data_9OC4
# 
_entry.id   9OC4 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9OC4         pdb_00009oc4 10.2210/pdb9oc4/pdb 
WWPDB D_1000294626 ?            ?                   
EMDB  EMD-70308    ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-21 
_pdbx_audit_revision_history.part_number         ? 
# 
_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_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9OC4 
_pdbx_database_status.recvd_initial_deposition_date   2025-04-23 
_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           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'High-resolution cryo-EM structure of KdpFABC in the E1P-ADP state in lipid nanodisc' 
_pdbx_database_related.db_id          EMD-70308 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              stokes@nyu.edu 
_pdbx_contact_author.name_first         David 
_pdbx_contact_author.name_last          Stokes 
_pdbx_contact_author.name_mi            L 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5455-8163 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Hussein, A.K.'  1 0000-0001-6963-9118 
'Zhang, X.'      2 0000-0001-5488-0021 
'Pedersen, B.P.' 3 0000-0001-7860-7230 
'Stokes, D.L.'   4 0000-0001-5455-8163 
# 
_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            Biorxiv 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2692-8205 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Conduction pathway for potassium through the E. coli pump KdpFABC' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1101/2025.05.05.652293 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Hussein, A.'    1 ? 
primary 'Zhang, X.'      2 ? 
primary 'Pedersen, B.P.' 3 ? 
primary 'Stokes, D.L.'   4 ? 
# 
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 'Potassium-transporting ATPase potassium-binding subunit'                                      59218.613 1  ? ? 
? ? 
2 polymer     man 'Potassium-transporting ATPase ATP-binding subunit'                                            72347.844 1  
7.2.2.6 ? ? ? 
3 polymer     man 'Potassium-transporting ATPase KdpC subunit'                                                   22299.225 1  ? ? 
? ? 
4 polymer     man 'Potassium-transporting ATPase KdpF subunit'                                                   3071.714  1  ? ? 
? ? 
5 non-polymer syn 'POTASSIUM ION'                                                                                39.098    2  ? ? 
? ? 
6 non-polymer syn '(2R)-3-(((2-aminoethoxy)(hydroxy)phosphoryl)oxy)-2-(palmitoyloxy)propyl (E)-octadec-9-enoate' 717.996   2  ? ? 
? ? 
7 non-polymer syn "ADENOSINE-5'-DIPHOSPHATE"                                                                     427.201   1  ? ? 
? ? 
8 non-polymer nat 'MAGNESIUM ION'                                                                                24.305    2  ? ? 
? ? 
9 water       nat water                                                                                          18.015    90 ? ? 
? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 
;ATP phosphohydrolase [potassium-transporting] A chain,Potassium-binding and translocating subunit A,Potassium-translocating ATPase A chain
;
2 
;ATP phosphohydrolase [potassium-transporting] B chain,Potassium-binding and translocating subunit B,Potassium-translocating ATPase B chain
;
3 
;ATP phosphohydrolase [potassium-transporting] C chain,Potassium-binding and translocating subunit C,Potassium-translocating ATPase C chain
;
4 
;ATP phosphohydrolase [potassium-transporting] F chain,Potassium-binding and translocating subunit F,Potassium-translocating ATPase F chain
;
# 
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  
;MAAQGFLLIATFLLVLMVLARPLGSGLARLINDIPLPGTTGVERVLFRALGVSDREMNWKQYLCAILGLNMLGLAVLFFM
LLGQHYLPLNPQQLPGLSWDLALNTAVSFVTNTNWQSYSGETTLSYFSQMAGLTVQNFLSAASGIAVIFALIRAFTRQSM
STLGNAWVDLLRITLWVLVPVALLIALFFIQQGALQNFLPYQAVNTVEGAQQLLPMGPVASQEAIKMLGTNGGGFFNANS
SHPFENPTALTNFVQMLAIFLIPTALCFAFGEVMGDRRQGRMLLWAMSVIFVICVGVVMWAEVQGNPHLLALGTDSSINM
EGKESRFGVLVSSLFAVVTTAASCGAVIAMHDSFTALGGMVPMWLMQIGEVVFGGVGSGLYGMMLFVLLAVFIAGLMIGR
TPEYLGKKIDVREMKLTALAILVTPTLVLMGAALAMMTDAGRSAMLNPGPHGFSEVLYAVSSAANNNGSAFAGLSANSPF
WNCLLAFCMFVGRFGVIIPVMAIAGSLVSKKSQAASSGTLPTHGPLFVGLLIGTVLLVGALTFIPALALGPVAEYLS
;
;MAAQGFLLIATFLLVLMVLARPLGSGLARLINDIPLPGTTGVERVLFRALGVSDREMNWKQYLCAILGLNMLGLAVLFFM
LLGQHYLPLNPQQLPGLSWDLALNTAVSFVTNTNWQSYSGETTLSYFSQMAGLTVQNFLSAASGIAVIFALIRAFTRQSM
STLGNAWVDLLRITLWVLVPVALLIALFFIQQGALQNFLPYQAVNTVEGAQQLLPMGPVASQEAIKMLGTNGGGFFNANS
SHPFENPTALTNFVQMLAIFLIPTALCFAFGEVMGDRRQGRMLLWAMSVIFVICVGVVMWAEVQGNPHLLALGTDSSINM
EGKESRFGVLVSSLFAVVTTAASCGAVIAMHDSFTALGGMVPMWLMQIGEVVFGGVGSGLYGMMLFVLLAVFIAGLMIGR
TPEYLGKKIDVREMKLTALAILVTPTLVLMGAALAMMTDAGRSAMLNPGPHGFSEVLYAVSSAANNNGSAFAGLSANSPF
WNCLLAFCMFVGRFGVIIPVMAIAGSLVSKKSQAASSGTLPTHGPLFVGLLIGTVLLVGALTFIPALALGPVAEYLS
;
A ? 
2 'polypeptide(L)' no yes 
;MSRKQLALFEPTLVVQALKEAVKKLNPQAQWRNPVMFIVWIGSLLTTCISIAMASGAMPGNALFSAAISGWLWITVLFAN
FAEALAEGRSKAQANSLKGVKKTAFARKLREPKYGAAADKVPADQLRKGDIVLVEAGDIIPCDGEVIEGGASVDESAITG
ESAPVIRESGGDFASVTGGTRILSDWLVIECSVNPGETFLDRMIAMVEGAQRRKTPNEIALTILLIALTIVFLLATATLW
PFSAWGGNAVSVTVLVALLVCLIPTTIGGLLSAIGVAGMSRMLGANVIATSGRAVEAAGDVDVLLL(PHD)KTGTITLGN
RQASEFIPAQGVDEKTLADAAQLASLADETPEGRSIVILAKQRFNLRERDVQSLHATFVPFTAQSRMSGINIDNRMIRKG
SVDAIRRHVEANGGHFPTDVDQKVDQVARQGATPLVVVEGSRVLGVIALKDIVKGGIKERFAQLRKMGIKTVMITGDNRL
TAAAIAAEAGVDDFLAEATPEAKLALIRQYQAEGRLVAMTGDGTNDAPALAQADVAVAMNSGTQAAKEAGNMVDLDSNPT
KLIEVVHIGKQMLMTRGSLTTFSIANDVAKYFAIIPAAFAATYPQLNALNIMCLHSPDSAILSAVIFNALIIVFLIPLAL
KGVSYKPLTASAMLRRNLWIYGLGGLLVPFIGIKVIDLLLTVCGLV
;
;MSRKQLALFEPTLVVQALKEAVKKLNPQAQWRNPVMFIVWIGSLLTTCISIAMASGAMPGNALFSAAISGWLWITVLFAN
FAEALAEGRSKAQANSLKGVKKTAFARKLREPKYGAAADKVPADQLRKGDIVLVEAGDIIPCDGEVIEGGASVDESAITG
ESAPVIRESGGDFASVTGGTRILSDWLVIECSVNPGETFLDRMIAMVEGAQRRKTPNEIALTILLIALTIVFLLATATLW
PFSAWGGNAVSVTVLVALLVCLIPTTIGGLLSAIGVAGMSRMLGANVIATSGRAVEAAGDVDVLLLDKTGTITLGNRQAS
EFIPAQGVDEKTLADAAQLASLADETPEGRSIVILAKQRFNLRERDVQSLHATFVPFTAQSRMSGINIDNRMIRKGSVDA
IRRHVEANGGHFPTDVDQKVDQVARQGATPLVVVEGSRVLGVIALKDIVKGGIKERFAQLRKMGIKTVMITGDNRLTAAA
IAAEAGVDDFLAEATPEAKLALIRQYQAEGRLVAMTGDGTNDAPALAQADVAVAMNSGTQAAKEAGNMVDLDSNPTKLIE
VVHIGKQMLMTRGSLTTFSIANDVAKYFAIIPAAFAATYPQLNALNIMCLHSPDSAILSAVIFNALIIVFLIPLALKGVS
YKPLTASAMLRRNLWIYGLGGLLVPFIGIKVIDLLLTVCGLV
;
B ? 
3 'polypeptide(L)' no no  
;MSGLRPALSTFIFLLLITGGVYPLLTTVLGQWWFPWQANGSLIREGDTVRGSALIGQNFTGNGYFHGRPSATAEMPYNPQ
ASGGSNLAVSNPELDKLIAARVAALRAANPDASASVPVELVTASASGLDNNITPQAAAWQIPRVAKARNLSVEQLTQLIA
KYSQQPLVKYIGQPVVNIVELNLALDKLDEGTGLVPRGSSHHHHHHHH
;
;MSGLRPALSTFIFLLLITGGVYPLLTTVLGQWWFPWQANGSLIREGDTVRGSALIGQNFTGNGYFHGRPSATAEMPYNPQ
ASGGSNLAVSNPELDKLIAARVAALRAANPDASASVPVELVTASASGLDNNITPQAAAWQIPRVAKARNLSVEQLTQLIA
KYSQQPLVKYIGQPVVNIVELNLALDKLDEGTGLVPRGSSHHHHHHHH
;
C ? 
4 'polypeptide(L)' no no  MSAGVITGVLLVFLLLGYLVYALINAEAF MSAGVITGVLLVFLLLGYLVYALINAEAF D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
5 'POTASSIUM ION'                                                                                K   
6 '(2R)-3-(((2-aminoethoxy)(hydroxy)phosphoryl)oxy)-2-(palmitoyloxy)propyl (E)-octadec-9-enoate' 9Y0 
7 "ADENOSINE-5'-DIPHOSPHATE"                                                                     ADP 
8 'MAGNESIUM ION'                                                                                MG  
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   ALA n 
1 3   ALA n 
1 4   GLN n 
1 5   GLY n 
1 6   PHE n 
1 7   LEU n 
1 8   LEU n 
1 9   ILE n 
1 10  ALA n 
1 11  THR n 
1 12  PHE n 
1 13  LEU n 
1 14  LEU n 
1 15  VAL n 
1 16  LEU n 
1 17  MET n 
1 18  VAL n 
1 19  LEU n 
1 20  ALA n 
1 21  ARG n 
1 22  PRO n 
1 23  LEU n 
1 24  GLY n 
1 25  SER n 
1 26  GLY n 
1 27  LEU n 
1 28  ALA n 
1 29  ARG n 
1 30  LEU n 
1 31  ILE n 
1 32  ASN n 
1 33  ASP n 
1 34  ILE n 
1 35  PRO n 
1 36  LEU n 
1 37  PRO n 
1 38  GLY n 
1 39  THR n 
1 40  THR n 
1 41  GLY n 
1 42  VAL n 
1 43  GLU n 
1 44  ARG n 
1 45  VAL n 
1 46  LEU n 
1 47  PHE n 
1 48  ARG n 
1 49  ALA n 
1 50  LEU n 
1 51  GLY n 
1 52  VAL n 
1 53  SER n 
1 54  ASP n 
1 55  ARG n 
1 56  GLU n 
1 57  MET n 
1 58  ASN n 
1 59  TRP n 
1 60  LYS n 
1 61  GLN n 
1 62  TYR n 
1 63  LEU n 
1 64  CYS n 
1 65  ALA n 
1 66  ILE n 
1 67  LEU n 
1 68  GLY n 
1 69  LEU n 
1 70  ASN n 
1 71  MET n 
1 72  LEU n 
1 73  GLY n 
1 74  LEU n 
1 75  ALA n 
1 76  VAL n 
1 77  LEU n 
1 78  PHE n 
1 79  PHE n 
1 80  MET n 
1 81  LEU n 
1 82  LEU n 
1 83  GLY n 
1 84  GLN n 
1 85  HIS n 
1 86  TYR n 
1 87  LEU n 
1 88  PRO n 
1 89  LEU n 
1 90  ASN n 
1 91  PRO n 
1 92  GLN n 
1 93  GLN n 
1 94  LEU n 
1 95  PRO n 
1 96  GLY n 
1 97  LEU n 
1 98  SER n 
1 99  TRP n 
1 100 ASP n 
1 101 LEU n 
1 102 ALA n 
1 103 LEU n 
1 104 ASN n 
1 105 THR n 
1 106 ALA n 
1 107 VAL n 
1 108 SER n 
1 109 PHE n 
1 110 VAL n 
1 111 THR n 
1 112 ASN n 
1 113 THR n 
1 114 ASN n 
1 115 TRP n 
1 116 GLN n 
1 117 SER n 
1 118 TYR n 
1 119 SER n 
1 120 GLY n 
1 121 GLU n 
1 122 THR n 
1 123 THR n 
1 124 LEU n 
1 125 SER n 
1 126 TYR n 
1 127 PHE n 
1 128 SER n 
1 129 GLN n 
1 130 MET n 
1 131 ALA n 
1 132 GLY n 
1 133 LEU n 
1 134 THR n 
1 135 VAL n 
1 136 GLN n 
1 137 ASN n 
1 138 PHE n 
1 139 LEU n 
1 140 SER n 
1 141 ALA n 
1 142 ALA n 
1 143 SER n 
1 144 GLY n 
1 145 ILE n 
1 146 ALA n 
1 147 VAL n 
1 148 ILE n 
1 149 PHE n 
1 150 ALA n 
1 151 LEU n 
1 152 ILE n 
1 153 ARG n 
1 154 ALA n 
1 155 PHE n 
1 156 THR n 
1 157 ARG n 
1 158 GLN n 
1 159 SER n 
1 160 MET n 
1 161 SER n 
1 162 THR n 
1 163 LEU n 
1 164 GLY n 
1 165 ASN n 
1 166 ALA n 
1 167 TRP n 
1 168 VAL n 
1 169 ASP n 
1 170 LEU n 
1 171 LEU n 
1 172 ARG n 
1 173 ILE n 
1 174 THR n 
1 175 LEU n 
1 176 TRP n 
1 177 VAL n 
1 178 LEU n 
1 179 VAL n 
1 180 PRO n 
1 181 VAL n 
1 182 ALA n 
1 183 LEU n 
1 184 LEU n 
1 185 ILE n 
1 186 ALA n 
1 187 LEU n 
1 188 PHE n 
1 189 PHE n 
1 190 ILE n 
1 191 GLN n 
1 192 GLN n 
1 193 GLY n 
1 194 ALA n 
1 195 LEU n 
1 196 GLN n 
1 197 ASN n 
1 198 PHE n 
1 199 LEU n 
1 200 PRO n 
1 201 TYR n 
1 202 GLN n 
1 203 ALA n 
1 204 VAL n 
1 205 ASN n 
1 206 THR n 
1 207 VAL n 
1 208 GLU n 
1 209 GLY n 
1 210 ALA n 
1 211 GLN n 
1 212 GLN n 
1 213 LEU n 
1 214 LEU n 
1 215 PRO n 
1 216 MET n 
1 217 GLY n 
1 218 PRO n 
1 219 VAL n 
1 220 ALA n 
1 221 SER n 
1 222 GLN n 
1 223 GLU n 
1 224 ALA n 
1 225 ILE n 
1 226 LYS n 
1 227 MET n 
1 228 LEU n 
1 229 GLY n 
1 230 THR n 
1 231 ASN n 
1 232 GLY n 
1 233 GLY n 
1 234 GLY n 
1 235 PHE n 
1 236 PHE n 
1 237 ASN n 
1 238 ALA n 
1 239 ASN n 
1 240 SER n 
1 241 SER n 
1 242 HIS n 
1 243 PRO n 
1 244 PHE n 
1 245 GLU n 
1 246 ASN n 
1 247 PRO n 
1 248 THR n 
1 249 ALA n 
1 250 LEU n 
1 251 THR n 
1 252 ASN n 
1 253 PHE n 
1 254 VAL n 
1 255 GLN n 
1 256 MET n 
1 257 LEU n 
1 258 ALA n 
1 259 ILE n 
1 260 PHE n 
1 261 LEU n 
1 262 ILE n 
1 263 PRO n 
1 264 THR n 
1 265 ALA n 
1 266 LEU n 
1 267 CYS n 
1 268 PHE n 
1 269 ALA n 
1 270 PHE n 
1 271 GLY n 
1 272 GLU n 
1 273 VAL n 
1 274 MET n 
1 275 GLY n 
1 276 ASP n 
1 277 ARG n 
1 278 ARG n 
1 279 GLN n 
1 280 GLY n 
1 281 ARG n 
1 282 MET n 
1 283 LEU n 
1 284 LEU n 
1 285 TRP n 
1 286 ALA n 
1 287 MET n 
1 288 SER n 
1 289 VAL n 
1 290 ILE n 
1 291 PHE n 
1 292 VAL n 
1 293 ILE n 
1 294 CYS n 
1 295 VAL n 
1 296 GLY n 
1 297 VAL n 
1 298 VAL n 
1 299 MET n 
1 300 TRP n 
1 301 ALA n 
1 302 GLU n 
1 303 VAL n 
1 304 GLN n 
1 305 GLY n 
1 306 ASN n 
1 307 PRO n 
1 308 HIS n 
1 309 LEU n 
1 310 LEU n 
1 311 ALA n 
1 312 LEU n 
1 313 GLY n 
1 314 THR n 
1 315 ASP n 
1 316 SER n 
1 317 SER n 
1 318 ILE n 
1 319 ASN n 
1 320 MET n 
1 321 GLU n 
1 322 GLY n 
1 323 LYS n 
1 324 GLU n 
1 325 SER n 
1 326 ARG n 
1 327 PHE n 
1 328 GLY n 
1 329 VAL n 
1 330 LEU n 
1 331 VAL n 
1 332 SER n 
1 333 SER n 
1 334 LEU n 
1 335 PHE n 
1 336 ALA n 
1 337 VAL n 
1 338 VAL n 
1 339 THR n 
1 340 THR n 
1 341 ALA n 
1 342 ALA n 
1 343 SER n 
1 344 CYS n 
1 345 GLY n 
1 346 ALA n 
1 347 VAL n 
1 348 ILE n 
1 349 ALA n 
1 350 MET n 
1 351 HIS n 
1 352 ASP n 
1 353 SER n 
1 354 PHE n 
1 355 THR n 
1 356 ALA n 
1 357 LEU n 
1 358 GLY n 
1 359 GLY n 
1 360 MET n 
1 361 VAL n 
1 362 PRO n 
1 363 MET n 
1 364 TRP n 
1 365 LEU n 
1 366 MET n 
1 367 GLN n 
1 368 ILE n 
1 369 GLY n 
1 370 GLU n 
1 371 VAL n 
1 372 VAL n 
1 373 PHE n 
1 374 GLY n 
1 375 GLY n 
1 376 VAL n 
1 377 GLY n 
1 378 SER n 
1 379 GLY n 
1 380 LEU n 
1 381 TYR n 
1 382 GLY n 
1 383 MET n 
1 384 MET n 
1 385 LEU n 
1 386 PHE n 
1 387 VAL n 
1 388 LEU n 
1 389 LEU n 
1 390 ALA n 
1 391 VAL n 
1 392 PHE n 
1 393 ILE n 
1 394 ALA n 
1 395 GLY n 
1 396 LEU n 
1 397 MET n 
1 398 ILE n 
1 399 GLY n 
1 400 ARG n 
1 401 THR n 
1 402 PRO n 
1 403 GLU n 
1 404 TYR n 
1 405 LEU n 
1 406 GLY n 
1 407 LYS n 
1 408 LYS n 
1 409 ILE n 
1 410 ASP n 
1 411 VAL n 
1 412 ARG n 
1 413 GLU n 
1 414 MET n 
1 415 LYS n 
1 416 LEU n 
1 417 THR n 
1 418 ALA n 
1 419 LEU n 
1 420 ALA n 
1 421 ILE n 
1 422 LEU n 
1 423 VAL n 
1 424 THR n 
1 425 PRO n 
1 426 THR n 
1 427 LEU n 
1 428 VAL n 
1 429 LEU n 
1 430 MET n 
1 431 GLY n 
1 432 ALA n 
1 433 ALA n 
1 434 LEU n 
1 435 ALA n 
1 436 MET n 
1 437 MET n 
1 438 THR n 
1 439 ASP n 
1 440 ALA n 
1 441 GLY n 
1 442 ARG n 
1 443 SER n 
1 444 ALA n 
1 445 MET n 
1 446 LEU n 
1 447 ASN n 
1 448 PRO n 
1 449 GLY n 
1 450 PRO n 
1 451 HIS n 
1 452 GLY n 
1 453 PHE n 
1 454 SER n 
1 455 GLU n 
1 456 VAL n 
1 457 LEU n 
1 458 TYR n 
1 459 ALA n 
1 460 VAL n 
1 461 SER n 
1 462 SER n 
1 463 ALA n 
1 464 ALA n 
1 465 ASN n 
1 466 ASN n 
1 467 ASN n 
1 468 GLY n 
1 469 SER n 
1 470 ALA n 
1 471 PHE n 
1 472 ALA n 
1 473 GLY n 
1 474 LEU n 
1 475 SER n 
1 476 ALA n 
1 477 ASN n 
1 478 SER n 
1 479 PRO n 
1 480 PHE n 
1 481 TRP n 
1 482 ASN n 
1 483 CYS n 
1 484 LEU n 
1 485 LEU n 
1 486 ALA n 
1 487 PHE n 
1 488 CYS n 
1 489 MET n 
1 490 PHE n 
1 491 VAL n 
1 492 GLY n 
1 493 ARG n 
1 494 PHE n 
1 495 GLY n 
1 496 VAL n 
1 497 ILE n 
1 498 ILE n 
1 499 PRO n 
1 500 VAL n 
1 501 MET n 
1 502 ALA n 
1 503 ILE n 
1 504 ALA n 
1 505 GLY n 
1 506 SER n 
1 507 LEU n 
1 508 VAL n 
1 509 SER n 
1 510 LYS n 
1 511 LYS n 
1 512 SER n 
1 513 GLN n 
1 514 ALA n 
1 515 ALA n 
1 516 SER n 
1 517 SER n 
1 518 GLY n 
1 519 THR n 
1 520 LEU n 
1 521 PRO n 
1 522 THR n 
1 523 HIS n 
1 524 GLY n 
1 525 PRO n 
1 526 LEU n 
1 527 PHE n 
1 528 VAL n 
1 529 GLY n 
1 530 LEU n 
1 531 LEU n 
1 532 ILE n 
1 533 GLY n 
1 534 THR n 
1 535 VAL n 
1 536 LEU n 
1 537 LEU n 
1 538 VAL n 
1 539 GLY n 
1 540 ALA n 
1 541 LEU n 
1 542 THR n 
1 543 PHE n 
1 544 ILE n 
1 545 PRO n 
1 546 ALA n 
1 547 LEU n 
1 548 ALA n 
1 549 LEU n 
1 550 GLY n 
1 551 PRO n 
1 552 VAL n 
1 553 ALA n 
1 554 GLU n 
1 555 TYR n 
1 556 LEU n 
1 557 SER n 
2 1   MET n 
2 2   SER n 
2 3   ARG n 
2 4   LYS n 
2 5   GLN n 
2 6   LEU n 
2 7   ALA n 
2 8   LEU n 
2 9   PHE n 
2 10  GLU n 
2 11  PRO n 
2 12  THR n 
2 13  LEU n 
2 14  VAL n 
2 15  VAL n 
2 16  GLN n 
2 17  ALA n 
2 18  LEU n 
2 19  LYS n 
2 20  GLU n 
2 21  ALA n 
2 22  VAL n 
2 23  LYS n 
2 24  LYS n 
2 25  LEU n 
2 26  ASN n 
2 27  PRO n 
2 28  GLN n 
2 29  ALA n 
2 30  GLN n 
2 31  TRP n 
2 32  ARG n 
2 33  ASN n 
2 34  PRO n 
2 35  VAL n 
2 36  MET n 
2 37  PHE n 
2 38  ILE n 
2 39  VAL n 
2 40  TRP n 
2 41  ILE n 
2 42  GLY n 
2 43  SER n 
2 44  LEU n 
2 45  LEU n 
2 46  THR n 
2 47  THR n 
2 48  CYS n 
2 49  ILE n 
2 50  SER n 
2 51  ILE n 
2 52  ALA n 
2 53  MET n 
2 54  ALA n 
2 55  SER n 
2 56  GLY n 
2 57  ALA n 
2 58  MET n 
2 59  PRO n 
2 60  GLY n 
2 61  ASN n 
2 62  ALA n 
2 63  LEU n 
2 64  PHE n 
2 65  SER n 
2 66  ALA n 
2 67  ALA n 
2 68  ILE n 
2 69  SER n 
2 70  GLY n 
2 71  TRP n 
2 72  LEU n 
2 73  TRP n 
2 74  ILE n 
2 75  THR n 
2 76  VAL n 
2 77  LEU n 
2 78  PHE n 
2 79  ALA n 
2 80  ASN n 
2 81  PHE n 
2 82  ALA n 
2 83  GLU n 
2 84  ALA n 
2 85  LEU n 
2 86  ALA n 
2 87  GLU n 
2 88  GLY n 
2 89  ARG n 
2 90  SER n 
2 91  LYS n 
2 92  ALA n 
2 93  GLN n 
2 94  ALA n 
2 95  ASN n 
2 96  SER n 
2 97  LEU n 
2 98  LYS n 
2 99  GLY n 
2 100 VAL n 
2 101 LYS n 
2 102 LYS n 
2 103 THR n 
2 104 ALA n 
2 105 PHE n 
2 106 ALA n 
2 107 ARG n 
2 108 LYS n 
2 109 LEU n 
2 110 ARG n 
2 111 GLU n 
2 112 PRO n 
2 113 LYS n 
2 114 TYR n 
2 115 GLY n 
2 116 ALA n 
2 117 ALA n 
2 118 ALA n 
2 119 ASP n 
2 120 LYS n 
2 121 VAL n 
2 122 PRO n 
2 123 ALA n 
2 124 ASP n 
2 125 GLN n 
2 126 LEU n 
2 127 ARG n 
2 128 LYS n 
2 129 GLY n 
2 130 ASP n 
2 131 ILE n 
2 132 VAL n 
2 133 LEU n 
2 134 VAL n 
2 135 GLU n 
2 136 ALA n 
2 137 GLY n 
2 138 ASP n 
2 139 ILE n 
2 140 ILE n 
2 141 PRO n 
2 142 CYS n 
2 143 ASP n 
2 144 GLY n 
2 145 GLU n 
2 146 VAL n 
2 147 ILE n 
2 148 GLU n 
2 149 GLY n 
2 150 GLY n 
2 151 ALA n 
2 152 SER n 
2 153 VAL n 
2 154 ASP n 
2 155 GLU n 
2 156 SER n 
2 157 ALA n 
2 158 ILE n 
2 159 THR n 
2 160 GLY n 
2 161 GLU n 
2 162 SER n 
2 163 ALA n 
2 164 PRO n 
2 165 VAL n 
2 166 ILE n 
2 167 ARG n 
2 168 GLU n 
2 169 SER n 
2 170 GLY n 
2 171 GLY n 
2 172 ASP n 
2 173 PHE n 
2 174 ALA n 
2 175 SER n 
2 176 VAL n 
2 177 THR n 
2 178 GLY n 
2 179 GLY n 
2 180 THR n 
2 181 ARG n 
2 182 ILE n 
2 183 LEU n 
2 184 SER n 
2 185 ASP n 
2 186 TRP n 
2 187 LEU n 
2 188 VAL n 
2 189 ILE n 
2 190 GLU n 
2 191 CYS n 
2 192 SER n 
2 193 VAL n 
2 194 ASN n 
2 195 PRO n 
2 196 GLY n 
2 197 GLU n 
2 198 THR n 
2 199 PHE n 
2 200 LEU n 
2 201 ASP n 
2 202 ARG n 
2 203 MET n 
2 204 ILE n 
2 205 ALA n 
2 206 MET n 
2 207 VAL n 
2 208 GLU n 
2 209 GLY n 
2 210 ALA n 
2 211 GLN n 
2 212 ARG n 
2 213 ARG n 
2 214 LYS n 
2 215 THR n 
2 216 PRO n 
2 217 ASN n 
2 218 GLU n 
2 219 ILE n 
2 220 ALA n 
2 221 LEU n 
2 222 THR n 
2 223 ILE n 
2 224 LEU n 
2 225 LEU n 
2 226 ILE n 
2 227 ALA n 
2 228 LEU n 
2 229 THR n 
2 230 ILE n 
2 231 VAL n 
2 232 PHE n 
2 233 LEU n 
2 234 LEU n 
2 235 ALA n 
2 236 THR n 
2 237 ALA n 
2 238 THR n 
2 239 LEU n 
2 240 TRP n 
2 241 PRO n 
2 242 PHE n 
2 243 SER n 
2 244 ALA n 
2 245 TRP n 
2 246 GLY n 
2 247 GLY n 
2 248 ASN n 
2 249 ALA n 
2 250 VAL n 
2 251 SER n 
2 252 VAL n 
2 253 THR n 
2 254 VAL n 
2 255 LEU n 
2 256 VAL n 
2 257 ALA n 
2 258 LEU n 
2 259 LEU n 
2 260 VAL n 
2 261 CYS n 
2 262 LEU n 
2 263 ILE n 
2 264 PRO n 
2 265 THR n 
2 266 THR n 
2 267 ILE n 
2 268 GLY n 
2 269 GLY n 
2 270 LEU n 
2 271 LEU n 
2 272 SER n 
2 273 ALA n 
2 274 ILE n 
2 275 GLY n 
2 276 VAL n 
2 277 ALA n 
2 278 GLY n 
2 279 MET n 
2 280 SER n 
2 281 ARG n 
2 282 MET n 
2 283 LEU n 
2 284 GLY n 
2 285 ALA n 
2 286 ASN n 
2 287 VAL n 
2 288 ILE n 
2 289 ALA n 
2 290 THR n 
2 291 SER n 
2 292 GLY n 
2 293 ARG n 
2 294 ALA n 
2 295 VAL n 
2 296 GLU n 
2 297 ALA n 
2 298 ALA n 
2 299 GLY n 
2 300 ASP n 
2 301 VAL n 
2 302 ASP n 
2 303 VAL n 
2 304 LEU n 
2 305 LEU n 
2 306 LEU n 
2 307 PHD n 
2 308 LYS n 
2 309 THR n 
2 310 GLY n 
2 311 THR n 
2 312 ILE n 
2 313 THR n 
2 314 LEU n 
2 315 GLY n 
2 316 ASN n 
2 317 ARG n 
2 318 GLN n 
2 319 ALA n 
2 320 SER n 
2 321 GLU n 
2 322 PHE n 
2 323 ILE n 
2 324 PRO n 
2 325 ALA n 
2 326 GLN n 
2 327 GLY n 
2 328 VAL n 
2 329 ASP n 
2 330 GLU n 
2 331 LYS n 
2 332 THR n 
2 333 LEU n 
2 334 ALA n 
2 335 ASP n 
2 336 ALA n 
2 337 ALA n 
2 338 GLN n 
2 339 LEU n 
2 340 ALA n 
2 341 SER n 
2 342 LEU n 
2 343 ALA n 
2 344 ASP n 
2 345 GLU n 
2 346 THR n 
2 347 PRO n 
2 348 GLU n 
2 349 GLY n 
2 350 ARG n 
2 351 SER n 
2 352 ILE n 
2 353 VAL n 
2 354 ILE n 
2 355 LEU n 
2 356 ALA n 
2 357 LYS n 
2 358 GLN n 
2 359 ARG n 
2 360 PHE n 
2 361 ASN n 
2 362 LEU n 
2 363 ARG n 
2 364 GLU n 
2 365 ARG n 
2 366 ASP n 
2 367 VAL n 
2 368 GLN n 
2 369 SER n 
2 370 LEU n 
2 371 HIS n 
2 372 ALA n 
2 373 THR n 
2 374 PHE n 
2 375 VAL n 
2 376 PRO n 
2 377 PHE n 
2 378 THR n 
2 379 ALA n 
2 380 GLN n 
2 381 SER n 
2 382 ARG n 
2 383 MET n 
2 384 SER n 
2 385 GLY n 
2 386 ILE n 
2 387 ASN n 
2 388 ILE n 
2 389 ASP n 
2 390 ASN n 
2 391 ARG n 
2 392 MET n 
2 393 ILE n 
2 394 ARG n 
2 395 LYS n 
2 396 GLY n 
2 397 SER n 
2 398 VAL n 
2 399 ASP n 
2 400 ALA n 
2 401 ILE n 
2 402 ARG n 
2 403 ARG n 
2 404 HIS n 
2 405 VAL n 
2 406 GLU n 
2 407 ALA n 
2 408 ASN n 
2 409 GLY n 
2 410 GLY n 
2 411 HIS n 
2 412 PHE n 
2 413 PRO n 
2 414 THR n 
2 415 ASP n 
2 416 VAL n 
2 417 ASP n 
2 418 GLN n 
2 419 LYS n 
2 420 VAL n 
2 421 ASP n 
2 422 GLN n 
2 423 VAL n 
2 424 ALA n 
2 425 ARG n 
2 426 GLN n 
2 427 GLY n 
2 428 ALA n 
2 429 THR n 
2 430 PRO n 
2 431 LEU n 
2 432 VAL n 
2 433 VAL n 
2 434 VAL n 
2 435 GLU n 
2 436 GLY n 
2 437 SER n 
2 438 ARG n 
2 439 VAL n 
2 440 LEU n 
2 441 GLY n 
2 442 VAL n 
2 443 ILE n 
2 444 ALA n 
2 445 LEU n 
2 446 LYS n 
2 447 ASP n 
2 448 ILE n 
2 449 VAL n 
2 450 LYS n 
2 451 GLY n 
2 452 GLY n 
2 453 ILE n 
2 454 LYS n 
2 455 GLU n 
2 456 ARG n 
2 457 PHE n 
2 458 ALA n 
2 459 GLN n 
2 460 LEU n 
2 461 ARG n 
2 462 LYS n 
2 463 MET n 
2 464 GLY n 
2 465 ILE n 
2 466 LYS n 
2 467 THR n 
2 468 VAL n 
2 469 MET n 
2 470 ILE n 
2 471 THR n 
2 472 GLY n 
2 473 ASP n 
2 474 ASN n 
2 475 ARG n 
2 476 LEU n 
2 477 THR n 
2 478 ALA n 
2 479 ALA n 
2 480 ALA n 
2 481 ILE n 
2 482 ALA n 
2 483 ALA n 
2 484 GLU n 
2 485 ALA n 
2 486 GLY n 
2 487 VAL n 
2 488 ASP n 
2 489 ASP n 
2 490 PHE n 
2 491 LEU n 
2 492 ALA n 
2 493 GLU n 
2 494 ALA n 
2 495 THR n 
2 496 PRO n 
2 497 GLU n 
2 498 ALA n 
2 499 LYS n 
2 500 LEU n 
2 501 ALA n 
2 502 LEU n 
2 503 ILE n 
2 504 ARG n 
2 505 GLN n 
2 506 TYR n 
2 507 GLN n 
2 508 ALA n 
2 509 GLU n 
2 510 GLY n 
2 511 ARG n 
2 512 LEU n 
2 513 VAL n 
2 514 ALA n 
2 515 MET n 
2 516 THR n 
2 517 GLY n 
2 518 ASP n 
2 519 GLY n 
2 520 THR n 
2 521 ASN n 
2 522 ASP n 
2 523 ALA n 
2 524 PRO n 
2 525 ALA n 
2 526 LEU n 
2 527 ALA n 
2 528 GLN n 
2 529 ALA n 
2 530 ASP n 
2 531 VAL n 
2 532 ALA n 
2 533 VAL n 
2 534 ALA n 
2 535 MET n 
2 536 ASN n 
2 537 SER n 
2 538 GLY n 
2 539 THR n 
2 540 GLN n 
2 541 ALA n 
2 542 ALA n 
2 543 LYS n 
2 544 GLU n 
2 545 ALA n 
2 546 GLY n 
2 547 ASN n 
2 548 MET n 
2 549 VAL n 
2 550 ASP n 
2 551 LEU n 
2 552 ASP n 
2 553 SER n 
2 554 ASN n 
2 555 PRO n 
2 556 THR n 
2 557 LYS n 
2 558 LEU n 
2 559 ILE n 
2 560 GLU n 
2 561 VAL n 
2 562 VAL n 
2 563 HIS n 
2 564 ILE n 
2 565 GLY n 
2 566 LYS n 
2 567 GLN n 
2 568 MET n 
2 569 LEU n 
2 570 MET n 
2 571 THR n 
2 572 ARG n 
2 573 GLY n 
2 574 SER n 
2 575 LEU n 
2 576 THR n 
2 577 THR n 
2 578 PHE n 
2 579 SER n 
2 580 ILE n 
2 581 ALA n 
2 582 ASN n 
2 583 ASP n 
2 584 VAL n 
2 585 ALA n 
2 586 LYS n 
2 587 TYR n 
2 588 PHE n 
2 589 ALA n 
2 590 ILE n 
2 591 ILE n 
2 592 PRO n 
2 593 ALA n 
2 594 ALA n 
2 595 PHE n 
2 596 ALA n 
2 597 ALA n 
2 598 THR n 
2 599 TYR n 
2 600 PRO n 
2 601 GLN n 
2 602 LEU n 
2 603 ASN n 
2 604 ALA n 
2 605 LEU n 
2 606 ASN n 
2 607 ILE n 
2 608 MET n 
2 609 CYS n 
2 610 LEU n 
2 611 HIS n 
2 612 SER n 
2 613 PRO n 
2 614 ASP n 
2 615 SER n 
2 616 ALA n 
2 617 ILE n 
2 618 LEU n 
2 619 SER n 
2 620 ALA n 
2 621 VAL n 
2 622 ILE n 
2 623 PHE n 
2 624 ASN n 
2 625 ALA n 
2 626 LEU n 
2 627 ILE n 
2 628 ILE n 
2 629 VAL n 
2 630 PHE n 
2 631 LEU n 
2 632 ILE n 
2 633 PRO n 
2 634 LEU n 
2 635 ALA n 
2 636 LEU n 
2 637 LYS n 
2 638 GLY n 
2 639 VAL n 
2 640 SER n 
2 641 TYR n 
2 642 LYS n 
2 643 PRO n 
2 644 LEU n 
2 645 THR n 
2 646 ALA n 
2 647 SER n 
2 648 ALA n 
2 649 MET n 
2 650 LEU n 
2 651 ARG n 
2 652 ARG n 
2 653 ASN n 
2 654 LEU n 
2 655 TRP n 
2 656 ILE n 
2 657 TYR n 
2 658 GLY n 
2 659 LEU n 
2 660 GLY n 
2 661 GLY n 
2 662 LEU n 
2 663 LEU n 
2 664 VAL n 
2 665 PRO n 
2 666 PHE n 
2 667 ILE n 
2 668 GLY n 
2 669 ILE n 
2 670 LYS n 
2 671 VAL n 
2 672 ILE n 
2 673 ASP n 
2 674 LEU n 
2 675 LEU n 
2 676 LEU n 
2 677 THR n 
2 678 VAL n 
2 679 CYS n 
2 680 GLY n 
2 681 LEU n 
2 682 VAL n 
3 1   MET n 
3 2   SER n 
3 3   GLY n 
3 4   LEU n 
3 5   ARG n 
3 6   PRO n 
3 7   ALA n 
3 8   LEU n 
3 9   SER n 
3 10  THR n 
3 11  PHE n 
3 12  ILE n 
3 13  PHE n 
3 14  LEU n 
3 15  LEU n 
3 16  LEU n 
3 17  ILE n 
3 18  THR n 
3 19  GLY n 
3 20  GLY n 
3 21  VAL n 
3 22  TYR n 
3 23  PRO n 
3 24  LEU n 
3 25  LEU n 
3 26  THR n 
3 27  THR n 
3 28  VAL n 
3 29  LEU n 
3 30  GLY n 
3 31  GLN n 
3 32  TRP n 
3 33  TRP n 
3 34  PHE n 
3 35  PRO n 
3 36  TRP n 
3 37  GLN n 
3 38  ALA n 
3 39  ASN n 
3 40  GLY n 
3 41  SER n 
3 42  LEU n 
3 43  ILE n 
3 44  ARG n 
3 45  GLU n 
3 46  GLY n 
3 47  ASP n 
3 48  THR n 
3 49  VAL n 
3 50  ARG n 
3 51  GLY n 
3 52  SER n 
3 53  ALA n 
3 54  LEU n 
3 55  ILE n 
3 56  GLY n 
3 57  GLN n 
3 58  ASN n 
3 59  PHE n 
3 60  THR n 
3 61  GLY n 
3 62  ASN n 
3 63  GLY n 
3 64  TYR n 
3 65  PHE n 
3 66  HIS n 
3 67  GLY n 
3 68  ARG n 
3 69  PRO n 
3 70  SER n 
3 71  ALA n 
3 72  THR n 
3 73  ALA n 
3 74  GLU n 
3 75  MET n 
3 76  PRO n 
3 77  TYR n 
3 78  ASN n 
3 79  PRO n 
3 80  GLN n 
3 81  ALA n 
3 82  SER n 
3 83  GLY n 
3 84  GLY n 
3 85  SER n 
3 86  ASN n 
3 87  LEU n 
3 88  ALA n 
3 89  VAL n 
3 90  SER n 
3 91  ASN n 
3 92  PRO n 
3 93  GLU n 
3 94  LEU n 
3 95  ASP n 
3 96  LYS n 
3 97  LEU n 
3 98  ILE n 
3 99  ALA n 
3 100 ALA n 
3 101 ARG n 
3 102 VAL n 
3 103 ALA n 
3 104 ALA n 
3 105 LEU n 
3 106 ARG n 
3 107 ALA n 
3 108 ALA n 
3 109 ASN n 
3 110 PRO n 
3 111 ASP n 
3 112 ALA n 
3 113 SER n 
3 114 ALA n 
3 115 SER n 
3 116 VAL n 
3 117 PRO n 
3 118 VAL n 
3 119 GLU n 
3 120 LEU n 
3 121 VAL n 
3 122 THR n 
3 123 ALA n 
3 124 SER n 
3 125 ALA n 
3 126 SER n 
3 127 GLY n 
3 128 LEU n 
3 129 ASP n 
3 130 ASN n 
3 131 ASN n 
3 132 ILE n 
3 133 THR n 
3 134 PRO n 
3 135 GLN n 
3 136 ALA n 
3 137 ALA n 
3 138 ALA n 
3 139 TRP n 
3 140 GLN n 
3 141 ILE n 
3 142 PRO n 
3 143 ARG n 
3 144 VAL n 
3 145 ALA n 
3 146 LYS n 
3 147 ALA n 
3 148 ARG n 
3 149 ASN n 
3 150 LEU n 
3 151 SER n 
3 152 VAL n 
3 153 GLU n 
3 154 GLN n 
3 155 LEU n 
3 156 THR n 
3 157 GLN n 
3 158 LEU n 
3 159 ILE n 
3 160 ALA n 
3 161 LYS n 
3 162 TYR n 
3 163 SER n 
3 164 GLN n 
3 165 GLN n 
3 166 PRO n 
3 167 LEU n 
3 168 VAL n 
3 169 LYS n 
3 170 TYR n 
3 171 ILE n 
3 172 GLY n 
3 173 GLN n 
3 174 PRO n 
3 175 VAL n 
3 176 VAL n 
3 177 ASN n 
3 178 ILE n 
3 179 VAL n 
3 180 GLU n 
3 181 LEU n 
3 182 ASN n 
3 183 LEU n 
3 184 ALA n 
3 185 LEU n 
3 186 ASP n 
3 187 LYS n 
3 188 LEU n 
3 189 ASP n 
3 190 GLU n 
3 191 GLY n 
3 192 THR n 
3 193 GLY n 
3 194 LEU n 
3 195 VAL n 
3 196 PRO n 
3 197 ARG n 
3 198 GLY n 
3 199 SER n 
3 200 SER n 
3 201 HIS n 
3 202 HIS n 
3 203 HIS n 
3 204 HIS n 
3 205 HIS n 
3 206 HIS n 
3 207 HIS n 
3 208 HIS n 
4 1   MET n 
4 2   SER n 
4 3   ALA n 
4 4   GLY n 
4 5   VAL n 
4 6   ILE n 
4 7   THR n 
4 8   GLY n 
4 9   VAL n 
4 10  LEU n 
4 11  LEU n 
4 12  VAL n 
4 13  PHE n 
4 14  LEU n 
4 15  LEU n 
4 16  LEU n 
4 17  GLY n 
4 18  TYR n 
4 19  LEU n 
4 20  VAL n 
4 21  TYR n 
4 22  ALA n 
4 23  LEU n 
4 24  ILE n 
4 25  ASN n 
4 26  ALA n 
4 27  GLU n 
4 28  ALA n 
4 29  PHE 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' 1 557 ? ? 'kdpA, b0698, JW0686' ? ? ? ? ? ? 'Escherichia coli K-12' 83333 ? ? ? ? ? ? ? ? 
'Escherichia coli K-12' 83333 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 682 ? ? 'kdpB, b0697, JW0685' ? ? ? ? ? ? 'Escherichia coli K-12' 83333 ? ? ? ? ? ? ? ? 
'Escherichia coli K-12' 83333 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 208 ? ? 'kdpC, b0696, JW0684' ? ? ? ? ? ? 'Escherichia coli K-12' 83333 ? ? ? ? ? ? ? ? 
'Escherichia coli K-12' 83333 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
4 1 sample 'Biological sequence' 1 29  ? ? 'kdpF, b4513, JW0687' ? ? ? ? ? ? 'Escherichia coli K-12' 83333 ? ? ? ? ? ? ? ? 
'Escherichia coli K-12' 83333 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
9Y0 non-polymer         . '(2R)-3-(((2-aminoethoxy)(hydroxy)phosphoryl)oxy)-2-(palmitoyloxy)propyl (E)-octadec-9-enoate' ? 
'C39 H76 N O8 P'    717.996 
ADP non-polymer         n "ADENOSINE-5'-DIPHOSPHATE"                                                                     ? 
'C10 H15 N5 O10 P2' 427.201 
ALA 'L-peptide linking' y ALANINE                                                                                        ? 
'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                                                                                       ? 
'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                                     ? 
'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                                ? 
'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                                       ? 
'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE                                                                                      ? 
'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                                ? 
'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                                                                                        ? 
'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                                      ? 
'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                                                                                          ? 'H2 O' 
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                                     ? 
'C6 H13 N O2'       131.173 
K   non-polymer         . 'POTASSIUM ION'                                                                                ? 'K 1' 
39.098  
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  
PHD 'L-peptide linking' n 'ASPARTYL PHOSPHATE'                                                                           ? 
'C4 H8 N O7 P'      213.083 
PHE 'L-peptide linking' y PHENYLALANINE                                                                                  ? 
'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                                                                                        ? 
'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                                                                                         ? 
'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                                                                                      ? 
'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                                     ? 
'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                                                                                       ? 
'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                                                                                         ? 
'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_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   1   MET MET A . n 
A 1 2   ALA 2   2   2   ALA ALA A . n 
A 1 3   ALA 3   3   3   ALA ALA A . n 
A 1 4   GLN 4   4   4   GLN GLN A . n 
A 1 5   GLY 5   5   5   GLY GLY A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   LEU 7   7   7   LEU LEU A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   ILE 9   9   9   ILE ILE A . n 
A 1 10  ALA 10  10  10  ALA ALA A . n 
A 1 11  THR 11  11  11  THR THR A . n 
A 1 12  PHE 12  12  12  PHE PHE A . n 
A 1 13  LEU 13  13  13  LEU LEU A . n 
A 1 14  LEU 14  14  14  LEU LEU A . n 
A 1 15  VAL 15  15  15  VAL VAL A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  LEU 19  19  19  LEU LEU A . n 
A 1 20  ALA 20  20  20  ALA ALA A . n 
A 1 21  ARG 21  21  21  ARG ARG A . n 
A 1 22  PRO 22  22  22  PRO PRO A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  GLY 24  24  24  GLY GLY A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  ARG 29  29  29  ARG ARG A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  ILE 31  31  31  ILE ILE A . n 
A 1 32  ASN 32  32  32  ASN ASN A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  ILE 34  34  34  ILE ILE A . n 
A 1 35  PRO 35  35  35  PRO PRO A . n 
A 1 36  LEU 36  36  36  LEU LEU A . n 
A 1 37  PRO 37  37  37  PRO PRO A . n 
A 1 38  GLY 38  38  38  GLY GLY A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  THR 40  40  40  THR THR A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  GLU 43  43  43  GLU GLU A . n 
A 1 44  ARG 44  44  44  ARG ARG A . n 
A 1 45  VAL 45  45  45  VAL VAL A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  PHE 47  47  47  PHE PHE A . n 
A 1 48  ARG 48  48  48  ARG ARG A . n 
A 1 49  ALA 49  49  49  ALA ALA A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  VAL 52  52  52  VAL VAL A . n 
A 1 53  SER 53  53  53  SER SER A . n 
A 1 54  ASP 54  54  54  ASP ASP A . n 
A 1 55  ARG 55  55  55  ARG ARG A . n 
A 1 56  GLU 56  56  56  GLU GLU A . n 
A 1 57  MET 57  57  57  MET MET A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  TRP 59  59  59  TRP TRP A . n 
A 1 60  LYS 60  60  60  LYS LYS A . n 
A 1 61  GLN 61  61  61  GLN GLN A . n 
A 1 62  TYR 62  62  62  TYR TYR A . n 
A 1 63  LEU 63  63  63  LEU LEU A . n 
A 1 64  CYS 64  64  64  CYS CYS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  ILE 66  66  66  ILE ILE A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  GLY 68  68  68  GLY GLY A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  ASN 70  70  70  ASN ASN A . n 
A 1 71  MET 71  71  71  MET MET A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  LEU 74  74  74  LEU LEU A . n 
A 1 75  ALA 75  75  75  ALA ALA A . n 
A 1 76  VAL 76  76  76  VAL VAL A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  PHE 78  78  78  PHE PHE A . n 
A 1 79  PHE 79  79  79  PHE PHE A . n 
A 1 80  MET 80  80  80  MET MET A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  GLY 83  83  83  GLY GLY A . n 
A 1 84  GLN 84  84  84  GLN GLN A . n 
A 1 85  HIS 85  85  85  HIS HIS A . n 
A 1 86  TYR 86  86  86  TYR TYR A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  PRO 88  88  88  PRO PRO A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  ASN 90  90  90  ASN ASN A . n 
A 1 91  PRO 91  91  91  PRO PRO A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  GLN 93  93  93  GLN GLN A . n 
A 1 94  LEU 94  94  94  LEU LEU A . n 
A 1 95  PRO 95  95  95  PRO PRO A . n 
A 1 96  GLY 96  96  96  GLY GLY A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  SER 98  98  98  SER SER A . n 
A 1 99  TRP 99  99  99  TRP TRP A . n 
A 1 100 ASP 100 100 100 ASP ASP A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 ALA 102 102 102 ALA ALA A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 ASN 104 104 104 ASN ASN A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 ALA 106 106 106 ALA ALA A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 PHE 109 109 109 PHE PHE A . n 
A 1 110 VAL 110 110 110 VAL VAL A . n 
A 1 111 THR 111 111 111 THR THR A . n 
A 1 112 ASN 112 112 112 ASN ASN A . n 
A 1 113 THR 113 113 113 THR THR A . n 
A 1 114 ASN 114 114 114 ASN ASN A . n 
A 1 115 TRP 115 115 115 TRP TRP A . n 
A 1 116 GLN 116 116 116 GLN GLN A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 SER 119 119 119 SER SER A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 THR 122 122 122 THR THR A . n 
A 1 123 THR 123 123 123 THR THR A . n 
A 1 124 LEU 124 124 124 LEU LEU A . n 
A 1 125 SER 125 125 125 SER SER A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 PHE 127 127 127 PHE PHE A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 GLN 129 129 129 GLN GLN A . n 
A 1 130 MET 130 130 130 MET MET A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 GLY 132 132 132 GLY GLY A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 THR 134 134 134 THR THR A . n 
A 1 135 VAL 135 135 135 VAL VAL A . n 
A 1 136 GLN 136 136 136 GLN GLN A . n 
A 1 137 ASN 137 137 137 ASN ASN A . n 
A 1 138 PHE 138 138 138 PHE PHE A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 SER 140 140 140 SER SER A . n 
A 1 141 ALA 141 141 141 ALA ALA A . n 
A 1 142 ALA 142 142 142 ALA ALA A . n 
A 1 143 SER 143 143 143 SER SER A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 ILE 145 145 145 ILE ILE A . n 
A 1 146 ALA 146 146 146 ALA ALA A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ILE 148 148 148 ILE ILE A . n 
A 1 149 PHE 149 149 149 PHE PHE A . n 
A 1 150 ALA 150 150 150 ALA ALA A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 ARG 153 153 153 ARG ARG A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 PHE 155 155 155 PHE PHE A . n 
A 1 156 THR 156 156 156 THR THR A . n 
A 1 157 ARG 157 157 157 ARG ARG A . n 
A 1 158 GLN 158 158 158 GLN GLN A . n 
A 1 159 SER 159 159 159 SER SER A . n 
A 1 160 MET 160 160 160 MET MET A . n 
A 1 161 SER 161 161 161 SER SER A . n 
A 1 162 THR 162 162 162 THR THR A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 GLY 164 164 164 GLY GLY A . n 
A 1 165 ASN 165 165 165 ASN ASN A . n 
A 1 166 ALA 166 166 166 ALA ALA A . n 
A 1 167 TRP 167 167 167 TRP TRP A . n 
A 1 168 VAL 168 168 168 VAL VAL A . n 
A 1 169 ASP 169 169 169 ASP ASP A . n 
A 1 170 LEU 170 170 170 LEU LEU A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 ARG 172 172 172 ARG ARG A . n 
A 1 173 ILE 173 173 173 ILE ILE A . n 
A 1 174 THR 174 174 174 THR THR A . n 
A 1 175 LEU 175 175 175 LEU LEU A . n 
A 1 176 TRP 176 176 176 TRP TRP A . n 
A 1 177 VAL 177 177 177 VAL VAL A . n 
A 1 178 LEU 178 178 178 LEU LEU A . n 
A 1 179 VAL 179 179 179 VAL VAL A . n 
A 1 180 PRO 180 180 180 PRO PRO A . n 
A 1 181 VAL 181 181 181 VAL VAL A . n 
A 1 182 ALA 182 182 182 ALA ALA A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 ILE 185 185 185 ILE ILE A . n 
A 1 186 ALA 186 186 186 ALA ALA A . n 
A 1 187 LEU 187 187 187 LEU LEU A . n 
A 1 188 PHE 188 188 188 PHE PHE A . n 
A 1 189 PHE 189 189 189 PHE PHE A . n 
A 1 190 ILE 190 190 190 ILE ILE A . n 
A 1 191 GLN 191 191 191 GLN GLN A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 GLY 193 193 193 GLY GLY A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 LEU 195 195 195 LEU LEU A . n 
A 1 196 GLN 196 196 196 GLN GLN A . n 
A 1 197 ASN 197 197 197 ASN ASN A . n 
A 1 198 PHE 198 198 198 PHE PHE A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 TYR 201 201 201 TYR TYR A . n 
A 1 202 GLN 202 202 202 GLN GLN A . n 
A 1 203 ALA 203 203 203 ALA ALA A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 ASN 205 205 205 ASN ASN A . n 
A 1 206 THR 206 206 206 THR THR A . n 
A 1 207 VAL 207 207 207 VAL VAL A . n 
A 1 208 GLU 208 208 208 GLU GLU A . n 
A 1 209 GLY 209 209 209 GLY GLY A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 GLN 211 211 211 GLN GLN A . n 
A 1 212 GLN 212 212 212 GLN GLN A . n 
A 1 213 LEU 213 213 213 LEU LEU A . n 
A 1 214 LEU 214 214 214 LEU LEU A . n 
A 1 215 PRO 215 215 215 PRO PRO A . n 
A 1 216 MET 216 216 216 MET MET A . n 
A 1 217 GLY 217 217 217 GLY GLY A . n 
A 1 218 PRO 218 218 218 PRO PRO A . n 
A 1 219 VAL 219 219 219 VAL VAL A . n 
A 1 220 ALA 220 220 220 ALA ALA A . n 
A 1 221 SER 221 221 221 SER SER A . n 
A 1 222 GLN 222 222 222 GLN GLN A . n 
A 1 223 GLU 223 223 223 GLU GLU A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 ILE 225 225 225 ILE ILE A . n 
A 1 226 LYS 226 226 226 LYS LYS A . n 
A 1 227 MET 227 227 227 MET MET A . n 
A 1 228 LEU 228 228 228 LEU LEU A . n 
A 1 229 GLY 229 229 229 GLY GLY A . n 
A 1 230 THR 230 230 230 THR THR A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 GLY 232 232 232 GLY GLY A . n 
A 1 233 GLY 233 233 233 GLY GLY A . n 
A 1 234 GLY 234 234 234 GLY GLY A . n 
A 1 235 PHE 235 235 235 PHE PHE A . n 
A 1 236 PHE 236 236 236 PHE PHE A . n 
A 1 237 ASN 237 237 237 ASN ASN A . n 
A 1 238 ALA 238 238 238 ALA ALA A . n 
A 1 239 ASN 239 239 239 ASN ASN A . n 
A 1 240 SER 240 240 240 SER SER A . n 
A 1 241 SER 241 241 241 SER SER A . n 
A 1 242 HIS 242 242 242 HIS HIS A . n 
A 1 243 PRO 243 243 243 PRO PRO A . n 
A 1 244 PHE 244 244 244 PHE PHE A . n 
A 1 245 GLU 245 245 245 GLU GLU A . n 
A 1 246 ASN 246 246 246 ASN ASN A . n 
A 1 247 PRO 247 247 247 PRO PRO A . n 
A 1 248 THR 248 248 248 THR THR A . n 
A 1 249 ALA 249 249 249 ALA ALA A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 THR 251 251 251 THR THR A . n 
A 1 252 ASN 252 252 252 ASN ASN A . n 
A 1 253 PHE 253 253 253 PHE PHE A . n 
A 1 254 VAL 254 254 254 VAL VAL A . n 
A 1 255 GLN 255 255 255 GLN GLN A . n 
A 1 256 MET 256 256 256 MET MET A . n 
A 1 257 LEU 257 257 257 LEU LEU A . n 
A 1 258 ALA 258 258 258 ALA ALA A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 PHE 260 260 260 PHE PHE A . n 
A 1 261 LEU 261 261 261 LEU LEU A . n 
A 1 262 ILE 262 262 262 ILE ILE A . n 
A 1 263 PRO 263 263 263 PRO PRO A . n 
A 1 264 THR 264 264 264 THR THR A . n 
A 1 265 ALA 265 265 265 ALA ALA A . n 
A 1 266 LEU 266 266 266 LEU LEU A . n 
A 1 267 CYS 267 267 267 CYS CYS A . n 
A 1 268 PHE 268 268 268 PHE PHE A . n 
A 1 269 ALA 269 269 269 ALA ALA A . n 
A 1 270 PHE 270 270 270 PHE PHE 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 VAL 273 273 273 VAL VAL A . n 
A 1 274 MET 274 274 274 MET MET A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 ASP 276 276 276 ASP ASP A . n 
A 1 277 ARG 277 277 277 ARG ARG A . n 
A 1 278 ARG 278 278 278 ARG ARG A . n 
A 1 279 GLN 279 279 279 GLN GLN A . n 
A 1 280 GLY 280 280 280 GLY GLY A . n 
A 1 281 ARG 281 281 281 ARG ARG A . n 
A 1 282 MET 282 282 282 MET MET A . n 
A 1 283 LEU 283 283 283 LEU LEU A . n 
A 1 284 LEU 284 284 284 LEU LEU A . n 
A 1 285 TRP 285 285 285 TRP TRP A . n 
A 1 286 ALA 286 286 286 ALA ALA A . n 
A 1 287 MET 287 287 287 MET MET A . n 
A 1 288 SER 288 288 288 SER SER A . n 
A 1 289 VAL 289 289 289 VAL VAL A . n 
A 1 290 ILE 290 290 290 ILE ILE A . n 
A 1 291 PHE 291 291 291 PHE PHE A . n 
A 1 292 VAL 292 292 292 VAL VAL A . n 
A 1 293 ILE 293 293 293 ILE ILE A . n 
A 1 294 CYS 294 294 294 CYS CYS A . n 
A 1 295 VAL 295 295 295 VAL VAL 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 VAL 298 298 298 VAL VAL A . n 
A 1 299 MET 299 299 299 MET MET A . n 
A 1 300 TRP 300 300 300 TRP TRP A . n 
A 1 301 ALA 301 301 301 ALA ALA A . n 
A 1 302 GLU 302 302 302 GLU GLU A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 GLN 304 304 304 GLN GLN A . n 
A 1 305 GLY 305 305 305 GLY GLY A . n 
A 1 306 ASN 306 306 306 ASN ASN A . n 
A 1 307 PRO 307 307 307 PRO PRO A . n 
A 1 308 HIS 308 308 308 HIS HIS A . n 
A 1 309 LEU 309 309 309 LEU LEU A . n 
A 1 310 LEU 310 310 310 LEU LEU A . n 
A 1 311 ALA 311 311 311 ALA ALA A . n 
A 1 312 LEU 312 312 312 LEU LEU A . n 
A 1 313 GLY 313 313 313 GLY GLY A . n 
A 1 314 THR 314 314 314 THR THR A . n 
A 1 315 ASP 315 315 315 ASP ASP A . n 
A 1 316 SER 316 316 316 SER SER A . n 
A 1 317 SER 317 317 317 SER SER A . n 
A 1 318 ILE 318 318 318 ILE ILE A . n 
A 1 319 ASN 319 319 319 ASN ASN A . n 
A 1 320 MET 320 320 320 MET MET A . n 
A 1 321 GLU 321 321 321 GLU GLU A . n 
A 1 322 GLY 322 322 322 GLY GLY A . n 
A 1 323 LYS 323 323 323 LYS LYS A . n 
A 1 324 GLU 324 324 324 GLU GLU A . n 
A 1 325 SER 325 325 325 SER SER A . n 
A 1 326 ARG 326 326 326 ARG ARG A . n 
A 1 327 PHE 327 327 327 PHE PHE A . n 
A 1 328 GLY 328 328 328 GLY GLY A . n 
A 1 329 VAL 329 329 329 VAL VAL A . n 
A 1 330 LEU 330 330 330 LEU LEU A . n 
A 1 331 VAL 331 331 331 VAL VAL A . n 
A 1 332 SER 332 332 332 SER SER A . n 
A 1 333 SER 333 333 333 SER SER A . n 
A 1 334 LEU 334 334 334 LEU LEU A . n 
A 1 335 PHE 335 335 335 PHE PHE A . n 
A 1 336 ALA 336 336 336 ALA ALA A . n 
A 1 337 VAL 337 337 337 VAL VAL A . n 
A 1 338 VAL 338 338 338 VAL VAL A . n 
A 1 339 THR 339 339 339 THR THR A . n 
A 1 340 THR 340 340 340 THR THR A . n 
A 1 341 ALA 341 341 341 ALA ALA A . n 
A 1 342 ALA 342 342 342 ALA ALA A . n 
A 1 343 SER 343 343 343 SER SER A . n 
A 1 344 CYS 344 344 344 CYS CYS A . n 
A 1 345 GLY 345 345 345 GLY GLY A . n 
A 1 346 ALA 346 346 346 ALA ALA A . n 
A 1 347 VAL 347 347 347 VAL VAL A . n 
A 1 348 ILE 348 348 348 ILE ILE A . n 
A 1 349 ALA 349 349 349 ALA ALA A . n 
A 1 350 MET 350 350 350 MET MET A . n 
A 1 351 HIS 351 351 351 HIS HIS A . n 
A 1 352 ASP 352 352 352 ASP ASP A . n 
A 1 353 SER 353 353 353 SER SER A . n 
A 1 354 PHE 354 354 354 PHE PHE A . n 
A 1 355 THR 355 355 355 THR THR A . n 
A 1 356 ALA 356 356 356 ALA ALA A . n 
A 1 357 LEU 357 357 357 LEU LEU A . n 
A 1 358 GLY 358 358 358 GLY GLY A . n 
A 1 359 GLY 359 359 359 GLY GLY A . n 
A 1 360 MET 360 360 360 MET MET 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 MET 363 363 363 MET MET A . n 
A 1 364 TRP 364 364 364 TRP TRP A . n 
A 1 365 LEU 365 365 365 LEU LEU A . n 
A 1 366 MET 366 366 366 MET MET A . n 
A 1 367 GLN 367 367 367 GLN GLN A . n 
A 1 368 ILE 368 368 368 ILE ILE A . n 
A 1 369 GLY 369 369 369 GLY GLY A . n 
A 1 370 GLU 370 370 370 GLU GLU A . n 
A 1 371 VAL 371 371 371 VAL VAL A . n 
A 1 372 VAL 372 372 372 VAL VAL A . n 
A 1 373 PHE 373 373 373 PHE PHE A . n 
A 1 374 GLY 374 374 374 GLY GLY A . n 
A 1 375 GLY 375 375 375 GLY GLY A . n 
A 1 376 VAL 376 376 376 VAL VAL A . n 
A 1 377 GLY 377 377 377 GLY GLY A . n 
A 1 378 SER 378 378 378 SER SER A . n 
A 1 379 GLY 379 379 379 GLY GLY A . n 
A 1 380 LEU 380 380 380 LEU LEU A . n 
A 1 381 TYR 381 381 381 TYR TYR A . n 
A 1 382 GLY 382 382 382 GLY GLY A . n 
A 1 383 MET 383 383 383 MET MET A . n 
A 1 384 MET 384 384 384 MET MET A . n 
A 1 385 LEU 385 385 385 LEU LEU A . n 
A 1 386 PHE 386 386 386 PHE PHE A . n 
A 1 387 VAL 387 387 387 VAL VAL A . n 
A 1 388 LEU 388 388 388 LEU LEU A . n 
A 1 389 LEU 389 389 389 LEU LEU A . n 
A 1 390 ALA 390 390 390 ALA ALA A . n 
A 1 391 VAL 391 391 391 VAL VAL A . n 
A 1 392 PHE 392 392 392 PHE PHE A . n 
A 1 393 ILE 393 393 393 ILE ILE A . n 
A 1 394 ALA 394 394 394 ALA ALA A . n 
A 1 395 GLY 395 395 395 GLY GLY A . n 
A 1 396 LEU 396 396 396 LEU LEU A . n 
A 1 397 MET 397 397 397 MET MET A . n 
A 1 398 ILE 398 398 398 ILE ILE A . n 
A 1 399 GLY 399 399 399 GLY GLY A . n 
A 1 400 ARG 400 400 400 ARG ARG A . n 
A 1 401 THR 401 401 401 THR THR A . n 
A 1 402 PRO 402 402 402 PRO PRO A . n 
A 1 403 GLU 403 403 403 GLU GLU A . n 
A 1 404 TYR 404 404 404 TYR TYR A . n 
A 1 405 LEU 405 405 405 LEU LEU A . n 
A 1 406 GLY 406 406 406 GLY GLY A . n 
A 1 407 LYS 407 407 407 LYS LYS A . n 
A 1 408 LYS 408 408 408 LYS LYS A . n 
A 1 409 ILE 409 409 409 ILE ILE A . n 
A 1 410 ASP 410 410 410 ASP ASP A . n 
A 1 411 VAL 411 411 411 VAL VAL A . n 
A 1 412 ARG 412 412 412 ARG ARG A . n 
A 1 413 GLU 413 413 413 GLU GLU A . n 
A 1 414 MET 414 414 414 MET MET A . n 
A 1 415 LYS 415 415 415 LYS LYS A . n 
A 1 416 LEU 416 416 416 LEU LEU A . n 
A 1 417 THR 417 417 417 THR THR A . n 
A 1 418 ALA 418 418 418 ALA ALA A . n 
A 1 419 LEU 419 419 419 LEU LEU A . n 
A 1 420 ALA 420 420 420 ALA ALA A . n 
A 1 421 ILE 421 421 421 ILE ILE A . n 
A 1 422 LEU 422 422 422 LEU LEU A . n 
A 1 423 VAL 423 423 423 VAL VAL A . n 
A 1 424 THR 424 424 424 THR THR A . n 
A 1 425 PRO 425 425 425 PRO PRO A . n 
A 1 426 THR 426 426 426 THR THR A . n 
A 1 427 LEU 427 427 427 LEU LEU A . n 
A 1 428 VAL 428 428 428 VAL VAL A . n 
A 1 429 LEU 429 429 429 LEU LEU A . n 
A 1 430 MET 430 430 430 MET MET A . n 
A 1 431 GLY 431 431 431 GLY GLY A . n 
A 1 432 ALA 432 432 432 ALA ALA A . n 
A 1 433 ALA 433 433 433 ALA ALA A . n 
A 1 434 LEU 434 434 434 LEU LEU A . n 
A 1 435 ALA 435 435 435 ALA ALA A . n 
A 1 436 MET 436 436 436 MET MET A . n 
A 1 437 MET 437 437 437 MET MET A . n 
A 1 438 THR 438 438 438 THR THR A . n 
A 1 439 ASP 439 439 439 ASP ASP A . n 
A 1 440 ALA 440 440 440 ALA ALA A . n 
A 1 441 GLY 441 441 441 GLY GLY A . n 
A 1 442 ARG 442 442 442 ARG ARG A . n 
A 1 443 SER 443 443 443 SER SER A . n 
A 1 444 ALA 444 444 444 ALA ALA A . n 
A 1 445 MET 445 445 445 MET MET A . n 
A 1 446 LEU 446 446 446 LEU LEU A . n 
A 1 447 ASN 447 447 447 ASN ASN A . n 
A 1 448 PRO 448 448 448 PRO PRO A . n 
A 1 449 GLY 449 449 449 GLY GLY A . n 
A 1 450 PRO 450 450 450 PRO PRO A . n 
A 1 451 HIS 451 451 451 HIS HIS A . n 
A 1 452 GLY 452 452 452 GLY GLY A . n 
A 1 453 PHE 453 453 453 PHE PHE A . n 
A 1 454 SER 454 454 454 SER SER A . n 
A 1 455 GLU 455 455 455 GLU GLU A . n 
A 1 456 VAL 456 456 456 VAL VAL A . n 
A 1 457 LEU 457 457 457 LEU LEU A . n 
A 1 458 TYR 458 458 458 TYR TYR A . n 
A 1 459 ALA 459 459 459 ALA ALA A . n 
A 1 460 VAL 460 460 460 VAL VAL A . n 
A 1 461 SER 461 461 461 SER SER A . n 
A 1 462 SER 462 462 462 SER SER A . n 
A 1 463 ALA 463 463 463 ALA ALA A . n 
A 1 464 ALA 464 464 464 ALA ALA A . n 
A 1 465 ASN 465 465 465 ASN ASN A . n 
A 1 466 ASN 466 466 466 ASN ASN A . n 
A 1 467 ASN 467 467 467 ASN ASN A . n 
A 1 468 GLY 468 468 468 GLY GLY A . n 
A 1 469 SER 469 469 469 SER SER A . n 
A 1 470 ALA 470 470 470 ALA ALA A . n 
A 1 471 PHE 471 471 471 PHE PHE A . n 
A 1 472 ALA 472 472 472 ALA ALA A . n 
A 1 473 GLY 473 473 473 GLY GLY A . n 
A 1 474 LEU 474 474 474 LEU LEU A . n 
A 1 475 SER 475 475 475 SER SER A . n 
A 1 476 ALA 476 476 476 ALA ALA A . n 
A 1 477 ASN 477 477 477 ASN ASN A . n 
A 1 478 SER 478 478 478 SER SER A . n 
A 1 479 PRO 479 479 479 PRO PRO A . n 
A 1 480 PHE 480 480 480 PHE PHE A . n 
A 1 481 TRP 481 481 481 TRP TRP A . n 
A 1 482 ASN 482 482 482 ASN ASN A . n 
A 1 483 CYS 483 483 483 CYS CYS A . n 
A 1 484 LEU 484 484 484 LEU LEU A . n 
A 1 485 LEU 485 485 485 LEU LEU A . n 
A 1 486 ALA 486 486 486 ALA ALA A . n 
A 1 487 PHE 487 487 487 PHE PHE A . n 
A 1 488 CYS 488 488 488 CYS CYS A . n 
A 1 489 MET 489 489 489 MET MET A . n 
A 1 490 PHE 490 490 490 PHE PHE A . n 
A 1 491 VAL 491 491 491 VAL VAL A . n 
A 1 492 GLY 492 492 492 GLY GLY A . n 
A 1 493 ARG 493 493 493 ARG ARG A . n 
A 1 494 PHE 494 494 494 PHE PHE A . n 
A 1 495 GLY 495 495 495 GLY GLY A . n 
A 1 496 VAL 496 496 496 VAL VAL A . n 
A 1 497 ILE 497 497 497 ILE ILE A . n 
A 1 498 ILE 498 498 498 ILE ILE A . n 
A 1 499 PRO 499 499 499 PRO PRO A . n 
A 1 500 VAL 500 500 500 VAL VAL A . n 
A 1 501 MET 501 501 501 MET MET A . n 
A 1 502 ALA 502 502 502 ALA ALA A . n 
A 1 503 ILE 503 503 503 ILE ILE A . n 
A 1 504 ALA 504 504 504 ALA ALA A . n 
A 1 505 GLY 505 505 505 GLY GLY A . n 
A 1 506 SER 506 506 506 SER SER A . n 
A 1 507 LEU 507 507 507 LEU LEU A . n 
A 1 508 VAL 508 508 508 VAL VAL A . n 
A 1 509 SER 509 509 509 SER SER A . n 
A 1 510 LYS 510 510 510 LYS LYS A . n 
A 1 511 LYS 511 511 511 LYS LYS A . n 
A 1 512 SER 512 512 512 SER SER A . n 
A 1 513 GLN 513 513 513 GLN GLN A . n 
A 1 514 ALA 514 514 514 ALA ALA A . n 
A 1 515 ALA 515 515 515 ALA ALA A . n 
A 1 516 SER 516 516 516 SER SER A . n 
A 1 517 SER 517 517 517 SER SER A . n 
A 1 518 GLY 518 518 518 GLY GLY A . n 
A 1 519 THR 519 519 519 THR THR A . n 
A 1 520 LEU 520 520 520 LEU LEU A . n 
A 1 521 PRO 521 521 521 PRO PRO A . n 
A 1 522 THR 522 522 522 THR THR A . n 
A 1 523 HIS 523 523 523 HIS HIS A . n 
A 1 524 GLY 524 524 524 GLY GLY A . n 
A 1 525 PRO 525 525 525 PRO PRO A . n 
A 1 526 LEU 526 526 526 LEU LEU A . n 
A 1 527 PHE 527 527 527 PHE PHE A . n 
A 1 528 VAL 528 528 528 VAL VAL A . n 
A 1 529 GLY 529 529 529 GLY GLY A . n 
A 1 530 LEU 530 530 530 LEU LEU A . n 
A 1 531 LEU 531 531 531 LEU LEU A . n 
A 1 532 ILE 532 532 532 ILE ILE A . n 
A 1 533 GLY 533 533 533 GLY GLY A . n 
A 1 534 THR 534 534 534 THR THR A . n 
A 1 535 VAL 535 535 535 VAL VAL A . n 
A 1 536 LEU 536 536 536 LEU LEU A . n 
A 1 537 LEU 537 537 537 LEU LEU A . n 
A 1 538 VAL 538 538 538 VAL VAL A . n 
A 1 539 GLY 539 539 539 GLY GLY A . n 
A 1 540 ALA 540 540 540 ALA ALA A . n 
A 1 541 LEU 541 541 541 LEU LEU A . n 
A 1 542 THR 542 542 542 THR THR A . n 
A 1 543 PHE 543 543 543 PHE PHE A . n 
A 1 544 ILE 544 544 544 ILE ILE A . n 
A 1 545 PRO 545 545 545 PRO PRO A . n 
A 1 546 ALA 546 546 546 ALA ALA A . n 
A 1 547 LEU 547 547 547 LEU LEU A . n 
A 1 548 ALA 548 548 548 ALA ALA A . n 
A 1 549 LEU 549 549 549 LEU LEU A . n 
A 1 550 GLY 550 550 550 GLY GLY A . n 
A 1 551 PRO 551 551 551 PRO PRO A . n 
A 1 552 VAL 552 552 552 VAL VAL A . n 
A 1 553 ALA 553 553 553 ALA ALA A . n 
A 1 554 GLU 554 554 554 GLU GLU A . n 
A 1 555 TYR 555 555 555 TYR TYR A . n 
A 1 556 LEU 556 556 556 LEU LEU A . n 
A 1 557 SER 557 557 557 SER SER A . n 
B 2 1   MET 1   1   ?   ?   ?   B . n 
B 2 2   SER 2   2   2   SER SER B . n 
B 2 3   ARG 3   3   3   ARG ARG B . n 
B 2 4   LYS 4   4   4   LYS LYS B . n 
B 2 5   GLN 5   5   5   GLN GLN B . n 
B 2 6   LEU 6   6   6   LEU LEU B . n 
B 2 7   ALA 7   7   7   ALA ALA B . n 
B 2 8   LEU 8   8   8   LEU LEU B . n 
B 2 9   PHE 9   9   9   PHE PHE B . n 
B 2 10  GLU 10  10  10  GLU GLU B . n 
B 2 11  PRO 11  11  11  PRO PRO B . n 
B 2 12  THR 12  12  12  THR THR B . n 
B 2 13  LEU 13  13  13  LEU LEU B . n 
B 2 14  VAL 14  14  14  VAL VAL B . n 
B 2 15  VAL 15  15  15  VAL VAL B . n 
B 2 16  GLN 16  16  16  GLN GLN B . n 
B 2 17  ALA 17  17  17  ALA ALA B . n 
B 2 18  LEU 18  18  18  LEU LEU B . n 
B 2 19  LYS 19  19  19  LYS LYS B . n 
B 2 20  GLU 20  20  20  GLU GLU B . n 
B 2 21  ALA 21  21  21  ALA ALA B . n 
B 2 22  VAL 22  22  22  VAL VAL B . n 
B 2 23  LYS 23  23  23  LYS LYS B . n 
B 2 24  LYS 24  24  24  LYS LYS B . n 
B 2 25  LEU 25  25  25  LEU LEU B . n 
B 2 26  ASN 26  26  26  ASN ASN B . n 
B 2 27  PRO 27  27  27  PRO PRO B . n 
B 2 28  GLN 28  28  28  GLN GLN B . n 
B 2 29  ALA 29  29  29  ALA ALA B . n 
B 2 30  GLN 30  30  30  GLN GLN B . n 
B 2 31  TRP 31  31  31  TRP TRP B . n 
B 2 32  ARG 32  32  32  ARG ARG B . n 
B 2 33  ASN 33  33  33  ASN ASN B . n 
B 2 34  PRO 34  34  34  PRO PRO B . n 
B 2 35  VAL 35  35  35  VAL VAL B . n 
B 2 36  MET 36  36  36  MET MET B . n 
B 2 37  PHE 37  37  37  PHE PHE B . n 
B 2 38  ILE 38  38  38  ILE ILE B . n 
B 2 39  VAL 39  39  39  VAL VAL B . n 
B 2 40  TRP 40  40  40  TRP TRP B . n 
B 2 41  ILE 41  41  41  ILE ILE B . n 
B 2 42  GLY 42  42  42  GLY GLY B . n 
B 2 43  SER 43  43  43  SER SER B . n 
B 2 44  LEU 44  44  44  LEU LEU B . n 
B 2 45  LEU 45  45  45  LEU LEU B . n 
B 2 46  THR 46  46  46  THR THR B . n 
B 2 47  THR 47  47  47  THR THR B . n 
B 2 48  CYS 48  48  48  CYS CYS B . n 
B 2 49  ILE 49  49  49  ILE ILE B . n 
B 2 50  SER 50  50  50  SER SER B . n 
B 2 51  ILE 51  51  51  ILE ILE B . n 
B 2 52  ALA 52  52  52  ALA ALA B . n 
B 2 53  MET 53  53  53  MET MET B . n 
B 2 54  ALA 54  54  54  ALA ALA B . n 
B 2 55  SER 55  55  55  SER SER B . n 
B 2 56  GLY 56  56  56  GLY GLY B . n 
B 2 57  ALA 57  57  57  ALA ALA B . n 
B 2 58  MET 58  58  58  MET MET B . n 
B 2 59  PRO 59  59  59  PRO PRO B . n 
B 2 60  GLY 60  60  60  GLY GLY B . n 
B 2 61  ASN 61  61  61  ASN ASN B . n 
B 2 62  ALA 62  62  62  ALA ALA B . n 
B 2 63  LEU 63  63  63  LEU LEU B . n 
B 2 64  PHE 64  64  64  PHE PHE B . n 
B 2 65  SER 65  65  65  SER SER B . n 
B 2 66  ALA 66  66  66  ALA ALA B . n 
B 2 67  ALA 67  67  67  ALA ALA B . n 
B 2 68  ILE 68  68  68  ILE ILE B . n 
B 2 69  SER 69  69  69  SER SER B . n 
B 2 70  GLY 70  70  70  GLY GLY B . n 
B 2 71  TRP 71  71  71  TRP TRP B . n 
B 2 72  LEU 72  72  72  LEU LEU B . n 
B 2 73  TRP 73  73  73  TRP TRP B . n 
B 2 74  ILE 74  74  74  ILE ILE B . n 
B 2 75  THR 75  75  75  THR THR B . n 
B 2 76  VAL 76  76  76  VAL VAL B . n 
B 2 77  LEU 77  77  77  LEU LEU B . n 
B 2 78  PHE 78  78  78  PHE PHE B . n 
B 2 79  ALA 79  79  79  ALA ALA B . n 
B 2 80  ASN 80  80  80  ASN ASN B . n 
B 2 81  PHE 81  81  81  PHE PHE B . n 
B 2 82  ALA 82  82  82  ALA ALA B . n 
B 2 83  GLU 83  83  83  GLU GLU B . n 
B 2 84  ALA 84  84  84  ALA ALA B . n 
B 2 85  LEU 85  85  85  LEU LEU B . n 
B 2 86  ALA 86  86  86  ALA ALA B . n 
B 2 87  GLU 87  87  87  GLU GLU B . n 
B 2 88  GLY 88  88  88  GLY GLY B . n 
B 2 89  ARG 89  89  89  ARG ARG B . n 
B 2 90  SER 90  90  90  SER SER B . n 
B 2 91  LYS 91  91  91  LYS LYS B . n 
B 2 92  ALA 92  92  92  ALA ALA B . n 
B 2 93  GLN 93  93  93  GLN GLN B . n 
B 2 94  ALA 94  94  94  ALA ALA B . n 
B 2 95  ASN 95  95  95  ASN ASN B . n 
B 2 96  SER 96  96  96  SER SER B . n 
B 2 97  LEU 97  97  97  LEU LEU B . n 
B 2 98  LYS 98  98  98  LYS LYS B . n 
B 2 99  GLY 99  99  99  GLY GLY B . n 
B 2 100 VAL 100 100 100 VAL VAL B . n 
B 2 101 LYS 101 101 101 LYS LYS B . n 
B 2 102 LYS 102 102 102 LYS LYS B . n 
B 2 103 THR 103 103 103 THR THR B . n 
B 2 104 ALA 104 104 104 ALA ALA B . n 
B 2 105 PHE 105 105 105 PHE PHE B . n 
B 2 106 ALA 106 106 106 ALA ALA B . n 
B 2 107 ARG 107 107 107 ARG ARG B . n 
B 2 108 LYS 108 108 108 LYS LYS B . n 
B 2 109 LEU 109 109 109 LEU LEU B . n 
B 2 110 ARG 110 110 110 ARG ARG B . n 
B 2 111 GLU 111 111 111 GLU GLU B . n 
B 2 112 PRO 112 112 112 PRO PRO B . n 
B 2 113 LYS 113 113 113 LYS LYS B . n 
B 2 114 TYR 114 114 114 TYR TYR B . n 
B 2 115 GLY 115 115 115 GLY GLY B . n 
B 2 116 ALA 116 116 116 ALA ALA B . n 
B 2 117 ALA 117 117 117 ALA ALA B . n 
B 2 118 ALA 118 118 118 ALA ALA B . n 
B 2 119 ASP 119 119 119 ASP ASP B . n 
B 2 120 LYS 120 120 120 LYS LYS B . n 
B 2 121 VAL 121 121 121 VAL VAL B . n 
B 2 122 PRO 122 122 122 PRO PRO B . n 
B 2 123 ALA 123 123 123 ALA ALA B . n 
B 2 124 ASP 124 124 124 ASP ASP B . n 
B 2 125 GLN 125 125 125 GLN GLN B . n 
B 2 126 LEU 126 126 126 LEU LEU B . n 
B 2 127 ARG 127 127 127 ARG ARG B . n 
B 2 128 LYS 128 128 128 LYS LYS B . n 
B 2 129 GLY 129 129 129 GLY GLY B . n 
B 2 130 ASP 130 130 130 ASP ASP B . n 
B 2 131 ILE 131 131 131 ILE ILE B . n 
B 2 132 VAL 132 132 132 VAL VAL B . n 
B 2 133 LEU 133 133 133 LEU LEU B . n 
B 2 134 VAL 134 134 134 VAL VAL B . n 
B 2 135 GLU 135 135 135 GLU GLU B . n 
B 2 136 ALA 136 136 136 ALA ALA B . n 
B 2 137 GLY 137 137 137 GLY GLY B . n 
B 2 138 ASP 138 138 138 ASP ASP B . n 
B 2 139 ILE 139 139 139 ILE ILE B . n 
B 2 140 ILE 140 140 140 ILE ILE B . n 
B 2 141 PRO 141 141 141 PRO PRO B . n 
B 2 142 CYS 142 142 142 CYS CYS B . n 
B 2 143 ASP 143 143 143 ASP ASP B . n 
B 2 144 GLY 144 144 144 GLY GLY B . n 
B 2 145 GLU 145 145 145 GLU GLU B . n 
B 2 146 VAL 146 146 146 VAL VAL B . n 
B 2 147 ILE 147 147 147 ILE ILE B . n 
B 2 148 GLU 148 148 148 GLU GLU B . n 
B 2 149 GLY 149 149 149 GLY GLY B . n 
B 2 150 GLY 150 150 150 GLY GLY B . n 
B 2 151 ALA 151 151 151 ALA ALA B . n 
B 2 152 SER 152 152 152 SER SER B . n 
B 2 153 VAL 153 153 153 VAL VAL B . n 
B 2 154 ASP 154 154 154 ASP ASP B . n 
B 2 155 GLU 155 155 155 GLU GLU B . n 
B 2 156 SER 156 156 156 SER SER B . n 
B 2 157 ALA 157 157 157 ALA ALA B . n 
B 2 158 ILE 158 158 158 ILE ILE B . n 
B 2 159 THR 159 159 159 THR THR B . n 
B 2 160 GLY 160 160 160 GLY GLY B . n 
B 2 161 GLU 161 161 161 GLU GLU B . n 
B 2 162 SER 162 162 162 SER SER B . n 
B 2 163 ALA 163 163 163 ALA ALA B . n 
B 2 164 PRO 164 164 164 PRO PRO B . n 
B 2 165 VAL 165 165 165 VAL VAL B . n 
B 2 166 ILE 166 166 166 ILE ILE B . n 
B 2 167 ARG 167 167 167 ARG ARG B . n 
B 2 168 GLU 168 168 168 GLU GLU B . n 
B 2 169 SER 169 169 169 SER SER B . n 
B 2 170 GLY 170 170 170 GLY GLY B . n 
B 2 171 GLY 171 171 171 GLY GLY B . n 
B 2 172 ASP 172 172 172 ASP ASP B . n 
B 2 173 PHE 173 173 173 PHE PHE B . n 
B 2 174 ALA 174 174 174 ALA ALA B . n 
B 2 175 SER 175 175 175 SER SER B . n 
B 2 176 VAL 176 176 176 VAL VAL B . n 
B 2 177 THR 177 177 177 THR THR B . n 
B 2 178 GLY 178 178 178 GLY GLY B . n 
B 2 179 GLY 179 179 179 GLY GLY B . n 
B 2 180 THR 180 180 180 THR THR B . n 
B 2 181 ARG 181 181 181 ARG ARG B . n 
B 2 182 ILE 182 182 182 ILE ILE B . n 
B 2 183 LEU 183 183 183 LEU LEU B . n 
B 2 184 SER 184 184 184 SER SER B . n 
B 2 185 ASP 185 185 185 ASP ASP B . n 
B 2 186 TRP 186 186 186 TRP TRP B . n 
B 2 187 LEU 187 187 187 LEU LEU B . n 
B 2 188 VAL 188 188 188 VAL VAL B . n 
B 2 189 ILE 189 189 189 ILE ILE B . n 
B 2 190 GLU 190 190 190 GLU GLU B . n 
B 2 191 CYS 191 191 191 CYS CYS B . n 
B 2 192 SER 192 192 192 SER SER B . n 
B 2 193 VAL 193 193 193 VAL VAL B . n 
B 2 194 ASN 194 194 194 ASN ASN B . n 
B 2 195 PRO 195 195 195 PRO PRO B . n 
B 2 196 GLY 196 196 196 GLY GLY B . n 
B 2 197 GLU 197 197 197 GLU GLU B . n 
B 2 198 THR 198 198 198 THR THR B . n 
B 2 199 PHE 199 199 199 PHE PHE B . n 
B 2 200 LEU 200 200 200 LEU LEU B . n 
B 2 201 ASP 201 201 201 ASP ASP B . n 
B 2 202 ARG 202 202 202 ARG ARG B . n 
B 2 203 MET 203 203 203 MET MET B . n 
B 2 204 ILE 204 204 204 ILE ILE B . n 
B 2 205 ALA 205 205 205 ALA ALA B . n 
B 2 206 MET 206 206 206 MET MET B . n 
B 2 207 VAL 207 207 207 VAL VAL B . n 
B 2 208 GLU 208 208 208 GLU GLU B . n 
B 2 209 GLY 209 209 209 GLY GLY B . n 
B 2 210 ALA 210 210 210 ALA ALA B . n 
B 2 211 GLN 211 211 211 GLN GLN B . n 
B 2 212 ARG 212 212 212 ARG ARG B . n 
B 2 213 ARG 213 213 213 ARG ARG B . n 
B 2 214 LYS 214 214 214 LYS LYS B . n 
B 2 215 THR 215 215 215 THR THR B . n 
B 2 216 PRO 216 216 216 PRO PRO B . n 
B 2 217 ASN 217 217 217 ASN ASN B . n 
B 2 218 GLU 218 218 218 GLU GLU B . n 
B 2 219 ILE 219 219 219 ILE ILE B . n 
B 2 220 ALA 220 220 220 ALA ALA B . n 
B 2 221 LEU 221 221 221 LEU LEU B . n 
B 2 222 THR 222 222 222 THR THR B . n 
B 2 223 ILE 223 223 223 ILE ILE B . n 
B 2 224 LEU 224 224 224 LEU LEU B . n 
B 2 225 LEU 225 225 225 LEU LEU B . n 
B 2 226 ILE 226 226 226 ILE ILE B . n 
B 2 227 ALA 227 227 227 ALA ALA B . n 
B 2 228 LEU 228 228 228 LEU LEU B . n 
B 2 229 THR 229 229 229 THR THR B . n 
B 2 230 ILE 230 230 230 ILE ILE B . n 
B 2 231 VAL 231 231 231 VAL VAL B . n 
B 2 232 PHE 232 232 232 PHE PHE B . n 
B 2 233 LEU 233 233 233 LEU LEU B . n 
B 2 234 LEU 234 234 234 LEU LEU B . n 
B 2 235 ALA 235 235 235 ALA ALA B . n 
B 2 236 THR 236 236 236 THR THR B . n 
B 2 237 ALA 237 237 237 ALA ALA B . n 
B 2 238 THR 238 238 238 THR THR B . n 
B 2 239 LEU 239 239 239 LEU LEU B . n 
B 2 240 TRP 240 240 240 TRP TRP B . n 
B 2 241 PRO 241 241 241 PRO PRO B . n 
B 2 242 PHE 242 242 242 PHE PHE B . n 
B 2 243 SER 243 243 243 SER SER B . n 
B 2 244 ALA 244 244 244 ALA ALA B . n 
B 2 245 TRP 245 245 245 TRP TRP B . n 
B 2 246 GLY 246 246 246 GLY GLY B . n 
B 2 247 GLY 247 247 247 GLY GLY B . n 
B 2 248 ASN 248 248 248 ASN ASN B . n 
B 2 249 ALA 249 249 249 ALA ALA B . n 
B 2 250 VAL 250 250 250 VAL VAL B . n 
B 2 251 SER 251 251 251 SER SER B . n 
B 2 252 VAL 252 252 252 VAL VAL B . n 
B 2 253 THR 253 253 253 THR THR B . n 
B 2 254 VAL 254 254 254 VAL VAL B . n 
B 2 255 LEU 255 255 255 LEU LEU B . n 
B 2 256 VAL 256 256 256 VAL VAL B . n 
B 2 257 ALA 257 257 257 ALA ALA B . n 
B 2 258 LEU 258 258 258 LEU LEU B . n 
B 2 259 LEU 259 259 259 LEU LEU B . n 
B 2 260 VAL 260 260 260 VAL VAL B . n 
B 2 261 CYS 261 261 261 CYS CYS B . n 
B 2 262 LEU 262 262 262 LEU LEU B . n 
B 2 263 ILE 263 263 263 ILE ILE B . n 
B 2 264 PRO 264 264 264 PRO PRO B . n 
B 2 265 THR 265 265 265 THR THR B . n 
B 2 266 THR 266 266 266 THR THR B . n 
B 2 267 ILE 267 267 267 ILE ILE B . n 
B 2 268 GLY 268 268 268 GLY GLY B . n 
B 2 269 GLY 269 269 269 GLY GLY B . n 
B 2 270 LEU 270 270 270 LEU LEU B . n 
B 2 271 LEU 271 271 271 LEU LEU B . n 
B 2 272 SER 272 272 272 SER SER B . n 
B 2 273 ALA 273 273 273 ALA ALA B . n 
B 2 274 ILE 274 274 274 ILE ILE B . n 
B 2 275 GLY 275 275 275 GLY GLY B . n 
B 2 276 VAL 276 276 276 VAL VAL B . n 
B 2 277 ALA 277 277 277 ALA ALA B . n 
B 2 278 GLY 278 278 278 GLY GLY B . n 
B 2 279 MET 279 279 279 MET MET B . n 
B 2 280 SER 280 280 280 SER SER B . n 
B 2 281 ARG 281 281 281 ARG ARG B . n 
B 2 282 MET 282 282 282 MET MET B . n 
B 2 283 LEU 283 283 283 LEU LEU B . n 
B 2 284 GLY 284 284 284 GLY GLY B . n 
B 2 285 ALA 285 285 285 ALA ALA B . n 
B 2 286 ASN 286 286 286 ASN ASN B . n 
B 2 287 VAL 287 287 287 VAL VAL B . n 
B 2 288 ILE 288 288 288 ILE ILE B . n 
B 2 289 ALA 289 289 289 ALA ALA B . n 
B 2 290 THR 290 290 290 THR THR B . n 
B 2 291 SER 291 291 291 SER SER B . n 
B 2 292 GLY 292 292 292 GLY GLY B . n 
B 2 293 ARG 293 293 293 ARG ARG B . n 
B 2 294 ALA 294 294 294 ALA ALA B . n 
B 2 295 VAL 295 295 295 VAL VAL B . n 
B 2 296 GLU 296 296 296 GLU GLU B . n 
B 2 297 ALA 297 297 297 ALA ALA B . n 
B 2 298 ALA 298 298 298 ALA ALA B . n 
B 2 299 GLY 299 299 299 GLY GLY B . n 
B 2 300 ASP 300 300 300 ASP ASP B . n 
B 2 301 VAL 301 301 301 VAL VAL B . n 
B 2 302 ASP 302 302 302 ASP ASP B . n 
B 2 303 VAL 303 303 303 VAL VAL B . n 
B 2 304 LEU 304 304 304 LEU LEU B . n 
B 2 305 LEU 305 305 305 LEU LEU B . n 
B 2 306 LEU 306 306 306 LEU LEU B . n 
B 2 307 PHD 307 307 307 PHD PHD B . n 
B 2 308 LYS 308 308 308 LYS LYS B . n 
B 2 309 THR 309 309 309 THR THR B . n 
B 2 310 GLY 310 310 310 GLY GLY B . n 
B 2 311 THR 311 311 311 THR THR B . n 
B 2 312 ILE 312 312 312 ILE ILE B . n 
B 2 313 THR 313 313 313 THR THR B . n 
B 2 314 LEU 314 314 314 LEU LEU B . n 
B 2 315 GLY 315 315 315 GLY GLY B . n 
B 2 316 ASN 316 316 316 ASN ASN B . n 
B 2 317 ARG 317 317 317 ARG ARG B . n 
B 2 318 GLN 318 318 318 GLN GLN B . n 
B 2 319 ALA 319 319 319 ALA ALA B . n 
B 2 320 SER 320 320 320 SER SER B . n 
B 2 321 GLU 321 321 321 GLU GLU B . n 
B 2 322 PHE 322 322 322 PHE PHE B . n 
B 2 323 ILE 323 323 323 ILE ILE B . n 
B 2 324 PRO 324 324 324 PRO PRO B . n 
B 2 325 ALA 325 325 325 ALA ALA B . n 
B 2 326 GLN 326 326 326 GLN GLN B . n 
B 2 327 GLY 327 327 327 GLY GLY B . n 
B 2 328 VAL 328 328 328 VAL VAL B . n 
B 2 329 ASP 329 329 329 ASP ASP B . n 
B 2 330 GLU 330 330 330 GLU GLU B . n 
B 2 331 LYS 331 331 331 LYS LYS B . n 
B 2 332 THR 332 332 332 THR THR B . n 
B 2 333 LEU 333 333 333 LEU LEU B . n 
B 2 334 ALA 334 334 334 ALA ALA B . n 
B 2 335 ASP 335 335 335 ASP ASP B . n 
B 2 336 ALA 336 336 336 ALA ALA B . n 
B 2 337 ALA 337 337 337 ALA ALA B . n 
B 2 338 GLN 338 338 338 GLN GLN B . n 
B 2 339 LEU 339 339 339 LEU LEU B . n 
B 2 340 ALA 340 340 340 ALA ALA B . n 
B 2 341 SER 341 341 341 SER SER B . n 
B 2 342 LEU 342 342 342 LEU LEU B . n 
B 2 343 ALA 343 343 343 ALA ALA B . n 
B 2 344 ASP 344 344 344 ASP ASP B . n 
B 2 345 GLU 345 345 345 GLU GLU B . n 
B 2 346 THR 346 346 346 THR THR B . n 
B 2 347 PRO 347 347 347 PRO PRO B . n 
B 2 348 GLU 348 348 348 GLU GLU B . n 
B 2 349 GLY 349 349 349 GLY GLY B . n 
B 2 350 ARG 350 350 350 ARG ARG B . n 
B 2 351 SER 351 351 351 SER SER B . n 
B 2 352 ILE 352 352 352 ILE ILE B . n 
B 2 353 VAL 353 353 353 VAL VAL B . n 
B 2 354 ILE 354 354 354 ILE ILE B . n 
B 2 355 LEU 355 355 355 LEU LEU B . n 
B 2 356 ALA 356 356 356 ALA ALA B . n 
B 2 357 LYS 357 357 357 LYS LYS B . n 
B 2 358 GLN 358 358 358 GLN GLN B . n 
B 2 359 ARG 359 359 359 ARG ARG B . n 
B 2 360 PHE 360 360 360 PHE PHE B . n 
B 2 361 ASN 361 361 361 ASN ASN B . n 
B 2 362 LEU 362 362 362 LEU LEU B . n 
B 2 363 ARG 363 363 363 ARG ARG B . n 
B 2 364 GLU 364 364 364 GLU GLU B . n 
B 2 365 ARG 365 365 365 ARG ARG B . n 
B 2 366 ASP 366 366 366 ASP ASP B . n 
B 2 367 VAL 367 367 367 VAL VAL B . n 
B 2 368 GLN 368 368 368 GLN GLN B . n 
B 2 369 SER 369 369 369 SER SER B . n 
B 2 370 LEU 370 370 370 LEU LEU B . n 
B 2 371 HIS 371 371 371 HIS HIS B . n 
B 2 372 ALA 372 372 372 ALA ALA B . n 
B 2 373 THR 373 373 373 THR THR B . n 
B 2 374 PHE 374 374 374 PHE PHE B . n 
B 2 375 VAL 375 375 375 VAL VAL B . n 
B 2 376 PRO 376 376 376 PRO PRO B . n 
B 2 377 PHE 377 377 377 PHE PHE B . n 
B 2 378 THR 378 378 378 THR THR B . n 
B 2 379 ALA 379 379 379 ALA ALA B . n 
B 2 380 GLN 380 380 380 GLN GLN B . n 
B 2 381 SER 381 381 381 SER SER B . n 
B 2 382 ARG 382 382 382 ARG ARG B . n 
B 2 383 MET 383 383 383 MET MET B . n 
B 2 384 SER 384 384 384 SER SER B . n 
B 2 385 GLY 385 385 385 GLY GLY B . n 
B 2 386 ILE 386 386 386 ILE ILE B . n 
B 2 387 ASN 387 387 387 ASN ASN B . n 
B 2 388 ILE 388 388 388 ILE ILE B . n 
B 2 389 ASP 389 389 389 ASP ASP B . n 
B 2 390 ASN 390 390 390 ASN ASN B . n 
B 2 391 ARG 391 391 391 ARG ARG B . n 
B 2 392 MET 392 392 392 MET MET B . n 
B 2 393 ILE 393 393 393 ILE ILE B . n 
B 2 394 ARG 394 394 394 ARG ARG B . n 
B 2 395 LYS 395 395 395 LYS LYS B . n 
B 2 396 GLY 396 396 396 GLY GLY B . n 
B 2 397 SER 397 397 397 SER SER B . n 
B 2 398 VAL 398 398 398 VAL VAL B . n 
B 2 399 ASP 399 399 399 ASP ASP B . n 
B 2 400 ALA 400 400 400 ALA ALA B . n 
B 2 401 ILE 401 401 401 ILE ILE B . n 
B 2 402 ARG 402 402 402 ARG ARG B . n 
B 2 403 ARG 403 403 403 ARG ARG B . n 
B 2 404 HIS 404 404 404 HIS HIS B . n 
B 2 405 VAL 405 405 405 VAL VAL B . n 
B 2 406 GLU 406 406 406 GLU GLU B . n 
B 2 407 ALA 407 407 407 ALA ALA B . n 
B 2 408 ASN 408 408 408 ASN ASN B . n 
B 2 409 GLY 409 409 409 GLY GLY B . n 
B 2 410 GLY 410 410 410 GLY GLY B . n 
B 2 411 HIS 411 411 411 HIS HIS B . n 
B 2 412 PHE 412 412 412 PHE PHE B . n 
B 2 413 PRO 413 413 413 PRO PRO B . n 
B 2 414 THR 414 414 414 THR THR B . n 
B 2 415 ASP 415 415 415 ASP ASP B . n 
B 2 416 VAL 416 416 416 VAL VAL B . n 
B 2 417 ASP 417 417 417 ASP ASP B . n 
B 2 418 GLN 418 418 418 GLN GLN B . n 
B 2 419 LYS 419 419 419 LYS LYS B . n 
B 2 420 VAL 420 420 420 VAL VAL B . n 
B 2 421 ASP 421 421 421 ASP ASP B . n 
B 2 422 GLN 422 422 422 GLN GLN B . n 
B 2 423 VAL 423 423 423 VAL VAL B . n 
B 2 424 ALA 424 424 424 ALA ALA B . n 
B 2 425 ARG 425 425 425 ARG ARG B . n 
B 2 426 GLN 426 426 426 GLN GLN B . n 
B 2 427 GLY 427 427 427 GLY GLY B . n 
B 2 428 ALA 428 428 428 ALA ALA B . n 
B 2 429 THR 429 429 429 THR THR B . n 
B 2 430 PRO 430 430 430 PRO PRO B . n 
B 2 431 LEU 431 431 431 LEU LEU B . n 
B 2 432 VAL 432 432 432 VAL VAL B . n 
B 2 433 VAL 433 433 433 VAL VAL B . n 
B 2 434 VAL 434 434 434 VAL VAL B . n 
B 2 435 GLU 435 435 435 GLU GLU B . n 
B 2 436 GLY 436 436 436 GLY GLY B . n 
B 2 437 SER 437 437 437 SER SER B . n 
B 2 438 ARG 438 438 438 ARG ARG B . n 
B 2 439 VAL 439 439 439 VAL VAL B . n 
B 2 440 LEU 440 440 440 LEU LEU B . n 
B 2 441 GLY 441 441 441 GLY GLY B . n 
B 2 442 VAL 442 442 442 VAL VAL B . n 
B 2 443 ILE 443 443 443 ILE ILE B . n 
B 2 444 ALA 444 444 444 ALA ALA B . n 
B 2 445 LEU 445 445 445 LEU LEU B . n 
B 2 446 LYS 446 446 446 LYS LYS B . n 
B 2 447 ASP 447 447 447 ASP ASP B . n 
B 2 448 ILE 448 448 448 ILE ILE B . n 
B 2 449 VAL 449 449 449 VAL VAL B . n 
B 2 450 LYS 450 450 450 LYS LYS B . n 
B 2 451 GLY 451 451 451 GLY GLY B . n 
B 2 452 GLY 452 452 452 GLY GLY B . n 
B 2 453 ILE 453 453 453 ILE ILE B . n 
B 2 454 LYS 454 454 454 LYS LYS B . n 
B 2 455 GLU 455 455 455 GLU GLU B . n 
B 2 456 ARG 456 456 456 ARG ARG B . n 
B 2 457 PHE 457 457 457 PHE PHE B . n 
B 2 458 ALA 458 458 458 ALA ALA B . n 
B 2 459 GLN 459 459 459 GLN GLN B . n 
B 2 460 LEU 460 460 460 LEU LEU B . n 
B 2 461 ARG 461 461 461 ARG ARG B . n 
B 2 462 LYS 462 462 462 LYS LYS B . n 
B 2 463 MET 463 463 463 MET MET B . n 
B 2 464 GLY 464 464 464 GLY GLY B . n 
B 2 465 ILE 465 465 465 ILE ILE B . n 
B 2 466 LYS 466 466 466 LYS LYS B . n 
B 2 467 THR 467 467 467 THR THR B . n 
B 2 468 VAL 468 468 468 VAL VAL B . n 
B 2 469 MET 469 469 469 MET MET B . n 
B 2 470 ILE 470 470 470 ILE ILE B . n 
B 2 471 THR 471 471 471 THR THR B . n 
B 2 472 GLY 472 472 472 GLY GLY B . n 
B 2 473 ASP 473 473 473 ASP ASP B . n 
B 2 474 ASN 474 474 474 ASN ASN B . n 
B 2 475 ARG 475 475 475 ARG ARG B . n 
B 2 476 LEU 476 476 476 LEU LEU B . n 
B 2 477 THR 477 477 477 THR THR B . n 
B 2 478 ALA 478 478 478 ALA ALA B . n 
B 2 479 ALA 479 479 479 ALA ALA B . n 
B 2 480 ALA 480 480 480 ALA ALA B . n 
B 2 481 ILE 481 481 481 ILE ILE B . n 
B 2 482 ALA 482 482 482 ALA ALA B . n 
B 2 483 ALA 483 483 483 ALA ALA B . n 
B 2 484 GLU 484 484 484 GLU GLU B . n 
B 2 485 ALA 485 485 485 ALA ALA B . n 
B 2 486 GLY 486 486 486 GLY GLY B . n 
B 2 487 VAL 487 487 487 VAL VAL B . n 
B 2 488 ASP 488 488 488 ASP ASP B . n 
B 2 489 ASP 489 489 489 ASP ASP B . n 
B 2 490 PHE 490 490 490 PHE PHE B . n 
B 2 491 LEU 491 491 491 LEU LEU B . n 
B 2 492 ALA 492 492 492 ALA ALA B . n 
B 2 493 GLU 493 493 493 GLU GLU B . n 
B 2 494 ALA 494 494 494 ALA ALA B . n 
B 2 495 THR 495 495 495 THR THR B . n 
B 2 496 PRO 496 496 496 PRO PRO B . n 
B 2 497 GLU 497 497 497 GLU GLU B . n 
B 2 498 ALA 498 498 498 ALA ALA B . n 
B 2 499 LYS 499 499 499 LYS LYS B . n 
B 2 500 LEU 500 500 500 LEU LEU B . n 
B 2 501 ALA 501 501 501 ALA ALA B . n 
B 2 502 LEU 502 502 502 LEU LEU B . n 
B 2 503 ILE 503 503 503 ILE ILE B . n 
B 2 504 ARG 504 504 504 ARG ARG B . n 
B 2 505 GLN 505 505 505 GLN GLN B . n 
B 2 506 TYR 506 506 506 TYR TYR B . n 
B 2 507 GLN 507 507 507 GLN GLN B . n 
B 2 508 ALA 508 508 508 ALA ALA B . n 
B 2 509 GLU 509 509 509 GLU GLU B . n 
B 2 510 GLY 510 510 510 GLY GLY B . n 
B 2 511 ARG 511 511 511 ARG ARG B . n 
B 2 512 LEU 512 512 512 LEU LEU B . n 
B 2 513 VAL 513 513 513 VAL VAL B . n 
B 2 514 ALA 514 514 514 ALA ALA B . n 
B 2 515 MET 515 515 515 MET MET B . n 
B 2 516 THR 516 516 516 THR THR B . n 
B 2 517 GLY 517 517 517 GLY GLY B . n 
B 2 518 ASP 518 518 518 ASP ASP B . n 
B 2 519 GLY 519 519 519 GLY GLY B . n 
B 2 520 THR 520 520 520 THR THR B . n 
B 2 521 ASN 521 521 521 ASN ASN B . n 
B 2 522 ASP 522 522 522 ASP ASP B . n 
B 2 523 ALA 523 523 523 ALA ALA B . n 
B 2 524 PRO 524 524 524 PRO PRO B . n 
B 2 525 ALA 525 525 525 ALA ALA B . n 
B 2 526 LEU 526 526 526 LEU LEU B . n 
B 2 527 ALA 527 527 527 ALA ALA B . n 
B 2 528 GLN 528 528 528 GLN GLN B . n 
B 2 529 ALA 529 529 529 ALA ALA B . n 
B 2 530 ASP 530 530 530 ASP ASP B . n 
B 2 531 VAL 531 531 531 VAL VAL B . n 
B 2 532 ALA 532 532 532 ALA ALA B . n 
B 2 533 VAL 533 533 533 VAL VAL B . n 
B 2 534 ALA 534 534 534 ALA ALA B . n 
B 2 535 MET 535 535 535 MET MET B . n 
B 2 536 ASN 536 536 536 ASN ASN B . n 
B 2 537 SER 537 537 537 SER SER B . n 
B 2 538 GLY 538 538 538 GLY GLY B . n 
B 2 539 THR 539 539 539 THR THR B . n 
B 2 540 GLN 540 540 540 GLN GLN B . n 
B 2 541 ALA 541 541 541 ALA ALA B . n 
B 2 542 ALA 542 542 542 ALA ALA B . n 
B 2 543 LYS 543 543 543 LYS LYS B . n 
B 2 544 GLU 544 544 544 GLU GLU B . n 
B 2 545 ALA 545 545 545 ALA ALA B . n 
B 2 546 GLY 546 546 546 GLY GLY B . n 
B 2 547 ASN 547 547 547 ASN ASN B . n 
B 2 548 MET 548 548 548 MET MET B . n 
B 2 549 VAL 549 549 549 VAL VAL B . n 
B 2 550 ASP 550 550 550 ASP ASP B . n 
B 2 551 LEU 551 551 551 LEU LEU B . n 
B 2 552 ASP 552 552 552 ASP ASP B . n 
B 2 553 SER 553 553 553 SER SER B . n 
B 2 554 ASN 554 554 554 ASN ASN B . n 
B 2 555 PRO 555 555 555 PRO PRO B . n 
B 2 556 THR 556 556 556 THR THR B . n 
B 2 557 LYS 557 557 557 LYS LYS B . n 
B 2 558 LEU 558 558 558 LEU LEU B . n 
B 2 559 ILE 559 559 559 ILE ILE B . n 
B 2 560 GLU 560 560 560 GLU GLU B . n 
B 2 561 VAL 561 561 561 VAL VAL B . n 
B 2 562 VAL 562 562 562 VAL VAL B . n 
B 2 563 HIS 563 563 563 HIS HIS B . n 
B 2 564 ILE 564 564 564 ILE ILE B . n 
B 2 565 GLY 565 565 565 GLY GLY B . n 
B 2 566 LYS 566 566 566 LYS LYS B . n 
B 2 567 GLN 567 567 567 GLN GLN B . n 
B 2 568 MET 568 568 568 MET MET B . n 
B 2 569 LEU 569 569 569 LEU LEU B . n 
B 2 570 MET 570 570 570 MET MET B . n 
B 2 571 THR 571 571 571 THR THR B . n 
B 2 572 ARG 572 572 572 ARG ARG B . n 
B 2 573 GLY 573 573 573 GLY GLY B . n 
B 2 574 SER 574 574 574 SER SER B . n 
B 2 575 LEU 575 575 575 LEU LEU B . n 
B 2 576 THR 576 576 576 THR THR B . n 
B 2 577 THR 577 577 577 THR THR B . n 
B 2 578 PHE 578 578 578 PHE PHE B . n 
B 2 579 SER 579 579 579 SER SER B . n 
B 2 580 ILE 580 580 580 ILE ILE B . n 
B 2 581 ALA 581 581 581 ALA ALA B . n 
B 2 582 ASN 582 582 582 ASN ASN B . n 
B 2 583 ASP 583 583 583 ASP ASP B . n 
B 2 584 VAL 584 584 584 VAL VAL B . n 
B 2 585 ALA 585 585 585 ALA ALA B . n 
B 2 586 LYS 586 586 586 LYS LYS B . n 
B 2 587 TYR 587 587 587 TYR TYR B . n 
B 2 588 PHE 588 588 588 PHE PHE B . n 
B 2 589 ALA 589 589 589 ALA ALA B . n 
B 2 590 ILE 590 590 590 ILE ILE B . n 
B 2 591 ILE 591 591 591 ILE ILE B . n 
B 2 592 PRO 592 592 592 PRO PRO B . n 
B 2 593 ALA 593 593 593 ALA ALA B . n 
B 2 594 ALA 594 594 594 ALA ALA B . n 
B 2 595 PHE 595 595 595 PHE PHE B . n 
B 2 596 ALA 596 596 596 ALA ALA B . n 
B 2 597 ALA 597 597 597 ALA ALA B . n 
B 2 598 THR 598 598 598 THR THR B . n 
B 2 599 TYR 599 599 599 TYR TYR B . n 
B 2 600 PRO 600 600 600 PRO PRO B . n 
B 2 601 GLN 601 601 601 GLN GLN B . n 
B 2 602 LEU 602 602 602 LEU LEU B . n 
B 2 603 ASN 603 603 603 ASN ASN B . n 
B 2 604 ALA 604 604 604 ALA ALA B . n 
B 2 605 LEU 605 605 605 LEU LEU B . n 
B 2 606 ASN 606 606 606 ASN ASN B . n 
B 2 607 ILE 607 607 607 ILE ILE B . n 
B 2 608 MET 608 608 608 MET MET B . n 
B 2 609 CYS 609 609 609 CYS CYS B . n 
B 2 610 LEU 610 610 610 LEU LEU B . n 
B 2 611 HIS 611 611 611 HIS HIS B . n 
B 2 612 SER 612 612 612 SER SER B . n 
B 2 613 PRO 613 613 613 PRO PRO B . n 
B 2 614 ASP 614 614 614 ASP ASP B . n 
B 2 615 SER 615 615 615 SER SER B . n 
B 2 616 ALA 616 616 616 ALA ALA B . n 
B 2 617 ILE 617 617 617 ILE ILE B . n 
B 2 618 LEU 618 618 618 LEU LEU B . n 
B 2 619 SER 619 619 619 SER SER B . n 
B 2 620 ALA 620 620 620 ALA ALA B . n 
B 2 621 VAL 621 621 621 VAL VAL B . n 
B 2 622 ILE 622 622 622 ILE ILE B . n 
B 2 623 PHE 623 623 623 PHE PHE B . n 
B 2 624 ASN 624 624 624 ASN ASN B . n 
B 2 625 ALA 625 625 625 ALA ALA B . n 
B 2 626 LEU 626 626 626 LEU LEU B . n 
B 2 627 ILE 627 627 627 ILE ILE B . n 
B 2 628 ILE 628 628 628 ILE ILE B . n 
B 2 629 VAL 629 629 629 VAL VAL B . n 
B 2 630 PHE 630 630 630 PHE PHE B . n 
B 2 631 LEU 631 631 631 LEU LEU B . n 
B 2 632 ILE 632 632 632 ILE ILE B . n 
B 2 633 PRO 633 633 633 PRO PRO B . n 
B 2 634 LEU 634 634 634 LEU LEU B . n 
B 2 635 ALA 635 635 635 ALA ALA B . n 
B 2 636 LEU 636 636 636 LEU LEU B . n 
B 2 637 LYS 637 637 637 LYS LYS B . n 
B 2 638 GLY 638 638 638 GLY GLY B . n 
B 2 639 VAL 639 639 639 VAL VAL B . n 
B 2 640 SER 640 640 640 SER SER B . n 
B 2 641 TYR 641 641 641 TYR TYR B . n 
B 2 642 LYS 642 642 642 LYS LYS B . n 
B 2 643 PRO 643 643 643 PRO PRO B . n 
B 2 644 LEU 644 644 644 LEU LEU B . n 
B 2 645 THR 645 645 645 THR THR B . n 
B 2 646 ALA 646 646 646 ALA ALA B . n 
B 2 647 SER 647 647 647 SER SER B . n 
B 2 648 ALA 648 648 648 ALA ALA B . n 
B 2 649 MET 649 649 649 MET MET B . n 
B 2 650 LEU 650 650 650 LEU LEU B . n 
B 2 651 ARG 651 651 651 ARG ARG B . n 
B 2 652 ARG 652 652 652 ARG ARG B . n 
B 2 653 ASN 653 653 653 ASN ASN B . n 
B 2 654 LEU 654 654 654 LEU LEU B . n 
B 2 655 TRP 655 655 655 TRP TRP B . n 
B 2 656 ILE 656 656 656 ILE ILE B . n 
B 2 657 TYR 657 657 657 TYR TYR B . n 
B 2 658 GLY 658 658 658 GLY GLY B . n 
B 2 659 LEU 659 659 659 LEU LEU B . n 
B 2 660 GLY 660 660 660 GLY GLY B . n 
B 2 661 GLY 661 661 661 GLY GLY B . n 
B 2 662 LEU 662 662 662 LEU LEU B . n 
B 2 663 LEU 663 663 663 LEU LEU B . n 
B 2 664 VAL 664 664 664 VAL VAL B . n 
B 2 665 PRO 665 665 665 PRO PRO B . n 
B 2 666 PHE 666 666 666 PHE PHE B . n 
B 2 667 ILE 667 667 667 ILE ILE B . n 
B 2 668 GLY 668 668 668 GLY GLY B . n 
B 2 669 ILE 669 669 669 ILE ILE B . n 
B 2 670 LYS 670 670 670 LYS LYS B . n 
B 2 671 VAL 671 671 671 VAL VAL B . n 
B 2 672 ILE 672 672 672 ILE ILE B . n 
B 2 673 ASP 673 673 673 ASP ASP B . n 
B 2 674 LEU 674 674 674 LEU LEU B . n 
B 2 675 LEU 675 675 675 LEU LEU B . n 
B 2 676 LEU 676 676 676 LEU LEU B . n 
B 2 677 THR 677 677 677 THR THR B . n 
B 2 678 VAL 678 678 678 VAL VAL B . n 
B 2 679 CYS 679 679 679 CYS CYS B . n 
B 2 680 GLY 680 680 680 GLY GLY B . n 
B 2 681 LEU 681 681 681 LEU LEU B . n 
B 2 682 VAL 682 682 682 VAL VAL B . n 
C 3 1   MET 1   1   ?   ?   ?   C . n 
C 3 2   SER 2   2   ?   ?   ?   C . n 
C 3 3   GLY 3   3   3   GLY GLY C . n 
C 3 4   LEU 4   4   4   LEU LEU C . n 
C 3 5   ARG 5   5   5   ARG ARG C . n 
C 3 6   PRO 6   6   6   PRO PRO C . n 
C 3 7   ALA 7   7   7   ALA ALA C . n 
C 3 8   LEU 8   8   8   LEU LEU C . n 
C 3 9   SER 9   9   9   SER SER C . n 
C 3 10  THR 10  10  10  THR THR C . n 
C 3 11  PHE 11  11  11  PHE PHE C . n 
C 3 12  ILE 12  12  12  ILE ILE C . n 
C 3 13  PHE 13  13  13  PHE PHE C . n 
C 3 14  LEU 14  14  14  LEU LEU C . n 
C 3 15  LEU 15  15  15  LEU LEU C . n 
C 3 16  LEU 16  16  16  LEU LEU C . n 
C 3 17  ILE 17  17  17  ILE ILE C . n 
C 3 18  THR 18  18  18  THR THR C . n 
C 3 19  GLY 19  19  19  GLY GLY C . n 
C 3 20  GLY 20  20  20  GLY GLY C . n 
C 3 21  VAL 21  21  21  VAL VAL C . n 
C 3 22  TYR 22  22  22  TYR TYR C . n 
C 3 23  PRO 23  23  23  PRO PRO C . n 
C 3 24  LEU 24  24  24  LEU LEU C . n 
C 3 25  LEU 25  25  25  LEU LEU C . n 
C 3 26  THR 26  26  26  THR THR C . n 
C 3 27  THR 27  27  27  THR THR C . n 
C 3 28  VAL 28  28  28  VAL VAL C . n 
C 3 29  LEU 29  29  29  LEU LEU C . n 
C 3 30  GLY 30  30  30  GLY GLY C . n 
C 3 31  GLN 31  31  31  GLN GLN C . n 
C 3 32  TRP 32  32  32  TRP TRP C . n 
C 3 33  TRP 33  33  33  TRP TRP C . n 
C 3 34  PHE 34  34  34  PHE PHE C . n 
C 3 35  PRO 35  35  35  PRO PRO C . n 
C 3 36  TRP 36  36  36  TRP TRP C . n 
C 3 37  GLN 37  37  37  GLN GLN C . n 
C 3 38  ALA 38  38  38  ALA ALA C . n 
C 3 39  ASN 39  39  39  ASN ASN C . n 
C 3 40  GLY 40  40  40  GLY GLY C . n 
C 3 41  SER 41  41  41  SER SER C . n 
C 3 42  LEU 42  42  42  LEU LEU C . n 
C 3 43  ILE 43  43  43  ILE ILE C . n 
C 3 44  ARG 44  44  44  ARG ARG C . n 
C 3 45  GLU 45  45  45  GLU GLU C . n 
C 3 46  GLY 46  46  46  GLY GLY C . n 
C 3 47  ASP 47  47  47  ASP ASP C . n 
C 3 48  THR 48  48  48  THR THR C . n 
C 3 49  VAL 49  49  49  VAL VAL C . n 
C 3 50  ARG 50  50  50  ARG ARG C . n 
C 3 51  GLY 51  51  51  GLY GLY C . n 
C 3 52  SER 52  52  52  SER SER C . n 
C 3 53  ALA 53  53  53  ALA ALA C . n 
C 3 54  LEU 54  54  54  LEU LEU C . n 
C 3 55  ILE 55  55  55  ILE ILE C . n 
C 3 56  GLY 56  56  56  GLY GLY C . n 
C 3 57  GLN 57  57  57  GLN GLN C . n 
C 3 58  ASN 58  58  58  ASN ASN C . n 
C 3 59  PHE 59  59  59  PHE PHE C . n 
C 3 60  THR 60  60  60  THR THR C . n 
C 3 61  GLY 61  61  61  GLY GLY C . n 
C 3 62  ASN 62  62  62  ASN ASN C . n 
C 3 63  GLY 63  63  63  GLY GLY C . n 
C 3 64  TYR 64  64  64  TYR TYR C . n 
C 3 65  PHE 65  65  65  PHE PHE C . n 
C 3 66  HIS 66  66  66  HIS HIS C . n 
C 3 67  GLY 67  67  67  GLY GLY C . n 
C 3 68  ARG 68  68  68  ARG ARG C . n 
C 3 69  PRO 69  69  69  PRO PRO C . n 
C 3 70  SER 70  70  70  SER SER C . n 
C 3 71  ALA 71  71  71  ALA ALA C . n 
C 3 72  THR 72  72  72  THR THR C . n 
C 3 73  ALA 73  73  73  ALA ALA C . n 
C 3 74  GLU 74  74  74  GLU GLU C . n 
C 3 75  MET 75  75  75  MET MET C . n 
C 3 76  PRO 76  76  76  PRO PRO C . n 
C 3 77  TYR 77  77  77  TYR TYR C . n 
C 3 78  ASN 78  78  78  ASN ASN C . n 
C 3 79  PRO 79  79  79  PRO PRO C . n 
C 3 80  GLN 80  80  80  GLN GLN C . n 
C 3 81  ALA 81  81  81  ALA ALA C . n 
C 3 82  SER 82  82  82  SER SER C . n 
C 3 83  GLY 83  83  83  GLY GLY C . n 
C 3 84  GLY 84  84  84  GLY GLY C . n 
C 3 85  SER 85  85  85  SER SER C . n 
C 3 86  ASN 86  86  86  ASN ASN C . n 
C 3 87  LEU 87  87  87  LEU LEU C . n 
C 3 88  ALA 88  88  88  ALA ALA C . n 
C 3 89  VAL 89  89  89  VAL VAL C . n 
C 3 90  SER 90  90  90  SER SER C . n 
C 3 91  ASN 91  91  91  ASN ASN C . n 
C 3 92  PRO 92  92  92  PRO PRO C . n 
C 3 93  GLU 93  93  93  GLU GLU C . n 
C 3 94  LEU 94  94  94  LEU LEU C . n 
C 3 95  ASP 95  95  95  ASP ASP C . n 
C 3 96  LYS 96  96  96  LYS LYS C . n 
C 3 97  LEU 97  97  97  LEU LEU C . n 
C 3 98  ILE 98  98  98  ILE ILE C . n 
C 3 99  ALA 99  99  99  ALA ALA C . n 
C 3 100 ALA 100 100 100 ALA ALA C . n 
C 3 101 ARG 101 101 101 ARG ARG C . n 
C 3 102 VAL 102 102 102 VAL VAL C . n 
C 3 103 ALA 103 103 103 ALA ALA C . n 
C 3 104 ALA 104 104 104 ALA ALA C . n 
C 3 105 LEU 105 105 105 LEU LEU C . n 
C 3 106 ARG 106 106 106 ARG ARG C . n 
C 3 107 ALA 107 107 107 ALA ALA C . n 
C 3 108 ALA 108 108 108 ALA ALA C . n 
C 3 109 ASN 109 109 109 ASN ASN C . n 
C 3 110 PRO 110 110 110 PRO PRO C . n 
C 3 111 ASP 111 111 111 ASP ASP C . n 
C 3 112 ALA 112 112 112 ALA ALA C . n 
C 3 113 SER 113 113 113 SER SER C . n 
C 3 114 ALA 114 114 114 ALA ALA C . n 
C 3 115 SER 115 115 115 SER SER C . n 
C 3 116 VAL 116 116 116 VAL VAL C . n 
C 3 117 PRO 117 117 117 PRO PRO C . n 
C 3 118 VAL 118 118 118 VAL VAL C . n 
C 3 119 GLU 119 119 119 GLU GLU C . n 
C 3 120 LEU 120 120 120 LEU LEU C . n 
C 3 121 VAL 121 121 121 VAL VAL C . n 
C 3 122 THR 122 122 122 THR THR C . n 
C 3 123 ALA 123 123 123 ALA ALA C . n 
C 3 124 SER 124 124 124 SER SER C . n 
C 3 125 ALA 125 125 125 ALA ALA C . n 
C 3 126 SER 126 126 126 SER SER C . n 
C 3 127 GLY 127 127 127 GLY GLY C . n 
C 3 128 LEU 128 128 128 LEU LEU C . n 
C 3 129 ASP 129 129 129 ASP ASP C . n 
C 3 130 ASN 130 130 130 ASN ASN C . n 
C 3 131 ASN 131 131 131 ASN ASN C . n 
C 3 132 ILE 132 132 132 ILE ILE C . n 
C 3 133 THR 133 133 133 THR THR C . n 
C 3 134 PRO 134 134 134 PRO PRO C . n 
C 3 135 GLN 135 135 135 GLN GLN C . n 
C 3 136 ALA 136 136 136 ALA ALA C . n 
C 3 137 ALA 137 137 137 ALA ALA C . n 
C 3 138 ALA 138 138 138 ALA ALA C . n 
C 3 139 TRP 139 139 139 TRP TRP C . n 
C 3 140 GLN 140 140 140 GLN GLN C . n 
C 3 141 ILE 141 141 141 ILE ILE C . n 
C 3 142 PRO 142 142 142 PRO PRO C . n 
C 3 143 ARG 143 143 143 ARG ARG C . n 
C 3 144 VAL 144 144 144 VAL VAL C . n 
C 3 145 ALA 145 145 145 ALA ALA C . n 
C 3 146 LYS 146 146 146 LYS LYS C . n 
C 3 147 ALA 147 147 147 ALA ALA C . n 
C 3 148 ARG 148 148 148 ARG ARG C . n 
C 3 149 ASN 149 149 149 ASN ASN C . n 
C 3 150 LEU 150 150 150 LEU LEU C . n 
C 3 151 SER 151 151 151 SER SER C . n 
C 3 152 VAL 152 152 152 VAL VAL C . n 
C 3 153 GLU 153 153 153 GLU GLU C . n 
C 3 154 GLN 154 154 154 GLN GLN C . n 
C 3 155 LEU 155 155 155 LEU LEU C . n 
C 3 156 THR 156 156 156 THR THR C . n 
C 3 157 GLN 157 157 157 GLN GLN C . n 
C 3 158 LEU 158 158 158 LEU LEU C . n 
C 3 159 ILE 159 159 159 ILE ILE C . n 
C 3 160 ALA 160 160 160 ALA ALA C . n 
C 3 161 LYS 161 161 161 LYS LYS C . n 
C 3 162 TYR 162 162 162 TYR TYR C . n 
C 3 163 SER 163 163 163 SER SER C . n 
C 3 164 GLN 164 164 164 GLN GLN C . n 
C 3 165 GLN 165 165 165 GLN GLN C . n 
C 3 166 PRO 166 166 166 PRO PRO C . n 
C 3 167 LEU 167 167 167 LEU LEU C . n 
C 3 168 VAL 168 168 168 VAL VAL C . n 
C 3 169 LYS 169 169 169 LYS LYS C . n 
C 3 170 TYR 170 170 170 TYR TYR C . n 
C 3 171 ILE 171 171 171 ILE ILE C . n 
C 3 172 GLY 172 172 172 GLY GLY C . n 
C 3 173 GLN 173 173 173 GLN GLN C . n 
C 3 174 PRO 174 174 174 PRO PRO C . n 
C 3 175 VAL 175 175 175 VAL VAL C . n 
C 3 176 VAL 176 176 176 VAL VAL C . n 
C 3 177 ASN 177 177 177 ASN ASN C . n 
C 3 178 ILE 178 178 178 ILE ILE C . n 
C 3 179 VAL 179 179 179 VAL VAL C . n 
C 3 180 GLU 180 180 180 GLU GLU C . n 
C 3 181 LEU 181 181 181 LEU LEU C . n 
C 3 182 ASN 182 182 182 ASN ASN C . n 
C 3 183 LEU 183 183 183 LEU LEU C . n 
C 3 184 ALA 184 184 184 ALA ALA C . n 
C 3 185 LEU 185 185 185 LEU LEU C . n 
C 3 186 ASP 186 186 186 ASP ASP C . n 
C 3 187 LYS 187 187 187 LYS LYS C . n 
C 3 188 LEU 188 188 188 LEU LEU C . n 
C 3 189 ASP 189 189 189 ASP ASP C . n 
C 3 190 GLU 190 190 190 GLU GLU C . n 
C 3 191 GLY 191 191 ?   ?   ?   C . n 
C 3 192 THR 192 192 ?   ?   ?   C . n 
C 3 193 GLY 193 193 ?   ?   ?   C . n 
C 3 194 LEU 194 194 ?   ?   ?   C . n 
C 3 195 VAL 195 195 ?   ?   ?   C . n 
C 3 196 PRO 196 196 ?   ?   ?   C . n 
C 3 197 ARG 197 197 ?   ?   ?   C . n 
C 3 198 GLY 198 198 ?   ?   ?   C . n 
C 3 199 SER 199 199 ?   ?   ?   C . n 
C 3 200 SER 200 200 ?   ?   ?   C . n 
C 3 201 HIS 201 201 ?   ?   ?   C . n 
C 3 202 HIS 202 202 ?   ?   ?   C . n 
C 3 203 HIS 203 203 ?   ?   ?   C . n 
C 3 204 HIS 204 204 ?   ?   ?   C . n 
C 3 205 HIS 205 205 ?   ?   ?   C . n 
C 3 206 HIS 206 206 ?   ?   ?   C . n 
C 3 207 HIS 207 207 ?   ?   ?   C . n 
C 3 208 HIS 208 208 ?   ?   ?   C . n 
D 4 1   MET 1   1   1   MET MET D . n 
D 4 2   SER 2   2   2   SER SER D . n 
D 4 3   ALA 3   3   3   ALA ALA D . n 
D 4 4   GLY 4   4   4   GLY GLY D . n 
D 4 5   VAL 5   5   5   VAL VAL D . n 
D 4 6   ILE 6   6   6   ILE ILE D . n 
D 4 7   THR 7   7   7   THR THR D . n 
D 4 8   GLY 8   8   8   GLY GLY D . n 
D 4 9   VAL 9   9   9   VAL VAL D . n 
D 4 10  LEU 10  10  10  LEU LEU D . n 
D 4 11  LEU 11  11  11  LEU LEU D . n 
D 4 12  VAL 12  12  12  VAL VAL D . n 
D 4 13  PHE 13  13  13  PHE PHE D . n 
D 4 14  LEU 14  14  14  LEU LEU D . n 
D 4 15  LEU 15  15  15  LEU LEU D . n 
D 4 16  LEU 16  16  16  LEU LEU D . n 
D 4 17  GLY 17  17  17  GLY GLY D . n 
D 4 18  TYR 18  18  18  TYR TYR D . n 
D 4 19  LEU 19  19  19  LEU LEU D . n 
D 4 20  VAL 20  20  20  VAL VAL D . n 
D 4 21  TYR 21  21  21  TYR TYR D . n 
D 4 22  ALA 22  22  22  ALA ALA D . n 
D 4 23  LEU 23  23  23  LEU LEU D . n 
D 4 24  ILE 24  24  24  ILE ILE D . n 
D 4 25  ASN 25  25  25  ASN ASN D . n 
D 4 26  ALA 26  26  26  ALA ALA D . n 
D 4 27  GLU 27  27  27  GLU GLU D . n 
D 4 28  ALA 28  28  28  ALA ALA D . n 
D 4 29  PHE 29  29  29  PHE PHE 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 ADP ? ? ADP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 K   ? ? K   ? ? 'SUBJECT OF INVESTIGATION' ? 
