00 60.68  ?  684  ILE   A CA    1 
ATOM   5459  C  C     . ILE   A 1 684 ? 163.792 112.756 116.351 1.00 65.36  ?  684  ILE   A C     1 
ATOM   5460  O  O     . ILE   A 1 684 ? 164.494 112.565 117.352 1.00 75.55  ?  684  ILE   A O     1 
ATOM   5461  C  CB    . ILE   A 1 684 ? 164.781 112.440 114.036 1.00 63.99  ?  684  ILE   A CB    1 
ATOM   5462  C  CG1   . ILE   A 1 684 ? 165.106 111.382 112.983 1.00 68.30  ?  684  ILE   A CG1   1 
ATOM   5463  C  CG2   . ILE   A 1 684 ? 166.063 113.001 114.628 1.00 60.47  ?  684  ILE   A CG2   1 
ATOM   5464  C  CD1   . ILE   A 1 684 ? 165.453 111.956 111.632 1.00 69.79  ?  684  ILE   A CD1   1 
ATOM   5465  N  N     . MET   A 1 685 ? 162.923 113.768 116.282 1.00 68.90  ?  685  MET   A N     1 
ATOM   5466  C  CA    . MET   A 1 685 ? 162.688 114.621 117.444 1.00 64.34  ?  685  MET   A CA    1 
ATOM   5467  C  C     . MET   A 1 685 ? 162.127 113.820 118.613 1.00 69.26  ?  685  MET   A C     1 
ATOM   5468  O  O     . MET   A 1 685 ? 162.547 114.003 119.761 1.00 75.85  ?  685  MET   A O     1 
ATOM   5469  C  CB    . MET   A 1 685 ? 161.734 115.759 117.080 1.00 66.94  ?  685  MET   A CB    1 
ATOM   5470  C  CG    . MET   A 1 685 ? 162.233 116.694 115.998 1.00 67.73  ?  685  MET   A CG    1 
ATOM   5471  S  SD    . MET   A 1 685 ? 161.042 117.996 115.624 1.00 89.83  ?  685  MET   A SD    1 
ATOM   5472  C  CE    . MET   A 1 685 ? 161.074 117.997 113.836 1.00 77.34  ?  685  MET   A CE    1 
ATOM   5473  N  N     . GLN   A 1 686 ? 161.177 112.923 118.337 1.00 59.10  ?  686  GLN   A N     1 
ATOM   5474  C  CA    . GLN   A 1 686 ? 160.556 112.118 119.381 1.00 56.93  ?  686  GLN   A CA    1 
ATOM   5475  C  C     . GLN   A 1 686 ? 161.533 111.137 120.012 1.00 62.93  ?  686  GLN   A C     1 
ATOM   5476  O  O     . GLN   A 1 686 ? 161.275 110.650 121.118 1.00 71.08  ?  686  GLN   A O     1 
ATOM   5477  C  CB    . GLN   A 1 686 ? 159.349 111.368 118.812 1.00 55.23  ?  686  GLN   A CB    1 
ATOM   5478  C  CG    . GLN   A 1 686 ? 158.456 110.701 119.850 1.00 55.55  ?  686  GLN   A CG    1 
ATOM   5479  C  CD    . GLN   A 1 686 ? 157.941 111.665 120.900 1.00 64.75  ?  686  GLN   A CD    1 
ATOM   5480  O  OE1   . GLN   A 1 686 ? 156.883 112.269 120.734 1.00 73.50  ?  686  GLN   A OE1   1 
ATOM   5481  N  NE2   . GLN   A 1 686 ? 158.679 111.801 121.994 1.00 64.31  ?  686  GLN   A NE2   1 
ATOM   5482  N  N     . LYS   A 1 687 ? 162.645 110.837 119.337 1.00 61.26  ?  687  LYS   A N     1 
ATOM   5483  C  CA    . LYS   A 1 687 ? 163.670 109.998 119.950 1.00 58.79  ?  687  LYS   A CA    1 
ATOM   5484  C  C     . LYS   A 1 687 ? 164.164 110.584 121.269 1.00 64.92  ?  687  LYS   A C     1 
ATOM   5485  O  O     . LYS   A 1 687 ? 164.468 109.835 122.205 1.00 70.98  ?  687  LYS   A O     1 
ATOM   5486  C  CB    . LYS   A 1 687 ? 164.840 109.806 118.984 1.00 64.41  ?  687  LYS   A CB    1 
ATOM   5487  C  CG    . LYS   A 1 687 ? 166.067 109.165 119.610 1.00 62.00  ?  687  LYS   A CG    1 
ATOM   5488  C  CD    . LYS   A 1 687 ? 167.124 108.849 118.570 1.00 63.08  ?  687  LYS   A CD    1 
ATOM   5489  C  CE    . LYS   A 1 687 ? 168.334 108.189 119.206 1.00 64.69  ?  687  LYS   A CE    1 
ATOM   5490  N  NZ    . LYS   A 1 687 ? 169.274 107.657 118.186 1.00 66.08  ?  687  LYS   A NZ    1 
ATOM   5491  N  N     . PHE   A 1 688 ? 164.234 111.911 121.372 1.00 65.37  ?  688  PHE   A N     1 
ATOM   5492  C  CA    . PHE   A 1 688 ? 164.770 112.569 122.556 1.00 62.76  ?  688  PHE   A CA    1 
ATOM   5493  C  C     . PHE   A 1 688 ? 163.725 113.269 123.409 1.00 68.46  ?  688  PHE   A C     1 
ATOM   5494  O  O     . PHE   A 1 688 ? 163.904 113.358 124.624 1.00 78.75  ?  688  PHE   A O     1 
ATOM   5495  C  CB    . PHE   A 1 688 ? 165.842 113.589 122.154 1.00 65.13  ?  688  PHE   A CB    1 
ATOM   5496  C  CG    . PHE   A 1 688 ? 167.026 112.978 121.469 1.00 71.14  ?  688  PHE   A CG    1 
ATOM   5497  C  CD1   . PHE   A 1 688 ? 168.001 112.322 122.198 1.00 68.01  ?  688  PHE   A CD1   1 
ATOM   5498  C  CD2   . PHE   A 1 688 ? 167.162 113.053 120.094 1.00 70.86  ?  688  PHE   A CD2   1 
ATOM   5499  C  CE1   . PHE   A 1 688 ? 169.091 111.755 121.570 1.00 69.71  ?  688  PHE   A CE1   1 
ATOM   5500  C  CE2   . PHE   A 1 688 ? 168.251 112.488 119.461 1.00 72.32  ?  688  PHE   A CE2   1 
ATOM   5501  C  CZ    . PHE   A 1 688 ? 169.215 111.838 120.200 1.00 71.83  ?  688  PHE   A CZ    1 
ATOM   5502  N  N     . ILE   A 1 689 ? 162.642 113.766 122.812 1.00 69.34  ?  689  ILE   A N     1 
ATOM   5503  C  CA    . ILE   A 1 689 ? 161.643 114.513 123.567 1.00 66.13  ?  689  ILE   A CA    1 
ATOM   5504  C  C     . ILE   A 1 689 ? 160.877 113.558 124.475 1.00 63.11  ?  689  ILE   A C     1 
ATOM   5505  O  O     . ILE   A 1 689 ? 160.482 112.461 124.059 1.00 65.26  ?  689  ILE   A O     1 
ATOM   5506  C  CB    . ILE   A 1 689 ? 160.711 115.275 122.611 1.00 59.23  ?  689  ILE   A CB    1 
ATOM   5507  C  CG1   . ILE   A 1 689 ? 161.154 116.731 122.477 1.00 64.20  ?  689  ILE   A CG1   1 
ATOM   5508  C  CG2   . ILE   A 1 689 ? 159.286 115.258 123.104 1.00 61.23  ?  689  ILE   A CG2   1 
ATOM   5509  C  CD1   . ILE   A 1 689 ? 162.565 116.904 122.001 1.00 66.96  ?  689  ILE   A CD1   1 
ATOM   5510  N  N     . ASP   A 1 690 ? 160.683 113.965 125.733 1.00 70.32  ?  690  ASP   A N     1 
ATOM   5511  C  CA    . ASP   A 1 690 ? 160.045 113.091 126.713 1.00 70.58  ?  690  ASP   A CA    1 
ATOM   5512  C  C     . ASP   A 1 690 ? 158.561 112.906 126.417 1.00 76.35  ?  690  ASP   A C     1 
ATOM   5513  O  O     . ASP   A 1 690 ? 158.046 111.783 126.451 1.00 81.34  ?  690  ASP   A O     1 
ATOM   5514  C  CB    . ASP   A 1 690 ? 160.239 113.653 128.122 1.00 72.71  ?  690  ASP   A CB    1 
ATOM   5515  C  CG    . ASP   A 1 690 ? 161.699 113.799 128.497 1.00 81.79  ?  690  ASP   A CG    1 
ATOM   5516  O  OD1   . ASP   A 1 690 ? 162.481 112.865 128.224 1.00 86.10  ?  690  ASP   A OD1   1 
ATOM   5517  O  OD2   . ASP   A 1 690 ? 162.065 114.846 129.068 1.00 80.35  ?  690  ASP   A OD2   1 
ATOM   5518  N  N     . GLN   A 1 691 ? 157.857 113.996 126.138 1.00 66.12  ?  691  GLN   A N     1 
ATOM   5519  C  CA    . GLN   A 1 691 ? 156.417 113.962 125.923 1.00 58.72  ?  691  GLN   A CA    1 
ATOM   5520  C  C     . GLN   A 1 691 ? 156.134 113.773 124.431 1.00 61.65  ?  691  GLN   A C     1 
ATOM   5521  O  O     . GLN   A 1 691 ? 157.005 113.344 123.671 1.00 65.06  ?  691  GLN   A O     1 
ATOM   5522  C  CB    . GLN   A 1 691 ? 155.780 115.220 126.518 1.00 61.07  ?  691  GLN   A CB    1 
ATOM   5523  C  CG    . GLN   A 1 691 ? 156.019 115.356 128.014 1.00 60.14  ?  691  GLN   A CG    1 
ATOM   5524  C  CD    . GLN   A 1 691 ? 155.071 116.329 128.679 1.00 69.02  ?  691  GLN   A CD    1 
ATOM   5525  O  OE1   . GLN   A 1 691 ? 153.911 116.010 128.926 1.00 72.10  ?  691  GLN   A OE1   1 
ATOM   5526  N  NE2   . GLN   A 1 691 ? 155.565 117.523 128.983 1.00 70.04  ?  691  GLN   A NE2   1 
ATOM   5527  N  N     . SER   A 1 692 ? 154.903 114.032 124.002 1.00 66.92  ?  692  SER   A N     1 
ATOM   5528  C  CA    . SER   A 1 692 ? 154.530 113.855 122.609 1.00 56.48  ?  692  SER   A CA    1 
ATOM   5529  C  C     . SER   A 1 692 ? 154.881 115.098 121.792 1.00 52.25  ?  692  SER   A C     1 
ATOM   5530  O  O     . SER   A 1 692 ? 155.407 116.088 122.303 1.00 60.93  ?  692  SER   A O     1 
ATOM   5531  C  CB    . SER   A 1 692 ? 153.043 113.529 122.496 1.00 62.15  ?  692  SER   A CB    1 
ATOM   5532  O  OG    . SER   A 1 692 ? 152.763 112.879 121.271 1.00 68.80  ?  692  SER   A OG    1 
ATOM   5533  N  N     . ILE   A 1 693 ? 154.592 115.037 120.493 1.00 60.06  ?  693  ILE   A N     1 
ATOM   5534  C  CA    . ILE   A 1 693 ? 154.844 116.129 119.560 1.00 60.73  ?  693  ILE   A CA    1 
ATOM   5535  C  C     . ILE   A 1 693 ? 153.579 116.366 118.748 1.00 61.53  ?  693  ILE   A C     1 
ATOM   5536  O  O     . ILE   A 1 693 ? 152.961 115.411 118.265 1.00 69.98  ?  693  ILE   A O     1 
ATOM   5537  C  CB    . ILE   A 1 693 ? 156.029 115.825 118.623 1.00 58.27  ?  693  ILE   A CB    1 
ATOM   5538  C  CG1   . ILE   A 1 693 ? 157.289 115.505 119.427 1.00 56.85  ?  693  ILE   A CG1   1 
ATOM   5539  C  CG2   . ILE   A 1 693 ? 156.277 116.987 117.675 1.00 53.15  ?  693  ILE   A CG2   1 
ATOM   5540  C  CD1   . ILE   A 1 693 ? 158.479 115.150 118.572 1.00 56.88  ?  693  ILE   A CD1   1 
ATOM   5541  N  N     . SER   A 1 694 ? 153.196 117.632 118.597 1.00 63.12  ?  694  SER   A N     1 
ATOM   5542  C  CA    . SER   A 1 694 ? 152.050 118.000 117.766 1.00 68.30  ?  694  SER   A CA    1 
ATOM   5543  C  C     . SER   A 1 694 ? 152.496 117.986 116.309 1.00 75.84  ?  694  SER   A C     1 
ATOM   5544  O  O     . SER   A 1 694 ? 153.011 118.972 115.781 1.00 82.54  ?  694  SER   A O     1 
ATOM   5545  C  CB    . SER   A 1 694 ? 151.503 119.363 118.170 1.00 70.82  ?  694  SER   A CB    1 
ATOM   5546  O  OG    . SER   A 1 694 ? 150.782 119.284 119.386 1.00 81.47  ?  694  SER   A OG    1 
ATOM   5547  N  N     . ALA   A 1 695 ? 152.295 116.848 115.651 1.00 72.41  ?  695  ALA   A N     1 
ATOM   5548  C  CA    . ALA   A 1 695 ? 152.715 116.644 114.272 1.00 69.29  ?  695  ALA   A CA    1 
ATOM   5549  C  C     . ALA   A 1 695 ? 151.502 116.692 113.354 1.00 72.08  ?  695  ALA   A C     1 
ATOM   5550  O  O     . ALA   A 1 695 ? 150.507 116.002 113.597 1.00 78.54  ?  695  ALA   A O     1 
ATOM   5551  C  CB    . ALA   A 1 695 ? 153.445 115.309 114.113 1.00 69.92  ?  695  ALA   A CB    1 
ATOM   5552  N  N     . ASN   A 1 696 ? 151.592 117.498 112.302 1.00 69.16  ?  696  ASN   A N     1 
ATOM   5553  C  CA    . ASN   A 1 696 ? 150.516 117.659 111.338 1.00 66.11  ?  696  ASN   A CA    1 
ATOM   5554  C  C     . ASN   A 1 696 ? 150.802 116.854 110.077 1.00 71.80  ?  696  ASN   A C     1 
ATOM   5555  O  O     . ASN   A 1 696 ? 151.954 116.690 109.669 1.00 79.39  ?  696  ASN   A O     1 
ATOM   5556  C  CB    . ASN   A 1 696 ? 150.325 119.132 110.970 1.00 68.62  ?  696  ASN   A CB    1 
ATOM   5557  C  CG    . ASN   A 1 696 ? 149.679 119.934 112.079 1.00 76.23  ?  696  ASN   A CG    1 
ATOM   5558  O  OD1   . ASN   A 1 696 ? 148.899 119.406 112.868 1.00 81.28  ?  696  ASN   A OD1   1 
ATOM   5559  N  ND2   . ASN   A 1 696 ? 149.998 121.221 112.141 1.00 77.23  ?  696  ASN   A ND2   1 
ATOM   5560  N  N     . THR   A 1 697 ? 149.737 116.349 109.464 1.00 72.78  ?  697  THR   A N     1 
ATOM   5561  C  CA    . THR   A 1 697 ? 149.805 115.713 108.156 1.00 75.30  ?  697  THR   A CA    1 
ATOM   5562  C  C     . THR   A 1 697 ? 149.100 116.610 107.149 1.00 78.10  ?  697  THR   A C     1 
ATOM   5563  O  O     . THR   A 1 697 ? 147.937 116.974 107.345 1.00 79.38  ?  697  THR   A O     1 
ATOM   5564  C  CB    . THR   A 1 697 ? 149.162 114.324 108.175 1.00 74.09  ?  697  THR   A CB    1 
ATOM   5565  O  OG1   . THR   A 1 697 ? 147.859 114.404 108.763 1.00 79.10  ?  697  THR   A OG1   1 
ATOM   5566  C  CG2   . THR   A 1 697 ? 150.015 113.353 108.976 1.00 71.84  ?  697  THR   A CG2   1 
ATOM   5567  N  N     . ASN   A 1 698 ? 149.803 116.967 106.079 1.00 85.74  ?  698  ASN   A N     1 
ATOM   5568  C  CA    . ASN   A 1 698 ? 149.307 117.921 105.098 1.00 80.95  ?  698  ASN   A CA    1 
ATOM   5569  C  C     . ASN   A 1 698 ? 149.132 117.231 103.754 1.00 81.34  ?  698  ASN   A C     1 
ATOM   5570  O  O     . ASN   A 1 698 ? 150.027 116.512 103.298 1.00 84.58  ?  698  ASN   A O     1 
ATOM   5571  C  CB    . ASN   A 1 698 ? 150.258 119.112 104.968 1.00 78.83  ?  698  ASN   A CB    1 
ATOM   5572  C  CG    . ASN   A 1 698 ? 150.806 119.564 106.306 1.00 84.23  ?  698  ASN   A CG    1 
ATOM   5573  O  OD1   . ASN   A 1 698 ? 150.188 120.368 107.002 1.00 86.34  ?  698  ASN   A OD1   1 
ATOM   5574  N  ND2   . ASN   A 1 698 ? 151.970 119.045 106.674 1.00 87.57  ?  698  ASN   A ND2   1 
ATOM   5575  N  N     . TYR   A 1 699 ? 147.981 117.455 103.127 1.00 76.87  ?  699  TYR   A N     1 
ATOM   5576  C  CA    . TYR   A 1 699 ? 147.659 116.855 101.841 1.00 78.34  ?  699  TYR   A CA    1 
ATOM   5577  C  C     . TYR   A 1 699 ? 147.142 117.916 100.884 1.00 84.05  ?  699  TYR   A C     1 
ATOM   5578  O  O     . TYR   A 1 699 ? 146.314 118.752 101.256 1.00 85.90  ?  699  TYR   A O     1 
ATOM   5579  C  CB    . TYR   A 1 699 ? 146.615 115.748 101.990 1.00 76.63  ?  699  TYR   A CB    1 
ATOM   5580  C  CG    . TYR   A 1 699 ? 147.123 114.534 102.723 1.00 78.98  ?  699  TYR   A CG    1 
ATOM   5581  C  CD1   . TYR   A 1 699 ? 147.907 113.589 102.078 1.00 76.91  ?  699  TYR   A CD1   1 
ATOM   5582  C  CD2   . TYR   A 1 699 ? 146.824 114.335 104.061 1.00 82.17  ?  699  TYR   A CD2   1 
ATOM   5583  C  CE1   . TYR   A 1 699 ? 148.375 112.477 102.747 1.00 74.99  ?  699  TYR   A CE1   1 
ATOM   5584  C  CE2   . TYR   A 1 699 ? 147.288 113.229 104.737 1.00 80.72  ?  699  TYR   A CE2   1 
ATOM   5585  C  CZ    . TYR   A 1 699 ? 148.062 112.303 104.076 1.00 79.29  ?  699  TYR   A CZ    1 
ATOM   5586  O  OH    . TYR   A 1 699 ? 148.523 111.199 104.750 1.00 83.79  ?  699  TYR   A OH    1 
ATOM   5587  N  N     . ASP   A 1 700 ? 147.636 117.877 99.652  1.00 103.72 ?  700  ASP   A N     1 
ATOM   5588  C  CA    . ASP   A 1 700 ? 147.132 118.736 98.588  1.00 101.06 ?  700  ASP   A CA    1 
ATOM   5589  C  C     . ASP   A 1 700 ? 146.445 117.865 97.548  1.00 102.70 ?  700  ASP   A C     1 
ATOM   5590  O  O     . ASP   A 1 700 ? 147.123 117.088 96.857  1.00 106.31 ?  700  ASP   A O     1 
ATOM   5591  C  CB    . ASP   A 1 700 ? 148.268 119.540 97.954  1.00 102.30 ?  700  ASP   A CB    1 
ATOM   5592  C  CG    . ASP   A 1 700 ? 147.768 120.600 96.993  1.00 107.53 ?  700  ASP   A CG    1 
ATOM   5593  O  OD1   . ASP   A 1 700 ? 146.537 120.777 96.880  1.00 108.27 ?  700  ASP   A OD1   1 
ATOM   5594  O  OD2   . ASP   A 1 700 ? 148.608 121.260 96.348  1.00 109.97 ?  700  ASP   A OD2   1 
ATOM   5595  N  N     . PRO   A 1 701 ? 145.119 117.938 97.408  1.00 95.30  ?  701  PRO   A N     1 
ATOM   5596  C  CA    . PRO   A 1 701 ? 144.437 117.067 96.436  1.00 96.98  ?  701  PRO   A CA    1 
ATOM   5597  C  C     . PRO   A 1 701 ? 144.875 117.291 95.000  1.00 99.86  ?  701  PRO   A C     1 
ATOM   5598  O  O     . PRO   A 1 701 ? 144.769 116.370 94.181  1.00 101.38 ?  701  PRO   A O     1 
ATOM   5599  C  CB    . PRO   A 1 701 ? 142.955 117.417 96.635  1.00 95.62  ?  701  PRO   A CB    1 
ATOM   5600  C  CG    . PRO   A 1 701 ? 142.881 118.022 98.000  1.00 96.11  ?  701  PRO   A CG    1 
ATOM   5601  C  CD    . PRO   A 1 701 ? 144.171 118.755 98.182  1.00 94.98  ?  701  PRO   A CD    1 
ATOM   5602  N  N     . SER   A 1 702 ? 145.362 118.489 94.667  1.00 104.47 ?  702  SER   A N     1 
ATOM   5603  C  CA    . SER   A 1 702 ? 145.810 118.754 93.303  1.00 103.41 ?  702  SER   A CA    1 
ATOM   5604  C  C     . SER   A 1 702 ? 147.001 117.884 92.923  1.00 104.01 ?  702  SER   A C     1 
ATOM   5605  O  O     . SER   A 1 702 ? 147.163 117.532 91.749  1.00 103.36 ?  702  SER   A O     1 
ATOM   5606  C  CB    . SER   A 1 702 ? 146.162 120.232 93.144  1.00 102.48 ?  702  SER   A CB    1 
ATOM   5607  O  OG    . SER   A 1 702 ? 147.560 120.436 93.260  1.00 104.56 ?  702  SER   A OG    1 
ATOM   5608  N  N     . ARG   A 1 703 ? 147.841 117.526 93.896  1.00 103.77 ?  703  ARG   A N     1 
ATOM   5609  C  CA    . ARG   A 1 703 ? 149.002 116.688 93.626  1.00 102.23 ?  703  ARG   A CA    1 
ATOM   5610  C  C     . ARG   A 1 703 ? 148.631 115.244 93.320  1.00 104.51 ?  703  ARG   A C     1 
ATOM   5611  O  O     . ARG   A 1 703 ? 149.504 114.475 92.905  1.00 105.88 ?  703  ARG   A O     1 
ATOM   5612  C  CB    . ARG   A 1 703 ? 149.964 116.730 94.814  1.00 100.16 ?  703  ARG   A CB    1 
ATOM   5613  C  CG    . ARG   A 1 703 ? 150.657 118.067 95.001  1.00 102.15 ?  703  ARG   A CG    1 
ATOM   5614  C  CD    . ARG   A 1 703 ? 151.697 117.996 96.103  1.00 102.49 ?  703  ARG   A CD    1 
ATOM   5615  N  NE    . ARG   A 1 703 ? 153.013 117.644 95.586  1.00 103.90 ?  703  ARG   A NE    1 
ATOM   5616  C  CZ    . ARG   A 1 703 ? 154.047 118.472 95.546  1.00 107.12 ?  703  ARG   A CZ    1 
ATOM   5617  N  NH1   . ARG   A 1 703 ? 153.956 119.715 95.990  1.00 105.66 ?  703  ARG   A NH1   1 
ATOM   5618  N  NH2   . ARG   A 1 703 ? 155.202 118.043 95.046  1.00 104.97 ?  703  ARG   A NH2   1 
ATOM   5619  N  N     . PHE   A 1 704 ? 147.372 114.857 93.516  1.00 107.43 ?  704  PHE   A N     1 
ATOM   5620  C  CA    . PHE   A 1 704 ? 146.930 113.494 93.285  1.00 108.31 ?  704  PHE   A CA    1 
ATOM   5621  C  C     . PHE   A 1 704 ? 146.027 113.419 92.058  1.00 110.07 ?  704  PHE   A C     1 
ATOM   5622  O  O     . PHE   A 1 704 ? 145.329 114.386 91.734  1.00 108.12 ?  704  PHE   A O     1 
ATOM   5623  C  CB    . PHE   A 1 704 ? 146.178 112.952 94.506  1.00 106.27 ?  704  PHE   A CB    1 
ATOM   5624  C  CG    . PHE   A 1 704 ? 147.035 112.817 95.730  1.00 107.40 ?  704  PHE   A CG    1 
ATOM   5625  C  CD1   . PHE   A 1 704 ? 147.788 111.675 95.941  1.00 106.31 ?  704  PHE   A CD1   1 
ATOM   5626  C  CD2   . PHE   A 1 704 ? 147.095 113.835 96.664  1.00 107.96 ?  704  PHE   A CD2   1 
ATOM   5627  C  CE1   . PHE   A 1 704 ? 148.580 111.549 97.064  1.00 104.05 ?  704  PHE   A CE1   1 
ATOM   5628  C  CE2   . PHE   A 1 704 ? 147.886 113.715 97.789  1.00 108.00 ?  704  PHE   A CE2   1 
ATOM   5629  C  CZ    . PHE   A 1 704 ? 148.630 112.571 97.989  1.00 107.72 ?  704  PHE   A CZ    1 
ATOM   5630  N  N     . PRO   A 1 705 ? 146.027 112.290 91.349  1.00 122.23 ?  705  PRO   A N     1 
ATOM   5631  C  CA    . PRO   A 1 705 ? 145.148 112.155 90.182  1.00 121.42 ?  705  PRO   A CA    1 
ATOM   5632  C  C     . PRO   A 1 705 ? 143.682 112.253 90.576  1.00 120.90 ?  705  PRO   A C     1 
ATOM   5633  O  O     . PRO   A 1 705 ? 143.278 111.840 91.665  1.00 122.05 ?  705  PRO   A O     1 
ATOM   5634  C  CB    . PRO   A 1 705 ? 145.488 110.764 89.634  1.00 119.30 ?  705  PRO   A CB    1 
ATOM   5635  C  CG    . PRO   A 1 705 ? 146.822 110.428 90.212  1.00 118.65 ?  705  PRO   A CG    1 
ATOM   5636  C  CD    . PRO   A 1 705 ? 146.892 111.114 91.537  1.00 118.18 ?  705  PRO   A CD    1 
ATOM   5637  N  N     . SER   A 1 706 ? 142.888 112.824 89.671  1.00 116.95 ?  706  SER   A N     1 
ATOM   5638  C  CA    . SER   A 1 706 ? 141.451 113.034 89.828  1.00 117.11 ?  706  SER   A CA    1 
ATOM   5639  C  C     . SER   A 1 706 ? 141.108 113.973 90.979  1.00 118.27 ?  706  SER   A C     1 
ATOM   5640  O  O     . SER   A 1 706 ? 139.929 114.112 91.327  1.00 121.18 ?  706  SER   A O     1 
ATOM   5641  C  CB    . SER   A 1 706 ? 140.701 111.705 90.000  1.00 117.38 ?  706  SER   A CB    1 
ATOM   5642  O  OG    . SER   A 1 706 ? 140.933 111.147 91.282  1.00 117.89 ?  706  SER   A OG    1 
ATOM   5643  N  N     . GLY   A 1 707 ? 142.102 114.624 91.579  1.00 115.87 ?  707  GLY   A N     1 
ATOM   5644  C  CA    . GLY   A 1 707 ? 141.837 115.578 92.637  1.00 117.30 ?  707  GLY   A CA    1 
ATOM   5645  C  C     . GLY   A 1 707 ? 141.375 114.976 93.943  1.00 117.33 ?  707  GLY   A C     1 
ATOM   5646  O  O     . GLY   A 1 707 ? 140.853 115.699 94.795  1.00 115.97 ?  707  GLY   A O     1 
ATOM   5647  N  N     . LYS   A 1 708 ? 141.549 113.671 94.130  1.00 119.50 ?  708  LYS   A N     1 
ATOM   5648  C  CA    . LYS   A 1 708 ? 141.121 112.983 95.340  1.00 119.40 ?  708  LYS   A CA    1 
ATOM   5649  C  C     . LYS   A 1 708 ? 142.317 112.297 95.983  1.00 120.35 ?  708  LYS   A C     1 
ATOM   5650  O  O     . LYS   A 1 708 ? 143.095 111.625 95.297  1.00 119.48 ?  708  LYS   A O     1 
ATOM   5651  C  CB    . LYS   A 1 708 ? 140.025 111.957 95.035  1.00 121.01 ?  708  LYS   A CB    1 
ATOM   5652  C  CG    . LYS   A 1 708 ? 139.029 112.401 93.975  1.00 120.82 ?  708  LYS   A CG    1 
ATOM   5653  C  CD    . LYS   A 1 708 ? 137.731 111.613 94.063  1.00 120.13 ?  708  LYS   A CD    1 
ATOM   5654  C  CE    . LYS   A 1 708 ? 137.992 110.123 94.221  1.00 122.12 ?  708  LYS   A CE    1 
ATOM   5655  N  NZ    . LYS   A 1 708 ? 137.916 109.404 92.919  1.00 121.61 ?  708  LYS   A NZ    1 
ATOM   5656  N  N     . VAL   A 1 709 ? 142.460 112.467 97.293  1.00 106.63 ?  709  VAL   A N     1 
ATOM   5657  C  CA    . VAL   A 1 709 ? 143.529 111.814 98.044  1.00 101.76 ?  709  VAL   A CA    1 
ATOM   5658  C  C     . VAL   A 1 709 ? 143.101 110.380 98.334  1.00 100.53 ?  709  VAL   A C     1 
ATOM   5659  O  O     . VAL   A 1 709 ? 142.083 110.163 99.005  1.00 105.65 ?  709  VAL   A O     1 
ATOM   5660  C  CB    . VAL   A 1 709 ? 143.849 112.575 99.340  1.00 98.60  ?  709  VAL   A CB    1 
ATOM   5661  C  CG1   . VAL   A 1 709 ? 145.090 111.999 100.001 1.00 97.57  ?  709  VAL   A CG1   1 
ATOM   5662  C  CG2   . VAL   A 1 709 ? 144.028 114.057 99.055  1.00 100.59 ?  709  VAL   A CG2   1 
ATOM   5663  N  N     . PRO   A 1 710 ? 143.832 109.380 97.852  1.00 89.47  ?  710  PRO   A N     1 
ATOM   5664  C  CA    . PRO   A 1 710 ? 143.411 107.992 98.068  1.00 94.96  ?  710  PRO   A CA    1 
ATOM   5665  C  C     . PRO   A 1 710 ? 143.551 107.570 99.523  1.00 99.37  ?  710  PRO   A C     1 
ATOM   5666  O  O     . PRO   A 1 710 ? 144.383 108.090 100.271 1.00 101.51 ?  710  PRO   A O     1 
ATOM   5667  C  CB    . PRO   A 1 710 ? 144.355 107.191 97.165  1.00 94.07  ?  710  PRO   A CB    1 
ATOM   5668  C  CG    . PRO   A 1 710 ? 145.556 108.059 97.012  1.00 94.17  ?  710  PRO   A CG    1 
ATOM   5669  C  CD    . PRO   A 1 710 ? 145.054 109.472 97.036  1.00 92.67  ?  710  PRO   A CD    1 
ATOM   5670  N  N     . MET   A 1 711 ? 142.713 106.607 99.918  1.00 99.84  ?  711  MET   A N     1 
ATOM   5671  C  CA    . MET   A 1 711 ? 142.818 106.034 101.256 1.00 95.25  ?  711  MET   A CA    1 
ATOM   5672  C  C     . MET   A 1 711 ? 144.138 105.302 101.447 1.00 96.17  ?  711  MET   A C     1 
ATOM   5673  O  O     . MET   A 1 711 ? 144.657 105.240 102.569 1.00 101.53 ?  711  MET   A O     1 
ATOM   5674  C  CB    . MET   A 1 711 ? 141.648 105.086 101.519 1.00 93.86  ?  711  MET   A CB    1 
ATOM   5675  C  CG    . MET   A 1 711 ? 141.554 104.588 102.956 1.00 95.34  ?  711  MET   A CG    1 
ATOM   5676  S  SD    . MET   A 1 711 ? 141.087 105.860 104.146 1.00 105.99 ?  711  MET   A SD    1 
ATOM   5677  C  CE    . MET   A 1 711 ? 139.810 106.725 103.242 1.00 98.41  ?  711  MET   A CE    1 
ATOM   5678  N  N     . GLN   A 1 712 ? 144.692 104.738 100.371 1.00 108.24 ?  712  GLN   A N     1 
ATOM   5679  C  CA    . GLN   A 1 712 ? 145.958 104.024 100.484 1.00 108.15 ?  712  GLN   A CA    1 
ATOM   5680  C  C     . GLN   A 1 712 ? 147.076 104.957 100.927 1.00 108.93 ?  712  GLN   A C     1 
ATOM   5681  O  O     . GLN   A 1 712 ? 147.915 104.581 101.750 1.00 111.48 ?  712  GLN   A O     1 
ATOM   5682  C  CB    . GLN   A 1 712 ? 146.308 103.357 99.154  1.00 109.35 ?  712  GLN   A CB    1 
ATOM   5683  C  CG    . GLN   A 1 712 ? 147.540 102.471 99.219  1.00 112.60 ?  712  GLN   A CG    1 
ATOM   5684  C  CD    . GLN   A 1 712 ? 147.203 101.024 99.514  1.00 117.57 ?  712  GLN   A CD    1 
ATOM   5685  O  OE1   . GLN   A 1 712 ? 146.115 100.713 99.996  1.00 117.65 ?  712  GLN   A OE1   1 
ATOM   5686  N  NE2   . GLN   A 1 712 ? 148.139 100.129 99.222  1.00 117.69 ?  712  GLN   A NE2   1 
ATOM   5687  N  N     . GLN   A 1 713 ? 147.100 106.182 100.395 1.00 87.62  ?  713  GLN   A N     1 
ATOM   5688  C  CA    . GLN   A 1 713 ? 148.112 107.148 100.812 1.00 82.52  ?  713  GLN   A CA    1 
ATOM   5689  C  C     . GLN   A 1 713 ? 147.957 107.518 102.282 1.00 84.90  ?  713  GLN   A C     1 
ATOM   5690  O  O     . GLN   A 1 713 ? 148.951 107.622 103.010 1.00 90.69  ?  713  GLN   A O     1 
ATOM   5691  C  CB    . GLN   A 1 713 ? 148.038 108.396 99.933  1.00 82.23  ?  713  GLN   A CB    1 
ATOM   5692  C  CG    . GLN   A 1 713 ? 149.175 109.378 100.158 1.00 83.91  ?  713  GLN   A CG    1 
ATOM   5693  C  CD    . GLN   A 1 713 ? 150.538 108.736 100.000 1.00 91.31  ?  713  GLN   A CD    1 
ATOM   5694  O  OE1   . GLN   A 1 713 ? 150.771 107.968 99.067  1.00 95.52  ?  713  GLN   A OE1   1 
ATOM   5695  N  NE2   . GLN   A 1 713 ? 151.448 109.048 100.914 1.00 89.38  ?  713  GLN   A NE2   1 
ATOM   5696  N  N     . LEU   A 1 714 ? 146.717 107.721 102.736 1.00 75.35  ?  714  LEU   A N     1 
ATOM   5697  C  CA    . LEU   A 1 714 ? 146.482 108.047 104.140 1.00 71.07  ?  714  LEU   A CA    1 
ATOM   5698  C  C     . LEU   A 1 714 ? 146.955 106.921 105.051 1.00 71.37  ?  714  LEU   A C     1 
ATOM   5699  O  O     . LEU   A 1 714 ? 147.637 107.160 106.057 1.00 76.81  ?  714  LEU   A O     1 
ATOM   5700  C  CB    . LEU   A 1 714 ? 144.997 108.330 104.369 1.00 74.22  ?  714  LEU   A CB    1 
ATOM   5701  C  CG    . LEU   A 1 714 ? 144.330 109.414 103.521 1.00 74.40  ?  714  LEU   A CG    1 
ATOM   5702  C  CD1   . LEU   A 1 714 ? 142.848 109.503 103.842 1.00 77.33  ?  714  LEU   A CD1   1 
ATOM   5703  C  CD2   . LEU   A 1 714 ? 145.000 110.753 103.741 1.00 69.34  ?  714  LEU   A CD2   1 
ATOM   5704  N  N     . LEU   A 1 715 ? 146.603 105.680 104.710 1.00 65.61  ?  715  LEU   A N     1 
ATOM   5705  C  CA    . LEU   A 1 715 ? 147.009 104.547 105.534 1.00 60.89  ?  715  LEU   A CA    1 
ATOM   5706  C  C     . LEU   A 1 715 ? 148.519 104.351 105.502 1.00 61.69  ?  715  LEU   A C     1 
ATOM   5707  O  O     . LEU   A 1 715 ? 149.127 104.008 106.523 1.00 70.48  ?  715  LEU   A O     1 
ATOM   5708  C  CB    . LEU   A 1 715 ? 146.285 103.281 105.078 1.00 64.59  ?  715  LEU   A CB    1 
ATOM   5709  C  CG    . LEU   A 1 715 ? 144.790 103.247 105.398 1.00 66.42  ?  715  LEU   A CG    1 
ATOM   5710  C  CD1   . LEU   A 1 715 ? 144.133 102.018 104.795 1.00 68.29  ?  715  LEU   A CD1   1 
ATOM   5711  C  CD2   . LEU   A 1 715 ? 144.561 103.299 106.900 1.00 67.11  ?  715  LEU   A CD2   1 
ATOM   5712  N  N     . LYS   A 1 716 ? 149.144 104.570 104.343 1.00 75.77  ?  716  LYS   A N     1 
ATOM   5713  C  CA    . LYS   A 1 716 ? 150.594 104.459 104.249 1.00 73.46  ?  716  LYS   A CA    1 
ATOM   5714  C  C     . LYS   A 1 716 ? 151.283 105.509 105.107 1.00 75.79  ?  716  LYS   A C     1 
ATOM   5715  O  O     . LYS   A 1 716 ? 152.280 105.216 105.773 1.00 79.10  ?  716  LYS   A O     1 
ATOM   5716  C  CB    . LYS   A 1 716 ? 151.036 104.582 102.792 1.00 72.99  ?  716  LYS   A CB    1 
ATOM   5717  C  CG    . LYS   A 1 716 ? 152.428 104.042 102.521 1.00 78.29  ?  716  LYS   A CG    1 
ATOM   5718  C  CD    . LYS   A 1 716 ? 153.252 105.028 101.710 1.00 81.31  ?  716  LYS   A CD    1 
ATOM   5719  C  CE    . LYS   A 1 716 ? 154.406 104.333 101.006 1.00 82.97  ?  716  LYS   A CE    1 
ATOM   5720  N  NZ    . LYS   A 1 716 ? 155.000 103.257 101.845 1.00 81.60  ?  716  LYS   A NZ    1 
ATOM   5721  N  N     . ASP   A 1 717 ? 150.767 106.740 105.106 1.00 79.39  ?  717  ASP   A N     1 
ATOM   5722  C  CA    . ASP   A 1 717 ? 151.356 107.782 105.942 1.00 74.71  ?  717  ASP   A CA    1 
ATOM   5723  C  C     . ASP   A 1 717 ? 151.165 107.480 107.423 1.00 78.95  ?  717  ASP   A C     1 
ATOM   5724  O  O     . ASP   A 1 717 ? 152.070 107.718 108.231 1.00 79.49  ?  717  ASP   A O     1 
ATOM   5725  C  CB    . ASP   A 1 717 ? 150.760 109.141 105.587 1.00 74.91  ?  717  ASP   A CB    1 
ATOM   5726  C  CG    . ASP   A 1 717 ? 151.332 109.708 104.305 1.00 83.59  ?  717  ASP   A CG    1 
ATOM   5727  O  OD1   . ASP   A 1 717 ? 152.523 109.460 104.025 1.00 87.93  ?  717  ASP   A OD1   1 
ATOM   5728  O  OD2   . ASP   A 1 717 ? 150.594 110.403 103.578 1.00 85.75  ?  717  ASP   A OD2   1 
ATOM   5729  N  N     . LEU   A 1 718 ? 149.995 106.958 107.800 1.00 66.15  ?  718  LEU   A N     1 
ATOM   5730  C  CA    . LEU   A 1 718 ? 149.777 106.576 109.193 1.00 62.45  ?  718  LEU   A CA    1 
ATOM   5731  C  C     . LEU   A 1 718 ? 150.736 105.468 109.619 1.00 65.07  ?  718  LEU   A C     1 
ATOM   5732  O  O     . LEU   A 1 718 ? 151.322 105.522 110.710 1.00 68.66  ?  718  LEU   A O     1 
ATOM   5733  C  CB    . LEU   A 1 718 ? 148.323 106.143 109.387 1.00 56.09  ?  718  LEU   A CB    1 
ATOM   5734  C  CG    . LEU   A 1 718 ? 147.902 105.641 110.767 1.00 54.45  ?  718  LEU   A CG    1 
ATOM   5735  C  CD1   . LEU   A 1 718 ? 147.606 106.807 111.690 1.00 59.33  ?  718  LEU   A CD1   1 
ATOM   5736  C  CD2   . LEU   A 1 718 ? 146.693 104.732 110.649 1.00 57.26  ?  718  LEU   A CD2   1 
ATOM   5737  N  N     . LEU   A 1 719 ? 150.924 104.463 108.760 1.00 70.49  ?  719  LEU   A N     1 
ATOM   5738  C  CA    . LEU   A 1 719 ? 151.851 103.381 109.073 1.00 65.53  ?  719  LEU   A CA    1 
ATOM   5739  C  C     . LEU   A 1 719 ? 153.289 103.881 109.129 1.00 70.63  ?  719  LEU   A C     1 
ATOM   5740  O  O     . LEU   A 1 719 ? 154.081 103.411 109.952 1.00 81.08  ?  719  LEU   A O     1 
ATOM   5741  C  CB    . LEU   A 1 719 ? 151.708 102.258 108.047 1.00 70.53  ?  719  LEU   A CB    1 
ATOM   5742  C  CG    . LEU   A 1 719 ? 150.436 101.420 108.170 1.00 72.22  ?  719  LEU   A CG    1 
ATOM   5743  C  CD1   . LEU   A 1 719 ? 150.115 100.736 106.852 1.00 77.67  ?  719  LEU   A CD1   1 
ATOM   5744  C  CD2   . LEU   A 1 719 ? 150.575 100.403 109.289 1.00 74.47  ?  719  LEU   A CD2   1 
ATOM   5745  N  N     . THR   A 1 720 ? 153.648 104.821 108.252 1.00 67.12  ?  720  THR   A N     1 
ATOM   5746  C  CA    . THR   A 1 720 ? 154.983 105.408 108.294 1.00 68.46  ?  720  THR   A CA    1 
ATOM   5747  C  C     . THR   A 1 720 ? 155.204 106.165 109.596 1.00 68.68  ?  720  THR   A C     1 
ATOM   5748  O  O     . THR   A 1 720 ? 156.270 106.057 110.214 1.00 70.62  ?  720  THR   A O     1 
ATOM   5749  C  CB    . THR   A 1 720 ? 155.184 106.331 107.090 1.00 67.71  ?  720  THR   A CB    1 
ATOM   5750  O  OG1   . THR   A 1 720 ? 155.422 105.543 105.917 1.00 77.69  ?  720  THR   A OG1   1 
ATOM   5751  C  CG2   . THR   A 1 720 ? 156.364 107.265 107.311 1.00 67.59  ?  720  THR   A CG2   1 
ATOM   5752  N  N     . ALA   A 1 721 ? 154.201 106.930 110.033 1.00 78.39  ?  721  ALA   A N     1 
ATOM   5753  C  CA    . ALA   A 1 721 ? 154.307 107.631 111.307 1.00 75.59  ?  721  ALA   A CA    1 
ATOM   5754  C  C     . ALA   A 1 721 ? 154.479 106.650 112.457 1.00 75.55  ?  721  ALA   A C     1 
ATOM   5755  O  O     . ALA   A 1 721 ? 155.295 106.876 113.358 1.00 79.79  ?  721  ALA   A O     1 
ATOM   5756  C  CB    . ALA   A 1 721 ? 153.076 108.509 111.530 1.00 72.60  ?  721  ALA   A CB    1 
ATOM   5757  N  N     . TYR   A 1 722 ? 153.721 105.552 112.444 1.00 74.99  ?  722  TYR   A N     1 
ATOM   5758  C  CA    . TYR   A 1 722 ? 153.865 104.561 113.507 1.00 75.25  ?  722  TYR   A CA    1 
ATOM   5759  C  C     . TYR   A 1 722 ? 155.240 103.902 113.480 1.00 72.19  ?  722  TYR   A C     1 
ATOM   5760  O  O     . TYR   A 1 722 ? 155.837 103.658 114.535 1.00 78.86  ?  722  TYR   A O     1 
ATOM   5761  C  CB    . TYR   A 1 722 ? 152.775 103.497 113.407 1.00 74.15  ?  722  TYR   A CB    1 
ATOM   5762  C  CG    . TYR   A 1 722 ? 152.955 102.399 114.426 1.00 72.15  ?  722  TYR   A CG    1 
ATOM   5763  C  CD1   . TYR   A 1 722 ? 152.631 102.607 115.757 1.00 73.08  ?  722  TYR   A CD1   1 
ATOM   5764  C  CD2   . TYR   A 1 722 ? 153.470 101.164 114.066 1.00 72.85  ?  722  TYR   A CD2   1 
ATOM   5765  C  CE1   . TYR   A 1 722 ? 152.799 101.614 116.696 1.00 75.16  ?  722  TYR   A CE1   1 
ATOM   5766  C  CE2   . TYR   A 1 722 ? 153.645 100.162 114.999 1.00 77.18  ?  722  TYR   A CE2   1 
ATOM   5767  C  CZ    . TYR   A 1 722 ? 153.308 100.394 116.313 1.00 77.86  ?  722  TYR   A CZ    1 
ATOM   5768  O  OH    . TYR   A 1 722 ? 153.478 99.404  117.251 1.00 77.97  ?  722  TYR   A OH    1 
ATOM   5769  N  N     . LYS   A 1 723 ? 155.753 103.596 112.286 1.00 72.37  ?  723  LYS   A N     1 
ATOM   5770  C  CA    . LYS   A 1 723 ? 157.004 102.850 112.176 1.00 75.28  ?  723  LYS   A CA    1 
ATOM   5771  C  C     . LYS   A 1 723 ? 158.174 103.630 112.763 1.00 78.86  ?  723  LYS   A C     1 
ATOM   5772  O  O     . LYS   A 1 723 ? 159.082 103.044 113.365 1.00 85.33  ?  723  LYS   A O     1 
ATOM   5773  C  CB    . LYS   A 1 723 ? 157.269 102.494 110.712 1.00 78.02  ?  723  LYS   A CB    1 
ATOM   5774  C  CG    . LYS   A 1 723 ? 158.737 102.364 110.343 1.00 78.64  ?  723  LYS   A CG    1 
ATOM   5775  C  CD    . LYS   A 1 723 ? 158.919 101.580 109.057 1.00 76.95  ?  723  LYS   A CD    1 
ATOM   5776  C  CE    . LYS   A 1 723 ? 159.060 102.508 107.864 1.00 80.59  ?  723  LYS   A CE    1 
ATOM   5777  N  NZ    . LYS   A 1 723 ? 160.241 102.159 107.027 1.00 81.73  ?  723  LYS   A NZ    1 
ATOM   5778  N  N     . PHE   A 1 724 ? 158.165 104.950 112.612 1.00 73.57  ?  724  PHE   A N     1 
ATOM   5779  C  CA    . PHE   A 1 724 ? 159.255 105.788 113.089 1.00 73.43  ?  724  PHE   A CA    1 
ATOM   5780  C  C     . PHE   A 1 724 ? 159.069 106.251 114.527 1.00 75.88  ?  724  PHE   A C     1 
ATOM   5781  O  O     . PHE   A 1 724 ? 159.883 107.040 115.018 1.00 85.05  ?  724  PHE   A O     1 
ATOM   5782  C  CB    . PHE   A 1 724 ? 159.428 106.996 112.166 1.00 75.02  ?  724  PHE   A CB    1 
ATOM   5783  C  CG    . PHE   A 1 724 ? 159.981 106.643 110.817 1.00 78.90  ?  724  PHE   A CG    1 
ATOM   5784  C  CD1   . PHE   A 1 724 ? 161.201 106.001 110.704 1.00 77.45  ?  724  PHE   A CD1   1 
ATOM   5785  C  CD2   . PHE   A 1 724 ? 159.276 106.938 109.664 1.00 79.44  ?  724  PHE   A CD2   1 
ATOM   5786  C  CE1   . PHE   A 1 724 ? 161.712 105.667 109.467 1.00 73.94  ?  724  PHE   A CE1   1 
ATOM   5787  C  CE2   . PHE   A 1 724 ? 159.782 106.605 108.423 1.00 80.53  ?  724  PHE   A CE2   1 
ATOM   5788  C  CZ    . PHE   A 1 724 ? 161.002 105.970 108.325 1.00 79.66  ?  724  PHE   A CZ    1 
ATOM   5789  N  N     . GLY   A 1 725 ? 158.029 105.786 115.212 1.00 55.92  ?  725  GLY   A N     1 
ATOM   5790  C  CA    . GLY   A 1 725 ? 157.856 106.090 116.616 1.00 53.75  ?  725  GLY   A CA    1 
ATOM   5791  C  C     . GLY   A 1 725 ? 157.094 107.355 116.927 1.00 59.36  ?  725  GLY   A C     1 
ATOM   5792  O  O     . GLY   A 1 725 ? 157.190 107.852 118.055 1.00 65.67  ?  725  GLY   A O     1 
ATOM   5793  N  N     . VAL   A 1 726 ? 156.346 107.901 115.969 1.00 60.91  ?  726  VAL   A N     1 
ATOM   5794  C  CA    . VAL   A 1 726 ? 155.546 109.090 116.235 1.00 59.44  ?  726  VAL   A CA    1 
ATOM   5795  C  C     . VAL   A 1 726 ? 154.437 108.737 117.216 1.00 62.55  ?  726  VAL   A C     1 
ATOM   5796  O  O     . VAL   A 1 726 ? 153.693 107.768 117.018 1.00 67.80  ?  726  VAL   A O     1 
ATOM   5797  C  CB    . VAL   A 1 726 ? 154.979 109.663 114.928 1.00 55.73  ?  726  VAL   A CB    1 
ATOM   5798  C  CG1   . VAL   A 1 726 ? 154.071 110.843 115.215 1.00 55.91  ?  726  VAL   A CG1   1 
ATOM   5799  C  CG2   . VAL   A 1 726 ? 156.108 110.069 113.997 1.00 54.18  ?  726  VAL   A CG2   1 
ATOM   5800  N  N     . LYS   A 1 727 ? 154.327 109.522 118.287 1.00 60.86  ?  727  LYS   A N     1 
ATOM   5801  C  CA    . LYS   A 1 727 ? 153.375 109.211 119.347 1.00 52.43  ?  727  LYS   A CA    1 
ATOM   5802  C  C     . LYS   A 1 727 ? 151.965 109.669 118.999 1.00 58.18  ?  727  LYS   A C     1 
ATOM   5803  O  O     . LYS   A 1 727 ? 151.001 108.924 119.206 1.00 62.02  ?  727  LYS   A O     1 
ATOM   5804  C  CB    . LYS   A 1 727 ? 153.827 109.852 120.658 1.00 53.89  ?  727  LYS   A CB    1 
ATOM   5805  C  CG    . LYS   A 1 727 ? 155.004 109.163 121.316 1.00 50.51  ?  727  LYS   A CG    1 
ATOM   5806  C  CD    . LYS   A 1 727 ? 155.346 109.828 122.635 1.00 52.50  ?  727  LYS   A CD    1 
ATOM   5807  C  CE    . LYS   A 1 727 ? 156.454 109.089 123.357 1.00 57.18  ?  727  LYS   A CE    1 
ATOM   5808  N  NZ    . LYS   A 1 727 ? 157.065 109.928 124.421 1.00 56.62  ?  727  LYS   A NZ    1 
ATOM   5809  N  N     . THR   A 1 728 ? 151.822 110.884 118.477 1.00 59.52  ?  728  THR   A N     1 
ATOM   5810  C  CA    . THR   A 1 728 ? 150.516 111.467 118.220 1.00 60.25  ?  728  THR   A CA    1 
ATOM   5811  C  C     . THR   A 1 728 ? 150.489 112.111 116.842 1.00 59.89  ?  728  THR   A C     1 
ATOM   5812  O  O     . THR   A 1 728 ? 151.521 112.530 116.314 1.00 70.49  ?  728  THR   A O     1 
ATOM   5813  C  CB    . THR   A 1 728 ? 150.147 112.514 119.281 1.00 66.69  ?  728  THR   A CB    1 
ATOM   5814  O  OG1   . THR   A 1 728 ? 151.261 113.385 119.505 1.00 70.36  ?  728  THR   A OG1   1 
ATOM   5815  C  CG2   . THR   A 1 728 ? 149.768 111.839 120.589 1.00 64.79  ?  728  THR   A CG2   1 
ATOM   5816  N  N     . LEU   A 1 729 ? 149.290 112.187 116.266 1.00 56.58  ?  729  LEU   A N     1 
ATOM   5817  C  CA    . LEU   A 1 729 ? 149.067 112.819 114.969 1.00 50.36  ?  729  LEU   A CA    1 
ATOM   5818  C  C     . LEU   A 1 729 ? 148.035 113.925 115.142 1.00 51.11  ?  729  LEU   A C     1 
ATOM   5819  O  O     . LEU   A 1 729 ? 146.869 113.651 115.445 1.00 65.75  ?  729  LEU   A O     1 
ATOM   5820  C  CB    . LEU   A 1 729 ? 148.612 111.797 113.929 1.00 46.29  ?  729  LEU   A CB    1 
ATOM   5821  C  CG    . LEU   A 1 729 ? 149.720 110.970 113.277 1.00 52.45  ?  729  LEU   A CG    1 
ATOM   5822  C  CD1   . LEU   A 1 729 ? 149.161 110.123 112.148 1.00 57.45  ?  729  LEU   A CD1   1 
ATOM   5823  C  CD2   . LEU   A 1 729 ? 150.835 111.872 112.774 1.00 52.15  ?  729  LEU   A CD2   1 
ATOM   5824  N  N     . TYR   A 1 730 ? 148.467 115.176 114.977 1.00 51.74  ?  730  TYR   A N     1 
ATOM   5825  C  CA    . TYR   A 1 730 ? 147.545 116.319 115.207 1.00 54.55  ?  730  TYR   A CA    1 
ATOM   5826  C  C     . TYR   A 1 730 ? 146.823 116.682 113.905 1.00 61.69  ?  730  TYR   A C     1 
ATOM   5827  O  O     . TYR   A 1 730 ? 146.793 115.846 112.981 1.00 70.65  ?  730  TYR   A O     1 
ATOM   5828  C  CB    . TYR   A 1 730 ? 148.314 117.509 115.786 1.00 62.25  ?  730  TYR   A CB    1 
ATOM   5829  C  CG    . TYR   A 1 730 ? 147.469 118.455 116.600 1.00 60.73  ?  730  TYR   A CG    1 
ATOM   5830  C  CD1   . TYR   A 1 730 ? 146.373 117.998 117.312 1.00 59.54  ?  730  TYR   A CD1   1 
ATOM   5831  C  CD2   . TYR   A 1 730 ? 147.754 119.808 116.642 1.00 63.82  ?  730  TYR   A CD2   1 
ATOM   5832  C  CE1   . TYR   A 1 730 ? 145.584 118.861 118.052 1.00 59.35  ?  730  TYR   A CE1   1 
ATOM   5833  C  CE2   . TYR   A 1 730 ? 146.979 120.684 117.382 1.00 62.09  ?  730  TYR   A CE2   1 
ATOM   5834  C  CZ    . TYR   A 1 730 ? 145.888 120.209 118.087 1.00 62.47  ?  730  TYR   A CZ    1 
ATOM   5835  O  OH    . TYR   A 1 730 ? 145.118 121.077 118.821 1.00 68.92  ?  730  TYR   A OH    1 
ATOM   5836  N  N     . TYR   A 1 731 ? 146.189 117.843 113.857 1.00 60.06  ?  731  TYR   A N     1 
ATOM   5837  C  CA    A TYR   A 1 731 ? 145.513 118.290 112.606 0.56 61.08  ?  731  TYR   A CA    1 
ATOM   5838  C  CA    B TYR   A 1 731 ? 145.495 118.299 112.622 0.44 61.89  ?  731  TYR   A CA    1 
ATOM   5839  C  C     . TYR   A 1 731 ? 145.853 117.712 111.197 1.00 58.21  ?  731  TYR   A C     1 
ATOM   5840  O  O     . TYR   A 1 731 ? 146.981 117.283 110.678 1.00 65.46  ?  731  TYR   A O     1 
ATOM   5841  C  CB    A TYR   A 1 731 ? 145.677 119.808 112.476 0.56 61.50  ?  731  TYR   A CB    1 
ATOM   5842  C  CB    B TYR   A 1 731 ? 145.634 119.825 112.551 0.44 62.30  ?  731  TYR   A CB    1 
ATOM   5843  C  CG    A TYR   A 1 731 ? 145.062 120.602 113.597 0.56 65.10  ?  731  TYR   A CG    1 
ATOM   5844  C  CG    B TYR   A 1 731 ? 144.631 120.505 111.657 0.44 64.76  ?  731  TYR   A CG    1 
ATOM   5845  C  CD1   A TYR   A 1 731 ? 144.012 120.090 114.340 0.56 66.88  ?  731  TYR   A CD1   1 
ATOM   5846  C  CD1   B TYR   A 1 731 ? 143.277 120.447 111.933 0.44 63.90  ?  731  TYR   A CD1   1 
ATOM   5847  C  CD2   A TYR   A 1 731 ? 145.526 121.865 113.916 0.56 61.83  ?  731  TYR   A CD2   1 
ATOM   5848  C  CD2   B TYR   A 1 731 ? 145.033 121.203 110.531 0.44 66.03  ?  731  TYR   A CD2   1 
ATOM   5849  C  CE1   A TYR   A 1 731 ? 143.448 120.809 115.378 0.56 66.36  ?  731  TYR   A CE1   1 
ATOM   5850  C  CE1   B TYR   A 1 731 ? 142.344 121.059 111.114 0.44 63.15  ?  731  TYR   A CE1   1 
ATOM   5851  C  CE2   A TYR   A 1 731 ? 144.966 122.602 114.945 0.56 61.18  ?  731  TYR   A CE2   1 
ATOM   5852  C  CE2   B TYR   A 1 731 ? 144.115 121.828 109.705 0.44 65.97  ?  731  TYR   A CE2   1 
ATOM   5853  C  CZ    A TYR   A 1 731 ? 143.921 122.072 115.678 0.56 64.80  ?  731  TYR   A CZ    1 
ATOM   5854  C  CZ    B TYR   A 1 731 ? 142.765 121.754 109.996 0.44 65.88  ?  731  TYR   A CZ    1 
ATOM   5855  O  OH    A TYR   A 1 731 ? 143.358 122.791 116.703 0.56 66.44  ?  731  TYR   A OH    1 
ATOM   5856  O  OH    B TYR   A 1 731 ? 141.850 122.371 109.179 0.44 64.05  ?  731  TYR   A OH    1 
ATOM   5857  N  N     . GLN   A 1 732 ? 144.754 117.554 110.465 1.00 61.79  ?  732  GLN   A N     1 
ATOM   5858  C  CA    . GLN   A 1 732 ? 144.959 117.082 109.068 1.00 64.21  ?  732  GLN   A CA    1 
ATOM   5859  C  C     . GLN   A 1 732 ? 144.699 118.246 108.104 1.00 68.96  ?  732  GLN   A C     1 
ATOM   5860  O  O     . GLN   A 1 732 ? 143.516 118.557 107.866 1.00 73.28  ?  732  GLN   A O     1 
ATOM   5861  C  CB    . GLN   A 1 732 ? 144.035 115.902 108.770 1.00 62.28  ?  732  GLN   A CB    1 
ATOM   5862  C  CG    . GLN   A 1 732 ? 144.647 114.891 107.814 1.00 63.48  ?  732  GLN   A CG    1 
ATOM   5863  C  CD    . GLN   A 1 732 ? 143.895 114.799 106.510 1.00 68.55  ?  732  GLN   A CD    1 
ATOM   5864  O  OE1   . GLN   A 1 732 ? 143.285 115.763 106.051 1.00 73.84  ?  732  GLN   A OE1   1 
ATOM   5865  N  NE2   . GLN   A 1 732 ? 143.937 113.627 105.898 1.00 70.07  ?  732  GLN   A NE2   1 
ATOM   5866  N  N     . ASN   A 1 733 ? 145.766 118.862 107.583 1.00 76.28  ?  733  ASN   A N     1 
ATOM   5867  C  CA    A ASN   A 1 733 ? 145.512 120.091 106.839 0.56 75.50  ?  733  ASN   A CA    1 
ATOM   5868  C  CA    B ASN   A 1 733 ? 145.500 120.087 106.844 0.44 76.30  ?  733  ASN   A CA    1 
ATOM   5869  C  C     . ASN   A 1 733 ? 145.431 119.773 105.353 1.00 80.31  ?  733  ASN   A C     1 
ATOM   5870  O  O     . ASN   A 1 733 ? 146.387 119.243 104.777 1.00 84.09  ?  733  ASN   A O     1 
ATOM   5871  C  CB    A ASN   A 1 733 ? 146.605 121.129 107.095 0.56 75.72  ?  733  ASN   A CB    1 
ATOM   5872  C  CB    B ASN   A 1 733 ? 146.576 121.130 107.152 0.44 76.51  ?  733  ASN   A CB    1 
ATOM   5873  C  CG    A ASN   A 1 733 ? 146.917 121.301 108.566 0.56 78.70  ?  733  ASN   A CG    1 
ATOM   5874  C  CG    B ASN   A 1 733 ? 146.499 122.342 106.254 0.44 78.39  ?  733  ASN   A CG    1 
ATOM   5875  O  OD1   A ASN   A 1 733 ? 146.106 120.969 109.429 0.56 80.31  ?  733  ASN   A OD1   1 
ATOM   5876  O  OD1   B ASN   A 1 733 ? 147.525 122.885 105.851 0.44 79.75  ?  733  ASN   A OD1   1 
ATOM   5877  N  ND2   A ASN   A 1 733 ? 148.100 121.826 108.860 0.56 79.53  ?  733  ASN   A ND2   1 
ATOM   5878  N  ND2   B ASN   A 1 733 ? 145.286 122.783 105.944 0.44 78.42  ?  733  ASN   A ND2   1 
ATOM   5879  N  N     . THR   A 1 734 ? 144.298 120.097 104.739 1.00 86.74  ?  734  THR   A N     1 
ATOM   5880  C  CA    . THR   A 1 734 ? 144.089 119.926 103.308 1.00 82.65  ?  734  THR   A CA    1 
ATOM   5881  C  C     . THR   A 1 734 ? 144.025 121.303 102.662 1.00 83.36  ?  734  THR   A C     1 
ATOM   5882  O  O     . THR   A 1 734 ? 143.301 122.181 103.142 1.00 89.37  ?  734  THR   A O     1 
ATOM   5883  C  CB    . THR   A 1 734 ? 142.804 119.141 103.027 1.00 85.29  ?  734  THR   A CB    1 
ATOM   5884  O  OG1   . THR   A 1 734 ? 143.057 117.738 103.167 1.00 88.88  ?  734  THR   A OG1   1 
ATOM   5885  C  CG2   . THR   A 1 734 ? 142.295 119.419 101.619 1.00 88.12  ?  734  THR   A CG2   1 
ATOM   5886  N  N     . ARG   A 1 735 ? 144.817 121.520 101.609 1.00 96.27  ?  735  ARG   A N     1 
ATOM   5887  C  CA    . ARG   A 1 735 ? 144.843 122.819 100.892 1.00 97.37  ?  735  ARG   A CA    1 
ATOM   5888  C  C     . ARG   A 1 735 ? 143.574 122.938 100.049 1.00 101.59 ?  735  ARG   A C     1 
ATOM   5889  O  O     . ARG   A 1 735 ? 143.243 121.959 99.356  1.00 103.91 ?  735  ARG   A O     1 
ATOM   5890  C  CB    . ARG   A 1 735 ? 146.043 122.965 99.959  1.00 95.94  ?  735  ARG   A CB    1 
ATOM   5891  C  CG    . ARG   A 1 735 ? 146.007 124.319 99.269  1.00 101.34 ?  735  ARG   A CG    1 
ATOM   5892  C  CD    . ARG   A 1 735 ? 147.368 124.816 98.850  1.00 101.58 ?  735  ARG   A CD    1 
ATOM   5893  N  NE    . ARG   A 1 735 ? 147.882 124.127 97.664  1.00 101.49 ?  735  ARG   A NE    1 
ATOM   5894  C  CZ    . ARG   A 1 735 ? 148.997 124.449 97.024  1.00 100.78 ?  735  ARG   A CZ    1 
ATOM   5895  N  NH1   . ARG   A 1 735 ? 149.841 125.331 97.531  1.00 101.37 ?  735  ARG   A NH1   1 
ATOM   5896  N  NH2   . ARG   A 1 735 ? 149.260 123.896 95.857  1.00 101.83 ?  735  ARG   A NH2   1 
ATOM   5897  N  N     . ASP   A 1 736 ? 142.905 124.088 100.099 1.00 121.06 ?  736  ASP   A N     1 
ATOM   5898  C  CA    . ASP   A 1 736 ? 141.633 124.306 99.364  1.00 122.96 ?  736  ASP   A CA    1 
ATOM   5899  C  C     . ASP   A 1 736 ? 141.925 124.880 97.978  1.00 125.98 ?  736  ASP   A C     1 
ATOM   5900  O  O     . ASP   A 1 736 ? 141.112 124.630 97.062  1.00 124.46 ?  736  ASP   A O     1 
ATOM   5901  C  CB    . ASP   A 1 736 ? 140.721 125.242 100.133 1.00 123.59 ?  736  ASP   A CB    1 
ATOM   5902  C  CG    . ASP   A 1 736 ? 139.456 125.666 99.403  1.00 126.49 ?  736  ASP   A CG    1 
ATOM   5903  O  OD1   . ASP   A 1 736 ? 138.645 124.777 99.072  1.00 126.24 ?  736  ASP   A OD1   1 
ATOM   5904  O  OD2   . ASP   A 1 736 ? 139.296 126.882 99.167  1.00 126.06 ?  736  ASP   A OD2   1 
ATOM   5905  N  N     . GLY   A 1 737 ? 143.029 125.612 97.823  1.00 134.13 ?  737  GLY   A N     1 
ATOM   5906  C  CA    . GLY   A 1 737 ? 143.377 126.270 96.547  1.00 133.69 ?  737  GLY   A CA    1 
ATOM   5907  C  C     . GLY   A 1 737 ? 143.097 127.749 96.638  1.00 135.36 ?  737  GLY   A C     1 
ATOM   5908  O  O     . GLY   A 1 737 ? 143.610 128.494 95.778  1.00 134.70 ?  737  GLY   A O     1 
ATOM   5909  N  N     . ALA   A 1 738 ? 142.332 128.169 97.647  1.00 151.11 ?  738  ALA   A N     1 
ATOM   5910  C  CA    . ALA   A 1 738 ? 142.054 129.599 97.895  1.00 151.47 ?  738  ALA   A CA    1 
ATOM   5911  C  C     . ALA   A 1 738 ? 143.056 130.083 98.940  1.00 151.74 ?  738  ALA   A C     1 
ATOM   5912  O  O     . ALA   A 1 738 ? 142.833 131.170 99.514  1.00 150.23 ?  738  ALA   A O     1 
ATOM   5913  C  CB    . ALA   A 1 738 ? 140.629 129.785 98.353  1.00 149.24 ?  738  ALA   A CB    1 
ATOM   5914  N  N     . GLU   A 1 739 ? 144.109 129.297 99.207  1.00 146.11 ?  739  GLU   A N     1 
ATOM   5915  C  CA    . GLU   A 1 739 ? 145.170 129.743 100.147 1.00 145.07 ?  739  GLU   A CA    1 
ATOM   5916  C  C     . GLU   A 1 739 ? 145.327 131.270 100.047 1.00 144.63 ?  739  GLU   A C     1 
ATOM   5917  O  O     . GLU   A 1 739 ? 145.816 131.730 98.991  1.00 145.45 ?  739  GLU   A O     1 
ATOM   5918  C  CB    . GLU   A 1 739 ? 146.464 128.995 99.826  1.00 144.13 ?  739  GLU   A CB    1 
ATOM   5919  C  CG    . GLU   A 1 739 ? 147.563 129.210 100.862 1.00 144.06 ?  739  GLU   A CG    1 
ATOM   5920  C  CD    . GLU   A 1 739 ? 148.878 128.530 100.530 1.00 145.24 ?  739  GLU   A CD    1 
ATOM   5921  O  OE1   . GLU   A 1 739 ? 148.963 127.881 99.466  1.00 143.54 ?  739  GLU   A OE1   1 
ATOM   5922  O  OE2   . GLU   A 1 739 ? 149.819 128.652 101.341 1.00 145.45 ?  739  GLU   A OE2   1 
ATOM   5923  N  N     . ASN   B 1 2   ? 95.702  74.041  110.441 1.00 128.07 ?  2    ASN   B N     1 
ATOM   5924  C  CA    A ASN   B 1 2   ? 96.928  73.290  110.685 0.50 130.14 ?  2    ASN   B CA    1 
ATOM   5925  C  CA    B ASN   B 1 2   ? 97.028  73.290  110.685 0.50 130.14 ?  2    ASN   B CA    1 
ATOM   5926  C  C     . ASN   B 1 2   ? 98.047  73.746  109.756 1.00 132.81 ?  2    ASN   B C     1 
ATOM   5927  O  O     . ASN   B 1 2   ? 99.039  74.324  110.204 1.00 132.65 ?  2    ASN   B O     1 
ATOM   5928  C  CB    A ASN   B 1 2   ? 96.682  71.789  110.512 0.50 131.58 ?  2    ASN   B CB    1 
ATOM   5929  C  CB    B ASN   B 1 2   ? 96.782  71.789  110.512 0.50 131.58 ?  2    ASN   B CB    1 
ATOM   5930  C  CG    A ASN   B 1 2   ? 97.969  70.988  110.476 0.50 132.81 ?  2    ASN   B CG    1 
ATOM   5931  C  CG    B ASN   B 1 2   ? 95.956  71.200  111.639 0.50 132.81 ?  2    ASN   B CG    1 
ATOM   5932  O  OD1   A ASN   B 1 2   ? 98.871  71.202  111.285 0.50 132.64 ?  2    ASN   B OD1   1 
ATOM   5933  O  OD1   B ASN   B 1 2   ? 95.906  71.748  112.740 0.50 132.64 ?  2    ASN   B OD1   1 
ATOM   5934  N  ND2   A ASN   B 1 2   ? 98.058  70.055  109.536 0.50 130.38 ?  2    ASN   B ND2   1 
ATOM   5935  N  ND2   B ASN   B 1 2   ? 95.300  70.079  111.368 0.50 130.38 ?  2    ASN   B ND2   1 
ATOM   5936  N  N     . GLN   B 1 3   ? 97.881  73.469  108.462 1.00 135.77 ?  3    GLN   B N     1 
ATOM   5937  C  CA    . GLN   B 1 3   ? 98.845  73.825  107.421 1.00 133.46 ?  3    GLN   B CA    1 
ATOM   5938  C  C     . GLN   B 1 3   ? 100.208 73.175  107.639 1.00 134.42 ?  3    GLN   B C     1 
ATOM   5939  O  O     . GLN   B 1 3   ? 101.210 73.632  107.079 1.00 133.13 ?  3    GLN   B O     1 
ATOM   5940  C  CB    . GLN   B 1 3   ? 99.001  75.346  107.301 1.00 130.25 ?  3    GLN   B CB    1 
ATOM   5941  C  CG    . GLN   B 1 3   ? 97.749  76.063  106.824 1.00 131.83 ?  3    GLN   B CG    1 
ATOM   5942  C  CD    . GLN   B 1 3   ? 96.952  76.663  107.966 1.00 133.15 ?  3    GLN   B CD    1 
ATOM   5943  O  OE1   . GLN   B 1 3   ? 97.491  76.936  109.038 1.00 133.16 ?  3    GLN   B OE1   1 
ATOM   5944  N  NE2   . GLN   B 1 3   ? 95.661  76.872  107.740 1.00 132.63 ?  3    GLN   B NE2   1 
ATOM   5945  N  N     . ASN   B 1 4   ? 100.256 72.109  108.444 1.00 131.70 ?  4    ASN   B N     1 
ATOM   5946  C  CA    . ASN   B 1 4   ? 101.497 71.394  108.751 1.00 128.57 ?  4    ASN   B CA    1 
ATOM   5947  C  C     . ASN   B 1 4   ? 102.557 72.336  109.319 1.00 127.53 ?  4    ASN   B C     1 
ATOM   5948  O  O     . ASN   B 1 4   ? 103.749 72.205  109.034 1.00 126.60 ?  4    ASN   B O     1 
ATOM   5949  C  CB    . ASN   B 1 4   ? 102.026 70.654  107.520 1.00 127.78 ?  4    ASN   B CB    1 
ATOM   5950  C  CG    . ASN   B 1 4   ? 102.955 69.511  107.880 1.00 130.05 ?  4    ASN   B CG    1 
ATOM   5951  O  OD1   . ASN   B 1 4   ? 104.173 69.618  107.740 1.00 131.80 ?  4    ASN   B OD1   1 
ATOM   5952  N  ND2   . ASN   B 1 4   ? 102.382 68.408  108.341 1.00 129.89 ?  4    ASN   B ND2   1 
ATOM   5953  N  N     . LEU   B 1 5   ? 102.119 73.295  110.129 1.00 115.75 ?  5    LEU   B N     1 
ATOM   5954  C  CA    . LEU   B 1 5   ? 103.033 74.264  110.716 1.00 114.51 ?  5    LEU   B CA    1 
ATOM   5955  C  C     . LEU   B 1 5   ? 103.747 73.675  111.921 1.00 114.10 ?  5    LEU   B C     1 
ATOM   5956  O  O     . LEU   B 1 5   ? 103.199 72.849  112.655 1.00 117.47 ?  5    LEU   B O     1 
ATOM   5957  C  CB    . LEU   B 1 5   ? 102.295 75.530  111.145 1.00 113.90 ?  5    LEU   B CB    1 
ATOM   5958  C  CG    . LEU   B 1 5   ? 101.918 76.474  110.005 1.00 113.94 ?  5    LEU   B CG    1 
ATOM   5959  C  CD1   . LEU   B 1 5   ? 101.013 77.625  110.418 1.00 110.58 ?  5    LEU   B CD1   1 
ATOM   5960  C  CD2   . LEU   B 1 5   ? 103.120 76.984  109.218 1.00 114.22 ?  5    LEU   B CD2   1 
ATOM   5961  N  N     . LEU   B 1 6   ? 104.980 74.124  112.126 1.00 101.55 ?  6    LEU   B N     1 
ATOM   5962  C  CA    . LEU   B 1 6   ? 105.825 73.653  113.211 1.00 100.60 ?  6    LEU   B CA    1 
ATOM   5963  C  C     . LEU   B 1 6   ? 106.291 74.852  114.024 1.00 104.87 ?  6    LEU   B C     1 
ATOM   5964  O  O     . LEU   B 1 6   ? 106.721 75.860  113.456 1.00 105.44 ?  6    LEU   B O     1 
ATOM   5965  C  CB    . LEU   B 1 6   ? 107.021 72.864  112.668 1.00 99.09  ?  6    LEU   B CB    1 
ATOM   5966  C  CG    . LEU   B 1 6   ? 107.013 71.354  112.909 1.00 101.55 ?  6    LEU   B CG    1 
ATOM   5967  C  CD1   . LEU   B 1 6   ? 105.971 70.681  112.044 1.00 102.53 ?  6    LEU   B CD1   1 
ATOM   5968  C  CD2   . LEU   B 1 6   ? 108.378 70.764  112.629 1.00 102.25 ?  6    LEU   B CD2   1 
ATOM   5969  N  N     . VAL   B 1 7   ? 106.193 74.746  115.345 1.00 95.97  ?  7    VAL   B N     1 
ATOM   5970  C  CA    . VAL   B 1 7   ? 106.568 75.827  116.246 1.00 92.38  ?  7    VAL   B CA    1 
ATOM   5971  C  C     . VAL   B 1 7   ? 107.889 75.489  116.922 1.00 91.57  ?  7    VAL   B C     1 
ATOM   5972  O  O     . VAL   B 1 7   ? 108.291 74.326  117.031 1.00 100.33 ?  7    VAL   B O     1 
ATOM   5973  C  CB    . VAL   B 1 7   ? 105.481 76.108  117.303 1.00 92.92  ?  7    VAL   B CB    1 
ATOM   5974  C  CG1   . VAL   B 1 7   ? 104.153 76.335  116.635 1.00 92.49  ?  7    VAL   B CG1   1 
ATOM   5975  C  CG2   . VAL   B 1 7   ? 105.390 74.954  118.289 1.00 88.71  ?  7    VAL   B CG2   1 
ATOM   5976  N  N     . THR   B 1 8   ? 108.568 76.533  117.384 1.00 76.61  ?  8    THR   B N     1 
ATOM   5977  C  CA    . THR   B 1 8   ? 109.789 76.402  118.166 1.00 80.96  ?  8    THR   B CA    1 
ATOM   5978  C  C     . THR   B 1 8   ? 109.436 76.566  119.639 1.00 85.19  ?  8    THR   B C     1 
ATOM   5979  O  O     . THR   B 1 8   ? 108.907 77.608  120.040 1.00 89.16  ?  8    THR   B O     1 
ATOM   5980  C  CB    . THR   B 1 8   ? 110.827 77.439  117.741 1.00 80.24  ?  8    THR   B CB    1 
ATOM   5981  O  OG1   . THR   B 1 8   ? 111.023 77.362  116.324 1.00 85.52  ?  8    THR   B OG1   1 
ATOM   5982  C  CG2   . THR   B 1 8   ? 112.149 77.181  118.444 1.00 77.84  ?  8    THR   B CG2   1 
ATOM   5983  N  N     . LYS   B 1 9   ? 109.727 75.544  120.438 1.00 83.46  ?  9    LYS   B N     1 
ATOM   5984  C  CA    . LYS   B 1 9   ? 109.404 75.584  121.854 1.00 78.57  ?  9    LYS   B CA    1 
ATOM   5985  C  C     . LYS   B 1 9   ? 110.426 76.427  122.614 1.00 82.73  ?  9    LYS   B C     1 
ATOM   5986  O  O     . LYS   B 1 9   ? 111.461 76.837  122.081 1.00 86.12  ?  9    LYS   B O     1 
ATOM   5987  C  CB    . LYS   B 1 9   ? 109.339 74.170  122.427 1.00 78.33  ?  9    LYS   B CB    1 
ATOM   5988  C  CG    . LYS   B 1 9   ? 108.065 73.424  122.075 1.00 76.60  ?  9    LYS   B CG    1 
ATOM   5989  C  CD    . LYS   B 1 9   ? 107.236 73.147  123.316 1.00 75.44  ?  9    LYS   B CD    1 
ATOM   5990  C  CE    . LYS   B 1 9   ? 105.764 73.013  122.982 1.00 79.70  ?  9    LYS   B CE    1 
ATOM   5991  N  NZ    . LYS   B 1 9   ? 104.899 73.286  124.159 1.00 80.79  ?  9    LYS   B NZ    1 
ATOM   5992  N  N     . ARG   B 1 10  ? 110.113 76.695  123.883 1.00 97.64  ?  10   ARG   B N     1 
ATOM   5993  C  CA    . ARG   B 1 10  ? 110.991 77.522  124.705 1.00 98.51  ?  10   ARG   B CA    1 
ATOM   5994  C  C     . ARG   B 1 10  ? 112.319 76.825  124.977 1.00 103.20 ?  10   ARG   B C     1 
ATOM   5995  O  O     . ARG   B 1 10  ? 113.374 77.470  124.984 1.00 104.66 ?  10   ARG   B O     1 
ATOM   5996  C  CB    . ARG   B 1 10  ? 110.286 77.886  126.012 1.00 97.87  ?  10   ARG   B CB    1 
ATOM   5997  C  CG    . ARG   B 1 10  ? 109.512 79.194  125.978 1.00 102.10 ?  10   ARG   B CG    1 
ATOM   5998  C  CD    . ARG   B 1 10  ? 108.906 79.514  127.332 1.00 104.88 ?  10   ARG   B CD    1 
ATOM   5999  N  NE    . ARG   B 1 10  ? 108.143 80.754  127.304 1.00 106.51 ?  10   ARG   B NE    1 
ATOM   6000  C  CZ    . ARG   B 1 10  ? 108.661 81.971  127.428 1.00 104.23 ?  10   ARG   B CZ    1 
ATOM   6001  N  NH1   . ARG   B 1 10  ? 109.959 82.163  127.588 1.00 102.39 ?  10   ARG   B NH1   1 
ATOM   6002  N  NH2   . ARG   B 1 10  ? 107.858 83.025  127.341 1.00 101.80 ?  10   ARG   B NH2   1 
ATOM   6003  N  N     . ASP   B 1 11  ? 112.292 75.510  125.185 1.00 108.73 ?  11   ASP   B N     1 
ATOM   6004  C  CA    . ASP   B 1 11  ? 113.513 74.753  125.456 1.00 107.22 ?  11   ASP   B CA    1 
ATOM   6005  C  C     . ASP   B 1 11  ? 114.384 74.557  124.224 1.00 105.49 ?  11   ASP   B C     1 
ATOM   6006  O  O     . ASP   B 1 11  ? 115.372 73.813  124.299 1.00 107.19 ?  11   ASP   B O     1 
ATOM   6007  C  CB    . ASP   B 1 11  ? 113.162 73.393  126.064 1.00 108.67 ?  11   ASP   B CB    1 
ATOM   6008  C  CG    . ASP   B 1 11  ? 112.089 72.658  125.280 1.00 110.81 ?  11   ASP   B CG    1 
ATOM   6009  O  OD1   . ASP   B 1 11  ? 111.921 72.942  124.076 1.00 107.72 ?  11   ASP   B OD1   1 
ATOM   6010  O  OD2   . ASP   B 1 11  ? 111.414 71.789  125.870 1.00 113.08 ?  11   ASP   B OD2   1 
ATOM   6011  N  N     . GLY   B 1 12  ? 114.068 75.188  123.096 1.00 99.28  ?  12   GLY   B N     1 
ATOM   6012  C  CA    . GLY   B 1 12  ? 114.816 75.015  121.877 1.00 100.76 ?  12   GLY   B CA    1 
ATOM   6013  C  C     . GLY   B 1 12  ? 114.297 73.929  120.963 1.00 103.85 ?  12   GLY   B C     1 
ATOM   6014  O  O     . GLY   B 1 12  ? 114.761 73.826  119.823 1.00 102.85 ?  12   GLY   B O     1 
ATOM   6015  N  N     . SER   B 1 13  ? 113.433 73.051  121.465 1.00 102.41 ?  13   SER   B N     1 
ATOM   6016  C  CA    . SER   B 1 13  ? 112.906 71.960  120.666 1.00 99.93  ?  13   SER   B CA    1 
ATOM   6017  C  C     . SER   B 1 13  ? 111.837 72.481  119.715 1.00 98.54  ?  13   SER   B C     1 
ATOM   6018  O  O     . SER   B 1 13  ? 111.326 73.593  119.860 1.00 100.61 ?  13   SER   B O     1 
ATOM   6019  C  CB    . SER   B 1 13  ? 112.328 70.861  121.557 1.00 101.21 ?  13   SER   B CB    1 
ATOM   6020  O  OG    . SER   B 1 13  ? 111.284 70.167  120.894 1.00 101.90 ?  13   SER   B OG    1 
ATOM   6021  N  N     . THR   B 1 14  ? 111.494 71.656  118.732 1.00 95.81  ?  14   THR   B N     1 
ATOM   6022  C  CA    . THR   B 1 14  ? 110.504 72.002  117.723 1.00 96.38  ?  14   THR   B CA    1 
ATOM   6023  C  C     . THR   B 1 14  ? 109.347 71.017  117.801 1.00 94.31  ?  14   THR   B C     1 
ATOM   6024  O  O     . THR   B 1 14  ? 109.560 69.801  117.803 1.00 97.15  ?  14   THR   B O     1 
ATOM   6025  C  CB    . THR   B 1 14  ? 111.121 72.006  116.323 1.00 95.70  ?  14   THR   B CB    1 
ATOM   6026  O  OG1   . THR   B 1 14  ? 112.015 73.119  116.208 1.00 97.71  ?  14   THR   B OG1   1 
ATOM   6027  C  CG2   . THR   B 1 14  ? 110.038 72.161  115.293 1.00 94.30  ?  14   THR   B CG2   1 
ATOM   6028  N  N     . GLU   B 1 15  ? 108.129 71.546  117.868 1.00 94.65  ?  15   GLU   B N     1 
ATOM   6029  C  CA    . GLU   B 1 15  ? 106.914 70.755  117.992 1.00 94.88  ?  15   GLU   B CA    1 
ATOM   6030  C  C     . GLU   B 1 15  ? 105.979 71.072  116.832 1.00 97.68  ?  15   GLU   B C     1 
ATOM   6031  O  O     . GLU   B 1 15  ? 106.235 71.966  116.026 1.00 99.56  ?  15   GLU   B O     1 
ATOM   6032  C  CB    . GLU   B 1 15  ? 106.216 71.027  119.333 1.00 98.45  ?  15   GLU   B CB    1 
ATOM   6033  C  CG    . GLU   B 1 15  ? 105.387 69.865  119.867 1.00 98.24  ?  15   GLU   B CG    1 
ATOM   6034  C  CD    . GLU   B 1 15  ? 104.934 70.091  121.295 1.00 100.58 ?  15   GLU   B CD    1 
ATOM   6035  O  OE1   . GLU   B 1 15  ? 103.914 70.782  121.499 1.00 101.88 ?  15   GLU   B OE1   1 
ATOM   6036  O  OE2   . GLU   B 1 15  ? 105.633 69.627  122.220 1.00 100.93 ?  15   GLU   B OE2   1 
ATOM   6037  N  N     . ARG   B 1 16  ? 104.882 70.327  116.751 1.00 104.07 ?  16   ARG   B N     1 
ATOM   6038  C  CA    . ARG   B 1 16  ? 103.856 70.580  115.752 1.00 103.57 ?  16   ARG   B CA    1 
ATOM   6039  C  C     . ARG   B 1 16  ? 102.835 71.580  116.281 1.00 105.71 ?  16   ARG   B C     1 
ATOM   6040  O  O     . ARG   B 1 16  ? 102.614 71.689  117.491 1.00 109.72 ?  16   ARG   B O     1 
ATOM   6041  C  CB    . ARG   B 1 16  ? 103.156 69.279  115.356 1.00 104.60 ?  16   ARG   B CB    1 
ATOM   6042  C  CG    . ARG   B 1 16  ? 102.872 69.147  113.868 1.00 104.51 ?  16   ARG   B CG    1 
ATOM   6043  C  CD    . ARG   B 1 16  ? 102.428 67.735  113.513 1.00 106.59 ?  16   ARG   B CD    1 
ATOM   6044  N  NE    . ARG   B 1 16  ? 101.156 67.390  114.136 1.00 111.11 ?  16   ARG   B NE    1 
ATOM   6045  C  CZ    . ARG   B 1 16  ? 100.064 67.041  113.469 1.00 110.32 ?  16   ARG   B CZ    1 
ATOM   6046  N  NH1   . ARG   B 1 16  ? 100.055 66.972  112.148 1.00 107.69 ?  16   ARG   B NH1   1 
ATOM   6047  N  NH2   . ARG   B 1 16  ? 98.959  66.742  114.145 1.00 106.65 ?  16   ARG   B NH2   1 
ATOM   6048  N  N     . ILE   B 1 17  ? 102.214 72.316  115.355 1.00 95.63  ?  17   ILE   B N     1 
ATOM   6049  C  CA    . ILE   B 1 17  ? 101.158 73.250  115.727 1.00 94.02  ?  17   ILE   B CA    1 
ATOM   6050  C  C     . ILE   B 1 17  ? 100.014 72.490  116.387 1.00 96.77  ?  17   ILE   B C     1 
ATOM   6051  O  O     . ILE   B 1 17  ? 99.718  71.338  116.043 1.00 100.68 ?  17   ILE   B O     1 
ATOM   6052  C  CB    . ILE   B 1 17  ? 100.682 74.043  114.496 1.00 94.27  ?  17   ILE   B CB    1 
ATOM   6053  C  CG1   . ILE   B 1 17  ? 100.007 75.355  114.908 1.00 93.31  ?  17   ILE   B CG1   1 
ATOM   6054  C  CG2   . ILE   B 1 17  ? 99.734  73.218  113.638 1.00 97.30  ?  17   ILE   B CG2   1 
ATOM   6055  C  CD1   . ILE   B 1 17  ? 100.785 76.176  115.898 1.00 95.86  ?  17   ILE   B CD1   1 
ATOM   6056  N  N     . ASN   B 1 18  ? 99.386  73.127  117.374 1.00 94.05  ?  18   ASN   B N     1 
ATOM   6057  C  CA    . ASN   B 1 18  ? 98.266  72.526  118.095 1.00 93.28  ?  18   ASN   B CA    1 
ATOM   6058  C  C     . ASN   B 1 18  ? 97.392  73.678  118.584 1.00 95.58  ?  18   ASN   B C     1 
ATOM   6059  O  O     . ASN   B 1 18  ? 97.691  74.295  119.610 1.00 103.53 ?  18   ASN   B O     1 
ATOM   6060  C  CB    . ASN   B 1 18  ? 98.755  71.650  119.241 1.00 93.35  ?  18   ASN   B CB    1 
ATOM   6061  C  CG    . ASN   B 1 18  ? 97.619  71.042  120.047 1.00 95.92  ?  18   ASN   B CG    1 
ATOM   6062  O  OD1   . ASN   B 1 18  ? 96.448  71.147  119.684 1.00 99.01  ?  18   ASN   B OD1   1 
ATOM   6063  N  ND2   . ASN   B 1 18  ? 97.962  70.448  121.182 1.00 94.56  ?  18   ASN   B ND2   1 
ATOM   6064  N  N     . LEU   B 1 19  ? 96.321  73.958  117.841 1.00 86.30  ?  19   LEU   B N     1 
ATOM   6065  C  CA    . LEU   B 1 19  ? 95.434  75.064  118.176 1.00 90.45  ?  19   LEU   B CA    1 
ATOM   6066  C  C     . LEU   B 1 19  ? 94.673  74.827  119.474 1.00 93.72  ?  19   LEU   B C     1 
ATOM   6067  O  O     . LEU   B 1 19  ? 94.205  75.792  120.092 1.00 97.51  ?  19   LEU   B O     1 
ATOM   6068  C  CB    . LEU   B 1 19  ? 94.452  75.303  117.028 1.00 92.35  ?  19   LEU   B CB    1 
ATOM   6069  C  CG    . LEU   B 1 19  ? 95.033  75.832  115.715 1.00 91.27  ?  19   LEU   B CG    1 
ATOM   6070  C  CD1   . LEU   B 1 19  ? 93.991  76.641  114.967 1.00 91.77  ?  19   LEU   B CD1   1 
ATOM   6071  C  CD2   . LEU   B 1 19  ? 96.279  76.667  115.959 1.00 88.57  ?  19   LEU   B CD2   1 
ATOM   6072  N  N     . ASP   B 1 20  ? 94.542  73.568  119.898 1.00 98.14  ?  20   ASP   B N     1 
ATOM   6073  C  CA    . ASP   B 1 20  ? 93.797  73.267  121.115 1.00 96.33  ?  20   ASP   B CA    1 
ATOM   6074  C  C     . ASP   B 1 20  ? 94.479  73.855  122.343 1.00 96.86  ?  20   ASP   B C     1 
ATOM   6075  O  O     . ASP   B 1 20  ? 93.805  74.291  123.280 1.00 99.62  ?  20   ASP   B O     1 
ATOM   6076  C  CB    . ASP   B 1 20  ? 93.622  71.755  121.267 1.00 100.44 ?  20   ASP   B CB    1 
ATOM   6077  C  CG    . ASP   B 1 20  ? 92.559  71.199  120.338 1.00 107.91 ?  20   ASP   B CG    1 
ATOM   6078  O  OD1   . ASP   B 1 20  ? 91.641  71.961  119.965 1.00 108.23 ?  20   ASP   B OD1   1 
ATOM   6079  O  OD2   . ASP   B 1 20  ? 92.675  70.021  119.935 1.00 107.07 ?  20   ASP   B OD2   1 
ATOM   6080  N  N     . LYS   B 1 21  ? 95.814  73.875  122.361 1.00 83.98  ?  21   LYS   B N     1 
ATOM   6081  C  CA    . LYS   B 1 21  ? 96.527  74.475  123.485 1.00 86.84  ?  21   LYS   B CA    1 
ATOM   6082  C  C     . LYS   B 1 21  ? 96.268  75.976  123.571 1.00 89.92  ?  21   LYS   B C     1 
ATOM   6083  O  O     . LYS   B 1 21  ? 96.042  76.515  124.664 1.00 90.70  ?  21   LYS   B O     1 
ATOM   6084  C  CB    . LYS   B 1 21  ? 98.023  74.191  123.361 1.00 84.91  ?  21   LYS   B CB    1 
ATOM   6085  C  CG    . LYS   B 1 21  ? 98.401  72.748  123.640 1.00 86.89  ?  21   LYS   B CG    1 
ATOM   6086  C  CD    . LYS   B 1 21  ? 99.907  72.562  123.655 1.00 88.56  ?  21   LYS   B CD    1 
ATOM   6087  C  CE    . LYS   B 1 21  ? 100.278 71.090  123.604 1.00 89.74  ?  21   LYS   B CE    1 
ATOM   6088  N  NZ    . LYS   B 1 21  ? 101.742 70.895  123.425 1.00 91.27  ?  21   LYS   B NZ    1 
ATOM   6089  N  N     . ILE   B 1 22  ? 96.298  76.666  122.428 1.00 78.33  ?  22   ILE   B N     1 
ATOM   6090  C  CA    . ILE   B 1 22  ? 96.008  78.096  122.413 1.00 73.44  ?  22   ILE   B CA    1 
ATOM   6091  C  C     . ILE   B 1 22  ? 94.576  78.349  122.864 1.00 78.12  ?  22   ILE   B C     1 
ATOM   6092  O  O     . ILE   B 1 22  ? 94.305  79.282  123.632 1.00 85.24  ?  22   ILE   B O     1 
ATOM   6093  C  CB    . ILE   B 1 22  ? 96.277  78.682  121.014 1.00 73.44  ?  22   ILE   B CB    1 
ATOM   6094  C  CG1   . ILE   B 1 22  ? 97.781  78.757  120.745 1.00 76.49  ?  22   ILE   B CG1   1 
ATOM   6095  C  CG2   . ILE   B 1 22  ? 95.653  80.061  120.880 1.00 77.92  ?  22   ILE   B CG2   1 
ATOM   6096  C  CD1   . ILE   B 1 22  ? 98.137  78.694  119.277 1.00 80.19  ?  22   ILE   B CD1   1 
ATOM   6097  N  N     . HIS   B 1 23  ? 93.637  77.521  122.398 1.00 81.62  ?  23   HIS   B N     1 
ATOM   6098  C  CA    . HIS   B 1 23  ? 92.251  77.670  122.829 1.00 76.82  ?  23   HIS   B CA    1 
ATOM   6099  C  C     . HIS   B 1 23  ? 92.108  77.429  124.326 1.00 77.42  ?  23   HIS   B C     1 
ATOM   6100  O  O     . HIS   B 1 23  ? 91.318  78.102  124.995 1.00 81.04  ?  23   HIS   B O     1 
ATOM   6101  C  CB    . HIS   B 1 23  ? 91.344  76.722  122.045 1.00 79.89  ?  23   HIS   B CB    1 
ATOM   6102  C  CG    . HIS   B 1 23  ? 89.886  76.934  122.310 1.00 82.04  ?  23   HIS   B CG    1 
ATOM   6103  N  ND1   . HIS   B 1 23  ? 89.076  77.672  121.474 1.00 85.11  ?  23   HIS   B ND1   1 
ATOM   6104  C  CD2   . HIS   B 1 23  ? 89.093  76.506  123.320 1.00 80.41  ?  23   HIS   B CD2   1 
ATOM   6105  C  CE1   . HIS   B 1 23  ? 87.847  77.686  121.957 1.00 83.37  ?  23   HIS   B CE1   1 
ATOM   6106  N  NE2   . HIS   B 1 23  ? 87.838  77.016  123.094 1.00 80.31  ?  23   HIS   B NE2   1 
ATOM   6107  N  N     . ARG   B 1 24  ? 92.855  76.466  124.870 1.00 83.74  ?  24   ARG   B N     1 
ATOM   6108  C  CA    . ARG   B 1 24  ? 92.804  76.212  126.306 1.00 84.59  ?  24   ARG   B CA    1 
ATOM   6109  C  C     . ARG   B 1 24  ? 93.321  77.406  127.095 1.00 87.49  ?  24   ARG   B C     1 
ATOM   6110  O  O     . ARG   B 1 24  ? 92.728  77.794  128.109 1.00 91.35  ?  24   ARG   B O     1 
ATOM   6111  C  CB    . ARG   B 1 24  ? 93.607  74.957  126.648 1.00 83.24  ?  24   ARG   B CB    1 
ATOM   6112  C  CG    . ARG   B 1 24  ? 93.242  74.336  127.985 1.00 85.04  ?  24   ARG   B CG    1 
ATOM   6113  C  CD    . ARG   B 1 24  ? 93.869  72.963  128.146 1.00 86.22  ?  24   ARG   B CD    1 
ATOM   6114  N  NE    . ARG   B 1 24  ? 95.063  73.004  128.980 1.00 88.42  ?  24   ARG   B NE    1 
ATOM   6115  C  CZ    . ARG   B 1 24  ? 96.273  72.648  128.571 1.00 91.61  ?  24   ARG   B CZ    1 
ATOM   6116  N  NH1   . ARG   B 1 24  ? 96.488  72.218  127.338 1.00 88.68  ?  24   ARG   B NH1   1 
ATOM   6117  N  NH2   . ARG   B 1 24  ? 97.293  72.725  129.421 1.00 89.02  ?  24   ARG   B NH2   1 
ATOM   6118  N  N     . VAL   B 1 25  ? 94.424  78.005  126.644 1.00 77.67  ?  25   VAL   B N     1 
ATOM   6119  C  CA    . VAL   B 1 25  ? 94.942  79.194  127.318 1.00 74.15  ?  25   VAL   B CA    1 
ATOM   6120  C  C     . VAL   B 1 25  ? 93.925  80.329  127.252 1.00 78.33  ?  25   VAL   B C     1 
ATOM   6121  O  O     . VAL   B 1 25  ? 93.665  81.016  128.251 1.00 83.10  ?  25   VAL   B O     1 
ATOM   6122  C  CB    . VAL   B 1 25  ? 96.295  79.609  126.710 1.00 72.32  ?  25   VAL   B CB    1 
ATOM   6123  C  CG1   . VAL   B 1 25  ? 96.764  80.924  127.299 1.00 76.98  ?  25   VAL   B CG1   1 
ATOM   6124  C  CG2   . VAL   B 1 25  ? 97.341  78.524  126.903 1.00 76.38  ?  25   VAL   B CG2   1 
ATOM   6125  N  N     . LEU   B 1 26  ? 93.320  80.533  126.077 1.00 76.60  ?  26   LEU   B N     1 
ATOM   6126  C  CA    . LEU   B 1 26  ? 92.333  81.598  125.922 1.00 71.48  ?  26   LEU   B CA    1 
ATOM   6127  C  C     . LEU   B 1 26  ? 91.123  81.369  126.818 1.00 73.01  ?  26   LEU   B C     1 
ATOM   6128  O  O     . LEU   B 1 26  ? 90.605  82.312  127.425 1.00 83.69  ?  26   LEU   B O     1 
ATOM   6129  C  CB    . LEU   B 1 26  ? 91.901  81.703  124.461 1.00 73.76  ?  26   LEU   B CB    1 
ATOM   6130  C  CG    . LEU   B 1 26  ? 92.910  82.351  123.514 1.00 75.88  ?  26   LEU   B CG    1 
ATOM   6131  C  CD1   . LEU   B 1 26  ? 92.430  82.333  122.075 1.00 74.76  ?  26   LEU   B CD1   1 
ATOM   6132  C  CD2   . LEU   B 1 26  ? 93.248  83.767  123.943 1.00 73.53  ?  26   LEU   B CD2   1 
ATOM   6133  N  N     . ASP   B 1 27  ? 90.654  80.121  126.907 1.00 79.02  ?  27   ASP   B N     1 
ATOM   6134  C  CA    . ASP   B 1 27  ? 89.531  79.801  127.783 1.00 77.22  ?  27   ASP   B CA    1 
ATOM   6135  C  C     . ASP   B 1 27  ? 89.897  80.016  129.243 1.00 78.77  ?  27   ASP   B C     1 
ATOM   6136  O  O     . ASP   B 1 27  ? 89.061  80.455  130.042 1.00 86.00  ?  27   ASP   B O     1 
ATOM   6137  C  CB    . ASP   B 1 27  ? 89.070  78.359  127.559 1.00 80.67  ?  27   ASP   B CB    1 
ATOM   6138  C  CG    . ASP   B 1 27  ? 87.735  78.280  126.849 1.00 92.24  ?  27   ASP   B CG    1 
ATOM   6139  O  OD1   . ASP   B 1 27  ? 86.933  79.228  126.987 1.00 94.09  ?  27   ASP   B OD1   1 
ATOM   6140  O  OD2   . ASP   B 1 27  ? 87.538  77.331  126.060 1.00 88.25  ?  27   ASP   B OD2   1 
ATOM   6141  N  N     . TRP   B 1 28  ? 91.140  79.698  129.613 1.00 75.76  ?  28   TRP   B N     1 
ATOM   6142  C  CA    . TRP   B 1 28  ? 91.610  79.991  130.962 1.00 74.99  ?  28   TRP   B CA    1 
ATOM   6143  C  C     . TRP   B 1 28  ? 91.532  81.482  131.251 1.00 75.69  ?  28   TRP   B C     1 
ATOM   6144  O  O     . TRP   B 1 28  ? 91.109  81.893  132.338 1.00 74.98  ?  28   TRP   B O     1 
ATOM   6145  C  CB    . TRP   B 1 28  ? 93.044  79.495  131.137 1.00 77.96  ?  28   TRP   B CB    1 
ATOM   6146  C  CG    . TRP   B 1 28  ? 93.157  78.142  131.758 1.00 77.32  ?  28   TRP   B CG    1 
ATOM   6147  C  CD1   . TRP   B 1 28  ? 92.266  77.547  132.600 1.00 78.01  ?  28   TRP   B CD1   1 
ATOM   6148  C  CD2   . TRP   B 1 28  ? 94.230  77.211  131.585 1.00 74.38  ?  28   TRP   B CD2   1 
ATOM   6149  N  NE1   . TRP   B 1 28  ? 92.718  76.301  132.962 1.00 81.94  ?  28   TRP   B NE1   1 
ATOM   6150  C  CE2   . TRP   B 1 28  ? 93.922  76.072  132.351 1.00 80.03  ?  28   TRP   B CE2   1 
ATOM   6151  C  CE3   . TRP   B 1 28  ? 95.421  77.231  130.855 1.00 73.08  ?  28   TRP   B CE3   1 
ATOM   6152  C  CZ2   . TRP   B 1 28  ? 94.763  74.963  132.409 1.00 83.04  ?  28   TRP   B CZ2   1 
ATOM   6153  C  CZ3   . TRP   B 1 28  ? 96.253  76.131  130.913 1.00 77.69  ?  28   TRP   B CZ3   1 
ATOM   6154  C  CH2   . TRP   B 1 28  ? 95.921  75.013  131.684 1.00 82.53  ?  28   TRP   B CH2   1 
ATOM   6155  N  N     . ALA   B 1 29  ? 91.932  82.310  130.286 1.00 70.35  ?  29   ALA   B N     1 
ATOM   6156  C  CA    . ALA   B 1 29  ? 91.876  83.754  130.469 1.00 66.72  ?  29   ALA   B CA    1 
ATOM   6157  C  C     . ALA   B 1 29  ? 90.469  84.327  130.342 1.00 69.13  ?  29   ALA   B C     1 
ATOM   6158  O  O     . ALA   B 1 29  ? 90.266  85.497  130.680 1.00 76.84  ?  29   ALA   B O     1 
ATOM   6159  C  CB    . ALA   B 1 29  ? 92.797  84.446  129.464 1.00 67.56  ?  29   ALA   B CB    1 
ATOM   6160  N  N     . ALA   B 1 30  ? 89.498  83.544  129.875 1.00 77.95  ?  30   ALA   B N     1 
ATOM   6161  C  CA    . ALA   B 1 30  ? 88.161  84.043  129.579 1.00 74.31  ?  30   ALA   B CA    1 
ATOM   6162  C  C     . ALA   B 1 30  ? 87.144  83.737  130.672 1.00 76.65  ?  30   ALA   B C     1 
ATOM   6163  O  O     . ALA   B 1 30  ? 85.952  83.994  130.479 1.00 78.66  ?  30   ALA   B O     1 
ATOM   6164  C  CB    . ALA   B 1 30  ? 87.670  83.470  128.249 1.00 77.00  ?  30   ALA   B CB    1 
ATOM   6165  N  N     . GLU   B 1 31  ? 87.579  83.201  131.808 1.00 93.20  ?  31   GLU   B N     1 
ATOM   6166  C  CA    . GLU   B 1 31  ? 86.641  82.798  132.847 1.00 95.61  ?  31   GLU   B CA    1 
ATOM   6167  C  C     . GLU   B 1 31  ? 85.980  84.016  133.481 1.00 97.15  ?  31   GLU   B C     1 
ATOM   6168  O  O     . GLU   B 1 31  ? 86.660  84.948  133.921 1.00 98.04  ?  31   GLU   B O     1 
ATOM   6169  C  CB    . GLU   B 1 31  ? 87.357  81.970  133.912 1.00 94.51  ?  31   GLU   B CB    1 
ATOM   6170  C  CG    . GLU   B 1 31  ? 87.145  80.472  133.779 1.00 96.98  ?  31   GLU   B CG    1 
ATOM   6171  C  CD    . GLU   B 1 31  ? 88.408  79.679  134.049 1.00 102.63 ?  31   GLU   B CD    1 
ATOM   6172  O  OE1   . GLU   B 1 31  ? 89.213  80.113  134.900 1.00 102.41 ?  31   GLU   B OE1   1 
ATOM   6173  O  OE2   . GLU   B 1 31  ? 88.597  78.624  133.409 1.00 101.04 ?  31   GLU   B OE2   1 
ATOM   6174  N  N     . GLY   B 1 32  ? 84.649  84.004  133.529 1.00 88.22  ?  32   GLY   B N     1 
ATOM   6175  C  CA    . GLY   B 1 32  ? 83.897  85.047  134.195 1.00 88.03  ?  32   GLY   B CA    1 
ATOM   6176  C  C     . GLY   B 1 32  ? 83.727  86.336  133.424 1.00 90.96  ?  32   GLY   B C     1 
ATOM   6177  O  O     . GLY   B 1 32  ? 83.236  87.316  133.995 1.00 92.32  ?  32   GLY   B O     1 
ATOM   6178  N  N     . LEU   B 1 33  ? 84.106  86.373  132.151 1.00 83.29  ?  33   LEU   B N     1 
ATOM   6179  C  CA    . LEU   B 1 33  ? 83.999  87.579  131.344 1.00 78.87  ?  33   LEU   B CA    1 
ATOM   6180  C  C     . LEU   B 1 33  ? 82.746  87.535  130.478 1.00 81.39  ?  33   LEU   B C     1 
ATOM   6181  O  O     . LEU   B 1 33  ? 82.253  86.464  130.115 1.00 84.10  ?  33   LEU   B O     1 
ATOM   6182  C  CB    . LEU   B 1 33  ? 85.237  87.759  130.464 1.00 77.50  ?  33   LEU   B CB    1 
ATOM   6183  C  CG    . LEU   B 1 33  ? 86.556  88.001  131.202 1.00 78.28  ?  33   LEU   B CG    1 
ATOM   6184  C  CD1   . LEU   B 1 33  ? 87.614  88.512  130.242 1.00 77.87  ?  33   LEU   B CD1   1 
ATOM   6185  C  CD2   . LEU   B 1 33  ? 86.360  88.971  132.357 1.00 79.10  ?  33   LEU   B CD2   1 
ATOM   6186  N  N     . HIS   B 1 34  ? 82.234  88.719  130.148 1.00 94.66  ?  34   HIS   B N     1 
ATOM   6187  C  CA    . HIS   B 1 34  ? 81.013  88.863  129.371 1.00 93.61  ?  34   HIS   B CA    1 
ATOM   6188  C  C     . HIS   B 1 34  ? 81.310  89.558  128.051 1.00 92.83  ?  34   HIS   B C     1 
ATOM   6189  O  O     . HIS   B 1 34  ? 82.208  90.401  127.961 1.00 94.84  ?  34   HIS   B O     1 
ATOM   6190  C  CB    . HIS   B 1 34  ? 79.950  89.658  130.141 1.00 93.69  ?  34   HIS   B CB    1 
ATOM   6191  C  CG    . HIS   B 1 34  ? 79.588  89.060  131.464 1.00 96.82  ?  34   HIS   B CG    1 
ATOM   6192  N  ND1   . HIS   B 1 34  ? 78.851  89.739  132.410 1.00 99.09  ?  34   HIS   B ND1   1 
ATOM   6193  C  CD2   . HIS   B 1 34  ? 79.872  87.852  132.006 1.00 96.89  ?  34   HIS   B CD2   1 
ATOM   6194  C  CE1   . HIS   B 1 34  ? 78.698  88.976  133.477 1.00 99.00  ?  34   HIS   B CE1   1 
ATOM   6195  N  NE2   . HIS   B 1 34  ? 79.265  87.808  133.237 1.00 97.98  ?  34   HIS   B NE2   1 
ATOM   6196  N  N     . ASN   B 1 35  ? 80.539  89.190  127.026 1.00 99.15  ?  35   ASN   B N     1 
ATOM   6197  C  CA    . ASN   B 1 35  ? 80.652  89.775  125.691 1.00 100.11 ?  35   ASN   B CA    1 
ATOM   6198  C  C     . ASN   B 1 35  ? 82.066  89.643  125.129 1.00 100.27 ?  35   ASN   B C     1 
ATOM   6199  O  O     . ASN   B 1 35  ? 82.541  90.525  124.412 1.00 101.18 ?  35   ASN   B O     1 
ATOM   6200  C  CB    . ASN   B 1 35  ? 80.210  91.242  125.687 1.00 100.08 ?  35   ASN   B CB    1 
ATOM   6201  C  CG    . ASN   B 1 35  ? 78.784  91.422  126.165 1.00 104.84 ?  35   ASN   B CG    1 
ATOM   6202  O  OD1   . ASN   B 1 35  ? 77.846  90.888  125.574 1.00 107.88 ?  35   ASN   B OD1   1 
ATOM   6203  N  ND2   . ASN   B 1 35  ? 78.613  92.178  127.242 1.00 104.54 ?  35   ASN   B ND2   1 
ATOM   6204  N  N     . VAL   B 1 36  ? 82.759  88.555  125.459 1.00 83.38  ?  36   VAL   B N     1 
ATOM   6205  C  CA    . VAL   B 1 36  ? 84.087  88.269  124.926 1.00 82.84  ?  36   VAL   B CA    1 
ATOM   6206  C  C     . VAL   B 1 36  ? 84.013  86.960  124.154 1.00 85.35  ?  36   VAL   B C     1 
ATOM   6207  O  O     . VAL   B 1 36  ? 83.499  85.959  124.667 1.00 87.66  ?  36   VAL   B O     1 
ATOM   6208  C  CB    . VAL   B 1 36  ? 85.157  88.192  126.034 1.00 81.02  ?  36   VAL   B CB    1 
ATOM   6209  C  CG1   . VAL   B 1 36  ? 86.318  87.302  125.603 1.00 82.47  ?  36   VAL   B CG1   1 
ATOM   6210  C  CG2   . VAL   B 1 36  ? 85.668  89.580  126.398 1.00 80.60  ?  36   VAL   B CG2   1 
ATOM   6211  N  N     . SER   B 1 37  ? 84.523  86.970  122.924 1.00 92.51  ?  37   SER   B N     1 
ATOM   6212  C  CA    . SER   B 1 37  ? 84.522  85.805  122.048 1.00 92.22  ?  37   SER   B CA    1 
ATOM   6213  C  C     . SER   B 1 37  ? 85.955  85.340  121.829 1.00 93.07  ?  37   SER   B C     1 
ATOM   6214  O  O     . SER   B 1 37  ? 86.800  86.116  121.370 1.00 92.77  ?  37   SER   B O     1 
ATOM   6215  C  CB    . SER   B 1 37  ? 83.855  86.126  120.710 1.00 93.37  ?  37   SER   B CB    1 
ATOM   6216  O  OG    . SER   B 1 37  ? 84.660  86.996  119.934 1.00 94.68  ?  37   SER   B OG    1 
ATOM   6217  N  N     . ILE   B 1 38  ? 86.224  84.076  122.159 1.00 87.96  ?  38   ILE   B N     1 
ATOM   6218  C  CA    . ILE   B 1 38  ? 87.531  83.493  121.879 1.00 86.78  ?  38   ILE   B CA    1 
ATOM   6219  C  C     . ILE   B 1 38  ? 87.745  83.374  120.376 1.00 90.23  ?  38   ILE   B C     1 
ATOM   6220  O  O     . ILE   B 1 38  ? 88.881  83.464  119.888 1.00 89.79  ?  38   ILE   B O     1 
ATOM   6221  C  CB    . ILE   B 1 38  ? 87.656  82.134  122.597 1.00 85.45  ?  38   ILE   B CB    1 
ATOM   6222  C  CG1   . ILE   B 1 38  ? 87.840  82.339  124.102 1.00 86.37  ?  38   ILE   B CG1   1 
ATOM   6223  C  CG2   . ILE   B 1 38  ? 88.804  81.309  122.038 1.00 87.84  ?  38   ILE   B CG2   1 
ATOM   6224  C  CD1   . ILE   B 1 38  ? 88.748  83.496  124.461 1.00 87.28  ?  38   ILE   B CD1   1 
ATOM   6225  N  N     . SER   B 1 39  ? 86.657  83.207  119.619 1.00 99.61  ?  39   SER   B N     1 
ATOM   6226  C  CA    . SER   B 1 39  ? 86.760  83.002  118.178 1.00 96.38  ?  39   SER   B CA    1 
ATOM   6227  C  C     . SER   B 1 39  ? 87.418  84.188  117.486 1.00 95.58  ?  39   SER   B C     1 
ATOM   6228  O  O     . SER   B 1 39  ? 88.227  84.005  116.572 1.00 97.35  ?  39   SER   B O     1 
ATOM   6229  C  CB    . SER   B 1 39  ? 85.374  82.743  117.591 1.00 97.00  ?  39   SER   B CB    1 
ATOM   6230  O  OG    . SER   B 1 39  ? 84.382  83.478  118.287 1.00 99.61  ?  39   SER   B OG    1 
ATOM   6231  N  N     . GLN   B 1 40  ? 87.076  85.413  117.895 1.00 92.41  ?  40   GLN   B N     1 
ATOM   6232  C  CA    . GLN   B 1 40  ? 87.669  86.591  117.266 1.00 92.01  ?  40   GLN   B CA    1 
ATOM   6233  C  C     . GLN   B 1 40  ? 89.170  86.667  117.528 1.00 93.93  ?  40   GLN   B C     1 
ATOM   6234  O  O     . GLN   B 1 40  ? 89.950  86.993  116.622 1.00 99.19  ?  40   GLN   B O     1 
ATOM   6235  C  CB    . GLN   B 1 40  ? 86.971  87.856  117.764 1.00 89.99  ?  40   GLN   B CB    1 
ATOM   6236  C  CG    . GLN   B 1 40  ? 85.867  88.355  116.849 1.00 93.31  ?  40   GLN   B CG    1 
ATOM   6237  C  CD    . GLN   B 1 40  ? 86.402  89.097  115.641 1.00 97.93  ?  40   GLN   B CD    1 
ATOM   6238  O  OE1   . GLN   B 1 40  ? 87.172  90.049  115.773 1.00 98.20  ?  40   GLN   B OE1   1 
ATOM   6239  N  NE2   . GLN   B 1 40  ? 85.992  88.668  114.454 1.00 96.80  ?  40   GLN   B NE2   1 
ATOM   6240  N  N     . VAL   B 1 41  ? 89.590  86.372  118.762 1.00 81.98  ?  41   VAL   B N     1 
ATOM   6241  C  CA    . VAL   B 1 41  ? 91.013  86.368  119.089 1.00 81.45  ?  41   VAL   B CA    1 
ATOM   6242  C  C     . VAL   B 1 41  ? 91.744  85.317  118.268 1.00 84.64  ?  41   VAL   B C     1 
ATOM   6243  O  O     . VAL   B 1 41  ? 92.827  85.573  117.726 1.00 88.84  ?  41   VAL   B O     1 
ATOM   6244  C  CB    . VAL   B 1 41  ? 91.215  86.151  120.600 1.00 81.72  ?  41   VAL   B CB    1 
ATOM   6245  C  CG1   . VAL   B 1 41  ? 92.611  86.589  121.006 1.00 81.40  ?  41   VAL   B CG1   1 
ATOM   6246  C  CG2   . VAL   B 1 41  ? 90.178  86.952  121.368 1.00 81.88  ?  41   VAL   B CG2   1 
ATOM   6247  N  N     . GLU   B 1 42  ? 91.164  84.120  118.162 1.00 91.44  ?  42   GLU   B N     1 
ATOM   6248  C  CA    . GLU   B 1 42  ? 91.784  83.075  117.354 1.00 86.13  ?  42   GLU   B CA    1 
ATOM   6249  C  C     . GLU   B 1 42  ? 91.868  83.489  115.891 1.00 89.09  ?  42   GLU   B C     1 
ATOM   6250  O  O     . GLU   B 1 42  ? 92.872  83.226  115.221 1.00 93.73  ?  42   GLU   B O     1 
ATOM   6251  C  CB    . GLU   B 1 42  ? 91.010  81.765  117.499 1.00 89.03  ?  42   GLU   B CB    1 
ATOM   6252  C  CG    . GLU   B 1 42  ? 90.934  81.241  118.921 1.00 92.19  ?  42   GLU   B CG    1 
ATOM   6253  C  CD    . GLU   B 1 42  ? 91.029  79.732  118.993 1.00 98.48  ?  42   GLU   B CD    1 
ATOM   6254  O  OE1   . GLU   B 1 42  ? 91.997  79.169  118.441 1.00 101.04 ?  42   GLU   B OE1   1 
ATOM   6255  O  OE2   . GLU   B 1 42  ? 90.137  79.107  119.604 1.00 99.15  ?  42   GLU   B OE2   1 
ATOM   6256  N  N     . LEU   B 1 43  ? 90.822  84.141  115.379 1.00 90.45  ?  43   LEU   B N     1 
ATOM   6257  C  CA    . LEU   B 1 43  ? 90.822  84.575  113.986 1.00 89.65  ?  43   LEU   B CA    1 
ATOM   6258  C  C     . LEU   B 1 43  ? 91.918  85.598  113.724 1.00 91.63  ?  43   LEU   B C     1 
ATOM   6259  O  O     . LEU   B 1 43  ? 92.613  85.526  112.704 1.00 95.73  ?  43   LEU   B O     1 
ATOM   6260  C  CB    . LEU   B 1 43  ? 89.454  85.151  113.620 1.00 90.04  ?  43   LEU   B CB    1 
ATOM   6261  C  CG    . LEU   B 1 43  ? 89.041  85.083  112.149 1.00 91.33  ?  43   LEU   B CG    1 
ATOM   6262  C  CD1   . LEU   B 1 43  ? 87.552  84.802  112.032 1.00 92.92  ?  43   LEU   B CD1   1 
ATOM   6263  C  CD2   . LEU   B 1 43  ? 89.401  86.368  111.416 1.00 91.48  ?  43   LEU   B CD2   1 
ATOM   6264  N  N     . ARG   B 1 44  ? 92.088  86.559  114.631 1.00 91.28  ?  44   ARG   B N     1 
ATOM   6265  C  CA    . ARG   B 1 44  ? 93.112  87.578  114.436 1.00 87.68  ?  44   ARG   B CA    1 
ATOM   6266  C  C     . ARG   B 1 44  ? 94.515  87.091  114.782 1.00 92.40  ?  44   ARG   B C     1 
ATOM   6267  O  O     . ARG   B 1 44  ? 95.488  87.759  114.415 1.00 93.27  ?  44   ARG   B O     1 
ATOM   6268  C  CB    . ARG   B 1 44  ? 92.786  88.828  115.260 1.00 87.20  ?  44   ARG   B CB    1 
ATOM   6269  C  CG    . ARG   B 1 44  ? 91.491  89.525  114.864 1.00 89.68  ?  44   ARG   B CG    1 
ATOM   6270  C  CD    . ARG   B 1 44  ? 91.583  90.108  113.469 1.00 93.26  ?  44   ARG   B CD    1 
ATOM   6271  N  NE    . ARG   B 1 44  ? 90.375  90.803  113.060 1.00 96.37  ?  44   ARG   B NE    1 
ATOM   6272  C  CZ    . ARG   B 1 44  ? 90.110  91.203  111.822 1.00 99.29  ?  44   ARG   B CZ    1 
ATOM   6273  N  NH1   . ARG   B 1 44  ? 90.948  90.977  110.820 1.00 95.65  ?  44   ARG   B NH1   1 
ATOM   6274  N  NH2   . ARG   B 1 44  ? 88.999  91.895  111.594 1.00 94.62  ?  44   ARG   B NH2   1 
ATOM   6275  N  N     . SER   B 1 45  ? 94.650  85.957  115.471 1.00 87.08  ?  45   SER   B N     1 
ATOM   6276  C  CA    . SER   B 1 45  ? 95.965  85.436  115.826 1.00 82.03  ?  45   SER   B CA    1 
ATOM   6277  C  C     . SER   B 1 45  ? 96.485  84.373  114.866 1.00 85.38  ?  45   SER   B C     1 
ATOM   6278  O  O     . SER   B 1 45  ? 97.684  84.354  114.575 1.00 91.42  ?  45   SER   B O     1 
ATOM   6279  C  CB    . SER   B 1 45  ? 95.939  84.860  117.245 1.00 82.84  ?  45   SER   B CB    1 
ATOM   6280  O  OG    . SER   B 1 45  ? 95.755  85.884  118.205 1.00 90.66  ?  45   SER   B OG    1 
ATOM   6281  N  N     . HIS   B 1 46  ? 95.616  83.486  114.367 1.00 92.55  ?  46   HIS   B N     1 
ATOM   6282  C  CA    . HIS   B 1 46  ? 96.075  82.367  113.548 1.00 93.58  ?  46   HIS   B CA    1 
ATOM   6283  C  C     . HIS   B 1 46  ? 96.665  82.831  112.223 1.00 95.90  ?  46   HIS   B C     1 
ATOM   6284  O  O     . HIS   B 1 46  ? 97.542  82.157  111.669 1.00 97.12  ?  46   HIS   B O     1 
ATOM   6285  C  CB    . HIS   B 1 46  ? 94.925  81.393  113.296 1.00 93.81  ?  46   HIS   B CB    1 
ATOM   6286  C  CG    . HIS   B 1 46  ? 94.403  80.742  114.538 1.00 97.51  ?  46   HIS   B CG    1 
ATOM   6287  N  ND1   . HIS   B 1 46  ? 95.069  80.797  115.743 1.00 98.74  ?  46   HIS   B ND1   1 
ATOM   6288  C  CD2   . HIS   B 1 46  ? 93.274  80.030  114.765 1.00 95.79  ?  46   HIS   B CD2   1 
ATOM   6289  C  CE1   . HIS   B 1 46  ? 94.377  80.141  116.657 1.00 99.39  ?  46   HIS   B CE1   1 
ATOM   6290  N  NE2   . HIS   B 1 46  ? 93.282  79.668  116.090 1.00 100.91 ?  46   HIS   B NE2   1 
ATOM   6291  N  N     . ILE   B 1 47  ? 96.200  83.967  111.698 1.00 83.14  ?  47   ILE   B N     1 
ATOM   6292  C  CA    . ILE   B 1 47  ? 96.705  84.462  110.423 1.00 81.16  ?  47   ILE   B CA    1 
ATOM   6293  C  C     . ILE   B 1 47  ? 98.175  84.852  110.510 1.00 83.66  ?  47   ILE   B C     1 
ATOM   6294  O  O     . ILE   B 1 47  ? 98.860  84.915  109.483 1.00 84.40  ?  47   ILE   B O     1 
ATOM   6295  C  CB    . ILE   B 1 47  ? 95.844  85.645  109.931 1.00 79.85  ?  47   ILE   B CB    1 
ATOM   6296  C  CG1   . ILE   B 1 47  ? 96.077  85.913  108.443 1.00 83.94  ?  47   ILE   B CG1   1 
ATOM   6297  C  CG2   . ILE   B 1 47  ? 96.109  86.914  110.754 1.00 82.13  ?  47   ILE   B CG2   1 
ATOM   6298  C  CD1   . ILE   B 1 47  ? 95.116  86.909  107.880 1.00 86.85  ?  47   ILE   B CD1   1 
ATOM   6299  N  N     . GLN   B 1 48  ? 98.687  85.097  111.713 1.00 78.35  ?  48   GLN   B N     1 
ATOM   6300  C  CA    . GLN   B 1 48  ? 100.062 85.533  111.905 1.00 74.01  ?  48   GLN   B CA    1 
ATOM   6301  C  C     . GLN   B 1 48  ? 101.015 84.394  112.241 1.00 78.53  ?  48   GLN   B C     1 
ATOM   6302  O  O     . GLN   B 1 48  ? 102.193 84.652  112.508 1.00 81.38  ?  48   GLN   B O     1 
ATOM   6303  C  CB    . GLN   B 1 48  ? 100.122 86.596  113.003 1.00 73.57  ?  48   GLN   B CB    1 
ATOM   6304  C  CG    . GLN   B 1 48  ? 99.101  87.700  112.832 1.00 78.11  ?  48   GLN   B CG    1 
ATOM   6305  C  CD    . GLN   B 1 48  ? 99.029  88.617  114.029 1.00 80.89  ?  48   GLN   B CD    1 
ATOM   6306  O  OE1   . GLN   B 1 48  ? 100.042 89.157  114.472 1.00 79.93  ?  48   GLN   B OE1   1 
ATOM   6307  N  NE2   . GLN   B 1 48  ? 97.826  88.809  114.555 1.00 80.12  ?  48   GLN   B NE2   1 
ATOM   6308  N  N     . PHE   B 1 49  ? 100.546 83.150  112.232 1.00 82.08  ?  49   PHE   B N     1 
ATOM   6309  C  CA    . PHE   B 1 49  ? 101.379 82.010  112.588 1.00 81.41  ?  49   PHE   B CA    1 
ATOM   6310  C  C     . PHE   B 1 49  ? 102.065 81.456  111.346 1.00 84.53  ?  49   PHE   B C     1 
ATOM   6311  O  O     . PHE   B 1 49  ? 101.402 81.117  110.361 1.00 89.12  ?  49   PHE   B O     1 
ATOM   6312  C  CB    . PHE   B 1 49  ? 100.547 80.918  113.262 1.00 81.12  ?  49   PHE   B CB    1 
ATOM   6313  C  CG    . PHE   B 1 49  ? 99.986  81.318  114.596 1.00 80.99  ?  49   PHE   B CG    1 
ATOM   6314  C  CD1   . PHE   B 1 49  ? 100.518 82.387  115.297 1.00 84.61  ?  49   PHE   B CD1   1 
ATOM   6315  C  CD2   . PHE   B 1 49  ? 98.927  80.622  115.151 1.00 78.85  ?  49   PHE   B CD2   1 
ATOM   6316  C  CE1   . PHE   B 1 49  ? 100.001 82.755  116.523 1.00 83.91  ?  49   PHE   B CE1   1 
ATOM   6317  C  CE2   . PHE   B 1 49  ? 98.407  80.985  116.377 1.00 80.99  ?  49   PHE   B CE2   1 
ATOM   6318  C  CZ    . PHE   B 1 49  ? 98.946  82.053  117.064 1.00 83.54  ?  49   PHE   B CZ    1 
ATOM   6319  N  N     . TYR   B 1 50  ? 103.387 81.362  111.401 1.00 87.95  ?  50   TYR   B N     1 
ATOM   6320  C  CA    . TYR   B 1 50  ? 104.202 80.844  110.312 1.00 87.59  ?  50   TYR   B CA    1 
ATOM   6321  C  C     . TYR   B 1 50  ? 104.968 79.614  110.789 1.00 92.11  ?  50   TYR   B C     1 
ATOM   6322  O  O     . TYR   B 1 50  ? 104.813 79.157  111.923 1.00 97.08  ?  50   TYR   B O     1 
ATOM   6323  C  CB    . TYR   B 1 50  ? 105.160 81.919  109.789 1.00 85.74  ?  50   TYR   B CB    1 
ATOM   6324  C  CG    . TYR   B 1 50  ? 105.914 82.654  110.874 1.00 84.40  ?  50   TYR   B CG    1 
ATOM   6325  C  CD1   . TYR   B 1 50  ? 107.137 82.187  111.334 1.00 86.22  ?  50   TYR   B CD1   1 
ATOM   6326  C  CD2   . TYR   B 1 50  ? 105.406 83.817  111.434 1.00 89.15  ?  50   TYR   B CD2   1 
ATOM   6327  C  CE1   . TYR   B 1 50  ? 107.830 82.856  112.324 1.00 89.10  ?  50   TYR   B CE1   1 
ATOM   6328  C  CE2   . TYR   B 1 50  ? 106.092 84.492  112.425 1.00 92.14  ?  50   TYR   B CE2   1 
ATOM   6329  C  CZ    . TYR   B 1 50  ? 107.303 84.007  112.866 1.00 92.19  ?  50   TYR   B CZ    1 
ATOM   6330  O  OH    . TYR   B 1 50  ? 107.989 84.677  113.853 1.00 93.05  ?  50   TYR   B OH    1 
ATOM   6331  N  N     . ASP   B 1 51  ? 105.799 79.075  109.902 1.00 104.89 ?  51   ASP   B N     1 
ATOM   6332  C  CA    . ASP   B 1 51  ? 106.616 77.919  110.240 1.00 105.58 ?  51   ASP   B CA    1 
ATOM   6333  C  C     . ASP   B 1 51  ? 107.781 78.341  111.123 1.00 108.92 ?  51   ASP   B C     1 
ATOM   6334  O  O     . ASP   B 1 51  ? 108.473 79.320  110.827 1.00 109.05 ?  51   ASP   B O     1 
ATOM   6335  C  CB    . ASP   B 1 51  ? 107.133 77.240  108.976 1.00 105.86 ?  51   ASP   B CB    1 
ATOM   6336  C  CG    . ASP   B 1 51  ? 107.643 75.840  109.236 1.00 110.23 ?  51   ASP   B CG    1 
ATOM   6337  O  OD1   . ASP   B 1 51  ? 106.981 75.096  109.988 1.00 109.56 ?  51   ASP   B OD1   1 
ATOM   6338  O  OD2   . ASP   B 1 51  ? 108.677 75.462  108.646 1.00 112.58 ?  51   ASP   B OD2   1 
ATOM   6339  N  N     . GLY   B 1 52  ? 107.999 77.600  112.205 1.00 95.21  ?  52   GLY   B N     1 
ATOM   6340  C  CA    . GLY   B 1 52  ? 109.072 77.926  113.121 1.00 91.28  ?  52   GLY   B CA    1 
ATOM   6341  C  C     . GLY   B 1 52  ? 108.792 79.074  114.059 1.00 93.01  ?  52   GLY   B C     1 
ATOM   6342  O  O     . GLY   B 1 52  ? 109.735 79.652  114.606 1.00 96.53  ?  52   GLY   B O     1 
ATOM   6343  N  N     . ILE   B 1 53  ? 107.523 79.428  114.262 1.00 82.23  ?  53   ILE   B N     1 
ATOM   6344  C  CA    . ILE   B 1 53  ? 107.187 80.537  115.145 1.00 81.07  ?  53   ILE   B CA    1 
ATOM   6345  C  C     . ILE   B 1 53  ? 107.445 80.133  116.590 1.00 84.33  ?  53   ILE   B C     1 
ATOM   6346  O  O     . ILE   B 1 53  ? 107.094 79.026  117.018 1.00 83.75  ?  53   ILE   B O     1 
ATOM   6347  C  CB    . ILE   B 1 53  ? 105.729 80.975  114.933 1.00 78.49  ?  53   ILE   B CB    1 
ATOM   6348  C  CG1   . ILE   B 1 53  ? 105.356 82.092  115.910 1.00 78.92  ?  53   ILE   B CG1   1 
ATOM   6349  C  CG2   . ILE   B 1 53  ? 104.779 79.795  115.077 1.00 78.56  ?  53   ILE   B CG2   1 
ATOM   6350  C  CD1   . ILE   B 1 53  ? 104.307 83.042  115.381 1.00 80.57  ?  53   ILE   B CD1   1 
ATOM   6351  N  N     . LYS   B 1 54  ? 108.083 81.022  117.344 1.00 79.70  ?  54   LYS   B N     1 
ATOM   6352  C  CA    . LYS   B 1 54  ? 108.328 80.773  118.756 1.00 72.56  ?  54   LYS   B CA    1 
ATOM   6353  C  C     . LYS   B 1 54  ? 107.019 80.809  119.537 1.00 73.01  ?  54   LYS   B C     1 
ATOM   6354  O  O     . LYS   B 1 54  ? 106.105 81.575  119.223 1.00 82.05  ?  54   LYS   B O     1 
ATOM   6355  C  CB    . LYS   B 1 54  ? 109.303 81.806  119.316 1.00 73.65  ?  54   LYS   B CB    1 
ATOM   6356  C  CG    . LYS   B 1 54  ? 110.695 81.737  118.714 1.00 76.16  ?  54   LYS   B CG    1 
ATOM   6357  C  CD    . LYS   B 1 54  ? 111.436 83.050  118.887 1.00 80.37  ?  54   LYS   B CD    1 
ATOM   6358  C  CE    . LYS   B 1 54  ? 112.558 82.923  119.901 1.00 83.35  ?  54   LYS   B CE    1 
ATOM   6359  N  NZ    . LYS   B 1 54  ? 113.898 83.064  119.267 1.00 85.20  ?  54   LYS   B NZ    1 
ATOM   6360  N  N     . THR   B 1 55  ? 106.931 79.959  120.564 1.00 67.81  ?  55   THR   B N     1 
ATOM   6361  C  CA    . THR   B 1 55  ? 105.741 79.944  121.410 1.00 70.99  ?  55   THR   B CA    1 
ATOM   6362  C  C     . THR   B 1 55  ? 105.584 81.252  122.174 1.00 74.45  ?  55   THR   B C     1 
ATOM   6363  O  O     . THR   B 1 55  ? 104.455 81.703  122.411 1.00 81.04  ?  55   THR   B O     1 
ATOM   6364  C  CB    . THR   B 1 55  ? 105.798 78.765  122.380 1.00 74.47  ?  55   THR   B CB    1 
ATOM   6365  O  OG1   . THR   B 1 55  ? 107.101 78.694  122.971 1.00 80.41  ?  55   THR   B OG1   1 
ATOM   6366  C  CG2   . THR   B 1 55  ? 105.506 77.464  121.652 1.00 70.65  ?  55   THR   B CG2   1 
ATOM   6367  N  N     . SER   B 1 56  ? 106.700 81.871  122.568 1.00 78.17  ?  56   SER   B N     1 
ATOM   6368  C  CA    . SER   B 1 56  ? 106.633 83.187  123.195 1.00 81.33  ?  56   SER   B CA    1 
ATOM   6369  C  C     . SER   B 1 56  ? 105.974 84.195  122.264 1.00 83.98  ?  56   SER   B C     1 
ATOM   6370  O  O     . SER   B 1 56  ? 105.143 85.002  122.698 1.00 84.28  ?  56   SER   B O     1 
ATOM   6371  C  CB    . SER   B 1 56  ? 108.032 83.658  123.588 1.00 81.92  ?  56   SER   B CB    1 
ATOM   6372  O  OG    . SER   B 1 56  ? 108.878 83.714  122.454 1.00 87.11  ?  56   SER   B OG    1 
ATOM   6373  N  N     . ASP   B 1 57  ? 106.325 84.156  120.977 1.00 84.22  ?  57   ASP   B N     1 
ATOM   6374  C  CA    . ASP   B 1 57  ? 105.689 85.045  120.014 1.00 78.01  ?  57   ASP   B CA    1 
ATOM   6375  C  C     . ASP   B 1 57  ? 104.218 84.704  119.819 1.00 76.54  ?  57   ASP   B C     1 
ATOM   6376  O  O     . ASP   B 1 57  ? 103.414 85.600  119.556 1.00 85.31  ?  57   ASP   B O     1 
ATOM   6377  C  CB    . ASP   B 1 57  ? 106.437 85.000  118.684 1.00 79.41  ?  57   ASP   B CB    1 
ATOM   6378  C  CG    . ASP   B 1 57  ? 107.780 85.698  118.754 1.00 86.84  ?  57   ASP   B CG    1 
ATOM   6379  O  OD1   . ASP   B 1 57  ? 108.159 86.141  119.859 1.00 89.24  ?  57   ASP   B OD1   1 
ATOM   6380  O  OD2   . ASP   B 1 57  ? 108.455 85.807  117.710 1.00 88.93  ?  57   ASP   B OD2   1 
ATOM   6381  N  N     . ILE   B 1 58  ? 103.841 83.431  119.955 1.00 67.96  ?  58   ILE   B N     1 
ATOM   6382  C  CA    . ILE   B 1 58  ? 102.423 83.075  119.922 1.00 65.47  ?  58   ILE   B CA    1 
ATOM   6383  C  C     . ILE   B 1 58  ? 101.688 83.734  121.082 1.00 71.91  ?  58   ILE   B C     1 
ATOM   6384  O  O     . ILE   B 1 58  ? 100.582 84.272  120.920 1.00 80.08  ?  58   ILE   B O     1 
ATOM   6385  C  CB    . ILE   B 1 58  ? 102.255 81.543  119.943 1.00 65.22  ?  58   ILE   B CB    1 
ATOM   6386  C  CG1   . ILE   B 1 58  ? 102.696 80.935  118.611 1.00 69.44  ?  58   ILE   B CG1   1 
ATOM   6387  C  CG2   . ILE   B 1 58  ? 100.816 81.162  120.249 1.00 66.08  ?  58   ILE   B CG2   1 
ATOM   6388  C  CD1   . ILE   B 1 58  ? 102.766 79.425  118.626 1.00 71.05  ?  58   ILE   B CD1   1 
ATOM   6389  N  N     . HIS   B 1 59  ? 102.289 83.698  122.274 1.00 71.76  ?  59   HIS   B N     1 
ATOM   6390  C  CA    . HIS   B 1 59  ? 101.672 84.337  123.431 1.00 70.67  ?  59   HIS   B CA    1 
ATOM   6391  C  C     . HIS   B 1 59  ? 101.556 85.845  123.233 1.00 76.51  ?  59   HIS   B C     1 
ATOM   6392  O  O     . HIS   B 1 59  ? 100.515 86.442  123.536 1.00 82.41  ?  59   HIS   B O     1 
ATOM   6393  C  CB    . HIS   B 1 59  ? 102.472 84.018  124.692 1.00 70.16  ?  59   HIS   B CB    1 
ATOM   6394  C  CG    . HIS   B 1 59  ? 101.636 83.925  125.929 1.00 74.48  ?  59   HIS   B CG    1 
ATOM   6395  N  ND1   . HIS   B 1 59  ? 101.951 83.090  126.978 1.00 78.33  ?  59   HIS   B ND1   1 
ATOM   6396  C  CD2   . HIS   B 1 59  ? 100.498 84.564  126.286 1.00 77.37  ?  59   HIS   B CD2   1 
ATOM   6397  C  CE1   . HIS   B 1 59  ? 101.043 83.218  127.928 1.00 78.55  ?  59   HIS   B CE1   1 
ATOM   6398  N  NE2   . HIS   B 1 59  ? 100.149 84.106  127.532 1.00 75.65  ?  59   HIS   B NE2   1 
ATOM   6399  N  N     . GLU   B 1 60  ? 102.614 86.477  122.719 1.00 79.69  ?  60   GLU   B N     1 
ATOM   6400  C  CA    . GLU   B 1 60  ? 102.548 87.910  122.452 1.00 77.47  ?  60   GLU   B CA    1 
ATOM   6401  C  C     . GLU   B 1 60  ? 101.480 88.227  121.414 1.00 77.75  ?  60   GLU   B C     1 
ATOM   6402  O  O     . GLU   B 1 60  ? 100.765 89.229  121.534 1.00 84.91  ?  60   GLU   B O     1 
ATOM   6403  C  CB    . GLU   B 1 60  ? 103.909 88.435  121.992 1.00 74.51  ?  60   GLU   B CB    1 
ATOM   6404  C  CG    . GLU   B 1 60  ? 104.990 88.397  123.046 1.00 81.59  ?  60   GLU   B CG    1 
ATOM   6405  C  CD    . GLU   B 1 60  ? 106.335 88.857  122.528 1.00 95.28  ?  60   GLU   B CD    1 
ATOM   6406  O  OE1   . GLU   B 1 60  ? 106.481 89.030  121.301 1.00 95.22  ?  60   GLU   B OE1   1 
ATOM   6407  O  OE2   . GLU   B 1 60  ? 107.264 89.009  123.345 1.00 96.57  ?  60   GLU   B OE2   1 
ATOM   6408  N  N     . THR   B 1 61  ? 101.354 87.378  120.391 1.00 66.13  ?  61   THR   B N     1 
ATOM   6409  C  CA    . THR   B 1 61  ? 100.355 87.592  119.352 1.00 64.93  ?  61   THR   B CA    1 
ATOM   6410  C  C     . THR   B 1 61  ? 98.945  87.528  119.921 1.00 67.74  ?  61   THR   B C     1 
ATOM   6411  O  O     . THR   B 1 61  ? 98.108  88.388  119.627 1.00 77.30  ?  61   THR   B O     1 
ATOM   6412  C  CB    . THR   B 1 61  ? 100.529 86.563  118.234 1.00 65.88  ?  61   THR   B CB    1 
ATOM   6413  O  OG1   . THR   B 1 61  ? 101.791 86.774  117.589 1.00 76.19  ?  61   THR   B OG1   1 
ATOM   6414  C  CG2   . THR   B 1 61  ? 99.419  86.723  117.210 1.00 66.52  ?  61   THR   B CG2   1 
ATOM   6415  N  N     . ILE   B 1 62  ? 98.660  86.514  120.740 1.00 59.12  ?  62   ILE   B N     1 
ATOM   6416  C  CA    . ILE   B 1 62  ? 97.308  86.400  121.283 1.00 51.69  ?  62   ILE   B CA    1 
ATOM   6417  C  C     . ILE   B 1 62  ? 97.026  87.537  122.259 1.00 56.96  ?  62   ILE   B C     1 
ATOM   6418  O  O     . ILE   B 1 62  ? 95.907  88.063  122.305 1.00 64.07  ?  62   ILE   B O     1 
ATOM   6419  C  CB    . ILE   B 1 62  ? 97.070  85.016  121.919 1.00 56.13  ?  62   ILE   B CB    1 
ATOM   6420  C  CG1   . ILE   B 1 62  ? 98.012  84.763  123.095 1.00 58.03  ?  62   ILE   B CG1   1 
ATOM   6421  C  CG2   . ILE   B 1 62  ? 97.205  83.918  120.874 1.00 55.06  ?  62   ILE   B CG2   1 
ATOM   6422  C  CD1   . ILE   B 1 62  ? 97.736  83.468  123.826 1.00 59.36  ?  62   ILE   B CD1   1 
ATOM   6423  N  N     . ILE   B 1 63  ? 98.035  87.961  123.029 1.00 61.71  ?  63   ILE   B N     1 
ATOM   6424  C  CA    . ILE   B 1 63  ? 97.841  89.085  123.944 1.00 55.29  ?  63   ILE   B CA    1 
ATOM   6425  C  C     . ILE   B 1 63  ? 97.520  90.356  123.167 1.00 62.13  ?  63   ILE   B C     1 
ATOM   6426  O  O     . ILE   B 1 63  ? 96.592  91.098  123.510 1.00 67.54  ?  63   ILE   B O     1 
ATOM   6427  C  CB    . ILE   B 1 63  ? 99.077  89.272  124.842 1.00 56.51  ?  63   ILE   B CB    1 
ATOM   6428  C  CG1   . ILE   B 1 63  ? 99.153  88.166  125.892 1.00 59.79  ?  63   ILE   B CG1   1 
ATOM   6429  C  CG2   . ILE   B 1 63  ? 99.043  90.633  125.519 1.00 59.98  ?  63   ILE   B CG2   1 
ATOM   6430  C  CD1   . ILE   B 1 63  ? 100.533 87.973  126.465 1.00 61.51  ?  63   ILE   B CD1   1 
ATOM   6431  N  N     . LYS   B 1 64  ? 98.284  90.625  122.104 1.00 67.89  ?  64   LYS   B N     1 
ATOM   6432  C  CA    . LYS   B 1 64  ? 98.052  91.824  121.304 1.00 61.24  ?  64   LYS   B CA    1 
ATOM   6433  C  C     . LYS   B 1 64  ? 96.698  91.774  120.606 1.00 65.09  ?  64   LYS   B C     1 
ATOM   6434  O  O     . LYS   B 1 64  ? 95.999  92.791  120.520 1.00 70.84  ?  64   LYS   B O     1 
ATOM   6435  C  CB    . LYS   B 1 64  ? 99.179  91.995  120.288 1.00 61.97  ?  64   LYS   B CB    1 
ATOM   6436  C  CG    . LYS   B 1 64  ? 99.125  93.284  119.525 1.00 70.86  ?  64   LYS   B CG    1 
ATOM   6437  C  CD    . LYS   B 1 64  ? 99.607  94.482  120.331 1.00 71.10  ?  64   LYS   B CD    1 
ATOM   6438  C  CE    . LYS   B 1 64  ? 98.829  95.725  119.940 1.00 71.95  ?  64   LYS   B CE    1 
ATOM   6439  N  NZ    . LYS   B 1 64  ? 98.979  96.052  118.495 1.00 73.54  ?  64   LYS   B NZ    1 
ATOM   6440  N  N     . ALA   B 1 65  ? 96.312  90.600  120.099 1.00 63.84  ?  65   ALA   B N     1 
ATOM   6441  C  CA    . ALA   B 1 65  ? 95.015  90.459  119.445 1.00 65.79  ?  65   ALA   B CA    1 
ATOM   6442  C  C     . ALA   B 1 65  ? 93.875  90.695  120.424 1.00 67.97  ?  65   ALA   B C     1 
ATOM   6443  O  O     . ALA   B 1 65  ? 92.879  91.343  120.083 1.00 74.87  ?  65   ALA   B O     1 
ATOM   6444  C  CB    . ALA   B 1 65  ? 94.902  89.079  118.804 1.00 61.96  ?  65   ALA   B CB    1 
ATOM   6445  N  N     . ALA   B 1 66  ? 94.005  90.185  121.650 1.00 63.15  ?  66   ALA   B N     1 
ATOM   6446  C  CA    . ALA   B 1 66  ? 92.998  90.452  122.670 1.00 55.51  ?  66   ALA   B CA    1 
ATOM   6447  C  C     . ALA   B 1 66  ? 92.957  91.929  123.038 1.00 57.61  ?  66   ALA   B C     1 
ATOM   6448  O  O     . ALA   B 1 66  ? 91.874  92.495  123.224 1.00 65.16  ?  66   ALA   B O     1 
ATOM   6449  C  CB    . ALA   B 1 66  ? 93.269  89.599  123.903 1.00 53.44  ?  66   ALA   B CB    1 
ATOM   6450  N  N     . ALA   B 1 67  ? 94.124  92.568  123.143 1.00 62.01  ?  67   ALA   B N     1 
ATOM   6451  C  CA    . ALA   B 1 67  ? 94.177  93.968  123.545 1.00 63.30  ?  67   ALA   B CA    1 
ATOM   6452  C  C     . ALA   B 1 67  ? 93.610  94.889  122.475 1.00 68.50  ?  67   ALA   B C     1 
ATOM   6453  O  O     . ALA   B 1 67  ? 93.038  95.933  122.805 1.00 73.15  ?  67   ALA   B O     1 
ATOM   6454  C  CB    . ALA   B 1 67  ? 95.613  94.355  123.882 1.00 58.77  ?  67   ALA   B CB    1 
ATOM   6455  N  N     . ASP   B 1 68  ? 93.755  94.526  121.199 1.00 71.08  ?  68   ASP   B N     1 
ATOM   6456  C  CA    . ASP   B 1 68  ? 93.196  95.335  120.123 1.00 64.64  ?  68   ASP   B CA    1 
ATOM   6457  C  C     . ASP   B 1 68  ? 91.675  95.317  120.104 1.00 66.47  ?  68   ASP   B C     1 
ATOM   6458  O  O     . ASP   B 1 68  ? 91.075  96.152  119.420 1.00 73.55  ?  68   ASP   B O     1 
ATOM   6459  C  CB    . ASP   B 1 68  ? 93.733  94.862  118.770 1.00 70.82  ?  68   ASP   B CB    1 
ATOM   6460  C  CG    . ASP   B 1 68  ? 95.181  95.241  118.558 1.00 77.87  ?  68   ASP   B CG    1 
ATOM   6461  O  OD1   . ASP   B 1 68  ? 95.666  96.122  119.298 1.00 76.25  ?  68   ASP   B OD1   1 
ATOM   6462  O  OD2   . ASP   B 1 68  ? 95.842  94.627  117.695 1.00 79.44  ?  68   ASP   B OD2   1 
ATOM   6463  N  N     . LEU   B 1 69  ? 91.042  94.401  120.833 1.00 66.39  ?  69   LEU   B N     1 
ATOM   6464  C  CA    . LEU   B 1 69  ? 89.591  94.292  120.865 1.00 65.10  ?  69   LEU   B CA    1 
ATOM   6465  C  C     . LEU   B 1 69  ? 88.957  95.071  122.009 1.00 65.44  ?  69   LEU   B C     1 
ATOM   6466  O  O     . LEU   B 1 69  ? 87.734  95.016  122.171 1.00 74.60  ?  69   LEU   B O     1 
ATOM   6467  C  CB    . LEU   B 1 69  ? 89.178  92.821  120.957 1.00 66.58  ?  69   LEU   B CB    1 
ATOM   6468  C  CG    . LEU   B 1 69  ? 89.385  91.996  119.687 1.00 68.88  ?  69   LEU   B CG    1 
ATOM   6469  C  CD1   . LEU   B 1 69  ? 88.962  90.554  119.908 1.00 68.87  ?  69   LEU   B CD1   1 
ATOM   6470  C  CD2   . LEU   B 1 69  ? 88.625  92.610  118.525 1.00 69.38  ?  69   LEU   B CD2   1 
ATOM   6471  N  N     . ILE   B 1 70  ? 89.748  95.788  122.805 1.00 63.60  ?  70   ILE   B N     1 
ATOM   6472  C  CA    . ILE   B 1 70  ? 89.195  96.574  123.902 1.00 61.87  ?  70   ILE   B CA    1 
ATOM   6473  C  C     . ILE   B 1 70  ? 88.449  97.767  123.320 1.00 66.55  ?  70   ILE   B C     1 
ATOM   6474  O  O     . ILE   B 1 70  ? 89.023  98.580  122.586 1.00 71.23  ?  70   ILE   B O     1 
ATOM   6475  C  CB    . ILE   B 1 70  ? 90.299  97.024  124.867 1.00 66.28  ?  70   ILE   B CB    1 
ATOM   6476  C  CG1   . ILE   B 1 70  ? 90.896  95.820  125.595 1.00 64.46  ?  70   ILE   B CG1   1 
ATOM   6477  C  CG2   . ILE   B 1 70  ? 89.754  98.031  125.864 1.00 65.47  ?  70   ILE   B CG2   1 
ATOM   6478  C  CD1   . ILE   B 1 70  ? 92.334  96.013  126.015 1.00 60.06  ?  70   ILE   B CD1   1 
ATOM   6479  N  N     . SER   B 1 71  ? 87.166  97.880  123.649 1.00 71.63  ?  71   SER   B N     1 
ATOM   6480  C  CA    . SER   B 1 71  ? 86.318  98.928  123.096 1.00 73.60  ?  71   SER   B CA    1 
ATOM   6481  C  C     . SER   B 1 71  ? 85.155  99.160  124.051 1.00 77.96  ?  71   SER   B C     1 
ATOM   6482  O  O     . SER   B 1 71  ? 85.000  98.462  125.056 1.00 79.63  ?  71   SER   B O     1 
ATOM   6483  C  CB    . SER   B 1 71  ? 85.819  98.562  121.697 1.00 73.81  ?  71   SER   B CB    1 
ATOM   6484  O  OG    . SER   B 1 71  ? 85.545  97.176  121.621 1.00 77.22  ?  71   SER   B OG    1 
ATOM   6485  N  N     . ARG   B 1 72  ? 84.335  100.157 123.723 1.00 84.98  ?  72   ARG   B N     1 
ATOM   6486  C  CA    . ARG   B 1 72  ? 83.156  100.441 124.531 1.00 81.24  ?  72   ARG   B CA    1 
ATOM   6487  C  C     . ARG   B 1 72  ? 82.116  99.335  124.415 1.00 84.65  ?  72   ARG   B C     1 
ATOM   6488  O  O     . ARG   B 1 72  ? 81.352  99.103  125.358 1.00 87.06  ?  72   ARG   B O     1 
ATOM   6489  C  CB    . ARG   B 1 72  ? 82.555  101.783 124.119 1.00 79.72  ?  72   ARG   B CB    1 
ATOM   6490  C  CG    . ARG   B 1 72  ? 83.584  102.867 123.863 1.00 83.72  ?  72   ARG   B CG    1 
ATOM   6491  C  CD    . ARG   B 1 72  ? 82.925  104.157 123.414 1.00 84.17  ?  72   ARG   B CD    1 
ATOM   6492  N  NE    . ARG   B 1 72  ? 81.590  104.307 123.979 1.00 88.90  ?  72   ARG   B NE    1 
ATOM   6493  C  CZ    . ARG   B 1 72  ? 80.789  105.337 123.744 1.00 90.40  ?  72   ARG   B CZ    1 
ATOM   6494  N  NH1   . ARG   B 1 72  ? 81.156  106.331 122.952 1.00 87.05  ?  72   ARG   B NH1   1 
ATOM   6495  N  NH2   . ARG   B 1 72  ? 79.589  105.369 124.315 1.00 90.25  ?  72   ARG   B NH2   1 
ATOM   6496  N  N     . ASP   B 1 73  ? 82.124  98.597  123.327 1.00 89.32  ?  73   ASP   B N     1 
ATOM   6497  C  CA    . ASP   B 1 73  ? 81.079  97.566  123.178 1.00 87.96  ?  73   ASP   B CA    1 
ATOM   6498  C  C     . ASP   B 1 73  ? 81.449  96.339  123.990 1.00 90.34  ?  73   ASP   B C     1 
ATOM   6499  O  O     . ASP   B 1 73  ? 80.579  95.751  124.607 1.00 93.28  ?  73   ASP   B O     1 
ATOM   6500  C  CB    . ASP   B 1 73  ? 80.970  97.133  121.754 1.00 89.25  ?  73   ASP   B CB    1 
ATOM   6501  C  CG    . ASP   B 1 73  ? 81.074  98.286  120.770 1.00 96.33  ?  73   ASP   B CG    1 
ATOM   6502  O  OD1   . ASP   B 1 73  ? 82.135  98.947  120.756 1.00 97.84  ?  73   ASP   B OD1   1 
ATOM   6503  O  OD2   . ASP   B 1 73  ? 80.084  98.535  120.052 1.00 95.90  ?  73   ASP   B OD2   1 
ATOM   6504  N  N     . ALA   B 1 74  ? 82.717  96.000  124.002 1.00 79.45  ?  74   ALA   B N     1 
ATOM   6505  C  CA    . ALA   B 1 74  ? 83.184  94.853  124.779 1.00 78.67  ?  74   ALA   B CA    1 
ATOM   6506  C  C     . ALA   B 1 74  ? 84.356  95.281  125.652 1.00 80.35  ?  74   ALA   B C     1 
ATOM   6507  O  O     . ALA   B 1 74  ? 85.514  94.955  125.366 1.00 85.49  ?  74   ALA   B O     1 
ATOM   6508  C  CB    . ALA   B 1 74  ? 83.575  93.693  123.863 1.00 76.74  ?  74   ALA   B CB    1 
ATOM   6509  N  N     . PRO   B 1 75  ? 84.089  96.025  126.729 1.00 76.40  ?  75   PRO   B N     1 
ATOM   6510  C  CA    . PRO   B 1 75  ? 85.183  96.449  127.615 1.00 75.76  ?  75   PRO   B CA    1 
ATOM   6511  C  C     . PRO   B 1 75  ? 85.852  95.303  128.358 1.00 76.95  ?  75   PRO   B C     1 
ATOM   6512  O  O     . PRO   B 1 75  ? 87.006  95.452  128.781 1.00 78.13  ?  75   PRO   B O     1 
ATOM   6513  C  CB    . PRO   B 1 75  ? 84.480  97.404  128.584 1.00 73.69  ?  75   PRO   B CB    1 
ATOM   6514  C  CG    . PRO   B 1 75  ? 83.113  96.813  128.670 1.00 73.38  ?  75   PRO   B CG    1 
ATOM   6515  C  CD    . PRO   B 1 75  ? 82.793  96.506  127.232 1.00 75.08  ?  75   PRO   B CD    1 
ATOM   6516  N  N     . ASP   B 1 76  ? 85.177  94.160  128.516 1.00 76.30  ?  76   ASP   B N     1 
ATOM   6517  C  CA    . ASP   B 1 76  ? 85.728  93.068  129.310 1.00 74.38  ?  76   ASP   B CA    1 
ATOM   6518  C  C     . ASP   B 1 76  ? 86.997  92.488  128.702 1.00 75.32  ?  76   ASP   B C     1 
ATOM   6519  O  O     . ASP   B 1 76  ? 87.736  91.783  129.398 1.00 81.24  ?  76   ASP   B O     1 
ATOM   6520  C  CB    . ASP   B 1 76  ? 84.683  91.967  129.489 1.00 79.38  ?  76   ASP   B CB    1 
ATOM   6521  C  CG    . ASP   B 1 76  ? 84.032  92.002  130.857 1.00 85.75  ?  76   ASP   B CG    1 
ATOM   6522  O  OD1   . ASP   B 1 76  ? 83.988  93.091  131.466 1.00 88.24  ?  76   ASP   B OD1   1 
ATOM   6523  O  OD2   . ASP   B 1 76  ? 83.569  90.943  131.327 1.00 87.63  ?  76   ASP   B OD2   1 
ATOM   6524  N  N     . TYR   B 1 77  ? 87.270  92.772  127.426 1.00 63.61  ?  77   TYR   B N     1 
ATOM   6525  C  CA    . TYR   B 1 77  ? 88.536  92.353  126.836 1.00 62.63  ?  77   TYR   B CA    1 
ATOM   6526  C  C     . TYR   B 1 77  ? 89.718  92.915  127.612 1.00 67.63  ?  77   TYR   B C     1 
ATOM   6527  O  O     . TYR   B 1 77  ? 90.785  92.290  127.653 1.00 75.34  ?  77   TYR   B O     1 
ATOM   6528  C  CB    . TYR   B 1 77  ? 88.606  92.786  125.371 1.00 64.81  ?  77   TYR   B CB    1 
ATOM   6529  C  CG    . TYR   B 1 77  ? 87.938  91.821  124.421 1.00 68.50  ?  77   TYR   B CG    1 
ATOM   6530  C  CD1   . TYR   B 1 77  ? 88.433  90.538  124.242 1.00 67.96  ?  77   TYR   B CD1   1 
ATOM   6531  C  CD2   . TYR   B 1 77  ? 86.808  92.191  123.707 1.00 67.36  ?  77   TYR   B CD2   1 
ATOM   6532  C  CE1   . TYR   B 1 77  ? 87.823  89.652  123.377 1.00 68.25  ?  77   TYR   B CE1   1 
ATOM   6533  C  CE2   . TYR   B 1 77  ? 86.192  91.312  122.841 1.00 64.36  ?  77   TYR   B CE2   1 
ATOM   6534  C  CZ    . TYR   B 1 77  ? 86.703  90.044  122.679 1.00 66.95  ?  77   TYR   B CZ    1 
ATOM   6535  O  OH    . TYR   B 1 77  ? 86.091  89.166  121.816 1.00 74.05  ?  77   TYR   B OH    1 
ATOM   6536  N  N     . GLN   B 1 78  ? 89.532  94.067  128.265 1.00 64.85  ?  78   GLN   B N     1 
ATOM   6537  C  CA    . GLN   B 1 78  ? 90.599  94.654  129.069 1.00 60.71  ?  78   GLN   B CA    1 
ATOM   6538  C  C     . GLN   B 1 78  ? 91.081  93.692  130.145 1.00 66.53  ?  78   GLN   B C     1 
ATOM   6539  O  O     . GLN   B 1 78  ? 92.228  93.790  130.595 1.00 76.58  ?  78   GLN   B O     1 
ATOM   6540  C  CB    . GLN   B 1 78  ? 90.123  95.963  129.700 1.00 61.05  ?  78   GLN   B CB    1 
ATOM   6541  C  CG    . GLN   B 1 78  ? 89.244  95.780  130.929 1.00 62.57  ?  78   GLN   B CG    1 
ATOM   6542  C  CD    . GLN   B 1 78  ? 89.043  97.064  131.705 1.00 68.10  ?  78   GLN   B CD    1 
ATOM   6543  O  OE1   . GLN   B 1 78  ? 89.547  98.119  131.323 1.00 70.59  ?  78   GLN   B OE1   1 
ATOM   6544  N  NE2   . GLN   B 1 78  ? 88.306  96.980  132.804 1.00 69.34  ?  78   GLN   B NE2   1 
ATOM   6545  N  N     . TYR   B 1 79  ? 90.230  92.759  130.567 1.00 67.71  ?  79   TYR   B N     1 
ATOM   6546  C  CA    . TYR   B 1 79  ? 90.658  91.733  131.504 1.00 61.08  ?  79   TYR   B CA    1 
ATOM   6547  C  C     . TYR   B 1 79  ? 91.266  90.532  130.795 1.00 63.17  ?  79   TYR   B C     1 
ATOM   6548  O  O     . TYR   B 1 79  ? 92.263  89.977  131.269 1.00 77.40  ?  79   TYR   B O     1 
ATOM   6549  C  CB    . TYR   B 1 79  ? 89.480  91.296  132.374 1.00 57.48  ?  79   TYR   B CB    1 
ATOM   6550  C  CG    . TYR   B 1 79  ? 88.938  92.406  133.241 1.00 64.86  ?  79   TYR   B CG    1 
ATOM   6551  C  CD1   . TYR   B 1 79  ? 89.682  92.912  134.298 1.00 67.12  ?  79   TYR   B CD1   1 
ATOM   6552  C  CD2   . TYR   B 1 79  ? 87.689  92.957  132.998 1.00 64.37  ?  79   TYR   B CD2   1 
ATOM   6553  C  CE1   . TYR   B 1 79  ? 89.194  93.928  135.096 1.00 66.94  ?  79   TYR   B CE1   1 
ATOM   6554  C  CE2   . TYR   B 1 79  ? 87.196  93.976  133.786 1.00 65.67  ?  79   TYR   B CE2   1 
ATOM   6555  C  CZ    . TYR   B 1 79  ? 87.956  94.467  134.824 1.00 68.94  ?  79   TYR   B CZ    1 
ATOM   6556  O  OH    . TYR   B 1 79  ? 87.432  95.455  135.622 1.00 73.59  ?  79   TYR   B OH    1 
ATOM   6557  N  N     . LEU   B 1 80  ? 90.700  90.131  129.652 1.00 52.09  ?  80   LEU   B N     1 
ATOM   6558  C  CA    . LEU   B 1 80  ? 91.231  88.970  128.945 1.00 53.93  ?  80   LEU   B CA    1 
ATOM   6559  C  C     . LEU   B 1 80  ? 92.646  89.229  128.449 1.00 61.85  ?  80   LEU   B C     1 
ATOM   6560  O  O     . LEU   B 1 80  ? 93.517  88.358  128.552 1.00 69.27  ?  80   LEU   B O     1 
ATOM   6561  C  CB    . LEU   B 1 80  ? 90.315  88.589  127.784 1.00 56.35  ?  80   LEU   B CB    1 
ATOM   6562  C  CG    . LEU   B 1 80  ? 90.630  87.227  127.163 1.00 57.85  ?  80   LEU   B CG    1 
ATOM   6563  C  CD1   . LEU   B 1 80  ? 89.389  86.384  127.066 1.00 65.69  ?  80   LEU   B CD1   1 
ATOM   6564  C  CD2   . LEU   B 1 80  ? 91.256  87.397  125.796 1.00 59.43  ?  80   LEU   B CD2   1 
ATOM   6565  N  N     . ALA   B 1 81  ? 92.896  90.423  127.911 1.00 59.30  ?  81   ALA   B N     1 
ATOM   6566  C  CA    . ALA   B 1 81  ? 94.250  90.792  127.523 1.00 56.79  ?  81   ALA   B CA    1 
ATOM   6567  C  C     . ALA   B 1 81  ? 95.167  90.947  128.727 1.00 67.19  ?  81   ALA   B C     1 
ATOM   6568  O  O     . ALA   B 1 81  ? 96.391  90.928  128.565 1.00 72.96  ?  81   ALA   B O     1 
ATOM   6569  C  CB    . ALA   B 1 81  ? 94.234  92.086  126.712 1.00 59.60  ?  81   ALA   B CB    1 
ATOM   6570  N  N     . ALA   B 1 82  ? 94.605  91.095  129.928 1.00 66.31  ?  82   ALA   B N     1 
ATOM   6571  C  CA    . ALA   B 1 82  ? 95.429  91.234  131.120 1.00 57.36  ?  82   ALA   B CA    1 
ATOM   6572  C  C     . ALA   B 1 82  ? 95.845  89.875  131.664 1.00 59.61  ?  82   ALA   B C     1 
ATOM   6573  O  O     . ALA   B 1 82  ? 97.038  89.620  131.862 1.00 68.22  ?  82   ALA   B O     1 
ATOM   6574  C  CB    . ALA   B 1 82  ? 94.684  92.038  132.180 1.00 58.12  ?  82   ALA   B CB    1 
ATOM   6575  N  N     . ARG   B 1 83  ? 94.876  88.979  131.870 1.00 55.82  ?  83   ARG   B N     1 
ATOM   6576  C  CA    . ARG   B 1 83  ? 95.180  87.655  132.400 1.00 55.47  ?  83   ARG   B CA    1 
ATOM   6577  C  C     . ARG   B 1 83  ? 96.145  86.908  131.492 1.00 60.07  ?  83   ARG   B C     1 
ATOM   6578  O  O     . ARG   B 1 83  ? 97.092  86.274  131.973 1.00 71.85  ?  83   ARG   B O     1 
ATOM   6579  C  CB    . ARG   B 1 83  ? 93.888  86.864  132.589 1.00 50.05  ?  83   ARG   B CB    1 
ATOM   6580  C  CG    . ARG   B 1 83  ? 92.972  87.457  133.640 1.00 57.57  ?  83   ARG   B CG    1 
ATOM   6581  C  CD    . ARG   B 1 83  ? 91.539  87.002  133.458 1.00 58.06  ?  83   ARG   B CD    1 
ATOM   6582  N  NE    . ARG   B 1 83  ? 90.655  87.635  134.428 1.00 63.31  ?  83   ARG   B NE    1 
ATOM   6583  C  CZ    . ARG   B 1 83  ? 89.371  87.343  134.576 1.00 66.94  ?  83   ARG   B CZ    1 
ATOM   6584  N  NH1   . ARG   B 1 83  ? 88.778  86.432  133.823 1.00 63.69  ?  83   ARG   B NH1   1 
ATOM   6585  N  NH2   . ARG   B 1 83  ? 88.662  87.988  135.497 1.00 64.04  ?  83   ARG   B NH2   1 
ATOM   6586  N  N     . LEU   B 1 84  ? 95.932  86.984  130.176 1.00 57.25  ?  84   LEU   B N     1 
ATOM   6587  C  CA    . LEU   B 1 84  ? 96.893  86.419  129.236 1.00 54.93  ?  84   LEU   B CA    1 
ATOM   6588  C  C     . LEU   B 1 84  ? 98.286  86.974  129.495 1.00 59.45  ?  84   LEU   B C     1 
ATOM   6589  O  O     . LEU   B 1 84  ? 99.260  86.220  129.604 1.00 66.76  ?  84   LEU   B O     1 
ATOM   6590  C  CB    . LEU   B 1 84  ? 96.462  86.713  127.799 1.00 58.07  ?  84   LEU   B CB    1 
ATOM   6591  C  CG    . LEU   B 1 84  ? 95.321  85.883  127.216 1.00 58.93  ?  84   LEU   B CG    1 
ATOM   6592  C  CD1   . LEU   B 1 84  ? 94.879  86.447  125.879 1.00 59.77  ?  84   LEU   B CD1   1 
ATOM   6593  C  CD2   . LEU   B 1 84  ? 95.724  84.430  127.078 1.00 61.07  ?  84   LEU   B CD2   1 
ATOM   6594  N  N     . ALA   B 1 85  ? 98.391  88.298  129.631 1.00 63.80  ?  85   ALA   B N     1 
ATOM   6595  C  CA    . ALA   B 1 85  ? 99.684  88.902  129.929 1.00 58.12  ?  85   ALA   B CA    1 
ATOM   6596  C  C     . ALA   B 1 85  ? 100.211 88.440  131.279 1.00 62.12  ?  85   ALA   B C     1 
ATOM   6597  O  O     . ALA   B 1 85  ? 101.429 88.306  131.457 1.00 68.42  ?  85   ALA   B O     1 
ATOM   6598  C  CB    . ALA   B 1 85  ? 99.578  90.424  129.878 1.00 60.91  ?  85   ALA   B CB    1 
ATOM   6599  N  N     . ILE   B 1 86  ? 99.318  88.159  132.231 1.00 59.89  ?  86   ILE   B N     1 
ATOM   6600  C  CA    . ILE   B 1 86  ? 99.751  87.543  133.481 1.00 56.17  ?  86   ILE   B CA    1 
ATOM   6601  C  C     . ILE   B 1 86  ? 100.298 86.148  133.212 1.00 58.88  ?  86   ILE   B C     1 
ATOM   6602  O  O     . ILE   B 1 86  ? 101.370 85.779  133.709 1.00 69.89  ?  86   ILE   B O     1 
ATOM   6603  C  CB    . ILE   B 1 86  ? 98.595  87.510  134.499 1.00 58.30  ?  86   ILE   B CB    1 
ATOM   6604  C  CG1   . ILE   B 1 86  ? 98.187  88.926  134.903 1.00 59.64  ?  86   ILE   B CG1   1 
ATOM   6605  C  CG2   . ILE   B 1 86  ? 98.997  86.710  135.726 1.00 56.05  ?  86   ILE   B CG2   1 
ATOM   6606  C  CD1   . ILE   B 1 86  ? 99.308  89.713  135.549 1.00 53.76  ?  86   ILE   B CD1   1 
ATOM   6607  N  N     . PHE   B 1 87  ? 99.588  85.366  132.389 1.00 56.05  ?  87   PHE   B N     1 
ATOM   6608  C  CA    . PHE   B 1 87  ? 99.989  83.984  132.135 1.00 53.01  ?  87   PHE   B CA    1 
ATOM   6609  C  C     . PHE   B 1 87  ? 101.401 83.926  131.591 1.00 58.43  ?  87   PHE   B C     1 
ATOM   6610  O  O     . PHE   B 1 87  ? 102.185 83.039  131.954 1.00 67.59  ?  87   PHE   B O     1 
ATOM   6611  C  CB    . PHE   B 1 87  ? 99.011  83.322  131.164 1.00 55.88  ?  87   PHE   B CB    1 
ATOM   6612  C  CG    . PHE   B 1 87  ? 97.620  83.168  131.709 1.00 62.99  ?  87   PHE   B CG    1 
ATOM   6613  C  CD1   . PHE   B 1 87  ? 97.369  83.291  133.064 1.00 63.78  ?  87   PHE   B CD1   1 
ATOM   6614  C  CD2   . PHE   B 1 87  ? 96.562  82.898  130.860 1.00 62.51  ?  87   PHE   B CD2   1 
ATOM   6615  C  CE1   . PHE   B 1 87  ? 96.088  83.150  133.561 1.00 61.79  ?  87   PHE   B CE1   1 
ATOM   6616  C  CE2   . PHE   B 1 87  ? 95.281  82.754  131.352 1.00 58.89  ?  87   PHE   B CE2   1 
ATOM   6617  C  CZ    . PHE   B 1 87  ? 95.045  82.881  132.705 1.00 58.20  ?  87   PHE   B CZ    1 
ATOM   6618  N  N     . HIS   B 1 88  ? 101.775 84.962  130.850 1.00 62.46  ?  88   HIS   B N     1 
ATOM   6619  C  CA    . HIS   B 1 88  ? 103.052 84.949  130.194 1.00 63.65  ?  88   HIS   B CA    1 
ATOM   6620  C  C     . HIS   B 1 88  ? 104.101 85.342  131.175 1.00 67.98  ?  88   HIS   B C     1 
ATOM   6621  O  O     . HIS   B 1 88  ? 105.191 84.817  131.107 1.00 78.27  ?  88   HIS   B O     1 
ATOM   6622  C  CB    . HIS   B 1 88  ? 103.053 85.907  129.025 1.00 64.35  ?  88   HIS   B CB    1 
ATOM   6623  C  CG    . HIS   B 1 88  ? 104.194 85.714  128.105 1.00 68.98  ?  88   HIS   B CG    1 
ATOM   6624  N  ND1   . HIS   B 1 88  ? 104.701 84.470  127.814 1.00 75.13  ?  88   HIS   B ND1   1 
ATOM   6625  C  CD2   . HIS   B 1 88  ? 104.913 86.600  127.387 1.00 70.23  ?  88   HIS   B CD2   1 
ATOM   6626  C  CE1   . HIS   B 1 88  ? 105.699 84.603  126.963 1.00 74.47  ?  88   HIS   B CE1   1 
ATOM   6627  N  NE2   . HIS   B 1 88  ? 105.851 85.885  126.692 1.00 78.09  ?  88   HIS   B NE2   1 
ATOM   6628  N  N     . LEU   B 1 89  ? 103.782 86.245  132.104 1.00 66.36  ?  89   LEU   B N     1 
ATOM   6629  C  CA    . LEU   B 1 89  ? 104.748 86.706  133.098 1.00 62.52  ?  89   LEU   B CA    1 
ATOM   6630  C  C     . LEU   B 1 89  ? 105.112 85.594  134.071 1.00 63.88  ?  89   LEU   B C     1 
ATOM   6631  O  O     . LEU   B 1 89  ? 106.294 85.367  134.355 1.00 73.48  ?  89   LEU   B O     1 
ATOM   6632  C  CB    . LEU   B 1 89  ? 104.181 87.913  133.849 1.00 59.61  ?  89   LEU   B CB    1 
ATOM   6633  C  CG    . LEU   B 1 89  ? 104.057 89.215  133.057 1.00 65.44  ?  89   LEU   B CG    1 
ATOM   6634  C  CD1   . LEU   B 1 89  ? 103.288 90.254  133.855 1.00 67.94  ?  89   LEU   B CD1   1 
ATOM   6635  C  CD2   . LEU   B 1 89  ? 105.430 89.738  132.672 1.00 68.24  ?  89   LEU   B CD2   1 
ATOM   6636  N  N     . ARG   B 1 90  ? 104.107 84.878  134.580 1.00 62.59  ?  90   ARG   B N     1 
ATOM   6637  C  CA    . ARG   B 1 90  ? 104.378 83.743  135.455 1.00 66.38  ?  90   ARG   B CA    1 
ATOM   6638  C  C     . ARG   B 1 90  ? 105.308 82.751  134.774 1.00 71.27  ?  90   ARG   B C     1 
ATOM   6639  O  O     . ARG   B 1 90  ? 106.324 82.339  135.349 1.00 80.35  ?  90   ARG   B O     1 
ATOM   6640  C  CB    . ARG   B 1 90  ? 103.068 83.068  135.859 1.00 62.69  ?  90   ARG   B CB    1 
ATOM   6641  C  CG    . ARG   B 1 90  ? 102.082 83.994  136.543 1.00 69.36  ?  90   ARG   B CG    1 
ATOM   6642  C  CD    . ARG   B 1 90  ? 102.137 83.834  138.050 1.00 67.94  ?  90   ARG   B CD    1 
ATOM   6643  N  NE    . ARG   B 1 90  ? 101.114 84.624  138.721 1.00 69.54  ?  90   ARG   B NE    1 
ATOM   6644  C  CZ    . ARG   B 1 90  ? 99.959  84.139  139.153 1.00 71.74  ?  90   ARG   B CZ    1 
ATOM   6645  N  NH1   . ARG   B 1 90  ? 99.643  82.865  138.997 1.00 69.44  ?  90   ARG   B NH1   1 
ATOM   6646  N  NH2   . ARG   B 1 90  ? 99.091  84.957  139.739 1.00 75.13  ?  90   ARG   B NH2   1 
ATOM   6647  N  N     . LYS   B 1 91  ? 105.004 82.402  133.513 1.00 68.33  ?  91   LYS   B N     1 
ATOM   6648  C  CA    . LYS   B 1 91  ? 105.865 81.465  132.803 1.00 67.12  ?  91   LYS   B CA    1 
ATOM   6649  C  C     . LYS   B 1 91  ? 107.246 82.063  132.587 1.00 70.68  ?  91   LYS   B C     1 
ATOM   6650  O  O     . LYS   B 1 91  ? 108.246 81.337  132.567 1.00 73.22  ?  91   LYS   B O     1 
ATOM   6651  C  CB    . LYS   B 1 91  ? 105.222 81.076  131.472 1.00 61.23  ?  91   LYS   B CB    1 
ATOM   6652  C  CG    . LYS   B 1 91  ? 106.121 80.277  130.546 1.00 71.24  ?  91   LYS   B CG    1 
ATOM   6653  C  CD    . LYS   B 1 91  ? 106.272 78.838  131.013 1.00 75.60  ?  91   LYS   B CD    1 
ATOM   6654  C  CE    . LYS   B 1 91  ? 104.923 78.186  131.256 1.00 74.08  ?  91   LYS   B CE    1 
ATOM   6655  N  NZ    . LYS   B 1 91  ? 105.033 76.707  131.379 1.00 73.38  ?  91   LYS   B NZ    1 
ATOM   6656  N  N     . LYS   B 1 92  ? 107.326 83.385  132.450 1.00 65.19  ?  92   LYS   B N     1 
ATOM   6657  C  CA    . LYS   B 1 92  ? 108.611 84.048  132.297 1.00 55.78  ?  92   LYS   B CA    1 
ATOM   6658  C  C     . LYS   B 1 92  ? 109.342 84.225  133.619 1.00 59.99  ?  92   LYS   B C     1 
ATOM   6659  O  O     . LYS   B 1 92  ? 110.530 84.565  133.607 1.00 70.32  ?  92   LYS   B O     1 
ATOM   6660  C  CB    . LYS   B 1 92  ? 108.421 85.410  131.629 1.00 63.00  ?  92   LYS   B CB    1 
ATOM   6661  C  CG    . LYS   B 1 92  ? 109.235 85.600  130.365 1.00 65.47  ?  92   LYS   B CG    1 
ATOM   6662  C  CD    . LYS   B 1 92  ? 109.176 87.039  129.890 1.00 70.47  ?  92   LYS   B CD    1 
ATOM   6663  C  CE    . LYS   B 1 92  ? 107.875 87.320  129.164 1.00 70.14  ?  92   LYS   B CE    1 
ATOM   6664  N  NZ    . LYS   B 1 92  ? 107.624 88.780  129.016 1.00 72.74  ?  92   LYS   B NZ    1 
ATOM   6665  N  N     . ALA   B 1 93  ? 108.674 83.999  134.749 1.00 61.39  ?  93   ALA   B N     1 
ATOM   6666  C  CA    . ALA   B 1 93  ? 109.276 84.205  136.060 1.00 57.45  ?  93   ALA   B CA    1 
ATOM   6667  C  C     . ALA   B 1 93  ? 109.605 82.914  136.788 1.00 64.02  ?  93   ALA   B C     1 
ATOM   6668  O  O     . ALA   B 1 93  ? 110.658 82.825  137.418 1.00 73.12  ?  93   ALA   B O     1 
ATOM   6669  C  CB    . ALA   B 1 93  ? 108.358 85.062  136.936 1.00 56.70  ?  93   ALA   B CB    1 
ATOM   6670  N  N     . TYR   B 1 94  ? 108.744 81.901  136.692 1.00 69.27  ?  94   TYR   B N     1 
ATOM   6671  C  CA    . TYR   B 1 94  ? 108.963 80.637  137.375 1.00 67.05  ?  94   TYR   B CA    1 
ATOM   6672  C  C     . TYR   B 1 94  ? 108.927 79.429  136.452 1.00 70.76  ?  94   TYR   B C     1 
ATOM   6673  O  O     . TYR   B 1 94  ? 109.077 78.302  136.936 1.00 77.12  ?  94   TYR   B O     1 
ATOM   6674  C  CB    . TYR   B 1 94  ? 107.921 80.446  138.486 1.00 68.91  ?  94   TYR   B CB    1 
ATOM   6675  C  CG    . TYR   B 1 94  ? 107.485 81.730  139.152 1.00 69.52  ?  94   TYR   B CG    1 
ATOM   6676  C  CD1   . TYR   B 1 94  ? 108.383 82.494  139.883 1.00 68.94  ?  94   TYR   B CD1   1 
ATOM   6677  C  CD2   . TYR   B 1 94  ? 106.174 82.175  139.055 1.00 69.49  ?  94   TYR   B CD2   1 
ATOM   6678  C  CE1   . TYR   B 1 94  ? 107.992 83.664  140.497 1.00 72.79  ?  94   TYR   B CE1   1 
ATOM   6679  C  CE2   . TYR   B 1 94  ? 105.776 83.348  139.660 1.00 69.98  ?  94   TYR   B CE2   1 
ATOM   6680  C  CZ    . TYR   B 1 94  ? 106.685 84.079  140.392 1.00 74.01  ?  94   TYR   B CZ    1 
ATOM   6681  O  OH    . TYR   B 1 94  ? 106.290 85.251  140.989 1.00 77.61  ?  94   TYR   B OH    1 
ATOM   6682  N  N     . GLY   B 1 95  ? 108.726 79.620  135.150 1.00 72.68  ?  95   GLY   B N     1 
ATOM   6683  C  CA    . GLY   B 1 95  ? 108.595 78.491  134.254 1.00 70.39  ?  95   GLY   B CA    1 
ATOM   6684  C  C     . GLY   B 1 95  ? 107.304 77.723  134.393 1.00 73.00  ?  95   GLY   B C     1 
ATOM   6685  O  O     . GLY   B 1 95  ? 107.185 76.629  133.833 1.00 81.51  ?  95   GLY   B O     1 
ATOM   6686  N  N     . GLN   B 1 96  ? 106.335 78.260  135.127 1.00 77.54  ?  96   GLN   B N     1 
ATOM   6687  C  CA    . GLN   B 1 96  ? 105.060 77.596  135.359 1.00 77.93  ?  96   GLN   B CA    1 
ATOM   6688  C  C     . GLN   B 1 96  ? 104.058 78.648  135.814 1.00 83.69  ?  96   GLN   B C     1 
ATOM   6689  O  O     . GLN   B 1 96  ? 104.398 79.821  135.993 1.00 90.11  ?  96   GLN   B O     1 
ATOM   6690  C  CB    . GLN   B 1 96  ? 105.201 76.473  136.388 1.00 76.88  ?  96   GLN   B CB    1 
ATOM   6691  C  CG    . GLN   B 1 96  ? 105.421 76.971  137.808 1.00 79.20  ?  96   GLN   B CG    1 
ATOM   6692  C  CD    . GLN   B 1 96  ? 105.983 75.902  138.718 1.00 83.35  ?  96   GLN   B CD    1 
ATOM   6693  O  OE1   . GLN   B 1 96  ? 107.154 75.537  138.615 1.00 85.85  ?  96   GLN   B OE1   1 
ATOM   6694  N  NE2   . GLN   B 1 96  ? 105.138 75.360  139.586 1.00 82.49  ?  96   GLN   B NE2   1 
ATOM   6695  N  N     . PHE   B 1 97  ? 102.812 78.217  136.010 1.00 76.13  ?  97   PHE   B N     1 
ATOM   6696  C  CA    . PHE   B 1 97  ? 101.770 79.152  136.419 1.00 73.97  ?  97   PHE   B CA    1 
ATOM   6697  C  C     . PHE   B 1 97  ? 101.791 79.400  137.922 1.00 79.61  ?  97   PHE   B C     1 
ATOM   6698  O  O     . PHE   B 1 97  ? 101.692 80.548  138.367 1.00 81.33  ?  97   PHE   B O     1 
ATOM   6699  C  CB    . PHE   B 1 97  ? 100.397 78.639  135.989 1.00 68.79  ?  97   PHE   B CB    1 
ATOM   6700  C  CG    . PHE   B 1 97  ? 99.269  79.549  136.376 1.00 69.93  ?  97   PHE   B CG    1 
ATOM   6701  C  CD1   . PHE   B 1 97  ? 99.172  80.820  135.836 1.00 73.53  ?  97   PHE   B CD1   1 
ATOM   6702  C  CD2   . PHE   B 1 97  ? 98.311  79.140  137.287 1.00 68.96  ?  97   PHE   B CD2   1 
ATOM   6703  C  CE1   . PHE   B 1 97  ? 98.138  81.662  136.191 1.00 68.64  ?  97   PHE   B CE1   1 
ATOM   6704  C  CE2   . PHE   B 1 97  ? 97.276  79.978  137.647 1.00 71.39  ?  97   PHE   B CE2   1 
ATOM   6705  C  CZ    . PHE   B 1 97  ? 97.189  81.240  137.098 1.00 70.25  ?  97   PHE   B CZ    1 
ATOM   6706  N  N     . GLU   B 1 98  ? 101.913 78.344  138.716 1.00 88.25  ?  98   GLU   B N     1 
ATOM   6707  C  CA    . GLU   B 1 98  ? 101.836 78.483  140.168 1.00 85.73  ?  98   GLU   B CA    1 
ATOM   6708  C  C     . GLU   B 1 98  ? 103.115 79.110  140.707 1.00 91.36  ?  98   GLU   B C     1 
ATOM   6709  O  O     . GLU   B 1 98  ? 104.201 78.555  140.497 1.00 92.29  ?  98   GLU   B O     1 
ATOM   6710  C  CB    . GLU   B 1 98  ? 101.599 77.127  140.821 1.00 84.77  ?  98   GLU   B CB    1 
ATOM   6711  C  CG    . GLU   B 1 98  ? 100.834 77.199  142.132 1.00 90.45  ?  98   GLU   B CG    1 
ATOM   6712  C  CD    . GLU   B 1 98  ? 101.254 76.121  143.112 1.00 98.50  ?  98   GLU   B CD    1 
ATOM   6713  O  OE1   . GLU   B 1 98  ? 101.995 75.201  142.705 1.00 97.79  ?  98   GLU   B OE1   1 
ATOM   6714  O  OE2   . GLU   B 1 98  ? 100.841 76.193  144.289 1.00 96.28  ?  98   GLU   B OE2   1 
ATOM   6715  N  N     . PRO   B 1 99  ? 103.042 80.257  141.385 1.00 78.76  ?  99   PRO   B N     1 
ATOM   6716  C  CA    . PRO   B 1 99  ? 104.253 80.848  141.950 1.00 73.19  ?  99   PRO   B CA    1 
ATOM   6717  C  C     . PRO   B 1 99  ? 104.806 79.985  143.068 1.00 73.86  ?  99   PRO   B C     1 
ATOM   6718  O  O     . PRO   B 1 99  ? 104.054 79.263  143.746 1.00 73.81  ?  99   PRO   B O     1 
ATOM   6719  C  CB    . PRO   B 1 99  ? 103.773 82.211  142.480 1.00 72.52  ?  99   PRO   B CB    1 
ATOM   6720  C  CG    . PRO   B 1 99  ? 102.432 82.435  141.903 1.00 71.54  ?  99   PRO   B CG    1 
ATOM   6721  C  CD    . PRO   B 1 99  ? 101.860 81.122  141.521 1.00 73.08  ?  99   PRO   B CD    1 
ATOM   6722  N  N     . PRO   B 1 100 ? 106.118 80.022  143.300 1.00 68.31  ?  100  PRO   B N     1 
ATOM   6723  C  CA    . PRO   B 1 100 ? 106.704 79.226  144.385 1.00 67.74  ?  100  PRO   B CA    1 
ATOM   6724  C  C     . PRO   B 1 100 ? 106.348 79.760  145.767 1.00 69.28  ?  100  PRO   B C     1 
ATOM   6725  O  O     . PRO   B 1 100 ? 105.616 80.747  145.894 1.00 77.49  ?  100  PRO   B O     1 
ATOM   6726  C  CB    . PRO   B 1 100 ? 108.205 79.349  144.104 1.00 66.78  ?  100  PRO   B CB    1 
ATOM   6727  C  CG    . PRO   B 1 100 ? 108.287 80.711  143.552 1.00 64.33  ?  100  PRO   B CG    1 
ATOM   6728  C  CD    . PRO   B 1 100 ? 107.167 80.733  142.558 1.00 65.26  ?  100  PRO   B CD    1 
ATOM   6729  N  N     . ALA   B 1 101 ? 106.852 79.107  146.810 1.00 69.18  ?  101  ALA   B N     1 
ATOM   6730  C  CA    . ALA   B 1 101 ? 106.691 79.625  148.160 1.00 67.41  ?  101  ALA   B CA    1 
ATOM   6731  C  C     . ALA   B 1 101 ? 107.439 80.944  148.307 1.00 73.92  ?  101  ALA   B C     1 
ATOM   6732  O  O     . ALA   B 1 101 ? 108.461 81.180  147.657 1.00 81.11  ?  101  ALA   B O     1 
ATOM   6733  C  CB    . ALA   B 1 101 ? 107.193 78.612  149.187 1.00 68.90  ?  101  ALA   B CB    1 
ATOM   6734  N  N     . LEU   B 1 102 ? 106.913 81.813  149.171 1.00 64.36  ?  102  LEU   B N     1 
ATOM   6735  C  CA    . LEU   B 1 102 ? 107.493 83.142  149.326 1.00 60.18  ?  102  LEU   B CA    1 
ATOM   6736  C  C     . LEU   B 1 102 ? 108.926 83.070  149.836 1.00 66.55  ?  102  LEU   B C     1 
ATOM   6737  O  O     . LEU   B 1 102 ? 109.801 83.794  149.348 1.00 73.59  ?  102  LEU   B O     1 
ATOM   6738  C  CB    . LEU   B 1 102 ? 106.631 83.982  150.267 1.00 61.95  ?  102  LEU   B CB    1 
ATOM   6739  C  CG    . LEU   B 1 102 ? 107.157 85.378  150.602 1.00 60.87  ?  102  LEU   B CG    1 
ATOM   6740  C  CD1   . LEU   B 1 102 ? 107.365 86.195  149.340 1.00 60.94  ?  102  LEU   B CD1   1 
ATOM   6741  C  CD2   . LEU   B 1 102 ? 106.210 86.087  151.549 1.00 64.34  ?  102  LEU   B CD2   1 
ATOM   6742  N  N     . TYR   B 1 103 ? 109.188 82.202  150.817 1.00 69.26  ?  103  TYR   B N     1 
ATOM   6743  C  CA    . TYR   B 1 103 ? 110.526 82.126  151.395 1.00 69.89  ?  103  TYR   B CA    1 
ATOM   6744  C  C     . TYR   B 1 103 ? 111.552 81.652  150.373 1.00 73.66  ?  103  TYR   B C     1 
ATOM   6745  O  O     . TYR   B 1 103 ? 112.650 82.213  150.282 1.00 75.06  ?  103  TYR   B O     1 
ATOM   6746  C  CB    . TYR   B 1 103 ? 110.522 81.203  152.614 1.00 74.09  ?  103  TYR   B CB    1 
ATOM   6747  C  CG    . TYR   B 1 103 ? 111.891 81.015  153.225 1.00 76.27  ?  103  TYR   B CG    1 
ATOM   6748  C  CD1   . TYR   B 1 103 ? 112.463 82.006  154.009 1.00 76.14  ?  103  TYR   B CD1   1 
ATOM   6749  C  CD2   . TYR   B 1 103 ? 112.612 79.849  153.014 1.00 73.73  ?  103  TYR   B CD2   1 
ATOM   6750  C  CE1   . TYR   B 1 103 ? 113.715 81.842  154.565 1.00 75.29  ?  103  TYR   B CE1   1 
ATOM   6751  C  CE2   . TYR   B 1 103 ? 113.868 79.679  153.562 1.00 74.27  ?  103  TYR   B CE2   1 
ATOM   6752  C  CZ    . TYR   B 1 103 ? 114.402 80.667  154.358 1.00 74.83  ?  103  TYR   B CZ    1 
ATOM   6753  O  OH    . TYR   B 1 103 ? 115.663 80.514  154.886 1.00 77.57  ?  103  TYR   B OH    1 
ATOM   6754  N  N     . ASP   B 1 104 ? 111.217 80.615  149.602 1.00 77.43  ?  104  ASP   B N     1 
ATOM   6755  C  CA    . ASP   B 1 104 ? 112.153 80.107  148.604 1.00 79.07  ?  104  ASP   B CA    1 
ATOM   6756  C  C     . ASP   B 1 104 ? 112.428 81.149  147.528 1.00 78.95  ?  104  ASP   B C     1 
ATOM   6757  O  O     . ASP   B 1 104 ? 113.577 81.326  147.104 1.00 79.02  ?  104  ASP   B O     1 
ATOM   6758  C  CB    . ASP   B 1 104 ? 111.612 78.819  147.985 1.00 75.45  ?  104  ASP   B CB    1 
ATOM   6759  C  CG    . ASP   B 1 104 ? 111.377 77.736  149.016 1.00 83.32  ?  104  ASP   B CG    1 
ATOM   6760  O  OD1   . ASP   B 1 104 ? 111.660 77.981  150.207 1.00 85.66  ?  104  ASP   B OD1   1 
ATOM   6761  O  OD2   . ASP   B 1 104 ? 110.915 76.640  148.637 1.00 84.62  ?  104  ASP   B OD2   1 
ATOM   6762  N  N     . HIS   B 1 105 ? 111.386 81.851  147.079 1.00 65.58  ?  105  HIS   B N     1 
ATOM   6763  C  CA    . HIS   B 1 105 ? 111.575 82.918  146.103 1.00 60.79  ?  105  HIS   B CA    1 
ATOM   6764  C  C     . HIS   B 1 105 ? 112.469 84.019  146.659 1.00 67.35  ?  105  HIS   B C     1 
ATOM   6765  O  O     . HIS   B 1 105 ? 113.361 84.513  145.961 1.00 74.53  ?  105  HIS   B O     1 
ATOM   6766  C  CB    . HIS   B 1 105 ? 110.219 83.488  145.678 1.00 61.53  ?  105  HIS   B CB    1 
ATOM   6767  C  CG    . HIS   B 1 105 ? 110.319 84.726  144.842 1.00 66.50  ?  105  HIS   B CG    1 
ATOM   6768  N  ND1   . HIS   B 1 105 ? 110.312 84.695  143.464 1.00 69.00  ?  105  HIS   B ND1   1 
ATOM   6769  C  CD2   . HIS   B 1 105 ? 110.418 86.030  145.188 1.00 64.02  ?  105  HIS   B CD2   1 
ATOM   6770  C  CE1   . HIS   B 1 105 ? 110.403 85.927  142.999 1.00 66.37  ?  105  HIS   B CE1   1 
ATOM   6771  N  NE2   . HIS   B 1 105 ? 110.513 86.752  144.024 1.00 63.40  ?  105  HIS   B NE2   1 
ATOM   6772  N  N     . VAL   B 1 106 ? 112.248 84.411  147.916 1.00 62.24  ?  106  VAL   B N     1 
ATOM   6773  C  CA    . VAL   B 1 106 ? 113.056 85.469  148.518 1.00 60.47  ?  106  VAL   B CA    1 
ATOM   6774  C  C     . VAL   B 1 106 ? 114.515 85.040  148.616 1.00 67.60  ?  106  VAL   B C     1 
ATOM   6775  O  O     . VAL   B 1 106 ? 115.425 85.813  148.295 1.00 70.05  ?  106  VAL   B O     1 
ATOM   6776  C  CB    . VAL   B 1 106 ? 112.485 85.865  149.893 1.00 60.66  ?  106  VAL   B CB    1 
ATOM   6777  C  CG1   . VAL   B 1 106 ? 113.502 86.675  150.679 1.00 61.31  ?  106  VAL   B CG1   1 
ATOM   6778  C  CG2   . VAL   B 1 106 ? 111.201 86.655  149.728 1.00 64.73  ?  106  VAL   B CG2   1 
ATOM   6779  N  N     . VAL   B 1 107 ? 114.762 83.803  149.055 1.00 65.98  ?  107  VAL   B N     1 
ATOM   6780  C  CA    . VAL   B 1 107 ? 116.136 83.319  149.189 1.00 67.09  ?  107  VAL   B CA    1 
ATOM   6781  C  C     . VAL   B 1 107 ? 116.818 83.267  147.829 1.00 70.86  ?  107  VAL   B C     1 
ATOM   6782  O  O     . VAL   B 1 107 ? 117.965 83.706  147.671 1.00 73.49  ?  107  VAL   B O     1 
ATOM   6783  C  CB    . VAL   B 1 107 ? 116.161 81.949  149.888 1.00 62.21  ?  107  VAL   B CB    1 
ATOM   6784  C  CG1   . VAL   B 1 107 ? 117.579 81.413  149.953 1.00 64.03  ?  107  VAL   B CG1   1 
ATOM   6785  C  CG2   . VAL   B 1 107 ? 115.627 82.089  151.299 1.00 65.23  ?  107  VAL   B CG2   1 
ATOM   6786  N  N     . LYS   B 1 108 ? 116.120 82.735  146.823 1.00 76.96  ?  108  LYS   B N     1 
ATOM   6787  C  CA    . LYS   B 1 108 ? 116.706 82.638  145.492 1.00 71.60  ?  108  LYS   B CA    1 
ATOM   6788  C  C     . LYS   B 1 108 ? 116.999 84.017  144.916 1.00 70.34  ?  108  LYS   B C     1 
ATOM   6789  O  O     . LYS   B 1 108 ? 118.037 84.223  144.278 1.00 76.94  ?  108  LYS   B O     1 
ATOM   6790  C  CB    . LYS   B 1 108 ? 115.774 81.848  144.572 1.00 71.68  ?  108  LYS   B CB    1 
ATOM   6791  C  CG    . LYS   B 1 108 ? 116.070 81.996  143.090 1.00 73.19  ?  108  LYS   B CG    1 
ATOM   6792  C  CD    . LYS   B 1 108 ? 115.118 81.156  142.258 1.00 73.90  ?  108  LYS   B CD    1 
ATOM   6793  C  CE    . LYS   B 1 108 ? 114.962 81.720  140.856 1.00 76.13  ?  108  LYS   B CE    1 
ATOM   6794  N  NZ    . LYS   B 1 108 ? 114.785 80.645  139.841 1.00 80.67  ?  108  LYS   B NZ    1 
ATOM   6795  N  N     . MET   B 1 109 ? 116.099 84.979  145.138 1.00 71.35  ?  109  MET   B N     1 
ATOM   6796  C  CA    . MET   B 1 109 ? 116.311 86.326  144.620 1.00 70.45  ?  109  MET   B CA    1 
ATOM   6797  C  C     . MET   B 1 109 ? 117.458 87.026  145.336 1.00 74.52  ?  109  MET   B C     1 
ATOM   6798  O  O     . MET   B 1 109 ? 118.236 87.753  144.708 1.00 78.95  ?  109  MET   B O     1 
ATOM   6799  C  CB    . MET   B 1 109 ? 115.027 87.145  144.747 1.00 72.83  ?  109  MET   B CB    1 
ATOM   6800  C  CG    . MET   B 1 109 ? 114.091 87.142  143.531 1.00 72.97  ?  109  MET   B CG    1 
ATOM   6801  S  SD    . MET   B 1 109 ? 114.855 87.169  141.896 1.00 91.37  ?  109  MET   B SD    1 
ATOM   6802  C  CE    . MET   B 1 109 ? 114.958 85.424  141.511 1.00 74.15  ?  109  MET   B CE    1 
ATOM   6803  N  N     . VAL   B 1 110 ? 117.569 86.835  146.652 1.00 68.64  ?  110  VAL   B N     1 
ATOM   6804  C  CA    . VAL   B 1 110 ? 118.653 87.456  147.405 1.00 68.15  ?  110  VAL   B CA    1 
ATOM   6805  C  C     . VAL   B 1 110 ? 119.994 86.857  147.000 1.00 73.08  ?  110  VAL   B C     1 
ATOM   6806  O  O     . VAL   B 1 110 ? 121.011 87.559  146.942 1.00 74.67  ?  110  VAL   B O     1 
ATOM   6807  C  CB    . VAL   B 1 110 ? 118.394 87.319  148.918 1.00 68.72  ?  110  VAL   B CB    1 
ATOM   6808  C  CG1   . VAL   B 1 110 ? 119.657 87.606  149.716 1.00 68.76  ?  110  VAL   B CG1   1 
ATOM   6809  C  CG2   . VAL   B 1 110 ? 117.273 88.250  149.348 1.00 70.31  ?  110  VAL   B CG2   1 
ATOM   6810  N  N     . GLU   B 1 111 ? 120.055 85.562  146.825 1.00 85.79  ?  111  GLU   B N     1 
ATOM   6811  C  CA    . GLU   B 1 111 ? 121.337 84.990  146.339 1.00 86.60  ?  111  GLU   B CA    1 
ATOM   6812  C  C     . GLU   B 1 111 ? 121.896 85.699  145.115 1.00 87.76  ?  111  GLU   B C     1 
ATOM   6813  O  O     . GLU   B 1 111 ? 123.075 85.960  145.083 1.00 93.55  ?  111  GLU   B O     1 
ATOM   6814  C  CB    . GLU   B 1 111 ? 121.174 83.521  146.034 1.00 86.53  ?  111  GLU   B CB    1 
ATOM   6815  C  CG    . GLU   B 1 111 ? 122.449 82.726  146.085 1.00 91.05  ?  111  GLU   B CG    1 
ATOM   6816  C  CD    . GLU   B 1 111 ? 122.213 81.295  145.640 1.00 99.50  ?  111  GLU   B CD    1 
ATOM   6817  O  OE1   . GLU   B 1 111 ? 121.085 81.001  145.198 1.00 98.13  ?  111  GLU   B OE1   1 
ATOM   6818  O  OE2   . GLU   B 1 111 ? 123.152 80.479  145.733 1.00 97.77  ?  111  GLU   B OE2   1 
ATOM   6819  N  N     . MET   B 1 112 ? 121.078 85.896  144.112 1.00 81.74  ?  112  MET   B N     1 
ATOM   6820  C  CA    . MET   B 1 112 ? 121.577 86.518  142.893 1.00 82.39  ?  112  MET   B CA    1 
ATOM   6821  C  C     . MET   B 1 112 ? 121.593 88.041  142.965 1.00 82.53  ?  112  MET   B C     1 
ATOM   6822  O  O     . MET   B 1 112 ? 121.903 88.692  141.962 1.00 84.24  ?  112  MET   B O     1 
ATOM   6823  C  CB    . MET   B 1 112 ? 120.754 86.060  141.688 1.00 81.59  ?  112  MET   B CB    1 
ATOM   6824  C  CG    . MET   B 1 112 ? 119.263 86.251  141.833 1.00 83.35  ?  112  MET   B CG    1 
ATOM   6825  S  SD    . MET   B 1 112 ? 118.360 84.945  140.984 1.00 100.09 ?  112  MET   B SD    1 
ATOM   6826  C  CE    . MET   B 1 112 ? 118.991 85.116  139.319 1.00 83.52  ?  112  MET   B CE    1 
ATOM   6827  N  N     . GLY   B 1 113 ? 121.271 88.620  144.119 1.00 76.59  ?  113  GLY   B N     1 
ATOM   6828  C  CA    . GLY   B 1 113 ? 121.363 90.054  144.296 1.00 76.88  ?  113  GLY   B CA    1 
ATOM   6829  C  C     . GLY   B 1 113 ? 120.189 90.854  143.786 1.00 77.86  ?  113  GLY   B C     1 
ATOM   6830  O  O     . GLY   B 1 113 ? 120.312 92.075  143.642 1.00 78.53  ?  113  GLY   B O     1 
ATOM   6831  N  N     . LYS   B 1 114 ? 119.056 90.212  143.499 1.00 74.58  ?  114  LYS   B N     1 
ATOM   6832  C  CA    . LYS   B 1 114 ? 117.889 90.948  143.030 1.00 70.04  ?  114  LYS   B CA    1 
ATOM   6833  C  C     . LYS   B 1 114 ? 117.179 91.682  144.160 1.00 71.53  ?  114  LYS   B C     1 
ATOM   6834  O  O     . LYS   B 1 114 ? 116.622 92.762  143.936 1.00 77.78  ?  114  LYS   B O     1 
ATOM   6835  C  CB    . LYS   B 1 114 ? 116.921 90.000  142.323 1.00 69.68  ?  114  LYS   B CB    1 
ATOM   6836  C  CG    . LYS   B 1 114 ? 117.421 89.512  140.976 1.00 68.46  ?  114  LYS   B CG    1 
ATOM   6837  C  CD    . LYS   B 1 114 ? 117.879 90.675  140.113 1.00 74.31  ?  114  LYS   B CD    1 
ATOM   6838  C  CE    . LYS   B 1 114 ? 119.013 90.268  139.189 1.00 76.59  ?  114  LYS   B CE    1 
ATOM   6839  N  NZ    . LYS   B 1 114 ? 119.486 91.411  138.361 1.00 76.98  ?  114  LYS   B NZ    1 
ATOM   6840  N  N     . TYR   B 1 115 ? 117.186 91.124  145.366 1.00 64.22  ?  115  TYR   B N     1 
ATOM   6841  C  CA    . TYR   B 1 115 ? 116.564 91.744  146.525 1.00 61.46  ?  115  TYR   B CA    1 
ATOM   6842  C  C     . TYR   B 1 115 ? 117.622 92.134  147.549 1.00 69.98  ?  115  TYR   B C     1 
ATOM   6843  O  O     . TYR   B 1 115 ? 118.746 91.626  147.543 1.00 75.82  ?  115  TYR   B O     1 
ATOM   6844  C  CB    . TYR   B 1 115 ? 115.540 90.807  147.174 1.00 58.16  ?  115  TYR   B CB    1 
ATOM   6845  C  CG    . TYR   B 1 115 ? 114.318 90.541  146.328 1.00 63.84  ?  115  TYR   B CG    1 
ATOM   6846  C  CD1   . TYR   B 1 115 ? 113.988 91.369  145.266 1.00 67.44  ?  115  TYR   B CD1   1 
ATOM   6847  C  CD2   . TYR   B 1 115 ? 113.491 89.463  146.596 1.00 65.34  ?  115  TYR   B CD2   1 
ATOM   6848  C  CE1   . TYR   B 1 115 ? 112.872 91.125  144.492 1.00 66.02  ?  115  TYR   B CE1   1 
ATOM   6849  C  CE2   . TYR   B 1 115 ? 112.381 89.206  145.821 1.00 67.67  ?  115  TYR   B CE2   1 
ATOM   6850  C  CZ    . TYR   B 1 115 ? 112.070 90.044  144.777 1.00 69.99  ?  115  TYR   B CZ    1 
ATOM   6851  O  OH    . TYR   B 1 115 ? 110.955 89.792  144.011 1.00 79.25  ?  115  TYR   B OH    1 
ATOM   6852  N  N     . ASP   B 1 116 ? 117.243 93.052  148.433 1.00 80.34  ?  116  ASP   B N     1 
ATOM   6853  C  CA    . ASP   B 1 116 ? 118.137 93.495  149.492 1.00 78.60  ?  116  ASP   B CA    1 
ATOM   6854  C  C     . ASP   B 1 116 ? 118.317 92.386  150.524 1.00 79.82  ?  116  ASP   B C     1 
ATOM   6855  O  O     . ASP   B 1 116 ? 117.364 91.688  150.880 1.00 83.92  ?  116  ASP   B O     1 
ATOM   6856  C  CB    . ASP   B 1 116 ? 117.587 94.769  150.144 1.00 77.13  ?  116  ASP   B CB    1 
ATOM   6857  C  CG    . ASP   B 1 116 ? 118.655 95.554  150.876 1.00 84.35  ?  116  ASP   B CG    1 
ATOM   6858  O  OD1   . ASP   B 1 116 ? 119.787 95.646  150.360 1.00 88.31  ?  116  ASP   B OD1   1 
ATOM   6859  O  OD2   . ASP   B 1 116 ? 118.394 95.983  152.016 1.00 86.00  ?  116  ASP   B OD2   1 
ATOM   6860  N  N     . ASN   B 1 117 ? 119.529 92.154  150.969 1.00 83.92  ?  117  ASN   B N     1 
ATOM   6861  C  CA    A ASN   B 1 117 ? 119.868 91.134  151.924 0.50 84.01  ?  117  ASN   B CA    1 
ATOM   6862  C  CA    B ASN   B 1 117 ? 119.811 91.074  151.942 0.50 84.01  ?  117  ASN   B CA    1 
ATOM   6863  C  C     . ASN   B 1 117 ? 119.069 91.235  153.293 1.00 83.60  ?  117  ASN   B C     1 
ATOM   6864  O  O     . ASN   B 1 117 ? 118.568 90.311  153.986 1.00 82.94  ?  117  ASN   B O     1 
ATOM   6865  C  CB    A ASN   B 1 117 ? 121.374 91.084  152.202 0.50 81.72  ?  117  ASN   B CB    1 
ATOM   6866  C  CB    B ASN   B 1 117 ? 121.316 90.930  152.131 0.50 81.72  ?  117  ASN   B CB    1 
ATOM   6867  C  CG    A ASN   B 1 117 ? 122.203 91.488  150.999 0.50 87.93  ?  117  ASN   B CG    1 
ATOM   6868  C  CG    B ASN   B 1 117 ? 121.665 89.830  153.109 0.50 87.93  ?  117  ASN   B CG    1 
ATOM   6869  O  OD1   A ASN   B 1 117 ? 122.108 92.616  150.515 0.50 89.50  ?  117  ASN   B OD1   1 
ATOM   6870  O  OD1   B ASN   B 1 117 ? 121.017 88.788  153.137 0.50 89.50  ?  117  ASN   B OD1   1 
ATOM   6871  N  ND2   A ASN   B 1 117 ? 122.988 90.551  150.479 0.50 88.03  ?  117  ASN   B ND2   1 
ATOM   6872  N  ND2   B ASN   B 1 117 ? 122.688 90.053  153.915 0.50 88.03  ?  117  ASN   B ND2   1 
ATOM   6873  N  N     . HIS   B 1 118 ? 118.783 92.484  153.653 1.00 76.64  ?  118  HIS   B N     1 
ATOM   6874  C  CA    . HIS   B 1 118 ? 118.166 92.698  154.959 1.00 75.96  ?  118  HIS   B CA    1 
ATOM   6875  C  C     . HIS   B 1 118 ? 116.863 91.926  155.107 1.00 81.07  ?  118  HIS   B C     1 
ATOM   6876  O  O     . HIS   B 1 118 ? 116.478 91.571  156.228 1.00 85.73  ?  118  HIS   B O     1 
ATOM   6877  C  CB    . HIS   B 1 118 ? 117.923 94.190  155.184 1.00 76.11  ?  118  HIS   B CB    1 
ATOM   6878  C  CG    . HIS   B 1 118 ? 116.551 94.643  154.793 1.00 80.19  ?  118  HIS   B CG    1 
ATOM   6879  N  ND1   . HIS   B 1 118 ? 115.512 94.734  155.693 1.00 84.04  ?  118  HIS   B ND1   1 
ATOM   6880  C  CD2   . HIS   B 1 118 ? 116.045 95.021  153.595 1.00 80.74  ?  118  HIS   B CD2   1 
ATOM   6881  C  CE1   . HIS   B 1 118 ? 114.426 95.152  155.068 1.00 81.43  ?  118  HIS   B CE1   1 
ATOM   6882  N  NE2   . HIS   B 1 118 ? 114.723 95.336  153.795 1.00 81.41  ?  118  HIS   B NE2   1 
ATOM   6883  N  N     . LEU   B 1 119 ? 116.179 91.648  153.994 1.00 80.68  ?  119  LEU   B N     1 
ATOM   6884  C  CA    . LEU   B 1 119 ? 114.923 90.909  154.058 1.00 79.31  ?  119  LEU   B CA    1 
ATOM   6885  C  C     . LEU   B 1 119 ? 115.119 89.538  154.688 1.00 80.99  ?  119  LEU   B C     1 
ATOM   6886  O  O     . LEU   B 1 119 ? 114.244 89.048  155.411 1.00 83.60  ?  119  LEU   B O     1 
ATOM   6887  C  CB    . LEU   B 1 119 ? 114.323 90.774  152.659 1.00 75.68  ?  119  LEU   B CB    1 
ATOM   6888  C  CG    . LEU   B 1 119 ? 113.568 91.993  152.128 1.00 77.29  ?  119  LEU   B CG    1 
ATOM   6889  C  CD1   . LEU   B 1 119 ? 113.153 91.777  150.682 1.00 78.20  ?  119  LEU   B CD1   1 
ATOM   6890  C  CD2   . LEU   B 1 119 ? 112.359 92.294  152.999 1.00 79.45  ?  119  LEU   B CD2   1 
ATOM   6891  N  N     . LEU   B 1 120 ? 116.261 88.902  154.430 1.00 79.03  ?  120  LEU   B N     1 
ATOM   6892  C  CA    . LEU   B 1 120 ? 116.536 87.603  155.028 1.00 76.58  ?  120  LEU   B CA    1 
ATOM   6893  C  C     . LEU   B 1 120 ? 117.027 87.710  156.463 1.00 78.93  ?  120  LEU   B C     1 
ATOM   6894  O  O     . LEU   B 1 120 ? 117.027 86.703  157.178 1.00 77.63  ?  120  LEU   B O     1 
ATOM   6895  C  CB    . LEU   B 1 120 ? 117.562 86.841  154.187 1.00 73.54  ?  120  LEU   B CB    1 
ATOM   6896  C  CG    . LEU   B 1 120 ? 117.003 86.131  152.955 1.00 73.96  ?  120  LEU   B CG    1 
ATOM   6897  C  CD1   . LEU   B 1 120 ? 118.087 85.329  152.256 1.00 78.16  ?  120  LEU   B CD1   1 
ATOM   6898  C  CD2   . LEU   B 1 120 ? 115.832 85.240  153.335 1.00 75.23  ?  120  LEU   B CD2   1 
ATOM   6899  N  N     . GLU   B 1 121 ? 117.436 88.899  156.901 1.00 93.82  ?  121  GLU   B N     1 
ATOM   6900  C  CA    . GLU   B 1 121 ? 117.924 89.083  158.260 1.00 91.57  ?  121  GLU   B CA    1 
ATOM   6901  C  C     . GLU   B 1 121 ? 116.829 89.557  159.206 1.00 92.13  ?  121  GLU   B C     1 
ATOM   6902  O  O     . GLU   B 1 121 ? 116.749 89.086  160.346 1.00 95.62  ?  121  GLU   B O     1 
ATOM   6903  C  CB    . GLU   B 1 121 ? 119.085 90.080  158.272 1.00 93.30  ?  121  GLU   B CB    1 
ATOM   6904  C  CG    . GLU   B 1 121 ? 120.086 89.882  157.148 1.00 95.53  ?  121  GLU   B CG    1 
ATOM   6905  C  CD    . GLU   B 1 121 ? 120.923 91.119  156.891 1.00 100.22 ?  121  GLU   B CD    1 
ATOM   6906  O  OE1   . GLU   B 1 121 ? 120.564 92.199  157.405 1.00 101.17 ?  121  GLU   B OE1   1 
ATOM   6907  O  OE2   . GLU   B 1 121 ? 121.936 91.014  156.168 1.00 99.74  ?  121  GLU   B OE2   1 
ATOM   6908  N  N     . ASP   B 1 122 ? 115.981 90.480  158.752 1.00 89.76  ?  122  ASP   B N     1 
ATOM   6909  C  CA    . ASP   B 1 122 ? 114.933 91.029  159.601 1.00 90.34  ?  122  ASP   B CA    1 
ATOM   6910  C  C     . ASP   B 1 122 ? 113.757 90.080  159.782 1.00 93.03  ?  122  ASP   B C     1 
ATOM   6911  O  O     . ASP   B 1 122 ? 113.001 90.232  160.747 1.00 96.60  ?  122  ASP   B O     1 
ATOM   6912  C  CB    . ASP   B 1 122 ? 114.438 92.356  159.025 1.00 92.71  ?  122  ASP   B CB    1 
ATOM   6913  C  CG    . ASP   B 1 122 ? 115.562 93.345  158.796 1.00 98.04  ?  122  ASP   B CG    1 
ATOM   6914  O  OD1   . ASP   B 1 122 ? 116.643 93.166  159.396 1.00 96.57  ?  122  ASP   B OD1   1 
ATOM   6915  O  OD2   . ASP   B 1 122 ? 115.367 94.302  158.020 1.00 104.27 ?  122  ASP   B OD2   1 
ATOM   6916  N  N     . TYR   B 1 123 ? 113.584 89.113  158.887 1.00 73.35  ?  123  TYR   B N     1 
ATOM   6917  C  CA    . TYR   B 1 123 ? 112.486 88.161  158.962 1.00 73.07  ?  123  TYR   B CA    1 
ATOM   6918  C  C     . TYR   B 1 123 ? 113.032 86.742  158.986 1.00 77.70  ?  123  TYR   B C     1 
ATOM   6919  O  O     . TYR   B 1 123 ? 113.975 86.416  158.257 1.00 79.38  ?  123  TYR   B O     1 
ATOM   6920  C  CB    . TYR   B 1 123 ? 111.524 88.324  157.781 1.00 70.74  ?  123  TYR   B CB    1 
ATOM   6921  C  CG    . TYR   B 1 123 ? 110.762 89.628  157.781 1.00 70.44  ?  123  TYR   B CG    1 
ATOM   6922  C  CD1   . TYR   B 1 123 ? 109.620 89.787  158.551 1.00 68.09  ?  123  TYR   B CD1   1 
ATOM   6923  C  CD2   . TYR   B 1 123 ? 111.182 90.698  157.006 1.00 69.16  ?  123  TYR   B CD2   1 
ATOM   6924  C  CE1   . TYR   B 1 123 ? 108.919 90.975  158.551 1.00 67.50  ?  123  TYR   B CE1   1 
ATOM   6925  C  CE2   . TYR   B 1 123 ? 110.488 91.890  157.001 1.00 70.22  ?  123  TYR   B CE2   1 
ATOM   6926  C  CZ    . TYR   B 1 123 ? 109.358 92.023  157.775 1.00 72.68  ?  123  TYR   B CZ    1 
ATOM   6927  O  OH    . TYR   B 1 123 ? 108.664 93.210  157.772 1.00 76.69  ?  123  TYR   B OH    1 
ATOM   6928  N  N     . THR   B 1 124 ? 112.435 85.902  159.826 1.00 90.96  ?  124  THR   B N     1 
ATOM   6929  C  CA    . THR   B 1 124 ? 112.791 84.496  159.887 1.00 89.70  ?  124  THR   B CA    1 
ATOM   6930  C  C     . THR   B 1 124 ? 111.970 83.712  158.865 1.00 91.43  ?  124  THR   B C     1 
ATOM   6931  O  O     . THR   B 1 124 ? 111.156 84.268  158.124 1.00 93.92  ?  124  THR   B O     1 
ATOM   6932  C  CB    . THR   B 1 124 ? 112.582 83.953  161.300 1.00 89.92  ?  124  THR   B CB    1 
ATOM   6933  O  OG1   . THR   B 1 124 ? 111.180 83.900  161.591 1.00 93.91  ?  124  THR   B OG1   1 
ATOM   6934  C  CG2   . THR   B 1 124 ? 113.269 84.847  162.318 1.00 90.31  ?  124  THR   B CG2   1 
ATOM   6935  N  N     . GLU   B 1 125 ? 112.188 82.397  158.820 1.00 92.74  ?  125  GLU   B N     1 
ATOM   6936  C  CA    . GLU   B 1 125 ? 111.457 81.562  157.872 1.00 90.06  ?  125  GLU   B CA    1 
ATOM   6937  C  C     . GLU   B 1 125 ? 109.980 81.467  158.236 1.00 96.85  ?  125  GLU   B C     1 
ATOM   6938  O  O     . GLU   B 1 125 ? 109.116 81.464  157.351 1.00 101.24 ?  125  GLU   B O     1 
ATOM   6939  C  CB    . GLU   B 1 125 ? 112.088 80.172  157.803 1.00 91.13  ?  125  GLU   B CB    1 
ATOM   6940  C  CG    . GLU   B 1 125 ? 111.395 79.224  156.841 1.00 96.58  ?  125  GLU   B CG    1 
ATOM   6941  C  CD    . GLU   B 1 125 ? 112.240 78.015  156.504 1.00 100.63 ?  125  GLU   B CD    1 
ATOM   6942  O  OE1   . GLU   B 1 125 ? 113.377 77.922  157.011 1.00 99.81  ?  125  GLU   B OE1   1 
ATOM   6943  O  OE2   . GLU   B 1 125 ? 111.767 77.158  155.729 1.00 102.70 ?  125  GLU   B OE2   1 
ATOM   6944  N  N     . GLU   B 1 126 ? 109.670 81.385  159.533 1.00 102.55 ?  126  GLU   B N     1 
ATOM   6945  C  CA    . GLU   B 1 126 ? 108.276 81.284  159.958 1.00 101.23 ?  126  GLU   B CA    1 
ATOM   6946  C  C     . GLU   B 1 126 ? 107.494 82.541  159.602 1.00 101.46 ?  126  GLU   B C     1 
ATOM   6947  O  O     . GLU   B 1 126 ? 106.339 82.463  159.165 1.00 104.74 ?  126  GLU   B O     1 
ATOM   6948  C  CB    . GLU   B 1 126 ? 108.206 81.013  161.458 1.00 100.60 ?  126  GLU   B CB    1 
ATOM   6949  C  CG    . GLU   B 1 126 ? 109.080 79.866  161.910 1.00 104.17 ?  126  GLU   B CG    1 
ATOM   6950  C  CD    . GLU   B 1 126 ? 108.985 78.647  161.011 1.00 110.60 ?  126  GLU   B CD    1 
ATOM   6951  O  OE1   . GLU   B 1 126 ? 107.852 78.220  160.708 1.00 111.84 ?  126  GLU   B OE1   1 
ATOM   6952  O  OE2   . GLU   B 1 126 ? 110.039 78.044  160.725 1.00 109.89 ?  126  GLU   B OE2   1 
ATOM   6953  N  N     . GLU   B 1 127 ? 108.106 83.713  159.785 1.00 93.58  ?  127  GLU   B N     1 
ATOM   6954  C  CA    . GLU   B 1 127 ? 107.443 84.954  159.401 1.00 93.20  ?  127  GLU   B CA    1 
ATOM   6955  C  C     . GLU   B 1 127 ? 107.225 85.015  157.895 1.00 94.70  ?  127  GLU   B C     1 
ATOM   6956  O  O     . GLU   B 1 127 ? 106.199 85.523  157.429 1.00 95.73  ?  127  GLU   B O     1 
ATOM   6957  C  CB    . GLU   B 1 127 ? 108.257 86.155  159.879 1.00 91.98  ?  127  GLU   B CB    1 
ATOM   6958  C  CG    . GLU   B 1 127 ? 108.064 86.481  161.350 1.00 94.22  ?  127  GLU   B CG    1 
ATOM   6959  C  CD    . GLU   B 1 127 ? 109.277 87.146  161.964 1.00 99.81  ?  127  GLU   B CD    1 
ATOM   6960  O  OE1   . GLU   B 1 127 ? 110.346 87.147  161.317 1.00 97.97  ?  127  GLU   B OE1   1 
ATOM   6961  O  OE2   . GLU   B 1 127 ? 109.166 87.658  163.097 1.00 102.38 ?  127  GLU   B OE2   1 
ATOM   6962  N  N     . PHE   B 1 128 ? 108.182 84.504  157.117 1.00 83.46  ?  128  PHE   B N     1 
ATOM   6963  C  CA    . PHE   B 1 128 ? 108.002 84.452  155.670 1.00 77.59  ?  128  PHE   B CA    1 
ATOM   6964  C  C     . PHE   B 1 128 ? 106.856 83.522  155.293 1.00 79.25  ?  128  PHE   B C     1 
ATOM   6965  O  O     . PHE   B 1 128 ? 106.088 83.815  154.371 1.00 85.21  ?  128  PHE   B O     1 
ATOM   6966  C  CB    . PHE   B 1 128 ? 109.300 84.018  154.993 1.00 77.72  ?  128  PHE   B CB    1 
ATOM   6967  C  CG    . PHE   B 1 128 ? 110.181 85.164  154.594 1.00 77.44  ?  128  PHE   B CG    1 
ATOM   6968  C  CD1   . PHE   B 1 128 ? 109.746 86.098  153.672 1.00 76.78  ?  128  PHE   B CD1   1 
ATOM   6969  C  CD2   . PHE   B 1 128 ? 111.440 85.314  155.147 1.00 79.96  ?  128  PHE   B CD2   1 
ATOM   6970  C  CE1   . PHE   B 1 128 ? 110.552 87.158  153.305 1.00 77.27  ?  128  PHE   B CE1   1 
ATOM   6971  C  CE2   . PHE   B 1 128 ? 112.250 86.371  154.784 1.00 80.19  ?  128  PHE   B CE2   1 
ATOM   6972  C  CZ    . PHE   B 1 128 ? 111.805 87.294  153.862 1.00 77.23  ?  128  PHE   B CZ    1 
ATOM   6973  N  N     . LYS   B 1 129 ? 106.720 82.398  155.999 1.00 86.31  ?  129  LYS   B N     1 
ATOM   6974  C  CA    . LYS   B 1 129 ? 105.591 81.506  155.753 1.00 89.76  ?  129  LYS   B CA    1 
ATOM   6975  C  C     . LYS   B 1 129 ? 104.269 82.185  156.096 1.00 91.85  ?  129  LYS   B C     1 
ATOM   6976  O  O     . LYS   B 1 129 ? 103.270 82.015  155.387 1.00 93.42  ?  129  LYS   B O     1 
ATOM   6977  C  CB    . LYS   B 1 129 ? 105.761 80.215  156.552 1.00 86.48  ?  129  LYS   B CB    1 
ATOM   6978  C  CG    . LYS   B 1 129 ? 106.871 79.315  156.035 1.00 89.62  ?  129  LYS   B CG    1 
ATOM   6979  C  CD    . LYS   B 1 129 ? 107.004 78.057  156.875 1.00 92.36  ?  129  LYS   B CD    1 
ATOM   6980  C  CE    . LYS   B 1 129 ? 107.077 76.817  156.003 1.00 95.55  ?  129  LYS   B CE    1 
ATOM   6981  N  NZ    . LYS   B 1 129 ? 108.433 76.202  156.024 1.00 92.21  ?  129  LYS   B NZ    1 
ATOM   6982  N  N     . GLN   B 1 130 ? 104.245 82.962  157.179 1.00 85.61  ?  130  GLN   B N     1 
ATOM   6983  C  CA    . GLN   B 1 130 ? 103.030 83.693  157.532 1.00 82.64  ?  130  GLN   B CA    1 
ATOM   6984  C  C     . GLN   B 1 130 ? 102.685 84.744  156.480 1.00 84.89  ?  130  GLN   B C     1 
ATOM   6985  O  O     . GLN   B 1 130 ? 101.512 84.912  156.120 1.00 89.97  ?  130  GLN   B O     1 
ATOM   6986  C  CB    . GLN   B 1 130 ? 103.187 84.334  158.909 1.00 81.93  ?  130  GLN   B CB    1 
ATOM   6987  C  CG    . GLN   B 1 130 ? 103.034 83.355  160.057 1.00 87.57  ?  130  GLN   B CG    1 
ATOM   6988  C  CD    . GLN   B 1 130 ? 102.916 84.045  161.398 1.00 92.76  ?  130  GLN   B CD    1 
ATOM   6989  O  OE1   . GLN   B 1 130 ? 101.880 84.627  161.719 1.00 92.58  ?  130  GLN   B OE1   1 
ATOM   6990  N  NE2   . GLN   B 1 130 ? 103.978 83.983  162.191 1.00 90.73  ?  130  GLN   B NE2   1 
ATOM   6991  N  N     . MET   B 1 131 ? 103.689 85.464  155.976 1.00 77.34  ?  131  MET   B N     1 
ATOM   6992  C  CA    . MET   B 1 131 ? 103.430 86.424  154.907 1.00 73.53  ?  131  MET   B CA    1 
ATOM   6993  C  C     . MET   B 1 131 ? 102.971 85.727  153.632 1.00 77.36  ?  131  MET   B C     1 
ATOM   6994  O  O     . MET   B 1 131 ? 102.158 86.280  152.883 1.00 86.72  ?  131  MET   B O     1 
ATOM   6995  C  CB    . MET   B 1 131 ? 104.672 87.270  154.634 1.00 72.15  ?  131  MET   B CB    1 
ATOM   6996  C  CG    . MET   B 1 131 ? 105.140 88.089  155.821 1.00 77.08  ?  131  MET   B CG    1 
ATOM   6997  S  SD    . MET   B 1 131 ? 106.546 89.135  155.413 1.00 85.01  ?  131  MET   B SD    1 
ATOM   6998  C  CE    . MET   B 1 131 ? 107.899 88.157  156.052 1.00 80.68  ?  131  MET   B CE    1 
ATOM   6999  N  N     . ASP   B 1 132 ? 103.398 84.480  153.449 1.00 79.72  ?  132  ASP   B N     1 
ATOM   7000  C  CA    . ASP   B 1 132 ? 102.989 83.656  152.291 1.00 79.51  ?  132  ASP   B CA    1 
ATOM   7001  C  C     . ASP   B 1 132 ? 101.533 83.297  152.497 1.00 80.12  ?  132  ASP   B C     1 
ATOM   7002  O  O     . ASP   B 1 132 ? 100.813 83.137  151.504 1.00 86.69  ?  132  ASP   B O     1 
ATOM   7003  C  CB    . ASP   B 1 132 ? 103.819 82.395  152.235 1.00 84.95  ?  132  ASP   B CB    1 
ATOM   7004  C  CG    . ASP   B 1 132 ? 103.796 81.690  150.899 1.00 88.02  ?  132  ASP   B CG    1 
ATOM   7005  O  OD1   . ASP   B 1 132 ? 104.125 82.368  149.928 1.00 86.45  ?  132  ASP   B OD1   1 
ATOM   7006  O  OD2   . ASP   B 1 132 ? 103.458 80.490  150.860 1.00 87.20  ?  132  ASP   B OD2   1 
ATOM   7007  N  N     . THR   B 1 133 ? 101.138 83.097  153.743 1.00 72.66  ?  133  THR   B N     1 
ATOM   7008  C  CA    . THR   B 1 133 ? 99.735  82.871  154.076 1.00 73.47  ?  133  THR   B CA    1 
ATOM   7009  C  C     . THR   B 1 133 ? 98.898  84.113  153.792 1.00 69.54  ?  133  THR   B C     1 
ATOM   7010  O  O     . THR   B 1 133 ? 97.749  84.008  153.348 1.00 71.38  ?  133  THR   B O     1 
ATOM   7011  C  CB    . THR   B 1 133 ? 99.597  82.452  155.541 1.00 74.11  ?  133  THR   B CB    1 
ATOM   7012  O  OG1   . THR   B 1 133 ? 100.479 81.355  155.809 1.00 78.73  ?  133  THR   B OG1   1 
ATOM   7013  C  CG2   . THR   B 1 133 ? 98.169  82.028  155.843 1.00 74.30  ?  133  THR   B CG2   1 
ATOM   7014  N  N     . PHE   B 1 134 ? 99.458  85.300  154.044 1.00 72.54  ?  134  PHE   B N     1 
ATOM   7015  C  CA    . PHE   B 1 134 ? 98.754  86.533  153.695 1.00 69.95  ?  134  PHE   B CA    1 
ATOM   7016  C  C     . PHE   B 1 134 ? 98.530  86.649  152.192 1.00 72.58  ?  134  PHE   B C     1 
ATOM   7017  O  O     . PHE   B 1 134 ? 97.552  87.266  151.756 1.00 78.01  ?  134  PHE   B O     1 
ATOM   7018  C  CB    . PHE   B 1 134 ? 99.530  87.758  154.184 1.00 72.09  ?  134  PHE   B CB    1 
ATOM   7019  C  CG    . PHE   B 1 134 ? 99.742  87.804  155.670 1.00 73.17  ?  134  PHE   B CG    1 
ATOM   7020  C  CD1   . PHE   B 1 134 ? 98.897  87.129  156.533 1.00 76.23  ?  134  PHE   B CD1   1 
ATOM   7021  C  CD2   . PHE   B 1 134 ? 100.787 88.540  156.202 1.00 68.78  ?  134  PHE   B CD2   1 
ATOM   7022  C  CE1   . PHE   B 1 134 ? 99.098  87.179  157.898 1.00 78.55  ?  134  PHE   B CE1   1 
ATOM   7023  C  CE2   . PHE   B 1 134 ? 100.992 88.594  157.565 1.00 75.22  ?  134  PHE   B CE2   1 
ATOM   7024  C  CZ    . PHE   B 1 134 ? 100.146 87.913  158.414 1.00 78.12  ?  134  PHE   B CZ    1 
ATOM   7025  N  N     . ILE   B 1 135 ? 99.420  86.064  151.390 1.00 75.94  ?  135  ILE   B N     1 
ATOM   7026  C  CA    . ILE   B 1 135 ? 99.413  86.275  149.948 1.00 69.04  ?  135  ILE   B CA    1 
ATOM   7027  C  C     . ILE   B 1 135 ? 98.214  85.580  149.315 1.00 74.95  ?  135  ILE   B C     1 
ATOM   7028  O  O     . ILE   B 1 135 ? 97.806  84.491  149.738 1.00 80.86  ?  135  ILE   B O     1 
ATOM   7029  C  CB    . ILE   B 1 135 ? 100.735 85.769  149.344 1.00 74.17  ?  135  ILE   B CB    1 
ATOM   7030  C  CG1   . ILE   B 1 135 ? 101.783 86.878  149.311 1.00 71.75  ?  135  ILE   B CG1   1 
ATOM   7031  C  CG2   . ILE   B 1 135 ? 100.535 85.218  147.947 1.00 78.95  ?  135  ILE   B CG2   1 
ATOM   7032  C  CD1   . ILE   B 1 135 ? 103.159 86.370  148.971 1.00 70.49  ?  135  ILE   B CD1   1 
ATOM   7033  N  N     . ASP   B 1 136 ? 97.639  86.217  148.294 1.00 89.29  ?  136  ASP   B N     1 
ATOM   7034  C  CA    . ASP   B 1 136 ? 96.598  85.608  147.464 1.00 92.46  ?  136  ASP   B CA    1 
ATOM   7035  C  C     . ASP   B 1 136 ? 96.923  85.965  146.016 1.00 91.93  ?  136  ASP   B C     1 
ATOM   7036  O  O     . ASP   B 1 136 ? 96.685  87.097  145.586 1.00 92.16  ?  136  ASP   B O     1 
ATOM   7037  C  CB    . ASP   B 1 136 ? 95.212  86.094  147.875 1.00 92.74  ?  136  ASP   B CB    1 
ATOM   7038  C  CG    . ASP   B 1 136 ? 94.139  85.737  146.864 1.00 98.13  ?  136  ASP   B CG    1 
ATOM   7039  O  OD1   . ASP   B 1 136 ? 94.289  84.729  146.142 1.00 98.85  ?  136  ASP   B OD1   1 
ATOM   7040  O  OD2   . ASP   B 1 136 ? 93.151  86.493  146.773 1.00 98.12  ?  136  ASP   B OD2   1 
ATOM   7041  N  N     . HIS   B 1 137 ? 97.468  85.000  145.266 1.00 78.67  ?  137  HIS   B N     1 
ATOM   7042  C  CA    . HIS   B 1 137 ? 97.877  85.276  143.892 1.00 78.22  ?  137  HIS   B CA    1 
ATOM   7043  C  C     . HIS   B 1 137 ? 96.694  85.446  142.949 1.00 81.40  ?  137  HIS   B C     1 
ATOM   7044  O  O     . HIS   B 1 137 ? 96.868  86.000  141.858 1.00 85.78  ?  137  HIS   B O     1 
ATOM   7045  C  CB    . HIS   B 1 137 ? 98.789  84.167  143.357 1.00 76.98  ?  137  HIS   B CB    1 
ATOM   7046  C  CG    . HIS   B 1 137 ? 99.972  83.878  144.226 1.00 79.78  ?  137  HIS   B CG    1 
ATOM   7047  N  ND1   . HIS   B 1 137 ? 101.179 84.532  144.095 1.00 73.50  ?  137  HIS   B ND1   1 
ATOM   7048  C  CD2   . HIS   B 1 137 ? 100.140 82.979  145.222 1.00 80.96  ?  137  HIS   B CD2   1 
ATOM   7049  C  CE1   . HIS   B 1 137 ? 102.033 84.057  144.983 1.00 73.39  ?  137  HIS   B CE1   1 
ATOM   7050  N  NE2   . HIS   B 1 137 ? 101.415 83.140  145.704 1.00 80.09  ?  137  HIS   B NE2   1 
ATOM   7051  N  N     . ASP   B 1 138 ? 95.502  84.986  143.336 1.00 85.39  ?  138  ASP   B N     1 
ATOM   7052  C  CA    . ASP   B 1 138 ? 94.330  85.161  142.485 1.00 84.01  ?  138  ASP   B CA    1 
ATOM   7053  C  C     . ASP   B 1 138 ? 94.017  86.630  142.242 1.00 88.50  ?  138  ASP   B C     1 
ATOM   7054  O  O     . ASP   B 1 138 ? 93.376  86.961  141.237 1.00 92.04  ?  138  ASP   B O     1 
ATOM   7055  C  CB    . ASP   B 1 138 ? 93.120  84.462  143.103 1.00 85.77  ?  138  ASP   B CB    1 
ATOM   7056  C  CG    . ASP   B 1 138 ? 93.064  82.985  142.763 1.00 94.02  ?  138  ASP   B CG    1 
ATOM   7057  O  OD1   . ASP   B 1 138 ? 93.125  82.649  141.562 1.00 95.86  ?  138  ASP   B OD1   1 
ATOM   7058  O  OD2   . ASP   B 1 138 ? 92.963  82.161  143.696 1.00 95.20  ?  138  ASP   B OD2   1 
ATOM   7059  N  N     . ARG   B 1 139 ? 94.471  87.519  143.129 1.00 74.83  ?  139  ARG   B N     1 
ATOM   7060  C  CA    . ARG   B 1 139 ? 94.290  88.949  142.919 1.00 74.23  ?  139  ARG   B CA    1 
ATOM   7061  C  C     . ARG   B 1 139 ? 94.982  89.432  141.652 1.00 76.89  ?  139  ARG   B C     1 
ATOM   7062  O  O     . ARG   B 1 139 ? 94.621  90.492  141.127 1.00 85.04  ?  139  ARG   B O     1 
ATOM   7063  C  CB    . ARG   B 1 139 ? 94.810  89.724  144.131 1.00 74.14  ?  139  ARG   B CB    1 
ATOM   7064  C  CG    . ARG   B 1 139 ? 93.746  90.008  145.175 1.00 77.32  ?  139  ARG   B CG    1 
ATOM   7065  C  CD    . ARG   B 1 139 ? 94.214  91.041  146.182 1.00 78.24  ?  139  ARG   B CD    1 
ATOM   7066  N  NE    . ARG   B 1 139 ? 94.689  90.430  147.416 1.00 82.07  ?  139  ARG   B NE    1 
ATOM   7067  C  CZ    . ARG   B 1 139 ? 93.978  90.342  148.532 1.00 77.77  ?  139  ARG   B CZ    1 
ATOM   7068  N  NH1   . ARG   B 1 139 ? 92.738  90.793  148.599 1.00 75.49  ?  139  ARG   B NH1   1 
ATOM   7069  N  NH2   . ARG   B 1 139 ? 94.516  89.760  149.598 1.00 77.54  ?  139  ARG   B NH2   1 
ATOM   7070  N  N     . ASP   B 1 140 ? 95.952  88.669  141.141 1.00 76.24  ?  140  ASP   B N     1 
ATOM   7071  C  CA    . ASP   B 1 140 ? 96.576  89.004  139.867 1.00 74.79  ?  140  ASP   B CA    1 
ATOM   7072  C  C     . ASP   B 1 140 ? 95.571  89.018  138.725 1.00 77.12  ?  140  ASP   B C     1 
ATOM   7073  O  O     . ASP   B 1 140 ? 95.836  89.635  137.687 1.00 76.36  ?  140  ASP   B O     1 
ATOM   7074  C  CB    . ASP   B 1 140 ? 97.700  88.016  139.550 1.00 71.75  ?  140  ASP   B CB    1 
ATOM   7075  C  CG    . ASP   B 1 140 ? 99.023  88.435  140.144 1.00 81.82  ?  140  ASP   B CG    1 
ATOM   7076  O  OD1   . ASP   B 1 140 ? 99.214  89.649  140.370 1.00 84.19  ?  140  ASP   B OD1   1 
ATOM   7077  O  OD2   . ASP   B 1 140 ? 99.871  87.554  140.405 1.00 79.93  ?  140  ASP   B OD2   1 
ATOM   7078  N  N     . MET   B 1 141 ? 94.427  88.353  138.889 1.00 75.61  ?  141  MET   B N     1 
ATOM   7079  C  CA    . MET   B 1 141 ? 93.390  88.370  137.867 1.00 74.69  ?  141  MET   B CA    1 
ATOM   7080  C  C     . MET   B 1 141 ? 92.530  89.625  137.913 1.00 77.04  ?  141  MET   B C     1 
ATOM   7081  O  O     . MET   B 1 141 ? 91.694  89.813  137.023 1.00 82.85  ?  141  MET   B O     1 
ATOM   7082  C  CB    . MET   B 1 141 ? 92.509  87.130  138.002 1.00 77.53  ?  141  MET   B CB    1 
ATOM   7083  C  CG    . MET   B 1 141 ? 93.266  85.841  137.749 1.00 80.55  ?  141  MET   B CG    1 
ATOM   7084  S  SD    . MET   B 1 141 ? 93.902  85.746  136.056 1.00 91.16  ?  141  MET   B SD    1 
ATOM   7085  C  CE    . MET   B 1 141 ? 95.615  86.134  136.385 1.00 83.84  ?  141  MET   B CE    1 
ATOM   7086  N  N     . THR   B 1 142 ? 92.710  90.484  138.914 1.00 72.42  ?  142  THR   B N     1 
ATOM   7087  C  CA    . THR   B 1 142 ? 91.938  91.715  139.009 1.00 73.25  ?  142  THR   B CA    1 
ATOM   7088  C  C     . THR   B 1 142 ? 92.580  92.880  138.267 1.00 70.74  ?  142  THR   B C     1 
ATOM   7089  O  O     . THR   B 1 142 ? 91.973  93.954  138.190 1.00 73.86  ?  142  THR   B O     1 
ATOM   7090  C  CB    . THR   B 1 142 ? 91.731  92.102  140.477 1.00 71.15  ?  142  THR   B CB    1 
ATOM   7091  O  OG1   . THR   B 1 142 ? 92.973  92.544  141.034 1.00 77.06  ?  142  THR   B OG1   1 
ATOM   7092  C  CG2   . THR   B 1 142 ? 91.223  90.915  141.273 1.00 69.95  ?  142  THR   B CG2   1 
ATOM   7093  N  N     . PHE   B 1 143 ? 93.778  92.698  137.721 1.00 57.54  ?  143  PHE   B N     1 
ATOM   7094  C  CA    . PHE   B 1 143 ? 94.447  93.769  137.002 1.00 58.25  ?  143  PHE   B CA    1 
ATOM   7095  C  C     . PHE   B 1 143 ? 93.803  93.993  135.637 1.00 64.73  ?  143  PHE   B C     1 
ATOM   7096  O  O     . PHE   B 1 143 ? 93.165  93.108  135.062 1.00 69.11  ?  143  PHE   B O     1 
ATOM   7097  C  CB    . PHE   B 1 143 ? 95.930  93.450  136.818 1.00 59.14  ?  143  PHE   B CB    1 
ATOM   7098  C  CG    . PHE   B 1 143 ? 96.748  93.601  138.066 1.00 62.98  ?  143  PHE   B CG    1 
ATOM   7099  C  CD1   . PHE   B 1 143 ? 96.997  94.852  138.601 1.00 63.32  ?  143  PHE   B CD1   1 
ATOM   7100  C  CD2   . PHE   B 1 143 ? 97.276  92.491  138.700 1.00 63.00  ?  143  PHE   B CD2   1 
ATOM   7101  C  CE1   . PHE   B 1 143 ? 97.754  94.992  139.747 1.00 61.55  ?  143  PHE   B CE1   1 
ATOM   7102  C  CE2   . PHE   B 1 143 ? 98.031  92.625  139.846 1.00 66.02  ?  143  PHE   B CE2   1 
ATOM   7103  C  CZ    . PHE   B 1 143 ? 98.270  93.877  140.370 1.00 64.14  ?  143  PHE   B CZ    1 
ATOM   7104  N  N     . SER   B 1 144 ? 93.983  95.201  135.123 1.00 70.64  ?  144  SER   B N     1 
ATOM   7105  C  CA    . SER   B 1 144 ? 93.600  95.552  133.766 1.00 60.08  ?  144  SER   B CA    1 
ATOM   7106  C  C     . SER   B 1 144 ? 94.812  95.429  132.844 1.00 63.53  ?  144  SER   B C     1 
ATOM   7107  O  O     . SER   B 1 144 ? 95.949  95.267  133.291 1.00 73.48  ?  144  SER   B O     1 
ATOM   7108  C  CB    . SER   B 1 144 ? 93.012  96.964  133.734 1.00 69.04  ?  144  SER   B CB    1 
ATOM   7109  O  OG    . SER   B 1 144 ? 91.610  96.911  133.923 1.00 76.43  ?  144  SER   B OG    1 
ATOM   7110  N  N     . TYR   B 1 145 ? 94.557  95.498  131.536 1.00 53.44  ?  145  TYR   B N     1 
ATOM   7111  C  CA    . TYR   B 1 145 ? 95.633  95.300  130.568 1.00 55.92  ?  145  TYR   B CA    1 
ATOM   7112  C  C     . TYR   B 1 145 ? 96.730  96.346  130.729 1.00 57.96  ?  145  TYR   B C     1 
ATOM   7113  O  O     . TYR   B 1 145 ? 97.922  96.016  130.713 1.00 71.55  ?  145  TYR   B O     1 
ATOM   7114  C  CB    . TYR   B 1 145 ? 95.073  95.327  129.147 1.00 55.47  ?  145  TYR   B CB    1 
ATOM   7115  C  CG    . TYR   B 1 145 ? 96.146  95.263  128.089 1.00 59.11  ?  145  TYR   B CG    1 
ATOM   7116  C  CD1   . TYR   B 1 145 ? 96.962  94.149  127.973 1.00 55.85  ?  145  TYR   B CD1   1 
ATOM   7117  C  CD2   . TYR   B 1 145 ? 96.356  96.322  127.218 1.00 53.26  ?  145  TYR   B CD2   1 
ATOM   7118  C  CE1   . TYR   B 1 145 ? 97.946  94.087  127.013 1.00 56.12  ?  145  TYR   B CE1   1 
ATOM   7119  C  CE2   . TYR   B 1 145 ? 97.336  96.266  126.250 1.00 54.24  ?  145  TYR   B CE2   1 
ATOM   7120  C  CZ    . TYR   B 1 145 ? 98.136  95.150  126.159 1.00 60.97  ?  145  TYR   B CZ    1 
ATOM   7121  O  OH    . TYR   B 1 145 ? 99.126  95.073  125.209 1.00 68.00  ?  145  TYR   B OH    1 
ATOM   7122  N  N     . ALA   B 1 146 ? 96.345  97.614  130.886 1.00 57.56  ?  146  ALA   B N     1 
ATOM   7123  C  CA    . ALA   B 1 146 ? 97.335  98.667  131.082 1.00 60.30  ?  146  ALA   B CA    1 
ATOM   7124  C  C     . ALA   B 1 146 ? 98.109  98.457  132.376 1.00 61.71  ?  146  ALA   B C     1 
ATOM   7125  O  O     . ALA   B 1 146 ? 99.320  98.702  132.432 1.00 65.20  ?  146  ALA   B O     1 
ATOM   7126  C  CB    . ALA   B 1 146 ? 96.653  100.034 131.074 1.00 53.65  ?  146  ALA   B CB    1 
ATOM   7127  N  N     . ALA   B 1 147 ? 97.425  97.996  133.424 1.00 53.00  ?  147  ALA   B N     1 
ATOM   7128  C  CA    . ALA   B 1 147 ? 98.092  97.710  134.688 1.00 44.87  ?  147  ALA   B CA    1 
ATOM   7129  C  C     . ALA   B 1 147 ? 99.167  96.645  134.513 1.00 51.46  ?  147  ALA   B C     1 
ATOM   7130  O  O     . ALA   B 1 147 ? 100.296 96.798  134.993 1.00 63.39  ?  147  ALA   B O     1 
ATOM   7131  C  CB    . ALA   B 1 147 ? 97.059  97.269  135.723 1.00 45.20  ?  147  ALA   B CB    1 
ATOM   7132  N  N     . VAL   B 1 148 ? 98.838  95.558  133.817 1.00 52.30  ?  148  VAL   B N     1 
ATOM   7133  C  CA    . VAL   B 1 148 ? 99.804  94.480  133.642 1.00 53.15  ?  148  VAL   B CA    1 
ATOM   7134  C  C     . VAL   B 1 148 ? 100.949 94.928  132.747 1.00 57.75  ?  148  VAL   B C     1 
ATOM   7135  O  O     . VAL   B 1 148 ? 102.103 94.552  132.970 1.00 66.77  ?  148  VAL   B O     1 
ATOM   7136  C  CB    . VAL   B 1 148 ? 99.110  93.224  133.084 1.00 54.92  ?  148  VAL   B CB    1 
ATOM   7137  C  CG1   . VAL   B 1 148 ? 100.090 92.082  132.899 1.00 55.13  ?  148  VAL   B CG1   1 
ATOM   7138  C  CG2   . VAL   B 1 148 ? 97.948  92.811  133.959 1.00 56.16  ?  148  VAL   B CG2   1 
ATOM   7139  N  N     . LYS   B 1 149 ? 100.657 95.725  131.716 1.00 56.28  ?  149  LYS   B N     1 
ATOM   7140  C  CA    A LYS   B 1 149 ? 101.721 96.227  130.850 0.39 55.91  ?  149  LYS   B CA    1 
ATOM   7141  C  CA    B LYS   B 1 149 ? 101.731 96.208  130.857 0.61 54.60  ?  149  LYS   B CA    1 
ATOM   7142  C  C     . LYS   B 1 149 ? 102.681 97.123  131.620 1.00 58.73  ?  149  LYS   B C     1 
ATOM   7143  O  O     . LYS   B 1 149 ? 103.901 97.054  131.429 1.00 70.50  ?  149  LYS   B O     1 
ATOM   7144  C  CB    A LYS   B 1 149 ? 101.122 96.984  129.665 0.39 56.34  ?  149  LYS   B CB    1 
ATOM   7145  C  CB    B LYS   B 1 149 ? 101.155 96.911  129.630 0.61 54.97  ?  149  LYS   B CB    1 
ATOM   7146  C  CG    A LYS   B 1 149 ? 100.489 96.102  128.622 0.39 58.44  ?  149  LYS   B CG    1 
ATOM   7147  C  CG    B LYS   B 1 149 ? 100.724 95.944  128.526 0.61 57.79  ?  149  LYS   B CG    1 
ATOM   7148  C  CD    A LYS   B 1 149 ? 101.445 95.029  128.243 0.39 61.00  ?  149  LYS   B CD    1 
ATOM   7149  C  CD    B LYS   B 1 149 ? 101.863 95.004  128.083 0.61 62.30  ?  149  LYS   B CD    1 
ATOM   7150  C  CE    A LYS   B 1 149 ? 102.571 95.520  127.355 0.39 60.70  ?  149  LYS   B CE    1 
ATOM   7151  C  CE    B LYS   B 1 149 ? 101.376 93.876  127.243 0.61 62.71  ?  149  LYS   B CE    1 
ATOM   7152  N  NZ    A LYS   B 1 149 ? 102.095 96.394  126.255 0.39 58.85  ?  149  LYS   B NZ    1 
ATOM   7153  N  NZ    B LYS   B 1 149 ? 102.484 92.943  126.930 0.61 61.93  ?  149  LYS   B NZ    1 
ATOM   7154  N  N     . GLN   B 1 150 ? 102.147 97.982  132.493 1.00 60.60  ?  150  GLN   B N     1 
ATOM   7155  C  CA    . GLN   B 1 150 ? 103.015 98.825  133.310 1.00 52.48  ?  150  GLN   B CA    1 
ATOM   7156  C  C     . GLN   B 1 150 ? 103.819 97.992  134.301 1.00 59.84  ?  150  GLN   B C     1 
ATOM   7157  O  O     . GLN   B 1 150 ? 104.995 98.279  134.548 1.00 69.15  ?  150  GLN   B O     1 
ATOM   7158  C  CB    . GLN   B 1 150 ? 102.193 99.887  134.042 1.00 57.59  ?  150  GLN   B CB    1 
ATOM   7159  C  CG    . GLN   B 1 150 ? 101.511 100.897 133.132 1.00 62.27  ?  150  GLN   B CG    1 
ATOM   7160  C  CD    . GLN   B 1 150 ? 102.487 101.807 132.412 1.00 66.28  ?  150  GLN   B CD    1 
ATOM   7161  O  OE1   . GLN   B 1 150 ? 103.671 101.859 132.741 1.00 72.23  ?  150  GLN   B OE1   1 
ATOM   7162  N  NE2   . GLN   B 1 150 ? 101.998 102.504 131.397 1.00 66.31  ?  150  GLN   B NE2   1 
ATOM   7163  N  N     . LEU   B 1 151 ? 103.203 96.960  134.883 1.00 58.50  ?  151  LEU   B N     1 
ATOM   7164  C  CA    . LEU   B 1 151 ? 103.931 96.078  135.791 1.00 48.01  ?  151  LEU   B CA    1 
ATOM   7165  C  C     . LEU   B 1 151 ? 105.078 95.378  135.076 1.00 52.48  ?  151  LEU   B C     1 
ATOM   7166  O  O     . LEU   B 1 151 ? 106.198 95.306  135.592 1.00 68.65  ?  151  LEU   B O     1 
ATOM   7167  C  CB    . LEU   B 1 151 ? 102.984 95.041  136.392 1.00 46.97  ?  151  LEU   B CB    1 
ATOM   7168  C  CG    . LEU   B 1 151 ? 102.056 95.509  137.509 1.00 51.52  ?  151  LEU   B CG    1 
ATOM   7169  C  CD1   . LEU   B 1 151 ? 101.052 94.443  137.901 1.00 57.35  ?  151  LEU   B CD1   1 
ATOM   7170  C  CD2   . LEU   B 1 151 ? 102.834 95.980  138.723 1.00 60.56  ?  151  LEU   B CD2   1 
ATOM   7171  N  N     . GLU   B 1 152 ? 104.812 94.853  133.880 1.00 69.63  ?  152  GLU   B N     1 
ATOM   7172  C  CA    . GLU   B 1 152 ? 105.831 94.112  133.146 1.00 69.94  ?  152  GLU   B CA    1 
ATOM   7173  C  C     . GLU   B 1 152 ? 106.942 95.030  132.653 1.00 68.58  ?  152  GLU   B C     1 
ATOM   7174  O  O     . GLU   B 1 152 ? 108.124 94.676  132.726 1.00 78.50  ?  152  GLU   B O     1 
ATOM   7175  C  CB    . GLU   B 1 152 ? 105.189 93.365  131.976 1.00 63.85  ?  152  GLU   B CB    1 
ATOM   7176  C  CG    . GLU   B 1 152 ? 106.151 93.019  130.852 1.00 73.65  ?  152  GLU   B CG    1 
ATOM   7177  C  CD    . GLU   B 1 152 ? 105.444 92.584  129.584 1.00 85.46  ?  152  GLU   B CD    1 
ATOM   7178  O  OE1   . GLU   B 1 152 ? 104.444 91.844  129.681 1.00 84.68  ?  152  GLU   B OE1   1 
ATOM   7179  O  OE2   . GLU   B 1 152 ? 105.888 92.985  128.487 1.00 88.69  ?  152  GLU   B OE2   1 
ATOM   7180  N  N     . GLY   B 1 153 ? 106.589 96.212  132.158 1.00 57.38  ?  153  GLY   B N     1 
ATOM   7181  C  CA    . GLY   B 1 153 ? 107.578 97.088  131.568 1.00 61.95  ?  153  GLY   B CA    1 
ATOM   7182  C  C     . GLY   B 1 153 ? 108.265 98.034  132.529 1.00 70.56  ?  153  GLY   B C     1 
ATOM   7183  O  O     . GLY   B 1 153 ? 109.336 98.560  132.214 1.00 77.31  ?  153  GLY   B O     1 
ATOM   7184  N  N     . LYS   B 1 154 ? 107.683 98.257  133.698 1.00 68.53  ?  154  LYS   B N     1 
ATOM   7185  C  CA    . LYS   B 1 154 ? 108.229 99.304  134.555 1.00 65.54  ?  154  LYS   B CA    1 
ATOM   7186  C  C     . LYS   B 1 154 ? 108.534 98.853  135.976 1.00 68.40  ?  154  LYS   B C     1 
ATOM   7187  O  O     . LYS   B 1 154 ? 109.541 99.283  136.542 1.00 77.37  ?  154  LYS   B O     1 
ATOM   7188  C  CB    . LYS   B 1 154 ? 107.256 100.493 134.599 1.00 65.84  ?  154  LYS   B CB    1 
ATOM   7189  C  CG    . LYS   B 1 154 ? 107.500 101.547 133.537 1.00 69.25  ?  154  LYS   B CG    1 
ATOM   7190  C  CD    . LYS   B 1 154 ? 106.804 102.847 133.894 1.00 69.37  ?  154  LYS   B CD    1 
ATOM   7191  C  CE    . LYS   B 1 154 ? 107.017 103.902 132.824 1.00 67.95  ?  154  LYS   B CE    1 
ATOM   7192  N  NZ    . LYS   B 1 154 ? 106.194 103.628 131.615 1.00 71.38  ?  154  LYS   B NZ    1 
ATOM   7193  N  N     . TYR   B 1 155 ? 107.701 98.002  136.567 1.00 64.50  ?  155  TYR   B N     1 
ATOM   7194  C  CA    . TYR   B 1 155 ? 107.715 97.804  138.012 1.00 60.10  ?  155  TYR   B CA    1 
ATOM   7195  C  C     . TYR   B 1 155 ? 108.288 96.471  138.462 1.00 63.29  ?  155  TYR   B C     1 
ATOM   7196  O  O     . TYR   B 1 155 ? 109.015 96.430  139.456 1.00 71.97  ?  155  TYR   B O     1 
ATOM   7197  C  CB    . TYR   B 1 155 ? 106.297 97.954  138.566 1.00 53.32  ?  155  TYR   B CB    1 
ATOM   7198  C  CG    . TYR   B 1 155 ? 105.748 99.352  138.422 1.00 61.14  ?  155  TYR   B CG    1 
ATOM   7199  C  CD1   . TYR   B 1 155 ? 106.596 100.452 138.435 1.00 63.55  ?  155  TYR   B CD1   1 
ATOM   7200  C  CD2   . TYR   B 1 155 ? 104.391 99.577  138.269 1.00 69.30  ?  155  TYR   B CD2   1 
ATOM   7201  C  CE1   . TYR   B 1 155 ? 106.110 101.735 138.303 1.00 64.72  ?  155  TYR   B CE1   1 
ATOM   7202  C  CE2   . TYR   B 1 155 ? 103.898 100.857 138.126 1.00 70.22  ?  155  TYR   B CE2   1 
ATOM   7203  C  CZ    . TYR   B 1 155 ? 104.759 101.930 138.146 1.00 69.10  ?  155  TYR   B CZ    1 
ATOM   7204  O  OH    . TYR   B 1 155 ? 104.216 103.187 138.037 1.00 73.04  ?  155  TYR   B OH    1 
ATOM   7205  N  N     . LEU   B 1 156 ? 107.977 95.376  137.773 1.00 56.74  ?  156  LEU   B N     1 
ATOM   7206  C  CA    . LEU   B 1 156 ? 108.465 94.072  138.200 1.00 50.94  ?  156  LEU   B CA    1 
ATOM   7207  C  C     . LEU   B 1 156 ? 109.983 94.015  138.105 1.00 60.71  ?  156  LEU   B C     1 
ATOM   7208  O  O     . LEU   B 1 156 ? 110.583 94.531  137.161 1.00 67.85  ?  156  LEU   B O     1 
ATOM   7209  C  CB    . LEU   B 1 156 ? 107.840 92.967  137.350 1.00 52.12  ?  156  LEU   B CB    1 
ATOM   7210  C  CG    . LEU   B 1 156 ? 106.344 92.733  137.562 1.00 56.49  ?  156  LEU   B CG    1 
ATOM   7211  C  CD1   . LEU   B 1 156 ? 105.806 91.755  136.526 1.00 56.33  ?  156  LEU   B CD1   1 
ATOM   7212  C  CD2   . LEU   B 1 156 ? 106.058 92.246  138.974 1.00 53.55  ?  156  LEU   B CD2   1 
ATOM   7213  N  N     . VAL   B 1 157 ? 110.610 93.392  139.104 1.00 61.21  ?  157  VAL   B N     1 
ATOM   7214  C  CA    . VAL   B 1 157 ? 112.062 93.277  139.102 1.00 66.95  ?  157  VAL   B CA    1 
ATOM   7215  C  C     . VAL   B 1 157 ? 112.484 92.425  137.920 1.00 67.81  ?  157  VAL   B C     1 
ATOM   7216  O  O     . VAL   B 1 157 ? 112.017 91.293  137.747 1.00 72.18  ?  157  VAL   B O     1 
ATOM   7217  C  CB    . VAL   B 1 157 ? 112.550 92.677  140.431 1.00 60.32  ?  157  VAL   B CB    1 
ATOM   7218  C  CG1   . VAL   B 1 157 ? 113.915 92.009  140.317 1.00 61.74  ?  157  VAL   B CG1   1 
ATOM   7219  C  CG2   . VAL   B 1 157 ? 112.527 93.688  141.560 1.00 64.59  ?  157  VAL   B CG2   1 
ATOM   7220  N  N     . GLN   B 1 158 ? 113.373 92.970  137.099 1.00 60.12  ?  158  GLN   B N     1 
ATOM   7221  C  CA    . GLN   B 1 158 ? 113.729 92.335  135.846 1.00 57.93  ?  158  GLN   B CA    1 
ATOM   7222  C  C     . GLN   B 1 158 ? 115.137 92.747  135.454 1.00 65.25  ?  158  GLN   B C     1 
ATOM   7223  O  O     . GLN   B 1 158 ? 115.678 93.742  135.943 1.00 68.71  ?  158  GLN   B O     1 
ATOM   7224  C  CB    . GLN   B 1 158 ? 112.741 92.706  134.738 1.00 59.98  ?  158  GLN   B CB    1 
ATOM   7225  C  CG    . GLN   B 1 158 ? 112.780 94.176  134.355 1.00 59.54  ?  158  GLN   B CG    1 
ATOM   7226  C  CD    . GLN   B 1 158 ? 111.539 94.620  133.609 1.00 67.65  ?  158  GLN   B CD    1 
ATOM   7227  O  OE1   . GLN   B 1 158 ? 111.588 94.901  132.412 1.00 74.37  ?  158  GLN   B OE1   1 
ATOM   7228  N  NE2   . GLN   B 1 158 ? 110.418 94.692  134.315 1.00 65.13  ?  158  GLN   B NE2   1 
ATOM   7229  N  N     . ASN   B 1 159 ? 115.724 91.960  134.558 1.00 69.57  ?  159  ASN   B N     1 
ATOM   7230  C  CA    . ASN   B 1 159 ? 117.008 92.298  133.960 1.00 62.39  ?  159  ASN   B CA    1 
ATOM   7231  C  C     . ASN   B 1 159 ? 116.771 93.223  132.774 1.00 66.69  ?  159  ASN   B C     1 
ATOM   7232  O  O     . ASN   B 1 159 ? 116.084 92.850  131.817 1.00 70.74  ?  159  ASN   B O     1 
ATOM   7233  C  CB    . ASN   B 1 159 ? 117.742 91.033  133.524 1.00 61.76  ?  159  ASN   B CB    1 
ATOM   7234  C  CG    . ASN   B 1 159 ? 119.247 91.191  133.556 1.00 68.84  ?  159  ASN   B CG    1 
ATOM   7235  O  OD1   . ASN   B 1 159 ? 119.819 91.946  132.771 1.00 69.69  ?  159  ASN   B OD1   1 
ATOM   7236  N  ND2   . ASN   B 1 159 ? 119.897 90.476  134.464 1.00 73.51  ?  159  ASN   B ND2   1 
ATOM   7237  N  N     . ARG   B 1 160 ? 117.330 94.432  132.836 1.00 67.17  ?  160  ARG   B N     1 
ATOM   7238  C  CA    . ARG   B 1 160 ? 117.118 95.405  131.773 1.00 64.88  ?  160  ARG   B CA    1 
ATOM   7239  C  C     . ARG   B 1 160 ? 117.910 95.088  130.513 1.00 72.63  ?  160  ARG   B C     1 
ATOM   7240  O  O     . ARG   B 1 160 ? 117.682 95.732  129.484 1.00 78.74  ?  160  ARG   B O     1 
ATOM   7241  C  CB    . ARG   B 1 160 ? 117.474 96.807  132.268 1.00 69.26  ?  160  ARG   B CB    1 
ATOM   7242  C  CG    . ARG   B 1 160 ? 116.591 97.300  133.399 1.00 70.18  ?  160  ARG   B CG    1 
ATOM   7243  C  CD    . ARG   B 1 160 ? 115.129 97.321  132.989 1.00 66.51  ?  160  ARG   B CD    1 
ATOM   7244  N  NE    . ARG   B 1 160 ? 114.254 97.633  134.113 1.00 72.98  ?  160  ARG   B NE    1 
ATOM   7245  C  CZ    . ARG   B 1 160 ? 112.970 97.944  134.000 1.00 74.24  ?  160  ARG   B CZ    1 
ATOM   7246  N  NH1   . ARG   B 1 160 ? 112.374 98.000  132.821 1.00 68.26  ?  160  ARG   B NH1   1 
ATOM   7247  N  NH2   . ARG   B 1 160 ? 112.267 98.202  135.099 1.00 74.39  ?  160  ARG   B NH2   1 
ATOM   7248  N  N     . VAL   B 1 161 ? 118.822 94.123  130.564 1.00 68.95  ?  161  VAL   B N     1 
ATOM   7249  C  CA    . VAL   B 1 161 ? 119.647 93.759  129.417 1.00 62.99  ?  161  VAL   B CA    1 
ATOM   7250  C  C     . VAL   B 1 161 ? 119.143 92.489  128.748 1.00 61.05  ?  161  VAL   B C     1 
ATOM   7251  O  O     . VAL   B 1 161 ? 118.984 92.442  127.529 1.00 69.48  ?  161  VAL   B O     1 
ATOM   7252  C  CB    . VAL   B 1 161 ? 121.123 93.620  129.848 1.00 61.94  ?  161  VAL   B CB    1 
ATOM   7253  C  CG1   . VAL   B 1 161 ? 122.015 93.436  128.634 1.00 64.02  ?  161  VAL   B CG1   1 
ATOM   7254  C  CG2   . VAL   B 1 161 ? 121.545 94.848  130.628 1.00 65.44  ?  161  VAL   B CG2   1 
ATOM   7255  N  N     . THR   B 1 162 ? 118.893 91.444  129.532 1.00 69.18  ?  162  THR   B N     1 
ATOM   7256  C  CA    . THR   B 1 162 ? 118.387 90.188  129.001 1.00 69.02  ?  162  THR   B CA    1 
ATOM   7257  C  C     . THR   B 1 162 ? 116.867 90.144  128.906 1.00 70.02  ?  162  THR   B C     1 
ATOM   7258  O  O     . THR   B 1 162 ? 116.330 89.260  128.230 1.00 75.36  ?  162  THR   B O     1 
ATOM   7259  C  CB    . THR   B 1 162 ? 118.872 89.016  129.861 1.00 72.48  ?  162  THR   B CB    1 
ATOM   7260  O  OG1   . THR   B 1 162 ? 118.022 88.877  131.005 1.00 75.12  ?  162  THR   B OG1   1 
ATOM   7261  C  CG2   . THR   B 1 162 ? 120.304 89.238  130.319 1.00 70.89  ?  162  THR   B CG2   1 
ATOM   7262  N  N     . GLY   B 1 163 ? 116.166 91.069  129.557 1.00 70.97  ?  163  GLY   B N     1 
ATOM   7263  C  CA    . GLY   B 1 163 ? 114.719 91.095  129.514 1.00 73.18  ?  163  GLY   B CA    1 
ATOM   7264  C  C     . GLY   B 1 163 ? 114.027 90.072  130.383 1.00 74.56  ?  163  GLY   B C     1 
ATOM   7265  O  O     . GLY   B 1 163 ? 112.803 89.926  130.283 1.00 81.05  ?  163  GLY   B O     1 
ATOM   7266  N  N     . GLU   B 1 164 ? 114.763 89.362  131.233 1.00 77.32  ?  164  GLU   B N     1 
ATOM   7267  C  CA    . GLU   B 1 164 ? 114.183 88.302  132.045 1.00 79.14  ?  164  GLU   B CA    1 
ATOM   7268  C  C     . GLU   B 1 164 ? 113.490 88.887  133.271 1.00 81.12  ?  164  GLU   B C     1 
ATOM   7269  O  O     . GLU   B 1 164 ? 114.055 89.732  133.971 1.00 86.38  ?  164  GLU   B O     1 
ATOM   7270  C  CB    . GLU   B 1 164 ? 115.269 87.310  132.465 1.00 81.03  ?  164  GLU   B CB    1 
ATOM   7271  C  CG    . GLU   B 1 164 ? 115.005 86.596  133.786 1.00 85.46  ?  164  GLU   B CG    1 
ATOM   7272  C  CD    . GLU   B 1 164 ? 116.001 85.481  134.047 1.00 91.55  ?  164  GLU   B CD    1 
ATOM   7273  O  OE1   . GLU   B 1 164 ? 117.220 85.750  134.022 1.00 91.95  ?  164  GLU   B OE1   1 
ATOM   7274  O  OE2   . GLU   B 1 164 ? 115.568 84.320  134.199 1.00 91.14  ?  164  GLU   B OE2   1 
ATOM   7275  N  N     . ILE   B 1 165 ? 112.262 88.436  133.525 1.00 72.08  ?  165  ILE   B N     1 
ATOM   7276  C  CA    . ILE   B 1 165 ? 111.485 88.859  134.684 1.00 68.81  ?  165  ILE   B CA    1 
ATOM   7277  C  C     . ILE   B 1 165 ? 111.726 87.874  135.818 1.00 72.69  ?  165  ILE   B C     1 
ATOM   7278  O  O     . ILE   B 1 165 ? 112.003 86.692  135.593 1.00 77.95  ?  165  ILE   B O     1 
ATOM   7279  C  CB    . ILE   B 1 165 ? 109.985 88.966  134.335 1.00 65.78  ?  165  ILE   B CB    1 
ATOM   7280  C  CG1   . ILE   B 1 165 ? 109.805 89.551  132.933 1.00 70.97  ?  165  ILE   B CG1   1 
ATOM   7281  C  CG2   . ILE   B 1 165 ? 109.251 89.813  135.361 1.00 66.05  ?  165  ILE   B CG2   1 
ATOM   7282  C  CD1   . ILE   B 1 165 ? 110.053 91.040  132.853 1.00 71.51  ?  165  ILE   B CD1   1 
ATOM   7283  N  N     . TYR   B 1 166 ? 111.619 88.360  137.056 1.00 65.87  ?  166  TYR   B N     1 
ATOM   7284  C  CA    . TYR   B 1 166 ? 111.934 87.552  138.224 1.00 64.57  ?  166  TYR   B CA    1 
ATOM   7285  C  C     . TYR   B 1 166 ? 110.787 87.374  139.206 1.00 72.46  ?  166  TYR   B C     1 
ATOM   7286  O  O     . TYR   B 1 166 ? 110.856 86.461  140.035 1.00 80.41  ?  166  TYR   B O     1 
ATOM   7287  C  CB    . TYR   B 1 166 ? 113.126 88.154  138.987 1.00 62.55  ?  166  TYR   B CB    1 
ATOM   7288  C  CG    . TYR   B 1 166 ? 114.403 88.222  138.185 1.00 65.51  ?  166  TYR   B CG    1 
ATOM   7289  C  CD1   . TYR   B 1 166 ? 115.123 87.074  137.890 1.00 68.45  ?  166  TYR   B CD1   1 
ATOM   7290  C  CD2   . TYR   B 1 166 ? 114.893 89.434  137.732 1.00 68.50  ?  166  TYR   B CD2   1 
ATOM   7291  C  CE1   . TYR   B 1 166 ? 116.292 87.133  137.156 1.00 69.36  ?  166  TYR   B CE1   1 
ATOM   7292  C  CE2   . TYR   B 1 166 ? 116.056 89.503  136.999 1.00 70.47  ?  166  TYR   B CE2   1 
ATOM   7293  C  CZ    . TYR   B 1 166 ? 116.762 88.353  136.725 1.00 72.71  ?  166  TYR   B CZ    1 
ATOM   7294  O  OH    . TYR   B 1 166 ? 117.916 88.419  135.977 1.00 76.58  ?  166  TYR   B OH    1 
ATOM   7295  N  N     . GLU   B 1 167 ? 109.744 88.199  139.145 1.00 71.66  ?  167  GLU   B N     1 
ATOM   7296  C  CA    . GLU   B 1 167 ? 108.723 88.181  140.182 1.00 65.55  ?  167  GLU   B CA    1 
ATOM   7297  C  C     . GLU   B 1 167 ? 107.363 88.503  139.582 1.00 67.51  ?  167  GLU   B C     1 
ATOM   7298  O  O     . GLU   B 1 167 ? 107.259 89.042  138.478 1.00 77.28  ?  167  GLU   B O     1 
ATOM   7299  C  CB    . GLU   B 1 167 ? 109.048 89.180  141.298 1.00 65.94  ?  167  GLU   B CB    1 
ATOM   7300  C  CG    . GLU   B 1 167 ? 109.032 90.625  140.834 1.00 72.03  ?  167  GLU   B CG    1 
ATOM   7301  C  CD    . GLU   B 1 167 ? 109.186 91.610  141.973 1.00 77.02  ?  167  GLU   B CD    1 
ATOM   7302  O  OE1   . GLU   B 1 167 ? 109.192 91.187  143.143 1.00 78.96  ?  167  GLU   B OE1   1 
ATOM   7303  O  OE2   . GLU   B 1 167 ? 109.445 92.794  141.694 1.00 76.90  ?  167  GLU   B OE2   1 
ATOM   7304  N  N     . SER   B 1 168 ? 106.316 88.159  140.331 1.00 66.39  ?  168  SER   B N     1 
ATOM   7305  C  CA    . SER   B 1 168 ? 104.946 88.516  139.999 1.00 70.20  ?  168  SER   B CA    1 
ATOM   7306  C  C     . SER   B 1 168 ? 104.525 89.742  140.806 1.00 76.01  ?  168  SER   B C     1 
ATOM   7307  O  O     . SER   B 1 168 ? 105.309 90.330  141.551 1.00 79.20  ?  168  SER   B O     1 
ATOM   7308  C  CB    . SER   B 1 168 ? 103.998 87.344  140.251 1.00 69.91  ?  168  SER   B CB    1 
ATOM   7309  O  OG    . SER   B 1 168 ? 104.156 86.841  141.563 1.00 81.53  ?  168  SER   B OG    1 
ATOM   7310  N  N     . ALA   B 1 169 ? 103.264 90.141  140.645 1.00 69.68  ?  169  ALA   B N     1 
ATOM   7311  C  CA    . ALA   B 1 169 ? 102.792 91.362  141.288 1.00 69.60  ?  169  ALA   B CA    1 
ATOM   7312  C  C     . ALA   B 1 169 ? 102.532 91.160  142.776 1.00 65.60  ?  169  ALA   B C     1 
ATOM   7313  O  O     . ALA   B 1 169 ? 102.785 92.064  143.582 1.00 75.13  ?  169  ALA   B O     1 
ATOM   7314  C  CB    . ALA   B 1 169 ? 101.530 91.866  140.588 1.00 68.62  ?  169  ALA   B CB    1 
ATOM   7315  N  N     . GLN   B 1 170 ? 102.017 89.992  143.160 1.00 57.92  ?  170  GLN   B N     1 
ATOM   7316  C  CA    . GLN   B 1 170 ? 101.717 89.752  144.568 1.00 57.90  ?  170  GLN   B CA    1 
ATOM   7317  C  C     . GLN   B 1 170 ? 102.988 89.707  145.405 1.00 65.99  ?  170  GLN   B C     1 
ATOM   7318  O  O     . GLN   B 1 170 ? 103.010 90.207  146.536 1.00 69.88  ?  170  GLN   B O     1 
ATOM   7319  C  CB    . GLN   B 1 170 ? 100.917 88.464  144.722 1.00 65.33  ?  170  GLN   B CB    1 
ATOM   7320  C  CG    . GLN   B 1 170 ? 99.559  88.525  144.057 1.00 63.75  ?  170  GLN   B CG    1 
ATOM   7321  C  CD    . GLN   B 1 170 ? 98.796  89.778  144.418 1.00 67.46  ?  170  GLN   B CD    1 
ATOM   7322  O  OE1   . GLN   B 1 170 ? 98.642  90.103  145.593 1.00 75.81  ?  170  GLN   B OE1   1 
ATOM   7323  N  NE2   . GLN   B 1 170 ? 98.267  90.460  143.412 1.00 60.84  ?  170  GLN   B NE2   1 
ATOM   7324  N  N     . PHE   B 1 171 ? 104.055 89.110  144.869 1.00 65.89  ?  171  PHE   B N     1 
ATOM   7325  C  CA    . PHE   B 1 171 ? 105.341 89.156  145.554 1.00 60.03  ?  171  PHE   B CA    1 
ATOM   7326  C  C     . PHE   B 1 171 ? 105.831 90.590  145.689 1.00 66.46  ?  171  PHE   B C     1 
ATOM   7327  O  O     . PHE   B 1 171 ? 106.351 90.979  146.740 1.00 75.01  ?  171  PHE   B O     1 
ATOM   7328  C  CB    . PHE   B 1 171 ? 106.368 88.303  144.810 1.00 57.62  ?  171  PHE   B CB    1 
ATOM   7329  C  CG    . PHE   B 1 171 ? 106.239 86.832  145.077 1.00 62.07  ?  171  PHE   B CG    1 
ATOM   7330  C  CD1   . PHE   B 1 171 ? 105.472 86.371  146.132 1.00 66.48  ?  171  PHE   B CD1   1 
ATOM   7331  C  CD2   . PHE   B 1 171 ? 106.886 85.909  144.274 1.00 64.49  ?  171  PHE   B CD2   1 
ATOM   7332  C  CE1   . PHE   B 1 171 ? 105.351 85.018  146.380 1.00 67.70  ?  171  PHE   B CE1   1 
ATOM   7333  C  CE2   . PHE   B 1 171 ? 106.769 84.555  144.518 1.00 65.22  ?  171  PHE   B CE2   1 
ATOM   7334  C  CZ    . PHE   B 1 171 ? 106.000 84.110  145.573 1.00 66.15  ?  171  PHE   B CZ    1 
ATOM   7335  N  N     . LEU   B 1 172 ? 105.660 91.393  144.636 1.00 57.84  ?  172  LEU   B N     1 
ATOM   7336  C  CA    . LEU   B 1 172 ? 106.006 92.810  144.703 1.00 55.02  ?  172  LEU   B CA    1 
ATOM   7337  C  C     . LEU   B 1 172 ? 105.288 93.494  145.861 1.00 59.36  ?  172  LEU   B C     1 
ATOM   7338  O  O     . LEU   B 1 172 ? 105.916 94.168  146.687 1.00 68.33  ?  172  LEU   B O     1 
ATOM   7339  C  CB    . LEU   B 1 172 ? 105.656 93.483  143.373 1.00 53.84  ?  172  LEU   B CB    1 
ATOM   7340  C  CG    . LEU   B 1 172 ? 106.034 94.939  143.086 1.00 58.99  ?  172  LEU   B CG    1 
ATOM   7341  C  CD1   . LEU   B 1 172 ? 106.183 95.141  141.590 1.00 66.15  ?  172  LEU   B CD1   1 
ATOM   7342  C  CD2   . LEU   B 1 172 ? 105.003 95.908  143.641 1.00 55.72  ?  172  LEU   B CD2   1 
ATOM   7343  N  N     . TYR   B 1 173 ? 103.968 93.317  145.943 1.00 60.17  ?  173  TYR   B N     1 
ATOM   7344  C  CA    . TYR   B 1 173 ? 103.185 93.994  146.973 1.00 52.88  ?  173  TYR   B CA    1 
ATOM   7345  C  C     . TYR   B 1 173 ? 103.580 93.525  148.366 1.00 58.42  ?  173  TYR   B C     1 
ATOM   7346  O  O     . TYR   B 1 173 ? 103.806 94.342  149.270 1.00 68.36  ?  173  TYR   B O     1 
ATOM   7347  C  CB    . TYR   B 1 173 ? 101.694 93.758  146.734 1.00 55.53  ?  173  TYR   B CB    1 
ATOM   7348  C  CG    . TYR   B 1 173 ? 101.106 94.622  145.646 1.00 60.33  ?  173  TYR   B CG    1 
ATOM   7349  C  CD1   . TYR   B 1 173 ? 101.525 95.932  145.473 1.00 61.12  ?  173  TYR   B CD1   1 
ATOM   7350  C  CD2   . TYR   B 1 173 ? 100.130 94.128  144.794 1.00 61.91  ?  173  TYR   B CD2   1 
ATOM   7351  C  CE1   . TYR   B 1 173 ? 100.989 96.725  144.482 1.00 62.86  ?  173  TYR   B CE1   1 
ATOM   7352  C  CE2   . TYR   B 1 173 ? 99.589  94.914  143.799 1.00 62.86  ?  173  TYR   B CE2   1 
ATOM   7353  C  CZ    . TYR   B 1 173 ? 100.022 96.212  143.648 1.00 66.33  ?  173  TYR   B CZ    1 
ATOM   7354  O  OH    . TYR   B 1 173 ? 99.486  97.001  142.658 1.00 69.96  ?  173  TYR   B OH    1 
ATOM   7355  N  N     . ILE   B 1 174 ? 103.667 92.208  148.562 1.00 54.10  ?  174  ILE   B N     1 
ATOM   7356  C  CA    . ILE   B 1 174 ? 103.960 91.695  149.892 1.00 51.82  ?  174  ILE   B CA    1 
ATOM   7357  C  C     . ILE   B 1 174 ? 105.367 92.076  150.324 1.00 57.13  ?  174  ILE   B C     1 
ATOM   7358  O  O     . ILE   B 1 174 ? 105.601 92.355  151.503 1.00 64.99  ?  174  ILE   B O     1 
ATOM   7359  C  CB    . ILE   B 1 174 ? 103.735 90.176  149.963 1.00 55.90  ?  174  ILE   B CB    1 
ATOM   7360  C  CG1   . ILE   B 1 174 ? 103.665 89.759  151.428 1.00 56.94  ?  174  ILE   B CG1   1 
ATOM   7361  C  CG2   . ILE   B 1 174 ? 104.840 89.417  149.237 1.00 58.02  ?  174  ILE   B CG2   1 
ATOM   7362  C  CD1   . ILE   B 1 174 ? 102.268 89.668  151.997 1.00 58.20  ?  174  ILE   B CD1   1 
ATOM   7363  N  N     . LEU   B 1 175 ? 106.321 92.130  149.394 1.00 56.58  ?  175  LEU   B N     1 
ATOM   7364  C  CA    . LEU   B 1 175 ? 107.673 92.494  149.780 1.00 57.52  ?  175  LEU   B CA    1 
ATOM   7365  C  C     . LEU   B 1 175 ? 107.810 93.986  150.026 1.00 64.01  ?  175  LEU   B C     1 
ATOM   7366  O  O     . LEU   B 1 175 ? 108.572 94.385  150.908 1.00 76.28  ?  175  LEU   B O     1 
ATOM   7367  C  CB    . LEU   B 1 175 ? 108.666 92.020  148.723 1.00 57.20  ?  175  LEU   B CB    1 
ATOM   7368  C  CG    . LEU   B 1 175 ? 108.904 90.511  148.789 1.00 58.66  ?  175  LEU   B CG    1 
ATOM   7369  C  CD1   . LEU   B 1 175 ? 110.177 90.163  148.084 1.00 63.87  ?  175  LEU   B CD1   1 
ATOM   7370  C  CD2   . LEU   B 1 175 ? 108.951 90.025  150.232 1.00 55.78  ?  175  LEU   B CD2   1 
ATOM   7371  N  N     . VAL   B 1 176 ? 107.067 94.821  149.297 1.00 60.42  ?  176  VAL   B N     1 
ATOM   7372  C  CA    . VAL   B 1 176 ? 107.031 96.243  149.630 1.00 51.25  ?  176  VAL   B CA    1 
ATOM   7373  C  C     . VAL   B 1 176 ? 106.471 96.436  151.035 1.00 49.91  ?  176  VAL   B C     1 
ATOM   7374  O  O     . VAL   B 1 176 ? 107.026 97.183  151.851 1.00 59.91  ?  176  VAL   B O     1 
ATOM   7375  C  CB    . VAL   B 1 176 ? 106.216 97.022  148.581 1.00 49.69  ?  176  VAL   B CB    1 
ATOM   7376  C  CG1   . VAL   B 1 176 ? 105.859 98.403  149.102 1.00 49.17  ?  176  VAL   B CG1   1 
ATOM   7377  C  CG2   . VAL   B 1 176 ? 106.993 97.133  147.283 1.00 53.07  ?  176  VAL   B CG2   1 
ATOM   7378  N  N     . ALA   B 1 177 ? 105.378 95.736  151.346 1.00 51.31  ?  177  ALA   B N     1 
ATOM   7379  C  CA    . ALA   B 1 177 ? 104.774 95.857  152.669 1.00 52.41  ?  177  ALA   B CA    1 
ATOM   7380  C  C     . ALA   B 1 177 ? 105.706 95.352  153.766 1.00 54.87  ?  177  ALA   B C     1 
ATOM   7381  O  O     . ALA   B 1 177 ? 105.823 95.979  154.823 1.00 65.32  ?  177  ALA   B O     1 
ATOM   7382  C  CB    . ALA   B 1 177 ? 103.444 95.111  152.705 1.00 54.39  ?  177  ALA   B CB    1 
ATOM   7383  N  N     . ALA   B 1 178 ? 106.390 94.230  153.526 1.00 57.29  ?  178  ALA   B N     1 
ATOM   7384  C  CA    . ALA   B 1 178 ? 107.278 93.663  154.534 1.00 62.33  ?  178  ALA   B CA    1 
ATOM   7385  C  C     . ALA   B 1 178 ? 108.560 94.467  154.681 1.00 63.89  ?  178  ALA   B C     1 
ATOM   7386  O  O     . ALA   B 1 178 ? 109.165 94.469  155.758 1.00 70.91  ?  178  ALA   B O     1 
ATOM   7387  C  CB    . ALA   B 1 178 ? 107.603 92.214  154.183 1.00 58.60  ?  178  ALA   B CB    1 
ATOM   7388  N  N     . CYS   B 1 179 ? 108.985 95.153  153.620 1.00 62.19  ?  179  CYS   B N     1 
ATOM   7389  C  CA    . CYS   B 1 179 ? 110.217 95.922  153.646 1.00 65.26  ?  179  CYS   B CA    1 
ATOM   7390  C  C     . CYS   B 1 179 ? 110.009 97.316  154.219 1.00 70.77  ?  179  CYS   B C     1 
ATOM   7391  O  O     . CYS   B 1 179 ? 110.948 97.900  154.770 1.00 76.31  ?  179  CYS   B O     1 
ATOM   7392  C  CB    . CYS   B 1 179 ? 110.785 96.010  152.230 1.00 68.34  ?  179  CYS   B CB    1 
ATOM   7393  S  SG    . CYS   B 1 179 ? 112.468 96.610  152.149 1.00 84.97  ?  179  CYS   B SG    1 
ATOM   7394  N  N     . LEU   B 1 180 ? 108.802 97.869  154.091 1.00 63.13  ?  180  LEU   B N     1 
ATOM   7395  C  CA    . LEU   B 1 180 ? 108.530 99.162  154.709 1.00 55.17  ?  180  LEU   B CA    1 
ATOM   7396  C  C     . LEU   B 1 180 ? 108.398 99.037  156.222 1.00 55.12  ?  180  LEU   B C     1 
ATOM   7397  O  O     . LEU   B 1 180 ? 108.891 99.892  156.964 1.00 70.37  ?  180  LEU   B O     1 
ATOM   7398  C  CB    . LEU   B 1 180 ? 107.269 99.777  154.107 1.00 51.50  ?  180  LEU   B CB    1 
ATOM   7399  C  CG    . LEU   B 1 180 ? 107.441 100.332 152.694 1.00 58.64  ?  180  LEU   B CG    1 
ATOM   7400  C  CD1   . LEU   B 1 180 ? 106.216 101.114 152.255 1.00 62.83  ?  180  LEU   B CD1   1 
ATOM   7401  C  CD2   . LEU   B 1 180 ? 108.690 101.190 152.604 1.00 58.64  ?  180  LEU   B CD2   1 
ATOM   7402  N  N     . PHE   B 1 181 ? 107.753 97.973  156.700 1.00 51.02  ?  181  PHE   B N     1 
ATOM   7403  C  CA    . PHE   B 1 181 ? 107.520 97.770  158.125 1.00 58.83  ?  181  PHE   B CA    1 
ATOM   7404  C  C     . PHE   B 1 181 ? 108.555 96.847  158.760 1.00 62.52  ?  181  PHE   B C     1 
ATOM   7405  O  O     . PHE   B 1 181 ? 108.259 96.185  159.759 1.00 67.34  ?  181  PHE   B O     1 
ATOM   7406  C  CB    . PHE   B 1 181 ? 106.113 97.220  158.358 1.00 62.17  ?  181  PHE   B CB    1 
ATOM   7407  C  CG    . PHE   B 1 181 ? 105.020 98.199  158.046 1.00 63.69  ?  181  PHE   B CG    1 
ATOM   7408  C  CD1   . PHE   B 1 181 ? 104.626 99.137  158.983 1.00 62.14  ?  181  PHE   B CD1   1 
ATOM   7409  C  CD2   . PHE   B 1 181 ? 104.387 98.182  156.816 1.00 63.43  ?  181  PHE   B CD2   1 
ATOM   7410  C  CE1   . PHE   B 1 181 ? 103.621 100.040 158.699 1.00 63.40  ?  181  PHE   B CE1   1 
ATOM   7411  C  CE2   . PHE   B 1 181 ? 103.384 99.083  156.527 1.00 61.40  ?  181  PHE   B CE2   1 
ATOM   7412  C  CZ    . PHE   B 1 181 ? 103.000 100.013 157.469 1.00 59.10  ?  181  PHE   B CZ    1 
ATOM   7413  N  N     . SER   B 1 182 ? 109.766 96.792  158.203 1.00 67.12  ?  182  SER   B N     1 
ATOM   7414  C  CA    . SER   B 1 182 ? 110.773 95.867  158.716 1.00 67.72  ?  182  SER   B CA    1 
ATOM   7415  C  C     . SER   B 1 182 ? 111.214 96.237  160.128 1.00 74.42  ?  182  SER   B C     1 
ATOM   7416  O  O     . SER   B 1 182 ? 111.424 95.354  160.968 1.00 75.87  ?  182  SER   B O     1 
ATOM   7417  C  CB    . SER   B 1 182 ? 111.975 95.826  157.773 1.00 69.10  ?  182  SER   B CB    1 
ATOM   7418  O  OG    . SER   B 1 182 ? 112.317 97.125  157.324 1.00 79.62  ?  182  SER   B OG    1 
ATOM   7419  N  N     . ASN   B 1 183 ? 111.358 97.529  160.410 1.00 80.10  ?  183  ASN   B N     1 
ATOM   7420  C  CA    . ASN   B 1 183 ? 111.898 97.993  161.681 1.00 76.11  ?  183  ASN   B CA    1 
ATOM   7421  C  C     . ASN   B 1 183 ? 110.850 98.103  162.780 1.00 78.28  ?  183  ASN   B C     1 
ATOM   7422  O  O     . ASN   B 1 183 ? 111.192 98.492  163.901 1.00 85.62  ?  183  ASN   B O     1 
ATOM   7423  C  CB    . ASN   B 1 183 ? 112.585 99.350  161.496 1.00 76.43  ?  183  ASN   B CB    1 
ATOM   7424  C  CG    . ASN   B 1 183 ? 113.883 99.245  160.725 1.00 88.73  ?  183  ASN   B CG    1 
ATOM   7425  O  OD1   . ASN   B 1 183 ? 114.131 100.016 159.797 1.00 90.90  ?  183  ASN   B OD1   1 
ATOM   7426  N  ND2   . ASN   B 1 183 ? 114.716 98.280  161.096 1.00 87.08  ?  183  ASN   B ND2   1 
ATOM   7427  N  N     . TYR   B 1 184 ? 109.594 97.776  162.494 1.00 74.49  ?  184  TYR   B N     1 
ATOM   7428  C  CA    . TYR   B 1 184 ? 108.549 97.895  163.492 1.00 75.78  ?  184  TYR   B CA    1 
ATOM   7429  C  C     . TYR   B 1 184 ? 108.716 96.830  164.574 1.00 80.71  ?  184  TYR   B C     1 
ATOM   7430  O  O     . TYR   B 1 184 ? 109.369 95.808  164.357 1.00 83.97  ?  184  TYR   B O     1 
ATOM   7431  C  CB    . TYR   B 1 184 ? 107.176 97.781  162.835 1.00 75.43  ?  184  TYR   B CB    1 
ATOM   7432  C  CG    . TYR   B 1 184 ? 106.567 99.125  162.527 1.00 76.50  ?  184  TYR   B CG    1 
ATOM   7433  C  CD1   . TYR   B 1 184 ? 107.284 100.080 161.823 1.00 75.68  ?  184  TYR   B CD1   1 
ATOM   7434  C  CD2   . TYR   B 1 184 ? 105.287 99.447  162.952 1.00 74.70  ?  184  TYR   B CD2   1 
ATOM   7435  C  CE1   . TYR   B 1 184 ? 106.743 101.314 161.542 1.00 76.25  ?  184  TYR   B CE1   1 
ATOM   7436  C  CE2   . TYR   B 1 184 ? 104.736 100.683 162.674 1.00 76.76  ?  184  TYR   B CE2   1 
ATOM   7437  C  CZ    . TYR   B 1 184 ? 105.471 101.612 161.969 1.00 78.57  ?  184  TYR   B CZ    1 
ATOM   7438  O  OH    . TYR   B 1 184 ? 104.935 102.845 161.686 1.00 83.05  ?  184  TYR   B OH    1 
ATOM   7439  N  N     . PRO   B 1 185 ? 108.153 97.065  165.761 1.00 88.01  ?  185  PRO   B N     1 
ATOM   7440  C  CA    . PRO   B 1 185 ? 108.239 96.061  166.829 1.00 86.41  ?  185  PRO   B CA    1 
ATOM   7441  C  C     . PRO   B 1 185 ? 107.664 94.725  166.382 1.00 88.80  ?  185  PRO   B C     1 
ATOM   7442  O  O     . PRO   B 1 185 ? 106.658 94.666  165.673 1.00 95.29  ?  185  PRO   B O     1 
ATOM   7443  C  CB    . PRO   B 1 185 ? 107.413 96.679  167.961 1.00 85.64  ?  185  PRO   B CB    1 
ATOM   7444  C  CG    . PRO   B 1 185 ? 107.505 98.143  167.727 1.00 86.46  ?  185  PRO   B CG    1 
ATOM   7445  C  CD    . PRO   B 1 185 ? 107.625 98.350  166.247 1.00 86.77  ?  185  PRO   B CD    1 
ATOM   7446  N  N     . ARG   B 1 186 ? 108.319 93.645  166.815 1.00 97.84  ?  186  ARG   B N     1 
ATOM   7447  C  CA    . ARG   B 1 186 ? 107.965 92.307  166.352 1.00 100.92 ?  186  ARG   B CA    1 
ATOM   7448  C  C     . ARG   B 1 186 ? 106.548 91.906  166.741 1.00 102.95 ?  186  ARG   B C     1 
ATOM   7449  O  O     . ARG   B 1 186 ? 105.987 90.990  166.131 1.00 106.99 ?  186  ARG   B O     1 
ATOM   7450  C  CB    . ARG   B 1 186 ? 108.965 91.288  166.902 1.00 101.08 ?  186  ARG   B CB    1 
ATOM   7451  C  CG    . ARG   B 1 186 ? 109.887 90.691  165.854 1.00 102.67 ?  186  ARG   B CG    1 
ATOM   7452  C  CD    . ARG   B 1 186 ? 111.046 91.625  165.545 1.00 103.70 ?  186  ARG   B CD    1 
ATOM   7453  N  NE    . ARG   B 1 186 ? 111.995 91.030  164.612 1.00 107.80 ?  186  ARG   B NE    1 
ATOM   7454  C  CZ    . ARG   B 1 186 ? 113.014 91.678  164.065 1.00 107.35 ?  186  ARG   B CZ    1 
ATOM   7455  N  NH1   . ARG   B 1 186 ? 113.247 92.952  164.334 1.00 105.39 ?  186  ARG   B NH1   1 
ATOM   7456  N  NH2   . ARG   B 1 186 ? 113.795 91.042  163.195 1.00 104.03 ?  186  ARG   B NH2   1 
ATOM   7457  N  N     . GLU   B 1 187 ? 105.953 92.576  167.729 1.00 111.73 ?  187  GLU   B N     1 
ATOM   7458  C  CA    . GLU   B 1 187 ? 104.622 92.197  168.196 1.00 112.51 ?  187  GLU   B CA    1 
ATOM   7459  C  C     . GLU   B 1 187 ? 103.562 92.612  167.198 1.00 113.20 ?  187  GLU   B C     1 
ATOM   7460  O  O     . GLU   B 1 187 ? 102.617 91.859  166.938 1.00 113.63 ?  187  GLU   B O     1 
ATOM   7461  C  CB    . GLU   B 1 187 ? 104.321 92.837  169.550 1.00 109.95 ?  187  GLU   B CB    1 
ATOM   7462  C  CG    . GLU   B 1 187 ? 105.162 92.312  170.694 1.00 114.11 ?  187  GLU   B CG    1 
ATOM   7463  C  CD    . GLU   B 1 187 ? 106.594 92.025  170.288 1.00 117.30 ?  187  GLU   B CD    1 
ATOM   7464  O  OE1   . GLU   B 1 187 ? 107.228 92.908  169.665 1.00 116.26 ?  187  GLU   B OE1   1 
ATOM   7465  O  OE2   . GLU   B 1 187 ? 107.080 90.912  170.565 1.00 117.06 ?  187  GLU   B OE2   1 
ATOM   7466  N  N     . THR   B 1 188 ? 103.703 93.810  166.635 1.00 95.12  ?  188  THR   B N     1 
ATOM   7467  C  CA    . THR   B 1 188 ? 102.730 94.381  165.717 1.00 93.25  ?  188  THR   B CA    1 
ATOM   7468  C  C     . THR   B 1 188 ? 103.264 94.520  164.297 1.00 93.75  ?  188  THR   B C     1 
ATOM   7469  O  O     . THR   B 1 188 ? 102.597 95.130  163.456 1.00 98.44  ?  188  THR   B O     1 
ATOM   7470  C  CB    . THR   B 1 188 ? 102.259 95.747  166.227 1.00 94.78  ?  188  THR   B CB    1 
ATOM   7471  O  OG1   . THR   B 1 188 ? 103.280 96.727  165.998 1.00 92.14  ?  188  THR   B OG1   1 
ATOM   7472  C  CG2   . THR   B 1 188 ? 101.943 95.687  167.715 1.00 96.07  ?  188  THR   B CG2   1 
ATOM   7473  N  N     . ARG   B 1 189 ? 104.444 93.968  164.006 1.00 77.99  ?  189  ARG   B N     1 
ATOM   7474  C  CA    . ARG   B 1 189 ? 105.027 94.120  162.676 1.00 74.54  ?  189  ARG   B CA    1 
ATOM   7475  C  C     . ARG   B 1 189 ? 104.198 93.401  161.618 1.00 79.81  ?  189  ARG   B C     1 
ATOM   7476  O  O     . ARG   B 1 189 ? 103.842 93.987  160.588 1.00 85.44  ?  189  ARG   B O     1 
ATOM   7477  C  CB    . ARG   B 1 189 ? 106.464 93.601  162.674 1.00 73.07  ?  189  ARG   B CB    1 
ATOM   7478  C  CG    . ARG   B 1 189 ? 107.170 93.744  161.343 1.00 74.89  ?  189  ARG   B CG    1 
ATOM   7479  C  CD    . ARG   B 1 189 ? 108.659 93.494  161.485 1.00 76.36  ?  189  ARG   B CD    1 
ATOM   7480  N  NE    . ARG   B 1 189 ? 108.944 92.130  161.910 1.00 73.48  ?  189  ARG   B NE    1 
ATOM   7481  C  CZ    . ARG   B 1 189 ? 110.079 91.492  161.663 1.00 76.59  ?  189  ARG   B CZ    1 
ATOM   7482  N  NH1   . ARG   B 1 189 ? 111.067 92.071  161.000 1.00 76.14  ?  189  ARG   B NH1   1 
ATOM   7483  N  NH2   . ARG   B 1 189 ? 110.227 90.242  162.092 1.00 81.02  ?  189  ARG   B NH2   1 
ATOM   7484  N  N     . LEU   B 1 190 ? 103.873 92.129  161.858 1.00 80.79  ?  190  LEU   B N     1 
ATOM   7485  C  CA    . LEU   B 1 190 ? 103.190 91.340  160.839 1.00 77.07  ?  190  LEU   B CA    1 
ATOM   7486  C  C     . LEU   B 1 190 ? 101.761 91.816  160.614 1.00 80.35  ?  190  LEU   B C     1 
ATOM   7487  O  O     . LEU   B 1 190 ? 101.257 91.732  159.489 1.00 84.17  ?  190  LEU   B O     1 
ATOM   7488  C  CB    . LEU   B 1 190 ? 103.212 89.860  161.215 1.00 71.59  ?  190  LEU   B CB    1 
ATOM   7489  C  CG    . LEU   B 1 190 ? 104.535 89.154  160.907 1.00 74.86  ?  190  LEU   B CG    1 
ATOM   7490  C  CD1   . LEU   B 1 190 ? 104.427 87.660  161.162 1.00 77.60  ?  190  LEU   B CD1   1 
ATOM   7491  C  CD2   . LEU   B 1 190 ? 104.967 89.431  159.472 1.00 77.99  ?  190  LEU   B CD2   1 
ATOM   7492  N  N     . GLN   B 1 191 ? 101.179 92.315  161.672 1.00 83.08  ?  191  GLN   B N     1 
ATOM   7493  C  CA    A GLN   B 1 191 ? 99.766  92.889  161.461 0.50 78.75  ?  191  GLN   B CA    1 
ATOM   7494  C  CA    B GLN   B 1 191 ? 99.830  92.886  161.541 0.50 78.75  ?  191  GLN   B CA    1 
ATOM   7495  C  C     . GLN   B 1 191 ? 99.834  94.113  160.590 1.00 83.72  ?  191  GLN   B C     1 
ATOM   7496  O  O     . GLN   B 1 191 ? 98.954  94.343  159.718 1.00 90.45  ?  191  GLN   B O     1 
ATOM   7497  C  CB    A GLN   B 1 191 ? 99.157  93.283  162.808 0.50 81.51  ?  191  GLN   B CB    1 
ATOM   7498  C  CB    B GLN   B 1 191 ? 99.261  93.115  162.938 0.50 81.51  ?  191  GLN   B CB    1 
ATOM   7499  C  CG    A GLN   B 1 191 ? 99.192  92.185  163.847 0.50 88.23  ?  191  GLN   B CG    1 
ATOM   7500  C  CG    B GLN   B 1 191 ? 98.771  91.843  163.605 0.50 88.23  ?  191  GLN   B CG    1 
ATOM   7501  C  CD    A GLN   B 1 191 ? 98.650  92.624  165.196 0.50 93.45  ?  191  GLN   B CD    1 
ATOM   7502  C  CD    B GLN   B 1 191 ? 99.915  91.049  164.182 0.50 93.45  ?  191  GLN   B CD    1 
ATOM   7503  O  OE1   A GLN   B 1 191 ? 98.864  93.765  165.578 0.50 97.20  ?  191  GLN   B OE1   1 
ATOM   7504  O  OE1   B GLN   B 1 191 ? 100.171 89.915  163.787 0.50 97.20  ?  191  GLN   B OE1   1 
ATOM   7505  N  NE2   A GLN   B 1 191 ? 98.065  91.697  165.971 0.50 89.20  ?  191  GLN   B NE2   1 
ATOM   7506  N  NE2   B GLN   B 1 191 ? 100.619 91.648  165.127 0.50 89.20  ?  191  GLN   B NE2   1 
ATOM   7507  N  N     . TYR   B 1 192 ? 100.812 94.967  160.725 1.00 68.66  ?  192  TYR   B N     1 
ATOM   7508  C  CA    . TYR   B 1 192 ? 100.974 96.115  159.841 1.00 65.69  ?  192  TYR   B CA    1 
ATOM   7509  C  C     . TYR   B 1 192 ? 101.313 95.677  158.423 1.00 73.98  ?  192  TYR   B C     1 
ATOM   7510  O  O     . TYR   B 1 192 ? 100.814 96.258  157.453 1.00 79.74  ?  192  TYR   B O     1 
ATOM   7511  C  CB    . TYR   B 1 192 ? 102.051 97.051  160.387 1.00 65.75  ?  192  TYR   B CB    1 
ATOM   7512  C  CG    . TYR   B 1 192 ? 101.532 98.065  161.377 1.00 70.48  ?  192  TYR   B CG    1 
ATOM   7513  C  CD1   . TYR   B 1 192 ? 100.580 99.006  161.003 1.00 71.14  ?  192  TYR   B CD1   1 
ATOM   7514  C  CD2   . TYR   B 1 192 ? 101.996 98.079  162.685 1.00 75.76  ?  192  TYR   B CD2   1 
ATOM   7515  C  CE1   . TYR   B 1 192 ? 100.104 99.934  161.905 1.00 72.79  ?  192  TYR   B CE1   1 
ATOM   7516  C  CE2   . TYR   B 1 192 ? 101.538 99.001  163.591 1.00 75.51  ?  192  TYR   B CE2   1 
ATOM   7517  C  CZ    . TYR   B 1 192 ? 100.581 99.926  163.200 1.00 74.69  ?  192  TYR   B CZ    1 
ATOM   7518  O  OH    . TYR   B 1 192 ? 100.105 100.856 164.098 1.00 78.98  ?  192  TYR   B OH    1 
ATOM   7519  N  N     . VAL   B 1 193 ? 102.163 94.655  158.282 1.00 69.15  ?  193  VAL   B N     1 
ATOM   7520  C  CA    . VAL   B 1 193 ? 102.501 94.146  156.953 1.00 62.42  ?  193  VAL   B CA    1 
ATOM   7521  C  C     . VAL   B 1 193 ? 101.253 93.635  156.248 1.00 63.76  ?  193  VAL   B C     1 
ATOM   7522  O  O     . VAL   B 1 193 ? 101.016 93.935  155.072 1.00 72.92  ?  193  VAL   B O     1 
ATOM   7523  C  CB    . VAL   B 1 193 ? 103.585 93.057  157.046 1.00 62.46  ?  193  VAL   B CB    1 
ATOM   7524  C  CG1   . VAL   B 1 193 ? 103.892 92.501  155.671 1.00 66.91  ?  193  VAL   B CG1   1 
ATOM   7525  C  CG2   . VAL   B 1 193 ? 104.854 93.661  157.613 1.00 62.65  ?  193  VAL   B CG2   1 
ATOM   7526  N  N     . LYS   B 1 194 ? 100.435 92.859  156.960 1.00 63.81  ?  194  LYS   B N     1 
ATOM   7527  C  CA    . LYS   B 1 194 ? 99.220  92.320  156.359 1.00 62.62  ?  194  LYS   B CA    1 
ATOM   7528  C  C     . LYS   B 1 194 ? 98.254  93.430  155.969 1.00 70.22  ?  194  LYS   B C     1 
ATOM   7529  O  O     . LYS   B 1 194 ? 97.672  93.399  154.878 1.00 76.55  ?  194  LYS   B O     1 
ATOM   7530  C  CB    . LYS   B 1 194 ? 98.545  91.341  157.317 1.00 65.77  ?  194  LYS   B CB    1 
ATOM   7531  C  CG    . LYS   B 1 194 ? 97.237  90.784  156.785 1.00 71.14  ?  194  LYS   B CG    1 
ATOM   7532  C  CD    . LYS   B 1 194 ? 96.630  89.767  157.733 1.00 73.68  ?  194  LYS   B CD    1 
ATOM   7533  C  CE    . LYS   B 1 194 ? 95.228  89.388  157.292 1.00 73.48  ?  194  LYS   B CE    1 
ATOM   7534  N  NZ    . LYS   B 1 194 ? 95.176  89.071  155.840 1.00 72.34  ?  194  LYS   B NZ    1 
ATOM   7535  N  N     . ARG   B 1 195 ? 98.068  94.420  156.845 1.00 73.08  ?  195  ARG   B N     1 
ATOM   7536  C  CA    . ARG   B 1 195 ? 97.137  95.501  156.535 1.00 68.46  ?  195  ARG   B CA    1 
ATOM   7537  C  C     . ARG   B 1 195 ? 97.620  96.329  155.349 1.00 70.79  ?  195  ARG   B C     1 
ATOM   7538  O  O     . ARG   B 1 195 ? 96.824  96.685  154.472 1.00 71.33  ?  195  ARG   B O     1 
ATOM   7539  C  CB    . ARG   B 1 195 ? 96.913  96.374  157.769 1.00 63.93  ?  195  ARG   B CB    1 
ATOM   7540  C  CG    . ARG   B 1 195 ? 96.254  95.622  158.916 1.00 68.38  ?  195  ARG   B CG    1 
ATOM   7541  C  CD    . ARG   B 1 195 ? 95.311  96.496  159.722 1.00 72.47  ?  195  ARG   B CD    1 
ATOM   7542  N  NE    . ARG   B 1 195 ? 95.846  97.830  159.962 1.00 72.78  ?  195  ARG   B NE    1 
ATOM   7543  C  CZ    . ARG   B 1 195 ? 96.619  98.153  160.990 1.00 77.50  ?  195  ARG   B CZ    1 
ATOM   7544  N  NH1   . ARG   B 1 195 ? 96.988  97.252  161.886 1.00 77.70  ?  195  ARG   B NH1   1 
ATOM   7545  N  NH2   . ARG   B 1 195 ? 97.031  99.410  161.122 1.00 74.59  ?  195  ARG   B NH2   1 
ATOM   7546  N  N     . PHE   B 1 196 ? 98.921  96.627  155.285 1.00 58.94  ?  196  PHE   B N     1 
ATOM   7547  C  CA    . PHE   B 1 196 ? 99.438  97.375  154.144 1.00 57.05  ?  196  PHE   B CA    1 
ATOM   7548  C  C     . PHE   B 1 196 ? 99.328  96.575  152.853 1.00 63.05  ?  196  PHE   B C     1 
ATOM   7549  O  O     . PHE   B 1 196 ? 98.989  97.133  151.801 1.00 74.18  ?  196  PHE   B O     1 
ATOM   7550  C  CB    . PHE   B 1 196 ? 100.885 97.791  154.382 1.00 53.20  ?  196  PHE   B CB    1 
ATOM   7551  C  CG    . PHE   B 1 196 ? 101.337 98.912  153.494 1.00 59.94  ?  196  PHE   B CG    1 
ATOM   7552  C  CD1   . PHE   B 1 196 ? 100.613 100.089 153.430 1.00 62.32  ?  196  PHE   B CD1   1 
ATOM   7553  C  CD2   . PHE   B 1 196 ? 102.472 98.786  152.712 1.00 62.88  ?  196  PHE   B CD2   1 
ATOM   7554  C  CE1   . PHE   B 1 196 ? 101.007 101.113 152.601 1.00 62.18  ?  196  PHE   B CE1   1 
ATOM   7555  C  CE2   . PHE   B 1 196 ? 102.875 99.818  151.884 1.00 60.00  ?  196  PHE   B CE2   1 
ATOM   7556  C  CZ    . PHE   B 1 196 ? 102.164 100.997 151.866 1.00 61.02  ?  196  PHE   B CZ    1 
ATOM   7557  N  N     . TYR   B 1 197 ? 99.625  95.273  152.905 1.00 57.44  ?  197  TYR   B N     1 
ATOM   7558  C  CA    . TYR   B 1 197 ? 99.503  94.449  151.708 1.00 57.55  ?  197  TYR   B CA    1 
ATOM   7559  C  C     . TYR   B 1 197 ? 98.061  94.396  151.227 1.00 59.75  ?  197  TYR   B C     1 
ATOM   7560  O  O     . TYR   B 1 197 ? 97.798  94.484  150.023 1.00 71.15  ?  197  TYR   B O     1 
ATOM   7561  C  CB    . TYR   B 1 197 ? 100.024 93.037  151.974 1.00 58.27  ?  197  TYR   B CB    1 
ATOM   7562  C  CG    . TYR   B 1 197 ? 99.580  92.034  150.933 1.00 58.62  ?  197  TYR   B CG    1 
ATOM   7563  C  CD1   . TYR   B 1 197 ? 100.198 91.976  149.693 1.00 58.88  ?  197  TYR   B CD1   1 
ATOM   7564  C  CD2   . TYR   B 1 197 ? 98.537  91.154  151.186 1.00 57.97  ?  197  TYR   B CD2   1 
ATOM   7565  C  CE1   . TYR   B 1 197 ? 99.794  91.068  148.737 1.00 58.45  ?  197  TYR   B CE1   1 
ATOM   7566  C  CE2   . TYR   B 1 197 ? 98.124  90.246  150.234 1.00 58.31  ?  197  TYR   B CE2   1 
ATOM   7567  C  CZ    . TYR   B 1 197 ? 98.768  90.195  149.017 1.00 60.15  ?  197  TYR   B CZ    1 
ATOM   7568  O  OH    . TYR   B 1 197 ? 98.351  89.297  148.063 1.00 67.25  ?  197  TYR   B OH    1 
ATOM   7569  N  N     . ASP   B 1 198 ? 97.113  94.240  152.153 1.00 62.28  ?  198  ASP   B N     1 
ATOM   7570  C  CA    . ASP   B 1 198 ? 95.705  94.236  151.776 1.00 63.31  ?  198  ASP   B CA    1 
ATOM   7571  C  C     . ASP   B 1 198 ? 95.277  95.590  151.227 1.00 65.00  ?  198  ASP   B C     1 
ATOM   7572  O  O     . ASP   B 1 198 ? 94.403  95.658  150.356 1.00 70.99  ?  198  ASP   B O     1 
ATOM   7573  C  CB    . ASP   B 1 198 ? 94.839  93.834  152.976 1.00 67.95  ?  198  ASP   B CB    1 
ATOM   7574  C  CG    . ASP   B 1 198 ? 94.853  92.343  153.219 1.00 80.51  ?  198  ASP   B CG    1 
ATOM   7575  O  OD1   . ASP   B 1 198 ? 95.132  91.644  152.222 1.00 80.47  ?  198  ASP   B OD1   1 
ATOM   7576  O  OD2   . ASP   B 1 198 ? 94.623  91.910  154.378 1.00 82.70  ?  198  ASP   B OD2   1 
ATOM   7577  N  N     . ALA   B 1 199 ? 95.875  96.675  151.722 1.00 64.51  ?  199  ALA   B N     1 
ATOM   7578  C  CA    . ALA   B 1 199 ? 95.545  97.997  151.203 1.00 57.69  ?  199  ALA   B CA    1 
ATOM   7579  C  C     . ALA   B 1 199 ? 96.051  98.182  149.777 1.00 59.77  ?  199  ALA   B C     1 
ATOM   7580  O  O     . ALA   B 1 199 ? 95.342  98.739  148.932 1.00 71.79  ?  199  ALA   B O     1 
ATOM   7581  C  CB    . ALA   B 1 199 ? 96.116  99.077  152.121 1.00 60.00  ?  199  ALA   B CB    1 
ATOM   7582  N  N     . VAL   B 1 200 ? 97.272  97.730  149.487 1.00 54.94  ?  200  VAL   B N     1 
ATOM   7583  C  CA    . VAL   B 1 200 ? 97.839  97.994  148.166 1.00 54.94  ?  200  VAL   B CA    1 
ATOM   7584  C  C     . VAL   B 1 200 ? 97.310  97.009  147.127 1.00 57.31  ?  200  VAL   B C     1 
ATOM   7585  O  O     . VAL   B 1 200 ? 97.007  97.397  145.994 1.00 67.50  ?  200  VAL   B O     1 
ATOM   7586  C  CB    . VAL   B 1 200 ? 99.380  97.991  148.211 1.00 59.72  ?  200  VAL   B CB    1 
ATOM   7587  C  CG1   . VAL   B 1 200 ? 99.900  99.260  148.872 1.00 57.00  ?  200  VAL   B CG1   1 
ATOM   7588  C  CG2   . VAL   B 1 200 ? 99.908  96.745  148.902 1.00 64.80  ?  200  VAL   B CG2   1 
ATOM   7589  N  N     . SER   B 1 201 ? 97.194  95.726  147.482 1.00 55.45  ?  201  SER   B N     1 
ATOM   7590  C  CA    . SER   B 1 201 ? 96.769  94.726  146.506 1.00 57.07  ?  201  SER   B CA    1 
ATOM   7591  C  C     . SER   B 1 201 ? 95.310  94.907  146.106 1.00 64.77  ?  201  SER   B C     1 
ATOM   7592  O  O     . SER   B 1 201 ? 94.937  94.584  144.973 1.00 68.71  ?  201  SER   B O     1 
ATOM   7593  C  CB    . SER   B 1 201 ? 96.997  93.319  147.054 1.00 60.12  ?  201  SER   B CB    1 
ATOM   7594  O  OG    . SER   B 1 201 ? 96.674  93.261  148.430 1.00 70.13  ?  201  SER   B OG    1 
ATOM   7595  N  N     . THR   B 1 202 ? 94.476  95.415  147.010 1.00 61.01  ?  202  THR   B N     1 
ATOM   7596  C  CA    . THR   B 1 202 ? 93.073  95.673  146.719 1.00 59.12  ?  202  THR   B CA    1 
ATOM   7597  C  C     . THR   B 1 202 ? 92.837  97.069  146.154 1.00 59.02  ?  202  THR   B C     1 
ATOM   7598  O  O     . THR   B 1 202 ? 91.680  97.473  146.003 1.00 66.56  ?  202  THR   B O     1 
ATOM   7599  C  CB    . THR   B 1 202 ? 92.223  95.474  147.975 1.00 64.04  ?  202  THR   B CB    1 
ATOM   7600  O  OG1   . THR   B 1 202 ? 92.653  96.382  148.995 1.00 68.35  ?  202  THR   B OG1   1 
ATOM   7601  C  CG2   . THR   B 1 202 ? 92.340  94.049  148.486 1.00 63.23  ?  202  THR   B CG2   1 
ATOM   7602  N  N     . PHE   B 1 203 ? 93.906  97.813  145.865 1.00 55.48  ?  203  PHE   B N     1 
ATOM   7603  C  CA    . PHE   B 1 203 ? 93.838  99.095  145.159 1.00 52.70  ?  203  PHE   B CA    1 
ATOM   7604  C  C     . PHE   B 1 203 ? 93.147  100.177 145.988 1.00 58.96  ?  203  PHE   B C     1 
ATOM   7605  O  O     . PHE   B 1 203 ? 92.385  100.986 145.460 1.00 73.64  ?  203  PHE   B O     1 
ATOM   7606  C  CB    . PHE   B 1 203 ? 93.159  98.950  143.795 1.00 55.00  ?  203  PHE   B CB    1 
ATOM   7607  C  CG    . PHE   B 1 203 ? 93.764  97.887  142.930 1.00 59.97  ?  203  PHE   B CG    1 
ATOM   7608  C  CD1   . PHE   B 1 203 ? 95.131  97.834  142.733 1.00 61.91  ?  203  PHE   B CD1   1 
ATOM   7609  C  CD2   . PHE   B 1 203 ? 92.965  96.941  142.314 1.00 60.64  ?  203  PHE   B CD2   1 
ATOM   7610  C  CE1   . PHE   B 1 203 ? 95.691  96.854  141.939 1.00 62.41  ?  203  PHE   B CE1   1 
ATOM   7611  C  CE2   . PHE   B 1 203 ? 93.519  95.961  141.518 1.00 62.83  ?  203  PHE   B CE2   1 
ATOM   7612  C  CZ    . PHE   B 1 203 ? 94.883  95.918  141.331 1.00 62.82  ?  203  PHE   B CZ    1 
ATOM   7613  N  N     . LYS   B 1 204 ? 93.406  100.191 147.294 1.00 55.01  ?  204  LYS   B N     1 
ATOM   7614  C  CA    A LYS   B 1 204 ? 92.955  101.283 148.150 0.57 57.13  ?  204  LYS   B CA    1 
ATOM   7615  C  CA    B LYS   B 1 204 ? 92.946  101.293 148.127 0.43 57.30  ?  204  LYS   B CA    1 
ATOM   7616  C  C     . LYS   B 1 204 ? 93.995  102.386 148.266 1.00 58.50  ?  204  LYS   B C     1 
ATOM   7617  O  O     . LYS   B 1 204 ? 93.636  103.561 148.398 1.00 63.47  ?  204  LYS   B O     1 
ATOM   7618  C  CB    A LYS   B 1 204 ? 92.614  100.764 149.550 0.57 56.67  ?  204  LYS   B CB    1 
ATOM   7619  C  CB    B LYS   B 1 204 ? 92.536  100.777 149.508 0.43 56.84  ?  204  LYS   B CB    1 
ATOM   7620  C  CG    A LYS   B 1 204 ? 91.174  100.318 149.734 0.57 58.47  ?  204  LYS   B CG    1 
ATOM   7621  C  CG    B LYS   B 1 204 ? 91.378  99.797  149.462 0.43 60.97  ?  204  LYS   B CG    1 
ATOM   7622  C  CD    A LYS   B 1 204 ? 90.924  98.989  149.055 0.57 63.20  ?  204  LYS   B CD    1 
ATOM   7623  C  CD    B LYS   B 1 204 ? 91.157  99.116  150.799 0.43 60.50  ?  204  LYS   B CD    1 
ATOM   7624  C  CE    A LYS   B 1 204 ? 89.572  98.410  149.433 0.57 62.39  ?  204  LYS   B CE    1 
ATOM   7625  C  CE    B LYS   B 1 204 ? 90.129  98.008  150.679 0.43 62.41  ?  204  LYS   B CE    1 
ATOM   7626  N  NZ    A LYS   B 1 204 ? 89.340  97.091  148.782 0.57 59.20  ?  204  LYS   B NZ    1 
ATOM   7627  N  NZ    B LYS   B 1 204 ? 89.976  97.253  151.953 0.43 59.35  ?  204  LYS   B NZ    1 
ATOM   7628  N  N     . ILE   B 1 205 ? 95.277  102.027 148.226 1.00 60.65  ?  205  ILE   B N     1 
ATOM   7629  C  CA    . ILE   B 1 205 ? 96.384  102.975 148.259 1.00 54.62  ?  205  ILE   B CA    1 
ATOM   7630  C  C     . ILE   B 1 205 ? 97.245  102.721 147.032 1.00 60.71  ?  205  ILE   B C     1 
ATOM   7631  O  O     . ILE   B 1 205 ? 97.596  101.573 146.740 1.00 74.89  ?  205  ILE   B O     1 
ATOM   7632  C  CB    . ILE   B 1 205 ? 97.216  102.854 149.552 1.00 56.95  ?  205  ILE   B CB    1 
ATOM   7633  C  CG1   . ILE   B 1 205 ? 96.369  103.231 150.763 1.00 64.12  ?  205  ILE   B CG1   1 
ATOM   7634  C  CG2   . ILE   B 1 205 ? 98.498  103.733 149.505 1.00 51.78  ?  205  ILE   B CG2   1 
ATOM   7635  C  CD1   . ILE   B 1 205 ? 97.106  103.120 152.051 1.00 62.57  ?  205  ILE   B CD1   1 
ATOM   7636  N  N     . SER   B 1 206 ? 97.574  103.787 146.315 1.00 55.15  ?  206  SER   B N     1 
ATOM   7637  C  CA    . SER   B 1 206 ? 98.402  103.709 145.123 1.00 54.51  ?  206  SER   B CA    1 
ATOM   7638  C  C     . SER   B 1 206 ? 99.805  104.190 145.454 1.00 59.34  ?  206  SER   B C     1 
ATOM   7639  O  O     . SER   B 1 206 ? 99.972  105.255 146.055 1.00 69.52  ?  206  SER   B O     1 
ATOM   7640  C  CB    . SER   B 1 206 ? 97.816  104.553 143.994 1.00 59.19  ?  206  SER   B CB    1 
ATOM   7641  O  OG    . SER   B 1 206 ? 98.798  104.829 143.013 1.00 64.88  ?  206  SER   B OG    1 
ATOM   7642  N  N     . LEU   B 1 207 ? 100.805 103.412 145.054 1.00 61.72  ?  207  LEU   B N     1 
ATOM   7643  C  CA    . LEU   B 1 207 ? 102.207 103.711 145.277 1.00 64.14  ?  207  LEU   B CA    1 
ATOM   7644  C  C     . LEU   B 1 207 ? 102.847 104.250 144.003 1.00 60.94  ?  207  LEU   B C     1 
ATOM   7645  O  O     . LEU   B 1 207 ? 102.467 103.857 142.896 1.00 69.03  ?  207  LEU   B O     1 
ATOM   7646  C  CB    . LEU   B 1 207 ? 102.955 102.456 145.740 1.00 61.80  ?  207  LEU   B CB    1 
ATOM   7647  C  CG    . LEU   B 1 207 ? 102.343 101.738 146.943 1.00 63.76  ?  207  LEU   B CG    1 
ATOM   7648  C  CD1   . LEU   B 1 207 ? 103.062 100.430 147.219 1.00 64.45  ?  207  LEU   B CD1   1 
ATOM   7649  C  CD2   . LEU   B 1 207 ? 102.363 102.643 148.168 1.00 55.73  ?  207  LEU   B CD2   1 
ATOM   7650  N  N     . PRO   B 1 208 ? 103.817 105.146 144.117 1.00 50.74  ?  208  PRO   B N     1 
ATOM   7651  C  CA    . PRO   B 1 208 ? 104.430 105.743 142.930 1.00 53.72  ?  208  PRO   B CA    1 
ATOM   7652  C  C     . PRO   B 1 208 ? 105.485 104.810 142.342 1.00 59.26  ?  208  PRO   B C     1 
ATOM   7653  O  O     . PRO   B 1 208 ? 105.799 103.755 142.890 1.00 68.77  ?  208  PRO   B O     1 
ATOM   7654  C  CB    . PRO   B 1 208 ? 105.039 107.038 143.471 1.00 60.21  ?  208  PRO   B CB    1 
ATOM   7655  C  CG    . PRO   B 1 208 ? 105.315 106.760 144.913 1.00 62.94  ?  208  PRO   B CG    1 
ATOM   7656  C  CD    . PRO   B 1 208 ? 104.502 105.566 145.350 1.00 50.33  ?  208  PRO   B CD    1 
ATOM   7657  N  N     . THR   B 1 209 ? 106.026 105.223 141.196 1.00 62.30  ?  209  THR   B N     1 
ATOM   7658  C  CA    . THR   B 1 209 ? 106.964 104.379 140.457 1.00 63.80  ?  209  THR   B CA    1 
ATOM   7659  C  C     . THR   B 1 209 ? 108.208 104.004 141.257 1.00 69.51  ?  209  THR   B C     1 
ATOM   7660  O  O     . THR   B 1 209 ? 108.560 102.810 141.274 1.00 73.97  ?  209  THR   B O     1 
ATOM   7661  C  CB    . THR   B 1 209 ? 107.330 105.068 139.137 1.00 62.30  ?  209  THR   B CB    1 
ATOM   7662  O  OG1   . THR   B 1 209 ? 106.215 105.002 138.239 1.00 71.77  ?  209  THR   B OG1   1 
ATOM   7663  C  CG2   . THR   B 1 209 ? 108.533 104.401 138.491 1.00 66.98  ?  209  THR   B CG2   1 
ATOM   7664  N  N     . PRO   B 1 210 ? 108.919 104.930 141.920 1.00 64.26  ?  210  PRO   B N     1 
ATOM   7665  C  CA    . PRO   B 1 210 ? 110.110 104.503 142.677 1.00 62.99  ?  210  PRO   B CA    1 
ATOM   7666  C  C     . PRO   B 1 210 ? 109.808 103.481 143.758 1.00 58.43  ?  210  PRO   B C     1 
ATOM   7667  O  O     . PRO   B 1 210 ? 110.568 102.520 143.928 1.00 64.26  ?  210  PRO   B O     1 
ATOM   7668  C  CB    . PRO   B 1 210 ? 110.637 105.818 143.269 1.00 58.36  ?  210  PRO   B CB    1 
ATOM   7669  C  CG    . PRO   B 1 210 ? 110.081 106.879 142.395 1.00 56.05  ?  210  PRO   B CG    1 
ATOM   7670  C  CD    . PRO   B 1 210 ? 108.730 106.390 142.000 1.00 54.12  ?  210  PRO   B CD    1 
ATOM   7671  N  N     . ILE   B 1 211 ? 108.702 103.652 144.483 1.00 58.14  ?  211  ILE   B N     1 
ATOM   7672  C  CA    . ILE   B 1 211 ? 108.342 102.692 145.521 1.00 57.93  ?  211  ILE   B CA    1 
ATOM   7673  C  C     . ILE   B 1 211 ? 107.899 101.374 144.900 1.00 56.53  ?  211  ILE   B C     1 
ATOM   7674  O  O     . ILE   B 1 211 ? 108.302 100.294 145.346 1.00 61.33  ?  211  ILE   B O     1 
ATOM   7675  C  CB    . ILE   B 1 211 ? 107.257 103.286 146.438 1.00 51.42  ?  211  ILE   B CB    1 
ATOM   7676  C  CG1   . ILE   B 1 211 ? 107.821 104.471 147.223 1.00 52.15  ?  211  ILE   B CG1   1 
ATOM   7677  C  CG2   . ILE   B 1 211 ? 106.709 102.228 147.379 1.00 50.13  ?  211  ILE   B CG2   1 
ATOM   7678  C  CD1   . ILE   B 1 211 ? 106.822 105.129 148.135 1.00 59.28  ?  211  ILE   B CD1   1 
ATOM   7679  N  N     . MET   B 1 212 ? 107.071 101.439 143.856 1.00 68.21  ?  212  MET   B N     1 
ATOM   7680  C  CA    . MET   B 1 212 ? 106.571 100.224 143.226 1.00 65.95  ?  212  MET   B CA    1 
ATOM   7681  C  C     . MET   B 1 212 ? 107.671 99.435  142.528 1.00 63.92  ?  212  MET   B C     1 
ATOM   7682  O  O     . MET   B 1 212 ? 107.481 98.245  142.258 1.00 72.89  ?  212  MET   B O     1 
ATOM   7683  C  CB    . MET   B 1 212 ? 105.459 100.565 142.227 1.00 61.63  ?  212  MET   B CB    1 
ATOM   7684  C  CG    . MET   B 1 212 ? 104.072 100.770 142.850 1.00 64.56  ?  212  MET   B CG    1 
ATOM   7685  S  SD    . MET   B 1 212 ? 103.255 99.201  143.174 1.00 83.76  ?  212  MET   B SD    1 
ATOM   7686  C  CE    . MET   B 1 212 ? 102.924 98.638  141.509 1.00 68.26  ?  212  MET   B CE    1 
ATOM   7687  N  N     . SER   B 1 213 ? 108.811 100.060 142.231 1.00 48.68  ?  213  SER   B N     1 
ATOM   7688  C  CA    . SER   B 1 213 ? 109.858 99.399  141.468 1.00 52.83  ?  213  SER   B CA    1 
ATOM   7689  C  C     . SER   B 1 213 ? 111.187 99.258  142.200 1.00 62.76  ?  213  SER   B C     1 
ATOM   7690  O  O     . SER   B 1 213 ? 112.120 98.681  141.630 1.00 71.67  ?  213  SER   B O     1 
ATOM   7691  C  CB    . SER   B 1 213 ? 110.093 100.143 140.146 1.00 56.72  ?  213  SER   B CB    1 
ATOM   7692  O  OG    . SER   B 1 213 ? 110.934 101.267 140.333 1.00 52.83  ?  213  SER   B OG    1 
ATOM   7693  N  N     . GLY   B 1 214 ? 111.317 99.752  143.431 1.00 64.35  ?  214  GLY   B N     1 
ATOM   7694  C  CA    . GLY   B 1 214 ? 112.625 99.689  144.055 1.00 62.62  ?  214  GLY   B CA    1 
ATOM   7695  C  C     . GLY   B 1 214 ? 112.731 99.373  145.535 1.00 66.14  ?  214  GLY   B C     1 
ATOM   7696  O  O     . GLY   B 1 214 ? 113.849 99.334  146.059 1.00 71.43  ?  214  GLY   B O     1 
ATOM   7697  N  N     . VAL   B 1 215 ? 111.598 99.131  146.221 1.00 61.74  ?  215  VAL   B N     1 
ATOM   7698  C  CA    . VAL   B 1 215 ? 111.615 98.984  147.688 1.00 68.09  ?  215  VAL   B CA    1 
ATOM   7699  C  C     . VAL   B 1 215 ? 112.284 97.682  148.127 1.00 75.85  ?  215  VAL   B C     1 
ATOM   7700  O  O     . VAL   B 1 215 ? 113.053 97.686  149.092 1.00 80.44  ?  215  VAL   B O     1 
ATOM   7701  C  CB    . VAL   B 1 215 ? 110.208 99.176  148.317 1.00 59.75  ?  215  VAL   B CB    1 
ATOM   7702  C  CG1   . VAL   B 1 215 ? 110.076 98.519  149.683 1.00 60.44  ?  215  VAL   B CG1   1 
ATOM   7703  C  CG2   . VAL   B 1 215 ? 109.892 100.660 148.440 1.00 60.60  ?  215  VAL   B CG2   1 
ATOM   7704  N  N     . ARG   B 1 216 ? 112.059 96.573  147.415 1.00 66.53  ?  216  ARG   B N     1 
ATOM   7705  C  CA    . ARG   B 1 216 ? 112.734 95.316  147.714 1.00 61.50  ?  216  ARG   B CA    1 
ATOM   7706  C  C     . ARG   B 1 216 ? 114.134 95.238  147.115 1.00 64.97  ?  216  ARG   B C     1 
ATOM   7707  O  O     . ARG   B 1 216 ? 114.916 94.380  147.516 1.00 73.22  ?  216  ARG   B O     1 
ATOM   7708  C  CB    . ARG   B 1 216 ? 111.884 94.140  147.229 1.00 62.10  ?  216  ARG   B CB    1 
ATOM   7709  C  CG    . ARG   B 1 216 ? 111.548 94.194  145.755 1.00 62.29  ?  216  ARG   B CG    1 
ATOM   7710  C  CD    . ARG   B 1 216 ? 110.066 93.988  145.510 1.00 62.45  ?  216  ARG   B CD    1 
ATOM   7711  N  NE    . ARG   B 1 216 ? 109.718 94.249  144.120 1.00 63.99  ?  216  ARG   B NE    1 
ATOM   7712  C  CZ    . ARG   B 1 216 ? 109.624 95.458  143.585 1.00 61.80  ?  216  ARG   B CZ    1 
ATOM   7713  N  NH1   . ARG   B 1 216 ? 109.818 96.550  144.305 1.00 64.38  ?  216  ARG   B NH1   1 
ATOM   7714  N  NH2   . ARG   B 1 216 ? 109.331 95.575  142.295 1.00 63.24  ?  216  ARG   B NH2   1 
ATOM   7715  N  N     . THR   B 1 217 ? 114.517 96.178  146.366 1.00 62.79  ?  217  THR   B N     1 
ATOM   7716  C  CA    . THR   B 1 217 ? 115.692 96.105  145.547 1.00 56.73  ?  217  THR   B CA    1 
ATOM   7717  C  C     . THR   B 1 217 ? 116.835 96.548  146.410 1.00 62.65  ?  217  THR   B C     1 
ATOM   7718  O  O     . THR   B 1 217 ? 116.582 97.094  147.454 1.00 74.48  ?  217  THR   B O     1 
ATOM   7719  C  CB    . THR   B 1 217 ? 115.402 96.963  144.340 1.00 64.08  ?  217  THR   B CB    1 
ATOM   7720  O  OG1   . THR   B 1 217 ? 114.630 96.120  143.484 1.00 70.14  ?  217  THR   B OG1   1 
ATOM   7721  C  CG2   . THR   B 1 217 ? 116.606 97.524  143.644 1.00 64.85  ?  217  THR   B CG2   1 
ATOM   7722  N  N     . PRO   B 1 218 ? 118.094 96.254  146.099 1.00 64.87  ?  218  PRO   B N     1 
ATOM   7723  C  CA    . PRO   B 1 218 ? 119.171 96.738  146.969 1.00 64.42  ?  218  PRO   B CA    1 
ATOM   7724  C  C     . PRO   B 1 218 ? 119.546 98.198  146.752 1.00 64.07  ?  218  PRO   B C     1 
ATOM   7725  O  O     . PRO   B 1 218 ? 120.360 98.723  147.523 1.00 70.26  ?  218  PRO   B O     1 
ATOM   7726  C  CB    . PRO   B 1 218 ? 120.344 95.809  146.620 1.00 63.63  ?  218  PRO   B CB    1 
ATOM   7727  C  CG    . PRO   B 1 218 ? 119.796 94.783  145.663 1.00 64.07  ?  218  PRO   B CG    1 
ATOM   7728  C  CD    . PRO   B 1 218 ? 118.610 95.397  145.030 1.00 62.63  ?  218  PRO   B CD    1 
ATOM   7729  N  N     . THR   B 1 219 ? 118.996 98.867  145.739 1.00 73.59  ?  219  THR   B N     1 
ATOM   7730  C  CA    . THR   B 1 219 ? 119.193 100.305 145.555 1.00 70.32  ?  219  THR   B CA    1 
ATOM   7731  C  C     . THR   B 1 219 ? 118.115 101.042 146.357 1.00 72.72  ?  219  THR   B C     1 
ATOM   7732  O  O     . THR   B 1 219 ? 116.938 100.972 146.022 1.00 80.28  ?  219  THR   B O     1 
ATOM   7733  C  CB    . THR   B 1 219 ? 119.129 100.688 144.079 1.00 72.94  ?  219  THR   B CB    1 
ATOM   7734  O  OG1   . THR   B 1 219 ? 120.121 99.957  143.350 1.00 79.61  ?  219  THR   B OG1   1 
ATOM   7735  C  CG2   . THR   B 1 219 ? 119.408 102.174 143.935 1.00 70.57  ?  219  THR   B CG2   1 
ATOM   7736  N  N     . ARG   B 1 220 ? 118.500 101.772 147.402 1.00 69.64  ?  220  ARG   B N     1 
ATOM   7737  C  CA    A ARG   B 1 220 ? 117.582 102.271 148.437 0.45 69.21  ?  220  ARG   B CA    1 
ATOM   7738  C  CA    B ARG   B 1 220 ? 117.483 102.241 148.376 0.55 68.87  ?  220  ARG   B CA    1 
ATOM   7739  C  C     . ARG   B 1 220 ? 117.235 103.761 148.304 1.00 71.70  ?  220  ARG   B C     1 
ATOM   7740  O  O     . ARG   B 1 220 ? 117.571 104.614 149.139 1.00 80.62  ?  220  ARG   B O     1 
ATOM   7741  C  CB    A ARG   B 1 220 ? 118.144 101.965 149.822 0.45 68.94  ?  220  ARG   B CB    1 
ATOM   7742  C  CB    B ARG   B 1 220 ? 117.893 101.710 149.735 0.55 67.86  ?  220  ARG   B CB    1 
ATOM   7743  C  CG    A ARG   B 1 220 ? 118.407 100.498 150.066 0.45 70.43  ?  220  ARG   B CG    1 
ATOM   7744  C  CG    B ARG   B 1 220 ? 117.460 100.267 149.987 0.55 69.28  ?  220  ARG   B CG    1 
ATOM   7745  C  CD    A ARG   B 1 220 ? 117.594 99.992  151.232 0.45 70.57  ?  220  ARG   B CD    1 
ATOM   7746  C  CD    B ARG   B 1 220 ? 118.014 99.775  151.301 0.55 71.07  ?  220  ARG   B CD    1 
ATOM   7747  N  NE    A ARG   B 1 220 ? 118.232 98.870  151.908 0.45 70.33  ?  220  ARG   B NE    1 
ATOM   7748  N  NE    B ARG   B 1 220 ? 119.387 100.239 151.443 0.55 74.11  ?  220  ARG   B NE    1 
ATOM   7749  C  CZ    A ARG   B 1 220 ? 118.622 98.885  153.175 0.45 70.57  ?  220  ARG   B CZ    1 
ATOM   7750  C  CZ    B ARG   B 1 220 ? 120.444 99.535  151.075 0.55 71.87  ?  220  ARG   B CZ    1 
ATOM   7751  N  NH1   A ARG   B 1 220 ? 118.469 99.959  153.932 0.45 70.58  ?  220  ARG   B NH1   1 
ATOM   7752  N  NH1   B ARG   B 1 220 ? 120.316 98.325  150.564 0.55 70.62  ?  220  ARG   B NH1   1 
ATOM   7753  N  NH2   A ARG   B 1 220 ? 119.209 97.808  153.686 0.45 71.81  ?  220  ARG   B NH2   1 
ATOM   7754  N  NH2   B ARG   B 1 220 ? 121.659 100.051 151.237 0.55 68.59  ?  220  ARG   B NH2   1 
ATOM   7755  N  N     . GLN   B 1 221 ? 116.555 104.130 147.267 1.00 61.78  ?  221  GLN   B N     1 
ATOM   7756  C  CA    . GLN   B 1 221 ? 116.183 105.523 147.110 1.00 60.12  ?  221  GLN   B CA    1 
ATOM   7757  C  C     . GLN   B 1 221 ? 114.805 105.530 146.480 1.00 63.09  ?  221  GLN   B C     1 
ATOM   7758  O  O     . GLN   B 1 221 ? 114.626 104.999 145.380 1.00 66.74  ?  221  GLN   B O     1 
ATOM   7759  C  CB    . GLN   B 1 221 ? 117.206 106.279 146.258 1.00 56.00  ?  221  GLN   B CB    1 
ATOM   7760  C  CG    . GLN   B 1 221 ? 116.625 107.312 145.313 1.00 56.62  ?  221  GLN   B CG    1 
ATOM   7761  C  CD    . GLN   B 1 221 ? 115.969 108.480 146.018 1.00 60.58  ?  221  GLN   B CD    1 
ATOM   7762  O  OE1   . GLN   B 1 221 ? 116.259 108.767 147.178 1.00 71.00  ?  221  GLN   B OE1   1 
ATOM   7763  N  NE2   . GLN   B 1 221 ? 115.084 109.170 145.310 1.00 63.89  ?  221  GLN   B NE2   1 
ATOM   7764  N  N     . PHE   B 1 222 ? 113.829 106.098 147.190 1.00 61.01  ?  222  PHE   B N     1 
ATOM   7765  C  CA    . PHE   B 1 222 ? 112.437 106.048 146.770 1.00 54.73  ?  222  PHE   B CA    1 
ATOM   7766  C  C     . PHE   B 1 222 ? 111.764 107.413 146.811 1.00 61.75  ?  222  PHE   B C     1 
ATOM   7767  O  O     . PHE   B 1 222 ? 110.538 107.489 146.680 1.00 70.69  ?  222  PHE   B O     1 
ATOM   7768  C  CB    . PHE   B 1 222 ? 111.659 105.052 147.635 1.00 58.71  ?  222  PHE   B CB    1 
ATOM   7769  C  CG    . PHE   B 1 222 ? 112.495 103.913 148.136 1.00 64.93  ?  222  PHE   B CG    1 
ATOM   7770  C  CD1   . PHE   B 1 222 ? 112.906 102.909 147.278 1.00 64.47  ?  222  PHE   B CD1   1 
ATOM   7771  C  CD2   . PHE   B 1 222 ? 112.887 103.854 149.461 1.00 62.09  ?  222  PHE   B CD2   1 
ATOM   7772  C  CE1   . PHE   B 1 222 ? 113.683 101.866 147.735 1.00 59.99  ?  222  PHE   B CE1   1 
ATOM   7773  C  CE2   . PHE   B 1 222 ? 113.661 102.811 149.922 1.00 62.65  ?  222  PHE   B CE2   1 
ATOM   7774  C  CZ    . PHE   B 1 222 ? 114.058 101.816 149.058 1.00 59.50  ?  222  PHE   B CZ    1 
ATOM   7775  N  N     . SER   B 1 223 ? 112.525 108.488 146.996 1.00 68.78  ?  223  SER   B N     1 
ATOM   7776  C  CA    . SER   B 1 223 ? 111.958 109.827 146.924 1.00 59.98  ?  223  SER   B CA    1 
ATOM   7777  C  C     . SER   B 1 223 ? 111.591 110.137 145.480 1.00 60.56  ?  223  SER   B C     1 
ATOM   7778  O  O     . SER   B 1 223 ? 112.463 110.192 144.607 1.00 62.91  ?  223  SER   B O     1 
ATOM   7779  C  CB    . SER   B 1 223 ? 112.946 110.855 147.465 1.00 61.77  ?  223  SER   B CB    1 
ATOM   7780  O  OG    . SER   B 1 223 ? 112.847 110.957 148.874 1.00 70.74  ?  223  SER   B OG    1 
ATOM   7781  N  N     . SER   B 1 224 ? 110.296 110.331 145.228 1.00 64.52  ?  224  SER   B N     1 
ATOM   7782  C  CA    . SER   B 1 224 ? 109.837 110.557 143.862 1.00 59.21  ?  224  SER   B CA    1 
ATOM   7783  C  C     . SER   B 1 224 ? 110.220 111.936 143.352 1.00 59.41  ?  224  SER   B C     1 
ATOM   7784  O  O     . SER   B 1 224 ? 110.483 112.098 142.156 1.00 62.68  ?  224  SER   B O     1 
ATOM   7785  C  CB    . SER   B 1 224 ? 108.325 110.378 143.767 1.00 62.82  ?  224  SER   B CB    1 
ATOM   7786  O  OG    . SER   B 1 224 ? 107.867 110.639 142.460 1.00 72.34  ?  224  SER   B OG    1 
ATOM   7787  N  N     . CYS   B 1 225 ? 110.266 112.934 144.227 1.00 68.67  ?  225  CYS   B N     1 
ATOM   7788  C  CA    . CYS   B 1 225 ? 110.451 114.318 143.816 1.00 63.51  ?  225  CYS   B CA    1 
ATOM   7789  C  C     . CYS   B 1 225 ? 111.691 114.912 144.480 1.00 66.06  ?  225  CYS   B C     1 
ATOM   7790  O  O     . CYS   B 1 225 ? 111.843 114.824 145.701 1.00 71.74  ?  225  CYS   B O     1 
ATOM   7791  C  CB    . CYS   B 1 225 ? 109.198 115.119 144.165 1.00 67.11  ?  225  CYS   B CB    1 
ATOM   7792  S  SG    . CYS   B 1 225 ? 107.740 114.769 143.112 1.00 86.86  ?  225  CYS   B SG    1 
ATOM   7793  N  N     . VAL   B 1 226 ? 112.572 115.518 143.686 1.00 55.34  ?  226  VAL   B N     1 
ATOM   7794  C  CA    . VAL   B 1 226 ? 113.786 116.155 144.190 1.00 50.12  ?  226  VAL   B CA    1 
ATOM   7795  C  C     . VAL   B 1 226 ? 113.784 117.613 143.763 1.00 56.52  ?  226  VAL   B C     1 
ATOM   7796  O  O     . VAL   B 1 226 ? 113.635 117.915 142.574 1.00 67.24  ?  226  VAL   B O     1 
ATOM   7797  C  CB    . VAL   B 1 226 ? 115.058 115.448 143.689 1.00 53.81  ?  226  VAL   B CB    1 
ATOM   7798  C  CG1   . VAL   B 1 226 ? 116.286 115.977 144.391 1.00 49.61  ?  226  VAL   B CG1   1 
ATOM   7799  C  CG2   . VAL   B 1 226 ? 114.961 113.969 143.965 1.00 63.85  ?  226  VAL   B CG2   1 
ATOM   7800  N  N     . LEU   B 1 227 ? 113.969 118.509 144.728 1.00 50.07  ?  227  LEU   B N     1 
ATOM   7801  C  CA    . LEU   B 1 227 ? 113.998 119.946 144.498 1.00 42.93  ?  227  LEU   B CA    1 
ATOM   7802  C  C     . LEU   B 1 227 ? 115.388 120.459 144.844 1.00 54.00  ?  227  LEU   B C     1 
ATOM   7803  O  O     . LEU   B 1 227 ? 115.821 120.357 145.999 1.00 65.39  ?  227  LEU   B O     1 
ATOM   7804  C  CB    . LEU   B 1 227 ? 112.938 120.660 145.338 1.00 49.19  ?  227  LEU   B CB    1 
ATOM   7805  C  CG    . LEU   B 1 227 ? 111.506 120.728 144.805 1.00 52.76  ?  227  LEU   B CG    1 
ATOM   7806  C  CD1   . LEU   B 1 227 ? 110.861 119.355 144.783 1.00 52.89  ?  227  LEU   B CD1   1 
ATOM   7807  C  CD2   . LEU   B 1 227 ? 110.681 121.688 145.648 1.00 54.22  ?  227  LEU   B CD2   1 
ATOM   7808  N  N     . ILE   B 1 228 ? 116.079 121.006 143.847 1.00 46.68  ?  228  ILE   B N     1 
ATOM   7809  C  CA    . ILE   B 1 228 ? 117.435 121.519 143.994 1.00 43.20  ?  228  ILE   B CA    1 
ATOM   7810  C  C     . ILE   B 1 228 ? 117.433 122.991 143.614 1.00 55.28  ?  228  ILE   B C     1 
ATOM   7811  O  O     . ILE   B 1 228 ? 116.903 123.364 142.562 1.00 63.53  ?  228  ILE   B O     1 
ATOM   7812  C  CB    . ILE   B 1 228 ? 118.438 120.738 143.124 1.00 48.39  ?  228  ILE   B CB    1 
ATOM   7813  C  CG1   . ILE   B 1 228 ? 118.343 119.238 143.407 1.00 60.63  ?  228  ILE   B CG1   1 
ATOM   7814  C  CG2   . ILE   B 1 228 ? 119.852 121.233 143.365 1.00 53.19  ?  228  ILE   B CG2   1 
ATOM   7815  C  CD1   . ILE   B 1 228 ? 118.717 118.372 142.225 1.00 56.32  ?  228  ILE   B CD1   1 
ATOM   7816  N  N     . GLU   B 1 229 ? 118.025 123.821 144.465 1.00 76.29  ?  229  GLU   B N     1 
ATOM   7817  C  CA    . GLU   B 1 229 ? 118.155 125.249 144.210 1.00 73.26  ?  229  GLU   B CA    1 
ATOM   7818  C  C     . GLU   B 1 229 ? 119.570 125.552 143.738 1.00 76.73  ?  229  GLU   B C     1 
ATOM   7819  O  O     . GLU   B 1 229 ? 120.544 125.170 144.395 1.00 84.48  ?  229  GLU   B O     1 
ATOM   7820  C  CB    . GLU   B 1 229 ? 117.831 126.059 145.466 1.00 72.86  ?  229  GLU   B CB    1 
ATOM   7821  C  CG    . GLU   B 1 229 ? 118.051 127.556 145.315 1.00 76.23  ?  229  GLU   B CG    1 
ATOM   7822  C  CD    . GLU   B 1 229 ? 117.050 128.374 146.106 1.00 86.87  ?  229  GLU   B CD    1 
ATOM   7823  O  OE1   . GLU   B 1 229 ? 116.390 127.807 147.001 1.00 89.66  ?  229  GLU   B OE1   1 
ATOM   7824  O  OE2   . GLU   B 1 229 ? 116.880 129.568 145.793 1.00 86.75  ?  229  GLU   B OE2   1 
ATOM   7825  N  N     . CYS   B 1 230 ? 119.679 126.231 142.600 1.00 75.13  ?  230  CYS   B N     1 
ATOM   7826  C  CA    . CYS   B 1 230 ? 120.964 126.606 142.028 1.00 70.88  ?  230  CYS   B CA    1 
ATOM   7827  C  C     . CYS   B 1 230 ? 121.295 128.040 142.415 1.00 77.84  ?  230  CYS   B C     1 
ATOM   7828  O  O     . CYS   B 1 230 ? 120.449 128.932 142.293 1.00 84.54  ?  230  CYS   B O     1 
ATOM   7829  C  CB    . CYS   B 1 230 ? 120.954 126.465 140.505 1.00 69.22  ?  230  CYS   B CB    1 
ATOM   7830  S  SG    . CYS   B 1 230 ? 122.582 126.186 139.788 1.00 90.59  ?  230  CYS   B SG    1 
ATOM   7831  N  N     . GLY   B 1 231 ? 122.523 128.255 142.881 1.00 66.58  ?  231  GLY   B N     1 
ATOM   7832  C  CA    . GLY   B 1 231 ? 122.993 129.577 143.221 1.00 63.95  ?  231  GLY   B CA    1 
ATOM   7833  C  C     . GLY   B 1 231 ? 123.788 130.210 142.095 1.00 70.04  ?  231  GLY   B C     1 
ATOM   7834  O  O     . GLY   B 1 231 ? 124.296 129.533 141.205 1.00 77.99  ?  231  GLY   B O     1 
ATOM   7835  N  N     . ASP   B 1 232 ? 123.907 131.536 142.158 1.00 72.92  ?  232  ASP   B N     1 
ATOM   7836  C  CA    . ASP   B 1 232 ? 124.642 132.301 141.151 1.00 69.85  ?  232  ASP   B CA    1 
ATOM   7837  C  C     . ASP   B 1 232 ? 126.143 132.123 141.384 1.00 70.88  ?  232  ASP   B C     1 
ATOM   7838  O  O     . ASP   B 1 232 ? 126.868 133.037 141.782 1.00 78.06  ?  232  ASP   B O     1 
ATOM   7839  C  CB    . ASP   B 1 232 ? 124.229 133.765 141.197 1.00 70.89  ?  232  ASP   B CB    1 
ATOM   7840  C  CG    . ASP   B 1 232 ? 124.718 134.546 139.997 1.00 80.14  ?  232  ASP   B CG    1 
ATOM   7841  O  OD1   . ASP   B 1 232 ? 124.567 134.058 138.858 1.00 83.78  ?  232  ASP   B OD1   1 
ATOM   7842  O  OD2   . ASP   B 1 232 ? 125.263 135.649 140.196 1.00 83.91  ?  232  ASP   B OD2   1 
ATOM   7843  N  N     . SER   B 1 233 ? 126.607 130.904 141.121 1.00 66.44  ?  233  SER   B N     1 
ATOM   7844  C  CA    . SER   B 1 233 ? 127.995 130.543 141.363 1.00 61.36  ?  233  SER   B CA    1 
ATOM   7845  C  C     . SER   B 1 233 ? 128.351 129.338 140.507 1.00 67.90  ?  233  SER   B C     1 
ATOM   7846  O  O     . SER   B 1 233 ? 127.511 128.471 140.252 1.00 73.51  ?  233  SER   B O     1 
ATOM   7847  C  CB    . SER   B 1 233 ? 128.239 130.235 142.844 1.00 66.49  ?  233  SER   B CB    1 
ATOM   7848  O  OG    . SER   B 1 233 ? 129.612 130.001 143.098 1.00 75.19  ?  233  SER   B OG    1 
ATOM   7849  N  N     . LEU   B 1 234 ? 129.610 129.299 140.063 1.00 64.24  ?  234  LEU   B N     1 
ATOM   7850  C  CA    . LEU   B 1 234 ? 130.092 128.151 139.303 1.00 55.55  ?  234  LEU   B CA    1 
ATOM   7851  C  C     . LEU   B 1 234 ? 130.070 126.884 140.147 1.00 60.34  ?  234  LEU   B C     1 
ATOM   7852  O  O     . LEU   B 1 234 ? 129.680 125.813 139.665 1.00 70.32  ?  234  LEU   B O     1 
ATOM   7853  C  CB    . LEU   B 1 234 ? 131.503 128.420 138.787 1.00 61.04  ?  234  LEU   B CB    1 
ATOM   7854  C  CG    . LEU   B 1 234 ? 131.631 128.945 137.360 1.00 61.43  ?  234  LEU   B CG    1 
ATOM   7855  C  CD1   . LEU   B 1 234 ? 133.066 128.824 136.910 1.00 62.14  ?  234  LEU   B CD1   1 
ATOM   7856  C  CD2   . LEU   B 1 234 ? 130.709 128.202 136.418 1.00 59.65  ?  234  LEU   B CD2   1 
ATOM   7857  N  N     . ASP   B 1 235 ? 130.496 126.986 141.409 1.00 72.19  ?  235  ASP   B N     1 
ATOM   7858  C  CA    . ASP   B 1 235 ? 130.440 125.837 142.307 1.00 75.33  ?  235  ASP   B CA    1 
ATOM   7859  C  C     . ASP   B 1 235 ? 129.005 125.372 142.504 1.00 76.90  ?  235  ASP   B C     1 
ATOM   7860  O  O     . ASP   B 1 235 ? 128.734 124.167 142.542 1.00 80.21  ?  235  ASP   B O     1 
ATOM   7861  C  CB    . ASP   B 1 235 ? 131.079 126.179 143.656 1.00 76.21  ?  235  ASP   B CB    1 
ATOM   7862  C  CG    . ASP   B 1 235 ? 132.571 126.439 143.551 1.00 87.60  ?  235  ASP   B CG    1 
ATOM   7863  O  OD1   . ASP   B 1 235 ? 133.147 126.148 142.482 1.00 87.02  ?  235  ASP   B OD1   1 
ATOM   7864  O  OD2   . ASP   B 1 235 ? 133.145 126.993 144.513 1.00 88.93  ?  235  ASP   B OD2   1 
ATOM   7865  N  N     . SER   B 1 236 ? 128.071 126.317 142.635 1.00 64.46  ?  236  SER   B N     1 
ATOM   7866  C  CA    . SER   B 1 236 ? 126.666 125.955 142.783 1.00 59.97  ?  236  SER   B CA    1 
ATOM   7867  C  C     . SER   B 1 236 ? 126.141 125.246 141.542 1.00 65.61  ?  236  SER   B C     1 
ATOM   7868  O  O     . SER   B 1 236 ? 125.394 124.268 141.648 1.00 67.03  ?  236  SER   B O     1 
ATOM   7869  C  CB    . SER   B 1 236 ? 125.829 127.197 143.081 1.00 60.09  ?  236  SER   B CB    1 
ATOM   7870  O  OG    . SER   B 1 236 ? 124.726 126.870 143.906 1.00 69.70  ?  236  SER   B OG    1 
ATOM   7871  N  N     . ILE   B 1 237 ? 126.519 125.725 140.355 1.00 58.40  ?  237  ILE   B N     1 
ATOM   7872  C  CA    . ILE   B 1 237 ? 126.075 125.085 139.120 1.00 52.78  ?  237  ILE   B CA    1 
ATOM   7873  C  C     . ILE   B 1 237 ? 126.641 123.674 139.016 1.00 59.31  ?  237  ILE   B C     1 
ATOM   7874  O  O     . ILE   B 1 237 ? 125.935 122.731 138.635 1.00 61.93  ?  237  ILE   B O     1 
ATOM   7875  C  CB    . ILE   B 1 237 ? 126.459 125.947 137.903 1.00 52.68  ?  237  ILE   B CB    1 
ATOM   7876  C  CG1   . ILE   B 1 237 ? 125.629 127.233 137.880 1.00 53.34  ?  237  ILE   B CG1   1 
ATOM   7877  C  CG2   . ILE   B 1 237 ? 126.264 125.172 136.610 1.00 56.42  ?  237  ILE   B CG2   1 
ATOM   7878  C  CD1   . ILE   B 1 237 ? 126.233 128.335 137.041 1.00 60.26  ?  237  ILE   B CD1   1 
ATOM   7879  N  N     . ASN   B 1 238 ? 127.922 123.504 139.356 1.00 59.60  ?  238  ASN   B N     1 
ATOM   7880  C  CA    . ASN   B 1 238 ? 128.525 122.174 139.322 1.00 53.78  ?  238  ASN   B CA    1 
ATOM   7881  C  C     . ASN   B 1 238 ? 127.852 121.235 140.315 1.00 52.44  ?  238  ASN   B C     1 
ATOM   7882  O  O     . ASN   B 1 238 ? 127.587 120.069 139.998 1.00 65.30  ?  238  ASN   B O     1 
ATOM   7883  C  CB    . ASN   B 1 238 ? 130.023 122.269 139.610 1.00 58.69  ?  238  ASN   B CB    1 
ATOM   7884  C  CG    . ASN   B 1 238 ? 130.825 122.655 138.389 1.00 62.26  ?  238  ASN   B CG    1 
ATOM   7885  O  OD1   . ASN   B 1 238 ? 130.517 122.235 137.275 1.00 66.07  ?  238  ASN   B OD1   1 
ATOM   7886  N  ND2   . ASN   B 1 238 ? 131.854 123.468 138.590 1.00 66.00  ?  238  ASN   B ND2   1 
ATOM   7887  N  N     . ALA   B 1 239 ? 127.568 121.726 141.523 1.00 47.59  ?  239  ALA   B N     1 
ATOM   7888  C  CA    . ALA   B 1 239 ? 126.901 120.897 142.520 1.00 54.53  ?  239  ALA   B CA    1 
ATOM   7889  C  C     . ALA   B 1 239 ? 125.495 120.522 142.076 1.00 57.46  ?  239  ALA   B C     1 
ATOM   7890  O  O     . ALA   B 1 239 ? 125.061 119.382 142.275 1.00 60.17  ?  239  ALA   B O     1 
ATOM   7891  C  CB    . ALA   B 1 239 ? 126.872 121.619 143.864 1.00 54.81  ?  239  ALA   B CB    1 
ATOM   7892  N  N     . THR   B 1 240 ? 124.772 121.464 141.463 1.00 57.96  ?  240  THR   B N     1 
ATOM   7893  C  CA    . THR   B 1 240 ? 123.442 121.169 140.947 1.00 52.99  ?  240  THR   B CA    1 
ATOM   7894  C  C     . THR   B 1 240 ? 123.499 120.116 139.850 1.00 52.16  ?  240  THR   B C     1 
ATOM   7895  O  O     . THR   B 1 240 ? 122.675 119.197 139.822 1.00 59.86  ?  240  THR   B O     1 
ATOM   7896  C  CB    . THR   B 1 240 ? 122.786 122.447 140.428 1.00 53.23  ?  240  THR   B CB    1 
ATOM   7897  O  OG1   . THR   B 1 240 ? 122.916 123.483 141.409 1.00 65.86  ?  240  THR   B OG1   1 
ATOM   7898  C  CG2   . THR   B 1 240 ? 121.313 122.209 140.143 1.00 47.68  ?  240  THR   B CG2   1 
ATOM   7899  N  N     . SER   B 1 241 ? 124.467 120.232 138.937 1.00 52.13  ?  241  SER   B N     1 
ATOM   7900  C  CA    . SER   B 1 241 ? 124.604 119.239 137.876 1.00 49.18  ?  241  SER   B CA    1 
ATOM   7901  C  C     . SER   B 1 241 ? 124.928 117.864 138.445 1.00 55.83  ?  241  SER   B C     1 
ATOM   7902  O  O     . SER   B 1 241 ? 124.363 116.851 138.011 1.00 63.14  ?  241  SER   B O     1 
ATOM   7903  C  CB    . SER   B 1 241 ? 125.683 119.675 136.885 1.00 53.98  ?  241  SER   B CB    1 
ATOM   7904  O  OG    . SER   B 1 241 ? 125.867 118.705 135.870 1.00 70.44  ?  241  SER   B OG    1 
ATOM   7905  N  N     . SER   B 1 242 ? 125.837 117.809 139.420 1.00 61.27  ?  242  SER   B N     1 
ATOM   7906  C  CA    . SER   B 1 242 ? 126.187 116.533 140.032 1.00 52.88  ?  242  SER   B CA    1 
ATOM   7907  C  C     . SER   B 1 242 ? 124.994 115.917 140.749 1.00 55.18  ?  242  SER   B C     1 
ATOM   7908  O  O     . SER   B 1 242 ? 124.756 114.708 140.646 1.00 67.84  ?  242  SER   B O     1 
ATOM   7909  C  CB    . SER   B 1 242 ? 127.351 116.724 141.001 1.00 55.07  ?  242  SER   B CB    1 
ATOM   7910  O  OG    . SER   B 1 242 ? 128.558 117.021 140.325 1.00 65.70  ?  242  SER   B OG    1 
ATOM   7911  N  N     . ALA   B 1 243 ? 124.230 116.732 141.481 1.00 49.31  ?  243  ALA   B N     1 
ATOM   7912  C  CA    . ALA   B 1 243 ? 123.047 116.224 142.168 1.00 49.27  ?  243  ALA   B CA    1 
ATOM   7913  C  C     . ALA   B 1 243 ? 122.000 115.740 141.176 1.00 53.49  ?  243  ALA   B C     1 
ATOM   7914  O  O     . ALA   B 1 243 ? 121.348 114.715 141.403 1.00 56.31  ?  243  ALA   B O     1 
ATOM   7915  C  CB    . ALA   B 1 243 ? 122.466 117.302 143.081 1.00 47.14  ?  243  ALA   B CB    1 
ATOM   7916  N  N     . ILE   B 1 244 ? 121.826 116.462 140.067 1.00 50.98  ?  244  ILE   B N     1 
ATOM   7917  C  CA    . ILE   B 1 244 ? 120.873 116.039 139.045 1.00 45.37  ?  244  ILE   B CA    1 
ATOM   7918  C  C     . ILE   B 1 244 ? 121.274 114.684 138.479 1.00 54.65  ?  244  ILE   B C     1 
ATOM   7919  O  O     . ILE   B 1 244 ? 120.453 113.766 138.379 1.00 65.27  ?  244  ILE   B O     1 
ATOM   7920  C  CB    . ILE   B 1 244 ? 120.769 117.099 137.933 1.00 49.04  ?  244  ILE   B CB    1 
ATOM   7921  C  CG1   . ILE   B 1 244 ? 119.919 118.284 138.387 1.00 53.78  ?  244  ILE   B CG1   1 
ATOM   7922  C  CG2   . ILE   B 1 244 ? 120.182 116.488 136.676 1.00 45.77  ?  244  ILE   B CG2   1 
ATOM   7923  C  CD1   . ILE   B 1 244 ? 120.250 119.570 137.664 1.00 54.70  ?  244  ILE   B CD1   1 
ATOM   7924  N  N     . VAL   B 1 245 ? 122.547 114.536 138.108 1.00 59.07  ?  245  VAL   B N     1 
ATOM   7925  C  CA    . VAL   B 1 245 ? 123.004 113.267 137.547 1.00 50.92  ?  245  VAL   B CA    1 
ATOM   7926  C  C     . VAL   B 1 245 ? 122.838 112.146 138.564 1.00 49.45  ?  245  VAL   B C     1 
ATOM   7927  O  O     . VAL   B 1 245 ? 122.397 111.040 138.227 1.00 63.14  ?  245  VAL   B O     1 
ATOM   7928  C  CB    . VAL   B 1 245 ? 124.460 113.384 137.064 1.00 48.32  ?  245  VAL   B CB    1 
ATOM   7929  C  CG1   . VAL   B 1 245 ? 125.034 112.009 136.765 1.00 49.37  ?  245  VAL   B CG1   1 
ATOM   7930  C  CG2   . VAL   B 1 245 ? 124.539 114.269 135.835 1.00 50.28  ?  245  VAL   B CG2   1 
ATOM   7931  N  N     . LYS   B 1 246 ? 123.168 112.417 139.829 1.00 54.45  ?  246  LYS   B N     1 
ATOM   7932  C  CA    . LYS   B 1 246 ? 123.098 111.380 140.849 1.00 56.09  ?  246  LYS   B CA    1 
ATOM   7933  C  C     . LYS   B 1 246 ? 121.663 110.980 141.166 1.00 58.94  ?  246  LYS   B C     1 
ATOM   7934  O  O     . LYS   B 1 246 ? 121.413 109.818 141.503 1.00 68.71  ?  246  LYS   B O     1 
ATOM   7935  C  CB    . LYS   B 1 246 ? 123.811 111.846 142.117 1.00 57.38  ?  246  LYS   B CB    1 
ATOM   7936  C  CG    . LYS   B 1 246 ? 125.215 111.291 142.268 1.00 57.86  ?  246  LYS   B CG    1 
ATOM   7937  C  CD    . LYS   B 1 246 ? 125.182 109.821 142.641 1.00 67.37  ?  246  LYS   B CD    1 
ATOM   7938  C  CE    . LYS   B 1 246 ? 126.345 109.068 142.020 1.00 70.92  ?  246  LYS   B CE    1 
ATOM   7939  N  NZ    . LYS   B 1 246 ? 126.262 107.606 142.285 1.00 75.21  ?  246  LYS   B NZ    1 
ATOM   7940  N  N     . TYR   B 1 247 ? 120.711 111.907 141.066 1.00 58.70  ?  247  TYR   B N     1 
ATOM   7941  C  CA    . TYR   B 1 247 ? 119.347 111.613 141.486 1.00 57.10  ?  247  TYR   B CA    1 
ATOM   7942  C  C     . TYR   B 1 247 ? 118.432 111.170 140.354 1.00 62.53  ?  247  TYR   B C     1 
ATOM   7943  O  O     . TYR   B 1 247 ? 117.486 110.418 140.609 1.00 66.08  ?  247  TYR   B O     1 
ATOM   7944  C  CB    . TYR   B 1 247 ? 118.736 112.825 142.196 1.00 56.56  ?  247  TYR   B CB    1 
ATOM   7945  C  CG    . TYR   B 1 247 ? 118.693 112.640 143.692 1.00 60.22  ?  247  TYR   B CG    1 
ATOM   7946  C  CD1   . TYR   B 1 247 ? 117.826 111.725 144.267 1.00 60.18  ?  247  TYR   B CD1   1 
ATOM   7947  C  CD2   . TYR   B 1 247 ? 119.537 113.355 144.527 1.00 58.27  ?  247  TYR   B CD2   1 
ATOM   7948  C  CE1   . TYR   B 1 247 ? 117.788 111.538 145.631 1.00 62.12  ?  247  TYR   B CE1   1 
ATOM   7949  C  CE2   . TYR   B 1 247 ? 119.505 113.174 145.895 1.00 58.62  ?  247  TYR   B CE2   1 
ATOM   7950  C  CZ    . TYR   B 1 247 ? 118.630 112.264 146.440 1.00 63.01  ?  247  TYR   B CZ    1 
ATOM   7951  O  OH    . TYR   B 1 247 ? 118.592 112.078 147.801 1.00 70.01  ?  247  TYR   B OH    1 
ATOM   7952  N  N     . VAL   B 1 248 ? 118.675 111.606 139.116 1.00 55.18  ?  248  VAL   B N     1 
ATOM   7953  C  CA    . VAL   B 1 248 ? 117.932 111.046 137.990 1.00 51.41  ?  248  VAL   B CA    1 
ATOM   7954  C  C     . VAL   B 1 248 ? 118.239 109.564 137.846 1.00 58.64  ?  248  VAL   B C     1 
ATOM   7955  O  O     . VAL   B 1 248 ? 117.344 108.752 137.591 1.00 68.72  ?  248  VAL   B O     1 
ATOM   7956  C  CB    . VAL   B 1 248 ? 118.236 111.814 136.691 1.00 51.52  ?  248  VAL   B CB    1 
ATOM   7957  C  CG1   . VAL   B 1 248 ? 117.446 111.233 135.540 1.00 52.83  ?  248  VAL   B CG1   1 
ATOM   7958  C  CG2   . VAL   B 1 248 ? 117.850 113.263 136.848 1.00 56.52  ?  248  VAL   B CG2   1 
ATOM   7959  N  N     . SER   B 1 249 ? 119.505 109.184 138.025 1.00 58.67  ?  249  SER   B N     1 
ATOM   7960  C  CA    . SER   B 1 249 ? 119.887 107.782 137.930 1.00 54.43  ?  249  SER   B CA    1 
ATOM   7961  C  C     . SER   B 1 249 ? 119.252 106.929 139.016 1.00 59.19  ?  249  SER   B C     1 
ATOM   7962  O  O     . SER   B 1 249 ? 119.299 105.698 138.919 1.00 66.97  ?  249  SER   B O     1 
ATOM   7963  C  CB    . SER   B 1 249 ? 121.406 107.646 138.000 1.00 52.78  ?  249  SER   B CB    1 
ATOM   7964  O  OG    . SER   B 1 249 ? 121.942 108.515 138.981 1.00 61.62  ?  249  SER   B OG    1 
ATOM   7965  N  N     . GLN   B 1 250 ? 118.668 107.544 140.042 1.00 55.13  ?  250  GLN   B N     1 
ATOM   7966  C  CA    . GLN   B 1 250 ? 118.063 106.798 141.134 1.00 57.19  ?  250  GLN   B CA    1 
ATOM   7967  C  C     . GLN   B 1 250 ? 116.574 107.099 141.259 1.00 63.19  ?  250  GLN   B C     1 
ATOM   7968  O  O     . GLN   B 1 250 ? 116.084 107.383 142.355 1.00 65.32  ?  250  GLN   B O     1 
ATOM   7969  C  CB    . GLN   B 1 250 ? 118.790 107.098 142.445 1.00 55.04  ?  250  GLN   B CB    1 
ATOM   7970  C  CG    . GLN   B 1 250 ? 120.303 106.982 142.338 1.00 59.13  ?  250  GLN   B CG    1 
ATOM   7971  C  CD    . GLN   B 1 250 ? 120.940 106.400 143.582 1.00 65.63  ?  250  GLN   B CD    1 
ATOM   7972  O  OE1   . GLN   B 1 250 ? 120.423 105.455 144.174 1.00 69.54  ?  250  GLN   B OE1   1 
ATOM   7973  N  NE2   . GLN   B 1 250 ? 122.073 106.962 143.984 1.00 67.43  ?  250  GLN   B NE2   1 
ATOM   7974  N  N     . ARG   B 1 251 ? 115.854 107.062 140.136 1.00 67.96  ?  251  ARG   B N     1 
ATOM   7975  C  CA    . ARG   B 1 251 ? 114.389 107.019 140.134 1.00 60.40  ?  251  ARG   B CA    1 
ATOM   7976  C  C     . ARG   B 1 251 ? 113.769 108.308 140.676 1.00 67.91  ?  251  ARG   B C     1 
ATOM   7977  O  O     . ARG   B 1 251 ? 112.875 108.275 141.521 1.00 85.04  ?  251  ARG   B O     1 
ATOM   7978  C  CB    . ARG   B 1 251 ? 113.881 105.812 140.931 1.00 58.67  ?  251  ARG   B CB    1 
ATOM   7979  C  CG    . ARG   B 1 251 ? 114.518 104.482 140.580 1.00 65.11  ?  251  ARG   B CG    1 
ATOM   7980  C  CD    . ARG   B 1 251 ? 113.848 103.358 141.346 1.00 67.33  ?  251  ARG   B CD    1 
ATOM   7981  N  NE    . ARG   B 1 251 ? 114.398 103.223 142.687 1.00 63.11  ?  251  ARG   B NE    1 
ATOM   7982  C  CZ    . ARG   B 1 251 ? 115.075 102.169 143.116 1.00 65.97  ?  251  ARG   B CZ    1 
ATOM   7983  N  NH1   . ARG   B 1 251 ? 115.279 101.117 142.342 1.00 60.70  ?  251  ARG   B NH1   1 
ATOM   7984  N  NH2   . ARG   B 1 251 ? 115.528 102.154 144.365 1.00 70.71  ?  251  ARG   B NH2   1 
ATOM   7985  N  N     . ALA   B 1 252 ? 114.231 109.451 140.177 1.00 59.10  ?  252  ALA   B N     1 
ATOM   7986  C  CA    . ALA   B 1 252 ? 113.738 110.714 140.712 1.00 54.22  ?  252  ALA   B CA    1 
ATOM   7987  C  C     . ALA   B 1 252 ? 113.693 111.790 139.638 1.00 56.94  ?  252  ALA   B C     1 
ATOM   7988  O  O     . ALA   B 1 252 ? 114.648 111.949 138.873 1.00 63.04  ?  252  ALA   B O     1 
ATOM   7989  C  CB    . ALA   B 1 252 ? 114.606 111.179 141.883 1.00 41.82  ?  252  ALA   B CB    1 
ATOM   7990  N  N     . GLY   B 1 253 ? 112.574 112.532 139.595 1.00 59.61  ?  253  GLY   B N     1 
ATOM   7991  C  CA    . GLY   B 1 253 ? 112.482 113.718 138.773 1.00 51.78  ?  253  GLY   B CA    1 
ATOM   7992  C  C     . GLY   B 1 253 ? 113.001 114.947 139.494 1.00 57.25  ?  253  GLY   B C     1 
ATOM   7993  O  O     . GLY   B 1 253 ? 113.033 115.001 140.720 1.00 68.63  ?  253  GLY   B O     1 
ATOM   7994  N  N     . ILE   B 1 254 ? 113.396 115.954 138.719 1.00 51.04  ?  254  ILE   B N     1 
ATOM   7995  C  CA    . ILE   B 1 254 ? 114.155 117.087 139.234 1.00 53.82  ?  254  ILE   B CA    1 
ATOM   7996  C  C     . ILE   B 1 254 ? 113.413 118.384 138.943 1.00 58.14  ?  254  ILE   B C     1 
ATOM   7997  O  O     . ILE   B 1 254 ? 112.957 118.612 137.816 1.00 66.45  ?  254  ILE   B O     1 
ATOM   7998  C  CB    . ILE   B 1 254 ? 115.574 117.135 138.639 1.00 55.55  ?  254  ILE   B CB    1 
ATOM   7999  C  CG1   . ILE   B 1 254 ? 116.270 115.783 138.790 1.00 53.28  ?  254  ILE   B CG1   1 
ATOM   8000  C  CG2   . ILE   B 1 254 ? 116.390 118.208 139.318 1.00 58.51  ?  254  ILE   B CG2   1 
ATOM   8001  C  CD1   . ILE   B 1 254 ? 116.356 115.289 140.214 1.00 55.82  ?  254  ILE   B CD1   1 
ATOM   8002  N  N     . GLY   B 1 255 ? 113.299 119.232 139.961 1.00 53.50  ?  255  GLY   B N     1 
ATOM   8003  C  CA    . GLY   B 1 255 ? 112.888 120.606 139.769 1.00 43.51  ?  255  GLY   B CA    1 
ATOM   8004  C  C     . GLY   B 1 255 ? 114.007 121.554 140.146 1.00 52.34  ?  255  GLY   B C     1 
ATOM   8005  O  O     . GLY   B 1 255 ? 114.334 121.694 141.327 1.00 70.68  ?  255  GLY   B O     1 
ATOM   8006  N  N     . ILE   B 1 256 ? 114.607 122.206 139.155 1.00 48.00  ?  256  ILE   B N     1 
ATOM   8007  C  CA    . ILE   B 1 256 ? 115.740 123.097 139.368 1.00 47.99  ?  256  ILE   B CA    1 
ATOM   8008  C  C     . ILE   B 1 256 ? 115.235 124.531 139.394 1.00 51.75  ?  256  ILE   B C     1 
ATOM   8009  O  O     . ILE   B 1 256 ? 114.579 124.984 138.449 1.00 61.90  ?  256  ILE   B O     1 
ATOM   8010  C  CB    . ILE   B 1 256 ? 116.809 122.922 138.276 1.00 44.76  ?  256  ILE   B CB    1 
ATOM   8011  C  CG1   . ILE   B 1 256 ? 117.135 121.447 138.052 1.00 51.27  ?  256  ILE   B CG1   1 
ATOM   8012  C  CG2   . ILE   B 1 256 ? 118.059 123.702 138.635 1.00 52.38  ?  256  ILE   B CG2   1 
ATOM   8013  C  CD1   . ILE   B 1 256 ? 116.816 120.973 136.654 1.00 50.26  ?  256  ILE   B CD1   1 
ATOM   8014  N  N     . ASN   B 1 257 ? 115.546 125.246 140.470 1.00 53.18  ?  257  ASN   B N     1 
ATOM   8015  C  CA    . ASN   B 1 257 ? 115.298 126.682 140.548 1.00 57.19  ?  257  ASN   B CA    1 
ATOM   8016  C  C     . ASN   B 1 257 ? 116.569 127.382 140.087 1.00 63.86  ?  257  ASN   B C     1 
ATOM   8017  O  O     . ASN   B 1 257 ? 117.558 127.450 140.820 1.00 65.30  ?  257  ASN   B O     1 
ATOM   8018  C  CB    . ASN   B 1 257 ? 114.900 127.089 141.963 1.00 57.73  ?  257  ASN   B CB    1 
ATOM   8019  C  CG    . ASN   B 1 257 ? 114.844 128.591 142.143 1.00 59.83  ?  257  ASN   B CG    1 
ATOM   8020  O  OD1   . ASN   B 1 257 ? 114.547 129.331 141.206 1.00 57.49  ?  257  ASN   B OD1   1 
ATOM   8021  N  ND2   . ASN   B 1 257 ? 115.172 129.055 143.343 1.00 63.39  ?  257  ASN   B ND2   1 
ATOM   8022  N  N     . ALA   B 1 258 ? 116.545 127.894 138.858 1.00 64.51  ?  258  ALA   B N     1 
ATOM   8023  C  CA    . ALA   B 1 258 ? 117.694 128.562 138.263 1.00 63.71  ?  258  ALA   B CA    1 
ATOM   8024  C  C     . ALA   B 1 258 ? 117.413 130.034 137.992 1.00 65.87  ?  258  ALA   B C     1 
ATOM   8025  O  O     . ALA   B 1 258 ? 118.025 130.635 137.109 1.00 74.57  ?  258  ALA   B O     1 
ATOM   8026  C  CB    . ALA   B 1 258 ? 118.129 127.852 136.983 1.00 64.52  ?  258  ALA   B CB    1 
ATOM   8027  N  N     . GLY   B 1 259 ? 116.534 130.640 138.785 1.00 56.00  ?  259  GLY   B N     1 
ATOM   8028  C  CA    . GLY   B 1 259 ? 116.250 132.050 138.659 1.00 57.93  ?  259  GLY   B CA    1 
ATOM   8029  C  C     . GLY   B 1 259 ? 117.227 132.967 139.347 1.00 63.95  ?  259  GLY   B C     1 
ATOM   8030  O  O     . GLY   B 1 259 ? 117.026 134.183 139.342 1.00 72.24  ?  259  GLY   B O     1 
ATOM   8031  N  N     . ARG   B 1 260 ? 118.231 132.401 140.007 1.00 69.42  ?  260  ARG   B N     1 
ATOM   8032  C  CA    A ARG   B 1 260 ? 119.282 133.254 140.628 0.50 70.30  ?  260  ARG   B CA    1 
ATOM   8033  C  CA    B ARG   B 1 260 ? 119.247 133.291 140.597 0.50 70.30  ?  260  ARG   B CA    1 
ATOM   8034  C  C     . ARG   B 1 260 ? 120.510 133.542 139.738 1.00 71.04  ?  260  ARG   B C     1 
ATOM   8035  O  O     . ARG   B 1 260 ? 121.343 134.459 139.966 1.00 75.48  ?  260  ARG   B O     1 
ATOM   8036  C  CB    A ARG   B 1 260 ? 119.776 132.640 141.941 0.50 70.93  ?  260  ARG   B CB    1 
ATOM   8037  C  CB    B ARG   B 1 260 ? 119.792 132.796 141.933 0.50 70.93  ?  260  ARG   B CB    1 
ATOM   8038  C  CG    A ARG   B 1 260 ? 118.855 132.891 143.124 0.50 68.18  ?  260  ARG   B CG    1 
ATOM   8039  C  CG    B ARG   B 1 260 ? 118.786 132.792 143.065 0.50 68.18  ?  260  ARG   B CG    1 
ATOM   8040  C  CD    A ARG   B 1 260 ? 118.881 134.356 143.506 0.50 69.56  ?  260  ARG   B CD    1 
ATOM   8041  C  CD    B ARG   B 1 260 ? 119.300 131.842 144.119 0.50 69.56  ?  260  ARG   B CD    1 
ATOM   8042  N  NE    A ARG   B 1 260 ? 120.073 134.695 144.267 0.50 74.73  ?  260  ARG   B NE    1 
ATOM   8043  N  NE    B ARG   B 1 260 ? 118.465 131.905 145.299 0.50 74.73  ?  260  ARG   B NE    1 
ATOM   8044  C  CZ    A ARG   B 1 260 ? 120.173 134.578 145.585 0.50 81.68  ?  260  ARG   B CZ    1 
ATOM   8045  C  CZ    B ARG   B 1 260 ? 118.924 132.041 146.529 0.50 81.68  ?  260  ARG   B CZ    1 
ATOM   8046  N  NH1   A ARG   B 1 260 ? 119.149 134.126 146.288 0.50 79.45  ?  260  ARG   B NH1   1 
ATOM   8047  N  NH1   B ARG   B 1 260 ? 120.226 132.114 146.744 0.50 79.45  ?  260  ARG   B NH1   1 
ATOM   8048  N  NH2   A ARG   B 1 260 ? 121.296 134.910 146.195 0.50 80.20  ?  260  ARG   B NH2   1 
ATOM   8049  N  NH2   B ARG   B 1 260 ? 118.078 132.094 147.539 0.50 80.20  ?  260  ARG   B NH2   1 
ATOM   8050  N  N     . ILE   B 1 261 ? 120.596 132.807 138.629 1.00 57.25  ?  261  ILE   B N     1 
ATOM   8051  C  CA    . ILE   B 1 261 ? 121.725 133.016 137.732 1.00 58.00  ?  261  ILE   B CA    1 
ATOM   8052  C  C     . ILE   B 1 261 ? 121.606 134.387 137.084 1.00 64.62  ?  261  ILE   B C     1 
ATOM   8053  O  O     . ILE   B 1 261 ? 120.549 134.752 136.554 1.00 70.94  ?  261  ILE   B O     1 
ATOM   8054  C  CB    . ILE   B 1 261 ? 121.790 131.900 136.680 1.00 60.03  ?  261  ILE   B CB    1 
ATOM   8055  C  CG1   . ILE   B 1 261 ? 121.716 130.529 137.357 1.00 58.67  ?  261  ILE   B CG1   1 
ATOM   8056  C  CG2   . ILE   B 1 261 ? 123.058 132.022 135.851 1.00 64.74  ?  261  ILE   B CG2   1 
ATOM   8057  C  CD1   . ILE   B 1 261 ? 122.000 129.368 136.431 1.00 61.52  ?  261  ILE   B CD1   1 
ATOM   8058  N  N     . ARG   B 1 262 ? 122.691 135.155 137.126 1.00 67.03  ?  262  ARG   B N     1 
ATOM   8059  C  CA    . ARG   B 1 262 ? 122.671 136.513 136.610 1.00 63.81  ?  262  ARG   B CA    1 
ATOM   8060  C  C     . ARG   B 1 262 ? 122.495 136.513 135.093 1.00 67.60  ?  262  ARG   B C     1 
ATOM   8061  O  O     . ARG   B 1 262 ? 122.825 135.549 134.398 1.00 77.74  ?  262  ARG   B O     1 
ATOM   8062  C  CB    . ARG   B 1 262 ? 123.948 137.255 137.002 1.00 61.85  ?  262  ARG   B CB    1 
ATOM   8063  C  CG    . ARG   B 1 262 ? 125.204 136.753 136.322 1.00 64.11  ?  262  ARG   B CG    1 
ATOM   8064  C  CD    . ARG   B 1 262 ? 126.448 137.322 136.978 1.00 67.35  ?  262  ARG   B CD    1 
ATOM   8065  N  NE    . ARG   B 1 262 ? 126.516 136.999 138.397 1.00 66.47  ?  262  ARG   B NE    1 
ATOM   8066  C  CZ    . ARG   B 1 262 ? 127.581 137.199 139.161 1.00 66.46  ?  262  ARG   B CZ    1 
ATOM   8067  N  NH1   . ARG   B 1 262 ? 128.689 137.736 138.677 1.00 70.38  ?  262  ARG   B NH1   1 
ATOM   8068  N  NH2   . ARG   B 1 262 ? 127.534 136.849 140.443 1.00 64.44  ?  262  ARG   B NH2   1 
ATOM   8069  N  N     . ALA   B 1 263 ? 121.960 137.620 134.586 1.00 67.24  ?  263  ALA   B N     1 
ATOM   8070  C  CA    . ALA   B 1 263 ? 121.588 137.713 133.185 1.00 67.83  ?  263  ALA   B CA    1 
ATOM   8071  C  C     . ALA   B 1 263 ? 122.825 137.823 132.294 1.00 74.72  ?  263  ALA   B C     1 
ATOM   8072  O  O     . ALA   B 1 263 ? 123.952 138.018 132.758 1.00 79.49  ?  263  ALA   B O     1 
ATOM   8073  C  CB    . ALA   B 1 263 ? 120.665 138.908 132.957 1.00 65.72  ?  263  ALA   B CB    1 
ATOM   8074  N  N     . LEU   B 1 264 ? 122.592 137.683 130.990 1.00 76.21  ?  264  LEU   B N     1 
ATOM   8075  C  CA    . LEU   B 1 264 ? 123.660 137.819 130.008 1.00 76.41  ?  264  LEU   B CA    1 
ATOM   8076  C  C     . LEU   B 1 264 ? 124.251 139.221 130.053 1.00 73.64  ?  264  LEU   B C     1 
ATOM   8077  O  O     . LEU   B 1 264 ? 123.531 140.216 130.162 1.00 77.69  ?  264  LEU   B O     1 
ATOM   8078  C  CB    . LEU   B 1 264 ? 123.134 137.521 128.601 1.00 73.25  ?  264  LEU   B CB    1 
ATOM   8079  C  CG    . LEU   B 1 264 ? 123.965 137.999 127.407 1.00 74.32  ?  264  LEU   B CG    1 
ATOM   8080  C  CD1   . LEU   B 1 264 ? 124.982 136.939 127.038 1.00 74.64  ?  264  LEU   B CD1   1 
ATOM   8081  C  CD2   . LEU   B 1 264 ? 123.032 138.254 126.238 1.00 76.05  ?  264  LEU   B CD2   1 
ATOM   8082  N  N     . GLY   B 1 265 ? 125.574 139.298 129.973 1.00 63.82  ?  265  GLY   B N     1 
ATOM   8083  C  CA    . GLY   B 1 265 ? 126.260 140.567 130.017 1.00 64.84  ?  265  GLY   B CA    1 
ATOM   8084  C  C     . GLY   B 1 265 ? 126.566 141.081 131.404 1.00 68.01  ?  265  GLY   B C     1 
ATOM   8085  O  O     . GLY   B 1 265 ? 127.129 142.173 131.528 1.00 71.79  ?  265  GLY   B O     1 
ATOM   8086  N  N     . SER   B 1 266 ? 126.120 140.389 132.443 1.00 72.27  ?  266  SER   B N     1 
ATOM   8087  C  CA    . SER   B 1 266 ? 126.345 140.857 133.800 1.00 71.02  ?  266  SER   B CA    1 
ATOM   8088  C  C     . SER   B 1 266 ? 127.822 140.714 134.158 1.00 74.92  ?  266  SER   B C     1 
ATOM   8089  O  O     . SER   B 1 266 ? 128.447 139.710 133.812 1.00 77.54  ?  266  SER   B O     1 
ATOM   8090  C  CB    . SER   B 1 266 ? 125.487 140.063 134.782 1.00 68.92  ?  266  SER   B CB    1 
ATOM   8091  O  OG    . SER   B 1 266 ? 124.261 140.720 135.050 1.00 76.33  ?  266  SER   B OG    1 
ATOM   8092  N  N     . PRO   B 1 267 ? 128.406 141.692 134.843 1.00 74.86  ?  267  PRO   B N     1 
ATOM   8093  C  CA    . PRO   B 1 267 ? 129.828 141.600 135.189 1.00 68.55  ?  267  PRO   B CA    1 
ATOM   8094  C  C     . PRO   B 1 267 ? 130.105 140.466 136.164 1.00 73.21  ?  267  PRO   B C     1 
ATOM   8095  O  O     . PRO   B 1 267 ? 129.269 140.108 136.997 1.00 78.95  ?  267  PRO   B O     1 
ATOM   8096  C  CB    . PRO   B 1 267 ? 130.128 142.962 135.825 1.00 66.18  ?  267  PRO   B CB    1 
ATOM   8097  C  CG    . PRO   B 1 267 ? 128.802 143.474 136.274 1.00 69.62  ?  267  PRO   B CG    1 
ATOM   8098  C  CD    . PRO   B 1 267 ? 127.803 142.955 135.292 1.00 73.05  ?  267  PRO   B CD    1 
ATOM   8099  N  N     . ILE   B 1 268 ? 131.303 139.900 136.047 1.00 68.60  ?  268  ILE   B N     1 
ATOM   8100  C  CA    . ILE   B 1 268 ? 131.782 138.850 136.938 1.00 64.93  ?  268  ILE   B CA    1 
ATOM   8101  C  C     . ILE   B 1 268 ? 133.068 139.337 137.587 1.00 69.72  ?  268  ILE   B C     1 
ATOM   8102  O  O     . ILE   B 1 268 ? 133.987 139.785 136.891 1.00 79.68  ?  268  ILE   B O     1 
ATOM   8103  C  CB    . ILE   B 1 268 ? 132.015 137.526 136.189 1.00 69.62  ?  268  ILE   B CB    1 
ATOM   8104  C  CG1   . ILE   B 1 268 ? 130.698 136.988 135.634 1.00 68.79  ?  268  ILE   B CG1   1 
ATOM   8105  C  CG2   . ILE   B 1 268 ? 132.666 136.500 137.102 1.00 67.40  ?  268  ILE   B CG2   1 
ATOM   8106  C  CD1   . ILE   B 1 268 ? 130.877 136.047 134.476 1.00 68.24  ?  268  ILE   B CD1   1 
ATOM   8107  N  N     . ARG   B 1 269 ? 133.129 139.249 138.917 1.00 78.20  ?  269  ARG   B N     1 
ATOM   8108  C  CA    . ARG   B 1 269 ? 134.284 139.707 139.691 1.00 80.45  ?  269  ARG   B CA    1 
ATOM   8109  C  C     . ARG   B 1 269 ? 134.579 141.183 139.430 1.00 84.87  ?  269  ARG   B C     1 
ATOM   8110  O  O     . ARG   B 1 269 ? 135.736 141.605 139.377 1.00 87.00  ?  269  ARG   B O     1 
ATOM   8111  C  CB    . ARG   B 1 269 ? 135.518 138.846 139.409 1.00 76.72  ?  269  ARG   B CB    1 
ATOM   8112  C  CG    . ARG   B 1 269 ? 135.606 137.599 140.267 1.00 77.83  ?  269  ARG   B CG    1 
ATOM   8113  C  CD    . ARG   B 1 269 ? 136.833 136.773 139.930 1.00 80.09  ?  269  ARG   B CD    1 
ATOM   8114  N  NE    . ARG   B 1 269 ? 137.017 136.621 138.492 1.00 83.88  ?  269  ARG   B NE    1 
ATOM   8115  C  CZ    . ARG   B 1 269 ? 136.603 135.576 137.790 1.00 83.98  ?  269  ARG   B CZ    1 
ATOM   8116  N  NH1   . ARG   B 1 269 ? 135.963 134.569 138.362 1.00 80.11  ?  269  ARG   B NH1   1 
ATOM   8117  N  NH2   . ARG   B 1 269 ? 136.857 135.529 136.486 1.00 82.67  ?  269  ARG   B NH2   1 
ATOM   8118  N  N     . GLY   B 1 270 ? 133.522 141.974 139.263 1.00 85.94  ?  270  GLY   B N     1 
ATOM   8119  C  CA    . GLY   B 1 270 ? 133.655 143.404 139.089 1.00 85.97  ?  270  GLY   B CA    1 
ATOM   8120  C  C     . GLY   B 1 270 ? 133.958 143.868 137.682 1.00 87.35  ?  270  GLY   B C     1 
ATOM   8121  O  O     . GLY   B 1 270 ? 134.037 145.082 137.455 1.00 91.83  ?  270  GLY   B O     1 
ATOM   8122  N  N     . GLY   B 1 271 ? 134.131 142.954 136.731 1.00 82.87  ?  271  GLY   B N     1 
ATOM   8123  C  CA    . GLY   B 1 271 ? 134.397 143.346 135.363 1.00 82.08  ?  271  GLY   B CA    1 
ATOM   8124  C  C     . GLY   B 1 271 ? 135.492 142.545 134.693 1.00 83.64  ?  271  GLY   B C     1 
ATOM   8125  O  O     . GLY   B 1 271 ? 135.776 142.751 133.510 1.00 83.74  ?  271  GLY   B O     1 
ATOM   8126  N  N     . GLU   B 1 272 ? 136.123 141.635 135.439 1.00 99.17  ?  272  GLU   B N     1 
ATOM   8127  C  CA    . GLU   B 1 272 ? 137.158 140.791 134.852 1.00 101.02 ?  272  GLU   B CA    1 
ATOM   8128  C  C     . GLU   B 1 272 ? 136.584 139.898 133.760 1.00 104.07 ?  272  GLU   B C     1 
ATOM   8129  O  O     . GLU   B 1 272 ? 137.201 139.716 132.704 1.00 108.82 ?  272  GLU   B O     1 
ATOM   8130  C  CB    . GLU   B 1 272 ? 137.828 139.950 135.937 1.00 98.36  ?  272  GLU   B CB    1 
ATOM   8131  C  CG    . GLU   B 1 272 ? 138.147 140.719 137.202 1.00 102.76 ?  272  GLU   B CG    1 
ATOM   8132  C  CD    . GLU   B 1 272 ? 139.031 139.938 138.148 1.00 107.41 ?  272  GLU   B CD    1 
ATOM   8133  O  OE1   . GLU   B 1 272 ? 139.823 140.576 138.872 1.00 110.49 ?  272  GLU   B OE1   1 
ATOM   8134  O  OE2   . GLU   B 1 272 ? 139.041 138.694 138.057 1.00 105.57 ?  272  GLU   B OE2   1 
ATOM   8135  N  N     . ALA   B 1 273 ? 135.406 139.332 133.997 1.00 89.29  ?  273  ALA   B N     1 
ATOM   8136  C  CA    . ALA   B 1 273 ? 134.695 138.546 133.004 1.00 84.99  ?  273  ALA   B CA    1 
ATOM   8137  C  C     . ALA   B 1 273 ? 133.252 139.021 132.950 1.00 82.82  ?  273  ALA   B C     1 
ATOM   8138  O  O     . ALA   B 1 273 ? 132.753 139.667 133.875 1.00 85.80  ?  273  ALA   B O     1 
ATOM   8139  C  CB    . ALA   B 1 273 ? 134.737 137.038 133.316 1.00 81.91  ?  273  ALA   B CB    1 
ATOM   8140  N  N     . PHE   B 1 274 ? 132.565 138.651 131.874 1.00 73.23  ?  274  PHE   B N     1 
ATOM   8141  C  CA    . PHE   B 1 274 ? 131.164 139.001 131.689 1.00 74.21  ?  274  PHE   B CA    1 
ATOM   8142  C  C     . PHE   B 1 274 ? 130.348 137.741 131.422 1.00 75.95  ?  274  PHE   B C     1 
ATOM   8143  O  O     . PHE   B 1 274 ? 130.802 136.838 130.721 1.00 79.26  ?  274  PHE   B O     1 
ATOM   8144  C  CB    . PHE   B 1 274 ? 130.995 140.008 130.548 1.00 72.80  ?  274  PHE   B CB    1 
ATOM   8145  C  CG    . PHE   B 1 274 ? 131.391 141.406 130.920 1.00 78.78  ?  274  PHE   B CG    1 
ATOM   8146  C  CD1   . PHE   B 1 274 ? 130.495 142.244 131.561 1.00 80.41  ?  274  PHE   B CD1   1 
ATOM   8147  C  CD2   . PHE   B 1 274 ? 132.663 141.876 130.647 1.00 79.32  ?  274  PHE   B CD2   1 
ATOM   8148  C  CE1   . PHE   B 1 274 ? 130.855 143.526 131.912 1.00 78.76  ?  274  PHE   B CE1   1 
ATOM   8149  C  CE2   . PHE   B 1 274 ? 133.031 143.160 130.997 1.00 79.41  ?  274  PHE   B CE2   1 
ATOM   8150  C  CZ    . PHE   B 1 274 ? 132.126 143.986 131.631 1.00 78.88  ?  274  PHE   B CZ    1 
ATOM   8151  N  N     . HIS   B 1 275 ? 129.152 137.671 132.001 1.00 66.17  ?  275  HIS   B N     1 
ATOM   8152  C  CA    . HIS   B 1 275 ? 128.344 136.458 131.930 1.00 61.25  ?  275  HIS   B CA    1 
ATOM   8153  C  C     . HIS   B 1 275 ? 127.911 136.218 130.505 1.00 68.60  ?  275  HIS   B C     1 
ATOM   8154  O  O     . HIS   B 1 275 ? 127.620 137.157 129.786 1.00 75.53  ?  275  HIS   B O     1 
ATOM   8155  C  CB    . HIS   B 1 275 ? 127.143 136.599 132.853 1.00 59.37  ?  275  HIS   B CB    1 
ATOM   8156  C  CG    . HIS   B 1 275 ? 126.598 135.320 133.365 1.00 64.95  ?  275  HIS   B CG    1 
ATOM   8157  N  ND1   . HIS   B 1 275 ? 125.521 134.708 132.777 1.00 69.38  ?  275  HIS   B ND1   1 
ATOM   8158  C  CD2   . HIS   B 1 275 ? 126.913 134.583 134.448 1.00 67.03  ?  275  HIS   B CD2   1 
ATOM   8159  C  CE1   . HIS   B 1 275 ? 125.214 133.623 133.457 1.00 66.97  ?  275  HIS   B CE1   1 
ATOM   8160  N  NE2   . HIS   B 1 275 ? 126.036 133.531 134.484 1.00 70.10  ?  275  HIS   B NE2   1 
ATOM   8161  N  N     . THR   B 1 276 ? 127.901 134.963 130.098 1.00 74.26  ?  276  THR   B N     1 
ATOM   8162  C  CA    . THR   B 1 276 ? 127.513 134.549 128.760 1.00 73.52  ?  276  THR   B CA    1 
ATOM   8163  C  C     . THR   B 1 276 ? 126.048 134.144 128.669 1.00 71.34  ?  276  THR   B C     1 
ATOM   8164  O  O     . THR   B 1 276 ? 125.610 133.700 127.604 1.00 73.53  ?  276  THR   B O     1 
ATOM   8165  C  CB    . THR   B 1 276 ? 128.397 133.386 128.298 1.00 71.73  ?  276  THR   B CB    1 
ATOM   8166  O  OG1   . THR   B 1 276 ? 128.371 132.343 129.280 1.00 79.33  ?  276  THR   B OG1   1 
ATOM   8167  C  CG2   . THR   B 1 276 ? 129.830 133.855 128.102 1.00 69.58  ?  276  THR   B CG2   1 
ATOM   8168  N  N     . GLY   B 1 277 ? 125.287 134.283 129.748 1.00 72.07  ?  277  GLY   B N     1 
ATOM   8169  C  CA    . GLY   B 1 277 ? 123.873 133.981 129.743 1.00 73.24  ?  277  GLY   B CA    1 
ATOM   8170  C  C     . GLY   B 1 277 ? 123.557 132.669 130.438 1.00 80.10  ?  277  GLY   B C     1 
ATOM   8171  O  O     . GLY   B 1 277 ? 124.430 131.856 130.750 1.00 82.69  ?  277  GLY   B O     1 
ATOM   8172  N  N     . CYS   B 1 278 ? 122.263 132.472 130.687 1.00 83.07  ?  278  CYS   B N     1 
ATOM   8173  C  CA    . CYS   B 1 278 ? 121.786 131.265 131.345 1.00 82.79  ?  278  CYS   B CA    1 
ATOM   8174  C  C     . CYS   B 1 278 ? 121.570 130.103 130.384 1.00 84.22  ?  278  CYS   B C     1 
ATOM   8175  O  O     . CYS   B 1 278 ? 121.411 128.967 130.842 1.00 88.50  ?  278  CYS   B O     1 
ATOM   8176  C  CB    . CYS   B 1 278 ? 120.480 131.559 132.084 1.00 84.46  ?  278  CYS   B CB    1 
ATOM   8177  S  SG    . CYS   B 1 278 ? 120.557 132.958 133.224 1.00 102.75 ?  278  CYS   B SG    1 
ATOM   8178  N  N     . ILE   B 1 279 ? 121.561 130.359 129.074 1.00 71.58  ?  279  ILE   B N     1 
ATOM   8179  C  CA    . ILE   B 1 279 ? 121.266 129.295 128.111 1.00 61.56  ?  279  ILE   B CA    1 
ATOM   8180  C  C     . ILE   B 1 279 ? 122.303 128.177 128.134 1.00 66.63  ?  279  ILE   B C     1 
ATOM   8181  O  O     . ILE   B 1 279 ? 121.906 127.000 128.138 1.00 74.49  ?  279  ILE   B O     1 
ATOM   8182  C  CB    . ILE   B 1 279 ? 121.071 129.893 126.706 1.00 70.76  ?  279  ILE   B CB    1 
ATOM   8183  C  CG1   . ILE   B 1 279 ? 120.197 131.145 126.776 1.00 72.85  ?  279  ILE   B CG1   1 
ATOM   8184  C  CG2   . ILE   B 1 279 ? 120.446 128.868 125.774 1.00 68.10  ?  279  ILE   B CG2   1 
ATOM   8185  C  CD1   . ILE   B 1 279 ? 118.738 130.877 127.001 1.00 71.18  ?  279  ILE   B CD1   1 
ATOM   8186  N  N     . PRO   B 1 280 ? 123.617 128.447 128.119 1.00 62.85  ?  280  PRO   B N     1 
ATOM   8187  C  CA    . PRO   B 1 280 ? 124.571 127.324 128.186 1.00 63.91  ?  280  PRO   B CA    1 
ATOM   8188  C  C     . PRO   B 1 280 ? 124.454 126.505 129.461 1.00 67.35  ?  280  PRO   B C     1 
ATOM   8189  O  O     . PRO   B 1 280 ? 124.602 125.276 129.424 1.00 76.28  ?  280  PRO   B O     1 
ATOM   8190  C  CB    . PRO   B 1 280 ? 125.933 128.021 128.067 1.00 62.13  ?  280  PRO   B CB    1 
ATOM   8191  C  CG    . PRO   B 1 280 ? 125.631 129.316 127.395 1.00 59.34  ?  280  PRO   B CG    1 
ATOM   8192  C  CD    . PRO   B 1 280 ? 124.323 129.733 127.968 1.00 58.96  ?  280  PRO   B CD    1 
ATOM   8193  N  N     . PHE   B 1 281 ? 124.162 127.145 130.594 1.00 57.18  ?  281  PHE   B N     1 
ATOM   8194  C  CA    . PHE   B 1 281 ? 123.969 126.392 131.828 1.00 57.79  ?  281  PHE   B CA    1 
ATOM   8195  C  C     . PHE   B 1 281 ? 122.677 125.585 131.791 1.00 58.07  ?  281  PHE   B C     1 
ATOM   8196  O  O     . PHE   B 1 281 ? 122.620 124.479 132.340 1.00 69.17  ?  281  PHE   B O     1 
ATOM   8197  C  CB    . PHE   B 1 281 ? 123.990 127.338 133.026 1.00 57.96  ?  281  PHE   B CB    1 
ATOM   8198  C  CG    . PHE   B 1 281 ? 125.298 128.054 133.200 1.00 62.26  ?  281  PHE   B CG    1 
ATOM   8199  C  CD1   . PHE   B 1 281 ? 126.468 127.342 133.400 1.00 61.55  ?  281  PHE   B CD1   1 
ATOM   8200  C  CD2   . PHE   B 1 281 ? 125.360 129.435 133.153 1.00 60.76  ?  281  PHE   B CD2   1 
ATOM   8201  C  CE1   . PHE   B 1 281 ? 127.675 127.995 133.556 1.00 60.85  ?  281  PHE   B CE1   1 
ATOM   8202  C  CE2   . PHE   B 1 281 ? 126.565 130.093 133.309 1.00 60.09  ?  281  PHE   B CE2   1 
ATOM   8203  C  CZ    . PHE   B 1 281 ? 127.723 129.371 133.510 1.00 62.39  ?  281  PHE   B CZ    1 
ATOM   8204  N  N     . TYR   B 1 282 ? 121.639 126.112 131.139 1.00 53.40  ?  282  TYR   B N     1 
ATOM   8205  C  CA    . TYR   B 1 282 ? 120.420 125.334 130.943 1.00 56.72  ?  282  TYR   B CA    1 
ATOM   8206  C  C     . TYR   B 1 282 ? 120.689 124.116 130.069 1.00 64.52  ?  282  TYR   B C     1 
ATOM   8207  O  O     . TYR   B 1 282 ? 120.146 123.033 130.313 1.00 68.67  ?  282  TYR   B O     1 
ATOM   8208  C  CB    . TYR   B 1 282 ? 119.330 126.210 130.324 1.00 57.72  ?  282  TYR   B CB    1 
ATOM   8209  C  CG    . TYR   B 1 282 ? 118.707 127.210 131.275 1.00 56.03  ?  282  TYR   B CG    1 
ATOM   8210  C  CD1   . TYR   B 1 282 ? 119.264 127.462 132.521 1.00 56.49  ?  282  TYR   B CD1   1 
ATOM   8211  C  CD2   . TYR   B 1 282 ? 117.559 127.905 130.923 1.00 62.33  ?  282  TYR   B CD2   1 
ATOM   8212  C  CE1   . TYR   B 1 282 ? 118.696 128.375 133.386 1.00 62.09  ?  282  TYR   B CE1   1 
ATOM   8213  C  CE2   . TYR   B 1 282 ? 116.984 128.818 131.783 1.00 62.11  ?  282  TYR   B CE2   1 
ATOM   8214  C  CZ    . TYR   B 1 282 ? 117.557 129.050 133.012 1.00 65.89  ?  282  TYR   B CZ    1 
ATOM   8215  O  OH    . TYR   B 1 282 ? 116.986 129.960 133.871 1.00 69.51  ?  282  TYR   B OH    1 
ATOM   8216  N  N     . LYS   B 1 283 ? 121.527 124.277 129.042 1.00 51.54  ?  283  LYS   B N     1 
ATOM   8217  C  CA    . LYS   B 1 283 ? 121.920 123.141 128.215 1.00 48.44  ?  283  LYS   B CA    1 
ATOM   8218  C  C     . LYS   B 1 283 ? 122.696 122.114 129.028 1.00 58.19  ?  283  LYS   B C     1 
ATOM   8219  O  O     . LYS   B 1 283 ? 122.520 120.903 128.847 1.00 71.55  ?  283  LYS   B O     1 
ATOM   8220  C  CB    . LYS   B 1 283 ? 122.749 123.622 127.026 1.00 52.74  ?  283  LYS   B CB    1 
ATOM   8221  C  CG    . LYS   B 1 283 ? 121.927 124.187 125.887 1.00 53.21  ?  283  LYS   B CG    1 
ATOM   8222  C  CD    . LYS   B 1 283 ? 122.719 125.211 125.094 1.00 60.25  ?  283  LYS   B CD    1 
ATOM   8223  C  CE    . LYS   B 1 283 ? 121.975 125.622 123.838 1.00 66.86  ?  283  LYS   B CE    1 
ATOM   8224  N  NZ    . LYS   B 1 283 ? 121.344 124.455 123.166 1.00 65.12  ?  283  LYS   B NZ    1 
ATOM   8225  N  N     . HIS   B 1 284 ? 123.572 122.582 129.921 1.00 48.16  ?  284  HIS   B N     1 
ATOM   8226  C  CA    . HIS   B 1 284 ? 124.285 121.665 130.805 1.00 46.83  ?  284  HIS   B CA    1 
ATOM   8227  C  C     . HIS   B 1 284 ? 123.319 120.890 131.691 1.00 52.64  ?  284  HIS   B C     1 
ATOM   8228  O  O     . HIS   B 1 284 ? 123.467 119.676 131.873 1.00 61.43  ?  284  HIS   B O     1 
ATOM   8229  C  CB    . HIS   B 1 284 ? 125.292 122.427 131.662 1.00 48.99  ?  284  HIS   B CB    1 
ATOM   8230  C  CG    . HIS   B 1 284 ? 126.387 121.567 132.210 1.00 53.77  ?  284  HIS   B CG    1 
ATOM   8231  N  ND1   . HIS   B 1 284 ? 127.179 121.950 133.270 1.00 60.44  ?  284  HIS   B ND1   1 
ATOM   8232  C  CD2   . HIS   B 1 284 ? 126.812 120.335 131.851 1.00 56.00  ?  284  HIS   B CD2   1 
ATOM   8233  C  CE1   . HIS   B 1 284 ? 128.051 120.994 133.532 1.00 59.26  ?  284  HIS   B CE1   1 
ATOM   8234  N  NE2   . HIS   B 1 284 ? 127.870 120.017 132.664 1.00 54.12  ?  284  HIS   B NE2   1 
ATOM   8235  N  N     . PHE   B 1 285 ? 122.320 121.576 132.250 1.00 46.28  ?  285  PHE   B N     1 
ATOM   8236  C  CA    . PHE   B 1 285 ? 121.322 120.892 133.067 1.00 40.80  ?  285  PHE   B CA    1 
ATOM   8237  C  C     . PHE   B 1 285 ? 120.546 119.869 132.246 1.00 49.86  ?  285  PHE   B C     1 
ATOM   8238  O  O     . PHE   B 1 285 ? 120.268 118.761 132.720 1.00 61.60  ?  285  PHE   B O     1 
ATOM   8239  C  CB    . PHE   B 1 285 ? 120.366 121.906 133.696 1.00 40.11  ?  285  PHE   B CB    1 
ATOM   8240  C  CG    . PHE   B 1 285 ? 121.005 122.784 134.731 1.00 43.69  ?  285  PHE   B CG    1 
ATOM   8241  C  CD1   . PHE   B 1 285 ? 122.095 122.341 135.458 1.00 47.12  ?  285  PHE   B CD1   1 
ATOM   8242  C  CD2   . PHE   B 1 285 ? 120.512 124.054 134.980 1.00 52.21  ?  285  PHE   B CD2   1 
ATOM   8243  C  CE1   . PHE   B 1 285 ? 122.683 123.148 136.410 1.00 51.37  ?  285  PHE   B CE1   1 
ATOM   8244  C  CE2   . PHE   B 1 285 ? 121.097 124.865 135.932 1.00 53.07  ?  285  PHE   B CE2   1 
ATOM   8245  C  CZ    . PHE   B 1 285 ? 122.184 124.413 136.646 1.00 47.15  ?  285  PHE   B CZ    1 
ATOM   8246  N  N     . GLN   B 1 286 ? 120.185 120.225 131.012 1.00 49.87  ?  286  GLN   B N     1 
ATOM   8247  C  CA    . GLN   B 1 286 ? 119.443 119.303 130.158 1.00 46.73  ?  286  GLN   B CA    1 
ATOM   8248  C  C     . GLN   B 1 286 ? 120.264 118.062 129.837 1.00 51.14  ?  286  GLN   B C     1 
ATOM   8249  O  O     . GLN   B 1 286 ? 119.746 116.940 129.862 1.00 62.69  ?  286  GLN   B O     1 
ATOM   8250  C  CB    . GLN   B 1 286 ? 119.009 120.009 128.874 1.00 46.51  ?  286  GLN   B CB    1 
ATOM   8251  C  CG    . GLN   B 1 286 ? 118.419 119.076 127.816 1.00 53.79  ?  286  GLN   B CG    1 
ATOM   8252  C  CD    . GLN   B 1 286 ? 118.193 119.784 126.497 1.00 63.88  ?  286  GLN   B CD    1 
ATOM   8253  O  OE1   . GLN   B 1 286 ? 117.058 119.964 126.062 1.00 71.67  ?  286  GLN   B OE1   1 
ATOM   8254  N  NE2   . GLN   B 1 286 ? 119.267 120.293 125.915 1.00 68.44  ?  286  GLN   B NE2   1 
ATOM   8255  N  N     . THR   B 1 287 ? 121.547 118.242 129.529 1.00 51.94  ?  287  THR   B N     1 
ATOM   8256  C  CA    . THR   B 1 287 ? 122.397 117.089 129.261 1.00 45.92  ?  287  THR   B CA    1 
ATOM   8257  C  C     . THR   B 1 287 ? 122.608 116.244 130.511 1.00 52.19  ?  287  THR   B C     1 
ATOM   8258  O  O     . THR   B 1 287 ? 122.702 115.016 130.417 1.00 63.43  ?  287  THR   B O     1 
ATOM   8259  C  CB    . THR   B 1 287 ? 123.744 117.534 128.697 1.00 48.41  ?  287  THR   B CB    1 
ATOM   8260  O  OG1   . THR   B 1 287 ? 124.279 118.608 129.479 1.00 63.91  ?  287  THR   B OG1   1 
ATOM   8261  C  CG2   . THR   B 1 287 ? 123.625 117.955 127.243 1.00 47.79  ?  287  THR   B CG2   1 
ATOM   8262  N  N     . ALA   B 1 288 ? 122.679 116.877 131.684 1.00 46.49  ?  288  ALA   B N     1 
ATOM   8263  C  CA    . ALA   B 1 288 ? 122.759 116.119 132.928 1.00 44.59  ?  288  ALA   B CA    1 
ATOM   8264  C  C     . ALA   B 1 288 ? 121.508 115.274 133.136 1.00 54.45  ?  288  ALA   B C     1 
ATOM   8265  O  O     . ALA   B 1 288 ? 121.594 114.119 133.568 1.00 70.65  ?  288  ALA   B O     1 
ATOM   8266  C  CB    . ALA   B 1 288 ? 122.970 117.067 134.108 1.00 43.82  ?  288  ALA   B CB    1 
ATOM   8267  N  N     . VAL   B 1 289 ? 120.335 115.837 132.839 1.00 57.82  ?  289  VAL   B N     1 
ATOM   8268  C  CA    . VAL   B 1 289 ? 119.089 115.089 132.992 1.00 53.28  ?  289  VAL   B CA    1 
ATOM   8269  C  C     . VAL   B 1 289 ? 119.018 113.942 131.992 1.00 59.30  ?  289  VAL   B C     1 
ATOM   8270  O  O     . VAL   B 1 289 ? 118.601 112.830 132.334 1.00 66.95  ?  289  VAL   B O     1 
ATOM   8271  C  CB    . VAL   B 1 289 ? 117.877 116.028 132.862 1.00 50.10  ?  289  VAL   B CB    1 
ATOM   8272  C  CG1   . VAL   B 1 289 ? 116.584 115.252 133.005 1.00 57.27  ?  289  VAL   B CG1   1 
ATOM   8273  C  CG2   . VAL   B 1 289 ? 117.938 117.087 133.938 1.00 58.65  ?  289  VAL   B CG2   1 
ATOM   8274  N  N     . LYS   B 1 290 ? 119.417 114.190 130.746 1.00 61.17  ?  290  LYS   B N     1 
ATOM   8275  C  CA    . LYS   B 1 290 ? 119.267 113.192 129.694 1.00 59.27  ?  290  LYS   B CA    1 
ATOM   8276  C  C     . LYS   B 1 290 ? 120.408 112.182 129.644 1.00 64.06  ?  290  LYS   B C     1 
ATOM   8277  O  O     . LYS   B 1 290 ? 120.309 111.208 128.890 1.00 66.07  ?  290  LYS   B O     1 
ATOM   8278  C  CB    . LYS   B 1 290 ? 119.140 113.878 128.331 1.00 56.61  ?  290  LYS   B CB    1 
ATOM   8279  C  CG    . LYS   B 1 290 ? 117.960 114.826 128.216 1.00 62.21  ?  290  LYS   B CG    1 
ATOM   8280  C  CD    . LYS   B 1 290 ? 116.641 114.078 128.282 1.00 63.27  ?  290  LYS   B CD    1 
ATOM   8281  C  CE    . LYS   B 1 290 ? 115.558 114.930 128.922 1.00 66.48  ?  290  LYS   B CE    1 
ATOM   8282  N  NZ    . LYS   B 1 290 ? 114.247 114.227 128.964 1.00 68.39  ?  290  LYS   B NZ    1 
ATOM   8283  N  N     . SER   B 1 291 ? 121.483 112.386 130.413 1.00 61.35  ?  291  SER   B N     1 
ATOM   8284  C  CA    . SER   B 1 291 ? 122.612 111.460 130.365 1.00 61.40  ?  291  SER   B CA    1 
ATOM   8285  C  C     . SER   B 1 291 ? 122.216 110.074 130.854 1.00 58.75  ?  291  SER   B C     1 
ATOM   8286  O  O     . SER   B 1 291 ? 122.620 109.063 130.269 1.00 65.10  ?  291  SER   B O     1 
ATOM   8287  C  CB    . SER   B 1 291 ? 123.778 111.999 131.193 1.00 62.04  ?  291  SER   B CB    1 
ATOM   8288  O  OG    . SER   B 1 291 ? 123.351 112.327 132.504 1.00 67.02  ?  291  SER   B OG    1 
ATOM   8289  N  N     . CYS   B 1 292 ? 121.426 110.003 131.917 1.00 67.39  ?  292  CYS   B N     1 
ATOM   8290  C  CA    . CYS   B 1 292 ? 121.057 108.739 132.531 1.00 70.11  ?  292  CYS   B CA    1 
ATOM   8291  C  C     . CYS   B 1 292 ? 119.554 108.515 132.424 1.00 72.61  ?  292  CYS   B C     1 
ATOM   8292  O  O     . CYS   B 1 292 ? 118.794 109.397 132.021 1.00 79.44  ?  292  CYS   B O     1 
ATOM   8293  C  CB    . CYS   B 1 292 ? 121.490 108.701 134.001 1.00 72.57  ?  292  CYS   B CB    1 
ATOM   8294  S  SG    . CYS   B 1 292 ? 123.271 108.757 134.273 1.00 89.39  ?  292  CYS   B SG    1 
ATOM   8295  N  N     . SER   B 1 293 ? 119.135 107.308 132.781 1.00 66.45  ?  293  SER   B N     1 
ATOM   8296  C  CA    . SER   B 1 293 ? 117.727 106.966 132.890 1.00 68.92  ?  293  SER   B CA    1 
ATOM   8297  C  C     . SER   B 1 293 ? 117.310 106.960 134.357 1.00 71.90  ?  293  SER   B C     1 
ATOM   8298  O  O     . SER   B 1 293 ? 118.141 106.995 135.267 1.00 75.82  ?  293  SER   B O     1 
ATOM   8299  C  CB    . SER   B 1 293 ? 117.447 105.606 132.242 1.00 70.58  ?  293  SER   B CB    1 
ATOM   8300  O  OG    . SER   B 1 293 ? 118.353 104.622 132.708 1.00 77.65  ?  293  SER   B OG    1 
ATOM   8301  N  N     . GLN   B 1 294 ? 115.998 106.921 134.584 1.00 65.92  ?  294  GLN   B N     1 
ATOM   8302  C  CA    . GLN   B 1 294 ? 115.458 106.940 135.942 1.00 65.95  ?  294  GLN   B CA    1 
ATOM   8303  C  C     . GLN   B 1 294 ? 115.457 105.515 136.487 1.00 70.63  ?  294  GLN   B C     1 
ATOM   8304  O  O     . GLN   B 1 294 ? 114.443 104.813 136.500 1.00 75.94  ?  294  GLN   B O     1 
ATOM   8305  C  CB    . GLN   B 1 294 ? 114.070 107.563 135.964 1.00 62.66  ?  294  GLN   B CB    1 
ATOM   8306  C  CG    . GLN   B 1 294 ? 114.064 108.996 136.465 1.00 64.34  ?  294  GLN   B CG    1 
ATOM   8307  C  CD    . GLN   B 1 294 ? 112.692 109.626 136.417 1.00 74.64  ?  294  GLN   B CD    1 
ATOM   8308  O  OE1   . GLN   B 1 294 ? 111.684 108.960 136.644 1.00 75.63  ?  294  GLN   B OE1   1 
ATOM   8309  N  NE2   . GLN   B 1 294 ? 112.644 110.913 136.098 1.00 74.01  ?  294  GLN   B NE2   1 
ATOM   8310  N  N     . GLY   B 1 295 ? 116.629 105.090 136.951 1.00 64.59  ?  295  GLY   B N     1 
ATOM   8311  C  CA    . GLY   B 1 295 ? 116.787 103.747 137.481 1.00 64.16  ?  295  GLY   B CA    1 
ATOM   8312  C  C     . GLY   B 1 295 ? 116.538 102.657 136.466 1.00 73.77  ?  295  GLY   B C     1 
ATOM   8313  O  O     . GLY   B 1 295 ? 116.056 101.578 136.829 1.00 77.95  ?  295  GLY   B O     1 
ATOM   8314  N  N     . GLY   B 1 296 ? 116.861 102.905 135.200 1.00 73.15  ?  296  GLY   B N     1 
ATOM   8315  C  CA    . GLY   B 1 296 ? 116.588 101.932 134.157 1.00 72.09  ?  296  GLY   B CA    1 
ATOM   8316  C  C     . GLY   B 1 296 ? 115.118 101.639 133.964 1.00 73.93  ?  296  GLY   B C     1 
ATOM   8317  O  O     . GLY   B 1 296 ? 114.757 100.504 133.637 1.00 79.14  ?  296  GLY   B O     1 
ATOM   8318  N  N     . VAL   B 1 297 ? 114.255 102.637 134.163 1.00 61.70  ?  297  VAL   B N     1 
ATOM   8319  C  CA    . VAL   B 1 297 ? 112.811 102.492 134.020 1.00 64.53  ?  297  VAL   B CA    1 
ATOM   8320  C  C     . VAL   B 1 297 ? 112.268 103.406 132.929 1.00 69.51  ?  297  VAL   B C     1 
ATOM   8321  O  O     . VAL   B 1 297 ? 111.467 102.983 132.089 1.00 73.97  ?  297  VAL   B O     1 
ATOM   8322  C  CB    . VAL   B 1 297 ? 112.085 102.748 135.359 1.00 67.56  ?  297  VAL   B CB    1 
ATOM   8323  C  CG1   . VAL   B 1 297 ? 110.594 102.514 135.200 1.00 63.48  ?  297  VAL   B CG1   1 
ATOM   8324  C  CG2   . VAL   B 1 297 ? 112.638 101.809 136.411 1.00 72.06  ?  297  VAL   B CG2   1 
ATOM   8325  N  N     . ARG   B 1 298 ? 112.696 104.663 132.925 1.00 69.75  ?  298  ARG   B N     1 
ATOM   8326  C  CA    . ARG   B 1 298 ? 112.237 105.634 131.943 1.00 66.89  ?  298  ARG   B CA    1 
ATOM   8327  C  C     . ARG   B 1 298 ? 113.258 106.758 131.868 1.00 68.60  ?  298  ARG   B C     1 
ATOM   8328  O  O     . ARG   B 1 298 ? 114.146 106.877 132.714 1.00 73.96  ?  298  ARG   B O     1 
ATOM   8329  C  CB    . ARG   B 1 298 ? 110.848 106.172 132.295 1.00 66.79  ?  298  ARG   B CB    1 
ATOM   8330  C  CG    . ARG   B 1 298 ? 110.649 106.458 133.772 1.00 61.91  ?  298  ARG   B CG    1 
ATOM   8331  C  CD    . ARG   B 1 298 ? 109.365 107.227 134.004 1.00 66.55  ?  298  ARG   B CD    1 
ATOM   8332  N  NE    . ARG   B 1 298 ? 109.212 107.646 135.392 1.00 67.47  ?  298  ARG   B NE    1 
ATOM   8333  C  CZ    . ARG   B 1 298 ? 108.089 107.534 136.087 1.00 66.86  ?  298  ARG   B CZ    1 
ATOM   8334  N  NH1   . ARG   B 1 298 ? 106.999 107.005 135.556 1.00 68.01  ?  298  ARG   B NH1   1 
ATOM   8335  N  NH2   . ARG   B 1 298 ? 108.060 107.960 137.346 1.00 66.17  ?  298  ARG   B NH2   1 
ATOM   8336  N  N     . GLY   B 1 299 ? 113.124 107.582 130.834 1.00 67.02  ?  299  GLY   B N     1 
ATOM   8337  C  CA    . GLY   B 1 299 ? 114.024 108.703 130.675 1.00 66.62  ?  299  GLY   B CA    1 
ATOM   8338  C  C     . GLY   B 1 299 ? 113.806 109.765 131.736 1.00 67.31  ?  299  GLY   B C     1 
ATOM   8339  O  O     . GLY   B 1 299 ? 112.696 109.983 132.221 1.00 72.35  ?  299  GLY   B O     1 
ATOM   8340  N  N     . GLY   B 1 300 ? 114.890 110.451 132.082 1.00 59.02  ?  300  GLY   B N     1 
ATOM   8341  C  CA    . GLY   B 1 300 ? 114.807 111.492 133.085 1.00 55.32  ?  300  GLY   B CA    1 
ATOM   8342  C  C     . GLY   B 1 300 ? 114.094 112.728 132.572 1.00 56.64  ?  300  GLY   B C     1 
ATOM   8343  O  O     . GLY   B 1 300 ? 114.066 113.014 131.375 1.00 59.89  ?  300  GLY   B O     1 
ATOM   8344  N  N     . ALA   B 1 301 ? 113.498 113.468 133.503 1.00 52.82  ?  301  ALA   B N     1 
ATOM   8345  C  CA    . ALA   B 1 301 ? 112.792 114.699 133.185 1.00 46.26  ?  301  ALA   B CA    1 
ATOM   8346  C  C     . ALA   B 1 301 ? 113.025 115.713 134.293 1.00 53.00  ?  301  ALA   B C     1 
ATOM   8347  O  O     . ALA   B 1 301 ? 113.185 115.351 135.461 1.00 63.66  ?  301  ALA   B O     1 
ATOM   8348  C  CB    . ALA   B 1 301 ? 111.290 114.455 132.999 1.00 48.90  ?  301  ALA   B CB    1 
ATOM   8349  N  N     . ALA   B 1 302 ? 113.043 116.990 133.916 1.00 58.15  ?  302  ALA   B N     1 
ATOM   8350  C  CA    . ALA   B 1 302 ? 113.278 118.059 134.873 1.00 47.26  ?  302  ALA   B CA    1 
ATOM   8351  C  C     . ALA   B 1 302 ? 112.498 119.296 134.456 1.00 50.35  ?  302  ALA   B C     1 
ATOM   8352  O  O     . ALA   B 1 302 ? 112.125 119.460 133.292 1.00 60.15  ?  302  ALA   B O     1 
ATOM   8353  C  CB    . ALA   B 1 302 ? 114.768 118.388 134.997 1.00 46.23  ?  302  ALA   B CB    1 
ATOM   8354  N  N     . THR   B 1 303 ? 112.251 120.165 135.435 1.00 50.22  ?  303  THR   B N     1 
ATOM   8355  C  CA    . THR   B 1 303 ? 111.559 121.429 135.212 1.00 48.55  ?  303  THR   B CA    1 
ATOM   8356  C  C     . THR   B 1 303 ? 112.398 122.572 135.761 1.00 48.00  ?  303  THR   B C     1 
ATOM   8357  O  O     . THR   B 1 303 ? 112.836 122.523 136.913 1.00 60.89  ?  303  THR   B O     1 
ATOM   8358  C  CB    . THR   B 1 303 ? 110.173 121.443 135.868 1.00 54.97  ?  303  THR   B CB    1 
ATOM   8359  O  OG1   . THR   B 1 303 ? 109.396 120.354 135.362 1.00 67.22  ?  303  THR   B OG1   1 
ATOM   8360  C  CG2   . THR   B 1 303 ? 109.457 122.746 135.545 1.00 50.03  ?  303  THR   B CG2   1 
ATOM   8361  N  N     . LEU   B 1 304 ? 112.598 123.605 134.948 1.00 49.48  ?  304  LEU   B N     1 
ATOM   8362  C  CA    . LEU   B 1 304 ? 113.358 124.783 135.339 1.00 41.53  ?  304  LEU   B CA    1 
ATOM   8363  C  C     . LEU   B 1 304 ? 112.414 125.896 135.776 1.00 53.57  ?  304  LEU   B C     1 
ATOM   8364  O  O     . LEU   B 1 304 ? 111.365 126.110 135.164 1.00 66.53  ?  304  LEU   B O     1 
ATOM   8365  C  CB    . LEU   B 1 304 ? 114.234 125.273 134.187 1.00 56.33  ?  304  LEU   B CB    1 
ATOM   8366  C  CG    . LEU   B 1 304 ? 115.647 124.701 134.097 1.00 59.08  ?  304  LEU   B CG    1 
ATOM   8367  C  CD1   . LEU   B 1 304 ? 116.347 125.254 132.879 1.00 65.52  ?  304  LEU   B CD1   1 
ATOM   8368  C  CD2   . LEU   B 1 304 ? 116.434 125.024 135.350 1.00 57.31  ?  304  LEU   B CD2   1 
ATOM   8369  N  N     . PHE   B 1 305 ? 112.794 126.603 136.836 1.00 55.20  ?  305  PHE   B N     1 
ATOM   8370  C  CA    . PHE   B 1 305 ? 111.988 127.682 137.387 1.00 39.76  ?  305  PHE   B CA    1 
ATOM   8371  C  C     . PHE   B 1 305 ? 112.773 128.984 137.371 1.00 49.86  ?  305  PHE   B C     1 
ATOM   8372  O  O     . PHE   B 1 305 ? 113.966 129.005 137.689 1.00 68.77  ?  305  PHE   B O     1 
ATOM   8373  C  CB    . PHE   B 1 305 ? 111.542 127.362 138.816 1.00 38.17  ?  305  PHE   B CB    1 
ATOM   8374  C  CG    . PHE   B 1 305 ? 110.548 126.245 138.900 1.00 47.11  ?  305  PHE   B CG    1 
ATOM   8375  C  CD1   . PHE   B 1 305 ? 110.970 124.928 138.937 1.00 45.45  ?  305  PHE   B CD1   1 
ATOM   8376  C  CD2   . PHE   B 1 305 ? 109.191 126.509 138.930 1.00 46.61  ?  305  PHE   B CD2   1 
ATOM   8377  C  CE1   . PHE   B 1 305 ? 110.058 123.898 139.007 1.00 50.87  ?  305  PHE   B CE1   1 
ATOM   8378  C  CE2   . PHE   B 1 305 ? 108.276 125.482 139.001 1.00 44.84  ?  305  PHE   B CE2   1 
ATOM   8379  C  CZ    . PHE   B 1 305 ? 108.710 124.175 139.038 1.00 49.97  ?  305  PHE   B CZ    1 
ATOM   8380  N  N     . TYR   B 1 306 ? 112.097 130.068 137.000 1.00 45.32  ?  306  TYR   B N     1 
ATOM   8381  C  CA    . TYR   B 1 306 ? 112.689 131.397 136.999 1.00 47.15  ?  306  TYR   B CA    1 
ATOM   8382  C  C     . TYR   B 1 306 ? 111.585 132.418 137.211 1.00 41.93  ?  306  TYR   B C     1 
ATOM   8383  O  O     . TYR   B 1 306 ? 110.437 132.173 136.822 1.00 50.74  ?  306  TYR   B O     1 
ATOM   8384  C  CB    . TYR   B 1 306 ? 113.438 131.688 135.690 1.00 47.57  ?  306  TYR   B CB    1 
ATOM   8385  C  CG    . TYR   B 1 306 ? 112.624 131.449 134.438 1.00 47.18  ?  306  TYR   B CG    1 
ATOM   8386  C  CD1   . TYR   B 1 306 ? 111.824 132.450 133.904 1.00 48.86  ?  306  TYR   B CD1   1 
ATOM   8387  C  CD2   . TYR   B 1 306 ? 112.660 130.225 133.786 1.00 45.61  ?  306  TYR   B CD2   1 
ATOM   8388  C  CE1   . TYR   B 1 306 ? 111.080 132.236 132.759 1.00 51.31  ?  306  TYR   B CE1   1 
ATOM   8389  C  CE2   . TYR   B 1 306 ? 111.920 130.002 132.642 1.00 50.52  ?  306  TYR   B CE2   1 
ATOM   8390  C  CZ    . TYR   B 1 306 ? 111.133 131.011 132.133 1.00 56.66  ?  306  TYR   B CZ    1 
ATOM   8391  O  OH    . TYR   B 1 306 ? 110.395 130.795 130.993 1.00 60.37  ?  306  TYR   B OH    1 
ATOM   8392  N  N     . PRO   B 1 307 ? 111.888 133.553 137.833 1.00 50.79  ?  307  PRO   B N     1 
ATOM   8393  C  CA    . PRO   B 1 307 ? 110.872 134.595 138.004 1.00 48.18  ?  307  PRO   B CA    1 
ATOM   8394  C  C     . PRO   B 1 307 ? 110.524 135.264 136.683 1.00 50.47  ?  307  PRO   B C     1 
ATOM   8395  O  O     . PRO   B 1 307 ? 111.289 135.242 135.717 1.00 65.88  ?  307  PRO   B O     1 
ATOM   8396  C  CB    . PRO   B 1 307 ? 111.550 135.578 138.960 1.00 46.61  ?  307  PRO   B CB    1 
ATOM   8397  C  CG    . PRO   B 1 307 ? 112.991 135.425 138.611 1.00 55.93  ?  307  PRO   B CG    1 
ATOM   8398  C  CD    . PRO   B 1 307 ? 113.147 133.936 138.491 1.00 53.25  ?  307  PRO   B CD    1 
ATOM   8399  N  N     . MET   B 1 308 ? 109.334 135.869 136.653 1.00 62.06  ?  308  MET   B N     1 
ATOM   8400  C  CA    . MET   B 1 308 ? 108.883 136.544 135.441 1.00 63.96  ?  308  MET   B CA    1 
ATOM   8401  C  C     . MET   B 1 308 ? 109.676 137.815 135.169 1.00 65.51  ?  308  MET   B C     1 
ATOM   8402  O  O     . MET   B 1 308 ? 109.856 138.191 134.006 1.00 74.11  ?  308  MET   B O     1 
ATOM   8403  C  CB    . MET   B 1 308 ? 107.392 136.865 135.538 1.00 63.42  ?  308  MET   B CB    1 
ATOM   8404  C  CG    . MET   B 1 308 ? 106.726 137.074 134.190 1.00 64.78  ?  308  MET   B CG    1 
ATOM   8405  S  SD    . MET   B 1 308 ? 104.991 137.537 134.318 1.00 91.12  ?  308  MET   B SD    1 
ATOM   8406  C  CE    . MET   B 1 308 ? 104.380 136.991 132.727 1.00 71.78  ?  308  MET   B CE    1 
ATOM   8407  N  N     . TRP   B 1 309 ? 110.154 138.488 136.214 1.00 55.93  ?  309  TRP   B N     1 
ATOM   8408  C  CA    . TRP   B 1 309 ? 110.892 139.734 136.057 1.00 49.30  ?  309  TRP   B CA    1 
ATOM   8409  C  C     . TRP   B 1 309 ? 112.369 139.520 135.753 1.00 53.18  ?  309  TRP   B C     1 
ATOM   8410  O  O     . TRP   B 1 309 ? 113.155 140.463 135.891 1.00 61.23  ?  309  TRP   B O     1 
ATOM   8411  C  CB    . TRP   B 1 309 ? 110.740 140.604 137.307 1.00 51.65  ?  309  TRP   B CB    1 
ATOM   8412  C  CG    . TRP   B 1 309 ? 110.979 139.872 138.585 1.00 53.24  ?  309  TRP   B CG    1 
ATOM   8413  C  CD1   . TRP   B 1 309 ? 110.048 139.242 139.353 1.00 53.42  ?  309  TRP   B CD1   1 
ATOM   8414  C  CD2   . TRP   B 1 309 ? 112.235 139.695 139.249 1.00 54.19  ?  309  TRP   B CD2   1 
ATOM   8415  N  NE1   . TRP   B 1 309 ? 110.645 138.682 140.455 1.00 54.89  ?  309  TRP   B NE1   1 
ATOM   8416  C  CE2   . TRP   B 1 309 ? 111.988 138.945 140.414 1.00 53.77  ?  309  TRP   B CE2   1 
ATOM   8417  C  CE3   . TRP   B 1 309 ? 113.545 140.096 138.971 1.00 52.48  ?  309  TRP   B CE3   1 
ATOM   8418  C  CZ2   . TRP   B 1 309 ? 113.000 138.591 141.300 1.00 53.04  ?  309  TRP   B CZ2   1 
ATOM   8419  C  CZ3   . TRP   B 1 309 ? 114.547 139.743 139.851 1.00 52.35  ?  309  TRP   B CZ3   1 
ATOM   8420  C  CH2   . TRP   B 1 309 ? 114.271 138.993 140.998 1.00 54.59  ?  309  TRP   B CH2   1 
ATOM   8421  N  N     . HIS   B 1 310 ? 112.768 138.316 135.355 1.00 59.53  ?  310  HIS   B N     1 
ATOM   8422  C  CA    . HIS   B 1 310 ? 114.153 138.081 134.973 1.00 50.43  ?  310  HIS   B CA    1 
ATOM   8423  C  C     . HIS   B 1 310 ? 114.485 138.849 133.700 1.00 55.66  ?  310  HIS   B C     1 
ATOM   8424  O  O     . HIS   B 1 310 ? 113.644 139.001 132.811 1.00 71.32  ?  310  HIS   B O     1 
ATOM   8425  C  CB    . HIS   B 1 310 ? 114.405 136.587 134.774 1.00 53.88  ?  310  HIS   B CB    1 
ATOM   8426  C  CG    . HIS   B 1 310 ? 115.836 136.186 134.956 1.00 60.26  ?  310  HIS   B CG    1 
ATOM   8427  N  ND1   . HIS   B 1 310 ? 116.800 136.417 134.000 1.00 66.37  ?  310  HIS   B ND1   1 
ATOM   8428  C  CD2   . HIS   B 1 310 ? 116.466 135.572 135.985 1.00 62.17  ?  310  HIS   B CD2   1 
ATOM   8429  C  CE1   . HIS   B 1 310 ? 117.962 135.962 134.431 1.00 65.56  ?  310  HIS   B CE1   1 
ATOM   8430  N  NE2   . HIS   B 1 310 ? 117.788 135.447 135.634 1.00 66.19  ?  310  HIS   B NE2   1 
ATOM   8431  N  N     . LEU   B 1 311 ? 115.725 139.338 133.617 1.00 58.27  ?  311  LEU   B N     1 
ATOM   8432  C  CA    . LEU   B 1 311 ? 116.134 140.153 132.478 1.00 62.04  ?  311  LEU   B CA    1 
ATOM   8433  C  C     . LEU   B 1 311 ? 116.120 139.377 131.169 1.00 66.73  ?  311  LEU   B C     1 
ATOM   8434  O  O     . LEU   B 1 311 ? 116.012 139.989 130.101 1.00 73.83  ?  311  LEU   B O     1 
ATOM   8435  C  CB    . LEU   B 1 311 ? 117.528 140.738 132.710 1.00 64.91  ?  311  LEU   B CB    1 
ATOM   8436  C  CG    . LEU   B 1 311 ? 117.960 141.914 131.832 1.00 63.81  ?  311  LEU   B CG    1 
ATOM   8437  C  CD1   . LEU   B 1 311 ? 117.009 143.070 132.030 1.00 61.63  ?  311  LEU   B CD1   1 
ATOM   8438  C  CD2   . LEU   B 1 311 ? 119.356 142.327 132.257 1.00 66.42  ?  311  LEU   B CD2   1 
ATOM   8439  N  N     . GLU   B 1 312 ? 116.221 138.049 131.223 1.00 74.52  ?  312  GLU   B N     1 
ATOM   8440  C  CA    . GLU   B 1 312 ? 116.235 137.212 130.031 1.00 74.27  ?  312  GLU   B CA    1 
ATOM   8441  C  C     . GLU   B 1 312 ? 114.921 136.469 129.826 1.00 77.23  ?  312  GLU   B C     1 
ATOM   8442  O  O     . GLU   B 1 312 ? 114.892 135.467 129.107 1.00 83.53  ?  312  GLU   B O     1 
ATOM   8443  C  CB    . GLU   B 1 312 ? 117.389 136.212 130.102 1.00 76.91  ?  312  GLU   B CB    1 
ATOM   8444  C  CG    . GLU   B 1 312 ? 118.747 136.790 129.788 1.00 79.30  ?  312  GLU   B CG    1 
ATOM   8445  C  CD    . GLU   B 1 312 ? 119.823 135.728 129.715 1.00 88.42  ?  312  GLU   B CD    1 
ATOM   8446  O  OE1   . GLU   B 1 312 ? 120.209 135.199 130.778 1.00 89.26  ?  312  GLU   B OE1   1 
ATOM   8447  O  OE2   . GLU   B 1 312 ? 120.322 135.461 128.603 1.00 89.22  ?  312  GLU   B OE2   1 
ATOM   8448  N  N     . VAL   B 1 313 ? 113.830 136.949 130.430 1.00 68.14  ?  313  VAL   B N     1 
ATOM   8449  C  CA    . VAL   B 1 313 ? 112.586 136.182 130.445 1.00 66.70  ?  313  VAL   B CA    1 
ATOM   8450  C  C     . VAL   B 1 313 ? 112.056 135.970 129.033 1.00 71.50  ?  313  VAL   B C     1 
ATOM   8451  O  O     . VAL   B 1 313 ? 111.491 134.914 128.727 1.00 77.76  ?  313  VAL   B O     1 
ATOM   8452  C  CB    . VAL   B 1 313 ? 111.543 136.869 131.352 1.00 60.90  ?  313  VAL   B CB    1 
ATOM   8453  C  CG1   . VAL   B 1 313 ? 111.112 138.208 130.779 1.00 59.43  ?  313  VAL   B CG1   1 
ATOM   8454  C  CG2   . VAL   B 1 313 ? 110.341 135.963 131.564 1.00 60.18  ?  313  VAL   B CG2   1 
ATOM   8455  N  N     . GLU   B 1 314 ? 112.242 136.951 128.148 1.00 77.19  ?  314  GLU   B N     1 
ATOM   8456  C  CA    . GLU   B 1 314 ? 111.766 136.802 126.779 1.00 76.13  ?  314  GLU   B CA    1 
ATOM   8457  C  C     . GLU   B 1 314 ? 112.522 135.709 126.035 1.00 79.60  ?  314  GLU   B C     1 
ATOM   8458  O  O     . GLU   B 1 314 ? 111.944 135.029 125.182 1.00 82.63  ?  314  GLU   B O     1 
ATOM   8459  C  CB    . GLU   B 1 314 ? 111.877 138.132 126.038 1.00 74.72  ?  314  GLU   B CB    1 
ATOM   8460  C  CG    . GLU   B 1 314 ? 111.159 139.271 126.718 1.00 78.63  ?  314  GLU   B CG    1 
ATOM   8461  C  CD    . GLU   B 1 314 ? 111.626 140.629 126.245 1.00 88.89  ?  314  GLU   B CD    1 
ATOM   8462  O  OE1   . GLU   B 1 314 ? 112.650 141.119 126.763 1.00 91.12  ?  314  GLU   B OE1   1 
ATOM   8463  O  OE2   . GLU   B 1 314 ? 110.913 141.246 125.429 1.00 85.38  ?  314  GLU   B OE2   1 
ATOM   8464  N  N     . SER   B 1 315 ? 113.809 135.523 126.336 1.00 74.79  ?  315  SER   B N     1 
ATOM   8465  C  CA    . SER   B 1 315 ? 114.554 134.420 125.745 1.00 69.84  ?  315  SER   B CA    1 
ATOM   8466  C  C     . SER   B 1 315 ? 114.179 133.100 126.387 1.00 67.76  ?  315  SER   B C     1 
ATOM   8467  O  O     . SER   B 1 315 ? 114.082 132.086 125.694 1.00 74.92  ?  315  SER   B O     1 
ATOM   8468  C  CB    . SER   B 1 315 ? 116.040 134.669 125.868 1.00 70.88  ?  315  SER   B CB    1 
ATOM   8469  O  OG    . SER   B 1 315 ? 116.448 135.644 124.930 1.00 81.36  ?  315  SER   B OG    1 
ATOM   8470  N  N     . LEU   B 1 316 ? 113.963 133.094 127.709 1.00 55.33  ?  316  LEU   B N     1 
ATOM   8471  C  CA    . LEU   B 1 316 ? 113.649 131.848 128.396 1.00 57.28  ?  316  LEU   B CA    1 
ATOM   8472  C  C     . LEU   B 1 316 ? 112.250 131.351 128.059 1.00 63.55  ?  316  LEU   B C     1 
ATOM   8473  O  O     . LEU   B 1 316 ? 112.001 130.141 128.091 1.00 76.29  ?  316  LEU   B O     1 
ATOM   8474  C  CB    . LEU   B 1 316 ? 113.794 132.025 129.908 1.00 57.56  ?  316  LEU   B CB    1 
ATOM   8475  C  CG    . LEU   B 1 316 ? 115.100 132.629 130.423 1.00 58.88  ?  316  LEU   B CG    1 
ATOM   8476  C  CD1   . LEU   B 1 316 ? 115.068 132.768 131.936 1.00 57.38  ?  316  LEU   B CD1   1 
ATOM   8477  C  CD2   . LEU   B 1 316 ? 116.296 131.805 129.984 1.00 63.53  ?  316  LEU   B CD2   1 
ATOM   8478  N  N     . LEU   B 1 317 ? 111.327 132.262 127.740 1.00 49.17  ?  317  LEU   B N     1 
ATOM   8479  C  CA    . LEU   B 1 317 ? 109.955 131.859 127.447 1.00 54.63  ?  317  LEU   B CA    1 
ATOM   8480  C  C     . LEU   B 1 317 ? 109.873 131.025 126.174 1.00 61.28  ?  317  LEU   B C     1 
ATOM   8481  O  O     . LEU   B 1 317 ? 109.056 130.102 126.086 1.00 67.95  ?  317  LEU   B O     1 
ATOM   8482  C  CB    . LEU   B 1 317 ? 109.058 133.088 127.327 1.00 53.50  ?  317  LEU   B CB    1 
ATOM   8483  C  CG    . LEU   B 1 317 ? 108.556 133.684 128.641 1.00 51.81  ?  317  LEU   B CG    1 
ATOM   8484  C  CD1   . LEU   B 1 317 ? 107.548 134.794 128.423 1.00 56.34  ?  317  LEU   B CD1   1 
ATOM   8485  C  CD2   . LEU   B 1 317 ? 107.974 132.615 129.550 1.00 52.82  ?  317  LEU   B CD2   1 
ATOM   8486  N  N     . VAL   B 1 318 ? 110.703 131.335 125.180 1.00 56.78  ?  318  VAL   B N     1 
ATOM   8487  C  CA    . VAL   B 1 318 ? 110.641 130.664 123.886 1.00 52.35  ?  318  VAL   B CA    1 
ATOM   8488  C  C     . VAL   B 1 318 ? 111.627 129.503 123.802 1.00 59.94  ?  318  VAL   B C     1 
ATOM   8489  O  O     . VAL   B 1 318 ? 111.880 128.983 122.713 1.00 73.34  ?  318  VAL   B O     1 
ATOM   8490  C  CB    . VAL   B 1 318 ? 110.886 131.662 122.740 1.00 52.61  ?  318  VAL   B CB    1 
ATOM   8491  C  CG1   . VAL   B 1 318 ? 109.889 132.803 122.810 1.00 59.01  ?  318  VAL   B CG1   1 
ATOM   8492  C  CG2   . VAL   B 1 318 ? 112.310 132.187 122.787 1.00 55.63  ?  318  VAL   B CG2   1 
ATOM   8493  N  N     . LEU   B 1 319 ? 112.179 129.075 124.940 1.00 54.99  ?  319  LEU   B N     1 
ATOM   8494  C  CA    . LEU   B 1 319 ? 113.194 128.025 124.926 1.00 48.76  ?  319  LEU   B CA    1 
ATOM   8495  C  C     . LEU   B 1 319 ? 112.640 126.666 124.518 1.00 52.44  ?  319  LEU   B C     1 
ATOM   8496  O  O     . LEU   B 1 319 ? 113.419 125.778 124.158 1.00 60.74  ?  319  LEU   B O     1 
ATOM   8497  C  CB    . LEU   B 1 319 ? 113.851 127.908 126.302 1.00 43.06  ?  319  LEU   B CB    1 
ATOM   8498  C  CG    . LEU   B 1 319 ? 115.005 128.861 126.603 1.00 44.67  ?  319  LEU   B CG    1 
ATOM   8499  C  CD1   . LEU   B 1 319 ? 115.590 128.583 127.976 1.00 50.23  ?  319  LEU   B CD1   1 
ATOM   8500  C  CD2   . LEU   B 1 319 ? 116.078 128.764 125.534 1.00 51.96  ?  319  LEU   B CD2   1 
ATOM   8501  N  N     . LYS   B 1 320 ? 111.321 126.483 124.555 1.00 55.06  ?  320  LYS   B N     1 
ATOM   8502  C  CA    . LYS   B 1 320 ? 110.729 125.168 124.360 1.00 50.22  ?  320  LYS   B CA    1 
ATOM   8503  C  C     . LYS   B 1 320 ? 110.110 124.961 122.984 1.00 61.00  ?  320  LYS   B C     1 
ATOM   8504  O  O     . LYS   B 1 320 ? 110.000 123.811 122.545 1.00 70.43  ?  320  LYS   B O     1 
ATOM   8505  C  CB    . LYS   B 1 320 ? 109.662 124.912 125.431 1.00 54.46  ?  320  LYS   B CB    1 
ATOM   8506  C  CG    . LYS   B 1 320 ? 109.208 123.469 125.518 1.00 52.29  ?  320  LYS   B CG    1 
ATOM   8507  C  CD    . LYS   B 1 320 ? 109.206 122.971 126.943 1.00 62.31  ?  320  LYS   B CD    1 
ATOM   8508  C  CE    . LYS   B 1 320 ? 109.016 121.472 126.982 1.00 56.93  ?  320  LYS   B CE    1 
ATOM   8509  N  NZ    . LYS   B 1 320 ? 109.645 120.805 125.814 1.00 53.56  ?  320  LYS   B NZ    1 
ATOM   8510  N  N     . ASN   B 1 321 ? 109.718 126.025 122.287 1.00 56.50  ?  321  ASN   B N     1 
ATOM   8511  C  CA    . ASN   B 1 321 ? 108.966 125.845 121.054 1.00 56.32  ?  321  ASN   B CA    1 
ATOM   8512  C  C     . ASN   B 1 321 ? 109.858 125.283 119.947 1.00 57.36  ?  321  ASN   B C     1 
ATOM   8513  O  O     . ASN   B 1 321 ? 111.089 125.280 120.035 1.00 65.56  ?  321  ASN   B O     1 
ATOM   8514  C  CB    . ASN   B 1 321 ? 108.310 127.159 120.618 1.00 53.77  ?  321  ASN   B CB    1 
ATOM   8515  C  CG    . ASN   B 1 321 ? 109.306 128.281 120.402 1.00 59.57  ?  321  ASN   B CG    1 
ATOM   8516  O  OD1   . ASN   B 1 321 ? 110.327 128.111 119.738 1.00 62.46  ?  321  ASN   B OD1   1 
ATOM   8517  N  ND2   . ASN   B 1 321 ? 109.002 129.446 120.957 1.00 67.66  ?  321  ASN   B ND2   1 
ATOM   8518  N  N     . ASN   B 1 322 ? 109.207 124.798 118.888 1.00 59.42  ?  322  ASN   B N     1 
ATOM   8519  C  CA    . ASN   B 1 322 ? 109.882 124.166 117.761 1.00 62.63  ?  322  ASN   B CA    1 
ATOM   8520  C  C     . ASN   B 1 322 ? 110.249 125.157 116.664 1.00 62.22  ?  322  ASN   B C     1 
ATOM   8521  O  O     . ASN   B 1 322 ? 110.347 124.769 115.494 1.00 71.49  ?  322  ASN   B O     1 
ATOM   8522  C  CB    . ASN   B 1 322 ? 109.009 123.045 117.194 1.00 62.77  ?  322  ASN   B CB    1 
ATOM   8523  C  CG    . ASN   B 1 322 ? 107.564 123.470 117.000 1.00 63.63  ?  322  ASN   B CG    1 
ATOM   8524  O  OD1   . ASN   B 1 322 ? 107.264 124.656 116.878 1.00 63.43  ?  322  ASN   B OD1   1 
ATOM   8525  N  ND2   . ASN   B 1 322 ? 106.662 122.499 116.969 1.00 63.96  ?  322  ASN   B ND2   1 
ATOM   8526  N  N     . ARG   B 1 323 ? 110.458 126.426 117.008 1.00 54.99  ?  323  ARG   B N     1 
ATOM   8527  C  CA    . ARG   B 1 323 ? 110.746 127.447 116.011 1.00 61.79  ?  323  ARG   B CA    1 
ATOM   8528  C  C     . ARG   B 1 323 ? 112.043 128.174 116.329 1.00 68.47  ?  323  ARG   B C     1 
ATOM   8529  O  O     . ARG   B 1 323 ? 112.083 129.408 116.338 1.00 81.20  ?  323  ARG   B O     1 
ATOM   8530  C  CB    . ARG   B 1 323 ? 109.598 128.452 115.918 1.00 63.18  ?  323  ARG   B CB    1 
ATOM   8531  C  CG    . ARG   B 1 323 ? 108.482 128.041 114.984 1.00 58.22  ?  323  ARG   B CG    1 
ATOM   8532  C  CD    . ARG   B 1 323 ? 107.144 128.468 115.542 1.00 62.97  ?  323  ARG   B CD    1 
ATOM   8533  N  NE    . ARG   B 1 323 ? 106.700 127.583 116.611 1.00 68.98  ?  323  ARG   B NE    1 
ATOM   8534  C  CZ    . ARG   B 1 323 ? 106.096 127.992 117.717 1.00 70.35  ?  323  ARG   B CZ    1 
ATOM   8535  N  NH1   . ARG   B 1 323 ? 105.859 129.273 117.940 1.00 67.75  ?  323  ARG   B NH1   1 
ATOM   8536  N  NH2   . ARG   B 1 323 ? 105.712 127.092 118.617 1.00 70.08  ?  323  ARG   B NH2   1 
ATOM   8537  N  N     . GLY   B 1 324 ? 113.102 127.426 116.610 1.00 46.50  ?  324  GLY   B N     1 
ATOM   8538  C  CA    . GLY   B 1 324 ? 114.394 128.034 116.848 1.00 51.82  ?  324  GLY   B CA    1 
ATOM   8539  C  C     . GLY   B 1 324 ? 115.532 127.224 116.270 1.00 57.55  ?  324  GLY   B C     1 
ATOM   8540  O  O     . GLY   B 1 324 ? 115.316 126.376 115.401 1.00 67.35  ?  324  GLY   B O     1 
ATOM   8541  N  N     . VAL   B 1 325 ? 116.751 127.482 116.736 1.00 68.31  ?  325  VAL   B N     1 
ATOM   8542  C  CA    . VAL   B 1 325 ? 117.915 126.695 116.349 1.00 69.52  ?  325  VAL   B CA    1 
ATOM   8543  C  C     . VAL   B 1 325 ? 118.493 126.079 117.614 1.00 75.16  ?  325  VAL   B C     1 
ATOM   8544  O  O     . VAL   B 1 325 ? 117.966 126.283 118.713 1.00 81.20  ?  325  VAL   B O     1 
ATOM   8545  C  CB    . VAL   B 1 325 ? 118.958 127.544 115.604 1.00 69.80  ?  325  VAL   B CB    1 
ATOM   8546  C  CG1   . VAL   B 1 325 ? 118.403 127.972 114.254 1.00 68.24  ?  325  VAL   B CG1   1 
ATOM   8547  C  CG2   . VAL   B 1 325 ? 119.318 128.752 116.438 1.00 70.73  ?  325  VAL   B CG2   1 
ATOM   8548  N  N     . GLU   B 1 326 ? 119.574 125.316 117.470 1.00 91.52  ?  326  GLU   B N     1 
ATOM   8549  C  CA    . GLU   B 1 326 ? 120.167 124.662 118.625 1.00 89.26  ?  326  GLU   B CA    1 
ATOM   8550  C  C     . GLU   B 1 326 ? 120.820 125.641 119.589 1.00 86.92  ?  326  GLU   B C     1 
ATOM   8551  O  O     . GLU   B 1 326 ? 120.981 125.313 120.769 1.00 92.33  ?  326  GLU   B O     1 
ATOM   8552  C  CB    . GLU   B 1 326 ? 121.185 123.612 118.174 1.00 94.96  ?  326  GLU   B CB    1 
ATOM   8553  C  CG    . GLU   B 1 326 ? 120.593 122.299 117.640 1.00 98.35  ?  326  GLU   B CG    1 
ATOM   8554  C  CD    . GLU   B 1 326 ? 119.226 121.947 118.228 1.00 105.68 ?  326  GLU   B CD    1 
ATOM   8555  O  OE1   . GLU   B 1 326 ? 118.993 122.255 119.414 1.00 104.93 ?  326  GLU   B OE1   1 
ATOM   8556  O  OE2   . GLU   B 1 326 ? 118.386 121.353 117.513 1.00 104.13 ?  326  GLU   B OE2   1 
ATOM   8557  N  N     . GLY   B 1 327 ? 121.192 126.832 119.123 1.00 66.85  ?  327  GLY   B N     1 
ATOM   8558  C  CA    . GLY   B 1 327 ? 121.867 127.785 119.983 1.00 70.74  ?  327  GLY   B CA    1 
ATOM   8559  C  C     . GLY   B 1 327 ? 120.966 128.629 120.855 1.00 72.68  ?  327  GLY   B C     1 
ATOM   8560  O  O     . GLY   B 1 327 ? 121.473 129.382 121.691 1.00 78.63  ?  327  GLY   B O     1 
ATOM   8561  N  N     . ASN   B 1 328 ? 119.645 128.554 120.666 1.00 62.27  ?  328  ASN   B N     1 
ATOM   8562  C  CA    . ASN   B 1 328 ? 118.731 129.344 121.482 1.00 56.80  ?  328  ASN   B CA    1 
ATOM   8563  C  C     . ASN   B 1 328 ? 117.514 128.540 121.926 1.00 58.58  ?  328  ASN   B C     1 
ATOM   8564  O  O     . ASN   B 1 328 ? 116.483 129.132 122.266 1.00 58.57  ?  328  ASN   B O     1 
ATOM   8565  C  CB    . ASN   B 1 328 ? 118.273 130.603 120.733 1.00 55.14  ?  328  ASN   B CB    1 
ATOM   8566  C  CG    . ASN   B 1 328 ? 117.539 130.286 119.444 1.00 57.90  ?  328  ASN   B CG    1 
ATOM   8567  O  OD1   . ASN   B 1 328 ? 117.471 129.135 119.018 1.00 66.90  ?  328  ASN   B OD1   1 
ATOM   8568  N  ND2   . ASN   B 1 328 ? 116.997 131.315 118.807 1.00 57.67  ?  328  ASN   B ND2   1 
ATOM   8569  N  N     . ARG   B 1 329 ? 117.601 127.212 121.926 1.00 54.30  ?  329  ARG   B N     1 
ATOM   8570  C  CA    . ARG   B 1 329 ? 116.482 126.364 122.305 1.00 47.37  ?  329  ARG   B CA    1 
ATOM   8571  C  C     . ARG   B 1 329 ? 116.969 125.237 123.200 1.00 53.64  ?  329  ARG   B C     1 
ATOM   8572  O  O     . ARG   B 1 329 ? 118.000 124.616 122.931 1.00 60.55  ?  329  ARG   B O     1 
ATOM   8573  C  CB    . ARG   B 1 329 ? 115.779 125.778 121.074 1.00 48.04  ?  329  ARG   B CB    1 
ATOM   8574  C  CG    . ARG   B 1 329 ? 115.023 126.798 120.246 1.00 47.72  ?  329  ARG   B CG    1 
ATOM   8575  C  CD    . ARG   B 1 329 ? 113.708 127.165 120.901 1.00 51.47  ?  329  ARG   B CD    1 
ATOM   8576  N  NE    . ARG   B 1 329 ? 112.916 128.068 120.075 1.00 52.84  ?  329  ARG   B NE    1 
ATOM   8577  C  CZ    . ARG   B 1 329 ? 113.135 129.370 119.962 1.00 46.12  ?  329  ARG   B CZ    1 
ATOM   8578  N  NH1   . ARG   B 1 329 ? 114.120 129.966 120.614 1.00 52.45  ?  329  ARG   B NH1   1 
ATOM   8579  N  NH2   . ARG   B 1 329 ? 112.345 130.095 119.175 1.00 44.90  ?  329  ARG   B NH2   1 
ATOM   8580  N  N     . VAL   B 1 330 ? 116.223 124.989 124.272 1.00 50.43  ?  330  VAL   B N     1 
ATOM   8581  C  CA    . VAL   B 1 330 ? 116.422 123.823 125.133 1.00 45.05  ?  330  VAL   B CA    1 
ATOM   8582  C  C     . VAL   B 1 330 ? 115.047 123.172 125.258 1.00 44.52  ?  330  VAL   B C     1 
ATOM   8583  O  O     . VAL   B 1 330 ? 114.260 123.510 126.148 1.00 54.93  ?  330  VAL   B O     1 
ATOM   8584  C  CB    . VAL   B 1 330 ? 116.999 124.191 126.504 1.00 40.59  ?  330  VAL   B CB    1 
ATOM   8585  C  CG1   . VAL   B 1 330 ? 117.190 122.952 127.362 1.00 43.46  ?  330  VAL   B CG1   1 
ATOM   8586  C  CG2   . VAL   B 1 330 ? 118.308 124.952 126.352 1.00 44.07  ?  330  VAL   B CG2   1 
ATOM   8587  N  N     . ARG   B 1 331 ? 114.746 122.233 124.362 1.00 52.76  ?  331  ARG   B N     1 
ATOM   8588  C  CA    . ARG   B 1 331 ? 113.384 121.744 124.177 1.00 56.81  ?  331  ARG   B CA    1 
ATOM   8589  C  C     . ARG   B 1 331 ? 113.064 120.512 124.991 1.00 54.97  ?  331  ARG   B C     1 
ATOM   8590  O  O     . ARG   B 1 331 ? 111.905 120.077 125.017 1.00 69.20  ?  331  ARG   B O     1 
ATOM   8591  C  CB    . ARG   B 1 331 ? 113.125 121.440 122.703 1.00 57.08  ?  331  ARG   B CB    1 
ATOM   8592  C  CG    . ARG   B 1 331 ? 113.399 122.591 121.758 1.00 52.76  ?  331  ARG   B CG    1 
ATOM   8593  C  CD    . ARG   B 1 331 ? 112.887 122.257 120.368 1.00 54.20  ?  331  ARG   B CD    1 
ATOM   8594  N  NE    . ARG   B 1 331 ? 113.241 123.272 119.385 1.00 57.88  ?  331  ARG   B NE    1 
ATOM   8595  C  CZ    . ARG   B 1 331 ? 114.350 123.254 118.659 1.00 60.62  ?  331  ARG   B CZ    1 
ATOM   8596  N  NH1   . ARG   B 1 331 ? 115.241 122.284 118.783 1.00 54.66  ?  331  ARG   B NH1   1 
ATOM   8597  N  NH2   . ARG   B 1 331 ? 114.570 124.232 117.786 1.00 58.75  ?  331  ARG   B NH2   1 
ATOM   8598  N  N     . HIS   B 1 332 ? 114.037 119.976 125.700 1.00 67.06  ?  332  HIS   B N     1 
ATOM   8599  C  CA    . HIS   B 1 332 ? 113.812 118.711 126.346 1.00 65.85  ?  332  HIS   B CA    1 
ATOM   8600  C  C     . HIS   B 1 332 ? 113.793 118.856 127.839 1.00 74.33  ?  332  HIS   B C     1 
ATOM   8601  O  O     . HIS   B 1 332 ? 113.952 117.884 128.534 1.00 83.01  ?  332  HIS   B O     1 
ATOM   8602  C  CB    . HIS   B 1 332 ? 114.799 117.697 125.789 1.00 67.03  ?  332  HIS   B CB    1 
ATOM   8603  C  CG    . HIS   B 1 332 ? 114.411 117.324 124.410 1.00 76.05  ?  332  HIS   B CG    1 
ATOM   8604  N  ND1   . HIS   B 1 332 ? 115.251 117.461 123.335 1.00 77.29  ?  332  HIS   B ND1   1 
ATOM   8605  C  CD2   . HIS   B 1 332 ? 113.215 116.938 123.916 1.00 78.24  ?  332  HIS   B CD2   1 
ATOM   8606  C  CE1   . HIS   B 1 332 ? 114.606 117.116 122.239 1.00 79.09  ?  332  HIS   B CE1   1 
ATOM   8607  N  NE2   . HIS   B 1 332 ? 113.366 116.802 122.564 1.00 78.87  ?  332  HIS   B NE2   1 
ATOM   8608  N  N     . MET   B 1 333 ? 113.522 120.051 128.330 1.00 69.09  ?  333  MET   B N     1 
ATOM   8609  C  CA    . MET   B 1 333 ? 113.251 120.328 129.727 1.00 61.60  ?  333  MET   B CA    1 
ATOM   8610  C  C     . MET   B 1 333 ? 112.039 121.245 129.796 1.00 63.94  ?  333  MET   B C     1 
ATOM   8611  O  O     . MET   B 1 333 ? 111.833 122.086 128.918 1.00 75.81  ?  333  MET   B O     1 
ATOM   8612  C  CB    . MET   B 1 333 ? 114.458 120.982 130.410 1.00 65.81  ?  333  MET   B CB    1 
ATOM   8613  C  CG    . MET   B 1 333 ? 115.499 119.989 130.900 1.00 70.62  ?  333  MET   B CG    1 
ATOM   8614  S  SD    . MET   B 1 333 ? 116.730 120.748 131.971 1.00 90.68  ?  333  MET   B SD    1 
ATOM   8615  C  CE    . MET   B 1 333 ? 116.966 122.312 131.139 1.00 75.89  ?  333  MET   B CE    1 
ATOM   8616  N  N     . ASP   B 1 334 ? 111.228 121.068 130.831 1.00 59.78  ?  334  ASP   B N     1 
ATOM   8617  C  CA    . ASP   B 1 334 ? 110.060 121.913 131.023 1.00 56.73  ?  334  ASP   B CA    1 
ATOM   8618  C  C     . ASP   B 1 334 ? 110.434 123.152 131.832 1.00 57.85  ?  334  ASP   B C     1 
ATOM   8619  O  O     . ASP   B 1 334 ? 111.497 123.222 132.450 1.00 68.94  ?  334  ASP   B O     1 
ATOM   8620  C  CB    . ASP   B 1 334 ? 108.941 121.133 131.710 1.00 59.03  ?  334  ASP   B CB    1 
ATOM   8621  C  CG    . ASP   B 1 334 ? 108.338 120.070 130.810 1.00 70.79  ?  334  ASP   B CG    1 
ATOM   8622  O  OD1   . ASP   B 1 334 ? 108.888 119.835 129.715 1.00 78.16  ?  334  ASP   B OD1   1 
ATOM   8623  O  OD2   . ASP   B 1 334 ? 107.314 119.470 131.194 1.00 71.07  ?  334  ASP   B OD2   1 
ATOM   8624  N  N     . TYR   B 1 335 ? 109.550 124.145 131.810 1.00 48.23  ?  335  TYR   B N     1 
ATOM   8625  C  CA    . TYR   B 1 335 ? 109.845 125.440 132.403 1.00 49.66  ?  335  TYR   B CA    1 
ATOM   8626  C  C     . TYR   B 1 335 ? 108.672 125.925 133.235 1.00 55.42  ?  335  TYR   B C     1 
ATOM   8627  O  O     . TYR   B 1 335 ? 107.513 125.683 132.890 1.00 64.97  ?  335  TYR   B O     1 
ATOM   8628  C  CB    . TYR   B 1 335 ? 110.180 126.471 131.327 1.00 46.06  ?  335  TYR   B CB    1 
ATOM   8629  C  CG    . TYR   B 1 335 ? 111.401 126.095 130.536 1.00 49.72  ?  335  TYR   B CG    1 
ATOM   8630  C  CD1   . TYR   B 1 335 ? 112.670 126.388 131.008 1.00 54.97  ?  335  TYR   B CD1   1 
ATOM   8631  C  CD2   . TYR   B 1 335 ? 111.287 125.425 129.329 1.00 53.24  ?  335  TYR   B CD2   1 
ATOM   8632  C  CE1   . TYR   B 1 335 ? 113.789 126.036 130.294 1.00 56.14  ?  335  TYR   B CE1   1 
ATOM   8633  C  CE2   . TYR   B 1 335 ? 112.400 125.071 128.608 1.00 52.68  ?  335  TYR   B CE2   1 
ATOM   8634  C  CZ    . TYR   B 1 335 ? 113.647 125.378 129.096 1.00 56.71  ?  335  TYR   B CZ    1 
ATOM   8635  O  OH    . TYR   B 1 335 ? 114.761 125.027 128.384 1.00 71.07  ?  335  TYR   B OH    1 
ATOM   8636  N  N     . GLY   B 1 336 ? 108.987 126.611 134.330 1.00 48.68  ?  336  GLY   B N     1 
ATOM   8637  C  CA    . GLY   B 1 336 ? 107.980 127.208 135.182 1.00 42.13  ?  336  GLY   B CA    1 
ATOM   8638  C  C     . GLY   B 1 336 ? 108.239 128.677 135.434 1.00 50.01  ?  336  GLY   B C     1 
ATOM   8639  O  O     . GLY   B 1 336 ? 109.308 129.050 135.924 1.00 61.36  ?  336  GLY   B O     1 
ATOM   8640  N  N     . VAL   B 1 337 ? 107.275 129.522 135.095 1.00 44.96  ?  337  VAL   B N     1 
ATOM   8641  C  CA    . VAL   B 1 337 ? 107.386 130.961 135.296 1.00 40.06  ?  337  VAL   B CA    1 
ATOM   8642  C  C     . VAL   B 1 337 ? 106.752 131.316 136.631 1.00 45.94  ?  337  VAL   B C     1 
ATOM   8643  O  O     . VAL   B 1 337 ? 105.624 130.904 136.922 1.00 57.72  ?  337  VAL   B O     1 
ATOM   8644  C  CB    . VAL   B 1 337 ? 106.712 131.728 134.146 1.00 39.93  ?  337  VAL   B CB    1 
ATOM   8645  C  CG1   . VAL   B 1 337 ? 107.110 133.194 134.145 1.00 49.47  ?  337  VAL   B CG1   1 
ATOM   8646  C  CG2   . VAL   B 1 337 ? 107.037 131.086 132.810 1.00 42.02  ?  337  VAL   B CG2   1 
ATOM   8647  N  N     . GLN   B 1 338 ? 107.471 132.086 137.438 1.00 48.92  ?  338  GLN   B N     1 
ATOM   8648  C  CA    . GLN   B 1 338 ? 107.021 132.465 138.770 1.00 45.51  ?  338  GLN   B CA    1 
ATOM   8649  C  C     . GLN   B 1 338 ? 106.473 133.886 138.731 1.00 52.84  ?  338  GLN   B C     1 
ATOM   8650  O  O     . GLN   B 1 338 ? 107.164 134.812 138.293 1.00 62.95  ?  338  GLN   B O     1 
ATOM   8651  C  CB    . GLN   B 1 338 ? 108.166 132.342 139.773 1.00 48.80  ?  338  GLN   B CB    1 
ATOM   8652  C  CG    . GLN   B 1 338 ? 108.539 130.904 140.079 1.00 48.36  ?  338  GLN   B CG    1 
ATOM   8653  C  CD    . GLN   B 1 338 ? 109.931 130.765 140.649 1.00 52.20  ?  338  GLN   B CD    1 
ATOM   8654  O  OE1   . GLN   B 1 338 ? 110.829 131.533 140.314 1.00 65.57  ?  338  GLN   B OE1   1 
ATOM   8655  N  NE2   . GLN   B 1 338 ? 110.129 129.756 141.483 1.00 52.47  ?  338  GLN   B NE2   1 
ATOM   8656  N  N     . ILE   B 1 339 ? 105.231 134.050 139.181 1.00 56.39  ?  339  ILE   B N     1 
ATOM   8657  C  CA    . ILE   B 1 339 ? 104.514 135.318 139.115 1.00 52.18  ?  339  ILE   B CA    1 
ATOM   8658  C  C     . ILE   B 1 339 ? 103.871 135.588 140.468 1.00 54.84  ?  339  ILE   B C     1 
ATOM   8659  O  O     . ILE   B 1 339 ? 103.400 134.661 141.134 1.00 69.21  ?  339  ILE   B O     1 
ATOM   8660  C  CB    . ILE   B 1 339 ? 103.442 135.302 138.001 1.00 55.46  ?  339  ILE   B CB    1 
ATOM   8661  C  CG1   . ILE   B 1 339 ? 104.046 134.859 136.668 1.00 61.11  ?  339  ILE   B CG1   1 
ATOM   8662  C  CG2   . ILE   B 1 339 ? 102.800 136.662 137.850 1.00 57.81  ?  339  ILE   B CG2   1 
ATOM   8663  C  CD1   . ILE   B 1 339 ? 103.047 134.239 135.723 1.00 60.24  ?  339  ILE   B CD1   1 
ATOM   8664  N  N     . ASN   B 1 340 ? 103.853 136.852 140.878 1.00 61.89  ?  340  ASN   B N     1 
ATOM   8665  C  CA    . ASN   B 1 340 ? 103.162 137.265 142.094 1.00 60.51  ?  340  ASN   B CA    1 
ATOM   8666  C  C     . ASN   B 1 340 ? 102.054 138.260 141.747 1.00 61.62  ?  340  ASN   B C     1 
ATOM   8667  O  O     . ASN   B 1 340 ? 101.757 138.511 140.577 1.00 68.54  ?  340  ASN   B O     1 
ATOM   8668  C  CB    . ASN   B 1 340 ? 104.142 137.845 143.120 1.00 61.06  ?  340  ASN   B CB    1 
ATOM   8669  C  CG    . ASN   B 1 340 ? 104.896 139.054 142.601 1.00 66.00  ?  340  ASN   B CG    1 
ATOM   8670  O  OD1   . ASN   B 1 340 ? 104.642 139.542 141.502 1.00 73.92  ?  340  ASN   B OD1   1 
ATOM   8671  N  ND2   . ASN   B 1 340 ? 105.884 139.495 143.365 1.00 67.20  ?  340  ASN   B ND2   1 
ATOM   8672  N  N     . LYS   B 1 341 ? 101.447 138.833 142.790 1.00 62.61  ?  341  LYS   B N     1 
ATOM   8673  C  CA    . LYS   B 1 341 ? 100.326 139.750 142.602 1.00 57.74  ?  341  LYS   B CA    1 
ATOM   8674  C  C     . LYS   B 1 341 ? 100.729 140.994 141.822 1.00 62.27  ?  341  LYS   B C     1 
ATOM   8675  O  O     . LYS   B 1 341 ? 99.913  141.546 141.074 1.00 69.32  ?  341  LYS   B O     1 
ATOM   8676  C  CB    . LYS   B 1 341 ? 99.748  140.148 143.960 1.00 64.24  ?  341  LYS   B CB    1 
ATOM   8677  C  CG    . LYS   B 1 341 ? 98.608  141.151 143.894 1.00 63.55  ?  341  LYS   B CG    1 
ATOM   8678  C  CD    . LYS   B 1 341 ? 97.392  140.659 144.659 1.00 66.59  ?  341  LYS   B CD    1 
ATOM   8679  C  CE    . LYS   B 1 341 ? 96.232  141.630 144.528 1.00 69.49  ?  341  LYS   B CE    1 
ATOM   8680  N  NZ    . LYS   B 1 341 ? 96.269  142.683 145.580 1.00 70.13  ?  341  LYS   B NZ    1 
ATOM   8681  N  N     . LEU   B 1 342 ? 101.972 141.450 141.984 1.00 63.19  ?  342  LEU   B N     1 
ATOM   8682  C  CA    . LEU   B 1 342 ? 102.394 142.691 141.345 1.00 62.20  ?  342  LEU   B CA    1 
ATOM   8683  C  C     . LEU   B 1 342 ? 102.329 142.590 139.826 1.00 67.77  ?  342  LEU   B C     1 
ATOM   8684  O  O     . LEU   B 1 342 ? 101.842 143.509 139.158 1.00 82.73  ?  342  LEU   B O     1 
ATOM   8685  C  CB    . LEU   B 1 342 ? 103.806 143.050 141.803 1.00 67.29  ?  342  LEU   B CB    1 
ATOM   8686  C  CG    . LEU   B 1 342 ? 104.271 144.478 141.537 1.00 67.73  ?  342  LEU   B CG    1 
ATOM   8687  C  CD1   . LEU   B 1 342 ? 105.031 145.047 142.718 1.00 69.38  ?  342  LEU   B CD1   1 
ATOM   8688  C  CD2   . LEU   B 1 342 ? 105.091 144.600 140.259 1.00 71.80  ?  342  LEU   B CD2   1 
ATOM   8689  N  N     . MET   B 1 343 ? 102.812 141.481 139.261 1.00 61.67  ?  343  MET   B N     1 
ATOM   8690  C  CA    . MET   B 1 343 ? 102.776 141.317 137.811 1.00 65.65  ?  343  MET   B CA    1 
ATOM   8691  C  C     . MET   B 1 343 ? 101.345 141.268 137.294 1.00 70.96  ?  343  MET   B C     1 
ATOM   8692  O  O     . MET   B 1 343 ? 101.033 141.851 136.248 1.00 75.45  ?  343  MET   B O     1 
ATOM   8693  C  CB    . MET   B 1 343 ? 103.531 140.057 137.402 1.00 72.60  ?  343  MET   B CB    1 
ATOM   8694  C  CG    . MET   B 1 343 ? 104.763 139.761 138.223 1.00 73.92  ?  343  MET   B CG    1 
ATOM   8695  S  SD    . MET   B 1 343 ? 106.251 140.674 137.780 1.00 91.99  ?  343  MET   B SD    1 
ATOM   8696  C  CE    . MET   B 1 343 ? 106.209 141.964 139.011 1.00 74.78  ?  343  MET   B CE    1 
ATOM   8697  N  N     . TYR   B 1 344 ? 100.460 140.572 138.011 1.00 63.48  ?  344  TYR   B N     1 
ATOM   8698  C  CA    . TYR   B 1 344 ? 99.060  140.523 137.606 1.00 58.79  ?  344  TYR   B CA    1 
ATOM   8699  C  C     . TYR   B 1 344 ? 98.427  141.907 137.650 1.00 63.16  ?  344  TYR   B C     1 
ATOM   8700  O  O     . TYR   B 1 344 ? 97.634  142.260 136.772 1.00 72.33  ?  344  TYR   B O     1 
ATOM   8701  C  CB    . TYR   B 1 344 ? 98.286  139.558 138.498 1.00 58.30  ?  344  TYR   B CB    1 
ATOM   8702  C  CG    . TYR   B 1 344 ? 98.543  138.095 138.224 1.00 59.35  ?  344  TYR   B CG    1 
ATOM   8703  C  CD1   . TYR   B 1 344 ? 98.021  137.475 137.098 1.00 65.42  ?  344  TYR   B CD1   1 
ATOM   8704  C  CD2   . TYR   B 1 344 ? 99.289  137.330 139.101 1.00 62.06  ?  344  TYR   B CD2   1 
ATOM   8705  C  CE1   . TYR   B 1 344 ? 98.244  136.132 136.850 1.00 64.31  ?  344  TYR   B CE1   1 
ATOM   8706  C  CE2   . TYR   B 1 344 ? 99.526  135.998 138.858 1.00 63.81  ?  344  TYR   B CE2   1 
ATOM   8707  C  CZ    . TYR   B 1 344 ? 99.005  135.400 137.733 1.00 65.21  ?  344  TYR   B CZ    1 
ATOM   8708  O  OH    . TYR   B 1 344 ? 99.229  134.058 137.534 1.00 63.05  ?  344  TYR   B OH    1 
ATOM   8709  N  N     . THR   B 1 345 ? 98.759  142.704 138.670 1.00 62.50  ?  345  THR   B N     1 
ATOM   8710  C  CA    . THR   B 1 345 ? 98.233  144.064 138.743 1.00 62.44  ?  345  THR   B CA    1 
ATOM   8711  C  C     . THR   B 1 345 ? 98.757  144.922 137.598 1.00 66.92  ?  345  THR   B C     1 
ATOM   8712  O  O     . THR   B 1 345 ? 98.016  145.737 137.036 1.00 75.08  ?  345  THR   B O     1 
ATOM   8713  C  CB    . THR   B 1 345 ? 98.578  144.699 140.090 1.00 65.26  ?  345  THR   B CB    1 
ATOM   8714  O  OG1   . THR   B 1 345 ? 98.506  143.703 141.118 1.00 73.93  ?  345  THR   B OG1   1 
ATOM   8715  C  CG2   . THR   B 1 345 ? 97.597  145.819 140.404 1.00 66.26  ?  345  THR   B CG2   1 
ATOM   8716  N  N     . ARG   B 1 346 ? 100.034 144.760 137.245 1.00 62.07  ?  346  ARG   B N     1 
ATOM   8717  C  CA    . ARG   B 1 346 ? 100.583 145.497 136.111 1.00 59.84  ?  346  ARG   B CA    1 
ATOM   8718  C  C     . ARG   B 1 346 ? 99.885  145.104 134.816 1.00 64.44  ?  346  ARG   B C     1 
ATOM   8719  O  O     . ARG   B 1 346 ? 99.657  145.949 133.943 1.00 71.51  ?  346  ARG   B O     1 
ATOM   8720  C  CB    . ARG   B 1 346 ? 102.088 145.262 136.002 1.00 57.78  ?  346  ARG   B CB    1 
ATOM   8721  C  CG    . ARG   B 1 346 ? 102.861 145.616 137.254 1.00 65.23  ?  346  ARG   B CG    1 
ATOM   8722  C  CD    . ARG   B 1 346 ? 102.779 147.094 137.561 1.00 66.91  ?  346  ARG   B CD    1 
ATOM   8723  N  NE    . ARG   B 1 346 ? 103.969 147.788 137.091 1.00 72.37  ?  346  ARG   B NE    1 
ATOM   8724  C  CZ    . ARG   B 1 346 ? 105.013 148.078 137.852 1.00 69.37  ?  346  ARG   B CZ    1 
ATOM   8725  N  NH1   . ARG   B 1 346 ? 105.030 147.782 139.140 1.00 63.48  ?  346  ARG   B NH1   1 
ATOM   8726  N  NH2   . ARG   B 1 346 ? 106.033 148.749 137.326 1.00 70.62  ?  346  ARG   B NH2   1 
ATOM   8727  N  N     . LEU   B 1 347 ? 99.549  143.820 134.668 1.00 56.56  ?  347  LEU   B N     1 
ATOM   8728  C  CA    . LEU   B 1 347 ? 98.783  143.388 133.501 1.00 57.08  ?  347  LEU   B CA    1 
ATOM   8729  C  C     . LEU   B 1 347 ? 97.383  143.987 133.503 1.00 57.81  ?  347  LEU   B C     1 
ATOM   8730  O  O     . LEU   B 1 347 ? 96.889  144.426 132.459 1.00 67.22  ?  347  LEU   B O     1 
ATOM   8731  C  CB    . LEU   B 1 347 ? 98.699  141.863 133.442 1.00 59.23  ?  347  LEU   B CB    1 
ATOM   8732  C  CG    . LEU   B 1 347 ? 97.680  141.239 132.485 1.00 57.58  ?  347  LEU   B CG    1 
ATOM   8733  C  CD1   . LEU   B 1 347 ? 98.239  141.315 131.080 1.00 52.83  ?  347  LEU   B CD1   1 
ATOM   8734  C  CD2   . LEU   B 1 347 ? 97.492  139.795 132.899 1.00 55.82  ?  347  LEU   B CD2   1 
ATOM   8735  N  N     . LEU   B 1 348 ? 96.725  144.001 134.664 1.00 63.91  ?  348  LEU   B N     1 
ATOM   8736  C  CA    . LEU   B 1 348 ? 95.361  144.515 134.747 1.00 66.53  ?  348  LEU   B CA    1 
ATOM   8737  C  C     . LEU   B 1 348 ? 95.303  146.007 134.446 1.00 64.86  ?  348  LEU   B C     1 
ATOM   8738  O  O     . LEU   B 1 348 ? 94.406  146.466 133.729 1.00 72.70  ?  348  LEU   B O     1 
ATOM   8739  C  CB    . LEU   B 1 348 ? 94.773  144.231 136.129 1.00 66.10  ?  348  LEU   B CB    1 
ATOM   8740  C  CG    . LEU   B 1 348 ? 94.445  142.777 136.468 1.00 69.30  ?  348  LEU   B CG    1 
ATOM   8741  C  CD1   . LEU   B 1 348 ? 93.379  142.711 137.548 1.00 70.95  ?  348  LEU   B CD1   1 
ATOM   8742  C  CD2   . LEU   B 1 348 ? 94.001  142.024 135.227 1.00 68.14  ?  348  LEU   B CD2   1 
ATOM   8743  N  N     . LYS   B 1 349 ? 96.176  146.794 135.001 1.00 73.14  ?  349  LYS   B N     1 
ATOM   8744  C  CA    A LYS   B 1 349 ? 96.242  148.224 134.792 0.50 73.90  ?  349  LYS   B CA    1 
ATOM   8745  C  CA    B LYS   B 1 349 ? 96.254  148.257 134.743 0.50 73.90  ?  349  LYS   B CA    1 
ATOM   8746  C  C     . LYS   B 1 349 ? 96.965  148.716 133.446 1.00 79.03  ?  349  LYS   B C     1 
ATOM   8747  O  O     . LYS   B 1 349 ? 97.132  149.901 133.036 1.00 82.29  ?  349  LYS   B O     1 
ATOM   8748  C  CB    A LYS   B 1 349 ? 96.946  148.911 135.965 0.50 70.81  ?  349  LYS   B CB    1 
ATOM   8749  C  CB    B LYS   B 1 349 ? 97.017  148.951 135.876 0.50 70.81  ?  349  LYS   B CB    1 
ATOM   8750  C  CG    A LYS   B 1 349 ? 96.124  148.958 137.240 0.50 73.71  ?  349  LYS   B CG    1 
ATOM   8751  C  CG    B LYS   B 1 349 ? 96.363  148.912 137.247 0.50 73.71  ?  349  LYS   B CG    1 
ATOM   8752  C  CD    A LYS   B 1 349 ? 97.017  149.001 138.468 0.50 80.74  ?  349  LYS   B CD    1 
ATOM   8753  C  CD    B LYS   B 1 349 ? 94.860  149.012 137.182 0.50 80.74  ?  349  LYS   B CD    1 
ATOM   8754  C  CE    A LYS   B 1 349 ? 96.413  149.868 139.559 0.50 83.58  ?  349  LYS   B CE    1 
ATOM   8755  C  CE    B LYS   B 1 349 ? 94.162  147.727 137.568 0.50 83.58  ?  349  LYS   B CE    1 
ATOM   8756  N  NZ    A LYS   B 1 349 ? 95.862  151.139 139.015 0.50 83.87  ?  349  LYS   B NZ    1 
ATOM   8757  N  NZ    B LYS   B 1 349 ? 92.819  147.640 136.950 0.50 83.87  ?  349  LYS   B NZ    1 
ATOM   8758  N  N     . GLY   B 1 350 ? 97.437  147.711 132.711 1.00 75.95  ?  350  GLY   B N     1 
ATOM   8759  C  CA    . GLY   B 1 350 ? 98.049  148.056 131.445 1.00 72.68  ?  350  GLY   B CA    1 
ATOM   8760  C  C     . GLY   B 1 350 ? 99.355  148.804 131.554 1.00 78.60  ?  350  GLY   B C     1 
ATOM   8761  O  O     . GLY   B 1 350 ? 99.757  149.469 130.597 1.00 80.71  ?  350  GLY   B O     1 
ATOM   8762  N  N     . GLU   B 1 351 ? 100.033 148.717 132.694 1.00 86.33  ?  351  GLU   B N     1 
ATOM   8763  C  CA    . GLU   B 1 351 ? 101.308 149.390 132.883 1.00 85.48  ?  351  GLU   B CA    1 
ATOM   8764  C  C     . GLU   B 1 351 ? 102.438 148.500 132.368 1.00 88.17  ?  351  GLU   B C     1 
ATOM   8765  O  O     . GLU   B 1 351 ? 102.211 147.494 131.691 1.00 90.13  ?  351  GLU   B O     1 
ATOM   8766  C  CB    . GLU   B 1 351 ? 101.503 149.763 134.350 1.00 82.90  ?  351  GLU   B CB    1 
ATOM   8767  C  CG    . GLU   B 1 351 ? 100.216 150.019 135.103 1.00 87.52  ?  351  GLU   B CG    1 
ATOM   8768  C  CD    . GLU   B 1 351 ? 100.453 150.624 136.473 1.00 96.33  ?  351  GLU   B CD    1 
ATOM   8769  O  OE1   . GLU   B 1 351 ? 101.180 150.006 137.279 1.00 94.96  ?  351  GLU   B OE1   1 
ATOM   8770  O  OE2   . GLU   B 1 351 ? 99.913  151.717 136.744 1.00 98.51  ?  351  GLU   B OE2   1 
ATOM   8771  N  N     . ASP   B 1 352 ? 103.673 148.867 132.686 1.00 88.26  ?  352  ASP   B N     1 
ATOM   8772  C  CA    . ASP   B 1 352 ? 104.847 148.153 132.213 1.00 81.30  ?  352  ASP   B CA    1 
ATOM   8773  C  C     . ASP   B 1 352 ? 105.450 147.306 133.326 1.00 86.62  ?  352  ASP   B C     1 
ATOM   8774  O  O     . ASP   B 1 352 ? 105.346 147.632 134.511 1.00 91.68  ?  352  ASP   B O     1 
ATOM   8775  C  CB    . ASP   B 1 352 ? 105.898 149.129 131.682 1.00 85.60  ?  352  ASP   B CB    1 
ATOM   8776  C  CG    . ASP   B 1 352 ? 105.809 149.321 130.183 1.00 97.75  ?  352  ASP   B CG    1 
ATOM   8777  O  OD1   . ASP   B 1 352 ? 104.757 148.985 129.600 1.00 99.53  ?  352  ASP   B OD1   1 
ATOM   8778  O  OD2   . ASP   B 1 352 ? 106.790 149.807 129.583 1.00 100.23 ?  352  ASP   B OD2   1 
ATOM   8779  N  N     . ILE   B 1 353 ? 106.079 146.208 132.924 1.00 72.43  ?  353  ILE   B N     1 
ATOM   8780  C  CA    . ILE   B 1 353 ? 106.830 145.340 133.820 1.00 66.80  ?  353  ILE   B CA    1 
ATOM   8781  C  C     . ILE   B 1 353 ? 108.313 145.589 133.585 1.00 69.03  ?  353  ILE   B C     1 