3 MG  ? ? MG  ? ? 'SUBJECT OF INVESTIGATION' ? 
4 PHD ? ? PHD ? ? '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 5 K   1  601 558 K   K   A . 
F 6 9Y0 1  602 683 9Y0 9Y0 A . 
G 6 9Y0 1  701 684 9Y0 9Y0 B . 
H 7 ADP 1  702 685 ADP ADP B . 
I 8 MG  1  703 686 MG  MG  B . 
J 5 K   1  704 687 K   K   B . 
K 8 MG  1  705 688 MG  MG  B . 
L 9 HOH 1  701 582 HOH HOH A . 
L 9 HOH 2  702 597 HOH HOH A . 
L 9 HOH 3  703 565 HOH HOH A . 
L 9 HOH 4  704 568 HOH HOH A . 
L 9 HOH 5  705 591 HOH HOH A . 
L 9 HOH 6  706 573 HOH HOH A . 
L 9 HOH 7  707 574 HOH HOH A . 
L 9 HOH 8  708 567 HOH HOH A . 
L 9 HOH 9  709 569 HOH HOH A . 
L 9 HOH 10 710 585 HOH HOH A . 
L 9 HOH 11 711 612 HOH HOH A . 
L 9 HOH 12 712 579 HOH HOH A . 
L 9 HOH 13 713 560 HOH HOH A . 
L 9 HOH 14 714 603 HOH HOH A . 
L 9 HOH 15 715 578 HOH HOH A . 
L 9 HOH 16 716 586 HOH HOH A . 
L 9 HOH 17 717 581 HOH HOH A . 
L 9 HOH 18 718 570 HOH HOH A . 
L 9 HOH 19 719 608 HOH HOH A . 
L 9 HOH 20 720 593 HOH HOH A . 
L 9 HOH 21 721 562 HOH HOH A . 
L 9 HOH 22 722 600 HOH HOH A . 
L 9 HOH 23 723 583 HOH HOH A . 
L 9 HOH 24 724 584 HOH HOH A . 
L 9 HOH 25 725 589 HOH HOH A . 
L 9 HOH 26 726 618 HOH HOH A . 
L 9 HOH 27 727 594 HOH HOH A . 
L 9 HOH 28 728 606 HOH HOH A . 
L 9 HOH 29 729 559 HOH HOH A . 
L 9 HOH 30 730 572 HOH HOH A . 
L 9 HOH 31 731 564 HOH HOH A . 
L 9 HOH 32 732 575 HOH HOH A . 
L 9 HOH 33 733 571 HOH HOH A . 
L 9 HOH 34 734 596 HOH HOH A . 
L 9 HOH 35 735 561 HOH HOH A . 
L 9 HOH 36 736 604 HOH HOH A . 
L 9 HOH 37 737 595 HOH HOH A . 
L 9 HOH 38 738 587 HOH HOH A . 
L 9 HOH 39 739 563 HOH HOH A . 
L 9 HOH 40 740 566 HOH HOH A . 
L 9 HOH 41 741 590 HOH HOH A . 
L 9 HOH 42 742 576 HOH HOH A . 
L 9 HOH 43 743 599 HOH HOH A . 
L 9 HOH 44 744 601 HOH HOH A . 
L 9 HOH 45 745 611 HOH HOH A . 
L 9 HOH 46 746 577 HOH HOH A . 
L 9 HOH 47 747 613 HOH HOH A . 
L 9 HOH 48 748 609 HOH HOH A . 
L 9 HOH 49 749 592 HOH HOH A . 
L 9 HOH 50 750 610 HOH HOH A . 
L 9 HOH 51 751 598 HOH HOH A . 
L 9 HOH 52 752 602 HOH HOH A . 
L 9 HOH 53 753 607 HOH HOH A . 
L 9 HOH 54 754 614 HOH HOH A . 
L 9 HOH 55 755 605 HOH HOH A . 
L 9 HOH 56 756 615 HOH HOH A . 
L 9 HOH 57 757 617 HOH HOH A . 
L 9 HOH 58 758 621 HOH HOH A . 
L 9 HOH 59 759 619 HOH HOH A . 
M 9 HOH 1  801 711 HOH HOH B . 
M 9 HOH 2  802 700 HOH HOH B . 
M 9 HOH 3  803 697 HOH HOH B . 
M 9 HOH 4  804 699 HOH HOH B . 
M 9 HOH 5  805 692 HOH HOH B . 
M 9 HOH 6  806 689 HOH HOH B . 
M 9 HOH 7  807 704 HOH HOH B . 
M 9 HOH 8  808 698 HOH HOH B . 
M 9 HOH 9  809 693 HOH HOH B . 
M 9 HOH 10 810 702 HOH HOH B . 
M 9 HOH 11 811 695 HOH HOH B . 
M 9 HOH 12 812 691 HOH HOH B . 
M 9 HOH 13 813 712 HOH HOH B . 
M 9 HOH 14 814 701 HOH HOH B . 
M 9 HOH 15 815 696 HOH HOH B . 
M 9 HOH 16 816 694 HOH HOH B . 
M 9 HOH 17 817 690 HOH HOH B . 
M 9 HOH 18 818 710 HOH HOH B . 
M 9 HOH 19 819 706 HOH HOH B . 
M 9 HOH 20 820 707 HOH HOH B . 
M 9 HOH 21 821 620 HOH HOH B . 
M 9 HOH 22 822 708 HOH HOH B . 
M 9 HOH 23 823 703 HOH HOH B . 
M 9 HOH 24 824 709 HOH HOH B . 
M 9 HOH 25 825 705 HOH HOH B . 
M 9 HOH 26 826 616 HOH HOH B . 
N 9 HOH 1  301 588 HOH HOH C . 
N 9 HOH 2  302 193 HOH HOH C . 
N 9 HOH 3  303 192 HOH HOH C . 
N 9 HOH 4  304 580 HOH HOH C . 
N 9 HOH 5  305 191 HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 N 1 B 9Y0 701 ? N  ? G 9Y0 1 N  
2 1 N 1 B 9Y0 701 ? C3 ? G 9Y0 1 C3 
3 1 N 1 B 9Y0 701 ? C4 ? G 9Y0 1 C4 
# 
_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                     9OC4 
_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                         9OC4 
_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                   9OC4 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9OC4 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.10 
_refine.ls_d_res_low                             ? 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
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_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'ELECTRON MICROSCOPY' ? 0.003 ? 9372  ? f_bond_d           ? ? ? 
'ELECTRON MICROSCOPY' ? 0.476 ? 12746 ? f_angle_d          ? ? ? 
'ELECTRON MICROSCOPY' ? 7.027 ? 1349  ? f_dihedral_angle_d ? ? ? 
'ELECTRON MICROSCOPY' ? 0.035 ? 1535  ? f_chiral_restr     ? ? ? 
'ELECTRON MICROSCOPY' ? 0.003 ? 1586  ? f_plane_restr      ? ? ? 
# 
_struct.entry_id                     9OC4 
_struct.title                        'High-resolution cryo-EM structure of KdpFABC in the E1P-ADP state in lipid nanodisc' 
_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        9OC4 
_struct_keywords.text            'P-type ATPase potassium channel transporter pump, TRANSPORT PROTEIN' 
_struct_keywords.pdbx_keywords   'TRANSPORT PROTEIN' 
# 
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 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
G N N 6 ? 
H N N 7 ? 
I N N 8 ? 
J N N 5 ? 
K N N 8 ? 
L N N 9 ? 
M N N 9 ? 
N 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 KDPA_ECOLI P03959 ? 1 
;MAAQGFLLIATFLLVLMVLARPLGSGLARLINDIPLPGTTGVERVLFRALGVSDREMNWKQYLCAILGLNMLGLAVLFFM
LLGQHYLPLNPQQLPGLSWDLALNTAVSFVTNTNWQSYSGETTLSYFSQMAGLTVQNFLSAASGIAVIFALIRAFTRQSM
STLGNAWVDLLRITLWVLVPVALLIALFFIQQGALQNFLPYQAVNTVEGAQQLLPMGPVASQEAIKMLGTNGGGFFNANS
SHPFENPTALTNFVQMLAIFLIPTALCFAFGEVMGDRRQGRMLLWAMSVIFVICVGVVMWAEVQGNPHLLALGTDSSINM
EGKESRFGVLVSSLFAVVTTAASCGAVIAMHDSFTALGGMVPMWLMQIGEVVFGGVGSGLYGMMLFVLLAVFIAGLMIGR
TPEYLGKKIDVREMKLTALAILVTPTLVLMGAALAMMTDAGRSAMLNPGPHGFSEVLYAVSSAANNNGSAFAGLSANSPF
WNCLLAFCMFVGRFGVIIPVMAIAGSLVSKKSQAASSGTLPTHGPLFVGLLIGTVLLVGALTFIPALALGPVAEYLS
;
1 
2 UNP KDPB_ECOLI P03960 ? 2 
;MSRKQLALFEPTLVVQALKEAVKKLNPQAQWRNPVMFIVWIGSLLTTCISIAMASGAMPGNALFSAAISGWLWITVLFAN
FAEALAEGRSKAQANSLKGVKKTAFARKLREPKYGAAADKVPADQLRKGDIVLVEAGDIIPCDGEVIEGGASVDESAITG
ESAPVIRESGGDFASVTGGTRILSDWLVIECSVNPGETFLDRMIAMVEGAQRRKTPNEIALTILLIALTIVFLLATATLW
PFSAWGGNAVSVTVLVALLVCLIPTTIGGLLSAIGVAGMSRMLGANVIATSGRAVEAAGDVDVLLLDKTGTITLGNRQAS
EFIPAQGVDEKTLADAAQLASLADETPEGRSIVILAKQRFNLRERDVQSLHATFVPFTAQSRMSGINIDNRMIRKGSVDA
IRRHVEANGGHFPTDVDQKVDQVARQGATPLVVVEGSRVLGVIALKDIVKGGIKERFAQLRKMGIKTVMITGDNRLTAAA
IAAEAGVDDFLAEATPEAKLALIRQYQAEGRLVAMTGDGTNDAPALAQADVAVAMNSGTQAAKEAGNMVDLDSNPTKLIE
VVHIGKQMLMTRGSLTTFSIANDVAKYFAIIPAAFAATYPQLNALNIMCLHSPDSAILSAVIFNALIIVFLIPLALKGVS
YKPLTASAMLRRNLWIYGLGGLLVPFIGIKVIDLLLTVCGLV
;
1 
3 UNP KDPC_ECOLI P03961 ? 3 
;MSGLRPALSTFIFLLLITGGVYPLLTTVLGQWWFPWQANGSLIREGDTVRGSALIGQNFTGNGYFHGRPSATAEMPYNPQ
ASGGSNLAVSNPELDKLIAARVAALRAANPDASASVPVELVTASASGLDNNITPQAAAWQIPRVAKARNLSVEQLTQLIA
KYSQQPLVKYIGQPVVNIVELNLALDKLDE
;
1 
4 UNP KDPF_ECOLI P36937 ? 4 MSAGVITGVLLVFLLLGYLVYALINAEAF 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 9OC4 A 1 ? 557 ? P03959 1 ? 557 ? 1 557 
2 2 9OC4 B 1 ? 682 ? P03960 1 ? 682 ? 1 682 
3 3 9OC4 C 1 ? 190 ? P03961 1 ? 190 ? 1 190 
4 4 9OC4 D 1 ? 29  ? P36937 1 ? 29  ? 1 29  
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
3 9OC4 GLY C 191 ? UNP P03961 ? ? 'expression tag' 191 1  
3 9OC4 THR C 192 ? UNP P03961 ? ? 'expression tag' 192 2  
3 9OC4 GLY C 193 ? UNP P03961 ? ? 'expression tag' 193 3  
3 9OC4 LEU C 194 ? UNP P03961 ? ? 'expression tag' 194 4  
3 9OC4 VAL C 195 ? UNP P03961 ? ? 'expression tag' 195 5  
3 9OC4 PRO C 196 ? UNP P03961 ? ? 'expression tag' 196 6  
3 9OC4 ARG C 197 ? UNP P03961 ? ? 'expression tag' 197 7  
3 9OC4 GLY C 198 ? UNP P03961 ? ? 'expression tag' 198 8  
3 9OC4 SER C 199 ? UNP P03961 ? ? 'expression tag' 199 9  
3 9OC4 SER C 200 ? UNP P03961 ? ? 'expression tag' 200 10 
3 9OC4 HIS C 201 ? UNP P03961 ? ? 'expression tag' 201 11 
3 9OC4 HIS C 202 ? UNP P03961 ? ? 'expression tag' 202 12 
3 9OC4 HIS C 203 ? UNP P03961 ? ? 'expression tag' 203 13 
3 9OC4 HIS C 204 ? UNP P03961 ? ? 'expression tag' 204 14 
3 9OC4 HIS C 205 ? UNP P03961 ? ? 'expression tag' 205 15 
3 9OC4 HIS C 206 ? UNP P03961 ? ? 'expression tag' 206 16 
3 9OC4 HIS C 207 ? UNP P03961 ? ? 'expression tag' 207 17 
3 9OC4 HIS C 208 ? UNP P03961 ? ? 'expression tag' 208 18 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                'part of a single operon' 
# 
_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   ? 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
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 MET A 1   ? ASN A 32  ? MET A 1   ASN A 32  1 ? 32 
HELX_P HELX_P2  AA2 THR A 39  ? LEU A 50  ? THR A 39  LEU A 50  1 ? 12 
HELX_P HELX_P3  AA3 ASN A 58  ? GLY A 83  ? ASN A 58  GLY A 83  1 ? 26 
HELX_P HELX_P4  AA4 GLN A 84  ? LEU A 87  ? GLN A 84  LEU A 87  5 ? 4  
HELX_P HELX_P5  AA5 SER A 98  ? THR A 111 ? SER A 98  THR A 111 1 ? 14 
HELX_P HELX_P6  AA6 SER A 119 ? LEU A 124 ? SER A 119 LEU A 124 1 ? 6  
HELX_P HELX_P7  AA7 SER A 125 ? GLY A 132 ? SER A 125 GLY A 132 1 ? 8  
HELX_P HELX_P8  AA8 GLY A 132 ? ARG A 157 ? GLY A 132 ARG A 157 1 ? 26 
HELX_P HELX_P9  AA9 ASN A 165 ? VAL A 177 ? ASN A 165 VAL A 177 1 ? 13 
HELX_P HELX_P10 AB1 VAL A 177 ? GLY A 193 ? VAL A 177 GLY A 193 1 ? 17 
HELX_P HELX_P11 AB2 PRO A 218 ? GLY A 229 ? PRO A 218 GLY A 229 1 ? 12 
HELX_P HELX_P12 AB3 ALA A 238 ? HIS A 242 ? ALA A 238 HIS A 242 5 ? 5  
HELX_P HELX_P13 AB4 THR A 248 ? GLY A 275 ? THR A 248 GLY A 275 1 ? 28 
HELX_P HELX_P14 AB5 ASP A 276 ? GLY A 305 ? ASP A 276 GLY A 305 1 ? 30 
HELX_P HELX_P15 AB6 PRO A 307 ? GLY A 313 ? PRO A 307 GLY A 313 1 ? 7  
HELX_P HELX_P16 AB7 PHE A 327 ? ALA A 342 ? PHE A 327 ALA A 342 1 ? 16 
HELX_P HELX_P17 AB8 MET A 350 ? PHE A 354 ? MET A 350 PHE A 354 5 ? 5  
HELX_P HELX_P18 AB9 THR A 355 ? ILE A 368 ? THR A 355 ILE A 368 1 ? 14 
HELX_P HELX_P19 AC1 GLY A 377 ? ILE A 398 ? GLY A 377 ILE A 398 1 ? 22 
HELX_P HELX_P20 AC2 ASP A 410 ? MET A 437 ? ASP A 410 MET A 437 1 ? 28 
HELX_P HELX_P21 AC3 THR A 438 ? ALA A 444 ? THR A 438 ALA A 444 1 ? 7  
HELX_P HELX_P22 AC4 GLY A 449 ? ASN A 465 ? GLY A 449 ASN A 465 1 ? 17 
HELX_P HELX_P23 AC5 SER A 478 ? SER A 509 ? SER A 478 SER A 509 1 ? 32 
HELX_P HELX_P24 AC6 GLY A 524 ? LEU A 549 ? GLY A 524 LEU A 549 1 ? 26 
HELX_P HELX_P25 AC7 GLY A 550 ? SER A 557 ? GLY A 550 SER A 557 1 ? 8  
HELX_P HELX_P26 AC8 GLU B 10  ? LYS B 24  ? GLU B 10  LYS B 24  1 ? 15 
HELX_P HELX_P27 AC9 ASN B 26  ? TRP B 31  ? ASN B 26  TRP B 31  1 ? 6  
HELX_P HELX_P28 AD1 ASN B 33  ? SER B 55  ? ASN B 33  SER B 55  1 ? 23 
HELX_P HELX_P29 AD2 ASN B 61  ? GLY B 99  ? ASN B 61  GLY B 99  1 ? 39 
HELX_P HELX_P30 AD3 PRO B 122 ? LEU B 126 ? PRO B 122 LEU B 126 5 ? 5  
HELX_P HELX_P31 AD4 THR B 198 ? GLU B 208 ? THR B 198 GLU B 208 1 ? 11 
HELX_P HELX_P32 AD5 THR B 215 ? THR B 238 ? THR B 215 THR B 238 1 ? 24 
HELX_P HELX_P33 AD6 THR B 238 ? GLY B 246 ? THR B 238 GLY B 246 1 ? 9  
HELX_P HELX_P34 AD7 SER B 251 ? ILE B 263 ? SER B 251 ILE B 263 1 ? 13 
HELX_P HELX_P35 AD8 PRO B 264 ? ALA B 285 ? PRO B 264 ALA B 285 1 ? 22 
HELX_P HELX_P36 AD9 SER B 291 ? ALA B 298 ? SER B 291 ALA B 298 1 ? 8  
HELX_P HELX_P37 AE1 ASP B 329 ? SER B 341 ? ASP B 329 SER B 341 1 ? 13 
HELX_P HELX_P38 AE2 THR B 346 ? PHE B 360 ? THR B 346 PHE B 360 1 ? 15 
HELX_P HELX_P39 AE3 ASP B 366 ? HIS B 371 ? ASP B 366 HIS B 371 1 ? 6  
HELX_P HELX_P40 AE4 SER B 397 ? GLY B 409 ? SER B 397 GLY B 409 1 ? 13 
HELX_P HELX_P41 AE5 PRO B 413 ? GLY B 427 ? PRO B 413 GLY B 427 1 ? 15 
HELX_P HELX_P42 AE6 GLY B 452 ? MET B 463 ? GLY B 452 MET B 463 1 ? 12 
HELX_P HELX_P43 AE7 ASN B 474 ? GLY B 486 ? ASN B 474 GLY B 486 1 ? 13 
HELX_P HELX_P44 AE8 THR B 495 ? GLU B 509 ? THR B 495 GLU B 509 1 ? 15 
HELX_P HELX_P45 AE9 GLY B 519 ? ASN B 521 ? GLY B 519 ASN B 521 5 ? 3  
HELX_P HELX_P46 AF1 ASP B 522 ? ALA B 527 ? ASP B 522 ALA B 527 1 ? 6  
HELX_P HELX_P47 AF2 THR B 539 ? GLY B 546 ? THR B 539 GLY B 546 1 ? 8  
HELX_P HELX_P48 AF3 LYS B 557 ? ASN B 582 ? LYS B 557 ASN B 582 1 ? 26 
HELX_P HELX_P49 AF4 ASN B 582 ? PHE B 595 ? ASN B 582 PHE B 595 1 ? 14 
HELX_P HELX_P50 AF5 TYR B 599 ? ASN B 606 ? TYR B 599 ASN B 606 5 ? 8  
HELX_P HELX_P51 AF6 SER B 612 ? LEU B 631 ? SER B 612 LEU B 631 1 ? 20 
HELX_P HELX_P52 AF7 LEU B 631 ? GLY B 638 ? LEU B 631 GLY B 638 1 ? 8  
HELX_P HELX_P53 AF8 THR B 645 ? TYR B 657 ? THR B 645 TYR B 657 1 ? 13 
HELX_P HELX_P54 AF9 TYR B 657 ? CYS B 679 ? TYR B 657 CYS B 679 1 ? 23 
HELX_P HELX_P55 AG1 LEU C 4   ? VAL C 21  ? LEU C 4   VAL C 21  1 ? 18 
HELX_P HELX_P56 AG2 VAL C 21  ? PHE C 34  ? VAL C 21  PHE C 34  1 ? 14 
HELX_P HELX_P57 AG3 PHE C 34  ? ASN C 39  ? PHE C 34  ASN C 39  1 ? 6  
HELX_P HELX_P58 AG4 ASN C 91  ? ASN C 109 ? ASN C 91  ASN C 109 1 ? 19 
HELX_P HELX_P59 AG5 PRO C 117 ? THR C 122 ? PRO C 117 THR C 122 5 ? 6  
HELX_P HELX_P60 AG6 THR C 133 ? GLN C 140 ? THR C 133 GLN C 140 1 ? 8  
HELX_P HELX_P61 AG7 GLN C 140 ? ASN C 149 ? GLN C 140 ASN C 149 1 ? 10 
HELX_P HELX_P62 AG8 SER C 151 ? TYR C 162 ? SER C 151 TYR C 162 1 ? 12 
HELX_P HELX_P63 AG9 ILE C 178 ? GLU C 190 ? ILE C 178 GLU C 190 1 ? 13 
HELX_P HELX_P64 AH1 SER D 2   ? ASN D 25  ? SER D 2   ASN D 25  1 ? 24 
# 
_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 ?    ? B CYS 142 SG  ? ? ? 1_555 B CYS 191 SG ? ? B CYS 142 B CYS 191 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
covale1  covale both ? B LEU 306 C   ? ? ? 1_555 B PHD 307 N  ? ? B LEU 306 B PHD 307 1_555 ? ? ? ? ? ? ? 1.329 ? ? 
covale2  covale both ? B PHD 307 C   ? ? ? 1_555 B LYS 308 N  ? ? B PHD 307 B LYS 308 1_555 ? ? ? ? ? ? ? 1.329 ? ? 
metalc1  metalc ?    ? A ASN 112 O   ? ? ? 1_555 E K   .   K  ? ? A ASN 112 A K   601 1_555 ? ? ? ? ? ? ? 2.690 ? ? 
metalc2  metalc ?    ? A THR 113 O   ? ? ? 1_555 E K   .   K  ? ? A THR 113 A K   601 1_555 ? ? ? ? ? ? ? 2.919 ? ? 
metalc3  metalc ?    ? A THR 230 O   ? ? ? 1_555 E K   .   K  ? ? A THR 230 A K   601 1_555 ? ? ? ? ? ? ? 2.971 ? ? 
metalc4  metalc ?    ? A ASN 231 O   ? ? ? 1_555 E K   .   K  ? ? A ASN 231 A K   601 1_555 ? ? ? ? ? ? ? 2.701 ? ? 
metalc5  metalc ?    ? A SER 343 O   ? ? ? 1_555 E K   .   K  ? ? A SER 343 A K   601 1_555 ? ? ? ? ? ? ? 2.596 ? ? 
metalc6  metalc ?    ? A CYS 344 O   ? ? ? 1_555 E K   .   K  ? ? A CYS 344 A K   601 1_555 ? ? ? ? ? ? ? 2.842 ? ? 
metalc7  metalc ?    ? A ASN 466 O   ? ? ? 1_555 E K   .   K  ? ? A ASN 466 A K   601 1_555 ? ? ? ? ? ? ? 3.282 ? ? 
metalc8  metalc ?    ? A ASN 467 O   ? ? ? 1_555 E K   .   K  ? ? A ASN 467 A K   601 1_555 ? ? ? ? ? ? ? 2.780 ? ? 
metalc9  metalc ?    ? E K   .   K   ? ? ? 1_555 L HOH .   O  ? ? A K   601 A HOH 713 1_555 ? ? ? ? ? ? ? 3.410 ? ? 
metalc10 metalc ?    ? B VAL 260 O   ? ? ? 1_555 J K   .   K  ? ? B VAL 260 B K   704 1_555 ? ? ? ? ? ? ? 2.994 ? ? 
metalc11 metalc ?    ? B CYS 261 O   ? ? ? 1_555 J K   .   K  ? ? B CYS 261 B K   704 1_555 ? ? ? ? ? ? ? 2.781 ? ? 
metalc12 metalc ?    ? B ILE 263 O   ? ? ? 1_555 J K   .   K  ? ? B ILE 263 B K   704 1_555 ? ? ? ? ? ? ? 2.615 ? ? 
metalc13 metalc ?    ? B THR 265 OG1 ? ? ? 1_555 J K   .   K  ? ? B THR 265 B K   704 1_555 ? ? ? ? ? ? ? 2.895 ? ? 
metalc14 metalc ?    ? B PHD 307 OD2 ? ? ? 1_555 I MG  .   MG ? ? B PHD 307 B MG  703 1_555 ? ? ? ? ? ? ? 2.729 ? ? 
metalc15 metalc ?    ? B ASN 624 OD1 ? ? ? 1_555 J K   .   K  ? ? B ASN 624 B K   704 1_555 ? ? ? ? ? ? ? 2.644 ? ? 
metalc16 metalc ?    ? H ADP .   O1B ? ? ? 1_555 I MG  .   MG ? ? B ADP 702 B MG  703 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
metalc17 metalc ?    ? H ADP .   O2B ? ? ? 1_555 K MG  .   MG ? ? B ADP 702 B MG  705 1_555 ? ? ? ? ? ? ? 2.661 ? ? 
metalc18 metalc ?    ? H ADP .   O2A ? ? ? 1_555 K MG  .   MG ? ? B ADP 702 B MG  705 1_555 ? ? ? ? ? ? ? 2.191 ? ? 
metalc19 metalc ?    ? J K   .   K   ? ? ? 1_555 M HOH .   O  ? ? B K   704 B HOH 810 1_555 ? ? ? ? ? ? ? 3.186 ? ? 
metalc20 metalc ?    ? J K   .   K   ? ? ? 1_555 M HOH .   O  ? ? B K   704 B HOH 817 1_555 ? ? ? ? ? ? ? 2.970 ? ? 
# 
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  O   ? A ASN 112 ? A ASN 112 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? A THR 113 ? A THR 113 ? 1_555 89.7  ? 
2  O   ? A ASN 112 ? A ASN 112 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? A THR 230 ? A THR 230 ? 1_555 87.7  ? 
3  O   ? A THR 113 ? A THR 113 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? A THR 230 ? A THR 230 ? 1_555 148.5 ? 
4  O   ? A ASN 112 ? A ASN 112 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? A ASN 231 ? A ASN 231 ? 1_555 111.9 ? 
5  O   ? A THR 113 ? A THR 113 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? A ASN 231 ? A ASN 231 ? 1_555 72.4  ? 
6  O   ? A THR 230 ? A THR 230 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? A ASN 231 ? A ASN 231 ? 1_555 79.5  ? 
7  O   ? A ASN 112 ? A ASN 112 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? A SER 343 ? A SER 343 ? 1_555 106.6 ? 
8  O   ? A THR 113 ? A THR 113 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? A SER 343 ? A SER 343 ? 1_555 145.7 ? 
9  O   ? A THR 230 ? A THR 230 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? A SER 343 ? A SER 343 ? 1_555 64.1  ? 
10 O   ? A ASN 231 ? A ASN 231 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? A SER 343 ? A SER 343 ? 1_555 124.9 ? 
11 O   ? A ASN 112 ? A ASN 112 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? A CYS 344 ? A CYS 344 ? 1_555 167.3 ? 
12 O   ? A THR 113 ? A THR 113 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? A CYS 344 ? A CYS 344 ? 1_555 96.1  ? 
13 O   ? A THR 230 ? A THR 230 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? A CYS 344 ? A CYS 344 ? 1_555 81.4  ? 
14 O   ? A ASN 231 ? A ASN 231 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? A CYS 344 ? A CYS 344 ? 1_555 59.7  ? 
15 O   ? A SER 343 ? A SER 343 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? A CYS 344 ? A CYS 344 ? 1_555 74.5  ? 
16 O   ? A ASN 112 ? A ASN 112 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? A ASN 466 ? A ASN 466 ? 1_555 65.5  ? 
17 O   ? A THR 113 ? A THR 113 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? A ASN 466 ? A ASN 466 ? 1_555 92.0  ? 
18 O   ? A THR 230 ? A THR 230 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? A ASN 466 ? A ASN 466 ? 1_555 115.2 ? 
19 O   ? A ASN 231 ? A ASN 231 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? A ASN 466 ? A ASN 466 ? 1_555 164.3 ? 
20 O   ? A SER 343 ? A SER 343 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? A ASN 466 ? A ASN 466 ? 1_555 69.2  ? 
21 O   ? A CYS 344 ? A CYS 344 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? A ASN 466 ? A ASN 466 ? 1_555 125.3 ? 
22 O   ? A ASN 112 ? A ASN 112 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? A ASN 467 ? A ASN 467 ? 1_555 131.9 ? 
23 O   ? A THR 113 ? A THR 113 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? A ASN 467 ? A ASN 467 ? 1_555 67.0  ? 
24 O   ? A THR 230 ? A THR 230 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? A ASN 467 ? A ASN 467 ? 1_555 133.8 ? 
25 O   ? A ASN 231 ? A ASN 231 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? A ASN 467 ? A ASN 467 ? 1_555 100.6 ? 
26 O   ? A SER 343 ? A SER 343 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? A ASN 467 ? A ASN 467 ? 1_555 79.9  ? 
27 O   ? A CYS 344 ? A CYS 344 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? A ASN 467 ? A ASN 467 ? 1_555 60.8  ? 
28 O   ? A ASN 466 ? A ASN 466 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? A ASN 467 ? A ASN 467 ? 1_555 73.5  ? 
29 O   ? A ASN 112 ? A ASN 112 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? L HOH .   ? A HOH 713 ? 1_555 48.8  ? 
30 O   ? A THR 113 ? A THR 113 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? L HOH .   ? A HOH 713 ? 1_555 132.3 ? 
31 O   ? A THR 230 ? A THR 230 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? L HOH .   ? A HOH 713 ? 1_555 64.4  ? 
32 O   ? A ASN 231 ? A ASN 231 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? L HOH .   ? A HOH 713 ? 1_555 137.8 ? 
33 O   ? A SER 343 ? A SER 343 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? L HOH .   ? A HOH 713 ? 1_555 58.0  ? 
34 O   ? A CYS 344 ? A CYS 344 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? L HOH .   ? A HOH 713 ? 1_555 129.6 ? 
35 O   ? A ASN 466 ? A ASN 466 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? L HOH .   ? A HOH 713 ? 1_555 53.3  ? 
36 O   ? A ASN 467 ? A ASN 467 ? 1_555 K  ? E K  . ? A K  601 ? 1_555 O   ? L HOH .   ? A HOH 713 ? 1_555 119.9 ? 
37 O   ? B VAL 260 ? B VAL 260 ? 1_555 K  ? J K  . ? B K  704 ? 1_555 O   ? B CYS 261 ? B CYS 261 ? 1_555 80.3  ? 
38 O   ? B VAL 260 ? B VAL 260 ? 1_555 K  ? J K  . ? B K  704 ? 1_555 O   ? B ILE 263 ? B ILE 263 ? 1_555 75.5  ? 
39 O   ? B CYS 261 ? B CYS 261 ? 1_555 K  ? J K  . ? B K  704 ? 1_555 O   ? B ILE 263 ? B ILE 263 ? 1_555 105.7 ? 
40 O   ? B VAL 260 ? B VAL 260 ? 1_555 K  ? J K  . ? B K  704 ? 1_555 OG1 ? B THR 265 ? B THR 265 ? 1_555 81.2  ? 
41 O   ? B CYS 261 ? B CYS 261 ? 1_555 K  ? J K  . ? B K  704 ? 1_555 OG1 ? B THR 265 ? B THR 265 ? 1_555 156.7 ? 
42 O   ? B ILE 263 ? B ILE 263 ? 1_555 K  ? J K  . ? B K  704 ? 1_555 OG1 ? B THR 265 ? B THR 265 ? 1_555 83.2  ? 
43 O   ? B VAL 260 ? B VAL 260 ? 1_555 K  ? J K  . ? B K  704 ? 1_555 OD1 ? B ASN 624 ? B ASN 624 ? 1_555 81.8  ? 
44 O   ? B CYS 261 ? B CYS 261 ? 1_555 K  ? J K  . ? B K  704 ? 1_555 OD1 ? B ASN 624 ? B ASN 624 ? 1_555 93.1  ? 
45 O   ? B ILE 263 ? B ILE 263 ? 1_555 K  ? J K  . ? B K  704 ? 1_555 OD1 ? B ASN 624 ? B ASN 624 ? 1_555 147.4 ? 
46 OG1 ? B THR 265 ? B THR 265 ? 1_555 K  ? J K  . ? B K  704 ? 1_555 OD1 ? B ASN 624 ? B ASN 624 ? 1_555 70.2  ? 
47 O   ? B VAL 260 ? B VAL 260 ? 1_555 K  ? J K  . ? B K  704 ? 1_555 O   ? M HOH .   ? B HOH 810 ? 1_555 135.3 ? 
48 O   ? B CYS 261 ? B CYS 261 ? 1_555 K  ? J K  . ? B K  704 ? 1_555 O   ? M HOH .   ? B HOH 810 ? 1_555 56.5  ? 
49 O   ? B ILE 263 ? B ILE 263 ? 1_555 K  ? J K  . ? B K  704 ? 1_555 O   ? M HOH .   ? B HOH 810 ? 1_555 123.6 ? 
50 OG1 ? B THR 265 ? B THR 265 ? 1_555 K  ? J K  . ? B K  704 ? 1_555 O   ? M HOH .   ? B HOH 810 ? 1_555 135.9 ? 
51 OD1 ? B ASN 624 ? B ASN 624 ? 1_555 K  ? J K  . ? B K  704 ? 1_555 O   ? M HOH .   ? B HOH 810 ? 1_555 89.0  ? 
52 O   ? B VAL 260 ? B VAL 260 ? 1_555 K  ? J K  . ? B K  704 ? 1_555 O   ? M HOH .   ? B HOH 817 ? 1_555 152.0 ? 
53 O   ? B CYS 261 ? B CYS 261 ? 1_555 K  ? J K  . ? B K  704 ? 1_555 O   ? M HOH .   ? B HOH 817 ? 1_555 124.2 ? 
54 O   ? B ILE 263 ? B ILE 263 ? 1_555 K  ? J K  . ? B K  704 ? 1_555 O   ? M HOH .   ? B HOH 817 ? 1_555 83.9  ? 
55 OG1 ? B THR 265 ? B THR 265 ? 1_555 K  ? J K  . ? B K  704 ? 1_555 O   ? M HOH .   ? B HOH 817 ? 1_555 77.6  ? 
56 OD1 ? B ASN 624 ? B ASN 624 ? 1_555 K  ? J K  . ? B K  704 ? 1_555 O   ? M HOH .   ? B HOH 817 ? 1_555 107.6 ? 
57 O   ? M HOH .   ? B HOH 810 ? 1_555 K  ? J K  . ? B K  704 ? 1_555 O   ? M HOH .   ? B HOH 817 ? 1_555 72.3  ? 
58 OD2 ? B PHD 307 ? B PHD 307 ? 1_555 MG ? I MG . ? B MG 703 ? 1_555 O1B ? H ADP .   ? B ADP 702 ? 1_555 112.3 ? 
59 O2B ? H ADP .   ? B ADP 702 ? 1_555 MG ? K MG . ? B MG 705 ? 1_555 O2A ? H ADP .   ? B ADP 702 ? 1_555 69.9  ? 
# 
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 PHD B 307 ? .   . .   . PHD B 307 ? 1_555 .   . .   . .     .  .  ASP 1 PHD Phosphorylation 'Named protein modification' 
2 CYS B 142 ? CYS B 191 ? CYS B 142 ? 1_555 CYS B 191 ? 1_555 SG SG .   . .   None            'Disulfide bridge'           
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 6 ? 
AA4 ? 3 ? 
AA5 ? 7 ? 
AA6 ? 3 ? 
AA7 ? 6 ? 
AA8 ? 2 ? 
AA9 ? 3 ? 
# 
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 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA5 4 5 ? parallel      
AA5 5 6 ? parallel      
AA5 6 7 ? parallel      
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA7 5 6 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? 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 GLN A 202 ? ASN A 205 ? GLN A 202 ASN A 205 
AA1 2 GLN A 211 ? LEU A 214 ? GLN A 211 LEU A 214 
AA2 1 GLU A 403 ? TYR A 404 ? GLU A 403 TYR A 404 
AA2 2 LYS A 407 ? LYS A 408 ? LYS A 407 LYS A 408 
AA3 1 ALA B 118 ? VAL B 121 ? ALA B 118 VAL B 121 
AA3 2 ALA B 106 ? LEU B 109 ? ALA B 106 LEU B 109 
AA3 3 ILE B 131 ? GLU B 135 ? ILE B 131 GLU B 135 
AA3 4 TRP B 186 ? CYS B 191 ? TRP B 186 CYS B 191 
AA3 5 GLY B 144 ? GLU B 148 ? GLY B 144 GLU B 148 
AA3 6 SER B 175 ? VAL B 176 ? SER B 175 VAL B 176 
AA4 1 VAL B 165 ? GLU B 168 ? VAL B 165 GLU B 168 
AA4 2 GLY B 150 ? ASP B 154 ? GLY B 150 ASP B 154 
AA4 3 ARG B 181 ? ILE B 182 ? ARG B 181 ILE B 182 
AA5 1 VAL B 287 ? ALA B 289 ? VAL B 287 ALA B 289 
AA5 2 MET B 548 ? ASP B 550 ? MET B 548 ASP B 550 
AA5 3 VAL B 531 ? MET B 535 ? VAL B 531 MET B 535 
AA5 4 LEU B 512 ? GLY B 517 ? LEU B 512 GLY B 517 
AA5 5 VAL B 301 ? PHD B 307 ? VAL B 301 PHD B 307 
AA5 6 LYS B 466 ? ILE B 470 ? LYS B 466 ILE B 470 
AA5 7 ASP B 489 ? LEU B 491 ? ASP B 489 LEU B 491 
AA6 1 GLN B 318 ? ALA B 319 ? GLN B 318 ALA B 319 
AA6 2 ARG B 438 ? LYS B 446 ? ARG B 438 LYS B 446 
AA6 3 ILE B 323 ? PRO B 324 ? ILE B 323 PRO B 324 
AA7 1 GLN B 318 ? ALA B 319 ? GLN B 318 ALA B 319 
AA7 2 ARG B 438 ? LYS B 446 ? ARG B 438 LYS B 446 
AA7 3 THR B 429 ? GLU B 435 ? THR B 429 GLU B 435 
AA7 4 ILE B 393 ? GLY B 396 ? ILE B 393 GLY B 396 
AA7 5 MET B 383 ? ASN B 387 ? MET B 383 ASN B 387 
AA7 6 THR B 373 ? VAL B 375 ? THR B 373 VAL B 375 
AA8 1 LEU C 42  ? GLU C 45  ? LEU C 42  GLU C 45  
AA8 2 THR C 48  ? SER C 52  ? THR C 48  SER C 52  
AA9 1 ASN C 131 ? ILE C 132 ? ASN C 131 ILE C 132 
AA9 2 VAL C 175 ? ASN C 177 ? VAL C 175 ASN C 177 
AA9 3 SER C 163 ? GLN C 164 ? SER C 163 GLN C 164 
# 
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 GLN A 202 ? N GLN A 202 O LEU A 214 ? O LEU A 214 
AA2 1 2 N TYR A 404 ? N TYR A 404 O LYS A 407 ? O LYS A 407 
AA3 1 2 O VAL B 121 ? O VAL B 121 N ALA B 106 ? N ALA B 106 
AA3 2 3 N ARG B 107 ? N ARG B 107 O LEU B 133 ? O LEU B 133 
AA3 3 4 N VAL B 132 ? N VAL B 132 O ILE B 189 ? O ILE B 189 
AA3 4 5 O VAL B 188 ? O VAL B 188 N ILE B 147 ? N ILE B 147 
AA3 5 6 N GLY B 144 ? N GLY B 144 O VAL B 176 ? O VAL B 176 
AA4 1 2 O VAL B 165 ? O VAL B 165 N VAL B 153 ? N VAL B 153 
AA4 2 3 N ASP B 154 ? N ASP B 154 O ARG B 181 ? O ARG B 181 
AA5 1 2 N ILE B 288 ? N ILE B 288 O VAL B 549 ? O VAL B 549 
AA5 2 3 O MET B 548 ? O MET B 548 N ALA B 532 ? N ALA B 532 
AA5 3 4 O VAL B 531 ? O VAL B 531 N MET B 515 ? N MET B 515 
AA5 4 5 O ALA B 514 ? O ALA B 514 N LEU B 305 ? N LEU B 305 
AA5 5 6 N LEU B 304 ? N LEU B 304 O LYS B 466 ? O LYS B 466 
AA5 6 7 N MET B 469 ? N MET B 469 O LEU B 491 ? O LEU B 491 
AA6 1 2 N GLN B 318 ? N GLN B 318 O LYS B 446 ? O LYS B 446 
AA6 2 3 O VAL B 442 ? O VAL B 442 N ILE B 323 ? N ILE B 323 
AA7 1 2 N GLN B 318 ? N GLN B 318 O LYS B 446 ? O LYS B 446 
AA7 2 3 O ARG B 438 ? O ARG B 438 N GLU B 435 ? N GLU B 435 
AA7 3 4 O VAL B 434 ? O VAL B 434 N ARG B 394 ? N ARG B 394 
AA7 4 5 O LYS B 395 ? O LYS B 395 N SER B 384 ? N SER B 384 
AA7 5 6 O GLY B 385 ? O GLY B 385 N VAL B 375 ? N VAL B 375 
AA8 1 2 N ILE C 43  ? N ILE C 43  O GLY C 51  ? O GLY C 51  
AA9 1 2 N ILE C 132 ? N ILE C 132 O VAL C 176 ? O VAL C 176 
AA9 2 3 O VAL C 175 ? O VAL C 175 N GLN C 164 ? N GLN C 164 
# 
_pdbx_entry_details.entry_id                   9OC4 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   NH1 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   ARG 
_pdbx_validate_close_contact.auth_seq_id_1    3 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   OD2 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   ASP 
_pdbx_validate_close_contact.auth_seq_id_2    552 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.06 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CG 
_pdbx_validate_rmsd_bond.auth_asym_id_1            B 
_pdbx_validate_rmsd_bond.auth_comp_id_1            PRO 
_pdbx_validate_rmsd_bond.auth_seq_id_1             524 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            CD 
_pdbx_validate_rmsd_bond.auth_asym_id_2            B 
_pdbx_validate_rmsd_bond.auth_comp_id_2            PRO 
_pdbx_validate_rmsd_bond.auth_seq_id_2             524 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.294 
_pdbx_validate_rmsd_bond.bond_target_value         1.502 
_pdbx_validate_rmsd_bond.bond_deviation            -0.208 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.033 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             N 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_1              524 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CD 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_2              524 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_3              524 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                88.47 
_pdbx_validate_rmsd_angle.angle_target_value         103.20 
_pdbx_validate_rmsd_angle.angle_deviation            -14.73 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.50 
_pdbx_validate_rmsd_angle.linker_flag                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 VAL A 177 ? ? -122.47 -59.78  
2  1 ASN A 239 ? ? 61.90   -135.86 
3  1 SER A 343 ? ? -97.97  32.01   
4  1 PHE A 373 ? ? 72.18   -14.02  
5  1 ARG B 3   ? ? 83.43   -1.06   
6  1 LEU B 6   ? ? -92.93  -66.33  
7  1 ALA B 7   ? ? -176.10 -177.37 
8  1 SER B 184 ? ? -109.33 -62.75  
9  1 ASP B 185 ? ? -120.23 -67.12  
10 1 TRP B 186 ? ? 177.18  160.80  
11 1 LYS B 308 ? ? -85.91  -74.96  
12 1 THR B 311 ? ? -101.74 -66.26  
13 1 ASN B 390 ? ? 62.77   -68.76  
14 1 ALA C 71  ? ? -97.68  56.56   
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    B 
_pdbx_validate_planes.auth_seq_id     3 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.101 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_pdbx_struct_mod_residue.id               1 
_pdbx_struct_mod_residue.label_asym_id    B 
_pdbx_struct_mod_residue.label_comp_id    PHD 
_pdbx_struct_mod_residue.label_seq_id     307 
_pdbx_struct_mod_residue.auth_asym_id     B 
_pdbx_struct_mod_residue.auth_comp_id     PHD 
_pdbx_struct_mod_residue.auth_seq_id      307 
_pdbx_struct_mod_residue.PDB_ins_code     ? 
_pdbx_struct_mod_residue.parent_comp_id   ASP 
_pdbx_struct_mod_residue.details          'modified residue' 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9OC4 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   cross-correlation 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   59.2 
_em_3d_fitting.ref_space         REAL 
_em_3d_fitting.ref_protocol      'FLEXIBLE FIT' 
# 
_em_3d_fitting_list.id                            1 
_em_3d_fitting_list.3d_fitting_id                 1 
_em_3d_fitting_list.pdb_entry_id                  7LC3 
_em_3d_fitting_list.pdb_chain_id                  ? 
_em_3d_fitting_list.pdb_chain_residue_range       ? 
_em_3d_fitting_list.details                       ? 
_em_3d_fitting_list.chain_id                      ? 
_em_3d_fitting_list.chain_residue_range           ? 
_em_3d_fitting_list.source_name                   PDB 
_em_3d_fitting_list.type                          'experimental model' 
_em_3d_fitting_list.accession_code                7LC3 
_em_3d_fitting_list.initial_refinement_model_id   1 
# 
_em_3d_reconstruction.entry_id                    9OC4 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   'FOURIER SPACE' 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  2.1 
_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               672405 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          1 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       '20 mM Tris pH 7.4, 100 mM KCl, and 0.5 mM TCEP' 
_em_buffer.pH            7.4 
# 
_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                 'KdpFABC complex in the E1P-ADP state in lipid nanodisc' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1,2,3,4 
# 
_em_imaging.entry_id                        9OC4 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      2.7 
_em_imaging.nominal_defocus_min             700 
_em_imaging.nominal_defocus_max             2200 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           130000 
_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             'COMA FREE' 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         NITROGEN 
_em_imaging.objective_aperture              ? 
_em_imaging.microscope_serial_number        ? 
_em_imaging.microscope_version              ? 
# 
_em_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    COPPER 
_em_sample_support.grid_mesh_size   400 
_em_sample_support.grid_type        C-flat-1.2/1.3 
_em_sample_support.details          EasyGlow 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              9OC4 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              100 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   277 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9OC4 
_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              9OC4 
_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 B MET 1   ? B MET 1   
2  1 Y 1 C MET 1   ? C MET 1   
3  1 Y 1 C SER 2   ? C SER 2   
4  1 Y 1 C GLY 191 ? C GLY 191 
5  1 Y 1 C THR 192 ? C THR 192 
6  1 Y 1 C GLY 193 ? C GLY 193 
7  1 Y 1 C LEU 194 ? C LEU 194 
8  1 Y 1 C VAL 195 ? C VAL 195 
9  1 Y 1 C PRO 196 ? C PRO 196 
10 1 Y 1 C ARG 197 ? C ARG 197 
11 1 Y 1 C GLY 198 ? C GLY 198 
12 1 Y 1 C SER 199 ? C SER 199 
13 1 Y 1 C SER 200 ? C SER 200 
14 1 Y 1 C HIS 201 ? C HIS 201 
15 1 Y 1 C HIS 202 ? C HIS 202 
16 1 Y 1 C HIS 203 ? C HIS 203 
17 1 Y 1 C HIS 204 ? C HIS 204 
18 1 Y 1 C HIS 205 ? C HIS 205 
19 1 Y 1 C HIS 206 ? C HIS 206 
20 1 Y 1 C HIS 207 ? C HIS 207 
21 1 Y 1 C HIS 208 ? C HIS 208 
# 
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 
9Y0 N      N  N N 1   
9Y0 C      C  N N 2   
9Y0 O      O  N N 3   
9Y0 C1     C  N R 4   
9Y0 C10    C  N N 5   
9Y0 C11    C  N N 6   
9Y0 C12    C  N N 7   
9Y0 C13    C  N N 8   
9Y0 C14    C  N N 9   
9Y0 C15    C  N N 10  
9Y0 C16    C  N N 11  
9Y0 C17    C  N N 12  
9Y0 C18    C  N N 13  
9Y0 C19    C  N N 14  
9Y0 C2     C  N N 15  
9Y0 C20    C  N N 16  
9Y0 C21    C  N N 17  
9Y0 C22    C  N N 18  
9Y0 C23    C  N N 19  
9Y0 C24    C  N N 20  
9Y0 C25    C  N N 21  
9Y0 C26    C  N N 22  
9Y0 C27    C  N N 23  
9Y0 C28    C  N N 24  
9Y0 C29    C  N N 25  
9Y0 C3     C  N N 26  
9Y0 C30    C  N N 27  
9Y0 C31    C  N N 28  
9Y0 C32    C  N N 29  
9Y0 C33    C  N N 30  
9Y0 C34    C  N N 31  
9Y0 C35    C  N N 32  
9Y0 C36    C  N N 33  
9Y0 C37    C  N N 34  
9Y0 C38    C  N N 35  
9Y0 C4     C  N N 36  
9Y0 C5     C  N N 37  
9Y0 C6     C  N N 38  
9Y0 C7     C  N N 39  
9Y0 C8     C  N N 40  
9Y0 C9     C  N N 41  
9Y0 O1     O  N N 42  
9Y0 O2     O  N N 43  
9Y0 O3     O  N N 44  
9Y0 O4     O  N N 45  
9Y0 O5     O  N N 46  
9Y0 O6     O  N N 47  
9Y0 O7     O  N N 48  
9Y0 P      P  N N 49  
9Y0 H1     H  N N 50  
9Y0 H2     H  N N 51  
9Y0 H4     H  N N 52  
9Y0 H5     H  N N 53  
9Y0 H6     H  N N 54  
9Y0 H7     H  N N 55  
9Y0 H8     H  N N 56  
9Y0 H9     H  N N 57  
9Y0 H10    H  N N 58  
9Y0 H11    H  N N 59  
9Y0 H12    H  N N 60  
9Y0 H13    H  N N 61  
9Y0 H14    H  N N 62  
9Y0 H15    H  N N 63  
9Y0 H16    H  N N 64  
9Y0 H17    H  N N 65  
9Y0 H18    H  N N 66  
9Y0 H19    H  N N 67  
9Y0 H20    H  N N 68  
9Y0 H21    H  N N 69  
9Y0 H22    H  N N 70  
9Y0 H23    H  N N 71  
9Y0 H24    H  N N 72  
9Y0 H25    H  N N 73  
9Y0 H26    H  N N 74  
9Y0 H27    H  N N 75  
9Y0 H28    H  N N 76  
9Y0 H29    H  N N 77  
9Y0 H30    H  N N 78  
9Y0 H31    H  N N 79  
9Y0 H32    H  N N 80  
9Y0 H33    H  N N 81  
9Y0 H34    H  N N 82  
9Y0 H35    H  N N 83  
9Y0 H36    H  N N 84  
9Y0 H37    H  N N 85  
9Y0 H38    H  N N 86  
9Y0 H39    H  N N 87  
9Y0 H40    H  N N 88  
9Y0 H41    H  N N 89  
9Y0 H42    H  N N 90  
9Y0 H43    H  N N 91  
9Y0 H44    H  N N 92  
9Y0 H45    H  N N 93  
9Y0 H46    H  N N 94  
9Y0 H47    H  N N 95  
9Y0 H48    H  N N 96  
9Y0 H49    H  N N 97  
9Y0 H50    H  N N 98  
9Y0 H51    H  N N 99  
9Y0 H52    H  N N 100 
9Y0 H53    H  N N 101 
9Y0 H54    H  N N 102 
9Y0 H55    H  N N 103 
9Y0 H56    H  N N 104 
9Y0 H57    H  N N 105 
9Y0 H58    H  N N 106 
9Y0 H59    H  N N 107 
9Y0 H60    H  N N 108 
9Y0 H61    H  N N 109 
9Y0 H62    H  N N 110 
9Y0 H63    H  N N 111 
9Y0 H64    H  N N 112 
9Y0 H65    H  N N 113 
9Y0 H66    H  N N 114 
9Y0 H67    H  N N 115 
9Y0 H68    H  N N 116 
9Y0 H69    H  N N 117 
9Y0 H70    H  N N 118 
9Y0 H71    H  N N 119 
9Y0 H72    H  N N 120 
9Y0 H73    H  N N 121 
9Y0 H74    H  N N 122 
9Y0 H75    H  N N 123 
9Y0 H76    H  N N 124 
9Y0 H77    H  N N 125 
ADP PB     P  N N 126 
ADP O1B    O  N N 127 
ADP O2B    O  N N 128 
ADP O3B    O  N N 129 
ADP PA     P  N S 130 
ADP O1A    O  N N 131 
ADP O2A    O  N N 132 
ADP O3A    O  N N 133 
ADP "O5'"  O  N N 134 
ADP "C5'"  C  N N 135 
ADP "C4'"  C  N R 136 
ADP "O4'"  O  N N 137 
ADP "C3'"  C  N S 138 
ADP "O3'"  O  N N 139 
ADP "C2'"  C  N R 140 
ADP "O2'"  O  N N 141 
ADP "C1'"  C  N R 142 
ADP N9     N  Y N 143 
ADP C8     C  Y N 144 
ADP N7     N  Y N 145 
ADP C5     C  Y N 146 
ADP C6     C  Y N 147 
ADP N6     N  N N 148 
ADP N1     N  Y N 149 
ADP C2     C  Y N 150 
ADP N3     N  Y N 151 
ADP C4     C  Y N 152 
ADP HOB2   H  N N 153 
ADP HOB3   H  N N 154 
ADP HOA2   H  N N 155 
ADP "H5'1" H  N N 156 
ADP "H5'2" H  N N 157 
ADP "H4'"  H  N N 158 
ADP "H3'"  H  N N 159 
ADP "HO3'" H  N N 160 
ADP "H2'"  H  N N 161 
ADP "HO2'" H  N N 162 
ADP "H1'"  H  N N 163 
ADP H8     H  N N 164 
ADP HN61   H  N N 165 
ADP HN62   H  N N 166 
ADP H2     H  N N 167 
ALA N      N  N N 168 
ALA CA     C  N S 169 
ALA C      C  N N 170 
ALA O      O  N N 171 
ALA CB     C  N N 172 
ALA OXT    O  N N 173 
ALA H      H  N N 174 
ALA H2     H  N N 175 
ALA HA     H  N N 176 
ALA HB1    H  N N 177 
ALA HB2    H  N N 178 
ALA HB3    H  N N 179 
ALA HXT    H  N N 180 
ARG N      N  N N 181 
ARG CA     C  N S 182 
ARG C      C  N N 183 
ARG O      O  N N 184 
ARG CB     C  N N 185 
ARG CG     C  N N 186 
ARG CD     C  N N 187 
ARG NE     N  N N 188 
ARG CZ     C  N N 189 
ARG NH1    N  N N 190 
ARG NH2    N  N N 191 
ARG OXT    O  N N 192 
ARG H      H  N N 193 
ARG H2     H  N N 194 
ARG HA     H  N N 195 
ARG HB2    H  N N 196 
ARG HB3    H  N N 197 
ARG HG2    H  N N 198 
ARG HG3    H  N N 199 
ARG HD2    H  N N 200 
ARG HD3    H  N N 201 
ARG HE     H  N N 202 
ARG HH11   H  N N 203 
ARG HH12   H  N N 204 
ARG HH21   H  N N 205 
ARG HH22   H  N N 206 
ARG HXT    H  N N 207 
ASN N      N  N N 208 
ASN CA     C  N S 209 
ASN C      C  N N 210 
ASN O      O  N N 211 
ASN CB     C  N N 212 
ASN CG     C  N N 213 
ASN OD1    O  N N 214 
ASN ND2    N  N N 215 
ASN OXT    O  N N 216 
ASN H      H  N N 217 
ASN H2     H  N N 218 
ASN HA     H  N N 219 
ASN HB2    H  N N 220 
ASN HB3    H  N N 221 
ASN HD21   H  N N 222 
ASN HD22   H  N N 223 
ASN HXT    H  N N 224 
ASP N      N  N N 225 
ASP CA     C  N S 226 
ASP C      C  N N 227 
ASP O      O  N N 228 
ASP CB     C  N N 229 
ASP CG     C  N N 230 
ASP OD1    O  N N 231 
ASP OD2    O  N N 232 
ASP OXT    O  N N 233 
ASP H      H  N N 234 
ASP H2     H  N N 235 
ASP HA     H  N N 236 
ASP HB2    H  N N 237 
ASP HB3    H  N N 238 
ASP HD2    H  N N 239 
ASP HXT    H  N N 240 
CYS N      N  N N 241 
CYS CA     C  N R 242 
CYS C      C  N N 243 
CYS O      O  N N 244 
CYS CB     C  N N 245 
CYS SG     S  N N 246 
CYS OXT    O  N N 247 
CYS H      H  N N 248 
CYS H2     H  N N 249 
CYS HA     H  N N 250 
CYS HB2    H  N N 251 
CYS HB3    H  N N 252 
CYS HG     H  N N 253 
CYS HXT    H  N N 254 
GLN N      N  N N 255 
GLN CA     C  N S 256 
GLN C      C  N N 257 
GLN O      O  N N 258 
GLN CB     C  N N 259 
GLN CG     C  N N 260 
GLN CD     C  N N 261 
GLN OE1    O  N N 262 
GLN NE2    N  N N 263 
GLN OXT    O  N N 264 
GLN H      H  N N 265 
GLN H2     H  N N 266 
GLN HA     H  N N 267 
GLN HB2    H  N N 268 
GLN HB3    H  N N 269 
GLN HG2    H  N N 270 
GLN HG3    H  N N 271 
GLN HE21   H  N N 272 
GLN HE22   H  N N 273 
GLN HXT    H  N N 274 
GLU N      N  N N 275 
GLU CA     C  N S 276 
GLU C      C  N N 277 
GLU O      O  N N 278 
GLU CB     C  N N 279 
GLU CG     C  N N 280 
GLU CD     C  N N 281 
GLU OE1    O  N N 282 
GLU OE2    O  N N 283 
GLU OXT    O  N N 284 
GLU H      H  N N 285 
GLU H2     H  N N 286 
GLU HA     H  N N 287 
GLU HB2    H  N N 288 
GLU HB3    H  N N 289 
GLU HG2    H  N N 290 
GLU HG3    H  N N 291 
GLU HE2    H  N N 292 
GLU HXT    H  N N 293 
GLY N      N  N N 294 
GLY CA     C  N N 295 
GLY C      C  N N 296 
GLY O      O  N N 297 
GLY OXT    O  N N 298 
GLY H      H  N N 299 
GLY H2     H  N N 300 
GLY HA2    H  N N 301 
GLY HA3    H  N N 302 
GLY HXT    H  N N 303 
HIS N      N  N N 304 
HIS CA     C  N S 305 
HIS C      C  N N 306 
HIS O      O  N N 307 
HIS CB     C  N N 308 
HIS CG     C  Y N 309 
HIS ND1    N  Y N 310 
HIS CD2    C  Y N 311 
HIS CE1    C  Y N 312 
HIS NE2    N  Y N 313 
HIS OXT    O  N N 314 
HIS H      H  N N 315 
HIS H2     H  N N 316 
HIS HA     H  N N 317 
HIS HB2    H  N N 318 
HIS HB3    H  N N 319 
HIS HD1    H  N N 320 
HIS HD2    H  N N 321 
HIS HE1    H  N N 322 
HIS HE2    H  N N 323 
HIS HXT    H  N N 324 
HOH O      O  N N 325 
HOH H1     H  N N 326 
HOH H2     H  N N 327 
ILE N      N  N N 328 
ILE CA     C  N S 329 
ILE C      C  N N 330 
ILE O      O  N N 331 
ILE CB     C  N S 332 
ILE CG1    C  N N 333 
ILE CG2    C  N N 334 
ILE CD1    C  N N 335 
ILE OXT    O  N N 336 
ILE H      H  N N 337 
ILE H2     H  N N 338 
ILE HA     H  N N 339 
ILE HB     H  N N 340 
ILE HG12   H  N N 341 
ILE HG13   H  N N 342 
ILE HG21   H  N N 343 
ILE HG22   H  N N 344 
ILE HG23   H  N N 345 
ILE HD11   H  N N 346 
ILE HD12   H  N N 347 
ILE HD13   H  N N 348 
ILE HXT    H  N N 349 
K   K      K  N N 350 
LEU N      N  N N 351 
LEU CA     C  N S 352 
LEU C      C  N N 353 
LEU O      O  N N 354 
LEU CB     C  N N 355 
LEU CG     C  N N 356 
LEU CD1    C  N N 357 
LEU CD2    C  N N 358 
LEU OXT    O  N N 359 
LEU H      H  N N 360 
LEU H2     H  N N 361 
LEU HA     H  N N 362 
LEU HB2    H  N N 363 
LEU HB3    H  N N 364 
LEU HG     H  N N 365 
LEU HD11   H  N N 366 
LEU HD12   H  N N 367 
LEU HD13   H  N N 368 
LEU HD21   H  N N 369 
LEU HD22   H  N N 370 
LEU HD23   H  N N 371 
LEU HXT    H  N N 372 
LYS N      N  N N 373 
LYS CA     C  N S 374 
LYS C      C  N N 375 
LYS O      O  N N 376 
LYS CB     C  N N 377 
LYS CG     C  N N 378 
LYS CD     C  N N 379 
LYS CE     C  N N 380 
LYS NZ     N  N N 381 
LYS OXT    O  N N 382 
LYS H      H  N N 383 
LYS H2     H  N N 384 
LYS HA     H  N N 385 
LYS HB2    H  N N 386 
LYS HB3    H  N N 387 
LYS HG2    H  N N 388 
LYS HG3    H  N N 389 
LYS HD2    H  N N 390 
LYS HD3    H  N N 391 
LYS HE2    H  N N 392 
LYS HE3    H  N N 393 
LYS HZ1    H  N N 394 
LYS HZ2    H  N N 395 
LYS HZ3    H  N N 396 
LYS HXT    H  N N 397 
MET N      N  N N 398 
MET CA     C  N S 399 
MET C      C  N N 400 
MET O      O  N N 401 
MET CB     C  N N 402 
MET CG     C  N N 403 
MET SD     S  N N 404 
MET CE     C  N N 405 
MET OXT    O  N N 406 
MET H      H  N N 407 
MET H2     H  N N 408 
MET HA     H  N N 409 
MET HB2    H  N N 410 
MET HB3    H  N N 411 
MET HG2    H  N N 412 
MET HG3    H  N N 413 
MET HE1    H  N N 414 
MET HE2    H  N N 415 
MET HE3    H  N N 416 
MET HXT    H  N N 417 
MG  MG     MG N N 418 
PHD N      N  N N 419 
PHD CA     C  N S 420 
PHD C      C  N N 421 
PHD O      O  N N 422 
PHD CB     C  N N 423 
PHD CG     C  N N 424 
PHD OD1    O  N N 425 
PHD OD2    O  N N 426 
PHD P      P  N N 427 
PHD OP1    O  N N 428 
PHD OP2    O  N N 429 
PHD OP3    O  N N 430 
PHD OXT    O  N N 431 
PHD H2     H  N N 432 
PHD H      H  N N 433 
PHD HA     H  N N 434 
PHD HB2    H  N N 435 
PHD HB3    H  N N 436 
PHD H2O    H  N N 437 
PHD H3O    H  N N 438 
PHD HXT    H  N N 439 
PHE N      N  N N 440 
PHE CA     C  N S 441 
PHE C      C  N N 442 
PHE O      O  N N 443 
PHE CB     C  N N 444 
PHE CG     C  Y N 445 
PHE CD1    C  Y N 446 
PHE CD2    C  Y N 447 
PHE CE1    C  Y N 448 
PHE CE2    C  Y N 449 
PHE CZ     C  Y N 450 
PHE OXT    O  N N 451 
PHE H      H  N N 452 
PHE H2     H  N N 453 
PHE HA     H  N N 454 
PHE HB2    H  N N 455 
PHE HB3    H  N N 456 
PHE HD1    H  N N 457 
PHE HD2    H  N N 458 
PHE HE1    H  N N 459 
PHE HE2    H  N N 460 
PHE HZ     H  N N 461 
PHE HXT    H  N N 462 
PRO N      N  N N 463 
PRO CA     C  N S 464 
PRO C      C  N N 465 
PRO O      O  N N 466 
PRO CB     C  N N 467 
PRO CG     C  N N 468 
PRO CD     C  N N 469 
PRO OXT    O  N N 470 
PRO H      H  N N 471 
PRO HA     H  N N 472 
PRO HB2    H  N N 473 
PRO HB3    H  N N 474 
PRO HG2    H  N N 475 
PRO HG3    H  N N 476 
PRO HD2    H  N N 477 
PRO HD3    H  N N 478 
PRO HXT    H  N N 479 
SER N      N  N N 480 
SER CA     C  N S 481 
SER C      C  N N 482 
SER O      O  N N 483 
SER CB     C  N N 484 
SER OG     O  N N 485 
SER OXT    O  N N 486 
SER H      H  N N 487 
SER H2     H  N N 488 
SER HA     H  N N 489 
SER HB2    H  N N 490 
SER HB3    H  N N 491 
SER HG     H  N N 492 
SER HXT    H  N N 493 
THR N      N  N N 494 
THR CA     C  N S 495 
THR C      C  N N 496 
THR O      O  N N 497 
THR CB     C  N R 498 
THR OG1    O  N N 499 
THR CG2    C  N N 500 
THR OXT    O  N N 501 
THR H      H  N N 502 
THR H2     H  N N 503 
THR HA     H  N N 504 
THR HB     H  N N 505 
THR HG1    H  N N 506 
THR HG21   H  N N 507 
THR HG22   H  N N 508 
THR HG23   H  N N 509 
THR HXT    H  N N 510 
TRP N      N  N N 511 
TRP CA     C  N S 512 
TRP C      C  N N 513 
TRP O      O  N N 514 
TRP CB     C  N N 515 
TRP CG     C  Y N 516 
TRP CD1    C  Y N 517 
TRP CD2    C  Y N 518 
TRP NE1    N  Y N 519 
TRP CE2    C  Y N 520 
TRP CE3    C  Y N 521 
TRP CZ2    C  Y N 522 
TRP CZ3    C  Y N 523 
TRP CH2    C  Y N 524 
TRP OXT    O  N N 525 
TRP H      H  N N 526 
TRP H2     H  N N 527 
TRP HA     H  N N 528 
TRP HB2    H  N N 529 
TRP HB3    H  N N 530 
TRP HD1    H  N N 531 
TRP HE1    H  N N 532 
TRP HE3    H  N N 533 
TRP HZ2    H  N N 534 
TRP HZ3    H  N N 535 
TRP HH2    H  N N 536 
TRP HXT    H  N N 537 
TYR N      N  N N 538 
TYR CA     C  N S 539 
TYR C      C  N N 540 
TYR O      O  N N 541 
TYR CB     C  N N 542 
TYR CG     C  Y N 543 
TYR CD1    C  Y N 544 
TYR CD2    C  Y N 545 
TYR CE1    C  Y N 546 
TYR CE2    C  Y N 547 
TYR CZ     C  Y N 548 
TYR OH     O  N N 549 
TYR OXT    O  N N 550 
TYR H      H  N N 551 
TYR H2     H  N N 552 
TYR HA     H  N N 553 
TYR HB2    H  N N 554 
TYR HB3    H  N N 555 
TYR HD1    H  N N 556 
TYR HD2    H  N N 557 
TYR HE1    H  N N 558 
TYR HE2    H  N N 559 
TYR HH     H  N N 560 
TYR HXT    H  N N 561 
VAL N      N  N N 562 
VAL CA     C  N S 563 
VAL C      C  N N 564 
VAL O      O  N N 565 
VAL CB     C  N N 566 
VAL CG1    C  N N 567 
VAL CG2    C  N N 568 
VAL OXT    O  N N 569 
VAL H      H  N N 570 
VAL H2     H  N N 571 
VAL HA     H  N N 572 
VAL HB     H  N N 573 
VAL HG11   H  N N 574 
VAL HG12   H  N N 575 
VAL HG13   H  N N 576 
VAL HG21   H  N N 577 
VAL HG22   H  N N 578 
VAL HG23   H  N N 579 
VAL HXT    H  N N 580 
# 
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 
9Y0 C20   C37    sing N N 1   
9Y0 C20   C19    sing N N 2   
9Y0 C37   C38    sing N N 3   
9Y0 C18   C19    sing N N 4   
9Y0 C18   C17    sing N N 5   
9Y0 C17   C16    sing N N 6   
9Y0 C16   C15    sing N N 7   
9Y0 C15   C14    sing N N 8   
9Y0 C33   C34    sing N N 9   
9Y0 C33   C32    sing N N 10  
9Y0 C14   C13    doub N Z 11  
9Y0 C34   C35    sing N N 12  
9Y0 C35   C36    sing N N 13  
9Y0 C32   C31    sing N N 14  
9Y0 C13   C12    sing N N 15  
9Y0 C31   C30    sing N N 16  
9Y0 C12   C11    sing N N 17  
9Y0 C30   C29    sing N N 18  
9Y0 C11   C10    sing N N 19  
9Y0 C29   C28    sing N N 20  
9Y0 C10   C9     sing N N 21  
9Y0 C28   C27    sing N N 22  
9Y0 C9    C8     sing N N 23  
9Y0 C27   C26    sing N N 24  
9Y0 C8    C7     sing N N 25  
9Y0 C26   C25    sing N N 26  
9Y0 C25   C24    sing N N 27  
9Y0 C7    C6     sing N N 28  
9Y0 C6    C5     sing N N 29  
9Y0 C24   C23    sing N N 30  
9Y0 C23   C22    sing N N 31  
9Y0 C5    O5     sing N N 32  
9Y0 C5    O4     doub N N 33  
9Y0 O5    C      sing N N 34  
9Y0 O6    C21    doub N N 35  
9Y0 C21   C22    sing N N 36  
9Y0 C21   O7     sing N N 37  
9Y0 C     C1     sing N N 38  
9Y0 O7    C1     sing N N 39  
9Y0 C1    C2     sing N N 40  
9Y0 C2    O3     sing N N 41  
9Y0 O3    P      sing N N 42  
9Y0 C3    C4     sing N N 43  
9Y0 C3    O1     sing N N 44  
9Y0 C4    N      sing N N 45  
9Y0 P     O1     sing N N 46  
9Y0 P     O      doub N N 47  
9Y0 P     O2     sing N N 48  
9Y0 N     H1     sing N N 49  
9Y0 N     H2     sing N N 50  
9Y0 C     H4     sing N N 51  
9Y0 C     H5     sing N N 52  
9Y0 C1    H6     sing N N 53  
9Y0 C10   H7     sing N N 54  
9Y0 C10   H8     sing N N 55  
9Y0 C11   H9     sing N N 56  
9Y0 C11   H10    sing N N 57  
9Y0 C12   H11    sing N N 58  
9Y0 C12   H12    sing N N 59  
9Y0 C13   H13    sing N N 60  
9Y0 C14   H14    sing N N 61  
9Y0 C15   H15    sing N N 62  
9Y0 C15   H16    sing N N 63  
9Y0 C16   H17    sing N N 64  
9Y0 C16   H18    sing N N 65  
9Y0 C17   H19    sing N N 66  
9Y0 C17   H20    sing N N 67  
9Y0 C18   H21    sing N N 68  
9Y0 C18   H22    sing N N 69  
9Y0 C19   H23    sing N N 70  
9Y0 C19   H24    sing N N 71  
9Y0 C2    H25    sing N N 72  
9Y0 C2    H26    sing N N 73  
9Y0 C20   H27    sing N N 74  
9Y0 C20   H28    sing N N 75  
9Y0 C22   H29    sing N N 76  
9Y0 C22   H30    sing N N 77  
9Y0 C23   H31    sing N N 78  
9Y0 C23   H32    sing N N 79  
9Y0 C24   H33    sing N N 80  
9Y0 C24   H34    sing N N 81  
9Y0 C25   H35    sing N N 82  
9Y0 C25   H36    sing N N 83  
9Y0 C26   H37    sing N N 84  
9Y0 C26   H38    sing N N 85  
9Y0 C27   H39    sing N N 86  
9Y0 C27   H40    sing N N 87  
9Y0 C28   H41    sing N N 88  
9Y0 C28   H42    sing N N 89  
9Y0 C29   H43    sing N N 90  
9Y0 C29   H44    sing N N 91  
9Y0 C3    H45    sing N N 92  
9Y0 C3    H46    sing N N 93  
9Y0 C30   H47    sing N N 94  
9Y0 C30   H48    sing N N 95  
9Y0 C31   H49    sing N N 96  
9Y0 C31   H50    sing N N 97  
9Y0 C32   H51    sing N N 98  
9Y0 C32   H52    sing N N 99  
9Y0 C33   H53    sing N N 100 
9Y0 C33   H54    sing N N 101 
9Y0 C34   H55    sing N N 102 
9Y0 C34   H56    sing N N 103 
9Y0 C35   H57    sing N N 104 
9Y0 C35   H58    sing N N 105 
9Y0 C36   H59    sing N N 106 
9Y0 C36   H60    sing N N 107 
9Y0 C36   H61    sing N N 108 
9Y0 C37   H62    sing N N 109 
9Y0 C37   H63    sing N N 110 
9Y0 C38   H64    sing N N 111 
9Y0 C38   H65    sing N N 112 
9Y0 C38   H66    sing N N 113 
9Y0 C4    H67    sing N N 114 
9Y0 C4    H68    sing N N 115 
9Y0 C6    H69    sing N N 116 
9Y0 C6    H70    sing N N 117 
9Y0 C7    H71    sing N N 118 
9Y0 C7    H72    sing N N 119 
9Y0 C8    H73    sing N N 120 
9Y0 C8    H74    sing N N 121 
9Y0 C9    H75    sing N N 122 
9Y0 C9    H76    sing N N 123 
9Y0 O2    H77    sing N N 124 
ADP PB    O1B    doub N N 125 
ADP PB    O2B    sing N N 126 
ADP PB    O3B    sing N N 127 
ADP PB    O3A    sing N N 128 
ADP O2B   HOB2   sing N N 129 
ADP O3B   HOB3   sing N N 130 
ADP PA    O1A    doub N N 131 
ADP PA    O2A    sing N N 132 
ADP PA    O3A    sing N N 133 
ADP PA    "O5'"  sing N N 134 
ADP O2A   HOA2   sing N N 135 
ADP "O5'" "C5'"  sing N N 136 
ADP "C5'" "C4'"  sing N N 137 
ADP "C5'" "H5'1" sing N N 138 
ADP "C5'" "H5'2" sing N N 139 
ADP "C4'" "O4'"  sing N N 140 
ADP "C4'" "C3'"  sing N N 141 
ADP "C4'" "H4'"  sing N N 142 
ADP "O4'" "C1'"  sing N N 143 
ADP "C3'" "O3'"  sing N N 144 
ADP "C3'" "C2'"  sing N N 145 
ADP "C3'" "H3'"  sing N N 146 
ADP "O3'" "HO3'" sing N N 147 
ADP "C2'" "O2'"  sing N N 148 
ADP "C2'" "C1'"  sing N N 149 
ADP "C2'" "H2'"  sing N N 150 
ADP "O2'" "HO2'" sing N N 151 
ADP "C1'" N9     sing N N 152 
ADP "C1'" "H1'"  sing N N 153 
ADP N9    C8     sing Y N 154 
ADP N9    C4     sing Y N 155 
ADP C8    N7     doub Y N 156 
ADP C8    H8     sing N N 157 
ADP N7    C5     sing Y N 158 
ADP C5    C6     sing Y N 159 
ADP C5    C4     doub Y N 160 
ADP C6    N6     sing N N 161 
ADP C6    N1     doub Y N 162 
ADP N6    HN61   sing N N 163 
ADP N6    HN62   sing N N 164 
ADP N1    C2     sing Y N 165 
ADP C2    N3     doub Y N 166 
ADP C2    H2     sing N N 167 
ADP N3    C4     sing Y N 168 
ALA N     CA     sing N N 169 
ALA N     H      sing N N 170 
ALA N     H2     sing N N 171 
ALA CA    C      sing N N 172 
ALA CA    CB     sing N N 173 
ALA CA    HA     sing N N 174 
ALA C     O      doub N N 175 
ALA C     OXT    sing N N 176 
ALA CB    HB1    sing N N 177 
ALA CB    HB2    sing N N 178 
ALA CB    HB3    sing N N 179 
ALA OXT   HXT    sing N N 180 
ARG N     CA     sing N N 181 
ARG N     H      sing N N 182 
ARG N     H2     sing N N 183 
ARG CA    C      sing N N 184 
ARG CA    CB     sing N N 185 
ARG CA    HA     sing N N 186 
ARG C     O      doub N N 187 
ARG C     OXT    sing N N 188 
ARG CB    CG     sing N N 189 
ARG CB    HB2    sing N N 190 
ARG CB    HB3    sing N N 191 
ARG CG    CD     sing N N 192 
ARG CG    HG2    sing N N 193 
ARG CG    HG3    sing N N 194 
ARG CD    NE     sing N N 195 
ARG CD    HD2    sing N N 196 
ARG CD    HD3    sing N N 197 
ARG NE    CZ     sing N N 198 
ARG NE    HE     sing N N 199 
ARG CZ    NH1    sing N N 200 
ARG CZ    NH2    doub N N 201 
ARG NH1   HH11   sing N N 202 
ARG NH1   HH12   sing N N 203 
ARG NH2   HH21   sing N N 204 
ARG NH2   HH22   sing N N 205 
ARG OXT   HXT    sing N N 206 
ASN N     CA     sing N N 207 
ASN N     H      sing N N 208 
ASN N     H2     sing N N 209 
ASN CA    C      sing N N 210 
ASN CA    CB     sing N N 211 
ASN CA    HA     sing N N 212 
ASN C     O      doub N N 213 
ASN C     OXT    sing N N 214 
ASN CB    CG     sing N N 215 
ASN CB    HB2    sing N N 216 
ASN CB    HB3    sing N N 217 
ASN CG    OD1    doub N N 218 
ASN CG    ND2    sing N N 219 
ASN ND2   HD21   sing N N 220 
ASN ND2   HD22   sing N N 221 
ASN OXT   HXT    sing N N 222 
ASP N     CA     sing N N 223 
ASP N     H      sing N N 224 
ASP N     H2     sing N N 225 
ASP CA    C      sing N N 226 
ASP CA    CB     sing N N 227 
ASP CA    HA     sing N N 228 
ASP C     O      doub N N 229 
ASP C     OXT    sing N N 230 
ASP CB    CG     sing N N 231 
ASP CB    HB2    sing N N 232 
ASP CB    HB3    sing N N 233 
ASP CG    OD1    doub N N 234 
ASP CG    OD2    sing N N 235 
ASP OD2   HD2    sing N N 236 
ASP OXT   HXT    sing N N 237 
CYS N     CA     sing N N 238 
CYS N     H      sing N N 239 
CYS N     H2     sing N N 240 
CYS CA    C      sing N N 241 
CYS CA    CB     sing N N 242 
CYS CA    HA     sing N N 243 
CYS C     O      doub N N 244 
CYS C     OXT    sing N N 245 
CYS CB    SG     sing N N 246 
CYS CB    HB2    sing N N 247 
CYS CB    HB3    sing N N 248 
CYS SG    HG     sing N N 249 
CYS OXT   HXT    sing N N 250 
GLN N     CA     sing N N 251 
GLN N     H      sing N N 252 
GLN N     H2     sing N N 253 
GLN CA    C      sing N N 254 
GLN CA    CB     sing N N 255 
GLN CA    HA     sing N N 256 
GLN C     O      doub N N 257 
GLN C     OXT    sing N N 258 
GLN CB    CG     sing N N 259 
GLN CB    HB2    sing N N 260 
GLN CB    HB3    sing N N 261 
GLN CG    CD     sing N N 262 
GLN CG    HG2    sing N N 263 
GLN CG    HG3    sing N N 264 
GLN CD    OE1    doub N N 265 
GLN CD    NE2    sing N N 266 
GLN NE2   HE21   sing N N 267 
GLN NE2   HE22   sing N N 268 
GLN OXT   HXT    sing N N 269 
GLU N     CA     sing N N 270 
GLU N     H      sing N N 271 
GLU N     H2     sing N N 272 
GLU CA    C      sing N N 273 
GLU CA    CB     sing N N 274 
GLU CA    HA     sing N N 275 
GLU C     O      doub N N 276 
GLU C     OXT    sing N N 277 
GLU CB    CG     sing N N 278 
GLU CB    HB2    sing N N 279 
GLU CB    HB3    sing N N 280 
GLU CG    CD     sing N N 281 
GLU CG    HG2    sing N N 282 
GLU CG    HG3    sing N N 283 
GLU CD    OE1    doub N N 284 
GLU CD    OE2    sing N N 285 
GLU OE2   HE2    sing N N 286 
GLU OXT   HXT    sing N N 287 
GLY N     CA     sing N N 288 
GLY N     H      sing N N 289 
GLY N     H2     sing N N 290 
GLY CA    C      sing N N 291 
GLY CA    HA2    sing N N 292 
GLY CA    HA3    sing N N 293 
GLY C     O      doub N N 294 
GLY C     OXT    sing N N 295 
GLY OXT   HXT    sing N N 296 
HIS N     CA     sing N N 297 
HIS N     H      sing N N 298 
HIS N     H2     sing N N 299 
HIS CA    C      sing N N 300 
HIS CA    CB     sing N N 301 
HIS CA    HA     sing N N 302 
HIS C     O      doub N N 303 
HIS C     OXT    sing N N 304 
HIS CB    CG     sing N N 305 
HIS CB    HB2    sing N N 306 
HIS CB    HB3    sing N N 307 
HIS CG    ND1    sing Y N 308 
HIS CG    CD2    doub Y N 309 
HIS ND1   CE1    doub Y N 310 
HIS ND1   HD1    sing N N 311 
HIS CD2   NE2    sing Y N 312 
HIS CD2   HD2    sing N N 313 
HIS CE1   NE2    sing Y N 314 
HIS CE1   HE1    sing N N 315 
HIS NE2   HE2    sing N N 316 
HIS OXT   HXT    sing N N 317 
HOH O     H1     sing N N 318 
HOH O     H2     sing N N 319 
ILE N     CA     sing N N 320 
ILE N     H      sing N N 321 
ILE N     H2     sing N N 322 
ILE CA    C      sing N N 323 
ILE CA    CB     sing N N 324 
ILE CA    HA     sing N N 325 
ILE C     O      doub N N 326 
ILE C     OXT    sing N N 327 
ILE CB    CG1    sing N N 328 
ILE CB    CG2    sing N N 329 
ILE CB    HB     sing N N 330 
ILE CG1   CD1    sing N N 331 
ILE CG1   HG12   sing N N 332 
ILE CG1   HG13   sing N N 333 
ILE CG2   HG21   sing N N 334 
ILE CG2   HG22   sing N N 335 
ILE CG2   HG23   sing N N 336 
ILE CD1   HD11   sing N N 337 
ILE CD1   HD12   sing N N 338 
ILE CD1   HD13   sing N N 339 
ILE OXT   HXT    sing N N 340 
LEU N     CA     sing N N 341 
LEU N     H      sing N N 342 
LEU N     H2     sing N N 343 
LEU CA    C      sing N N 344 
LEU CA    CB     sing N N 345 
LEU CA    HA     sing N N 346 
LEU C     O      doub N N 347 
LEU C     OXT    sing N N 348 
LEU CB    CG     sing N N 349 
LEU CB    HB2    sing N N 350 
LEU CB    HB3    sing N N 351 
LEU CG    CD1    sing N N 352 
LEU CG    CD2    sing N N 353 
LEU CG    HG     sing N N 354 
LEU CD1   HD11   sing N N 355 
LEU CD1   HD12   sing N N 356 
LEU CD1   HD13   sing N N 357 
LEU CD2   HD21   sing N N 358 
LEU CD2   HD22   sing N N 359 
LEU CD2   HD23   sing N N 360 
LEU OXT   HXT    sing N N 361 
LYS N     CA     sing N N 362 
LYS N     H      sing N N 363 
LYS N     H2     sing N N 364 
LYS CA    C      sing N N 365 
LYS CA    CB     sing N N 366 
LYS CA    HA     sing N N 367 
LYS C     O      doub N N 368 
LYS C     OXT    sing N N 369 
LYS CB    CG     sing N N 370 
LYS CB    HB2    sing N N 371 
LYS CB    HB3    sing N N 372 
LYS CG    CD     sing N N 373 
LYS CG    HG2    sing N N 374 
LYS CG    HG3    sing N N 375 
LYS CD    CE     sing N N 376 
LYS CD    HD2    sing N N 377 
LYS CD    HD3    sing N N 378 
LYS CE    NZ     sing N N 379 
LYS CE    HE2    sing N N 380 
LYS CE    HE3    sing N N 381 
LYS NZ    HZ1    sing N N 382 
LYS NZ    HZ2    sing N N 383 
LYS NZ    HZ3    sing N N 384 
LYS OXT   HXT    sing N N 385 
MET N     CA     sing N N 386 
MET N     H      sing N N 387 
MET N     H2     sing N N 388 
MET CA    C      sing N N 389 
MET CA    CB     sing N N 390 
MET CA    HA     sing N N 391 
MET C     O      doub N N 392 
MET C     OXT    sing N N 393 
MET CB    CG     sing N N 394 
MET CB    HB2    sing N N 395 
MET CB    HB3    sing N N 396 
MET CG    SD     sing N N 397 
MET CG    HG2    sing N N 398 
MET CG    HG3    sing N N 399 
MET SD    CE     sing N N 400 
MET CE    HE1    sing N N 401 
MET CE    HE2    sing N N 402 
MET CE    HE3    sing N N 403 
MET OXT   HXT    sing N N 404 
PHD N     CA     sing N N 405 
PHD N     H2     sing N N 406 
PHD N     H      sing N N 407 
PHD CA    C      sing N N 408 
PHD CA    CB     sing N N 409 
PHD CA    HA     sing N N 410 
PHD C     O      doub N N 411 
PHD C     OXT    sing N N 412 
PHD CB    CG     sing N N 413 
PHD CB    HB2    sing N N 414 
PHD CB    HB3    sing N N 415 
PHD CG    OD1    sing N N 416 
PHD CG    OD2    doub N N 417 
PHD OD1   P      sing N N 418 
PHD P     OP1    doub N N 419 
PHD P     OP2    sing N N 420 
PHD P     OP3    sing N N 421 
PHD OP2   H2O    sing N N 422 
PHD OP3   H3O    sing N N 423 
PHD OXT   HXT    sing N N 424 
PHE N     CA     sing N N 425 
PHE N     H      sing N N 426 
PHE N     H2     sing N N 427 
PHE CA    C      sing N N 428 
PHE CA    CB     sing N N 429 
PHE CA    HA     sing N N 430 
PHE C     O      doub N N 431 
PHE C     OXT    sing N N 432 
PHE CB    CG     sing N N 433 
PHE CB    HB2    sing N N 434 
PHE CB    HB3    sing N N 435 
PHE CG    CD1    doub Y N 436 
PHE CG    CD2    sing Y N 437 
PHE CD1   CE1    sing Y N 438 
PHE CD1   HD1    sing N N 439 
PHE CD2   CE2    doub Y N 440 
PHE CD2   HD2    sing N N 441 
PHE CE1   CZ     doub Y N 442 
PHE CE1   HE1    sing N N 443 
PHE CE2   CZ     sing Y N 444 
PHE CE2   HE2    sing N N 445 
PHE CZ    HZ     sing N N 446 
PHE OXT   HXT    sing N N 447 
PRO N     CA     sing N N 448 
PRO N     CD     sing N N 449 
PRO N     H      sing N N 450 
PRO CA    C      sing N N 451 
PRO CA    CB     sing N N 452 
PRO CA    HA     sing N N 453 
PRO C     O      doub N N 454 
PRO C     OXT    sing N N 455 
PRO CB    CG     sing N N 456 
PRO CB    HB2    sing N N 457 
PRO CB    HB3    sing N N 458 
PRO CG    CD     sing N N 459 
PRO CG    HG2    sing N N 460 
PRO CG    HG3    sing N N 461 
PRO CD    HD2    sing N N 462 
PRO CD    HD3    sing N N 463 
PRO OXT   HXT    sing N N 464 
SER N     CA     sing N N 465 
SER N     H      sing N N 466 
SER N     H2     sing N N 467 
SER CA    C      sing N N 468 
SER CA    CB     sing N N 469 
SER CA    HA     sing N N 470 
SER C     O      doub N N 471 
SER C     OXT    sing N N 472 
SER CB    OG     sing N N 473 
SER CB    HB2    sing N N 474 
SER CB    HB3    sing N N 475 
SER OG    HG     sing N N 476 
SER OXT   HXT    sing N N 477 
THR N     CA     sing N N 478 
THR N     H      sing N N 479 
THR N     H2     sing N N 480 
THR CA    C      sing N N 481 
THR CA    CB     sing N N 482 
THR CA    HA     sing N N 483 
THR C     O      doub N N 484 
THR C     OXT    sing N N 485 
THR CB    OG1    sing N N 486 
THR CB    CG2    sing N N 487 
THR CB    HB     sing N N 488 
THR OG1   HG1    sing N N 489 
THR CG2   HG21   sing N N 490 
THR CG2   HG22   sing N N 491 
THR CG2   HG23   sing N N 492 
THR OXT   HXT    sing N N 493 
TRP N     CA     sing N N 494 
TRP N     H      sing N N 495 
TRP N     H2     sing N N 496 
TRP CA    C      sing N N 497 
TRP CA    CB     sing N N 498 
TRP CA    HA     sing N N 499 
TRP C     O      doub N N 500 
TRP C     OXT    sing N N 501 
TRP CB    CG     sing N N 502 
TRP CB    HB2    sing N N 503 
TRP CB    HB3    sing N N 504 
TRP CG    CD1    doub Y N 505 
TRP CG    CD2    sing Y N 506 
TRP CD1   NE1    sing Y N 507 
TRP CD1   HD1    sing N N 508 
TRP CD2   CE2    doub Y N 509 
TRP CD2   CE3    sing Y N 510 
TRP NE1   CE2    sing Y N 511 
TRP NE1   HE1    sing N N 512 
TRP CE2   CZ2    sing Y N 513 
TRP CE3   CZ3    doub Y N 514 
TRP CE3   HE3    sing N N 515 
TRP CZ2   CH2    doub Y N 516 
TRP CZ2   HZ2    sing N N 517 
TRP CZ3   CH2    sing Y N 518 
TRP CZ3   HZ3    sing N N 519 
TRP CH2   HH2    sing N N 520 
TRP OXT   HXT    sing N N 521 
TYR N     CA     sing N N 522 
TYR N     H      sing N N 523 
TYR N     H2     sing N N 524 
TYR CA    C      sing N N 525 
TYR CA    CB     sing N N 526 
TYR CA    HA     sing N N 527 
TYR C     O      doub N N 528 
TYR C     OXT    sing N N 529 
TYR CB    CG     sing N N 530 
TYR CB    HB2    sing N N 531 
TYR CB    HB3    sing N N 532 
TYR CG    CD1    doub Y N 533 
TYR CG    CD2    sing Y N 534 
TYR CD1   CE1    sing Y N 535 
TYR CD1   HD1    sing N N 536 
TYR CD2   CE2    doub Y N 537 
TYR CD2   HD2    sing N N 538 
TYR CE1   CZ     doub Y N 539 
TYR CE1   HE1    sing N N 540 
TYR CE2   CZ     sing Y N 541 
TYR CE2   HE2    sing N N 542 
TYR CZ    OH     sing N N 543 
TYR OH    HH     sing N N 544 
TYR OXT   HXT    sing N N 545 
VAL N     CA     sing N N 546 
VAL N     H      sing N N 547 
VAL N     H2     sing N N 548 
VAL CA    C      sing N N 549 
VAL CA    CB     sing N N 550 
VAL CA    HA     sing N N 551 
VAL C     O      doub N N 552 
VAL C     OXT    sing N N 553 
VAL CB    CG1    sing N N 554 
VAL CB    CG2    sing N N 555 
VAL CB    HB     sing N N 556 
VAL CG1   HG11   sing N N 557 
VAL CG1   HG12   sing N N 558 
VAL CG1   HG13   sing N N 559 
VAL CG2   HG21   sing N N 560 
VAL CG2   HG22   sing N N 561 
VAL CG2   HG23   sing N N 562 
VAL OXT   HXT    sing N N 563 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2025-04-23 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9OC4 
_em_admin.last_update        2025-05-21 
_em_admin.map_release_date   2025-05-21 
_em_admin.title              'High-resolution cryo-EM structure of KdpFABC in the E1P-ADP state in lipid nanodisc' 
# 
loop_
_em_buffer_component.buffer_id 
_em_buffer_component.concentration 
_em_buffer_component.concentration_units 
_em_buffer_component.formula 
_em_buffer_component.id 
_em_buffer_component.name 
1 20  mM ?   1 Tris                 
1 100 mM KCl 2 'potassium chloride' 
1 0.5 mM ?   3 TCEP                 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    NO 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                MEGADALTONS 
_em_entity_assembly_molwt.value                0.154150 
# 
_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          83333 
_em_entity_assembly_naturalsource.organism             'Escherichia coli K-12' 
_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          83333 
_em_entity_assembly_recombinant.organism             'Escherichia coli K-12' 
_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 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'FEI FALCON IV (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                    4 
_em_image_recording.num_real_images                     50000 
# 
_em_imaging_optics.chr_aberration_corrector   ? 