ATOM   8782  O  O     . ILE   B 1 353 ? 108.777 145.601 132.436 1.00 76.92  ?  353  ILE   B O     1 
ATOM   8783  C  CB    . ILE   B 1 353 ? 106.470 143.861 133.595 1.00 68.50  ?  353  ILE   B CB    1 
ATOM   8784  C  CG1   . ILE   B 1 353 ? 105.217 143.489 134.390 1.00 70.27  ?  353  ILE   B CG1   1 
ATOM   8785  C  CG2   . ILE   B 1 353 ? 107.631 142.958 133.976 1.00 67.66  ?  353  ILE   B CG2   1 
ATOM   8786  C  CD1   . ILE   B 1 353 ? 104.623 142.155 134.002 1.00 70.65  ?  353  ILE   B CD1   1 
ATOM   8787  N  N     . THR   B 1 354 ? 109.053 145.802 134.669 1.00 67.94  ?  354  THR   B N     1 
ATOM   8788  C  CA    . THR   B 1 354 ? 110.486 146.045 134.607 1.00 66.93  ?  354  THR   B CA    1 
ATOM   8789  C  C     . THR   B 1 354 ? 111.233 144.766 134.957 1.00 66.09  ?  354  THR   B C     1 
ATOM   8790  O  O     . THR   B 1 354 ? 110.925 144.116 135.961 1.00 77.48  ?  354  THR   B O     1 
ATOM   8791  C  CB    . THR   B 1 354 ? 110.895 147.171 135.554 1.00 67.58  ?  354  THR   B CB    1 
ATOM   8792  O  OG1   . THR   B 1 354 ? 109.859 148.159 135.590 1.00 73.04  ?  354  THR   B OG1   1 
ATOM   8793  C  CG2   . THR   B 1 354 ? 112.170 147.816 135.059 1.00 69.49  ?  354  THR   B CG2   1 
ATOM   8794  N  N     . LEU   B 1 355 ? 112.209 144.410 134.129 1.00 55.51  ?  355  LEU   B N     1 
ATOM   8795  C  CA    . LEU   B 1 355 ? 113.019 143.216 134.314 1.00 58.81  ?  355  LEU   B CA    1 
ATOM   8796  C  C     . LEU   B 1 355 ? 114.417 143.624 134.746 1.00 61.47  ?  355  LEU   B C     1 
ATOM   8797  O  O     . LEU   B 1 355 ? 115.031 144.502 134.128 1.00 68.59  ?  355  LEU   B O     1 
ATOM   8798  C  CB    . LEU   B 1 355 ? 113.091 142.388 133.030 1.00 57.09  ?  355  LEU   B CB    1 
ATOM   8799  C  CG    . LEU   B 1 355 ? 111.801 142.276 132.218 1.00 56.15  ?  355  LEU   B CG    1 
ATOM   8800  C  CD1   . LEU   B 1 355 ? 112.064 142.037 130.742 1.00 54.94  ?  355  LEU   B CD1   1 
ATOM   8801  C  CD2   . LEU   B 1 355 ? 110.860 141.220 132.773 1.00 58.79  ?  355  LEU   B CD2   1 
ATOM   8802  N  N     . PHE   B 1 356 ? 114.907 142.988 135.806 1.00 64.19  ?  356  PHE   B N     1 
ATOM   8803  C  CA    . PHE   B 1 356 ? 116.252 143.194 136.313 1.00 62.72  ?  356  PHE   B CA    1 
ATOM   8804  C  C     . PHE   B 1 356 ? 116.998 141.869 136.332 1.00 59.97  ?  356  PHE   B C     1 
ATOM   8805  O  O     . PHE   B 1 356 ? 116.397 140.792 136.368 1.00 59.58  ?  356  PHE   B O     1 
ATOM   8806  C  CB    . PHE   B 1 356 ? 116.254 143.778 137.735 1.00 60.12  ?  356  PHE   B CB    1 
ATOM   8807  C  CG    . PHE   B 1 356 ? 115.232 144.850 137.967 1.00 59.62  ?  356  PHE   B CG    1 
ATOM   8808  C  CD1   . PHE   B 1 356 ? 113.961 144.530 138.410 1.00 60.53  ?  356  PHE   B CD1   1 
ATOM   8809  C  CD2   . PHE   B 1 356 ? 115.552 146.181 137.772 1.00 59.51  ?  356  PHE   B CD2   1 
ATOM   8810  C  CE1   . PHE   B 1 356 ? 113.024 145.516 138.635 1.00 64.84  ?  356  PHE   B CE1   1 
ATOM   8811  C  CE2   . PHE   B 1 356 ? 114.619 147.171 137.996 1.00 61.78  ?  356  PHE   B CE2   1 
ATOM   8812  C  CZ    . PHE   B 1 356 ? 113.353 146.838 138.428 1.00 64.90  ?  356  PHE   B CZ    1 
ATOM   8813  N  N     . SER   B 1 357 ? 118.317 141.959 136.303 1.00 67.27  ?  357  SER   B N     1 
ATOM   8814  C  CA    . SER   B 1 357 ? 119.137 140.808 136.644 1.00 67.65  ?  357  SER   B CA    1 
ATOM   8815  C  C     . SER   B 1 357 ? 119.059 140.583 138.150 1.00 71.30  ?  357  SER   B C     1 
ATOM   8816  O  O     . SER   B 1 357 ? 119.168 141.546 138.918 1.00 76.92  ?  357  SER   B O     1 
ATOM   8817  C  CB    . SER   B 1 357 ? 120.583 141.023 136.208 1.00 71.73  ?  357  SER   B CB    1 
ATOM   8818  O  OG    . SER   B 1 357 ? 121.367 139.866 136.444 1.00 73.54  ?  357  SER   B OG    1 
ATOM   8819  N  N     . PRO   B 1 358 ? 118.848 139.348 138.611 1.00 71.83  ?  358  PRO   B N     1 
ATOM   8820  C  CA    . PRO   B 1 358 ? 118.742 139.119 140.062 1.00 71.15  ?  358  PRO   B CA    1 
ATOM   8821  C  C     . PRO   B 1 358 ? 119.974 139.545 140.841 1.00 72.87  ?  358  PRO   B C     1 
ATOM   8822  O  O     . PRO   B 1 358 ? 119.861 139.876 142.028 1.00 73.06  ?  358  PRO   B O     1 
ATOM   8823  C  CB    . PRO   B 1 358 ? 118.511 137.604 140.154 1.00 70.61  ?  358  PRO   B CB    1 
ATOM   8824  C  CG    . PRO   B 1 358 ? 119.006 137.076 138.835 1.00 73.12  ?  358  PRO   B CG    1 
ATOM   8825  C  CD    . PRO   B 1 358 ? 118.600 138.113 137.855 1.00 70.26  ?  358  PRO   B CD    1 
ATOM   8826  N  N     . SER   B 1 359 ? 121.150 139.545 140.212 1.00 77.17  ?  359  SER   B N     1 
ATOM   8827  C  CA    . SER   B 1 359 ? 122.362 139.973 140.897 1.00 76.35  ?  359  SER   B CA    1 
ATOM   8828  C  C     . SER   B 1 359 ? 122.422 141.481 141.095 1.00 79.66  ?  359  SER   B C     1 
ATOM   8829  O  O     . SER   B 1 359 ? 123.122 141.945 142.000 1.00 83.22  ?  359  SER   B O     1 
ATOM   8830  C  CB    . SER   B 1 359 ? 123.592 139.503 140.124 1.00 75.90  ?  359  SER   B CB    1 
ATOM   8831  O  OG    . SER   B 1 359 ? 123.582 140.012 138.804 1.00 78.11  ?  359  SER   B OG    1 
ATOM   8832  N  N     . ASP   B 1 360 ? 121.711 142.254 140.276 1.00 82.90  ?  360  ASP   B N     1 
ATOM   8833  C  CA    . ASP   B 1 360 ? 121.768 143.708 140.343 1.00 80.07  ?  360  ASP   B CA    1 
ATOM   8834  C  C     . ASP   B 1 360 ? 120.742 144.313 141.292 1.00 81.33  ?  360  ASP   B C     1 
ATOM   8835  O  O     . ASP   B 1 360 ? 120.790 145.523 141.537 1.00 85.85  ?  360  ASP   B O     1 
ATOM   8836  C  CB    . ASP   B 1 360 ? 121.578 144.305 138.945 1.00 82.90  ?  360  ASP   B CB    1 
ATOM   8837  C  CG    . ASP   B 1 360 ? 122.761 144.043 138.034 1.00 90.49  ?  360  ASP   B CG    1 
ATOM   8838  O  OD1   . ASP   B 1 360 ? 123.771 143.488 138.513 1.00 89.20  ?  360  ASP   B OD1   1 
ATOM   8839  O  OD2   . ASP   B 1 360 ? 122.681 144.393 136.837 1.00 89.04  ?  360  ASP   B OD2   1 
ATOM   8840  N  N     . VAL   B 1 361 ? 119.826 143.514 141.831 1.00 74.55  ?  361  VAL   B N     1 
ATOM   8841  C  CA    . VAL   B 1 361 ? 118.794 144.022 142.732 1.00 71.15  ?  361  VAL   B CA    1 
ATOM   8842  C  C     . VAL   B 1 361 ? 118.911 143.307 144.074 1.00 75.66  ?  361  VAL   B C     1 
ATOM   8843  O  O     . VAL   B 1 361 ? 118.339 142.223 144.256 1.00 78.36  ?  361  VAL   B O     1 
ATOM   8844  C  CB    . VAL   B 1 361 ? 117.394 143.860 142.118 1.00 65.75  ?  361  VAL   B CB    1 
ATOM   8845  C  CG1   . VAL   B 1 361 ? 117.109 145.006 141.164 1.00 72.41  ?  361  VAL   B CG1   1 
ATOM   8846  C  CG2   . VAL   B 1 361 ? 117.278 142.533 141.386 1.00 69.70  ?  361  VAL   B CG2   1 
ATOM   8847  N  N     . PRO   B 1 362 ? 119.629 143.876 145.044 1.00 77.05  ?  362  PRO   B N     1 
ATOM   8848  C  CA    . PRO   B 1 362 ? 119.845 143.179 146.321 1.00 71.22  ?  362  PRO   B CA    1 
ATOM   8849  C  C     . PRO   B 1 362 ? 118.558 143.106 147.130 1.00 68.51  ?  362  PRO   B C     1 
ATOM   8850  O  O     . PRO   B 1 362 ? 117.945 144.129 147.442 1.00 71.03  ?  362  PRO   B O     1 
ATOM   8851  C  CB    . PRO   B 1 362 ? 120.908 144.037 147.021 1.00 69.83  ?  362  PRO   B CB    1 
ATOM   8852  C  CG    . PRO   B 1 362 ? 121.420 144.987 145.964 1.00 71.99  ?  362  PRO   B CG    1 
ATOM   8853  C  CD    . PRO   B 1 362 ? 120.286 145.190 145.025 1.00 71.26  ?  362  PRO   B CD    1 
ATOM   8854  N  N     . GLY   B 1 363 ? 118.151 141.883 147.468 1.00 68.33  ?  363  GLY   B N     1 
ATOM   8855  C  CA    . GLY   B 1 363 ? 116.976 141.650 148.274 1.00 63.56  ?  363  GLY   B CA    1 
ATOM   8856  C  C     . GLY   B 1 363 ? 115.696 141.430 147.498 1.00 68.38  ?  363  GLY   B C     1 
ATOM   8857  O  O     . GLY   B 1 363 ? 114.720 140.936 148.072 1.00 69.77  ?  363  GLY   B O     1 
ATOM   8858  N  N     . LEU   B 1 364 ? 115.668 141.785 146.211 1.00 69.89  ?  364  LEU   B N     1 
ATOM   8859  C  CA    . LEU   B 1 364 ? 114.449 141.620 145.426 1.00 62.05  ?  364  LEU   B CA    1 
ATOM   8860  C  C     . LEU   B 1 364 ? 114.080 140.151 145.268 1.00 62.31  ?  364  LEU   B C     1 
ATOM   8861  O  O     . LEU   B 1 364 ? 112.906 139.785 145.392 1.00 66.13  ?  364  LEU   B O     1 
ATOM   8862  C  CB    . LEU   B 1 364 ? 114.610 142.279 144.057 1.00 60.91  ?  364  LEU   B CB    1 
ATOM   8863  C  CG    . LEU   B 1 364 ? 113.307 142.541 143.301 1.00 62.44  ?  364  LEU   B CG    1 
ATOM   8864  C  CD1   . LEU   B 1 364 ? 112.515 143.651 143.968 1.00 65.38  ?  364  LEU   B CD1   1 
ATOM   8865  C  CD2   . LEU   B 1 364 ? 113.584 142.876 141.847 1.00 64.11  ?  364  LEU   B CD2   1 
ATOM   8866  N  N     . TYR   B 1 365 ? 115.066 139.294 144.992 1.00 61.29  ?  365  TYR   B N     1 
ATOM   8867  C  CA    . TYR   B 1 365 ? 114.772 137.880 144.785 1.00 55.53  ?  365  TYR   B CA    1 
ATOM   8868  C  C     . TYR   B 1 365 ? 114.246 137.228 146.058 1.00 67.76  ?  365  TYR   B C     1 
ATOM   8869  O  O     . TYR   B 1 365 ? 113.299 136.435 146.007 1.00 81.12  ?  365  TYR   B O     1 
ATOM   8870  C  CB    . TYR   B 1 365 ? 116.013 137.147 144.279 1.00 61.04  ?  365  TYR   B CB    1 
ATOM   8871  C  CG    . TYR   B 1 365 ? 115.744 135.709 143.902 1.00 64.28  ?  365  TYR   B CG    1 
ATOM   8872  C  CD1   . TYR   B 1 365 ? 115.252 135.381 142.647 1.00 62.75  ?  365  TYR   B CD1   1 
ATOM   8873  C  CD2   . TYR   B 1 365 ? 115.974 134.679 144.803 1.00 64.43  ?  365  TYR   B CD2   1 
ATOM   8874  C  CE1   . TYR   B 1 365 ? 114.997 134.070 142.301 1.00 60.26  ?  365  TYR   B CE1   1 
ATOM   8875  C  CE2   . TYR   B 1 365 ? 115.716 133.366 144.467 1.00 62.08  ?  365  TYR   B CE2   1 
ATOM   8876  C  CZ    . TYR   B 1 365 ? 115.251 133.065 143.206 1.00 64.80  ?  365  TYR   B CZ    1 
ATOM   8877  O  OH    . TYR   B 1 365 ? 114.974 131.760 142.875 1.00 76.28  ?  365  TYR   B OH    1 
ATOM   8878  N  N     . ASP   B 1 366 ? 114.851 137.539 147.206 1.00 73.90  ?  366  ASP   B N     1 
ATOM   8879  C  CA    . ASP   B 1 366 ? 114.380 136.965 148.462 1.00 74.23  ?  366  ASP   B CA    1 
ATOM   8880  C  C     . ASP   B 1 366 ? 112.979 137.454 148.805 1.00 74.71  ?  366  ASP   B C     1 
ATOM   8881  O  O     . ASP   B 1 366 ? 112.127 136.665 149.231 1.00 76.51  ?  366  ASP   B O     1 
ATOM   8882  C  CB    . ASP   B 1 366 ? 115.359 137.293 149.587 1.00 79.11  ?  366  ASP   B CB    1 
ATOM   8883  C  CG    . ASP   B 1 366 ? 116.787 136.927 149.239 1.00 87.40  ?  366  ASP   B CG    1 
ATOM   8884  O  OD1   . ASP   B 1 366 ? 117.312 137.460 148.243 1.00 90.22  ?  366  ASP   B OD1   1 
ATOM   8885  O  OD2   . ASP   B 1 366 ? 117.385 136.109 149.966 1.00 88.49  ?  366  ASP   B OD2   1 
ATOM   8886  N  N     . ALA   B 1 367 ? 112.717 138.747 148.612 1.00 62.86  ?  367  ALA   B N     1 
ATOM   8887  C  CA    . ALA   B 1 367 ? 111.398 139.294 148.897 1.00 57.79  ?  367  ALA   B CA    1 
ATOM   8888  C  C     . ALA   B 1 367 ? 110.352 138.874 147.876 1.00 61.32  ?  367  ALA   B C     1 
ATOM   8889  O  O     . ALA   B 1 367 ? 109.159 139.054 148.136 1.00 70.57  ?  367  ALA   B O     1 
ATOM   8890  C  CB    . ALA   B 1 367 ? 111.469 140.819 148.968 1.00 58.01  ?  367  ALA   B CB    1 
ATOM   8891  N  N     . PHE   B 1 368 ? 110.772 138.343 146.723 1.00 61.58  ?  368  PHE   B N     1 
ATOM   8892  C  CA    . PHE   B 1 368 ? 109.822 137.836 145.740 1.00 47.72  ?  368  PHE   B CA    1 
ATOM   8893  C  C     . PHE   B 1 368 ? 108.956 136.735 146.331 1.00 52.73  ?  368  PHE   B C     1 
ATOM   8894  O  O     . PHE   B 1 368 ? 107.769 136.626 146.006 1.00 59.36  ?  368  PHE   B O     1 
ATOM   8895  C  CB    . PHE   B 1 368 ? 110.571 137.323 144.513 1.00 46.82  ?  368  PHE   B CB    1 
ATOM   8896  C  CG    . PHE   B 1 368 ? 109.684 136.983 143.353 1.00 50.68  ?  368  PHE   B CG    1 
ATOM   8897  C  CD1   . PHE   B 1 368 ? 108.630 137.807 143.004 1.00 52.61  ?  368  PHE   B CD1   1 
ATOM   8898  C  CD2   . PHE   B 1 368 ? 109.907 135.837 142.606 1.00 55.63  ?  368  PHE   B CD2   1 
ATOM   8899  C  CE1   . PHE   B 1 368 ? 107.807 137.481 141.945 1.00 53.48  ?  368  PHE   B CE1   1 
ATOM   8900  C  CE2   . PHE   B 1 368 ? 109.080 135.514 141.547 1.00 54.85  ?  368  PHE   B CE2   1 
ATOM   8901  C  CZ    . PHE   B 1 368 ? 108.076 136.374 141.180 1.00 57.04  ?  368  PHE   B CZ    1 
ATOM   8902  N  N     . PHE   B 1 369 ? 109.532 135.912 147.206 1.00 59.74  ?  369  PHE   B N     1 
ATOM   8903  C  CA    . PHE   B 1 369 ? 108.831 134.789 147.810 1.00 58.02  ?  369  PHE   B CA    1 
ATOM   8904  C  C     . PHE   B 1 369 ? 108.473 135.000 149.273 1.00 69.06  ?  369  PHE   B C     1 
ATOM   8905  O  O     . PHE   B 1 369 ? 107.457 134.473 149.724 1.00 74.58  ?  369  PHE   B O     1 
ATOM   8906  C  CB    . PHE   B 1 369 ? 109.673 133.509 147.699 1.00 55.71  ?  369  PHE   B CB    1 
ATOM   8907  C  CG    . PHE   B 1 369 ? 110.292 133.296 146.345 1.00 57.71  ?  369  PHE   B CG    1 
ATOM   8908  C  CD1   . PHE   B 1 369 ? 111.507 133.875 146.021 1.00 55.12  ?  369  PHE   B CD1   1 
ATOM   8909  C  CD2   . PHE   B 1 369 ? 109.667 132.503 145.401 1.00 60.37  ?  369  PHE   B CD2   1 
ATOM   8910  C  CE1   . PHE   B 1 369 ? 112.076 133.681 144.779 1.00 56.96  ?  369  PHE   B CE1   1 
ATOM   8911  C  CE2   . PHE   B 1 369 ? 110.234 132.302 144.160 1.00 50.41  ?  369  PHE   B CE2   1 
ATOM   8912  C  CZ    . PHE   B 1 369 ? 111.442 132.886 143.852 1.00 53.18  ?  369  PHE   B CZ    1 
ATOM   8913  N  N     . ALA   B 1 370 ? 109.272 135.763 150.021 1.00 78.92  ?  370  ALA   B N     1 
ATOM   8914  C  CA    . ALA   B 1 370 ? 109.097 135.830 151.468 1.00 74.83  ?  370  ALA   B CA    1 
ATOM   8915  C  C     . ALA   B 1 370 ? 107.885 136.672 151.847 1.00 78.14  ?  370  ALA   B C     1 
ATOM   8916  O  O     . ALA   B 1 370 ? 106.909 136.154 152.401 1.00 83.98  ?  370  ALA   B O     1 
ATOM   8917  C  CB    . ALA   B 1 370 ? 110.370 136.370 152.115 1.00 73.94  ?  370  ALA   B CB    1 
ATOM   8918  N  N     . ASP   B 1 371 ? 107.905 137.962 151.517 1.00 85.22  ?  371  ASP   B N     1 
ATOM   8919  C  CA    . ASP   B 1 371 ? 106.783 138.842 151.804 1.00 88.51  ?  371  ASP   B CA    1 
ATOM   8920  C  C     . ASP   B 1 371 ? 106.659 139.862 150.683 1.00 86.91  ?  371  ASP   B C     1 
ATOM   8921  O  O     . ASP   B 1 371 ? 107.667 140.331 150.148 1.00 87.56  ?  371  ASP   B O     1 
ATOM   8922  C  CB    . ASP   B 1 371 ? 106.949 139.532 153.161 1.00 90.23  ?  371  ASP   B CB    1 
ATOM   8923  C  CG    . ASP   B 1 371 ? 107.946 140.668 153.121 1.00 93.65  ?  371  ASP   B CG    1 
ATOM   8924  O  OD1   . ASP   B 1 371 ? 109.156 140.397 152.978 1.00 93.63  ?  371  ASP   B OD1   1 
ATOM   8925  O  OD2   . ASP   B 1 371 ? 107.517 141.833 153.245 1.00 95.01  ?  371  ASP   B OD2   1 
ATOM   8926  N  N     . GLN   B 1 372 ? 105.419 140.201 150.336 1.00 81.03  ?  372  GLN   B N     1 
ATOM   8927  C  CA    . GLN   B 1 372 ? 105.161 140.986 149.138 1.00 80.16  ?  372  GLN   B CA    1 
ATOM   8928  C  C     . GLN   B 1 372 ? 105.155 142.489 149.376 1.00 85.64  ?  372  GLN   B C     1 
ATOM   8929  O  O     . GLN   B 1 372 ? 105.316 143.247 148.414 1.00 93.61  ?  372  GLN   B O     1 
ATOM   8930  C  CB    . GLN   B 1 372 ? 103.832 140.560 148.507 1.00 78.46  ?  372  GLN   B CB    1 
ATOM   8931  C  CG    . GLN   B 1 372 ? 103.670 139.058 148.366 1.00 84.24  ?  372  GLN   B CG    1 
ATOM   8932  C  CD    . GLN   B 1 372 ? 104.645 138.425 147.385 1.00 84.82  ?  372  GLN   B CD    1 
ATOM   8933  O  OE1   . GLN   B 1 372 ? 104.258 138.017 146.296 1.00 90.07  ?  372  GLN   B OE1   1 
ATOM   8934  N  NE2   . GLN   B 1 372 ? 105.885 138.241 147.814 1.00 82.89  ?  372  GLN   B NE2   1 
ATOM   8935  N  N     . GLU   B 1 373 ? 104.978 142.945 150.617 1.00 87.85  ?  373  GLU   B N     1 
ATOM   8936  C  CA    . GLU   B 1 373 ? 105.147 144.367 150.899 1.00 85.90  ?  373  GLU   B CA    1 
ATOM   8937  C  C     . GLU   B 1 373 ? 106.587 144.794 150.643 1.00 90.17  ?  373  GLU   B C     1 
ATOM   8938  O  O     . GLU   B 1 373 ? 106.846 145.814 149.989 1.00 93.36  ?  373  GLU   B O     1 
ATOM   8939  C  CB    . GLU   B 1 373 ? 104.736 144.668 152.343 1.00 91.46  ?  373  GLU   B CB    1 
ATOM   8940  C  CG    . GLU   B 1 373 ? 103.249 144.491 152.639 1.00 100.03 ?  373  GLU   B CG    1 
ATOM   8941  C  CD    . GLU   B 1 373 ? 102.897 144.730 154.101 1.00 104.33 ?  373  GLU   B CD    1 
ATOM   8942  O  OE1   . GLU   B 1 373 ? 103.826 144.848 154.927 1.00 102.07 ?  373  GLU   B OE1   1 
ATOM   8943  O  OE2   . GLU   B 1 373 ? 101.690 144.799 154.412 1.00 102.35 ?  373  GLU   B OE2   1 
ATOM   8944  N  N     . GLU   B 1 374 ? 107.542 144.009 151.148 1.00 78.84  ?  374  GLU   B N     1 
ATOM   8945  C  CA    . GLU   B 1 374 ? 108.949 144.300 150.905 1.00 79.77  ?  374  GLU   B CA    1 
ATOM   8946  C  C     . GLU   B 1 374 ? 109.278 144.204 149.424 1.00 80.24  ?  374  GLU   B C     1 
ATOM   8947  O  O     . GLU   B 1 374 ? 110.053 145.014 148.901 1.00 83.93  ?  374  GLU   B O     1 
ATOM   8948  C  CB    . GLU   B 1 374 ? 109.832 143.352 151.718 1.00 81.37  ?  374  GLU   B CB    1 
ATOM   8949  C  CG    . GLU   B 1 374 ? 111.329 143.543 151.517 1.00 85.00  ?  374  GLU   B CG    1 
ATOM   8950  C  CD    . GLU   B 1 374 ? 111.854 144.834 152.123 1.00 91.37  ?  374  GLU   B CD    1 
ATOM   8951  O  OE1   . GLU   B 1 374 ? 111.076 145.558 152.780 1.00 90.65  ?  374  GLU   B OE1   1 
ATOM   8952  O  OE2   . GLU   B 1 374 ? 113.053 145.129 151.936 1.00 90.64  ?  374  GLU   B OE2   1 
ATOM   8953  N  N     . PHE   B 1 375 ? 108.701 143.220 148.729 1.00 67.67  ?  375  PHE   B N     1 
ATOM   8954  C  CA    . PHE   B 1 375 ? 108.947 143.110 147.297 1.00 63.79  ?  375  PHE   B CA    1 
ATOM   8955  C  C     . PHE   B 1 375 ? 108.424 144.328 146.553 1.00 68.89  ?  375  PHE   B C     1 
ATOM   8956  O  O     . PHE   B 1 375 ? 109.094 144.841 145.655 1.00 76.89  ?  375  PHE   B O     1 
ATOM   8957  C  CB    . PHE   B 1 375 ? 108.319 141.845 146.717 1.00 61.87  ?  375  PHE   B CB    1 
ATOM   8958  C  CG    . PHE   B 1 375 ? 108.523 141.714 145.232 1.00 62.42  ?  375  PHE   B CG    1 
ATOM   8959  C  CD1   . PHE   B 1 375 ? 109.721 141.244 144.725 1.00 64.78  ?  375  PHE   B CD1   1 
ATOM   8960  C  CD2   . PHE   B 1 375 ? 107.533 142.099 144.344 1.00 60.80  ?  375  PHE   B CD2   1 
ATOM   8961  C  CE1   . PHE   B 1 375 ? 109.920 141.138 143.362 1.00 67.74  ?  375  PHE   B CE1   1 
ATOM   8962  C  CE2   . PHE   B 1 375 ? 107.729 141.999 142.980 1.00 61.15  ?  375  PHE   B CE2   1 
ATOM   8963  C  CZ    . PHE   B 1 375 ? 108.923 141.517 142.490 1.00 66.69  ?  375  PHE   B CZ    1 
ATOM   8964  N  N     . GLU   B 1 376 ? 107.221 144.796 146.896 1.00 78.74  ?  376  GLU   B N     1 
ATOM   8965  C  CA    . GLU   B 1 376 ? 106.689 145.977 146.226 1.00 75.08  ?  376  GLU   B CA    1 
ATOM   8966  C  C     . GLU   B 1 376 ? 107.556 147.197 146.497 1.00 82.11  ?  376  GLU   B C     1 
ATOM   8967  O  O     . GLU   B 1 376 ? 107.850 147.973 145.579 1.00 90.26  ?  376  GLU   B O     1 
ATOM   8968  C  CB    . GLU   B 1 376 ? 105.249 146.240 146.660 1.00 75.50  ?  376  GLU   B CB    1 
ATOM   8969  C  CG    . GLU   B 1 376 ? 104.628 147.446 145.969 1.00 83.63  ?  376  GLU   B CG    1 
ATOM   8970  C  CD    . GLU   B 1 376 ? 103.235 147.174 145.437 1.00 93.75  ?  376  GLU   B CD    1 
ATOM   8971  O  OE1   . GLU   B 1 376 ? 102.474 148.146 145.244 1.00 92.35  ?  376  GLU   B OE1   1 
ATOM   8972  O  OE2   . GLU   B 1 376 ? 102.902 145.990 145.226 1.00 92.36  ?  376  GLU   B OE2   1 
ATOM   8973  N  N     . ARG   B 1 377 ? 107.987 147.380 147.748 1.00 74.03  ?  377  ARG   B N     1 
ATOM   8974  C  CA    . ARG   B 1 377 ? 108.830 148.528 148.067 1.00 73.05  ?  377  ARG   B CA    1 
ATOM   8975  C  C     . ARG   B 1 377 ? 110.142 148.478 147.294 1.00 76.20  ?  377  ARG   B C     1 
ATOM   8976  O  O     . ARG   B 1 377 ? 110.555 149.470 146.680 1.00 79.65  ?  377  ARG   B O     1 
ATOM   8977  C  CB    . ARG   B 1 377 ? 109.091 148.593 149.572 1.00 73.56  ?  377  ARG   B CB    1 
ATOM   8978  C  CG    . ARG   B 1 377 ? 109.308 150.005 150.090 1.00 75.30  ?  377  ARG   B CG    1 
ATOM   8979  C  CD    . ARG   B 1 377 ? 110.198 150.028 151.320 1.00 77.80  ?  377  ARG   B CD    1 
ATOM   8980  N  NE    . ARG   B 1 377 ? 111.610 149.934 150.972 1.00 83.73  ?  377  ARG   B NE    1 
ATOM   8981  C  CZ    . ARG   B 1 377 ? 112.395 148.921 151.310 1.00 81.45  ?  377  ARG   B CZ    1 
ATOM   8982  N  NH1   . ARG   B 1 377 ? 111.940 147.902 152.019 1.00 75.48  ?  377  ARG   B NH1   1 
ATOM   8983  N  NH2   . ARG   B 1 377 ? 113.669 148.932 150.929 1.00 81.13  ?  377  ARG   B NH2   1 
ATOM   8984  N  N     . LEU   B 1 378 ? 110.804 147.318 147.297 1.00 74.15  ?  378  LEU   B N     1 
ATOM   8985  C  CA    . LEU   B 1 378 ? 112.079 147.188 146.600 1.00 70.05  ?  378  LEU   B CA    1 
ATOM   8986  C  C     . LEU   B 1 378 ? 111.910 147.341 145.094 1.00 73.11  ?  378  LEU   B C     1 
ATOM   8987  O  O     . LEU   B 1 378 ? 112.734 147.984 144.436 1.00 80.88  ?  378  LEU   B O     1 
ATOM   8988  C  CB    . LEU   B 1 378 ? 112.725 145.845 146.936 1.00 70.05  ?  378  LEU   B CB    1 
ATOM   8989  C  CG    . LEU   B 1 378 ? 113.406 145.763 148.302 1.00 70.49  ?  378  LEU   B CG    1 
ATOM   8990  C  CD1   . LEU   B 1 378 ? 113.861 144.344 148.594 1.00 71.18  ?  378  LEU   B CD1   1 
ATOM   8991  C  CD2   . LEU   B 1 378 ? 114.575 146.733 148.376 1.00 72.46  ?  378  LEU   B CD2   1 
ATOM   8992  N  N     . TYR   B 1 379 ? 110.849 146.759 144.531 1.00 60.88  ?  379  TYR   B N     1 
ATOM   8993  C  CA    . TYR   B 1 379 ? 110.598 146.862 143.099 1.00 58.79  ?  379  TYR   B CA    1 
ATOM   8994  C  C     . TYR   B 1 379 ? 110.363 148.308 142.690 1.00 65.93  ?  379  TYR   B C     1 
ATOM   8995  O  O     . TYR   B 1 379 ? 110.926 148.785 141.697 1.00 72.73  ?  379  TYR   B O     1 
ATOM   8996  C  CB    . TYR   B 1 379 ? 109.395 145.989 142.734 1.00 64.24  ?  379  TYR   B CB    1 
ATOM   8997  C  CG    . TYR   B 1 379 ? 109.293 145.612 141.275 1.00 66.51  ?  379  TYR   B CG    1 
ATOM   8998  C  CD1   . TYR   B 1 379 ? 110.018 144.547 140.760 1.00 68.72  ?  379  TYR   B CD1   1 
ATOM   8999  C  CD2   . TYR   B 1 379 ? 108.454 146.307 140.418 1.00 61.80  ?  379  TYR   B CD2   1 
ATOM   9000  C  CE1   . TYR   B 1 379 ? 109.921 144.195 139.429 1.00 68.10  ?  379  TYR   B CE1   1 
ATOM   9001  C  CE2   . TYR   B 1 379 ? 108.353 145.964 139.087 1.00 59.77  ?  379  TYR   B CE2   1 
ATOM   9002  C  CZ    . TYR   B 1 379 ? 109.075 144.899 138.601 1.00 67.69  ?  379  TYR   B CZ    1 
ATOM   9003  O  OH    . TYR   B 1 379 ? 108.992 144.566 137.271 1.00 79.35  ?  379  TYR   B OH    1 
ATOM   9004  N  N     . THR   B 1 380 ? 109.542 149.030 143.457 1.00 66.24  ?  380  THR   B N     1 
ATOM   9005  C  CA    . THR   B 1 380 ? 109.295 150.434 143.153 1.00 67.06  ?  380  THR   B CA    1 
ATOM   9006  C  C     . THR   B 1 380 ? 110.571 151.257 143.281 1.00 75.73  ?  380  THR   B C     1 
ATOM   9007  O  O     . THR   B 1 380 ? 110.841 152.126 142.443 1.00 82.88  ?  380  THR   B O     1 
ATOM   9008  C  CB    . THR   B 1 380 ? 108.204 150.986 144.072 1.00 74.55  ?  380  THR   B CB    1 
ATOM   9009  O  OG1   . THR   B 1 380 ? 107.003 150.223 143.901 1.00 78.09  ?  380  THR   B OG1   1 
ATOM   9010  C  CG2   . THR   B 1 380 ? 107.922 152.447 143.751 1.00 75.89  ?  380  THR   B CG2   1 
ATOM   9011  N  N     . LYS   B 1 381 ? 111.371 150.994 144.324 1.00 73.90  ?  381  LYS   B N     1 
ATOM   9012  C  CA    A LYS   B 1 381 ? 112.621 151.725 144.519 0.50 70.73  ?  381  LYS   B CA    1 
ATOM   9013  C  CA    B LYS   B 1 381 ? 112.721 151.725 144.519 0.50 70.73  ?  381  LYS   B CA    1 
ATOM   9014  C  C     . LYS   B 1 381 ? 113.556 151.513 143.350 1.00 70.06  ?  381  LYS   B C     1 
ATOM   9015  O  O     . LYS   B 1 381 ? 114.133 152.464 142.812 1.00 77.05  ?  381  LYS   B O     1 
ATOM   9016  C  CB    A LYS   B 1 381 ? 113.321 151.270 145.801 0.50 68.58  ?  381  LYS   B CB    1 
ATOM   9017  C  CB    B LYS   B 1 381 ? 113.421 151.270 145.801 0.50 68.58  ?  381  LYS   B CB    1 
ATOM   9018  C  CG    A LYS   B 1 381 ? 114.749 151.811 145.951 0.50 70.11  ?  381  LYS   B CG    1 
ATOM   9019  C  CG    B LYS   B 1 381 ? 114.732 152.014 146.087 0.50 70.11  ?  381  LYS   B CG    1 
ATOM   9020  C  CD    A LYS   B 1 381 ? 115.598 150.976 146.907 0.50 68.79  ?  381  LYS   B CD    1 
ATOM   9021  C  CD    B LYS   B 1 381 ? 115.385 151.575 147.396 0.50 68.79  ?  381  LYS   B CD    1 
ATOM   9022  C  CE    A LYS   B 1 381 ? 115.028 150.951 148.316 0.50 77.05  ?  381  LYS   B CE    1 
ATOM   9023  C  CE    B LYS   B 1 381 ? 116.696 152.299 147.660 0.50 77.05  ?  381  LYS   B CE    1 
ATOM   9024  N  NZ    A LYS   B 1 381 ? 116.115 150.938 149.334 0.50 80.68  ?  381  LYS   B NZ    1 
ATOM   9025  N  NZ    B LYS   B 1 381 ? 117.307 151.850 148.941 0.50 80.68  ?  381  LYS   B NZ    1 
ATOM   9026  N  N     . TYR   B 1 382 ? 113.729 150.254 142.958 1.00 73.09  ?  382  TYR   B N     1 
ATOM   9027  C  CA    . TYR   B 1 382 ? 114.688 149.902 141.930 1.00 72.31  ?  382  TYR   B CA    1 
ATOM   9028  C  C     . TYR   B 1 382 ? 114.218 150.301 140.543 1.00 74.46  ?  382  TYR   B C     1 
ATOM   9029  O  O     . TYR   B 1 382 ? 115.057 150.488 139.658 1.00 80.08  ?  382  TYR   B O     1 
ATOM   9030  C  CB    . TYR   B 1 382 ? 114.968 148.402 141.980 1.00 73.72  ?  382  TYR   B CB    1 
ATOM   9031  C  CG    . TYR   B 1 382 ? 115.753 147.957 143.194 1.00 73.68  ?  382  TYR   B CG    1 
ATOM   9032  C  CD1   . TYR   B 1 382 ? 116.800 148.724 143.687 1.00 77.61  ?  382  TYR   B CD1   1 
ATOM   9033  C  CD2   . TYR   B 1 382 ? 115.452 146.772 143.846 1.00 70.25  ?  382  TYR   B CD2   1 
ATOM   9034  C  CE1   . TYR   B 1 382 ? 117.527 148.326 144.790 1.00 78.69  ?  382  TYR   B CE1   1 
ATOM   9035  C  CE2   . TYR   B 1 382 ? 116.162 146.376 144.959 1.00 69.83  ?  382  TYR   B CE2   1 
ATOM   9036  C  CZ    . TYR   B 1 382 ? 117.202 147.149 145.420 1.00 76.01  ?  382  TYR   B CZ    1 
ATOM   9037  O  OH    . TYR   B 1 382 ? 117.891 146.686 146.514 1.00 82.01  ?  382  TYR   B OH    1 
ATOM   9038  N  N     . GLU   B 1 383 ? 112.906 150.430 140.327 1.00 82.04  ?  383  GLU   B N     1 
ATOM   9039  C  CA    . GLU   B 1 383 ? 112.423 150.891 139.030 1.00 78.01  ?  383  GLU   B CA    1 
ATOM   9040  C  C     . GLU   B 1 383 ? 112.794 152.345 138.774 1.00 83.98  ?  383  GLU   B C     1 
ATOM   9041  O  O     . GLU   B 1 383 ? 113.031 152.728 137.623 1.00 88.90  ?  383  GLU   B O     1 
ATOM   9042  C  CB    . GLU   B 1 383 ? 110.911 150.710 138.935 1.00 77.31  ?  383  GLU   B CB    1 
ATOM   9043  C  CG    . GLU   B 1 383 ? 110.475 149.307 138.600 1.00 81.50  ?  383  GLU   B CG    1 
ATOM   9044  C  CD    . GLU   B 1 383 ? 108.978 149.180 138.440 1.00 87.58  ?  383  GLU   B CD    1 
ATOM   9045  O  OE1   . GLU   B 1 383 ? 108.243 149.584 139.363 1.00 89.21  ?  383  GLU   B OE1   1 
ATOM   9046  O  OE2   . GLU   B 1 383 ? 108.541 148.595 137.429 1.00 87.59  ?  383  GLU   B OE2   1 
ATOM   9047  N  N     . LYS   B 1 384 ? 112.842 153.169 139.820 1.00 86.61  ?  384  LYS   B N     1 
ATOM   9048  C  CA    . LYS   B 1 384 ? 113.218 154.568 139.673 1.00 88.32  ?  384  LYS   B CA    1 
ATOM   9049  C  C     . LYS   B 1 384 ? 114.722 154.795 139.749 1.00 90.63  ?  384  LYS   B C     1 
ATOM   9050  O  O     . LYS   B 1 384 ? 115.172 155.925 139.533 1.00 94.37  ?  384  LYS   B O     1 
ATOM   9051  C  CB    . LYS   B 1 384 ? 112.521 155.421 140.738 1.00 89.01  ?  384  LYS   B CB    1 
ATOM   9052  C  CG    . LYS   B 1 384 ? 111.108 154.976 141.061 1.00 90.14  ?  384  LYS   B CG    1 
ATOM   9053  C  CD    . LYS   B 1 384 ? 110.528 155.773 142.215 1.00 92.91  ?  384  LYS   B CD    1 
ATOM   9054  C  CE    . LYS   B 1 384 ? 109.038 156.002 142.028 1.00 94.29  ?  384  LYS   B CE    1 
ATOM   9055  N  NZ    . LYS   B 1 384 ? 108.721 156.470 140.650 1.00 94.38  ?  384  LYS   B NZ    1 
ATOM   9056  N  N     . ASP   B 1 385 ? 115.505 153.762 140.046 1.00 92.29  ?  385  ASP   B N     1 
ATOM   9057  C  CA    . ASP   B 1 385 ? 116.956 153.892 140.079 1.00 93.69  ?  385  ASP   B CA    1 
ATOM   9058  C  C     . ASP   B 1 385 ? 117.494 153.801 138.657 1.00 95.68  ?  385  ASP   B C     1 
ATOM   9059  O  O     . ASP   B 1 385 ? 117.275 152.800 137.967 1.00 98.14  ?  385  ASP   B O     1 
ATOM   9060  C  CB    . ASP   B 1 385 ? 117.570 152.810 140.964 1.00 96.34  ?  385  ASP   B CB    1 
ATOM   9061  C  CG    . ASP   B 1 385 ? 119.027 153.078 141.295 1.00 100.36 ?  385  ASP   B CG    1 
ATOM   9062  O  OD1   . ASP   B 1 385 ? 119.639 153.963 140.660 1.00 102.06 ?  385  ASP   B OD1   1 
ATOM   9063  O  OD2   . ASP   B 1 385 ? 119.561 152.403 142.198 1.00 99.18  ?  385  ASP   B OD2   1 
ATOM   9064  N  N     . ASP   B 1 386 ? 118.194 154.846 138.218 1.00 102.02 ?  386  ASP   B N     1 
ATOM   9065  C  CA    . ASP   B 1 386 ? 118.730 154.901 136.865 1.00 101.97 ?  386  ASP   B CA    1 
ATOM   9066  C  C     . ASP   B 1 386 ? 120.101 154.253 136.737 1.00 99.36  ?  386  ASP   B C     1 
ATOM   9067  O  O     . ASP   B 1 386 ? 120.599 154.116 135.615 1.00 101.23 ?  386  ASP   B O     1 
ATOM   9068  C  CB    . ASP   B 1 386 ? 118.813 156.355 136.380 1.00 103.70 ?  386  ASP   B CB    1 
ATOM   9069  C  CG    . ASP   B 1 386 ? 117.444 156.962 136.127 1.00 108.16 ?  386  ASP   B CG    1 
ATOM   9070  O  OD1   . ASP   B 1 386 ? 116.563 156.262 135.585 1.00 107.38 ?  386  ASP   B OD1   1 
ATOM   9071  O  OD2   . ASP   B 1 386 ? 117.220 158.115 136.546 1.00 107.19 ?  386  ASP   B OD2   1 
ATOM   9072  N  N     . SER   B 1 387 ? 120.718 153.854 137.846 1.00 90.79  ?  387  SER   B N     1 
ATOM   9073  C  CA    . SER   B 1 387 ? 122.036 153.234 137.827 1.00 94.34  ?  387  SER   B CA    1 
ATOM   9074  C  C     . SER   B 1 387 ? 121.979 151.713 137.782 1.00 97.27  ?  387  SER   B C     1 
ATOM   9075  O  O     . SER   B 1 387 ? 123.031 151.067 137.819 1.00 97.32  ?  387  SER   B O     1 
ATOM   9076  C  CB    . SER   B 1 387 ? 122.843 153.679 139.051 1.00 96.04  ?  387  SER   B CB    1 
ATOM   9077  O  OG    . SER   B 1 387 ? 122.324 153.104 140.238 1.00 95.94  ?  387  SER   B OG    1 
ATOM   9078  N  N     . ILE   B 1 388 ? 120.787 151.128 137.701 1.00 85.01  ?  388  ILE   B N     1 
ATOM   9079  C  CA    . ILE   B 1 388 ? 120.606 149.681 137.697 1.00 81.37  ?  388  ILE   B CA    1 
ATOM   9080  C  C     . ILE   B 1 388 ? 120.209 149.251 136.293 1.00 82.55  ?  388  ILE   B C     1 
ATOM   9081  O  O     . ILE   B 1 388 ? 119.310 149.846 135.686 1.00 84.43  ?  388  ILE   B O     1 
ATOM   9082  C  CB    . ILE   B 1 388 ? 119.550 149.244 138.727 1.00 77.77  ?  388  ILE   B CB    1 
ATOM   9083  C  CG1   . ILE   B 1 388 ? 120.152 149.241 140.131 1.00 78.78  ?  388  ILE   B CG1   1 
ATOM   9084  C  CG2   . ILE   B 1 388 ? 118.997 147.870 138.387 1.00 82.39  ?  388  ILE   B CG2   1 
ATOM   9085  C  CD1   . ILE   B 1 388 ? 119.123 149.318 141.224 1.00 79.30  ?  388  ILE   B CD1   1 
ATOM   9086  N  N     . ARG   B 1 389 ? 120.885 148.229 135.774 1.00 78.42  ?  389  ARG   B N     1 
ATOM   9087  C  CA    . ARG   B 1 389 ? 120.538 147.699 134.463 1.00 77.27  ?  389  ARG   B CA    1 
ATOM   9088  C  C     . ARG   B 1 389 ? 119.160 147.052 134.513 1.00 80.36  ?  389  ARG   B C     1 
ATOM   9089  O  O     . ARG   B 1 389 ? 118.901 146.178 135.346 1.00 83.60  ?  389  ARG   B O     1 
ATOM   9090  C  CB    . ARG   B 1 389 ? 121.584 146.687 134.003 1.00 77.35  ?  389  ARG   B CB    1 
ATOM   9091  C  CG    . ARG   B 1 389 ? 121.246 146.014 132.686 1.00 78.36  ?  389  ARG   B CG    1 
ATOM   9092  C  CD    . ARG   B 1 389 ? 122.498 145.598 131.940 1.00 79.58  ?  389  ARG   B CD    1 
ATOM   9093  N  NE    . ARG   B 1 389 ? 122.884 144.228 132.249 1.00 82.53  ?  389  ARG   B NE    1 
ATOM   9094  C  CZ    . ARG   B 1 389 ? 122.664 143.190 131.454 1.00 82.71  ?  389  ARG   B CZ    1 
ATOM   9095  N  NH1   . ARG   B 1 389 ? 122.059 143.330 130.286 1.00 79.09  ?  389  ARG   B NH1   1 
ATOM   9096  N  NH2   . ARG   B 1 389 ? 123.054 141.981 131.843 1.00 82.14  ?  389  ARG   B NH2   1 
ATOM   9097  N  N     . LYS   B 1 390 ? 118.278 147.485 133.617 1.00 72.06  ?  390  LYS   B N     1 
ATOM   9098  C  CA    . LYS   B 1 390 ? 116.900 147.023 133.608 1.00 70.91  ?  390  LYS   B CA    1 
ATOM   9099  C  C     . LYS   B 1 390 ? 116.344 147.166 132.202 1.00 76.06  ?  390  LYS   B C     1 
ATOM   9100  O  O     . LYS   B 1 390 ? 116.901 147.880 131.364 1.00 83.26  ?  390  LYS   B O     1 
ATOM   9101  C  CB    . LYS   B 1 390 ? 116.039 147.810 134.603 1.00 71.58  ?  390  LYS   B CB    1 
ATOM   9102  C  CG    . LYS   B 1 390 ? 115.442 149.083 134.025 1.00 73.76  ?  390  LYS   B CG    1 
ATOM   9103  C  CD    . LYS   B 1 390 ? 115.004 150.042 135.117 1.00 73.91  ?  390  LYS   B CD    1 
ATOM   9104  C  CE    . LYS   B 1 390 ? 116.189 150.561 135.903 1.00 74.87  ?  390  LYS   B CE    1 
ATOM   9105  N  NZ    . LYS   B 1 390 ? 115.791 151.052 137.247 1.00 80.22  ?  390  LYS   B NZ    1 
ATOM   9106  N  N     . GLN   B 1 391 ? 115.236 146.476 131.947 1.00 81.25  ?  391  GLN   B N     1 
ATOM   9107  C  CA    . GLN   B 1 391 ? 114.541 146.612 130.674 1.00 79.68  ?  391  GLN   B CA    1 
ATOM   9108  C  C     . GLN   B 1 391 ? 113.044 146.655 130.927 1.00 81.45  ?  391  GLN   B C     1 
ATOM   9109  O  O     . GLN   B 1 391 ? 112.517 145.832 131.677 1.00 82.80  ?  391  GLN   B O     1 
ATOM   9110  C  CB    . GLN   B 1 391 ? 114.886 145.461 129.724 1.00 80.81  ?  391  GLN   B CB    1 
ATOM   9111  C  CG    . GLN   B 1 391 ? 114.136 145.511 128.411 1.00 84.12  ?  391  GLN   B CG    1 
ATOM   9112  C  CD    . GLN   B 1 391 ? 114.086 144.171 127.710 1.00 91.56  ?  391  GLN   B CD    1 
ATOM   9113  O  OE1   . GLN   B 1 391 ? 114.999 143.357 127.847 1.00 94.94  ?  391  GLN   B OE1   1 
ATOM   9114  N  NE2   . GLN   B 1 391 ? 112.980 143.900 127.027 1.00 84.06  ?  391  GLN   B NE2   1 
ATOM   9115  N  N     . ARG   B 1 392 ? 112.360 147.605 130.302 1.00 85.56  ?  392  ARG   B N     1 
ATOM   9116  C  CA    . ARG   B 1 392 ? 110.922 147.759 130.467 1.00 83.76  ?  392  ARG   B CA    1 
ATOM   9117  C  C     . ARG   B 1 392 ? 110.200 147.102 129.300 1.00 84.81  ?  392  ARG   B C     1 
ATOM   9118  O  O     . ARG   B 1 392 ? 110.557 147.326 128.139 1.00 90.28  ?  392  ARG   B O     1 
ATOM   9119  C  CB    . ARG   B 1 392 ? 110.539 149.236 130.564 1.00 82.47  ?  392  ARG   B CB    1 
ATOM   9120  C  CG    . ARG   B 1 392 ? 110.197 149.692 131.970 1.00 86.20  ?  392  ARG   B CG    1 
ATOM   9121  C  CD    . ARG   B 1 392 ? 110.445 151.179 132.140 1.00 90.58  ?  392  ARG   B CD    1 
ATOM   9122  N  NE    . ARG   B 1 392 ? 110.817 151.513 133.509 1.00 94.06  ?  392  ARG   B NE    1 
ATOM   9123  C  CZ    . ARG   B 1 392 ? 112.005 151.980 133.870 1.00 93.80  ?  392  ARG   B CZ    1 
ATOM   9124  N  NH1   . ARG   B 1 392 ? 112.964 152.187 132.983 1.00 90.55  ?  392  ARG   B NH1   1 
ATOM   9125  N  NH2   . ARG   B 1 392 ? 112.231 152.258 135.150 1.00 92.81  ?  392  ARG   B NH2   1 
ATOM   9126  N  N     . VAL   B 1 393 ? 109.192 146.287 129.610 1.00 74.84  ?  393  VAL   B N     1 
ATOM   9127  C  CA    . VAL   B 1 393 ? 108.339 145.685 128.597 1.00 76.53  ?  393  VAL   B CA    1 
ATOM   9128  C  C     . VAL   B 1 393 ? 106.895 145.965 128.978 1.00 75.26  ?  393  VAL   B C     1 
ATOM   9129  O  O     . VAL   B 1 393 ? 106.588 146.327 130.113 1.00 81.19  ?  393  VAL   B O     1 
ATOM   9130  C  CB    . VAL   B 1 393 ? 108.569 144.166 128.444 1.00 70.98  ?  393  VAL   B CB    1 
ATOM   9131  C  CG1   . VAL   B 1 393 ? 109.942 143.894 127.864 1.00 75.99  ?  393  VAL   B CG1   1 
ATOM   9132  C  CG2   . VAL   B 1 393 ? 108.396 143.467 129.785 1.00 69.92  ?  393  VAL   B CG2   1 
ATOM   9133  N  N     . LYS   B 1 394 ? 106.006 145.818 128.005 1.00 73.46  ?  394  LYS   B N     1 
ATOM   9134  C  CA    . LYS   B 1 394 ? 104.583 145.938 128.280 1.00 70.32  ?  394  LYS   B CA    1 
ATOM   9135  C  C     . LYS   B 1 394 ? 104.098 144.665 128.958 1.00 73.11  ?  394  LYS   B C     1 
ATOM   9136  O  O     . LYS   B 1 394 ? 104.417 143.558 128.514 1.00 80.25  ?  394  LYS   B O     1 
ATOM   9137  C  CB    . LYS   B 1 394 ? 103.806 146.198 126.992 1.00 73.39  ?  394  LYS   B CB    1 
ATOM   9138  C  CG    . LYS   B 1 394 ? 104.143 147.527 126.341 1.00 76.18  ?  394  LYS   B CG    1 
ATOM   9139  C  CD    . LYS   B 1 394 ? 102.917 148.405 126.189 1.00 76.98  ?  394  LYS   B CD    1 
ATOM   9140  C  CE    . LYS   B 1 394 ? 102.977 149.180 124.883 1.00 79.14  ?  394  LYS   B CE    1 
ATOM   9141  N  NZ    . LYS   B 1 394 ? 104.376 149.600 124.580 1.00 84.54  ?  394  LYS   B NZ    1 
ATOM   9142  N  N     . ALA   B 1 395 ? 103.340 144.824 130.045 1.00 64.92  ?  395  ALA   B N     1 
ATOM   9143  C  CA    . ALA   B 1 395 ? 102.855 143.660 130.778 1.00 62.66  ?  395  ALA   B CA    1 
ATOM   9144  C  C     . ALA   B 1 395 ? 101.975 142.786 129.897 1.00 63.98  ?  395  ALA   B C     1 
ATOM   9145  O  O     . ALA   B 1 395 ? 102.071 141.553 129.936 1.00 73.47  ?  395  ALA   B O     1 
ATOM   9146  C  CB    . ALA   B 1 395 ? 102.096 144.105 132.027 1.00 62.31  ?  395  ALA   B CB    1 
ATOM   9147  N  N     . VAL   B 1 396 ? 101.119 143.410 129.086 1.00 63.57  ?  396  VAL   B N     1 
ATOM   9148  C  CA    . VAL   B 1 396 ? 100.265 142.645 128.185 1.00 63.86  ?  396  VAL   B CA    1 
ATOM   9149  C  C     . VAL   B 1 396 ? 101.109 141.900 127.158 1.00 65.67  ?  396  VAL   B C     1 
ATOM   9150  O  O     . VAL   B 1 396 ? 100.798 140.763 126.794 1.00 69.77  ?  396  VAL   B O     1 
ATOM   9151  C  CB    . VAL   B 1 396 ? 99.213  143.562 127.527 1.00 64.40  ?  396  VAL   B CB    1 
ATOM   9152  C  CG1   . VAL   B 1 396 ? 99.817  144.402 126.410 1.00 61.95  ?  396  VAL   B CG1   1 
ATOM   9153  C  CG2   . VAL   B 1 396 ? 98.051  142.741 127.008 1.00 66.37  ?  396  VAL   B CG2   1 
ATOM   9154  N  N     . GLU   B 1 397 ? 102.214 142.504 126.711 1.00 70.67  ?  397  GLU   B N     1 
ATOM   9155  C  CA    . GLU   B 1 397 ? 103.078 141.837 125.741 1.00 65.28  ?  397  GLU   B CA    1 
ATOM   9156  C  C     . GLU   B 1 397 ? 103.775 140.630 126.355 1.00 69.82  ?  397  GLU   B C     1 
ATOM   9157  O  O     . GLU   B 1 397 ? 103.834 139.560 125.738 1.00 76.00  ?  397  GLU   B O     1 
ATOM   9158  C  CB    . GLU   B 1 397 ? 104.103 142.824 125.185 1.00 69.60  ?  397  GLU   B CB    1 
ATOM   9159  C  CG    . GLU   B 1 397 ? 103.564 143.724 124.081 1.00 76.42  ?  397  GLU   B CG    1 
ATOM   9160  C  CD    . GLU   B 1 397 ? 104.671 144.434 123.323 1.00 84.26  ?  397  GLU   B CD    1 
ATOM   9161  O  OE1   . GLU   B 1 397 ? 105.807 143.915 123.294 1.00 82.35  ?  397  GLU   B OE1   1 
ATOM   9162  O  OE2   . GLU   B 1 397 ? 104.433 145.561 122.839 1.00 83.89  ?  397  GLU   B OE2   1 
ATOM   9163  N  N     . LEU   B 1 398 ? 104.312 140.784 127.569 1.00 61.38  ?  398  LEU   B N     1 
ATOM   9164  C  CA    . LEU   B 1 398 ? 104.973 139.664 128.233 1.00 53.57  ?  398  LEU   B CA    1 
ATOM   9165  C  C     . LEU   B 1 398 ? 103.993 138.532 128.506 1.00 58.81  ?  398  LEU   B C     1 
ATOM   9166  O  O     . LEU   B 1 398 ? 104.305 137.358 128.267 1.00 70.00  ?  398  LEU   B O     1 
ATOM   9167  C  CB    . LEU   B 1 398 ? 105.626 140.126 129.538 1.00 58.29  ?  398  LEU   B CB    1 
ATOM   9168  C  CG    . LEU   B 1 398 ? 106.707 139.228 130.144 1.00 62.66  ?  398  LEU   B CG    1 
ATOM   9169  C  CD1   . LEU   B 1 398 ? 107.588 138.672 129.040 1.00 61.53  ?  398  LEU   B CD1   1 
ATOM   9170  C  CD2   . LEU   B 1 398 ? 107.530 140.040 131.126 1.00 64.95  ?  398  LEU   B CD2   1 
ATOM   9171  N  N     . PHE   B 1 399 ? 102.798 138.865 129.000 1.00 56.27  ?  399  PHE   B N     1 
ATOM   9172  C  CA    . PHE   B 1 399 ? 101.812 137.827 129.277 1.00 48.67  ?  399  PHE   B CA    1 
ATOM   9173  C  C     . PHE   B 1 399 ? 101.332 137.162 127.993 1.00 56.78  ?  399  PHE   B C     1 
ATOM   9174  O  O     . PHE   B 1 399 ? 101.102 135.949 127.969 1.00 66.00  ?  399  PHE   B O     1 
ATOM   9175  C  CB    . PHE   B 1 399 ? 100.641 138.410 130.065 1.00 54.62  ?  399  PHE   B CB    1 
ATOM   9176  C  CG    . PHE   B 1 399 ? 100.839 138.375 131.554 1.00 56.58  ?  399  PHE   B CG    1 
ATOM   9177  C  CD1   . PHE   B 1 399 ? 100.463 137.264 132.289 1.00 58.96  ?  399  PHE   B CD1   1 
ATOM   9178  C  CD2   . PHE   B 1 399 ? 101.406 139.449 132.217 1.00 58.18  ?  399  PHE   B CD2   1 
ATOM   9179  C  CE1   . PHE   B 1 399 ? 100.647 137.227 133.658 1.00 58.73  ?  399  PHE   B CE1   1 
ATOM   9180  C  CE2   . PHE   B 1 399 ? 101.592 139.417 133.586 1.00 56.89  ?  399  PHE   B CE2   1 
ATOM   9181  C  CZ    . PHE   B 1 399 ? 101.211 138.305 134.306 1.00 55.24  ?  399  PHE   B CZ    1 
ATOM   9182  N  N     . SER   B 1 400 ? 101.185 137.933 126.912 1.00 62.49  ?  400  SER   B N     1 
ATOM   9183  C  CA    . SER   B 1 400 ? 100.803 137.349 125.634 1.00 57.33  ?  400  SER   B CA    1 
ATOM   9184  C  C     . SER   B 1 400 ? 101.871 136.394 125.123 1.00 64.43  ?  400  SER   B C     1 
ATOM   9185  O  O     . SER   B 1 400 ? 101.552 135.314 124.620 1.00 71.36  ?  400  SER   B O     1 
ATOM   9186  C  CB    . SER   B 1 400 ? 100.537 138.454 124.612 1.00 56.87  ?  400  SER   B CB    1 
ATOM   9187  O  OG    . SER   B 1 400 ? 99.480  139.298 125.031 1.00 70.24  ?  400  SER   B OG    1 
ATOM   9188  N  N     . LEU   B 1 401 ? 103.147 136.773 125.241 1.00 60.16  ?  401  LEU   B N     1 
ATOM   9189  C  CA    . LEU   B 1 401 ? 104.219 135.866 124.833 1.00 59.82  ?  401  LEU   B CA    1 
ATOM   9190  C  C     . LEU   B 1 401 ? 104.204 134.593 125.666 1.00 61.89  ?  401  LEU   B C     1 
ATOM   9191  O  O     . LEU   B 1 401 ? 104.341 133.485 125.128 1.00 69.23  ?  401  LEU   B O     1 
ATOM   9192  C  CB    . LEU   B 1 401 ? 105.580 136.554 124.948 1.00 61.18  ?  401  LEU   B CB    1 
ATOM   9193  C  CG    . LEU   B 1 401 ? 106.830 135.734 124.619 1.00 61.85  ?  401  LEU   B CG    1 
ATOM   9194  C  CD1   . LEU   B 1 401 ? 106.725 135.233 123.192 1.00 63.96  ?  401  LEU   B CD1   1 
ATOM   9195  C  CD2   . LEU   B 1 401 ? 108.029 136.648 124.765 1.00 62.26  ?  401  LEU   B CD2   1 
ATOM   9196  N  N     . MET   B 1 402 ? 104.028 134.732 126.982 1.00 67.11  ?  402  MET   B N     1 
ATOM   9197  C  CA    . MET   B 1 402 ? 104.015 133.562 127.852 1.00 63.39  ?  402  MET   B CA    1 
ATOM   9198  C  C     . MET   B 1 402 ? 102.855 132.634 127.515 1.00 67.10  ?  402  MET   B C     1 
ATOM   9199  O  O     . MET   B 1 402 ? 103.028 131.413 127.453 1.00 74.56  ?  402  MET   B O     1 
ATOM   9200  C  CB    . MET   B 1 402 ? 103.950 133.995 129.316 1.00 64.63  ?  402  MET   B CB    1 
ATOM   9201  C  CG    . MET   B 1 402 ? 103.988 132.837 130.304 1.00 67.23  ?  402  MET   B CG    1 
ATOM   9202  S  SD    . MET   B 1 402 ? 103.730 133.361 132.007 1.00 87.86  ?  402  MET   B SD    1 
ATOM   9203  C  CE    . MET   B 1 402 ? 102.077 134.027 131.924 1.00 69.64  ?  402  MET   B CE    1 
ATOM   9204  N  N     . MET   B 1 403 ? 101.665 133.193 127.281 1.00 63.04  ?  403  MET   B N     1 
ATOM   9205  C  CA    . MET   B 1 403 ? 100.517 132.353 126.958 1.00 58.25  ?  403  MET   B CA    1 
ATOM   9206  C  C     . MET   B 1 403 ? 100.626 131.757 125.560 1.00 63.03  ?  403  MET   B C     1 
ATOM   9207  O  O     . MET   B 1 403 ? 100.178 130.629 125.338 1.00 66.87  ?  403  MET   B O     1 
ATOM   9208  C  CB    . MET   B 1 403 ? 99.220  133.144 127.105 1.00 60.52  ?  403  MET   B CB    1 
ATOM   9209  C  CG    . MET   B 1 403 ? 98.741  133.304 128.542 1.00 65.64  ?  403  MET   B CG    1 
ATOM   9210  S  SD    . MET   B 1 403 ? 99.187  131.970 129.677 1.00 80.77  ?  403  MET   B SD    1 
ATOM   9211  C  CE    . MET   B 1 403 ? 97.625  131.113 129.865 1.00 69.25  ?  403  MET   B CE    1 
ATOM   9212  N  N     . GLN   B 1 404 ? 101.226 132.483 124.613 1.00 67.04  ?  404  GLN   B N     1 
ATOM   9213  C  CA    . GLN   B 1 404 ? 101.484 131.918 123.293 1.00 62.79  ?  404  GLN   B CA    1 
ATOM   9214  C  C     . GLN   B 1 404 ? 102.386 130.699 123.399 1.00 65.94  ?  404  GLN   B C     1 
ATOM   9215  O  O     . GLN   B 1 404 ? 102.119 129.655 122.791 1.00 70.92  ?  404  GLN   B O     1 
ATOM   9216  C  CB    . GLN   B 1 404 ? 102.124 132.971 122.383 1.00 59.11  ?  404  GLN   B CB    1 
ATOM   9217  C  CG    . GLN   B 1 404 ? 101.160 133.929 121.701 1.00 62.34  ?  404  GLN   B CG    1 
ATOM   9218  C  CD    . GLN   B 1 404 ? 100.412 133.294 120.548 1.00 73.03  ?  404  GLN   B CD    1 
ATOM   9219  O  OE1   . GLN   B 1 404 ? 100.735 132.189 120.113 1.00 77.79  ?  404  GLN   B OE1   1 
ATOM   9220  N  NE2   . GLN   B 1 404 ? 99.343  133.945 120.116 1.00 76.91  ?  404  GLN   B NE2   1 
ATOM   9221  N  N     . GLU   B 1 405 ? 103.461 130.812 124.182 1.00 68.47  ?  405  GLU   B N     1 
ATOM   9222  C  CA    . GLU   B 1 405 ? 104.377 129.686 124.331 1.00 61.60  ?  405  GLU   B CA    1 
ATOM   9223  C  C     . GLU   B 1 405 ? 103.735 128.541 125.101 1.00 62.65  ?  405  GLU   B C     1 
ATOM   9224  O  O     . GLU   B 1 405 ? 103.958 127.369 124.779 1.00 70.62  ?  405  GLU   B O     1 
ATOM   9225  C  CB    . GLU   B 1 405 ? 105.674 130.145 124.999 1.00 62.90  ?  405  GLU   B CB    1 
ATOM   9226  C  CG    . GLU   B 1 405 ? 106.521 131.081 124.133 1.00 70.32  ?  405  GLU   B CG    1 
ATOM   9227  C  CD    . GLU   B 1 405 ? 106.203 130.930 122.652 1.00 86.07  ?  405  GLU   B CD    1 
ATOM   9228  O  OE1   . GLU   B 1 405 ? 105.864 131.941 122.001 1.00 86.43  ?  405  GLU   B OE1   1 
ATOM   9229  O  OE2   . GLU   B 1 405 ? 106.274 129.796 122.136 1.00 87.46  ?  405  GLU   B OE2   1 
ATOM   9230  N  N     . ARG   B 1 406 ? 102.929 128.862 126.114 1.00 51.24  ?  406  ARG   B N     1 
ATOM   9231  C  CA    . ARG   B 1 406 ? 102.228 127.827 126.861 1.00 44.89  ?  406  ARG   B CA    1 
ATOM   9232  C  C     . ARG   B 1 406 ? 101.216 127.093 125.991 1.00 53.12  ?  406  ARG   B C     1 
ATOM   9233  O  O     . ARG   B 1 406 ? 100.998 125.894 126.177 1.00 57.26  ?  406  ARG   B O     1 
ATOM   9234  C  CB    . ARG   B 1 406 ? 101.541 128.437 128.083 1.00 43.77  ?  406  ARG   B CB    1 
ATOM   9235  C  CG    . ARG   B 1 406 ? 100.810 127.430 128.956 1.00 41.11  ?  406  ARG   B CG    1 
ATOM   9236  C  CD    . ARG   B 1 406 ? 100.073 128.105 130.099 1.00 41.61  ?  406  ARG   B CD    1 
ATOM   9237  N  NE    . ARG   B 1 406 ? 99.112  127.211 130.735 1.00 43.45  ?  406  ARG   B NE    1 
ATOM   9238  C  CZ    . ARG   B 1 406 ? 99.432  126.238 131.576 1.00 44.11  ?  406  ARG   B CZ    1 
ATOM   9239  N  NH1   . ARG   B 1 406 ? 100.688 126.003 131.916 1.00 48.95  ?  406  ARG   B NH1   1 
ATOM   9240  N  NH2   . ARG   B 1 406 ? 98.471  125.458 132.058 1.00 45.37  ?  406  ARG   B NH2   1 
ATOM   9241  N  N     . ALA   B 1 407 ? 100.583 127.791 125.049 1.00 56.57  ?  407  ALA   B N     1 
ATOM   9242  C  CA    . ALA   B 1 407 ? 99.651  127.127 124.147 1.00 48.71  ?  407  ALA   B CA    1 
ATOM   9243  C  C     . ALA   B 1 407 ? 100.380 126.299 123.099 1.00 57.17  ?  407  ALA   B C     1 
ATOM   9244  O  O     . ALA   B 1 407 ? 99.963  125.177 122.790 1.00 70.47  ?  407  ALA   B O     1 
ATOM   9245  C  CB    . ALA   B 1 407 ? 98.743  128.158 123.481 1.00 49.47  ?  407  ALA   B CB    1 
ATOM   9246  N  N     . SER   B 1 408 ? 101.477 126.823 122.553 1.00 63.38  ?  408  SER   B N     1 
ATOM   9247  C  CA    . SER   B 1 408 ? 102.153 126.137 121.458 1.00 57.56  ?  408  SER   B CA    1 
ATOM   9248  C  C     . SER   B 1 408 ? 102.938 124.924 121.944 1.00 62.28  ?  408  SER   B C     1 
ATOM   9249  O  O     . SER   B 1 408 ? 102.999 123.906 121.247 1.00 70.48  ?  408  SER   B O     1 
ATOM   9250  C  CB    . SER   B 1 408 ? 103.066 127.111 120.716 1.00 61.00  ?  408  SER   B CB    1 
ATOM   9251  O  OG    . SER   B 1 408 ? 104.102 127.577 121.554 1.00 75.20  ?  408  SER   B OG    1 
ATOM   9252  N  N     . THR   B 1 409 ? 103.545 125.006 123.127 1.00 58.20  ?  409  THR   B N     1 
ATOM   9253  C  CA    . THR   B 1 409 ? 104.312 123.887 123.654 1.00 52.38  ?  409  THR   B CA    1 
ATOM   9254  C  C     . THR   B 1 409 ? 103.578 123.103 124.733 1.00 54.38  ?  409  THR   B C     1 
ATOM   9255  O  O     . THR   B 1 409 ? 103.949 121.957 125.000 1.00 63.22  ?  409  THR   B O     1 
ATOM   9256  C  CB    . THR   B 1 409 ? 105.651 124.370 124.225 1.00 53.78  ?  409  THR   B CB    1 
ATOM   9257  O  OG1   . THR   B 1 409 ? 105.461 124.818 125.571 1.00 60.60  ?  409  THR   B OG1   1 
ATOM   9258  C  CG2   . THR   B 1 409 ? 106.236 125.491 123.387 1.00 57.20  ?  409  THR   B CG2   1 
ATOM   9259  N  N     . GLY   B 1 410 ? 102.565 123.691 125.365 1.00 53.55  ?  410  GLY   B N     1 
ATOM   9260  C  CA    . GLY   B 1 410 ? 101.810 122.996 126.387 1.00 49.71  ?  410  GLY   B CA    1 
ATOM   9261  C  C     . GLY   B 1 410 ? 102.563 122.716 127.664 1.00 56.83  ?  410  GLY   B C     1 
ATOM   9262  O  O     . GLY   B 1 410 ? 102.037 122.017 128.534 1.00 64.41  ?  410  GLY   B O     1 
ATOM   9263  N  N     . ARG   B 1 411 ? 103.783 123.241 127.808 1.00 49.16  ?  411  ARG   B N     1 
ATOM   9264  C  CA    . ARG   B 1 411 ? 104.641 122.879 128.928 1.00 47.12  ?  411  ARG   B CA    1 
ATOM   9265  C  C     . ARG   B 1 411 ? 105.356 124.094 129.508 1.00 53.49  ?  411  ARG   B C     1 
ATOM   9266  O  O     . ARG   B 1 411 ? 106.490 123.982 129.985 1.00 57.06  ?  411  ARG   B O     1 
ATOM   9267  C  CB    . ARG   B 1 411 ? 105.656 121.813 128.510 1.00 42.63  ?  411  ARG   B CB    1 
ATOM   9268  C  CG    . ARG   B 1 411 ? 105.018 120.507 128.054 1.00 41.83  ?  411  ARG   B CG    1 
ATOM   9269  C  CD    . ARG   B 1 411 ? 105.968 119.687 127.209 1.00 55.62  ?  411  ARG   B CD    1 
ATOM   9270  N  NE    . ARG   B 1 411 ? 106.987 119.034 128.021 1.00 64.67  ?  411  ARG   B NE    1 
ATOM   9271  C  CZ    . ARG   B 1 411 ? 106.988 117.743 128.318 1.00 63.04  ?  411  ARG   B CZ    1 
ATOM   9272  N  NH1   . ARG   B 1 411 ? 106.041 116.933 127.878 1.00 65.49  ?  411  ARG   B NH1   1 
ATOM   9273  N  NH2   . ARG   B 1 411 ? 107.943 117.259 129.105 1.00 63.62  ?  411  ARG   B NH2   1 
ATOM   9274  N  N     . ILE   B 1 412 ? 104.718 125.258 129.467 1.00 51.40  ?  412  ILE   B N     1 
ATOM   9275  C  CA    . ILE   B 1 412 ? 105.189 126.450 130.160 1.00 39.64  ?  412  ILE   B CA    1 
ATOM   9276  C  C     . ILE   B 1 412 ? 104.267 126.639 131.357 1.00 49.85  ?  412  ILE   B C     1 
ATOM   9277  O  O     . ILE   B 1 412 ? 103.184 127.222 131.239 1.00 66.86  ?  412  ILE   B O     1 
ATOM   9278  C  CB    . ILE   B 1 412 ? 105.199 127.685 129.253 1.00 43.79  ?  412  ILE   B CB    1 
ATOM   9279  C  CG1   . ILE   B 1 412 ? 106.045 127.425 128.006 1.00 46.98  ?  412  ILE   B CG1   1 
ATOM   9280  C  CG2   . ILE   B 1 412 ? 105.728 128.894 130.006 1.00 41.11  ?  412  ILE   B CG2   1 
ATOM   9281  C  CD1   . ILE   B 1 412 ? 107.496 127.131 128.302 1.00 45.46  ?  412  ILE   B CD1   1 
ATOM   9282  N  N     . TYR   B 1 413 ? 104.688 126.135 132.512 1.00 48.93  ?  413  TYR   B N     1 
ATOM   9283  C  CA    . TYR   B 1 413 ? 103.847 126.117 133.694 1.00 37.86  ?  413  TYR   B CA    1 
ATOM   9284  C  C     . TYR   B 1 413 ? 103.928 127.444 134.440 1.00 39.80  ?  413  TYR   B C     1 
ATOM   9285  O  O     . TYR   B 1 413 ? 104.837 128.250 134.235 1.00 55.17  ?  413  TYR   B O     1 
ATOM   9286  C  CB    . TYR   B 1 413 ? 104.255 124.966 134.609 1.00 41.73  ?  413  TYR   B CB    1 
ATOM   9287  C  CG    . TYR   B 1 413 ? 104.519 123.688 133.852 1.00 54.26  ?  413  TYR   B CG    1 
ATOM   9288  C  CD1   . TYR   B 1 413 ? 103.583 123.181 132.964 1.00 50.13  ?  413  TYR   B CD1   1 
ATOM   9289  C  CD2   . TYR   B 1 413 ? 105.710 123.000 134.008 1.00 52.80  ?  413  TYR   B CD2   1 
ATOM   9290  C  CE1   . TYR   B 1 413 ? 103.821 122.019 132.264 1.00 43.90  ?  413  TYR   B CE1   1 
ATOM   9291  C  CE2   . TYR   B 1 413 ? 105.955 121.836 133.315 1.00 49.72  ?  413  TYR   B CE2   1 
ATOM   9292  C  CZ    . TYR   B 1 413 ? 105.009 121.351 132.443 1.00 47.99  ?  413  TYR   B CZ    1 
ATOM   9293  O  OH    . TYR   B 1 413 ? 105.257 120.192 131.750 1.00 62.53  ?  413  TYR   B OH    1 
ATOM   9294  N  N     . ILE   B 1 414 ? 102.956 127.658 135.320 1.00 48.52  ?  414  ILE   B N     1 
ATOM   9295  C  CA    . ILE   B 1 414 ? 102.845 128.877 136.108 1.00 43.28  ?  414  ILE   B CA    1 
ATOM   9296  C  C     . ILE   B 1 414 ? 102.952 128.511 137.579 1.00 45.38  ?  414  ILE   B C     1 
ATOM   9297  O  O     . ILE   B 1 414 ? 102.428 127.478 138.008 1.00 50.99  ?  414  ILE   B O     1 
ATOM   9298  C  CB    . ILE   B 1 414 ? 101.517 129.614 135.831 1.00 43.55  ?  414  ILE   B CB    1 
ATOM   9299  C  CG1   . ILE   B 1 414 ? 101.230 129.663 134.330 1.00 41.19  ?  414  ILE   B CG1   1 
ATOM   9300  C  CG2   . ILE   B 1 414 ? 101.544 131.010 136.426 1.00 43.63  ?  414  ILE   B CG2   1 
ATOM   9301  C  CD1   . ILE   B 1 414 ? 102.153 130.571 133.563 1.00 42.95  ?  414  ILE   B CD1   1 
ATOM   9302  N  N     . GLN   B 1 415 ? 103.644 129.348 138.348 1.00 58.75  ?  415  GLN   B N     1 
ATOM   9303  C  CA    . GLN   B 1 415 ? 103.678 129.229 139.800 1.00 56.03  ?  415  GLN   B CA    1 
ATOM   9304  C  C     . GLN   B 1 415 ? 103.401 130.594 140.407 1.00 63.18  ?  415  GLN   B C     1 
ATOM   9305  O  O     . GLN   B 1 415 ? 104.168 131.538 140.194 1.00 70.95  ?  415  GLN   B O     1 
ATOM   9306  C  CB    . GLN   B 1 415 ? 105.023 128.688 140.294 1.00 52.70  ?  415  GLN   B CB    1 
ATOM   9307  C  CG    . GLN   B 1 415 ? 105.069 128.495 141.807 1.00 56.35  ?  415  GLN   B CG    1 
ATOM   9308  C  CD    . GLN   B 1 415 ? 106.385 127.928 142.293 1.00 68.32  ?  415  GLN   B CD    1 
ATOM   9309  O  OE1   . GLN   B 1 415 ? 107.457 128.399 141.917 1.00 75.01  ?  415  GLN   B OE1   1 
ATOM   9310  N  NE2   . GLN   B 1 415 ? 106.311 126.881 143.103 1.00 72.38  ?  415  GLN   B NE2   1 
ATOM   9311  N  N     . ASN   B 1 416 ? 102.309 130.694 141.160 1.00 59.26  ?  416  ASN   B N     1 
ATOM   9312  C  CA    . ASN   B 1 416 ? 101.979 131.908 141.900 1.00 50.65  ?  416  ASN   B CA    1 
ATOM   9313  C  C     . ASN   B 1 416 ? 102.724 131.853 143.225 1.00 54.28  ?  416  ASN   B C     1 
ATOM   9314  O  O     . ASN   B 1 416 ? 102.293 131.192 144.171 1.00 63.40  ?  416  ASN   B O     1 
ATOM   9315  C  CB    . ASN   B 1 416 ? 100.474 132.027 142.097 1.00 50.78  ?  416  ASN   B CB    1 
ATOM   9316  C  CG    . ASN   B 1 416 ? 99.716  132.031 140.784 1.00 58.21  ?  416  ASN   B CG    1 
ATOM   9317  O  OD1   . ASN   B 1 416 ? 100.089 132.728 139.843 1.00 63.47  ?  416  ASN   B OD1   1 
ATOM   9318  N  ND2   . ASN   B 1 416 ? 98.649  131.247 140.714 1.00 57.53  ?  416  ASN   B ND2   1 
ATOM   9319  N  N     . VAL   B 1 417 ? 103.859 132.548 143.287 1.00 61.70  ?  417  VAL   B N     1 
ATOM   9320  C  CA    . VAL   B 1 417 ? 104.760 132.411 144.424 1.00 59.59  ?  417  VAL   B CA    1 
ATOM   9321  C  C     . VAL   B 1 417 ? 104.143 132.973 145.698 1.00 65.29  ?  417  VAL   B C     1 
ATOM   9322  O  O     . VAL   B 1 417 ? 104.393 132.456 146.794 1.00 76.52  ?  417  VAL   B O     1 
ATOM   9323  C  CB    . VAL   B 1 417 ? 106.107 133.079 144.105 1.00 59.08  ?  417  VAL   B CB    1 
ATOM   9324  C  CG1   . VAL   B 1 417 ? 106.939 132.203 143.199 1.00 59.18  ?  417  VAL   B CG1   1 
ATOM   9325  C  CG2   . VAL   B 1 417 ? 105.900 134.454 143.484 1.00 66.28  ?  417  VAL   B CG2   1 
ATOM   9326  N  N     . ASP   B 1 418 ? 103.349 134.039 145.589 1.00 67.22  ?  418  ASP   B N     1 
ATOM   9327  C  CA    . ASP   B 1 418 ? 102.700 134.589 146.773 1.00 66.32  ?  418  ASP   B CA    1 
ATOM   9328  C  C     . ASP   B 1 418 ? 101.738 133.581 147.392 1.00 73.63  ?  418  ASP   B C     1 
ATOM   9329  O  O     . ASP   B 1 418 ? 101.707 133.413 148.616 1.00 83.34  ?  418  ASP   B O     1 
ATOM   9330  C  CB    . ASP   B 1 418 ? 101.982 135.892 146.416 1.00 67.02  ?  418  ASP   B CB    1 
ATOM   9331  C  CG    . ASP   B 1 418 ? 101.043 135.739 145.242 1.00 79.97  ?  418  ASP   B CG    1 
ATOM   9332  O  OD1   . ASP   B 1 418 ? 100.992 134.636 144.665 1.00 84.68  ?  418  ASP   B OD1   1 
ATOM   9333  O  OD2   . ASP   B 1 418 ? 100.266 136.678 144.978 1.00 86.02  ?  418  ASP   B OD2   1 
ATOM   9334  N  N     . HIS   B 1 419 ? 100.955 132.887 146.563 1.00 66.76  ?  419  HIS   B N     1 
ATOM   9335  C  CA    . HIS   B 1 419 ? 100.051 131.869 147.087 1.00 62.77  ?  419  HIS   B CA    1 
ATOM   9336  C  C     . HIS   B 1 419 ? 100.815 130.688 147.668 1.00 64.72  ?  419  HIS   B C     1 
ATOM   9337  O  O     . HIS   B 1 419 ? 100.344 130.052 148.618 1.00 69.51  ?  419  HIS   B O     1 
ATOM   9338  C  CB    . HIS   B 1 419 ? 99.099  131.388 145.993 1.00 58.77  ?  419  HIS   B CB    1 
ATOM   9339  C  CG    . HIS   B 1 419 ? 98.071  132.400 145.599 1.00 64.32  ?  419  HIS   B CG    1 
ATOM   9340  N  ND1   . HIS   B 1 419 ? 97.409  133.182 146.519 1.00 69.36  ?  419  HIS   B ND1   1 
ATOM   9341  C  CD2   . HIS   B 1 419 ? 97.587  132.755 144.386 1.00 66.58  ?  419  HIS   B CD2   1 
ATOM   9342  C  CE1   . HIS   B 1 419 ? 96.564  133.978 145.890 1.00 69.76  ?  419  HIS   B CE1   1 
ATOM   9343  N  NE2   . HIS   B 1 419 ? 96.656  133.742 144.594 1.00 69.50  ?  419  HIS   B NE2   1 
ATOM   9344  N  N     . CYS   B 1 420 ? 101.987 130.381 147.114 1.00 66.12  ?  420  CYS   B N     1 
ATOM   9345  C  CA    . CYS   B 1 420 ? 102.789 129.261 147.586 1.00 63.65  ?  420  CYS   B CA    1 
ATOM   9346  C  C     . CYS   B 1 420 ? 103.412 129.512 148.953 1.00 69.41  ?  420  CYS   B C     1 
ATOM   9347  O  O     . CYS   B 1 420 ? 103.947 128.572 149.550 1.00 79.53  ?  420  CYS   B O     1 
ATOM   9348  C  CB    . CYS   B 1 420 ? 103.879 128.945 146.560 1.00 66.75  ?  420  CYS   B CB    1 
ATOM   9349  S  SG    . CYS   B 1 420 ? 103.480 127.557 145.472 1.00 92.72  ?  420  CYS   B SG    1 
ATOM   9350  N  N     . ASN   B 1 421 ? 103.361 130.741 149.458 1.00 65.23  ?  421  ASN   B N     1 
ATOM   9351  C  CA    . ASN   B 1 421 ? 103.988 131.084 150.728 1.00 60.90  ?  421  ASN   B CA    1 
ATOM   9352  C  C     . ASN   B 1 421 ? 103.001 131.533 151.792 1.00 62.03  ?  421  ASN   B C     1 
ATOM   9353  O  O     . ASN   B 1 421 ? 103.147 131.150 152.955 1.00 73.57  ?  421  ASN   B O     1 
ATOM   9354  C  CB    . ASN   B 1 421 ? 105.043 132.175 150.513 1.00 52.61  ?  421  ASN   B CB    1 
ATOM   9355  C  CG    . ASN   B 1 421 ? 106.339 131.627 149.956 1.00 59.30  ?  421  ASN   B CG    1 
ATOM   9356  O  OD1   . ASN   B 1 421 ? 107.121 131.004 150.672 1.00 65.59  ?  421  ASN   B OD1   1 
ATOM   9357  N  ND2   . ASN   B 1 421 ? 106.574 131.857 148.672 1.00 55.44  ?  421  ASN   B ND2   1 
ATOM   9358  N  N     . THR   B 1 422 ? 102.002 132.342 151.433 1.00 64.45  ?  422  THR   B N     1 
ATOM   9359  C  CA    . THR   B 1 422 ? 100.995 132.733 152.414 1.00 66.26  ?  422  THR   B CA    1 
ATOM   9360  C  C     . THR   B 1 422 ? 100.152 131.539 152.846 1.00 67.37  ?  422  THR   B C     1 
ATOM   9361  O  O     . THR   B 1 422 ? 99.886  131.358 154.040 1.00 74.18  ?  422  THR   B O     1 
ATOM   9362  C  CB    . THR   B 1 422 ? 100.103 133.841 151.853 1.00 62.42  ?  422  THR   B CB    1 
ATOM   9363  O  OG1   . THR   B 1 422 ? 99.224  133.298 150.862 1.00 68.53  ?  422  THR   B OG1   1 
ATOM   9364  C  CG2   . THR   B 1 422 ? 100.940 134.958 151.245 1.00 61.75  ?  422  THR   B CG2   1 
ATOM   9365  N  N     . HIS   B 1 423 ? 99.722  130.718 151.894 1.00 62.56  ?  423  HIS   B N     1 
ATOM   9366  C  CA    . HIS   B 1 423 ? 98.985  129.490 152.194 1.00 61.27  ?  423  HIS   B CA    1 
ATOM   9367  C  C     . HIS   B 1 423 ? 99.927  128.287 152.163 1.00 63.81  ?  423  HIS   B C     1 
ATOM   9368  O  O     . HIS   B 1 423 ? 99.813  127.385 151.337 1.00 72.23  ?  423  HIS   B O     1 
ATOM   9369  C  CB    . HIS   B 1 423 ? 97.824  129.319 151.216 1.00 61.07  ?  423  HIS   B CB    1 
ATOM   9370  C  CG    . HIS   B 1 423 ? 96.956  128.136 151.509 1.00 64.66  ?  423  HIS   B CG    1 
ATOM   9371  N  ND1   . HIS   B 1 423 ? 96.252  128.003 152.685 1.00 68.14  ?  423  HIS   B ND1   1 
ATOM   9372  C  CD2   . HIS   B 1 423 ? 96.672  127.035 150.774 1.00 64.22  ?  423  HIS   B CD2   1 
ATOM   9373  C  CE1   . HIS   B 1 423 ? 95.575  126.870 152.664 1.00 61.26  ?  423  HIS   B CE1   1 
ATOM   9374  N  NE2   . HIS   B 1 423 ? 95.834  126.250 151.528 1.00 63.29  ?  423  HIS   B NE2   1 
ATOM   9375  N  N     . SER   B 1 424 ? 100.879 128.289 153.088 1.00 62.54  ?  424  SER   B N     1 
ATOM   9376  C  CA    . SER   B 1 424 ? 101.909 127.266 153.138 1.00 62.54  ?  424  SER   B CA    1 
ATOM   9377  C  C     . SER   B 1 424 ? 102.035 126.717 154.548 1.00 64.02  ?  424  SER   B C     1 
ATOM   9378  O  O     . SER   B 1 424 ? 101.818 127.442 155.523 1.00 64.07  ?  424  SER   B O     1 
ATOM   9379  C  CB    . SER   B 1 424 ? 103.269 127.822 152.694 1.00 67.89  ?  424  SER   B CB    1 
ATOM   9380  O  OG    . SER   B 1 424 ? 104.254 126.810 152.767 1.00 68.94  ?  424  SER   B OG    1 
ATOM   9381  N  N     . PRO   B 1 425 ? 102.382 125.434 154.689 1.00 63.26  ?  425  PRO   B N     1 
ATOM   9382  C  CA    . PRO   B 1 425 ? 102.714 124.914 156.024 1.00 57.57  ?  425  PRO   B CA    1 
ATOM   9383  C  C     . PRO   B 1 425 ? 103.979 125.513 156.608 1.00 60.54  ?  425  PRO   B C     1 
ATOM   9384  O  O     . PRO   B 1 425 ? 104.171 125.438 157.827 1.00 74.66  ?  425  PRO   B O     1 
ATOM   9385  C  CB    . PRO   B 1 425 ? 102.874 123.408 155.781 1.00 55.97  ?  425  PRO   B CB    1 
ATOM   9386  C  CG    . PRO   B 1 425 ? 103.256 123.320 154.349 1.00 59.57  ?  425  PRO   B CG    1 
ATOM   9387  C  CD    . PRO   B 1 425 ? 102.446 124.379 153.666 1.00 65.53  ?  425  PRO   B CD    1 
ATOM   9388  N  N     . PHE   B 1 426 ? 104.841 126.107 155.791 1.00 59.46  ?  426  PHE   B N     1 
ATOM   9389  C  CA    . PHE   B 1 426 ? 106.122 126.631 156.238 1.00 64.10  ?  426  PHE   B CA    1 
ATOM   9390  C  C     . PHE   B 1 426 ? 106.052 128.138 156.457 1.00 71.88  ?  426  PHE   B C     1 
ATOM   9391  O  O     . PHE   B 1 426 ? 105.188 128.834 155.919 1.00 79.74  ?  426  PHE   B O     1 
ATOM   9392  C  CB    . PHE   B 1 426 ? 107.224 126.301 155.228 1.00 63.79  ?  426  PHE   B CB    1 
ATOM   9393  C  CG    . PHE   B 1 426 ? 107.421 124.832 155.011 1.00 69.63  ?  426  PHE   B CG    1 
ATOM   9394  C  CD1   . PHE   B 1 426 ? 108.250 124.100 155.843 1.00 70.19  ?  426  PHE   B CD1   1 
ATOM   9395  C  CD2   . PHE   B 1 426 ? 106.775 124.179 153.976 1.00 65.85  ?  426  PHE   B CD2   1 
ATOM   9396  C  CE1   . PHE   B 1 426 ? 108.440 122.750 155.636 1.00 69.83  ?  426  PHE   B CE1   1 
ATOM   9397  C  CE2   . PHE   B 1 426 ? 106.959 122.829 153.772 1.00 69.82  ?  426  PHE   B CE2   1 
ATOM   9398  C  CZ    . PHE   B 1 426 ? 107.764 122.108 154.626 1.00 72.41  ?  426  PHE   B CZ    1 
ATOM   9399  N  N     . ASP   B 1 427 ? 106.989 128.635 157.262 1.00 87.41  ?  427  ASP   B N     1 
ATOM   9400  C  CA    . ASP   B 1 427 ? 107.071 130.057 157.560 1.00 88.83  ?  427  ASP   B CA    1 
ATOM   9401  C  C     . ASP   B 1 427 ? 107.946 130.744 156.521 1.00 89.85  ?  427  ASP   B C     1 
ATOM   9402  O  O     . ASP   B 1 427 ? 109.128 130.397 156.399 1.00 88.86  ?  427  ASP   B O     1 
ATOM   9403  C  CB    . ASP   B 1 427 ? 107.640 130.279 158.951 1.00 89.84  ?  427  ASP   B CB    1 
ATOM   9404  C  CG    . ASP   B 1 427 ? 107.330 131.658 159.495 1.00 94.06  ?  427  ASP   B CG    1 
ATOM   9405  O  OD1   . ASP   B 1 427 ? 106.464 132.345 158.917 1.00 92.51  ?  427  ASP   B OD1   1 
ATOM   9406  O  OD2   . ASP   B 1 427 ? 107.956 132.060 160.498 1.00 95.75  ?  427  ASP   B OD2   1 
ATOM   9407  N  N     . PRO   B 1 428 ? 107.417 131.699 155.752 1.00 73.93  ?  428  PRO   B N     1 
ATOM   9408  C  CA    . PRO   B 1 428 ? 108.237 132.350 154.716 1.00 71.75  ?  428  PRO   B CA    1 
ATOM   9409  C  C     . PRO   B 1 428 ? 109.495 133.008 155.250 1.00 77.96  ?  428  PRO   B C     1 
ATOM   9410  O  O     . PRO   B 1 428 ? 110.520 133.017 154.558 1.00 78.08  ?  428  PRO   B O     1 
ATOM   9411  C  CB    . PRO   B 1 428 ? 107.280 133.388 154.117 1.00 71.51  ?  428  PRO   B CB    1 
ATOM   9412  C  CG    . PRO   B 1 428 ? 105.923 132.857 154.379 1.00 74.35  ?  428  PRO   B CG    1 
ATOM   9413  C  CD    . PRO   B 1 428 ? 105.988 132.033 155.631 1.00 74.39  ?  428  PRO   B CD    1 
ATOM   9414  N  N     . ALA   B 1 429 ? 109.444 133.571 156.457 1.00 80.59  ?  429  ALA   B N     1 
ATOM   9415  C  CA    . ALA   B 1 429 ? 110.616 134.234 157.014 1.00 75.91  ?  429  ALA   B CA    1 
ATOM   9416  C  C     . ALA   B 1 429 ? 111.751 133.249 157.257 1.00 83.04  ?  429  ALA   B C     1 
ATOM   9417  O  O     . ALA   B 1 429 ? 112.920 133.560 156.999 1.00 85.17  ?  429  ALA   B O     1 
ATOM   9418  C  CB    . ALA   B 1 429 ? 110.238 134.949 158.308 1.00 73.55  ?  429  ALA   B CB    1 
ATOM   9419  N  N     . ILE   B 1 430 ? 111.429 132.058 157.750 1.00 88.18  ?  430  ILE   B N     1 
ATOM   9420  C  CA    . ILE   B 1 430 ? 112.446 131.063 158.065 1.00 85.48  ?  430  ILE   B CA    1 
ATOM   9421  C  C     . ILE   B 1 430 ? 112.703 130.132 156.885 1.00 87.41  ?  430  ILE   B C     1 
ATOM   9422  O  O     . ILE   B 1 430 ? 113.844 129.970 156.444 1.00 89.28  ?  430  ILE   B O     1 
ATOM   9423  C  CB    . ILE   B 1 430 ? 112.033 130.278 159.328 1.00 81.86  ?  430  ILE   B CB    1 
ATOM   9424  C  CG1   . ILE   B 1 430 ? 111.214 131.163 160.274 1.00 87.01  ?  430  ILE   B CG1   1 
ATOM   9425  C  CG2   . ILE   B 1 430 ? 113.261 129.766 160.047 1.00 82.94  ?  430  ILE   B CG2   1 
ATOM   9426  C  CD1   . ILE   B 1 430 ? 110.813 130.447 161.542 1.00 87.06  ?  430  ILE   B CD1   1 
ATOM   9427  N  N     . ALA   B 1 431 ? 111.652 129.515 156.348 1.00 72.02  ?  431  ALA   B N     1 
ATOM   9428  C  CA    . ALA   B 1 431 ? 111.772 128.492 155.310 1.00 67.30  ?  431  ALA   B CA    1 
ATOM   9429  C  C     . ALA   B 1 431 ? 110.829 128.818 154.159 1.00 70.46  ?  431  ALA   B C     1 
ATOM   9430  O  O     . ALA   B 1 431 ? 109.756 128.214 154.028 1.00 77.26  ?  431  ALA   B O     1 
ATOM   9431  C  CB    . ALA   B 1 431 ? 111.486 127.103 155.881 1.00 68.29  ?  431  ALA   B CB    1 
ATOM   9432  N  N     . PRO   B 1 432 ? 111.199 129.765 153.303 1.00 65.08  ?  432  PRO   B N     1 
ATOM   9433  C  CA    . PRO   B 1 432 ? 110.334 130.119 152.175 1.00 61.31  ?  432  PRO   B CA    1 
ATOM   9434  C  C     . PRO   B 1 432 ? 110.342 129.046 151.097 1.00 64.56  ?  432  PRO   B C     1 
ATOM   9435  O  O     . PRO   B 1 432 ? 111.285 128.266 150.955 1.00 72.38  ?  432  PRO   B O     1 
ATOM   9436  C  CB    . PRO   B 1 432 ? 110.946 131.423 151.658 1.00 60.39  ?  432  PRO   B CB    1 
ATOM   9437  C  CG    . PRO   B 1 432 ? 112.389 131.303 152.004 1.00 60.52  ?  432  PRO   B CG    1 
ATOM   9438  C  CD    . PRO   B 1 432 ? 112.451 130.541 153.305 1.00 65.02  ?  432  PRO   B CD    1 
ATOM   9439  N  N     . VAL   B 1 433 ? 109.262 129.020 150.324 1.00 58.93  ?  433  VAL   B N     1 
ATOM   9440  C  CA    . VAL   B 1 433 ? 109.140 128.146 149.164 1.00 57.45  ?  433  VAL   B CA    1 
ATOM   9441  C  C     . VAL   B 1 433 ? 109.491 128.961 147.928 1.00 60.05  ?  433  VAL   B C     1 
ATOM   9442  O  O     . VAL   B 1 433 ? 108.851 129.981 147.645 1.00 67.83  ?  433  VAL   B O     1 
ATOM   9443  C  CB    . VAL   B 1 433 ? 107.728 127.551 149.052 1.00 54.46  ?  433  VAL   B CB    1 
ATOM   9444  C  CG1   . VAL   B 1 433 ? 107.574 126.745 147.783 1.00 60.06  ?  433  VAL   B CG1   1 
ATOM   9445  C  CG2   . VAL   B 1 433 ? 107.410 126.687 150.261 1.00 54.68  ?  433  VAL   B CG2   1 
ATOM   9446  N  N     . ARG   B 1 434 ? 110.497 128.507 147.186 1.00 55.02  ?  434  ARG   B N     1 
ATOM   9447  C  CA    . ARG   B 1 434 ? 111.020 129.256 146.056 1.00 54.50  ?  434  ARG   B CA    1 
ATOM   9448  C  C     . ARG   B 1 434 ? 110.902 128.528 144.726 1.00 61.38  ?  434  ARG   B C     1 
ATOM   9449  O  O     . ARG   B 1 434 ? 111.397 129.043 143.717 1.00 73.46  ?  434  ARG   B O     1 
ATOM   9450  C  CB    . ARG   B 1 434 ? 112.492 129.616 146.299 1.00 59.41  ?  434  ARG   B CB    1 
ATOM   9451  C  CG    . ARG   B 1 434 ? 112.710 130.692 147.343 1.00 61.42  ?  434  ARG   B CG    1 
ATOM   9452  C  CD    . ARG   B 1 434 ? 113.999 131.449 147.081 1.00 66.77  ?  434  ARG   B CD    1 
ATOM   9453  N  NE    . ARG   B 1 434 ? 114.587 131.972 148.307 1.00 68.83  ?  434  ARG   B NE    1 
ATOM   9454  C  CZ    . ARG   B 1 434 ? 115.232 131.238 149.202 1.00 69.03  ?  434  ARG   B CZ    1 
ATOM   9455  N  NH1   . ARG   B 1 434 ? 115.398 129.936 149.039 1.00 67.11  ?  434  ARG   B NH1   1 
ATOM   9456  N  NH2   . ARG   B 1 434 ? 115.723 131.826 150.289 1.00 68.58  ?  434  ARG   B NH2   1 
ATOM   9457  N  N     . GLN   B 1 435 ? 110.268 127.362 144.685 1.00 57.28  ?  435  GLN   B N     1 
ATOM   9458  C  CA    . GLN   B 1 435 ? 110.226 126.554 143.470 1.00 58.32  ?  435  GLN   B CA    1 
ATOM   9459  C  C     . GLN   B 1 435 ? 109.216 125.432 143.669 1.00 63.19  ?  435  GLN   B C     1 
ATOM   9460  O  O     . GLN   B 1 435 ? 108.538 125.351 144.698 1.00 69.08  ?  435  GLN   B O     1 
ATOM   9461  C  CB    . GLN   B 1 435 ? 111.605 125.987 143.131 1.00 55.01  ?  435  GLN   B CB    1 
ATOM   9462  C  CG    . GLN   B 1 435 ? 112.075 124.928 144.124 1.00 57.48  ?  435  GLN   B CG    1 
ATOM   9463  C  CD    . GLN   B 1 435 ? 113.296 124.178 143.645 1.00 63.45  ?  435  GLN   B CD    1 
ATOM   9464  O  OE1   . GLN   B 1 435 ? 114.420 124.502 144.019 1.00 69.89  ?  435  GLN   B OE1   1 
ATOM   9465  N  NE2   . GLN   B 1 435 ? 113.088 123.220 142.752 1.00 66.96  ?  435  GLN   B NE2   1 
ATOM   9466  N  N     . SER   B 1 436 ? 109.129 124.559 142.669 1.00 56.14  ?  436  SER   B N     1 
ATOM   9467  C  CA    . SER   B 1 436 ? 108.284 123.376 142.732 1.00 50.59  ?  436  SER   B CA    1 
ATOM   9468  C  C     . SER   B 1 436 ? 109.046 122.207 142.113 1.00 53.27  ?  436  SER   B C     1 
ATOM   9469  O  O     . SER   B 1 436 ? 110.234 122.313 141.793 1.00 62.80  ?  436  SER   B O     1 
ATOM   9470  C  CB    . SER   B 1 436 ? 106.940 123.627 142.039 1.00 54.12  ?  436  SER   B CB    1 
ATOM   9471  O  OG    . SER   B 1 436 ? 105.997 122.633 142.393 1.00 66.28  ?  436  SER   B OG    1 
ATOM   9472  N  N     . ASN   B 1 437 ? 108.354 121.082 141.949 1.00 54.34  ?  437  ASN   B N     1 
ATOM   9473  C  CA    . ASN   B 1 437 ? 108.938 119.860 141.415 1.00 53.42  ?  437  ASN   B CA    1 
ATOM   9474  C  C     . ASN   B 1 437 ? 108.733 119.785 139.902 1.00 56.33  ?  437  ASN   B C     1 
ATOM   9475  O  O     . ASN   B 1 437 ? 108.382 120.770 139.250 1.00 60.90  ?  437  ASN   B O     1 
ATOM   9476  C  CB    . ASN   B 1 437 ? 108.346 118.642 142.116 1.00 53.55  ?  437  ASN   B CB    1 
ATOM   9477  C  CG    . ASN   B 1 437 ? 106.850 118.531 141.927 1.00 60.26  ?  437  ASN   B CG    1 
ATOM   9478  O  OD1   . ASN   B 1 437 ? 106.151 119.535 141.805 1.00 71.30  ?  437  ASN   B OD1   1 
ATOM   9479  N  ND2   . ASN   B 1 437 ? 106.348 117.306 141.908 1.00 57.35  ?  437  ASN   B ND2   1 
ATOM   9480  N  N     . LEU   B 1 438 ? 108.968 118.600 139.326 1.00 59.25  ?  438  LEU   B N     1 
ATOM   9481  C  CA    . LEU   B 1 438 ? 108.792 118.421 137.887 1.00 57.58  ?  438  LEU   B CA    1 
ATOM   9482  C  C     . LEU   B 1 438 ? 107.339 118.621 137.472 1.00 59.69  ?  438  LEU   B C     1 
ATOM   9483  O  O     . LEU   B 1 438 ? 107.061 119.261 136.452 1.00 64.23  ?  438  LEU   B O     1 
ATOM   9484  C  CB    . LEU   B 1 438 ? 109.286 117.037 137.457 1.00 55.44  ?  438  LEU   B CB    1 
ATOM   9485  C  CG    . LEU   B 1 438 ? 108.922 116.583 136.036 1.00 55.31  ?  438  LEU   B CG    1 
ATOM   9486  C  CD1   . LEU   B 1 438 ? 109.781 117.275 135.004 1.00 55.09  ?  438  LEU   B CD1   1 
ATOM   9487  C  CD2   . LEU   B 1 438 ? 109.055 115.083 135.877 1.00 54.75  ?  438  LEU   B CD2   1 
ATOM   9488  N  N     . CYS   B 1 439 ? 106.397 118.090 138.248 1.00 65.52  ?  439  CYS   B N     1 
ATOM   9489  C  CA    . CYS   B 1 439 ? 104.984 118.132 137.896 1.00 59.37  ?  439  CYS   B CA    1 
ATOM   9490  C  C     . CYS   B 1 439 ? 104.199 119.186 138.673 1.00 64.73  ?  439  CYS   B C     1 
ATOM   9491  O  O     . CYS   B 1 439 ? 102.965 119.138 138.683 1.00 67.32  ?  439  CYS   B O     1 
ATOM   9492  C  CB    . CYS   B 1 439 ? 104.354 116.757 138.101 1.00 53.42  ?  439  CYS   B CB    1 
ATOM   9493  S  SG    . CYS   B 1 439 ? 104.972 115.457 137.009 1.00 80.39  ?  439  CYS   B SG    1 
ATOM   9494  N  N     . LEU   B 1 440 ? 104.887 120.119 139.332 1.00 61.72  ?  440  LEU   B N     1 
ATOM   9495  C  CA    . LEU   B 1 440 ? 104.269 121.323 139.897 1.00 57.07  ?  440  LEU   B CA    1 
ATOM   9496  C  C     . LEU   B 1 440 ? 103.224 120.995 140.963 1.00 54.36  ?  440  LEU   B C     1 
ATOM   9497  O  O     . LEU   B 1 440 ? 102.184 121.649 141.057 1.00 64.33  ?  440  LEU   B O     1 
ATOM   9498  C  CB    . LEU   B 1 440 ? 103.654 122.190 138.794 1.00 58.90  ?  440  LEU   B CB    1 
ATOM   9499  C  CG    . LEU   B 1 440 ? 104.549 123.172 138.032 1.00 60.29  ?  440  LEU   B CG    1 
ATOM   9500  C  CD1   . LEU   B 1 440 ? 104.979 124.306 138.936 1.00 66.41  ?  440  LEU   B CD1   1 
ATOM   9501  C  CD2   . LEU   B 1 440 ? 105.758 122.485 137.423 1.00 63.91  ?  440  LEU   B CD2   1 
ATOM   9502  N  N     . GLU   B 1 441 ? 103.500 119.981 141.782 1.00 61.60  ?  441  GLU   B N     1 
ATOM   9503  C  CA    . GLU   B 1 441 ? 102.642 119.656 142.910 1.00 59.34  ?  441  GLU   B CA    1 
ATOM   9504  C  C     . GLU   B 1 441 ? 103.360 119.695 144.249 1.00 65.89  ?  441  GLU   B C     1 
ATOM   9505  O  O     . GLU   B 1 441 ? 102.697 119.613 145.288 1.00 71.08  ?  441  GLU   B O     1 
ATOM   9506  C  CB    . GLU   B 1 441 ? 102.007 118.268 142.725 1.00 57.15  ?  441  GLU   B CB    1 
ATOM   9507  C  CG    . GLU   B 1 441 ? 102.828 117.119 143.294 1.00 67.25  ?  441  GLU   B CG    1 
ATOM   9508  C  CD    . GLU   B 1 441 ? 103.673 116.422 142.243 1.00 78.48  ?  441  GLU   B CD    1 
ATOM   9509  O  OE1   . GLU   B 1 441 ? 104.013 117.078 141.236 1.00 81.07  ?  441  GLU   B OE1   1 
ATOM   9510  O  OE2   . GLU   B 1 441 ? 104.008 115.228 142.427 1.00 80.89  ?  441  GLU   B OE2   1 
ATOM   9511  N  N     . ILE   B 1 442 ? 104.683 119.828 144.257 1.00 64.41  ?  442  ILE   B N     1 
ATOM   9512  C  CA    . ILE   B 1 442 ? 105.488 119.793 145.472 1.00 61.91  ?  442  ILE   B CA    1 
ATOM   9513  C  C     . ILE   B 1 442 ? 106.042 121.185 145.715 1.00 62.57  ?  442  ILE   B C     1 
ATOM   9514  O  O     . ILE   B 1 442 ? 106.628 121.789 144.811 1.00 75.40  ?  442  ILE   B O     1 
ATOM   9515  C  CB    . ILE   B 1 442 ? 106.618 118.759 145.353 1.00 64.62  ?  442  ILE   B CB    1 
ATOM   9516  C  CG1   . ILE   B 1 442 ? 106.013 117.365 145.260 1.00 56.19  ?  442  ILE   B CG1   1 
ATOM   9517  C  CG2   . ILE   B 1 442 ? 107.606 118.863 146.505 1.00 67.13  ?  442  ILE   B CG2   1 
ATOM   9518  C  CD1   . ILE   B 1 442 ? 105.029 117.035 146.343 1.00 57.12  ?  442  ILE   B CD1   1 
ATOM   9519  N  N     . ALA   B 1 443 ? 105.856 121.696 146.930 1.00 63.63  ?  443  ALA   B N     1 
ATOM   9520  C  CA    . ALA   B 1 443 ? 106.302 123.040 147.301 1.00 66.72  ?  443  ALA   B CA    1 
ATOM   9521  C  C     . ALA   B 1 443 ? 107.028 122.950 148.640 1.00 70.37  ?  443  ALA   B C     1 
ATOM   9522  O  O     . ALA   B 1 443 ? 106.393 122.989 149.695 1.00 76.92  ?  443  ALA   B O     1 
ATOM   9523  C  CB    . ALA   B 1 443 ? 105.124 124.007 147.364 1.00 65.90  ?  443  ALA   B CB    1 
ATOM   9524  N  N     . LEU   B 1 444 ? 108.353 122.835 148.598 1.00 62.39  ?  444  LEU   B N     1 
ATOM   9525  C  CA    . LEU   B 1 444 ? 109.152 122.649 149.800 1.00 57.90  ?  444  LEU   B CA    1 
ATOM   9526  C  C     . LEU   B 1 444 ? 110.325 123.615 149.826 1.00 61.36  ?  444  LEU   B C     1 
ATOM   9527  O  O     . LEU   B 1 444 ? 110.840 124.005 148.776 1.00 66.59  ?  444  LEU   B O     1 
ATOM   9528  C  CB    . LEU   B 1 444 ? 109.698 121.218 149.902 1.00 52.70  ?  444  LEU   B CB    1 
ATOM   9529  C  CG    . LEU   B 1 444 ? 108.642 120.117 149.879 1.00 57.74  ?  444  LEU   B CG    1 
ATOM   9530  C  CD1   . LEU   B 1 444 ? 109.196 118.708 149.855 1.00 62.76  ?  444  LEU   B CD1   1 
ATOM   9531  C  CD2   . LEU   B 1 444 ? 107.632 120.250 151.019 1.00 54.87  ?  444  LEU   B CD2   1 
ATOM   9532  N  N     . PRO   B 1 445 ? 110.760 124.017 151.018 1.00 59.33  ?  445  PRO   B N     1 
ATOM   9533  C  CA    . PRO   B 1 445 ? 111.935 124.888 151.129 1.00 54.26  ?  445  PRO   B CA    1 
ATOM   9534  C  C     . PRO   B 1 445 ? 113.193 124.218 150.607 1.00 60.92  ?  445  PRO   B C     1 
ATOM   9535  O  O     . PRO   B 1 445 ? 113.380 123.006 150.731 1.00 73.37  ?  445  PRO   B O     1 
ATOM   9536  C  CB    . PRO   B 1 445 ? 112.039 125.153 152.634 1.00 52.43  ?  445  PRO   B CB    1 
ATOM   9537  C  CG    . PRO   B 1 445 ? 110.666 124.957 153.144 1.00 52.60  ?  445  PRO   B CG    1 
ATOM   9538  C  CD    . PRO   B 1 445 ? 109.998 123.943 152.273 1.00 56.26  ?  445  PRO   B CD    1 
ATOM   9539  N  N     . THR   B 1 446 ? 114.071 125.033 150.031 1.00 63.49  ?  446  THR   B N     1 
ATOM   9540  C  CA    . THR   B 1 446 ? 115.356 124.569 149.540 1.00 66.58  ?  446  THR   B CA    1 
ATOM   9541  C  C     . THR   B 1 446 ? 116.424 125.603 149.865 1.00 67.54  ?  446  THR   B C     1 
ATOM   9542  O  O     . THR   B 1 446 ? 116.130 126.777 150.094 1.00 75.24  ?  446  THR   B O     1 
ATOM   9543  C  CB    . THR   B 1 446 ? 115.339 124.311 148.025 1.00 67.87  ?  446  THR   B CB    1 
ATOM   9544  O  OG1   . THR   B 1 446 ? 114.807 125.446 147.328 1.00 74.46  ?  446  THR   B OG1   1 
ATOM   9545  C  CG2   . THR   B 1 446 ? 114.545 123.067 147.669 1.00 60.29  ?  446  THR   B CG2   1 
ATOM   9546  N  N     . LYS   B 1 447 ? 117.676 125.149 149.891 1.00 77.65  ?  447  LYS   B N     1 
ATOM   9547  C  CA    . LYS   B 1 447 ? 118.821 126.029 150.058 1.00 75.87  ?  447  LYS   B CA    1 
ATOM   9548  C  C     . LYS   B 1 447 ? 119.868 125.707 149.002 1.00 81.26  ?  447  LYS   B C     1 
ATOM   9549  O  O     . LYS   B 1 447 ? 120.128 124.530 148.725 1.00 85.94  ?  447  LYS   B O     1 
ATOM   9550  C  CB    . LYS   B 1 447 ? 119.436 125.890 151.458 1.00 77.18  ?  447  LYS   B CB    1 
ATOM   9551  C  CG    . LYS   B 1 447 ? 118.825 126.803 152.506 1.00 80.72  ?  447  LYS   B CG    1 
ATOM   9552  C  CD    . LYS   B 1 447 ? 118.750 126.106 153.854 1.00 86.96  ?  447  LYS   B CD    1 
ATOM   9553  C  CE    . LYS   B 1 447 ? 118.212 127.034 154.931 1.00 88.54  ?  447  LYS   B CE    1 
ATOM   9554  N  NZ    . LYS   B 1 447 ? 118.625 128.446 154.721 1.00 85.95  ?  447  LYS   B NZ    1 
ATOM   9555  N  N     . PRO   B 1 448 ? 120.469 126.722 148.382 1.00 71.80  ?  448  PRO   B N     1 
ATOM   9556  C  CA    . PRO   B 1 448 ? 121.505 126.465 147.374 1.00 71.22  ?  448  PRO   B CA    1 
ATOM   9557  C  C     . PRO   B 1 448 ? 122.705 125.738 147.961 1.00 72.12  ?  448  PRO   B C     1 
ATOM   9558  O  O     . PRO   B 1 448 ? 123.051 125.903 149.132 1.00 78.85  ?  448  PRO   B O     1 
ATOM   9559  C  CB    . PRO   B 1 448 ? 121.888 127.870 146.898 1.00 65.77  ?  448  PRO   B CB    1 
ATOM   9560  C  CG    . PRO   B 1 448 ? 121.405 128.765 148.000 1.00 74.84  ?  448  PRO   B CG    1 
ATOM   9561  C  CD    . PRO   B 1 448 ? 120.144 128.152 148.462 1.00 70.33  ?  448  PRO   B CD    1 
ATOM   9562  N  N     . LEU   B 1 449 ? 123.342 124.928 147.121 1.00 73.54  ?  449  LEU   B N     1 
ATOM   9563  C  CA    . LEU   B 1 449 ? 124.523 124.162 147.487 1.00 78.18  ?  449  LEU   B CA    1 
ATOM   9564  C  C     . LEU   B 1 449 ? 125.754 124.761 146.824 1.00 83.01  ?  449  LEU   B C     1 
ATOM   9565  O  O     . LEU   B 1 449 ? 125.704 125.163 145.659 1.00 88.78  ?  449  LEU   B O     1 
ATOM   9566  C  CB    . LEU   B 1 449 ? 124.385 122.701 147.055 1.00 78.26  ?  449  LEU   B CB    1 
ATOM   9567  C  CG    . LEU   B 1 449 ? 123.752 121.720 148.037 1.00 80.03  ?  449  LEU   B CG    1 
ATOM   9568  C  CD1   . LEU   B 1 449 ? 122.255 121.931 148.148 1.00 83.00  ?  449  LEU   B CD1   1 
ATOM   9569  C  CD2   . LEU   B 1 449 ? 124.069 120.276 147.680 1.00 78.11  ?  449  LEU   B CD2   1 
ATOM   9570  N  N     . ASN   B 1 450 ? 126.857 124.822 147.568 1.00 92.02  ?  450  ASN   B N     1 
ATOM   9571  C  CA    . ASN   B 1 450 ? 128.138 125.224 147.005 1.00 91.02  ?  450  ASN   B CA    1 
ATOM   9572  C  C     . ASN   B 1 450 ? 129.029 124.038 146.656 1.00 93.76  ?  450  ASN   B C     1 
ATOM   9573  O  O     . ASN   B 1 450 ? 130.048 124.224 145.985 1.00 95.51  ?  450  ASN   B O     1 
ATOM   9574  C  CB    . ASN   B 1 450 ? 128.879 126.161 147.971 1.00 89.85  ?  450  ASN   B CB    1 
ATOM   9575  C  CG    . ASN   B 1 450 ? 129.176 125.512 149.309 1.00 96.63  ?  450  ASN   B CG    1 
ATOM   9576  O  OD1   . ASN   B 1 450 ? 129.956 124.563 149.396 1.00 96.99  ?  450  ASN   B OD1   1 
ATOM   9577  N  ND2   . ASN   B 1 450 ? 128.558 126.027 150.364 1.00 96.64  ?  450  ASN   B ND2   1 
ATOM   9578  N  N     . ASP   B 1 451 ? 128.670 122.833 147.092 1.00 97.06  ?  451  ASP   B N     1 
ATOM   9579  C  CA    . ASP   B 1 451 ? 129.411 121.623 146.773 1.00 94.41  ?  451  ASP   B CA    1 
ATOM   9580  C  C     . ASP   B 1 451 ? 128.446 120.451 146.898 1.00 96.43  ?  451  ASP   B C     1 
ATOM   9581  O  O     . ASP   B 1 451 ? 127.475 120.513 147.656 1.00 101.96 ?  451  ASP   B O     1 
ATOM   9582  C  CB    . ASP   B 1 451 ? 130.641 121.457 147.691 1.00 98.21  ?  451  ASP   B CB    1 
ATOM   9583  C  CG    . ASP   B 1 451 ? 131.322 120.109 147.513 1.00 104.20 ?  451  ASP   B CG    1 
ATOM   9584  O  OD1   . ASP   B 1 451 ? 131.822 119.838 146.402 1.00 103.39 ?  451  ASP   B OD1   1 
ATOM   9585  O  OD2   . ASP   B 1 451 ? 131.215 119.270 148.429 1.00 106.37 ?  451  ASP   B OD2   1 
ATOM   9586  N  N     . VAL   B 1 452 ? 128.710 119.387 146.134 1.00 87.15  ?  452  VAL   B N     1 
ATOM   9587  C  CA    . VAL   B 1 452 ? 127.834 118.221 146.171 1.00 87.19  ?  452  VAL   B CA    1 
ATOM   9588  C  C     . VAL   B 1 452 ? 127.853 117.549 147.537 1.00 87.79  ?  452  VAL   B C     1 
ATOM   9589  O  O     . VAL   B 1 452 ? 126.943 116.778 147.859 1.00 91.61  ?  452  VAL   B O     1 
ATOM   9590  C  CB    . VAL   B 1 452 ? 128.211 117.225 145.054 1.00 88.59  ?  452  VAL   B CB    1 
ATOM   9591  C  CG1   . VAL   B 1 452 ? 129.389 116.365 145.473 1.00 85.23  ?  452  VAL   B CG1   1 
ATOM   9592  C  CG2   . VAL   B 1 452 ? 127.011 116.366 144.682 1.00 87.57  ?  452  VAL   B CG2   1 
ATOM   9593  N  N     . ASN   B 1 453 ? 128.868 117.823 148.355 1.00 93.26  ?  453  ASN   B N     1 
ATOM   9594  C  CA    . ASN   B 1 453 ? 128.931 117.320 149.720 1.00 94.33  ?  453  ASN   B CA    1 
ATOM   9595  C  C     . ASN   B 1 453 ? 128.833 118.434 150.756 1.00 96.47  ?  453  ASN   B C     1 
ATOM   9596  O  O     . ASN   B 1 453 ? 129.141 118.205 151.930 1.00 99.95  ?  453  ASN   B O     1 
ATOM   9597  C  CB    . ASN   B 1 453 ? 130.215 116.516 149.926 1.00 94.41  ?  453  ASN   B CB    1 
ATOM   9598  C  CG    . ASN   B 1 453 ? 130.134 115.129 149.322 1.00 95.71  ?  453  ASN   B CG    1 
ATOM   9599  O  OD1   . ASN   B 1 453 ? 129.148 114.417 149.507 1.00 98.39  ?  453  ASN   B OD1   1 
ATOM   9600  N  ND2   . ASN   B 1 453 ? 131.176 114.736 148.600 1.00 97.09  ?  453  ASN   B ND2   1 
ATOM   9601  N  N     . ASP   B 1 454 ? 128.417 119.630 150.349 1.00 102.98 ?  454  ASP   B N     1 
ATOM   9602  C  CA    . ASP   B 1 454 ? 128.261 120.736 151.284 1.00 103.74 ?  454  ASP   B CA    1 
ATOM   9603  C  C     . ASP   B 1 454 ? 127.101 120.462 152.235 1.00 106.92 ?  454  ASP   B C     1 
ATOM   9604  O  O     . ASP   B 1 454 ? 126.043 119.973 151.827 1.00 108.30 ?  454  ASP   B O     1 
ATOM   9605  C  CB    . ASP   B 1 454 ? 128.040 122.048 150.520 1.00 104.12 ?  454  ASP   B CB    1 
ATOM   9606  C  CG    . ASP   B 1 454 ? 127.505 123.158 151.408 1.00 109.29 ?  454  ASP   B CG    1 
ATOM   9607  O  OD1   . ASP   B 1 454 ? 127.997 123.300 152.547 1.00 108.57 ?  454  ASP   B OD1   1 
ATOM   9608  O  OD2   . ASP   B 1 454 ? 126.528 123.825 151.004 1.00 108.59 ?  454  ASP   B OD2   1 
ATOM   9609  N  N     . GLU   B 1 455 ? 127.307 120.775 153.514 1.00 105.32 ?  455  GLU   B N     1 
ATOM   9610  C  CA    . GLU   B 1 455 ? 126.289 120.538 154.528 1.00 102.88 ?  455  GLU   B CA    1 
ATOM   9611  C  C     . GLU   B 1 455 ? 125.416 121.753 154.807 1.00 102.77 ?  455  GLU   B C     1 
ATOM   9612  O  O     . GLU   B 1 455 ? 124.405 121.620 155.504 1.00 101.81 ?  455  GLU   B O     1 
ATOM   9613  C  CB    . GLU   B 1 455 ? 126.932 120.063 155.840 1.00 102.22 ?  455  GLU   B CB    1 
ATOM   9614  C  CG    . GLU   B 1 455 ? 127.351 118.582 155.875 1.00 106.88 ?  455  GLU   B CG    1 
ATOM   9615  C  CD    . GLU   B 1 455 ? 126.205 117.581 155.675 1.00 109.12 ?  455  GLU   B CD    1 
ATOM   9616  O  OE1   . GLU   B 1 455 ? 125.103 117.954 155.223 1.00 109.35 ?  455  GLU   B OE1   1 
ATOM   9617  O  OE2   . GLU   B 1 455 ? 126.424 116.387 155.964 1.00 109.51 ?  455  GLU   B OE2   1 
ATOM   9618  N  N     . ASN   B 1 456 ? 125.774 122.927 154.289 1.00 102.23 ?  456  ASN   B N     1 
ATOM   9619  C  CA    . ASN   B 1 456 ? 124.923 124.099 154.451 1.00 98.60  ?  456  ASN   B CA    1 
ATOM   9620  C  C     . ASN   B 1 456 ? 123.756 124.111 153.474 1.00 99.85  ?  456  ASN   B C     1 
ATOM   9621  O  O     . ASN   B 1 456 ? 122.789 124.848 153.695 1.00 102.74 ?  456  ASN   B O     1 
ATOM   9622  C  CB    . ASN   B 1 456 ? 125.746 125.377 154.287 1.00 102.94 ?  456  ASN   B CB    1 
ATOM   9623  C  CG    . ASN   B 1 456 ? 126.934 125.430 155.225 1.00 105.49 ?  456  ASN   B CG    1 
ATOM   9624  O  OD1   . ASN   B 1 456 ? 126.882 124.913 156.340 1.00 105.36 ?  456  ASN   B OD1   1 
ATOM   9625  N  ND2   . ASN   B 1 456 ? 128.012 126.065 154.779 1.00 104.22 ?  456  ASN   B ND2   1 
ATOM   9626  N  N     . GLY   B 1 457 ? 123.825 123.313 152.407 1.00 86.34  ?  457  GLY   B N     1 
ATOM   9627  C  CA    . GLY   B 1 457 ? 122.741 123.257 151.455 1.00 83.89  ?  457  GLY   B CA    1 
ATOM   9628  C  C     . GLY   B 1 457 ? 121.589 122.391 151.925 1.00 85.52  ?  457  GLY   B C     1 
ATOM   9629  O  O     . GLY   B 1 457 ? 121.719 121.567 152.827 1.00 90.72  ?  457  GLY   B O     1 
ATOM   9630  N  N     . GLU   B 1 458 ? 120.448 122.556 151.259 1.00 80.01  ?  458  GLU   B N     1 
ATOM   9631  C  CA    . GLU   B 1 458 ? 119.250 121.786 151.568 1.00 74.00  ?  458  GLU   B CA    1 
ATOM   9632  C  C     . GLU   B 1 458 ? 118.559 121.413 150.267 1.00 74.26  ?  458  GLU   B C     1 
ATOM   9633  O  O     . GLU   B 1 458 ? 118.088 122.292 149.539 1.00 79.79  ?  458  GLU   B O     1 
ATOM   9634  C  CB    . GLU   B 1 458 ? 118.304 122.577 152.475 1.00 77.36  ?  458  GLU   B CB    1 
ATOM   9635  C  CG    . GLU   B 1 458 ? 117.288 121.722 153.208 1.00 79.93  ?  458  GLU   B CG    1 
ATOM   9636  C  CD    . GLU   B 1 458 ? 115.968 122.437 153.416 1.00 87.85  ?  458  GLU   B CD    1 
ATOM   9637  O  OE1   . GLU   B 1 458 ? 115.986 123.610 153.843 1.00 88.60  ?  458  GLU   B OE1   1 
ATOM   9638  O  OE2   . GLU   B 1 458 ? 114.911 121.826 153.152 1.00 85.82  ?  458  GLU   B OE2   1 
ATOM   9639  N  N     . ILE   B 1 459 ? 118.499 120.118 149.975 1.00 63.74  ?  459  ILE   B N     1 
ATOM   9640  C  CA    . ILE   B 1 459 ? 117.787 119.597 148.816 1.00 65.26  ?  459  ILE   B CA    1 
ATOM   9641  C  C     . ILE   B 1 459 ? 116.498 118.961 149.311 1.00 70.15  ?  459  ILE   B C     1 
ATOM   9642  O  O     . ILE   B 1 459 ? 116.525 118.106 150.204 1.00 75.19  ?  459  ILE   B O     1 
ATOM   9643  C  CB    . ILE   B 1 459 ? 118.644 118.586 148.035 1.00 64.40  ?  459  ILE   B CB    1 
ATOM   9644  C  CG1   . ILE   B 1 459 ? 119.634 119.314 147.126 1.00 65.82  ?  459  ILE   B CG1   1 
ATOM   9645  C  CG2   . ILE   B 1 459 ? 117.767 117.657 147.221 1.00 63.79  ?  459  ILE   B CG2   1 
ATOM   9646  C  CD1   . ILE   B 1 459 ? 120.870 118.509 146.805 1.00 66.41  ?  459  ILE   B CD1   1 
ATOM   9647  N  N     . ALA   B 1 460 ? 115.371 119.379 148.742 1.00 59.13  ?  460  ALA   B N     1 
ATOM   9648  C  CA    . ALA   B 1 460 ? 114.078 118.908 149.219 1.00 52.49  ?  460  ALA   B CA    1 
ATOM   9649  C  C     . ALA   B 1 460 ? 113.733 117.570 148.580 1.00 54.51  ?  460  ALA   B C     1 
ATOM   9650  O  O     . ALA   B 1 460 ? 113.849 117.406 147.364 1.00 61.60  ?  460  ALA   B O     1 
ATOM   9651  C  CB    . ALA   B 1 460 ? 112.990 119.937 148.920 1.00 53.47  ?  460  ALA   B CB    1 
ATOM   9652  N  N     . LEU   B 1 461 ? 113.309 116.613 149.399 1.00 54.10  ?  461  LEU   B N     1 
ATOM   9653  C  CA    . LEU   B 1 461 ? 112.913 115.293 148.930 1.00 54.80  ?  461  LEU   B CA    1 
ATOM   9654  C  C     . LEU   B 1 461 ? 111.465 115.046 149.319 1.00 61.88  ?  461  LEU   B C     1 
ATOM   9655  O  O     . LEU   B 1 461 ? 111.080 115.287 150.467 1.00 76.01  ?  461  LEU   B O     1 
ATOM   9656  C  CB    . LEU   B 1 461 ? 113.806 114.198 149.522 1.00 58.57  ?  461  LEU   B CB    1 
ATOM   9657  C  CG    . LEU   B 1 461 ? 115.241 114.084 149.012 1.00 59.58  ?  461  LEU   B CG    1 
ATOM   9658  C  CD1   . LEU   B 1 461 ? 115.714 112.651 149.131 1.00 61.11  ?  461  LEU   B CD1   1 
ATOM   9659  C  CD2   . LEU   B 1 461 ? 115.353 114.560 147.581 1.00 65.20  ?  461  LEU   B CD2   1 
ATOM   9660  N  N     . CYS   B 1 462 ? 110.660 114.573 148.372 1.00 67.44  ?  462  CYS   B N     1 
ATOM   9661  C  CA    . CYS   B 1 462 ? 109.285 114.209 148.682 1.00 68.63  ?  462  CYS   B CA    1 
ATOM   9662  C  C     . CYS   B 1 462 ? 108.976 112.819 148.151 1.00 72.72  ?  462  CYS   B C     1 
ATOM   9663  O  O     . CYS   B 1 462 ? 109.147 112.551 146.956 1.00 77.50  ?  462  CYS   B O     1 
ATOM   9664  C  CB    . CYS   B 1 462 ? 108.279 115.214 148.118 1.00 74.70  ?  462  CYS   B CB    1 
ATOM   9665  S  SG    . CYS   B 1 462 ? 106.719 115.173 149.030 1.00 83.67  ?  462  CYS   B SG    1 
ATOM   9666  N  N     . THR   B 1 463 ? 108.513 111.950 149.049 1.00 66.66  ?  463  THR   B N     1 
ATOM   9667  C  CA    . THR   B 1 463 ? 108.007 110.626 148.722 1.00 72.89  ?  463  THR   B CA    1 
ATOM   9668  C  C     . THR   B 1 463 ? 106.486 110.677 148.690 1.00 71.22  ?  463  THR   B C     1 
ATOM   9669  O  O     . THR   B 1 463 ? 105.862 111.328 149.533 1.00 67.52  ?  463  THR   B O     1 
ATOM   9670  C  CB    . THR   B 1 463 ? 108.478 109.589 149.744 1.00 71.78  ?  463  THR   B CB    1 
ATOM   9671  O  OG1   . THR   B 1 463 ? 107.692 109.702 150.937 1.00 75.86  ?  463  THR   B OG1   1 
ATOM   9672  C  CG2   . THR   B 1 463 ? 109.938 109.816 150.091 1.00 70.28  ?  463  THR   B CG2   1 
ATOM   9673  N  N     . LEU   B 1 464 ? 105.893 109.997 147.714 1.00 61.44  ?  464  LEU   B N     1 
ATOM   9674  C  CA    . LEU   B 1 464 ? 104.487 110.188 147.406 1.00 54.82  ?  464  LEU   B CA    1 
ATOM   9675  C  C     . LEU   B 1 464 ? 103.682 108.912 147.598 1.00 58.48  ?  464  LEU   B C     1 
ATOM   9676  O  O     . LEU   B 1 464 ? 104.220 107.807 147.706 1.00 67.07  ?  464  LEU   B O     1 
ATOM   9677  C  CB    . LEU   B 1 464 ? 104.297 110.688 145.971 1.00 50.63  ?  464  LEU   B CB    1 
ATOM   9678  C  CG    . LEU   B 1 464 ? 105.270 111.757 145.481 1.00 53.54  ?  464  LEU   B CG    1 
ATOM   9679  C  CD1   . LEU   B 1 464 ? 105.119 111.996 143.988 1.00 58.86  ?  464  LEU   B CD1   1 
ATOM   9680  C  CD2   . LEU   B 1 464 ? 105.111 113.055 146.253 1.00 60.76  ?  464  LEU   B CD2   1 
ATOM   9681  N  N     . SER   B 1 465 ? 102.369 109.108 147.651 1.00 63.20  ?  465  SER   B N     1 
ATOM   9682  C  CA    . SER   B 1 465 ? 101.383 108.036 147.673 1.00 58.38  ?  465  SER   B CA    1 
ATOM   9683  C  C     . SER   B 1 465 ? 100.044 108.648 147.277 1.00 63.35  ?  465  SER   B C     1 
ATOM   9684  O  O     . SER   B 1 465 ? 99.925  109.863 147.119 1.00 71.95  ?  465  SER   B O     1 
ATOM   9685  C  CB    . SER   B 1 465 ? 101.342 107.354 149.042 1.00 61.07  ?  465  SER   B CB    1 
ATOM   9686  O  OG    . SER   B 1 465 ? 102.287 106.299 149.074 1.00 67.35  ?  465  SER   B OG    1 
ATOM   9687  N  N     . ALA   B 1 466 ? 99.035  107.801 147.096 1.00 58.11  ?  466  ALA   B N     1 
ATOM   9688  C  CA    . ALA   B 1 466 ? 97.728  108.320 146.721 1.00 48.63  ?  466  ALA   B CA    1 
ATOM   9689  C  C     . ALA   B 1 466 ? 96.628  107.462 147.323 1.00 56.82  ?  466  ALA   B C     1 
ATOM   9690  O  O     . ALA   B 1 466 ? 96.805  106.264 147.541 1.00 66.14  ?  466  ALA   B O     1 
ATOM   9691  C  CB    . ALA   B 1 466 ? 97.563  108.386 145.198 1.00 49.24  ?  466  ALA   B CB    1 
ATOM   9692  N  N     . PHE   B 1 467 ? 95.486  108.091 147.577 1.00 60.72  ?  467  PHE   B N     1 
ATOM   9693  C  CA    . PHE   B 1 467 ? 94.272  107.397 147.983 1.00 55.64  ?  467  PHE   B CA    1 
ATOM   9694  C  C     . PHE   B 1 467 ? 93.409  107.143 146.757 1.00 58.88  ?  467  PHE   B C     1 
ATOM   9695  O  O     . PHE   B 1 467 ? 93.194  108.048 145.945 1.00 66.53  ?  467  PHE   B O     1 
ATOM   9696  C  CB    . PHE   B 1 467 ? 93.481  108.210 149.008 1.00 51.30  ?  467  PHE   B CB    1 
ATOM   9697  C  CG    . PHE   B 1 467 ? 94.172  108.365 150.325 1.00 56.30  ?  467  PHE   B CG    1 
ATOM   9698  C  CD1   . PHE   B 1 467 ? 94.786  107.287 150.934 1.00 61.03  ?  467  PHE   B CD1   1 
ATOM   9699  C  CD2   . PHE   B 1 467 ? 94.196  109.593 150.962 1.00 57.88  ?  467  PHE   B CD2   1 
ATOM   9700  C  CE1   . PHE   B 1 467 ? 95.419  107.432 152.150 1.00 64.15  ?  467  PHE   B CE1   1 
ATOM   9701  C  CE2   . PHE   B 1 467 ? 94.826  109.743 152.178 1.00 58.69  ?  467  PHE   B CE2   1 
ATOM   9702  C  CZ    . PHE   B 1 467 ? 95.438  108.662 152.772 1.00 59.18  ?  467  PHE   B CZ    1 
ATOM   9703  N  N     . ASN   B 1 468 ? 92.916  105.918 146.624 1.00 56.31  ?  468  ASN   B N     1 
ATOM   9704  C  CA    . ASN   B 1 468 ? 92.010  105.581 145.530 1.00 53.75  ?  468  ASN   B CA    1 
ATOM   9705  C  C     . ASN   B 1 468 ? 90.605  105.976 145.961 1.00 62.61  ?  468  ASN   B C     1 
ATOM   9706  O  O     . ASN   B 1 468 ? 89.946  105.258 146.715 1.00 68.84  ?  468  ASN   B O     1 
ATOM   9707  C  CB    . ASN   B 1 468 ? 92.114  104.100 145.182 1.00 53.42  ?  468  ASN   B CB    1 
ATOM   9708  C  CG    . ASN   B 1 468 ? 91.247  103.707 144.000 1.00 58.39  ?  468  ASN   B CG    1 
ATOM   9709  O  OD1   . ASN   B 1 468 ? 90.496  104.519 143.465 1.00 66.38  ?  468  ASN   B OD1   1 
ATOM   9710  N  ND2   . ASN   B 1 468 ? 91.267  102.426 143.662 1.00 60.59  ?  468  ASN   B ND2   1 
ATOM   9711  N  N     . LEU   B 1 469 ? 90.146  107.136 145.485 1.00 61.78  ?  469  LEU   B N     1 
ATOM   9712  C  CA    . LEU   B 1 469 ? 88.814  107.618 145.830 1.00 54.14  ?  469  LEU   B CA    1 
ATOM   9713  C  C     . LEU   B 1 469 ? 87.712  106.720 145.284 1.00 63.29  ?  469  LEU   B C     1 
ATOM   9714  O  O     . LEU   B 1 469 ? 86.592  106.750 145.804 1.00 70.59  ?  469  LEU   B O     1 
ATOM   9715  C  CB    . LEU   B 1 469 ? 88.628  109.049 145.317 1.00 58.86  ?  469  LEU   B CB    1 
ATOM   9716  C  CG    . LEU   B 1 469 ? 89.450  110.150 145.992 1.00 64.95  ?  469  LEU   B CG    1 
ATOM   9717  C  CD1   . LEU   B 1 469 ? 88.790  111.494 145.768 1.00 64.38  ?  469  LEU   B CD1   1 
ATOM   9718  C  CD2   . LEU   B 1 469 ? 89.568  109.871 147.482 1.00 65.83  ?  469  LEU   B CD2   1 
ATOM   9719  N  N     . GLY   B 1 470 ? 88.002  105.927 144.256 1.00 60.66  ?  470  GLY   B N     1 
ATOM   9720  C  CA    . GLY   B 1 470 ? 87.049  104.993 143.697 1.00 58.65  ?  470  GLY   B CA    1 
ATOM   9721  C  C     . GLY   B 1 470 ? 86.967  103.667 144.405 1.00 65.11  ?  470  GLY   B C     1 
ATOM   9722  O  O     . GLY   B 1 470 ? 86.308  102.745 143.919 1.00 77.09  ?  470  GLY   B O     1 
ATOM   9723  N  N     . ALA   B 1 471 ? 87.701  103.515 145.499 1.00 65.95  ?  471  ALA   B N     1 
ATOM   9724  C  CA    . ALA   B 1 471 ? 87.688  102.301 146.289 1.00 69.49  ?  471  ALA   B CA    1 
ATOM   9725  C  C     . ALA   B 1 471 ? 87.187  102.543 147.699 1.00 74.33  ?  471  ALA   B C     1 
ATOM   9726  O  O     . ALA   B 1 471 ? 87.025  101.580 148.456 1.00 78.74  ?  471  ALA   B O     1 
ATOM   9727  C  CB    . ALA   B 1 471 ? 89.092  101.680 146.338 1.00 66.16  ?  471  ALA   B CB    1 
ATOM   9728  N  N     . ILE   B 1 472 ? 86.940  103.797 148.069 1.00 78.07  ?  472  ILE   B N     1 
ATOM   9729  C  CA    . ILE   B 1 472 ? 86.411  104.158 149.378 1.00 76.14  ?  472  ILE   B CA    1 
ATOM   9730  C  C     . ILE   B 1 472 ? 84.905  104.339 149.242 1.00 82.50  ?  472  ILE   B C     1 
ATOM   9731  O  O     . ILE   B 1 472 ? 84.437  105.058 148.350 1.00 86.31  ?  472  ILE   B O     1 
ATOM   9732  C  CB    . ILE   B 1 472 ? 87.093  105.427 149.932 1.00 79.92  ?  472  ILE   B CB    1 
ATOM   9733  C  CG1   . ILE   B 1 472 ? 86.736  106.684 149.126 1.00 81.34  ?  472  ILE   B CG1   1 
ATOM   9734  C  CG2   . ILE   B 1 472 ? 88.605  105.244 149.984 1.00 80.18  ?  472  ILE   B CG2   1 
ATOM   9735  C  CD1   . ILE   B 1 472 ? 87.136  107.976 149.818 1.00 80.30  ?  472  ILE   B CD1   1 
ATOM   9736  N  N     . ASN   B 1 473 ? 84.138  103.642 150.088 1.00 100.93 ?  473  ASN   B N     1 
ATOM   9737  C  CA    . ASN   B 1 473 ? 82.685  103.766 150.084 1.00 102.65 ?  473  ASN   B CA    1 
ATOM   9738  C  C     . ASN   B 1 473 ? 82.213  104.838 151.043 1.00 101.38 ?  473  ASN   B C     1 
ATOM   9739  O  O     . ASN   B 1 473 ? 81.112  105.377 150.875 1.00 103.30 ?  473  ASN   B O     1 
ATOM   9740  C  CB    . ASN   B 1 473 ? 82.018  102.430 150.445 1.00 104.45 ?  473  ASN   B CB    1 
ATOM   9741  C  CG    . ASN   B 1 473 ? 82.149  101.395 149.345 1.00 105.02 ?  473  ASN   B CG    1 
ATOM   9742  O  OD1   . ASN   B 1 473 ? 81.456  101.458 148.332 1.00 103.67 ?  473  ASN   B OD1   1 
ATOM   9743  N  ND2   . ASN   B 1 473 ? 83.037  100.428 149.544 1.00 102.36 ?  473  ASN   B ND2   1 
ATOM   9744  N  N     . ASN   B 1 474 ? 83.039  105.162 152.030 1.00 92.05  ?  474  ASN   B N     1 
ATOM   9745  C  CA    . ASN   B 1 474 ? 82.761  106.218 152.982 1.00 90.16  ?  474  ASN   B CA    1 
ATOM   9746  C  C     . ASN   B 1 474 ? 84.054  106.962 153.278 1.00 90.96  ?  474  ASN   B C     1 
ATOM   9747  O  O     . ASN   B 1 474 ? 85.148  106.400 153.186 1.00 96.50  ?  474  ASN   B O     1 
ATOM   9748  C  CB    . ASN   B 1 474 ? 82.153  105.657 154.271 1.00 89.20  ?  474  ASN   B CB    1 
ATOM   9749  C  CG    . ASN   B 1 474 ? 81.571  106.737 155.153 1.00 96.34  ?  474  ASN   B CG    1 
ATOM   9750  O  OD1   . ASN   B 1 474 ? 80.906  107.655 154.672 1.00 100.83 ?  474  ASN   B OD1   1 
ATOM   9751  N  ND2   . ASN   B 1 474 ? 81.816  106.634 156.455 1.00 93.51  ?  474  ASN   B ND2   1 
ATOM   9752  N  N     . LEU   B 1 475 ? 83.916  108.242 153.630 1.00 79.05  ?  475  LEU   B N     1 
ATOM   9753  C  CA    . LEU   B 1 475 ? 85.093  109.052 153.925 1.00 79.82  ?  475  LEU   B CA    1 
ATOM   9754  C  C     . LEU   B 1 475 ? 85.777  108.612 155.210 1.00 85.97  ?  475  LEU   B C     1 
ATOM   9755  O  O     . LEU   B 1 475 ? 86.991  108.796 155.355 1.00 92.66  ?  475  LEU   B O     1 
ATOM   9756  C  CB    . LEU   B 1 475 ? 84.716  110.526 154.021 1.00 81.60  ?  475  LEU   B CB    1 
ATOM   9757  C  CG    . LEU   B 1 475 ? 84.376  111.192 152.690 1.00 82.25  ?  475  LEU   B CG    1 
ATOM   9758  C  CD1   . LEU   B 1 475 ? 84.087  112.674 152.826 1.00 78.04  ?  475  LEU   B CD1   1 
ATOM   9759  C  CD2   . LEU   B 1 475 ? 85.425  110.940 151.615 1.00 79.87  ?  475  LEU   B CD2   1 
ATOM   9760  N  N     . ASP   B 1 476 ? 85.024  108.036 156.150 1.00 92.27  ?  476  ASP   B N     1 
ATOM   9761  C  CA    . ASP   B 1 476 ? 85.622  107.555 157.390 1.00 91.16  ?  476  ASP   B CA    1 
ATOM   9762  C  C     . ASP   B 1 476 ? 86.638  106.450 157.145 1.00 92.21  ?  476  ASP   B C     1 
ATOM   9763  O  O     . ASP   B 1 476 ? 87.543  106.262 157.966 1.00 94.20  ?  476  ASP   B O     1 
ATOM   9764  C  CB    . ASP   B 1 476 ? 84.533  107.065 158.344 1.00 95.36  ?  476  ASP   B CB    1 
ATOM   9765  C  CG    . ASP   B 1 476 ? 83.633  108.187 158.823 1.00 101.35 ?  476  ASP   B CG    1 
ATOM   9766  O  OD1   . ASP   B 1 476 ? 83.834  109.338 158.384 1.00 98.47  ?  476  ASP   B OD1   1 
ATOM   9767  O  OD2   . ASP   B 1 476 ? 82.727  107.917 159.639 1.00 103.83 ?  476  ASP   B OD2   1 
ATOM   9768  N  N     . GLU   B 1 477 ? 86.516  105.723 156.031 1.00 95.42  ?  477  GLU   B N     1 
ATOM   9769  C  CA    . GLU   B 1 477 ? 87.518  104.725 155.677 1.00 94.39  ?  477  GLU   B CA    1 
ATOM   9770  C  C     . GLU   B 1 477 ? 88.894  105.343 155.481 1.00 94.13  ?  477  GLU   B C     1 
ATOM   9771  O  O     . GLU   B 1 477 ? 89.900  104.630 155.558 1.00 94.71  ?  477  GLU   B O     1 
ATOM   9772  C  CB    . GLU   B 1 477 ? 87.099  103.984 154.407 1.00 92.27  ?  477  GLU   B CB    1 
ATOM   9773  C  CG    . GLU   B 1 477 ? 85.963  102.999 154.607 1.00 96.98  ?  477  GLU   B CG    1 
ATOM   9774  C  CD    . GLU   B 1 477 ? 85.508  102.371 153.306 1.00 102.61 ?  477  GLU   B CD    1 
ATOM   9775  O  OE1   . GLU   B 1 477 ? 86.147  101.395 152.861 1.00 102.01 ?  477  GLU   B OE1   1 
ATOM   9776  O  OE2   . GLU   B 1 477 ? 84.513  102.855 152.727 1.00 104.26 ?  477  GLU   B OE2   1 
ATOM   9777  N  N     . LEU   B 1 478 ? 88.960  106.651 155.227 1.00 83.89  ?  478  LEU   B N     1 
ATOM   9778  C  CA    . LEU   B 1 478 ? 90.241  107.335 155.126 1.00 78.41  ?  478  LEU   B CA    1 
ATOM   9779  C  C     . LEU   B 1 478 ? 90.974  107.414 156.457 1.00 83.76  ?  478  LEU   B C     1 
ATOM   9780  O  O     . LEU   B 1 478 ? 92.159  107.761 156.466 1.00 88.60  ?  478  LEU   B O     1 
ATOM   9781  C  CB    . LEU   B 1 478 ? 90.041  108.744 154.568 1.00 78.05  ?  478  LEU   B CB    1 
ATOM   9782  C  CG    . LEU   B 1 478 ? 89.630  108.845 153.100 1.00 80.72  ?  478  LEU   B CG    1 
ATOM   9783  C  CD1   . LEU   B 1 478 ? 89.039  110.212 152.808 1.00 82.20  ?  478  LEU   B CD1   1 
ATOM   9784  C  CD2   . LEU   B 1 478 ? 90.815  108.563 152.192 1.00 79.41  ?  478  LEU   B CD2   1 
ATOM   9785  N  N     . GLU   B 1 479 ? 90.305  107.115 157.574 1.00 89.38  ?  479  GLU   B N     1 
ATOM   9786  C  CA    . GLU   B 1 479 ? 90.974  107.177 158.870 1.00 86.80  ?  479  GLU   B CA    1 
ATOM   9787  C  C     . GLU   B 1 479 ? 92.085  106.140 158.969 1.00 90.15  ?  479  GLU   B C     1 
ATOM   9788  O  O     . GLU   B 1 479 ? 93.233  106.472 159.286 1.00 93.24  ?  479  GLU   B O     1 
ATOM   9789  C  CB    . GLU   B 1 479 ? 89.961  106.980 159.997 1.00 87.60  ?  479  GLU   B CB    1 
ATOM   9790  C  CG    . GLU   B 1 479 ? 90.542  107.205 161.384 1.00 87.67  ?  479  GLU   B CG    1 
ATOM   9791  C  CD    . GLU   B 1 479 ? 89.500  107.093 162.479 1.00 96.14  ?  479  GLU   B CD    1 
ATOM   9792  O  OE1   . GLU   B 1 479 ? 88.957  105.986 162.676 1.00 97.80  ?  479  GLU   B OE1   1 
ATOM   9793  O  OE2   . GLU   B 1 479 ? 89.205  108.119 163.127 1.00 97.54  ?  479  GLU   B OE2   1 
ATOM   9794  N  N     . GLU   B 1 480 ? 91.770  104.870 158.826 1.00 81.81  ?  480  GLU   B N     1 
ATOM   9795  C  CA    A GLU   B 1 480 ? 92.768  103.822 158.812 0.50 81.43  ?  480  GLU   B CA    1 
ATOM   9796  C  CA    B GLU   B 1 480 ? 92.836  103.839 158.802 0.50 81.43  ?  480  GLU   B CA    1 
ATOM   9797  C  C     . GLU   B 1 480 ? 93.870  103.913 157.648 1.00 84.94  ?  480  GLU   B C     1 
ATOM   9798  O  O     . GLU   B 1 480 ? 95.130  103.961 157.733 1.00 88.23  ?  480  GLU   B O     1 
ATOM   9799  C  CB    A GLU   B 1 480 ? 92.090  102.449 158.797 0.50 81.39  ?  480  GLU   B CB    1 
ATOM   9800  C  CB    B GLU   B 1 480 ? 92.162  102.468 158.807 0.50 81.39  ?  480  GLU   B CB    1 
ATOM   9801  C  CG    A GLU   B 1 480 ? 92.920  101.332 158.170 0.50 89.11  ?  480  GLU   B CG    1 
ATOM   9802  C  CG    B GLU   B 1 480 ? 91.827  101.963 160.194 0.50 89.11  ?  480  GLU   B CG    1 
ATOM   9803  C  CD    A GLU   B 1 480 ? 93.821  100.637 159.175 0.50 95.69  ?  480  GLU   B CD    1 
ATOM   9804  C  CD    B GLU   B 1 480 ? 91.804  103.025 161.278 0.50 95.69  ?  480  GLU   B CD    1 
ATOM   9805  O  OE1   A GLU   B 1 480 ? 94.131  101.248 160.217 0.50 94.21  ?  480  GLU   B OE1   1 
ATOM   9806  O  OE1   B GLU   B 1 480 ? 92.738  103.041 162.101 0.50 94.21  ?  480  GLU   B OE1   1 
ATOM   9807  O  OE2   A GLU   B 1 480 ? 94.211  99.475  158.932 0.50 91.38  ?  480  GLU   B OE2   1 
ATOM   9808  O  OE2   B GLU   B 1 480 ? 90.850  103.828 161.301 0.50 91.38  ?  480  GLU   B OE2   1 
ATOM   9809  N  N     . LEU   B 1 481 ? 93.347  104.043 156.452 1.00 72.96  ?  481  LEU   B N     1 
ATOM   9810  C  CA    . LEU   B 1 481 ? 94.257  104.047 155.310 1.00 72.05  ?  481  LEU   B CA    1 
ATOM   9811  C  C     . LEU   B 1 481 ? 95.339  105.102 155.476 1.00 70.07  ?  481  LEU   B C     1 
ATOM   9812  O  O     . LEU   B 1 481 ? 96.537  104.800 155.384 1.00 77.72  ?  481  LEU   B O     1 
ATOM   9813  C  CB    . LEU   B 1 481 ? 93.474  104.283 154.017 1.00 69.16  ?  481  LEU   B CB    1 
ATOM   9814  C  CG    . LEU   B 1 481 ? 92.478  103.199 153.609 1.00 72.29  ?  481  LEU   B CG    1 
ATOM   9815  C  CD1   . LEU   B 1 481 ? 91.963  103.449 152.199 1.00 68.20  ?  481  LEU   B CD1   1 
ATOM   9816  C  CD2   . LEU   B 1 481 ? 93.107  101.828 153.733 1.00 73.23  ?  481  LEU   B CD2   1 
ATOM   9817  N  N     . ALA   B 1 482 ? 94.932  106.338 155.779 1.00 64.42  ?  482  ALA   B N     1 
ATOM   9818  C  CA    . ALA   B 1 482 ? 95.895  107.415 155.975 1.00 63.22  ?  482  ALA   B CA    1 
ATOM   9819  C  C     . ALA   B 1 482 ? 96.978  106.993 156.952 1.00 65.17  ?  482  ALA   B C     1 
ATOM   9820  O  O     . ALA   B 1 482 ? 98.173  107.076 156.639 1.00 73.03  ?  482  ALA   B O     1 
ATOM   9821  C  CB    . ALA   B 1 482 ? 95.184  108.676 156.469 1.00 57.25  ?  482  ALA   B CB    1 
ATOM   9822  N  N     . ILE   B 1 483 ? 96.571  106.462 158.111 1.00 62.28  ?  483  ILE   B N     1 
ATOM   9823  C  CA    . ILE   B 1 483 ? 97.540  105.982 159.094 1.00 63.45  ?  483  ILE   B CA    1 
ATOM   9824  C  C     . ILE   B 1 483 ? 98.563  105.093 158.407 1.00 66.62  ?  483  ILE   B C     1 
ATOM   9825  O  O     . ILE   B 1 483 ? 99.755  105.426 158.334 1.00 73.53  ?  483  ILE   B O     1 
ATOM   9826  C  CB    . ILE   B 1 483 ? 96.830  105.241 160.241 1.00 58.28  ?  483  ILE   B CB    1 
ATOM   9827  C  CG1   . ILE   B 1 483 ? 96.130  106.234 161.169 1.00 63.99  ?  483  ILE   B CG1   1 
ATOM   9828  C  CG2   . ILE   B 1 483 ? 97.821  104.398 161.029 1.00 62.63  ?  483  ILE   B CG2   1 
ATOM   9829  C  CD1   . ILE   B 1 483 ? 95.012  105.622 161.983 1.00 64.06  ?  483  ILE   B CD1   1 
ATOM   9830  N  N     . LEU   B 1 484 ? 98.082  104.000 157.802 1.00 60.46  ?  484  LEU   B N     1 
ATOM   9831  C  CA    . LEU   B 1 484 ? 98.961  103.100 157.067 1.00 63.01  ?  484  LEU   B CA    1 
ATOM   9832  C  C     . LEU   B 1 484 ? 99.869  103.894 156.145 1.00 60.72  ?  484  LEU   B C     1 
ATOM   9833  O  O     . LEU   B 1 484 ? 101.098 103.882 156.299 1.00 66.28  ?  484  LEU   B O     1 
ATOM   9834  C  CB    . LEU   B 1 484 ? 98.136  102.087 156.271 1.00 60.08  ?  484  LEU   B CB    1 
ATOM   9835  C  CG    . LEU   B 1 484 ? 97.415  100.995 157.059 1.00 61.43  ?  484  LEU   B CG    1 
ATOM   9836  C  CD1   . LEU   B 1 484 ? 96.583  100.130 156.129 1.00 63.48  ?  484  LEU   B CD1   1 
ATOM   9837  C  CD2   . LEU   B 1 484 ? 98.408  100.149 157.836 1.00 59.95  ?  484  LEU   B CD2   1 
ATOM   9838  N  N     . ALA   B 1 485 ? 99.259  104.666 155.240 1.00 56.00  ?  485  ALA   B N     1 
ATOM   9839  C  CA    . ALA   B 1 485 ? 100.022 105.474 154.300 1.00 54.98  ?  485  ALA   B CA    1 
ATOM   9840  C  C     . ALA   B 1 485 ? 101.122 106.227 155.028 1.00 58.38  ?  485  ALA   B C     1 
ATOM   9841  O  O     . ALA   B 1 485 ? 102.316 105.976 154.808 1.00 66.36  ?  485  ALA   B O     1 
ATOM   9842  C  CB    . ALA   B 1 485 ? 99.091  106.438 153.560 1.00 54.42  ?  485  ALA   B CB    1 
ATOM   9843  N  N     . VAL   B 1 486 ? 100.732 107.070 155.990 1.00 57.87  ?  486  VAL   B N     1 
ATOM   9844  C  CA    . VAL   B 1 486 ? 101.717 107.898 156.676 1.00 60.55  ?  486  VAL   B CA    1 
ATOM   9845  C  C     . VAL   B 1 486 ? 102.792 107.014 157.278 1.00 62.08  ?  486  VAL   B C     1 
ATOM   9846  O  O     . VAL   B 1 486 ? 103.986 107.171 156.982 1.00 71.31  ?  486  VAL   B O     1 
ATOM   9847  C  CB    . VAL   B 1 486 ? 101.040 108.780 157.741 1.00 60.30  ?  486  VAL   B CB    1 
ATOM   9848  C  CG1   . VAL   B 1 486 ? 102.057 109.689 158.399 1.00 60.67  ?  486  VAL   B CG1   1 
ATOM   9849  C  CG2   . VAL   B 1 486 ? 99.967  109.632 157.090 1.00 63.03  ?  486  VAL   B CG2   1 
ATOM   9850  N  N     . ARG   B 1 487 ? 102.369 105.995 158.031 1.00 57.60  ?  487  ARG   B N     1 
ATOM   9851  C  CA    . ARG   B 1 487 ? 103.331 105.115 158.676 1.00 62.07  ?  487  ARG   B CA    1 
ATOM   9852  C  C     . ARG   B 1 487 ? 104.302 104.571 157.645 1.00 67.77  ?  487  ARG   B C     1 
ATOM   9853  O  O     . ARG   B 1 487 ? 105.520 104.769 157.756 1.00 72.09  ?  487  ARG   B O     1 
ATOM   9854  C  CB    . ARG   B 1 487 ? 102.605 103.981 159.400 1.00 63.92  ?  487  ARG   B CB    1 
ATOM   9855  C  CG    . ARG   B 1 487 ? 102.021 104.375 160.745 1.00 60.96  ?  487  ARG   B CG    1 
ATOM   9856  C  CD    . ARG   B 1 487 ? 101.808 103.155 161.623 1.00 70.25  ?  487  ARG   B CD    1 
ATOM   9857  N  NE    . ARG   B 1 487 ? 100.729 103.347 162.583 1.00 74.66  ?  487  ARG   B NE    1 
ATOM   9858  C  CZ    . ARG   B 1 487 ? 100.875 103.916 163.770 1.00 75.56  ?  487  ARG   B CZ    1 
ATOM   9859  N  NH1   . ARG   B 1 487 ? 102.047 104.374 164.178 1.00 68.83  ?  487  ARG   B NH1   1 
ATOM   9860  N  NH2   . ARG   B 1 487 ? 99.812  104.059 164.555 1.00 75.14  ?  487  ARG   B NH2   1 
ATOM   9861  N  N     . ALA   B 1 488 ? 103.765 103.995 156.567 1.00 64.24  ?  488  ALA   B N     1 
ATOM   9862  C  CA    . ALA   B 1 488 ? 104.622 103.415 155.545 1.00 60.68  ?  488  ALA   B CA    1 
ATOM   9863  C  C     . ALA   B 1 488 ? 105.607 104.449 155.034 1.00 62.27  ?  488  ALA   B C     1 
ATOM   9864  O  O     . ALA   B 1 488 ? 106.826 104.259 155.131 1.00 68.51  ?  488  ALA   B O     1 
ATOM   9865  C  CB    . ALA   B 1 488 ? 103.772 102.848 154.412 1.00 61.21  ?  488  ALA   B CB    1 
ATOM   9866  N  N     . LEU   B 1 489 ? 105.095 105.614 154.626 1.00 63.98  ?  489  LEU   B N     1 
ATOM   9867  C  CA    . LEU   B 1 489 ? 105.974 106.633 154.075 1.00 61.07  ?  489  LEU   B CA    1 
ATOM   9868  C  C     . LEU   B 1 489 ? 107.007 107.051 155.105 1.00 69.33  ?  489  LEU   B C     1 
ATOM   9869  O  O     . LEU   B 1 489 ? 108.199 107.156 154.789 1.00 79.67  ?  489  LEU   B O     1 
ATOM   9870  C  CB    . LEU   B 1 489 ? 105.156 107.828 153.590 1.00 64.04  ?  489  LEU   B CB    1 
ATOM   9871  C  CG    . LEU   B 1 489 ? 104.307 107.590 152.338 1.00 64.52  ?  489  LEU   B CG    1 
ATOM   9872  C  CD1   . LEU   B 1 489 ? 103.996 108.904 151.641 1.00 69.21  ?  489  LEU   B CD1   1 
ATOM   9873  C  CD2   . LEU   B 1 489 ? 104.996 106.626 151.383 1.00 64.64  ?  489  LEU   B CD2   1 
ATOM   9874  N  N     . ASP   B 1 490 ? 106.582 107.222 156.361 1.00 69.22  ?  490  ASP   B N     1 
ATOM   9875  C  CA    . ASP   B 1 490 ? 107.529 107.628 157.389 1.00 66.49  ?  490  ASP   B CA    1 
ATOM   9876  C  C     . ASP   B 1 490 ? 108.617 106.580 157.553 1.00 73.49  ?  490  ASP   B C     1 
ATOM   9877  O  O     . ASP   B 1 490 ? 109.808 106.912 157.618 1.00 78.09  ?  490  ASP   B O     1 
ATOM   9878  C  CB    . ASP   B 1 490 ? 106.805 107.879 158.712 1.00 71.61  ?  490  ASP   B CB    1 
ATOM   9879  C  CG    . ASP   B 1 490 ? 107.511 108.910 159.567 1.00 82.88  ?  490  ASP   B CG    1 
ATOM   9880  O  OD1   . ASP   B 1 490 ? 107.360 110.117 159.288 1.00 85.01  ?  490  ASP   B OD1   1 
ATOM   9881  O  OD2   . ASP   B 1 490 ? 108.256 108.510 160.485 1.00 87.12  ?  490  ASP   B OD2   1 
ATOM   9882  N  N     . ALA   B 1 491 ? 108.232 105.303 157.560 1.00 61.40  ?  491  ALA   B N     1 
ATOM   9883  C  CA    . ALA   B 1 491 ? 109.232 104.250 157.668 1.00 52.08  ?  491  ALA   B CA    1 
ATOM   9884  C  C     . ALA   B 1 491 ? 110.183 104.295 156.484 1.00 59.21  ?  491  ALA   B C     1 
ATOM   9885  O  O     . ALA   B 1 491 ? 111.397 104.114 156.645 1.00 67.79  ?  491  ALA   B O     1 
ATOM   9886  C  CB    . ALA   B 1 491 ? 108.551 102.891 157.778 1.00 58.30  ?  491  ALA   B CB    1 
ATOM   9887  N  N     . LEU   B 1 492 ? 109.657 104.616 155.299 1.00 57.54  ?  492  LEU   B N     1 
ATOM   9888  C  CA    . LEU   B 1 492 ? 110.502 104.728 154.118 1.00 54.28  ?  492  LEU   B CA    1 
ATOM   9889  C  C     . LEU   B 1 492 ? 111.589 105.771 154.327 1.00 58.18  ?  492  LEU   B C     1 
ATOM   9890  O  O     . LEU   B 1 492 ? 112.723 105.597 153.865 1.00 68.82  ?  492  LEU   B O     1 
ATOM   9891  C  CB    . LEU   B 1 492 ? 109.643 105.067 152.903 1.00 57.79  ?  492  LEU   B CB    1 
ATOM   9892  C  CG    . LEU   B 1 492 ? 110.291 104.932 151.529 1.00 62.73  ?  492  LEU   B CG    1 
ATOM   9893  C  CD1   . LEU   B 1 492 ? 109.377 104.177 150.585 1.00 66.32  ?  492  LEU   B CD1   1 
ATOM   9894  C  CD2   . LEU   B 1 492 ? 110.624 106.299 150.969 1.00 67.60  ?  492  LEU   B CD2   1 
ATOM   9895  N  N     . LEU   B 1 493 ? 111.272 106.847 155.053 1.00 65.53  ?  493  LEU   B N     1 
ATOM   9896  C  CA    . LEU   B 1 493 ? 112.262 107.891 155.286 1.00 66.16  ?  493  LEU   B CA    1 
ATOM   9897  C  C     . LEU   B 1 493 ? 113.446 107.370 156.086 1.00 70.74  ?  493  LEU   B C     1 
ATOM   9898  O  O     . LEU   B 1 493 ? 114.576 107.834 155.895 1.00 75.61  ?  493  LEU   B O     1 
ATOM   9899  C  CB    . LEU   B 1 493 ? 111.613 109.076 155.997 1.00 67.45  ?  493  LEU   B CB    1 
ATOM   9900  C  CG    . LEU   B 1 493 ? 110.739 109.958 155.106 1.00 69.83  ?  493  LEU   B CG    1 
ATOM   9901  C  CD1   . LEU   B 1 493 ? 109.955 110.944 155.946 1.00 68.27  ?  493  LEU   B CD1   1 
ATOM   9902  C  CD2   . LEU   B 1 493 ? 111.583 110.680 154.069 1.00 65.63  ?  493  LEU   B CD2   1 
ATOM   9903  N  N     . ASP   B 1 494 ? 113.216 106.410 156.978 1.00 74.83  ?  494  ASP   B N     1 
ATOM   9904  C  CA    . ASP   B 1 494 ? 114.299 105.807 157.741 1.00 70.58  ?  494  ASP   B CA    1 
ATOM   9905  C  C     . ASP   B 1 494 ? 114.937 104.634 157.014 1.00 73.63  ?  494  ASP   B C     1 
ATOM   9906  O  O     . ASP   B 1 494 ? 115.927 104.080 157.503 1.00 79.88  ?  494  ASP   B O     1 
ATOM   9907  C  CB    . ASP   B 1 494 ? 113.790 105.358 159.112 1.00 77.15  ?  494  ASP   B CB    1 
ATOM   9908  C  CG    . ASP   B 1 494 ? 113.280 106.513 159.947 1.00 82.67  ?  494  ASP   B CG    1 
ATOM   9909  O  OD1   . ASP   B 1 494 ? 114.039 107.485 160.140 1.00 84.81  ?  494  ASP   B OD1   1 
ATOM   9910  O  OD2   . ASP   B 1 494 ? 112.126 106.450 160.416 1.00 82.39  ?  494  ASP   B OD2   1 
ATOM   9911  N  N     . TYR   B 1 495 ? 114.394 104.250 155.861 1.00 73.74  ?  495  TYR   B N     1 
ATOM   9912  C  CA    . TYR   B 1 495 ? 114.916 103.144 155.076 1.00 69.48  ?  495  TYR   B CA    1 
ATOM   9913  C  C     . TYR   B 1 495 ? 115.753 103.582 153.876 1.00 75.99  ?  495  TYR   B C     1 
ATOM   9914  O  O     . TYR   B 1 495 ? 116.489 102.779 153.323 1.00 80.61  ?  495  TYR   B O     1 
ATOM   9915  C  CB    . TYR   B 1 495 ? 113.753 102.266 154.593 1.00 71.50  ?  495  TYR   B CB    1 
ATOM   9916  C  CG    . TYR   B 1 495 ? 114.172 100.991 153.912 1.00 70.87  ?  495  TYR   B CG    1 
ATOM   9917  C  CD1   . TYR   B 1 495 ? 114.981 100.071 154.558 1.00 70.25  ?  495  TYR   B CD1   1 
ATOM   9918  C  CD2   . TYR   B 1 495 ? 113.757 100.707 152.622 1.00 73.51  ?  495  TYR   B CD2   1 
ATOM   9919  C  CE1   . TYR   B 1 495 ? 115.367 98.905  153.936 1.00 74.57  ?  495  TYR   B CE1   1 
ATOM   9920  C  CE2   . TYR   B 1 495 ? 114.144 99.551  151.990 1.00 72.83  ?  495  TYR   B CE2   1 
ATOM   9921  C  CZ    . TYR   B 1 495 ? 114.919 98.636  152.663 1.00 77.39  ?  495  TYR   B CZ    1 
ATOM   9922  O  OH    . TYR   B 1 495 ? 115.325 97.498  152.010 1.00 81.67  ?  495  TYR   B OH    1 
ATOM   9923  N  N     . GLN   B 1 496 ? 115.683 104.807 153.458 1.00 72.56  ?  496  GLN   B N     1 
ATOM   9924  C  CA    . GLN   B 1 496 ? 116.234 105.216 152.191 1.00 68.52  ?  496  GLN   B CA    1 
ATOM   9925  C  C     . GLN   B 1 496 ? 117.678 105.620 152.381 1.00 74.65  ?  496  GLN   B C     1 
ATOM   9926  O  O     . GLN   B 1 496 ? 118.075 105.902 153.484 1.00 80.16  ?  496  GLN   B O     1 
ATOM   9927  C  CB    . GLN   B 1 496 ? 115.342 106.357 151.793 1.00 68.71  ?  496  GLN   B CB    1 
ATOM   9928  C  CG    . GLN   B 1 496 ? 115.010 106.524 150.368 1.00 72.11  ?  496  GLN   B CG    1 
ATOM   9929  C  CD    . GLN   B 1 496 ? 114.502 107.919 150.255 1.00 74.54  ?  496  GLN   B CD    1 
ATOM   9930  O  OE1   . GLN   B 1 496 ? 113.697 108.346 151.071 1.00 74.90  ?  496  GLN   B OE1   1 
ATOM   9931  N  NE2   . GLN   B 1 496 ? 115.014 108.668 149.304 1.00 80.16  ?  496  GLN   B NE2   1 
ATOM   9932  N  N     . ASP   B 1 497 ? 118.439 105.681 151.303 1.00 77.20  ?  497  ASP   B N     1 
ATOM   9933  C  CA    . ASP   B 1 497 ? 119.831 106.103 151.265 1.00 75.08  ?  497  ASP   B CA    1 
ATOM   9934  C  C     . ASP   B 1 497 ? 119.917 107.381 150.445 1.00 77.42  ?  497  ASP   B C     1 
ATOM   9935  O  O     . ASP   B 1 497 ? 119.158 107.575 149.490 1.00 81.61  ?  497  ASP   B O     1 
ATOM   9936  C  CB    . ASP   B 1 497 ? 120.720 105.017 150.640 1.00 75.76  ?  497  ASP   B CB    1 
ATOM   9937  C  CG    . ASP   B 1 497 ? 120.978 103.860 151.583 1.00 87.89  ?  497  ASP   B CG    1 
ATOM   9938  O  OD1   . ASP   B 1 497 ? 121.087 104.098 152.803 1.00 92.21  ?  497  ASP   B OD1   1 
ATOM   9939  O  OD2   . ASP   B 1 497 ? 121.073 102.712 151.104 1.00 89.06  ?  497  ASP   B OD2   1 
ATOM   9940  N  N     . TYR   B 1 498 ? 120.834 108.260 150.825 1.00 70.19  ?  498  TYR   B N     1 
ATOM   9941  C  CA    . TYR   B 1 498 ? 120.920 109.590 150.225 1.00 68.87  ?  498  TYR   B CA    1 
ATOM   9942  C  C     . TYR   B 1 498 ? 122.293 109.825 149.618 1.00 71.53  ?  498  TYR   B C     1 
ATOM   9943  O  O     . TYR   B 1 498 ? 123.274 110.009 150.364 1.00 76.42  ?  498  TYR   B O     1 
ATOM   9944  C  CB    . TYR   B 1 498 ? 120.603 110.659 151.270 1.00 67.54  ?  498  TYR   B CB    1 
ATOM   9945  C  CG    . TYR   B 1 498 ? 119.248 110.475 151.911 1.00 67.99  ?  498  TYR   B CG    1 
ATOM   9946  C  CD1   . TYR   B 1 498 ? 118.114 111.049 151.357 1.00 69.99  ?  498  TYR   B CD1   1 
ATOM   9947  C  CD2   . TYR   B 1 498 ? 119.100 109.717 153.063 1.00 64.89  ?  498  TYR   B CD2   1 
ATOM   9948  C  CE1   . TYR   B 1 498 ? 116.872 110.877 151.936 1.00 67.90  ?  498  TYR   B CE1   1 
ATOM   9949  C  CE2   . TYR   B 1 498 ? 117.862 109.540 153.647 1.00 67.23  ?  498  TYR   B CE2   1 
ATOM   9950  C  CZ    . TYR   B 1 498 ? 116.752 110.122 153.079 1.00 69.07  ?  498  TYR   B CZ    1 
ATOM   9951  O  OH    . TYR   B 1 498 ? 115.517 109.953 153.656 1.00 70.69  ?  498  TYR   B OH    1 
ATOM   9952  N  N     . PRO   B 1 499 ? 122.422 109.816 148.289 1.00 65.93  ?  499  PRO   B N     1 
ATOM   9953  C  CA    . PRO   B 1 499 ? 123.726 110.119 147.679 1.00 67.89  ?  499  PRO   B CA    1 
ATOM   9954  C  C     . PRO   B 1 499 ? 124.242 111.513 147.995 1.00 72.49  ?  499  PRO   B C     1 
ATOM   9955  O  O     . PRO   B 1 499 ? 125.461 111.710 148.066 1.00 77.64  ?  499  PRO   B O     1 
ATOM   9956  C  CB    . PRO   B 1 499 ? 123.445 109.947 146.181 1.00 68.41  ?  499  PRO   B CB    1 
ATOM   9957  C  CG    . PRO   B 1 499 ? 121.987 110.237 146.076 1.00 67.06  ?  499  PRO   B CG    1 
ATOM   9958  C  CD    . PRO   B 1 499 ? 121.407 109.541 147.262 1.00 63.45  ?  499  PRO   B CD    1 
ATOM   9959  N  N     . ILE   B 1 500 ? 123.359 112.484 148.181 1.00 70.16  ?  500  ILE   B N     1 
ATOM   9960  C  CA    . ILE   B 1 500 ? 123.732 113.863 148.484 1.00 69.11  ?  500  ILE   B CA    1 
ATOM   9961  C  C     . ILE   B 1 500 ? 123.415 114.124 149.953 1.00 73.22  ?  500  ILE   B C     1 
ATOM   9962  O  O     . ILE   B 1 500 ? 122.256 113.976 150.363 1.00 76.63  ?  500  ILE   B O     1 
ATOM   9963  C  CB    . ILE   B 1 500 ? 123.000 114.864 147.575 1.00 69.12  ?  500  ILE   B CB    1 
ATOM   9964  C  CG1   . ILE   B 1 500 ? 122.782 114.265 146.184 1.00 66.98  ?  500  ILE   B CG1   1 
ATOM   9965  C  CG2   . ILE   B 1 500 ? 123.780 116.165 147.480 1.00 65.63  ?  500  ILE   B CG2   1 
ATOM   9966  C  CD1   . ILE   B 1 500 ? 124.048 114.125 145.373 1.00 67.41  ?  500  ILE   B CD1   1 
ATOM   9967  N  N     . PRO   B 1 501 ? 124.400 114.486 150.780 1.00 80.51  ?  501  PRO   B N     1 
ATOM   9968  C  CA    . PRO   B 1 501 ? 124.103 114.778 152.194 1.00 78.43  ?  501  PRO   B CA    1 
ATOM   9969  C  C     . PRO   B 1 501 ? 123.093 115.892 152.407 1.00 77.11  ?  501  PRO   B C     1 
ATOM   9970  O  O     . PRO   B 1 501 ? 122.386 115.883 153.422 1.00 74.87  ?  501  PRO   B O     1 
ATOM   9971  C  CB    . PRO   B 1 501 ? 125.478 115.156 152.761 1.00 74.57  ?  501  PRO   B CB    1 
ATOM   9972  C  CG    . PRO   B 1 501 ? 126.310 115.466 151.542 1.00 74.72  ?  501  PRO   B CG    1 
ATOM   9973  C  CD    . PRO   B 1 501 ? 125.850 114.486 150.539 1.00 76.79  ?  501  PRO   B CD    1 
ATOM   9974  N  N     . ALA   B 1 502 ? 123.012 116.862 151.495 1.00 72.28  ?  502  ALA   B N     1 
ATOM   9975  C  CA    . ALA   B 1 502 ? 122.019 117.922 151.637 1.00 70.11  ?  502  ALA   B CA    1 
ATOM   9976  C  C     . ALA   B 1 502 ? 120.604 117.374 151.532 1.00 71.60  ?  502  ALA   B C     1 
ATOM   9977  O  O     . ALA   B 1 502 ? 119.699 117.830 152.243 1.00 80.79  ?  502  ALA   B O     1 
ATOM   9978  C  CB    . ALA   B 1 502 ? 122.255 119.009 150.592 1.00 72.47  ?  502  ALA   B CB    1 
ATOM   9979  N  N     . ALA   B 1 503 ? 120.392 116.401 150.642 1.00 63.65  ?  503  ALA   B N     1 
ATOM   9980  C  CA    . ALA   B 1 503 ? 119.090 115.758 150.534 1.00 55.38  ?  503  ALA   B CA    1 
ATOM   9981  C  C     . ALA   B 1 503 ? 118.746 115.000 151.806 1.00 60.06  ?  503  ALA   B C     1 
ATOM   9982  O  O     . ALA   B 1 503 ? 117.596 115.025 152.253 1.00 72.67  ?  503  ALA   B O     1 
ATOM   9983  C  CB    . ALA   B 1 503 ? 119.067 114.834 149.321 1.00 57.13  ?  503  ALA   B CB    1 
ATOM   9984  N  N     . LYS   B 1 504 ? 119.734 114.334 152.413 1.00 63.33  ?  504  LYS   B N     1 
ATOM   9985  C  CA    . LYS   B 1 504 ? 119.503 113.679 153.696 1.00 63.78  ?  504  LYS   B CA    1 
ATOM   9986  C  C     . LYS   B 1 504 ? 119.145 114.694 154.770 1.00 62.98  ?  504  LYS   B C     1 
ATOM   9987  O  O     . LYS   B 1 504 ? 118.249 114.453 155.585 1.00 66.58  ?  504  LYS   B O     1 
ATOM   9988  C  CB    . LYS   B 1 504 ? 120.736 112.878 154.110 1.00 70.25  ?  504  LYS   B CB    1 
ATOM   9989  C  CG    . LYS   B 1 504 ? 120.531 112.047 155.365 1.00 63.12  ?  504  LYS   B CG    1 
ATOM   9990  C  CD    . LYS   B 1 504 ? 121.696 111.103 155.603 1.00 67.25  ?  504  LYS   B CD    1 
ATOM   9991  C  CE    . LYS   B 1 504 ? 121.276 109.917 156.454 1.00 72.04  ?  504  LYS   B CE    1 
ATOM   9992  N  NZ    . LYS   B 1 504 ? 120.284 110.300 157.494 1.00 76.88  ?  504  LYS   B NZ    1 
ATOM   9993  N  N     . ARG   B 1 505 ? 119.841 115.833 154.788 1.00 72.89  ?  505  ARG   B N     1 
ATOM   9994  C  CA    . ARG   B 1 505 ? 119.516 116.893 155.736 1.00 71.23  ?  505  ARG   B CA    1 
ATOM   9995  C  C     . ARG   B 1 505 ? 118.068 117.331 155.582 1.00 75.39  ?  505  ARG   B C     1 
ATOM   9996  O  O     . ARG   B 1 505 ? 117.318 117.394 156.562 1.00 76.52  ?  505  ARG   B O     1 
ATOM   9997  C  CB    . ARG   B 1 505 ? 120.455 118.081 155.532 1.00 73.02  ?  505  ARG   B CB    1 
ATOM   9998  C  CG    . ARG   B 1 505 ? 121.725 118.028 156.350 1.00 74.63  ?  505  ARG   B CG    1 
ATOM   9999  C  CD    . ARG   B 1 505 ? 122.316 119.416 156.504 1.00 77.78  ?  505  ARG   B CD    1 
ATOM   10000 N  NE    . ARG   B 1 505 ? 121.509 120.265 157.372 1.00 81.52  ?  505  ARG   B NE    1 
ATOM   10001 C  CZ    . ARG   B 1 505 ? 121.174 121.519 157.099 1.00 81.04  ?  505  ARG   B CZ    1 
ATOM   10002 N  NH1   . ARG   B 1 505 ? 121.549 122.107 155.976 1.00 82.37  ?  505  ARG   B NH1   1 
ATOM   10003 N  NH2   . ARG   B 1 505 ? 120.458 122.206 157.983 1.00 77.55  ?  505  ARG   B NH2   1 
ATOM   10004 N  N     . GLY   B 1 506 ? 117.654 117.626 154.349 1.00 71.75  ?  506  GLY   B N     1 
ATOM   10005 C  CA    . GLY   B 1 506 ? 116.286 118.067 154.126 1.00 68.71  ?  506  GLY   B CA    1 
ATOM   10006 C  C     . GLY   B 1 506 ? 115.259 117.016 154.504 1.00 72.49  ?  506  GLY   B C     1 
ATOM   10007 O  O     . GLY   B 1 506 ? 114.257 117.317 155.160 1.00 75.44  ?  506  GLY   B O     1 
ATOM   10008 N  N     . ALA   B 1 507 ? 115.500 115.766 154.107 1.00 63.19  ?  507  ALA   B N     1 
ATOM   10009 C  CA    . ALA   B 1 507 ? 114.539 114.702 154.365 1.00 60.45  ?  507  ALA   B CA    1 
ATOM   10010 C  C     . ALA   B 1 507 ? 114.419 114.396 155.853 1.00 67.12  ?  507  ALA   B C     1 
ATOM   10011 O  O     . ALA   B 1 507 ? 113.308 114.202 156.357 1.00 72.70  ?  507  ALA   B O     1 
ATOM   10012 C  CB    . ALA   B 1 507 ? 114.924 113.454 153.577 1.00 65.66  ?  507  ALA   B CB    1 
ATOM   10013 N  N     . MET   B 1 508 ? 115.537 114.389 156.583 1.00 79.91  ?  508  MET   B N     1 
ATOM   10014 C  CA    . MET   B 1 508 ? 115.478 114.107 158.011 1.00 74.52  ?  508  MET   B CA    1 
ATOM   10015 C  C     . MET   B 1 508 ? 114.997 115.303 158.817 1.00 82.65  ?  508  MET   B C     1 
ATOM   10016 O  O     . MET   B 1 508 ? 114.437 115.119 159.901 1.00 89.99  ?  508  MET   B O     1 
ATOM   10017 C  CB    . MET   B 1 508 ? 116.842 113.635 158.517 1.00 83.16  ?  508  MET   B CB    1 
ATOM   10018 C  CG    . MET   B 1 508 ? 117.296 112.238 158.040 1.00 86.61  ?  508  MET   B CG    1 
ATOM   10019 S  SD    . MET   B 1 508 ? 116.203 110.780 158.110 1.00 98.75  ?  508  MET   B SD    1 
ATOM   10020 C  CE    . MET   B 1 508 ? 114.926 111.095 156.884 1.00 83.87  ?  508  MET   B CE    1 
ATOM   10021 N  N     . GLY   B 1 509 ? 115.201 116.521 158.322 1.00 69.26  ?  509  GLY   B N     1 
ATOM   10022 C  CA    . GLY   B 1 509 ? 114.735 117.692 159.031 1.00 67.00  ?  509  GLY   B CA    1 
ATOM   10023 C  C     . GLY   B 1 509 ? 113.253 117.936 158.860 1.00 66.45  ?  509  GLY   B C     1 
ATOM   10024 O  O     . GLY   B 1 509 ? 112.565 118.264 159.828 1.00 67.46  ?  509  GLY   B O     1 
ATOM   10025 N  N     . ARG   B 1 510 ? 112.743 117.769 157.640 1.00 66.42  ?  510  ARG   B N     1 
ATOM   10026 C  CA    . ARG   B 1 510 ? 111.348 118.079 157.355 1.00 62.73  ?  510  ARG   B CA    1 
ATOM   10027 C  C     . ARG   B 1 510 ? 110.448 116.854 157.304 1.00 69.09  ?  510  ARG   B C     1 
ATOM   10028 O  O     . ARG   B 1 510 ? 109.286 116.943 157.712 1.00 73.33  ?  510  ARG   B O     1 
ATOM   10029 C  CB    . ARG   B 1 510 ? 111.239 118.842 156.032 1.00 61.12  ?  510  ARG   B CB    1 
ATOM   10030 C  CG    . ARG   B 1 510 ? 112.251 119.962 155.899 1.00 63.64  ?  510  ARG   B CG    1 
ATOM   10031 C  CD    . ARG   B 1 510 ? 111.689 121.139 155.126 1.00 70.05  ?  510  ARG   B CD    1 
ATOM   10032 N  NE    . ARG   B 1 510 ? 112.626 122.254 155.094 1.00 68.82  ?  510  ARG   B NE    1 
ATOM   10033 C  CZ    . ARG   B 1 510 ? 112.700 123.195 156.025 1.00 64.95  ?  510  ARG   B CZ    1 
ATOM   10034 N  NH1   . ARG   B 1 510 ? 111.897 123.191 157.076 1.00 62.96  ?  510  ARG   B NH1   1 
ATOM   10035 N  NH2   . ARG   B 1 510 ? 113.602 124.163 155.898 1.00 70.75  ?  510  ARG   B NH2   1 
ATOM   10036 N  N     . ARG   B 1 511 ? 110.957 115.717 156.822 1.00 68.07  ?  511  ARG   B N     1 
ATOM   10037 C  CA    . ARG   B 1 511 ? 110.180 114.479 156.719 1.00 62.56  ?  511  ARG   B CA    1 
ATOM   10038 C  C     . ARG   B 1 511 ? 108.899 114.691 155.915 1.00 63.46  ?  511  ARG   B C     1 
ATOM   10039 O  O     . ARG   B 1 511 ? 107.823 114.226 156.292 1.00 67.57  ?  511  ARG   B O     1 
ATOM   10040 C  CB    . ARG   B 1 511 ? 109.867 113.906 158.103 1.00 58.44  ?  511  ARG   B CB    1 
ATOM   10041 C  CG    . ARG   B 1 511 ? 111.073 113.811 159.020 1.00 63.84  ?  511  ARG   B CG    1 
ATOM   10042 C  CD    . ARG   B 1 511 ? 110.763 112.992 160.260 1.00 65.66  ?  511  ARG   B CD    1 
ATOM   10043 N  NE    . ARG   B 1 511 ? 110.463 111.601 159.942 1.00 68.74  ?  511  ARG   B NE    1 
ATOM   10044 C  CZ    . ARG   B 1 511 ? 111.367 110.633 159.894 1.00 70.75  ?  511  ARG   B CZ    1 
ATOM   10045 N  NH1   . ARG   B 1 511 ? 112.647 110.871 160.125 1.00 70.75  ?  511  ARG   B NH1   1 
ATOM   10046 N  NH2   . ARG   B 1 511 ? 110.980 109.400 159.581 1.00 60.26  ?  511  ARG   B NH2   1 
ATOM   10047 N  N     . THR   B 1 512 ? 109.019 115.392 154.793 1.00 63.35  ?  512  THR   B N     1 
ATOM   10048 C  CA    . THR   B 1 512 ? 107.857 115.773 154.005 1.00 67.75  ?  512  THR   B CA    1 
ATOM   10049 C  C     . THR   B 1 512 ? 107.362 114.607 153.160 1.00 70.93  ?  512  THR   B C     1 
ATOM   10050 O  O     . THR   B 1 512 ? 108.151 113.899 152.530 1.00 76.75  ?  512  THR   B O     1 
ATOM   10051 C  CB    . THR   B 1 512 ? 108.196 116.962 153.106 1.00 72.96  ?  512  THR   B CB    1 
ATOM   10052 O  OG1   . THR   B 1 512 ? 109.439 116.716 152.438 1.00 72.87  ?  512  THR   B OG1   1 
ATOM   10053 C  CG2   . THR   B 1 512 ? 108.320 118.228 153.935 1.00 73.00  ?  512  THR   B CG2   1 
ATOM   10054 N  N     . LEU   B 1 513 ? 106.044 114.410 153.155 1.00 64.14  ?  513  LEU   B N     1 
ATOM   10055 C  CA    . LEU   B 1 513 ? 105.395 113.407 152.324 1.00 62.86  ?  513  LEU   B CA    1 
ATOM   10056 C  C     . LEU   B 1 513 ? 104.318 114.065 151.478 1.00 67.09  ?  513  LEU   B C     1 
ATOM   10057 O  O     . LEU   B 1 513 ? 103.728 115.074 151.870 1.00 66.57  ?  513  LEU   B O     1 
ATOM   10058 C  CB    . LEU   B 1 513 ? 104.752 112.288 153.150 1.00 60.03  ?  513  LEU   B CB    1 
ATOM   10059 C  CG    . LEU   B 1 513 ? 105.420 111.879 154.457 1.00 62.90  ?  513  LEU   B CG    1 
ATOM   10060 C  CD1   . LEU   B 1 513 ? 104.490 111.056 155.329 1.00 61.60  ?  513  LEU   B CD1   1 
ATOM   10061 C  CD2   . LEU   B 1 513 ? 106.719 111.128 154.211 1.00 67.47  ?  513  LEU   B CD2   1 
ATOM   10062 N  N     . GLY   B 1 514 ? 104.066 113.484 150.309 1.00 72.30  ?  514  GLY   B N     1 
ATOM   10063 C  CA    . GLY   B 1 514 ? 102.980 113.948 149.473 1.00 59.45  ?  514  GLY   B CA    1 
ATOM   10064 C  C     . GLY   B 1 514 ? 101.969 112.856 149.198 1.00 57.41  ?  514  GLY   B C     1 
ATOM   10065 O  O     . GLY   B 1 514 ? 102.254 111.902 148.470 1.00 71.65  ?  514  GLY   B O     1 
ATOM   10066 N  N     . ILE   B 1 515 ? 100.779 112.983 149.771 1.00 51.45  ?  515  ILE   B N     1 
ATOM   10067 C  CA    . ILE   B 1 515 ? 99.711  112.014 149.576 1.00 51.36  ?  515  ILE   B CA    1 
ATOM   10068 C  C     . ILE   B 1 515 ? 98.603  112.716 148.806 1.00 56.50  ?  515  ILE   B C     1 
ATOM   10069 O  O     . ILE   B 1 515 ? 97.984  113.663 149.306 1.00 61.12  ?  515  ILE   B O     1 
ATOM   10070 C  CB    . ILE   B 1 515 ? 99.202  111.440 150.904 1.00 51.47  ?  515  ILE   B CB    1 
ATOM   10071 C  CG1   . ILE   B 1 515 ? 100.169 110.375 151.423 1.00 51.52  ?  515  ILE   B CG1   1 
ATOM   10072 C  CG2   . ILE   B 1 515 ? 97.825  110.836 150.729 1.00 51.80  ?  515  ILE   B CG2   1 
ATOM   10073 C  CD1   . ILE   B 1 515 ? 100.347 110.394 152.924 1.00 52.68  ?  515  ILE   B CD1   1 
ATOM   10074 N  N     . GLY   B 1 516 ? 98.364  112.257 147.577 1.00 53.77  ?  516  GLY   B N     1 
ATOM   10075 C  CA    . GLY   B 1 516 ? 97.327  112.783 146.735 1.00 54.01  ?  516  GLY   B CA    1 
ATOM   10076 C  C     . GLY   B 1 516 ? 96.150  111.843 146.614 1.00 57.76  ?  516  GLY   B C     1 
ATOM   10077 O  O     . GLY   B 1 516 ? 95.969  110.915 147.412 1.00 62.84  ?  516  GLY   B O     1 
ATOM   10078 N  N     . VAL   B 1 517 ? 95.367  112.043 145.557 1.00 66.28  ?  517  VAL   B N     1 
ATOM   10079 C  CA    . VAL   B 1 517 ? 94.217  111.198 145.279 1.00 55.38  ?  517  VAL   B CA    1 
ATOM   10080 C  C     . VAL   B 1 517 ? 94.254  110.765 143.821 1.00 60.36  ?  517  VAL   B C     1 
ATOM   10081 O  O     . VAL   B 1 517 ? 94.870  111.406 142.967 1.00 73.37  ?  517  VAL   B O     1 
ATOM   10082 C  CB    . VAL   B 1 517 ? 92.882  111.908 145.593 1.00 54.57  ?  517  VAL   B CB    1 
ATOM   10083 C  CG1   . VAL   B 1 517 ? 92.836  112.337 147.046 1.00 58.04  ?  517  VAL   B CG1   1 
ATOM   10084 C  CG2   . VAL   B 1 517 ? 92.681  113.095 144.665 1.00 61.23  ?  517  VAL   B CG2   1 
ATOM   10085 N  N     . ILE   B 1 518 ? 93.592  109.642 143.553 1.00 47.90  ?  518  ILE   B N     1 
ATOM   10086 C  CA    . ILE   B 1 518 ? 93.336  109.163 142.205 1.00 43.19  ?  518  ILE   B CA    1 
ATOM   10087 C  C     . ILE   B 1 518 ? 91.867  108.770 142.129 1.00 52.42  ?  518  ILE   B C     1 
ATOM   10088 O  O     . ILE   B 1 518 ? 91.172  108.691 143.142 1.00 61.97  ?  518  ILE   B O     1 
ATOM   10089 C  CB    . ILE   B 1 518 ? 94.248  107.981 141.812 1.00 49.64  ?  518  ILE   B CB    1 
ATOM   10090 C  CG1   . ILE   B 1 518 ? 93.972  106.753 142.678 1.00 47.82  ?  518  ILE   B CG1   1 
ATOM   10091 C  CG2   . ILE   B 1 518 ? 95.710  108.366 141.937 1.00 52.96  ?  518  ILE   B CG2   1 
ATOM   10092 C  CD1   . ILE   B 1 518 ? 94.489  105.473 142.060 1.00 44.51  ?  518  ILE   B CD1   1 
ATOM   10093 N  N     . ASN   B 1 519 ? 91.395  108.537 140.902 1.00 49.07  ?  519  ASN   B N     1 
ATOM   10094 C  CA    . ASN   B 1 519 ? 90.003  108.159 140.643 1.00 51.47  ?  519  ASN   B CA    1 
ATOM   10095 C  C     . ASN   B 1 519 ? 89.025  109.253 141.061 1.00 52.44  ?  519  ASN   B C     1 
ATOM   10096 O  O     . ASN   B 1 519 ? 87.895  108.963 141.460 1.00 67.71  ?  519  ASN   B O     1 
ATOM   10097 C  CB    . ASN   B 1 519 ? 89.637  106.844 141.338 1.00 50.29  ?  519  ASN   B CB    1 
ATOM   10098 C  CG    . ASN   B 1 519 ? 89.365  105.722 140.366 1.00 49.91  ?  519  ASN   B CG    1 
ATOM   10099 O  OD1   . ASN   B 1 519 ? 89.071  105.951 139.195 1.00 63.33  ?  519  ASN   B OD1   1 
ATOM   10100 N  ND2   . ASN   B 1 519 ? 89.533  104.494 140.831 1.00 54.67  ?  519  ASN   B ND2   1 
ATOM   10101 N  N     . PHE   B 1 520 ? 89.440  110.520 140.986 1.00 47.43  ?  520  PHE   B N     1 
ATOM   10102 C  CA    . PHE   B 1 520 ? 88.540  111.600 141.378 1.00 49.57  ?  520  PHE   B CA    1 
ATOM   10103 C  C     . PHE   B 1 520 ? 87.382  111.744 140.399 1.00 53.07  ?  520  PHE   B C     1 
ATOM   10104 O  O     . PHE   B 1 520 ? 86.244  111.998 140.810 1.00 59.00  ?  520  PHE   B O     1 
ATOM   10105 C  CB    . PHE   B 1 520 ? 89.301  112.918 141.499 1.00 50.50  ?  520  PHE   B CB    1 
ATOM   10106 C  CG    . PHE   B 1 520 ? 88.442  114.063 141.950 1.00 58.48  ?  520  PHE   B CG    1 
ATOM   10107 C  CD1   . PHE   B 1 520 ? 87.893  114.072 143.221 1.00 57.44  ?  520  PHE   B CD1   1 
ATOM   10108 C  CD2   . PHE   B 1 520 ? 88.166  115.118 141.099 1.00 56.64  ?  520  PHE   B CD2   1 
ATOM   10109 C  CE1   . PHE   B 1 520 ? 87.096  115.117 143.638 1.00 52.85  ?  520  PHE   B CE1   1 
ATOM   10110 C  CE2   . PHE   B 1 520 ? 87.367  116.165 141.511 1.00 53.34  ?  520  PHE   B CE2   1 
ATOM   10111 C  CZ    . PHE   B 1 520 ? 86.833  116.166 142.782 1.00 53.74  ?  520  PHE   B CZ    1 
ATOM   10112 N  N     . ALA   B 1 521 ? 87.652  111.594 139.101 1.00 59.29  ?  521  ALA   B N     1 
ATOM   10113 C  CA    . ALA   B 1 521 ? 86.580  111.650 138.113 1.00 55.85  ?  521  ALA   B CA    1 
ATOM   10114 C  C     . ALA   B 1 521 ? 85.595  110.506 138.305 1.00 63.68  ?  521  ALA   B C     1 
ATOM   10115 O  O     . ALA   B 1 521 ? 84.378  110.702 138.205 1.00 71.79  ?  521  ALA   B O     1 
ATOM   10116 C  CB    . ALA   B 1 521 ? 87.163  111.630 136.704 1.00 52.35  ?  521  ALA   B CB    1 
ATOM   10117 N  N     . TYR   B 1 522 ? 86.101  109.309 138.609 1.00 56.05  ?  522  TYR   B N     1 
ATOM   10118 C  CA    . TYR   B 1 522 ? 85.226  108.182 138.911 1.00 53.64  ?  522  TYR   B CA    1 
ATOM   10119 C  C     . TYR   B 1 522 ? 84.418  108.441 140.176 1.00 61.75  ?  522  TYR   B C     1 
ATOM   10120 O  O     . TYR   B 1 522 ? 83.242  108.076 140.254 1.00 67.27  ?  522  TYR   B O     1 
ATOM   10121 C  CB    . TYR   B 1 522 ? 86.058  106.907 139.042 1.00 53.04  ?  522  TYR   B CB    1 
ATOM   10122 C  CG    . TYR   B 1 522 ? 85.279  105.672 139.433 1.00 56.01  ?  522  TYR   B CG    1 
ATOM   10123 C  CD1   . TYR   B 1 522 ? 84.019  105.422 138.912 1.00 59.99  ?  522  TYR   B CD1   1 
ATOM   10124 C  CD2   . TYR   B 1 522 ? 85.814  104.749 140.319 1.00 58.83  ?  522  TYR   B CD2   1 
ATOM   10125 C  CE1   . TYR   B 1 522 ? 83.312  104.291 139.270 1.00 64.02  ?  522  TYR   B CE1   1 
ATOM   10126 C  CE2   . TYR   B 1 522 ? 85.118  103.613 140.678 1.00 61.26  ?  522  TYR   B CE2   1 
ATOM   10127 C  CZ    . TYR   B 1 522 ? 83.866  103.392 140.152 1.00 65.32  ?  522  TYR   B CZ    1 
ATOM   10128 O  OH    . TYR   B 1 522 ? 83.149  102.275 140.507 1.00 72.25  ?  522  TYR   B OH    1 
ATOM   10129 N  N     . TYR   B 1 523 ? 85.036  109.069 141.177 1.00 61.30  ?  523  TYR   B N     1 
ATOM   10130 C  CA    . TYR   B 1 523 ? 84.323  109.431 142.399 1.00 56.56  ?  523  TYR   B CA    1 
ATOM   10131 C  C     . TYR   B 1 523 ? 83.170  110.384 142.097 1.00 58.28  ?  523  TYR   B C     1 
ATOM   10132 O  O     . TYR   B 1 523 ? 82.036  110.181 142.556 1.00 67.90  ?  523  TYR   B O     1 
ATOM   10133 C  CB    . TYR   B 1 523 ? 85.319  110.053 143.383 1.00 56.61  ?  523  TYR   B CB    1 
ATOM   10134 C  CG    . TYR   B 1 523 ? 84.782  110.404 144.749 1.00 58.48  ?  523  TYR   B CG    1 
ATOM   10135 C  CD1   . TYR   B 1 523 ? 84.584  109.428 145.714 1.00 62.63  ?  523  TYR   B CD1   1 
ATOM   10136 C  CD2   . TYR   B 1 523 ? 84.510  111.722 145.088 1.00 61.83  ?  523  TYR   B CD2   1 
ATOM   10137 C  CE1   . TYR   B 1 523 ? 84.106  109.751 146.968 1.00 62.54  ?  523  TYR   B CE1   1 
ATOM   10138 C  CE2   . TYR   B 1 523 ? 84.026  112.052 146.337 1.00 61.23  ?  523  TYR   B CE2   1 
ATOM   10139 C  CZ    . TYR   B 1 523 ? 83.847  111.067 147.279 1.00 62.70  ?  523  TYR   B CZ    1 
ATOM   10140 O  OH    . TYR   B 1 523 ? 83.351  111.391 148.519 1.00 67.83  ?  523  TYR   B OH    1 
ATOM   10141 N  N     . LEU   B 1 524 ? 83.439  111.420 141.298 1.00 50.69  ?  524  LEU   B N     1 
ATOM   10142 C  CA    . LEU   B 1 524 ? 82.399  112.378 140.936 1.00 44.93  ?  524  LEU   B CA    1 
ATOM   10143 C  C     . LEU   B 1 524 ? 81.288  111.714 140.134 1.00 49.98  ?  524  LEU   B C     1 
ATOM   10144 O  O     . LEU   B 1 524 ? 80.103  111.982 140.362 1.00 60.00  ?  524  LEU   B O     1 
ATOM   10145 C  CB    . LEU   B 1 524 ? 83.005  113.536 140.145 1.00 51.87  ?  524  LEU   B CB    1 
ATOM   10146 C  CG    . LEU   B 1 524 ? 83.841  114.554 140.921 1.00 55.41  ?  524  LEU   B CG    1 
ATOM   10147 C  CD1   . LEU   B 1 524 ? 84.188  115.736 140.034 1.00 49.31  ?  524  LEU   B CD1   1 
ATOM   10148 C  CD2   . LEU   B 1 524 ? 83.113  115.010 142.168 1.00 52.12  ?  524  LEU   B CD2   1 
ATOM   10149 N  N     . ALA   B 1 525 ? 81.651  110.842 139.191 1.00 53.91  ?  525  ALA   B N     1 
ATOM   10150 C  CA    . ALA   B 1 525 ? 80.646  110.161 138.384 1.00 54.21  ?  525  ALA   B CA    1 
ATOM   10151 C  C     . ALA   B 1 525 ? 79.802  109.216 139.225 1.00 58.11  ?  525  ALA   B C     1 
ATOM   10152 O  O     . ALA   B 1 525 ? 78.584  109.133 139.031 1.00 67.98  ?  525  ALA   B O     1 
ATOM   10153 C  CB    . ALA   B 1 525 ? 81.315  109.419 137.232 1.00 56.00  ?  525  ALA   B CB    1 
ATOM   10154 N  N     . LYS   B 1 526 ? 80.421  108.526 140.187 1.00 58.35  ?  526  LYS   B N     1 
ATOM   10155 C  CA    . LYS   B 1 526 ? 79.677  107.666 141.097 1.00 57.52  ?  526  LYS   B CA    1 
ATOM   10156 C  C     . LYS   B 1 526 ? 78.733  108.470 141.974 1.00 63.92  ?  526  LYS   B C     1 
ATOM   10157 O  O     . LYS   B 1 526 ? 77.660  107.979 142.337 1.00 74.17  ?  526  LYS   B O     1 
ATOM   10158 C  CB    . LYS   B 1 526 ? 80.646  106.858 141.957 1.00 60.47  ?  526  LYS   B CB    1 
ATOM   10159 C  CG    . LYS   B 1 526 ? 80.228  105.417 142.168 1.00 70.60  ?  526  LYS   B CG    1 
ATOM   10160 C  CD    . LYS   B 1 526 ? 81.414  104.555 142.559 1.00 69.22  ?  526  LYS   B CD    1 
ATOM   10161 C  CE    . LYS   B 1 526 ? 82.068  105.061 143.830 1.00 68.70  ?  526  LYS   B CE    1 
ATOM   10162 N  NZ    . LYS   B 1 526 ? 83.339  104.347 144.120 1.00 72.72  ?  526  LYS   B NZ    1 
ATOM   10163 N  N     . HIS   B 1 527 ? 79.109  109.696 142.326 1.00 69.01  ?  527  HIS   B N     1 
ATOM   10164 C  CA    . HIS   B 1 527 ? 78.227  110.565 143.092 1.00 64.48  ?  527  HIS   B CA    1 
ATOM   10165 C  C     . HIS   B 1 527 ? 77.284  111.378 142.214 1.00 65.97  ?  527  HIS   B C     1 
ATOM   10166 O  O     . HIS   B 1 527 ? 76.515  112.189 142.742 1.00 72.30  ?  527  HIS   B O     1 
ATOM   10167 C  CB    . HIS   B 1 527 ? 79.051  111.501 143.976 1.00 69.58  ?  527  HIS   B CB    1 
ATOM   10168 C  CG    . HIS   B 1 527 ? 79.589  110.844 145.208 1.00 70.52  ?  527  HIS   B CG    1 
ATOM   10169 N  ND1   . HIS   B 1 527 ? 78.775  110.297 146.175 1.00 71.63  ?  527  HIS   B ND1   1 
ATOM   10170 C  CD2   . HIS   B 1 527 ? 80.860  110.638 145.625 1.00 68.77  ?  527  HIS   B CD2   1 
ATOM   10171 C  CE1   . HIS   B 1 527 ? 79.521  109.786 147.138 1.00 72.91  ?  527  HIS   B CE1   1 
ATOM   10172 N  NE2   . HIS   B 1 527 ? 80.790  109.984 146.831 1.00 71.59  ?  527  HIS   B NE2   1 
ATOM   10173 N  N     . GLY   B 1 528 ? 77.318  111.179 140.901 1.00 69.31  ?  528  GLY   B N     1 
ATOM   10174 C  CA    . GLY   B 1 528 ? 76.434  111.897 140.000 1.00 65.62  ?  528  GLY   B CA    1 
ATOM   10175 C  C     . GLY   B 1 528 ? 76.692  113.385 139.910 1.00 68.39  ?  528  GLY   B C     1 
ATOM   10176 O  O     . GLY   B 1 528 ? 75.739  114.175 139.913 1.00 76.31  ?  528  GLY   B O     1 
ATOM   10177 N  N     . LYS   B 1 529 ? 77.957  113.791 139.833 1.00 68.94  ?  529  LYS   B N     1 
ATOM   10178 C  CA    . LYS   B 1 529 ? 78.328  115.193 139.721 1.00 69.33  ?  529  LYS   B CA    1 
ATOM   10179 C  C     . LYS   B 1 529 ? 79.337  115.361 138.594 1.00 69.88  ?  529  LYS   B C     1 
ATOM   10180 O  O     . LYS   B 1 529 ? 79.980  114.402 138.160 1.00 78.89  ?  529  LYS   B O     1 
ATOM   10181 C  CB    . LYS   B 1 529 ? 78.905  115.733 141.037 1.00 66.18  ?  529  LYS   B CB    1 
ATOM   10182 C  CG    . LYS   B 1 529 ? 78.146  115.273 142.269 1.00 68.93  ?  529  LYS   B CG    1 
ATOM   10183 C  CD    . LYS   B 1 529 ? 78.129  116.331 143.343 1.00 74.10  ?  529  LYS   B CD    1 
ATOM   10184 C  CE    . LYS   B 1 529 ? 76.986  116.106 144.315 1.00 74.22  ?  529  LYS   B CE    1 
ATOM   10185 N  NZ    . LYS   B 1 529 ? 75.674  116.441 143.704 1.00 74.02  ?  529  LYS   B NZ    1 
ATOM   10186 N  N     . ARG   B 1 530 ? 79.465  116.597 138.117 1.00 76.04  ?  530  ARG   B N     1 
ATOM   10187 C  CA    . ARG   B 1 530 ? 80.345  116.921 137.004 1.00 74.19  ?  530  ARG   B CA    1 
ATOM   10188 C  C     . ARG   B 1 530 ? 81.254  118.083 137.379 1.00 80.48  ?  530  ARG   B C     1 
ATOM   10189 O  O     . ARG   B 1 530 ? 81.037  118.782 138.373 1.00 90.48  ?  530  ARG   B O     1 
ATOM   10190 C  CB    . ARG   B 1 530 ? 79.548  117.264 135.738 1.00 74.81  ?  530  ARG   B CB    1 
ATOM   10191 C  CG    . ARG   B 1 530 ? 78.077  116.899 135.802 1.00 77.76  ?  530  ARG   B CG    1 
ATOM   10192 C  CD    . ARG   B 1 530 ? 77.430  116.998 134.434 1.00 80.29  ?  530  ARG   B CD    1 
ATOM   10193 N  NE    . ARG   B 1 530 ? 77.930  115.977 133.521 1.00 86.41  ?  530  ARG   B NE    1 
ATOM   10194 C  CZ    . ARG   B 1 530 ? 77.393  114.773 133.379 1.00 85.48  ?  530  ARG   B CZ    1 
ATOM   10195 N  NH1   . ARG   B 1 530 ? 76.333  114.402 134.076 1.00 83.64  ?  530  ARG   B NH1   1 
ATOM   10196 N  NH2   . ARG   B 1 530 ? 77.935  113.919 132.515 1.00 79.53  ?  530  ARG   B NH2   1 
ATOM   10197 N  N     . TYR   B 1 531 ? 82.286  118.283 136.554 1.00 73.12  ?  531  TYR   B N     1 
ATOM   10198 C  CA    . TYR   B 1 531 ? 83.242  119.361 136.781 1.00 73.45  ?  531  TYR   B CA    1 
ATOM   10199 C  C     . TYR   B 1 531 ? 82.671  120.726 136.422 1.00 81.59  ?  531  TYR   B C     1 
ATOM   10200 O  O     . TYR   B 1 531 ? 83.016  121.726 137.061 1.00 86.80  ?  531  TYR   B O     1 
ATOM   10201 C  CB    . TYR   B 1 531 ? 84.510  119.123 135.962 1.00 67.58  ?  531  TYR   B CB    1 
ATOM   10202 C  CG    . TYR   B 1 531 ? 85.349  117.946 136.398 1.00 74.76  ?  531  TYR   B CG    1 
ATOM   10203 C  CD1   . TYR   B 1 531 ? 85.117  116.676 135.888 1.00 77.32  ?  531  TYR   B CD1   1 
ATOM   10204 C  CD2   . TYR   B 1 531 ? 86.384  118.106 137.304 1.00 79.13  ?  531  TYR   B CD2   1 
ATOM   10205 C  CE1   . TYR   B 1 531 ? 85.884  115.595 136.277 1.00 77.84  ?  531  TYR   B CE1   1 
ATOM   10206 C  CE2   . TYR   B 1 531 ? 87.146  117.033 137.707 1.00 78.07  ?  531  TYR   B CE2   1 
ATOM   10207 C  CZ    . TYR   B 1 531 ? 86.913  115.788 137.170 1.00 80.95  ?  531  TYR   B CZ    1 
ATOM   10208 O  OH    . TYR   B 1 531 ? 87.698  114.748 137.605 1.00 84.28  ?  531  TYR   B OH    1 
ATOM   10209 N  N     . SER   B 1 532 ? 81.808  120.792 135.408 1.00 83.58  ?  532  SER   B N     1 
ATOM   10210 C  CA    . SER   B 1 532 ? 81.476  122.071 134.788 1.00 81.79  ?  532  SER   B CA    1 
ATOM   10211 C  C     . SER   B 1 532 ? 80.431  122.847 135.582 1.00 82.04  ?  532  SER   B C     1 
ATOM   10212 O  O     . SER   B 1 532 ? 80.652  124.010 135.938 1.00 85.09  ?  532  SER   B O     1 
ATOM   10213 C  CB    . SER   B 1 532 ? 80.992  121.839 133.356 1.00 82.65  ?  532  SER   B CB    1 
ATOM   10214 O  OG    . SER   B 1 532 ? 81.969  121.155 132.593 1.00 85.75  ?  532  SER   B OG    1 
ATOM   10215 N  N     . ASP   B 1 533 ? 79.286  122.224 135.867 1.00 92.39  ?  533  ASP   B N     1 
ATOM   10216 C  CA    . ASP   B 1 533 ? 78.150  122.949 136.426 1.00 94.67  ?  533  ASP   B CA    1 
ATOM   10217 C  C     . ASP   B 1 533 ? 78.390  123.449 137.844 1.00 95.76  ?  533  ASP   B C     1 
ATOM   10218 O  O     . ASP   B 1 533 ? 77.591  124.252 138.338 1.00 95.75  ?  533  ASP   B O     1 
ATOM   10219 C  CB    . ASP   B 1 533 ? 76.898  122.071 136.400 1.00 99.61  ?  533  ASP   B CB    1 
ATOM   10220 C  CG    . ASP   B 1 533 ? 77.193  120.621 136.721 1.00 102.19 ?  533  ASP   B CG    1 
ATOM   10221 O  OD1   . ASP   B 1 533 ? 78.041  120.364 137.601 1.00 99.89  ?  533  ASP   B OD1   1 
ATOM   10222 O  OD2   . ASP   B 1 533 ? 76.574  119.738 136.093 1.00 101.24 ?  533  ASP   B OD2   1 
ATOM   10223 N  N     . GLY   B 1 534 ? 79.452  123.010 138.507 1.00 88.48  ?  534  GLY   B N     1 
ATOM   10224 C  CA    . GLY   B 1 534 ? 79.711  123.433 139.864 1.00 84.19  ?  534  GLY   B CA    1 
ATOM   10225 C  C     . GLY   B 1 534 ? 78.999  122.636 140.931 1.00 87.43  ?  534  GLY   B C     1 
ATOM   10226 O  O     . GLY   B 1 534 ? 79.004  123.051 142.095 1.00 92.83  ?  534  GLY   B O     1 
ATOM   10227 N  N     . SER   B 1 535 ? 78.352  121.526 140.568 1.00 83.13  ?  535  SER   B N     1 
ATOM   10228 C  CA    . SER   B 1 535 ? 77.679  120.693 141.556 1.00 84.48  ?  535  SER   B CA    1 
ATOM   10229 C  C     . SER   B 1 535 ? 78.659  119.991 142.481 1.00 84.34  ?  535  SER   B C     1 
ATOM   10230 O  O     . SER   B 1 535 ? 78.266  119.576 143.575 1.00 86.03  ?  535  SER   B O     1 
ATOM   10231 C  CB    . SER   B 1 535 ? 76.796  119.653 140.865 1.00 82.67  ?  535  SER   B CB    1 
ATOM   10232 O  OG    . SER   B 1 535 ? 77.388  119.241 139.649 1.00 81.59  ?  535  SER   B OG    1 
ATOM   10233 N  N     . ALA   B 1 536 ? 79.920  119.857 142.076 1.00 72.29  ?  536  ALA   B N     1 
ATOM   10234 C  CA    . ALA   B 1 536 ? 80.916  119.108 142.829 1.00 71.16  ?  536  ALA   B CA    1 
ATOM   10235 C  C     . ALA   B 1 536 ? 81.655  119.951 143.858 1.00 77.41  ?  536  ALA   B C     1 
ATOM   10236 O  O     . ALA   B 1 536 ? 82.524  119.420 144.556 1.00 86.05  ?  536  ALA   B O     1 
ATOM   10237 C  CB    . ALA   B 1 536 ? 81.929  118.471 141.872 1.00 74.87  ?  536  ALA   B CB    1 
ATOM   10238 N  N     . ASN   B 1 537 ? 81.323  121.237 143.982 1.00 72.94  ?  537  ASN   B N     1 
ATOM   10239 C  CA    . ASN   B 1 537 ? 82.067  122.119 144.879 1.00 67.55  ?  537  ASN   B CA    1 
ATOM   10240 C  C     . ASN   B 1 537 ? 81.965  121.655 146.329 1.00 70.60  ?  537  ASN   B C     1 
ATOM   10241 O  O     . ASN   B 1 537 ? 82.981  121.501 147.017 1.00 76.16  ?  537  ASN   B O     1 
ATOM   10242 C  CB    . ASN   B 1 537 ? 81.561  123.555 144.734 1.00 66.81  ?  537  ASN   B CB    1 
ATOM   10243 C  CG    . ASN   B 1 537 ? 81.953  124.179 143.408 1.00 73.25  ?  537  ASN   B CG    1 
ATOM   10244 O  OD1   . ASN   B 1 537 ? 81.781  123.574 142.352 1.00 79.73  ?  537  ASN   B OD1   1 
ATOM   10245 N  ND2   . ASN   B 1 537 ? 82.507  125.383 143.459 1.00 73.26  ?  537  ASN   B ND2   1 
ATOM   10246 N  N     . ASN   B 1 538 ? 80.743  121.416 146.808 1.00 67.89  ?  538  ASN   B N     1 
ATOM   10247 C  CA    . ASN   B 1 538 ? 80.561  121.004 148.196 1.00 67.71  ?  538  ASN   B CA    1 
ATOM   10248 C  C     . ASN   B 1 538 ? 81.114  119.605 148.439 1.00 73.20  ?  538  ASN   B C     1 
ATOM   10249 O  O     . ASN   B 1 538 ? 81.713  119.341 149.489 1.00 80.38  ?  538  ASN   B O     1 
ATOM   10250 C  CB    . ASN   B 1 538 ? 79.082  121.073 148.572 1.00 64.56  ?  538  ASN   B CB    1 
ATOM   10251 C  CG    . ASN   B 1 538 ? 78.554  122.491 148.596 1.00 70.11  ?  538  ASN   B CG    1 
ATOM   10252 O  OD1   . ASN   B 1 538 ? 79.119  123.364 149.252 1.00 71.11  ?  538  ASN   B OD1   1 
ATOM   10253 N  ND2   . ASN   B 1 538 ? 77.463  122.730 147.876 1.00 74.24  ?  538  ASN   B ND2   1 
ATOM   10254 N  N     . LEU   B 1 539 ? 80.917  118.694 147.482 1.00 67.79  ?  539  LEU   B N     1 
ATOM   10255 C  CA    . LEU   B 1 539 ? 81.452  117.343 147.627 1.00 65.48  ?  539  LEU   B CA    1 
ATOM   10256 C  C     . LEU   B 1 539 ? 82.973  117.355 147.668 1.00 68.48  ?  539  LEU   B C     1 
ATOM   10257 O  O     . LEU   B 1 539 ? 83.584  116.656 148.485 1.00 73.12  ?  539  LEU   B O     1 
ATOM   10258 C  CB    . LEU   B 1 539 ? 80.960  116.449 146.490 1.00 58.56  ?  539  LEU   B CB    1 
ATOM   10259 C  CG    . LEU   B 1 539 ? 81.418  114.992 146.522 1.00 60.93  ?  539  LEU   B CG    1 
ATOM   10260 C  CD1   . LEU   B 1 539 ? 81.057  114.376 147.860 1.00 66.55  ?  539  LEU   B CD1   1 
ATOM   10261 C  CD2   . LEU   B 1 539 ? 80.722  114.261 145.398 1.00 67.41  ?  539  LEU   B CD2   1 
ATOM   10262 N  N     . THR   B 1 540 ? 83.603  118.139 146.789 1.00 56.06  ?  540  THR   B N     1 
ATOM   10263 C  CA    . THR   B 1 540 ? 85.056  118.263 146.813 1.00 53.06  ?  540  THR   B CA    1 
ATOM   10264 C  C     . THR   B 1 540 ? 85.528  118.863 148.129 1.00 59.51  ?  540  THR   B C     1 
ATOM   10265 O  O     . THR   B 1 540 ? 86.517  118.402 148.714 1.00 72.00  ?  540  THR   B O     1 
ATOM   10266 C  CB    . THR   B 1 540 ? 85.530  119.120 145.639 1.00 56.12  ?  540  THR   B CB    1 
ATOM   10267 O  OG1   . THR   B 1 540 ? 84.936  118.644 144.426 1.00 69.42  ?  540  THR   B OG1   1 
ATOM   10268 C  CG2   . THR   B 1 540 ? 87.040  119.066 145.512 1.00 65.06  ?  540  THR   B CG2   1 
ATOM   10269 N  N     . HIS   B 1 541 ? 84.827  119.895 148.607 1.00 59.03  ?  541  HIS   B N     1 
ATOM   10270 C  CA    . HIS   B 1 541 ? 85.164  120.504 149.889 1.00 59.85  ?  541  HIS   B CA    1 
ATOM   10271 C  C     . HIS   B 1 541 ? 85.152  119.468 151.003 1.00 61.33  ?  541  HIS   B C     1 
ATOM   10272 O  O     . HIS   B 1 541 ? 86.123  119.339 151.758 1.00 72.24  ?  541  HIS   B O     1 
ATOM   10273 C  CB    . HIS   B 1 541 ? 84.182  121.637 150.193 1.00 58.52  ?  541  HIS   B CB    1 
ATOM   10274 C  CG    . HIS   B 1 541 ? 84.532  122.434 151.410 1.00 64.08  ?  541  HIS   B CG    1 
ATOM   10275 N  ND1   . HIS   B 1 541 ? 84.249  122.003 152.688 1.00 68.16  ?  541  HIS   B ND1   1 
ATOM   10276 C  CD2   . HIS   B 1 541 ? 85.135  123.638 151.544 1.00 62.94  ?  541  HIS   B CD2   1 
ATOM   10277 C  CE1   . HIS   B 1 541 ? 84.667  122.906 153.556 1.00 67.86  ?  541  HIS   B CE1   1 
ATOM   10278 N  NE2   . HIS   B 1 541 ? 85.208  123.908 152.888 1.00 66.87  ?  541  HIS   B NE2   1 
ATOM   10279 N  N     . LYS   B 1 542 ? 84.064  118.703 151.105 1.00 56.80  ?  542  LYS   B N     1 
ATOM   10280 C  CA    . LYS   B 1 542 ? 83.945  117.713 152.170 1.00 61.34  ?  542  LYS   B CA    1 
ATOM   10281 C  C     . LYS   B 1 542 ? 85.006  116.625 152.042 1.00 67.66  ?  542  LYS   B C     1 
ATOM   10282 O  O     . LYS   B 1 542 ? 85.646  116.249 153.035 1.00 73.12  ?  542  LYS   B O     1 
ATOM   10283 C  CB    . LYS   B 1 542 ? 82.542  117.108 152.157 1.00 61.02  ?  542  LYS   B CB    1 
ATOM   10284 C  CG    . LYS   B 1 542 ? 82.371  115.890 153.046 1.00 70.30  ?  542  LYS   B CG    1 
ATOM   10285 C  CD    . LYS   B 1 542 ? 80.918  115.421 153.094 1.00 68.75  ?  542  LYS   B CD    1 
ATOM   10286 C  CE    . LYS   B 1 542 ? 80.437  114.955 151.731 1.00 74.39  ?  542  LYS   B CE    1 
ATOM   10287 N  NZ    . LYS   B 1 542 ? 79.167  115.620 151.326 1.00 74.37  ?  542  LYS   B NZ    1 
ATOM   10288 N  N     . THR   B 1 543 ? 85.219  116.119 150.824 1.00 67.23  ?  543  THR   B N     1 
ATOM   10289 C  CA    . THR   B 1 543 ? 86.173  115.033 150.620 1.00 61.61  ?  543  THR   B CA    1 
ATOM   10290 C  C     . THR   B 1 543 ? 87.584  115.460 151.000 1.00 62.92  ?  543  THR   B C     1 
ATOM   10291 O  O     . THR   B 1 543 ? 88.292  114.743 151.718 1.00 73.17  ?  543  THR   B O     1 
ATOM   10292 C  CB    . THR   B 1 543 ? 86.131  114.567 149.163 1.00 62.92  ?  543  THR   B CB    1 
ATOM   10293 O  OG1   . THR   B 1 543 ? 84.769  114.460 148.732 1.00 74.65  ?  543  THR   B OG1   1 
ATOM   10294 C  CG2   . THR   B 1 543 ? 86.818  113.215 149.008 1.00 66.27  ?  543  THR   B CG2   1 
ATOM   10295 N  N     . PHE   B 1 544 ? 88.013  116.634 150.537 1.00 55.40  ?  544  PHE   B N     1 
ATOM   10296 C  CA    . PHE   B 1 544 ? 89.381  117.042 150.820 1.00 56.10  ?  544  PHE   B CA    1 
ATOM   10297 C  C     . PHE   B 1 544 ? 89.548  117.540 152.249 1.00 58.00  ?  544  PHE   B C     1 
ATOM   10298 O  O     . PHE   B 1 544 ? 90.641  117.413 152.814 1.00 65.15  ?  544  PHE   B O     1 
ATOM   10299 C  CB    . PHE   B 1 544 ? 89.837  118.081 149.798 1.00 53.29  ?  544  PHE   B CB    1 
ATOM   10300 C  CG    . PHE   B 1 544 ? 90.201  117.479 148.473 1.00 60.32  ?  544  PHE   B CG    1 
ATOM   10301 C  CD1   . PHE   B 1 544 ? 89.214  117.068 147.596 1.00 59.46  ?  544  PHE   B CD1   1 
ATOM   10302 C  CD2   . PHE   B 1 544 ? 91.525  117.281 148.122 1.00 56.46  ?  544  PHE   B CD2   1 
ATOM   10303 C  CE1   . PHE   B 1 544 ? 89.538  116.507 146.387 1.00 55.48  ?  544  PHE   B CE1   1 
ATOM   10304 C  CE2   . PHE   B 1 544 ? 91.857  116.712 146.905 1.00 58.78  ?  544  PHE   B CE2   1 
ATOM   10305 C  CZ    . PHE   B 1 544 ? 90.861  116.303 146.050 1.00 58.36  ?  544  PHE   B CZ    1 
ATOM   10306 N  N     . GLU   B 1 545 ? 88.485  118.060 152.870 1.00 64.42  ?  545  GLU   B N     1 
ATOM   10307 C  CA    . GLU   B 1 545 ? 88.540  118.325 154.302 1.00 63.66  ?  545  GLU   B CA    1 
ATOM   10308 C  C     . GLU   B 1 545 ? 88.784  117.038 155.074 1.00 69.20  ?  545  GLU   B C     1 
ATOM   10309 O  O     . GLU   B 1 545 ? 89.628  116.992 155.976 1.00 80.42  ?  545  GLU   B O     1 
ATOM   10310 C  CB    . GLU   B 1 545 ? 87.245  118.990 154.768 1.00 68.44  ?  545  GLU   B CB    1 
ATOM   10311 C  CG    . GLU   B 1 545 ? 87.252  119.373 156.239 1.00 70.82  ?  545  GLU   B CG    1 
ATOM   10312 C  CD    . GLU   B 1 545 ? 85.957  119.023 156.940 1.00 78.71  ?  545  GLU   B CD    1 
ATOM   10313 O  OE1   . GLU   B 1 545 ? 84.987  118.651 156.249 1.00 82.86  ?  545  GLU   B OE1   1 
ATOM   10314 O  OE2   . GLU   B 1 545 ? 85.909  119.117 158.183 1.00 78.55  ?  545  GLU   B OE2   1 
ATOM   10315 N  N     . ALA   B 1 546 ? 88.061  115.972 154.719 1.00 61.44  ?  546  ALA   B N     1 
ATOM   10316 C  CA    . ALA   B 1 546 ? 88.279  114.686 155.372 1.00 58.86  ?  546  ALA   B CA    1 
ATOM   10317 C  C     . ALA   B 1 546 ? 89.698  114.184 155.142 1.00 67.57  ?  546  ALA   B C     1 
ATOM   10318 O  O     . ALA   B 1 546 ? 90.355  113.704 156.075 1.00 75.17  ?  546  ALA   B O     1 
ATOM   10319 C  CB    . ALA   B 1 546 ? 87.261  113.663 154.872 1.00 59.44  ?  546  ALA   B CB    1 
ATOM   10320 N  N     . ILE   B 1 547 ? 90.192  114.299 153.907 1.00 56.94  ?  547  ILE   B N     1 
ATOM   10321 C  CA    . ILE   B 1 547 ? 91.530  113.805 153.588 1.00 53.09  ?  547  ILE   B CA    1 
ATOM   10322 C  C     . ILE   B 1 547 ? 92.580  114.533 154.419 1.00 56.77  ?  547  ILE   B C     1 
ATOM   10323 O  O     . ILE   B 1 547 ? 93.434  113.906 155.061 1.00 68.14  ?  547  ILE   B O     1 
ATOM   10324 C  CB    . ILE   B 1 547 ? 91.808  113.944 152.080 1.00 58.70  ?  547  ILE   B CB    1 
ATOM   10325 C  CG1   . ILE   B 1 547 ? 91.172  112.786 151.312 1.00 61.98  ?  547  ILE   B CG1   1 
ATOM   10326 C  CG2   . ILE   B 1 547 ? 93.305  113.999 151.809 1.00 55.35  ?  547  ILE   B CG2   1 
ATOM   10327 C  CD1   . ILE   B 1 547 ? 90.736  113.151 149.914 1.00 60.14  ?  547  ILE   B CD1   1 
ATOM   10328 N  N     . GLN   B 1 548 ? 92.529  115.868 154.425 1.00 57.04  ?  548  GLN   B N     1 
ATOM   10329 C  CA    . GLN   B 1 548 ? 93.521  116.638 155.167 1.00 49.52  ?  548  GLN   B CA    1 
ATOM   10330 C  C     . GLN   B 1 548 ? 93.411  116.388 156.665 1.00 56.93  ?  548  GLN   B C     1 
ATOM   10331 O  O     . GLN   B 1 548 ? 94.430  116.245 157.351 1.00 65.77  ?  548  GLN   B O     1 
ATOM   10332 C  CB    . GLN   B 1 548 ? 93.377  118.127 154.860 1.00 53.51  ?  548  GLN   B CB    1 
ATOM   10333 C  CG    . GLN   B 1 548 ? 94.456  118.991 155.496 1.00 63.91  ?  548  GLN   B CG    1 
ATOM   10334 C  CD    . GLN   B 1 548 ? 95.839  118.696 154.951 1.00 66.20  ?  548  GLN   B CD    1 
ATOM   10335 O  OE1   . GLN   B 1 548 ? 95.996  118.345 153.784 1.00 68.63  ?  548  GLN   B OE1   1 
ATOM   10336 N  NE2   . GLN   B 1 548 ? 96.851  118.832 155.799 1.00 64.34  ?  548  GLN   B NE2   1 
ATOM   10337 N  N     . TYR   B 1 549 ? 92.184  116.323 157.192 1.00 60.14  ?  549  TYR   B N     1 
ATOM   10338 C  CA    . TYR   B 1 549 ? 92.012  116.087 158.620 1.00 56.94  ?  549  TYR   B CA    1 
ATOM   10339 C  C     . TYR   B 1 549 ? 92.594  114.743 159.029 1.00 62.85  ?  549  TYR   B C     1 
ATOM   10340 O  O     . TYR   B 1 549 ? 93.292  114.647 160.045 1.00 67.14  ?  549  TYR   B O     1 
ATOM   10341 C  CB    . TYR   B 1 549 ? 90.532  116.162 158.994 1.00 58.95  ?  549  TYR   B CB    1 
ATOM   10342 C  CG    . TYR   B 1 549 ? 90.251  115.767 160.426 1.00 60.09  ?  549  TYR   B CG    1 
ATOM   10343 C  CD1   . TYR   B 1 549 ? 90.422  116.672 161.462 1.00 59.04  ?  549  TYR   B CD1   1 
ATOM   10344 C  CD2   . TYR   B 1 549 ? 89.820  114.486 160.743 1.00 61.34  ?  549  TYR   B CD2   1 
ATOM   10345 C  CE1   . TYR   B 1 549 ? 90.171  116.315 162.771 1.00 60.41  ?  549  TYR   B CE1   1 
ATOM   10346 C  CE2   . TYR   B 1 549 ? 89.567  114.121 162.049 1.00 63.11  ?  549  TYR   B CE2   1 
ATOM   10347 C  CZ    . TYR   B 1 549 ? 89.737  115.042 163.058 1.00 64.11  ?  549  TYR   B CZ    1 
ATOM   10348 O  OH    . TYR   B 1 549 ? 89.494  114.680 164.363 1.00 71.13  ?  549  TYR   B OH    1 
ATOM   10349 N  N     . TYR   B 1 550 ? 92.331  113.693 158.249 1.00 61.59  ?  550  TYR   B N     1 
ATOM   10350 C  CA    . TYR   B 1 550 ? 92.818  112.376 158.640 1.00 51.45  ?  550  TYR   B CA    1 
ATOM   10351 C  C     . TYR   B 1 550 ? 94.323  112.251 158.451 1.00 58.77  ?  550  TYR   B C     1 
ATOM   10352 O  O     . TYR   B 1 550 ? 94.990  111.595 159.259 1.00 63.91  ?  550  TYR   B O     1 
ATOM   10353 C  CB    . TYR   B 1 550 ? 92.068  111.293 157.873 1.00 53.35  ?  550  TYR   B CB    1 
ATOM   10354 C  CG    . TYR   B 1 550 ? 90.689  111.037 158.435 1.00 59.93  ?  550  TYR   B CG    1 
ATOM   10355 C  CD1   . TYR   B 1 550 ? 90.524  110.637 159.754 1.00 62.66  ?  550  TYR   B CD1   1 
ATOM   10356 C  CD2   . TYR   B 1 550 ? 89.553  111.210 157.658 1.00 62.99  ?  550  TYR   B CD2   1 
ATOM   10357 C  CE1   . TYR   B 1 550 ? 89.273  110.410 160.278 1.00 61.98  ?  550  TYR   B CE1   1 
ATOM   10358 C  CE2   . TYR   B 1 550 ? 88.294  110.995 158.180 1.00 65.61  ?  550  TYR   B CE2   1 
ATOM   10359 C  CZ    . TYR   B 1 550 ? 88.164  110.577 159.484 1.00 64.54  ?  550  TYR   B CZ    1 
ATOM   10360 O  OH    . TYR   B 1 550 ? 86.907  110.355 159.993 1.00 68.52  ?  550  TYR   B OH    1 
ATOM   10361 N  N     . LEU   B 1 551 ? 94.885  112.884 157.417 1.00 54.52  ?  551  LEU   B N     1 
ATOM   10362 C  CA    . LEU   B 1 551 ? 96.338  112.892 157.279 1.00 50.98  ?  551  LEU   B CA    1 
ATOM   10363 C  C     . LEU   B 1 551 ? 96.998  113.608 158.451 1.00 55.29  ?  551  LEU   B C     1 
ATOM   10364 O  O     . LEU   B 1 551 ? 97.994  113.124 159.007 1.00 64.87  ?  551  LEU   B O     1 
ATOM   10365 C  CB    . LEU   B 1 551 ? 96.741  113.549 155.962 1.00 54.19  ?  551  LEU   B CB    1 
ATOM   10366 C  CG    . LEU   B 1 551 ? 96.531  112.711 154.702 1.00 54.16  ?  551  LEU   B CG    1 
ATOM   10367 C  CD1   . LEU   B 1 551 ? 96.998  113.443 153.457 1.00 55.93  ?  551  LEU   B CD1   1 
ATOM   10368 C  CD2   . LEU   B 1 551 ? 97.215  111.361 154.816 1.00 51.04  ?  551  LEU   B CD2   1 
ATOM   10369 N  N     . LEU   B 1 552 ? 96.448  114.759 158.850 1.00 60.76  ?  552  LEU   B N     1 
ATOM   10370 C  CA    . LEU   B 1 552 ? 96.999  115.488 159.986 1.00 55.34  ?  552  LEU   B CA    1 
ATOM   10371 C  C     . LEU   B 1 552 ? 96.869  114.685 161.271 1.00 58.80  ?  552  LEU   B C     1 
ATOM   10372 O  O     . LEU   B 1 552 ? 97.787  114.675 162.096 1.00 66.89  ?  552  LEU   B O     1 
ATOM   10373 C  CB    . LEU   B 1 552 ? 96.305  116.840 160.135 1.00 57.10  ?  552  LEU   B CB    1 
ATOM   10374 C  CG    . LEU   B 1 552 ? 96.662  117.905 159.099 1.00 63.72  ?  552  LEU   B CG    1 
ATOM   10375 C  CD1   . LEU   B 1 552 ? 95.839  119.166 159.282 1.00 63.80  ?  552  LEU   B CD1   1 
ATOM   10376 C  CD2   . LEU   B 1 552 ? 98.143  118.235 159.129 1.00 60.53  ?  552  LEU   B CD2   1 
ATOM   10377 N  N     . LYS   B 1 553 ? 95.734  114.009 161.463 1.00 59.90  ?  553  LYS   B N     1 
ATOM   10378 C  CA    . LYS   B 1 553 ? 95.558  113.189 162.657 1.00 56.89  ?  553  LYS   B CA    1 
ATOM   10379 C  C     . LYS   B 1 553 ? 96.557  112.040 162.691 1.00 63.45  ?  553  LYS   B C     1 
ATOM   10380 O  O     . LYS   B 1 553 ? 97.137  111.744 163.743 1.00 69.71  ?  553  LYS   B O     1 
ATOM   10381 C  CB    . LYS   B 1 553 ? 94.127  112.657 162.722 1.00 56.90  ?  553  LYS   B CB    1 
ATOM   10382 C  CG    . LYS   B 1 553 ? 93.249  113.371 163.733 1.00 65.07  ?  553  LYS   B CG    1 
ATOM   10383 C  CD    . LYS   B 1 553 ? 91.866  112.747 163.799 1.00 66.44  ?  553  LYS   B CD    1 
ATOM   10384 C  CE    . LYS   B 1 553 ? 91.910  111.380 164.457 1.00 73.05  ?  553  LYS   B CE    1 
ATOM   10385 N  NZ    . LYS   B 1 553 ? 92.247  111.469 165.903 1.00 74.35  ?  553  LYS   B NZ    1 
ATOM   10386 N  N     . ALA   B 1 554 ? 96.771  111.379 161.551 1.00 69.54  ?  554  ALA   B N     1 
ATOM   10387 C  CA    . ALA   B 1 554 ? 97.739  110.289 161.501 1.00 63.89  ?  554  ALA   B CA    1 
ATOM   10388 C  C     . ALA   B 1 554 ? 99.145  110.785 161.808 1.00 66.39  ?  554  ALA   B C     1 
ATOM   10389 O  O     . ALA   B 1 554 ? 99.876  110.159 162.586 1.00 71.56  ?  554  ALA   B O     1 
ATOM   10390 C  CB    . ALA   B 1 554 ? 97.696  109.611 160.133 1.00 61.35  ?  554  ALA   B CB    1 
ATOM   10391 N  N     . SER   B 1 555 ? 99.538  111.919 161.220 1.00 61.41  ?  555  SER   B N     1 
ATOM   10392 C  CA    . SER   B 1 555 ? 100.864 112.464 161.497 1.00 60.93  ?  555  SER   B CA    1 
ATOM   10393 C  C     . SER   B 1 555 ? 100.999 112.895 162.954 1.00 69.06  ?  555  SER   B C     1 
ATOM   10394 O  O     . SER   B 1 555 ? 102.067 112.739 163.553 1.00 74.26  ?  555  SER   B O     1 
ATOM   10395 C  CB    . SER   B 1 555 ? 101.167 113.634 160.564 1.00 62.04  ?  555  SER   B CB    1 
ATOM   10396 O  OG    . SER   B 1 555 ? 102.566 113.799 160.414 1.00 63.38  ?  555  SER   B OG    1 
ATOM   10397 N  N     . ASN   B 1 556 ? 99.931  113.441 163.541 1.00 68.33  ?  556  ASN   B N     1 
ATOM   10398 C  CA    . ASN   B 1 556 ? 99.975  113.850 164.941 1.00 64.65  ?  556  ASN   B CA    1 
ATOM   10399 C  C     . ASN   B 1 556 ? 100.126 112.651 165.869 1.00 68.88  ?  556  ASN   B C     1 
ATOM   10400 O  O     . ASN   B 1 556 ? 100.901 112.697 166.833 1.00 78.34  ?  556  ASN   B O     1 
ATOM   10401 C  CB    . ASN   B 1 556 ? 98.717  114.646 165.289 1.00 63.96  ?  556  ASN   B CB    1 
ATOM   10402 C  CG    . ASN   B 1 556 ? 98.682  115.078 166.738 1.00 68.53  ?  556  ASN   B CG    1 
ATOM   10403 O  OD1   . ASN   B 1 556 ? 97.897  114.563 167.532 1.00 74.35  ?  556  ASN   B OD1   1 
ATOM   10404 N  ND2   . ASN   B 1 556 ? 99.535  116.030 167.092 1.00 69.81  ?  556  ASN   B ND2   1 
ATOM   10405 N  N     . GLU   B 1 557 ? 99.387  111.571 165.602 1.00 71.42  ?  557  GLU   B N     1 
ATOM   10406 C  CA    . GLU   B 1 557 ? 99.553  110.358 166.395 1.00 73.26  ?  557  GLU   B CA    1 
ATOM   10407 C  C     . GLU   B 1 557 ? 100.958 109.791 166.238 1.00 78.26  ?  557  GLU   B C     1 
ATOM   10408 O  O     . GLU   B 1 557 ? 101.583 109.372 167.221 1.00 82.04  ?  557  GLU   B O     1 
ATOM   10409 C  CB    . GLU   B 1 557 ? 98.508  109.314 166.001 1.00 77.12  ?  557  GLU   B CB    1 
ATOM   10410 C  CG    . GLU   B 1 557 ? 97.066  109.776 166.141 1.00 85.91  ?  557  GLU   B CG    1 
ATOM   10411 C  CD    . GLU   B 1 557 ? 96.659  110.038 167.578 1.00 94.72  ?  557  GLU   B CD    1 
ATOM   10412 O  OE1   . GLU   B 1 557 ? 97.317  109.510 168.500 1.00 93.06  ?  557  GLU   B OE1   1 
ATOM   10413 O  OE2   . GLU   B 1 557 ? 95.658  110.754 167.784 1.00 89.69  ?  557  GLU   B OE2   1 
ATOM   10414 N  N     . LEU   B 1 558 ? 101.478 109.783 165.007 1.00 71.16  ?  558  LEU   B N     1 
ATOM   10415 C  CA    . LEU   B 1 558 ? 102.830 109.279 164.783 1.00 63.26  ?  558  LEU   B CA    1 
ATOM   10416 C  C     . LEU   B 1 558 ? 103.862 110.130 165.509 1.00 67.70  ?  558  LEU   B C     1 
ATOM   10417 O  O     . LEU   B 1 558 ? 104.866 109.609 166.000 1.00 76.96  ?  558  LEU   B O     1 
ATOM   10418 C  CB    . LEU   B 1 558 ? 103.140 109.225 163.287 1.00 65.87  ?  558  LEU   B CB    1 
ATOM   10419 C  CG    . LEU   B 1 558 ? 104.297 108.321 162.858 1.00 71.26  ?  558  LEU   B CG    1 
ATOM   10420 C  CD1   . LEU   B 1 558 ? 104.132 106.958 163.505 1.00 73.67  ?  558  LEU   B CD1   1 
ATOM   10421 C  CD2   . LEU   B 1 558 ? 104.272 108.205 161.347 1.00 72.92  ?  558  LEU   B CD2   1 
ATOM   10422 N  N     . ALA   B 1 559 ? 103.636 111.443 165.583 1.00 72.75  ?  559  ALA   B N     1 
ATOM   10423 C  CA    . ALA   B 1 559 ? 104.567 112.313 166.292 1.00 69.65  ?  559  ALA   B CA    1 
ATOM   10424 C  C     . ALA   B 1 559 ? 104.500 112.092 167.796 1.00 73.44  ?  559  ALA   B C     1 
ATOM   10425 O  O     . ALA   B 1 559 ? 105.538 112.014 168.461 1.00 79.44  ?  559  ALA   B O     1 
ATOM   10426 C  CB    . ALA   B 1 559 ? 104.286 113.772 165.952 1.00 68.10  ?  559  ALA   B CB    1 
ATOM   10427 N  N     . LYS   B 1 560 ? 103.293 111.975 168.350 1.00 79.74  ?  560  LYS   B N     1 
ATOM   10428 C  CA    . LYS   B 1 560 ? 103.169 111.749 169.784 1.00 78.10  ?  560  LYS   B CA    1 
ATOM   10429 C  C     . LYS   B 1 560 ? 103.617 110.350 170.186 1.00 79.85  ?  560  LYS   B C     1 
ATOM   10430 O  O     . LYS   B 1 560 ? 103.864 110.111 171.373 1.00 86.24  ?  560  LYS   B O     1 
ATOM   10431 C  CB    . LYS   B 1 560 ? 101.730 112.000 170.236 1.00 78.08  ?  560  LYS   B CB    1 
ATOM   10432 C  CG    . LYS   B 1 560 ? 100.798 110.818 170.073 1.00 81.07  ?  560  LYS   B CG    1 
ATOM   10433 C  CD    . LYS   B 1 560 ? 99.740  110.812 171.161 1.00 83.63  ?  560  LYS   B CD    1 
ATOM   10434 C  CE    . LYS   B 1 560 ? 98.785  111.983 171.004 1.00 83.95  ?  560  LYS   B CE    1 
ATOM   10435 N  NZ    . LYS   B 1 560 ? 98.215  112.053 169.631 1.00 83.98  ?  560  LYS   B NZ    1 
ATOM   10436 N  N     . GLU   B 1 561 ? 103.724 109.425 169.232 1.00 89.79  ?  561  GLU   B N     1 
ATOM   10437 C  CA    . GLU   B 1 561 ? 104.235 108.092 169.531 1.00 87.00  ?  561  GLU   B CA    1 
ATOM   10438 C  C     . GLU   B 1 561 ? 105.737 107.963 169.301 1.00 88.22  ?  561  GLU   B C     1 
ATOM   10439 O  O     . GLU   B 1 561 ? 106.411 107.249 170.054 1.00 92.97  ?  561  GLU   B O     1 
ATOM   10440 C  CB    . GLU   B 1 561 ? 103.490 107.051 168.688 1.00 88.00  ?  561  GLU   B CB    1 
ATOM   10441 C  CG    . GLU   B 1 561 ? 104.095 105.659 168.710 1.00 89.71  ?  561  GLU   B CG    1 
ATOM   10442 C  CD    . GLU   B 1 561 ? 103.630 104.807 167.546 1.00 94.43  ?  561  GLU   B CD    1 
ATOM   10443 O  OE1   . GLU   B 1 561 ? 102.481 104.993 167.095 1.00 92.35  ?  561  GLU   B OE1   1 
ATOM   10444 O  OE2   . GLU   B 1 561 ? 104.412 103.952 167.082 1.00 92.66  ?  561  GLU   B OE2   1 
ATOM   10445 N  N     . GLN   B 1 562 ? 106.282 108.649 168.296 1.00 78.53  ?  562  GLN   B N     1 
ATOM   10446 C  CA    . GLN   B 1 562 ? 107.664 108.460 167.873 1.00 73.67  ?  562  GLN   B CA    1 
ATOM   10447 C  C     . GLN   B 1 562 ? 108.474 109.750 167.876 1.00 74.39  ?  562  GLN   B C     1 
ATOM   10448 O  O     . GLN   B 1 562 ? 109.573 109.776 167.310 1.00 78.84  ?  562  GLN   B O     1 
ATOM   10449 C  CB    . GLN   B 1 562 ? 107.703 107.841 166.472 1.00 76.37  ?  562  GLN   B CB    1 
ATOM   10450 C  CG    . GLN   B 1 562 ? 108.007 106.357 166.439 1.00 81.30  ?  562  GLN   B CG    1 
ATOM   10451 C  CD    . GLN   B 1 562 ? 108.031 105.810 165.028 1.00 85.39  ?  562  GLN   B CD    1 
ATOM   10452 O  OE1   . GLN   B 1 562 ? 108.565 106.441 164.117 1.00 85.38  ?  562  GLN   B OE1   1 
ATOM   10453 N  NE2   . GLN   B 1 562 ? 107.463 104.624 164.841 1.00 84.77  ?  562  GLN   B NE2   1 
ATOM   10454 N  N     . GLY   B 1 563 ? 107.972 110.813 168.483 1.00 79.51  ?  563  GLY   B N     1 
ATOM   10455 C  CA    . GLY   B 1 563 ? 108.693 112.077 168.450 1.00 76.08  ?  563  GLY   B CA    1 
ATOM   10456 C  C     . GLY   B 1 563 ? 108.275 112.944 167.279 1.00 75.82  ?  563  GLY   B C     1 
ATOM   10457 O  O     . GLY   B 1 563 ? 107.898 112.466 166.212 1.00 80.73  ?  563  GLY   B O     1 
ATOM   10458 N  N     . ALA   B 1 564 ? 108.351 114.254 167.487 1.00 84.33  ?  564  ALA   B N     1 
ATOM   10459 C  CA    . ALA   B 1 564 ? 107.925 115.203 166.473 1.00 82.30  ?  564  ALA   B CA    1 
ATOM   10460 C  C     . ALA   B 1 564 ? 109.013 115.396 165.421 1.00 85.24  ?  564  ALA   B C     1 
ATOM   10461 O  O     . ALA   B 1 564 ? 110.114 114.848 165.513 1.00 92.55  ?  564  ALA   B O     1 
ATOM   10462 C  CB    . ALA   B 1 564 ? 107.550 116.533 167.115 1.00 79.09  ?  564  ALA   B CB    1 
ATOM   10463 N  N     . CYS   B 1 565 ? 108.660 116.136 164.377 1.00 78.41  ?  565  CYS   B N     1 
ATOM   10464 C  CA    . CYS   B 1 565 ? 109.585 116.397 163.286 1.00 75.53  ?  565  CYS   B CA    1 
ATOM   10465 C  C     . CYS   B 1 565 ? 110.712 117.308 163.768 1.00 80.01  ?  565  CYS   B C     1 
ATOM   10466 O  O     . CYS   B 1 565 ? 110.462 118.265 164.507 1.00 87.61  ?  565  CYS   B O     1 
ATOM   10467 C  CB    . CYS   B 1 565 ? 108.836 117.033 162.116 1.00 82.58  ?  565  CYS   B CB    1 
ATOM   10468 S  SG    . CYS   B 1 565 ? 109.820 118.047 161.022 1.00 96.41  ?  565  CYS   B SG    1 
ATOM   10469 N  N     . PRO   B 1 566 ? 111.963 117.032 163.378 1.00 66.12  ?  566  PRO   B N     1 
ATOM   10470 C  CA    . PRO   B 1 566 ? 113.084 117.824 163.912 1.00 68.03  ?  566  PRO   B CA    1 
ATOM   10471 C  C     . PRO   B 1 566 ? 113.008 119.307 163.592 1.00 68.19  ?  566  PRO   B C     1 
ATOM   10472 O  O     . PRO   B 1 566 ? 113.394 120.135 164.427 1.00 68.21  ?  566  PRO   B O     1 
ATOM   10473 C  CB    . PRO   B 1 566 ? 114.300 117.153 163.259 1.00 63.99  ?  566  PRO   B CB    1 
ATOM   10474 C  CG    . PRO   B 1 566 ? 113.834 115.741 163.058 1.00 63.76  ?  566  PRO   B CG    1 
ATOM   10475 C  CD    . PRO   B 1 566 ? 112.456 115.950 162.513 1.00 66.88  ?  566  PRO   B CD    1 
ATOM   10476 N  N     . TRP   B 1 567 ? 112.524 119.672 162.406 1.00 70.22  ?  567  TRP   B N     1 
ATOM   10477 C  CA    . TRP   B 1 567 ? 112.370 121.069 162.019 1.00 60.55  ?  567  TRP   B CA    1 
ATOM   10478 C  C     . TRP   B 1 567 ? 110.909 121.504 162.056 1.00 68.32  ?  567  TRP   B C     1 
ATOM   10479 O  O     . TRP   B 1 567 ? 110.492 122.372 161.286 1.00 79.23  ?  567  TRP   B O     1 
ATOM   10480 C  CB    . TRP   B 1 567 ? 112.959 121.318 160.632 1.00 63.54  ?  567  TRP   B CB    1 
ATOM   10481 C  CG    . TRP   B 1 567 ? 114.442 121.153 160.562 1.00 69.57  ?  567  TRP   B CG    1 
ATOM   10482 C  CD1   . TRP   B 1 567 ? 115.292 120.920 161.601 1.00 71.57  ?  567  TRP   B CD1   1 
ATOM   10483 C  CD2   . TRP   B 1 567 ? 115.254 121.209 159.384 1.00 72.94  ?  567  TRP   B CD2   1 
ATOM   10484 N  NE1   . TRP   B 1 567 ? 116.584 120.827 161.144 1.00 70.05  ?  567  TRP   B NE1   1 
ATOM   10485 C  CE2   . TRP   B 1 567 ? 116.586 121.001 159.785 1.00 73.28  ?  567  TRP   B CE2   1 
ATOM   10486 C  CE3   . TRP   B 1 567 ? 114.983 121.416 158.029 1.00 72.03  ?  567  TRP   B CE3   1 
ATOM   10487 C  CZ2   . TRP   B 1 567 ? 117.644 120.993 158.881 1.00 75.53  ?  567  TRP   B CZ2   1 
ATOM   10488 C  CZ3   . TRP   B 1 567 ? 116.034 121.407 157.133 1.00 71.57  ?  567  TRP   B CZ3   1 
ATOM   10489 C  CH2   . TRP   B 1 567 ? 117.348 121.196 157.562 1.00 72.05  ?  567  TRP   B CH2   1 
ATOM   10490 N  N     . PHE   B 1 568 ? 110.121 120.901 162.949 1.00 68.05  ?  568  PHE   B N     1 
ATOM   10491 C  CA    . PHE   B 1 568 ? 108.710 121.251 163.052 1.00 63.04  ?  568  PHE   B CA    1 
ATOM   10492 C  C     . PHE   B 1 568 ? 108.520 122.695 163.493 1.00 74.20  ?  568  PHE   B C     1 
ATOM   10493 O  O     . PHE   B 1 568 ? 107.502 123.315 163.166 1.00 83.74  ?  568  PHE   B O     1 
ATOM   10494 C  CB    . PHE   B 1 568 ? 108.010 120.298 164.021 1.00 67.65  ?  568  PHE   B CB    1 
ATOM   10495 C  CG    . PHE   B 1 568 ? 106.564 120.617 164.247 1.00 69.93  ?  568  PHE   B CG    1 
ATOM   10496 C  CD1   . PHE   B 1 568 ? 105.645 120.494 163.221 1.00 69.25  ?  568  PHE   B CD1   1 
ATOM   10497 C  CD2   . PHE   B 1 568 ? 106.123 121.040 165.488 1.00 73.89  ?  568  PHE   B CD2   1 
ATOM   10498 C  CE1   . PHE   B 1 568 ? 104.314 120.787 163.429 1.00 71.55  ?  568  PHE   B CE1   1 
ATOM   10499 C  CE2   . PHE   B 1 568 ? 104.793 121.335 165.700 1.00 76.46  ?  568  PHE   B CE2   1 
ATOM   10500 C  CZ    . PHE   B 1 568 ? 103.888 121.207 164.671 1.00 73.11  ?  568  PHE   B CZ    1 
ATOM   10501 N  N     . ASN   B 1 569 ? 109.488 123.250 164.227 1.00 79.89  ?  569  ASN   B N     1 
ATOM   10502 C  CA    A ASN   B 1 569 ? 109.393 124.634 164.678 0.50 75.07  ?  569  ASN   B CA    1 
ATOM   10503 C  CA    B ASN   B 1 569 ? 109.493 124.634 164.678 0.50 75.07  ?  569  ASN   B CA    1 
ATOM   10504 C  C     . ASN   B 1 569 ? 109.426 125.628 163.524 1.00 81.13  ?  569  ASN   B C     1 
ATOM   10505 O  O     . ASN   B 1 569 ? 109.000 126.774 163.699 1.00 89.21  ?  569  ASN   B O     1 
ATOM   10506 C  CB    A ASN   B 1 569 ? 110.523 124.946 165.662 0.50 78.33  ?  569  ASN   B CB    1 
ATOM   10507 C  CB    B ASN   B 1 569 ? 110.623 124.946 165.662 0.50 78.33  ?  569  ASN   B CB    1 
ATOM   10508 C  CG    A ASN   B 1 569 ? 111.863 125.100 164.974 0.50 84.22  ?  569  ASN   B CG    1 
ATOM   10509 C  CG    B ASN   B 1 569 ? 110.404 124.306 167.017 0.50 84.22  ?  569  ASN   B CG    1 
ATOM   10510 O  OD1   A ASN   B 1 569 ? 112.311 124.204 164.262 0.50 86.06  ?  569  ASN   B OD1   1 
ATOM   10511 O  OD1   B ASN   B 1 569 ? 109.275 123.992 167.389 0.50 86.06  ?  569  ASN   B OD1   1 
ATOM   10512 N  ND2   A ASN   B 1 569 ? 112.493 126.254 165.154 0.50 85.84  ?  569  ASN   B ND2   1 
ATOM   10513 N  ND2   B ASN   B 1 569 ? 111.488 124.075 167.746 0.50 85.84  ?  569  ASN   B ND2   1 
ATOM   10514 N  N     . GLU   B 1 570 ? 109.918 125.220 162.356 1.00 80.32  ?  570  GLU   B N     1 
ATOM   10515 C  CA    . GLU   B 1 570 ? 109.971 126.097 161.194 1.00 80.13  ?  570  GLU   B CA    1 
ATOM   10516 C  C     . GLU   B 1 570 ? 108.671 126.113 160.403 1.00 84.13  ?  570  GLU   B C     1 
ATOM   10517 O  O     . GLU   B 1 570 ? 108.584 126.832 159.402 1.00 86.08  ?  570  GLU   B O     1 
ATOM   10518 C  CB    . GLU   B 1 570 ? 111.123 125.685 160.275 1.00 80.88  ?  570  GLU   B CB    1 
ATOM   10519 C  CG    . GLU   B 1 570 ? 112.488 126.149 160.748 1.00 84.74  ?  570  GLU   B CG    1 
ATOM   10520 C  CD    . GLU   B 1 570 ? 113.616 125.608 159.893 1.00 90.79  ?  570  GLU   B CD    1 
ATOM   10521 O  OE1   . GLU   B 1 570 ? 113.351 125.215 158.739 1.00 91.14  ?  570  GLU   B OE1   1 
ATOM   10522 O  OE2   . GLU   B 1 570 ? 114.763 125.559 160.381 1.00 90.53  ?  570  GLU   B OE2   1 
ATOM   10523 N  N     . THR   B 1 571 ? 107.669 125.347 160.819 1.00 77.13  ?  571  THR   B N     1 
ATOM   10524 C  CA    . THR   B 1 571 ? 106.402 125.262 160.112 1.00 74.42  ?  571  THR   B CA    1 
ATOM   10525 C  C     . THR   B 1 571 ? 105.337 126.090 160.820 1.00 72.18  ?  571  THR   B C     1 
ATOM   10526 O  O     . THR   B 1 571 ? 105.413 126.335 162.027 1.00 79.25  ?  571  THR   B O     1 
ATOM   10527 C  CB    . THR   B 1 571 ? 105.936 123.809 160.002 1.00 71.85  ?  571  THR   B CB    1 
ATOM   10528 O  OG1   . THR   B 1 571 ? 105.725 123.272 161.312 1.00 74.96  ?  571  THR   B OG1   1 
ATOM   10529 C  CG2   . THR   B 1 571 ? 106.972 122.969 159.276 1.00 71.11  ?  571  THR   B CG2   1 
ATOM   10530 N  N     . THR   B 1 572 ? 104.338 126.525 160.049 1.00 68.76  ?  572  THR   B N     1 
ATOM   10531 C  CA    . THR   B 1 572 ? 103.232 127.284 160.621 1.00 68.45  ?  572  THR   B CA    1 
ATOM   10532 C  C     . THR   B 1 572 ? 102.345 126.428 161.515 1.00 70.48  ?  572  THR   B C     1 
ATOM   10533 O  O     . THR   B 1 572 ? 101.584 126.979 162.318 1.00 74.75  ?  572  THR   B O     1 
ATOM   10534 C  CB    . THR   B 1 572 ? 102.391 127.918 159.511 1.00 69.25  ?  572  THR   B CB    1 
ATOM   10535 O  OG1   . THR   B 1 572 ? 101.793 126.889 158.714 1.00 72.10  ?  572  THR   B OG1   1 
ATOM   10536 C  CG2   . THR   B 1 572 ? 103.255 128.802 158.627 1.00 66.69  ?  572  THR   B CG2   1 
ATOM   10537 N  N     . TYR   B 1 573 ? 102.422 125.100 161.392 1.00 69.62  ?  573  TYR   B N     1 
ATOM   10538 C  CA    . TYR   B 1 573 ? 101.660 124.230 162.282 1.00 67.74  ?  573  TYR   B CA    1 
ATOM   10539 C  C     . TYR   B 1 573 ? 102.116 124.372 163.726 1.00 71.52  ?  573  TYR   B C     1 
ATOM   10540 O  O     . TYR   B 1 573 ? 101.317 124.187 164.651 1.00 75.68  ?  573  TYR   B O     1 
ATOM   10541 C  CB    . TYR   B 1 573 ? 101.789 122.773 161.841 1.00 67.62  ?  573  TYR   B CB    1 
ATOM   10542 C  CG    . TYR   B 1 573 ? 101.008 122.420 160.599 1.00 68.06  ?  573  TYR   B CG    1 
ATOM   10543 C  CD1   . TYR   B 1 573 ? 99.631  122.262 160.643 1.00 68.61  ?  573  TYR   B CD1   1 
ATOM   10544 C  CD2   . TYR   B 1 573 ? 101.650 122.223 159.386 1.00 66.93  ?  573  TYR   B CD2   1 
ATOM   10545 C  CE1   . TYR   B 1 573 ? 98.915  121.933 159.510 1.00 71.72  ?  573  TYR   B CE1   1 
ATOM   10546 C  CE2   . TYR   B 1 573 ? 100.943 121.892 158.250 1.00 68.68  ?  573  TYR   B CE2   1 
ATOM   10547 C  CZ    . TYR   B 1 573 ? 99.578  121.749 158.317 1.00 71.85  ?  573  TYR   B CZ    1 
ATOM   10548 O  OH    . TYR   B 1 573 ? 98.876  121.416 157.184 1.00 75.41  ?  573  TYR   B OH    1 
ATOM   10549 N  N     . ALA   B 1 574 ? 103.391 124.703 163.940 1.00 75.87  ?  574  ALA   B N     1 
ATOM   10550 C  CA    . ALA   B 1 574 ? 103.910 124.841 165.292 1.00 77.15  ?  574  ALA   B CA    1 
ATOM   10551 C  C     . ALA   B 1 574 ? 103.338 126.043 166.021 1.00 79.96  ?  574  ALA   B C     1 
ATOM   10552 O  O     . ALA   B 1 574 ? 103.414 126.082 167.253 1.00 81.50  ?  574  ALA   B O     1 
ATOM   10553 C  CB    . ALA   B 1 574 ? 105.434 124.929 165.266 1.00 75.73  ?  574  ALA   B CB    1 
ATOM   10554 N  N     . LYS   B 1 575 ? 102.762 127.004 165.298 1.00 79.55  ?  575  LYS   B N     1 
ATOM   10555 C  CA    . LYS   B 1 575 ? 102.147 128.182 165.886 1.00 80.47  ?  575  LYS   B CA    1 
ATOM   10556 C  C     . LYS   B 1 575 ? 100.628 128.095 165.912 1.00 82.83  ?  575  LYS   B C     1 
ATOM   10557 O  O     . LYS   B 1 575 ? 99.966  129.099 166.184 1.00 89.36  ?  575  LYS   B O     1 
ATOM   10558 C  CB    . LYS   B 1 575 ? 102.594 129.431 165.127 1.00 79.70  ?  575  LYS   B CB    1 
ATOM   10559 C  CG    . LYS   B 1 575 ? 104.054 129.400 164.716 1.00 78.64  ?  575  LYS   B CG    1 
ATOM   10560 C  CD    . LYS   B 1 575 ? 104.275 130.086 163.383 1.00 83.02  ?  575  LYS   B CD    1 
ATOM   10561 C  CE    . LYS   B 1 575 ? 105.757 130.306 163.140 1.00 83.93  ?  575  LYS   B CE    1 
ATOM   10562 N  NZ    . LYS   B 1 575 ? 106.487 129.016 162.988 1.00 85.08  ?  575  LYS   B NZ    1 
ATOM   10563 N  N     . GLY   B 1 576 ? 100.062 126.922 165.639 1.00 73.54  ?  576  GLY   B N     1 
ATOM   10564 C  CA    . GLY   B 1 576 ? 98.624  126.754 165.646 1.00 74.42  ?  576  GLY   B CA    1 
ATOM   10565 C  C     . GLY   B 1 576 ? 97.920  127.157 164.372 1.00 75.91  ?  576  GLY   B C     1 
ATOM   10566 O  O     . GLY   B 1 576 ? 96.684  127.183 164.351 1.00 80.45  ?  576  GLY   B O     1 
ATOM   10567 N  N     . ILE   B 1 577 ? 98.660  127.486 163.317 1.00 77.68  ?  577  ILE   B N     1 
ATOM   10568 C  CA    . ILE   B 1 577 ? 98.061  127.886 162.049 1.00 78.72  ?  577  ILE   B CA    1 
ATOM   10569 C  C     . ILE   B 1 577 ? 97.733  126.638 161.242 1.00 78.58  ?  577  ILE   B C     1 
ATOM   10570 O  O     . ILE   B 1 577 ? 98.602  125.793 161.001 1.00 81.64  ?  577  ILE   B O     1 
ATOM   10571 C  CB    . ILE   B 1 577 ? 99.002  128.818 161.270 1.00 80.28  ?  577  ILE   B CB    1 
ATOM   10572 C  CG1   . ILE   B 1 577 ? 99.176  130.145 162.009 1.00 79.09  ?  577  ILE   B CG1   1 
ATOM   10573 C  CG2   . ILE   B 1 577 ? 98.473  129.058 159.865 1.00 76.67  ?  577  ILE   B CG2   1 
ATOM   10574 C  CD1   . ILE   B 1 577 ? 100.550 130.750 161.849 1.00 80.58  ?  577  ILE   B CD1   1 
ATOM   10575 N  N     . LEU   B 1 578 ? 96.481  126.523 160.823 1.00 74.15  ?  578  LEU   B N     1 
ATOM   10576 C  CA    . LEU   B 1 578 ? 95.977  125.388 160.070 1.00 72.02  ?  578  LEU   B CA    1 
ATOM   10577 C  C     . LEU   B 1 578 ? 95.640  125.796 158.641 1.00 78.50  ?  578  LEU   B C     1 
ATOM   10578 O  O     . LEU   B 1 578 ? 95.475  126.985 158.347 1.00 82.98  ?  578  LEU   B O     1 
ATOM   10579 C  CB    . LEU   B 1 578 ? 94.729  124.810 160.752 1.00 69.44  ?  578  LEU   B CB    1 
ATOM   10580 C  CG    . LEU   B 1 578 ? 94.982  123.985 162.015 1.00 71.06  ?  578  LEU   B CG    1 
ATOM   10581 C  CD1   . LEU   B 1 578 ? 93.681  123.419 162.556 1.00 72.48  ?  578  LEU   B CD1   1 
ATOM   10582 C  CD2   . LEU   B 1 578 ? 95.981  122.874 161.738 1.00 71.62  ?  578  LEU   B CD2   1 
ATOM   10583 N  N     . PRO   B 1 579 ? 95.544  124.835 157.717 1.00 80.11  ?  579  PRO   B N     1 
ATOM   10584 C  CA    . PRO   B 1 579 ? 95.155  125.184 156.340 1.00 74.39  ?  579  PRO   B CA    1 
ATOM   10585 C  C     . PRO   B 1 579 ? 93.775  125.806 156.237 1.00 74.80  ?  579  PRO   B C     1 
ATOM   10586 O  O     . PRO   B 1 579 ? 93.481  126.463 155.231 1.00 81.38  ?  579  PRO   B O     1 
ATOM   10587 C  CB    . PRO   B 1 579 ? 95.217  123.839 155.603 1.00 72.39  ?  579  PRO   B CB    1 
ATOM   10588 C  CG    . PRO   B 1 579 ? 96.127  122.996 156.420 1.00 74.30  ?  579  PRO   B CG    1 
ATOM   10589 C  CD    . PRO   B 1 579 ? 95.919  123.416 157.840 1.00 74.41  ?  579  PRO   B CD    1 
ATOM   10590 N  N     . ILE   B 1 580 ? 92.922  125.628 157.244 1.00 74.26  ?  580  ILE   B N     1 
ATOM   10591 C  CA    . ILE   B 1 580 ? 91.574  126.184 157.234 1.00 74.67  ?  580  ILE   B CA    1 
ATOM   10592 C  C     . ILE   B 1 580 ? 91.614  127.624 157.727 1.00 76.96  ?  580  ILE   B C     1 
ATOM   10593 O  O     . ILE   B 1 580 ? 90.570  128.234 157.983 1.00 79.27  ?  580  ILE   B O     1 
ATOM   10594 C  CB    . ILE   B 1 580 ? 90.617  125.336 158.091 1.00 74.56  ?  580  ILE   B CB    1 
ATOM   10595 C  CG1   . ILE   B 1 580 ? 91.152  125.209 159.518 1.00 75.98  ?  580  ILE   B CG1   1 
ATOM   10596 C  CG2   . ILE   B 1 580 ? 90.423  123.963 157.471 1.00 70.68  ?  580  ILE   B CG2   1 
ATOM   10597 C  CD1   . ILE   B 1 580 ? 90.082  125.299 160.581 1.00 77.59  ?  580  ILE   B CD1   1 
ATOM   10598 N  N     . ASP   B 1 581 ? 92.818  128.174 157.872 1.00 84.08  ?  581  ASP   B N     1 
ATOM   10599 C  CA    . ASP   B 1 581 ? 93.002  129.538 158.346 1.00 84.45  ?  581  ASP   B CA    1 
ATOM   10600 C  C     . ASP   B 1 581 ? 93.623  130.474 157.321 1.00 85.09  ?  581  ASP   B C     1 
ATOM   10601 O  O     . ASP   B 1 581 ? 93.268  131.654 157.296 1.00 87.26  ?  581  ASP   B O     1 
ATOM   10602 C  CB    . ASP   B 1 581 ? 93.874  129.548 159.610 1.00 82.15  ?  581  ASP   B CB    1 
ATOM   10603 C  CG    . ASP   B 1 581 ? 93.170  128.946 160.808 1.00 90.44  ?  581  ASP   B CG    1 
ATOM   10604 O  OD1   . ASP   B 1 581 ? 91.954  129.180 160.964 1.00 93.48  ?  581  ASP   B OD1   1 
ATOM   10605 O  OD2   . ASP   B 1 581 ? 93.836  128.254 161.605 1.00 89.51  ?  581  ASP   B OD2   1 
ATOM   10606 N  N     . THR   B 1 582 ? 94.533  129.988 156.479 1.00 78.87  ?  582  THR   B N     1 
ATOM   10607 C  CA    . THR   B 1 582 ? 95.261  130.834 155.543 1.00 76.78  ?  582  THR   B CA    1 
ATOM   10608 C  C     . THR   B 1 582 ? 94.777  130.690 154.105 1.00 80.51  ?  582  THR   B C     1 
ATOM   10609 O  O     . THR   B 1 582 ? 95.456  131.157 153.185 1.00 80.19  ?  582  THR   B O     1 
ATOM   10610 C  CB    . THR   B 1 582 ? 96.760  130.532 155.616 1.00 75.96  ?  582  THR   B CB    1 
ATOM   10611 O  OG1   . THR   B 1 582 ? 96.965  129.115 155.659 1.00 82.22  ?  582  THR   B OG1   1 
ATOM   10612 C  CG2   . THR   B 1 582 ? 97.377  131.162 156.855 1.00 76.45  ?  582  THR   B CG2   1 
ATOM   10613 N  N     . TYR   B 1 583 ? 93.629  130.056 153.886 1.00 76.01  ?  583  TYR   B N     1 
ATOM   10614 C  CA    . TYR   B 1 583 ? 93.113  129.902 152.535 1.00 74.07  ?  583  TYR   B CA    1 
ATOM   10615 C  C     . TYR   B 1 583 ? 92.582  131.232 152.005 1.00 80.93  ?  583  TYR   B C     1 
ATOM   10616 O  O     . TYR   B 1 583 ? 92.226  132.139 152.763 1.00 85.05  ?  583  TYR   B O     1 
ATOM   10617 C  CB    . TYR   B 1 583 ? 92.012  128.841 152.496 1.00 72.09  ?  583  TYR   B CB    1 
ATOM   10618 C  CG    . TYR   B 1 583 ? 90.718  129.267 153.152 1.00 77.15  ?  583  TYR   B CG    1 
ATOM   10619 C  CD1   . TYR   B 1 583 ? 90.576  129.245 154.531 1.00 78.54  ?  583  TYR   B CD1   1 
ATOM   10620 C  CD2   . TYR   B 1 583 ? 89.637  129.686 152.391 1.00 77.67  ?  583  TYR   B CD2   1 
ATOM   10621 C  CE1   . TYR   B 1 583 ? 89.395  129.633 155.133 1.00 79.99  ?  583  TYR   B CE1   1 
ATOM   10622 C  CE2   . TYR   B 1 583 ? 88.452  130.075 152.984 1.00 77.46  ?  583  TYR   B CE2   1 
ATOM   10623 C  CZ    . TYR   B 1 583 ? 88.337  130.046 154.354 1.00 77.64  ?  583  TYR   B CZ    1 
ATOM   10624 O  OH    . TYR   B 1 583 ? 87.159  130.433 154.950 1.00 79.25  ?  583  TYR   B OH    1 
ATOM   10625 N  N     . LYS   B 1 584 ? 92.539  131.341 150.679 1.00 80.60  ?  584  LYS   B N     1 
ATOM   10626 C  CA    . LYS   B 1 584 ? 92.055  132.557 150.038 1.00 81.64  ?  584  LYS   B CA    1 
ATOM   10627 C  C     . LYS   B 1 584 ? 90.567  132.742 150.310 1.00 82.61  ?  584  LYS   B C     1 
ATOM   10628 O  O     . LYS   B 1 584 ? 89.778  131.804 150.169 1.00 86.32  ?  584  LYS   B O     1 
ATOM   10629 C  CB    . LYS   B 1 584 ? 92.315  132.502 148.535 1.00 72.90  ?  584  LYS   B CB    1 
ATOM   10630 C  CG    . LYS   B 1 584 ? 92.176  133.840 147.840 1.00 74.01  ?  584  LYS   B CG    1 
ATOM   10631 C  CD    . LYS   B 1 584 ? 93.392  134.147 146.995 1.00 73.75  ?  584  LYS   B CD    1 
ATOM   10632 C  CE    . LYS   B 1 584 ? 93.367  135.577 146.488 1.00 80.15  ?  584  LYS   B CE    1 
ATOM   10633 N  NZ    . LYS   B 1 584 ? 92.215  135.815 145.583 1.00 84.84  ?  584  LYS   B NZ    1 
ATOM   10634 N  N     . LYS   B 1 585 ? 90.183  133.963 150.690 1.00 81.63  ?  585  LYS   B N     1 
ATOM   10635 C  CA    . LYS   B 1 585 ? 88.809  134.219 151.105 1.00 82.17  ?  585  LYS   B CA    1 
ATOM   10636 C  C     . LYS   B 1 585 ? 87.823  134.186 149.945 1.00 84.68  ?  585  LYS   B C     1 
ATOM   10637 O  O     . LYS   B 1 585 ? 86.630  133.955 150.175 1.00 84.76  ?  585  LYS   B O     1 
ATOM   10638 C  CB    . LYS   B 1 585 ? 88.722  135.563 151.829 1.00 81.61  ?  585  LYS   B CB    1 
ATOM   10639 C  CG    . LYS   B 1 585 ? 89.196  135.527 153.276 1.00 83.93  ?  585  LYS   B CG    1 
ATOM   10640 C  CD    . LYS   B 1 585 ? 89.056  134.139 153.858 1.00 84.02  ?  585  LYS   B CD    1 
ATOM   10641 C  CE    . LYS   B 1 585 ? 89.066  134.132 155.377 1.00 86.16  ?  585  LYS   B CE    1 
ATOM   10642 N  NZ    . LYS   B 1 585 ? 88.129  133.121 155.937 1.00 84.58  ?  585  LYS   B NZ    1 
ATOM   10643 N  N     . ASP   B 1 586 ? 88.284  134.408 148.711 1.00 88.77  ?  586  ASP   B N     1 
ATOM   10644 C  CA    . ASP   B 1 586 ? 87.385  134.332 147.564 1.00 90.13  ?  586  ASP   B CA    1 
ATOM   10645 C  C     . ASP   B 1 586 ? 86.740  132.959 147.445 1.00 90.94  ?  586  ASP   B C     1 
ATOM   10646 O  O     . ASP   B 1 586 ? 85.642  132.842 146.887 1.00 93.33  ?  586  ASP   B O     1 
ATOM   10647 C  CB    . ASP   B 1 586 ? 88.139  134.674 146.277 1.00 88.96  ?  586  ASP   B CB    1 
ATOM   10648 C  CG    . ASP   B 1 586 ? 88.962  135.942 146.404 1.00 95.03  ?  586  ASP   B CG    1 
ATOM   10649 O  OD1   . ASP   B 1 586 ? 89.794  136.023 147.331 1.00 96.24  ?  586  ASP   B OD1   1 
ATOM   10650 O  OD2   . ASP   B 1 586 ? 88.769  136.862 145.582 1.00 93.96  ?  586  ASP   B OD2   1 
ATOM   10651 N  N     . LEU   B 1 587 ? 87.387  131.925 147.986 1.00 76.44  ?  587  LEU   B N     1 
ATOM   10652 C  CA    . LEU   B 1 587 ? 86.818  130.585 147.980 1.00 72.21  ?  587  LEU   B CA    1 
ATOM   10653 C  C     . LEU   B 1 587 ? 85.483  130.522 148.703 1.00 77.60  ?  587  LEU   B C     1 
ATOM   10654 O  O     . LEU   B 1 587 ? 84.700  129.599 148.454 1.00 81.86  ?  587  LEU   B O     1 
ATOM   10655 C  CB    . LEU   B 1 587 ? 87.797  129.605 148.622 1.00 71.19  ?  587  LEU   B CB    1 
ATOM   10656 C  CG    . LEU   B 1 587 ? 89.010  129.217 147.781 1.00 73.85  ?  587  LEU   B CG    1 
ATOM   10657 C  CD1   . LEU   B 1 587 ? 89.677  128.010 148.388 1.00 72.88  ?  587  LEU   B CD1   1 
ATOM   10658 C  CD2   . LEU   B 1 587 ? 88.602  128.940 146.346 1.00 75.67  ?  587  LEU   B CD2   1 
ATOM   10659 N  N     . ASP   B 1 588 ? 85.205  131.475 149.595 1.00 86.78  ?  588  ASP   B N     1 
ATOM   10660 C  CA    . ASP   B 1 588 ? 83.920  131.492 150.281 1.00 88.54  ?  588  ASP   B CA    1 
ATOM   10661 C  C     . ASP   B 1 588 ? 82.767  131.819 149.342 1.00 88.63  ?  588  ASP   B C     1 
ATOM   10662 O  O     . ASP   B 1 588 ? 81.616  131.507 149.665 1.00 86.96  ?  588  ASP   B O     1 
ATOM   10663 C  CB    . ASP   B 1 588 ? 83.952  132.492 151.437 1.00 88.83  ?  588  ASP   B CB    1 
ATOM   10664 C  CG    . ASP   B 1 588 ? 84.737  131.978 152.626 1.00 96.10  ?  588  ASP   B CG    1 
ATOM   10665 O  OD1   . ASP   B 1 588 ? 84.255  131.051 153.308 1.00 99.58  ?  588  ASP   B OD1   1 
ATOM   10666 O  OD2   . ASP   B 1 588 ? 85.848  132.487 152.870 1.00 93.51  ?  588  ASP   B OD2   1 
ATOM   10667 N  N     . THR   B 1 589 ? 83.043  132.434 148.191 1.00 87.78  ?  589  THR   B N     1 
ATOM   10668 C  CA    . THR   B 1 589 ? 81.977  132.791 147.265 1.00 84.93  ?  589  THR   B CA    1 
ATOM   10669 C  C     . THR   B 1 589 ? 81.524  131.626 146.392 1.00 87.45  ?  589  THR   B C     1 
ATOM   10670 O  O     . THR   B 1 589 ? 80.475  131.731 145.748 1.00 89.14  ?  589  THR   B O     1 
ATOM   10671 C  CB    . THR   B 1 589 ? 82.416  133.951 146.367 1.00 86.76  ?  589  THR   B CB    1 
ATOM   10672 O  OG1   . THR   B 1 589 ? 83.183  133.440 145.272 1.00 88.10  ?  589  THR   B OG1   1 
ATOM   10673 C  CG2   . THR   B 1 589 ? 83.245  134.963 147.148 1.00 85.08  ?  589  THR   B CG2   1 
ATOM   10674 N  N     . ILE   B 1 590 ? 82.272  130.526 146.354 1.00 80.95  ?  590  ILE   B N     1 
ATOM   10675 C  CA    . ILE   B 1 590 ? 81.916  129.390 145.514 1.00 80.69  ?  590  ILE   B CA    1 
ATOM   10676 C  C     . ILE   B 1 590 ? 81.629  128.122 146.305 1.00 77.50  ?  590  ILE   B C     1 
ATOM   10677 O  O     . ILE   B 1 590 ? 81.027  127.189 145.749 1.00 80.68  ?  590  ILE   B O     1 
ATOM   10678 C  CB    . ILE   B 1 590 ? 83.006  129.119 144.455 1.00 78.01  ?  590  ILE   B CB    1 
ATOM   10679 C  CG1   . ILE   B 1 590 ? 84.374  128.961 145.120 1.00 74.64  ?  590  ILE   B CG1   1 
ATOM   10680 C  CG2   . ILE   B 1 590 ? 83.035  130.235 143.425 1.00 78.19  ?  590  ILE   B CG2   1 
ATOM   10681 C  CD1   . ILE   B 1 590 ? 85.308  128.039 144.375 1.00 77.05  ?  590  ILE   B CD1   1 
ATOM   10682 N  N     . ALA   B 1 591 ? 82.031  128.036 147.570 1.00 84.39  ?  591  ALA   B N     1 
ATOM   10683 C  CA    . ALA   B 1 591 ? 81.755  126.875 148.403 1.00 87.16  ?  591  ALA   B CA    1 
ATOM   10684 C  C     . ALA   B 1 591 ? 81.147  127.339 149.712 1.00 89.25  ?  591  ALA   B C     1 
ATOM   10685 O  O     . ALA   B 1 591 ? 81.681  128.240 150.370 1.00 92.12  ?  591  ALA   B O     1 
ATOM   10686 C  CB    . ALA   B 1 591 ? 83.020  126.054 148.669 1.00 87.24  ?  591  ALA   B CB    1 
ATOM   10687 N  N     . ASN   B 1 592 ? 80.025  126.716 150.067 1.00 89.08  ?  592  ASN   B N     1 
ATOM   10688 C  CA    . ASN   B 1 592 ? 79.272  126.976 151.282 1.00 89.02  ?  592  ASN   B CA    1 
ATOM   10689 C  C     . ASN   B 1 592 ? 79.296  125.844 152.271 1.00 91.56  ?  592  ASN   B C     1 
ATOM   10690 O  O     . ASN   B 1 592 ? 78.519  125.897 153.213 1.00 92.58  ?  592  ASN   B O     1 
ATOM   10691 C  CB    . ASN   B 1 592 ? 77.784  127.230 151.005 1.00 90.01  ?  592  ASN   B CB    1 
ATOM   10692 C  CG    . ASN   B 1 592 ? 76.988  125.965 150.636 1.00 94.45  ?  592  ASN   B CG    1 
ATOM   10693 O  OD1   . ASN   B 1 592 ? 77.286  124.872 151.071 1.00 97.21  ?  592  ASN   B OD1   1 
ATOM   10694 N  ND2   . ASN   B 1 592 ? 75.950  126.138 149.824 1.00 92.44  ?  592  ASN   B ND2   1 
ATOM   10695 N  N     . GLU   B 1 593 ? 80.104  124.815 152.069 1.00 90.67  ?  593  GLU   B N     1 
ATOM   10696 C  CA    . GLU   B 1 593 ? 80.051  123.613 152.899 1.00 88.50  ?  593  GLU   B CA    1 
ATOM   10697 C  C     . GLU   B 1 593 ? 80.759  123.856 154.226 1.00 91.09  ?  593  GLU   B C     1 
ATOM   10698 O  O     . GLU   B 1 593 ? 81.936  124.233 154.227 1.00 87.00  ?  593  GLU   B O     1 
ATOM   10699 C  CB    . GLU   B 1 593 ? 80.699  122.443 152.167 1.00 86.29  ?  593  GLU   B CB    1 
ATOM   10700 C  CG    . GLU   B 1 593 ? 80.713  121.149 152.959 1.00 88.70  ?  593  GLU   B CG    1 
ATOM   10701 C  CD    . GLU   B 1 593 ? 79.583  120.219 152.571 1.00 91.38  ?  593  GLU   B CD    1 
ATOM   10702 O  OE1   . GLU   B 1 593 ? 78.601  120.698 151.966 1.00 89.97  ?  593  GLU   B OE1   1 
ATOM   10703 O  OE2   . GLU   B 1 593 ? 79.674  119.011 152.872 1.00 93.76  ?  593  GLU   B OE2   1 
ATOM   10704 N  N     . PRO   B 1 594 ? 80.091  123.671 155.360 1.00 93.03  ?  594  PRO   B N     1 
ATOM   10705 C  CA    . PRO   B 1 594 ? 80.766  123.824 156.652 1.00 89.45  ?  594  PRO   B CA    1 
ATOM   10706 C  C     . PRO   B 1 594 ? 81.716  122.669 156.929 1.00 89.11  ?  594  PRO   B C     1 
ATOM   10707 O  O     . PRO   B 1 594 ? 81.605  121.579 156.363 1.00 92.73  ?  594  PRO   B O     1 
ATOM   10708 C  CB    . PRO   B 1 594 ? 79.604  123.830 157.646 1.00 88.17  ?  594  PRO   B CB    1 
ATOM   10709 C  CG    . PRO   B 1 594 ? 78.611  122.939 156.975 1.00 86.95  ?  594  PRO   B CG    1 
ATOM   10710 C  CD    . PRO   B 1 594 ? 78.661  123.376 155.540 1.00 89.42  ?  594  PRO   B CD    1 
ATOM   10711 N  N     . LEU   B 1 595 ? 82.669  122.926 157.821 1.00 80.51  ?  595  LEU   B N     1 
ATOM   10712 C  CA    . LEU   B 1 595 ? 83.583  121.879 158.256 1.00 78.45  ?  595  LEU   B CA    1 
ATOM   10713 C  C     . LEU   B 1 595 ? 82.854  120.867 159.128 1.00 81.60  ?  595  LEU   B C     1 
ATOM   10714 O  O     . LEU   B 1 595 ? 82.057  121.232 159.997 1.00 85.52  ?  595  LEU   B O     1 
ATOM   10715 C  CB    . LEU   B 1 595 ? 84.758  122.472 159.029 1.00 74.07  ?  595  LEU   B CB    1 
ATOM   10716 C  CG    . LEU   B 1 595 ? 85.528  123.571 158.299 1.00 76.37  ?  595  LEU   B CG    1 
ATOM   10717 C  CD1   . LEU   B 1 595 ? 86.672  124.137 159.121 1.00 78.06  ?  595  LEU   B CD1   1 
ATOM   10718 C  CD2   . LEU   B 1 595 ? 86.036  123.100 156.940 1.00 76.10  ?  595  LEU   B CD2   1 
ATOM   10719 N  N     . HIS   B 1 596 ? 83.135  119.586 158.895 1.00 79.91  ?  596  HIS   B N     1 
ATOM   10720 C  CA    . HIS   B 1 596 ? 82.461  118.512 159.611 1.00 76.49  ?  596  HIS   B CA    1 
ATOM   10721 C  C     . HIS   B 1 596 ? 83.285  117.926 160.748 1.00 79.40  ?  596  HIS   B C     1 
ATOM   10722 O  O     . HIS   B 1 596 ? 82.707  117.343 161.671 1.00 84.69  ?  596  HIS   B O     1 
ATOM   10723 C  CB    . HIS   B 1 596 ? 82.079  117.384 158.644 1.00 78.12  ?  596  HIS   B CB    1 
ATOM   10724 C  CG    . HIS   B 1 596 ? 81.106  117.801 157.586 1.00 83.10  ?  596  HIS   B CG    1 
ATOM   10725 N  ND1   . HIS   B 1 596 ? 79.904  118.408 157.877 1.00 85.65  ?  596  HIS   B ND1   1 
ATOM   10726 C  CD2   . HIS   B 1 596 ? 81.158  117.695 156.238 1.00 83.80  ?  596  HIS   B CD2   1 
ATOM   10727 C  CE1   . HIS   B 1 596 ? 79.256  118.656 156.753 1.00 85.92  ?  596  HIS   B CE1   1 
ATOM   10728 N  NE2   . HIS   B 1 596 ? 80.008  118.258 155.743 1.00 88.44  ?  596  HIS   B NE2   1 
ATOM   10729 N  N     . TYR   B 1 597 ? 84.605  118.064 160.709 1.00 78.72  ?  597  TYR   B N     1 
ATOM   10730 C  CA    . TYR   B 1 597 ? 85.477  117.483 161.717 1.00 80.55  ?  597  TYR   B CA    1 
ATOM   10731 C  C     . TYR   B 1 597 ? 85.945  118.547 162.700 1.00 83.75  ?  597  TYR   B C     1 
ATOM   10732 O  O     . TYR   B 1 597 ? 86.037  119.732 162.370 1.00 86.64  ?  597  TYR   B O     1 
ATOM   10733 C  CB    . TYR   B 1 597 ? 86.680  116.804 161.062 1.00 79.18  ?  597  TYR   B CB    1 
ATOM   10734 C  CG    . TYR   B 1 597 ? 86.296  115.639 160.182 1.00 80.38  ?  597  TYR   B CG    1 
ATOM   10735 C  CD1   . TYR   B 1 597 ? 85.995  114.402 160.731 1.00 79.39  ?  597  TYR   B CD1   1 
ATOM   10736 C  CD2   . TYR   B 1 597 ? 86.219  115.780 158.804 1.00 78.16  ?  597  TYR   B CD2   1 
ATOM   10737 C  CE1   . TYR   B 1 597 ? 85.637  113.335 159.934 1.00 79.46  ?  597  TYR   B CE1   1 
ATOM   10738 C  CE2   . TYR   B 1 597 ? 85.861  114.718 157.999 1.00 76.86  ?  597  TYR   B CE2   1 
ATOM   10739 C  CZ    . TYR   B 1 597 ? 85.571  113.498 158.568 1.00 80.11  ?  597  TYR   B CZ    1 
ATOM   10740 O  OH    . TYR   B 1 597 ? 85.216  112.435 157.771 1.00 85.84  ?  597  TYR   B OH    1 
ATOM   10741 N  N     . ASP   B 1 598 ? 86.233  118.107 163.923 1.00 90.74  ?  598  ASP   B N     1 
ATOM   10742 C  CA    . ASP   B 1 598 ? 86.676  119.016 164.972 1.00 92.55  ?  598  ASP   B CA    1 
ATOM   10743 C  C     . ASP   B 1 598 ? 88.118  119.432 164.719 1.00 90.22  ?  598  ASP   B C     1 
ATOM   10744 O  O     . ASP   B 1 598 ? 89.053  118.741 165.134 1.00 86.29  ?  598  ASP   B O     1 
ATOM   10745 C  CB    . ASP   B 1 598 ? 86.523  118.357 166.346 1.00 92.53  ?  598  ASP   B CB    1 
ATOM   10746 C  CG    . ASP   B 1 598 ? 86.775  119.312 167.502 1.00 96.57  ?  598  ASP   B CG    1 
ATOM   10747 O  OD1   . ASP   B 1 598 ? 87.522  120.296 167.335 1.00 97.49  ?  598  ASP   B OD1   1 
ATOM   10748 O  OD2   . ASP   B 1 598 ? 86.328  118.998 168.623 1.00 97.05  ?  598  ASP   B OD2   1 
ATOM   10749 N  N     . TRP   B 1 599 ? 88.306  120.562 164.037 1.00 74.81  ?  599  TRP   B N     1 
ATOM   10750 C  CA    . TRP   B 1 599 ? 89.648  121.054 163.762 1.00 70.61  ?  599  TRP   B CA    1 
ATOM   10751 C  C     . TRP   B 1 599 ? 90.278  121.751 164.960 1.00 80.23  ?  599  TRP   B C     1 
ATOM   10752 O  O     . TRP   B 1 599 ? 91.503  121.898 164.996 1.00 86.10  ?  599  TRP   B O     1 
ATOM   10753 C  CB    . TRP   B 1 599 ? 89.627  122.006 162.564 1.00 71.34  ?  599  TRP   B CB    1 
ATOM   10754 C  CG    . TRP   B 1 599 ? 89.476  121.309 161.247 1.00 69.34  ?  599  TRP   B CG    1 
ATOM   10755 C  CD1   . TRP   B 1 599 ? 88.318  120.851 160.692 1.00 70.81  ?  599  TRP   B CD1   1 
ATOM   10756 C  CD2   . TRP   B 1 599 ? 90.519  120.988 160.319 1.00 71.54  ?  599  TRP   B CD2   1 
ATOM   10757 N  NE1   . TRP   B 1 599 ? 88.574  120.265 159.477 1.00 71.73  ?  599  TRP   B NE1   1 
ATOM   10758 C  CE2   . TRP   B 1 599 ? 89.918  120.336 159.225 1.00 73.86  ?  599  TRP   B CE2   1 
ATOM   10759 C  CE3   . TRP   B 1 599 ? 91.902  121.187 160.307 1.00 72.75  ?  599  TRP   B CE3   1 
ATOM   10760 C  CZ2   . TRP   B 1 599 ? 90.652  119.884 158.131 1.00 75.77  ?  599  TRP   B CZ2   1 
ATOM   10761 C  CZ3   . TRP   B 1 599 ? 92.627  120.738 159.220 1.00 72.28  ?  599  TRP   B CZ3   1 
ATOM   10762 C  CH2   . TRP   B 1 599 ? 92.002  120.094 158.148 1.00 74.48  ?  599  TRP   B CH2   1 
ATOM   10763 N  N     . GLU   B 1 600 ? 89.478  122.182 165.938 1.00 91.29  ?  600  GLU   B N     1 
ATOM   10764 C  CA    . GLU   B 1 600 ? 90.041  122.841 167.114 1.00 90.96  ?  600  GLU   B CA    1 
ATOM   10765 C  C     . GLU   B 1 600 ? 90.798  121.853 167.992 1.00 91.46  ?  600  GLU   B C     1 
ATOM   10766 O  O     . GLU   B 1 600 ? 91.890  122.160 168.490 1.00 95.85  ?  600  GLU   B O     1 
ATOM   10767 C  CB    . GLU   B 1 600 ? 88.934  123.532 167.908 1.00 91.41  ?  600  GLU   B CB    1 
ATOM   10768 C  CG    . GLU   B 1 600 ? 88.313  124.726 167.200 1.00 93.66  ?  600  GLU   B CG    1 
ATOM   10769 C  CD    . GLU   B 1 600 ? 89.347  125.635 166.567 1.00 97.03  ?  600  GLU   B CD    1 
ATOM   10770 O  OE1   . GLU   B 1 600 ? 90.312  126.021 167.259 1.00 95.08  ?  600  GLU   B OE1   1 
ATOM   10771 O  OE2   . GLU   B 1 600 ? 89.186  125.971 165.378 1.00 97.75  ?  600  GLU   B OE2   1 
ATOM   10772 N  N     . ALA   B 1 601 ? 90.235  120.660 168.189 1.00 75.73  ?  601  ALA   B N     1 
ATOM   10773 C  CA    . ALA   B 1 601 ? 90.931  119.630 168.949 1.00 74.52  ?  601  ALA   B CA    1 
ATOM   10774 C  C     . ALA   B 1 601 ? 92.209  119.198 168.245 1.00 81.16  ?  601  ALA   B C     1 
ATOM   10775 O  O     . ALA   B 1 601 ? 93.248  119.028 168.893 1.00 85.35  ?  601  ALA   B O     1 
ATOM   10776 C  CB    . ALA   B 1 601 ? 90.004  118.444 169.188 1.00 75.92  ?  601  ALA   B CB    1 
ATOM   10777 N  N     . LEU   B 1 602 ? 92.168  119.084 166.912 1.00 76.62  ?  602  LEU   B N     1 
ATOM   10778 C  CA    . LEU   B 1 602 ? 93.371  118.776 166.146 1.00 70.85  ?  602  LEU   B CA    1 
ATOM   10779 C  C     . LEU   B 1 602 ? 94.409  119.879 166.282 1.00 74.96  ?  602  LEU   B C     1 
ATOM   10780 O  O     . LEU   B 1 602 ? 95.605  119.598 166.394 1.00 80.27  ?  602  LEU   B O     1 
ATOM   10781 C  CB    . LEU   B 1 602 ? 93.023  118.553 164.675 1.00 71.74  ?  602  LEU   B CB    1 
ATOM   10782 C  CG    . LEU   B 1 602 ? 94.172  118.142 163.755 1.00 73.19  ?  602  LEU   B CG    1 
ATOM   10783 C  CD1   . LEU   B 1 602 ? 94.768  116.842 164.266 1.00 73.23  ?  602  LEU   B CD1   1 
ATOM   10784 C  CD2   . LEU   B 1 602 ? 93.613  117.957 162.360 1.00 76.26  ?  602  LEU   B CD2   1 
ATOM   10785 N  N     . ARG   B 1 603 ? 93.974  121.141 166.262 1.00 76.50  ?  603  ARG   B N     1 
ATOM   10786 C  CA    . ARG   B 1 603 ? 94.907  122.252 166.424 1.00 76.06  ?  603  ARG   B CA    1 
ATOM   10787 C  C     . ARG   B 1 603 ? 95.581  122.212 167.789 1.00 80.67  ?  603  ARG   B C     1 
ATOM   10788 O  O     . ARG   B 1 603 ? 96.800  122.396 167.897 1.00 82.43  ?  603  ARG   B O     1 
ATOM   10789 C  CB    . ARG   B 1 603 ? 94.173  123.578 166.224 1.00 72.13  ?  603  ARG   B CB    1 
ATOM   10790 C  CG    . ARG   B 1 603 ? 95.065  124.805 166.262 1.00 76.99  ?  603  ARG   B CG    1 
ATOM   10791 C  CD    . ARG   B 1 603 ? 94.265  126.055 166.588 1.00 75.07  ?  603  ARG   B CD    1 
ATOM   10792 N  NE    . ARG   B 1 603 ? 93.074  126.178 165.758 1.00 80.49  ?  603  ARG   B NE    1 
ATOM   10793 C  CZ    . ARG   B 1 603 ? 93.052  126.736 164.555 1.00 80.03  ?  603  ARG   B CZ    1 
ATOM   10794 N  NH1   . ARG   B 1 603 ? 94.149  127.222 163.998 1.00 78.67  ?  603  ARG   B NH1   1 
ATOM   10795 N  NH2   . ARG   B 1 603 ? 91.908  126.775 163.880 1.00 78.43  ?  603  ARG   B NH2   1 
ATOM   10796 N  N     . GLU   B 1 604 ? 94.802  121.965 168.845 1.00 90.36  ?  604  GLU   B N     1 
ATOM   10797 C  CA    . GLU   B 1 604 ? 95.383  121.879 170.182 1.00 87.67  ?  604  GLU   B CA    1 
ATOM   10798 C  C     . GLU   B 1 604 ? 96.342  120.698 170.294 1.00 89.99  ?  604  GLU   B C     1 
ATOM   10799 O  O     . GLU   B 1 604 ? 97.415  120.814 170.900 1.00 91.88  ?  604  GLU   B O     1 
ATOM   10800 C  CB    . GLU   B 1 604 ? 94.277  121.776 171.232 1.00 88.76  ?  604  GLU   B CB    1 
ATOM   10801 C  CG    . GLU   B 1 604 ? 94.758  122.001 172.656 1.00 94.85  ?  604  GLU   B CG    1 
ATOM   10802 C  CD    . GLU   B 1 604 ? 93.626  122.000 173.663 1.00 98.42  ?  604  GLU   B CD    1 
ATOM   10803 O  OE1   . GLU   B 1 604 ? 92.453  122.038 173.236 1.00 96.60  ?  604  GLU   B OE1   1 
ATOM   10804 O  OE2   . GLU   B 1 604 ? 93.912  122.012 174.879 1.00 97.20  ?  604  GLU   B OE2   1 
ATOM   10805 N  N     . SER   B 1 605 ? 95.973  119.554 169.713 1.00 81.56  ?  605  SER   B N     1 
ATOM   10806 C  CA    . SER   B 1 605 ? 96.846  118.384 169.752 1.00 78.70  ?  605  SER   B CA    1 
ATOM   10807 C  C     . SER   B 1 605 ? 98.146  118.637 168.998 1.00 80.62  ?  605  SER   B C     1 
ATOM   10808 O  O     . SER   B 1 605 ? 99.221  118.217 169.442 1.00 80.93  ?  605  SER   B O     1 
ATOM   10809 C  CB    . SER   B 1 605 ? 96.117  117.170 169.176 1.00 79.07  ?  605  SER   B CB    1 
ATOM   10810 O  OG    . SER   B 1 605 ? 96.867  115.985 169.371 1.00 85.10  ?  605  SER   B OG    1 
ATOM   10811 N  N     . ILE   B 1 606 ? 98.066  119.313 167.851 1.00 70.77  ?  606  ILE   B N     1 
ATOM   10812 C  CA    . ILE   B 1 606 ? 99.267  119.631 167.086 1.00 65.42  ?  606  ILE   B CA    1 
ATOM   10813 C  C     . ILE   B 1 606 ? 100.145 120.607 167.857 1.00 68.36  ?  606  ILE   B C     1 
ATOM   10814 O  O     . ILE   B 1 606 ? 101.376 120.487 167.859 1.00 72.22  ?  606  ILE   B O     1 
ATOM   10815 C  CB    . ILE   B 1 606 ? 98.884  120.176 165.698 1.00 62.78  ?  606  ILE   B CB    1 
ATOM   10816 C  CG1   . ILE   B 1 606 ? 98.397  119.040 164.797 1.00 66.60  ?  606  ILE   B CG1   1 
ATOM   10817 C  CG2   . ILE   B 1 606 ? 100.059 120.891 165.050 1.00 61.86  ?  606  ILE   B CG2   1 
ATOM   10818 C  CD1   . ILE   B 1 606 ? 97.616  119.509 163.593 1.00 67.84  ?  606  ILE   B CD1   1 
ATOM   10819 N  N     . LYS   B 1 607 ? 99.533  121.585 168.529 1.00 83.75  ?  607  LYS   B N     1 
ATOM   10820 C  CA    . LYS   B 1 607 ? 100.315 122.505 169.348 1.00 84.63  ?  607  LYS   B CA    1 
ATOM   10821 C  C     . LYS   B 1 607 ? 101.020 121.770 170.482 1.00 88.22  ?  607  LYS   B C     1 
ATOM   10822 O  O     . LYS   B 1 607 ? 102.185 122.053 170.785 1.00 91.37  ?  607  LYS   B O     1 
ATOM   10823 C  CB    . LYS   B 1 607 ? 99.418  123.610 169.903 1.00 83.92  ?  607  LYS   B CB    1 
ATOM   10824 C  CG    . LYS   B 1 607 ? 99.620  124.963 169.239 1.00 86.26  ?  607  LYS   B CG    1 
ATOM   10825 C  CD    . LYS   B 1 607 ? 98.340  125.783 169.256 1.00 89.34  ?  607  LYS   B CD    1 
ATOM   10826 C  CE    . LYS   B 1 607 ? 97.459  125.402 170.430 1.00 90.98  ?  607  LYS   B CE    1 
ATOM   10827 N  NZ    . LYS   B 1 607 ? 96.179  126.157 170.425 1.00 86.97  ?  607  LYS   B NZ    1 
ATOM   10828 N  N     . THR   B 1 608 ? 100.328 120.822 171.120 1.00 86.59  ?  608  THR   B N     1 
ATOM   10829 C  CA    . THR   B 1 608 ? 100.915 120.112 172.254 1.00 84.35  ?  608  THR   B CA    1 
ATOM   10830 C  C     . THR   B 1 608 ? 102.033 119.173 171.811 1.00 86.65  ?  608  THR   B C     1 
ATOM   10831 O  O     . THR   B 1 608 ? 103.135 119.198 172.371 1.00 87.46  ?  608  THR   B O     1 
ATOM   10832 C  CB    . THR   B 1 608 ? 99.834  119.346 173.018 1.00 87.53  ?  608  THR   B CB    1 
ATOM   10833 O  OG1   . THR   B 1 608 ? 99.161  120.253 173.897 1.00 88.86  ?  608  THR   B OG1   1 
ATOM   10834 C  CG2   . THR   B 1 608 ? 100.471 118.248 173.857 1.00 85.89  ?  608  THR   B CG2   1 
ATOM   10835 N  N     . HIS   B 1 609 ? 101.772 118.295 170.824 1.00 83.66  ?  609  HIS   B N     1 
ATOM   10836 C  CA    . HIS   B 1 609 ? 102.753 117.247 170.400 1.00 79.56  ?  609  HIS   B CA    1 
ATOM   10837 C  C     . HIS   B 1 609 ? 103.435 117.530 169.056 1.00 83.47  ?  609  HIS   B C     1 
ATOM   10838 O  O     . HIS   B 1 609 ? 104.621 117.213 168.948 1.00 89.49  ?  609  HIS   B O     1 
ATOM   10839 C  CB    . HIS   B 1 609 ? 102.067 115.888 170.299 1.00 80.53  ?  609  HIS   B CB    1 
ATOM   10840 C  CG    . HIS   B 1 609 ? 100.989 115.666 171.303 1.00 87.48  ?  609  HIS   B CG    1 
ATOM   10841 N  ND1   . HIS   B 1 609 ? 101.213 114.996 172.486 1.00 87.99  ?  609  HIS   B ND1   1 
ATOM   10842 C  CD2   . HIS   B 1 609 ? 99.682  116.000 171.299 1.00 87.42  ?  609  HIS   B CD2   1 
ATOM   10843 C  CE1   . HIS   B 1 609 ? 100.093 114.936 173.174 1.00 87.14  ?  609  HIS   B CE1   1 
ATOM   10844 N  NE2   . HIS   B 1 609 ? 99.139  115.546 172.468 1.00 89.29  ?  609  HIS   B NE2   1 
ATOM   10845 N  N     . GLY   B 1 610 ? 102.710 118.025 168.055 1.00 72.55  ?  610  GLY   B N     1 
ATOM   10846 C  CA    . GLY   B 1 610 ? 103.306 118.319 166.767 1.00 66.57  ?  610  GLY   B CA    1 
ATOM   10847 C  C     . GLY   B 1 610 ? 102.938 117.278 165.726 1.00 69.75  ?  610  GLY   B C     1 
ATOM   10848 O  O     . GLY   B 1 610 ? 102.275 116.278 166.001 1.00 75.19  ?  610  GLY   B O     1 
ATOM   10849 N  N     . LEU   B 1 611 ? 103.465 117.499 164.527 1.00 71.92  ?  611  LEU   B N     1 
ATOM   10850 C  CA    . LEU   B 1 611 ? 103.322 116.577 163.411 1.00 68.91  ?  611  LEU   B CA    1 
ATOM   10851 C  C     . LEU   B 1 611 ? 104.653 115.903 163.114 1.00 68.60  ?  611  LEU   B C     1 
ATOM   10852 O  O     . LEU   B 1 611 ? 105.704 116.551 163.121 1.00 75.80  ?  611  LEU   B O     1 
ATOM   10853 C  CB    . LEU   B 1 611 ? 102.834 117.294 162.153 1.00 66.23  ?  611  LEU   B CB    1 
ATOM   10854 C  CG    . LEU   B 1 611 ? 101.495 118.019 162.253 1.00 64.57  ?  611  LEU   B CG    1 
ATOM   10855 C  CD1   . LEU   B 1 611 ? 101.273 118.975 161.098 1.00 71.32  ?  611  LEU   B CD1   1 
ATOM   10856 C  CD2   . LEU   B 1 611 ? 100.343 117.033 162.340 1.00 68.05  ?  611  LEU   B CD2   1 
ATOM   10857 N  N     . ARG   B 1 612 ? 104.599 114.598 162.852 1.00 65.39  ?  612  ARG   B N     1 
ATOM   10858 C  CA    . ARG   B 1 612 ? 105.803 113.873 162.468 1.00 63.08  ?  612  ARG   B CA    1 
ATOM   10859 C  C     . ARG   B 1 612 ? 106.322 114.337 161.114 1.00 72.28  ?  612  ARG   B C     1 
ATOM   10860 O  O     . ARG   B 1 612 ? 107.526 114.249 160.847 1.00 77.81  ?  612  ARG   B O     1 
ATOM   10861 C  CB    . ARG   B 1 612 ? 105.518 112.371 162.455 1.00 63.41  ?  612  ARG   B CB    1 
ATOM   10862 C  CG    . ARG   B 1 612 ? 106.699 111.504 162.064 1.00 64.72  ?  612  ARG   B CG    1 
ATOM   10863 C  CD    . ARG   B 1 612 ? 107.560 111.158 163.264 1.00 67.34  ?  612  ARG   B CD    1 
ATOM   10864 N  NE    . ARG   B 1 612 ? 108.611 110.205 162.927 1.00 71.39  ?  612  ARG   B NE    1 
ATOM   10865 C  CZ    . ARG   B 1 612 ? 109.836 110.233 163.431 1.00 70.48  ?  612  ARG   B CZ    1 
ATOM   10866 N  NH1   . ARG   B 1 612 ? 110.205 111.159 164.298 1.00 71.09  ?  612  ARG   B NH1   1 
ATOM   10867 N  NH2   . ARG   B 1 612 ? 110.732 109.347 163.006 1.00 75.33  ?  612  ARG   B NH2   1 
ATOM   10868 N  N     . ASN   B 1 613 ? 105.441 114.853 160.263 1.00 67.59  ?  613  ASN   B N     1 
ATOM   10869 C  CA    . ASN   B 1 613 ? 105.789 115.264 158.913 1.00 59.56  ?  613  ASN   B CA    1 
ATOM   10870 C  C     . ASN   B 1 613 ? 105.396 116.718 158.692 1.00 64.64  ?  613  ASN   B C     1 
ATOM   10871 O  O     . ASN   B 1 613 ? 104.336 117.160 159.144 1.00 75.54  ?  613  ASN   B O     1 
ATOM   10872 C  CB    . ASN   B 1 613 ? 105.098 114.369 157.892 1.00 59.67  ?  613  ASN   B CB    1 
ATOM   10873 C  CG    . ASN   B 1 613 ? 105.312 112.899 158.170 1.00 65.60  ?  613  ASN   B CG    1 
ATOM   10874 O  OD1   . ASN   B 1 613 ? 104.449 112.231 158.736 1.00 71.57  ?  613  ASN   B OD1   1 
ATOM   10875 N  ND2   . ASN   B 1 613 ? 106.445 112.374 157.728 1.00 69.46  ?  613  ASN   B ND2   1 
ATOM   10876 N  N     . SER   B 1 614 ? 106.267 117.460 158.002 1.00 72.47  ?  614  SER   B N     1 
ATOM   10877 C  CA    . SER   B 1 614 ? 105.985 118.864 157.719 1.00 71.09  ?  614  SER   B CA    1 
ATOM   10878 C  C     . SER   B 1 614 ? 104.799 119.013 156.774 1.00 71.10  ?  614  SER   B C     1 
ATOM   10879 O  O     . SER   B 1 614 ? 103.921 119.854 156.998 1.00 78.88  ?  614  SER   B O     1 
ATOM   10880 C  CB    . SER   B 1 614 ? 107.229 119.537 157.143 1.00 71.57  ?  614  SER   B CB    1 
ATOM   10881 O  OG    . SER   B 1 614 ? 108.051 120.015 158.191 1.00 79.82  ?  614  SER   B OG    1 
ATOM   10882 N  N     . THR   B 1 615 ? 104.755 118.207 155.719 1.00 70.20  ?  615  THR   B N     1 
ATOM   10883 C  CA    . THR   B 1 615 ? 103.666 118.222 154.758 1.00 69.20  ?  615  THR   B CA    1 
ATOM   10884 C  C     . THR   B 1 615 ? 103.093 116.820 154.621 1.00 72.08  ?  615  THR   B C     1 
ATOM   10885 O  O     . THR   B 1 615 ? 103.779 115.828 154.877 1.00 78.24  ?  615  THR   B O     1 
ATOM   10886 C  CB    . THR   B 1 615 ? 104.125 118.715 153.382 1.00 73.72  ?  615  THR   B CB    1 
ATOM   10887 O  OG1   . THR   B 1 615 ? 105.023 117.766 152.795 1.00 78.22  ?  615  THR   B OG1   1 
ATOM   10888 C  CG2   . THR   B 1 615 ? 104.805 120.069 153.470 1.00 73.69  ?  615  THR   B CG2   1 
ATOM   10889 N  N     . LEU   B 1 616 ? 101.822 116.742 154.223 1.00 67.23  ?  616  LEU   B N     1 
ATOM   10890 C  CA    . LEU   B 1 616 ? 101.168 115.445 154.092 1.00 64.50  ?  616  LEU   B CA    1 
ATOM   10891 C  C     . LEU   B 1 616 ? 100.402 115.296 152.784 1.00 66.46  ?  616  LEU   B C     1 
ATOM   10892 O  O     . LEU   B 1 616 ? 100.201 114.174 152.310 1.00 77.00  ?  616  LEU   B O     1 
ATOM   10893 C  CB    . LEU   B 1 616 ? 100.218 115.207 155.265 1.00 62.78  ?  616  LEU   B CB    1 
ATOM   10894 C  CG    . LEU   B 1 616 ? 100.898 115.086 156.628 1.00 67.07  ?  616  LEU   B CG    1 
ATOM   10895 C  CD1   . LEU   B 1 616 ? 99.970  115.481 157.750 1.00 71.18  ?  616  LEU   B CD1   1 
ATOM   10896 C  CD2   . LEU   B 1 616 ? 101.459 113.695 156.857 1.00 68.21  ?  616  LEU   B CD2   1 
ATOM   10897 N  N     . SER   B 1 617 ? 99.964  116.405 152.192 1.00 58.81  ?  617  SER   B N     1 
ATOM   10898 C  CA    . SER   B 1 617 ? 99.071  116.368 151.042 1.00 56.13  ?  617  SER   B CA    1 
ATOM   10899 C  C     . SER   B 1 617 ? 99.699  117.064 149.844 1.00 60.13  ?  617  SER   B C     1 
ATOM   10900 O  O     . SER   B 1 617 ? 100.278 118.147 149.972 1.00 69.39  ?  617  SER   B O     1 
ATOM   10901 C  CB    . SER   B 1 617 ? 97.727  117.024 151.366 1.00 56.15  ?  617  SER   B CB    1 
ATOM   10902 O  OG    . SER   B 1 617 ? 97.926  118.261 152.023 1.00 61.65  ?  617  SER   B OG    1 
ATOM   10903 N  N     . ALA   B 1 618 ? 99.570  116.430 148.679 1.00 61.25  ?  618  ALA   B N     1 
ATOM   10904 C  CA    . ALA   B 1 618 ? 100.007 116.999 147.410 1.00 62.95  ?  618  ALA   B CA    1 
ATOM   10905 C  C     . ALA   B 1 618 ? 99.375  116.189 146.289 1.00 68.04  ?  618  ALA   B C     1 
ATOM   10906 O  O     . ALA   B 1 618 ? 99.504  114.963 146.268 1.00 76.93  ?  618  ALA   B O     1 
ATOM   10907 C  CB    . ALA   B 1 618 ? 101.533 116.989 147.288 1.00 57.57  ?  618  ALA   B CB    1 
ATOM   10908 N  N     . LEU   B 1 619 ? 98.704  116.868 145.362 1.00 52.27  ?  619  LEU   B N     1 
ATOM   10909 C  CA    . LEU   B 1 619 ? 97.943  116.194 144.309 1.00 50.74  ?  619  LEU   B CA    1 
ATOM   10910 C  C     . LEU   B 1 619 ? 98.845  115.977 143.099 1.00 60.91  ?  619  LEU   B C     1 
ATOM   10911 O  O     . LEU   B 1 619 ? 99.070  116.890 142.302 1.00 65.09  ?  619  LEU   B O     1 
ATOM   10912 C  CB    . LEU   B 1 619 ? 96.703  117.002 143.948 1.00 54.53  ?  619  LEU   B CB    1 
ATOM   10913 C  CG    . LEU   B 1 619 ? 95.670  117.173 145.063 1.00 55.98  ?  619  LEU   B CG    1 
ATOM   10914 C  CD1   . LEU   B 1 619 ? 94.325  117.557 144.482 1.00 60.53  ?  619  LEU   B CD1   1 
ATOM   10915 C  CD2   . LEU   B 1 619 ? 95.549  115.905 145.889 1.00 52.38  ?  619  LEU   B CD2   1 
ATOM   10916 N  N     . MET   B 1 620 ? 99.354  114.756 142.961 1.00 68.21  ?  620  MET   B N     1 
ATOM   10917 C  CA    . MET   B 1 620 ? 100.195 114.374 141.840 1.00 62.03  ?  620  MET   B CA    1 
ATOM   10918 C  C     . MET   B 1 620 ? 99.341  113.968 140.641 1.00 61.41  ?  620  MET   B C     1 
ATOM   10919 O  O     . MET   B 1 620 ? 98.160  113.645 140.790 1.00 65.98  ?  620  MET   B O     1 
ATOM   10920 C  CB    . MET   B 1 620 ? 101.112 113.226 142.251 1.00 63.86  ?  620  MET   B CB    1 
ATOM   10921 C  CG    . MET   B 1 620 ? 100.383 111.934 142.535 1.00 67.60  ?  620  MET   B CG    1 
ATOM   10922 S  SD    . MET   B 1 620 ? 99.113  112.078 143.801 1.00 84.94  ?  620  MET   B SD    1 
ATOM   10923 C  CE    . MET   B 1 620 ? 100.120 112.071 145.279 1.00 65.74  ?  620  MET   B CE    1 
ATOM   10924 N  N     . PRO   B 1 621 ? 99.915  113.973 139.431 1.00 61.90  ?  621  PRO   B N     1 
ATOM   10925 C  CA    . PRO   B 1 621 ? 99.116  113.577 138.261 1.00 65.80  ?  621  PRO   B CA    1 
ATOM   10926 C  C     . PRO   B 1 621 ? 98.809  112.087 138.206 1.00 67.67  ?  621  PRO   B C     1 
ATOM   10927 O  O     . PRO   B 1 621 ? 97.775  111.711 137.642 1.00 72.96  ?  621  PRO   B O     1 
ATOM   10928 C  CB    . PRO   B 1 621 ? 99.981  114.023 137.071 1.00 61.65  ?  621  PRO   B CB    1 
ATOM   10929 C  CG    . PRO   B 1 621 ? 101.101 114.842 137.660 1.00 60.94  ?  621  PRO   B CG    1 
ATOM   10930 C  CD    . PRO   B 1 621 ? 101.284 114.346 139.044 1.00 62.19  ?  621  PRO   B CD    1 
ATOM   10931 N  N     . SER   B 1 622 ? 99.664  111.233 138.776 1.00 61.34  ?  622  SER   B N     1 
ATOM   10932 C  CA    . SER   B 1 622 ? 99.463  109.779 138.768 1.00 49.47  ?  622  SER   B CA    1 
ATOM   10933 C  C     . SER   B 1 622 ? 99.297  109.248 137.344 1.00 60.72  ?  622  SER   B C     1 
ATOM   10934 O  O     . SER   B 1 622 ? 98.413  108.442 137.053 1.00 71.26  ?  622  SER   B O     1 
ATOM   10935 C  CB    . SER   B 1 622 ? 98.276  109.382 139.648 1.00 55.44  ?  622  SER   B CB    1 
ATOM   10936 O  OG    . SER   B 1 622 ? 98.598  109.525 141.020 1.00 67.78  ?  622  SER   B OG    1 
ATOM   10937 N  N     . GLU   B 1 623 ? 100.169 109.714 136.448 1.00 72.46  ?  623  GLU   B N     1 
ATOM   10938 C  CA    . GLU   B 1 623 ? 100.086 109.305 135.050 1.00 75.82  ?  623  GLU   B CA    1 
ATOM   10939 C  C     . GLU   B 1 623 ? 100.310 107.806 134.894 1.00 81.24  ?  623  GLU   B C     1 
ATOM   10940 O  O     . GLU   B 1 623 ? 99.611  107.143 134.119 1.00 82.79  ?  623  GLU   B O     1 
ATOM   10941 C  CB    . GLU   B 1 623 ? 101.099 110.089 134.216 1.00 75.16  ?  623  GLU   B CB    1 
ATOM   10942 C  CG    . GLU   B 1 623 ? 100.766 110.159 132.739 1.00 81.88  ?  623  GLU   B CG    1 
ATOM   10943 C  CD    . GLU   B 1 623 ? 99.414  110.794 132.479 1.00 88.69  ?  623  GLU   B CD    1 
ATOM   10944 O  OE1   . GLU   B 1 623 ? 98.516  110.092 131.969 1.00 89.00  ?  623  GLU   B OE1   1 
ATOM   10945 O  OE2   . GLU   B 1 623 ? 99.254  111.996 132.779 1.00 85.23  ?  623  GLU   B OE2   1 
ATOM   10946 N  N     . THR   B 1 624 ? 101.277 107.254 135.624 1.00 71.39  ?  624  THR   B N     1 
ATOM   10947 C  CA    . THR   B 1 624 ? 101.603 105.837 135.542 1.00 61.99  ?  624  THR   B CA    1 
ATOM   10948 C  C     . THR   B 1 624 ? 101.047 105.028 136.704 1.00 66.89  ?  624  THR   B C     1 
ATOM   10949 O  O     . THR   B 1 624 ? 100.637 103.881 136.509 1.00 80.97  ?  624  THR   B O     1 
ATOM   10950 C  CB    . THR   B 1 624 ? 103.122 105.647 135.476 1.00 63.95  ?  624  THR   B CB    1 
ATOM   10951 O  OG1   . THR   B 1 624 ? 103.689 106.626 134.598 1.00 74.22  ?  624  THR   B OG1   1 
ATOM   10952 C  CG2   . THR   B 1 624 ? 103.466 104.262 134.963 1.00 67.89  ?  624  THR   B CG2   1 
ATOM   10953 N  N     . SER   B 1 625 ? 101.006 105.593 137.911 1.00 55.50  ?  625  SER   B N     1 
ATOM   10954 C  CA    . SER   B 1 625 ? 100.591 104.794 139.059 1.00 55.76  ?  625  SER   B CA    1 
ATOM   10955 C  C     . SER   B 1 625 ? 99.086  104.540 139.071 1.00 68.12  ?  625  SER   B C     1 
ATOM   10956 O  O     . SER   B 1 625 ? 98.650  103.519 139.610 1.00 69.30  ?  625  SER   B O     1 
ATOM   10957 C  CB    . SER   B 1 625 ? 101.030 105.456 140.360 1.00 64.51  ?  625  SER   B CB    1 
ATOM   10958 O  OG    . SER   B 1 625 ? 100.863 106.855 140.266 1.00 78.55  ?  625  SER   B OG    1 
ATOM   10959 N  N     . SER   B 1 626 ? 98.276  105.438 138.491 1.00 66.63  ?  626  SER   B N     1 
ATOM   10960 C  CA    . SER   B 1 626 ? 96.831  105.200 138.438 1.00 58.70  ?  626  SER   B CA    1 
ATOM   10961 C  C     . SER   B 1 626 ? 96.481  104.044 137.511 1.00 60.14  ?  626  SER   B C     1 
ATOM   10962 O  O     . SER   B 1 626 ? 95.457  103.382 137.708 1.00 65.71  ?  626  SER   B O     1 
ATOM   10963 C  CB    . SER   B 1 626 ? 96.085  106.458 137.987 1.00 61.66  ?  626  SER   B CB    1 
ATOM   10964 O  OG    . SER   B 1 626 ? 96.682  106.980 136.817 1.00 69.03  ?  626  SER   B OG    1 
ATOM   10965 N  N     . GLN   B 1 627 ? 97.310  103.787 136.497 1.00 62.66  ?  627  GLN   B N     1 
ATOM   10966 C  CA    . GLN   B 1 627 ? 97.021  102.705 135.562 1.00 58.46  ?  627  GLN   B CA    1 
ATOM   10967 C  C     . GLN   B 1 627 ? 97.040  101.346 136.246 1.00 62.45  ?  627  GLN   B C     1 
ATOM   10968 O  O     . GLN   B 1 627 ? 96.387  100.408 135.776 1.00 76.67  ?  627  GLN   B O     1 
ATOM   10969 C  CB    . GLN   B 1 627 ? 98.023  102.729 134.408 1.00 60.28  ?  627  GLN   B CB    1 
ATOM   10970 C  CG    . GLN   B 1 627 ? 97.878  103.926 133.487 1.00 59.05  ?  627  GLN   B CG    1 
ATOM   10971 C  CD    . GLN   B 1 627 ? 98.917  103.941 132.388 1.00 69.80  ?  627  GLN   B CD    1 
ATOM   10972 O  OE1   . GLN   B 1 627 ? 99.002  103.013 131.586 1.00 76.52  ?  627  GLN   B OE1   1 
ATOM   10973 N  NE2   . GLN   B 1 627 ? 99.718  104.999 132.345 1.00 67.27  ?  627  GLN   B NE2   1 
ATOM   10974 N  N     . ILE   B 1 628 ? 97.778  101.218 137.351 1.00 52.74  ?  628  ILE   B N     1 
ATOM   10975 C  CA    . ILE   B 1 628 ? 97.852  99.942  138.058 1.00 53.65  ?  628  ILE   B CA    1 
ATOM   10976 C  C     . ILE   B 1 628 ? 96.491  99.565  138.630 1.00 59.99  ?  628  ILE   B C     1 
ATOM   10977 O  O     . ILE   B 1 628 ? 96.064  98.407  138.545 1.00 67.90  ?  628  ILE   B O     1 
ATOM   10978 C  CB    . ILE   B 1 628 ? 98.932  100.001 139.153 1.00 51.32  ?  628  ILE   B CB    1 
ATOM   10979 C  CG1   . ILE   B 1 628 ? 100.303 100.247 138.525 1.00 53.93  ?  628  ILE   B CG1   1 
ATOM   10980 C  CG2   . ILE   B 1 628 ? 98.938  98.722  139.969 1.00 54.22  ?  628  ILE   B CG2   1 
ATOM   10981 C  CD1   . ILE   B 1 628 ? 100.860 99.050  137.796 1.00 55.12  ?  628  ILE   B CD1   1 
ATOM   10982 N  N     . SER   B 1 629 ? 95.789  100.529 139.218 1.00 58.47  ?  629  SER   B N     1 
ATOM   10983 C  CA    . SER   B 1 629 ? 94.468  100.289 139.783 1.00 57.29  ?  629  SER   B CA    1 
ATOM   10984 C  C     . SER   B 1 629 ? 93.346  100.509 138.778 1.00 63.02  ?  629  SER   B C     1 
ATOM   10985 O  O     . SER   B 1 629 ? 92.176  100.390 139.151 1.00 66.99  ?  629  SER   B O     1 
ATOM   10986 C  CB    . SER   B 1 629 ? 94.241  101.186 141.005 1.00 62.42  ?  629  SER   B CB    1 
ATOM   10987 O  OG    . SER   B 1 629 ? 94.760  102.480 140.766 1.00 70.88  ?  629  SER   B OG    1 
ATOM   10988 N  N     . ASN   B 1 630 ? 93.674  100.819 137.522 1.00 66.72  ?  630  ASN   B N     1 
ATOM   10989 C  CA    . ASN   B 1 630 ? 92.686  101.154 136.497 1.00 59.16  ?  630  ASN   B CA    1 
ATOM   10990 C  C     . ASN   B 1 630 ? 91.825  102.332 136.958 1.00 66.51  ?  630  ASN   B C     1 
ATOM   10991 O  O     . ASN   B 1 630 ? 90.608  102.235 137.114 1.00 74.24  ?  630  ASN   B O     1 
ATOM   10992 C  CB    . ASN   B 1 630 ? 91.831  99.932  136.130 1.00 58.93  ?  630  ASN   B CB    1 
ATOM   10993 C  CG    . ASN   B 1 630 ? 90.966  100.172 134.908 1.00 67.09  ?  630  ASN   B CG    1 
ATOM   10994 O  OD1   . ASN   B 1 630 ? 91.457  100.586 133.861 1.00 69.31  ?  630  ASN   B OD1   1 
ATOM   10995 N  ND2   . ASN   B 1 630 ? 89.661  99.997  135.064 1.00 66.23  ?  630  ASN   B ND2   1 
ATOM   10996 N  N     . ALA   B 1 631 ? 92.496  103.459 137.182 1.00 67.36  ?  631  ALA   B N     1 
ATOM   10997 C  CA    . ALA   B 1 631 ? 91.877  104.644 137.750 1.00 59.71  ?  631  ALA   B CA    1 
ATOM   10998 C  C     . ALA   B 1 631 ? 92.154  105.849 136.867 1.00 64.65  ?  631  ALA   B C     1 
ATOM   10999 O  O     . ALA   B 1 631 ? 93.165  105.903 136.162 1.00 74.58  ?  631  ALA   B O     1 
ATOM   11000 C  CB    . ALA   B 1 631 ? 92.396  104.912 139.166 1.00 56.38  ?  631  ALA   B CB    1 
ATOM   11001 N  N     . THR   B 1 632 ? 91.243  106.817 136.909 1.00 56.13  ?  632  THR   B N     1 
ATOM   11002 C  CA    . THR   B 1 632 ? 91.483  108.088 136.243 1.00 56.94  ?  632  THR   B CA    1 
ATOM   11003 C  C     . THR   B 1 632 ? 92.630  108.811 136.937 1.00 59.54  ?  632  THR   B C     1 
ATOM   11004 O  O     . THR   B 1 632 ? 92.662  108.908 138.167 1.00 67.69  ?  632  THR   B O     1 
ATOM   11005 C  CB    . THR   B 1 632 ? 90.219  108.946 136.254 1.00 57.14  ?  632  THR   B CB    1 
ATOM   11006 O  OG1   . THR   B 1 632 ? 90.059  109.552 137.542 1.00 70.71  ?  632  THR   B OG1   1 
ATOM   11007 C  CG2   . THR   B 1 632 ? 88.998  108.094 135.947 1.00 52.01  ?  632  THR   B CG2   1 
ATOM   11008 N  N     . ASN   B 1 633 ? 93.574  109.314 136.146 1.00 65.70  ?  633  ASN   B N     1 
ATOM   11009 C  CA    . ASN   B 1 633 ? 94.817  109.841 136.695 1.00 66.54  ?  633  ASN   B CA    1 
ATOM   11010 C  C     . ASN   B 1 633 ? 94.550  111.092 137.521 1.00 70.53  ?  633  ASN   B C     1 
ATOM   11011 O  O     . ASN   B 1 633 ? 94.102  112.113 136.989 1.00 73.20  ?  633  ASN   B O     1 
ATOM   11012 C  CB    . ASN   B 1 633 ? 95.799  110.144 135.568 1.00 61.59  ?  633  ASN   B CB    1 
ATOM   11013 C  CG    . ASN   B 1 633 ? 95.130  110.775 134.368 1.00 77.48  ?  633  ASN   B CG    1 
ATOM   11014 O  OD1   . ASN   B 1 633 ? 94.226  110.192 133.771 1.00 87.13  ?  633  ASN   B OD1   1 
ATOM   11015 N  ND2   . ASN   B 1 633 ? 95.582  111.965 133.996 1.00 79.38  ?  633  ASN   B ND2   1 
ATOM   11016 N  N     . GLY   B 1 634 ? 94.831  111.010 138.820 1.00 61.51  ?  634  GLY   B N     1 
ATOM   11017 C  CA    . GLY   B 1 634 ? 94.711  112.174 139.682 1.00 56.84  ?  634  GLY   B CA    1 
ATOM   11018 C  C     . GLY   B 1 634 ? 93.295  112.712 139.721 1.00 60.52  ?  634  GLY   B C     1 
ATOM   11019 O  O     . GLY   B 1 634 ? 92.332  111.988 139.997 1.00 65.61  ?  634  GLY   B O     1 
ATOM   11020 N  N     . ILE   B 1 635 ? 93.166  114.005 139.443 1.00 68.45  ?  635  ILE   B N     1 
ATOM   11021 C  CA    . ILE   B 1 635 ? 91.885  114.692 139.443 1.00 64.55  ?  635  ILE   B CA    1 
ATOM   11022 C  C     . ILE   B 1 635 ? 91.492  115.130 138.033 1.00 65.50  ?  635  ILE   B C     1 
ATOM   11023 O  O     . ILE   B 1 635 ? 90.660  116.017 137.868 1.00 69.93  ?  635  ILE   B O     1 
ATOM   11024 C  CB    . ILE   B 1 635 ? 91.896  115.879 140.420 1.00 67.00  ?  635  ILE   B CB    1 
ATOM   11025 C  CG1   . ILE   B 1 635 ? 93.004  116.879 140.071 1.00 65.45  ?  635  ILE   B CG1   1 
ATOM   11026 C  CG2   . ILE   B 1 635 ? 92.082  115.384 141.835 1.00 61.68  ?  635  ILE   B CG2   1 
ATOM   11027 C  CD1   . ILE   B 1 635 ? 92.504  118.302 140.000 1.00 69.92  ?  635  ILE   B CD1   1 
ATOM   11028 N  N     . GLU   B 1 636 ? 92.083  114.516 137.014 1.00 75.22  ?  636  GLU   B N     1 
ATOM   11029 C  CA    . GLU   B 1 636 ? 91.839  114.881 135.623 1.00 73.60  ?  636  GLU   B CA    1 
ATOM   11030 C  C     . GLU   B 1 636 ? 90.703  114.043 135.049 1.00 79.88  ?  636  GLU   B C     1 
ATOM   11031 O  O     . GLU   B 1 636 ? 90.713  112.816 135.200 1.00 84.68  ?  636  GLU   B O     1 
ATOM   11032 C  CB    . GLU   B 1 636 ? 93.093  114.684 134.785 1.00 75.90  ?  636  GLU   B CB    1 
ATOM   11033 C  CG    . GLU   B 1 636 ? 94.262  115.541 135.218 1.00 78.64  ?  636  GLU   B CG    1 
ATOM   11034 C  CD    . GLU   B 1 636 ? 93.993  117.018 135.042 1.00 86.54  ?  636  GLU   B CD    1 
ATOM   11035 O  OE1   . GLU   B 1 636 ? 93.248  117.382 134.109 1.00 86.46  ?  636  GLU   B OE1   1 
ATOM   11036 O  OE2   . GLU   B 1 636 ? 94.532  117.819 135.831 1.00 89.09  ?  636  GLU   B OE2   1 
ATOM   11037 N  N     . PRO   B 1 637 ? 89.708  114.660 134.416 1.00 71.62  ?  637  PRO   B N     1 
ATOM   11038 C  CA    . PRO   B 1 637 ? 88.696  113.876 133.715 1.00 64.93  ?  637  PRO   B CA    1 
ATOM   11039 C  C     . PRO   B 1 637 ? 89.322  113.067 132.599 1.00 65.27  ?  637  PRO   B C     1 
ATOM   11040 O  O     . PRO   B 1 637 ? 90.321  113.490 131.987 1.00 74.74  ?  637  PRO   B O     1 
ATOM   11041 C  CB    . PRO   B 1 637 ? 87.744  114.947 133.164 1.00 63.23  ?  637  PRO   B CB    1 
ATOM   11042 C  CG    . PRO   B 1 637 ? 88.551  116.206 133.206 1.00 67.84  ?  637  PRO   B CG    1 
ATOM   11043 C  CD    . PRO   B 1 637 ? 89.352  116.084 134.442 1.00 67.52  ?  637  PRO   B CD    1 
ATOM   11044 N  N     . PRO   B 1 638 ? 88.765  111.901 132.288 1.00 58.72  ?  638  PRO   B N     1 
ATOM   11045 C  CA    . PRO   B 1 638 ? 89.341  111.081 131.222 1.00 59.51  ?  638  PRO   B CA    1 
ATOM   11046 C  C     . PRO   B 1 638 ? 89.010  111.643 129.849 1.00 63.86  ?  638  PRO   B C     1 
ATOM   11047 O  O     . PRO   B 1 638 ? 87.949  112.230 129.626 1.00 66.39  ?  638  PRO   B O     1 
ATOM   11048 C  CB    . PRO   B 1 638 ? 88.694  109.707 131.439 1.00 55.02  ?  638  PRO   B CB    1 
ATOM   11049 C  CG    . PRO   B 1 638 ? 87.515  109.941 132.361 1.00 61.18  ?  638  PRO   B CG    1 
ATOM   11050 C  CD    . PRO   B 1 638 ? 87.456  111.391 132.726 1.00 59.06  ?  638  PRO   B CD    1 
ATOM   11051 N  N     . ARG   B 1 639 ? 89.952  111.462 128.921 1.00 65.97  ?  639  ARG   B N     1 
ATOM   11052 C  CA    . ARG   B 1 639 ? 89.778  112.007 127.578 1.00 63.46  ?  639  ARG   B CA    1 
ATOM   11053 C  C     . ARG   B 1 639 ? 88.707  111.259 126.793 1.00 67.02  ?  639  ARG   B C     1 
ATOM   11054 O  O     . ARG   B 1 639 ? 88.000  111.866 125.981 1.00 76.81  ?  639  ARG   B O     1 
ATOM   11055 C  CB    . ARG   B 1 639 ? 91.108  111.983 126.828 1.00 58.39  ?  639  ARG   B CB    1 
ATOM   11056 C  CG    . ARG   B 1 639 ? 91.891  113.276 126.952 1.00 62.17  ?  639  ARG   B CG    1 
ATOM   11057 C  CD    . ARG   B 1 639 ? 93.357  113.079 126.634 1.00 62.53  ?  639  ARG   B CD    1 
ATOM   11058 N  NE    . ARG   B 1 639 ? 94.208  113.875 127.507 1.00 67.54  ?  639  ARG   B NE    1 
ATOM   11059 C  CZ    . ARG   B 1 639 ? 94.995  114.859 127.096 1.00 70.75  ?  639  ARG   B CZ    1 
ATOM   11060 N  NH1   . ARG   B 1 639 ? 95.061  115.204 125.821 1.00 69.56  ?  639  ARG   B NH1   1 
ATOM   11061 N  NH2   . ARG   B 1 639 ? 95.725  115.521 127.988 1.00 71.76  ?  639  ARG   B NH2   1 
ATOM   11062 N  N     . GLY   B 1 640 ? 88.571  109.952 127.016 1.00 55.63  ?  640  GLY   B N     1 
ATOM   11063 C  CA    . GLY   B 1 640 ? 87.551  109.169 126.351 1.00 55.19  ?  640  GLY   B CA    1 
ATOM   11064 C  C     . GLY   B 1 640 ? 87.097  108.036 127.243 1.00 61.76  ?  640  GLY   B C     1 
ATOM   11065 O  O     . GLY   B 1 640 ? 87.759  107.687 128.221 1.00 69.88  ?  640  GLY   B O     1 
ATOM   11066 N  N     . TYR   B 1 641 ? 85.975  107.422 126.858 1.00 57.80  ?  641  TYR   B N     1 
ATOM   11067 C  CA    . TYR   B 1 641 ? 85.521  106.221 127.551 1.00 55.72  ?  641  TYR   B CA    1 
ATOM   11068 C  C     . TYR   B 1 641 ? 86.550  105.106 127.433 1.00 61.08  ?  641  TYR   B C     1 
ATOM   11069 O  O     . TYR   B 1 641 ? 86.813  104.384 128.402 1.00 65.06  ?  641  TYR   B O     1 
ATOM   11070 C  CB    . TYR   B 1 641 ? 84.170  105.773 126.999 1.00 58.14  ?  641  TYR   B CB    1 
ATOM   11071 C  CG    . TYR   B 1 641 ? 83.053  106.754 127.265 1.00 64.78  ?  641  TYR   B CG    1 
ATOM   11072 C  CD1   . TYR   B 1 641 ? 82.617  107.002 128.558 1.00 66.81  ?  641  TYR   B CD1   1 
ATOM   11073 C  CD2   . TYR   B 1 641 ? 82.436  107.432 126.224 1.00 64.16  ?  641  TYR   B CD2   1 
ATOM   11074 C  CE1   . TYR   B 1 641 ? 81.599  107.899 128.807 1.00 66.35  ?  641  TYR   B CE1   1 
ATOM   11075 C  CE2   . TYR   B 1 641 ? 81.415  108.331 126.464 1.00 61.63  ?  641  TYR   B CE2   1 
ATOM   11076 C  CZ    . TYR   B 1 641 ? 81.001  108.559 127.757 1.00 66.86  ?  641  TYR   B CZ    1 
ATOM   11077 O  OH    . TYR   B 1 641 ? 79.984  109.453 128.000 1.00 71.61  ?  641  TYR   B OH    1 
ATOM   11078 N  N     . VAL   B 1 642 ? 87.138  104.950 126.252 1.00 62.04  ?  642  VAL   B N     1 
ATOM   11079 C  CA    . VAL   B 1 642 ? 88.305  104.103 126.046 1.00 56.89  ?  642  VAL   B CA    1 
ATOM   11080 C  C     . VAL   B 1 642 ? 89.427  105.040 125.622 1.00 60.28  ?  642  VAL   B C     1 
ATOM   11081 O  O     . VAL   B 1 642 ? 89.492  105.464 124.463 1.00 70.74  ?  642  VAL   B O     1 
ATOM   11082 C  CB    . VAL   B 1 642 ? 88.060  103.007 125.003 1.00 53.61  ?  642  VAL   B CB    1 
ATOM   11083 C  CG1   . VAL   B 1 642 ? 89.356  102.277 124.688 1.00 57.49  ?  642  VAL   B CG1   1 
ATOM   11084 C  CG2   . VAL   B 1 642 ? 87.003  102.034 125.498 1.00 62.62  ?  642  VAL   B CG2   1 
ATOM   11085 N  N     . SER   B 1 643 ? 90.300  105.383 126.560 1.00 60.92  ?  643  SER   B N     1 
ATOM   11086 C  CA    . SER   B 1 643 ? 91.402  106.290 126.288 1.00 62.01  ?  643  SER   B CA    1 
ATOM   11087 C  C     . SER   B 1 643 ? 92.657  105.505 125.929 1.00 63.71  ?  643  SER   B C     1 
ATOM   11088 O  O     . SER   B 1 643 ? 92.761  104.303 126.175 1.00 71.22  ?  643  SER   B O     1 
ATOM   11089 C  CB    . SER   B 1 643 ? 91.669  107.192 127.493 1.00 63.25  ?  643  SER   B CB    1 
ATOM   11090 O  OG    . SER   B 1 643 ? 92.092  106.436 128.614 1.00 74.76  ?  643  SER   B OG    1 
ATOM   11091 N  N     . ILE   B 1 644 ? 93.616  106.204 125.332 1.00 59.92  ?  644  ILE   B N     1 
ATOM   11092 C  CA    . ILE   B 1 644 ? 94.872  105.605 124.903 1.00 56.89  ?  644  ILE   B CA    1 
ATOM   11093 C  C     . ILE   B 1 644 ? 95.999  106.245 125.698 1.00 60.89  ?  644  ILE   B C     1 
ATOM   11094 O  O     . ILE   B 1 644 ? 96.235  107.454 125.589 1.00 70.63  ?  644  ILE   B O     1 
ATOM   11095 C  CB    . ILE   B 1 644 ? 95.101  105.774 123.393 1.00 63.76  ?  644  ILE   B CB    1 
ATOM   11096 C  CG1   . ILE   B 1 644 ? 93.945  105.154 122.607 1.00 65.51  ?  644  ILE   B CG1   1 
ATOM   11097 C  CG2   . ILE   B 1 644 ? 96.422  105.147 122.984 1.00 61.10  ?  644  ILE   B CG2   1 
ATOM   11098 C  CD1   . ILE   B 1 644 ? 93.877  103.648 122.705 1.00 66.93  ?  644  ILE   B CD1   1 
ATOM   11099 N  N     . LYS   B 1 645 ? 96.690  105.436 126.493 1.00 62.78  ?  645  LYS   B N     1 
ATOM   11100 C  CA    . LYS   B 1 645 ? 97.869  105.870 127.229 1.00 56.32  ?  645  LYS   B CA    1 
ATOM   11101 C  C     . LYS   B 1 645 ? 99.102  105.429 126.453 1.00 63.03  ?  645  LYS   B C     1 
ATOM   11102 O  O     . LYS   B 1 645 ? 99.320  104.229 126.257 1.00 73.55  ?  645  LYS   B O     1 
ATOM   11103 C  CB    . LYS   B 1 645 ? 97.880  105.289 128.642 1.00 56.05  ?  645  LYS   B CB    1 
ATOM   11104 C  CG    . LYS   B 1 645 ? 96.555  105.410 129.373 1.00 60.71  ?  645  LYS   B CG    1 
ATOM   11105 C  CD    . LYS   B 1 645 ? 96.360  106.809 129.928 1.00 64.01  ?  645  LYS   B CD    1 
ATOM   11106 C  CE    . LYS   B 1 645 ? 94.957  106.997 130.471 1.00 63.76  ?  645  LYS   B CE    1 
ATOM   11107 N  NZ    . LYS   B 1 645 ? 94.949  107.087 131.954 1.00 65.18  ?  645  LYS   B NZ    1 
ATOM   11108 N  N     . ALA   B 1 646 ? 99.895  106.394 126.003 1.00 63.45  ?  646  ALA   B N     1 
ATOM   11109 C  CA    . ALA   B 1 646 ? 101.067 106.126 125.185 1.00 59.41  ?  646  ALA   B CA    1 
ATOM   11110 C  C     . ALA   B 1 646 ? 102.327 106.397 125.992 1.00 66.73  ?  646  ALA   B C     1 
ATOM   11111 O  O     . ALA   B 1 646 ? 102.454 107.453 126.619 1.00 73.13  ?  646  ALA   B O     1 
ATOM   11112 C  CB    . ALA   B 1 646 ? 101.052 106.980 123.916 1.00 65.78  ?  646  ALA   B CB    1 
ATOM   11113 N  N     . SER   B 1 647 ? 103.248 105.438 125.982 1.00 78.55  ?  647  SER   B N     1 
ATOM   11114 C  CA    . SER   B 1 647 ? 104.548 105.601 126.619 1.00 81.19  ?  647  SER   B CA    1 
ATOM   11115 C  C     . SER   B 1 647 ? 105.526 104.664 125.930 1.00 83.79  ?  647  SER   B C     1 
ATOM   11116 O  O     . SER   B 1 647 ? 105.143 103.828 125.107 1.00 84.83  ?  647  SER   B O     1 
ATOM   11117 C  CB    . SER   B 1 647 ? 104.489 105.310 128.121 1.00 80.02  ?  647  SER   B CB    1 
ATOM   11118 O  OG    . SER   B 1 647 ? 103.945 104.024 128.356 1.00 78.96  ?  647  SER   B OG    1 
ATOM   11119 N  N     . LYS   B 1 648 ? 106.801 104.802 126.292 1.00 88.18  ?  648  LYS   B N     1 
ATOM   11120 C  CA    . LYS   B 1 648 ? 107.819 103.914 125.746 1.00 86.93  ?  648  LYS   B CA    1 
ATOM   11121 C  C     . LYS   B 1 648 ? 107.560 102.461 126.113 1.00 86.88  ?  648  LYS   B C     1 
ATOM   11122 O  O     . LYS   B 1 648 ? 108.104 101.560 125.465 1.00 91.31  ?  648  LYS   B O     1 
ATOM   11123 C  CB    . LYS   B 1 648 ? 109.204 104.336 126.233 1.00 81.63  ?  648  LYS   B CB    1 
ATOM   11124 C  CG    . LYS   B 1 648 ? 109.527 105.797 125.988 1.00 84.76  ?  648  LYS   B CG    1 
ATOM   11125 C  CD    . LYS   B 1 648 ? 110.000 106.027 124.568 1.00 81.91  ?  648  LYS   B CD    1 
ATOM   11126 C  CE    . LYS   B 1 648 ? 110.357 107.485 124.340 1.00 87.52  ?  648  LYS   B CE    1 
ATOM   11127 N  NZ    . LYS   B 1 648 ? 110.498 107.806 122.894 1.00 89.84  ?  648  LYS   B NZ    1 
ATOM   11128 N  N     . ASP   B 1 649 ? 106.741 102.215 127.131 1.00 86.51  ?  649  ASP   B N     1 
ATOM   11129 C  CA    . ASP   B 1 649 ? 106.386 100.870 127.550 1.00 90.13  ?  649  ASP   B CA    1 
ATOM   11130 C  C     . ASP   B 1 649 ? 105.084 100.375 126.929 1.00 89.35  ?  649  ASP   B C     1 
ATOM   11131 O  O     . ASP   B 1 649 ? 104.617 99.293  127.293 1.00 89.25  ?  649  ASP   B O     1 
ATOM   11132 C  CB    . ASP   B 1 649 ? 106.301 100.802 129.076 1.00 90.70  ?  649  ASP   B CB    1 
ATOM   11133 C  CG    . ASP   B 1 649 ? 107.668 100.850 129.733 1.00 94.45  ?  649  ASP   B CG    1 
ATOM   11134 O  OD1   . ASP   B 1 649 ? 108.289 99.779  129.899 1.00 92.60  ?  649  ASP   B OD1   1 
ATOM   11135 O  OD2   . ASP   B 1 649 ? 108.131 101.960 130.068 1.00 96.50  ?  649  ASP   B OD2   1 
ATOM   11136 N  N     . GLY   B 1 650 ? 104.493 101.123 126.014 1.00 76.34  ?  650  GLY   B N     1 
ATOM   11137 C  CA    . GLY   B 1 650 ? 103.367 100.606 125.263 1.00 71.58  ?  650  GLY   B CA    1 
ATOM   11138 C  C     . GLY   B 1 650 ? 102.353 101.674 124.921 1.00 72.15  ?  650  GLY   B C     1 
ATOM   11139 O  O     . GLY   B 1 650 ? 102.259 102.723 125.553 1.00 77.51  ?  650  GLY   B O     1 
ATOM   11140 N  N     . ILE   B 1 651 ? 101.511 101.348 123.946 1.00 69.63  ?  651  ILE   B N     1 
ATOM   11141 C  CA    . ILE   B 1 651 ? 100.279 102.076 123.669 1.00 73.02  ?  651  ILE   B CA    1 
ATOM   11142 C  C     . ILE   B 1 651 ? 99.144  101.201 124.190 1.00 74.33  ?  651  ILE   B C     1 
ATOM   11143 O  O     . ILE   B 1 651 ? 98.929  100.087 123.698 1.00 83.06  ?  651  ILE   B O     1 
ATOM   11144 C  CB    . ILE   B 1 651 ? 100.124 102.390 122.173 1.00 70.03  ?  651  ILE   B CB    1 
ATOM   11145 C  CG1   . ILE   B 1 651 ? 100.803 103.718 121.823 1.00 76.80  ?  651  ILE   B CG1   1 
ATOM   11146 C  CG2   . ILE   B 1 651 ? 98.658  102.458 121.776 1.00 71.84  ?  651  ILE   B CG2   1 
ATOM   11147 C  CD1   . ILE   B 1 651 ? 102.309 103.713 121.951 1.00 77.63  ?  651  ILE   B CD1   1 
ATOM   11148 N  N     . LEU   B 1 652 ? 98.435  101.682 125.207 1.00 56.38  ?  652  LEU   B N     1 
ATOM   11149 C  CA    . LEU   B 1 652 ? 97.502  100.861 125.963 1.00 55.53  ?  652  LEU   B CA    1 
ATOM   11150 C  C     . LEU   B 1 652 ? 96.108  101.467 125.925 1.00 55.39  ?  652  LEU   B C     1 
ATOM   11151 O  O     . LEU   B 1 652 ? 95.949  102.688 126.000 1.00 60.53  ?  652  LEU   B O     1 
ATOM   11152 C  CB    . LEU   B 1 652 ? 97.965  100.710 127.415 1.00 53.23  ?  652  LEU   B CB    1 
ATOM   11153 C  CG    . LEU   B 1 652 ? 99.479  100.620 127.616 1.00 53.36  ?  652  LEU   B CG    1 
ATOM   11154 C  CD1   . LEU   B 1 652 ? 99.844  100.732 129.086 1.00 53.27  ?  652  LEU   B CD1   1 
ATOM   11155 C  CD2   . LEU   B 1 652 ? 100.016 99.330  127.022 1.00 55.53  ?  652  LEU   B CD2   1 
ATOM   11156 N  N     . ARG   B 1 653 ? 95.103  100.606 125.811 1.00 56.73  ?  653  ARG   B N     1 
ATOM   11157 C  CA    . ARG   B 1 653 ? 93.708  101.018 125.823 1.00 57.50  ?  653  ARG   B CA    1 
ATOM   11158 C  C     . ARG   B 1 653 ? 93.162  100.840 127.234 1.00 63.57  ?  653  ARG   B C     1 
ATOM   11159 O  O     . ARG   B 1 653 ? 93.143  99.723  127.760 1.00 74.27  ?  653  ARG   B O     1 
ATOM   11160 C  CB    . ARG   B 1 653 ? 92.891  100.209 124.817 1.00 54.19  ?  653  ARG   B CB    1 
ATOM   11161 C  CG    . ARG   B 1 653 ? 93.597  99.983  123.493 1.00 59.42  ?  653  ARG   B CG    1 
ATOM   11162 C  CD    . ARG   B 1 653 ? 92.703  99.261  122.502 1.00 57.13  ?  653  ARG   B CD    1 
ATOM   11163 N  NE    . ARG   B 1 653 ? 91.473  99.997  122.239 1.00 66.54  ?  653  ARG   B NE    1 
ATOM   11164 C  CZ    . ARG   B 1 653 ? 91.268  100.752 121.170 1.00 69.94  ?  653  ARG   B CZ    1 
ATOM   11165 N  NH1   . ARG   B 1 653 ? 92.197  100.900 120.241 1.00 67.61  ?  653  ARG   B NH1   1 
ATOM   11166 N  NH2   . ARG   B 1 653 ? 90.112  101.397 121.043 1.00 69.77  ?  653  ARG   B NH2   1 
ATOM   11167 N  N     . GLN   B 1 654 ? 92.727  101.939 127.842 1.00 60.68  ?  654  GLN   B N     1 
ATOM   11168 C  CA    . GLN   B 1 654 ? 92.218  101.940 129.205 1.00 52.47  ?  654  GLN   B CA    1 
ATOM   11169 C  C     . GLN   B 1 654 ? 90.753  102.343 129.197 1.00 64.70  ?  654  GLN   B C     1 
ATOM   11170 O  O     . GLN   B 1 654 ? 90.398  103.399 128.665 1.00 71.70  ?  654  GLN   B O     1 
ATOM   11171 C  CB    . GLN   B 1 654 ? 93.022  102.894 130.090 1.00 53.97  ?  654  GLN   B CB    1 
ATOM   11172 C  CG    . GLN   B 1 654 ? 93.167  102.432 131.526 1.00 64.27  ?  654  GLN   B CG    1 
ATOM   11173 C  CD    . GLN   B 1 654 ? 93.645  103.537 132.443 1.00 68.63  ?  654  GLN   B CD    1 
ATOM   11174 O  OE1   . GLN   B 1 654 ? 94.748  104.056 132.285 1.00 74.05  ?  654  GLN   B OE1   1 
ATOM   11175 N  NE2   . GLN   B 1 654 ? 92.814  103.905 133.408 1.00 72.12  ?  654  GLN   B NE2   1 
ATOM   11176 N  N     . VAL   B 1 655 ? 89.913  101.509 129.786 1.00 63.82  ?  655  VAL   B N     1 
ATOM   11177 C  CA    . VAL   B 1 655 ? 88.497  101.812 129.942 1.00 58.14  ?  655  VAL   B CA    1 
ATOM   11178 C  C     . VAL   B 1 655 ? 88.298  102.511 131.277 1.00 59.92  ?  655  VAL   B C     1 
ATOM   11179 O  O     . VAL   B 1 655 ? 88.959  102.183 132.269 1.00 66.43  ?  655  VAL   B O     1 
ATOM   11180 C  CB    . VAL   B 1 655 ? 87.646  100.532 129.850 1.00 55.61  ?  655  VAL   B CB    1 
ATOM   11181 C  CG1   . VAL   B 1 655 ? 86.180  100.881 129.662 1.00 59.35  ?  655  VAL   B CG1   1 
ATOM   11182 C  CG2   . VAL   B 1 655 ? 88.136  99.654  128.715 1.00 58.03  ?  655  VAL   B CG2   1 
ATOM   11183 N  N     . VAL   B 1 656 ? 87.398  103.490 131.300 1.00 55.90  ?  656  VAL   B N     1 
ATOM   11184 C  CA    . VAL   B 1 656 ? 87.092  104.156 132.569 1.00 55.08  ?  656  VAL   B CA    1 
ATOM   11185 C  C     . VAL   B 1 656 ? 86.483  103.141 133.525 1.00 60.04  ?  656  VAL   B C     1 
ATOM   11186 O  O     . VAL   B 1 656 ? 85.744  102.238 133.080 1.00 61.06  ?  656  VAL   B O     1 
ATOM   11187 C  CB    . VAL   B 1 656 ? 86.146  105.348 132.345 1.00 52.72  ?  656  VAL   B CB    1 
ATOM   11188 C  CG1   . VAL   B 1 656 ? 86.835  106.415 131.516 1.00 53.70  ?  656  VAL   B CG1   1 
ATOM   11189 C  CG2   . VAL   B 1 656 ? 84.859  104.898 131.670 1.00 57.13  ?  656  VAL   B CG2   1 
ATOM   11190 N  N     . PRO   B 1 657 ? 86.779  103.199 134.823 1.00 59.00  ?  657  PRO   B N     1 
ATOM   11191 C  CA    . PRO   B 1 657 ? 86.215  102.212 135.750 1.00 61.12  ?  657  PRO   B CA    1 
ATOM   11192 C  C     . PRO   B 1 657 ? 84.695  102.271 135.778 1.00 58.85  ?  657  PRO   B C     1 
ATOM   11193 O  O     . PRO   B 1 657 ? 84.095  103.348 135.746 1.00 60.90  ?  657  PRO   B O     1 
ATOM   11194 C  CB    . PRO   B 1 657 ? 86.820  102.620 137.096 1.00 57.02  ?  657  PRO   B CB    1 
ATOM   11195 C  CG    . PRO   B 1 657 ? 87.092  104.078 136.917 1.00 50.89  ?  657  PRO   B CG    1 
ATOM   11196 C  CD    . PRO   B 1 657 ? 87.640  104.156 135.533 1.00 49.60  ?  657  PRO   B CD    1 
ATOM   11197 N  N     . ASP   B 1 658 ? 84.078  101.093 135.843 1.00 80.94  ?  658  ASP   B N     1 
ATOM   11198 C  CA    . ASP   B 1 658 ? 82.625  100.944 135.855 1.00 78.17  ?  658  ASP   B CA    1 
ATOM   11199 C  C     . ASP   B 1 658 ? 81.994  101.675 134.668 1.00 75.81  ?  658  ASP   B C     1 
ATOM   11200 O  O     . ASP   B 1 658 ? 81.164  102.571 134.815 1.00 85.19  ?  658  ASP   B O     1 
ATOM   11201 C  CB    . ASP   B 1 658 ? 82.046  101.428 137.187 1.00 76.09  ?  658  ASP   B CB    1 
ATOM   11202 C  CG    . ASP   B 1 658 ? 80.621  100.962 137.420 1.00 85.77  ?  658  ASP   B CG    1 
ATOM   11203 O  OD1   . ASP   B 1 658 ? 79.862  100.827 136.441 1.00 90.33  ?  658  ASP   B OD1   1 
ATOM   11204 O  OD2   . ASP   B 1 658 ? 80.223  100.840 138.596 1.00 87.69  ?  658  ASP   B OD2   1 
ATOM   11205 N  N     . TYR   B 1 659 ? 82.412  101.270 133.468 1.00 72.04  ?  659  TYR   B N     1 
ATOM   11206 C  CA    . TYR   B 1 659 ? 81.895  101.910 132.265 1.00 72.73  ?  659  TYR   B CA    1 
ATOM   11207 C  C     . TYR   B 1 659 ? 80.458  101.496 131.976 1.00 75.41  ?  659  TYR   B C     1 
ATOM   11208 O  O     . TYR   B 1 659 ? 79.678  102.299 131.453 1.00 78.80  ?  659  TYR   B O     1 
ATOM   11209 C  CB    . TYR   B 1 659 ? 82.788  101.589 131.065 1.00 70.41  ?  659  TYR   B CB    1 
ATOM   11210 C  CG    . TYR   B 1 659 ? 82.123  101.861 129.735 1.00 72.26  ?  659  TYR   B CG    1 
ATOM   11211 C  CD1   . TYR   B 1 659 ? 82.047  103.149 129.229 1.00 76.24  ?  659  TYR   B CD1   1 
ATOM   11212 C  CD2   . TYR   B 1 659 ? 81.562  100.833 128.991 1.00 70.84  ?  659  TYR   B CD2   1 
ATOM   11213 C  CE1   . TYR   B 1 659 ? 81.437  103.407 128.020 1.00 74.48  ?  659  TYR   B CE1   1 
ATOM   11214 C  CE2   . TYR   B 1 659 ? 80.946  101.083 127.781 1.00 74.34  ?  659  TYR   B CE2   1 
ATOM   11215 C  CZ    . TYR   B 1 659 ? 80.890  102.372 127.299 1.00 75.89  ?  659  TYR   B CZ    1 
ATOM   11216 O  OH    . TYR   B 1 659 ? 80.274  102.631 126.097 1.00 78.91  ?  659  TYR   B OH    1 
ATOM   11217 N  N     . GLU   B 1 660 ? 80.092  100.254 132.303 1.00 95.21  ?  660  GLU   B N     1 
ATOM   11218 C  CA    . GLU   B 1 660 ? 78.774  99.746  131.935 1.00 96.53  ?  660  GLU   B CA    1 
ATOM   11219 C  C     . GLU   B 1 660 ? 77.657  100.516 132.629 1.00 100.08 ?  660  GLU   B C     1 
ATOM   11220 O  O     . GLU   B 1 660 ? 76.656  100.874 131.998 1.00 104.29 ?  660  GLU   B O     1 
ATOM   11221 C  CB    . GLU   B 1 660 ? 78.677  98.257  132.267 1.00 97.45  ?  660  GLU   B CB    1 
ATOM   11222 C  CG    . GLU   B 1 660 ? 79.205  97.340  131.179 1.00 100.76 ?  660  GLU   B CG    1 
ATOM   11223 C  CD    . GLU   B 1 660 ? 80.628  96.890  131.442 1.00 106.04 ?  660  GLU   B CD    1 
ATOM   11224 O  OE1   . GLU   B 1 660 ? 81.384  97.651  132.081 1.00 106.99 ?  660  GLU   B OE1   1 
ATOM   11225 O  OE2   . GLU   B 1 660 ? 80.993  95.778  131.005 1.00 104.37 ?  660  GLU   B OE2   1 
ATOM   11226 N  N     . HIS   B 1 661 ? 77.808  100.782 133.924 1.00 93.97  ?  661  HIS   B N     1 
ATOM   11227 C  CA    . HIS   B 1 661 ? 76.756  101.408 134.712 1.00 93.70  ?  661  HIS   B CA    1 
ATOM   11228 C  C     . HIS   B 1 661 ? 76.991  102.891 134.970 1.00 96.27  ?  661  HIS   B C     1 
ATOM   11229 O  O     . HIS   B 1 661 ? 76.189  103.513 135.673 1.00 103.09 ?  661  HIS   B O     1 
ATOM   11230 C  CB    . HIS   B 1 661 ? 76.591  100.679 136.053 1.00 94.61  ?  661  HIS   B CB    1 
ATOM   11231 C  CG    . HIS   B 1 661 ? 76.686  99.188  135.951 1.00 100.43 ?  661  HIS   B CG    1 
ATOM   11232 N  ND1   . HIS   B 1 661 ? 75.598  98.388  135.676 1.00 104.08 ?  661  HIS   B ND1   1 
ATOM   11233 C  CD2   . HIS   B 1 661 ? 77.738  98.350  136.106 1.00 100.01 ?  661  HIS   B CD2   1 
ATOM   11234 C  CE1   . HIS   B 1 661 ? 75.977  97.123  135.660 1.00 100.96 ?  661  HIS   B CE1   1 
ATOM   11235 N  NE2   . HIS   B 1 661 ? 77.276  97.074  135.892 1.00 102.99 ?  661  HIS   B NE2   1 
ATOM   11236 N  N     . LEU   B 1 662 ? 78.057  103.478 134.422 1.00 77.74  ?  662  LEU   B N     1 
ATOM   11237 C  CA    . LEU   B 1 662 ? 78.369  104.867 134.734 1.00 78.41  ?  662  LEU   B CA    1 
ATOM   11238 C  C     . LEU   B 1 662 ? 78.836  105.675 133.529 1.00 78.69  ?  662  LEU   B C     1 
ATOM   11239 O  O     . LEU   B 1 662 ? 79.353  106.783 133.716 1.00 85.03  ?  662  LEU   B O     1 
ATOM   11240 C  CB    . LEU   B 1 662 ? 79.434  104.936 135.836 1.00 75.81  ?  662  LEU   B CB    1 
ATOM   11241 C  CG    . LEU   B 1 662 ? 79.273  106.002 136.918 1.00 76.19  ?  662  LEU   B CG    1 
ATOM   11242 C  CD1   . LEU   B 1 662 ? 77.904  105.906 137.566 1.00 79.43  ?  662  LEU   B CD1   1 
ATOM   11243 C  CD2   . LEU   B 1 662 ? 80.372  105.852 137.952 1.00 78.97  ?  662  LEU   B CD2   1 
ATOM   11244 N  N     . HIS   B 1 663 ? 78.671  105.171 132.303 1.00 81.43  ?  663  HIS   B N     1 
ATOM   11245 C  CA    . HIS   B 1 663 ? 79.145  105.912 131.138 1.00 83.70  ?  663  HIS   B CA    1 
ATOM   11246 C  C     . HIS   B 1 663 ? 78.396  107.226 130.961 1.00 86.24  ?  663  HIS   B C     1 
ATOM   11247 O  O     . HIS   B 1 663 ? 78.986  108.222 130.527 1.00 88.28  ?  663  HIS   B O     1 
ATOM   11248 C  CB    . HIS   B 1 663 ? 79.024  105.053 129.879 1.00 82.06  ?  663  HIS   B CB    1 
ATOM   11249 C  CG    . HIS   B 1 663 ? 77.613  104.759 129.476 1.00 85.39  ?  663  HIS   B CG    1 
ATOM   11250 N  ND1   . HIS   B 1 663 ? 76.942  103.629 129.891 1.00 86.21  ?  663  HIS   B ND1   1 
ATOM   11251 C  CD2   . HIS   B 1 663 ? 76.748  105.444 128.692 1.00 86.65  ?  663  HIS   B CD2   1 
ATOM   11252 C  CE1   . HIS   B 1 663 ? 75.723  103.632 129.383 1.00 85.82  ?  663  HIS   B CE1   1 
ATOM   11253 N  NE2   . HIS   B 1 663 ? 75.579  104.723 128.652 1.00 86.69  ?  663  HIS   B NE2   1 
ATOM   11254 N  N     . ASP   B 1 664 ? 77.104  107.254 131.292 1.00 86.03  ?  664  ASP   B N     1 
ATOM   11255 C  CA    . ASP   B 1 664 ? 76.334  108.484 131.164 1.00 84.54  ?  664  ASP   B CA    1 
ATOM   11256 C  C     . ASP   B 1 664 ? 76.705  109.514 132.222 1.00 86.73  ?  664  ASP   B C     1 
ATOM   11257 O  O     . ASP   B 1 664 ? 76.496  110.712 132.002 1.00 88.36  ?  664  ASP   B O     1 
ATOM   11258 C  CB    . ASP   B 1 664 ? 74.839  108.176 131.242 1.00 88.86  ?  664  ASP   B CB    1 
ATOM   11259 C  CG    . ASP   B 1 664 ? 74.279  107.682 129.924 1.00 95.40  ?  664  ASP   B CG    1 
ATOM   11260 O  OD1   . ASP   B 1 664 ? 74.928  107.904 128.880 1.00 95.61  ?  664  ASP   B OD1   1 
ATOM   11261 O  OD2   . ASP   B 1 664 ? 73.194  107.064 129.933 1.00 97.79  ?  664  ASP   B OD2   1 
ATOM   11262 N  N     . ALA   B 1 665 ? 77.249  109.081 133.357 1.00 78.85  ?  665  ALA   B N     1 
ATOM   11263 C  CA    . ALA   B 1 665 ? 77.607  109.988 134.436 1.00 74.27  ?  665  ALA   B CA    1 
ATOM   11264 C  C     . ALA   B 1 665 ? 78.998  110.586 134.287 1.00 72.75  ?  665  ALA   B C     1 
ATOM   11265 O  O     . ALA   B 1 665 ? 79.345  111.493 135.049 1.00 76.32  ?  665  ALA   B O     1 
ATOM   11266 C  CB    . ALA   B 1 665 ? 77.508  109.267 135.785 1.00 73.38  ?  665  ALA   B CB    1 
ATOM   11267 N  N     . TYR   B 1 666 ? 79.799  110.100 133.343 1.00 68.86  ?  666  TYR   B N     1 
ATOM   11268 C  CA    . TYR   B 1 666 ? 81.131  110.640 133.129 1.00 58.88  ?  666  TYR   B CA    1 
ATOM   11269 C  C     . TYR   B 1 666 ? 81.066  111.914 132.299 1.00 64.34  ?  666  TYR   B C     1 
ATOM   11270 O  O     . TYR   B 1 666 ? 80.203  112.077 131.432 1.00 74.53  ?  666  TYR   B O     1 
ATOM   11271 C  CB    . TYR   B 1 666 ? 82.022  109.616 132.428 1.00 64.70  ?  666  TYR   B CB    1 
ATOM   11272 C  CG    . TYR   B 1 666 ? 82.742  108.675 133.365 1.00 67.92  ?  666  TYR   B CG    1 
ATOM   11273 C  CD1   . TYR   B 1 666 ? 83.814  109.109 134.130 1.00 65.82  ?  666  TYR   B CD1   1 
ATOM   11274 C  CD2   . TYR   B 1 666 ? 82.353  107.350 133.479 1.00 65.90  ?  666  TYR   B CD2   1 
ATOM   11275 C  CE1   . TYR   B 1 666 ? 84.473  108.250 134.987 1.00 60.97  ?  666  TYR   B CE1   1 
ATOM   11276 C  CE2   . TYR   B 1 666 ? 83.004  106.486 134.331 1.00 64.07  ?  666  TYR   B CE2   1 
ATOM   11277 C  CZ    . TYR   B 1 666 ? 84.063  106.940 135.082 1.00 62.91  ?  666  TYR   B CZ    1 
ATOM   11278 O  OH    . TYR   B 1 666 ? 84.713  106.076 135.931 1.00 71.41  ?  666  TYR   B OH    1 
ATOM   11279 N  N     . GLU   B 1 667 ? 81.994  112.838 132.574 1.00 73.22  ?  667  GLU   B N     1 
ATOM   11280 C  CA    . GLU   B 1 667 ? 82.138  114.083 131.778 1.00 73.60  ?  667  GLU   B CA    1 
ATOM   11281 C  C     . GLU   B 1 667 ? 83.550  114.043 131.189 1.00 76.23  ?  667  GLU   B C     1 
ATOM   11282 O  O     . GLU   B 1 667 ? 84.489  114.149 131.976 1.00 87.29  ?  667  GLU   B O     1 
ATOM   11283 C  CB    . GLU   B 1 667 ? 81.914  115.358 132.585 1.00 76.11  ?  667  GLU   B CB    1 
ATOM   11284 C  CG    . GLU   B 1 667 ? 81.905  116.608 131.712 1.00 77.66  ?  667  GLU   B CG    1 
ATOM   11285 C  CD    . GLU   B 1 667 ? 81.326  117.829 132.395 1.00 87.18  ?  667  GLU   B CD    1 
ATOM   11286 O  OE1   . GLU   B 1 667 ? 81.903  118.245 133.415 1.00 91.00  ?  667  GLU   B OE1   1 
ATOM   11287 O  OE2   . GLU   B 1 667 ? 80.304  118.359 131.916 1.00 89.18  ?  667  GLU   B OE2   1 
ATOM   11288 N  N     . LEU   B 1 668 ? 83.697  113.887 129.875 1.00 62.33  ?  668  LEU   B N     1 
ATOM   11289 C  CA    . LEU   B 1 668 ? 85.027  113.700 129.245 1.00 66.58  ?  668  LEU   B CA    1 
ATOM   11290 C  C     . LEU   B 1 668 ? 85.696  115.058 129.076 1.00 63.53  ?  668  LEU   B C     1 
ATOM   11291 O  O     . LEU   B 1 668 ? 84.978  116.057 129.043 1.00 69.01  ?  668  LEU   B O     1 
ATOM   11292 C  CB    . LEU   B 1 668 ? 84.873  112.925 127.940 1.00 64.42  ?  668  LEU   B CB    1 
ATOM   11293 C  CG    . LEU   B 1 668 ? 84.179  111.564 128.060 1.00 64.08  ?  668  LEU   B CG    1 
ATOM   11294 C  CD1   . LEU   B 1 668 ? 84.121  110.867 126.725 1.00 67.66  ?  668  LEU   B CD1   1 
ATOM   11295 C  CD2   . LEU   B 1 668 ? 84.867  110.676 129.078 1.00 57.73  ?  668  LEU   B CD2   1 
ATOM   11296 N  N     . LEU   B 1 669 ? 87.015  115.090 129.006 1.00 57.74  ?  669  LEU   B N     1 
ATOM   11297 C  CA    . LEU   B 1 669 ? 87.760  116.369 128.968 1.00 55.22  ?  669  LEU   B CA    1 
ATOM   11298 C  C     . LEU   B 1 669 ? 87.251  117.302 127.862 1.00 62.03  ?  669  LEU   B C     1 
ATOM   11299 O  O     . LEU   B 1 669 ? 87.135  118.497 128.151 1.00 68.80  ?  669  LEU   B O     1 
ATOM   11300 C  CB    . LEU   B 1 669 ? 89.233  116.041 128.771 1.00 55.61  ?  669  LEU   B CB    1 
ATOM   11301 C  CG    . LEU   B 1 669 ? 90.200  117.219 128.862 1.00 58.01  ?  669  LEU   B CG    1 
ATOM   11302 C  CD1   . LEU   B 1 669 ? 90.475  117.474 130.319 1.00 61.17  ?  669  LEU   B CD1   1 
ATOM   11303 C  CD2   . LEU   B 1 669 ? 91.478  116.973 128.090 1.00 61.00  ?  669  LEU   B CD2   1 
ATOM   11304 N  N     . TRP   B 1 670 ? 86.980  116.826 126.651 1.00 59.82  ?  670  TRP   B N     1 
ATOM   11305 C  CA    . TRP   B 1 670 ? 86.616  117.701 125.507 1.00 57.70  ?  670  TRP   B CA    1 
ATOM   11306 C  C     . TRP   B 1 670 ? 85.109  117.923 125.474 1.00 62.84  ?  670  TRP   B C     1 
ATOM   11307 O  O     . TRP   B 1 670 ? 84.617  118.376 124.437 1.00 73.45  ?  670  TRP   B O     1 
ATOM   11308 C  CB    . TRP   B 1 670 ? 87.157  117.081 124.213 1.00 58.53  ?  670  TRP   B CB    1 
ATOM   11309 C  CG    . TRP   B 1 670 ? 88.653  116.927 124.211 1.00 56.29  ?  670  TRP   B CG    1 
ATOM   11310 C  CD1   . TRP   B 1 670 ? 89.351  115.792 123.935 1.00 58.62  ?  670  TRP   B CD1   1 
ATOM   11311 C  CD2   . TRP   B 1 670 ? 89.635  117.944 124.503 1.00 57.75  ?  670  TRP   B CD2   1 
ATOM   11312 N  NE1   . TRP   B 1 670 ? 90.694  116.025 124.035 1.00 65.29  ?  670  TRP   B NE1   1 
ATOM   11313 C  CE2   . TRP   B 1 670 ? 90.900  117.334 124.377 1.00 65.32  ?  670  TRP   B CE2   1 
ATOM   11314 C  CE3   . TRP   B 1 670 ? 89.572  119.296 124.852 1.00 54.68  ?  670  TRP   B CE3   1 
ATOM   11315 C  CZ2   . TRP   B 1 670 ? 92.084  118.031 124.593 1.00 60.86  ?  670  TRP   B CZ2   1 
ATOM   11316 C  CZ3   . TRP   B 1 670 ? 90.745  119.985 125.057 1.00 56.35  ?  670  TRP   B CZ3   1 
ATOM   11317 C  CH2   . TRP   B 1 670 ? 91.982  119.359 124.932 1.00 57.52  ?  670  TRP   B CH2   1 
ATOM   11318 N  N     . GLU   B 1 671 ? 84.404  117.630 126.564 1.00 71.59  ?  671  GLU   B N     1 
ATOM   11319 C  CA    . GLU   B 1 671 ? 82.949  117.875 126.687 1.00 70.49  ?  671  GLU   B CA    1 
ATOM   11320 C  C     . GLU   B 1 671 ? 82.742  118.943 127.756 1.00 71.78  ?  671  GLU   B C     1 
ATOM   11321 O  O     . GLU   B 1 671 ? 81.593  119.124 128.180 1.00 80.69  ?  671  GLU   B O     1 
ATOM   11322 C  CB    . GLU   B 1 671 ? 82.210  116.594 127.054 1.00 73.08  ?  671  GLU   B CB    1 
ATOM   11323 C  CG    . GLU   B 1 671 ? 82.402  115.458 126.056 1.00 77.03  ?  671  GLU   B CG    1 
ATOM   11324 C  CD    . GLU   B 1 671 ? 81.677  114.181 126.439 1.00 85.48  ?  671  GLU   B CD    1 
ATOM   11325 O  OE1   . GLU   B 1 671 ? 81.079  114.130 127.535 1.00 84.36  ?  671  GLU   B OE1   1 
ATOM   11326 O  OE2   . GLU   B 1 671 ? 81.701  113.234 125.626 1.00 83.50  ?  671  GLU   B OE2   1 
ATOM   11327 N  N     . MET   B 1 672 ? 83.800  119.644 128.137 1.00 76.58  ?  672  MET   B N     1 
ATOM   11328 C  CA    . MET   B 1 672 ? 83.725  120.642 129.223 1.00 78.38  ?  672  MET   B CA    1 
ATOM   11329 C  C     . MET   B 1 672 ? 83.483  122.014 128.600 1.00 81.95  ?  672  MET   B C     1 
ATOM   11330 O  O     . MET   B 1 672 ? 84.318  122.421 127.781 1.00 88.94  ?  672  MET   B O     1 
ATOM   11331 C  CB    . MET   B 1 672 ? 85.038  120.670 130.007 1.00 79.98  ?  672  MET   B CB    1 
ATOM   11332 C  CG    . MET   B 1 672 ? 85.500  119.314 130.486 1.00 82.20  ?  672  MET   B CG    1 
ATOM   11333 S  SD    . MET   B 1 672 ? 84.883  118.925 132.130 1.00 91.11  ?  672  MET   B SD    1 
ATOM   11334 C  CE    . MET   B 1 672 ? 86.369  119.266 133.080 1.00 82.06  ?  672  MET   B CE    1 
ATOM   11335 N  N     . PRO   B 1 673 ? 82.373  122.726 128.878 1.00 75.14  ?  673  PRO   B N     1 
ATOM   11336 C  CA    . PRO   B 1 673 ? 82.206  124.077 128.384 1.00 72.50  ?  673  PRO   B CA    1 
ATOM   11337 C  C     . PRO   B 1 673 ? 83.533  124.819 128.354 1.00 77.58  ?  673  PRO   B C     1 
ATOM   11338 O  O     . PRO   B 1 673 ? 83.886  125.252 127.265 1.00 83.50  ?  673  PRO   B O     1 
ATOM   11339 C  CB    . PRO   B 1 673 ? 81.203  124.651 129.382 1.00 75.92  ?  673  PRO   B CB    1 
ATOM   11340 C  CG    . PRO   B 1 673 ? 80.909  123.514 130.337 1.00 75.42  ?  673  PRO   B CG    1 
ATOM   11341 C  CD    . PRO   B 1 673 ? 81.168  122.281 129.512 1.00 76.51  ?  673  PRO   B CD    1 
ATOM   11342 N  N     . GLY   B 1 674 ? 84.256  124.920 129.474 1.00 77.80  ?  674  GLY   B N     1 
ATOM   11343 C  CA    . GLY   B 1 674 ? 85.557  125.619 129.549 1.00 72.97  ?  674  GLY   B CA    1 
ATOM   11344 C  C     . GLY   B 1 674 ? 86.383  125.192 130.743 1.00 76.38  ?  674  GLY   B C     1 
ATOM   11345 O  O     . GLY   B 1 674 ? 86.455  123.975 130.957 1.00 80.52  ?  674  GLY   B O     1 
ATOM   11346 N  N     . ASN   B 1 675 ? 86.989  126.126 131.495 1.00 79.27  ?  675  ASN   B N     1 
ATOM   11347 C  CA    . ASN   B 1 675 ? 87.900  125.807 132.585 1.00 75.30  ?  675  ASN   B CA    1 
ATOM   11348 C  C     . ASN   B 1 675 ? 87.436  126.338 133.934 1.00 79.27  ?  675  ASN   B C     1 
ATOM   11349 O  O     . ASN   B 1 675 ? 88.120  126.108 134.937 1.00 83.58  ?  675  ASN   B O     1 
ATOM   11350 C  CB    . ASN   B 1 675 ? 89.304  126.358 132.290 1.00 71.44  ?  675  ASN   B CB    1 
ATOM   11351 C  CG    . ASN   B 1 675 ? 90.126  125.426 131.426 1.00 77.56  ?  675  ASN   B CG    1 
ATOM   11352 O  OD1   . ASN   B 1 675 ? 90.487  124.327 131.845 1.00 82.06  ?  675  ASN   B OD1   1 
ATOM   11353 N  ND2   . ASN   B 1 675 ? 90.391  125.844 130.196 1.00 78.63  ?  675  ASN   B ND2   1 
ATOM   11354 N  N     . ASP   B 1 676 ? 86.300  127.038 133.991 1.00 93.97  ?  676  ASP   B N     1 
ATOM   11355 C  CA    . ASP   B 1 676 ? 85.896  127.708 135.225 1.00 93.87  ?  676  ASP   B CA    1 
ATOM   11356 C  C     . ASP   B 1 676 ? 85.588  126.707 136.333 1.00 93.61  ?  676  ASP   B C     1 
ATOM   11357 O  O     . ASP   B 1 676 ? 86.076  126.846 137.460 1.00 95.11  ?  676  ASP   B O     1 
ATOM   11358 C  CB    . ASP   B 1 676 ? 84.685  128.605 134.960 1.00 95.92  ?  676  ASP   B CB    1 
ATOM   11359 C  CG    . ASP   B 1 676 ? 84.655  129.824 135.862 1.00 101.97 ?  676  ASP   B CG    1 
ATOM   11360 O  OD1   . ASP   B 1 676 ? 85.032  129.703 137.047 1.00 99.66  ?  676  ASP   B OD1   1 
ATOM   11361 O  OD2   . ASP   B 1 676 ? 84.283  130.913 135.379 1.00 102.41 ?  676  ASP   B OD2   1 
ATOM   11362 N  N     . GLY   B 1 677 ? 84.774  125.693 136.034 1.00 70.53  ?  677  GLY   B N     1 
ATOM   11363 C  CA    . GLY   B 1 677 ? 84.407  124.729 137.060 1.00 65.85  ?  677  GLY   B CA    1 
ATOM   11364 C  C     . GLY   B 1 677 ? 85.590  123.919 137.553 1.00 71.64  ?  677  GLY   B C     1 
ATOM   11365 O  O     . GLY   B 1 677 ? 85.729  123.671 138.756 1.00 79.57  ?  677  GLY   B O     1 
ATOM   11366 N  N     . TYR   B 1 678 ? 86.459  123.497 136.634 1.00 70.94  ?  678  TYR   B N     1 
ATOM   11367 C  CA    . TYR   B 1 678 ? 87.647  122.748 137.025 1.00 64.59  ?  678  TYR   B CA    1 
ATOM   11368 C  C     . TYR   B 1 678 ? 88.562  123.591 137.904 1.00 67.24  ?  678  TYR   B C     1 
ATOM   11369 O  O     . TYR   B 1 678 ? 89.103  123.099 138.901 1.00 75.05  ?  678  TYR   B O     1 
ATOM   11370 C  CB    . TYR   B 1 678 ? 88.388  122.259 135.780 1.00 63.06  ?  678  TYR   B CB    1 
ATOM   11371 C  CG    . TYR   B 1 678 ? 89.635  121.463 136.077 1.00 68.24  ?  678  TYR   B CG    1 
ATOM   11372 C  CD1   . TYR   B 1 678 ? 89.565  120.108 136.363 1.00 66.81  ?  678  TYR   B CD1   1 
ATOM   11373 C  CD2   . TYR   B 1 678 ? 90.884  122.066 136.070 1.00 69.74  ?  678  TYR   B CD2   1 
ATOM   11374 C  CE1   . TYR   B 1 678 ? 90.703  119.377 136.636 1.00 65.69  ?  678  TYR   B CE1   1 
ATOM   11375 C  CE2   . TYR   B 1 678 ? 92.025  121.343 136.345 1.00 69.47  ?  678  TYR   B CE2   1 
ATOM   11376 C  CZ    . TYR   B 1 678 ? 91.931  119.998 136.618 1.00 71.36  ?  678  TYR   B CZ    1 
ATOM   11377 O  OH    . TYR   B 1 678 ? 93.069  119.280 136.899 1.00 81.62  ?  678  TYR   B OH    1 
ATOM   11378 N  N     . LEU   B 1 679 ? 88.740  124.867 137.558 1.00 60.35  ?  679  LEU   B N     1 
ATOM   11379 C  CA    . LEU   B 1 679 ? 89.585  125.740 138.367 1.00 62.74  ?  679  LEU   B CA    1 
ATOM   11380 C  C     . LEU   B 1 679 ? 88.967  125.999 139.736 1.00 62.94  ?  679  LEU   B C     1 
ATOM   11381 O  O     . LEU   B 1 679 ? 89.685  126.102 140.736 1.00 65.72  ?  679  LEU   B O     1 
ATOM   11382 C  CB    . LEU   B 1 679 ? 89.844  127.052 137.630 1.00 61.24  ?  679  LEU   B CB    1 
ATOM   11383 C  CG    . LEU   B 1 679 ? 90.859  126.965 136.488 1.00 57.02  ?  679  LEU   B CG    1 
ATOM   11384 C  CD1   . LEU   B 1 679 ? 91.002  128.305 135.790 1.00 64.01  ?  679  LEU   B CD1   1 
ATOM   11385 C  CD2   . LEU   B 1 679 ? 92.203  126.472 136.999 1.00 55.37  ?  679  LEU   B CD2   1 
ATOM   11386 N  N     . GLN   B 1 680 ? 87.638  126.113 139.804 1.00 62.27  ?  680  GLN   B N     1 
ATOM   11387 C  CA    . GLN   B 1 680 ? 86.980  126.259 141.099 1.00 56.84  ?  680  GLN   B CA    1 
ATOM   11388 C  C     . GLN   B 1 680 ? 87.193  125.023 141.965 1.00 63.30  ?  680  GLN   B C     1 
ATOM   11389 O  O     . GLN   B 1 680 ? 87.476  125.134 143.166 1.00 70.83  ?  680  GLN   B O     1 
ATOM   11390 C  CB    . GLN   B 1 680 ? 85.489  126.527 140.903 1.00 58.81  ?  680  GLN   B CB    1 
ATOM   11391 C  CG    . GLN   B 1 680 ? 85.157  127.974 140.589 1.00 61.23  ?  680  GLN   B CG    1 
ATOM   11392 C  CD    . GLN   B 1 680 ? 83.707  128.167 140.199 1.00 69.24  ?  680  GLN   B CD    1 
ATOM   11393 O  OE1   . GLN   B 1 680 ? 82.928  127.217 140.172 1.00 72.83  ?  680  GLN   B OE1   1 
ATOM   11394 N  NE2   . GLN   B 1 680 ? 83.338  129.404 139.892 1.00 70.13  ?  680  GLN   B NE2   1 
ATOM   11395 N  N     . LEU   B 1 681 ? 87.068  123.835 141.369 1.00 57.47  ?  681  LEU   B N     1 
ATOM   11396 C  CA    . LEU   B 1 681 ? 87.340  122.607 142.110 1.00 51.36  ?  681  LEU   B CA    1 
ATOM   11397 C  C     . LEU   B 1 681 ? 88.789  122.562 142.583 1.00 62.15  ?  681  LEU   B C     1 
ATOM   11398 O  O     . LEU   B 1 681 ? 89.069  122.146 143.712 1.00 70.84  ?  681  LEU   B O     1 
ATOM   11399 C  CB    . LEU   B 1 681 ? 87.018  121.389 141.245 1.00 51.09  ?  681  LEU   B CB    1 
ATOM   11400 C  CG    . LEU   B 1 681 ? 85.537  121.099 140.998 1.00 56.67  ?  681  LEU   B CG    1 
ATOM   11401 C  CD1   . LEU   B 1 681 ? 85.356  119.727 140.375 1.00 56.15  ?  681  LEU   B CD1   1 
ATOM   11402 C  CD2   . LEU   B 1 681 ? 84.746  121.212 142.290 1.00 57.95  ?  681  LEU   B CD2   1 
ATOM   11403 N  N     . VAL   B 1 682 ? 89.721  122.995 141.731 1.00 59.18  ?  682  VAL   B N     1 
ATOM   11404 C  CA    . VAL   B 1 682 ? 91.134  122.992 142.099 1.00 53.34  ?  682  VAL   B CA    1 
ATOM   11405 C  C     . VAL   B 1 682 ? 91.389  123.946 143.259 1.00 62.53  ?  682  VAL   B C     1 
ATOM   11406 O  O     . VAL   B 1 682 ? 92.153  123.636 144.178 1.00 71.29  ?  682  VAL   B O     1 
ATOM   11407 C  CB    . VAL   B 1 682 ? 92.005  123.332 140.875 1.00 47.93  ?  682  VAL   B CB    1 
ATOM   11408 C  CG1   . VAL   B 1 682 ? 93.420  123.680 141.302 1.00 49.68  ?  682  VAL   B CG1   1 
ATOM   11409 C  CG2   . VAL   B 1 682 ? 92.018  122.166 139.901 1.00 47.89  ?  682  VAL   B CG2   1 
ATOM   11410 N  N     . GLY   B 1 683 ? 90.760  125.122 143.235 1.00 54.40  ?  683  GLY   B N     1 
ATOM   11411 C  CA    . GLY   B 1 683 ? 90.899  126.044 144.352 1.00 45.40  ?  683  GLY   B CA    1 
ATOM   11412 C  C     . GLY   B 1 683 ? 90.328  125.488 145.643 1.00 53.91  ?  683  GLY   B C     1 
ATOM   11413 O  O     . GLY   B 1 683 ? 90.920  125.643 146.718 1.00 68.54  ?  683  GLY   B O     1 
ATOM   11414 N  N     . ILE   B 1 684 ? 89.171  124.828 145.557 1.00 48.46  ?  684  ILE   B N     1 
ATOM   11415 C  CA    . ILE   B 1 684 ? 88.584  124.211 146.743 1.00 50.05  ?  684  ILE   B CA    1 
ATOM   11416 C  C     . ILE   B 1 684 ? 89.515  123.144 147.305 1.00 55.70  ?  684  ILE   B C     1 
ATOM   11417 O  O     . ILE   B 1 684 ? 89.681  123.023 148.525 1.00 63.31  ?  684  ILE   B O     1 
ATOM   11418 C  CB    . ILE   B 1 684 ? 87.191  123.643 146.417 1.00 55.94  ?  684  ILE   B CB    1 
ATOM   11419 C  CG1   . ILE   B 1 684 ? 86.206  124.782 146.158 1.00 52.89  ?  684  ILE   B CG1   1 
ATOM   11420 C  CG2   . ILE   B 1 684 ? 86.689  122.774 147.550 1.00 55.46  ?  684  ILE   B CG2   1 
ATOM   11421 C  CD1   . ILE   B 1 684 ? 85.049  124.389 145.283 1.00 57.25  ?  684  ILE   B CD1   1 
ATOM   11422 N  N     . MET   B 1 685 ? 90.140  122.355 146.427 1.00 56.54  ?  685  MET   B N     1 
ATOM   11423 C  CA    . MET   B 1 685 ? 91.141  121.393 146.881 1.00 50.84  ?  685  MET   B CA    1 
ATOM   11424 C  C     . MET   B 1 685 ? 92.316  122.098 147.549 1.00 56.35  ?  685  MET   B C     1 
ATOM   11425 O  O     . MET   B 1 685 ? 92.768  121.694 148.626 1.00 65.57  ?  685  MET   B O     1 
ATOM   11426 C  CB    . MET   B 1 685 ? 91.636  120.551 145.706 1.00 51.57  ?  685  MET   B CB    1 
ATOM   11427 C  CG    . MET   B 1 685 ? 90.558  119.918 144.863 1.00 53.30  ?  685  MET   B CG    1 
ATOM   11428 S  SD    . MET   B 1 685 ? 91.261  119.095 143.420 1.00 73.14  ?  685  MET   B SD    1 
ATOM   11429 C  CE    . MET   B 1 685 ? 89.998  117.870 143.131 1.00 62.88  ?  685  MET   B CE    1 
ATOM   11430 N  N     . GLN   B 1 686 ? 92.820  123.161 146.919 1.00 50.29  ?  686  GLN   B N     1 
ATOM   11431 C  CA    . GLN   B 1 686 ? 93.979  123.879 147.435 1.00 49.92  ?  686  GLN   B CA    1 
ATOM   11432 C  C     . GLN   B 1 686 ? 93.704  124.517 148.787 1.00 57.97  ?  686  GLN   B C     1 
ATOM   11433 O  O     . GLN   B 1 686 ? 94.648  124.794 149.535 1.00 62.11  ?  686  GLN   B O     1 
ATOM   11434 C  CB    . GLN   B 1 686 ? 94.422  124.945 146.430 1.00 48.90  ?  686  GLN   B CB    1 
ATOM   11435 C  CG    . GLN   B 1 686 ? 95.750  125.606 146.755 1.00 50.96  ?  686  GLN   B CG    1 
ATOM   11436 C  CD    . GLN   B 1 686 ? 96.915  124.639 146.695 1.00 63.55  ?  686  GLN   B CD    1 
ATOM   11437 O  OE1   . GLN   B 1 686 ? 97.543  124.473 145.651 1.00 70.70  ?  686  GLN   B OE1   1 
ATOM   11438 N  NE2   . GLN   B 1 686 ? 97.215  124.000 147.819 1.00 59.18  ?  686  GLN   B NE2   1 
ATOM   11439 N  N     . LYS   B 1 687 ? 92.433  124.765 149.109 1.00 59.55  ?  687  LYS   B N     1 
ATOM   11440 C  CA    . LYS   B 1 687 ? 92.100  125.251 150.446 1.00 57.43  ?  687  LYS   B CA    1 
ATOM   11441 C  C     . LYS   B 1 687 ? 92.650  124.326 151.526 1.00 63.65  ?  687  LYS   B C     1 
ATOM   11442 O  O     . LYS   B 1 687 ? 93.107  124.788 152.578 1.00 68.33  ?  687  LYS   B O     1 
ATOM   11443 C  CB    . LYS   B 1 687 ? 90.586  125.395 150.600 1.00 58.00  ?  687  LYS   B CB    1 
ATOM   11444 C  CG    . LYS   B 1 687 ? 90.141  125.607 152.039 1.00 56.69  ?  687  LYS   B CG    1 
ATOM   11445 C  CD    . LYS   B 1 687 ? 88.754  126.214 152.129 1.00 61.47  ?  687  LYS   B CD    1 
ATOM   11446 C  CE    . LYS   B 1 687 ? 88.306  126.316 153.577 1.00 62.80  ?  687  LYS   B CE    1 
ATOM   11447 N  NZ    . LYS   B 1 687 ? 86.831  126.233 153.719 1.00 62.73  ?  687  LYS   B NZ    1 
ATOM   11448 N  N     . PHE   B 1 688 ? 92.631  123.017 151.279 1.00 55.03  ?  688  PHE   B N     1 
ATOM   11449 C  CA    . PHE   B 1 688 ? 93.029  122.033 152.277 1.00 46.24  ?  688  PHE   B CA    1 
ATOM   11450 C  C     . PHE   B 1 688 ? 94.389  121.402 152.029 1.00 52.20  ?  688  PHE   B C     1 
ATOM   11451 O  O     . PHE   B 1 688 ? 95.033  120.971 152.986 1.00 66.86  ?  688  PHE   B O     1 
ATOM   11452 C  CB    . PHE   B 1 688 ? 91.981  120.918 152.365 1.00 51.70  ?  688  PHE   B CB    1 
ATOM   11453 C  CG    . PHE   B 1 688 ? 90.649  121.379 152.875 1.00 54.65  ?  688  PHE   B CG    1 
ATOM   11454 C  CD1   . PHE   B 1 688 ? 90.438  121.562 154.230 1.00 53.64  ?  688  PHE   B CD1   1 
ATOM   11455 C  CD2   . PHE   B 1 688 ? 89.608  121.633 152.000 1.00 55.02  ?  688  PHE   B CD2   1 
ATOM   11456 C  CE1   . PHE   B 1 688 ? 89.216  121.995 154.701 1.00 57.79  ?  688  PHE   B CE1   1 
ATOM   11457 C  CE2   . PHE   B 1 688 ? 88.384  122.066 152.466 1.00 60.86  ?  688  PHE   B CE2   1 
ATOM   11458 C  CZ    . PHE   B 1 688 ? 88.180  122.220 153.819 1.00 57.76  ?  688  PHE   B CZ    1 
ATOM   11459 N  N     . ILE   B 1 689 ? 94.845  121.332 150.779 1.00 48.60  ?  689  ILE   B N     1 
ATOM   11460 C  CA    . ILE   B 1 689 ? 96.088  120.634 150.478 1.00 51.55  ?  689  ILE   B CA    1 
ATOM   11461 C  C     . ILE   B 1 689 ? 97.276  121.471 150.932 1.00 57.86  ?  689  ILE   B C     1 
ATOM   11462 O  O     . ILE   B 1 689 ? 97.329  122.687 150.707 1.00 70.06  ?  689  ILE   B O     1 
ATOM   11463 C  CB    . ILE   B 1 689 ? 96.170  120.305 148.978 1.00 54.46  ?  689  ILE   B CB    1 
ATOM   11464 C  CG1   . ILE   B 1 689 ? 94.996  119.416 148.567 1.00 53.99  ?  689  ILE   B CG1   1 
ATOM   11465 C  CG2   . ILE   B 1 689 ? 97.484  119.616 148.650 1.00 53.65  ?  689  ILE   B CG2   1 
ATOM   11466 C  CD1   . ILE   B 1 689 ? 95.152  117.966 148.967 1.00 51.98  ?  689  ILE   B CD1   1 
ATOM   11467 N  N     . ASP   B 1 690 ? 98.238  120.814 151.589 1.00 65.71  ?  690  ASP   B N     1 
ATOM   11468 C  CA    . ASP   B 1 690 ? 99.426  121.508 152.080 1.00 63.94  ?  690  ASP   B CA    1 
ATOM   11469 C  C     . ASP   B 1 690 ? 100.290 122.020 150.936 1.00 67.21  ?  690  ASP   B C     1 
ATOM   11470 O  O     . ASP   B 1 690 ? 100.870 123.107 151.029 1.00 76.88  ?  690  ASP   B O     1 
ATOM   11471 C  CB    . ASP   B 1 690 ? 100.246 120.585 152.981 1.00 66.10  ?  690  ASP   B CB    1 
ATOM   11472 C  CG    . ASP   B 1 690 ? 99.604  120.373 154.334 1.00 80.84  ?  690  ASP   B CG    1 
ATOM   11473 O  OD1   . ASP   B 1 690 ? 99.044  121.339 154.892 1.00 87.04  ?  690  ASP   B OD1   1 
ATOM   11474 O  OD2   . ASP   B 1 690 ? 99.597  119.222 154.812 1.00 79.67  ?  690  ASP   B OD2   1 
ATOM   11475 N  N     . GLN   B 1 691 ? 100.401 121.251 149.859 1.00 57.15  ?  691  GLN   B N     1 
ATOM   11476 C  CA    . GLN   B 1 691 ? 101.251 121.575 148.725 1.00 58.97  ?  691  GLN   B CA    1 
ATOM   11477 C  C     . GLN   B 1 691 ? 100.390 121.917 147.509 1.00 60.30  ?  691  GLN   B C     1 
ATOM   11478 O  O     . GLN   B 1 691 ? 99.169  122.071 147.610 1.00 66.45  ?  691  GLN   B O     1 
ATOM   11479 C  CB    . GLN   B 1 691 ? 102.214 120.419 148.453 1.00 60.82  ?  691  GLN   B CB    1 
ATOM   11480 C  CG    . GLN   B 1 691 ? 103.417 120.406 149.381 1.00 58.62  ?  691  GLN   B CG    1 
ATOM   11481 C  CD    . GLN   B 1 691 ? 104.070 119.046 149.478 1.00 67.31  ?  691  GLN   B CD    1 
ATOM   11482 O  OE1   . GLN   B 1 691 ? 105.199 118.855 149.029 1.00 69.62  ?  691  GLN   B OE1   1 
ATOM   11483 N  NE2   . GLN   B 1 691 ? 103.363 118.091 150.068 1.00 63.72  ?  691  GLN   B NE2   1 
ATOM   11484 N  N     . SER   B 1 692 ? 101.013 121.991 146.356 1.00 60.99  ?  692  SER   B N     1 
ATOM   11485 C  CA    . SER   B 1 692 ? 100.223 122.439 145.197 1.00 56.54  ?  692  SER   B CA    1 
ATOM   11486 C  C     . SER   B 1 692 ? 99.402  121.317 144.594 1.00 59.01  ?  692  SER   B C     1 
ATOM   11487 O  O     . SER   B 1 692 ? 99.302  120.228 145.168 1.00 61.95  ?  692  SER   B O     1 
ATOM   11488 C  CB    . SER   B 1 692 ? 101.112 123.022 144.144 1.00 60.94  ?  692  SER   B CB    1 
ATOM   11489 O  OG    . SER   B 1 692 ? 100.379 123.902 143.312 1.00 66.58  ?  692  SER   B OG    1 
ATOM   11490 N  N     . ILE   B 1 693 ? 98.854  121.631 143.443 1.00 56.99  ?  693  ILE   B N     1 
ATOM   11491 C  CA    . ILE   B 1 693 ? 98.042  120.670 142.707 1.00 56.50  ?  693  ILE   B CA    1 
ATOM   11492 C  C     . ILE   B 1 693 ? 98.451  120.730 141.243 1.00 58.55  ?  693  ILE   B C     1 
ATOM   11493 O  O     . ILE   B 1 693 ? 98.607  121.821 140.684 1.00 67.81  ?  693  ILE   B O     1 
ATOM   11494 C  CB    . ILE   B 1 693 ? 96.535  120.958 142.856 1.00 56.77  ?  693  ILE   B CB    1 
ATOM   11495 C  CG1   . ILE   B 1 693 ? 96.114  120.885 144.323 1.00 49.84  ?  693  ILE   B CG1   1 
ATOM   11496 C  CG2   . ILE   B 1 693 ? 95.715  119.994 142.013 1.00 51.58  ?  693  ILE   B CG2   1 
ATOM   11497 C  CD1   . ILE   B 1 693 ? 94.911  121.728 144.644 1.00 51.32  ?  693  ILE   B CD1   1 
ATOM   11498 N  N     . SER   B 1 694 ? 98.629  119.563 140.625 1.00 60.48  ?  694  SER   B N     1 
ATOM   11499 C  CA    . SER   B 1 694 ? 98.952  119.481 139.200 1.00 60.39  ?  694  SER   B CA    1 
ATOM   11500 C  C     . SER   B 1 694 ? 97.678  119.757 138.405 1.00 69.32  ?  694  SER   B C     1 
ATOM   11501 O  O     . SER   B 1 694 ? 96.985  118.852 137.933 1.00 74.62  ?  694  SER   B O     1 
ATOM   11502 C  CB    . SER   B 1 694 ? 99.549  118.122 138.861 1.00 57.29  ?  694  SER   B CB    1 
ATOM   11503 O  OG    . SER   B 1 694 ? 100.915 118.059 139.229 1.00 70.29  ?  694  SER   B OG    1 
ATOM   11504 N  N     . ALA   B 1 695 ? 97.371  121.042 138.254 1.00 61.34  ?  695  ALA   B N     1 
ATOM   11505 C  CA    . ALA   B 1 695 ? 96.135  121.490 137.627 1.00 57.41  ?  695  ALA   B CA    1 
ATOM   11506 C  C     . ALA   B 1 695 ? 96.369  121.783 136.151 1.00 62.34  ?  695  ALA   B C     1 
ATOM   11507 O  O     . ALA   B 1 695 ? 97.255  122.569 135.803 1.00 71.50  ?  695  ALA   B O     1 
ATOM   11508 C  CB    . ALA   B 1 695 ? 95.592  122.735 138.329 1.00 57.86  ?  695  ALA   B CB    1 
ATOM   11509 N  N     . ASN   B 1 696 ? 95.563  121.165 135.294 1.00 53.93  ?  696  ASN   B N     1 
ATOM   11510 C  CA    . ASN   B 1 696 ? 95.659  121.343 133.853 1.00 48.62  ?  696  ASN   B CA    1 
ATOM   11511 C  C     . ASN   B 1 696 ? 94.621  122.344 133.364 1.00 56.02  ?  696  ASN   B C     1 
ATOM   11512 O  O     . ASN   B 1 696 ? 93.535  122.471 133.933 1.00 70.84  ?  696  ASN   B O     1 
ATOM   11513 C  CB    . ASN   B 1 696 ? 95.462  120.014 133.119 1.00 51.74  ?  696  ASN   B CB    1 
ATOM   11514 C  CG    . ASN   B 1 696 ? 96.533  118.997 133.449 1.00 57.93  ?  696  ASN   B CG    1 
ATOM   11515 O  OD1   . ASN   B 1 696 ? 97.438  119.262 134.236 1.00 61.33  ?  696  ASN   B OD1   1 
ATOM   11516 N  ND2   . ASN   B 1 696 ? 96.436  117.821 132.843 1.00 63.27  ?  696  ASN   B ND2   1 
ATOM   11517 N  N     . THR   B 1 697 ? 94.970  123.059 132.300 1.00 58.85  ?  697  THR   B N     1 
ATOM   11518 C  CA    . THR   B 1 697 ? 94.031  123.894 131.564 1.00 60.61  ?  697  THR   B CA    1 
ATOM   11519 C  C     . THR   B 1 697 ? 93.872  123.316 130.166 1.00 61.93  ?  697  THR   B C     1 
ATOM   11520 O  O     . THR   B 1 697 ? 94.865  123.018 129.498 1.00 65.62  ?  697  THR   B O     1 
ATOM   11521 C  CB    . THR   B 1 697 ? 94.506  125.347 131.490 1.00 60.07  ?  697  THR   B CB    1 
ATOM   11522 O  OG1   . THR   B 1 697 ? 95.850  125.391 130.995 1.00 68.51  ?  697  THR   B OG1   1 
ATOM   11523 C  CG2   . THR   B 1 697 ? 94.450  125.998 132.863 1.00 58.65  ?  697  THR   B CG2   1 
ATOM   11524 N  N     . ASN   B 1 698 ? 92.629  123.152 129.731 1.00 62.04  ?  698  ASN   B N     1 
ATOM   11525 C  CA    . ASN   B 1 698 ? 92.320  122.480 128.479 1.00 56.42  ?  698  ASN   B CA    1 
ATOM   11526 C  C     . ASN   B 1 698 ? 91.497  123.398 127.593 1.00 59.54  ?  698  ASN   B C     1 
ATOM   11527 O  O     . ASN   B 1 698 ? 90.509  123.983 128.047 1.00 67.68  ?  698  ASN   B O     1 
ATOM   11528 C  CB    . ASN   B 1 698 ? 91.578  121.181 128.757 1.00 57.78  ?  698  ASN   B CB    1 
ATOM   11529 C  CG    . ASN   B 1 698 ? 92.103  120.468 129.978 1.00 65.42  ?  698  ASN   B CG    1 
ATOM   11530 O  OD1   . ASN   B 1 698 ? 93.232  119.984 129.986 1.00 69.29  ?  698  ASN   B OD1   1 
ATOM   11531 N  ND2   . ASN   B 1 698 ? 91.263  120.340 130.995 1.00 73.40  ?  698  ASN   B ND2   1 
ATOM   11532 N  N     . TYR   B 1 699 ? 91.908  123.526 126.334 1.00 59.34  ?  699  TYR   B N     1 
ATOM   11533 C  CA    . TYR   B 1 699 ? 91.235  124.402 125.385 1.00 57.46  ?  699  TYR   B CA    1 
ATOM   11534 C  C     . TYR   B 1 699 ? 91.003  123.666 124.077 1.00 61.32  ?  699  TYR   B C     1 
ATOM   11535 O  O     . TYR   B 1 699 ? 91.911  123.011 123.557 1.00 70.88  ?  699  TYR   B O     1 
ATOM   11536 C  CB    . TYR   B 1 699 ? 92.046  125.675 125.132 1.00 59.85  ?  699  TYR   B CB    1 
ATOM   11537 C  CG    . TYR   B 1 699 ? 92.226  126.525 126.363 1.00 61.39  ?  699  TYR   B CG    1 
ATOM   11538 C  CD1   . TYR   B 1 699 ? 91.262  127.450 126.739 1.00 57.12  ?  699  TYR   B CD1   1 
ATOM   11539 C  CD2   . TYR   B 1 699 ? 93.356  126.399 127.154 1.00 65.15  ?  699  TYR   B CD2   1 
ATOM   11540 C  CE1   . TYR   B 1 699 ? 91.422  128.226 127.866 1.00 57.09  ?  699  TYR   B CE1   1 
ATOM   11541 C  CE2   . TYR   B 1 699 ? 93.524  127.169 128.280 1.00 65.55  ?  699  TYR   B CE2   1 
ATOM   11542 C  CZ    . TYR   B 1 699 ? 92.556  128.081 128.633 1.00 65.22  ?  699  TYR   B CZ    1 
ATOM   11543 O  OH    . TYR   B 1 699 ? 92.726  128.851 129.758 1.00 74.90  ?  699  TYR   B OH    1 
ATOM   11544 N  N     . ASP   B 1 700 ? 89.789  123.776 123.553 1.00 65.21  ?  700  ASP   B N     1 
ATOM   11545 C  CA    . ASP   B 1 700 ? 89.447  123.238 122.243 1.00 61.71  ?  700  ASP   B CA    1 
ATOM   11546 C  C     . ASP   B 1 700 ? 89.105  124.400 121.323 1.00 66.77  ?  700  ASP   B C     1 
ATOM   11547 O  O     . ASP   B 1 700 ? 88.097  125.087 121.552 1.00 72.80  ?  700  ASP   B O     1 
ATOM   11548 C  CB    . ASP   B 1 700 ? 88.275  122.260 122.346 1.00 62.95  ?  700  ASP   B CB    1 
ATOM   11549 C  CG    . ASP   B 1 700 ? 87.592  122.020 121.019 1.00 72.44  ?  700  ASP   B CG    1 
ATOM   11550 O  OD1   . ASP   B 1 700 ? 88.295  121.848 120.002 1.00 74.94  ?  700  ASP   B OD1   1 
ATOM   11551 O  OD2   . ASP   B 1 700 ? 86.345  121.999 120.997 1.00 79.36  ?  700  ASP   B OD2   1 
ATOM   11552 N  N     . PRO   B 1 701 ? 89.904  124.668 120.284 1.00 60.06  ?  701  PRO   B N     1 
ATOM   11553 C  CA    . PRO   B 1 701 ? 89.672  125.869 119.467 1.00 60.16  ?  701  PRO   B CA    1 
ATOM   11554 C  C     . PRO   B 1 701 ? 88.423  125.798 118.603 1.00 63.12  ?  701  PRO   B C     1 
ATOM   11555 O  O     . PRO   B 1 701 ? 88.021  126.830 118.052 1.00 68.55  ?  701  PRO   B O     1 
ATOM   11556 C  CB    . PRO   B 1 701 ? 90.940  125.962 118.603 1.00 53.96  ?  701  PRO   B CB    1 
ATOM   11557 C  CG    . PRO   B 1 701 ? 91.886  124.913 119.149 1.00 59.11  ?  701  PRO   B CG    1 
ATOM   11558 C  CD    . PRO   B 1 701 ? 91.020  123.869 119.763 1.00 57.28  ?  701  PRO   B CD    1 
ATOM   11559 N  N     . SER   B 1 702 ? 87.798  124.629 118.462 1.00 68.85  ?  702  SER   B N     1 
ATOM   11560 C  CA    . SER   B 1 702 ? 86.552  124.537 117.712 1.00 66.16  ?  702  SER   B CA    1 
ATOM   11561 C  C     . SER   B 1 702 ? 85.347  125.006 118.514 1.00 66.42  ?  702  SER   B C     1 
ATOM   11562 O  O     . SER   B 1 702 ? 84.253  125.114 117.949 1.00 72.99  ?  702  SER   B O     1 
ATOM   11563 C  CB    . SER   B 1 702 ? 86.321  123.101 117.233 1.00 66.69  ?  702  SER   B CB    1 
ATOM   11564 O  OG    . SER   B 1 702 ? 86.244  122.205 118.326 1.00 73.16  ?  702  SER   B OG    1 
ATOM   11565 N  N     . ARG   B 1 703 ? 85.517  125.283 119.804 1.00 66.35  ?  703  ARG   B N     1 
ATOM   11566 C  CA    . ARG   B 1 703 ? 84.444  125.792 120.645 1.00 70.06  ?  703  ARG   B CA    1 
ATOM   11567 C  C     . ARG   B 1 703 ? 84.300  127.305 120.567 1.00 76.86  ?  703  ARG   B C     1 
ATOM   11568 O  O     . ARG   B 1 703 ? 83.409  127.862 121.215 1.00 82.47  ?  703  ARG   B O     1 
ATOM   11569 C  CB    . ARG   B 1 703 ? 84.671  125.375 122.101 1.00 67.66  ?  703  ARG   B CB    1 
ATOM   11570 C  CG    . ARG   B 1 703 ? 84.200  123.970 122.418 1.00 70.39  ?  703  ARG   B CG    1 
ATOM   11571 C  CD    . ARG   B 1 703 ? 84.328  123.667 123.897 1.00 72.71  ?  703  ARG   B CD    1 
ATOM   11572 N  NE    . ARG   B 1 703 ? 83.673  122.413 124.248 1.00 76.98  ?  703  ARG   B NE    1 
ATOM   11573 C  CZ    . ARG   B 1 703 ? 82.388  122.302 124.553 1.00 77.80  ?  703  ARG   B CZ    1 
ATOM   11574 N  NH1   . ARG   B 1 703 ? 81.585  123.353 124.556 1.00 77.87  ?  703  ARG   B NH1   1 
ATOM   11575 N  NH2   . ARG   B 1 703 ? 81.896  121.106 124.862 1.00 73.93  ?  703  ARG   B NH2   1 
ATOM   11576 N  N     . PHE   B 1 704 ? 85.148  127.978 119.798 1.00 74.98  ?  704  PHE   B N     1 
ATOM   11577 C  CA    . PHE   B 1 704 ? 85.093  129.421 119.664 1.00 74.91  ?  704  PHE   B CA    1 
ATOM   11578 C  C     . PHE   B 1 704 ? 84.685  129.812 118.246 1.00 81.35  ?  704  PHE   B C     1 
ATOM   11579 O  O     . PHE   B 1 704 ? 84.993  129.096 117.287 1.00 81.43  ?  704  PHE   B O     1 
ATOM   11580 C  CB    . PHE   B 1 704 ? 86.448  130.049 120.010 1.00 74.12  ?  704  PHE   B CB    1 
ATOM   11581 C  CG    . PHE   B 1 704 ? 86.945  129.685 121.380 1.00 78.19  ?  704  PHE   B CG    1 
ATOM   11582 C  CD1   . PHE   B 1 704 ? 86.526  130.391 122.494 1.00 72.95  ?  704  PHE   B CD1   1 
ATOM   11583 C  CD2   . PHE   B 1 704 ? 87.822  128.628 121.555 1.00 79.28  ?  704  PHE   B CD2   1 
ATOM   11584 C  CE1   . PHE   B 1 704 ? 86.978  130.053 123.756 1.00 70.92  ?  704  PHE   B CE1   1 
ATOM   11585 C  CE2   . PHE   B 1 704 ? 88.277  128.287 122.814 1.00 77.03  ?  704  PHE   B CE2   1 
ATOM   11586 C  CZ    . PHE   B 1 704 ? 87.859  129.003 123.914 1.00 75.61  ?  704  PHE   B CZ    1 
ATOM   11587 N  N     . PRO   B 1 705 ? 83.967  130.930 118.088 1.00 90.87  ?  705  PRO   B N     1 
ATOM   11588 C  CA    . PRO   B 1 705 ? 83.448  131.290 116.754 1.00 89.06  ?  705  PRO   B CA    1 
ATOM   11589 C  C     . PRO   B 1 705 ? 84.503  131.401 115.669 1.00 91.34  ?  705  PRO   B C     1 
ATOM   11590 O  O     . PRO   B 1 705 ? 84.256  130.982 114.531 1.00 89.59  ?  705  PRO   B O     1 
ATOM   11591 C  CB    . PRO   B 1 705 ? 82.771  132.646 117.006 1.00 88.20  ?  705  PRO   B CB    1 
ATOM   11592 C  CG    . PRO   B 1 705 ? 83.246  133.072 118.381 1.00 88.83  ?  705  PRO   B CG    1 
ATOM   11593 C  CD    . PRO   B 1 705 ? 83.406  131.807 119.126 1.00 87.36  ?  705  PRO   B CD    1 
ATOM   11594 N  N     . SER   B 1 706 ? 85.669  131.957 115.980 1.00 85.66  ?  706  SER   B N     1 
ATOM   11595 C  CA    . SER   B 1 706 ? 86.697  132.174 114.971 1.00 81.33  ?  706  SER   B CA    1 
ATOM   11596 C  C     . SER   B 1 706 ? 87.553  130.943 114.715 1.00 81.45  ?  706  SER   B C     1 
ATOM   11597 O  O     . SER   B 1 706 ? 88.420  130.986 113.836 1.00 83.34  ?  706  SER   B O     1 
ATOM   11598 C  CB    . SER   B 1 706 ? 87.596  133.343 115.380 1.00 84.93  ?  706  SER   B CB    1 
ATOM   11599 O  OG    . SER   B 1 706 ? 87.918  133.283 116.758 1.00 88.67  ?  706  SER   B OG    1 
ATOM   11600 N  N     . GLY   B 1 707 ? 87.337  129.856 115.450 1.00 67.92  ?  707  GLY   B N     1 
ATOM   11601 C  CA    . GLY   B 1 707 ? 88.197  128.699 115.343 1.00 64.84  ?  707  GLY   B CA    1 
ATOM   11602 C  C     . GLY   B 1 707 ? 89.524  128.839 116.047 1.00 68.83  ?  707  GLY   B C     1 
ATOM   11603 O  O     . GLY   B 1 707 ? 90.380  127.959 115.907 1.00 70.09  ?  707  GLY   B O     1 
ATOM   11604 N  N     . LYS   B 1 708 ? 89.724  129.919 116.798 1.00 68.09  ?  708  LYS   B N     1 
ATOM   11605 C  CA    . LYS   B 1 708 ? 90.965  130.174 117.511 1.00 62.37  ?  708  LYS   B CA    1 
ATOM   11606 C  C     . LYS   B 1 708 ? 90.654  130.524 118.957 1.00 64.17  ?  708  LYS   B C     1 
ATOM   11607 O  O     . LYS   B 1 708 ? 89.721  131.284 119.233 1.00 69.64  ?  708  LYS   B O     1 
ATOM   11608 C  CB    . LYS   B 1 708 ? 91.758  131.312 116.859 1.00 65.11  ?  708  LYS   B CB    1 
ATOM   11609 C  CG    . LYS   B 1 708 ? 92.227  131.015 115.448 1.00 70.82  ?  708  LYS   B CG    1 
ATOM   11610 C  CD    . LYS   B 1 708 ? 93.189  132.078 114.950 1.00 68.88  ?  708  LYS   B CD    1 
ATOM   11611 C  CE    . LYS   B 1 708 ? 92.456  133.168 114.189 1.00 73.99  ?  708  LYS   B CE    1 
ATOM   11612 N  NZ    . LYS   B 1 708 ? 92.050  134.289 115.080 1.00 76.54  ?  708  LYS   B NZ    1 
ATOM   11613 N  N     . VAL   B 1 709 ? 91.432  129.964 119.873 1.00 66.44  ?  709  VAL   B N     1 
ATOM   11614 C  CA    . VAL   B 1 709 ? 91.289  130.308 121.292 1.00 64.34  ?  709  VAL   B CA    1 
ATOM   11615 C  C     . VAL   B 1 709 ? 91.678  131.769 121.488 1.00 65.06  ?  709  VAL   B C     1 
ATOM   11616 O  O     . VAL   B 1 709 ? 92.757  132.183 121.035 1.00 70.45  ?  709  VAL   B O     1 
ATOM   11617 C  CB    . VAL   B 1 709 ? 92.157  129.388 122.150 1.00 68.25  ?  709  VAL   B CB    1 
ATOM   11618 C  CG1   . VAL   B 1 709 ? 91.858  129.594 123.627 1.00 68.42  ?  709  VAL   B CG1   1 
ATOM   11619 C  CG2   . VAL   B 1 709 ? 91.940  127.936 121.751 1.00 65.64  ?  709  VAL   B CG2   1 
ATOM   11620 N  N     . PRO   B 1 710 ? 90.854  132.586 122.138 1.00 61.23  ?  710  PRO   B N     1 
ATOM   11621 C  CA    . PRO   B 1 710 ? 91.210  133.996 122.306 1.00 64.54  ?  710  PRO   B CA    1 
ATOM   11622 C  C     . PRO   B 1 710 ? 92.192  134.198 123.451 1.00 66.46  ?  710  PRO   B C     1 
ATOM   11623 O  O     . PRO   B 1 710 ? 92.105  133.551 124.497 1.00 68.44  ?  710  PRO   B O     1 
ATOM   11624 C  CB    . PRO   B 1 710 ? 89.863  134.675 122.593 1.00 57.99  ?  710  PRO   B CB    1 
ATOM   11625 C  CG    . PRO   B 1 710 ? 88.856  133.555 122.789 1.00 56.66  ?  710  PRO   B CG    1 
ATOM   11626 C  CD    . PRO   B 1 710 ? 89.595  132.257 122.820 1.00 59.97  ?  710  PRO   B CD    1 
ATOM   11627 N  N     . MET   B 1 711 ? 93.146  135.107 123.229 1.00 70.14  ?  711  MET   B N     1 
ATOM   11628 C  CA    . MET   B 1 711 ? 94.091  135.476 124.278 1.00 67.28  ?  711  MET   B CA    1 
ATOM   11629 C  C     . MET   B 1 711 ? 93.373  136.016 125.505 1.00 69.17  ?  711  MET   B C     1 
ATOM   11630 O  O     . MET   B 1 711 ? 93.845  135.835 126.636 1.00 73.05  ?  711  MET   B O     1 
ATOM   11631 C  CB    . MET   B 1 711 ? 95.077  136.513 123.745 1.00 66.45  ?  711  MET   B CB    1 
ATOM   11632 C  CG    . MET   B 1 711 ? 96.184  136.877 124.710 1.00 65.59  ?  711  MET   B CG    1 
ATOM   11633 S  SD    . MET   B 1 711 ? 97.110  135.465 125.316 1.00 82.98  ?  711  MET   B SD    1 
ATOM   11634 C  CE    . MET   B 1 711 ? 98.091  135.080 123.874 1.00 69.66  ?  711  MET   B CE    1 
ATOM   11635 N  N     . GLN   B 1 712 ? 92.233  136.678 125.298 1.00 73.65  ?  712  GLN   B N     1 
ATOM   11636 C  CA    . GLN   B 1 712 ? 91.440  137.162 126.419 1.00 73.08  ?  712  GLN   B CA    1 
ATOM   11637 C  C     . GLN   B 1 712 ? 90.988  136.011 127.305 1.00 75.60  ?  712  GLN   B C     1 
ATOM   11638 O  O     . GLN   B 1 712 ? 91.034  136.114 128.534 1.00 74.39  ?  712  GLN   B O     1 
ATOM   11639 C  CB    . GLN   B 1 712 ? 90.235  137.949 125.907 1.00 72.97  ?  712  GLN   B CB    1 
ATOM   11640 C  CG    . GLN   B 1 712 ? 89.481  138.693 126.990 1.00 75.92  ?  712  GLN   B CG    1 
ATOM   11641 C  CD    . GLN   B 1 712 ? 90.080  140.051 127.279 1.00 82.12  ?  712  GLN   B CD    1 
ATOM   11642 O  OE1   . GLN   B 1 712 ? 90.984  140.503 126.579 1.00 85.92  ?  712  GLN   B OE1   1 
ATOM   11643 N  NE2   . GLN   B 1 712 ? 89.582  140.709 128.317 1.00 83.33  ?  712  GLN   B NE2   1 
ATOM   11644 N  N     . GLN   B 1 713 ? 90.555  134.903 126.700 1.00 71.73  ?  713  GLN   B N     1 
ATOM   11645 C  CA    . GLN   B 1 713 ? 90.124  133.753 127.488 1.00 65.42  ?  713  GLN   B CA    1 
ATOM   11646 C  C     . GLN   B 1 713 ? 91.280  133.152 128.278 1.00 68.34  ?  713  GLN   B C     1 
ATOM   11647 O  O     . GLN   B 1 713 ? 91.112  132.780 129.444 1.00 74.92  ?  713  GLN   B O     1 
ATOM   11648 C  CB    . GLN   B 1 713 ? 89.489  132.701 126.582 1.00 66.44  ?  713  GLN   B CB    1 
ATOM   11649 C  CG    . GLN   B 1 713 ? 88.714  131.640 127.335 1.00 68.35  ?  713  GLN   B CG    1 
ATOM   11650 C  CD    . GLN   B 1 713 ? 87.722  132.236 128.312 1.00 74.53  ?  713  GLN   B CD    1 
ATOM   11651 O  OE1   . GLN   B 1 713 ? 86.919  133.095 127.951 1.00 78.14  ?  713  GLN   B OE1   1 
ATOM   11652 N  NE2   . GLN   B 1 713 ? 87.774  131.785 129.559 1.00 71.72  ?  713  GLN   B NE2   1 
ATOM   11653 N  N     . LEU   B 1 714 ? 92.460  133.046 127.662 1.00 56.76  ?  714  LEU   B N     1 
ATOM   11654 C  CA    . LEU   B 1 714 ? 93.617  132.498 128.364 1.00 52.38  ?  714  LEU   B CA    1 
ATOM   11655 C  C     . LEU   B 1 714 ? 94.000  133.370 129.553 1.00 61.49  ?  714  LEU   B C     1 
ATOM   11656 O  O     . LEU   B 1 714 ? 94.227  132.868 130.663 1.00 70.56  ?  714  LEU   B O     1 
ATOM   11657 C  CB    . LEU   B 1 714 ? 94.796  132.356 127.399 1.00 55.43  ?  714  LEU   B CB    1 
ATOM   11658 C  CG    . LEU   B 1 714 ? 94.572  131.542 126.123 1.00 54.34  ?  714  LEU   B CG    1 
ATOM   11659 C  CD1   . LEU   B 1 714 ? 95.749  131.694 125.176 1.00 54.88  ?  714  LEU   B CD1   1 
ATOM   11660 C  CD2   . LEU   B 1 714 ? 94.344  130.082 126.454 1.00 54.58  ?  714  LEU   B CD2   1 
ATOM   11661 N  N     . LEU   B 1 715 ? 94.072  134.686 129.339 1.00 61.21  ?  715  LEU   B N     1 
ATOM   11662 C  CA    . LEU   B 1 715 ? 94.420  135.587 130.433 1.00 55.11  ?  715  LEU   B CA    1 
ATOM   11663 C  C     . LEU   B 1 715 ? 93.350  135.579 131.518 1.00 58.12  ?  715  LEU   B C     1 
ATOM   11664 O  O     . LEU   B 1 715 ? 93.669  135.641 132.711 1.00 65.65  ?  715  LEU   B O     1 
ATOM   11665 C  CB    . LEU   B 1 715 ? 94.642  137.000 129.899 1.00 55.65  ?  715  LEU   B CB    1 
ATOM   11666 C  CG    . LEU   B 1 715 ? 95.864  137.166 128.996 1.00 60.62  ?  715  LEU   B CG    1 
ATOM   11667 C  CD1   . LEU   B 1 715 ? 95.940  138.574 128.433 1.00 63.64  ?  715  LEU   B CD1   1 
ATOM   11668 C  CD2   . LEU   B 1 715 ? 97.138  136.815 129.743 1.00 54.77  ?  715  LEU   B CD2   1 
ATOM   11669 N  N     . LYS   B 1 716 ? 92.077  135.497 131.125 1.00 69.26  ?  716  LYS   B N     1 
ATOM   11670 C  CA    . LYS   B 1 716 ? 90.998  135.445 132.103 1.00 70.21  ?  716  LYS   B CA    1 
ATOM   11671 C  C     . LYS   B 1 716 ? 91.074  134.178 132.941 1.00 73.67  ?  716  LYS   B C     1 
ATOM   11672 O  O     . LYS   B 1 716 ? 90.845  134.216 134.152 1.00 79.26  ?  716  LYS   B O     1 
ATOM   11673 C  CB    . LYS   B 1 716 ? 89.646  135.539 131.396 1.00 71.71  ?  716  LYS   B CB    1 
ATOM   11674 C  CG    . LYS   B 1 716 ? 88.532  136.090 132.264 1.00 76.24  ?  716  LYS   B CG    1 
ATOM   11675 C  CD    . LYS   B 1 716 ? 88.373  137.588 132.069 1.00 83.33  ?  716  LYS   B CD    1 
ATOM   11676 C  CE    . LYS   B 1 716 ? 87.968  137.916 130.641 1.00 84.92  ?  716  LYS   B CE    1 
ATOM   11677 N  NZ    . LYS   B 1 716 ? 86.763  137.150 130.218 1.00 84.76  ?  716  LYS   B NZ    1 
ATOM   11678 N  N     . ASP   B 1 717 ? 91.391  133.043 132.314 1.00 73.73  ?  717  ASP   B N     1 
ATOM   11679 C  CA    . ASP   B 1 717 ? 91.530  131.803 133.070 1.00 64.55  ?  717  ASP   B CA    1 
ATOM   11680 C  C     . ASP   B 1 717 ? 92.730  131.859 134.008 1.00 69.32  ?  717  ASP   B C     1 
ATOM   11681 O  O     . ASP   B 1 717 ? 92.663  131.360 135.137 1.00 77.66  ?  717  ASP   B O     1 
ATOM   11682 C  CB    . ASP   B 1 717 ? 91.643  130.616 132.118 1.00 69.18  ?  717  ASP   B CB    1 
ATOM   11683 C  CG    . ASP   B 1 717 ? 90.310  130.234 131.505 1.00 81.82  ?  717  ASP   B CG    1 
ATOM   11684 O  OD1   . ASP   B 1 717 ? 89.290  130.279 132.225 1.00 81.41  ?  717  ASP   B OD1   1 
ATOM   11685 O  OD2   . ASP   B 1 717 ? 90.281  129.887 130.306 1.00 85.61  ?  717  ASP   B OD2   1 
ATOM   11686 N  N     . LEU   B 1 718 ? 93.836  132.461 133.560 1.00 63.79  ?  718  LEU   B N     1 
ATOM   11687 C  CA    . LEU   B 1 718 ? 94.992  132.634 134.438 1.00 57.76  ?  718  LEU   B CA    1 
ATOM   11688 C  C     . LEU   B 1 718 ? 94.634  133.485 135.653 1.00 60.95  ?  718  LEU   B C     1 
ATOM   11689 O  O     . LEU   B 1 718 ? 94.954  133.133 136.798 1.00 67.95  ?  718  LEU   B O     1 
ATOM   11690 C  CB    . LEU   B 1 718 ? 96.149  133.265 133.658 1.00 55.67  ?  718  LEU   B CB    1 
ATOM   11691 C  CG    . LEU   B 1 718 ? 97.506  133.473 134.330 1.00 61.02  ?  718  LEU   B CG    1 
ATOM   11692 C  CD1   . LEU   B 1 718 ? 98.021  132.149 134.841 1.00 64.17  ?  718  LEU   B CD1   1 
ATOM   11693 C  CD2   . LEU   B 1 718 ? 98.460  134.041 133.298 1.00 66.36  ?  718  LEU   B CD2   1 
ATOM   11694 N  N     . LEU   B 1 719 ? 93.945  134.604 135.419 1.00 60.71  ?  719  LEU   B N     1 
ATOM   11695 C  CA    . LEU   B 1 719 ? 93.543  135.477 136.517 1.00 56.31  ?  719  LEU   B CA    1 
ATOM   11696 C  C     . LEU   B 1 719 ? 92.539  134.792 137.435 1.00 62.12  ?  719  LEU   B C     1 
ATOM   11697 O  O     . LEU   B 1 719 ? 92.566  134.998 138.651 1.00 73.72  ?  719  LEU   B O     1 
ATOM   11698 C  CB    . LEU   B 1 719 ? 92.962  136.778 135.966 1.00 62.46  ?  719  LEU   B CB    1 
ATOM   11699 C  CG    . LEU   B 1 719 ? 93.932  137.691 135.217 1.00 64.23  ?  719  LEU   B CG    1 
ATOM   11700 C  CD1   . LEU   B 1 719 ? 93.176  138.583 134.248 1.00 63.10  ?  719  LEU   B CD1   1 
ATOM   11701 C  CD2   . LEU   B 1 719 ? 94.748  138.520 136.191 1.00 69.18  ?  719  LEU   B CD2   1 
ATOM   11702 N  N     . THR   B 1 720 ? 91.634  133.990 136.870 1.00 57.56  ?  720  THR   B N     1 
ATOM   11703 C  CA    . THR   B 1 720 ? 90.667  133.255 137.679 1.00 59.49  ?  720  THR   B CA    1 
ATOM   11704 C  C     . THR   B 1 720 ? 91.359  132.227 138.561 1.00 63.05  ?  720  THR   B C     1 
ATOM   11705 O  O     . THR   B 1 720 ? 91.001  132.060 139.733 1.00 68.22  ?  720  THR   B O     1 
ATOM   11706 C  CB    . THR   B 1 720 ? 89.635  132.580 136.777 1.00 59.01  ?  720  THR   B CB    1 
ATOM   11707 O  OG1   . THR   B 1 720 ? 88.945  133.577 136.012 1.00 69.46  ?  720  THR   B OG1   1 
ATOM   11708 C  CG2   . THR   B 1 720 ? 88.627  131.802 137.607 1.00 59.72  ?  720  THR   B CG2   1 
ATOM   11709 N  N     . ALA   B 1 721 ? 92.354  131.528 138.013 1.00 62.49  ?  721  ALA   B N     1 
ATOM   11710 C  CA    . ALA   B 1 721 ? 93.124  130.590 138.817 1.00 58.11  ?  721  ALA   B CA    1 
ATOM   11711 C  C     . ALA   B 1 721 ? 93.851  131.307 139.943 1.00 61.04  ?  721  ALA   B C     1 
ATOM   11712 O  O     . ALA   B 1 721 ? 93.886  130.816 141.076 1.00 67.70  ?  721  ALA   B O     1 
ATOM   11713 C  CB    . ALA   B 1 721 ? 94.107  129.825 137.935 1.00 59.25  ?  721  ALA   B CB    1 
ATOM   11714 N  N     . TYR   B 1 722 ? 94.417  132.484 139.662 1.00 66.91  ?  722  TYR   B N     1 
ATOM   11715 C  CA    . TYR   B 1 722 ? 95.043  133.253 140.733 1.00 66.47  ?  722  TYR   B CA    1 
ATOM   11716 C  C     . TYR   B 1 722 ? 94.021  133.679 141.783 1.00 65.69  ?  722  TYR   B C     1 
ATOM   11717 O  O     . TYR   B 1 722 ? 94.312  133.664 142.984 1.00 75.03  ?  722  TYR   B O     1 
ATOM   11718 C  CB    . TYR   B 1 722 ? 95.766  134.476 140.173 1.00 64.77  ?  722  TYR   B CB    1 
ATOM   11719 C  CG    . TYR   B 1 722 ? 96.441  135.277 141.260 1.00 70.15  ?  722  TYR   B CG    1 
ATOM   11720 C  CD1   . TYR   B 1 722 ? 97.720  134.957 141.689 1.00 67.98  ?  722  TYR   B CD1   1 
ATOM   11721 C  CD2   . TYR   B 1 722 ? 95.789  136.337 141.878 1.00 69.75  ?  722  TYR   B CD2   1 
ATOM   11722 C  CE1   . TYR   B 1 722 ? 98.335  135.675 142.691 1.00 69.24  ?  722  TYR   B CE1   1 
ATOM   11723 C  CE2   . TYR   B 1 722 ? 96.395  137.055 142.884 1.00 66.98  ?  722  TYR   B CE2   1 
ATOM   11724 C  CZ    . TYR   B 1 722 ? 97.674  136.732 143.274 1.00 70.40  ?  722  TYR   B CZ    1 
ATOM   11725 O  OH    . TYR   B 1 722 ? 98.275  137.430 144.291 1.00 77.03  ?  722  TYR   B OH    1 
ATOM   11726 N  N     . LYS   B 1 723 ? 92.822  134.069 141.347 1.00 60.94  ?  723  LYS   B N     1 
ATOM   11727 C  CA    . LYS   B 1 723 ? 91.828  134.625 142.259 1.00 61.47  ?  723  LYS   B CA    1 
ATOM   11728 C  C     . LYS   B 1 723 ? 91.334  133.592 143.264 1.00 68.87  ?  723  LYS   B C     1 
ATOM   11729 O  O     . LYS   B 1 723 ? 91.016  133.944 144.406 1.00 72.68  ?  723  LYS   B O     1 
ATOM   11730 C  CB    . LYS   B 1 723 ? 90.658  135.196 141.457 1.00 61.43  ?  723  LYS   B CB    1 
ATOM   11731 C  CG    . LYS   B 1 723 ? 89.497  135.706 142.290 1.00 64.51  ?  723  LYS   B CG    1 
ATOM   11732 C  CD    . LYS   B 1 723 ? 88.327  136.105 141.408 1.00 67.41  ?  723  LYS   B CD    1 
ATOM   11733 C  CE    . LYS   B 1 723 ? 87.011  136.002 142.155 1.00 72.57  ?  723  LYS   B CE    1 
ATOM   11734 N  NZ    . LYS   B 1 723 ? 86.046  135.122 141.446 1.00 73.15  ?  723  LYS   B NZ    1 
ATOM   11735 N  N     . PHE   B 1 724 ? 91.267  132.324 142.870 1.00 63.04  ?  724  PHE   B N     1 
ATOM   11736 C  CA    . PHE   B 1 724 ? 90.779  131.264 143.739 1.00 59.70  ?  724  PHE   B CA    1 
ATOM   11737 C  C     . PHE   B 1 724 ? 91.891  130.579 144.522 1.00 64.93  ?  724  PHE   B C     1 
ATOM   11738 O  O     . PHE   B 1 724 ? 91.630  129.581 145.199 1.00 72.25  ?  724  PHE   B O     1 
ATOM   11739 C  CB    . PHE   B 1 724 ? 89.999  130.235 142.920 1.00 56.82  ?  724  PHE   B CB    1 
ATOM   11740 C  CG    . PHE   B 1 724 ? 88.651  130.719 142.474 1.00 60.84  ?  724  PHE   B CG    1 
ATOM   11741 C  CD1   . PHE   B 1 724 ? 87.799  131.349 143.365 1.00 64.23  ?  724  PHE   B CD1   1 
ATOM   11742 C  CD2   . PHE   B 1 724 ? 88.238  130.554 141.164 1.00 64.14  ?  724  PHE   B CD2   1 
ATOM   11743 C  CE1   . PHE   B 1 724 ? 86.561  131.804 142.958 1.00 62.50  ?  724  PHE   B CE1   1 
ATOM   11744 C  CE2   . PHE   B 1 724 ? 87.001  131.008 140.753 1.00 69.20  ?  724  PHE   B CE2   1 
ATOM   11745 C  CZ    . PHE   B 1 724 ? 86.156  131.617 141.656 1.00 68.65  ?  724  PHE   B CZ    1 
ATOM   11746 N  N     . GLY   B 1 725 ? 93.117  131.086 144.446 1.00 55.27  ?  725  GLY   B N     1 
ATOM   11747 C  CA    . GLY   B 1 725 ? 94.205  130.547 145.233 1.00 55.58  ?  725  GLY   B CA    1 
ATOM   11748 C  C     . GLY   B 1 725 ? 94.945  129.384 144.618 1.00 60.75  ?  725  GLY   B C     1 
ATOM   11749 O  O     . GLY   B 1 725 ? 95.648  128.670 145.340 1.00 69.67  ?  725  GLY   B O     1 
ATOM   11750 N  N     . VAL   B 1 726 ? 94.810  129.163 143.312 1.00 55.03  ?  726  VAL   B N     1 
ATOM   11751 C  CA    . VAL   B 1 726 ? 95.538  128.085 142.653 1.00 52.91  ?  726  VAL   B CA    1 
ATOM   11752 C  C     . VAL   B 1 726 ? 97.019  128.437 142.636 1.00 59.51  ?  726  VAL   B C     1 
ATOM   11753 O  O     . VAL   B 1 726 ? 97.420  129.477 142.101 1.00 68.71  ?  726  VAL   B O     1 
ATOM   11754 C  CB    . VAL   B 1 726 ? 95.004  127.847 141.235 1.00 53.78  ?  726  VAL   B CB    1 
ATOM   11755 C  CG1   . VAL   B 1 726 ? 95.891  126.868 140.490 1.00 56.61  ?  726  VAL   B CG1   1 
ATOM   11756 C  CG2   . VAL   B 1 726 ? 93.570  127.346 141.286 1.00 57.48  ?  726  VAL   B CG2   1 
ATOM   11757 N  N     . LYS   B 1 727 ? 97.840  127.570 143.233 1.00 55.92  ?  727  LYS   B N     1 
ATOM   11758 C  CA    . LYS   B 1 727 ? 99.267  127.857 143.345 1.00 52.26  ?  727  LYS   B CA    1 
ATOM   11759 C  C     . LYS   B 1 727 ? 99.986  127.684 142.015 1.00 53.15  ?  727  LYS   B C     1 
ATOM   11760 O  O     . LYS   B 1 727 ? 100.813 128.522 141.638 1.00 60.66  ?  727  LYS   B O     1 
ATOM   11761 C  CB    . LYS   B 1 727 ? 99.900  126.956 144.403 1.00 55.14  ?  727  LYS   B CB    1 
ATOM   11762 C  CG    . LYS   B 1 727 ? 99.642  127.387 145.829 1.00 52.23  ?  727  LYS   B CG    1 
ATOM   11763 C  CD    . LYS   B 1 727 ? 100.016 126.282 146.797 1.00 53.55  ?  727  LYS   B CD    1 
ATOM   11764 C  CE    . LYS   B 1 727 ? 99.994  126.775 148.224 1.00 59.00  ?  727  LYS   B CE    1 
ATOM   11765 N  NZ    . LYS   B 1 727 ? 99.270  125.843 149.122 1.00 60.36  ?  727  LYS   B NZ    1 
ATOM   11766 N  N     . THR   B 1 728 ? 99.699  126.603 141.296 1.00 55.38  ?  728  THR   B N     1 
ATOM   11767 C  CA    . THR   B 1 728 ? 100.441 126.270 140.093 1.00 59.42  ?  728  THR   B CA    1 
ATOM   11768 C  C     . THR   B 1 728 ? 99.501  125.771 139.007 1.00 59.30  ?  728  THR   B C     1 
ATOM   11769 O  O     . THR   B 1 728 ? 98.428  125.235 139.293 1.00 64.92  ?  728  THR   B O     1 
ATOM   11770 C  CB    . THR   B 1 728 ? 101.512 125.200 140.362 1.00 64.16  ?  728  THR   B CB    1 
ATOM   11771 O  OG1   . THR   B 1 728 ? 100.926 124.058 140.999 1.00 65.48  ?  728  THR   B OG1   1 
ATOM   11772 C  CG2   . THR   B 1 728 ? 102.641 125.738 141.228 1.00 65.03  ?  728  THR   B CG2   1 
ATOM   11773 N  N     . LEU   B 1 729 ? 99.921  125.945 137.755 1.00 53.10  ?  729  LEU   B N     1 
ATOM   11774 C  CA    . LEU   B 1 729 ? 99.211  125.412 136.599 1.00 48.97  ?  729  LEU   B CA    1 
ATOM   11775 C  C     . LEU   B 1 729 ? 100.110 124.433 135.864 1.00 47.69  ?  729  LEU   B C     1 
ATOM   11776 O  O     . LEU   B 1 729 ? 101.244 124.769 135.513 1.00 57.69  ?  729  LEU   B O     1 
ATOM   11777 C  CB    . LEU   B 1 729 ? 98.773  126.517 135.640 1.00 42.61  ?  729  LEU   B CB    1 
ATOM   11778 C  CG    . LEU   B 1 729 ? 97.650  127.421 136.141 1.00 42.07  ?  729  LEU   B CG    1 
ATOM   11779 C  CD1   . LEU   B 1 729 ? 97.439  128.649 135.280 1.00 49.47  ?  729  LEU   B CD1   1 
ATOM   11780 C  CD2   . LEU   B 1 729 ? 96.336  126.685 136.350 1.00 45.19  ?  729  LEU   B CD2   1 
ATOM   11781 N  N     . TYR   B 1 730 ? 99.594  123.237 135.624 1.00 49.36  ?  730  TYR   B N     1 
ATOM   11782 C  CA    . TYR   B 1 730 ? 100.300 122.172 134.926 1.00 49.07  ?  730  TYR   B CA    1 
ATOM   11783 C  C     . TYR   B 1 730 ? 99.998  122.277 133.429 1.00 54.06  ?  730  TYR   B C     1 
ATOM   11784 O  O     . TYR   B 1 730 ? 99.647  123.354 132.938 1.00 65.19  ?  730  TYR   B O     1 
ATOM   11785 C  CB    . TYR   B 1 730 ? 99.928  120.816 135.527 1.00 59.28  ?  730  TYR   B CB    1 
ATOM   11786 C  CG    . TYR   B 1 730 ? 100.989 119.760 135.333 1.00 56.08  ?  730  TYR   B CG    1 
ATOM   11787 C  CD1   . TYR   B 1 730 ? 102.289 120.112 135.007 1.00 51.15  ?  730  TYR   B CD1   1 
ATOM   11788 C  CD2   . TYR   B 1 730 ? 100.689 118.413 135.469 1.00 61.92  ?  730  TYR   B CD2   1 
ATOM   11789 C  CE1   . TYR   B 1 730 ? 103.261 119.153 134.826 1.00 54.99  ?  730  TYR   B CE1   1 
ATOM   11790 C  CE2   . TYR   B 1 730 ? 101.658 117.448 135.303 1.00 58.94  ?  730  TYR   B CE2   1 
ATOM   11791 C  CZ    . TYR   B 1 730 ? 102.938 117.822 134.967 1.00 59.03  ?  730  TYR   B CZ    1 
ATOM   11792 O  OH    . TYR   B 1 730 ? 103.905 116.862 134.782 1.00 62.00  ?  730  TYR   B OH    1 
ATOM   11793 N  N     . TYR   B 1 731 ? 100.182 121.177 132.691 1.00 57.67  ?  731  TYR   B N     1 
ATOM   11794 C  CA    . TYR   B 1 731 ? 100.019 121.137 131.238 1.00 55.37  ?  731  TYR   B CA    1 
ATOM   11795 C  C     . TYR   B 1 731 ? 98.813  121.932 130.765 1.00 57.52  ?  731  TYR   B C     1 
ATOM   11796 O  O     . TYR   B 1 731 ? 97.771  121.966 131.422 1.00 63.82  ?  731  TYR   B O     1 
ATOM   11797 C  CB    . TYR   B 1 731 ? 99.834  119.693 130.757 1.00 51.44  ?  731  TYR   B CB    1 
ATOM   11798 C  CG    . TYR   B 1 731 ? 100.897 118.703 131.143 1.00 62.37  ?  731  TYR   B CG    1 
ATOM   11799 C  CD1   . TYR   B 1 731 ? 102.224 118.902 130.798 1.00 67.24  ?  731  TYR   B CD1   1 
ATOM   11800 C  CD2   . TYR   B 1 731 ? 100.564 117.543 131.821 1.00 59.00  ?  731  TYR   B CD2   1 
ATOM   11801 C  CE1   . TYR   B 1 731 ? 103.191 117.981 131.139 1.00 66.17  ?  731  TYR   B CE1   1 
ATOM   11802 C  CE2   . TYR   B 1 731 ? 101.518 116.626 132.158 1.00 60.95  ?  731  TYR   B CE2   1 
ATOM   11803 C  CZ    . TYR   B 1 731 ? 102.832 116.845 131.825 1.00 68.10  ?  731  TYR   B CZ    1 
ATOM   11804 O  OH    . TYR   B 1 731 ? 103.787 115.918 132.169 1.00 73.01  ?  731  TYR   B OH    1 
ATOM   11805 N  N     . GLN   B 1 732 ? 98.961  122.561 129.604 1.00 55.49  ?  732  GLN   B N     1 
ATOM   11806 C  CA    . GLN   B 1 732 ? 97.827  123.047 128.834 1.00 50.74  ?  732  GLN   B CA    1 
ATOM   11807 C  C     . GLN   B 1 732 ? 97.593  122.080 127.681 1.00 60.84  ?  732  GLN   B C     1 
ATOM   11808 O  O     . GLN   B 1 732 ? 98.454  121.924 126.810 1.00 67.09  ?  732  GLN   B O     1 
ATOM   11809 C  CB    . GLN   B 1 732 ? 98.057  124.464 128.312 1.00 49.30  ?  732  GLN   B CB    1 
ATOM   11810 C  CG    . GLN   B 1 732 ? 96.805  125.079 127.708 1.00 53.89  ?  732  GLN   B CG    1 
ATOM   11811 C  CD    . GLN   B 1 732 ? 97.056  126.417 127.055 1.00 62.21  ?  732  GLN   B CD    1 
ATOM   11812 O  OE1   . GLN   B 1 732 ? 96.961  126.552 125.837 1.00 69.05  ?  732  GLN   B OE1   1 
ATOM   11813 N  NE2   . GLN   B 1 732 ? 97.372  127.421 127.864 1.00 63.14  ?  732  GLN   B NE2   1 
ATOM   11814 N  N     . ASN   B 1 733 ? 96.438  121.432 127.685 1.00 62.47  ?  733  ASN   B N     1 
ATOM   11815 C  CA    . ASN   B 1 733 ? 96.075  120.476 126.651 1.00 57.41  ?  733  ASN   B CA    1 
ATOM   11816 C  C     . ASN   B 1 733 ? 95.211  121.150 125.594 1.00 63.31  ?  733  ASN   B C     1 
ATOM   11817 O  O     . ASN   B 1 733 ? 94.350  121.978 125.909 1.00 71.55  ?  733  ASN   B O     1 
ATOM   11818 C  CB    . ASN   B 1 733 ? 95.343  119.272 127.246 1.00 60.31  ?  733  ASN   B CB    1 
ATOM   11819 C  CG    . ASN   B 1 733 ? 96.032  118.730 128.482 1.00 69.55  ?  733  ASN   B CG    1 
ATOM   11820 O  OD1   . ASN   B 1 733 ? 97.160  118.242 128.418 1.00 75.04  ?  733  ASN   B OD1   1 
ATOM   11821 N  ND2   . ASN   B 1 733 ? 95.365  118.842 129.622 1.00 69.82  ?  733  ASN   B ND2   1 
ATOM   11822 N  N     . THR   B 1 734 ? 95.464  120.799 124.337 1.00 67.77  ?  734  THR   B N     1 
ATOM   11823 C  CA    . THR   B 1 734 ? 94.768  121.372 123.196 1.00 65.14  ?  734  THR   B CA    1 
ATOM   11824 C  C     . THR   B 1 734 ? 94.202  120.255 122.333 1.00 68.52  ?  734  THR   B C     1 
ATOM   11825 O  O     . THR   B 1 734 ? 94.824  119.202 122.173 1.00 78.88  ?  734  THR   B O     1 
ATOM   11826 C  CB    . THR   B 1 734 ? 95.704  122.261 122.363 1.00 69.02  ?  734  THR   B CB    1 
ATOM   11827 O  OG1   . THR   B 1 734 ? 96.279  123.270 123.202 1.00 76.84  ?  734  THR   B OG1   1 
ATOM   11828 C  CG2   . THR   B 1 734 ? 94.948  122.935 121.233 1.00 68.21  ?  734  THR   B CG2   1 
ATOM   11829 N  N     . ARG   B 1 735 ? 93.011  120.491 121.791 1.00 62.62  ?  735  ARG   B N     1 
ATOM   11830 C  CA    . ARG   B 1 735 ? 92.349  119.548 120.895 1.00 56.95  ?  735  ARG   B CA    1 
ATOM   11831 C  C     . ARG   B 1 735 ? 92.710  119.935 119.467 1.00 65.25  ?  735  ARG   B C     1 
ATOM   11832 O  O     . ARG   B 1 735 ? 92.075  120.807 118.869 1.00 74.19  ?  735  ARG   B O     1 
ATOM   11833 C  CB    . ARG   B 1 735 ? 90.844  119.568 121.128 1.00 52.56  ?  735  ARG   B CB    1 
ATOM   11834 C  CG    . ARG   B 1 735 ? 90.110  118.322 120.683 1.00 57.18  ?  735  ARG   B CG    1 
ATOM   11835 C  CD    . ARG   B 1 735 ? 88.614  118.512 120.853 1.00 57.32  ?  735  ARG   B CD    1 
ATOM   11836 N  NE    . ARG   B 1 735 ? 87.846  117.398 120.313 1.00 59.50  ?  735  ARG   B NE    1 
ATOM   11837 C  CZ    . ARG   B 1 735 ? 86.528  117.290 120.399 1.00 64.19  ?  735  ARG   B CZ    1 
ATOM   11838 N  NH1   . ARG   B 1 735 ? 85.801  118.206 121.013 1.00 65.44  ?  735  ARG   B NH1   1 
ATOM   11839 N  NH2   . ARG   B 1 735 ? 85.941  116.178 119.972 1.00 67.39  ?  735  ARG   B NH2   1 
ATOM   11840 N  N     . ASP   B 1 736 ? 93.740  119.286 118.916 1.00 67.67  ?  736  ASP   B N     1 
ATOM   11841 C  CA    . ASP   B 1 736 ? 94.201  119.642 117.578 1.00 68.58  ?  736  ASP   B CA    1 
ATOM   11842 C  C     . ASP   B 1 736 ? 93.173  119.320 116.503 1.00 74.46  ?  736  ASP   B C     1 
ATOM   11843 O  O     . ASP   B 1 736 ? 93.232  119.896 115.412 1.00 78.16  ?  736  ASP   B O     1 
ATOM   11844 C  CB    . ASP   B 1 736 ? 95.540  118.954 117.265 1.00 70.02  ?  736  ASP   B CB    1 
ATOM   11845 C  CG    . ASP   B 1 736 ? 95.436  117.432 117.150 1.00 80.54  ?  736  ASP   B CG    1 
ATOM   11846 O  OD1   . ASP   B 1 736 ? 94.319  116.872 117.069 1.00 88.07  ?  736  ASP   B OD1   1 
ATOM   11847 O  OD2   . ASP   B 1 736 ? 96.506  116.790 117.204 1.00 81.71  ?  736  ASP   B OD2   1 
ATOM   11848 N  N     . GLY   B 1 737 ? 92.236  118.421 116.783 1.00 70.70  ?  737  GLY   B N     1 
ATOM   11849 C  CA    . GLY   B 1 737 ? 91.227  118.070 115.809 1.00 71.16  ?  737  GLY   B CA    1 
ATOM   11850 C  C     . GLY   B 1 737 ? 91.669  117.085 114.753 1.00 77.07  ?  737  GLY   B C     1 
ATOM   11851 O  O     . GLY   B 1 737 ? 90.969  116.930 113.746 1.00 77.32  ?  737  GLY   B O     1 
ATOM   11852 N  N     . ALA   B 1 738 ? 92.834  116.463 114.914 1.00 81.82  ?  738  ALA   B N     1 
ATOM   11853 C  CA    . ALA   B 1 738 ? 93.315  115.495 113.937 1.00 78.73  ?  738  ALA   B CA    1 
ATOM   11854 C  C     . ALA   B 1 738 ? 92.460  114.239 114.003 1.00 80.59  ?  738  ALA   B C     1 
ATOM   11855 O  O     . ALA   B 1 738 ? 92.420  113.562 115.035 1.00 81.71  ?  738  ALA   B O     1 
ATOM   11856 C  CB    . ALA   B 1 738 ? 94.781  115.159 114.197 1.00 77.23  ?  738  ALA   B CB    1 
ATOM   11857 N  N     . GLU   B 1 739 ? 91.768  113.933 112.909 1.00 91.84  ?  739  GLU   B N     1 
ATOM   11858 C  CA    . GLU   B 1 739 ? 90.878  112.777 112.879 1.00 91.72  ?  739  GLU   B CA    1 
ATOM   11859 C  C     . GLU   B 1 739 ? 90.825  112.242 111.456 1.00 94.29  ?  739  GLU   B C     1 
ATOM   11860 O  O     . GLU   B 1 739 ? 90.257  112.886 110.570 1.00 96.53  ?  739  GLU   B O     1 
ATOM   11861 C  CB    . GLU   B 1 739 ? 89.483  113.144 113.376 1.00 94.65  ?  739  GLU   B CB    1 
ATOM   11862 C  CG    . GLU   B 1 739 ? 88.490  111.994 113.333 1.00 96.80  ?  739  GLU   B CG    1 
ATOM   11863 C  CD    . GLU   B 1 739 ? 87.543  111.999 114.519 1.00 101.56 ?  739  GLU   B CD    1 
ATOM   11864 O  OE1   . GLU   B 1 739 ? 87.221  113.098 115.018 1.00 101.85 ?  739  GLU   B OE1   1 
ATOM   11865 O  OE2   . GLU   B 1 739 ? 87.139  110.904 114.963 1.00 100.03 ?  739  GLU   B OE2   1 
ATOM   11866 N  N     . ASP   B 1 740 ? 91.422  111.074 111.242 1.00 89.53  ?  740  ASP   B N     1 
ATOM   11867 C  CA    . ASP   B 1 740 ? 91.262  110.304 110.012 1.00 87.25  ?  740  ASP   B CA    1 
ATOM   11868 C  C     . ASP   B 1 740 ? 90.774  108.930 110.448 1.00 88.55  ?  740  ASP   B C     1 
ATOM   11869 O  O     . ASP   B 1 740 ? 91.554  107.987 110.591 1.00 92.31  ?  740  ASP   B O     1 
ATOM   11870 C  CB    . ASP   B 1 740 ? 92.574  110.232 109.219 1.00 86.89  ?  740  ASP   B CB    1 
ATOM   11871 C  CG    . ASP   B 1 740 ? 92.420  109.493 107.904 1.00 90.08  ?  740  ASP   B CG    1 
ATOM   11872 O  OD1   . ASP   B 1 740 ? 91.711  110.001 107.010 1.00 91.17  ?  740  ASP   B OD1   1 
ATOM   11873 O  OD2   . ASP   B 1 740 ? 92.990  108.391 107.773 1.00 88.33  ?  740  ASP   B OD2   1 
ATOM   11874 N  N     . ALA   B 1 741 ? 89.466  108.823 110.664 1.00 90.71  ?  741  ALA   B N     1 
ATOM   11875 C  CA    . ALA   B 1 741 ? 88.897  107.600 111.208 1.00 90.24  ?  741  ALA   B CA    1 
ATOM   11876 C  C     . ALA   B 1 741 ? 88.888  106.508 110.151 1.00 91.65  ?  741  ALA   B C     1 
ATOM   11877 O  O     . ALA   B 1 741 ? 88.475  106.732 109.009 1.00 88.10  ?  741  ALA   B O     1 
ATOM   11878 C  CB    . ALA   B 1 741 ? 87.481  107.855 111.720 1.00 89.58  ?  741  ALA   B CB    1 
ATOM   11879 N  N     . GLN   B 1 742 ? 89.354  105.323 110.530 1.00 82.98  ?  742  GLN   B N     1 
ATOM   11880 C  CA    . GLN   B 1 742 ? 89.303  104.148 109.668 1.00 77.87  ?  742  GLN   B CA    1 
ATOM   11881 C  C     . GLN   B 1 742 ? 88.542  103.068 110.428 1.00 81.81  ?  742  GLN   B C     1 
ATOM   11882 O  O     . GLN   B 1 742 ? 89.127  102.200 111.079 1.00 80.70  ?  742  GLN   B O     1 
ATOM   11883 C  CB    . GLN   B 1 742 ? 90.710  103.706 109.259 1.00 73.22  ?  742  GLN   B CB    1 
ATOM   11884 C  CG    . GLN   B 1 742 ? 91.471  104.799 108.519 1.00 74.39  ?  742  GLN   B CG    1 
ATOM   11885 C  CD    . GLN   B 1 742 ? 92.819  104.350 108.001 1.00 77.33  ?  742  GLN   B CD    1 
ATOM   11886 O  OE1   . GLN   B 1 742 ? 93.221  103.204 108.187 1.00 79.73  ?  742  GLN   B OE1   1 
ATOM   11887 N  NE2   . GLN   B 1 742 ? 93.559  105.280 107.412 1.00 78.51  ?  742  GLN   B NE2   1 
ATOM   11888 N  N     . ASP   B 1 743 ? 87.219  103.133 110.334 1.00 102.27 ?  743  ASP   B N     1 
ATOM   11889 C  CA    . ASP   B 1 743 ? 86.311  102.129 110.865 1.00 105.27 ?  743  ASP   B CA    1 
ATOM   11890 C  C     . ASP   B 1 743 ? 85.728  101.324 109.708 1.00 106.14 ?  743  ASP   B C     1 
ATOM   11891 O  O     . ASP   B 1 743 ? 86.005  101.590 108.535 1.00 104.18 ?  743  ASP   B O     1 
ATOM   11892 C  CB    . ASP   B 1 743 ? 85.211  102.783 111.702 1.00 103.53 ?  743  ASP   B CB    1 
ATOM   11893 C  CG    . ASP   B 1 743 ? 85.763  103.566 112.879 1.00 105.00 ?  743  ASP   B CG    1 
ATOM   11894 O  OD1   . ASP   B 1 743 ? 86.028  102.952 113.934 1.00 105.08 ?  743  ASP   B OD1   1 
ATOM   11895 O  OD2   . ASP   B 1 743 ? 85.935  104.797 112.750 1.00 104.83 ?  743  ASP   B OD2   1 
ATOM   11896 N  N     . ASP   B 1 744 ? 84.899  100.338 110.045 1.00 124.22 ?  744  ASP   B N     1 
ATOM   11897 C  CA    . ASP   B 1 744 ? 84.400  99.404  109.038 1.00 125.25 ?  744  ASP   B CA    1 
ATOM   11898 C  C     . ASP   B 1 744 ? 83.566  100.150 107.979 1.00 125.59 ?  744  ASP   B C     1 
ATOM   11899 O  O     . ASP   B 1 744 ? 83.158  101.285 108.170 1.00 126.49 ?  744  ASP   B O     1 
ATOM   11900 C  CB    . ASP   B 1 744 ? 83.597  98.287  109.704 1.00 125.41 ?  744  ASP   B CB    1 
ATOM   11901 C  CG    . ASP   B 1 744 ? 82.474  98.810  110.578 1.00 128.06 ?  744  ASP   B CG    1 
ATOM   11902 O  OD1   . ASP   B 1 744 ? 82.363  100.042 110.747 1.00 127.97 ?  744  ASP   B OD1   1 
ATOM   11903 O  OD2   . ASP   B 1 744 ? 81.698  97.981  111.098 1.00 128.29 ?  744  ASP   B OD2   1 
ATOM   11904 N  N     . LEU   B 1 745 ? 83.270  99.523  106.854 1.00 111.82 ?  745  LEU   B N     1 
ATOM   11905 C  CA    . LEU   B 1 745 ? 82.544  100.278 105.813 1.00 111.02 ?  745  LEU   B CA    1 
ATOM   11906 C  C     . LEU   B 1 745 ? 81.039  99.999  105.908 1.00 110.80 ?  745  LEU   B C     1 
ATOM   11907 O  O     . LEU   B 1 745 ? 80.628  99.415  106.927 1.00 110.36 ?  745  LEU   B O     1 
ATOM   11908 C  CB    . LEU   B 1 745 ? 83.093  99.962  104.439 1.00 111.07 ?  745  LEU   B CB    1 
ATOM   11909 C  CG    . LEU   B 1 745 ? 82.774  101.010 103.378 1.00 113.80 ?  745  LEU   B CG    1 
ATOM   11910 C  CD1   . LEU   B 1 745 ? 82.618  102.272 104.201 1.00 111.41 ?  745  LEU   B CD1   1 
ATOM   11911 C  CD2   . LEU   B 1 745 ? 83.877  101.137 102.345 1.00 110.01 ?  745  LEU   B CD2   1 
ATOM   11912 N  N     . ALA   C 2 2   ? 99.517  132.477 76.884  1.00 100.43 ?  1    ALA   C N     1 
ATOM   11913 C  CA    . ALA   C 2 2   ? 100.780 132.421 77.611  1.00 99.28  ?  1    ALA   C CA    1 
ATOM   11914 C  C     . ALA   C 2 2   ? 100.561 132.649 79.100  1.00 100.92 ?  1    ALA   C C     1 
ATOM   11915 O  O     . ALA   C 2 2   ? 99.781  133.515 79.497  1.00 101.93 ?  1    ALA   C O     1 
ATOM   11916 C  CB    . ALA   C 2 2   ? 101.758 133.443 77.055  1.00 98.17  ?  1    ALA   C CB    1 
ATOM   11917 N  N     . TYR   C 2 3   ? 101.250 131.863 79.922  1.00 95.02  ?  2    TYR   C N     1 
ATOM   11918 C  CA    . TYR   C 2 3   ? 101.134 132.009 81.365  1.00 89.82  ?  2    TYR   C CA    1 
ATOM   11919 C  C     . TYR   C 2 3   ? 101.768 133.316 81.823  1.00 91.20  ?  2    TYR   C C     1 
ATOM   11920 O  O     . TYR   C 2 3   ? 102.797 133.746 81.295  1.00 89.52  ?  2    TYR   C O     1 
ATOM   11921 C  CB    . TYR   C 2 3   ? 101.795 130.830 82.077  1.00 84.69  ?  2    TYR   C CB    1 
ATOM   11922 C  CG    . TYR   C 2 3   ? 101.768 130.943 83.583  1.00 87.65  ?  2    TYR   C CG    1 
ATOM   11923 C  CD1   . TYR   C 2 3   ? 100.585 130.778 84.289  1.00 88.46  ?  2    TYR   C CD1   1 
ATOM   11924 C  CD2   . TYR   C 2 3   ? 102.923 131.222 84.299  1.00 88.89  ?  2    TYR   C CD2   1 
ATOM   11925 C  CE1   . TYR   C 2 3   ? 100.555 130.885 85.666  1.00 90.28  ?  2    TYR   C CE1   1 
ATOM   11926 C  CE2   . TYR   C 2 3   ? 102.901 131.331 85.676  1.00 90.75  ?  2    TYR   C CE2   1 
ATOM   11927 C  CZ    . TYR   C 2 3   ? 101.715 131.160 86.354  1.00 91.47  ?  2    TYR   C CZ    1 
ATOM   11928 O  OH    . TYR   C 2 3   ? 101.688 131.267 87.724  1.00 90.51  ?  2    TYR   C OH    1 
ATOM   11929 N  N     . THR   C 2 4   ? 101.144 133.950 82.812  1.00 88.27  ?  3    THR   C N     1 
ATOM   11930 C  CA    . THR   C 2 4   ? 101.659 135.179 83.392  1.00 86.58  ?  3    THR   C CA    1 
ATOM   11931 C  C     . THR   C 2 4   ? 101.541 135.107 84.906  1.00 86.96  ?  3    THR   C C     1 
ATOM   11932 O  O     . THR   C 2 4   ? 100.511 134.683 85.438  1.00 87.70  ?  3    THR   C O     1 
ATOM   11933 C  CB    . THR   C 2 4   ? 100.913 136.412 82.862  1.00 87.30  ?  3    THR   C CB    1 
ATOM   11934 O  OG1   . THR   C 2 4   ? 101.203 137.545 83.690  1.00 89.49  ?  3    THR   C OG1   1 
ATOM   11935 C  CG2   . THR   C 2 4   ? 99.410  136.168 82.848  1.00 86.85  ?  3    THR   C CG2   1 
ATOM   11936 N  N     . THR   C 2 5   ? 102.607 135.517 85.596  1.00 79.73  ?  4    THR   C N     1 
ATOM   11937 C  CA    . THR   C 2 5   ? 102.583 135.526 87.055  1.00 83.75  ?  4    THR   C CA    1 
ATOM   11938 C  C     . THR   C 2 5   ? 101.568 136.531 87.584  1.00 88.18  ?  4    THR   C C     1 
ATOM   11939 O  O     . THR   C 2 5   ? 100.855 136.251 88.555  1.00 88.50  ?  4    THR   C O     1 
ATOM   11940 C  CB    . THR   C 2 5   ? 103.977 135.826 87.604  1.00 86.12  ?  4    THR   C CB    1 
ATOM   11941 O  OG1   . THR   C 2 5   ? 104.601 136.833 86.798  1.00 87.69  ?  4    THR   C OG1   1 
ATOM   11942 C  CG2   . THR   C 2 5   ? 104.833 134.571 87.585  1.00 84.97  ?  4    THR   C CG2   1 
ATOM   11943 N  N     . PHE   C 2 6   ? 101.484 137.703 86.959  1.00 89.08  ?  5    PHE   C N     1 
ATOM   11944 C  CA    . PHE   C 2 6   ? 100.497 138.716 87.308  1.00 85.62  ?  5    PHE   C CA    1 
ATOM   11945 C  C     . PHE   C 2 6   ? 99.714  139.087 86.057  1.00 86.52  ?  5    PHE   C C     1 
ATOM   11946 O  O     . PHE   C 2 6   ? 100.308 139.446 85.037  1.00 90.27  ?  5    PHE   C O     1 
ATOM   11947 C  CB    . PHE   C 2 6   ? 101.167 139.959 87.908  1.00 85.30  ?  5    PHE   C CB    1 
ATOM   11948 C  CG    . PHE   C 2 6   ? 100.228 140.843 88.675  1.00 86.47  ?  5    PHE   C CG    1 
ATOM   11949 C  CD1   . PHE   C 2 6   ? 99.488  141.818 88.031  1.00 88.96  ?  5    PHE   C CD1   1 
ATOM   11950 C  CD2   . PHE   C 2 6   ? 100.091 140.704 90.042  1.00 86.73  ?  5    PHE   C CD2   1 
ATOM   11951 C  CE1   . PHE   C 2 6   ? 98.622  142.631 88.736  1.00 89.73  ?  5    PHE   C CE1   1 
ATOM   11952 C  CE2   . PHE   C 2 6   ? 99.222  141.511 90.754  1.00 84.87  ?  5    PHE   C CE2   1 
ATOM   11953 C  CZ    . PHE   C 2 6   ? 98.489  142.477 90.099  1.00 88.42  ?  5    PHE   C CZ    1 
ATOM   11954 N  N     . SER   C 2 7   ? 98.391  139.007 86.134  1.00 95.36  ?  6    SER   C N     1 
ATOM   11955 C  CA    . SER   C 2 7   ? 97.521  139.302 85.004  1.00 98.64  ?  6    SER   C CA    1 
ATOM   11956 C  C     . SER   C 2 7   ? 96.829  140.637 85.221  1.00 101.79 ?  6    SER   C C     1 
ATOM   11957 O  O     . SER   C 2 7   ? 96.248  140.874 86.286  1.00 105.95 ?  6    SER   C O     1 
ATOM   11958 C  CB    . SER   C 2 7   ? 96.482  138.203 84.819  1.00 97.98  ?  6    SER   C CB    1 
ATOM   11959 O  OG    . SER   C 2 7   ? 95.712  138.037 86.001  1.00 99.92  ?  6    SER   C OG    1 
ATOM   11960 N  N     . GLN   C 2 8   ? 96.997  141.501 84.218  1.00 104.34 ?  7    GLN   C N     1 
ATOM   11961 C  CA    A GLN   C 2 8   ? 96.482  142.895 84.342  0.50 103.94 ?  7    GLN   C CA    1 
ATOM   11962 C  CA    B GLN   C 2 8   ? 96.456  142.872 84.270  0.50 103.94 ?  7    GLN   C CA    1 
ATOM   11963 C  C     . GLN   C 2 8   ? 94.934  143.093 84.127  1.00 104.56 ?  7    GLN   C C     1 
ATOM   11964 O  O     . GLN   C 2 8   ? 94.316  144.205 84.275  1.00 107.55 ?  7    GLN   C O     1 
ATOM   11965 C  CB    A GLN   C 2 8   ? 97.075  143.740 83.212  0.50 104.36 ?  7    GLN   C CB    1 
ATOM   11966 C  CB    B GLN   C 2 8   ? 97.194  143.607 83.160  0.50 104.36 ?  7    GLN   C CB    1 
ATOM   11967 C  CG    A GLN   C 2 8   ? 98.584  143.887 83.273  0.50 105.87 ?  7    GLN   C CG    1 
ATOM   11968 C  CG    B GLN   C 2 8   ? 98.657  143.216 83.055  0.50 105.87 ?  7    GLN   C CG    1 
ATOM   11969 C  CD    A GLN   C 2 8   ? 99.050  144.547 84.556  0.50 107.69 ?  7    GLN   C CD    1 
ATOM   11970 C  CD    B GLN   C 2 8   ? 99.374  144.008 81.991  0.50 107.69 ?  7    GLN   C CD    1 
ATOM   11971 O  OE1   A GLN   C 2 8   ? 98.429  145.492 85.042  0.50 109.11 ?  7    GLN   C OE1   1 
ATOM   11972 O  OE1   B GLN   C 2 8   ? 98.894  145.039 81.528  0.50 109.11 ?  7    GLN   C OE1   1 
ATOM   11973 N  NE2   A GLN   C 2 8   ? 100.151 144.054 85.110  0.50 105.51 ?  7    GLN   C NE2   1 
ATOM   11974 N  NE2   B GLN   C 2 8   ? 100.539 143.525 81.593  0.50 105.51 ?  7    GLN   C NE2   1 
ATOM   11975 N  N     . THR   C 2 9   ? 94.229  141.983 84.009  1.00 97.50  ?  8    THR   C N     1 
ATOM   11976 C  CA    . THR   C 2 9   ? 92.776  142.064 83.941  1.00 98.89  ?  8    THR   C CA    1 
ATOM   11977 C  C     . THR   C 2 9   ? 92.169  141.918 85.330  1.00 99.59  ?  8    THR   C C     1 
ATOM   11978 O  O     . THR   C 2 9   ? 92.470  140.962 86.051  1.00 100.32 ?  8    THR   C O     1 
ATOM   11979 C  CB    . THR   C 2 9   ? 92.221  140.983 83.017  1.00 99.71  ?  8    THR   C CB    1 
ATOM   11980 O  OG1   . THR   C 2 9   ? 92.857  141.067 81.736  1.00 100.95 ?  8    THR   C OG1   1 
ATOM   11981 C  CG2   . THR   C 2 9   ? 90.717  141.149 82.844  1.00 97.85  ?  8    THR   C CG2   1 
ATOM   11982 N  N     . LYS   C 2 10  ? 91.333  142.881 85.716  1.00 106.10 ?  9    LYS   C N     1 
ATOM   11983 C  CA    . LYS   C 2 10  ? 90.650  142.830 87.008  1.00 107.07 ?  9    LYS   C CA    1 
ATOM   11984 C  C     . LYS   C 2 10  ? 89.475  141.873 86.882  1.00 107.83 ?  9    LYS   C C     1 
ATOM   11985 O  O     . LYS   C 2 10  ? 88.373  142.249 86.481  1.00 109.16 ?  9    LYS   C O     1 
ATOM   11986 C  CB    . LYS   C 2 10  ? 90.189  144.214 87.449  1.00 106.10 ?  9    LYS   C CB    1 
ATOM   11987 C  CG    . LYS   C 2 10  ? 89.362  144.188 88.733  1.00 106.13 ?  9    LYS   C CG    1 
ATOM   11988 C  CD    . LYS   C 2 10  ? 88.952  145.577 89.182  1.00 105.73 ?  9    LYS   C CD    1 
ATOM   11989 C  CE    . LYS   C 2 10  ? 87.462  145.807 88.997  1.00 107.35 ?  9    LYS   C CE    1 
ATOM   11990 N  NZ    . LYS   C 2 10  ? 87.087  145.901 87.559  1.00 107.42 ?  9    LYS   C NZ    1 
ATOM   11991 N  N     . ASN   C 2 11  ? 89.717  140.614 87.222  1.00 104.29 ?  10   ASN   C N     1 
ATOM   11992 C  CA    . ASN   C 2 11  ? 88.668  139.611 87.248  1.00 103.14 ?  10   ASN   C CA    1 
ATOM   11993 C  C     . ASN   C 2 11  ? 88.072  139.510 88.647  1.00 104.35 ?  10   ASN   C C     1 
ATOM   11994 O  O     . ASN   C 2 11  ? 88.675  139.928 89.638  1.00 105.17 ?  10   ASN   C O     1 
ATOM   11995 C  CB    . ASN   C 2 11  ? 89.212  138.252 86.812  1.00 103.94 ?  10   ASN   C CB    1 
ATOM   11996 C  CG    . ASN   C 2 11  ? 90.197  137.674 87.809  1.00 104.96 ?  10   ASN   C CG    1 
ATOM   11997 O  OD1   . ASN   C 2 11  ? 90.988  138.400 88.410  1.00 105.83 ?  10   ASN   C OD1   1 
ATOM   11998 N  ND2   . ASN   C 2 11  ? 90.152  136.361 87.992  1.00 104.40 ?  10   ASN   C ND2   1 
ATOM   11999 N  N     . ASP   C 2 12  ? 86.863  138.963 88.715  1.00 106.00 ?  11   ASP   C N     1 
ATOM   12000 C  CA    . ASP   C 2 12  ? 86.227  138.653 89.987  1.00 104.93 ?  11   ASP   C CA    1 
ATOM   12001 C  C     . ASP   C 2 12  ? 86.532  137.199 90.319  1.00 107.86 ?  11   ASP   C C     1 
ATOM   12002 O  O     . ASP   C 2 12  ? 86.148  136.293 89.572  1.00 110.49 ?  11   ASP   C O     1 
ATOM   12003 C  CB    . ASP   C 2 12  ? 84.722  138.902 89.923  1.00 105.38 ?  11   ASP   C CB    1 
ATOM   12004 C  CG    . ASP   C 2 12  ? 83.974  138.259 91.074  1.00 108.31 ?  11   ASP   C CG    1 
ATOM   12005 O  OD1   . ASP   C 2 12  ? 84.583  138.002 92.132  1.00 109.08 ?  11   ASP   C OD1   1 
ATOM   12006 O  OD2   . ASP   C 2 12  ? 82.763  138.032 90.934  1.00 109.84 ?  11   ASP   C OD2   1 
ATOM   12007 N  N     . GLN   C 2 13  ? 87.211  136.980 91.441  1.00 101.56 ?  12   GLN   C N     1 
ATOM   12008 C  CA    . GLN   C 2 13  ? 87.758  135.670 91.762  1.00 100.04 ?  12   GLN   C CA    1 
ATOM   12009 C  C     . GLN   C 2 13  ? 86.751  134.736 92.419  1.00 105.00 ?  12   GLN   C C     1 
ATOM   12010 O  O     . GLN   C 2 13  ? 87.096  133.582 92.693  1.00 107.94 ?  12   GLN   C O     1 
ATOM   12011 C  CB    . GLN   C 2 13  ? 88.983  135.826 92.665  1.00 99.83  ?  12   GLN   C CB    1 
ATOM   12012 C  CG    . GLN   C 2 13  ? 90.097  136.651 92.044  1.00 101.17 ?  12   GLN   C CG    1 
ATOM   12013 C  CD    . GLN   C 2 13  ? 91.204  136.968 93.027  1.00 103.68 ?  12   GLN   C CD    1 
ATOM   12014 O  OE1   . GLN   C 2 13  ? 90.985  137.003 94.237  1.00 108.08 ?  12   GLN   C OE1   1 
ATOM   12015 N  NE2   . GLN   C 2 13  ? 92.403  137.202 92.511  1.00 101.81 ?  12   GLN   C NE2   1 
ATOM   12016 N  N     . LEU   C 2 14  ? 85.531  135.190 92.685  1.00 105.91 ?  13   LEU   C N     1 
ATOM   12017 C  CA    . LEU   C 2 14  ? 84.510  134.325 93.262  1.00 103.63 ?  13   LEU   C CA    1 
ATOM   12018 C  C     . LEU   C 2 14  ? 83.658  133.661 92.198  1.00 103.28 ?  13   LEU   C C     1 
ATOM   12019 O  O     . LEU   C 2 14  ? 82.767  132.869 92.522  1.00 105.48 ?  13   LEU   C O     1 
ATOM   12020 C  CB    . LEU   C 2 14  ? 83.632  135.119 94.229  1.00 102.82 ?  13   LEU   C CB    1 
ATOM   12021 C  CG    . LEU   C 2 14  ? 84.399  135.853 95.334  1.00 103.22 ?  13   LEU   C CG    1 
ATOM   12022 C  CD1   . LEU   C 2 14  ? 83.486  136.787 96.117  1.00 102.61 ?  13   LEU   C CD1   1 
ATOM   12023 C  CD2   . LEU   C 2 14  ? 85.077  134.865 96.268  1.00 103.91 ?  13   LEU   C CD2   1 
ATOM   12024 N  N     . LYS   C 2 15  ? 83.961  133.929 90.945  1.00 102.76 ?  14   LYS   C N     1 
ATOM   12025 C  CA    . LYS   C 2 15  ? 83.234  133.408 89.817  1.00 103.58 ?  14   LYS   C CA    1 
ATOM   12026 C  C     . LYS   C 2 15  ? 84.129  132.662 88.841  1.00 104.53 ?  14   LYS   C C     1 
ATOM   12027 O  O     . LYS   C 2 15  ? 83.629  132.102 87.847  1.00 102.81 ?  14   LYS   C O     1 
ATOM   12028 C  CB    . LYS   C 2 15  ? 82.569  134.572 89.084  1.00 100.14 ?  14   LYS   C CB    1 
ATOM   12029 C  CG    . LYS   C 2 15  ? 81.744  135.558 89.896  1.00 101.77 ?  14   LYS   C CG    1 
ATOM   12030 C  CD    . LYS   C 2 15  ? 80.367  135.894 89.431  1.00 104.38 ?  14   LYS   C CD    1 
ATOM   12031 C  CE    . LYS   C 2 15  ? 79.432  136.126 90.600  1.00 105.00 ?  14   LYS   C CE    1 
ATOM   12032 N  NZ    . LYS   C 2 15  ? 78.991  134.858 91.236  1.00 103.68 ?  14   LYS   C NZ    1 
ATOM   12033 N  N     . GLU   C 2 16  ? 85.446  132.685 89.081  1.00 102.88 ?  15   GLU   C N     1 
ATOM   12034 C  CA    . GLU   C 2 16  ? 86.439  131.990 88.293  1.00 101.58 ?  15   GLU   C CA    1 
ATOM   12035 C  C     . GLU   C 2 16  ? 86.439  130.505 88.643  1.00 102.61 ?  15   GLU   C C     1 
ATOM   12036 O  O     . GLU   C 2 16  ? 86.158  130.126 89.782  1.00 106.90 ?  15   GLU   C O     1 
ATOM   12037 C  CB    . GLU   C 2 16  ? 87.824  132.586 88.535  1.00 98.92  ?  15   GLU   C CB    1 
ATOM   12038 C  CG    . GLU   C 2 16  ? 88.111  133.816 87.687  1.00 101.83 ?  15   GLU   C CG    1 
ATOM   12039 C  CD    . GLU   C 2 16  ? 88.419  133.494 86.242  1.00 105.95 ?  15   GLU   C CD    1 
ATOM   12040 O  OE1   . GLU   C 2 16  ? 88.984  132.416 85.977  1.00 105.34 ?  15   GLU   C OE1   1 
ATOM   12041 O  OE2   . GLU   C 2 16  ? 88.097  134.330 85.372  1.00 107.27 ?  15   GLU   C OE2   1 
ATOM   12042 N  N     . PRO   C 2 17  ? 86.735  129.643 87.677  1.00 81.07  ?  16   PRO   C N     1 
ATOM   12043 C  CA    . PRO   C 2 17  ? 86.883  128.218 87.981  1.00 79.09  ?  16   PRO   C CA    1 
ATOM   12044 C  C     . PRO   C 2 17  ? 88.134  127.966 88.810  1.00 82.90  ?  16   PRO   C C     1 
ATOM   12045 O  O     . PRO   C 2 17  ? 89.011  128.819 88.950  1.00 86.12  ?  16   PRO   C O     1 
ATOM   12046 C  CB    . PRO   C 2 17  ? 86.985  127.575 86.598  1.00 78.47  ?  16   PRO   C CB    1 
ATOM   12047 C  CG    . PRO   C 2 17  ? 87.573  128.653 85.751  1.00 78.16  ?  16   PRO   C CG    1 
ATOM   12048 C  CD    . PRO   C 2 17  ? 86.933  129.918 86.245  1.00 78.86  ?  16   PRO   C CD    1 
ATOM   12049 N  N     . MET   C 2 18  ? 88.202  126.765 89.385  1.00 82.30  ?  17   MET   C N     1 
ATOM   12050 C  CA    . MET   C 2 18  ? 89.386  126.393 90.152  1.00 81.68  ?  17   MET   C CA    1 
ATOM   12051 C  C     . MET   C 2 18  ? 90.603  126.230 89.250  1.00 86.65  ?  17   MET   C C     1 
ATOM   12052 O  O     . MET   C 2 18  ? 91.693  126.706 89.585  1.00 86.94  ?  17   MET   C O     1 
ATOM   12053 C  CB    . MET   C 2 18  ? 89.121  125.121 90.950  1.00 80.63  ?  17   MET   C CB    1 
ATOM   12054 C  CG    . MET   C 2 18  ? 88.207  125.310 92.136  1.00 91.80  ?  17   MET   C CG    1 
ATOM   12055 S  SD    . MET   C 2 18  ? 87.958  123.832 93.146  1.00 107.84 ?  17   MET   C SD    1 
ATOM   12056 C  CE    . MET   C 2 18  ? 88.807  122.589 92.188  1.00 81.17  ?  17   MET   C CE    1 
ATOM   12057 N  N     . PHE   C 2 19  ? 90.422  125.633 88.074  1.00 72.62  ?  18   PHE   C N     1 
ATOM   12058 C  CA    . PHE   C 2 19  ? 91.495  125.453 87.110  1.00 67.99  ?  18   PHE   C CA    1 
ATOM   12059 C  C     . PHE   C 2 19  ? 91.075  126.003 85.754  1.00 68.03  ?  18   PHE   C C     1 
ATOM   12060 O  O     . PHE   C 2 19  ? 89.888  126.192 85.473  1.00 74.45  ?  18   PHE   C O     1 
ATOM   12061 C  CB    . PHE   C 2 19  ? 91.883  123.977 86.960  1.00 70.95  ?  18   PHE   C CB    1 
ATOM   12062 C  CG    . PHE   C 2 19  ? 92.208  123.292 88.255  1.00 73.30  ?  18   PHE   C CG    1 
ATOM   12063 C  CD1   . PHE   C 2 19  ? 93.483  123.361 88.790  1.00 68.93  ?  18   PHE   C CD1   1 
ATOM   12064 C  CD2   . PHE   C 2 19  ? 91.246  122.559 88.925  1.00 68.09  ?  18   PHE   C CD2   1 
ATOM   12065 C  CE1   . PHE   C 2 19  ? 93.787  122.723 89.977  1.00 65.77  ?  18   PHE   C CE1   1 
ATOM   12066 C  CE2   . PHE   C 2 19  ? 91.546  121.918 90.110  1.00 67.91  ?  18   PHE   C CE2   1 
ATOM   12067 C  CZ    . PHE   C 2 19  ? 92.817  122.000 90.636  1.00 66.53  ?  18   PHE   C CZ    1 
ATOM   12068 N  N     . PHE   C 2 20  ? 92.081  126.263 84.920  1.00 72.45  ?  19   PHE   C N     1 
ATOM   12069 C  CA    . PHE   C 2 20  ? 91.911  126.615 83.511  1.00 73.70  ?  19   PHE   C CA    1 
ATOM   12070 C  C     . PHE   C 2 20  ? 91.184  127.939 83.314  1.00 75.03  ?  19   PHE   C C     1 
ATOM   12071 O  O     . PHE   C 2 20  ? 90.589  128.172 82.258  1.00 76.72  ?  19   PHE   C O     1 
ATOM   12072 C  CB    . PHE   C 2 20  ? 91.198  125.493 82.752  1.00 72.00  ?  19   PHE   C CB    1 
ATOM   12073 C  CG    . PHE   C 2 20  ? 91.779  124.137 83.007  1.00 73.36  ?  19   PHE   C CG    1 
ATOM   12074 C  CD1   . PHE   C 2 20  ? 93.056  123.831 82.582  1.00 71.80  ?  19   PHE   C CD1   1 
ATOM   12075 C  CD2   . PHE   C 2 20  ? 91.044  123.164 83.659  1.00 71.67  ?  19   PHE   C CD2   1 
ATOM   12076 C  CE1   . PHE   C 2 20  ? 93.599  122.587 82.819  1.00 71.77  ?  19   PHE   C CE1   1 
ATOM   12077 C  CE2   . PHE   C 2 20  ? 91.586  121.921 83.907  1.00 73.36  ?  19   PHE   C CE2   1 
ATOM   12078 C  CZ    . PHE   C 2 20  ? 92.862  121.629 83.479  1.00 72.80  ?  19   PHE   C CZ    1 
ATOM   12079 N  N     . GLY   C 2 21  ? 91.222  128.816 84.311  1.00 84.01  ?  20   GLY   C N     1 
ATOM   12080 C  CA    . GLY   C 2 21  ? 90.697  130.156 84.192  1.00 81.94  ?  20   GLY   C CA    1 
ATOM   12081 C  C     . GLY   C 2 21  ? 91.797  131.178 84.000  1.00 85.35  ?  20   GLY   C C     1 
ATOM   12082 O  O     . GLY   C 2 21  ? 92.907  130.866 83.554  1.00 90.98  ?  20   GLY   C O     1 
ATOM   12083 N  N     . GLN   C 2 22  ? 91.485  132.419 84.339  1.00 88.80  ?  21   GLN   C N     1 
ATOM   12084 C  CA    . GLN   C 2 22  ? 92.494  133.468 84.305  1.00 85.43  ?  21   GLN   C CA    1 
ATOM   12085 C  C     . GLN   C 2 22  ? 93.490  133.249 85.437  1.00 92.31  ?  21   GLN   C C     1 
ATOM   12086 O  O     . GLN   C 2 22  ? 93.078  133.016 86.579  1.00 95.32  ?  21   GLN   C O     1 
ATOM   12087 C  CB    . GLN   C 2 22  ? 91.843  134.843 84.428  1.00 87.13  ?  21   GLN   C CB    1 
ATOM   12088 C  CG    . GLN   C 2 22  ? 92.798  135.941 84.855  1.00 90.60  ?  21   GLN   C CG    1 
ATOM   12089 C  CD    . GLN   C 2 22  ? 92.207  137.326 84.692  1.00 94.89  ?  21   GLN   C CD    1 
ATOM   12090 O  OE1   . GLN   C 2 22  ? 91.205  137.509 84.003  1.00 98.49  ?  21   GLN   C OE1   1 
ATOM   12091 N  NE2   . GLN   C 2 22  ? 92.827  138.312 85.329  1.00 94.53  ?  21   GLN   C NE2   1 
ATOM   12092 N  N     . PRO   C 2 23  ? 94.794  133.308 85.169  1.00 91.25  ?  22   PRO   C N     1 
ATOM   12093 C  CA    . PRO   C 2 23  ? 95.776  133.105 86.241  1.00 91.33  ?  22   PRO   C CA    1 
ATOM   12094 C  C     . PRO   C 2 23  ? 95.619  134.140 87.346  1.00 95.92  ?  22   PRO   C C     1 
ATOM   12095 O  O     . PRO   C 2 23  ? 95.304  135.304 87.094  1.00 99.15  ?  22   PRO   C O     1 
ATOM   12096 C  CB    . PRO   C 2 23  ? 97.122  133.248 85.524  1.00 90.80  ?  22   PRO   C CB    1 
ATOM   12097 C  CG    . PRO   C 2 23  ? 96.823  133.026 84.079  1.00 91.03  ?  22   PRO   C CG    1 
ATOM   12098 C  CD    . PRO   C 2 23  ? 95.434  133.533 83.863  1.00 90.44  ?  22   PRO   C CD    1 
ATOM   12099 N  N     . VAL   C 2 24  ? 95.848  133.699 88.585  1.00 84.56  ?  23   VAL   C N     1 
ATOM   12100 C  CA    . VAL   C 2 24  ? 95.659  134.568 89.740  1.00 80.77  ?  23   VAL   C CA    1 
ATOM   12101 C  C     . VAL   C 2 24  ? 96.647  135.722 89.690  1.00 85.42  ?  23   VAL   C C     1 
ATOM   12102 O  O     . VAL   C 2 24  ? 97.815  135.554 89.315  1.00 89.35  ?  23   VAL   C O     1 
ATOM   12103 C  CB    . VAL   C 2 24  ? 95.815  133.771 91.045  1.00 77.17  ?  23   VAL   C CB    1 
ATOM   12104 C  CG1   . VAL   C 2 24  ? 95.145  134.503 92.196  1.00 80.25  ?  23   VAL   C CG1   1 