_em_imaging_optics.energyfilter_lower         ? 
_em_imaging_optics.energyfilter_slit_width    ? 
_em_imaging_optics.energyfilter_name          'TFS Selectris' 
_em_imaging_optics.energyfilter_upper         ? 
_em_imaging_optics.id                         1 
_em_imaging_optics.imaging_id                 1 
_em_imaging_optics.phase_plate                ? 
_em_imaging_optics.sph_aberration_corrector   ? 
_em_imaging_optics.details                    ? 
# 
_em_particle_selection.details                  ? 
_em_particle_selection.id                       1 
_em_particle_selection.image_processing_id      1 
_em_particle_selection.method                   ? 
_em_particle_selection.num_particles_selected   10282000 
_em_particle_selection.reference_model          ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
_em_software.reference_DOI 
'PARTICLE SELECTION'            ? 1  1 ? ? cryoSPARC      4.6.0    ? 
'IMAGE ACQUISITION'             ? 2  ? ? 1 SerialEM       ?        ? 
MASKING                         ? 3  ? ? ? ?              ?        ? 
'CTF CORRECTION'                ? 4  1 ? ? cryoSPARC      4.6.0    ? 
'LAYERLINE INDEXING'            ? 5  ? ? ? ?              ?        ? 
'DIFFRACTION INDEXING'          ? 6  ? ? ? ?              ?        ? 
'MODEL FITTING'                 ? 7  ? 1 ? 'UCSF Chimera' 1.14     ? 
'MODEL FITTING'                 ? 8  ? 1 ? Coot           0.9.8.95 ? 
OTHER                           ? 9  ? ? ? ?              ?        ? 
'INITIAL EULER ASSIGNMENT'      ? 10 1 ? ? cryoSPARC      4.6.0    ? 
'FINAL EULER ASSIGNMENT'        ? 11 1 ? ? cryoSPARC      4.6.0    ? 
CLASSIFICATION                  ? 12 1 ? ? cryoSPARC      4.6.0    ? 
RECONSTRUCTION                  ? 13 1 ? ? cryoSPARC      4.6.0    ? 
'MODEL REFINEMENT'              ? 14 ? 1 ? PHENIX         1.18     ? 
'VOLUME SELECTION'              ? 15 1 1 1 ?              ?        ? 
'SERIES ALIGNMENT'              ? 16 1 1 1 ?              ?        ? 
'MOLECULAR REPLACEMENT'         ? 17 1 1 1 ?              ?        ? 
'LATTICE DISTORTION CORRECTION' ? 18 1 1 1 ?              ?        ? 
'SYMMETRY DETERMINATION'        ? 19 1 1 1 ?              ?        ? 
'CRYSTALLOGRAPHY MERGING'       ? 20 1 1 1 ?              ?        ? 
# 
_em_specimen.concentration           3.4 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           GM144109 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7LC3 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9OC4 
_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  
K  
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     . MET A 1 1   ? 174.627 198.848 156.240 1.00 36.43  ? 1   MET A N     1 
ATOM   2     C  CA    . MET A 1 1   ? 174.699 197.392 156.269 1.00 31.12  ? 1   MET A CA    1 
ATOM   3     C  C     . MET A 1 1   ? 173.500 196.805 157.004 1.00 31.56  ? 1   MET A C     1 
ATOM   4     O  O     . MET A 1 1   ? 172.880 195.850 156.537 1.00 35.52  ? 1   MET A O     1 
ATOM   5     C  CB    . MET A 1 1   ? 176.000 196.931 156.927 1.00 32.16  ? 1   MET A CB    1 
ATOM   6     C  CG    . MET A 1 1   ? 176.512 195.595 156.419 1.00 29.59  ? 1   MET A CG    1 
ATOM   7     S  SD    . MET A 1 1   ? 177.625 195.778 155.013 1.00 51.00  ? 1   MET A SD    1 
ATOM   8     C  CE    . MET A 1 1   ? 177.676 194.097 154.400 1.00 31.65  ? 1   MET A CE    1 
ATOM   9     N  N     . ALA A 1 2   ? 173.183 197.383 158.166 1.00 32.31  ? 2   ALA A N     1 
ATOM   10    C  CA    . ALA A 1 2   ? 172.022 196.929 158.925 1.00 26.17  ? 2   ALA A CA    1 
ATOM   11    C  C     . ALA A 1 2   ? 170.729 197.186 158.162 1.00 24.91  ? 2   ALA A C     1 
ATOM   12    O  O     . ALA A 1 2   ? 169.823 196.345 158.159 1.00 31.11  ? 2   ALA A O     1 
ATOM   13    C  CB    . ALA A 1 2   ? 171.987 197.612 160.291 1.00 25.20  ? 2   ALA A CB    1 
ATOM   14    N  N     . ALA A 1 3   ? 170.622 198.349 157.514 1.00 30.41  ? 3   ALA A N     1 
ATOM   15    C  CA    . ALA A 1 3   ? 169.431 198.651 156.726 1.00 28.76  ? 3   ALA A CA    1 
ATOM   16    C  C     . ALA A 1 3   ? 169.287 197.689 155.553 1.00 27.93  ? 3   ALA A C     1 
ATOM   17    O  O     . ALA A 1 3   ? 168.178 197.235 155.247 1.00 31.37  ? 3   ALA A O     1 
ATOM   18    C  CB    . ALA A 1 3   ? 169.480 200.097 156.233 1.00 23.61  ? 3   ALA A CB    1 
ATOM   19    N  N     . GLN A 1 4   ? 170.396 197.372 154.882 1.00 28.27  ? 4   GLN A N     1 
ATOM   20    C  CA    . GLN A 1 4   ? 170.347 196.418 153.778 1.00 29.53  ? 4   GLN A CA    1 
ATOM   21    C  C     . GLN A 1 4   ? 169.927 195.037 154.263 1.00 23.99  ? 4   GLN A C     1 
ATOM   22    O  O     . GLN A 1 4   ? 169.141 194.350 153.599 1.00 23.85  ? 4   GLN A O     1 
ATOM   23    C  CB    . GLN A 1 4   ? 171.705 196.353 153.079 1.00 24.81  ? 4   GLN A CB    1 
ATOM   24    C  CG    . GLN A 1 4   ? 172.075 197.616 152.321 1.00 30.25  ? 4   GLN A CG    1 
ATOM   25    C  CD    . GLN A 1 4   ? 171.500 197.644 150.919 1.00 40.25  ? 4   GLN A CD    1 
ATOM   26    O  OE1   . GLN A 1 4   ? 170.473 198.275 150.669 1.00 40.49  ? 4   GLN A OE1   1 
ATOM   27    N  NE2   . GLN A 1 4   ? 172.162 196.959 149.994 1.00 33.69  ? 4   GLN A NE2   1 
ATOM   28    N  N     . GLY A 1 5   ? 170.445 194.610 155.416 1.00 23.87  ? 5   GLY A N     1 
ATOM   29    C  CA    . GLY A 1 5   ? 170.043 193.326 155.966 1.00 20.37  ? 5   GLY A CA    1 
ATOM   30    C  C     . GLY A 1 5   ? 168.581 193.292 156.366 1.00 25.63  ? 5   GLY A C     1 
ATOM   31    O  O     . GLY A 1 5   ? 167.890 192.296 156.140 1.00 25.06  ? 5   GLY A O     1 
ATOM   32    N  N     . PHE A 1 6   ? 168.091 194.377 156.973 1.00 22.43  ? 6   PHE A N     1 
ATOM   33    C  CA    . PHE A 1 6   ? 166.684 194.443 157.352 1.00 22.63  ? 6   PHE A CA    1 
ATOM   34    C  C     . PHE A 1 6   ? 165.779 194.400 156.127 1.00 20.64  ? 6   PHE A C     1 
ATOM   35    O  O     . PHE A 1 6   ? 164.738 193.733 156.138 1.00 22.87  ? 6   PHE A O     1 
ATOM   36    C  CB    . PHE A 1 6   ? 166.419 195.707 158.170 1.00 23.91  ? 6   PHE A CB    1 
ATOM   37    C  CG    . PHE A 1 6   ? 164.972 196.105 158.221 1.00 25.25  ? 6   PHE A CG    1 
ATOM   38    C  CD1   . PHE A 1 6   ? 164.081 195.425 159.036 1.00 26.71  ? 6   PHE A CD1   1 
ATOM   39    C  CD2   . PHE A 1 6   ? 164.500 197.160 157.457 1.00 22.25  ? 6   PHE A CD2   1 
ATOM   40    C  CE1   . PHE A 1 6   ? 162.749 195.787 159.086 1.00 25.71  ? 6   PHE A CE1   1 
ATOM   41    C  CE2   . PHE A 1 6   ? 163.169 197.526 157.502 1.00 27.77  ? 6   PHE A CE2   1 
ATOM   42    C  CZ    . PHE A 1 6   ? 162.292 196.839 158.317 1.00 27.89  ? 6   PHE A CZ    1 
ATOM   43    N  N     . LEU A 1 7   ? 166.156 195.114 155.064 1.00 20.54  ? 7   LEU A N     1 
ATOM   44    C  CA    . LEU A 1 7   ? 165.357 195.104 153.842 1.00 21.46  ? 7   LEU A CA    1 
ATOM   45    C  C     . LEU A 1 7   ? 165.334 193.719 153.209 1.00 14.36  ? 7   LEU A C     1 
ATOM   46    O  O     . LEU A 1 7   ? 164.303 193.286 152.683 1.00 27.53  ? 7   LEU A O     1 
ATOM   47    C  CB    . LEU A 1 7   ? 165.897 196.137 152.853 1.00 21.71  ? 7   LEU A CB    1 
ATOM   48    C  CG    . LEU A 1 7   ? 165.567 197.601 153.150 1.00 28.82  ? 7   LEU A CG    1 
ATOM   49    C  CD1   . LEU A 1 7   ? 166.218 198.517 152.125 1.00 25.14  ? 7   LEU A CD1   1 
ATOM   50    C  CD2   . LEU A 1 7   ? 164.063 197.817 153.188 1.00 22.09  ? 7   LEU A CD2   1 
ATOM   51    N  N     . LEU A 1 8   ? 166.468 193.014 153.240 1.00 15.49  ? 8   LEU A N     1 
ATOM   52    C  CA    . LEU A 1 8   ? 166.521 191.668 152.678 1.00 18.73  ? 8   LEU A CA    1 
ATOM   53    C  C     . LEU A 1 8   ? 165.613 190.711 153.443 1.00 17.91  ? 8   LEU A C     1 
ATOM   54    O  O     . LEU A 1 8   ? 164.911 189.893 152.837 1.00 18.93  ? 8   LEU A O     1 
ATOM   55    C  CB    . LEU A 1 8   ? 167.964 191.163 152.678 1.00 19.58  ? 8   LEU A CB    1 
ATOM   56    C  CG    . LEU A 1 8   ? 168.204 189.720 152.232 1.00 22.98  ? 8   LEU A CG    1 
ATOM   57    C  CD1   . LEU A 1 8   ? 167.740 189.512 150.798 1.00 15.44  ? 8   LEU A CD1   1 
ATOM   58    C  CD2   . LEU A 1 8   ? 169.671 189.351 152.386 1.00 17.00  ? 8   LEU A CD2   1 
ATOM   59    N  N     . ILE A 1 9   ? 165.616 190.797 154.775 1.00 17.89  ? 9   ILE A N     1 
ATOM   60    C  CA    . ILE A 1 9   ? 164.756 189.934 155.579 1.00 17.27  ? 9   ILE A CA    1 
ATOM   61    C  C     . ILE A 1 9   ? 163.288 190.273 155.350 1.00 24.24  ? 9   ILE A C     1 
ATOM   62    O  O     . ILE A 1 9   ? 162.448 189.379 155.189 1.00 22.86  ? 9   ILE A O     1 
ATOM   63    C  CB    . ILE A 1 9   ? 165.134 190.041 157.068 1.00 21.88  ? 9   ILE A CB    1 
ATOM   64    C  CG1   . ILE A 1 9   ? 166.573 189.574 157.292 1.00 16.96  ? 9   ILE A CG1   1 
ATOM   65    C  CG2   . ILE A 1 9   ? 164.172 189.230 157.925 1.00 20.58  ? 9   ILE A CG2   1 
ATOM   66    C  CD1   . ILE A 1 9   ? 167.195 190.116 158.560 1.00 19.45  ? 9   ILE A CD1   1 
ATOM   67    N  N     . ALA A 1 10  ? 162.955 191.566 155.336 1.00 18.37  ? 10  ALA A N     1 
ATOM   68    C  CA    . ALA A 1 10  ? 161.564 191.973 155.160 1.00 22.65  ? 10  ALA A CA    1 
ATOM   69    C  C     . ALA A 1 10  ? 161.036 191.571 153.789 1.00 21.97  ? 10  ALA A C     1 
ATOM   70    O  O     . ALA A 1 10  ? 159.899 191.102 153.667 1.00 27.12  ? 10  ALA A O     1 
ATOM   71    C  CB    . ALA A 1 10  ? 161.429 193.481 155.366 1.00 19.49  ? 10  ALA A CB    1 
ATOM   72    N  N     . THR A 1 11  ? 161.846 191.752 152.743 1.00 21.12  ? 11  THR A N     1 
ATOM   73    C  CA    . THR A 1 11  ? 161.416 191.374 151.401 1.00 19.82  ? 11  THR A CA    1 
ATOM   74    C  C     . THR A 1 11  ? 161.215 189.867 151.288 1.00 24.98  ? 11  THR A C     1 
ATOM   75    O  O     . THR A 1 11  ? 160.248 189.407 150.671 1.00 26.62  ? 11  THR A O     1 
ATOM   76    C  CB    . THR A 1 11  ? 162.434 191.858 150.368 1.00 24.40  ? 11  THR A CB    1 
ATOM   77    O  OG1   . THR A 1 11  ? 162.623 193.272 150.510 1.00 31.07  ? 11  THR A OG1   1 
ATOM   78    C  CG2   . THR A 1 11  ? 161.949 191.559 148.957 1.00 17.28  ? 11  THR A CG2   1 
ATOM   79    N  N     . PHE A 1 12  ? 162.122 189.083 151.877 1.00 15.44  ? 12  PHE A N     1 
ATOM   80    C  CA    . PHE A 1 12  ? 161.999 187.630 151.811 1.00 18.76  ? 12  PHE A CA    1 
ATOM   81    C  C     . PHE A 1 12  ? 160.740 187.145 152.518 1.00 13.41  ? 12  PHE A C     1 
ATOM   82    O  O     . PHE A 1 12  ? 160.021 186.282 152.000 1.00 11.87  ? 12  PHE A O     1 
ATOM   83    C  CB    . PHE A 1 12  ? 163.240 186.973 152.415 1.00 13.27  ? 12  PHE A CB    1 
ATOM   84    C  CG    . PHE A 1 12  ? 163.091 185.497 152.653 1.00 15.00  ? 12  PHE A CG    1 
ATOM   85    C  CD1   . PHE A 1 12  ? 163.081 184.608 151.591 1.00 18.68  ? 12  PHE A CD1   1 
ATOM   86    C  CD2   . PHE A 1 12  ? 162.961 184.999 153.939 1.00 14.86  ? 12  PHE A CD2   1 
ATOM   87    C  CE1   . PHE A 1 12  ? 162.944 183.250 151.807 1.00 15.67  ? 12  PHE A CE1   1 
ATOM   88    C  CE2   . PHE A 1 12  ? 162.824 183.642 154.161 1.00 15.96  ? 12  PHE A CE2   1 
ATOM   89    C  CZ    . PHE A 1 12  ? 162.816 182.766 153.093 1.00 14.15  ? 12  PHE A CZ    1 
ATOM   90    N  N     . LEU A 1 13  ? 160.452 187.692 153.701 1.00 21.24  ? 13  LEU A N     1 
ATOM   91    C  CA    . LEU A 1 13  ? 159.281 187.250 154.452 1.00 15.33  ? 13  LEU A CA    1 
ATOM   92    C  C     . LEU A 1 13  ? 157.988 187.712 153.791 1.00 18.80  ? 13  LEU A C     1 
ATOM   93    O  O     . LEU A 1 13  ? 157.002 186.967 153.760 1.00 24.43  ? 13  LEU A O     1 
ATOM   94    C  CB    . LEU A 1 13  ? 159.359 187.756 155.892 1.00 20.29  ? 13  LEU A CB    1 
ATOM   95    C  CG    . LEU A 1 13  ? 160.320 187.003 156.814 1.00 24.72  ? 13  LEU A CG    1 
ATOM   96    C  CD1   . LEU A 1 13  ? 160.243 187.546 158.231 1.00 17.36  ? 13  LEU A CD1   1 
ATOM   97    C  CD2   . LEU A 1 13  ? 160.029 185.510 156.789 1.00 20.20  ? 13  LEU A CD2   1 
ATOM   98    N  N     . LEU A 1 14  ? 157.970 188.939 153.263 1.00 19.68  ? 14  LEU A N     1 
ATOM   99    C  CA    . LEU A 1 14  ? 156.757 189.454 152.635 1.00 25.45  ? 14  LEU A CA    1 
ATOM   100   C  C     . LEU A 1 14  ? 156.389 188.652 151.393 1.00 21.71  ? 14  LEU A C     1 
ATOM   101   O  O     . LEU A 1 14  ? 155.217 188.317 151.186 1.00 24.18  ? 14  LEU A O     1 
ATOM   102   C  CB    . LEU A 1 14  ? 156.933 190.932 152.287 1.00 21.14  ? 14  LEU A CB    1 
ATOM   103   C  CG    . LEU A 1 14  ? 155.768 191.593 151.547 1.00 28.75  ? 14  LEU A CG    1 
ATOM   104   C  CD1   . LEU A 1 14  ? 154.723 192.095 152.530 1.00 26.56  ? 14  LEU A CD1   1 
ATOM   105   C  CD2   . LEU A 1 14  ? 156.265 192.725 150.661 1.00 30.11  ? 14  LEU A CD2   1 
ATOM   106   N  N     . VAL A 1 15  ? 157.377 188.332 150.555 1.00 17.18  ? 15  VAL A N     1 
ATOM   107   C  CA    . VAL A 1 15  ? 157.103 187.549 149.354 1.00 22.59  ? 15  VAL A CA    1 
ATOM   108   C  C     . VAL A 1 15  ? 156.715 186.122 149.724 1.00 24.56  ? 15  VAL A C     1 
ATOM   109   O  O     . VAL A 1 15  ? 155.836 185.521 149.095 1.00 19.85  ? 15  VAL A O     1 
ATOM   110   C  CB    . VAL A 1 15  ? 158.316 187.584 148.405 1.00 18.94  ? 15  VAL A CB    1 
ATOM   111   C  CG1   . VAL A 1 15  ? 158.100 186.653 147.222 1.00 17.96  ? 15  VAL A CG1   1 
ATOM   112   C  CG2   . VAL A 1 15  ? 158.571 189.004 147.924 1.00 12.07  ? 15  VAL A CG2   1 
ATOM   113   N  N     . LEU A 1 16  ? 157.357 185.561 150.752 1.00 16.17  ? 16  LEU A N     1 
ATOM   114   C  CA    . LEU A 1 16  ? 157.042 184.197 151.169 1.00 15.03  ? 16  LEU A CA    1 
ATOM   115   C  C     . LEU A 1 16  ? 155.602 184.082 151.652 1.00 16.25  ? 16  LEU A C     1 
ATOM   116   O  O     . LEU A 1 16  ? 154.900 183.124 151.309 1.00 17.81  ? 16  LEU A O     1 
ATOM   117   C  CB    . LEU A 1 16  ? 158.012 183.747 152.261 1.00 10.21  ? 16  LEU A CB    1 
ATOM   118   C  CG    . LEU A 1 16  ? 157.616 182.497 153.050 1.00 17.08  ? 16  LEU A CG    1 
ATOM   119   C  CD1   . LEU A 1 16  ? 157.717 181.257 152.176 1.00 16.09  ? 16  LEU A CD1   1 
ATOM   120   C  CD2   . LEU A 1 16  ? 158.472 182.351 154.299 1.00 17.09  ? 16  LEU A CD2   1 
ATOM   121   N  N     . MET A 1 17  ? 155.142 185.050 152.448 1.00 20.49  ? 17  MET A N     1 
ATOM   122   C  CA    . MET A 1 17  ? 153.771 185.008 152.949 1.00 20.72  ? 17  MET A CA    1 
ATOM   123   C  C     . MET A 1 17  ? 152.762 185.161 151.818 1.00 21.63  ? 17  MET A C     1 
ATOM   124   O  O     . MET A 1 17  ? 151.699 184.530 151.837 1.00 26.08  ? 17  MET A O     1 
ATOM   125   C  CB    . MET A 1 17  ? 153.563 186.095 154.004 1.00 15.82  ? 17  MET A CB    1 
ATOM   126   C  CG    . MET A 1 17  ? 154.300 185.844 155.310 1.00 21.99  ? 17  MET A CG    1 
ATOM   127   S  SD    . MET A 1 17  ? 154.361 184.098 155.751 1.00 36.91  ? 17  MET A SD    1 
ATOM   128   C  CE    . MET A 1 17  ? 155.455 184.140 157.168 1.00 19.11  ? 17  MET A CE    1 
ATOM   129   N  N     . VAL A 1 18  ? 153.075 186.000 150.828 1.00 21.16  ? 18  VAL A N     1 
ATOM   130   C  CA    . VAL A 1 18  ? 152.163 186.209 149.707 1.00 20.11  ? 18  VAL A CA    1 
ATOM   131   C  C     . VAL A 1 18  ? 151.991 184.922 148.910 1.00 21.91  ? 18  VAL A C     1 
ATOM   132   O  O     . VAL A 1 18  ? 150.877 184.569 148.506 1.00 29.12  ? 18  VAL A O     1 
ATOM   133   C  CB    . VAL A 1 18  ? 152.664 187.367 148.822 1.00 22.66  ? 18  VAL A CB    1 
ATOM   134   C  CG1   . VAL A 1 18  ? 151.994 187.333 147.458 1.00 18.15  ? 18  VAL A CG1   1 
ATOM   135   C  CG2   . VAL A 1 18  ? 152.415 188.701 149.508 1.00 20.92  ? 18  VAL A CG2   1 
ATOM   136   N  N     . LEU A 1 19  ? 153.088 184.201 148.669 1.00 20.98  ? 19  LEU A N     1 
ATOM   137   C  CA    . LEU A 1 19  ? 153.020 182.972 147.886 1.00 20.08  ? 19  LEU A CA    1 
ATOM   138   C  C     . LEU A 1 19  ? 152.458 181.799 148.681 1.00 23.54  ? 19  LEU A C     1 
ATOM   139   O  O     . LEU A 1 19  ? 151.787 180.935 148.107 1.00 22.05  ? 19  LEU A O     1 
ATOM   140   C  CB    . LEU A 1 19  ? 154.407 182.614 147.350 1.00 21.25  ? 19  LEU A CB    1 
ATOM   141   C  CG    . LEU A 1 19  ? 154.961 183.505 146.238 1.00 28.30  ? 19  LEU A CG    1 
ATOM   142   C  CD1   . LEU A 1 19  ? 156.434 183.210 146.002 1.00 25.55  ? 19  LEU A CD1   1 
ATOM   143   C  CD2   . LEU A 1 19  ? 154.162 183.324 144.958 1.00 20.80  ? 19  LEU A CD2   1 
ATOM   144   N  N     . ALA A 1 20  ? 152.719 181.746 149.990 1.00 19.77  ? 20  ALA A N     1 
ATOM   145   C  CA    . ALA A 1 20  ? 152.346 180.569 150.769 1.00 17.46  ? 20  ALA A CA    1 
ATOM   146   C  C     . ALA A 1 20  ? 150.848 180.507 151.040 1.00 21.67  ? 20  ALA A C     1 
ATOM   147   O  O     . ALA A 1 20  ? 150.298 179.411 151.195 1.00 25.30  ? 20  ALA A O     1 
ATOM   148   C  CB    . ALA A 1 20  ? 153.120 180.543 152.086 1.00 6.37   ? 20  ALA A CB    1 
ATOM   149   N  N     . ARG A 1 21  ? 150.176 181.656 151.114 1.00 21.89  ? 21  ARG A N     1 
ATOM   150   C  CA    . ARG A 1 21  ? 148.747 181.655 151.424 1.00 24.94  ? 21  ARG A CA    1 
ATOM   151   C  C     . ARG A 1 21  ? 147.908 180.937 150.371 1.00 22.78  ? 21  ARG A C     1 
ATOM   152   O  O     . ARG A 1 21  ? 147.082 180.090 150.753 1.00 28.13  ? 21  ARG A O     1 
ATOM   153   C  CB    . ARG A 1 21  ? 148.267 183.094 151.647 1.00 32.17  ? 21  ARG A CB    1 
ATOM   154   C  CG    . ARG A 1 21  ? 146.957 183.199 152.408 1.00 30.27  ? 21  ARG A CG    1 
ATOM   155   C  CD    . ARG A 1 21  ? 147.125 184.002 153.686 1.00 34.67  ? 21  ARG A CD    1 
ATOM   156   N  NE    . ARG A 1 21  ? 147.031 185.437 153.446 1.00 37.89  ? 21  ARG A NE    1 
ATOM   157   C  CZ    . ARG A 1 21  ? 145.892 186.107 153.340 1.00 40.78  ? 21  ARG A CZ    1 
ATOM   158   N  NH1   . ARG A 1 21  ? 144.721 185.501 153.450 1.00 32.56  ? 21  ARG A NH1   1 
ATOM   159   N  NH2   . ARG A 1 21  ? 145.928 187.418 153.119 1.00 38.41  ? 21  ARG A NH2   1 
ATOM   160   N  N     . PRO A 1 22  ? 148.039 181.213 149.066 1.00 24.19  ? 22  PRO A N     1 
ATOM   161   C  CA    . PRO A 1 22  ? 147.286 180.410 148.087 1.00 26.96  ? 22  PRO A CA    1 
ATOM   162   C  C     . PRO A 1 22  ? 147.651 178.938 148.108 1.00 25.39  ? 22  PRO A C     1 
ATOM   163   O  O     . PRO A 1 22  ? 146.779 178.089 147.882 1.00 26.31  ? 22  PRO A O     1 
ATOM   164   C  CB    . PRO A 1 22  ? 147.647 181.062 146.744 1.00 24.66  ? 22  PRO A CB    1 
ATOM   165   C  CG    . PRO A 1 22  ? 148.103 182.429 147.093 1.00 23.68  ? 22  PRO A CG    1 
ATOM   166   C  CD    . PRO A 1 22  ? 148.805 182.280 148.401 1.00 20.48  ? 22  PRO A CD    1 
ATOM   167   N  N     . LEU A 1 23  ? 148.918 178.608 148.369 1.00 16.08  ? 23  LEU A N     1 
ATOM   168   C  CA    . LEU A 1 23  ? 149.313 177.206 148.447 1.00 17.11  ? 23  LEU A CA    1 
ATOM   169   C  C     . LEU A 1 23  ? 148.705 176.522 149.664 1.00 18.63  ? 23  LEU A C     1 
ATOM   170   O  O     . LEU A 1 23  ? 148.392 175.328 149.609 1.00 19.28  ? 23  LEU A O     1 
ATOM   171   C  CB    . LEU A 1 23  ? 150.837 177.087 148.472 1.00 21.81  ? 23  LEU A CB    1 
ATOM   172   C  CG    . LEU A 1 23  ? 151.403 175.676 148.299 1.00 15.25  ? 23  LEU A CG    1 
ATOM   173   C  CD1   . LEU A 1 23  ? 150.824 175.012 147.060 1.00 23.87  ? 23  LEU A CD1   1 
ATOM   174   C  CD2   . LEU A 1 23  ? 152.921 175.710 148.233 1.00 24.11  ? 23  LEU A CD2   1 
ATOM   175   N  N     . GLY A 1 24  ? 148.533 177.257 150.764 1.00 20.09  ? 24  GLY A N     1 
ATOM   176   C  CA    . GLY A 1 24  ? 147.881 176.683 151.930 1.00 19.47  ? 24  GLY A CA    1 
ATOM   177   C  C     . GLY A 1 24  ? 146.445 176.279 151.654 1.00 19.07  ? 24  GLY A C     1 
ATOM   178   O  O     . GLY A 1 24  ? 145.976 175.248 152.141 1.00 28.28  ? 24  GLY A O     1 
ATOM   179   N  N     . SER A 1 25  ? 145.727 177.089 150.873 1.00 24.81  ? 25  SER A N     1 
ATOM   180   C  CA    . SER A 1 25  ? 144.360 176.737 150.501 1.00 22.56  ? 25  SER A CA    1 
ATOM   181   C  C     . SER A 1 25  ? 144.329 175.463 149.666 1.00 24.30  ? 25  SER A C     1 
ATOM   182   O  O     . SER A 1 25  ? 143.449 174.613 149.850 1.00 29.67  ? 25  SER A O     1 
ATOM   183   C  CB    . SER A 1 25  ? 143.707 177.893 149.744 1.00 21.88  ? 25  SER A CB    1 
ATOM   184   O  OG    . SER A 1 25  ? 143.417 178.971 150.615 1.00 35.84  ? 25  SER A OG    1 
ATOM   185   N  N     . GLY A 1 26  ? 145.275 175.317 148.736 1.00 24.60  ? 26  GLY A N     1 
ATOM   186   C  CA    . GLY A 1 26  ? 145.350 174.092 147.959 1.00 16.40  ? 26  GLY A CA    1 
ATOM   187   C  C     . GLY A 1 26  ? 145.702 172.883 148.806 1.00 23.69  ? 26  GLY A C     1 
ATOM   188   O  O     . GLY A 1 26  ? 145.135 171.802 148.625 1.00 29.24  ? 26  GLY A O     1 
ATOM   189   N  N     . LEU A 1 27  ? 146.641 173.048 149.741 1.00 16.56  ? 27  LEU A N     1 
ATOM   190   C  CA    . LEU A 1 27  ? 146.999 171.949 150.632 1.00 21.00  ? 27  LEU A CA    1 
ATOM   191   C  C     . LEU A 1 27  ? 145.852 171.588 151.565 1.00 16.70  ? 27  LEU A C     1 
ATOM   192   O  O     . LEU A 1 27  ? 145.708 170.420 151.943 1.00 28.14  ? 27  LEU A O     1 
ATOM   193   C  CB    . LEU A 1 27  ? 148.246 172.308 151.440 1.00 17.95  ? 27  LEU A CB    1 
ATOM   194   C  CG    . LEU A 1 27  ? 149.554 172.437 150.658 1.00 19.99  ? 27  LEU A CG    1 
ATOM   195   C  CD1   . LEU A 1 27  ? 150.672 172.931 151.563 1.00 16.52  ? 27  LEU A CD1   1 
ATOM   196   C  CD2   . LEU A 1 27  ? 149.927 171.114 150.011 1.00 19.33  ? 27  LEU A CD2   1 
ATOM   197   N  N     . ALA A 1 28  ? 145.033 172.570 151.949 1.00 20.09  ? 28  ALA A N     1 
ATOM   198   C  CA    . ALA A 1 28  ? 143.881 172.287 152.799 1.00 21.31  ? 28  ALA A CA    1 
ATOM   199   C  C     . ALA A 1 28  ? 142.886 171.376 152.091 1.00 22.48  ? 28  ALA A C     1 
ATOM   200   O  O     . ALA A 1 28  ? 142.263 170.515 152.724 1.00 26.23  ? 28  ALA A O     1 
ATOM   201   C  CB    . ALA A 1 28  ? 143.209 173.592 153.226 1.00 20.66  ? 28  ALA A CB    1 
ATOM   202   N  N     . ARG A 1 29  ? 142.717 171.556 150.779 1.00 18.11  ? 29  ARG A N     1 
ATOM   203   C  CA    . ARG A 1 29  ? 141.832 170.681 150.017 1.00 24.77  ? 29  ARG A CA    1 
ATOM   204   C  C     . ARG A 1 29  ? 142.330 169.241 150.036 1.00 25.91  ? 29  ARG A C     1 
ATOM   205   O  O     . ARG A 1 29  ? 141.535 168.303 150.164 1.00 32.22  ? 29  ARG A O     1 
ATOM   206   C  CB    . ARG A 1 29  ? 141.706 171.185 148.580 1.00 26.96  ? 29  ARG A CB    1 
ATOM   207   C  CG    . ARG A 1 29  ? 140.570 172.167 148.363 1.00 29.24  ? 29  ARG A CG    1 
ATOM   208   C  CD    . ARG A 1 29  ? 140.554 172.678 146.933 1.00 30.22  ? 29  ARG A CD    1 
ATOM   209   N  NE    . ARG A 1 29  ? 139.373 173.486 146.653 1.00 37.81  ? 29  ARG A NE    1 
ATOM   210   C  CZ    . ARG A 1 29  ? 138.467 173.193 145.731 1.00 36.25  ? 29  ARG A CZ    1 
ATOM   211   N  NH1   . ARG A 1 29  ? 138.573 172.112 144.976 1.00 33.98  ? 29  ARG A NH1   1 
ATOM   212   N  NH2   . ARG A 1 29  ? 137.427 174.005 145.563 1.00 35.99  ? 29  ARG A NH2   1 
ATOM   213   N  N     . LEU A 1 30  ? 143.644 169.046 149.900 1.00 20.89  ? 30  LEU A N     1 
ATOM   214   C  CA    . LEU A 1 30  ? 144.205 167.700 149.963 1.00 20.41  ? 30  LEU A CA    1 
ATOM   215   C  C     . LEU A 1 30  ? 144.024 167.089 151.347 1.00 20.40  ? 30  LEU A C     1 
ATOM   216   O  O     . LEU A 1 30  ? 143.748 165.890 151.471 1.00 25.09  ? 30  LEU A O     1 
ATOM   217   C  CB    . LEU A 1 30  ? 145.683 167.728 149.573 1.00 18.95  ? 30  LEU A CB    1 
ATOM   218   C  CG    . LEU A 1 30  ? 146.010 168.300 148.192 1.00 21.31  ? 30  LEU A CG    1 
ATOM   219   C  CD1   . LEU A 1 30  ? 147.489 168.138 147.879 1.00 22.51  ? 30  LEU A CD1   1 
ATOM   220   C  CD2   . LEU A 1 30  ? 145.156 167.642 147.119 1.00 22.23  ? 30  LEU A CD2   1 
ATOM   221   N  N     . ILE A 1 31  ? 144.186 167.894 152.400 1.00 22.40  ? 31  ILE A N     1 
ATOM   222   C  CA    . ILE A 1 31  ? 143.976 167.397 153.757 1.00 17.29  ? 31  ILE A CA    1 
ATOM   223   C  C     . ILE A 1 31  ? 142.518 167.009 153.963 1.00 22.16  ? 31  ILE A C     1 
ATOM   224   O  O     . ILE A 1 31  ? 142.214 165.966 154.556 1.00 24.52  ? 31  ILE A O     1 
ATOM   225   C  CB    . ILE A 1 31  ? 144.437 168.444 154.788 1.00 25.95  ? 31  ILE A CB    1 
ATOM   226   C  CG1   . ILE A 1 31  ? 145.946 168.670 154.677 1.00 20.91  ? 31  ILE A CG1   1 
ATOM   227   C  CG2   . ILE A 1 31  ? 144.071 168.006 156.198 1.00 20.08  ? 31  ILE A CG2   1 
ATOM   228   C  CD1   . ILE A 1 31  ? 146.429 169.924 155.369 1.00 18.71  ? 31  ILE A CD1   1 
ATOM   229   N  N     . ASN A 1 32  ? 141.594 167.832 153.471 1.00 26.38  ? 32  ASN A N     1 
ATOM   230   C  CA    . ASN A 1 32  ? 140.166 167.573 153.595 1.00 25.13  ? 32  ASN A CA    1 
ATOM   231   C  C     . ASN A 1 32  ? 139.659 166.540 152.595 1.00 25.75  ? 32  ASN A C     1 
ATOM   232   O  O     . ASN A 1 32  ? 138.441 166.364 152.479 1.00 36.25  ? 32  ASN A O     1 
ATOM   233   C  CB    . ASN A 1 32  ? 139.380 168.877 153.432 1.00 23.83  ? 32  ASN A CB    1 
ATOM   234   C  CG    . ASN A 1 32  ? 139.467 169.766 154.655 1.00 23.42  ? 32  ASN A CG    1 
ATOM   235   O  OD1   . ASN A 1 32  ? 139.500 169.284 155.786 1.00 31.53  ? 32  ASN A OD1   1 
ATOM   236   N  ND2   . ASN A 1 32  ? 139.501 171.075 154.433 1.00 27.69  ? 32  ASN A ND2   1 
ATOM   237   N  N     . ASP A 1 33  ? 140.560 165.866 151.876 1.00 32.40  ? 33  ASP A N     1 
ATOM   238   C  CA    . ASP A 1 33  ? 140.203 164.849 150.885 1.00 29.16  ? 33  ASP A CA    1 
ATOM   239   C  C     . ASP A 1 33  ? 139.296 165.415 149.796 1.00 30.90  ? 33  ASP A C     1 
ATOM   240   O  O     . ASP A 1 33  ? 138.417 164.722 149.278 1.00 37.22  ? 33  ASP A O     1 
ATOM   241   C  CB    . ASP A 1 33  ? 139.555 163.629 151.549 1.00 34.87  ? 33  ASP A CB    1 
ATOM   242   C  CG    . ASP A 1 33  ? 139.611 162.390 150.677 1.00 41.18  ? 33  ASP A CG    1 
ATOM   243   O  OD1   . ASP A 1 33  ? 140.728 161.912 150.392 1.00 44.64  ? 33  ASP A OD1   1 
ATOM   244   O  OD2   . ASP A 1 33  ? 138.537 161.894 150.277 1.00 42.48  ? 33  ASP A OD2   1 
ATOM   245   N  N     . ILE A 1 34  ? 139.500 166.679 149.442 1.00 30.94  ? 34  ILE A N     1 
ATOM   246   C  CA    . ILE A 1 34  ? 138.767 167.343 148.372 1.00 31.09  ? 34  ILE A CA    1 
ATOM   247   C  C     . ILE A 1 34  ? 139.711 167.468 147.177 1.00 38.85  ? 34  ILE A C     1 
ATOM   248   O  O     . ILE A 1 34  ? 140.731 168.167 147.268 1.00 40.23  ? 34  ILE A O     1 
ATOM   249   C  CB    . ILE A 1 34  ? 138.234 168.713 148.810 1.00 33.87  ? 34  ILE A CB    1 
ATOM   250   C  CG1   . ILE A 1 34  ? 137.124 168.545 149.848 1.00 32.18  ? 34  ILE A CG1   1 
ATOM   251   C  CG2   . ILE A 1 34  ? 137.725 169.496 147.609 1.00 34.36  ? 34  ILE A CG2   1 
ATOM   252   C  CD1   . ILE A 1 34  ? 136.920 169.759 150.725 1.00 34.95  ? 34  ILE A CD1   1 
ATOM   253   N  N     . PRO A 1 35  ? 139.429 166.808 146.055 1.00 39.61  ? 35  PRO A N     1 
ATOM   254   C  CA    . PRO A 1 35  ? 140.338 166.887 144.907 1.00 38.38  ? 35  PRO A CA    1 
ATOM   255   C  C     . PRO A 1 35  ? 140.430 168.302 144.357 1.00 37.41  ? 35  PRO A C     1 
ATOM   256   O  O     . PRO A 1 35  ? 139.466 169.070 144.386 1.00 41.91  ? 35  PRO A O     1 
ATOM   257   C  CB    . PRO A 1 35  ? 139.710 165.929 143.888 1.00 36.84  ? 35  PRO A CB    1 
ATOM   258   C  CG    . PRO A 1 35  ? 138.273 165.845 144.281 1.00 36.99  ? 35  PRO A CG    1 
ATOM   259   C  CD    . PRO A 1 35  ? 138.249 165.973 145.775 1.00 36.33  ? 35  PRO A CD    1 
ATOM   260   N  N     . LEU A 1 36  ? 141.614 168.641 143.855 1.00 38.63  ? 36  LEU A N     1 
ATOM   261   C  CA    . LEU A 1 36  ? 141.818 169.942 143.245 1.00 37.40  ? 36  LEU A CA    1 
ATOM   262   C  C     . LEU A 1 36  ? 140.999 170.050 141.958 1.00 42.26  ? 36  LEU A C     1 
ATOM   263   O  O     . LEU A 1 36  ? 140.735 169.042 141.297 1.00 44.91  ? 36  LEU A O     1 
ATOM   264   C  CB    . LEU A 1 36  ? 143.298 170.165 142.947 1.00 33.79  ? 36  LEU A CB    1 
ATOM   265   C  CG    . LEU A 1 36  ? 144.235 170.153 144.158 1.00 36.89  ? 36  LEU A CG    1 
ATOM   266   C  CD1   . LEU A 1 36  ? 145.686 170.270 143.719 1.00 39.22  ? 36  LEU A CD1   1 
ATOM   267   C  CD2   . LEU A 1 36  ? 143.876 171.266 145.130 1.00 37.21  ? 36  LEU A CD2   1 
ATOM   268   N  N     . PRO A 1 37  ? 140.569 171.259 141.593 1.00 42.30  ? 37  PRO A N     1 
ATOM   269   C  CA    . PRO A 1 37  ? 139.758 171.411 140.379 1.00 41.25  ? 37  PRO A CA    1 
ATOM   270   C  C     . PRO A 1 37  ? 140.511 170.949 139.140 1.00 40.10  ? 37  PRO A C     1 
ATOM   271   O  O     . PRO A 1 37  ? 141.715 171.174 139.000 1.00 39.43  ? 37  PRO A O     1 
ATOM   272   C  CB    . PRO A 1 37  ? 139.463 172.916 140.332 1.00 39.47  ? 37  PRO A CB    1 
ATOM   273   C  CG    . PRO A 1 37  ? 140.483 173.546 141.224 1.00 39.02  ? 37  PRO A CG    1 
ATOM   274   C  CD    . PRO A 1 37  ? 140.773 172.540 142.289 1.00 40.00  ? 37  PRO A CD    1 
ATOM   275   N  N     . GLY A 1 38  ? 139.784 170.294 138.238 1.00 43.31  ? 38  GLY A N     1 
ATOM   276   C  CA    . GLY A 1 38  ? 140.358 169.782 137.013 1.00 41.32  ? 38  GLY A CA    1 
ATOM   277   C  C     . GLY A 1 38  ? 141.088 168.463 137.141 1.00 43.52  ? 38  GLY A C     1 
ATOM   278   O  O     . GLY A 1 38  ? 141.620 167.973 136.137 1.00 50.47  ? 38  GLY A O     1 
ATOM   279   N  N     . THR A 1 39  ? 141.132 167.871 138.333 1.00 38.04  ? 39  THR A N     1 
ATOM   280   C  CA    . THR A 1 39  ? 141.835 166.615 138.555 1.00 39.40  ? 39  THR A CA    1 
ATOM   281   C  C     . THR A 1 39  ? 140.909 165.466 138.928 1.00 37.40  ? 39  THR A C     1 
ATOM   282   O  O     . THR A 1 39  ? 141.384 164.337 139.088 1.00 41.13  ? 39  THR A O     1 
ATOM   283   C  CB    . THR A 1 39  ? 142.899 166.786 139.648 1.00 36.91  ? 39  THR A CB    1 
ATOM   284   O  OG1   . THR A 1 39  ? 142.261 166.902 140.926 1.00 43.31  ? 39  THR A OG1   1 
ATOM   285   C  CG2   . THR A 1 39  ? 143.736 168.029 139.390 1.00 39.02  ? 39  THR A CG2   1 
ATOM   286   N  N     . THR A 1 40  ? 139.606 165.720 139.077 1.00 43.00  ? 40  THR A N     1 
ATOM   287   C  CA    . THR A 1 40  ? 138.684 164.657 139.467 1.00 41.41  ? 40  THR A CA    1 
ATOM   288   C  C     . THR A 1 40  ? 138.613 163.565 138.407 1.00 41.34  ? 40  THR A C     1 
ATOM   289   O  O     . THR A 1 40  ? 138.604 162.372 138.733 1.00 43.83  ? 40  THR A O     1 
ATOM   290   C  CB    . THR A 1 40  ? 137.294 165.236 139.730 1.00 42.25  ? 40  THR A CB    1 
ATOM   291   O  OG1   . THR A 1 40  ? 137.417 166.480 140.430 1.00 45.55  ? 40  THR A OG1   1 
ATOM   292   C  CG2   . THR A 1 40  ? 136.467 164.271 140.565 1.00 40.85  ? 40  THR A CG2   1 
ATOM   293   N  N     . GLY A 1 41  ? 138.555 163.952 137.131 1.00 40.68  ? 41  GLY A N     1 
ATOM   294   C  CA    . GLY A 1 41  ? 138.487 162.959 136.071 1.00 38.22  ? 41  GLY A CA    1 
ATOM   295   C  C     . GLY A 1 41  ? 139.753 162.132 135.954 1.00 40.84  ? 41  GLY A C     1 
ATOM   296   O  O     . GLY A 1 41  ? 139.694 160.913 135.769 1.00 43.34  ? 41  GLY A O     1 
ATOM   297   N  N     . VAL A 1 42  ? 140.915 162.780 136.057 1.00 38.22  ? 42  VAL A N     1 
ATOM   298   C  CA    . VAL A 1 42  ? 142.181 162.063 135.936 1.00 36.50  ? 42  VAL A CA    1 
ATOM   299   C  C     . VAL A 1 42  ? 142.396 161.144 137.132 1.00 39.03  ? 42  VAL A C     1 
ATOM   300   O  O     . VAL A 1 42  ? 142.902 160.024 136.987 1.00 42.03  ? 42  VAL A O     1 
ATOM   301   C  CB    . VAL A 1 42  ? 143.343 163.058 135.772 1.00 42.17  ? 42  VAL A CB    1 
ATOM   302   C  CG1   . VAL A 1 42  ? 144.537 162.376 135.123 1.00 35.19  ? 42  VAL A CG1   1 
ATOM   303   C  CG2   . VAL A 1 42  ? 142.900 164.262 134.955 1.00 41.73  ? 42  VAL A CG2   1 
ATOM   304   N  N     . GLU A 1 43  ? 142.023 161.600 138.331 1.00 36.88  ? 43  GLU A N     1 
ATOM   305   C  CA    . GLU A 1 43  ? 142.248 160.802 139.532 1.00 38.26  ? 43  GLU A CA    1 
ATOM   306   C  C     . GLU A 1 43  ? 141.436 159.512 139.508 1.00 38.13  ? 43  GLU A C     1 
ATOM   307   O  O     . GLU A 1 43  ? 141.925 158.457 139.928 1.00 38.90  ? 43  GLU A O     1 
ATOM   308   C  CB    . GLU A 1 43  ? 141.912 161.621 140.778 1.00 36.16  ? 43  GLU A CB    1 
ATOM   309   C  CG    . GLU A 1 43  ? 143.050 162.501 141.266 1.00 34.84  ? 43  GLU A CG    1 
ATOM   310   C  CD    . GLU A 1 43  ? 142.672 163.317 142.485 1.00 40.76  ? 43  GLU A CD    1 
ATOM   311   O  OE1   . GLU A 1 43  ? 141.699 162.945 143.173 1.00 42.14  ? 43  GLU A OE1   1 
ATOM   312   O  OE2   . GLU A 1 43  ? 143.348 164.332 142.754 1.00 47.18  ? 43  GLU A OE2   1 
ATOM   313   N  N     . ARG A 1 44  ? 140.193 159.578 139.026 1.00 43.03  ? 44  ARG A N     1 
ATOM   314   C  CA    . ARG A 1 44  ? 139.346 158.388 139.002 1.00 43.64  ? 44  ARG A CA    1 
ATOM   315   C  C     . ARG A 1 44  ? 139.937 157.303 138.111 1.00 42.81  ? 44  ARG A C     1 
ATOM   316   O  O     . ARG A 1 44  ? 139.947 156.123 138.479 1.00 43.06  ? 44  ARG A O     1 
ATOM   317   C  CB    . ARG A 1 44  ? 137.938 158.757 138.537 1.00 43.47  ? 44  ARG A CB    1 
ATOM   318   C  CG    . ARG A 1 44  ? 136.911 157.653 138.728 1.00 45.58  ? 44  ARG A CG    1 
ATOM   319   C  CD    . ARG A 1 44  ? 135.828 157.711 137.662 1.00 47.16  ? 44  ARG A CD    1 
ATOM   320   N  NE    . ARG A 1 44  ? 135.802 158.998 136.976 1.00 47.82  ? 44  ARG A NE    1 
ATOM   321   C  CZ    . ARG A 1 44  ? 135.806 159.144 135.659 1.00 47.82  ? 44  ARG A CZ    1 
ATOM   322   N  NH1   . ARG A 1 44  ? 135.836 158.100 134.847 1.00 46.14  ? 44  ARG A NH1   1 
ATOM   323   N  NH2   . ARG A 1 44  ? 135.780 160.370 135.142 1.00 47.17  ? 44  ARG A NH2   1 
ATOM   324   N  N     . VAL A 1 45  ? 140.436 157.683 136.933 1.00 38.96  ? 45  VAL A N     1 
ATOM   325   C  CA    . VAL A 1 45  ? 141.036 156.705 136.033 1.00 38.43  ? 45  VAL A CA    1 
ATOM   326   C  C     . VAL A 1 45  ? 142.365 156.207 136.589 1.00 42.02  ? 45  VAL A C     1 
ATOM   327   O  O     . VAL A 1 45  ? 142.643 155.001 136.584 1.00 44.84  ? 45  VAL A O     1 
ATOM   328   C  CB    . VAL A 1 45  ? 141.197 157.311 134.626 1.00 38.64  ? 45  VAL A CB    1 
ATOM   329   C  CG1   . VAL A 1 45  ? 142.290 156.592 133.849 1.00 41.01  ? 45  VAL A CG1   1 
ATOM   330   C  CG2   . VAL A 1 45  ? 139.876 157.257 133.873 1.00 39.47  ? 45  VAL A CG2   1 
ATOM   331   N  N     . LEU A 1 46  ? 143.203 157.122 137.083 1.00 34.11  ? 46  LEU A N     1 
ATOM   332   C  CA    . LEU A 1 46  ? 144.527 156.738 137.565 1.00 30.38  ? 46  LEU A CA    1 
ATOM   333   C  C     . LEU A 1 46  ? 144.442 155.838 138.793 1.00 32.92  ? 46  LEU A C     1 
ATOM   334   O  O     . LEU A 1 46  ? 145.178 154.850 138.894 1.00 34.43  ? 46  LEU A O     1 
ATOM   335   C  CB    . LEU A 1 46  ? 145.354 157.985 137.874 1.00 32.83  ? 46  LEU A CB    1 
ATOM   336   C  CG    . LEU A 1 46  ? 146.727 157.733 138.498 1.00 30.17  ? 46  LEU A CG    1 
ATOM   337   C  CD1   . LEU A 1 46  ? 147.645 157.038 137.505 1.00 32.13  ? 46  LEU A CD1   1 
ATOM   338   C  CD2   . LEU A 1 46  ? 147.341 159.034 138.984 1.00 31.61  ? 46  LEU A CD2   1 
ATOM   339   N  N     . PHE A 1 47  ? 143.557 156.166 139.738 1.00 35.67  ? 47  PHE A N     1 
ATOM   340   C  CA    . PHE A 1 47  ? 143.466 155.382 140.967 1.00 34.50  ? 47  PHE A CA    1 
ATOM   341   C  C     . PHE A 1 47  ? 143.010 153.957 140.682 1.00 31.66  ? 47  PHE A C     1 
ATOM   342   O  O     . PHE A 1 47  ? 143.501 153.005 141.302 1.00 37.58  ? 47  PHE A O     1 
ATOM   343   C  CB    . PHE A 1 47  ? 142.521 156.062 141.958 1.00 36.18  ? 47  PHE A CB    1 
ATOM   344   C  CG    . PHE A 1 47  ? 143.083 157.313 142.575 1.00 33.95  ? 47  PHE A CG    1 
ATOM   345   C  CD1   . PHE A 1 47  ? 144.422 157.637 142.426 1.00 34.37  ? 47  PHE A CD1   1 
ATOM   346   C  CD2   . PHE A 1 47  ? 142.271 158.165 143.305 1.00 32.09  ? 47  PHE A CD2   1 
ATOM   347   C  CE1   . PHE A 1 47  ? 144.939 158.787 142.991 1.00 33.65  ? 47  PHE A CE1   1 
ATOM   348   C  CE2   . PHE A 1 47  ? 142.783 159.316 143.873 1.00 33.17  ? 47  PHE A CE2   1 
ATOM   349   C  CZ    . PHE A 1 47  ? 144.119 159.627 143.716 1.00 33.63  ? 47  PHE A CZ    1 
ATOM   350   N  N     . ARG A 1 48  ? 142.065 153.790 139.755 1.00 34.09  ? 48  ARG A N     1 
ATOM   351   C  CA    . ARG A 1 48  ? 141.621 152.449 139.385 1.00 37.52  ? 48  ARG A CA    1 
ATOM   352   C  C     . ARG A 1 48  ? 142.743 151.656 138.725 1.00 39.23  ? 48  ARG A C     1 
ATOM   353   O  O     . ARG A 1 48  ? 142.902 150.459 138.990 1.00 42.66  ? 48  ARG A O     1 
ATOM   354   C  CB    . ARG A 1 48  ? 140.408 152.536 138.459 1.00 41.33  ? 48  ARG A CB    1 
ATOM   355   C  CG    . ARG A 1 48  ? 139.584 151.260 138.397 1.00 41.46  ? 48  ARG A CG    1 
ATOM   356   C  CD    . ARG A 1 48  ? 138.258 151.488 137.687 1.00 42.07  ? 48  ARG A CD    1 
ATOM   357   N  NE    . ARG A 1 48  ? 138.340 152.557 136.699 1.00 46.06  ? 48  ARG A NE    1 
ATOM   358   C  CZ    . ARG A 1 48  ? 137.594 153.653 136.715 1.00 48.60  ? 48  ARG A CZ    1 
ATOM   359   N  NH1   . ARG A 1 48  ? 136.693 153.861 137.661 1.00 46.51  ? 48  ARG A NH1   1 
ATOM   360   N  NH2   . ARG A 1 48  ? 137.756 154.563 135.759 1.00 45.70  ? 48  ARG A NH2   1 
ATOM   361   N  N     . ALA A 1 49  ? 143.527 152.306 137.861 1.00 36.91  ? 49  ALA A N     1 
ATOM   362   C  CA    . ALA A 1 49  ? 144.623 151.616 137.186 1.00 34.13  ? 49  ALA A CA    1 
ATOM   363   C  C     . ALA A 1 49  ? 145.689 151.162 138.176 1.00 35.12  ? 49  ALA A C     1 
ATOM   364   O  O     . ALA A 1 49  ? 146.248 150.068 138.035 1.00 40.29  ? 49  ALA A O     1 
ATOM   365   C  CB    . ALA A 1 49  ? 145.233 152.520 136.117 1.00 34.26  ? 49  ALA A CB    1 
ATOM   366   N  N     . LEU A 1 50  ? 145.983 151.984 139.180 1.00 32.12  ? 50  LEU A N     1 
ATOM   367   C  CA    . LEU A 1 50  ? 146.989 151.662 140.183 1.00 30.40  ? 50  LEU A CA    1 
ATOM   368   C  C     . LEU A 1 50  ? 146.446 150.800 141.313 1.00 32.63  ? 50  LEU A C     1 
ATOM   369   O  O     . LEU A 1 50  ? 147.205 150.445 142.221 1.00 39.41  ? 50  LEU A O     1 
ATOM   370   C  CB    . LEU A 1 50  ? 147.587 152.949 140.761 1.00 30.39  ? 50  LEU A CB    1 
ATOM   371   C  CG    . LEU A 1 50  ? 148.325 153.858 139.777 1.00 32.39  ? 50  LEU A CG    1 
ATOM   372   C  CD1   . LEU A 1 50  ? 148.858 155.092 140.486 1.00 31.50  ? 50  LEU A CD1   1 
ATOM   373   C  CD2   . LEU A 1 50  ? 149.451 153.103 139.089 1.00 29.56  ? 50  LEU A CD2   1 
ATOM   374   N  N     . GLY A 1 51  ? 145.164 150.455 141.281 1.00 34.59  ? 51  GLY A N     1 
ATOM   375   C  CA    . GLY A 1 51  ? 144.572 149.650 142.335 1.00 30.01  ? 51  GLY A CA    1 
ATOM   376   C  C     . GLY A 1 51  ? 144.487 150.344 143.676 1.00 37.27  ? 51  GLY A C     1 
ATOM   377   O  O     . GLY A 1 51  ? 144.672 149.699 144.717 1.00 35.53  ? 51  GLY A O     1 
ATOM   378   N  N     . VAL A 1 52  ? 144.212 151.644 143.680 1.00 38.61  ? 52  VAL A N     1 
ATOM   379   C  CA    . VAL A 1 52  ? 144.017 152.414 144.903 1.00 37.76  ? 52  VAL A CA    1 
ATOM   380   C  C     . VAL A 1 52  ? 142.548 152.807 144.966 1.00 39.53  ? 52  VAL A C     1 
ATOM   381   O  O     . VAL A 1 52  ? 142.064 153.567 144.119 1.00 42.72  ? 52  VAL A O     1 
ATOM   382   C  CB    . VAL A 1 52  ? 144.926 153.651 144.950 1.00 38.59  ? 52  VAL A CB    1 
ATOM   383   C  CG1   . VAL A 1 52  ? 144.633 154.474 146.192 1.00 43.19  ? 52  VAL A CG1   1 
ATOM   384   C  CG2   . VAL A 1 52  ? 146.389 153.237 144.910 1.00 34.71  ? 52  VAL A CG2   1 
ATOM   385   N  N     . SER A 1 53  ? 141.840 152.290 145.968 1.00 48.16  ? 53  SER A N     1 
ATOM   386   C  CA    . SER A 1 53  ? 140.404 152.491 146.100 1.00 45.59  ? 53  SER A CA    1 
ATOM   387   C  C     . SER A 1 53  ? 140.049 153.566 147.117 1.00 46.01  ? 53  SER A C     1 
ATOM   388   O  O     . SER A 1 53  ? 138.878 153.677 147.498 1.00 49.92  ? 53  SER A O     1 
ATOM   389   C  CB    . SER A 1 53  ? 139.724 151.174 146.476 1.00 49.06  ? 53  SER A CB    1 
ATOM   390   O  OG    . SER A 1 53  ? 140.482 150.468 147.443 1.00 51.07  ? 53  SER A OG    1 
ATOM   391   N  N     . ASP A 1 54  ? 141.029 154.353 147.566 1.00 44.20  ? 54  ASP A N     1 
ATOM   392   C  CA    . ASP A 1 54  ? 140.820 155.390 148.578 1.00 45.24  ? 54  ASP A CA    1 
ATOM   393   C  C     . ASP A 1 54  ? 140.227 154.812 149.860 1.00 47.48  ? 54  ASP A C     1 
ATOM   394   O  O     . ASP A 1 54  ? 139.451 155.475 150.552 1.00 44.12  ? 54  ASP A O     1 
ATOM   395   C  CB    . ASP A 1 54  ? 139.939 156.524 148.045 1.00 45.59  ? 54  ASP A CB    1 
ATOM   396   C  CG    . ASP A 1 54  ? 140.408 157.891 148.504 1.00 51.99  ? 54  ASP A CG    1 
ATOM   397   O  OD1   . ASP A 1 54  ? 140.674 158.055 149.713 1.00 48.14  ? 54  ASP A OD1   1 
ATOM   398   O  OD2   . ASP A 1 54  ? 140.508 158.803 147.655 1.00 50.42  ? 54  ASP A OD2   1 
ATOM   399   N  N     . ARG A 1 55  ? 140.588 153.573 150.182 1.00 44.14  ? 55  ARG A N     1 
ATOM   400   C  CA    . ARG A 1 55  ? 140.086 152.934 151.390 1.00 40.79  ? 55  ARG A CA    1 
ATOM   401   C  C     . ARG A 1 55  ? 140.711 153.577 152.621 1.00 37.36  ? 55  ARG A C     1 
ATOM   402   O  O     . ARG A 1 55  ? 141.932 153.751 152.692 1.00 39.91  ? 55  ARG A O     1 
ATOM   403   C  CB    . ARG A 1 55  ? 140.388 151.436 151.361 1.00 38.26  ? 55  ARG A CB    1 
ATOM   404   C  CG    . ARG A 1 55  ? 140.274 150.751 152.712 1.00 43.42  ? 55  ARG A CG    1 
ATOM   405   C  CD    . ARG A 1 55  ? 140.990 149.410 152.714 1.00 44.52  ? 55  ARG A CD    1 
ATOM   406   N  NE    . ARG A 1 55  ? 142.425 149.557 152.927 1.00 44.92  ? 55  ARG A NE    1 
ATOM   407   C  CZ    . ARG A 1 55  ? 142.996 149.699 154.115 1.00 42.38  ? 55  ARG A CZ    1 
ATOM   408   N  NH1   . ARG A 1 55  ? 142.280 149.724 155.227 1.00 41.86  ? 55  ARG A NH1   1 
ATOM   409   N  NH2   . ARG A 1 55  ? 144.318 149.820 154.189 1.00 41.05  ? 55  ARG A NH2   1 
ATOM   410   N  N     . GLU A 1 56  ? 139.871 153.935 153.588 1.00 35.96  ? 56  GLU A N     1 
ATOM   411   C  CA    . GLU A 1 56  ? 140.358 154.553 154.813 1.00 32.27  ? 56  GLU A CA    1 
ATOM   412   C  C     . GLU A 1 56  ? 141.150 153.540 155.631 1.00 31.34  ? 56  GLU A C     1 
ATOM   413   O  O     . GLU A 1 56  ? 140.734 152.387 155.783 1.00 33.36  ? 56  GLU A O     1 
ATOM   414   C  CB    . GLU A 1 56  ? 139.189 155.101 155.629 1.00 32.72  ? 56  GLU A CB    1 
ATOM   415   C  CG    . GLU A 1 56  ? 138.554 156.353 155.044 1.00 37.45  ? 56  GLU A CG    1 
ATOM   416   C  CD    . GLU A 1 56  ? 139.318 157.616 155.390 1.00 37.62  ? 56  GLU A CD    1 
ATOM   417   O  OE1   . GLU A 1 56  ? 139.986 157.639 156.443 1.00 37.95  ? 56  GLU A OE1   1 
ATOM   418   O  OE2   . GLU A 1 56  ? 139.251 158.587 154.607 1.00 40.40  ? 56  GLU A OE2   1 
ATOM   419   N  N     . MET A 1 57  ? 142.293 153.970 156.158 1.00 28.30  ? 57  MET A N     1 
ATOM   420   C  CA    . MET A 1 57  ? 143.155 153.111 156.954 1.00 25.97  ? 57  MET A CA    1 
ATOM   421   C  C     . MET A 1 57  ? 143.457 153.779 158.287 1.00 25.04  ? 57  MET A C     1 
ATOM   422   O  O     . MET A 1 57  ? 143.475 155.008 158.396 1.00 30.86  ? 57  MET A O     1 
ATOM   423   C  CB    . MET A 1 57  ? 144.467 152.786 156.222 1.00 27.25  ? 57  MET A CB    1 
ATOM   424   C  CG    . MET A 1 57  ? 144.865 153.787 155.153 1.00 30.35  ? 57  MET A CG    1 
ATOM   425   S  SD    . MET A 1 57  ? 146.490 153.459 154.440 1.00 37.10  ? 57  MET A SD    1 
ATOM   426   C  CE    . MET A 1 57  ? 146.045 152.528 152.977 1.00 36.84  ? 57  MET A CE    1 
ATOM   427   N  N     . ASN A 1 58  ? 143.693 152.953 159.304 1.00 17.55  ? 58  ASN A N     1 
ATOM   428   C  CA    . ASN A 1 58  ? 144.040 153.451 160.624 1.00 17.93  ? 58  ASN A CA    1 
ATOM   429   C  C     . ASN A 1 58  ? 145.497 153.910 160.642 1.00 21.33  ? 58  ASN A C     1 
ATOM   430   O  O     . ASN A 1 58  ? 146.203 153.873 159.631 1.00 25.36  ? 58  ASN A O     1 
ATOM   431   C  CB    . ASN A 1 58  ? 143.778 152.382 161.684 1.00 22.42  ? 58  ASN A CB    1 
ATOM   432   C  CG    . ASN A 1 58  ? 144.363 151.034 161.312 1.00 23.77  ? 58  ASN A CG    1 
ATOM   433   O  OD1   . ASN A 1 58  ? 145.578 150.880 161.197 1.00 26.75  ? 58  ASN A OD1   1 
ATOM   434   N  ND2   . ASN A 1 58  ? 143.497 150.045 161.126 1.00 28.44  ? 58  ASN A ND2   1 
ATOM   435   N  N     . TRP A 1 59  ? 145.957 154.352 161.815 1.00 20.68  ? 59  TRP A N     1 
ATOM   436   C  CA    . TRP A 1 59  ? 147.320 154.864 161.922 1.00 17.48  ? 59  TRP A CA    1 
ATOM   437   C  C     . TRP A 1 59  ? 148.355 153.768 161.704 1.00 15.50  ? 59  TRP A C     1 
ATOM   438   O  O     . TRP A 1 59  ? 149.422 154.034 161.139 1.00 26.00  ? 59  TRP A O     1 
ATOM   439   C  CB    . TRP A 1 59  ? 147.526 155.543 163.278 1.00 14.78  ? 59  TRP A CB    1 
ATOM   440   C  CG    . TRP A 1 59  ? 147.681 154.600 164.433 1.00 19.21  ? 59  TRP A CG    1 
ATOM   441   C  CD1   . TRP A 1 59  ? 146.684 154.080 165.205 1.00 13.51  ? 59  TRP A CD1   1 
ATOM   442   C  CD2   . TRP A 1 59  ? 148.907 154.077 164.956 1.00 18.88  ? 59  TRP A CD2   1 
ATOM   443   N  NE1   . TRP A 1 59  ? 147.212 153.261 166.172 1.00 21.84  ? 59  TRP A NE1   1 
ATOM   444   C  CE2   . TRP A 1 59  ? 148.576 153.243 166.041 1.00 20.81  ? 59  TRP A CE2   1 
ATOM   445   C  CE3   . TRP A 1 59  ? 150.253 154.231 164.610 1.00 16.58  ? 59  TRP A CE3   1 
ATOM   446   C  CZ2   . TRP A 1 59  ? 149.540 152.564 166.784 1.00 19.43  ? 59  TRP A CZ2   1 
ATOM   447   C  CZ3   . TRP A 1 59  ? 151.209 153.557 165.348 1.00 15.83  ? 59  TRP A CZ3   1 
ATOM   448   C  CH2   . TRP A 1 59  ? 150.848 152.734 166.422 1.00 18.70  ? 59  TRP A CH2   1 
ATOM   449   N  N     . LYS A 1 60  ? 148.067 152.540 162.143 1.00 23.71  ? 60  LYS A N     1 
ATOM   450   C  CA    . LYS A 1 60  ? 149.002 151.441 161.924 1.00 14.02  ? 60  LYS A CA    1 
ATOM   451   C  C     . LYS A 1 60  ? 149.158 151.131 160.440 1.00 16.48  ? 60  LYS A C     1 
ATOM   452   O  O     . LYS A 1 60  ? 150.277 150.915 159.960 1.00 20.52  ? 60  LYS A O     1 
ATOM   453   C  CB    . LYS A 1 60  ? 148.541 150.200 162.687 1.00 22.44  ? 60  LYS A CB    1 
ATOM   454   C  CG    . LYS A 1 60  ? 148.860 150.233 164.173 1.00 20.15  ? 60  LYS A CG    1 
ATOM   455   C  CD    . LYS A 1 60  ? 148.613 148.884 164.832 1.00 26.56  ? 60  LYS A CD    1 
ATOM   456   C  CE    . LYS A 1 60  ? 147.258 148.832 165.525 1.00 28.36  ? 60  LYS A CE    1 
ATOM   457   N  NZ    . LYS A 1 60  ? 146.132 149.224 164.633 1.00 34.52  ? 60  LYS A NZ    1 
ATOM   458   N  N     . GLN A 1 61  ? 148.049 151.102 159.699 1.00 20.02  ? 61  GLN A N     1 
ATOM   459   C  CA    . GLN A 1 61  ? 148.127 150.847 158.264 1.00 15.89  ? 61  GLN A CA    1 
ATOM   460   C  C     . GLN A 1 61  ? 148.725 152.037 157.523 1.00 19.57  ? 61  GLN A C     1 
ATOM   461   O  O     . GLN A 1 61  ? 149.491 151.859 156.569 1.00 21.03  ? 61  GLN A O     1 
ATOM   462   C  CB    . GLN A 1 61  ? 146.743 150.510 157.715 1.00 20.58  ? 61  GLN A CB    1 
ATOM   463   C  CG    . GLN A 1 61  ? 146.124 149.255 158.308 1.00 24.57  ? 61  GLN A CG    1 
ATOM   464   C  CD    . GLN A 1 61  ? 144.653 149.117 157.969 1.00 28.27  ? 61  GLN A CD    1 
ATOM   465   O  OE1   . GLN A 1 61  ? 143.874 150.053 158.143 1.00 28.06  ? 61  GLN A OE1   1 
ATOM   466   N  NE2   . GLN A 1 61  ? 144.266 147.944 157.480 1.00 28.17  ? 61  GLN A NE2   1 
ATOM   467   N  N     . TYR A 1 62  ? 148.377 153.258 157.940 1.00 21.60  ? 62  TYR A N     1 
ATOM   468   C  CA    . TYR A 1 62  ? 148.948 154.447 157.316 1.00 12.22  ? 62  TYR A CA    1 
ATOM   469   C  C     . TYR A 1 62  ? 150.457 154.504 157.519 1.00 19.14  ? 62  TYR A C     1 
ATOM   470   O  O     . TYR A 1 62  ? 151.205 154.817 156.585 1.00 15.55  ? 62  TYR A O     1 
ATOM   471   C  CB    . TYR A 1 62  ? 148.283 155.704 157.880 1.00 12.80  ? 62  TYR A CB    1 
ATOM   472   C  CG    . TYR A 1 62  ? 148.412 156.929 157.002 1.00 15.79  ? 62  TYR A CG    1 
ATOM   473   C  CD1   . TYR A 1 62  ? 149.606 157.638 156.935 1.00 17.86  ? 62  TYR A CD1   1 
ATOM   474   C  CD2   . TYR A 1 62  ? 147.338 157.384 156.249 1.00 17.17  ? 62  TYR A CD2   1 
ATOM   475   C  CE1   . TYR A 1 62  ? 149.728 158.758 156.137 1.00 15.75  ? 62  TYR A CE1   1 
ATOM   476   C  CE2   . TYR A 1 62  ? 147.450 158.506 155.449 1.00 16.24  ? 62  TYR A CE2   1 
ATOM   477   C  CZ    . TYR A 1 62  ? 148.648 159.188 155.396 1.00 20.36  ? 62  TYR A CZ    1 
ATOM   478   O  OH    . TYR A 1 62  ? 148.767 160.304 154.601 1.00 24.22  ? 62  TYR A OH    1 
ATOM   479   N  N     . LEU A 1 63  ? 150.921 154.206 158.735 1.00 17.65  ? 63  LEU A N     1 
ATOM   480   C  CA    . LEU A 1 63  ? 152.356 154.199 159.001 1.00 18.64  ? 63  LEU A CA    1 
ATOM   481   C  C     . LEU A 1 63  ? 153.060 153.113 158.198 1.00 15.57  ? 63  LEU A C     1 
ATOM   482   O  O     . LEU A 1 63  ? 154.154 153.335 157.665 1.00 25.12  ? 63  LEU A O     1 
ATOM   483   C  CB    . LEU A 1 63  ? 152.607 154.013 160.498 1.00 20.62  ? 63  LEU A CB    1 
ATOM   484   C  CG    . LEU A 1 63  ? 154.044 153.723 160.936 1.00 19.55  ? 63  LEU A CG    1 
ATOM   485   C  CD1   . LEU A 1 63  ? 154.940 154.922 160.671 1.00 17.41  ? 63  LEU A CD1   1 
ATOM   486   C  CD2   . LEU A 1 63  ? 154.086 153.333 162.404 1.00 18.20  ? 63  LEU A CD2   1 
ATOM   487   N  N     . CYS A 1 64  ? 152.446 151.931 158.098 1.00 20.18  ? 64  CYS A N     1 
ATOM   488   C  CA    . CYS A 1 64  ? 153.053 150.837 157.347 1.00 20.55  ? 64  CYS A CA    1 
ATOM   489   C  C     . CYS A 1 64  ? 153.194 151.189 155.872 1.00 21.25  ? 64  CYS A C     1 
ATOM   490   O  O     . CYS A 1 64  ? 154.191 150.831 155.233 1.00 19.79  ? 64  CYS A O     1 
ATOM   491   C  CB    . CYS A 1 64  ? 152.228 149.562 157.519 1.00 16.84  ? 64  CYS A CB    1 
ATOM   492   S  SG    . CYS A 1 64  ? 153.022 148.067 156.889 1.00 50.15  ? 64  CYS A SG    1 
ATOM   493   N  N     . ALA A 1 65  ? 152.200 151.881 155.310 1.00 20.64  ? 65  ALA A N     1 
ATOM   494   C  CA    . ALA A 1 65  ? 152.282 152.294 153.913 1.00 18.61  ? 65  ALA A CA    1 
ATOM   495   C  C     . ALA A 1 65  ? 153.448 153.248 153.685 1.00 21.97  ? 65  ALA A C     1 
ATOM   496   O  O     . ALA A 1 65  ? 154.173 153.128 152.690 1.00 20.45  ? 65  ALA A O     1 
ATOM   497   C  CB    . ALA A 1 65  ? 150.967 152.940 153.479 1.00 9.51   ? 65  ALA A CB    1 
ATOM   498   N  N     . ILE A 1 66  ? 153.642 154.206 154.594 1.00 16.98  ? 66  ILE A N     1 
ATOM   499   C  CA    . ILE A 1 66  ? 154.772 155.124 154.480 1.00 17.23  ? 66  ILE A CA    1 
ATOM   500   C  C     . ILE A 1 66  ? 156.086 154.375 154.663 1.00 20.38  ? 66  ILE A C     1 
ATOM   501   O  O     . ILE A 1 66  ? 157.042 154.568 153.902 1.00 23.86  ? 66  ILE A O     1 
ATOM   502   C  CB    . ILE A 1 66  ? 154.632 156.275 155.493 1.00 20.64  ? 66  ILE A CB    1 
ATOM   503   C  CG1   . ILE A 1 66  ? 153.319 157.029 155.268 1.00 16.87  ? 66  ILE A CG1   1 
ATOM   504   C  CG2   . ILE A 1 66  ? 155.824 157.217 155.401 1.00 16.13  ? 66  ILE A CG2   1 
ATOM   505   C  CD1   . ILE A 1 66  ? 153.350 157.980 154.095 1.00 22.41  ? 66  ILE A CD1   1 
ATOM   506   N  N     . LEU A 1 67  ? 156.153 153.509 155.678 1.00 21.22  ? 67  LEU A N     1 
ATOM   507   C  CA    . LEU A 1 67  ? 157.372 152.744 155.923 1.00 17.37  ? 67  LEU A CA    1 
ATOM   508   C  C     . LEU A 1 67  ? 157.663 151.779 154.780 1.00 18.18  ? 67  LEU A C     1 
ATOM   509   O  O     . LEU A 1 67  ? 158.821 151.615 154.380 1.00 23.58  ? 67  LEU A O     1 
ATOM   510   C  CB    . LEU A 1 67  ? 157.259 151.989 157.248 1.00 16.60  ? 67  LEU A CB    1 
ATOM   511   C  CG    . LEU A 1 67  ? 157.243 152.840 158.520 1.00 22.50  ? 67  LEU A CG    1 
ATOM   512   C  CD1   . LEU A 1 67  ? 157.204 151.957 159.757 1.00 21.35  ? 67  LEU A CD1   1 
ATOM   513   C  CD2   . LEU A 1 67  ? 158.439 153.777 158.561 1.00 20.47  ? 67  LEU A CD2   1 
ATOM   514   N  N     . GLY A 1 68  ? 156.627 151.129 154.247 1.00 19.01  ? 68  GLY A N     1 
ATOM   515   C  CA    . GLY A 1 68  ? 156.839 150.186 153.160 1.00 19.10  ? 68  GLY A CA    1 
ATOM   516   C  C     . GLY A 1 68  ? 157.352 150.849 151.896 1.00 20.39  ? 68  GLY A C     1 
ATOM   517   O  O     . GLY A 1 68  ? 158.253 150.329 151.234 1.00 24.44  ? 68  GLY A O     1 
ATOM   518   N  N     . LEU A 1 69  ? 156.782 152.002 151.540 1.00 20.19  ? 69  LEU A N     1 
ATOM   519   C  CA    . LEU A 1 69  ? 157.239 152.718 150.353 1.00 21.07  ? 69  LEU A CA    1 
ATOM   520   C  C     . LEU A 1 69  ? 158.671 153.211 150.518 1.00 17.26  ? 69  LEU A C     1 
ATOM   521   O  O     . LEU A 1 69  ? 159.467 153.148 149.573 1.00 21.48  ? 69  LEU A O     1 
ATOM   522   C  CB    . LEU A 1 69  ? 156.300 153.885 150.049 1.00 14.35  ? 69  LEU A CB    1 
ATOM   523   C  CG    . LEU A 1 69  ? 156.628 154.702 148.797 1.00 26.83  ? 69  LEU A CG    1 
ATOM   524   C  CD1   . LEU A 1 69  ? 155.472 154.666 147.812 1.00 25.76  ? 69  LEU A CD1   1 
ATOM   525   C  CD2   . LEU A 1 69  ? 156.979 156.135 149.167 1.00 24.36  ? 69  LEU A CD2   1 
ATOM   526   N  N     . ASN A 1 70  ? 159.015 153.712 151.707 1.00 16.34  ? 70  ASN A N     1 
ATOM   527   C  CA    . ASN A 1 70  ? 160.375 154.185 151.946 1.00 10.33  ? 70  ASN A CA    1 
ATOM   528   C  C     . ASN A 1 70  ? 161.381 153.042 151.877 1.00 19.91  ? 70  ASN A C     1 
ATOM   529   O  O     . ASN A 1 70  ? 162.477 153.206 151.328 1.00 19.75  ? 70  ASN A O     1 
ATOM   530   C  CB    . ASN A 1 70  ? 160.454 154.891 153.299 1.00 13.76  ? 70  ASN A CB    1 
ATOM   531   C  CG    . ASN A 1 70  ? 159.950 156.319 153.241 1.00 14.90  ? 70  ASN A CG    1 
ATOM   532   O  OD1   . ASN A 1 70  ? 160.708 157.265 153.450 1.00 30.33  ? 70  ASN A OD1   1 
ATOM   533   N  ND2   . ASN A 1 70  ? 158.663 156.482 152.958 1.00 17.11  ? 70  ASN A ND2   1 
ATOM   534   N  N     . MET A 1 71  ? 161.032 151.881 152.437 1.00 23.78  ? 71  MET A N     1 
ATOM   535   C  CA    . MET A 1 71  ? 161.931 150.732 152.378 1.00 16.41  ? 71  MET A CA    1 
ATOM   536   C  C     . MET A 1 71  ? 162.123 150.251 150.946 1.00 17.44  ? 71  MET A C     1 
ATOM   537   O  O     . MET A 1 71  ? 163.233 149.871 150.556 1.00 22.61  ? 71  MET A O     1 
ATOM   538   C  CB    . MET A 1 71  ? 161.400 149.600 153.258 1.00 19.72  ? 71  MET A CB    1 
ATOM   539   C  CG    . MET A 1 71  ? 161.489 149.857 154.760 1.00 22.11  ? 71  MET A CG    1 
ATOM   540   S  SD    . MET A 1 71  ? 163.059 150.560 155.308 1.00 43.03  ? 71  MET A SD    1 
ATOM   541   C  CE    . MET A 1 71  ? 162.626 152.289 155.501 1.00 24.84  ? 71  MET A CE    1 
ATOM   542   N  N     . LEU A 1 72  ? 161.050 150.249 150.151 1.00 19.17  ? 72  LEU A N     1 
ATOM   543   C  CA    . LEU A 1 72  ? 161.169 149.867 148.747 1.00 17.20  ? 72  LEU A CA    1 
ATOM   544   C  C     . LEU A 1 72  ? 162.063 150.838 147.986 1.00 23.44  ? 72  LEU A C     1 
ATOM   545   O  O     . LEU A 1 72  ? 162.891 150.421 147.169 1.00 22.23  ? 72  LEU A O     1 
ATOM   546   C  CB    . LEU A 1 72  ? 159.784 149.792 148.106 1.00 18.38  ? 72  LEU A CB    1 
ATOM   547   C  CG    . LEU A 1 72  ? 159.722 149.331 146.650 1.00 25.96  ? 72  LEU A CG    1 
ATOM   548   C  CD1   . LEU A 1 72  ? 160.483 148.027 146.462 1.00 24.80  ? 72  LEU A CD1   1 
ATOM   549   C  CD2   . LEU A 1 72  ? 158.277 149.181 146.205 1.00 26.17  ? 72  LEU A CD2   1 
ATOM   550   N  N     . GLY A 1 73  ? 161.905 152.139 148.238 1.00 20.94  ? 73  GLY A N     1 
ATOM   551   C  CA    . GLY A 1 73  ? 162.784 153.117 147.622 1.00 14.21  ? 73  GLY A CA    1 
ATOM   552   C  C     . GLY A 1 73  ? 164.223 152.995 148.079 1.00 14.26  ? 73  GLY A C     1 
ATOM   553   O  O     . GLY A 1 73  ? 165.148 153.237 147.298 1.00 18.18  ? 73  GLY A O     1 
ATOM   554   N  N     . LEU A 1 74  ? 164.433 152.630 149.346 1.00 14.25  ? 74  LEU A N     1 
ATOM   555   C  CA    . LEU A 1 74  ? 165.789 152.449 149.854 1.00 16.40  ? 74  LEU A CA    1 
ATOM   556   C  C     . LEU A 1 74  ? 166.504 151.312 149.135 1.00 18.62  ? 74  LEU A C     1 
ATOM   557   O  O     . LEU A 1 74  ? 167.680 151.437 148.775 1.00 22.40  ? 74  LEU A O     1 
ATOM   558   C  CB    . LEU A 1 74  ? 165.751 152.193 151.361 1.00 15.89  ? 74  LEU A CB    1 
ATOM   559   C  CG    . LEU A 1 74  ? 167.078 151.864 152.046 1.00 19.32  ? 74  LEU A CG    1 
ATOM   560   C  CD1   . LEU A 1 74  ? 168.080 152.988 151.846 1.00 11.81  ? 74  LEU A CD1   1 
ATOM   561   C  CD2   . LEU A 1 74  ? 166.862 151.590 153.526 1.00 17.60  ? 74  LEU A CD2   1 
ATOM   562   N  N     . ALA A 1 75  ? 165.810 150.191 148.922 1.00 20.01  ? 75  ALA A N     1 
ATOM   563   C  CA    . ALA A 1 75  ? 166.430 149.053 148.250 1.00 21.55  ? 75  ALA A CA    1 
ATOM   564   C  C     . ALA A 1 75  ? 166.736 149.366 146.791 1.00 25.16  ? 75  ALA A C     1 
ATOM   565   O  O     . ALA A 1 75  ? 167.800 148.994 146.282 1.00 26.62  ? 75  ALA A O     1 
ATOM   566   C  CB    . ALA A 1 75  ? 165.526 147.826 148.358 1.00 20.32  ? 75  ALA A CB    1 
ATOM   567   N  N     . VAL A 1 76  ? 165.816 150.044 146.102 1.00 17.77  ? 76  VAL A N     1 
ATOM   568   C  CA    . VAL A 1 76  ? 166.017 150.356 144.690 1.00 12.40  ? 76  VAL A CA    1 
ATOM   569   C  C     . VAL A 1 76  ? 167.197 151.306 144.514 1.00 18.08  ? 76  VAL A C     1 
ATOM   570   O  O     . VAL A 1 76  ? 168.051 151.106 143.642 1.00 25.95  ? 76  VAL A O     1 
ATOM   571   C  CB    . VAL A 1 76  ? 164.726 150.935 144.083 1.00 22.48  ? 76  VAL A CB    1 
ATOM   572   C  CG1   . VAL A 1 76  ? 165.008 151.571 142.731 1.00 17.64  ? 76  VAL A CG1   1 
ATOM   573   C  CG2   . VAL A 1 76  ? 163.669 149.848 143.957 1.00 19.43  ? 76  VAL A CG2   1 
ATOM   574   N  N     . LEU A 1 77  ? 167.265 152.350 145.343 1.00 20.84  ? 77  LEU A N     1 
ATOM   575   C  CA    . LEU A 1 77  ? 168.360 153.309 145.237 1.00 20.67  ? 77  LEU A CA    1 
ATOM   576   C  C     . LEU A 1 77  ? 169.696 152.672 145.599 1.00 16.91  ? 77  LEU A C     1 
ATOM   577   O  O     . LEU A 1 77  ? 170.717 152.959 144.964 1.00 18.84  ? 77  LEU A O     1 
ATOM   578   C  CB    . LEU A 1 77  ? 168.082 154.522 146.125 1.00 16.43  ? 77  LEU A CB    1 
ATOM   579   C  CG    . LEU A 1 77  ? 169.124 155.644 146.119 1.00 23.20  ? 77  LEU A CG    1 
ATOM   580   C  CD1   . LEU A 1 77  ? 169.501 156.029 144.697 1.00 15.26  ? 77  LEU A CD1   1 
ATOM   581   C  CD2   . LEU A 1 77  ? 168.612 156.855 146.883 1.00 13.22  ? 77  LEU A CD2   1 
ATOM   582   N  N     . PHE A 1 78  ? 169.710 151.809 146.618 1.00 19.53  ? 78  PHE A N     1 
ATOM   583   C  CA    . PHE A 1 78  ? 170.959 151.182 147.040 1.00 14.54  ? 78  PHE A CA    1 
ATOM   584   C  C     . PHE A 1 78  ? 171.546 150.314 145.934 1.00 17.52  ? 78  PHE A C     1 
ATOM   585   O  O     . PHE A 1 78  ? 172.756 150.352 145.682 1.00 18.13  ? 78  PHE A O     1 
ATOM   586   C  CB    . PHE A 1 78  ? 170.726 150.355 148.305 1.00 11.05  ? 78  PHE A CB    1 
ATOM   587   C  CG    . PHE A 1 78  ? 171.933 149.585 148.759 1.00 21.76  ? 78  PHE A CG    1 
ATOM   588   C  CD1   . PHE A 1 78  ? 173.067 150.245 149.200 1.00 18.33  ? 78  PHE A CD1   1 
ATOM   589   C  CD2   . PHE A 1 78  ? 171.932 148.200 148.745 1.00 18.52  ? 78  PHE A CD2   1 
ATOM   590   C  CE1   . PHE A 1 78  ? 174.178 149.539 149.619 1.00 19.43  ? 78  PHE A CE1   1 
ATOM   591   C  CE2   . PHE A 1 78  ? 173.040 147.488 149.164 1.00 21.42  ? 78  PHE A CE2   1 
ATOM   592   C  CZ    . PHE A 1 78  ? 174.164 148.158 149.601 1.00 24.93  ? 78  PHE A CZ    1 
ATOM   593   N  N     . PHE A 1 79  ? 170.706 149.528 145.260 1.00 19.93  ? 79  PHE A N     1 
ATOM   594   C  CA    . PHE A 1 79  ? 171.192 148.673 144.184 1.00 22.38  ? 79  PHE A CA    1 
ATOM   595   C  C     . PHE A 1 79  ? 171.470 149.458 142.909 1.00 21.48  ? 79  PHE A C     1 
ATOM   596   O  O     . PHE A 1 79  ? 172.334 149.061 142.120 1.00 23.94  ? 79  PHE A O     1 
ATOM   597   C  CB    . PHE A 1 79  ? 170.190 147.551 143.913 1.00 21.19  ? 79  PHE A CB    1 
ATOM   598   C  CG    . PHE A 1 79  ? 170.179 146.486 144.973 1.00 22.39  ? 79  PHE A CG    1 
ATOM   599   C  CD1   . PHE A 1 79  ? 171.339 145.802 145.295 1.00 27.20  ? 79  PHE A CD1   1 
ATOM   600   C  CD2   . PHE A 1 79  ? 169.014 146.175 145.652 1.00 25.64  ? 79  PHE A CD2   1 
ATOM   601   C  CE1   . PHE A 1 79  ? 171.336 144.825 146.272 1.00 24.35  ? 79  PHE A CE1   1 
ATOM   602   C  CE2   . PHE A 1 79  ? 169.004 145.199 146.630 1.00 27.33  ? 79  PHE A CE2   1 
ATOM   603   C  CZ    . PHE A 1 79  ? 170.167 144.523 146.940 1.00 26.09  ? 79  PHE A CZ    1 
ATOM   604   N  N     . MET A 1 80  ? 170.750 150.561 142.686 1.00 22.20  ? 80  MET A N     1 
ATOM   605   C  CA    . MET A 1 80  ? 171.031 151.406 141.529 1.00 19.31  ? 80  MET A CA    1 
ATOM   606   C  C     . MET A 1 80  ? 172.428 152.006 141.614 1.00 21.63  ? 80  MET A C     1 
ATOM   607   O  O     . MET A 1 80  ? 173.154 152.055 140.614 1.00 23.86  ? 80  MET A O     1 
ATOM   608   C  CB    . MET A 1 80  ? 169.979 152.509 141.418 1.00 20.33  ? 80  MET A CB    1 
ATOM   609   C  CG    . MET A 1 80  ? 170.193 153.460 140.251 1.00 29.30  ? 80  MET A CG    1 
ATOM   610   S  SD    . MET A 1 80  ? 168.722 154.405 139.803 1.00 49.53  ? 80  MET A SD    1 
ATOM   611   C  CE    . MET A 1 80  ? 167.434 153.473 140.629 1.00 21.19  ? 80  MET A CE    1 
ATOM   612   N  N     . LEU A 1 81  ? 172.821 152.474 142.801 1.00 17.36  ? 81  LEU A N     1 
ATOM   613   C  CA    . LEU A 1 81  ? 174.160 153.026 142.976 1.00 18.95  ? 81  LEU A CA    1 
ATOM   614   C  C     . LEU A 1 81  ? 175.227 151.946 142.844 1.00 24.31  ? 81  LEU A C     1 
ATOM   615   O  O     . LEU A 1 81  ? 176.301 152.193 142.283 1.00 26.81  ? 81  LEU A O     1 
ATOM   616   C  CB    . LEU A 1 81  ? 174.262 153.729 144.329 1.00 15.94  ? 81  LEU A CB    1 
ATOM   617   C  CG    . LEU A 1 81  ? 173.315 154.915 144.530 1.00 23.77  ? 81  LEU A CG    1 
ATOM   618   C  CD1   . LEU A 1 81  ? 173.237 155.310 145.997 1.00 23.24  ? 81  LEU A CD1   1 
ATOM   619   C  CD2   . LEU A 1 81  ? 173.740 156.097 143.673 1.00 14.31  ? 81  LEU A CD2   1 
ATOM   620   N  N     . LEU A 1 82  ? 174.956 150.746 143.365 1.00 20.02  ? 82  LEU A N     1 
ATOM   621   C  CA    . LEU A 1 82  ? 175.919 149.654 143.254 1.00 22.33  ? 82  LEU A CA    1 
ATOM   622   C  C     . LEU A 1 82  ? 176.122 149.234 141.803 1.00 18.19  ? 82  LEU A C     1 
ATOM   623   O  O     . LEU A 1 82  ? 177.258 149.008 141.370 1.00 27.43  ? 82  LEU A O     1 
ATOM   624   C  CB    . LEU A 1 82  ? 175.460 148.460 144.090 1.00 24.25  ? 82  LEU A CB    1 
ATOM   625   C  CG    . LEU A 1 82  ? 175.607 148.549 145.608 1.00 24.84  ? 82  LEU A CG    1 
ATOM   626   C  CD1   . LEU A 1 82  ? 175.087 147.277 146.254 1.00 29.56  ? 82  LEU A CD1   1 
ATOM   627   C  CD2   . LEU A 1 82  ? 177.052 148.799 146.003 1.00 24.83  ? 82  LEU A CD2   1 
ATOM   628   N  N     . GLY A 1 83  ? 175.038 149.123 141.040 1.00 17.23  ? 83  GLY A N     1 
ATOM   629   C  CA    . GLY A 1 83  ? 175.124 148.709 139.654 1.00 22.56  ? 83  GLY A CA    1 
ATOM   630   C  C     . GLY A 1 83  ? 175.073 149.873 138.689 1.00 15.91  ? 83  GLY A C     1 
ATOM   631   O  O     . GLY A 1 83  ? 174.537 149.753 137.583 1.00 30.88  ? 83  GLY A O     1 
ATOM   632   N  N     . GLN A 1 84  ? 175.634 151.010 139.104 1.00 20.46  ? 84  GLN A N     1 
ATOM   633   C  CA    . GLN A 1 84  ? 175.589 152.213 138.279 1.00 24.60  ? 84  GLN A CA    1 
ATOM   634   C  C     . GLN A 1 84  ? 176.368 152.027 136.982 1.00 24.39  ? 84  GLN A C     1 
ATOM   635   O  O     . GLN A 1 84  ? 175.959 152.527 135.926 1.00 26.20  ? 84  GLN A O     1 
ATOM   636   C  CB    . GLN A 1 84  ? 176.122 153.404 139.077 1.00 24.37  ? 84  GLN A CB    1 
ATOM   637   C  CG    . GLN A 1 84  ? 176.768 154.497 138.250 1.00 23.62  ? 84  GLN A CG    1 
ATOM   638   C  CD    . GLN A 1 84  ? 177.378 155.584 139.110 1.00 24.78  ? 84  GLN A CD    1 
ATOM   639   O  OE1   . GLN A 1 84  ? 176.700 156.533 139.500 1.00 26.59  ? 84  GLN A OE1   1 
ATOM   640   N  NE2   . GLN A 1 84  ? 178.663 155.450 139.412 1.00 27.14  ? 84  GLN A NE2   1 
ATOM   641   N  N     . HIS A 1 85  ? 177.489 151.303 137.037 1.00 28.65  ? 85  HIS A N     1 
ATOM   642   C  CA    . HIS A 1 85  ? 178.297 151.082 135.843 1.00 26.03  ? 85  HIS A CA    1 
ATOM   643   C  C     . HIS A 1 85  ? 177.560 150.277 134.780 1.00 29.41  ? 85  HIS A C     1 
ATOM   644   O  O     . HIS A 1 85  ? 177.915 150.361 133.599 1.00 36.97  ? 85  HIS A O     1 
ATOM   645   C  CB    . HIS A 1 85  ? 179.602 150.377 136.216 1.00 25.82  ? 85  HIS A CB    1 
ATOM   646   C  CG    . HIS A 1 85  ? 180.652 150.449 135.152 1.00 36.39  ? 85  HIS A CG    1 
ATOM   647   N  ND1   . HIS A 1 85  ? 180.967 149.378 134.344 1.00 38.35  ? 85  HIS A ND1   1 
ATOM   648   C  CD2   . HIS A 1 85  ? 181.458 151.464 134.762 1.00 32.94  ? 85  HIS A CD2   1 
ATOM   649   C  CE1   . HIS A 1 85  ? 181.923 149.730 133.502 1.00 37.03  ? 85  HIS A CE1   1 
ATOM   650   N  NE2   . HIS A 1 85  ? 182.239 150.991 133.735 1.00 38.71  ? 85  HIS A NE2   1 
ATOM   651   N  N     . TYR A 1 86  ? 176.549 149.503 135.166 1.00 30.55  ? 86  TYR A N     1 
ATOM   652   C  CA    . TYR A 1 86  ? 175.770 148.709 134.225 1.00 30.24  ? 86  TYR A CA    1 
ATOM   653   C  C     . TYR A 1 86  ? 174.533 149.436 133.715 1.00 30.26  ? 86  TYR A C     1 
ATOM   654   O  O     . TYR A 1 86  ? 173.758 148.848 132.954 1.00 34.87  ? 86  TYR A O     1 
ATOM   655   C  CB    . TYR A 1 86  ? 175.355 147.384 134.871 1.00 29.72  ? 86  TYR A CB    1 
ATOM   656   C  CG    . TYR A 1 86  ? 176.510 146.452 135.154 1.00 36.94  ? 86  TYR A CG    1 
ATOM   657   C  CD1   . TYR A 1 86  ? 177.335 146.007 134.130 1.00 35.93  ? 86  TYR A CD1   1 
ATOM   658   C  CD2   . TYR A 1 86  ? 176.777 146.018 136.446 1.00 34.99  ? 86  TYR A CD2   1 
ATOM   659   C  CE1   . TYR A 1 86  ? 178.393 145.155 134.384 1.00 35.24  ? 86  TYR A CE1   1 
ATOM   660   C  CE2   . TYR A 1 86  ? 177.833 145.166 136.710 1.00 37.81  ? 86  TYR A CE2   1 
ATOM   661   C  CZ    . TYR A 1 86  ? 178.637 144.738 135.676 1.00 38.27  ? 86  TYR A CZ    1 
ATOM   662   O  OH    . TYR A 1 86  ? 179.689 143.891 135.933 1.00 42.47  ? 86  TYR A OH    1 
ATOM   663   N  N     . LEU A 1 87  ? 174.329 150.690 134.111 1.00 27.80  ? 87  LEU A N     1 
ATOM   664   C  CA    . LEU A 1 87  ? 173.153 151.457 133.741 1.00 23.89  ? 87  LEU A CA    1 
ATOM   665   C  C     . LEU A 1 87  ? 173.495 152.491 132.670 1.00 23.36  ? 87  LEU A C     1 
ATOM   666   O  O     . LEU A 1 87  ? 174.643 152.937 132.575 1.00 33.72  ? 87  LEU A O     1 
ATOM   667   C  CB    . LEU A 1 87  ? 172.558 152.163 134.965 1.00 26.07  ? 87  LEU A CB    1 
ATOM   668   C  CG    . LEU A 1 87  ? 172.005 151.227 136.043 1.00 25.64  ? 87  LEU A CG    1 
ATOM   669   C  CD1   . LEU A 1 87  ? 171.903 151.941 137.380 1.00 29.86  ? 87  LEU A CD1   1 
ATOM   670   C  CD2   . LEU A 1 87  ? 170.657 150.660 135.627 1.00 27.07  ? 87  LEU A CD2   1 
ATOM   671   N  N     . PRO A 1 88  ? 172.521 152.892 131.843 1.00 30.24  ? 88  PRO A N     1 
ATOM   672   C  CA    . PRO A 1 88  ? 172.817 153.845 130.764 1.00 25.57  ? 88  PRO A CA    1 
ATOM   673   C  C     . PRO A 1 88  ? 173.030 155.264 131.265 1.00 24.03  ? 88  PRO A C     1 
ATOM   674   O  O     . PRO A 1 88  ? 173.046 155.509 132.476 1.00 26.27  ? 88  PRO A O     1 
ATOM   675   C  CB    . PRO A 1 88  ? 171.576 153.750 129.868 1.00 25.40  ? 88  PRO A CB    1 
ATOM   676   C  CG    . PRO A 1 88  ? 170.485 153.349 130.796 1.00 26.04  ? 88  PRO A CG    1 
ATOM   677   C  CD    . PRO A 1 88  ? 171.120 152.435 131.806 1.00 24.25  ? 88  PRO A CD    1 
ATOM   678   N  N     . LEU A 1 89  ? 173.197 156.202 130.329 1.00 21.27  ? 89  LEU A N     1 
ATOM   679   C  CA    . LEU A 1 89  ? 173.433 157.613 130.642 1.00 25.16  ? 89  LEU A CA    1 
ATOM   680   C  C     . LEU A 1 89  ? 174.664 157.781 131.532 1.00 22.43  ? 89  LEU A C     1 
ATOM   681   O  O     . LEU A 1 89  ? 174.624 158.432 132.579 1.00 27.36  ? 89  LEU A O     1 
ATOM   682   C  CB    . LEU A 1 89  ? 172.196 158.252 131.280 1.00 21.81  ? 89  LEU A CB    1 
ATOM   683   C  CG    . LEU A 1 89  ? 170.940 158.269 130.408 1.00 21.59  ? 89  LEU A CG    1 
ATOM   684   C  CD1   . LEU A 1 89  ? 169.714 158.627 131.232 1.00 22.97  ? 89  LEU A CD1   1 
ATOM   685   C  CD2   . LEU A 1 89  ? 171.110 159.232 129.245 1.00 23.20  ? 89  LEU A CD2   1 
ATOM   686   N  N     . ASN A 1 90  ? 175.770 157.179 131.103 1.00 32.56  ? 90  ASN A N     1 
ATOM   687   C  CA    . ASN A 1 90  ? 177.042 157.228 131.822 1.00 20.96  ? 90  ASN A CA    1 
ATOM   688   C  C     . ASN A 1 90  ? 178.146 157.625 130.850 1.00 25.33  ? 90  ASN A C     1 
ATOM   689   O  O     . ASN A 1 90  ? 178.974 156.794 130.457 1.00 35.80  ? 90  ASN A O     1 
ATOM   690   C  CB    . ASN A 1 90  ? 177.344 155.881 132.481 1.00 28.92  ? 90  ASN A CB    1 
ATOM   691   C  CG    . ASN A 1 90  ? 178.187 156.018 133.731 1.00 23.56  ? 90  ASN A CG    1 
ATOM   692   O  OD1   . ASN A 1 90  ? 178.464 157.125 134.187 1.00 34.17  ? 90  ASN A OD1   1 
ATOM   693   N  ND2   . ASN A 1 90  ? 178.598 154.889 134.295 1.00 18.93  ? 90  ASN A ND2   1 
ATOM   694   N  N     . PRO A 1 91  ? 178.180 158.896 130.429 1.00 26.43  ? 91  PRO A N     1 
ATOM   695   C  CA    . PRO A 1 91  ? 179.229 159.319 129.484 1.00 23.88  ? 91  PRO A CA    1 
ATOM   696   C  C     . PRO A 1 91  ? 180.635 159.138 130.029 1.00 26.43  ? 91  PRO A C     1 
ATOM   697   O  O     . PRO A 1 91  ? 181.554 158.806 129.270 1.00 31.33  ? 91  PRO A O     1 
ATOM   698   C  CB    . PRO A 1 91  ? 178.895 160.796 129.231 1.00 26.15  ? 91  PRO A CB    1 
ATOM   699   C  CG    . PRO A 1 91  ? 178.114 161.219 130.426 1.00 25.19  ? 91  PRO A CG    1 
ATOM   700   C  CD    . PRO A 1 91  ? 177.323 160.018 130.847 1.00 21.24  ? 91  PRO A CD    1 
ATOM   701   N  N     . GLN A 1 92  ? 180.826 159.348 131.327 1.00 30.34  ? 92  GLN A N     1 
ATOM   702   C  CA    . GLN A 1 92  ? 182.075 159.031 132.004 1.00 24.67  ? 92  GLN A CA    1 
ATOM   703   C  C     . GLN A 1 92  ? 181.911 157.670 132.665 1.00 31.72  ? 92  GLN A C     1 
ATOM   704   O  O     . GLN A 1 92  ? 181.004 157.482 133.481 1.00 45.27  ? 92  GLN A O     1 
ATOM   705   C  CB    . GLN A 1 92  ? 182.427 160.097 133.041 1.00 27.36  ? 92  GLN A CB    1 
ATOM   706   C  CG    . GLN A 1 92  ? 182.327 161.526 132.533 1.00 23.60  ? 92  GLN A CG    1 
ATOM   707   C  CD    . GLN A 1 92  ? 183.673 162.100 132.141 1.00 27.26  ? 92  GLN A CD    1 
ATOM   708   O  OE1   . GLN A 1 92  ? 184.535 162.327 132.990 1.00 24.98  ? 92  GLN A OE1   1 
ATOM   709   N  NE2   . GLN A 1 92  ? 183.861 162.339 130.849 1.00 33.61  ? 92  GLN A NE2   1 
ATOM   710   N  N     . GLN A 1 93  ? 182.790 156.729 132.330 1.00 35.03  ? 93  GLN A N     1 
ATOM   711   C  CA    . GLN A 1 93  ? 182.609 155.357 132.789 1.00 30.06  ? 93  GLN A CA    1 
ATOM   712   C  C     . GLN A 1 93  ? 182.901 155.239 134.280 1.00 32.37  ? 93  GLN A C     1 
ATOM   713   O  O     . GLN A 1 93  ? 183.871 154.591 134.683 1.00 43.02  ? 93  GLN A O     1 
ATOM   714   C  CB    . GLN A 1 93  ? 183.501 154.404 131.991 1.00 35.18  ? 93  GLN A CB    1 
ATOM   715   C  CG    . GLN A 1 93  ? 183.334 154.522 130.487 1.00 34.51  ? 93  GLN A CG    1 
ATOM   716   C  CD    . GLN A 1 93  ? 181.907 154.276 130.038 1.00 41.22  ? 93  GLN A CD    1 
ATOM   717   O  OE1   . GLN A 1 93  ? 181.312 153.247 130.359 1.00 42.73  ? 93  GLN A OE1   1 
ATOM   718   N  NE2   . GLN A 1 93  ? 181.350 155.222 129.291 1.00 36.98  ? 93  GLN A NE2   1 
ATOM   719   N  N     . LEU A 1 94  ? 182.062 155.863 135.097 1.00 23.17  ? 94  LEU A N     1 
ATOM   720   C  CA    . LEU A 1 94  ? 182.242 155.811 136.541 1.00 27.31  ? 94  LEU A CA    1 
ATOM   721   C  C     . LEU A 1 94  ? 181.833 154.439 137.066 1.00 30.80  ? 94  LEU A C     1 
ATOM   722   O  O     . LEU A 1 94  ? 180.767 153.933 136.698 1.00 23.86  ? 94  LEU A O     1 
ATOM   723   C  CB    . LEU A 1 94  ? 181.422 156.906 137.219 1.00 22.47  ? 94  LEU A CB    1 
ATOM   724   C  CG    . LEU A 1 94  ? 181.667 158.331 136.718 1.00 22.10  ? 94  LEU A CG    1 
ATOM   725   C  CD1   . LEU A 1 94  ? 180.664 159.298 137.326 1.00 22.81  ? 94  LEU A CD1   1 
ATOM   726   C  CD2   . LEU A 1 94  ? 183.091 158.770 137.019 1.00 19.01  ? 94  LEU A CD2   1 
ATOM   727   N  N     . PRO A 1 95  ? 182.641 153.811 137.915 1.00 29.60  ? 95  PRO A N     1 