ATOM   12105 C  CG2   . VAL   C 2 24  ? 95.251  132.375 90.887  1.00 79.49  ?  23   VAL   C CG2   1 
ATOM   12106 N  N     . ASN   C 2 25  ? 96.171  136.915 90.045  1.00 87.20  ?  24   ASN   C N     1 
ATOM   12107 C  CA    . ASN   C 2 25  ? 97.003  138.111 90.070  1.00 86.76  ?  24   ASN   C CA    1 
ATOM   12108 C  C     . ASN   C 2 25  ? 97.255  138.599 91.491  1.00 88.62  ?  24   ASN   C C     1 
ATOM   12109 O  O     . ASN   C 2 25  ? 98.411  138.738 91.901  1.00 94.20  ?  24   ASN   C O     1 
ATOM   12110 C  CB    . ASN   C 2 25  ? 96.359  139.222 89.227  1.00 81.95  ?  24   ASN   C CB    1 
ATOM   12111 C  CG    . ASN   C 2 25  ? 94.863  139.328 89.444  1.00 86.35  ?  24   ASN   C CG    1 
ATOM   12112 O  OD1   . ASN   C 2 25  ? 94.321  138.769 90.396  1.00 94.41  ?  24   ASN   C OD1   1 
ATOM   12113 N  ND2   . ASN   C 2 25  ? 94.187  140.047 88.557  1.00 87.47  ?  24   ASN   C ND2   1 
ATOM   12114 N  N     . VAL   C 2 26  ? 96.203  138.846 92.266  1.00 84.89  ?  25   VAL   C N     1 
ATOM   12115 C  CA    . VAL   C 2 26  ? 96.320  139.359 93.626  1.00 84.67  ?  25   VAL   C CA    1 
ATOM   12116 C  C     . VAL   C 2 26  ? 95.917  138.257 94.593  1.00 84.46  ?  25   VAL   C C     1 
ATOM   12117 O  O     . VAL   C 2 26  ? 94.845  137.658 94.451  1.00 88.61  ?  25   VAL   C O     1 
ATOM   12118 C  CB    . VAL   C 2 26  ? 95.457  140.616 93.830  1.00 81.70  ?  25   VAL   C CB    1 
ATOM   12119 C  CG1   . VAL   C 2 26  ? 95.403  140.991 95.302  1.00 82.59  ?  25   VAL   C CG1   1 
ATOM   12120 C  CG2   . VAL   C 2 26  ? 96.004  141.767 93.007  1.00 85.50  ?  25   VAL   C CG2   1 
ATOM   12121 N  N     . ALA   C 2 27  ? 96.778  137.990 95.573  1.00 82.68  ?  26   ALA   C N     1 
ATOM   12122 C  CA    . ALA   C 2 27  ? 96.529  136.957 96.575  1.00 83.15  ?  26   ALA   C CA    1 
ATOM   12123 C  C     . ALA   C 2 27  ? 95.718  137.572 97.708  1.00 84.65  ?  26   ALA   C C     1 
ATOM   12124 O  O     . ALA   C 2 27  ? 96.246  138.328 98.528  1.00 85.46  ?  26   ALA   C O     1 
ATOM   12125 C  CB    . ALA   C 2 27  ? 97.841  136.370 97.082  1.00 82.63  ?  26   ALA   C CB    1 
ATOM   12126 N  N     . ARG   C 2 28  ? 94.430  137.249 97.752  1.00 90.71  ?  27   ARG   C N     1 
ATOM   12127 C  CA    . ARG   C 2 28  ? 93.529  137.723 98.790  1.00 87.36  ?  27   ARG   C CA    1 
ATOM   12128 C  C     . ARG   C 2 28  ? 93.050  136.551 99.634  1.00 90.79  ?  27   ARG   C C     1 
ATOM   12129 O  O     . ARG   C 2 28  ? 92.882  135.433 99.138  1.00 100.11 ?  27   ARG   C O     1 
ATOM   12130 C  CB    . ARG   C 2 28  ? 92.321  138.451 98.193  1.00 88.73  ?  27   ARG   C CB    1 
ATOM   12131 C  CG    . ARG   C 2 28  ? 92.609  139.213 96.917  1.00 92.88  ?  27   ARG   C CG    1 
ATOM   12132 C  CD    . ARG   C 2 28  ? 91.324  139.736 96.297  1.00 94.47  ?  27   ARG   C CD    1 
ATOM   12133 N  NE    . ARG   C 2 28  ? 90.341  140.094 97.313  1.00 96.87  ?  27   ARG   C NE    1 
ATOM   12134 C  CZ    . ARG   C 2 28  ? 89.288  140.869 97.099  1.00 97.05  ?  27   ARG   C CZ    1 
ATOM   12135 N  NH1   . ARG   C 2 28  ? 89.045  141.390 95.908  1.00 93.99  ?  27   ARG   C NH1   1 
ATOM   12136 N  NH2   . ARG   C 2 28  ? 88.456  141.127 98.104  1.00 94.60  ?  27   ARG   C NH2   1 
ATOM   12137 N  N     . TYR   C 2 29  ? 92.829  136.818 100.922 1.00 75.29  ?  28   TYR   C N     1 
ATOM   12138 C  CA    . TYR   C 2 29  ? 92.358  135.799 101.849 1.00 77.17  ?  28   TYR   C CA    1 
ATOM   12139 C  C     . TYR   C 2 29  ? 91.168  136.273 102.673 1.00 81.75  ?  28   TYR   C C     1 
ATOM   12140 O  O     . TYR   C 2 29  ? 90.765  135.578 103.614 1.00 82.89  ?  28   TYR   C O     1 
ATOM   12141 C  CB    . TYR   C 2 29  ? 93.497  135.344 102.770 1.00 78.13  ?  28   TYR   C CB    1 
ATOM   12142 C  CG    . TYR   C 2 29  ? 94.751  134.962 102.016 1.00 82.35  ?  28   TYR   C CG    1 
ATOM   12143 C  CD1   . TYR   C 2 29  ? 95.727  135.906 101.734 1.00 85.75  ?  28   TYR   C CD1   1 
ATOM   12144 C  CD2   . TYR   C 2 29  ? 94.953  133.660 101.575 1.00 81.33  ?  28   TYR   C CD2   1 
ATOM   12145 C  CE1   . TYR   C 2 29  ? 96.867  135.567 101.031 1.00 85.24  ?  28   TYR   C CE1   1 
ATOM   12146 C  CE2   . TYR   C 2 29  ? 96.092  133.310 100.882 1.00 81.88  ?  28   TYR   C CE2   1 
ATOM   12147 C  CZ    . TYR   C 2 29  ? 97.047  134.265 100.613 1.00 84.22  ?  28   TYR   C CZ    1 
ATOM   12148 O  OH    . TYR   C 2 29  ? 98.184  133.918 99.921  1.00 85.15  ?  28   TYR   C OH    1 
ATOM   12149 N  N     . ASP   C 2 30  ? 90.599  137.433 102.347 1.00 95.16  ?  29   ASP   C N     1 
ATOM   12150 C  CA    . ASP   C 2 30  ? 89.396  137.914 103.011 1.00 96.68  ?  29   ASP   C CA    1 
ATOM   12151 C  C     . ASP   C 2 30  ? 88.125  137.290 102.455 1.00 98.74  ?  29   ASP   C C     1 
ATOM   12152 O  O     . ASP   C 2 30  ? 87.071  137.403 103.089 1.00 101.23 ?  29   ASP   C O     1 
ATOM   12153 C  CB    . ASP   C 2 30  ? 89.306  139.436 102.891 1.00 97.60  ?  29   ASP   C CB    1 
ATOM   12154 C  CG    . ASP   C 2 30  ? 89.079  139.894 101.463 1.00 99.87  ?  29   ASP   C CG    1 
ATOM   12155 O  OD1   . ASP   C 2 30  ? 89.999  139.737 100.634 1.00 98.92  ?  29   ASP   C OD1   1 
ATOM   12156 O  OD2   . ASP   C 2 30  ? 87.981  140.408 101.168 1.00 100.73 ?  29   ASP   C OD2   1 
ATOM   12157 N  N     . GLN   C 2 31  ? 88.197  136.652 101.289 1.00 93.65  ?  30   GLN   C N     1 
ATOM   12158 C  CA    . GLN   C 2 31  ? 87.040  136.035 100.660 1.00 91.36  ?  30   GLN   C CA    1 
ATOM   12159 C  C     . GLN   C 2 31  ? 87.515  134.861 99.819  1.00 95.23  ?  30   GLN   C C     1 
ATOM   12160 O  O     . GLN   C 2 31  ? 88.504  134.973 99.091  1.00 98.32  ?  30   GLN   C O     1 
ATOM   12161 C  CB    . GLN   C 2 31  ? 86.277  137.036 99.788  1.00 89.58  ?  30   GLN   C CB    1 
ATOM   12162 C  CG    . GLN   C 2 31  ? 87.080  137.549 98.607  1.00 92.22  ?  30   GLN   C CG    1 
ATOM   12163 C  CD    . GLN   C 2 31  ? 86.307  138.535 97.760  1.00 96.53  ?  30   GLN   C CD    1 
ATOM   12164 O  OE1   . GLN   C 2 31  ? 85.328  139.127 98.213  1.00 96.89  ?  30   GLN   C OE1   1 
ATOM   12165 N  NE2   . GLN   C 2 31  ? 86.743  138.718 96.519  1.00 96.34  ?  30   GLN   C NE2   1 
ATOM   12166 N  N     . GLN   C 2 32  ? 86.808  133.739 99.924  1.00 89.89  ?  31   GLN   C N     1 
ATOM   12167 C  CA    . GLN   C 2 32  ? 87.160  132.530 99.194  1.00 85.66  ?  31   GLN   C CA    1 
ATOM   12168 C  C     . GLN   C 2 32  ? 85.945  132.006 98.447  1.00 84.49  ?  31   GLN   C C     1 
ATOM   12169 O  O     . GLN   C 2 32  ? 84.835  131.981 98.986  1.00 88.38  ?  31   GLN   C O     1 
ATOM   12170 C  CB    . GLN   C 2 32  ? 87.704  131.438 100.134 1.00 86.96  ?  31   GLN   C CB    1 
ATOM   12171 C  CG    . GLN   C 2 32  ? 88.652  131.958 101.203 1.00 86.86  ?  31   GLN   C CG    1 
ATOM   12172 C  CD    . GLN   C 2 32  ? 87.946  132.351 102.480 1.00 91.87  ?  31   GLN   C CD    1 
ATOM   12173 O  OE1   . GLN   C 2 32  ? 86.811  131.947 102.729 1.00 94.59  ?  31   GLN   C OE1   1 
ATOM   12174 N  NE2   . GLN   C 2 32  ? 88.616  133.152 103.300 1.00 90.72  ?  31   GLN   C NE2   1 
ATOM   12175 N  N     . LYS   C 2 33  ? 86.164  131.596 97.196  1.00 82.49  ?  32   LYS   C N     1 
ATOM   12176 C  CA    . LYS   C 2 33  ? 85.121  130.892 96.459  1.00 84.64  ?  32   LYS   C CA    1 
ATOM   12177 C  C     . LYS   C 2 33  ? 84.785  129.571 97.136  1.00 85.64  ?  32   LYS   C C     1 
ATOM   12178 O  O     . LYS   C 2 33  ? 83.613  129.187 97.224  1.00 87.74  ?  32   LYS   C O     1 
ATOM   12179 C  CB    . LYS   C 2 33  ? 85.564  130.668 95.014  1.00 85.08  ?  32   LYS   C CB    1 
ATOM   12180 C  CG    . LYS   C 2 33  ? 84.784  129.596 94.276  1.00 87.57  ?  32   LYS   C CG    1 
ATOM   12181 C  CD    . LYS   C 2 33  ? 84.825  129.826 92.777  1.00 85.42  ?  32   LYS   C CD    1 
ATOM   12182 C  CE    . LYS   C 2 33  ? 83.770  129.000 92.064  1.00 84.12  ?  32   LYS   C CE    1 
ATOM   12183 N  NZ    . LYS   C 2 33  ? 84.000  128.959 90.595  1.00 89.18  ?  32   LYS   C NZ    1 
ATOM   12184 N  N     . TYR   C 2 34  ? 85.803  128.866 97.626  1.00 86.12  ?  33   TYR   C N     1 
ATOM   12185 C  CA    . TYR   C 2 34  ? 85.630  127.647 98.405  1.00 86.20  ?  33   TYR   C CA    1 
ATOM   12186 C  C     . TYR   C 2 34  ? 86.391  127.809 99.710  1.00 89.23  ?  33   TYR   C C     1 
ATOM   12187 O  O     . TYR   C 2 34  ? 87.621  127.920 99.704  1.00 90.00  ?  33   TYR   C O     1 
ATOM   12188 C  CB    . TYR   C 2 34  ? 86.123  126.422 97.632  1.00 84.41  ?  33   TYR   C CB    1 
ATOM   12189 C  CG    . TYR   C 2 34  ? 85.354  126.178 96.358  1.00 84.82  ?  33   TYR   C CG    1 
ATOM   12190 C  CD1   . TYR   C 2 34  ? 83.995  125.905 96.389  1.00 87.25  ?  33   TYR   C CD1   1 
ATOM   12191 C  CD2   . TYR   C 2 34  ? 85.982  126.237 95.124  1.00 79.31  ?  33   TYR   C CD2   1 
ATOM   12192 C  CE1   . TYR   C 2 34  ? 83.284  125.687 95.229  1.00 85.98  ?  33   TYR   C CE1   1 
ATOM   12193 C  CE2   . TYR   C 2 34  ? 85.279  126.022 93.958  1.00 80.68  ?  33   TYR   C CE2   1 
ATOM   12194 C  CZ    . TYR   C 2 34  ? 83.931  125.746 94.016  1.00 89.68  ?  33   TYR   C CZ    1 
ATOM   12195 O  OH    . TYR   C 2 34  ? 83.227  125.530 92.854  1.00 95.61  ?  33   TYR   C OH    1 
ATOM   12196 N  N     . ASP   C 2 35  ? 85.659  127.830 100.825 1.00 94.36  ?  34   ASP   C N     1 
ATOM   12197 C  CA    . ASP   C 2 35  ? 86.284  128.040 102.124 1.00 90.45  ?  34   ASP   C CA    1 
ATOM   12198 C  C     . ASP   C 2 35  ? 87.073  126.826 102.596 1.00 89.91  ?  34   ASP   C C     1 
ATOM   12199 O  O     . ASP   C 2 35  ? 87.899  126.958 103.505 1.00 96.36  ?  34   ASP   C O     1 
ATOM   12200 C  CB    . ASP   C 2 35  ? 85.222  128.407 103.161 1.00 87.98  ?  34   ASP   C CB    1 
ATOM   12201 C  CG    . ASP   C 2 35  ? 84.080  127.416 103.201 1.00 95.78  ?  34   ASP   C CG    1 
ATOM   12202 O  OD1   . ASP   C 2 35  ? 83.618  126.995 102.121 1.00 97.82  ?  34   ASP   C OD1   1 
ATOM   12203 O  OD2   . ASP   C 2 35  ? 83.641  127.061 104.314 1.00 98.43  ?  34   ASP   C OD2   1 
ATOM   12204 N  N     . ILE   C 2 36  ? 86.845  125.656 101.994 1.00 77.03  ?  35   ILE   C N     1 
ATOM   12205 C  CA    . ILE   C 2 36  ? 87.501  124.434 102.453 1.00 76.17  ?  35   ILE   C CA    1 
ATOM   12206 C  C     . ILE   C 2 36  ? 89.013  124.549 102.317 1.00 75.99  ?  35   ILE   C C     1 
ATOM   12207 O  O     . ILE   C 2 36  ? 89.760  124.117 103.201 1.00 83.46  ?  35   ILE   C O     1 
ATOM   12208 C  CB    . ILE   C 2 36  ? 86.946  123.212 101.699 1.00 76.33  ?  35   ILE   C CB    1 
ATOM   12209 C  CG1   . ILE   C 2 36  ? 87.761  121.963 102.037 1.00 74.87  ?  35   ILE   C CG1   1 
ATOM   12210 C  CG2   . ILE   C 2 36  ? 86.948  123.459 100.197 1.00 75.80  ?  35   ILE   C CG2   1 
ATOM   12211 C  CD1   . ILE   C 2 36  ? 87.701  121.565 103.499 1.00 73.65  ?  35   ILE   C CD1   1 
ATOM   12212 N  N     . PHE   C 2 37  ? 89.490  125.165 101.234 1.00 60.53  ?  36   PHE   C N     1 
ATOM   12213 C  CA    . PHE   C 2 37  ? 90.925  125.357 101.073 1.00 56.36  ?  36   PHE   C CA    1 
ATOM   12214 C  C     . PHE   C 2 37  ? 91.474  126.353 102.085 1.00 70.06  ?  36   PHE   C C     1 
ATOM   12215 O  O     . PHE   C 2 37  ? 92.603  126.190 102.556 1.00 79.76  ?  36   PHE   C O     1 
ATOM   12216 C  CB    . PHE   C 2 37  ? 91.233  125.796 99.645  1.00 60.76  ?  36   PHE   C CB    1 
ATOM   12217 C  CG    . PHE   C 2 37  ? 90.801  124.800 98.609  1.00 65.90  ?  36   PHE   C CG    1 
ATOM   12218 C  CD1   . PHE   C 2 37  ? 91.187  123.473 98.706  1.00 66.46  ?  36   PHE   C CD1   1 
ATOM   12219 C  CD2   . PHE   C 2 37  ? 89.999  125.182 97.548  1.00 68.89  ?  36   PHE   C CD2   1 
ATOM   12220 C  CE1   . PHE   C 2 37  ? 90.788  122.549 97.762  1.00 66.32  ?  36   PHE   C CE1   1 
ATOM   12221 C  CE2   . PHE   C 2 37  ? 89.598  124.260 96.600  1.00 69.40  ?  36   PHE   C CE2   1 
ATOM   12222 C  CZ    . PHE   C 2 37  ? 89.993  122.942 96.708  1.00 68.32  ?  36   PHE   C CZ    1 
ATOM   12223 N  N     . GLU   C 2 38  ? 90.693  127.375 102.443 1.00 78.03  ?  37   GLU   C N     1 
ATOM   12224 C  CA    . GLU   C 2 38  ? 91.108  128.289 103.504 1.00 73.81  ?  37   GLU   C CA    1 
ATOM   12225 C  C     . GLU   C 2 38  ? 91.260  127.558 104.832 1.00 74.66  ?  37   GLU   C C     1 
ATOM   12226 O  O     . GLU   C 2 38  ? 92.246  127.751 105.557 1.00 80.10  ?  37   GLU   C O     1 
ATOM   12227 C  CB    . GLU   C 2 38  ? 90.102  129.432 103.632 1.00 77.47  ?  37   GLU   C CB    1 
ATOM   12228 C  CG    . GLU   C 2 38  ? 90.482  130.493 104.659 1.00 84.69  ?  37   GLU   C CG    1 
ATOM   12229 C  CD    . GLU   C 2 38  ? 91.745  131.257 104.324 1.00 90.49  ?  37   GLU   C CD    1 
ATOM   12230 O  OE1   . GLU   C 2 38  ? 92.205  131.189 103.169 1.00 90.30  ?  37   GLU   C OE1   1 
ATOM   12231 O  OE2   . GLU   C 2 38  ? 92.271  131.939 105.229 1.00 88.38  ?  37   GLU   C OE2   1 
ATOM   12232 N  N     . LYS   C 2 39  ? 90.288  126.709 105.166 1.00 69.79  ?  38   LYS   C N     1 
ATOM   12233 C  CA    . LYS   C 2 39  ? 90.381  125.929 106.394 1.00 70.05  ?  38   LYS   C CA    1 
ATOM   12234 C  C     . LYS   C 2 39  ? 91.571  124.980 106.352 1.00 70.97  ?  38   LYS   C C     1 
ATOM   12235 O  O     . LYS   C 2 39  ? 92.249  124.776 107.366 1.00 75.45  ?  38   LYS   C O     1 
ATOM   12236 C  CB    . LYS   C 2 39  ? 89.088  125.148 106.616 1.00 69.73  ?  38   LYS   C CB    1 
ATOM   12237 C  CG    . LYS   C 2 39  ? 87.894  125.968 107.064 1.00 71.50  ?  38   LYS   C CG    1 
ATOM   12238 C  CD    . LYS   C 2 39  ? 86.670  125.617 106.233 1.00 78.65  ?  38   LYS   C CD    1 
ATOM   12239 C  CE    . LYS   C 2 39  ? 85.399  126.153 106.863 1.00 80.39  ?  38   LYS   C CE    1 
ATOM   12240 N  NZ    . LYS   C 2 39  ? 84.197  125.750 106.084 1.00 82.21  ?  38   LYS   C NZ    1 
ATOM   12241 N  N     . LEU   C 2 40  ? 91.832  124.379 105.189 1.00 53.58  ?  39   LEU   C N     1 
ATOM   12242 C  CA    . LEU   C 2 40  ? 92.979  123.487 105.051 1.00 51.79  ?  39   LEU   C CA    1 
ATOM   12243 C  C     . LEU   C 2 40  ? 94.288  124.233 105.262 1.00 54.74  ?  39   LEU   C C     1 
ATOM   12244 O  O     . LEU   C 2 40  ? 95.195  123.730 105.934 1.00 67.82  ?  39   LEU   C O     1 
ATOM   12245 C  CB    . LEU   C 2 40  ? 92.962  122.817 103.679 1.00 48.02  ?  39   LEU   C CB    1 
ATOM   12246 C  CG    . LEU   C 2 40  ? 91.975  121.662 103.530 1.00 51.82  ?  39   LEU   C CG    1 
ATOM   12247 C  CD1   . LEU   C 2 40  ? 91.747  121.372 102.063 1.00 57.08  ?  39   LEU   C CD1   1 
ATOM   12248 C  CD2   . LEU   C 2 40  ? 92.477  120.427 104.256 1.00 55.02  ?  39   LEU   C CD2   1 
ATOM   12249 N  N     . ILE   C 2 41  ? 94.406  125.434 104.695 1.00 52.59  ?  40   ILE   C N     1 
ATOM   12250 C  CA    . ILE   C 2 41  ? 95.615  126.229 104.886 1.00 49.84  ?  40   ILE   C CA    1 
ATOM   12251 C  C     . ILE   C 2 41  ? 95.790  126.585 106.354 1.00 57.18  ?  40   ILE   C C     1 
ATOM   12252 O  O     . ILE   C 2 41  ? 96.891  126.475 106.905 1.00 68.40  ?  40   ILE   C O     1 
ATOM   12253 C  CB    . ILE   C 2 41  ? 95.582  127.490 104.004 1.00 51.01  ?  40   ILE   C CB    1 
ATOM   12254 C  CG1   . ILE   C 2 41  ? 95.613  127.121 102.523 1.00 52.54  ?  40   ILE   C CG1   1 
ATOM   12255 C  CG2   . ILE   C 2 41  ? 96.749  128.406 104.342 1.00 52.63  ?  40   ILE   C CG2   1 
ATOM   12256 C  CD1   . ILE   C 2 41  ? 95.041  128.196 101.626 1.00 48.52  ?  40   ILE   C CD1   1 
ATOM   12257 N  N     . GLU   C 2 42  ? 94.707  127.002 107.014 1.00 68.33  ?  41   GLU   C N     1 
ATOM   12258 C  CA    . GLU   C 2 42  ? 94.797  127.353 108.428 1.00 62.86  ?  41   GLU   C CA    1 
ATOM   12259 C  C     . GLU   C 2 42  ? 95.206  126.152 109.272 1.00 66.92  ?  41   GLU   C C     1 
ATOM   12260 O  O     . GLU   C 2 42  ? 96.055  126.272 110.163 1.00 77.04  ?  41   GLU   C O     1 
ATOM   12261 C  CB    . GLU   C 2 42  ? 93.465  127.923 108.910 1.00 68.24  ?  41   GLU   C CB    1 
ATOM   12262 C  CG    . GLU   C 2 42  ? 93.607  129.067 109.896 1.00 76.97  ?  41   GLU   C CG    1 
ATOM   12263 C  CD    . GLU   C 2 42  ? 92.507  129.076 110.937 1.00 87.79  ?  41   GLU   C CD    1 
ATOM   12264 O  OE1   . GLU   C 2 42  ? 91.553  128.281 110.801 1.00 86.46  ?  41   GLU   C OE1   1 
ATOM   12265 O  OE2   . GLU   C 2 42  ? 92.596  129.877 111.890 1.00 84.93  ?  41   GLU   C OE2   1 
ATOM   12266 N  N     . LYS   C 2 43  ? 94.619  124.984 109.003 1.00 63.74  ?  42   LYS   C N     1 
ATOM   12267 C  CA    . LYS   C 2 43  ? 94.961  123.789 109.766 1.00 58.24  ?  42   LYS   C CA    1 
ATOM   12268 C  C     . LYS   C 2 43  ? 96.404  123.366 109.521 1.00 59.49  ?  42   LYS   C C     1 
ATOM   12269 O  O     . LYS   C 2 43  ? 97.106  122.973 110.459 1.00 68.07  ?  42   LYS   C O     1 
ATOM   12270 C  CB    . LYS   C 2 43  ? 94.000  122.653 109.421 1.00 58.49  ?  42   LYS   C CB    1 
ATOM   12271 C  CG    . LYS   C 2 43  ? 92.929  122.415 110.469 1.00 68.16  ?  42   LYS   C CG    1 
ATOM   12272 C  CD    . LYS   C 2 43  ? 92.135  121.156 110.178 1.00 71.15  ?  42   LYS   C CD    1 
ATOM   12273 C  CE    . LYS   C 2 43  ? 91.999  120.296 111.423 1.00 76.70  ?  42   LYS   C CE    1 
ATOM   12274 N  NZ    . LYS   C 2 43  ? 91.898  121.121 112.657 1.00 77.17  ?  42   LYS   C NZ    1 
ATOM   12275 N  N     . GLN   C 2 44  ? 96.863  123.437 108.269 1.00 55.65  ?  43   GLN   C N     1 
ATOM   12276 C  CA    . GLN   C 2 44  ? 98.246  123.086 107.964 1.00 47.08  ?  43   GLN   C CA    1 
ATOM   12277 C  C     . GLN   C 2 44  ? 99.218  124.032 108.654 1.00 47.96  ?  43   GLN   C C     1 
ATOM   12278 O  O     . GLN   C 2 44  ? 100.268 123.604 109.146 1.00 59.14  ?  43   GLN   C O     1 
ATOM   12279 C  CB    . GLN   C 2 44  ? 98.468  123.095 106.452 1.00 54.33  ?  43   GLN   C CB    1 
ATOM   12280 C  CG    . GLN   C 2 44  ? 99.740  122.389 105.999 1.00 55.61  ?  43   GLN   C CG    1 
ATOM   12281 C  CD    . GLN   C 2 44  ? 99.944  121.046 106.670 1.00 58.37  ?  43   GLN   C CD    1 
ATOM   12282 O  OE1   . GLN   C 2 44  ? 99.297  120.061 106.321 1.00 62.68  ?  43   GLN   C OE1   1 
ATOM   12283 N  NE2   . GLN   C 2 44  ? 100.854 121.000 107.635 1.00 61.03  ?  43   GLN   C NE2   1 
ATOM   12284 N  N     . LEU   C 2 45  ? 98.893  125.325 108.688 1.00 52.36  ?  44   LEU   C N     1 
ATOM   12285 C  CA    . LEU   C 2 45  ? 99.747  126.275 109.392 1.00 46.27  ?  44   LEU   C CA    1 
ATOM   12286 C  C     . LEU   C 2 45  ? 99.758  126.007 110.891 1.00 48.83  ?  44   LEU   C C     1 
ATOM   12287 O  O     . LEU   C 2 45  ? 100.816 126.066 111.525 1.00 59.62  ?  44   LEU   C O     1 
ATOM   12288 C  CB    . LEU   C 2 45  ? 99.294  127.703 109.104 1.00 44.47  ?  44   LEU   C CB    1 
ATOM   12289 C  CG    . LEU   C 2 45  ? 99.465  128.182 107.666 1.00 48.95  ?  44   LEU   C CG    1 
ATOM   12290 C  CD1   . LEU   C 2 45  ? 98.998  129.619 107.509 1.00 52.99  ?  44   LEU   C CD1   1 
ATOM   12291 C  CD2   . LEU   C 2 45  ? 100.907 128.028 107.240 1.00 52.87  ?  44   LEU   C CD2   1 
ATOM   12292 N  N     . SER   C 2 46  ? 98.598  125.699 111.475 1.00 49.84  ?  45   SER   C N     1 
ATOM   12293 C  CA    . SER   C 2 46  ? 98.564  125.369 112.895 1.00 42.53  ?  45   SER   C CA    1 
ATOM   12294 C  C     . SER   C 2 46  ? 99.283  124.058 113.187 1.00 51.25  ?  45   SER   C C     1 
ATOM   12295 O  O     . SER   C 2 46  ? 99.772  123.858 114.304 1.00 57.07  ?  45   SER   C O     1 
ATOM   12296 C  CB    . SER   C 2 46  ? 97.120  125.303 113.383 1.00 36.09  ?  45   SER   C CB    1 
ATOM   12297 O  OG    . SER   C 2 46  ? 96.465  124.148 112.894 1.00 53.98  ?  45   SER   C OG    1 
ATOM   12298 N  N     . PHE   C 2 47  ? 99.360  123.162 112.205 1.00 51.82  ?  46   PHE   C N     1 
ATOM   12299 C  CA    . PHE   C 2 47  ? 100.013 121.870 112.357 1.00 40.01  ?  46   PHE   C CA    1 
ATOM   12300 C  C     . PHE   C 2 47  ? 101.518 121.936 112.146 1.00 51.11  ?  46   PHE   C C     1 
ATOM   12301 O  O     . PHE   C 2 47  ? 102.133 120.894 111.896 1.00 63.80  ?  46   PHE   C O     1 
ATOM   12302 C  CB    . PHE   C 2 47  ? 99.409  120.853 111.385 1.00 47.14  ?  46   PHE   C CB    1 
ATOM   12303 C  CG    . PHE   C 2 47  ? 98.078  120.310 111.816 1.00 46.11  ?  46   PHE   C CG    1 
ATOM   12304 C  CD1   . PHE   C 2 47  ? 97.522  120.670 113.030 1.00 48.86  ?  46   PHE   C CD1   1 
ATOM   12305 C  CD2   . PHE   C 2 47  ? 97.382  119.436 111.001 1.00 44.88  ?  46   PHE   C CD2   1 
ATOM   12306 C  CE1   . PHE   C 2 47  ? 96.297  120.168 113.421 1.00 54.25  ?  46   PHE   C CE1   1 
ATOM   12307 C  CE2   . PHE   C 2 47  ? 96.157  118.934 111.386 1.00 55.97  ?  46   PHE   C CE2   1 
ATOM   12308 C  CZ    . PHE   C 2 47  ? 95.615  119.299 112.599 1.00 59.72  ?  46   PHE   C CZ    1 
ATOM   12309 N  N     . PHE   C 2 48  ? 102.123 123.118 112.226 1.00 50.78  ?  47   PHE   C N     1 
ATOM   12310 C  CA    . PHE   C 2 48  ? 103.556 123.242 112.000 1.00 47.72  ?  47   PHE   C CA    1 
ATOM   12311 C  C     . PHE   C 2 48  ? 104.334 122.460 113.050 1.00 53.58  ?  47   PHE   C C     1 
ATOM   12312 O  O     . PHE   C 2 48  ? 103.991 122.461 114.235 1.00 66.55  ?  47   PHE   C O     1 
ATOM   12313 C  CB    . PHE   C 2 48  ? 103.972 124.715 112.021 1.00 50.93  ?  47   PHE   C CB    1 
ATOM   12314 C  CG    . PHE   C 2 48  ? 105.433 124.936 111.736 1.00 51.71  ?  47   PHE   C CG    1 
ATOM   12315 C  CD1   . PHE   C 2 48  ? 105.906 124.936 110.436 1.00 51.76  ?  47   PHE   C CD1   1 
ATOM   12316 C  CD2   . PHE   C 2 48  ? 106.343 125.069 112.771 1.00 45.61  ?  47   PHE   C CD2   1 
ATOM   12317 C  CE1   . PHE   C 2 48  ? 107.247 125.131 110.171 1.00 56.74  ?  47   PHE   C CE1   1 
ATOM   12318 C  CE2   . PHE   C 2 48  ? 107.684 125.266 112.513 1.00 45.22  ?  47   PHE   C CE2   1 
ATOM   12319 C  CZ    . PHE   C 2 48  ? 108.137 125.292 111.211 1.00 48.34  ?  47   PHE   C CZ    1 
ATOM   12320 N  N     . TRP   C 2 49  ? 105.389 121.788 112.602 1.00 52.36  ?  48   TRP   C N     1 
ATOM   12321 C  CA    . TRP   C 2 49  ? 106.238 120.998 113.481 1.00 41.85  ?  48   TRP   C CA    1 
ATOM   12322 C  C     . TRP   C 2 49  ? 107.564 120.763 112.775 1.00 46.72  ?  48   TRP   C C     1 
ATOM   12323 O  O     . TRP   C 2 49  ? 107.700 120.999 111.572 1.00 59.99  ?  48   TRP   C O     1 
ATOM   12324 C  CB    . TRP   C 2 49  ? 105.575 119.671 113.855 1.00 41.72  ?  48   TRP   C CB    1 
ATOM   12325 C  CG    . TRP   C 2 49  ? 105.355 118.778 112.678 1.00 51.31  ?  48   TRP   C CG    1 
ATOM   12326 C  CD1   . TRP   C 2 49  ? 104.335 118.847 111.780 1.00 50.01  ?  48   TRP   C CD1   1 
ATOM   12327 C  CD2   . TRP   C 2 49  ? 106.182 117.686 112.263 1.00 47.97  ?  48   TRP   C CD2   1 
ATOM   12328 N  NE1   . TRP   C 2 49  ? 104.470 117.864 110.833 1.00 47.79  ?  48   TRP   C NE1   1 
ATOM   12329 C  CE2   . TRP   C 2 49  ? 105.598 117.137 111.107 1.00 47.63  ?  48   TRP   C CE2   1 
ATOM   12330 C  CE3   . TRP   C 2 49  ? 107.358 117.117 112.758 1.00 47.25  ?  48   TRP   C CE3   1 
ATOM   12331 C  CZ2   . TRP   C 2 49  ? 106.147 116.049 110.439 1.00 50.13  ?  48   TRP   C CZ2   1 
ATOM   12332 C  CZ3   . TRP   C 2 49  ? 107.902 116.037 112.094 1.00 46.02  ?  48   TRP   C CZ3   1 
ATOM   12333 C  CH2   . TRP   C 2 49  ? 107.296 115.513 110.948 1.00 48.66  ?  48   TRP   C CH2   1 
ATOM   12334 N  N     . ARG   C 2 50  ? 108.543 120.297 113.540 1.00 49.05  ?  49   ARG   C N     1 
ATOM   12335 C  CA    . ARG   C 2 50  ? 109.846 119.944 113.004 1.00 50.85  ?  49   ARG   C CA    1 
ATOM   12336 C  C     . ARG   C 2 50  ? 110.325 118.665 113.670 1.00 56.83  ?  49   ARG   C C     1 
ATOM   12337 O  O     . ARG   C 2 50  ? 109.970 118.393 114.823 1.00 68.27  ?  49   ARG   C O     1 
ATOM   12338 C  CB    . ARG   C 2 50  ? 110.870 121.068 113.223 1.00 51.75  ?  49   ARG   C CB    1 
ATOM   12339 C  CG    . ARG   C 2 50  ? 110.751 122.204 112.224 1.00 50.03  ?  49   ARG   C CG    1 
ATOM   12340 C  CD    . ARG   C 2 50  ? 111.384 123.471 112.756 1.00 52.51  ?  49   ARG   C CD    1 
ATOM   12341 N  NE    . ARG   C 2 50  ? 112.817 123.507 112.501 1.00 54.82  ?  49   ARG   C NE    1 
ATOM   12342 C  CZ    . ARG   C 2 50  ? 113.679 124.254 113.176 1.00 56.36  ?  49   ARG   C CZ    1 
ATOM   12343 N  NH1   . ARG   C 2 50  ? 113.285 125.042 114.162 1.00 54.58  ?  49   ARG   C NH1   1 
ATOM   12344 N  NH2   . ARG   C 2 50  ? 114.968 124.209 112.854 1.00 61.60  ?  49   ARG   C NH2   1 
ATOM   12345 N  N     . PRO   C 2 51  ? 111.123 117.857 112.968 1.00 57.49  ?  50   PRO   C N     1 
ATOM   12346 C  CA    . PRO   C 2 51  ? 111.612 116.609 113.575 1.00 54.29  ?  50   PRO   C CA    1 
ATOM   12347 C  C     . PRO   C 2 51  ? 112.508 116.831 114.781 1.00 60.95  ?  50   PRO   C C     1 
ATOM   12348 O  O     . PRO   C 2 51  ? 112.712 115.892 115.559 1.00 64.79  ?  50   PRO   C O     1 
ATOM   12349 C  CB    . PRO   C 2 51  ? 112.372 115.931 112.426 1.00 53.01  ?  50   PRO   C CB    1 
ATOM   12350 C  CG    . PRO   C 2 51  ? 112.676 117.023 111.459 1.00 54.18  ?  50   PRO   C CG    1 
ATOM   12351 C  CD    . PRO   C 2 51  ? 111.550 117.999 111.567 1.00 56.67  ?  50   PRO   C CD    1 
ATOM   12352 N  N     . GLU   C 2 52  ? 113.087 118.023 114.937 1.00 78.88  ?  51   GLU   C N     1 
ATOM   12353 C  CA    . GLU   C 2 52  ? 113.998 118.274 116.047 1.00 74.95  ?  51   GLU   C CA    1 
ATOM   12354 C  C     . GLU   C 2 52  ? 113.284 118.305 117.391 1.00 80.63  ?  51   GLU   C C     1 
ATOM   12355 O  O     . GLU   C 2 52  ? 113.945 118.201 118.430 1.00 89.17  ?  51   GLU   C O     1 
ATOM   12356 C  CB    . GLU   C 2 52  ? 114.739 119.596 115.839 1.00 75.97  ?  51   GLU   C CB    1 
ATOM   12357 C  CG    . GLU   C 2 52  ? 115.829 119.576 114.774 1.00 83.42  ?  51   GLU   C CG    1 
ATOM   12358 C  CD    . GLU   C 2 52  ? 115.310 119.839 113.377 1.00 89.05  ?  51   GLU   C CD    1 
ATOM   12359 O  OE1   . GLU   C 2 52  ? 114.081 119.955 113.211 1.00 90.99  ?  51   GLU   C OE1   1 
ATOM   12360 O  OE2   . GLU   C 2 52  ? 116.134 119.928 112.443 1.00 91.63  ?  51   GLU   C OE2   1 
ATOM   12361 N  N     . GLU   C 2 53  ? 111.958 118.444 117.398 1.00 73.04  ?  52   GLU   C N     1 
ATOM   12362 C  CA    . GLU   C 2 53  ? 111.204 118.546 118.640 1.00 73.32  ?  52   GLU   C CA    1 
ATOM   12363 C  C     . GLU   C 2 53  ? 110.939 117.196 119.291 1.00 76.31  ?  52   GLU   C C     1 
ATOM   12364 O  O     . GLU   C 2 53  ? 110.402 117.162 120.403 1.00 85.10  ?  52   GLU   C O     1 
ATOM   12365 C  CB    . GLU   C 2 53  ? 109.875 119.264 118.391 1.00 72.29  ?  52   GLU   C CB    1 
ATOM   12366 C  CG    . GLU   C 2 53  ? 108.739 118.351 117.968 1.00 76.68  ?  52   GLU   C CG    1 
ATOM   12367 C  CD    . GLU   C 2 53  ? 107.546 119.115 117.429 1.00 83.21  ?  52   GLU   C CD    1 
ATOM   12368 O  OE1   . GLU   C 2 53  ? 107.741 120.005 116.576 1.00 86.10  ?  52   GLU   C OE1   1 
ATOM   12369 O  OE2   . GLU   C 2 53  ? 106.412 118.828 117.861 1.00 84.15  ?  52   GLU   C OE2   1 
ATOM   12370 N  N     . VAL   C 2 54  ? 111.296 116.094 118.638 1.00 73.22  ?  53   VAL   C N     1 
ATOM   12371 C  CA    . VAL   C 2 54  ? 111.058 114.753 119.161 1.00 71.74  ?  53   VAL   C CA    1 
ATOM   12372 C  C     . VAL   C 2 54  ? 112.404 114.124 119.494 1.00 75.16  ?  53   VAL   C C     1 
ATOM   12373 O  O     . VAL   C 2 54  ? 113.272 114.003 118.622 1.00 82.68  ?  53   VAL   C O     1 
ATOM   12374 C  CB    . VAL   C 2 54  ? 110.274 113.885 118.165 1.00 68.60  ?  53   VAL   C CB    1 
ATOM   12375 C  CG1   . VAL   C 2 54  ? 110.159 112.461 118.686 1.00 68.40  ?  53   VAL   C CG1   1 
ATOM   12376 C  CG2   . VAL   C 2 54  ? 108.898 114.479 117.917 1.00 71.29  ?  53   VAL   C CG2   1 
ATOM   12377 N  N     . ASP   C 2 55  ? 112.576 113.721 120.750 1.00 79.79  ?  54   ASP   C N     1 
ATOM   12378 C  CA    . ASP   C 2 55  ? 113.795 113.031 121.153 1.00 79.57  ?  54   ASP   C CA    1 
ATOM   12379 C  C     . ASP   C 2 55  ? 113.794 111.615 120.590 1.00 82.92  ?  54   ASP   C C     1 
ATOM   12380 O  O     . ASP   C 2 55  ? 112.833 110.864 120.774 1.00 86.31  ?  54   ASP   C O     1 
ATOM   12381 C  CB    . ASP   C 2 55  ? 113.910 113.002 122.675 1.00 79.80  ?  54   ASP   C CB    1 
ATOM   12382 C  CG    . ASP   C 2 55  ? 115.124 112.232 123.155 1.00 88.91  ?  54   ASP   C CG    1 
ATOM   12383 O  OD1   . ASP   C 2 55  ? 115.032 110.995 123.294 1.00 98.08  ?  54   ASP   C OD1   1 
ATOM   12384 O  OD2   . ASP   C 2 55  ? 116.173 112.864 123.396 1.00 91.24  ?  54   ASP   C OD2   1 
ATOM   12385 N  N     . VAL   C 2 56  ? 114.874 111.252 119.903 1.00 68.36  ?  55   VAL   C N     1 
ATOM   12386 C  CA    . VAL   C 2 56  ? 114.955 109.984 119.192 1.00 68.51  ?  55   VAL   C CA    1 
ATOM   12387 C  C     . VAL   C 2 56  ? 116.153 109.156 119.653 1.00 75.04  ?  55   VAL   C C     1 
ATOM   12388 O  O     . VAL   C 2 56  ? 116.654 108.323 118.907 1.00 77.58  ?  55   VAL   C O     1 
ATOM   12389 C  CB    . VAL   C 2 56  ? 114.988 110.211 117.668 1.00 66.09  ?  55   VAL   C CB    1 
ATOM   12390 C  CG1   . VAL   C 2 56  ? 113.635 110.700 117.174 1.00 64.63  ?  55   VAL   C CG1   1 
ATOM   12391 C  CG2   . VAL   C 2 56  ? 116.077 111.204 117.306 1.00 68.53  ?  55   VAL   C CG2   1 
ATOM   12392 N  N     . SER   C 2 57  ? 116.625 109.382 120.881 1.00 84.09  ?  56   SER   C N     1 
ATOM   12393 C  CA    . SER   C 2 57  ? 117.787 108.648 121.374 1.00 83.22  ?  56   SER   C CA    1 
ATOM   12394 C  C     . SER   C 2 57  ? 117.491 107.158 121.503 1.00 87.01  ?  56   SER   C C     1 
ATOM   12395 O  O     . SER   C 2 57  ? 118.326 106.318 121.145 1.00 88.55  ?  56   SER   C O     1 
ATOM   12396 C  CB    . SER   C 2 57  ? 118.239 109.223 122.714 1.00 80.62  ?  56   SER   C CB    1 
ATOM   12397 O  OG    . SER   C 2 57  ? 117.134 109.689 123.471 1.00 86.05  ?  56   SER   C OG    1 
ATOM   12398 N  N     . ARG   C 2 58  ? 116.307 106.811 122.007 1.00 89.41  ?  57   ARG   C N     1 
ATOM   12399 C  CA    . ARG   C 2 58  ? 115.927 105.410 122.148 1.00 86.73  ?  57   ARG   C CA    1 
ATOM   12400 C  C     . ARG   C 2 58  ? 115.703 104.729 120.806 1.00 89.40  ?  57   ARG   C C     1 
ATOM   12401 O  O     . ARG   C 2 58  ? 115.769 103.497 120.730 1.00 93.64  ?  57   ARG   C O     1 
ATOM   12402 C  CB    . ARG   C 2 58  ? 114.661 105.296 122.996 1.00 88.08  ?  57   ARG   C CB    1 
ATOM   12403 C  CG    . ARG   C 2 58  ? 114.913 104.998 124.455 1.00 89.09  ?  57   ARG   C CG    1 
ATOM   12404 C  CD    . ARG   C 2 58  ? 115.196 103.519 124.670 1.00 93.01  ?  57   ARG   C CD    1 
ATOM   12405 N  NE    . ARG   C 2 58  ? 113.990 102.728 124.880 1.00 96.41  ?  57   ARG   C NE    1 
ATOM   12406 C  CZ    . ARG   C 2 58  ? 113.127 102.899 125.874 1.00 96.53  ?  57   ARG   C CZ    1 
ATOM   12407 N  NH1   . ARG   C 2 58  ? 113.302 103.832 126.796 1.00 94.74  ?  57   ARG   C NH1   1 
ATOM   12408 N  NH2   . ARG   C 2 58  ? 112.057 102.113 125.943 1.00 93.27  ?  57   ARG   C NH2   1 
ATOM   12409 N  N     . ASP   C 2 59  ? 115.423 105.503 119.755 1.00 87.08  ?  58   ASP   C N     1 
ATOM   12410 C  CA    . ASP   C 2 59  ? 115.132 104.926 118.446 1.00 81.22  ?  58   ASP   C CA    1 
ATOM   12411 C  C     . ASP   C 2 59  ? 116.339 104.197 117.894 1.00 85.59  ?  58   ASP   C C     1 
ATOM   12412 O  O     . ASP   C 2 59  ? 116.219 103.091 117.348 1.00 91.52  ?  58   ASP   C O     1 
ATOM   12413 C  CB    . ASP   C 2 59  ? 114.696 106.024 117.485 1.00 87.04  ?  58   ASP   C CB    1 
ATOM   12414 C  CG    . ASP   C 2 59  ? 113.268 106.445 117.699 1.00 95.96  ?  58   ASP   C CG    1 
ATOM   12415 O  OD1   . ASP   C 2 59  ? 112.437 105.579 118.017 1.00 99.52  ?  58   ASP   C OD1   1 
ATOM   12416 O  OD2   . ASP   C 2 59  ? 112.973 107.643 117.538 1.00 100.32 ?  58   ASP   C OD2   1 
ATOM   12417 N  N     . ARG   C 2 60  ? 117.522 104.808 118.006 1.00 71.72  ?  59   ARG   C N     1 
ATOM   12418 C  CA    A ARG   C 2 60  ? 118.777 104.122 117.641 0.18 72.70  ?  59   ARG   C CA    1 
ATOM   12419 C  CA    B ARG   C 2 60  ? 118.793 104.161 117.644 0.32 72.44  ?  59   ARG   C CA    1 
ATOM   12420 C  CA    C ARG   C 2 60  ? 118.877 104.122 117.641 0.50 72.70  ?  59   ARG   C CA    1 
ATOM   12421 C  C     . ARG   C 2 60  ? 119.007 102.773 118.396 1.00 76.17  ?  59   ARG   C C     1 
ATOM   12422 O  O     . ARG   C 2 60  ? 119.288 101.650 117.801 1.00 81.89  ?  59   ARG   C O     1 
ATOM   12423 C  CB    A ARG   C 2 60  ? 119.937 105.052 117.974 0.18 72.49  ?  59   ARG   C CB    1 
ATOM   12424 C  CB    B ARG   C 2 60  ? 119.916 105.173 117.951 0.32 72.08  ?  59   ARG   C CB    1 
ATOM   12425 C  CB    C ARG   C 2 60  ? 120.037 105.052 117.974 0.50 72.49  ?  59   ARG   C CB    1 
ATOM   12426 C  CG    A ARG   C 2 60  ? 121.084 105.014 116.984 0.18 74.67  ?  59   ARG   C CG    1 
ATOM   12427 C  CG    B ARG   C 2 60  ? 121.139 104.989 117.083 0.32 74.68  ?  59   ARG   C CG    1 
ATOM   12428 C  CG    C ARG   C 2 60  ? 121.408 104.500 117.639 0.50 74.67  ?  59   ARG   C CG    1 
ATOM   12429 C  CD    A ARG   C 2 60  ? 121.905 106.283 117.128 0.18 76.52  ?  59   ARG   C CD    1 
ATOM   12430 C  CD    B ARG   C 2 60  ? 122.051 106.180 117.231 0.32 76.41  ?  59   ARG   C CD    1 
ATOM   12431 C  CD    C ARG   C 2 60  ? 122.456 105.553 117.951 0.50 76.52  ?  59   ARG   C CD    1 
ATOM   12432 N  NE    A ARG   C 2 60  ? 121.048 107.436 117.400 0.18 77.29  ?  59   ARG   C NE    1 
ATOM   12433 N  NE    B ARG   C 2 60  ? 123.441 105.827 116.978 0.32 74.13  ?  59   ARG   C NE    1 
ATOM   12434 N  NE    C ARG   C 2 60  ? 122.507 105.835 119.385 0.50 77.29  ?  59   ARG   C NE    1 
ATOM   12435 C  CZ    A ARG   C 2 60  ? 121.079 108.134 118.524 0.18 75.74  ?  59   ARG   C CZ    1 
ATOM   12436 C  CZ    B ARG   C 2 60  ? 123.984 105.773 115.772 0.32 75.38  ?  59   ARG   C CZ    1 
ATOM   12437 C  CZ    C ARG   C 2 60  ? 123.183 105.107 120.260 0.50 75.74  ?  59   ARG   C CZ    1 
ATOM   12438 N  NH1   A ARG   C 2 60  ? 122.047 107.969 119.402 0.18 74.85  ?  59   ARG   C NH1   1 
ATOM   12439 N  NH1   B ARG   C 2 60  ? 123.281 106.044 114.689 0.32 72.05  ?  59   ARG   C NH1   1 
ATOM   12440 N  NH1   C ARG   C 2 60  ? 124.044 104.192 119.865 0.50 74.85  ?  59   ARG   C NH1   1 
ATOM   12441 N  NH2   A ARG   C 2 60  ? 120.108 109.013 118.775 0.18 73.10  ?  59   ARG   C NH2   1 
ATOM   12442 N  NH2   B ARG   C 2 60  ? 125.265 105.440 115.653 0.32 77.24  ?  59   ARG   C NH2   1 
ATOM   12443 N  NH2   C ARG   C 2 60  ? 122.982 105.299 121.564 0.50 73.10  ?  59   ARG   C NH2   1 
ATOM   12444 N  N     . ILE   C 2 61  ? 118.822 102.796 119.672 1.00 68.31  ?  60   ILE   C N     1 
ATOM   12445 C  CA    . ILE   C 2 61  ? 119.020 101.586 120.445 1.00 70.23  ?  60   ILE   C CA    1 
ATOM   12446 C  C     . ILE   C 2 61  ? 118.021 100.512 120.035 1.00 71.35  ?  60   ILE   C C     1 
ATOM   12447 O  O     . ILE   C 2 61  ? 118.374 99.335  119.891 1.00 78.03  ?  60   ILE   C O     1 
ATOM   12448 C  CB    . ILE   C 2 61  ? 118.931 101.908 121.944 1.00 67.82  ?  60   ILE   C CB    1 
ATOM   12449 C  CG1   . ILE   C 2 61  ? 120.029 102.901 122.333 1.00 69.98  ?  60   ILE   C CG1   1 
ATOM   12450 C  CG2   . ILE   C 2 61  ? 119.025 100.640 122.775 1.00 67.69  ?  60   ILE   C CG2   1 
ATOM   12451 C  CD1   . ILE   C 2 61  ? 119.670 103.788 123.501 1.00 72.85  ?  60   ILE   C CD1   1 
ATOM   12452 N  N     . ASP   C 2 62  ? 116.763 100.899 119.834 1.00 72.02  ?  61   ASP   C N     1 
ATOM   12453 C  CA    . ASP   C 2 62  ? 115.750 99.931  119.437 1.00 71.28  ?  61   ASP   C CA    1 
ATOM   12454 C  C     . ASP   C 2 62  ? 115.984 99.408  118.026 1.00 74.34  ?  61   ASP   C C     1 
ATOM   12455 O  O     . ASP   C 2 62  ? 115.686 98.241  117.749 1.00 80.40  ?  61   ASP   C O     1 
ATOM   12456 C  CB    . ASP   C 2 62  ? 114.360 100.552 119.553 1.00 76.86  ?  61   ASP   C CB    1 
ATOM   12457 C  CG    . ASP   C 2 62  ? 113.834 100.542 120.973 1.00 85.09  ?  61   ASP   C CG    1 
ATOM   12458 O  OD1   . ASP   C 2 62  ? 114.520 99.995  121.858 1.00 85.75  ?  61   ASP   C OD1   1 
ATOM   12459 O  OD2   . ASP   C 2 62  ? 112.732 101.081 121.204 1.00 86.97  ?  61   ASP   C OD2   1 
ATOM   12460 N  N     . TYR   C 2 63  ? 116.513 100.245 117.128 1.00 63.52  ?  62   TYR   C N     1 
ATOM   12461 C  CA    . TYR   C 2 63  ? 116.736 99.816  115.754 1.00 58.50  ?  62   TYR   C CA    1 
ATOM   12462 C  C     . TYR   C 2 63  ? 117.925 98.872  115.652 1.00 67.85  ?  62   TYR   C C     1 
ATOM   12463 O  O     . TYR   C 2 63  ? 117.864 97.868  114.935 1.00 75.29  ?  62   TYR   C O     1 
ATOM   12464 C  CB    . TYR   C 2 63  ? 116.940 101.031 114.851 1.00 60.64  ?  62   TYR   C CB    1 
ATOM   12465 C  CG    . TYR   C 2 63  ? 117.223 100.671 113.412 1.00 65.35  ?  62   TYR   C CG    1 
ATOM   12466 C  CD1   . TYR   C 2 63  ? 116.200 100.275 112.563 1.00 62.52  ?  62   TYR   C CD1   1 
ATOM   12467 C  CD2   . TYR   C 2 63  ? 118.513 100.722 112.904 1.00 66.05  ?  62   TYR   C CD2   1 
ATOM   12468 C  CE1   . TYR   C 2 63  ? 116.452 99.943  111.249 1.00 62.30  ?  62   TYR   C CE1   1 
ATOM   12469 C  CE2   . TYR   C 2 63  ? 118.775 100.390 111.591 1.00 61.50  ?  62   TYR   C CE2   1 
ATOM   12470 C  CZ    . TYR   C 2 63  ? 117.742 100.001 110.768 1.00 67.71  ?  62   TYR   C CZ    1 
ATOM   12471 O  OH    . TYR   C 2 63  ? 118.000 99.671  109.458 1.00 72.94  ?  62   TYR   C OH    1 
ATOM   12472 N  N     . GLN   C 2 64  ? 119.018 99.173  116.356 1.00 76.09  ?  63   GLN   C N     1 
ATOM   12473 C  CA    . GLN   C 2 64  ? 120.191 98.311  116.288 1.00 71.40  ?  63   GLN   C CA    1 
ATOM   12474 C  C     . GLN   C 2 64  ? 119.942 96.942  116.909 1.00 74.78  ?  63   GLN   C C     1 
ATOM   12475 O  O     . GLN   C 2 64  ? 120.684 95.999  116.613 1.00 77.33  ?  63   GLN   C O     1 
ATOM   12476 C  CB    . GLN   C 2 64  ? 121.385 98.980  116.966 1.00 69.38  ?  63   GLN   C CB    1 
ATOM   12477 C  CG    . GLN   C 2 64  ? 121.777 100.320 116.367 1.00 74.54  ?  63   GLN   C CG    1 
ATOM   12478 C  CD    . GLN   C 2 64  ? 122.184 100.226 114.912 1.00 85.98  ?  63   GLN   C CD    1 
ATOM   12479 O  OE1   . GLN   C 2 64  ? 122.685 99.197  114.461 1.00 85.85  ?  63   GLN   C OE1   1 
ATOM   12480 N  NE2   . GLN   C 2 64  ? 121.978 101.309 114.169 1.00 82.50  ?  63   GLN   C NE2   1 
ATOM   12481 N  N     . ALA   C 2 65  ? 118.919 96.808  117.749 1.00 71.02  ?  64   ALA   C N     1 
ATOM   12482 C  CA    . ALA   C 2 65  ? 118.582 95.537  118.372 1.00 68.91  ?  64   ALA   C CA    1 
ATOM   12483 C  C     . ALA   C 2 65  ? 117.575 94.730  117.564 1.00 69.57  ?  64   ALA   C C     1 
ATOM   12484 O  O     . ALA   C 2 65  ? 117.188 93.639  117.994 1.00 71.76  ?  64   ALA   C O     1 
ATOM   12485 C  CB    . ALA   C 2 65  ? 118.038 95.768  119.786 1.00 68.10  ?  64   ALA   C CB    1 
ATOM   12486 N  N     . LEU   C 2 66  ? 117.143 95.235  116.414 1.00 70.25  ?  65   LEU   C N     1 
ATOM   12487 C  CA    . LEU   C 2 66  ? 116.160 94.555  115.590 1.00 63.15  ?  65   LEU   C CA    1 
ATOM   12488 C  C     . LEU   C 2 66  ? 116.815 93.457  114.754 1.00 66.11  ?  65   LEU   C C     1 
ATOM   12489 O  O     . LEU   C 2 66  ? 117.990 93.559  114.392 1.00 74.22  ?  65   LEU   C O     1 
ATOM   12490 C  CB    . LEU   C 2 66  ? 115.467 95.549  114.665 1.00 61.79  ?  65   LEU   C CB    1 
ATOM   12491 C  CG    . LEU   C 2 66  ? 114.390 96.462  115.252 1.00 61.83  ?  65   LEU   C CG    1 
ATOM   12492 C  CD1   . LEU   C 2 66  ? 113.687 97.227  114.144 1.00 65.18  ?  65   LEU   C CD1   1 
ATOM   12493 C  CD2   . LEU   C 2 66  ? 113.391 95.668  116.074 1.00 67.95  ?  65   LEU   C CD2   1 
ATOM   12494 N  N     . PRO   C 2 67  ? 116.075 92.398  114.434 1.00 72.56  ?  66   PRO   C N     1 
ATOM   12495 C  CA    . PRO   C 2 67  ? 116.570 91.428  113.455 1.00 75.14  ?  66   PRO   C CA    1 
ATOM   12496 C  C     . PRO   C 2 67  ? 116.602 92.033  112.060 1.00 81.34  ?  66   PRO   C C     1 
ATOM   12497 O  O     . PRO   C 2 67  ? 115.947 93.036  111.772 1.00 91.32  ?  66   PRO   C O     1 
ATOM   12498 C  CB    . PRO   C 2 67  ? 115.558 90.280  113.542 1.00 75.53  ?  66   PRO   C CB    1 
ATOM   12499 C  CG    . PRO   C 2 67  ? 114.326 90.902  114.092 1.00 76.14  ?  66   PRO   C CG    1 
ATOM   12500 C  CD    . PRO   C 2 67  ? 114.788 91.987  115.019 1.00 72.93  ?  66   PRO   C CD    1 
ATOM   12501 N  N     . GLU   C 2 68  ? 117.336 91.362  111.170 1.00 85.73  ?  67   GLU   C N     1 
ATOM   12502 C  CA    . GLU   C 2 68  ? 117.662 91.949  109.869 1.00 85.30  ?  67   GLU   C CA    1 
ATOM   12503 C  C     . GLU   C 2 68  ? 116.416 92.225  109.054 1.00 86.72  ?  67   GLU   C C     1 
ATOM   12504 O  O     . GLU   C 2 68  ? 116.312 93.260  108.376 1.00 86.67  ?  67   GLU   C O     1 
ATOM   12505 C  CB    . GLU   C 2 68  ? 118.602 91.021  109.103 1.00 86.58  ?  67   GLU   C CB    1 
ATOM   12506 C  CG    . GLU   C 2 68  ? 120.064 91.165  109.496 1.00 90.19  ?  67   GLU   C CG    1 
ATOM   12507 C  CD    . GLU   C 2 68  ? 120.470 92.609  109.726 1.00 94.19  ?  67   GLU   C CD    1 
ATOM   12508 O  OE1   . GLU   C 2 68  ? 120.364 93.417  108.780 1.00 93.20  ?  67   GLU   C OE1   1 
ATOM   12509 O  OE2   . GLU   C 2 68  ? 120.898 92.936  110.853 1.00 94.71  ?  67   GLU   C OE2   1 
ATOM   12510 N  N     . HIS   C 2 69  ? 115.460 91.308  109.142 1.00 84.34  ?  68   HIS   C N     1 
ATOM   12511 C  CA    . HIS   C 2 69  ? 114.245 91.374  108.369 1.00 83.01  ?  68   HIS   C CA    1 
ATOM   12512 C  C     . HIS   C 2 69  ? 113.401 92.569  108.749 1.00 88.11  ?  68   HIS   C C     1 
ATOM   12513 O  O     . HIS   C 2 69  ? 112.905 93.257  107.866 1.00 93.06  ?  68   HIS   C O     1 
ATOM   12514 C  CB    . HIS   C 2 69  ? 113.541 90.015  108.457 1.00 81.01  ?  68   HIS   C CB    1 
ATOM   12515 C  CG    . HIS   C 2 69  ? 112.825 89.694  109.722 1.00 85.63  ?  68   HIS   C CG    1 
ATOM   12516 N  ND1   . HIS   C 2 69  ? 113.436 89.050  110.772 1.00 88.20  ?  68   HIS   C ND1   1 
ATOM   12517 C  CD2   . HIS   C 2 69  ? 111.508 89.737  110.018 1.00 86.69  ?  68   HIS   C CD2   1 
ATOM   12518 C  CE1   . HIS   C 2 69  ? 112.541 88.809  111.710 1.00 88.63  ?  68   HIS   C CE1   1 
ATOM   12519 N  NE2   . HIS   C 2 69  ? 111.361 89.201  111.271 1.00 88.31  ?  68   HIS   C NE2   1 
ATOM   12520 N  N     . GLU   C 2 70  ? 113.288 92.875  110.036 1.00 82.49  ?  69   GLU   C N     1 
ATOM   12521 C  CA    . GLU   C 2 70  ? 112.539 94.033  110.516 1.00 78.90  ?  69   GLU   C CA    1 
ATOM   12522 C  C     . GLU   C 2 70  ? 113.227 95.343  110.148 1.00 79.87  ?  69   GLU   C C     1 
ATOM   12523 O  O     . GLU   C 2 70  ? 112.562 96.323  109.781 1.00 87.13  ?  69   GLU   C O     1 
ATOM   12524 C  CB    . GLU   C 2 70  ? 112.364 93.914  112.031 1.00 74.18  ?  69   GLU   C CB    1 
ATOM   12525 C  CG    . GLU   C 2 70  ? 111.131 93.126  112.442 1.00 82.58  ?  69   GLU   C CG    1 
ATOM   12526 C  CD    . GLU   C 2 70  ? 111.260 92.502  113.816 1.00 93.12  ?  69   GLU   C CD    1 
ATOM   12527 O  OE1   . GLU   C 2 70  ? 111.787 93.171  114.727 1.00 97.63  ?  69   GLU   C OE1   1 
ATOM   12528 O  OE2   . GLU   C 2 70  ? 110.836 91.340  113.986 1.00 94.45  ?  69   GLU   C OE2   1 
ATOM   12529 N  N     . LYS   C 2 71  ? 114.559 95.376  110.239 1.00 57.28  ?  70   LYS   C N     1 
ATOM   12530 C  CA    . LYS   C 2 71  ? 115.302 96.544  109.782 1.00 60.64  ?  70   LYS   C CA    1 
ATOM   12531 C  C     . LYS   C 2 71  ? 115.065 96.788  108.301 1.00 64.78  ?  70   LYS   C C     1 
ATOM   12532 O  O     . LYS   C 2 71  ? 114.919 97.937  107.868 1.00 71.89  ?  70   LYS   C O     1 
ATOM   12533 C  CB    . LYS   C 2 71  ? 116.795 96.363  110.053 1.00 53.97  ?  70   LYS   C CB    1 
ATOM   12534 C  CG    . LYS   C 2 71  ? 117.147 96.081  111.497 1.00 60.50  ?  70   LYS   C CG    1 
ATOM   12535 C  CD    . LYS   C 2 71  ? 118.573 95.575  111.617 1.00 61.15  ?  70   LYS   C CD    1 
ATOM   12536 C  CE    . LYS   C 2 71  ? 119.536 96.707  111.912 1.00 60.77  ?  70   LYS   C CE    1 
ATOM   12537 N  NZ    . LYS   C 2 71  ? 120.357 96.425  113.118 1.00 62.25  ?  70   LYS   C NZ    1 
ATOM   12538 N  N     . HIS   C 2 72  ? 114.966 95.707  107.532 1.00 66.67  ?  71   HIS   C N     1 
ATOM   12539 C  CA    A HIS   C 2 72  ? 114.738 95.826  106.072 0.50 64.77  ?  71   HIS   C CA    1 
ATOM   12540 C  CA    B HIS   C 2 72  ? 114.838 95.826  106.072 0.50 64.77  ?  71   HIS   C CA    1 
ATOM   12541 C  C     . HIS   C 2 72  ? 113.369 96.452  105.843 1.00 68.50  ?  71   HIS   C C     1 
ATOM   12542 O  O     . HIS   C 2 72  ? 113.257 97.329  104.986 1.00 73.33  ?  71   HIS   C O     1 
ATOM   12543 C  CB    A HIS   C 2 72  ? 114.839 94.460  105.389 0.50 65.61  ?  71   HIS   C CB    1 
ATOM   12544 C  CB    B HIS   C 2 72  ? 114.939 94.460  105.389 0.50 65.61  ?  71   HIS   C CB    1 
ATOM   12545 C  CG    A HIS   C 2 72  ? 113.906 94.275  104.239 0.50 67.49  ?  71   HIS   C CG    1 
ATOM   12546 C  CG    B HIS   C 2 72  ? 114.865 94.508  103.899 0.50 67.49  ?  71   HIS   C CG    1 
ATOM   12547 N  ND1   A HIS   C 2 72  ? 114.164 94.783  102.983 0.50 70.67  ?  71   HIS   C ND1   1 
ATOM   12548 N  ND1   B HIS   C 2 72  ? 115.795 95.174  103.129 0.50 70.67  ?  71   HIS   C ND1   1 
ATOM   12549 C  CD2   A HIS   C 2 72  ? 112.724 93.634  104.148 0.50 70.22  ?  71   HIS   C CD2   1 
ATOM   12550 C  CD2   B HIS   C 2 72  ? 113.981 93.970  103.036 0.50 70.22  ?  71   HIS   C CD2   1 
ATOM   12551 C  CE1   A HIS   C 2 72  ? 113.182 94.463  102.168 0.50 72.91  ?  71   HIS   C CE1   1 
ATOM   12552 C  CE1   B HIS   C 2 72  ? 115.489 95.044  101.857 0.50 72.91  ?  71   HIS   C CE1   1 
ATOM   12553 N  NE2   A HIS   C 2 72  ? 112.287 93.762  102.859 0.50 74.53  ?  71   HIS   C NE2   1 
ATOM   12554 N  NE2   B HIS   C 2 72  ? 114.380 94.313  101.774 0.50 74.53  ?  71   HIS   C NE2   1 
ATOM   12555 N  N     . ILE   C 2 73  ? 112.371 95.991  106.578 1.00 60.27  ?  72   ILE   C N     1 
ATOM   12556 C  CA    . ILE   C 2 73  ? 111.019 96.530  106.413 1.00 63.51  ?  72   ILE   C CA    1 
ATOM   12557 C  C     . ILE   C 2 73  ? 110.994 98.022  106.731 1.00 68.96  ?  72   ILE   C C     1 
ATOM   12558 O  O     . ILE   C 2 73  ? 110.495 98.842  105.942 1.00 79.85  ?  72   ILE   C O     1 
ATOM   12559 C  CB    . ILE   C 2 73  ? 110.026 95.756  107.298 1.00 57.76  ?  72   ILE   C CB    1 
ATOM   12560 C  CG1   . ILE   C 2 73  ? 109.953 94.288  106.878 1.00 67.64  ?  72   ILE   C CG1   1 
ATOM   12561 C  CG2   . ILE   C 2 73  ? 108.651 96.401  107.256 1.00 60.22  ?  72   ILE   C CG2   1 
ATOM   12562 C  CD1   . ILE   C 2 73  ? 109.551 93.353  108.000 1.00 66.86  ?  72   ILE   C CD1   1 
ATOM   12563 N  N     . PHE   C 2 74  ? 111.546 98.393  107.890 1.00 54.53  ?  73   PHE   C N     1 
ATOM   12564 C  CA    . PHE   C 2 74  ? 111.515 99.790  108.314 1.00 50.41  ?  73   PHE   C CA    1 
ATOM   12565 C  C     . PHE   C 2 74  ? 112.262 100.681 107.327 1.00 56.18  ?  73   PHE   C C     1 
ATOM   12566 O  O     . PHE   C 2 74  ? 111.752 101.728 106.907 1.00 63.52  ?  73   PHE   C O     1 
ATOM   12567 C  CB    . PHE   C 2 74  ? 112.101 99.918  109.724 1.00 49.02  ?  73   PHE   C CB    1 
ATOM   12568 C  CG    . PHE   C 2 74  ? 111.700 101.180 110.438 1.00 59.74  ?  73   PHE   C CG    1 
ATOM   12569 C  CD1   . PHE   C 2 74  ? 110.405 101.352 110.897 1.00 65.98  ?  73   PHE   C CD1   1 
ATOM   12570 C  CD2   . PHE   C 2 74  ? 112.607 102.211 110.612 1.00 51.02  ?  73   PHE   C CD2   1 
ATOM   12571 C  CE1   . PHE   C 2 74  ? 110.033 102.515 111.542 1.00 63.17  ?  73   PHE   C CE1   1 
ATOM   12572 C  CE2   . PHE   C 2 74  ? 112.245 103.367 111.268 1.00 51.81  ?  73   PHE   C CE2   1 
ATOM   12573 C  CZ    . PHE   C 2 74  ? 110.956 103.523 111.730 1.00 58.97  ?  73   PHE   C CZ    1 
ATOM   12574 N  N     . ILE   C 2 75  ? 113.468 100.269 106.926 1.00 52.12  ?  74   ILE   C N     1 
ATOM   12575 C  CA    . ILE   C 2 75  ? 114.275 101.107 106.049 1.00 52.53  ?  74   ILE   C CA    1 
ATOM   12576 C  C     . ILE   C 2 75  ? 113.668 101.187 104.652 1.00 61.50  ?  74   ILE   C C     1 
ATOM   12577 O  O     . ILE   C 2 75  ? 113.758 102.229 103.996 1.00 68.43  ?  74   ILE   C O     1 
ATOM   12578 C  CB    . ILE   C 2 75  ? 115.736 100.613 106.028 1.00 54.22  ?  74   ILE   C CB    1 
ATOM   12579 C  CG1   . ILE   C 2 75  ? 116.695 101.804 106.001 1.00 55.90  ?  74   ILE   C CG1   1 
ATOM   12580 C  CG2   . ILE   C 2 75  ? 116.003 99.685  104.852 1.00 62.08  ?  74   ILE   C CG2   1 
ATOM   12581 C  CD1   . ILE   C 2 75  ? 116.710 102.603 107.284 1.00 54.16  ?  74   ILE   C CD1   1 
ATOM   12582 N  N     . SER   C 2 76  ? 113.017 100.119 104.180 1.00 54.73  ?  75   SER   C N     1 
ATOM   12583 C  CA    . SER   C 2 76  ? 112.388 100.169 102.865 1.00 54.43  ?  75   SER   C CA    1 
ATOM   12584 C  C     . SER   C 2 76  ? 111.200 101.119 102.862 1.00 57.81  ?  75   SER   C C     1 
ATOM   12585 O  O     . SER   C 2 76  ? 111.038 101.920 101.929 1.00 63.20  ?  75   SER   C O     1 
ATOM   12586 C  CB    . SER   C 2 76  ? 111.959 98.768  102.437 1.00 50.89  ?  75   SER   C CB    1 
ATOM   12587 O  OG    . SER   C 2 76  ? 113.069 97.892  102.372 1.00 62.38  ?  75   SER   C OG    1 
ATOM   12588 N  N     . ASN   C 2 77  ? 110.369 101.060 103.905 1.00 62.84  ?  76   ASN   C N     1 
ATOM   12589 C  CA    . ASN   C 2 77  ? 109.263 102.006 103.999 1.00 51.94  ?  76   ASN   C CA    1 
ATOM   12590 C  C     . ASN   C 2 77  ? 109.771 103.439 104.081 1.00 57.61  ?  76   ASN   C C     1 
ATOM   12591 O  O     . ASN   C 2 77  ? 109.239 104.331 103.408 1.00 68.94  ?  76   ASN   C O     1 
ATOM   12592 C  CB    . ASN   C 2 77  ? 108.383 101.670 105.198 1.00 53.04  ?  76   ASN   C CB    1 
ATOM   12593 C  CG    . ASN   C 2 77  ? 107.399 100.563 104.900 1.00 58.14  ?  76   ASN   C CG    1 
ATOM   12594 O  OD1   . ASN   C 2 77  ? 106.446 100.748 104.144 1.00 67.76  ?  76   ASN   C OD1   1 
ATOM   12595 N  ND2   . ASN   C 2 77  ? 107.625 99.401  105.495 1.00 64.50  ?  76   ASN   C ND2   1 
ATOM   12596 N  N     . LEU   C 2 78  ? 110.825 103.671 104.869 1.00 59.64  ?  77   LEU   C N     1 
ATOM   12597 C  CA    . LEU   C 2 78  ? 111.379 105.016 104.983 1.00 56.12  ?  77   LEU   C CA    1 
ATOM   12598 C  C     . LEU   C 2 78  ? 111.931 105.512 103.653 1.00 57.19  ?  77   LEU   C C     1 
ATOM   12599 O  O     . LEU   C 2 78  ? 111.730 106.674 103.290 1.00 68.43  ?  77   LEU   C O     1 
ATOM   12600 C  CB    . LEU   C 2 78  ? 112.464 105.044 106.052 1.00 60.72  ?  77   LEU   C CB    1 
ATOM   12601 C  CG    . LEU   C 2 78  ? 112.074 105.554 107.434 1.00 58.58  ?  77   LEU   C CG    1 
ATOM   12602 C  CD1   . LEU   C 2 78  ? 110.720 104.995 107.812 1.00 58.32  ?  77   LEU   C CD1   1 
ATOM   12603 C  CD2   . LEU   C 2 78  ? 113.125 105.175 108.459 1.00 63.92  ?  77   LEU   C CD2   1 
ATOM   12604 N  N     . LYS   C 2 79  ? 112.627 104.645 102.912 1.00 55.91  ?  78   LYS   C N     1 
ATOM   12605 C  CA    . LYS   C 2 79  ? 113.192 105.041 101.627 1.00 53.64  ?  78   LYS   C CA    1 
ATOM   12606 C  C     . LYS   C 2 79  ? 112.099 105.384 100.623 1.00 52.14  ?  78   LYS   C C     1 
ATOM   12607 O  O     . LYS   C 2 79  ? 112.184 106.403 99.919  1.00 59.14  ?  78   LYS   C O     1 
ATOM   12608 C  CB    . LYS   C 2 79  ? 114.095 103.925 101.103 1.00 55.03  ?  78   LYS   C CB    1 
ATOM   12609 C  CG    . LYS   C 2 79  ? 115.505 104.007 101.657 1.00 60.05  ?  78   LYS   C CG    1 
ATOM   12610 C  CD    . LYS   C 2 79  ? 116.409 102.961 101.013 1.00 59.34  ?  78   LYS   C CD    1 
ATOM   12611 C  CE    . LYS   C 2 79  ? 115.840 101.556 101.138 1.00 57.98  ?  78   LYS   C CE    1 
ATOM   12612 N  NZ    . LYS   C 2 79  ? 116.734 100.543 100.512 1.00 61.69  ?  78   LYS   C NZ    1 
ATOM   12613 N  N     . TYR   C 2 80  ? 111.056 104.554 100.551 1.00 52.95  ?  79   TYR   C N     1 
ATOM   12614 C  CA    . TYR   C 2 80  ? 109.961 104.847 99.635  1.00 54.59  ?  79   TYR   C CA    1 
ATOM   12615 C  C     . TYR   C 2 80  ? 109.278 106.158 99.998  1.00 58.88  ?  79   TYR   C C     1 
ATOM   12616 O  O     . TYR   C 2 80  ? 108.981 106.976 99.118  1.00 65.68  ?  79   TYR   C O     1 
ATOM   12617 C  CB    . TYR   C 2 80  ? 108.943 103.709 99.630  1.00 54.83  ?  79   TYR   C CB    1 
ATOM   12618 C  CG    . TYR   C 2 80  ? 107.741 104.007 98.762  1.00 61.92  ?  79   TYR   C CG    1 
ATOM   12619 C  CD1   . TYR   C 2 80  ? 107.785 103.802 97.392  1.00 63.64  ?  79   TYR   C CD1   1 
ATOM   12620 C  CD2   . TYR   C 2 80  ? 106.572 104.519 99.308  1.00 64.70  ?  79   TYR   C CD2   1 
ATOM   12621 C  CE1   . TYR   C 2 80  ? 106.696 104.077 96.593  1.00 67.36  ?  79   TYR   C CE1   1 
ATOM   12622 C  CE2   . TYR   C 2 80  ? 105.479 104.805 98.515  1.00 62.83  ?  79   TYR   C CE2   1 
ATOM   12623 C  CZ    . TYR   C 2 80  ? 105.546 104.580 97.159  1.00 67.08  ?  79   TYR   C CZ    1 
ATOM   12624 O  OH    . TYR   C 2 80  ? 104.459 104.860 96.365  1.00 72.30  ?  79   TYR   C OH    1 
ATOM   12625 N  N     . GLN   C 2 81  ? 109.015 106.372 101.289 1.00 56.54  ?  80   GLN   C N     1 
ATOM   12626 C  CA    . GLN   C 2 81  ? 108.364 107.607 101.710 1.00 43.92  ?  80   GLN   C CA    1 
ATOM   12627 C  C     . GLN   C 2 81  ? 109.235 108.819 101.408 1.00 49.12  ?  80   GLN   C C     1 
ATOM   12628 O  O     . GLN   C 2 81  ? 108.732 109.858 100.966 1.00 60.77  ?  80   GLN   C O     1 
ATOM   12629 C  CB    . GLN   C 2 81  ? 108.028 107.534 103.196 1.00 47.18  ?  80   GLN   C CB    1 
ATOM   12630 C  CG    . GLN   C 2 81  ? 106.649 106.980 103.487 1.00 46.63  ?  80   GLN   C CG    1 
ATOM   12631 C  CD    . GLN   C 2 81  ? 106.521 106.445 104.896 1.00 60.48  ?  80   GLN   C CD    1 
ATOM   12632 O  OE1   . GLN   C 2 81  ? 105.727 106.945 105.689 1.00 66.39  ?  80   GLN   C OE1   1 
ATOM   12633 N  NE2   . GLN   C 2 81  ? 107.303 105.422 105.215 1.00 64.70  ?  80   GLN   C NE2   1 
ATOM   12634 N  N     . THR   C 2 82  ? 110.546 108.701 101.631 1.00 53.10  ?  81   THR   C N     1 
ATOM   12635 C  CA    . THR   C 2 82  ? 111.459 109.796 101.326 1.00 55.09  ?  81   THR   C CA    1 
ATOM   12636 C  C     . THR   C 2 82  ? 111.400 110.163 99.851  1.00 61.95  ?  81   THR   C C     1 
ATOM   12637 O  O     . THR   C 2 82  ? 111.258 111.339 99.498  1.00 70.33  ?  81   THR   C O     1 
ATOM   12638 C  CB    . THR   C 2 82  ? 112.887 109.414 101.721 1.00 57.41  ?  81   THR   C CB    1 
ATOM   12639 O  OG1   . THR   C 2 82  ? 112.902 108.927 103.068 1.00 67.87  ?  81   THR   C OG1   1 
ATOM   12640 C  CG2   . THR   C 2 82  ? 113.810 110.616 101.610 1.00 58.28  ?  81   THR   C CG2   1 
ATOM   12641 N  N     . LEU   C 2 83  ? 111.496 109.164 98.970  1.00 55.78  ?  82   LEU   C N     1 
ATOM   12642 C  CA    . LEU   C 2 83  ? 111.473 109.458 97.539  1.00 49.21  ?  82   LEU   C CA    1 
ATOM   12643 C  C     . LEU   C 2 83  ? 110.135 110.048 97.108  1.00 55.12  ?  82   LEU   C C     1 
ATOM   12644 O  O     . LEU   C 2 83  ? 110.092 111.050 96.378  1.00 63.80  ?  82   LEU   C O     1 
ATOM   12645 C  CB    . LEU   C 2 83  ? 111.789 108.202 96.732  1.00 53.49  ?  82   LEU   C CB    1 
ATOM   12646 C  CG    . LEU   C 2 83  ? 111.627 108.384 95.222  1.00 55.34  ?  82   LEU   C CG    1 
ATOM   12647 C  CD1   . LEU   C 2 83  ? 112.705 109.308 94.683  1.00 59.42  ?  82   LEU   C CD1   1 
ATOM   12648 C  CD2   . LEU   C 2 83  ? 111.655 107.052 94.496  1.00 56.58  ?  82   LEU   C CD2   1 
ATOM   12649 N  N     . LEU   C 2 84  ? 109.029 109.479 97.591  1.00 52.11  ?  83   LEU   C N     1 
ATOM   12650 C  CA    . LEU   C 2 84  ? 107.724 109.942 97.140  1.00 46.51  ?  83   LEU   C CA    1 
ATOM   12651 C  C     . LEU   C 2 84  ? 107.417 111.340 97.656  1.00 52.92  ?  83   LEU   C C     1 
ATOM   12652 O  O     . LEU   C 2 84  ? 106.801 112.139 96.947  1.00 61.12  ?  83   LEU   C O     1 
ATOM   12653 C  CB    . LEU   C 2 84  ? 106.642 108.954 97.556  1.00 54.98  ?  83   LEU   C CB    1 
ATOM   12654 C  CG    . LEU   C 2 84  ? 106.132 108.131 96.375  1.00 56.96  ?  83   LEU   C CG    1 
ATOM   12655 C  CD1   . LEU   C 2 84  ? 105.479 109.034 95.346  1.00 59.03  ?  83   LEU   C CD1   1 
ATOM   12656 C  CD2   . LEU   C 2 84  ? 107.280 107.370 95.748  1.00 54.72  ?  83   LEU   C CD2   1 
ATOM   12657 N  N     . ASP   C 2 85  ? 107.851 111.672 98.872  1.00 52.70  ?  84   ASP   C N     1 
ATOM   12658 C  CA    . ASP   C 2 85  ? 107.613 113.025 99.351  1.00 47.20  ?  84   ASP   C CA    1 
ATOM   12659 C  C     . ASP   C 2 85  ? 108.594 114.023 98.752  1.00 56.35  ?  84   ASP   C C     1 
ATOM   12660 O  O     . ASP   C 2 85  ? 108.257 115.204 98.628  1.00 66.26  ?  84   ASP   C O     1 
ATOM   12661 C  CB    . ASP   C 2 85  ? 107.644 113.060 100.877 1.00 49.63  ?  84   ASP   C CB    1 
ATOM   12662 C  CG    . ASP   C 2 85  ? 106.257 112.953 101.475 1.00 61.94  ?  84   ASP   C CG    1 
ATOM   12663 O  OD1   . ASP   C 2 85  ? 105.283 112.984 100.699 1.00 63.06  ?  84   ASP   C OD1   1 
ATOM   12664 O  OD2   . ASP   C 2 85  ? 106.131 112.833 102.709 1.00 65.85  ?  84   ASP   C OD2   1 
ATOM   12665 N  N     . SER   C 2 86  ? 109.781 113.573 98.334  1.00 56.14  ?  85   SER   C N     1 
ATOM   12666 C  CA    . SER   C 2 86  ? 110.634 114.430 97.520  1.00 54.69  ?  85   SER   C CA    1 
ATOM   12667 C  C     . SER   C 2 86  ? 109.951 114.774 96.204  1.00 60.39  ?  85   SER   C C     1 
ATOM   12668 O  O     . SER   C 2 86  ? 110.028 115.913 95.731  1.00 61.68  ?  85   SER   C O     1 
ATOM   12669 C  CB    . SER   C 2 86  ? 111.978 113.750 97.267  1.00 54.04  ?  85   SER   C CB    1 
ATOM   12670 O  OG    . SER   C 2 86  ? 112.466 113.129 98.442  1.00 64.30  ?  85   SER   C OG    1 
ATOM   12671 N  N     . ILE   C 2 87  ? 109.265 113.799 95.606  1.00 60.86  ?  86   ILE   C N     1 
ATOM   12672 C  CA    . ILE   C 2 87  ? 108.499 114.066 94.389  1.00 54.32  ?  86   ILE   C CA    1 
ATOM   12673 C  C     . ILE   C 2 87  ? 107.335 115.010 94.679  1.00 57.23  ?  86   ILE   C C     1 
ATOM   12674 O  O     . ILE   C 2 87  ? 107.112 115.984 93.947  1.00 64.45  ?  86   ILE   C O     1 
ATOM   12675 C  CB    . ILE   C 2 87  ? 108.014 112.747 93.764  1.00 54.27  ?  86   ILE   C CB    1 
ATOM   12676 C  CG1   . ILE   C 2 87  ? 109.179 111.987 93.128  1.00 54.77  ?  86   ILE   C CG1   1 
ATOM   12677 C  CG2   . ILE   C 2 87  ? 106.921 113.010 92.738  1.00 58.35  ?  86   ILE   C CG2   1 
ATOM   12678 C  CD1   . ILE   C 2 87  ? 108.930 110.502 92.998  1.00 58.44  ?  86   ILE   C CD1   1 
ATOM   12679 N  N     . GLN   C 2 88  ? 106.595 114.746 95.761  1.00 57.28  ?  87   GLN   C N     1 
ATOM   12680 C  CA    . GLN   C 2 88  ? 105.411 115.519 96.116  1.00 54.46  ?  87   GLN   C CA    1 
ATOM   12681 C  C     . GLN   C 2 88  ? 105.744 116.933 96.562  1.00 63.67  ?  87   GLN   C C     1 
ATOM   12682 O  O     . GLN   C 2 88  ? 104.854 117.787 96.577  1.00 69.81  ?  87   GLN   C O     1 
ATOM   12683 C  CB    . GLN   C 2 88  ? 104.637 114.809 97.225  1.00 57.10  ?  87   GLN   C CB    1 
ATOM   12684 C  CG    . GLN   C 2 88  ? 103.765 113.667 96.749  1.00 59.83  ?  87   GLN   C CG    1 
ATOM   12685 C  CD    . GLN   C 2 88  ? 102.556 114.145 95.976  1.00 65.93  ?  87   GLN   C CD    1 
ATOM   12686 O  OE1   . GLN   C 2 88  ? 102.542 114.121 94.746  1.00 73.72  ?  87   GLN   C OE1   1 
ATOM   12687 N  NE2   . GLN   C 2 88  ? 101.532 114.586 96.694  1.00 63.02  ?  87   GLN   C NE2   1 
ATOM   12688 N  N     . GLY   C 2 89  ? 106.984 117.195 96.966  1.00 63.86  ?  88   GLY   C N     1 
ATOM   12689 C  CA    . GLY   C 2 89  ? 107.364 118.563 97.262  1.00 55.54  ?  88   GLY   C CA    1 
ATOM   12690 C  C     . GLY   C 2 89  ? 107.366 119.440 96.026  1.00 63.68  ?  88   GLY   C C     1 
ATOM   12691 O  O     . GLY   C 2 89  ? 106.887 120.577 96.059  1.00 73.54  ?  88   GLY   C O     1 
ATOM   12692 N  N     . ARG   C 2 90  ? 107.899 118.928 94.920  1.00 65.13  ?  89   ARG   C N     1 
ATOM   12693 C  CA    . ARG   C 2 90  ? 108.083 119.723 93.717  1.00 62.23  ?  89   ARG   C CA    1 
ATOM   12694 C  C     . ARG   C 2 90  ? 106.945 119.591 92.718  1.00 65.80  ?  89   ARG   C C     1 
ATOM   12695 O  O     . ARG   C 2 90  ? 106.780 120.479 91.875  1.00 75.84  ?  89   ARG   C O     1 
ATOM   12696 C  CB    . ARG   C 2 90  ? 109.394 119.329 93.024  1.00 64.30  ?  89   ARG   C CB    1 
ATOM   12697 C  CG    . ARG   C 2 90  ? 109.418 117.880 92.571  1.00 69.42  ?  89   ARG   C CG    1 
ATOM   12698 C  CD    . ARG   C 2 90  ? 110.599 117.571 91.672  1.00 66.88  ?  89   ARG   C CD    1 
ATOM   12699 N  NE    . ARG   C 2 90  ? 111.817 117.430 92.456  1.00 71.23  ?  89   ARG   C NE    1 
ATOM   12700 C  CZ    . ARG   C 2 90  ? 112.173 116.307 93.061  1.00 68.85  ?  89   ARG   C CZ    1 
ATOM   12701 N  NH1   . ARG   C 2 90  ? 111.436 115.214 92.969  1.00 66.29  ?  89   ARG   C NH1   1 
ATOM   12702 N  NH2   . ARG   C 2 90  ? 113.294 116.279 93.775  1.00 70.15  ?  89   ARG   C NH2   1 
ATOM   12703 N  N     . SER   C 2 91  ? 106.154 118.517 92.791  1.00 66.01  ?  90   SER   C N     1 
ATOM   12704 C  CA    . SER   C 2 91  ? 105.226 118.233 91.698  1.00 63.39  ?  90   SER   C CA    1 
ATOM   12705 C  C     . SER   C 2 91  ? 104.014 119.158 91.677  1.00 69.12  ?  90   SER   C C     1 
ATOM   12706 O  O     . SER   C 2 91  ? 103.641 119.617 90.583  1.00 73.30  ?  90   SER   C O     1 
ATOM   12707 C  CB    . SER   C 2 91  ? 104.819 116.759 91.743  1.00 70.39  ?  90   SER   C CB    1 
ATOM   12708 O  OG    . SER   C 2 91  ? 105.879 115.924 91.312  1.00 78.37  ?  90   SER   C OG    1 
ATOM   12709 N  N     . PRO   C 2 92  ? 103.332 119.441 92.796  1.00 70.40  ?  91   PRO   C N     1 
ATOM   12710 C  CA    . PRO   C 2 92  ? 102.183 120.362 92.720  1.00 66.52  ?  91   PRO   C CA    1 
ATOM   12711 C  C     . PRO   C 2 92  ? 102.529 121.745 92.241  1.00 68.59  ?  91   PRO   C C     1 
ATOM   12712 O  O     . PRO   C 2 92  ? 101.735 122.394 91.551  1.00 78.57  ?  91   PRO   C O     1 
ATOM   12713 C  CB    . PRO   C 2 92  ? 101.666 120.384 94.163  1.00 68.27  ?  91   PRO   C CB    1 
ATOM   12714 C  CG    . PRO   C 2 92  ? 102.053 119.068 94.706  1.00 68.03  ?  91   PRO   C CG    1 
ATOM   12715 C  CD    . PRO   C 2 92  ? 103.401 118.789 94.114  1.00 66.88  ?  91   PRO   C CD    1 
ATOM   12716 N  N     . ASN   C 2 93  ? 103.689 122.220 92.621  1.00 68.21  ?  92   ASN   C N     1 
ATOM   12717 C  CA    . ASN   C 2 93  ? 104.053 123.545 92.236  1.00 63.43  ?  92   ASN   C CA    1 
ATOM   12718 C  C     . ASN   C 2 93  ? 104.274 123.651 90.733  1.00 69.24  ?  92   ASN   C C     1 
ATOM   12719 O  O     . ASN   C 2 93  ? 104.085 124.723 90.210  1.00 79.99  ?  92   ASN   C O     1 
ATOM   12720 C  CB    . ASN   C 2 93  ? 105.253 123.953 93.078  1.00 65.04  ?  92   ASN   C CB    1 
ATOM   12721 C  CG    . ASN   C 2 93  ? 104.909 124.069 94.543  1.00 73.15  ?  92   ASN   C CG    1 
ATOM   12722 O  OD1   . ASN   C 2 93  ? 103.752 124.237 94.900  1.00 78.63  ?  92   ASN   C OD1   1 
ATOM   12723 N  ND2   . ASN   C 2 93  ? 105.912 123.972 95.398  1.00 76.28  ?  92   ASN   C ND2   1 
ATOM   12724 N  N     . VAL   C 2 94  ? 104.653 122.582 90.024  1.00 62.46  ?  93   VAL   C N     1 
ATOM   12725 C  CA    . VAL   C 2 94  ? 104.935 122.599 88.581  1.00 59.65  ?  93   VAL   C CA    1 
ATOM   12726 C  C     . VAL   C 2 94  ? 103.711 122.196 87.772  1.00 62.65  ?  93   VAL   C C     1 
ATOM   12727 O  O     . VAL   C 2 94  ? 103.364 122.858 86.792  1.00 72.92  ?  93   VAL   C O     1 
ATOM   12728 C  CB    . VAL   C 2 94  ? 106.135 121.679 88.272  1.00 60.24  ?  93   VAL   C CB    1 
ATOM   12729 C  CG1   . VAL   C 2 94  ? 106.459 121.720 86.787  1.00 66.98  ?  93   VAL   C CG1   1 
ATOM   12730 C  CG2   . VAL   C 2 94  ? 107.339 122.093 89.094  1.00 57.40  ?  93   VAL   C CG2   1 
ATOM   12731 N  N     . ALA   C 2 95  ? 103.002 121.156 88.210  1.00 62.46  ?  94   ALA   C N     1 
ATOM   12732 C  CA    . ALA   C 2 95  ? 101.856 120.657 87.461  1.00 68.92  ?  94   ALA   C CA    1 
ATOM   12733 C  C     . ALA   C 2 95  ? 100.607 121.499 87.689  1.00 69.14  ?  94   ALA   C C     1 
ATOM   12734 O  O     . ALA   C 2 95  ? 99.880  121.802 86.736  1.00 74.64  ?  94   ALA   C O     1 
ATOM   12735 C  CB    . ALA   C 2 95  ? 101.586 119.200 87.828  1.00 71.37  ?  94   ALA   C CB    1 
ATOM   12736 N  N     . LEU   C 2 96  ? 100.342 121.889 88.933  1.00 61.40  ?  95   LEU   C N     1 
ATOM   12737 C  CA    . LEU   C 2 96  ? 99.078  122.522 89.280  1.00 62.88  ?  95   LEU   C CA    1 
ATOM   12738 C  C     . LEU   C 2 96  ? 99.130  124.041 89.295  1.00 63.95  ?  95   LEU   C C     1 
ATOM   12739 O  O     . LEU   C 2 96  ? 98.113  124.676 89.006  1.00 70.56  ?  95   LEU   C O     1 
ATOM   12740 C  CB    . LEU   C 2 96  ? 98.600  122.029 90.652  1.00 60.57  ?  95   LEU   C CB    1 
ATOM   12741 C  CG    . LEU   C 2 96  ? 98.308  120.532 90.788  1.00 59.21  ?  95   LEU   C CG    1 
ATOM   12742 C  CD1   . LEU   C 2 96  ? 97.602  120.239 92.101  1.00 60.46  ?  95   LEU   C CD1   1 
ATOM   12743 C  CD2   . LEU   C 2 96  ? 97.487  120.034 89.613  1.00 58.56  ?  95   LEU   C CD2   1 
ATOM   12744 N  N     . LEU   C 2 97  ? 100.266 124.634 89.667  1.00 63.14  ?  96   LEU   C N     1 
ATOM   12745 C  CA    . LEU   C 2 97  ? 100.332 126.085 89.835  1.00 63.87  ?  96   LEU   C CA    1 
ATOM   12746 C  C     . LEU   C 2 97  ? 100.011 126.856 88.560  1.00 69.54  ?  96   LEU   C C     1 
ATOM   12747 O  O     . LEU   C 2 97  ? 99.229  127.820 88.633  1.00 73.64  ?  96   LEU   C O     1 
ATOM   12748 C  CB    . LEU   C 2 97  ? 101.705 126.472 90.393  1.00 62.87  ?  96   LEU   C CB    1 
ATOM   12749 C  CG    . LEU   C 2 97  ? 101.686 127.490 91.530  1.00 64.79  ?  96   LEU   C CG    1 
ATOM   12750 C  CD1   . LEU   C 2 97  ? 100.670 127.090 92.584  1.00 61.69  ?  96   LEU   C CD1   1 
ATOM   12751 C  CD2   . LEU   C 2 97  ? 103.065 127.634 92.144  1.00 67.21  ?  96   LEU   C CD2   1 
ATOM   12752 N  N     . PRO   C 2 98  ? 100.548 126.505 87.376  1.00 70.45  ?  97   PRO   C N     1 
ATOM   12753 C  CA    . PRO   C 2 98  ? 100.196 127.264 86.165  1.00 68.77  ?  97   PRO   C CA    1 
ATOM   12754 C  C     . PRO   C 2 98  ? 98.787  126.993 85.653  1.00 70.15  ?  97   PRO   C C     1 
ATOM   12755 O  O     . PRO   C 2 98  ? 98.450  127.410 84.542  1.00 74.68  ?  97   PRO   C O     1 
ATOM   12756 C  CB    . PRO   C 2 98  ? 101.245 126.800 85.141  1.00 65.91  ?  97   PRO   C CB    1 
ATOM   12757 C  CG    . PRO   C 2 98  ? 102.277 126.051 85.921  1.00 67.49  ?  97   PRO   C CG    1 
ATOM   12758 C  CD    . PRO   C 2 98  ? 101.563 125.481 87.084  1.00 66.00  ?  97   PRO   C CD    1 
ATOM   12759 N  N     . LEU   C 2 99  ? 97.984  126.231 86.399  1.00 63.29  ?  98   LEU   C N     1 
ATOM   12760 C  CA    . LEU   C 2 99  ? 96.605  125.949 86.024  1.00 61.36  ?  98   LEU   C CA    1 
ATOM   12761 C  C     . LEU   C 2 99  ? 95.581  126.506 86.999  1.00 65.15  ?  98   LEU   C C     1 
ATOM   12762 O  O     . LEU   C 2 99  ? 94.430  126.712 86.605  1.00 72.23  ?  98   LEU   C O     1 
ATOM   12763 C  CB    . LEU   C 2 99  ? 96.376  124.433 85.892  1.00 62.98  ?  98   LEU   C CB    1 
ATOM   12764 C  CG    . LEU   C 2 99  ? 97.079  123.736 84.728  1.00 66.46  ?  98   LEU   C CG    1 
ATOM   12765 C  CD1   . LEU   C 2 99  ? 96.776  122.248 84.729  1.00 65.81  ?  98   LEU   C CD1   1 
ATOM   12766 C  CD2   . LEU   C 2 99  ? 96.678  124.369 83.407  1.00 67.49  ?  98   LEU   C CD2   1 
ATOM   12767 N  N     . ILE   C 2 100 ? 95.968  126.769 88.245  1.00 65.17  ?  99   ILE   C N     1 
ATOM   12768 C  CA    . ILE   C 2 100 ? 95.029  127.231 89.258  1.00 64.77  ?  99   ILE   C CA    1 
ATOM   12769 C  C     . ILE   C 2 100 ? 94.649  128.682 88.996  1.00 66.13  ?  99   ILE   C C     1 
ATOM   12770 O  O     . ILE   C 2 100 ? 95.496  129.508 88.633  1.00 69.10  ?  99   ILE   C O     1 
ATOM   12771 C  CB    . ILE   C 2 100 ? 95.654  127.056 90.652  1.00 67.99  ?  99   ILE   C CB    1 
ATOM   12772 C  CG1   . ILE   C 2 100 ? 95.682  125.578 91.033  1.00 67.78  ?  99   ILE   C CG1   1 
ATOM   12773 C  CG2   . ILE   C 2 100 ? 94.882  127.848 91.700  1.00 70.04  ?  99   ILE   C CG2   1 
ATOM   12774 C  CD1   . ILE   C 2 100 ? 96.610  125.265 92.175  1.00 70.24  ?  99   ILE   C CD1   1 
ATOM   12775 N  N     . SER   C 2 101 ? 93.369  129.010 89.190  1.00 76.41  ?  100  SER   C N     1 
ATOM   12776 C  CA    . SER   C 2 101 ? 92.876  130.343 88.873  1.00 77.38  ?  100  SER   C CA    1 
ATOM   12777 C  C     . SER   C 2 101 ? 92.194  131.005 90.061  1.00 75.96  ?  100  SER   C C     1 
ATOM   12778 O  O     . SER   C 2 101 ? 91.574  132.058 89.893  1.00 79.35  ?  100  SER   C O     1 
ATOM   12779 C  CB    . SER   C 2 101 ? 91.913  130.292 87.684  1.00 75.77  ?  100  SER   C CB    1 
ATOM   12780 O  OG    . SER   C 2 101 ? 90.932  129.286 87.877  1.00 80.62  ?  100  SER   C OG    1 
ATOM   12781 N  N     . ILE   C 2 102 ? 92.307  130.435 91.257  1.00 73.81  ?  101  ILE   C N     1 
ATOM   12782 C  CA    . ILE   C 2 102 ? 91.786  131.075 92.463  1.00 70.25  ?  101  ILE   C CA    1 
ATOM   12783 C  C     . ILE   C 2 102 ? 92.894  131.149 93.508  1.00 76.74  ?  101  ILE   C C     1 
ATOM   12784 O  O     . ILE   C 2 102 ? 93.697  130.213 93.627  1.00 87.14  ?  101  ILE   C O     1 
ATOM   12785 C  CB    . ILE   C 2 102 ? 90.554  130.334 93.007  1.00 65.01  ?  101  ILE   C CB    1 
ATOM   12786 C  CG1   . ILE   C 2 102 ? 90.794  128.825 93.021  1.00 73.70  ?  101  ILE   C CG1   1 
ATOM   12787 C  CG2   . ILE   C 2 102 ? 89.324  130.667 92.179  1.00 70.06  ?  101  ILE   C CG2   1 
ATOM   12788 C  CD1   . ILE   C 2 102 ? 89.724  128.048 93.754  1.00 77.14  ?  101  ILE   C CD1   1 
ATOM   12789 N  N     . PRO   C 2 103 ? 92.982  132.238 94.276  1.00 73.45  ?  102  PRO   C N     1 
ATOM   12790 C  CA    . PRO   C 2 103 ? 94.090  132.362 95.237  1.00 74.92  ?  102  PRO   C CA    1 
ATOM   12791 C  C     . PRO   C 2 103 ? 94.099  131.289 96.315  1.00 77.95  ?  102  PRO   C C     1 
ATOM   12792 O  O     . PRO   C 2 103 ? 95.177  130.927 96.803  1.00 83.96  ?  102  PRO   C O     1 
ATOM   12793 C  CB    . PRO   C 2 103 ? 93.876  133.764 95.833  1.00 76.06  ?  102  PRO   C CB    1 
ATOM   12794 C  CG    . PRO   C 2 103 ? 92.438  134.075 95.587  1.00 72.11  ?  102  PRO   C CG    1 
ATOM   12795 C  CD    . PRO   C 2 103 ? 92.080  133.401 94.305  1.00 71.71  ?  102  PRO   C CD    1 
ATOM   12796 N  N     . GLU   C 2 104 ? 92.924  130.841 96.770  1.00 73.72  ?  103  GLU   C N     1 
ATOM   12797 C  CA    . GLU   C 2 104 ? 92.871  129.886 97.875  1.00 73.12  ?  103  GLU   C CA    1 
ATOM   12798 C  C     . GLU   C 2 104 ? 93.530  128.571 97.485  1.00 81.68  ?  103  GLU   C C     1 
ATOM   12799 O  O     . GLU   C 2 104 ? 94.338  128.021 98.241  1.00 88.78  ?  103  GLU   C O     1 
ATOM   12800 C  CB    . GLU   C 2 104 ? 91.421  129.652 98.310  1.00 75.63  ?  103  GLU   C CB    1 
ATOM   12801 C  CG    . GLU   C 2 104 ? 90.474  129.392 97.149  1.00 81.61  ?  103  GLU   C CG    1 
ATOM   12802 C  CD    . GLU   C 2 104 ? 89.387  130.433 97.027  1.00 90.07  ?  103  GLU   C CD    1 
ATOM   12803 O  OE1   . GLU   C 2 104 ? 89.724  131.625 96.887  1.00 91.35  ?  103  GLU   C OE1   1 
ATOM   12804 O  OE2   . GLU   C 2 104 ? 88.196  130.059 97.058  1.00 90.91  ?  103  GLU   C OE2   1 
ATOM   12805 N  N     . LEU   C 2 105 ? 93.205  128.060 96.294  1.00 67.95  ?  104  LEU   C N     1 
ATOM   12806 C  CA    . LEU   C 2 105 ? 93.789  126.807 95.827  1.00 62.11  ?  104  LEU   C CA    1 
ATOM   12807 C  C     . LEU   C 2 105 ? 95.288  126.945 95.607  1.00 64.48  ?  104  LEU   C C     1 
ATOM   12808 O  O     . LEU   C 2 105 ? 96.054  126.026 95.913  1.00 78.27  ?  104  LEU   C O     1 
ATOM   12809 C  CB    . LEU   C 2 105 ? 93.096  126.358 94.541  1.00 62.26  ?  104  LEU   C CB    1 
ATOM   12810 C  CG    . LEU   C 2 105 ? 93.263  124.893 94.146  1.00 64.45  ?  104  LEU   C CG    1 
ATOM   12811 C  CD1   . LEU   C 2 105 ? 93.123  123.993 95.360  1.00 64.89  ?  104  LEU   C CD1   1 
ATOM   12812 C  CD2   . LEU   C 2 105 ? 92.250  124.523 93.079  1.00 66.09  ?  104  LEU   C CD2   1 
ATOM   12813 N  N     . GLU   C 2 106 ? 95.720  128.086 95.071  1.00 63.09  ?  105  GLU   C N     1 
ATOM   12814 C  CA    . GLU   C 2 106 ? 97.140  128.341 94.857  1.00 65.34  ?  105  GLU   C CA    1 
ATOM   12815 C  C     . GLU   C 2 106 ? 97.910  128.323 96.175  1.00 71.46  ?  105  GLU   C C     1 
ATOM   12816 O  O     . GLU   C 2 106 ? 98.949  127.654 96.302  1.00 79.80  ?  105  GLU   C O     1 
ATOM   12817 C  CB    . GLU   C 2 106 ? 97.289  129.687 94.153  1.00 63.21  ?  105  GLU   C CB    1 
ATOM   12818 C  CG    . GLU   C 2 106 ? 98.564  129.903 93.395  1.00 77.61  ?  105  GLU   C CG    1 
ATOM   12819 C  CD    . GLU   C 2 106 ? 98.953  131.365 93.417  1.00 87.06  ?  105  GLU   C CD    1 
ATOM   12820 O  OE1   . GLU   C 2 106 ? 98.229  132.161 94.053  1.00 86.27  ?  105  GLU   C OE1   1 
ATOM   12821 O  OE2   . GLU   C 2 106 ? 99.966  131.728 92.801  1.00 87.11  ?  105  GLU   C OE2   1 
ATOM   12822 N  N     . THR   C 2 107 ? 97.404  129.051 97.174  1.00 57.85  ?  106  THR   C N     1 
ATOM   12823 C  CA    . THR   C 2 107 ? 98.052  129.066 98.481  1.00 53.02  ?  106  THR   C CA    1 
ATOM   12824 C  C     . THR   C 2 107 ? 98.036  127.683 99.119  1.00 56.39  ?  106  THR   C C     1 
ATOM   12825 O  O     . THR   C 2 107 ? 99.016  127.276 99.753  1.00 66.69  ?  106  THR   C O     1 
ATOM   12826 C  CB    . THR   C 2 107 ? 97.376  130.089 99.393  1.00 60.84  ?  106  THR   C CB    1 
ATOM   12827 O  OG1   . THR   C 2 107 ? 97.371  131.370 98.753  1.00 69.65  ?  106  THR   C OG1   1 
ATOM   12828 C  CG2   . THR   C 2 107 ? 98.114  130.197 100.719 1.00 61.56  ?  106  THR   C CG2   1 
ATOM   12829 N  N     . TRP   C 2 108 ? 96.932  126.945 98.965  1.00 50.79  ?  107  TRP   C N     1 
ATOM   12830 C  CA    . TRP   C 2 108 ? 96.871  125.599 99.522  1.00 48.75  ?  107  TRP   C CA    1 
ATOM   12831 C  C     . TRP   C 2 108 ? 97.900  124.685 98.875  1.00 53.10  ?  107  TRP   C C     1 
ATOM   12832 O  O     . TRP   C 2 108 ? 98.541  123.883 99.560  1.00 64.23  ?  107  TRP   C O     1 
ATOM   12833 C  CB    . TRP   C 2 108 ? 95.473  125.007 99.362  1.00 46.87  ?  107  TRP   C CB    1 
ATOM   12834 C  CG    . TRP   C 2 108 ? 95.455  123.524 99.590  1.00 52.34  ?  107  TRP   C CG    1 
ATOM   12835 C  CD1   . TRP   C 2 108 ? 95.031  122.566 98.718  1.00 57.93  ?  107  TRP   C CD1   1 
ATOM   12836 C  CD2   . TRP   C 2 108 ? 95.898  122.829 100.764 1.00 54.36  ?  107  TRP   C CD2   1 
ATOM   12837 N  NE1   . TRP   C 2 108 ? 95.176  121.320 99.277  1.00 53.39  ?  107  TRP   C NE1   1 
ATOM   12838 C  CE2   . TRP   C 2 108 ? 95.706  121.455 100.532 1.00 50.78  ?  107  TRP   C CE2   1 
ATOM   12839 C  CE3   . TRP   C 2 108 ? 96.433  123.237 101.990 1.00 54.07  ?  107  TRP   C CE3   1 
ATOM   12840 C  CZ2   . TRP   C 2 108 ? 96.031  120.487 101.479 1.00 55.03  ?  107  TRP   C CZ2   1 
ATOM   12841 C  CZ3   . TRP   C 2 108 ? 96.756  122.276 102.926 1.00 52.75  ?  107  TRP   C CZ3   1 
ATOM   12842 C  CH2   . TRP   C 2 108 ? 96.554  120.918 102.667 1.00 53.92  ?  107  TRP   C CH2   1 
ATOM   12843 N  N     . VAL   C 2 109 ? 98.065  124.782 97.556  1.00 46.78  ?  108  VAL   C N     1 
ATOM   12844 C  CA    . VAL   C 2 109 ? 99.040  123.941 96.867  1.00 56.44  ?  108  VAL   C CA    1 
ATOM   12845 C  C     . VAL   C 2 109 ? 100.450 124.265 97.340  1.00 59.82  ?  108  VAL   C C     1 
ATOM   12846 O  O     . VAL   C 2 109 ? 101.261 123.365 97.591  1.00 71.59  ?  108  VAL   C O     1 
ATOM   12847 C  CB    . VAL   C 2 109 ? 98.892  124.095 95.342  1.00 50.41  ?  108  VAL   C CB    1 
ATOM   12848 C  CG1   . VAL   C 2 109 ? 100.201 123.785 94.637  1.00 49.44  ?  108  VAL   C CG1   1 
ATOM   12849 C  CG2   . VAL   C 2 109 ? 97.791  123.184 94.835  1.00 48.73  ?  108  VAL   C CG2   1 
ATOM   12850 N  N     . GLU   C 2 110 ? 100.762 125.553 97.487  1.00 58.61  ?  109  GLU   C N     1 
ATOM   12851 C  CA    . GLU   C 2 110 ? 102.097 125.920 97.949  1.00 57.29  ?  109  GLU   C CA    1 
ATOM   12852 C  C     . GLU   C 2 110 ? 102.344 125.465 99.388  1.00 60.29  ?  109  GLU   C C     1 
ATOM   12853 O  O     . GLU   C 2 110 ? 103.431 124.963 99.712  1.00 66.51  ?  109  GLU   C O     1 
ATOM   12854 C  CB    . GLU   C 2 110 ? 102.287 127.424 97.794  1.00 57.56  ?  109  GLU   C CB    1 
ATOM   12855 C  CG    . GLU   C 2 110 ? 102.287 127.859 96.338  1.00 69.16  ?  109  GLU   C CG    1 
ATOM   12856 C  CD    . GLU   C 2 110 ? 102.419 129.350 96.157  1.00 79.33  ?  109  GLU   C CD    1 
ATOM   12857 O  OE1   . GLU   C 2 110 ? 103.566 129.825 96.100  1.00 82.76  ?  109  GLU   C OE1   1 
ATOM   12858 O  OE2   . GLU   C 2 110 ? 101.384 130.042 96.055  1.00 78.84  ?  109  GLU   C OE2   1 
ATOM   12859 N  N     . THR   C 2 111 ? 101.343 125.613 100.261 1.00 50.07  ?  110  THR   C N     1 
ATOM   12860 C  CA    . THR   C 2 111 ? 101.470 125.140 101.637 1.00 48.85  ?  110  THR   C CA    1 
ATOM   12861 C  C     . THR   C 2 111 ? 101.633 123.626 101.688 1.00 55.77  ?  110  THR   C C     1 
ATOM   12862 O  O     . THR   C 2 111 ? 102.415 123.102 102.489 1.00 71.90  ?  110  THR   C O     1 
ATOM   12863 C  CB    . THR   C 2 111 ? 100.251 125.573 102.453 1.00 49.71  ?  110  THR   C CB    1 
ATOM   12864 O  OG1   . THR   C 2 111 ? 99.997  126.966 102.231 1.00 61.12  ?  110  THR   C OG1   1 
ATOM   12865 C  CG2   . THR   C 2 111 ? 100.486 125.337 103.933 1.00 56.76  ?  110  THR   C CG2   1 
ATOM   12866 N  N     . TRP   C 2 112 ? 100.897 122.910 100.839 1.00 43.08  ?  111  TRP   C N     1 
ATOM   12867 C  CA    . TRP   C 2 112 ? 100.989 121.456 100.774 1.00 41.85  ?  111  TRP   C CA    1 
ATOM   12868 C  C     . TRP   C 2 112 ? 102.374 121.014 100.314 1.00 50.82  ?  111  TRP   C C     1 
ATOM   12869 O  O     . TRP   C 2 112 ? 102.952 120.068 100.866 1.00 60.36  ?  111  TRP   C O     1 
ATOM   12870 C  CB    . TRP   C 2 112 ? 99.875  120.954 99.849  1.00 33.95  ?  111  TRP   C CB    1 
ATOM   12871 C  CG    . TRP   C 2 112 ? 99.922  119.536 99.376  1.00 43.51  ?  111  TRP   C CG    1 
ATOM   12872 C  CD1   . TRP   C 2 112 ? 100.492 118.468 99.999  1.00 51.92  ?  111  TRP   C CD1   1 
ATOM   12873 C  CD2   . TRP   C 2 112 ? 99.326  119.029 98.176  1.00 44.83  ?  111  TRP   C CD2   1 
ATOM   12874 N  NE1   . TRP   C 2 112 ? 100.295 117.330 99.257  1.00 52.81  ?  111  TRP   C NE1   1 
ATOM   12875 C  CE2   . TRP   C 2 112 ? 99.603  117.654 98.121  1.00 48.32  ?  111  TRP   C CE2   1 
ATOM   12876 C  CE3   . TRP   C 2 112 ? 98.592  119.611 97.138  1.00 48.13  ?  111  TRP   C CE3   1 
ATOM   12877 C  CZ2   . TRP   C 2 112 ? 99.158  116.846 97.078  1.00 52.11  ?  111  TRP   C CZ2   1 
ATOM   12878 C  CZ3   . TRP   C 2 112 ? 98.170  118.813 96.094  1.00 49.70  ?  111  TRP   C CZ3   1 
ATOM   12879 C  CH2   . TRP   C 2 112 ? 98.455  117.446 96.070  1.00 51.33  ?  111  TRP   C CH2   1 
ATOM   12880 N  N     . ALA   C 2 113 ? 102.938 121.710 99.325  1.00 39.95  ?  112  ALA   C N     1 
ATOM   12881 C  CA    . ALA   C 2 113 ? 104.299 121.408 98.891  1.00 34.18  ?  112  ALA   C CA    1 
ATOM   12882 C  C     . ALA   C 2 113 ? 105.309 121.657 100.006 1.00 46.71  ?  112  ALA   C C     1 
ATOM   12883 O  O     . ALA   C 2 113 ? 106.233 120.857 100.211 1.00 61.21  ?  112  ALA   C O     1 
ATOM   12884 C  CB    . ALA   C 2 113 ? 104.647 122.236 97.660  1.00 43.13  ?  112  ALA   C CB    1 
ATOM   12885 N  N     . PHE   C 2 114 ? 105.154 122.765 100.736 1.00 45.63  ?  113  PHE   C N     1 
ATOM   12886 C  CA    . PHE   C 2 114 ? 106.053 123.038 101.856 1.00 42.27  ?  113  PHE   C CA    1 
ATOM   12887 C  C     . PHE   C 2 114 ? 105.942 121.957 102.928 1.00 49.20  ?  113  PHE   C C     1 
ATOM   12888 O  O     . PHE   C 2 114 ? 106.953 121.522 103.503 1.00 62.42  ?  113  PHE   C O     1 
ATOM   12889 C  CB    . PHE   C 2 114 ? 105.747 124.419 102.436 1.00 44.94  ?  113  PHE   C CB    1 
ATOM   12890 C  CG    . PHE   C 2 114 ? 106.408 124.682 103.756 1.00 47.92  ?  113  PHE   C CG    1 
ATOM   12891 C  CD1   . PHE   C 2 114 ? 107.759 124.968 103.823 1.00 47.30  ?  113  PHE   C CD1   1 
ATOM   12892 C  CD2   . PHE   C 2 114 ? 105.687 124.605 104.934 1.00 46.89  ?  113  PHE   C CD2   1 
ATOM   12893 C  CE1   . PHE   C 2 114 ? 108.368 125.204 105.033 1.00 50.62  ?  113  PHE   C CE1   1 
ATOM   12894 C  CE2   . PHE   C 2 114 ? 106.292 124.841 106.148 1.00 50.48  ?  113  PHE   C CE2   1 
ATOM   12895 C  CZ    . PHE   C 2 114 ? 107.634 125.139 106.197 1.00 56.43  ?  113  PHE   C CZ    1 
ATOM   12896 N  N     . SER   C 2 115 ? 104.717 121.508 103.206 1.00 44.24  ?  114  SER   C N     1 
ATOM   12897 C  CA    . SER   C 2 115 ? 104.518 120.426 104.162 1.00 40.52  ?  114  SER   C CA    1 
ATOM   12898 C  C     . SER   C 2 115 ? 105.212 119.152 103.700 1.00 49.03  ?  114  SER   C C     1 
ATOM   12899 O  O     . SER   C 2 115 ? 105.786 118.418 104.512 1.00 60.44  ?  114  SER   C O     1 
ATOM   12900 C  CB    . SER   C 2 115 ? 103.024 120.179 104.370 1.00 42.94  ?  114  SER   C CB    1 
ATOM   12901 O  OG    . SER   C 2 115 ? 102.781 119.542 105.610 1.00 63.89  ?  114  SER   C OG    1 
ATOM   12902 N  N     . GLU   C 2 116 ? 105.168 118.868 102.397 1.00 51.19  ?  115  GLU   C N     1 
ATOM   12903 C  CA    . GLU   C 2 116 ? 105.862 117.685 101.899 1.00 41.42  ?  115  GLU   C CA    1 
ATOM   12904 C  C     . GLU   C 2 116 ? 107.376 117.824 102.014 1.00 50.34  ?  115  GLU   C C     1 
ATOM   12905 O  O     . GLU   C 2 116 ? 108.069 116.827 102.247 1.00 63.37  ?  115  GLU   C O     1 
ATOM   12906 C  CB    . GLU   C 2 116 ? 105.461 117.390 100.455 1.00 36.48  ?  115  GLU   C CB    1 
ATOM   12907 C  CG    . GLU   C 2 116 ? 103.971 117.166 100.226 1.00 41.66  ?  115  GLU   C CG    1 
ATOM   12908 C  CD    . GLU   C 2 116 ? 103.385 115.987 100.992 1.00 52.30  ?  115  GLU   C CD    1 
ATOM   12909 O  OE1   . GLU   C 2 116 ? 104.126 115.232 101.651 1.00 68.14  ?  115  GLU   C OE1   1 
ATOM   12910 O  OE2   . GLU   C 2 116 ? 102.154 115.810 100.926 1.00 55.04  ?  115  GLU   C OE2   1 
ATOM   12911 N  N     . THR   C 2 117 ? 107.910 119.036 101.846 1.00 49.30  ?  116  THR   C N     1 
ATOM   12912 C  CA    . THR   C 2 117 ? 109.338 119.231 102.098 1.00 43.09  ?  116  THR   C CA    1 
ATOM   12913 C  C     . THR   C 2 117 ? 109.678 118.942 103.557 1.00 43.28  ?  116  THR   C C     1 
ATOM   12914 O  O     . THR   C 2 117 ? 110.701 118.312 103.857 1.00 57.89  ?  116  THR   C O     1 
ATOM   12915 C  CB    . THR   C 2 117 ? 109.774 120.652 101.731 1.00 48.42  ?  116  THR   C CB    1 
ATOM   12916 O  OG1   . THR   C 2 117 ? 109.208 121.587 102.658 1.00 57.04  ?  116  THR   C OG1   1 
ATOM   12917 C  CG2   . THR   C 2 117 ? 109.348 121.003 100.317 1.00 54.26  ?  116  THR   C CG2   1 
ATOM   12918 N  N     . ILE   C 2 118 ? 108.823 119.392 104.477 1.00 48.81  ?  117  ILE   C N     1 
ATOM   12919 C  CA    . ILE   C 2 118 ? 109.033 119.089 105.893 1.00 45.09  ?  117  ILE   C CA    1 
ATOM   12920 C  C     . ILE   C 2 118 ? 108.990 117.582 106.131 1.00 43.12  ?  117  ILE   C C     1 
ATOM   12921 O  O     . ILE   C 2 118 ? 109.814 117.031 106.870 1.00 59.86  ?  117  ILE   C O     1 
ATOM   12922 C  CB    . ILE   C 2 118 ? 108.002 119.833 106.761 1.00 53.36  ?  117  ILE   C CB    1 
ATOM   12923 C  CG1   . ILE   C 2 118 ? 108.361 121.314 106.874 1.00 50.16  ?  117  ILE   C CG1   1 
ATOM   12924 C  CG2   . ILE   C 2 118 ? 107.911 119.203 108.145 1.00 49.31  ?  117  ILE   C CG2   1 
ATOM   12925 C  CD1   . ILE   C 2 118 ? 109.598 121.570 107.687 1.00 57.50  ?  117  ILE   C CD1   1 
ATOM   12926 N  N     . HIS   C 2 119 ? 108.052 116.891 105.479 1.00 50.56  ?  118  HIS   C N     1 
ATOM   12927 C  CA    . HIS   C 2 119 ? 107.941 115.443 105.632 1.00 42.63  ?  118  HIS   C CA    1 
ATOM   12928 C  C     . HIS   C 2 119 ? 109.183 114.724 105.118 1.00 42.74  ?  118  HIS   C C     1 
ATOM   12929 O  O     . HIS   C 2 119 ? 109.662 113.772 105.747 1.00 53.47  ?  118  HIS   C O     1 
ATOM   12930 C  CB    . HIS   C 2 119 ? 106.701 114.940 104.902 1.00 31.56  ?  118  HIS   C CB    1 
ATOM   12931 C  CG    . HIS   C 2 119 ? 105.414 115.355 105.538 1.00 37.53  ?  118  HIS   C CG    1 
ATOM   12932 N  ND1   . HIS   C 2 119 ? 104.186 114.977 105.042 1.00 41.05  ?  118  HIS   C ND1   1 
ATOM   12933 C  CD2   . HIS   C 2 119 ? 105.162 116.111 106.632 1.00 46.10  ?  118  HIS   C CD2   1 
ATOM   12934 C  CE1   . HIS   C 2 119 ? 103.233 115.486 105.801 1.00 51.67  ?  118  HIS   C CE1   1 
ATOM   12935 N  NE2   . HIS   C 2 119 ? 103.799 116.177 106.773 1.00 55.16  ?  118  HIS   C NE2   1 
ATOM   12936 N  N     . SER   C 2 120 ? 109.701 115.143 103.962 1.00 48.88  ?  119  SER   C N     1 
ATOM   12937 C  CA    . SER   C 2 120 ? 110.919 114.530 103.441 1.00 49.67  ?  119  SER   C CA    1 
ATOM   12938 C  C     . SER   C 2 120 ? 112.093 114.769 104.380 1.00 49.41  ?  119  SER   C C     1 
ATOM   12939 O  O     . SER   C 2 120 ? 112.910 113.866 104.613 1.00 59.94  ?  119  SER   C O     1 
ATOM   12940 C  CB    . SER   C 2 120 ? 111.224 115.065 102.044 1.00 48.67  ?  119  SER   C CB    1 
ATOM   12941 O  OG    . SER   C 2 120 ? 111.750 116.378 102.099 1.00 67.96  ?  119  SER   C OG    1 
ATOM   12942 N  N     . ARG   C 2 121 ? 112.190 115.980 104.935 1.00 51.09  ?  120  ARG   C N     1 
ATOM   12943 C  CA    . ARG   C 2 121 ? 113.228 116.250 105.923 1.00 48.91  ?  120  ARG   C CA    1 
ATOM   12944 C  C     . ARG   C 2 121 ? 113.080 115.338 107.134 1.00 54.15  ?  120  ARG   C C     1 
ATOM   12945 O  O     . ARG   C 2 121 ? 114.076 114.866 107.686 1.00 63.71  ?  120  ARG   C O     1 
ATOM   12946 C  CB    . ARG   C 2 121 ? 113.193 117.719 106.344 1.00 51.75  ?  120  ARG   C CB    1 
ATOM   12947 C  CG    . ARG   C 2 121 ? 113.969 118.015 107.619 1.00 56.22  ?  120  ARG   C CG    1 
ATOM   12948 C  CD    . ARG   C 2 121 ? 113.894 119.481 107.999 1.00 55.43  ?  120  ARG   C CD    1 
ATOM   12949 N  NE    . ARG   C 2 121 ? 115.121 120.191 107.661 1.00 59.61  ?  120  ARG   C NE    1 
ATOM   12950 C  CZ    . ARG   C 2 121 ? 115.310 120.880 106.549 1.00 70.55  ?  120  ARG   C CZ    1 
ATOM   12951 N  NH1   . ARG   C 2 121 ? 114.387 120.982 105.650 1.00 80.16  ?  120  ARG   C NH1   1 
ATOM   12952 N  NH2   . ARG   C 2 121 ? 116.468 121.480 106.331 1.00 65.38  ?  120  ARG   C NH2   1 
ATOM   12953 N  N     . SER   C 2 122 ? 111.844 115.060 107.549 1.00 51.99  ?  121  SER   C N     1 
ATOM   12954 C  CA    . SER   C 2 122 ? 111.634 114.208 108.718 1.00 46.11  ?  121  SER   C CA    1 
ATOM   12955 C  C     . SER   C 2 122 ? 112.010 112.755 108.438 1.00 47.42  ?  121  SER   C C     1 
ATOM   12956 O  O     . SER   C 2 122 ? 112.598 112.081 109.295 1.00 58.45  ?  121  SER   C O     1 
ATOM   12957 C  CB    . SER   C 2 122 ? 110.183 114.305 109.175 1.00 48.73  ?  121  SER   C CB    1 
ATOM   12958 O  OG    . SER   C 2 122 ? 109.719 115.638 109.082 1.00 62.66  ?  121  SER   C OG    1 
ATOM   12959 N  N     . TYR   C 2 123 ? 111.668 112.251 107.251 1.00 46.52  ?  122  TYR   C N     1 
ATOM   12960 C  CA    . TYR   C 2 123 ? 112.085 110.901 106.875 1.00 44.16  ?  122  TYR   C CA    1 
ATOM   12961 C  C     . TYR   C 2 123 ? 113.605 110.794 106.843 1.00 51.72  ?  122  TYR   C C     1 
ATOM   12962 O  O     . TYR   C 2 123 ? 114.189 109.827 107.353 1.00 59.22  ?  122  TYR   C O     1 
ATOM   12963 C  CB    . TYR   C 2 123 ? 111.505 110.520 105.512 1.00 42.08  ?  122  TYR   C CB    1 
ATOM   12964 C  CG    . TYR   C 2 123 ? 110.004 110.367 105.475 1.00 49.41  ?  122  TYR   C CG    1 
ATOM   12965 C  CD1   . TYR   C 2 123 ? 109.344 109.570 106.393 1.00 46.76  ?  122  TYR   C CD1   1 
ATOM   12966 C  CD2   . TYR   C 2 123 ? 109.249 111.011 104.507 1.00 52.80  ?  122  TYR   C CD2   1 
ATOM   12967 C  CE1   . TYR   C 2 123 ? 107.971 109.429 106.358 1.00 42.85  ?  122  TYR   C CE1   1 
ATOM   12968 C  CE2   . TYR   C 2 123 ? 107.878 110.878 104.465 1.00 41.69  ?  122  TYR   C CE2   1 
ATOM   12969 C  CZ    . TYR   C 2 123 ? 107.243 110.085 105.391 1.00 46.23  ?  122  TYR   C CZ    1 
ATOM   12970 O  OH    . TYR   C 2 123 ? 105.876 109.949 105.347 1.00 56.38  ?  122  TYR   C OH    1 
ATOM   12971 N  N     . THR   C 2 124 ? 114.262 111.789 106.239 1.00 53.96  ?  123  THR   C N     1 
ATOM   12972 C  CA    . THR   C 2 124 ? 115.720 111.810 106.215 1.00 44.52  ?  123  THR   C CA    1 
ATOM   12973 C  C     . THR   C 2 124 ? 116.289 111.881 107.627 1.00 57.64  ?  123  THR   C C     1 
ATOM   12974 O  O     . THR   C 2 124 ? 117.310 111.254 107.924 1.00 63.60  ?  123  THR   C O     1 
ATOM   12975 C  CB    . THR   C 2 124 ? 116.202 112.987 105.368 1.00 55.41  ?  123  THR   C CB    1 
ATOM   12976 O  OG1   . THR   C 2 124 ? 115.776 112.803 104.013 1.00 63.54  ?  123  THR   C OG1   1 
ATOM   12977 C  CG2   . THR   C 2 124 ? 117.711 113.090 105.394 1.00 68.53  ?  123  THR   C CG2   1 
ATOM   12978 N  N     . HIS   C 2 125 ? 115.631 112.632 108.511 1.00 63.33  ?  124  HIS   C N     1 
ATOM   12979 C  CA    . HIS   C 2 125 ? 116.063 112.731 109.901 1.00 53.33  ?  124  HIS   C CA    1 
ATOM   12980 C  C     . HIS   C 2 125 ? 116.000 111.378 110.597 1.00 50.00  ?  124  HIS   C C     1 
ATOM   12981 O  O     . HIS   C 2 125 ? 116.934 110.994 111.312 1.00 56.96  ?  124  HIS   C O     1 
ATOM   12982 C  CB    . HIS   C 2 125 ? 115.190 113.761 110.624 1.00 52.93  ?  124  HIS   C CB    1 
ATOM   12983 C  CG    . HIS   C 2 125 ? 115.489 113.908 112.083 1.00 58.41  ?  124  HIS   C CG    1 
ATOM   12984 N  ND1   . HIS   C 2 125 ? 116.273 114.925 112.582 1.00 61.12  ?  124  HIS   C ND1   1 
ATOM   12985 C  CD2   . HIS   C 2 125 ? 115.086 113.184 113.154 1.00 57.57  ?  124  HIS   C CD2   1 
ATOM   12986 C  CE1   . HIS   C 2 125 ? 116.352 114.813 113.896 1.00 61.74  ?  124  HIS   C CE1   1 
ATOM   12987 N  NE2   . HIS   C 2 125 ? 115.642 113.764 114.268 1.00 61.50  ?  124  HIS   C NE2   1 
ATOM   12988 N  N     . ILE   C 2 126 ? 114.910 110.637 110.390 1.00 44.38  ?  125  ILE   C N     1 
ATOM   12989 C  CA    . ILE   C 2 126 ? 114.782 109.314 111.002 1.00 43.70  ?  125  ILE   C CA    1 
ATOM   12990 C  C     . ILE   C 2 126 ? 115.877 108.386 110.490 1.00 47.66  ?  125  ILE   C C     1 
ATOM   12991 O  O     . ILE   C 2 126 ? 116.523 107.664 111.265 1.00 56.72  ?  125  ILE   C O     1 
ATOM   12992 C  CB    . ILE   C 2 126 ? 113.382 108.729 110.744 1.00 41.59  ?  125  ILE   C CB    1 
ATOM   12993 C  CG1   . ILE   C 2 126 ? 112.312 109.554 111.457 1.00 46.61  ?  125  ILE   C CG1   1 
ATOM   12994 C  CG2   . ILE   C 2 126 ? 113.318 107.287 111.209 1.00 41.42  ?  125  ILE   C CG2   1 
ATOM   12995 C  CD1   . ILE   C 2 126 ? 110.915 109.007 111.285 1.00 45.81  ?  125  ILE   C CD1   1 
ATOM   12996 N  N     . ILE   C 2 127 ? 116.109 108.399 109.174 1.00 60.39  ?  126  ILE   C N     1 
ATOM   12997 C  CA    . ILE   C 2 127 ? 117.132 107.526 108.600 1.00 50.80  ?  126  ILE   C CA    1 
ATOM   12998 C  C     . ILE   C 2 127 ? 118.512 107.889 109.137 1.00 51.22  ?  126  ILE   C C     1 
ATOM   12999 O  O     . ILE   C 2 127 ? 119.300 107.009 109.500 1.00 54.32  ?  126  ILE   C O     1 
ATOM   13000 C  CB    . ILE   C 2 127 ? 117.090 107.571 107.063 1.00 54.56  ?  126  ILE   C CB    1 
ATOM   13001 C  CG1   . ILE   C 2 127 ? 115.879 106.802 106.538 1.00 55.92  ?  126  ILE   C CG1   1 
ATOM   13002 C  CG2   . ILE   C 2 127 ? 118.369 106.991 106.481 1.00 55.34  ?  126  ILE   C CG2   1 
ATOM   13003 C  CD1   . ILE   C 2 127 ? 115.629 107.001 105.062 1.00 55.25  ?  126  ILE   C CD1   1 
ATOM   13004 N  N     . ARG   C 2 128 ? 118.815 109.187 109.221 1.00 59.47  ?  127  ARG   C N     1 
ATOM   13005 C  CA    . ARG   C 2 128 ? 120.101 109.627 109.750 1.00 51.02  ?  127  ARG   C CA    1 
ATOM   13006 C  C     . ARG   C 2 128 ? 120.268 109.226 111.207 1.00 58.91  ?  127  ARG   C C     1 
ATOM   13007 O  O     . ARG   C 2 128 ? 121.377 108.905 111.646 1.00 75.98  ?  127  ARG   C O     1 
ATOM   13008 C  CB    . ARG   C 2 128 ? 120.237 111.140 109.605 1.00 55.28  ?  127  ARG   C CB    1 
ATOM   13009 C  CG    . ARG   C 2 128 ? 120.465 111.619 108.198 1.00 54.15  ?  127  ARG   C CG    1 
ATOM   13010 C  CD    . ARG   C 2 128 ? 120.010 113.055 108.033 1.00 52.80  ?  127  ARG   C CD    1 
ATOM   13011 N  NE    . ARG   C 2 128 ? 121.117 113.976 107.816 1.00 63.97  ?  127  ARG   C NE    1 
ATOM   13012 C  CZ    . ARG   C 2 128 ? 121.118 115.235 108.225 1.00 61.23  ?  127  ARG   C CZ    1 
ATOM   13013 N  NH1   . ARG   C 2 128 ? 120.068 115.764 108.829 1.00 64.02  ?  127  ARG   C NH1   1 
ATOM   13014 N  NH2   . ARG   C 2 128 ? 122.199 115.984 108.025 1.00 62.01  ?  127  ARG   C NH2   1 
ATOM   13015 N  N     . ASN   C 2 129 ? 119.181 109.258 111.980 1.00 62.95  ?  128  ASN   C N     1 
ATOM   13016 C  CA    . ASN   C 2 129 ? 119.274 108.890 113.387 1.00 56.89  ?  128  ASN   C CA    1 
ATOM   13017 C  C     . ASN   C 2 129 ? 119.539 107.399 113.557 1.00 59.21  ?  128  ASN   C C     1 
ATOM   13018 O  O     . ASN   C 2 129 ? 120.439 107.002 114.306 1.00 65.57  ?  128  ASN   C O     1 
ATOM   13019 C  CB    . ASN   C 2 129 ? 117.995 109.291 114.123 1.00 62.83  ?  128  ASN   C CB    1 
ATOM   13020 C  CG    . ASN   C 2 129 ? 118.023 108.904 115.586 1.00 65.33  ?  128  ASN   C CG    1 
ATOM   13021 O  OD1   . ASN   C 2 129 ? 118.903 109.326 116.334 1.00 66.13  ?  128  ASN   C OD1   1 
ATOM   13022 N  ND2   . ASN   C 2 129 ? 117.061 108.091 116.001 1.00 68.83  ?  128  ASN   C ND2   1 
ATOM   13023 N  N     . ILE   C 2 130 ? 118.771 106.553 112.866 1.00 64.64  ?  129  ILE   C N     1 
ATOM   13024 C  CA    . ILE   C 2 130 ? 118.840 105.124 113.164 1.00 57.97  ?  129  ILE   C CA    1 
ATOM   13025 C  C     . ILE   C 2 130 ? 119.999 104.419 112.471 1.00 60.30  ?  129  ILE   C C     1 
ATOM   13026 O  O     . ILE   C 2 130 ? 120.366 103.310 112.880 1.00 67.76  ?  129  ILE   C O     1 
ATOM   13027 C  CB    . ILE   C 2 130 ? 117.527 104.413 112.798 1.00 60.92  ?  129  ILE   C CB    1 
ATOM   13028 C  CG1   . ILE   C 2 130 ? 117.352 104.354 111.280 1.00 54.76  ?  129  ILE   C CG1   1 
ATOM   13029 C  CG2   . ILE   C 2 130 ? 116.345 105.109 113.456 1.00 63.08  ?  129  ILE   C CG2   1 
ATOM   13030 C  CD1   . ILE   C 2 130 ? 116.039 103.753 110.841 1.00 60.36  ?  129  ILE   C CD1   1 
ATOM   13031 N  N     . VAL   C 2 131 ? 120.593 105.019 111.444 1.00 71.62  ?  130  VAL   C N     1 
ATOM   13032 C  CA    . VAL   C 2 131 ? 121.627 104.373 110.642 1.00 74.31  ?  130  VAL   C CA    1 
ATOM   13033 C  C     . VAL   C 2 131 ? 122.946 105.098 110.868 1.00 81.34  ?  130  VAL   C C     1 
ATOM   13034 O  O     . VAL   C 2 131 ? 123.003 106.332 110.811 1.00 87.92  ?  130  VAL   C O     1 
ATOM   13035 C  CB    . VAL   C 2 131 ? 121.248 104.351 109.150 1.00 70.88  ?  130  VAL   C CB    1 
ATOM   13036 C  CG1   . VAL   C 2 131 ? 122.434 103.931 108.303 1.00 73.92  ?  130  VAL   C CG1   1 
ATOM   13037 C  CG2   . VAL   C 2 131 ? 120.075 103.409 108.923 1.00 76.25  ?  130  VAL   C CG2   1 
ATOM   13038 N  N     . ASN   C 2 132 ? 124.006 104.330 111.125 1.00 89.31  ?  131  ASN   C N     1 
ATOM   13039 C  CA    . ASN   C 2 132 ? 125.316 104.910 111.389 1.00 85.76  ?  131  ASN   C CA    1 
ATOM   13040 C  C     . ASN   C 2 132 ? 126.001 105.437 110.135 1.00 86.19  ?  131  ASN   C C     1 
ATOM   13041 O  O     . ASN   C 2 132 ? 126.998 106.155 110.257 1.00 85.88  ?  131  ASN   C O     1 
ATOM   13042 C  CB    . ASN   C 2 132 ? 126.212 103.872 112.070 1.00 88.31  ?  131  ASN   C CB    1 
ATOM   13043 C  CG    . ASN   C 2 132 ? 127.291 104.500 112.926 1.00 93.27  ?  131  ASN   C CG    1 
ATOM   13044 O  OD1   . ASN   C 2 132 ? 127.170 104.562 114.148 1.00 95.55  ?  131  ASN   C OD1   1 
ATOM   13045 N  ND2   . ASN   C 2 132 ? 128.356 104.969 112.287 1.00 91.09  ?  131  ASN   C ND2   1 
ATOM   13046 N  N     . ASP   C 2 133 ? 125.524 105.068 108.947 1.00 92.39  ?  132  ASP   C N     1 
ATOM   13047 C  CA    . ASP   C 2 133 ? 126.083 105.569 107.692 1.00 94.14  ?  132  ASP   C CA    1 
ATOM   13048 C  C     . ASP   C 2 133 ? 124.943 105.697 106.699 1.00 96.04  ?  132  ASP   C C     1 
ATOM   13049 O  O     . ASP   C 2 133 ? 124.627 104.753 105.963 1.00 96.78  ?  132  ASP   C O     1 
ATOM   13050 C  CB    . ASP   C 2 133 ? 127.182 104.655 107.154 1.00 97.46  ?  132  ASP   C CB    1 
ATOM   13051 C  CG    . ASP   C 2 133 ? 127.889 105.238 105.947 1.00 101.79 ?  132  ASP   C CG    1 
ATOM   13052 O  OD1   . ASP   C 2 133 ? 127.578 106.386 105.566 1.00 100.60 ?  132  ASP   C OD1   1 
ATOM   13053 O  OD2   . ASP   C 2 133 ? 128.761 104.547 105.380 1.00 103.48 ?  132  ASP   C OD2   1 
ATOM   13054 N  N     . PRO   C 2 134 ? 124.292 106.862 106.650 1.00 87.89  ?  133  PRO   C N     1 
ATOM   13055 C  CA    . PRO   C 2 134 ? 123.085 107.000 105.822 1.00 83.52  ?  133  PRO   C CA    1 
ATOM   13056 C  C     . PRO   C 2 134 ? 123.362 107.080 104.330 1.00 78.66  ?  133  PRO   C C     1 
ATOM   13057 O  O     . PRO   C 2 134 ? 122.404 107.071 103.547 1.00 81.99  ?  133  PRO   C O     1 
ATOM   13058 C  CB    . PRO   C 2 134 ? 122.451 108.305 106.333 1.00 81.29  ?  133  PRO   C CB    1 
ATOM   13059 C  CG    . PRO   C 2 134 ? 123.398 108.863 107.385 1.00 78.71  ?  133  PRO   C CG    1 
ATOM   13060 C  CD    . PRO   C 2 134 ? 124.692 108.137 107.264 1.00 81.51  ?  133  PRO   C CD    1 
ATOM   13061 N  N     . SER   C 2 135 ? 124.619 107.246 103.915 1.00 83.44  ?  134  SER   C N     1 
ATOM   13062 C  CA    . SER   C 2 135 ? 124.921 107.305 102.489 1.00 83.59  ?  134  SER   C CA    1 
ATOM   13063 C  C     . SER   C 2 135 ? 124.567 105.991 101.809 1.00 84.24  ?  134  SER   C C     1 
ATOM   13064 O  O     . SER   C 2 135 ? 124.083 105.980 100.671 1.00 89.16  ?  134  SER   C O     1 
ATOM   13065 C  CB    . SER   C 2 135 ? 126.397 107.644 102.276 1.00 87.99  ?  134  SER   C CB    1 
ATOM   13066 O  OG    . SER   C 2 135 ? 126.649 109.010 102.554 1.00 92.86  ?  134  SER   C OG    1 
ATOM   13067 N  N     . VAL   C 2 136 ? 124.777 104.873 102.510 1.00 81.48  ?  135  VAL   C N     1 
ATOM   13068 C  CA    . VAL   C 2 136 ? 124.508 103.532 101.905 1.00 83.46  ?  135  VAL   C CA    1 
ATOM   13069 C  C     . VAL   C 2 136 ? 122.996 103.349 101.732 1.00 85.02  ?  135  VAL   C C     1 
ATOM   13070 O  O     . VAL   C 2 136 ? 122.601 102.503 100.906 1.00 83.52  ?  135  VAL   C O     1 
ATOM   13071 C  CB    . VAL   C 2 136 ? 125.119 102.401 102.755 1.00 81.86  ?  135  VAL   C CB    1 
ATOM   13072 C  CG1   . VAL   C 2 136 ? 126.588 102.659 103.056 1.00 81.13  ?  135  VAL   C CG1   1 
ATOM   13073 C  CG2   . VAL   C 2 136 ? 124.343 102.175 104.043 1.00 85.07  ?  135  VAL   C CG2   1 
ATOM   13074 N  N     . VAL   C 2 137 ? 122.187 104.112 102.472 1.00 76.14  ?  136  VAL   C N     1 
ATOM   13075 C  CA    . VAL   C 2 137 ? 120.735 103.990 102.405 1.00 71.39  ?  136  VAL   C CA    1 
ATOM   13076 C  C     . VAL   C 2 137 ? 120.146 104.930 101.365 1.00 73.91  ?  136  VAL   C C     1 
ATOM   13077 O  O     . VAL   C 2 137 ? 119.291 104.531 100.572 1.00 82.26  ?  136  VAL   C O     1 
ATOM   13078 C  CB    . VAL   C 2 137 ? 120.122 104.238 103.801 1.00 70.55  ?  136  VAL   C CB    1 
ATOM   13079 C  CG1   . VAL   C 2 137 ? 118.612 104.397 103.703 1.00 70.97  ?  136  VAL   C CG1   1 
ATOM   13080 C  CG2   . VAL   C 2 137 ? 120.481 103.103 104.748 1.00 71.33  ?  136  VAL   C CG2   1 
ATOM   13081 N  N     . PHE   C 2 138 ? 120.598 106.186 101.341 1.00 70.41  ?  137  PHE   C N     1 
ATOM   13082 C  CA    . PHE   C 2 138 ? 120.049 107.152 100.394 1.00 71.36  ?  137  PHE   C CA    1 
ATOM   13083 C  C     . PHE   C 2 138 ? 120.443 106.828 98.960  1.00 76.12  ?  137  PHE   C C     1 
ATOM   13084 O  O     . PHE   C 2 138 ? 119.716 107.182 98.025  1.00 81.80  ?  137  PHE   C O     1 
ATOM   13085 C  CB    . PHE   C 2 138 ? 120.503 108.562 100.764 1.00 68.08  ?  137  PHE   C CB    1 
ATOM   13086 C  CG    . PHE   C 2 138 ? 119.984 109.033 102.088 1.00 73.06  ?  137  PHE   C CG    1 
ATOM   13087 C  CD1   . PHE   C 2 138 ? 118.680 108.768 102.466 1.00 72.08  ?  137  PHE   C CD1   1 
ATOM   13088 C  CD2   . PHE   C 2 138 ? 120.800 109.732 102.960 1.00 77.50  ?  137  PHE   C CD2   1 
ATOM   13089 C  CE1   . PHE   C 2 138 ? 118.198 109.195 103.684 1.00 70.02  ?  137  PHE   C CE1   1 
ATOM   13090 C  CE2   . PHE   C 2 138 ? 120.322 110.162 104.181 1.00 74.44  ?  137  PHE   C CE2   1 
ATOM   13091 C  CZ    . PHE   C 2 138 ? 119.020 109.892 104.542 1.00 69.95  ?  137  PHE   C CZ    1 
ATOM   13092 N  N     . ASP   C 2 139 ? 121.584 106.166 98.763  1.00 90.61  ?  138  ASP   C N     1 
ATOM   13093 C  CA    . ASP   C 2 139 ? 122.004 105.805 97.415  1.00 92.92  ?  138  ASP   C CA    1 
ATOM   13094 C  C     . ASP   C 2 139 ? 121.202 104.642 96.849  1.00 93.58  ?  138  ASP   C C     1 
ATOM   13095 O  O     . ASP   C 2 139 ? 121.126 104.497 95.625  1.00 100.04 ?  138  ASP   C O     1 
ATOM   13096 C  CB    . ASP   C 2 139 ? 123.495 105.473 97.403  1.00 95.83  ?  138  ASP   C CB    1 
ATOM   13097 C  CG    . ASP   C 2 139 ? 124.365 106.700 97.575  1.00 101.64 ?  138  ASP   C CG    1 
ATOM   13098 O  OD1   . ASP   C 2 139 ? 123.983 107.778 97.072  1.00 100.23 ?  138  ASP   C OD1   1 
ATOM   13099 O  OD2   . ASP   C 2 139 ? 125.434 106.593 98.214  1.00 101.66 ?  138  ASP   C OD2   1 
ATOM   13100 N  N     . ASP   C 2 140 ? 120.610 103.812 97.702  1.00 83.98  ?  139  ASP   C N     1 
ATOM   13101 C  CA    . ASP   C 2 140 ? 119.764 102.708 97.252  1.00 87.86  ?  139  ASP   C CA    1 
ATOM   13102 C  C     . ASP   C 2 140 ? 118.291 103.112 97.285  1.00 91.48  ?  139  ASP   C C     1 
ATOM   13103 O  O     . ASP   C 2 140 ? 117.453 102.483 97.929  1.00 95.83  ?  139  ASP   C O     1 
ATOM   13104 C  CB    . ASP   C 2 140 ? 120.017 101.468 98.104  1.00 91.11  ?  139  ASP   C CB    1 
ATOM   13105 C  CG    . ASP   C 2 140 ? 119.411 100.214 97.505  1.00 96.89  ?  139  ASP   C CG    1 
ATOM   13106 O  OD1   . ASP   C 2 140 ? 119.989 99.677  96.538  1.00 100.62 ?  139  ASP   C OD1   1 
ATOM   13107 O  OD2   . ASP   C 2 140 ? 118.354 99.767  98.000  1.00 94.61  ?  139  ASP   C OD2   1 
ATOM   13108 N  N     . ILE   C 2 141 ? 117.978 104.190 96.571  1.00 77.26  ?  140  ILE   C N     1 
ATOM   13109 C  CA    . ILE   C 2 141 ? 116.609 104.688 96.506  1.00 71.10  ?  140  ILE   C CA    1 
ATOM   13110 C  C     . ILE   C 2 141 ? 116.180 104.800 95.050  1.00 75.10  ?  140  ILE   C C     1 
ATOM   13111 O  O     . ILE   C 2 141 ? 115.162 104.229 94.643  1.00 79.39  ?  140  ILE   C O     1 
ATOM   13112 C  CB    . ILE   C 2 141 ? 116.467 106.038 97.230  1.00 69.44  ?  140  ILE   C CB    1 
ATOM   13113 C  CG1   . ILE   C 2 141 ? 116.662 105.857 98.736  1.00 69.23  ?  140  ILE   C CG1   1 
ATOM   13114 C  CG2   . ILE   C 2 141 ? 115.104 106.648 96.944  1.00 71.60  ?  140  ILE   C CG2   1 
ATOM   13115 C  CD1   . ILE   C 2 141 ? 116.302 107.076 99.555  1.00 65.71  ?  140  ILE   C CD1   1 
ATOM   13116 N  N     . VAL   C 2 142 ? 116.952 105.542 94.255  1.00 82.37  ?  141  VAL   C N     1 
ATOM   13117 C  CA    . VAL   C 2 142 ? 116.616 105.719 92.850  1.00 81.95  ?  141  VAL   C CA    1 
ATOM   13118 C  C     . VAL   C 2 142 ? 116.902 104.455 92.047  1.00 85.10  ?  141  VAL   C C     1 
ATOM   13119 O  O     . VAL   C 2 142 ? 116.411 104.313 90.921  1.00 92.05  ?  141  VAL   C O     1 
ATOM   13120 C  CB    . VAL   C 2 142 ? 117.382 106.940 92.298  1.00 79.15  ?  141  VAL   C CB    1 
ATOM   13121 C  CG1   . VAL   C 2 142 ? 116.943 107.284 90.884  1.00 81.79  ?  141  VAL   C CG1   1 
ATOM   13122 C  CG2   . VAL   C 2 142 ? 117.185 108.141 93.215  1.00 82.76  ?  141  VAL   C CG2   1 
ATOM   13123 N  N     . THR   C 2 143 ? 117.724 103.548 92.574  1.00 87.78  ?  142  THR   C N     1 
ATOM   13124 C  CA    . THR   C 2 143 ? 118.067 102.318 91.874  1.00 88.30  ?  142  THR   C CA    1 
ATOM   13125 C  C     . THR   C 2 143 ? 117.330 101.095 92.404  1.00 88.52  ?  142  THR   C C     1 
ATOM   13126 O  O     . THR   C 2 143 ? 117.447 100.020 91.809  1.00 91.65  ?  142  THR   C O     1 
ATOM   13127 C  CB    . THR   C 2 143 ? 119.578 102.058 91.946  1.00 90.70  ?  142  THR   C CB    1 
ATOM   13128 O  OG1   . THR   C 2 143 ? 120.065 102.415 93.245  1.00 96.91  ?  142  THR   C OG1   1 
ATOM   13129 C  CG2   . THR   C 2 143 ? 120.307 102.873 90.893  1.00 87.48  ?  142  THR   C CG2   1 
ATOM   13130 N  N     . ASN   C 2 144 ? 116.584 101.223 93.498  1.00 83.90  ?  143  ASN   C N     1 
ATOM   13131 C  CA    . ASN   C 2 144 ? 115.827 100.093 94.021  1.00 83.65  ?  143  ASN   C CA    1 
ATOM   13132 C  C     . ASN   C 2 144 ? 114.719 99.718  93.047  1.00 84.46  ?  143  ASN   C C     1 
ATOM   13133 O  O     . ASN   C 2 144 ? 113.946 100.576 92.612  1.00 89.86  ?  143  ASN   C O     1 
ATOM   13134 C  CB    . ASN   C 2 144 ? 115.246 100.440 95.389  1.00 82.21  ?  143  ASN   C CB    1 
ATOM   13135 C  CG    . ASN   C 2 144 ? 114.801 99.217  96.164  1.00 81.44  ?  143  ASN   C CG    1 
ATOM   13136 O  OD1   . ASN   C 2 144 ? 113.858 98.528  95.776  1.00 88.62  ?  143  ASN   C OD1   1 
ATOM   13137 N  ND2   . ASN   C 2 144 ? 115.475 98.945  97.272  1.00 79.98  ?  143  ASN   C ND2   1 
ATOM   13138 N  N     . GLU   C 2 145 ? 114.663 98.433  92.684  1.00 88.75  ?  144  GLU   C N     1 
ATOM   13139 C  CA    . GLU   C 2 145 ? 113.726 97.992  91.657  1.00 87.08  ?  144  GLU   C CA    1 
ATOM   13140 C  C     . GLU   C 2 145 ? 112.287 98.114  92.133  1.00 88.34  ?  144  GLU   C C     1 
ATOM   13141 O  O     . GLU   C 2 145 ? 111.429 98.641  91.418  1.00 93.56  ?  144  GLU   C O     1 
ATOM   13142 C  CB    . GLU   C 2 145 ? 114.032 96.554  91.241  1.00 89.58  ?  144  GLU   C CB    1 
ATOM   13143 C  CG    . GLU   C 2 145 ? 114.117 96.361  89.736  1.00 96.40  ?  144  GLU   C CG    1 
ATOM   13144 C  CD    . GLU   C 2 145 ? 113.803 94.937  89.314  1.00 100.37 ?  144  GLU   C CD    1 
ATOM   13145 O  OE1   . GLU   C 2 145 ? 113.163 94.758  88.256  1.00 98.30  ?  144  GLU   C OE1   1 
ATOM   13146 O  OE2   . GLU   C 2 145 ? 114.193 93.997  90.039  1.00 99.69  ?  144  GLU   C OE2   1 
ATOM   13147 N  N     . GLN   C 2 146 ? 112.002 97.640  93.341  1.00 79.64  ?  145  GLN   C N     1 
ATOM   13148 C  CA    A GLN   C 2 146 ? 110.634 97.695  93.838  0.50 81.92  ?  145  GLN   C CA    1 
ATOM   13149 C  CA    B GLN   C 2 146 ? 110.734 97.695  93.838  0.50 81.92  ?  145  GLN   C CA    1 
ATOM   13150 C  C     . GLN   C 2 146 ? 110.194 99.132  94.098  1.00 83.93  ?  145  GLN   C C     1 
ATOM   13151 O  O     . GLN   C 2 146 ? 109.025 99.481  93.886  1.00 88.84  ?  145  GLN   C O     1 
ATOM   13152 C  CB    A GLN   C 2 146 ? 110.509 96.877  95.118  0.50 80.16  ?  145  GLN   C CB    1 
ATOM   13153 C  CB    B GLN   C 2 146 ? 110.609 96.877  95.118  0.50 80.16  ?  145  GLN   C CB    1 
ATOM   13154 C  CG    A GLN   C 2 146 ? 110.744 95.376  95.042  0.50 81.55  ?  145  GLN   C CG    1 
ATOM   13155 C  CG    B GLN   C 2 146 ? 110.775 95.367  95.030  0.50 81.55  ?  145  GLN   C CG    1 
ATOM   13156 C  CD    A GLN   C 2 146 ? 112.185 95.016  94.746  0.50 89.05  ?  145  GLN   C CD    1 
ATOM   13157 C  CD    B GLN   C 2 146 ? 109.759 94.712  94.117  0.50 89.05  ?  145  GLN   C CD    1 
ATOM   13158 O  OE1   A GLN   C 2 146 ? 113.097 95.785  95.039  0.50 90.79  ?  145  GLN   C OE1   1 
ATOM   13159 O  OE1   B GLN   C 2 146 ? 108.589 95.087  94.108  0.50 90.79  ?  145  GLN   C OE1   1 
ATOM   13160 N  NE2   A GLN   C 2 146 ? 112.399 93.840  94.160  0.50 88.20  ?  145  GLN   C NE2   1 
ATOM   13161 N  NE2   B GLN   C 2 146 ? 110.202 93.725  93.341  0.50 88.20  ?  145  GLN   C NE2   1 
ATOM   13162 N  N     . ILE   C 2 147 ? 111.113 99.972  94.583  1.00 67.99  ?  146  ILE   C N     1 
ATOM   13163 C  CA    . ILE   C 2 147 ? 110.797 101.377 94.815  1.00 68.02  ?  146  ILE   C CA    1 
ATOM   13164 C  C     . ILE   C 2 147 ? 110.443 102.064 93.504  1.00 71.29  ?  146  ILE   C C     1 
ATOM   13165 O  O     . ILE   C 2 147 ? 109.479 102.835 93.433  1.00 81.99  ?  146  ILE   C O     1 
ATOM   13166 C  CB    . ILE   C 2 147 ? 111.964 102.077 95.536  1.00 67.55  ?  146  ILE   C CB    1 
ATOM   13167 C  CG1   . ILE   C 2 147 ? 111.854 101.887 97.048  1.00 68.63  ?  146  ILE   C CG1   1 
ATOM   13168 C  CG2   . ILE   C 2 147 ? 111.994 103.556 95.196  1.00 69.26  ?  146  ILE   C CG2   1 
ATOM   13169 C  CD1   . ILE   C 2 147 ? 113.000 102.499 97.820  1.00 66.89  ?  146  ILE   C CD1   1 
ATOM   13170 N  N     . GLN   C 2 148 ? 111.193 101.771 92.439  1.00 77.54  ?  147  GLN   C N     1 
ATOM   13171 C  CA    . GLN   C 2 148 ? 110.861 102.306 91.123  1.00 75.52  ?  147  GLN   C CA    1 
ATOM   13172 C  C     . GLN   C 2 148 ? 109.527 101.766 90.623  1.00 79.25  ?  147  GLN   C C     1 
ATOM   13173 O  O     . GLN   C 2 148 ? 108.741 102.504 90.017  1.00 85.27  ?  147  GLN   C O     1 
ATOM   13174 C  CB    . GLN   C 2 148 ? 111.978 101.980 90.135  1.00 78.08  ?  147  GLN   C CB    1 
ATOM   13175 C  CG    . GLN   C 2 148 ? 113.126 102.971 90.147  1.00 80.95  ?  147  GLN   C CG    1 
ATOM   13176 C  CD    . GLN   C 2 148 ? 114.030 102.824 88.941  1.00 89.62  ?  147  GLN   C CD    1 
ATOM   13177 O  OE1   . GLN   C 2 148 ? 113.572 102.851 87.799  1.00 90.87  ?  147  GLN   C OE1   1 
ATOM   13178 N  NE2   . GLN   C 2 148 ? 115.325 102.670 89.189  1.00 86.95  ?  147  GLN   C NE2   1 
ATOM   13179 N  N     . LYS   C 2 149 ? 109.255 100.481 90.861  1.00 77.99  ?  148  LYS   C N     1 
ATOM   13180 C  CA    . LYS   C 2 149 ? 107.993 99.898  90.415  1.00 80.76  ?  148  LYS   C CA    1 
ATOM   13181 C  C     . LYS   C 2 149 ? 106.802 100.483 91.163  1.00 83.46  ?  148  LYS   C C     1 
ATOM   13182 O  O     . LYS   C 2 149 ? 105.681 100.476 90.642  1.00 88.14  ?  148  LYS   C O     1 
ATOM   13183 C  CB    . LYS   C 2 149 ? 108.021 98.379  90.584  1.00 79.23  ?  148  LYS   C CB    1 
ATOM   13184 C  CG    . LYS   C 2 149 ? 108.957 97.663  89.631  1.00 83.27  ?  148  LYS   C CG    1 
ATOM   13185 C  CD    . LYS   C 2 149 ? 109.131 96.205  90.023  1.00 86.56  ?  148  LYS   C CD    1 
ATOM   13186 C  CE    . LYS   C 2 149 ? 109.135 95.304  88.799  1.00 86.15  ?  148  LYS   C CE    1 
ATOM   13187 N  NZ    . LYS   C 2 149 ? 108.302 95.864  87.699  1.00 85.01  ?  148  LYS   C NZ    1 
ATOM   13188 N  N     . ARG   C 2 150 ? 107.018 100.984 92.377  1.00 71.16  ?  149  ARG   C N     1 
ATOM   13189 C  CA    . ARG   C 2 150 ? 105.946 101.534 93.194  1.00 69.63  ?  149  ARG   C CA    1 
ATOM   13190 C  C     . ARG   C 2 150 ? 105.848 103.054 93.102  1.00 73.61  ?  149  ARG   C C     1 
ATOM   13191 O  O     . ARG   C 2 150 ? 105.086 103.659 93.861  1.00 77.26  ?  149  ARG   C O     1 
ATOM   13192 C  CB    . ARG   C 2 150 ? 106.132 101.107 94.652  1.00 64.83  ?  149  ARG   C CB    1 
ATOM   13193 C  CG    . ARG   C 2 150 ? 104.838 100.877 95.414  1.00 62.42  ?  149  ARG   C CG    1 
ATOM   13194 C  CD    . ARG   C 2 150 ? 105.064 101.000 96.911  1.00 65.69  ?  149  ARG   C CD    1 
ATOM   13195 N  NE    . ARG   C 2 150 ? 103.813 101.038 97.659  1.00 69.80  ?  149  ARG   C NE    1 
ATOM   13196 C  CZ    . ARG   C 2 150 ? 103.704 101.455 98.913  1.00 70.35  ?  149  ARG   C CZ    1 
ATOM   13197 N  NH1   . ARG   C 2 150 ? 104.752 101.887 99.591  1.00 61.76  ?  149  ARG   C NH1   1 
ATOM   13198 N  NH2   . ARG   C 2 150 ? 102.511 101.438 99.500  1.00 73.71  ?  149  ARG   C NH2   1 
ATOM   13199 N  N     . ALA   C 2 151 ? 106.582 103.684 92.185  1.00 80.97  ?  150  ALA   C N     1 
ATOM   13200 C  CA    . ALA   C 2 151 ? 106.656 105.140 92.140  1.00 78.39  ?  150  ALA   C CA    1 
ATOM   13201 C  C     . ALA   C 2 151 ? 106.430 105.748 90.765  1.00 87.44  ?  150  ALA   C C     1 
ATOM   13202 O  O     . ALA   C 2 151 ? 106.163 106.953 90.691  1.00 91.26  ?  150  ALA   C O     1 
ATOM   13203 C  CB    . ALA   C 2 151 ? 108.016 105.626 92.664  1.00 76.37  ?  150  ALA   C CB    1 
ATOM   13204 N  N     . GLU   C 2 152 ? 106.527 104.977 89.679  1.00 100.73 ?  151  GLU   C N     1 
ATOM   13205 C  CA    . GLU   C 2 152 ? 106.428 105.573 88.349  1.00 101.89 ?  151  GLU   C CA    1 
ATOM   13206 C  C     . GLU   C 2 152 ? 104.996 105.967 88.003  1.00 100.96 ?  151  GLU   C C     1 
ATOM   13207 O  O     . GLU   C 2 152 ? 104.788 106.894 87.208  1.00 101.33 ?  151  GLU   C O     1 
ATOM   13208 C  CB    . GLU   C 2 152 ? 106.991 104.612 87.300  1.00 101.68 ?  151  GLU   C CB    1 
ATOM   13209 C  CG    . GLU   C 2 152 ? 105.954 103.735 86.613  1.00 105.08 ?  151  GLU   C CG    1 
ATOM   13210 C  CD    . GLU   C 2 152 ? 105.636 102.478 87.399  1.00 107.00 ?  151  GLU   C CD    1 
ATOM   13211 O  OE1   . GLU   C 2 152 ? 106.015 102.403 88.586  1.00 107.76 ?  151  GLU   C OE1   1 
ATOM   13212 O  OE2   . GLU   C 2 152 ? 105.003 101.565 86.830  1.00 106.27 ?  151  GLU   C OE2   1 
ATOM   13213 N  N     . GLY   C 2 153 ? 104.005 105.305 88.603  1.00 87.30  ?  152  GLY   C N     1 
ATOM   13214 C  CA    . GLY   C 2 153 ? 102.611 105.545 88.282  1.00 88.84  ?  152  GLY   C CA    1 
ATOM   13215 C  C     . GLY   C 2 153 ? 102.069 106.841 88.845  1.00 93.01  ?  152  GLY   C C     1 
ATOM   13216 O  O     . GLY   C 2 153 ? 100.853 107.058 88.865  1.00 100.61 ?  152  GLY   C O     1 
ATOM   13217 N  N     . ILE   C 2 154 ? 102.966 107.705 89.319  1.00 77.46  ?  153  ILE   C N     1 
ATOM   13218 C  CA    . ILE   C 2 154 ? 102.627 109.047 89.773  1.00 76.44  ?  153  ILE   C CA    1 
ATOM   13219 C  C     . ILE   C 2 154 ? 103.406 110.100 89.000  1.00 78.40  ?  153  ILE   C C     1 
ATOM   13220 O  O     . ILE   C 2 154 ? 102.826 111.056 88.463  1.00 85.50  ?  153  ILE   C O     1 
ATOM   13221 C  CB    . ILE   C 2 154 ? 102.859 109.203 91.292  1.00 74.53  ?  153  ILE   C CB    1 
ATOM   13222 C  CG1   . ILE   C 2 154 ? 102.002 108.208 92.076  1.00 79.23  ?  153  ILE   C CG1   1 
ATOM   13223 C  CG2   . ILE   C 2 154 ? 102.577 110.633 91.732  1.00 78.54  ?  153  ILE   C CG2   1 
ATOM   13224 C  CD1   . ILE   C 2 154 ? 102.784 107.427 93.110  1.00 78.70  ?  153  ILE   C CD1   1 
ATOM   13225 N  N     . SER   C 2 155 ? 104.728 109.922 88.901  1.00 75.06  ?  154  SER   C N     1 
ATOM   13226 C  CA    . SER   C 2 155 ? 105.551 110.816 88.104  1.00 76.53  ?  154  SER   C CA    1 
ATOM   13227 C  C     . SER   C 2 155 ? 105.150 110.778 86.641  1.00 74.05  ?  154  SER   C C     1 
ATOM   13228 O  O     . SER   C 2 155 ? 105.264 111.790 85.948  1.00 76.57  ?  154  SER   C O     1 
ATOM   13229 C  CB    . SER   C 2 155 ? 107.026 110.450 88.261  1.00 73.80  ?  154  SER   C CB    1 
ATOM   13230 O  OG    . SER   C 2 155 ? 107.432 109.535 87.258  1.00 80.40  ?  154  SER   C OG    1 
ATOM   13231 N  N     . SER   C 2 156 ? 104.664 109.636 86.151  1.00 76.35  ?  155  SER   C N     1 
ATOM   13232 C  CA    . SER   C 2 156 ? 104.229 109.580 84.760  1.00 74.91  ?  155  SER   C CA    1 
ATOM   13233 C  C     . SER   C 2 156 ? 103.055 110.522 84.517  1.00 78.07  ?  155  SER   C C     1 
ATOM   13234 O  O     . SER   C 2 156 ? 103.093 111.355 83.604  1.00 82.78  ?  155  SER   C O     1 
ATOM   13235 C  CB    . SER   C 2 156 ? 103.865 108.147 84.378  1.00 76.23  ?  155  SER   C CB    1 
ATOM   13236 O  OG    . SER   C 2 156 ? 102.560 107.812 84.815  1.00 83.35  ?  155  SER   C OG    1 
ATOM   13237 N  N     . TYR   C 2 157 ? 102.011 110.417 85.345  1.00 76.82  ?  156  TYR   C N     1 
ATOM   13238 C  CA    . TYR   C 2 157 ? 100.853 111.297 85.205  1.00 72.93  ?  156  TYR   C CA    1 
ATOM   13239 C  C     . TYR   C 2 157 ? 101.250 112.756 85.373  1.00 70.89  ?  156  TYR   C C     1 
ATOM   13240 O  O     . TYR   C 2 157 ? 100.778 113.628 84.629  1.00 77.57  ?  156  TYR   C O     1 
ATOM   13241 C  CB    . TYR   C 2 157 ? 99.775  110.921 86.223  1.00 70.53  ?  156  TYR   C CB    1 
ATOM   13242 C  CG    . TYR   C 2 157 ? 99.044  109.640 85.900  1.00 75.59  ?  156  TYR   C CG    1 
ATOM   13243 C  CD1   . TYR   C 2 157 ? 98.035  109.616 84.950  1.00 76.02  ?  156  TYR   C CD1   1 
ATOM   13244 C  CD2   . TYR   C 2 157 ? 99.359  108.456 86.548  1.00 75.70  ?  156  TYR   C CD2   1 
ATOM   13245 C  CE1   . TYR   C 2 157 ? 97.367  108.446 84.647  1.00 76.10  ?  156  TYR   C CE1   1 
ATOM   13246 C  CE2   . TYR   C 2 157 ? 98.696  107.282 86.255  1.00 76.65  ?  156  TYR   C CE2   1 
ATOM   13247 C  CZ    . TYR   C 2 157 ? 97.701  107.282 85.303  1.00 78.99  ?  156  TYR   C CZ    1 
ATOM   13248 O  OH    . TYR   C 2 157 ? 97.037  106.114 85.008  1.00 82.44  ?  156  TYR   C OH    1 
ATOM   13249 N  N     . TYR   C 2 158 ? 102.124 113.040 86.343  1.00 66.70  ?  157  TYR   C N     1 
ATOM   13250 C  CA    . TYR   C 2 158 ? 102.609 114.405 86.519  1.00 62.11  ?  157  TYR   C CA    1 
ATOM   13251 C  C     . TYR   C 2 158 ? 103.298 114.910 85.258  1.00 70.95  ?  157  TYR   C C     1 
ATOM   13252 O  O     . TYR   C 2 158 ? 103.078 116.050 84.833  1.00 80.55  ?  157  TYR   C O     1 
ATOM   13253 C  CB    . TYR   C 2 158 ? 103.566 114.467 87.708  1.00 70.35  ?  157  TYR   C CB    1 
ATOM   13254 C  CG    . TYR   C 2 158 ? 102.912 114.835 89.017  1.00 72.91  ?  157  TYR   C CG    1 
ATOM   13255 C  CD1   . TYR   C 2 158 ? 102.210 116.022 89.152  1.00 73.44  ?  157  TYR   C CD1   1 
ATOM   13256 C  CD2   . TYR   C 2 158 ? 103.006 114.000 90.122  1.00 72.09  ?  157  TYR   C CD2   1 
ATOM   13257 C  CE1   . TYR   C 2 158 ? 101.617 116.367 90.347  1.00 77.67  ?  157  TYR   C CE1   1 
ATOM   13258 C  CE2   . TYR   C 2 158 ? 102.413 114.336 91.322  1.00 70.46  ?  157  TYR   C CE2   1 
ATOM   13259 C  CZ    . TYR   C 2 158 ? 101.718 115.522 91.429  1.00 75.80  ?  157  TYR   C CZ    1 
ATOM   13260 O  OH    . TYR   C 2 158 ? 101.129 115.870 92.621  1.00 77.47  ?  157  TYR   C OH    1 
ATOM   13261 N  N     . ASP   C 2 159 ? 104.134 114.070 84.646  1.00 76.92  ?  158  ASP   C N     1 
ATOM   13262 C  CA    . ASP   C 2 159 ? 104.870 114.469 83.453  1.00 76.52  ?  158  ASP   C CA    1 
ATOM   13263 C  C     . ASP   C 2 159 ? 103.934 114.721 82.282  1.00 77.76  ?  158  ASP   C C     1 
ATOM   13264 O  O     . ASP   C 2 159 ? 104.113 115.688 81.537  1.00 81.77  ?  158  ASP   C O     1 
ATOM   13265 C  CB    . ASP   C 2 159 ? 105.899 113.401 83.097  1.00 79.33  ?  158  ASP   C CB    1 
ATOM   13266 C  CG    . ASP   C 2 159 ? 107.078 113.389 84.041  1.00 85.77  ?  158  ASP   C CG    1 
ATOM   13267 O  OD1   . ASP   C 2 159 ? 107.126 114.246 84.944  1.00 84.01  ?  158  ASP   C OD1   1 
ATOM   13268 O  OD2   . ASP   C 2 159 ? 107.959 112.518 83.876  1.00 89.36  ?  158  ASP   C OD2   1 
ATOM   13269 N  N     . GLU   C 2 160 ? 102.921 113.872 82.115  1.00 79.23  ?  159  GLU   C N     1 
ATOM   13270 C  CA    . GLU   C 2 160 ? 101.966 114.071 81.031  1.00 74.45  ?  159  GLU   C CA    1 
ATOM   13271 C  C     . GLU   C 2 160 ? 101.199 115.374 81.211  1.00 76.82  ?  159  GLU   C C     1 
ATOM   13272 O  O     . GLU   C 2 160 ? 100.996 116.135 80.246  1.00 81.02  ?  159  GLU   C O     1 
ATOM   13273 C  CB    . GLU   C 2 160 ? 101.001 112.892 80.974  1.00 76.09  ?  159  GLU   C CB    1 
ATOM   13274 C  CG    . GLU   C 2 160 ? 101.642 111.513 80.918  1.00 83.68  ?  159  GLU   C CG    1 
ATOM   13275 C  CD    . GLU   C 2 160 ? 102.007 111.045 79.530  1.00 90.24  ?  159  GLU   C CD    1 
ATOM   13276 O  OE1   . GLU   C 2 160 ? 102.656 109.985 79.409  1.00 89.33  ?  159  GLU   C OE1   1 
ATOM   13277 O  OE2   . GLU   C 2 160 ? 101.655 111.749 78.562  1.00 92.64  ?  159  GLU   C OE2   1 
ATOM   13278 N  N     . LEU   C 2 161 ? 100.777 115.648 82.451  1.00 66.66  ?  160  LEU   C N     1 
ATOM   13279 C  CA    . LEU   C 2 161 ? 100.064 116.884 82.750  1.00 58.31  ?  160  LEU   C CA    1 
ATOM   13280 C  C     . LEU   C 2 161 ? 100.937 118.099 82.470  1.00 65.08  ?  160  LEU   C C     1 
ATOM   13281 O  O     . LEU   C 2 161 ? 100.489 119.063 81.842  1.00 76.87  ?  160  LEU   C O     1 
ATOM   13282 C  CB    . LEU   C 2 161 ? 99.596  116.881 84.205  1.00 60.37  ?  160  LEU   C CB    1 
ATOM   13283 C  CG    . LEU   C 2 161 ? 98.820  118.110 84.680  1.00 62.77  ?  160  LEU   C CG    1 
ATOM   13284 C  CD1   . LEU   C 2 161 ? 97.672  118.427 83.735  1.00 61.83  ?  160  LEU   C CD1   1 
ATOM   13285 C  CD2   . LEU   C 2 161 ? 98.313  117.906 86.097  1.00 67.14  ?  160  LEU   C CD2   1 
ATOM   13286 N  N     . ILE   C 2 162 ? 102.196 118.062 82.914  1.00 66.68  ?  161  ILE   C N     1 
ATOM   13287 C  CA    . ILE   C 2 162 ? 103.097 119.192 82.700  1.00 66.77  ?  161  ILE   C CA    1 
ATOM   13288 C  C     . ILE   C 2 162 ? 103.360 119.395 81.214  1.00 70.61  ?  161  ILE   C C     1 
ATOM   13289 O  O     . ILE   C 2 162 ? 103.377 120.531 80.722  1.00 79.06  ?  161  ILE   C O     1 
ATOM   13290 C  CB    . ILE   C 2 162 ? 104.406 118.988 83.485  1.00 62.60  ?  161  ILE   C CB    1 
ATOM   13291 C  CG1   . ILE   C 2 162 ? 104.153 119.085 84.989  1.00 62.73  ?  161  ILE   C CG1   1 
ATOM   13292 C  CG2   . ILE   C 2 162 ? 105.455 120.002 83.055  1.00 62.58  ?  161  ILE   C CG2   1 
ATOM   13293 C  CD1   . ILE   C 2 162 ? 105.184 118.363 85.827  1.00 66.72  ?  161  ILE   C CD1   1 
ATOM   13294 N  N     . GLU   C 2 163 ? 103.555 118.298 80.476  1.00 77.60  ?  162  GLU   C N     1 
ATOM   13295 C  CA    . GLU   C 2 163 ? 103.813 118.378 79.044  1.00 77.97  ?  162  GLU   C CA    1 
ATOM   13296 C  C     . GLU   C 2 163 ? 102.682 119.089 78.318  1.00 78.79  ?  162  GLU   C C     1 
ATOM   13297 O  O     . GLU   C 2 163 ? 102.903 120.082 77.608  1.00 80.45  ?  162  GLU   C O     1 
ATOM   13298 C  CB    . GLU   C 2 163 ? 104.001 116.972 78.477  1.00 81.53  ?  162  GLU   C CB    1 
ATOM   13299 C  CG    . GLU   C 2 163 ? 104.163 116.937 76.969  1.00 83.07  ?  162  GLU   C CG    1 
ATOM   13300 C  CD    . GLU   C 2 163 ? 105.599 117.009 76.523  1.00 94.15  ?  162  GLU   C CD    1 
ATOM   13301 O  OE1   . GLU   C 2 163 ? 106.378 117.741 77.162  1.00 97.39  ?  162  GLU   C OE1   1 
ATOM   13302 O  OE2   . GLU   C 2 163 ? 105.948 116.334 75.533  1.00 92.00  ?  162  GLU   C OE2   1 
ATOM   13303 N  N     . MET   C 2 164 ? 101.452 118.612 78.492  1.00 76.42  ?  163  MET   C N     1 
ATOM   13304 C  CA    . MET   C 2 164 ? 100.411 119.260 77.706  1.00 76.34  ?  163  MET   C CA    1 
ATOM   13305 C  C     . MET   C 2 164 ? 99.945  120.578 78.314  1.00 78.18  ?  163  MET   C C     1 
ATOM   13306 O  O     . MET   C 2 164 ? 99.367  121.394 77.593  1.00 85.42  ?  163  MET   C O     1 
ATOM   13307 C  CB    . MET   C 2 164 ? 99.238  118.313 77.456  1.00 78.13  ?  163  MET   C CB    1 
ATOM   13308 C  CG    . MET   C 2 164 ? 98.211  118.204 78.539  1.00 85.26  ?  163  MET   C CG    1 
ATOM   13309 S  SD    . MET   C 2 164 ? 96.922  117.050 78.044  1.00 102.59 ?  163  MET   C SD    1 
ATOM   13310 C  CE    . MET   C 2 164 ? 97.107  117.024 76.265  1.00 81.55  ?  163  MET   C CE    1 
ATOM   13311 N  N     . THR   C 2 165 ? 100.233 120.843 79.593  1.00 68.55  ?  164  THR   C N     1 
ATOM   13312 C  CA    . THR   C 2 165 ? 100.034 122.189 80.119  1.00 66.57  ?  164  THR   C CA    1 
ATOM   13313 C  C     . THR   C 2 165 ? 100.973 123.178 79.444  1.00 69.10  ?  164  THR   C C     1 
ATOM   13314 O  O     . THR   C 2 165 ? 100.564 124.288 79.084  1.00 77.05  ?  164  THR   C O     1 
ATOM   13315 C  CB    . THR   C 2 165 ? 100.244 122.205 81.633  1.00 71.76  ?  164  THR   C CB    1 
ATOM   13316 O  OG1   . THR   C 2 165 ? 99.309  121.318 82.257  1.00 82.71  ?  164  THR   C OG1   1 
ATOM   13317 C  CG2   . THR   C 2 165 ? 100.055 123.609 82.186  1.00 70.87  ?  164  THR   C CG2   1 
ATOM   13318 N  N     . SER   C 2 166 ? 102.238 122.793 79.263  1.00 73.79  ?  165  SER   C N     1 
ATOM   13319 C  CA    . SER   C 2 166 ? 103.168 123.652 78.539  1.00 75.28  ?  165  SER   C CA    1 
ATOM   13320 C  C     . SER   C 2 166 ? 102.719 123.843 77.098  1.00 77.06  ?  165  SER   C C     1 
ATOM   13321 O  O     . SER   C 2 166 ? 102.767 124.959 76.564  1.00 84.20  ?  165  SER   C O     1 
ATOM   13322 C  CB    . SER   C 2 166 ? 104.575 123.063 78.586  1.00 76.18  ?  165  SER   C CB    1 
ATOM   13323 O  OG    . SER   C 2 166 ? 105.112 123.101 79.893  1.00 84.02  ?  165  SER   C OG    1 
ATOM   13324 N  N     . TYR   C 2 167 ? 102.251 122.766 76.462  1.00 80.94  ?  166  TYR   C N     1 
ATOM   13325 C  CA    . TYR   C 2 167 ? 101.740 122.879 75.097  1.00 79.25  ?  166  TYR   C CA    1 
ATOM   13326 C  C     . TYR   C 2 167 ? 100.565 123.849 75.022  1.00 78.22  ?  166  TYR   C C     1 
ATOM   13327 O  O     . TYR   C 2 167 ? 100.495 124.681 74.109  1.00 77.58  ?  166  TYR   C O     1 
ATOM   13328 C  CB    . TYR   C 2 167 ? 101.326 121.505 74.572  1.00 79.81  ?  166  TYR   C CB    1 
ATOM   13329 C  CG    . TYR   C 2 167 ? 102.382 120.826 73.735  1.00 79.22  ?  166  TYR   C CG    1 
ATOM   13330 C  CD1   . TYR   C 2 167 ? 102.821 121.388 72.548  1.00 80.37  ?  166  TYR   C CD1   1 
ATOM   13331 C  CD2   . TYR   C 2 167 ? 102.936 119.618 74.131  1.00 81.56  ?  166  TYR   C CD2   1 
ATOM   13332 C  CE1   . TYR   C 2 167 ? 103.789 120.769 71.781  1.00 83.75  ?  166  TYR   C CE1   1 
ATOM   13333 C  CE2   . TYR   C 2 167 ? 103.903 118.992 73.371  1.00 80.30  ?  166  TYR   C CE2   1 
ATOM   13334 C  CZ    . TYR   C 2 167 ? 104.326 119.572 72.197  1.00 81.37  ?  166  TYR   C CZ    1 
ATOM   13335 O  OH    . TYR   C 2 167 ? 105.289 118.951 71.436  1.00 82.21  ?  166  TYR   C OH    1 
ATOM   13336 N  N     . TRP   C 2 168 ? 99.633  123.757 75.974  1.00 77.22  ?  167  TRP   C N     1 
ATOM   13337 C  CA    . TRP   C 2 168 ? 98.471  124.639 75.977  1.00 72.81  ?  167  TRP   C CA    1 
ATOM   13338 C  C     . TRP   C 2 168 ? 98.867  126.091 76.215  1.00 73.36  ?  167  TRP   C C     1 
ATOM   13339 O  O     . TRP   C 2 168 ? 98.378  126.993 75.527  1.00 76.33  ?  167  TRP   C O     1 
ATOM   13340 C  CB    . TRP   C 2 168 ? 97.477  124.174 77.038  1.00 72.02  ?  167  TRP   C CB    1 
ATOM   13341 C  CG    . TRP   C 2 168 ? 96.264  125.034 77.158  1.00 75.78  ?  167  TRP   C CG    1 
ATOM   13342 C  CD1   . TRP   C 2 168 ? 95.361  125.322 76.178  1.00 77.30  ?  167  TRP   C CD1   1 
ATOM   13343 C  CD2   . TRP   C 2 168 ? 95.809  125.713 78.333  1.00 76.44  ?  167  TRP   C CD2   1 
ATOM   13344 N  NE1   . TRP   C 2 168 ? 94.390  126.160 76.665  1.00 77.65  ?  167  TRP   C NE1   1 
ATOM   13345 C  CE2   . TRP   C 2 168 ? 94.609  126.365 78.000  1.00 75.29  ?  167  TRP   C CE2   1 
ATOM   13346 C  CE3   . TRP   C 2 168 ? 96.297  125.825 79.639  1.00 76.07  ?  167  TRP   C CE3   1 
ATOM   13347 C  CZ2   . TRP   C 2 168 ? 93.919  127.163 78.906  1.00 76.97  ?  167  TRP   C CZ2   1 
ATOM   13348 C  CZ3   . TRP   C 2 168 ? 95.583  126.578 80.551  1.00 75.62  ?  167  TRP   C CZ3   1 
ATOM   13349 C  CH2   . TRP   C 2 168 ? 94.412  127.243 80.179  1.00 76.83  ?  167  TRP   C CH2   1 
ATOM   13350 N  N     . HIS   C 2 169 ? 99.749  126.338 77.186  1.00 84.11  ?  168  HIS   C N     1 
ATOM   13351 C  CA    . HIS   C 2 169 ? 100.170 127.703 77.475  1.00 80.77  ?  168  HIS   C CA    1 
ATOM   13352 C  C     . HIS   C 2 169 ? 101.013 128.295 76.358  1.00 81.68  ?  168  HIS   C C     1 
ATOM   13353 O  O     . HIS   C 2 169 ? 101.096 129.522 76.245  1.00 86.35  ?  168  HIS   C O     1 
ATOM   13354 C  CB    . HIS   C 2 169 ? 100.955 127.749 78.786  1.00 78.07  ?  168  HIS   C CB    1 
ATOM   13355 C  CG    . HIS   C 2 169 ? 100.092 127.811 80.007  1.00 82.82  ?  168  HIS   C CG    1 
ATOM   13356 N  ND1   . HIS   C 2 169 ? 98.936  128.559 80.063  1.00 84.48  ?  168  HIS   C ND1   1 
ATOM   13357 C  CD2   . HIS   C 2 169 ? 100.217 127.220 81.218  1.00 84.78  ?  168  HIS   C CD2   1 
ATOM   13358 C  CE1   . HIS   C 2 169 ? 98.384  128.422 81.255  1.00 87.22  ?  168  HIS   C CE1   1 
ATOM   13359 N  NE2   . HIS   C 2 169 ? 99.142  127.616 81.975  1.00 88.62  ?  168  HIS   C NE2   1 
ATOM   13360 N  N     . LEU   C 2 170 ? 101.635 127.458 75.533  1.00 81.16  ?  169  LEU   C N     1 
ATOM   13361 C  CA    . LEU   C 2 170 ? 102.560 127.951 74.526  1.00 81.32  ?  169  LEU   C CA    1 
ATOM   13362 C  C     . LEU   C 2 170 ? 101.965 128.055 73.132  1.00 82.60  ?  169  LEU   C C     1 
ATOM   13363 O  O     . LEU   C 2 170 ? 102.395 128.912 72.355  1.00 83.06  ?  169  LEU   C O     1 
ATOM   13364 C  CB    . LEU   C 2 170 ? 103.795 127.051 74.482  1.00 81.81  ?  169  LEU   C CB    1 
ATOM   13365 C  CG    . LEU   C 2 170 ? 104.989 127.613 75.243  1.00 83.64  ?  169  LEU   C CG    1 
ATOM   13366 C  CD1   . LEU   C 2 170 ? 106.256 127.016 74.724  1.00 82.01  ?  169  LEU   C CD1   1 
ATOM   13367 C  CD2   . LEU   C 2 170 ? 105.008 129.121 75.115  1.00 84.80  ?  169  LEU   C CD2   1 
ATOM   13368 N  N     . LEU   C 2 171 ? 100.986 127.223 72.802  1.00 86.14  ?  170  LEU   C N     1 
ATOM   13369 C  CA    . LEU   C 2 171 ? 100.409 127.191 71.470  1.00 82.13  ?  170  LEU   C CA    1 
ATOM   13370 C  C     . LEU   C 2 171 ? 98.936  127.558 71.434  1.00 84.22  ?  170  LEU   C C     1 
ATOM   13371 O  O     . LEU   C 2 171 ? 98.494  128.191 70.472  1.00 90.00  ?  170  LEU   C O     1 
ATOM   13372 C  CB    . LEU   C 2 171 ? 100.592 125.793 70.864  1.00 83.05  ?  170  LEU   C CB    1 
ATOM   13373 C  CG    . LEU   C 2 171 ? 102.040 125.348 70.668  1.00 83.73  ?  170  LEU   C CG    1 
ATOM   13374 C  CD1   . LEU   C 2 171 ? 102.102 124.047 69.882  1.00 80.14  ?  170  LEU   C CD1   1 
ATOM   13375 C  CD2   . LEU   C 2 171 ? 102.845 126.437 69.980  1.00 84.84  ?  170  LEU   C CD2   1 
ATOM   13376 N  N     . GLY   C 2 172 ? 98.173  127.194 72.455  1.00 87.87  ?  171  GLY   C N     1 
ATOM   13377 C  CA    . GLY   C 2 172 ? 96.747  127.413 72.465  1.00 88.80  ?  171  GLY   C CA    1 
ATOM   13378 C  C     . GLY   C 2 172 ? 95.984  126.242 71.879  1.00 93.01  ?  171  GLY   C C     1 
ATOM   13379 O  O     . GLY   C 2 172 ? 96.542  125.295 71.323  1.00 96.61  ?  171  GLY   C O     1 
ATOM   13380 N  N     . GLU   C 2 173 ? 94.671  126.307 72.053  1.00 106.16 ?  172  GLU   C N     1 
ATOM   13381 C  CA    . GLU   C 2 173 ? 93.805  125.211 71.571  1.00 104.92 ?  172  GLU   C CA    1 
ATOM   13382 C  C     . GLU   C 2 173 ? 93.847  125.132 70.051  1.00 107.01 ?  172  GLU   C C     1 
ATOM   13383 O  O     . GLU   C 2 173 ? 93.913  126.189 69.412  1.00 109.82 ?  172  GLU   C O     1 
ATOM   13384 C  CB    . GLU   C 2 173 ? 92.375  125.478 72.034  1.00 104.52 ?  172  GLU   C CB    1 
ATOM   13385 C  CG    . GLU   C 2 173 ? 91.400  124.361 71.722  1.00 109.47 ?  172  GLU   C CG    1 
ATOM   13386 C  CD    . GLU   C 2 173 ? 91.085  123.520 72.944  1.00 112.94 ?  172  GLU   C CD    1 
ATOM   13387 O  OE1   . GLU   C 2 173 ? 91.686  123.792 73.996  1.00 110.82 ?  172  GLU   C OE1   1 
ATOM   13388 O  OE2   . GLU   C 2 173 ? 90.235  122.614 72.845  1.00 112.32 ?  172  GLU   C OE2   1 
ATOM   13389 N  N     . GLY   C 2 174 ? 93.839  123.925 69.510  1.00 103.22 ?  173  GLY   C N     1 
ATOM   13390 C  CA    . GLY   C 2 174 ? 93.758  123.682 68.085  1.00 104.48 ?  173  GLY   C CA    1 
ATOM   13391 C  C     . GLY   C 2 174 ? 94.837  122.732 67.623  1.00 104.47 ?  173  GLY   C C     1 
ATOM   13392 O  O     . GLY   C 2 174 ? 95.538  122.105 68.423  1.00 105.44 ?  173  GLY   C O     1 
ATOM   13393 N  N     . THR   C 2 175 ? 94.981  122.624 66.306  1.00 105.41 ?  174  THR   C N     1 
ATOM   13394 C  CA    . THR   C 2 175 ? 95.972  121.752 65.691  1.00 105.81 ?  174  THR   C CA    1 
ATOM   13395 C  C     . THR   C 2 175 ? 97.127  122.595 65.169  1.00 104.62 ?  174  THR   C C     1 
ATOM   13396 O  O     . THR   C 2 175 ? 96.909  123.575 64.449  1.00 103.99 ?  174  THR   C O     1 
ATOM   13397 C  CB    . THR   C 2 175 ? 95.349  120.938 64.554  1.00 106.70 ?  174  THR   C CB    1 
ATOM   13398 O  OG1   . THR   C 2 175 ? 94.565  119.872 65.102  1.00 108.89 ?  174  THR   C OG1   1 
ATOM   13399 C  CG2   . THR   C 2 175 ? 96.427  120.354 63.655  1.00 105.95 ?  174  THR   C CG2   1 
ATOM   13400 N  N     . HIS   C 2 176 ? 98.349  122.218 65.537  1.00 91.31  ?  175  HIS   C N     1 
ATOM   13401 C  CA    . HIS   C 2 176 ? 99.539  122.961 65.163  1.00 92.26  ?  175  HIS   C CA    1 
ATOM   13402 C  C     . HIS   C 2 176 ? 100.571 122.004 64.585  1.00 95.08  ?  175  HIS   C C     1 
ATOM   13403 O  O     . HIS   C 2 176 ? 100.470 120.783 64.731  1.00 92.70  ?  175  HIS   C O     1 
ATOM   13404 C  CB    . HIS   C 2 176 ? 100.127 123.717 66.364  1.00 92.26  ?  175  HIS   C CB    1 
ATOM   13405 C  CG    . HIS   C 2 176 ? 99.099  124.409 67.203  1.00 92.52  ?  175  HIS   C CG    1 
ATOM   13406 N  ND1   . HIS   C 2 176 ? 98.882  125.769 67.143  1.00 91.46  ?  175  HIS   C ND1   1 
ATOM   13407 C  CD2   . HIS   C 2 176 ? 98.228  123.930 68.122  1.00 91.79  ?  175  HIS   C CD2   1 
ATOM   13408 C  CE1   . HIS   C 2 176 ? 97.922  126.097 67.988  1.00 90.30  ?  175  HIS   C CE1   1 
ATOM   13409 N  NE2   . HIS   C 2 176 ? 97.507  125.000 68.594  1.00 90.58  ?  175  HIS   C NE2   1 
ATOM   13410 N  N     . THR   C 2 177 ? 101.567 122.576 63.913  1.00 111.46 ?  176  THR   C N     1 
ATOM   13411 C  CA    . THR   C 2 177 ? 102.631 121.809 63.277  1.00 110.83 ?  176  THR   C CA    1 
ATOM   13412 C  C     . THR   C 2 177 ? 103.951 122.143 63.957  1.00 110.53 ?  176  THR   C C     1 
ATOM   13413 O  O     . THR   C 2 177 ? 104.408 123.289 63.905  1.00 111.31 ?  176  THR   C O     1 
ATOM   13414 C  CB    . THR   C 2 177 ? 102.702 122.104 61.778  1.00 110.26 ?  176  THR   C CB    1 
ATOM   13415 O  OG1   . THR   C 2 177 ? 101.375 122.180 61.243  1.00 111.30 ?  176  THR   C OG1   1 
ATOM   13416 C  CG2   . THR   C 2 177 ? 103.466 121.006 61.058  1.00 107.53 ?  176  THR   C CG2   1 
ATOM   13417 N  N     . VAL   C 2 178 ? 104.545 121.149 64.610  1.00 104.68 ?  177  VAL   C N     1 
ATOM   13418 C  CA    . VAL   C 2 178 ? 105.820 121.291 65.303  1.00 103.77 ?  177  VAL   C CA    1 
ATOM   13419 C  C     . VAL   C 2 178 ? 106.805 120.336 64.643  1.00 106.64 ?  177  VAL   C C     1 
ATOM   13420 O  O     . VAL   C 2 178 ? 106.633 119.112 64.713  1.00 107.37 ?  177  VAL   C O     1 
ATOM   13421 C  CB    . VAL   C 2 178 ? 105.692 121.003 66.804  1.00 104.83 ?  177  VAL   C CB    1 
ATOM   13422 C  CG1   . VAL   C 2 178 ? 107.060 120.965 67.445  1.00 105.18 ?  177  VAL   C CG1   1 
ATOM   13423 C  CG2   . VAL   C 2 178 ? 104.815 122.049 67.471  1.00 104.00 ?  177  VAL   C CG2   1 
ATOM   13424 N  N     . ASN   C 2 179 ? 107.840 120.893 64.006  1.00 108.45 ?  178  ASN   C N     1 
ATOM   13425 C  CA    . ASN   C 2 179 ? 108.849 120.119 63.276  1.00 107.03 ?  178  ASN   C CA    1 
ATOM   13426 C  C     . ASN   C 2 179 ? 108.212 119.214 62.227  1.00 108.48 ?  178  ASN   C C     1 
ATOM   13427 O  O     . ASN   C 2 179 ? 108.701 118.115 61.960  1.00 110.29 ?  178  ASN   C O     1 
ATOM   13428 C  CB    . ASN   C 2 179 ? 109.733 119.299 64.226  1.00 104.14 ?  178  ASN   C CB    1 
ATOM   13429 C  CG    . ASN   C 2 179 ? 110.380 120.153 65.295  1.00 105.56 ?  178  ASN   C CG    1 
ATOM   13430 O  OD1   . ASN   C 2 179 ? 111.175 121.037 64.990  1.00 106.22 ?  178  ASN   C OD1   1 
ATOM   13431 N  ND2   . ASN   C 2 179 ? 110.030 119.907 66.552  1.00 106.46 ?  178  ASN   C ND2   1 
ATOM   13432 N  N     . GLY   C 2 180 ? 107.106 119.659 61.631  1.00 110.46 ?  179  GLY   C N     1 
ATOM   13433 C  CA    . GLY   C 2 180 ? 106.407 118.865 60.645  1.00 113.37 ?  179  GLY   C CA    1 
ATOM   13434 C  C     . GLY   C 2 180 ? 105.449 117.836 61.203  1.00 113.87 ?  179  GLY   C C     1 
ATOM   13435 O  O     . GLY   C 2 180 ? 104.745 117.182 60.422  1.00 116.49 ?  179  GLY   C O     1 
ATOM   13436 N  N     . LYS   C 2 181 ? 105.390 117.673 62.520  1.00 109.68 ?  180  LYS   C N     1 
ATOM   13437 C  CA    . LYS   C 2 181 ? 104.482 116.734 63.160  1.00 109.20 ?  180  LYS   C CA    1 
ATOM   13438 C  C     . LYS   C 2 181 ? 103.234 117.461 63.641  1.00 109.90 ?  180  LYS   C C     1 
ATOM   13439 O  O     . LYS   C 2 181 ? 103.293 118.615 64.070  1.00 112.58 ?  180  LYS   C O     1 
ATOM   13440 C  CB    . LYS   C 2 181 ? 105.162 116.033 64.337  1.00 108.92 ?  180  LYS   C CB    1 
ATOM   13441 C  CG    . LYS   C 2 181 ? 106.149 114.953 63.933  1.00 110.94 ?  180  LYS   C CG    1 
ATOM   13442 C  CD    . LYS   C 2 181 ? 106.497 114.057 65.112  1.00 111.18 ?  180  LYS   C CD    1 
ATOM   13443 C  CE    . LYS   C 2 181 ? 107.068 112.728 64.646  1.00 110.52 ?  180  LYS   C CE    1 
ATOM   13444 N  NZ    . LYS   C 2 181 ? 107.080 111.718 65.740  1.00 110.27 ?  180  LYS   C NZ    1 
ATOM   13445 N  N     . THR   C 2 182 ? 102.100 116.774 63.571  1.00 104.85 ?  181  THR   C N     1 
ATOM   13446 C  CA    . THR   C 2 182 ? 100.823 117.355 63.966  1.00 105.05 ?  181  THR   C CA    1 
ATOM   13447 C  C     . THR   C 2 182 ? 100.621 117.169 65.465  1.00 106.68 ?  181  THR   C C     1 
ATOM   13448 O  O     . THR   C 2 182 ? 100.596 116.036 65.958  1.00 105.12 ?  181  THR   C O     1 
ATOM   13449 C  CB    . THR   C 2 182 ? 99.674  116.718 63.189  1.00 106.30 ?  181  THR   C CB    1 
ATOM   13450 O  OG1   . THR   C 2 182 ? 99.768  117.081 61.807  1.00 108.64 ?  181  THR   C OG1   1 
ATOM   13451 C  CG2   . THR   C 2 182 ? 98.336  117.188 63.740  1.00 104.51 ?  181  THR   C CG2   1 
ATOM   13452 N  N     . VAL   C 2 183 ? 100.498 118.279 66.188  1.00 103.49 ?  182  VAL   C N     1 
ATOM   13453 C  CA    . VAL   C 2 183 ? 100.258 118.273 67.626  1.00 101.01 ?  182  VAL   C CA    1 
ATOM   13454 C  C     . VAL   C 2 183 ? 98.910  118.935 67.869  1.00 102.01 ?  182  VAL   C C     1 
ATOM   13455 O  O     . VAL   C 2 183 ? 98.696  120.087 67.470  1.00 102.31 ?  182  VAL   C O     1 
ATOM   13456 C  CB    . VAL   C 2 183 ? 101.374 118.998 68.396  1.00 97.21  ?  182  VAL   C CB    1 
ATOM   13457 C  CG1   . VAL   C 2 183 ? 100.961 119.222 69.842  1.00 97.65  ?  182  VAL   C CG1   1 
ATOM   13458 C  CG2   . VAL   C 2 183 ? 102.668 118.207 68.319  1.00 100.13 ?  182  VAL   C CG2   1 
ATOM   13459 N  N     . THR   C 2 184 ? 98.002  118.213 68.517  1.00 102.69 ?  183  THR   C N     1 
ATOM   13460 C  CA    . THR   C 2 184 ? 96.672  118.727 68.817  1.00 102.55 ?  183  THR   C CA    1 
ATOM   13461 C  C     . THR   C 2 184 ? 96.600  119.085 70.297  1.00 104.04 ?  183  THR   C C     1 
ATOM   13462 O  O     . THR   C 2 184 ? 96.859  118.241 71.161  1.00 105.36 ?  183  THR   C O     1 
ATOM   13463 C  CB    . THR   C 2 184 ? 95.591  117.710 68.445  1.00 104.24 ?  183  THR   C CB    1 
ATOM   13464 O  OG1   . THR   C 2 184 ? 94.343  118.095 69.037  1.00 107.68 ?  183  THR   C OG1   1 
ATOM   13465 C  CG2   . THR   C 2 184 ? 95.971  116.307 68.911  1.00 102.32 ?  183  THR   C CG2   1 
ATOM   13466 N  N     . VAL   C 2 185 ? 96.270  120.340 70.583  1.00 89.71  ?  184  VAL   C N     1 
ATOM   13467 C  CA    . VAL   C 2 185 ? 96.122  120.834 71.944  1.00 87.05  ?  184  VAL   C CA    1 
ATOM   13468 C  C     . VAL   C 2 185 ? 94.634  121.032 72.187  1.00 90.53  ?  184  VAL   C C     1 
ATOM   13469 O  O     . VAL   C 2 185 ? 94.019  121.950 71.631  1.00 96.00  ?  184  VAL   C O     1 
ATOM   13470 C  CB    . VAL   C 2 185 ? 96.902  122.136 72.168  1.00 87.50  ?  184  VAL   C CB    1 
ATOM   13471 C  CG1   . VAL   C 2 185 ? 96.571  122.722 73.529  1.00 87.68  ?  184  VAL   C CG1   1 
ATOM   13472 C  CG2   . VAL   C 2 185 ? 98.396  121.888 72.035  1.00 90.10  ?  184  VAL   C CG2   1 
ATOM   13473 N  N     . SER   C 2 186 ? 94.054  120.168 73.012  1.00 88.16  ?  185  SER   C N     1 
ATOM   13474 C  CA    . SER   C 2 186 ? 92.640  120.220 73.346  1.00 89.25  ?  185  SER   C CA    1 
ATOM   13475 C  C     . SER   C 2 186 ? 92.493  120.491 74.833  1.00 93.53  ?  185  SER   C C     1 
ATOM   13476 O  O     . SER   C 2 186 ? 93.137  119.830 75.655  1.00 95.90  ?  185  SER   C O     1 
ATOM   13477 C  CB    . SER   C 2 186 ? 91.936  118.912 72.973  1.00 88.91  ?  185  SER   C CB    1 
ATOM   13478 O  OG    . SER   C 2 186 ? 90.826  118.671 73.820  1.00 92.38  ?  185  SER   C OG    1 
ATOM   13479 N  N     . LEU   C 2 187 ? 91.646  121.461 75.176  1.00 88.38  ?  186  LEU   C N     1 
ATOM   13480 C  CA    . LEU   C 2 187 ? 91.381  121.734 76.581  1.00 85.63  ?  186  LEU   C CA    1 
ATOM   13481 C  C     . LEU   C 2 187 ? 90.623  120.591 77.240  1.00 89.46  ?  186  LEU   C C     1 
ATOM   13482 O  O     . LEU   C 2 187 ? 90.787  120.359 78.442  1.00 97.48  ?  186  LEU   C O     1 
ATOM   13483 C  CB    . LEU   C 2 187 ? 90.621  123.051 76.724  1.00 84.40  ?  186  LEU   C CB    1 
ATOM   13484 C  CG    . LEU   C 2 187 ? 90.005  123.384 78.083  1.00 88.08  ?  186  LEU   C CG    1 
ATOM   13485 C  CD1   . LEU   C 2 187 ? 91.037  124.044 78.980  1.00 85.00  ?  186  LEU   C CD1   1 
ATOM   13486 C  CD2   . LEU   C 2 187 ? 88.787  124.276 77.918  1.00 88.72  ?  186  LEU   C CD2   1 
ATOM   13487 N  N     . ARG   C 2 188 ? 89.819  119.851 76.471  1.00 95.53  ?  187  ARG   C N     1 
ATOM   13488 C  CA    . ARG   C 2 188 ? 89.142  118.677 77.011  1.00 98.35  ?  187  ARG   C CA    1 
ATOM   13489 C  C     . ARG   C 2 188 ? 90.146  117.607 77.429  1.00 99.65  ?  187  ARG   C C     1 
ATOM   13490 O  O     . ARG   C 2 188 ? 90.034  117.021 78.512  1.00 100.02 ?  187  ARG   C O     1 
ATOM   13491 C  CB    . ARG   C 2 188 ? 88.161  118.129 75.976  1.00 95.77  ?  187  ARG   C CB    1 
ATOM   13492 C  CG    . ARG   C 2 188 ? 87.347  116.951 76.459  1.00 96.18  ?  187  ARG   C CG    1 
ATOM   13493 C  CD    . ARG   C 2 188 ? 86.234  116.611 75.485  1.00 97.77  ?  187  ARG   C CD    1 
ATOM   13494 N  NE    . ARG   C 2 188 ? 85.314  115.624 76.036  1.00 100.02 ?  187  ARG   C NE    1 
ATOM   13495 C  CZ    . ARG   C 2 188 ? 84.233  115.912 76.746  1.00 102.99 ?  187  ARG   C CZ    1 
ATOM   13496 N  NH1   . ARG   C 2 188 ? 83.889  117.163 77.006  1.00 101.24 ?  187  ARG   C NH1   1 
ATOM   13497 N  NH2   . ARG   C 2 188 ? 83.481  114.919 77.209  1.00 102.47 ?  187  ARG   C NH2   1 
ATOM   13498 N  N     . GLU   C 2 189 ? 91.141  117.341 76.580  1.00 95.38  ?  188  GLU   C N     1 
ATOM   13499 C  CA    . GLU   C 2 189 ? 92.172  116.369 76.928  1.00 94.26  ?  188  GLU   C CA    1 
ATOM   13500 C  C     . GLU   C 2 189 ? 92.993  116.842 78.121  1.00 94.93  ?  188  GLU   C C     1 
ATOM   13501 O  O     . GLU   C 2 189 ? 93.372  116.041 78.984  1.00 98.40  ?  188  GLU   C O     1 
ATOM   13502 C  CB    . GLU   C 2 189 ? 93.074  116.118 75.721  1.00 94.28  ?  188  GLU   C CB    1 
ATOM   13503 C  CG    . GLU   C 2 189 ? 92.610  115.010 74.791  1.00 98.43  ?  188  GLU   C CG    1 
ATOM   13504 C  CD    . GLU   C 2 189 ? 92.942  113.625 75.299  1.00 104.77 ?  188  GLU   C CD    1 
ATOM   13505 O  OE1   . GLU   C 2 189 ? 92.141  112.699 75.057  1.00 103.98 ?  188  GLU   C OE1   1 
ATOM   13506 O  OE2   . GLU   C 2 189 ? 93.998  113.464 75.945  1.00 106.92 ?  188  GLU   C OE2   1 
ATOM   13507 N  N     . LEU   C 2 190 ? 93.280  118.143 78.184  1.00 73.38  ?  189  LEU   C N     1 
ATOM   13508 C  CA    . LEU   C 2 190 ? 94.023  118.685 79.317  1.00 72.21  ?  189  LEU   C CA    1 
ATOM   13509 C  C     . LEU   C 2 190 ? 93.237  118.539 80.615  1.00 74.78  ?  189  LEU   C C     1 
ATOM   13510 O  O     . LEU   C 2 190 ? 93.806  118.187 81.653  1.00 82.16  ?  189  LEU   C O     1 
ATOM   13511 C  CB    . LEU   C 2 190 ? 94.382  120.144 79.050  1.00 74.33  ?  189  LEU   C CB    1 
ATOM   13512 C  CG    . LEU   C 2 190 ? 95.118  120.915 80.145  1.00 76.29  ?  189  LEU   C CG    1 
ATOM   13513 C  CD1   . LEU   C 2 190 ? 96.437  120.260 80.486  1.00 74.55  ?  189  LEU   C CD1   1 
ATOM   13514 C  CD2   . LEU   C 2 190 ? 95.342  122.352 79.712  1.00 76.04  ?  189  LEU   C CD2   1 
ATOM   13515 N  N     . LYS   C 2 191 ? 91.924  118.781 80.570  1.00 68.64  ?  190  LYS   C N     1 
ATOM   13516 C  CA    . LYS   C 2 191 ? 91.083  118.570 81.744  1.00 68.92  ?  190  LYS   C CA    1 
ATOM   13517 C  C     . LYS   C 2 191 ? 91.054  117.100 82.142  1.00 75.49  ?  190  LYS   C C     1 
ATOM   13518 O  O     . LYS   C 2 191 ? 91.107  116.770 83.334  1.00 80.68  ?  190  LYS   C O     1 
ATOM   13519 C  CB    . LYS   C 2 191 ? 89.670  119.079 81.468  1.00 70.76  ?  190  LYS   C CB    1 
ATOM   13520 C  CG    . LYS   C 2 191 ? 89.546  120.590 81.457  1.00 75.15  ?  190  LYS   C CG    1 
ATOM   13521 C  CD    . LYS   C 2 191 ? 88.168  121.031 81.005  1.00 75.42  ?  190  LYS   C CD    1 
ATOM   13522 C  CE    . LYS   C 2 191 ? 88.034  122.540 81.064  1.00 73.47  ?  190  LYS   C CE    1 
ATOM   13523 N  NZ    . LYS   C 2 191 ? 86.746  123.006 80.486  1.00 79.65  ?  190  LYS   C NZ    1 
ATOM   13524 N  N     . LYS   C 2 192 ? 90.961  116.204 81.157  1.00 76.35  ?  191  LYS   C N     1 
ATOM   13525 C  CA    . LYS   C 2 192 ? 90.980  114.774 81.447  1.00 72.61  ?  191  LYS   C CA    1 
ATOM   13526 C  C     . LYS   C 2 192 ? 92.274  114.377 82.147  1.00 74.18  ?  191  LYS   C C     1 
ATOM   13527 O  O     . LYS   C 2 192 ? 92.260  113.649 83.148  1.00 76.44  ?  191  LYS   C O     1 
ATOM   13528 C  CB    . LYS   C 2 192 ? 90.806  113.985 80.149  1.00 71.85  ?  191  LYS   C CB    1 
ATOM   13529 C  CG    . LYS   C 2 192 ? 90.143  112.631 80.313  1.00 76.14  ?  191  LYS   C CG    1 
ATOM   13530 C  CD    . LYS   C 2 192 ? 89.541  112.164 78.997  1.00 80.18  ?  191  LYS   C CD    1 
ATOM   13531 C  CE    . LYS   C 2 192 ? 89.747  110.675 78.785  1.00 82.26  ?  191  LYS   C CE    1 
ATOM   13532 N  NZ    . LYS   C 2 192 ? 91.192  110.319 78.749  1.00 84.13  ?  191  LYS   C NZ    1 
ATOM   13533 N  N     . LYS   C 2 193 ? 93.405  114.864 81.639  1.00 73.32  ?  192  LYS   C N     1 
ATOM   13534 C  CA    . LYS   C 2 193 ? 94.793  114.530 82.233  1.00 69.88  ?  192  LYS   C CA    1 
ATOM   13535 C  C     . LYS   C 2 193 ? 94.842  115.144 83.620  1.00 77.07  ?  192  LYS   C C     1 
ATOM   13536 O  O     . LYS   C 2 193 ? 95.436  114.533 84.513  1.00 83.07  ?  192  LYS   C O     1 
ATOM   13537 C  CB    . LYS   C 2 193 ? 95.922  114.983 81.310  1.00 66.59  ?  192  LYS   C CB    1 
ATOM   13538 C  CG    . LYS   C 2 193 ? 95.940  114.267 79.974  1.00 73.71  ?  192  LYS   C CG    1 
ATOM   13539 C  CD    . LYS   C 2 193 ? 96.298  112.813 80.096  1.00 79.54  ?  192  LYS   C CD    1 
ATOM   13540 C  CE    . LYS   C 2 193 ? 96.404  112.144 78.745  1.00 82.86  ?  192  LYS   C CE    1 
ATOM   13541 N  NZ    . LYS   C 2 193 ? 95.073  111.979 78.100  1.00 81.04  ?  192  LYS   C NZ    1 
ATOM   13542 N  N     . LEU   C 2 194 ? 94.313  116.353 83.817  1.00 70.80  ?  193  LEU   C N     1 
ATOM   13543 C  CA    . LEU   C 2 194 ? 94.356  116.978 85.134  1.00 64.19  ?  193  LEU   C CA    1 
ATOM   13544 C  C     . LEU   C 2 194 ? 93.553  116.177 86.149  1.00 68.25  ?  193  LEU   C C     1 
ATOM   13545 O  O     . LEU   C 2 194 ? 94.023  115.933 87.267  1.00 77.82  ?  193  LEU   C O     1 
ATOM   13546 C  CB    . LEU   C 2 194 ? 93.852  118.417 85.034  1.00 66.44  ?  193  LEU   C CB    1 
ATOM   13547 C  CG    . LEU   C 2 194 ? 93.817  119.343 86.256  1.00 67.09  ?  193  LEU   C CG    1 
ATOM   13548 C  CD1   . LEU   C 2 194 ? 92.490  119.256 87.004  1.00 64.37  ?  193  LEU   C CD1   1 
ATOM   13549 C  CD2   . LEU   C 2 194 ? 94.982  119.078 87.191  1.00 67.03  ?  193  LEU   C CD2   1 
ATOM   13550 N  N     . TYR   C 2 195 ? 92.358  115.721 85.760  1.00 65.33  ?  194  TYR   C N     1 
ATOM   13551 C  CA    . TYR   C 2 195 ? 91.559  114.874 86.639  1.00 61.15  ?  194  TYR   C CA    1 
ATOM   13552 C  C     . TYR   C 2 195 ? 92.277  113.565 86.942  1.00 69.64  ?  194  TYR   C C     1 
ATOM   13553 O  O     . TYR   C 2 195 ? 92.279  113.100 88.088  1.00 79.51  ?  194  TYR   C O     1 
ATOM   13554 C  CB    . TYR   C 2 195 ? 90.195  114.608 86.005  1.00 61.61  ?  194  TYR   C CB    1 
ATOM   13555 C  CG    . TYR   C 2 195 ? 89.156  114.094 86.974  1.00 67.88  ?  194  TYR   C CG    1 
ATOM   13556 C  CD1   . TYR   C 2 195 ? 88.447  114.963 87.790  1.00 73.18  ?  194  TYR   C CD1   1 
ATOM   13557 C  CD2   . TYR   C 2 195 ? 88.881  112.738 87.070  1.00 69.72  ?  194  TYR   C CD2   1 
ATOM   13558 C  CE1   . TYR   C 2 195 ? 87.495  114.496 88.675  1.00 74.00  ?  194  TYR   C CE1   1 
ATOM   13559 C  CE2   . TYR   C 2 195 ? 87.932  112.262 87.954  1.00 72.63  ?  194  TYR   C CE2   1 
ATOM   13560 C  CZ    . TYR   C 2 195 ? 87.242  113.145 88.754  1.00 76.52  ?  194  TYR   C CZ    1 
ATOM   13561 O  OH    . TYR   C 2 195 ? 86.296  112.675 89.634  1.00 80.83  ?  194  TYR   C OH    1 
ATOM   13562 N  N     . LEU   C 2 196 ? 92.903  112.962 85.928  1.00 69.12  ?  195  LEU   C N     1 
ATOM   13563 C  CA    . LEU   C 2 196 ? 93.623  111.710 86.141  1.00 62.56  ?  195  LEU   C CA    1 
ATOM   13564 C  C     . LEU   C 2 196 ? 94.802  111.897 87.088  1.00 67.46  ?  195  LEU   C C     1 
ATOM   13565 O  O     . LEU   C 2 196 ? 95.027  111.070 87.979  1.00 77.63  ?  195  LEU   C O     1 
ATOM   13566 C  CB    . LEU   C 2 196 ? 94.091  111.146 84.804  1.00 63.84  ?  195  LEU   C CB    1 
ATOM   13567 C  CG    . LEU   C 2 196 ? 93.102  110.254 84.059  1.00 67.44  ?  195  LEU   C CG    1 
ATOM   13568 C  CD1   . LEU   C 2 196 ? 93.685  109.818 82.726  1.00 70.06  ?  195  LEU   C CD1   1 
ATOM   13569 C  CD2   . LEU   C 2 196 ? 92.726  109.053 84.907  1.00 71.04  ?  195  LEU   C CD2   1 
ATOM   13570 N  N     . CYS   C 2 197 ? 95.556  112.985 86.923  1.00 62.33  ?  196  CYS   C N     1 
ATOM   13571 C  CA    . CYS   C 2 197 ? 96.686  113.254 87.805  1.00 62.02  ?  196  CYS   C CA    1 
ATOM   13572 C  C     . CYS   C 2 197 ? 96.224  113.513 89.232  1.00 64.95  ?  196  CYS   C C     1 
ATOM   13573 O  O     . CYS   C 2 197 ? 96.852  113.042 90.188  1.00 67.93  ?  196  CYS   C O     1 
ATOM   13574 C  CB    . CYS   C 2 197 ? 97.492  114.437 87.277  1.00 60.64  ?  196  CYS   C CB    1 
ATOM   13575 S  SG    . CYS   C 2 197 ? 98.919  114.879 88.292  1.00 83.73  ?  196  CYS   C SG    1 
ATOM   13576 N  N     . LEU   C 2 198 ? 95.126  114.252 89.398  1.00 58.01  ?  197  LEU   C N     1 
ATOM   13577 C  CA    . LEU   C 2 198 ? 94.597  114.484 90.736  1.00 56.24  ?  197  LEU   C CA    1 
ATOM   13578 C  C     . LEU   C 2 198 ? 94.143  113.182 91.382  1.00 57.30  ?  197  LEU   C C     1 
ATOM   13579 O  O     . LEU   C 2 198 ? 94.371  112.963 92.576  1.00 65.67  ?  197  LEU   C O     1 
ATOM   13580 C  CB    . LEU   C 2 198 ? 93.454  115.494 90.680  1.00 54.15  ?  197  LEU   C CB    1 
ATOM   13581 C  CG    . LEU   C 2 198 ? 93.856  116.967 90.746  1.00 55.30  ?  197  LEU   C CG    1 
ATOM   13582 C  CD1   . LEU   C 2 198 ? 92.635  117.848 90.947  1.00 61.59  ?  197  LEU   C CD1   1 
ATOM   13583 C  CD2   . LEU   C 2 198 ? 94.874  117.194 91.850  1.00 61.67  ?  197  LEU   C CD2   1 
ATOM   13584 N  N     . MET   C 2 199 ? 93.571  112.268 90.594  1.00 65.80  ?  198  MET   C N     1 
ATOM   13585 C  CA    . MET   C 2 199 ? 93.082  110.951 91.079  1.00 64.08  ?  198  MET   C CA    1 
ATOM   13586 C  C     . MET   C 2 199 ? 94.281  110.077 91.434  1.00 67.89  ?  198  MET   C C     1 
ATOM   13587 O  O     . MET   C 2 199 ? 94.133  109.244 92.324  1.00 72.28  ?  198  MET   C O     1 
ATOM   13588 C  CB    . MET   C 2 199 ? 92.280  110.184 90.024  1.00 62.83  ?  198  MET   C CB    1 
ATOM   13589 C  CG    . MET   C 2 199 ? 90.972  110.827 89.636  1.00 73.66  ?  198  MET   C CG    1 
ATOM   13590 S  SD    . MET   C 2 199 ? 89.843  111.014 91.028  1.00 91.76  ?  198  MET   C SD    1 
ATOM   13591 C  CE    . MET   C 2 199 ? 89.400  109.337 91.484  1.00 79.65  ?  198  MET   C CE    1 
ATOM   13592 N  N     . SER   C 2 200 ? 95.391  110.208 90.717  1.00 64.77  ?  199  SER   C N     1 
ATOM   13593 C  CA    . SER   C 2 200 ? 96.612  109.480 91.046  1.00 59.60  ?  199  SER   C CA    1 
ATOM   13594 C  C     . SER   C 2 200 ? 97.230  109.996 92.339  1.00 65.54  ?  199  SER   C C     1 
ATOM   13595 O  O     . SER   C 2 200 ? 97.685  109.209 93.177  1.00 70.03  ?  199  SER   C O     1 
ATOM   13596 C  CB    . SER   C 2 200 ? 97.609  109.588 89.894  1.00 58.32  ?  199  SER   C CB    1 
ATOM   13597 O  OG    . SER   C 2 200 ? 98.743  108.773 90.123  1.00 69.68  ?  199  SER   C OG    1 
ATOM   13598 N  N     . VAL   C 2 201 ? 97.264  111.318 92.513  1.00 60.21  ?  200  VAL   C N     1 
ATOM   13599 C  CA    . VAL   C 2 201 ? 97.800  111.890 93.746  1.00 61.49  ?  200  VAL   C CA    1 
ATOM   13600 C  C     . VAL   C 2 201 ? 96.930  111.499 94.936  1.00 62.63  ?  200  VAL   C C     1 
ATOM   13601 O  O     . VAL   C 2 201 ? 97.439  111.223 96.032  1.00 66.58  ?  200  VAL   C O     1 
ATOM   13602 C  CB    . VAL   C 2 201 ? 97.932  113.417 93.612  1.00 59.85  ?  200  VAL   C CB    1 
ATOM   13603 C  CG1   . VAL   C 2 201 ? 98.399  114.033 94.921  1.00 49.40  ?  200  VAL   C CG1   1 
ATOM   13604 C  CG2   . VAL   C 2 201 ? 98.887  113.757 92.491  1.00 59.64  ?  200  VAL   C CG2   1 
ATOM   13605 N  N     . ASN   C 2 202 ? 95.607  111.478 94.745  1.00 61.01  ?  201  ASN   C N     1 
ATOM   13606 C  CA    . ASN   C 2 202 ? 94.708  111.026 95.803  1.00 52.78  ?  201  ASN   C CA    1 
ATOM   13607 C  C     . ASN   C 2 202 ? 95.027  109.599 96.205  1.00 56.45  ?  201  ASN   C C     1 
ATOM   13608 O  O     . ASN   C 2 202 ? 95.137  109.282 97.394  1.00 64.61  ?  201  ASN   C O     1 
ATOM   13609 C  CB    . ASN   C 2 202 ? 93.252  111.116 95.348  1.00 55.92  ?  201  ASN   C CB    1 
ATOM   13610 C  CG    . ASN   C 2 202 ? 92.278  110.957 96.499  1.00 64.38  ?  201  ASN   C CG    1 
ATOM   13611 O  OD1   . ASN   C 2 202 ? 92.235  111.784 97.410  1.00 70.18  ?  201  ASN   C OD1   1 
ATOM   13612 N  ND2   . ASN   C 2 202 ? 91.498  109.884 96.469  1.00 68.94  ?  201  ASN   C ND2   1 
ATOM   13613 N  N     . ALA   C 2 203 ? 95.178  108.724 95.211  1.00 61.04  ?  202  ALA   C N     1 
ATOM   13614 C  CA    . ALA   C 2 203 ? 95.478  107.325 95.478  1.00 59.48  ?  202  ALA   C CA    1 
ATOM   13615 C  C     . ALA   C 2 203 ? 96.783  107.199 96.246  1.00 65.48  ?  202  ALA   C C     1 
ATOM   13616 O  O     . ALA   C 2 203 ? 96.849  106.512 97.271  1.00 75.48  ?  202  ALA   C O     1 
ATOM   13617 C  CB    . ALA   C 2 203 ? 95.540  106.547 94.163  1.00 56.51  ?  202  ALA   C CB    1 
ATOM   13618 N  N     . LEU   C 2 204 ? 97.815  107.917 95.795  1.00 62.63  ?  203  LEU   C N     1 
ATOM   13619 C  CA    . LEU   C 2 204 ? 99.109  107.893 96.469  1.00 61.69  ?  203  LEU   C CA    1 
ATOM   13620 C  C     . LEU   C 2 204 ? 98.962  108.285 97.930  1.00 64.96  ?  203  LEU   C C     1 
ATOM   13621 O  O     . LEU   C 2 204 ? 99.078  107.437 98.823  1.00 75.28  ?  203  LEU   C O     1 
ATOM   13622 C  CB    . LEU   C 2 204 ? 100.092 108.820 95.751  1.00 59.48  ?  203  LEU   C CB    1 
ATOM   13623 C  CG    . LEU   C 2 204 ? 101.297 109.325 96.557  1.00 61.56  ?  203  LEU   C CG    1 
ATOM   13624 C  CD1   . LEU   C 2 204 ? 102.278 108.201 96.864  1.00 66.77  ?  203  LEU   C CD1   1 
ATOM   13625 C  CD2   . LEU   C 2 204 ? 102.003 110.467 95.840  1.00 61.01  ?  203  LEU   C CD2   1 
ATOM   13626 N  N     . GLU   C 2 205 ? 98.561  109.536 98.176  1.00 63.09  ?  204  GLU   C N     1 
ATOM   13627 C  CA    . GLU   C 2 205 ? 98.528  110.095 99.521  1.00 59.17  ?  204  GLU   C CA    1 
ATOM   13628 C  C     . GLU   C 2 205 ? 97.493  109.437 100.421 1.00 63.77  ?  204  GLU   C C     1 
ATOM   13629 O  O     . GLU   C 2 205 ? 97.578  109.582 101.644 1.00 75.14  ?  204  GLU   C O     1 
ATOM   13630 C  CB    . GLU   C 2 205 ? 98.243  111.592 99.444  1.00 55.44  ?  204  GLU   C CB    1 
ATOM   13631 C  CG    . GLU   C 2 205 ? 99.201  112.378 98.578  1.00 68.45  ?  204  GLU   C CG    1 
ATOM   13632 C  CD    . GLU   C 2 205 ? 99.366  113.800 99.034  1.00 70.48  ?  204  GLU   C CD    1 
ATOM   13633 O  OE1   . GLU   C 2 205 ? 98.366  114.539 99.013  1.00 76.65  ?  204  GLU   C OE1   1 
ATOM   13634 O  OE2   . GLU   C 2 205 ? 100.497 114.175 99.403  1.00 61.58  ?  204  GLU   C OE2   1 
ATOM   13635 N  N     . ALA   C 2 206 ? 96.526  108.719 99.858  1.00 53.47  ?  205  ALA   C N     1 
ATOM   13636 C  CA    . ALA   C 2 206 ? 95.434  108.170 100.642 1.00 49.65  ?  205  ALA   C CA    1 
ATOM   13637 C  C     . ALA   C 2 206 ? 95.574  106.680 100.881 1.00 60.76  ?  205  ALA   C C     1 
ATOM   13638 O  O     . ALA   C 2 206 ? 94.918  106.156 101.787 1.00 69.61  ?  205  ALA   C O     1 
ATOM   13639 C  CB    . ALA   C 2 206 ? 94.089  108.454 99.954  1.00 50.83  ?  205  ALA   C CB    1 
ATOM   13640 N  N     . ILE   C 2 207 ? 96.417  105.987 100.109 1.00 56.37  ?  206  ILE   C N     1 
ATOM   13641 C  CA    . ILE   C 2 207 ? 96.560  104.545 100.266 1.00 52.21  ?  206  ILE   C CA    1 
ATOM   13642 C  C     . ILE   C 2 207 ? 98.013  104.132 100.478 1.00 60.72  ?  206  ILE   C C     1 
ATOM   13643 O  O     . ILE   C 2 207 ? 98.316  103.422 101.443 1.00 75.87  ?  206  ILE   C O     1 
ATOM   13644 C  CB    . ILE   C 2 207 ? 95.948  103.799 99.070  1.00 50.05  ?  206  ILE   C CB    1 
ATOM   13645 C  CG1   . ILE   C 2 207 ? 94.509  104.234 98.838  1.00 53.98  ?  206  ILE   C CG1   1 
ATOM   13646 C  CG2   . ILE   C 2 207 ? 95.885  102.345 99.356  1.00 56.26  ?  206  ILE   C CG2   1 
ATOM   13647 C  CD1   . ILE   C 2 207 ? 94.040  103.953 97.451  1.00 54.72  ?  206  ILE   C CD1   1 
ATOM   13648 N  N     . ARG   C 2 208 ? 98.927  104.570 99.603  1.00 52.78  ?  207  ARG   C N     1 
ATOM   13649 C  CA    . ARG   C 2 208 ? 100.296 104.061 99.682  1.00 56.10  ?  207  ARG   C CA    1 
ATOM   13650 C  C     . ARG   C 2 208 ? 101.002 104.582 100.928 1.00 62.28  ?  207  ARG   C C     1 
ATOM   13651 O  O     . ARG   C 2 208 ? 101.634 103.815 101.673 1.00 69.64  ?  207  ARG   C O     1 
ATOM   13652 C  CB    . ARG   C 2 208 ? 101.078 104.443 98.424  1.00 56.42  ?  207  ARG   C CB    1 
ATOM   13653 C  CG    . ARG   C 2 208 ? 100.308 104.316 97.119  1.00 57.27  ?  207  ARG   C CG    1 
ATOM   13654 C  CD    . ARG   C 2 208 ? 101.096 104.923 95.972  1.00 64.18  ?  207  ARG   C CD    1 
ATOM   13655 N  NE    . ARG   C 2 208 ? 100.630 104.486 94.661  1.00 68.86  ?  207  ARG   C NE    1 
ATOM   13656 C  CZ    . ARG   C 2 208 ? 101.029 103.378 94.053  1.00 68.73  ?  207  ARG   C CZ    1 
ATOM   13657 N  NH1   . ARG   C 2 208 ? 101.903 102.558 94.612  1.00 69.98  ?  207  ARG   C NH1   1 
ATOM   13658 N  NH2   . ARG   C 2 208 ? 100.539 103.086 92.851  1.00 64.33  ?  207  ARG   C NH2   1 
ATOM   13659 N  N     . PHE   C 2 209 ? 100.898 105.889 101.171 1.00 57.39  ?  208  PHE   C N     1 
ATOM   13660 C  CA    . PHE   C 2 209 ? 101.514 106.466 102.355 1.00 59.33  ?  208  PHE   C CA    1 
ATOM   13661 C  C     . PHE   C 2 209 ? 100.893 105.915 103.627 1.00 59.43  ?  208  PHE   C C     1 
ATOM   13662 O  O     . PHE   C 2 209 ? 101.584 105.773 104.635 1.00 68.79  ?  208  PHE   C O     1 
ATOM   13663 C  CB    . PHE   C 2 209 ? 101.410 107.989 102.313 1.00 51.88  ?  208  PHE   C CB    1 
ATOM   13664 C  CG    . PHE   C 2 209 ? 102.634 108.657 101.763 1.00 57.30  ?  208  PHE   C CG    1 
ATOM   13665 C  CD1   . PHE   C 2 209 ? 103.679 109.011 102.596 1.00 58.51  ?  208  PHE   C CD1   1 
ATOM   13666 C  CD2   . PHE   C 2 209 ? 102.745 108.922 100.410 1.00 63.40  ?  208  PHE   C CD2   1 
ATOM   13667 C  CE1   . PHE   C 2 209 ? 104.808 109.623 102.090 1.00 62.14  ?  208  PHE   C CE1   1 
ATOM   13668 C  CE2   . PHE   C 2 209 ? 103.872 109.530 99.899  1.00 62.46  ?  208  PHE   C CE2   1 
ATOM   13669 C  CZ    . PHE   C 2 209 ? 104.905 109.880 100.740 1.00 64.67  ?  208  PHE   C CZ    1 
ATOM   13670 N  N     . TYR   C 2 210 ? 99.607  105.561 103.595 1.00 57.57  ?  209  TYR   C N     1 
ATOM   13671 C  CA    . TYR   C 2 210 ? 98.982  104.988 104.782 1.00 57.82  ?  209  TYR   C CA    1 
ATOM   13672 C  C     . TYR   C 2 210 ? 99.404  103.542 105.014 1.00 59.73  ?  209  TYR   C C     1 
ATOM   13673 O  O     . TYR   C 2 210 ? 99.510  103.111 106.167 1.00 68.82  ?  209  TYR   C O     1 
ATOM   13674 C  CB    . TYR   C 2 210 ? 97.462  105.100 104.682 1.00 51.80  ?  209  TYR   C CB    1 
ATOM   13675 C  CG    . TYR   C 2 210 ? 96.956  106.411 105.228 1.00 61.21  ?  209  TYR   C CG    1 
ATOM   13676 C  CD1   . TYR   C 2 210 ? 97.016  107.568 104.468 1.00 61.80  ?  209  TYR   C CD1   1 
ATOM   13677 C  CD2   . TYR   C 2 210 ? 96.449  106.499 106.514 1.00 62.51  ?  209  TYR   C CD2   1 
ATOM   13678 C  CE1   . TYR   C 2 210 ? 96.570  108.772 104.967 1.00 61.06  ?  209  TYR   C CE1   1 
ATOM   13679 C  CE2   . TYR   C 2 210 ? 96.000  107.699 107.022 1.00 62.13  ?  209  TYR   C CE2   1 
ATOM   13680 C  CZ    . TYR   C 2 210 ? 96.061  108.833 106.244 1.00 64.91  ?  209  TYR   C CZ    1 
ATOM   13681 O  OH    . TYR   C 2 210 ? 95.614  110.033 106.744 1.00 74.42  ?  209  TYR   C OH    1 
ATOM   13682 N  N     . VAL   C 2 211 ? 99.662  102.786 103.947 1.00 51.07  ?  210  VAL   C N     1 
ATOM   13683 C  CA    . VAL   C 2 211 ? 100.249 101.458 104.114 1.00 50.28  ?  210  VAL   C CA    1 
ATOM   13684 C  C     . VAL   C 2 211 ? 101.628 101.572 104.754 1.00 58.84  ?  210  VAL   C C     1 
ATOM   13685 O  O     . VAL   C 2 211 ? 101.969 100.826 105.686 1.00 65.79  ?  210  VAL   C O     1 
ATOM   13686 C  CB    . VAL   C 2 211 ? 100.307 100.728 102.760 1.00 46.58  ?  210  VAL   C CB    1 
ATOM   13687 C  CG1   . VAL   C 2 211 ? 101.122 99.450  102.872 1.00 50.17  ?  210  VAL   C CG1   1 
ATOM   13688 C  CG2   . VAL   C 2 211 ? 98.906  100.429 102.268 1.00 49.98  ?  210  VAL   C CG2   1 
ATOM   13689 N  N     . SER   C 2 212 ? 102.437 102.520 104.276 1.00 54.68  ?  211  SER   C N     1 
ATOM   13690 C  CA    . SER   C 2 212 ? 103.743 102.745 104.893 1.00 54.24  ?  211  SER   C CA    1 
ATOM   13691 C  C     . SER   C 2 212 ? 103.601 103.197 106.346 1.00 59.08  ?  211  SER   C C     1 
ATOM   13692 O  O     . SER   C 2 212 ? 104.396 102.805 107.211 1.00 67.51  ?  211  SER   C O     1 
ATOM   13693 C  CB    . SER   C 2 212 ? 104.534 103.768 104.078 1.00 59.22  ?  211  SER   C CB    1 
ATOM   13694 O  OG    . SER   C 2 212 ? 104.994 103.202 102.863 1.00 65.49  ?  211  SER   C OG    1 
ATOM   13695 N  N     . PHE   C 2 213 ? 102.594 104.027 106.628 1.00 52.87  ?  212  PHE   C N     1 
ATOM   13696 C  CA    . PHE   C 2 213 ? 102.337 104.470 107.993 1.00 50.74  ?  212  PHE   C CA    1 
ATOM   13697 C  C     . PHE   C 2 213 ? 102.011 103.293 108.899 1.00 56.48  ?  212  PHE   C C     1 
ATOM   13698 O  O     . PHE   C 2 213 ? 102.485 103.226 110.036 1.00 62.97  ?  212  PHE   C O     1 
ATOM   13699 C  CB    . PHE   C 2 213 ? 101.188 105.477 108.005 1.00 48.67  ?  212  PHE   C CB    1 
ATOM   13700 C  CG    . PHE   C 2 213 ? 101.521 106.798 107.375 1.00 53.68  ?  212  PHE   C CG    1 
ATOM   13701 C  CD1   . PHE   C 2 213 ? 102.836 107.191 107.202 1.00 54.41  ?  212  PHE   C CD1   1 
ATOM   13702 C  CD2   . PHE   C 2 213 ? 100.513 107.672 107.006 1.00 49.12  ?  212  PHE   C CD2   1 
ATOM   13703 C  CE1   . PHE   C 2 213 ? 103.137 108.410 106.640 1.00 55.58  ?  212  PHE   C CE1   1 
ATOM   13704 C  CE2   . PHE   C 2 213 ? 100.810 108.890 106.438 1.00 53.63  ?  212  PHE   C CE2   1 
ATOM   13705 C  CZ    . PHE   C 2 213 ? 102.122 109.263 106.263 1.00 54.72  ?  212  PHE   C CZ    1 
ATOM   13706 N  N     . ALA   C 2 214 ? 101.184 102.365 108.414 1.00 60.36  ?  213  ALA   C N     1 
ATOM   13707 C  CA    . ALA   C 2 214 ? 100.853 101.180 109.197 1.00 64.81  ?  213  ALA   C CA    1 
ATOM   13708 C  C     . ALA   C 2 214 ? 102.093 100.341 109.456 1.00 62.28  ?  213  ALA   C C     1 
ATOM   13709 O  O     . ALA   C 2 214 ? 102.292 99.834  110.570 1.00 66.56  ?  213  ALA   C O     1 
ATOM   13710 C  CB    . ALA   C 2 214 ? 99.787  100.355 108.477 1.00 61.94  ?  213  ALA   C CB    1 
ATOM   13711 N  N     . CYS   C 2 215 ? 102.946 100.194 108.440 1.00 69.12  ?  214  CYS   C N     1 
ATOM   13712 C  CA    . CYS   C 2 215 ? 104.189 99.453  108.630 1.00 68.22  ?  214  CYS   C CA    1 
ATOM   13713 C  C     . CYS   C 2 215 ? 105.061 100.096 109.704 1.00 68.44  ?  214  CYS   C C     1 
ATOM   13714 O  O     . CYS   C 2 215 ? 105.650 99.397  110.536 1.00 70.10  ?  214  CYS   C O     1 
ATOM   13715 C  CB    . CYS   C 2 215 ? 104.952 99.352  107.310 1.00 68.84  ?  214  CYS   C CB    1 
ATOM   13716 S  SG    . CYS   C 2 215 ? 104.187 98.261  106.098 1.00 91.21  ?  214  CYS   C SG    1 
ATOM   13717 N  N     . SER   C 2 216 ? 105.160 101.428 109.702 1.00 70.56  ?  215  SER   C N     1 
ATOM   13718 C  CA    . SER   C 2 216 ? 105.975 102.103 110.711 1.00 63.27  ?  215  SER   C CA    1 
ATOM   13719 C  C     . SER   C 2 216 ? 105.336 102.053 112.097 1.00 64.90  ?  215  SER   C C     1 
ATOM   13720 O  O     . SER   C 2 216 ? 106.049 101.997 113.105 1.00 66.53  ?  215  SER   C O     1 
ATOM   13721 C  CB    . SER   C 2 216 ? 106.231 103.551 110.298 1.00 65.50  ?  215  SER   C CB    1 
ATOM   13722 O  OG    . SER   C 2 216 ? 106.979 103.616 109.096 1.00 78.84  ?  215  SER   C OG    1 
ATOM   13723 N  N     . PHE   C 2 217 ? 104.005 102.082 112.170 1.00 69.86  ?  216  PHE   C N     1 
ATOM   13724 C  CA    . PHE   C 2 217 ? 103.309 102.098 113.452 1.00 56.59  ?  216  PHE   C CA    1 
ATOM   13725 C  C     . PHE   C 2 217 ? 103.299 100.730 114.120 1.00 60.43  ?  216  PHE   C C     1 
ATOM   13726 O  O     . PHE   C 2 217 ? 103.207 100.644 115.352 1.00 67.42  ?  216  PHE   C O     1 
ATOM   13727 C  CB    . PHE   C 2 217 ? 101.879 102.597 113.254 1.00 51.19  ?  216  PHE   C CB    1 
ATOM   13728 C  CG    . PHE   C 2 217 ? 101.786 104.056 112.916 1.00 58.98  ?  216  PHE   C CG    1 
ATOM   13729 C  CD1   . PHE   C 2 217 ? 102.742 104.946 113.366 1.00 61.03  ?  216  PHE   C CD1   1 
ATOM   13730 C  CD2   . PHE   C 2 217 ? 100.703 104.548 112.209 1.00 59.66  ?  216  PHE   C CD2   1 
ATOM   13731 C  CE1   . PHE   C 2 217 ? 102.649 106.287 113.075 1.00 63.13  ?  216  PHE   C CE1   1 
ATOM   13732 C  CE2   . PHE   C 2 217 ? 100.610 105.889 111.906 1.00 55.13  ?  216  PHE   C CE2   1 
ATOM   13733 C  CZ    . PHE   C 2 217 ? 101.576 106.760 112.346 1.00 60.07  ?  216  PHE   C CZ    1 
ATOM   13734 N  N     . ALA   C 2 218 ? 103.387 99.660  113.325 1.00 55.84  ?  217  ALA   C N     1 
ATOM   13735 C  CA    . ALA   C 2 218 ? 103.403 98.319  113.898 1.00 49.80  ?  217  ALA   C CA    1 
ATOM   13736 C  C     . ALA   C 2 218 ? 104.595 98.130  114.823 1.00 58.24  ?  217  ALA   C C     1 
ATOM   13737 O  O     . ALA   C 2 218 ? 104.501 97.405  115.819 1.00 62.49  ?  217  ALA   C O     1 
ATOM   13738 C  CB    . ALA   C 2 218 ? 103.416 97.270  112.786 1.00 54.79  ?  217  ALA   C CB    1 
ATOM   13739 N  N     . PHE   C 2 219 ? 105.720 98.780  114.516 1.00 64.14  ?  218  PHE   C N     1 
ATOM   13740 C  CA    . PHE   C 2 219 ? 106.886 98.703  115.390 1.00 59.65  ?  218  PHE   C CA    1 
ATOM   13741 C  C     . PHE   C 2 219 ? 106.615 99.356  116.739 1.00 63.31  ?  218  PHE   C C     1 
ATOM   13742 O  O     . PHE   C 2 219 ? 106.994 98.814  117.782 1.00 74.44  ?  218  PHE   C O     1 
ATOM   13743 C  CB    . PHE   C 2 219 ? 108.096 99.352  114.717 1.00 61.21  ?  218  PHE   C CB    1 
ATOM   13744 C  CG    . PHE   C 2 219 ? 108.757 98.476  113.695 1.00 59.43  ?  218  PHE   C CG    1 
ATOM   13745 C  CD1   . PHE   C 2 219 ? 109.466 97.354  114.082 1.00 58.36  ?  218  PHE   C CD1   1 
ATOM   13746 C  CD2   . PHE   C 2 219 ? 108.666 98.772  112.349 1.00 57.83  ?  218  PHE   C CD2   1 
ATOM   13747 C  CE1   . PHE   C 2 219 ? 110.070 96.544  113.146 1.00 60.13  ?  218  PHE   C CE1   1 
ATOM   13748 C  CE2   . PHE   C 2 219 ? 109.263 97.962  111.406 1.00 66.45  ?  218  PHE   C CE2   1 
ATOM   13749 C  CZ    . PHE   C 2 219 ? 109.964 96.842  111.806 1.00 66.67  ?  218  PHE   C CZ    1 
ATOM   13750 N  N     . ALA   C 2 220 ? 105.970 100.524 116.740 1.00 57.84  ?  219  ALA   C N     1 
ATOM   13751 C  CA    . ALA   C 2 220 ? 105.600 101.157 118.001 1.00 48.91  ?  219  ALA   C CA    1 
ATOM   13752 C  C     . ALA   C 2 220 ? 104.577 100.340 118.778 1.00 56.67  ?  219  ALA   C C     1 
ATOM   13753 O  O     . ALA   C 2 220 ? 104.577 100.371 120.014 1.00 68.63  ?  219  ALA   C O     1 
ATOM   13754 C  CB    . ALA   C 2 220 ? 105.058 102.554 117.747 1.00 55.23  ?  219  ALA   C CB    1 
ATOM   13755 N  N     . GLU   C 2 221 ? 103.688 99.630  118.083 1.00 69.97  ?  220  GLU   C N     1 
ATOM   13756 C  CA    . GLU   C 2 221 ? 102.759 98.750  118.778 1.00 70.74  ?  220  GLU   C CA    1 
ATOM   13757 C  C     . GLU   C 2 221 ? 103.482 97.667  119.568 1.00 75.32  ?  220  GLU   C C     1 
ATOM   13758 O  O     . GLU   C 2 221 ? 102.911 97.120  120.517 1.00 78.30  ?  220  GLU   C O     1 
ATOM   13759 C  CB    . GLU   C 2 221 ? 101.793 98.115  117.780 1.00 75.06  ?  220  GLU   C CB    1 
ATOM   13760 C  CG    . GLU   C 2 221 ? 100.882 99.111  117.095 1.00 77.56  ?  220  GLU   C CG    1 
ATOM   13761 C  CD    . GLU   C 2 221 ? 99.967  99.824  118.067 1.00 83.28  ?  220  GLU   C CD    1 
ATOM   13762 O  OE1   . GLU   C 2 221 ? 99.331  99.143  118.898 1.00 86.13  ?  220  GLU   C OE1   1 
ATOM   13763 O  OE2   . GLU   C 2 221 ? 99.883  101.068 118.002 1.00 86.72  ?  220  GLU   C OE2   1 
ATOM   13764 N  N     . ARG   C 2 222 ? 104.724 97.351  119.204 1.00 75.51  ?  221  ARG   C N     1 
ATOM   13765 C  CA    . ARG   C 2 222 ? 105.533 96.372  119.915 1.00 71.36  ?  221  ARG   C CA    1 
ATOM   13766 C  C     . ARG   C 2 222 ? 106.549 97.025  120.846 1.00 75.02  ?  221  ARG   C C     1 
ATOM   13767 O  O     . ARG   C 2 222 ? 107.579 96.416  121.153 1.00 82.97  ?  221  ARG   C O     1 
ATOM   13768 C  CB    . ARG   C 2 222 ? 106.237 95.450  118.919 1.00 75.01  ?  221  ARG   C CB    1 
ATOM   13769 C  CG    . ARG   C 2 222 ? 105.353 94.343  118.378 1.00 77.84  ?  221  ARG   C CG    1 
ATOM   13770 C  CD    . ARG   C 2 222 ? 106.151 93.358  117.548 1.00 79.34  ?  221  ARG   C CD    1 
ATOM   13771 N  NE    . ARG   C 2 222 ? 107.256 93.988  116.837 1.00 83.58  ?  221  ARG   C NE    1 
ATOM   13772 C  CZ    . ARG   C 2 222 ? 108.512 93.566  116.889 1.00 79.29  ?  221  ARG   C CZ    1 
ATOM   13773 N  NH1   . ARG   C 2 222 ? 108.861 92.524  117.626 1.00 72.62  ?  221  ARG   C NH1   1 
ATOM   13774 N  NH2   . ARG   C 2 222 ? 109.440 94.204  116.183 1.00 79.55  ?  221  ARG   C NH2   1 
ATOM   13775 N  N     . GLU   C 2 223 ? 106.277 98.251  121.295 1.00 78.78  ?  222  GLU   C N     1 
ATOM   13776 C  CA    . GLU   C 2 223 ? 107.134 98.965  122.244 1.00 79.54  ?  222  GLU   C CA    1 
ATOM   13777 C  C     . GLU   C 2 223 ? 108.543 99.158  121.693 1.00 79.91  ?  222  GLU   C C     1 
ATOM   13778 O  O     . GLU   C 2 223 ? 109.529 99.076  122.424 1.00 87.26  ?  222  GLU   C O     1 
ATOM   13779 C  CB    . GLU   C 2 223 ? 107.171 98.254  123.599 1.00 82.10  ?  222  GLU   C CB    1 
ATOM   13780 C  CG    . GLU   C 2 223 ? 105.847 98.309  124.319 1.00 85.33  ?  222  GLU   C CG    1 
ATOM   13781 C  CD    . GLU   C 2 223 ? 105.359 96.948  124.760 1.00 94.36  ?  222  GLU   C CD    1 
ATOM   13782 O  OE1   . GLU   C 2 223 ? 106.199 96.045  124.959 1.00 92.52  ?  222  GLU   C OE1   1 
ATOM   13783 O  OE2   . GLU   C 2 223 ? 104.130 96.778  124.901 1.00 96.62  ?  222  GLU   C OE2   1 
ATOM   13784 N  N     . LEU   C 2 224 ? 108.643 99.421  120.393 1.00 64.25  ?  223  LEU   C N     1 
ATOM   13785 C  CA    . LEU   C 2 224 ? 109.929 99.620  119.738 1.00 66.09  ?  223  LEU   C CA    1 
ATOM   13786 C  C     . LEU   C 2 224 ? 109.866 100.863 118.867 1.00 71.06  ?  223  LEU   C C     1 
ATOM   13787 O  O     . LEU   C 2 224 ? 108.911 101.040 118.104 1.00 78.29  ?  223  LEU   C O     1 
ATOM   13788 C  CB    . LEU   C 2 224 ? 110.314 98.404  118.890 1.00 65.89  ?  223  LEU   C CB    1 
ATOM   13789 C  CG    . LEU   C 2 224 ? 110.786 97.166  119.649 1.00 68.53  ?  223  LEU   C CG    1 
ATOM   13790 C  CD1   . LEU   C 2 224 ? 110.550 95.918  118.822 1.00 70.87  ?  223  LEU   C CD1   1 
ATOM   13791 C  CD2   . LEU   C 2 224 ? 112.253 97.297  120.019 1.00 69.86  ?  223  LEU   C CD2   1 
ATOM   13792 N  N     . MET   C 2 225 ? 110.884 101.715 118.983 1.00 75.13  ?  224  MET   C N     1 
ATOM   13793 C  CA    . MET   C 2 225 ? 111.045 102.888 118.127 1.00 72.09  ?  224  MET   C CA    1 
ATOM   13794 C  C     . MET   C 2 225 ? 109.827 103.813 118.210 1.00 71.89  ?  224  MET   C C     1 
ATOM   13795 O  O     . MET   C 2 225 ? 109.093 104.017 117.242 1.00 81.51  ?  224  MET   C O     1 
ATOM   13796 C  CB    . MET   C 2 225 ? 111.337 102.465 116.684 1.00 70.73  ?  224  MET   C CB    1 
ATOM   13797 C  CG    . MET   C 2 225 ? 112.798 102.118 116.445 1.00 71.84  ?  224  MET   C CG    1 
ATOM   13798 S  SD    . MET   C 2 225 ? 113.232 102.049 114.703 1.00 90.74  ?  224  MET   C SD    1 
ATOM   13799 C  CE    . MET   C 2 225 ? 112.067 100.818 114.134 1.00 74.11  ?  224  MET   C CE    1 
ATOM   13800 N  N     . GLU   C 2 226 ? 109.624 104.373 119.405 1.00 73.12  ?  225  GLU   C N     1 
ATOM   13801 C  CA    . GLU   C 2 226 ? 108.460 105.216 119.659 1.00 72.74  ?  225  GLU   C CA    1 
ATOM   13802 C  C     . GLU   C 2 226 ? 108.651 106.649 119.169 1.00 76.37  ?  225  GLU   C C     1 
ATOM   13803 O  O     . GLU   C 2 226 ? 107.671 107.313 118.818 1.00 83.67  ?  225  GLU   C O     1 
ATOM   13804 C  CB    . GLU   C 2 226 ? 108.133 105.208 121.154 1.00 76.13  ?  225  GLU   C CB    1 
ATOM   13805 C  CG    . GLU   C 2 226 ? 106.645 105.260 121.480 1.00 83.92  ?  225  GLU   C CG    1 
ATOM   13806 C  CD    . GLU   C 2 226 ? 106.164 106.681 121.701 1.00 88.44  ?  225  GLU   C CD    1 
ATOM   13807 O  OE1   . GLU   C 2 226 ? 107.034 107.560 121.846 1.00 90.60  ?  225  GLU   C OE1   1 
ATOM   13808 O  OE2   . GLU   C 2 226 ? 104.936 106.927 121.725 1.00 81.99  ?  225  GLU   C OE2   1 
ATOM   13809 N  N     . GLY   C 2 227 ? 109.884 107.157 119.167 1.00 63.00  ?  226  GLY   C N     1 
ATOM   13810 C  CA    . GLY   C 2 227 ? 110.118 108.498 118.652 1.00 64.63  ?  226  GLY   C CA    1 
ATOM   13811 C  C     . GLY   C 2 227 ? 109.910 108.604 117.153 1.00 66.94  ?  226  GLY   C C     1 
ATOM   13812 O  O     . GLY   C 2 227 ? 109.304 109.564 116.664 1.00 76.44  ?  226  GLY   C O     1 
ATOM   13813 N  N     . ASN   C 2 228 ? 110.418 107.628 116.398 1.00 51.72  ?  227  ASN   C N     1 
ATOM   13814 C  CA    . ASN   C 2 228 ? 110.095 107.568 114.979 1.00 50.93  ?  227  ASN   C CA    1 
ATOM   13815 C  C     . ASN   C 2 228 ? 108.589 107.444 114.782 1.00 58.65  ?  227  ASN   C C     1 
ATOM   13816 O  O     . ASN   C 2 228 ? 108.030 107.952 113.803 1.00 70.16  ?  227  ASN   C O     1 
ATOM   13817 C  CB    . ASN   C 2 228 ? 110.810 106.380 114.328 1.00 54.44  ?  227  ASN   C CB    1 
ATOM   13818 C  CG    . ASN   C 2 228 ? 112.307 106.411 114.521 1.00 60.89  ?  227  ASN   C CG    1 
ATOM   13819 O  OD1   . ASN   C 2 228 ? 112.893 107.466 114.763 1.00 63.13  ?  227  ASN   C OD1   1 
ATOM   13820 N  ND2   . ASN   C 2 228 ? 112.943 105.246 114.397 1.00 62.51  ?  227  ASN   C ND2   1 
ATOM   13821 N  N     . ALA   C 2 229 ? 107.917 106.738 115.684 1.00 50.21  ?  228  ALA   C N     1 
ATOM   13822 C  CA    . ALA   C 2 229 ? 106.465 106.636 115.594 1.00 44.01  ?  228  ALA   C CA    1 
ATOM   13823 C  C     . ALA   C 2 229 ? 105.800 107.990 115.797 1.00 54.37  ?  228  ALA   C C     1 
ATOM   13824 O  O     . ALA   C 2 229 ? 104.819 108.312 115.121 1.00 65.61  ?  228  ALA   C O     1 
ATOM   13825 C  CB    . ALA   C 2 229 ? 105.943 105.636 116.616 1.00 53.64  ?  228  ALA   C CB    1 
ATOM   13826 N  N     . LYS   C 2 230 ? 106.304 108.786 116.742 1.00 49.28  ?  229  LYS   C N     1 
ATOM   13827 C  CA    . LYS   C 2 230 ? 105.768 110.129 116.942 1.00 52.04  ?  229  LYS   C CA    1 
ATOM   13828 C  C     . LYS   C 2 230 ? 105.974 110.989 115.703 1.00 55.61  ?  229  LYS   C C     1 
ATOM   13829 O  O     . LYS   C 2 230 ? 105.076 111.738 115.296 1.00 65.67  ?  229  LYS   C O     1 
ATOM   13830 C  CB    . LYS   C 2 230 ? 106.417 110.782 118.162 1.00 53.17  ?  229  LYS   C CB    1 
ATOM   13831 C  CG    . LYS   C 2 230 ? 105.919 112.190 118.461 1.00 53.05  ?  229  LYS   C CG    1 
ATOM   13832 C  CD    . LYS   C 2 230 ? 105.077 112.251 119.723 1.00 59.85  ?  229  LYS   C CD    1 
ATOM   13833 C  CE    . LYS   C 2 230 ? 104.250 110.990 119.905 1.00 63.42  ?  229  LYS   C CE    1 
ATOM   13834 N  NZ    . LYS   C 2 230 ? 103.317 111.097 121.058 1.00 70.08  ?  229  LYS   C NZ    1 
ATOM   13835 N  N     . ILE   C 2 231 ? 107.152 110.885 115.084 1.00 39.47  ?  230  ILE   C N     1 
ATOM   13836 C  CA    . ILE   C 2 231 ? 107.413 111.638 113.859 1.00 38.34  ?  230  ILE   C CA    1 
ATOM   13837 C  C     . ILE   C 2 231 ? 106.453 111.213 112.752 1.00 47.12  ?  230  ILE   C C     1 
ATOM   13838 O  O     . ILE   C 2 231 ? 105.883 112.053 112.042 1.00 55.70  ?  230  ILE   C O     1 
ATOM   13839 C  CB    . ILE   C 2 231 ? 108.882 111.470 113.430 1.00 36.92  ?  230  ILE   C CB    1 
ATOM   13840 C  CG1   . ILE   C 2 231 ? 109.816 112.059 114.488 1.00 44.20  ?  230  ILE   C CG1   1 
ATOM   13841 C  CG2   . ILE   C 2 231 ? 109.121 112.128 112.080 1.00 39.92  ?  230  ILE   C CG2   1 
ATOM   13842 C  CD1   . ILE   C 2 231 ? 111.268 112.097 114.071 1.00 52.94  ?  230  ILE   C CD1   1 
ATOM   13843 N  N     . ILE   C 2 232 ? 106.253 109.904 112.591 1.00 42.32  ?  231  ILE   C N     1 
ATOM   13844 C  CA    . ILE   C 2 232 ? 105.369 109.412 111.540 1.00 44.69  ?  231  ILE   C CA    1 
ATOM   13845 C  C     . ILE   C 2 232 ? 103.924 109.800 111.817 1.00 48.84  ?  231  ILE   C C     1 
ATOM   13846 O  O     . ILE   C 2 232 ? 103.160 110.068 110.886 1.00 62.38  ?  231  ILE   C O     1 
ATOM   13847 C  CB    . ILE   C 2 232 ? 105.532 107.890 111.374 1.00 43.37  ?  231  ILE   C CB    1 
ATOM   13848 C  CG1   . ILE   C 2 232 ? 106.963 107.543 110.969 1.00 44.78  ?  231  ILE   C CG1   1 
ATOM   13849 C  CG2   . ILE   C 2 232 ? 104.568 107.349 110.332 1.00 49.59  ?  231  ILE   C CG2   1 
ATOM   13850 C  CD1   . ILE   C 2 232 ? 107.329 107.996 109.582 1.00 56.74  ?  231  ILE   C CD1   1 
ATOM   13851 N  N     . ARG   C 2 233 ? 103.520 109.829 113.088 1.00 43.74  ?  232  ARG   C N     1 
ATOM   13852 C  CA    . ARG   C 2 233 ? 102.177 110.275 113.437 1.00 44.47  ?  232  ARG   C CA    1 
ATOM   13853 C  C     . ARG   C 2 233 ? 101.986 111.750 113.107 1.00 50.24  ?  232  ARG   C C     1 
ATOM   13854 O  O     . ARG   C 2 233 ? 100.931 112.149 112.598 1.00 63.43  ?  232  ARG   C O     1 
ATOM   13855 C  CB    . ARG   C 2 233 ? 101.917 110.002 114.916 1.00 39.01  ?  232  ARG   C CB    1 
ATOM   13856 C  CG    . ARG   C 2 233 ? 100.755 110.771 115.501 1.00 46.57  ?  232  ARG   C CG    1 
ATOM   13857 C  CD    . ARG   C 2 233 ? 100.778 110.715 117.014 1.00 49.27  ?  232  ARG   C CD    1 
ATOM   13858 N  NE    . ARG   C 2 233 ? 99.800  109.776 117.547 1.00 55.33  ?  232  ARG   C NE    1 
ATOM   13859 C  CZ    . ARG   C 2 233 ? 98.500  110.018 117.639 1.00 55.23  ?  232  ARG   C CZ    1 
ATOM   13860 N  NH1   . ARG   C 2 233 ? 97.979  111.163 117.231 1.00 52.64  ?  232  ARG   C NH1   1 
ATOM   13861 N  NH2   . ARG   C 2 233 ? 97.701  109.086 118.150 1.00 60.66  ?  232  ARG   C NH2   1 
ATOM   13862 N  N     . LEU   C 2 234 ? 103.001 112.572 113.382 1.00 50.81  ?  233  LEU   C N     1 
ATOM   13863 C  CA    . LEU   C 2 234 ? 102.934 113.975 112.988 1.00 47.45  ?  233  LEU   C CA    1 
ATOM   13864 C  C     . LEU   C 2 234 ? 102.833 114.114 111.474 1.00 52.10  ?  233  LEU   C C     1 
ATOM   13865 O  O     . LEU   C 2 234 ? 102.129 114.995 110.968 1.00 54.65  ?  233  LEU   C O     1 
ATOM   13866 C  CB    . LEU   C 2 234 ? 104.152 114.730 113.519 1.00 38.01  ?  233  LEU   C CB    1 
ATOM   13867 C  CG    . LEU   C 2 234 ? 104.106 115.108 114.999 1.00 43.02  ?  233  LEU   C CG    1 
ATOM   13868 C  CD1   . LEU   C 2 234 ? 105.431 115.704 115.444 1.00 47.56  ?  233  LEU   C CD1   1 
ATOM   13869 C  CD2   . LEU   C 2 234 ? 102.965 116.074 115.265 1.00 47.56  ?  233  LEU   C CD2   1 
ATOM   13870 N  N     . ILE   C 2 235 ? 103.536 113.253 110.735 1.00 49.28  ?  234  ILE   C N     1 
ATOM   13871 C  CA    . ILE   C 2 235 ? 103.440 113.268 109.277 1.00 41.47  ?  234  ILE   C CA    1 
ATOM   13872 C  C     . ILE   C 2 235 ? 102.034 112.882 108.824 1.00 41.74  ?  234  ILE   C C     1 
ATOM   13873 O  O     . ILE   C 2 235 ? 101.459 113.509 107.926 1.00 59.69  ?  234  ILE   C O     1 
ATOM   13874 C  CB    . ILE   C 2 235 ? 104.508 112.342 108.666 1.00 42.08  ?  234  ILE   C CB    1 
ATOM   13875 C  CG1   . ILE   C 2 235 ? 105.893 112.979 108.783 1.00 40.51  ?  234  ILE   C CG1   1 
ATOM   13876 C  CG2   . ILE   C 2 235 ? 104.186 112.032 107.216 1.00 42.97  ?  234  ILE   C CG2   1 
ATOM   13877 C  CD1   . ILE   C 2 235 ? 107.030 111.997 108.656 1.00 49.67  ?  234  ILE   C CD1   1 
ATOM   13878 N  N     . ALA   C 2 236 ? 101.463 111.840 109.432 1.00 36.90  ?  235  ALA   C N     1 
ATOM   13879 C  CA    . ALA   C 2 236 ? 100.126 111.390 109.058 1.00 43.43  ?  235  ALA   C CA    1 
ATOM   13880 C  C     . ALA   C 2 236 ? 99.072  112.441 109.375 1.00 49.26  ?  235  ALA   C C     1 
ATOM   13881 O  O     . ALA   C 2 236 ? 98.041  112.518 108.692 1.00 64.05  ?  235  ALA   C O     1 
ATOM   13882 C  CB    . ALA   C 2 236 ? 99.799  110.077 109.768 1.00 43.08  ?  235  ALA   C CB    1 
ATOM   13883 N  N     . ARG   C 2 237 ? 99.314  113.258 110.402 1.00 49.12  ?  236  ARG   C N     1 
ATOM   13884 C  CA    . ARG   C 2 237 ? 98.397  114.351 110.708 1.00 46.62  ?  236  ARG   C CA    1 
ATOM   13885 C  C     . ARG   C 2 237 ? 98.256  115.302 109.524 1.00 49.68  ?  236  ARG   C C     1 
ATOM   13886 O  O     . ARG   C 2 237 ? 97.146  115.729 109.191 1.00 60.68  ?  236  ARG   C O     1 
ATOM   13887 C  CB    . ARG   C 2 237 ? 98.876  115.100 111.951 1.00 49.01  ?  236  ARG   C CB    1 
ATOM   13888 C  CG    . ARG   C 2 237 ? 97.854  116.057 112.532 1.00 49.60  ?  236  ARG   C CG    1 
ATOM   13889 C  CD    . ARG   C 2 237 ? 98.301  116.594 113.879 1.00 51.04  ?  236  ARG   C CD    1 
ATOM   13890 N  NE    . ARG   C 2 237 ? 99.503  117.410 113.769 1.00 62.34  ?  236  ARG   C NE    1 
ATOM   13891 C  CZ    . ARG   C 2 237 ? 99.882  118.311 114.665 1.00 58.67  ?  236  ARG   C CZ    1 
ATOM   13892 N  NH1   . ARG   C 2 237 ? 99.171  118.540 115.756 1.00 57.69  ?  236  ARG   C NH1   1 
ATOM   13893 N  NH2   . ARG   C 2 237 ? 101.000 119.000 114.459 1.00 53.75  ?  236  ARG   C NH2   1 
ATOM   13894 N  N     . ASP   C 2 238 ? 99.372  115.647 108.876 1.00 51.60  ?  237  ASP   C N     1 
ATOM   13895 C  CA    . ASP   C 2 238 ? 99.317  116.480 107.678 1.00 48.60  ?  237  ASP   C CA    1 
ATOM   13896 C  C     . ASP   C 2 238 ? 98.845  115.700 106.458 1.00 56.01  ?  237  ASP   C C     1 
ATOM   13897 O  O     . ASP   C 2 238 ? 98.233  116.280 105.551 1.00 71.68  ?  237  ASP   C O     1 
ATOM   13898 C  CB    . ASP   C 2 238 ? 100.689 117.092 107.395 1.00 51.12  ?  237  ASP   C CB    1 
ATOM   13899 C  CG    . ASP   C 2 238 ? 101.343 117.655 108.636 1.00 69.85  ?  237  ASP   C CG    1 
ATOM   13900 O  OD1   . ASP   C 2 238 ? 100.626 117.887 109.630 1.00 78.09  ?  237  ASP   C OD1   1 
ATOM   13901 O  OD2   . ASP   C 2 238 ? 102.573 117.866 108.620 1.00 65.42  ?  237  ASP   C OD2   1 
ATOM   13902 N  N     . GLU   C 2 239 ? 99.139  114.400 106.409 1.00 56.75  ?  238  GLU   C N     1 
ATOM   13903 C  CA    . GLU   C 2 239 ? 98.690  113.582 105.288 1.00 55.59  ?  238  GLU   C CA    1 
ATOM   13904 C  C     . GLU   C 2 239 ? 97.170  113.517 105.224 1.00 62.37  ?  238  GLU   C C     1 
ATOM   13905 O  O     . GLU   C 2 239 ? 96.589  113.461 104.134 1.00 65.92  ?  238  GLU   C O     1 
ATOM   13906 C  CB    . GLU   C 2 239 ? 99.282  112.179 105.388 1.00 52.36  ?  238  GLU   C CB    1 
ATOM   13907 C  CG    . GLU   C 2 239 ? 99.278  111.438 104.070 1.00 60.09  ?  238  GLU   C CG    1 
ATOM   13908 C  CD    . GLU   C 2 239 ? 100.324 111.965 103.111 1.00 70.94  ?  238  GLU   C CD    1 
ATOM   13909 O  OE1   . GLU   C 2 239 ? 101.501 112.092 103.506 1.00 77.28  ?  238  GLU   C OE1   1 
ATOM   13910 O  OE2   . GLU   C 2 239 ? 99.971  112.258 101.956 1.00 74.91  ?  238  GLU   C OE2   1 
ATOM   13911 N  N     . ALA   C 2 240 ? 96.509  113.508 106.385 1.00 53.52  ?  239  ALA   C N     1 
ATOM   13912 C  CA    . ALA   C 2 240 ? 95.050  113.574 106.402 1.00 44.77  ?  239  ALA   C CA    1 
ATOM   13913 C  C     . ALA   C 2 240 ? 94.551  114.843 105.719 1.00 50.35  ?  239  ALA   C C     1 
ATOM   13914 O  O     . ALA   C 2 240 ? 93.619  114.798 104.906 1.00 61.57  ?  239  ALA   C O     1 
ATOM   13915 C  CB    . ALA   C 2 240 ? 94.536  113.494 107.840 1.00 47.97  ?  239  ALA   C CB    1 
ATOM   13916 N  N     . LEU   C 2 241 ? 95.178  115.981 106.017 1.00 44.26  ?  240  LEU   C N     1 
ATOM   13917 C  CA    . LEU   C 2 241 ? 94.794  117.233 105.377 1.00 43.11  ?  240  LEU   C CA    1 
ATOM   13918 C  C     . LEU   C 2 241 ? 95.050  117.196 103.879 1.00 49.69  ?  240  LEU   C C     1 
ATOM   13919 O  O     . LEU   C 2 241 ? 94.227  117.678 103.094 1.00 65.77  ?  240  LEU   C O     1 
ATOM   13920 C  CB    . LEU   C 2 241 ? 95.544  118.399 106.013 1.00 45.69  ?  240  LEU   C CB    1 
ATOM   13921 C  CG    . LEU   C 2 241 ? 95.201  118.792 107.444 1.00 49.82  ?  240  LEU   C CG    1 
ATOM   13922 C  CD1   . LEU   C 2 241 ? 96.006  120.012 107.846 1.00 52.28  ?  240  LEU   C CD1   1 
ATOM   13923 C  CD2   . LEU   C 2 241 ? 93.715  119.052 107.575 1.00 51.51  ?  240  LEU   C CD2   1 
ATOM   13924 N  N     . HIS   C 2 242 ? 96.182  116.622 103.465 1.00 50.28  ?  241  HIS   C N     1 
ATOM   13925 C  CA    . HIS   C 2 242 ? 96.499  116.544 102.042 1.00 38.61  ?  241  HIS   C CA    1 
ATOM   13926 C  C     . HIS   C 2 242 ? 95.475  115.701 101.293 1.00 41.59  ?  241  HIS   C C     1 
ATOM   13927 O  O     . HIS   C 2 242 ? 95.002  116.091 100.216 1.00 57.79  ?  241  HIS   C O     1 
ATOM   13928 C  CB    . HIS   C 2 242 ? 97.904  115.979 101.856 1.00 42.01  ?  241  HIS   C CB    1 
ATOM   13929 C  CG    . HIS   C 2 242 ? 98.977  116.807 102.491 1.00 45.77  ?  241  HIS   C CG    1 
ATOM   13930 N  ND1   . HIS   C 2 242 ? 100.281 116.378 102.594 1.00 55.01  ?  241  HIS   C ND1   1 
ATOM   13931 C  CD2   . HIS   C 2 242 ? 98.941  118.038 103.053 1.00 47.56  ?  241  HIS   C CD2   1 
ATOM   13932 C  CE1   . HIS   C 2 242 ? 101.003 117.307 103.193 1.00 41.56  ?  241  HIS   C CE1   1 
ATOM   13933 N  NE2   . HIS   C 2 242 ? 100.213 118.325 103.482 1.00 48.46  ?  241  HIS   C NE2   1 
ATOM   13934 N  N     . LEU   C 2 243 ? 95.111  114.545 101.853 1.00 56.17  ?  242  LEU   C N     1 
ATOM   13935 C  CA    . LEU   C 2 243 ? 94.126  113.698 101.192 1.00 55.17  ?  242  LEU   C CA    1 
ATOM   13936 C  C     . LEU   C 2 243 ? 92.752  114.354 101.183 1.00 54.00  ?  242  LEU   C C     1 
ATOM   13937 O  O     . LEU   C 2 243 ? 92.010  114.221 100.205 1.00 57.69  ?  242  LEU   C O     1 
ATOM   13938 C  CB    . LEU   C 2 243 ? 94.082  112.315 101.848 1.00 52.11  ?  242  LEU   C CB    1 
ATOM   13939 C  CG    . LEU   C 2 243 ? 93.311  112.059 103.147 1.00 56.82  ?  242  LEU   C CG    1 
ATOM   13940 C  CD1   . LEU   C 2 243 ? 91.873  111.638 102.881 1.00 56.70  ?  242  LEU   C CD1   1 
ATOM   13941 C  CD2   . LEU   C 2 243 ? 94.023  111.000 103.971 1.00 58.60  ?  242  LEU   C CD2   1 
ATOM   13942 N  N     . THR   C 2 244 ? 92.400  115.077 102.253 1.00 57.94  ?  243  THR   C N     1 
ATOM   13943 C  CA    . THR   C 2 244 ? 91.139  115.812 102.265 1.00 51.90  ?  243  THR   C CA    1 
ATOM   13944 C  C     . THR   C 2 244 ? 91.119  116.877 101.178 1.00 53.31  ?  243  THR   C C     1 
ATOM   13945 O  O     . THR   C 2 244 ? 90.111  117.051 100.481 1.00 63.41  ?  243  THR   C O     1 
ATOM   13946 C  CB    . THR   C 2 244 ? 90.915  116.447 103.636 1.00 48.34  ?  243  THR   C CB    1 
ATOM   13947 O  OG1   . THR   C 2 244 ? 90.785  115.421 104.628 1.00 63.77  ?  243  THR   C OG1   1 
ATOM   13948 C  CG2   . THR   C 2 244 ? 89.657  117.303 103.624 1.00 46.12  ?  243  THR   C CG2   1 
ATOM   13949 N  N     . GLY   C 2 245 ? 92.229  117.593 101.013 1.00 50.57  ?  244  GLY   C N     1 
ATOM   13950 C  CA    . GLY   C 2 245 ? 92.288  118.617 99.988  1.00 45.96  ?  244  GLY   C CA    1 
ATOM   13951 C  C     . GLY   C 2 245 ? 92.166  118.044 98.593  1.00 56.16  ?  244  GLY   C C     1 
ATOM   13952 O  O     . GLY   C 2 245 ? 91.439  118.577 97.752  1.00 60.78  ?  244  GLY   C O     1 
ATOM   13953 N  N     . THR   C 2 246 ? 92.871  116.947 98.328  1.00 65.67  ?  245  THR   C N     1 
ATOM   13954 C  CA    . THR   C 2 246 ? 92.748  116.333 97.014  1.00 55.81  ?  245  THR   C CA    1 
ATOM   13955 C  C     . THR   C 2 246 ? 91.335  115.803 96.786  1.00 58.52  ?  245  THR   C C     1 
ATOM   13956 O  O     . THR   C 2 246 ? 90.813  115.868 95.666  1.00 69.76  ?  245  THR   C O     1 
ATOM   13957 C  CB    . THR   C 2 246 ? 93.785  115.222 96.847  1.00 61.84  ?  245  THR   C CB    1 
ATOM   13958 O  OG1   . THR   C 2 246 ? 95.062  115.803 96.562  1.00 74.46  ?  245  THR   C OG1   1 
ATOM   13959 C  CG2   . THR   C 2 246 ? 93.422  114.374 95.689  1.00 65.67  ?  245  THR   C CG2   1 
ATOM   13960 N  N     . GLN   C 2 247 ? 90.726  115.213 97.820  1.00 58.08  ?  246  GLN   C N     1 
ATOM   13961 C  CA    . GLN   C 2 247 ? 89.369  114.696 97.690  1.00 56.72  ?  246  GLN   C CA    1 
ATOM   13962 C  C     . GLN   C 2 247 ? 88.391  115.809 97.356  1.00 61.08  ?  246  GLN   C C     1 
ATOM   13963 O  O     . GLN   C 2 247 ? 87.511  115.638 96.507  1.00 68.38  ?  246  GLN   C O     1 
ATOM   13964 C  CB    . GLN   C 2 247 ? 88.947  113.992 98.980  1.00 54.58  ?  246  GLN   C CB    1 
ATOM   13965 C  CG    . GLN   C 2 247 ? 89.336  112.530 99.058  1.00 62.24  ?  246  GLN   C CG    1 
ATOM   13966 C  CD    . GLN   C 2 247 ? 88.958  111.901 100.381 1.00 67.02  ?  246  GLN   C CD    1 
ATOM   13967 O  OE1   . GLN   C 2 247 ? 88.403  112.561 101.258 1.00 70.50  ?  246  GLN   C OE1   1 
ATOM   13968 N  NE2   . GLN   C 2 247 ? 89.261  110.619 100.535 1.00 68.38  ?  246  GLN   C NE2   1 
ATOM   13969 N  N     . HIS   C 2 248 ? 88.528  116.958 98.018  1.00 65.60  ?  247  HIS   C N     1 
ATOM   13970 C  CA    . HIS   C 2 248 ? 87.653  118.086 97.722  1.00 60.45  ?  247  HIS   C CA    1 
ATOM   13971 C  C     . HIS   C 2 248 ? 87.908  118.634 96.323  1.00 66.91  ?  247  HIS   C C     1 
ATOM   13972 O  O     . HIS   C 2 248 ? 86.964  119.000 95.612  1.00 72.99  ?  247  HIS   C O     1 
ATOM   13973 C  CB    . HIS   C 2 248 ? 87.834  119.176 98.775  1.00 61.97  ?  247  HIS   C CB    1 
ATOM   13974 C  CG    . HIS   C 2 248 ? 86.960  119.000 99.977  1.00 68.28  ?  247  HIS   C CG    1 
ATOM   13975 N  ND1   . HIS   C 2 248 ? 87.467  118.781 101.238 1.00 69.04  ?  247  HIS   C ND1   1 
ATOM   13976 C  CD2   . HIS   C 2 248 ? 85.613  119.011 100.110 1.00 69.52  ?  247  HIS   C CD2   1 
ATOM   13977 C  CE1   . HIS   C 2 248 ? 86.471  118.655 102.095 1.00 69.39  ?  247  HIS   C CE1   1 
ATOM   13978 N  NE2   . HIS   C 2 248 ? 85.335  118.794 101.437 1.00 72.79  ?  247  HIS   C NE2   1 
ATOM   13979 N  N     . MET   C 2 249 ? 89.176  118.684 95.908  1.00 73.06  ?  248  MET   C N     1 
ATOM   13980 C  CA    . MET   C 2 249 ? 89.502  119.126 94.556  1.00 65.19  ?  248  MET   C CA    1 
ATOM   13981 C  C     . MET   C 2 249 ? 88.868  118.217 93.511  1.00 70.90  ?  248  MET   C C     1 
ATOM   13982 O  O     . MET   C 2 249 ? 88.376  118.693 92.482  1.00 80.35  ?  248  MET   C O     1 
ATOM   13983 C  CB    . MET   C 2 249 ? 91.017  119.173 94.376  1.00 64.59  ?  248  MET   C CB    1 
ATOM   13984 C  CG    . MET   C 2 249 ? 91.603  120.565 94.273  1.00 72.28  ?  248  MET   C CG    1 
ATOM   13985 S  SD    . MET   C 2 249 ? 93.380  120.538 93.963  1.00 84.82  ?  248  MET   C SD    1 
ATOM   13986 C  CE    . MET   C 2 249 ? 93.996  120.000 95.555  1.00 66.33  ?  248  MET   C CE    1 
ATOM   13987 N  N     . LEU   C 2 250 ? 88.863  116.907 93.764  1.00 67.03  ?  249  LEU   C N     1 
ATOM   13988 C  CA    . LEU   C 2 250 ? 88.267  115.967 92.822  1.00 61.18  ?  249  LEU   C CA    1 
ATOM   13989 C  C     . LEU   C 2 250 ? 86.746  116.038 92.842  1.00 64.82  ?  249  LEU   C C     1 
ATOM   13990 O  O     . LEU   C 2 250 ? 86.105  115.961 91.788  1.00 73.98  ?  249  LEU   C O     1 
ATOM   13991 C  CB    . LEU   C 2 250 ? 88.741  114.550 93.132  1.00 61.04  ?  249  LEU   C CB    1 
ATOM   13992 C  CG    . LEU   C 2 250 ? 90.134  114.208 92.611  1.00 65.33  ?  249  LEU   C CG    1 
ATOM   13993 C  CD1   . LEU   C 2 250 ? 90.637  112.910 93.217  1.00 64.77  ?  249  LEU   C CD1   1 
ATOM   13994 C  CD2   . LEU   C 2 250 ? 90.111  114.135 91.097  1.00 61.11  ?  249  LEU   C CD2   1 
ATOM   13995 N  N     . ASN   C 2 251 ? 86.150  116.187 94.027  1.00 69.13  ?  250  ASN   C N     1 
ATOM   13996 C  CA    . ASN   C 2 251 ? 84.696  116.192 94.126  1.00 69.75  ?  250  ASN   C CA    1 
ATOM   13997 C  C     . ASN   C 2 251 ? 84.097  117.477 93.575  1.00 72.71  ?  250  ASN   C C     1 
ATOM   13998 O  O     . ASN   C 2 251 ? 82.964  117.464 93.082  1.00 78.98  ?  250  ASN   C O     1 
ATOM   13999 C  CB    . ASN   C 2 251 ? 84.270  115.981 95.578  1.00 66.88  ?  250  ASN   C CB    1 
ATOM   14000 C  CG    . ASN   C 2 251 ? 84.321  114.524 95.992  1.00 74.27  ?  250  ASN   C CG    1 
ATOM   14001 O  OD1   . ASN   C 2 251 ? 84.010  113.632 95.204  1.00 80.37  ?  250  ASN   C OD1   1 
ATOM   14002 N  ND2   . ASN   C 2 251 ? 84.716  114.275 97.234  1.00 76.83  ?  250  ASN   C ND2   1 
ATOM   14003 N  N     . LEU   C 2 252 ? 84.829  118.591 93.648  1.00 67.50  ?  251  LEU   C N     1 
ATOM   14004 C  CA    . LEU   C 2 252 ? 84.330  119.826 93.058  1.00 70.23  ?  251  LEU   C CA    1 
ATOM   14005 C  C     . LEU   C 2 252 ? 84.406  119.811 91.538  1.00 74.28  ?  251  LEU   C C     1 
ATOM   14006 O  O     . LEU   C 2 252 ? 83.697  120.586 90.889  1.00 80.03  ?  251  LEU   C O     1 
ATOM   14007 C  CB    . LEU   C 2 252 ? 85.100  121.023 93.615  1.00 70.04  ?  251  LEU   C CB    1 
ATOM   14008 C  CG    . LEU   C 2 252 ? 84.694  121.447 95.027  1.00 71.37  ?  251  LEU   C CG    1 
ATOM   14009 C  CD1   . LEU   C 2 252 ? 85.748  122.344 95.654  1.00 73.09  ?  251  LEU   C CD1   1 
ATOM   14010 C  CD2   . LEU   C 2 252 ? 83.340  122.133 95.008  1.00 72.75  ?  251  LEU   C CD2   1 
ATOM   14011 N  N     . LEU   C 2 253 ? 85.248  118.956 90.961  1.00 76.16  ?  252  LEU   C N     1 
ATOM   14012 C  CA    . LEU   C 2 253 ? 85.341  118.808 89.516  1.00 75.55  ?  252  LEU   C CA    1 
ATOM   14013 C  C     . LEU   C 2 253 ? 84.380  117.766 88.963  1.00 78.44  ?  252  LEU   C C     1 
ATOM   14014 O  O     . LEU   C 2 253 ? 84.211  117.691 87.742  1.00 84.62  ?  252  LEU   C O     1 
ATOM   14015 C  CB    . LEU   C 2 253 ? 86.771  118.435 89.113  1.00 74.77  ?  252  LEU   C CB    1 
ATOM   14016 C  CG    . LEU   C 2 253 ? 87.755  119.550 88.755  1.00 74.62  ?  252  LEU   C CG    1 
ATOM   14017 C  CD1   . LEU   C 2 253 ? 87.619  120.726 89.695  1.00 78.83  ?  252  LEU   C CD1   1 
ATOM   14018 C  CD2   . LEU   C 2 253 ? 89.176  119.016 88.772  1.00 75.67  ?  252  LEU   C CD2   1 
ATOM   14019 N  N     . ARG   C 2 254 ? 83.757  116.961 89.822  1.00 85.95  ?  253  ARG   C N     1 
ATOM   14020 C  CA    . ARG   C 2 254 ? 82.838  115.914 89.398  1.00 83.49  ?  253  ARG   C CA    1 
ATOM   14021 C  C     . ARG   C 2 254 ? 81.382  116.352 89.453  1.00 86.65  ?  253  ARG   C C     1 
ATOM   14022 O  O     . ARG   C 2 254 ? 80.591  115.968 88.587  1.00 90.02  ?  253  ARG   C O     1 
ATOM   14023 C  CB    . ARG   C 2 254 ? 83.030  114.665 90.263  1.00 78.72  ?  253  ARG   C CB    1 
ATOM   14024 C  CG    . ARG   C 2 254 ? 82.293  113.437 89.767  1.00 83.15  ?  253  ARG   C CG    1 
ATOM   14025 C  CD    . ARG   C 2 254 ? 82.813  112.181 90.442  1.00 88.10  ?  253  ARG   C CD    1 
ATOM   14026 N  NE    . ARG   C 2 254 ? 82.952  112.356 91.882  1.00 85.39  ?  253  ARG   C NE    1 
ATOM   14027 C  CZ    . ARG   C 2 254 ? 81.997  112.096 92.764  1.00 86.63  ?  253  ARG   C CZ    1 
ATOM   14028 N  NH1   . ARG   C 2 254 ? 80.812  111.645 92.387  1.00 87.53  ?  253  ARG   C NH1   1 
ATOM   14029 N  NH2   . ARG   C 2 254 ? 82.236  112.294 94.057  1.00 85.96  ?  253  ARG   C NH2   1 
ATOM   14030 N  N     . SER   C 2 255 ? 81.013  117.156 90.452  1.00 95.94  ?  254  SER   C N     1 
ATOM   14031 C  CA    . SER   C 2 255 ? 79.646  117.647 90.573  1.00 99.39  ?  254  SER   C CA    1 
ATOM   14032 C  C     . SER   C 2 255 ? 79.301  118.705 89.534  1.00 100.95 ?  254  SER   C C     1 
ATOM   14033 O  O     . SER   C 2 255 ? 78.117  119.007 89.349  1.00 103.98 ?  254  SER   C O     1 
ATOM   14034 C  CB    . SER   C 2 255 ? 79.415  118.208 91.976  1.00 97.99  ?  254  SER   C CB    1 
ATOM   14035 O  OG    . SER   C 2 255 ? 80.144  119.403 92.171  1.00 95.84  ?  254  SER   C OG    1 
ATOM   14036 N  N     . GLY   C 2 256 ? 80.294  119.269 88.855  1.00 100.27 ?  255  GLY   C N     1 
ATOM   14037 C  CA    . GLY   C 2 256 ? 80.053  120.296 87.867  1.00 100.55 ?  255  GLY   C CA    1 
ATOM   14038 C  C     . GLY   C 2 256 ? 79.877  121.691 88.418  1.00 104.53 ?  255  GLY   C C     1 
ATOM   14039 O  O     . GLY   C 2 256 ? 79.497  122.593 87.661  1.00 103.07 ?  255  GLY   C O     1 
ATOM   14040 N  N     . ALA   C 2 257 ? 80.157  121.905 89.707  1.00 106.96 ?  256  ALA   C N     1 
ATOM   14041 C  CA    . ALA   C 2 257 ? 79.941  123.213 90.311  1.00 103.33 ?  256  ALA   C CA    1 
ATOM   14042 C  C     . ALA   C 2 257 ? 80.944  124.239 89.812  1.00 105.01 ?  256  ALA   C C     1 
ATOM   14043 O  O     . ALA   C 2 257 ? 80.723  125.442 89.983  1.00 105.01 ?  256  ALA   C O     1 
ATOM   14044 C  CB    . ALA   C 2 257 ? 80.007  123.115 91.836  1.00 101.64 ?  256  ALA   C CB    1 
ATOM   14045 N  N     . ASP   C 2 258 ? 82.037  123.793 89.201  1.00 109.58 ?  257  ASP   C N     1 
ATOM   14046 C  CA    . ASP   C 2 258 ? 83.032  124.692 88.634  1.00 109.21 ?  257  ASP   C CA    1 
ATOM   14047 C  C     . ASP   C 2 258 ? 82.983  124.770 87.118  1.00 113.08 ?  257  ASP   C C     1 
ATOM   14048 O  O     . ASP   C 2 258 ? 83.256  125.831 86.555  1.00 113.00 ?  257  ASP   C O     1 
ATOM   14049 C  CB    . ASP   C 2 258 ? 84.441  124.267 89.066  1.00 109.86 ?  257  ASP   C CB    1 
ATOM   14050 C  CG    . ASP   C 2 258 ? 84.902  124.971 90.327  1.00 112.00 ?  257  ASP   C CG    1 
ATOM   14051 O  OD1   . ASP   C 2 258 ? 85.178  126.187 90.268  1.00 111.35 ?  257  ASP   C OD1   1 
ATOM   14052 O  OD2   . ASP   C 2 258 ? 84.989  124.303 91.377  1.00 113.52 ?  257  ASP   C OD2   1 
ATOM   14053 N  N     . ASP   C 2 259 ? 82.695  123.659 86.444  1.00 121.81 ?  258  ASP   C N     1 
ATOM   14054 C  CA    . ASP   C 2 259 ? 82.646  123.600 84.990  1.00 119.17 ?  258  ASP   C CA    1 
ATOM   14055 C  C     . ASP   C 2 259 ? 81.727  122.458 84.581  1.00 120.64 ?  258  ASP   C C     1 
ATOM   14056 O  O     . ASP   C 2 259 ? 81.964  121.306 84.965  1.00 123.01 ?  258  ASP   C O     1 
ATOM   14057 C  CB    . ASP   C 2 259 ? 84.053  123.415 84.412  1.00 117.46 ?  258  ASP   C CB    1 
ATOM   14058 C  CG    . ASP   C 2 259 ? 84.072  123.389 82.893  1.00 121.02 ?  258  ASP   C CG    1 
ATOM   14059 O  OD1   . ASP   C 2 259 ? 83.014  123.590 82.263  1.00 121.24 ?  258  ASP   C OD1   1 
ATOM   14060 O  OD2   . ASP   C 2 259 ? 85.162  123.168 82.327  1.00 121.16 ?  258  ASP   C OD2   1 
ATOM   14061 N  N     . PRO   C 2 260 ? 80.659  122.736 83.832  1.00 107.32 ?  259  PRO   C N     1 
ATOM   14062 C  CA    . PRO   C 2 260 ? 79.783  121.640 83.388  1.00 108.20 ?  259  PRO   C CA    1 
ATOM   14063 C  C     . PRO   C 2 260 ? 80.508  120.596 82.556  1.00 109.06 ?  259  PRO   C C     1 
ATOM   14064 O  O     . PRO   C 2 260 ? 80.039  119.455 82.466  1.00 109.73 ?  259  PRO   C O     1 
ATOM   14065 C  CB    . PRO   C 2 260 ? 78.694  122.351 82.567  1.00 106.89 ?  259  PRO   C CB    1 
ATOM   14066 C  CG    . PRO   C 2 260 ? 78.843  123.808 82.824  1.00 108.40 ?  259  PRO   C CG    1 
ATOM   14067 C  CD    . PRO   C 2 260 ? 80.115  124.076 83.549  1.00 105.02 ?  259  PRO   C CD    1 
ATOM   14068 N  N     . GLU   C 2 261 ? 81.575  120.984 81.853  1.00 113.14 ?  260  GLU   C N     1 
ATOM   14069 C  CA    . GLU   C 2 261 ? 82.308  120.032 81.026  1.00 110.93 ?  260  GLU   C CA    1 
ATOM   14070 C  C     . GLU   C 2 261 ? 83.075  119.030 81.877  1.00 113.37 ?  260  GLU   C C     1 
ATOM   14071 O  O     . GLU   C 2 261 ? 83.214  117.864 81.485  1.00 114.54 ?  260  GLU   C O     1 
ATOM   14072 C  CB    . GLU   C 2 261 ? 83.266  120.771 80.088  1.00 110.46 ?  260  GLU   C CB    1 
ATOM   14073 C  CG    . GLU   C 2 261 ? 83.839  119.908 78.975  1.00 114.20 ?  260  GLU   C CG    1 
ATOM   14074 C  CD    . GLU   C 2 261 ? 84.774  120.680 78.065  1.00 117.31 ?  260  GLU   C CD    1 
ATOM   14075 O  OE1   . GLU   C 2 261 ? 85.221  121.773 78.469  1.00 116.36 ?  260  GLU   C OE1   1 
ATOM   14076 O  OE2   . GLU   C 2 261 ? 85.064  120.197 76.949  1.00 117.49 ?  260  GLU   C OE2   1 
ATOM   14077 N  N     . MET   C 2 262 ? 83.584  119.467 83.033  1.00 106.16 ?  261  MET   C N     1 
ATOM   14078 C  CA    . MET   C 2 262 ? 84.350  118.575 83.896  1.00 101.96 ?  261  MET   C CA    1 
ATOM   14079 C  C     . MET   C 2 262 ? 83.502  117.419 84.403  1.00 104.37 ?  261  MET   C C     1 
ATOM   14080 O  O     . MET   C 2 262 ? 84.017  116.312 84.591  1.00 109.90 ?  261  MET   C O     1 
ATOM   14081 C  CB    . MET   C 2 262 ? 84.941  119.350 85.074  1.00 102.78 ?  261  MET   C CB    1 
ATOM   14082 C  CG    . MET   C 2 262 ? 86.443  119.558 84.980  1.00 103.67 ?  261  MET   C CG    1 
ATOM   14083 S  SD    . MET   C 2 262 ? 87.352  118.004 85.036  1.00 108.72 ?  261  MET   C SD    1 
ATOM   14084 C  CE    . MET   C 2 262 ? 89.033  118.599 84.907  1.00 104.35 ?  261  MET   C CE    1 
ATOM   14085 N  N     . ALA   C 2 263 ? 82.206  117.651 84.625  1.00 98.26  ?  262  ALA   C N     1 
ATOM   14086 C  CA    . ALA   C 2 263 ? 81.339  116.581 85.107  1.00 100.13 ?  262  ALA   C CA    1 
ATOM   14087 C  C     . ALA   C 2 263 ? 81.269  115.441 84.100  1.00 102.30 ?  262  ALA   C C     1 
ATOM   14088 O  O     . ALA   C 2 263 ? 81.488  114.272 84.444  1.00 105.99 ?  262  ALA   C O     1 
ATOM   14089 C  CB    . ALA   C 2 263 ? 79.943  117.129 85.404  1.00 99.22  ?  262  ALA   C CB    1 
ATOM   14090 N  N     . GLU   C 2 264 ? 80.990  115.766 82.837  1.00 103.06 ?  263  GLU   C N     1 
ATOM   14091 C  CA    . GLU   C 2 264 ? 80.919  114.718 81.827  1.00 104.95 ?  263  GLU   C CA    1 
ATOM   14092 C  C     . GLU   C 2 264 ? 82.295  114.134 81.529  1.00 105.78 ?  263  GLU   C C     1 
ATOM   14093 O  O     . GLU   C 2 264 ? 82.402  112.941 81.225  1.00 108.13 ?  263  GLU   C O     1 
ATOM   14094 C  CB    . GLU   C 2 264 ? 80.255  115.246 80.554  1.00 102.87 ?  263  GLU   C CB    1 
ATOM   14095 C  CG    . GLU   C 2 264 ? 80.996  116.365 79.854  1.00 104.68 ?  263  GLU   C CG    1 
ATOM   14096 C  CD    . GLU   C 2 264 ? 80.222  116.917 78.674  1.00 110.23 ?  263  GLU   C CD    1 
ATOM   14097 O  OE1   . GLU   C 2 264 ? 79.296  116.229 78.195  1.00 109.74 ?  263  GLU   C OE1   1 
ATOM   14098 O  OE2   . GLU   C 2 264 ? 80.542  118.037 78.221  1.00 109.29 ?  263  GLU   C OE2   1 
ATOM   14099 N  N     . ILE   C 2 265 ? 83.357  114.938 81.636  1.00 95.87  ?  264  ILE   C N     1 
ATOM   14100 C  CA    . ILE   C 2 265 ? 84.702  114.399 81.443  1.00 92.50  ?  264  ILE   C CA    1 
ATOM   14101 C  C     . ILE   C 2 265 ? 85.006  113.342 82.500  1.00 94.90  ?  264  ILE   C C     1 
ATOM   14102 O  O     . ILE   C 2 265 ? 85.531  112.262 82.193  1.00 98.96  ?  264  ILE   C O     1 
ATOM   14103 C  CB    . ILE   C 2 265 ? 85.740  115.537 81.456  1.00 90.00  ?  264  ILE   C CB    1 
ATOM   14104 C  CG1   . ILE   C 2 265 ? 85.746  116.271 80.115  1.00 91.79  ?  264  ILE   C CG1   1 
ATOM   14105 C  CG2   . ILE   C 2 265 ? 87.127  114.996 81.771  1.00 92.55  ?  264  ILE   C CG2   1 
ATOM   14106 C  CD1   . ILE   C 2 265 ? 86.745  117.399 80.044  1.00 94.36  ?  264  ILE   C CD1   1 
ATOM   14107 N  N     . ALA   C 2 266 ? 84.666  113.628 83.759  1.00 94.89  ?  265  ALA   C N     1 
ATOM   14108 C  CA    . ALA   C 2 266 ? 84.851  112.647 84.821  1.00 94.83  ?  265  ALA   C CA    1 
ATOM   14109 C  C     . ALA   C 2 266 ? 83.955  111.432 84.616  1.00 98.79  ?  265  ALA   C C     1 
ATOM   14110 O  O     . ALA   C 2 266 ? 84.354  110.305 84.925  1.00 106.98 ?  265  ALA   C O     1 
ATOM   14111 C  CB    . ALA   C 2 266 ? 84.589  113.291 86.181  1.00 92.97  ?  265  ALA   C CB    1 
ATOM   14112 N  N     . GLU   C 2 267 ? 82.739  111.640 84.103  1.00 105.41 ?  266  GLU   C N     1 
ATOM   14113 C  CA    . GLU   C 2 267 ? 81.865  110.508 83.805  1.00 106.99 ?  266  GLU   C CA    1 
ATOM   14114 C  C     . GLU   C 2 267 ? 82.488  109.588 82.766  1.00 107.66 ?  266  GLU   C C     1 
ATOM   14115 O  O     . GLU   C 2 267 ? 82.387  108.360 82.865  1.00 108.81 ?  266  GLU   C O     1 
ATOM   14116 C  CB    . GLU   C 2 267 ? 80.496  111.004 83.337  1.00 107.75 ?  266  GLU   C CB    1 
ATOM   14117 C  CG    . GLU   C 2 267 ? 79.358  109.994 83.502  1.00 110.62 ?  266  GLU   C CG    1 
ATOM   14118 C  CD    . GLU   C 2 267 ? 79.245  109.428 84.907  1.00 114.29 ?  266  GLU   C CD    1 
ATOM   14119 O  OE1   . GLU   C 2 267 ? 79.866  109.989 85.831  1.00 112.08 ?  266  GLU   C OE1   1 
ATOM   14120 O  OE2   . GLU   C 2 267 ? 78.536  108.418 85.095  1.00 115.43 ?  266  GLU   C OE2   1 
ATOM   14121 N  N     . GLU   C 2 268 ? 83.258  110.173 81.845  1.00 111.11 ?  267  GLU   C N     1 
ATOM   14122 C  CA    . GLU   C 2 268 ? 83.982  109.342 80.845  1.00 110.22 ?  267  GLU   C CA    1 
ATOM   14123 C  C     . GLU   C 2 268 ? 85.162  108.629 81.519  1.00 112.69 ?  267  GLU   C C     1 
ATOM   14124 O  O     . GLU   C 2 268 ? 85.866  107.875 80.818  1.00 115.56 ?  267  GLU   C O     1 
ATOM   14125 C  CB    . GLU   C 2 268 ? 84.464  110.217 79.687  1.00 111.93 ?  267  GLU   C CB    1 
ATOM   14126 C  CG    . GLU   C 2 268 ? 83.328  110.819 78.882  1.00 114.57 ?  267  GLU   C CG    1 
ATOM   14127 C  CD    . GLU   C 2 268 ? 83.755  111.878 77.882  1.00 117.15 ?  267  GLU   C CD    1 
ATOM   14128 O  OE1   . GLU   C 2 268 ? 84.962  112.186 77.827  1.00 115.36 ?  267  GLU   C OE1   1 
ATOM   14129 O  OE2   . GLU   C 2 268 ? 82.878  112.392 77.160  1.00 117.94 ?  267  GLU   C OE2   1 
ATOM   14130 N  N     . CYS   C 2 269 ? 85.369  108.856 82.822  1.00 109.36 ?  268  CYS   C N     1 
ATOM   14131 C  CA    . CYS   C 2 269 ? 86.476  108.187 83.563  1.00 106.10 ?  268  CYS   C CA    1 
ATOM   14132 C  C     . CYS   C 2 269 ? 85.903  107.295 84.669  1.00 109.37 ?  268  CYS   C C     1 
ATOM   14133 O  O     . CYS   C 2 269 ? 86.480  107.282 85.773  1.00 114.71 ?  268  CYS   C O     1 
ATOM   14134 C  CB    . CYS   C 2 269 ? 87.423  109.199 84.199  1.00 106.12 ?  268  CYS   C CB    1 
ATOM   14135 S  SG    . CYS   C 2 269 ? 88.927  108.439 84.871  1.00 129.81 ?  268  CYS   C SG    1 
ATOM   14136 N  N     . LYS   C 2 270 ? 84.811  106.596 84.466  1.00 97.89  ?  269  LYS   C N     1 
ATOM   14137 C  CA    . LYS   C 2 270 ? 84.419  105.725 85.604  1.00 96.86  ?  269  LYS   C CA    1 
ATOM   14138 C  C     . LYS   C 2 270 ? 85.128  104.368 85.442  1.00 100.62 ?  269  LYS   C C     1 
ATOM   14139 O  O     . LYS   C 2 270 ? 84.928  103.516 86.323  1.00 107.07 ?  269  LYS   C O     1 
ATOM   14140 C  CB    . LYS   C 2 270 ? 82.901  105.694 85.805  1.00 95.61  ?  269  LYS   C CB    1 
ATOM   14141 C  CG    . LYS   C 2 270 ? 82.287  107.045 86.144  1.00 98.13  ?  269  LYS   C CG    1 
ATOM   14142 C  CD    . LYS   C 2 270 ? 80.801  106.972 86.408  1.00 100.86 ?  269  LYS   C CD    1 
ATOM   14143 C  CE    . LYS   C 2 270 ? 80.469  106.283 87.714  1.00 100.36 ?  269  LYS   C CE    1 
ATOM   14144 N  NZ    . LYS   C 2 270 ? 80.905  107.084 88.882  1.00 100.83 ?  269  LYS   C NZ    1 
ATOM   14145 N  N     . GLN   C 2 271 ? 85.940  104.176 84.393  1.00 98.31  ?  270  GLN   C N     1 
ATOM   14146 C  CA    . GLN   C 2 271 ? 86.739  102.927 84.271  1.00 95.70  ?  270  GLN   C CA    1 
ATOM   14147 C  C     . GLN   C 2 271 ? 88.228  103.249 84.441  1.00 95.61  ?  270  GLN   C C     1 
ATOM   14148 O  O     . GLN   C 2 271 ? 88.902  102.523 85.188  1.00 99.07  ?  270  GLN   C O     1 
ATOM   14149 C  CB    . GLN   C 2 271 ? 86.481  102.251 82.924  1.00 96.13  ?  270  GLN   C CB    1 
ATOM   14150 C  CG    . GLN   C 2 271 ? 87.074  100.853 82.833  1.00 98.04  ?  270  GLN   C CG    1 
ATOM   14151 C  CD    . GLN   C 2 271 ? 86.535  99.950  83.915  1.00 101.34 ?  270  GLN   C CD    1 
ATOM   14152 O  OE1   . GLN   C 2 271 ? 85.335  99.699  83.999  1.00 103.24 ?  270  GLN   C OE1   1 
ATOM   14153 N  NE2   . GLN   C 2 271 ? 87.424  99.453  84.759  1.00 98.06  ?  270  GLN   C NE2   1 
ATOM   14154 N  N     . GLU   C 2 272 ? 88.677  104.335 83.843  1.00 90.92  ?  271  GLU   C N     1 
ATOM   14155 C  CA    . GLU   C 2 272 ? 90.102  104.713 83.882  1.00 86.66  ?  271  GLU   C CA    1 
ATOM   14156 C  C     . GLU   C 2 272 ? 90.474  105.017 85.314  1.00 90.99  ?  271  GLU   C C     1 
ATOM   14157 O  O     . GLU   C 2 272 ? 91.375  104.415 85.821  1.00 97.49  ?  271  GLU   C O     1 
ATOM   14158 C  CB    . GLU   C 2 272 ? 90.412  105.866 82.953  1.00 84.97  ?  271  GLU   C CB    1 
ATOM   14159 C  CG    . GLU   C 2 272 ? 91.860  106.271 82.967  1.00 92.71  ?  271  GLU   C CG    1 
ATOM   14160 C  CD    . GLU   C 2 272 ? 92.334  106.864 81.655  1.00 97.43  ?  271  GLU   C CD    1 
ATOM   14161 O  OE1   . GLU   C 2 272 ? 91.481  107.163 80.801  1.00 96.49  ?  271  GLU   C OE1   1 
ATOM   14162 O  OE2   . GLU   C 2 272 ? 93.558  107.010 81.483  1.00 95.36  ?  271  GLU   C OE2   1 
ATOM   14163 N  N     . CYS   C 2 273 ? 89.826  105.981 85.909  1.00 91.73  ?  272  CYS   C N     1 
ATOM   14164 C  CA    . CYS   C 2 273 ? 90.045  106.335 87.330  1.00 90.24  ?  272  CYS   C CA    1 
ATOM   14165 C  C     . CYS   C 2 273 ? 89.996  105.039 88.143  1.00 90.71  ?  272  CYS   C C     1 
ATOM   14166 O  O     . CYS   C 2 273 ? 90.891  104.847 88.972  1.00 96.46  ?  272  CYS   C O     1 
ATOM   14167 C  CB    . CYS   C 2 273 ? 88.995  107.350 87.781  1.00 91.66  ?  272  CYS   C CB    1 
ATOM   14168 S  SG    . CYS   C 2 273 ? 88.943  108.917 86.853  1.00 110.01 ?  272  CYS   C SG    1 
ATOM   14169 N  N     . TYR   C 2 274 ? 88.995  104.190 87.922  1.00 84.04  ?  273  TYR   C N     1 
ATOM   14170 C  CA    . TYR   C 2 274 ? 88.888  102.876 88.603  1.00 85.13  ?  273  TYR   C CA    1 
ATOM   14171 C  C     . TYR   C 2 274 ? 90.133  102.035 88.334  1.00 85.49  ?  273  TYR   C C     1 
ATOM   14172 O  O     . TYR   C 2 274 ? 90.760  101.589 89.299  1.00 90.09  ?  273  TYR   C O     1 
ATOM   14173 C  CB    . TYR   C 2 274 ? 87.710  102.101 88.030  1.00 84.99  ?  273  TYR   C CB    1 
ATOM   14174 C  CG    . TYR   C 2 274 ? 87.233  100.917 88.827  1.00 89.66  ?  273  TYR   C CG    1 
ATOM   14175 C  CD1   . TYR   C 2 274 ? 86.442  101.081 89.950  1.00 90.67  ?  273  TYR   C CD1   1 
ATOM   14176 C  CD2   . TYR   C 2 274 ? 87.563  99.628  88.447  1.00 88.49  ?  273  TYR   C CD2   1 
ATOM   14177 C  CE1   . TYR   C 2 274 ? 85.989  99.994  90.677  1.00 93.35  ?  273  TYR   C CE1   1 
ATOM   14178 C  CE2   . TYR   C 2 274 ? 87.123  98.531  89.164  1.00 88.48  ?  273  TYR   C CE2   1 
ATOM   14179 C  CZ    . TYR   C 2 274 ? 86.332  98.716  90.281  1.00 93.38  ?  273  TYR   C CZ    1 
ATOM   14180 O  OH    . TYR   C 2 274 ? 85.890  97.634  90.995  1.00 93.61  ?  273  TYR   C OH    1 
ATOM   14181 N  N     . ASP   C 2 275 ? 90.455  101.790 87.069  1.00 84.67  ?  274  ASP   C N     1 
ATOM   14182 C  CA    . ASP   C 2 275 ? 91.626  100.994 86.713  1.00 82.17  ?  274  ASP   C CA    1 
ATOM   14183 C  C     . ASP   C 2 275 ? 92.881  101.504 87.409  1.00 85.68  ?  274  ASP   C C     1 
ATOM   14184 O  O     . ASP   C 2 275 ? 93.714  100.712 87.861  1.00 89.42  ?  274  ASP   C O     1 
ATOM   14185 C  CB    . ASP   C 2 275 ? 91.813  101.002 85.194  1.00 86.42  ?  274  ASP   C CB    1 
ATOM   14186 C  CG    . ASP   C 2 275 ? 90.789  100.144 84.478  1.00 92.63  ?  274  ASP   C CG    1 
ATOM   14187 O  OD1   . ASP   C 2 275 ? 89.971  99.496  85.164  1.00 95.18  ?  274  ASP   C OD1   1 
ATOM   14188 O  OD2   . ASP   C 2 275 ? 90.800  100.119 83.230  1.00 93.35  ?  274  ASP   C OD2   1 
ATOM   14189 N  N     . LEU   C 2 276 ? 93.025  102.825 87.512  1.00 71.67  ?  275  LEU   C N     1 
ATOM   14190 C  CA    . LEU   C 2 276 ? 94.184  103.405 88.183  1.00 68.63  ?  275  LEU   C CA    1 
ATOM   14191 C  C     . LEU   C 2 276 ? 94.220  103.011 89.653  1.00 72.64  ?  275  LEU   C C     1 
ATOM   14192 O  O     . LEU   C 2 276 ? 95.278  102.641 90.178  1.00 76.07  ?  275  LEU   C O     1 
ATOM   14193 C  CB    . LEU   C 2 276 ? 94.163  104.925 88.021  1.00 69.07  ?  275  LEU   C CB    1 
ATOM   14194 C  CG    . LEU   C 2 276 ? 95.191  105.825 88.715  1.00 72.97  ?  275  LEU   C CG    1 
ATOM   14195 C  CD1   . LEU   C 2 276 ? 95.383  107.091 87.903  1.00 71.27  ?  275  LEU   C CD1   1 
ATOM   14196 C  CD2   . LEU   C 2 276 ? 94.781  106.188 90.136  1.00 71.48  ?  275  LEU   C CD2   1 
ATOM   14197 N  N     . PHE   C 2 277 ? 93.067  103.069 90.326  1.00 71.23  ?  276  PHE   C N     1 
ATOM   14198 C  CA    . PHE   C 2 277 ? 93.031  102.689 91.738  1.00 64.42  ?  276  PHE   C CA    1 
ATOM   14199 C  C     . PHE   C 2 277 ? 93.311  101.200 91.925  1.00 70.04  ?  276  PHE   C C     1 
ATOM   14200 O  O     . PHE   C 2 277 ? 94.015  100.807 92.864  1.00 70.46  ?  276  PHE   C O     1 
ATOM   14201 C  CB    . PHE   C 2 277 ? 91.687  103.077 92.345  1.00 66.22  ?  276  PHE   C CB    1 
ATOM   14202 C  CG    . PHE   C 2 277 ? 91.738  104.338 93.158  1.00 69.16  ?  276  PHE   C CG    1 
ATOM   14203 C  CD1   . PHE   C 2 277 ? 91.548  105.571 92.565  1.00 63.13  ?  276  PHE   C CD1   1 
ATOM   14204 C  CD2   . PHE   C 2 277 ? 92.001  104.293 94.513  1.00 71.88  ?  276  PHE   C CD2   1 
ATOM   14205 C  CE1   . PHE   C 2 277 ? 91.603  106.729 93.316  1.00 62.78  ?  276  PHE   C CE1   1 
ATOM   14206 C  CE2   . PHE   C 2 277 ? 92.043  105.452 95.262  1.00 73.97  ?  276  PHE   C CE2   1 
ATOM   14207 C  CZ    . PHE   C 2 277 ? 91.849  106.668 94.662  1.00 66.32  ?  276  PHE   C CZ    1 
ATOM   14208 N  N     . VAL   C 2 278 ? 92.781  100.359 91.034  1.00 77.01  ?  277  VAL   C N     1 
ATOM   14209 C  CA    . VAL   C 2 278 ? 93.059  98.924  91.113  1.00 69.62  ?  277  VAL   C CA    1 
ATOM   14210 C  C     . VAL   C 2 278 ? 94.549  98.658  90.917  1.00 73.71  ?  277  VAL   C C     1 
ATOM   14211 O  O     . VAL   C 2 278 ? 95.149  97.830  91.618  1.00 80.43  ?  277  VAL   C O     1 
ATOM   14212 C  CB    . VAL   C 2 278 ? 92.201  98.155  90.092  1.00 72.42  ?  277  VAL   C CB    1 
ATOM   14213 C  CG1   . VAL   C 2 278 ? 92.742  96.750  89.882  1.00 76.35  ?  277  VAL   C CG1   1 
ATOM   14214 C  CG2   . VAL   C 2 278 ? 90.753  98.107  90.550  1.00 71.45  ?  277  VAL   C CG2   1 
ATOM   14215 N  N     . GLN   C 2 279 ? 95.169  99.357  89.963  1.00 73.21  ?  278  GLN   C N     1 
ATOM   14216 C  CA    . GLN   C 2 279 ? 96.599  99.188  89.725  1.00 71.96  ?  278  GLN   C CA    1 
ATOM   14217 C  C     . GLN   C 2 279 ? 97.414  99.633  90.931  1.00 74.64  ?  278  GLN   C C     1 
ATOM   14218 O  O     . GLN   C 2 279 ? 98.415  98.997  91.282  1.00 79.97  ?  278  GLN   C O     1 
ATOM   14219 C  CB    . GLN   C 2 279 ? 97.019  99.963  88.477  1.00 73.79  ?  278  GLN   C CB    1 
ATOM   14220 C  CG    . GLN   C 2 279 ? 98.525  100.013 88.231  1.00 77.62  ?  278  GLN   C CG    1 
ATOM   14221 C  CD    . GLN   C 2 279 ? 98.854  100.008 86.754  1.00 86.35  ?  278  GLN   C CD    1 
ATOM   14222 O  OE1   . GLN   C 2 279 ? 99.439  99.056  86.236  1.00 87.34  ?  278  GLN   C OE1   1 
ATOM   14223 N  NE2   . GLN   C 2 279 ? 98.463  101.072 86.061  1.00 87.00  ?  278  GLN   C NE2   1 
ATOM   14224 N  N     . ALA   C 2 280 ? 97.006  100.727 91.578  1.00 70.64  ?  279  ALA   C N     1 
ATOM   14225 C  CA    . ALA   C 2 280 ? 97.705  101.164 92.784  1.00 68.92  ?  279  ALA   C CA    1 
ATOM   14226 C  C     . ALA   C 2 280 ? 97.588  100.127 93.896  1.00 69.88  ?  279  ALA   C C     1 
ATOM   14227 O  O     . ALA   C 2 280 ? 98.567  99.846  94.600  1.00 72.98  ?  279  ALA   C O     1 
ATOM   14228 C  CB    . ALA   C 2 280 ? 97.171  102.522 93.238  1.00 69.51  ?  279  ALA   C CB    1 
ATOM   14229 N  N     . ALA   C 2 281 ? 96.402  99.536  94.056  1.00 70.42  ?  280  ALA   C N     1 
ATOM   14230 C  CA    . ALA   C 2 281 ? 96.235  98.484  95.054  1.00 66.51  ?  280  ALA   C CA    1 
ATOM   14231 C  C     . ALA   C 2 281 ? 97.131  97.287  94.753  1.00 74.46  ?  280  ALA   C C     1 
ATOM   14232 O  O     . ALA   C 2 281 ? 97.748  96.720  95.663  1.00 80.37  ?  280  ALA   C O     1 
ATOM   14233 C  CB    . ALA   C 2 281 ? 94.770  98.059  95.122  1.00 66.00  ?  280  ALA   C CB    1 
ATOM   14234 N  N     . GLN   C 2 282 ? 97.216  96.889  93.481  1.00 72.71  ?  281  GLN   C N     1 
ATOM   14235 C  CA    . GLN   C 2 282 ? 98.084  95.770  93.113  1.00 67.32  ?  281  GLN   C CA    1 
ATOM   14236 C  C     . GLN   C 2 282 ? 99.551  96.092  93.376  1.00 68.66  ?  281  GLN   C C     1 
ATOM   14237 O  O     . GLN   C 2 282 ? 100.316 95.231  93.833  1.00 75.77  ?  281  GLN   C O     1 
ATOM   14238 C  CB    . GLN   C 2 282 ? 97.875  95.398  91.647  1.00 69.29  ?  281  GLN   C CB    1 
ATOM   14239 C  CG    . GLN   C 2 282 ? 98.149  93.934  91.328  1.00 70.61  ?  281  GLN   C CG    1 
ATOM   14240 C  CD    . GLN   C 2 282 ? 97.864  93.005  92.490  1.00 75.04  ?  281  GLN   C CD    1 
ATOM   14241 O  OE1   . GLN   C 2 282 ? 96.726  92.885  92.939  1.00 80.65  ?  281  GLN   C OE1   1 
ATOM   14242 N  NE2   . GLN   C 2 282 ? 98.901  92.335  92.978  1.00 69.91  ?  281  GLN   C NE2   1 
ATOM   14243 N  N     . GLN   C 2 283 ? 99.966  97.325  93.078  1.00 65.45  ?  282  GLN   C N     1 
ATOM   14244 C  CA    . GLN   C 2 283 ? 101.340 97.727  93.356  1.00 67.28  ?  282  GLN   C CA    1 
ATOM   14245 C  C     . GLN   C 2 283 ? 101.633 97.667  94.848  1.00 73.72  ?  282  GLN   C C     1 
ATOM   14246 O  O     . GLN   C 2 283 ? 102.728 97.266  95.260  1.00 79.71  ?  282  GLN   C O     1 
ATOM   14247 C  CB    . GLN   C 2 283 ? 101.597 99.132  92.814  1.00 70.37  ?  282  GLN   C CB    1 
ATOM   14248 C  CG    . GLN   C 2 283 ? 102.068 99.161  91.373  1.00 70.85  ?  282  GLN   C CG    1 
ATOM   14249 C  CD    . GLN   C 2 283 ? 101.897 100.522 90.735  1.00 74.57  ?  282  GLN   C CD    1 
ATOM   14250 O  OE1   . GLN   C 2 283 ? 102.019 101.550 91.399  1.00 79.53  ?  282  GLN   C OE1   1 
ATOM   14251 N  NE2   . GLN   C 2 283 ? 101.610 100.536 89.440  1.00 78.22  ?  282  GLN   C NE2   1 
ATOM   14252 N  N     . GLU   C 2 284 ? 100.664 98.059  95.676  1.00 73.57  ?  283  GLU   C N     1 
ATOM   14253 C  CA    . GLU   C 2 284 ? 100.851 97.941  97.119  1.00 68.92  ?  283  GLU   C CA    1 
ATOM   14254 C  C     . GLU   C 2 284 ? 100.929 96.487  97.557  1.00 72.78  ?  283  GLU   C C     1 
ATOM   14255 O  O     . GLU   C 2 284 ? 101.663 96.157  98.492  1.00 76.96  ?  283  GLU   C O     1 
ATOM   14256 C  CB    . GLU   C 2 284 ? 99.723  98.633  97.862  1.00 70.72  ?  283  GLU   C CB    1 
ATOM   14257 C  CG    . GLU   C 2 284 ? 99.888  100.107 97.997  1.00 78.23  ?  283  GLU   C CG    1 
ATOM   14258 C  CD    . GLU   C 2 284 ? 98.550  100.763 98.012  1.00 93.16  ?  283  GLU   C CD    1 
ATOM   14259 O  OE1   . GLU   C 2 284 ? 97.641  100.148 98.603  1.00 93.70  ?  283  GLU   C OE1   1 
ATOM   14260 O  OE2   . GLU   C 2 284 ? 98.395  101.851 97.422  1.00 94.06  ?  283  GLU   C OE2   1 
ATOM   14261 N  N     . LYS   C 2 285 ? 100.149 95.612  96.925  1.00 75.25  ?  284  LYS   C N     1 
ATOM   14262 C  CA    . LYS   C 2 285 ? 100.259 94.189  97.229  1.00 67.86  ?  284  LYS   C CA    1 
ATOM   14263 C  C     . LYS   C 2 285 ? 101.664 93.679  96.929  1.00 69.21  ?  284  LYS   C C     1 
ATOM   14264 O  O     . LYS   C 2 285 ? 102.249 92.922  97.717  1.00 76.17  ?  284  LYS   C O     1 
ATOM   14265 C  CB    . LYS   C 2 285 ? 99.228  93.400  96.424  1.00 72.98  ?  284  LYS   C CB    1 
ATOM   14266 C  CG    . LYS   C 2 285 ? 97.775  93.747  96.697  1.00 70.86  ?  284  LYS   C CG    1 
ATOM   14267 C  CD    . LYS   C 2 285 ? 97.224  92.986  97.881  1.00 68.51  ?  284  LYS   C CD    1 
ATOM   14268 C  CE    . LYS   C 2 285 ? 95.714  93.109  97.958  1.00 70.01  ?  284  LYS   C CE    1 
ATOM   14269 N  NZ    . LYS   C 2 285 ? 95.086  93.060  96.611  1.00 69.23  ?  284  LYS   C NZ    1 
ATOM   14270 N  N     . ASP   C 2 286 ? 102.221 94.094  95.790  1.00 69.58  ?  285  ASP   C N     1 
ATOM   14271 C  CA    . ASP   C 2 286 ? 103.587 93.710  95.446  1.00 68.44  ?  285  ASP   C CA    1 
ATOM   14272 C  C     . ASP   C 2 286 ? 104.593 94.272  96.444  1.00 71.33  ?  285  ASP   C C     1 
ATOM   14273 O  O     . ASP   C 2 286 ? 105.548 93.585  96.826  1.00 74.38  ?  285  ASP   C O     1 
ATOM   14274 C  CB    . ASP   C 2 286 ? 103.922 94.167  94.029  1.00 73.57  ?  285  ASP   C CB    1 
ATOM   14275 C  CG    . ASP   C 2 286 ? 102.918 93.681  93.008  1.00 85.25  ?  285  ASP   C CG    1 
ATOM   14276 O  OD1   . ASP   C 2 286 ? 102.417 92.550  93.159  1.00 88.12  ?  285  ASP   C OD1   1 
ATOM   14277 O  OD2   . ASP   C 2 286 ? 102.636 94.431  92.048  1.00 85.79  ?  285  ASP   C OD2   1 
ATOM   14278 N  N     . TRP   C 2 287 ? 104.391 95.519  96.880  1.00 59.54  ?  286  TRP   C N     1 
ATOM   14279 C  CA    . TRP   C 2 287 ? 105.267 96.114  97.886  1.00 55.53  ?  286  TRP   C CA    1 
ATOM   14280 C  C     . TRP   C 2 287 ? 105.192 95.353  99.203  1.00 59.55  ?  286  TRP   C C     1 
ATOM   14281 O  O     . TRP   C 2 287 ? 106.213 95.149  99.868  1.00 65.55  ?  286  TRP   C O     1 
ATOM   14282 C  CB    . TRP   C 2 287 ? 104.901 97.583  98.089  1.00 56.10  ?  286  TRP   C CB    1 
ATOM   14283 C  CG    . TRP   C 2 287 ? 105.750 98.287  99.101  1.00 53.83  ?  286  TRP   C CG    1 
ATOM   14284 C  CD1   . TRP   C 2 287 ? 105.398 98.622  100.374 1.00 55.06  ?  286  TRP   C CD1   1 
ATOM   14285 C  CD2   . TRP   C 2 287 ? 107.092 98.754  98.921  1.00 55.34  ?  286  TRP   C CD2   1 
ATOM   14286 N  NE1   . TRP   C 2 287 ? 106.437 99.263  101.000 1.00 59.10  ?  286  TRP   C NE1   1 
ATOM   14287 C  CE2   . TRP   C 2 287 ? 107.490 99.357  100.129 1.00 58.80  ?  286  TRP   C CE2   1 
ATOM   14288 C  CE3   . TRP   C 2 287 ? 107.997 98.718  97.857  1.00 53.17  ?  286  TRP   C CE3   1 
ATOM   14289 C  CZ2   . TRP   C 2 287 ? 108.752 99.919  100.302 1.00 56.42  ?  286  TRP   C CZ2   1 
ATOM   14290 C  CZ3   . TRP   C 2 287 ? 109.248 99.276  98.031  1.00 56.17  ?  286  TRP   C CZ3   1 
ATOM   14291 C  CH2   . TRP   C 2 287 ? 109.614 99.869  99.244  1.00 55.55  ?  286  TRP   C CH2   1 
ATOM   14292 N  N     . ALA   C 2 288 ? 103.988 94.937  99.600  1.00 65.42  ?  287  ALA   C N     1 
ATOM   14293 C  CA    . ALA   C 2 288 ? 103.827 94.149  100.816 1.00 59.88  ?  287  ALA   C CA    1 
ATOM   14294 C  C     . ALA   C 2 288 ? 104.543 92.814  100.698 1.00 66.08  ?  287  ALA   C C     1 
ATOM   14295 O  O     . ALA   C 2 288 ? 105.167 92.346  101.658 1.00 74.05  ?  287  ALA   C O     1 
ATOM   14296 C  CB    . ALA   C 2 288 ? 102.343 93.940  101.116 1.00 62.07  ?  287  ALA   C CB    1 
ATOM   14297 N  N     . ASP   C 2 289 ? 104.519 92.198  99.517  1.00 74.69  ?  288  ASP   C N     1 
ATOM   14298 C  CA    . ASP   C 2 289 ? 105.229 90.910  99.299  1.00 71.63  ?  288  ASP   C CA    1 
ATOM   14299 C  C     . ASP   C 2 289 ? 106.731 91.158  99.396  1.00 73.30  ?  288  ASP   C C     1 
ATOM   14300 O  O     . ASP   C 2 289 ? 107.434 90.329  99.985  1.00 77.84  ?  288  ASP   C O     1 
ATOM   14301 C  CB    . ASP   C 2 289 ? 104.921 90.281  97.942  1.00 77.00  ?  288  ASP   C CB    1 
ATOM   14302 C  CG    . ASP   C 2 289 ? 105.340 88.828  97.817  1.00 85.81  ?  288  ASP   C CG    1 
ATOM   14303 O  OD1   . ASP   C 2 289 ? 105.817 88.264  98.819  1.00 88.52  ?  288  ASP   C OD1   1 
ATOM   14304 O  OD2   . ASP   C 2 289 ? 105.190 88.275  96.712  1.00 84.38  ?  288  ASP   C OD2   1 
ATOM   14305 N  N     . TYR   C 2 290 ? 107.190 92.278  98.851  1.00 63.84  ?  289  TYR   C N     1 
ATOM   14306 C  CA    . TYR   C 2 290 ? 108.614 92.594  98.918  1.00 60.00  ?  289  TYR   C CA    1 
ATOM   14307 C  C     . TYR   C 2 290 ? 109.065 92.889  100.343 1.00 61.86  ?  289  TYR   C C     1 
ATOM   14308 O  O     . TYR   C 2 290 ? 110.203 92.577  100.704 1.00 66.05  ?  289  TYR   C O     1 
ATOM   14309 C  CB    . TYR   C 2 290 ? 108.925 93.778  98.005  1.00 66.23  ?  289  TYR   C CB    1 
ATOM   14310 C  CG    . TYR   C 2 290 ? 110.258 94.436  98.275  1.00 62.53  ?  289  TYR   C CG    1 
ATOM   14311 C  CD1   . TYR   C 2 290 ? 111.447 93.777  98.003  1.00 64.06  ?  289  TYR   C CD1   1 
ATOM   14312 C  CD2   . TYR   C 2 290 ? 110.327 95.721  98.793  1.00 62.88  ?  289  TYR   C CD2   1 
ATOM   14313 C  CE1   . TYR   C 2 290 ? 112.668 94.379  98.242  1.00 62.29  ?  289  TYR   C CE1   1 
ATOM   14314 C  CE2   . TYR   C 2 290 ? 111.543 96.329  99.036  1.00 60.79  ?  289  TYR   C CE2   1 
ATOM   14315 C  CZ    . TYR   C 2 290 ? 112.710 95.653  98.760  1.00 63.97  ?  289  TYR   C CZ    1 
ATOM   14316 O  OH    . TYR   C 2 290 ? 113.923 96.254  99.001  1.00 66.72  ?  289  TYR   C OH    1 
ATOM   14317 N  N     . LEU   C 2 291 ? 108.202 93.495  101.159 1.00 65.41  ?  290  LEU   C N     1 
ATOM   14318 C  CA    . LEU   C 2 291 ? 108.584 93.832  102.527 1.00 58.96  ?  290  LEU   C CA    1 
ATOM   14319 C  C     . LEU   C 2 291 ? 108.789 92.579  103.369 1.00 63.50  ?  290  LEU   C C     1 
ATOM   14320 O  O     . LEU   C 2 291 ? 109.828 92.419  104.017 1.00 69.55  ?  290  LEU   C O     1 
ATOM   14321 C  CB    . LEU   C 2 291 ? 107.529 94.736  103.157 1.00 59.03  ?  290  LEU   C CB    1 
ATOM   14322 C  CG    . LEU   C 2 291 ? 107.505 96.206  102.752 1.00 61.09  ?  290  LEU   C CG    1 
ATOM   14323 C  CD1   . LEU   C 2 291 ? 106.381 96.932  103.469 1.00 58.28  ?  290  LEU   C CD1   1 
ATOM   14324 C  CD2   . LEU   C 2 291 ? 108.842 96.861  103.040 1.00 57.81  ?  290  LEU   C CD2   1 
ATOM   14325 N  N     . PHE   C 2 292 ? 107.828 91.664  103.340 1.00 71.47  ?  291  PHE   C N     1 
ATOM   14326 C  CA    . PHE   C 2 292 ? 107.892 90.439  104.133 1.00 69.93  ?  291  PHE   C CA    1 
ATOM   14327 C  C     . PHE   C 2 292 ? 108.388 89.265  103.289 1.00 73.34  ?  291  PHE   C C     1 
ATOM   14328 O  O     . PHE   C 2 292 ? 107.682 88.286  103.054 1.00 82.18  ?  291  PHE   C O     1 
ATOM   14329 C  CB    . PHE   C 2 292 ? 106.529 90.147  104.746 1.00 65.54  ?  291  PHE   C CB    1 
ATOM   14330 C  CG    . PHE   C 2 292 ? 105.905 91.330  105.423 1.00 68.39  ?  291  PHE   C CG    1 
ATOM   14331 C  CD1   . PHE   C 2 292 ? 106.162 91.595  106.754 1.00 72.31  ?  291  PHE   C CD1   1 
ATOM   14332 C  CD2   . PHE   C 2 292 ? 104.998 92.128  104.753 1.00 66.10  ?  291  PHE   C CD2   1 
ATOM   14333 C  CE1   . PHE   C 2 292 ? 105.584 92.678  107.381 1.00 71.03  ?  291  PHE   C CE1   1 
ATOM   14334 C  CE2   . PHE   C 2 292 ? 104.418 93.212  105.372 1.00 70.82  ?  291  PHE   C CE2   1 
ATOM   14335 C  CZ    . PHE   C 2 292 ? 104.707 93.485  106.690 1.00 72.30  ?  291  PHE   C CZ    1 
ATOM   14336 N  N     . ARG   C 2 293 ? 109.633 89.376  102.831 1.00 79.87  ?  292  ARG   C N     1 
ATOM   14337 C  CA    . ARG   C 2 293 ? 110.280 88.286  102.109 1.00 81.53  ?  292  ARG   C CA    1 
ATOM   14338 C  C     . ARG   C 2 293 ? 111.233 87.487  102.985 1.00 86.32  ?  292  ARG   C C     1 
ATOM   14339 O  O     . ARG   C 2 293 ? 111.227 86.254  102.930 1.00 89.56  ?  292  ARG   C O     1 
ATOM   14340 C  CB    . ARG   C 2 293 ? 111.033 88.819  100.884 1.00 80.87  ?  292  ARG   C CB    1 
ATOM   14341 C  CG    . ARG   C 2 293 ? 111.946 89.983  101.172 1.00 83.30  ?  292  ARG   C CG    1 
ATOM   14342 C  CD    . ARG   C 2 293 ? 113.096 90.071  100.183 1.00 83.13  ?  292  ARG   C CD    1 
ATOM   14343 N  NE    . ARG   C 2 293 ? 114.117 91.026  100.597 1.00 87.89  ?  292  ARG   C NE    1 
ATOM   14344 C  CZ    . ARG   C 2 293 ? 114.868 91.731  99.762  1.00 89.50  ?  292  ARG   C CZ    1 
ATOM   14345 N  NH1   . ARG   C 2 293 ? 114.717 91.641  98.450  1.00 85.84  ?  292  ARG   C NH1   1 
ATOM   14346 N  NH2   . ARG   C 2 293 ? 115.790 92.550  100.257 1.00 84.71  ?  292  ARG   C NH2   1 
ATOM   14347 N  N     . ASP   C 2 294 ? 112.050 88.161  103.799 1.00 98.68  ?  293  ASP   C N     1 
ATOM   14348 C  CA    . ASP   C 2 294 ? 112.935 87.475  104.730 1.00 97.44  ?  293  ASP   C CA    1 
ATOM   14349 C  C     . ASP   C 2 294 ? 112.212 87.010  105.984 1.00 99.58  ?  293  ASP   C C     1 
ATOM   14350 O  O     . ASP   C 2 294 ? 112.719 86.124  106.681 1.00 105.43 ?  293  ASP   C O     1 
ATOM   14351 C  CB    . ASP   C 2 294 ? 114.104 88.381  105.118 1.00 99.66  ?  293  ASP   C CB    1 
ATOM   14352 C  CG    . ASP   C 2 294 ? 114.842 88.924  103.914 1.00 105.03 ?  293  ASP   C CG    1 
ATOM   14353 O  OD1   . ASP   C 2 294 ? 115.536 88.137  103.237 1.00 104.31 ?  293  ASP   C OD1   1 
ATOM   14354 O  OD2   . ASP   C 2 294 ? 114.727 90.137  103.644 1.00 105.25 ?  293  ASP   C OD2   1 
ATOM   14355 N  N     . GLY   C 2 295 ? 111.037 87.549  106.262 1.00 87.94  ?  294  GLY   C N     1 
ATOM   14356 C  CA    . GLY   C 2 295 ? 110.306 87.183  107.455 1.00 89.54  ?  294  GLY   C CA    1 
ATOM   14357 C  C     . GLY   C 2 295 ? 109.223 88.196  107.749 1.00 91.48  ?  294  GLY   C C     1 
ATOM   14358 O  O     . GLY   C 2 295 ? 109.085 89.212  107.070 1.00 93.90  ?  294  GLY   C O     1 
ATOM   14359 N  N     . SER   C 2 296 ? 108.458 87.897  108.791 1.00 87.96  ?  295  SER   C N     1 
ATOM   14360 C  CA    . SER   C 2 296 ? 107.329 88.716  109.206 1.00 86.66  ?  295  SER   C CA    1 
ATOM   14361 C  C     . SER   C 2 296 ? 107.583 89.262  110.606 1.00 90.34  ?  295  SER   C C     1 
ATOM   14362 O  O     . SER   C 2 296 ? 108.627 89.023  111.214 1.00 95.30  ?  295  SER   C O     1 
ATOM   14363 C  CB    . SER   C 2 296 ? 106.022 87.921  109.158 1.00 88.85  ?  295  SER   C CB    1 
ATOM   14364 O  OG    . SER   C 2 296 ? 105.657 87.466  110.450 1.00 91.52  ?  295  SER   C OG    1 
ATOM   14365 N  N     . MET   C 2 297 ? 106.611 90.017  111.103 1.00 87.98  ?  296  MET   C N     1 
ATOM   14366 C  CA    . MET   C 2 297 ? 106.697 90.682  112.393 1.00 85.64  ?  296  MET   C CA    1 
ATOM   14367 C  C     . MET   C 2 297 ? 105.397 90.451  113.148 1.00 89.47  ?  296  MET   C C     1 
ATOM   14368 O  O     . MET   C 2 297 ? 104.345 90.231  112.542 1.00 93.58  ?  296  MET   C O     1 
ATOM   14369 C  CB    . MET   C 2 297 ? 106.968 92.187  112.215 1.00 84.77  ?  296  MET   C CB    1 
ATOM   14370 C  CG    . MET   C 2 297 ? 106.985 93.007  113.494 1.00 87.51  ?  296  MET   C CG    1 
ATOM   14371 S  SD    . MET   C 2 297 ? 107.364 94.750  113.215 1.00 99.88  ?  296  MET   C SD    1 
ATOM   14372 C  CE    . MET   C 2 297 ? 105.843 95.328  112.468 1.00 90.69  ?  296  MET   C CE    1 
ATOM   14373 N  N     . ILE   C 2 298 ? 105.480 90.471  114.480 1.00 77.80  ?  297  ILE   C N     1 
ATOM   14374 C  CA    . ILE   C 2 298 ? 104.283 90.296  115.289 1.00 76.24  ?  297  ILE   C CA    1 
ATOM   14375 C  C     . ILE   C 2 298 ? 103.342 91.466  115.046 1.00 76.84  ?  297  ILE   C C     1 
ATOM   14376 O  O     . ILE   C 2 298 ? 103.724 92.635  115.183 1.00 78.90  ?  297  ILE   C O     1 
ATOM   14377 C  CB    . ILE   C 2 298 ? 104.653 90.161  116.775 1.00 72.40  ?  297  ILE   C CB    1 
ATOM   14378 C  CG1   . ILE   C 2 298 ? 105.001 88.710  117.107 1.00 76.57  ?  297  ILE   C CG1   1 
ATOM   14379 C  CG2   . ILE   C 2 298 ? 103.527 90.659  117.671 1.00 71.75  ?  297  ILE   C CG2   1 
ATOM   14380 C  CD1   . ILE   C 2 298 ? 105.113 88.435  118.584 1.00 81.02  ?  297  ILE   C CD1   1 
ATOM   14381 N  N     . GLY   C 2 299 ? 102.099 91.152  114.692 1.00 75.37  ?  298  GLY   C N     1 
ATOM   14382 C  CA    . GLY   C 2 299 ? 101.095 92.158  114.430 1.00 68.23  ?  298  GLY   C CA    1 
ATOM   14383 C  C     . GLY   C 2 299 ? 101.008 92.630  112.995 1.00 73.98  ?  298  GLY   C C     1 
ATOM   14384 O  O     . GLY   C 2 299 ? 100.092 93.396  112.670 1.00 83.25  ?  298  GLY   C O     1 
ATOM   14385 N  N     . LEU   C 2 300 ? 101.920 92.201  112.124 1.00 69.76  ?  299  LEU   C N     1 
ATOM   14386 C  CA    . LEU   C 2 300 ? 101.908 92.661  110.737 1.00 67.21  ?  299  LEU   C CA    1 
ATOM   14387 C  C     . LEU   C 2 300 ? 102.672 91.675  109.870 1.00 66.52  ?  299  LEU   C C     1 
ATOM   14388 O  O     . LEU   C 2 300 ? 103.865 91.450  110.096 1.00 74.20  ?  299  LEU   C O     1 
ATOM   14389 C  CB    . LEU   C 2 300 ? 102.517 94.058  110.623 1.00 68.46  ?  299  LEU   C CB    1 
ATOM   14390 C  CG    . LEU   C 2 300 ? 102.233 94.801  109.318 1.00 70.50  ?  299  LEU   C CG    1 
ATOM   14391 C  CD1   . LEU   C 2 300 ? 100.795 95.292  109.285 1.00 71.86  ?  299  LEU   C CD1   1 
ATOM   14392 C  CD2   . LEU   C 2 300 ? 103.202 95.954  109.138 1.00 67.55  ?  299  LEU   C CD2   1 
ATOM   14393 N  N     . ASN   C 2 301 ? 101.996 91.102  108.878 1.00 70.41  ?  300  ASN   C N     1 
ATOM   14394 C  CA    . ASN   C 2 301 ? 102.631 90.234  107.894 1.00 67.51  ?  300  ASN   C CA    1 
ATOM   14395 C  C     . ASN   C 2 301 ? 102.043 90.563  106.526 1.00 75.64  ?  300  ASN   C C     1 
ATOM   14396 O  O     . ASN   C 2 301 ? 101.367 91.581  106.349 1.00 78.66  ?  300  ASN   C O     1 
ATOM   14397 C  CB    . ASN   C 2 301 ? 102.463 88.756  108.272 1.00 65.28  ?  300  ASN   C CB    1 
ATOM   14398 C  CG    . ASN   C 2 301 ? 101.014 88.362  108.490 1.00 76.19  ?  300  ASN   C CG    1 
ATOM   14399 O  OD1   . ASN   C 2 301 ? 100.093 89.077  108.100 1.00 85.46  ?  300  ASN   C OD1   1 
ATOM   14400 N  ND2   . ASN   C 2 301 ? 100.807 87.211  109.114 1.00 78.26  ?  300  ASN   C ND2   1 
ATOM   14401 N  N     . LYS   C 2 302 ? 102.313 89.695  105.547 1.00 77.75  ?  301  LYS   C N     1 
ATOM   14402 C  CA    . LYS   C 2 302 ? 101.846 89.938  104.185 1.00 71.81  ?  301  LYS   C CA    1 
ATOM   14403 C  C     . LYS   C 2 302 ? 100.326 89.921  104.108 1.00 74.16  ?  301  LYS   C C     1 
ATOM   14404 O  O     . LYS   C 2 302 ? 99.715  90.804  103.497 1.00 83.47  ?  301  LYS   C O     1 
ATOM   14405 C  CB    . LYS   C 2 302 ? 102.438 88.901  103.232 1.00 74.96  ?  301  LYS   C CB    1 
ATOM   14406 C  CG    . LYS   C 2 302 ? 102.780 89.459  101.862 1.00 79.55  ?  301  LYS   C CG    1 
ATOM   14407 C  CD    . LYS   C 2 302 ? 103.077 88.337  100.876 1.00 81.93  ?  301  LYS   C CD    1 
ATOM   14408 C  CE    . LYS   C 2 302 ? 101.926 87.346  100.783 1.00 82.46  ?  301  LYS   C CE    1 
ATOM   14409 N  NZ    . LYS   C 2 302 ? 100.601 88.021  100.689 1.00 85.10  ?  301  LYS   C NZ    1 
ATOM   14410 N  N     . ASP   C 2 303 ? 99.696  88.914  104.720 1.00 76.71  ?  302  ASP   C N     1 
ATOM   14411 C  CA    . ASP   C 2 303 ? 98.244  88.783  104.627 1.00 78.74  ?  302  ASP   C CA    1 
ATOM   14412 C  C     . ASP   C 2 303 ? 97.536  89.960  105.284 1.00 79.41  ?  302  ASP   C C     1 
ATOM   14413 O  O     . ASP   C 2 303 ? 96.581  90.514  104.725 1.00 85.56  ?  302  ASP   C O     1 
ATOM   14414 C  CB    . ASP   C 2 303 ? 97.798  87.466  105.262 1.00 82.11  ?  302  ASP   C CB    1 
ATOM   14415 C  CG    . ASP   C 2 303 ? 98.191  86.259  104.435 1.00 91.04  ?  302  ASP   C CG    1 
ATOM   14416 O  OD1   . ASP   C 2 303 ? 98.549  86.437  103.252 1.00 92.27  ?  302  ASP   C OD1   1 
ATOM   14417 O  OD2   . ASP   C 2 303 ? 98.142  85.130  104.967 1.00 94.41  ?  302  ASP   C OD2   1 
ATOM   14418 N  N     . ILE   C 2 304 ? 97.997  90.360  106.470 1.00 70.83  ?  303  ILE   C N     1 
ATOM   14419 C  CA    . ILE   C 2 304 ? 97.372  91.469  107.184 1.00 73.40  ?  303  ILE   C CA    1 
ATOM   14420 C  C     . ILE   C 2 304 ? 97.529  92.768  106.404 1.00 78.01  ?  303  ILE   C C     1 
ATOM   14421 O  O     . ILE   C 2 304 ? 96.577  93.547  106.273 1.00 81.49  ?  303  ILE   C O     1 
ATOM   14422 C  CB    . ILE   C 2 304 ? 97.958  91.584  108.602 1.00 69.85  ?  303  ILE   C CB    1 
ATOM   14423 C  CG1   . ILE   C 2 304 ? 97.466  90.435  109.481 1.00 71.08  ?  303  ILE   C CG1   1 
ATOM   14424 C  CG2   . ILE   C 2 304 ? 97.595  92.920  109.222 1.00 71.43  ?  303  ILE   C CG2   1 
ATOM   14425 C  CD1   . ILE   C 2 304 ? 97.949  90.522  110.909 1.00 74.40  ?  303  ILE   C CD1   1 
ATOM   14426 N  N     . LEU   C 2 305 ? 98.722  93.016  105.864 1.00 69.72  ?  304  LEU   C N     1 
ATOM   14427 C  CA    . LEU   C 2 305 ? 98.945  94.249  105.121 1.00 65.25  ?  304  LEU   C CA    1 
ATOM   14428 C  C     . LEU   C 2 305 ? 98.147  94.269  103.824 1.00 69.70  ?  304  LEU   C C     1 
ATOM   14429 O  O     . LEU   C 2 305 ? 97.658  95.325  103.415 1.00 73.43  ?  304  LEU   C O     1 
ATOM   14430 C  CB    . LEU   C 2 305 ? 100.434 94.442  104.852 1.00 61.73  ?  304  LEU   C CB    1 
ATOM   14431 C  CG    . LEU   C 2 305 ? 100.844 95.884  104.551 1.00 61.53  ?  304  LEU   C CG    1 
ATOM   14432 C  CD1   . LEU   C 2 305 ? 100.594 96.768  105.758 1.00 61.28  ?  304  LEU   C CD1   1 
ATOM   14433 C  CD2   . LEU   C 2 305 ? 102.299 95.957  104.125 1.00 64.45  ?  304  LEU   C CD2   1 
ATOM   14434 N  N     . CYS   C 2 306 ? 97.990  93.115  103.169 1.00 77.02  ?  305  CYS   C N     1 
ATOM   14435 C  CA    . CYS   C 2 306 ? 97.164  93.059  101.966 1.00 73.36  ?  305  CYS   C CA    1 
ATOM   14436 C  C     . CYS   C 2 306 ? 95.695  93.308  102.290 1.00 76.06  ?  305  CYS   C C     1 
ATOM   14437 O  O     . CYS   C 2 306 ? 94.994  94.011  101.546 1.00 83.85  ?  305  CYS   C O     1 
ATOM   14438 C  CB    . CYS   C 2 306 ? 97.350  91.710  101.271 1.00 76.86  ?  305  CYS   C CB    1 
ATOM   14439 S  SG    . CYS   C 2 306 ? 98.984  91.480  100.530 1.00 99.56  ?  305  CYS   C SG    1 
ATOM   14440 N  N     . GLN   C 2 307 ? 95.214  92.741  103.400 1.00 65.04  ?  306  GLN   C N     1 
ATOM   14441 C  CA    . GLN   C 2 307 ? 93.849  93.011  103.839 1.00 64.42  ?  306  GLN   C CA    1 
ATOM   14442 C  C     . GLN   C 2 307 ? 93.652  94.492  104.125 1.00 71.57  ?  306  GLN   C C     1 
ATOM   14443 O  O     . GLN   C 2 307 ? 92.625  95.076  103.755 1.00 77.24  ?  306  GLN   C O     1 
ATOM   14444 C  CB    . GLN   C 2 307 ? 93.526  92.181  105.080 1.00 66.71  ?  306  GLN   C CB    1 
ATOM   14445 C  CG    . GLN   C 2 307 ? 93.004  90.792  104.778 1.00 75.66  ?  306  GLN   C CG    1 
ATOM   14446 C  CD    . GLN   C 2 307 ? 92.583  90.055  106.033 1.00 76.32  ?  306  GLN   C CD    1 
ATOM   14447 O  OE1   . GLN   C 2 307 ? 91.395  89.904  106.308 1.00 79.22  ?  306  GLN   C OE1   1 
ATOM   14448 N  NE2   . GLN   C 2 307 ? 93.559  89.605  106.811 1.00 71.92  ?  306  GLN   C NE2   1 
ATOM   14449 N  N     . TYR   C 2 308 ? 94.629  95.117  104.785 1.00 61.48  ?  307  TYR   C N     1 
ATOM   14450 C  CA    . TYR   C 2 308 ? 94.538  96.548  105.051 1.00 58.98  ?  307  TYR   C CA    1 
ATOM   14451 C  C     . TYR   C 2 308 ? 94.569  97.351  103.759 1.00 63.11  ?  307  TYR   C C     1 
ATOM   14452 O  O     . TYR   C 2 308 ? 93.889  98.375  103.643 1.00 70.46  ?  307  TYR   C O     1 
ATOM   14453 C  CB    . TYR   C 2 308 ? 95.665  96.991  105.981 1.00 56.41  ?  307  TYR   C CB    1 
ATOM   14454 C  CG    . TYR   C 2 308 ? 95.647  98.475  106.257 1.00 61.84  ?  307  TYR   C CG    1 
ATOM   14455 C  CD1   . TYR   C 2 308 ? 94.607  99.053  106.969 1.00 62.81  ?  307  TYR   C CD1   1 
ATOM   14456 C  CD2   . TYR   C 2 308 ? 96.659  99.301  105.791 1.00 60.03  ?  307  TYR   C CD2   1 
ATOM   14457 C  CE1   . TYR   C 2 308 ? 94.580  100.408 107.220 1.00 59.28  ?  307  TYR   C CE1   1 
ATOM   14458 C  CE2   . TYR   C 2 308 ? 96.639  100.659 106.036 1.00 63.93  ?  307  TYR   C CE2   1 
ATOM   14459 C  CZ    . TYR   C 2 308 ? 95.597  101.206 106.753 1.00 65.71  ?  307  TYR   C CZ    1 
ATOM   14460 O  OH    . TYR   C 2 308 ? 95.572  102.559 107.000 1.00 69.76  ?  307  TYR   C OH    1 
ATOM   14461 N  N     . VAL   C 2 309 ? 95.364  96.909  102.782 1.00 61.72  ?  308  VAL   C N     1 
ATOM   14462 C  CA    . VAL   C 2 309 ? 95.402  97.576  101.484 1.00 58.43  ?  308  VAL   C CA    1 
ATOM   14463 C  C     . VAL   C 2 309 ? 94.020  97.568  100.851 1.00 61.38  ?  308  VAL   C C     1 
ATOM   14464 O  O     . VAL   C 2 309 ? 93.521  98.601  100.391 1.00 66.22  ?  308  VAL   C O     1 
ATOM   14465 C  CB    . VAL   C 2 309 ? 96.439  96.905  100.564 1.00 60.04  ?  308  VAL   C CB    1 
ATOM   14466 C  CG1   . VAL   C 2 309 ? 96.134  97.207  99.103  1.00 59.89  ?  308  VAL   C CG1   1 
ATOM   14467 C  CG2   . VAL   C 2 309 ? 97.842  97.351  100.918 1.00 64.77  ?  308  VAL   C CG2   1 
ATOM   14468 N  N     . GLU   C 2 310 ? 93.376  96.400  100.833 1.00 71.96  ?  309  GLU   C N     1 
ATOM   14469 C  CA    . GLU   C 2 310 ? 92.041  96.309  100.247 1.00 64.05  ?  309  GLU   C CA    1 
ATOM   14470 C  C     . GLU   C 2 310 ? 91.042  97.174  101.008 1.00 66.30  ?  309  GLU   C C     1 
ATOM   14471 O  O     . GLU   C 2 310 ? 90.229  97.885  100.399 1.00 74.15  ?  309  GLU   C O     1 
ATOM   14472 C  CB    . GLU   C 2 310 ? 91.578  94.854  100.217 1.00 65.67  ?  309  GLU   C CB    1 
ATOM   14473 C  CG    . GLU   C 2 310 ? 92.455  93.953  99.373  1.00 71.44  ?  309  GLU   C CG    1 
ATOM   14474 C  CD    . GLU   C 2 310 ? 91.771  92.654  99.002  1.00 80.47  ?  309  GLU   C CD    1 
ATOM   14475 O  OE1   . GLU   C 2 310 ? 90.924  92.182  99.788  1.00 83.88  ?  309  GLU   C OE1   1 
ATOM   14476 O  OE2   . GLU   C 2 310 ? 92.081  92.106  97.924  1.00 77.84  ?  309  GLU   C OE2   1 
ATOM   14477 N  N     . TYR   C 2 311 ? 91.100  97.141  102.342 1.00 57.45  ?  310  TYR   C N     1 
ATOM   14478 C  CA    . TYR   C 2 311 ? 90.158  97.914  103.145 1.00 61.95  ?  310  TYR   C CA    1 
ATOM   14479 C  C     . TYR   C 2 311 ? 90.313  99.410  102.894 1.00 67.99  ?  310  TYR   C C     1 
ATOM   14480 O  O     . TYR   C 2 311 ? 89.326  100.121 102.667 1.00 67.86  ?  310  TYR   C O     1 
ATOM   14481 C  CB    . TYR   C 2 311 ? 90.352  97.596  104.628 1.00 61.88  ?  310  TYR   C CB    1 
ATOM   14482 C  CG    . TYR   C 2 311 ? 89.770  98.647  105.541 1.00 66.74  ?  310  TYR   C CG    1 
ATOM   14483 C  CD1   . TYR   C 2 311 ? 88.430  98.618  105.890 1.00 65.74  ?  310  TYR   C CD1   1 
ATOM   14484 C  CD2   . TYR   C 2 311 ? 90.559  99.671  106.049 1.00 66.43  ?  310  TYR   C CD2   1 
ATOM   14485 C  CE1   . TYR   C 2 311 ? 87.891  99.576  106.715 1.00 67.62  ?  310  TYR   C CE1   1 
ATOM   14486 C  CE2   . TYR   C 2 311 ? 90.027  100.634 106.872 1.00 63.18  ?  310  TYR   C CE2   1 
ATOM   14487 C  CZ    . TYR   C 2 311 ? 88.694  100.580 107.202 1.00 67.42  ?  310  TYR   C CZ    1 
ATOM   14488 O  OH    . TYR   C 2 311 ? 88.158  101.536 108.022 1.00 77.82  ?  310  TYR   C OH    1 
ATOM   14489 N  N     . ILE   C 2 312 ? 91.551  99.910  102.939 1.00 61.91  ?  311  ILE   C N     1 
ATOM   14490 C  CA    . ILE   C 2 312 ? 91.774  101.339 102.761 1.00 55.73  ?  311  ILE   C CA    1 
ATOM   14491 C  C     . ILE   C 2 312 ? 91.482  101.758 101.327 1.00 62.02  ?  311  ILE   C C     1 
ATOM   14492 O  O     . ILE   C 2 312 ? 91.001  102.872 101.090 1.00 72.21  ?  311  ILE   C O     1 
ATOM   14493 C  CB    . ILE   C 2 312 ? 93.198  101.727 103.203 1.00 53.07  ?  311  ILE   C CB    1 
ATOM   14494 C  CG1   . ILE   C 2 312 ? 93.333  103.247 103.309 1.00 61.88  ?  311  ILE   C CG1   1 
ATOM   14495 C  CG2   . ILE   C 2 312 ? 94.241  101.167 102.255 1.00 61.79  ?  311  ILE   C CG2   1 
ATOM   14496 C  CD1   . ILE   C 2 312 ? 92.529  103.850 104.440 1.00 64.01  ?  311  ILE   C CD1   1 
ATOM   14497 N  N     . THR   C 2 313 ? 91.733  100.879 100.350 1.00 64.51  ?  312  THR   C N     1 
ATOM   14498 C  CA    . THR   C 2 313 ? 91.365  101.191 98.975  1.00 54.88  ?  312  THR   C CA    1 
ATOM   14499 C  C     . THR   C 2 313 ? 89.859  101.355 98.840  1.00 59.59  ?  312  THR   C C     1 
ATOM   14500 O  O     . THR   C 2 313 ? 89.387  102.308 98.211  1.00 68.02  ?  312  THR   C O     1 
ATOM   14501 C  CB    . THR   C 2 313 ? 91.873  100.100 98.032  1.00 57.53  ?  312  THR   C CB    1 
ATOM   14502 O  OG1   . THR   C 2 313 ? 93.251  99.828  98.313  1.00 74.22  ?  312  THR   C OG1   1 
ATOM   14503 C  CG2   . THR   C 2 313 ? 91.736  100.543 96.585  1.00 59.54  ?  312  THR   C CG2   1 
ATOM   14504 N  N     . ASN   C 2 314 ? 89.087  100.446 99.443  1.00 67.81  ?  313  ASN   C N     1 
ATOM   14505 C  CA    . ASN   C 2 314 ? 87.634  100.586 99.418  1.00 60.94  ?  313  ASN   C CA    1 
ATOM   14506 C  C     . ASN   C 2 314 ? 87.194  101.878 100.096 1.00 66.08  ?  313  ASN   C C     1 
ATOM   14507 O  O     . ASN   C 2 314 ? 86.353  102.618 99.566  1.00 74.38  ?  313  ASN   C O     1 
ATOM   14508 C  CB    . ASN   C 2 314 ? 86.981  99.380  100.094 1.00 62.80  ?  313  ASN   C CB    1 
ATOM   14509 C  CG    . ASN   C 2 314 ? 86.786  98.215  99.147  1.00 75.09  ?  313  ASN   C CG    1 
ATOM   14510 O  OD1   . ASN   C 2 314 ? 87.347  98.188  98.054  1.00 79.35  ?  313  ASN   C OD1   1 
ATOM   14511 N  ND2   . ASN   C 2 314 ? 85.985  97.243  99.564  1.00 78.05  ?  313  ASN   C ND2   1 
ATOM   14512 N  N     . ILE   C 2 315 ? 87.777  102.175 101.260 1.00 66.88  ?  314  ILE   C N     1 
ATOM   14513 C  CA    . ILE   C 2 315 ? 87.365  103.343 102.034 1.00 65.44  ?  314  ILE   C CA    1 
ATOM   14514 C  C     . ILE   C 2 315 ? 87.639  104.628 101.264 1.00 59.97  ?  314  ILE   C C     1 
ATOM   14515 O  O     . ILE   C 2 315 ? 86.776  105.510 101.179 1.00 62.39  ?  314  ILE   C O     1 
ATOM   14516 C  CB    . ILE   C 2 315 ? 88.063  103.344 103.406 1.00 66.41  ?  314  ILE   C CB    1 
ATOM   14517 C  CG1   . ILE   C 2 315 ? 87.280  102.494 104.408 1.00 68.58  ?  314  ILE   C CG1   1 
ATOM   14518 C  CG2   . ILE   C 2 315 ? 88.241  104.771 103.917 1.00 61.76  ?  314  ILE   C CG2   1 
ATOM   14519 C  CD1   . ILE   C 2 315 ? 85.851  102.936 104.603 1.00 75.64  ?  314  ILE   C CD1   1 
ATOM   14520 N  N     . ARG   C 2 316 ? 88.821  104.741 100.661 1.00 58.99  ?  315  ARG   C N     1 
ATOM   14521 C  CA    . ARG   C 2 316 ? 89.193  105.960 99.960  1.00 59.63  ?  315  ARG   C CA    1 
ATOM   14522 C  C     . ARG   C 2 316 ? 88.673  106.012 98.532  1.00 62.78  ?  315  ARG   C C     1 
ATOM   14523 O  O     . ARG   C 2 316 ? 88.762  107.070 97.902  1.00 71.48  ?  315  ARG   C O     1 
ATOM   14524 C  CB    . ARG   C 2 316 ? 90.711  106.117 99.974  1.00 54.21  ?  315  ARG   C CB    1 
ATOM   14525 C  CG    . ARG   C 2 316 ? 91.295  106.022 101.365 1.00 58.75  ?  315  ARG   C CG    1 
ATOM   14526 C  CD    . ARG   C 2 316 ? 91.429  107.390 102.005 1.00 60.28  ?  315  ARG   C CD    1 
ATOM   14527 N  NE    . ARG   C 2 316 ? 92.514  107.433 102.975 1.00 64.05  ?  315  ARG   C NE    1 
ATOM   14528 C  CZ    . ARG   C 2 316 ? 92.334  107.507 104.285 1.00 61.91  ?  315  ARG   C CZ    1 
ATOM   14529 N  NH1   . ARG   C 2 316 ? 91.122  107.551 104.812 1.00 66.63  ?  315  ARG   C NH1   1 
ATOM   14530 N  NH2   . ARG   C 2 316 ? 93.394  107.536 105.086 1.00 61.36  ?  315  ARG   C NH2   1 
ATOM   14531 N  N     . MET   C 2 317 ? 88.137  104.912 98.007  1.00 71.82  ?  316  MET   C N     1 
ATOM   14532 C  CA    . MET   C 2 317 ? 87.442  104.964 96.731  1.00 68.80  ?  316  MET   C CA    1 
ATOM   14533 C  C     . MET   C 2 317 ? 85.972  105.307 96.886  1.00 70.53  ?  316  MET   C C     1 
ATOM   14534 O  O     . MET   C 2 317 ? 85.392  105.916 95.981  1.00 74.69  ?  316  MET   C O     1 
ATOM   14535 C  CB    . MET   C 2 317 ? 87.585  103.631 95.998  1.00 66.93  ?  316  MET   C CB    1 
ATOM   14536 C  CG    . MET   C 2 317 ? 88.740  103.585 95.030  1.00 72.02  ?  316  MET   C CG    1 
ATOM   14537 S  SD    . MET   C 2 317 ? 88.938  101.984 94.236  1.00 86.21  ?  316  MET   C SD    1 
ATOM   14538 C  CE    . MET   C 2 317 ? 87.973  102.227 92.751  1.00 74.62  ?  316  MET   C CE    1 
ATOM   14539 N  N     . GLN   C 2 318 ? 85.365  104.946 98.021  1.00 76.04  ?  317  GLN   C N     1 
ATOM   14540 C  CA    . GLN   C 2 318 ? 84.003  105.383 98.300  1.00 73.35  ?  317  GLN   C CA    1 
ATOM   14541 C  C     . GLN   C 2 318 ? 83.920  106.898 98.424  1.00 78.56  ?  317  GLN   C C     1 
ATOM   14542 O  O     . GLN   C 2 318 ? 82.884  107.491 98.106  1.00 82.31  ?  317  GLN   C O     1 
ATOM   14543 C  CB    . GLN   C 2 318 ? 83.495  104.711 99.575  1.00 75.38  ?  317  GLN   C CB    1 
ATOM   14544 C  CG    . GLN   C 2 318 ? 82.044  105.002 99.895  1.00 74.70  ?  317  GLN   C CG    1 
ATOM   14545 C  CD    . GLN   C 2 318 ? 81.523  104.170 101.042 1.00 84.59  ?  317  GLN   C CD    1 
ATOM   14546 O  OE1   . GLN   C 2 318 ? 82.102  104.167 102.115 1.00 86.30  ?  317  GLN   C OE1   1 
ATOM   14547 N  NE2   . GLN   C 2 318 ? 80.415  103.474 100.819 1.00 86.79  ?  317  GLN   C NE2   1 
ATOM   14548 N  N     . ALA   C 2 319 ? 85.002  107.542 98.865  1.00 77.06  ?  318  ALA   C N     1 
ATOM   14549 C  CA    . ALA   C 2 319 ? 84.994  108.975 99.131  1.00 69.94  ?  318  ALA   C CA    1 
ATOM   14550 C  C     . ALA   C 2 319 ? 85.118  109.829 97.876  1.00 70.30  ?  318  ALA   C C     1 
ATOM   14551 O  O     . ALA   C 2 319 ? 84.933  111.047 97.962  1.00 79.05  ?  318  ALA   C O     1 
ATOM   14552 C  CB    . ALA   C 2 319 ? 86.121  109.333 100.101 1.00 65.33  ?  318  ALA   C CB    1 
ATOM   14553 N  N     . VAL   C 2 320 ? 85.425  109.241 96.722  1.00 71.88  ?  319  VAL   C N     1 
ATOM   14554 C  CA    . VAL   C 2 320 ? 85.577  110.019 95.497  1.00 73.30  ?  319  VAL   C CA    1 
ATOM   14555 C  C     . VAL   C 2 320 ? 84.600  109.519 94.441  1.00 76.76  ?  319  VAL   C C     1 
ATOM   14556 O  O     . VAL   C 2 320 ? 84.865  109.622 93.238  1.00 77.44  ?  319  VAL   C O     1 
ATOM   14557 C  CB    . VAL   C 2 320 ? 87.024  109.957 94.978  1.00 67.33  ?  319  VAL   C CB    1 
ATOM   14558 C  CG1   . VAL   C 2 320 ? 87.924  110.846 95.815  1.00 67.23  ?  319  VAL   C CG1   1 
ATOM   14559 C  CG2   . VAL   C 2 320 ? 87.530  108.524 94.983  1.00 72.14  ?  319  VAL   C CG2   1 
ATOM   14560 N  N     . GLY   C 2 321 ? 83.487  108.939 94.884  1.00 81.34  ?  320  GLY   C N     1 
ATOM   14561 C  CA    . GLY   C 2 321 ? 82.446  108.490 93.979  1.00 81.34  ?  320  GLY   C CA    1 
ATOM   14562 C  C     . GLY   C 2 321 ? 82.859  107.384 93.030  1.00 80.86  ?  320  GLY   C C     1 
ATOM   14563 O  O     . GLY   C 2 321 ? 82.584  107.454 91.829  1.00 84.94  ?  320  GLY   C O     1 
ATOM   14564 N  N     . LEU   C 2 322 ? 83.520  106.356 93.553  1.00 79.87  ?  321  LEU   C N     1 
ATOM   14565 C  CA    . LEU   C 2 322 ? 83.958  105.221 92.758  1.00 79.90  ?  321  LEU   C CA    1 
ATOM   14566 C  C     . LEU   C 2 322 ? 83.418  103.931 93.357  1.00 85.90  ?  321  LEU   C C     1 
ATOM   14567 O  O     . LEU   C 2 322 ? 83.123  103.858 94.553  1.00 90.54  ?  321  LEU   C O     1 
ATOM   14568 C  CB    . LEU   C 2 322 ? 85.486  105.152 92.673  1.00 83.74  ?  321  LEU   C CB    1 
ATOM   14569 C  CG    . LEU   C 2 322 ? 86.158  106.145 91.727  1.00 80.73  ?  321  LEU   C CG    1 
ATOM   14570 C  CD1   . LEU   C 2 322 ? 87.656  105.917 91.706  1.00 82.97  ?  321  LEU   C CD1   1 
ATOM   14571 C  CD2   . LEU   C 2 322 ? 85.576  106.033 90.329  1.00 81.81  ?  321  LEU   C CD2   1 
ATOM   14572 N  N     . ASP   C 2 323 ? 83.284  102.915 92.510  1.00 99.07  ?  322  ASP   C N     1 
ATOM   14573 C  CA    . ASP   C 2 323 ? 82.804  101.620 92.964  1.00 99.30  ?  322  ASP   C CA    1 
ATOM   14574 C  C     . ASP   C 2 323 ? 83.862  100.927 93.818  1.00 101.14 ?  322  ASP   C C     1 
ATOM   14575 O  O     . ASP   C 2 323 ? 85.058  101.214 93.732  1.00 104.59 ?  322  ASP   C O     1 
ATOM   14576 C  CB    . ASP   C 2 323 ? 82.429  100.739 91.773  1.00 99.76  ?  322  ASP   C CB    1 
ATOM   14577 C  CG    . ASP   C 2 323 ? 80.938  100.722 91.509  1.00 106.51 ?  322  ASP   C CG    1 
ATOM   14578 O  OD1   . ASP   C 2 323 ? 80.166  101.041 92.437  1.00 107.69 ?  322  ASP   C OD1   1 
ATOM   14579 O  OD2   . ASP   C 2 323 ? 80.536  100.391 90.374  1.00 106.53 ?  322  ASP   C OD2   1 
ATOM   14580 N  N     . LEU   C 2 324 ? 83.404  100.001 94.656  1.00 86.66  ?  323  LEU   C N     1 
ATOM   14581 C  CA    . LEU   C 2 324 ? 84.295  99.297  95.569  1.00 84.24  ?  323  LEU   C CA    1 
ATOM   14582 C  C     . LEU   C 2 324 ? 84.858  98.059  94.886  1.00 83.33  ?  323  LEU   C C     1 
ATOM   14583 O  O     . LEU   C 2 324 ? 84.088  97.155  94.535  1.00 85.92  ?  323  LEU   C O     1 
ATOM   14584 C  CB    . LEU   C 2 324 ? 83.559  98.905  96.837  1.00 82.07  ?  323  LEU   C CB    1 
ATOM   14585 C  CG    . LEU   C 2 324 ? 83.063  100.045 97.726  1.00 81.98  ?  323  LEU   C CG    1 
ATOM   14586 C  CD1   . LEU   C 2 324 ? 82.223  99.513  98.874  1.00 78.74  ?  323  LEU   C CD1   1 
ATOM   14587 C  CD2   . LEU   C 2 324 ? 84.232  100.832 98.239  1.00 83.77  ?  323  LEU   C CD2   1 
ATOM   14588 N  N     . PRO   C 2 325 ? 86.169  97.974  94.669  1.00 79.90  ?  324  PRO   C N     1 
ATOM   14589 C  CA    . PRO   C 2 325 ? 86.751  96.817  93.976  1.00 79.20  ?  324  PRO   C CA    1 
ATOM   14590 C  C     . PRO   C 2 325 ? 87.113  95.641  94.871  1.00 78.28  ?  324  PRO   C C     1 
ATOM   14591 O  O     . PRO   C 2 325 ? 87.754  94.705  94.385  1.00 86.61  ?  324  PRO   C O     1 
ATOM   14592 C  CB    . PRO   C 2 325 ? 88.022  97.418  93.363  1.00 77.20  ?  324  PRO   C CB    1 
ATOM   14593 C  CG    . PRO   C 2 325 ? 88.443  98.446  94.351  1.00 79.11  ?  324  PRO   C CG    1 
ATOM   14594 C  CD    . PRO   C 2 325 ? 87.179  99.006  94.963  1.00 82.75  ?  324  PRO   C CD    1 
ATOM   14595 N  N     . PHE   C 2 326 ? 86.779  95.684  96.158  1.00 67.96  ?  325  PHE   C N     1 
ATOM   14596 C  CA    . PHE   C 2 326 ? 87.128  94.623  97.091  1.00 68.81  ?  325  PHE   C CA    1 
ATOM   14597 C  C     . PHE   C 2 326 ? 85.932  94.347  97.991  1.00 74.59  ?  325  PHE   C C     1 
ATOM   14598 O  O     . PHE   C 2 326 ? 84.964  95.110  98.026  1.00 80.79  ?  325  PHE   C O     1 
ATOM   14599 C  CB    . PHE   C 2 326 ? 88.366  94.984  97.925  1.00 68.27  ?  325  PHE   C CB    1 
ATOM   14600 C  CG    . PHE   C 2 326 ? 89.602  95.218  97.103  1.00 70.39  ?  325  PHE   C CG    1 
ATOM   14601 C  CD1   . PHE   C 2 326 ? 90.188  94.183  96.396  1.00 71.20  ?  325  PHE   C CD1   1 
ATOM   14602 C  CD2   . PHE   C 2 326 ? 90.146  96.486  96.995  1.00 74.13  ?  325  PHE   C CD2   1 
ATOM   14603 C  CE1   . PHE   C 2 326 ? 91.320  94.402  95.632  1.00 72.51  ?  325  PHE   C CE1   1 
ATOM   14604 C  CE2   . PHE   C 2 326 ? 91.279  96.710  96.239  1.00 71.91  ?  325  PHE   C CE2   1 
ATOM   14605 C  CZ    . PHE   C 2 326 ? 91.865  95.668  95.553  1.00 73.21  ?  325  PHE   C CZ    1 
ATOM   14606 N  N     . GLN   C 2 327 ? 86.010  93.235  98.719  1.00 95.00  ?  326  GLN   C N     1 
ATOM   14607 C  CA    . GLN   C 2 327 ? 84.933  92.835  99.614  1.00 99.32  ?  326  GLN   C CA    1 
ATOM   14608 C  C     . GLN   C 2 327 ? 84.797  93.830  100.766 1.00 101.27 ?  326  GLN   C C     1 
ATOM   14609 O  O     . GLN   C 2 327 ? 85.791  94.236  101.371 1.00 96.77  ?  326  GLN   C O     1 
ATOM   14610 C  CB    . GLN   C 2 327 ? 85.185  91.416  100.125 1.00 98.02  ?  326  GLN   C CB    1 
ATOM   14611 C  CG    . GLN   C 2 327 ? 85.065  90.274  99.063  1.00 97.93  ?  326  GLN   C CG    1 
ATOM   14612 C  CD    . GLN   C 2 327 ? 84.045  90.402  97.925  1.00 103.25 ?  326  GLN   C CD    1 
ATOM   14613 O  OE1   . GLN   C 2 327 ? 83.204  91.294  97.873  1.00 102.32 ?  326  GLN   C OE1   1 
ATOM   14614 N  NE2   . GLN   C 2 327 ? 84.118  89.443  97.005  1.00 101.97 ?  326  GLN   C NE2   1 
ATOM   14615 N  N     . THR   C 2 328 ? 83.564  94.233  101.065 1.00 113.69 ?  327  THR   C N     1 
ATOM   14616 C  CA    . THR   C 2 328 ? 83.309  95.257  102.076 1.00 113.02 ?  327  THR   C CA    1 
ATOM   14617 C  C     . THR   C 2 328 ? 83.499  94.667  103.457 1.00 112.59 ?  327  THR   C C     1 
ATOM   14618 O  O     . THR   C 2 328 ? 82.550  94.192  104.099 1.00 114.78 ?  327  THR   C O     1 
ATOM   14619 C  CB    . THR   C 2 328 ? 81.916  95.844  101.914 1.00 111.49 ?  327  THR   C CB    1 
ATOM   14620 O  OG1   . THR   C 2 328 ? 81.674  96.105  100.527 1.00 109.58 ?  327  THR   C OG1   1 
ATOM   14621 C  CG2   . THR   C 2 328 ? 81.780  97.130  102.701 1.00 110.52 ?  327  THR   C CG2   1 
ATOM   14622 N  N     . ARG   C 2 329 ? 84.696  94.923  103.968 1.00 114.46 ?  328  ARG   C N     1 
ATOM   14623 C  CA    . ARG   C 2 329 ? 84.996  94.264  105.238 1.00 116.71 ?  328  ARG   C CA    1 
ATOM   14624 C  C     . ARG   C 2 329 ? 85.273  95.283  106.312 1.00 115.59 ?  328  ARG   C C     1 
ATOM   14625 O  O     . ARG   C 2 329 ? 84.997  96.451  106.100 1.00 114.06 ?  328  ARG   C O     1 
ATOM   14626 C  CB    . ARG   C 2 329 ? 86.270  93.439  105.124 1.00 115.45 ?  328  ARG   C CB    1 
ATOM   14627 C  CG    . ARG   C 2 329 ? 86.207  92.310  104.112 1.00 114.86 ?  328  ARG   C CG    1 
ATOM   14628 C  CD    . ARG   C 2 329 ? 85.205  91.205  104.402 1.00 117.37 ?  328  ARG   C CD    1 
ATOM   14629 N  NE    . ARG   C 2 329 ? 85.495  90.538  105.657 1.00 121.28 ?  328  ARG   C NE    1 
ATOM   14630 C  CZ    . ARG   C 2 329 ? 86.394  89.573  105.812 1.00 121.09 ?  328  ARG   C CZ    1 
ATOM   14631 N  NH1   . ARG   C 2 329 ? 87.127  89.169  104.790 1.00 119.36 ?  328  ARG   C NH1   1 
ATOM   14632 N  NH2   . ARG   C 2 329 ? 86.575  89.024  106.998 1.00 118.58 ?  328  ARG   C NH2   1 
ATOM   14633 N  N     . SER   C 2 330 ? 85.857  94.819  107.399 1.00 100.04 ?  329  SER   C N     1 
ATOM   14634 C  CA    . SER   C 2 330 ? 86.233  95.746  108.440 1.00 102.23 ?  329  SER   C CA    1 
ATOM   14635 C  C     . SER   C 2 330 ? 87.739  95.986  108.406 1.00 101.62 ?  329  SER   C C     1 
ATOM   14636 O  O     . SER   C 2 330 ? 88.478  95.387  107.621 1.00 99.46  ?  329  SER   C O     1 
ATOM   14637 C  CB    . SER   C 2 330 ? 85.781  95.235  109.806 1.00 101.26 ?  329  SER   C CB    1 
ATOM   14638 O  OG    . SER   C 2 330 ? 86.101  93.865  109.968 1.00 101.25 ?  329  SER   C OG    1 
ATOM   14639 N  N     . ASN   C 2 331 ? 88.195  96.874  109.275 1.00 84.15  ?  330  ASN   C N     1 
ATOM   14640 C  CA    . ASN   C 2 331 ? 89.618  97.170  109.375 1.00 78.29  ?  330  ASN   C CA    1 
ATOM   14641 C  C     . ASN   C 2 331 ? 90.342  95.984  109.997 1.00 80.80  ?  330  ASN   C C     1 
ATOM   14642 O  O     . ASN   C 2 331 ? 90.018  95.595  111.127 1.00 83.39  ?  330  ASN   C O     1 
ATOM   14643 C  CB    . ASN   C 2 331 ? 89.829  98.432  110.210 1.00 79.79  ?  330  ASN   C CB    1 
ATOM   14644 C  CG    . ASN   C 2 331 ? 91.190  99.060  109.993 1.00 79.83  ?  330  ASN   C CG    1 
ATOM   14645 O  OD1   . ASN   C 2 331 ? 92.114  98.419  109.500 1.00 82.89  ?  330  ASN   C OD1   1 
ATOM   14646 N  ND2   . ASN   C 2 331 ? 91.317  100.328 110.363 1.00 79.29  ?  330  ASN   C ND2   1 
ATOM   14647 N  N     . PRO   C 2 332 ? 91.310  95.375  109.307 1.00 69.49  ?  331  PRO   C N     1 
ATOM   14648 C  CA    . PRO   C 2 332 ? 92.033  94.248  109.910 1.00 67.13  ?  331  PRO   C CA    1 
ATOM   14649 C  C     . PRO   C 2 332 ? 93.013  94.666  110.994 1.00 72.55  ?  331  PRO   C C     1 
ATOM   14650 O  O     . PRO   C 2 332 ? 93.537  93.792  111.693 1.00 79.33  ?  331  PRO   C O     1 
ATOM   14651 C  CB    . PRO   C 2 332 ? 92.765  93.624  108.714 1.00 69.50  ?  331  PRO   C CB    1 
ATOM   14652 C  CG    . PRO   C 2 332 ? 92.949  94.752  107.766 1.00 72.44  ?  331  PRO   C CG    1 
ATOM   14653 C  CD    . PRO   C 2 332 ? 91.758  95.656  107.932 1.00 69.97  ?  331  PRO   C CD    1 
ATOM   14654 N  N     . ILE   C 2 333 ? 93.378  95.942  111.070 1.00 64.73  ?  332  ILE   C N     1 
ATOM   14655 C  CA    . ILE   C 2 333 ? 94.300  96.433  112.094 1.00 64.02  ?  332  ILE   C CA    1 
ATOM   14656 C  C     . ILE   C 2 333 ? 93.659  97.638  112.772 1.00 63.29  ?  332  ILE   C C     1 
ATOM   14657 O  O     . ILE   C 2 333 ? 94.000  98.785  112.451 1.00 73.27  ?  332  ILE   C O     1 
ATOM   14658 C  CB    . ILE   C 2 333 ? 95.678  96.789  111.510 1.00 64.01  ?  332  ILE   C CB    1 
ATOM   14659 C  CG1   . ILE   C 2 333 ? 95.540  97.405  110.118 1.00 60.88  ?  332  ILE   C CG1   1 
ATOM   14660 C  CG2   . ILE   C 2 333 ? 96.559  95.559  111.452 1.00 65.28  ?  332  ILE   C CG2   1 
ATOM   14661 C  CD1   . ILE   C 2 333 ? 96.800  98.077  109.625 1.00 57.67  ?  332  ILE   C CD1   1 
ATOM   14662 N  N     . PRO   C 2 334 ? 92.714  97.431  113.690 1.00 69.60  ?  333  PRO   C N     1 
ATOM   14663 C  CA    . PRO   C 2 334 ? 92.031  98.579  114.309 1.00 72.21  ?  333  PRO   C CA    1 
ATOM   14664 C  C     . PRO   C 2 334 ? 92.952  99.489  115.102 1.00 76.87  ?  333  PRO   C C     1 
ATOM   14665 O  O     . PRO   C 2 334 ? 92.613  100.664 115.298 1.00 79.24  ?  333  PRO   C O     1 
ATOM   14666 C  CB    . PRO   C 2 334 ? 90.981  97.918  115.213 1.00 76.68  ?  333  PRO   C CB    1 
ATOM   14667 C  CG    . PRO   C 2 334 ? 91.492  96.535  115.450 1.00 76.25  ?  333  PRO   C CG    1 
ATOM   14668 C  CD    . PRO   C 2 334 ? 92.216  96.144  114.200 1.00 73.14  ?  333  PRO   C CD    1 
ATOM   14669 N  N     . TRP   C 2 335 ? 94.108  98.995  115.554 1.00 61.84  ?  334  TRP   C N     1 
ATOM   14670 C  CA    . TRP   C 2 335 ? 95.006  99.821  116.353 1.00 57.86  ?  334  TRP   C CA    1 
ATOM   14671 C  C     . TRP   C 2 335 ? 95.518  101.032 115.585 1.00 65.07  ?  334  TRP   C C     1 
ATOM   14672 O  O     . TRP   C 2 335 ? 95.935  102.015 116.210 1.00 77.99  ?  334  TRP   C O     1 
ATOM   14673 C  CB    . TRP   C 2 335 ? 96.184  98.989  116.864 1.00 60.23  ?  334  TRP   C CB    1 
ATOM   14674 C  CG    . TRP   C 2 335 ? 96.860  98.154  115.817 1.00 63.22  ?  334  TRP   C CG    1 
ATOM   14675 C  CD1   . TRP   C 2 335 ? 96.647  96.833  115.562 1.00 59.59  ?  334  TRP   C CD1   1 
ATOM   14676 C  CD2   . TRP   C 2 335 ? 97.870  98.583  114.894 1.00 65.84  ?  334  TRP   C CD2   1 
ATOM   14677 N  NE1   . TRP   C 2 335 ? 97.456  96.412  114.536 1.00 62.29  ?  334  TRP   C NE1   1 
ATOM   14678 C  CE2   . TRP   C 2 335 ? 98.216  97.468  114.107 1.00 67.44  ?  334  TRP   C CE2   1 
ATOM   14679 C  CE3   . TRP   C 2 335 ? 98.510  99.801  114.654 1.00 56.65  ?  334  TRP   C CE3   1 
ATOM   14680 C  CZ2   . TRP   C 2 335 ? 99.174  97.535  113.099 1.00 62.77  ?  334  TRP   C CZ2   1 
ATOM   14681 C  CZ3   . TRP   C 2 335 ? 99.461  99.865  113.653 1.00 59.58  ?  334  TRP   C CZ3   1 
ATOM   14682 C  CH2   . TRP   C 2 335 ? 99.784  98.740  112.889 1.00 61.52  ?  334  TRP   C CH2   1 
ATOM   14683 N  N     . ILE   C 2 336 ? 95.478  100.995 114.250 1.00 56.80  ?  335  ILE   C N     1 
ATOM   14684 C  CA    . ILE   C 2 336 ? 95.880  102.157 113.461 1.00 56.02  ?  335  ILE   C CA    1 
ATOM   14685 C  C     . ILE   C 2 336 ? 95.027  103.365 113.817 1.00 64.87  ?  335  ILE   C C     1 
ATOM   14686 O  O     . ILE   C 2 336 ? 95.479  104.511 113.708 1.00 73.00  ?  335  ILE   C O     1 
ATOM   14687 C  CB    . ILE   C 2 336 ? 95.812  101.835 111.953 1.00 54.59  ?  335  ILE   C CB    1 
ATOM   14688 C  CG1   . ILE   C 2 336 ? 96.594  102.874 111.150 1.00 62.61  ?  335  ILE   C CG1   1 
ATOM   14689 C  CG2   . ILE   C 2 336 ? 94.373  101.777 111.466 1.00 58.49  ?  335  ILE   C CG2   1 
ATOM   14690 C  CD1   . ILE   C 2 336 ? 98.052  102.549 111.001 1.00 61.88  ?  335  ILE   C CD1   1 
ATOM   14691 N  N     . ASN   C 2 337 ? 93.795  103.133 114.272 1.00 65.74  ?  336  ASN   C N     1 
ATOM   14692 C  CA    . ASN   C 2 337 ? 92.916  104.234 114.632 1.00 58.97  ?  336  ASN   C CA    1 
ATOM   14693 C  C     . ASN   C 2 337 ? 93.421  105.017 115.835 1.00 64.06  ?  336  ASN   C C     1 
ATOM   14694 O  O     . ASN   C 2 337 ? 92.978  106.150 116.043 1.00 71.84  ?  336  ASN   C O     1 
ATOM   14695 C  CB    . ASN   C 2 337 ? 91.510  103.706 114.901 1.00 64.74  ?  336  ASN   C CB    1 
ATOM   14696 C  CG    . ASN   C 2 337 ? 90.717  103.490 113.630 1.00 73.14  ?  336  ASN   C CG    1 
ATOM   14697 O  OD1   . ASN   C 2 337 ? 90.303  104.443 112.971 1.00 82.62  ?  336  ASN   C OD1   1 
ATOM   14698 N  ND2   . ASN   C 2 337 ? 90.495  102.230 113.283 1.00 75.03  ?  336  ASN   C ND2   1 
ATOM   14699 N  N     . THR   C 2 338 ? 94.325  104.446 116.630 1.00 61.31  ?  337  THR   C N     1 
ATOM   14700 C  CA    . THR   C 2 338 ? 94.915  105.195 117.727 1.00 60.35  ?  337  THR   C CA    1 
ATOM   14701 C  C     . THR   C 2 338 ? 96.030  106.120 117.265 1.00 65.10  ?  337  THR   C C     1 
ATOM   14702 O  O     . THR   C 2 338 ? 96.513  106.926 118.064 1.00 76.03  ?  337  THR   C O     1 
ATOM   14703 C  CB    . THR   C 2 338 ? 95.456  104.238 118.794 1.00 62.27  ?  337  THR   C CB    1 
ATOM   14704 O  OG1   . THR   C 2 338 ? 96.734  103.732 118.389 1.00 66.72  ?  337  THR   C OG1   1 
ATOM   14705 C  CG2   . THR   C 2 338 ? 94.494  103.082 118.991 1.00 64.20  ?  337  THR   C CG2   1 
ATOM   14706 N  N     . TRP   C 2 339 ? 96.481  105.992 116.018 1.00 51.74  ?  338  TRP   C N     1 
ATOM   14707 C  CA    . TRP   C 2 339 ? 97.562  106.816 115.498 1.00 44.12  ?  338  TRP   C CA    1 
ATOM   14708 C  C     . TRP   C 2 339 ? 97.077  107.918 114.569 1.00 59.61  ?  338  TRP   C C     1 
ATOM   14709 O  O     . TRP   C 2 339 ? 97.859  108.813 114.234 1.00 69.93  ?  338  TRP   C O     1 
ATOM   14710 C  CB    . TRP   C 2 339 ? 98.585  105.942 114.765 1.00 42.29  ?  338  TRP   C CB    1 
ATOM   14711 C  CG    . TRP   C 2 339 ? 99.325  105.021 115.674 1.00 45.69  ?  338  TRP   C CG    1 
ATOM   14712 C  CD1   . TRP   C 2 339 ? 99.015  103.726 115.955 1.00 50.68  ?  338  TRP   C CD1   1 
ATOM   14713 C  CD2   . TRP   C 2 339 ? 100.499 105.328 116.433 1.00 57.99  ?  338  TRP   C CD2   1 
ATOM   14714 N  NE1   . TRP   C 2 339 ? 99.923  103.204 116.840 1.00 57.49  ?  338  TRP   C NE1   1 
ATOM   14715 C  CE2   . TRP   C 2 339 ? 100.846 104.168 117.148 1.00 60.17  ?  338  TRP   C CE2   1 
ATOM   14716 C  CE3   . TRP   C 2 339 ? 101.290 106.470 116.577 1.00 55.91  ?  338  TRP   C CE3   1 
ATOM   14717 C  CZ2   . TRP   C 2 339 ? 101.947 104.117 117.997 1.00 56.76  ?  338  TRP   C CZ2   1 
ATOM   14718 C  CZ3   . TRP   C 2 339 ? 102.384 106.417 117.417 1.00 53.81  ?  338  TRP   C CZ3   1 
ATOM   14719 C  CH2   . TRP   C 2 339 ? 102.703 105.249 118.116 1.00 56.51  ?  338  TRP   C CH2   1 
ATOM   14720 N  N     . LEU   C 2 340 ? 95.813  107.876 114.147 1.00 57.88  ?  339  LEU   C N     1 
ATOM   14721 C  CA    . LEU   C 2 340 ? 95.251  108.892 113.272 1.00 57.82  ?  339  LEU   C CA    1 
ATOM   14722 C  C     . LEU   C 2 340 ? 94.171  109.733 113.934 1.00 65.86  ?  339  LEU   C C     1 
ATOM   14723 O  O     . LEU   C 2 340 ? 93.854  110.811 113.424 1.00 73.42  ?  339  LEU   C O     1 
ATOM   14724 C  CB    . LEU   C 2 340 ? 94.676  108.241 112.006 1.00 61.64  ?  339  LEU   C CB    1 
ATOM   14725 C  CG    . LEU   C 2 340 ? 95.534  107.117 111.422 1.00 57.46  ?  339  LEU   C CG    1 
ATOM   14726 C  CD1   . LEU   C 2 340 ? 94.787  106.375 110.330 1.00 57.76  ?  339  LEU   C CD1   1 
ATOM   14727 C  CD2   . LEU   C 2 340 ? 96.851  107.668 110.897 1.00 58.13  ?  339  LEU   C CD2   1 
ATOM   14728 N  N     . VAL   C 2 341 ? 93.607  109.273 115.047 1.00 76.06  ?  340  VAL   C N     1 
ATOM   14729 C  CA    . VAL   C 2 341 ? 92.628  110.028 115.820 1.00 71.33  ?  340  VAL   C CA    1 
ATOM   14730 C  C     . VAL   C 2 341 ? 93.254  110.336 117.172 1.00 76.23  ?  340  VAL   C C     1 
ATOM   14731 O  O     . VAL   C 2 341 ? 93.571  109.420 117.940 1.00 76.35  ?  340  VAL   C O     1 
ATOM   14732 C  CB    . VAL   C 2 341 ? 91.311  109.254 115.980 1.00 71.81  ?  340  VAL   C CB    1 
ATOM   14733 C  CG1   . VAL   C 2 341 ? 90.358  110.010 116.890 1.00 76.09  ?  340  VAL   C CG1   1 
ATOM   14734 C  CG2   . VAL   C 2 341 ? 90.677  109.001 114.621 1.00 70.40  ?  340  VAL   C CG2   1 
ATOM   14735 N  N     . SER   C 2 342 ? 93.430  111.625 117.464 1.00 78.92  ?  341  SER   C N     1 
ATOM   14736 C  CA    . SER   C 2 342 ? 94.130  112.068 118.662 1.00 75.99  ?  341  SER   C CA    1 
ATOM   14737 C  C     . SER   C 2 342 ? 93.191  112.651 119.713 1.00 74.08  ?  341  SER   C C     1 
ATOM   14738 O  O     . SER   C 2 342 ? 93.646  113.354 120.620 1.00 81.94  ?  341  SER   C O     1 
ATOM   14739 C  CB    . SER   C 2 342 ? 95.207  113.088 118.293 1.00 79.61  ?  341  SER   C CB    1 
ATOM   14740 O  OG    . SER   C 2 342 ? 94.647  114.376 118.113 1.00 79.04  ?  341  SER   C OG    1 
ATOM   14741 N  N     . ASP   C 2 343 ? 91.892  112.370 119.617 1.00 75.09  ?  342  ASP   C N     1 
ATOM   14742 C  CA    . ASP   C 2 343 ? 90.944  112.945 120.565 1.00 70.18  ?  342  ASP   C CA    1 
ATOM   14743 C  C     . ASP   C 2 343 ? 91.013  112.267 121.928 1.00 72.15  ?  342  ASP   C C     1 
ATOM   14744 O  O     . ASP   C 2 343 ? 91.002  112.948 122.958 1.00 74.85  ?  342  ASP   C O     1 
ATOM   14745 C  CB    . ASP   C 2 343 ? 89.530  112.869 119.997 1.00 72.59  ?  342  ASP   C CB    1 
ATOM   14746 C  CG    . ASP   C 2 343 ? 88.651  114.007 120.471 1.00 82.09  ?  342  ASP   C CG    1 
ATOM   14747 O  OD1   . ASP   C 2 343 ? 89.138  115.154 120.508 1.00 83.78  ?  342  ASP   C OD1   1 
ATOM   14748 O  OD2   . ASP   C 2 343 ? 87.472  113.757 120.803 1.00 86.44  ?  342  ASP   C OD2   1 
ATOM   14749 N  N     . ASN   C 2 344 ? 91.104  110.939 121.956 1.00 64.03  ?  343  ASN   C N     1 
ATOM   14750 C  CA    . ASN   C 2 344 ? 91.143  110.180 123.197 1.00 61.10  ?  343  ASN   C CA    1 
ATOM   14751 C  C     . ASN   C 2 344 ? 92.545  109.712 123.555 1.00 61.81  ?  343  ASN   C C     1 
ATOM   14752 O  O     . ASN   C 2 344 ? 92.696  108.862 124.437 1.00 69.40  ?  343  ASN   C O     1 
ATOM   14753 C  CB    . ASN   C 2 344 ? 90.197  108.982 123.110 1.00 61.83  ?  343  ASN   C CB    1 
ATOM   14754 C  CG    . ASN   C 2 344 ? 90.574  108.019 122.002 1.00 64.33  ?  343  ASN   C CG    1 
ATOM   14755 O  OD1   . ASN   C 2 344 ? 91.321  108.367 121.089 1.00 69.22  ?  343  ASN   C OD1   1 
ATOM   14756 N  ND2   . ASN   C 2 344 ? 90.056  106.800 122.078 1.00 67.65  ?  343  ASN   C ND2   1 
ATOM   14757 N  N     . VAL   C 2 345 ? 93.568  110.240 122.894 1.00 60.88  ?  344  VAL   C N     1 
ATOM   14758 C  CA    . VAL   C 2 345 ? 94.946  109.822 123.124 1.00 58.59  ?  344  VAL   C CA    1 
ATOM   14759 C  C     . VAL   C 2 345 ? 95.538  110.684 124.230 1.00 67.26  ?  344  VAL   C C     1 
ATOM   14760 O  O     . VAL   C 2 345 ? 95.564  111.915 124.123 1.00 71.37  ?  344  VAL   C O     1 
ATOM   14761 C  CB    . VAL   C 2 345 ? 95.777  109.925 121.838 1.00 60.39  ?  344  VAL   C CB    1 
ATOM   14762 C  CG1   . VAL   C 2 345 ? 97.257  109.788 122.150 1.00 63.33  ?  344  VAL   C CG1   1 
ATOM   14763 C  CG2   . VAL   C 2 345 ? 95.336  108.870 120.838 1.00 64.68  ?  344  VAL   C CG2   1 
ATOM   14764 N  N     . GLN   C 2 346 ? 95.939  110.055 125.330 1.00 77.46  ?  345  GLN   C N     1 
ATOM   14765 C  CA    . GLN   C 2 346 ? 96.622  110.762 126.443 1.00 72.14  ?  345  GLN   C CA    1 
ATOM   14766 C  C     . GLN   C 2 346 ? 98.000  110.163 126.624 1.00 78.15  ?  345  GLN   C C     1 
ATOM   14767 O  O     . GLN   C 2 346 ? 98.110  109.116 127.143 1.00 85.04  ?  345  GLN   C O     1 
ATOM   14768 C  CB    . GLN   C 2 346 ? 95.935  110.578 127.774 1.00 73.20  ?  345  GLN   C CB    1 
ATOM   14769 C  CG    . GLN   C 2 346 ? 96.619  111.335 128.885 1.00 72.26  ?  345  GLN   C CG    1 
ATOM   14770 C  CD    . GLN   C 2 346 ? 95.774  111.164 130.112 1.00 78.62  ?  345  GLN   C CD    1 
ATOM   14771 O  OE1   . GLN   C 2 346 ? 94.583  110.912 130.022 1.00 75.97  ?  345  GLN   C OE1   1 
ATOM   14772 N  NE2   . GLN   C 2 346 ? 96.390  111.284 131.268 1.00 87.16  ?  345  GLN   C NE2   1 
ATOM   14773 N  N     . VAL   C 2 347 ? 98.979  110.809 126.036 1.00 78.21  ?  346  VAL   C N     1 
ATOM   14774 C  CA    . VAL   C 2 347 ? 100.381 110.340 126.131 1.00 75.47  ?  346  VAL   C CA    1 
ATOM   14775 C  C     . VAL   C 2 347 ? 100.957 110.817 127.455 1.00 78.80  ?  346  VAL   C C     1 
ATOM   14776 O  O     . VAL   C 2 347 ? 100.440 111.797 128.002 1.00 81.45  ?  346  VAL   C O     1 
ATOM   14777 C  CB    . VAL   C 2 347 ? 101.215 110.890 124.962 1.00 73.65  ?  346  VAL   C CB    1 
ATOM   14778 C  CG1   . VAL   C 2 347 ? 100.580 110.594 123.616 1.00 79.19  ?  346  VAL   C CG1   1 
ATOM   14779 C  CG2   . VAL   C 2 347 ? 101.491 112.375 125.108 1.00 73.83  ?  346  VAL   C CG2   1 
ATOM   14780 N  N     . ALA   C 2 348 ? 101.960 110.112 127.963 1.00 77.75  ?  347  ALA   C N     1 
ATOM   14781 C  CA    . ALA   C 2 348 ? 102.660 110.553 129.163 1.00 70.95  ?  347  ALA   C CA    1 
ATOM   14782 C  C     . ALA   C 2 348 ? 103.669 111.620 128.766 1.00 75.56  ?  347  ALA   C C     1 
ATOM   14783 O  O     . ALA   C 2 348 ? 104.736 111.297 128.229 1.00 77.70  ?  347  ALA   C O     1 
ATOM   14784 C  CB    . ALA   C 2 348 ? 103.348 109.380 129.863 1.00 68.80  ?  347  ALA   C CB    1 
ATOM   14785 N  N     . PRO   C 2 349 ? 103.367 112.897 129.000 1.00 66.54  ?  348  PRO   C N     1 
ATOM   14786 C  CA    . PRO   C 2 349 ? 104.221 113.960 128.455 1.00 61.40  ?  348  PRO   C CA    1 
ATOM   14787 C  C     . PRO   C 2 349 ? 105.634 113.956 129.010 1.00 63.21  ?  348  PRO   C C     1 
ATOM   14788 O  O     . PRO   C 2 349 ? 106.521 114.563 128.402 1.00 64.17  ?  348  PRO   C O     1 
ATOM   14789 C  CB    . PRO   C 2 349 ? 103.466 115.242 128.843 1.00 56.77  ?  348  PRO   C CB    1 
ATOM   14790 C  CG    . PRO   C 2 349 ? 102.055 114.782 129.131 1.00 60.62  ?  348  PRO   C CG    1 
ATOM   14791 C  CD    . PRO   C 2 349 ? 102.243 113.449 129.770 1.00 61.49  ?  348  PRO   C CD    1 
ATOM   14792 N  N     . GLN   C 2 350 ? 105.853 113.385 130.192 1.00 71.85  ?  349  GLN   C N     1 
ATOM   14793 C  CA    . GLN   C 2 350 ? 107.191 113.357 130.765 1.00 66.67  ?  349  GLN   C CA    1 
ATOM   14794 C  C     . GLN   C 2 350 ? 108.018 112.188 130.256 1.00 71.29  ?  349  GLN   C C     1 
ATOM   14795 O  O     . GLN   C 2 350 ? 109.210 112.106 130.570 1.00 78.98  ?  349  GLN   C O     1 
ATOM   14796 C  CB    . GLN   C 2 350 ? 107.119 113.304 132.293 1.00 65.46  ?  349  GLN   C CB    1 
ATOM   14797 C  CG    . GLN   C 2 350 ? 106.564 114.550 132.973 1.00 66.50  ?  349  GLN   C CG    1 
ATOM   14798 C  CD    . GLN   C 2 350 ? 107.293 115.829 132.593 1.00 75.31  ?  349  GLN   C CD    1 
ATOM   14799 O  OE1   . GLN   C 2 350 ? 108.435 115.800 132.139 1.00 82.17  ?  349  GLN   C OE1   1 
ATOM   14800 N  NE2   . GLN   C 2 350 ? 106.632 116.964 132.788 1.00 71.71  ?  349  GLN   C NE2   1 
ATOM   14801 N  N     . GLU   C 2 351 ? 107.416 111.290 129.485 1.00 71.07  ?  350  GLU   C N     1 
ATOM   14802 C  CA    . GLU   C 2 351 ? 108.114 110.167 128.880 1.00 72.14  ?  350  GLU   C CA    1 
ATOM   14803 C  C     . GLU   C 2 351 ? 108.215 110.266 127.368 1.00 74.15  ?  350  GLU   C C     1 
ATOM   14804 O  O     . GLU   C 2 351 ? 109.266 109.958 126.801 1.00 79.40  ?  350  GLU   C O     1 
ATOM   14805 C  CB    . GLU   C 2 351 ? 107.408 108.859 129.243 1.00 76.02  ?  350  GLU   C CB    1 
ATOM   14806 C  CG    . GLU   C 2 351 ? 107.260 108.607 130.729 1.00 77.21  ?  350  GLU   C CG    1 
ATOM   14807 C  CD    . GLU   C 2 351 ? 106.656 107.263 131.056 1.00 83.70  ?  350  GLU   C CD    1 
ATOM   14808 O  OE1   . GLU   C 2 351 ? 106.894 106.304 130.298 1.00 86.48  ?  350  GLU   C OE1   1 
ATOM   14809 O  OE2   . GLU   C 2 351 ? 105.957 107.169 132.086 1.00 84.49  ?  350  GLU   C OE2   1 
ATOM   14810 N  N     . VAL   C 2 352 ? 107.139 110.684 126.700 1.00 72.51  ?  351  VAL   C N     1 
ATOM   14811 C  CA    . VAL   C 2 352 ? 107.100 110.801 125.251 1.00 70.87  ?  351  VAL   C CA    1 
ATOM   14812 C  C     . VAL   C 2 352 ? 106.566 112.179 124.891 1.00 70.71  ?  351  VAL   C C     1 
ATOM   14813 O  O     . VAL   C 2 352 ? 105.929 112.858 125.698 1.00 75.38  ?  351  VAL   C O     1 
ATOM   14814 C  CB    . VAL   C 2 352 ? 106.237 109.700 124.597 1.00 67.38  ?  351  VAL   C CB    1 
ATOM   14815 C  CG1   . VAL   C 2 352 ? 106.745 108.322 124.992 1.00 74.32  ?  351  VAL   C CG1   1 
ATOM   14816 C  CG2   . VAL   C 2 352 ? 104.784 109.865 124.992 1.00 64.58  ?  351  VAL   C CG2   1 
ATOM   14817 N  N     . GLU   C 2 353 ? 106.845 112.592 123.660 1.00 80.44  ?  352  GLU   C N     1 
ATOM   14818 C  CA    . GLU   C 2 353 ? 106.396 113.892 123.190 1.00 79.58  ?  352  GLU   C CA    1 
ATOM   14819 C  C     . GLU   C 2 353 ? 104.888 113.888 122.947 1.00 81.72  ?  352  GLU   C C     1 
ATOM   14820 O  O     . GLU   C 2 353 ? 104.267 112.847 122.720 1.00 82.87  ?  352  GLU   C O     1 
ATOM   14821 C  CB    . GLU   C 2 353 ? 107.135 114.278 121.911 1.00 76.28  ?  352  GLU   C CB    1 
ATOM   14822 C  CG    . GLU   C 2 353 ? 108.332 115.180 122.135 1.00 81.24  ?  352  GLU   C CG    1 
ATOM   14823 C  CD    . GLU   C 2 353 ? 109.527 114.425 122.688 1.00 90.20  ?  352  GLU   C CD    1 
ATOM   14824 O  OE1   . GLU   C 2 353 ? 109.703 113.243 122.322 1.00 88.10  ?  352  GLU   C OE1   1 
ATOM   14825 O  OE2   . GLU   C 2 353 ? 110.287 115.007 123.489 1.00 89.05  ?  352  GLU   C OE2   1 
ATOM   14826 N  N     . VAL   C 2 354 ? 104.300 115.079 123.002 1.00 78.70  ?  353  VAL   C N     1 
ATOM   14827 C  CA    . VAL   C 2 354 ? 102.878 115.273 122.738 1.00 77.03  ?  353  VAL   C CA    1 
ATOM   14828 C  C     . VAL   C 2 354 ? 102.724 115.779 121.312 1.00 79.79  ?  353  VAL   C C     1 
ATOM   14829 O  O     . VAL   C 2 354 ? 103.390 116.741 120.911 1.00 86.73  ?  353  VAL   C O     1 
ATOM   14830 C  CB    . VAL   C 2 354 ? 102.250 116.255 123.742 1.00 80.12  ?  353  VAL   C CB    1 
ATOM   14831 C  CG1   . VAL   C 2 354 ? 100.803 116.543 123.373 1.00 78.15  ?  353  VAL   C CG1   1 
ATOM   14832 C  CG2   . VAL   C 2 354 ? 102.356 115.724 125.159 1.00 77.44  ?  353  VAL   C CG2   1 
ATOM   14833 N  N     . SER   C 2 355 ? 101.863 115.118 120.539 1.00 73.67  ?  354  SER   C N     1 
ATOM   14834 C  CA    . SER   C 2 355 ? 101.642 115.451 119.139 1.00 74.78  ?  354  SER   C CA    1 
ATOM   14835 C  C     . SER   C 2 355 ? 100.340 116.211 118.914 1.00 74.00  ?  354  SER   C C     1 
ATOM   14836 O  O     . SER   C 2 355 ? 99.830  116.231 117.789 1.00 78.93  ?  354  SER   C O     1 
ATOM   14837 C  CB    . SER   C 2 355 ? 101.655 114.180 118.295 1.00 76.54  ?  354  SER   C CB    1 
ATOM   14838 O  OG    . SER   C 2 355 ? 100.687 113.264 118.773 1.00 83.71  ?  354  SER   C OG    1 
ATOM   14839 N  N     . SER   C 2 356 ? 99.794  116.834 119.954 1.00 67.13  ?  355  SER   C N     1 
ATOM   14840 C  CA    . SER   C 2 356 ? 98.506  117.505 119.843 1.00 69.38  ?  355  SER   C CA    1 
ATOM   14841 C  C     . SER   C 2 356 ? 98.637  118.991 120.146 1.00 76.46  ?  355  SER   C C     1 
ATOM   14842 O  O     . SER   C 2 356 ? 97.828  119.551 120.892 1.00 82.61  ?  355  SER   C O     1 
ATOM   14843 C  CB    . SER   C 2 356 ? 97.487  116.857 120.781 1.00 73.40  ?  355  SER   C CB    1 
ATOM   14844 O  OG    . SER   C 2 356 ? 96.196  117.409 120.593 1.00 78.59  ?  355  SER   C OG    1 
ATOM   14845 N  N     . TYR   C 2 357 ? 99.650  119.636 119.577 1.00 73.48  ?  356  TYR   C N     1 
ATOM   14846 C  CA    . TYR   C 2 357 ? 99.900  121.052 119.794 1.00 72.21  ?  356  TYR   C CA    1 
ATOM   14847 C  C     . TYR   C 2 357 ? 99.653  121.831 118.511 1.00 73.45  ?  356  TYR   C C     1 
ATOM   14848 O  O     . TYR   C 2 357 ? 99.987  121.368 117.416 1.00 79.18  ?  356  TYR   C O     1 
ATOM   14849 C  CB    . TYR   C 2 357 ? 101.331 121.293 120.275 1.00 72.01  ?  356  TYR   C CB    1 
ATOM   14850 C  CG    . TYR   C 2 357 ? 101.604 120.773 121.664 1.00 74.04  ?  356  TYR   C CG    1 
ATOM   14851 C  CD1   . TYR   C 2 357 ? 100.650 120.881 122.666 1.00 72.68  ?  356  TYR   C CD1   1 
ATOM   14852 C  CD2   . TYR   C 2 357 ? 102.814 120.173 121.975 1.00 72.17  ?  356  TYR   C CD2   1 
ATOM   14853 C  CE1   . TYR   C 2 357 ? 100.893 120.404 123.935 1.00 74.23  ?  356  TYR   C CE1   1 
ATOM   14854 C  CE2   . TYR   C 2 357 ? 103.067 119.699 123.241 1.00 73.09  ?  356  TYR   C CE2   1 
ATOM   14855 C  CZ    . TYR   C 2 357 ? 102.103 119.813 124.218 1.00 78.43  ?  356  TYR   C CZ    1 
ATOM   14856 O  OH    . TYR   C 2 357 ? 102.353 119.339 125.484 1.00 80.73  ?  356  TYR   C OH    1 
ATOM   14857 N  N     . LEU   C 2 358 ? 99.067  123.015 118.656 1.00 63.51  ?  357  LEU   C N     1 
ATOM   14858 C  CA    . LEU   C 2 358 ? 98.835  123.927 117.547 1.00 57.16  ?  357  LEU   C CA    1 
ATOM   14859 C  C     . LEU   C 2 358 ? 99.736  125.143 117.698 1.00 61.52  ?  357  LEU   C C     1 
ATOM   14860 O  O     . LEU   C 2 358 ? 100.000 125.597 118.815 1.00 75.60  ?  357  LEU   C O     1 
ATOM   14861 C  CB    . LEU   C 2 358 ? 97.369  124.361 117.487 1.00 60.49  ?  357  LEU   C CB    1 
ATOM   14862 C  CG    . LEU   C 2 358 ? 96.344  123.231 117.400 1.00 58.65  ?  357  LEU   C CG    1 
ATOM   14863 C  CD1   . LEU   C 2 358 ? 94.933  123.789 117.377 1.00 63.30  ?  357  LEU   C CD1   1 
ATOM   14864 C  CD2   . LEU   C 2 358 ? 96.606  122.375 116.175 1.00 61.11  ?  357  LEU   C CD2   1 
ATOM   14865 N  N     . VAL   C 2 359 ? 100.209 125.666 116.572 1.00 57.05  ?  358  VAL   C N     1 
ATOM   14866 C  CA    . VAL   C 2 359 ? 101.133 126.793 116.550 1.00 59.57  ?  358  VAL   C CA    1 
ATOM   14867 C  C     . VAL   C 2 359 ? 100.369 128.023 116.082 1.00 65.04  ?  358  VAL   C C     1 
ATOM   14868 O  O     . VAL   C 2 359 ? 99.841  128.048 114.963 1.00 69.68  ?  358  VAL   C O     1 
ATOM   14869 C  CB    . VAL   C 2 359 ? 102.341 126.516 115.643 1.00 56.02  ?  358  VAL   C CB    1 
ATOM   14870 C  CG1   . VAL   C 2 359 ? 103.098 127.799 115.367 1.00 55.65  ?  358  VAL   C CG1   1 
ATOM   14871 C  CG2   . VAL   C 2 359 ? 103.249 125.474 116.275 1.00 54.56  ?  358  VAL   C CG2   1 
ATOM   14872 N  N     . GLY   C 2 360 ? 100.312 129.039 116.936 1.00 66.98  ?  359  GLY   C N     1 
ATOM   14873 C  CA    . GLY   C 2 360 ? 99.677  130.298 116.584 1.00 64.58  ?  359  GLY   C CA    1 
ATOM   14874 C  C     . GLY   C 2 360 ? 98.186  130.223 116.340 1.00 72.15  ?  359  GLY   C C     1 
ATOM   14875 O  O     . GLY   C 2 360 ? 97.668  130.944 115.478 1.00 78.57  ?  359  GLY   C O     1 
ATOM   14876 N  N     . GLN   C 2 361 ? 97.476  129.375 117.088 1.00 68.58  ?  360  GLN   C N     1 
ATOM   14877 C  CA    . GLN   C 2 361 ? 96.026  129.262 116.989 1.00 68.46  ?  360  GLN   C CA    1 
ATOM   14878 C  C     . GLN   C 2 361 ? 95.306  130.137 118.005 1.00 74.48  ?  360  GLN   C C     1 
ATOM   14879 O  O     . GLN   C 2 361 ? 94.224  129.772 118.481 1.00 76.40  ?  360  GLN   C O     1 
ATOM   14880 C  CB    . GLN   C 2 361 ? 95.598  127.800 117.133 1.00 60.11  ?  360  GLN   C CB    1 
ATOM   14881 C  CG    . GLN   C 2 361 ? 94.384  127.406 116.281 1.00 60.29  ?  360  GLN   C CG    1 
ATOM   14882 C  CD    . GLN   C 2 361 ? 94.456  127.874 114.838 1.00 69.26  ?  360  GLN   C CD    1 
ATOM   14883 O  OE1   . GLN   C 2 361 ? 95.529  127.963 114.246 1.00 82.79  ?  360  GLN   C OE1   1 
ATOM   14884 N  NE2   . GLN   C 2 361 ? 93.297  128.157 114.258 1.00 63.71  ?  360  GLN   C NE2   1 
ATOM   14885 N  N     . ILE   C 2 362 ? 95.884  131.285 118.350 1.00 76.43  ?  361  ILE   C N     1 
ATOM   14886 C  CA    . ILE   C 2 362 ? 95.339  132.193 119.351 1.00 68.35  ?  361  ILE   C CA    1 
ATOM   14887 C  C     . ILE   C 2 362 ? 94.856  133.456 118.654 1.00 73.41  ?  361  ILE   C C     1 
ATOM   14888 O  O     . ILE   C 2 362 ? 95.511  133.959 117.734 1.00 79.50  ?  361  ILE   C O     1 
ATOM   14889 C  CB    . ILE   C 2 362 ? 96.384  132.524 120.434 1.00 67.39  ?  361  ILE   C CB    1 
ATOM   14890 C  CG1   . ILE   C 2 362 ? 97.007  131.240 120.983 1.00 67.08  ?  361  ILE   C CG1   1 
ATOM   14891 C  CG2   . ILE   C 2 362 ? 95.763  133.340 121.554 1.00 67.01  ?  361  ILE   C CG2   1 
ATOM   14892 C  CD1   . ILE   C 2 362 ? 96.017  130.324 121.662 1.00 72.21  ?  361  ILE   C CD1   1 
ATOM   14893 N  N     . ASP   C 2 363 ? 93.696  133.960 119.084 1.00 85.47  ?  362  ASP   C N     1 
ATOM   14894 C  CA    . ASP   C 2 363 ? 93.141  135.166 118.481 1.00 84.00  ?  362  ASP   C CA    1 
ATOM   14895 C  C     . ASP   C 2 363 ? 94.004  136.390 118.762 1.00 86.75  ?  362  ASP   C C     1 
ATOM   14896 O  O     . ASP   C 2 363 ? 94.028  137.320 117.949 1.00 93.23  ?  362  ASP   C O     1 
ATOM   14897 C  CB    . ASP   C 2 363 ? 91.715  135.393 118.978 1.00 87.26  ?  362  ASP   C CB    1 
ATOM   14898 C  CG    . ASP   C 2 363 ? 90.975  136.446 118.179 1.00 96.16  ?  362  ASP   C CG    1 
ATOM   14899 O  OD1   . ASP   C 2 363 ? 91.227  137.650 118.392 1.00 96.02  ?  362  ASP   C OD1   1 
ATOM   14900 O  OD2   . ASP   C 2 363 ? 90.127  136.065 117.346 1.00 97.45  ?  362  ASP   C OD2   1 
ATOM   14901 N  N     . SER   C 2 364 ? 94.695  136.421 119.901 1.00 80.89  ?  363  SER   C N     1 
ATOM   14902 C  CA    . SER   C 2 364 ? 95.697  137.424 120.264 1.00 83.83  ?  363  SER   C CA    1 
ATOM   14903 C  C     . SER   C 2 364 ? 95.087  138.779 120.604 1.00 87.03  ?  363  SER   C C     1 
ATOM   14904 O  O     . SER   C 2 364 ? 95.829  139.700 120.957 1.00 88.61  ?  363  SER   C O     1 
ATOM   14905 C  CB    . SER   C 2 364 ? 96.770  137.625 119.179 1.00 78.72  ?  363  SER   C CB    1 
ATOM   14906 O  OG    . SER   C 2 364 ? 97.495  138.821 119.414 1.00 89.23  ?  363  SER   C OG    1 
ATOM   14907 N  N     . GLU   C 2 365 ? 93.768  138.935 120.519 1.00 101.80 ?  364  GLU   C N     1 
ATOM   14908 C  CA    . GLU   C 2 365 ? 93.125  140.193 120.879 1.00 98.19  ?  364  GLU   C CA    1 
ATOM   14909 C  C     . GLU   C 2 365 ? 92.958  140.266 122.392 1.00 101.63 ?  364  GLU   C C     1 
ATOM   14910 O  O     . GLU   C 2 365 ? 92.366  139.368 123.000 1.00 106.17 ?  364  GLU   C O     1 
ATOM   14911 C  CB    . GLU   C 2 365 ? 91.772  140.320 120.184 1.00 104.12 ?  364  GLU   C CB    1 
ATOM   14912 C  CG    . GLU   C 2 365 ? 91.268  141.744 120.051 1.00 104.42 ?  364  GLU   C CG    1 
ATOM   14913 C  CD    . GLU   C 2 365 ? 89.939  141.824 119.326 1.00 109.05 ?  364  GLU   C CD    1 
ATOM   14914 O  OE1   . GLU   C 2 365 ? 89.938  141.800 118.077 1.00 108.18 ?  364  GLU   C OE1   1 
ATOM   14915 O  OE2   . GLU   C 2 365 ? 88.894  141.911 120.005 1.00 107.59 ?  364  GLU   C OE2   1 
ATOM   14916 N  N     . VAL   C 2 366 ? 93.475  141.332 122.999 1.00 88.96  ?  365  VAL   C N     1 
ATOM   14917 C  CA    . VAL   C 2 366 ? 93.372  141.547 124.439 1.00 90.08  ?  365  VAL   C CA    1 
ATOM   14918 C  C     . VAL   C 2 366 ? 92.769  142.923 124.676 1.00 93.05  ?  365  VAL   C C     1 
ATOM   14919 O  O     . VAL   C 2 366 ? 93.284  143.926 124.168 1.00 97.16  ?  365  VAL   C O     1 
ATOM   14920 C  CB    . VAL   C 2 366 ? 94.732  141.433 125.143 1.00 86.16  ?  365  VAL   C CB    1 
ATOM   14921 C  CG1   . VAL   C 2 366 ? 94.582  141.756 126.622 1.00 88.96  ?  365  VAL   C CG1   1 
ATOM   14922 C  CG2   . VAL   C 2 366 ? 95.314  140.052 124.955 1.00 89.05  ?  365  VAL   C CG2   1 
ATOM   14923 N  N     . ASP   C 2 367 ? 91.674  142.969 125.429 1.00 106.07 ?  366  ASP   C N     1 
ATOM   14924 C  CA    . ASP   C 2 367 ? 91.023  144.219 125.806 1.00 106.18 ?  366  ASP   C CA    1 
ATOM   14925 C  C     . ASP   C 2 367 ? 91.345  144.489 127.270 1.00 108.04 ?  366  ASP   C C     1 
ATOM   14926 O  O     . ASP   C 2 367 ? 90.868  143.775 128.158 1.00 109.05 ?  366  ASP   C O     1 
ATOM   14927 C  CB    . ASP   C 2 367 ? 89.515  144.148 125.575 1.00 107.63 ?  366  ASP   C CB    1 
ATOM   14928 C  CG    . ASP   C 2 367 ? 88.780  145.339 126.157 1.00 112.36 ?  366  ASP   C CG    1 
ATOM   14929 O  OD1   . ASP   C 2 367 ? 89.003  146.471 125.681 1.00 110.72 ?  366  ASP   C OD1   1 
ATOM   14930 O  OD2   . ASP   C 2 367 ? 87.980  145.143 127.092 1.00 115.85 ?  366  ASP   C OD2   1 
ATOM   14931 N  N     . THR   C 2 368 ? 92.163  145.512 127.518 1.00 111.92 ?  367  THR   C N     1 
ATOM   14932 C  CA    . THR   C 2 368 ? 92.553  145.828 128.885 1.00 113.36 ?  367  THR   C CA    1 
ATOM   14933 C  C     . THR   C 2 368 ? 91.384  146.342 129.716 1.00 112.67 ?  367  THR   C C     1 
ATOM   14934 O  O     . THR   C 2 368 ? 91.483  146.373 130.946 1.00 113.72 ?  367  THR   C O     1 
ATOM   14935 C  CB    . THR   C 2 368 ? 93.689  146.859 128.880 1.00 114.54 ?  367  THR   C CB    1 
ATOM   14936 O  OG1   . THR   C 2 368 ? 93.410  147.887 127.919 1.00 115.09 ?  367  THR   C OG1   1 
ATOM   14937 C  CG2   . THR   C 2 368 ? 95.009  146.184 128.516 1.00 111.13 ?  367  THR   C CG2   1 
ATOM   14938 N  N     . ASP   C 2 369 ? 90.330  146.848 129.073 1.00 104.13 ?  368  ASP   C N     1 
ATOM   14939 C  CA    . ASP   C 2 369 ? 89.204  147.401 129.819 1.00 104.56 ?  368  ASP   C CA    1 
ATOM   14940 C  C     . ASP   C 2 369 ? 88.439  146.306 130.549 1.00 104.26 ?  368  ASP   C C     1 
ATOM   14941 O  O     . ASP   C 2 369 ? 88.045  146.485 131.707 1.00 105.85 ?  368  ASP   C O     1 
ATOM   14942 C  CB    . ASP   C 2 369 ? 88.279  148.177 128.883 1.00 106.40 ?  368  ASP   C CB    1 
ATOM   14943 C  CG    . ASP   C 2 369 ? 88.839  149.532 128.503 1.00 111.33 ?  368  ASP   C CG    1 
ATOM   14944 O  OD1   . ASP   C 2 369 ? 90.055  149.747 128.690 1.00 112.04 ?  368  ASP   C OD1   1 
ATOM   14945 O  OD2   . ASP   C 2 369 ? 88.061  150.382 128.021 1.00 111.16 ?  368  ASP   C OD2   1 
ATOM   14946 N  N     . ASP   C 2 370 ? 88.243  145.156 129.899 1.00 105.36 ?  369  ASP   C N     1 
ATOM   14947 C  CA    . ASP   C 2 370 ? 87.581  144.040 130.564 1.00 105.89 ?  369  ASP   C CA    1 
ATOM   14948 C  C     . ASP   C 2 370 ? 88.452  143.436 131.656 1.00 107.24 ?  369  ASP   C C     1 
ATOM   14949 O  O     . ASP   C 2 370 ? 87.928  142.972 132.674 1.00 107.96 ?  369  ASP   C O     1 
ATOM   14950 C  CB    . ASP   C 2 370 ? 87.192  142.972 129.545 1.00 105.85 ?  369  ASP   C CB    1 
ATOM   14951 C  CG    . ASP   C 2 370 ? 86.260  143.500 128.473 1.00 111.73 ?  369  ASP   C CG    1 
ATOM   14952 O  OD1   . ASP   C 2 370 ? 85.467  144.418 128.774 1.00 111.49 ?  369  ASP   C OD1   1 
ATOM   14953 O  OD2   . ASP   C 2 370 ? 86.321  143.004 127.328 1.00 111.78 ?  369  ASP   C OD2   1 
ATOM   14954 N  N     . LEU   C 2 371 ? 89.771  143.428 131.465 1.00 98.52  ?  370  LEU   C N     1 
ATOM   14955 C  CA    . LEU   C 2 371 ? 90.664  142.889 132.481 1.00 97.07  ?  370  LEU   C CA    1 
ATOM   14956 C  C     . LEU   C 2 371 ? 90.820  143.834 133.664 1.00 97.01  ?  370  LEU   C C     1 
ATOM   14957 O  O     . LEU   C 2 371 ? 91.092  143.376 134.779 1.00 99.89  ?  370  LEU   C O     1 
ATOM   14958 C  CB    . LEU   C 2 371 ? 92.029  142.578 131.868 1.00 96.37  ?  370  LEU   C CB    1 
ATOM   14959 C  CG    . LEU   C 2 371 ? 92.129  141.330 130.989 1.00 95.56  ?  370  LEU   C CG    1 
ATOM   14960 C  CD1   . LEU   C 2 371 ? 93.557  140.812 130.959 1.00 93.33  ?  370  LEU   C CD1   1 
ATOM   14961 C  CD2   . LEU   C 2 371 ? 91.172  140.249 131.467 1.00 93.74  ?  370  LEU   C CD2   1 
ATOM   14962 N  N     . SER   C 2 372 ? 90.657  145.142 133.444 1.00 96.64  ?  371  SER   C N     1 
ATOM   14963 C  CA    . SER   C 2 372 ? 90.793  146.099 134.535 1.00 95.66  ?  371  SER   C CA    1 
ATOM   14964 C  C     . SER   C 2 372 ? 89.736  145.866 135.607 1.00 98.52  ?  371  SER   C C     1 
ATOM   14965 O  O     . SER   C 2 372 ? 90.026  145.959 136.805 1.00 97.26  ?  371  SER   C O     1 
ATOM   14966 C  CB    . SER   C 2 372 ? 90.707  147.524 133.993 1.00 95.31  ?  371  SER   C CB    1 
ATOM   14967 O  OG    . SER   C 2 372 ? 89.364  147.974 133.947 1.00 98.97  ?  371  SER   C OG    1 
ATOM   14968 N  N     . ASN   C 2 373 ? 88.502  145.570 135.196 1.00 110.59 ?  372  ASN   C N     1 
ATOM   14969 C  CA    . ASN   C 2 373 ? 87.426  145.249 136.135 1.00 109.84 ?  372  ASN   C CA    1 
ATOM   14970 C  C     . ASN   C 2 373 ? 87.517  143.766 136.502 1.00 111.09 ?  372  ASN   C C     1 
ATOM   14971 O  O     . ASN   C 2 373 ? 86.718  142.924 136.087 1.00 113.52 ?  372  ASN   C O     1 
ATOM   14972 C  CB    . ASN   C 2 373 ? 86.068  145.606 135.547 1.00 110.95 ?  372  ASN   C CB    1 
ATOM   14973 C  CG    . ASN   C 2 373 ? 85.986  147.053 135.110 1.00 111.00 ?  372  ASN   C CG    1 
ATOM   14974 O  OD1   . ASN   C 2 373 ? 85.903  147.352 133.918 1.00 110.37 ?  372  ASN   C OD1   1 
ATOM   14975 N  ND2   . ASN   C 2 373 ? 86.010  147.961 136.076 1.00 110.54 ?  372  ASN   C ND2   1 
ATOM   14976 N  N     . PHE   C 2 374 ? 88.533  143.457 137.302 1.00 93.81  ?  373  PHE   C N     1 
ATOM   14977 C  CA    . PHE   C 2 374 ? 88.761  142.096 137.777 1.00 92.38  ?  373  PHE   C CA    1 
ATOM   14978 C  C     . PHE   C 2 374 ? 89.417  142.173 139.145 1.00 89.95  ?  373  PHE   C C     1 
ATOM   14979 O  O     . PHE   C 2 374 ? 90.475  142.792 139.290 1.00 91.57  ?  373  PHE   C O     1 
ATOM   14980 C  CB    . PHE   C 2 374 ? 89.637  141.307 136.801 1.00 89.39  ?  373  PHE   C CB    1 
ATOM   14981 C  CG    . PHE   C 2 374 ? 89.599  139.821 137.015 1.00 89.19  ?  373  PHE   C CG    1 
ATOM   14982 C  CD1   . PHE   C 2 374 ? 90.395  139.225 137.979 1.00 91.02  ?  373  PHE   C CD1   1 
ATOM   14983 C  CD2   . PHE   C 2 374 ? 88.773  139.019 136.248 1.00 87.79  ?  373  PHE   C CD2   1 
ATOM   14984 C  CE1   . PHE   C 2 374 ? 90.362  137.860 138.177 1.00 87.99  ?  373  PHE   C CE1   1 
ATOM   14985 C  CE2   . PHE   C 2 374 ? 88.737  137.651 136.441 1.00 89.77  ?  373  PHE   C CE2   1 
ATOM   14986 C  CZ    . PHE   C 2 374 ? 89.533  137.072 137.408 1.00 89.43  ?  373  PHE   C CZ    1 
ATOM   14987 N  N     . GLN   C 2 375 ? 88.793  141.551 140.140 1.00 97.83  ?  374  GLN   C N     1 
ATOM   14988 C  CA    . GLN   C 2 375 ? 89.298  141.556 141.506 1.00 100.10 ?  374  GLN   C CA    1 
ATOM   14989 C  C     . GLN   C 2 375 ? 90.123  140.296 141.735 1.00 104.04 ?  374  GLN   C C     1 
ATOM   14990 O  O     . GLN   C 2 375 ? 89.610  139.180 141.597 1.00 106.39 ?  374  GLN   C O     1 
ATOM   14991 C  CB    . GLN   C 2 375 ? 88.151  141.640 142.513 1.00 102.28 ?  374  GLN   C CB    1 
ATOM   14992 C  CG    . GLN   C 2 375 ? 87.347  142.931 142.446 1.00 102.51 ?  374  GLN   C CG    1 
ATOM   14993 C  CD    . GLN   C 2 375 ? 88.157  144.102 141.927 1.00 105.56 ?  374  GLN   C CD    1 
ATOM   14994 O  OE1   . GLN   C 2 375 ? 89.034  144.622 142.618 1.00 106.68 ?  374  GLN   C OE1   1 
ATOM   14995 N  NE2   . GLN   C 2 375 ? 87.864  144.528 140.704 1.00 104.64 ?  374  GLN   C NE2   1 
ATOM   14996 N  N     . LEU   C 2 376 ? 91.392  140.476 142.084 1.00 99.31  ?  375  LEU   C N     1 
ATOM   14997 C  CA    . LEU   C 2 376 ? 92.278  139.352 142.355 1.00 102.47 ?  375  LEU   C CA    1 
ATOM   14998 C  C     . LEU   C 2 376 ? 92.044  138.803 143.757 1.00 104.38 ?  375  LEU   C C     1 
ATOM   14999 O  O     . LEU   C 2 376 ? 92.472  137.697 144.084 1.00 102.29 ?  375  LEU   C O     1 
ATOM   15000 C  CB    . LEU   C 2 376 ? 93.740  139.769 142.189 1.00 99.08  ?  375  LEU   C CB    1 
ATOM   15001 C  CG    . LEU   C 2 376 ? 94.193  140.103 140.768 1.00 95.84  ?  375  LEU   C CG    1 
ATOM   15002 C  CD1   . LEU   C 2 376 ? 95.616  140.630 140.774 1.00 95.78  ?  375  LEU   C CD1   1 
ATOM   15003 C  CD2   . LEU   C 2 376 ? 94.073  138.883 139.871 1.00 95.63  ?  375  LEU   C CD2   1 
ATOM   15004 O  OXT   . LEU   C 2 376 ? 91.421  139.454 144.595 1.00 102.70 ?  375  LEU   C OXT   1 
ATOM   15005 N  N     . ALA   D 2 2   ? 112.724 116.993 77.878  1.00 93.21  ?  1    ALA   D N     1 
ATOM   15006 C  CA    . ALA   D 2 2   ? 111.431 117.000 78.552  1.00 90.38  ?  1    ALA   D CA    1 
ATOM   15007 C  C     . ALA   D 2 2   ? 111.606 116.977 80.064  1.00 89.74  ?  1    ALA   D C     1 
ATOM   15008 O  O     . ALA   D 2 2   ? 112.388 116.189 80.595  1.00 91.84  ?  1    ALA   D O     1 
ATOM   15009 C  CB    . ALA   D 2 2   ? 110.589 115.818 78.098  1.00 89.73  ?  1    ALA   D CB    1 
ATOM   15010 N  N     . TYR   D 2 3   ? 110.879 117.851 80.755  1.00 87.40  ?  2    TYR   D N     1 
ATOM   15011 C  CA    . TYR   D 2 3   ? 110.946 117.888 82.209  1.00 87.32  ?  2    TYR   D CA    1 
ATOM   15012 C  C     . TYR   D 2 3   ? 110.266 116.660 82.797  1.00 86.67  ?  2    TYR   D C     1 
ATOM   15013 O  O     . TYR   D 2 3   ? 109.161 116.292 82.388  1.00 85.74  ?  2    TYR   D O     1 
ATOM   15014 C  CB    . TYR   D 2 3   ? 110.291 119.160 82.744  1.00 78.51  ?  2    TYR   D CB    1 
ATOM   15015 C  CG    . TYR   D 2 3   ? 110.242 119.221 84.254  1.00 78.47  ?  2    TYR   D CG    1 
ATOM   15016 C  CD1   . TYR   D 2 3   ? 111.371 119.548 84.990  1.00 80.99  ?  2    TYR   D CD1   1 
ATOM   15017 C  CD2   . TYR   D 2 3   ? 109.070 118.946 84.943  1.00 79.62  ?  2    TYR   D CD2   1 
ATOM   15018 C  CE1   . TYR   D 2 3   ? 111.333 119.601 86.370  1.00 81.87  ?  2    TYR   D CE1   1 
ATOM   15019 C  CE2   . TYR   D 2 3   ? 109.024 118.996 86.323  1.00 81.80  ?  2    TYR   D CE2   1 
ATOM   15020 C  CZ    . TYR   D 2 3   ? 110.158 119.324 87.031  1.00 83.14  ?  2    TYR   D CZ    1 
ATOM   15021 O  OH    . TYR   D 2 3   ? 110.117 119.376 88.404  1.00 85.02  ?  2    TYR   D OH    1 
ATOM   15022 N  N     . THR   D 2 4   ? 110.931 116.024 83.756  1.00 77.16  ?  3    THR   D N     1 
ATOM   15023 C  CA    . THR   D 2 4   ? 110.381 114.879 84.467  1.00 73.14  ?  3    THR   D CA    1 
ATOM   15024 C  C     . THR   D 2 4   ? 110.434 115.158 85.961  1.00 75.38  ?  3    THR   D C     1 
ATOM   15025 O  O     . THR   D 2 4   ? 111.455 115.627 86.473  1.00 77.54  ?  3    THR   D O     1 
ATOM   15026 C  CB    . THR   D 2 4   ? 111.142 113.590 84.131  1.00 73.03  ?  3    THR   D CB    1 
ATOM   15027 O  OG1   . THR   D 2 4   ? 110.757 112.552 85.040  1.00 74.93  ?  3    THR   D OG1   1 
ATOM   15028 C  CG2   . THR   D 2 4   ? 112.647 113.809 84.215  1.00 73.99  ?  3    THR   D CG2   1 
ATOM   15029 N  N     . THR   D 2 5   ? 109.327 114.886 86.652  1.00 77.96  ?  4    THR   D N     1 
ATOM   15030 C  CA    . THR   D 2 5   ? 109.292 115.096 88.095  1.00 77.36  ?  4    THR   D CA    1 
ATOM   15031 C  C     . THR   D 2 5   ? 110.256 114.160 88.812  1.00 80.43  ?  4    THR   D C     1 
ATOM   15032 O  O     . THR   D 2 5   ? 110.933 114.566 89.763  1.00 84.56  ?  4    THR   D O     1 
ATOM   15033 C  CB    . THR   D 2 5   ? 107.870 114.910 88.621  1.00 78.89  ?  4    THR   D CB    1 
ATOM   15034 O  OG1   . THR   D 2 5   ? 107.282 113.754 88.013  1.00 80.91  ?  4    THR   D OG1   1 
ATOM   15035 C  CG2   . THR   D 2 5   ? 107.023 116.128 88.296  1.00 79.02  ?  4    THR   D CG2   1 
ATOM   15036 N  N     . PHE   D 2 6   ? 110.345 112.910 88.363  1.00 69.24  ?  5    PHE   D N     1 
ATOM   15037 C  CA    . PHE   D 2 6   ? 111.215 111.910 88.973  1.00 65.83  ?  5    PHE   D CA    1 
ATOM   15038 C  C     . PHE   D 2 6   ? 112.115 111.334 87.888  1.00 68.16  ?  5    PHE   D C     1 
ATOM   15039 O  O     . PHE   D 2 6   ? 111.661 110.548 87.051  1.00 75.40  ?  5    PHE   D O     1 
ATOM   15040 C  CB    . PHE   D 2 6   ? 110.389 110.818 89.657  1.00 68.35  ?  5    PHE   D CB    1 
ATOM   15041 C  CG    . PHE   D 2 6   ? 111.176 109.592 90.032  1.00 67.85  ?  5    PHE   D CG    1 
ATOM   15042 C  CD1   . PHE   D 2 6   ? 112.367 109.693 90.733  1.00 69.83  ?  5    PHE   D CD1   1 
ATOM   15043 C  CD2   . PHE   D 2 6   ? 110.734 108.336 89.655  1.00 71.09  ?  5    PHE   D CD2   1 
ATOM   15044 C  CE1   . PHE   D 2 6   ? 113.086 108.565 91.071  1.00 73.53  ?  5    PHE   D CE1   1 
ATOM   15045 C  CE2   . PHE   D 2 6   ? 111.444 107.204 90.000  1.00 72.40  ?  5    PHE   D CE2   1 
ATOM   15046 C  CZ    . PHE   D 2 6   ? 112.624 107.319 90.705  1.00 72.03  ?  5    PHE   D CZ    1 
ATOM   15047 N  N     . SER   D 2 7   ? 113.386 111.723 87.905  1.00 74.90  ?  6    SER   D N     1 
ATOM   15048 C  CA    . SER   D 2 7   ? 114.363 111.236 86.940  1.00 72.67  ?  6    SER   D CA    1 
ATOM   15049 C  C     . SER   D 2 7   ? 114.960 109.925 87.428  1.00 79.08  ?  6    SER   D C     1 
ATOM   15050 O  O     . SER   D 2 7   ? 115.454 109.840 88.557  1.00 83.76  ?  6    SER   D O     1 
ATOM   15051 C  CB    . SER   D 2 7   ? 115.466 112.269 86.721  1.00 74.39  ?  6    SER   D CB    1 
ATOM   15052 O  OG    . SER   D 2 7   ? 115.956 112.763 87.956  1.00 76.16  ?  6    SER   D OG    1 
ATOM   15053 N  N     . GLN   D 2 8   ? 114.894 108.901 86.577  1.00 84.04  ?  7    GLN   D N     1 
ATOM   15054 C  CA    . GLN   D 2 8   ? 115.253 107.548 86.977  1.00 82.70  ?  7    GLN   D CA    1 
ATOM   15055 C  C     . GLN   D 2 8   ? 116.754 107.340 87.098  1.00 85.66  ?  7    GLN   D C     1 
ATOM   15056 O  O     . GLN   D 2 8   ? 117.177 106.358 87.715  1.00 88.20  ?  7    GLN   D O     1 
ATOM   15057 C  CB    . GLN   D 2 8   ? 114.682 106.539 85.980  1.00 82.85  ?  7    GLN   D CB    1 
ATOM   15058 C  CG    . GLN   D 2 8   ? 113.184 106.647 85.756  1.00 86.01  ?  7    GLN   D CG    1 
ATOM   15059 C  CD    . GLN   D 2 8   ? 112.376 106.096 86.913  1.00 91.58  ?  7    GLN   D CD    1 
ATOM   15060 O  OE1   . GLN   D 2 8   ? 112.928 105.554 87.868  1.00 91.04  ?  7    GLN   D OE1   1 
ATOM   15061 N  NE2   . GLN   D 2 8   ? 111.058 106.229 86.829  1.00 89.78  ?  7    GLN   D NE2   1 
ATOM   15062 N  N     . THR   D 2 9   ? 117.564 108.225 86.522  1.00 84.24  ?  8    THR   D N     1 
ATOM   15063 C  CA    . THR   D 2 9   ? 119.011 108.067 86.560  1.00 80.42  ?  8    THR   D CA    1 
ATOM   15064 C  C     . THR   D 2 9   ? 119.552 108.481 87.922  1.00 84.67  ?  8    THR   D C     1 
ATOM   15065 O  O     . THR   D 2 9   ? 119.265 109.580 88.405  1.00 91.46  ?  8    THR   D O     1 
ATOM   15066 C  CB    . THR   D 2 9   ? 119.669 108.895 85.458  1.00 84.19  ?  8    THR   D CB    1 
ATOM   15067 O  OG1   . THR   D 2 9   ? 119.488 108.243 84.196  1.00 89.15  ?  8    THR   D OG1   1 
ATOM   15068 C  CG2   . THR   D 2 9   ? 121.159 109.056 85.723  1.00 84.32  ?  8    THR   D CG2   1 
ATOM   15069 N  N     . LYS   D 2 10  ? 120.322 107.591 88.550  1.00 91.72  ?  9    LYS   D N     1 
ATOM   15070 C  CA    . LYS   D 2 10  ? 120.905 107.858 89.865  1.00 94.72  ?  9    LYS   D CA    1 
ATOM   15071 C  C     . LYS   D 2 10  ? 122.187 108.661 89.673  1.00 95.18  ?  9    LYS   D C     1 
ATOM   15072 O  O     . LYS   D 2 10  ? 123.307 108.156 89.782  1.00 94.59  ?  9    LYS   D O     1 
ATOM   15073 C  CB    . LYS   D 2 10  ? 121.164 106.559 90.618  1.00 94.08  ?  9    LYS   D CB    1 
ATOM   15074 C  CG    . LYS   D 2 10  ? 121.528 106.758 92.081  1.00 94.14  ?  9    LYS   D CG    1 
ATOM   15075 C  CD    . LYS   D 2 10  ? 122.168 105.513 92.669  1.00 94.31  ?  9    LYS   D CD    1 
ATOM   15076 C  CE    . LYS   D 2 10  ? 123.617 105.381 92.236  1.00 94.21  ?  9    LYS   D CE    1 
ATOM   15077 N  NZ    . LYS   D 2 10  ? 124.263 104.175 92.824  1.00 95.18  ?  9    LYS   D NZ    1 
ATOM   15078 N  N     . ASN   D 2 11  ? 122.009 109.945 89.378  1.00 88.39  ?  10   ASN   D N     1 
ATOM   15079 C  CA    . ASN   D 2 11  ? 123.130 110.847 89.182  1.00 85.15  ?  10   ASN   D CA    1 
ATOM   15080 C  C     . ASN   D 2 11  ? 123.754 111.225 90.523  1.00 88.02  ?  10   ASN   D C     1 
ATOM   15081 O  O     . ASN   D 2 11  ? 123.183 111.004 91.594  1.00 88.94  ?  10   ASN   D O     1 
ATOM   15082 C  CB    . ASN   D 2 11  ? 122.682 112.100 88.433  1.00 87.09  ?  10   ASN   D CB    1 
ATOM   15083 C  CG    . ASN   D 2 11  ? 121.695 112.931 89.229  1.00 87.95  ?  10   ASN   D CG    1 
ATOM   15084 O  OD1   . ASN   D 2 11  ? 120.936 112.404 90.042  1.00 89.06  ?  10   ASN   D OD1   1 
ATOM   15085 N  ND2   . ASN   D 2 11  ? 121.699 114.236 88.998  1.00 87.12  ?  10   ASN   D ND2   1 
ATOM   15086 N  N     . ASP   D 2 12  ? 124.952 111.800 90.454  1.00 101.25 ?  11   ASP   D N     1 
ATOM   15087 C  CA    . ASP   D 2 12  ? 125.642 112.306 91.635  1.00 99.22  ?  11   ASP   D CA    1 
ATOM   15088 C  C     . ASP   D 2 12  ? 125.281 113.777 91.802  1.00 100.86 ?  11   ASP   D C     1 
ATOM   15089 O  O     . ASP   D 2 12  ? 125.744 114.630 91.038  1.00 103.36 ?  11   ASP   D O     1 
ATOM   15090 C  CB    . ASP   D 2 12  ? 127.150 112.116 91.508  1.00 102.14 ?  11   ASP   D CB    1 
ATOM   15091 C  CG    . ASP   D 2 12  ? 127.890 112.468 92.783  1.00 106.54 ?  11   ASP   D CG    1 
ATOM   15092 O  OD1   . ASP   D 2 12  ? 127.251 112.494 93.855  1.00 109.94 ?  11   ASP   D OD1   1 
ATOM   15093 O  OD2   . ASP   D 2 12  ? 129.112 112.714 92.716  1.00 107.53 ?  11   ASP   D OD2   1 
ATOM   15094 N  N     . GLN   D 2 13  ? 124.450 114.073 92.802  1.00 88.00  ?  12   GLN   D N     1 
ATOM   15095 C  CA    . GLN   D 2 13  ? 123.943 115.424 92.993  1.00 86.78  ?  12   GLN   D CA    1 
ATOM   15096 C  C     . GLN   D 2 13  ? 124.981 116.374 93.574  1.00 86.40  ?  12   GLN   D C     1 
ATOM   15097 O  O     . GLN   D 2 13  ? 124.731 117.583 93.615  1.00 90.02  ?  12   GLN   D O     1 
ATOM   15098 C  CB    . GLN   D 2 13  ? 122.708 115.384 93.891  1.00 89.31  ?  12   GLN   D CB    1 
ATOM   15099 C  CG    . GLN   D 2 13  ? 121.659 114.385 93.434  1.00 89.21  ?  12   GLN   D CG    1 
ATOM   15100 C  CD    . GLN   D 2 13  ? 120.464 114.321 94.355  1.00 85.23  ?  12   GLN   D CD    1 
ATOM   15101 O  OE1   . GLN   D 2 13  ? 120.595 114.025 95.541  1.00 88.29  ?  12   GLN   D OE1   1 
ATOM   15102 N  NE2   . GLN   D 2 13  ? 119.288 114.601 93.813  1.00 85.93  ?  12   GLN   D NE2   1 
ATOM   15103 N  N     . LEU   D 2 14  ? 126.128 115.866 94.018  1.00 88.19  ?  13   LEU   D N     1 
ATOM   15104 C  CA    . LEU   D 2 14  ? 127.179 116.723 94.544  1.00 90.09  ?  13   LEU   D CA    1 
ATOM   15105 C  C     . LEU   D 2 14  ? 128.007 117.389 93.455  1.00 92.32  ?  13   LEU   D C     1 
ATOM   15106 O  O     . LEU   D 2 14  ? 128.771 118.310 93.763  1.00 94.03  ?  13   LEU   D O     1 
ATOM   15107 C  CB    . LEU   D 2 14  ? 128.094 115.915 95.466  1.00 89.99  ?  13   LEU   D CB    1 
ATOM   15108 C  CG    . LEU   D 2 14  ? 127.666 115.777 96.929  1.00 90.37  ?  13   LEU   D CG    1 
ATOM   15109 C  CD1   . LEU   D 2 14  ? 128.856 115.428 97.808  1.00 90.79  ?  13   LEU   D CD1   1 
ATOM   15110 C  CD2   . LEU   D 2 14  ? 126.989 117.046 97.419  1.00 89.69  ?  13   LEU   D CD2   1 
ATOM   15111 N  N     . LYS   D 2 15  ? 127.883 116.946 92.204  1.00 89.77  ?  14   LYS   D N     1 
ATOM   15112 C  CA    . LYS   D 2 15  ? 128.609 117.524 91.083  1.00 89.72  ?  14   LYS   D CA    1 
ATOM   15113 C  C     . LYS   D 2 15  ? 127.692 118.129 90.032  1.00 89.22  ?  14   LYS   D C     1 
ATOM   15114 O  O     . LYS   D 2 15  ? 128.186 118.651 89.027  1.00 90.26  ?  14   LYS   D O     1 
ATOM   15115 C  CB    . LYS   D 2 15  ? 129.500 116.464 90.427  1.00 89.74  ?  14   LYS   D CB    1 
ATOM   15116 C  CG    . LYS   D 2 15  ? 130.082 115.469 91.410  1.00 88.05  ?  14   LYS   D CG    1 
ATOM   15117 C  CD    . LYS   D 2 15  ? 131.235 114.703 90.807  1.00 90.82  ?  14   LYS   D CD    1 
ATOM   15118 C  CE    . LYS   D 2 15  ? 132.494 115.544 90.853  1.00 92.68  ?  14   LYS   D CE    1 
ATOM   15119 N  NZ    . LYS   D 2 15  ? 132.724 116.110 92.212  1.00 92.66  ?  14   LYS   D NZ    1 
ATOM   15120 N  N     . GLU   D 2 16  ? 126.381 118.058 90.221  1.00 87.00  ?  15   GLU   D N     1 
ATOM   15121 C  CA    . GLU   D 2 16  ? 125.456 118.632 89.263  1.00 85.71  ?  15   GLU   D CA    1 
ATOM   15122 C  C     . GLU   D 2 16  ? 125.523 120.160 89.307  1.00 86.95  ?  15   GLU   D C     1 
ATOM   15123 O  O     . GLU   D 2 16  ? 125.832 120.748 90.346  1.00 88.87  ?  15   GLU   D O     1 
ATOM   15124 C  CB    . GLU   D 2 16  ? 124.037 118.155 89.555  1.00 85.35  ?  15   GLU   D CB    1 
ATOM   15125 C  CG    . GLU   D 2 16  ? 123.717 116.794 88.952  1.00 89.71  ?  15   GLU   D CG    1 
ATOM   15126 C  CD    . GLU   D 2 16  ? 123.373 116.848 87.479  1.00 93.22  ?  15   GLU   D CD    1 
ATOM   15127 O  OE1   . GLU   D 2 16  ? 122.952 117.918 87.002  1.00 91.86  ?  15   GLU   D OE1   1 
ATOM   15128 O  OE2   . GLU   D 2 16  ? 123.522 115.808 86.803  1.00 91.03  ?  15   GLU   D OE2   1 
ATOM   15129 N  N     . PRO   D 2 17  ? 125.253 120.828 88.190  1.00 72.45  ?  16   PRO   D N     1 
ATOM   15130 C  CA    . PRO   D 2 17  ? 125.173 122.292 88.212  1.00 69.15  ?  16   PRO   D CA    1 
ATOM   15131 C  C     . PRO   D 2 17  ? 123.947 122.759 88.982  1.00 73.93  ?  16   PRO   D C     1 
ATOM   15132 O  O     . PRO   D 2 17  ? 123.029 121.996 89.281  1.00 78.55  ?  16   PRO   D O     1 
ATOM   15133 C  CB    . PRO   D 2 17  ? 125.081 122.665 86.733  1.00 68.02  ?  16   PRO   D CB    1 
ATOM   15134 C  CG    . PRO   D 2 17  ? 124.482 121.461 86.091  1.00 69.02  ?  16   PRO   D CG    1 
ATOM   15135 C  CD    . PRO   D 2 17  ? 125.071 120.295 86.830  1.00 72.11  ?  16   PRO   D CD    1 
ATOM   15136 N  N     . MET   D 2 18  ? 123.952 124.050 89.316  1.00 81.71  ?  17   MET   D N     1 
ATOM   15137 C  CA    . MET   D 2 18  ? 122.820 124.644 90.020  1.00 76.52  ?  17   MET   D CA    1 
ATOM   15138 C  C     . MET   D 2 18  ? 121.545 124.551 89.192  1.00 79.52  ?  17   MET   D C     1 
ATOM   15139 O  O     . MET   D 2 18  ? 120.521 124.046 89.666  1.00 79.91  ?  17   MET   D O     1 
ATOM   15140 C  CB    . MET   D 2 18  ? 123.142 126.093 90.364  1.00 78.98  ?  17   MET   D CB    1 
ATOM   15141 C  CG    . MET   D 2 18  ? 123.235 126.393 91.835  1.00 79.77  ?  17   MET   D CG    1 
ATOM   15142 S  SD    . MET   D 2 18  ? 123.703 128.108 92.121  1.00 94.64  ?  17   MET   D SD    1 
ATOM   15143 C  CE    . MET   D 2 18  ? 123.784 128.121 93.902  1.00 85.92  ?  17   MET   D CE    1 
ATOM   15144 N  N     . PHE   D 2 19  ? 121.618 124.944 87.922  1.00 63.54  ?  18   PHE   D N     1 
ATOM   15145 C  CA    . PHE   D 2 19  ? 120.481 124.908 87.020  1.00 60.12  ?  18   PHE   D CA    1 
ATOM   15146 C  C     . PHE   D 2 19  ? 120.848 124.147 85.753  1.00 60.44  ?  18   PHE   D C     1 
ATOM   15147 O  O     . PHE   D 2 19  ? 122.023 123.930 85.447  1.00 66.56  ?  18   PHE   D O     1 
ATOM   15148 C  CB    . PHE   D 2 19  ? 120.013 126.320 86.654  1.00 60.54  ?  18   PHE   D CB    1 
ATOM   15149 C  CG    . PHE   D 2 19  ? 119.710 127.192 87.839  1.00 59.83  ?  18   PHE   D CG    1 
ATOM   15150 C  CD1   . PHE   D 2 19  ? 118.445 127.203 88.401  1.00 59.47  ?  18   PHE   D CD1   1 
ATOM   15151 C  CD2   . PHE   D 2 19  ? 120.685 128.014 88.378  1.00 61.92  ?  18   PHE   D CD2   1 
ATOM   15152 C  CE1   . PHE   D 2 19  ? 118.161 128.011 89.486  1.00 61.18  ?  18   PHE   D CE1   1 
ATOM   15153 C  CE2   . PHE   D 2 19  ? 120.405 128.824 89.463  1.00 61.74  ?  18   PHE   D CE2   1 
ATOM   15154 C  CZ    . PHE   D 2 19  ? 119.142 128.823 90.016  1.00 59.62  ?  18   PHE   D CZ    1 
ATOM   15155 N  N     . PHE   D 2 20  ? 119.809 123.733 85.028  1.00 66.61  ?  19   PHE   D N     1 
ATOM   15156 C  CA    . PHE   D 2 20  ? 119.910 123.154 83.692  1.00 62.48  ?  19   PHE   D CA    1 
ATOM   15157 C  C     . PHE   D 2 20  ? 120.623 121.809 83.671  1.00 69.37  ?  19   PHE   D C     1 
ATOM   15158 O  O     . PHE   D 2 20  ? 121.079 121.367 82.613  1.00 74.27  ?  19   PHE   D O     1 
ATOM   15159 C  CB    . PHE   D 2 20  ? 120.588 124.130 82.727  1.00 60.07  ?  19   PHE   D CB    1 
ATOM   15160 C  CG    . PHE   D 2 20  ? 120.033 125.518 82.795  1.00 66.37  ?  19   PHE   D CG    1 
ATOM   15161 C  CD1   . PHE   D 2 20  ? 118.730 125.770 82.412  1.00 67.85  ?  19   PHE   D CD1   1 
ATOM   15162 C  CD2   . PHE   D 2 20  ? 120.815 126.573 83.227  1.00 67.78  ?  19   PHE   D CD2   1 
ATOM   15163 C  CE1   . PHE   D 2 20  ? 118.210 127.045 82.475  1.00 70.28  ?  19   PHE   D CE1   1 
ATOM   15164 C  CE2   . PHE   D 2 20  ? 120.296 127.848 83.301  1.00 69.11  ?  19   PHE   D CE2   1 
ATOM   15165 C  CZ    . PHE   D 2 20  ? 118.995 128.085 82.918  1.00 69.04  ?  19   PHE   D CZ    1 
ATOM   15166 N  N     . GLY   D 2 21  ? 120.724 121.142 84.813  1.00 79.30  ?  20   GLY   D N     1 
ATOM   15167 C  CA    . GLY   D 2 21  ? 121.239 119.792 84.880  1.00 74.84  ?  20   GLY   D CA    1 
ATOM   15168 C  C     . GLY   D 2 21  ? 120.120 118.774 84.846  1.00 76.48  ?  20   GLY   D C     1 
ATOM   15169 O  O     . GLY   D 2 21  ? 119.012 119.041 84.374  1.00 80.16  ?  20   GLY   D O     1 
ATOM   15170 N  N     . GLN   D 2 22  ? 120.419 117.588 85.351  1.00 80.13  ?  21   GLN   D N     1 
ATOM   15171 C  CA    . GLN   D 2 22  ? 119.393 116.562 85.475  1.00 78.80  ?  21   GLN   D CA    1 
ATOM   15172 C  C     . GLN   D 2 22  ? 118.384 116.982 86.538  1.00 85.10  ?  21   GLN   D C     1 
ATOM   15173 O  O     . GLN   D 2 22  ? 118.784 117.411 87.626  1.00 90.27  ?  21   GLN   D O     1 
ATOM   15174 C  CB    . GLN   D 2 22  ? 120.018 115.217 85.837  1.00 79.23  ?  21   GLN   D CB    1 
ATOM   15175 C  CG    . GLN   D 2 22  ? 119.084 114.282 86.582  1.00 78.35  ?  21   GLN   D CG    1 
ATOM   15176 C  CD    . GLN   D 2 22  ? 119.506 112.832 86.482  1.00 79.28  ?  21   GLN   D CD    1 
ATOM   15177 O  OE1   . GLN   D 2 22  ? 120.303 112.463 85.621  1.00 83.61  ?  21   GLN   D OE1   1 
ATOM   15178 N  NE2   . GLN   D 2 22  ? 118.973 111.999 87.367  1.00 81.16  ?  21   GLN   D NE2   1 
ATOM   15179 N  N     . PRO   D 2 23  ? 117.083 116.890 86.264  1.00 69.29  ?  22   PRO   D N     1 
ATOM   15180 C  CA    . PRO   D 2 23  ? 116.090 117.268 87.277  1.00 66.64  ?  22   PRO   D CA    1 
ATOM   15181 C  C     . PRO   D 2 23  ? 116.231 116.426 88.536  1.00 70.55  ?  22   PRO   D C     1 
ATOM   15182 O  O     . PRO   D 2 23  ? 116.520 115.230 88.477  1.00 79.55  ?  22   PRO   D O     1 
ATOM   15183 C  CB    . PRO   D 2 23  ? 114.752 117.013 86.576  1.00 67.25  ?  22   PRO   D CB    1 
ATOM   15184 C  CG    . PRO   D 2 23  ? 115.069 117.009 85.119  1.00 68.36  ?  22   PRO   D CG    1 
ATOM   15185 C  CD    . PRO   D 2 23  ? 116.458 116.472 84.999  1.00 66.42  ?  22   PRO   D CD    1 
ATOM   15186 N  N     . VAL   D 2 24  ? 116.022 117.070 89.686  1.00 60.75  ?  23   VAL   D N     1 
ATOM   15187 C  CA    . VAL   D 2 24  ? 116.195 116.396 90.966  1.00 61.93  ?  23   VAL   D CA    1 
ATOM   15188 C  C     . VAL   D 2 24  ? 115.173 115.279 91.107  1.00 71.11  ?  23   VAL   D C     1 
ATOM   15189 O  O     . VAL   D 2 24  ? 114.006 115.423 90.721  1.00 77.55  ?  23   VAL   D O     1 
ATOM   15190 C  CB    . VAL   D 2 24  ? 116.077 117.401 92.123  1.00 59.78  ?  23   VAL   D CB    1 
ATOM   15191 C  CG1   . VAL   D 2 24  ? 116.624 116.801 93.406  1.00 63.39  ?  23   VAL   D CG1   1 
ATOM   15192 C  CG2   . VAL   D 2 24  ? 116.790 118.693 91.782  1.00 61.18  ?  23   VAL   D CG2   1 
ATOM   15193 N  N     . ASN   D 2 25  ? 115.618 114.142 91.639  1.00 73.23  ?  24   ASN   D N     1 
ATOM   15194 C  CA    . ASN   D 2 25  ? 114.747 113.000 91.885  1.00 75.87  ?  24   ASN   D CA    1 
ATOM   15195 C  C     . ASN   D 2 25  ? 114.491 112.766 93.366  1.00 77.88  ?  24   ASN   D C     1 
ATOM   15196 O  O     . ASN   D 2 25  ? 113.335 112.632 93.777  1.00 87.28  ?  24   ASN   D O     1 
ATOM   15197 C  CB    . ASN   D 2 25  ? 115.335 111.731 91.250  1.00 73.83  ?  24   ASN   D CB    1 
ATOM   15198 C  CG    . ASN   D 2 25  ? 116.833 111.616 91.448  1.00 75.02  ?  24   ASN   D CG    1 
ATOM   15199 O  OD1   . ASN   D 2 25  ? 117.358 111.935 92.513  1.00 82.52  ?  24   ASN   D OD1   1 
ATOM   15200 N  ND2   . ASN   D 2 25  ? 117.530 111.152 90.419  1.00 72.53  ?  24   ASN   D ND2   1 
ATOM   15201 N  N     . VAL   D 2 26  ? 115.539 112.722 94.184  1.00 66.40  ?  25   VAL   D N     1 
ATOM   15202 C  CA    . VAL   D 2 26  ? 115.410 112.508 95.619  1.00 69.43  ?  25   VAL   D CA    1 
ATOM   15203 C  C     . VAL   D 2 26  ? 116.076 113.669 96.344  1.00 69.09  ?  25   VAL   D C     1 
ATOM   15204 O  O     . VAL   D 2 26  ? 117.104 114.188 95.896  1.00 74.02  ?  25   VAL   D O     1 
ATOM   15205 C  CB    . VAL   D 2 26  ? 116.010 111.150 96.051  1.00 64.89  ?  25   VAL   D CB    1 
ATOM   15206 C  CG1   . VAL   D 2 26  ? 117.528 111.163 95.983  1.00 68.77  ?  25   VAL   D CG1   1 
ATOM   15207 C  CG2   . VAL   D 2 26  ? 115.528 110.773 97.439  1.00 59.99  ?  25   VAL   D CG2   1 
ATOM   15208 N  N     . ALA   D 2 27  ? 115.485 114.078 97.464  1.00 68.74  ?  26   ALA   D N     1 
ATOM   15209 C  CA    . ALA   D 2 27  ? 116.002 115.186 98.254  1.00 69.63  ?  26   ALA   D CA    1 
ATOM   15210 C  C     . ALA   D 2 27  ? 117.011 114.670 99.271  1.00 76.95  ?  26   ALA   D C     1 
ATOM   15211 O  O     . ALA   D 2 27  ? 116.735 113.711 100.000 1.00 77.40  ?  26   ALA   D O     1 
ATOM   15212 C  CB    . ALA   D 2 27  ? 114.863 115.920 98.961  1.00 69.60  ?  26   ALA   D CB    1 
ATOM   15213 N  N     . ARG   D 2 28  ? 118.176 115.307 99.317  1.00 80.76  ?  27   ARG   D N     1 
ATOM   15214 C  CA    . ARG   D 2 28  ? 119.248 114.929 100.226 1.00 76.29  ?  27   ARG   D CA    1 
ATOM   15215 C  C     . ARG   D 2 28  ? 119.482 116.050 101.228 1.00 75.66  ?  27   ARG   D C     1 
ATOM   15216 O  O     . ARG   D 2 28  ? 119.682 117.206 100.839 1.00 74.60  ?  27   ARG   D O     1 
ATOM   15217 C  CB    . ARG   D 2 28  ? 120.537 114.627 99.458  1.00 75.80  ?  27   ARG   D CB    1 
ATOM   15218 C  CG    . ARG   D 2 28  ? 120.570 113.249 98.812  1.00 75.48  ?  27   ARG   D CG    1 
ATOM   15219 C  CD    . ARG   D 2 28  ? 120.544 112.157 99.862  1.00 73.37  ?  27   ARG   D CD    1 
ATOM   15220 N  NE    . ARG   D 2 28  ? 121.871 111.861 100.388 1.00 75.17  ?  27   ARG   D NE    1 
ATOM   15221 C  CZ    . ARG   D 2 28  ? 122.784 111.133 99.759  1.00 78.32  ?  27   ARG   D CZ    1 
ATOM   15222 N  NH1   . ARG   D 2 28  ? 122.549 110.607 98.568  1.00 80.13  ?  27   ARG   D NH1   1 
ATOM   15223 N  NH2   . ARG   D 2 28  ? 123.962 110.926 100.339 1.00 77.96  ?  27   ARG   D NH2   1 
ATOM   15224 N  N     . TYR   D 2 29  ? 119.453 115.705 102.516 1.00 70.86  ?  28   TYR   D N     1 
ATOM   15225 C  CA    . TYR   D 2 29  ? 119.726 116.659 103.579 1.00 71.19  ?  28   TYR   D CA    1 
ATOM   15226 C  C     . TYR   D 2 29  ? 121.025 116.385 104.318 1.00 74.07  ?  28   TYR   D C     1 
ATOM   15227 O  O     . TYR   D 2 29  ? 121.523 117.280 105.009 1.00 80.69  ?  28   TYR   D O     1 
ATOM   15228 C  CB    . TYR   D 2 29  ? 118.571 116.676 104.591 1.00 71.29  ?  28   TYR   D CB    1 
ATOM   15229 C  CG    . TYR   D 2 29  ? 117.256 117.127 103.999 1.00 71.01  ?  28   TYR   D CG    1 
ATOM   15230 C  CD1   . TYR   D 2 29  ? 116.899 118.467 103.993 1.00 72.74  ?  28   TYR   D CD1   1 
ATOM   15231 C  CD2   . TYR   D 2 29  ? 116.375 116.213 103.439 1.00 68.86  ?  28   TYR   D CD2   1 
ATOM   15232 C  CE1   . TYR   D 2 29  ? 115.699 118.882 103.451 1.00 69.60  ?  28   TYR   D CE1   1 
ATOM   15233 C  CE2   . TYR   D 2 29  ? 115.175 116.620 102.893 1.00 70.21  ?  28   TYR   D CE2   1 
ATOM   15234 C  CZ    . TYR   D 2 29  ? 114.842 117.955 102.900 1.00 73.91  ?  28   TYR   D CZ    1 
ATOM   15235 O  OH    . TYR   D 2 29  ? 113.646 118.365 102.358 1.00 79.41  ?  28   TYR   D OH    1 
ATOM   15236 N  N     . ASP   D 2 30  ? 121.585 115.183 104.190 1.00 75.23  ?  29   ASP   D N     1 
ATOM   15237 C  CA    . ASP   D 2 30  ? 122.834 114.849 104.856 1.00 74.25  ?  29   ASP   D CA    1 
ATOM   15238 C  C     . ASP   D 2 30  ? 124.058 115.384 104.134 1.00 79.44  ?  29   ASP   D C     1 
ATOM   15239 O  O     . ASP   D 2 30  ? 125.137 115.410 104.736 1.00 84.51  ?  29   ASP   D O     1 
ATOM   15240 C  CB    . ASP   D 2 30  ? 122.955 113.334 105.007 1.00 78.03  ?  29   ASP   D CB    1 
ATOM   15241 C  CG    . ASP   D 2 30  ? 123.050 112.622 103.672 1.00 84.12  ?  29   ASP   D CG    1 
ATOM   15242 O  OD1   . ASP   D 2 30  ? 122.227 112.921 102.781 1.00 85.69  ?  29   ASP   D OD1   1 
ATOM   15243 O  OD2   . ASP   D 2 30  ? 123.947 111.769 103.506 1.00 86.04  ?  29   ASP   D OD2   1 
ATOM   15244 N  N     . GLN   D 2 31  ? 123.919 115.812 102.880 1.00 75.78  ?  30   GLN   D N     1 
ATOM   15245 C  CA    . GLN   D 2 31  ? 125.029 116.357 102.117 1.00 72.39  ?  30   GLN   D CA    1 
ATOM   15246 C  C     . GLN   D 2 31  ? 124.486 117.369 101.123 1.00 75.59  ?  30   GLN   D C     1 
ATOM   15247 O  O     . GLN   D 2 31  ? 123.442 117.146 100.505 1.00 81.74  ?  30   GLN   D O     1 
ATOM   15248 C  CB    . GLN   D 2 31  ? 125.801 115.255 101.389 1.00 71.40  ?  30   GLN   D CB    1 
ATOM   15249 C  CG    . GLN   D 2 31  ? 124.915 114.239 100.694 1.00 74.61  ?  30   GLN   D CG    1 
ATOM   15250 C  CD    . GLN   D 2 31  ? 125.577 113.637 99.471  1.00 80.22  ?  30   GLN   D CD    1 
ATOM   15251 O  OE1   . GLN   D 2 31  ? 126.597 112.957 99.576  1.00 83.13  ?  30   GLN   D OE1   1 
ATOM   15252 N  NE2   . GLN   D 2 31  ? 125.003 113.889 98.301  1.00 79.64  ?  30   GLN   D NE2   1 
ATOM   15253 N  N     . GLN   D 2 32  ? 125.202 118.478 100.975 1.00 79.20  ?  31   GLN   D N     1 
ATOM   15254 C  CA    . GLN   D 2 32  ? 124.812 119.535 100.057 1.00 75.81  ?  31   GLN   D CA    1 
ATOM   15255 C  C     . GLN   D 2 32  ? 126.030 120.000 99.278  1.00 78.97  ?  31   GLN   D C     1 
ATOM   15256 O  O     . GLN   D 2 32  ? 127.131 120.087 99.828  1.00 87.03  ?  31   GLN   D O     1 
ATOM   15257 C  CB    . GLN   D 2 32  ? 124.187 120.723 100.801 1.00 79.62  ?  31   GLN   D CB    1 
ATOM   15258 C  CG    . GLN   D 2 32  ? 122.893 120.398 101.525 1.00 86.01  ?  31   GLN   D CG    1 
ATOM   15259 C  CD    . GLN   D 2 32  ? 123.123 119.983 102.964 1.00 87.90  ?  31   GLN   D CD    1 
ATOM   15260 O  OE1   . GLN   D 2 32  ? 124.200 120.195 103.518 1.00 87.48  ?  31   GLN   D OE1   1 
ATOM   15261 N  NE2   . GLN   D 2 32  ? 122.109 119.384 103.576 1.00 86.97  ?  31   GLN   D NE2   1 
ATOM   15262 N  N     . LYS   D 2 33  ? 125.828 120.290 97.992  1.00 71.59  ?  32   LYS   D N     1 
ATOM   15263 C  CA    . LYS   D 2 33  ? 126.877 120.942 97.218  1.00 71.82  ?  32   LYS   D CA    1 
ATOM   15264 C  C     . LYS   D 2 33  ? 127.163 122.333 97.766  1.00 73.54  ?  32   LYS   D C     1 
ATOM   15265 O  O     . LYS   D 2 33  ? 128.323 122.753 97.850  1.00 74.08  ?  32   LYS   D O     1 
ATOM   15266 C  CB    . LYS   D 2 33  ? 126.479 121.010 95.744  1.00 71.08  ?  32   LYS   D CB    1 
ATOM   15267 C  CG    . LYS   D 2 33  ? 127.506 121.688 94.856  1.00 72.14  ?  32   LYS   D CG    1 
ATOM   15268 C  CD    . LYS   D 2 33  ? 127.078 121.664 93.400  1.00 71.54  ?  32   LYS   D CD    1 
ATOM   15269 C  CE    . LYS   D 2 33  ? 128.164 122.224 92.499  1.00 74.70  ?  32   LYS   D CE    1 
ATOM   15270 N  NZ    . LYS   D 2 33  ? 127.750 122.234 91.071  1.00 76.41  ?  32   LYS   D NZ    1 
ATOM   15271 N  N     . TYR   D 2 34  ? 126.115 123.059 98.149  1.00 81.61  ?  33   TYR   D N     1 
ATOM   15272 C  CA    . TYR   D 2 34  ? 126.236 124.367 98.783  1.00 75.88  ?  33   TYR   D CA    1 
ATOM   15273 C  C     . TYR   D 2 34  ? 125.423 124.342 100.069 1.00 80.55  ?  33   TYR   D C     1 
ATOM   15274 O  O     . TYR   D 2 34  ? 124.190 124.275 100.026 1.00 84.51  ?  33   TYR   D O     1 
ATOM   15275 C  CB    . TYR   D 2 34  ? 125.760 125.478 97.849  1.00 74.72  ?  33   TYR   D CB    1 
ATOM   15276 C  CG    . TYR   D 2 34  ? 126.491 125.497 96.529  1.00 76.55  ?  33   TYR   D CG    1 
ATOM   15277 C  CD1   . TYR   D 2 34  ? 127.832 125.844 96.464  1.00 78.58  ?  33   TYR   D CD1   1 
ATOM   15278 C  CD2   . TYR   D 2 34  ? 125.846 125.154 95.349  1.00 76.24  ?  33   TYR   D CD2   1 
ATOM   15279 C  CE1   . TYR   D 2 34  ? 128.508 125.859 95.263  1.00 80.89  ?  33   TYR   D CE1   1 
ATOM   15280 C  CE2   . TYR   D 2 34  ? 126.514 125.166 94.142  1.00 77.20  ?  33   TYR   D CE2   1 
ATOM   15281 C  CZ    . TYR   D 2 34  ? 127.845 125.519 94.105  1.00 82.62  ?  33   TYR   D CZ    1 
ATOM   15282 O  OH    . TYR   D 2 34  ? 128.520 125.532 92.908  1.00 85.85  ?  33   TYR   D OH    1 
ATOM   15283 N  N     . ASP   D 2 35  ? 126.113 124.394 101.210 1.00 92.16  ?  34   ASP   D N     1 
ATOM   15284 C  CA    . ASP   D 2 35  ? 125.435 124.325 102.499 1.00 93.25  ?  34   ASP   D CA    1 
ATOM   15285 C  C     . ASP   D 2 35  ? 124.640 125.586 102.810 1.00 93.39  ?  34   ASP   D C     1 
ATOM   15286 O  O     . ASP   D 2 35  ? 123.788 125.557 103.705 1.00 96.55  ?  34   ASP   D O     1 
ATOM   15287 C  CB    . ASP   D 2 35  ? 126.450 124.057 103.615 1.00 95.29  ?  34   ASP   D CB    1 
ATOM   15288 C  CG    . ASP   D 2 35  ? 127.485 125.161 103.747 1.00 99.18  ?  34   ASP   D CG    1 
ATOM   15289 O  OD1   . ASP   D 2 35  ? 127.469 126.098 102.926 1.00 99.53  ?  34   ASP   D OD1   1 
ATOM   15290 O  OD2   . ASP   D 2 35  ? 128.321 125.096 104.674 1.00 100.24 ?  34   ASP   D OD2   1 
ATOM   15291 N  N     . ILE   D 2 36  ? 124.899 126.682 102.092 1.00 75.50  ?  35   ILE   D N     1 
ATOM   15292 C  CA    . ILE   D 2 36  ? 124.255 127.955 102.400 1.00 73.90  ?  35   ILE   D CA    1 
ATOM   15293 C  C     . ILE   D 2 36  ? 122.744 127.841 102.260 1.00 74.92  ?  35   ILE   D C     1 
ATOM   15294 O  O     . ILE   D 2 36  ? 121.993 128.395 103.068 1.00 82.70  ?  35   ILE   D O     1 
ATOM   15295 C  CB    . ILE   D 2 36  ? 124.834 129.074 101.514 1.00 77.39  ?  35   ILE   D CB    1 
ATOM   15296 C  CG1   . ILE   D 2 36  ? 123.993 130.347 101.636 1.00 76.23  ?  35   ILE   D CG1   1 
ATOM   15297 C  CG2   . ILE   D 2 36  ? 124.908 128.623 100.062 1.00 77.29  ?  35   ILE   D CG2   1 
ATOM   15298 C  CD1   . ILE   D 2 36  ? 124.064 131.003 102.998 1.00 70.80  ?  35   ILE   D CD1   1 
ATOM   15299 N  N     . PHE   D 2 37  ? 122.274 127.083 101.269 1.00 71.27  ?  36   PHE   D N     1 
ATOM   15300 C  CA    . PHE   D 2 37  ? 120.838 126.895 101.106 1.00 72.43  ?  36   PHE   D CA    1 
ATOM   15301 C  C     . PHE   D 2 37  ? 120.253 126.061 102.238 1.00 74.55  ?  36   PHE   D C     1 
ATOM   15302 O  O     . PHE   D 2 37  ? 119.123 126.307 102.671 1.00 84.32  ?  36   PHE   D O     1 
ATOM   15303 C  CB    . PHE   D 2 37  ? 120.549 126.266 99.748  1.00 71.04  ?  36   PHE   D CB    1 
ATOM   15304 C  CG    . PHE   D 2 37  ? 121.042 127.088 98.598  1.00 72.67  ?  36   PHE   D CG    1 
ATOM   15305 C  CD1   . PHE   D 2 37  ? 120.614 128.395 98.435  1.00 71.36  ?  36   PHE   D CD1   1 
ATOM   15306 C  CD2   . PHE   D 2 37  ? 121.945 126.566 97.692  1.00 75.10  ?  36   PHE   D CD2   1 
ATOM   15307 C  CE1   . PHE   D 2 37  ? 121.071 129.162 97.386  1.00 73.83  ?  36   PHE   D CE1   1 
ATOM   15308 C  CE2   . PHE   D 2 37  ? 122.404 127.328 96.639  1.00 74.70  ?  36   PHE   D CE2   1 
ATOM   15309 C  CZ    . PHE   D 2 37  ? 121.967 128.629 96.486  1.00 75.38  ?  36   PHE   D CZ    1 
ATOM   15310 N  N     . GLU   D 2 38  ? 121.004 125.078 102.741 1.00 76.96  ?  37   GLU   D N     1 
ATOM   15311 C  CA    . GLU   D 2 38  ? 120.528 124.328 103.899 1.00 76.22  ?  37   GLU   D CA    1 
ATOM   15312 C  C     . GLU   D 2 38  ? 120.431 125.212 105.132 1.00 78.18  ?  37   GLU   D C     1 
ATOM   15313 O  O     . GLU   D 2 38  ? 119.463 125.122 105.898 1.00 79.60  ?  37   GLU   D O     1 
ATOM   15314 C  CB    . GLU   D 2 38  ? 121.432 123.128 104.172 1.00 74.39  ?  37   GLU   D CB    1 
ATOM   15315 C  CG    . GLU   D 2 38  ? 120.994 122.255 105.358 1.00 80.33  ?  37   GLU   D CG    1 
ATOM   15316 C  CD    . GLU   D 2 38  ? 119.564 121.729 105.263 1.00 90.73  ?  37   GLU   D CD    1 
ATOM   15317 O  OE1   . GLU   D 2 38  ? 118.889 122.005 104.253 1.00 94.91  ?  37   GLU   D OE1   1 
ATOM   15318 O  OE2   . GLU   D 2 38  ? 119.106 121.034 106.195 1.00 89.84  ?  37   GLU   D OE2   1 
ATOM   15319 N  N     . LYS   D 2 39  ? 121.425 126.073 105.341 1.00 69.03  ?  38   LYS   D N     1 
ATOM   15320 C  CA    . LYS   D 2 39  ? 121.356 127.010 106.456 1.00 62.39  ?  38   LYS   D CA    1 
ATOM   15321 C  C     . LYS   D 2 39  ? 120.180 127.964 106.293 1.00 69.37  ?  38   LYS   D C     1 
ATOM   15322 O  O     . LYS   D 2 39  ? 119.517 128.317 107.274 1.00 76.51  ?  38   LYS   D O     1 
ATOM   15323 C  CB    . LYS   D 2 39  ? 122.661 127.796 106.565 1.00 67.34  ?  38   LYS   D CB    1 
ATOM   15324 C  CG    . LYS   D 2 39  ? 123.870 127.025 107.066 1.00 69.91  ?  38   LYS   D CG    1 
ATOM   15325 C  CD    . LYS   D 2 39  ? 125.036 127.157 106.102 1.00 75.69  ?  38   LYS   D CD    1 
ATOM   15326 C  CE    . LYS   D 2 39  ? 126.367 126.974 106.808 1.00 77.71  ?  38   LYS   D CE    1 
ATOM   15327 N  NZ    . LYS   D 2 39  ? 126.269 126.007 107.936 1.00 76.95  ?  38   LYS   D NZ    1 
ATOM   15328 N  N     . LEU   D 2 40  ? 119.915 128.400 105.059 1.00 61.21  ?  39   LEU   D N     1 
ATOM   15329 C  CA    . LEU   D 2 40  ? 118.782 129.284 104.804 1.00 60.15  ?  39   LEU   D CA    1 
ATOM   15330 C  C     . LEU   D 2 40  ? 117.459 128.590 105.097 1.00 62.15  ?  39   LEU   D C     1 
ATOM   15331 O  O     . LEU   D 2 40  ? 116.551 129.192 105.677 1.00 69.38  ?  39   LEU   D O     1 
ATOM   15332 C  CB    . LEU   D 2 40  ? 118.817 129.778 103.359 1.00 58.24  ?  39   LEU   D CB    1 
ATOM   15333 C  CG    . LEU   D 2 40  ? 119.837 130.879 103.072 1.00 65.03  ?  39   LEU   D CG    1 
ATOM   15334 C  CD1   . LEU   D 2 40  ? 120.248 130.835 101.615 1.00 65.65  ?  39   LEU   D CD1   1 
ATOM   15335 C  CD2   . LEU   D 2 40  ? 119.274 132.241 103.435 1.00 69.05  ?  39   LEU   D CD2   1 
ATOM   15336 N  N     . ILE   D 2 41  ? 117.333 127.321 104.706 1.00 56.78  ?  40   ILE   D N     1 
ATOM   15337 C  CA    . ILE   D 2 41  ? 116.117 126.568 105.002 1.00 53.55  ?  40   ILE   D CA    1 
ATOM   15338 C  C     . ILE   D 2 41  ? 115.938 126.419 106.505 1.00 61.20  ?  40   ILE   D C     1 
ATOM   15339 O  O     . ILE   D 2 41  ? 114.835 126.604 107.034 1.00 70.50  ?  40   ILE   D O     1 
ATOM   15340 C  CB    . ILE   D 2 41  ? 116.143 125.198 104.300 1.00 56.27  ?  40   ILE   D CB    1 
ATOM   15341 C  CG1   . ILE   D 2 41  ? 116.081 125.361 102.784 1.00 59.49  ?  40   ILE   D CG1   1 
ATOM   15342 C  CG2   . ILE   D 2 41  ? 114.992 124.329 104.785 1.00 55.12  ?  40   ILE   D CG2   1 
ATOM   15343 C  CD1   . ILE   D 2 41  ? 116.678 124.194 102.030 1.00 57.51  ?  40   ILE   D CD1   1 
ATOM   15344 N  N     . GLU   D 2 42  ? 117.021 126.093 107.217 1.00 67.74  ?  41   GLU   D N     1 
ATOM   15345 C  CA    . GLU   D 2 42  ? 116.935 125.947 108.666 1.00 66.27  ?  41   GLU   D CA    1 
ATOM   15346 C  C     . GLU   D 2 42  ? 116.547 127.260 109.332 1.00 70.15  ?  41   GLU   D C     1 
ATOM   15347 O  O     . GLU   D 2 42  ? 115.734 127.274 110.260 1.00 76.83  ?  41   GLU   D O     1 
ATOM   15348 C  CB    . GLU   D 2 42  ? 118.261 125.431 109.219 1.00 73.49  ?  41   GLU   D CB    1 
ATOM   15349 C  CG    . GLU   D 2 42  ? 118.121 124.630 110.499 1.00 77.38  ?  41   GLU   D CG    1 
ATOM   15350 C  CD    . GLU   D 2 42  ? 119.328 124.766 111.404 1.00 88.77  ?  41   GLU   D CD    1 
ATOM   15351 O  OE1   . GLU   D 2 42  ? 120.275 125.488 111.028 1.00 90.77  ?  41   GLU   D OE1   1 
ATOM   15352 O  OE2   . GLU   D 2 42  ? 119.329 124.150 112.491 1.00 87.10  ?  41   GLU   D OE2   1 
ATOM   15353 N  N     . LYS   D 2 43  ? 117.142 128.363 108.894 1.00 58.83  ?  42   LYS   D N     1 
ATOM   15354 C  CA    A LYS   D 2 43  ? 116.766 129.701 109.431 0.50 52.63  ?  42   LYS   D CA    1 
ATOM   15355 C  CA    B LYS   D 2 43  ? 116.765 129.701 109.432 0.50 52.63  ?  42   LYS   D CA    1 
ATOM   15356 C  C     . LYS   D 2 43  ? 115.296 130.109 109.142 1.00 56.69  ?  42   LYS   D C     1 
ATOM   15357 O  O     . LYS   D 2 43  ? 114.505 130.716 109.951 1.00 63.07  ?  42   LYS   D O     1 
ATOM   15358 C  CB    A LYS   D 2 43  ? 117.734 130.773 108.920 0.50 57.50  ?  42   LYS   D CB    1 
ATOM   15359 C  CB    B LYS   D 2 43  ? 117.730 130.771 108.915 0.50 57.50  ?  42   LYS   D CB    1 
ATOM   15360 C  CG    A LYS   D 2 43  ? 119.092 130.799 109.603 0.50 63.62  ?  42   LYS   D CG    1 
ATOM   15361 C  CG    B LYS   D 2 43  ? 119.155 130.678 109.439 0.50 63.62  ?  42   LYS   D CG    1 
ATOM   15362 C  CD    A LYS   D 2 43  ? 119.002 130.614 111.100 0.50 69.91  ?  42   LYS   D CD    1 
ATOM   15363 C  CD    B LYS   D 2 43  ? 119.996 131.878 109.066 0.50 69.91  ?  42   LYS   D CD    1 
ATOM   15364 C  CE    A LYS   D 2 43  ? 118.494 131.847 111.813 0.50 70.89  ?  42   LYS   D CE    1 
ATOM   15365 C  CE    B LYS   D 2 43  ? 120.279 131.965 107.581 0.50 70.89  ?  42   LYS   D CE    1 
ATOM   15366 N  NZ    A LYS   D 2 43  ? 119.042 131.952 113.186 0.50 65.26  ?  42   LYS   D NZ    1 
ATOM   15367 N  NZ    B LYS   D 2 43  ? 121.200 133.081 107.262 0.50 65.26  ?  42   LYS   D NZ    1 
ATOM   15368 N  N     . GLN   D 2 44  ? 114.855 129.761 107.935 1.00 60.57  ?  43   GLN   D N     1 
ATOM   15369 C  CA    . GLN   D 2 44  ? 113.464 130.043 107.595 1.00 54.66  ?  43   GLN   D CA    1 
ATOM   15370 C  C     . GLN   D 2 44  ? 112.512 129.229 108.458 1.00 57.41  ?  43   GLN   D C     1 
ATOM   15371 O  O     . GLN   D 2 44  ? 111.489 129.744 108.924 1.00 64.22  ?  43   GLN   D O     1 
ATOM   15372 C  CB    . GLN   D 2 44  ? 113.220 129.766 106.112 1.00 55.60  ?  43   GLN   D CB    1 
ATOM   15373 C  CG    . GLN   D 2 44  ? 111.940 130.373 105.558 1.00 56.08  ?  43   GLN   D CG    1 
ATOM   15374 C  CD    . GLN   D 2 44  ? 111.764 131.830 105.936 1.00 65.94  ?  43   GLN   D CD    1 
ATOM   15375 O  OE1   . GLN   D 2 44  ? 112.394 132.713 105.358 1.00 73.63  ?  43   GLN   D OE1   1 
ATOM   15376 N  NE2   . GLN   D 2 44  ? 110.894 132.088 106.904 1.00 65.07  ?  43   GLN   D NE2   1 
ATOM   15377 N  N     . LEU   D 2 45  ? 112.832 127.954 108.687 1.00 53.33  ?  44   LEU   D N     1 
ATOM   15378 C  CA    . LEU   D 2 45  ? 111.999 127.147 109.570 1.00 51.50  ?  44   LEU   D CA    1 
ATOM   15379 C  C     . LEU   D 2 45  ? 112.111 127.601 111.018 1.00 57.53  ?  44   LEU   D C     1 
ATOM   15380 O  O     . LEU   D 2 45  ? 111.163 127.427 111.790 1.00 68.47  ?  44   LEU   D O     1 
ATOM   15381 C  CB    . LEU   D 2 45  ? 112.366 125.671 109.445 1.00 55.45  ?  44   LEU   D CB    1 
ATOM   15382 C  CG    . LEU   D 2 45  ? 112.249 125.062 108.051 1.00 52.71  ?  44   LEU   D CG    1 
ATOM   15383 C  CD1   . LEU   D 2 45  ? 112.888 123.684 108.000 1.00 55.31  ?  44   LEU   D CD1   1 
ATOM   15384 C  CD2   . LEU   D 2 45  ? 110.796 125.004 107.642 1.00 50.56  ?  44   LEU   D CD2   1 
ATOM   15385 N  N     . SER   D 2 46  ? 113.247 128.181 111.403 1.00 61.63  ?  45   SER   D N     1 
ATOM   15386 C  CA    . SER   D 2 46  ? 113.411 128.715 112.747 1.00 53.63  ?  45   SER   D CA    1 
ATOM   15387 C  C     . SER   D 2 46  ? 112.805 130.100 112.920 1.00 62.18  ?  45   SER   D C     1 
ATOM   15388 O  O     . SER   D 2 46  ? 112.792 130.615 114.041 1.00 70.69  ?  45   SER   D O     1 
ATOM   15389 C  CB    . SER   D 2 46  ? 114.893 128.758 113.112 1.00 55.42  ?  45   SER   D CB    1 
ATOM   15390 O  OG    . SER   D 2 46  ? 115.449 130.028 112.827 1.00 65.74  ?  45   SER   D OG    1 
ATOM   15391 N  N     . PHE   D 2 47  ? 112.315 130.719 111.847 1.00 56.03  ?  46   PHE   D N     1 
ATOM   15392 C  CA    . PHE   D 2 47  ? 111.656 132.016 111.915 1.00 39.96  ?  46   PHE   D CA    1 
ATOM   15393 C  C     . PHE   D 2 47  ? 110.166 131.917 111.619 1.00 56.56  ?  46   PHE   D C     1 
ATOM   15394 O  O     . PHE   D 2 47  ? 109.530 132.935 111.330 1.00 72.30  ?  46   PHE   D O     1 
ATOM   15395 C  CB    . PHE   D 2 47  ? 112.307 133.005 110.947 1.00 51.21  ?  46   PHE   D CB    1 
ATOM   15396 C  CG    . PHE   D 2 47  ? 113.665 133.470 111.374 1.00 56.74  ?  46   PHE   D CG    1 
ATOM   15397 C  CD1   . PHE   D 2 47  ? 114.001 133.544 112.713 1.00 56.04  ?  46   PHE   D CD1   1 
ATOM   15398 C  CD2   . PHE   D 2 47  ? 114.629 133.778 110.429 1.00 56.56  ?  46   PHE   D CD2   1 
ATOM   15399 C  CE1   . PHE   D 2 47  ? 115.261 133.961 113.102 1.00 58.11  ?  46   PHE   D CE1   1 
ATOM   15400 C  CE2   . PHE   D 2 47  ? 115.885 134.204 110.810 1.00 56.85  ?  46   PHE   D CE2   1 
ATOM   15401 C  CZ    . PHE   D 2 47  ? 116.204 134.290 112.148 1.00 60.47  ?  46   PHE   D CZ    1 
ATOM   15402 N  N     . PHE   D 2 48  ? 109.599 130.713 111.670 1.00 55.78  ?  47   PHE   D N     1 
ATOM   15403 C  CA    . PHE   D 2 48  ? 108.199 130.528 111.314 1.00 48.45  ?  47   PHE   D CA    1 
ATOM   15404 C  C     . PHE   D 2 48  ? 107.304 131.341 112.237 1.00 56.54  ?  47   PHE   D C     1 
ATOM   15405 O  O     . PHE   D 2 48  ? 107.442 131.293 113.463 1.00 65.68  ?  47   PHE   D O     1 
ATOM   15406 C  CB    . PHE   D 2 48  ? 107.829 129.045 111.380 1.00 50.93  ?  47   PHE   D CB    1 
ATOM   15407 C  CG    . PHE   D 2 48  ? 106.397 128.762 111.016 1.00 51.61  ?  47   PHE   D CG    1 
ATOM   15408 C  CD1   . PHE   D 2 48  ? 105.980 128.814 109.699 1.00 54.28  ?  47   PHE   D CD1   1 
ATOM   15409 C  CD2   . PHE   D 2 48  ? 105.453 128.518 112.000 1.00 53.37  ?  47   PHE   D CD2   1 
ATOM   15410 C  CE1   . PHE   D 2 48  ? 104.663 128.561 109.364 1.00 60.72  ?  47   PHE   D CE1   1 
ATOM   15411 C  CE2   . PHE   D 2 48  ? 104.137 128.263 111.672 1.00 46.87  ?  47   PHE   D CE2   1 
ATOM   15412 C  CZ    . PHE   D 2 48  ? 103.741 128.290 110.352 1.00 54.73  ?  47   PHE   D CZ    1 
ATOM   15413 N  N     . TRP   D 2 49  ? 106.384 132.092 111.640 1.00 52.27  ?  48   TRP   D N     1 
ATOM   15414 C  CA    . TRP   D 2 49  ? 105.480 132.944 112.392 1.00 52.17  ?  48   TRP   D CA    1 
ATOM   15415 C  C     . TRP   D 2 49  ? 104.147 132.998 111.667 1.00 59.22  ?  48   TRP   D C     1 
ATOM   15416 O  O     . TRP   D 2 49  ? 104.050 132.686 110.478 1.00 64.08  ?  48   TRP   D O     1 
ATOM   15417 C  CB    . TRP   D 2 49  ? 106.048 134.356 112.572 1.00 53.78  ?  48   TRP   D CB    1 
ATOM   15418 C  CG    . TRP   D 2 49  ? 106.262 135.083 111.279 1.00 52.85  ?  48   TRP   D CG    1 
ATOM   15419 C  CD1   . TRP   D 2 49  ? 107.330 134.966 110.442 1.00 52.53  ?  48   TRP   D CD1   1 
ATOM   15420 C  CD2   . TRP   D 2 49  ? 105.381 136.037 110.674 1.00 51.47  ?  48   TRP   D CD2   1 
ATOM   15421 N  NE1   . TRP   D 2 49  ? 107.171 135.788 109.354 1.00 52.53  ?  48   TRP   D NE1   1 
ATOM   15422 C  CE2   . TRP   D 2 49  ? 105.981 136.456 109.473 1.00 49.13  ?  48   TRP   D CE2   1 
ATOM   15423 C  CE3   . TRP   D 2 49  ? 104.143 136.577 111.032 1.00 55.57  ?  48   TRP   D CE3   1 
ATOM   15424 C  CZ2   . TRP   D 2 49  ? 105.389 137.389 108.629 1.00 53.04  ?  48   TRP   D CZ2   1 
ATOM   15425 C  CZ3   . TRP   D 2 49  ? 103.557 137.504 110.192 1.00 59.00  ?  48   TRP   D CZ3   1 
ATOM   15426 C  CH2   . TRP   D 2 49  ? 104.179 137.900 109.005 1.00 57.76  ?  48   TRP   D CH2   1 
ATOM   15427 N  N     . ARG   D 2 50  ? 103.116 133.396 112.402 1.00 64.12  ?  49   ARG   D N     1 
ATOM   15428 C  CA    . ARG   D 2 50  ? 101.789 133.543 111.838 1.00 58.46  ?  49   ARG   D CA    1 