ATOM   728   C  CA    . PRO A 1 95  ? 182.286 152.486 138.433 1.00 28.21  ? 95  PRO A CA    1 
ATOM   729   C  C     . PRO A 1 95  ? 181.171 152.574 139.464 1.00 26.02  ? 95  PRO A C     1 
ATOM   730   O  O     . PRO A 1 95  ? 180.768 153.650 139.908 1.00 30.25  ? 95  PRO A O     1 
ATOM   731   C  CB    . PRO A 1 95  ? 183.591 151.992 139.060 1.00 28.65  ? 95  PRO A CB    1 
ATOM   732   C  CG    . PRO A 1 95  ? 184.289 153.243 139.474 1.00 22.85  ? 95  PRO A CG    1 
ATOM   733   C  CD    . PRO A 1 95  ? 183.924 154.293 138.454 1.00 23.56  ? 95  PRO A CD    1 
ATOM   734   N  N     . GLY A 1 96  ? 180.664 151.402 139.838 1.00 25.52  ? 96  GLY A N     1 
ATOM   735   C  CA    . GLY A 1 96  ? 179.667 151.339 140.886 1.00 16.69  ? 96  GLY A CA    1 
ATOM   736   C  C     . GLY A 1 96  ? 180.230 151.770 142.227 1.00 24.32  ? 96  GLY A C     1 
ATOM   737   O  O     . GLY A 1 96  ? 181.419 151.623 142.509 1.00 33.22  ? 96  GLY A O     1 
ATOM   738   N  N     . LEU A 1 97  ? 179.354 152.316 143.064 1.00 17.29  ? 97  LEU A N     1 
ATOM   739   C  CA    . LEU A 1 97  ? 179.773 152.818 144.362 1.00 12.84  ? 97  LEU A CA    1 
ATOM   740   C  C     . LEU A 1 97  ? 180.128 151.666 145.298 1.00 22.78  ? 97  LEU A C     1 
ATOM   741   O  O     . LEU A 1 97  ? 179.691 150.526 145.123 1.00 29.74  ? 97  LEU A O     1 
ATOM   742   C  CB    . LEU A 1 97  ? 178.675 153.678 144.988 1.00 17.02  ? 97  LEU A CB    1 
ATOM   743   C  CG    . LEU A 1 97  ? 178.231 154.927 144.221 1.00 25.40  ? 97  LEU A CG    1 
ATOM   744   C  CD1   . LEU A 1 97  ? 177.601 155.939 145.165 1.00 18.65  ? 97  LEU A CD1   1 
ATOM   745   C  CD2   . LEU A 1 97  ? 179.393 155.548 143.465 1.00 22.41  ? 97  LEU A CD2   1 
ATOM   746   N  N     . SER A 1 98  ? 180.941 151.981 146.303 1.00 20.72  ? 98  SER A N     1 
ATOM   747   C  CA    . SER A 1 98  ? 181.271 151.009 147.331 1.00 17.22  ? 98  SER A CA    1 
ATOM   748   C  C     . SER A 1 98  ? 180.050 150.743 148.211 1.00 23.26  ? 98  SER A C     1 
ATOM   749   O  O     . SER A 1 98  ? 179.065 151.486 148.196 1.00 27.58  ? 98  SER A O     1 
ATOM   750   C  CB    . SER A 1 98  ? 182.446 151.499 148.176 1.00 20.03  ? 98  SER A CB    1 
ATOM   751   O  OG    . SER A 1 98  ? 182.092 152.645 148.929 1.00 27.83  ? 98  SER A OG    1 
ATOM   752   N  N     . TRP A 1 99  ? 180.124 149.659 148.987 1.00 18.61  ? 99  TRP A N     1 
ATOM   753   C  CA    . TRP A 1 99  ? 178.981 149.262 149.804 1.00 12.71  ? 99  TRP A CA    1 
ATOM   754   C  C     . TRP A 1 99  ? 178.641 150.325 150.842 1.00 14.60  ? 99  TRP A C     1 
ATOM   755   O  O     . TRP A 1 99  ? 177.462 150.616 151.077 1.00 24.62  ? 99  TRP A O     1 
ATOM   756   C  CB    . TRP A 1 99  ? 179.254 147.912 150.475 1.00 11.88  ? 99  TRP A CB    1 
ATOM   757   C  CG    . TRP A 1 99  ? 180.264 147.960 151.585 1.00 16.30  ? 99  TRP A CG    1 
ATOM   758   C  CD1   . TRP A 1 99  ? 181.606 147.738 151.483 1.00 15.70  ? 99  TRP A CD1   1 
ATOM   759   C  CD2   . TRP A 1 99  ? 180.010 148.247 152.967 1.00 17.65  ? 99  TRP A CD2   1 
ATOM   760   N  NE1   . TRP A 1 99  ? 182.203 147.870 152.712 1.00 27.12  ? 99  TRP A NE1   1 
ATOM   761   C  CE2   . TRP A 1 99  ? 181.245 148.184 153.640 1.00 19.04  ? 99  TRP A CE2   1 
ATOM   762   C  CE3   . TRP A 1 99  ? 178.858 148.555 153.698 1.00 15.84  ? 99  TRP A CE3   1 
ATOM   763   C  CZ2   . TRP A 1 99  ? 181.362 148.414 155.009 1.00 16.34  ? 99  TRP A CZ2   1 
ATOM   764   C  CZ3   . TRP A 1 99  ? 178.976 148.785 155.057 1.00 19.02  ? 99  TRP A CZ3   1 
ATOM   765   C  CH2   . TRP A 1 99  ? 180.218 148.713 155.698 1.00 20.69  ? 99  TRP A CH2   1 
ATOM   766   N  N     . ASP A 1 100 ? 179.656 150.923 151.470 1.00 16.07  ? 100 ASP A N     1 
ATOM   767   C  CA    . ASP A 1 100 ? 179.395 151.910 152.513 1.00 17.91  ? 100 ASP A CA    1 
ATOM   768   C  C     . ASP A 1 100 ? 178.913 153.229 151.923 1.00 15.27  ? 100 ASP A C     1 
ATOM   769   O  O     . ASP A 1 100 ? 178.006 153.866 152.473 1.00 19.47  ? 100 ASP A O     1 
ATOM   770   C  CB    . ASP A 1 100 ? 180.648 152.121 153.363 1.00 15.21  ? 100 ASP A CB    1 
ATOM   771   C  CG    . ASP A 1 100 ? 181.878 152.409 152.528 1.00 23.10  ? 100 ASP A CG    1 
ATOM   772   O  OD1   . ASP A 1 100 ? 182.290 151.524 151.749 1.00 26.68  ? 100 ASP A OD1   1 
ATOM   773   O  OD2   . ASP A 1 100 ? 182.435 153.520 152.651 1.00 29.65  ? 100 ASP A OD2   1 
ATOM   774   N  N     . LEU A 1 101 ? 179.510 153.662 150.810 1.00 15.44  ? 101 LEU A N     1 
ATOM   775   C  CA    . LEU A 1 101 ? 179.076 154.905 150.179 1.00 17.70  ? 101 LEU A CA    1 
ATOM   776   C  C     . LEU A 1 101 ? 177.671 154.773 149.604 1.00 14.18  ? 101 LEU A C     1 
ATOM   777   O  O     . LEU A 1 101 ? 176.853 155.691 149.737 1.00 14.38  ? 101 LEU A O     1 
ATOM   778   C  CB    . LEU A 1 101 ? 180.067 155.319 149.091 1.00 16.73  ? 101 LEU A CB    1 
ATOM   779   C  CG    . LEU A 1 101 ? 179.780 156.659 148.409 1.00 18.44  ? 101 LEU A CG    1 
ATOM   780   C  CD1   . LEU A 1 101 ? 179.737 157.784 149.432 1.00 19.09  ? 101 LEU A CD1   1 
ATOM   781   C  CD2   . LEU A 1 101 ? 180.810 156.951 147.329 1.00 13.19  ? 101 LEU A CD2   1 
ATOM   782   N  N     . ALA A 1 102 ? 177.375 153.644 148.955 1.00 16.19  ? 102 ALA A N     1 
ATOM   783   C  CA    . ALA A 1 102 ? 176.038 153.438 148.407 1.00 13.47  ? 102 ALA A CA    1 
ATOM   784   C  C     . ALA A 1 102 ? 174.992 153.364 149.512 1.00 15.23  ? 102 ALA A C     1 
ATOM   785   O  O     . ALA A 1 102 ? 173.904 153.937 149.386 1.00 16.09  ? 102 ALA A O     1 
ATOM   786   C  CB    . ALA A 1 102 ? 176.006 152.170 147.554 1.00 14.84  ? 102 ALA A CB    1 
ATOM   787   N  N     . LEU A 1 103 ? 175.302 152.657 150.602 1.00 16.98  ? 103 LEU A N     1 
ATOM   788   C  CA    . LEU A 1 103 ? 174.358 152.558 151.711 1.00 14.34  ? 103 LEU A CA    1 
ATOM   789   C  C     . LEU A 1 103 ? 174.102 153.921 152.342 1.00 13.80  ? 103 LEU A C     1 
ATOM   790   O  O     . LEU A 1 103 ? 172.954 154.268 152.641 1.00 16.75  ? 103 LEU A O     1 
ATOM   791   C  CB    . LEU A 1 103 ? 174.876 151.571 152.757 1.00 16.97  ? 103 LEU A CB    1 
ATOM   792   C  CG    . LEU A 1 103 ? 174.148 151.551 154.103 1.00 16.90  ? 103 LEU A CG    1 
ATOM   793   C  CD1   . LEU A 1 103 ? 172.722 151.048 153.937 1.00 10.19  ? 103 LEU A CD1   1 
ATOM   794   C  CD2   . LEU A 1 103 ? 174.905 150.701 155.111 1.00 17.18  ? 103 LEU A CD2   1 
ATOM   795   N  N     . ASN A 1 104 ? 175.160 154.707 152.550 1.00 6.73   ? 104 ASN A N     1 
ATOM   796   C  CA    . ASN A 1 104 ? 174.987 156.033 153.135 1.00 16.95  ? 104 ASN A CA    1 
ATOM   797   C  C     . ASN A 1 104 ? 174.186 156.944 152.213 1.00 10.05  ? 104 ASN A C     1 
ATOM   798   O  O     . ASN A 1 104 ? 173.288 157.662 152.667 1.00 17.31  ? 104 ASN A O     1 
ATOM   799   C  CB    . ASN A 1 104 ? 176.349 156.650 153.451 1.00 5.16   ? 104 ASN A CB    1 
ATOM   800   C  CG    . ASN A 1 104 ? 176.234 158.018 154.094 1.00 8.65   ? 104 ASN A CG    1 
ATOM   801   O  OD1   . ASN A 1 104 ? 176.226 159.039 153.408 1.00 19.33  ? 104 ASN A OD1   1 
ATOM   802   N  ND2   . ASN A 1 104 ? 176.144 158.046 155.418 1.00 16.44  ? 104 ASN A ND2   1 
ATOM   803   N  N     . THR A 1 105 ? 174.493 156.924 150.914 1.00 14.74  ? 105 THR A N     1 
ATOM   804   C  CA    . THR A 1 105 ? 173.779 157.779 149.970 1.00 10.66  ? 105 THR A CA    1 
ATOM   805   C  C     . THR A 1 105 ? 172.323 157.352 149.819 1.00 8.12   ? 105 THR A C     1 
ATOM   806   O  O     . THR A 1 105 ? 171.428 158.202 149.738 1.00 11.19  ? 105 THR A O     1 
ATOM   807   C  CB    . THR A 1 105 ? 174.485 157.768 148.614 1.00 7.44   ? 105 THR A CB    1 
ATOM   808   O  OG1   . THR A 1 105 ? 175.884 158.014 148.800 1.00 21.71  ? 105 THR A OG1   1 
ATOM   809   C  CG2   . THR A 1 105 ? 173.907 158.841 147.703 1.00 13.38  ? 105 THR A CG2   1 
ATOM   810   N  N     . ALA A 1 106 ? 172.066 156.042 149.771 1.00 8.31   ? 106 ALA A N     1 
ATOM   811   C  CA    . ALA A 1 106 ? 170.692 155.565 149.647 1.00 10.48  ? 106 ALA A CA    1 
ATOM   812   C  C     . ALA A 1 106 ? 169.864 155.937 150.871 1.00 9.20   ? 106 ALA A C     1 
ATOM   813   O  O     . ALA A 1 106 ? 168.716 156.376 150.742 1.00 17.76  ? 106 ALA A O     1 
ATOM   814   C  CB    . ALA A 1 106 ? 170.677 154.053 149.426 1.00 12.03  ? 106 ALA A CB    1 
ATOM   815   N  N     . VAL A 1 107 ? 170.431 155.767 152.067 1.00 7.70   ? 107 VAL A N     1 
ATOM   816   C  CA    . VAL A 1 107 ? 169.719 156.134 153.287 1.00 6.99   ? 107 VAL A CA    1 
ATOM   817   C  C     . VAL A 1 107 ? 169.539 157.645 153.366 1.00 12.06  ? 107 VAL A C     1 
ATOM   818   O  O     . VAL A 1 107 ? 168.486 158.138 153.790 1.00 12.99  ? 107 VAL A O     1 
ATOM   819   C  CB    . VAL A 1 107 ? 170.460 155.580 154.519 1.00 12.33  ? 107 VAL A CB    1 
ATOM   820   C  CG1   . VAL A 1 107 ? 169.959 156.239 155.797 1.00 10.24  ? 107 VAL A CG1   1 
ATOM   821   C  CG2   . VAL A 1 107 ? 170.302 154.069 154.598 1.00 11.05  ? 107 VAL A CG2   1 
ATOM   822   N  N     . SER A 1 108 ? 170.555 158.403 152.945 1.00 10.91  ? 108 SER A N     1 
ATOM   823   C  CA    . SER A 1 108 ? 170.511 159.857 153.068 1.00 15.97  ? 108 SER A CA    1 
ATOM   824   C  C     . SER A 1 108 ? 169.361 160.453 152.265 1.00 14.62  ? 108 SER A C     1 
ATOM   825   O  O     . SER A 1 108 ? 168.628 161.319 152.757 1.00 18.75  ? 108 SER A O     1 
ATOM   826   C  CB    . SER A 1 108 ? 171.844 160.455 152.618 1.00 9.20   ? 108 SER A CB    1 
ATOM   827   O  OG    . SER A 1 108 ? 171.927 161.823 152.958 1.00 26.73  ? 108 SER A OG    1 
ATOM   828   N  N     . PHE A 1 109 ? 169.188 160.005 151.022 1.00 8.01   ? 109 PHE A N     1 
ATOM   829   C  CA    . PHE A 1 109 ? 168.157 160.587 150.171 1.00 14.32  ? 109 PHE A CA    1 
ATOM   830   C  C     . PHE A 1 109 ? 166.769 160.049 150.493 1.00 13.35  ? 109 PHE A C     1 
ATOM   831   O  O     . PHE A 1 109 ? 165.775 160.757 150.295 1.00 14.71  ? 109 PHE A O     1 
ATOM   832   C  CB    . PHE A 1 109 ? 168.503 160.353 148.700 1.00 3.99   ? 109 PHE A CB    1 
ATOM   833   C  CG    . PHE A 1 109 ? 169.483 161.351 148.150 1.00 12.39  ? 109 PHE A CG    1 
ATOM   834   C  CD1   . PHE A 1 109 ? 170.809 161.330 148.550 1.00 7.82   ? 109 PHE A CD1   1 
ATOM   835   C  CD2   . PHE A 1 109 ? 169.076 162.319 147.247 1.00 6.80   ? 109 PHE A CD2   1 
ATOM   836   C  CE1   . PHE A 1 109 ? 171.713 162.250 148.054 1.00 15.12  ? 109 PHE A CE1   1 
ATOM   837   C  CE2   . PHE A 1 109 ? 169.976 163.242 146.748 1.00 5.94   ? 109 PHE A CE2   1 
ATOM   838   C  CZ    . PHE A 1 109 ? 171.295 163.208 147.153 1.00 16.85  ? 109 PHE A CZ    1 
ATOM   839   N  N     . VAL A 1 110 ? 166.677 158.812 150.985 1.00 9.25   ? 110 VAL A N     1 
ATOM   840   C  CA    . VAL A 1 110 ? 165.383 158.267 151.380 1.00 8.08   ? 110 VAL A CA    1 
ATOM   841   C  C     . VAL A 1 110 ? 164.854 158.986 152.617 1.00 5.58   ? 110 VAL A C     1 
ATOM   842   O  O     . VAL A 1 110 ? 163.654 159.266 152.723 1.00 12.17  ? 110 VAL A O     1 
ATOM   843   C  CB    . VAL A 1 110 ? 165.494 156.747 151.602 1.00 14.71  ? 110 VAL A CB    1 
ATOM   844   C  CG1   . VAL A 1 110 ? 164.344 156.236 152.458 1.00 16.49  ? 110 VAL A CG1   1 
ATOM   845   C  CG2   . VAL A 1 110 ? 165.526 156.026 150.267 1.00 15.14  ? 110 VAL A CG2   1 
ATOM   846   N  N     . THR A 1 111 ? 165.737 159.308 153.560 1.00 4.02   ? 111 THR A N     1 
ATOM   847   C  CA    . THR A 1 111 ? 165.356 159.972 154.800 1.00 13.96  ? 111 THR A CA    1 
ATOM   848   C  C     . THR A 1 111 ? 165.240 161.487 154.660 1.00 16.61  ? 111 THR A C     1 
ATOM   849   O  O     . THR A 1 111 ? 165.178 162.178 155.683 1.00 15.45  ? 111 THR A O     1 
ATOM   850   C  CB    . THR A 1 111 ? 166.360 159.639 155.909 1.00 5.70   ? 111 THR A CB    1 
ATOM   851   O  OG1   . THR A 1 111 ? 167.681 159.995 155.482 1.00 16.25  ? 111 THR A OG1   1 
ATOM   852   C  CG2   . THR A 1 111 ? 166.319 158.155 156.240 1.00 6.24   ? 111 THR A CG2   1 
ATOM   853   N  N     . ASN A 1 112 ? 165.218 162.010 153.432 1.00 11.49  ? 112 ASN A N     1 
ATOM   854   C  CA    . ASN A 1 112 ? 165.090 163.446 153.173 1.00 16.33  ? 112 ASN A CA    1 
ATOM   855   C  C     . ASN A 1 112 ? 166.232 164.243 153.802 1.00 11.23  ? 112 ASN A C     1 
ATOM   856   O  O     . ASN A 1 112 ? 166.062 165.407 154.170 1.00 3.58   ? 112 ASN A O     1 
ATOM   857   C  CB    . ASN A 1 112 ? 163.734 163.979 153.654 1.00 6.22   ? 112 ASN A CB    1 
ATOM   858   C  CG    . ASN A 1 112 ? 163.301 165.233 152.915 1.00 14.45  ? 112 ASN A CG    1 
ATOM   859   O  OD1   . ASN A 1 112 ? 162.918 166.227 153.530 1.00 17.71  ? 112 ASN A OD1   1 
ATOM   860   N  ND2   . ASN A 1 112 ? 163.360 165.190 151.590 1.00 25.60  ? 112 ASN A ND2   1 
ATOM   861   N  N     . THR A 1 113 ? 167.405 163.625 153.928 1.00 11.27  ? 113 THR A N     1 
ATOM   862   C  CA    . THR A 1 113 ? 168.585 164.284 154.476 1.00 6.55   ? 113 THR A CA    1 
ATOM   863   C  C     . THR A 1 113 ? 169.506 164.822 153.391 1.00 8.31   ? 113 THR A C     1 
ATOM   864   O  O     . THR A 1 113 ? 169.912 165.987 153.443 1.00 16.20  ? 113 THR A O     1 
ATOM   865   C  CB    . THR A 1 113 ? 169.370 163.320 155.373 1.00 12.13  ? 113 THR A CB    1 
ATOM   866   O  OG1   . THR A 1 113 ? 168.482 162.694 156.306 1.00 14.93  ? 113 THR A OG1   1 
ATOM   867   C  CG2   . THR A 1 113 ? 170.461 164.072 156.126 1.00 0.86   ? 113 THR A CG2   1 
ATOM   868   N  N     . ASN A 1 114 ? 169.844 163.984 152.409 1.00 16.77  ? 114 ASN A N     1 
ATOM   869   C  CA    . ASN A 1 114 ? 170.734 164.351 151.307 1.00 11.78  ? 114 ASN A CA    1 
ATOM   870   C  C     . ASN A 1 114 ? 172.113 164.774 151.808 1.00 21.02  ? 114 ASN A C     1 
ATOM   871   O  O     . ASN A 1 114 ? 172.739 165.685 151.265 1.00 19.98  ? 114 ASN A O     1 
ATOM   872   C  CB    . ASN A 1 114 ? 170.115 165.441 150.432 1.00 1.42   ? 114 ASN A CB    1 
ATOM   873   C  CG    . ASN A 1 114 ? 168.889 164.959 149.686 1.00 5.94   ? 114 ASN A CG    1 
ATOM   874   O  OD1   . ASN A 1 114 ? 168.182 164.062 150.144 1.00 15.88  ? 114 ASN A OD1   1 
ATOM   875   N  ND2   . ASN A 1 114 ? 168.634 165.548 148.526 1.00 14.57  ? 114 ASN A ND2   1 
ATOM   876   N  N     . TRP A 1 115 ? 172.590 164.109 152.857 1.00 25.52  ? 115 TRP A N     1 
ATOM   877   C  CA    . TRP A 1 115 ? 173.995 164.215 153.220 1.00 14.50  ? 115 TRP A CA    1 
ATOM   878   C  C     . TRP A 1 115 ? 174.842 163.580 152.125 1.00 7.05   ? 115 TRP A C     1 
ATOM   879   O  O     . TRP A 1 115 ? 174.527 162.497 151.625 1.00 26.52  ? 115 TRP A O     1 
ATOM   880   C  CB    . TRP A 1 115 ? 174.258 163.531 154.563 1.00 16.36  ? 115 TRP A CB    1 
ATOM   881   C  CG    . TRP A 1 115 ? 175.715 163.415 154.913 1.00 20.03  ? 115 TRP A CG    1 
ATOM   882   C  CD1   . TRP A 1 115 ? 176.591 162.458 154.484 1.00 21.47  ? 115 TRP A CD1   1 
ATOM   883   C  CD2   . TRP A 1 115 ? 176.464 164.285 155.770 1.00 12.31  ? 115 TRP A CD2   1 
ATOM   884   N  NE1   . TRP A 1 115 ? 177.836 162.683 155.016 1.00 18.93  ? 115 TRP A NE1   1 
ATOM   885   C  CE2   . TRP A 1 115 ? 177.785 163.798 155.809 1.00 15.00  ? 115 TRP A CE2   1 
ATOM   886   C  CE3   . TRP A 1 115 ? 176.145 165.430 156.505 1.00 23.06  ? 115 TRP A CE3   1 
ATOM   887   C  CZ2   . TRP A 1 115 ? 178.786 164.416 156.556 1.00 18.62  ? 115 TRP A CZ2   1 
ATOM   888   C  CZ3   . TRP A 1 115 ? 177.138 166.039 157.247 1.00 16.60  ? 115 TRP A CZ3   1 
ATOM   889   C  CH2   . TRP A 1 115 ? 178.443 165.533 157.266 1.00 10.79  ? 115 TRP A CH2   1 
ATOM   890   N  N     . GLN A 1 116 ? 175.922 164.258 151.747 1.00 12.22  ? 116 GLN A N     1 
ATOM   891   C  CA    . GLN A 1 116 ? 176.763 163.821 150.637 1.00 14.92  ? 116 GLN A CA    1 
ATOM   892   C  C     . GLN A 1 116 ? 178.218 163.818 151.082 1.00 22.19  ? 116 GLN A C     1 
ATOM   893   O  O     . GLN A 1 116 ? 178.781 164.875 151.385 1.00 31.27  ? 116 GLN A O     1 
ATOM   894   C  CB    . GLN A 1 116 ? 176.566 164.720 149.416 1.00 21.00  ? 116 GLN A CB    1 
ATOM   895   C  CG    . GLN A 1 116 ? 175.185 164.610 148.789 1.00 22.68  ? 116 GLN A CG    1 
ATOM   896   C  CD    . GLN A 1 116 ? 174.908 165.713 147.788 1.00 17.59  ? 116 GLN A CD    1 
ATOM   897   O  OE1   . GLN A 1 116 ? 174.840 166.888 148.145 1.00 23.84  ? 116 GLN A OE1   1 
ATOM   898   N  NE2   . GLN A 1 116 ? 174.748 165.339 146.525 1.00 16.21  ? 116 GLN A NE2   1 
ATOM   899   N  N     . SER A 1 117 ? 178.822 162.630 151.121 1.00 18.26  ? 117 SER A N     1 
ATOM   900   C  CA    . SER A 1 117 ? 180.244 162.471 151.394 1.00 26.83  ? 117 SER A CA    1 
ATOM   901   C  C     . SER A 1 117 ? 181.042 162.211 150.121 1.00 23.48  ? 117 SER A C     1 
ATOM   902   O  O     . SER A 1 117 ? 182.092 161.562 150.163 1.00 30.53  ? 117 SER A O     1 
ATOM   903   C  CB    . SER A 1 117 ? 180.468 161.348 152.407 1.00 17.47  ? 117 SER A CB    1 
ATOM   904   O  OG    . SER A 1 117 ? 180.151 160.085 151.849 1.00 29.84  ? 117 SER A OG    1 
ATOM   905   N  N     . TYR A 1 118 ? 180.556 162.708 148.986 1.00 23.86  ? 118 TYR A N     1 
ATOM   906   C  CA    . TYR A 1 118 ? 181.179 162.485 147.691 1.00 18.38  ? 118 TYR A CA    1 
ATOM   907   C  C     . TYR A 1 118 ? 181.088 163.766 146.873 1.00 19.88  ? 118 TYR A C     1 
ATOM   908   O  O     . TYR A 1 118 ? 180.458 164.746 147.280 1.00 34.37  ? 118 TYR A O     1 
ATOM   909   C  CB    . TYR A 1 118 ? 180.508 161.326 146.940 1.00 9.46   ? 118 TYR A CB    1 
ATOM   910   C  CG    . TYR A 1 118 ? 179.043 161.572 146.646 1.00 28.24  ? 118 TYR A CG    1 
ATOM   911   C  CD1   . TYR A 1 118 ? 178.061 161.213 147.561 1.00 19.88  ? 118 TYR A CD1   1 
ATOM   912   C  CD2   . TYR A 1 118 ? 178.642 162.171 145.458 1.00 16.67  ? 118 TYR A CD2   1 
ATOM   913   C  CE1   . TYR A 1 118 ? 176.724 161.441 147.300 1.00 15.22  ? 118 TYR A CE1   1 
ATOM   914   C  CE2   . TYR A 1 118 ? 177.309 162.405 145.190 1.00 16.55  ? 118 TYR A CE2   1 
ATOM   915   C  CZ    . TYR A 1 118 ? 176.353 162.037 146.113 1.00 18.09  ? 118 TYR A CZ    1 
ATOM   916   O  OH    . TYR A 1 118 ? 175.023 162.267 145.849 1.00 22.07  ? 118 TYR A OH    1 
ATOM   917   N  N     . SER A 1 119 ? 181.721 163.747 145.704 1.00 23.94  ? 119 SER A N     1 
ATOM   918   C  CA    . SER A 1 119 ? 181.605 164.817 144.721 1.00 17.70  ? 119 SER A CA    1 
ATOM   919   C  C     . SER A 1 119 ? 180.846 164.276 143.518 1.00 22.22  ? 119 SER A C     1 
ATOM   920   O  O     . SER A 1 119 ? 181.315 163.345 142.855 1.00 30.93  ? 119 SER A O     1 
ATOM   921   C  CB    . SER A 1 119 ? 182.981 165.340 144.307 1.00 22.71  ? 119 SER A CB    1 
ATOM   922   O  OG    . SER A 1 119 ? 183.753 165.692 145.441 1.00 39.89  ? 119 SER A OG    1 
ATOM   923   N  N     . GLY A 1 120 ? 179.686 164.869 143.232 1.00 24.20  ? 120 GLY A N     1 
ATOM   924   C  CA    . GLY A 1 120 ? 178.809 164.321 142.210 1.00 15.18  ? 120 GLY A CA    1 
ATOM   925   C  C     . GLY A 1 120 ? 179.412 164.315 140.820 1.00 18.38  ? 120 GLY A C     1 
ATOM   926   O  O     . GLY A 1 120 ? 179.140 163.410 140.027 1.00 31.85  ? 120 GLY A O     1 
ATOM   927   N  N     . GLU A 1 121 ? 180.236 165.316 140.502 1.00 20.60  ? 121 GLU A N     1 
ATOM   928   C  CA    . GLU A 1 121 ? 180.790 165.430 139.158 1.00 17.65  ? 121 GLU A CA    1 
ATOM   929   C  C     . GLU A 1 121 ? 181.749 164.296 138.816 1.00 19.44  ? 121 GLU A C     1 
ATOM   930   O  O     . GLU A 1 121 ? 182.005 164.057 137.631 1.00 21.74  ? 121 GLU A O     1 
ATOM   931   C  CB    . GLU A 1 121 ? 181.497 166.776 138.996 1.00 17.44  ? 121 GLU A CB    1 
ATOM   932   C  CG    . GLU A 1 121 ? 182.446 167.118 140.131 1.00 24.42  ? 121 GLU A CG    1 
ATOM   933   C  CD    . GLU A 1 121 ? 181.824 168.046 141.156 1.00 23.74  ? 121 GLU A CD    1 
ATOM   934   O  OE1   . GLU A 1 121 ? 180.955 167.587 141.925 1.00 23.96  ? 121 GLU A OE1   1 
ATOM   935   O  OE2   . GLU A 1 121 ? 182.207 169.234 141.193 1.00 30.22  ? 121 GLU A OE2   1 
ATOM   936   N  N     . THR A 1 122 ? 182.285 163.592 139.816 1.00 15.47  ? 122 THR A N     1 
ATOM   937   C  CA    . THR A 1 122 ? 183.210 162.492 139.572 1.00 20.27  ? 122 THR A CA    1 
ATOM   938   C  C     . THR A 1 122 ? 182.767 161.189 140.228 1.00 20.71  ? 122 THR A C     1 
ATOM   939   O  O     . THR A 1 122 ? 183.552 160.235 140.270 1.00 24.53  ? 122 THR A O     1 
ATOM   940   C  CB    . THR A 1 122 ? 184.621 162.853 140.054 1.00 20.37  ? 122 THR A CB    1 
ATOM   941   O  OG1   . THR A 1 122 ? 184.561 163.336 141.402 1.00 25.38  ? 122 THR A OG1   1 
ATOM   942   C  CG2   . THR A 1 122 ? 185.233 163.924 139.163 1.00 19.90  ? 122 THR A CG2   1 
ATOM   943   N  N     . THR A 1 123 ? 181.540 161.118 140.741 1.00 25.25  ? 123 THR A N     1 
ATOM   944   C  CA    . THR A 1 123 ? 181.057 159.927 141.430 1.00 16.48  ? 123 THR A CA    1 
ATOM   945   C  C     . THR A 1 123 ? 179.827 159.322 140.775 1.00 21.82  ? 123 THR A C     1 
ATOM   946   O  O     . THR A 1 123 ? 179.776 158.103 140.572 1.00 33.35  ? 123 THR A O     1 
ATOM   947   C  CB    . THR A 1 123 ? 180.751 160.256 142.901 1.00 20.12  ? 123 THR A CB    1 
ATOM   948   O  OG1   . THR A 1 123 ? 181.888 160.890 143.499 1.00 30.22  ? 123 THR A OG1   1 
ATOM   949   C  CG2   . THR A 1 123 ? 180.418 158.994 143.676 1.00 19.78  ? 123 THR A CG2   1 
ATOM   950   N  N     . LEU A 1 124 ? 178.835 160.135 140.430 1.00 22.57  ? 124 LEU A N     1 
ATOM   951   C  CA    . LEU A 1 124 ? 177.534 159.643 140.006 1.00 22.12  ? 124 LEU A CA    1 
ATOM   952   C  C     . LEU A 1 124 ? 177.297 159.907 138.525 1.00 17.02  ? 124 LEU A C     1 
ATOM   953   O  O     . LEU A 1 124 ? 177.723 160.928 137.978 1.00 28.35  ? 124 LEU A O     1 
ATOM   954   C  CB    . LEU A 1 124 ? 176.415 160.290 140.826 1.00 18.06  ? 124 LEU A CB    1 
ATOM   955   C  CG    . LEU A 1 124 ? 176.400 159.932 142.312 1.00 18.15  ? 124 LEU A CG    1 
ATOM   956   C  CD1   . LEU A 1 124 ? 175.205 160.564 142.998 1.00 20.07  ? 124 LEU A CD1   1 
ATOM   957   C  CD2   . LEU A 1 124 ? 176.393 158.423 142.498 1.00 18.86  ? 124 LEU A CD2   1 
ATOM   958   N  N     . SER A 1 125 ? 176.608 158.967 137.885 1.00 19.49  ? 125 SER A N     1 
ATOM   959   C  CA    . SER A 1 125 ? 176.195 159.110 136.501 1.00 18.04  ? 125 SER A CA    1 
ATOM   960   C  C     . SER A 1 125 ? 174.930 159.960 136.407 1.00 16.60  ? 125 SER A C     1 
ATOM   961   O  O     . SER A 1 125 ? 174.308 160.312 137.412 1.00 19.61  ? 125 SER A O     1 
ATOM   962   C  CB    . SER A 1 125 ? 175.954 157.740 135.871 1.00 4.02   ? 125 SER A CB    1 
ATOM   963   O  OG    . SER A 1 125 ? 174.812 157.115 136.430 1.00 19.46  ? 125 SER A OG    1 
ATOM   964   N  N     . TYR A 1 126 ? 174.550 160.289 135.171 1.00 18.26  ? 126 TYR A N     1 
ATOM   965   C  CA    . TYR A 1 126 ? 173.312 161.031 134.957 1.00 10.13  ? 126 TYR A CA    1 
ATOM   966   C  C     . TYR A 1 126 ? 172.103 160.209 135.383 1.00 18.67  ? 126 TYR A C     1 
ATOM   967   O  O     . TYR A 1 126 ? 171.145 160.747 135.949 1.00 22.01  ? 126 TYR A O     1 
ATOM   968   C  CB    . TYR A 1 126 ? 173.186 161.447 133.490 1.00 8.14   ? 126 TYR A CB    1 
ATOM   969   C  CG    . TYR A 1 126 ? 174.280 162.370 133.000 1.00 14.13  ? 126 TYR A CG    1 
ATOM   970   C  CD1   . TYR A 1 126 ? 175.120 163.026 133.891 1.00 13.04  ? 126 TYR A CD1   1 
ATOM   971   C  CD2   . TYR A 1 126 ? 174.470 162.588 131.641 1.00 14.70  ? 126 TYR A CD2   1 
ATOM   972   C  CE1   . TYR A 1 126 ? 176.119 163.866 133.444 1.00 11.24  ? 126 TYR A CE1   1 
ATOM   973   C  CE2   . TYR A 1 126 ? 175.464 163.429 131.185 1.00 13.98  ? 126 TYR A CE2   1 
ATOM   974   C  CZ    . TYR A 1 126 ? 176.286 164.065 132.090 1.00 14.51  ? 126 TYR A CZ    1 
ATOM   975   O  OH    . TYR A 1 126 ? 177.279 164.901 131.638 1.00 27.63  ? 126 TYR A OH    1 
ATOM   976   N  N     . PHE A 1 127 ? 172.129 158.902 135.111 1.00 23.45  ? 127 PHE A N     1 
ATOM   977   C  CA    . PHE A 1 127 ? 171.029 158.033 135.517 1.00 17.49  ? 127 PHE A CA    1 
ATOM   978   C  C     . PHE A 1 127 ? 170.887 157.991 137.033 1.00 12.87  ? 127 PHE A C     1 
ATOM   979   O  O     . PHE A 1 127 ? 169.770 158.033 137.561 1.00 21.63  ? 127 PHE A O     1 
ATOM   980   C  CB    . PHE A 1 127 ? 171.242 156.626 134.957 1.00 10.43  ? 127 PHE A CB    1 
ATOM   981   C  CG    . PHE A 1 127 ? 170.032 155.743 135.059 1.00 22.76  ? 127 PHE A CG    1 
ATOM   982   C  CD1   . PHE A 1 127 ? 169.051 155.774 134.082 1.00 24.73  ? 127 PHE A CD1   1 
ATOM   983   C  CD2   . PHE A 1 127 ? 169.877 154.878 136.129 1.00 18.57  ? 127 PHE A CD2   1 
ATOM   984   C  CE1   . PHE A 1 127 ? 167.938 154.961 134.172 1.00 23.73  ? 127 PHE A CE1   1 
ATOM   985   C  CE2   . PHE A 1 127 ? 168.766 154.063 136.225 1.00 19.15  ? 127 PHE A CE2   1 
ATOM   986   C  CZ    . PHE A 1 127 ? 167.795 154.105 135.245 1.00 20.67  ? 127 PHE A CZ    1 
ATOM   987   N  N     . SER A 1 128 ? 172.010 157.900 137.751 1.00 19.28  ? 128 SER A N     1 
ATOM   988   C  CA    . SER A 1 128 ? 171.957 157.885 139.209 1.00 9.24   ? 128 SER A CA    1 
ATOM   989   C  C     . SER A 1 128 ? 171.391 159.190 139.755 1.00 16.02  ? 128 SER A C     1 
ATOM   990   O  O     . SER A 1 128 ? 170.581 159.182 140.688 1.00 24.75  ? 128 SER A O     1 
ATOM   991   C  CB    . SER A 1 128 ? 173.349 157.623 139.783 1.00 14.31  ? 128 SER A CB    1 
ATOM   992   O  OG    . SER A 1 128 ? 173.779 156.303 139.500 1.00 32.32  ? 128 SER A OG    1 
ATOM   993   N  N     . GLN A 1 129 ? 171.814 160.323 139.190 1.00 17.21  ? 129 GLN A N     1 
ATOM   994   C  CA    . GLN A 1 129 ? 171.292 161.611 139.633 1.00 19.68  ? 129 GLN A CA    1 
ATOM   995   C  C     . GLN A 1 129 ? 169.815 161.762 139.291 1.00 14.48  ? 129 GLN A C     1 
ATOM   996   O  O     . GLN A 1 129 ? 169.032 162.273 140.100 1.00 18.19  ? 129 GLN A O     1 
ATOM   997   C  CB    . GLN A 1 129 ? 172.102 162.747 139.009 1.00 10.32  ? 129 GLN A CB    1 
ATOM   998   C  CG    . GLN A 1 129 ? 173.576 162.736 139.369 1.00 16.50  ? 129 GLN A CG    1 
ATOM   999   C  CD    . GLN A 1 129 ? 173.920 163.752 140.437 1.00 2.39   ? 129 GLN A CD    1 
ATOM   1000  O  OE1   . GLN A 1 129 ? 173.123 164.021 141.335 1.00 24.39  ? 129 GLN A OE1   1 
ATOM   1001  N  NE2   . GLN A 1 129 ? 175.114 164.324 140.346 1.00 14.49  ? 129 GLN A NE2   1 
ATOM   1002  N  N     . MET A 1 130 ? 169.415 161.318 138.099 1.00 16.13  ? 130 MET A N     1 
ATOM   1003  C  CA    . MET A 1 130 ? 168.056 161.554 137.624 1.00 16.63  ? 130 MET A CA    1 
ATOM   1004  C  C     . MET A 1 130 ? 167.078 160.521 138.176 1.00 23.78  ? 130 MET A C     1 
ATOM   1005  O  O     . MET A 1 130 ? 166.069 160.873 138.795 1.00 22.70  ? 130 MET A O     1 
ATOM   1006  C  CB    . MET A 1 130 ? 168.035 161.555 136.093 1.00 17.71  ? 130 MET A CB    1 
ATOM   1007  C  CG    . MET A 1 130 ? 166.672 161.820 135.487 1.00 22.29  ? 130 MET A CG    1 
ATOM   1008  S  SD    . MET A 1 130 ? 166.530 161.203 133.798 1.00 41.73  ? 130 MET A SD    1 
ATOM   1009  C  CE    . MET A 1 130 ? 167.370 159.629 133.940 1.00 24.17  ? 130 MET A CE    1 
ATOM   1010  N  N     . ALA A 1 131 ? 167.360 159.238 137.956 1.00 20.91  ? 131 ALA A N     1 
ATOM   1011  C  CA    . ALA A 1 131 ? 166.448 158.177 138.358 1.00 15.93  ? 131 ALA A CA    1 
ATOM   1012  C  C     . ALA A 1 131 ? 166.651 157.712 139.794 1.00 22.32  ? 131 ALA A C     1 
ATOM   1013  O  O     . ALA A 1 131 ? 165.770 157.036 140.337 1.00 27.98  ? 131 ALA A O     1 
ATOM   1014  C  CB    . ALA A 1 131 ? 166.585 156.978 137.415 1.00 17.04  ? 131 ALA A CB    1 
ATOM   1015  N  N     . GLY A 1 132 ? 167.777 158.044 140.420 1.00 14.85  ? 132 GLY A N     1 
ATOM   1016  C  CA    . GLY A 1 132 ? 168.028 157.586 141.772 1.00 20.24  ? 132 GLY A CA    1 
ATOM   1017  C  C     . GLY A 1 132 ? 167.887 158.649 142.841 1.00 13.98  ? 132 GLY A C     1 
ATOM   1018  O  O     . GLY A 1 132 ? 167.301 158.397 143.898 1.00 31.89  ? 132 GLY A O     1 
ATOM   1019  N  N     . LEU A 1 133 ? 168.408 159.846 142.578 1.00 17.44  ? 133 LEU A N     1 
ATOM   1020  C  CA    . LEU A 1 133 ? 168.400 160.914 143.571 1.00 13.80  ? 133 LEU A CA    1 
ATOM   1021  C  C     . LEU A 1 133 ? 167.162 161.796 143.455 1.00 15.77  ? 133 LEU A C     1 
ATOM   1022  O  O     . LEU A 1 133 ? 166.519 162.101 144.464 1.00 12.61  ? 133 LEU A O     1 
ATOM   1023  C  CB    . LEU A 1 133 ? 169.665 161.768 143.438 1.00 13.47  ? 133 LEU A CB    1 
ATOM   1024  C  CG    . LEU A 1 133 ? 171.011 161.089 143.695 1.00 22.87  ? 133 LEU A CG    1 
ATOM   1025  C  CD1   . LEU A 1 133 ? 172.088 162.137 143.908 1.00 20.42  ? 133 LEU A CD1   1 
ATOM   1026  C  CD2   . LEU A 1 133 ? 170.936 160.144 144.884 1.00 14.48  ? 133 LEU A CD2   1 
ATOM   1027  N  N     . THR A 1 134 ? 166.823 162.215 142.234 1.00 14.27  ? 134 THR A N     1 
ATOM   1028  C  CA    . THR A 1 134 ? 165.657 163.071 142.041 1.00 17.83  ? 134 THR A CA    1 
ATOM   1029  C  C     . THR A 1 134 ? 164.372 162.346 142.422 1.00 3.16   ? 134 THR A C     1 
ATOM   1030  O  O     . THR A 1 134 ? 163.446 162.955 142.968 1.00 25.26  ? 134 THR A O     1 
ATOM   1031  C  CB    . THR A 1 134 ? 165.595 163.555 140.592 1.00 18.16  ? 134 THR A CB    1 
ATOM   1032  O  OG1   . THR A 1 134 ? 166.862 164.108 140.218 1.00 20.34  ? 134 THR A OG1   1 
ATOM   1033  C  CG2   . THR A 1 134 ? 164.517 164.615 140.426 1.00 6.00   ? 134 THR A CG2   1 
ATOM   1034  N  N     . VAL A 1 135 ? 164.298 161.043 142.139 1.00 20.93  ? 135 VAL A N     1 
ATOM   1035  C  CA    . VAL A 1 135 ? 163.111 160.269 142.494 1.00 18.67  ? 135 VAL A CA    1 
ATOM   1036  C  C     . VAL A 1 135 ? 162.907 160.276 144.004 1.00 19.41  ? 135 VAL A C     1 
ATOM   1037  O  O     . VAL A 1 135 ? 161.799 160.510 144.499 1.00 20.80  ? 135 VAL A O     1 
ATOM   1038  C  CB    . VAL A 1 135 ? 163.221 158.836 141.945 1.00 16.18  ? 135 VAL A CB    1 
ATOM   1039  C  CG1   . VAL A 1 135 ? 162.215 157.922 142.628 1.00 10.64  ? 135 VAL A CG1   1 
ATOM   1040  C  CG2   . VAL A 1 135 ? 163.016 158.832 140.442 1.00 15.30  ? 135 VAL A CG2   1 
ATOM   1041  N  N     . GLN A 1 136 ? 163.980 160.033 144.760 1.00 10.49  ? 136 GLN A N     1 
ATOM   1042  C  CA    . GLN A 1 136 ? 163.880 160.074 146.213 1.00 15.53  ? 136 GLN A CA    1 
ATOM   1043  C  C     . GLN A 1 136 ? 163.680 161.488 146.739 1.00 7.58   ? 136 GLN A C     1 
ATOM   1044  O  O     . GLN A 1 136 ? 163.136 161.654 147.834 1.00 15.41  ? 136 GLN A O     1 
ATOM   1045  C  CB    . GLN A 1 136 ? 165.120 159.446 146.848 1.00 9.75   ? 136 GLN A CB    1 
ATOM   1046  C  CG    . GLN A 1 136 ? 165.047 157.933 146.946 1.00 14.14  ? 136 GLN A CG    1 
ATOM   1047  C  CD    . GLN A 1 136 ? 163.758 157.455 147.587 1.00 20.79  ? 136 GLN A CD    1 
ATOM   1048  O  OE1   . GLN A 1 136 ? 163.331 157.978 148.616 1.00 23.41  ? 136 GLN A OE1   1 
ATOM   1049  N  NE2   . GLN A 1 136 ? 163.128 156.459 146.976 1.00 20.48  ? 136 GLN A NE2   1 
ATOM   1050  N  N     . ASN A 1 137 ? 164.105 162.507 145.988 1.00 12.86  ? 137 ASN A N     1 
ATOM   1051  C  CA    . ASN A 1 137 ? 163.803 163.879 146.380 1.00 4.53   ? 137 ASN A CA    1 
ATOM   1052  C  C     . ASN A 1 137 ? 162.299 164.122 146.384 1.00 17.92  ? 137 ASN A C     1 
ATOM   1053  O  O     . ASN A 1 137 ? 161.772 164.790 147.281 1.00 18.26  ? 137 ASN A O     1 
ATOM   1054  C  CB    . ASN A 1 137 ? 164.506 164.863 145.445 1.00 10.48  ? 137 ASN A CB    1 
ATOM   1055  C  CG    . ASN A 1 137 ? 165.920 165.184 145.889 1.00 5.00   ? 137 ASN A CG    1 
ATOM   1056  O  OD1   . ASN A 1 137 ? 166.429 164.610 146.851 1.00 20.45  ? 137 ASN A OD1   1 
ATOM   1057  N  ND2   . ASN A 1 137 ? 166.563 166.108 145.188 1.00 18.16  ? 137 ASN A ND2   1 
ATOM   1058  N  N     . PHE A 1 138 ? 161.592 163.588 145.386 1.00 11.17  ? 138 PHE A N     1 
ATOM   1059  C  CA    . PHE A 1 138 ? 160.138 163.701 145.363 1.00 16.59  ? 138 PHE A CA    1 
ATOM   1060  C  C     . PHE A 1 138 ? 159.493 162.803 146.412 1.00 7.77   ? 138 PHE A C     1 
ATOM   1061  O  O     . PHE A 1 138 ? 158.581 163.232 147.128 1.00 11.24  ? 138 PHE A O     1 
ATOM   1062  C  CB    . PHE A 1 138 ? 159.606 163.351 143.973 1.00 12.41  ? 138 PHE A CB    1 
ATOM   1063  C  CG    . PHE A 1 138 ? 159.724 164.467 142.975 1.00 8.34   ? 138 PHE A CG    1 
ATOM   1064  C  CD1   . PHE A 1 138 ? 158.775 165.473 142.924 1.00 9.72   ? 138 PHE A CD1   1 
ATOM   1065  C  CD2   . PHE A 1 138 ? 160.780 164.501 142.079 1.00 9.84   ? 138 PHE A CD2   1 
ATOM   1066  C  CE1   . PHE A 1 138 ? 158.881 166.498 142.003 1.00 8.56   ? 138 PHE A CE1   1 
ATOM   1067  C  CE2   . PHE A 1 138 ? 160.890 165.522 141.156 1.00 11.85  ? 138 PHE A CE2   1 
ATOM   1068  C  CZ    . PHE A 1 138 ? 159.939 166.522 141.118 1.00 10.15  ? 138 PHE A CZ    1 
ATOM   1069  N  N     . LEU A 1 139 ? 159.954 161.554 146.518 1.00 11.55  ? 139 LEU A N     1 
ATOM   1070  C  CA    . LEU A 1 139 ? 159.273 160.579 147.367 1.00 12.97  ? 139 LEU A CA    1 
ATOM   1071  C  C     . LEU A 1 139 ? 159.478 160.878 148.847 1.00 4.38   ? 139 LEU A C     1 
ATOM   1072  O  O     . LEU A 1 139 ? 158.525 160.813 149.633 1.00 11.61  ? 139 LEU A O     1 
ATOM   1073  C  CB    . LEU A 1 139 ? 159.754 159.168 147.031 1.00 11.04  ? 139 LEU A CB    1 
ATOM   1074  C  CG    . LEU A 1 139 ? 159.349 158.626 145.657 1.00 20.41  ? 139 LEU A CG    1 
ATOM   1075  C  CD1   . LEU A 1 139 ? 159.509 157.115 145.604 1.00 18.62  ? 139 LEU A CD1   1 
ATOM   1076  C  CD2   . LEU A 1 139 ? 157.924 159.030 145.310 1.00 15.56  ? 139 LEU A CD2   1 
ATOM   1077  N  N     . SER A 1 140 ? 160.711 161.197 149.251 1.00 11.78  ? 140 SER A N     1 
ATOM   1078  C  CA    . SER A 1 140 ? 160.969 161.494 150.657 1.00 8.86   ? 140 SER A CA    1 
ATOM   1079  C  C     . SER A 1 140 ? 160.208 162.734 151.106 1.00 13.45  ? 140 SER A C     1 
ATOM   1080  O  O     . SER A 1 140 ? 159.679 162.776 152.223 1.00 20.07  ? 140 SER A O     1 
ATOM   1081  C  CB    . SER A 1 140 ? 162.469 161.669 150.895 1.00 4.09   ? 140 SER A CB    1 
ATOM   1082  O  OG    . SER A 1 140 ? 162.959 162.823 150.237 1.00 15.71  ? 140 SER A OG    1 
ATOM   1083  N  N     . ALA A 1 141 ? 160.154 163.760 150.253 1.00 15.56  ? 141 ALA A N     1 
ATOM   1084  C  CA    . ALA A 1 141 ? 159.390 164.957 150.585 1.00 10.92  ? 141 ALA A CA    1 
ATOM   1085  C  C     . ALA A 1 141 ? 157.903 164.648 150.702 1.00 10.84  ? 141 ALA A C     1 
ATOM   1086  O  O     . ALA A 1 141 ? 157.230 165.134 151.618 1.00 12.28  ? 141 ALA A O     1 
ATOM   1087  C  CB    . ALA A 1 141 ? 159.633 166.043 149.537 1.00 5.02   ? 141 ALA A CB    1 
ATOM   1088  N  N     . ALA A 1 142 ? 157.371 163.837 149.783 1.00 9.45   ? 142 ALA A N     1 
ATOM   1089  C  CA    . ALA A 1 142 ? 155.958 163.483 149.839 1.00 11.21  ? 142 ALA A CA    1 
ATOM   1090  C  C     . ALA A 1 142 ? 155.635 162.644 151.067 1.00 14.31  ? 142 ALA A C     1 
ATOM   1091  O  O     . ALA A 1 142 ? 154.532 162.750 151.614 1.00 18.20  ? 142 ALA A O     1 
ATOM   1092  C  CB    . ALA A 1 142 ? 155.548 162.741 148.567 1.00 3.62   ? 142 ALA A CB    1 
ATOM   1093  N  N     . SER A 1 143 ? 156.575 161.803 151.508 1.00 18.58  ? 143 SER A N     1 
ATOM   1094  C  CA    . SER A 1 143 ? 156.350 161.003 152.708 1.00 11.15  ? 143 SER A CA    1 
ATOM   1095  C  C     . SER A 1 143 ? 156.185 161.886 153.939 1.00 10.14  ? 143 SER A C     1 
ATOM   1096  O  O     . SER A 1 143 ? 155.310 161.638 154.776 1.00 20.22  ? 143 SER A O     1 
ATOM   1097  C  CB    . SER A 1 143 ? 157.502 160.017 152.905 1.00 13.12  ? 143 SER A CB    1 
ATOM   1098  O  OG    . SER A 1 143 ? 157.695 159.218 151.752 1.00 18.87  ? 143 SER A OG    1 
ATOM   1099  N  N     . GLY A 1 144 ? 157.018 162.921 154.066 1.00 12.08  ? 144 GLY A N     1 
ATOM   1100  C  CA    . GLY A 1 144 ? 156.891 163.823 155.199 1.00 12.25  ? 144 GLY A CA    1 
ATOM   1101  C  C     . GLY A 1 144 ? 155.598 164.615 155.176 1.00 11.95  ? 144 GLY A C     1 
ATOM   1102  O  O     . GLY A 1 144 ? 154.954 164.799 156.213 1.00 21.62  ? 144 GLY A O     1 
ATOM   1103  N  N     . ILE A 1 145 ? 155.201 165.097 153.996 1.00 13.17  ? 145 ILE A N     1 
ATOM   1104  C  CA    . ILE A 1 145 ? 153.944 165.829 153.874 1.00 16.31  ? 145 ILE A CA    1 
ATOM   1105  C  C     . ILE A 1 145 ? 152.755 164.909 154.123 1.00 15.59  ? 145 ILE A C     1 
ATOM   1106  O  O     . ILE A 1 145 ? 151.735 165.336 154.677 1.00 25.46  ? 145 ILE A O     1 
ATOM   1107  C  CB    . ILE A 1 145 ? 153.857 166.514 152.497 1.00 19.12  ? 145 ILE A CB    1 
ATOM   1108  C  CG1   . ILE A 1 145 ? 155.083 167.402 152.269 1.00 17.77  ? 145 ILE A CG1   1 
ATOM   1109  C  CG2   . ILE A 1 145 ? 152.588 167.344 152.386 1.00 13.83  ? 145 ILE A CG2   1 
ATOM   1110  C  CD1   . ILE A 1 145 ? 155.309 167.775 150.821 1.00 12.22  ? 145 ILE A CD1   1 
ATOM   1111  N  N     . ALA A 1 146 ? 152.853 163.642 153.716 1.00 11.80  ? 146 ALA A N     1 
ATOM   1112  C  CA    . ALA A 1 146 ? 151.766 162.701 153.968 1.00 16.20  ? 146 ALA A CA    1 
ATOM   1113  C  C     . ALA A 1 146 ? 151.567 162.472 155.462 1.00 13.21  ? 146 ALA A C     1 
ATOM   1114  O  O     . ALA A 1 146 ? 150.429 162.360 155.934 1.00 16.24  ? 146 ALA A O     1 
ATOM   1115  C  CB    . ALA A 1 146 ? 152.036 161.378 153.254 1.00 9.20   ? 146 ALA A CB    1 
ATOM   1116  N  N     . VAL A 1 147 ? 152.661 162.390 156.221 1.00 13.03  ? 147 VAL A N     1 
ATOM   1117  C  CA    . VAL A 1 147 ? 152.557 162.133 157.654 1.00 18.33  ? 147 VAL A CA    1 
ATOM   1118  C  C     . VAL A 1 147 ? 151.874 163.298 158.362 1.00 15.15  ? 147 VAL A C     1 
ATOM   1119  O  O     . VAL A 1 147 ? 150.991 163.099 159.205 1.00 20.47  ? 147 VAL A O     1 
ATOM   1120  C  CB    . VAL A 1 147 ? 153.947 161.842 158.250 1.00 15.28  ? 147 VAL A CB    1 
ATOM   1121  C  CG1   . VAL A 1 147 ? 153.881 161.842 159.767 1.00 13.58  ? 147 VAL A CG1   1 
ATOM   1122  C  CG2   . VAL A 1 147 ? 154.473 160.511 157.740 1.00 18.65  ? 147 VAL A CG2   1 
ATOM   1123  N  N     . ILE A 1 148 ? 152.269 164.531 158.033 1.00 8.24   ? 148 ILE A N     1 
ATOM   1124  C  CA    . ILE A 1 148 ? 151.648 165.689 158.670 1.00 18.22  ? 148 ILE A CA    1 
ATOM   1125  C  C     . ILE A 1 148 ? 150.187 165.818 158.252 1.00 11.99  ? 148 ILE A C     1 
ATOM   1126  O  O     . ILE A 1 148 ? 149.376 166.399 158.983 1.00 19.04  ? 148 ILE A O     1 
ATOM   1127  C  CB    . ILE A 1 148 ? 152.448 166.973 158.369 1.00 19.19  ? 148 ILE A CB    1 
ATOM   1128  C  CG1   . ILE A 1 148 ? 152.022 168.103 159.308 1.00 14.56  ? 148 ILE A CG1   1 
ATOM   1129  C  CG2   . ILE A 1 148 ? 152.269 167.409 156.929 1.00 14.21  ? 148 ILE A CG2   1 
ATOM   1130  C  CD1   . ILE A 1 148 ? 151.994 167.715 160.767 1.00 20.04  ? 148 ILE A CD1   1 
ATOM   1131  N  N     . PHE A 1 149 ? 149.824 165.284 157.082 1.00 10.60  ? 149 PHE A N     1 
ATOM   1132  C  CA    . PHE A 1 149 ? 148.417 165.244 156.696 1.00 17.08  ? 149 PHE A CA    1 
ATOM   1133  C  C     . PHE A 1 149 ? 147.610 164.395 157.671 1.00 18.40  ? 149 PHE A C     1 
ATOM   1134  O  O     . PHE A 1 149 ? 146.502 164.774 158.068 1.00 25.40  ? 149 PHE A O     1 
ATOM   1135  C  CB    . PHE A 1 149 ? 148.274 164.699 155.274 1.00 9.51   ? 149 PHE A CB    1 
ATOM   1136  C  CG    . PHE A 1 149 ? 148.441 165.737 154.199 1.00 16.95  ? 149 PHE A CG    1 
ATOM   1137  C  CD1   . PHE A 1 149 ? 149.054 166.949 154.468 1.00 16.96  ? 149 PHE A CD1   1 
ATOM   1138  C  CD2   . PHE A 1 149 ? 147.986 165.494 152.913 1.00 23.61  ? 149 PHE A CD2   1 
ATOM   1139  C  CE1   . PHE A 1 149 ? 149.208 167.899 153.477 1.00 13.29  ? 149 PHE A CE1   1 
ATOM   1140  C  CE2   . PHE A 1 149 ? 148.138 166.440 151.917 1.00 17.25  ? 149 PHE A CE2   1 
ATOM   1141  C  CZ    . PHE A 1 149 ? 148.750 167.644 152.200 1.00 19.02  ? 149 PHE A CZ    1 
ATOM   1142  N  N     . ALA A 1 150 ? 148.152 163.240 158.066 1.00 14.36  ? 150 ALA A N     1 
ATOM   1143  C  CA    . ALA A 1 150 ? 147.457 162.376 159.013 1.00 21.24  ? 150 ALA A CA    1 
ATOM   1144  C  C     . ALA A 1 150 ? 147.332 163.034 160.382 1.00 20.45  ? 150 ALA A C     1 
ATOM   1145  O  O     . ALA A 1 150 ? 146.282 162.936 161.028 1.00 29.44  ? 150 ALA A O     1 
ATOM   1146  C  CB    . ALA A 1 150 ? 148.180 161.034 159.126 1.00 13.56  ? 150 ALA A CB    1 
ATOM   1147  N  N     . LEU A 1 151 ? 148.393 163.702 160.844 1.00 10.01  ? 151 LEU A N     1 
ATOM   1148  C  CA    . LEU A 1 151 ? 148.342 164.359 162.146 1.00 18.94  ? 151 LEU A CA    1 
ATOM   1149  C  C     . LEU A 1 151 ? 147.335 165.502 162.156 1.00 15.90  ? 151 LEU A C     1 
ATOM   1150  O  O     . LEU A 1 151 ? 146.604 165.682 163.137 1.00 24.33  ? 151 LEU A O     1 
ATOM   1151  C  CB    . LEU A 1 151 ? 149.730 164.866 162.538 1.00 16.15  ? 151 LEU A CB    1 
ATOM   1152  C  CG    . LEU A 1 151 ? 149.825 165.475 163.939 1.00 15.01  ? 151 LEU A CG    1 
ATOM   1153  C  CD1   . LEU A 1 151 ? 149.561 164.421 165.003 1.00 8.22   ? 151 LEU A CD1   1 
ATOM   1154  C  CD2   . LEU A 1 151 ? 151.176 166.133 164.156 1.00 17.90  ? 151 LEU A CD2   1 
ATOM   1155  N  N     . ILE A 1 152 ? 147.287 166.290 161.079 1.00 11.22  ? 152 ILE A N     1 
ATOM   1156  C  CA    . ILE A 1 152 ? 146.315 167.377 160.997 1.00 20.51  ? 152 ILE A CA    1 
ATOM   1157  C  C     . ILE A 1 152 ? 144.898 166.819 160.973 1.00 14.01  ? 152 ILE A C     1 
ATOM   1158  O  O     . ILE A 1 152 ? 143.991 167.355 161.622 1.00 23.60  ? 152 ILE A O     1 
ATOM   1159  C  CB    . ILE A 1 152 ? 146.602 168.262 159.769 1.00 20.79  ? 152 ILE A CB    1 
ATOM   1160  C  CG1   . ILE A 1 152 ? 147.862 169.099 160.000 1.00 16.65  ? 152 ILE A CG1   1 
ATOM   1161  C  CG2   . ILE A 1 152 ? 145.417 169.168 159.467 1.00 15.68  ? 152 ILE A CG2   1 
ATOM   1162  C  CD1   . ILE A 1 152 ? 148.244 169.966 158.823 1.00 14.59  ? 152 ILE A CD1   1 
ATOM   1163  N  N     . ARG A 1 153 ? 144.686 165.728 160.231 1.00 15.64  ? 153 ARG A N     1 
ATOM   1164  C  CA    . ARG A 1 153 ? 143.371 165.096 160.199 1.00 20.77  ? 153 ARG A CA    1 
ATOM   1165  C  C     . ARG A 1 153 ? 142.965 164.574 161.571 1.00 21.15  ? 153 ARG A C     1 
ATOM   1166  O  O     . ARG A 1 153 ? 141.775 164.567 161.902 1.00 27.97  ? 153 ARG A O     1 
ATOM   1167  C  CB    . ARG A 1 153 ? 143.357 163.961 159.176 1.00 15.44  ? 153 ARG A CB    1 
ATOM   1168  C  CG    . ARG A 1 153 ? 143.221 164.425 157.737 1.00 15.43  ? 153 ARG A CG    1 
ATOM   1169  C  CD    . ARG A 1 153 ? 143.222 163.248 156.778 1.00 17.37  ? 153 ARG A CD    1 
ATOM   1170  N  NE    . ARG A 1 153 ? 143.323 163.680 155.389 1.00 29.44  ? 153 ARG A NE    1 
ATOM   1171  C  CZ    . ARG A 1 153 ? 144.150 163.152 154.499 1.00 20.41  ? 153 ARG A CZ    1 
ATOM   1172  N  NH1   . ARG A 1 153 ? 144.965 162.159 154.816 1.00 19.28  ? 153 ARG A NH1   1 
ATOM   1173  N  NH2   . ARG A 1 153 ? 144.160 163.631 153.258 1.00 21.97  ? 153 ARG A NH2   1 
ATOM   1174  N  N     . ALA A 1 154 ? 143.934 164.138 162.379 1.00 17.06  ? 154 ALA A N     1 
ATOM   1175  C  CA    . ALA A 1 154 ? 143.617 163.625 163.708 1.00 20.37  ? 154 ALA A CA    1 
ATOM   1176  C  C     . ALA A 1 154 ? 142.992 164.703 164.585 1.00 25.89  ? 154 ALA A C     1 
ATOM   1177  O  O     . ALA A 1 154 ? 142.077 164.425 165.368 1.00 30.68  ? 154 ALA A O     1 
ATOM   1178  C  CB    . ALA A 1 154 ? 144.875 163.060 164.366 1.00 18.77  ? 154 ALA A CB    1 
ATOM   1179  N  N     . PHE A 1 155 ? 143.480 165.940 164.474 1.00 30.10  ? 155 PHE A N     1 
ATOM   1180  C  CA    . PHE A 1 155 ? 142.920 167.029 165.268 1.00 24.89  ? 155 PHE A CA    1 
ATOM   1181  C  C     . PHE A 1 155 ? 141.526 167.416 164.785 1.00 28.25  ? 155 PHE A C     1 
ATOM   1182  O  O     . PHE A 1 155 ? 140.651 167.737 165.596 1.00 36.83  ? 155 PHE A O     1 
ATOM   1183  C  CB    . PHE A 1 155 ? 143.853 168.239 165.230 1.00 23.70  ? 155 PHE A CB    1 
ATOM   1184  C  CG    . PHE A 1 155 ? 145.024 168.132 166.163 1.00 24.89  ? 155 PHE A CG    1 
ATOM   1185  C  CD1   . PHE A 1 155 ? 144.862 168.335 167.524 1.00 31.26  ? 155 PHE A CD1   1 
ATOM   1186  C  CD2   . PHE A 1 155 ? 146.286 167.829 165.681 1.00 24.13  ? 155 PHE A CD2   1 
ATOM   1187  C  CE1   . PHE A 1 155 ? 145.938 168.239 168.386 1.00 28.53  ? 155 PHE A CE1   1 
ATOM   1188  C  CE2   . PHE A 1 155 ? 147.365 167.731 166.538 1.00 25.86  ? 155 PHE A CE2   1 
ATOM   1189  C  CZ    . PHE A 1 155 ? 147.191 167.937 167.892 1.00 28.44  ? 155 PHE A CZ    1 
ATOM   1190  N  N     . THR A 1 156 ? 141.301 167.394 163.471 1.00 22.04  ? 156 THR A N     1 
ATOM   1191  C  CA    . THR A 1 156 ? 140.053 167.884 162.899 1.00 20.99  ? 156 THR A CA    1 
ATOM   1192  C  C     . THR A 1 156 ? 138.968 166.819 162.790 1.00 28.86  ? 156 THR A C     1 
ATOM   1193  O  O     . THR A 1 156 ? 137.824 167.160 162.470 1.00 39.25  ? 156 THR A O     1 
ATOM   1194  C  CB    . THR A 1 156 ? 140.306 168.486 161.511 1.00 27.35  ? 156 THR A CB    1 
ATOM   1195  O  OG1   . THR A 1 156 ? 139.189 169.298 161.131 1.00 37.90  ? 156 THR A OG1   1 
ATOM   1196  C  CG2   . THR A 1 156 ? 140.498 167.387 160.478 1.00 26.79  ? 156 THR A CG2   1 
ATOM   1197  N  N     . ARG A 1 157 ? 139.283 165.553 163.046 1.00 27.47  ? 157 ARG A N     1 
ATOM   1198  C  CA    . ARG A 1 157 ? 138.305 164.478 162.958 1.00 26.14  ? 157 ARG A CA    1 
ATOM   1199  C  C     . ARG A 1 157 ? 137.823 164.096 164.351 1.00 31.68  ? 157 ARG A C     1 
ATOM   1200  O  O     . ARG A 1 157 ? 138.598 164.100 165.312 1.00 28.39  ? 157 ARG A O     1 
ATOM   1201  C  CB    . ARG A 1 157 ? 138.893 163.256 162.250 1.00 27.06  ? 157 ARG A CB    1 
ATOM   1202  C  CG    . ARG A 1 157 ? 139.005 163.421 160.742 1.00 21.76  ? 157 ARG A CG    1 
ATOM   1203  C  CD    . ARG A 1 157 ? 139.582 162.180 160.084 1.00 21.21  ? 157 ARG A CD    1 
ATOM   1204  N  NE    . ARG A 1 157 ? 139.691 162.336 158.638 1.00 24.45  ? 157 ARG A NE    1 
ATOM   1205  C  CZ    . ARG A 1 157 ? 139.809 161.331 157.783 1.00 29.97  ? 157 ARG A CZ    1 
ATOM   1206  N  NH1   . ARG A 1 157 ? 139.834 160.073 158.193 1.00 33.02  ? 157 ARG A NH1   1 
ATOM   1207  N  NH2   . ARG A 1 157 ? 139.904 161.593 156.483 1.00 29.50  ? 157 ARG A NH2   1 
ATOM   1208  N  N     . GLN A 1 158 ? 136.538 163.771 164.454 1.00 35.64  ? 158 GLN A N     1 
ATOM   1209  C  CA    . GLN A 1 158 ? 135.889 163.491 165.728 1.00 30.61  ? 158 GLN A CA    1 
ATOM   1210  C  C     . GLN A 1 158 ? 135.489 162.023 165.787 1.00 32.15  ? 158 GLN A C     1 
ATOM   1211  O  O     . GLN A 1 158 ? 134.719 161.554 164.942 1.00 40.22  ? 158 GLN A O     1 
ATOM   1212  C  CB    . GLN A 1 158 ? 134.664 164.385 165.920 1.00 28.45  ? 158 GLN A CB    1 
ATOM   1213  C  CG    . GLN A 1 158 ? 134.891 165.837 165.544 1.00 30.75  ? 158 GLN A CG    1 
ATOM   1214  C  CD    . GLN A 1 158 ? 135.655 166.597 166.608 1.00 35.68  ? 158 GLN A CD    1 
ATOM   1215  O  OE1   . GLN A 1 158 ? 135.313 166.542 167.788 1.00 43.33  ? 158 GLN A OE1   1 
ATOM   1216  N  NE2   . GLN A 1 158 ? 136.696 167.310 166.195 1.00 33.48  ? 158 GLN A NE2   1 
ATOM   1217  N  N     . SER A 1 159 ? 136.005 161.312 166.792 1.00 25.10  ? 159 SER A N     1 
ATOM   1218  C  CA    . SER A 1 159 ? 135.607 159.932 167.082 1.00 29.13  ? 159 SER A CA    1 
ATOM   1219  C  C     . SER A 1 159 ? 135.756 159.030 165.859 1.00 30.56  ? 159 SER A C     1 
ATOM   1220  O  O     . SER A 1 159 ? 134.877 158.227 165.540 1.00 37.51  ? 159 SER A O     1 
ATOM   1221  C  CB    . SER A 1 159 ? 134.178 159.882 167.625 1.00 38.68  ? 159 SER A CB    1 
ATOM   1222  O  OG    . SER A 1 159 ? 134.027 160.741 168.741 1.00 35.47  ? 159 SER A OG    1 
ATOM   1223  N  N     . MET A 1 160 ? 136.884 159.162 165.168 1.00 32.94  ? 160 MET A N     1 
ATOM   1224  C  CA    . MET A 1 160 ? 137.177 158.367 163.986 1.00 31.29  ? 160 MET A CA    1 
ATOM   1225  C  C     . MET A 1 160 ? 138.431 157.537 164.222 1.00 28.93  ? 160 MET A C     1 
ATOM   1226  O  O     . MET A 1 160 ? 139.328 157.935 164.971 1.00 42.33  ? 160 MET A O     1 
ATOM   1227  C  CB    . MET A 1 160 ? 137.356 159.253 162.748 1.00 28.03  ? 160 MET A CB    1 
ATOM   1228  C  CG    . MET A 1 160 ? 136.084 159.959 162.309 1.00 28.76  ? 160 MET A CG    1 
ATOM   1229  S  SD    . MET A 1 160 ? 136.288 160.889 160.779 1.00 47.11  ? 160 MET A SD    1 
ATOM   1230  C  CE    . MET A 1 160 ? 136.700 159.574 159.636 1.00 31.44  ? 160 MET A CE    1 
ATOM   1231  N  N     . SER A 1 161 ? 138.481 156.370 163.582 1.00 30.62  ? 161 SER A N     1 
ATOM   1232  C  CA    . SER A 1 161 ? 139.602 155.449 163.719 1.00 34.53  ? 161 SER A CA    1 
ATOM   1233  C  C     . SER A 1 161 ? 140.489 155.409 162.481 1.00 32.80  ? 161 SER A C     1 
ATOM   1234  O  O     . SER A 1 161 ? 141.393 154.571 162.407 1.00 39.53  ? 161 SER A O     1 
ATOM   1235  C  CB    . SER A 1 161 ? 139.091 154.043 164.041 1.00 35.15  ? 161 SER A CB    1 
ATOM   1236  O  OG    . SER A 1 161 ? 138.026 153.678 163.182 1.00 38.29  ? 161 SER A OG    1 
ATOM   1237  N  N     . THR A 1 162 ? 140.257 156.289 161.510 1.00 28.23  ? 162 THR A N     1 
ATOM   1238  C  CA    . THR A 1 162 ? 141.014 156.301 160.268 1.00 24.90  ? 162 THR A CA    1 
ATOM   1239  C  C     . THR A 1 162 ? 141.535 157.706 159.998 1.00 26.77  ? 162 THR A C     1 
ATOM   1240  O  O     . THR A 1 162 ? 140.993 158.699 160.490 1.00 38.44  ? 162 THR A O     1 
ATOM   1241  C  CB    . THR A 1 162 ? 140.166 155.819 159.084 1.00 31.91  ? 162 THR A CB    1 
ATOM   1242  O  OG1   . THR A 1 162 ? 138.946 156.568 159.030 1.00 37.62  ? 162 THR A OG1   1 
ATOM   1243  C  CG2   . THR A 1 162 ? 139.841 154.338 159.225 1.00 24.02  ? 162 THR A CG2   1 
ATOM   1244  N  N     . LEU A 1 163 ? 142.604 157.777 159.202 1.00 27.30  ? 163 LEU A N     1 
ATOM   1245  C  CA    . LEU A 1 163 ? 143.292 159.033 158.925 1.00 21.72  ? 163 LEU A CA    1 
ATOM   1246  C  C     . LEU A 1 163 ? 143.484 159.253 157.429 1.00 24.33  ? 163 LEU A C     1 
ATOM   1247  O  O     . LEU A 1 163 ? 144.447 159.901 157.011 1.00 29.12  ? 163 LEU A O     1 
ATOM   1248  C  CB    . LEU A 1 163 ? 144.640 159.082 159.644 1.00 20.01  ? 163 LEU A CB    1 
ATOM   1249  C  CG    . LEU A 1 163 ? 144.603 159.035 161.172 1.00 27.95  ? 163 LEU A CG    1 
ATOM   1250  C  CD1   . LEU A 1 163 ? 145.927 158.535 161.729 1.00 24.78  ? 163 LEU A CD1   1 
ATOM   1251  C  CD2   . LEU A 1 163 ? 144.261 160.402 161.738 1.00 20.80  ? 163 LEU A CD2   1 
ATOM   1252  N  N     . GLY A 1 164 ? 142.580 158.729 156.610 1.00 25.75  ? 164 GLY A N     1 
ATOM   1253  C  CA    . GLY A 1 164 ? 142.704 158.865 155.174 1.00 20.35  ? 164 GLY A CA    1 
ATOM   1254  C  C     . GLY A 1 164 ? 143.486 157.728 154.549 1.00 23.81  ? 164 GLY A C     1 
ATOM   1255  O  O     . GLY A 1 164 ? 143.842 156.737 155.191 1.00 30.52  ? 164 GLY A O     1 
ATOM   1256  N  N     . ASN A 1 165 ? 143.758 157.886 153.256 1.00 24.08  ? 165 ASN A N     1 
ATOM   1257  C  CA    . ASN A 1 165 ? 144.477 156.892 152.468 1.00 20.52  ? 165 ASN A CA    1 
ATOM   1258  C  C     . ASN A 1 165 ? 145.870 157.422 152.153 1.00 22.28  ? 165 ASN A C     1 
ATOM   1259  O  O     . ASN A 1 165 ? 146.009 158.511 151.586 1.00 24.84  ? 165 ASN A O     1 
ATOM   1260  C  CB    . ASN A 1 165 ? 143.719 156.564 151.181 1.00 23.50  ? 165 ASN A CB    1 
ATOM   1261  C  CG    . ASN A 1 165 ? 144.246 155.320 150.495 1.00 25.86  ? 165 ASN A CG    1 
ATOM   1262  O  OD1   . ASN A 1 165 ? 145.224 155.375 149.750 1.00 32.26  ? 165 ASN A OD1   1 
ATOM   1263  N  ND2   . ASN A 1 165 ? 143.598 154.188 150.741 1.00 32.38  ? 165 ASN A ND2   1 
ATOM   1264  N  N     . ALA A 1 166 ? 146.896 156.648 152.516 1.00 23.59  ? 166 ALA A N     1 
ATOM   1265  C  CA    . ALA A 1 166 ? 148.270 157.094 152.307 1.00 16.01  ? 166 ALA A CA    1 
ATOM   1266  C  C     . ALA A 1 166 ? 148.641 157.099 150.829 1.00 22.68  ? 166 ALA A C     1 
ATOM   1267  O  O     . ALA A 1 166 ? 149.342 158.006 150.365 1.00 22.51  ? 166 ALA A O     1 
ATOM   1268  C  CB    . ALA A 1 166 ? 149.234 156.213 153.101 1.00 11.01  ? 166 ALA A CB    1 
ATOM   1269  N  N     . TRP A 1 167 ? 148.189 156.093 150.076 1.00 20.17  ? 167 TRP A N     1 
ATOM   1270  C  CA    . TRP A 1 167 ? 148.512 156.033 148.653 1.00 18.79  ? 167 TRP A CA    1 
ATOM   1271  C  C     . TRP A 1 167 ? 147.895 157.203 147.897 1.00 21.14  ? 167 TRP A C     1 
ATOM   1272  O  O     . TRP A 1 167 ? 148.532 157.785 147.011 1.00 24.12  ? 167 TRP A O     1 
ATOM   1273  C  CB    . TRP A 1 167 ? 148.044 154.704 148.060 1.00 21.25  ? 167 TRP A CB    1 
ATOM   1274  C  CG    . TRP A 1 167 ? 148.522 153.502 148.818 1.00 21.65  ? 167 TRP A CG    1 
ATOM   1275  C  CD1   . TRP A 1 167 ? 147.751 152.506 149.342 1.00 20.64  ? 167 TRP A CD1   1 
ATOM   1276  C  CD2   . TRP A 1 167 ? 149.880 153.166 149.134 1.00 23.14  ? 167 TRP A CD2   1 
ATOM   1277  N  NE1   . TRP A 1 167 ? 148.542 151.573 149.966 1.00 25.69  ? 167 TRP A NE1   1 
ATOM   1278  C  CE2   . TRP A 1 167 ? 149.853 151.955 149.852 1.00 20.12  ? 167 TRP A CE2   1 
ATOM   1279  C  CE3   . TRP A 1 167 ? 151.115 153.771 148.880 1.00 21.48  ? 167 TRP A CE3   1 
ATOM   1280  C  CZ2   . TRP A 1 167 ? 151.012 151.338 150.320 1.00 20.01  ? 167 TRP A CZ2   1 
ATOM   1281  C  CZ3   . TRP A 1 167 ? 152.263 153.159 149.346 1.00 22.69  ? 167 TRP A CZ3   1 
ATOM   1282  C  CH2   . TRP A 1 167 ? 152.204 151.955 150.058 1.00 23.22  ? 167 TRP A CH2   1 
ATOM   1283  N  N     . VAL A 1 168 ? 146.652 157.558 148.230 1.00 24.20  ? 168 VAL A N     1 
ATOM   1284  C  CA    . VAL A 1 168 ? 146.015 158.712 147.603 1.00 26.78  ? 168 VAL A CA    1 
ATOM   1285  C  C     . VAL A 1 168 ? 146.772 159.989 147.949 1.00 22.02  ? 168 VAL A C     1 
ATOM   1286  O  O     . VAL A 1 168 ? 147.010 160.841 147.084 1.00 27.65  ? 168 VAL A O     1 
ATOM   1287  C  CB    . VAL A 1 168 ? 144.534 158.794 148.020 1.00 23.47  ? 168 VAL A CB    1 
ATOM   1288  C  CG1   . VAL A 1 168 ? 144.019 160.219 147.902 1.00 23.79  ? 168 VAL A CG1   1 
ATOM   1289  C  CG2   . VAL A 1 168 ? 143.696 157.852 147.175 1.00 21.26  ? 168 VAL A CG2   1 
ATOM   1290  N  N     . ASP A 1 169 ? 147.167 160.138 149.216 1.00 11.60  ? 169 ASP A N     1 
ATOM   1291  C  CA    . ASP A 1 169 ? 147.893 161.334 149.632 1.00 16.84  ? 169 ASP A CA    1 
ATOM   1292  C  C     . ASP A 1 169 ? 149.230 161.452 148.911 1.00 18.28  ? 169 ASP A C     1 
ATOM   1293  O  O     . ASP A 1 169 ? 149.598 162.537 148.447 1.00 28.74  ? 169 ASP A O     1 
ATOM   1294  C  CB    . ASP A 1 169 ? 148.103 161.322 151.146 1.00 17.69  ? 169 ASP A CB    1 
ATOM   1295  C  CG    . ASP A 1 169 ? 146.806 161.460 151.916 1.00 26.30  ? 169 ASP A CG    1 
ATOM   1296  O  OD1   . ASP A 1 169 ? 145.865 162.091 151.391 1.00 34.83  ? 169 ASP A OD1   1 
ATOM   1297  O  OD2   . ASP A 1 169 ? 146.727 160.936 153.046 1.00 27.21  ? 169 ASP A OD2   1 
ATOM   1298  N  N     . LEU A 1 170 ? 149.972 160.347 148.809 1.00 12.57  ? 170 LEU A N     1 
ATOM   1299  C  CA    . LEU A 1 170 ? 151.272 160.387 148.147 1.00 15.18  ? 170 LEU A CA    1 
ATOM   1300  C  C     . LEU A 1 170 ? 151.133 160.754 146.675 1.00 20.38  ? 170 LEU A C     1 
ATOM   1301  O  O     . LEU A 1 170 ? 151.915 161.555 146.150 1.00 17.31  ? 170 LEU A O     1 
ATOM   1302  C  CB    . LEU A 1 170 ? 151.982 159.042 148.299 1.00 14.41  ? 170 LEU A CB    1 
ATOM   1303  C  CG    . LEU A 1 170 ? 152.547 158.714 149.681 1.00 22.99  ? 170 LEU A CG    1 
ATOM   1304  C  CD1   . LEU A 1 170 ? 152.888 157.235 149.782 1.00 19.26  ? 170 LEU A CD1   1 
ATOM   1305  C  CD2   . LEU A 1 170 ? 153.765 159.572 149.984 1.00 13.62  ? 170 LEU A CD2   1 
ATOM   1306  N  N     . LEU A 1 171 ? 150.145 160.173 145.991 1.00 18.90  ? 171 LEU A N     1 
ATOM   1307  C  CA    . LEU A 1 171 ? 149.936 160.488 144.582 1.00 20.42  ? 171 LEU A CA    1 
ATOM   1308  C  C     . LEU A 1 171 ? 149.507 161.938 144.394 1.00 13.20  ? 171 LEU A C     1 
ATOM   1309  O  O     . LEU A 1 171 ? 149.999 162.623 143.491 1.00 27.47  ? 171 LEU A O     1 
ATOM   1310  C  CB    . LEU A 1 171 ? 148.899 159.537 143.984 1.00 17.04  ? 171 LEU A CB    1 
ATOM   1311  C  CG    . LEU A 1 171 ? 149.369 158.101 143.741 1.00 24.68  ? 171 LEU A CG    1 
ATOM   1312  C  CD1   . LEU A 1 171 ? 148.182 157.178 143.512 1.00 25.32  ? 171 LEU A CD1   1 
ATOM   1313  C  CD2   . LEU A 1 171 ? 150.336 158.041 142.570 1.00 17.36  ? 171 LEU A CD2   1 
ATOM   1314  N  N     . ARG A 1 172 ? 148.590 162.422 145.235 1.00 20.07  ? 172 ARG A N     1 
ATOM   1315  C  CA    . ARG A 1 172 ? 148.099 163.789 145.090 1.00 21.15  ? 172 ARG A CA    1 
ATOM   1316  C  C     . ARG A 1 172 ? 149.190 164.810 145.390 1.00 20.82  ? 172 ARG A C     1 
ATOM   1317  O  O     . ARG A 1 172 ? 149.307 165.824 144.692 1.00 22.51  ? 172 ARG A O     1 
ATOM   1318  C  CB    . ARG A 1 172 ? 146.890 164.010 145.998 1.00 22.65  ? 172 ARG A CB    1 
ATOM   1319  C  CG    . ARG A 1 172 ? 145.630 163.294 145.538 1.00 20.32  ? 172 ARG A CG    1 
ATOM   1320  C  CD    . ARG A 1 172 ? 144.386 164.117 145.823 1.00 27.93  ? 172 ARG A CD    1 
ATOM   1321  N  NE    . ARG A 1 172 ? 143.728 163.710 147.059 1.00 35.63  ? 172 ARG A NE    1 
ATOM   1322  C  CZ    . ARG A 1 172 ? 142.479 163.274 147.134 1.00 32.26  ? 172 ARG A CZ    1 
ATOM   1323  N  NH1   . ARG A 1 172 ? 141.719 163.163 146.057 1.00 27.45  ? 172 ARG A NH1   1 
ATOM   1324  N  NH2   . ARG A 1 172 ? 141.979 162.939 148.320 1.00 33.18  ? 172 ARG A NH2   1 
ATOM   1325  N  N     . ILE A 1 173 ? 149.994 164.564 146.426 1.00 17.09  ? 173 ILE A N     1 
ATOM   1326  C  CA    . ILE A 1 173 ? 151.050 165.504 146.791 1.00 18.48  ? 173 ILE A CA    1 
ATOM   1327  C  C     . ILE A 1 173 ? 152.099 165.584 145.688 1.00 18.40  ? 173 ILE A C     1 
ATOM   1328  O  O     . ILE A 1 173 ? 152.520 166.675 145.285 1.00 16.67  ? 173 ILE A O     1 
ATOM   1329  C  CB    . ILE A 1 173 ? 151.678 165.107 148.139 1.00 19.03  ? 173 ILE A CB    1 
ATOM   1330  C  CG1   . ILE A 1 173 ? 150.739 165.461 149.294 1.00 20.38  ? 173 ILE A CG1   1 
ATOM   1331  C  CG2   . ILE A 1 173 ? 153.031 165.779 148.325 1.00 13.49  ? 173 ILE A CG2   1 
ATOM   1332  C  CD1   . ILE A 1 173 ? 150.953 164.618 150.533 1.00 16.47  ? 173 ILE A CD1   1 
ATOM   1333  N  N     . THR A 1 174 ? 152.535 164.430 145.180 1.00 19.57  ? 174 THR A N     1 
ATOM   1334  C  CA    . THR A 1 174 ? 153.603 164.416 144.186 1.00 15.59  ? 174 THR A CA    1 
ATOM   1335  C  C     . THR A 1 174 ? 153.126 164.960 142.844 1.00 22.34  ? 174 THR A C     1 
ATOM   1336  O  O     . THR A 1 174 ? 153.783 165.818 142.243 1.00 22.68  ? 174 THR A O     1 
ATOM   1337  C  CB    . THR A 1 174 ? 154.149 162.996 144.026 1.00 18.07  ? 174 THR A CB    1 
ATOM   1338  O  OG1   . THR A 1 174 ? 154.408 162.432 145.317 1.00 26.66  ? 174 THR A OG1   1 
ATOM   1339  C  CG2   . THR A 1 174 ? 155.437 163.007 143.216 1.00 21.32  ? 174 THR A CG2   1 
ATOM   1340  N  N     . LEU A 1 175 ? 151.980 164.478 142.361 1.00 18.83  ? 175 LEU A N     1 
ATOM   1341  C  CA    . LEU A 1 175 ? 151.557 164.795 141.000 1.00 19.06  ? 175 LEU A CA    1 
ATOM   1342  C  C     . LEU A 1 175 ? 150.988 166.205 140.880 1.00 22.40  ? 175 LEU A C     1 
ATOM   1343  O  O     . LEU A 1 175 ? 151.243 166.891 139.884 1.00 27.09  ? 175 LEU A O     1 
ATOM   1344  C  CB    . LEU A 1 175 ? 150.529 163.771 140.518 1.00 20.12  ? 175 LEU A CB    1 
ATOM   1345  C  CG    . LEU A 1 175 ? 151.026 162.329 140.401 1.00 23.71  ? 175 LEU A CG    1 
ATOM   1346  C  CD1   . LEU A 1 175 ? 149.854 161.375 140.258 1.00 24.59  ? 175 LEU A CD1   1 
ATOM   1347  C  CD2   . LEU A 1 175 ? 151.988 162.182 139.233 1.00 25.03  ? 175 LEU A CD2   1 
ATOM   1348  N  N     . TRP A 1 176 ? 150.216 166.656 141.868 1.00 19.04  ? 176 TRP A N     1 
ATOM   1349  C  CA    . TRP A 1 176 ? 149.517 167.929 141.757 1.00 21.77  ? 176 TRP A CA    1 
ATOM   1350  C  C     . TRP A 1 176 ? 150.234 169.087 142.439 1.00 22.12  ? 176 TRP A C     1 
ATOM   1351  O  O     . TRP A 1 176 ? 149.860 170.241 142.208 1.00 29.37  ? 176 TRP A O     1 
ATOM   1352  C  CB    . TRP A 1 176 ? 148.097 167.814 142.330 1.00 20.86  ? 176 TRP A CB    1 
ATOM   1353  C  CG    . TRP A 1 176 ? 147.314 166.616 141.858 1.00 24.19  ? 176 TRP A CG    1 
ATOM   1354  C  CD1   . TRP A 1 176 ? 146.577 165.770 142.634 1.00 28.59  ? 176 TRP A CD1   1 
ATOM   1355  C  CD2   . TRP A 1 176 ? 147.177 166.140 140.510 1.00 24.62  ? 176 TRP A CD2   1 
ATOM   1356  N  NE1   . TRP A 1 176 ? 145.997 164.797 141.859 1.00 28.65  ? 176 TRP A NE1   1 
ATOM   1357  C  CE2   . TRP A 1 176 ? 146.349 165.001 140.552 1.00 28.08  ? 176 TRP A CE2   1 
ATOM   1358  C  CE3   . TRP A 1 176 ? 147.676 166.565 139.273 1.00 26.26  ? 176 TRP A CE3   1 
ATOM   1359  C  CZ2   . TRP A 1 176 ? 146.010 164.281 139.408 1.00 29.26  ? 176 TRP A CZ2   1 
ATOM   1360  C  CZ3   . TRP A 1 176 ? 147.338 165.848 138.140 1.00 31.86  ? 176 TRP A CZ3   1 
ATOM   1361  C  CH2   . TRP A 1 176 ? 146.513 164.720 138.215 1.00 26.52  ? 176 TRP A CH2   1 
ATOM   1362  N  N     . VAL A 1 177 ? 151.241 168.820 143.269 1.00 20.70  ? 177 VAL A N     1 
ATOM   1363  C  CA    . VAL A 1 177 ? 151.920 169.893 143.989 1.00 15.63  ? 177 VAL A CA    1 
ATOM   1364  C  C     . VAL A 1 177 ? 153.410 169.887 143.673 1.00 17.52  ? 177 VAL A C     1 
ATOM   1365  O  O     . VAL A 1 177 ? 153.949 170.873 143.161 1.00 25.90  ? 177 VAL A O     1 
ATOM   1366  C  CB    . VAL A 1 177 ? 151.683 169.783 145.506 1.00 17.88  ? 177 VAL A CB    1 
ATOM   1367  C  CG1   . VAL A 1 177 ? 152.490 170.839 146.246 1.00 16.41  ? 177 VAL A CG1   1 
ATOM   1368  C  CG2   . VAL A 1 177 ? 150.203 169.919 145.824 1.00 13.07  ? 177 VAL A CG2   1 
ATOM   1369  N  N     . LEU A 1 178 ? 154.086 168.777 143.978 1.00 18.40  ? 178 LEU A N     1 
ATOM   1370  C  CA    . LEU A 1 178 ? 155.540 168.736 143.849 1.00 6.77   ? 178 LEU A CA    1 
ATOM   1371  C  C     . LEU A 1 178 ? 155.978 168.852 142.393 1.00 17.51  ? 178 LEU A C     1 
ATOM   1372  O  O     . LEU A 1 178 ? 156.834 169.678 142.058 1.00 20.68  ? 178 LEU A O     1 
ATOM   1373  C  CB    . LEU A 1 178 ? 156.085 167.452 144.474 1.00 14.22  ? 178 LEU A CB    1 
ATOM   1374  C  CG    . LEU A 1 178 ? 155.946 167.315 145.992 1.00 18.82  ? 178 LEU A CG    1 
ATOM   1375  C  CD1   . LEU A 1 178 ? 156.711 166.101 146.495 1.00 9.66   ? 178 LEU A CD1   1 
ATOM   1376  C  CD2   . LEU A 1 178 ? 156.416 168.579 146.693 1.00 5.48   ? 178 LEU A CD2   1 
ATOM   1377  N  N     . VAL A 1 179 ? 155.403 168.028 141.513 1.00 20.58  ? 179 VAL A N     1 
ATOM   1378  C  CA    . VAL A 1 179 ? 155.845 168.011 140.116 1.00 19.36  ? 179 VAL A CA    1 
ATOM   1379  C  C     . VAL A 1 179 ? 155.573 169.329 139.396 1.00 15.53  ? 179 VAL A C     1 
ATOM   1380  O  O     . VAL A 1 179 ? 156.504 169.869 138.777 1.00 14.90  ? 179 VAL A O     1 
ATOM   1381  C  CB    . VAL A 1 179 ? 155.237 166.800 139.386 1.00 15.91  ? 179 VAL A CB    1 
ATOM   1382  C  CG1   . VAL A 1 179 ? 155.304 166.996 137.879 1.00 12.04  ? 179 VAL A CG1   1 
ATOM   1383  C  CG2   . VAL A 1 179 ? 155.956 165.523 139.791 1.00 15.73  ? 179 VAL A CG2   1 
ATOM   1384  N  N     . PRO A 1 180 ? 154.358 169.897 139.424 1.00 22.80  ? 180 PRO A N     1 
ATOM   1385  C  CA    . PRO A 1 180 ? 154.136 171.118 138.630 1.00 16.70  ? 180 PRO A CA    1 
ATOM   1386  C  C     . PRO A 1 180 ? 154.896 172.326 139.147 1.00 17.45  ? 180 PRO A C     1 
ATOM   1387  O  O     . PRO A 1 180 ? 155.362 173.145 138.345 1.00 16.90  ? 180 PRO A O     1 
ATOM   1388  C  CB    . PRO A 1 180 ? 152.616 171.318 138.713 1.00 19.13  ? 180 PRO A CB    1 
ATOM   1389  C  CG    . PRO A 1 180 ? 152.225 170.660 139.975 1.00 20.51  ? 180 PRO A CG    1 
ATOM   1390  C  CD    . PRO A 1 180 ? 153.125 169.471 140.113 1.00 16.16  ? 180 PRO A CD    1 
ATOM   1391  N  N     . VAL A 1 181 ? 155.034 172.469 140.467 1.00 10.85  ? 181 VAL A N     1 
ATOM   1392  C  CA    . VAL A 1 181 ? 155.767 173.606 141.013 1.00 15.66  ? 181 VAL A CA    1 
ATOM   1393  C  C     . VAL A 1 181 ? 157.255 173.483 140.702 1.00 17.04  ? 181 VAL A C     1 
ATOM   1394  O  O     . VAL A 1 181 ? 157.917 174.472 140.368 1.00 18.73  ? 181 VAL A O     1 
ATOM   1395  C  CB    . VAL A 1 181 ? 155.505 173.736 142.525 1.00 14.13  ? 181 VAL A CB    1 
ATOM   1396  C  CG1   . VAL A 1 181 ? 156.395 174.808 143.135 1.00 11.31  ? 181 VAL A CG1   1 
ATOM   1397  C  CG2   . VAL A 1 181 ? 154.040 174.058 142.779 1.00 14.38  ? 181 VAL A CG2   1 
ATOM   1398  N  N     . ALA A 1 182 ? 157.802 172.269 140.801 1.00 9.45   ? 182 ALA A N     1 
ATOM   1399  C  CA    . ALA A 1 182 ? 159.214 172.067 140.488 1.00 17.24  ? 182 ALA A CA    1 
ATOM   1400  C  C     . ALA A 1 182 ? 159.499 172.338 139.016 1.00 9.84   ? 182 ALA A C     1 
ATOM   1401  O  O     . ALA A 1 182 ? 160.559 172.873 138.671 1.00 19.62  ? 182 ALA A O     1 
ATOM   1402  C  CB    . ALA A 1 182 ? 159.641 170.648 140.865 1.00 8.28   ? 182 ALA A CB    1 
ATOM   1403  N  N     . LEU A 1 183 ? 158.567 171.972 138.133 1.00 10.37  ? 183 LEU A N     1 
ATOM   1404  C  CA    . LEU A 1 183 ? 158.770 172.203 136.707 1.00 15.82  ? 183 LEU A CA    1 
ATOM   1405  C  C     . LEU A 1 183 ? 158.888 173.691 136.396 1.00 15.50  ? 183 LEU A C     1 
ATOM   1406  O  O     . LEU A 1 183 ? 159.758 174.103 135.620 1.00 22.67  ? 183 LEU A O     1 
ATOM   1407  C  CB    . LEU A 1 183 ? 157.628 171.577 135.907 1.00 15.17  ? 183 LEU A CB    1 
ATOM   1408  C  CG    . LEU A 1 183 ? 157.699 171.736 134.387 1.00 22.41  ? 183 LEU A CG    1 
ATOM   1409  C  CD1   . LEU A 1 183 ? 158.978 171.120 133.841 1.00 15.43  ? 183 LEU A CD1   1 
ATOM   1410  C  CD2   . LEU A 1 183 ? 156.477 171.120 133.724 1.00 23.73  ? 183 LEU A CD2   1 
ATOM   1411  N  N     . LEU A 1 184 ? 158.021 174.513 136.993 1.00 13.75  ? 184 LEU A N     1 
ATOM   1412  C  CA    . LEU A 1 184 ? 158.098 175.954 136.776 1.00 18.29  ? 184 LEU A CA    1 
ATOM   1413  C  C     . LEU A 1 184 ? 159.388 176.533 137.344 1.00 15.69  ? 184 LEU A C     1 
ATOM   1414  O  O     . LEU A 1 184 ? 160.012 177.401 136.723 1.00 23.67  ? 184 LEU A O     1 
ATOM   1415  C  CB    . LEU A 1 184 ? 156.882 176.644 137.394 1.00 14.60  ? 184 LEU A CB    1 
ATOM   1416  C  CG    . LEU A 1 184 ? 155.516 176.210 136.859 1.00 28.04  ? 184 LEU A CG    1 
ATOM   1417  C  CD1   . LEU A 1 184 ? 154.401 176.700 137.769 1.00 26.15  ? 184 LEU A CD1   1 
ATOM   1418  C  CD2   . LEU A 1 184 ? 155.313 176.713 135.439 1.00 27.20  ? 184 LEU A CD2   1 
ATOM   1419  N  N     . ILE A 1 185 ? 159.796 176.072 138.528 1.00 12.84  ? 185 ILE A N     1 
ATOM   1420  C  CA    . ILE A 1 185 ? 161.041 176.543 139.125 1.00 14.77  ? 185 ILE A CA    1 
ATOM   1421  C  C     . ILE A 1 185 ? 162.237 176.113 138.282 1.00 18.55  ? 185 ILE A C     1 
ATOM   1422  O  O     . ILE A 1 185 ? 163.168 176.895 138.058 1.00 13.38  ? 185 ILE A O     1 
ATOM   1423  C  CB    . ILE A 1 185 ? 161.156 176.042 140.577 1.00 18.71  ? 185 ILE A CB    1 
ATOM   1424  C  CG1   . ILE A 1 185 ? 160.084 176.693 141.451 1.00 12.05  ? 185 ILE A CG1   1 
ATOM   1425  C  CG2   . ILE A 1 185 ? 162.541 176.325 141.136 1.00 9.26   ? 185 ILE A CG2   1 
ATOM   1426  C  CD1   . ILE A 1 185 ? 159.960 176.074 142.824 1.00 18.46  ? 185 ILE A CD1   1 
ATOM   1427  N  N     . ALA A 1 186 ? 162.231 174.866 137.804 1.00 14.68  ? 186 ALA A N     1 
ATOM   1428  C  CA    . ALA A 1 186 ? 163.343 174.375 136.995 1.00 17.66  ? 186 ALA A CA    1 
ATOM   1429  C  C     . ALA A 1 186 ? 163.473 175.157 135.695 1.00 12.32  ? 186 ALA A C     1 
ATOM   1430  O  O     . ALA A 1 186 ? 164.587 175.482 135.267 1.00 12.30  ? 186 ALA A O     1 
ATOM   1431  C  CB    . ALA A 1 186 ? 163.168 172.884 136.710 1.00 13.69  ? 186 ALA A CB    1 
ATOM   1432  N  N     . LEU A 1 187 ? 162.346 175.465 135.049 1.00 18.24  ? 187 LEU A N     1 
ATOM   1433  C  CA    . LEU A 1 187 ? 162.391 176.228 133.806 1.00 12.87  ? 187 LEU A CA    1 
ATOM   1434  C  C     . LEU A 1 187 ? 162.941 177.629 134.039 1.00 11.19  ? 187 LEU A C     1 
ATOM   1435  O  O     . LEU A 1 187 ? 163.693 178.155 133.210 1.00 22.32  ? 187 LEU A O     1 
ATOM   1436  C  CB    . LEU A 1 187 ? 161.000 176.291 133.176 1.00 20.53  ? 187 LEU A CB    1 
ATOM   1437  C  CG    . LEU A 1 187 ? 160.523 175.005 132.496 1.00 20.55  ? 187 LEU A CG    1 
ATOM   1438  C  CD1   . LEU A 1 187 ? 159.085 175.146 132.019 1.00 19.64  ? 187 LEU A CD1   1 
ATOM   1439  C  CD2   . LEU A 1 187 ? 161.443 174.634 131.343 1.00 19.31  ? 187 LEU A CD2   1 
ATOM   1440  N  N     . PHE A 1 188 ? 162.573 178.253 135.161 1.00 7.70   ? 188 PHE A N     1 
ATOM   1441  C  CA    . PHE A 1 188 ? 163.142 179.551 135.505 1.00 12.10  ? 188 PHE A CA    1 
ATOM   1442  C  C     . PHE A 1 188 ? 164.639 179.442 135.767 1.00 11.64  ? 188 PHE A C     1 
ATOM   1443  O  O     . PHE A 1 188 ? 165.405 180.349 135.422 1.00 13.45  ? 188 PHE A O     1 
ATOM   1444  C  CB    . PHE A 1 188 ? 162.423 180.136 136.721 1.00 11.67  ? 188 PHE A CB    1 
ATOM   1445  C  CG    . PHE A 1 188 ? 163.139 181.301 137.344 1.00 14.73  ? 188 PHE A CG    1 
ATOM   1446  C  CD1   . PHE A 1 188 ? 163.191 182.525 136.699 1.00 11.10  ? 188 PHE A CD1   1 
ATOM   1447  C  CD2   . PHE A 1 188 ? 163.763 181.170 138.573 1.00 14.05  ? 188 PHE A CD2   1 
ATOM   1448  C  CE1   . PHE A 1 188 ? 163.850 183.597 137.268 1.00 10.63  ? 188 PHE A CE1   1 
ATOM   1449  C  CE2   . PHE A 1 188 ? 164.425 182.238 139.147 1.00 13.56  ? 188 PHE A CE2   1 
ATOM   1450  C  CZ    . PHE A 1 188 ? 164.468 183.453 138.494 1.00 13.70  ? 188 PHE A CZ    1 
ATOM   1451  N  N     . PHE A 1 189 ? 165.072 178.340 136.386 1.00 17.24  ? 189 PHE A N     1 
ATOM   1452  C  CA    . PHE A 1 189 ? 166.497 178.132 136.619 1.00 10.95  ? 189 PHE A CA    1 
ATOM   1453  C  C     . PHE A 1 189 ? 167.262 178.023 135.306 1.00 12.99  ? 189 PHE A C     1 
ATOM   1454  O  O     . PHE A 1 189 ? 168.355 178.585 135.168 1.00 19.12  ? 189 PHE A O     1 
ATOM   1455  C  CB    . PHE A 1 189 ? 166.715 176.880 137.470 1.00 13.83  ? 189 PHE A CB    1 
ATOM   1456  C  CG    . PHE A 1 189 ? 166.420 177.076 138.932 1.00 13.73  ? 189 PHE A CG    1 
ATOM   1457  C  CD1   . PHE A 1 189 ? 166.099 178.328 139.430 1.00 18.15  ? 189 PHE A CD1   1 
ATOM   1458  C  CD2   . PHE A 1 189 ? 166.464 176.004 139.808 1.00 18.93  ? 189 PHE A CD2   1 
ATOM   1459  C  CE1   . PHE A 1 189 ? 165.827 178.507 140.772 1.00 7.70   ? 189 PHE A CE1   1 
ATOM   1460  C  CE2   . PHE A 1 189 ? 166.194 176.177 141.152 1.00 21.94  ? 189 PHE A CE2   1 
ATOM   1461  C  CZ    . PHE A 1 189 ? 165.875 177.431 141.635 1.00 19.19  ? 189 PHE A CZ    1 
ATOM   1462  N  N     . ILE A 1 190 ? 166.701 177.307 134.327 1.00 16.25  ? 190 ILE A N     1 
ATOM   1463  C  CA    . ILE A 1 190 ? 167.373 177.144 133.039 1.00 10.51  ? 190 ILE A CA    1 
ATOM   1464  C  C     . ILE A 1 190 ? 167.540 178.491 132.349 1.00 8.70   ? 190 ILE A C     1 
ATOM   1465  O  O     . ILE A 1 190 ? 168.601 178.788 131.787 1.00 22.47  ? 190 ILE A O     1 
ATOM   1466  C  CB    . ILE A 1 190 ? 166.602 176.150 132.150 1.00 18.28  ? 190 ILE A CB    1 
ATOM   1467  C  CG1   . ILE A 1 190 ? 166.549 174.771 132.803 1.00 15.54  ? 190 ILE A CG1   1 
ATOM   1468  C  CG2   . ILE A 1 190 ? 167.245 176.053 130.775 1.00 12.44  ? 190 ILE A CG2   1 
ATOM   1469  C  CD1   . ILE A 1 190 ? 165.470 173.872 132.246 1.00 18.98  ? 190 ILE A CD1   1 
ATOM   1470  N  N     . GLN A 1 191 ? 166.497 179.325 132.380 1.00 14.36  ? 191 GLN A N     1 
ATOM   1471  C  CA    . GLN A 1 191 ? 166.567 180.630 131.731 1.00 17.54  ? 191 GLN A CA    1 
ATOM   1472  C  C     . GLN A 1 191 ? 167.695 181.482 132.298 1.00 10.62  ? 191 GLN A C     1 
ATOM   1473  O  O     . GLN A 1 191 ? 168.330 182.243 131.559 1.00 22.04  ? 191 GLN A O     1 
ATOM   1474  C  CB    . GLN A 1 191 ? 165.229 181.357 131.874 1.00 11.17  ? 191 GLN A CB    1 
ATOM   1475  C  CG    . GLN A 1 191 ? 165.119 182.638 131.061 1.00 13.84  ? 191 GLN A CG    1 
ATOM   1476  C  CD    . GLN A 1 191 ? 165.536 183.868 131.843 1.00 14.33  ? 191 GLN A CD    1 
ATOM   1477  O  OE1   . GLN A 1 191 ? 165.518 183.871 133.073 1.00 31.27  ? 191 GLN A OE1   1 
ATOM   1478  N  NE2   . GLN A 1 191 ? 165.915 184.921 131.130 1.00 21.36  ? 191 GLN A NE2   1 
ATOM   1479  N  N     . GLN A 1 192 ? 167.962 181.369 133.598 1.00 12.97  ? 192 GLN A N     1 
ATOM   1480  C  CA    . GLN A 1 192 ? 169.008 182.162 134.228 1.00 14.67  ? 192 GLN A CA    1 
ATOM   1481  C  C     . GLN A 1 192 ? 170.400 181.564 134.060 1.00 10.84  ? 192 GLN A C     1 