ATOM   15429 C  C     . ARG   D 2 50  ? 101.274 134.947 112.114 1.00 61.83  ?  49   ARG   D C     1 
ATOM   15430 O  O     . ARG   D 2 50  ? 101.568 135.524 113.168 1.00 66.84  ?  49   ARG   D O     1 
ATOM   15431 C  CB    . ARG   D 2 50  ? 100.821 132.504 112.420 1.00 51.55  ?  49   ARG   D CB    1 
ATOM   15432 C  CG    . ARG   D 2 50  ? 100.906 131.149 111.745 1.00 54.79  ?  49   ARG   D CG    1 
ATOM   15433 C  CD    . ARG   D 2 50  ? 99.995  130.139 112.414 1.00 53.68  ?  49   ARG   D CD    1 
ATOM   15434 N  NE    . ARG   D 2 50  ? 98.640  130.197 111.882 1.00 62.75  ?  49   ARG   D NE    1 
ATOM   15435 C  CZ    . ARG   D 2 50  ? 97.603  129.560 112.406 1.00 59.37  ?  49   ARG   D CZ    1 
ATOM   15436 N  NH1   . ARG   D 2 50  ? 97.731  128.800 113.480 1.00 58.93  ?  49   ARG   D NH1   1 
ATOM   15437 N  NH2   . ARG   D 2 50  ? 96.408  129.690 111.838 1.00 59.95  ?  49   ARG   D NH2   1 
ATOM   15438 N  N     . PRO   D 2 51  ? 100.513 135.524 111.185 1.00 67.20  ?  50   PRO   D N     1 
ATOM   15439 C  CA    . PRO   D 2 51  ? 100.003 136.886 111.399 1.00 61.80  ?  50   PRO   D CA    1 
ATOM   15440 C  C     . PRO   D 2 51  ? 99.070  136.997 112.589 1.00 67.06  ?  50   PRO   D C     1 
ATOM   15441 O  O     . PRO   D 2 51  ? 98.877  138.103 113.105 1.00 73.10  ?  50   PRO   D O     1 
ATOM   15442 C  CB    . PRO   D 2 51  ? 99.273  137.201 110.084 1.00 60.09  ?  50   PRO   D CB    1 
ATOM   15443 C  CG    . PRO   D 2 51  ? 99.767  136.175 109.105 1.00 64.87  ?  50   PRO   D CG    1 
ATOM   15444 C  CD    . PRO   D 2 51  ? 100.082 134.962 109.897 1.00 65.85  ?  50   PRO   D CD    1 
ATOM   15445 N  N     . GLU   D 2 52  ? 98.453  135.899 113.013 1.00 83.11  ?  51   GLU   D N     1 
ATOM   15446 C  CA    . GLU   D 2 52  ? 97.480  135.931 114.095 1.00 80.01  ?  51   GLU   D CA    1 
ATOM   15447 C  C     . GLU   D 2 52  ? 98.122  136.004 115.473 1.00 83.97  ?  51   GLU   D C     1 
ATOM   15448 O  O     . GLU   D 2 52  ? 97.398  136.118 116.467 1.00 88.64  ?  51   GLU   D O     1 
ATOM   15449 C  CB    . GLU   D 2 52  ? 96.576  134.701 114.019 1.00 83.07  ?  51   GLU   D CB    1 
ATOM   15450 C  CG    . GLU   D 2 52  ? 95.614  134.698 112.846 1.00 88.42  ?  51   GLU   D CG    1 
ATOM   15451 C  CD    . GLU   D 2 52  ? 96.084  133.824 111.702 1.00 93.08  ?  51   GLU   D CD    1 
ATOM   15452 O  OE1   . GLU   D 2 52  ? 97.256  133.952 111.296 1.00 90.68  ?  51   GLU   D OE1   1 
ATOM   15453 O  OE2   . GLU   D 2 52  ? 95.276  133.010 111.209 1.00 91.80  ?  51   GLU   D OE2   1 
ATOM   15454 N  N     . GLU   D 2 53  ? 99.447  135.929 115.559 1.00 83.29  ?  52   GLU   D N     1 
ATOM   15455 C  CA    . GLU   D 2 53  ? 100.151 136.056 116.826 1.00 80.29  ?  52   GLU   D CA    1 
ATOM   15456 C  C     . GLU   D 2 53  ? 100.446 137.502 117.195 1.00 86.72  ?  52   GLU   D C     1 
ATOM   15457 O  O     . GLU   D 2 53  ? 101.004 137.751 118.269 1.00 91.51  ?  52   GLU   D O     1 
ATOM   15458 C  CB    . GLU   D 2 53  ? 101.463 135.267 116.785 1.00 83.00  ?  52   GLU   D CB    1 
ATOM   15459 C  CG    . GLU   D 2 53  ? 101.303 133.777 116.553 1.00 89.12  ?  52   GLU   D CG    1 
ATOM   15460 C  CD    . GLU   D 2 53  ? 102.564 133.135 116.009 1.00 96.83  ?  52   GLU   D CD    1 
ATOM   15461 O  OE1   . GLU   D 2 53  ? 103.514 133.873 115.678 1.00 92.77  ?  52   GLU   D OE1   1 
ATOM   15462 O  OE2   . GLU   D 2 53  ? 102.606 131.890 115.918 1.00 95.54  ?  52   GLU   D OE2   1 
ATOM   15463 N  N     . VAL   D 2 54  ? 100.092 138.456 116.338 1.00 80.33  ?  53   VAL   D N     1 
ATOM   15464 C  CA    . VAL   D 2 54  ? 100.365 139.871 116.566 1.00 77.44  ?  53   VAL   D CA    1 
ATOM   15465 C  C     . VAL   D 2 54  ? 99.036  140.590 116.749 1.00 80.79  ?  53   VAL   D C     1 
ATOM   15466 O  O     . VAL   D 2 54  ? 98.153  140.508 115.887 1.00 83.27  ?  53   VAL   D O     1 
ATOM   15467 C  CB    . VAL   D 2 54  ? 101.168 140.486 115.411 1.00 74.57  ?  53   VAL   D CB    1 
ATOM   15468 C  CG1   . VAL   D 2 54  ? 101.178 142.003 115.521 1.00 74.28  ?  53   VAL   D CG1   1 
ATOM   15469 C  CG2   . VAL   D 2 54  ? 102.584 139.937 115.398 1.00 78.74  ?  53   VAL   D CG2   1 
ATOM   15470 N  N     . ASP   D 2 55  ? 98.895  141.295 117.869 1.00 97.39  ?  54   ASP   D N     1 
ATOM   15471 C  CA    . ASP   D 2 55  ? 97.683  142.055 118.141 1.00 94.72  ?  54   ASP   D CA    1 
ATOM   15472 C  C     . ASP   D 2 55  ? 97.674  143.329 117.307 1.00 94.60  ?  54   ASP   D C     1 
ATOM   15473 O  O     . ASP   D 2 55  ? 98.632  144.106 117.335 1.00 96.15  ?  54   ASP   D O     1 
ATOM   15474 C  CB    . ASP   D 2 55  ? 97.588  142.390 119.629 1.00 95.22  ?  54   ASP   D CB    1 
ATOM   15475 C  CG    . ASP   D 2 55  ? 96.269  143.037 120.001 1.00 100.09 ?  54   ASP   D CG    1 
ATOM   15476 O  OD1   . ASP   D 2 55  ? 95.325  142.984 119.186 1.00 101.89 ?  54   ASP   D OD1   1 
ATOM   15477 O  OD2   . ASP   D 2 55  ? 96.175  143.600 121.111 1.00 101.45 ?  54   ASP   D OD2   1 
ATOM   15478 N  N     . VAL   D 2 56  ? 96.589  143.540 116.563 1.00 83.87  ?  55   VAL   D N     1 
ATOM   15479 C  CA    . VAL   D 2 56  ? 96.465  144.704 115.692 1.00 84.24  ?  55   VAL   D CA    1 
ATOM   15480 C  C     . VAL   D 2 56  ? 95.164  145.432 116.001 1.00 87.52  ?  55   VAL   D C     1 
ATOM   15481 O  O     . VAL   D 2 56  ? 94.592  146.100 115.132 1.00 89.54  ?  55   VAL   D O     1 
ATOM   15482 C  CB    . VAL   D 2 56  ? 96.530  144.296 114.209 1.00 82.18  ?  55   VAL   D CB    1 
ATOM   15483 C  CG1   . VAL   D 2 56  ? 97.963  143.999 113.803 1.00 81.02  ?  55   VAL   D CG1   1 
ATOM   15484 C  CG2   . VAL   D 2 56  ? 95.637  143.093 113.952 1.00 81.04  ?  55   VAL   D CG2   1 
ATOM   15485 N  N     . SER   D 2 57  ? 94.683  145.301 117.238 1.00 99.70  ?  56   SER   D N     1 
ATOM   15486 C  CA    . SER   D 2 57  ? 93.406  145.905 117.606 1.00 96.84  ?  56   SER   D CA    1 
ATOM   15487 C  C     . SER   D 2 57  ? 93.483  147.427 117.606 1.00 97.93  ?  56   SER   D C     1 
ATOM   15488 O  O     . SER   D 2 57  ? 92.582  148.100 117.091 1.00 99.91  ?  56   SER   D O     1 
ATOM   15489 C  CB    . SER   D 2 57  ? 92.964  145.395 118.974 1.00 98.03  ?  56   SER   D CB    1 
ATOM   15490 O  OG    . SER   D 2 57  ? 93.215  144.008 119.101 1.00 100.22 ?  56   SER   D OG    1 
ATOM   15491 N  N     . ARG   D 2 58  ? 94.552  147.989 118.174 1.00 103.77 ?  57   ARG   D N     1 
ATOM   15492 C  CA    . ARG   D 2 58  ? 94.716  149.438 118.211 1.00 104.09 ?  57   ARG   D CA    1 
ATOM   15493 C  C     . ARG   D 2 58  ? 95.032  150.031 116.845 1.00 105.90 ?  57   ARG   D C     1 
ATOM   15494 O  O     . ARG   D 2 58  ? 94.951  151.255 116.686 1.00 108.24 ?  57   ARG   D O     1 
ATOM   15495 C  CB    . ARG   D 2 58  ? 95.821  149.815 119.199 1.00 103.22 ?  57   ARG   D CB    1 
ATOM   15496 C  CG    . ARG   D 2 58  ? 95.625  151.161 119.868 1.00 105.73 ?  57   ARG   D CG    1 
ATOM   15497 C  CD    . ARG   D 2 58  ? 96.705  151.424 120.904 1.00 108.06 ?  57   ARG   D CD    1 
ATOM   15498 N  NE    . ARG   D 2 58  ? 97.596  152.503 120.498 1.00 111.70 ?  57   ARG   D NE    1 
ATOM   15499 C  CZ    . ARG   D 2 58  ? 98.687  152.861 121.157 1.00 110.09 ?  57   ARG   D CZ    1 
ATOM   15500 N  NH1   . ARG   D 2 58  ? 99.059  152.242 122.266 1.00 108.01 ?  57   ARG   D NH1   1 
ATOM   15501 N  NH2   . ARG   D 2 58  ? 99.425  153.866 120.694 1.00 107.00 ?  57   ARG   D NH2   1 
ATOM   15502 N  N     . ASP   D 2 59  ? 95.390  149.198 115.867 1.00 105.82 ?  58   ASP   D N     1 
ATOM   15503 C  CA    . ASP   D 2 59  ? 95.750  149.704 114.547 1.00 103.33 ?  58   ASP   D CA    1 
ATOM   15504 C  C     . ASP   D 2 59  ? 94.560  150.352 113.854 1.00 103.67 ?  58   ASP   D C     1 
ATOM   15505 O  O     . ASP   D 2 59  ? 94.718  151.370 113.175 1.00 106.92 ?  58   ASP   D O     1 
ATOM   15506 C  CB    . ASP   D 2 59  ? 96.324  148.578 113.693 1.00 106.39 ?  58   ASP   D CB    1 
ATOM   15507 C  CG    . ASP   D 2 59  ? 97.752  148.243 114.057 1.00 108.86 ?  58   ASP   D CG    1 
ATOM   15508 O  OD1   . ASP   D 2 59  ? 98.060  148.155 115.264 1.00 108.72 ?  58   ASP   D OD1   1 
ATOM   15509 O  OD2   . ASP   D 2 59  ? 98.567  148.065 113.130 1.00 109.93 ?  58   ASP   D OD2   1 
ATOM   15510 N  N     . ARG   D 2 60  ? 93.360  149.794 114.030 1.00 101.91 ?  59   ARG   D N     1 
ATOM   15511 C  CA    . ARG   D 2 60  ? 92.167  150.395 113.441 1.00 101.34 ?  59   ARG   D CA    1 
ATOM   15512 C  C     . ARG   D 2 60  ? 91.910  151.784 114.013 1.00 103.21 ?  59   ARG   D C     1 
ATOM   15513 O  O     . ARG   D 2 60  ? 91.638  152.735 113.270 1.00 106.09 ?  59   ARG   D O     1 
ATOM   15514 C  CB    . ARG   D 2 60  ? 90.961  149.485 113.672 1.00 100.39 ?  59   ARG   D CB    1 
ATOM   15515 C  CG    . ARG   D 2 60  ? 89.669  150.019 113.102 1.00 101.96 ?  59   ARG   D CG    1 
ATOM   15516 C  CD    . ARG   D 2 60  ? 88.466  149.262 113.647 1.00 104.27 ?  59   ARG   D CD    1 
ATOM   15517 N  NE    . ARG   D 2 60  ? 88.174  148.060 112.872 1.00 105.74 ?  59   ARG   D NE    1 
ATOM   15518 C  CZ    . ARG   D 2 60  ? 87.833  148.031 111.589 1.00 107.91 ?  59   ARG   D CZ    1 
ATOM   15519 N  NH1   . ARG   D 2 60  ? 87.684  149.139 110.881 1.00 106.91 ?  59   ARG   D NH1   1 
ATOM   15520 N  NH2   . ARG   D 2 60  ? 87.635  146.855 111.001 1.00 105.95 ?  59   ARG   D NH2   1 
ATOM   15521 N  N     . ILE   D 2 61  ? 92.003  151.918 115.338 1.00 102.49 ?  60   ILE   D N     1 
ATOM   15522 C  CA    . ILE   D 2 61  ? 91.782  153.212 115.978 1.00 99.94  ?  60   ILE   D CA    1 
ATOM   15523 C  C     . ILE   D 2 61  ? 92.842  154.211 115.532 1.00 100.29 ?  60   ILE   D C     1 
ATOM   15524 O  O     . ILE   D 2 61  ? 92.541  155.381 115.263 1.00 104.06 ?  60   ILE   D O     1 
ATOM   15525 C  CB    . ILE   D 2 61  ? 91.749  153.049 117.511 1.00 99.90  ?  60   ILE   D CB    1 
ATOM   15526 C  CG1   . ILE   D 2 61  ? 90.886  151.846 117.902 1.00 102.63 ?  60   ILE   D CG1   1 
ATOM   15527 C  CG2   . ILE   D 2 61  ? 91.222  154.307 118.187 1.00 99.28  ?  60   ILE   D CG2   1 
ATOM   15528 C  CD1   . ILE   D 2 61  ? 90.885  151.541 119.387 1.00 102.54 ?  60   ILE   D CD1   1 
ATOM   15529 N  N     . ASP   D 2 62  ? 94.097  153.764 115.432 1.00 96.86  ?  61   ASP   D N     1 
ATOM   15530 C  CA    . ASP   D 2 62  ? 95.168  154.663 115.017 1.00 94.42  ?  61   ASP   D CA    1 
ATOM   15531 C  C     . ASP   D 2 62  ? 94.999  155.104 113.569 1.00 95.83  ?  61   ASP   D C     1 
ATOM   15532 O  O     . ASP   D 2 62  ? 95.231  156.274 113.245 1.00 98.38  ?  61   ASP   D O     1 
ATOM   15533 C  CB    . ASP   D 2 62  ? 96.521  153.992 115.225 1.00 98.09  ?  61   ASP   D CB    1 
ATOM   15534 C  CG    . ASP   D 2 62  ? 97.074  154.214 116.616 1.00 102.41 ?  61   ASP   D CG    1 
ATOM   15535 O  OD1   . ASP   D 2 62  ? 97.021  155.361 117.102 1.00 103.75 ?  61   ASP   D OD1   1 
ATOM   15536 O  OD2   . ASP   D 2 62  ? 97.570  153.240 117.219 1.00 105.49 ?  61   ASP   D OD2   1 
ATOM   15537 N  N     . TYR   D 2 63  ? 94.581  154.189 112.690 1.00 94.59  ?  62   TYR   D N     1 
ATOM   15538 C  CA    . TYR   D 2 63  ? 94.370  154.533 111.290 1.00 93.88  ?  62   TYR   D CA    1 
ATOM   15539 C  C     . TYR   D 2 63  ? 93.194  155.484 111.123 1.00 95.87  ?  62   TYR   D C     1 
ATOM   15540 O  O     . TYR   D 2 63  ? 93.249  156.407 110.304 1.00 97.84  ?  62   TYR   D O     1 
ATOM   15541 C  CB    . TYR   D 2 63  ? 94.154  153.262 110.469 1.00 93.76  ?  62   TYR   D CB    1 
ATOM   15542 C  CG    . TYR   D 2 63  ? 93.935  153.519 108.998 1.00 95.23  ?  62   TYR   D CG    1 
ATOM   15543 C  CD1   . TYR   D 2 63  ? 95.001  153.806 108.158 1.00 96.21  ?  62   TYR   D CD1   1 
ATOM   15544 C  CD2   . TYR   D 2 63  ? 92.663  153.474 108.448 1.00 95.03  ?  62   TYR   D CD2   1 
ATOM   15545 C  CE1   . TYR   D 2 63  ? 94.806  154.040 106.811 1.00 96.42  ?  62   TYR   D CE1   1 
ATOM   15546 C  CE2   . TYR   D 2 63  ? 92.458  153.708 107.103 1.00 95.02  ?  62   TYR   D CE2   1 
ATOM   15547 C  CZ    . TYR   D 2 63  ? 93.533  153.991 106.290 1.00 96.52  ?  62   TYR   D CZ    1 
ATOM   15548 O  OH    . TYR   D 2 63  ? 93.330  154.226 104.952 1.00 97.82  ?  62   TYR   D OH    1 
ATOM   15549 N  N     . GLN   D 2 64  ? 92.117  155.273 111.886 1.00 103.14 ?  63   GLN   D N     1 
ATOM   15550 C  CA    . GLN   D 2 64  ? 90.952  156.142 111.768 1.00 103.19 ?  63   GLN   D CA    1 
ATOM   15551 C  C     . GLN   D 2 64  ? 91.236  157.567 112.226 1.00 104.43 ?  63   GLN   D C     1 
ATOM   15552 O  O     . GLN   D 2 64  ? 90.550  158.494 111.782 1.00 104.76 ?  63   GLN   D O     1 
ATOM   15553 C  CB    . GLN   D 2 64  ? 89.781  155.565 112.563 1.00 102.94 ?  63   GLN   D CB    1 
ATOM   15554 C  CG    . GLN   D 2 64  ? 88.696  154.947 111.697 1.00 105.48 ?  63   GLN   D CG    1 
ATOM   15555 C  CD    . GLN   D 2 64  ? 88.031  153.755 112.355 1.00 109.38 ?  63   GLN   D CD    1 
ATOM   15556 O  OE1   . GLN   D 2 64  ? 87.981  153.656 113.580 1.00 109.53 ?  63   GLN   D OE1   1 
ATOM   15557 N  NE2   . GLN   D 2 64  ? 87.515  152.842 111.541 1.00 106.89 ?  63   GLN   D NE2   1 
ATOM   15558 N  N     . ALA   D 2 65  ? 92.224  157.764 113.095 1.00 95.41  ?  64   ALA   D N     1 
ATOM   15559 C  CA    . ALA   D 2 65  ? 92.576  159.089 113.587 1.00 93.96  ?  64   ALA   D CA    1 
ATOM   15560 C  C     . ALA   D 2 65  ? 93.649  159.773 112.749 1.00 96.23  ?  64   ALA   D C     1 
ATOM   15561 O  O     . ALA   D 2 65  ? 93.987  160.928 113.027 1.00 98.59  ?  64   ALA   D O     1 
ATOM   15562 C  CB    . ALA   D 2 65  ? 93.039  159.004 115.044 1.00 93.03  ?  64   ALA   D CB    1 
ATOM   15563 N  N     . LEU   D 2 66  ? 94.189  159.097 111.741 1.00 104.76 ?  65   LEU   D N     1 
ATOM   15564 C  CA    . LEU   D 2 66  ? 95.226  159.679 110.906 1.00 104.50 ?  65   LEU   D CA    1 
ATOM   15565 C  C     . LEU   D 2 66  ? 94.633  160.705 109.942 1.00 107.04 ?  65   LEU   D C     1 
ATOM   15566 O  O     . LEU   D 2 66  ? 93.462  160.610 109.565 1.00 107.22 ?  65   LEU   D O     1 
ATOM   15567 C  CB    . LEU   D 2 66  ? 95.941  158.590 110.115 1.00 103.01 ?  65   LEU   D CB    1 
ATOM   15568 C  CG    . LEU   D 2 66  ? 97.001  157.764 110.846 1.00 103.57 ?  65   LEU   D CG    1 
ATOM   15569 C  CD1   . LEU   D 2 66  ? 97.334  156.509 110.055 1.00 103.42 ?  65   LEU   D CD1   1 
ATOM   15570 C  CD2   . LEU   D 2 66  ? 98.254  158.587 111.097 1.00 103.66 ?  65   LEU   D CD2   1 
ATOM   15571 N  N     . PRO   D 2 67  ? 95.419  161.697 109.532 1.00 112.02 ?  66   PRO   D N     1 
ATOM   15572 C  CA    . PRO   D 2 67  ? 94.967  162.609 108.477 1.00 110.56 ?  66   PRO   D CA    1 
ATOM   15573 C  C     . PRO   D 2 67  ? 94.899  161.895 107.135 1.00 112.87 ?  66   PRO   D C     1 
ATOM   15574 O  O     . PRO   D 2 67  ? 95.476  160.826 106.932 1.00 115.94 ?  66   PRO   D O     1 
ATOM   15575 C  CB    . PRO   D 2 67  ? 96.033  163.709 108.473 1.00 109.06 ?  66   PRO   D CB    1 
ATOM   15576 C  CG    . PRO   D 2 67  ? 97.242  163.062 109.052 1.00 108.62 ?  66   PRO   D CG    1 
ATOM   15577 C  CD    . PRO   D 2 67  ? 96.727  162.095 110.079 1.00 108.10 ?  66   PRO   D CD    1 
ATOM   15578 N  N     . GLU   D 2 68  ? 94.217  162.544 106.186 1.00 119.77 ?  67   GLU   D N     1 
ATOM   15579 C  CA    . GLU   D 2 68  ? 93.922  161.904 104.906 1.00 121.10 ?  67   GLU   D CA    1 
ATOM   15580 C  C     . GLU   D 2 68  ? 95.192  161.548 104.155 1.00 121.61 ?  67   GLU   D C     1 
ATOM   15581 O  O     . GLU   D 2 68  ? 95.296  160.465 103.561 1.00 122.82 ?  67   GLU   D O     1 
ATOM   15582 C  CB    . GLU   D 2 68  ? 93.034  162.813 104.059 1.00 120.02 ?  67   GLU   D CB    1 
ATOM   15583 C  CG    . GLU   D 2 68  ? 91.623  162.977 104.603 1.00 122.30 ?  67   GLU   D CG    1 
ATOM   15584 C  CD    . GLU   D 2 68  ? 90.819  161.691 104.543 1.00 124.63 ?  67   GLU   D CD    1 
ATOM   15585 O  OE1   . GLU   D 2 68  ? 91.093  160.856 103.656 1.00 124.70 ?  67   GLU   D OE1   1 
ATOM   15586 O  OE2   . GLU   D 2 68  ? 89.912  161.516 105.384 1.00 124.22 ?  67   GLU   D OE2   1 
ATOM   15587 N  N     . HIS   D 2 69  ? 96.194  162.413 104.233 1.00 114.33 ?  68   HIS   D N     1 
ATOM   15588 C  CA    . HIS   D 2 69  ? 97.382  162.206 103.438 1.00 114.57 ?  68   HIS   D CA    1 
ATOM   15589 C  C     . HIS   D 2 69  ? 98.278  161.152 104.027 1.00 115.09 ?  68   HIS   D C     1 
ATOM   15590 O  O     . HIS   D 2 69  ? 99.029  160.539 103.284 1.00 117.21 ?  68   HIS   D O     1 
ATOM   15591 C  CB    . HIS   D 2 69  ? 98.134  163.518 103.242 1.00 115.56 ?  68   HIS   D CB    1 
ATOM   15592 C  CG    . HIS   D 2 69  ? 98.868  164.006 104.443 1.00 117.74 ?  68   HIS   D CG    1 
ATOM   15593 N  ND1   . HIS   D 2 69  ? 98.229  164.591 105.512 1.00 117.26 ?  68   HIS   D ND1   1 
ATOM   15594 C  CD2   . HIS   D 2 69  ? 100.193 164.076 104.704 1.00 117.31 ?  68   HIS   D CD2   1 
ATOM   15595 C  CE1   . HIS   D 2 69  ? 99.129  164.960 106.404 1.00 116.74 ?  68   HIS   D CE1   1 
ATOM   15596 N  NE2   . HIS   D 2 69  ? 100.328 164.664 105.935 1.00 117.09 ?  68   HIS   D NE2   1 
ATOM   15597 N  N     . GLU   D 2 70  ? 98.269  160.980 105.346 1.00 111.40 ?  69   GLU   D N     1 
ATOM   15598 C  CA    . GLU   D 2 70  ? 98.974  159.873 105.982 1.00 108.98 ?  69   GLU   D CA    1 
ATOM   15599 C  C     . GLU   D 2 70  ? 98.257  158.552 105.735 1.00 111.68 ?  69   GLU   D C     1 
ATOM   15600 O  O     . GLU   D 2 70  ? 98.901  157.515 105.529 1.00 118.14 ?  69   GLU   D O     1 
ATOM   15601 C  CB    . GLU   D 2 70  ? 99.109  160.149 107.481 1.00 110.68 ?  69   GLU   D CB    1 
ATOM   15602 C  CG    . GLU   D 2 70  ? 100.326 160.990 107.841 1.00 113.15 ?  69   GLU   D CG    1 
ATOM   15603 C  CD    . GLU   D 2 70  ? 100.656 160.959 109.320 1.00 117.19 ?  69   GLU   D CD    1 
ATOM   15604 O  OE1   . GLU   D 2 70  ? 99.787  161.324 110.136 1.00 117.38 ?  69   GLU   D OE1   1 
ATOM   15605 O  OE2   . GLU   D 2 70  ? 101.792 160.575 109.666 1.00 116.97 ?  69   GLU   D OE2   1 
ATOM   15606 N  N     . LYS   D 2 71  ? 96.921  158.571 105.747 1.00 94.11  ?  70   LYS   D N     1 
ATOM   15607 C  CA    . LYS   D 2 71  ? 96.158  157.379 105.395 1.00 92.75  ?  70   LYS   D CA    1 
ATOM   15608 C  C     . LYS   D 2 71  ? 96.464  156.949 103.971 1.00 93.93  ?  70   LYS   D C     1 
ATOM   15609 O  O     . LYS   D 2 71  ? 96.584  155.746 103.690 1.00 93.99  ?  70   LYS   D O     1 
ATOM   15610 C  CB    . LYS   D 2 71  ? 94.663  157.647 105.566 1.00 91.57  ?  70   LYS   D CB    1 
ATOM   15611 C  CG    . LYS   D 2 71  ? 94.164  157.546 106.995 1.00 93.83  ?  70   LYS   D CG    1 
ATOM   15612 C  CD    . LYS   D 2 71  ? 92.671  157.271 107.033 1.00 91.79  ?  70   LYS   D CD    1 
ATOM   15613 C  CE    . LYS   D 2 71  ? 91.892  158.509 107.439 1.00 94.19  ?  70   LYS   D CE    1 
ATOM   15614 N  NZ    . LYS   D 2 71  ? 91.436  158.436 108.853 1.00 97.57  ?  70   LYS   D NZ    1 
ATOM   15615 N  N     . HIS   D 2 72  ? 96.687  157.930 103.085 1.00 95.00  ?  71   HIS   D N     1 
ATOM   15616 C  CA    . HIS   D 2 72  ? 96.962  157.618 101.688 1.00 94.87  ?  71   HIS   D CA    1 
ATOM   15617 C  C     . HIS   D 2 72  ? 98.296  156.948 101.591 1.00 94.17  ?  71   HIS   D C     1 
ATOM   15618 O  O     . HIS   D 2 72  ? 98.448  155.943 100.904 1.00 98.33  ?  71   HIS   D O     1 
ATOM   15619 C  CB    . HIS   D 2 72  ? 96.944  158.869 100.795 1.00 94.50  ?  71   HIS   D CB    1 
ATOM   15620 C  CG    . HIS   D 2 72  ? 97.634  158.693 99.479  1.00 96.81  ?  71   HIS   D CG    1 
ATOM   15621 N  ND1   . HIS   D 2 72  ? 98.927  159.111 99.258  1.00 96.45  ?  71   HIS   D ND1   1 
ATOM   15622 C  CD2   . HIS   D 2 72  ? 97.205  158.163 98.311  1.00 98.06  ?  71   HIS   D CD2   1 
ATOM   15623 C  CE1   . HIS   D 2 72  ? 99.266  158.843 98.011  1.00 97.69  ?  71   HIS   D CE1   1 
ATOM   15624 N  NE2   . HIS   D 2 72  ? 98.239  158.266 97.416  1.00 99.50  ?  71   HIS   D NE2   1 
ATOM   15625 N  N     . ILE   D 2 73  ? 99.276  157.493 102.297 1.00 90.02  ?  72   ILE   D N     1 
ATOM   15626 C  CA    . ILE   D 2 73  ? 100.606 156.900 102.271 1.00 90.86  ?  72   ILE   D CA    1 
ATOM   15627 C  C     . ILE   D 2 73  ? 100.569 155.469 102.796 1.00 96.07  ?  72   ILE   D C     1 
ATOM   15628 O  O     . ILE   D 2 73  ? 101.130 154.549 102.184 1.00 100.24 ?  72   ILE   D O     1 
ATOM   15629 C  CB    . ILE   D 2 73  ? 101.581 157.767 103.083 1.00 91.85  ?  72   ILE   D CB    1 
ATOM   15630 C  CG1   . ILE   D 2 73  ? 101.553 159.219 102.613 1.00 97.98  ?  72   ILE   D CG1   1 
ATOM   15631 C  CG2   . ILE   D 2 73  ? 102.991 157.201 102.995 1.00 92.78  ?  72   ILE   D CG2   1 
ATOM   15632 C  CD1   . ILE   D 2 73  ? 102.039 160.198 103.663 1.00 96.96  ?  72   ILE   D CD1   1 
ATOM   15633 N  N     . PHE   D 2 74  ? 99.887  155.259 103.925 1.00 88.45  ?  73   PHE   D N     1 
ATOM   15634 C  CA    . PHE   D 2 74  ? 99.811  153.928 104.516 1.00 84.78  ?  73   PHE   D CA    1 
ATOM   15635 C  C     . PHE   D 2 74  ? 99.156  152.933 103.563 1.00 88.51  ?  73   PHE   D C     1 
ATOM   15636 O  O     . PHE   D 2 74  ? 99.666  151.825 103.356 1.00 93.73  ?  73   PHE   D O     1 
ATOM   15637 C  CB    . PHE   D 2 74  ? 99.048  153.992 105.839 1.00 83.17  ?  73   PHE   D CB    1 
ATOM   15638 C  CG    . PHE   D 2 74  ? 99.182  152.756 106.678 1.00 86.26  ?  73   PHE   D CG    1 
ATOM   15639 C  CD1   . PHE   D 2 74  ? 98.330  151.680 106.494 1.00 88.61  ?  73   PHE   D CD1   1 
ATOM   15640 C  CD2   . PHE   D 2 74  ? 100.159 152.668 107.653 1.00 88.21  ?  73   PHE   D CD2   1 
ATOM   15641 C  CE1   . PHE   D 2 74  ? 98.453  150.543 107.265 1.00 86.43  ?  73   PHE   D CE1   1 
ATOM   15642 C  CE2   . PHE   D 2 74  ? 100.286 151.532 108.426 1.00 89.63  ?  73   PHE   D CE2   1 
ATOM   15643 C  CZ    . PHE   D 2 74  ? 99.431  150.468 108.231 1.00 87.72  ?  73   PHE   D CZ    1 
ATOM   15644 N  N     . ILE   D 2 75  ? 98.027  153.314 102.964 1.00 86.50  ?  74   ILE   D N     1 
ATOM   15645 C  CA    . ILE   D 2 75  ? 97.300  152.373 102.119 1.00 85.09  ?  74   ILE   D CA    1 
ATOM   15646 C  C     . ILE   D 2 75  ? 98.062  152.099 100.823 1.00 86.78  ?  74   ILE   D C     1 
ATOM   15647 O  O     . ILE   D 2 75  ? 98.060  150.968 100.327 1.00 92.40  ?  74   ILE   D O     1 
ATOM   15648 C  CB    . ILE   D 2 75  ? 95.867  152.876 101.869 1.00 87.09  ?  74   ILE   D CB    1 
ATOM   15649 C  CG1   . ILE   D 2 75  ? 94.965  152.510 103.050 1.00 85.87  ?  74   ILE   D CG1   1 
ATOM   15650 C  CG2   . ILE   D 2 75  ? 95.300  152.306 100.581 1.00 90.54  ?  74   ILE   D CG2   1 
ATOM   15651 C  CD1   . ILE   D 2 75  ? 94.977  151.046 103.414 1.00 83.33  ?  74   ILE   D CD1   1 
ATOM   15652 N  N     . SER   D 2 76  ? 98.751  153.106 100.267 1.00 85.71  ?  75   SER   D N     1 
ATOM   15653 C  CA    . SER   D 2 76  ? 99.548  152.869 99.064  1.00 87.17  ?  75   SER   D CA    1 
ATOM   15654 C  C     . SER   D 2 76  ? 100.729 151.950 99.352  1.00 88.17  ?  75   SER   D C     1 
ATOM   15655 O  O     . SER   D 2 76  ? 101.046 151.062 98.549  1.00 96.35  ?  75   SER   D O     1 
ATOM   15656 C  CB    . SER   D 2 76  ? 100.031 154.194 98.479  1.00 91.46  ?  75   SER   D CB    1 
ATOM   15657 O  OG    . SER   D 2 76  ? 98.940  155.052 98.199  1.00 94.95  ?  75   SER   D OG    1 
ATOM   15658 N  N     . ASN   D 2 77  ? 101.382 152.137 100.501 1.00 77.33  ?  76   ASN   D N     1 
ATOM   15659 C  CA    . ASN   D 2 77  ? 102.463 151.240 100.890 1.00 77.58  ?  76   ASN   D CA    1 
ATOM   15660 C  C     . ASN   D 2 77  ? 101.959 149.813 101.067 1.00 80.05  ?  76   ASN   D C     1 
ATOM   15661 O  O     . ASN   D 2 77  ? 102.596 148.856 100.603 1.00 82.78  ?  76   ASN   D O     1 
ATOM   15662 C  CB    . ASN   D 2 77  ? 103.113 151.750 102.172 1.00 76.05  ?  76   ASN   D CB    1 
ATOM   15663 C  CG    . ASN   D 2 77  ? 104.583 151.433 102.239 1.00 83.93  ?  76   ASN   D CG    1 
ATOM   15664 O  OD1   . ASN   D 2 77  ? 105.362 151.884 101.403 1.00 87.41  ?  76   ASN   D OD1   1 
ATOM   15665 N  ND2   . ASN   D 2 77  ? 104.977 150.656 103.243 1.00 86.17  ?  76   ASN   D ND2   1 
ATOM   15666 N  N     . LEU   D 2 78  ? 100.802 149.655 101.714 1.00 77.72  ?  77   LEU   D N     1 
ATOM   15667 C  CA    . LEU   D 2 78  ? 100.228 148.327 101.895 1.00 73.70  ?  77   LEU   D CA    1 
ATOM   15668 C  C     . LEU   D 2 78  ? 99.881  147.685 100.558 1.00 80.42  ?  77   LEU   D C     1 
ATOM   15669 O  O     . LEU   D 2 78  ? 100.121 146.490 100.360 1.00 86.70  ?  77   LEU   D O     1 
ATOM   15670 C  CB    . LEU   D 2 78  ? 99.000  148.417 102.795 1.00 72.28  ?  77   LEU   D CB    1 
ATOM   15671 C  CG    . LEU   D 2 78  ? 98.755  147.273 103.774 1.00 76.63  ?  77   LEU   D CG    1 
ATOM   15672 C  CD1   . LEU   D 2 78  ? 100.069 146.705 104.279 1.00 80.20  ?  77   LEU   D CD1   1 
ATOM   15673 C  CD2   . LEU   D 2 78  ? 97.904  147.765 104.929 1.00 81.87  ?  77   LEU   D CD2   1 
ATOM   15674 N  N     . LYS   D 2 79  ? 99.331  148.467 99.623  1.00 77.34  ?  78   LYS   D N     1 
ATOM   15675 C  CA    . LYS   D 2 79  ? 99.008  147.942 98.300  1.00 74.28  ?  78   LYS   D CA    1 
ATOM   15676 C  C     . LYS   D 2 79  ? 100.260 147.489 97.561  1.00 74.39  ?  78   LYS   D C     1 
ATOM   15677 O  O     . LYS   D 2 79  ? 100.271 146.421 96.934  1.00 83.73  ?  78   LYS   D O     1 
ATOM   15678 C  CB    . LYS   D 2 79  ? 98.262  149.003 97.492  1.00 76.03  ?  78   LYS   D CB    1 
ATOM   15679 C  CG    . LYS   D 2 79  ? 96.794  149.136 97.850  1.00 74.40  ?  78   LYS   D CG    1 
ATOM   15680 C  CD    . LYS   D 2 79  ? 96.034  149.840 96.739  1.00 79.98  ?  78   LYS   D CD    1 
ATOM   15681 C  CE    . LYS   D 2 79  ? 95.631  151.249 97.135  1.00 77.75  ?  78   LYS   D CE    1 
ATOM   15682 N  NZ    . LYS   D 2 79  ? 94.264  151.279 97.719  1.00 81.85  ?  78   LYS   D NZ    1 
ATOM   15683 N  N     . TYR   D 2 80  ? 101.324 148.294 97.616  1.00 73.66  ?  79   TYR   D N     1 
ATOM   15684 C  CA    . TYR   D 2 80  ? 102.569 147.921 96.950  1.00 76.07  ?  79   TYR   D CA    1 
ATOM   15685 C  C     . TYR   D 2 80  ? 103.125 146.624 97.522  1.00 80.40  ?  79   TYR   D C     1 
ATOM   15686 O  O     . TYR   D 2 80  ? 103.517 145.718 96.775  1.00 86.26  ?  79   TYR   D O     1 
ATOM   15687 C  CB    . TYR   D 2 80  ? 103.594 149.049 97.084  1.00 81.72  ?  79   TYR   D CB    1 
ATOM   15688 C  CG    . TYR   D 2 80  ? 104.720 149.000 96.072  1.00 81.19  ?  79   TYR   D CG    1 
ATOM   15689 C  CD1   . TYR   D 2 80  ? 104.748 148.034 95.077  1.00 82.54  ?  79   TYR   D CD1   1 
ATOM   15690 C  CD2   . TYR   D 2 80  ? 105.763 149.914 96.124  1.00 82.79  ?  79   TYR   D CD2   1 
ATOM   15691 C  CE1   . TYR   D 2 80  ? 105.759 148.007 94.137  1.00 84.30  ?  79   TYR   D CE1   1 
ATOM   15692 C  CE2   . TYR   D 2 80  ? 106.794 149.875 95.208  1.00 80.89  ?  79   TYR   D CE2   1 
ATOM   15693 C  CZ    . TYR   D 2 80  ? 106.791 148.917 94.219  1.00 85.00  ?  79   TYR   D CZ    1 
ATOM   15694 O  OH    . TYR   D 2 80  ? 107.816 148.879 93.303  1.00 91.84  ?  79   TYR   D OH    1 
ATOM   15695 N  N     . GLN   D 2 81  ? 103.163 146.516 98.852  1.00 75.61  ?  80   GLN   D N     1 
ATOM   15696 C  CA    . GLN   D 2 81  ? 103.680 145.296 99.465  1.00 73.17  ?  80   GLN   D CA    1 
ATOM   15697 C  C     . GLN   D 2 81  ? 102.816 144.092 99.109  1.00 74.92  ?  80   GLN   D C     1 
ATOM   15698 O  O     . GLN   D 2 81  ? 103.337 143.000 98.837  1.00 80.85  ?  80   GLN   D O     1 
ATOM   15699 C  CB    . GLN   D 2 81  ? 103.762 145.458 100.981 1.00 69.74  ?  80   GLN   D CB    1 
ATOM   15700 C  CG    . GLN   D 2 81  ? 104.922 146.305 101.470 1.00 73.93  ?  80   GLN   D CG    1 
ATOM   15701 C  CD    . GLN   D 2 81  ? 104.694 146.895 102.842 1.00 81.56  ?  80   GLN   D CD    1 
ATOM   15702 O  OE1   . GLN   D 2 81  ? 103.566 147.195 103.221 1.00 84.43  ?  80   GLN   D OE1   1 
ATOM   15703 N  NE2   . GLN   D 2 81  ? 105.773 147.074 103.593 1.00 79.43  ?  80   GLN   D NE2   1 
ATOM   15704 N  N     . THR   D 2 82  ? 101.491 144.272 99.111  1.00 67.29  ?  81   THR   D N     1 
ATOM   15705 C  CA    . THR   D 2 82  ? 100.588 143.176 98.784  1.00 69.37  ?  81   THR   D CA    1 
ATOM   15706 C  C     . THR   D 2 82  ? 100.819 142.682 97.364  1.00 73.51  ?  81   THR   D C     1 
ATOM   15707 O  O     . THR   D 2 82  ? 100.888 141.473 97.126  1.00 78.04  ?  81   THR   D O     1 
ATOM   15708 C  CB    . THR   D 2 82  ? 99.136  143.620 98.969  1.00 70.34  ?  81   THR   D CB    1 
ATOM   15709 O  OG1   . THR   D 2 82  ? 98.952  144.113 100.301 1.00 79.35  ?  81   THR   D OG1   1 
ATOM   15710 C  CG2   . THR   D 2 82  ? 98.189  142.455 98.733  1.00 68.67  ?  81   THR   D CG2   1 
ATOM   15711 N  N     . LEU   D 2 83  ? 100.955 143.603 96.407  1.00 69.24  ?  82   LEU   D N     1 
ATOM   15712 C  CA    . LEU   D 2 83  ? 101.199 143.188 95.028  1.00 69.90  ?  82   LEU   D CA    1 
ATOM   15713 C  C     . LEU   D 2 83  ? 102.549 142.494 94.890  1.00 72.80  ?  82   LEU   D C     1 
ATOM   15714 O  O     . LEU   D 2 83  ? 102.648 141.436 94.250  1.00 81.75  ?  82   LEU   D O     1 
ATOM   15715 C  CB    . LEU   D 2 83  ? 101.105 144.393 94.093  1.00 69.23  ?  82   LEU   D CB    1 
ATOM   15716 C  CG    . LEU   D 2 83  ? 101.254 144.142 92.587  1.00 72.75  ?  82   LEU   D CG    1 
ATOM   15717 C  CD1   . LEU   D 2 83  ? 100.599 145.256 91.797  1.00 79.72  ?  82   LEU   D CD1   1 
ATOM   15718 C  CD2   . LEU   D 2 83  ? 102.710 144.005 92.163  1.00 71.39  ?  82   LEU   D CD2   1 
ATOM   15719 N  N     . LEU   D 2 84  ? 103.590 143.053 95.511  1.00 66.29  ?  83   LEU   D N     1 
ATOM   15720 C  CA    . LEU   D 2 84  ? 104.922 142.475 95.383  1.00 62.20  ?  83   LEU   D CA    1 
ATOM   15721 C  C     . LEU   D 2 84  ? 104.956 141.051 95.919  1.00 62.38  ?  83   LEU   D C     1 
ATOM   15722 O  O     . LEU   D 2 84  ? 105.473 140.141 95.260  1.00 70.06  ?  83   LEU   D O     1 
ATOM   15723 C  CB    . LEU   D 2 84  ? 105.939 143.353 96.107  1.00 65.67  ?  83   LEU   D CB    1 
ATOM   15724 C  CG    . LEU   D 2 84  ? 106.387 144.617 95.379  1.00 70.12  ?  83   LEU   D CG    1 
ATOM   15725 C  CD1   . LEU   D 2 84  ? 107.436 145.357 96.191  1.00 69.91  ?  83   LEU   D CD1   1 
ATOM   15726 C  CD2   . LEU   D 2 84  ? 106.915 144.272 94.001  1.00 66.21  ?  83   LEU   D CD2   1 
ATOM   15727 N  N     . ASP   D 2 85  ? 104.363 140.823 97.091  1.00 70.18  ?  84   ASP   D N     1 
ATOM   15728 C  CA    . ASP   D 2 85  ? 104.416 139.478 97.644  1.00 74.07  ?  84   ASP   D CA    1 
ATOM   15729 C  C     . ASP   D 2 85  ? 103.388 138.542 97.024  1.00 72.27  ?  84   ASP   D C     1 
ATOM   15730 O  O     . ASP   D 2 85  ? 103.613 137.330 97.019  1.00 80.08  ?  84   ASP   D O     1 
ATOM   15731 C  CB    . ASP   D 2 85  ? 104.278 139.527 99.162  1.00 70.14  ?  84   ASP   D CB    1 
ATOM   15732 C  CG    . ASP   D 2 85  ? 105.627 139.556 99.848  1.00 78.06  ?  84   ASP   D CG    1 
ATOM   15733 O  OD1   . ASP   D 2 85  ? 106.632 139.293 99.157  1.00 80.03  ?  84   ASP   D OD1   1 
ATOM   15734 O  OD2   . ASP   D 2 85  ? 105.702 139.859 101.053 1.00 79.21  ?  84   ASP   D OD2   1 
ATOM   15735 N  N     . SER   D 2 86  ? 102.299 139.065 96.454  1.00 70.36  ?  85   SER   D N     1 
ATOM   15736 C  CA    . SER   D 2 86  ? 101.414 138.218 95.664  1.00 71.25  ?  85   SER   D CA    1 
ATOM   15737 C  C     . SER   D 2 86  ? 102.139 137.672 94.444  1.00 73.04  ?  85   SER   D C     1 
ATOM   15738 O  O     . SER   D 2 86  ? 101.953 136.508 94.070  1.00 77.55  ?  85   SER   D O     1 
ATOM   15739 C  CB    . SER   D 2 86  ? 100.169 138.999 95.249  1.00 71.92  ?  85   SER   D CB    1 
ATOM   15740 O  OG    . SER   D 2 86  ? 100.372 139.662 94.015  1.00 80.17  ?  85   SER   D OG    1 
ATOM   15741 N  N     . ILE   D 2 87  ? 102.976 138.495 93.813  1.00 68.28  ?  86   ILE   D N     1 
ATOM   15742 C  CA    . ILE   D 2 87  ? 103.808 137.998 92.720  1.00 63.34  ?  86   ILE   D CA    1 
ATOM   15743 C  C     . ILE   D 2 87  ? 104.828 136.989 93.240  1.00 70.67  ?  86   ILE   D C     1 
ATOM   15744 O  O     . ILE   D 2 87  ? 104.882 135.841 92.774  1.00 75.33  ?  86   ILE   D O     1 
ATOM   15745 C  CB    . ILE   D 2 87  ? 104.490 139.169 91.991  1.00 65.59  ?  86   ILE   D CB    1 
ATOM   15746 C  CG1   . ILE   D 2 87  ? 103.511 139.856 91.038  1.00 68.49  ?  86   ILE   D CG1   1 
ATOM   15747 C  CG2   . ILE   D 2 87  ? 105.717 138.685 91.231  1.00 62.71  ?  86   ILE   D CG2   1 
ATOM   15748 C  CD1   . ILE   D 2 87  ? 104.095 141.067 90.345  1.00 69.25  ?  86   ILE   D CD1   1 
ATOM   15749 N  N     . GLN   D 2 88  ? 105.586 137.374 94.274  1.00 77.29  ?  87   GLN   D N     1 
ATOM   15750 C  CA    . GLN   D 2 88  ? 106.686 136.565 94.784  1.00 70.55  ?  87   GLN   D CA    1 
ATOM   15751 C  C     . GLN   D 2 88  ? 106.232 135.267 95.432  1.00 72.90  ?  87   GLN   D C     1 
ATOM   15752 O  O     . GLN   D 2 88  ? 107.071 134.397 95.678  1.00 82.62  ?  87   GLN   D O     1 
ATOM   15753 C  CB    . GLN   D 2 88  ? 107.506 137.373 95.786  1.00 72.08  ?  87   GLN   D CB    1 
ATOM   15754 C  CG    . GLN   D 2 88  ? 108.607 138.198 95.153  1.00 76.28  ?  87   GLN   D CG    1 
ATOM   15755 C  CD    . GLN   D 2 88  ? 109.803 137.362 94.757  1.00 79.51  ?  87   GLN   D CD    1 
ATOM   15756 O  OE1   . GLN   D 2 88  ? 110.255 137.403 93.613  1.00 85.25  ?  87   GLN   D OE1   1 
ATOM   15757 N  NE2   . GLN   D 2 88  ? 110.324 136.594 95.704  1.00 80.51  ?  87   GLN   D NE2   1 
ATOM   15758 N  N     . GLY   D 2 89  ? 104.950 135.121 95.746  1.00 72.69  ?  88   GLY   D N     1 
ATOM   15759 C  CA    . GLY   D 2 89  ? 104.475 133.851 96.244  1.00 72.67  ?  88   GLY   D CA    1 
ATOM   15760 C  C     . GLY   D 2 89  ? 104.599 132.764 95.199  1.00 78.60  ?  88   GLY   D C     1 
ATOM   15761 O  O     . GLY   D 2 89  ? 105.265 131.749 95.420  1.00 87.31  ?  88   GLY   D O     1 
ATOM   15762 N  N     . ARG   D 2 90  ? 103.990 132.989 94.037  1.00 70.56  ?  89   ARG   D N     1 
ATOM   15763 C  CA    . ARG   D 2 90  ? 103.944 131.978 92.990  1.00 67.12  ?  89   ARG   D CA    1 
ATOM   15764 C  C     . ARG   D 2 90  ? 105.166 131.980 92.088  1.00 73.37  ?  89   ARG   D C     1 
ATOM   15765 O  O     . ARG   D 2 90  ? 105.559 130.916 91.598  1.00 78.72  ?  89   ARG   D O     1 
ATOM   15766 C  CB    . ARG   D 2 90  ? 102.702 132.172 92.121  1.00 69.68  ?  89   ARG   D CB    1 
ATOM   15767 C  CG    . ARG   D 2 90  ? 102.643 133.513 91.407  1.00 71.66  ?  89   ARG   D CG    1 
ATOM   15768 C  CD    . ARG   D 2 90  ? 101.323 133.721 90.690  1.00 72.81  ?  89   ARG   D CD    1 
ATOM   15769 N  NE    . ARG   D 2 90  ? 100.230 133.886 91.638  1.00 75.22  ?  89   ARG   D NE    1 
ATOM   15770 C  CZ    . ARG   D 2 90  ? 99.757  135.064 92.016  1.00 75.06  ?  89   ARG   D CZ    1 
ATOM   15771 N  NH1   . ARG   D 2 90  ? 100.246 136.190 91.527  1.00 74.48  ?  89   ARG   D NH1   1 
ATOM   15772 N  NH2   . ARG   D 2 90  ? 98.770  135.114 92.905  1.00 73.92  ?  89   ARG   D NH2   1 
ATOM   15773 N  N     . SER   D 2 91  ? 105.774 133.142 91.850  1.00 78.57  ?  90   SER   D N     1 
ATOM   15774 C  CA    . SER   D 2 91  ? 106.730 133.254 90.751  1.00 72.73  ?  90   SER   D CA    1 
ATOM   15775 C  C     . SER   D 2 91  ? 107.961 132.364 90.905  1.00 77.11  ?  90   SER   D C     1 
ATOM   15776 O  O     . SER   D 2 91  ? 108.345 131.714 89.917  1.00 80.01  ?  90   SER   D O     1 
ATOM   15777 C  CB    . SER   D 2 91  ? 107.101 134.726 90.572  1.00 80.36  ?  90   SER   D CB    1 
ATOM   15778 O  OG    . SER   D 2 91  ? 105.941 135.537 90.533  1.00 88.39  ?  90   SER   D OG    1 
ATOM   15779 N  N     . PRO   D 2 92  ? 108.637 132.298 92.059  1.00 73.51  ?  91   PRO   D N     1 
ATOM   15780 C  CA    . PRO   D 2 92  ? 109.779 131.374 92.168  1.00 67.46  ?  91   PRO   D CA    1 
ATOM   15781 C  C     . PRO   D 2 92  ? 109.409 129.912 91.985  1.00 73.06  ?  91   PRO   D C     1 
ATOM   15782 O  O     . PRO   D 2 92  ? 110.214 129.145 91.442  1.00 78.41  ?  91   PRO   D O     1 
ATOM   15783 C  CB    . PRO   D 2 92  ? 110.319 131.646 93.580  1.00 70.25  ?  91   PRO   D CB    1 
ATOM   15784 C  CG    . PRO   D 2 92  ? 109.191 132.284 94.305  1.00 72.97  ?  91   PRO   D CG    1 
ATOM   15785 C  CD    . PRO   D 2 92  ? 108.499 133.112 93.277  1.00 74.56  ?  91   PRO   D CD    1 
ATOM   15786 N  N     . ASN   D 2 93  ? 108.216 129.498 92.419  1.00 78.40  ?  92   ASN   D N     1 
ATOM   15787 C  CA    . ASN   D 2 93  ? 107.827 128.099 92.288  1.00 70.94  ?  92   ASN   D CA    1 
ATOM   15788 C  C     . ASN   D 2 93  ? 107.550 127.705 90.844  1.00 74.54  ?  92   ASN   D C     1 
ATOM   15789 O  O     . ASN   D 2 93  ? 107.612 126.515 90.522  1.00 85.77  ?  92   ASN   D O     1 
ATOM   15790 C  CB    . ASN   D 2 93  ? 106.593 127.803 93.142  1.00 73.23  ?  92   ASN   D CB    1 
ATOM   15791 C  CG    . ASN   D 2 93  ? 106.944 127.193 94.482  1.00 80.96  ?  92   ASN   D CG    1 
ATOM   15792 O  OD1   . ASN   D 2 93  ? 108.103 126.887 94.753  1.00 84.05  ?  92   ASN   D OD1   1 
ATOM   15793 N  ND2   . ASN   D 2 93  ? 105.938 127.008 95.329  1.00 82.55  ?  92   ASN   D ND2   1 
ATOM   15794 N  N     . VAL   D 2 94  ? 107.247 128.664 89.974  1.00 69.75  ?  93   VAL   D N     1 
ATOM   15795 C  CA    . VAL   D 2 94  ? 106.948 128.380 88.577  1.00 66.93  ?  93   VAL   D CA    1 
ATOM   15796 C  C     . VAL   D 2 94  ? 108.165 128.597 87.688  1.00 69.28  ?  93   VAL   D C     1 
ATOM   15797 O  O     . VAL   D 2 94  ? 108.487 127.746 86.860  1.00 76.79  ?  93   VAL   D O     1 
ATOM   15798 C  CB    . VAL   D 2 94  ? 105.748 129.224 88.096  1.00 68.85  ?  93   VAL   D CB    1 
ATOM   15799 C  CG1   . VAL   D 2 94  ? 105.395 128.859 86.662  1.00 67.54  ?  93   VAL   D CG1   1 
ATOM   15800 C  CG2   . VAL   D 2 94  ? 104.559 129.010 89.010  1.00 69.82  ?  93   VAL   D CG2   1 
ATOM   15801 N  N     . ALA   D 2 95  ? 108.888 129.697 87.895  1.00 66.76  ?  94   ALA   D N     1 
ATOM   15802 C  CA    . ALA   D 2 95  ? 110.004 130.035 87.020  1.00 67.24  ?  94   ALA   D CA    1 
ATOM   15803 C  C     . ALA   D 2 95  ? 111.247 129.203 87.310  1.00 69.04  ?  94   ALA   D C     1 
ATOM   15804 O  O     . ALA   D 2 95  ? 111.965 128.818 86.381  1.00 77.76  ?  94   ALA   D O     1 
ATOM   15805 C  CB    . ALA   D 2 95  ? 110.325 131.524 87.140  1.00 67.86  ?  94   ALA   D CB    1 
ATOM   15806 N  N     . LEU   D 2 96  ? 111.523 128.917 88.580  1.00 63.22  ?  95   LEU   D N     1 
ATOM   15807 C  CA    . LEU   D 2 96  ? 112.789 128.304 88.958  1.00 60.54  ?  95   LEU   D CA    1 
ATOM   15808 C  C     . LEU   D 2 96  ? 112.712 126.800 89.168  1.00 66.73  ?  95   LEU   D C     1 
ATOM   15809 O  O     . LEU   D 2 96  ? 113.723 126.119 88.981  1.00 76.29  ?  95   LEU   D O     1 
ATOM   15810 C  CB    . LEU   D 2 96  ? 113.333 128.955 90.236  1.00 59.39  ?  95   LEU   D CB    1 
ATOM   15811 C  CG    . LEU   D 2 96  ? 113.478 130.479 90.220  1.00 63.01  ?  95   LEU   D CG    1 
ATOM   15812 C  CD1   . LEU   D 2 96  ? 114.033 130.982 91.543  1.00 61.12  ?  95   LEU   D CD1   1 
ATOM   15813 C  CD2   . LEU   D 2 96  ? 114.356 130.926 89.064  1.00 62.00  ?  95   LEU   D CD2   1 
ATOM   15814 N  N     . LEU   D 2 97  ? 111.563 126.271 89.593  1.00 67.23  ?  96   LEU   D N     1 
ATOM   15815 C  CA    . LEU   D 2 97  ? 111.478 124.854 89.943  1.00 62.60  ?  96   LEU   D CA    1 
ATOM   15816 C  C     . LEU   D 2 97  ? 111.814 123.923 88.784  1.00 66.06  ?  96   LEU   D C     1 
ATOM   15817 O  O     . LEU   D 2 97  ? 112.586 122.971 88.994  1.00 69.50  ?  96   LEU   D O     1 
ATOM   15818 C  CB    . LEU   D 2 97  ? 110.090 124.551 90.517  1.00 64.46  ?  96   LEU   D CB    1 
ATOM   15819 C  CG    . LEU   D 2 97  ? 109.972 124.578 92.041  1.00 64.18  ?  96   LEU   D CG    1 
ATOM   15820 C  CD1   . LEU   D 2 97  ? 108.840 123.682 92.506  1.00 65.06  ?  96   LEU   D CD1   1 
ATOM   15821 C  CD2   . LEU   D 2 97  ? 111.279 124.175 92.698  1.00 62.20  ?  96   LEU   D CD2   1 
ATOM   15822 N  N     . PRO   D 2 98  ? 111.297 124.118 87.557  1.00 64.38  ?  97   PRO   D N     1 
ATOM   15823 C  CA    . PRO   D 2 98  ? 111.642 123.194 86.467  1.00 61.73  ?  97   PRO   D CA    1 
ATOM   15824 C  C     . PRO   D 2 98  ? 113.049 123.383 85.912  1.00 69.60  ?  97   PRO   D C     1 
ATOM   15825 O  O     . PRO   D 2 98  ? 113.362 122.843 84.849  1.00 76.40  ?  97   PRO   D O     1 
ATOM   15826 C  CB    . PRO   D 2 98  ? 110.591 123.509 85.390  1.00 61.01  ?  97   PRO   D CB    1 
ATOM   15827 C  CG    . PRO   D 2 98  ? 109.570 124.376 86.053  1.00 58.31  ?  97   PRO   D CG    1 
ATOM   15828 C  CD    . PRO   D 2 98  ? 110.293 125.103 87.119  1.00 59.19  ?  97   PRO   D CD    1 
ATOM   15829 N  N     . LEU   D 2 99  ? 113.880 124.200 86.566  1.00 63.45  ?  98   LEU   D N     1 
ATOM   15830 C  CA    . LEU   D 2 99  ? 115.243 124.449 86.117  1.00 54.89  ?  98   LEU   D CA    1 
ATOM   15831 C  C     . LEU   D 2 99  ? 116.307 124.020 87.115  1.00 61.96  ?  98   LEU   D C     1 
ATOM   15832 O  O     . LEU   D 2 99  ? 117.470 123.883 86.725  1.00 72.43  ?  98   LEU   D O     1 
ATOM   15833 C  CB    . LEU   D 2 99  ? 115.448 125.941 85.803  1.00 54.61  ?  98   LEU   D CB    1 
ATOM   15834 C  CG    . LEU   D 2 99  ? 114.746 126.475 84.555  1.00 62.90  ?  98   LEU   D CG    1 
ATOM   15835 C  CD1   . LEU   D 2 99  ? 115.127 127.923 84.303  1.00 62.93  ?  98   LEU   D CD1   1 
ATOM   15836 C  CD2   . LEU   D 2 99  ? 115.076 125.610 83.351  1.00 62.59  ?  98   LEU   D CD2   1 
ATOM   15837 N  N     . ILE   D 2 100 ? 115.945 123.794 88.368  1.00 61.23  ?  99   ILE   D N     1 
ATOM   15838 C  CA    . ILE   D 2 100 ? 116.907 123.496 89.423  1.00 57.89  ?  99   ILE   D CA    1 
ATOM   15839 C  C     . ILE   D 2 100 ? 117.332 122.037 89.335  1.00 63.30  ?  99   ILE   D C     1 
ATOM   15840 O  O     . ILE   D 2 100 ? 116.517 121.156 89.042  1.00 68.57  ?  99   ILE   D O     1 
ATOM   15841 C  CB    . ILE   D 2 100 ? 116.290 123.824 90.794  1.00 60.75  ?  99   ILE   D CB    1 
ATOM   15842 C  CG1   . ILE   D 2 100 ? 116.191 125.337 90.975  1.00 61.57  ?  99   ILE   D CG1   1 
ATOM   15843 C  CG2   . ILE   D 2 100 ? 117.115 123.225 91.924  1.00 62.68  ?  99   ILE   D CG2   1 
ATOM   15844 C  CD1   . ILE   D 2 100 ? 115.235 125.753 92.058  1.00 64.94  ?  99   ILE   D CD1   1 
ATOM   15845 N  N     . SER   D 2 101 ? 118.616 121.767 89.599  1.00 68.76  ?  100  SER   D N     1 
ATOM   15846 C  CA    . SER   D 2 101 ? 119.140 120.413 89.487  1.00 64.54  ?  100  SER   D CA    1 
ATOM   15847 C  C     . SER   D 2 101 ? 119.878 119.970 90.743  1.00 69.30  ?  100  SER   D C     1 
ATOM   15848 O  O     . SER   D 2 101 ? 120.544 118.932 90.719  1.00 72.43  ?  100  SER   D O     1 
ATOM   15849 C  CB    . SER   D 2 101 ? 120.064 120.287 88.271  1.00 61.69  ?  100  SER   D CB    1 
ATOM   15850 O  OG    . SER   D 2 101 ? 120.989 121.360 88.225  1.00 76.87  ?  100  SER   D OG    1 
ATOM   15851 N  N     . ILE   D 2 102 ? 119.765 120.712 91.841  1.00 72.76  ?  101  ILE   D N     1 
ATOM   15852 C  CA    . ILE   D 2 102 ? 120.289 120.260 93.129  1.00 68.74  ?  101  ILE   D CA    1 
ATOM   15853 C  C     . ILE   D 2 102 ? 119.164 120.301 94.157  1.00 73.96  ?  101  ILE   D C     1 
ATOM   15854 O  O     . ILE   D 2 102 ? 118.372 121.254 94.170  1.00 82.63  ?  101  ILE   D O     1 
ATOM   15855 C  CB    . ILE   D 2 102 ? 121.493 121.104 93.579  1.00 68.28  ?  101  ILE   D CB    1 
ATOM   15856 C  CG1   . ILE   D 2 102 ? 121.194 122.597 93.443  1.00 74.89  ?  101  ILE   D CG1   1 
ATOM   15857 C  CG2   . ILE   D 2 102 ? 122.731 120.738 92.776  1.00 68.62  ?  101  ILE   D CG2   1 
ATOM   15858 C  CD1   . ILE   D 2 102 ? 122.286 123.487 93.997  1.00 71.27  ?  101  ILE   D CD1   1 
ATOM   15859 N  N     . PRO   D 2 103 ? 119.047 119.292 95.024  1.00 67.75  ?  102  PRO   D N     1 
ATOM   15860 C  CA    . PRO   D 2 103 ? 117.903 119.259 95.952  1.00 71.08  ?  102  PRO   D CA    1 
ATOM   15861 C  C     . PRO   D 2 103 ? 117.847 120.435 96.917  1.00 72.98  ?  102  PRO   D C     1 
ATOM   15862 O  O     . PRO   D 2 103 ? 116.747 120.841 97.316  1.00 83.42  ?  102  PRO   D O     1 
ATOM   15863 C  CB    . PRO   D 2 103 ? 118.095 117.924 96.691  1.00 70.18  ?  102  PRO   D CB    1 
ATOM   15864 C  CG    . PRO   D 2 103 ? 119.532 117.569 96.499  1.00 70.31  ?  102  PRO   D CG    1 
ATOM   15865 C  CD    . PRO   D 2 103 ? 119.930 118.125 95.175  1.00 65.44  ?  102  PRO   D CD    1 
ATOM   15866 N  N     . GLU   D 2 104 ? 119.001 120.931 97.378  1.00 67.63  ?  103  GLU   D N     1 
ATOM   15867 C  CA    . GLU   D 2 104 ? 118.998 121.986 98.390  1.00 67.23  ?  103  GLU   D CA    1 
ATOM   15868 C  C     . GLU   D 2 104 ? 118.364 123.258 97.846  1.00 72.90  ?  103  GLU   D C     1 
ATOM   15869 O  O     . GLU   D 2 104 ? 117.561 123.902 98.531  1.00 81.64  ?  103  GLU   D O     1 
ATOM   15870 C  CB    . GLU   D 2 104 ? 120.420 122.264 98.886  1.00 70.28  ?  103  GLU   D CB    1 
ATOM   15871 C  CG    . GLU   D 2 104 ? 121.414 122.546 97.769  1.00 75.08  ?  103  GLU   D CG    1 
ATOM   15872 C  CD    . GLU   D 2 104 ? 122.463 121.470 97.618  1.00 79.60  ?  103  GLU   D CD    1 
ATOM   15873 O  OE1   . GLU   D 2 104 ? 122.085 120.315 97.343  1.00 85.71  ?  103  GLU   D OE1   1 
ATOM   15874 O  OE2   . GLU   D 2 104 ? 123.664 121.782 97.759  1.00 84.71  ?  103  GLU   D OE2   1 
ATOM   15875 N  N     . LEU   D 2 105 ? 118.700 123.623 96.605  1.00 58.84  ?  104  LEU   D N     1 
ATOM   15876 C  CA    . LEU   D 2 105 ? 118.112 124.806 95.989  1.00 58.63  ?  104  LEU   D CA    1 
ATOM   15877 C  C     . LEU   D 2 105 ? 116.613 124.632 95.788  1.00 60.05  ?  104  LEU   D C     1 
ATOM   15878 O  O     . LEU   D 2 105 ? 115.839 125.575 95.987  1.00 72.51  ?  104  LEU   D O     1 
ATOM   15879 C  CB    . LEU   D 2 105 ? 118.804 125.100 94.659  1.00 61.43  ?  104  LEU   D CB    1 
ATOM   15880 C  CG    . LEU   D 2 105 ? 118.579 126.487 94.060  1.00 64.84  ?  104  LEU   D CG    1 
ATOM   15881 C  CD1   . LEU   D 2 105 ? 118.837 127.559 95.099  1.00 61.77  ?  104  LEU   D CD1   1 
ATOM   15882 C  CD2   . LEU   D 2 105 ? 119.469 126.687 92.849  1.00 63.21  ?  104  LEU   D CD2   1 
ATOM   15883 N  N     . GLU   D 2 106 ? 116.187 123.431 95.391  1.00 55.63  ?  105  GLU   D N     1 
ATOM   15884 C  CA    . GLU   D 2 106 ? 114.763 123.155 95.236  1.00 62.16  ?  105  GLU   D CA    1 
ATOM   15885 C  C     . GLU   D 2 106 ? 114.020 123.355 96.550  1.00 64.21  ?  105  GLU   D C     1 
ATOM   15886 O  O     . GLU   D 2 106 ? 112.989 124.042 96.601  1.00 78.52  ?  105  GLU   D O     1 
ATOM   15887 C  CB    . GLU   D 2 106 ? 114.567 121.729 94.722  1.00 63.30  ?  105  GLU   D CB    1 
ATOM   15888 C  CG    . GLU   D 2 106 ? 113.272 121.514 93.967  1.00 72.27  ?  105  GLU   D CG    1 
ATOM   15889 C  CD    . GLU   D 2 106 ? 113.169 120.126 93.374  1.00 78.90  ?  105  GLU   D CD    1 
ATOM   15890 O  OE1   . GLU   D 2 106 ? 112.738 119.198 94.091  1.00 77.45  ?  105  GLU   D OE1   1 
ATOM   15891 O  OE2   . GLU   D 2 106 ? 113.520 119.962 92.187  1.00 81.60  ?  105  GLU   D OE2   1 
ATOM   15892 N  N     . THR   D 2 107 ? 114.538 122.762 97.629  1.00 50.79  ?  106  THR   D N     1 
ATOM   15893 C  CA    . THR   D 2 107 ? 113.890 122.895 98.930  1.00 53.07  ?  106  THR   D CA    1 
ATOM   15894 C  C     . THR   D 2 107 ? 113.870 124.347 99.388  1.00 57.79  ?  106  THR   D C     1 
ATOM   15895 O  O     . THR   D 2 107 ? 112.874 124.814 99.959  1.00 64.04  ?  106  THR   D O     1 
ATOM   15896 C  CB    . THR   D 2 107 ? 114.592 122.014 99.962  1.00 60.33  ?  106  THR   D CB    1 
ATOM   15897 O  OG1   . THR   D 2 107 ? 114.977 120.776 99.351  1.00 65.45  ?  106  THR   D OG1   1 
ATOM   15898 C  CG2   . THR   D 2 107 ? 113.668 121.727 101.133 1.00 64.38  ?  106  THR   D CG2   1 
ATOM   15899 N  N     . TRP   D 2 108 ? 114.960 125.080 99.143  1.00 54.09  ?  107  TRP   D N     1 
ATOM   15900 C  CA    . TRP   D 2 108 ? 114.987 126.490 99.510  1.00 46.61  ?  107  TRP   D CA    1 
ATOM   15901 C  C     . TRP   D 2 108 ? 113.938 127.281 98.742  1.00 49.96  ?  107  TRP   D C     1 
ATOM   15902 O  O     . TRP   D 2 108 ? 113.273 128.152 99.311  1.00 61.95  ?  107  TRP   D O     1 
ATOM   15903 C  CB    . TRP   D 2 108 ? 116.373 127.085 99.271  1.00 47.84  ?  107  TRP   D CB    1 
ATOM   15904 C  CG    . TRP   D 2 108 ? 116.361 128.583 99.302  1.00 51.53  ?  107  TRP   D CG    1 
ATOM   15905 C  CD1   . TRP   D 2 108 ? 116.775 129.426 98.315  1.00 55.70  ?  107  TRP   D CD1   1 
ATOM   15906 C  CD2   . TRP   D 2 108 ? 115.894 129.416 100.371 1.00 53.60  ?  107  TRP   D CD2   1 
ATOM   15907 N  NE1   . TRP   D 2 108 ? 116.601 130.731 98.704  1.00 56.47  ?  107  TRP   D NE1   1 
ATOM   15908 C  CE2   . TRP   D 2 108 ? 116.060 130.751 99.962  1.00 55.39  ?  107  TRP   D CE2   1 
ATOM   15909 C  CE3   . TRP   D 2 108 ? 115.352 129.161 101.635 1.00 56.82  ?  107  TRP   D CE3   1 
ATOM   15910 C  CZ2   . TRP   D 2 108 ? 115.708 131.828 100.771 1.00 59.45  ?  107  TRP   D CZ2   1 
ATOM   15911 C  CZ3   . TRP   D 2 108 ? 115.001 130.230 102.435 1.00 57.84  ?  107  TRP   D CZ3   1 
ATOM   15912 C  CH2   . TRP   D 2 108 ? 115.181 131.547 102.001 1.00 55.92  ?  107  TRP   D CH2   1 
ATOM   15913 N  N     . VAL   D 2 109 ? 113.780 127.000 97.448  1.00 47.77  ?  108  VAL   D N     1 
ATOM   15914 C  CA    . VAL   D 2 109 ? 112.788 127.716 96.649  1.00 51.47  ?  108  VAL   D CA    1 
ATOM   15915 C  C     . VAL   D 2 109 ? 111.382 127.423 97.158  1.00 57.66  ?  108  VAL   D C     1 
ATOM   15916 O  O     . VAL   D 2 109 ? 110.541 128.327 97.262  1.00 72.19  ?  108  VAL   D O     1 
ATOM   15917 C  CB    . VAL   D 2 109 ? 112.946 127.358 95.159  1.00 46.89  ?  108  VAL   D CB    1 
ATOM   15918 C  CG1   . VAL   D 2 109 ? 111.693 127.722 94.380  1.00 46.38  ?  108  VAL   D CG1   1 
ATOM   15919 C  CG2   . VAL   D 2 109 ? 114.157 128.067 94.580  1.00 46.40  ?  108  VAL   D CG2   1 
ATOM   15920 N  N     . GLU   D 2 110 ? 111.108 126.161 97.495  1.00 58.17  ?  109  GLU   D N     1 
ATOM   15921 C  CA    . GLU   D 2 110 ? 109.794 125.814 98.031  1.00 57.13  ?  109  GLU   D CA    1 
ATOM   15922 C  C     . GLU   D 2 110 ? 109.518 126.549 99.341  1.00 64.95  ?  109  GLU   D C     1 
ATOM   15923 O  O     . GLU   D 2 110 ? 108.443 127.138 99.527  1.00 73.41  ?  109  GLU   D O     1 
ATOM   15924 C  CB    . GLU   D 2 110 ? 109.693 124.302 98.235  1.00 61.15  ?  109  GLU   D CB    1 
ATOM   15925 C  CG    . GLU   D 2 110 ? 109.536 123.502 96.954  1.00 69.72  ?  109  GLU   D CG    1 
ATOM   15926 C  CD    . GLU   D 2 110 ? 110.154 122.121 97.045  1.00 81.35  ?  109  GLU   D CD    1 
ATOM   15927 O  OE1   . GLU   D 2 110 ? 111.388 122.016 97.156  1.00 81.32  ?  109  GLU   D OE1   1 
ATOM   15928 O  OE2   . GLU   D 2 110 ? 109.408 121.130 97.009  1.00 84.47  ?  109  GLU   D OE2   1 
ATOM   15929 N  N     . THR   D 2 111 ? 110.491 126.532 100.259 1.00 49.67  ?  110  THR   D N     1 
ATOM   15930 C  CA    . THR   D 2 111 ? 110.317 127.209 101.542 1.00 47.73  ?  110  THR   D CA    1 
ATOM   15931 C  C     . THR   D 2 111 ? 110.136 128.710 101.353 1.00 58.46  ?  110  THR   D C     1 
ATOM   15932 O  O     . THR   D 2 111 ? 109.317 129.340 102.033 1.00 70.68  ?  110  THR   D O     1 
ATOM   15933 C  CB    . THR   D 2 111 ? 111.516 126.927 102.447 1.00 50.62  ?  110  THR   D CB    1 
ATOM   15934 O  OG1   . THR   D 2 111 ? 111.959 125.579 102.249 1.00 59.81  ?  110  THR   D OG1   1 
ATOM   15935 C  CG2   . THR   D 2 111 ? 111.145 127.122 103.905 1.00 54.77  ?  110  THR   D CG2   1 
ATOM   15936 N  N     . TRP   D 2 112 ? 110.898 129.295 100.430 1.00 54.68  ?  111  TRP   D N     1 
ATOM   15937 C  CA    . TRP   D 2 112 ? 110.824 130.725 100.163 1.00 55.81  ?  111  TRP   D CA    1 
ATOM   15938 C  C     . TRP   D 2 112 ? 109.456 131.116 99.610  1.00 57.33  ?  111  TRP   D C     1 
ATOM   15939 O  O     . TRP   D 2 112 ? 108.865 132.117 100.038 1.00 63.23  ?  111  TRP   D O     1 
ATOM   15940 C  CB    . TRP   D 2 112 ? 111.971 131.079 99.211  1.00 50.32  ?  111  TRP   D CB    1 
ATOM   15941 C  CG    . TRP   D 2 112 ? 111.950 132.397 98.517  1.00 54.98  ?  111  TRP   D CG    1 
ATOM   15942 C  CD1   . TRP   D 2 112 ? 111.318 133.537 98.909  1.00 56.82  ?  111  TRP   D CD1   1 
ATOM   15943 C  CD2   . TRP   D 2 112 ? 112.637 132.714 97.304  1.00 58.58  ?  111  TRP   D CD2   1 
ATOM   15944 N  NE1   . TRP   D 2 112 ? 111.564 134.543 98.008  1.00 60.10  ?  111  TRP   D NE1   1 
ATOM   15945 C  CE2   . TRP   D 2 112 ? 112.356 134.056 97.004  1.00 59.45  ?  111  TRP   D CE2   1 
ATOM   15946 C  CE3   . TRP   D 2 112 ? 113.461 131.987 96.439  1.00 59.71  ?  111  TRP   D CE3   1 
ATOM   15947 C  CZ2   . TRP   D 2 112 ? 112.878 134.692 95.882  1.00 58.07  ?  111  TRP   D CZ2   1 
ATOM   15948 C  CZ3   . TRP   D 2 112 ? 113.960 132.613 95.317  1.00 59.10  ?  111  TRP   D CZ3   1 
ATOM   15949 C  CH2   . TRP   D 2 112 ? 113.666 133.950 95.046  1.00 57.38  ?  111  TRP   D CH2   1 
ATOM   15950 N  N     . ALA   D 2 113 ? 108.920 130.319 98.682  1.00 48.56  ?  112  ALA   D N     1 
ATOM   15951 C  CA    . ALA   D 2 113 ? 107.581 130.588 98.166  1.00 49.59  ?  112  ALA   D CA    1 
ATOM   15952 C  C     . ALA   D 2 113 ? 106.532 130.478 99.267  1.00 59.62  ?  112  ALA   D C     1 
ATOM   15953 O  O     . ALA   D 2 113 ? 105.608 131.301 99.345  1.00 67.74  ?  112  ALA   D O     1 
ATOM   15954 C  CB    . ALA   D 2 113 ? 107.259 129.633 97.019  1.00 50.71  ?  112  ALA   D CB    1 
ATOM   15955 N  N     . PHE   D 2 114 ? 106.659 129.469 100.134 1.00 52.99  ?  113  PHE   D N     1 
ATOM   15956 C  CA    . PHE   D 2 114 ? 105.710 129.331 101.236 1.00 48.80  ?  113  PHE   D CA    1 
ATOM   15957 C  C     . PHE   D 2 114 ? 105.768 130.536 102.173 1.00 57.85  ?  113  PHE   D C     1 
ATOM   15958 O  O     . PHE   D 2 114 ? 104.730 131.035 102.633 1.00 69.35  ?  113  PHE   D O     1 
ATOM   15959 C  CB    . PHE   D 2 114 ? 105.986 128.036 101.999 1.00 46.28  ?  113  PHE   D CB    1 
ATOM   15960 C  CG    . PHE   D 2 114 ? 105.317 127.968 103.338 1.00 50.29  ?  113  PHE   D CG    1 
ATOM   15961 C  CD1   . PHE   D 2 114 ? 103.960 127.723 103.435 1.00 52.38  ?  113  PHE   D CD1   1 
ATOM   15962 C  CD2   . PHE   D 2 114 ? 106.039 128.179 104.498 1.00 51.96  ?  113  PHE   D CD2   1 
ATOM   15963 C  CE1   . PHE   D 2 114 ? 103.343 127.664 104.664 1.00 56.50  ?  113  PHE   D CE1   1 
ATOM   15964 C  CE2   . PHE   D 2 114 ? 105.427 128.121 105.731 1.00 59.58  ?  113  PHE   D CE2   1 
ATOM   15965 C  CZ    . PHE   D 2 114 ? 104.077 127.865 105.813 1.00 61.49  ?  113  PHE   D CZ    1 
ATOM   15966 N  N     . SER   D 2 115 ? 106.977 131.018 102.466 1.00 48.76  ?  114  SER   D N     1 
ATOM   15967 C  CA    . SER   D 2 115 ? 107.113 132.187 103.328 1.00 50.86  ?  114  SER   D CA    1 
ATOM   15968 C  C     . SER   D 2 115 ? 106.499 133.424 102.683 1.00 56.56  ?  114  SER   D C     1 
ATOM   15969 O  O     . SER   D 2 115 ? 105.905 134.265 103.369 1.00 65.72  ?  114  SER   D O     1 
ATOM   15970 C  CB    . SER   D 2 115 ? 108.584 132.421 103.666 1.00 49.94  ?  114  SER   D CB    1 
ATOM   15971 O  OG    . SER   D 2 115 ? 109.209 133.213 102.679 1.00 70.04  ?  114  SER   D OG    1 
ATOM   15972 N  N     . GLU   D 2 116 ? 106.631 133.557 101.362 1.00 48.86  ?  115  GLU   D N     1 
ATOM   15973 C  CA    . GLU   D 2 116 ? 105.986 134.681 100.688 1.00 46.05  ?  115  GLU   D CA    1 
ATOM   15974 C  C     . GLU   D 2 116 ? 104.465 134.577 100.769 1.00 57.17  ?  115  GLU   D C     1 
ATOM   15975 O  O     . GLU   D 2 116 ? 103.771 135.596 100.882 1.00 68.46  ?  115  GLU   D O     1 
ATOM   15976 C  CB    . GLU   D 2 116 ? 106.446 134.770 99.233  1.00 45.22  ?  115  GLU   D CB    1 
ATOM   15977 C  CG    . GLU   D 2 116 ? 107.954 134.909 99.021  1.00 53.28  ?  115  GLU   D CG    1 
ATOM   15978 C  CD    . GLU   D 2 116 ? 108.549 136.210 99.544  1.00 64.09  ?  115  GLU   D CD    1 
ATOM   15979 O  OE1   . GLU   D 2 116 ? 107.812 137.062 100.078 1.00 71.31  ?  115  GLU   D OE1   1 
ATOM   15980 O  OE2   . GLU   D 2 116 ? 109.777 136.384 99.411  1.00 62.40  ?  115  GLU   D OE2   1 
ATOM   15981 N  N     . THR   D 2 117 ? 103.925 133.356 100.707 1.00 56.47  ?  116  THR   D N     1 
ATOM   15982 C  CA    . THR   D 2 117 ? 102.485 133.194 100.915 1.00 47.22  ?  116  THR   D CA    1 
ATOM   15983 C  C     . THR   D 2 117 ? 102.083 133.622 102.324 1.00 46.43  ?  116  THR   D C     1 
ATOM   15984 O  O     . THR   D 2 117 ? 101.018 134.222 102.525 1.00 60.22  ?  116  THR   D O     1 
ATOM   15985 C  CB    . THR   D 2 117 ? 102.057 131.747 100.662 1.00 52.99  ?  116  THR   D CB    1 
ATOM   15986 O  OG1   . THR   D 2 117 ? 102.679 130.883 101.621 1.00 62.93  ?  116  THR   D OG1   1 
ATOM   15987 C  CG2   . THR   D 2 117 ? 102.429 131.308 99.256  1.00 50.30  ?  116  THR   D CG2   1 
ATOM   15988 N  N     . ILE   D 2 118 ? 102.918 133.303 103.314 1.00 47.84  ?  117  ILE   D N     1 
ATOM   15989 C  CA    . ILE   D 2 118 ? 102.658 133.760 104.680 1.00 45.10  ?  117  ILE   D CA    1 
ATOM   15990 C  C     . ILE   D 2 118 ? 102.647 135.285 104.740 1.00 45.28  ?  117  ILE   D C     1 
ATOM   15991 O  O     . ILE   D 2 118 ? 101.788 135.892 105.393 1.00 50.23  ?  117  ILE   D O     1 
ATOM   15992 C  CB    . ILE   D 2 118 ? 103.688 133.157 105.652 1.00 47.89  ?  117  ILE   D CB    1 
ATOM   15993 C  CG1   . ILE   D 2 118 ? 103.383 131.683 105.914 1.00 55.39  ?  117  ILE   D CG1   1 
ATOM   15994 C  CG2   . ILE   D 2 118 ? 103.720 133.942 106.958 1.00 47.25  ?  117  ILE   D CG2   1 
ATOM   15995 C  CD1   . ILE   D 2 118 ? 102.192 131.462 106.807 1.00 58.83  ?  117  ILE   D CD1   1 
ATOM   15996 N  N     . HIS   D 2 119 ? 103.569 135.925 104.019 1.00 53.37  ?  118  HIS   D N     1 
ATOM   15997 C  CA    . HIS   D 2 119 ? 103.584 137.384 103.949 1.00 45.08  ?  118  HIS   D CA    1 
ATOM   15998 C  C     . HIS   D 2 119 ? 102.297 137.931 103.342 1.00 46.31  ?  118  HIS   D C     1 
ATOM   15999 O  O     . HIS   D 2 119 ? 101.753 138.935 103.819 1.00 57.19  ?  118  HIS   D O     1 
ATOM   16000 C  CB    . HIS   D 2 119 ? 104.780 137.856 103.132 1.00 47.83  ?  118  HIS   D CB    1 
ATOM   16001 C  CG    . HIS   D 2 119 ? 106.101 137.583 103.774 1.00 51.16  ?  118  HIS   D CG    1 
ATOM   16002 N  ND1   . HIS   D 2 119 ? 107.294 137.948 103.192 1.00 48.60  ?  118  HIS   D ND1   1 
ATOM   16003 C  CD2   . HIS   D 2 119 ? 106.419 136.985 104.945 1.00 47.55  ?  118  HIS   D CD2   1 
ATOM   16004 C  CE1   . HIS   D 2 119 ? 108.292 137.583 103.975 1.00 48.37  ?  118  HIS   D CE1   1 
ATOM   16005 N  NE2   . HIS   D 2 119 ? 107.788 136.997 105.045 1.00 49.98  ?  118  HIS   D NE2   1 
ATOM   16006 N  N     . SER   D 2 120 ? 101.815 137.303 102.269 1.00 48.79  ?  119  SER   D N     1 
ATOM   16007 C  CA    . SER   D 2 120 ? 100.571 137.755 101.651 1.00 48.32  ?  119  SER   D CA    1 
ATOM   16008 C  C     . SER   D 2 120 ? 99.399  137.629 102.618 1.00 54.62  ?  119  SER   D C     1 
ATOM   16009 O  O     . SER   D 2 120 ? 98.540  138.519 102.691 1.00 63.11  ?  119  SER   D O     1 
ATOM   16010 C  CB    . SER   D 2 120 ? 100.297 136.963 100.374 1.00 50.67  ?  119  SER   D CB    1 
ATOM   16011 O  OG    . SER   D 2 120 ? 101.410 137.001 99.499  1.00 62.47  ?  119  SER   D OG    1 
ATOM   16012 N  N     . ARG   D 2 121 ? 99.347  136.525 103.366 1.00 56.16  ?  120  ARG   D N     1 
ATOM   16013 C  CA    . ARG   D 2 121 ? 98.294  136.366 104.363 1.00 48.40  ?  120  ARG   D CA    1 
ATOM   16014 C  C     . ARG   D 2 121 ? 98.388  137.445 105.436 1.00 53.14  ?  120  ARG   D C     1 
ATOM   16015 O  O     . ARG   D 2 121 ? 97.366  137.961 105.899 1.00 58.53  ?  120  ARG   D O     1 
ATOM   16016 C  CB    . ARG   D 2 121 ? 98.361  134.971 104.983 1.00 53.14  ?  120  ARG   D CB    1 
ATOM   16017 C  CG    . ARG   D 2 121 ? 97.773  134.874 106.382 1.00 60.14  ?  120  ARG   D CG    1 
ATOM   16018 C  CD    . ARG   D 2 121 ? 97.609  133.429 106.825 1.00 60.81  ?  120  ARG   D CD    1 
ATOM   16019 N  NE    . ARG   D 2 121 ? 96.366  132.845 106.336 1.00 58.70  ?  120  ARG   D NE    1 
ATOM   16020 C  CZ    . ARG   D 2 121 ? 96.254  132.158 105.208 1.00 63.77  ?  120  ARG   D CZ    1 
ATOM   16021 N  NH1   . ARG   D 2 121 ? 97.297  131.938 104.425 1.00 64.79  ?  120  ARG   D NH1   1 
ATOM   16022 N  NH2   . ARG   D 2 121 ? 95.064  131.681 104.855 1.00 61.27  ?  120  ARG   D NH2   1 
ATOM   16023 N  N     . SER   D 2 122 ? 99.607  137.811 105.835 1.00 62.86  ?  121  SER   D N     1 
ATOM   16024 C  CA    . SER   D 2 122 ? 99.768  138.874 106.826 1.00 59.57  ?  121  SER   D CA    1 
ATOM   16025 C  C     . SER   D 2 122 ? 99.288  140.218 106.289 1.00 58.02  ?  121  SER   D C     1 
ATOM   16026 O  O     . SER   D 2 122 ? 98.665  141.002 107.017 1.00 64.57  ?  121  SER   D O     1 
ATOM   16027 C  CB    . SER   D 2 122 ? 101.226 138.968 107.259 1.00 61.74  ?  121  SER   D CB    1 
ATOM   16028 O  OG    . SER   D 2 122 ? 102.004 139.616 106.267 1.00 69.16  ?  121  SER   D OG    1 
ATOM   16029 N  N     . TYR   D 2 123 ? 99.586  140.506 105.021 1.00 58.88  ?  122  TYR   D N     1 
ATOM   16030 C  CA    . TYR   D 2 123 ? 99.102  141.742 104.411 1.00 52.02  ?  122  TYR   D CA    1 
ATOM   16031 C  C     . TYR   D 2 123 ? 97.580  141.772 104.372 1.00 51.46  ?  122  TYR   D C     1 
ATOM   16032 O  O     . TYR   D 2 123 ? 96.962  142.805 104.663 1.00 62.12  ?  122  TYR   D O     1 
ATOM   16033 C  CB    . TYR   D 2 123 ? 99.675  141.901 103.003 1.00 47.31  ?  122  TYR   D CB    1 
ATOM   16034 C  CG    . TYR   D 2 123 ? 101.156 142.182 102.976 1.00 54.37  ?  122  TYR   D CG    1 
ATOM   16035 C  CD1   . TYR   D 2 123 ? 101.728 143.055 103.886 1.00 57.35  ?  122  TYR   D CD1   1 
ATOM   16036 C  CD2   . TYR   D 2 123 ? 101.981 141.577 102.043 1.00 59.98  ?  122  TYR   D CD2   1 
ATOM   16037 C  CE1   . TYR   D 2 123 ? 103.081 143.316 103.872 1.00 59.05  ?  122  TYR   D CE1   1 
ATOM   16038 C  CE2   . TYR   D 2 123 ? 103.337 141.832 102.019 1.00 64.18  ?  122  TYR   D CE2   1 
ATOM   16039 C  CZ    . TYR   D 2 123 ? 103.882 142.701 102.937 1.00 64.21  ?  122  TYR   D CZ    1 
ATOM   16040 O  OH    . TYR   D 2 123 ? 105.232 142.959 102.915 1.00 70.82  ?  122  TYR   D OH    1 
ATOM   16041 N  N     . THR   D 2 124 ? 96.960  140.645 104.015 1.00 61.97  ?  123  THR   D N     1 
ATOM   16042 C  CA    . THR   D 2 124 ? 95.503  140.564 104.041 1.00 66.70  ?  123  THR   D CA    1 
ATOM   16043 C  C     . THR   D 2 124 ? 94.968  140.787 105.451 1.00 63.82  ?  123  THR   D C     1 
ATOM   16044 O  O     . THR   D 2 124 ? 93.960  141.476 105.640 1.00 71.72  ?  123  THR   D O     1 
ATOM   16045 C  CB    . THR   D 2 124 ? 95.043  139.210 103.495 1.00 73.01  ?  123  THR   D CB    1 
ATOM   16046 O  OG1   . THR   D 2 124 ? 95.137  139.213 102.065 1.00 75.23  ?  123  THR   D OG1   1 
ATOM   16047 C  CG2   . THR   D 2 124 ? 93.605  138.919 103.898 1.00 65.32  ?  123  THR   D CG2   1 
ATOM   16048 N  N     . HIS   D 2 125 ? 95.638  140.212 106.451 1.00 68.89  ?  124  HIS   D N     1 
ATOM   16049 C  CA    . HIS   D 2 125 ? 95.234  140.393 107.843 1.00 65.36  ?  124  HIS   D CA    1 
ATOM   16050 C  C     . HIS   D 2 125 ? 95.249  141.867 108.232 1.00 66.40  ?  124  HIS   D C     1 
ATOM   16051 O  O     . HIS   D 2 125 ? 94.282  142.383 108.808 1.00 68.30  ?  124  HIS   D O     1 
ATOM   16052 C  CB    . HIS   D 2 125 ? 96.166  139.577 108.742 1.00 65.31  ?  124  HIS   D CB    1 
ATOM   16053 C  CG    . HIS   D 2 125 ? 95.809  139.610 110.195 1.00 68.84  ?  124  HIS   D CG    1 
ATOM   16054 N  ND1   . HIS   D 2 125 ? 94.745  138.909 110.718 1.00 75.36  ?  124  HIS   D ND1   1 
ATOM   16055 C  CD2   . HIS   D 2 125 ? 96.394  140.241 111.240 1.00 68.67  ?  124  HIS   D CD2   1 
ATOM   16056 C  CE1   . HIS   D 2 125 ? 94.682  139.116 112.021 1.00 72.20  ?  124  HIS   D CE1   1 
ATOM   16057 N  NE2   . HIS   D 2 125 ? 95.670  139.922 112.363 1.00 69.42  ?  124  HIS   D NE2   1 
ATOM   16058 N  N     . ILE   D 2 126 ? 96.336  142.567 107.900 1.00 64.38  ?  125  ILE   D N     1 
ATOM   16059 C  CA    . ILE   D 2 126 ? 96.450  143.984 108.245 1.00 56.55  ?  125  ILE   D CA    1 
ATOM   16060 C  C     . ILE   D 2 126 ? 95.372  144.796 107.536 1.00 59.20  ?  125  ILE   D C     1 
ATOM   16061 O  O     . ILE   D 2 126 ? 94.702  145.643 108.144 1.00 64.70  ?  125  ILE   D O     1 
ATOM   16062 C  CB    . ILE   D 2 126 ? 97.859  144.508 107.913 1.00 57.80  ?  125  ILE   D CB    1 
ATOM   16063 C  CG1   . ILE   D 2 126 ? 98.908  143.810 108.777 1.00 62.39  ?  125  ILE   D CG1   1 
ATOM   16064 C  CG2   . ILE   D 2 126 ? 97.928  146.011 108.118 1.00 57.78  ?  125  ILE   D CG2   1 
ATOM   16065 C  CD1   . ILE   D 2 126 ? 100.328 144.083 108.343 1.00 60.74  ?  125  ILE   D CD1   1 
ATOM   16066 N  N     . ILE   D 2 127 ? 95.184  144.544 106.237 1.00 70.61  ?  126  ILE   D N     1 
ATOM   16067 C  CA    . ILE   D 2 127 ? 94.206  145.306 105.465 1.00 67.66  ?  126  ILE   D CA    1 
ATOM   16068 C  C     . ILE   D 2 127 ? 92.804  145.088 106.014 1.00 67.87  ?  126  ILE   D C     1 
ATOM   16069 O  O     . ILE   D 2 127 ? 92.030  146.040 106.170 1.00 76.27  ?  126  ILE   D O     1 
ATOM   16070 C  CB    . ILE   D 2 127 ? 94.294  144.935 103.973 1.00 67.54  ?  126  ILE   D CB    1 
ATOM   16071 C  CG1   . ILE   D 2 127 ? 95.486  145.626 103.314 1.00 67.48  ?  126  ILE   D CG1   1 
ATOM   16072 C  CG2   . ILE   D 2 127 ? 93.004  145.297 103.249 1.00 64.79  ?  126  ILE   D CG2   1 
ATOM   16073 C  CD1   . ILE   D 2 127 ? 95.895  145.003 101.998 1.00 67.98  ?  126  ILE   D CD1   1 
ATOM   16074 N  N     . ARG   D 2 128 ? 92.462  143.839 106.336 1.00 74.47  ?  127  ARG   D N     1 
ATOM   16075 C  CA    . ARG   D 2 128 ? 91.147  143.536 106.882 1.00 73.52  ?  127  ARG   D CA    1 
ATOM   16076 C  C     . ARG   D 2 128 ? 90.961  144.136 108.268 1.00 70.75  ?  127  ARG   D C     1 
ATOM   16077 O  O     . ARG   D 2 128 ? 89.834  144.471 108.647 1.00 77.58  ?  127  ARG   D O     1 
ATOM   16078 C  CB    . ARG   D 2 128 ? 90.949  142.022 106.913 1.00 75.63  ?  127  ARG   D CB    1 
ATOM   16079 C  CG    . ARG   D 2 128 ? 89.590  141.558 107.388 1.00 77.29  ?  127  ARG   D CG    1 
ATOM   16080 C  CD    . ARG   D 2 128 ? 89.741  140.545 108.505 1.00 77.45  ?  127  ARG   D CD    1 
ATOM   16081 N  NE    . ARG   D 2 128 ? 90.399  139.328 108.045 1.00 80.80  ?  127  ARG   D NE    1 
ATOM   16082 C  CZ    . ARG   D 2 128 ? 89.857  138.429 107.232 1.00 81.30  ?  127  ARG   D CZ    1 
ATOM   16083 N  NH1   . ARG   D 2 128 ? 88.620  138.558 106.780 1.00 78.20  ?  127  ARG   D NH1   1 
ATOM   16084 N  NH2   . ARG   D 2 128 ? 90.575  137.370 106.867 1.00 80.95  ?  127  ARG   D NH2   1 
ATOM   16085 N  N     . ASN   D 2 129 ? 92.040  144.283 109.036 1.00 78.31  ?  128  ASN   D N     1 
ATOM   16086 C  CA    . ASN   D 2 129 ? 91.915  144.804 110.390 1.00 76.13  ?  128  ASN   D CA    1 
ATOM   16087 C  C     . ASN   D 2 129 ? 91.978  146.325 110.477 1.00 80.71  ?  128  ASN   D C     1 
ATOM   16088 O  O     . ASN   D 2 129 ? 91.616  146.877 111.521 1.00 83.48  ?  128  ASN   D O     1 
ATOM   16089 C  CB    . ASN   D 2 129 ? 92.999  144.200 111.288 1.00 82.47  ?  128  ASN   D CB    1 
ATOM   16090 C  CG    . ASN   D 2 129 ? 92.503  142.999 112.066 1.00 87.39  ?  128  ASN   D CG    1 
ATOM   16091 O  OD1   . ASN   D 2 129 ? 92.566  141.866 111.589 1.00 89.20  ?  128  ASN   D OD1   1 
ATOM   16092 N  ND2   . ASN   D 2 129 ? 92.001  143.241 113.271 1.00 84.82  ?  128  ASN   D ND2   1 
ATOM   16093 N  N     . ILE   D 2 130 ? 92.419  147.023 109.430 1.00 89.85  ?  129  ILE   D N     1 
ATOM   16094 C  CA    . ILE   D 2 130 ? 92.519  148.480 109.484 1.00 83.93  ?  129  ILE   D CA    1 
ATOM   16095 C  C     . ILE   D 2 130 ? 91.517  149.195 108.589 1.00 83.93  ?  129  ILE   D C     1 
ATOM   16096 O  O     . ILE   D 2 130 ? 91.423  150.431 108.666 1.00 89.92  ?  129  ILE   D O     1 
ATOM   16097 C  CB    . ILE   D 2 130 ? 93.945  148.968 109.150 1.00 85.15  ?  129  ILE   D CB    1 
ATOM   16098 C  CG1   . ILE   D 2 130 ? 94.237  148.778 107.660 1.00 87.83  ?  129  ILE   D CG1   1 
ATOM   16099 C  CG2   . ILE   D 2 130 ? 94.973  148.254 110.014 1.00 87.38  ?  129  ILE   D CG2   1 
ATOM   16100 C  CD1   . ILE   D 2 130 ? 94.967  149.940 107.029 1.00 86.99  ?  129  ILE   D CD1   1 
ATOM   16101 N  N     . VAL   D 2 131 ? 90.770  148.482 107.752 1.00 97.32  ?  130  VAL   D N     1 
ATOM   16102 C  CA    . VAL   D 2 131 ? 89.881  149.103 106.775 1.00 96.25  ?  130  VAL   D CA    1 
ATOM   16103 C  C     . VAL   D 2 131 ? 88.499  148.473 106.892 1.00 98.98  ?  130  VAL   D C     1 
ATOM   16104 O  O     . VAL   D 2 131 ? 88.379  147.266 107.126 1.00 102.76 ?  130  VAL   D O     1 
ATOM   16105 C  CB    . VAL   D 2 131 ? 90.445  148.968 105.341 1.00 94.98  ?  130  VAL   D CB    1 
ATOM   16106 C  CG1   . VAL   D 2 131 ? 89.397  149.316 104.299 1.00 97.63  ?  130  VAL   D CG1   1 
ATOM   16107 C  CG2   . VAL   D 2 131 ? 91.667  149.863 105.175 1.00 94.78  ?  130  VAL   D CG2   1 
ATOM   16108 N  N     . ASN   D 2 132 ? 87.449  149.285 106.759 1.00 117.38 ?  131  ASN   D N     1 
ATOM   16109 C  CA    . ASN   D 2 132 ? 86.047  148.802 106.927 1.00 117.85 ?  131  ASN   D CA    1 
ATOM   16110 C  C     . ASN   D 2 132 ? 85.742  147.637 105.981 1.00 119.42 ?  131  ASN   D C     1 
ATOM   16111 O  O     . ASN   D 2 132 ? 85.179  146.636 106.460 1.00 119.44 ?  131  ASN   D O     1 
ATOM   16112 C  CB    . ASN   D 2 132 ? 85.040  149.934 106.723 1.00 117.75 ?  131  ASN   D CB    1 
ATOM   16113 C  CG    . ASN   D 2 132 ? 85.054  150.938 107.855 1.00 122.18 ?  131  ASN   D CG    1 
ATOM   16114 O  OD1   . ASN   D 2 132 ? 84.530  150.674 108.933 1.00 121.83 ?  131  ASN   D OD1   1 
ATOM   16115 N  ND2   . ASN   D 2 132 ? 85.651  152.095 107.619 1.00 121.13 ?  131  ASN   D ND2   1 
ATOM   16116 N  N     . ASP   D 2 133 ? 86.049  147.770 104.690 1.00 122.03 ?  132  ASP   D N     1 
ATOM   16117 C  CA    . ASP   D 2 133 ? 85.870  146.681 103.722 1.00 123.30 ?  132  ASP   D CA    1 
ATOM   16118 C  C     . ASP   D 2 133 ? 87.165  146.474 102.938 1.00 121.42 ?  132  ASP   D C     1 
ATOM   16119 O  O     . ASP   D 2 133 ? 87.693  147.427 102.343 1.00 120.90 ?  132  ASP   D O     1 
ATOM   16120 C  CB    . ASP   D 2 133 ? 84.665  146.960 102.802 1.00 123.96 ?  132  ASP   D CB    1 
ATOM   16121 C  CG    . ASP   D 2 133 ? 84.838  148.185 101.893 1.00 123.13 ?  132  ASP   D CG    1 
ATOM   16122 O  OD1   . ASP   D 2 133 ? 85.882  148.788 101.771 1.00 122.07 ?  132  ASP   D OD1   1 
ATOM   16123 O  OD2   . ASP   D 2 133 ? 83.877  148.612 101.261 1.00 122.95 ?  132  ASP   D OD2   1 
ATOM   16124 N  N     . PRO   D 2 134 ? 87.751  145.283 102.905 1.00 105.79 ?  133  PRO   D N     1 
ATOM   16125 C  CA    . PRO   D 2 134 ? 89.039  145.136 102.210 1.00 106.21 ?  133  PRO   D CA    1 
ATOM   16126 C  C     . PRO   D 2 134 ? 88.944  145.122 100.689 1.00 106.84 ?  133  PRO   D C     1 
ATOM   16127 O  O     . PRO   D 2 134 ? 89.973  144.958 100.022 1.00 108.53 ?  133  PRO   D O     1 
ATOM   16128 C  CB    . PRO   D 2 134 ? 89.559  143.795 102.736 1.00 103.60 ?  133  PRO   D CB    1 
ATOM   16129 C  CG    . PRO   D 2 134 ? 88.330  143.029 103.067 1.00 103.44 ?  133  PRO   D CG    1 
ATOM   16130 C  CD    . PRO   D 2 134 ? 87.246  144.010 103.434 1.00 103.97 ?  133  PRO   D CD    1 
ATOM   16131 N  N     . SER   D 2 135 ? 87.742  145.220 100.121 1.00 104.16 ?  134  SER   D N     1 
ATOM   16132 C  CA    . SER   D 2 135 ? 87.609  145.209 98.668  1.00 103.98 ?  134  SER   D CA    1 
ATOM   16133 C  C     . SER   D 2 135 ? 88.187  146.476 98.050  1.00 106.66 ?  134  SER   D C     1 
ATOM   16134 O  O     . SER   D 2 135 ? 88.947  146.414 97.077  1.00 108.29 ?  134  SER   D O     1 
ATOM   16135 C  CB    . SER   D 2 135 ? 86.141  145.041 98.275  1.00 101.55 ?  134  SER   D CB    1 
ATOM   16136 O  OG    . SER   D 2 135 ? 85.649  143.769 98.657  1.00 102.19 ?  134  SER   D OG    1 
ATOM   16137 N  N     . VAL   D 2 136 ? 87.865  147.641 98.617  1.00 107.34 ?  135  VAL   D N     1 
ATOM   16138 C  CA    . VAL   D 2 136 ? 88.241  148.911 98.008  1.00 108.40 ?  135  VAL   D CA    1 
ATOM   16139 C  C     . VAL   D 2 136 ? 89.751  149.072 97.917  1.00 110.42 ?  135  VAL   D C     1 
ATOM   16140 O  O     . VAL   D 2 136 ? 90.240  150.111 97.461  1.00 109.65 ?  135  VAL   D O     1 
ATOM   16141 C  CB    . VAL   D 2 136 ? 87.605  150.082 98.794  1.00 107.26 ?  135  VAL   D CB    1 
ATOM   16142 C  CG1   . VAL   D 2 136 ? 86.084  149.944 98.806  1.00 104.02 ?  135  VAL   D CG1   1 
ATOM   16143 C  CG2   . VAL   D 2 136 ? 88.148  150.145 100.214 1.00 107.00 ?  135  VAL   D CG2   1 
ATOM   16144 N  N     . VAL   D 2 137 ? 90.495  148.120 98.467  1.00 95.67  ?  136  VAL   D N     1 
ATOM   16145 C  CA    . VAL   D 2 137 ? 91.945  148.084 98.389  1.00 92.83  ?  136  VAL   D CA    1 
ATOM   16146 C  C     . VAL   D 2 137 ? 92.412  146.982 97.446  1.00 94.98  ?  136  VAL   D C     1 
ATOM   16147 O  O     . VAL   D 2 137 ? 93.242  147.215 96.566  1.00 100.60 ?  136  VAL   D O     1 
ATOM   16148 C  CB    . VAL   D 2 137 ? 92.570  147.916 99.793  1.00 89.70  ?  136  VAL   D CB    1 
ATOM   16149 C  CG1   . VAL   D 2 137 ? 94.043  147.554 99.684  1.00 91.22  ?  136  VAL   D CG1   1 
ATOM   16150 C  CG2   . VAL   D 2 137 ? 92.384  149.182 100.615 1.00 89.93  ?  136  VAL   D CG2   1 
ATOM   16151 N  N     . PHE   D 2 138 ? 91.868  145.772 97.604  1.00 87.02  ?  137  PHE   D N     1 
ATOM   16152 C  CA    . PHE   D 2 138 ? 92.311  144.647 96.786  1.00 87.81  ?  137  PHE   D CA    1 
ATOM   16153 C  C     . PHE   D 2 138 ? 91.935  144.836 95.320  1.00 91.88  ?  137  PHE   D C     1 
ATOM   16154 O  O     . PHE   D 2 138 ? 92.759  144.606 94.428  1.00 93.11  ?  137  PHE   D O     1 
ATOM   16155 C  CB    . PHE   D 2 138 ? 91.736  143.342 97.333  1.00 85.69  ?  137  PHE   D CB    1 
ATOM   16156 C  CG    . PHE   D 2 138 ? 92.412  142.864 98.586  1.00 87.64  ?  137  PHE   D CG    1 
ATOM   16157 C  CD1   . PHE   D 2 138 ? 93.787  142.938 98.717  1.00 88.03  ?  137  PHE   D CD1   1 
ATOM   16158 C  CD2   . PHE   D 2 138 ? 91.672  142.345 99.633  1.00 88.87  ?  137  PHE   D CD2   1 
ATOM   16159 C  CE1   . PHE   D 2 138 ? 94.412  142.500 99.868  1.00 86.64  ?  137  PHE   D CE1   1 
ATOM   16160 C  CE2   . PHE   D 2 138 ? 92.292  141.908 100.788 1.00 89.46  ?  137  PHE   D CE2   1 
ATOM   16161 C  CZ    . PHE   D 2 138 ? 93.664  141.985 100.904 1.00 86.33  ?  137  PHE   D CZ    1 
ATOM   16162 N  N     . ASP   D 2 139 ? 90.695  145.254 95.043  1.00 110.27 ?  138  ASP   D N     1 
ATOM   16163 C  CA    . ASP   D 2 139 ? 90.323  145.510 93.655  1.00 110.98 ?  138  ASP   D CA    1 
ATOM   16164 C  C     . ASP   D 2 139 ? 90.945  146.794 93.119  1.00 109.66 ?  138  ASP   D C     1 
ATOM   16165 O  O     . ASP   D 2 139 ? 90.980  146.987 91.900  1.00 112.37 ?  138  ASP   D O     1 
ATOM   16166 C  CB    . ASP   D 2 139 ? 88.802  145.566 93.496  1.00 111.82 ?  138  ASP   D CB    1 
ATOM   16167 C  CG    . ASP   D 2 139 ? 88.085  144.546 94.357  1.00 115.71 ?  138  ASP   D CG    1 
ATOM   16168 O  OD1   . ASP   D 2 139 ? 87.823  144.831 95.540  1.00 115.88 ?  138  ASP   D OD1   1 
ATOM   16169 O  OD2   . ASP   D 2 139 ? 87.777  143.451 93.853  1.00 116.09 ?  138  ASP   D OD2   1 
ATOM   16170 N  N     . ASP   D 2 140 ? 91.432  147.677 93.993  1.00 101.63 ?  139  ASP   D N     1 
ATOM   16171 C  CA    . ASP   D 2 140 ? 92.164  148.851 93.534  1.00 103.31 ?  139  ASP   D CA    1 
ATOM   16172 C  C     . ASP   D 2 140 ? 93.621  148.542 93.220  1.00 102.58 ?  139  ASP   D C     1 
ATOM   16173 O  O     . ASP   D 2 140 ? 94.249  149.288 92.462  1.00 103.32 ?  139  ASP   D O     1 
ATOM   16174 C  CB    . ASP   D 2 140 ? 92.091  149.968 94.577  1.00 105.36 ?  139  ASP   D CB    1 
ATOM   16175 C  CG    . ASP   D 2 140 ? 92.641  151.284 94.060  1.00 109.17 ?  139  ASP   D CG    1 
ATOM   16176 O  OD1   . ASP   D 2 140 ? 91.952  151.943 93.253  1.00 111.96 ?  139  ASP   D OD1   1 
ATOM   16177 O  OD2   . ASP   D 2 140 ? 93.763  151.658 94.458  1.00 108.08 ?  139  ASP   D OD2   1 
ATOM   16178 N  N     . ILE   D 2 141 ? 94.168  147.469 93.796  1.00 94.73  ?  140  ILE   D N     1 
ATOM   16179 C  CA    . ILE   D 2 141 ? 95.563  147.111 93.541  1.00 92.83  ?  140  ILE   D CA    1 
ATOM   16180 C  C     . ILE   D 2 141 ? 95.799  146.879 92.053  1.00 94.72  ?  140  ILE   D C     1 
ATOM   16181 O  O     . ILE   D 2 141 ? 96.790  147.354 91.484  1.00 96.22  ?  140  ILE   D O     1 
ATOM   16182 C  CB    . ILE   D 2 141 ? 95.957  145.874 94.371  1.00 90.36  ?  140  ILE   D CB    1 
ATOM   16183 C  CG1   . ILE   D 2 141 ? 96.189  146.256 95.832  1.00 90.05  ?  140  ILE   D CG1   1 
ATOM   16184 C  CG2   . ILE   D 2 141 ? 97.203  145.215 93.800  1.00 89.55  ?  140  ILE   D CG2   1 
ATOM   16185 C  CD1   . ILE   D 2 141 ? 96.085  145.092 96.791  1.00 89.24  ?  140  ILE   D CD1   1 
ATOM   16186 N  N     . VAL   D 2 142 ? 94.894  146.148 91.399  1.00 97.12  ?  141  VAL   D N     1 
ATOM   16187 C  CA    . VAL   D 2 142 ? 95.091  145.801 89.995  1.00 96.13  ?  141  VAL   D CA    1 
ATOM   16188 C  C     . VAL   D 2 142 ? 94.962  147.032 89.105  1.00 98.22  ?  141  VAL   D C     1 
ATOM   16189 O  O     . VAL   D 2 142 ? 95.776  147.248 88.199  1.00 96.77  ?  141  VAL   D O     1 
ATOM   16190 C  CB    . VAL   D 2 142 ? 94.104  144.698 89.573  1.00 96.56  ?  141  VAL   D CB    1 
ATOM   16191 C  CG1   . VAL   D 2 142 ? 94.545  144.067 88.262  1.00 94.44  ?  141  VAL   D CG1   1 
ATOM   16192 C  CG2   . VAL   D 2 142 ? 93.982  143.649 90.662  1.00 94.73  ?  141  VAL   D CG2   1 
ATOM   16193 N  N     . THR   D 2 143 ? 93.941  147.856 89.343  1.00 108.43 ?  142  THR   D N     1 
ATOM   16194 C  CA    . THR   D 2 143 ? 93.643  148.980 88.462  1.00 106.49 ?  142  THR   D CA    1 
ATOM   16195 C  C     . THR   D 2 143 ? 94.451  150.231 88.777  1.00 108.75 ?  142  THR   D C     1 
ATOM   16196 O  O     . THR   D 2 143 ? 94.404  151.186 87.994  1.00 109.73 ?  142  THR   D O     1 
ATOM   16197 C  CB    . THR   D 2 143 ? 92.155  149.327 88.528  1.00 108.51 ?  142  THR   D CB    1 
ATOM   16198 O  OG1   . THR   D 2 143 ? 91.928  150.264 89.588  1.00 109.57 ?  142  THR   D OG1   1 
ATOM   16199 C  CG2   . THR   D 2 143 ? 91.338  148.083 88.783  1.00 107.06 ?  142  THR   D CG2   1 
ATOM   16200 N  N     . ASN   D 2 144 ? 95.173  150.260 89.892  1.00 112.94 ?  143  ASN   D N     1 
ATOM   16201 C  CA    . ASN   D 2 144 ? 95.961  151.435 90.236  1.00 111.46 ?  143  ASN   D CA    1 
ATOM   16202 C  C     . ASN   D 2 144 ? 97.051  151.656 89.199  1.00 113.37 ?  143  ASN   D C     1 
ATOM   16203 O  O     . ASN   D 2 144 ? 97.914  150.795 89.003  1.00 116.24 ?  143  ASN   D O     1 
ATOM   16204 C  CB    . ASN   D 2 144 ? 96.567  151.271 91.626  1.00 111.93 ?  143  ASN   D CB    1 
ATOM   16205 C  CG    . ASN   D 2 144 ? 96.825  152.600 92.309  1.00 113.80 ?  143  ASN   D CG    1 
ATOM   16206 O  OD1   . ASN   D 2 144 ? 97.075  153.611 91.655  1.00 116.24 ?  143  ASN   D OD1   1 
ATOM   16207 N  ND2   . ASN   D 2 144 ? 96.757  152.605 93.635  1.00 113.95 ?  143  ASN   D ND2   1 
ATOM   16208 N  N     . GLU   D 2 145 ? 96.986  152.804 88.518  1.00 116.10 ?  144  GLU   D N     1 
ATOM   16209 C  CA    . GLU   D 2 145 ? 97.951  153.106 87.466  1.00 115.78 ?  144  GLU   D CA    1 
ATOM   16210 C  C     . GLU   D 2 145 ? 99.368  153.135 88.012  1.00 117.30 ?  144  GLU   D C     1 
ATOM   16211 O  O     . GLU   D 2 145 ? 100.306 152.670 87.358  1.00 118.37 ?  144  GLU   D O     1 
ATOM   16212 C  CB    . GLU   D 2 145 ? 97.613  154.442 86.805  1.00 116.50 ?  144  GLU   D CB    1 
ATOM   16213 C  CG    . GLU   D 2 145 ? 98.251  154.627 85.433  1.00 118.76 ?  144  GLU   D CG    1 
ATOM   16214 C  CD    . GLU   D 2 145 ? 97.288  154.439 84.286  1.00 120.90 ?  144  GLU   D CD    1 
ATOM   16215 O  OE1   . GLU   D 2 145 ? 97.721  153.925 83.234  1.00 119.53 ?  144  GLU   D OE1   1 
ATOM   16216 O  OE2   . GLU   D 2 145 ? 96.108  154.816 84.431  1.00 120.58 ?  144  GLU   D OE2   1 
ATOM   16217 N  N     . GLN   D 2 146 ? 99.540  153.666 89.210  1.00 110.43 ?  145  GLN   D N     1 
ATOM   16218 C  CA    . GLN   D 2 146 ? 100.859 153.857 89.786  1.00 108.83 ?  145  GLN   D CA    1 
ATOM   16219 C  C     . GLN   D 2 146 ? 101.482 152.576 90.333  1.00 109.63 ?  145  GLN   D C     1 
ATOM   16220 O  O     . GLN   D 2 146 ? 102.565 152.640 90.932  1.00 115.07 ?  145  GLN   D O     1 
ATOM   16221 C  CB    . GLN   D 2 146 ? 100.771 154.883 90.907  1.00 106.87 ?  145  GLN   D CB    1 
ATOM   16222 C  CG    . GLN   D 2 146 ? 100.212 156.254 90.559  1.00 108.94 ?  145  GLN   D CG    1 
ATOM   16223 C  CD    . GLN   D 2 146 ? 101.271 157.209 90.056  1.00 111.90 ?  145  GLN   D CD    1 
ATOM   16224 O  OE1   . GLN   D 2 146 ? 102.453 156.875 90.013  1.00 112.40 ?  145  GLN   D OE1   1 
ATOM   16225 N  NE2   . GLN   D 2 146 ? 100.852 158.415 89.686  1.00 111.57 ?  145  GLN   D NE2   1 
ATOM   16226 N  N     . ILE   D 2 147 ? 100.823 151.428 90.177  1.00 103.25 ?  146  ILE   D N     1 
ATOM   16227 C  CA    . ILE   D 2 147 ? 101.377 150.164 90.646  1.00 103.25 ?  146  ILE   D CA    1 
ATOM   16228 C  C     . ILE   D 2 147 ? 101.440 149.153 89.508  1.00 103.04 ?  146  ILE   D C     1 
ATOM   16229 O  O     . ILE   D 2 147 ? 102.275 148.240 89.525  1.00 106.44 ?  146  ILE   D O     1 
ATOM   16230 C  CB    . ILE   D 2 147 ? 100.567 149.599 91.828  1.00 104.34 ?  146  ILE   D CB    1 
ATOM   16231 C  CG1   . ILE   D 2 147 ? 100.105 150.717 92.764  1.00 103.03 ?  146  ILE   D CG1   1 
ATOM   16232 C  CG2   . ILE   D 2 147 ? 101.394 148.586 92.599  1.00 105.47 ?  146  ILE   D CG2   1 
ATOM   16233 C  CD1   . ILE   D 2 147 ? 99.607  150.227 94.106  1.00 102.15 ?  146  ILE   D CD1   1 
ATOM   16234 N  N     . GLN   D 2 148 ? 100.567 149.306 88.505  1.00 113.38 ?  147  GLN   D N     1 
ATOM   16235 C  CA    . GLN   D 2 148 ? 100.524 148.309 87.440  1.00 113.95 ?  147  GLN   D CA    1 
ATOM   16236 C  C     . GLN   D 2 148 ? 101.762 148.373 86.559  1.00 115.21 ?  147  GLN   D C     1 
ATOM   16237 O  O     . GLN   D 2 148 ? 102.188 147.340 86.040  1.00 119.91 ?  147  GLN   D O     1 
ATOM   16238 C  CB    . GLN   D 2 148 ? 99.260  148.459 86.591  1.00 113.66 ?  147  GLN   D CB    1 
ATOM   16239 C  CG    . GLN   D 2 148 ? 98.947  149.871 86.151  1.00 117.40 ?  147  GLN   D CG    1 
ATOM   16240 C  CD    . GLN   D 2 148 ? 97.945  149.888 85.007  1.00 118.79 ?  147  GLN   D CD    1 
ATOM   16241 O  OE1   . GLN   D 2 148 ? 97.046  149.047 84.947  1.00 116.78 ?  147  GLN   D OE1   1 
ATOM   16242 N  NE2   . GLN   D 2 148 ? 98.104  150.832 84.087  1.00 117.60 ?  147  GLN   D NE2   1 
ATOM   16243 N  N     . LYS   D 2 149 ? 102.354 149.557 86.374  1.00 110.65 ?  148  LYS   D N     1 
ATOM   16244 C  CA    . LYS   D 2 149 ? 103.585 149.638 85.590  1.00 112.64 ?  148  LYS   D CA    1 
ATOM   16245 C  C     . LYS   D 2 149 ? 104.695 148.819 86.238  1.00 112.38 ?  148  LYS   D C     1 
ATOM   16246 O  O     . LYS   D 2 149 ? 105.398 148.058 85.561  1.00 112.47 ?  148  LYS   D O     1 
ATOM   16247 C  CB    . LYS   D 2 149 ? 104.020 151.096 85.421  1.00 112.20 ?  148  LYS   D CB    1 
ATOM   16248 C  CG    . LYS   D 2 149 ? 103.637 151.993 86.586  1.00 112.40 ?  148  LYS   D CG    1 
ATOM   16249 C  CD    . LYS   D 2 149 ? 104.089 153.426 86.373  1.00 114.02 ?  148  LYS   D CD    1 
ATOM   16250 C  CE    . LYS   D 2 149 ? 103.332 154.103 85.246  1.00 113.10 ?  148  LYS   D CE    1 
ATOM   16251 N  NZ    . LYS   D 2 149 ? 103.787 155.508 85.050  1.00 112.76 ?  148  LYS   D NZ    1 
ATOM   16252 N  N     . ARG   D 2 150 ? 104.848 148.945 87.558  1.00 104.76 ?  149  ARG   D N     1 
ATOM   16253 C  CA    . ARG   D 2 150 ? 105.817 148.126 88.277  1.00 104.86 ?  149  ARG   D CA    1 
ATOM   16254 C  C     . ARG   D 2 150 ? 105.440 146.653 88.215  1.00 103.85 ?  149  ARG   D C     1 
ATOM   16255 O  O     . ARG   D 2 150 ? 106.315 145.785 88.119  1.00 105.37 ?  149  ARG   D O     1 
ATOM   16256 C  CB    . ARG   D 2 150 ? 105.925 148.597 89.726  1.00 102.03 ?  149  ARG   D CB    1 
ATOM   16257 C  CG    . ARG   D 2 150 ? 106.301 150.061 89.863  1.00 101.60 ?  149  ARG   D CG    1 
ATOM   16258 C  CD    . ARG   D 2 150 ? 105.804 150.650 91.171  1.00 100.70 ?  149  ARG   D CD    1 
ATOM   16259 N  NE    . ARG   D 2 150 ? 106.257 152.025 91.348  1.00 102.09 ?  149  ARG   D NE    1 
ATOM   16260 C  CZ    . ARG   D 2 150 ? 105.725 153.073 90.734  1.00 106.32 ?  149  ARG   D CZ    1 
ATOM   16261 N  NH1   . ARG   D 2 150 ? 104.709 152.943 89.897  1.00 107.19 ?  149  ARG   D NH1   1 
ATOM   16262 N  NH2   . ARG   D 2 150 ? 106.225 154.283 90.966  1.00 106.40 ?  149  ARG   D NH2   1 
ATOM   16263 N  N     . ALA   D 2 151 ? 104.140 146.353 88.268  1.00 102.70 ?  150  ALA   D N     1 
ATOM   16264 C  CA    . ALA   D 2 151 ? 103.697 144.965 88.168  1.00 100.48 ?  150  ALA   D CA    1 
ATOM   16265 C  C     . ALA   D 2 151 ? 104.141 144.337 86.852  1.00 101.37 ?  150  ALA   D C     1 
ATOM   16266 O  O     . ALA   D 2 151 ? 104.687 143.228 86.835  1.00 102.50 ?  150  ALA   D O     1 
ATOM   16267 C  CB    . ALA   D 2 151 ? 102.177 144.888 88.318  1.00 97.47  ?  150  ALA   D CB    1 
ATOM   16268 N  N     . GLU   D 2 152 ? 103.911 145.032 85.737  1.00 101.49 ?  151  GLU   D N     1 
ATOM   16269 C  CA    . GLU   D 2 152 ? 104.364 144.530 84.443  1.00 100.50 ?  151  GLU   D CA    1 
ATOM   16270 C  C     . GLU   D 2 152 ? 105.882 144.425 84.394  1.00 103.01 ?  151  GLU   D C     1 
ATOM   16271 O  O     . GLU   D 2 152 ? 106.431 143.417 83.932  1.00 106.75 ?  151  GLU   D O     1 
ATOM   16272 C  CB    . GLU   D 2 152 ? 103.878 145.434 83.311  1.00 102.32 ?  151  GLU   D CB    1 
ATOM   16273 C  CG    . GLU   D 2 152 ? 102.522 146.061 83.503  1.00 106.79 ?  151  GLU   D CG    1 
ATOM   16274 C  CD    . GLU   D 2 152 ? 102.069 146.848 82.292  1.00 108.96 ?  151  GLU   D CD    1 
ATOM   16275 O  OE1   . GLU   D 2 152 ? 102.535 146.525 81.182  1.00 108.77 ?  151  GLU   D OE1   1 
ATOM   16276 O  OE2   . GLU   D 2 152 ? 101.241 147.774 82.441  1.00 105.98 ?  151  GLU   D OE2   1 
ATOM   16277 N  N     . GLY   D 2 153 ? 106.579 145.468 84.859  1.00 98.85  ?  152  GLY   D N     1 
ATOM   16278 C  CA    . GLY   D 2 153 ? 108.030 145.466 84.789  1.00 97.82  ?  152  GLY   D CA    1 
ATOM   16279 C  C     . GLY   D 2 153 ? 108.657 144.353 85.600  1.00 99.32  ?  152  GLY   D C     1 
ATOM   16280 O  O     . GLY   D 2 153 ? 109.751 143.883 85.275  1.00 101.86 ?  152  GLY   D O     1 
ATOM   16281 N  N     . ILE   D 2 154 ? 107.976 143.910 86.651  1.00 88.40  ?  153  ILE   D N     1 
ATOM   16282 C  CA    . ILE   D 2 154 ? 108.493 142.842 87.495  1.00 86.41  ?  153  ILE   D CA    1 
ATOM   16283 C  C     . ILE   D 2 154 ? 108.094 141.469 86.976  1.00 87.80  ?  153  ILE   D C     1 
ATOM   16284 O  O     . ILE   D 2 154 ? 108.926 140.560 86.950  1.00 88.58  ?  153  ILE   D O     1 
ATOM   16285 C  CB    . ILE   D 2 154 ? 108.030 143.058 88.947  1.00 85.56  ?  153  ILE   D CB    1 
ATOM   16286 C  CG1   . ILE   D 2 154 ? 108.958 144.045 89.662  1.00 85.78  ?  153  ILE   D CG1   1 
ATOM   16287 C  CG2   . ILE   D 2 154 ? 107.960 141.735 89.697  1.00 83.77  ?  153  ILE   D CG2   1 
ATOM   16288 C  CD1   . ILE   D 2 154 ? 108.247 144.920 90.670  1.00 86.84  ?  153  ILE   D CD1   1 
ATOM   16289 N  N     . SER   D 2 155 ? 106.846 141.308 86.524  1.00 89.31  ?  154  SER   D N     1 
ATOM   16290 C  CA    . SER   D 2 155 ? 106.377 140.016 86.051  1.00 87.36  ?  154  SER   D CA    1 
ATOM   16291 C  C     . SER   D 2 155 ? 106.860 139.685 84.648  1.00 88.27  ?  154  SER   D C     1 
ATOM   16292 O  O     . SER   D 2 155 ? 106.770 138.521 84.245  1.00 92.45  ?  154  SER   D O     1 
ATOM   16293 C  CB    . SER   D 2 155 ? 104.849 139.970 86.098  1.00 85.79  ?  154  SER   D CB    1 
ATOM   16294 O  OG    . SER   D 2 155 ? 104.282 140.765 85.074  1.00 90.21  ?  154  SER   D OG    1 
ATOM   16295 N  N     . SER   D 2 156 ? 107.367 140.666 83.898  1.00 91.42  ?  155  SER   D N     1 
ATOM   16296 C  CA    . SER   D 2 156 ? 107.820 140.385 82.541  1.00 89.74  ?  155  SER   D CA    1 
ATOM   16297 C  C     . SER   D 2 156 ? 108.998 139.422 82.535  1.00 91.12  ?  155  SER   D C     1 
ATOM   16298 O  O     . SER   D 2 156 ? 109.041 138.494 81.722  1.00 94.65  ?  155  SER   D O     1 
ATOM   16299 C  CB    . SER   D 2 156 ? 108.189 141.687 81.834  1.00 91.63  ?  155  SER   D CB    1 
ATOM   16300 O  OG    . SER   D 2 156 ? 109.428 142.191 82.306  1.00 93.75  ?  155  SER   D OG    1 
ATOM   16301 N  N     . TYR   D 2 157 ? 109.962 139.625 83.436  1.00 89.41  ?  156  TYR   D N     1 
ATOM   16302 C  CA    . TYR   D 2 157 ? 111.116 138.733 83.490  1.00 89.48  ?  156  TYR   D CA    1 
ATOM   16303 C  C     . TYR   D 2 157 ? 110.692 137.307 83.815  1.00 91.58  ?  156  TYR   D C     1 
ATOM   16304 O  O     . TYR   D 2 157 ? 111.150 136.351 83.173  1.00 92.80  ?  156  TYR   D O     1 
ATOM   16305 C  CB    . TYR   D 2 157 ? 112.124 139.244 84.519  1.00 86.04  ?  156  TYR   D CB    1 
ATOM   16306 C  CG    . TYR   D 2 157 ? 112.785 140.540 84.117  1.00 88.66  ?  156  TYR   D CG    1 
ATOM   16307 C  CD1   . TYR   D 2 157 ? 113.936 140.542 83.345  1.00 88.77  ?  156  TYR   D CD1   1 
ATOM   16308 C  CD2   . TYR   D 2 157 ? 112.254 141.762 84.503  1.00 88.28  ?  156  TYR   D CD2   1 
ATOM   16309 C  CE1   . TYR   D 2 157 ? 114.541 141.725 82.968  1.00 89.78  ?  156  TYR   D CE1   1 
ATOM   16310 C  CE2   . TYR   D 2 157 ? 112.852 142.950 84.134  1.00 89.60  ?  156  TYR   D CE2   1 
ATOM   16311 C  CZ    . TYR   D 2 157 ? 113.994 142.925 83.364  1.00 92.29  ?  156  TYR   D CZ    1 
ATOM   16312 O  OH    . TYR   D 2 157 ? 114.597 144.105 82.994  1.00 94.82  ?  156  TYR   D OH    1 
ATOM   16313 N  N     . TYR   D 2 158 ? 109.799 137.151 84.795  1.00 78.21  ?  157  TYR   D N     1 
ATOM   16314 C  CA    . TYR   D 2 158 ? 109.287 135.830 85.136  1.00 71.57  ?  157  TYR   D CA    1 
ATOM   16315 C  C     . TYR   D 2 158 ? 108.588 135.188 83.947  1.00 77.81  ?  157  TYR   D C     1 
ATOM   16316 O  O     . TYR   D 2 158 ? 108.799 134.005 83.657  1.00 84.56  ?  157  TYR   D O     1 
ATOM   16317 C  CB    . TYR   D 2 158 ? 108.321 135.935 86.314  1.00 72.55  ?  157  TYR   D CB    1 
ATOM   16318 C  CG    . TYR   D 2 158 ? 108.964 135.957 87.679  1.00 74.47  ?  157  TYR   D CG    1 
ATOM   16319 C  CD1   . TYR   D 2 158 ? 109.694 134.874 88.145  1.00 77.73  ?  157  TYR   D CD1   1 
ATOM   16320 C  CD2   . TYR   D 2 158 ? 108.815 137.055 88.515  1.00 74.72  ?  157  TYR   D CD2   1 
ATOM   16321 C  CE1   . TYR   D 2 158 ? 110.270 134.890 89.400  1.00 76.60  ?  157  TYR   D CE1   1 
ATOM   16322 C  CE2   . TYR   D 2 158 ? 109.388 137.081 89.769  1.00 76.36  ?  157  TYR   D CE2   1 
ATOM   16323 C  CZ    . TYR   D 2 158 ? 110.114 135.996 90.207  1.00 77.70  ?  157  TYR   D CZ    1 
ATOM   16324 O  OH    . TYR   D 2 158 ? 110.672 136.017 91.461  1.00 81.77  ?  157  TYR   D OH    1 
ATOM   16325 N  N     . ASP   D 2 159 ? 107.751 135.956 83.245  1.00 87.18  ?  158  ASP   D N     1 
ATOM   16326 C  CA    . ASP   D 2 159 ? 106.988 135.400 82.132  1.00 86.37  ?  158  ASP   D CA    1 
ATOM   16327 C  C     . ASP   D 2 159 ? 107.893 134.973 80.984  1.00 86.37  ?  158  ASP   D C     1 
ATOM   16328 O  O     . ASP   D 2 159 ? 107.707 133.894 80.411  1.00 90.03  ?  158  ASP   D O     1 
ATOM   16329 C  CB    . ASP   D 2 159 ? 105.954 136.413 81.654  1.00 91.05  ?  158  ASP   D CB    1 
ATOM   16330 C  CG    . ASP   D 2 159 ? 104.912 136.720 82.706  1.00 96.38  ?  158  ASP   D CG    1 
ATOM   16331 O  OD1   . ASP   D 2 159 ? 104.868 136.000 83.724  1.00 94.93  ?  158  ASP   D OD1   1 
ATOM   16332 O  OD2   . ASP   D 2 159 ? 104.141 137.681 82.517  1.00 98.73  ?  158  ASP   D OD2   1 
ATOM   16333 N  N     . GLU   D 2 160 ? 108.886 135.793 80.647  1.00 82.10  ?  159  GLU   D N     1 
ATOM   16334 C  CA    . GLU   D 2 160 ? 109.816 135.430 79.584  1.00 80.10  ?  159  GLU   D CA    1 
ATOM   16335 C  C     . GLU   D 2 160 ? 110.642 134.205 79.962  1.00 82.97  ?  159  GLU   D C     1 
ATOM   16336 O  O     . GLU   D 2 160 ? 110.874 133.320 79.124  1.00 87.77  ?  159  GLU   D O     1 
ATOM   16337 C  CB    . GLU   D 2 160 ? 110.720 136.618 79.266  1.00 85.09  ?  159  GLU   D CB    1 
ATOM   16338 C  CG    . GLU   D 2 160 ? 109.966 137.906 78.958  1.00 91.75  ?  159  GLU   D CG    1 
ATOM   16339 C  CD    . GLU   D 2 160 ? 110.691 138.845 78.027  1.00 96.33  ?  159  GLU   D CD    1 
ATOM   16340 O  OE1   . GLU   D 2 160 ? 111.635 138.403 77.347  1.00 96.43  ?  159  GLU   D OE1   1 
ATOM   16341 O  OE2   . GLU   D 2 160 ? 110.295 140.029 77.970  1.00 93.16  ?  159  GLU   D OE2   1 
ATOM   16342 N  N     . LEU   D 2 161 ? 111.094 134.134 81.219  1.00 72.96  ?  160  LEU   D N     1 
ATOM   16343 C  CA    . LEU   D 2 161 ? 111.828 132.956 81.668  1.00 66.56  ?  160  LEU   D CA    1 
ATOM   16344 C  C     . LEU   D 2 161 ? 110.964 131.705 81.579  1.00 72.14  ?  160  LEU   D C     1 
ATOM   16345 O  O     . LEU   D 2 161 ? 111.428 130.654 81.124  1.00 75.14  ?  160  LEU   D O     1 
ATOM   16346 C  CB    . LEU   D 2 161 ? 112.332 133.156 83.096  1.00 66.37  ?  160  LEU   D CB    1 
ATOM   16347 C  CG    . LEU   D 2 161 ? 113.086 131.967 83.694  1.00 67.15  ?  160  LEU   D CG    1 
ATOM   16348 C  CD1   . LEU   D 2 161 ? 114.281 131.599 82.832  1.00 67.85  ?  160  LEU   D CD1   1 
ATOM   16349 C  CD2   . LEU   D 2 161 ? 113.519 132.261 85.120  1.00 71.19  ?  160  LEU   D CD2   1 
ATOM   16350 N  N     . ILE   D 2 162 ? 109.700 131.803 81.996  1.00 73.42  ?  161  ILE   D N     1 
ATOM   16351 C  CA    . ILE   D 2 162 ? 108.806 130.649 81.959  1.00 67.24  ?  161  ILE   D CA    1 
ATOM   16352 C  C     . ILE   D 2 162 ? 108.552 130.210 80.523  1.00 73.06  ?  161  ILE   D C     1 
ATOM   16353 O  O     . ILE   D 2 162 ? 108.562 129.011 80.215  1.00 77.57  ?  161  ILE   D O     1 
ATOM   16354 C  CB    . ILE   D 2 162 ? 107.494 130.970 82.700  1.00 68.34  ?  161  ILE   D CB    1 
ATOM   16355 C  CG1   . ILE   D 2 162 ? 107.722 130.985 84.212  1.00 70.18  ?  161  ILE   D CG1   1 
ATOM   16356 C  CG2   . ILE   D 2 162 ? 106.408 129.969 82.334  1.00 67.91  ?  161  ILE   D CG2   1 
ATOM   16357 C  CD1   . ILE   D 2 162 ? 106.745 131.857 84.968  1.00 71.64  ?  161  ILE   D CD1   1 
ATOM   16358 N  N     . GLU   D 2 163 ? 108.331 131.170 79.621  1.00 86.30  ?  162  GLU   D N     1 
ATOM   16359 C  CA    . GLU   D 2 163 ? 108.094 130.838 78.219  1.00 79.51  ?  162  GLU   D CA    1 
ATOM   16360 C  C     . GLU   D 2 163 ? 109.303 130.146 77.602  1.00 83.02  ?  162  GLU   D C     1 
ATOM   16361 O  O     . GLU   D 2 163 ? 109.166 129.136 76.898  1.00 85.87  ?  162  GLU   D O     1 
ATOM   16362 C  CB    . GLU   D 2 163 ? 107.742 132.103 77.437  1.00 80.31  ?  162  GLU   D CB    1 
ATOM   16363 C  CG    . GLU   D 2 163 ? 107.870 131.949 75.934  1.00 87.21  ?  162  GLU   D CG    1 
ATOM   16364 C  CD    . GLU   D 2 163 ? 106.751 132.631 75.175  1.00 93.97  ?  162  GLU   D CD    1 
ATOM   16365 O  OE1   . GLU   D 2 163 ? 107.050 133.470 74.300  1.00 94.43  ?  162  GLU   D OE1   1 
ATOM   16366 O  OE2   . GLU   D 2 163 ? 105.572 132.328 75.454  1.00 96.51  ?  162  GLU   D OE2   1 
ATOM   16367 N  N     . MET   D 2 164 ? 110.504 130.676 77.849  1.00 79.17  ?  163  MET   D N     1 
ATOM   16368 C  CA    . MET   D 2 164 ? 111.676 130.040 77.262  1.00 76.36  ?  163  MET   D CA    1 
ATOM   16369 C  C     . MET   D 2 164 ? 111.905 128.665 77.866  1.00 79.35  ?  163  MET   D C     1 
ATOM   16370 O  O     . MET   D 2 164 ? 112.262 127.730 77.146  1.00 84.05  ?  163  MET   D O     1 
ATOM   16371 C  CB    . MET   D 2 164 ? 112.915 130.914 77.421  1.00 76.78  ?  163  MET   D CB    1 
ATOM   16372 C  CG    . MET   D 2 164 ? 114.062 130.534 76.491  1.00 85.16  ?  163  MET   D CG    1 
ATOM   16373 S  SD    . MET   D 2 164 ? 114.996 131.995 76.023  1.00 99.13  ?  163  MET   D SD    1 
ATOM   16374 C  CE    . MET   D 2 164 ? 113.679 133.207 75.997  1.00 82.04  ?  163  MET   D CE    1 
ATOM   16375 N  N     . THR   D 2 165 ? 111.680 128.516 79.176  1.00 73.62  ?  164  THR   D N     1 
ATOM   16376 C  CA    . THR   D 2 165 ? 111.816 127.210 79.808  1.00 72.93  ?  164  THR   D CA    1 
ATOM   16377 C  C     . THR   D 2 165 ? 110.856 126.206 79.189  1.00 76.05  ?  164  THR   D C     1 
ATOM   16378 O  O     . THR   D 2 165 ? 111.221 125.049 78.956  1.00 84.17  ?  164  THR   D O     1 
ATOM   16379 C  CB    . THR   D 2 165 ? 111.576 127.324 81.314  1.00 72.63  ?  164  THR   D CB    1 
ATOM   16380 O  OG1   . THR   D 2 165 ? 112.526 128.232 81.883  1.00 79.07  ?  164  THR   D OG1   1 
ATOM   16381 C  CG2   . THR   D 2 165 ? 111.719 125.967 81.983  1.00 72.96  ?  164  THR   D CG2   1 
ATOM   16382 N  N     . SER   D 2 166 ? 109.625 126.633 78.905  1.00 73.41  ?  165  SER   D N     1 
ATOM   16383 C  CA    . SER   D 2 166 ? 108.671 125.732 78.268  1.00 74.40  ?  165  SER   D CA    1 
ATOM   16384 C  C     . SER   D 2 166 ? 109.116 125.345 76.862  1.00 75.32  ?  165  SER   D C     1 
ATOM   16385 O  O     . SER   D 2 166 ? 109.014 124.174 76.479  1.00 75.53  ?  165  SER   D O     1 
ATOM   16386 C  CB    . SER   D 2 166 ? 107.284 126.367 78.238  1.00 76.39  ?  165  SER   D CB    1 
ATOM   16387 O  OG    . SER   D 2 166 ? 106.535 126.037 79.393  1.00 79.45  ?  165  SER   D OG    1 
ATOM   16388 N  N     . TYR   D 2 167 ? 109.627 126.294 76.075  1.00 79.03  ?  166  TYR   D N     1 
ATOM   16389 C  CA    . TYR   D 2 167 ? 110.114 125.888 74.756  1.00 72.55  ?  166  TYR   D CA    1 
ATOM   16390 C  C     . TYR   D 2 167 ? 111.321 124.958 74.877  1.00 75.27  ?  166  TYR   D C     1 
ATOM   16391 O  O     . TYR   D 2 167 ? 111.434 123.990 74.122  1.00 76.51  ?  166  TYR   D O     1 
ATOM   16392 C  CB    . TYR   D 2 167 ? 110.442 127.098 73.876  1.00 71.85  ?  166  TYR   D CB    1 
ATOM   16393 C  CG    . TYR   D 2 167 ? 109.266 127.641 73.080  1.00 77.18  ?  166  TYR   D CG    1 
ATOM   16394 C  CD1   . TYR   D 2 167 ? 108.403 126.797 72.399  1.00 81.29  ?  166  TYR   D CD1   1 
ATOM   16395 C  CD2   . TYR   D 2 167 ? 109.037 129.006 73.001  1.00 78.71  ?  166  TYR   D CD2   1 
ATOM   16396 C  CE1   . TYR   D 2 167 ? 107.325 127.302 71.682  1.00 83.54  ?  166  TYR   D CE1   1 
ATOM   16397 C  CE2   . TYR   D 2 167 ? 107.971 129.517 72.283  1.00 80.65  ?  166  TYR   D CE2   1 
ATOM   16398 C  CZ    . TYR   D 2 167 ? 107.117 128.660 71.629  1.00 83.92  ?  166  TYR   D CZ    1 
ATOM   16399 O  OH    . TYR   D 2 167 ? 106.054 129.163 70.914  1.00 84.49  ?  166  TYR   D OH    1 
ATOM   16400 N  N     . TRP   D 2 168 ? 112.222 125.214 75.827  1.00 74.33  ?  167  TRP   D N     1 
ATOM   16401 C  CA    . TRP   D 2 168 ? 113.378 124.337 75.990  1.00 72.56  ?  167  TRP   D CA    1 
ATOM   16402 C  C     . TRP   D 2 168 ? 112.950 122.926 76.371  1.00 75.19  ?  167  TRP   D C     1 
ATOM   16403 O  O     . TRP   D 2 168 ? 113.481 121.944 75.841  1.00 81.21  ?  167  TRP   D O     1 
ATOM   16404 C  CB    . TRP   D 2 168 ? 114.334 124.905 77.035  1.00 72.99  ?  167  TRP   D CB    1 
ATOM   16405 C  CG    . TRP   D 2 168 ? 115.553 124.067 77.274  1.00 73.56  ?  167  TRP   D CG    1 
ATOM   16406 C  CD1   . TRP   D 2 168 ? 116.503 123.713 76.361  1.00 74.31  ?  167  TRP   D CD1   1 
ATOM   16407 C  CD2   . TRP   D 2 168 ? 115.960 123.487 78.518  1.00 73.94  ?  167  TRP   D CD2   1 
ATOM   16408 N  NE1   . TRP   D 2 168 ? 117.458 122.927 76.955  1.00 76.47  ?  167  TRP   D NE1   1 
ATOM   16409 C  CE2   . TRP   D 2 168 ? 117.180 122.826 78.292  1.00 74.37  ?  167  TRP   D CE2   1 
ATOM   16410 C  CE3   . TRP   D 2 168 ? 115.414 123.472 79.805  1.00 74.62  ?  167  TRP   D CE3   1 
ATOM   16411 C  CZ2   . TRP   D 2 168 ? 117.833 122.108 79.288  1.00 78.18  ?  167  TRP   D CZ2   1 
ATOM   16412 C  CZ3   . TRP   D 2 168 ? 116.091 122.803 80.805  1.00 73.55  ?  167  TRP   D CZ3   1 
ATOM   16413 C  CH2   . TRP   D 2 168 ? 117.283 122.123 80.540  1.00 76.87  ?  167  TRP   D CH2   1 
ATOM   16414 N  N     . HIS   D 2 169 ? 111.982 122.804 77.281  1.00 74.42  ?  168  HIS   D N     1 
ATOM   16415 C  CA    . HIS   D 2 169 ? 111.540 121.482 77.710  1.00 72.83  ?  168  HIS   D CA    1 
ATOM   16416 C  C     . HIS   D 2 169 ? 110.698 120.793 76.645  1.00 76.96  ?  168  HIS   D C     1 
ATOM   16417 O  O     . HIS   D 2 169 ? 110.631 119.559 76.615  1.00 79.66  ?  168  HIS   D O     1 
ATOM   16418 C  CB    . HIS   D 2 169 ? 110.759 121.587 79.019  1.00 69.22  ?  168  HIS   D CB    1 
ATOM   16419 C  CG    . HIS   D 2 169 ? 111.627 121.622 80.239  1.00 70.74  ?  168  HIS   D CG    1 
ATOM   16420 N  ND1   . HIS   D 2 169 ? 112.540 120.633 80.531  1.00 78.22  ?  168  HIS   D ND1   1 
ATOM   16421 C  CD2   . HIS   D 2 169 ? 111.717 122.525 81.243  1.00 73.09  ?  168  HIS   D CD2   1 
ATOM   16422 C  CE1   . HIS   D 2 169 ? 113.159 120.927 81.660  1.00 76.31  ?  168  HIS   D CE1   1 
ATOM   16423 N  NE2   . HIS   D 2 169 ? 112.678 122.070 82.113  1.00 73.50  ?  168  HIS   D NE2   1 
ATOM   16424 N  N     . LEU   D 2 170 ? 110.052 121.557 75.767  1.00 77.54  ?  169  LEU   D N     1 
ATOM   16425 C  CA    . LEU   D 2 170 ? 109.207 120.955 74.746  1.00 72.60  ?  169  LEU   D CA    1 
ATOM   16426 C  C     . LEU   D 2 170 ? 109.995 120.541 73.509  1.00 76.91  ?  169  LEU   D C     1 
ATOM   16427 O  O     . LEU   D 2 170 ? 109.840 119.418 73.025  1.00 81.55  ?  169  LEU   D O     1 
ATOM   16428 C  CB    . LEU   D 2 170 ? 108.089 121.924 74.360  1.00 75.85  ?  169  LEU   D CB    1 
ATOM   16429 C  CG    . LEU   D 2 170 ? 106.851 121.992 75.254  1.00 80.87  ?  169  LEU   D CG    1 
ATOM   16430 C  CD1   . LEU   D 2 170 ? 105.639 122.431 74.453  1.00 81.30  ?  169  LEU   D CD1   1 
ATOM   16431 C  CD2   . LEU   D 2 170 ? 106.597 120.654 75.922  1.00 79.08  ?  169  LEU   D CD2   1 
ATOM   16432 N  N     . LEU   D 2 171 ? 110.868 121.412 73.014  1.00 85.00  ?  170  LEU   D N     1 
ATOM   16433 C  CA    . LEU   D 2 171 ? 111.559 121.200 71.752  1.00 80.74  ?  170  LEU   D CA    1 
ATOM   16434 C  C     . LEU   D 2 171 ? 113.035 120.871 71.899  1.00 82.74  ?  170  LEU   D C     1 
ATOM   16435 O  O     . LEU   D 2 171 ? 113.596 120.216 71.020  1.00 88.25  ?  170  LEU   D O     1 
ATOM   16436 C  CB    . LEU   D 2 171 ? 111.420 122.445 70.871  1.00 79.49  ?  170  LEU   D CB    1 
ATOM   16437 C  CG    . LEU   D 2 171 ? 110.014 123.040 70.778  1.00 82.38  ?  170  LEU   D CG    1 
ATOM   16438 C  CD1   . LEU   D 2 171 ? 110.041 124.339 69.994  1.00 86.60  ?  170  LEU   D CD1   1 
ATOM   16439 C  CD2   . LEU   D 2 171 ? 109.036 122.064 70.153  1.00 82.14  ?  170  LEU   D CD2   1 
ATOM   16440 N  N     . GLY   D 2 172 ? 113.676 121.308 72.976  1.00 83.38  ?  171  GLY   D N     1 
ATOM   16441 C  CA    . GLY   D 2 172 ? 115.106 121.142 73.118  1.00 84.41  ?  171  GLY   D CA    1 
ATOM   16442 C  C     . GLY   D 2 172 ? 115.868 122.204 72.351  1.00 88.20  ?  171  GLY   D C     1 
ATOM   16443 O  O     . GLY   D 2 172 ? 115.304 123.037 71.641  1.00 95.21  ?  171  GLY   D O     1 
ATOM   16444 N  N     . GLU   D 2 173 ? 117.188 122.165 72.500  1.00 97.51  ?  172  GLU   D N     1 
ATOM   16445 C  CA    . GLU   D 2 173 ? 118.041 123.143 71.839  1.00 100.68 ?  172  GLU   D CA    1 
ATOM   16446 C  C     . GLU   D 2 173 ? 118.050 122.923 70.331  1.00 103.32 ?  172  GLU   D C     1 
ATOM   16447 O  O     . GLU   D 2 173 ? 118.098 121.786 69.853  1.00 101.86 ?  172  GLU   D O     1 
ATOM   16448 C  CB    . GLU   D 2 173 ? 119.463 123.061 72.391  1.00 99.48  ?  172  GLU   D CB    1 
ATOM   16449 C  CG    . GLU   D 2 173 ? 120.365 124.201 71.950  1.00 102.83 ?  172  GLU   D CG    1 
ATOM   16450 C  CD    . GLU   D 2 173 ? 121.537 124.413 72.887  1.00 107.04 ?  172  GLU   D CD    1 
ATOM   16451 O  OE1   . GLU   D 2 173 ? 121.988 123.429 73.511  1.00 105.95 ?  172  GLU   D OE1   1 
ATOM   16452 O  OE2   . GLU   D 2 173 ? 122.007 125.564 73.001  1.00 105.73 ?  172  GLU   D OE2   1 
ATOM   16453 N  N     . GLY   D 2 174 ? 118.002 124.017 69.582  1.00 98.25  ?  173  GLY   D N     1 
ATOM   16454 C  CA    . GLY   D 2 174 ? 118.092 123.979 68.141  1.00 96.54  ?  173  GLY   D CA    1 
ATOM   16455 C  C     . GLY   D 2 174 ? 117.082 124.912 67.509  1.00 95.65  ?  173  GLY   D C     1 
ATOM   16456 O  O     . GLY   D 2 174 ? 116.403 125.686 68.184  1.00 97.48  ?  173  GLY   D O     1 
ATOM   16457 N  N     . THR   D 2 175 ? 116.986 124.829 66.186  1.00 99.62  ?  174  THR   D N     1 
ATOM   16458 C  CA    . THR   D 2 175 ? 116.036 125.615 65.411  1.00 100.82 ?  174  THR   D CA    1 
ATOM   16459 C  C     . THR   D 2 175 ? 114.870 124.727 64.999  1.00 103.56 ?  174  THR   D C     1 
ATOM   16460 O  O     . THR   D 2 175 ? 115.073 123.675 64.385  1.00 105.37 ?  174  THR   D O     1 
ATOM   16461 C  CB    . THR   D 2 175 ? 116.705 126.217 64.174  1.00 100.90 ?  174  THR   D CB    1 
ATOM   16462 O  OG1   . THR   D 2 175 ? 117.690 127.175 64.579  1.00 103.50 ?  174  THR   D OG1   1 
ATOM   16463 C  CG2   . THR   D 2 175 ? 115.676 126.901 63.290  1.00 99.98  ?  174  THR   D CG2   1 
ATOM   16464 N  N     . HIS   D 2 176 ? 113.656 125.151 65.337  1.00 97.64  ?  175  HIS   D N     1 
ATOM   16465 C  CA    . HIS   D 2 176 ? 112.452 124.381 65.074  1.00 96.48  ?  175  HIS   D CA    1 
ATOM   16466 C  C     . HIS   D 2 176 ? 111.450 125.254 64.335  1.00 96.98  ?  175  HIS   D C     1 
ATOM   16467 O  O     . HIS   D 2 176 ? 111.592 126.476 64.259  1.00 97.42  ?  175  HIS   D O     1 
ATOM   16468 C  CB    . HIS   D 2 176 ? 111.837 123.846 66.375  1.00 94.13  ?  175  HIS   D CB    1 
ATOM   16469 C  CG    . HIS   D 2 176 ? 112.826 123.193 67.289  1.00 93.92  ?  175  HIS   D CG    1 
ATOM   16470 N  ND1   . HIS   D 2 176 ? 113.786 123.902 67.979  1.00 95.70  ?  175  HIS   D ND1   1 
ATOM   16471 C  CD2   . HIS   D 2 176 ? 113.009 121.893 67.622  1.00 94.18  ?  175  HIS   D CD2   1 
ATOM   16472 C  CE1   . HIS   D 2 176 ? 114.515 123.069 68.699  1.00 93.99  ?  175  HIS   D CE1   1 
ATOM   16473 N  NE2   . HIS   D 2 176 ? 114.064 121.844 68.501  1.00 94.32  ?  175  HIS   D NE2   1 
ATOM   16474 N  N     . THR   D 2 177 ? 110.424 124.611 63.784  1.00 107.46 ?  176  THR   D N     1 
ATOM   16475 C  CA    . THR   D 2 177 ? 109.363 125.298 63.056  1.00 110.25 ?  176  THR   D CA    1 
ATOM   16476 C  C     . THR   D 2 177 ? 108.034 125.014 63.737  1.00 110.13 ?  176  THR   D C     1 
ATOM   16477 O  O     . THR   D 2 177 ? 107.642 123.851 63.877  1.00 110.26 ?  176  THR   D O     1 
ATOM   16478 C  CB    . THR   D 2 177 ? 109.318 124.856 61.594  1.00 111.92 ?  176  THR   D CB    1 
ATOM   16479 O  OG1   . THR   D 2 177 ? 109.100 123.443 61.523  1.00 111.33 ?  176  THR   D OG1   1 
ATOM   16480 C  CG2   . THR   D 2 177 ? 110.625 125.198 60.895  1.00 109.48 ?  176  THR   D CG2   1 
ATOM   16481 N  N     . VAL   D 2 178 ? 107.361 126.069 64.189  1.00 109.11 ?  177  VAL   D N     1 
ATOM   16482 C  CA    . VAL   D 2 178 ? 106.051 125.966 64.820  1.00 108.63 ?  177  VAL   D CA    1 
ATOM   16483 C  C     . VAL   D 2 178 ? 105.100 126.872 64.055  1.00 108.03 ?  177  VAL   D C     1 
ATOM   16484 O  O     . VAL   D 2 178 ? 105.324 128.087 63.976  1.00 108.28 ?  177  VAL   D O     1 
ATOM   16485 C  CB    . VAL   D 2 178 ? 106.091 126.351 66.308  1.00 109.17 ?  177  VAL   D CB    1 
ATOM   16486 C  CG1   . VAL   D 2 178 ? 104.768 126.008 66.968  1.00 108.31 ?  177  VAL   D CG1   1 
ATOM   16487 C  CG2   . VAL   D 2 178 ? 107.241 125.653 67.015  1.00 105.61 ?  177  VAL   D CG2   1 
ATOM   16488 N  N     . ASN   D 2 179 ? 104.047 126.281 63.488  1.00 113.38 ?  178  ASN   D N     1 
ATOM   16489 C  CA    . ASN   D 2 179 ? 103.019 127.020 62.753  1.00 114.89 ?  178  ASN   D CA    1 
ATOM   16490 C  C     . ASN   D 2 179 ? 103.631 127.895 61.661  1.00 115.80 ?  178  ASN   D C     1 
ATOM   16491 O  O     . ASN   D 2 179 ? 103.189 129.019 61.412  1.00 113.70 ?  178  ASN   D O     1 
ATOM   16492 C  CB    . ASN   D 2 179 ? 102.161 127.855 63.706  1.00 115.69 ?  178  ASN   D CB    1 
ATOM   16493 C  CG    . ASN   D 2 179 ? 101.259 127.001 64.573  1.00 115.48 ?  178  ASN   D CG    1 
ATOM   16494 O  OD1   . ASN   D 2 179 ? 100.737 125.980 64.128  1.00 114.09 ?  178  ASN   D OD1   1 
ATOM   16495 N  ND2   . ASN   D 2 179 ? 101.073 127.415 65.820  1.00 115.09 ?  178  ASN   D ND2   1 
ATOM   16496 N  N     . GLY   D 2 180 ? 104.664 127.374 61.004  1.00 119.03 ?  179  GLY   D N     1 
ATOM   16497 C  CA    . GLY   D 2 180 ? 105.308 128.088 59.924  1.00 120.10 ?  179  GLY   D CA    1 
ATOM   16498 C  C     . GLY   D 2 180 ? 106.250 129.192 60.341  1.00 120.63 ?  179  GLY   D C     1 
ATOM   16499 O  O     . GLY   D 2 180 ? 106.732 129.930 59.474  1.00 119.44 ?  179  GLY   D O     1 
ATOM   16500 N  N     . LYS   D 2 181 ? 106.530 129.340 61.632  1.00 117.92 ?  180  LYS   D N     1 
ATOM   16501 C  CA    . LYS   D 2 181 ? 107.477 130.342 62.089  1.00 116.21 ?  180  LYS   D CA    1 
ATOM   16502 C  C     . LYS   D 2 181 ? 108.643 129.668 62.803  1.00 115.65 ?  180  LYS   D C     1 
ATOM   16503 O  O     . LYS   D 2 181 ? 108.472 128.645 63.474  1.00 115.37 ?  180  LYS   D O     1 
ATOM   16504 C  CB    . LYS   D 2 181 ? 106.810 131.375 63.003  1.00 116.45 ?  180  LYS   D CB    1 
ATOM   16505 C  CG    . LYS   D 2 181 ? 105.297 131.531 62.856  1.00 117.02 ?  180  LYS   D CG    1 
ATOM   16506 C  CD    . LYS   D 2 181 ? 104.795 132.837 63.442  1.00 117.77 ?  180  LYS   D CD    1 
ATOM   16507 C  CE    . LYS   D 2 181 ? 105.347 134.050 62.703  1.00 118.51 ?  180  LYS   D CE    1 
ATOM   16508 N  NZ    . LYS   D 2 181 ? 104.914 134.101 61.280  1.00 115.04 ?  180  LYS   D NZ    1 
ATOM   16509 N  N     . THR   D 2 182 ? 109.831 130.240 62.636  1.00 104.31 ?  181  THR   D N     1 
ATOM   16510 C  CA    . THR   D 2 182 ? 111.063 129.651 63.144  1.00 104.86 ?  181  THR   D CA    1 
ATOM   16511 C  C     . THR   D 2 182 ? 111.299 130.081 64.585  1.00 105.37 ?  181  THR   D C     1 
ATOM   16512 O  O     . THR   D 2 182 ? 111.272 131.275 64.898  1.00 103.80 ?  181  THR   D O     1 
ATOM   16513 C  CB    . THR   D 2 182 ? 112.250 130.059 62.270  1.00 104.25 ?  181  THR   D CB    1 
ATOM   16514 O  OG1   . THR   D 2 182 ? 112.278 129.253 61.085  1.00 105.63 ?  181  THR   D OG1   1 
ATOM   16515 C  CG2   . THR   D 2 182 ? 113.561 129.887 63.021  1.00 102.33 ?  181  THR   D CG2   1 
ATOM   16516 N  N     . VAL   D 2 183 ? 111.506 129.100 65.459  1.00 101.76 ?  182  VAL   D N     1 
ATOM   16517 C  CA    . VAL   D 2 183 ? 111.791 129.331 66.869  1.00 98.61  ?  182  VAL   D CA    1 
ATOM   16518 C  C     . VAL   D 2 183 ? 113.169 128.757 67.162  1.00 98.98  ?  182  VAL   D C     1 
ATOM   16519 O  O     . VAL   D 2 183 ? 113.422 127.573 66.908  1.00 100.25 ?  182  VAL   D O     1 
ATOM   16520 C  CB    . VAL   D 2 183 ? 110.728 128.695 67.779  1.00 99.00  ?  182  VAL   D CB    1 
ATOM   16521 C  CG1   . VAL   D 2 183 ? 110.988 129.064 69.231  1.00 97.74  ?  182  VAL   D CG1   1 
ATOM   16522 C  CG2   . VAL   D 2 183 ? 109.335 129.126 67.351  1.00 100.09 ?  182  VAL   D CG2   1 
ATOM   16523 N  N     . THR   D 2 184 ? 114.056 129.590 67.696  1.00 96.19  ?  183  THR   D N     1 
ATOM   16524 C  CA    . THR   D 2 184 ? 115.417 129.185 68.031  1.00 96.04  ?  183  THR   D CA    1 
ATOM   16525 C  C     . THR   D 2 184 ? 115.514 129.043 69.544  1.00 94.19  ?  183  THR   D C     1 
ATOM   16526 O  O     . THR   D 2 184 ? 115.480 130.043 70.269  1.00 96.10  ?  183  THR   D O     1 
ATOM   16527 C  CB    . THR   D 2 184 ? 116.435 130.198 67.510  1.00 97.24  ?  183  THR   D CB    1 
ATOM   16528 O  OG1   . THR   D 2 184 ? 115.915 131.524 67.667  1.00 98.37  ?  183  THR   D OG1   1 
ATOM   16529 C  CG2   . THR   D 2 184 ? 116.731 129.947 66.041  1.00 93.83  ?  183  THR   D CG2   1 
ATOM   16530 N  N     . VAL   D 2 185 ? 115.632 127.807 70.020  1.00 85.87  ?  184  VAL   D N     1 
ATOM   16531 C  CA    . VAL   D 2 185 ? 115.792 127.525 71.440  1.00 84.29  ?  184  VAL   D CA    1 
ATOM   16532 C  C     . VAL   D 2 185 ? 117.278 127.344 71.712  1.00 84.00  ?  184  VAL   D C     1 
ATOM   16533 O  O     . VAL   D 2 185 ? 117.916 126.446 71.152  1.00 88.86  ?  184  VAL   D O     1 
ATOM   16534 C  CB    . VAL   D 2 185 ? 114.996 126.282 71.863  1.00 84.08  ?  184  VAL   D CB    1 
ATOM   16535 C  CG1   . VAL   D 2 185 ? 115.333 125.903 73.293  1.00 84.74  ?  184  VAL   D CG1   1 
ATOM   16536 C  CG2   . VAL   D 2 185 ? 113.504 126.531 71.710  1.00 85.15  ?  184  VAL   D CG2   1 
ATOM   16537 N  N     . SER   D 2 186 ? 117.830 128.198 72.566  1.00 84.61  ?  185  SER   D N     1 
ATOM   16538 C  CA    . SER   D 2 186 ? 119.246 128.177 72.890  1.00 88.99  ?  185  SER   D CA    1 
ATOM   16539 C  C     . SER   D 2 186 ? 119.419 128.093 74.396  1.00 94.89  ?  185  SER   D C     1 
ATOM   16540 O  O     . SER   D 2 186 ? 118.695 128.750 75.151  1.00 97.61  ?  185  SER   D O     1 
ATOM   16541 C  CB    . SER   D 2 186 ? 119.961 129.422 72.350  1.00 88.34  ?  185  SER   D CB    1 
ATOM   16542 O  OG    . SER   D 2 186 ? 121.204 129.618 72.999  1.00 90.08  ?  185  SER   D OG    1 
ATOM   16543 N  N     . LEU   D 2 187 ? 120.381 127.278 74.829  1.00 89.58  ?  186  LEU   D N     1 
ATOM   16544 C  CA    . LEU   D 2 187 ? 120.687 127.203 76.251  1.00 88.51  ?  186  LEU   D CA    1 
ATOM   16545 C  C     . LEU   D 2 187 ? 121.348 128.480 76.749  1.00 90.35  ?  186  LEU   D C     1 
ATOM   16546 O  O     . LEU   D 2 187 ? 121.128 128.874 77.898  1.00 94.76  ?  186  LEU   D O     1 
ATOM   16547 C  CB    . LEU   D 2 187 ? 121.567 125.991 76.539  1.00 88.02  ?  186  LEU   D CB    1 
ATOM   16548 C  CG    . LEU   D 2 187 ? 121.554 125.489 77.983  1.00 90.01  ?  186  LEU   D CG    1 
ATOM   16549 C  CD1   . LEU   D 2 187 ? 120.171 124.979 78.347  1.00 89.10  ?  186  LEU   D CD1   1 
ATOM   16550 C  CD2   . LEU   D 2 187 ? 122.598 124.403 78.187  1.00 90.35  ?  186  LEU   D CD2   1 
ATOM   16551 N  N     . ARG   D 2 188 ? 122.138 129.144 75.901  1.00 92.59  ?  187  ARG   D N     1 
ATOM   16552 C  CA    . ARG   D 2 188 ? 122.736 130.420 76.279  1.00 91.45  ?  187  ARG   D CA    1 
ATOM   16553 C  C     . ARG   D 2 188 ? 121.670 131.484 76.506  1.00 93.91  ?  187  ARG   D C     1 
ATOM   16554 O  O     . ARG   D 2 188 ? 121.736 132.244 77.480  1.00 99.64  ?  187  ARG   D O     1 
ATOM   16555 C  CB    . ARG   D 2 188 ? 123.723 130.862 75.199  1.00 92.14  ?  187  ARG   D CB    1 
ATOM   16556 C  CG    . ARG   D 2 188 ? 124.391 132.198 75.460  1.00 94.52  ?  187  ARG   D CG    1 
ATOM   16557 C  CD    . ARG   D 2 188 ? 125.668 132.337 74.645  1.00 93.38  ?  187  ARG   D CD    1 
ATOM   16558 N  NE    . ARG   D 2 188 ? 126.568 133.341 75.197  1.00 97.38  ?  187  ARG   D NE    1 
ATOM   16559 C  CZ    . ARG   D 2 188 ? 127.707 133.067 75.819  1.00 99.27  ?  187  ARG   D CZ    1 
ATOM   16560 N  NH1   . ARG   D 2 188 ? 128.115 131.821 75.996  1.00 97.02  ?  187  ARG   D NH1   1 
ATOM   16561 N  NH2   . ARG   D 2 188 ? 128.452 134.068 76.278  1.00 96.77  ?  187  ARG   D NH2   1 
ATOM   16562 N  N     . GLU   D 2 189 ? 120.675 131.550 75.618  1.00 88.44  ?  188  GLU   D N     1 
ATOM   16563 C  CA    . GLU   D 2 189 ? 119.598 132.521 75.779  1.00 88.45  ?  188  GLU   D CA    1 
ATOM   16564 C  C     . GLU   D 2 189 ? 118.794 132.248 77.044  1.00 90.67  ?  188  GLU   D C     1 
ATOM   16565 O  O     . GLU   D 2 189 ? 118.423 133.180 77.768  1.00 94.79  ?  188  GLU   D O     1 
ATOM   16566 C  CB    . GLU   D 2 189 ? 118.688 132.498 74.551  1.00 89.06  ?  188  GLU   D CB    1 
ATOM   16567 C  CG    . GLU   D 2 189 ? 118.977 133.580 73.524  1.00 92.79  ?  188  GLU   D CG    1 
ATOM   16568 C  CD    . GLU   D 2 189 ? 119.315 134.917 74.157  1.00 99.70  ?  188  GLU   D CD    1 
ATOM   16569 O  OE1   . GLU   D 2 189 ? 118.493 135.426 74.948  1.00 100.89 ?  188  GLU   D OE1   1 
ATOM   16570 O  OE2   . GLU   D 2 189 ? 120.401 135.461 73.862  1.00 100.84 ?  188  GLU   D OE2   1 
ATOM   16571 N  N     . LEU   D 2 190 ? 118.517 130.975 77.328  1.00 73.32  ?  189  LEU   D N     1 
ATOM   16572 C  CA    . LEU   D 2 190 ? 117.766 130.634 78.531  1.00 71.69  ?  189  LEU   D CA    1 
ATOM   16573 C  C     . LEU   D 2 190 ? 118.574 130.924 79.790  1.00 76.97  ?  189  LEU   D C     1 
ATOM   16574 O  O     . LEU   D 2 190 ? 118.013 131.349 80.806  1.00 85.95  ?  189  LEU   D O     1 
ATOM   16575 C  CB    . LEU   D 2 190 ? 117.337 129.170 78.475  1.00 72.67  ?  189  LEU   D CB    1 
ATOM   16576 C  CG    . LEU   D 2 190 ? 116.568 128.607 79.669  1.00 75.18  ?  189  LEU   D CG    1 
ATOM   16577 C  CD1   . LEU   D 2 190 ? 115.269 129.362 79.866  1.00 78.25  ?  189  LEU   D CD1   1 
ATOM   16578 C  CD2   . LEU   D 2 190 ? 116.298 127.127 79.469  1.00 74.76  ?  189  LEU   D CD2   1 
ATOM   16579 N  N     . LYS   D 2 191 ? 119.893 130.718 79.739  1.00 78.02  ?  190  LYS   D N     1 
ATOM   16580 C  CA    . LYS   D 2 191 ? 120.749 131.087 80.862  1.00 77.60  ?  190  LYS   D CA    1 
ATOM   16581 C  C     . LYS   D 2 191 ? 120.733 132.592 81.090  1.00 78.96  ?  190  LYS   D C     1 
ATOM   16582 O  O     . LYS   D 2 191 ? 120.683 133.054 82.236  1.00 84.02  ?  190  LYS   D O     1 
ATOM   16583 C  CB    . LYS   D 2 191 ? 122.174 130.592 80.617  1.00 76.60  ?  190  LYS   D CB    1 
ATOM   16584 C  CG    . LYS   D 2 191 ? 122.372 129.120 80.921  1.00 77.22  ?  190  LYS   D CG    1 
ATOM   16585 C  CD    . LYS   D 2 191 ? 123.757 128.640 80.535  1.00 79.02  ?  190  LYS   D CD    1 
ATOM   16586 C  CE    . LYS   D 2 191 ? 123.921 127.160 80.837  1.00 77.98  ?  190  LYS   D CE    1 
ATOM   16587 N  NZ    . LYS   D 2 191 ? 125.172 126.606 80.255  1.00 83.39  ?  190  LYS   D NZ    1 
ATOM   16588 N  N     . LYS   D 2 192 ? 120.774 133.372 80.007  1.00 79.08  ?  191  LYS   D N     1 
ATOM   16589 C  CA    . LYS   D 2 192 ? 120.676 134.822 80.140  1.00 78.53  ?  191  LYS   D CA    1 
ATOM   16590 C  C     . LYS   D 2 192 ? 119.342 135.229 80.748  1.00 81.48  ?  191  LYS   D C     1 
ATOM   16591 O  O     . LYS   D 2 192 ? 119.285 136.113 81.612  1.00 86.93  ?  191  LYS   D O     1 
ATOM   16592 C  CB    . LYS   D 2 192 ? 120.867 135.492 78.780  1.00 81.83  ?  191  LYS   D CB    1 
ATOM   16593 C  CG    . LYS   D 2 192 ? 121.339 136.933 78.874  1.00 87.89  ?  191  LYS   D CG    1 
ATOM   16594 C  CD    . LYS   D 2 192 ? 122.117 137.349 77.639  1.00 88.22  ?  191  LYS   D CD    1 
ATOM   16595 C  CE    . LYS   D 2 192 ? 122.073 138.854 77.440  1.00 88.77  ?  191  LYS   D CE    1 
ATOM   16596 N  NZ    . LYS   D 2 192 ? 120.713 139.322 77.057  1.00 86.20  ?  191  LYS   D NZ    1 
ATOM   16597 N  N     . LYS   D 2 193 ? 118.256 134.596 80.305  1.00 73.80  ?  192  LYS   D N     1 
ATOM   16598 C  CA    . LYS   D 2 193 ? 116.943 134.908 80.856  1.00 71.08  ?  192  LYS   D CA    1 
ATOM   16599 C  C     . LYS   D 2 193 ? 116.875 134.578 82.341  1.00 73.79  ?  192  LYS   D C     1 
ATOM   16600 O  O     . LYS   D 2 193 ? 116.314 135.346 83.130  1.00 81.14  ?  192  LYS   D O     1 
ATOM   16601 C  CB    . LYS   D 2 193 ? 115.860 134.147 80.095  1.00 72.73  ?  192  LYS   D CB    1 
ATOM   16602 C  CG    . LYS   D 2 193 ? 115.524 134.698 78.725  1.00 77.94  ?  192  LYS   D CG    1 
ATOM   16603 C  CD    . LYS   D 2 193 ? 115.150 136.171 78.814  1.00 81.62  ?  192  LYS   D CD    1 
ATOM   16604 C  CE    . LYS   D 2 193 ? 115.004 136.789 77.435  1.00 81.14  ?  192  LYS   D CE    1 
ATOM   16605 N  NZ    . LYS   D 2 193 ? 114.597 138.220 77.502  1.00 81.89  ?  192  LYS   D NZ    1 
ATOM   16606 N  N     . LEU   D 2 194 ? 117.433 133.432 82.739  1.00 67.54  ?  193  LEU   D N     1 
ATOM   16607 C  CA    . LEU   D 2 194 ? 117.414 133.052 84.147  1.00 69.00  ?  193  LEU   D CA    1 
ATOM   16608 C  C     . LEU   D 2 194 ? 118.248 134.004 84.992  1.00 72.74  ?  193  LEU   D C     1 
ATOM   16609 O  O     . LEU   D 2 194 ? 117.825 134.392 86.086  1.00 77.21  ?  193  LEU   D O     1 
ATOM   16610 C  CB    . LEU   D 2 194 ? 117.898 131.615 84.318  1.00 68.80  ?  193  LEU   D CB    1 
ATOM   16611 C  CG    . LEU   D 2 194 ? 118.157 131.192 85.767  1.00 68.48  ?  193  LEU   D CG    1 
ATOM   16612 C  CD1   . LEU   D 2 194 ? 116.869 130.724 86.413  1.00 72.34  ?  193  LEU   D CD1   1 
ATOM   16613 C  CD2   . LEU   D 2 194 ? 119.217 130.110 85.850  1.00 68.15  ?  193  LEU   D CD2   1 
ATOM   16614 N  N     . TYR   D 2 195 ? 119.413 134.421 84.487  1.00 80.06  ?  194  TYR   D N     1 
ATOM   16615 C  CA    . TYR   D 2 195 ? 120.232 135.384 85.216  1.00 74.24  ?  194  TYR   D CA    1 
ATOM   16616 C  C     . TYR   D 2 195 ? 119.516 136.721 85.365  1.00 77.54  ?  194  TYR   D C     1 
ATOM   16617 O  O     . TYR   D 2 195 ? 119.536 137.328 86.443  1.00 84.10  ?  194  TYR   D O     1 
ATOM   16618 C  CB    . TYR   D 2 195 ? 121.572 135.567 84.511  1.00 76.89  ?  194  TYR   D CB    1 
ATOM   16619 C  CG    . TYR   D 2 195 ? 122.637 136.167 85.393  1.00 77.51  ?  194  TYR   D CG    1 
ATOM   16620 C  CD1   . TYR   D 2 195 ? 123.277 135.404 86.357  1.00 83.18  ?  194  TYR   D CD1   1 
ATOM   16621 C  CD2   . TYR   D 2 195 ? 123.003 137.498 85.264  1.00 77.38  ?  194  TYR   D CD2   1 
ATOM   16622 C  CE1   . TYR   D 2 195 ? 124.252 135.948 87.167  1.00 83.63  ?  194  TYR   D CE1   1 
ATOM   16623 C  CE2   . TYR   D 2 195 ? 123.977 138.051 86.071  1.00 80.02  ?  194  TYR   D CE2   1 
ATOM   16624 C  CZ    . TYR   D 2 195 ? 124.598 137.271 87.020  1.00 83.87  ?  194  TYR   D CZ    1 
ATOM   16625 O  OH    . TYR   D 2 195 ? 125.569 137.816 87.827  1.00 88.85  ?  194  TYR   D OH    1 
ATOM   16626 N  N     . LEU   D 2 196 ? 118.874 137.194 84.294  1.00 74.64  ?  195  LEU   D N     1 
ATOM   16627 C  CA    . LEU   D 2 196 ? 118.140 138.452 84.369  1.00 72.34  ?  195  LEU   D CA    1 
ATOM   16628 C  C     . LEU   D 2 196 ? 116.973 138.356 85.343  1.00 78.74  ?  195  LEU   D C     1 
ATOM   16629 O  O     . LEU   D 2 196 ? 116.730 139.283 86.124  1.00 90.20  ?  195  LEU   D O     1 
ATOM   16630 C  CB    . LEU   D 2 196 ? 117.653 138.855 82.981  1.00 77.39  ?  195  LEU   D CB    1 
ATOM   16631 C  CG    . LEU   D 2 196 ? 118.560 139.790 82.185  1.00 79.27  ?  195  LEU   D CG    1 
ATOM   16632 C  CD1   . LEU   D 2 196 ? 117.922 140.145 80.852  1.00 81.07  ?  195  LEU   D CD1   1 
ATOM   16633 C  CD2   . LEU   D 2 196 ? 118.869 141.041 82.988  1.00 83.20  ?  195  LEU   D CD2   1 
ATOM   16634 N  N     . CYS   D 2 197 ? 116.254 137.230 85.330  1.00 74.65  ?  196  CYS   D N     1 
ATOM   16635 C  CA    . CYS   D 2 197 ? 115.157 137.041 86.271  1.00 72.36  ?  196  CYS   D CA    1 
ATOM   16636 C  C     . CYS   D 2 197 ? 115.659 137.022 87.708  1.00 71.63  ?  196  CYS   D C     1 
ATOM   16637 O  O     . CYS   D 2 197 ? 115.047 137.630 88.592  1.00 76.51  ?  196  CYS   D O     1 
ATOM   16638 C  CB    . CYS   D 2 197 ? 114.404 135.754 85.947  1.00 73.54  ?  196  CYS   D CB    1 
ATOM   16639 S  SG    . CYS   D 2 197 ? 113.003 135.420 87.033  1.00 90.73  ?  196  CYS   D SG    1 
ATOM   16640 N  N     . LEU   D 2 198 ? 116.779 136.343 87.959  1.00 66.57  ?  197  LEU   D N     1 
ATOM   16641 C  CA    . LEU   D 2 198 ? 117.328 136.296 89.310  1.00 63.99  ?  197  LEU   D CA    1 
ATOM   16642 C  C     . LEU   D 2 198 ? 117.773 137.676 89.776  1.00 66.22  ?  197  LEU   D C     1 
ATOM   16643 O  O     . LEU   D 2 198 ? 117.572 138.039 90.940  1.00 76.00  ?  197  LEU   D O     1 
ATOM   16644 C  CB    . LEU   D 2 198 ? 118.484 135.303 89.370  1.00 66.26  ?  197  LEU   D CB    1 
ATOM   16645 C  CG    . LEU   D 2 198 ? 118.114 133.865 89.733  1.00 67.28  ?  197  LEU   D CG    1 
ATOM   16646 C  CD1   . LEU   D 2 198 ? 119.361 133.031 89.966  1.00 70.97  ?  197  LEU   D CD1   1 
ATOM   16647 C  CD2   . LEU   D 2 198 ? 117.212 133.837 90.954  1.00 73.35  ?  197  LEU   D CD2   1 
ATOM   16648 N  N     . MET   D 2 199 ? 118.369 138.464 88.878  1.00 79.11  ?  198  MET   D N     1 
ATOM   16649 C  CA    . MET   D 2 199 ? 118.732 139.831 89.228  1.00 77.35  ?  198  MET   D CA    1 
ATOM   16650 C  C     . MET   D 2 199 ? 117.498 140.672 89.527  1.00 79.88  ?  198  MET   D C     1 
ATOM   16651 O  O     . MET   D 2 199 ? 117.513 141.501 90.444  1.00 86.14  ?  198  MET   D O     1 
ATOM   16652 C  CB    . MET   D 2 199 ? 119.555 140.455 88.105  1.00 79.25  ?  198  MET   D CB    1 
ATOM   16653 C  CG    . MET   D 2 199 ? 121.003 140.023 88.097  1.00 86.20  ?  198  MET   D CG    1 
ATOM   16654 S  SD    . MET   D 2 199 ? 122.035 141.108 89.096  1.00 101.24 ?  198  MET   D SD    1 
ATOM   16655 C  CE    . MET   D 2 199 ? 123.652 140.395 88.818  1.00 83.50  ?  198  MET   D CE    1 
ATOM   16656 N  N     . SER   D 2 200 ? 116.419 140.471 88.766  1.00 73.37  ?  199  SER   D N     1 
ATOM   16657 C  CA    . SER   D 2 200 ? 115.175 141.184 89.044  1.00 68.48  ?  199  SER   D CA    1 
ATOM   16658 C  C     . SER   D 2 200 ? 114.623 140.813 90.414  1.00 70.31  ?  199  SER   D C     1 
ATOM   16659 O  O     . SER   D 2 200 ? 114.142 141.679 91.152  1.00 77.12  ?  199  SER   D O     1 
ATOM   16660 C  CB    . SER   D 2 200 ? 114.149 140.892 87.950  1.00 73.75  ?  199  SER   D CB    1 
ATOM   16661 O  OG    . SER   D 2 200 ? 112.829 141.078 88.427  1.00 82.33  ?  199  SER   D OG    1 
ATOM   16662 N  N     . VAL   D 2 201 ? 114.683 139.529 90.772  1.00 65.92  ?  200  VAL   D N     1 
ATOM   16663 C  CA    . VAL   D 2 201 ? 114.214 139.096 92.088  1.00 64.22  ?  200  VAL   D CA    1 
ATOM   16664 C  C     . VAL   D 2 201 ? 115.067 139.712 93.189  1.00 72.56  ?  200  VAL   D C     1 
ATOM   16665 O  O     . VAL   D 2 201 ? 114.555 140.131 94.238  1.00 78.00  ?  200  VAL   D O     1 
ATOM   16666 C  CB    . VAL   D 2 201 ? 114.213 137.561 92.184  1.00 64.41  ?  200  VAL   D CB    1 
ATOM   16667 C  CG1   . VAL   D 2 201 ? 113.844 137.125 93.587  1.00 64.98  ?  200  VAL   D CG1   1 
ATOM   16668 C  CG2   . VAL   D 2 201 ? 113.266 136.969 91.178  1.00 67.77  ?  200  VAL   D CG2   1 
ATOM   16669 N  N     . ASN   D 2 202 ? 116.386 139.740 92.985  1.00 77.54  ?  201  ASN   D N     1 
ATOM   16670 C  CA    . ASN   D 2 202 ? 117.278 140.335 93.974  1.00 69.41  ?  201  ASN   D CA    1 
ATOM   16671 C  C     . ASN   D 2 202 ? 116.977 141.816 94.161  1.00 74.52  ?  201  ASN   D C     1 
ATOM   16672 O  O     . ASN   D 2 202 ? 116.959 142.319 95.291  1.00 85.67  ?  201  ASN   D O     1 
ATOM   16673 C  CB    . ASN   D 2 202 ? 118.733 140.129 93.556  1.00 69.62  ?  201  ASN   D CB    1 
ATOM   16674 C  CG    . ASN   D 2 202 ? 119.712 140.618 94.600  1.00 78.92  ?  201  ASN   D CG    1 
ATOM   16675 O  OD1   . ASN   D 2 202 ? 119.889 139.992 95.644  1.00 79.64  ?  201  ASN   D OD1   1 
ATOM   16676 N  ND2   . ASN   D 2 202 ? 120.353 141.747 94.326  1.00 84.93  ?  201  ASN   D ND2   1 
ATOM   16677 N  N     . ALA   D 2 203 ? 116.723 142.525 93.059  1.00 67.58  ?  202  ALA   D N     1 
ATOM   16678 C  CA    . ALA   D 2 203 ? 116.373 143.938 93.143  1.00 66.08  ?  202  ALA   D CA    1 
ATOM   16679 C  C     . ALA   D 2 203 ? 115.030 144.125 93.834  1.00 68.25  ?  202  ALA   D C     1 
ATOM   16680 O  O     . ALA   D 2 203 ? 114.838 145.091 94.580  1.00 72.89  ?  202  ALA   D O     1 
ATOM   16681 C  CB    . ALA   D 2 203 ? 116.352 144.562 91.747  1.00 66.20  ?  202  ALA   D CB    1 
ATOM   16682 N  N     . LEU   D 2 204 ? 114.096 143.201 93.606  1.00 76.17  ?  203  LEU   D N     1 
ATOM   16683 C  CA    . LEU   D 2 204 ? 112.780 143.298 94.227  1.00 73.98  ?  203  LEU   D CA    1 
ATOM   16684 C  C     . LEU   D 2 204 ? 112.865 143.136 95.737  1.00 75.65  ?  203  LEU   D C     1 
ATOM   16685 O  O     . LEU   D 2 204 ? 112.355 143.974 96.487  1.00 82.82  ?  203  LEU   D O     1 
ATOM   16686 C  CB    . LEU   D 2 204 ? 111.842 142.254 93.624  1.00 73.66  ?  203  LEU   D CB    1 
ATOM   16687 C  CG    . LEU   D 2 204 ? 110.370 142.282 94.050  1.00 75.93  ?  203  LEU   D CG    1 
ATOM   16688 C  CD1   . LEU   D 2 204 ? 109.499 141.806 92.909  1.00 76.16  ?  203  LEU   D CD1   1 
ATOM   16689 C  CD2   . LEU   D 2 204 ? 110.102 141.440 95.291  1.00 77.07  ?  203  LEU   D CD2   1 
ATOM   16690 N  N     . GLU   D 2 205 ? 113.541 142.090 96.204  1.00 73.62  ?  204  GLU   D N     1 
ATOM   16691 C  CA    . GLU   D 2 205 ? 113.579 141.803 97.631  1.00 70.47  ?  204  GLU   D CA    1 
ATOM   16692 C  C     . GLU   D 2 205 ? 114.668 142.569 98.372  1.00 76.88  ?  204  GLU   D C     1 
ATOM   16693 O  O     . GLU   D 2 205 ? 114.689 142.546 99.606  1.00 85.64  ?  204  GLU   D O     1 
ATOM   16694 C  CB    . GLU   D 2 205 ? 113.754 140.298 97.849  1.00 70.94  ?  204  GLU   D CB    1 
ATOM   16695 C  CG    . GLU   D 2 205 ? 112.568 139.473 97.375  1.00 78.86  ?  204  GLU   D CG    1 
ATOM   16696 C  CD    . GLU   D 2 205 ? 112.472 138.123 98.038  1.00 81.21  ?  204  GLU   D CD    1 
ATOM   16697 O  OE1   . GLU   D 2 205 ? 113.223 137.225 97.617  1.00 82.63  ?  204  GLU   D OE1   1 
ATOM   16698 O  OE2   . GLU   D 2 205 ? 111.640 137.958 98.959  1.00 74.98  ?  204  GLU   D OE2   1 
ATOM   16699 N  N     . ALA   D 2 206 ? 115.544 143.269 97.654  1.00 80.03  ?  205  ALA   D N     1 
ATOM   16700 C  CA    . ALA   D 2 206 ? 116.652 144.001 98.247  1.00 79.70  ?  205  ALA   D CA    1 
ATOM   16701 C  C     . ALA   D 2 206 ? 116.364 145.482 98.357  1.00 82.37  ?  205  ALA   D C     1 
ATOM   16702 O  O     . ALA   D 2 206 ? 116.798 146.117 99.321  1.00 88.22  ?  205  ALA   D O     1 
ATOM   16703 C  CB    . ALA   D 2 206 ? 117.934 143.810 97.424  1.00 77.48  ?  205  ALA   D CB    1 
ATOM   16704 N  N     . ILE   D 2 207 ? 115.610 146.035 97.406  1.00 78.01  ?  206  ILE   D N     1 
ATOM   16705 C  CA    . ILE   D 2 207 ? 115.411 147.473 97.283  1.00 80.32  ?  206  ILE   D CA    1 
ATOM   16706 C  C     . ILE   D 2 207 ? 113.940 147.850 97.396  1.00 80.56  ?  206  ILE   D C     1 
ATOM   16707 O  O     . ILE   D 2 207 ? 113.567 148.695 98.214  1.00 89.69  ?  206  ILE   D O     1 
ATOM   16708 C  CB    . ILE   D 2 207 ? 116.009 148.012 95.967  1.00 80.47  ?  206  ILE   D CB    1 
ATOM   16709 C  CG1   . ILE   D 2 207 ? 117.434 147.499 95.775  1.00 80.70  ?  206  ILE   D CG1   1 
ATOM   16710 C  CG2   . ILE   D 2 207 ? 115.968 149.532 95.949  1.00 84.27  ?  206  ILE   D CG2   1 
ATOM   16711 C  CD1   . ILE   D 2 207 ? 118.030 147.878 94.445  1.00 83.62  ?  206  ILE   D CD1   1 
ATOM   16712 N  N     . ARG   D 2 208 ? 113.082 147.212 96.596  1.00 76.66  ?  207  ARG   D N     1 
ATOM   16713 C  CA    . ARG   D 2 208 ? 111.683 147.623 96.520  1.00 76.15  ?  207  ARG   D CA    1 
ATOM   16714 C  C     . ARG   D 2 208 ? 110.968 147.435 97.852  1.00 79.55  ?  207  ARG   D C     1 
ATOM   16715 O  O     . ARG   D 2 208 ? 110.157 148.277 98.252  1.00 84.75  ?  207  ARG   D O     1 
ATOM   16716 C  CB    . ARG   D 2 208 ? 110.974 146.847 95.412  1.00 76.14  ?  207  ARG   D CB    1 
ATOM   16717 C  CG    . ARG   D 2 208 ? 111.562 147.077 94.026  1.00 78.06  ?  207  ARG   D CG    1 
ATOM   16718 C  CD    . ARG   D 2 208 ? 110.870 146.212 92.989  1.00 79.23  ?  207  ARG   D CD    1 
ATOM   16719 N  NE    . ARG   D 2 208 ? 111.296 146.540 91.634  1.00 79.90  ?  207  ARG   D NE    1 
ATOM   16720 C  CZ    . ARG   D 2 208 ? 110.837 147.559 90.919  1.00 83.16  ?  207  ARG   D CZ    1 
ATOM   16721 N  NH1   . ARG   D 2 208 ? 109.910 148.376 91.392  1.00 83.97  ?  207  ARG   D NH1   1 
ATOM   16722 N  NH2   . ARG   D 2 208 ? 111.319 147.762 89.696  1.00 82.60  ?  207  ARG   D NH2   1 
ATOM   16723 N  N     . PHE   D 2 209 ? 111.252 146.337 98.553  1.00 78.51  ?  208  PHE   D N     1 
ATOM   16724 C  CA    . PHE   D 2 209 ? 110.557 146.071 99.806  1.00 79.40  ?  208  PHE   D CA    1 
ATOM   16725 C  C     . PHE   D 2 209 ? 111.076 146.928 100.953 1.00 81.14  ?  208  PHE   D C     1 
ATOM   16726 O  O     . PHE   D 2 209 ? 110.317 147.239 101.877 1.00 85.86  ?  208  PHE   D O     1 
ATOM   16727 C  CB    . PHE   D 2 209 ? 110.665 144.590 100.165 1.00 76.17  ?  208  PHE   D CB    1 
ATOM   16728 C  CG    . PHE   D 2 209 ? 109.413 143.818 99.890  1.00 76.52  ?  208  PHE   D CG    1 
ATOM   16729 C  CD1   . PHE   D 2 209 ? 108.254 144.087 100.593 1.00 76.64  ?  208  PHE   D CD1   1 
ATOM   16730 C  CD2   . PHE   D 2 209 ? 109.389 142.836 98.916  1.00 79.29  ?  208  PHE   D CD2   1 
ATOM   16731 C  CE1   . PHE   D 2 209 ? 107.096 143.386 100.338 1.00 78.70  ?  208  PHE   D CE1   1 
ATOM   16732 C  CE2   . PHE   D 2 209 ? 108.233 142.131 98.657  1.00 82.54  ?  208  PHE   D CE2   1 
ATOM   16733 C  CZ    . PHE   D 2 209 ? 107.085 142.409 99.369  1.00 82.17  ?  208  PHE   D CZ    1 
ATOM   16734 N  N     . TYR   D 2 210 ? 112.348 147.328 100.914 1.00 83.51  ?  209  TYR   D N     1 
ATOM   16735 C  CA    . TYR   D 2 210 ? 112.910 148.072 102.036 1.00 82.38  ?  209  TYR   D CA    1 
ATOM   16736 C  C     . TYR   D 2 210 ? 112.402 149.508 102.085 1.00 82.80  ?  209  TYR   D C     1 
ATOM   16737 O  O     . TYR   D 2 210 ? 112.291 150.083 103.173 1.00 92.31  ?  209  TYR   D O     1 
ATOM   16738 C  CB    . TYR   D 2 210 ? 114.435 148.032 101.979 1.00 80.37  ?  209  TYR   D CB    1 
ATOM   16739 C  CG    . TYR   D 2 210 ? 114.996 146.786 102.620 1.00 83.06  ?  209  TYR   D CG    1 
ATOM   16740 C  CD1   . TYR   D 2 210 ? 114.950 145.566 101.961 1.00 84.20  ?  209  TYR   D CD1   1 
ATOM   16741 C  CD2   . TYR   D 2 210 ? 115.541 146.822 103.894 1.00 84.64  ?  209  TYR   D CD2   1 
ATOM   16742 C  CE1   . TYR   D 2 210 ? 115.448 144.419 102.546 1.00 84.63  ?  209  TYR   D CE1   1 
ATOM   16743 C  CE2   . TYR   D 2 210 ? 116.041 145.681 104.488 1.00 85.27  ?  209  TYR   D CE2   1 
ATOM   16744 C  CZ    . TYR   D 2 210 ? 115.991 144.482 103.810 1.00 87.48  ?  209  TYR   D CZ    1 
ATOM   16745 O  OH    . TYR   D 2 210 ? 116.490 143.341 104.397 1.00 90.09  ?  209  TYR   D OH    1 
ATOM   16746 N  N     . VAL   D 2 211 ? 112.068 150.099 100.936 1.00 76.00  ?  210  VAL   D N     1 
ATOM   16747 C  CA    . VAL   D 2 211 ? 111.447 151.422 100.947 1.00 84.89  ?  210  VAL   D CA    1 
ATOM   16748 C  C     . VAL   D 2 211 ? 110.100 151.363 101.657 1.00 89.17  ?  210  VAL   D C     1 
ATOM   16749 O  O     . VAL   D 2 211 ? 109.793 152.194 102.523 1.00 92.73  ?  210  VAL   D O     1 
ATOM   16750 C  CB    . VAL   D 2 211 ? 111.307 151.963 99.513  1.00 87.14  ?  210  VAL   D CB    1 
ATOM   16751 C  CG1   . VAL   D 2 211 ? 110.969 153.446 99.534  1.00 86.66  ?  210  VAL   D CG1   1 
ATOM   16752 C  CG2   . VAL   D 2 211 ? 112.583 151.714 98.728  1.00 85.25  ?  210  VAL   D CG2   1 
ATOM   16753 N  N     . SER   D 2 212 ? 109.282 150.366 101.312 1.00 81.30  ?  211  SER   D N     1 
ATOM   16754 C  CA    . SER   D 2 212 ? 107.997 150.195 101.980 1.00 83.27  ?  211  SER   D CA    1 
ATOM   16755 C  C     . SER   D 2 212 ? 108.176 149.868 103.456 1.00 82.11  ?  211  SER   D C     1 
ATOM   16756 O  O     . SER   D 2 212 ? 107.368 150.291 104.291 1.00 82.86  ?  211  SER   D O     1 
ATOM   16757 C  CB    . SER   D 2 212 ? 107.188 149.102 101.281 1.00 84.81  ?  211  SER   D CB    1 
ATOM   16758 O  OG    . SER   D 2 212 ? 108.029 148.057 100.824 1.00 86.71  ?  211  SER   D OG    1 
ATOM   16759 N  N     . PHE   D 2 213 ? 109.226 149.118 103.793 1.00 80.93  ?  212  PHE   D N     1 
ATOM   16760 C  CA    . PHE   D 2 213 ? 109.545 148.876 105.194 1.00 80.62  ?  212  PHE   D CA    1 
ATOM   16761 C  C     . PHE   D 2 213 ? 109.828 150.183 105.920 1.00 81.15  ?  212  PHE   D C     1 
ATOM   16762 O  O     . PHE   D 2 213 ? 109.393 150.377 107.060 1.00 85.91  ?  212  PHE   D O     1 
ATOM   16763 C  CB    . PHE   D 2 213 ? 110.745 147.936 105.296 1.00 76.41  ?  212  PHE   D CB    1 
ATOM   16764 C  CG    . PHE   D 2 213 ? 110.451 146.526 104.880 1.00 77.69  ?  212  PHE   D CG    1 
ATOM   16765 C  CD1   . PHE   D 2 213 ? 109.146 146.071 104.798 1.00 79.94  ?  212  PHE   D CD1   1 
ATOM   16766 C  CD2   . PHE   D 2 213 ? 111.480 145.639 104.620 1.00 78.73  ?  212  PHE   D CD2   1 
ATOM   16767 C  CE1   . PHE   D 2 213 ? 108.873 144.773 104.431 1.00 81.05  ?  212  PHE   D CE1   1 
ATOM   16768 C  CE2   . PHE   D 2 213 ? 111.213 144.341 104.246 1.00 80.11  ?  212  PHE   D CE2   1 
ATOM   16769 C  CZ    . PHE   D 2 213 ? 109.910 143.904 104.161 1.00 82.56  ?  212  PHE   D CZ    1 
ATOM   16770 N  N     . ALA   D 2 214 ? 110.563 151.088 105.273 1.00 86.71  ?  213  ALA   D N     1 
ATOM   16771 C  CA    . ALA   D 2 214 ? 110.853 152.385 105.872 1.00 83.72  ?  213  ALA   D CA    1 
ATOM   16772 C  C     . ALA   D 2 214 ? 109.579 153.188 106.083 1.00 83.25  ?  213  ALA   D C     1 
ATOM   16773 O  O     . ALA   D 2 214 ? 109.389 153.802 107.141 1.00 89.29  ?  213  ALA   D O     1 
ATOM   16774 C  CB    . ALA   D 2 214 ? 111.837 153.162 104.995 1.00 83.03  ?  213  ALA   D CB    1 
ATOM   16775 N  N     . CYS   D 2 215 ? 108.686 153.188 105.088 1.00 89.60  ?  214  CYS   D N     1 
ATOM   16776 C  CA    . CYS   D 2 215 ? 107.417 153.898 105.254 1.00 90.41  ?  214  CYS   D CA    1 
ATOM   16777 C  C     . CYS   D 2 215 ? 106.602 153.314 106.404 1.00 91.46  ?  214  CYS   D C     1 
ATOM   16778 O  O     . CYS   D 2 215 ? 105.996 154.056 107.185 1.00 92.49  ?  214  CYS   D O     1 
ATOM   16779 C  CB    . CYS   D 2 215 ? 106.593 153.874 103.965 1.00 92.37  ?  214  CYS   D CB    1 
ATOM   16780 S  SG    . CYS   D 2 215 ? 107.517 153.966 102.422 1.00 108.00 ?  214  CYS   D SG    1 
ATOM   16781 N  N     . SER   D 2 216 ? 106.567 151.986 106.525 1.00 97.60  ?  215  SER   D N     1 
ATOM   16782 C  CA    . SER   D 2 216 ? 105.794 151.370 107.601 1.00 96.81  ?  215  SER   D CA    1 
ATOM   16783 C  C     . SER   D 2 216 ? 106.420 151.634 108.967 1.00 95.91  ?  215  SER   D C     1 
ATOM   16784 O  O     . SER   D 2 216 ? 105.705 151.835 109.956 1.00 96.04  ?  215  SER   D O     1 
ATOM   16785 C  CB    . SER   D 2 216 ? 105.659 149.869 107.355 1.00 97.26  ?  215  SER   D CB    1 
ATOM   16786 O  OG    . SER   D 2 216 ? 104.707 149.290 108.231 1.00 99.20  ?  215  SER   D OG    1 
ATOM   16787 N  N     . PHE   D 2 217 ? 107.750 151.637 109.043 1.00 91.88  ?  216  PHE   D N     1 
ATOM   16788 C  CA    . PHE   D 2 217 ? 108.442 151.819 110.310 1.00 88.40  ?  216  PHE   D CA    1 
ATOM   16789 C  C     . PHE   D 2 217 ? 108.436 153.267 110.776 1.00 92.56  ?  216  PHE   D C     1 
ATOM   16790 O  O     . PHE   D 2 217 ? 108.551 153.523 111.982 1.00 92.52  ?  216  PHE   D O     1 
ATOM   16791 C  CB    . PHE   D 2 217 ? 109.877 151.308 110.184 1.00 84.19  ?  216  PHE   D CB    1 
ATOM   16792 C  CG    . PHE   D 2 217 ? 109.980 149.814 110.086 1.00 87.46  ?  216  PHE   D CG    1 
ATOM   16793 C  CD1   . PHE   D 2 217 ? 109.041 149.005 110.700 1.00 88.51  ?  216  PHE   D CD1   1 
ATOM   16794 C  CD2   . PHE   D 2 217 ? 111.052 149.218 109.445 1.00 90.86  ?  216  PHE   D CD2   1 
ATOM   16795 C  CE1   . PHE   D 2 217 ? 109.138 147.632 110.631 1.00 89.52  ?  216  PHE   D CE1   1 
ATOM   16796 C  CE2   . PHE   D 2 217 ? 111.150 147.844 109.363 1.00 89.44  ?  216  PHE   D CE2   1 
ATOM   16797 C  CZ    . PHE   D 2 217 ? 110.200 147.051 109.964 1.00 89.02  ?  216  PHE   D CZ    1 
ATOM   16798 N  N     . ALA   D 2 218 ? 108.297 154.214 109.847 1.00 93.12  ?  217  ALA   D N     1 
ATOM   16799 C  CA    . ALA   D 2 218 ? 108.240 155.615 110.237 1.00 90.20  ?  217  ALA   D CA    1 
ATOM   16800 C  C     . ALA   D 2 218 ? 106.991 155.893 111.053 1.00 92.01  ?  217  ALA   D C     1 
ATOM   16801 O  O     . ALA   D 2 218 ? 107.014 156.730 111.961 1.00 95.85  ?  217  ALA   D O     1 
ATOM   16802 C  CB    . ALA   D 2 218 ? 108.292 156.512 108.999 1.00 91.18  ?  217  ALA   D CB    1 
ATOM   16803 N  N     . PHE   D 2 219 ? 105.897 155.188 110.751 1.00 93.44  ?  218  PHE   D N     1 
ATOM   16804 C  CA    . PHE   D 2 219 ? 104.710 155.255 111.596 1.00 93.92  ?  218  PHE   D CA    1 
ATOM   16805 C  C     . PHE   D 2 219 ? 104.986 154.673 112.976 1.00 94.11  ?  218  PHE   D C     1 
ATOM   16806 O  O     . PHE   D 2 219 ? 104.506 155.199 113.986 1.00 98.41  ?  218  PHE   D O     1 
ATOM   16807 C  CB    . PHE   D 2 219 ? 103.544 154.517 110.935 1.00 94.48  ?  218  PHE   D CB    1 
ATOM   16808 C  CG    . PHE   D 2 219 ? 102.742 155.366 109.993 1.00 94.66  ?  218  PHE   D CG    1 
ATOM   16809 C  CD1   . PHE   D 2 219 ? 102.108 156.511 110.440 1.00 96.87  ?  218  PHE   D CD1   1 
ATOM   16810 C  CD2   . PHE   D 2 219 ? 102.613 155.013 108.662 1.00 92.82  ?  218  PHE   D CD2   1 
ATOM   16811 C  CE1   . PHE   D 2 219 ? 101.368 157.293 109.578 1.00 97.42  ?  218  PHE   D CE1   1 
ATOM   16812 C  CE2   . PHE   D 2 219 ? 101.878 155.793 107.793 1.00 94.05  ?  218  PHE   D CE2   1 
ATOM   16813 C  CZ    . PHE   D 2 219 ? 101.257 156.937 108.252 1.00 96.53  ?  218  PHE   D CZ    1 
ATOM   16814 N  N     . ALA   D 2 220 ? 105.747 153.578 113.037 1.00 95.96  ?  219  ALA   D N     1 
ATOM   16815 C  CA    . ALA   D 2 220 ? 106.103 152.985 114.322 1.00 95.40  ?  219  ALA   D CA    1 
ATOM   16816 C  C     . ALA   D 2 220 ? 106.914 153.945 115.186 1.00 97.69  ?  219  ALA   D C     1 
ATOM   16817 O  O     . ALA   D 2 220 ? 106.709 154.015 116.403 1.00 97.54  ?  219  ALA   D O     1 
ATOM   16818 C  CB    . ALA   D 2 220 ? 106.881 151.695 114.099 1.00 99.40  ?  219  ALA   D CB    1 
ATOM   16819 N  N     . GLU   D 2 221 ? 107.854 154.675 114.582 1.00 111.41 ?  220  GLU   D N     1 
ATOM   16820 C  CA    . GLU   D 2 221 ? 108.631 155.646 115.343 1.00 108.56 ?  220  GLU   D CA    1 
ATOM   16821 C  C     . GLU   D 2 221 ? 107.755 156.750 115.919 1.00 107.41 ?  220  GLU   D C     1 
ATOM   16822 O  O     . GLU   D 2 221 ? 108.172 157.432 116.861 1.00 109.45 ?  220  GLU   D O     1 
ATOM   16823 C  CB    . GLU   D 2 221 ? 109.731 156.242 114.466 1.00 107.35 ?  220  GLU   D CB    1 
ATOM   16824 C  CG    . GLU   D 2 221 ? 110.941 155.339 114.327 1.00 109.87 ?  220  GLU   D CG    1 
ATOM   16825 C  CD    . GLU   D 2 221 ? 111.611 155.054 115.653 1.00 113.66 ?  220  GLU   D CD    1 
ATOM   16826 O  OE1   . GLU   D 2 221 ? 111.733 155.987 116.474 1.00 113.38 ?  220  GLU   D OE1   1 
ATOM   16827 O  OE2   . GLU   D 2 221 ? 112.012 153.894 115.876 1.00 113.60 ?  220  GLU   D OE2   1 
ATOM   16828 N  N     . ARG   D 2 222 ? 106.555 156.937 115.379 1.00 108.64 ?  221  ARG   D N     1 
ATOM   16829 C  CA    . ARG   D 2 222 ? 105.578 157.871 115.917 1.00 107.59 ?  221  ARG   D CA    1 
ATOM   16830 C  C     . ARG   D 2 222 ? 104.604 157.203 116.883 1.00 109.79 ?  221  ARG   D C     1 
ATOM   16831 O  O     . ARG   D 2 222 ? 103.603 157.821 117.259 1.00 111.71 ?  221  ARG   D O     1 
ATOM   16832 C  CB    . ARG   D 2 222 ? 104.808 158.537 114.773 1.00 108.72 ?  221  ARG   D CB    1 
ATOM   16833 C  CG    . ARG   D 2 222 ? 105.647 159.457 113.879 1.00 108.48 ?  221  ARG   D CG    1 
ATOM   16834 C  CD    . ARG   D 2 222 ? 105.194 160.898 114.046 1.00 110.54 ?  221  ARG   D CD    1 
ATOM   16835 N  NE    . ARG   D 2 222 ? 103.751 161.026 113.882 1.00 113.12 ?  221  ARG   D NE    1 
ATOM   16836 C  CZ    . ARG   D 2 222 ? 103.140 161.031 112.706 1.00 113.13 ?  221  ARG   D CZ    1 
ATOM   16837 N  NH1   . ARG   D 2 222 ? 103.816 160.912 111.577 1.00 113.96 ?  221  ARG   D NH1   1 
ATOM   16838 N  NH2   . ARG   D 2 222 ? 101.817 161.157 112.661 1.00 109.43 ?  221  ARG   D NH2   1 
ATOM   16839 N  N     . GLU   D 2 223 ? 104.879 155.960 117.288 1.00 111.72 ?  222  GLU   D N     1 
ATOM   16840 C  CA    . GLU   D 2 223 ? 104.001 155.188 118.172 1.00 112.67 ?  222  GLU   D CA    1 
ATOM   16841 C  C     . GLU   D 2 223 ? 102.601 155.044 117.579 1.00 114.83 ?  222  GLU   D C     1 
ATOM   16842 O  O     . GLU   D 2 223 ? 101.596 155.149 118.281 1.00 116.14 ?  222  GLU   D O     1 
ATOM   16843 C  CB    . GLU   D 2 223 ? 103.942 155.794 119.578 1.00 113.64 ?  222  GLU   D CB    1 
ATOM   16844 C  CG    . GLU   D 2 223 ? 104.991 155.222 120.513 1.00 113.67 ?  222  GLU   D CG    1 
ATOM   16845 C  CD    . GLU   D 2 223 ? 104.846 155.753 121.928 1.00 117.06 ?  222  GLU   D CD    1 
ATOM   16846 O  OE1   . GLU   D 2 223 ? 104.575 156.964 122.083 1.00 116.67 ?  222  GLU   D OE1   1 
ATOM   16847 O  OE2   . GLU   D 2 223 ? 104.991 154.966 122.888 1.00 116.65 ?  222  GLU   D OE2   1 
ATOM   16848 N  N     . LEU   D 2 224 ? 102.535 154.800 116.272 1.00 108.17 ?  223  LEU   D N     1 
ATOM   16849 C  CA    . LEU   D 2 224 ? 101.278 154.578 115.574 1.00 104.58 ?  223  LEU   D CA    1 
ATOM   16850 C  C     . LEU   D 2 224 ? 101.371 153.288 114.773 1.00 104.74 ?  223  LEU   D C     1 
ATOM   16851 O  O     . LEU   D 2 224 ? 102.432 152.959 114.234 1.00 108.66 ?  223  LEU   D O     1 
ATOM   16852 C  CB    . LEU   D 2 224 ? 100.936 155.746 114.640 1.00 103.94 ?  223  LEU   D CB    1 
ATOM   16853 C  CG    . LEU   D 2 224 ? 100.832 157.132 115.275 1.00 104.64 ?  223  LEU   D CG    1 
ATOM   16854 C  CD1   . LEU   D 2 224 ? 100.997 158.213 114.220 1.00 104.58 ?  223  LEU   D CD1   1 
ATOM   16855 C  CD2   . LEU   D 2 224 ? 99.507  157.286 116.001 1.00 102.90 ?  223  LEU   D CD2   1 
ATOM   16856 N  N     . MET   D 2 225 ? 100.251 152.573 114.688 1.00 99.69  ?  224  MET   D N     1 
ATOM   16857 C  CA    . MET   D 2 225 ? 100.164 151.292 113.986 1.00 99.69  ?  224  MET   D CA    1 
ATOM   16858 C  C     . MET   D 2 225 ? 101.271 150.342 114.447 1.00 101.09 ?  224  MET   D C     1 
ATOM   16859 O  O     . MET   D 2 225 ? 102.142 149.929 113.679 1.00 103.88 ?  224  MET   D O     1 
ATOM   16860 C  CB    . MET   D 2 225 ? 100.203 151.489 112.466 1.00 100.32 ?  224  MET   D CB    1 
ATOM   16861 C  CG    . MET   D 2 225 ? 99.737  152.855 111.979 1.00 99.10  ?  224  MET   D CG    1 
ATOM   16862 S  SD    . MET   D 2 225 ? 97.951  153.065 112.055 1.00 114.64 ?  224  MET   D SD    1 
ATOM   16863 C  CE    . MET   D 2 225 ? 97.401  151.596 111.196 1.00 102.26 ?  224  MET   D CE    1 
ATOM   16864 N  N     . GLU   D 2 226 ? 101.224 150.005 115.738 1.00 101.05 ?  225  GLU   D N     1 
ATOM   16865 C  CA    . GLU   D 2 226 ? 102.291 149.207 116.333 1.00 100.92 ?  225  GLU   D CA    1 
ATOM   16866 C  C     . GLU   D 2 226 ? 102.202 147.742 115.915 1.00 102.92 ?  225  GLU   D C     1 
ATOM   16867 O  O     . GLU   D 2 226 ? 103.231 147.087 115.719 1.00 104.99 ?  225  GLU   D O     1 
ATOM   16868 C  CB    . GLU   D 2 226 ? 102.258 149.343 117.854 1.00 103.55 ?  225  GLU   D CB    1 
ATOM   16869 C  CG    . GLU   D 2 226 ? 102.979 150.582 118.373 1.00 103.84 ?  225  GLU   D CG    1 
ATOM   16870 C  CD    . GLU   D 2 226 ? 103.769 150.306 119.637 1.00 109.03 ?  225  GLU   D CD    1 
ATOM   16871 O  OE1   . GLU   D 2 226 ? 103.196 150.445 120.737 1.00 108.50 ?  225  GLU   D OE1   1 
ATOM   16872 O  OE2   . GLU   D 2 226 ? 104.962 149.950 119.531 1.00 108.78 ?  225  GLU   D OE2   1 
ATOM   16873 N  N     . GLY   D 2 227 ? 100.987 147.206 115.785 1.00 91.21  ?  226  GLY   D N     1 
ATOM   16874 C  CA    . GLY   D 2 227 ? 100.844 145.835 115.316 1.00 90.61  ?  226  GLY   D CA    1 
ATOM   16875 C  C     . GLY   D 2 227 ? 101.298 145.662 113.879 1.00 90.90  ?  226  GLY   D C     1 
ATOM   16876 O  O     . GLY   D 2 227 ? 101.913 144.648 113.526 1.00 97.07  ?  226  GLY   D O     1 
ATOM   16877 N  N     . ASN   D 2 228 ? 101.001 146.649 113.030 1.00 76.35  ?  227  ASN   D N     1 
ATOM   16878 C  CA    . ASN   D 2 228 ? 101.500 146.623 111.660 1.00 78.56  ?  227  ASN   D CA    1 
ATOM   16879 C  C     . ASN   D 2 228 ? 103.022 146.593 111.638 1.00 81.80  ?  227  ASN   D C     1 
ATOM   16880 O  O     . ASN   D 2 228 ? 103.626 145.844 110.862 1.00 87.37  ?  227  ASN   D O     1 
ATOM   16881 C  CB    . ASN   D 2 228 ? 100.975 147.834 110.890 1.00 79.92  ?  227  ASN   D CB    1 
ATOM   16882 C  CG    . ASN   D 2 228 ? 101.832 148.176 109.688 1.00 82.04  ?  227  ASN   D CG    1 
ATOM   16883 O  OD1   . ASN   D 2 228 ? 101.999 147.365 108.776 1.00 82.56  ?  227  ASN   D OD1   1 
ATOM   16884 N  ND2   . ASN   D 2 228 ? 102.388 149.381 109.683 1.00 81.32  ?  227  ASN   D ND2   1 
ATOM   16885 N  N     . ALA   D 2 229 ? 103.656 147.395 112.494 1.00 72.84  ?  228  ALA   D N     1 
ATOM   16886 C  CA    . ALA   D 2 229 ? 105.111 147.398 112.587 1.00 70.06  ?  228  ALA   D CA    1 
ATOM   16887 C  C     . ALA   D 2 229 ? 105.635 146.061 113.087 1.00 77.57  ?  228  ALA   D C     1 
ATOM   16888 O  O     . ALA   D 2 229 ? 106.668 145.576 112.616 1.00 85.99  ?  228  ALA   D O     1 
ATOM   16889 C  CB    . ALA   D 2 229 ? 105.574 148.527 113.504 1.00 73.12  ?  228  ALA   D CB    1 
ATOM   16890 N  N     . LYS   D 2 230 ? 104.932 145.451 114.042 1.00 71.11  ?  229  LYS   D N     1 
ATOM   16891 C  CA    . LYS   D 2 230 ? 105.350 144.150 114.553 1.00 70.68  ?  229  LYS   D CA    1 
ATOM   16892 C  C     . LYS   D 2 230 ? 105.318 143.093 113.458 1.00 71.22  ?  229  LYS   D C     1 
ATOM   16893 O  O     . LYS   D 2 230 ? 106.214 142.245 113.378 1.00 74.86  ?  229  LYS   D O     1 
ATOM   16894 C  CB    . LYS   D 2 230 ? 104.461 143.736 115.725 1.00 71.12  ?  229  LYS   D CB    1 
ATOM   16895 C  CG    . LYS   D 2 230 ? 105.064 144.011 117.089 1.00 71.77  ?  229  LYS   D CG    1 
ATOM   16896 C  CD    . LYS   D 2 230 ? 104.001 143.997 118.174 1.00 74.99  ?  229  LYS   D CD    1 
ATOM   16897 C  CE    . LYS   D 2 230 ? 104.159 145.179 119.114 1.00 77.34  ?  229  LYS   D CE    1 
ATOM   16898 N  NZ    . LYS   D 2 230 ? 103.958 144.789 120.534 1.00 78.28  ?  229  LYS   D NZ    1 
ATOM   16899 N  N     . ILE   D 2 231 ? 104.287 143.123 112.612 1.00 63.10  ?  230  ILE   D N     1 
ATOM   16900 C  CA    . ILE   D 2 231 ? 104.216 142.179 111.497 1.00 60.35  ?  230  ILE   D CA    1 
ATOM   16901 C  C     . ILE   D 2 231 ? 105.299 142.481 110.464 1.00 64.18  ?  230  ILE   D C     1 
ATOM   16902 O  O     . ILE   D 2 231 ? 105.971 141.569 109.954 1.00 75.39  ?  230  ILE   D O     1 
ATOM   16903 C  CB    . ILE   D 2 231 ? 102.809 142.202 110.874 1.00 57.54  ?  230  ILE   D CB    1 
ATOM   16904 C  CG1   . ILE   D 2 231 ? 101.818 141.467 111.779 1.00 60.54  ?  230  ILE   D CG1   1 
ATOM   16905 C  CG2   . ILE   D 2 231 ? 102.824 141.581 109.487 1.00 58.09  ?  230  ILE   D CG2   1 
ATOM   16906 C  CD1   . ILE   D 2 231 ? 100.380 141.591 111.340 1.00 65.56  ?  230  ILE   D CD1   1 
ATOM   16907 N  N     . ILE   D 2 232 ? 105.492 143.762 110.145 1.00 59.47  ?  231  ILE   D N     1 
ATOM   16908 C  CA    . ILE   D 2 232 ? 106.462 144.147 109.129 1.00 59.72  ?  231  ILE   D CA    1 
ATOM   16909 C  C     . ILE   D 2 232 ? 107.882 143.819 109.572 1.00 64.09  ?  231  ILE   D C     1 
ATOM   16910 O  O     . ILE   D 2 232 ? 108.750 143.567 108.735 1.00 72.59  ?  231  ILE   D O     1 
ATOM   16911 C  CB    . ILE   D 2 232 ? 106.288 145.639 108.781 1.00 60.38  ?  231  ILE   D CB    1 
ATOM   16912 C  CG1   . ILE   D 2 232 ? 104.948 145.870 108.083 1.00 62.64  ?  231  ILE   D CG1   1 
ATOM   16913 C  CG2   . ILE   D 2 232 ? 107.412 146.140 107.888 1.00 65.65  ?  231  ILE   D CG2   1 
ATOM   16914 C  CD1   . ILE   D 2 232 ? 104.880 145.309 106.684 1.00 66.27  ?  231  ILE   D CD1   1 
ATOM   16915 N  N     . ARG   D 2 233 ? 108.144 143.791 110.880 1.00 61.94  ?  232  ARG   D N     1 
ATOM   16916 C  CA    . ARG   D 2 233 ? 109.466 143.404 111.366 1.00 62.93  ?  232  ARG   D CA    1 
ATOM   16917 C  C     . ARG   D 2 233 ? 109.790 141.958 110.999 1.00 71.57  ?  232  ARG   D C     1 
ATOM   16918 O  O     . ARG   D 2 233 ? 110.879 141.658 110.490 1.00 79.13  ?  232  ARG   D O     1 
ATOM   16919 C  CB    . ARG   D 2 233 ? 109.534 143.614 112.878 1.00 67.89  ?  232  ARG   D CB    1 
ATOM   16920 C  CG    . ARG   D 2 233 ? 110.911 143.439 113.479 1.00 75.20  ?  232  ARG   D CG    1 
ATOM   16921 C  CD    . ARG   D 2 233 ? 110.817 143.246 114.983 1.00 75.68  ?  232  ARG   D CD    1 
ATOM   16922 N  NE    . ARG   D 2 233 ? 110.968 144.509 115.695 1.00 80.46  ?  232  ARG   D NE    1 
ATOM   16923 C  CZ    . ARG   D 2 233 ? 112.122 144.996 116.130 1.00 83.23  ?  232  ARG   D CZ    1 
ATOM   16924 N  NH1   . ARG   D 2 233 ? 113.261 144.352 115.940 1.00 80.41  ?  232  ARG   D NH1   1 
ATOM   16925 N  NH2   . ARG   D 2 233 ? 112.132 146.161 116.773 1.00 79.82  ?  232  ARG   D NH2   1 
ATOM   16926 N  N     . LEU   D 2 234 ? 108.848 141.045 111.245 1.00 61.20  ?  233  LEU   D N     1 
ATOM   16927 C  CA    . LEU   D 2 234 ? 109.047 139.650 110.864 1.00 56.44  ?  233  LEU   D CA    1 
ATOM   16928 C  C     . LEU   D 2 234 ? 109.133 139.500 109.350 1.00 58.85  ?  233  LEU   D C     1 
ATOM   16929 O  O     . LEU   D 2 234 ? 109.942 138.711 108.835 1.00 68.24  ?  233  LEU   D O     1 
ATOM   16930 C  CB    . LEU   D 2 234 ? 107.917 138.791 111.429 1.00 52.46  ?  233  LEU   D CB    1 
ATOM   16931 C  CG    . LEU   D 2 234 ? 107.631 138.961 112.923 1.00 55.03  ?  233  LEU   D CG    1 
ATOM   16932 C  CD1   . LEU   D 2 234 ? 106.274 138.383 113.284 1.00 55.77  ?  233  LEU   D CD1   1 
ATOM   16933 C  CD2   . LEU   D 2 234 ? 108.727 138.317 113.755 1.00 60.88  ?  233  LEU   D CD2   1 
ATOM   16934 N  N     . ILE   D 2 235 ? 108.302 140.250 108.621 1.00 51.06  ?  234  ILE   D N     1 
ATOM   16935 C  CA    . ILE   D 2 235 ? 108.376 140.222 107.163 1.00 50.14  ?  234  ILE   D CA    1 
ATOM   16936 C  C     . ILE   D 2 235 ? 109.755 140.667 106.692 1.00 56.20  ?  234  ILE   D C     1 
ATOM   16937 O  O     . ILE   D 2 235 ? 110.320 140.094 105.756 1.00 66.03  ?  234  ILE   D O     1 
ATOM   16938 C  CB    . ILE   D 2 235 ? 107.260 141.087 106.550 1.00 50.11  ?  234  ILE   D CB    1 
ATOM   16939 C  CG1   . ILE   D 2 235 ? 105.892 140.468 106.829 1.00 51.31  ?  234  ILE   D CG1   1 
ATOM   16940 C  CG2   . ILE   D 2 235 ? 107.463 141.244 105.052 1.00 49.15  ?  234  ILE   D CG2   1 
ATOM   16941 C  CD1   . ILE   D 2 235 ? 104.747 141.245 106.232 1.00 51.12  ?  234  ILE   D CD1   1 
ATOM   16942 N  N     . ALA   D 2 236 ? 110.324 141.684 107.343 1.00 57.83  ?  235  ALA   D N     1 
ATOM   16943 C  CA    . ALA   D 2 236 ? 111.646 142.176 106.972 1.00 58.07  ?  235  ALA   D CA    1 
ATOM   16944 C  C     . ALA   D 2 236 ? 112.729 141.154 107.286 1.00 57.94  ?  235  ALA   D C     1 
ATOM   16945 O  O     . ALA   D 2 236 ? 113.701 141.023 106.535 1.00 67.33  ?  235  ALA   D O     1 
ATOM   16946 C  CB    . ALA   D 2 236 ? 111.931 143.496 107.687 1.00 57.80  ?  235  ALA   D CB    1 
ATOM   16947 N  N     . ARG   D 2 237 ? 112.590 140.436 108.401 1.00 49.12  ?  236  ARG   D N     1 
ATOM   16948 C  CA    . ARG   D 2 237 ? 113.529 139.357 108.701 1.00 52.79  ?  236  ARG   D CA    1 
ATOM   16949 C  C     . ARG   D 2 237 ? 113.517 138.303 107.597 1.00 58.90  ?  236  ARG   D C     1 
ATOM   16950 O  O     . ARG   D 2 237 ? 114.572 137.899 107.078 1.00 69.03  ?  236  ARG   D O     1 
ATOM   16951 C  CB    . ARG   D 2 237 ? 113.178 138.732 110.052 1.00 54.24  ?  236  ARG   D CB    1 
ATOM   16952 C  CG    . ARG   D 2 237 ? 114.316 137.982 110.717 1.00 60.38  ?  236  ARG   D CG    1 
ATOM   16953 C  CD    . ARG   D 2 237 ? 113.917 137.505 112.102 1.00 62.09  ?  236  ARG   D CD    1 
ATOM   16954 N  NE    . ARG   D 2 237 ? 112.627 136.825 112.091 1.00 63.43  ?  236  ARG   D NE    1 
ATOM   16955 C  CZ    . ARG   D 2 237 ? 112.063 136.270 113.155 1.00 63.04  ?  236  ARG   D CZ    1 
ATOM   16956 N  NH1   . ARG   D 2 237 ? 112.648 136.299 114.341 1.00 59.06  ?  236  ARG   D NH1   1 
ATOM   16957 N  NH2   . ARG   D 2 237 ? 110.883 135.671 113.025 1.00 62.58  ?  236  ARG   D NH2   1 
ATOM   16958 N  N     . ASP   D 2 238 ? 112.319 137.862 107.207 1.00 63.62  ?  237  ASP   D N     1 
ATOM   16959 C  CA    . ASP   D 2 238 ? 112.218 136.882 106.129 1.00 58.74  ?  237  ASP   D CA    1 
ATOM   16960 C  C     . ASP   D 2 238 ? 112.752 137.449 104.821 1.00 62.89  ?  237  ASP   D C     1 
ATOM   16961 O  O     . ASP   D 2 238 ? 113.350 136.723 104.016 1.00 73.53  ?  237  ASP   D O     1 
ATOM   16962 C  CB    . ASP   D 2 238 ? 110.773 136.427 105.959 1.00 60.66  ?  237  ASP   D CB    1 
ATOM   16963 C  CG    . ASP   D 2 238 ? 110.270 135.629 107.139 1.00 71.94  ?  237  ASP   D CG    1 
ATOM   16964 O  OD1   . ASP   D 2 238 ? 111.003 135.521 108.142 1.00 81.53  ?  237  ASP   D OD1   1 
ATOM   16965 O  OD2   . ASP   D 2 238 ? 109.138 135.108 107.065 1.00 72.51  ?  237  ASP   D OD2   1 
ATOM   16966 N  N     . GLU   D 2 239 ? 112.524 138.741 104.580 1.00 62.07  ?  238  GLU   D N     1 
ATOM   16967 C  CA    . GLU   D 2 239 ? 113.044 139.366 103.374 1.00 59.59  ?  238  GLU   D CA    1 
ATOM   16968 C  C     . GLU   D 2 239 ? 114.552 139.285 103.347 1.00 66.95  ?  238  GLU   D C     1 
ATOM   16969 O  O     . GLU   D 2 239 ? 115.142 138.916 102.332 1.00 70.71  ?  238  GLU   D O     1 
ATOM   16970 C  CB    . GLU   D 2 239 ? 112.612 140.826 103.285 1.00 64.73  ?  238  GLU   D CB    1 
ATOM   16971 C  CG    . GLU   D 2 239 ? 112.349 141.266 101.875 1.00 73.03  ?  238  GLU   D CG    1 
ATOM   16972 C  CD    . GLU   D 2 239 ? 111.153 140.553 101.299 1.00 78.08  ?  238  GLU   D CD    1 
ATOM   16973 O  OE1   . GLU   D 2 239 ? 110.135 140.386 102.004 1.00 78.96  ?  238  GLU   D OE1   1 
ATOM   16974 O  OE2   . GLU   D 2 239 ? 111.223 140.152 100.130 1.00 84.24  ?  238  GLU   D OE2   1 
ATOM   16975 N  N     . ALA   D 2 240 ? 115.188 139.661 104.455 1.00 62.04  ?  239  ALA   D N     1 
ATOM   16976 C  CA    . ALA   D 2 240 ? 116.637 139.577 104.549 1.00 52.22  ?  239  ALA   D CA    1 
ATOM   16977 C  C     . ALA   D 2 240 ? 117.116 138.167 104.247 1.00 57.21  ?  239  ALA   D C     1 
ATOM   16978 O  O     . ALA   D 2 240 ? 118.113 137.979 103.539 1.00 69.69  ?  239  ALA   D O     1 
ATOM   16979 C  CB    . ALA   D 2 240 ? 117.095 140.024 105.935 1.00 51.61  ?  239  ALA   D CB    1 
ATOM   16980 N  N     . LEU   D 2 241 ? 116.400 137.162 104.751 1.00 57.00  ?  240  LEU   D N     1 
ATOM   16981 C  CA    . LEU   D 2 241 ? 116.766 135.779 104.452 1.00 51.61  ?  240  LEU   D CA    1 
ATOM   16982 C  C     . LEU   D 2 241 ? 116.684 135.486 102.953 1.00 58.85  ?  240  LEU   D C     1 
ATOM   16983 O  O     . LEU   D 2 241 ? 117.624 134.936 102.361 1.00 66.12  ?  240  LEU   D O     1 
ATOM   16984 C  CB    . LEU   D 2 241 ? 115.871 134.836 105.248 1.00 52.98  ?  240  LEU   D CB    1 
ATOM   16985 C  CG    . LEU   D 2 241 ? 116.545 133.694 106.001 1.00 58.96  ?  240  LEU   D CG    1 
ATOM   16986 C  CD1   . LEU   D 2 241 ? 117.682 134.219 106.853 1.00 57.76  ?  240  LEU   D CD1   1 
ATOM   16987 C  CD2   . LEU   D 2 241 ? 115.526 132.972 106.859 1.00 60.87  ?  240  LEU   D CD2   1 
ATOM   16988 N  N     . HIS   D 2 242 ? 115.579 135.888 102.314 1.00 56.19  ?  241  HIS   D N     1 
ATOM   16989 C  CA    . HIS   D 2 242 ? 115.411 135.650 100.882 1.00 50.97  ?  241  HIS   D CA    1 
ATOM   16990 C  C     . HIS   D 2 242 ? 116.468 136.390 100.072 1.00 57.29  ?  241  HIS   D C     1 
ATOM   16991 O  O     . HIS   D 2 242 ? 116.971 135.876 99.064  1.00 70.12  ?  241  HIS   D O     1 
ATOM   16992 C  CB    . HIS   D 2 242 ? 114.019 136.085 100.425 1.00 49.25  ?  241  HIS   D CB    1 
ATOM   16993 C  CG    . HIS   D 2 242 ? 112.896 135.513 101.233 1.00 53.80  ?  241  HIS   D CG    1 
ATOM   16994 N  ND1   . HIS   D 2 242 ? 111.813 136.272 101.616 1.00 58.51  ?  241  HIS   D ND1   1 
ATOM   16995 C  CD2   . HIS   D 2 242 ? 112.718 134.294 101.794 1.00 55.34  ?  241  HIS   D CD2   1 
ATOM   16996 C  CE1   . HIS   D 2 242 ? 110.988 135.531 102.330 1.00 58.48  ?  241  HIS   D CE1   1 
ATOM   16997 N  NE2   . HIS   D 2 242 ? 111.516 134.327 102.459 1.00 53.53  ?  241  HIS   D NE2   1 
ATOM   16998 N  N     . LEU   D 2 243 ? 116.788 137.616 100.480 1.00 62.12  ?  242  LEU   D N     1 
ATOM   16999 C  CA    . LEU   D 2 243 ? 117.801 138.398 99.788  1.00 61.73  ?  242  LEU   D CA    1 
ATOM   17000 C  C     . LEU   D 2 243 ? 119.164 137.736 99.893  1.00 62.83  ?  242  LEU   D C     1 
ATOM   17001 O  O     . LEU   D 2 243 ? 119.914 137.698 98.914  1.00 67.42  ?  242  LEU   D O     1 
ATOM   17002 C  CB    . LEU   D 2 243 ? 117.844 139.818 100.346 1.00 59.29  ?  242  LEU   D CB    1 
ATOM   17003 C  CG    . LEU   D 2 243 ? 118.920 140.724 99.750  1.00 62.73  ?  242  LEU   D CG    1 
ATOM   17004 C  CD1   . LEU   D 2 243 ? 118.678 140.933 98.269  1.00 70.18  ?  242  LEU   D CD1   1 
ATOM   17005 C  CD2   . LEU   D 2 243 ? 118.955 142.042 100.485 1.00 67.07  ?  242  LEU   D CD2   1 
ATOM   17006 N  N     . THR   D 2 244 ? 119.500 137.203 101.071 1.00 62.12  ?  243  THR   D N     1 
ATOM   17007 C  CA    . THR   D 2 244 ? 120.744 136.454 101.205 1.00 52.32  ?  243  THR   D CA    1 
ATOM   17008 C  C     . THR   D 2 244 ? 120.754 135.260 100.263 1.00 61.47  ?  243  THR   D C     1 
ATOM   17009 O  O     . THR   D 2 244 ? 121.763 134.987 99.599  1.00 72.55  ?  243  THR   D O     1 
ATOM   17010 C  CB    . THR   D 2 244 ? 120.934 135.998 102.652 1.00 50.93  ?  243  THR   D CB    1 
ATOM   17011 O  OG1   . THR   D 2 244 ? 121.080 137.142 103.503 1.00 63.69  ?  243  THR   D OG1   1 
ATOM   17012 C  CG2   . THR   D 2 244 ? 122.167 135.117 102.770 1.00 58.44  ?  243  THR   D CG2   1 
ATOM   17013 N  N     . GLY   D 2 245 ? 119.629 134.550 100.175 1.00 63.63  ?  244  GLY   D N     1 
ATOM   17014 C  CA    . GLY   D 2 245 ? 119.573 133.390 99.297  1.00 61.69  ?  244  GLY   D CA    1 
ATOM   17015 C  C     . GLY   D 2 245 ? 119.797 133.742 97.838  1.00 63.62  ?  244  GLY   D C     1 
ATOM   17016 O  O     . GLY   D 2 245 ? 120.607 133.115 97.145  1.00 74.21  ?  244  GLY   D O     1 
ATOM   17017 N  N     . THR   D 2 246 ? 119.087 134.759 97.352  1.00 64.57  ?  245  THR   D N     1 
ATOM   17018 C  CA    . THR   D 2 246 ? 119.231 135.116 95.946  1.00 60.39  ?  245  THR   D CA    1 
ATOM   17019 C  C     . THR   D 2 246 ? 120.592 135.746 95.665  1.00 60.73  ?  245  THR   D C     1 
ATOM   17020 O  O     . THR   D 2 246 ? 121.107 135.627 94.547  1.00 67.75  ?  245  THR   D O     1 
ATOM   17021 C  CB    . THR   D 2 246 ? 118.087 136.043 95.509  1.00 62.61  ?  245  THR   D CB    1 
ATOM   17022 O  OG1   . THR   D 2 246 ? 118.192 136.314 94.106  1.00 73.70  ?  245  THR   D OG1   1 
ATOM   17023 C  CG2   . THR   D 2 246 ? 118.100 137.353 96.273  1.00 68.69  ?  245  THR   D CG2   1 
ATOM   17024 N  N     . GLN   D 2 247 ? 121.161 136.464 96.638  1.00 66.18  ?  246  GLN   D N     1 
ATOM   17025 C  CA    . GLN   D 2 247 ? 122.502 137.009 96.472  1.00 63.06  ?  246  GLN   D CA    1 
ATOM   17026 C  C     . GLN   D 2 247 ? 123.521 135.892 96.332  1.00 67.87  ?  246  GLN   D C     1 
ATOM   17027 O  O     . GLN   D 2 247 ? 124.424 135.969 95.494  1.00 74.89  ?  246  GLN   D O     1 
ATOM   17028 C  CB    . GLN   D 2 247 ? 122.857 137.905 97.659  1.00 59.95  ?  246  GLN   D CB    1 
ATOM   17029 C  CG    . GLN   D 2 247 ? 122.999 139.375 97.324  1.00 66.96  ?  246  GLN   D CG    1 
ATOM   17030 C  CD    . GLN   D 2 247 ? 122.955 140.251 98.558  1.00 72.95  ?  246  GLN   D CD    1 
ATOM   17031 O  OE1   . GLN   D 2 247 ? 123.156 139.777 99.676  1.00 74.89  ?  246  GLN   D OE1   1 
ATOM   17032 N  NE2   . GLN   D 2 247 ? 122.685 141.534 98.364  1.00 73.71  ?  246  GLN   D NE2   1 
ATOM   17033 N  N     . HIS   D 2 248 ? 123.392 134.845 97.151  1.00 69.63  ?  247  HIS   D N     1 
ATOM   17034 C  CA    . HIS   D 2 248 ? 124.290 133.703 97.027  1.00 66.83  ?  247  HIS   D CA    1 
ATOM   17035 C  C     . HIS   D 2 248 ? 124.108 133.007 95.686  1.00 68.78  ?  247  HIS   D C     1 
ATOM   17036 O  O     . HIS   D 2 248 ? 125.089 132.595 95.056  1.00 74.08  ?  247  HIS   D O     1 
ATOM   17037 C  CB    . HIS   D 2 248 ? 124.066 132.727 98.180  1.00 70.59  ?  247  HIS   D CB    1 
ATOM   17038 C  CG    . HIS   D 2 248 ? 124.853 133.058 99.408  1.00 72.99  ?  247  HIS   D CG    1 
ATOM   17039 N  ND1   . HIS   D 2 248 ? 126.003 132.385 99.760  1.00 75.68  ?  247  HIS   D ND1   1 
ATOM   17040 C  CD2   . HIS   D 2 248 ? 124.662 134.000 100.362 1.00 71.33  ?  247  HIS   D CD2   1 
ATOM   17041 C  CE1   . HIS   D 2 248 ? 126.482 132.894 100.881 1.00 76.01  ?  247  HIS   D CE1   1 
ATOM   17042 N  NE2   . HIS   D 2 248 ? 125.687 133.875 101.267 1.00 74.08  ?  247  HIS   D NE2   1 
ATOM   17043 N  N     . MET   D 2 249 ? 122.860 132.869 95.232  1.00 77.82  ?  248  MET   D N     1 
ATOM   17044 C  CA    . MET   D 2 249 ? 122.607 132.289 93.915  1.00 76.11  ?  248  MET   D CA    1 
ATOM   17045 C  C     . MET   D 2 249 ? 123.323 133.074 92.821  1.00 77.49  ?  248  MET   D C     1 
ATOM   17046 O  O     . MET   D 2 249 ? 124.064 132.502 92.008  1.00 84.72  ?  248  MET   D O     1 
ATOM   17047 C  CB    . MET   D 2 249 ? 121.104 132.252 93.647  1.00 74.19  ?  248  MET   D CB    1 
ATOM   17048 C  CG    . MET   D 2 249 ? 120.430 130.931 93.928  1.00 79.07  ?  248  MET   D CG    1 
ATOM   17049 S  SD    . MET   D 2 249 ? 118.679 130.985 93.497  1.00 97.00  ?  248  MET   D SD    1 
ATOM   17050 C  CE    . MET   D 2 249 ? 117.933 131.113 95.119  1.00 76.17  ?  248  MET   D CE    1 
ATOM   17051 N  N     . LEU   D 2 250 ? 123.144 134.398 92.816  1.00 67.17  ?  249  LEU   D N     1 
ATOM   17052 C  CA    . LEU   D 2 250 ? 123.764 135.233 91.792  1.00 64.76  ?  249  LEU   D CA    1 
ATOM   17053 C  C     . LEU   D 2 250 ? 125.284 135.185 91.872  1.00 72.34  ?  249  LEU   D C     1 
ATOM   17054 O  O     . LEU   D 2 250 ? 125.960 135.114 90.841  1.00 79.77  ?  249  LEU   D O     1 
ATOM   17055 C  CB    . LEU   D 2 250 ? 123.265 136.669 91.921  1.00 68.61  ?  249  LEU   D CB    1 
ATOM   17056 C  CG    . LEU   D 2 250 ? 121.873 136.955 91.360  1.00 68.66  ?  249  LEU   D CG    1 
ATOM   17057 C  CD1   . LEU   D 2 250 ? 121.410 138.341 91.772  1.00 68.49  ?  249  LEU   D CD1   1 
ATOM   17058 C  CD2   . LEU   D 2 250 ? 121.872 136.812 89.850  1.00 65.89  ?  249  LEU   D CD2   1 
ATOM   17059 N  N     . ASN   D 2 251 ? 125.841 135.223 93.085  1.00 74.55  ?  250  ASN   D N     1 
ATOM   17060 C  CA    . ASN   D 2 251 ? 127.291 135.215 93.232  1.00 72.49  ?  250  ASN   D CA    1 
ATOM   17061 C  C     . ASN   D 2 251 ? 127.891 133.892 92.778  1.00 74.95  ?  250  ASN   D C     1 
ATOM   17062 O  O     . ASN   D 2 251 ? 128.938 133.876 92.122  1.00 79.72  ?  250  ASN   D O     1 
ATOM   17063 C  CB    . ASN   D 2 251 ? 127.670 135.511 94.680  1.00 76.17  ?  250  ASN   D CB    1 
ATOM   17064 C  CG    . ASN   D 2 251 ? 127.690 136.994 94.983  1.00 79.70  ?  250  ASN   D CG    1 
ATOM   17065 O  OD1   . ASN   D 2 251 ? 127.742 137.824 94.077  1.00 80.02  ?  250  ASN   D OD1   1 
ATOM   17066 N  ND2   . ASN   D 2 251 ? 127.649 137.335 96.265  1.00 78.48  ?  250  ASN   D ND2   1 
ATOM   17067 N  N     . LEU   D 2 252 ? 127.238 132.773 93.104  1.00 78.90  ?  251  LEU   D N     1 
ATOM   17068 C  CA    . LEU   D 2 252 ? 127.753 131.477 92.681  1.00 78.56  ?  251  LEU   D CA    1 
ATOM   17069 C  C     . LEU   D 2 252 ? 127.598 131.274 91.182  1.00 78.51  ?  251  LEU   D C     1 
ATOM   17070 O  O     . LEU   D 2 252 ? 128.400 130.559 90.573  1.00 83.56  ?  251  LEU   D O     1 
ATOM   17071 C  CB    . LEU   D 2 252 ? 127.061 130.361 93.459  1.00 74.51  ?  251  LEU   D CB    1 
ATOM   17072 C  CG    . LEU   D 2 252 ? 127.588 130.187 94.885  1.00 79.46  ?  251  LEU   D CG    1 
ATOM   17073 C  CD1   . LEU   D 2 252 ? 126.839 129.098 95.627  1.00 78.43  ?  251  LEU   D CD1   1 
ATOM   17074 C  CD2   . LEU   D 2 252 ? 129.079 129.892 94.868  1.00 81.51  ?  251  LEU   D CD2   1 
ATOM   17075 N  N     . LEU   D 2 253 ? 126.584 131.888 90.567  1.00 78.58  ?  252  LEU   D N     1 
ATOM   17076 C  CA    . LEU   D 2 253 ? 126.490 131.832 89.113  1.00 74.91  ?  252  LEU   D CA    1 
ATOM   17077 C  C     . LEU   D 2 253 ? 127.522 132.730 88.445  1.00 75.67  ?  252  LEU   D C     1 
ATOM   17078 O  O     . LEU   D 2 253 ? 128.017 132.397 87.364  1.00 82.55  ?  252  LEU   D O     1 
ATOM   17079 C  CB    . LEU   D 2 253 ? 125.083 132.208 88.661  1.00 78.59  ?  252  LEU   D CB    1 
ATOM   17080 C  CG    . LEU   D 2 253 ? 123.990 131.171 88.911  1.00 78.53  ?  252  LEU   D CG    1 
ATOM   17081 C  CD1   . LEU   D 2 253 ? 122.615 131.799 88.755  1.00 80.31  ?  252  LEU   D CD1   1 
ATOM   17082 C  CD2   . LEU   D 2 253 ? 124.156 129.988 87.977  1.00 77.22  ?  252  LEU   D CD2   1 
ATOM   17083 N  N     . ARG   D 2 254 ? 127.866 133.858 89.073  1.00 91.02  ?  253  ARG   D N     1 
ATOM   17084 C  CA    . ARG   D 2 254 ? 128.824 134.791 88.492  1.00 91.38  ?  253  ARG   D CA    1 
ATOM   17085 C  C     . ARG   D 2 254 ? 130.257 134.294 88.629  1.00 94.10  ?  253  ARG   D C     1 
ATOM   17086 O  O     . ARG   D 2 254 ? 131.080 134.521 87.736  1.00 95.84  ?  253  ARG   D O     1 
ATOM   17087 C  CB    . ARG   D 2 254 ? 128.675 136.161 89.153  1.00 89.76  ?  253  ARG   D CB    1 
ATOM   17088 C  CG    . ARG   D 2 254 ? 129.170 137.319 88.311  1.00 91.75  ?  253  ARG   D CG    1 
ATOM   17089 C  CD    . ARG   D 2 254 ? 128.903 138.647 88.994  1.00 94.92  ?  253  ARG   D CD    1 