ATOM   1482  O  O     . GLN A 1 192 ? 171.385 182.254 134.341 1.00 24.54  ? 192 GLN A O     1 
ATOM   1483  C  CB    . GLN A 1 192 ? 168.701 182.345 135.714 1.00 11.38  ? 192 GLN A CB    1 
ATOM   1484  C  CG    . GLN A 1 192 ? 167.415 183.112 135.987 1.00 19.58  ? 192 GLN A CG    1 
ATOM   1485  C  CD    . GLN A 1 192 ? 167.606 184.613 135.913 1.00 18.41  ? 192 GLN A CD    1 
ATOM   1486  O  OE1   . GLN A 1 192 ? 168.264 185.209 136.764 1.00 29.08  ? 192 GLN A OE1   1 
ATOM   1487  N  NE2   . GLN A 1 192 ? 167.029 185.233 134.891 1.00 18.68  ? 192 GLN A NE2   1 
ATOM   1488  N  N     . GLY A 1 193 ? 170.511 180.313 133.617 1.00 9.69   ? 193 GLY A N     1 
ATOM   1489  C  CA    . GLY A 1 193 ? 171.813 179.742 133.335 1.00 1.52   ? 193 GLY A CA    1 
ATOM   1490  C  C     . GLY A 1 193 ? 172.076 178.369 133.920 1.00 6.82   ? 193 GLY A C     1 
ATOM   1491  O  O     . GLY A 1 193 ? 173.201 177.869 133.839 1.00 24.92  ? 193 GLY A O     1 
ATOM   1492  N  N     . ALA A 1 194 ? 171.060 177.743 134.509 1.00 20.27  ? 194 ALA A N     1 
ATOM   1493  C  CA    . ALA A 1 194 ? 171.241 176.414 135.075 1.00 7.58   ? 194 ALA A CA    1 
ATOM   1494  C  C     . ALA A 1 194 ? 171.361 175.367 133.972 1.00 13.91  ? 194 ALA A C     1 
ATOM   1495  O  O     . ALA A 1 194 ? 170.870 175.546 132.855 1.00 24.68  ? 194 ALA A O     1 
ATOM   1496  C  CB    . ALA A 1 194 ? 170.084 176.061 136.008 1.00 17.03  ? 194 ALA A CB    1 
ATOM   1497  N  N     . LEU A 1 195 ? 172.025 174.262 134.302 1.00 22.44  ? 195 LEU A N     1 
ATOM   1498  C  CA    . LEU A 1 195 ? 172.254 173.190 133.344 1.00 14.59  ? 195 LEU A CA    1 
ATOM   1499  C  C     . LEU A 1 195 ? 171.037 172.283 133.227 1.00 12.83  ? 195 LEU A C     1 
ATOM   1500  O  O     . LEU A 1 195 ? 170.429 171.900 134.231 1.00 23.29  ? 195 LEU A O     1 
ATOM   1501  C  CB    . LEU A 1 195 ? 173.468 172.357 133.754 1.00 20.74  ? 195 LEU A CB    1 
ATOM   1502  C  CG    . LEU A 1 195 ? 174.853 172.900 133.412 1.00 23.84  ? 195 LEU A CG    1 
ATOM   1503  C  CD1   . LEU A 1 195 ? 175.900 171.814 133.589 1.00 12.25  ? 195 LEU A CD1   1 
ATOM   1504  C  CD2   . LEU A 1 195 ? 174.866 173.431 131.996 1.00 12.47  ? 195 LEU A CD2   1 
ATOM   1505  N  N     . GLN A 1 196 ? 170.681 171.945 131.988 1.00 16.25  ? 196 GLN A N     1 
ATOM   1506  C  CA    . GLN A 1 196 ? 169.683 170.908 131.728 1.00 16.14  ? 196 GLN A CA    1 
ATOM   1507  C  C     . GLN A 1 196 ? 170.030 170.272 130.384 1.00 16.18  ? 196 GLN A C     1 
ATOM   1508  O  O     . GLN A 1 196 ? 169.624 170.779 129.334 1.00 18.85  ? 196 GLN A O     1 
ATOM   1509  C  CB    . GLN A 1 196 ? 168.271 171.477 131.732 1.00 10.17  ? 196 GLN A CB    1 
ATOM   1510  C  CG    . GLN A 1 196 ? 167.181 170.417 131.708 1.00 11.42  ? 196 GLN A CG    1 
ATOM   1511  C  CD    . GLN A 1 196 ? 167.128 169.601 132.986 1.00 19.26  ? 196 GLN A CD    1 
ATOM   1512  O  OE1   . GLN A 1 196 ? 167.485 170.084 134.059 1.00 12.48  ? 196 GLN A OE1   1 
ATOM   1513  N  NE2   . GLN A 1 196 ? 166.679 168.357 132.876 1.00 4.80   ? 196 GLN A NE2   1 
ATOM   1514  N  N     . ASN A 1 197 ? 170.768 169.168 130.426 1.00 15.41  ? 197 ASN A N     1 
ATOM   1515  C  CA    . ASN A 1 197 ? 171.190 168.475 129.215 1.00 7.10   ? 197 ASN A CA    1 
ATOM   1516  C  C     . ASN A 1 197 ? 171.663 167.078 129.596 1.00 14.76  ? 197 ASN A C     1 
ATOM   1517  O  O     . ASN A 1 197 ? 171.675 166.700 130.770 1.00 12.38  ? 197 ASN A O     1 
ATOM   1518  C  CB    . ASN A 1 197 ? 172.287 169.256 128.483 1.00 11.62  ? 197 ASN A CB    1 
ATOM   1519  C  CG    . ASN A 1 197 ? 173.587 169.315 129.267 1.00 17.28  ? 197 ASN A CG    1 
ATOM   1520  O  OD1   . ASN A 1 197 ? 174.382 168.376 129.246 1.00 19.43  ? 197 ASN A OD1   1 
ATOM   1521  N  ND2   . ASN A 1 197 ? 173.810 170.425 129.960 1.00 14.64  ? 197 ASN A ND2   1 
ATOM   1522  N  N     . PHE A 1 198 ? 172.050 166.305 128.579 1.00 19.51  ? 198 PHE A N     1 
ATOM   1523  C  CA    . PHE A 1 198 ? 172.633 164.983 128.778 1.00 12.68  ? 198 PHE A CA    1 
ATOM   1524  C  C     . PHE A 1 198 ? 173.916 164.816 127.973 1.00 19.82  ? 198 PHE A C     1 
ATOM   1525  O  O     . PHE A 1 198 ? 174.309 163.686 127.665 1.00 27.19  ? 198 PHE A O     1 
ATOM   1526  C  CB    . PHE A 1 198 ? 171.627 163.886 128.420 1.00 15.08  ? 198 PHE A CB    1 
ATOM   1527  C  CG    . PHE A 1 198 ? 170.476 163.786 129.379 1.00 14.11  ? 198 PHE A CG    1 
ATOM   1528  C  CD1   . PHE A 1 198 ? 169.322 164.525 129.177 1.00 13.50  ? 198 PHE A CD1   1 
ATOM   1529  C  CD2   . PHE A 1 198 ? 170.551 162.960 130.488 1.00 15.16  ? 198 PHE A CD2   1 
ATOM   1530  C  CE1   . PHE A 1 198 ? 168.263 164.438 130.059 1.00 18.90  ? 198 PHE A CE1   1 
ATOM   1531  C  CE2   . PHE A 1 198 ? 169.495 162.868 131.374 1.00 18.86  ? 198 PHE A CE2   1 
ATOM   1532  C  CZ    . PHE A 1 198 ? 168.350 163.608 131.159 1.00 21.08  ? 198 PHE A CZ    1 
ATOM   1533  N  N     . LEU A 1 199 ? 174.570 165.921 127.625 1.00 21.75  ? 199 LEU A N     1 
ATOM   1534  C  CA    . LEU A 1 199 ? 175.794 165.875 126.850 1.00 21.72  ? 199 LEU A CA    1 
ATOM   1535  C  C     . LEU A 1 199 ? 176.945 165.333 127.693 1.00 19.60  ? 199 LEU A C     1 
ATOM   1536  O  O     . LEU A 1 199 ? 176.923 165.419 128.923 1.00 30.16  ? 199 LEU A O     1 
ATOM   1537  C  CB    . LEU A 1 199 ? 176.142 167.269 126.333 1.00 20.79  ? 199 LEU A CB    1 
ATOM   1538  C  CG    . LEU A 1 199 ? 175.075 167.987 125.506 1.00 22.00  ? 199 LEU A CG    1 
ATOM   1539  C  CD1   . LEU A 1 199 ? 175.425 169.458 125.352 1.00 21.78  ? 199 LEU A CD1   1 
ATOM   1540  C  CD2   . LEU A 1 199 ? 174.913 167.325 124.149 1.00 22.26  ? 199 LEU A CD2   1 
ATOM   1541  N  N     . PRO A 1 200 ? 177.964 164.764 127.052 1.00 22.67  ? 200 PRO A N     1 
ATOM   1542  C  CA    . PRO A 1 200 ? 179.175 164.381 127.785 1.00 21.44  ? 200 PRO A CA    1 
ATOM   1543  C  C     . PRO A 1 200 ? 179.923 165.612 128.278 1.00 17.49  ? 200 PRO A C     1 
ATOM   1544  O  O     . PRO A 1 200 ? 179.595 166.754 127.950 1.00 25.48  ? 200 PRO A O     1 
ATOM   1545  C  CB    . PRO A 1 200 ? 179.993 163.604 126.750 1.00 16.11  ? 200 PRO A CB    1 
ATOM   1546  C  CG    . PRO A 1 200 ? 179.495 164.094 125.432 1.00 15.55  ? 200 PRO A CG    1 
ATOM   1547  C  CD    . PRO A 1 200 ? 178.038 164.389 125.630 1.00 22.14  ? 200 PRO A CD    1 
ATOM   1548  N  N     . TYR A 1 201 ? 180.948 165.358 129.087 1.00 18.62  ? 201 TYR A N     1 
ATOM   1549  C  CA    . TYR A 1 201 ? 181.735 166.446 129.652 1.00 18.51  ? 201 TYR A CA    1 
ATOM   1550  C  C     . TYR A 1 201 ? 182.439 167.220 128.543 1.00 15.86  ? 201 TYR A C     1 
ATOM   1551  O  O     . TYR A 1 201 ? 182.966 166.637 127.592 1.00 31.67  ? 201 TYR A O     1 
ATOM   1552  C  CB    . TYR A 1 201 ? 182.754 165.900 130.654 1.00 18.37  ? 201 TYR A CB    1 
ATOM   1553  C  CG    . TYR A 1 201 ? 182.167 165.540 132.004 1.00 15.62  ? 201 TYR A CG    1 
ATOM   1554  C  CD1   . TYR A 1 201 ? 180.820 165.223 132.140 1.00 19.58  ? 201 TYR A CD1   1 
ATOM   1555  C  CD2   . TYR A 1 201 ? 182.961 165.512 133.142 1.00 18.25  ? 201 TYR A CD2   1 
ATOM   1556  C  CE1   . TYR A 1 201 ? 180.282 164.892 133.368 1.00 16.65  ? 201 TYR A CE1   1 
ATOM   1557  C  CE2   . TYR A 1 201 ? 182.431 165.183 134.376 1.00 19.48  ? 201 TYR A CE2   1 
ATOM   1558  C  CZ    . TYR A 1 201 ? 181.091 164.873 134.483 1.00 19.91  ? 201 TYR A CZ    1 
ATOM   1559  O  OH    . TYR A 1 201 ? 180.558 164.545 135.707 1.00 22.58  ? 201 TYR A OH    1 
ATOM   1560  N  N     . GLN A 1 202 ? 182.445 168.543 128.672 1.00 13.43  ? 202 GLN A N     1 
ATOM   1561  C  CA    . GLN A 1 202 ? 182.944 169.431 127.631 1.00 20.27  ? 202 GLN A CA    1 
ATOM   1562  C  C     . GLN A 1 202 ? 184.352 169.901 127.971 1.00 21.61  ? 202 GLN A C     1 
ATOM   1563  O  O     . GLN A 1 202 ? 184.589 170.435 129.060 1.00 24.22  ? 202 GLN A O     1 
ATOM   1564  C  CB    . GLN A 1 202 ? 182.014 170.634 127.457 1.00 17.22  ? 202 GLN A CB    1 
ATOM   1565  C  CG    . GLN A 1 202 ? 182.553 171.709 126.530 1.00 21.35  ? 202 GLN A CG    1 
ATOM   1566  C  CD    . GLN A 1 202 ? 182.515 171.293 125.074 1.00 26.34  ? 202 GLN A CD    1 
ATOM   1567  O  OE1   . GLN A 1 202 ? 181.444 171.130 124.491 1.00 32.49  ? 202 GLN A OE1   1 
ATOM   1568  N  NE2   . GLN A 1 202 ? 183.688 171.120 124.478 1.00 24.80  ? 202 GLN A NE2   1 
ATOM   1569  N  N     . ALA A 1 203 ? 185.279 169.700 127.039 1.00 20.78  ? 203 ALA A N     1 
ATOM   1570  C  CA    . ALA A 1 203 ? 186.640 170.190 127.200 1.00 22.61  ? 203 ALA A CA    1 
ATOM   1571  C  C     . ALA A 1 203 ? 186.710 171.668 126.842 1.00 27.94  ? 203 ALA A C     1 
ATOM   1572  O  O     . ALA A 1 203 ? 186.100 172.116 125.867 1.00 29.35  ? 203 ALA A O     1 
ATOM   1573  C  CB    . ALA A 1 203 ? 187.606 169.389 126.327 1.00 22.11  ? 203 ALA A CB    1 
ATOM   1574  N  N     . VAL A 1 204 ? 187.458 172.426 127.638 1.00 27.69  ? 204 VAL A N     1 
ATOM   1575  C  CA    . VAL A 1 204 ? 187.565 173.871 127.484 1.00 29.95  ? 204 VAL A CA    1 
ATOM   1576  C  C     . VAL A 1 204 ? 189.033 174.238 127.323 1.00 28.62  ? 204 VAL A C     1 
ATOM   1577  O  O     . VAL A 1 204 ? 189.876 173.818 128.124 1.00 31.55  ? 204 VAL A O     1 
ATOM   1578  C  CB    . VAL A 1 204 ? 186.941 174.614 128.681 1.00 31.11  ? 204 VAL A CB    1 
ATOM   1579  C  CG1   . VAL A 1 204 ? 187.602 175.971 128.881 1.00 24.94  ? 204 VAL A CG1   1 
ATOM   1580  C  CG2   . VAL A 1 204 ? 185.442 174.769 128.482 1.00 33.05  ? 204 VAL A CG2   1 
ATOM   1581  N  N     . ASN A 1 205 ? 189.335 175.012 126.283 1.00 31.22  ? 205 ASN A N     1 
ATOM   1582  C  CA    . ASN A 1 205 ? 190.659 175.596 126.084 1.00 32.79  ? 205 ASN A CA    1 
ATOM   1583  C  C     . ASN A 1 205 ? 190.601 177.027 126.608 1.00 35.92  ? 205 ASN A C     1 
ATOM   1584  O  O     . ASN A 1 205 ? 190.075 177.922 125.943 1.00 38.64  ? 205 ASN A O     1 
ATOM   1585  C  CB    . ASN A 1 205 ? 191.065 175.548 124.614 1.00 36.40  ? 205 ASN A CB    1 
ATOM   1586  C  CG    . ASN A 1 205 ? 191.029 174.143 124.046 1.00 42.68  ? 205 ASN A CG    1 
ATOM   1587  O  OD1   . ASN A 1 205 ? 191.589 173.212 124.624 1.00 46.51  ? 205 ASN A OD1   1 
ATOM   1588  N  ND2   . ASN A 1 205 ? 190.366 173.982 122.907 1.00 40.27  ? 205 ASN A ND2   1 
ATOM   1589  N  N     . THR A 1 206 ? 191.142 177.238 127.805 1.00 29.47  ? 206 THR A N     1 
ATOM   1590  C  CA    . THR A 1 206 ? 191.026 178.526 128.470 1.00 29.42  ? 206 THR A CA    1 
ATOM   1591  C  C     . THR A 1 206 ? 191.853 179.587 127.746 1.00 37.10  ? 206 THR A C     1 
ATOM   1592  O  O     . THR A 1 206 ? 192.659 179.298 126.856 1.00 40.94  ? 206 THR A O     1 
ATOM   1593  C  CB    . THR A 1 206 ? 191.468 178.420 129.929 1.00 30.35  ? 206 THR A CB    1 
ATOM   1594  O  OG1   . THR A 1 206 ? 192.871 178.134 129.987 1.00 38.83  ? 206 THR A OG1   1 
ATOM   1595  C  CG2   . THR A 1 206 ? 190.700 177.316 130.639 1.00 29.22  ? 206 THR A CG2   1 
ATOM   1596  N  N     . VAL A 1 207 ? 191.631 180.843 128.141 1.00 38.67  ? 207 VAL A N     1 
ATOM   1597  C  CA    . VAL A 1 207 ? 192.358 181.958 127.539 1.00 39.73  ? 207 VAL A CA    1 
ATOM   1598  C  C     . VAL A 1 207 ? 193.850 181.839 127.823 1.00 42.23  ? 207 VAL A C     1 
ATOM   1599  O  O     . VAL A 1 207 ? 194.686 182.066 126.941 1.00 46.01  ? 207 VAL A O     1 
ATOM   1600  C  CB    . VAL A 1 207 ? 191.791 183.298 128.042 1.00 39.99  ? 207 VAL A CB    1 
ATOM   1601  C  CG1   . VAL A 1 207 ? 192.133 184.414 127.071 1.00 41.27  ? 207 VAL A CG1   1 
ATOM   1602  C  CG2   . VAL A 1 207 ? 190.286 183.198 128.242 1.00 37.54  ? 207 VAL A CG2   1 
ATOM   1603  N  N     . GLU A 1 208 ? 194.208 181.484 129.059 1.00 39.67  ? 208 GLU A N     1 
ATOM   1604  C  CA    . GLU A 1 208 ? 195.609 181.340 129.431 1.00 37.94  ? 208 GLU A CA    1 
ATOM   1605  C  C     . GLU A 1 208 ? 196.256 180.095 128.839 1.00 41.98  ? 208 GLU A C     1 
ATOM   1606  O  O     . GLU A 1 208 ? 197.484 179.968 128.904 1.00 46.62  ? 208 GLU A O     1 
ATOM   1607  C  CB    . GLU A 1 208 ? 195.746 181.314 130.955 1.00 38.75  ? 208 GLU A CB    1 
ATOM   1608  C  CG    . GLU A 1 208 ? 195.400 182.630 131.631 1.00 37.09  ? 208 GLU A CG    1 
ATOM   1609  C  CD    . GLU A 1 208 ? 196.616 183.505 131.857 1.00 38.30  ? 208 GLU A CD    1 
ATOM   1610  O  OE1   . GLU A 1 208 ? 197.644 183.284 131.184 1.00 46.71  ? 208 GLU A OE1   1 
ATOM   1611  O  OE2   . GLU A 1 208 ? 196.544 184.416 132.708 1.00 41.43  ? 208 GLU A OE2   1 
ATOM   1612  N  N     . GLY A 1 209 ? 195.474 179.182 128.267 1.00 38.67  ? 209 GLY A N     1 
ATOM   1613  C  CA    . GLY A 1 209 ? 196.004 177.972 127.676 1.00 37.03  ? 209 GLY A CA    1 
ATOM   1614  C  C     . GLY A 1 209 ? 195.884 176.728 128.527 1.00 37.67  ? 209 GLY A C     1 
ATOM   1615  O  O     . GLY A 1 209 ? 196.392 175.675 128.124 1.00 45.83  ? 209 GLY A O     1 
ATOM   1616  N  N     . ALA A 1 210 ? 195.233 176.811 129.684 1.00 39.58  ? 210 ALA A N     1 
ATOM   1617  C  CA    . ALA A 1 210 ? 195.056 175.652 130.544 1.00 34.04  ? 210 ALA A CA    1 
ATOM   1618  C  C     . ALA A 1 210 ? 193.892 174.798 130.045 1.00 37.25  ? 210 ALA A C     1 
ATOM   1619  O  O     . ALA A 1 210 ? 193.205 175.134 129.076 1.00 33.61  ? 210 ALA A O     1 
ATOM   1620  C  CB    . ALA A 1 210 ? 194.840 176.092 131.990 1.00 37.34  ? 210 ALA A CB    1 
ATOM   1621  N  N     . GLN A 1 211 ? 193.665 173.675 130.719 1.00 42.35  ? 211 GLN A N     1 
ATOM   1622  C  CA    . GLN A 1 211 ? 192.620 172.729 130.353 1.00 37.60  ? 211 GLN A CA    1 
ATOM   1623  C  C     . GLN A 1 211 ? 191.542 172.712 131.427 1.00 38.11  ? 211 GLN A C     1 
ATOM   1624  O  O     . GLN A 1 211 ? 191.845 172.564 132.616 1.00 44.47  ? 211 GLN A O     1 
ATOM   1625  C  CB    . GLN A 1 211 ? 193.197 171.325 130.163 1.00 42.66  ? 211 GLN A CB    1 
ATOM   1626  C  CG    . GLN A 1 211 ? 192.678 170.601 128.933 1.00 44.01  ? 211 GLN A CG    1 
ATOM   1627  C  CD    . GLN A 1 211 ? 193.294 171.120 127.650 1.00 44.00  ? 211 GLN A CD    1 
ATOM   1628  O  OE1   . GLN A 1 211 ? 194.464 171.502 127.620 1.00 45.09  ? 211 GLN A OE1   1 
ATOM   1629  N  NE2   . GLN A 1 211 ? 192.508 171.136 126.580 1.00 41.15  ? 211 GLN A NE2   1 
ATOM   1630  N  N     . GLN A 1 212 ? 190.289 172.866 131.006 1.00 31.61  ? 212 GLN A N     1 
ATOM   1631  C  CA    . GLN A 1 212 ? 189.138 172.786 131.894 1.00 26.23  ? 212 GLN A CA    1 
ATOM   1632  C  C     . GLN A 1 212 ? 188.151 171.777 131.327 1.00 27.50  ? 212 GLN A C     1 
ATOM   1633  O  O     . GLN A 1 212 ? 187.856 171.802 130.129 1.00 34.22  ? 212 GLN A O     1 
ATOM   1634  C  CB    . GLN A 1 212 ? 188.460 174.151 132.060 1.00 25.72  ? 212 GLN A CB    1 
ATOM   1635  C  CG    . GLN A 1 212 ? 188.983 174.978 133.222 1.00 32.76  ? 212 GLN A CG    1 
ATOM   1636  C  CD    . GLN A 1 212 ? 188.060 176.128 133.580 1.00 28.68  ? 212 GLN A CD    1 
ATOM   1637  O  OE1   . GLN A 1 212 ? 187.315 176.626 132.736 1.00 26.92  ? 212 GLN A OE1   1 
ATOM   1638  N  NE2   . GLN A 1 212 ? 188.108 176.557 134.835 1.00 26.26  ? 212 GLN A NE2   1 
ATOM   1639  N  N     . LEU A 1 213 ? 187.651 170.891 132.183 1.00 23.97  ? 213 LEU A N     1 
ATOM   1640  C  CA    . LEU A 1 213 ? 186.639 169.910 131.806 1.00 19.20  ? 213 LEU A CA    1 
ATOM   1641  C  C     . LEU A 1 213 ? 185.346 170.267 132.530 1.00 16.47  ? 213 LEU A C     1 
ATOM   1642  O  O     . LEU A 1 213 ? 185.272 170.179 133.760 1.00 26.47  ? 213 LEU A O     1 
ATOM   1643  C  CB    . LEU A 1 213 ? 187.092 168.492 132.144 1.00 18.11  ? 213 LEU A CB    1 
ATOM   1644  C  CG    . LEU A 1 213 ? 186.220 167.360 131.597 1.00 22.31  ? 213 LEU A CG    1 
ATOM   1645  C  CD1   . LEU A 1 213 ? 186.173 167.400 130.078 1.00 14.47  ? 213 LEU A CD1   1 
ATOM   1646  C  CD2   . LEU A 1 213 ? 186.721 166.011 132.087 1.00 19.35  ? 213 LEU A CD2   1 
ATOM   1647  N  N     . LEU A 1 214 ? 184.333 170.669 131.766 1.00 19.03  ? 214 LEU A N     1 
ATOM   1648  C  CA    . LEU A 1 214 ? 183.074 171.119 132.344 1.00 24.25  ? 214 LEU A CA    1 
ATOM   1649  C  C     . LEU A 1 214 ? 182.131 169.938 132.521 1.00 16.70  ? 214 LEU A C     1 
ATOM   1650  O  O     . LEU A 1 214 ? 181.770 169.296 131.525 1.00 27.06  ? 214 LEU A O     1 
ATOM   1651  C  CB    . LEU A 1 214 ? 182.424 172.171 131.462 1.00 16.83  ? 214 LEU A CB    1 
ATOM   1652  C  CG    . LEU A 1 214 ? 183.146 173.514 131.347 1.00 25.03  ? 214 LEU A CG    1 
ATOM   1653  C  CD1   . LEU A 1 214 ? 182.350 174.470 130.474 1.00 18.02  ? 214 LEU A CD1   1 
ATOM   1654  C  CD2   . LEU A 1 214 ? 183.390 174.115 132.722 1.00 19.00  ? 214 LEU A CD2   1 
ATOM   1655  N  N     . PRO A 1 215 ? 181.716 169.614 133.742 1.00 22.25  ? 215 PRO A N     1 
ATOM   1656  C  CA    . PRO A 1 215 ? 180.702 168.571 133.920 1.00 15.43  ? 215 PRO A CA    1 
ATOM   1657  C  C     . PRO A 1 215 ? 179.348 169.025 133.399 1.00 15.38  ? 215 PRO A C     1 
ATOM   1658  O  O     . PRO A 1 215 ? 179.036 170.218 133.360 1.00 29.37  ? 215 PRO A O     1 
ATOM   1659  C  CB    . PRO A 1 215 ? 180.673 168.358 135.437 1.00 16.40  ? 215 PRO A CB    1 
ATOM   1660  C  CG    . PRO A 1 215 ? 181.152 169.651 136.004 1.00 22.50  ? 215 PRO A CG    1 
ATOM   1661  C  CD    . PRO A 1 215 ? 182.154 170.192 135.024 1.00 14.57  ? 215 PRO A CD    1 
ATOM   1662  N  N     . MET A 1 216 ? 178.539 168.049 132.990 1.00 13.82  ? 216 MET A N     1 
ATOM   1663  C  CA    . MET A 1 216 ? 177.206 168.330 132.471 1.00 16.10  ? 216 MET A CA    1 
ATOM   1664  C  C     . MET A 1 216 ? 176.161 167.499 133.204 1.00 13.19  ? 216 MET A C     1 
ATOM   1665  O  O     . MET A 1 216 ? 176.467 166.867 134.220 1.00 26.44  ? 216 MET A O     1 
ATOM   1666  C  CB    . MET A 1 216 ? 177.151 168.059 130.966 1.00 16.84  ? 216 MET A CB    1 
ATOM   1667  C  CG    . MET A 1 216 ? 177.953 169.042 130.127 1.00 14.00  ? 216 MET A CG    1 
ATOM   1668  S  SD    . MET A 1 216 ? 177.271 170.710 130.165 1.00 33.05  ? 216 MET A SD    1 
ATOM   1669  C  CE    . MET A 1 216 ? 178.767 171.687 130.279 1.00 21.12  ? 216 MET A CE    1 
ATOM   1670  N  N     . GLY A 1 217 ? 174.926 167.502 132.708 1.00 17.27  ? 217 GLY A N     1 
ATOM   1671  C  CA    . GLY A 1 217 ? 173.870 166.712 133.294 1.00 19.03  ? 217 GLY A CA    1 
ATOM   1672  C  C     . GLY A 1 217 ? 172.599 167.503 133.530 1.00 15.00  ? 217 GLY A C     1 
ATOM   1673  O  O     . GLY A 1 217 ? 172.576 168.734 133.431 1.00 29.27  ? 217 GLY A O     1 
ATOM   1674  N  N     . PRO A 1 218 ? 171.506 166.801 133.845 1.00 19.25  ? 218 PRO A N     1 
ATOM   1675  C  CA    . PRO A 1 218 ? 170.211 167.466 134.114 1.00 12.69  ? 218 PRO A CA    1 
ATOM   1676  C  C     . PRO A 1 218 ? 170.164 168.084 135.507 1.00 9.83   ? 218 PRO A C     1 
ATOM   1677  O  O     . PRO A 1 218 ? 169.500 167.603 136.431 1.00 21.94  ? 218 PRO A O     1 
ATOM   1678  C  CB    . PRO A 1 218 ? 169.212 166.318 133.936 1.00 20.93  ? 218 PRO A CB    1 
ATOM   1679  C  CG    . PRO A 1 218 ? 169.974 165.102 134.333 1.00 16.27  ? 218 PRO A CG    1 
ATOM   1680  C  CD    . PRO A 1 218 ? 171.404 165.333 133.920 1.00 16.37  ? 218 PRO A CD    1 
ATOM   1681  N  N     . VAL A 1 219 ? 170.896 169.187 135.666 1.00 11.17  ? 219 VAL A N     1 
ATOM   1682  C  CA    . VAL A 1 219 ? 171.028 169.820 136.974 1.00 11.63  ? 219 VAL A CA    1 
ATOM   1683  C  C     . VAL A 1 219 ? 169.723 170.493 137.388 1.00 11.44  ? 219 VAL A C     1 
ATOM   1684  O  O     . VAL A 1 219 ? 169.271 170.355 138.530 1.00 23.11  ? 219 VAL A O     1 
ATOM   1685  C  CB    . VAL A 1 219 ? 172.197 170.822 136.961 1.00 13.92  ? 219 VAL A CB    1 
ATOM   1686  C  CG1   . VAL A 1 219 ? 172.248 171.594 138.266 1.00 14.86  ? 219 VAL A CG1   1 
ATOM   1687  C  CG2   . VAL A 1 219 ? 173.511 170.102 136.704 1.00 16.69  ? 219 VAL A CG2   1 
ATOM   1688  N  N     . ALA A 1 220 ? 169.098 171.227 136.463 1.00 12.84  ? 220 ALA A N     1 
ATOM   1689  C  CA    . ALA A 1 220 ? 167.989 172.105 136.831 1.00 12.30  ? 220 ALA A CA    1 
ATOM   1690  C  C     . ALA A 1 220 ? 166.788 171.322 137.346 1.00 16.44  ? 220 ALA A C     1 
ATOM   1691  O  O     . ALA A 1 220 ? 166.136 171.740 138.310 1.00 18.57  ? 220 ALA A O     1 
ATOM   1692  C  CB    . ALA A 1 220 ? 167.590 172.972 135.640 1.00 10.16  ? 220 ALA A CB    1 
ATOM   1693  N  N     . SER A 1 221 ? 166.470 170.190 136.713 1.00 18.78  ? 221 SER A N     1 
ATOM   1694  C  CA    . SER A 1 221 ? 165.336 169.391 137.167 1.00 16.85  ? 221 SER A CA    1 
ATOM   1695  C  C     . SER A 1 221 ? 165.557 168.881 138.586 1.00 6.33   ? 221 SER A C     1 
ATOM   1696  O  O     . SER A 1 221 ? 164.633 168.885 139.407 1.00 6.96   ? 221 SER A O     1 
ATOM   1697  C  CB    . SER A 1 221 ? 165.091 168.227 136.206 1.00 8.36   ? 221 SER A CB    1 
ATOM   1698  O  OG    . SER A 1 221 ? 166.286 167.510 135.950 1.00 24.50  ? 221 SER A OG    1 
ATOM   1699  N  N     . GLN A 1 222 ? 166.778 168.438 138.892 1.00 13.30  ? 222 GLN A N     1 
ATOM   1700  C  CA    . GLN A 1 222 ? 167.098 168.030 140.256 1.00 9.07   ? 222 GLN A CA    1 
ATOM   1701  C  C     . GLN A 1 222 ? 167.110 169.225 141.202 1.00 12.09  ? 222 GLN A C     1 
ATOM   1702  O  O     . GLN A 1 222 ? 166.675 169.115 142.354 1.00 17.41  ? 222 GLN A O     1 
ATOM   1703  C  CB    . GLN A 1 222 ? 168.446 167.312 140.285 1.00 9.53   ? 222 GLN A CB    1 
ATOM   1704  C  CG    . GLN A 1 222 ? 168.705 166.523 141.557 1.00 16.31  ? 222 GLN A CG    1 
ATOM   1705  C  CD    . GLN A 1 222 ? 169.938 165.645 141.457 1.00 24.32  ? 222 GLN A CD    1 
ATOM   1706  O  OE1   . GLN A 1 222 ? 170.182 165.014 140.430 1.00 24.46  ? 222 GLN A OE1   1 
ATOM   1707  N  NE2   . GLN A 1 222 ? 170.721 165.600 142.528 1.00 25.20  ? 222 GLN A NE2   1 
ATOM   1708  N  N     . GLU A 1 223 ? 167.598 170.375 140.730 1.00 8.82   ? 223 GLU A N     1 
ATOM   1709  C  CA    . GLU A 1 223 ? 167.761 171.536 141.601 1.00 9.02   ? 223 GLU A CA    1 
ATOM   1710  C  C     . GLU A 1 223 ? 166.422 172.031 142.135 1.00 19.11  ? 223 GLU A C     1 
ATOM   1711  O  O     . GLU A 1 223 ? 166.323 172.435 143.300 1.00 19.96  ? 223 GLU A O     1 
ATOM   1712  C  CB    . GLU A 1 223 ? 168.484 172.654 140.850 1.00 10.71  ? 223 GLU A CB    1 
ATOM   1713  C  CG    . GLU A 1 223 ? 169.024 173.756 141.745 1.00 14.71  ? 223 GLU A CG    1 
ATOM   1714  C  CD    . GLU A 1 223 ? 170.277 173.341 142.489 1.00 23.23  ? 223 GLU A CD    1 
ATOM   1715  O  OE1   . GLU A 1 223 ? 170.931 172.368 142.060 1.00 25.44  ? 223 GLU A OE1   1 
ATOM   1716  O  OE2   . GLU A 1 223 ? 170.608 173.988 143.505 1.00 29.87  ? 223 GLU A OE2   1 
ATOM   1717  N  N     . ALA A 1 224 ? 165.384 172.018 141.297 1.00 13.30  ? 224 ALA A N     1 
ATOM   1718  C  CA    . ALA A 1 224 ? 164.085 172.536 141.714 1.00 12.05  ? 224 ALA A CA    1 
ATOM   1719  C  C     . ALA A 1 224 ? 163.484 171.697 142.837 1.00 13.63  ? 224 ALA A C     1 
ATOM   1720  O  O     . ALA A 1 224 ? 163.044 172.236 143.859 1.00 24.30  ? 224 ALA A O     1 
ATOM   1721  C  CB    . ALA A 1 224 ? 163.137 172.594 140.517 1.00 4.44   ? 224 ALA A CB    1 
ATOM   1722  N  N     . ILE A 1 225 ? 163.455 170.372 142.668 1.00 9.66   ? 225 ILE A N     1 
ATOM   1723  C  CA    . ILE A 1 225 ? 162.900 169.514 143.710 1.00 18.13  ? 225 ILE A CA    1 
ATOM   1724  C  C     . ILE A 1 225 ? 163.831 169.460 144.915 1.00 8.21   ? 225 ILE A C     1 
ATOM   1725  O  O     . ILE A 1 225 ? 163.384 169.224 146.045 1.00 18.49  ? 225 ILE A O     1 
ATOM   1726  C  CB    . ILE A 1 225 ? 162.603 168.109 143.147 1.00 9.96   ? 225 ILE A CB    1 
ATOM   1727  C  CG1   . ILE A 1 225 ? 161.808 167.277 144.159 1.00 13.29  ? 225 ILE A CG1   1 
ATOM   1728  C  CG2   . ILE A 1 225 ? 163.888 167.400 142.749 1.00 2.01   ? 225 ILE A CG2   1 
ATOM   1729  C  CD1   . ILE A 1 225 ? 160.621 168.002 144.759 1.00 9.18   ? 225 ILE A CD1   1 
ATOM   1730  N  N     . LYS A 1 226 ? 165.129 169.687 144.705 1.00 10.15  ? 226 LYS A N     1 
ATOM   1731  C  CA    . LYS A 1 226 ? 166.059 169.766 145.827 1.00 5.66   ? 226 LYS A CA    1 
ATOM   1732  C  C     . LYS A 1 226 ? 165.707 170.930 146.745 1.00 20.47  ? 226 LYS A C     1 
ATOM   1733  O  O     . LYS A 1 226 ? 165.799 170.815 147.972 1.00 14.06  ? 226 LYS A O     1 
ATOM   1734  C  CB    . LYS A 1 226 ? 167.490 169.893 145.303 1.00 19.71  ? 226 LYS A CB    1 
ATOM   1735  C  CG    . LYS A 1 226 ? 168.463 170.591 146.235 1.00 5.19   ? 226 LYS A CG    1 
ATOM   1736  C  CD    . LYS A 1 226 ? 169.692 171.066 145.474 1.00 15.44  ? 226 LYS A CD    1 
ATOM   1737  C  CE    . LYS A 1 226 ? 170.572 171.959 146.329 1.00 9.71   ? 226 LYS A CE    1 
ATOM   1738  N  NZ    . LYS A 1 226 ? 171.863 172.275 145.660 1.00 10.11  ? 226 LYS A NZ    1 
ATOM   1739  N  N     . MET A 1 227 ? 165.291 172.057 146.165 1.00 19.32  ? 227 MET A N     1 
ATOM   1740  C  CA    . MET A 1 227 ? 164.924 173.223 146.959 1.00 16.36  ? 227 MET A CA    1 
ATOM   1741  C  C     . MET A 1 227 ? 163.503 173.101 147.501 1.00 21.01  ? 227 MET A C     1 
ATOM   1742  O  O     . MET A 1 227 ? 163.257 173.355 148.685 1.00 25.42  ? 227 MET A O     1 
ATOM   1743  C  CB    . MET A 1 227 ? 165.060 174.490 146.112 1.00 20.04  ? 227 MET A CB    1 
ATOM   1744  C  CG    . MET A 1 227 ? 166.492 174.899 145.808 1.00 18.68  ? 227 MET A CG    1 
ATOM   1745  S  SD    . MET A 1 227 ? 167.728 174.081 146.831 1.00 35.73  ? 227 MET A SD    1 
ATOM   1746  C  CE    . MET A 1 227 ? 167.792 175.192 148.228 1.00 13.37  ? 227 MET A CE    1 
ATOM   1747  N  N     . LEU A 1 228 ? 162.557 172.711 146.641 1.00 13.72  ? 228 LEU A N     1 
ATOM   1748  C  CA    . LEU A 1 228 ? 161.147 172.705 147.023 1.00 9.92   ? 228 LEU A CA    1 
ATOM   1749  C  C     . LEU A 1 228 ? 160.865 171.696 148.130 1.00 18.29  ? 228 LEU A C     1 
ATOM   1750  O  O     . LEU A 1 228 ? 160.095 171.980 149.055 1.00 20.75  ? 228 LEU A O     1 
ATOM   1751  C  CB    . LEU A 1 228 ? 160.280 172.410 145.799 1.00 18.13  ? 228 LEU A CB    1 
ATOM   1752  C  CG    . LEU A 1 228 ? 158.765 172.395 146.009 1.00 16.40  ? 228 LEU A CG    1 
ATOM   1753  C  CD1   . LEU A 1 228 ? 158.260 173.764 146.437 1.00 13.97  ? 228 LEU A CD1   1 
ATOM   1754  C  CD2   . LEU A 1 228 ? 158.058 171.927 144.747 1.00 11.10  ? 228 LEU A CD2   1 
ATOM   1755  N  N     . GLY A 1 229 ? 161.468 170.516 148.053 1.00 17.56  ? 229 GLY A N     1 
ATOM   1756  C  CA    . GLY A 1 229 ? 161.222 169.465 149.014 1.00 8.59   ? 229 GLY A CA    1 
ATOM   1757  C  C     . GLY A 1 229 ? 162.112 169.476 150.236 1.00 15.42  ? 229 GLY A C     1 
ATOM   1758  O  O     . GLY A 1 229 ? 162.113 168.493 150.984 1.00 9.90   ? 229 GLY A O     1 
ATOM   1759  N  N     . THR A 1 230 ? 162.865 170.556 150.461 1.00 13.33  ? 230 THR A N     1 
ATOM   1760  C  CA    . THR A 1 230 ? 163.830 170.643 151.561 1.00 17.32  ? 230 THR A CA    1 
ATOM   1761  C  C     . THR A 1 230 ? 164.785 169.452 151.547 1.00 14.78  ? 230 THR A C     1 
ATOM   1762  O  O     . THR A 1 230 ? 165.107 168.870 152.584 1.00 9.16   ? 230 THR A O     1 
ATOM   1763  C  CB    . THR A 1 230 ? 163.130 170.773 152.918 1.00 13.63  ? 230 THR A CB    1 
ATOM   1764  O  OG1   . THR A 1 230 ? 162.486 169.538 153.256 1.00 18.34  ? 230 THR A OG1   1 
ATOM   1765  C  CG2   . THR A 1 230 ? 162.104 171.897 152.889 1.00 14.60  ? 230 THR A CG2   1 
ATOM   1766  N  N     . ASN A 1 231 ? 165.237 169.085 150.349 1.00 19.44  ? 231 ASN A N     1 
ATOM   1767  C  CA    . ASN A 1 231 ? 166.164 167.971 150.177 1.00 10.22  ? 231 ASN A CA    1 
ATOM   1768  C  C     . ASN A 1 231 ? 167.610 168.421 150.370 1.00 1.00   ? 231 ASN A C     1 
ATOM   1769  O  O     . ASN A 1 231 ? 168.326 167.883 151.220 1.00 11.39  ? 231 ASN A O     1 
ATOM   1770  C  CB    . ASN A 1 231 ? 165.965 167.340 148.795 1.00 11.78  ? 231 ASN A CB    1 
ATOM   1771  C  CG    . ASN A 1 231 ? 164.645 166.606 148.674 1.00 5.47   ? 231 ASN A CG    1 
ATOM   1772  O  OD1   . ASN A 1 231 ? 164.479 165.512 149.211 1.00 18.30  ? 231 ASN A OD1   1 
ATOM   1773  N  ND2   . ASN A 1 231 ? 163.696 167.206 147.963 1.00 1.90   ? 231 ASN A ND2   1 
ATOM   1774  N  N     . GLY A 1 232 ? 168.048 169.407 149.590 1.00 11.41  ? 232 GLY A N     1 
ATOM   1775  C  CA    . GLY A 1 232 ? 169.364 169.989 149.747 1.00 8.65   ? 232 GLY A CA    1 
ATOM   1776  C  C     . GLY A 1 232 ? 170.498 169.253 149.068 1.00 16.04  ? 232 GLY A C     1 
ATOM   1777  O  O     . GLY A 1 232 ? 171.650 169.685 149.189 1.00 22.44  ? 232 GLY A O     1 
ATOM   1778  N  N     . GLY A 1 233 ? 170.218 168.163 148.358 1.00 9.23   ? 233 GLY A N     1 
ATOM   1779  C  CA    . GLY A 1 233 ? 171.263 167.415 147.687 1.00 3.75   ? 233 GLY A CA    1 
ATOM   1780  C  C     . GLY A 1 233 ? 171.725 168.060 146.398 1.00 14.01  ? 233 GLY A C     1 
ATOM   1781  O  O     . GLY A 1 233 ? 170.996 168.068 145.402 1.00 24.95  ? 233 GLY A O     1 
ATOM   1782  N  N     . GLY A 1 234 ? 172.940 168.604 146.405 1.00 8.34   ? 234 GLY A N     1 
ATOM   1783  C  CA    . GLY A 1 234 ? 173.451 169.278 145.230 1.00 18.04  ? 234 GLY A CA    1 
ATOM   1784  C  C     . GLY A 1 234 ? 173.910 168.311 144.154 1.00 17.33  ? 234 GLY A C     1 
ATOM   1785  O  O     . GLY A 1 234 ? 174.404 167.218 144.428 1.00 19.73  ? 234 GLY A O     1 
ATOM   1786  N  N     . PHE A 1 235 ? 173.732 168.733 142.900 1.00 16.99  ? 235 PHE A N     1 
ATOM   1787  C  CA    . PHE A 1 235 ? 174.221 167.944 141.775 1.00 13.06  ? 235 PHE A CA    1 
ATOM   1788  C  C     . PHE A 1 235 ? 175.740 167.832 141.806 1.00 17.58  ? 235 PHE A C     1 
ATOM   1789  O  O     . PHE A 1 235 ? 176.299 166.763 141.533 1.00 20.37  ? 235 PHE A O     1 
ATOM   1790  C  CB    . PHE A 1 235 ? 173.753 168.567 140.460 1.00 19.05  ? 235 PHE A CB    1 
ATOM   1791  C  CG    . PHE A 1 235 ? 173.724 167.605 139.307 1.00 24.04  ? 235 PHE A CG    1 
ATOM   1792  C  CD1   . PHE A 1 235 ? 174.867 167.352 138.568 1.00 9.80   ? 235 PHE A CD1   1 
ATOM   1793  C  CD2   . PHE A 1 235 ? 172.549 166.961 138.955 1.00 12.50  ? 235 PHE A CD2   1 
ATOM   1794  C  CE1   . PHE A 1 235 ? 174.841 166.470 137.503 1.00 10.39  ? 235 PHE A CE1   1 
ATOM   1795  C  CE2   . PHE A 1 235 ? 172.517 166.080 137.892 1.00 9.28   ? 235 PHE A CE2   1 
ATOM   1796  C  CZ    . PHE A 1 235 ? 173.664 165.833 137.166 1.00 8.89   ? 235 PHE A CZ    1 
ATOM   1797  N  N     . PHE A 1 236 ? 176.421 168.923 142.134 1.00 15.88  ? 236 PHE A N     1 
ATOM   1798  C  CA    . PHE A 1 236 ? 177.870 168.959 142.251 1.00 15.41  ? 236 PHE A CA    1 
ATOM   1799  C  C     . PHE A 1 236 ? 178.269 169.095 143.715 1.00 16.91  ? 236 PHE A C     1 
ATOM   1800  O  O     . PHE A 1 236 ? 177.433 169.297 144.598 1.00 15.32  ? 236 PHE A O     1 
ATOM   1801  C  CB    . PHE A 1 236 ? 178.453 170.110 141.423 1.00 7.67   ? 236 PHE A CB    1 
ATOM   1802  C  CG    . PHE A 1 236 ? 178.057 170.075 139.975 1.00 16.53  ? 236 PHE A CG    1 
ATOM   1803  C  CD1   . PHE A 1 236 ? 178.395 168.996 139.176 1.00 13.63  ? 236 PHE A CD1   1 
ATOM   1804  C  CD2   . PHE A 1 236 ? 177.342 171.120 139.414 1.00 12.49  ? 236 PHE A CD2   1 
ATOM   1805  C  CE1   . PHE A 1 236 ? 178.029 168.960 137.844 1.00 20.59  ? 236 PHE A CE1   1 
ATOM   1806  C  CE2   . PHE A 1 236 ? 176.974 171.090 138.082 1.00 10.96  ? 236 PHE A CE2   1 
ATOM   1807  C  CZ    . PHE A 1 236 ? 177.318 170.009 137.296 1.00 16.52  ? 236 PHE A CZ    1 
ATOM   1808  N  N     . ASN A 1 237 ? 179.575 168.975 143.962 1.00 19.19  ? 237 ASN A N     1 
ATOM   1809  C  CA    . ASN A 1 237 ? 180.081 169.054 145.329 1.00 14.89  ? 237 ASN A CA    1 
ATOM   1810  C  C     . ASN A 1 237 ? 179.866 170.441 145.923 1.00 20.96  ? 237 ASN A C     1 
ATOM   1811  O  O     . ASN A 1 237 ? 179.574 170.571 147.118 1.00 20.17  ? 237 ASN A O     1 
ATOM   1812  C  CB    . ASN A 1 237 ? 181.560 168.675 145.363 1.00 11.19  ? 237 ASN A CB    1 
ATOM   1813  C  CG    . ASN A 1 237 ? 182.117 168.626 146.772 1.00 17.26  ? 237 ASN A CG    1 
ATOM   1814  O  OD1   . ASN A 1 237 ? 181.637 167.869 147.614 1.00 24.63  ? 237 ASN A OD1   1 
ATOM   1815  N  ND2   . ASN A 1 237 ? 183.133 169.438 147.035 1.00 19.54  ? 237 ASN A ND2   1 
ATOM   1816  N  N     . ALA A 1 238 ? 180.003 171.489 145.108 1.00 21.33  ? 238 ALA A N     1 
ATOM   1817  C  CA    . ALA A 1 238 ? 179.820 172.854 145.586 1.00 10.58  ? 238 ALA A CA    1 
ATOM   1818  C  C     . ALA A 1 238 ? 178.383 173.156 145.990 1.00 15.08  ? 238 ALA A C     1 
ATOM   1819  O  O     . ALA A 1 238 ? 178.146 174.184 146.634 1.00 23.00  ? 238 ALA A O     1 
ATOM   1820  C  CB    . ALA A 1 238 ? 180.277 173.850 144.518 1.00 12.95  ? 238 ALA A CB    1 
ATOM   1821  N  N     . ASN A 1 239 ? 177.433 172.301 145.625 1.00 16.61  ? 239 ASN A N     1 
ATOM   1822  C  CA    . ASN A 1 239 ? 176.017 172.418 146.017 1.00 7.48   ? 239 ASN A CA    1 
ATOM   1823  C  C     . ASN A 1 239 ? 175.477 173.733 145.445 1.00 11.15  ? 239 ASN A C     1 
ATOM   1824  O  O     . ASN A 1 239 ? 175.753 174.058 144.280 1.00 22.18  ? 239 ASN A O     1 
ATOM   1825  C  CB    . ASN A 1 239 ? 175.885 172.268 147.521 1.00 15.34  ? 239 ASN A CB    1 
ATOM   1826  C  CG    . ASN A 1 239 ? 174.490 171.857 147.947 1.00 14.34  ? 239 ASN A CG    1 
ATOM   1827  O  OD1   . ASN A 1 239 ? 173.548 172.645 147.870 1.00 18.19  ? 239 ASN A OD1   1 
ATOM   1828  N  ND2   . ASN A 1 239 ? 174.350 170.617 148.399 1.00 8.82   ? 239 ASN A ND2   1 
ATOM   1829  N  N     . SER A 1 240 ? 174.720 174.507 146.224 1.00 9.87   ? 240 SER A N     1 
ATOM   1830  C  CA    . SER A 1 240 ? 174.103 175.728 145.721 1.00 12.39  ? 240 SER A CA    1 
ATOM   1831  C  C     . SER A 1 240 ? 175.104 176.850 145.480 1.00 16.62  ? 240 SER A C     1 
ATOM   1832  O  O     . SER A 1 240 ? 174.727 177.876 144.907 1.00 21.73  ? 240 SER A O     1 
ATOM   1833  C  CB    . SER A 1 240 ? 173.015 176.200 146.686 1.00 14.18  ? 240 SER A CB    1 
ATOM   1834  O  OG    . SER A 1 240 ? 171.752 175.665 146.331 1.00 21.83  ? 240 SER A OG    1 
ATOM   1835  N  N     . SER A 1 241 ? 176.357 176.696 145.909 1.00 20.07  ? 241 SER A N     1 
ATOM   1836  C  CA    . SER A 1 241 ? 177.378 177.675 145.559 1.00 11.24  ? 241 SER A CA    1 
ATOM   1837  C  C     . SER A 1 241 ? 177.896 177.487 144.139 1.00 13.87  ? 241 SER A C     1 
ATOM   1838  O  O     . SER A 1 241 ? 178.559 178.386 143.610 1.00 18.70  ? 241 SER A O     1 
ATOM   1839  C  CB    . SER A 1 241 ? 178.542 177.607 146.550 1.00 10.87  ? 241 SER A CB    1 
ATOM   1840  O  OG    . SER A 1 241 ? 179.479 176.614 146.175 1.00 20.62  ? 241 SER A OG    1 
ATOM   1841  N  N     . HIS A 1 242 ? 177.610 176.348 143.519 1.00 5.83   ? 242 HIS A N     1 
ATOM   1842  C  CA    . HIS A 1 242 ? 178.056 176.100 142.153 1.00 17.55  ? 242 HIS A CA    1 
ATOM   1843  C  C     . HIS A 1 242 ? 177.313 177.015 141.186 1.00 14.31  ? 242 HIS A C     1 
ATOM   1844  O  O     . HIS A 1 242 ? 176.083 177.117 141.260 1.00 8.47   ? 242 HIS A O     1 
ATOM   1845  C  CB    . HIS A 1 242 ? 177.827 174.637 141.778 1.00 14.71  ? 242 HIS A CB    1 
ATOM   1846  C  CG    . HIS A 1 242 ? 178.711 174.150 140.672 1.00 15.66  ? 242 HIS A CG    1 
ATOM   1847  N  ND1   . HIS A 1 242 ? 178.577 174.576 139.368 1.00 10.88  ? 242 HIS A ND1   1 
ATOM   1848  C  CD2   . HIS A 1 242 ? 179.738 173.268 140.675 1.00 2.67   ? 242 HIS A CD2   1 
ATOM   1849  C  CE1   . HIS A 1 242 ? 179.485 173.979 138.617 1.00 10.82  ? 242 HIS A CE1   1 
ATOM   1850  N  NE2   . HIS A 1 242 ? 180.202 173.180 139.385 1.00 20.28  ? 242 HIS A NE2   1 
ATOM   1851  N  N     . PRO A 1 243 ? 178.016 177.703 140.282 1.00 20.85  ? 243 PRO A N     1 
ATOM   1852  C  CA    . PRO A 1 243 ? 177.317 178.562 139.311 1.00 12.62  ? 243 PRO A CA    1 
ATOM   1853  C  C     . PRO A 1 243 ? 176.354 177.807 138.412 1.00 18.62  ? 243 PRO A C     1 
ATOM   1854  O  O     . PRO A 1 243 ? 175.333 178.372 138.003 1.00 20.56  ? 243 PRO A O     1 
ATOM   1855  C  CB    . PRO A 1 243 ? 178.467 179.190 138.509 1.00 10.45  ? 243 PRO A CB    1 
ATOM   1856  C  CG    . PRO A 1 243 ? 179.670 179.058 139.388 1.00 19.16  ? 243 PRO A CG    1 
ATOM   1857  C  CD    . PRO A 1 243 ? 179.479 177.782 140.144 1.00 14.82  ? 243 PRO A CD    1 
ATOM   1858  N  N     . PHE A 1 244 ? 176.649 176.548 138.080 1.00 22.08  ? 244 PHE A N     1 
ATOM   1859  C  CA    . PHE A 1 244 ? 175.749 175.774 137.234 1.00 10.64  ? 244 PHE A CA    1 
ATOM   1860  C  C     . PHE A 1 244 ? 174.461 175.391 137.953 1.00 19.46  ? 244 PHE A C     1 
ATOM   1861  O  O     . PHE A 1 244 ? 173.469 175.069 137.290 1.00 19.80  ? 244 PHE A O     1 
ATOM   1862  C  CB    . PHE A 1 244 ? 176.455 174.516 136.724 1.00 17.16  ? 244 PHE A CB    1 
ATOM   1863  C  CG    . PHE A 1 244 ? 177.254 174.735 135.471 1.00 15.73  ? 244 PHE A CG    1 
ATOM   1864  C  CD1   . PHE A 1 244 ? 176.946 175.774 134.609 1.00 11.08  ? 244 PHE A CD1   1 
ATOM   1865  C  CD2   . PHE A 1 244 ? 178.313 173.901 135.154 1.00 19.75  ? 244 PHE A CD2   1 
ATOM   1866  C  CE1   . PHE A 1 244 ? 177.679 175.978 133.456 1.00 11.44  ? 244 PHE A CE1   1 
ATOM   1867  C  CE2   . PHE A 1 244 ? 179.049 174.099 134.001 1.00 21.71  ? 244 PHE A CE2   1 
ATOM   1868  C  CZ    . PHE A 1 244 ? 178.732 175.139 133.152 1.00 17.69  ? 244 PHE A CZ    1 
ATOM   1869  N  N     . GLU A 1 245 ? 174.453 175.416 139.285 1.00 19.28  ? 245 GLU A N     1 
ATOM   1870  C  CA    . GLU A 1 245 ? 173.263 175.110 140.070 1.00 16.59  ? 245 GLU A CA    1 
ATOM   1871  C  C     . GLU A 1 245 ? 172.483 176.354 140.472 1.00 15.18  ? 245 GLU A C     1 
ATOM   1872  O  O     . GLU A 1 245 ? 171.251 176.357 140.402 1.00 30.28  ? 245 GLU A O     1 
ATOM   1873  C  CB    . GLU A 1 245 ? 173.647 174.321 141.328 1.00 14.97  ? 245 GLU A CB    1 
ATOM   1874  C  CG    . GLU A 1 245 ? 174.067 172.884 141.058 1.00 13.86  ? 245 GLU A CG    1 
ATOM   1875  C  CD    . GLU A 1 245 ? 174.381 172.111 142.325 1.00 19.37  ? 245 GLU A CD    1 
ATOM   1876  O  OE1   . GLU A 1 245 ? 173.513 172.050 143.220 1.00 29.87  ? 245 GLU A OE1   1 
ATOM   1877  O  OE2   . GLU A 1 245 ? 175.498 171.562 142.426 1.00 25.64  ? 245 GLU A OE2   1 
ATOM   1878  N  N     . ASN A 1 246 ? 173.175 177.410 140.896 1.00 14.85  ? 246 ASN A N     1 
ATOM   1879  C  CA    . ASN A 1 246 ? 172.555 178.662 141.328 1.00 20.15  ? 246 ASN A CA    1 
ATOM   1880  C  C     . ASN A 1 246 ? 173.273 179.806 140.624 1.00 5.05   ? 246 ASN A C     1 
ATOM   1881  O  O     . ASN A 1 246 ? 174.187 180.423 141.187 1.00 25.42  ? 246 ASN A O     1 
ATOM   1882  C  CB    . ASN A 1 246 ? 172.615 178.804 142.849 1.00 14.76  ? 246 ASN A CB    1 
ATOM   1883  C  CG    . ASN A 1 246 ? 171.730 179.914 143.370 1.00 10.55  ? 246 ASN A CG    1 
ATOM   1884  O  OD1   . ASN A 1 246 ? 170.940 180.497 142.629 1.00 25.96  ? 246 ASN A OD1   1 
ATOM   1885  N  ND2   . ASN A 1 246 ? 171.857 180.212 144.656 1.00 20.96  ? 246 ASN A ND2   1 
ATOM   1886  N  N     . PRO A 1 247 ? 172.885 180.115 139.383 1.00 19.60  ? 247 PRO A N     1 
ATOM   1887  C  CA    . PRO A 1 247 ? 173.696 181.051 138.585 1.00 16.10  ? 247 PRO A CA    1 
ATOM   1888  C  C     . PRO A 1 247 ? 173.607 182.498 139.039 1.00 13.41  ? 247 PRO A C     1 
ATOM   1889  O  O     . PRO A 1 247 ? 174.634 183.187 139.075 1.00 27.78  ? 247 PRO A O     1 
ATOM   1890  C  CB    . PRO A 1 247 ? 173.140 180.863 137.167 1.00 16.23  ? 247 PRO A CB    1 
ATOM   1891  C  CG    . PRO A 1 247 ? 171.736 180.408 137.372 1.00 13.86  ? 247 PRO A CG    1 
ATOM   1892  C  CD    . PRO A 1 247 ? 171.736 179.584 138.629 1.00 11.96  ? 247 PRO A CD    1 
ATOM   1893  N  N     . THR A 1 248 ? 172.418 182.988 139.377 1.00 17.26  ? 248 THR A N     1 
ATOM   1894  C  CA    . THR A 1 248 ? 172.219 184.403 139.657 1.00 18.53  ? 248 THR A CA    1 
ATOM   1895  C  C     . THR A 1 248 ? 171.594 184.583 141.033 1.00 19.04  ? 248 THR A C     1 
ATOM   1896  O  O     . THR A 1 248 ? 171.120 183.632 141.660 1.00 32.00  ? 248 THR A O     1 
ATOM   1897  C  CB    . THR A 1 248 ? 171.336 185.070 138.592 1.00 17.70  ? 248 THR A CB    1 
ATOM   1898  O  OG1   . THR A 1 248 ? 170.050 184.437 138.568 1.00 13.92  ? 248 THR A OG1   1 
ATOM   1899  C  CG2   . THR A 1 248 ? 171.977 184.961 137.216 1.00 8.06   ? 248 THR A CG2   1 
ATOM   1900  N  N     . ALA A 1 249 ? 171.604 185.834 141.502 1.00 15.97  ? 249 ALA A N     1 
ATOM   1901  C  CA    . ALA A 1 249 ? 170.938 186.160 142.758 1.00 17.21  ? 249 ALA A CA    1 
ATOM   1902  C  C     . ALA A 1 249 ? 169.428 186.000 142.648 1.00 14.82  ? 249 ALA A C     1 
ATOM   1903  O  O     . ALA A 1 249 ? 168.758 185.754 143.657 1.00 14.14  ? 249 ALA A O     1 
ATOM   1904  C  CB    . ALA A 1 249 ? 171.292 187.583 143.189 1.00 15.54  ? 249 ALA A CB    1 
ATOM   1905  N  N     . LEU A 1 250 ? 168.876 186.148 141.440 1.00 16.00  ? 250 LEU A N     1 
ATOM   1906  C  CA    . LEU A 1 250 ? 167.450 185.910 141.243 1.00 9.41   ? 250 LEU A CA    1 
ATOM   1907  C  C     . LEU A 1 250 ? 167.092 184.455 141.517 1.00 14.29  ? 250 LEU A C     1 
ATOM   1908  O  O     . LEU A 1 250 ? 166.083 184.168 142.171 1.00 23.92  ? 250 LEU A O     1 
ATOM   1909  C  CB    . LEU A 1 250 ? 167.043 186.305 139.824 1.00 19.71  ? 250 LEU A CB    1 
ATOM   1910  C  CG    . LEU A 1 250 ? 166.121 187.519 139.692 1.00 23.60  ? 250 LEU A CG    1 
ATOM   1911  C  CD1   . LEU A 1 250 ? 165.743 187.747 138.237 1.00 18.92  ? 250 LEU A CD1   1 
ATOM   1912  C  CD2   . LEU A 1 250 ? 164.879 187.347 140.552 1.00 24.72  ? 250 LEU A CD2   1 
ATOM   1913  N  N     . THR A 1 251 ? 167.909 183.520 141.026 1.00 12.20  ? 251 THR A N     1 
ATOM   1914  C  CA    . THR A 1 251 ? 167.681 182.112 141.335 1.00 19.42  ? 251 THR A CA    1 
ATOM   1915  C  C     . THR A 1 251 ? 167.907 181.834 142.814 1.00 11.39  ? 251 THR A C     1 
ATOM   1916  O  O     . THR A 1 251 ? 167.208 181.007 143.410 1.00 27.43  ? 251 THR A O     1 
ATOM   1917  C  CB    . THR A 1 251 ? 168.586 181.221 140.483 1.00 11.05  ? 251 THR A CB    1 
ATOM   1918  O  OG1   . THR A 1 251 ? 169.941 181.676 140.578 1.00 27.44  ? 251 THR A OG1   1 
ATOM   1919  C  CG2   . THR A 1 251 ? 168.145 181.249 139.035 1.00 13.71  ? 251 THR A CG2   1 
ATOM   1920  N  N     . ASN A 1 252 ? 168.884 182.513 143.420 1.00 6.82   ? 252 ASN A N     1 
ATOM   1921  C  CA    . ASN A 1 252 ? 169.139 182.330 144.844 1.00 9.36   ? 252 ASN A CA    1 
ATOM   1922  C  C     . ASN A 1 252 ? 167.941 182.761 145.681 1.00 8.87   ? 252 ASN A C     1 
ATOM   1923  O  O     . ASN A 1 252 ? 167.565 182.075 146.637 1.00 10.14  ? 252 ASN A O     1 
ATOM   1924  C  CB    . ASN A 1 252 ? 170.388 183.107 145.257 1.00 9.48   ? 252 ASN A CB    1 
ATOM   1925  C  CG    . ASN A 1 252 ? 170.861 182.746 146.649 1.00 6.89   ? 252 ASN A CG    1 
ATOM   1926  O  OD1   . ASN A 1 252 ? 171.518 181.726 146.848 1.00 20.87  ? 252 ASN A OD1   1 
ATOM   1927  N  ND2   . ASN A 1 252 ? 170.525 183.581 147.623 1.00 8.07   ? 252 ASN A ND2   1 
ATOM   1928  N  N     . PHE A 1 253 ? 167.327 183.895 145.333 1.00 8.07   ? 253 PHE A N     1 
ATOM   1929  C  CA    . PHE A 1 253 ? 166.150 184.351 146.066 1.00 17.42  ? 253 PHE A CA    1 
ATOM   1930  C  C     . PHE A 1 253 ? 165.001 183.359 145.934 1.00 13.89  ? 253 PHE A C     1 
ATOM   1931  O  O     . PHE A 1 253 ? 164.289 183.089 146.908 1.00 14.99  ? 253 PHE A O     1 
ATOM   1932  C  CB    . PHE A 1 253 ? 165.725 185.734 145.572 1.00 2.37   ? 253 PHE A CB    1 
ATOM   1933  C  CG    . PHE A 1 253 ? 164.789 186.448 146.505 1.00 14.38  ? 253 PHE A CG    1 
ATOM   1934  C  CD1   . PHE A 1 253 ? 165.239 186.932 147.722 1.00 17.29  ? 253 PHE A CD1   1 
ATOM   1935  C  CD2   . PHE A 1 253 ? 163.459 186.631 146.166 1.00 19.43  ? 253 PHE A CD2   1 
ATOM   1936  C  CE1   . PHE A 1 253 ? 164.380 187.588 148.583 1.00 22.15  ? 253 PHE A CE1   1 
ATOM   1937  C  CE2   . PHE A 1 253 ? 162.595 187.286 147.023 1.00 15.59  ? 253 PHE A CE2   1 
ATOM   1938  C  CZ    . PHE A 1 253 ? 163.056 187.765 148.233 1.00 20.80  ? 253 PHE A CZ    1 
ATOM   1939  N  N     . VAL A 1 254 ? 164.805 182.809 144.735 1.00 8.29   ? 254 VAL A N     1 
ATOM   1940  C  CA    . VAL A 1 254 ? 163.773 181.796 144.537 1.00 14.62  ? 254 VAL A CA    1 
ATOM   1941  C  C     . VAL A 1 254 ? 164.106 180.535 145.326 1.00 13.35  ? 254 VAL A C     1 
ATOM   1942  O  O     . VAL A 1 254 ? 163.214 179.878 145.878 1.00 21.13  ? 254 VAL A O     1 
ATOM   1943  C  CB    . VAL A 1 254 ? 163.598 181.506 143.034 1.00 22.63  ? 254 VAL A CB    1 
ATOM   1944  C  CG1   . VAL A 1 254 ? 162.778 180.242 142.814 1.00 8.26   ? 254 VAL A CG1   1 
ATOM   1945  C  CG2   . VAL A 1 254 ? 162.948 182.694 142.341 1.00 14.32  ? 254 VAL A CG2   1 
ATOM   1946  N  N     . GLN A 1 255 ? 165.393 180.183 145.402 1.00 7.92   ? 255 GLN A N     1 
ATOM   1947  C  CA    . GLN A 1 255 ? 165.795 178.994 146.149 1.00 12.95  ? 255 GLN A CA    1 
ATOM   1948  C  C     . GLN A 1 255 ? 165.432 179.114 147.624 1.00 14.58  ? 255 GLN A C     1 
ATOM   1949  O  O     . GLN A 1 255 ? 164.934 178.156 148.227 1.00 11.15  ? 255 GLN A O     1 
ATOM   1950  C  CB    . GLN A 1 255 ? 167.295 178.753 145.984 1.00 18.20  ? 255 GLN A CB    1 
ATOM   1951  C  CG    . GLN A 1 255 ? 167.681 178.104 144.665 1.00 18.22  ? 255 GLN A CG    1 
ATOM   1952  C  CD    . GLN A 1 255 ? 168.986 177.338 144.752 1.00 15.75  ? 255 GLN A CD    1 
ATOM   1953  O  OE1   . GLN A 1 255 ? 169.545 177.164 145.834 1.00 28.90  ? 255 GLN A OE1   1 
ATOM   1954  N  NE2   . GLN A 1 255 ? 169.477 176.874 143.609 1.00 14.09  ? 255 GLN A NE2   1 
ATOM   1955  N  N     . MET A 1 256 ? 165.676 180.283 148.225 1.00 13.89  ? 256 MET A N     1 
ATOM   1956  C  CA    . MET A 1 256 ? 165.292 180.487 149.619 1.00 14.12  ? 256 MET A CA    1 
ATOM   1957  C  C     . MET A 1 256 ? 163.779 180.440 149.787 1.00 14.37  ? 256 MET A C     1 
ATOM   1958  O  O     . MET A 1 256 ? 163.273 179.872 150.763 1.00 19.25  ? 256 MET A O     1 
ATOM   1959  C  CB    . MET A 1 256 ? 165.845 181.816 150.134 1.00 10.20  ? 256 MET A CB    1 
ATOM   1960  C  CG    . MET A 1 256 ? 167.288 182.082 149.750 1.00 22.88  ? 256 MET A CG    1 
ATOM   1961  S  SD    . MET A 1 256 ? 168.129 183.199 150.888 1.00 24.16  ? 256 MET A SD    1 
ATOM   1962  C  CE    . MET A 1 256 ? 168.304 184.653 149.858 1.00 23.41  ? 256 MET A CE    1 
ATOM   1963  N  N     . LEU A 1 257 ? 163.040 181.039 148.850 1.00 7.24   ? 257 LEU A N     1 
ATOM   1964  C  CA    . LEU A 1 257 ? 161.583 180.999 148.919 1.00 14.52  ? 257 LEU A CA    1 
ATOM   1965  C  C     . LEU A 1 257 ? 161.066 179.572 148.800 1.00 15.77  ? 257 LEU A C     1 
ATOM   1966  O  O     . LEU A 1 257 ? 160.130 179.182 149.507 1.00 20.98  ? 257 LEU A O     1 
ATOM   1967  C  CB    . LEU A 1 257 ? 160.980 181.882 147.826 1.00 18.14  ? 257 LEU A CB    1 
ATOM   1968  C  CG    . LEU A 1 257 ? 161.172 183.392 147.978 1.00 19.76  ? 257 LEU A CG    1 
ATOM   1969  C  CD1   . LEU A 1 257 ? 160.821 184.109 146.685 1.00 20.64  ? 257 LEU A CD1   1 
ATOM   1970  C  CD2   . LEU A 1 257 ? 160.344 183.930 149.135 1.00 17.90  ? 257 LEU A CD2   1 
ATOM   1971  N  N     . ALA A 1 258 ? 161.666 178.776 147.910 1.00 16.70  ? 258 ALA A N     1 
ATOM   1972  C  CA    . ALA A 1 258 ? 161.240 177.391 147.745 1.00 18.20  ? 258 ALA A CA    1 
ATOM   1973  C  C     . ALA A 1 258 ? 161.504 176.563 148.996 1.00 14.53  ? 258 ALA A C     1 
ATOM   1974  O  O     . ALA A 1 258 ? 160.767 175.609 149.270 1.00 19.50  ? 258 ALA A O     1 
ATOM   1975  C  CB    . ALA A 1 258 ? 161.939 176.765 146.538 1.00 3.88   ? 258 ALA A CB    1 
ATOM   1976  N  N     . ILE A 1 259 ? 162.547 176.903 149.758 1.00 16.69  ? 259 ILE A N     1 
ATOM   1977  C  CA    . ILE A 1 259 ? 162.836 176.178 150.993 1.00 18.19  ? 259 ILE A CA    1 
ATOM   1978  C  C     . ILE A 1 259 ? 161.692 176.345 151.986 1.00 15.56  ? 259 ILE A C     1 
ATOM   1979  O  O     . ILE A 1 259 ? 161.227 175.375 152.597 1.00 27.01  ? 259 ILE A O     1 
ATOM   1980  C  CB    . ILE A 1 259 ? 164.171 176.653 151.595 1.00 15.95  ? 259 ILE A CB    1 
ATOM   1981  C  CG1   . ILE A 1 259 ? 165.353 176.168 150.757 1.00 13.04  ? 259 ILE A CG1   1 
ATOM   1982  C  CG2   . ILE A 1 259 ? 164.316 176.165 153.026 1.00 5.06   ? 259 ILE A CG2   1 
ATOM   1983  C  CD1   . ILE A 1 259 ? 166.689 176.658 151.274 1.00 14.80  ? 259 ILE A CD1   1 
ATOM   1984  N  N     . PHE A 1 260 ? 161.217 177.576 152.154 1.00 17.38  ? 260 PHE A N     1 
ATOM   1985  C  CA    . PHE A 1 260 ? 160.195 177.892 153.141 1.00 20.45  ? 260 PHE A CA    1 
ATOM   1986  C  C     . PHE A 1 260 ? 158.778 177.844 152.582 1.00 13.33  ? 260 PHE A C     1 
ATOM   1987  O  O     . PHE A 1 260 ? 157.827 178.026 153.347 1.00 24.82  ? 260 PHE A O     1 
ATOM   1988  C  CB    . PHE A 1 260 ? 160.453 179.282 153.737 1.00 14.16  ? 260 PHE A CB    1 
ATOM   1989  C  CG    . PHE A 1 260 ? 161.398 179.283 154.907 1.00 15.61  ? 260 PHE A CG    1 
ATOM   1990  C  CD1   . PHE A 1 260 ? 162.127 178.151 155.232 1.00 15.09  ? 260 PHE A CD1   1 
ATOM   1991  C  CD2   . PHE A 1 260 ? 161.558 180.420 155.681 1.00 15.72  ? 260 PHE A CD2   1 
ATOM   1992  C  CE1   . PHE A 1 260 ? 162.996 178.156 156.307 1.00 16.22  ? 260 PHE A CE1   1 
ATOM   1993  C  CE2   . PHE A 1 260 ? 162.424 180.430 156.757 1.00 20.86  ? 260 PHE A CE2   1 
ATOM   1994  C  CZ    . PHE A 1 260 ? 163.144 179.295 157.070 1.00 17.46  ? 260 PHE A CZ    1 
ATOM   1995  N  N     . LEU A 1 261 ? 158.612 177.604 151.279 1.00 13.23  ? 261 LEU A N     1 
ATOM   1996  C  CA    . LEU A 1 261 ? 157.292 177.712 150.661 1.00 11.95  ? 261 LEU A CA    1 
ATOM   1997  C  C     . LEU A 1 261 ? 156.317 176.691 151.239 1.00 14.92  ? 261 LEU A C     1 
ATOM   1998  O  O     . LEU A 1 261 ? 155.310 177.055 151.857 1.00 20.24  ? 261 LEU A O     1 
ATOM   1999  C  CB    . LEU A 1 261 ? 157.410 177.546 149.145 1.00 16.65  ? 261 LEU A CB    1 
ATOM   2000  C  CG    . LEU A 1 261 ? 156.094 177.617 148.368 1.00 17.28  ? 261 LEU A CG    1 
ATOM   2001  C  CD1   . LEU A 1 261 ? 155.398 178.947 148.612 1.00 13.17  ? 261 LEU A CD1   1 
ATOM   2002  C  CD2   . LEU A 1 261 ? 156.329 177.395 146.882 1.00 12.40  ? 261 LEU A CD2   1 
ATOM   2003  N  N     . ILE A 1 262 ? 156.596 175.403 151.033 1.00 14.83  ? 262 ILE A N     1 
ATOM   2004  C  CA    . ILE A 1 262 ? 155.703 174.360 151.542 1.00 15.13  ? 262 ILE A CA    1 
ATOM   2005  C  C     . ILE A 1 262 ? 155.604 174.376 153.065 1.00 18.91  ? 262 ILE A C     1 
ATOM   2006  O  O     . ILE A 1 262 ? 154.483 174.271 153.588 1.00 22.36  ? 262 ILE A O     1 
ATOM   2007  C  CB    . ILE A 1 262 ? 156.121 172.987 150.985 1.00 7.15   ? 262 ILE A CB    1 
ATOM   2008  C  CG1   . ILE A 1 262 ? 155.911 172.945 149.470 1.00 12.57  ? 262 ILE A CG1   1 
ATOM   2009  C  CG2   . ILE A 1 262 ? 155.338 171.873 151.662 1.00 7.95   ? 262 ILE A CG2   1 
ATOM   2010  C  CD1   . ILE A 1 262 ? 156.240 171.611 148.842 1.00 2.56   ? 262 ILE A CD1   1 
ATOM   2011  N  N     . PRO A 1 263 ? 156.701 174.487 153.828 1.00 21.40  ? 263 PRO A N     1 
ATOM   2012  C  CA    . PRO A 1 263 ? 156.548 174.556 155.292 1.00 20.05  ? 263 PRO A CA    1 
ATOM   2013  C  C     . PRO A 1 263 ? 155.671 175.703 155.768 1.00 20.30  ? 263 PRO A C     1 
ATOM   2014  O  O     . PRO A 1 263 ? 154.914 175.536 156.732 1.00 22.28  ? 263 PRO A O     1 
ATOM   2015  C  CB    . PRO A 1 263 ? 157.993 174.710 155.779 1.00 18.78  ? 263 PRO A CB    1 
ATOM   2016  C  CG    . PRO A 1 263 ? 158.804 174.055 154.734 1.00 14.04  ? 263 PRO A CG    1 
ATOM   2017  C  CD    . PRO A 1 263 ? 158.123 174.395 153.445 1.00 19.33  ? 263 PRO A CD    1 
ATOM   2018  N  N     . THR A 1 264 ? 155.754 176.868 155.123 1.00 12.28  ? 264 THR A N     1 
ATOM   2019  C  CA    . THR A 1 264 ? 154.880 177.976 155.499 1.00 14.36  ? 264 THR A CA    1 
ATOM   2020  C  C     . THR A 1 264 ? 153.441 177.708 155.079 1.00 14.80  ? 264 THR A C     1 
ATOM   2021  O  O     . THR A 1 264 ? 152.504 178.007 155.829 1.00 28.33  ? 264 THR A O     1 
ATOM   2022  C  CB    . THR A 1 264 ? 155.382 179.283 154.884 1.00 15.44  ? 264 THR A CB    1 
ATOM   2023  O  OG1   . THR A 1 264 ? 156.777 179.443 155.169 1.00 15.40  ? 264 THR A OG1   1 
ATOM   2024  C  CG2   . THR A 1 264 ? 154.617 180.467 155.449 1.00 8.01   ? 264 THR A CG2   1 
ATOM   2025  N  N     . ALA A 1 265 ? 153.245 177.144 153.885 1.00 17.04  ? 265 ALA A N     1 
ATOM   2026  C  CA    . ALA A 1 265 ? 151.896 176.858 153.408 1.00 19.33  ? 265 ALA A CA    1 
ATOM   2027  C  C     . ALA A 1 265 ? 151.204 175.809 154.268 1.00 15.32  ? 265 ALA A C     1 
ATOM   2028  O  O     . ALA A 1 265 ? 149.974 175.829 154.394 1.00 25.17  ? 265 ALA A O     1 
ATOM   2029  C  CB    . ALA A 1 265 ? 151.938 176.408 151.949 1.00 2.75   ? 265 ALA A CB    1 
ATOM   2030  N  N     . LEU A 1 266 ? 151.967 174.884 154.854 1.00 13.99  ? 266 LEU A N     1 
ATOM   2031  C  CA    . LEU A 1 266 ? 151.373 173.891 155.742 1.00 12.32  ? 266 LEU A CA    1 
ATOM   2032  C  C     . LEU A 1 266 ? 150.785 174.546 156.985 1.00 19.64  ? 266 LEU A C     1 
ATOM   2033  O  O     . LEU A 1 266 ? 149.724 174.135 157.470 1.00 25.11  ? 266 LEU A O     1 
ATOM   2034  C  CB    . LEU A 1 266 ? 152.414 172.840 156.126 1.00 12.70  ? 266 LEU A CB    1 
ATOM   2035  C  CG    . LEU A 1 266 ? 152.611 171.708 155.114 1.00 19.63  ? 266 LEU A CG    1 
ATOM   2036  C  CD1   . LEU A 1 266 ? 153.923 170.981 155.360 1.00 15.01  ? 266 LEU A CD1   1 
ATOM   2037  C  CD2   . LEU A 1 266 ? 151.439 170.739 155.159 1.00 15.97  ? 266 LEU A CD2   1 
ATOM   2038  N  N     . CYS A 1 267 ? 151.466 175.562 157.523 1.00 18.54  ? 267 CYS A N     1 
ATOM   2039  C  CA    . CYS A 1 267 ? 150.917 176.301 158.655 1.00 28.81  ? 267 CYS A CA    1 
ATOM   2040  C  C     . CYS A 1 267 ? 149.638 177.032 158.266 1.00 22.36  ? 267 CYS A C     1 
ATOM   2041  O  O     . CYS A 1 267 ? 148.672 177.062 159.038 1.00 25.03  ? 267 CYS A O     1 
ATOM   2042  C  CB    . CYS A 1 267 ? 151.955 177.283 159.196 1.00 16.47  ? 267 CYS A CB    1 
ATOM   2043  S  SG    . CYS A 1 267 ? 153.397 176.504 159.960 1.00 33.89  ? 267 CYS A SG    1 
ATOM   2044  N  N     . PHE A 1 268 ? 149.616 177.633 157.074 1.00 20.75  ? 268 PHE A N     1 
ATOM   2045  C  CA    . PHE A 1 268 ? 148.398 178.277 156.592 1.00 18.15  ? 268 PHE A CA    1 
ATOM   2046  C  C     . PHE A 1 268 ? 147.285 177.258 156.380 1.00 24.56  ? 268 PHE A C     1 
ATOM   2047  O  O     . PHE A 1 268 ? 146.121 177.521 156.705 1.00 28.55  ? 268 PHE A O     1 
ATOM   2048  C  CB    . PHE A 1 268 ? 148.683 179.037 155.297 1.00 19.73  ? 268 PHE A CB    1 
ATOM   2049  C  CG    . PHE A 1 268 ? 149.238 180.417 155.511 1.00 21.85  ? 268 PHE A CG    1 
ATOM   2050  C  CD1   . PHE A 1 268 ? 148.536 181.353 156.252 1.00 20.21  ? 268 PHE A CD1   1 
ATOM   2051  C  CD2   . PHE A 1 268 ? 150.461 180.778 154.970 1.00 14.18  ? 268 PHE A CD2   1 
ATOM   2052  C  CE1   . PHE A 1 268 ? 149.044 182.623 156.450 1.00 24.37  ? 268 PHE A CE1   1 
ATOM   2053  C  CE2   . PHE A 1 268 ? 150.974 182.046 155.164 1.00 15.15  ? 268 PHE A CE2   1 
ATOM   2054  C  CZ    . PHE A 1 268 ? 150.264 182.970 155.905 1.00 23.33  ? 268 PHE A CZ    1 
ATOM   2055  N  N     . ALA A 1 269 ? 147.623 176.088 155.831 1.00 16.20  ? 269 ALA A N     1 
ATOM   2056  C  CA    . ALA A 1 269 ? 146.629 175.037 155.648 1.00 20.03  ? 269 ALA A CA    1 
ATOM   2057  C  C     . ALA A 1 269 ? 146.140 174.487 156.981 1.00 24.12  ? 269 ALA A C     1 
ATOM   2058  O  O     . ALA A 1 269 ? 144.980 174.075 157.092 1.00 26.55  ? 269 ALA A O     1 
ATOM   2059  C  CB    . ALA A 1 269 ? 147.205 173.910 154.791 1.00 13.69  ? 269 ALA A CB    1 
ATOM   2060  N  N     . PHE A 1 270 ? 147.009 174.462 157.994 1.00 22.09  ? 270 PHE A N     1 
ATOM   2061  C  CA    . PHE A 1 270 ? 146.611 173.958 159.305 1.00 21.69  ? 270 PHE A CA    1 
ATOM   2062  C  C     . PHE A 1 270 ? 145.503 174.810 159.912 1.00 23.47  ? 270 PHE A C     1 
ATOM   2063  O  O     . PHE A 1 270 ? 144.541 174.279 160.480 1.00 27.09  ? 270 PHE A O     1 
ATOM   2064  C  CB    . PHE A 1 270 ? 147.826 173.910 160.231 1.00 20.77  ? 270 PHE A CB    1 
ATOM   2065  C  CG    . PHE A 1 270 ? 147.520 173.405 161.609 1.00 18.65  ? 270 PHE A CG    1 
ATOM   2066  C  CD1   . PHE A 1 270 ? 147.019 172.128 161.799 1.00 23.72  ? 270 PHE A CD1   1 
ATOM   2067  C  CD2   . PHE A 1 270 ? 147.738 174.206 162.717 1.00 31.39  ? 270 PHE A CD2   1 
ATOM   2068  C  CE1   . PHE A 1 270 ? 146.739 171.661 163.068 1.00 30.29  ? 270 PHE A CE1   1 
ATOM   2069  C  CE2   . PHE A 1 270 ? 147.461 173.745 163.988 1.00 26.46  ? 270 PHE A CE2   1 
ATOM   2070  C  CZ    . PHE A 1 270 ? 146.962 172.471 164.164 1.00 29.76  ? 270 PHE A CZ    1 
ATOM   2071  N  N     . GLY A 1 271 ? 145.620 176.134 159.802 1.00 24.13  ? 271 GLY A N     1 
ATOM   2072  C  CA    . GLY A 1 271 ? 144.576 177.004 160.318 1.00 24.07  ? 271 GLY A CA    1 
ATOM   2073  C  C     . GLY A 1 271 ? 143.272 176.878 159.555 1.00 21.92  ? 271 GLY A C     1 
ATOM   2074  O  O     . GLY A 1 271 ? 142.191 176.884 160.150 1.00 23.28  ? 271 GLY A O     1 
ATOM   2075  N  N     . GLU A 1 272 ? 143.352 176.769 158.226 1.00 26.04  ? 272 GLU A N     1 
ATOM   2076  C  CA    . GLU A 1 272 ? 142.143 176.666 157.414 1.00 23.78  ? 272 GLU A CA    1 
ATOM   2077  C  C     . GLU A 1 272 ? 141.387 175.373 157.699 1.00 26.04  ? 272 GLU A C     1 
ATOM   2078  O  O     . GLU A 1 272 ? 140.154 175.378 157.791 1.00 31.91  ? 272 GLU A O     1 
ATOM   2079  C  CB    . GLU A 1 272 ? 142.499 176.765 155.931 1.00 25.59  ? 272 GLU A CB    1 
ATOM   2080  C  CG    . GLU A 1 272 ? 141.312 176.615 154.994 1.00 29.29  ? 272 GLU A CG    1 
ATOM   2081  C  CD    . GLU A 1 272 ? 141.577 177.198 153.621 1.00 39.47  ? 272 GLU A CD    1 
ATOM   2082  O  OE1   . GLU A 1 272 ? 142.619 177.865 153.449 1.00 40.61  ? 272 GLU A OE1   1 
ATOM   2083  O  OE2   . GLU A 1 272 ? 140.745 176.989 152.713 1.00 39.96  ? 272 GLU A OE2   1 
ATOM   2084  N  N     . VAL A 1 273 ? 142.107 174.258 157.838 1.00 24.14  ? 273 VAL A N     1 
ATOM   2085  C  CA    . VAL A 1 273 ? 141.457 172.977 158.101 1.00 26.02  ? 273 VAL A CA    1 
ATOM   2086  C  C     . VAL A 1 273 ? 140.769 172.993 159.461 1.00 24.87  ? 273 VAL A C     1 
ATOM   2087  O  O     . VAL A 1 273 ? 139.632 172.527 159.602 1.00 35.00  ? 273 VAL A O     1 
ATOM   2088  C  CB    . VAL A 1 273 ? 142.479 171.831 157.990 1.00 24.77  ? 273 VAL A CB    1 
ATOM   2089  C  CG1   . VAL A 1 273 ? 141.922 170.553 158.601 1.00 26.13  ? 273 VAL A CG1   1 
ATOM   2090  C  CG2   . VAL A 1 273 ? 142.865 171.606 156.537 1.00 26.09  ? 273 VAL A CG2   1 
ATOM   2091  N  N     . MET A 1 274 ? 141.439 173.536 160.478 1.00 28.69  ? 274 MET A N     1 
ATOM   2092  C  CA    . MET A 1 274 ? 140.866 173.597 161.817 1.00 29.26  ? 274 MET A CA    1 
ATOM   2093  C  C     . MET A 1 274 ? 139.724 174.598 161.930 1.00 30.89  ? 274 MET A C     1 
ATOM   2094  O  O     . MET A 1 274 ? 139.031 174.604 162.953 1.00 36.02  ? 274 MET A O     1 
ATOM   2095  C  CB    . MET A 1 274 ? 141.953 173.943 162.838 1.00 27.20  ? 274 MET A CB    1 
ATOM   2096  C  CG    . MET A 1 274 ? 142.973 172.838 163.066 1.00 28.78  ? 274 MET A CG    1 
ATOM   2097  S  SD    . MET A 1 274 ? 142.259 171.185 162.994 1.00 46.60  ? 274 MET A SD    1 
ATOM   2098  C  CE    . MET A 1 274 ? 141.344 171.140 164.534 1.00 28.24  ? 274 MET A CE    1 
ATOM   2099  N  N     . GLY A 1 275 ? 139.513 175.438 160.919 1.00 30.79  ? 275 GLY A N     1 
ATOM   2100  C  CA    . GLY A 1 275 ? 138.472 176.440 160.963 1.00 28.35  ? 275 GLY A CA    1 
ATOM   2101  C  C     . GLY A 1 275 ? 138.834 177.709 161.701 1.00 35.59  ? 275 GLY A C     1 
ATOM   2102  O  O     . GLY A 1 275 ? 137.983 178.599 161.820 1.00 44.96  ? 275 GLY A O     1 
ATOM   2103  N  N     . ASP A 1 276 ? 140.064 177.824 162.197 1.00 35.15  ? 276 ASP A N     1 
ATOM   2104  C  CA    . ASP A 1 276 ? 140.526 179.008 162.914 1.00 23.47  ? 276 ASP A CA    1 
ATOM   2105  C  C     . ASP A 1 276 ? 141.901 179.380 162.379 1.00 25.10  ? 276 ASP A C     1 
ATOM   2106  O  O     . ASP A 1 276 ? 142.894 178.717 162.695 1.00 33.07  ? 276 ASP A O     1 
ATOM   2107  C  CB    . ASP A 1 276 ? 140.574 178.758 164.422 1.00 28.66  ? 276 ASP A CB    1 
ATOM   2108  C  CG    . ASP A 1 276 ? 140.817 180.025 165.216 1.00 38.22  ? 276 ASP A CG    1 
ATOM   2109  O  OD1   . ASP A 1 276 ? 140.455 181.116 164.725 1.00 41.30  ? 276 ASP A OD1   1 
ATOM   2110  O  OD2   . ASP A 1 276 ? 141.370 179.931 166.332 1.00 40.11  ? 276 ASP A OD2   1 
ATOM   2111  N  N     . ARG A 1 277 ? 141.958 180.440 161.569 1.00 30.68  ? 277 ARG A N     1 
ATOM   2112  C  CA    . ARG A 1 277 ? 143.220 180.859 160.972 1.00 25.69  ? 277 ARG A CA    1 
ATOM   2113  C  C     . ARG A 1 277 ? 144.195 181.417 161.999 1.00 26.77  ? 277 ARG A C     1 
ATOM   2114  O  O     . ARG A 1 277 ? 145.392 181.515 161.708 1.00 35.49  ? 277 ARG A O     1 
ATOM   2115  C  CB    . ARG A 1 277 ? 142.964 181.895 159.877 1.00 27.45  ? 277 ARG A CB    1 
ATOM   2116  C  CG    . ARG A 1 277 ? 142.252 181.339 158.654 1.00 31.85  ? 277 ARG A CG    1 
ATOM   2117  C  CD    . ARG A 1 277 ? 142.313 182.309 157.486 1.00 29.91  ? 277 ARG A CD    1 
ATOM   2118  N  NE    . ARG A 1 277 ? 143.570 182.207 156.756 1.00 40.26  ? 277 ARG A NE    1 
ATOM   2119  C  CZ    . ARG A 1 277 ? 143.779 181.388 155.734 1.00 37.19  ? 277 ARG A CZ    1 
ATOM   2120  N  NH1   . ARG A 1 277 ? 142.830 180.580 155.290 1.00 34.53  ? 277 ARG A NH1   1 
ATOM   2121  N  NH2   . ARG A 1 277 ? 144.970 181.380 155.142 1.00 36.15  ? 277 ARG A NH2   1 
ATOM   2122  N  N     . ARG A 1 278 ? 143.715 181.789 163.188 1.00 29.43  ? 278 ARG A N     1 
ATOM   2123  C  CA    . ARG A 1 278 ? 144.614 182.281 164.226 1.00 30.34  ? 278 ARG A CA    1 
ATOM   2124  C  C     . ARG A 1 278 ? 145.569 181.194 164.704 1.00 22.24  ? 278 ARG A C     1 
ATOM   2125  O  O     . ARG A 1 278 ? 146.703 181.496 165.092 1.00 27.17  ? 278 ARG A O     1 
ATOM   2126  C  CB    . ARG A 1 278 ? 143.809 182.835 165.402 1.00 28.86  ? 278 ARG A CB    1 
ATOM   2127  C  CG    . ARG A 1 278 ? 142.935 184.026 165.049 1.00 30.40  ? 278 ARG A CG    1 
ATOM   2128  C  CD    . ARG A 1 278 ? 142.020 184.398 166.203 1.00 28.93  ? 278 ARG A CD    1 
ATOM   2129  N  NE    . ARG A 1 278 ? 141.198 183.272 166.628 1.00 36.68  ? 278 ARG A NE    1 
ATOM   2130  C  CZ    . ARG A 1 278 ? 140.302 183.324 167.605 1.00 35.31  ? 278 ARG A CZ    1 
ATOM   2131  N  NH1   . ARG A 1 278 ? 140.084 184.438 168.284 1.00 32.17  ? 278 ARG A NH1   1 
ATOM   2132  N  NH2   . ARG A 1 278 ? 139.609 182.230 167.908 1.00 29.54  ? 278 ARG A NH2   1 
ATOM   2133  N  N     . GLN A 1 279 ? 145.128 179.934 164.693 1.00 24.43  ? 279 GLN A N     1 
ATOM   2134  C  CA    . GLN A 1 279 ? 146.010 178.838 165.083 1.00 25.57  ? 279 GLN A CA    1 
ATOM   2135  C  C     . GLN A 1 279 ? 147.189 178.712 164.125 1.00 21.78  ? 279 GLN A C     1 
ATOM   2136  O  O     . GLN A 1 279 ? 148.329 178.504 164.556 1.00 32.29  ? 279 GLN A O     1 
ATOM   2137  C  CB    . GLN A 1 279 ? 145.223 177.529 165.144 1.00 23.46  ? 279 GLN A CB    1 
ATOM   2138  C  CG    . GLN A 1 279 ? 144.047 177.555 166.108 1.00 27.43  ? 279 GLN A CG    1 
ATOM   2139  C  CD    . GLN A 1 279 ? 144.463 177.882 167.530 1.00 30.81  ? 279 GLN A CD    1 
ATOM   2140  O  OE1   . GLN A 1 279 ? 145.449 177.350 168.039 1.00 33.15  ? 279 GLN A OE1   1 
ATOM   2141  N  NE2   . GLN A 1 279 ? 143.709 178.761 168.178 1.00 29.15  ? 279 GLN A NE2   1 
ATOM   2142  N  N     . GLY A 1 280 ? 146.932 178.830 162.821 1.00 22.40  ? 280 GLY A N     1 
ATOM   2143  C  CA    . GLY A 1 280 ? 148.019 178.785 161.857 1.00 22.80  ? 280 GLY A CA    1 
ATOM   2144  C  C     . GLY A 1 280 ? 148.949 179.978 161.964 1.00 24.80  ? 280 GLY A C     1 
ATOM   2145  O  O     . GLY A 1 280 ? 150.167 179.841 161.820 1.00 30.95  ? 280 GLY A O     1 
ATOM   2146  N  N     . ARG A 1 281 ? 148.391 181.164 162.216 1.00 21.67  ? 281 ARG A N     1 
ATOM   2147  C  CA    . ARG A 1 281 ? 149.218 182.358 162.357 1.00 25.25  ? 281 ARG A CA    1 
ATOM   2148  C  C     . ARG A 1 281 ? 150.065 182.310 163.622 1.00 25.54  ? 281 ARG A C     1 
ATOM   2149  O  O     . ARG A 1 281 ? 151.154 182.894 163.657 1.00 26.38  ? 281 ARG A O     1 
ATOM   2150  C  CB    . ARG A 1 281 ? 148.340 183.609 162.356 1.00 19.63  ? 281 ARG A CB    1 
ATOM   2151  C  CG    . ARG A 1 281 ? 147.820 184.002 160.984 1.00 24.99  ? 281 ARG A CG    1 
ATOM   2152  C  CD    . ARG A 1 281 ? 147.501 185.486 160.920 1.00 29.03  ? 281 ARG A CD    1 
ATOM   2153  N  NE    . ARG A 1 281 ? 146.351 185.834 161.746 1.00 34.27  ? 281 ARG A NE    1 
ATOM   2154  C  CZ    . ARG A 1 281 ? 145.088 185.641 161.393 1.00 29.33  ? 281 ARG A CZ    1 
ATOM   2155  N  NH1   . ARG A 1 281 ? 144.771 185.106 160.225 1.00 26.79  ? 281 ARG A NH1   1 
ATOM   2156  N  NH2   . ARG A 1 281 ? 144.118 185.995 162.231 1.00 31.70  ? 281 ARG A NH2   1 
ATOM   2157  N  N     . MET A 1 282 ? 149.581 181.636 164.667 1.00 21.26  ? 282 MET A N     1 
ATOM   2158  C  CA    . MET A 1 282 ? 150.362 181.510 165.894 1.00 22.63  ? 282 MET A CA    1 
ATOM   2159  C  C     . MET A 1 282 ? 151.648 180.734 165.639 1.00 21.70  ? 282 MET A C     1 
ATOM   2160  O  O     . MET A 1 282 ? 152.722 181.126 166.112 1.00 24.60  ? 282 MET A O     1 
ATOM   2161  C  CB    . MET A 1 282 ? 149.500 180.851 166.980 1.00 18.05  ? 282 MET A CB    1 
ATOM   2162  C  CG    . MET A 1 282 ? 150.145 180.539 168.347 1.00 26.91  ? 282 MET A CG    1 
ATOM   2163  S  SD    . MET A 1 282 ? 151.564 179.425 168.453 1.00 36.72  ? 282 MET A SD    1 
ATOM   2164  C  CE    . MET A 1 282 ? 150.744 177.834 168.408 1.00 25.36  ? 282 MET A CE    1 
ATOM   2165  N  N     . LEU A 1 283 ? 151.561 179.637 164.883 1.00 22.34  ? 283 LEU A N     1 
ATOM   2166  C  CA    . LEU A 1 283 ? 152.754 178.857 164.568 1.00 20.70  ? 283 LEU A CA    1 
ATOM   2167  C  C     . LEU A 1 283 ? 153.744 179.670 163.743 1.00 21.52  ? 283 LEU A C     1 
ATOM   2168  O  O     . LEU A 1 283 ? 154.957 179.602 163.972 1.00 20.72  ? 283 LEU A O     1 
ATOM   2169  C  CB    . LEU A 1 283 ? 152.365 177.579 163.827 1.00 19.19  ? 283 LEU A CB    1 
ATOM   2170  C  CG    . LEU A 1 283 ? 151.580 176.551 164.641 1.00 25.47  ? 283 LEU A CG    1 
ATOM   2171  C  CD1   . LEU A 1 283 ? 150.910 175.545 163.722 1.00 25.18  ? 283 LEU A CD1   1 
ATOM   2172  C  CD2   . LEU A 1 283 ? 152.497 175.855 165.634 1.00 20.60  ? 283 LEU A CD2   1 
ATOM   2173  N  N     . LEU A 1 284 ? 153.244 180.439 162.774 1.00 20.41  ? 284 LEU A N     1 
ATOM   2174  C  CA    . LEU A 1 284 ? 154.126 181.271 161.962 1.00 23.28  ? 284 LEU A CA    1 
ATOM   2175  C  C     . LEU A 1 284 ? 154.788 182.359 162.797 1.00 23.92  ? 284 LEU A C     1 
ATOM   2176  O  O     . LEU A 1 284 ? 155.969 182.665 162.599 1.00 24.97  ? 284 LEU A O     1 
ATOM   2177  C  CB    . LEU A 1 284 ? 153.346 181.881 160.798 1.00 19.36  ? 284 LEU A CB    1 
ATOM   2178  C  CG    . LEU A 1 284 ? 152.949 180.903 159.691 1.00 21.30  ? 284 LEU A CG    1 
ATOM   2179  C  CD1   . LEU A 1 284 ? 152.178 181.616 158.594 1.00 20.60  ? 284 LEU A CD1   1 
ATOM   2180  C  CD2   . LEU A 1 284 ? 154.177 180.208 159.124 1.00 24.21  ? 284 LEU A CD2   1 
ATOM   2181  N  N     . TRP A 1 285 ? 154.043 182.956 163.732 1.00 22.60  ? 285 TRP A N     1 
ATOM   2182  C  CA    . TRP A 1 285 ? 154.609 184.007 164.573 1.00 18.62  ? 285 TRP A CA    1 
ATOM   2183  C  C     . TRP A 1 285 ? 155.755 183.479 165.427 1.00 17.83  ? 285 TRP A C     1 
ATOM   2184  O  O     . TRP A 1 285 ? 156.803 184.125 165.540 1.00 29.10  ? 285 TRP A O     1 
ATOM   2185  C  CB    . TRP A 1 285 ? 153.520 184.615 165.457 1.00 16.35  ? 285 TRP A CB    1 
ATOM   2186  C  CG    . TRP A 1 285 ? 152.905 185.855 164.889 1.00 19.32  ? 285 TRP A CG    1 
ATOM   2187  C  CD1   . TRP A 1 285 ? 151.630 186.000 164.429 1.00 16.07  ? 285 TRP A CD1   1 
ATOM   2188  C  CD2   . TRP A 1 285 ? 153.540 187.129 164.722 1.00 18.50  ? 285 TRP A CD2   1 
ATOM   2189  N  NE1   . TRP A 1 285 ? 151.430 187.284 163.985 1.00 26.85  ? 285 TRP A NE1   1 
ATOM   2190  C  CE2   . TRP A 1 285 ? 152.587 187.998 164.154 1.00 20.88  ? 285 TRP A CE2   1 
ATOM   2191  C  CE3   . TRP A 1 285 ? 154.820 187.619 164.998 1.00 18.46  ? 285 TRP A CE3   1 
ATOM   2192  C  CZ2   . TRP A 1 285 ? 152.874 189.328 163.857 1.00 19.55  ? 285 TRP A CZ2   1 
ATOM   2193  C  CZ3   . TRP A 1 285 ? 155.103 188.939 164.701 1.00 19.07  ? 285 TRP A CZ3   1 
ATOM   2194  C  CH2   . TRP A 1 285 ? 154.135 189.778 164.137 1.00 20.55  ? 285 TRP A CH2   1 
ATOM   2195  N  N     . ALA A 1 286 ? 155.574 182.306 166.038 1.00 18.56  ? 286 ALA A N     1 
ATOM   2196  C  CA    . ALA A 1 286 ? 156.646 181.715 166.833 1.00 25.24  ? 286 ALA A CA    1 
ATOM   2197  C  C     . ALA A 1 286 ? 157.841 181.352 165.962 1.00 20.01  ? 286 ALA A C     1 
ATOM   2198  O  O     . ALA A 1 286 ? 158.995 181.555 166.359 1.00 22.26  ? 286 ALA A O     1 
ATOM   2199  C  CB    . ALA A 1 286 ? 156.130 180.484 167.578 1.00 16.24  ? 286 ALA A CB    1 
ATOM   2200  N  N     . MET A 1 287 ? 157.583 180.810 164.771 1.00 20.37  ? 287 MET A N     1 
ATOM   2201  C  CA    . MET A 1 287 ? 158.667 180.437 163.869 1.00 18.31  ? 287 MET A CA    1 
ATOM   2202  C  C     . MET A 1 287 ? 159.393 181.666 163.333 1.00 18.67  ? 287 MET A C     1 
ATOM   2203  O  O     . MET A 1 287 ? 160.625 181.671 163.233 1.00 20.49  ? 287 MET A O     1 
ATOM   2204  C  CB    . MET A 1 287 ? 158.113 179.595 162.719 1.00 16.68  ? 287 MET A CB    1 
ATOM   2205  C  CG    . MET A 1 287 ? 158.053 178.106 163.010 1.00 21.02  ? 287 MET A CG    1 
ATOM   2206  S  SD    . MET A 1 287 ? 157.091 177.207 161.778 1.00 31.71  ? 287 MET A SD    1 
ATOM   2207  C  CE    . MET A 1 287 ? 156.384 175.902 162.779 1.00 29.03  ? 287 MET A CE    1 
ATOM   2208  N  N     . SER A 1 288 ? 158.646 182.716 162.982 1.00 23.26  ? 288 SER A N     1 
ATOM   2209  C  CA    . SER A 1 288 ? 159.257 183.897 162.379 1.00 16.38  ? 288 SER A CA    1 
ATOM   2210  C  C     . SER A 1 288 ? 160.120 184.658 163.379 1.00 21.37  ? 288 SER A C     1 
ATOM   2211  O  O     . SER A 1 288 ? 161.188 185.166 163.020 1.00 21.85  ? 288 SER A O     1 
ATOM   2212  C  CB    . SER A 1 288 ? 158.177 184.811 161.802 1.00 10.40  ? 288 SER A CB    1 
ATOM   2213  O  OG    . SER A 1 288 ? 157.502 184.184 160.726 1.00 29.92  ? 288 SER A OG    1 
ATOM   2214  N  N     . VAL A 1 289 ? 159.671 184.757 164.633 1.00 15.24  ? 289 VAL A N     1 
ATOM   2215  C  CA    . VAL A 1 289 ? 160.413 185.522 165.633 1.00 16.76  ? 289 VAL A CA    1 
ATOM   2216  C  C     . VAL A 1 289 ? 161.783 184.898 165.871 1.00 15.65  ? 289 VAL A C     1 
ATOM   2217  O  O     . VAL A 1 289 ? 162.804 185.594 165.914 1.00 23.64  ? 289 VAL A O     1 
ATOM   2218  C  CB    . VAL A 1 289 ? 159.603 185.628 166.938 1.00 22.61  ? 289 VAL A CB    1 
ATOM   2219  C  CG1   . VAL A 1 289 ? 160.508 186.000 168.104 1.00 14.14  ? 289 VAL A CG1   1 
ATOM   2220  C  CG2   . VAL A 1 289 ? 158.483 186.646 166.784 1.00 16.04  ? 289 VAL A CG2   1 
ATOM   2221  N  N     . ILE A 1 290 ? 161.825 183.573 166.023 1.00 20.67  ? 290 ILE A N     1 
ATOM   2222  C  CA    . ILE A 1 290 ? 163.102 182.884 166.192 1.00 17.09  ? 290 ILE A CA    1 
ATOM   2223  C  C     . ILE A 1 290 ? 163.951 183.025 164.936 1.00 22.49  ? 290 ILE A C     1 
ATOM   2224  O  O     . ILE A 1 290 ? 165.164 183.260 165.010 1.00 18.24  ? 290 ILE A O     1 
ATOM   2225  C  CB    . ILE A 1 290 ? 162.868 181.406 166.555 1.00 19.59  ? 290 ILE A CB    1 
ATOM   2226  C  CG1   . ILE A 1 290 ? 162.109 181.293 167.879 1.00 25.33  ? 290 ILE A CG1   1 
ATOM   2227  C  CG2   . ILE A 1 290 ? 164.190 180.657 166.630 1.00 14.11  ? 290 ILE A CG2   1 
ATOM   2228  C  CD1   . ILE A 1 290 ? 161.488 179.935 168.108 1.00 14.89  ? 290 ILE A CD1   1 
ATOM   2229  N  N     . PHE A 1 291 ? 163.328 182.880 163.765 1.00 12.20  ? 291 PHE A N     1 
ATOM   2230  C  CA    . PHE A 1 291 ? 164.066 182.962 162.508 1.00 16.97  ? 291 PHE A CA    1 
ATOM   2231  C  C     . PHE A 1 291 ? 164.672 184.346 162.302 1.00 18.02  ? 291 PHE A C     1 
ATOM   2232  O  O     . PHE A 1 291 ? 165.826 184.467 161.877 1.00 14.97  ? 291 PHE A O     1 
ATOM   2233  C  CB    . PHE A 1 291 ? 163.145 182.599 161.343 1.00 16.24  ? 291 PHE A CB    1 
ATOM   2234  C  CG    . PHE A 1 291 ? 163.687 182.982 159.997 1.00 18.94  ? 291 PHE A CG    1 
ATOM   2235  C  CD1   . PHE A 1 291 ? 164.695 182.240 159.407 1.00 6.52   ? 291 PHE A CD1   1 
ATOM   2236  C  CD2   . PHE A 1 291 ? 163.184 184.080 159.320 1.00 14.88  ? 291 PHE A CD2   1 
ATOM   2237  C  CE1   . PHE A 1 291 ? 165.194 182.587 158.169 1.00 9.18   ? 291 PHE A CE1   1 
ATOM   2238  C  CE2   . PHE A 1 291 ? 163.680 184.433 158.080 1.00 16.25  ? 291 PHE A CE2   1 
ATOM   2239  C  CZ    . PHE A 1 291 ? 164.686 183.685 157.504 1.00 13.32  ? 291 PHE A CZ    1 
ATOM   2240  N  N     . VAL A 1 292 ? 163.908 185.401 162.595 1.00 11.39  ? 292 VAL A N     1 
ATOM   2241  C  CA    . VAL A 1 292 ? 164.383 186.760 162.346 1.00 22.55  ? 292 VAL A CA    1 
ATOM   2242  C  C     . VAL A 1 292 ? 165.586 187.079 163.226 1.00 17.52  ? 292 VAL A C     1 
ATOM   2243  O  O     . VAL A 1 292 ? 166.575 187.662 162.763 1.00 21.93  ? 292 VAL A O     1 
ATOM   2244  C  CB    . VAL A 1 292 ? 163.239 187.771 162.554 1.00 20.13  ? 292 VAL A CB    1 
ATOM   2245  C  CG1   . VAL A 1 292 ? 163.791 189.165 162.809 1.00 21.06  ? 292 VAL A CG1   1 
ATOM   2246  C  CG2   . VAL A 1 292 ? 162.313 187.774 161.348 1.00 22.93  ? 292 VAL A CG2   1 
ATOM   2247  N  N     . ILE A 1 293 ? 165.525 186.700 164.504 1.00 17.82  ? 293 ILE A N     1 
ATOM   2248  C  CA    . ILE A 1 293 ? 166.640 186.954 165.412 1.00 19.04  ? 293 ILE A CA    1 
ATOM   2249  C  C     . ILE A 1 293 ? 167.875 186.177 164.971 1.00 18.60  ? 293 ILE A C     1 
ATOM   2250  O  O     . ILE A 1 293 ? 168.999 186.692 165.012 1.00 23.00  ? 293 ILE A O     1 
ATOM   2251  C  CB    . ILE A 1 293 ? 166.237 186.612 166.859 1.00 17.87  ? 293 ILE A CB    1 
ATOM   2252  C  CG1   . ILE A 1 293 ? 165.176 187.592 167.363 1.00 21.81  ? 293 ILE A CG1   1 
ATOM   2253  C  CG2   . ILE A 1 293 ? 167.451 186.626 167.776 1.00 15.29  ? 293 ILE A CG2   1 
ATOM   2254  C  CD1   . ILE A 1 293 ? 164.308 187.035 168.468 1.00 17.48  ? 293 ILE A CD1   1 
ATOM   2255  N  N     . CYS A 1 294 ? 167.684 184.929 164.537 1.00 17.71  ? 294 CYS A N     1 
ATOM   2256  C  CA    . CYS A 1 294 ? 168.813 184.102 164.121 1.00 18.35  ? 294 CYS A CA    1 
ATOM   2257  C  C     . CYS A 1 294 ? 169.528 184.698 162.913 1.00 12.91  ? 294 CYS A C     1 
ATOM   2258  O  O     . CYS A 1 294 ? 170.763 184.672 162.841 1.00 20.43  ? 294 CYS A O     1 
ATOM   2259  C  CB    . CYS A 1 294 ? 168.336 182.682 163.818 1.00 12.93  ? 294 CYS A CB    1 
ATOM   2260  S  SG    . CYS A 1 294 ? 168.045 181.666 165.285 1.00 32.37  ? 294 CYS A SG    1 
ATOM   2261  N  N     . VAL A 1 295 ? 168.772 185.230 161.949 1.00 17.53  ? 295 VAL A N     1 
ATOM   2262  C  CA    . VAL A 1 295 ? 169.390 185.842 160.774 1.00 15.77  ? 295 VAL A CA    1 
ATOM   2263  C  C     . VAL A 1 295 ? 170.218 187.055 161.176 1.00 23.97  ? 295 VAL A C     1 
ATOM   2264  O  O     . VAL A 1 295 ? 171.341 187.247 160.693 1.00 20.72  ? 295 VAL A O     1 
ATOM   2265  C  CB    . VAL A 1 295 ? 168.318 186.213 159.732 1.00 15.75  ? 295 VAL A CB    1 
ATOM   2266  C  CG1   . VAL A 1 295 ? 168.953 186.930 158.553 1.00 13.66  ? 295 VAL A CG1   1 
ATOM   2267  C  CG2   . VAL A 1 295 ? 167.582 184.976 159.260 1.00 13.47  ? 295 VAL A CG2   1 
ATOM   2268  N  N     . GLY A 1 296 ? 169.681 187.891 162.067 1.00 17.51  ? 296 GLY A N     1 
ATOM   2269  C  CA    . GLY A 1 296 ? 170.398 189.090 162.472 1.00 8.44   ? 296 GLY A CA    1 
ATOM   2270  C  C     . GLY A 1 296 ? 171.711 188.788 163.169 1.00 12.53  ? 296 GLY A C     1 
ATOM   2271  O  O     . GLY A 1 296 ? 172.714 189.470 162.944 1.00 17.78  ? 296 GLY A O     1 
ATOM   2272  N  N     . VAL A 1 297 ? 171.721 187.768 164.029 1.00 17.31  ? 297 VAL A N     1 
ATOM   2273  C  CA    . VAL A 1 297 ? 172.946 187.398 164.734 1.00 14.77  ? 297 VAL A CA    1 
ATOM   2274  C  C     . VAL A 1 297 ? 174.000 186.902 163.751 1.00 16.88  ? 297 VAL A C     1 
ATOM   2275  O  O     . VAL A 1 297 ? 175.174 187.286 163.831 1.00 13.07  ? 297 VAL A O     1 
ATOM   2276  C  CB    . VAL A 1 297 ? 172.642 186.348 165.819 1.00 15.53  ? 297 VAL A CB    1 
ATOM   2277  C  CG1   . VAL A 1 297 ? 173.931 185.839 166.446 1.00 10.17  ? 297 VAL A CG1   1 
ATOM   2278  C  CG2   . VAL A 1 297 ? 171.724 186.934 166.880 1.00 12.89  ? 297 VAL A CG2   1 
ATOM   2279  N  N     . VAL A 1 298 ? 173.601 186.044 162.810 1.00 17.63  ? 298 VAL A N     1 
ATOM   2280  C  CA    . VAL A 1 298 ? 174.550 185.525 161.829 1.00 16.24  ? 298 VAL A CA    1 
ATOM   2281  C  C     . VAL A 1 298 ? 175.039 186.641 160.914 1.00 7.01   ? 298 VAL A C     1 
ATOM   2282  O  O     . VAL A 1 298 ? 176.229 186.714 160.584 1.00 14.10  ? 298 VAL A O     1 
ATOM   2283  C  CB    . VAL A 1 298 ? 173.917 184.368 161.035 1.00 20.60  ? 298 VAL A CB    1 
ATOM   2284  C  CG1   . VAL A 1 298 ? 174.840 183.923 159.913 1.00 5.94   ? 298 VAL A CG1   1 
ATOM   2285  C  CG2   . VAL A 1 298 ? 173.610 183.205 161.961 1.00 10.69  ? 298 VAL A CG2   1 
ATOM   2286  N  N     . MET A 1 299 ? 174.134 187.530 160.493 1.00 13.29  ? 299 MET A N     1 
ATOM   2287  C  CA    . MET A 1 299 ? 174.546 188.669 159.678 1.00 14.66  ? 299 MET A CA    1 
ATOM   2288  C  C     . MET A 1 299 ? 175.535 189.550 160.429 1.00 20.31  ? 299 MET A C     1 
ATOM   2289  O  O     . MET A 1 299 ? 176.546 189.984 159.865 1.00 23.12  ? 299 MET A O     1 
ATOM   2290  C  CB    . MET A 1 299 ? 173.326 189.486 159.254 1.00 10.39  ? 299 MET A CB    1 
ATOM   2291  C  CG    . MET A 1 299 ? 172.533 188.895 158.103 1.00 14.97  ? 299 MET A CG    1 
ATOM   2292  S  SD    . MET A 1 299 ? 171.011 189.811 157.794 1.00 30.33  ? 299 MET A SD    1 
ATOM   2293  C  CE    . MET A 1 299 ? 170.872 189.658 156.016 1.00 21.03  ? 299 MET A CE    1 
ATOM   2294  N  N     . TRP A 1 300 ? 175.261 189.820 161.707 1.00 18.12  ? 300 TRP A N     1 
ATOM   2295  C  CA    . TRP A 1 300 ? 176.172 190.633 162.505 1.00 17.16  ? 300 TRP A CA    1 
ATOM   2296  C  C     . TRP A 1 300 ? 177.516 189.940 162.690 1.00 17.96  ? 300 TRP A C     1 
ATOM   2297  O  O     . TRP A 1 300 ? 178.570 190.576 162.583 1.00 19.09  ? 300 TRP A O     1 
ATOM   2298  C  CB    . TRP A 1 300 ? 175.539 190.950 163.860 1.00 12.65  ? 300 TRP A CB    1 
ATOM   2299  C  CG    . TRP A 1 300 ? 176.488 191.572 164.834 1.00 21.59  ? 300 TRP A CG    1 
ATOM   2300  C  CD1   . TRP A 1 300 ? 176.881 192.877 164.875 1.00 19.81  ? 300 TRP A CD1   1 
ATOM   2301  C  CD2   . TRP A 1 300 ? 177.167 190.914 165.909 1.00 17.57  ? 300 TRP A CD2   1 
ATOM   2302  N  NE1   . TRP A 1 300 ? 177.763 193.073 165.910 1.00 23.01  ? 300 TRP A NE1   1 
ATOM   2303  C  CE2   . TRP A 1 300 ? 177.955 191.883 166.561 1.00 21.21  ? 300 TRP A CE2   1 
ATOM   2304  C  CE3   . TRP A 1 300 ? 177.185 189.599 166.386 1.00 14.13  ? 300 TRP A CE3   1 
ATOM   2305  C  CZ2   . TRP A 1 300 ? 178.752 191.580 167.662 1.00 22.43  ? 300 TRP A CZ2   1 
ATOM   2306  C  CZ3   . TRP A 1 300 ? 177.977 189.300 167.479 1.00 23.87  ? 300 TRP A CZ3   1 
ATOM   2307  C  CH2   . TRP A 1 300 ? 178.749 190.286 168.105 1.00 22.91  ? 300 TRP A CH2   1 
ATOM   2308  N  N     . ALA A 1 301 ? 177.499 188.633 162.965 1.00 14.73  ? 301 ALA A N     1 
ATOM   2309  C  CA    . ALA A 1 301 ? 178.743 187.903 163.190 1.00 14.69  ? 301 ALA A CA    1 
ATOM   2310  C  C     . ALA A 1 301 ? 179.602 187.860 161.931 1.00 23.02  ? 301 ALA A C     1 
ATOM   2311  O  O     . ALA A 1 301 ? 180.827 188.006 162.004 1.00 25.69  ? 301 ALA A O     1 
ATOM   2312  C  CB    . ALA A 1 301 ? 178.441 186.488 163.681 1.00 12.20  ? 301 ALA A CB    1 
ATOM   2313  N  N     . GLU A 1 302 ? 178.979 187.654 160.769 1.00 21.63  ? 302 GLU A N     1 
ATOM   2314  C  CA    . GLU A 1 302 ? 179.746 187.558 159.532 1.00 14.87  ? 302 GLU A CA    1 
ATOM   2315  C  C     . GLU A 1 302 ? 180.239 188.921 159.062 1.00 19.01  ? 302 GLU A C     1 
ATOM   2316  O  O     . GLU A 1 302 ? 181.255 189.001 158.362 1.00 17.65  ? 302 GLU A O     1 
ATOM   2317  C  CB    . GLU A 1 302 ? 178.906 186.888 158.445 1.00 14.66  ? 302 GLU A CB    1 
ATOM   2318  C  CG    . GLU A 1 302 ? 178.649 185.407 158.682 1.00 19.67  ? 302 GLU A CG    1 
ATOM   2319  C  CD    . GLU A 1 302 ? 179.915 184.635 159.003 1.00 17.94  ? 302 GLU A CD    1 
ATOM   2320  O  OE1   . GLU A 1 302 ? 180.761 184.474 158.100 1.00 24.38  ? 302 GLU A OE1   1 
ATOM   2321  O  OE2   . GLU A 1 302 ? 180.062 184.185 160.159 1.00 26.04  ? 302 GLU A OE2   1 
ATOM   2322  N  N     . VAL A 1 303 ? 179.536 189.998 159.423 1.00 20.19  ? 303 VAL A N     1 
ATOM   2323  C  CA    . VAL A 1 303 ? 179.979 191.337 159.040 1.00 21.26  ? 303 VAL A CA    1 
ATOM   2324  C  C     . VAL A 1 303 ? 181.297 191.678 159.726 1.00 20.82  ? 303 VAL A C     1 
ATOM   2325  O  O     . VAL A 1 303 ? 182.228 192.194 159.094 1.00 26.16  ? 303 VAL A O     1 
ATOM   2326  C  CB    . VAL A 1 303 ? 178.885 192.375 159.349 1.00 25.01  ? 303 VAL A CB    1 
ATOM   2327  C  CG1   . VAL A 1 303 ? 179.493 193.753 159.564 1.00 23.38  ? 303 VAL A CG1   1 
ATOM   2328  C  CG2   . VAL A 1 303 ? 177.867 192.417 158.221 1.00 24.85  ? 303 VAL A CG2   1 
ATOM   2329  N  N     . GLN A 1 304 ? 181.401 191.396 161.029 1.00 23.07  ? 304 GLN A N     1 
ATOM   2330  C  CA    . GLN A 1 304 ? 182.683 191.557 161.709 1.00 26.56  ? 304 GLN A CA    1 
ATOM   2331  C  C     . GLN A 1 304 ? 183.730 190.621 161.120 1.00 24.83  ? 304 GLN A C     1 
ATOM   2332  O  O     . GLN A 1 304 ? 184.876 191.024 160.890 1.00 34.22  ? 304 GLN A O     1 
ATOM   2333  C  CB    . GLN A 1 304 ? 182.529 191.313 163.211 1.00 27.03  ? 304 GLN A CB    1 
ATOM   2334  C  CG    . GLN A 1 304 ? 181.192 191.738 163.786 1.00 21.05  ? 304 GLN A CG    1 
ATOM   2335  C  CD    . GLN A 1 304 ? 181.173 193.194 164.205 1.00 32.63  ? 304 GLN A CD    1 
ATOM   2336  O  OE1   . GLN A 1 304 ? 180.420 194.000 163.659 1.00 32.54  ? 304 GLN A OE1   1 
ATOM   2337  N  NE2   . GLN A 1 304 ? 182.005 193.540 165.181 1.00 36.67  ? 304 GLN A NE2   1 
ATOM   2338  N  N     . GLY A 1 305 ? 183.351 189.370 160.869 1.00 21.61  ? 305 GLY A N     1 
ATOM   2339  C  CA    . GLY A 1 305 ? 184.201 188.456 160.125 1.00 25.23  ? 305 GLY A CA    1 
ATOM   2340  C  C     . GLY A 1 305 ? 185.509 188.157 160.828 1.00 25.19  ? 305 GLY A C     1 
ATOM   2341  O  O     . GLY A 1 305 ? 185.587 188.084 162.059 1.00 33.17  ? 305 GLY A O     1 
ATOM   2342  N  N     . ASN A 1 306 ? 186.554 187.980 160.028 1.00 30.70  ? 306 ASN A N     1 
ATOM   2343  C  CA    . ASN A 1 306 ? 187.870 187.640 160.552 1.00 26.91  ? 306 ASN A CA    1 
ATOM   2344  C  C     . ASN A 1 306 ? 188.552 188.885 161.104 1.00 29.82  ? 306 ASN A C     1 
ATOM   2345  O  O     . ASN A 1 306 ? 188.790 189.833 160.348 1.00 29.06  ? 306 ASN A O     1 
ATOM   2346  C  CB    . ASN A 1 306 ? 188.726 187.017 159.457 1.00 28.54  ? 306 ASN A CB    1 
ATOM   2347  C  CG    . ASN A 1 306 ? 189.739 186.031 159.995 1.00 33.87  ? 306 ASN A CG    1 
ATOM   2348  O  OD1   . ASN A 1 306 ? 190.281 186.213 161.085 1.00 45.40  ? 306 ASN A OD1   1 
ATOM   2349  N  ND2   . ASN A 1 306 ? 190.003 184.978 159.232 1.00 30.90  ? 306 ASN A ND2   1 
ATOM   2350  N  N     . PRO A 1 307 ? 188.881 188.929 162.398 1.00 36.58  ? 307 PRO A N     1 
ATOM   2351  C  CA    . PRO A 1 307 ? 189.629 190.082 162.923 1.00 34.45  ? 307 PRO A CA    1 
ATOM   2352  C  C     . PRO A 1 307 ? 191.042 190.185 162.380 1.00 35.55  ? 307 PRO A C     1 
ATOM   2353  O  O     . PRO A 1 307 ? 191.623 191.277 162.419 1.00 42.98  ? 307 PRO A O     1 
ATOM   2354  C  CB    . PRO A 1 307 ? 189.629 189.842 164.439 1.00 34.58  ? 307 PRO A CB    1 
ATOM   2355  C  CG    . PRO A 1 307 ? 189.455 188.368 164.587 1.00 35.51  ? 307 PRO A CG    1 
ATOM   2356  C  CD    . PRO A 1 307 ? 188.586 187.932 163.442 1.00 30.76  ? 307 PRO A CD    1 
ATOM   2357  N  N     . HIS A 1 308 ? 191.614 189.090 161.876 1.00 33.33  ? 308 HIS A N     1 
ATOM   2358  C  CA    . HIS A 1 308 ? 192.980 189.112 161.370 1.00 30.45  ? 308 HIS A CA    1 
ATOM   2359  C  C     . HIS A 1 308 ? 193.082 189.687 159.964 1.00 33.45  ? 308 HIS A C     1 
ATOM   2360  O  O     . HIS A 1 308 ? 194.189 190.023 159.530 1.00 41.05  ? 308 HIS A O     1 
ATOM   2361  C  CB    . HIS A 1 308 ? 193.569 187.700 161.383 1.00 30.99  ? 308 HIS A CB    1 
ATOM   2362  C  CG    . HIS A 1 308 ? 193.475 187.018 162.712 1.00 37.43  ? 308 HIS A CG    1 
ATOM   2363  N  ND1   . HIS A 1 308 ? 193.155 185.684 162.842 1.00 38.73  ? 308 HIS A ND1   1 
ATOM   2364  C  CD2   . HIS A 1 308 ? 193.660 187.485 163.969 1.00 37.34  ? 308 HIS A CD2   1 
ATOM   2365  C  CE1   . HIS A 1 308 ? 193.146 185.358 164.122 1.00 38.15  ? 308 HIS A CE1   1 
ATOM   2366  N  NE2   . HIS A 1 308 ? 193.449 186.433 164.827 1.00 38.88  ? 308 HIS A NE2   1 
ATOM   2367  N  N     . LEU A 1 309 ? 191.962 189.807 159.247 1.00 32.69  ? 309 LEU A N     1 
ATOM   2368  C  CA    . LEU A 1 309 ? 192.012 190.287 157.869 1.00 33.70  ? 309 LEU A CA    1 
ATOM   2369  C  C     . LEU A 1 309 ? 192.529 191.718 157.795 1.00 30.87  ? 309 LEU A C     1 
ATOM   2370  O  O     . LEU A 1 309 ? 193.341 192.047 156.923 1.00 33.68  ? 309 LEU A O     1 
ATOM   2371  C  CB    . LEU A 1 309 ? 190.629 190.181 157.227 1.00 30.09  ? 309 LEU A CB    1 
ATOM   2372  C  CG    . LEU A 1 309 ? 190.261 188.823 156.627 1.00 33.29  ? 309 LEU A CG    1 
ATOM   2373  C  CD1   . LEU A 1 309 ? 188.799 188.800 156.211 1.00 27.38  ? 309 LEU A CD1   1 
ATOM   2374  C  CD2   . LEU A 1 309 ? 191.164 188.491 155.449 1.00 31.92  ? 309 LEU A CD2   1 
ATOM   2375  N  N     . LEU A 1 310 ? 192.065 192.586 158.698 1.00 33.67  ? 310 LEU A N     1 
ATOM   2376  C  CA    . LEU A 1 310 ? 192.519 193.973 158.690 1.00 29.57  ? 310 LEU A CA    1 
ATOM   2377  C  C     . LEU A 1 310 ? 194.008 194.070 158.998 1.00 31.22  ? 310 LEU A C     1 
ATOM   2378  O  O     . LEU A 1 310 ? 194.733 194.841 158.358 1.00 33.63  ? 310 LEU A O     1 
ATOM   2379  C  CB    . LEU A 1 310 ? 191.710 194.797 159.692 1.00 32.95  ? 310 LEU A CB    1 
ATOM   2380  C  CG    . LEU A 1 310 ? 190.406 195.408 159.178 1.00 33.80  ? 310 LEU A CG    1 
ATOM   2381  C  CD1   . LEU A 1 310 ? 189.758 196.265 160.255 1.00 34.40  ? 310 LEU A CD1   1 
ATOM   2382  C  CD2   . LEU A 1 310 ? 190.650 196.220 157.917 1.00 31.13  ? 310 LEU A CD2   1 
ATOM   2383  N  N     . ALA A 1 311 ? 194.482 193.295 159.975 1.00 34.46  ? 311 ALA A N     1 
ATOM   2384  C  CA    . ALA A 1 311 ? 195.898 193.323 160.324 1.00 31.95  ? 311 ALA A CA    1 
ATOM   2385  C  C     . ALA A 1 311 ? 196.764 192.728 159.222 1.00 31.86  ? 311 ALA A C     1 
ATOM   2386  O  O     . ALA A 1 311 ? 197.902 193.167 159.026 1.00 38.80  ? 311 ALA A O     1 
ATOM   2387  C  CB    . ALA A 1 311 ? 196.131 192.582 161.640 1.00 32.81  ? 311 ALA A CB    1 
ATOM   2388  N  N     . LEU A 1 312 ? 196.249 191.731 158.498 1.00 34.31  ? 312 LEU A N     1 
ATOM   2389  C  CA    . LEU A 1 312 ? 197.030 191.101 157.441 1.00 27.37  ? 312 LEU A CA    1 
ATOM   2390  C  C     . LEU A 1 312 ? 197.177 191.992 156.214 1.00 27.26  ? 312 LEU A C     1 
ATOM   2391  O  O     . LEU A 1 312 ? 198.073 191.754 155.398 1.00 33.80  ? 312 LEU A O     1 
ATOM   2392  C  CB    . LEU A 1 312 ? 196.401 189.762 157.051 1.00 32.24  ? 312 LEU A CB    1 
ATOM   2393  C  CG    . LEU A 1 312 ? 196.699 188.603 158.006 1.00 30.18  ? 312 LEU A CG    1 
ATOM   2394  C  CD1   . LEU A 1 312 ? 195.595 187.557 157.964 1.00 32.85  ? 312 LEU A CD1   1 
ATOM   2395  C  CD2   . LEU A 1 312 ? 198.047 187.976 157.694 1.00 31.97  ? 312 LEU A CD2   1 
ATOM   2396  N  N     . GLY A 1 313 ? 196.326 193.005 156.061 1.00 27.97  ? 313 GLY A N     1 
ATOM   2397  C  CA    . GLY A 1 313 ? 196.497 193.963 154.987 1.00 26.45  ? 313 GLY A CA    1 
ATOM   2398  C  C     . GLY A 1 313 ? 195.328 194.094 154.032 1.00 32.70  ? 313 GLY A C     1 
ATOM   2399  O  O     . GLY A 1 313 ? 195.511 194.503 152.882 1.00 35.20  ? 313 GLY A O     1 
ATOM   2400  N  N     . THR A 1 314 ? 194.126 193.755 154.485 1.00 26.98  ? 314 THR A N     1 
ATOM   2401  C  CA    . THR A 1 314 ? 192.928 193.898 153.672 1.00 24.26  ? 314 THR A CA    1 
ATOM   2402  C  C     . THR A 1 314 ? 192.191 195.184 154.031 1.00 27.47  ? 314 THR A C     1 
ATOM   2403  O  O     . THR A 1 314 ? 192.394 195.770 155.097 1.00 35.76  ? 314 THR A O     1 
ATOM   2404  C  CB    . THR A 1 314 ? 191.995 192.696 153.845 1.00 22.69  ? 314 THR A CB    1 
ATOM   2405  O  OG1   . THR A 1 314 ? 191.389 192.737 155.143 1.00 34.55  ? 314 THR A OG1   1 
ATOM   2406  C  CG2   . THR A 1 314 ? 192.766 191.394 153.688 1.00 24.20  ? 314 THR A CG2   1 
ATOM   2407  N  N     . ASP A 1 315 ? 191.329 195.623 153.113 1.00 26.66  ? 315 ASP A N     1 
ATOM   2408  C  CA    . ASP A 1 315 ? 190.558 196.842 153.317 1.00 31.60  ? 315 ASP A CA    1 
ATOM   2409  C  C     . ASP A 1 315 ? 189.298 196.625 154.146 1.00 32.91  ? 315 ASP A C     1 
ATOM   2410  O  O     . ASP A 1 315 ? 188.677 197.608 154.565 1.00 35.29  ? 315 ASP A O     1 
ATOM   2411  C  CB    . ASP A 1 315 ? 190.188 197.463 151.965 1.00 30.71  ? 315 ASP A CB    1 
ATOM   2412  C  CG    . ASP A 1 315 ? 189.316 196.553 151.113 1.00 33.81  ? 315 ASP A CG    1 
ATOM   2413  O  OD1   . ASP A 1 315 ? 189.045 195.405 151.526 1.00 38.31  ? 315 ASP A OD1   1 
ATOM   2414  O  OD2   . ASP A 1 315 ? 188.898 196.991 150.021 1.00 39.38  ? 315 ASP A OD2   1 
ATOM   2415  N  N     . SER A 1 316 ? 188.908 195.376 154.391 1.00 33.66  ? 316 SER A N     1 
ATOM   2416  C  CA    . SER A 1 316 ? 187.707 195.088 155.160 1.00 27.59  ? 316 SER A CA    1 
ATOM   2417  C  C     . SER A 1 316 ? 187.905 193.784 155.919 1.00 27.96  ? 316 SER A C     1 
ATOM   2418  O  O     . SER A 1 316 ? 188.721 192.940 155.542 1.00 37.42  ? 316 SER A O     1 
ATOM   2419  C  CB    . SER A 1 316 ? 186.468 195.003 154.261 1.00 28.57  ? 316 SER A CB    1 
ATOM   2420  O  OG    . SER A 1 316 ? 185.287 194.865 155.030 1.00 38.12  ? 316 SER A OG    1 
ATOM   2421  N  N     . SER A 1 317 ? 187.143 193.632 157.000 1.00 32.54  ? 317 SER A N     1 
ATOM   2422  C  CA    . SER A 1 317 ? 187.200 192.443 157.837 1.00 29.05  ? 317 SER A CA    1 
ATOM   2423  C  C     . SER A 1 317 ? 186.034 191.493 157.593 1.00 26.84  ? 317 SER A C     1 
ATOM   2424  O  O     . SER A 1 317 ? 185.910 190.492 158.304 1.00 32.67  ? 317 SER A O     1 
ATOM   2425  C  CB    . SER A 1 317 ? 187.248 192.840 159.314 1.00 24.53  ? 317 SER A CB    1 
ATOM   2426  O  OG    . SER A 1 317 ? 185.943 192.933 159.859 1.00 33.77  ? 317 SER A OG    1 
ATOM   2427  N  N     . ILE A 1 318 ? 185.180 191.782 156.607 1.00 18.46  ? 318 ILE A N     1 
ATOM   2428  C  CA    . ILE A 1 318 ? 184.034 190.921 156.344 1.00 18.87  ? 318 ILE A CA    1 
ATOM   2429  C  C     . ILE A 1 318 ? 184.513 189.539 155.920 1.00 19.80  ? 318 ILE A C     1 
ATOM   2430  O  O     . ILE A 1 318 ? 185.460 189.396 155.135 1.00 27.55  ? 318 ILE A O     1 
ATOM   2431  C  CB    . ILE A 1 318 ? 183.114 191.551 155.285 1.00 23.97  ? 318 ILE A CB    1 
ATOM   2432  C  CG1   . ILE A 1 318 ? 183.883 191.836 153.993 1.00 27.97  ? 318 ILE A CG1   1 
ATOM   2433  C  CG2   . ILE A 1 318 ? 182.478 192.826 155.821 1.00 17.20  ? 318 ILE A CG2   1 
ATOM   2434  C  CD1   . ILE A 1 318 ? 183.005 191.903 152.765 1.00 22.68  ? 318 ILE A CD1   1 
ATOM   2435  N  N     . ASN A 1 319 ? 183.863 188.508 156.454 1.00 14.52  ? 319 ASN A N     1 
ATOM   2436  C  CA    . ASN A 1 319 ? 184.276 187.124 156.230 1.00 27.29  ? 319 ASN A CA    1 
ATOM   2437  C  C     . ASN A 1 319 ? 183.773 186.676 154.865 1.00 19.62  ? 319 ASN A C     1 
ATOM   2438  O  O     . ASN A 1 319 ? 182.712 186.065 154.735 1.00 25.87  ? 319 ASN A O     1 
ATOM   2439  C  CB    . ASN A 1 319 ? 183.755 186.219 157.340 1.00 20.27  ? 319 ASN A CB    1 
ATOM   2440  C  CG    . ASN A 1 319 ? 184.314 184.813 157.257 1.00 20.90  ? 319 ASN A CG    1 
ATOM   2441  O  OD1   . ASN A 1 319 ? 185.348 184.579 156.632 1.00 27.44  ? 319 ASN A OD1   1 
ATOM   2442  N  ND2   . ASN A 1 319 ? 183.631 183.867 157.890 1.00 19.06  ? 319 ASN A ND2   1 
ATOM   2443  N  N     . MET A 1 320 ? 184.550 186.985 153.831 1.00 22.68  ? 320 MET A N     1 
ATOM   2444  C  CA    . MET A 1 320 ? 184.247 186.554 152.474 1.00 14.82  ? 320 MET A CA    1 
ATOM   2445  C  C     . MET A 1 320 ? 184.833 185.188 152.147 1.00 12.22  ? 320 MET A C     1 
ATOM   2446  O  O     . MET A 1 320 ? 184.581 184.668 151.055 1.00 22.10  ? 320 MET A O     1 
ATOM   2447  C  CB    . MET A 1 320 ? 184.755 187.589 151.464 1.00 15.29  ? 320 MET A CB    1 
ATOM   2448  C  CG    . MET A 1 320 ? 183.709 188.608 151.040 1.00 18.32  ? 320 MET A CG    1 
ATOM   2449  S  SD    . MET A 1 320 ? 182.105 187.860 150.691 1.00 37.71  ? 320 MET A SD    1 
ATOM   2450  C  CE    . MET A 1 320 ? 182.280 187.471 148.951 1.00 19.09  ? 320 MET A CE    1 
ATOM   2451  N  N     . GLU A 1 321 ? 185.609 184.602 153.057 1.00 20.03  ? 321 GLU A N     1 
ATOM   2452  C  CA    . GLU A 1 321 ? 186.162 183.273 152.832 1.00 21.00  ? 321 GLU A CA    1 
ATOM   2453  C  C     . GLU A 1 321 ? 185.041 182.245 152.761 1.00 20.92  ? 321 GLU A C     1 
ATOM   2454  O  O     . GLU A 1 321 ? 184.140 182.233 153.606 1.00 20.09  ? 321 GLU A O     1 
ATOM   2455  C  CB    . GLU A 1 321 ? 187.146 182.915 153.946 1.00 16.13  ? 321 GLU A CB    1 
ATOM   2456  C  CG    . GLU A 1 321 ? 187.720 181.510 153.851 1.00 20.42  ? 321 GLU A CG    1 
ATOM   2457  C  CD    . GLU A 1 321 ? 188.688 181.348 152.695 1.00 28.89  ? 321 GLU A CD    1 
ATOM   2458  O  OE1   . GLU A 1 321 ? 189.347 182.342 152.325 1.00 34.77  ? 321 GLU A OE1   1 
ATOM   2459  O  OE2   . GLU A 1 321 ? 188.789 180.226 152.157 1.00 26.73  ? 321 GLU A OE2   1 
ATOM   2460  N  N     . GLY A 1 322 ? 185.098 181.381 151.752 1.00 14.55  ? 322 GLY A N     1 
ATOM   2461  C  CA    . GLY A 1 322 ? 184.041 180.407 151.545 1.00 3.66   ? 322 GLY A CA    1 
ATOM   2462  C  C     . GLY A 1 322 ? 182.705 181.019 151.195 1.00 13.32  ? 322 GLY A C     1 
ATOM   2463  O  O     . GLY A 1 322 ? 181.664 180.494 151.602 1.00 15.56  ? 322 GLY A O     1 
ATOM   2464  N  N     . LYS A 1 323 ? 182.704 182.120 150.446 1.00 15.54  ? 323 LYS A N     1 
ATOM   2465  C  CA    . LYS A 1 323 ? 181.478 182.787 150.035 1.00 15.52  ? 323 LYS A CA    1 
ATOM   2466  C  C     . LYS A 1 323 ? 181.603 183.210 148.579 1.00 6.26   ? 323 LYS A C     1 
ATOM   2467  O  O     . LYS A 1 323 ? 182.706 183.433 148.074 1.00 24.27  ? 323 LYS A O     1 
ATOM   2468  C  CB    . LYS A 1 323 ? 181.173 184.007 150.915 1.00 11.12  ? 323 LYS A CB    1 
ATOM   2469  C  CG    . LYS A 1 323 ? 180.590 183.666 152.277 1.00 11.27  ? 323 LYS A CG    1 
ATOM   2470  C  CD    . LYS A 1 323 ? 180.186 184.920 153.036 1.00 18.14  ? 323 LYS A CD    1 
ATOM   2471  C  CE    . LYS A 1 323 ? 179.707 184.592 154.441 1.00 12.64  ? 323 LYS A CE    1 
ATOM   2472  N  NZ    . LYS A 1 323 ? 180.772 183.961 155.268 1.00 15.30  ? 323 LYS A NZ    1 
ATOM   2473  N  N     . GLU A 1 324 ? 180.459 183.317 147.907 1.00 18.80  ? 324 GLU A N     1 
ATOM   2474  C  CA    . GLU A 1 324 ? 180.420 183.707 146.505 1.00 16.05  ? 324 GLU A CA    1 
ATOM   2475  C  C     . GLU A 1 324 ? 180.291 185.219 146.377 1.00 17.87  ? 324 GLU A C     1 
ATOM   2476  O  O     . GLU A 1 324 ? 179.600 185.867 147.169 1.00 25.81  ? 324 GLU A O     1 
ATOM   2477  C  CB    . GLU A 1 324 ? 179.258 183.021 145.785 1.00 16.47  ? 324 GLU A CB    1 
ATOM   2478  C  CG    . GLU A 1 324 ? 179.354 181.505 145.752 1.00 14.58  ? 324 GLU A CG    1 
ATOM   2479  C  CD    . GLU A 1 324 ? 180.548 181.012 144.958 1.00 26.23  ? 324 GLU A CD    1 
ATOM   2480  O  OE1   . GLU A 1 324 ? 180.506 181.081 143.712 1.00 23.51  ? 324 GLU A OE1   1 
ATOM   2481  O  OE2   . GLU A 1 324 ? 181.529 180.555 145.581 1.00 26.51  ? 324 GLU A OE2   1 
ATOM   2482  N  N     . SER A 1 325 ? 180.965 185.778 145.370 1.00 15.29  ? 325 SER A N     1 
ATOM   2483  C  CA    . SER A 1 325 ? 180.941 187.223 145.170 1.00 17.28  ? 325 SER A CA    1 
ATOM   2484  C  C     . SER A 1 325 ? 179.564 187.706 144.731 1.00 17.54  ? 325 SER A C     1 
ATOM   2485  O  O     . SER A 1 325 ? 179.125 188.791 145.130 1.00 25.20  ? 325 SER A O     1 
ATOM   2486  C  CB    . SER A 1 325 ? 182.001 187.630 144.148 1.00 11.79  ? 325 SER A CB    1 
ATOM   2487  O  OG    . SER A 1 325 ? 183.229 187.936 144.783 1.00 34.32  ? 325 SER A OG    1 
ATOM   2488  N  N     . ARG A 1 326 ? 178.868 186.920 143.906 1.00 19.93  ? 326 ARG A N     1 
ATOM   2489  C  CA    . ARG A 1 326 ? 177.577 187.341 143.378 1.00 15.76  ? 326 ARG A CA    1 
ATOM   2490  C  C     . ARG A 1 326 ? 176.475 187.351 144.429 1.00 6.63   ? 326 ARG A C     1 
ATOM   2491  O  O     . ARG A 1 326 ? 175.407 187.915 144.171 1.00 23.13  ? 326 ARG A O     1 
ATOM   2492  C  CB    . ARG A 1 326 ? 177.168 186.443 142.208 1.00 13.57  ? 326 ARG A CB    1 
ATOM   2493  C  CG    . ARG A 1 326 ? 176.785 185.025 142.598 1.00 6.22   ? 326 ARG A CG    1 
ATOM   2494  C  CD    . ARG A 1 326 ? 176.708 184.132 141.369 1.00 9.77   ? 326 ARG A CD    1 
ATOM   2495  N  NE    . ARG A 1 326 ? 176.413 182.744 141.704 1.00 18.85  ? 326 ARG A NE    1 
ATOM   2496  C  CZ    . ARG A 1 326 ? 177.320 181.856 142.090 1.00 17.98  ? 326 ARG A CZ    1 
ATOM   2497  N  NH1   . ARG A 1 326 ? 178.596 182.181 142.215 1.00 11.79  ? 326 ARG A NH1   1 
ATOM   2498  N  NH2   . ARG A 1 326 ? 176.936 180.611 142.356 1.00 13.17  ? 326 ARG A NH2   1 
ATOM   2499  N  N     . PHE A 1 327 ? 176.702 186.752 145.596 1.00 9.28   ? 327 PHE A N     1 
ATOM   2500  C  CA    . PHE A 1 327 ? 175.712 186.734 146.665 1.00 18.92  ? 327 PHE A CA    1 
ATOM   2501  C  C     . PHE A 1 327 ? 176.031 187.733 147.771 1.00 19.64  ? 327 PHE A C     1 
ATOM   2502  O  O     . PHE A 1 327 ? 175.157 188.499 148.184 1.00 29.00  ? 327 PHE A O     1 
ATOM   2503  C  CB    . PHE A 1 327 ? 175.595 185.320 147.248 1.00 6.67   ? 327 PHE A CB    1 
ATOM   2504  C  CG    . PHE A 1 327 ? 175.173 184.285 146.244 1.00 16.33  ? 327 PHE A CG    1 
ATOM   2505  C  CD1   . PHE A 1 327 ? 174.211 184.577 145.291 1.00 15.86  ? 327 PHE A CD1   1 
ATOM   2506  C  CD2   . PHE A 1 327 ? 175.739 183.022 146.251 1.00 14.57  ? 327 PHE A CD2   1 
ATOM   2507  C  CE1   . PHE A 1 327 ? 173.823 183.628 144.364 1.00 14.22  ? 327 PHE A CE1   1 
ATOM   2508  C  CE2   . PHE A 1 327 ? 175.354 182.068 145.328 1.00 16.20  ? 327 PHE A CE2   1 
ATOM   2509  C  CZ    . PHE A 1 327 ? 174.394 182.372 144.383 1.00 11.62  ? 327 PHE A CZ    1 
ATOM   2510  N  N     . GLY A 1 328 ? 177.271 187.751 148.248 1.00 9.67   ? 328 GLY A N     1 
ATOM   2511  C  CA    . GLY A 1 328 ? 177.671 188.653 149.305 1.00 18.74  ? 328 GLY A CA    1 
ATOM   2512  C  C     . GLY A 1 328 ? 177.541 188.036 150.686 1.00 16.34  ? 328 GLY A C     1 
ATOM   2513  O  O     . GLY A 1 328 ? 177.014 186.938 150.876 1.00 31.84  ? 328 GLY A O     1 
ATOM   2514  N  N     . VAL A 1 329 ? 178.042 188.777 151.676 1.00 14.29  ? 329 VAL A N     1 
ATOM   2515  C  CA    . VAL A 1 329 ? 178.053 188.280 153.049 1.00 16.50  ? 329 VAL A CA    1 
ATOM   2516  C  C     . VAL A 1 329 ? 176.640 188.237 153.625 1.00 18.55  ? 329 VAL A C     1 
ATOM   2517  O  O     . VAL A 1 329 ? 176.256 187.263 154.283 1.00 25.94  ? 329 VAL A O     1 
ATOM   2518  C  CB    . VAL A 1 329 ? 179.002 189.132 153.913 1.00 20.00  ? 329 VAL A CB    1 
ATOM   2519  C  CG1   . VAL A 1 329 ? 178.772 190.615 153.666 1.00 27.02  ? 329 VAL A CG1   1 
ATOM   2520  C  CG2   . VAL A 1 329 ? 178.832 188.799 155.385 1.00 14.89  ? 329 VAL A CG2   1 
ATOM   2521  N  N     . LEU A 1 330 ? 175.847 189.286 153.390 1.00 12.35  ? 330 LEU A N     1 
ATOM   2522  C  CA    . LEU A 1 330 ? 174.508 189.349 153.971 1.00 16.95  ? 330 LEU A CA    1 
ATOM   2523  C  C     . LEU A 1 330 ? 173.601 188.257 153.415 1.00 14.97  ? 330 LEU A C     1 
ATOM   2524  O  O     . LEU A 1 330 ? 172.851 187.625 154.167 1.00 16.35  ? 330 LEU A O     1 
ATOM   2525  C  CB    . LEU A 1 330 ? 173.896 190.729 153.729 1.00 12.71  ? 330 LEU A CB    1 
ATOM   2526  C  CG    . LEU A 1 330 ? 174.463 191.879 154.563 1.00 19.77  ? 330 LEU A CG    1 
ATOM   2527  C  CD1   . LEU A 1 330 ? 173.819 193.198 154.166 1.00 19.84  ? 330 LEU A CD1   1 
ATOM   2528  C  CD2   . LEU A 1 330 ? 174.276 191.612 156.048 1.00 13.85  ? 330 LEU A CD2   1 
ATOM   2529  N  N     . VAL A 1 331 ? 173.650 188.026 152.102 1.00 19.57  ? 331 VAL A N     1 
ATOM   2530  C  CA    . VAL A 1 331 ? 172.813 186.994 151.498 1.00 16.47  ? 331 VAL A CA    1 
ATOM   2531  C  C     . VAL A 1 331 ? 173.274 185.609 151.934 1.00 12.65  ? 331 VAL A C     1 
ATOM   2532  O  O     . VAL A 1 331 ? 172.454 184.716 152.180 1.00 12.75  ? 331 VAL A O     1 
ATOM   2533  C  CB    . VAL A 1 331 ? 172.808 187.144 149.966 1.00 12.41  ? 331 VAL A CB    1 
ATOM   2534  C  CG1   . VAL A 1 331 ? 172.050 186.000 149.316 1.00 9.83   ? 331 VAL A CG1   1 
ATOM   2535  C  CG2   . VAL A 1 331 ? 172.197 188.480 149.571 1.00 9.59   ? 331 VAL A CG2   1 
ATOM   2536  N  N     . SER A 1 332 ? 174.590 185.408 152.043 1.00 14.66  ? 332 SER A N     1 
ATOM   2537  C  CA    . SER A 1 332 ? 175.107 184.129 152.519 1.00 12.12  ? 332 SER A CA    1 
ATOM   2538  C  C     . SER A 1 332 ? 174.667 183.856 153.951 1.00 17.08  ? 332 SER A C     1 
ATOM   2539  O  O     . SER A 1 332 ? 174.354 182.713 154.305 1.00 19.53  ? 332 SER A O     1 
ATOM   2540  C  CB    . SER A 1 332 ? 176.632 184.107 152.414 1.00 8.00   ? 332 SER A CB    1 
ATOM   2541  O  OG    . SER A 1 332 ? 177.052 184.115 151.062 1.00 29.93  ? 332 SER A OG    1 
ATOM   2542  N  N     . SER A 1 333 ? 174.646 184.892 154.792 1.00 8.62   ? 333 SER A N     1 
ATOM   2543  C  CA    . SER A 1 333 ? 174.191 184.722 156.169 1.00 10.04  ? 333 SER A CA    1 
ATOM   2544  C  C     . SER A 1 333 ? 172.720 184.327 156.222 1.00 15.53  ? 333 SER A C     1 
ATOM   2545  O  O     . SER A 1 333 ? 172.333 183.452 157.005 1.00 16.17  ? 333 SER A O     1 
ATOM   2546  C  CB    . SER A 1 333 ? 174.431 186.007 156.961 1.00 6.77   ? 333 SER A CB    1 
ATOM   2547  O  OG    . SER A 1 333 ? 175.815 186.265 157.111 1.00 21.38  ? 333 SER A OG    1 
ATOM   2548  N  N     . LEU A 1 334 ? 171.884 184.968 155.400 1.00 16.03  ? 334 LEU A N     1 
ATOM   2549  C  CA    . LEU A 1 334 ? 170.463 184.634 155.383 1.00 11.28  ? 334 LEU A CA    1 
ATOM   2550  C  C     . LEU A 1 334 ? 170.236 183.208 154.898 1.00 15.69  ? 334 LEU A C     1 
ATOM   2551  O  O     . LEU A 1 334 ? 169.416 182.475 155.463 1.00 19.92  ? 334 LEU A O     1 
ATOM   2552  C  CB    . LEU A 1 334 ? 169.698 185.626 154.507 1.00 13.10  ? 334 LEU A CB    1 
ATOM   2553  C  CG    . LEU A 1 334 ? 168.249 185.249 154.184 1.00 17.18  ? 334 LEU A CG    1 
ATOM   2554  C  CD1   . LEU A 1 334 ? 167.400 185.237 155.446 1.00 10.26  ? 334 LEU A CD1   1 
ATOM   2555  C  CD2   . LEU A 1 334 ? 167.659 186.190 153.148 1.00 7.21   ? 334 LEU A CD2   1 
ATOM   2556  N  N     . PHE A 1 335 ? 170.956 182.796 153.851 1.00 12.89  ? 335 PHE A N     1 
ATOM   2557  C  CA    . PHE A 1 335 ? 170.791 181.444 153.325 1.00 8.97   ? 335 PHE A CA    1 
ATOM   2558  C  C     . PHE A 1 335 ? 171.195 180.397 154.355 1.00 6.79   ? 335 PHE A C     1 
ATOM   2559  O  O     . PHE A 1 335 ? 170.552 179.348 154.467 1.00 18.90  ? 335 PHE A O     1 
ATOM   2560  C  CB    . PHE A 1 335 ? 171.603 181.277 152.041 1.00 5.41   ? 335 PHE A CB    1 
ATOM   2561  C  CG    . PHE A 1 335 ? 171.139 180.140 151.172 1.00 3.11   ? 335 PHE A CG    1 
ATOM   2562  C  CD1   . PHE A 1 335 ? 171.496 178.833 151.464 1.00 7.51   ? 335 PHE A CD1   1 
ATOM   2563  C  CD2   . PHE A 1 335 ? 170.349 180.379 150.060 1.00 8.43   ? 335 PHE A CD2   1 
ATOM   2564  C  CE1   . PHE A 1 335 ? 171.070 177.788 150.666 1.00 10.74  ? 335 PHE A CE1   1 
ATOM   2565  C  CE2   . PHE A 1 335 ? 169.921 179.338 149.259 1.00 16.33  ? 335 PHE A CE2   1 
ATOM   2566  C  CZ    . PHE A 1 335 ? 170.281 178.041 149.562 1.00 11.40  ? 335 PHE A CZ    1 
ATOM   2567  N  N     . ALA A 1 336 ? 172.264 180.662 155.110 1.00 12.11  ? 336 ALA A N     1 
ATOM   2568  C  CA    . ALA A 1 336 ? 172.717 179.705 156.115 1.00 15.58  ? 336 ALA A CA    1 
ATOM   2569  C  C     . ALA A 1 336 ? 171.649 179.471 157.176 1.00 12.59  ? 336 ALA A C     1 
ATOM   2570  O  O     . ALA A 1 336 ? 171.414 178.329 157.588 1.00 16.14  ? 336 ALA A O     1 
ATOM   2571  C  CB    . ALA A 1 336 ? 174.015 180.192 156.758 1.00 3.94   ? 336 ALA A CB    1 
ATOM   2572  N  N     . VAL A 1 337 ? 170.994 180.540 157.633 1.00 4.38   ? 337 VAL A N     1 
ATOM   2573  C  CA    . VAL A 1 337 ? 169.929 180.387 158.619 1.00 12.85  ? 337 VAL A CA    1 
ATOM   2574  C  C     . VAL A 1 337 ? 168.721 179.694 158.001 1.00 10.46  ? 337 VAL A C     1 
ATOM   2575  O  O     . VAL A 1 337 ? 168.124 178.800 158.611 1.00 5.91   ? 337 VAL A O     1 
ATOM   2576  C  CB    . VAL A 1 337 ? 169.551 181.753 159.218 1.00 16.32  ? 337 VAL A CB    1 
ATOM   2577  C  CG1   . VAL A 1 337 ? 168.411 181.597 160.211 1.00 11.38  ? 337 VAL A CG1   1 
ATOM   2578  C  CG2   . VAL A 1 337 ? 170.757 182.389 159.884 1.00 12.42  ? 337 VAL A CG2   1 
ATOM   2579  N  N     . VAL A 1 338 ? 168.345 180.090 156.782 1.00 15.70  ? 338 VAL A N     1 
ATOM   2580  C  CA    . VAL A 1 338 ? 167.176 179.504 156.129 1.00 9.04   ? 338 VAL A CA    1 
ATOM   2581  C  C     . VAL A 1 338 ? 167.372 178.005 155.937 1.00 16.32  ? 338 VAL A C     1 
ATOM   2582  O  O     . VAL A 1 338 ? 166.475 177.201 156.219 1.00 16.10  ? 338 VAL A O     1 
ATOM   2583  C  CB    . VAL A 1 338 ? 166.900 180.211 154.788 1.00 16.10  ? 338 VAL A CB    1 
ATOM   2584  C  CG1   . VAL A 1 338 ? 165.938 179.394 153.939 1.00 11.97  ? 338 VAL A CG1   1 
ATOM   2585  C  CG2   . VAL A 1 338 ? 166.351 181.607 155.022 1.00 21.37  ? 338 VAL A CG2   1 
ATOM   2586  N  N     . THR A 1 339 ? 168.555 177.608 155.469 1.00 18.48  ? 339 THR A N     1 
ATOM   2587  C  CA    . THR A 1 339 ? 168.829 176.204 155.194 1.00 13.89  ? 339 THR A CA    1 
ATOM   2588  C  C     . THR A 1 339 ? 169.046 175.377 156.455 1.00 5.79   ? 339 THR A C     1 
ATOM   2589  O  O     . THR A 1 339 ? 169.017 174.145 156.374 1.00 16.09  ? 339 THR A O     1 
ATOM   2590  C  CB    . THR A 1 339 ? 170.050 176.082 154.280 1.00 10.58  ? 339 THR A CB    1 
ATOM   2591  O  OG1   . THR A 1 339 ? 169.987 174.848 153.554 1.00 25.31  ? 339 THR A OG1   1 
ATOM   2592  C  CG2   . THR A 1 339 ? 171.339 176.129 155.090 1.00 6.84   ? 339 THR A CG2   1 
ATOM   2593  N  N     . THR A 1 340 ? 169.262 176.012 157.607 1.00 16.11  ? 340 THR A N     1 
ATOM   2594  C  CA    . THR A 1 340 ? 169.451 175.291 158.860 1.00 14.63  ? 340 THR A CA    1 
ATOM   2595  C  C     . THR A 1 340 ? 168.276 175.411 159.815 1.00 14.02  ? 340 THR A C     1 
ATOM   2596  O  O     . THR A 1 340 ? 168.037 174.484 160.590 1.00 19.98  ? 340 THR A O     1 
ATOM   2597  C  CB    . THR A 1 340 ? 170.722 175.770 159.571 1.00 3.69   ? 340 THR A CB    1 
ATOM   2598  O  OG1   . THR A 1 340 ? 170.775 177.202 159.555 1.00 22.11  ? 340 THR A OG1   1 
ATOM   2599  C  CG2   . THR A 1 340 ? 171.954 175.209 158.877 1.00 20.10  ? 340 THR A CG2   1 
ATOM   2600  N  N     . ALA A 1 341 ? 167.546 176.529 159.792 1.00 13.09  ? 341 ALA A N     1 
ATOM   2601  C  CA    . ALA A 1 341 ? 166.255 176.561 160.469 1.00 18.77  ? 341 ALA A CA    1 
ATOM   2602  C  C     . ALA A 1 341 ? 165.310 175.547 159.844 1.00 21.78  ? 341 ALA A C     1 
ATOM   2603  O  O     . ALA A 1 341 ? 164.599 174.824 160.551 1.00 18.86  ? 341 ALA A O     1 
ATOM   2604  C  CB    . ALA A 1 341 ? 165.657 177.966 160.412 1.00 20.99  ? 341 ALA A CB    1 
ATOM   2605  N  N     . ALA A 1 342 ? 165.300 175.474 158.517 1.00 23.89  ? 342 ALA A N     1 
ATOM   2606  C  CA    . ALA A 1 342 ? 164.646 174.392 157.807 1.00 14.16  ? 342 ALA A CA    1 
ATOM   2607  C  C     . ALA A 1 342 ? 165.573 173.182 157.732 1.00 16.05  ? 342 ALA A C     1 
ATOM   2608  O  O     . ALA A 1 342 ? 166.749 173.239 158.099 1.00 26.58  ? 342 ALA A O     1 
ATOM   2609  C  CB    . ALA A 1 342 ? 164.238 174.840 156.405 1.00 12.42  ? 342 ALA A CB    1 
ATOM   2610  N  N     . SER A 1 343 ? 165.029 172.069 157.242 1.00 14.06  ? 343 SER A N     1 
ATOM   2611  C  CA    . SER A 1 343 ? 165.784 170.834 157.081 1.00 16.43  ? 343 SER A CA    1 
ATOM   2612  C  C     . SER A 1 343 ? 166.288 170.647 155.653 1.00 5.23   ? 343 SER A C     1 
ATOM   2613  O  O     . SER A 1 343 ? 166.399 169.511 155.181 1.00 28.06  ? 343 SER A O     1 
ATOM   2614  C  CB    . SER A 1 343 ? 164.936 169.636 157.506 1.00 15.16  ? 343 SER A CB    1 
ATOM   2615  O  OG    . SER A 1 343 ? 165.183 169.288 158.855 1.00 34.50  ? 343 SER A OG    1 
ATOM   2616  N  N     . CYS A 1 344 ? 166.595 171.741 154.955 1.00 8.26   ? 344 CYS A N     1 
ATOM   2617  C  CA    . CYS A 1 344 ? 167.016 171.637 153.561 1.00 14.63  ? 344 CYS A CA    1 
ATOM   2618  C  C     . CYS A 1 344 ? 168.447 171.124 153.453 1.00 10.94  ? 344 CYS A C     1 
ATOM   2619  O  O     . CYS A 1 344 ? 168.697 170.058 152.882 1.00 22.03  ? 344 CYS A O     1 
ATOM   2620  C  CB    . CYS A 1 344 ? 166.873 172.993 152.866 1.00 13.05  ? 344 CYS A CB    1 
ATOM   2621  S  SG    . CYS A 1 344 ? 167.386 172.988 151.134 1.00 21.42  ? 344 CYS A SG    1 
ATOM   2622  N  N     . GLY A 1 345 ? 169.405 171.872 154.000 1.00 14.64  ? 345 GLY A N     1 
ATOM   2623  C  CA    . GLY A 1 345 ? 170.795 171.473 153.983 1.00 15.13  ? 345 GLY A CA    1 
ATOM   2624  C  C     . GLY A 1 345 ? 171.606 171.971 152.804 1.00 12.61  ? 345 GLY A C     1 
ATOM   2625  O  O     . GLY A 1 345 ? 172.829 171.779 152.794 1.00 30.02  ? 345 GLY A O     1 
ATOM   2626  N  N     . ALA A 1 346 ? 170.977 172.592 151.811 1.00 10.97  ? 346 ALA A N     1 
ATOM   2627  C  CA    . ALA A 1 346 ? 171.724 173.193 150.716 1.00 14.25  ? 346 ALA A CA    1 
ATOM   2628  C  C     . ALA A 1 346 ? 172.502 174.407 151.211 1.00 14.22  ? 346 ALA A C     1 
ATOM   2629  O  O     . ALA A 1 346 ? 172.050 175.145 152.087 1.00 26.35  ? 346 ALA A O     1 
ATOM   2630  C  CB    . ALA A 1 346 ? 170.783 173.597 149.583 1.00 1.00   ? 346 ALA A CB    1 
ATOM   2631  N  N     . VAL A 1 347 ? 173.688 174.613 150.644 1.00 11.84  ? 347 VAL A N     1 
ATOM   2632  C  CA    . VAL A 1 347 ? 174.578 175.683 151.078 1.00 17.02  ? 347 VAL A CA    1 
ATOM   2633  C  C     . VAL A 1 347 ? 175.028 176.486 149.866 1.00 14.17  ? 347 VAL A C     1 
ATOM   2634  O  O     . VAL A 1 347 ? 175.410 175.913 148.840 1.00 27.41  ? 347 VAL A O     1 
ATOM   2635  C  CB    . VAL A 1 347 ? 175.797 175.140 151.849 1.00 7.16   ? 347 VAL A CB    1 
ATOM   2636  C  CG1   . VAL A 1 347 ? 175.394 174.726 153.256 1.00 4.41   ? 347 VAL A CG1   1 
ATOM   2637  C  CG2   . VAL A 1 347 ? 176.433 173.973 151.104 1.00 14.68  ? 347 VAL A CG2   1 
ATOM   2638  N  N     . ILE A 1 348 ? 174.971 177.816 149.984 1.00 18.65  ? 348 ILE A N     1 
ATOM   2639  C  CA    . ILE A 1 348 ? 175.625 178.708 149.035 1.00 16.74  ? 348 ILE A CA    1 
ATOM   2640  C  C     . ILE A 1 348 ? 176.960 179.212 149.555 1.00 11.26  ? 348 ILE A C     1 
ATOM   2641  O  O     . ILE A 1 348 ? 177.669 179.930 148.837 1.00 25.70  ? 348 ILE A O     1 
ATOM   2642  C  CB    . ILE A 1 348 ? 174.718 179.900 148.665 1.00 10.38  ? 348 ILE A CB    1 
ATOM   2643  C  CG1   . ILE A 1 348 ? 174.594 180.868 149.844 1.00 16.17  ? 348 ILE A CG1   1 
ATOM   2644  C  CG2   . ILE A 1 348 ? 173.352 179.414 148.222 1.00 6.96   ? 348 ILE A CG2   1 
ATOM   2645  C  CD1   . ILE A 1 348 ? 174.033 182.221 149.461 1.00 6.84   ? 348 ILE A CD1   1 
ATOM   2646  N  N     . ALA A 1 349 ? 177.321 178.859 150.786 1.00 14.06  ? 349 ALA A N     1 
ATOM   2647  C  CA    . ALA A 1 349 ? 178.589 179.242 151.383 1.00 18.75  ? 349 ALA A CA    1 
ATOM   2648  C  C     . ALA A 1 349 ? 179.071 178.105 152.270 1.00 19.71  ? 349 ALA A C     1 
ATOM   2649  O  O     . ALA A 1 349 ? 178.285 177.271 152.726 1.00 17.46  ? 349 ALA A O     1 
ATOM   2650  C  CB    . ALA A 1 349 ? 178.468 180.541 152.192 1.00 7.04   ? 349 ALA A CB    1 
ATOM   2651  N  N     . MET A 1 350 ? 180.378 178.077 152.512 1.00 22.13  ? 350 MET A N     1 
ATOM   2652  C  CA    . MET A 1 350 ? 180.983 177.027 153.324 1.00 12.70  ? 350 MET A CA    1 
ATOM   2653  C  C     . MET A 1 350 ? 180.787 177.365 154.796 1.00 13.53  ? 350 MET A C     1 
ATOM   2654  O  O     . MET A 1 350 ? 181.386 178.316 155.309 1.00 20.58  ? 350 MET A O     1 
ATOM   2655  C  CB    . MET A 1 350 ? 182.461 176.871 152.981 1.00 15.03  ? 350 MET A CB    1 
ATOM   2656  C  CG    . MET A 1 350 ? 182.775 176.483 151.528 1.00 20.33  ? 350 MET A CG    1 
ATOM   2657  S  SD    . MET A 1 350 ? 182.311 174.813 150.995 1.00 37.28  ? 350 MET A SD    1 
ATOM   2658  C  CE    . MET A 1 350 ? 180.561 174.963 150.630 1.00 13.70  ? 350 MET A CE    1 
ATOM   2659  N  N     . HIS A 1 351 ? 179.943 176.586 155.478 1.00 6.28   ? 351 HIS A N     1 
ATOM   2660  C  CA    . HIS A 1 351 ? 179.685 176.820 156.894 1.00 17.44  ? 351 HIS A CA    1 
ATOM   2661  C  C     . HIS A 1 351 ? 180.920 176.586 157.753 1.00 18.69  ? 351 HIS A C     1 
ATOM   2662  O  O     . HIS A 1 351 ? 181.013 177.150 158.848 1.00 20.13  ? 351 HIS A O     1 
ATOM   2663  C  CB    . HIS A 1 351 ? 178.536 175.929 157.372 1.00 17.14  ? 351 HIS A CB    1 
ATOM   2664  C  CG    . HIS A 1 351 ? 177.200 176.314 156.815 1.00 22.05  ? 351 HIS A CG    1 
ATOM   2665  N  ND1   . HIS A 1 351 ? 176.019 175.770 157.271 1.00 23.86  ? 351 HIS A ND1   1 
ATOM   2666  C  CD2   . HIS A 1 351 ? 176.859 177.186 155.837 1.00 16.47  ? 351 HIS A CD2   1 
ATOM   2667  C  CE1   . HIS A 1 351 ? 175.008 176.292 156.599 1.00 12.35  ? 351 HIS A CE1   1 
ATOM   2668  N  NE2   . HIS A 1 351 ? 175.491 177.153 155.722 1.00 12.40  ? 351 HIS A NE2   1 
ATOM   2669  N  N     . ASP A 1 352 ? 181.866 175.768 157.283 1.00 19.12  ? 352 ASP A N     1 
ATOM   2670  C  CA    . ASP A 1 352 ? 183.100 175.550 158.030 1.00 9.34   ? 352 ASP A CA    1 
ATOM   2671  C  C     . ASP A 1 352 ? 183.935 176.821 158.122 1.00 17.87  ? 352 ASP A C     1 
ATOM   2672  O  O     . ASP A 1 352 ? 184.645 177.023 159.114 1.00 23.18  ? 352 ASP A O     1 
ATOM   2673  C  CB    . ASP A 1 352 ? 183.912 174.428 157.382 1.00 18.71  ? 352 ASP A CB    1 
ATOM   2674  C  CG    . ASP A 1 352 ? 184.592 173.537 158.402 1.00 13.28  ? 352 ASP A CG    1 
ATOM   2675  O  OD1   . ASP A 1 352 ? 184.659 173.925 159.586 1.00 24.99  ? 352 ASP A OD1   1 
ATOM   2676  O  OD2   . ASP A 1 352 ? 185.061 172.446 158.018 1.00 25.37  ? 352 ASP A OD2   1 
ATOM   2677  N  N     . SER A 1 353 ? 183.866 177.683 157.111 1.00 23.66  ? 353 SER A N     1 
ATOM   2678  C  CA    . SER A 1 353 ? 184.620 178.930 157.092 1.00 14.45  ? 353 SER A CA    1 
ATOM   2679  C  C     . SER A 1 353 ? 183.893 180.076 157.783 1.00 9.62   ? 353 SER A C     1 
ATOM   2680  O  O     . SER A 1 353 ? 184.437 181.183 157.851 1.00 23.41  ? 353 SER A O     1 
ATOM   2681  C  CB    . SER A 1 353 ? 184.949 179.326 155.649 1.00 13.83  ? 353 SER A CB    1 
ATOM   2682  O  OG    . SER A 1 353 ? 185.905 178.445 155.086 1.00 21.50  ? 353 SER A OG    1 
ATOM   2683  N  N     . PHE A 1 354 ? 182.686 179.843 158.292 1.00 11.92  ? 354 PHE A N     1 
ATOM   2684  C  CA    . PHE A 1 354 ? 181.966 180.872 159.023 1.00 19.96  ? 354 PHE A CA    1 
ATOM   2685  C  C     . PHE A 1 354 ? 182.679 181.193 160.334 1.00 13.21  ? 354 PHE A C     1 
ATOM   2686  O  O     . PHE A 1 354 ? 183.484 180.410 160.845 1.00 28.39  ? 354 PHE A O     1 
ATOM   2687  C  CB    . PHE A 1 354 ? 180.532 180.424 159.312 1.00 15.54  ? 354 PHE A CB    1 
ATOM   2688  C  CG    . PHE A 1 354 ? 179.539 180.840 158.265 1.00 16.37  ? 354 PHE A CG    1 
ATOM   2689  C  CD1   . PHE A 1 354 ? 179.743 180.527 156.932 1.00 18.37  ? 354 PHE A CD1   1 
ATOM   2690  C  CD2   . PHE A 1 354 ? 178.396 181.539 158.616 1.00 22.27  ? 354 PHE A CD2   1 
ATOM   2691  C  CE1   . PHE A 1 354 ? 178.829 180.906 155.968 1.00 19.72  ? 354 PHE A CE1   1 
ATOM   2692  C  CE2   . PHE A 1 354 ? 177.478 181.921 157.657 1.00 23.06  ? 354 PHE A CE2   1 
ATOM   2693  C  CZ    . PHE A 1 354 ? 177.695 181.604 156.331 1.00 22.03  ? 354 PHE A CZ    1 
ATOM   2694  N  N     . THR A 1 355 ? 182.372 182.367 160.880 1.00 19.60  ? 355 THR A N     1 
ATOM   2695  C  CA    . THR A 1 355 ? 182.911 182.740 162.176 1.00 18.17  ? 355 THR A CA    1 
ATOM   2696  C  C     . THR A 1 355 ? 182.340 181.829 163.263 1.00 9.46   ? 355 THR A C     1 
ATOM   2697  O  O     . THR A 1 355 ? 181.372 181.092 163.051 1.00 19.78  ? 355 THR A O     1 
ATOM   2698  C  CB    . THR A 1 355 ? 182.605 184.204 162.491 1.00 18.45  ? 355 THR A CB    1 
ATOM   2699  O  OG1   . THR A 1 355 ? 181.194 184.375 162.667 1.00 23.76  ? 355 THR A OG1   1 
ATOM   2700  C  CG2   . THR A 1 355 ? 183.085 185.103 161.361 1.00 18.78  ? 355 THR A CG2   1 
ATOM   2701  N  N     . ALA A 1 356 ? 182.964 181.881 164.442 1.00 16.25  ? 356 ALA A N     1 
ATOM   2702  C  CA    . ALA A 1 356 ? 182.567 180.993 165.531 1.00 20.77  ? 356 ALA A CA    1 
ATOM   2703  C  C     . ALA A 1 356 ? 181.106 181.201 165.909 1.00 21.88  ? 356 ALA A C     1 
ATOM   2704  O  O     . ALA A 1 356 ? 180.336 180.240 166.012 1.00 28.67  ? 356 ALA A O     1 
ATOM   2705  C  CB    . ALA A 1 356 ? 183.476 181.211 166.740 1.00 18.69  ? 356 ALA A CB    1 
ATOM   2706  N  N     . LEU A 1 357 ? 180.701 182.456 166.113 1.00 27.64  ? 357 LEU A N     1 
ATOM   2707  C  CA    . LEU A 1 357 ? 179.298 182.742 166.384 1.00 24.68  ? 357 LEU A CA    1 
ATOM   2708  C  C     . LEU A 1 357 ? 178.447 182.644 165.126 1.00 22.59  ? 357 LEU A C     1 
ATOM   2709  O  O     . LEU A 1 357 ? 177.268 182.283 165.207 1.00 25.54  ? 357 LEU A O     1 
ATOM   2710  C  CB    . LEU A 1 357 ? 179.151 184.130 167.011 1.00 26.62  ? 357 LEU A CB    1 
ATOM   2711  C  CG    . LEU A 1 357 ? 179.585 184.291 168.470 1.00 30.89  ? 357 LEU A CG    1 
ATOM   2712  C  CD1   . LEU A 1 357 ? 178.763 185.372 169.156 1.00 30.57  ? 357 LEU A CD1   1 
ATOM   2713  C  CD2   . LEU A 1 357 ? 179.479 182.975 169.230 1.00 25.16  ? 357 LEU A CD2   1 
ATOM   2714  N  N     . GLY A 1 358 ? 179.023 182.959 163.963 1.00 14.40  ? 358 GLY A N     1 
ATOM   2715  C  CA    . GLY A 1 358 ? 178.273 182.869 162.723 1.00 19.00  ? 358 GLY A CA    1 
ATOM   2716  C  C     . GLY A 1 358 ? 177.853 181.454 162.381 1.00 19.41  ? 358 GLY A C     1 
ATOM   2717  O  O     . GLY A 1 358 ? 176.789 181.245 161.795 1.00 24.70  ? 358 GLY A O     1 
ATOM   2718  N  N     . GLY A 1 359 ? 178.680 180.469 162.728 1.00 18.22  ? 359 GLY A N     1 
ATOM   2719  C  CA    . GLY A 1 359 ? 178.348 179.078 162.497 1.00 17.96  ? 359 GLY A CA    1 
ATOM   2720  C  C     . GLY A 1 359 ? 177.666 178.374 163.645 1.00 25.63  ? 359 GLY A C     1 
ATOM   2721  O  O     . GLY A 1 359 ? 177.128 177.280 163.456 1.00 24.17  ? 359 GLY A O     1 
ATOM   2722  N  N     . MET A 1 360 ? 177.673 178.974 164.837 1.00 23.54  ? 360 MET A N     1 
ATOM   2723  C  CA    . MET A 1 360 ? 177.027 178.348 165.986 1.00 17.49  ? 360 MET A CA    1 
ATOM   2724  C  C     . MET A 1 360 ? 175.509 178.369 165.850 1.00 16.22  ? 360 MET A C     1 
ATOM   2725  O  O     . MET A 1 360 ? 174.840 177.378 166.165 1.00 18.29  ? 360 MET A O     1 
ATOM   2726  C  CB    . MET A 1 360 ? 177.460 179.048 167.274 1.00 13.67  ? 360 MET A CB    1 
ATOM   2727  C  CG    . MET A 1 360 ? 176.700 178.601 168.511 1.00 16.74  ? 360 MET A CG    1 
ATOM   2728  S  SD    . MET A 1 360 ? 177.370 179.305 170.029 1.00 45.70  ? 360 MET A SD    1 
ATOM   2729  C  CE    . MET A 1 360 ? 176.358 180.773 170.190 1.00 20.34  ? 360 MET A CE    1 
ATOM   2730  N  N     . VAL A 1 361 ? 174.950 179.491 165.391 1.00 16.58  ? 361 VAL A N     1 
ATOM   2731  C  CA    . VAL A 1 361 ? 173.496 179.593 165.253 1.00 21.72  ? 361 VAL A CA    1 
ATOM   2732  C  C     . VAL A 1 361 ? 172.937 178.566 164.273 1.00 15.68  ? 361 VAL A C     1 
ATOM   2733  O  O     . VAL A 1 361 ? 171.948 177.896 164.616 1.00 17.02  ? 361 VAL A O     1 
ATOM   2734  C  CB    . VAL A 1 361 ? 173.100 181.037 164.894 1.00 16.16  ? 361 VAL A CB    1 
ATOM   2735  C  CG1   . VAL A 1 361 ? 171.607 181.131 164.618 1.00 15.66  ? 361 VAL A CG1   1 
ATOM   2736  C  CG2   . VAL A 1 361 ? 173.506 181.991 166.007 1.00 18.17  ? 361 VAL A CG2   1 
ATOM   2737  N  N     . PRO A 1 362 ? 173.488 178.391 163.063 1.00 23.05  ? 362 PRO A N     1 
ATOM   2738  C  CA    . PRO A 1 362 ? 172.979 177.311 162.199 1.00 13.39  ? 362 PRO A CA    1 
ATOM   2739  C  C     . PRO A 1 362 ? 173.098 175.933 162.826 1.00 17.61  ? 362 PRO A C     1 
ATOM   2740  O  O     . PRO A 1 362 ? 172.210 175.093 162.639 1.00 22.85  ? 362 PRO A O     1 
ATOM   2741  C  CB    . PRO A 1 362 ? 173.843 177.440 160.936 1.00 18.52  ? 362 PRO A CB    1 
ATOM   2742  C  CG    . PRO A 1 362 ? 174.282 178.852 160.927 1.00 17.65  ? 362 PRO A CG    1 
ATOM   2743  C  CD    . PRO A 1 362 ? 174.503 179.199 162.363 1.00 13.03  ? 362 PRO A CD    1 
ATOM   2744  N  N     . MET A 1 363 ? 174.179 175.678 163.568 1.00 17.48  ? 363 MET A N     1 
ATOM   2745  C  CA    . MET A 1 363 ? 174.324 174.394 164.246 1.00 17.80  ? 363 MET A CA    1 
ATOM   2746  C  C     . MET A 1 363 ? 173.260 174.215 165.322 1.00 19.91  ? 363 MET A C     1 
ATOM   2747  O  O     . MET A 1 363 ? 172.699 173.124 165.474 1.00 24.89  ? 363 MET A O     1 
ATOM   2748  C  CB    . MET A 1 363 ? 175.725 174.274 164.845 1.00 20.46  ? 363 MET A CB    1 
ATOM   2749  C  CG    . MET A 1 363 ? 175.993 172.947 165.539 1.00 25.51  ? 363 MET A CG    1 
ATOM   2750  S  SD    . MET A 1 363 ? 177.539 172.935 166.468 1.00 38.99  ? 363 MET A SD    1 
ATOM   2751  C  CE    . MET A 1 363 ? 178.595 173.907 165.397 1.00 27.01  ? 363 MET A CE    1 
ATOM   2752  N  N     . TRP A 1 364 ? 172.969 175.276 166.078 1.00 17.63  ? 364 TRP A N     1 
ATOM   2753  C  CA    . TRP A 1 364 ? 171.954 175.185 167.123 1.00 18.73  ? 364 TRP A CA    1 
ATOM   2754  C  C     . TRP A 1 364 ? 170.552 175.073 166.538 1.00 21.30  ? 364 TRP A C     1 
ATOM   2755  O  O     . TRP A 1 364 ? 169.677 174.450 167.150 1.00 10.73  ? 364 TRP A O     1 
ATOM   2756  C  CB    . TRP A 1 364 ? 172.050 176.394 168.053 1.00 15.64  ? 364 TRP A CB    1 
ATOM   2757  C  CG    . TRP A 1 364 ? 171.111 176.332 169.217 1.00 28.04  ? 364 TRP A CG    1 
ATOM   2758  C  CD1   . TRP A 1 364 ? 171.126 175.424 170.235 1.00 18.82  ? 364 TRP A CD1   1 
ATOM   2759  C  CD2   . TRP A 1 364 ? 170.016 177.217 169.484 1.00 30.53  ? 364 TRP A CD2   1 
ATOM   2760  N  NE1   . TRP A 1 364 ? 170.110 175.688 171.120 1.00 28.27  ? 364 TRP A NE1   1 
ATOM   2761  C  CE2   . TRP A 1 364 ? 169.413 176.784 170.682 1.00 31.25  ? 364 TRP A CE2   1 
ATOM   2762  C  CE3   . TRP A 1 364 ? 169.488 178.332 168.827 1.00 26.04  ? 364 TRP A CE3   1 
ATOM   2763  C  CZ2   . TRP A 1 364 ? 168.308 177.427 171.236 1.00 26.36  ? 364 TRP A CZ2   1 
ATOM   2764  C  CZ3   . TRP A 1 364 ? 168.391 178.969 169.379 1.00 28.93  ? 364 TRP A CZ3   1 
ATOM   2765  C  CH2   . TRP A 1 364 ? 167.813 178.514 170.571 1.00 32.39  ? 364 TRP A CH2   1 
ATOM   2766  N  N     . LEU A 1 365 ? 170.317 175.669 165.366 1.00 21.05  ? 365 LEU A N     1 
ATOM   2767  C  CA    . LEU A 1 365 ? 169.009 175.559 164.728 1.00 18.12  ? 365 LEU A CA    1 
ATOM   2768  C  C     . LEU A 1 365 ? 168.688 174.111 164.381 1.00 14.94  ? 365 LEU A C     1 
ATOM   2769  O  O     . LEU A 1 365 ? 167.544 173.667 164.529 1.00 19.95  ? 365 LEU A O     1 
ATOM   2770  C  CB    . LEU A 1 365 ? 168.957 176.437 163.478 1.00 20.75  ? 365 LEU A CB    1 
ATOM   2771  C  CG    . LEU A 1 365 ? 168.670 177.923 163.703 1.00 19.95  ? 365 LEU A CG    1 
ATOM   2772  C  CD1   . LEU A 1 365 ? 168.929 178.714 162.433 1.00 18.51  ? 365 LEU A CD1   1 
ATOM   2773  C  CD2   . LEU A 1 365 ? 167.243 178.130 164.187 1.00 8.31   ? 365 LEU A CD2   1 
ATOM   2774  N  N     . MET A 1 366 ? 169.683 173.364 163.898 1.00 17.04  ? 366 MET A N     1 
ATOM   2775  C  CA    . MET A 1 366 ? 169.487 171.937 163.662 1.00 17.61  ? 366 MET A CA    1 
ATOM   2776  C  C     . MET A 1 366 ? 169.253 171.187 164.968 1.00 20.53  ? 366 MET A C     1 
ATOM   2777  O  O     . MET A 1 366 ? 168.383 170.314 165.042 1.00 16.42  ? 366 MET A O     1 
ATOM   2778  C  CB    . MET A 1 366 ? 170.695 171.357 162.928 1.00 18.25  ? 366 MET A CB    1 
ATOM   2779  C  CG    . MET A 1 366 ? 171.035 172.052 161.622 1.00 13.89  ? 366 MET A CG    1 
ATOM   2780  S  SD    . MET A 1 366 ? 172.247 171.133 160.655 1.00 20.66  ? 366 MET A SD    1 
ATOM   2781  C  CE    . MET A 1 366 ? 173.645 171.130 161.774 1.00 8.37   ? 366 MET A CE    1 
ATOM   2782  N  N     . GLN A 1 367 ? 170.011 171.529 166.014 1.00 21.94  ? 367 GLN A N     1 
ATOM   2783  C  CA    . GLN A 1 367 ? 170.007 170.732 167.238 1.00 18.17  ? 367 GLN A CA    1 
ATOM   2784  C  C     . GLN A 1 367 ? 168.674 170.798 167.973 1.00 22.02  ? 367 GLN A C     1 
ATOM   2785  O  O     . GLN A 1 367 ? 168.326 169.859 168.696 1.00 31.92  ? 367 GLN A O     1 
ATOM   2786  C  CB    . GLN A 1 367 ? 171.141 171.185 168.158 1.00 13.04  ? 367 GLN A CB    1 
ATOM   2787  C  CG    . GLN A 1 367 ? 172.507 170.652 167.761 1.00 16.08  ? 367 GLN A CG    1 
ATOM   2788  C  CD    . GLN A 1 367 ? 173.644 171.429 168.391 1.00 14.82  ? 367 GLN A CD    1 
ATOM   2789  O  OE1   . GLN A 1 367 ? 173.429 172.464 169.021 1.00 24.63  ? 367 GLN A OE1   1 
ATOM   2790  N  NE2   . GLN A 1 367 ? 174.863 170.933 168.224 1.00 15.56  ? 367 GLN A NE2   1 
ATOM   2791  N  N     . ILE A 1 368 ? 167.911 171.885 167.805 1.00 16.31  ? 368 ILE A N     1 
ATOM   2792  C  CA    . ILE A 1 368 ? 166.646 172.025 168.526 1.00 19.86  ? 368 ILE A CA    1 
ATOM   2793  C  C     . ILE A 1 368 ? 165.529 171.186 167.930 1.00 23.99  ? 368 ILE A C     1 
ATOM   2794  O  O     . ILE A 1 368 ? 164.388 171.270 168.402 1.00 28.30  ? 368 ILE A O     1 
ATOM   2795  C  CB    . ILE A 1 368 ? 166.183 173.496 168.587 1.00 16.27  ? 368 ILE A CB    1 
ATOM   2796  C  CG1   . ILE A 1 368 ? 165.881 174.027 167.186 1.00 21.31  ? 368 ILE A CG1   1 
ATOM   2797  C  CG2   . ILE A 1 368 ? 167.225 174.355 169.286 1.00 15.71  ? 368 ILE A CG2   1 
ATOM   2798  C  CD1   . ILE A 1 368 ? 165.144 175.347 167.181 1.00 25.90  ? 368 ILE A CD1   1 
ATOM   2799  N  N     . GLY A 1 369 ? 165.815 170.380 166.912 1.00 22.82  ? 369 GLY A N     1 
ATOM   2800  C  CA    . GLY A 1 369 ? 164.822 169.512 166.319 1.00 25.00  ? 369 GLY A CA    1 
ATOM   2801  C  C     . GLY A 1 369 ? 164.249 169.973 164.999 1.00 14.17  ? 369 GLY A C     1 
ATOM   2802  O  O     . GLY A 1 369 ? 163.295 169.353 164.515 1.00 28.42  ? 369 GLY A O     1 
ATOM   2803  N  N     . GLU A 1 370 ? 164.793 171.037 164.407 1.00 16.38  ? 370 GLU A N     1 
ATOM   2804  C  CA    . GLU A 1 370 ? 164.333 171.565 163.122 1.00 13.03  ? 370 GLU A CA    1 
ATOM   2805  C  C     . GLU A 1 370 ? 162.849 171.937 163.184 1.00 20.21  ? 370 GLU A C     1 
ATOM   2806  O  O     . GLU A 1 370 ? 162.003 171.364 162.496 1.00 35.29  ? 370 GLU A O     1 
ATOM   2807  C  CB    . GLU A 1 370 ? 164.610 170.571 161.988 1.00 19.91  ? 370 GLU A CB    1 
ATOM   2808  C  CG    . GLU A 1 370 ? 166.067 170.158 161.865 1.00 17.33  ? 370 GLU A CG    1 
ATOM   2809  C  CD    . GLU A 1 370 ? 166.874 171.114 161.009 1.00 17.36  ? 370 GLU A CD    1 
ATOM   2810  O  OE1   . GLU A 1 370 ? 166.385 172.230 160.740 1.00 24.99  ? 370 GLU A OE1   1 
ATOM   2811  O  OE2   . GLU A 1 370 ? 167.996 170.749 160.604 1.00 26.46  ? 370 GLU A OE2   1 
ATOM   2812  N  N     . VAL A 1 371 ? 162.548 172.911 164.039 1.00 25.19  ? 371 VAL A N     1 
ATOM   2813  C  CA    . VAL A 1 371 ? 161.180 173.385 164.222 1.00 25.58  ? 371 VAL A CA    1 
ATOM   2814  C  C     . VAL A 1 371 ? 160.980 174.813 163.741 1.00 23.37  ? 371 VAL A C     1 
ATOM   2815  O  O     . VAL A 1 371 ? 159.831 175.285 163.724 1.00 28.48  ? 371 VAL A O     1 
ATOM   2816  C  CB    . VAL A 1 371 ? 160.730 173.258 165.693 1.00 21.44  ? 371 VAL A CB    1 
ATOM   2817  C  CG1   . VAL A 1 371 ? 160.765 171.802 166.132 1.00 24.57  ? 371 VAL A CG1   1 
ATOM   2818  C  CG2   . VAL A 1 371 ? 161.606 174.114 166.592 1.00 19.55  ? 371 VAL A CG2   1 
ATOM   2819  N  N     . VAL A 1 372 ? 162.040 175.511 163.346 1.00 22.17  ? 372 VAL A N     1 
ATOM   2820  C  CA    . VAL A 1 372 ? 161.905 176.874 162.803 1.00 14.00  ? 372 VAL A CA    1 
ATOM   2821  C  C     . VAL A 1 372 ? 161.632 176.700 161.314 1.00 19.92  ? 372 VAL A C     1 
ATOM   2822  O  O     . VAL A 1 372 ? 162.525 176.732 160.464 1.00 25.66  ? 372 VAL A O     1 
ATOM   2823  C  CB    . VAL A 1 372 ? 163.135 177.739 163.092 1.00 26.56  ? 372 VAL A CB    1 
ATOM   2824  C  CG1   . VAL A 1 372 ? 162.855 179.192 162.741 1.00 17.07  ? 372 VAL A CG1   1 
ATOM   2825  C  CG2   . VAL A 1 372 ? 163.539 177.609 164.552 1.00 20.49  ? 372 VAL A CG2   1 
ATOM   2826  N  N     . PHE A 1 373 ? 160.353 176.481 161.000 1.00 25.99  ? 373 PHE A N     1 
ATOM   2827  C  CA    . PHE A 1 373 ? 159.806 176.176 159.680 1.00 16.51  ? 373 PHE A CA    1 
ATOM   2828  C  C     . PHE A 1 373 ? 160.162 174.761 159.237 1.00 24.48  ? 373 PHE A C     1 
ATOM   2829  O  O     . PHE A 1 373 ? 159.536 174.229 158.317 1.00 43.27  ? 373 PHE A O     1 
ATOM   2830  C  CB    . PHE A 1 373 ? 160.286 177.181 158.624 1.00 17.27  ? 373 PHE A CB    1 
ATOM   2831  C  CG    . PHE A 1 373 ? 159.785 178.582 158.833 1.00 22.90  ? 373 PHE A CG    1 
ATOM   2832  C  CD1   . PHE A 1 373 ? 158.594 178.998 158.261 1.00 21.86  ? 373 PHE A CD1   1 
ATOM   2833  C  CD2   . PHE A 1 373 ? 160.512 179.488 159.587 1.00 22.74  ? 373 PHE A CD2   1 
ATOM   2834  C  CE1   . PHE A 1 373 ? 158.133 180.288 158.445 1.00 24.24  ? 373 PHE A CE1   1 
ATOM   2835  C  CE2   . PHE A 1 373 ? 160.056 180.779 159.775 1.00 26.07  ? 373 PHE A CE2   1 
ATOM   2836  C  CZ    . PHE A 1 373 ? 158.865 181.180 159.203 1.00 28.71  ? 373 PHE A CZ    1 
ATOM   2837  N  N     . GLY A 1 374 ? 161.114 174.123 159.919 1.00 14.08  ? 374 GLY A N     1 
ATOM   2838  C  CA    . GLY A 1 374 ? 161.465 172.731 159.685 1.00 16.95  ? 374 GLY A CA    1 
ATOM   2839  C  C     . GLY A 1 374 ? 161.602 172.293 158.239 1.00 15.44  ? 374 GLY A C     1 
ATOM   2840  O  O     . GLY A 1 374 ? 161.818 173.113 157.344 1.00 30.10  ? 374 GLY A O     1 
ATOM   2841  N  N     . GLY A 1 375 ? 161.450 170.993 157.996 1.00 27.63  ? 375 GLY A N     1 
ATOM   2842  C  CA    . GLY A 1 375 ? 161.382 170.460 156.653 1.00 9.50   ? 375 GLY A CA    1 
ATOM   2843  C  C     . GLY A 1 375 ? 159.952 170.386 156.155 1.00 18.34  ? 375 GLY A C     1 
ATOM   2844  O  O     . GLY A 1 375 ? 159.017 170.906 156.767 1.00 32.26  ? 375 GLY A O     1 
ATOM   2845  N  N     . VAL A 1 376 ? 159.783 169.718 155.016 1.00 19.56  ? 376 VAL A N     1 
ATOM   2846  C  CA    . VAL A 1 376 ? 158.450 169.544 154.445 1.00 15.36  ? 376 VAL A CA    1 
ATOM   2847  C  C     . VAL A 1 376 ? 157.678 168.557 155.317 1.00 22.48  ? 376 VAL A C     1 
ATOM   2848  O  O     . VAL A 1 376 ? 157.980 167.360 155.350 1.00 23.97  ? 376 VAL A O     1 
ATOM   2849  C  CB    . VAL A 1 376 ? 158.511 169.088 152.981 1.00 11.02  ? 376 VAL A CB    1 
ATOM   2850  C  CG1   . VAL A 1 376 ? 158.965 170.236 152.100 1.00 16.66  ? 376 VAL A CG1   1 
ATOM   2851  C  CG2   . VAL A 1 376 ? 159.465 167.913 152.810 1.00 18.12  ? 376 VAL A CG2   1 
ATOM   2852  N  N     . GLY A 1 377 ? 156.694 169.066 156.053 1.00 17.50  ? 377 GLY A N     1 
ATOM   2853  C  CA    . GLY A 1 377 ? 155.912 168.236 156.948 1.00 9.81   ? 377 GLY A CA    1 
ATOM   2854  C  C     . GLY A 1 377 ? 156.603 167.954 158.266 1.00 17.70  ? 377 GLY A C     1 
ATOM   2855  O  O     . GLY A 1 377 ? 155.974 168.018 159.326 1.00 23.58  ? 377 GLY A O     1 
ATOM   2856  N  N     . SER A 1 378 ? 157.902 167.644 158.212 1.00 21.64  ? 378 SER A N     1 
ATOM   2857  C  CA    . SER A 1 378 ? 158.633 167.285 159.424 1.00 11.23  ? 378 SER A CA    1 
ATOM   2858  C  C     . SER A 1 378 ? 158.698 168.450 160.403 1.00 18.26  ? 378 SER A C     1 
ATOM   2859  O  O     . SER A 1 378 ? 158.672 168.248 161.622 1.00 25.61  ? 378 SER A O     1 
ATOM   2860  C  CB    . SER A 1 378 ? 160.037 166.796 159.068 1.00 12.29  ? 378 SER A CB    1 
ATOM   2861  O  OG    . SER A 1 378 ? 160.733 167.746 158.282 1.00 28.00  ? 378 SER A OG    1 
ATOM   2862  N  N     . GLY A 1 379 ? 158.790 169.677 159.890 1.00 17.14  ? 379 GLY A N     1 
ATOM   2863  C  CA    . GLY A 1 379 ? 158.809 170.831 160.771 1.00 18.68  ? 379 GLY A CA    1 
ATOM   2864  C  C     . GLY A 1 379 ? 157.498 171.036 161.505 1.00 26.43  ? 379 GLY A C     1 
ATOM   2865  O  O     . GLY A 1 379 ? 157.488 171.438 162.672 1.00 27.32  ? 379 GLY A O     1 
ATOM   2866  N  N     . LEU A 1 380 ? 156.376 170.766 160.836 1.00 20.81  ? 380 LEU A N     1 
ATOM   2867  C  CA    . LEU A 1 380 ? 155.075 171.008 161.452 1.00 21.52  ? 380 LEU A CA    1 
ATOM   2868  C  C     . LEU A 1 380 ? 154.813 170.037 162.599 1.00 17.51  ? 380 LEU A C     1 
ATOM   2869  O  O     . LEU A 1 380 ? 154.414 170.454 163.692 1.00 25.92  ? 380 LEU A O     1 
ATOM   2870  C  CB    . LEU A 1 380 ? 153.968 170.924 160.402 1.00 24.18  ? 380 LEU A CB    1 
ATOM   2871  C  CG    . LEU A 1 380 ? 152.597 171.461 160.828 1.00 27.36  ? 380 LEU A CG    1 
ATOM   2872  C  CD1   . LEU A 1 380 ? 152.738 172.698 161.706 1.00 17.38  ? 380 LEU A CD1   1 
ATOM   2873  C  CD2   . LEU A 1 380 ? 151.733 171.764 159.614 1.00 22.14  ? 380 LEU A CD2   1 
ATOM   2874  N  N     . TYR A 1 381 ? 155.027 168.737 162.376 1.00 10.74  ? 381 TYR A N     1 
ATOM   2875  C  CA    . TYR A 1 381 ? 154.823 167.798 163.473 1.00 23.54  ? 381 TYR A CA    1 
ATOM   2876  C  C     . TYR A 1 381 ? 155.974 167.814 164.469 1.00 21.20  ? 381 TYR A C     1 
ATOM   2877  O  O     . TYR A 1 381 ? 155.791 167.382 165.612 1.00 24.28  ? 381 TYR A O     1 
ATOM   2878  C  CB    . TYR A 1 381 ? 154.568 166.372 162.953 1.00 18.53  ? 381 TYR A CB    1 
ATOM   2879  C  CG    . TYR A 1 381 ? 155.661 165.697 162.142 1.00 19.50  ? 381 TYR A CG    1 
ATOM   2880  C  CD1   . TYR A 1 381 ? 156.888 165.370 162.707 1.00 17.53  ? 381 TYR A CD1   1 
ATOM   2881  C  CD2   . TYR A 1 381 ? 155.433 165.328 160.821 1.00 16.77  ? 381 TYR A CD2   1 
ATOM   2882  C  CE1   . TYR A 1 381 ? 157.870 164.735 161.969 1.00 18.23  ? 381 TYR A CE1   1 
ATOM   2883  C  CE2   . TYR A 1 381 ? 156.407 164.689 160.077 1.00 5.73   ? 381 TYR A CE2   1 
ATOM   2884  C  CZ    . TYR A 1 381 ? 157.623 164.394 160.656 1.00 24.26  ? 381 TYR A CZ    1 
ATOM   2885  O  OH    . TYR A 1 381 ? 158.596 163.761 159.917 1.00 28.31  ? 381 TYR A OH    1 
ATOM   2886  N  N     . GLY A 1 382 ? 157.149 168.300 164.065 1.00 16.01  ? 382 GLY A N     1 
ATOM   2887  C  CA    . GLY A 1 382 ? 158.196 168.561 165.037 1.00 10.37  ? 382 GLY A CA    1 
ATOM   2888  C  C     . GLY A 1 382 ? 157.827 169.690 165.980 1.00 17.47  ? 382 GLY A C     1 
ATOM   2889  O  O     . GLY A 1 382 ? 158.082 169.615 167.185 1.00 21.36  ? 382 GLY A O     1 
ATOM   2890  N  N     . MET A 1 383 ? 157.221 170.752 165.443 1.00 15.08  ? 383 MET A N     1 
ATOM   2891  C  CA    . MET A 1 383 ? 156.723 171.833 166.286 1.00 20.01  ? 383 MET A CA    1 
ATOM   2892  C  C     . MET A 1 383 ? 155.499 171.400 167.084 1.00 21.29  ? 383 MET A C     1 
ATOM   2893  O  O     . MET A 1 383 ? 155.287 171.886 168.201 1.00 23.19  ? 383 MET A O     1 
ATOM   2894  C  CB    . MET A 1 383 ? 156.399 173.059 165.430 1.00 15.03  ? 383 MET A CB    1 
ATOM   2895  C  CG    . MET A 1 383 ? 155.954 174.280 166.220 1.00 20.86  ? 383 MET A CG    1 
ATOM   2896  S  SD    . MET A 1 383 ? 157.184 174.836 167.416 1.00 37.33  ? 383 MET A SD    1 
ATOM   2897  C  CE    . MET A 1 383 ? 158.041 176.090 166.469 1.00 24.48  ? 383 MET A CE    1 
ATOM   2898  N  N     . MET A 1 384 ? 154.688 170.493 166.530 1.00 17.42  ? 384 MET A N     1 
ATOM   2899  C  CA    . MET A 1 384 ? 153.536 169.976 167.263 1.00 17.91  ? 384 MET A CA    1 
ATOM   2900  C  C     . MET A 1 384 ? 153.957 169.284 168.552 1.00 17.28  ? 384 MET A C     1 
ATOM   2901  O  O     . MET A 1 384 ? 153.221 169.321 169.544 1.00 27.68  ? 384 MET A O     1 
ATOM   2902  C  CB    . MET A 1 384 ? 152.741 169.010 166.384 1.00 19.89  ? 384 MET A CB    1 
ATOM   2903  C  CG    . MET A 1 384 ? 151.622 169.654 165.580 1.00 21.20  ? 384 MET A CG    1 
ATOM   2904  S  SD    . MET A 1 384 ? 150.791 170.989 166.460 1.00 47.92  ? 384 MET A SD    1 
ATOM   2905  C  CE    . MET A 1 384 ? 151.398 172.410 165.560 1.00 25.32  ? 384 MET A CE    1 
ATOM   2906  N  N     . LEU A 1 385 ? 155.130 168.646 168.556 1.00 18.59  ? 385 LEU A N     1 
ATOM   2907  C  CA    . LEU A 1 385 ? 155.627 168.024 169.779 1.00 23.57  ? 385 LEU A CA    1 
ATOM   2908  C  C     . LEU A 1 385 ? 155.874 169.066 170.862 1.00 20.73  ? 385 LEU A C     1 
ATOM   2909  O  O     . LEU A 1 385 ? 155.544 168.847 172.034 1.00 30.14  ? 385 LEU A O     1 
ATOM   2910  C  CB    . LEU A 1 385 ? 156.904 167.238 169.482 1.00 16.90  ? 385 LEU A CB    1 
ATOM   2911  C  CG    . LEU A 1 385 ? 156.775 166.069 168.502 1.00 25.64  ? 385 LEU A CG    1 
ATOM   2912  C  CD1   . LEU A 1 385 ? 158.147 165.586 168.055 1.00 25.91  ? 385 LEU A CD1   1 
ATOM   2913  C  CD2   . LEU A 1 385 ? 155.973 164.926 169.108 1.00 21.05  ? 385 LEU A CD2   1 
ATOM   2914  N  N     . PHE A 1 386 ? 156.451 170.212 170.489 1.00 17.74  ? 386 PHE A N     1 
ATOM   2915  C  CA    . PHE A 1 386 ? 156.667 171.282 171.457 1.00 21.15  ? 386 PHE A CA    1 
ATOM   2916  C  C     . PHE A 1 386 ? 155.364 171.976 171.830 1.00 20.01  ? 386 PHE A C     1 
ATOM   2917  O  O     . PHE A 1 386 ? 155.225 172.463 172.958 1.00 22.78  ? 386 PHE A O     1 
ATOM   2918  C  CB    . PHE A 1 386 ? 157.670 172.295 170.908 1.00 14.60  ? 386 PHE A CB    1 
ATOM   2919  C  CG    . PHE A 1 386 ? 159.084 171.798 170.891 1.00 22.11  ? 386 PHE A CG    1 
ATOM   2920  C  CD1   . PHE A 1 386 ? 159.763 171.566 172.076 1.00 26.58  ? 386 PHE A CD1   1 
ATOM   2921  C  CD2   . PHE A 1 386 ? 159.736 171.557 169.693 1.00 24.88  ? 386 PHE A CD2   1 
ATOM   2922  C  CE1   . PHE A 1 386 ? 161.065 171.106 172.067 1.00 24.79  ? 386 PHE A CE1   1 
ATOM   2923  C  CE2   . PHE A 1 386 ? 161.038 171.097 169.678 1.00 28.86  ? 386 PHE A CE2   1 
ATOM   2924  C  CZ    . PHE A 1 386 ? 161.704 170.871 170.866 1.00 28.40  ? 386 PHE A CZ    1 
ATOM   2925  N  N     . VAL A 1 387 ? 154.410 172.043 170.899 1.00 17.38  ? 387 VAL A N     1 
ATOM   2926  C  CA    . VAL A 1 387 ? 153.099 172.605 171.213 1.00 19.50  ? 387 VAL A CA    1 
ATOM   2927  C  C     . VAL A 1 387 ? 152.407 171.763 172.278 1.00 19.00  ? 387 VAL A C     1 
ATOM   2928  O  O     . VAL A 1 387 ? 151.775 172.295 173.200 1.00 24.02  ? 387 VAL A O     1 
ATOM   2929  C  CB    . VAL A 1 387 ? 152.248 172.723 169.934 1.00 28.44  ? 387 VAL A CB    1 
ATOM   2930  C  CG1   . VAL A 1 387 ? 150.782 172.944 170.276 1.00 17.86  ? 387 VAL A CG1   1 
ATOM   2931  C  CG2   . VAL A 1 387 ? 152.766 173.848 169.054 1.00 19.15  ? 387 VAL A CG2   1 
ATOM   2932  N  N     . LEU A 1 388 ? 152.517 170.437 172.170 1.00 15.42  ? 388 LEU A N     1 
ATOM   2933  C  CA    . LEU A 1 388 ? 151.914 169.556 173.167 1.00 16.12  ? 388 LEU A CA    1 
ATOM   2934  C  C     . LEU A 1 388 ? 152.552 169.749 174.539 1.00 18.07  ? 388 LEU A C     1 
ATOM   2935  O  O     . LEU A 1 388 ? 151.859 169.716 175.563 1.00 23.49  ? 388 LEU A O     1 
ATOM   2936  C  CB    . LEU A 1 388 ? 152.026 168.101 172.711 1.00 19.42  ? 388 LEU A CB    1 
ATOM   2937  C  CG    . LEU A 1 388 ? 151.170 167.732 171.495 1.00 26.23  ? 388 LEU A CG    1 
ATOM   2938  C  CD1   . LEU A 1 388 ? 151.182 166.230 171.249 1.00 24.49  ? 388 LEU A CD1   1 
ATOM   2939  C  CD2   . LEU A 1 388 ? 149.744 168.245 171.660 1.00 23.37  ? 388 LEU A CD2   1 
ATOM   2940  N  N     . LEU A 1 389 ? 153.873 169.940 174.584 1.00 21.56  ? 389 LEU A N     1 
ATOM   2941  C  CA    . LEU A 1 389 ? 154.523 170.281 175.847 1.00 24.08  ? 389 LEU A CA    1 
ATOM   2942  C  C     . LEU A 1 389 ? 154.051 171.633 176.363 1.00 16.37  ? 389 LEU A C     1 
ATOM   2943  O  O     . LEU A 1 389 ? 153.843 171.808 177.569 1.00 23.15  ? 389 LEU A O     1 
ATOM   2944  C  CB    . LEU A 1 389 ? 156.042 170.279 175.685 1.00 22.40  ? 389 LEU A CB    1 
ATOM   2945  C  CG    . LEU A 1 389 ? 156.789 168.984 176.003 1.00 30.99  ? 389 LEU A CG    1 
ATOM   2946  C  CD1   . LEU A 1 389 ? 156.353 167.852 175.097 1.00 27.38  ? 389 LEU A CD1   1 
ATOM   2947  C  CD2   . LEU A 1 389 ? 158.289 169.212 175.906 1.00 31.70  ? 389 LEU A CD2   1 
ATOM   2948  N  N     . ALA A 1 390 ? 153.885 172.604 175.462 1.00 24.32  ? 390 ALA A N     1 
ATOM   2949  C  CA    . ALA A 1 390 ? 153.477 173.942 175.876 1.00 21.80  ? 390 ALA A CA    1 
ATOM   2950  C  C     . ALA A 1 390 ? 152.085 173.934 176.497 1.00 22.11  ? 390 ALA A C     1 
ATOM   2951  O  O     . ALA A 1 390 ? 151.862 174.571 177.532 1.00 23.61  ? 390 ALA A O     1 
ATOM   2952  C  CB    . ALA A 1 390 ? 153.529 174.897 174.684 1.00 17.41  ? 390 ALA A CB    1 
ATOM   2953  N  N     . VAL A 1 391 ? 151.136 173.224 175.882 1.00 17.95  ? 391 VAL A N     1 
ATOM   2954  C  CA    . VAL A 1 391 ? 149.786 173.183 176.435 1.00 20.75  ? 391 VAL A CA    1 
ATOM   2955  C  C     . VAL A 1 391 ? 149.748 172.358 177.716 1.00 24.34  ? 391 VAL A C     1 
ATOM   2956  O  O     . VAL A 1 391 ? 148.937 172.628 178.610 1.00 22.50  ? 391 VAL A O     1 
ATOM   2957  C  CB    . VAL A 1 391 ? 148.781 172.662 175.389 1.00 17.14  ? 391 VAL A CB    1 
ATOM   2958  C  CG1   . VAL A 1 391 ? 148.753 173.582 174.178 1.00 21.30  ? 391 VAL A CG1   1 
ATOM   2959  C  CG2   . VAL A 1 391 ? 149.110 171.239 174.973 1.00 26.63  ? 391 VAL A CG2   1 
ATOM   2960  N  N     . PHE A 1 392 ? 150.607 171.340 177.830 1.00 15.33  ? 392 PHE A N     1 
ATOM   2961  C  CA    . PHE A 1 392 ? 150.660 170.556 179.061 1.00 21.67  ? 392 PHE A CA    1 
ATOM   2962  C  C     . PHE A 1 392 ? 151.145 171.401 180.232 1.00 24.05  ? 392 PHE A C     1 
ATOM   2963  O  O     . PHE A 1 392 ? 150.581 171.336 181.330 1.00 26.10  ? 392 PHE A O     1 
ATOM   2964  C  CB    . PHE A 1 392 ? 151.560 169.334 178.873 1.00 18.33  ? 392 PHE A CB    1 
ATOM   2965  C  CG    . PHE A 1 392 ? 151.670 168.470 180.098 1.00 16.16  ? 392 PHE A CG    1 
ATOM   2966  C  CD1   . PHE A 1 392 ? 150.685 167.545 180.400 1.00 23.52  ? 392 PHE A CD1   1 
ATOM   2967  C  CD2   . PHE A 1 392 ? 152.756 168.585 180.951 1.00 22.16  ? 392 PHE A CD2   1 
ATOM   2968  C  CE1   . PHE A 1 392 ? 150.780 166.752 181.527 1.00 26.86  ? 392 PHE A CE1   1 
ATOM   2969  C  CE2   . PHE A 1 392 ? 152.856 167.795 182.079 1.00 25.99  ? 392 PHE A CE2   1 
ATOM   2970  C  CZ    . PHE A 1 392 ? 151.867 166.876 182.367 1.00 27.23  ? 392 PHE A CZ    1 
ATOM   2971  N  N     . ILE A 1 393 ? 152.197 172.194 180.020 1.00 27.16  ? 393 ILE A N     1 
ATOM   2972  C  CA    . ILE A 1 393 ? 152.703 173.057 181.082 1.00 24.79  ? 393 ILE A CA    1 
ATOM   2973  C  C     . ILE A 1 393 ? 151.726 174.192 181.361 1.00 27.26  ? 393 ILE A C     1 
ATOM   2974  O  O     . ILE A 1 393 ? 151.455 174.525 182.521 1.00 30.29  ? 393 ILE A O     1 
ATOM   2975  C  CB    . ILE A 1 393 ? 154.103 173.584 180.715 1.00 27.05  ? 393 ILE A CB    1 
ATOM   2976  C  CG1   . ILE A 1 393 ? 155.161 172.513 180.986 1.00 32.60  ? 393 ILE A CG1   1 
ATOM   2977  C  CG2   . ILE A 1 393 ? 154.424 174.856 181.484 1.00 27.13  ? 393 ILE A CG2   1 
ATOM   2978  C  CD1   . ILE A 1 393 ? 155.310 172.158 182.450 1.00 30.14  ? 393 ILE A CD1   1 
ATOM   2979  N  N     . ALA A 1 394 ? 151.179 174.802 180.305 1.00 23.03  ? 394 ALA A N     1 
ATOM   2980  C  CA    . ALA A 1 394 ? 150.230 175.896 180.489 1.00 22.15  ? 394 ALA A CA    1 
ATOM   2981  C  C     . ALA A 1 394 ? 148.969 175.423 181.200 1.00 24.07  ? 394 ALA A C     1 
ATOM   2982  O  O     . ALA A 1 394 ? 148.437 176.124 182.068 1.00 33.25  ? 394 ALA A O     1 
ATOM   2983  C  CB    . ALA A 1 394 ? 149.880 176.522 179.141 1.00 24.43  ? 394 ALA A CB    1 
ATOM   2984  N  N     . GLY A 1 395 ? 148.470 174.239 180.839 1.00 21.70  ? 395 GLY A N     1 
ATOM   2985  C  CA    . GLY A 1 395 ? 147.288 173.715 181.501 1.00 21.09  ? 395 GLY A CA    1 
ATOM   2986  C  C     . GLY A 1 395 ? 147.511 173.466 182.980 1.00 25.43  ? 395 GLY A C     1 
ATOM   2987  O  O     . GLY A 1 395 ? 146.643 173.754 183.806 1.00 28.99  ? 395 GLY A O     1 
ATOM   2988  N  N     . LEU A 1 396 ? 148.680 172.926 183.332 1.00 26.78  ? 396 LEU A N     1 
ATOM   2989  C  CA    . LEU A 1 396 ? 148.998 172.703 184.739 1.00 28.38  ? 396 LEU A CA    1 