ATOM   17090 N  NE    . ARG   D 2 254 ? 129.002 138.539 90.444  1.00 95.76  ?  253  ARG   D NE    1 
ATOM   17091 C  CZ    . ARG   D 2 254 ? 129.981 139.065 91.168  1.00 95.87  ?  253  ARG   D CZ    1 
ATOM   17092 N  NH1   . ARG   D 2 254 ? 130.967 139.745 90.607  1.00 95.26  ?  253  ARG   D NH1   1 
ATOM   17093 N  NH2   . ARG   D 2 254 ? 129.970 138.904 92.488  1.00 95.15  ?  253  ARG   D NH2   1 
ATOM   17094 N  N     . SER   D 2 255 ? 130.574 133.623 89.739  1.00 95.49  ?  254  SER   D N     1 
ATOM   17095 C  CA    . SER   D 2 255 ? 131.950 133.219 90.004  1.00 91.87  ?  254  SER   D CA    1 
ATOM   17096 C  C     . SER   D 2 255 ? 132.468 132.206 88.993  1.00 93.72  ?  254  SER   D C     1 
ATOM   17097 O  O     . SER   D 2 255 ? 133.685 132.111 88.798  1.00 96.92  ?  254  SER   D O     1 
ATOM   17098 C  CB    . SER   D 2 255 ? 132.066 132.644 91.416  1.00 91.20  ?  254  SER   D CB    1 
ATOM   17099 O  OG    . SER   D 2 255 ? 131.792 131.255 91.424  1.00 93.72  ?  254  SER   D OG    1 
ATOM   17100 N  N     . GLY   D 2 256 ? 131.582 131.451 88.350  1.00 99.65  ?  255  GLY   D N     1 
ATOM   17101 C  CA    . GLY   D 2 256 ? 131.997 130.438 87.406  1.00 99.57  ?  255  GLY   D CA    1 
ATOM   17102 C  C     . GLY   D 2 256 ? 132.426 129.125 88.022  1.00 102.45 ?  255  GLY   D C     1 
ATOM   17103 O  O     . GLY   D 2 256 ? 132.809 128.210 87.281  1.00 102.37 ?  255  GLY   D O     1 
ATOM   17104 N  N     . ALA   D 2 257 ? 132.380 129.001 89.350  1.00 107.52 ?  256  ALA   D N     1 
ATOM   17105 C  CA    . ALA   D 2 257 ? 132.731 127.755 90.016  1.00 107.44 ?  256  ALA   D CA    1 
ATOM   17106 C  C     . ALA   D 2 257 ? 131.637 126.704 89.914  1.00 109.04 ?  256  ALA   D C     1 
ATOM   17107 O  O     . ALA   D 2 257 ? 131.893 125.535 90.220  1.00 111.30 ?  256  ALA   D O     1 
ATOM   17108 C  CB    . ALA   D 2 257 ? 133.056 128.017 91.489  1.00 106.89 ?  256  ALA   D CB    1 
ATOM   17109 N  N     . ASP   D 2 258 ? 130.435 127.088 89.492  1.00 108.89 ?  257  ASP   D N     1 
ATOM   17110 C  CA    . ASP   D 2 258 ? 129.334 126.154 89.316  1.00 109.89 ?  257  ASP   D CA    1 
ATOM   17111 C  C     . ASP   D 2 258 ? 129.029 125.845 87.861  1.00 111.53 ?  257  ASP   D C     1 
ATOM   17112 O  O     . ASP   D 2 258 ? 128.591 124.734 87.563  1.00 111.67 ?  257  ASP   D O     1 
ATOM   17113 C  CB    . ASP   D 2 258 ? 128.065 126.699 89.986  1.00 110.18 ?  257  ASP   D CB    1 
ATOM   17114 C  CG    . ASP   D 2 258 ? 126.884 125.759 89.860  1.00 113.45 ?  257  ASP   D CG    1 
ATOM   17115 O  OD1   . ASP   D 2 258 ? 126.813 124.783 90.636  1.00 113.52 ?  257  ASP   D OD1   1 
ATOM   17116 O  OD2   . ASP   D 2 258 ? 126.026 125.995 88.983  1.00 112.07 ?  257  ASP   D OD2   1 
ATOM   17117 N  N     . ASP   D 2 259 ? 129.207 126.810 86.963  1.00 124.17 ?  258  ASP   D N     1 
ATOM   17118 C  CA    . ASP   D 2 259 ? 128.965 126.618 85.541  1.00 122.57 ?  258  ASP   D CA    1 
ATOM   17119 C  C     . ASP   D 2 259 ? 129.965 127.449 84.749  1.00 123.71 ?  258  ASP   D C     1 
ATOM   17120 O  O     . ASP   D 2 259 ? 129.907 128.685 84.777  1.00 126.56 ?  258  ASP   D O     1 
ATOM   17121 C  CB    . ASP   D 2 259 ? 127.530 127.002 85.180  1.00 124.08 ?  258  ASP   D CB    1 
ATOM   17122 C  CG    . ASP   D 2 259 ? 127.176 126.652 83.750  1.00 127.02 ?  258  ASP   D CG    1 
ATOM   17123 O  OD1   . ASP   D 2 259 ? 127.872 125.805 83.154  1.00 125.95 ?  258  ASP   D OD1   1 
ATOM   17124 O  OD2   . ASP   D 2 259 ? 126.199 127.224 83.223  1.00 126.44 ?  258  ASP   D OD2   1 
ATOM   17125 N  N     . PRO   D 2 260 ? 130.895 126.813 84.030  1.00 108.46 ?  259  PRO   D N     1 
ATOM   17126 C  CA    . PRO   D 2 260 ? 131.915 127.577 83.296  1.00 108.90 ?  259  PRO   D CA    1 
ATOM   17127 C  C     . PRO   D 2 260 ? 131.357 128.414 82.154  1.00 110.46 ?  259  PRO   D C     1 
ATOM   17128 O  O     . PRO   D 2 260 ? 132.134 129.067 81.449  1.00 113.47 ?  259  PRO   D O     1 
ATOM   17129 C  CB    . PRO   D 2 260 ? 132.858 126.480 82.766  1.00 108.04 ?  259  PRO   D CB    1 
ATOM   17130 C  CG    . PRO   D 2 260 ? 132.541 125.255 83.583  1.00 108.71 ?  259  PRO   D CG    1 
ATOM   17131 C  CD    . PRO   D 2 260 ? 131.089 125.361 83.900  1.00 107.92 ?  259  PRO   D CD    1 
ATOM   17132 N  N     . GLU   D 2 261 ? 130.053 128.348 81.893  1.00 115.48 ?  260  GLU   D N     1 
ATOM   17133 C  CA    . GLU   D 2 261 ? 129.425 129.132 80.838  1.00 114.80 ?  260  GLU   D CA    1 
ATOM   17134 C  C     . GLU   D 2 261 ? 128.643 130.322 81.367  1.00 115.26 ?  260  GLU   D C     1 
ATOM   17135 O  O     . GLU   D 2 261 ? 128.540 131.337 80.671  1.00 113.86 ?  260  GLU   D O     1 
ATOM   17136 C  CB    . GLU   D 2 261 ? 128.490 128.250 80.000  1.00 115.47 ?  260  GLU   D CB    1 
ATOM   17137 C  CG    . GLU   D 2 261 ? 127.975 128.906 78.726  1.00 116.98 ?  260  GLU   D CG    1 
ATOM   17138 C  CD    . GLU   D 2 261 ? 126.955 128.049 78.004  1.00 119.40 ?  260  GLU   D CD    1 
ATOM   17139 O  OE1   . GLU   D 2 261 ? 127.073 126.807 78.064  1.00 117.94 ?  260  GLU   D OE1   1 
ATOM   17140 O  OE2   . GLU   D 2 261 ? 126.035 128.615 77.377  1.00 119.72 ?  260  GLU   D OE2   1 
ATOM   17141 N  N     . MET   D 2 262 ? 128.096 130.227 82.584  1.00 116.18 ?  261  MET   D N     1 
ATOM   17142 C  CA    . MET   D 2 262 ? 127.337 131.334 83.159  1.00 114.63 ?  261  MET   D CA    1 
ATOM   17143 C  C     . MET   D 2 262 ? 128.217 132.528 83.494  1.00 116.78 ?  261  MET   D C     1 
ATOM   17144 O  O     . MET   D 2 262 ? 127.699 133.642 83.628  1.00 119.81 ?  261  MET   D O     1 
ATOM   17145 C  CB    . MET   D 2 262 ? 126.588 130.879 84.413  1.00 111.60 ?  261  MET   D CB    1 
ATOM   17146 C  CG    . MET   D 2 262 ? 125.159 130.437 84.133  1.00 114.63 ?  261  MET   D CG    1 
ATOM   17147 S  SD    . MET   D 2 262 ? 124.068 131.837 83.820  1.00 121.71 ?  261  MET   D SD    1 
ATOM   17148 C  CE    . MET   D 2 262 ? 122.485 131.124 84.245  1.00 114.55 ?  261  MET   D CE    1 
ATOM   17149 N  N     . ALA   D 2 263 ? 129.528 132.322 83.642  1.00 114.40 ?  262  ALA   D N     1 
ATOM   17150 C  CA    . ALA   D 2 263 ? 130.422 133.447 83.894  1.00 113.48 ?  262  ALA   D CA    1 
ATOM   17151 C  C     . ALA   D 2 263 ? 130.401 134.422 82.730  1.00 117.41 ?  262  ALA   D C     1 
ATOM   17152 O  O     . ALA   D 2 263 ? 130.349 135.642 82.925  1.00 117.57 ?  262  ALA   D O     1 
ATOM   17153 C  CB    . ALA   D 2 263 ? 131.844 132.949 84.148  1.00 110.85 ?  262  ALA   D CB    1 
ATOM   17154 N  N     . GLU   D 2 264 ? 130.420 133.900 81.508  1.00 117.70 ?  263  GLU   D N     1 
ATOM   17155 C  CA    . GLU   D 2 264 ? 130.328 134.768 80.345  1.00 115.86 ?  263  GLU   D CA    1 
ATOM   17156 C  C     . GLU   D 2 264 ? 128.994 135.504 80.306  1.00 116.19 ?  263  GLU   D C     1 
ATOM   17157 O  O     . GLU   D 2 264 ? 128.948 136.701 80.007  1.00 119.09 ?  263  GLU   D O     1 
ATOM   17158 C  CB    . GLU   D 2 264 ? 130.520 133.946 79.075  1.00 116.03 ?  263  GLU   D CB    1 
ATOM   17159 C  CG    . GLU   D 2 264 ? 131.820 133.153 78.989  1.00 118.36 ?  263  GLU   D CG    1 
ATOM   17160 C  CD    . GLU   D 2 264 ? 131.951 132.344 77.720  1.00 120.77 ?  263  GLU   D CD    1 
ATOM   17161 O  OE1   . GLU   D 2 264 ? 131.162 132.573 76.783  1.00 120.76 ?  263  GLU   D OE1   1 
ATOM   17162 O  OE2   . GLU   D 2 264 ? 132.855 131.482 77.666  1.00 118.42 ?  263  GLU   D OE2   1 
ATOM   17163 N  N     . ILE   D 2 265 ? 127.894 134.806 80.601  1.00 108.99 ?  264  ILE   D N     1 
ATOM   17164 C  CA    . ILE   D 2 265 ? 126.585 135.454 80.573  1.00 110.91 ?  264  ILE   D CA    1 
ATOM   17165 C  C     . ILE   D 2 265 ? 126.527 136.583 81.593  1.00 112.83 ?  264  ILE   D C     1 
ATOM   17166 O  O     . ILE   D 2 265 ? 126.029 137.678 81.302  1.00 115.07 ?  264  ILE   D O     1 
ATOM   17167 C  CB    . ILE   D 2 265 ? 125.462 134.429 80.803  1.00 109.44 ?  264  ILE   D CB    1 
ATOM   17168 C  CG1   . ILE   D 2 265 ? 125.780 133.109 80.102  1.00 110.66 ?  264  ILE   D CG1   1 
ATOM   17169 C  CG2   . ILE   D 2 265 ? 124.156 134.984 80.293  1.00 108.75 ?  264  ILE   D CG2   1 
ATOM   17170 C  CD1   . ILE   D 2 265 ? 125.739 133.190 78.588  1.00 110.28 ?  264  ILE   D CD1   1 
ATOM   17171 N  N     . ALA   D 2 266 ? 127.042 136.342 82.800  1.00 110.07 ?  265  ALA   D N     1 
ATOM   17172 C  CA    . ALA   D 2 266 ? 127.121 137.403 83.800  1.00 108.27 ?  265  ALA   D CA    1 
ATOM   17173 C  C     . ALA   D 2 266 ? 127.993 138.565 83.331  1.00 113.32 ?  265  ALA   D C     1 
ATOM   17174 O  O     . ALA   D 2 266 ? 127.664 139.732 83.580  1.00 118.81 ?  265  ALA   D O     1 
ATOM   17175 C  CB    . ALA   D 2 266 ? 127.644 136.836 85.115  1.00 107.76 ?  265  ALA   D CB    1 
ATOM   17176 N  N     . GLU   D 2 267 ? 129.117 138.272 82.672  1.00 115.29 ?  266  GLU   D N     1 
ATOM   17177 C  CA    . GLU   D 2 267 ? 129.969 139.342 82.159  1.00 115.33 ?  266  GLU   D CA    1 
ATOM   17178 C  C     . GLU   D 2 267 ? 129.234 140.184 81.123  1.00 117.44 ?  266  GLU   D C     1 
ATOM   17179 O  O     . GLU   D 2 267 ? 129.365 141.414 81.104  1.00 119.11 ?  266  GLU   D O     1 
ATOM   17180 C  CB    . GLU   D 2 267 ? 131.246 138.752 81.563  1.00 114.46 ?  266  GLU   D CB    1 
ATOM   17181 C  CG    . GLU   D 2 267 ? 132.490 139.604 81.775  1.00 117.07 ?  266  GLU   D CG    1 
ATOM   17182 C  CD    . GLU   D 2 267 ? 132.697 140.004 83.222  1.00 120.00 ?  266  GLU   D CD    1 
ATOM   17183 O  OE1   . GLU   D 2 267 ? 132.174 141.062 83.631  1.00 118.92 ?  266  GLU   D OE1   1 
ATOM   17184 O  OE2   . GLU   D 2 267 ? 133.390 139.264 83.950  1.00 119.53 ?  266  GLU   D OE2   1 
ATOM   17185 N  N     . GLU   D 2 268 ? 128.459 139.540 80.253  1.00 124.02 ?  267  GLU   D N     1 
ATOM   17186 C  CA    . GLU   D 2 268 ? 127.694 140.255 79.238  1.00 122.72 ?  267  GLU   D CA    1 
ATOM   17187 C  C     . GLU   D 2 268 ? 126.422 140.896 79.787  1.00 124.23 ?  267  GLU   D C     1 
ATOM   17188 O  O     . GLU   D 2 268 ? 125.793 141.682 79.070  1.00 125.32 ?  267  GLU   D O     1 
ATOM   17189 C  CB    . GLU   D 2 268 ? 127.348 139.316 78.074  1.00 124.32 ?  267  GLU   D CB    1 
ATOM   17190 C  CG    . GLU   D 2 268 ? 128.314 139.397 76.880  1.00 125.04 ?  267  GLU   D CG    1 
ATOM   17191 C  CD    . GLU   D 2 268 ? 129.392 138.323 76.872  1.00 128.61 ?  267  GLU   D CD    1 
ATOM   17192 O  OE1   . GLU   D 2 268 ? 129.732 137.805 77.946  1.00 129.73 ?  267  GLU   D OE1   1 
ATOM   17193 O  OE2   . GLU   D 2 268 ? 129.920 138.013 75.783  1.00 128.00 ?  267  GLU   D OE2   1 
ATOM   17194 N  N     . CYS   D 2 269 ? 126.022 140.586 81.023  1.00 127.33 ?  268  CYS   D N     1 
ATOM   17195 C  CA    . CYS   D 2 269 ? 124.938 141.316 81.674  1.00 125.90 ?  268  CYS   D CA    1 
ATOM   17196 C  C     . CYS   D 2 269 ? 125.427 142.532 82.452  1.00 126.68 ?  268  CYS   D C     1 
ATOM   17197 O  O     . CYS   D 2 269 ? 124.616 143.205 83.096  1.00 127.53 ?  268  CYS   D O     1 
ATOM   17198 C  CB    . CYS   D 2 269 ? 124.143 140.403 82.619  1.00 124.87 ?  268  CYS   D CB    1 
ATOM   17199 S  SG    . CYS   D 2 269 ? 122.545 141.105 83.180  1.00 137.91 ?  268  CYS   D SG    1 
ATOM   17200 N  N     . LYS   D 2 270 ? 126.723 142.844 82.397  1.00 114.82 ?  269  LYS   D N     1 
ATOM   17201 C  CA    . LYS   D 2 270 ? 127.253 143.944 83.197  1.00 113.52 ?  269  LYS   D CA    1 
ATOM   17202 C  C     . LYS   D 2 270 ? 126.575 145.270 82.877  1.00 116.04 ?  269  LYS   D C     1 
ATOM   17203 O  O     . LYS   D 2 270 ? 126.609 146.186 83.705  1.00 117.91 ?  269  LYS   D O     1 
ATOM   17204 C  CB    . LYS   D 2 270 ? 128.763 144.064 82.991  1.00 115.15 ?  269  LYS   D CB    1 
ATOM   17205 C  CG    . LYS   D 2 270 ? 129.588 143.371 84.062  1.00 113.48 ?  269  LYS   D CG    1 
ATOM   17206 C  CD    . LYS   D 2 270 ? 129.121 143.755 85.456  1.00 114.86 ?  269  LYS   D CD    1 
ATOM   17207 C  CE    . LYS   D 2 270 ? 129.549 142.723 86.485  1.00 115.37 ?  269  LYS   D CE    1 
ATOM   17208 N  NZ    . LYS   D 2 270 ? 131.027 142.553 86.516  1.00 115.92 ?  269  LYS   D NZ    1 
ATOM   17209 N  N     . GLN   D 2 271 ? 125.959 145.390 81.703  1.00 120.35 ?  270  GLN   D N     1 
ATOM   17210 C  CA    . GLN   D 2 271 ? 125.177 146.563 81.336  1.00 120.94 ?  270  GLN   D CA    1 
ATOM   17211 C  C     . GLN   D 2 271 ? 123.682 146.361 81.534  1.00 121.08 ?  270  GLN   D C     1 
ATOM   17212 O  O     . GLN   D 2 271 ? 122.994 147.278 81.992  1.00 123.81 ?  270  GLN   D O     1 
ATOM   17213 C  CB    . GLN   D 2 271 ? 125.455 146.945 79.878  1.00 122.03 ?  270  GLN   D CB    1 
ATOM   17214 C  CG    . GLN   D 2 271 ? 124.789 148.234 79.392  1.00 122.79 ?  270  GLN   D CG    1 
ATOM   17215 C  CD    . GLN   D 2 271 ? 125.269 149.486 80.106  1.00 124.63 ?  270  GLN   D CD    1 
ATOM   17216 O  OE1   . GLN   D 2 271 ? 126.451 149.825 80.076  1.00 124.11 ?  270  GLN   D OE1   1 
ATOM   17217 N  NE2   . GLN   D 2 271 ? 124.338 150.195 80.732  1.00 123.12 ?  270  GLN   D NE2   1 
ATOM   17218 N  N     . GLU   D 2 272 ? 123.161 145.176 81.203  1.00 114.14 ?  271  GLU   D N     1 
ATOM   17219 C  CA    . GLU   D 2 272 ? 121.730 144.932 81.356  1.00 113.32 ?  271  GLU   D CA    1 
ATOM   17220 C  C     . GLU   D 2 272 ? 121.341 144.791 82.821  1.00 114.09 ?  271  GLU   D C     1 
ATOM   17221 O  O     . GLU   D 2 272 ? 120.297 145.302 83.241  1.00 115.47 ?  271  GLU   D O     1 
ATOM   17222 C  CB    . GLU   D 2 272 ? 121.319 143.680 80.582  1.00 111.64 ?  271  GLU   D CB    1 
ATOM   17223 C  CG    . GLU   D 2 272 ? 120.771 143.943 79.194  1.00 114.02 ?  271  GLU   D CG    1 
ATOM   17224 C  CD    . GLU   D 2 272 ? 119.938 142.787 78.675  1.00 117.44 ?  271  GLU   D CD    1 
ATOM   17225 O  OE1   . GLU   D 2 272 ? 120.507 141.897 78.009  1.00 117.85 ?  271  GLU   D OE1   1 
ATOM   17226 O  OE2   . GLU   D 2 272 ? 118.716 142.765 78.937  1.00 117.30 ?  271  GLU   D OE2   1 
ATOM   17227 N  N     . CYS   D 2 273 ? 122.154 144.085 83.610  1.00 108.48 ?  272  CYS   D N     1 
ATOM   17228 C  CA    . CYS   D 2 273 ? 121.866 143.947 85.034  1.00 104.85 ?  272  CYS   D CA    1 
ATOM   17229 C  C     . CYS   D 2 273 ? 121.917 145.302 85.738  1.00 107.30 ?  272  CYS   D C     1 
ATOM   17230 O  O     . CYS   D 2 273 ? 121.050 145.624 86.564  1.00 109.24 ?  272  CYS   D O     1 
ATOM   17231 C  CB    . CYS   D 2 273 ? 122.854 142.966 85.667  1.00 107.69 ?  272  CYS   D CB    1 
ATOM   17232 S  SG    . CYS   D 2 273 ? 122.668 141.199 85.212  1.00 115.87 ?  272  CYS   D SG    1 
ATOM   17233 N  N     . TYR   D 2 274 ? 122.923 146.116 85.407  1.00 106.02 ?  273  TYR   D N     1 
ATOM   17234 C  CA    . TYR   D 2 274 ? 123.026 147.460 85.968  1.00 103.04 ?  273  TYR   D CA    1 
ATOM   17235 C  C     . TYR   D 2 274 ? 121.843 148.325 85.549  1.00 103.18 ?  273  TYR   D C     1 
ATOM   17236 O  O     . TYR   D 2 274 ? 121.312 149.099 86.356  1.00 104.19 ?  273  TYR   D O     1 
ATOM   17237 C  CB    . TYR   D 2 274 ? 124.351 148.092 85.533  1.00 104.30 ?  273  TYR   D CB    1 
ATOM   17238 C  CG    . TYR   D 2 274 ? 124.556 149.533 85.952  1.00 106.61 ?  273  TYR   D CG    1 
ATOM   17239 C  CD1   . TYR   D 2 274 ? 125.182 149.846 87.151  1.00 106.33 ?  273  TYR   D CD1   1 
ATOM   17240 C  CD2   . TYR   D 2 274 ? 124.149 150.580 85.134  1.00 105.41 ?  273  TYR   D CD2   1 
ATOM   17241 C  CE1   . TYR   D 2 274 ? 125.378 151.161 87.532  1.00 106.00 ?  273  TYR   D CE1   1 
ATOM   17242 C  CE2   . TYR   D 2 274 ? 124.331 151.895 85.513  1.00 105.15 ?  273  TYR   D CE2   1 
ATOM   17243 C  CZ    . TYR   D 2 274 ? 124.953 152.180 86.707  1.00 106.74 ?  273  TYR   D CZ    1 
ATOM   17244 O  OH    . TYR   D 2 274 ? 125.145 153.490 87.078  1.00 105.71 ?  273  TYR   D OH    1 
ATOM   17245 N  N     . ASP   D 2 275 ? 121.424 148.218 84.284  1.00 107.70 ?  274  ASP   D N     1 
ATOM   17246 C  CA    . ASP   D 2 275 ? 120.251 148.957 83.825  1.00 106.03 ?  274  ASP   D CA    1 
ATOM   17247 C  C     . ASP   D 2 275 ? 119.006 148.540 84.592  1.00 108.70 ?  274  ASP   D C     1 
ATOM   17248 O  O     . ASP   D 2 275 ? 118.195 149.387 84.981  1.00 109.35 ?  274  ASP   D O     1 
ATOM   17249 C  CB    . ASP   D 2 275 ? 120.045 148.744 82.327  1.00 108.12 ?  274  ASP   D CB    1 
ATOM   17250 C  CG    . ASP   D 2 275 ? 120.862 149.697 81.488  1.00 110.99 ?  274  ASP   D CG    1 
ATOM   17251 O  OD1   . ASP   D 2 275 ? 121.185 150.797 81.982  1.00 111.02 ?  274  ASP   D OD1   1 
ATOM   17252 O  OD2   . ASP   D 2 275 ? 121.188 149.349 80.334  1.00 111.32 ?  274  ASP   D OD2   1 
ATOM   17253 N  N     . LEU   D 2 276 ? 118.841 147.237 84.823  1.00 103.25 ?  275  LEU   D N     1 
ATOM   17254 C  CA    . LEU   D 2 276 ? 117.701 146.753 85.591  1.00 98.68  ?  275  LEU   D CA    1 
ATOM   17255 C  C     . LEU   D 2 276 ? 117.710 147.321 87.002  1.00 98.42  ?  275  LEU   D C     1 
ATOM   17256 O  O     . LEU   D 2 276 ? 116.675 147.780 87.502  1.00 97.89  ?  275  LEU   D O     1 
ATOM   17257 C  CB    . LEU   D 2 276 ? 117.714 145.224 85.615  1.00 96.06  ?  275  LEU   D CB    1 
ATOM   17258 C  CG    . LEU   D 2 276 ? 116.651 144.434 86.382  1.00 97.07  ?  275  LEU   D CG    1 
ATOM   17259 C  CD1   . LEU   D 2 276 ? 116.444 143.091 85.713  1.00 97.60  ?  275  LEU   D CD1   1 
ATOM   17260 C  CD2   . LEU   D 2 276 ? 117.027 144.227 87.843  1.00 97.99  ?  275  LEU   D CD2   1 
ATOM   17261 N  N     . PHE   D 2 277 ? 118.878 147.325 87.648  1.00 93.52  ?  276  PHE   D N     1 
ATOM   17262 C  CA    . PHE   D 2 277 ? 118.961 147.821 89.017  1.00 88.87  ?  276  PHE   D CA    1 
ATOM   17263 C  C     . PHE   D 2 277 ? 118.680 149.318 89.092  1.00 90.88  ?  276  PHE   D C     1 
ATOM   17264 O  O     . PHE   D 2 277 ? 117.955 149.773 89.986  1.00 93.60  ?  276  PHE   D O     1 
ATOM   17265 C  CB    . PHE   D 2 277 ? 120.329 147.494 89.602  1.00 90.75  ?  276  PHE   D CB    1 
ATOM   17266 C  CG    . PHE   D 2 277 ? 120.331 146.286 90.489  1.00 91.81  ?  276  PHE   D CG    1 
ATOM   17267 C  CD1   . PHE   D 2 277 ? 119.883 146.371 91.795  1.00 90.21  ?  276  PHE   D CD1   1 
ATOM   17268 C  CD2   . PHE   D 2 277 ? 120.777 145.065 90.018  1.00 92.39  ?  276  PHE   D CD2   1 
ATOM   17269 C  CE1   . PHE   D 2 277 ? 119.883 145.263 92.615  1.00 90.75  ?  276  PHE   D CE1   1 
ATOM   17270 C  CE2   . PHE   D 2 277 ? 120.779 143.952 90.833  1.00 90.89  ?  276  PHE   D CE2   1 
ATOM   17271 C  CZ    . PHE   D 2 277 ? 120.330 144.052 92.133  1.00 90.92  ?  276  PHE   D CZ    1 
ATOM   17272 N  N     . VAL   D 2 278 ? 119.242 150.104 88.169  1.00 101.79 ?  277  VAL   D N     1 
ATOM   17273 C  CA    . VAL   D 2 278 ? 118.987 151.542 88.210  1.00 98.58  ?  277  VAL   D CA    1 
ATOM   17274 C  C     . VAL   D 2 278 ? 117.538 151.844 87.843  1.00 98.86  ?  277  VAL   D C     1 
ATOM   17275 O  O     . VAL   D 2 278 ? 116.951 152.804 88.355  1.00 101.12 ?  277  VAL   D O     1 
ATOM   17276 C  CB    . VAL   D 2 278 ? 119.981 152.311 87.317  1.00 99.86  ?  277  VAL   D CB    1 
ATOM   17277 C  CG1   . VAL   D 2 278 ? 121.404 152.113 87.815  1.00 101.45 ?  277  VAL   D CG1   1 
ATOM   17278 C  CG2   . VAL   D 2 278 ? 119.856 151.892 85.863  1.00 102.99 ?  277  VAL   D CG2   1 
ATOM   17279 N  N     . GLN   D 2 279 ? 116.929 151.034 86.971  1.00 104.91 ?  278  GLN   D N     1 
ATOM   17280 C  CA    . GLN   D 2 279 ? 115.510 151.197 86.678  1.00 105.96 ?  278  GLN   D CA    1 
ATOM   17281 C  C     . GLN   D 2 279 ? 114.664 150.926 87.913  1.00 107.88 ?  278  GLN   D C     1 
ATOM   17282 O  O     . GLN   D 2 279 ? 113.698 151.646 88.182  1.00 108.71 ?  278  GLN   D O     1 
ATOM   17283 C  CB    . GLN   D 2 279 ? 115.100 150.268 85.535  1.00 105.83 ?  278  GLN   D CB    1 
ATOM   17284 C  CG    . GLN   D 2 279 ? 113.695 150.502 85.001  1.00 107.75 ?  278  GLN   D CG    1 
ATOM   17285 C  CD    . GLN   D 2 279 ? 113.568 151.778 84.201  1.00 112.21 ?  278  GLN   D CD    1 
ATOM   17286 O  OE1   . GLN   D 2 279 ? 114.117 151.892 83.106  1.00 111.50 ?  278  GLN   D OE1   1 
ATOM   17287 N  NE2   . GLN   D 2 279 ? 112.831 152.747 84.741  1.00 111.99 ?  278  GLN   D NE2   1 
ATOM   17288 N  N     . ALA   D 2 280 ? 115.012 149.886 88.674  1.00 100.54 ?  279  ALA   D N     1 
ATOM   17289 C  CA    . ALA   D 2 280 ? 114.292 149.604 89.912  1.00 97.84  ?  279  ALA   D CA    1 
ATOM   17290 C  C     . ALA   D 2 280 ? 114.453 150.740 90.916  1.00 97.86  ?  279  ALA   D C     1 
ATOM   17291 O  O     . ALA   D 2 280 ? 113.489 151.128 91.589  1.00 98.81  ?  279  ALA   D O     1 
ATOM   17292 C  CB    . ALA   D 2 280 ? 114.774 148.284 90.511  1.00 96.89  ?  279  ALA   D CB    1 
ATOM   17293 N  N     . ALA   D 2 281 ? 115.667 151.285 91.032  1.00 98.77  ?  280  ALA   D N     1 
ATOM   17294 C  CA    . ALA   D 2 281 ? 115.889 152.406 91.942  1.00 95.00  ?  280  ALA   D CA    1 
ATOM   17295 C  C     . ALA   D 2 281 ? 115.078 153.627 91.524  1.00 95.87  ?  280  ALA   D C     1 
ATOM   17296 O  O     . ALA   D 2 281 ? 114.476 154.303 92.368  1.00 99.74  ?  280  ALA   D O     1 
ATOM   17297 C  CB    . ALA   D 2 281 ? 117.378 152.745 92.003  1.00 95.96  ?  280  ALA   D CB    1 
ATOM   17298 N  N     . GLN   D 2 282 ? 115.048 153.924 90.222  1.00 101.42 ?  281  GLN   D N     1 
ATOM   17299 C  CA    . GLN   D 2 282 ? 114.248 155.041 89.733  1.00 102.46 ?  281  GLN   D CA    1 
ATOM   17300 C  C     . GLN   D 2 282 ? 112.766 154.811 89.991  1.00 104.95 ?  281  GLN   D C     1 
ATOM   17301 O  O     . GLN   D 2 282 ? 112.040 155.740 90.358  1.00 107.01 ?  281  GLN   D O     1 
ATOM   17302 C  CB    . GLN   D 2 282 ? 114.499 155.259 88.242  1.00 104.12 ?  281  GLN   D CB    1 
ATOM   17303 C  CG    . GLN   D 2 282 ? 113.965 156.582 87.718  1.00 104.64 ?  281  GLN   D CG    1 
ATOM   17304 C  CD    . GLN   D 2 282 ? 114.636 157.786 88.338  1.00 106.91 ?  281  GLN   D CD    1 
ATOM   17305 O  OE1   . GLN   D 2 282 ? 113.999 158.570 89.041  1.00 106.82 ?  281  GLN   D OE1   1 
ATOM   17306 N  NE2   . GLN   D 2 282 ? 115.923 157.949 88.068  1.00 106.27 ?  281  GLN   D NE2   1 
ATOM   17307 N  N     . GLN   D 2 283 ? 112.295 153.582 89.789  1.00 106.67 ?  282  GLN   D N     1 
ATOM   17308 C  CA    . GLN   D 2 283 ? 110.896 153.276 90.057  1.00 104.13 ?  282  GLN   D CA    1 
ATOM   17309 C  C     . GLN   D 2 283 ? 110.565 153.479 91.530  1.00 105.35 ?  282  GLN   D C     1 
ATOM   17310 O  O     . GLN   D 2 283 ? 109.498 154.004 91.868  1.00 108.10 ?  282  GLN   D O     1 
ATOM   17311 C  CB    . GLN   D 2 283 ? 110.587 151.846 89.620  1.00 105.79 ?  282  GLN   D CB    1 
ATOM   17312 C  CG    . GLN   D 2 283 ? 110.452 151.673 88.117  1.00 104.74 ?  282  GLN   D CG    1 
ATOM   17313 C  CD    . GLN   D 2 283 ? 109.185 150.963 87.712  1.00 108.67 ?  282  GLN   D CD    1 
ATOM   17314 O  OE1   . GLN   D 2 283 ? 108.996 149.786 88.012  1.00 109.02 ?  282  GLN   D OE1   1 
ATOM   17315 N  NE2   . GLN   D 2 283 ? 108.310 151.675 87.013  1.00 111.25 ?  282  GLN   D NE2   1 
ATOM   17316 N  N     . GLU   D 2 284 ? 111.475 153.116 92.428  1.00 101.67 ?  283  GLU   D N     1 
ATOM   17317 C  CA    . GLU   D 2 284 ? 111.197 153.327 93.872  1.00 101.68 ?  283  GLU   D CA    1 
ATOM   17318 C  C     . GLU   D 2 284 ? 111.222 154.824 94.188  1.00 100.95 ?  283  GLU   D C     1 
ATOM   17319 O  O     . GLU   D 2 284 ? 110.422 155.254 95.027  1.00 101.64 ?  283  GLU   D O     1 
ATOM   17320 C  CB    . GLU   D 2 284 ? 112.172 152.566 94.770  1.00 103.24 ?  283  GLU   D CB    1 
ATOM   17321 C  CG    . GLU   D 2 284 ? 111.945 151.069 94.771  1.00 105.75 ?  283  GLU   D CG    1 
ATOM   17322 C  CD    . GLU   D 2 284 ? 110.499 150.671 95.006  1.00 107.58 ?  283  GLU   D CD    1 
ATOM   17323 O  OE1   . GLU   D 2 284 ? 109.954 151.027 96.068  1.00 107.30 ?  283  GLU   D OE1   1 
ATOM   17324 O  OE2   . GLU   D 2 284 ? 109.923 150.008 94.124  1.00 107.08 ?  283  GLU   D OE2   1 
ATOM   17325 N  N     . LYS   D 2 285 ? 112.110 155.579 93.542  1.00 105.08 ?  284  LYS   D N     1 
ATOM   17326 C  CA    . LYS   D 2 285 ? 112.114 157.021 93.776  1.00 103.38 ?  284  LYS   D CA    1 
ATOM   17327 C  C     . LYS   D 2 285 ? 110.812 157.665 93.309  1.00 103.95 ?  284  LYS   D C     1 
ATOM   17328 O  O     . LYS   D 2 285 ? 110.254 158.532 93.994  1.00 108.19 ?  284  LYS   D O     1 
ATOM   17329 C  CB    . LYS   D 2 285 ? 113.305 157.663 93.067  1.00 103.19 ?  284  LYS   D CB    1 
ATOM   17330 C  CG    . LYS   D 2 285 ? 114.657 157.280 93.632  1.00 104.56 ?  284  LYS   D CG    1 
ATOM   17331 C  CD    . LYS   D 2 285 ? 115.610 158.452 93.627  1.00 103.47 ?  284  LYS   D CD    1 
ATOM   17332 C  CE    . LYS   D 2 285 ? 116.581 158.350 92.468  1.00 103.74 ?  284  LYS   D CE    1 
ATOM   17333 N  NZ    . LYS   D 2 285 ? 117.899 157.814 92.891  1.00 106.64 ?  284  LYS   D NZ    1 
ATOM   17334 N  N     . ASP   D 2 286 ? 110.314 157.254 92.142  1.00 106.68 ?  285  ASP   D N     1 
ATOM   17335 C  CA    . ASP   D 2 286 ? 109.049 157.792 91.654  1.00 106.71 ?  285  ASP   D CA    1 
ATOM   17336 C  C     . ASP   D 2 286 ? 107.872 157.332 92.507  1.00 107.19 ?  285  ASP   D C     1 
ATOM   17337 O  O     . ASP   D 2 286 ? 106.908 158.085 92.680  1.00 110.32 ?  285  ASP   D O     1 
ATOM   17338 C  CB    . ASP   D 2 286 ? 108.844 157.408 90.190  1.00 109.38 ?  285  ASP   D CB    1 
ATOM   17339 C  CG    . ASP   D 2 286 ? 109.954 157.922 89.295  1.00 112.59 ?  285  ASP   D CG    1 
ATOM   17340 O  OD1   . ASP   D 2 286 ? 111.076 158.127 89.796  1.00 113.64 ?  285  ASP   D OD1   1 
ATOM   17341 O  OD2   . ASP   D 2 286 ? 109.712 158.115 88.087  1.00 111.12 ?  285  ASP   D OD2   1 
ATOM   17342 N  N     . TRP   D 2 287 ? 107.939 156.118 93.062  1.00 96.74  ?  286  TRP   D N     1 
ATOM   17343 C  CA    . TRP   D 2 287 ? 106.928 155.688 94.022  1.00 97.45  ?  286  TRP   D CA    1 
ATOM   17344 C  C     . TRP   D 2 287 ? 106.952 156.559 95.270  1.00 99.32  ?  286  TRP   D C     1 
ATOM   17345 O  O     . TRP   D 2 287 ? 105.898 156.912 95.810  1.00 99.82  ?  286  TRP   D O     1 
ATOM   17346 C  CB    . TRP   D 2 287 ? 107.140 154.220 94.389  1.00 97.72  ?  286  TRP   D CB    1 
ATOM   17347 C  CG    . TRP   D 2 287 ? 106.147 153.721 95.386  1.00 96.06  ?  286  TRP   D CG    1 
ATOM   17348 C  CD1   . TRP   D 2 287 ? 106.383 153.410 96.692  1.00 94.23  ?  286  TRP   D CD1   1 
ATOM   17349 C  CD2   . TRP   D 2 287 ? 104.754 153.481 95.161  1.00 94.16  ?  286  TRP   D CD2   1 
ATOM   17350 N  NE1   . TRP   D 2 287 ? 105.223 152.989 97.295  1.00 92.58  ?  286  TRP   D NE1   1 
ATOM   17351 C  CE2   . TRP   D 2 287 ? 104.208 153.023 96.375  1.00 93.04  ?  286  TRP   D CE2   1 
ATOM   17352 C  CE3   . TRP   D 2 287 ? 103.915 153.607 94.050  1.00 95.91  ?  286  TRP   D CE3   1 
ATOM   17353 C  CZ2   . TRP   D 2 287 ? 102.863 152.692 96.510  1.00 94.79  ?  286  TRP   D CZ2   1 
ATOM   17354 C  CZ3   . TRP   D 2 287 ? 102.581 153.277 94.186  1.00 98.74  ?  286  TRP   D CZ3   1 
ATOM   17355 C  CH2   . TRP   D 2 287 ? 102.068 152.825 95.406  1.00 96.02  ?  286  TRP   D CH2   1 
ATOM   17356 N  N     . ALA   D 2 288 ? 108.150 156.907 95.748  1.00 109.09 ?  287  ALA   D N     1 
ATOM   17357 C  CA    . ALA   D 2 288 ? 108.261 157.817 96.884  1.00 106.81 ?  287  ALA   D CA    1 
ATOM   17358 C  C     . ALA   D 2 288 ? 107.678 159.182 96.547  1.00 105.74 ?  287  ALA   D C     1 
ATOM   17359 O  O     . ALA   D 2 288 ? 107.020 159.811 97.384  1.00 108.80 ?  287  ALA   D O     1 
ATOM   17360 C  CB    . ALA   D 2 288 ? 109.723 157.945 97.314  1.00 107.49 ?  287  ALA   D CB    1 
ATOM   17361 N  N     . ASP   D 2 289 ? 107.917 159.656 95.324  1.00 112.15 ?  288  ASP   D N     1 
ATOM   17362 C  CA    . ASP   D 2 289 ? 107.299 160.895 94.861  1.00 113.72 ?  288  ASP   D CA    1 
ATOM   17363 C  C     . ASP   D 2 289 ? 105.781 160.801 94.931  1.00 115.25 ?  288  ASP   D C     1 
ATOM   17364 O  O     . ASP   D 2 289 ? 105.122 161.680 95.498  1.00 119.38 ?  288  ASP   D O     1 
ATOM   17365 C  CB    . ASP   D 2 289 ? 107.781 161.199 93.439  1.00 115.47 ?  288  ASP   D CB    1 
ATOM   17366 C  CG    . ASP   D 2 289 ? 107.114 162.436 92.817  1.00 119.51 ?  288  ASP   D CG    1 
ATOM   17367 O  OD1   . ASP   D 2 289 ? 105.889 162.650 92.955  1.00 120.96 ?  288  ASP   D OD1   1 
ATOM   17368 O  OD2   . ASP   D 2 289 ? 107.834 163.202 92.146  1.00 119.14 ?  288  ASP   D OD2   1 
ATOM   17369 N  N     . TYR   D 2 290 ? 105.215 159.710 94.407  1.00 104.87 ?  289  TYR   D N     1 
ATOM   17370 C  CA    . TYR   D 2 290 ? 103.767 159.531 94.418  1.00 105.11 ?  289  TYR   D CA    1 
ATOM   17371 C  C     . TYR   D 2 290 ? 103.220 159.417 95.835  1.00 103.97 ?  289  TYR   D C     1 
ATOM   17372 O  O     . TYR   D 2 290 ? 102.078 159.814 96.089  1.00 104.74 ?  289  TYR   D O     1 
ATOM   17373 C  CB    . TYR   D 2 290 ? 103.395 158.295 93.601  1.00 107.17 ?  289  TYR   D CB    1 
ATOM   17374 C  CG    . TYR   D 2 290 ? 101.987 157.801 93.835  1.00 106.52 ?  289  TYR   D CG    1 
ATOM   17375 C  CD1   . TYR   D 2 290 ? 100.893 158.525 93.386  1.00 107.91 ?  289  TYR   D CD1   1 
ATOM   17376 C  CD2   . TYR   D 2 290 ? 101.752 156.609 94.506  1.00 104.27 ?  289  TYR   D CD2   1 
ATOM   17377 C  CE1   . TYR   D 2 290 ? 99.604  158.076 93.598  1.00 107.81 ?  289  TYR   D CE1   1 
ATOM   17378 C  CE2   . TYR   D 2 290 ? 100.467 156.154 94.723  1.00 104.59 ?  289  TYR   D CE2   1 
ATOM   17379 C  CZ    . TYR   D 2 290 ? 99.396  156.891 94.266  1.00 106.27 ?  289  TYR   D CZ    1 
ATOM   17380 O  OH    . TYR   D 2 290 ? 98.114  156.441 94.481  1.00 105.62 ?  289  TYR   D OH    1 
ATOM   17381 N  N     . LEU   D 2 291 ? 104.012 158.883 96.767  1.00 104.25 ?  290  LEU   D N     1 
ATOM   17382 C  CA    . LEU   D 2 291 ? 103.538 158.702 98.136  1.00 103.64 ?  290  LEU   D CA    1 
ATOM   17383 C  C     . LEU   D 2 291 ? 103.286 160.040 98.819  1.00 106.81 ?  290  LEU   D C     1 
ATOM   17384 O  O     . LEU   D 2 291 ? 102.192 160.287 99.337  1.00 107.63 ?  290  LEU   D O     1 
ATOM   17385 C  CB    . LEU   D 2 291 ? 104.546 157.872 98.926  1.00 104.36 ?  290  LEU   D CB    1 
ATOM   17386 C  CG    . LEU   D 2 291 ? 104.421 156.353 98.851  1.00 104.38 ?  290  LEU   D CG    1 
ATOM   17387 C  CD1   . LEU   D 2 291 ? 105.593 155.689 99.554  1.00 103.30 ?  290  LEU   D CD1   1 
ATOM   17388 C  CD2   . LEU   D 2 291 ? 103.104 155.900 99.448  1.00 104.08 ?  290  LEU   D CD2   1 
ATOM   17389 N  N     . PHE   D 2 292 ? 104.270 160.939 98.783  1.00 113.76 ?  291  PHE   D N     1 
ATOM   17390 C  CA    . PHE   D 2 292 ? 104.144 162.259 99.393  1.00 111.55 ?  291  PHE   D CA    1 
ATOM   17391 C  C     . PHE   D 2 292 ? 103.926 163.290 98.288  1.00 112.43 ?  291  PHE   D C     1 
ATOM   17392 O  O     . PHE   D 2 292 ? 104.853 163.946 97.813  1.00 113.72 ?  291  PHE   D O     1 
ATOM   17393 C  CB    . PHE   D 2 292 ? 105.375 162.582 100.230 1.00 109.37 ?  291  PHE   D CB    1 
ATOM   17394 C  CG    . PHE   D 2 292 ? 105.950 161.400 100.952 1.00 110.48 ?  291  PHE   D CG    1 
ATOM   17395 C  CD1   . PHE   D 2 292 ? 105.513 161.069 102.220 1.00 112.10 ?  291  PHE   D CD1   1 
ATOM   17396 C  CD2   . PHE   D 2 292 ? 106.979 160.667 100.393 1.00 110.05 ?  291  PHE   D CD2   1 
ATOM   17397 C  CE1   . PHE   D 2 292 ? 106.047 159.989 102.891 1.00 112.89 ?  291  PHE   D CE1   1 
ATOM   17398 C  CE2   . PHE   D 2 292 ? 107.517 159.586 101.057 1.00 110.33 ?  291  PHE   D CE2   1 
ATOM   17399 C  CZ    . PHE   D 2 292 ? 107.054 159.248 102.310 1.00 111.88 ?  291  PHE   D CZ    1 
ATOM   17400 N  N     . ARG   D 2 293 ? 102.668 163.430 97.879  1.00 117.69 ?  292  ARG   D N     1 
ATOM   17401 C  CA    . ARG   D 2 293 ? 102.270 164.466 96.935  1.00 118.97 ?  292  ARG   D CA    1 
ATOM   17402 C  C     . ARG   D 2 293 ? 101.350 165.498 97.567  1.00 121.70 ?  292  ARG   D C     1 
ATOM   17403 O  O     . ARG   D 2 293 ? 101.633 166.698 97.508  1.00 121.72 ?  292  ARG   D O     1 
ATOM   17404 C  CB    . ARG   D 2 293 ? 101.594 163.843 95.705  1.00 117.07 ?  292  ARG   D CB    1 
ATOM   17405 C  CG    . ARG   D 2 293 ? 100.669 162.690 96.020  1.00 118.12 ?  292  ARG   D CG    1 
ATOM   17406 C  CD    . ARG   D 2 293 ? 99.584  162.536 94.966  1.00 119.60 ?  292  ARG   D CD    1 
ATOM   17407 N  NE    . ARG   D 2 293 ? 98.446  161.762 95.447  1.00 121.11 ?  292  ARG   D NE    1 
ATOM   17408 C  CZ    . ARG   D 2 293 ? 97.550  161.185 94.658  1.00 120.44 ?  292  ARG   D CZ    1 
ATOM   17409 N  NH1   . ARG   D 2 293 ? 97.632  161.274 93.340  1.00 117.93 ?  292  ARG   D NH1   1 
ATOM   17410 N  NH2   . ARG   D 2 293 ? 96.548  160.503 95.203  1.00 118.55 ?  292  ARG   D NH2   1 
ATOM   17411 N  N     . ASP   D 2 294 ? 100.251 165.060 98.174  1.00 128.98 ?  293  ASP   D N     1 
ATOM   17412 C  CA    . ASP   D 2 294 ? 99.343  165.958 98.886  1.00 128.11 ?  293  ASP   D CA    1 
ATOM   17413 C  C     . ASP   D 2 294 ? 99.673  166.021 100.375 1.00 127.68 ?  293  ASP   D C     1 
ATOM   17414 O  O     . ASP   D 2 294 ? 98.810  165.837 101.231 1.00 128.40 ?  293  ASP   D O     1 
ATOM   17415 C  CB    . ASP   D 2 294 ? 97.902  165.516 98.664  1.00 126.30 ?  293  ASP   D CB    1 
ATOM   17416 C  CG    . ASP   D 2 294 ? 97.724  164.017 98.806  1.00 128.01 ?  293  ASP   D CG    1 
ATOM   17417 O  OD1   . ASP   D 2 294 ? 97.571  163.540 99.950  1.00 128.22 ?  293  ASP   D OD1   1 
ATOM   17418 O  OD2   . ASP   D 2 294 ? 97.739  163.315 97.774  1.00 127.75 ?  293  ASP   D OD2   1 
ATOM   17419 N  N     . GLY   D 2 295 ? 100.937 166.286 100.695 1.00 121.08 ?  294  GLY   D N     1 
ATOM   17420 C  CA    . GLY   D 2 295 ? 101.389 166.406 102.062 1.00 121.86 ?  294  GLY   D CA    1 
ATOM   17421 C  C     . GLY   D 2 295 ? 102.624 165.571 102.305 1.00 123.41 ?  294  GLY   D C     1 
ATOM   17422 O  O     . GLY   D 2 295 ? 103.233 165.024 101.379 1.00 123.33 ?  294  GLY   D O     1 
ATOM   17423 N  N     . SER   D 2 296 ? 103.001 165.468 103.576 1.00 118.10 ?  295  SER   D N     1 
ATOM   17424 C  CA    . SER   D 2 296 ? 104.185 164.722 103.977 1.00 114.79 ?  295  SER   D CA    1 
ATOM   17425 C  C     . SER   D 2 296 ? 104.029 164.316 105.435 1.00 114.32 ?  295  SER   D C     1 
ATOM   17426 O  O     . SER   D 2 296 ? 103.148 164.803 106.147 1.00 114.82 ?  295  SER   D O     1 
ATOM   17427 C  CB    . SER   D 2 296 ? 105.463 165.538 103.768 1.00 113.55 ?  295  SER   D CB    1 
ATOM   17428 O  OG    . SER   D 2 296 ? 106.579 164.686 103.579 1.00 113.06 ?  295  SER   D OG    1 
ATOM   17429 N  N     . MET   D 2 297 ? 104.957 163.478 105.850 1.00 120.97 ?  296  MET   D N     1 
ATOM   17430 C  CA    A MET   D 2 297 ? 104.858 162.862 107.213 0.50 121.44 ?  296  MET   D CA    1 
ATOM   17431 C  CA    B MET   D 2 297 ? 104.899 162.922 107.229 0.50 121.44 ?  296  MET   D CA    1 
ATOM   17432 C  C     . MET   D 2 297 ? 106.007 163.470 108.140 1.00 120.95 ?  296  MET   D C     1 
ATOM   17433 O  O     . MET   D 2 297 ? 107.174 163.866 107.798 1.00 122.03 ?  296  MET   D O     1 
ATOM   17434 C  CB    A MET   D 2 297 ? 105.125 161.356 107.190 0.50 122.40 ?  296  MET   D CB    1 
ATOM   17435 C  CB    B MET   D 2 297 ? 105.023 161.399 107.220 0.50 122.40 ?  296  MET   D CB    1 
ATOM   17436 C  CG    A MET   D 2 297 ? 105.035 160.695 108.550 0.50 121.31 ?  296  MET   D CG    1 
ATOM   17437 C  CG    B MET   D 2 297 ? 103.712 160.667 107.292 0.50 121.31 ?  296  MET   D CG    1 
ATOM   17438 S  SD    A MET   D 2 297 ? 105.243 158.912 108.447 0.50 128.84 ?  296  MET   D SD    1 
ATOM   17439 S  SD    B MET   D 2 297 ? 103.961 158.985 107.899 0.50 128.84 ?  296  MET   D SD    1 
ATOM   17440 C  CE    A MET   D 2 297 ? 103.624 158.433 107.864 0.50 120.61 ?  296  MET   D CE    1 
ATOM   17441 C  CE    B MET   D 2 297 ? 105.567 159.142 108.677 0.50 120.61 ?  296  MET   D CE    1 
ATOM   17442 N  N     . ILE   D 2 298 ? 105.756 163.307 109.411 1.00 113.41 ?  297  ILE   D N     1 
ATOM   17443 C  CA    . ILE   D 2 298 ? 106.621 163.964 110.386 1.00 114.48 ?  297  ILE   D CA    1 
ATOM   17444 C  C     . ILE   D 2 298 ? 108.069 163.521 110.205 1.00 114.73 ?  297  ILE   D C     1 
ATOM   17445 O  O     . ILE   D 2 298 ? 108.987 164.348 110.139 1.00 116.31 ?  297  ILE   D O     1 
ATOM   17446 C  CB    . ILE   D 2 298 ? 106.117 163.691 111.815 1.00 114.50 ?  297  ILE   D CB    1 
ATOM   17447 C  CG1   . ILE   D 2 298 ? 104.958 164.632 112.158 1.00 114.58 ?  297  ILE   D CG1   1 
ATOM   17448 C  CG2   . ILE   D 2 298 ? 107.242 163.851 112.813 1.00 112.87 ?  297  ILE   D CG2   1 
ATOM   17449 C  CD1   . ILE   D 2 298 ? 105.321 166.104 112.070 1.00 112.74 ?  297  ILE   D CD1   1 
ATOM   17450 N  N     . GLY   D 2 299 ? 108.294 162.211 110.109 1.00 105.97 ?  298  GLY   D N     1 
ATOM   17451 C  CA    . GLY   D 2 299 ? 109.629 161.662 109.989 1.00 105.92 ?  298  GLY   D CA    1 
ATOM   17452 C  C     . GLY   D 2 299 ? 110.009 161.136 108.625 1.00 107.21 ?  298  GLY   D C     1 
ATOM   17453 O  O     . GLY   D 2 299 ? 111.098 160.562 108.485 1.00 106.63 ?  298  GLY   D O     1 
ATOM   17454 N  N     . LEU   D 2 300 ? 109.166 161.304 107.608 1.00 114.44 ?  299  LEU   D N     1 
ATOM   17455 C  CA    . LEU   D 2 300 ? 109.463 160.810 106.273 1.00 114.68 ?  299  LEU   D CA    1 
ATOM   17456 C  C     . LEU   D 2 300 ? 108.951 161.793 105.233 1.00 114.00 ?  299  LEU   D C     1 
ATOM   17457 O  O     . LEU   D 2 300 ? 107.839 162.315 105.354 1.00 112.89 ?  299  LEU   D O     1 
ATOM   17458 C  CB    . LEU   D 2 300 ? 108.843 159.428 106.035 1.00 113.77 ?  299  LEU   D CB    1 
ATOM   17459 C  CG    . LEU   D 2 300 ? 109.813 158.255 105.877 1.00 113.76 ?  299  LEU   D CG    1 
ATOM   17460 C  CD1   . LEU   D 2 300 ? 109.135 157.104 105.155 1.00 114.52 ?  299  LEU   D CD1   1 
ATOM   17461 C  CD2   . LEU   D 2 300 ? 111.076 158.681 105.143 1.00 113.36 ?  299  LEU   D CD2   1 
ATOM   17462 N  N     . ASN   D 2 301 ? 109.769 162.040 104.214 1.00 117.75 ?  300  ASN   D N     1 
ATOM   17463 C  CA    . ASN   D 2 301 ? 109.396 162.907 103.107 1.00 116.80 ?  300  ASN   D CA    1 
ATOM   17464 C  C     . ASN   D 2 301 ? 110.061 162.383 101.842 1.00 117.92 ?  300  ASN   D C     1 
ATOM   17465 O  O     . ASN   D 2 301 ? 110.718 161.339 101.851 1.00 118.08 ?  300  ASN   D O     1 
ATOM   17466 C  CB    . ASN   D 2 301 ? 109.779 164.362 103.392 1.00 114.61 ?  300  ASN   D CB    1 
ATOM   17467 C  CG    . ASN   D 2 301 ? 111.244 164.523 103.751 1.00 115.63 ?  300  ASN   D CG    1 
ATOM   17468 O  OD1   . ASN   D 2 301 ? 112.128 164.298 102.924 1.00 120.27 ?  300  ASN   D OD1   1 
ATOM   17469 N  ND2   . ASN   D 2 301 ? 111.509 164.916 104.990 1.00 115.15 ?  300  ASN   D ND2   1 
ATOM   17470 N  N     . LYS   D 2 302 ? 109.869 163.114 100.739 1.00 121.87 ?  301  LYS   D N     1 
ATOM   17471 C  CA    . LYS   D 2 302 ? 110.447 162.703 99.462  1.00 121.70 ?  301  LYS   D CA    1 
ATOM   17472 C  C     . LYS   D 2 302 ? 111.968 162.671 99.525  1.00 120.84 ?  301  LYS   D C     1 
ATOM   17473 O  O     . LYS   D 2 302 ? 112.598 161.715 99.056  1.00 122.94 ?  301  LYS   D O     1 
ATOM   17474 C  CB    . LYS   D 2 302 ? 109.991 163.642 98.347  1.00 122.50 ?  301  LYS   D CB    1 
ATOM   17475 C  CG    . LYS   D 2 302 ? 109.917 162.985 96.981  1.00 122.66 ?  301  LYS   D CG    1 
ATOM   17476 C  CD    . LYS   D 2 302 ? 109.725 164.037 95.894  1.00 123.36 ?  301  LYS   D CD    1 
ATOM   17477 C  CE    . LYS   D 2 302 ? 111.001 164.826 95.629  1.00 122.65 ?  301  LYS   D CE    1 
ATOM   17478 N  NZ    . LYS   D 2 302 ? 112.066 163.974 95.033  1.00 121.20 ?  301  LYS   D NZ    1 
ATOM   17479 N  N     . ASP   D 2 303 ? 112.572 163.706 100.111 1.00 117.03 ?  302  ASP   D N     1 
ATOM   17480 C  CA    . ASP   D 2 303 ? 114.023 163.849 100.077 1.00 116.61 ?  302  ASP   D CA    1 
ATOM   17481 C  C     . ASP   D 2 303 ? 114.713 162.702 100.806 1.00 118.06 ?  302  ASP   D C     1 
ATOM   17482 O  O     . ASP   D 2 303 ? 115.510 161.965 100.214 1.00 121.19 ?  302  ASP   D O     1 
ATOM   17483 C  CB    . ASP   D 2 303 ? 114.427 165.194 100.684 1.00 117.05 ?  302  ASP   D CB    1 
ATOM   17484 C  CG    . ASP   D 2 303 ? 114.127 166.361 99.764  1.00 122.90 ?  302  ASP   D CG    1 
ATOM   17485 O  OD1   . ASP   D 2 303 ? 114.123 166.161 98.530  1.00 124.75 ?  302  ASP   D OD1   1 
ATOM   17486 O  OD2   . ASP   D 2 303 ? 113.895 167.478 100.272 1.00 124.02 ?  302  ASP   D OD2   1 
ATOM   17487 N  N     . ILE   D 2 304 ? 114.415 162.539 102.097 1.00 113.72 ?  303  ILE   D N     1 
ATOM   17488 C  CA    . ILE   D 2 304 ? 115.128 161.554 102.903 1.00 113.19 ?  303  ILE   D CA    1 
ATOM   17489 C  C     . ILE   D 2 304 ? 114.827 160.141 102.429 1.00 114.52 ?  303  ILE   D C     1 
ATOM   17490 O  O     . ILE   D 2 304 ? 115.700 159.267 102.473 1.00 117.18 ?  303  ILE   D O     1 
ATOM   17491 C  CB    . ILE   D 2 304 ? 114.799 161.738 104.396 1.00 113.02 ?  303  ILE   D CB    1 
ATOM   17492 C  CG1   . ILE   D 2 304 ? 113.288 161.783 104.619 1.00 113.52 ?  303  ILE   D CG1   1 
ATOM   17493 C  CG2   . ILE   D 2 304 ? 115.452 163.002 104.935 1.00 114.72 ?  303  ILE   D CG2   1 
ATOM   17494 C  CD1   . ILE   D 2 304 ? 112.900 161.921 106.072 1.00 113.44 ?  303  ILE   D CD1   1 
ATOM   17495 N  N     . LEU   D 2 305 ? 113.602 159.887 101.963 1.00 106.63 ?  304  LEU   D N     1 
ATOM   17496 C  CA    . LEU   D 2 305 ? 113.290 158.566 101.430 1.00 105.35 ?  304  LEU   D CA    1 
ATOM   17497 C  C     . LEU   D 2 305 ? 114.063 158.289 100.147 1.00 106.24 ?  304  LEU   D C     1 
ATOM   17498 O  O     . LEU   D 2 305 ? 114.517 157.162 99.928  1.00 108.76 ?  304  LEU   D O     1 
ATOM   17499 C  CB    . LEU   D 2 305 ? 111.789 158.425 101.201 1.00 103.98 ?  304  LEU   D CB    1 
ATOM   17500 C  CG    . LEU   D 2 305 ? 111.304 156.981 101.062 1.00 105.20 ?  304  LEU   D CG    1 
ATOM   17501 C  CD1   . LEU   D 2 305 ? 111.658 156.183 102.305 1.00 105.12 ?  304  LEU   D CD1   1 
ATOM   17502 C  CD2   . LEU   D 2 305 ? 109.810 156.928 100.805 1.00 107.80 ?  304  LEU   D CD2   1 
ATOM   17503 N  N     . CYS   D 2 306 ? 114.240 159.304 99.294  1.00 109.32 ?  305  CYS   D N     1 
ATOM   17504 C  CA    . CYS   D 2 306 ? 115.060 159.123 98.099  1.00 107.59 ?  305  CYS   D CA    1 
ATOM   17505 C  C     . CYS   D 2 306 ? 116.515 158.854 98.464  1.00 108.97 ?  305  CYS   D C     1 
ATOM   17506 O  O     . CYS   D 2 306 ? 117.179 158.016 97.838  1.00 111.43 ?  305  CYS   D O     1 
ATOM   17507 C  CB    . CYS   D 2 306 ? 114.945 160.351 97.197  1.00 107.80 ?  305  CYS   D CB    1 
ATOM   17508 S  SG    . CYS   D 2 306 ? 113.508 160.331 96.102  1.00 113.50 ?  305  CYS   D SG    1 
ATOM   17509 N  N     . GLN   D 2 307 ? 117.028 159.560 99.475  1.00 108.18 ?  306  GLN   D N     1 
ATOM   17510 C  CA    . GLN   D 2 307 ? 118.382 159.287 99.951  1.00 106.57 ?  306  GLN   D CA    1 
ATOM   17511 C  C     . GLN   D 2 307 ? 118.500 157.860 100.467 1.00 107.45 ?  306  GLN   D C     1 
ATOM   17512 O  O     . GLN   D 2 307 ? 119.507 157.184 100.227 1.00 110.88 ?  306  GLN   D O     1 
ATOM   17513 C  CB    . GLN   D 2 307 ? 118.780 160.274 101.049 1.00 109.54 ?  306  GLN   D CB    1 
ATOM   17514 C  CG    . GLN   D 2 307 ? 118.410 161.718 100.780 1.00 111.72 ?  306  GLN   D CG    1 
ATOM   17515 C  CD    . GLN   D 2 307 ? 119.182 162.696 101.641 1.00 113.79 ?  306  GLN   D CD    1 
ATOM   17516 O  OE1   . GLN   D 2 307 ? 120.329 162.446 102.006 1.00 114.28 ?  306  GLN   D OE1   1 
ATOM   17517 N  NE2   . GLN   D 2 307 ? 118.555 163.822 101.965 1.00 110.85 ?  306  GLN   D NE2   1 
ATOM   17518 N  N     . TYR   D 2 308 ? 117.481 157.390 101.191 1.00 101.53 ?  307  TYR   D N     1 
ATOM   17519 C  CA    . TYR   D 2 308 ? 117.485 156.016 101.680 1.00 102.64 ?  307  TYR   D CA    1 
ATOM   17520 C  C     . TYR   D 2 308 ? 117.462 155.020 100.529 1.00 102.88 ?  307  TYR   D C     1 
ATOM   17521 O  O     . TYR   D 2 308 ? 118.132 153.984 100.585 1.00 106.74 ?  307  TYR   D O     1 
ATOM   17522 C  CB    . TYR   D 2 308 ? 116.295 155.783 102.609 1.00 101.99 ?  307  TYR   D CB    1 
ATOM   17523 C  CG    . TYR   D 2 308 ? 116.221 154.375 103.153 1.00 102.75 ?  307  TYR   D CG    1 
ATOM   17524 C  CD1   . TYR   D 2 308 ? 117.261 153.844 103.904 1.00 102.23 ?  307  TYR   D CD1   1 
ATOM   17525 C  CD2   . TYR   D 2 308 ? 115.111 153.577 102.918 1.00 98.58  ?  307  TYR   D CD2   1 
ATOM   17526 C  CE1   . TYR   D 2 308 ? 117.197 152.559 104.404 1.00 102.02 ?  307  TYR   D CE1   1 
ATOM   17527 C  CE2   . TYR   D 2 308 ? 115.037 152.292 103.414 1.00 99.82  ?  307  TYR   D CE2   1 
ATOM   17528 C  CZ    . TYR   D 2 308 ? 116.083 151.788 104.156 1.00 103.99 ?  307  TYR   D CZ    1 
ATOM   17529 O  OH    . TYR   D 2 308 ? 116.015 150.507 104.651 1.00 106.98 ?  307  TYR   D OH    1 
ATOM   17530 N  N     . VAL   D 2 309 ? 116.683 155.310 99.485  1.00 97.71  ?  308  VAL   D N     1 
ATOM   17531 C  CA    . VAL   D 2 309 ? 116.652 154.436 98.313  1.00 91.86  ?  308  VAL   D CA    1 
ATOM   17532 C  C     . VAL   D 2 309 ? 118.034 154.355 97.682  1.00 93.60  ?  308  VAL   D C     1 
ATOM   17533 O  O     . VAL   D 2 309 ? 118.527 153.268 97.360  1.00 98.41  ?  308  VAL   D O     1 
ATOM   17534 C  CB    . VAL   D 2 309 ? 115.603 154.926 97.297  1.00 91.62  ?  308  VAL   D CB    1 
ATOM   17535 C  CG1   . VAL   D 2 309 ? 115.696 154.119 96.012  1.00 92.96  ?  308  VAL   D CG1   1 
ATOM   17536 C  CG2   . VAL   D 2 309 ? 114.210 154.823 97.879  1.00 97.87  ?  308  VAL   D CG2   1 
ATOM   17537 N  N     . GLU   D 2 310 ? 118.684 155.508 97.506  1.00 105.24 ?  309  GLU   D N     1 
ATOM   17538 C  CA    . GLU   D 2 310 ? 120.014 155.518 96.902  1.00 105.76 ?  309  GLU   D CA    1 
ATOM   17539 C  C     . GLU   D 2 310 ? 121.015 154.756 97.761  1.00 103.95 ?  309  GLU   D C     1 
ATOM   17540 O  O     . GLU   D 2 310 ? 121.821 153.971 97.244  1.00 105.71 ?  309  GLU   D O     1 
ATOM   17541 C  CB    . GLU   D 2 310 ? 120.475 156.956 96.677  1.00 107.08 ?  309  GLU   D CB    1 
ATOM   17542 C  CG    . GLU   D 2 310 ? 119.725 157.660 95.562  1.00 109.60 ?  309  GLU   D CG    1 
ATOM   17543 C  CD    . GLU   D 2 310 ? 120.418 158.917 95.082  1.00 112.32 ?  309  GLU   D CD    1 
ATOM   17544 O  OE1   . GLU   D 2 310 ? 121.361 159.377 95.759  1.00 113.21 ?  309  GLU   D OE1   1 
ATOM   17545 O  OE2   . GLU   D 2 310 ? 120.017 159.448 94.024  1.00 111.35 ?  309  GLU   D OE2   1 
ATOM   17546 N  N     . TYR   D 2 311 ? 120.963 154.956 99.077  1.00 101.86 ?  310  TYR   D N     1 
ATOM   17547 C  CA    . TYR   D 2 311 ? 121.860 154.237 99.973  1.00 102.07 ?  310  TYR   D CA    1 
ATOM   17548 C  C     . TYR   D 2 311 ? 121.636 152.732 99.872  1.00 102.61 ?  310  TYR   D C     1 
ATOM   17549 O  O     . TYR   D 2 311 ? 122.575 151.969 99.618  1.00 105.76 ?  310  TYR   D O     1 
ATOM   17550 C  CB    . TYR   D 2 311 ? 121.658 154.744 101.405 1.00 101.26 ?  310  TYR   D CB    1 
ATOM   17551 C  CG    . TYR   D 2 311 ? 122.148 153.828 102.505 1.00 101.40 ?  310  TYR   D CG    1 
ATOM   17552 C  CD1   . TYR   D 2 311 ? 123.480 153.826 102.893 1.00 103.00 ?  310  TYR   D CD1   1 
ATOM   17553 C  CD2   . TYR   D 2 311 ? 121.271 152.987 103.176 1.00 102.35 ?  310  TYR   D CD2   1 
ATOM   17554 C  CE1   . TYR   D 2 311 ? 123.930 152.996 103.903 1.00 103.63 ?  310  TYR   D CE1   1 
ATOM   17555 C  CE2   . TYR   D 2 311 ? 121.712 152.154 104.186 1.00 104.37 ?  310  TYR   D CE2   1 
ATOM   17556 C  CZ    . TYR   D 2 311 ? 123.042 152.162 104.545 1.00 105.13 ?  310  TYR   D CZ    1 
ATOM   17557 O  OH    . TYR   D 2 311 ? 123.487 151.336 105.550 1.00 107.24 ?  310  TYR   D OH    1 
ATOM   17558 N  N     . ILE   D 2 312 ? 120.386 152.289 100.018 1.00 94.82  ?  311  ILE   D N     1 
ATOM   17559 C  CA    . ILE   D 2 312 ? 120.118 150.856 100.045 1.00 91.55  ?  311  ILE   D CA    1 
ATOM   17560 C  C     . ILE   D 2 312 ? 120.478 150.218 98.709  1.00 92.01  ?  311  ILE   D C     1 
ATOM   17561 O  O     . ILE   D 2 312 ? 121.029 149.113 98.672  1.00 94.89  ?  311  ILE   D O     1 
ATOM   17562 C  CB    . ILE   D 2 312 ? 118.657 150.577 100.453 1.00 92.23  ?  311  ILE   D CB    1 
ATOM   17563 C  CG1   . ILE   D 2 312 ? 118.476 149.095 100.787 1.00 92.44  ?  311  ILE   D CG1   1 
ATOM   17564 C  CG2   . ILE   D 2 312 ? 117.679 150.999 99.371  1.00 93.77  ?  311  ILE   D CG2   1 
ATOM   17565 C  CD1   . ILE   D 2 312 ? 119.116 148.684 102.094 1.00 92.37  ?  311  ILE   D CD1   1 
ATOM   17566 N  N     . THR   D 2 313 ? 120.229 150.914 97.593  1.00 93.59  ?  312  THR   D N     1 
ATOM   17567 C  CA    . THR   D 2 313 ? 120.560 150.315 96.306  1.00 93.63  ?  312  THR   D CA    1 
ATOM   17568 C  C     . THR   D 2 313 ? 122.065 150.287 96.069  1.00 93.52  ?  312  THR   D C     1 
ATOM   17569 O  O     . THR   D 2 313 ? 122.565 149.340 95.461  1.00 99.49  ?  312  THR   D O     1 
ATOM   17570 C  CB    . THR   D 2 313 ? 119.839 151.033 95.162  1.00 94.42  ?  312  THR   D CB    1 
ATOM   17571 O  OG1   . THR   D 2 313 ? 120.052 150.317 93.939  1.00 97.28  ?  312  THR   D OG1   1 
ATOM   17572 C  CG2   . THR   D 2 313 ? 120.350 152.432 94.990  1.00 96.67  ?  312  THR   D CG2   1 
ATOM   17573 N  N     . ASN   D 2 314 ? 122.808 151.282 96.566  1.00 96.87  ?  313  ASN   D N     1 
ATOM   17574 C  CA    . ASN   D 2 314 ? 124.265 151.212 96.488  1.00 96.10  ?  313  ASN   D CA    1 
ATOM   17575 C  C     . ASN   D 2 314 ? 124.788 149.994 97.236  1.00 98.33  ?  313  ASN   D C     1 
ATOM   17576 O  O     . ASN   D 2 314 ? 125.584 149.207 96.702  1.00 102.16 ?  313  ASN   D O     1 
ATOM   17577 C  CB    . ASN   D 2 314 ? 124.881 152.492 97.055  1.00 99.53  ?  313  ASN   D CB    1 
ATOM   17578 C  CG    . ASN   D 2 314 ? 125.360 153.438 95.975  1.00 101.90 ?  313  ASN   D CG    1 
ATOM   17579 O  OD1   . ASN   D 2 314 ? 124.766 153.526 94.902  1.00 103.77 ?  313  ASN   D OD1   1 
ATOM   17580 N  ND2   . ASN   D 2 314 ? 126.439 154.157 96.256  1.00 103.19 ?  313  ASN   D ND2   1 
ATOM   17581 N  N     . ILE   D 2 315 ? 124.316 149.804 98.470  1.00 94.20  ?  314  ILE   D N     1 
ATOM   17582 C  CA    . ILE   D 2 315 ? 124.808 148.698 99.289  1.00 92.32  ?  314  ILE   D CA    1 
ATOM   17583 C  C     . ILE   D 2 315 ? 124.411 147.353 98.673  1.00 93.96  ?  314  ILE   D C     1 
ATOM   17584 O  O     . ILE   D 2 315 ? 125.220 146.420 98.629  1.00 94.94  ?  314  ILE   D O     1 
ATOM   17585 C  CB    . ILE   D 2 315 ? 124.323 148.833 100.749 1.00 91.73  ?  314  ILE   D CB    1 
ATOM   17586 C  CG1   . ILE   D 2 315 ? 125.017 149.982 101.513 1.00 95.18  ?  314  ILE   D CG1   1 
ATOM   17587 C  CG2   . ILE   D 2 315 ? 124.618 147.548 101.519 1.00 92.26  ?  314  ILE   D CG2   1 
ATOM   17588 C  CD1   . ILE   D 2 315 ? 124.961 151.373 100.931 1.00 95.17  ?  314  ILE   D CD1   1 
ATOM   17589 N  N     . ARG   D 2 316 ? 123.183 147.234 98.153  1.00 92.23  ?  315  ARG   D N     1 
ATOM   17590 C  CA    . ARG   D 2 316 ? 122.752 145.961 97.581  1.00 87.16  ?  315  ARG   D CA    1 
ATOM   17591 C  C     . ARG   D 2 316 ? 123.285 145.722 96.175  1.00 87.61  ?  315  ARG   D C     1 
ATOM   17592 O  O     . ARG   D 2 316 ? 123.232 144.584 95.696  1.00 90.39  ?  315  ARG   D O     1 
ATOM   17593 C  CB    . ARG   D 2 316 ? 121.228 145.872 97.578  1.00 82.81  ?  315  ARG   D CB    1 
ATOM   17594 C  CG    . ARG   D 2 316 ? 120.637 146.116 98.942  1.00 85.90  ?  315  ARG   D CG    1 
ATOM   17595 C  CD    . ARG   D 2 316 ? 120.491 144.841 99.737  1.00 85.95  ?  315  ARG   D CD    1 
ATOM   17596 N  NE    . ARG   D 2 316 ? 119.511 145.008 100.799 1.00 85.74  ?  315  ARG   D NE    1 
ATOM   17597 C  CZ    . ARG   D 2 316 ? 119.827 145.027 102.085 1.00 89.90  ?  315  ARG   D CZ    1 
ATOM   17598 N  NH1   . ARG   D 2 316 ? 121.082 144.914 102.484 1.00 90.54  ?  315  ARG   D NH1   1 
ATOM   17599 N  NH2   . ARG   D 2 316 ? 118.865 145.161 102.990 1.00 91.68  ?  315  ARG   D NH2   1 
ATOM   17600 N  N     . MET   D 2 317 ? 123.793 146.753 95.505  1.00 100.99 ?  316  MET   D N     1 
ATOM   17601 C  CA    . MET   D 2 317 ? 124.413 146.569 94.204  1.00 98.35  ?  316  MET   D CA    1 
ATOM   17602 C  C     . MET   D 2 317 ? 125.892 146.248 94.310  1.00 99.59  ?  316  MET   D C     1 
ATOM   17603 O  O     . MET   D 2 317 ? 126.426 145.561 93.433  1.00 102.02 ?  316  MET   D O     1 
ATOM   17604 C  CB    . MET   D 2 317 ? 124.220 147.819 93.346  1.00 97.35  ?  316  MET   D CB    1 
ATOM   17605 C  CG    . MET   D 2 317 ? 122.827 147.975 92.773  1.00 101.24 ?  316  MET   D CG    1 
ATOM   17606 S  SD    . MET   D 2 317 ? 122.796 148.984 91.283  1.00 110.17 ?  316  MET   D SD    1 
ATOM   17607 C  CE    . MET   D 2 317 ? 124.529 149.008 90.871  1.00 102.38 ?  316  MET   D CE    1 
ATOM   17608 N  N     . GLN   D 2 318 ? 126.558 146.723 95.369  1.00 99.39  ?  317  GLN   D N     1 
ATOM   17609 C  CA    . GLN   D 2 318 ? 127.924 146.286 95.633  1.00 98.00  ?  317  GLN   D CA    1 
ATOM   17610 C  C     . GLN   D 2 318 ? 127.974 144.788 95.910  1.00 101.64 ?  317  GLN   D C     1 
ATOM   17611 O  O     . GLN   D 2 318 ? 128.919 144.102 95.501  1.00 103.10 ?  317  GLN   D O     1 
ATOM   17612 C  CB    . GLN   D 2 318 ? 128.510 147.066 96.810  1.00 101.13 ?  317  GLN   D CB    1 
ATOM   17613 C  CG    . GLN   D 2 318 ? 129.981 146.772 97.058  1.00 103.33 ?  317  GLN   D CG    1 
ATOM   17614 C  CD    . GLN   D 2 318 ? 130.597 147.666 98.110  1.00 107.25 ?  317  GLN   D CD    1 
ATOM   17615 O  OE1   . GLN   D 2 318 ? 129.957 148.588 98.613  1.00 107.43 ?  317  GLN   D OE1   1 
ATOM   17616 N  NE2   . GLN   D 2 318 ? 131.850 147.395 98.450  1.00 105.49 ?  317  GLN   D NE2   1 
ATOM   17617 N  N     . ALA   D 2 319 ? 126.959 144.260 96.599  1.00 95.17  ?  318  ALA   D N     1 
ATOM   17618 C  CA    . ALA   D 2 319 ? 126.989 142.865 97.028  1.00 92.91  ?  318  ALA   D CA    1 
ATOM   17619 C  C     . ALA   D 2 319 ? 126.990 141.889 95.856  1.00 93.90  ?  318  ALA   D C     1 
ATOM   17620 O  O     . ALA   D 2 319 ? 127.503 140.772 95.986  1.00 96.39  ?  318  ALA   D O     1 
ATOM   17621 C  CB    . ALA   D 2 319 ? 125.809 142.577 97.954  1.00 89.09  ?  318  ALA   D CB    1 
ATOM   17622 N  N     . VAL   D 2 320 ? 126.431 142.274 94.711  1.00 91.54  ?  319  VAL   D N     1 
ATOM   17623 C  CA    . VAL   D 2 320 ? 126.344 141.365 93.573  1.00 89.73  ?  319  VAL   D CA    1 
ATOM   17624 C  C     . VAL   D 2 320 ? 127.313 141.800 92.482  1.00 92.01  ?  319  VAL   D C     1 
ATOM   17625 O  O     . VAL   D 2 320 ? 127.070 141.565 91.293  1.00 94.10  ?  319  VAL   D O     1 
ATOM   17626 C  CB    . VAL   D 2 320 ? 124.906 141.293 93.031  1.00 87.35  ?  319  VAL   D CB    1 
ATOM   17627 C  CG1   . VAL   D 2 320 ? 124.067 140.343 93.870  1.00 85.50  ?  319  VAL   D CG1   1 
ATOM   17628 C  CG2   . VAL   D 2 320 ? 124.273 142.675 93.003  1.00 88.04  ?  319  VAL   D CG2   1 
ATOM   17629 N  N     . GLY   D 2 321 ? 128.390 142.475 92.875  1.00 103.64 ?  320  GLY   D N     1 
ATOM   17630 C  CA    . GLY   D 2 321 ? 129.449 142.824 91.948  1.00 102.88 ?  320  GLY   D CA    1 
ATOM   17631 C  C     . GLY   D 2 321 ? 129.064 143.779 90.837  1.00 105.46 ?  320  GLY   D C     1 
ATOM   17632 O  O     . GLY   D 2 321 ? 129.364 143.526 89.667  1.00 106.19 ?  320  GLY   D O     1 
ATOM   17633 N  N     . LEU   D 2 322 ? 128.399 144.878 91.182  1.00 98.04  ?  321  LEU   D N     1 
ATOM   17634 C  CA    . LEU   D 2 322 ? 127.992 145.882 90.211  1.00 95.99  ?  321  LEU   D CA    1 
ATOM   17635 C  C     . LEU   D 2 322 ? 128.521 147.252 90.620  1.00 101.22 ?  321  LEU   D C     1 
ATOM   17636 O  O     . LEU   D 2 322 ? 128.678 147.546 91.808  1.00 101.35 ?  321  LEU   D O     1 
ATOM   17637 C  CB    . LEU   D 2 322 ? 126.467 145.926 90.069  1.00 97.10  ?  321  LEU   D CB    1 
ATOM   17638 C  CG    . LEU   D 2 322 ? 125.831 144.778 89.285  1.00 95.25  ?  321  LEU   D CG    1 
ATOM   17639 C  CD1   . LEU   D 2 322 ? 124.325 144.759 89.483  1.00 96.25  ?  321  LEU   D CD1   1 
ATOM   17640 C  CD2   . LEU   D 2 322 ? 126.177 144.882 87.809  1.00 97.88  ?  321  LEU   D CD2   1 
ATOM   17641 N  N     . ASP   D 2 323 ? 128.800 148.085 89.618  1.00 123.16 ?  322  ASP   D N     1 
ATOM   17642 C  CA    . ASP   D 2 323 ? 129.369 149.405 89.866  1.00 122.40 ?  322  ASP   D CA    1 
ATOM   17643 C  C     . ASP   D 2 323 ? 128.332 150.327 90.497  1.00 122.77 ?  322  ASP   D C     1 
ATOM   17644 O  O     . ASP   D 2 323 ? 127.204 150.432 90.009  1.00 124.53 ?  322  ASP   D O     1 
ATOM   17645 C  CB    . ASP   D 2 323 ? 129.883 150.008 88.561  1.00 121.62 ?  322  ASP   D CB    1 
ATOM   17646 C  CG    . ASP   D 2 323 ? 130.972 149.173 87.921  1.00 124.82 ?  322  ASP   D CG    1 
ATOM   17647 O  OD1   . ASP   D 2 323 ? 131.583 148.346 88.627  1.00 123.38 ?  322  ASP   D OD1   1 
ATOM   17648 O  OD2   . ASP   D 2 323 ? 131.218 149.348 86.707  1.00 126.52 ?  322  ASP   D OD2   1 
ATOM   17649 N  N     . LEU   D 2 324 ? 128.720 151.004 91.573  1.00 112.81 ?  323  LEU   D N     1 
ATOM   17650 C  CA    . LEU   D 2 324 ? 127.777 151.817 92.331  1.00 111.69 ?  323  LEU   D CA    1 
ATOM   17651 C  C     . LEU   D 2 324 ? 127.255 152.966 91.472  1.00 111.06 ?  323  LEU   D C     1 
ATOM   17652 O  O     . LEU   D 2 324 ? 128.053 153.702 90.876  1.00 113.56 ?  323  LEU   D O     1 
ATOM   17653 C  CB    . LEU   D 2 324 ? 128.442 152.362 93.592  1.00 110.42 ?  323  LEU   D CB    1 
ATOM   17654 C  CG    . LEU   D 2 324 ? 129.051 151.348 94.561  1.00 109.84 ?  323  LEU   D CG    1 
ATOM   17655 C  CD1   . LEU   D 2 324 ? 129.059 151.901 95.978  1.00 110.91 ?  323  LEU   D CD1   1 
ATOM   17656 C  CD2   . LEU   D 2 324 ? 128.302 150.027 94.506  1.00 110.73 ?  323  LEU   D CD2   1 
ATOM   17657 N  N     . PRO   D 2 325 ? 125.939 153.143 91.367  1.00 110.07 ?  324  PRO   D N     1 
ATOM   17658 C  CA    . PRO   D 2 325 ? 125.381 154.201 90.519  1.00 110.68 ?  324  PRO   D CA    1 
ATOM   17659 C  C     . PRO   D 2 325 ? 125.129 155.525 91.222  1.00 111.29 ?  324  PRO   D C     1 
ATOM   17660 O  O     . PRO   D 2 325 ? 124.657 156.461 90.568  1.00 112.05 ?  324  PRO   D O     1 
ATOM   17661 C  CB    . PRO   D 2 325 ? 124.053 153.579 90.072  1.00 109.87 ?  324  PRO   D CB    1 
ATOM   17662 C  CG    . PRO   D 2 325 ? 123.624 152.768 91.257  1.00 108.33 ?  324  PRO   D CG    1 
ATOM   17663 C  CD    . PRO   D 2 325 ? 124.885 152.298 91.954  1.00 110.05 ?  324  PRO   D CD    1 
ATOM   17664 N  N     . PHE   D 2 326 ? 125.370 155.615 92.528  1.00 111.25 ?  325  PHE   D N     1 
ATOM   17665 C  CA    . PHE   D 2 326 ? 125.146 156.834 93.290  1.00 111.87 ?  325  PHE   D CA    1 
ATOM   17666 C  C     . PHE   D 2 326 ? 126.364 157.122 94.156  1.00 113.26 ?  325  PHE   D C     1 
ATOM   17667 O  O     . PHE   D 2 326 ? 127.227 156.265 94.361  1.00 113.85 ?  325  PHE   D O     1 
ATOM   17668 C  CB    . PHE   D 2 326 ? 123.888 156.739 94.172  1.00 109.96 ?  325  PHE   D CB    1 
ATOM   17669 C  CG    . PHE   D 2 326 ? 122.627 156.459 93.403  1.00 111.17 ?  325  PHE   D CG    1 
ATOM   17670 C  CD1   . PHE   D 2 326 ? 122.169 157.350 92.450  1.00 112.50 ?  325  PHE   D CD1   1 
ATOM   17671 C  CD2   . PHE   D 2 326 ? 121.936 155.276 93.589  1.00 111.00 ?  325  PHE   D CD2   1 
ATOM   17672 C  CE1   . PHE   D 2 326 ? 121.013 157.086 91.734  1.00 111.59 ?  325  PHE   D CE1   1 
ATOM   17673 C  CE2   . PHE   D 2 326 ? 120.779 155.013 92.883  1.00 110.00 ?  325  PHE   D CE2   1 
ATOM   17674 C  CZ    . PHE   D 2 326 ? 120.320 155.914 91.953  1.00 110.19 ?  325  PHE   D CZ    1 
ATOM   17675 N  N     . GLN   D 2 327 ? 126.428 158.352 94.656  1.00 123.64 ?  326  GLN   D N     1 
ATOM   17676 C  CA    . GLN   D 2 327 ? 127.518 158.751 95.533  1.00 122.91 ?  326  GLN   D CA    1 
ATOM   17677 C  C     . GLN   D 2 327 ? 127.413 158.040 96.877  1.00 124.43 ?  326  GLN   D C     1 
ATOM   17678 O  O     . GLN   D 2 327 ? 126.320 157.735 97.362  1.00 124.50 ?  326  GLN   D O     1 
ATOM   17679 C  CB    . GLN   D 2 327 ? 127.507 160.264 95.740  1.00 123.95 ?  326  GLN   D CB    1 
ATOM   17680 C  CG    . GLN   D 2 327 ? 126.200 160.797 96.299  1.00 125.86 ?  326  GLN   D CG    1 
ATOM   17681 C  CD    . GLN   D 2 327 ? 126.194 162.306 96.431  1.00 127.38 ?  326  GLN   D CD    1 
ATOM   17682 O  OE1   . GLN   D 2 327 ? 127.014 162.882 97.145  1.00 127.43 ?  326  GLN   D OE1   1 
ATOM   17683 N  NE2   . GLN   D 2 327 ? 125.265 162.957 95.739  1.00 125.34 ?  326  GLN   D NE2   1 
ATOM   17684 N  N     . THR   D 2 328 ? 128.570 157.774 97.478  1.00 128.05 ?  327  THR   D N     1 
ATOM   17685 C  CA    . THR   D 2 328 ? 128.603 157.137 98.787  1.00 129.14 ?  327  THR   D CA    1 
ATOM   17686 C  C     . THR   D 2 328 ? 128.030 158.078 99.839  1.00 128.18 ?  327  THR   D C     1 
ATOM   17687 O  O     . THR   D 2 328 ? 128.387 159.259 99.893  1.00 127.58 ?  327  THR   D O     1 
ATOM   17688 C  CB    . THR   D 2 328 ? 130.033 156.741 99.150  1.00 128.45 ?  327  THR   D CB    1 
ATOM   17689 O  OG1   . THR   D 2 328 ? 130.550 155.849 98.155  1.00 127.75 ?  327  THR   D OG1   1 
ATOM   17690 C  CG2   . THR   D 2 328 ? 130.069 156.052 100.506 1.00 125.49 ?  327  THR   D CG2   1 
ATOM   17691 N  N     . ARG   D 2 329 ? 127.137 157.553 100.673 1.00 130.46 ?  328  ARG   D N     1 
ATOM   17692 C  CA    . ARG   D 2 329 ? 126.477 158.354 101.693 1.00 129.84 ?  328  ARG   D CA    1 
ATOM   17693 C  C     . ARG   D 2 329 ? 125.967 157.423 102.782 1.00 130.63 ?  328  ARG   D C     1 
ATOM   17694 O  O     . ARG   D 2 329 ? 125.488 156.325 102.489 1.00 132.43 ?  328  ARG   D O     1 
ATOM   17695 C  CB    . ARG   D 2 329 ? 125.329 159.174 101.090 1.00 130.56 ?  328  ARG   D CB    1 
ATOM   17696 C  CG    . ARG   D 2 329 ? 124.365 159.772 102.103 1.00 130.76 ?  328  ARG   D CG    1 
ATOM   17697 C  CD    . ARG   D 2 329 ? 123.302 160.608 101.412 1.00 132.47 ?  328  ARG   D CD    1 
ATOM   17698 N  NE    . ARG   D 2 329 ? 122.783 159.948 100.220 1.00 132.70 ?  328  ARG   D NE    1 
ATOM   17699 C  CZ    . ARG   D 2 329 ? 121.932 160.502 99.367  1.00 130.90 ?  328  ARG   D CZ    1 
ATOM   17700 N  NH1   . ARG   D 2 329 ? 121.481 161.733 99.542  1.00 130.25 ?  328  ARG   D NH1   1 
ATOM   17701 N  NH2   . ARG   D 2 329 ? 121.525 159.804 98.311  1.00 129.60 ?  328  ARG   D NH2   1 
ATOM   17702 N  N     . SER   D 2 330 ? 126.076 157.867 104.032 1.00 128.20 ?  329  SER   D N     1 
ATOM   17703 C  CA    . SER   D 2 330 ? 125.640 157.062 105.162 1.00 127.48 ?  329  SER   D CA    1 
ATOM   17704 C  C     . SER   D 2 330 ? 124.118 156.923 105.158 1.00 126.82 ?  329  SER   D C     1 
ATOM   17705 O  O     . SER   D 2 330 ? 123.409 157.516 104.341 1.00 127.27 ?  329  SER   D O     1 
ATOM   17706 C  CB    . SER   D 2 330 ? 126.130 157.679 106.470 1.00 127.05 ?  329  SER   D CB    1 
ATOM   17707 O  OG    . SER   D 2 330 ? 125.881 159.074 106.501 1.00 126.95 ?  329  SER   D OG    1 
ATOM   17708 N  N     . ASN   D 2 331 ? 123.614 156.123 106.086 1.00 115.67 ?  330  ASN   D N     1 
ATOM   17709 C  CA    . ASN   D 2 331 ? 122.178 155.886 106.178 1.00 115.47 ?  330  ASN   D CA    1 
ATOM   17710 C  C     . ASN   D 2 331 ? 121.485 157.159 106.641 1.00 115.92 ?  330  ASN   D C     1 
ATOM   17711 O  O     . ASN   D 2 331 ? 121.778 157.649 107.740 1.00 114.19 ?  330  ASN   D O     1 
ATOM   17712 C  CB    . ASN   D 2 331 ? 121.905 154.730 107.143 1.00 113.96 ?  330  ASN   D CB    1 
ATOM   17713 C  CG    . ASN   D 2 331 ? 120.425 154.402 107.280 1.00 117.21 ?  330  ASN   D CG    1 
ATOM   17714 O  OD1   . ASN   D 2 331 ? 119.568 155.036 106.668 1.00 119.28 ?  330  ASN   D OD1   1 
ATOM   17715 N  ND2   . ASN   D 2 331 ? 120.124 153.397 108.094 1.00 116.29 ?  330  ASN   D ND2   1 
ATOM   17716 N  N     . PRO   D 2 332 ? 120.577 157.732 105.848 1.00 113.95 ?  331  PRO   D N     1 
ATOM   17717 C  CA    . PRO   D 2 332 ? 119.883 158.944 106.298 1.00 114.59 ?  331  PRO   D CA    1 
ATOM   17718 C  C     . PRO   D 2 332 ? 118.839 158.684 107.372 1.00 114.29 ?  331  PRO   D C     1 
ATOM   17719 O  O     . PRO   D 2 332 ? 118.315 159.649 107.939 1.00 116.15 ?  331  PRO   D O     1 
ATOM   17720 C  CB    . PRO   D 2 332 ? 119.234 159.477 105.011 1.00 113.98 ?  331  PRO   D CB    1 
ATOM   17721 C  CG    . PRO   D 2 332 ? 119.052 158.271 104.159 1.00 112.11 ?  331  PRO   D CG    1 
ATOM   17722 C  CD    . PRO   D 2 332 ? 120.182 157.333 104.485 1.00 112.45 ?  331  PRO   D CD    1 
ATOM   17723 N  N     . ILE   D 2 333 ? 118.432 157.434 107.586 1.00 110.22 ?  332  ILE   D N     1 
ATOM   17724 C  CA    . ILE   D 2 333 ? 117.426 157.106 108.598 1.00 109.30 ?  332  ILE   D CA    1 
ATOM   17725 C  C     . ILE   D 2 333 ? 117.977 155.998 109.491 1.00 111.49 ?  332  ILE   D C     1 
ATOM   17726 O  O     . ILE   D 2 333 ? 117.637 154.819 109.314 1.00 114.26 ?  332  ILE   D O     1 
ATOM   17727 C  CB    . ILE   D 2 333 ? 116.077 156.721 107.964 1.00 106.97 ?  332  ILE   D CB    1 
ATOM   17728 C  CG1   . ILE   D 2 333 ? 116.249 155.690 106.846 1.00 108.57 ?  332  ILE   D CG1   1 
ATOM   17729 C  CG2   . ILE   D 2 333 ? 115.384 157.957 107.409 1.00 108.79 ?  332  ILE   D CG2   1 
ATOM   17730 C  CD1   . ILE   D 2 333 ? 114.939 155.222 106.249 1.00 109.88 ?  332  ILE   D CD1   1 
ATOM   17731 N  N     . PRO   D 2 334 ? 118.851 156.324 110.445 1.00 112.59 ?  333  PRO   D N     1 
ATOM   17732 C  CA    . PRO   D 2 334 ? 119.438 155.274 111.294 1.00 111.34 ?  333  PRO   D CA    1 
ATOM   17733 C  C     . PRO   D 2 334 ? 118.426 154.532 112.150 1.00 112.44 ?  333  PRO   D C     1 
ATOM   17734 O  O     . PRO   D 2 334 ? 118.702 153.394 112.551 1.00 113.31 ?  333  PRO   D O     1 
ATOM   17735 C  CB    . PRO   D 2 334 ? 120.443 156.043 112.164 1.00 113.34 ?  333  PRO   D CB    1 
ATOM   17736 C  CG    . PRO   D 2 334 ? 120.678 157.337 111.442 1.00 113.43 ?  333  PRO   D CG    1 
ATOM   17737 C  CD    . PRO   D 2 334 ? 119.384 157.656 110.766 1.00 112.21 ?  333  PRO   D CD    1 
ATOM   17738 N  N     . TRP   D 2 335 ? 117.267 155.130 112.442 1.00 109.95 ?  334  TRP   D N     1 
ATOM   17739 C  CA    . TRP   D 2 335 ? 116.301 154.474 113.318 1.00 108.63 ?  334  TRP   D CA    1 
ATOM   17740 C  C     . TRP   D 2 335 ? 115.792 153.168 112.721 1.00 110.99 ?  334  TRP   D C     1 
ATOM   17741 O  O     . TRP   D 2 335 ? 115.432 152.246 113.463 1.00 114.20 ?  334  TRP   D O     1 
ATOM   17742 C  CB    . TRP   D 2 335 ? 115.131 155.413 113.621 1.00 107.79 ?  334  TRP   D CB    1 
ATOM   17743 C  CG    . TRP   D 2 335 ? 114.578 156.114 112.420 1.00 108.38 ?  334  TRP   D CG    1 
ATOM   17744 C  CD1   . TRP   D 2 335 ? 114.911 157.357 111.971 1.00 108.55 ?  334  TRP   D CD1   1 
ATOM   17745 C  CD2   . TRP   D 2 335 ? 113.582 155.616 111.518 1.00 111.31 ?  334  TRP   D CD2   1 
ATOM   17746 N  NE1   . TRP   D 2 335 ? 114.190 157.663 110.843 1.00 110.95 ?  334  TRP   D NE1   1 
ATOM   17747 C  CE2   . TRP   D 2 335 ? 113.366 156.610 110.544 1.00 111.43 ?  334  TRP   D CE2   1 
ATOM   17748 C  CE3   . TRP   D 2 335 ? 112.855 154.424 111.437 1.00 111.21 ?  334  TRP   D CE3   1 
ATOM   17749 C  CZ2   . TRP   D 2 335 ? 112.455 156.449 109.503 1.00 110.48 ?  334  TRP   D CZ2   1 
ATOM   17750 C  CZ3   . TRP   D 2 335 ? 111.952 154.267 110.403 1.00 110.60 ?  334  TRP   D CZ3   1 
ATOM   17751 C  CH2   . TRP   D 2 335 ? 111.760 155.273 109.450 1.00 109.86 ?  334  TRP   D CH2   1 
ATOM   17752 N  N     . ILE   D 2 336 ? 115.770 153.061 111.389 1.00 104.20 ?  335  ILE   D N     1 
ATOM   17753 C  CA    . ILE   D 2 336 ? 115.337 151.828 110.744 1.00 101.92 ?  335  ILE   D CA    1 
ATOM   17754 C  C     . ILE   D 2 336 ? 116.245 150.664 111.108 1.00 103.37 ?  335  ILE   D C     1 
ATOM   17755 O  O     . ILE   D 2 336 ? 115.845 149.503 110.978 1.00 106.56 ?  335  ILE   D O     1 
ATOM   17756 C  CB    . ILE   D 2 336 ? 115.263 152.010 109.213 1.00 102.37 ?  335  ILE   D CB    1 
ATOM   17757 C  CG1   . ILE   D 2 336 ? 114.284 151.003 108.607 1.00 104.42 ?  335  ILE   D CG1   1 
ATOM   17758 C  CG2   . ILE   D 2 336 ? 116.636 151.859 108.582 1.00 99.65  ?  335  ILE   D CG2   1 
ATOM   17759 C  CD1   . ILE   D 2 336 ? 114.069 151.179 107.127 1.00 102.90 ?  335  ILE   D CD1   1 
ATOM   17760 N  N     . ASN   D 2 337 ? 117.464 150.944 111.568 1.00 107.94 ?  336  ASN   D N     1 
ATOM   17761 C  CA    . ASN   D 2 337 ? 118.360 149.879 111.992 1.00 105.21 ?  336  ASN   D CA    1 
ATOM   17762 C  C     . ASN   D 2 337 ? 117.920 149.221 113.291 1.00 105.42 ?  336  ASN   D C     1 
ATOM   17763 O  O     . ASN   D 2 337 ? 118.440 148.152 113.624 1.00 109.11 ?  336  ASN   D O     1 
ATOM   17764 C  CB    . ASN   D 2 337 ? 119.782 150.421 112.132 1.00 105.89 ?  336  ASN   D CB    1 
ATOM   17765 C  CG    . ASN   D 2 337 ? 120.602 150.232 110.871 1.00 107.88 ?  336  ASN   D CG    1 
ATOM   17766 O  OD1   . ASN   D 2 337 ? 120.081 149.817 109.837 1.00 107.92 ?  336  ASN   D OD1   1 
ATOM   17767 N  ND2   . ASN   D 2 337 ? 121.893 150.537 110.950 1.00 110.62 ?  336  ASN   D ND2   1 
ATOM   17768 N  N     . THR   D 2 338 ? 116.994 149.828 114.028 1.00 102.95 ?  337  THR   D N     1 
ATOM   17769 C  CA    . THR   D 2 338 ? 116.403 149.210 115.205 1.00 103.20 ?  337  THR   D CA    1 
ATOM   17770 C  C     . THR   D 2 338 ? 115.142 148.428 114.869 1.00 103.98 ?  337  THR   D C     1 
ATOM   17771 O  O     . THR   D 2 338 ? 114.440 147.984 115.781 1.00 105.03 ?  337  THR   D O     1 
ATOM   17772 C  CB    . THR   D 2 338 ? 116.087 150.273 116.261 1.00 105.23 ?  337  THR   D CB    1 
ATOM   17773 O  OG1   . THR   D 2 338 ? 114.769 150.796 116.042 1.00 107.83 ?  337  THR   D OG1   1 
ATOM   17774 C  CG2   . THR   D 2 338 ? 117.096 151.415 116.192 1.00 103.94 ?  337  THR   D CG2   1 
ATOM   17775 N  N     . TRP   D 2 339 ? 114.822 148.288 113.581 1.00 98.34  ?  338  TRP   D N     1 
ATOM   17776 C  CA    . TRP   D 2 339 ? 113.649 147.556 113.136 1.00 95.30  ?  338  TRP   D CA    1 
ATOM   17777 C  C     . TRP   D 2 339 ? 113.969 146.432 112.162 1.00 99.97  ?  338  TRP   D C     1 
ATOM   17778 O  O     . TRP   D 2 339 ? 113.099 145.590 111.912 1.00 101.78 ?  338  TRP   D O     1 
ATOM   17779 C  CB    . TRP   D 2 339 ? 112.641 148.511 112.479 1.00 93.86  ?  338  TRP   D CB    1 
ATOM   17780 C  CG    . TRP   D 2 339 ? 111.812 149.276 113.457 1.00 98.02  ?  338  TRP   D CG    1 
ATOM   17781 C  CD1   . TRP   D 2 339 ? 111.969 150.581 113.822 1.00 98.38  ?  338  TRP   D CD1   1 
ATOM   17782 C  CD2   . TRP   D 2 339 ? 110.688 148.786 114.197 1.00 103.49 ?  338  TRP   D CD2   1 
ATOM   17783 N  NE1   . TRP   D 2 339 ? 111.015 150.933 114.745 1.00 100.59 ?  338  TRP   D NE1   1 
ATOM   17784 C  CE2   . TRP   D 2 339 ? 110.216 149.848 114.992 1.00 102.93 ?  338  TRP   D CE2   1 
ATOM   17785 C  CE3   . TRP   D 2 339 ? 110.035 147.552 114.264 1.00 100.39 ?  338  TRP   D CE3   1 
ATOM   17786 C  CZ2   . TRP   D 2 339 ? 109.124 149.713 115.846 1.00 97.23  ?  338  TRP   D CZ2   1 
ATOM   17787 C  CZ3   . TRP   D 2 339 ? 108.950 147.421 115.111 1.00 98.71  ?  338  TRP   D CZ3   1 
ATOM   17788 C  CH2   . TRP   D 2 339 ? 108.505 148.495 115.889 1.00 97.45  ?  338  TRP   D CH2   1 
ATOM   17789 N  N     . LEU   D 2 340 ? 115.177 146.392 111.609 1.00 98.52  ?  339  LEU   D N     1 
ATOM   17790 C  CA    . LEU   D 2 340 ? 115.555 145.357 110.655 1.00 96.44  ?  339  LEU   D CA    1 
ATOM   17791 C  C     . LEU   D 2 340 ? 116.406 144.281 111.319 1.00 98.26  ?  339  LEU   D C     1 
ATOM   17792 O  O     . LEU   D 2 340 ? 117.141 144.556 112.267 1.00 96.41  ?  339  LEU   D O     1 
ATOM   17793 C  CB    . LEU   D 2 340 ? 116.309 145.970 109.473 1.00 96.60  ?  339  LEU   D CB    1 
ATOM   17794 C  CG    . LEU   D 2 340 ? 115.596 147.089 108.711 1.00 95.56  ?  339  LEU   D CG    1 
ATOM   17795 C  CD1   . LEU   D 2 340 ? 116.513 147.689 107.659 1.00 94.00  ?  339  LEU   D CD1   1 
ATOM   17796 C  CD2   . LEU   D 2 340 ? 114.314 146.576 108.077 1.00 94.66  ?  339  LEU   D CD2   1 
ATOM   17797 N  N     . GLN   D 2 361 ? 135.765 113.429 97.746  1.00 139.16 ?  360  GLN   D N     1 
ATOM   17798 C  CA    . GLN   D 2 361 ? 137.081 113.973 97.435  1.00 141.06 ?  360  GLN   D CA    1 
ATOM   17799 C  C     . GLN   D 2 361 ? 138.186 113.040 97.917  1.00 140.93 ?  360  GLN   D C     1 
ATOM   17800 O  O     . GLN   D 2 361 ? 139.352 113.425 97.978  1.00 139.14 ?  360  GLN   D O     1 
ATOM   17801 C  CB    . GLN   D 2 361 ? 137.253 115.357 98.065  1.00 140.61 ?  360  GLN   D CB    1 
ATOM   17802 C  CG    . GLN   D 2 361 ? 136.570 115.514 99.414  1.00 140.29 ?  360  GLN   D CG    1 
ATOM   17803 C  CD    . GLN   D 2 361 ? 136.740 116.904 99.995  1.00 141.93 ?  360  GLN   D CD    1 
ATOM   17804 O  OE1   . GLN   D 2 361 ? 135.853 117.749 99.885  1.00 142.82 ?  360  GLN   D OE1   1 
ATOM   17805 N  NE2   . GLN   D 2 361 ? 137.886 117.147 100.621 1.00 141.36 ?  360  GLN   D NE2   1 
ATOM   17806 N  N     . ILE   D 2 362 ? 137.809 111.814 98.271  1.00 136.92 ?  361  ILE   D N     1 
ATOM   17807 C  CA    . ILE   D 2 362 ? 138.742 110.809 98.764  1.00 136.76 ?  361  ILE   D CA    1 
ATOM   17808 C  C     . ILE   D 2 362 ? 138.469 109.500 98.037  1.00 137.48 ?  361  ILE   D C     1 
ATOM   17809 O  O     . ILE   D 2 362 ? 137.313 109.077 97.927  1.00 138.02 ?  361  ILE   D O     1 
ATOM   17810 C  CB    . ILE   D 2 362 ? 138.623 110.619 100.288 1.00 134.94 ?  361  ILE   D CB    1 
ATOM   17811 C  CG1   . ILE   D 2 362 ? 139.018 111.903 101.024 1.00 133.86 ?  361  ILE   D CG1   1 
ATOM   17812 C  CG2   . ILE   D 2 362 ? 139.484 109.462 100.748 1.00 133.50 ?  361  ILE   D CG2   1 
ATOM   17813 C  CD1   . ILE   D 2 362 ? 140.512 112.147 101.079 1.00 133.16 ?  361  ILE   D CD1   1 
ATOM   17814 N  N     . ASP   D 2 363 ? 139.528 108.862 97.543  1.00 142.86 ?  362  ASP   D N     1 
ATOM   17815 C  CA    . ASP   D 2 363 ? 139.415 107.590 96.841  1.00 141.99 ?  362  ASP   D CA    1 
ATOM   17816 C  C     . ASP   D 2 363 ? 139.630 106.449 97.830  1.00 143.44 ?  362  ASP   D C     1 
ATOM   17817 O  O     . ASP   D 2 363 ? 140.681 106.371 98.475  1.00 143.02 ?  362  ASP   D O     1 
ATOM   17818 C  CB    . ASP   D 2 363 ? 140.427 107.516 95.699  1.00 142.53 ?  362  ASP   D CB    1 
ATOM   17819 C  CG    . ASP   D 2 363 ? 140.613 106.105 95.174  1.00 144.39 ?  362  ASP   D CG    1 
ATOM   17820 O  OD1   . ASP   D 2 363 ? 139.598 105.440 94.877  1.00 145.15 ?  362  ASP   D OD1   1 
ATOM   17821 O  OD2   . ASP   D 2 363 ? 141.775 105.662 95.055  1.00 143.21 ?  362  ASP   D OD2   1 
ATOM   17822 N  N     . SER   D 2 364 ? 138.609 105.595 97.962  1.00 155.61 ?  363  SER   D N     1 
ATOM   17823 C  CA    . SER   D 2 364 ? 138.665 104.471 98.934  1.00 155.77 ?  363  SER   D CA    1 
ATOM   17824 C  C     . SER   D 2 364 ? 139.105 103.183 98.241  1.00 156.59 ?  363  SER   D C     1 
ATOM   17825 O  O     . SER   D 2 364 ? 138.228 102.437 97.767  1.00 157.21 ?  363  SER   D O     1 
ATOM   17826 C  CB    . SER   D 2 364 ? 137.338 104.290 99.612  1.00 154.78 ?  363  SER   D CB    1 
ATOM   17827 O  OG    . SER   D 2 364 ? 136.997 105.446 100.361 1.00 154.65 ?  363  SER   D OG    1 
ATOM   17828 N  N     . GLU   D 2 365 ? 140.410 102.936 98.195  1.00 155.07 ?  364  GLU   D N     1 
ATOM   17829 C  CA    . GLU   D 2 365 ? 140.963 101.730 97.596  1.00 155.17 ?  364  GLU   D CA    1 
ATOM   17830 C  C     . GLU   D 2 365 ? 142.161 101.288 98.415  1.00 155.15 ?  364  GLU   D C     1 
ATOM   17831 O  O     . GLU   D 2 365 ? 143.010 102.117 98.771  1.00 153.75 ?  364  GLU   D O     1 
ATOM   17832 C  CB    . GLU   D 2 365 ? 141.368 101.966 96.138  1.00 155.40 ?  364  GLU   D CB    1 
ATOM   17833 C  CG    . GLU   D 2 365 ? 140.285 101.632 95.127  1.00 154.70 ?  364  GLU   D CG    1 
ATOM   17834 C  CD    . GLU   D 2 365 ? 140.622 102.118 93.733  1.00 155.77 ?  364  GLU   D CD    1 
ATOM   17835 O  OE1   . GLU   D 2 365 ? 141.774 102.547 93.515  1.00 155.92 ?  364  GLU   D OE1   1 
ATOM   17836 O  OE2   . GLU   D 2 365 ? 139.735 102.071 92.854  1.00 156.27 ?  364  GLU   D OE2   1 
ATOM   17837 N  N     . VAL   D 2 366 ? 142.221 99.992  98.730  1.00 152.91 ?  365  VAL   D N     1 
ATOM   17838 C  CA    . VAL   D 2 366 ? 143.303 99.446  99.552  1.00 151.81 ?  365  VAL   D CA    1 
ATOM   17839 C  C     . VAL   D 2 366 ? 143.838 98.173  98.899  1.00 151.59 ?  365  VAL   D C     1 
ATOM   17840 O  O     . VAL   D 2 366 ? 143.064 97.247  98.640  1.00 151.71 ?  365  VAL   D O     1 
ATOM   17841 C  CB    . VAL   D 2 366 ? 142.824 99.178  100.994 1.00 151.03 ?  365  VAL   D CB    1 
ATOM   17842 C  CG1   . VAL   D 2 366 ? 142.757 100.475 101.786 1.00 146.30 ?  365  VAL   D CG1   1 
ATOM   17843 C  CG2   . VAL   D 2 366 ? 141.466 98.492  100.997 1.00 152.38 ?  365  VAL   D CG2   1 
ATOM   17844 N  N     . ASP   D 2 367 ? 145.155 98.131  98.630  1.00 158.64 ?  366  ASP   D N     1 
ATOM   17845 C  CA    . ASP   D 2 367 ? 145.804 97.007  97.975  1.00 160.62 ?  366  ASP   D CA    1 
ATOM   17846 C  C     . ASP   D 2 367 ? 146.425 96.081  99.020  1.00 159.03 ?  366  ASP   D C     1 
ATOM   17847 O  O     . ASP   D 2 367 ? 146.295 96.285  100.229 1.00 155.11 ?  366  ASP   D O     1 
ATOM   17848 C  CB    . ASP   D 2 367 ? 146.857 97.504  96.982  1.00 160.14 ?  366  ASP   D CB    1 
ATOM   17849 C  CG    . ASP   D 2 367 ? 147.068 96.546  95.825  1.00 159.84 ?  366  ASP   D CG    1 
ATOM   17850 O  OD1   . ASP   D 2 367 ? 147.751 95.519  96.020  1.00 159.70 ?  366  ASP   D OD1   1 
ATOM   17851 O  OD2   . ASP   D 2 367 ? 146.552 96.820  94.721  1.00 158.74 ?  366  ASP   D OD2   1 
ATOM   17852 N  N     . THR   D 2 368 ? 147.109 95.042  98.540  1.00 163.90 ?  367  THR   D N     1 
ATOM   17853 C  CA    . THR   D 2 368 ? 147.767 94.067  99.401  1.00 163.50 ?  367  THR   D CA    1 
ATOM   17854 C  C     . THR   D 2 368 ? 149.276 94.283  99.469  1.00 163.55 ?  367  THR   D C     1 
ATOM   17855 O  O     . THR   D 2 368 ? 150.036 93.323  99.637  1.00 163.35 ?  367  THR   D O     1 
ATOM   17856 C  CB    . THR   D 2 368 ? 147.455 92.645  98.931  1.00 163.14 ?  367  THR   D CB    1 
ATOM   17857 O  OG1   . THR   D 2 368 ? 148.195 92.356  97.739  1.00 162.40 ?  367  THR   D OG1   1 
ATOM   17858 C  CG2   . THR   D 2 368 ? 145.967 92.496  98.649  1.00 161.22 ?  367  THR   D CG2   1 
ATOM   17859 N  N     . ASP   D 2 369 ? 149.729 95.523  99.296  1.00 161.21 ?  368  ASP   D N     1 
ATOM   17860 C  CA    . ASP   D 2 369 ? 151.142 95.850  99.419  1.00 160.43 ?  368  ASP   D CA    1 
ATOM   17861 C  C     . ASP   D 2 369 ? 151.534 96.257  100.832 1.00 160.04 ?  368  ASP   D C     1 
ATOM   17862 O  O     . ASP   D 2 369 ? 152.727 96.437  101.099 1.00 158.93 ?  368  ASP   D O     1 
ATOM   17863 C  CB    . ASP   D 2 369 ? 151.517 96.969  98.441  1.00 159.96 ?  368  ASP   D CB    1 
ATOM   17864 C  CG    . ASP   D 2 369 ? 150.821 98.277  98.756  1.00 159.50 ?  368  ASP   D CG    1 
ATOM   17865 O  OD1   . ASP   D 2 369 ? 149.709 98.501  98.233  1.00 158.74 ?  368  ASP   D OD1   1 
ATOM   17866 O  OD2   . ASP   D 2 369 ? 151.386 99.086  99.522  1.00 158.42 ?  368  ASP   D OD2   1 
ATOM   17867 N  N     . ASP   D 2 370 ? 150.565 96.412  101.737 1.00 153.34 ?  369  ASP   D N     1 
ATOM   17868 C  CA    . ASP   D 2 370 ? 150.877 96.705  103.128 1.00 151.73 ?  369  ASP   D CA    1 
ATOM   17869 C  C     . ASP   D 2 370 ? 151.350 95.476  103.886 1.00 151.98 ?  369  ASP   D C     1 
ATOM   17870 O  O     . ASP   D 2 370 ? 152.031 95.623  104.907 1.00 151.72 ?  369  ASP   D O     1 
ATOM   17871 C  CB    . ASP   D 2 370 ? 149.659 97.308  103.829 1.00 150.08 ?  369  ASP   D CB    1 
ATOM   17872 C  CG    . ASP   D 2 370 ? 149.192 98.593  103.177 1.00 150.78 ?  369  ASP   D CG    1 
ATOM   17873 O  OD1   . ASP   D 2 370 ? 149.846 99.043  102.213 1.00 151.22 ?  369  ASP   D OD1   1 
ATOM   17874 O  OD2   . ASP   D 2 370 ? 148.171 99.154  103.631 1.00 150.14 ?  369  ASP   D OD2   1 
ATOM   17875 N  N     . LEU   D 2 371 ? 151.000 94.277  103.412 1.00 157.15 ?  370  LEU   D N     1 
ATOM   17876 C  CA    . LEU   D 2 371 ? 151.521 93.054  104.010 1.00 157.40 ?  370  LEU   D CA    1 
ATOM   17877 C  C     . LEU   D 2 371 ? 153.039 93.071  104.052 1.00 158.68 ?  370  LEU   D C     1 
ATOM   17878 O  O     . LEU   D 2 371 ? 153.638 92.570  105.010 1.00 157.83 ?  370  LEU   D O     1 
ATOM   17879 C  CB    . LEU   D 2 371 ? 151.003 91.842  103.231 1.00 156.73 ?  370  LEU   D CB    1 
ATOM   17880 C  CG    . LEU   D 2 371 ? 151.482 90.420  103.548 1.00 157.02 ?  370  LEU   D CG    1 
ATOM   17881 C  CD1   . LEU   D 2 371 ? 150.391 89.419  103.200 1.00 156.56 ?  370  LEU   D CD1   1 
ATOM   17882 C  CD2   . LEU   D 2 371 ? 152.761 90.065  102.801 1.00 155.87 ?  370  LEU   D CD2   1 
ATOM   17883 N  N     . SER   D 2 372 ? 153.675 93.677  103.049 1.00 160.09 ?  371  SER   D N     1 
ATOM   17884 C  CA    . SER   D 2 372 ? 155.122 93.789  102.983 1.00 159.19 ?  371  SER   D CA    1 
ATOM   17885 C  C     . SER   D 2 372 ? 155.629 95.154  103.433 1.00 158.91 ?  371  SER   D C     1 
ATOM   17886 O  O     . SER   D 2 372 ? 156.743 95.541  103.060 1.00 158.63 ?  371  SER   D O     1 
ATOM   17887 C  CB    . SER   D 2 372 ? 155.592 93.488  101.561 1.00 157.61 ?  371  SER   D CB    1 
ATOM   17888 O  OG    . SER   D 2 372 ? 154.917 94.310  100.620 1.00 156.97 ?  371  SER   D OG    1 
ATOM   17889 N  N     . ASN   D 2 373 ? 154.857 95.809  104.307 1.00 151.97 ?  372  ASN   D N     1 
ATOM   17890 C  CA    . ASN   D 2 373 ? 155.301 97.108  104.875 1.00 151.94 ?  372  ASN   D CA    1 
ATOM   17891 C  C     . ASN   D 2 373 ? 156.296 96.827  106.002 1.00 151.81 ?  372  ASN   D C     1 
ATOM   17892 O  O     . ASN   D 2 373 ? 157.433 96.449  105.672 1.00 150.34 ?  372  ASN   D O     1 
ATOM   17893 C  CB    . ASN   D 2 373 ? 154.140 97.992  105.338 1.00 150.37 ?  372  ASN   D CB    1 
ATOM   17894 C  CG    . ASN   D 2 373 ? 154.582 99.382  105.749 1.00 149.93 ?  372  ASN   D CG    1 
ATOM   17895 O  OD1   . ASN   D 2 373 ? 155.344 100.027 105.036 1.00 149.87 ?  372  ASN   D OD1   1 
ATOM   17896 N  ND2   . ASN   D 2 373 ? 154.115 99.854  106.895 1.00 147.14 ?  372  ASN   D ND2   1 
ATOM   17897 N  N     . PHE   D 2 374 ? 155.897 96.996  107.263 1.00 144.39 ?  373  PHE   D N     1 
ATOM   17898 C  CA    . PHE   D 2 374 ? 156.828 96.836  108.412 1.00 143.05 ?  373  PHE   D CA    1 
ATOM   17899 C  C     . PHE   D 2 374 ? 158.015 95.964  108.001 1.00 145.55 ?  373  PHE   D C     1 
ATOM   17900 O  O     . PHE   D 2 374 ? 159.124 96.521  107.897 1.00 146.39 ?  373  PHE   D O     1 
ATOM   17901 C  CB    . PHE   D 2 374 ? 156.104 96.223  109.610 1.00 142.11 ?  373  PHE   D CB    1 
ATOM   17902 C  CG    . PHE   D 2 374 ? 155.344 97.209  110.457 1.00 143.25 ?  373  PHE   D CG    1 
ATOM   17903 C  CD1   . PHE   D 2 374 ? 155.617 98.563  110.379 1.00 142.96 ?  373  PHE   D CD1   1 
ATOM   17904 C  CD2   . PHE   D 2 374 ? 154.352 96.785  111.324 1.00 141.35 ?  373  PHE   D CD2   1 
ATOM   17905 C  CE1   . PHE   D 2 374 ? 154.910 99.471  111.149 1.00 142.90 ?  373  PHE   D CE1   1 
ATOM   17906 C  CE2   . PHE   D 2 374 ? 153.643 97.694  112.090 1.00 141.49 ?  373  PHE   D CE2   1 
ATOM   17907 C  CZ    . PHE   D 2 374 ? 153.926 99.032  111.999 1.00 143.71 ?  373  PHE   D CZ    1 
HETATM 17908 P  PG    . DTP   E 3 .   ? 128.126 99.079  138.500 1.00 66.39  ?  801  DTP   A PG    1 
HETATM 17909 O  O1G   . DTP   E 3 .   ? 127.601 98.145  137.440 1.00 69.95  ?  801  DTP   A O1G   1 
HETATM 17910 O  O2G   . DTP   E 3 .   ? 128.947 100.213 137.944 1.00 64.88  ?  801  DTP   A O2G   1 
HETATM 17911 O  O3G   . DTP   E 3 .   ? 128.929 98.301  139.511 1.00 66.48  ?  801  DTP   A O3G   1 
HETATM 17912 P  PB    . DTP   E 3 .   ? 127.192 101.110 140.118 1.00 72.13  ?  801  DTP   A PB    1 
HETATM 17913 O  O1B   . DTP   E 3 .   ? 126.115 101.230 141.167 1.00 70.97  ?  801  DTP   A O1B   1 
HETATM 17914 O  O2B   . DTP   E 3 .   ? 128.485 100.775 140.829 1.00 70.02  ?  801  DTP   A O2B   1 
HETATM 17915 O  O3B   . DTP   E 3 .   ? 126.896 99.814  139.219 1.00 72.75  ?  801  DTP   A O3B   1 
HETATM 17916 P  PA    . DTP   E 3 .   ? 128.145 103.278 138.416 1.00 62.15  ?  801  DTP   A PA    1 
HETATM 17917 O  O1A   . DTP   E 3 .   ? 127.925 104.731 138.740 1.00 68.89  ?  801  DTP   A O1A   1 
HETATM 17918 O  O2A   . DTP   E 3 .   ? 129.595 103.122 138.783 1.00 72.42  ?  801  DTP   A O2A   1 
HETATM 17919 O  O3A   . DTP   E 3 .   ? 127.009 102.408 139.168 1.00 63.97  ?  801  DTP   A O3A   1 
HETATM 17920 O  "O5'" . DTP   E 3 .   ? 127.891 103.399 136.833 1.00 60.61  ?  801  DTP   A "O5'" 1 
HETATM 17921 C  "C5'" . DTP   E 3 .   ? 128.539 102.572 135.872 1.00 55.40  ?  801  DTP   A "C5'" 1 
HETATM 17922 C  "C4'" . DTP   E 3 .   ? 128.395 103.197 134.487 1.00 57.11  ?  801  DTP   A "C4'" 1 
HETATM 17923 O  "O4'" . DTP   E 3 .   ? 127.023 103.209 134.110 1.00 66.14  ?  801  DTP   A "O4'" 1 
HETATM 17924 C  "C3'" . DTP   E 3 .   ? 128.916 104.627 134.446 1.00 63.00  ?  801  DTP   A "C3'" 1 
HETATM 17925 O  "O3'" . DTP   E 3 .   ? 129.527 104.874 133.178 1.00 69.69  ?  801  DTP   A "O3'" 1 
HETATM 17926 C  "C2'" . DTP   E 3 .   ? 127.661 105.476 134.598 1.00 63.14  ?  801  DTP   A "C2'" 1 
HETATM 17927 C  "C1'" . DTP   E 3 .   ? 126.613 104.568 133.971 1.00 60.75  ?  801  DTP   A "C1'" 1 
HETATM 17928 N  N9    . DTP   E 3 .   ? 125.301 104.705 134.647 1.00 54.67  ?  801  DTP   A N9    1 
HETATM 17929 C  C8    . DTP   E 3 .   ? 125.099 104.635 135.968 1.00 58.42  ?  801  DTP   A C8    1 
HETATM 17930 N  N7    . DTP   E 3 .   ? 123.781 104.781 136.220 1.00 57.88  ?  801  DTP   A N7    1 
HETATM 17931 C  C5    . DTP   E 3 .   ? 123.158 104.935 135.037 1.00 60.84  ?  801  DTP   A C5    1 
HETATM 17932 C  C6    . DTP   E 3 .   ? 121.825 105.122 134.673 1.00 60.34  ?  801  DTP   A C6    1 
HETATM 17933 N  N6    . DTP   E 3 .   ? 120.858 105.180 135.618 1.00 61.63  ?  801  DTP   A N6    1 
HETATM 17934 N  N1    . DTP   E 3 .   ? 121.514 105.246 133.366 1.00 61.19  ?  801  DTP   A N1    1 
HETATM 17935 C  C2    . DTP   E 3 .   ? 122.467 105.190 132.427 1.00 62.23  ?  801  DTP   A C2    1 
HETATM 17936 N  N3    . DTP   E 3 .   ? 123.753 105.010 132.753 1.00 61.38  ?  801  DTP   A N3    1 
HETATM 17937 C  C4    . DTP   E 3 .   ? 124.121 104.884 134.049 1.00 57.92  ?  801  DTP   A C4    1 
HETATM 17938 MG MG    . MG    F 4 .   ? 130.000 101.223 139.484 1.00 78.38  ?  802  MG    A MG    1 
HETATM 17939 P  PG    . ATP   G 5 .   ? 156.578 168.639 119.917 1.00 73.23  ?  803  ATP   A PG    1 
HETATM 17940 O  O1G   . ATP   G 5 .   ? 155.694 167.746 120.780 1.00 68.34  ?  803  ATP   A O1G   1 
HETATM 17941 O  O2G   . ATP   G 5 .   ? 155.844 169.772 119.338 1.00 82.34  ?  803  ATP   A O2G   1 
HETATM 17942 O  O3G   . ATP   G 5 .   ? 157.773 169.063 120.744 1.00 68.60  ?  803  ATP   A O3G   1 
HETATM 17943 P  PB    . ATP   G 5 .   ? 156.902 166.218 118.364 1.00 58.18  ?  803  ATP   A PB    1 
HETATM 17944 O  O1B   . ATP   G 5 .   ? 155.548 165.825 118.804 1.00 56.96  ?  803  ATP   A O1B   1 
HETATM 17945 O  O2B   . ATP   G 5 .   ? 157.054 166.018 116.867 1.00 63.11  ?  803  ATP   A O2B   1 
HETATM 17946 O  O3B   . ATP   G 5 .   ? 157.156 167.745 118.735 1.00 155.45 ?  803  ATP   A O3B   1 
HETATM 17947 P  PA    . ATP   G 5 .   ? 157.937 164.631 120.559 1.00 62.79  ?  803  ATP   A PA    1 
HETATM 17948 O  O1A   . ATP   G 5 .   ? 156.831 165.180 121.370 1.00 65.06  ?  803  ATP   A O1A   1 
HETATM 17949 O  O2A   . ATP   G 5 .   ? 159.248 164.948 121.245 1.00 67.07  ?  803  ATP   A O2A   1 
HETATM 17950 O  O3A   . ATP   G 5 .   ? 157.980 165.331 119.130 1.00 161.81 ?  803  ATP   A O3A   1 
HETATM 17951 O  "O5'" . ATP   G 5 .   ? 157.822 163.046 120.319 1.00 73.81  ?  803  ATP   A "O5'" 1 
HETATM 17952 C  "C5'" . ATP   G 5 .   ? 157.002 162.524 119.251 1.00 73.08  ?  803  ATP   A "C5'" 1 
HETATM 17953 C  "C4'" . ATP   G 5 .   ? 156.990 161.014 119.236 1.00 69.57  ?  803  ATP   A "C4'" 1 
HETATM 17954 O  "O4'" . ATP   G 5 .   ? 158.335 160.507 119.129 1.00 71.70  ?  803  ATP   A "O4'" 1 
HETATM 17955 C  "C3'" . ATP   G 5 .   ? 156.381 160.335 120.459 1.00 65.22  ?  803  ATP   A "C3'" 1 
HETATM 17956 O  "O3'" . ATP   G 5 .   ? 155.731 159.128 120.088 1.00 62.00  ?  803  ATP   A "O3'" 1 
HETATM 17957 C  "C2'" . ATP   G 5 .   ? 157.603 160.059 121.333 1.00 67.90  ?  803  ATP   A "C2'" 1 
HETATM 17958 O  "O2'" . ATP   G 5 .   ? 157.378 158.922 122.157 1.00 66.07  ?  803  ATP   A "O2'" 1 
HETATM 17959 C  "C1'" . ATP   G 5 .   ? 158.681 159.771 120.286 1.00 72.08  ?  803  ATP   A "C1'" 1 
HETATM 17960 N  N9    . ATP   G 5 .   ? 160.026 160.169 120.687 1.00 72.00  ?  803  ATP   A N9    1 
HETATM 17961 C  C8    . ATP   G 5 .   ? 160.383 161.312 121.355 1.00 70.67  ?  803  ATP   A C8    1 
HETATM 17962 N  N7    . ATP   G 5 .   ? 161.672 161.435 121.552 1.00 65.03  ?  803  ATP   A N7    1 
HETATM 17963 C  C5    . ATP   G 5 .   ? 162.205 160.291 120.976 1.00 64.91  ?  803  ATP   A C5    1 
HETATM 17964 C  C6    . ATP   G 5 .   ? 163.525 159.825 120.838 1.00 60.74  ?  803  ATP   A C6    1 
HETATM 17965 N  N6    . ATP   G 5 .   ? 164.591 160.467 121.315 1.00 57.65  ?  803  ATP   A N6    1 
HETATM 17966 N  N1    . ATP   G 5 .   ? 163.713 158.653 120.195 1.00 62.30  ?  803  ATP   A N1    1 
HETATM 17967 C  C2    . ATP   G 5 .   ? 162.646 157.995 119.733 1.00 63.61  ?  803  ATP   A C2    1 
HETATM 17968 N  N3    . ATP   G 5 .   ? 161.356 158.332 119.808 1.00 65.25  ?  803  ATP   A N3    1 
HETATM 17969 C  C4    . ATP   G 5 .   ? 161.201 159.500 120.441 1.00 67.99  ?  803  ATP   A C4    1 
HETATM 17970 P  PG    . ATP   H 5 .   ? 153.003 166.352 123.346 1.00 59.09  ?  804  ATP   A PG    1 
HETATM 17971 O  O1G   . ATP   H 5 .   ? 152.920 167.823 123.688 1.00 60.18  ?  804  ATP   A O1G   1 
HETATM 17972 O  O2G   . ATP   H 5 .   ? 154.291 165.986 122.753 1.00 62.40  ?  804  ATP   A O2G   1 
HETATM 17973 O  O3G   . ATP   H 5 .   ? 152.618 165.521 124.546 1.00 53.38  ?  804  ATP   A O3G   1 
HETATM 17974 P  PB    . ATP   H 5 .   ? 151.802 165.948 120.743 1.00 64.50  ?  804  ATP   A PB    1 
HETATM 17975 O  O1B   . ATP   H 5 .   ? 150.622 166.645 120.191 1.00 70.60  ?  804  ATP   A O1B   1 
HETATM 17976 O  O2B   . ATP   H 5 .   ? 153.089 166.527 120.180 1.00 64.26  ?  804  ATP   A O2B   1 
HETATM 17977 O  O3B   . ATP   H 5 .   ? 151.816 166.080 122.324 1.00 71.08  ?  804  ATP   A O3B   1 
HETATM 17978 P  PA    . ATP   H 5 .   ? 152.894 163.320 120.190 1.00 51.92  ?  804  ATP   A PA    1 
HETATM 17979 O  O1A   . ATP   H 5 .   ? 152.513 162.032 120.809 1.00 54.96  ?  804  ATP   A O1A   1 
HETATM 17980 O  O2A   . ATP   H 5 .   ? 154.180 163.859 120.794 1.00 50.62  ?  804  ATP   A O2A   1 
HETATM 17981 O  O3A   . ATP   H 5 .   ? 151.740 164.389 120.437 1.00 92.09  ?  804  ATP   A O3A   1 
HETATM 17982 O  "O5'" . ATP   H 5 .   ? 153.110 163.219 118.625 1.00 48.57  ?  804  ATP   A "O5'" 1 
HETATM 17983 C  "C5'" . ATP   H 5 .   ? 152.379 162.268 117.825 1.00 51.23  ?  804  ATP   A "C5'" 1 
HETATM 17984 C  "C4'" . ATP   H 5 .   ? 152.739 162.486 116.380 1.00 52.82  ?  804  ATP   A "C4'" 1 
HETATM 17985 O  "O4'" . ATP   H 5 .   ? 152.299 163.796 115.957 1.00 55.42  ?  804  ATP   A "O4'" 1 
HETATM 17986 C  "C3'" . ATP   H 5 .   ? 154.237 162.416 116.071 1.00 48.52  ?  804  ATP   A "C3'" 1 
HETATM 17987 O  "O3'" . ATP   H 5 .   ? 154.455 161.686 114.872 1.00 47.05  ?  804  ATP   A "O3'" 1 
HETATM 17988 C  "C2'" . ATP   H 5 .   ? 154.626 163.885 115.912 1.00 51.49  ?  804  ATP   A "C2'" 1 
HETATM 17989 O  "O2'" . ATP   H 5 .   ? 155.749 164.051 115.056 1.00 48.39  ?  804  ATP   A "O2'" 1 
HETATM 17990 C  "C1'" . ATP   H 5 .   ? 153.354 164.446 115.286 1.00 59.16  ?  804  ATP   A "C1'" 1 
HETATM 17991 N  N9    . ATP   H 5 .   ? 153.193 165.890 115.438 1.00 62.45  ?  804  ATP   A N9    1 
HETATM 17992 C  C8    . ATP   H 5 .   ? 153.214 166.599 116.607 1.00 60.91  ?  804  ATP   A C8    1 
HETATM 17993 N  N7    . ATP   H 5 .   ? 153.093 167.896 116.449 1.00 62.17  ?  804  ATP   A N7    1 
HETATM 17994 C  C5    . ATP   H 5 .   ? 152.982 168.049 115.079 1.00 64.73  ?  804  ATP   A C5    1 
HETATM 17995 C  C6    . ATP   H 5 .   ? 152.841 169.188 114.257 1.00 63.28  ?  804  ATP   A C6    1 
HETATM 17996 N  N6    . ATP   H 5 .   ? 152.758 170.435 114.725 1.00 58.48  ?  804  ATP   A N6    1 
HETATM 17997 N  N1    . ATP   H 5 .   ? 152.776 168.996 112.923 1.00 63.14  ?  804  ATP   A N1    1 
HETATM 17998 C  C2    . ATP   H 5 .   ? 152.838 167.747 112.449 1.00 61.62  ?  804  ATP   A C2    1 
HETATM 17999 N  N3    . ATP   H 5 .   ? 152.966 166.601 113.121 1.00 63.33  ?  804  ATP   A N3    1 
HETATM 18000 C  C4    . ATP   H 5 .   ? 153.036 166.822 114.436 1.00 64.68  ?  804  ATP   A C4    1 
HETATM 18001 MG MG    . MG    I 4 .   ? 154.951 165.807 120.790 1.00 48.88  ?  805  MG    A MG    1 
HETATM 18002 N  N     . UNL   J 6 .   ? 147.274 122.966 123.544 1.00 61.46  ?  806  UNL   A N     1 
HETATM 18003 P  PG    . ATP   K 5 .   ? 102.861 72.069  126.820 1.00 96.20  ?  801  ATP   B PG    1 
HETATM 18004 O  O1G   . ATP   K 5 .   ? 102.186 71.304  127.921 1.00 87.46  ?  801  ATP   B O1G   1 
HETATM 18005 O  O2G   . ATP   K 5 .   ? 103.221 71.147  125.693 1.00 89.96  ?  801  ATP   B O2G   1 
HETATM 18006 O  O3G   . ATP   K 5 .   ? 104.110 72.772  127.271 1.00 96.24  ?  801  ATP   B O3G   1 
HETATM 18007 P  PB    . ATP   K 5 .   ? 101.668 74.635  126.953 1.00 95.45  ?  801  ATP   B PB    1 
HETATM 18008 O  O1B   . ATP   K 5 .   ? 103.044 75.239  127.077 1.00 96.85  ?  801  ATP   B O1B   1 
HETATM 18009 O  O2B   . ATP   K 5 .   ? 100.821 75.488  126.058 1.00 87.50  ?  801  ATP   B O2B   1 
HETATM 18010 O  O3B   . ATP   K 5 .   ? 101.794 73.164  126.263 1.00 91.95  ?  801  ATP   B O3B   1 
HETATM 18011 P  PA    . ATP   K 5 .   ? 101.501 75.171  129.794 1.00 87.16  ?  801  ATP   B PA    1 
HETATM 18012 O  O1A   . ATP   K 5 .   ? 101.038 74.386  130.986 1.00 87.57  ?  801  ATP   B O1A   1 
HETATM 18013 O  O2A   . ATP   K 5 .   ? 103.001 75.229  129.785 1.00 87.80  ?  801  ATP   B O2A   1 
HETATM 18014 O  O3A   . ATP   K 5 .   ? 100.955 74.456  128.421 1.00 88.96  ?  801  ATP   B O3A   1 
HETATM 18015 O  "O5'" . ATP   K 5 .   ? 100.873 76.687  129.860 1.00 89.28  ?  801  ATP   B "O5'" 1 
HETATM 18016 C  "C5'" . ATP   K 5 .   ? 101.157 77.589  128.826 1.00 86.60  ?  801  ATP   B "C5'" 1 
HETATM 18017 C  "C4'" . ATP   K 5 .   ? 100.826 78.888  129.157 1.00 85.35  ?  801  ATP   B "C4'" 1 
HETATM 18018 O  "O4'" . ATP   K 5 .   ? 99.506  78.950  129.955 1.00 91.98  ?  801  ATP   B "O4'" 1 
HETATM 18019 C  "C3'" . ATP   K 5 .   ? 101.899 79.526  130.134 1.00 86.87  ?  801  ATP   B "C3'" 1 
HETATM 18020 O  "O3'" . ATP   K 5 .   ? 101.998 80.991  129.867 1.00 87.84  ?  801  ATP   B "O3'" 1 
HETATM 18021 C  "C2'" . ATP   K 5 .   ? 101.438 79.297  131.286 1.00 89.11  ?  801  ATP   B "C2'" 1 
HETATM 18022 O  "O2'" . ATP   K 5 .   ? 101.902 80.272  132.260 1.00 94.36  ?  801  ATP   B "O2'" 1 
HETATM 18023 C  "C1'" . ATP   K 5 .   ? 99.788  79.425  131.115 1.00 88.35  ?  801  ATP   B "C1'" 1 
HETATM 18024 N  N9    . ATP   K 5 .   ? 99.167  78.594  132.062 1.00 88.07  ?  801  ATP   B N9    1 
HETATM 18025 C  C8    . ATP   K 5 .   ? 99.592  77.392  132.394 1.00 86.36  ?  801  ATP   B C8    1 
HETATM 18026 N  N7    . ATP   K 5 .   ? 98.784  76.871  133.292 1.00 84.27  ?  801  ATP   B N7    1 
HETATM 18027 C  C5    . ATP   K 5 .   ? 97.824  77.768  133.534 1.00 85.85  ?  801  ATP   B C5    1 
HETATM 18028 C  C6    . ATP   K 5 .   ? 96.713  77.774  134.375 1.00 87.94  ?  801  ATP   B C6    1 
HETATM 18029 N  N6    . ATP   K 5 .   ? 96.424  76.638  135.219 1.00 88.03  ?  801  ATP   B N6    1 
HETATM 18030 N  N1    . ATP   K 5 .   ? 95.935  78.833  134.385 1.00 87.85  ?  801  ATP   B N1    1 
HETATM 18031 C  C2    . ATP   K 5 .   ? 96.180  79.878  133.625 1.00 87.66  ?  801  ATP   B C2    1 
HETATM 18032 N  N3    . ATP   K 5 .   ? 97.219  79.906  132.819 1.00 86.89  ?  801  ATP   B N3    1 
HETATM 18033 C  C4    . ATP   K 5 .   ? 98.055  78.868  132.751 1.00 87.08  ?  801  ATP   B C4    1 
HETATM 18034 P  PG    . ATP   L 5 .   ? 107.062 75.143  128.123 1.00 104.77 ?  802  ATP   B PG    1 
HETATM 18035 O  O1G   . ATP   L 5 .   ? 105.569 75.126  128.278 1.00 86.79  ?  802  ATP   B O1G   1 
HETATM 18036 O  O2G   . ATP   L 5 .   ? 107.583 73.734  128.112 1.00 98.88  ?  802  ATP   B O2G   1 
HETATM 18037 O  O3G   . ATP   L 5 .   ? 107.698 75.916  129.240 1.00 89.52  ?  802  ATP   B O3G   1 
HETATM 18038 P  PB    . ATP   L 5 .   ? 106.434 76.601  125.711 1.00 85.64  ?  802  ATP   B PB    1 
HETATM 18039 O  O1B   . ATP   L 5 .   ? 105.135 75.866  125.671 1.00 85.95  ?  802  ATP   B O1B   1 
HETATM 18040 O  O2B   . ATP   L 5 .   ? 107.078 76.567  124.361 1.00 93.82  ?  802  ATP   B O2B   1 
HETATM 18041 O  O3B   . ATP   L 5 .   ? 107.484 75.882  126.730 1.00 99.67  ?  802  ATP   B O3B   1 
HETATM 18042 P  PA    . ATP   L 5 .   ? 104.793 78.661  126.879 1.00 95.32  ?  802  ATP   B PA    1 
HETATM 18043 O  O1A   . ATP   L 5 .   ? 104.334 77.680  127.915 1.00 93.77  ?  802  ATP   B O1A   1 
HETATM 18044 O  O2A   . ATP   L 5 .   ? 105.040 79.995  127.504 1.00 88.68  ?  802  ATP   B O2A   1 
HETATM 18045 O  O3A   . ATP   L 5 .   ? 106.179 78.152  126.169 1.00 94.24  ?  802  ATP   B O3A   1 
HETATM 18046 O  "O5'" . ATP   L 5 .   ? 103.613 78.792  125.742 1.00 93.18  ?  802  ATP   B "O5'" 1 
HETATM 18047 C  "C5'" . ATP   L 5 .   ? 103.332 80.023  125.138 1.00 86.52  ?  802  ATP   B "C5'" 1 
HETATM 18048 C  "C4'" . ATP   L 5 .   ? 102.279 79.858  124.269 1.00 86.06  ?  802  ATP   B "C4'" 1 
HETATM 18049 O  "O4'" . ATP   L 5 .   ? 102.644 78.845  123.166 1.00 92.92  ?  802  ATP   B "O4'" 1 
HETATM 18050 C  "C3'" . ATP   L 5 .   ? 101.037 79.219  125.022 1.00 87.88  ?  802  ATP   B "C3'" 1 
HETATM 18051 O  "O3'" . ATP   L 5 .   ? 99.874  80.145  124.871 1.00 94.35  ?  802  ATP   B "O3'" 1 
HETATM 18052 C  "C2'" . ATP   L 5 .   ? 100.825 78.092  124.479 1.00 88.02  ?  802  ATP   B "C2'" 1 
HETATM 18053 O  "O2'" . ATP   L 5 .   ? 99.411  77.856  124.236 1.00 97.12  ?  802  ATP   B "O2'" 1 
HETATM 18054 C  "C1'" . ATP   L 5 .   ? 101.598 78.117  123.004 1.00 91.50  ?  802  ATP   B "C1'" 1 
HETATM 18055 N  N9    . ATP   L 5 .   ? 101.970 76.796  122.662 1.00 88.91  ?  802  ATP   B N9    1 
HETATM 18056 C  C8    . ATP   L 5 .   ? 102.725 75.984  123.374 1.00 85.82  ?  802  ATP   B C8    1 
HETATM 18057 N  N7    . ATP   L 5 .   ? 102.854 74.841  122.730 1.00 89.74  ?  802  ATP   B N7    1 
HETATM 18058 C  C5    . ATP   L 5 .   ? 102.165 74.925  121.585 1.00 89.79  ?  802  ATP   B C5    1 
HETATM 18059 C  C6    . ATP   L 5 .   ? 101.935 74.054  120.510 1.00 88.24  ?  802  ATP   B C6    1 
HETATM 18060 N  N6    . ATP   L 5 .   ? 102.498 72.725  120.492 1.00 91.11  ?  802  ATP   B N6    1 
HETATM 18061 N  N1    . ATP   L 5 .   ? 101.184 74.469  119.508 1.00 90.24  ?  802  ATP   B N1    1 
HETATM 18062 C  C2    . ATP   L 5 .   ? 100.658 75.677  119.494 1.00 89.88  ?  802  ATP   B C2    1 
HETATM 18063 N  N3    . ATP   L 5 .   ? 100.856 76.515  120.488 1.00 90.20  ?  802  ATP   B N3    1 
HETATM 18064 C  C4    . ATP   L 5 .   ? 101.601 76.172  121.540 1.00 91.18  ?  802  ATP   B C4    1 
HETATM 18065 P  PG    . DTP   M 3 .   ? 131.288 136.983 141.512 1.00 74.45  ?  803  DTP   B PG    1 
HETATM 18066 O  O1G   . DTP   M 3 .   ? 130.086 136.162 141.903 1.00 72.67  ?  803  DTP   B O1G   1 
HETATM 18067 O  O2G   . DTP   M 3 .   ? 131.968 137.521 142.745 1.00 71.12  ?  803  DTP   B O2G   1 
HETATM 18068 O  O3G   . DTP   M 3 .   ? 130.860 138.127 140.628 1.00 73.47  ?  803  DTP   B O3G   1 
HETATM 18069 P  PB    . DTP   M 3 .   ? 132.918 134.712 141.342 1.00 69.88  ?  803  DTP   B PB    1 
HETATM 18070 O  O1B   . DTP   M 3 .   ? 132.446 134.574 142.768 1.00 66.23  ?  803  DTP   B O1B   1 
HETATM 18071 O  O2B   . DTP   M 3 .   ? 134.421 134.828 141.368 1.00 74.74  ?  803  DTP   B O2B   1 
HETATM 18072 O  O3B   . DTP   M 3 .   ? 132.303 136.046 140.688 1.00 74.14  ?  803  DTP   B O3B   1 
HETATM 18073 P  PA    . DTP   M 3 .   ? 131.008 132.962 140.199 1.00 73.44  ?  803  DTP   B PA    1 
HETATM 18074 O  O1A   . DTP   M 3 .   ? 130.183 133.230 141.430 1.00 74.22  ?  803  DTP   B O1A   1 
HETATM 18075 O  O2A   . DTP   M 3 .   ? 130.895 131.474 139.989 1.00 72.10  ?  803  DTP   B O2A   1 
HETATM 18076 O  O3A   . DTP   M 3 .   ? 132.531 133.416 140.464 1.00 74.25  ?  803  DTP   B O3A   1 
HETATM 18077 O  "O5'" . DTP   M 3 .   ? 130.314 133.783 139.000 1.00 69.05  ?  803  DTP   B "O5'" 1 
HETATM 18078 C  "C5'" . DTP   M 3 .   ? 128.915 134.067 139.024 1.00 63.17  ?  803  DTP   B "C5'" 1 
HETATM 18079 C  "C4'" . DTP   M 3 .   ? 128.152 133.503 137.828 1.00 62.60  ?  803  DTP   B "C4'" 1 
HETATM 18080 O  "O4'" . DTP   M 3 .   ? 128.868 133.755 136.619 1.00 67.38  ?  803  DTP   B "O4'" 1 
HETATM 18081 C  "C3'" . DTP   M 3 .   ? 127.911 132.005 137.940 1.00 71.71  ?  803  DTP   B "C3'" 1 
HETATM 18082 O  "O3'" . DTP   M 3 .   ? 126.596 131.697 137.469 1.00 74.24  ?  803  DTP   B "O3'" 1 
HETATM 18083 C  "C2'" . DTP   M 3 .   ? 128.949 131.390 137.019 1.00 67.66  ?  803  DTP   B "C2'" 1 
HETATM 18084 C  "C1'" . DTP   M 3 .   ? 129.144 132.499 135.997 1.00 66.33  ?  803  DTP   B "C1'" 1 
HETATM 18085 N  N9    . DTP   M 3 .   ? 130.540 132.483 135.497 1.00 64.77  ?  803  DTP   B N9    1 
HETATM 18086 C  C8    . DTP   M 3 .   ? 131.634 132.291 136.244 1.00 67.76  ?  803  DTP   B C8    1 
HETATM 18087 N  N7    . DTP   M 3 .   ? 132.725 132.345 135.449 1.00 68.78  ?  803  DTP   B N7    1 
HETATM 18088 C  C5    . DTP   M 3 .   ? 132.299 132.574 134.192 1.00 65.40  ?  803  DTP   B C5    1 
HETATM 18089 C  C6    . DTP   M 3 .   ? 132.954 132.726 132.970 1.00 66.65  ?  803  DTP   B C6    1 
HETATM 18090 N  N6    . DTP   M 3 .   ? 134.304 132.647 132.903 1.00 67.77  ?  803  DTP   B N6    1 
HETATM 18091 N  N1    . DTP   M 3 .   ? 132.225 132.953 131.858 1.00 66.41  ?  803  DTP   B N1    1 
HETATM 18092 C  C2    . DTP   M 3 .   ? 130.889 133.030 131.921 1.00 66.80  ?  803  DTP   B C2    1 
HETATM 18093 N  N3    . DTP   M 3 .   ? 130.238 132.888 133.082 1.00 65.64  ?  803  DTP   B N3    1 
HETATM 18094 C  C4    . DTP   M 3 .   ? 130.920 132.657 134.229 1.00 64.00  ?  803  DTP   B C4    1 
HETATM 18095 MG MG    . MG    N 4 .   ? 130.377 134.460 143.110 1.00 73.26  ?  804  MG    B MG    1 
HETATM 18096 MG MG    . MG    O 4 .   ? 104.444 75.627  127.873 1.00 93.75  ?  805  MG    B MG    1 
HETATM 18097 C  C2    . A1A3L P 7 .   ? 109.372 111.684 136.640 1.00 73.16  ?  806  A1A3L B C2    1 
HETATM 18098 N  N3    . A1A3L P 7 .   ? 109.303 111.107 135.242 1.00 69.45  ?  806  A1A3L B N3    1 
HETATM 18099 C  C4    . A1A3L P 7 .   ? 107.986 110.717 134.665 1.00 70.98  ?  806  A1A3L B C4    1 
HETATM 18100 C  C5    . A1A3L P 7 .   ? 106.750 110.893 135.458 1.00 72.37  ?  806  A1A3L B C5    1 
HETATM 18101 C  C6    . A1A3L P 7 .   ? 106.856 111.488 136.890 1.00 68.72  ?  806  A1A3L B C6    1 
HETATM 18102 C  "C1'" . A1A3L P 7 .   ? 108.286 112.412 138.759 1.00 68.71  ?  806  A1A3L B "C1'" 1 
HETATM 18103 C  "C2'" . A1A3L P 7 .   ? 108.071 113.931 138.960 1.00 73.46  ?  806  A1A3L B "C2'" 1 
HETATM 18104 C  "C3'" . A1A3L P 7 .   ? 107.309 114.130 140.277 1.00 76.00  ?  806  A1A3L B "C3'" 1 
HETATM 18105 C  "C4'" . A1A3L P 7 .   ? 106.566 112.754 140.338 1.00 67.53  ?  806  A1A3L B "C4'" 1 
HETATM 18106 C  "C5'" . A1A3L P 7 .   ? 105.230 112.868 139.642 1.00 73.18  ?  806  A1A3L B "C5'" 1 
HETATM 18107 N  N01   . A1A3L P 7 .   ? 107.987 114.283 141.566 1.00 80.95  ?  806  A1A3L B N01   1 
HETATM 18108 N  N1    . A1A3L P 7 .   ? 108.173 111.860 137.446 1.00 69.94  ?  806  A1A3L B N1    1 
HETATM 18109 N  N4    . A1A3L P 7 .   ? 107.924 110.186 133.380 1.00 79.91  ?  806  A1A3L B N4    1 
HETATM 18110 O  O01   . A1A3L P 7 .   ? 106.404 115.222 140.116 1.00 74.58  ?  806  A1A3L B O01   1 
HETATM 18111 O  O1A   . A1A3L P 7 .   ? 103.755 111.195 137.868 1.00 70.70  ?  806  A1A3L B O1A   1 
HETATM 18112 O  O1B   . A1A3L P 7 .   ? 102.888 108.058 137.757 1.00 83.25  ?  806  A1A3L B O1B   1 
HETATM 18113 O  O2    . A1A3L P 7 .   ? 110.400 111.989 137.088 1.00 75.36  ?  806  A1A3L B O2    1 
HETATM 18114 O  O2A   . A1A3L P 7 .   ? 102.118 110.995 139.399 1.00 74.12  ?  806  A1A3L B O2A   1 
HETATM 18115 O  O2B   . A1A3L P 7 .   ? 105.195 107.969 137.742 1.00 75.43  ?  806  A1A3L B O2B   1 
HETATM 18116 O  O3A   . A1A3L P 7 .   ? 104.105 109.370 139.652 1.00 74.53  ?  806  A1A3L B O3A   1 
HETATM 18117 O  O3B   . A1A3L P 7 .   ? 104.004 106.797 139.329 1.00 76.04  ?  806  A1A3L B O3B   1 
HETATM 18118 O  "O4'" . A1A3L P 7 .   ? 107.353 111.766 139.690 1.00 66.30  ?  806  A1A3L B "O4'" 1 
HETATM 18119 O  "O5'" . A1A3L P 7 .   ? 104.282 111.983 140.255 1.00 80.80  ?  806  A1A3L B "O5'" 1 
HETATM 18120 P  PA    . A1A3L P 7 .   ? 103.560 110.879 139.276 1.00 82.27  ?  806  A1A3L B PA    1 
HETATM 18121 P  PB    . A1A3L P 7 .   ? 104.051 108.079 138.639 1.00 74.45  ?  806  A1A3L B PB    1 
HETATM 18122 FE FE1   . FEO   Q 8 .   ? 104.289 113.839 103.115 1.00 90.49  ?  401  FEO   C FE1   1 
HETATM 18123 FE FE2   . FEO   Q 8 .   ? 101.387 114.488 102.276 1.00 91.73  ?  401  FEO   C FE2   1 
HETATM 18124 O  O     . FEO   Q 8 .   ? 102.752 113.317 102.339 1.00 87.70  ?  401  FEO   C O     1 
HETATM 18125 FE FE1   . FEO   R 8 .   ? 107.563 138.778 101.130 1.00 100.37 ?  401  FEO   D FE1   1 
HETATM 18126 FE FE2   . FEO   R 8 .   ? 110.469 137.789 100.689 1.00 103.50 ?  401  FEO   D FE2   1 
HETATM 18127 O  O     . FEO   R 8 .   ? 109.213 139.068 100.460 1.00 101.41 ?  401  FEO   D O     1 
HETATM 18128 O  O     . HOH   S 9 .   ? 128.226 137.981 127.145 1.00 30.00  ?  901  HOH   A O     1 
HETATM 18129 O  O     . HOH   S 9 .   ? 138.199 106.998 131.081 1.00 30.00  ?  902  HOH   A O     1 
HETATM 18130 O  O     . HOH   S 9 .   ? 162.588 99.972  117.943 1.00 30.00  ?  903  HOH   A O     1 
HETATM 18131 O  O     . HOH   S 9 .   ? 149.945 105.898 113.171 1.00 30.00  ?  904  HOH   A O     1 
HETATM 18132 O  O     . HOH   S 9 .   ? 128.985 131.012 119.158 1.00 30.00  ?  905  HOH   A O     1 
HETATM 18133 O  O     . HOH   S 9 .   ? 165.077 141.644 121.927 1.00 30.00  ?  906  HOH   A O     1 
HETATM 18134 O  O     . HOH   S 9 .   ? 162.960 135.035 114.994 1.00 22.52  ?  907  HOH   A O     1 
HETATM 18135 O  O     . HOH   S 9 .   ? 129.281 119.158 111.929 1.00 30.00  ?  908  HOH   A O     1 
HETATM 18136 O  O     . HOH   S 9 .   ? 123.948 107.099 129.012 1.00 28.63  ?  909  HOH   A O     1 
HETATM 18137 O  O     . HOH   S 9 .   ? 142.936 141.092 114.207 1.00 30.00  ?  910  HOH   A O     1 
HETATM 18138 O  O     . HOH   S 9 .   ? 154.880 106.149 144.062 1.00 30.00  ?  911  HOH   A O     1 
HETATM 18139 O  O     . HOH   S 9 .   ? 147.151 143.995 136.440 1.00 30.00  ?  912  HOH   A O     1 
HETATM 18140 O  O     . HOH   S 9 .   ? 133.978 100.023 109.967 1.00 30.00  ?  913  HOH   A O     1 
HETATM 18141 O  O     . HOH   S 9 .   ? 134.049 106.150 125.787 1.00 30.00  ?  914  HOH   A O     1 
HETATM 18142 O  O     . HOH   S 9 .   ? 121.342 104.138 138.134 1.00 30.00  ?  915  HOH   A O     1 
HETATM 18143 O  O     . HOH   S 9 .   ? 153.130 126.546 101.295 1.00 36.58  ?  916  HOH   A O     1 
HETATM 18144 O  O     . HOH   S 9 .   ? 141.071 105.754 126.917 1.00 17.85  ?  917  HOH   A O     1 
HETATM 18145 O  O     . HOH   S 9 .   ? 143.504 123.640 145.096 1.00 30.00  ?  918  HOH   A O     1 
HETATM 18146 O  O     . HOH   S 9 .   ? 133.976 106.559 141.918 1.00 30.00  ?  919  HOH   A O     1 
HETATM 18147 O  O     . HOH   S 9 .   ? 146.979 100.606 132.043 1.00 30.00  ?  920  HOH   A O     1 
HETATM 18148 O  O     . HOH   S 9 .   ? 152.776 99.449  126.275 1.00 30.00  ?  921  HOH   A O     1 
HETATM 18149 O  O     . HOH   S 9 .   ? 154.259 140.910 100.055 1.00 24.63  ?  922  HOH   A O     1 
HETATM 18150 O  O     . HOH   S 9 .   ? 161.863 112.078 145.189 1.00 30.00  ?  923  HOH   A O     1 
HETATM 18151 O  O     . HOH   S 9 .   ? 150.454 122.061 109.073 1.00 30.00  ?  924  HOH   A O     1 
HETATM 18152 O  O     . HOH   S 9 .   ? 131.959 93.597  125.429 1.00 30.00  ?  925  HOH   A O     1 
HETATM 18153 O  O     . HOH   S 9 .   ? 167.821 161.027 117.464 1.00 30.00  ?  926  HOH   A O     1 
HETATM 18154 O  O     . HOH   S 9 .   ? 129.956 95.134  130.691 1.00 30.00  ?  927  HOH   A O     1 
HETATM 18155 O  O     . HOH   S 9 .   ? 154.964 109.210 126.225 1.00 24.66  ?  928  HOH   A O     1 
HETATM 18156 O  O     . HOH   S 9 .   ? 156.075 101.155 120.959 1.00 30.00  ?  929  HOH   A O     1 
HETATM 18157 O  O     . HOH   S 9 .   ? 156.868 119.189 144.756 1.00 30.00  ?  930  HOH   A O     1 
HETATM 18158 O  O     . HOH   S 9 .   ? 131.053 99.447  139.860 1.00 68.69  ?  931  HOH   A O     1 
HETATM 18159 O  O     . HOH   S 9 .   ? 153.053 121.982 114.911 1.00 30.00  ?  932  HOH   A O     1 
HETATM 18160 O  O     . HOH   S 9 .   ? 157.410 148.419 124.775 1.00 30.00  ?  933  HOH   A O     1 
HETATM 18161 O  O     . HOH   S 9 .   ? 146.833 126.909 144.885 1.00 30.00  ?  934  HOH   A O     1 
HETATM 18162 O  O     . HOH   S 9 .   ? 135.768 129.308 118.407 1.00 30.00  ?  935  HOH   A O     1 
HETATM 18163 O  O     . HOH   S 9 .   ? 172.655 138.934 142.108 1.00 30.00  ?  936  HOH   A O     1 
HETATM 18164 O  O     . HOH   S 9 .   ? 149.755 100.079 134.053 1.00 25.84  ?  937  HOH   A O     1 
HETATM 18165 O  O     . HOH   S 9 .   ? 130.901 117.871 141.360 1.00 30.00  ?  938  HOH   A O     1 
HETATM 18166 O  O     . HOH   S 9 .   ? 133.222 94.554  108.986 1.00 30.00  ?  939  HOH   A O     1 
HETATM 18167 O  O     . HOH   S 9 .   ? 150.294 95.731  121.125 1.00 29.95  ?  940  HOH   A O     1 
HETATM 18168 O  O     . HOH   S 9 .   ? 141.016 117.031 143.321 1.00 30.00  ?  941  HOH   A O     1 
HETATM 18169 O  O     . HOH   S 9 .   ? 160.094 102.884 121.904 1.00 30.00  ?  942  HOH   A O     1 
HETATM 18170 O  O     . HOH   S 9 .   ? 143.843 128.110 135.407 1.00 30.00  ?  943  HOH   A O     1 
HETATM 18171 O  O     . HOH   S 9 .   ? 131.534 101.672 138.121 1.00 70.62  ?  944  HOH   A O     1 
HETATM 18172 O  O     . HOH   S 9 .   ? 142.628 120.964 119.149 1.00 30.50  ?  945  HOH   A O     1 
HETATM 18173 O  O     . HOH   S 9 .   ? 155.856 128.184 111.009 1.00 30.00  ?  946  HOH   A O     1 
HETATM 18174 O  O     . HOH   S 9 .   ? 163.994 152.042 139.991 1.00 30.00  ?  947  HOH   A O     1 
HETATM 18175 O  O     . HOH   S 9 .   ? 158.179 103.960 129.879 1.00 30.00  ?  948  HOH   A O     1 
HETATM 18176 O  O     . HOH   S 9 .   ? 170.350 139.044 145.089 1.00 33.81  ?  949  HOH   A O     1 
HETATM 18177 O  O     . HOH   S 9 .   ? 164.599 155.143 131.862 1.00 30.00  ?  950  HOH   A O     1 
HETATM 18178 O  O     . HOH   S 9 .   ? 122.981 95.915  143.004 1.00 30.00  ?  951  HOH   A O     1 
HETATM 18179 O  O     . HOH   S 9 .   ? 147.918 110.038 106.978 1.00 30.00  ?  952  HOH   A O     1 
HETATM 18180 O  O     . HOH   S 9 .   ? 171.012 113.899 107.878 1.00 30.00  ?  953  HOH   A O     1 
HETATM 18181 O  O     . HOH   S 9 .   ? 148.856 149.010 117.008 1.00 30.00  ?  954  HOH   A O     1 
HETATM 18182 O  O     . HOH   S 9 .   ? 153.976 170.214 123.841 1.00 30.00  ?  955  HOH   A O     1 
HETATM 18183 O  O     . HOH   S 9 .   ? 135.928 110.769 116.972 1.00 30.00  ?  956  HOH   A O     1 
HETATM 18184 O  O     . HOH   S 9 .   ? 130.994 100.034 116.993 1.00 20.58  ?  957  HOH   A O     1 
HETATM 18185 O  O     . HOH   S 9 .   ? 134.090 99.194  134.044 1.00 30.00  ?  958  HOH   A O     1 
HETATM 18186 O  O     . HOH   S 9 .   ? 147.012 109.970 131.192 1.00 30.00  ?  959  HOH   A O     1 
HETATM 18187 O  O     . HOH   S 9 .   ? 156.505 111.062 138.697 1.00 30.00  ?  960  HOH   A O     1 
HETATM 18188 O  O     . HOH   S 9 .   ? 152.123 111.945 102.037 1.00 30.00  ?  961  HOH   A O     1 
HETATM 18189 O  O     . HOH   S 9 .   ? 125.968 105.918 122.863 1.00 28.22  ?  962  HOH   A O     1 
HETATM 18190 O  O     . HOH   S 9 .   ? 129.094 106.249 141.027 1.00 19.38  ?  963  HOH   A O     1 
HETATM 18191 O  O     . HOH   S 9 .   ? 169.082 107.062 115.580 1.00 30.00  ?  964  HOH   A O     1 
HETATM 18192 O  O     . HOH   S 9 .   ? 125.721 118.912 123.997 1.00 30.00  ?  965  HOH   A O     1 
HETATM 18193 O  O     . HOH   S 9 .   ? 128.930 94.995  127.048 1.00 30.66  ?  966  HOH   A O     1 
HETATM 18194 O  O     . HOH   S 9 .   ? 126.937 108.103 116.892 1.00 28.50  ?  967  HOH   A O     1 
HETATM 18195 O  O     . HOH   S 9 .   ? 142.017 112.973 136.047 1.00 22.74  ?  968  HOH   A O     1 
HETATM 18196 O  O     . HOH   S 9 .   ? 142.199 133.172 134.128 1.00 30.00  ?  969  HOH   A O     1 
HETATM 18197 O  O     . HOH   S 9 .   ? 150.938 118.232 135.867 1.00 21.97  ?  970  HOH   A O     1 
HETATM 18198 O  O     . HOH   S 9 .   ? 166.420 150.056 149.668 1.00 30.00  ?  971  HOH   A O     1 
HETATM 18199 O  O     . HOH   S 9 .   ? 126.890 103.484 119.943 1.00 30.00  ?  972  HOH   A O     1 
HETATM 18200 O  O     . HOH   S 9 .   ? 155.213 110.947 128.072 1.00 30.00  ?  973  HOH   A O     1 
HETATM 18201 O  O     . HOH   S 9 .   ? 136.915 130.869 136.999 1.00 30.00  ?  974  HOH   A O     1 
HETATM 18202 O  O     . HOH   S 9 .   ? 126.903 95.056  136.205 1.00 30.00  ?  975  HOH   A O     1 
HETATM 18203 O  O     . HOH   S 9 .   ? 133.217 127.797 127.773 1.00 21.30  ?  976  HOH   A O     1 
HETATM 18204 O  O     . HOH   S 9 .   ? 124.076 129.142 124.004 1.00 30.00  ?  977  HOH   A O     1 
HETATM 18205 O  O     . HOH   S 9 .   ? 146.064 112.000 107.938 1.00 25.92  ?  978  HOH   A O     1 
HETATM 18206 O  O     . HOH   S 9 .   ? 129.050 119.953 136.106 1.00 30.00  ?  979  HOH   A O     1 
HETATM 18207 O  O     . HOH   S 9 .   ? 130.045 104.410 142.030 1.00 30.00  ?  980  HOH   A O     1 
HETATM 18208 O  O     . HOH   S 9 .   ? 178.932 115.927 127.012 1.00 30.00  ?  981  HOH   A O     1 
HETATM 18209 O  O     . HOH   S 9 .   ? 129.195 118.024 137.596 1.00 17.19  ?  982  HOH   A O     1 
HETATM 18210 O  O     . HOH   S 9 .   ? 161.463 161.468 128.177 1.00 30.00  ?  983  HOH   A O     1 
HETATM 18211 O  O     . HOH   S 9 .   ? 131.047 102.222 141.002 1.00 74.18  ?  984  HOH   A O     1 
HETATM 18212 O  O     . HOH   S 9 .   ? 154.125 132.788 107.092 1.00 32.81  ?  985  HOH   A O     1 
HETATM 18213 O  O     . HOH   S 9 .   ? 170.996 135.009 129.828 1.00 30.00  ?  986  HOH   A O     1 
HETATM 18214 O  O     . HOH   S 9 .   ? 148.917 100.996 137.048 1.00 30.00  ?  987  HOH   A O     1 
HETATM 18215 O  O     . HOH   S 9 .   ? 146.109 94.243  132.996 1.00 19.89  ?  988  HOH   A O     1 
HETATM 18216 O  O     . HOH   S 9 .   ? 123.346 114.016 127.818 1.00 23.07  ?  989  HOH   A O     1 
HETATM 18217 O  O     . HOH   S 9 .   ? 160.900 110.003 144.908 1.00 36.69  ?  990  HOH   A O     1 
HETATM 18218 O  O     . HOH   S 9 .   ? 156.815 135.917 124.945 1.00 30.00  ?  991  HOH   A O     1 
HETATM 18219 O  O     . HOH   S 9 .   ? 155.956 111.989 118.054 1.00 30.00  ?  992  HOH   A O     1 
HETATM 18220 O  O     . HOH   S 9 .   ? 156.949 141.660 96.929  1.00 30.00  ?  993  HOH   A O     1 
HETATM 18221 O  O     . HOH   S 9 .   ? 135.659 129.115 127.871 1.00 30.00  ?  994  HOH   A O     1 
HETATM 18222 O  O     . HOH   S 9 .   ? 169.141 141.897 103.845 1.00 30.00  ?  995  HOH   A O     1 
HETATM 18223 O  O     . HOH   S 9 .   ? 162.976 107.040 128.239 1.00 30.00  ?  996  HOH   A O     1 
HETATM 18224 O  O     . HOH   S 9 .   ? 125.724 105.061 140.600 1.00 30.00  ?  997  HOH   A O     1 
HETATM 18225 O  O     . HOH   S 9 .   ? 128.984 113.008 142.027 1.00 25.58  ?  998  HOH   A O     1 
HETATM 18226 O  O     . HOH   S 9 .   ? 127.119 92.895  120.474 1.00 30.00  ?  999  HOH   A O     1 
HETATM 18227 O  O     . HOH   S 9 .   ? 133.553 90.150  111.003 1.00 31.26  ?  1000 HOH   A O     1 
HETATM 18228 O  O     . HOH   S 9 .   ? 139.052 81.923  126.172 1.00 30.00  ?  1001 HOH   A O     1 
HETATM 18229 O  O     . HOH   S 9 .   ? 160.958 99.200  116.426 1.00 30.00  ?  1002 HOH   A O     1 
HETATM 18230 O  O     . HOH   S 9 .   ? 129.039 95.956  132.852 1.00 30.00  ?  1003 HOH   A O     1 
HETATM 18231 O  O     . HOH   S 9 .   ? 117.813 101.373 131.148 1.00 30.00  ?  1004 HOH   A O     1 
HETATM 18232 O  O     . HOH   S 9 .   ? 123.998 117.854 123.117 1.00 30.00  ?  1005 HOH   A O     1 
HETATM 18233 O  O     . HOH   S 9 .   ? 119.913 107.989 128.962 1.00 26.68  ?  1006 HOH   A O     1 
HETATM 18234 O  O     . HOH   S 9 .   ? 125.865 103.809 142.665 1.00 34.51  ?  1007 HOH   A O     1 
HETATM 18235 O  O     . HOH   S 9 .   ? 139.805 119.043 149.110 1.00 30.00  ?  1008 HOH   A O     1 
HETATM 18236 O  O     . HOH   S 9 .   ? 151.070 116.072 145.850 1.00 35.41  ?  1009 HOH   A O     1 
HETATM 18237 O  O     . HOH   S 9 .   ? 134.848 102.998 105.791 1.00 30.00  ?  1010 HOH   A O     1 
HETATM 18238 O  O     . HOH   S 9 .   ? 136.807 128.770 127.092 1.00 30.00  ?  1011 HOH   A O     1 
HETATM 18239 O  O     . HOH   S 9 .   ? 164.626 156.824 103.535 1.00 30.00  ?  1012 HOH   A O     1 
HETATM 18240 O  O     . HOH   S 9 .   ? 131.246 113.593 141.998 1.00 30.00  ?  1013 HOH   A O     1 
HETATM 18241 O  O     . HOH   S 9 .   ? 143.181 90.147  133.981 1.00 30.00  ?  1014 HOH   A O     1 
HETATM 18242 O  O     . HOH   S 9 .   ? 155.990 124.217 123.384 1.00 29.51  ?  1015 HOH   A O     1 
HETATM 18243 O  O     . HOH   S 9 .   ? 136.926 102.986 136.137 1.00 30.00  ?  1016 HOH   A O     1 
HETATM 18244 O  O     . HOH   S 9 .   ? 154.986 96.994  126.084 1.00 30.00  ?  1017 HOH   A O     1 
HETATM 18245 O  O     . HOH   S 9 .   ? 177.091 108.281 126.586 1.00 30.00  ?  1018 HOH   A O     1 
HETATM 18246 O  O     . HOH   S 9 .   ? 166.896 114.255 146.078 1.00 30.00  ?  1019 HOH   A O     1 
HETATM 18247 O  O     . HOH   S 9 .   ? 156.005 112.067 101.196 1.00 30.00  ?  1020 HOH   A O     1 
HETATM 18248 O  O     . HOH   S 9 .   ? 175.094 123.533 114.081 1.00 30.00  ?  1021 HOH   A O     1 
HETATM 18249 O  O     . HOH   S 9 .   ? 126.951 118.590 118.920 1.00 29.03  ?  1022 HOH   A O     1 
HETATM 18250 O  O     . HOH   S 9 .   ? 138.975 126.126 126.188 1.00 19.39  ?  1023 HOH   A O     1 
HETATM 18251 O  O     . HOH   S 9 .   ? 181.051 114.157 119.913 1.00 30.00  ?  1024 HOH   A O     1 
HETATM 18252 O  O     . HOH   S 9 .   ? 167.338 151.822 129.065 1.00 30.00  ?  1025 HOH   A O     1 
HETATM 18253 O  O     . HOH   S 9 .   ? 157.221 134.118 110.991 1.00 30.00  ?  1026 HOH   A O     1 
HETATM 18254 O  O     . HOH   S 9 .   ? 151.891 88.038  129.063 1.00 30.56  ?  1027 HOH   A O     1 
HETATM 18255 O  O     . HOH   S 9 .   ? 117.844 113.695 118.047 1.00 30.00  ?  1028 HOH   A O     1 
HETATM 18256 O  O     . HOH   S 9 .   ? 144.983 123.997 95.796  1.00 30.00  ?  1029 HOH   A O     1 
HETATM 18257 O  O     . HOH   S 9 .   ? 154.739 122.834 116.005 1.00 32.18  ?  1030 HOH   A O     1 
HETATM 18258 O  O     . HOH   S 9 .   ? 161.023 107.021 119.119 1.00 30.00  ?  1031 HOH   A O     1 
HETATM 18259 O  O     . HOH   S 9 .   ? 156.048 132.016 145.093 1.00 30.00  ?  1032 HOH   A O     1 
HETATM 18260 O  O     . HOH   S 9 .   ? 128.572 88.828  121.247 1.00 30.00  ?  1033 HOH   A O     1 
HETATM 18261 O  O     . HOH   S 9 .   ? 127.042 99.109  121.249 1.00 30.00  ?  1034 HOH   A O     1 
HETATM 18262 O  O     . HOH   S 9 .   ? 169.608 113.942 102.100 1.00 30.00  ?  1035 HOH   A O     1 
HETATM 18263 O  O     . HOH   S 9 .   ? 131.940 115.950 142.037 1.00 19.72  ?  1036 HOH   A O     1 
HETATM 18264 O  O     . HOH   S 9 .   ? 141.166 97.086  133.004 1.00 30.00  ?  1037 HOH   A O     1 
HETATM 18265 O  O     . HOH   S 9 .   ? 163.051 127.007 141.032 1.00 32.93  ?  1038 HOH   A O     1 
HETATM 18266 O  O     . HOH   S 9 .   ? 146.818 87.982  117.020 1.00 30.00  ?  1039 HOH   A O     1 
HETATM 18267 O  O     . HOH   S 9 .   ? 131.304 96.617  135.017 1.00 30.00  ?  1040 HOH   A O     1 
HETATM 18268 O  O     . HOH   S 9 .   ? 155.451 129.153 124.653 1.00 30.00  ?  1041 HOH   A O     1 
HETATM 18269 O  O     . HOH   S 9 .   ? 151.430 116.005 136.029 1.00 30.00  ?  1042 HOH   A O     1 
HETATM 18270 O  O     . HOH   S 9 .   ? 126.917 122.022 123.896 1.00 30.00  ?  1043 HOH   A O     1 
HETATM 18271 O  O     . HOH   S 9 .   ? 129.119 115.976 102.043 1.00 30.00  ?  1044 HOH   A O     1 
HETATM 18272 O  O     . HOH   S 9 .   ? 160.037 136.111 124.208 1.00 30.00  ?  1045 HOH   A O     1 
HETATM 18273 O  O     . HOH   S 9 .   ? 128.374 101.288 117.172 1.00 30.00  ?  1046 HOH   A O     1 
HETATM 18274 O  O     . HOH   S 9 .   ? 148.938 95.080  131.983 1.00 27.06  ?  1047 HOH   A O     1 
HETATM 18275 O  O     . HOH   S 9 .   ? 133.105 98.816  137.780 1.00 30.00  ?  1048 HOH   A O     1 
HETATM 18276 O  O     . HOH   S 9 .   ? 126.045 124.166 124.894 1.00 25.70  ?  1049 HOH   A O     1 
HETATM 18277 O  O     . HOH   S 9 .   ? 149.014 97.846  134.150 1.00 30.00  ?  1050 HOH   A O     1 
HETATM 18278 O  O     . HOH   T 9 .   ? 114.996 98.383  149.043 1.00 30.00  ?  901  HOH   B O     1 
HETATM 18279 O  O     . HOH   T 9 .   ? 90.800  104.102 134.061 1.00 30.00  ?  902  HOH   B O     1 
HETATM 18280 O  O     . HOH   T 9 .   ? 114.147 126.991 146.014 1.00 30.00  ?  903  HOH   B O     1 
HETATM 18281 O  O     . HOH   T 9 .   ? 124.905 141.509 138.047 1.00 30.00  ?  904  HOH   B O     1 
HETATM 18282 O  O     . HOH   T 9 .   ? 88.793  107.565 107.050 1.00 30.00  ?  905  HOH   B O     1 
HETATM 18283 O  O     . HOH   T 9 .   ? 113.601 131.166 140.575 1.00 30.00  ?  906  HOH   B O     1 
HETATM 18284 O  O     . HOH   T 9 .   ? 96.370  112.997 143.049 1.00 30.00  ?  907  HOH   B O     1 
HETATM 18285 O  O     . HOH   T 9 .   ? 91.938  119.523 132.926 1.00 30.00  ?  908  HOH   B O     1 
HETATM 18286 O  O     . HOH   T 9 .   ? 118.108 138.990 146.867 1.00 30.00  ?  909  HOH   B O     1 
HETATM 18287 O  O     . HOH   T 9 .   ? 119.113 144.005 136.029 1.00 30.00  ?  910  HOH   B O     1 
HETATM 18288 O  O     . HOH   T 9 .   ? 102.828 82.088  148.157 1.00 30.00  ?  911  HOH   B O     1 
HETATM 18289 O  O     . HOH   T 9 .   ? 99.973  125.738 158.192 1.00 30.00  ?  912  HOH   B O     1 
HETATM 18290 O  O     . HOH   T 9 .   ? 94.992  106.005 134.906 1.00 31.97  ?  913  HOH   B O     1 
HETATM 18291 O  O     . HOH   T 9 .   ? 97.897  102.841 141.589 1.00 30.00  ?  914  HOH   B O     1 
HETATM 18292 O  O     . HOH   T 9 .   ? 101.241 105.860 130.973 1.00 30.00  ?  915  HOH   B O     1 
HETATM 18293 O  O     . HOH   T 9 .   ? 123.098 143.007 134.097 1.00 30.00  ?  916  HOH   B O     1 
HETATM 18294 O  O     . HOH   T 9 .   ? 83.846  120.296 154.070 1.00 30.00  ?  917  HOH   B O     1 
HETATM 18295 O  O     . HOH   T 9 .   ? 104.142 108.915 136.010 1.00 30.00  ?  918  HOH   B O     1 
HETATM 18296 O  O     . HOH   T 9 .   ? 90.073  111.765 137.870 1.00 23.92  ?  919  HOH   B O     1 
HETATM 18297 O  O     . HOH   T 9 .   ? 135.147 133.107 136.877 1.00 30.00  ?  920  HOH   B O     1 
HETATM 18298 O  O     . HOH   T 9 .   ? 87.093  113.899 125.743 1.00 22.75  ?  921  HOH   B O     1 
HETATM 18299 O  O     . HOH   T 9 .   ? 101.960 87.038  141.961 1.00 21.17  ?  922  HOH   B O     1 
HETATM 18300 O  O     . HOH   T 9 .   ? 92.982  116.989 131.913 1.00 30.00  ?  923  HOH   B O     1 
HETATM 18301 O  O     . HOH   T 9 .   ? 102.896 71.862  129.984 1.00 30.00  ?  924  HOH   B O     1 
HETATM 18302 O  O     . HOH   T 9 .   ? 87.896  131.075 133.808 1.00 26.91  ?  925  HOH   B O     1 
HETATM 18303 O  O     . HOH   T 9 .   ? 96.840  107.930 132.860 1.00 30.00  ?  926  HOH   B O     1 
HETATM 18304 O  O     . HOH   T 9 .   ? 92.057  110.808 133.962 1.00 21.16  ?  927  HOH   B O     1 
HETATM 18305 O  O     . HOH   T 9 .   ? 121.995 94.251  148.942 1.00 30.00  ?  928  HOH   B O     1 
HETATM 18306 O  O     . HOH   T 9 .   ? 92.160  127.542 146.966 1.00 30.00  ?  929  HOH   B O     1 
HETATM 18307 O  O     . HOH   T 9 .   ? 92.148  132.953 154.897 1.00 30.00  ?  930  HOH   B O     1 
HETATM 18308 O  O     . HOH   T 9 .   ? 106.307 104.261 160.523 1.00 30.00  ?  931  HOH   B O     1 
HETATM 18309 O  O     . HOH   T 9 .   ? 120.010 93.883  126.073 1.00 30.00  ?  932  HOH   B O     1 
HETATM 18310 O  O     . HOH   T 9 .   ? 97.889  132.224 137.845 1.00 28.78  ?  933  HOH   B O     1 
HETATM 18311 O  O     . HOH   T 9 .   ? 117.902 140.022 144.735 1.00 30.00  ?  934  HOH   B O     1 
HETATM 18312 O  O     . HOH   T 9 .   ? 82.033  121.966 139.121 1.00 30.00  ?  935  HOH   B O     1 
HETATM 18313 O  O     . HOH   T 9 .   ? 108.844 121.943 121.879 1.00 34.69  ?  936  HOH   B O     1 
HETATM 18314 O  O     . HOH   T 9 .   ? 96.461  127.844 129.929 1.00 34.44  ?  937  HOH   B O     1 
HETATM 18315 O  O     . HOH   T 9 .   ? 85.832  133.223 125.931 1.00 30.00  ?  938  HOH   B O     1 
HETATM 18316 O  O     . HOH   T 9 .   ? 97.837  124.063 141.180 1.00 30.00  ?  939  HOH   B O     1 
HETATM 18317 O  O     . HOH   T 9 .   ? 124.970 111.031 151.547 1.00 30.00  ?  940  HOH   B O     1 
HETATM 18318 O  O     . HOH   T 9 .   ? 101.279 100.791 166.083 1.00 30.00  ?  941  HOH   B O     1 
HETATM 18319 O  O     . HOH   T 9 .   ? 115.028 143.931 151.929 1.00 30.00  ?  942  HOH   B O     1 
HETATM 18320 O  O     . HOH   T 9 .   ? 83.512  97.976  132.935 1.00 30.00  ?  943  HOH   B O     1 
HETATM 18321 O  O     . HOH   T 9 .   ? 95.858  72.123  116.505 1.00 30.00  ?  944  HOH   B O     1 
HETATM 18322 O  O     . HOH   T 9 .   ? 112.030 94.893  163.936 1.00 30.00  ?  945  HOH   B O     1 
HETATM 18323 O  O     . HOH   T 9 .   ? 101.279 88.816  139.048 1.00 24.67  ?  946  HOH   B O     1 
HETATM 18324 O  O     . HOH   T 9 .   ? 97.998  95.472  162.995 1.00 25.14  ?  947  HOH   B O     1 
HETATM 18325 O  O     . HOH   T 9 .   ? 100.919 94.047  124.118 1.00 30.00  ?  948  HOH   B O     1 
HETATM 18326 O  O     . HOH   T 9 .   ? 115.824 125.889 158.325 1.00 30.00  ?  949  HOH   B O     1 
HETATM 18327 O  O     . HOH   T 9 .   ? 78.964  119.112 159.903 1.00 30.00  ?  950  HOH   B O     1 
HETATM 18328 O  O     . HOH   T 9 .   ? 99.457  97.098  124.075 1.00 30.00  ?  951  HOH   B O     1 
HETATM 18329 O  O     . HOH   T 9 .   ? 85.840  94.978  120.786 1.00 30.00  ?  952  HOH   B O     1 
HETATM 18330 O  O     . HOH   T 9 .   ? 91.720  98.982  131.118 1.00 30.00  ?  953  HOH   B O     1 
HETATM 18331 O  O     . HOH   T 9 .   ? 100.051 106.975 142.465 1.00 29.51  ?  954  HOH   B O     1 
HETATM 18332 O  O     . HOH   T 9 .   ? 97.850  114.874 117.006 1.00 24.16  ?  955  HOH   B O     1 
HETATM 18333 O  O     . HOH   T 9 .   ? 88.096  133.116 119.120 1.00 30.00  ?  956  HOH   B O     1 
HETATM 18334 O  O     . HOH   T 9 .   ? 98.819  123.516 124.052 1.00 30.00  ?  957  HOH   B O     1 
HETATM 18335 O  O     . HOH   T 9 .   ? 110.035 117.786 128.087 1.00 30.00  ?  958  HOH   B O     1 
HETATM 18336 O  O     . HOH   T 9 .   ? 94.964  99.991  133.905 1.00 30.00  ?  959  HOH   B O     1 
HETATM 18337 O  O     . HOH   T 9 .   ? 110.194 122.034 158.285 1.00 30.00  ?  960  HOH   B O     1 
HETATM 18338 O  O     . HOH   T 9 .   ? 92.878  108.047 132.662 1.00 30.00  ?  961  HOH   B O     1 
HETATM 18339 O  O     . HOH   T 9 .   ? 85.991  99.862  133.186 1.00 30.00  ?  962  HOH   B O     1 
HETATM 18340 O  O     . HOH   T 9 .   ? 109.123 146.915 153.165 1.00 30.00  ?  963  HOH   B O     1 
HETATM 18341 O  O     . HOH   T 9 .   ? 78.816  119.098 145.890 1.00 30.00  ?  964  HOH   B O     1 
HETATM 18342 O  O     . HOH   T 9 .   ? 90.919  112.094 106.060 1.00 30.00  ?  965  HOH   B O     1 
HETATM 18343 O  O     . HOH   T 9 .   ? 98.049  82.086  150.012 1.00 30.00  ?  966  HOH   B O     1 
HETATM 18344 O  O     . HOH   T 9 .   ? 97.059  125.006 143.325 1.00 29.75  ?  967  HOH   B O     1 
HETATM 18345 O  O     . HOH   T 9 .   ? 103.914 82.108  128.039 1.00 24.93  ?  968  HOH   B O     1 
HETATM 18346 O  O     . HOH   T 9 .   ? 90.027  106.308 129.912 1.00 30.00  ?  969  HOH   B O     1 
HETATM 18347 O  O     . HOH   T 9 .   ? 98.704  74.761  127.038 1.00 30.00  ?  970  HOH   B O     1 
HETATM 18348 O  O     . HOH   T 9 .   ? 83.755  112.145 136.330 1.00 30.00  ?  971  HOH   B O     1 
HETATM 18349 O  O     . HOH   T 9 .   ? 89.325  104.622 158.832 1.00 21.68  ?  972  HOH   B O     1 
HETATM 18350 O  O     . HOH   T 9 .   ? 118.026 131.949 134.872 1.00 30.00  ?  973  HOH   B O     1 
HETATM 18351 O  O     . HOH   T 9 .   ? 100.013 129.029 156.041 1.00 25.39  ?  974  HOH   B O     1 
HETATM 18352 O  O     . HOH   T 9 .   ? 83.014  83.069  131.947 1.00 30.00  ?  975  HOH   B O     1 
HETATM 18353 O  O     . HOH   T 9 .   ? 85.115  127.010 126.051 1.00 30.00  ?  976  HOH   B O     1 
HETATM 18354 O  O     . HOH   T 9 .   ? 98.061  93.836  116.957 1.00 30.00  ?  977  HOH   B O     1 
HETATM 18355 O  O     . HOH   T 9 .   ? 109.839 103.736 129.886 1.00 30.00  ?  978  HOH   B O     1 
HETATM 18356 O  O     . HOH   T 9 .   ? 90.863  114.134 108.525 1.00 30.00  ?  979  HOH   B O     1 
HETATM 18357 O  O     . HOH   T 9 .   ? 102.088 76.077  137.735 1.00 26.57  ?  980  HOH   B O     1 
HETATM 18358 O  O     . HOH   T 9 .   ? 82.914  114.924 161.118 1.00 30.00  ?  981  HOH   B O     1 
HETATM 18359 O  O     . HOH   T 9 .   ? 110.052 109.988 132.049 1.00 17.39  ?  982  HOH   B O     1 
HETATM 18360 O  O     . HOH   T 9 .   ? 104.592 150.821 133.987 1.00 30.00  ?  983  HOH   B O     1 
HETATM 18361 O  O     . HOH   T 9 .   ? 107.051 109.156 140.579 1.00 28.14  ?  984  HOH   B O     1 
HETATM 18362 O  O     . HOH   T 9 .   ? 124.913 117.905 150.181 1.00 30.00  ?  985  HOH   B O     1 
HETATM 18363 O  O     . HOH   T 9 .   ? 84.541  83.587  124.007 1.00 30.00  ?  986  HOH   B O     1 
HETATM 18364 O  O     . HOH   T 9 .   ? 114.156 112.851 161.035 1.00 32.32  ?  987  HOH   B O     1 
HETATM 18365 O  O     . HOH   T 9 .   ? 126.352 124.504 127.730 1.00 27.33  ?  988  HOH   B O     1 
HETATM 18366 O  O     . HOH   T 9 .   ? 107.053 146.041 125.683 1.00 30.00  ?  989  HOH   B O     1 
HETATM 18367 O  O     . HOH   T 9 .   ? 128.309 134.341 143.446 1.00 80.95  ?  990  HOH   B O     1 
HETATM 18368 O  O     . HOH   T 9 .   ? 112.077 125.914 147.589 1.00 27.17  ?  991  HOH   B O     1 
HETATM 18369 O  O     . HOH   T 9 .   ? 102.883 109.157 141.908 1.00 30.00  ?  992  HOH   B O     1 
HETATM 18370 O  O     . HOH   T 9 .   ? 108.517 106.017 161.074 1.00 30.00  ?  993  HOH   B O     1 
HETATM 18371 O  O     . HOH   T 9 .   ? 116.062 100.941 158.365 1.00 30.00  ?  994  HOH   B O     1 
HETATM 18372 O  O     . HOH   T 9 .   ? 88.023  124.972 125.024 1.00 21.12  ?  995  HOH   B O     1 
HETATM 18373 O  O     . HOH   T 9 .   ? 117.134 94.268  141.880 1.00 26.10  ?  996  HOH   B O     1 
HETATM 18374 O  O     . HOH   T 9 .   ? 81.000  125.887 124.689 1.00 30.00  ?  997  HOH   B O     1 
HETATM 18375 O  O     . HOH   T 9 .   ? 94.991  129.895 130.516 1.00 30.00  ?  998  HOH   B O     1 
HETATM 18376 O  O     . HOH   T 9 .   ? 131.991 129.833 142.041 1.00 29.38  ?  999  HOH   B O     1 
HETATM 18377 O  O     . HOH   T 9 .   ? 85.779  120.900 123.961 1.00 30.00  ?  1000 HOH   B O     1 
HETATM 18378 O  O     . HOH   T 9 .   ? 85.861  122.849 133.240 1.00 30.00  ?  1001 HOH   B O     1 
HETATM 18379 O  O     . HOH   T 9 .   ? 98.901  124.986 151.833 1.00 30.00  ?  1002 HOH   B O     1 
HETATM 18380 O  O     . HOH   T 9 .   ? 89.503  102.096 139.781 1.00 30.00  ?  1003 HOH   B O     1 
HETATM 18381 O  O     . HOH   T 9 .   ? 109.126 83.031  116.015 1.00 33.14  ?  1004 HOH   B O     1 
HETATM 18382 O  O     . HOH   T 9 .   ? 85.995  121.910 165.931 1.00 30.00  ?  1005 HOH   B O     1 
HETATM 18383 O  O     . HOH   T 9 .   ? 100.817 102.015 141.976 1.00 27.01  ?  1006 HOH   B O     1 
HETATM 18384 O  O     . HOH   T 9 .   ? 119.104 122.964 146.862 1.00 26.93  ?  1007 HOH   B O     1 
HETATM 18385 O  O     . HOH   T 9 .   ? 127.777 116.957 136.389 1.00 30.00  ?  1008 HOH   B O     1 
HETATM 18386 O  O     . HOH   T 9 .   ? 121.153 119.988 159.976 1.00 30.00  ?  1009 HOH   B O     1 
HETATM 18387 O  O     . HOH   T 9 .   ? 104.067 124.117 150.272 1.00 30.00  ?  1010 HOH   B O     1 
HETATM 18388 O  O     . HOH   T 9 .   ? 76.044  108.362 139.030 1.00 30.00  ?  1011 HOH   B O     1 
HETATM 18389 O  O     . HOH   T 9 .   ? 106.943 71.705  126.517 1.00 30.00  ?  1012 HOH   B O     1 
HETATM 18390 O  O     . HOH   T 9 .   ? 102.964 90.755  163.963 1.00 30.00  ?  1013 HOH   B O     1 
HETATM 18391 O  O     . HOH   T 9 .   ? 102.412 113.961 133.397 1.00 30.93  ?  1014 HOH   B O     1 
HETATM 18392 O  O     . HOH   T 9 .   ? 121.935 120.088 125.619 1.00 25.84  ?  1015 HOH   B O     1 
HETATM 18393 O  O     . HOH   T 9 .   ? 90.348  125.623 114.565 1.00 30.00  ?  1016 HOH   B O     1 
HETATM 18394 O  O     . HOH   T 9 .   ? 84.861  112.988 134.392 1.00 30.00  ?  1017 HOH   B O     1 
HETATM 18395 O  O     . HOH   T 9 .   ? 101.327 104.046 129.051 1.00 30.00  ?  1018 HOH   B O     1 
HETATM 18396 O  O     . HOH   T 9 .   ? 92.138  109.906 129.304 1.00 30.00  ?  1019 HOH   B O     1 
HETATM 18397 O  O     . HOH   T 9 .   ? 112.104 84.055  139.908 1.00 30.00  ?  1020 HOH   B O     1 
HETATM 18398 O  O     . HOH   T 9 .   ? 82.997  91.565  133.910 1.00 30.00  ?  1021 HOH   B O     1 
HETATM 18399 O  O     . HOH   T 9 .   ? 113.515 132.509 119.861 1.00 30.00  ?  1022 HOH   B O     1 
HETATM 18400 O  O     . HOH   T 9 .   ? 103.906 89.268  128.990 1.00 26.39  ?  1023 HOH   B O     1 
HETATM 18401 O  O     . HOH   T 9 .   ? 114.110 139.138 127.924 1.00 20.29  ?  1024 HOH   B O     1 
HETATM 18402 O  O     . HOH   T 9 .   ? 109.976 116.065 140.997 1.00 30.82  ?  1025 HOH   B O     1 
HETATM 18403 O  O     . HOH   T 9 .   ? 93.022  98.124  129.970 1.00 18.57  ?  1026 HOH   B O     1 
HETATM 18404 O  O     . HOH   T 9 .   ? 103.891 112.948 135.778 1.00 27.59  ?  1027 HOH   B O     1 
HETATM 18405 O  O     . HOH   T 9 .   ? 96.668  116.254 137.152 1.00 30.00  ?  1028 HOH   B O     1 
HETATM 18406 O  O     . HOH   T 9 .   ? 92.844  113.948 131.032 1.00 32.32  ?  1029 HOH   B O     1 
HETATM 18407 O  O     . HOH   T 9 .   ? 103.831 114.413 173.065 1.00 30.00  ?  1030 HOH   B O     1 
HETATM 18408 O  O     . HOH   T 9 .   ? 115.908 138.032 126.173 1.00 30.00  ?  1031 HOH   B O     1 
HETATM 18409 O  O     . HOH   T 9 .   ? 102.967 131.126 118.918 1.00 20.00  ?  1032 HOH   B O     1 
HETATM 18410 O  O     . HOH   T 9 .   ? 92.998  98.027  156.936 1.00 30.00  ?  1033 HOH   B O     1 
HETATM 18411 O  O     . HOH   T 9 .   ? 121.021 102.863 147.509 1.00 29.67  ?  1034 HOH   B O     1 
HETATM 18412 O  O     . HOH   T 9 .   ? 93.883  97.208  137.005 1.00 21.81  ?  1035 HOH   B O     1 
HETATM 18413 O  O     . HOH   T 9 .   ? 122.238 107.876 153.162 1.00 30.00  ?  1036 HOH   B O     1 
HETATM 18414 O  O     . HOH   T 9 .   ? 111.129 136.126 122.789 1.00 25.07  ?  1037 HOH   B O     1 
HETATM 18415 O  O     . HOH   T 9 .   ? 117.027 110.035 130.000 1.00 30.83  ?  1038 HOH   B O     1 
HETATM 18416 O  O     . HOH   T 9 .   ? 93.750  93.950  156.020 1.00 30.00  ?  1039 HOH   B O     1 
HETATM 18417 O  O     . HOH   T 9 .   ? 114.083 114.041 126.193 1.00 30.00  ?  1040 HOH   B O     1 
HETATM 18418 O  O     . HOH   T 9 .   ? 87.996  128.210 129.948 1.00 30.00  ?  1041 HOH   B O     1 
HETATM 18419 O  O     . HOH   T 9 .   ? 121.143 131.925 122.778 1.00 30.00  ?  1042 HOH   B O     1 
HETATM 18420 O  O     . HOH   T 9 .   ? 96.058  129.137 148.056 1.00 26.16  ?  1043 HOH   B O     1 
HETATM 18421 O  O     . HOH   T 9 .   ? 108.005 108.947 146.028 1.00 32.30  ?  1044 HOH   B O     1 
HETATM 18422 O  O     . HOH   T 9 .   ? 85.960  115.325 163.891 1.00 30.00  ?  1045 HOH   B O     1 
HETATM 18423 O  O     . HOH   T 9 .   ? 100.216 146.038 129.430 1.00 23.72  ?  1046 HOH   B O     1 
HETATM 18424 O  O     . HOH   T 9 .   ? 94.094  97.041  154.995 1.00 30.00  ?  1047 HOH   B O     1 
HETATM 18425 O  O     . HOH   T 9 .   ? 117.022 123.017 115.716 1.00 27.91  ?  1048 HOH   B O     1 
HETATM 18426 O  O     . HOH   T 9 .   ? 120.971 105.933 146.883 1.00 30.00  ?  1049 HOH   B O     1 
HETATM 18427 O  O     . HOH   T 9 .   ? 102.846 126.046 149.009 1.00 22.49  ?  1050 HOH   B O     1 
HETATM 18428 O  O     . HOH   T 9 .   ? 119.934 149.042 131.967 1.00 30.00  ?  1051 HOH   B O     1 
HETATM 18429 O  O     . HOH   T 9 .   ? 105.032 73.046  130.090 1.00 30.00  ?  1052 HOH   B O     1 
HETATM 18430 O  O     . HOH   T 9 .   ? 93.765  79.521  136.037 1.00 30.00  ?  1053 HOH   B O     1 
HETATM 18431 O  O     . HOH   T 9 .   ? 103.484 138.752 151.780 1.00 30.00  ?  1054 HOH   B O     1 
HETATM 18432 O  O     . HOH   T 9 .   ? 111.063 132.019 116.070 1.00 30.00  ?  1055 HOH   B O     1 
HETATM 18433 O  O     . HOH   T 9 .   ? 103.326 105.902 131.896 1.00 30.00  ?  1056 HOH   B O     1 
HETATM 18434 O  O     . HOH   T 9 .   ? 112.009 106.108 121.223 1.00 30.66  ?  1057 HOH   B O     1 
HETATM 18435 O  O     . HOH   T 9 .   ? 111.057 82.164  142.457 1.00 22.73  ?  1058 HOH   B O     1 
HETATM 18436 O  O     . HOH   T 9 .   ? 123.110 114.972 156.001 1.00 30.00  ?  1059 HOH   B O     1 
HETATM 18437 O  O     . HOH   T 9 .   ? 96.247  97.977  121.357 1.00 30.00  ?  1060 HOH   B O     1 
HETATM 18438 O  O     . HOH   T 9 .   ? 98.781  135.001 148.202 1.00 35.15  ?  1061 HOH   B O     1 
HETATM 18439 O  O     . HOH   T 9 .   ? 113.097 134.094 149.933 1.00 30.00  ?  1062 HOH   B O     1 
HETATM 18440 O  O     . HOH   T 9 .   ? 94.006  109.014 160.283 1.00 30.00  ?  1063 HOH   B O     1 
HETATM 18441 O  O     . HOH   T 9 .   ? 78.027  122.089 144.882 1.00 25.72  ?  1064 HOH   B O     1 
HETATM 18442 O  O     . HOH   T 9 .   ? 112.745 80.769  161.083 1.00 37.30  ?  1065 HOH   B O     1 
HETATM 18443 O  O     . HOH   T 9 .   ? 105.044 136.011 149.681 1.00 30.00  ?  1066 HOH   B O     1 
HETATM 18444 O  O     . HOH   T 9 .   ? 113.060 119.943 152.020 1.00 30.00  ?  1067 HOH   B O     1 
HETATM 18445 O  O     . HOH   T 9 .   ? 112.115 117.734 152.153 1.00 30.00  ?  1068 HOH   B O     1 
HETATM 18446 O  O     . HOH   T 9 .   ? 87.900  100.941 142.337 1.00 30.00  ?  1069 HOH   B O     1 
HETATM 18447 O  O     . HOH   T 9 .   ? 96.277  115.066 132.010 1.00 30.00  ?  1070 HOH   B O     1 
HETATM 18448 O  O     . HOH   T 9 .   ? 107.828 128.028 166.029 1.00 30.00  ?  1071 HOH   B O     1 
HETATM 18449 O  O     . HOH   T 9 .   ? 111.235 121.268 165.998 1.00 26.17  ?  1072 HOH   B O     1 
HETATM 18450 O  O     . HOH   T 9 .   ? 100.538 95.082  116.247 1.00 30.00  ?  1073 HOH   B O     1 
HETATM 18451 O  O     . HOH   T 9 .   ? 95.853  115.009 138.923 1.00 25.50  ?  1074 HOH   B O     1 
HETATM 18452 O  O     . HOH   T 9 .   ? 98.650  127.031 156.813 1.00 30.00  ?  1075 HOH   B O     1 
HETATM 18453 O  O     . HOH   T 9 .   ? 90.093  121.953 117.058 1.00 17.93  ?  1076 HOH   B O     1 
HETATM 18454 O  O     . HOH   T 9 .   ? 90.055  100.846 141.515 1.00 36.24  ?  1077 HOH   B O     1 
HETATM 18455 O  O     . HOH   T 9 .   ? 96.408  92.997  142.999 1.00 30.00  ?  1078 HOH   B O     1 
HETATM 18456 O  O     . HOH   T 9 .   ? 83.978  90.201  120.071 1.00 30.00  ?  1079 HOH   B O     1 
HETATM 18457 O  O     . HOH   T 9 .   ? 105.008 109.924 133.229 1.00 23.10  ?  1080 HOH   B O     1 
HETATM 18458 O  O     . HOH   T 9 .   ? 103.747 139.040 122.853 1.00 18.76  ?  1081 HOH   B O     1 
HETATM 18459 O  O     . HOH   T 9 .   ? 121.958 132.905 127.664 1.00 30.00  ?  1082 HOH   B O     1 
HETATM 18460 O  O     . HOH   T 9 .   ? 95.079  125.953 123.078 1.00 30.00  ?  1083 HOH   B O     1 
HETATM 18461 O  O     . HOH   T 9 .   ? 88.760  97.957  119.147 1.00 30.00  ?  1084 HOH   B O     1 
HETATM 18462 O  O     . HOH   T 9 .   ? 120.279 139.873 147.092 1.00 30.00  ?  1085 HOH   B O     1 
HETATM 18463 O  O     . HOH   T 9 .   ? 119.034 117.157 158.953 1.00 28.74  ?  1086 HOH   B O     1 
HETATM 18464 O  O     . HOH   T 9 .   ? 130.665 132.764 144.314 1.00 88.87  ?  1087 HOH   B O     1 
HETATM 18465 O  O     . HOH   T 9 .   ? 106.409 120.653 123.990 1.00 30.00  ?  1088 HOH   B O     1 
HETATM 18466 O  O     . HOH   T 9 .   ? 82.969  124.553 133.969 1.00 30.00  ?  1089 HOH   B O     1 
HETATM 18467 O  O     . HOH   T 9 .   ? 130.570 135.693 144.797 1.00 72.97  ?  1090 HOH   B O     1 
HETATM 18468 O  O     . HOH   T 9 .   ? 114.976 97.147  136.969 1.00 28.33  ?  1091 HOH   B O     1 
HETATM 18469 O  O     . HOH   T 9 .   ? 117.063 121.083 122.851 1.00 14.34  ?  1092 HOH   B O     1 
HETATM 18470 O  O     . HOH   T 9 .   ? 98.103  115.647 126.166 1.00 26.25  ?  1093 HOH   B O     1 
HETATM 18471 O  O     . HOH   T 9 .   ? 112.052 100.145 157.640 1.00 30.00  ?  1094 HOH   B O     1 
HETATM 18472 O  O     . HOH   T 9 .   ? 114.318 140.917 151.044 1.00 30.94  ?  1095 HOH   B O     1 
HETATM 18473 O  O     . HOH   T 9 .   ? 96.298  131.949 149.024 1.00 30.00  ?  1096 HOH   B O     1 
HETATM 18474 O  O     . HOH   T 9 .   ? 85.008  107.950 124.056 1.00 17.98  ?  1097 HOH   B O     1 
HETATM 18475 O  O     . HOH   T 9 .   ? 112.132 102.113 158.977 1.00 30.00  ?  1098 HOH   B O     1 
HETATM 18476 O  O     . HOH   T 9 .   ? 86.830  122.090 126.147 1.00 29.09  ?  1099 HOH   B O     1 
HETATM 18477 O  O     . HOH   T 9 .   ? 115.987 131.953 123.222 1.00 34.09  ?  1100 HOH   B O     1 
HETATM 18478 O  O     . HOH   T 9 .   ? 102.165 75.449  134.978 1.00 30.00  ?  1101 HOH   B O     1 
HETATM 18479 O  O     . HOH   T 9 .   ? 110.805 107.132 128.943 1.00 25.03  ?  1102 HOH   B O     1 
HETATM 18480 O  O     . HOH   T 9 .   ? 120.088 83.831  149.832 1.00 30.00  ?  1103 HOH   B O     1 
HETATM 18481 O  O     . HOH   T 9 .   ? 97.907  119.012 124.107 1.00 30.00  ?  1104 HOH   B O     1 
HETATM 18482 O  O     . HOH   T 9 .   ? 112.040 97.103  139.033 1.00 24.49  ?  1105 HOH   B O     1 
HETATM 18483 O  O     . HOH   T 9 .   ? 92.317  136.122 150.394 1.00 30.00  ?  1106 HOH   B O     1 
HETATM 18484 O  O     . HOH   T 9 .   ? 102.941 79.025  154.794 1.00 30.00  ?  1107 HOH   B O     1 
HETATM 18485 O  O     . HOH   T 9 .   ? 107.208 76.053  146.791 1.00 30.00  ?  1108 HOH   B O     1 
HETATM 18486 O  O     . HOH   T 9 .   ? 119.844 109.973 126.112 1.00 25.40  ?  1109 HOH   B O     1 
HETATM 18487 O  O     . HOH   T 9 .   ? 98.955  139.836 122.046 1.00 30.00  ?  1110 HOH   B O     1 
HETATM 18488 O  O     . HOH   T 9 .   ? 85.903  102.091 121.902 1.00 16.74  ?  1111 HOH   B O     1 
HETATM 18489 O  O     . HOH   T 9 .   ? 90.949  96.618  137.013 1.00 30.00  ?  1112 HOH   B O     1 
HETATM 18490 O  O     . HOH   T 9 .   ? 97.347  100.028 144.077 1.00 30.00  ?  1113 HOH   B O     1 
HETATM 18491 O  O     . HOH   T 9 .   ? 90.071  113.348 117.038 1.00 30.00  ?  1114 HOH   B O     1 
HETATM 18492 O  O     . HOH   T 9 .   ? 96.515  117.366 124.148 1.00 32.84  ?  1115 HOH   B O     1 
HETATM 18493 O  O     . HOH   T 9 .   ? 92.257  92.996  144.018 1.00 24.18  ?  1116 HOH   B O     1 
HETATM 18494 O  O     . HOH   T 9 .   ? 95.027  92.141  116.011 1.00 30.00  ?  1117 HOH   B O     1 
HETATM 18495 O  O     . HOH   T 9 .   ? 123.498 133.035 144.862 1.00 30.00  ?  1118 HOH   B O     1 
HETATM 18496 O  O     . HOH   T 9 .   ? 123.582 136.952 142.485 1.00 30.00  ?  1119 HOH   B O     1 
HETATM 18497 O  O     . HOH   T 9 .   ? 109.169 117.857 124.876 1.00 30.00  ?  1120 HOH   B O     1 
HETATM 18498 O  O     . HOH   T 9 .   ? 90.772  106.195 132.755 1.00 22.62  ?  1121 HOH   B O     1 
HETATM 18499 O  O     . HOH   T 9 .   ? 127.002 141.030 138.970 1.00 23.81  ?  1122 HOH   B O     1 
HETATM 18500 O  O     . HOH   T 9 .   ? 86.722  106.497 123.387 1.00 30.00  ?  1123 HOH   B O     1 
HETATM 18501 O  O     . HOH   T 9 .   ? 109.865 131.921 118.500 1.00 24.56  ?  1124 HOH   B O     1 
HETATM 18502 O  O     . HOH   T 9 .   ? 114.087 148.987 128.053 1.00 30.00  ?  1125 HOH   B O     1 
HETATM 18503 O  O     . HOH   T 9 .   ? 115.700 78.990  147.072 1.00 30.00  ?  1126 HOH   B O     1 
HETATM 18504 O  O     . HOH   T 9 .   ? 85.297  128.298 151.869 1.00 30.00  ?  1127 HOH   B O     1 
HETATM 18505 O  O     . HOH   T 9 .   ? 130.056 141.128 139.998 1.00 30.00  ?  1128 HOH   B O     1 
HETATM 18506 O  O     . HOH   T 9 .   ? 98.005  115.060 130.146 1.00 30.00  ?  1129 HOH   B O     1 
HETATM 18507 O  O     . HOH   T 9 .   ? 112.106 103.892 138.981 1.00 30.00  ?  1130 HOH   B O     1 
HETATM 18508 O  O     . HOH   T 9 .   ? 95.894  82.972  140.030 1.00 30.00  ?  1131 HOH   B O     1 
HETATM 18509 O  O     . HOH   T 9 .   ? 115.353 98.109  157.238 1.00 30.00  ?  1132 HOH   B O     1 
HETATM 18510 O  O     . HOH   T 9 .   ? 99.236  107.065 163.100 1.00 32.29  ?  1133 HOH   B O     1 
HETATM 18511 O  O     . HOH   T 9 .   ? 92.127  116.063 119.272 1.00 30.00  ?  1134 HOH   B O     1 
HETATM 18512 O  O     . HOH   T 9 .   ? 88.034  121.207 131.395 1.00 30.00  ?  1135 HOH   B O     1 
HETATM 18513 O  O     . HOH   T 9 .   ? 97.932  115.834 134.884 1.00 18.37  ?  1136 HOH   B O     1 
HETATM 18514 O  O     . HOH   T 9 .   ? 92.159  92.082  117.034 1.00 30.00  ?  1137 HOH   B O     1 
HETATM 18515 O  O     . HOH   T 9 .   ? 131.049 121.996 143.102 1.00 19.70  ?  1138 HOH   B O     1 
HETATM 18516 O  O     . HOH   T 9 .   ? 103.675 86.988  114.982 1.00 30.00  ?  1139 HOH   B O     1 
HETATM 18517 O  O     . HOH   T 9 .   ? 105.963 124.128 119.986 1.00 32.02  ?  1140 HOH   B O     1 
HETATM 18518 O  O     . HOH   T 9 .   ? 99.947  108.097 129.867 1.00 30.00  ?  1141 HOH   B O     1 
HETATM 18519 O  O     . HOH   T 9 .   ? 123.292 106.379 141.042 1.00 30.00  ?  1142 HOH   B O     1 
HETATM 18520 O  O     . HOH   T 9 .   ? 94.077  129.008 149.019 1.00 30.00  ?  1143 HOH   B O     1 
HETATM 18521 O  O     . HOH   T 9 .   ? 134.096 130.626 139.871 1.00 30.00  ?  1144 HOH   B O     1 
HETATM 18522 O  O     . HOH   T 9 .   ? 102.960 141.102 145.068 1.00 30.00  ?  1145 HOH   B O     1 
HETATM 18523 O  O     . HOH   T 9 .   ? 84.008  115.555 155.979 1.00 30.00  ?  1146 HOH   B O     1 
HETATM 18524 O  O     . HOH   T 9 .   ? 90.124  100.875 117.719 1.00 30.00  ?  1147 HOH   B O     1 
HETATM 18525 O  O     . HOH   T 9 .   ? 102.131 91.938  122.753 1.00 29.01  ?  1148 HOH   B O     1 
HETATM 18526 O  O     . HOH   T 9 .   ? 99.530  100.028 143.944 1.00 32.19  ?  1149 HOH   B O     1 
HETATM 18527 O  O     . HOH   T 9 .   ? 105.479 121.887 119.996 1.00 30.00  ?  1150 HOH   B O     1 
HETATM 18528 O  O     . HOH   T 9 .   ? 110.573 152.971 146.858 1.00 30.00  ?  1151 HOH   B O     1 
HETATM 18529 O  O     . HOH   T 9 .   ? 84.200  127.881 131.119 1.00 30.00  ?  1152 HOH   B O     1 
HETATM 18530 O  O     . HOH   T 9 .   ? 87.278  129.005 127.804 1.00 37.28  ?  1153 HOH   B O     1 
HETATM 18531 O  O     . HOH   T 9 .   ? 126.004 129.005 146.113 1.00 30.00  ?  1154 HOH   B O     1 
HETATM 18532 O  O     . HOH   T 9 .   ? 75.908  111.979 146.036 1.00 30.00  ?  1155 HOH   B O     1 
HETATM 18533 O  O     . HOH   T 9 .   ? 105.997 87.103  114.959 1.00 38.17  ?  1156 HOH   B O     1 
HETATM 18534 O  O     . HOH   T 9 .   ? 95.876  97.973  123.924 1.00 30.00  ?  1157 HOH   B O     1 
HETATM 18535 O  O     . HOH   T 9 .   ? 112.855 139.101 151.921 1.00 23.58  ?  1158 HOH   B O     1 
HETATM 18536 O  O     . HOH   T 9 .   ? 85.136  126.166 114.905 1.00 30.00  ?  1159 HOH   B O     1 
HETATM 18537 O  O     . HOH   T 9 .   ? 88.000  99.988  137.966 1.00 30.00  ?  1160 HOH   B O     1 
HETATM 18538 O  O     . HOH   T 9 .   ? 132.661 122.879 141.891 1.00 29.37  ?  1161 HOH   B O     1 
HETATM 18539 O  O     . HOH   T 9 .   ? 104.299 122.957 168.144 1.00 30.00  ?  1162 HOH   B O     1 
HETATM 18540 O  O     . HOH   T 9 .   ? 74.459  109.008 142.049 1.00 30.00  ?  1163 HOH   B O     1 
HETATM 18541 O  O     . HOH   T 9 .   ? 116.110 97.078  140.579 1.00 30.00  ?  1164 HOH   B O     1 
HETATM 18542 O  O     . HOH   T 9 .   ? 92.935  116.288 110.725 1.00 34.60  ?  1165 HOH   B O     1 
HETATM 18543 O  O     . HOH   T 9 .   ? 87.946  118.527 117.063 1.00 34.22  ?  1166 HOH   B O     1 
HETATM 18544 O  O     . HOH   T 9 .   ? 115.038 126.952 153.941 1.00 30.00  ?  1167 HOH   B O     1 
HETATM 18545 O  O     . HOH   T 9 .   ? 117.840 99.989  161.092 1.00 30.00  ?  1168 HOH   B O     1 
HETATM 18546 O  O     . HOH   T 9 .   ? 133.204 122.869 145.031 1.00 30.00  ?  1169 HOH   B O     1 
HETATM 18547 O  O     . HOH   T 9 .   ? 130.440 119.149 143.025 1.00 27.40  ?  1170 HOH   B O     1 
HETATM 18548 O  O     . HOH   T 9 .   ? 78.962  115.760 160.081 1.00 30.00  ?  1171 HOH   B O     1 
HETATM 18549 O  O     . HOH   T 9 .   ? 75.149  120.002 148.054 1.00 30.00  ?  1172 HOH   B O     1 
HETATM 18550 O  O     . HOH   T 9 .   ? 117.966 138.218 127.015 1.00 30.00  ?  1173 HOH   B O     1 
HETATM 18551 O  O     . HOH   T 9 .   ? 106.729 147.468 153.260 1.00 30.00  ?  1174 HOH   B O     1 
HETATM 18552 O  O     . HOH   T 9 .   ? 84.893  113.886 123.909 1.00 30.00  ?  1175 HOH   B O     1 
HETATM 18553 O  O     . HOH   T 9 .   ? 98.760  124.916 153.935 1.00 30.00  ?  1176 HOH   B O     1 
HETATM 18554 O  O     . HOH   T 9 .   ? 95.907  100.562 120.168 1.00 32.73  ?  1177 HOH   B O     1 
HETATM 18555 O  O     . HOH   T 9 .   ? 117.316 107.841 128.953 1.00 18.29  ?  1178 HOH   B O     1 
HETATM 18556 O  O     . HOH   T 9 .   ? 101.281 108.356 143.896 1.00 30.00  ?  1179 HOH   B O     1 
HETATM 18557 O  O     . HOH   T 9 .   ? 92.212  83.951  135.357 1.00 30.00  ?  1180 HOH   B O     1 
HETATM 18558 O  O     . HOH   T 9 .   ? 114.096 133.025 116.969 1.00 30.00  ?  1181 HOH   B O     1 
HETATM 18559 O  O     . HOH   T 9 .   ? 116.031 105.852 128.950 1.00 30.00  ?  1182 HOH   B O     1 
HETATM 18560 O  O     . HOH   T 9 .   ? 76.771  117.141 147.368 1.00 30.00  ?  1183 HOH   B O     1 
HETATM 18561 O  O     . HOH   T 9 .   ? 80.966  110.033 151.574 1.00 30.00  ?  1184 HOH   B O     1 
HETATM 18562 O  O     . HOH   T 9 .   ? 78.980  111.055 150.149 1.00 30.00  ?  1185 HOH   B O     1 
HETATM 18563 O  O     . HOH   T 9 .   ? 124.099 131.120 146.832 1.00 30.00  ?  1186 HOH   B O     1 
HETATM 18564 O  O     . HOH   T 9 .   ? 111.946 134.121 119.097 1.00 30.00  ?  1187 HOH   B O     1 
HETATM 18565 O  O     . HOH   T 9 .   ? 93.758  108.947 163.079 1.00 30.00  ?  1188 HOH   B O     1 
HETATM 18566 O  O     . HOH   T 9 .   ? 81.800  113.143 159.892 1.00 30.00  ?  1189 HOH   B O     1 
HETATM 18567 O  O     . HOH   T 9 .   ? 116.966 97.829  126.021 1.00 30.00  ?  1190 HOH   B O     1 
HETATM 18568 O  O     . HOH   T 9 .   ? 118.806 101.340 158.636 1.00 30.00  ?  1191 HOH   B O     1 
HETATM 18569 O  O     . HOH   T 9 .   ? 97.039  90.069  161.053 1.00 30.00  ?  1192 HOH   B O     1 
HETATM 18570 O  O     . HOH   T 9 .   ? 79.838  114.034 158.876 1.00 30.00  ?  1193 HOH   B O     1 
HETATM 18571 O  O     . HOH   T 9 .   ? 87.965  101.390 158.025 1.00 30.00  ?  1194 HOH   B O     1 
HETATM 18572 O  O     . HOH   T 9 .   ? 121.977 114.815 125.943 1.00 31.42  ?  1195 HOH   B O     1 
HETATM 18573 O  O     . HOH   T 9 .   ? 109.931 102.124 161.072 1.00 30.00  ?  1196 HOH   B O     1 
HETATM 18574 O  O     . HOH   U 9 .   ? 104.084 103.684 90.095  1.00 18.14  ?  501  HOH   C O     1 
HETATM 18575 O  O     . HOH   U 9 .   ? 108.398 105.291 129.041 1.00 30.00  ?  502  HOH   C O     1 
HETATM 18576 O  O     . HOH   U 9 .   ? 110.039 117.063 131.282 1.00 27.52  ?  503  HOH   C O     1 
HETATM 18577 O  O     . HOH   U 9 .   ? 119.968 99.166  108.565 1.00 30.00  ?  504  HOH   C O     1 
HETATM 18578 O  O     . HOH   U 9 .   ? 106.306 104.987 107.483 1.00 34.03  ?  505  HOH   C O     1 
HETATM 18579 O  O     . HOH   U 9 .   ? 91.219  137.748 121.996 1.00 30.00  ?  506  HOH   C O     1 
HETATM 18580 O  O     . HOH   U 9 .   ? 100.750 119.060 127.022 1.00 19.05  ?  507  HOH   C O     1 
HETATM 18581 O  O     . HOH   U 9 .   ? 90.049  109.194 98.045  1.00 18.15  ?  508  HOH   C O     1 
HETATM 18582 O  O     . HOH   U 9 .   ? 114.827 114.266 117.009 1.00 30.00  ?  509  HOH   C O     1 
HETATM 18583 O  O     . HOH   U 9 .   ? 95.065  111.984 111.911 1.00 29.25  ?  510  HOH   C O     1 
HETATM 18584 O  O     . HOH   U 9 .   ? 103.936 112.032 103.813 1.00 14.44  ?  511  HOH   C O     1 
HETATM 18585 O  O     . HOH   U 9 .   ? 101.314 122.001 84.944  1.00 32.11  ?  512  HOH   C O     1 
HETATM 18586 O  O     . HOH   U 9 .   ? 114.035 108.915 123.325 1.00 30.00  ?  513  HOH   C O     1 
HETATM 18587 O  O     . HOH   U 9 .   ? 87.131  140.391 139.016 1.00 30.00  ?  514  HOH   C O     1 
HETATM 18588 O  O     . HOH   U 9 .   ? 93.004  136.904 89.973  1.00 30.50  ?  515  HOH   C O     1 
HETATM 18589 O  O     . HOH   U 9 .   ? 105.491 117.045 119.970 1.00 30.00  ?  516  HOH   C O     1 
HETATM 18590 O  O     . HOH   U 9 .   ? 100.940 117.660 111.955 1.00 30.00  ?  517  HOH   C O     1 
HETATM 18591 O  O     . HOH   U 9 .   ? 115.427 95.881  95.024  1.00 30.00  ?  518  HOH   C O     1 
HETATM 18592 O  O     . HOH   U 9 .   ? 112.027 103.754 128.795 1.00 30.00  ?  519  HOH   C O     1 
HETATM 18593 O  O     . HOH   U 9 .   ? 97.076  125.863 65.068  1.00 30.00  ?  520  HOH   C O     1 
HETATM 18594 O  O     . HOH   U 9 .   ? 107.891 109.779 121.920 1.00 30.00  ?  521  HOH   C O     1 
HETATM 18595 O  O     . HOH   U 9 .   ? 97.970  111.007 113.308 1.00 21.80  ?  522  HOH   C O     1 
HETATM 18596 O  O     . HOH   U 9 .   ? 82.922  127.818 99.984  1.00 28.43  ?  523  HOH   C O     1 
HETATM 18597 O  O     . HOH   U 9 .   ? 104.170 95.971  91.026  1.00 30.00  ?  524  HOH   C O     1 
HETATM 18598 O  O     . HOH   U 9 .   ? 81.160  103.994 95.955  1.00 30.00  ?  525  HOH   C O     1 
HETATM 18599 O  O     . HOH   U 9 .   ? 126.086 107.133 114.118 1.00 30.00  ?  526  HOH   C O     1 
HETATM 18600 O  O     . HOH   U 9 .   ? 115.214 98.672  100.854 1.00 30.00  ?  527  HOH   C O     1 
HETATM 18601 O  O     . HOH   U 9 .   ? 125.112 102.130 110.799 1.00 30.00  ?  528  HOH   C O     1 
HETATM 18602 O  O     . HOH   U 9 .   ? 97.941  93.766  113.897 1.00 20.23  ?  529  HOH   C O     1 
HETATM 18603 O  O     . HOH   U 9 .   ? 95.862  118.078 98.943  1.00 25.73  ?  530  HOH   C O     1 
HETATM 18604 O  O     . HOH   U 9 .   ? 100.009 132.149 95.996  1.00 30.00  ?  531  HOH   C O     1 
HETATM 18605 O  O     . HOH   U 9 .   ? 115.850 88.799  110.081 1.00 29.45  ?  532  HOH   C O     1 
HETATM 18606 O  O     . HOH   U 9 .   ? 114.144 121.292 111.065 1.00 34.68  ?  533  HOH   C O     1 
HETATM 18607 O  O     . HOH   U 9 .   ? 83.200  103.092 89.987  1.00 30.00  ?  534  HOH   C O     1 
HETATM 18608 O  O     . HOH   U 9 .   ? 92.085  107.027 119.039 1.00 30.00  ?  535  HOH   C O     1 
HETATM 18609 O  O     . HOH   U 9 .   ? 102.153 121.890 115.967 1.00 21.29  ?  536  HOH   C O     1 
HETATM 18610 O  O     . HOH   U 9 .   ? 93.040  114.151 124.026 1.00 30.00  ?  537  HOH   C O     1 
HETATM 18611 O  O     . HOH   U 9 .   ? 85.933  105.000 81.928  1.00 30.00  ?  538  HOH   C O     1 
HETATM 18612 O  O     . HOH   U 9 .   ? 121.941 107.872 122.007 1.00 30.00  ?  539  HOH   C O     1 
HETATM 18613 O  O     . HOH   U 9 .   ? 107.104 97.245  94.414  1.00 30.00  ?  540  HOH   C O     1 
HETATM 18614 O  O     . HOH   U 9 .   ? 99.042  105.581 90.092  1.00 30.00  ?  541  HOH   C O     1 
HETATM 18615 O  O     . HOH   U 9 .   ? 98.759  106.038 119.165 1.00 30.00  ?  542  HOH   C O     1 
HETATM 18616 O  O     . HOH   U 9 .   ? 110.065 114.180 129.132 1.00 30.00  ?  543  HOH   C O     1 
HETATM 18617 O  O     . HOH   U 9 .   ? 95.125  92.115  113.034 1.00 34.87  ?  544  HOH   C O     1 
HETATM 18618 O  O     . HOH   U 9 .   ? 102.993 87.990  111.971 1.00 30.00  ?  545  HOH   C O     1 
HETATM 18619 O  O     . HOH   U 9 .   ? 103.945 119.913 117.764 1.00 26.18  ?  546  HOH   C O     1 
HETATM 18620 O  O     . HOH   U 9 .   ? 89.160  135.900 95.949  1.00 30.00  ?  547  HOH   C O     1 
HETATM 18621 O  O     . HOH   U 9 .   ? 104.023 124.052 82.216  1.00 33.43  ?  548  HOH   C O     1 
HETATM 18622 O  O     . HOH   U 9 .   ? 85.907  109.930 87.172  1.00 20.80  ?  549  HOH   C O     1 
HETATM 18623 O  O     . HOH   U 9 .   ? 84.187  132.652 102.211 1.00 30.00  ?  550  HOH   C O     1 
HETATM 18624 O  O     . HOH   U 9 .   ? 94.972  114.980 110.748 1.00 26.89  ?  551  HOH   C O     1 
HETATM 18625 O  O     . HOH   U 9 .   ? 90.897  125.709 109.971 1.00 28.27  ?  552  HOH   C O     1 
HETATM 18626 O  O     . HOH   U 9 .   ? 117.042 112.991 120.012 1.00 30.00  ?  553  HOH   C O     1 
HETATM 18627 O  O     . HOH   U 9 .   ? 84.607  125.353 100.104 1.00 30.00  ?  554  HOH   C O     1 
HETATM 18628 O  O     . HOH   U 9 .   ? 103.489 87.163  105.815 1.00 28.66  ?  555  HOH   C O     1 
HETATM 18629 O  O     . HOH   U 9 .   ? 97.889  127.073 119.934 1.00 13.88  ?  556  HOH   C O     1 
HETATM 18630 O  O     . HOH   U 9 .   ? 111.177 122.994 104.085 1.00 17.68  ?  557  HOH   C O     1 
HETATM 18631 O  O     . HOH   U 9 .   ? 93.574  116.150 121.227 1.00 30.00  ?  558  HOH   C O     1 
HETATM 18632 O  O     . HOH   U 9 .   ? 119.021 100.016 102.161 1.00 35.96  ?  559  HOH   C O     1 
HETATM 18633 O  O     . HOH   U 9 .   ? 115.001 97.147  122.012 1.00 30.00  ?  560  HOH   C O     1 
HETATM 18634 O  O     . HOH   U 9 .   ? 127.975 108.612 109.018 1.00 29.16  ?  561  HOH   C O     1 
HETATM 18635 O  O     . HOH   U 9 .   ? 98.808  114.222 127.849 1.00 30.00  ?  562  HOH   C O     1 
HETATM 18636 O  O     . HOH   U 9 .   ? 93.761  123.927 113.999 1.00 30.00  ?  563  HOH   C O     1 
HETATM 18637 O  O     . HOH   U 9 .   ? 104.024 112.010 132.036 1.00 29.72  ?  564  HOH   C O     1 
HETATM 18638 O  O     . HOH   U 9 .   ? 107.954 86.008  104.893 1.00 30.00  ?  565  HOH   C O     1 
HETATM 18639 O  O     . HOH   U 9 .   ? 87.932  124.022 87.748  1.00 30.00  ?  566  HOH   C O     1 
HETATM 18640 O  O     . HOH   U 9 .   ? 109.074 114.113 126.918 1.00 30.00  ?  567  HOH   C O     1 
HETATM 18641 O  O     . HOH   U 9 .   ? 103.020 122.840 83.815  1.00 30.00  ?  568  HOH   C O     1 
HETATM 18642 O  O     . HOH   U 9 .   ? 99.033  106.363 92.948  1.00 30.00  ?  569  HOH   C O     1 
HETATM 18643 O  O     . HOH   U 9 .   ? 102.943 124.095 107.856 1.00 30.00  ?  570  HOH   C O     1 
HETATM 18644 O  O     . HOH   U 9 .   ? 92.168  125.623 112.088 1.00 30.00  ?  571  HOH   C O     1 
HETATM 18645 O  O     . HOH   U 9 .   ? 117.162 115.704 107.959 1.00 29.24  ?  572  HOH   C O     1 
HETATM 18646 O  O     . HOH   U 9 .   ? 100.085 129.096 119.967 1.00 21.53  ?  573  HOH   C O     1 
HETATM 18647 O  O     . HOH   U 9 .   ? 86.072  114.559 101.017 1.00 30.00  ?  574  HOH   C O     1 
HETATM 18648 O  O     . HOH   U 9 .   ? 111.285 103.960 121.974 1.00 36.47  ?  575  HOH   C O     1 
HETATM 18649 O  O     . HOH   U 9 .   ? 101.166 98.010  122.934 1.00 30.00  ?  576  HOH   C O     1 
HETATM 18650 O  O     . HOH   U 9 .   ? 97.940  113.933 123.800 1.00 30.00  ?  577  HOH   C O     1 
HETATM 18651 O  O     . HOH   U 9 .   ? 119.076 88.911  112.084 1.00 30.00  ?  578  HOH   C O     1 
HETATM 18652 O  O     . HOH   U 9 .   ? 97.940  112.716 83.544  1.00 30.00  ?  579  HOH   C O     1 
HETATM 18653 O  O     . HOH   U 9 .   ? 118.156 111.214 126.076 1.00 30.00  ?  580  HOH   C O     1 
HETATM 18654 O  O     . HOH   U 9 .   ? 93.356  90.390  100.856 1.00 30.00  ?  581  HOH   C O     1 
HETATM 18655 O  O     . HOH   U 9 .   ? 109.982 119.901 122.030 1.00 26.73  ?  582  HOH   C O     1 
HETATM 18656 O  O     . HOH   U 9 .   ? 88.007  109.090 103.075 1.00 30.00  ?  583  HOH   C O     1 
HETATM 18657 O  O     . HOH   U 9 .   ? 113.757 107.026 127.032 1.00 30.00  ?  584  HOH   C O     1 
HETATM 18658 O  O     . HOH   U 9 .   ? 116.991 117.950 110.028 1.00 30.00  ?  585  HOH   C O     1 
HETATM 18659 O  O     . HOH   U 9 .   ? 99.303  113.767 122.000 1.00 30.00  ?  586  HOH   C O     1 
HETATM 18660 O  O     . HOH   U 9 .   ? 103.930 130.137 79.292  1.00 30.00  ?  587  HOH   C O     1 
HETATM 18661 O  O     . HOH   U 9 .   ? 83.791  109.871 89.948  1.00 30.00  ?  588  HOH   C O     1 
HETATM 18662 O  O     . HOH   U 9 .   ? 100.947 108.100 120.108 1.00 32.73  ?  589  HOH   C O     1 
HETATM 18663 O  O     . HOH   U 9 .   ? 95.946  129.518 83.276  1.00 30.00  ?  590  HOH   C O     1 
HETATM 18664 O  O     . HOH   U 9 .   ? 112.050 111.289 129.018 1.00 30.70  ?  591  HOH   C O     1 
HETATM 18665 O  O     . HOH   U 9 .   ? 129.939 104.988 109.187 1.00 30.00  ?  592  HOH   C O     1 
HETATM 18666 O  O     . HOH   U 9 .   ? 83.720  134.460 101.047 1.00 30.00  ?  593  HOH   C O     1 
HETATM 18667 O  O     . HOH   U 9 .   ? 105.953 117.807 124.115 1.00 32.36  ?  594  HOH   C O     1 
HETATM 18668 O  O     . HOH   U 9 .   ? 111.032 117.894 99.141  1.00 33.33  ?  595  HOH   C O     1 
HETATM 18669 O  O     . HOH   U 9 .   ? 129.984 107.181 107.935 1.00 30.00  ?  596  HOH   C O     1 
HETATM 18670 O  O     . HOH   U 9 .   ? 114.113 94.882  119.064 1.00 33.51  ?  597  HOH   C O     1 
HETATM 18671 O  O     . HOH   U 9 .   ? 87.963  123.217 85.381  1.00 30.00  ?  598  HOH   C O     1 
HETATM 18672 O  O     . HOH   U 9 .   ? 88.909  140.084 123.334 1.00 30.00  ?  599  HOH   C O     1 
HETATM 18673 O  O     . HOH   U 9 .   ? 115.049 103.993 129.973 1.00 30.00  ?  600  HOH   C O     1 
HETATM 18674 O  O     . HOH   U 9 .   ? 104.983 121.134 109.042 1.00 30.00  ?  601  HOH   C O     1 
HETATM 18675 O  O     . HOH   U 9 .   ? 116.944 103.852 126.958 1.00 30.00  ?  602  HOH   C O     1 
HETATM 18676 O  O     . HOH   U 9 .   ? 117.170 106.956 125.950 1.00 30.00  ?  603  HOH   C O     1 
HETATM 18677 O  O     . HOH   U 9 .   ? 109.024 93.625  126.112 1.00 30.00  ?  604  HOH   C O     1 
HETATM 18678 O  O     . HOH   U 9 .   ? 95.814  127.014 120.740 1.00 30.00  ?  605  HOH   C O     1 
HETATM 18679 O  O     . HOH   U 9 .   ? 81.673  134.284 98.844  1.00 30.00  ?  606  HOH   C O     1 
HETATM 18680 O  O     . HOH   U 9 .   ? 116.980 100.171 126.192 1.00 30.00  ?  607  HOH   C O     1 
HETATM 18681 O  O     . HOH   U 9 .   ? 127.019 101.145 119.245 1.00 30.00  ?  608  HOH   C O     1 
HETATM 18682 O  O     . HOH   V 9 .   ? 114.150 119.444 79.584  1.00 30.00  ?  501  HOH   D O     1 
HETATM 18683 O  O     . HOH   V 9 .   ? 110.774 128.570 84.482  1.00 30.00  ?  502  HOH   D O     1 
HETATM 18684 O  O     . HOH   V 9 .   ? 142.901 104.232 97.964  1.00 31.73  ?  503  HOH   D O     1 
HETATM 18685 O  O     . HOH   V 9 .   ? 107.894 140.715 101.866 1.00 30.00  ?  504  HOH   D O     1 
HETATM 18686 O  O     . HOH   V 9 .   ? 119.833 113.500 102.936 1.00 30.00  ?  505  HOH   D O     1 
HETATM 18687 O  O     . HOH   V 9 .   ? 121.577 111.147 96.581  1.00 30.00  ?  506  HOH   D O     1 
HETATM 18688 O  O     . HOH   V 9 .   ? 110.720 136.707 110.065 1.00 30.00  ?  507  HOH   D O     1 
HETATM 18689 O  O     . HOH   V 9 .   ? 130.985 150.973 91.083  1.00 30.00  ?  508  HOH   D O     1 
HETATM 18690 O  O     . HOH   V 9 .   ? 127.454 115.482 104.975 1.00 30.00  ?  509  HOH   D O     1 
HETATM 18691 O  O     . HOH   V 9 .   ? 97.880  132.104 109.957 1.00 28.96  ?  510  HOH   D O     1 
HETATM 18692 O  O     . HOH   V 9 .   ? 125.953 144.036 79.248  1.00 36.62  ?  511  HOH   D O     1 
HETATM 18693 O  O     . HOH   V 9 .   ? 120.021 119.023 107.081 1.00 30.00  ?  512  HOH   D O     1 
HETATM 18694 O  O     . HOH   V 9 .   ? 103.706 150.962 110.942 1.00 30.00  ?  513  HOH   D O     1 
HETATM 18695 O  O     . HOH   V 9 .   ? 124.808 126.839 87.055  1.00 30.00  ?  514  HOH   D O     1 
HETATM 18696 O  O     . HOH   V 9 .   ? 127.573 131.475 98.136  1.00 30.00  ?  515  HOH   D O     1 
HETATM 18697 O  O     . HOH   V 9 .   ? 120.887 127.616 110.014 1.00 30.00  ?  516  HOH   D O     1 
HETATM 18698 O  O     . HOH   V 9 .   ? 129.637 156.035 93.997  1.00 30.00  ?  517  HOH   D O     1 
HETATM 18699 O  O     . HOH   V 9 .   ? 103.955 156.050 88.243  1.00 30.00  ?  518  HOH   D O     1 
HETATM 18700 O  O     . HOH   V 9 .   ? 112.796 145.033 90.389  1.00 30.00  ?  519  HOH   D O     1 
HETATM 18701 O  O     . HOH   V 9 .   ? 125.129 159.997 93.297  1.00 30.00  ?  520  HOH   D O     1 
HETATM 18702 O  O     . HOH   V 9 .   ? 100.991 141.825 119.152 1.00 30.00  ?  521  HOH   D O     1 
HETATM 18703 O  O     . HOH   V 9 .   ? 108.849 144.059 116.983 1.00 23.83  ?  522  HOH   D O     1 
HETATM 18704 O  O     . HOH   V 9 .   ? 113.054 142.708 111.245 1.00 24.80  ?  523  HOH   D O     1 
HETATM 18705 O  O     . HOH   V 9 .   ? 116.123 133.756 97.972  1.00 30.00  ?  524  HOH   D O     1 
HETATM 18706 O  O     . HOH   V 9 .   ? 100.792 129.860 102.980 1.00 18.16  ?  525  HOH   D O     1 
HETATM 18707 O  O     . HOH   V 9 .   ? 87.256  152.866 105.740 1.00 30.00  ?  526  HOH   D O     1 
HETATM 18708 O  O     . HOH   V 9 .   ? 107.022 117.018 81.111  1.00 30.00  ?  527  HOH   D O     1 
HETATM 18709 O  O     . HOH   V 9 .   ? 119.957 116.231 89.763  1.00 30.00  ?  528  HOH   D O     1 
HETATM 18710 O  O     . HOH   V 9 .   ? 126.950 136.350 75.940  1.00 30.00  ?  529  HOH   D O     1 
HETATM 18711 O  O     . HOH   V 9 .   ? 119.039 114.921 91.088  1.00 25.80  ?  530  HOH   D O     1 
HETATM 18712 O  O     . HOH   V 9 .   ? 117.056 119.094 100.069 1.00 19.70  ?  531  HOH   D O     1 
HETATM 18713 O  O     . HOH   V 9 .   ? 105.052 136.143 116.202 1.00 30.00  ?  532  HOH   D O     1 
HETATM 18714 O  O     . HOH   V 9 .   ? 95.034  136.870 106.996 1.00 30.00  ?  533  HOH   D O     1 
HETATM 18715 O  O     . HOH   V 9 .   ? 119.953 110.839 92.150  1.00 30.00  ?  534  HOH   D O     1 
HETATM 18716 O  O     . HOH   V 9 .   ? 116.918 131.918 115.039 1.00 25.63  ?  535  HOH   D O     1 
HETATM 18717 O  O     . HOH   V 9 .   ? 100.907 134.087 95.089  1.00 27.35  ?  536  HOH   D O     1 
HETATM 18718 O  O     . HOH   V 9 .   ? 105.947 125.986 97.981  1.00 28.67  ?  537  HOH   D O     1 
HETATM 18719 O  O     . HOH   V 9 .   ? 158.055 99.248  105.713 1.00 30.00  ?  538  HOH   D O     1 
HETATM 18720 O  O     . HOH   V 9 .   ? 109.865 166.050 100.732 1.00 29.46  ?  539  HOH   D O     1 
HETATM 18721 O  O     . HOH   V 9 .   ? 121.193 136.066 106.267 1.00 30.00  ?  540  HOH   D O     1 
HETATM 18722 O  O     . HOH   V 9 .   ? 113.906 137.008 82.267  1.00 30.00  ?  541  HOH   D O     1 
HETATM 18723 O  O     . HOH   V 9 .   ? 126.107 114.897 88.061  1.00 30.00  ?  542  HOH   D O     1 
HETATM 18724 O  O     . HOH   V 9 .   ? 100.059 136.908 121.049 1.00 30.00  ?  543  HOH   D O     1 
HETATM 18725 O  O     . HOH   V 9 .   ? 95.487  161.295 99.933  1.00 30.00  ?  544  HOH   D O     1 
HETATM 18726 O  O     . HOH   V 9 .   ? 108.930 146.843 86.911  1.00 30.00  ?  545  HOH   D O     1 
HETATM 18727 O  O     . HOH   V 9 .   ? 106.127 131.962 116.162 1.00 23.63  ?  546  HOH   D O     1 
HETATM 18728 O  O     . HOH   V 9 .   ? 121.214 105.055 87.025  1.00 30.00  ?  547  HOH   D O     1 
HETATM 18729 O  O     . HOH   V 9 .   ? 104.088 138.115 117.928 1.00 30.00  ?  548  HOH   D O     1 
HETATM 18730 O  O     . HOH   V 9 .   ? 98.610  146.109 88.923  1.00 30.00  ?  549  HOH   D O     1 
HETATM 18731 O  O     . HOH   V 9 .   ? 138.090 114.971 102.875 1.00 30.00  ?  550  HOH   D O     1 
HETATM 18732 O  O     . HOH   V 9 .   ? 109.213 133.854 114.983 1.00 30.00  ?  551  HOH   D O     1 
HETATM 18733 O  O     . HOH   V 9 .   ? 123.281 143.156 101.009 1.00 30.00  ?  552  HOH   D O     1 
HETATM 18734 O  O     . HOH   V 9 .   ? 107.856 125.473 82.249  1.00 32.74  ?  553  HOH   D O     1 
HETATM 18735 O  O     . HOH   V 9 .   ? 117.059 137.829 109.092 1.00 30.00  ?  554  HOH   D O     1 
HETATM 18736 O  O     . HOH   V 9 .   ? 126.684 140.610 86.717  1.00 30.00  ?  555  HOH   D O     1 
HETATM 18737 O  O     . HOH   V 9 .   ? 107.867 141.226 115.963 1.00 34.87  ?  556  HOH   D O     1 
HETATM 18738 O  O     . HOH   V 9 .   ? 116.108 120.933 84.333  1.00 30.00  ?  557  HOH   D O     1 
HETATM 18739 O  O     . HOH   V 9 .   ? 123.012 116.610 97.189  1.00 30.30  ?  558  HOH   D O     1 
HETATM 18740 O  O     . HOH   V 9 .   ? 107.840 119.136 79.984  1.00 34.35  ?  559  HOH   D O     1 
HETATM 18741 O  O     . HOH   V 9 .   ? 106.353 131.956 108.083 1.00 30.00  ?  560  HOH   D O     1 
HETATM 18742 O  O     . HOH   V 9 .   ? 113.010 109.964 83.919  1.00 30.00  ?  561  HOH   D O     1 
HETATM 18743 O  O     . HOH   V 9 .   ? 104.243 133.997 119.114 1.00 30.00  ?  562  HOH   D O     1 
HETATM 18744 O  O     . HOH   V 9 .   ? 112.794 144.850 88.166  1.00 30.00  ?  563  HOH   D O     1 
HETATM 18745 O  O     . HOH   V 9 .   ? 121.152 109.952 94.405  1.00 30.00  ?  564  HOH   D O     1 
HETATM 18746 O  O     . HOH   V 9 .   ? 107.099 134.860 116.211 1.00 30.00  ?  565  HOH   D O     1 
HETATM 18747 O  O     . HOH   V 9 .   ? 120.115 137.917 107.095 1.00 30.00  ?  566  HOH   D O     1 
HETATM 18748 O  O     . HOH   V 9 .   ? 103.553 126.267 82.044  1.00 30.00  ?  567  HOH   D O     1 
HETATM 18749 O  O     . HOH   V 9 .   ? 103.952 136.073 120.721 1.00 30.00  ?  568  HOH   D O     1 
HETATM 18750 O  O     . HOH   V 9 .   ? 105.026 126.919 83.484  1.00 30.00  ?  569  HOH   D O     1 
HETATM 18751 O  O     . HOH   V 9 .   ? 105.925 139.044 117.098 1.00 30.00  ?  570  HOH   D O     1 
# 