ATOM   2990  C  C     . LEU A 1 396 ? 149.078 174.019 185.502 1.00 25.14  ? 396 LEU A C     1 
ATOM   2991  O  O     . LEU A 1 396 ? 148.572 174.126 186.624 1.00 35.09  ? 396 LEU A O     1 
ATOM   2992  C  CB    . LEU A 1 396 ? 150.311 171.931 184.864 1.00 24.24  ? 396 LEU A CB    1 
ATOM   2993  C  CG    . LEU A 1 396 ? 150.208 170.424 185.105 1.00 29.80  ? 396 LEU A CG    1 
ATOM   2994  C  CD1   . LEU A 1 396 ? 149.363 169.760 184.029 1.00 31.15  ? 396 LEU A CD1   1 
ATOM   2995  C  CD2   . LEU A 1 396 ? 151.591 169.797 185.167 1.00 28.11  ? 396 LEU A CD2   1 
ATOM   2996  N  N     . MET A 1 397 ? 149.703 175.036 184.905 1.00 23.39  ? 397 MET A N     1 
ATOM   2997  C  CA    . MET A 1 397 ? 149.886 176.315 185.580 1.00 30.23  ? 397 MET A CA    1 
ATOM   2998  C  C     . MET A 1 397 ? 148.588 177.095 185.746 1.00 25.75  ? 397 MET A C     1 
ATOM   2999  O  O     . MET A 1 397 ? 148.569 178.069 186.505 1.00 31.34  ? 397 MET A O     1 
ATOM   3000  C  CB    . MET A 1 397 ? 150.908 177.164 184.824 1.00 27.52  ? 397 MET A CB    1 
ATOM   3001  C  CG    . MET A 1 397 ? 152.347 176.721 185.032 1.00 23.70  ? 397 MET A CG    1 
ATOM   3002  S  SD    . MET A 1 397 ? 153.523 177.691 184.073 1.00 50.74  ? 397 MET A SD    1 
ATOM   3003  C  CE    . MET A 1 397 ? 154.353 178.592 185.380 1.00 31.17  ? 397 MET A CE    1 
ATOM   3004  N  N     . ILE A 1 398 ? 147.516 176.702 185.062 1.00 28.64  ? 398 ILE A N     1 
ATOM   3005  C  CA    . ILE A 1 398 ? 146.210 177.329 185.221 1.00 22.07  ? 398 ILE A CA    1 
ATOM   3006  C  C     . ILE A 1 398 ? 145.220 176.399 185.910 1.00 26.33  ? 398 ILE A C     1 
ATOM   3007  O  O     . ILE A 1 398 ? 144.035 176.731 186.017 1.00 35.80  ? 398 ILE A O     1 
ATOM   3008  C  CB    . ILE A 1 398 ? 145.653 177.819 183.874 1.00 26.04  ? 398 ILE A CB    1 
ATOM   3009  C  CG1   . ILE A 1 398 ? 145.292 176.631 182.980 1.00 29.24  ? 398 ILE A CG1   1 
ATOM   3010  C  CG2   . ILE A 1 398 ? 146.652 178.732 183.184 1.00 28.22  ? 398 ILE A CG2   1 
ATOM   3011  C  CD1   . ILE A 1 398 ? 144.506 177.013 181.746 1.00 29.48  ? 398 ILE A CD1   1 
ATOM   3012  N  N     . GLY A 1 399 ? 145.676 175.244 186.382 1.00 26.80  ? 399 GLY A N     1 
ATOM   3013  C  CA    . GLY A 1 399 ? 144.801 174.300 187.056 1.00 31.64  ? 399 GLY A CA    1 
ATOM   3014  C  C     . GLY A 1 399 ? 143.738 173.687 186.171 1.00 31.05  ? 399 GLY A C     1 
ATOM   3015  O  O     . GLY A 1 399 ? 142.590 173.533 186.606 1.00 36.32  ? 399 GLY A O     1 
ATOM   3016  N  N     . ARG A 1 400 ? 144.091 173.328 184.939 1.00 29.26  ? 400 ARG A N     1 
ATOM   3017  C  CA    . ARG A 1 400 ? 143.145 172.743 184.002 1.00 28.85  ? 400 ARG A CA    1 
ATOM   3018  C  C     . ARG A 1 400 ? 143.799 171.573 183.283 1.00 31.08  ? 400 ARG A C     1 
ATOM   3019  O  O     . ARG A 1 400 ? 145.026 171.474 183.200 1.00 31.52  ? 400 ARG A O     1 
ATOM   3020  C  CB    . ARG A 1 400 ? 142.644 173.773 182.981 1.00 32.33  ? 400 ARG A CB    1 
ATOM   3021  C  CG    . ARG A 1 400 ? 141.582 174.716 183.518 1.00 33.21  ? 400 ARG A CG    1 
ATOM   3022  C  CD    . ARG A 1 400 ? 141.050 175.623 182.422 1.00 36.62  ? 400 ARG A CD    1 
ATOM   3023  N  NE    . ARG A 1 400 ? 140.049 174.957 181.598 1.00 42.35  ? 400 ARG A NE    1 
ATOM   3024  C  CZ    . ARG A 1 400 ? 138.773 174.820 181.932 1.00 40.05  ? 400 ARG A CZ    1 
ATOM   3025  N  NH1   . ARG A 1 400 ? 138.302 175.296 183.072 1.00 41.12  ? 400 ARG A NH1   1 
ATOM   3026  N  NH2   . ARG A 1 400 ? 137.949 174.190 181.099 1.00 38.67  ? 400 ARG A NH2   1 
ATOM   3027  N  N     . THR A 1 401 ? 142.960 170.681 182.771 1.00 33.22  ? 401 THR A N     1 
ATOM   3028  C  CA    . THR A 1 401 ? 143.451 169.564 181.979 1.00 34.41  ? 401 THR A CA    1 
ATOM   3029  C  C     . THR A 1 401 ? 144.093 170.090 180.698 1.00 33.75  ? 401 THR A C     1 
ATOM   3030  O  O     . THR A 1 401 ? 143.522 170.974 180.044 1.00 34.15  ? 401 THR A O     1 
ATOM   3031  C  CB    . THR A 1 401 ? 142.310 168.604 181.643 1.00 34.11  ? 401 THR A CB    1 
ATOM   3032  O  OG1   . THR A 1 401 ? 141.527 168.360 182.818 1.00 43.70  ? 401 THR A OG1   1 
ATOM   3033  C  CG2   . THR A 1 401 ? 142.853 167.282 181.122 1.00 32.70  ? 401 THR A CG2   1 
ATOM   3034  N  N     . PRO A 1 402 ? 145.274 169.599 180.319 1.00 26.54  ? 402 PRO A N     1 
ATOM   3035  C  CA    . PRO A 1 402 ? 145.907 170.074 179.082 1.00 29.47  ? 402 PRO A CA    1 
ATOM   3036  C  C     . PRO A 1 402 ? 145.023 169.821 177.870 1.00 23.70  ? 402 PRO A C     1 
ATOM   3037  O  O     . PRO A 1 402 ? 144.367 168.783 177.759 1.00 31.04  ? 402 PRO A O     1 
ATOM   3038  C  CB    . PRO A 1 402 ? 147.204 169.260 179.015 1.00 27.75  ? 402 PRO A CB    1 
ATOM   3039  C  CG    . PRO A 1 402 ? 147.486 168.893 180.431 1.00 28.89  ? 402 PRO A CG    1 
ATOM   3040  C  CD    . PRO A 1 402 ? 146.149 168.689 181.076 1.00 26.10  ? 402 PRO A CD    1 
ATOM   3041  N  N     . GLU A 1 403 ? 145.016 170.786 176.954 1.00 34.49  ? 403 GLU A N     1 
ATOM   3042  C  CA    . GLU A 1 403 ? 144.114 170.750 175.813 1.00 32.68  ? 403 GLU A CA    1 
ATOM   3043  C  C     . GLU A 1 403 ? 144.736 171.501 174.647 1.00 30.50  ? 403 GLU A C     1 
ATOM   3044  O  O     . GLU A 1 403 ? 145.421 172.509 174.841 1.00 37.62  ? 403 GLU A O     1 
ATOM   3045  C  CB    . GLU A 1 403 ? 142.755 171.362 176.173 1.00 30.31  ? 403 GLU A CB    1 
ATOM   3046  C  CG    . GLU A 1 403 ? 141.558 170.515 175.787 1.00 35.32  ? 403 GLU A CG    1 
ATOM   3047  C  CD    . GLU A 1 403 ? 140.257 171.290 175.860 1.00 44.57  ? 403 GLU A CD    1 
ATOM   3048  O  OE1   . GLU A 1 403 ? 139.500 171.091 176.833 1.00 47.00  ? 403 GLU A OE1   1 
ATOM   3049  O  OE2   . GLU A 1 403 ? 139.995 172.104 174.951 1.00 43.73  ? 403 GLU A OE2   1 
ATOM   3050  N  N     . TYR A 1 404 ? 144.492 171.002 173.438 1.00 26.33  ? 404 TYR A N     1 
ATOM   3051  C  CA    . TYR A 1 404 ? 144.903 171.690 172.219 1.00 23.27  ? 404 TYR A CA    1 
ATOM   3052  C  C     . TYR A 1 404 ? 143.850 171.435 171.154 1.00 23.95  ? 404 TYR A C     1 
ATOM   3053  O  O     . TYR A 1 404 ? 143.573 170.278 170.825 1.00 31.09  ? 404 TYR A O     1 
ATOM   3054  C  CB    . TYR A 1 404 ? 146.279 171.219 171.743 1.00 23.77  ? 404 TYR A CB    1 
ATOM   3055  C  CG    . TYR A 1 404 ? 146.812 172.013 170.570 1.00 23.54  ? 404 TYR A CG    1 
ATOM   3056  C  CD1   . TYR A 1 404 ? 146.883 173.399 170.622 1.00 24.75  ? 404 TYR A CD1   1 
ATOM   3057  C  CD2   . TYR A 1 404 ? 147.233 171.378 169.410 1.00 24.35  ? 404 TYR A CD2   1 
ATOM   3058  C  CE1   . TYR A 1 404 ? 147.364 174.131 169.553 1.00 25.38  ? 404 TYR A CE1   1 
ATOM   3059  C  CE2   . TYR A 1 404 ? 147.717 172.102 168.336 1.00 25.01  ? 404 TYR A CE2   1 
ATOM   3060  C  CZ    . TYR A 1 404 ? 147.780 173.477 168.413 1.00 27.92  ? 404 TYR A CZ    1 
ATOM   3061  O  OH    . TYR A 1 404 ? 148.260 174.201 167.346 1.00 36.75  ? 404 TYR A OH    1 
ATOM   3062  N  N     . LEU A 1 405 ? 143.267 172.514 170.627 1.00 27.24  ? 405 LEU A N     1 
ATOM   3063  C  CA    . LEU A 1 405 ? 142.208 172.441 169.620 1.00 28.37  ? 405 LEU A CA    1 
ATOM   3064  C  C     . LEU A 1 405 ? 141.014 171.627 170.110 1.00 27.98  ? 405 LEU A C     1 
ATOM   3065  O  O     . LEU A 1 405 ? 140.367 170.922 169.331 1.00 36.85  ? 405 LEU A O     1 
ATOM   3066  C  CB    . LEU A 1 405 ? 142.732 171.876 168.297 1.00 26.70  ? 405 LEU A CB    1 
ATOM   3067  C  CG    . LEU A 1 405 ? 143.974 172.555 167.719 1.00 28.64  ? 405 LEU A CG    1 
ATOM   3068  C  CD1   . LEU A 1 405 ? 144.452 171.816 166.484 1.00 25.31  ? 405 LEU A CD1   1 
ATOM   3069  C  CD2   . LEU A 1 405 ? 143.689 174.014 167.400 1.00 28.73  ? 405 LEU A CD2   1 
ATOM   3070  N  N     . GLY A 1 406 ? 140.714 171.717 171.404 1.00 28.46  ? 406 GLY A N     1 
ATOM   3071  C  CA    . GLY A 1 406 ? 139.575 171.037 171.978 1.00 31.07  ? 406 GLY A CA    1 
ATOM   3072  C  C     . GLY A 1 406 ? 139.783 169.577 172.310 1.00 32.12  ? 406 GLY A C     1 
ATOM   3073  O  O     . GLY A 1 406 ? 138.851 168.939 172.814 1.00 37.22  ? 406 GLY A O     1 
ATOM   3074  N  N     . LYS A 1 407 ? 140.967 169.027 172.061 1.00 27.77  ? 407 LYS A N     1 
ATOM   3075  C  CA    . LYS A 1 407 ? 141.241 167.617 172.302 1.00 29.72  ? 407 LYS A CA    1 
ATOM   3076  C  C     . LYS A 1 407 ? 142.072 167.460 173.568 1.00 30.34  ? 407 LYS A C     1 
ATOM   3077  O  O     . LYS A 1 407 ? 143.090 168.140 173.738 1.00 35.64  ? 407 LYS A O     1 
ATOM   3078  C  CB    . LYS A 1 407 ? 141.966 166.990 171.110 1.00 28.75  ? 407 LYS A CB    1 
ATOM   3079  C  CG    . LYS A 1 407 ? 141.142 166.963 169.835 1.00 31.78  ? 407 LYS A CG    1 
ATOM   3080  C  CD    . LYS A 1 407 ? 141.261 165.627 169.125 1.00 30.03  ? 407 LYS A CD    1 
ATOM   3081  C  CE    . LYS A 1 407 ? 140.176 165.467 168.074 1.00 26.05  ? 407 LYS A CE    1 
ATOM   3082  N  NZ    . LYS A 1 407 ? 140.340 164.213 167.291 1.00 19.30  ? 407 LYS A NZ    1 
ATOM   3083  N  N     . LYS A 1 408 ? 141.632 166.568 174.451 1.00 34.31  ? 408 LYS A N     1 
ATOM   3084  C  CA    . LYS A 1 408 ? 142.346 166.324 175.695 1.00 32.76  ? 408 LYS A CA    1 
ATOM   3085  C  C     . LYS A 1 408 ? 143.691 165.661 175.423 1.00 34.91  ? 408 LYS A C     1 
ATOM   3086  O  O     . LYS A 1 408 ? 143.815 164.804 174.544 1.00 39.75  ? 408 LYS A O     1 
ATOM   3087  C  CB    . LYS A 1 408 ? 141.510 165.445 176.624 1.00 32.21  ? 408 LYS A CB    1 
ATOM   3088  C  CG    . LYS A 1 408 ? 140.216 166.086 177.099 1.00 38.84  ? 408 LYS A CG    1 
ATOM   3089  C  CD    . LYS A 1 408 ? 140.455 167.484 177.644 1.00 40.67  ? 408 LYS A CD    1 
ATOM   3090  C  CE    . LYS A 1 408 ? 139.563 167.767 178.841 1.00 41.30  ? 408 LYS A CE    1 
ATOM   3091  N  NZ    . LYS A 1 408 ? 139.306 166.540 179.644 1.00 40.58  ? 408 LYS A NZ    1 
ATOM   3092  N  N     . ILE A 1 409 ? 144.701 166.064 176.185 1.00 31.10  ? 409 ILE A N     1 
ATOM   3093  C  CA    . ILE A 1 409 ? 146.032 165.475 176.111 1.00 32.80  ? 409 ILE A CA    1 
ATOM   3094  C  C     . ILE A 1 409 ? 146.190 164.538 177.299 1.00 34.92  ? 409 ILE A C     1 
ATOM   3095  O  O     . ILE A 1 409 ? 146.129 164.972 178.456 1.00 42.10  ? 409 ILE A O     1 
ATOM   3096  C  CB    . ILE A 1 409 ? 147.126 166.554 176.101 1.00 33.44  ? 409 ILE A CB    1 
ATOM   3097  C  CG1   . ILE A 1 409 ? 146.789 167.646 175.084 1.00 33.78  ? 409 ILE A CG1   1 
ATOM   3098  C  CG2   . ILE A 1 409 ? 148.471 165.937 175.780 1.00 33.30  ? 409 ILE A CG2   1 
ATOM   3099  C  CD1   . ILE A 1 409 ? 146.682 167.145 173.660 1.00 31.13  ? 409 ILE A CD1   1 
ATOM   3100  N  N     . ASP A 1 410 ? 146.397 163.255 177.019 1.00 35.03  ? 410 ASP A N     1 
ATOM   3101  C  CA    . ASP A 1 410 ? 146.405 162.215 178.034 1.00 33.65  ? 410 ASP A CA    1 
ATOM   3102  C  C     . ASP A 1 410 ? 147.825 161.700 178.264 1.00 36.83  ? 410 ASP A C     1 
ATOM   3103  O  O     . ASP A 1 410 ? 148.801 162.225 177.716 1.00 36.54  ? 410 ASP A O     1 
ATOM   3104  C  CB    . ASP A 1 410 ? 145.452 161.087 177.630 1.00 33.30  ? 410 ASP A CB    1 
ATOM   3105  C  CG    . ASP A 1 410 ? 144.041 161.304 178.141 1.00 45.74  ? 410 ASP A CG    1 
ATOM   3106  O  OD1   . ASP A 1 410 ? 143.888 161.832 179.262 1.00 49.52  ? 410 ASP A OD1   1 
ATOM   3107  O  OD2   . ASP A 1 410 ? 143.085 160.947 177.421 1.00 49.17  ? 410 ASP A OD2   1 
ATOM   3108  N  N     . VAL A 1 411 ? 147.933 160.660 179.094 1.00 34.07  ? 411 VAL A N     1 
ATOM   3109  C  CA    . VAL A 1 411 ? 149.235 160.089 179.429 1.00 24.16  ? 411 VAL A CA    1 
ATOM   3110  C  C     . VAL A 1 411 ? 149.893 159.487 178.194 1.00 29.02  ? 411 VAL A C     1 
ATOM   3111  O  O     . VAL A 1 411 ? 151.103 159.637 177.982 1.00 33.83  ? 411 VAL A O     1 
ATOM   3112  C  CB    . VAL A 1 411 ? 149.081 159.051 180.558 1.00 27.34  ? 411 VAL A CB    1 
ATOM   3113  C  CG1   . VAL A 1 411 ? 150.307 158.153 180.642 1.00 31.65  ? 411 VAL A CG1   1 
ATOM   3114  C  CG2   . VAL A 1 411 ? 148.828 159.746 181.887 1.00 29.34  ? 411 VAL A CG2   1 
ATOM   3115  N  N     . ARG A 1 412 ? 149.109 158.801 177.357 1.00 32.05  ? 412 ARG A N     1 
ATOM   3116  C  CA    . ARG A 1 412 ? 149.673 158.141 176.183 1.00 30.10  ? 412 ARG A CA    1 
ATOM   3117  C  C     . ARG A 1 412 ? 150.316 159.144 175.232 1.00 25.15  ? 412 ARG A C     1 
ATOM   3118  O  O     . ARG A 1 412 ? 151.393 158.886 174.683 1.00 26.64  ? 412 ARG A O     1 
ATOM   3119  C  CB    . ARG A 1 412 ? 148.591 157.337 175.463 1.00 29.90  ? 412 ARG A CB    1 
ATOM   3120  C  CG    . ARG A 1 412 ? 149.092 156.594 174.235 1.00 31.03  ? 412 ARG A CG    1 
ATOM   3121  C  CD    . ARG A 1 412 ? 148.046 155.634 173.695 1.00 37.21  ? 412 ARG A CD    1 
ATOM   3122  N  NE    . ARG A 1 412 ? 148.408 155.120 172.380 1.00 39.49  ? 412 ARG A NE    1 
ATOM   3123  C  CZ    . ARG A 1 412 ? 149.293 154.155 172.168 1.00 39.45  ? 412 ARG A CZ    1 
ATOM   3124  N  NH1   . ARG A 1 412 ? 149.924 153.564 173.170 1.00 36.00  ? 412 ARG A NH1   1 
ATOM   3125  N  NH2   . ARG A 1 412 ? 149.551 153.773 170.921 1.00 39.31  ? 412 ARG A NH2   1 
ATOM   3126  N  N     . GLU A 1 413 ? 149.669 160.293 175.022 1.00 27.55  ? 413 GLU A N     1 
ATOM   3127  C  CA    . GLU A 1 413 ? 150.249 161.318 174.160 1.00 27.81  ? 413 GLU A CA    1 
ATOM   3128  C  C     . GLU A 1 413 ? 151.561 161.842 174.730 1.00 28.26  ? 413 GLU A C     1 
ATOM   3129  O  O     . GLU A 1 413 ? 152.532 162.037 173.990 1.00 35.04  ? 413 GLU A O     1 
ATOM   3130  C  CB    . GLU A 1 413 ? 149.256 162.462 173.961 1.00 27.35  ? 413 GLU A CB    1 
ATOM   3131  C  CG    . GLU A 1 413 ? 148.223 162.197 172.884 1.00 34.03  ? 413 GLU A CG    1 
ATOM   3132  C  CD    . GLU A 1 413 ? 146.896 161.737 173.450 1.00 38.34  ? 413 GLU A CD    1 
ATOM   3133  O  OE1   . GLU A 1 413 ? 146.813 161.519 174.677 1.00 36.22  ? 413 GLU A OE1   1 
ATOM   3134  O  OE2   . GLU A 1 413 ? 145.935 161.594 172.667 1.00 41.13  ? 413 GLU A OE2   1 
ATOM   3135  N  N     . MET A 1 414 ? 151.609 162.075 176.044 1.00 29.08  ? 414 MET A N     1 
ATOM   3136  C  CA    . MET A 1 414 ? 152.848 162.522 176.674 1.00 28.47  ? 414 MET A CA    1 
ATOM   3137  C  C     . MET A 1 414 ? 153.938 161.463 176.574 1.00 24.93  ? 414 MET A C     1 
ATOM   3138  O  O     . MET A 1 414 ? 155.115 161.793 176.388 1.00 31.15  ? 414 MET A O     1 
ATOM   3139  C  CB    . MET A 1 414 ? 152.586 162.900 178.132 1.00 27.15  ? 414 MET A CB    1 
ATOM   3140  C  CG    . MET A 1 414 ? 151.882 164.250 178.392 1.00 32.37  ? 414 MET A CG    1 
ATOM   3141  S  SD    . MET A 1 414 ? 152.525 165.767 177.619 1.00 50.19  ? 414 MET A SD    1 
ATOM   3142  C  CE    . MET A 1 414 ? 152.028 165.662 175.898 1.00 34.62  ? 414 MET A CE    1 
ATOM   3143  N  N     . LYS A 1 415 ? 153.569 160.186 176.702 1.00 23.24  ? 415 LYS A N     1 
ATOM   3144  C  CA    . LYS A 1 415 ? 154.556 159.119 176.569 1.00 27.54  ? 415 LYS A CA    1 
ATOM   3145  C  C     . LYS A 1 415 ? 155.165 159.103 175.172 1.00 27.12  ? 415 LYS A C     1 
ATOM   3146  O  O     . LYS A 1 415 ? 156.384 158.966 175.018 1.00 35.44  ? 415 LYS A O     1 
ATOM   3147  C  CB    . LYS A 1 415 ? 153.918 157.768 176.890 1.00 27.43  ? 415 LYS A CB    1 
ATOM   3148  C  CG    . LYS A 1 415 ? 154.756 156.883 177.797 1.00 30.51  ? 415 LYS A CG    1 
ATOM   3149  C  CD    . LYS A 1 415 ? 154.021 155.598 178.146 1.00 30.99  ? 415 LYS A CD    1 
ATOM   3150  C  CE    . LYS A 1 415 ? 153.521 155.616 179.581 1.00 29.27  ? 415 LYS A CE    1 
ATOM   3151  N  NZ    . LYS A 1 415 ? 152.654 154.443 179.880 1.00 33.61  ? 415 LYS A NZ    1 
ATOM   3152  N  N     . LEU A 1 416 ? 154.332 159.253 174.140 1.00 22.42  ? 416 LEU A N     1 
ATOM   3153  C  CA    . LEU A 1 416 ? 154.845 159.241 172.775 1.00 21.74  ? 416 LEU A CA    1 
ATOM   3154  C  C     . LEU A 1 416 ? 155.574 160.538 172.445 1.00 21.83  ? 416 LEU A C     1 
ATOM   3155  O  O     . LEU A 1 416 ? 156.599 160.521 171.755 1.00 25.70  ? 416 LEU A O     1 
ATOM   3156  C  CB    . LEU A 1 416 ? 153.703 159.005 171.788 1.00 22.00  ? 416 LEU A CB    1 
ATOM   3157  C  CG    . LEU A 1 416 ? 152.923 157.698 171.938 1.00 26.39  ? 416 LEU A CG    1 
ATOM   3158  C  CD1   . LEU A 1 416 ? 151.576 157.803 171.243 1.00 27.25  ? 416 LEU A CD1   1 
ATOM   3159  C  CD2   . LEU A 1 416 ? 153.719 156.520 171.401 1.00 20.03  ? 416 LEU A CD2   1 
ATOM   3160  N  N     . THR A 1 417 ? 155.055 161.672 172.924 1.00 22.68  ? 417 THR A N     1 
ATOM   3161  C  CA    . THR A 1 417 ? 155.693 162.954 172.641 1.00 13.84  ? 417 THR A CA    1 
ATOM   3162  C  C     . THR A 1 417 ? 157.077 163.030 173.271 1.00 22.62  ? 417 THR A C     1 
ATOM   3163  O  O     . THR A 1 417 ? 158.025 163.527 172.650 1.00 26.13  ? 417 THR A O     1 
ATOM   3164  C  CB    . THR A 1 417 ? 154.814 164.101 173.141 1.00 25.21  ? 417 THR A CB    1 
ATOM   3165  O  OG1   . THR A 1 417 ? 153.475 163.922 172.662 1.00 33.30  ? 417 THR A OG1   1 
ATOM   3166  C  CG2   . THR A 1 417 ? 155.344 165.434 172.643 1.00 20.57  ? 417 THR A CG2   1 
ATOM   3167  N  N     . ALA A 1 418 ? 157.212 162.545 174.507 1.00 25.70  ? 418 ALA A N     1 
ATOM   3168  C  CA    . ALA A 1 418 ? 158.517 162.523 175.157 1.00 22.72  ? 418 ALA A CA    1 
ATOM   3169  C  C     . ALA A 1 418 ? 159.493 161.629 174.404 1.00 23.13  ? 418 ALA A C     1 
ATOM   3170  O  O     . ALA A 1 418 ? 160.663 161.986 174.224 1.00 21.72  ? 418 ALA A O     1 
ATOM   3171  C  CB    . ALA A 1 418 ? 158.374 162.060 176.606 1.00 21.89  ? 418 ALA A CB    1 
ATOM   3172  N  N     . LEU A 1 419 ? 159.030 160.458 173.961 1.00 25.31  ? 419 LEU A N     1 
ATOM   3173  C  CA    . LEU A 1 419 ? 159.898 159.558 173.209 1.00 20.62  ? 419 LEU A CA    1 
ATOM   3174  C  C     . LEU A 1 419 ? 160.313 160.172 171.878 1.00 24.36  ? 419 LEU A C     1 
ATOM   3175  O  O     . LEU A 1 419 ? 161.479 160.074 171.482 1.00 29.62  ? 419 LEU A O     1 
ATOM   3176  C  CB    . LEU A 1 419 ? 159.198 158.217 172.988 1.00 22.09  ? 419 LEU A CB    1 
ATOM   3177  C  CG    . LEU A 1 419 ? 159.081 157.296 174.205 1.00 31.52  ? 419 LEU A CG    1 
ATOM   3178  C  CD1   . LEU A 1 419 ? 158.141 156.136 173.911 1.00 30.13  ? 419 LEU A CD1   1 
ATOM   3179  C  CD2   . LEU A 1 419 ? 160.449 156.788 174.628 1.00 24.90  ? 419 LEU A CD2   1 
ATOM   3180  N  N     . ALA A 1 420 ? 159.372 160.809 171.176 1.00 14.23  ? 420 ALA A N     1 
ATOM   3181  C  CA    . ALA A 1 420 ? 159.691 161.418 169.889 1.00 15.98  ? 420 ALA A CA    1 
ATOM   3182  C  C     . ALA A 1 420 ? 160.682 162.564 170.045 1.00 27.84  ? 420 ALA A C     1 
ATOM   3183  O  O     . ALA A 1 420 ? 161.606 162.709 169.236 1.00 23.23  ? 420 ALA A O     1 
ATOM   3184  C  CB    . ALA A 1 420 ? 158.412 161.906 169.209 1.00 18.11  ? 420 ALA A CB    1 
ATOM   3185  N  N     . ILE A 1 421 ? 160.503 163.392 171.076 1.00 20.44  ? 421 ILE A N     1 
ATOM   3186  C  CA    . ILE A 1 421 ? 161.401 164.522 171.289 1.00 18.91  ? 421 ILE A CA    1 
ATOM   3187  C  C     . ILE A 1 421 ? 162.797 164.035 171.662 1.00 23.41  ? 421 ILE A C     1 
ATOM   3188  O  O     . ILE A 1 421 ? 163.803 164.626 171.254 1.00 23.50  ? 421 ILE A O     1 
ATOM   3189  C  CB    . ILE A 1 421 ? 160.813 165.470 172.352 1.00 23.11  ? 421 ILE A CB    1 
ATOM   3190  C  CG1   . ILE A 1 421 ? 159.720 166.344 171.734 1.00 29.12  ? 421 ILE A CG1   1 
ATOM   3191  C  CG2   . ILE A 1 421 ? 161.895 166.339 172.977 1.00 28.77  ? 421 ILE A CG2   1 
ATOM   3192  C  CD1   . ILE A 1 421 ? 159.099 167.330 172.700 1.00 31.19  ? 421 ILE A CD1   1 
ATOM   3193  N  N     . LEU A 1 422 ? 162.884 162.941 172.418 1.00 21.60  ? 422 LEU A N     1 
ATOM   3194  C  CA    . LEU A 1 422 ? 164.165 162.438 172.899 1.00 22.15  ? 422 LEU A CA    1 
ATOM   3195  C  C     . LEU A 1 422 ? 164.979 161.714 171.834 1.00 24.22  ? 422 LEU A C     1 
ATOM   3196  O  O     . LEU A 1 422 ? 166.161 161.442 172.069 1.00 32.50  ? 422 LEU A O     1 
ATOM   3197  C  CB    . LEU A 1 422 ? 163.946 161.493 174.084 1.00 27.24  ? 422 LEU A CB    1 
ATOM   3198  C  CG    . LEU A 1 422 ? 163.787 162.123 175.467 1.00 27.13  ? 422 LEU A CG    1 
ATOM   3199  C  CD1   . LEU A 1 422 ? 163.514 161.048 176.506 1.00 22.48  ? 422 LEU A CD1   1 
ATOM   3200  C  CD2   . LEU A 1 422 ? 165.022 162.928 175.836 1.00 28.03  ? 422 LEU A CD2   1 
ATOM   3201  N  N     . VAL A 1 423 ? 164.391 161.395 170.679 1.00 18.85  ? 423 VAL A N     1 
ATOM   3202  C  CA    . VAL A 1 423 ? 165.083 160.562 169.697 1.00 23.66  ? 423 VAL A CA    1 
ATOM   3203  C  C     . VAL A 1 423 ? 166.280 161.302 169.110 1.00 21.19  ? 423 VAL A C     1 
ATOM   3204  O  O     . VAL A 1 423 ? 167.418 160.823 169.169 1.00 15.72  ? 423 VAL A O     1 
ATOM   3205  C  CB    . VAL A 1 423 ? 164.110 160.103 168.595 1.00 19.28  ? 423 VAL A CB    1 
ATOM   3206  C  CG1   . VAL A 1 423 ? 164.874 159.700 167.340 1.00 17.88  ? 423 VAL A CG1   1 
ATOM   3207  C  CG2   . VAL A 1 423 ? 163.258 158.946 169.088 1.00 25.70  ? 423 VAL A CG2   1 
ATOM   3208  N  N     . THR A 1 424 ? 166.038 162.478 168.531 1.00 14.88  ? 424 THR A N     1 
ATOM   3209  C  CA    . THR A 1 424 ? 167.102 163.186 167.820 1.00 13.68  ? 424 THR A CA    1 
ATOM   3210  C  C     . THR A 1 424 ? 168.245 163.638 168.726 1.00 22.89  ? 424 THR A C     1 
ATOM   3211  O  O     . THR A 1 424 ? 169.410 163.382 168.376 1.00 23.43  ? 424 THR A O     1 
ATOM   3212  C  CB    . THR A 1 424 ? 166.498 164.359 167.038 1.00 26.61  ? 424 THR A CB    1 
ATOM   3213  O  OG1   . THR A 1 424 ? 165.957 163.880 165.799 1.00 30.56  ? 424 THR A OG1   1 
ATOM   3214  C  CG2   . THR A 1 424 ? 167.552 165.400 166.749 1.00 27.49  ? 424 THR A CG2   1 
ATOM   3215  N  N     . PRO A 1 425 ? 168.012 164.301 169.868 1.00 24.48  ? 425 PRO A N     1 
ATOM   3216  C  CA    . PRO A 1 425 ? 169.154 164.685 170.718 1.00 20.97  ? 425 PRO A CA    1 
ATOM   3217  C  C     . PRO A 1 425 ? 169.959 163.503 171.224 1.00 20.71  ? 425 PRO A C     1 
ATOM   3218  O  O     . PRO A 1 425 ? 171.172 163.637 171.429 1.00 23.08  ? 425 PRO A O     1 
ATOM   3219  C  CB    . PRO A 1 425 ? 168.494 165.456 171.871 1.00 18.12  ? 425 PRO A CB    1 
ATOM   3220  C  CG    . PRO A 1 425 ? 167.076 165.022 171.863 1.00 27.58  ? 425 PRO A CG    1 
ATOM   3221  C  CD    . PRO A 1 425 ? 166.744 164.798 170.426 1.00 16.51  ? 425 PRO A CD    1 
ATOM   3222  N  N     . THR A 1 426 ? 169.321 162.351 171.444 1.00 12.03  ? 426 THR A N     1 
ATOM   3223  C  CA    . THR A 1 426 ? 170.060 161.168 171.870 1.00 16.80  ? 426 THR A CA    1 
ATOM   3224  C  C     . THR A 1 426 ? 171.063 160.736 170.808 1.00 22.87  ? 426 THR A C     1 
ATOM   3225  O  O     . THR A 1 426 ? 172.210 160.400 171.126 1.00 23.94  ? 426 THR A O     1 
ATOM   3226  C  CB    . THR A 1 426 ? 169.091 160.027 172.187 1.00 23.27  ? 426 THR A CB    1 
ATOM   3227  O  OG1   . THR A 1 426 ? 168.215 160.423 173.250 1.00 29.56  ? 426 THR A OG1   1 
ATOM   3228  C  CG2   . THR A 1 426 ? 169.850 158.777 172.605 1.00 17.01  ? 426 THR A CG2   1 
ATOM   3229  N  N     . LEU A 1 427 ? 170.651 160.744 169.539 1.00 19.41  ? 427 LEU A N     1 
ATOM   3230  C  CA    . LEU A 1 427 ? 171.560 160.363 168.463 1.00 17.24  ? 427 LEU A CA    1 
ATOM   3231  C  C     . LEU A 1 427 ? 172.694 161.369 168.310 1.00 10.97  ? 427 LEU A C     1 
ATOM   3232  O  O     . LEU A 1 427 ? 173.839 160.984 168.043 1.00 20.89  ? 427 LEU A O     1 
ATOM   3233  C  CB    . LEU A 1 427 ? 170.789 160.220 167.151 1.00 15.30  ? 427 LEU A CB    1 
ATOM   3234  C  CG    . LEU A 1 427 ? 169.713 159.134 167.112 1.00 22.29  ? 427 LEU A CG    1 
ATOM   3235  C  CD1   . LEU A 1 427 ? 168.741 159.391 165.973 1.00 16.88  ? 427 LEU A CD1   1 
ATOM   3236  C  CD2   . LEU A 1 427 ? 170.342 157.757 166.983 1.00 9.73   ? 427 LEU A CD2   1 
ATOM   3237  N  N     . VAL A 1 428 ? 172.396 162.661 168.464 1.00 12.37  ? 428 VAL A N     1 
ATOM   3238  C  CA    . VAL A 1 428 ? 173.418 163.691 168.285 1.00 15.58  ? 428 VAL A CA    1 
ATOM   3239  C  C     . VAL A 1 428 ? 174.507 163.552 169.342 1.00 17.73  ? 428 VAL A C     1 
ATOM   3240  O  O     . VAL A 1 428 ? 175.703 163.569 169.033 1.00 21.90  ? 428 VAL A O     1 
ATOM   3241  C  CB    . VAL A 1 428 ? 172.782 165.092 168.317 1.00 24.71  ? 428 VAL A CB    1 
ATOM   3242  C  CG1   . VAL A 1 428 ? 173.861 166.164 168.330 1.00 12.57  ? 428 VAL A CG1   1 
ATOM   3243  C  CG2   . VAL A 1 428 ? 171.850 165.281 167.133 1.00 12.55  ? 428 VAL A CG2   1 
ATOM   3244  N  N     . LEU A 1 429 ? 174.107 163.407 170.607 1.00 14.23  ? 429 LEU A N     1 
ATOM   3245  C  CA    . LEU A 1 429 ? 175.091 163.329 171.682 1.00 16.26  ? 429 LEU A CA    1 
ATOM   3246  C  C     . LEU A 1 429 ? 175.829 161.996 171.665 1.00 23.90  ? 429 LEU A C     1 
ATOM   3247  O  O     . LEU A 1 429 ? 177.056 161.959 171.813 1.00 19.90  ? 429 LEU A O     1 
ATOM   3248  C  CB    . LEU A 1 429 ? 174.410 163.555 173.030 1.00 19.03  ? 429 LEU A CB    1 
ATOM   3249  C  CG    . LEU A 1 429 ? 173.746 164.922 173.207 1.00 21.21  ? 429 LEU A CG    1 
ATOM   3250  C  CD1   . LEU A 1 429 ? 172.969 164.981 174.512 1.00 20.55  ? 429 LEU A CD1   1 
ATOM   3251  C  CD2   . LEU A 1 429 ? 174.780 166.036 173.140 1.00 17.79  ? 429 LEU A CD2   1 
ATOM   3252  N  N     . MET A 1 430 ? 175.102 160.890 171.490 1.00 23.69  ? 430 MET A N     1 
ATOM   3253  C  CA    . MET A 1 430 ? 175.748 159.583 171.443 1.00 22.55  ? 430 MET A CA    1 
ATOM   3254  C  C     . MET A 1 430 ? 176.598 159.429 170.188 1.00 24.08  ? 430 MET A C     1 
ATOM   3255  O  O     . MET A 1 430 ? 177.704 158.880 170.244 1.00 19.95  ? 430 MET A O     1 
ATOM   3256  C  CB    . MET A 1 430 ? 174.697 158.476 171.519 1.00 22.91  ? 430 MET A CB    1 
ATOM   3257  C  CG    . MET A 1 430 ? 174.295 158.100 172.934 1.00 29.33  ? 430 MET A CG    1 
ATOM   3258  S  SD    . MET A 1 430 ? 172.976 156.871 172.976 1.00 50.43  ? 430 MET A SD    1 
ATOM   3259  C  CE    . MET A 1 430 ? 173.923 155.354 173.003 1.00 32.96  ? 430 MET A CE    1 
ATOM   3260  N  N     . GLY A 1 431 ? 176.096 159.903 169.045 1.00 15.18  ? 431 GLY A N     1 
ATOM   3261  C  CA    . GLY A 1 431 ? 176.857 159.789 167.812 1.00 11.67  ? 431 GLY A CA    1 
ATOM   3262  C  C     . GLY A 1 431 ? 178.125 160.621 167.821 1.00 15.07  ? 431 GLY A C     1 
ATOM   3263  O  O     . GLY A 1 431 ? 179.186 160.153 167.400 1.00 24.02  ? 431 GLY A O     1 
ATOM   3264  N  N     . ALA A 1 432 ? 178.033 161.865 168.295 1.00 12.69  ? 432 ALA A N     1 
ATOM   3265  C  CA    . ALA A 1 432 ? 179.219 162.710 168.385 1.00 13.33  ? 432 ALA A CA    1 
ATOM   3266  C  C     . ALA A 1 432 ? 180.218 162.151 169.388 1.00 17.22  ? 432 ALA A C     1 
ATOM   3267  O  O     . ALA A 1 432 ? 181.432 162.205 169.159 1.00 18.23  ? 432 ALA A O     1 
ATOM   3268  C  CB    . ALA A 1 432 ? 178.825 164.139 168.757 1.00 6.43   ? 432 ALA A CB    1 
ATOM   3269  N  N     . ALA A 1 433 ? 179.727 161.616 170.509 1.00 17.96  ? 433 ALA A N     1 
ATOM   3270  C  CA    . ALA A 1 433 ? 180.623 161.031 171.501 1.00 20.66  ? 433 ALA A CA    1 
ATOM   3271  C  C     . ALA A 1 433 ? 181.379 159.840 170.928 1.00 21.13  ? 433 ALA A C     1 
ATOM   3272  O  O     . ALA A 1 433 ? 182.588 159.706 171.141 1.00 24.30  ? 433 ALA A O     1 
ATOM   3273  C  CB    . ALA A 1 433 ? 179.836 160.619 172.745 1.00 17.38  ? 433 ALA A CB    1 
ATOM   3274  N  N     . LEU A 1 434 ? 180.689 158.975 170.181 1.00 24.90  ? 434 LEU A N     1 
ATOM   3275  C  CA    . LEU A 1 434 ? 181.343 157.803 169.607 1.00 18.94  ? 434 LEU A CA    1 
ATOM   3276  C  C     . LEU A 1 434 ? 182.447 158.204 168.637 1.00 18.37  ? 434 LEU A C     1 
ATOM   3277  O  O     . LEU A 1 434 ? 183.507 157.567 168.592 1.00 21.84  ? 434 LEU A O     1 
ATOM   3278  C  CB    . LEU A 1 434 ? 180.311 156.915 168.910 1.00 23.29  ? 434 LEU A CB    1 
ATOM   3279  C  CG    . LEU A 1 434 ? 180.847 155.684 168.175 1.00 21.36  ? 434 LEU A CG    1 
ATOM   3280  C  CD1   . LEU A 1 434 ? 181.514 154.722 169.146 1.00 21.46  ? 434 LEU A CD1   1 
ATOM   3281  C  CD2   . LEU A 1 434 ? 179.735 154.988 167.406 1.00 24.31  ? 434 LEU A CD2   1 
ATOM   3282  N  N     . ALA A 1 435 ? 182.217 159.257 167.849 1.00 13.36  ? 435 ALA A N     1 
ATOM   3283  C  CA    . ALA A 1 435 ? 183.248 159.734 166.933 1.00 19.56  ? 435 ALA A CA    1 
ATOM   3284  C  C     . ALA A 1 435 ? 184.466 160.250 167.690 1.00 24.38  ? 435 ALA A C     1 
ATOM   3285  O  O     . ALA A 1 435 ? 185.607 160.032 167.268 1.00 26.65  ? 435 ALA A O     1 
ATOM   3286  C  CB    . ALA A 1 435 ? 182.678 160.822 166.024 1.00 15.09  ? 435 ALA A CB    1 
ATOM   3287  N  N     . MET A 1 436 ? 184.244 160.936 168.814 1.00 16.61  ? 436 MET A N     1 
ATOM   3288  C  CA    . MET A 1 436 ? 185.349 161.513 169.572 1.00 13.04  ? 436 MET A CA    1 
ATOM   3289  C  C     . MET A 1 436 ? 186.184 160.463 170.295 1.00 21.97  ? 436 MET A C     1 
ATOM   3290  O  O     . MET A 1 436 ? 187.335 160.744 170.644 1.00 31.36  ? 436 MET A O     1 
ATOM   3291  C  CB    . MET A 1 436 ? 184.819 162.535 170.579 1.00 25.02  ? 436 MET A CB    1 
ATOM   3292  C  CG    . MET A 1 436 ? 184.139 163.740 169.949 1.00 20.71  ? 436 MET A CG    1 
ATOM   3293  S  SD    . MET A 1 436 ? 185.138 164.529 168.672 1.00 31.45  ? 436 MET A SD    1 
ATOM   3294  C  CE    . MET A 1 436 ? 186.256 165.501 169.677 1.00 25.22  ? 436 MET A CE    1 
ATOM   3295  N  N     . MET A 1 437 ? 185.640 159.272 170.535 1.00 26.16  ? 437 MET A N     1 
ATOM   3296  C  CA    . MET A 1 437 ? 186.376 158.207 171.205 1.00 25.19  ? 437 MET A CA    1 
ATOM   3297  C  C     . MET A 1 437 ? 187.040 157.235 170.237 1.00 25.60  ? 437 MET A C     1 
ATOM   3298  O  O     . MET A 1 437 ? 187.646 156.257 170.686 1.00 39.23  ? 437 MET A O     1 
ATOM   3299  C  CB    . MET A 1 437 ? 185.452 157.432 172.151 1.00 26.42  ? 437 MET A CB    1 
ATOM   3300  C  CG    . MET A 1 437 ? 184.549 158.313 172.992 1.00 30.16  ? 437 MET A CG    1 
ATOM   3301  S  SD    . MET A 1 437 ? 183.299 157.393 173.909 1.00 45.80  ? 437 MET A SD    1 
ATOM   3302  C  CE    . MET A 1 437 ? 184.145 157.141 175.465 1.00 32.88  ? 437 MET A CE    1 
ATOM   3303  N  N     . THR A 1 438 ? 186.945 157.475 168.933 1.00 27.67  ? 438 THR A N     1 
ATOM   3304  C  CA    . THR A 1 438 ? 187.544 156.610 167.928 1.00 24.64  ? 438 THR A CA    1 
ATOM   3305  C  C     . THR A 1 438 ? 188.529 157.407 167.085 1.00 25.13  ? 438 THR A C     1 
ATOM   3306  O  O     . THR A 1 438 ? 188.314 158.594 166.818 1.00 28.23  ? 438 THR A O     1 
ATOM   3307  C  CB    . THR A 1 438 ? 186.478 155.981 167.024 1.00 22.02  ? 438 THR A CB    1 
ATOM   3308  O  OG1   . THR A 1 438 ? 185.700 157.013 166.406 1.00 29.77  ? 438 THR A OG1   1 
ATOM   3309  C  CG2   . THR A 1 438 ? 185.561 155.075 167.831 1.00 24.43  ? 438 THR A CG2   1 
ATOM   3310  N  N     . ASP A 1 439 ? 189.615 156.748 166.675 1.00 32.05  ? 439 ASP A N     1 
ATOM   3311  C  CA    . ASP A 1 439 ? 190.603 157.407 165.828 1.00 25.30  ? 439 ASP A CA    1 
ATOM   3312  C  C     . ASP A 1 439 ? 190.016 157.764 164.469 1.00 24.99  ? 439 ASP A C     1 
ATOM   3313  O  O     . ASP A 1 439 ? 190.320 158.827 163.917 1.00 28.22  ? 439 ASP A O     1 
ATOM   3314  C  CB    . ASP A 1 439 ? 191.834 156.515 165.665 1.00 25.30  ? 439 ASP A CB    1 
ATOM   3315  C  CG    . ASP A 1 439 ? 192.692 156.918 164.481 1.00 37.59  ? 439 ASP A CG    1 
ATOM   3316  O  OD1   . ASP A 1 439 ? 193.498 157.862 164.624 1.00 37.25  ? 439 ASP A OD1   1 
ATOM   3317  O  OD2   . ASP A 1 439 ? 192.560 156.293 163.408 1.00 39.98  ? 439 ASP A OD2   1 
ATOM   3318  N  N     . ALA A 1 440 ? 189.178 156.885 163.913 1.00 27.69  ? 440 ALA A N     1 
ATOM   3319  C  CA    . ALA A 1 440 ? 188.588 157.146 162.603 1.00 30.78  ? 440 ALA A CA    1 
ATOM   3320  C  C     . ALA A 1 440 ? 187.728 158.403 162.622 1.00 30.64  ? 440 ALA A C     1 
ATOM   3321  O  O     . ALA A 1 440 ? 187.774 159.210 161.685 1.00 35.08  ? 440 ALA A O     1 
ATOM   3322  C  CB    . ALA A 1 440 ? 187.767 155.940 162.148 1.00 23.35  ? 440 ALA A CB    1 
ATOM   3323  N  N     . GLY A 1 441 ? 186.930 158.584 163.675 1.00 25.56  ? 441 GLY A N     1 
ATOM   3324  C  CA    . GLY A 1 441 ? 186.125 159.790 163.780 1.00 18.39  ? 441 GLY A CA    1 
ATOM   3325  C  C     . GLY A 1 441 ? 186.960 161.042 163.970 1.00 24.20  ? 441 GLY A C     1 
ATOM   3326  O  O     . GLY A 1 441 ? 186.694 162.075 163.350 1.00 27.27  ? 441 GLY A O     1 
ATOM   3327  N  N     . ARG A 1 442 ? 187.981 160.968 164.827 1.00 30.88  ? 442 ARG A N     1 
ATOM   3328  C  CA    . ARG A 1 442 ? 188.790 162.147 165.123 1.00 21.16  ? 442 ARG A CA    1 
ATOM   3329  C  C     . ARG A 1 442 ? 189.671 162.536 163.941 1.00 22.87  ? 442 ARG A C     1 
ATOM   3330  O  O     . ARG A 1 442 ? 189.876 163.726 163.680 1.00 30.07  ? 442 ARG A O     1 
ATOM   3331  C  CB    . ARG A 1 442 ? 189.642 161.898 166.367 1.00 29.82  ? 442 ARG A CB    1 
ATOM   3332  C  CG    . ARG A 1 442 ? 188.884 162.038 167.676 1.00 24.64  ? 442 ARG A CG    1 
ATOM   3333  C  CD    . ARG A 1 442 ? 189.813 161.899 168.870 1.00 22.65  ? 442 ARG A CD    1 
ATOM   3334  N  NE    . ARG A 1 442 ? 190.720 160.766 168.730 1.00 29.93  ? 442 ARG A NE    1 
ATOM   3335  C  CZ    . ARG A 1 442 ? 190.650 159.657 169.453 1.00 25.21  ? 442 ARG A CZ    1 
ATOM   3336  N  NH1   . ARG A 1 442 ? 189.720 159.493 170.378 1.00 22.07  ? 442 ARG A NH1   1 
ATOM   3337  N  NH2   . ARG A 1 442 ? 191.536 158.688 169.242 1.00 28.73  ? 442 ARG A NH2   1 
ATOM   3338  N  N     . SER A 1 443 ? 190.203 161.548 163.217 1.00 27.52  ? 443 SER A N     1 
ATOM   3339  C  CA    . SER A 1 443 ? 191.116 161.835 162.116 1.00 22.16  ? 443 SER A CA    1 
ATOM   3340  C  C     . SER A 1 443 ? 190.430 162.530 160.947 1.00 22.59  ? 443 SER A C     1 
ATOM   3341  O  O     . SER A 1 443 ? 191.117 163.107 160.098 1.00 27.93  ? 443 SER A O     1 
ATOM   3342  C  CB    . SER A 1 443 ? 191.780 160.545 161.633 1.00 19.15  ? 443 SER A CB    1 
ATOM   3343  O  OG    . SER A 1 443 ? 190.816 159.625 161.151 1.00 27.50  ? 443 SER A OG    1 
ATOM   3344  N  N     . ALA A 1 444 ? 189.098 162.489 160.880 1.00 17.41  ? 444 ALA A N     1 
ATOM   3345  C  CA    . ALA A 1 444 ? 188.377 163.129 159.788 1.00 21.00  ? 444 ALA A CA    1 
ATOM   3346  C  C     . ALA A 1 444 ? 188.365 164.648 159.893 1.00 23.66  ? 444 ALA A C     1 
ATOM   3347  O  O     . ALA A 1 444 ? 187.959 165.312 158.933 1.00 23.74  ? 444 ALA A O     1 
ATOM   3348  C  CB    . ALA A 1 444 ? 186.941 162.606 159.731 1.00 17.63  ? 444 ALA A CB    1 
ATOM   3349  N  N     . MET A 1 445 ? 188.789 165.208 161.022 1.00 23.92  ? 445 MET A N     1 
ATOM   3350  C  CA    . MET A 1 445 ? 188.790 166.653 161.193 1.00 19.97  ? 445 MET A CA    1 
ATOM   3351  C  C     . MET A 1 445 ? 189.808 167.310 160.269 1.00 26.03  ? 445 MET A C     1 
ATOM   3352  O  O     . MET A 1 445 ? 190.860 166.744 159.960 1.00 31.82  ? 445 MET A O     1 
ATOM   3353  C  CB    . MET A 1 445 ? 189.102 167.020 162.644 1.00 22.77  ? 445 MET A CB    1 
ATOM   3354  C  CG    . MET A 1 445 ? 188.122 166.466 163.661 1.00 24.88  ? 445 MET A CG    1 
ATOM   3355  S  SD    . MET A 1 445 ? 188.801 166.518 165.330 1.00 35.25  ? 445 MET A SD    1 
ATOM   3356  C  CE    . MET A 1 445 ? 187.310 166.450 166.316 1.00 22.23  ? 445 MET A CE    1 
ATOM   3357  N  N     . LEU A 1 446 ? 189.482 168.521 159.823 1.00 23.19  ? 446 LEU A N     1 
ATOM   3358  C  CA    . LEU A 1 446 ? 190.392 169.333 159.026 1.00 22.04  ? 446 LEU A CA    1 
ATOM   3359  C  C     . LEU A 1 446 ? 191.016 170.470 159.822 1.00 14.29  ? 446 LEU A C     1 
ATOM   3360  O  O     . LEU A 1 446 ? 192.226 170.696 159.727 1.00 28.33  ? 446 LEU A O     1 
ATOM   3361  C  CB    . LEU A 1 446 ? 189.666 169.908 157.806 1.00 16.12  ? 446 LEU A CB    1 
ATOM   3362  C  CG    . LEU A 1 446 ? 190.468 170.908 156.970 1.00 20.60  ? 446 LEU A CG    1 
ATOM   3363  C  CD1   . LEU A 1 446 ? 191.580 170.201 156.212 1.00 20.65  ? 446 LEU A CD1   1 
ATOM   3364  C  CD2   . LEU A 1 446 ? 189.566 171.674 156.015 1.00 20.60  ? 446 LEU A CD2   1 
ATOM   3365  N  N     . ASN A 1 447 ? 190.217 171.188 160.610 1.00 8.06   ? 447 ASN A N     1 
ATOM   3366  C  CA    . ASN A 1 447 ? 190.695 172.304 161.409 1.00 16.46  ? 447 ASN A CA    1 
ATOM   3367  C  C     . ASN A 1 447 ? 191.041 171.847 162.822 1.00 15.48  ? 447 ASN A C     1 
ATOM   3368  O  O     . ASN A 1 447 ? 190.439 170.902 163.342 1.00 28.92  ? 447 ASN A O     1 
ATOM   3369  C  CB    . ASN A 1 447 ? 189.639 173.404 161.470 1.00 17.89  ? 447 ASN A CB    1 
ATOM   3370  C  CG    . ASN A 1 447 ? 189.337 173.997 160.108 1.00 14.97  ? 447 ASN A CG    1 
ATOM   3371  O  OD1   . ASN A 1 447 ? 190.142 174.743 159.552 1.00 23.88  ? 447 ASN A OD1   1 
ATOM   3372  N  ND2   . ASN A 1 447 ? 188.173 173.666 159.563 1.00 13.68  ? 447 ASN A ND2   1 
ATOM   3373  N  N     . PRO A 1 448 ? 192.018 172.491 163.463 1.00 25.86  ? 448 PRO A N     1 
ATOM   3374  C  CA    . PRO A 1 448 ? 192.380 172.105 164.832 1.00 21.51  ? 448 PRO A CA    1 
ATOM   3375  C  C     . PRO A 1 448 ? 191.607 172.883 165.886 1.00 23.59  ? 448 PRO A C     1 
ATOM   3376  O  O     . PRO A 1 448 ? 190.810 173.767 165.559 1.00 31.38  ? 448 PRO A O     1 
ATOM   3377  C  CB    . PRO A 1 448 ? 193.877 172.421 164.889 1.00 18.07  ? 448 PRO A CB    1 
ATOM   3378  C  CG    . PRO A 1 448 ? 194.032 173.594 163.964 1.00 18.55  ? 448 PRO A CG    1 
ATOM   3379  C  CD    . PRO A 1 448 ? 192.937 173.506 162.917 1.00 21.36  ? 448 PRO A CD    1 
ATOM   3380  N  N     . GLY A 1 449 ? 191.837 172.556 167.155 1.00 25.96  ? 449 GLY A N     1 
ATOM   3381  C  CA    . GLY A 1 449 ? 191.246 173.281 168.254 1.00 22.99  ? 449 GLY A CA    1 
ATOM   3382  C  C     . GLY A 1 449 ? 189.765 173.010 168.417 1.00 24.51  ? 449 GLY A C     1 
ATOM   3383  O  O     . GLY A 1 449 ? 189.231 172.017 167.915 1.00 24.40  ? 449 GLY A O     1 
ATOM   3384  N  N     . PRO A 1 450 ? 189.071 173.901 169.131 1.00 28.10  ? 450 PRO A N     1 
ATOM   3385  C  CA    . PRO A 1 450 ? 187.626 173.703 169.344 1.00 19.99  ? 450 PRO A CA    1 
ATOM   3386  C  C     . PRO A 1 450 ? 186.825 173.630 168.056 1.00 19.15  ? 450 PRO A C     1 
ATOM   3387  O  O     . PRO A 1 450 ? 185.790 172.953 168.022 1.00 18.66  ? 450 PRO A O     1 
ATOM   3388  C  CB    . PRO A 1 450 ? 187.216 174.918 170.190 1.00 17.86  ? 450 PRO A CB    1 
ATOM   3389  C  CG    . PRO A 1 450 ? 188.474 175.500 170.719 1.00 21.46  ? 450 PRO A CG    1 
ATOM   3390  C  CD    . PRO A 1 450 ? 189.604 175.073 169.844 1.00 20.75  ? 450 PRO A CD    1 
ATOM   3391  N  N     . HIS A 1 451 ? 187.264 174.314 166.996 1.00 12.82  ? 451 HIS A N     1 
ATOM   3392  C  CA    . HIS A 1 451 ? 186.551 174.235 165.725 1.00 12.46  ? 451 HIS A CA    1 
ATOM   3393  C  C     . HIS A 1 451 ? 186.599 172.830 165.141 1.00 17.99  ? 451 HIS A C     1 
ATOM   3394  O  O     . HIS A 1 451 ? 185.681 172.430 164.416 1.00 17.10  ? 451 HIS A O     1 
ATOM   3395  C  CB    . HIS A 1 451 ? 187.126 175.244 164.731 1.00 5.47   ? 451 HIS A CB    1 
ATOM   3396  C  CG    . HIS A 1 451 ? 186.227 175.520 163.566 1.00 14.19  ? 451 HIS A CG    1 
ATOM   3397  N  ND1   . HIS A 1 451 ? 185.447 176.652 163.479 1.00 22.97  ? 451 HIS A ND1   1 
ATOM   3398  C  CD2   . HIS A 1 451 ? 185.984 174.808 162.440 1.00 5.45   ? 451 HIS A CD2   1 
ATOM   3399  C  CE1   . HIS A 1 451 ? 184.763 176.627 162.350 1.00 11.82  ? 451 HIS A CE1   1 
ATOM   3400  N  NE2   . HIS A 1 451 ? 185.070 175.519 161.701 1.00 22.90  ? 451 HIS A NE2   1 
ATOM   3401  N  N     . GLY A 1 452 ? 187.655 172.071 165.439 1.00 17.17  ? 452 GLY A N     1 
ATOM   3402  C  CA    . GLY A 1 452 ? 187.708 170.691 164.986 1.00 8.79   ? 452 GLY A CA    1 
ATOM   3403  C  C     . GLY A 1 452 ? 186.593 169.846 165.570 1.00 10.90  ? 452 GLY A C     1 
ATOM   3404  O  O     . GLY A 1 452 ? 185.989 169.029 164.873 1.00 16.45  ? 452 GLY A O     1 
ATOM   3405  N  N     . PHE A 1 453 ? 186.305 170.034 166.861 1.00 15.38  ? 453 PHE A N     1 
ATOM   3406  C  CA    . PHE A 1 453 ? 185.166 169.360 167.472 1.00 14.11  ? 453 PHE A CA    1 
ATOM   3407  C  C     . PHE A 1 453 ? 183.849 169.837 166.874 1.00 11.82  ? 453 PHE A C     1 
ATOM   3408  O  O     . PHE A 1 453 ? 182.896 169.056 166.773 1.00 17.71  ? 453 PHE A O     1 
ATOM   3409  C  CB    . PHE A 1 453 ? 185.180 169.579 168.986 1.00 7.22   ? 453 PHE A CB    1 
ATOM   3410  C  CG    . PHE A 1 453 ? 183.912 169.160 169.675 1.00 8.54   ? 453 PHE A CG    1 
ATOM   3411  C  CD1   . PHE A 1 453 ? 183.476 167.846 169.617 1.00 14.19  ? 453 PHE A CD1   1 
ATOM   3412  C  CD2   . PHE A 1 453 ? 183.158 170.080 170.384 1.00 8.46   ? 453 PHE A CD2   1 
ATOM   3413  C  CE1   . PHE A 1 453 ? 182.310 167.458 170.250 1.00 15.28  ? 453 PHE A CE1   1 
ATOM   3414  C  CE2   . PHE A 1 453 ? 181.991 169.699 171.021 1.00 14.70  ? 453 PHE A CE2   1 
ATOM   3415  C  CZ    . PHE A 1 453 ? 181.567 168.387 170.954 1.00 12.64  ? 453 PHE A CZ    1 
ATOM   3416  N  N     . SER A 1 454 ? 183.778 171.109 166.470 1.00 7.58   ? 454 SER A N     1 
ATOM   3417  C  CA    . SER A 1 454 ? 182.565 171.623 165.844 1.00 17.97  ? 454 SER A CA    1 
ATOM   3418  C  C     . SER A 1 454 ? 182.259 170.904 164.537 1.00 6.60   ? 454 SER A C     1 
ATOM   3419  O  O     . SER A 1 454 ? 181.086 170.730 164.187 1.00 25.30  ? 454 SER A O     1 
ATOM   3420  C  CB    . SER A 1 454 ? 182.692 173.127 165.602 1.00 14.57  ? 454 SER A CB    1 
ATOM   3421  O  OG    . SER A 1 454 ? 182.937 173.822 166.812 1.00 24.26  ? 454 SER A OG    1 
ATOM   3422  N  N     . GLU A 1 455 ? 183.292 170.485 163.801 1.00 8.91   ? 455 GLU A N     1 
ATOM   3423  C  CA    . GLU A 1 455 ? 183.069 169.733 162.570 1.00 13.87  ? 455 GLU A CA    1 
ATOM   3424  C  C     . GLU A 1 455 ? 182.375 168.406 162.853 1.00 15.10  ? 455 GLU A C     1 
ATOM   3425  O  O     . GLU A 1 455 ? 181.446 168.017 162.136 1.00 12.75  ? 455 GLU A O     1 
ATOM   3426  C  CB    . GLU A 1 455 ? 184.396 169.496 161.848 1.00 18.32  ? 455 GLU A CB    1 
ATOM   3427  C  CG    . GLU A 1 455 ? 184.985 170.730 161.186 1.00 16.24  ? 455 GLU A CG    1 
ATOM   3428  C  CD    . GLU A 1 455 ? 186.415 170.515 160.729 1.00 27.71  ? 455 GLU A CD    1 
ATOM   3429  O  OE1   . GLU A 1 455 ? 187.270 170.190 161.578 1.00 32.84  ? 455 GLU A OE1   1 
ATOM   3430  O  OE2   . GLU A 1 455 ? 186.686 170.667 159.519 1.00 18.64  ? 455 GLU A OE2   1 
ATOM   3431  N  N     . VAL A 1 456 ? 182.817 167.697 163.894 1.00 8.03   ? 456 VAL A N     1 
ATOM   3432  C  CA    . VAL A 1 456 ? 182.195 166.426 164.251 1.00 15.27  ? 456 VAL A CA    1 
ATOM   3433  C  C     . VAL A 1 456 ? 180.781 166.649 164.773 1.00 10.81  ? 456 VAL A C     1 
ATOM   3434  O  O     . VAL A 1 456 ? 179.845 165.935 164.395 1.00 17.18  ? 456 VAL A O     1 
ATOM   3435  C  CB    . VAL A 1 456 ? 183.070 165.679 165.275 1.00 11.90  ? 456 VAL A CB    1 
ATOM   3436  C  CG1   . VAL A 1 456 ? 182.271 164.588 165.972 1.00 7.32   ? 456 VAL A CG1   1 
ATOM   3437  C  CG2   . VAL A 1 456 ? 184.300 165.097 164.597 1.00 14.82  ? 456 VAL A CG2   1 
ATOM   3438  N  N     . LEU A 1 457 ? 180.603 167.645 165.644 1.00 12.38  ? 457 LEU A N     1 
ATOM   3439  C  CA    . LEU A 1 457 ? 179.285 167.917 166.208 1.00 10.40  ? 457 LEU A CA    1 
ATOM   3440  C  C     . LEU A 1 457 ? 178.294 168.334 165.128 1.00 14.54  ? 457 LEU A C     1 
ATOM   3441  O  O     . LEU A 1 457 ? 177.129 167.921 165.151 1.00 15.86  ? 457 LEU A O     1 
ATOM   3442  C  CB    . LEU A 1 457 ? 179.392 168.994 167.287 1.00 10.80  ? 457 LEU A CB    1 
ATOM   3443  C  CG    . LEU A 1 457 ? 178.118 169.314 168.072 1.00 17.99  ? 457 LEU A CG    1 
ATOM   3444  C  CD1   . LEU A 1 457 ? 177.588 168.069 168.763 1.00 8.42   ? 457 LEU A CD1   1 
ATOM   3445  C  CD2   . LEU A 1 457 ? 178.376 170.424 169.080 1.00 15.55  ? 457 LEU A CD2   1 
ATOM   3446  N  N     . TYR A 1 458 ? 178.738 169.159 164.176 1.00 7.52   ? 458 TYR A N     1 
ATOM   3447  C  CA    . TYR A 1 458 ? 177.858 169.590 163.094 1.00 13.58  ? 458 TYR A CA    1 
ATOM   3448  C  C     . TYR A 1 458 ? 177.423 168.412 162.230 1.00 13.79  ? 458 TYR A C     1 
ATOM   3449  O  O     . TYR A 1 458 ? 176.259 168.331 161.821 1.00 18.25  ? 458 TYR A O     1 
ATOM   3450  C  CB    . TYR A 1 458 ? 178.559 170.650 162.243 1.00 4.96   ? 458 TYR A CB    1 
ATOM   3451  C  CG    . TYR A 1 458 ? 177.631 171.467 161.372 1.00 13.96  ? 458 TYR A CG    1 
ATOM   3452  C  CD1   . TYR A 1 458 ? 177.241 171.011 160.119 1.00 9.81   ? 458 TYR A CD1   1 
ATOM   3453  C  CD2   . TYR A 1 458 ? 177.153 172.700 161.798 1.00 6.64   ? 458 TYR A CD2   1 
ATOM   3454  C  CE1   . TYR A 1 458 ? 176.397 171.756 159.318 1.00 8.95   ? 458 TYR A CE1   1 
ATOM   3455  C  CE2   . TYR A 1 458 ? 176.309 173.452 161.003 1.00 9.32   ? 458 TYR A CE2   1 
ATOM   3456  C  CZ    . TYR A 1 458 ? 175.934 172.975 159.764 1.00 13.12  ? 458 TYR A CZ    1 
ATOM   3457  O  OH    . TYR A 1 458 ? 175.094 173.719 158.970 1.00 18.39  ? 458 TYR A OH    1 
ATOM   3458  N  N     . ALA A 1 459 ? 178.347 167.495 161.934 1.00 7.96   ? 459 ALA A N     1 
ATOM   3459  C  CA    . ALA A 1 459 ? 178.027 166.368 161.062 1.00 7.11   ? 459 ALA A CA    1 
ATOM   3460  C  C     . ALA A 1 459 ? 176.960 165.472 161.679 1.00 10.63  ? 459 ALA A C     1 
ATOM   3461  O  O     . ALA A 1 459 ? 176.002 165.073 161.006 1.00 12.51  ? 459 ALA A O     1 
ATOM   3462  C  CB    . ALA A 1 459 ? 179.293 165.567 160.758 1.00 8.22   ? 459 ALA A CB    1 
ATOM   3463  N  N     . VAL A 1 460 ? 177.108 165.145 162.964 1.00 16.86  ? 460 VAL A N     1 
ATOM   3464  C  CA    . VAL A 1 460 ? 176.146 164.262 163.618 1.00 10.37  ? 460 VAL A CA    1 
ATOM   3465  C  C     . VAL A 1 460 ? 174.810 164.970 163.809 1.00 8.78   ? 460 VAL A C     1 
ATOM   3466  O  O     . VAL A 1 460 ? 173.744 164.366 163.644 1.00 20.98  ? 460 VAL A O     1 
ATOM   3467  C  CB    . VAL A 1 460 ? 176.713 163.745 164.952 1.00 17.16  ? 460 VAL A CB    1 
ATOM   3468  C  CG1   . VAL A 1 460 ? 175.778 162.712 165.560 1.00 10.67  ? 460 VAL A CG1   1 
ATOM   3469  C  CG2   . VAL A 1 460 ? 178.098 163.154 164.744 1.00 16.59  ? 460 VAL A CG2   1 
ATOM   3470  N  N     . SER A 1 461 ? 174.844 166.256 164.166 1.00 14.55  ? 461 SER A N     1 
ATOM   3471  C  CA    . SER A 1 461 ? 173.605 167.009 164.333 1.00 15.68  ? 461 SER A CA    1 
ATOM   3472  C  C     . SER A 1 461 ? 172.839 167.113 163.020 1.00 16.79  ? 461 SER A C     1 
ATOM   3473  O  O     . SER A 1 461 ? 171.610 166.985 162.997 1.00 8.22   ? 461 SER A O     1 
ATOM   3474  C  CB    . SER A 1 461 ? 173.907 168.401 164.888 1.00 2.91   ? 461 SER A CB    1 
ATOM   3475  O  OG    . SER A 1 461 ? 174.823 168.334 165.967 1.00 24.37  ? 461 SER A OG    1 
ATOM   3476  N  N     . SER A 1 462 ? 173.551 167.350 161.917 1.00 13.18  ? 462 SER A N     1 
ATOM   3477  C  CA    . SER A 1 462 ? 172.896 167.449 160.616 1.00 14.37  ? 462 SER A CA    1 
ATOM   3478  C  C     . SER A 1 462 ? 172.285 166.119 160.193 1.00 14.11  ? 462 SER A C     1 
ATOM   3479  O  O     . SER A 1 462 ? 171.158 166.082 159.685 1.00 5.65   ? 462 SER A O     1 
ATOM   3480  C  CB    . SER A 1 462 ? 173.895 167.937 159.570 1.00 8.32   ? 462 SER A CB    1 
ATOM   3481  O  OG    . SER A 1 462 ? 173.240 168.330 158.378 1.00 28.58  ? 462 SER A OG    1 
ATOM   3482  N  N     . ALA A 1 463 ? 173.014 165.017 160.389 1.00 8.21   ? 463 ALA A N     1 
ATOM   3483  C  CA    . ALA A 1 463 ? 172.520 163.715 159.950 1.00 14.44  ? 463 ALA A CA    1 
ATOM   3484  C  C     . ALA A 1 463 ? 171.331 163.256 160.785 1.00 11.40  ? 463 ALA A C     1 
ATOM   3485  O  O     . ALA A 1 463 ? 170.337 162.763 160.239 1.00 14.25  ? 463 ALA A O     1 
ATOM   3486  C  CB    . ALA A 1 463 ? 173.645 162.683 160.004 1.00 8.43   ? 463 ALA A CB    1 
ATOM   3487  N  N     . ALA A 1 464 ? 171.412 163.408 162.109 1.00 6.15   ? 464 ALA A N     1 
ATOM   3488  C  CA    . ALA A 1 464 ? 170.326 162.956 162.972 1.00 12.37  ? 464 ALA A CA    1 
ATOM   3489  C  C     . ALA A 1 464 ? 169.055 163.764 162.750 1.00 13.36  ? 464 ALA A C     1 
ATOM   3490  O  O     . ALA A 1 464 ? 167.950 163.220 162.856 1.00 19.01  ? 464 ALA A O     1 
ATOM   3491  C  CB    . ALA A 1 464 ? 170.753 163.027 164.437 1.00 17.69  ? 464 ALA A CB    1 
ATOM   3492  N  N     . ASN A 1 465 ? 169.187 165.051 162.441 1.00 10.75  ? 465 ASN A N     1 
ATOM   3493  C  CA    . ASN A 1 465 ? 168.044 165.916 162.188 1.00 7.12   ? 465 ASN A CA    1 
ATOM   3494  C  C     . ASN A 1 465 ? 167.618 165.922 160.727 1.00 10.92  ? 465 ASN A C     1 
ATOM   3495  O  O     . ASN A 1 465 ? 166.706 166.675 160.369 1.00 18.04  ? 465 ASN A O     1 
ATOM   3496  C  CB    . ASN A 1 465 ? 168.357 167.344 162.638 1.00 13.44  ? 465 ASN A CB    1 
ATOM   3497  C  CG    . ASN A 1 465 ? 168.248 167.515 164.134 1.00 16.69  ? 465 ASN A CG    1 
ATOM   3498  O  OD1   . ASN A 1 465 ? 167.163 167.747 164.665 1.00 30.91  ? 465 ASN A OD1   1 
ATOM   3499  N  ND2   . ASN A 1 465 ? 169.375 167.399 164.827 1.00 10.35  ? 465 ASN A ND2   1 
ATOM   3500  N  N     . ASN A 1 466 ? 168.258 165.109 159.885 1.00 7.90   ? 466 ASN A N     1 
ATOM   3501  C  CA    . ASN A 1 466 ? 167.927 165.013 158.463 1.00 13.25  ? 466 ASN A CA    1 
ATOM   3502  C  C     . ASN A 1 466 ? 168.046 166.367 157.765 1.00 10.37  ? 466 ASN A C     1 
ATOM   3503  O  O     . ASN A 1 466 ? 167.217 166.730 156.928 1.00 16.10  ? 466 ASN A O     1 
ATOM   3504  C  CB    . ASN A 1 466 ? 166.534 164.411 158.258 1.00 8.20   ? 466 ASN A CB    1 
ATOM   3505  C  CG    . ASN A 1 466 ? 166.356 163.092 158.989 1.00 14.14  ? 466 ASN A CG    1 
ATOM   3506  O  OD1   . ASN A 1 466 ? 165.513 162.972 159.877 1.00 23.03  ? 466 ASN A OD1   1 
ATOM   3507  N  ND2   . ASN A 1 466 ? 167.152 162.096 158.618 1.00 7.20   ? 466 ASN A ND2   1 
ATOM   3508  N  N     . ASN A 1 467 ? 169.090 167.121 158.110 1.00 14.88  ? 467 ASN A N     1 
ATOM   3509  C  CA    . ASN A 1 467 ? 169.345 168.411 157.476 1.00 10.38  ? 467 ASN A CA    1 
ATOM   3510  C  C     . ASN A 1 467 ? 170.176 168.249 156.205 1.00 0.50   ? 467 ASN A C     1 
ATOM   3511  O  O     . ASN A 1 467 ? 169.744 168.646 155.119 1.00 17.87  ? 467 ASN A O     1 
ATOM   3512  C  CB    . ASN A 1 467 ? 170.043 169.355 158.462 1.00 6.72   ? 467 ASN A CB    1 
ATOM   3513  C  CG    . ASN A 1 467 ? 170.181 170.764 157.920 1.00 13.53  ? 467 ASN A CG    1 
ATOM   3514  O  OD1   . ASN A 1 467 ? 171.135 171.077 157.209 1.00 11.26  ? 467 ASN A OD1   1 
ATOM   3515  N  ND2   . ASN A 1 467 ? 169.226 171.624 158.253 1.00 7.93   ? 467 ASN A ND2   1 
ATOM   3516  N  N     . GLY A 1 468 ? 171.365 167.663 156.326 1.00 8.22   ? 468 GLY A N     1 
ATOM   3517  C  CA    . GLY A 1 468 ? 172.215 167.375 155.194 1.00 19.77  ? 468 GLY A CA    1 
ATOM   3518  C  C     . GLY A 1 468 ? 173.355 168.350 154.979 1.00 1.55   ? 468 GLY A C     1 
ATOM   3519  O  O     . GLY A 1 468 ? 174.315 168.006 154.281 1.00 20.99  ? 468 GLY A O     1 
ATOM   3520  N  N     . SER A 1 469 ? 173.279 169.549 155.550 1.00 14.19  ? 469 SER A N     1 
ATOM   3521  C  CA    . SER A 1 469 ? 174.393 170.480 155.454 1.00 14.02  ? 469 SER A CA    1 
ATOM   3522  C  C     . SER A 1 469 ? 175.574 169.967 156.272 1.00 10.30  ? 469 SER A C     1 
ATOM   3523  O  O     . SER A 1 469 ? 175.426 169.136 157.170 1.00 21.03  ? 469 SER A O     1 
ATOM   3524  C  CB    . SER A 1 469 ? 173.980 171.873 155.932 1.00 8.21   ? 469 SER A CB    1 
ATOM   3525  O  OG    . SER A 1 469 ? 173.645 171.864 157.308 1.00 33.28  ? 469 SER A OG    1 
ATOM   3526  N  N     . ALA A 1 470 ? 176.764 170.464 155.949 1.00 3.22   ? 470 ALA A N     1 
ATOM   3527  C  CA    . ALA A 1 470 ? 177.961 169.934 156.578 1.00 21.86  ? 470 ALA A CA    1 
ATOM   3528  C  C     . ALA A 1 470 ? 179.004 171.024 156.756 1.00 18.70  ? 470 ALA A C     1 
ATOM   3529  O  O     . ALA A 1 470 ? 179.042 172.003 156.007 1.00 30.99  ? 470 ALA A O     1 
ATOM   3530  C  CB    . ALA A 1 470 ? 178.560 168.787 155.755 1.00 19.00  ? 470 ALA A CB    1 
ATOM   3531  N  N     . PHE A 1 471 ? 179.846 170.839 157.769 1.00 32.79  ? 471 PHE A N     1 
ATOM   3532  C  CA    . PHE A 1 471 ? 181.154 171.483 157.815 1.00 14.27  ? 471 PHE A CA    1 
ATOM   3533  C  C     . PHE A 1 471 ? 182.043 170.672 156.884 1.00 13.85  ? 471 PHE A C     1 
ATOM   3534  O  O     . PHE A 1 471 ? 182.598 169.643 157.275 1.00 30.00  ? 471 PHE A O     1 
ATOM   3535  C  CB    . PHE A 1 471 ? 181.700 171.514 159.238 1.00 21.06  ? 471 PHE A CB    1 
ATOM   3536  C  CG    . PHE A 1 471 ? 181.264 172.713 160.035 1.00 13.95  ? 471 PHE A CG    1 
ATOM   3537  C  CD1   . PHE A 1 471 ? 180.127 173.423 159.685 1.00 16.82  ? 471 PHE A CD1   1 
ATOM   3538  C  CD2   . PHE A 1 471 ? 181.989 173.125 161.141 1.00 19.70  ? 471 PHE A CD2   1 
ATOM   3539  C  CE1   . PHE A 1 471 ? 179.726 174.524 160.419 1.00 17.48  ? 471 PHE A CE1   1 
ATOM   3540  C  CE2   . PHE A 1 471 ? 181.593 174.224 161.880 1.00 16.48  ? 471 PHE A CE2   1 
ATOM   3541  C  CZ    . PHE A 1 471 ? 180.460 174.924 161.518 1.00 19.02  ? 471 PHE A CZ    1 
ATOM   3542  N  N     . ALA A 1 472 ? 182.175 171.133 155.639 1.00 17.96  ? 472 ALA A N     1 
ATOM   3543  C  CA    . ALA A 1 472 ? 182.694 170.295 154.564 1.00 20.10  ? 472 ALA A CA    1 
ATOM   3544  C  C     . ALA A 1 472 ? 184.159 169.919 154.744 1.00 12.90  ? 472 ALA A C     1 
ATOM   3545  O  O     . ALA A 1 472 ? 184.649 169.057 154.007 1.00 24.27  ? 472 ALA A O     1 
ATOM   3546  C  CB    . ALA A 1 472 ? 182.497 170.992 153.217 1.00 24.35  ? 472 ALA A CB    1 
ATOM   3547  N  N     . GLY A 1 473 ? 184.866 170.540 155.690 1.00 14.53  ? 473 GLY A N     1 
ATOM   3548  C  CA    . GLY A 1 473 ? 186.238 170.142 155.954 1.00 13.86  ? 473 GLY A CA    1 
ATOM   3549  C  C     . GLY A 1 473 ? 186.363 168.714 156.447 1.00 13.33  ? 473 GLY A C     1 
ATOM   3550  O  O     . GLY A 1 473 ? 187.393 168.069 156.236 1.00 29.94  ? 473 GLY A O     1 
ATOM   3551  N  N     . LEU A 1 474 ? 185.329 168.203 157.111 1.00 10.46  ? 474 LEU A N     1 
ATOM   3552  C  CA    . LEU A 1 474 ? 185.351 166.829 157.594 1.00 21.67  ? 474 LEU A CA    1 
ATOM   3553  C  C     . LEU A 1 474 ? 185.344 165.846 156.429 1.00 23.68  ? 474 LEU A C     1 
ATOM   3554  O  O     . LEU A 1 474 ? 184.597 166.009 155.460 1.00 30.11  ? 474 LEU A O     1 
ATOM   3555  C  CB    . LEU A 1 474 ? 184.153 166.569 158.507 1.00 20.37  ? 474 LEU A CB    1 
ATOM   3556  C  CG    . LEU A 1 474 ? 184.227 165.329 159.401 1.00 18.17  ? 474 LEU A CG    1 
ATOM   3557  C  CD1   . LEU A 1 474 ? 184.963 165.638 160.695 1.00 19.61  ? 474 LEU A CD1   1 
ATOM   3558  C  CD2   . LEU A 1 474 ? 182.834 164.790 159.689 1.00 15.81  ? 474 LEU A CD2   1 
ATOM   3559  N  N     . SER A 1 475 ? 186.185 164.818 156.530 1.00 14.42  ? 475 SER A N     1 
ATOM   3560  C  CA    . SER A 1 475 ? 186.282 163.770 155.515 1.00 18.58  ? 475 SER A CA    1 
ATOM   3561  C  C     . SER A 1 475 ? 185.434 162.593 155.985 1.00 23.62  ? 475 SER A C     1 
ATOM   3562  O  O     . SER A 1 475 ? 185.893 161.731 156.735 1.00 27.00  ? 475 SER A O     1 
ATOM   3563  C  CB    . SER A 1 475 ? 187.734 163.368 155.284 1.00 20.96  ? 475 SER A CB    1 
ATOM   3564  O  OG    . SER A 1 475 ? 188.498 164.462 154.808 1.00 29.72  ? 475 SER A OG    1 
ATOM   3565  N  N     . ALA A 1 476 ? 184.182 162.558 155.532 1.00 15.71  ? 476 ALA A N     1 
ATOM   3566  C  CA    . ALA A 1 476 ? 183.222 161.553 155.965 1.00 19.31  ? 476 ALA A CA    1 
ATOM   3567  C  C     . ALA A 1 476 ? 183.134 160.358 155.026 1.00 14.14  ? 476 ALA A C     1 
ATOM   3568  O  O     . ALA A 1 476 ? 182.294 159.480 155.245 1.00 29.25  ? 476 ALA A O     1 
ATOM   3569  C  CB    . ALA A 1 476 ? 181.836 162.186 156.125 1.00 23.13  ? 476 ALA A CB    1 
ATOM   3570  N  N     . ASN A 1 477 ? 183.971 160.298 153.992 1.00 23.13  ? 477 ASN A N     1 
ATOM   3571  C  CA    . ASN A 1 477 ? 183.946 159.184 153.043 1.00 18.72  ? 477 ASN A CA    1 
ATOM   3572  C  C     . ASN A 1 477 ? 184.791 158.017 153.559 1.00 19.99  ? 477 ASN A C     1 
ATOM   3573  O  O     . ASN A 1 477 ? 185.801 157.624 152.977 1.00 31.95  ? 477 ASN A O     1 
ATOM   3574  C  CB    . ASN A 1 477 ? 184.417 159.647 151.669 1.00 26.21  ? 477 ASN A CB    1 
ATOM   3575  C  CG    . ASN A 1 477 ? 183.879 158.780 150.547 1.00 28.32  ? 477 ASN A CG    1 
ATOM   3576  O  OD1   . ASN A 1 477 ? 183.210 157.776 150.789 1.00 27.39  ? 477 ASN A OD1   1 
ATOM   3577  N  ND2   . ASN A 1 477 ? 184.168 159.166 149.310 1.00 33.99  ? 477 ASN A ND2   1 
ATOM   3578  N  N     . SER A 1 478 ? 184.350 157.466 154.685 1.00 20.57  ? 478 SER A N     1 
ATOM   3579  C  CA    . SER A 1 478 ? 184.976 156.313 155.310 1.00 18.88  ? 478 SER A CA    1 
ATOM   3580  C  C     . SER A 1 478 ? 183.886 155.359 155.773 1.00 23.18  ? 478 SER A C     1 
ATOM   3581  O  O     . SER A 1 478 ? 182.759 155.790 156.047 1.00 24.07  ? 478 SER A O     1 
ATOM   3582  C  CB    . SER A 1 478 ? 185.856 156.721 156.503 1.00 25.21  ? 478 SER A CB    1 
ATOM   3583  O  OG    . SER A 1 478 ? 185.070 157.005 157.647 1.00 28.70  ? 478 SER A OG    1 
ATOM   3584  N  N     . PRO A 1 479 ? 184.186 154.060 155.858 1.00 24.93  ? 479 PRO A N     1 
ATOM   3585  C  CA    . PRO A 1 479 ? 183.161 153.107 156.319 1.00 17.05  ? 479 PRO A CA    1 
ATOM   3586  C  C     . PRO A 1 479 ? 182.622 153.418 157.704 1.00 15.08  ? 479 PRO A C     1 
ATOM   3587  O  O     . PRO A 1 479 ? 181.434 153.184 157.960 1.00 23.91  ? 479 PRO A O     1 
ATOM   3588  C  CB    . PRO A 1 479 ? 183.890 151.754 156.286 1.00 17.56  ? 479 PRO A CB    1 
ATOM   3589  C  CG    . PRO A 1 479 ? 185.342 152.071 156.106 1.00 26.87  ? 479 PRO A CG    1 
ATOM   3590  C  CD    . PRO A 1 479 ? 185.412 153.384 155.407 1.00 22.69  ? 479 PRO A CD    1 
ATOM   3591  N  N     . PHE A 1 480 ? 183.455 153.937 158.609 1.00 19.01  ? 480 PHE A N     1 
ATOM   3592  C  CA    . PHE A 1 480 ? 182.967 154.299 159.936 1.00 15.31  ? 480 PHE A CA    1 
ATOM   3593  C  C     . PHE A 1 480 ? 181.986 155.463 159.862 1.00 14.38  ? 480 PHE A C     1 
ATOM   3594  O  O     . PHE A 1 480 ? 180.895 155.406 160.440 1.00 21.04  ? 480 PHE A O     1 
ATOM   3595  C  CB    . PHE A 1 480 ? 184.140 154.643 160.854 1.00 14.53  ? 480 PHE A CB    1 
ATOM   3596  C  CG    . PHE A 1 480 ? 183.734 155.359 162.112 1.00 17.59  ? 480 PHE A CG    1 
ATOM   3597  C  CD1   . PHE A 1 480 ? 183.222 154.656 163.190 1.00 11.31  ? 480 PHE A CD1   1 
ATOM   3598  C  CD2   . PHE A 1 480 ? 183.861 156.735 162.216 1.00 17.32  ? 480 PHE A CD2   1 
ATOM   3599  C  CE1   . PHE A 1 480 ? 182.846 155.310 164.347 1.00 19.23  ? 480 PHE A CE1   1 
ATOM   3600  C  CE2   . PHE A 1 480 ? 183.483 157.395 163.369 1.00 19.98  ? 480 PHE A CE2   1 
ATOM   3601  C  CZ    . PHE A 1 480 ? 182.976 156.681 164.437 1.00 19.78  ? 480 PHE A CZ    1 
ATOM   3602  N  N     . TRP A 1 481 ? 182.360 156.531 159.154 1.00 14.75  ? 481 TRP A N     1 
ATOM   3603  C  CA    . TRP A 1 481 ? 181.498 157.706 159.079 1.00 14.44  ? 481 TRP A CA    1 
ATOM   3604  C  C     . TRP A 1 481 ? 180.261 157.435 158.232 1.00 17.95  ? 481 TRP A C     1 
ATOM   3605  O  O     . TRP A 1 481 ? 179.174 157.940 158.535 1.00 15.97  ? 481 TRP A O     1 
ATOM   3606  C  CB    . TRP A 1 481 ? 182.280 158.898 158.529 1.00 10.39  ? 481 TRP A CB    1 
ATOM   3607  C  CG    . TRP A 1 481 ? 182.990 159.681 159.590 1.00 17.95  ? 481 TRP A CG    1 
ATOM   3608  C  CD1   . TRP A 1 481 ? 184.330 159.692 159.841 1.00 13.97  ? 481 TRP A CD1   1 
ATOM   3609  C  CD2   . TRP A 1 481 ? 182.396 160.564 160.549 1.00 14.50  ? 481 TRP A CD2   1 
ATOM   3610  N  NE1   . TRP A 1 481 ? 184.609 160.527 160.894 1.00 23.13  ? 481 TRP A NE1   1 
ATOM   3611  C  CE2   . TRP A 1 481 ? 183.438 161.075 161.348 1.00 13.23  ? 481 TRP A CE2   1 
ATOM   3612  C  CE3   . TRP A 1 481 ? 181.084 160.972 160.810 1.00 16.50  ? 481 TRP A CE3   1 
ATOM   3613  C  CZ2   . TRP A 1 481 ? 183.210 161.973 162.388 1.00 14.62  ? 481 TRP A CZ2   1 
ATOM   3614  C  CZ3   . TRP A 1 481 ? 180.860 161.864 161.843 1.00 18.62  ? 481 TRP A CZ3   1 
ATOM   3615  C  CH2   . TRP A 1 481 ? 181.917 162.355 162.619 1.00 16.44  ? 481 TRP A CH2   1 
ATOM   3616  N  N     . ASN A 1 482 ? 180.406 156.649 157.163 1.00 14.11  ? 482 ASN A N     1 
ATOM   3617  C  CA    . ASN A 1 482 ? 179.252 156.316 156.334 1.00 12.64  ? 482 ASN A CA    1 
ATOM   3618  C  C     . ASN A 1 482 ? 178.220 155.517 157.120 1.00 21.16  ? 482 ASN A C     1 
ATOM   3619  O  O     . ASN A 1 482 ? 177.015 155.771 157.012 1.00 17.68  ? 482 ASN A O     1 
ATOM   3620  C  CB    . ASN A 1 482 ? 179.699 155.544 155.093 1.00 16.67  ? 482 ASN A CB    1 
ATOM   3621  C  CG    . ASN A 1 482 ? 180.170 156.456 153.977 1.00 19.34  ? 482 ASN A CG    1 
ATOM   3622  O  OD1   . ASN A 1 482 ? 179.586 157.512 153.735 1.00 25.68  ? 482 ASN A OD1   1 
ATOM   3623  N  ND2   . ASN A 1 482 ? 181.231 156.052 153.290 1.00 12.69  ? 482 ASN A ND2   1 
ATOM   3624  N  N     . CYS A 1 483 ? 178.673 154.550 157.920 1.00 23.37  ? 483 CYS A N     1 
ATOM   3625  C  CA    . CYS A 1 483 ? 177.741 153.724 158.681 1.00 20.49  ? 483 CYS A CA    1 
ATOM   3626  C  C     . CYS A 1 483 ? 177.149 154.488 159.859 1.00 19.16  ? 483 CYS A C     1 
ATOM   3627  O  O     . CYS A 1 483 ? 175.950 154.371 160.140 1.00 23.31  ? 483 CYS A O     1 
ATOM   3628  C  CB    . CYS A 1 483 ? 178.441 152.453 159.162 1.00 16.45  ? 483 CYS A CB    1 
ATOM   3629  S  SG    . CYS A 1 483 ? 178.712 151.219 157.871 1.00 34.62  ? 483 CYS A SG    1 
ATOM   3630  N  N     . LEU A 1 484 ? 177.972 155.270 160.563 1.00 13.91  ? 484 LEU A N     1 
ATOM   3631  C  CA    . LEU A 1 484 ? 177.482 155.998 161.729 1.00 17.96  ? 484 LEU A CA    1 
ATOM   3632  C  C     . LEU A 1 484 ? 176.434 157.033 161.339 1.00 21.96  ? 484 LEU A C     1 
ATOM   3633  O  O     . LEU A 1 484 ? 175.400 157.163 162.005 1.00 14.32  ? 484 LEU A O     1 
ATOM   3634  C  CB    . LEU A 1 484 ? 178.647 156.665 162.461 1.00 16.27  ? 484 LEU A CB    1 
ATOM   3635  C  CG    . LEU A 1 484 ? 178.287 157.762 163.465 1.00 18.62  ? 484 LEU A CG    1 
ATOM   3636  C  CD1   . LEU A 1 484 ? 177.609 157.170 164.690 1.00 15.11  ? 484 LEU A CD1   1 
ATOM   3637  C  CD2   . LEU A 1 484 ? 179.520 158.558 163.861 1.00 19.71  ? 484 LEU A CD2   1 
ATOM   3638  N  N     . LEU A 1 485 ? 176.679 157.777 160.258 1.00 15.13  ? 485 LEU A N     1 
ATOM   3639  C  CA    . LEU A 1 485 ? 175.715 158.784 159.832 1.00 15.15  ? 485 LEU A CA    1 
ATOM   3640  C  C     . LEU A 1 485 ? 174.474 158.151 159.216 1.00 13.56  ? 485 LEU A C     1 
ATOM   3641  O  O     . LEU A 1 485 ? 173.376 158.704 159.336 1.00 21.99  ? 485 LEU A O     1 
ATOM   3642  C  CB    . LEU A 1 485 ? 176.369 159.756 158.850 1.00 11.59  ? 485 LEU A CB    1 
ATOM   3643  C  CG    . LEU A 1 485 ? 177.524 160.581 159.424 1.00 16.45  ? 485 LEU A CG    1 
ATOM   3644  C  CD1   . LEU A 1 485 ? 178.140 161.461 158.352 1.00 14.62  ? 485 LEU A CD1   1 
ATOM   3645  C  CD2   . LEU A 1 485 ? 177.064 161.416 160.611 1.00 16.02  ? 485 LEU A CD2   1 
ATOM   3646  N  N     . ALA A 1 486 ? 174.626 156.998 158.557 1.00 18.04  ? 486 ALA A N     1 
ATOM   3647  C  CA    . ALA A 1 486 ? 173.463 156.296 158.021 1.00 14.61  ? 486 ALA A CA    1 
ATOM   3648  C  C     . ALA A 1 486 ? 172.530 155.849 159.138 1.00 14.23  ? 486 ALA A C     1 
ATOM   3649  O  O     . ALA A 1 486 ? 171.304 155.949 159.012 1.00 18.59  ? 486 ALA A O     1 
ATOM   3650  C  CB    . ALA A 1 486 ? 173.908 155.099 157.181 1.00 12.13  ? 486 ALA A CB    1 
ATOM   3651  N  N     . PHE A 1 487 ? 173.095 155.349 160.239 1.00 11.13  ? 487 PHE A N     1 
ATOM   3652  C  CA    . PHE A 1 487 ? 172.278 154.982 161.391 1.00 15.78  ? 487 PHE A CA    1 
ATOM   3653  C  C     . PHE A 1 487 ? 171.567 156.199 161.969 1.00 16.32  ? 487 PHE A C     1 
ATOM   3654  O  O     . PHE A 1 487 ? 170.379 156.132 162.304 1.00 20.88  ? 487 PHE A O     1 
ATOM   3655  C  CB    . PHE A 1 487 ? 173.152 154.312 162.453 1.00 11.15  ? 487 PHE A CB    1 
ATOM   3656  C  CG    . PHE A 1 487 ? 172.399 153.880 163.679 1.00 17.94  ? 487 PHE A CG    1 
ATOM   3657  C  CD1   . PHE A 1 487 ? 171.735 152.665 163.707 1.00 12.25  ? 487 PHE A CD1   1 
ATOM   3658  C  CD2   . PHE A 1 487 ? 172.361 154.685 164.807 1.00 21.01  ? 487 PHE A CD2   1 
ATOM   3659  C  CE1   . PHE A 1 487 ? 171.045 152.263 164.834 1.00 15.20  ? 487 PHE A CE1   1 
ATOM   3660  C  CE2   . PHE A 1 487 ? 171.672 154.289 165.936 1.00 14.23  ? 487 PHE A CE2   1 
ATOM   3661  C  CZ    . PHE A 1 487 ? 171.013 153.076 165.949 1.00 15.47  ? 487 PHE A CZ    1 
ATOM   3662  N  N     . CYS A 1 488 ? 172.279 157.321 162.091 1.00 7.02   ? 488 CYS A N     1 
ATOM   3663  C  CA    . CYS A 1 488 ? 171.668 158.532 162.630 1.00 12.45  ? 488 CYS A CA    1 
ATOM   3664  C  C     . CYS A 1 488 ? 170.569 159.057 161.714 1.00 16.64  ? 488 CYS A C     1 
ATOM   3665  O  O     . CYS A 1 488 ? 169.515 159.495 162.190 1.00 21.45  ? 488 CYS A O     1 
ATOM   3666  C  CB    . CYS A 1 488 ? 172.737 159.600 162.857 1.00 15.83  ? 488 CYS A CB    1 
ATOM   3667  S  SG    . CYS A 1 488 ? 173.912 159.206 164.173 1.00 34.47  ? 488 CYS A SG    1 
ATOM   3668  N  N     . MET A 1 489 ? 170.798 159.030 160.398 1.00 12.28  ? 489 MET A N     1 
ATOM   3669  C  CA    . MET A 1 489 ? 169.782 159.506 159.464 1.00 16.71  ? 489 MET A CA    1 
ATOM   3670  C  C     . MET A 1 489 ? 168.551 158.607 159.478 1.00 6.56   ? 489 MET A C     1 
ATOM   3671  O  O     . MET A 1 489 ? 167.417 159.099 159.458 1.00 8.49   ? 489 MET A O     1 
ATOM   3672  C  CB    . MET A 1 489 ? 170.362 159.598 158.051 1.00 8.13   ? 489 MET A CB    1 
ATOM   3673  C  CG    . MET A 1 489 ? 171.119 160.889 157.774 1.00 6.15   ? 489 MET A CG    1 
ATOM   3674  S  SD    . MET A 1 489 ? 172.037 160.911 156.218 1.00 20.97  ? 489 MET A SD    1 
ATOM   3675  C  CE    . MET A 1 489 ? 172.864 159.328 156.243 1.00 7.60   ? 489 MET A CE    1 
ATOM   3676  N  N     . PHE A 1 490 ? 168.753 157.288 159.511 1.00 11.91  ? 490 PHE A N     1 
ATOM   3677  C  CA    . PHE A 1 490 ? 167.628 156.359 159.476 1.00 13.04  ? 490 PHE A CA    1 
ATOM   3678  C  C     . PHE A 1 490 ? 166.807 156.434 160.758 1.00 19.78  ? 490 PHE A C     1 
ATOM   3679  O  O     . PHE A 1 490 ? 165.575 156.536 160.714 1.00 14.33  ? 490 PHE A O     1 
ATOM   3680  C  CB    . PHE A 1 490 ? 168.135 154.936 159.241 1.00 14.11  ? 490 PHE A CB    1 
ATOM   3681  C  CG    . PHE A 1 490 ? 167.047 153.941 158.956 1.00 14.47  ? 490 PHE A CG    1 
ATOM   3682  C  CD1   . PHE A 1 490 ? 166.605 153.730 157.661 1.00 15.70  ? 490 PHE A CD1   1 
ATOM   3683  C  CD2   . PHE A 1 490 ? 166.470 153.211 159.982 1.00 16.38  ? 490 PHE A CD2   1 
ATOM   3684  C  CE1   . PHE A 1 490 ? 165.606 152.812 157.395 1.00 11.67  ? 490 PHE A CE1   1 
ATOM   3685  C  CE2   . PHE A 1 490 ? 165.470 152.294 159.724 1.00 18.33  ? 490 PHE A CE2   1 
ATOM   3686  C  CZ    . PHE A 1 490 ? 165.038 152.094 158.428 1.00 22.62  ? 490 PHE A CZ    1 
ATOM   3687  N  N     . VAL A 1 491 ? 167.473 156.382 161.913 1.00 13.16  ? 491 VAL A N     1 
ATOM   3688  C  CA    . VAL A 1 491 ? 166.757 156.428 163.184 1.00 14.35  ? 491 VAL A CA    1 
ATOM   3689  C  C     . VAL A 1 491 ? 166.172 157.815 163.420 1.00 12.60  ? 491 VAL A C     1 
ATOM   3690  O  O     . VAL A 1 491 ? 165.049 157.953 163.919 1.00 17.94  ? 491 VAL A O     1 
ATOM   3691  C  CB    . VAL A 1 491 ? 167.684 155.995 164.336 1.00 16.16  ? 491 VAL A CB    1 
ATOM   3692  C  CG1   . VAL A 1 491 ? 166.965 156.109 165.671 1.00 11.25  ? 491 VAL A CG1   1 
ATOM   3693  C  CG2   . VAL A 1 491 ? 168.174 154.572 164.114 1.00 11.64  ? 491 VAL A CG2   1 
ATOM   3694  N  N     . GLY A 1 492 ? 166.914 158.863 163.060 1.00 18.49  ? 492 GLY A N     1 
ATOM   3695  C  CA    . GLY A 1 492 ? 166.432 160.218 163.262 1.00 8.38   ? 492 GLY A CA    1 
ATOM   3696  C  C     . GLY A 1 492 ? 165.210 160.567 162.439 1.00 16.38  ? 492 GLY A C     1 
ATOM   3697  O  O     . GLY A 1 492 ? 164.468 161.485 162.805 1.00 27.14  ? 492 GLY A O     1 
ATOM   3698  N  N     . ARG A 1 493 ? 164.979 159.857 161.336 1.00 18.66  ? 493 ARG A N     1 
ATOM   3699  C  CA    . ARG A 1 493 ? 163.832 160.126 160.475 1.00 7.30   ? 493 ARG A CA    1 
ATOM   3700  C  C     . ARG A 1 493 ? 162.632 159.260 160.851 1.00 15.51  ? 493 ARG A C     1 
ATOM   3701  O  O     . ARG A 1 493 ? 161.558 159.779 161.168 1.00 14.05  ? 493 ARG A O     1 
ATOM   3702  C  CB    . ARG A 1 493 ? 164.218 159.905 159.009 1.00 13.69  ? 493 ARG A CB    1 
ATOM   3703  C  CG    . ARG A 1 493 ? 163.051 159.982 158.040 1.00 9.44   ? 493 ARG A CG    1 
ATOM   3704  C  CD    . ARG A 1 493 ? 162.632 161.422 157.805 1.00 13.05  ? 493 ARG A CD    1 
ATOM   3705  N  NE    . ARG A 1 493 ? 161.794 161.563 156.621 1.00 13.77  ? 493 ARG A NE    1 
ATOM   3706  C  CZ    . ARG A 1 493 ? 161.241 162.702 156.227 1.00 5.60   ? 493 ARG A CZ    1 
ATOM   3707  N  NH1   . ARG A 1 493 ? 161.413 163.825 156.905 1.00 18.05  ? 493 ARG A NH1   1 
ATOM   3708  N  NH2   . ARG A 1 493 ? 160.498 162.715 155.124 1.00 12.81  ? 493 ARG A NH2   1 
ATOM   3709  N  N     . PHE A 1 494 ? 162.803 157.938 160.817 1.00 13.72  ? 494 PHE A N     1 
ATOM   3710  C  CA    . PHE A 1 494 ? 161.694 157.028 161.075 1.00 14.36  ? 494 PHE A CA    1 
ATOM   3711  C  C     . PHE A 1 494 ? 161.446 156.801 162.559 1.00 19.33  ? 494 PHE A C     1 
ATOM   3712  O  O     . PHE A 1 494 ? 160.381 156.291 162.923 1.00 29.83  ? 494 PHE A O     1 
ATOM   3713  C  CB    . PHE A 1 494 ? 161.945 155.692 160.374 1.00 14.82  ? 494 PHE A CB    1 
ATOM   3714  C  CG    . PHE A 1 494 ? 162.155 155.821 158.894 1.00 20.28  ? 494 PHE A CG    1 
ATOM   3715  C  CD1   . PHE A 1 494 ? 161.131 156.266 158.073 1.00 20.80  ? 494 PHE A CD1   1 
ATOM   3716  C  CD2   . PHE A 1 494 ? 163.378 155.512 158.323 1.00 17.37  ? 494 PHE A CD2   1 
ATOM   3717  C  CE1   . PHE A 1 494 ? 161.321 156.392 156.711 1.00 18.34  ? 494 PHE A CE1   1 
ATOM   3718  C  CE2   . PHE A 1 494 ? 163.574 155.636 156.962 1.00 17.89  ? 494 PHE A CE2   1 
ATOM   3719  C  CZ    . PHE A 1 494 ? 162.544 156.076 156.155 1.00 20.59  ? 494 PHE A CZ    1 
ATOM   3720  N  N     . GLY A 1 495 ? 162.393 157.170 163.422 1.00 17.83  ? 495 GLY A N     1 
ATOM   3721  C  CA    . GLY A 1 495 ? 162.168 157.083 164.851 1.00 13.05  ? 495 GLY A CA    1 
ATOM   3722  C  C     . GLY A 1 495 ? 161.303 158.183 165.420 1.00 16.53  ? 495 GLY A C     1 
ATOM   3723  O  O     . GLY A 1 495 ? 160.928 158.118 166.594 1.00 25.62  ? 495 GLY A O     1 
ATOM   3724  N  N     . VAL A 1 496 ? 160.987 159.193 164.612 1.00 16.08  ? 496 VAL A N     1 
ATOM   3725  C  CA    . VAL A 1 496 ? 160.093 160.272 165.010 1.00 17.55  ? 496 VAL A CA    1 
ATOM   3726  C  C     . VAL A 1 496 ? 158.756 160.068 164.310 1.00 12.93  ? 496 VAL A C     1 
ATOM   3727  O  O     . VAL A 1 496 ? 157.697 160.402 164.854 1.00 26.08  ? 496 VAL A O     1 
ATOM   3728  C  CB    . VAL A 1 496 ? 160.700 161.649 164.678 1.00 23.51  ? 496 VAL A CB    1 
ATOM   3729  C  CG1   . VAL A 1 496 ? 159.745 162.768 165.065 1.00 17.54  ? 496 VAL A CG1   1 
ATOM   3730  C  CG2   . VAL A 1 496 ? 162.039 161.820 165.380 1.00 18.32  ? 496 VAL A CG2   1 
ATOM   3731  N  N     . ILE A 1 497 ? 158.798 159.507 163.100 1.00 20.80  ? 497 ILE A N     1 
ATOM   3732  C  CA    . ILE A 1 497 ? 157.574 159.294 162.332 1.00 13.79  ? 497 ILE A CA    1 
ATOM   3733  C  C     . ILE A 1 497 ? 156.662 158.295 163.034 1.00 9.25   ? 497 ILE A C     1 
ATOM   3734  O  O     . ILE A 1 497 ? 155.444 158.497 163.114 1.00 19.85  ? 497 ILE A O     1 
ATOM   3735  C  CB    . ILE A 1 497 ? 157.916 158.850 160.896 1.00 16.82  ? 497 ILE A CB    1 
ATOM   3736  C  CG1   . ILE A 1 497 ? 158.322 160.060 160.053 1.00 14.60  ? 497 ILE A CG1   1 
ATOM   3737  C  CG2   . ILE A 1 497 ? 156.739 158.132 160.253 1.00 11.59  ? 497 ILE A CG2   1 
ATOM   3738  C  CD1   . ILE A 1 497 ? 159.030 159.703 158.766 1.00 14.12  ? 497 ILE A CD1   1 
ATOM   3739  N  N     . ILE A 1 498 ? 157.233 157.207 163.558 1.00 13.81  ? 498 ILE A N     1 
ATOM   3740  C  CA    . ILE A 1 498 ? 156.414 156.184 164.214 1.00 19.78  ? 498 ILE A CA    1 
ATOM   3741  C  C     . ILE A 1 498 ? 155.674 156.728 165.433 1.00 16.04  ? 498 ILE A C     1 
ATOM   3742  O  O     . ILE A 1 498 ? 154.450 156.534 165.519 1.00 23.85  ? 498 ILE A O     1 
ATOM   3743  C  CB    . ILE A 1 498 ? 157.272 154.949 164.540 1.00 17.21  ? 498 ILE A CB    1 
ATOM   3744  C  CG1   . ILE A 1 498 ? 157.729 154.259 163.252 1.00 19.99  ? 498 ILE A CG1   1 
ATOM   3745  C  CG2   . ILE A 1 498 ? 156.505 153.982 165.429 1.00 15.42  ? 498 ILE A CG2   1 
ATOM   3746  C  CD1   . ILE A 1 498 ? 158.928 153.355 163.438 1.00 16.45  ? 498 ILE A CD1   1 
ATOM   3747  N  N     . PRO A 1 499 ? 156.324 157.394 166.398 1.00 20.02  ? 499 PRO A N     1 
ATOM   3748  C  CA    . PRO A 1 499 ? 155.550 157.957 167.519 1.00 20.93  ? 499 PRO A CA    1 
ATOM   3749  C  C     . PRO A 1 499 ? 154.562 159.033 167.101 1.00 10.10  ? 499 PRO A C     1 
ATOM   3750  O  O     . PRO A 1 499 ? 153.489 159.141 167.708 1.00 22.50  ? 499 PRO A O     1 
ATOM   3751  C  CB    . PRO A 1 499 ? 156.634 158.514 168.454 1.00 15.68  ? 499 PRO A CB    1 
ATOM   3752  C  CG    . PRO A 1 499 ? 157.820 158.708 167.594 1.00 16.95  ? 499 PRO A CG    1 
ATOM   3753  C  CD    . PRO A 1 499 ? 157.770 157.616 166.581 1.00 9.45   ? 499 PRO A CD    1 
ATOM   3754  N  N     . VAL A 1 500 ? 154.889 159.835 166.085 1.00 6.43   ? 500 VAL A N     1 
ATOM   3755  C  CA    . VAL A 1 500 ? 153.961 160.863 165.622 1.00 17.64  ? 500 VAL A CA    1 
ATOM   3756  C  C     . VAL A 1 500 ? 152.708 160.225 165.036 1.00 19.86  ? 500 VAL A C     1 
ATOM   3757  O  O     . VAL A 1 500 ? 151.586 160.682 165.288 1.00 26.53  ? 500 VAL A O     1 
ATOM   3758  C  CB    . VAL A 1 500 ? 154.655 161.796 164.612 1.00 19.21  ? 500 VAL A CB    1 
ATOM   3759  C  CG1   . VAL A 1 500 ? 153.627 162.557 163.784 1.00 15.32  ? 500 VAL A CG1   1 
ATOM   3760  C  CG2   . VAL A 1 500 ? 155.578 162.765 165.334 1.00 20.95  ? 500 VAL A CG2   1 
ATOM   3761  N  N     . MET A 1 501 ? 152.875 159.160 164.249 1.00 18.31  ? 501 MET A N     1 
ATOM   3762  C  CA    . MET A 1 501 ? 151.720 158.442 163.719 1.00 15.61  ? 501 MET A CA    1 
ATOM   3763  C  C     . MET A 1 501 ? 150.886 157.841 164.844 1.00 13.39  ? 501 MET A C     1 
ATOM   3764  O  O     . MET A 1 501 ? 149.651 157.840 164.779 1.00 19.87  ? 501 MET A O     1 
ATOM   3765  C  CB    . MET A 1 501 ? 152.177 157.355 162.745 1.00 10.70  ? 501 MET A CB    1 
ATOM   3766  C  CG    . MET A 1 501 ? 152.522 157.861 161.348 1.00 18.89  ? 501 MET A CG    1 
ATOM   3767  S  SD    . MET A 1 501 ? 151.328 159.018 160.642 1.00 24.93  ? 501 MET A SD    1 
ATOM   3768  C  CE    . MET A 1 501 ? 149.801 158.087 160.777 1.00 17.59  ? 501 MET A CE    1 
ATOM   3769  N  N     . ALA A 1 502 ? 151.545 157.322 165.883 1.00 14.52  ? 502 ALA A N     1 
ATOM   3770  C  CA    . ALA A 1 502 ? 150.820 156.823 167.046 1.00 20.04  ? 502 ALA A CA    1 
ATOM   3771  C  C     . ALA A 1 502 ? 150.090 157.945 167.774 1.00 12.97  ? 502 ALA A C     1 
ATOM   3772  O  O     . ALA A 1 502 ? 149.009 157.720 168.330 1.00 23.32  ? 502 ALA A O     1 
ATOM   3773  C  CB    . ALA A 1 502 ? 151.777 156.105 167.996 1.00 9.86   ? 502 ALA A CB    1 
ATOM   3774  N  N     . ILE A 1 503 ? 150.666 159.150 167.790 1.00 17.24  ? 503 ILE A N     1 
ATOM   3775  C  CA    . ILE A 1 503 ? 149.978 160.299 168.373 1.00 17.99  ? 503 ILE A CA    1 
ATOM   3776  C  C     . ILE A 1 503 ? 148.713 160.615 167.586 1.00 14.94  ? 503 ILE A C     1 
ATOM   3777  O  O     . ILE A 1 503 ? 147.654 160.890 168.164 1.00 20.64  ? 503 ILE A O     1 
ATOM   3778  C  CB    . ILE A 1 503 ? 150.927 161.511 168.437 1.00 20.39  ? 503 ILE A CB    1 
ATOM   3779  C  CG1   . ILE A 1 503 ? 151.896 161.369 169.613 1.00 20.10  ? 503 ILE A CG1   1 
ATOM   3780  C  CG2   . ILE A 1 503 ? 150.142 162.809 168.548 1.00 11.35  ? 503 ILE A CG2   1 
ATOM   3781  C  CD1   . ILE A 1 503 ? 153.167 162.174 169.457 1.00 16.46  ? 503 ILE A CD1   1 
ATOM   3782  N  N     . ALA A 1 504 ? 148.801 160.577 166.254 1.00 13.99  ? 504 ALA A N     1 
ATOM   3783  C  CA    . ALA A 1 504 ? 147.628 160.828 165.423 1.00 17.68  ? 504 ALA A CA    1 
ATOM   3784  C  C     . ALA A 1 504 ? 146.557 159.767 165.643 1.00 17.70  ? 504 ALA A C     1 
ATOM   3785  O  O     . ALA A 1 504 ? 145.361 160.077 165.664 1.00 21.38  ? 504 ALA A O     1 
ATOM   3786  C  CB    . ALA A 1 504 ? 148.030 160.890 163.950 1.00 15.41  ? 504 ALA A CB    1 
ATOM   3787  N  N     . GLY A 1 505 ? 146.967 158.507 165.801 1.00 18.11  ? 505 GLY A N     1 
ATOM   3788  C  CA    . GLY A 1 505 ? 145.999 157.448 166.034 1.00 14.39  ? 505 GLY A CA    1 
ATOM   3789  C  C     . GLY A 1 505 ? 145.258 157.606 167.348 1.00 20.57  ? 505 GLY A C     1 
ATOM   3790  O  O     . GLY A 1 505 ? 144.064 157.308 167.439 1.00 27.96  ? 505 GLY A O     1 
ATOM   3791  N  N     . SER A 1 506 ? 145.955 158.068 168.388 1.00 17.75  ? 506 SER A N     1 
ATOM   3792  C  CA    . SER A 1 506 ? 145.309 158.263 169.681 1.00 23.29  ? 506 SER A CA    1 
ATOM   3793  C  C     . SER A 1 506 ? 144.431 159.510 169.690 1.00 26.52  ? 506 SER A C     1 
ATOM   3794  O  O     . SER A 1 506 ? 143.374 159.522 170.330 1.00 33.19  ? 506 SER A O     1 
ATOM   3795  C  CB    . SER A 1 506 ? 146.363 158.343 170.787 1.00 22.03  ? 506 SER A CB    1 
ATOM   3796  O  OG    . SER A 1 506 ? 146.910 159.647 170.881 1.00 36.26  ? 506 SER A OG    1 
ATOM   3797  N  N     . LEU A 1 507 ? 144.849 160.564 168.987 1.00 17.11  ? 507 LEU A N     1 
ATOM   3798  C  CA    . LEU A 1 507 ? 144.092 161.810 168.984 1.00 24.02  ? 507 LEU A CA    1 
ATOM   3799  C  C     . LEU A 1 507 ? 142.851 161.739 168.102 1.00 26.40  ? 507 LEU A C     1 
ATOM   3800  O  O     . LEU A 1 507 ? 141.846 162.391 168.406 1.00 27.40  ? 507 LEU A O     1 
ATOM   3801  C  CB    . LEU A 1 507 ? 144.986 162.966 168.531 1.00 18.85  ? 507 LEU A CB    1 
ATOM   3802  C  CG    . LEU A 1 507 ? 145.899 163.570 169.599 1.00 24.79  ? 507 LEU A CG    1 
ATOM   3803  C  CD1   . LEU A 1 507 ? 146.871 164.559 168.977 1.00 23.28  ? 507 LEU A CD1   1 
ATOM   3804  C  CD2   . LEU A 1 507 ? 145.080 164.235 170.694 1.00 23.48  ? 507 LEU A CD2   1 
ATOM   3805  N  N     . VAL A 1 508 ? 142.898 160.968 167.013 1.00 15.51  ? 508 VAL A N     1 
ATOM   3806  C  CA    . VAL A 1 508 ? 141.774 160.935 166.081 1.00 21.64  ? 508 VAL A CA    1 
ATOM   3807  C  C     . VAL A 1 508 ? 140.544 160.303 166.724 1.00 25.12  ? 508 VAL A C     1 
ATOM   3808  O  O     . VAL A 1 508 ? 139.410 160.703 166.433 1.00 23.40  ? 508 VAL A O     1 
ATOM   3809  C  CB    . VAL A 1 508 ? 142.177 160.216 164.777 1.00 18.63  ? 508 VAL A CB    1 
ATOM   3810  C  CG1   . VAL A 1 508 ? 142.465 158.742 165.023 1.00 16.49  ? 508 VAL A CG1   1 
ATOM   3811  C  CG2   . VAL A 1 508 ? 141.100 160.391 163.713 1.00 23.66  ? 508 VAL A CG2   1 
ATOM   3812  N  N     . SER A 1 509 ? 140.735 159.321 167.608 1.00 27.91  ? 509 SER A N     1 
ATOM   3813  C  CA    . SER A 1 509 ? 139.608 158.662 168.257 1.00 27.88  ? 509 SER A CA    1 
ATOM   3814  C  C     . SER A 1 509 ? 138.903 159.552 169.273 1.00 27.68  ? 509 SER A C     1 
ATOM   3815  O  O     . SER A 1 509 ? 137.787 159.222 169.686 1.00 33.08  ? 509 SER A O     1 
ATOM   3816  C  CB    . SER A 1 509 ? 140.075 157.374 168.939 1.00 25.89  ? 509 SER A CB    1 
ATOM   3817  O  OG    . SER A 1 509 ? 141.371 157.528 169.488 1.00 33.96  ? 509 SER A OG    1 
ATOM   3818  N  N     . LYS A 1 510 ? 139.519 160.657 169.682 1.00 31.05  ? 510 LYS A N     1 
ATOM   3819  C  CA    . LYS A 1 510 ? 138.920 161.538 170.670 1.00 27.96  ? 510 LYS A CA    1 
ATOM   3820  C  C     . LYS A 1 510 ? 137.953 162.518 170.009 1.00 32.16  ? 510 LYS A C     1 
ATOM   3821  O  O     . LYS A 1 510 ? 137.965 162.725 168.793 1.00 39.99  ? 510 LYS A O     1 
ATOM   3822  C  CB    . LYS A 1 510 ? 140.000 162.305 171.432 1.00 21.76  ? 510 LYS A CB    1 
ATOM   3823  C  CG    . LYS A 1 510 ? 140.915 161.424 172.264 1.00 30.15  ? 510 LYS A CG    1 
ATOM   3824  C  CD    . LYS A 1 510 ? 141.987 162.245 172.960 1.00 32.44  ? 510 LYS A CD    1 
ATOM   3825  C  CE    . LYS A 1 510 ? 142.847 161.376 173.862 1.00 30.57  ? 510 LYS A CE    1 
ATOM   3826  N  NZ    . LYS A 1 510 ? 143.741 162.190 174.729 1.00 35.31  ? 510 LYS A NZ    1 
ATOM   3827  N  N     . LYS A 1 511 ? 137.108 163.124 170.837 1.00 37.83  ? 511 LYS A N     1 
ATOM   3828  C  CA    . LYS A 1 511 ? 136.133 164.111 170.397 1.00 37.08  ? 511 LYS A CA    1 
ATOM   3829  C  C     . LYS A 1 511 ? 136.528 165.479 170.936 1.00 36.07  ? 511 LYS A C     1 
ATOM   3830  O  O     . LYS A 1 511 ? 136.799 165.623 172.133 1.00 42.94  ? 511 LYS A O     1 
ATOM   3831  C  CB    . LYS A 1 511 ? 134.725 163.735 170.867 1.00 37.94  ? 511 LYS A CB    1 
ATOM   3832  C  CG    . LYS A 1 511 ? 133.809 164.920 171.123 1.00 40.96  ? 511 LYS A CG    1 
ATOM   3833  C  CD    . LYS A 1 511 ? 132.364 164.476 171.279 1.00 41.65  ? 511 LYS A CD    1 
ATOM   3834  C  CE    . LYS A 1 511 ? 131.402 165.582 170.879 1.00 43.35  ? 511 LYS A CE    1 
ATOM   3835  N  NZ    . LYS A 1 511 ? 131.104 166.493 172.018 1.00 44.90  ? 511 LYS A NZ    1 
ATOM   3836  N  N     . SER A 1 512 ? 136.571 166.472 170.053 1.00 35.82  ? 512 SER A N     1 
ATOM   3837  C  CA    . SER A 1 512 ? 136.943 167.819 170.461 1.00 35.63  ? 512 SER A CA    1 
ATOM   3838  C  C     . SER A 1 512 ? 135.867 168.429 171.350 1.00 39.71  ? 512 SER A C     1 
ATOM   3839  O  O     . SER A 1 512 ? 134.668 168.276 171.101 1.00 47.85  ? 512 SER A O     1 
ATOM   3840  C  CB    . SER A 1 512 ? 137.173 168.704 169.237 1.00 38.35  ? 512 SER A CB    1 
ATOM   3841  O  OG    . SER A 1 512 ? 138.354 168.330 168.549 1.00 46.90  ? 512 SER A OG    1 
ATOM   3842  N  N     . GLN A 1 513 ? 136.304 169.126 172.394 1.00 45.74  ? 513 GLN A N     1 
ATOM   3843  C  CA    . GLN A 1 513 ? 135.407 169.805 173.317 1.00 45.93  ? 513 GLN A CA    1 
ATOM   3844  C  C     . GLN A 1 513 ? 135.326 171.284 172.965 1.00 45.71  ? 513 GLN A C     1 
ATOM   3845  O  O     . GLN A 1 513 ? 136.344 171.922 172.680 1.00 48.04  ? 513 GLN A O     1 
ATOM   3846  C  CB    . GLN A 1 513 ? 135.878 169.635 174.763 1.00 47.17  ? 513 GLN A CB    1 
ATOM   3847  C  CG    . GLN A 1 513 ? 135.486 168.308 175.393 1.00 50.24  ? 513 GLN A CG    1 
ATOM   3848  C  CD    . GLN A 1 513 ? 136.676 167.399 175.633 1.00 51.97  ? 513 GLN A CD    1 
ATOM   3849  O  OE1   . GLN A 1 513 ? 137.641 167.404 174.870 1.00 51.99  ? 513 GLN A OE1   1 
ATOM   3850  N  NE2   . GLN A 1 513 ? 136.612 166.610 176.700 1.00 52.47  ? 513 GLN A NE2   1 
ATOM   3851  N  N     . ALA A 1 514 ? 134.109 171.820 172.980 1.00 50.67  ? 514 ALA A N     1 
ATOM   3852  C  CA    . ALA A 1 514 ? 133.906 173.226 172.662 1.00 51.82  ? 514 ALA A CA    1 
ATOM   3853  C  C     . ALA A 1 514 ? 134.572 174.113 173.706 1.00 52.53  ? 514 ALA A C     1 
ATOM   3854  O  O     . ALA A 1 514 ? 134.610 173.782 174.894 1.00 53.02  ? 514 ALA A O     1 
ATOM   3855  C  CB    . ALA A 1 514 ? 132.413 173.543 172.575 1.00 53.12  ? 514 ALA A CB    1 
ATOM   3856  N  N     . ALA A 1 515 ? 135.104 175.245 173.253 1.00 51.67  ? 515 ALA A N     1 
ATOM   3857  C  CA    . ALA A 1 515 ? 135.799 176.159 174.149 1.00 53.05  ? 515 ALA A CA    1 
ATOM   3858  C  C     . ALA A 1 515 ? 134.814 176.814 175.109 1.00 50.80  ? 515 ALA A C     1 
ATOM   3859  O  O     . ALA A 1 515 ? 133.769 177.325 174.693 1.00 53.84  ? 515 ALA A O     1 
ATOM   3860  C  CB    . ALA A 1 515 ? 136.546 177.222 173.347 1.00 50.31  ? 515 ALA A CB    1 
ATOM   3861  N  N     . SER A 1 516 ? 135.150 176.799 176.394 1.00 49.73  ? 516 SER A N     1 
ATOM   3862  C  CA    . SER A 1 516 ? 134.334 177.404 177.430 1.00 48.57  ? 516 SER A CA    1 
ATOM   3863  C  C     . SER A 1 516 ? 134.940 178.743 177.845 1.00 50.71  ? 516 SER A C     1 
ATOM   3864  O  O     . SER A 1 516 ? 135.896 179.235 177.237 1.00 49.87  ? 516 SER A O     1 
ATOM   3865  C  CB    . SER A 1 516 ? 134.197 176.445 178.615 1.00 51.13  ? 516 SER A CB    1 
ATOM   3866  O  OG    . SER A 1 516 ? 135.277 176.592 179.520 1.00 53.19  ? 516 SER A OG    1 
ATOM   3867  N  N     . SER A 1 517 ? 134.372 179.350 178.890 1.00 52.85  ? 517 SER A N     1 
ATOM   3868  C  CA    . SER A 1 517 ? 134.890 180.625 179.378 1.00 49.59  ? 517 SER A CA    1 
ATOM   3869  C  C     . SER A 1 517 ? 136.300 180.475 179.936 1.00 49.59  ? 517 SER A C     1 
ATOM   3870  O  O     . SER A 1 517 ? 137.150 181.350 179.733 1.00 52.41  ? 517 SER A O     1 
ATOM   3871  C  CB    . SER A 1 517 ? 133.951 181.200 180.438 1.00 51.51  ? 517 SER A CB    1 
ATOM   3872  O  OG    . SER A 1 517 ? 133.750 180.279 181.495 1.00 55.55  ? 517 SER A OG    1 
ATOM   3873  N  N     . GLY A 1 518 ? 136.567 179.378 180.641 1.00 44.21  ? 518 GLY A N     1 
ATOM   3874  C  CA    . GLY A 1 518 ? 137.866 179.136 181.232 1.00 42.59  ? 518 GLY A CA    1 
ATOM   3875  C  C     . GLY A 1 518 ? 138.898 178.508 180.326 1.00 43.75  ? 518 GLY A C     1 
ATOM   3876  O  O     . GLY A 1 518 ? 140.019 178.250 180.772 1.00 44.76  ? 518 GLY A O     1 
ATOM   3877  N  N     . THR A 1 519 ? 138.558 178.249 179.066 1.00 44.10  ? 519 THR A N     1 
ATOM   3878  C  CA    . THR A 1 519 ? 139.501 177.630 178.145 1.00 40.31  ? 519 THR A CA    1 
ATOM   3879  C  C     . THR A 1 519 ? 140.636 178.595 177.821 1.00 41.29  ? 519 THR A C     1 
ATOM   3880  O  O     . THR A 1 519 ? 140.400 179.764 177.501 1.00 45.11  ? 519 THR A O     1 
ATOM   3881  C  CB    . THR A 1 519 ? 138.788 177.203 176.862 1.00 44.61  ? 519 THR A CB    1 
ATOM   3882  O  OG1   . THR A 1 519 ? 137.699 176.330 177.187 1.00 48.55  ? 519 THR A OG1   1 
ATOM   3883  C  CG2   . THR A 1 519 ? 139.749 176.480 175.930 1.00 40.90  ? 519 THR A CG2   1 
ATOM   3884  N  N     . LEU A 1 520 ? 141.867 178.104 177.905 1.00 33.09  ? 520 LEU A N     1 
ATOM   3885  C  CA    . LEU A 1 520 ? 143.028 178.932 177.607 1.00 33.61  ? 520 LEU A CA    1 
ATOM   3886  C  C     . LEU A 1 520 ? 143.213 179.041 176.099 1.00 36.89  ? 520 LEU A C     1 
ATOM   3887  O  O     . LEU A 1 520 ? 143.346 178.012 175.427 1.00 37.67  ? 520 LEU A O     1 
ATOM   3888  C  CB    . LEU A 1 520 ? 144.281 178.348 178.245 1.00 33.82  ? 520 LEU A CB    1 
ATOM   3889  C  CG    . LEU A 1 520 ? 145.599 179.004 177.825 1.00 37.21  ? 520 LEU A CG    1 
ATOM   3890  C  CD1   . LEU A 1 520 ? 145.840 180.284 178.611 1.00 31.26  ? 520 LEU A CD1   1 
ATOM   3891  C  CD2   . LEU A 1 520 ? 146.758 178.038 177.994 1.00 34.47  ? 520 LEU A CD2   1 
ATOM   3892  N  N     . PRO A 1 521 ? 143.220 180.245 175.531 1.00 34.88  ? 521 PRO A N     1 
ATOM   3893  C  CA    . PRO A 1 521 ? 143.462 180.372 174.089 1.00 35.36  ? 521 PRO A CA    1 
ATOM   3894  C  C     . PRO A 1 521 ? 144.881 179.961 173.730 1.00 35.63  ? 521 PRO A C     1 
ATOM   3895  O  O     . PRO A 1 521 ? 145.828 180.197 174.485 1.00 37.57  ? 521 PRO A O     1 
ATOM   3896  C  CB    . PRO A 1 521 ? 143.221 181.861 173.817 1.00 31.87  ? 521 PRO A CB    1 
ATOM   3897  C  CG    . PRO A 1 521 ? 143.455 182.528 175.128 1.00 32.79  ? 521 PRO A CG    1 
ATOM   3898  C  CD    . PRO A 1 521 ? 143.031 181.551 176.184 1.00 30.10  ? 521 PRO A CD    1 
ATOM   3899  N  N     . THR A 1 522 ? 145.021 179.344 172.559 1.00 33.14  ? 522 THR A N     1 
ATOM   3900  C  CA    . THR A 1 522 ? 146.312 178.901 172.054 1.00 30.11  ? 522 THR A CA    1 
ATOM   3901  C  C     . THR A 1 522 ? 146.885 179.853 171.014 1.00 28.13  ? 522 THR A C     1 
ATOM   3902  O  O     . THR A 1 522 ? 147.829 179.490 170.306 1.00 34.92  ? 522 THR A O     1 
ATOM   3903  C  CB    . THR A 1 522 ? 146.197 177.492 171.469 1.00 33.02  ? 522 THR A CB    1 
ATOM   3904  O  OG1   . THR A 1 522 ? 145.073 177.430 170.582 1.00 40.90  ? 522 THR A OG1   1 
ATOM   3905  C  CG2   . THR A 1 522 ? 146.017 176.471 172.581 1.00 31.78  ? 522 THR A CG2   1 
ATOM   3906  N  N     . HIS A 1 523 ? 146.328 181.055 170.902 1.00 32.11  ? 523 HIS A N     1 
ATOM   3907  C  CA    . HIS A 1 523 ? 146.799 182.066 169.970 1.00 29.01  ? 523 HIS A CA    1 
ATOM   3908  C  C     . HIS A 1 523 ? 147.028 183.368 170.721 1.00 30.61  ? 523 HIS A C     1 
ATOM   3909  O  O     . HIS A 1 523 ? 146.421 183.614 171.766 1.00 40.73  ? 523 HIS A O     1 
ATOM   3910  C  CB    . HIS A 1 523 ? 145.796 182.290 168.832 1.00 29.59  ? 523 HIS A CB    1 
ATOM   3911  C  CG    . HIS A 1 523 ? 144.455 182.765 169.298 1.00 33.56  ? 523 HIS A CG    1 
ATOM   3912  N  ND1   . HIS A 1 523 ? 144.158 184.099 169.474 1.00 30.96  ? 523 HIS A ND1   1 
ATOM   3913  C  CD2   . HIS A 1 523 ? 143.336 182.082 169.636 1.00 32.48  ? 523 HIS A CD2   1 
ATOM   3914  C  CE1   . HIS A 1 523 ? 142.912 184.218 169.895 1.00 34.75  ? 523 HIS A CE1   1 
ATOM   3915  N  NE2   . HIS A 1 523 ? 142.391 183.009 170.002 1.00 38.15  ? 523 HIS A NE2   1 
ATOM   3916  N  N     . GLY A 1 524 ? 147.912 184.199 170.180 1.00 26.86  ? 524 GLY A N     1 
ATOM   3917  C  CA    . GLY A 1 524 ? 148.214 185.476 170.780 1.00 28.28  ? 524 GLY A CA    1 
ATOM   3918  C  C     . GLY A 1 524 ? 149.653 185.574 171.239 1.00 27.34  ? 524 GLY A C     1 
ATOM   3919  O  O     . GLY A 1 524 ? 150.390 184.584 171.268 1.00 33.57  ? 524 GLY A O     1 
ATOM   3920  N  N     . PRO A 1 525 ? 150.082 186.786 171.603 1.00 29.86  ? 525 PRO A N     1 
ATOM   3921  C  CA    . PRO A 1 525 ? 151.486 186.968 172.016 1.00 33.97  ? 525 PRO A CA    1 
ATOM   3922  C  C     . PRO A 1 525 ? 151.882 186.140 173.228 1.00 32.11  ? 525 PRO A C     1 
ATOM   3923  O  O     . PRO A 1 525 ? 153.029 185.685 173.307 1.00 33.86  ? 525 PRO A O     1 
ATOM   3924  C  CB    . PRO A 1 525 ? 151.586 188.475 172.305 1.00 28.77  ? 525 PRO A CB    1 
ATOM   3925  C  CG    . PRO A 1 525 ? 150.199 189.008 172.283 1.00 28.22  ? 525 PRO A CG    1 
ATOM   3926  C  CD    . PRO A 1 525 ? 149.320 188.044 171.569 1.00 31.35  ? 525 PRO A CD    1 
ATOM   3927  N  N     . LEU A 1 526 ? 150.967 185.935 174.180 1.00 29.79  ? 526 LEU A N     1 
ATOM   3928  C  CA    . LEU A 1 526 ? 151.317 185.190 175.386 1.00 30.77  ? 526 LEU A CA    1 
ATOM   3929  C  C     . LEU A 1 526 ? 151.645 183.735 175.070 1.00 29.13  ? 526 LEU A C     1 
ATOM   3930  O  O     . LEU A 1 526 ? 152.635 183.195 175.576 1.00 31.97  ? 526 LEU A O     1 
ATOM   3931  C  CB    . LEU A 1 526 ? 150.184 185.274 176.408 1.00 32.79  ? 526 LEU A CB    1 
ATOM   3932  C  CG    . LEU A 1 526 ? 150.333 184.389 177.648 1.00 34.50  ? 526 LEU A CG    1 
ATOM   3933  C  CD1   . LEU A 1 526 ? 151.471 184.884 178.529 1.00 28.26  ? 526 LEU A CD1   1 
ATOM   3934  C  CD2   . LEU A 1 526 ? 149.030 184.328 178.432 1.00 32.63  ? 526 LEU A CD2   1 
ATOM   3935  N  N     . PHE A 1 527 ? 150.828 183.083 174.239 1.00 31.95  ? 527 PHE A N     1 
ATOM   3936  C  CA    . PHE A 1 527 ? 151.111 181.698 173.881 1.00 26.16  ? 527 PHE A CA    1 
ATOM   3937  C  C     . PHE A 1 527 ? 152.294 181.593 172.929 1.00 24.13  ? 527 PHE A C     1 
ATOM   3938  O  O     . PHE A 1 527 ? 153.035 180.605 172.972 1.00 33.74  ? 527 PHE A O     1 
ATOM   3939  C  CB    . PHE A 1 527 ? 149.877 181.039 173.267 1.00 23.48  ? 527 PHE A CB    1 
ATOM   3940  C  CG    . PHE A 1 527 ? 149.965 179.540 173.205 1.00 25.79  ? 527 PHE A CG    1 
ATOM   3941  C  CD1   . PHE A 1 527 ? 149.600 178.767 174.293 1.00 29.60  ? 527 PHE A CD1   1 
ATOM   3942  C  CD2   . PHE A 1 527 ? 150.427 178.906 172.063 1.00 23.91  ? 527 PHE A CD2   1 
ATOM   3943  C  CE1   . PHE A 1 527 ? 149.686 177.389 174.242 1.00 34.14  ? 527 PHE A CE1   1 
ATOM   3944  C  CE2   . PHE A 1 527 ? 150.516 177.529 172.006 1.00 25.77  ? 527 PHE A CE2   1 
ATOM   3945  C  CZ    . PHE A 1 527 ? 150.144 176.769 173.097 1.00 34.80  ? 527 PHE A CZ    1 
ATOM   3946  N  N     . VAL A 1 528 ? 152.480 182.589 172.059 1.00 22.01  ? 528 VAL A N     1 
ATOM   3947  C  CA    . VAL A 1 528 ? 153.641 182.594 171.173 1.00 24.21  ? 528 VAL A CA    1 
ATOM   3948  C  C     . VAL A 1 528 ? 154.926 182.664 171.988 1.00 25.88  ? 528 VAL A C     1 
ATOM   3949  O  O     . VAL A 1 528 ? 155.889 181.934 171.720 1.00 31.75  ? 528 VAL A O     1 
ATOM   3950  C  CB    . VAL A 1 528 ? 153.539 183.755 170.166 1.00 25.50  ? 528 VAL A CB    1 
ATOM   3951  C  CG1   . VAL A 1 528 ? 154.891 184.033 169.528 1.00 23.57  ? 528 VAL A CG1   1 
ATOM   3952  C  CG2   . VAL A 1 528 ? 152.501 183.442 169.101 1.00 23.47  ? 528 VAL A CG2   1 
ATOM   3953  N  N     . GLY A 1 529 ? 154.958 183.533 172.999 1.00 26.87  ? 529 GLY A N     1 
ATOM   3954  C  CA    . GLY A 1 529 ? 156.126 183.607 173.861 1.00 24.77  ? 529 GLY A CA    1 
ATOM   3955  C  C     . GLY A 1 529 ? 156.350 182.333 174.653 1.00 25.97  ? 529 GLY A C     1 
ATOM   3956  O  O     . GLY A 1 529 ? 157.490 181.899 174.840 1.00 32.12  ? 529 GLY A O     1 
ATOM   3957  N  N     . LEU A 1 530 ? 155.267 181.721 175.138 1.00 27.62  ? 530 LEU A N     1 
ATOM   3958  C  CA    . LEU A 1 530 ? 155.392 180.458 175.859 1.00 22.00  ? 530 LEU A CA    1 
ATOM   3959  C  C     . LEU A 1 530 ? 155.910 179.351 174.950 1.00 23.27  ? 530 LEU A C     1 
ATOM   3960  O  O     . LEU A 1 530 ? 156.771 178.560 175.352 1.00 22.76  ? 530 LEU A O     1 
ATOM   3961  C  CB    . LEU A 1 530 ? 154.046 180.065 176.469 1.00 21.49  ? 530 LEU A CB    1 
ATOM   3962  C  CG    . LEU A 1 530 ? 153.981 178.675 177.104 1.00 28.88  ? 530 LEU A CG    1 
ATOM   3963  C  CD1   . LEU A 1 530 ? 154.762 178.639 178.409 1.00 28.36  ? 530 LEU A CD1   1 
ATOM   3964  C  CD2   . LEU A 1 530 ? 152.539 178.253 177.325 1.00 28.95  ? 530 LEU A CD2   1 
ATOM   3965  N  N     . LEU A 1 531 ? 155.392 179.275 173.722 1.00 22.55  ? 531 LEU A N     1 
ATOM   3966  C  CA    . LEU A 1 531 ? 155.881 178.278 172.775 1.00 16.40  ? 531 LEU A CA    1 
ATOM   3967  C  C     . LEU A 1 531 ? 157.336 178.536 172.405 1.00 23.23  ? 531 LEU A C     1 
ATOM   3968  O  O     . LEU A 1 531 ? 158.132 177.595 172.302 1.00 18.97  ? 531 LEU A O     1 
ATOM   3969  C  CB    . LEU A 1 531 ? 155.002 178.265 171.525 1.00 20.49  ? 531 LEU A CB    1 
ATOM   3970  C  CG    . LEU A 1 531 ? 155.399 177.263 170.438 1.00 19.95  ? 531 LEU A CG    1 
ATOM   3971  C  CD1   . LEU A 1 531 ? 155.352 175.841 170.976 1.00 15.07  ? 531 LEU A CD1   1 
ATOM   3972  C  CD2   . LEU A 1 531 ? 154.505 177.410 169.218 1.00 20.50  ? 531 LEU A CD2   1 
ATOM   3973  N  N     . ILE A 1 532 ? 157.699 179.804 172.197 1.00 24.87  ? 532 ILE A N     1 
ATOM   3974  C  CA    . ILE A 1 532 ? 159.089 180.145 171.910 1.00 20.64  ? 532 ILE A CA    1 
ATOM   3975  C  C     . ILE A 1 532 ? 159.977 179.797 173.097 1.00 29.25  ? 532 ILE A C     1 
ATOM   3976  O  O     . ILE A 1 532 ? 161.060 179.221 172.935 1.00 29.33  ? 532 ILE A O     1 
ATOM   3977  C  CB    . ILE A 1 532 ? 159.203 181.634 171.530 1.00 27.60  ? 532 ILE A CB    1 
ATOM   3978  C  CG1   . ILE A 1 532 ? 158.719 181.858 170.097 1.00 22.77  ? 532 ILE A CG1   1 
ATOM   3979  C  CG2   . ILE A 1 532 ? 160.633 182.125 171.691 1.00 22.33  ? 532 ILE A CG2   1 
ATOM   3980  C  CD1   . ILE A 1 532 ? 158.525 183.314 169.744 1.00 22.93  ? 532 ILE A CD1   1 
ATOM   3981  N  N     . GLY A 1 533 ? 159.531 180.136 174.309 1.00 26.06  ? 533 GLY A N     1 
ATOM   3982  C  CA    . GLY A 1 533 ? 160.311 179.811 175.491 1.00 22.12  ? 533 GLY A CA    1 
ATOM   3983  C  C     . GLY A 1 533 ? 160.482 178.318 175.688 1.00 21.07  ? 533 GLY A C     1 
ATOM   3984  O  O     . GLY A 1 533 ? 161.558 177.853 176.071 1.00 28.85  ? 533 GLY A O     1 
ATOM   3985  N  N     . THR A 1 534 ? 159.423 177.546 175.433 1.00 26.19  ? 534 THR A N     1 
ATOM   3986  C  CA    . THR A 1 534 ? 159.516 176.096 175.562 1.00 24.63  ? 534 THR A CA    1 
ATOM   3987  C  C     . THR A 1 534 ? 160.521 175.515 174.574 1.00 27.38  ? 534 THR A C     1 
ATOM   3988  O  O     . THR A 1 534 ? 161.308 174.628 174.926 1.00 25.72  ? 534 THR A O     1 
ATOM   3989  C  CB    . THR A 1 534 ? 158.139 175.461 175.361 1.00 27.07  ? 534 THR A CB    1 
ATOM   3990  O  OG1   . THR A 1 534 ? 157.204 176.042 176.278 1.00 33.62  ? 534 THR A OG1   1 
ATOM   3991  C  CG2   . THR A 1 534 ? 158.202 173.959 175.597 1.00 25.50  ? 534 THR A CG2   1 
ATOM   3992  N  N     . VAL A 1 535 ? 160.509 176.002 173.332 1.00 27.36  ? 535 VAL A N     1 
ATOM   3993  C  CA    . VAL A 1 535 ? 161.432 175.491 172.323 1.00 24.18  ? 535 VAL A CA    1 
ATOM   3994  C  C     . VAL A 1 535 ? 162.865 175.893 172.653 1.00 29.54  ? 535 VAL A C     1 
ATOM   3995  O  O     . VAL A 1 535 ? 163.783 175.066 172.618 1.00 29.89  ? 535 VAL A O     1 
ATOM   3996  C  CB    . VAL A 1 535 ? 161.018 175.980 170.923 1.00 28.46  ? 535 VAL A CB    1 
ATOM   3997  C  CG1   . VAL A 1 535 ? 162.148 175.771 169.927 1.00 22.09  ? 535 VAL A CG1   1 
ATOM   3998  C  CG2   . VAL A 1 535 ? 159.756 175.268 170.463 1.00 23.62  ? 535 VAL A CG2   1 
ATOM   3999  N  N     . LEU A 1 536 ? 163.077 177.169 172.985 1.00 26.97  ? 536 LEU A N     1 
ATOM   4000  C  CA    . LEU A 1 536 ? 164.434 177.662 173.208 1.00 26.33  ? 536 LEU A CA    1 
ATOM   4001  C  C     . LEU A 1 536 ? 165.045 177.067 174.471 1.00 28.54  ? 536 LEU A C     1 
ATOM   4002  O  O     . LEU A 1 536 ? 166.202 176.632 174.464 1.00 36.21  ? 536 LEU A O     1 
ATOM   4003  C  CB    . LEU A 1 536 ? 164.439 179.191 173.281 1.00 27.55  ? 536 LEU A CB    1 
ATOM   4004  C  CG    . LEU A 1 536 ? 164.634 179.993 171.989 1.00 29.86  ? 536 LEU A CG    1 
ATOM   4005  C  CD1   . LEU A 1 536 ? 163.920 179.362 170.802 1.00 33.72  ? 536 LEU A CD1   1 
ATOM   4006  C  CD2   . LEU A 1 536 ? 164.189 181.436 172.184 1.00 29.29  ? 536 LEU A CD2   1 
ATOM   4007  N  N     . LEU A 1 537 ? 164.285 177.044 175.569 1.00 32.05  ? 537 LEU A N     1 
ATOM   4008  C  CA    . LEU A 1 537 ? 164.838 176.571 176.834 1.00 30.63  ? 537 LEU A CA    1 
ATOM   4009  C  C     . LEU A 1 537 ? 165.206 175.094 176.765 1.00 33.82  ? 537 LEU A C     1 
ATOM   4010  O  O     . LEU A 1 537 ? 166.273 174.691 177.240 1.00 43.61  ? 537 LEU A O     1 
ATOM   4011  C  CB    . LEU A 1 537 ? 163.849 176.827 177.971 1.00 32.47  ? 537 LEU A CB    1 
ATOM   4012  C  CG    . LEU A 1 537 ? 164.409 176.754 179.393 1.00 37.11  ? 537 LEU A CG    1 
ATOM   4013  C  CD1   . LEU A 1 537 ? 165.656 177.614 179.523 1.00 33.62  ? 537 LEU A CD1   1 
ATOM   4014  C  CD2   . LEU A 1 537 ? 163.355 177.179 180.401 1.00 35.01  ? 537 LEU A CD2   1 
ATOM   4015  N  N     . VAL A 1 538 ? 164.338 174.271 176.174 1.00 32.07  ? 538 VAL A N     1 
ATOM   4016  C  CA    . VAL A 1 538 ? 164.641 172.850 176.038 1.00 35.49  ? 538 VAL A CA    1 
ATOM   4017  C  C     . VAL A 1 538 ? 165.838 172.647 175.117 1.00 38.13  ? 538 VAL A C     1 
ATOM   4018  O  O     . VAL A 1 538 ? 166.755 171.875 175.423 1.00 37.82  ? 538 VAL A O     1 
ATOM   4019  C  CB    . VAL A 1 538 ? 163.403 172.083 175.536 1.00 34.57  ? 538 VAL A CB    1 
ATOM   4020  C  CG1   . VAL A 1 538 ? 163.814 170.782 174.863 1.00 35.74  ? 538 VAL A CG1   1 
ATOM   4021  C  CG2   . VAL A 1 538 ? 162.448 171.811 176.686 1.00 30.09  ? 538 VAL A CG2   1 
ATOM   4022  N  N     . GLY A 1 539 ? 165.853 173.345 173.980 1.00 30.59  ? 539 GLY A N     1 
ATOM   4023  C  CA    . GLY A 1 539 ? 166.947 173.181 173.037 1.00 26.63  ? 539 GLY A CA    1 
ATOM   4024  C  C     . GLY A 1 539 ? 168.274 173.682 173.572 1.00 31.14  ? 539 GLY A C     1 
ATOM   4025  O  O     . GLY A 1 539 ? 169.311 173.042 173.380 1.00 39.49  ? 539 GLY A O     1 
ATOM   4026  N  N     . ALA A 1 540 ? 168.265 174.835 174.244 1.00 23.64  ? 540 ALA A N     1 
ATOM   4027  C  CA    . ALA A 1 540 ? 169.509 175.395 174.763 1.00 31.99  ? 540 ALA A CA    1 
ATOM   4028  C  C     . ALA A 1 540 ? 170.090 174.522 175.869 1.00 26.64  ? 540 ALA A C     1 
ATOM   4029  O  O     . ALA A 1 540 ? 171.262 174.134 175.812 1.00 33.67  ? 540 ALA A O     1 
ATOM   4030  C  CB    . ALA A 1 540 ? 169.276 176.819 175.268 1.00 24.75  ? 540 ALA A CB    1 
ATOM   4031  N  N     . LEU A 1 541 ? 169.273 174.173 176.867 1.00 24.74  ? 541 LEU A N     1 
ATOM   4032  C  CA    . LEU A 1 541 ? 169.784 173.457 178.033 1.00 30.48  ? 541 LEU A CA    1 
ATOM   4033  C  C     . LEU A 1 541 ? 170.387 172.110 177.656 1.00 28.39  ? 541 LEU A C     1 
ATOM   4034  O  O     . LEU A 1 541 ? 171.268 171.606 178.362 1.00 33.81  ? 541 LEU A O     1 
ATOM   4035  C  CB    . LEU A 1 541 ? 168.669 173.266 179.062 1.00 30.45  ? 541 LEU A CB    1 
ATOM   4036  C  CG    . LEU A 1 541 ? 168.154 174.519 179.775 1.00 31.89  ? 541 LEU A CG    1 
ATOM   4037  C  CD1   . LEU A 1 541 ? 167.072 174.154 180.778 1.00 24.94  ? 541 LEU A CD1   1 
ATOM   4038  C  CD2   . LEU A 1 541 ? 169.288 175.271 180.452 1.00 31.06  ? 541 LEU A CD2   1 
ATOM   4039  N  N     . THR A 1 542 ? 169.931 171.513 176.555 1.00 22.88  ? 542 THR A N     1 
ATOM   4040  C  CA    . THR A 1 542 ? 170.466 170.220 176.143 1.00 18.34  ? 542 THR A CA    1 
ATOM   4041  C  C     . THR A 1 542 ? 171.859 170.359 175.538 1.00 25.42  ? 542 THR A C     1 
ATOM   4042  O  O     . THR A 1 542 ? 172.729 169.511 175.770 1.00 25.60  ? 542 THR A O     1 
ATOM   4043  C  CB    . THR A 1 542 ? 169.512 169.554 175.150 1.00 22.26  ? 542 THR A CB    1 
ATOM   4044  O  OG1   . THR A 1 542 ? 168.236 169.354 175.770 1.00 33.03  ? 542 THR A OG1   1 
ATOM   4045  C  CG2   . THR A 1 542 ? 170.061 168.210 174.692 1.00 22.18  ? 542 THR A CG2   1 
ATOM   4046  N  N     . PHE A 1 543 ? 172.098 171.426 174.775 1.00 16.35  ? 543 PHE A N     1 
ATOM   4047  C  CA    . PHE A 1 543 ? 173.295 171.532 173.949 1.00 10.84  ? 543 PHE A CA    1 
ATOM   4048  C  C     . PHE A 1 543 ? 174.258 172.629 174.393 1.00 17.55  ? 543 PHE A C     1 
ATOM   4049  O  O     . PHE A 1 543 ? 175.236 172.891 173.688 1.00 31.52  ? 543 PHE A O     1 
ATOM   4050  C  CB    . PHE A 1 543 ? 172.900 171.746 172.487 1.00 17.40  ? 543 PHE A CB    1 
ATOM   4051  C  CG    . PHE A 1 543 ? 172.229 170.556 171.863 1.00 19.02  ? 543 PHE A CG    1 
ATOM   4052  C  CD1   . PHE A 1 543 ? 172.980 169.510 171.352 1.00 17.97  ? 543 PHE A CD1   1 
ATOM   4053  C  CD2   . PHE A 1 543 ? 170.847 170.478 171.795 1.00 21.59  ? 543 PHE A CD2   1 
ATOM   4054  C  CE1   . PHE A 1 543 ? 172.367 168.412 170.782 1.00 18.27  ? 543 PHE A CE1   1 
ATOM   4055  C  CE2   . PHE A 1 543 ? 170.228 169.381 171.225 1.00 21.41  ? 543 PHE A CE2   1 
ATOM   4056  C  CZ    . PHE A 1 543 ? 170.990 168.347 170.718 1.00 17.40  ? 543 PHE A CZ    1 
ATOM   4057  N  N     . ILE A 1 544 ? 174.014 173.279 175.535 1.00 21.16  ? 544 ILE A N     1 
ATOM   4058  C  CA    . ILE A 1 544 ? 174.982 174.253 176.047 1.00 23.67  ? 544 ILE A CA    1 
ATOM   4059  C  C     . ILE A 1 544 ? 176.347 173.626 176.314 1.00 22.39  ? 544 ILE A C     1 
ATOM   4060  O  O     . ILE A 1 544 ? 177.357 174.190 175.863 1.00 20.66  ? 544 ILE A O     1 
ATOM   4061  C  CB    . ILE A 1 544 ? 174.411 174.978 177.280 1.00 22.66  ? 544 ILE A CB    1 
ATOM   4062  C  CG1   . ILE A 1 544 ? 173.370 176.017 176.864 1.00 25.69  ? 544 ILE A CG1   1 
ATOM   4063  C  CG2   . ILE A 1 544 ? 175.524 175.637 178.081 1.00 18.47  ? 544 ILE A CG2   1 
ATOM   4064  C  CD1   . ILE A 1 544 ? 173.884 177.032 175.870 1.00 32.83  ? 544 ILE A CD1   1 
ATOM   4065  N  N     . PRO A 1 545 ? 176.463 172.494 177.026 1.00 22.92  ? 545 PRO A N     1 
ATOM   4066  C  CA    . PRO A 1 545 ? 177.807 171.928 177.248 1.00 26.76  ? 545 PRO A CA    1 
ATOM   4067  C  C     . PRO A 1 545 ? 178.542 171.577 175.966 1.00 21.38  ? 545 PRO A C     1 
ATOM   4068  O  O     . PRO A 1 545 ? 179.759 171.785 175.880 1.00 21.14  ? 545 PRO A O     1 
ATOM   4069  C  CB    . PRO A 1 545 ? 177.524 170.681 178.100 1.00 22.99  ? 545 PRO A CB    1 
ATOM   4070  C  CG    . PRO A 1 545 ? 176.214 170.946 178.738 1.00 20.52  ? 545 PRO A CG    1 
ATOM   4071  C  CD    . PRO A 1 545 ? 175.429 171.705 177.721 1.00 22.44  ? 545 PRO A CD    1 
ATOM   4072  N  N     . ALA A 1 546 ? 177.837 171.052 174.962 1.00 24.89  ? 546 ALA A N     1 
ATOM   4073  C  CA    . ALA A 1 546 ? 178.492 170.708 173.705 1.00 21.50  ? 546 ALA A CA    1 
ATOM   4074  C  C     . ALA A 1 546 ? 178.925 171.957 172.947 1.00 16.73  ? 546 ALA A C     1 
ATOM   4075  O  O     . ALA A 1 546 ? 180.028 171.999 172.388 1.00 24.35  ? 546 ALA A O     1 
ATOM   4076  C  CB    . ALA A 1 546 ? 177.564 169.851 172.845 1.00 22.54  ? 546 ALA A CB    1 
ATOM   4077  N  N     . LEU A 1 547 ? 178.073 172.984 172.918 1.00 18.24  ? 547 LEU A N     1 
ATOM   4078  C  CA    . LEU A 1 547 ? 178.426 174.216 172.222 1.00 19.82  ? 547 LEU A CA    1 
ATOM   4079  C  C     . LEU A 1 547 ? 179.519 174.982 172.955 1.00 15.03  ? 547 LEU A C     1 
ATOM   4080  O  O     . LEU A 1 547 ? 180.296 175.706 172.322 1.00 20.76  ? 547 LEU A O     1 
ATOM   4081  C  CB    . LEU A 1 547 ? 177.187 175.093 172.044 1.00 20.88  ? 547 LEU A CB    1 
ATOM   4082  C  CG    . LEU A 1 547 ? 176.136 174.578 171.058 1.00 22.53  ? 547 LEU A CG    1 
ATOM   4083  C  CD1   . LEU A 1 547 ? 174.860 175.400 171.147 1.00 19.24  ? 547 LEU A CD1   1 
ATOM   4084  C  CD2   . LEU A 1 547 ? 176.683 174.580 169.639 1.00 17.43  ? 547 LEU A CD2   1 
ATOM   4085  N  N     . ALA A 1 548 ? 179.595 174.838 174.281 1.00 16.87  ? 548 ALA A N     1 
ATOM   4086  C  CA    . ALA A 1 548 ? 180.636 175.520 175.045 1.00 17.40  ? 548 ALA A CA    1 
ATOM   4087  C  C     . ALA A 1 548 ? 182.023 175.035 174.645 1.00 19.20  ? 548 ALA A C     1 
ATOM   4088  O  O     . ALA A 1 548 ? 182.969 175.828 174.571 1.00 23.82  ? 548 ALA A O     1 
ATOM   4089  C  CB    . ALA A 1 548 ? 180.408 175.316 176.543 1.00 14.38  ? 548 ALA A CB    1 
ATOM   4090  N  N     . LEU A 1 549 ? 182.165 173.737 174.385 1.00 18.99  ? 549 LEU A N     1 
ATOM   4091  C  CA    . LEU A 1 549 ? 183.445 173.165 173.987 1.00 22.23  ? 549 LEU A CA    1 
ATOM   4092  C  C     . LEU A 1 549 ? 183.731 173.324 172.499 1.00 21.52  ? 549 LEU A C     1 
ATOM   4093  O  O     . LEU A 1 549 ? 184.814 172.936 172.050 1.00 26.96  ? 549 LEU A O     1 
ATOM   4094  C  CB    . LEU A 1 549 ? 183.496 171.683 174.365 1.00 14.44  ? 549 LEU A CB    1 
ATOM   4095  C  CG    . LEU A 1 549 ? 183.404 171.361 175.859 1.00 23.44  ? 549 LEU A CG    1 
ATOM   4096  C  CD1   . LEU A 1 549 ? 183.674 169.888 176.108 1.00 14.62  ? 549 LEU A CD1   1 
ATOM   4097  C  CD2   . LEU A 1 549 ? 184.366 172.227 176.657 1.00 22.94  ? 549 LEU A CD2   1 
ATOM   4098  N  N     . GLY A 1 550 ? 182.799 173.881 171.731 1.00 20.75  ? 550 GLY A N     1 
ATOM   4099  C  CA    . GLY A 1 550 ? 182.988 174.060 170.312 1.00 15.76  ? 550 GLY A CA    1 
ATOM   4100  C  C     . GLY A 1 550 ? 183.076 175.518 169.912 1.00 16.37  ? 550 GLY A C     1 
ATOM   4101  O  O     . GLY A 1 550 ? 184.084 176.192 170.148 1.00 23.11  ? 550 GLY A O     1 
ATOM   4102  N  N     . PRO A 1 551 ? 182.016 176.029 169.281 1.00 18.41  ? 551 PRO A N     1 
ATOM   4103  C  CA    . PRO A 1 551 ? 182.046 177.424 168.806 1.00 19.34  ? 551 PRO A CA    1 
ATOM   4104  C  C     . PRO A 1 551 ? 182.233 178.451 169.911 1.00 15.25  ? 551 PRO A C     1 
ATOM   4105  O  O     . PRO A 1 551 ? 182.872 179.483 169.674 1.00 27.17  ? 551 PRO A O     1 
ATOM   4106  C  CB    . PRO A 1 551 ? 180.687 177.586 168.109 1.00 11.05  ? 551 PRO A CB    1 
ATOM   4107  C  CG    . PRO A 1 551 ? 179.825 176.505 168.677 1.00 22.24  ? 551 PRO A CG    1 
ATOM   4108  C  CD    . PRO A 1 551 ? 180.741 175.361 168.974 1.00 13.70  ? 551 PRO A CD    1 
ATOM   4109  N  N     . VAL A 1 552 ? 181.687 178.210 171.105 1.00 17.62  ? 552 VAL A N     1 
ATOM   4110  C  CA    . VAL A 1 552 ? 181.849 179.166 172.198 1.00 22.37  ? 552 VAL A CA    1 
ATOM   4111  C  C     . VAL A 1 552 ? 183.312 179.265 172.611 1.00 17.60  ? 552 VAL A C     1 
ATOM   4112  O  O     . VAL A 1 552 ? 183.838 180.365 172.822 1.00 22.45  ? 552 VAL A O     1 
ATOM   4113  C  CB    . VAL A 1 552 ? 180.949 178.782 173.386 1.00 21.03  ? 552 VAL A CB    1 
ATOM   4114  C  CG1   . VAL A 1 552 ? 181.194 179.715 174.562 1.00 22.66  ? 552 VAL A CG1   1 
ATOM   4115  C  CG2   . VAL A 1 552 ? 179.486 178.812 172.976 1.00 20.55  ? 552 VAL A CG2   1 
ATOM   4116  N  N     . ALA A 1 553 ? 183.992 178.123 172.734 1.00 23.00  ? 553 ALA A N     1 
ATOM   4117  C  CA    . ALA A 1 553 ? 185.416 178.142 173.054 1.00 23.64  ? 553 ALA A CA    1 
ATOM   4118  C  C     . ALA A 1 553 ? 186.221 178.796 171.938 1.00 24.01  ? 553 ALA A C     1 
ATOM   4119  O  O     . ALA A 1 553 ? 187.182 179.527 172.202 1.00 30.07  ? 553 ALA A O     1 
ATOM   4120  C  CB    . ALA A 1 553 ? 185.916 176.722 173.320 1.00 18.23  ? 553 ALA A CB    1 
ATOM   4121  N  N     . GLU A 1 554 ? 185.846 178.536 170.683 1.00 19.17  ? 554 GLU A N     1 
ATOM   4122  C  CA    . GLU A 1 554 ? 186.531 179.166 169.559 1.00 28.36  ? 554 GLU A CA    1 
ATOM   4123  C  C     . GLU A 1 554 ? 186.327 180.676 169.561 1.00 20.13  ? 554 GLU A C     1 
ATOM   4124  O  O     . GLU A 1 554 ? 187.260 181.437 169.278 1.00 29.36  ? 554 GLU A O     1 
ATOM   4125  C  CB    . GLU A 1 554 ? 186.042 178.560 168.244 1.00 19.75  ? 554 GLU A CB    1 
ATOM   4126  C  CG    . GLU A 1 554 ? 186.991 178.763 167.075 1.00 28.26  ? 554 GLU A CG    1 
ATOM   4127  C  CD    . GLU A 1 554 ? 186.282 178.733 165.735 1.00 29.57  ? 554 GLU A CD    1 
ATOM   4128  O  OE1   . GLU A 1 554 ? 185.333 177.936 165.580 1.00 32.44  ? 554 GLU A OE1   1 
ATOM   4129  O  OE2   . GLU A 1 554 ? 186.675 179.504 164.835 1.00 35.34  ? 554 GLU A OE2   1 
ATOM   4130  N  N     . TYR A 1 555 ? 185.108 181.128 169.869 1.00 17.38  ? 555 TYR A N     1 
ATOM   4131  C  CA    . TYR A 1 555 ? 184.826 182.561 169.876 1.00 23.78  ? 555 TYR A CA    1 
ATOM   4132  C  C     . TYR A 1 555 ? 185.605 183.281 170.969 1.00 28.76  ? 555 TYR A C     1 
ATOM   4133  O  O     . TYR A 1 555 ? 186.120 184.383 170.749 1.00 34.34  ? 555 TYR A O     1 
ATOM   4134  C  CB    . TYR A 1 555 ? 183.326 182.799 170.044 1.00 24.31  ? 555 TYR A CB    1 
ATOM   4135  C  CG    . TYR A 1 555 ? 182.947 184.259 170.130 1.00 32.23  ? 555 TYR A CG    1 
ATOM   4136  C  CD1   . TYR A 1 555 ? 182.993 185.075 169.008 1.00 31.69  ? 555 TYR A CD1   1 
ATOM   4137  C  CD2   . TYR A 1 555 ? 182.544 184.823 171.334 1.00 30.89  ? 555 TYR A CD2   1 
ATOM   4138  C  CE1   . TYR A 1 555 ? 182.648 186.411 169.081 1.00 30.87  ? 555 TYR A CE1   1 
ATOM   4139  C  CE2   . TYR A 1 555 ? 182.198 186.157 171.417 1.00 29.23  ? 555 TYR A CE2   1 
ATOM   4140  C  CZ    . TYR A 1 555 ? 182.251 186.946 170.288 1.00 36.73  ? 555 TYR A CZ    1 
ATOM   4141  O  OH    . TYR A 1 555 ? 181.907 188.276 170.366 1.00 40.72  ? 555 TYR A OH    1 
ATOM   4142  N  N     . LEU A 1 556 ? 185.701 182.678 172.154 1.00 26.90  ? 556 LEU A N     1 
ATOM   4143  C  CA    . LEU A 1 556 ? 186.354 183.323 173.285 1.00 24.55  ? 556 LEU A CA    1 
ATOM   4144  C  C     . LEU A 1 556 ? 187.872 183.210 173.245 1.00 23.31  ? 556 LEU A C     1 
ATOM   4145  O  O     . LEU A 1 556 ? 188.544 183.852 174.059 1.00 37.19  ? 556 LEU A O     1 
ATOM   4146  C  CB    . LEU A 1 556 ? 185.827 182.735 174.596 1.00 24.86  ? 556 LEU A CB    1 
ATOM   4147  C  CG    . LEU A 1 556 ? 184.355 183.026 174.896 1.00 25.73  ? 556 LEU A CG    1 
ATOM   4148  C  CD1   . LEU A 1 556 ? 183.918 182.342 176.181 1.00 26.99  ? 556 LEU A CD1   1 
ATOM   4149  C  CD2   . LEU A 1 556 ? 184.111 184.526 174.971 1.00 26.26  ? 556 LEU A CD2   1 
ATOM   4150  N  N     . SER A 1 557 ? 188.426 182.421 172.330 1.00 26.98  ? 557 SER A N     1 
ATOM   4151  C  CA    . SER A 1 557 ? 189.873 182.275 172.223 1.00 28.70  ? 557 SER A CA    1 
ATOM   4152  C  C     . SER A 1 557 ? 190.464 183.332 171.295 1.00 39.21  ? 557 SER A C     1 
ATOM   4153  O  O     . SER A 1 557 ? 190.403 184.527 171.582 1.00 40.25  ? 557 SER A O     1 
ATOM   4154  C  CB    . SER A 1 557 ? 190.236 180.876 171.724 1.00 29.33  ? 557 SER A CB    1 
ATOM   4155  O  OG    . SER A 1 557 ? 189.720 180.647 170.425 1.00 40.79  ? 557 SER A OG    1 
ATOM   4156  N  N     . SER B 2 2   ? 138.916 166.914 212.663 1.00 82.81  ? 2   SER B N     1 
ATOM   4157  C  CA    . SER B 2 2   ? 138.617 167.331 211.269 1.00 83.32  ? 2   SER B CA    1 
ATOM   4158  C  C     . SER B 2 2   ? 138.439 168.850 211.229 1.00 83.99  ? 2   SER B C     1 
ATOM   4159  O  O     . SER B 2 2   ? 137.632 169.353 212.036 1.00 83.17  ? 2   SER B O     1 
ATOM   4160  C  CB    . SER B 2 2   ? 137.406 166.611 210.759 1.00 81.25  ? 2   SER B CB    1 
ATOM   4161  O  OG    . SER B 2 2   ? 137.549 165.211 210.934 1.00 82.04  ? 2   SER B OG    1 
ATOM   4162  N  N     . ARG B 2 3   ? 139.217 169.551 210.400 1.00 81.98  ? 3   ARG B N     1 
ATOM   4163  C  CA    . ARG B 2 3   ? 139.102 171.033 210.232 1.00 81.30  ? 3   ARG B CA    1 
ATOM   4164  C  C     . ARG B 2 3   ? 139.869 171.816 211.310 1.00 81.34  ? 3   ARG B C     1 
ATOM   4165  O  O     . ARG B 2 3   ? 139.864 173.056 211.229 1.00 81.35  ? 3   ARG B O     1 
ATOM   4166  C  CB    . ARG B 2 3   ? 137.642 171.503 210.178 1.00 80.41  ? 3   ARG B CB    1 
ATOM   4167  C  CG    . ARG B 2 3   ? 137.459 172.806 209.412 1.00 80.82  ? 3   ARG B CG    1 
ATOM   4168  C  CD    . ARG B 2 3   ? 136.500 173.793 210.048 1.00 81.31  ? 3   ARG B CD    1 
ATOM   4169  N  NE    . ARG B 2 3   ? 135.116 173.467 209.747 1.00 82.36  ? 3   ARG B NE    1 
ATOM   4170  C  CZ    . ARG B 2 3   ? 134.328 174.197 208.966 1.00 81.45  ? 3   ARG B CZ    1 
ATOM   4171  N  NH1   . ARG B 2 3   ? 133.259 173.652 208.415 1.00 79.83  ? 3   ARG B NH1   1 
ATOM   4172  N  NH2   . ARG B 2 3   ? 134.625 175.462 208.719 1.00 79.80  ? 3   ARG B NH2   1 
ATOM   4173  N  N     . LYS B 2 4   ? 140.519 171.149 212.266 1.00 86.58  ? 4   LYS B N     1 
ATOM   4174  C  CA    . LYS B 2 4   ? 141.374 171.886 213.239 1.00 87.94  ? 4   LYS B CA    1 
ATOM   4175  C  C     . LYS B 2 4   ? 142.828 171.714 212.792 1.00 87.92  ? 4   LYS B C     1 
ATOM   4176  O  O     . LYS B 2 4   ? 143.369 170.614 212.991 1.00 87.55  ? 4   LYS B O     1 
ATOM   4177  C  CB    . LYS B 2 4   ? 141.165 171.328 214.646 1.00 87.18  ? 4   LYS B CB    1 
ATOM   4178  C  CG    . LYS B 2 4   ? 139.778 170.755 214.902 1.00 87.68  ? 4   LYS B CG    1 
ATOM   4179  C  CD    . LYS B 2 4   ? 139.698 169.947 216.177 1.00 87.90  ? 4   LYS B CD    1 
ATOM   4180  C  CE    . LYS B 2 4   ? 138.357 169.271 216.359 1.00 87.78  ? 4   LYS B CE    1 
ATOM   4181  N  NZ    . LYS B 2 4   ? 138.317 168.463 217.601 1.00 87.24  ? 4   LYS B NZ    1 
ATOM   4182  N  N     . GLN B 2 5   ? 143.448 172.761 212.243 1.00 86.28  ? 5   GLN B N     1 
ATOM   4183  C  CA    . GLN B 2 5   ? 144.816 172.606 211.676 1.00 86.47  ? 5   GLN B CA    1 
ATOM   4184  C  C     . GLN B 2 5   ? 145.841 172.509 212.808 1.00 86.46  ? 5   GLN B C     1 
ATOM   4185  O  O     . GLN B 2 5   ? 145.604 173.123 213.864 1.00 86.96  ? 5   GLN B O     1 
ATOM   4186  C  CB    . GLN B 2 5   ? 145.140 173.791 210.768 1.00 85.66  ? 5   GLN B CB    1 
ATOM   4187  C  CG    . GLN B 2 5   ? 143.965 174.249 209.916 1.00 85.66  ? 5   GLN B CG    1 
ATOM   4188  C  CD    . GLN B 2 5   ? 143.391 173.140 209.068 1.00 86.64  ? 5   GLN B CD    1 
ATOM   4189  O  OE1   . GLN B 2 5   ? 144.073 172.558 208.228 1.00 85.51  ? 5   GLN B OE1   1 
ATOM   4190  N  NE2   . GLN B 2 5   ? 142.121 172.841 209.283 1.00 85.49  ? 5   GLN B NE2   1 
ATOM   4191  N  N     . LEU B 2 6   ? 146.940 171.779 212.590 1.00 83.91  ? 6   LEU B N     1 
ATOM   4192  C  CA    . LEU B 2 6   ? 147.913 171.607 213.665 1.00 85.17  ? 6   LEU B CA    1 
ATOM   4193  C  C     . LEU B 2 6   ? 149.018 172.659 213.607 1.00 84.61  ? 6   LEU B C     1 
ATOM   4194  O  O     . LEU B 2 6   ? 149.111 173.517 214.491 1.00 84.99  ? 6   LEU B O     1 
ATOM   4195  C  CB    . LEU B 2 6   ? 148.517 170.198 213.598 1.00 84.60  ? 6   LEU B CB    1 
ATOM   4196  C  CG    . LEU B 2 6   ? 149.359 169.733 214.790 1.00 84.39  ? 6   LEU B CG    1 
ATOM   4197  C  CD1   . LEU B 2 6   ? 148.779 170.244 216.100 1.00 83.88  ? 6   LEU B CD1   1 
ATOM   4198  C  CD2   . LEU B 2 6   ? 149.486 168.215 214.807 1.00 83.99  ? 6   LEU B CD2   1 
ATOM   4199  N  N     . ALA B 2 7   ? 149.842 172.617 212.563 1.00 77.49  ? 7   ALA B N     1 
ATOM   4200  C  CA    . ALA B 2 7   ? 150.968 173.529 212.391 1.00 77.49  ? 7   ALA B CA    1 
ATOM   4201  C  C     . ALA B 2 7   ? 151.605 173.231 211.040 1.00 78.00  ? 7   ALA B C     1 
ATOM   4202  O  O     . ALA B 2 7   ? 151.176 172.329 210.314 1.00 78.07  ? 7   ALA B O     1 
ATOM   4203  C  CB    . ALA B 2 7   ? 152.007 173.400 213.508 1.00 77.39  ? 7   ALA B CB    1 
ATOM   4204  N  N     . LEU B 2 8   ? 152.692 173.934 210.727 1.00 73.55  ? 8   LEU B N     1 
ATOM   4205  C  CA    . LEU B 2 8   ? 153.372 173.548 209.461 1.00 72.81  ? 8   LEU B CA    1 
ATOM   4206  C  C     . LEU B 2 8   ? 154.617 172.780 209.876 1.00 71.95  ? 8   LEU B C     1 
ATOM   4207  O  O     . LEU B 2 8   ? 154.951 171.791 209.216 1.00 71.43  ? 8   LEU B O     1 
ATOM   4208  C  CB    . LEU B 2 8   ? 153.705 174.780 208.612 1.00 72.70  ? 8   LEU B CB    1 
ATOM   4209  C  CG    . LEU B 2 8   ? 154.044 174.498 207.149 1.00 73.78  ? 8   LEU B CG    1 
ATOM   4210  C  CD1   . LEU B 2 8   ? 152.778 174.286 206.334 1.00 71.51  ? 8   LEU B CD1   1 
ATOM   4211  C  CD2   . LEU B 2 8   ? 154.868 175.630 206.559 1.00 70.05  ? 8   LEU B CD2   1 
ATOM   4212  N  N     . PHE B 2 9   ? 155.226 173.211 210.971 1.00 72.00  ? 9   PHE B N     1 
ATOM   4213  C  CA    . PHE B 2 9   ? 156.415 172.510 211.490 1.00 71.84  ? 9   PHE B CA    1 
ATOM   4214  C  C     . PHE B 2 9   ? 156.248 172.243 212.990 1.00 73.05  ? 9   PHE B C     1 
ATOM   4215  O  O     . PHE B 2 9   ? 156.944 172.906 213.789 1.00 72.55  ? 9   PHE B O     1 
ATOM   4216  C  CB    . PHE B 2 9   ? 157.661 173.344 211.219 1.00 70.89  ? 9   PHE B CB    1 
ATOM   4217  C  CG    . PHE B 2 9   ? 158.164 173.339 209.799 1.00 72.79  ? 9   PHE B CG    1 
ATOM   4218  C  CD1   . PHE B 2 9   ? 158.685 172.189 209.231 1.00 71.62  ? 9   PHE B CD1   1 
ATOM   4219  C  CD2   . PHE B 2 9   ? 158.133 174.493 209.034 1.00 73.00  ? 9   PHE B CD2   1 
ATOM   4220  C  CE1   . PHE B 2 9   ? 159.162 172.193 207.931 1.00 70.19  ? 9   PHE B CE1   1 
ATOM   4221  C  CE2   . PHE B 2 9   ? 158.604 174.492 207.732 1.00 73.11  ? 9   PHE B CE2   1 
ATOM   4222  C  CZ    . PHE B 2 9   ? 159.117 173.342 207.181 1.00 70.88  ? 9   PHE B CZ    1 
ATOM   4223  N  N     . GLU B 2 10  ? 155.368 171.315 213.367 1.00 69.68  ? 10  GLU B N     1 
ATOM   4224  C  CA    . GLU B 2 10  ? 155.242 170.911 214.791 1.00 68.61  ? 10  GLU B CA    1 
ATOM   4225  C  C     . GLU B 2 10  ? 156.572 170.283 215.216 1.00 70.65  ? 10  GLU B C     1 
ATOM   4226  O  O     . GLU B 2 10  ? 157.022 169.384 214.504 1.00 71.44  ? 10  GLU B O     1 
ATOM   4227  C  CB    . GLU B 2 10  ? 154.162 169.838 214.948 1.00 30.00  ? 10  GLU B CB    1 
ATOM   4228  C  CG    . GLU B 2 10  ? 152.895 170.110 214.164 1.00 30.00  ? 10  GLU B CG    1 
ATOM   4229  C  CD    . GLU B 2 10  ? 152.952 169.767 212.684 1.00 30.00  ? 10  GLU B CD    1 
ATOM   4230  O  OE1   . GLU B 2 10  ? 154.029 169.341 212.217 1.00 30.00  ? 10  GLU B OE1   1 
ATOM   4231  O  OE2   . GLU B 2 10  ? 151.915 169.923 212.003 1.00 30.00  ? 10  GLU B OE2   1 
ATOM   4232  N  N     . PRO B 2 11  ? 157.203 170.622 216.359 1.00 68.43  ? 11  PRO B N     1 
ATOM   4233  C  CA    . PRO B 2 11  ? 158.460 169.964 216.758 1.00 64.76  ? 11  PRO B CA    1 
ATOM   4234  C  C     . PRO B 2 11  ? 158.340 168.464 216.952 1.00 65.69  ? 11  PRO B C     1 
ATOM   4235  O  O     . PRO B 2 11  ? 159.331 167.747 216.765 1.00 65.39  ? 11  PRO B O     1 
ATOM   4236  C  CB    . PRO B 2 11  ? 158.829 170.678 218.070 1.00 65.30  ? 11  PRO B CB    1 
ATOM   4237  C  CG    . PRO B 2 11  ? 157.952 171.906 218.118 1.00 65.70  ? 11  PRO B CG    1 
ATOM   4238  C  CD    . PRO B 2 11  ? 156.703 171.526 217.405 1.00 65.88  ? 11  PRO B CD    1 
ATOM   4239  N  N     . THR B 2 12  ? 157.161 167.963 217.325 1.00 64.03  ? 12  THR B N     1 
ATOM   4240  C  CA    . THR B 2 12  ? 157.002 166.524 217.508 1.00 64.21  ? 12  THR B CA    1 
ATOM   4241  C  C     . THR B 2 12  ? 157.084 165.781 216.179 1.00 64.84  ? 12  THR B C     1 
ATOM   4242  O  O     . THR B 2 12  ? 157.602 164.660 216.121 1.00 66.46  ? 12  THR B O     1 
ATOM   4243  C  CB    . THR B 2 12  ? 155.677 166.224 218.208 1.00 66.96  ? 12  THR B CB    1 
ATOM   4244  O  OG1   . THR B 2 12  ? 155.349 167.301 219.095 1.00 65.94  ? 12  THR B OG1   1 
ATOM   4245  C  CG2   . THR B 2 12  ? 155.777 164.931 219.004 1.00 65.69  ? 12  THR B CG2   1 
ATOM   4246  N  N     . LEU B 2 13  ? 156.580 166.386 215.102 1.00 59.84  ? 13  LEU B N     1 
ATOM   4247  C  CA    . LEU B 2 13  ? 156.558 165.713 213.809 1.00 60.49  ? 13  LEU B CA    1 
ATOM   4248  C  C     . LEU B 2 13  ? 157.773 166.030 212.946 1.00 58.56  ? 13  LEU B C     1 
ATOM   4249  O  O     . LEU B 2 13  ? 158.119 165.223 212.076 1.00 60.23  ? 13  LEU B O     1 
ATOM   4250  C  CB    . LEU B 2 13  ? 155.279 166.070 213.049 1.00 58.37  ? 13  LEU B CB    1 
ATOM   4251  C  CG    . LEU B 2 13  ? 153.978 165.546 213.661 1.00 58.96  ? 13  LEU B CG    1 
ATOM   4252  C  CD1   . LEU B 2 13  ? 152.781 166.315 213.130 1.00 58.00  ? 13  LEU B CD1   1 
ATOM   4253  C  CD2   . LEU B 2 13  ? 153.821 164.055 213.398 1.00 59.54  ? 13  LEU B CD2   1 
ATOM   4254  N  N     . VAL B 2 14  ? 158.421 167.179 213.152 1.00 55.76  ? 14  VAL B N     1 
ATOM   4255  C  CA    . VAL B 2 14  ? 159.628 167.491 212.390 1.00 55.06  ? 14  VAL B CA    1 
ATOM   4256  C  C     . VAL B 2 14  ? 160.745 166.516 212.740 1.00 53.70  ? 14  VAL B C     1 
ATOM   4257  O  O     . VAL B 2 14  ? 161.460 166.024 211.859 1.00 55.15  ? 14  VAL B O     1 
ATOM   4258  C  CB    . VAL B 2 14  ? 160.057 168.951 212.625 1.00 54.70  ? 14  VAL B CB    1 
ATOM   4259  C  CG1   . VAL B 2 14  ? 161.291 169.275 211.802 1.00 52.41  ? 14  VAL B CG1   1 
ATOM   4260  C  CG2   . VAL B 2 14  ? 158.929 169.897 212.256 1.00 55.07  ? 14  VAL B CG2   1 
ATOM   4261  N  N     . VAL B 2 15  ? 160.910 166.217 214.031 1.00 54.29  ? 15  VAL B N     1 
ATOM   4262  C  CA    . VAL B 2 15  ? 161.935 165.262 214.438 1.00 56.57  ? 15  VAL B CA    1 
ATOM   4263  C  C     . VAL B 2 15  ? 161.575 163.859 213.963 1.00 55.76  ? 15  VAL B C     1 
ATOM   4264  O  O     . VAL B 2 15  ? 162.457 163.050 213.650 1.00 58.48  ? 15  VAL B O     1 
ATOM   4265  C  CB    . VAL B 2 15  ? 162.149 165.314 215.963 1.00 56.87  ? 15  VAL B CB    1 
ATOM   4266  C  CG1   . VAL B 2 15  ? 162.613 166.700 216.386 1.00 56.56  ? 15  VAL B CG1   1 
ATOM   4267  C  CG2   . VAL B 2 15  ? 160.881 164.921 216.706 1.00 56.29  ? 15  VAL B CG2   1 
ATOM   4268  N  N     . GLN B 2 16  ? 160.278 163.547 213.899 1.00 48.66  ? 16  GLN B N     1 
ATOM   4269  C  CA    . GLN B 2 16  ? 159.860 162.246 213.388 1.00 50.92  ? 16  GLN B CA    1 
ATOM   4270  C  C     . GLN B 2 16  ? 159.982 162.186 211.871 1.00 50.17  ? 16  GLN B C     1 
ATOM   4271  O  O     . GLN B 2 16  ? 160.092 161.099 211.294 1.00 49.72  ? 16  GLN B O     1 
ATOM   4272  C  CB    . GLN B 2 16  ? 158.426 161.947 213.826 1.00 51.37  ? 16  GLN B CB    1 
ATOM   4273  C  CG    . GLN B 2 16  ? 158.095 160.463 213.942 1.00 52.19  ? 16  GLN B CG    1 
ATOM   4274  C  CD    . GLN B 2 16  ? 159.255 159.628 214.453 1.00 56.37  ? 16  GLN B CD    1 
ATOM   4275  O  OE1   . GLN B 2 16  ? 159.687 158.680 213.798 1.00 56.56  ? 16  GLN B OE1   1 
ATOM   4276  N  NE2   . GLN B 2 16  ? 159.748 159.960 215.643 1.00 54.95  ? 16  GLN B NE2   1 
ATOM   4277  N  N     . ALA B 2 17  ? 159.970 163.345 211.208 1.00 48.43  ? 17  ALA B N     1 
ATOM   4278  C  CA    . ALA B 2 17  ? 160.135 163.364 209.759 1.00 46.49  ? 17  ALA B CA    1 
ATOM   4279  C  C     . ALA B 2 17  ? 161.594 163.173 209.368 1.00 46.39  ? 17  ALA B C     1 
ATOM   4280  O  O     . ALA B 2 17  ? 161.891 162.577 208.327 1.00 45.88  ? 17  ALA B O     1 
ATOM   4281  C  CB    . ALA B 2 17  ? 159.588 164.669 209.183 1.00 43.02  ? 17  ALA B CB    1 
ATOM   4282  N  N     . LEU B 2 18  ? 162.520 163.671 210.192 1.00 48.13  ? 18  LEU B N     1 
ATOM   4283  C  CA    . LEU B 2 18  ? 163.938 163.466 209.915 1.00 47.73  ? 18  LEU B CA    1 
ATOM   4284  C  C     . LEU B 2 18  ? 164.330 162.009 210.120 1.00 48.17  ? 18  LEU B C     1 
ATOM   4285  O  O     . LEU B 2 18  ? 165.237 161.501 209.451 1.00 51.75  ? 18  LEU B O     1 
ATOM   4286  C  CB    . LEU B 2 18  ? 164.786 164.378 210.801 1.00 47.87  ? 18  LEU B CB    1 
ATOM   4287  C  CG    . LEU B 2 18  ? 164.580 165.885 210.641 1.00 51.23  ? 18  LEU B CG    1 
ATOM   4288  C  CD1   . LEU B 2 18  ? 164.732 166.590 211.980 1.00 50.13  ? 18  LEU B CD1   1 
ATOM   4289  C  CD2   . LEU B 2 18  ? 165.551 166.456 209.620 1.00 47.98  ? 18  LEU B CD2   1 
ATOM   4290  N  N     . LYS B 2 19  ? 163.657 161.319 211.044 1.00 45.84  ? 19  LYS B N     1 
ATOM   4291  C  CA    . LYS B 2 19  ? 163.933 159.902 211.249 1.00 45.15  ? 19  LYS B CA    1 
ATOM   4292  C  C     . LYS B 2 19  ? 163.411 159.070 210.086 1.00 45.31  ? 19  LYS B C     1 
ATOM   4293  O  O     . LYS B 2 19  ? 164.068 158.119 209.649 1.00 50.57  ? 19  LYS B O     1 
ATOM   4294  C  CB    . LYS B 2 19  ? 163.318 159.432 212.568 1.00 49.74  ? 19  LYS B CB    1 
ATOM   4295  C  CG    . LYS B 2 19  ? 163.951 160.052 213.802 1.00 50.11  ? 19  LYS B CG    1 
ATOM   4296  C  CD    . LYS B 2 19  ? 163.409 159.425 215.077 1.00 50.33  ? 19  LYS B CD    1 
ATOM   4297  C  CE    . LYS B 2 19  ? 163.988 160.097 216.311 1.00 50.30  ? 19  LYS B CE    1 
ATOM   4298  N  NZ    . LYS B 2 19  ? 163.529 159.445 217.568 1.00 51.45  ? 19  LYS B NZ    1 
ATOM   4299  N  N     . GLU B 2 20  ? 162.231 159.418 209.566 1.00 43.50  ? 20  GLU B N     1 
ATOM   4300  C  CA    . GLU B 2 20  ? 161.694 158.701 208.414 1.00 44.74  ? 20  GLU B CA    1 
ATOM   4301  C  C     . GLU B 2 20  ? 162.472 159.017 207.144 1.00 43.90  ? 20  GLU B C     1 
ATOM   4302  O  O     . GLU B 2 20  ? 162.541 158.180 206.238 1.00 42.26  ? 20  GLU B O     1 
ATOM   4303  C  CB    . GLU B 2 20  ? 160.214 159.037 208.225 1.00 41.13  ? 20  GLU B CB    1 
ATOM   4304  C  CG    . GLU B 2 20  ? 159.328 158.618 209.385 1.00 47.93  ? 20  GLU B CG    1 
ATOM   4305  C  CD    . GLU B 2 20  ? 159.486 157.154 209.740 1.00 51.10  ? 20  GLU B CD    1 
ATOM   4306  O  OE1   . GLU B 2 20  ? 159.196 156.297 208.879 1.00 52.48  ? 20  GLU B OE1   1 
ATOM   4307  O  OE2   . GLU B 2 20  ? 159.902 156.859 210.880 1.00 49.91  ? 20  GLU B OE2   1 
ATOM   4308  N  N     . ALA B 2 21  ? 163.061 160.212 207.058 1.00 41.92  ? 21  ALA B N     1 
ATOM   4309  C  CA    . ALA B 2 21  ? 163.855 160.558 205.885 1.00 39.33  ? 21  ALA B CA    1 
ATOM   4310  C  C     . ALA B 2 21  ? 165.134 159.733 205.825 1.00 42.82  ? 21  ALA B C     1 
ATOM   4311  O  O     . ALA B 2 21  ? 165.601 159.375 204.737 1.00 41.70  ? 21  ALA B O     1 
ATOM   4312  C  CB    . ALA B 2 21  ? 164.177 162.052 205.890 1.00 37.07  ? 21  ALA B CB    1 
ATOM   4313  N  N     . VAL B 2 22  ? 165.716 159.425 206.986 1.00 43.20  ? 22  VAL B N     1 
ATOM   4314  C  CA    . VAL B 2 22  ? 166.912 158.588 207.022 1.00 40.25  ? 22  VAL B CA    1 
ATOM   4315  C  C     . VAL B 2 22  ? 166.589 157.177 206.548 1.00 41.84  ? 22  VAL B C     1 
ATOM   4316  O  O     . VAL B 2 22  ? 167.335 156.583 205.759 1.00 49.12  ? 22  VAL B O     1 
ATOM   4317  C  CB    . VAL B 2 22  ? 167.522 158.590 208.436 1.00 43.14  ? 22  VAL B CB    1 
ATOM   4318  C  CG1   . VAL B 2 22  ? 168.450 157.400 208.624 1.00 43.74  ? 22  VAL B CG1   1 
ATOM   4319  C  CG2   . VAL B 2 22  ? 168.261 159.894 208.691 1.00 40.41  ? 22  VAL B CG2   1 
ATOM   4320  N  N     . LYS B 2 23  ? 165.465 156.620 207.008 1.00 36.76  ? 23  LYS B N     1 
ATOM   4321  C  CA    . LYS B 2 23  ? 165.078 155.278 206.589 1.00 41.86  ? 23  LYS B CA    1 
ATOM   4322  C  C     . LYS B 2 23  ? 164.571 155.241 205.154 1.00 41.76  ? 23  LYS B C     1 
ATOM   4323  O  O     . LYS B 2 23  ? 164.388 154.151 204.604 1.00 44.21  ? 23  LYS B O     1 
ATOM   4324  C  CB    . LYS B 2 23  ? 164.014 154.714 207.532 1.00 43.16  ? 23  LYS B CB    1 
ATOM   4325  C  CG    . LYS B 2 23  ? 164.261 155.019 208.999 1.00 46.51  ? 23  LYS B CG    1 
ATOM   4326  C  CD    . LYS B 2 23  ? 163.598 153.989 209.897 1.00 47.00  ? 23  LYS B CD    1 
ATOM   4327  C  CE    . LYS B 2 23  ? 162.120 154.290 210.083 1.00 45.95  ? 23  LYS B CE    1 
ATOM   4328  N  NZ    . LYS B 2 23  ? 161.882 155.226 211.216 1.00 45.31  ? 23  LYS B NZ    1 
ATOM   4329  N  N     . LYS B 2 24  ? 164.343 156.401 204.537 1.00 39.63  ? 24  LYS B N     1 
ATOM   4330  C  CA    . LYS B 2 24  ? 163.980 156.451 203.128 1.00 41.22  ? 24  LYS B CA    1 
ATOM   4331  C  C     . LYS B 2 24  ? 165.194 156.426 202.212 1.00 40.14  ? 24  LYS B C     1 
ATOM   4332  O  O     . LYS B 2 24  ? 165.027 156.388 200.988 1.00 43.87  ? 24  LYS B O     1 
ATOM   4333  C  CB    . LYS B 2 24  ? 163.144 157.701 202.841 1.00 38.73  ? 24  LYS B CB    1 
ATOM   4334  C  CG    . LYS B 2 24  ? 161.662 157.547 203.141 1.00 38.55  ? 24  LYS B CG    1 
ATOM   4335  C  CD    . LYS B 2 24  ? 160.991 158.903 203.300 1.00 39.08  ? 24  LYS B CD    1 
ATOM   4336  C  CE    . LYS B 2 24  ? 159.487 158.764 203.474 1.00 42.32  ? 24  LYS B CE    1 
ATOM   4337  N  NZ    . LYS B 2 24  ? 158.858 158.055 202.327 1.00 39.60  ? 24  LYS B NZ    1 
ATOM   4338  N  N     . LEU B 2 25  ? 166.406 156.444 202.772 1.00 38.79  ? 25  LEU B N     1 
ATOM   4339  C  CA    . LEU B 2 25  ? 167.625 156.353 201.978 1.00 37.60  ? 25  LEU B CA    1 
ATOM   4340  C  C     . LEU B 2 25  ? 167.847 154.963 201.400 1.00 42.87  ? 25  LEU B C     1 
ATOM   4341  O  O     . LEU B 2 25  ? 168.758 154.791 200.584 1.00 47.67  ? 25  LEU B O     1 
ATOM   4342  C  CB    . LEU B 2 25  ? 168.834 156.755 202.824 1.00 36.86  ? 25  LEU B CB    1 
ATOM   4343  C  CG    . LEU B 2 25  ? 168.899 158.211 203.287 1.00 42.09  ? 25  LEU B CG    1 
ATOM   4344  C  CD1   . LEU B 2 25  ? 170.012 158.397 204.304 1.00 40.39  ? 25  LEU B CD1   1 
ATOM   4345  C  CD2   . LEU B 2 25  ? 169.088 159.142 202.101 1.00 41.30  ? 25  LEU B CD2   1 
ATOM   4346  N  N     . ASN B 2 26  ? 167.054 153.978 201.810 1.00 44.88  ? 26  ASN B N     1 
ATOM   4347  C  CA    . ASN B 2 26  ? 167.214 152.628 201.297 1.00 42.11  ? 26  ASN B CA    1 
ATOM   4348  C  C     . ASN B 2 26  ? 166.955 152.607 199.792 1.00 45.95  ? 26  ASN B C     1 
ATOM   4349  O  O     . ASN B 2 26  ? 166.032 153.276 199.312 1.00 45.89  ? 26  ASN B O     1 
ATOM   4350  C  CB    . ASN B 2 26  ? 166.257 151.673 202.013 1.00 44.57  ? 26  ASN B CB    1 
ATOM   4351  C  CG    . ASN B 2 26  ? 166.625 150.218 201.812 1.00 48.55  ? 26  ASN B CG    1 
ATOM   4352  O  OD1   . ASN B 2 26  ? 166.465 149.671 200.723 1.00 48.90  ? 26  ASN B OD1   1 
ATOM   4353  N  ND2   . ASN B 2 26  ? 167.123 149.582 202.867 1.00 50.23  ? 26  ASN B ND2   1 
ATOM   4354  N  N     . PRO B 2 27  ? 167.755 151.867 199.019 1.00 47.32  ? 27  PRO B N     1 
ATOM   4355  C  CA    . PRO B 2 27  ? 167.545 151.834 197.561 1.00 44.57  ? 27  PRO B CA    1 
ATOM   4356  C  C     . PRO B 2 27  ? 166.172 151.336 197.144 1.00 43.35  ? 27  PRO B C     1 
ATOM   4357  O  O     . PRO B 2 27  ? 165.685 151.744 196.083 1.00 43.55  ? 27  PRO B O     1 
ATOM   4358  C  CB    . PRO B 2 27  ? 168.656 150.896 197.062 1.00 41.41  ? 27  PRO B CB    1 
ATOM   4359  C  CG    . PRO B 2 27  ? 169.176 150.197 198.284 1.00 40.41  ? 27  PRO B CG    1 
ATOM   4360  C  CD    . PRO B 2 27  ? 168.969 151.139 199.420 1.00 41.95  ? 27  PRO B CD    1 
ATOM   4361  N  N     . GLN B 2 28  ? 165.537 150.463 197.930 1.00 45.99  ? 28  GLN B N     1 
ATOM   4362  C  CA    . GLN B 2 28  ? 164.194 150.008 197.582 1.00 47.46  ? 28  GLN B CA    1 
ATOM   4363  C  C     . GLN B 2 28  ? 163.201 151.164 197.589 1.00 49.59  ? 28  GLN B C     1 
ATOM   4364  O  O     . GLN B 2 28  ? 162.348 151.266 196.699 1.00 52.85  ? 28  GLN B O     1 
ATOM   4365  C  CB    . GLN B 2 28  ? 163.741 148.903 198.537 1.00 44.90  ? 28  GLN B CB    1 
ATOM   4366  C  CG    . GLN B 2 28  ? 164.196 147.508 198.134 1.00 50.36  ? 28  GLN B CG    1 
ATOM   4367  C  CD    . GLN B 2 28  ? 165.104 146.864 199.164 1.00 55.19  ? 28  GLN B CD    1 
ATOM   4368  O  OE1   . GLN B 2 28  ? 165.146 147.284 200.319 1.00 57.21  ? 28  GLN B OE1   1 
ATOM   4369  N  NE2   . GLN B 2 28  ? 165.837 145.838 198.747 1.00 52.67  ? 28  GLN B NE2   1 
ATOM   4370  N  N     . ALA B 2 29  ? 163.292 152.043 198.589 1.00 46.48  ? 29  ALA B N     1 
ATOM   4371  C  CA    . ALA B 2 29  ? 162.407 153.202 198.638 1.00 45.05  ? 29  ALA B CA    1 
ATOM   4372  C  C     . ALA B 2 29  ? 162.696 154.173 197.499 1.00 44.88  ? 29  ALA B C     1 
ATOM   4373  O  O     . ALA B 2 29  ? 161.769 154.725 196.896 1.00 49.46  ? 29  ALA B O     1 
ATOM   4374  C  CB    . ALA B 2 29  ? 162.535 153.905 199.988 1.00 42.94  ? 29  ALA B CB    1 
ATOM   4375  N  N     . GLN B 2 30  ? 163.976 154.394 197.189 1.00 36.82  ? 30  GLN B N     1 
ATOM   4376  C  CA    . GLN B 2 30  ? 164.353 155.347 196.152 1.00 38.43  ? 30  GLN B CA    1 
ATOM   4377  C  C     . GLN B 2 30  ? 164.147 154.808 194.743 1.00 34.59  ? 30  GLN B C     1 
ATOM   4378  O  O     . GLN B 2 30  ? 164.244 155.582 193.785 1.00 36.31  ? 30  GLN B O     1 
ATOM   4379  C  CB    . GLN B 2 30  ? 165.816 155.761 196.329 1.00 36.35  ? 30  GLN B CB    1 
ATOM   4380  C  CG    . GLN B 2 30  ? 166.117 156.446 197.651 1.00 35.52  ? 30  GLN B CG    1 
ATOM   4381  C  CD    . GLN B 2 30  ? 165.576 157.860 197.712 1.00 38.44  ? 30  GLN B CD    1 
ATOM   4382  O  OE1   . GLN B 2 30  ? 165.197 158.346 198.777 1.00 39.76  ? 30  GLN B OE1   1 
ATOM   4383  N  NE2   . GLN B 2 30  ? 165.539 158.530 196.566 1.00 38.27  ? 30  GLN B NE2   1 
ATOM   4384  N  N     . TRP B 2 31  ? 163.864 153.512 194.594 1.00 39.95  ? 31  TRP B N     1 
ATOM   4385  C  CA    . TRP B 2 31  ? 163.717 152.930 193.264 1.00 39.75  ? 31  TRP B CA    1 
ATOM   4386  C  C     . TRP B 2 31  ? 162.475 153.451 192.550 1.00 39.61  ? 31  TRP B C     1 
ATOM   4387  O  O     . TRP B 2 31  ? 162.457 153.520 191.316 1.00 40.61  ? 31  TRP B O     1 
ATOM   4388  C  CB    . TRP B 2 31  ? 163.677 151.405 193.369 1.00 40.03  ? 31  TRP B CB    1 
ATOM   4389  C  CG    . TRP B 2 31  ? 163.300 150.708 192.096 1.00 42.46  ? 31  TRP B CG    1 
ATOM   4390  C  CD1   . TRP B 2 31  ? 162.043 150.353 191.697 1.00 44.95  ? 31  TRP B CD1   1 
ATOM   4391  C  CD2   . TRP B 2 31  ? 164.187 150.278 191.057 1.00 41.13  ? 31  TRP B CD2   1 
ATOM   4392  N  NE1   . TRP B 2 31  ? 162.094 149.731 190.474 1.00 43.69  ? 31  TRP B NE1   1 
ATOM   4393  C  CE2   . TRP B 2 31  ? 163.398 149.672 190.059 1.00 40.43  ? 31  TRP B CE2   1 
ATOM   4394  C  CE3   . TRP B 2 31  ? 165.571 150.346 190.873 1.00 43.70  ? 31  TRP B CE3   1 
ATOM   4395  C  CZ2   . TRP B 2 31  ? 163.947 149.138 188.895 1.00 43.75  ? 31  TRP B CZ2   1 
ATOM   4396  C  CZ3   . TRP B 2 31  ? 166.114 149.815 189.717 1.00 41.39  ? 31  TRP B CZ3   1 
ATOM   4397  C  CH2   . TRP B 2 31  ? 165.304 149.219 188.743 1.00 44.10  ? 31  TRP B CH2   1 
ATOM   4398  N  N     . ARG B 2 32  ? 161.439 153.827 193.299 1.00 38.30  ? 32  ARG B N     1 
ATOM   4399  C  CA    . ARG B 2 32  ? 160.181 154.251 192.698 1.00 38.08  ? 32  ARG B CA    1 
ATOM   4400  C  C     . ARG B 2 32  ? 160.185 155.709 192.259 1.00 35.81  ? 32  ARG B C     1 
ATOM   4401  O  O     . ARG B 2 32  ? 159.213 156.151 191.637 1.00 40.19  ? 32  ARG B O     1 
ATOM   4402  C  CB    . ARG B 2 32  ? 159.028 154.011 193.675 1.00 39.97  ? 32  ARG B CB    1 
ATOM   4403  C  CG    . ARG B 2 32  ? 158.678 152.543 193.871 1.00 42.61  ? 32  ARG B CG    1 
ATOM   4404  C  CD    . ARG B 2 32  ? 158.756 151.775 192.560 1.00 41.16  ? 32  ARG B CD    1 
ATOM   4405  N  NE    . ARG B 2 32  ? 157.896 150.597 192.562 1.00 47.37  ? 32  ARG B NE    1 
ATOM   4406  C  CZ    . ARG B 2 32  ? 157.761 149.767 191.537 1.00 47.06  ? 32  ARG B CZ    1 
ATOM   4407  N  NH1   . ARG B 2 32  ? 158.419 149.954 190.405 1.00 45.45  ? 32  ARG B NH1   1 
ATOM   4408  N  NH2   . ARG B 2 32  ? 156.945 148.723 191.651 1.00 47.61  ? 32  ARG B NH2   1 
ATOM   4409  N  N     . ASN B 2 33  ? 161.243 156.463 192.560 1.00 32.95  ? 33  ASN B N     1 
ATOM   4410  C  CA    . ASN B 2 33  ? 161.381 157.857 192.140 1.00 31.63  ? 33  ASN B CA    1 
ATOM   4411  C  C     . ASN B 2 33  ? 162.616 157.951 191.255 1.00 32.08  ? 33  ASN B C     1 
ATOM   4412  O  O     . ASN B 2 33  ? 163.741 158.101 191.756 1.00 34.85  ? 33  ASN B O     1 
ATOM   4413  C  CB    . ASN B 2 33  ? 161.483 158.790 193.344 1.00 31.97  ? 33  ASN B CB    1 
ATOM   4414  C  CG    . ASN B 2 33  ? 161.222 160.241 192.984 1.00 31.12  ? 33  ASN B CG    1 
ATOM   4415  O  OD1   . ASN B 2 33  ? 161.218 160.612 191.810 1.00 35.61  ? 33  ASN B OD1   1 
ATOM   4416  N  ND2   . ASN B 2 33  ? 160.999 161.070 193.997 1.00 25.14  ? 33  ASN B ND2   1 
ATOM   4417  N  N     . PRO B 2 34  ? 162.455 157.859 189.932 1.00 21.81  ? 34  PRO B N     1 
ATOM   4418  C  CA    . PRO B 2 34  ? 163.633 157.849 189.048 1.00 27.24  ? 34  PRO B CA    1 
ATOM   4419  C  C     . PRO B 2 34  ? 164.465 159.116 189.114 1.00 26.42  ? 34  PRO B C     1 
ATOM   4420  O  O     . PRO B 2 34  ? 165.689 159.047 188.947 1.00 32.53  ? 34  PRO B O     1 
ATOM   4421  C  CB    . PRO B 2 34  ? 163.020 157.646 187.655 1.00 29.73  ? 34  PRO B CB    1 
ATOM   4422  C  CG    . PRO B 2 34  ? 161.618 158.136 187.781 1.00 33.28  ? 34  PRO B CG    1 
ATOM   4423  C  CD    . PRO B 2 34  ? 161.190 157.817 189.180 1.00 29.31  ? 34  PRO B CD    1 
ATOM   4424  N  N     . VAL B 2 35  ? 163.844 160.273 189.349 1.00 30.91  ? 35  VAL B N     1 
ATOM   4425  C  CA    . VAL B 2 35  ? 164.605 161.517 189.428 1.00 25.40  ? 35  VAL B CA    1 
ATOM   4426  C  C     . VAL B 2 35  ? 165.497 161.518 190.663 1.00 21.61  ? 35  VAL B C     1 
ATOM   4427  O  O     . VAL B 2 35  ? 166.688 161.842 190.590 1.00 25.89  ? 35  VAL B O     1 
ATOM   4428  C  CB    . VAL B 2 35  ? 163.657 162.729 189.415 1.00 30.63  ? 35  VAL B CB    1 
ATOM   4429  C  CG1   . VAL B 2 35  ? 164.438 164.016 189.628 1.00 25.78  ? 35  VAL B CG1   1 
ATOM   4430  C  CG2   . VAL B 2 35  ? 162.883 162.782 188.107 1.00 29.27  ? 35  VAL B CG2   1 
ATOM   4431  N  N     . MET B 2 36  ? 164.937 161.147 191.816 1.00 29.00  ? 36  MET B N     1 
ATOM   4432  C  CA    . MET B 2 36  ? 165.717 161.111 193.046 1.00 28.58  ? 36  MET B CA    1 
ATOM   4433  C  C     . MET B 2 36  ? 166.637 159.900 193.121 1.00 25.01  ? 36  MET B C     1 
ATOM   4434  O  O     . MET B 2 36  ? 167.613 159.929 193.879 1.00 28.19  ? 36  MET B O     1 
ATOM   4435  C  CB    . MET B 2 36  ? 164.789 161.134 194.263 1.00 24.65  ? 36  MET B CB    1 
ATOM   4436  C  CG    . MET B 2 36  ? 164.070 162.463 194.477 1.00 30.42  ? 36  MET B CG    1 
ATOM   4437  S  SD    . MET B 2 36  ? 165.106 163.934 194.305 1.00 38.85  ? 36  MET B SD    1 
ATOM   4438  C  CE    . MET B 2 36  ? 166.435 163.588 195.458 1.00 24.37  ? 36  MET B CE    1 
ATOM   4439  N  N     . PHE B 2 37  ? 166.350 158.841 192.360 1.00 25.05  ? 37  PHE B N     1 
ATOM   4440  C  CA    . PHE B 2 37  ? 167.254 157.697 192.316 1.00 21.36  ? 37  PHE B CA    1 
ATOM   4441  C  C     . PHE B 2 37  ? 168.577 158.054 191.651 1.00 22.84  ? 37  PHE B C     1 
ATOM   4442  O  O     . PHE B 2 37  ? 169.627 157.538 192.050 1.00 19.06  ? 37  PHE B O     1 
ATOM   4443  C  CB    . PHE B 2 37  ? 166.596 156.527 191.586 1.00 22.59  ? 37  PHE B CB    1 
ATOM   4444  C  CG    . PHE B 2 37  ? 167.232 155.199 191.878 1.00 25.65  ? 37  PHE B CG    1 
ATOM   4445  C  CD1   . PHE B 2 37  ? 167.612 154.867 193.168 1.00 29.34  ? 37  PHE B CD1   1 
ATOM   4446  C  CD2   . PHE B 2 37  ? 167.459 154.286 190.863 1.00 28.64  ? 37  PHE B CD2   1 
ATOM   4447  C  CE1   . PHE B 2 37  ? 168.201 153.647 193.440 1.00 30.95  ? 37  PHE B CE1   1 
ATOM   4448  C  CE2   . PHE B 2 37  ? 168.048 153.065 191.129 1.00 28.28  ? 37  PHE B CE2   1 
ATOM   4449  C  CZ    . PHE B 2 37  ? 168.419 152.745 192.419 1.00 26.70  ? 37  PHE B CZ    1 
ATOM   4450  N  N     . ILE B 2 38  ? 168.545 158.920 190.636 1.00 20.10  ? 38  ILE B N     1 
ATOM   4451  C  CA    . ILE B 2 38  ? 169.779 159.358 189.989 1.00 23.18  ? 38  ILE B CA    1 
ATOM   4452  C  C     . ILE B 2 38  ? 170.657 160.112 190.979 1.00 21.50  ? 38  ILE B C     1 
ATOM   4453  O  O     . ILE B 2 38  ? 171.879 159.923 191.019 1.00 31.15  ? 38  ILE B O     1 
ATOM   4454  C  CB    . ILE B 2 38  ? 169.457 160.212 188.748 1.00 27.98  ? 38  ILE B CB    1 
ATOM   4455  C  CG1   . ILE B 2 38  ? 168.709 159.377 187.706 1.00 26.42  ? 38  ILE B CG1   1 
ATOM   4456  C  CG2   . ILE B 2 38  ? 170.729 160.795 188.151 1.00 22.42  ? 38  ILE B CG2   1 
ATOM   4457  C  CD1   . ILE B 2 38  ? 169.459 158.144 187.254 1.00 28.57  ? 38  ILE B CD1   1 
ATOM   4458  N  N     . VAL B 2 39  ? 170.049 160.979 191.792 1.00 19.31  ? 39  VAL B N     1 
ATOM   4459  C  CA    . VAL B 2 39  ? 170.800 161.686 192.826 1.00 21.50  ? 39  VAL B CA    1 
ATOM   4460  C  C     . VAL B 2 39  ? 171.342 160.704 193.855 1.00 19.84  ? 39  VAL B C     1 
ATOM   4461  O  O     . VAL B 2 39  ? 172.468 160.851 194.344 1.00 28.72  ? 39  VAL B O     1 
ATOM   4462  C  CB    . VAL B 2 39  ? 169.919 162.764 193.484 1.00 20.37  ? 39  VAL B CB    1 
ATOM   4463  C  CG1   . VAL B 2 39  ? 170.774 163.723 194.296 1.00 24.24  ? 39  VAL B CG1   1 
ATOM   4464  C  CG2   . VAL B 2 39  ? 169.124 163.512 192.430 1.00 24.12  ? 39  VAL B CG2   1 
ATOM   4465  N  N     . TRP B 2 40  ? 170.543 159.694 194.210 1.00 23.86  ? 40  TRP B N     1 
ATOM   4466  C  CA    . TRP B 2 40  ? 171.012 158.666 195.134 1.00 20.25  ? 40  TRP B CA    1 
ATOM   4467  C  C     . TRP B 2 40  ? 172.195 157.902 194.554 1.00 24.74  ? 40  TRP B C     1 
ATOM   4468  O  O     . TRP B 2 40  ? 173.170 157.622 195.261 1.00 27.69  ? 40  TRP B O     1 
ATOM   4469  C  CB    . TRP B 2 40  ? 169.868 157.711 195.474 1.00 24.72  ? 40  TRP B CB    1 
ATOM   4470  C  CG    . TRP B 2 40  ? 170.145 156.830 196.652 1.00 25.55  ? 40  TRP B CG    1 
ATOM   4471  C  CD1   . TRP B 2 40  ? 169.782 157.056 197.947 1.00 29.27  ? 40  TRP B CD1   1 
ATOM   4472  C  CD2   . TRP B 2 40  ? 170.838 155.577 196.642 1.00 26.93  ? 40  TRP B CD2   1 
ATOM   4473  N  NE1   . TRP B 2 40  ? 170.209 156.023 198.745 1.00 26.76  ? 40  TRP B NE1   1 
ATOM   4474  C  CE2   . TRP B 2 40  ? 170.861 155.102 197.968 1.00 30.32  ? 40  TRP B CE2   1 
ATOM   4475  C  CE3   . TRP B 2 40  ? 171.444 154.811 195.641 1.00 27.52  ? 40  TRP B CE3   1 
ATOM   4476  C  CZ2   . TRP B 2 40  ? 171.464 153.896 198.318 1.00 28.21  ? 40  TRP B CZ2   1 
ATOM   4477  C  CZ3   . TRP B 2 40  ? 172.043 153.615 195.991 1.00 27.87  ? 40  TRP B CZ3   1 
ATOM   4478  C  CH2   . TRP B 2 40  ? 172.048 153.169 197.318 1.00 29.84  ? 40  TRP B CH2   1 
ATOM   4479  N  N     . ILE B 2 41  ? 172.125 157.551 193.268 1.00 21.42  ? 41  ILE B N     1 
ATOM   4480  C  CA    . ILE B 2 41  ? 173.235 156.859 192.622 1.00 26.85  ? 41  ILE B CA    1 
ATOM   4481  C  C     . ILE B 2 41  ? 174.458 157.763 192.546 1.00 24.37  ? 41  ILE B C     1 
ATOM   4482  O  O     . ILE B 2 41  ? 175.586 157.329 192.809 1.00 26.82  ? 41  ILE B O     1 
ATOM   4483  C  CB    . ILE B 2 41  ? 172.809 156.357 191.229 1.00 25.27  ? 41  ILE B CB    1 
ATOM   4484  C  CG1   . ILE B 2 41  ? 171.876 155.151 191.361 1.00 25.72  ? 41  ILE B CG1   1 
ATOM   4485  C  CG2   . ILE B 2 41  ? 174.026 156.016 190.380 1.00 25.27  ? 41  ILE B CG2   1 
ATOM   4486  C  CD1   . ILE B 2 41  ? 172.595 153.837 191.584 1.00 30.77  ? 41  ILE B CD1   1 
ATOM   4487  N  N     . GLY B 2 42  ? 174.256 159.035 192.194 1.00 27.23  ? 42  GLY B N     1 
ATOM   4488  C  CA    . GLY B 2 42  ? 175.377 159.957 192.112 1.00 19.92  ? 42  GLY B CA    1 
ATOM   4489  C  C     . GLY B 2 42  ? 176.039 160.197 193.455 1.00 25.16  ? 42  GLY B C     1 
ATOM   4490  O  O     . GLY B 2 42  ? 177.256 160.387 193.532 1.00 29.15  ? 42  GLY B O     1 
ATOM   4491  N  N     . SER B 2 43  ? 175.248 160.200 194.531 1.00 23.05  ? 43  SER B N     1 
ATOM   4492  C  CA    . SER B 2 43  ? 175.817 160.367 195.864 1.00 22.57  ? 43  SER B CA    1 
ATOM   4493  C  C     . SER B 2 43  ? 176.704 159.185 196.237 1.00 23.10  ? 43  SER B C     1 
ATOM   4494  O  O     . SER B 2 43  ? 177.771 159.364 196.835 1.00 28.43  ? 43  SER B O     1 
ATOM   4495  C  CB    . SER B 2 43  ? 174.702 160.548 196.893 1.00 24.37  ? 43  SER B CB    1 
ATOM   4496  O  OG    . SER B 2 43  ? 173.592 161.224 196.330 1.00 30.38  ? 43  SER B OG    1 
ATOM   4497  N  N     . LEU B 2 44  ? 176.275 157.968 195.896 1.00 26.04  ? 44  LEU B N     1 
ATOM   4498  C  CA    . LEU B 2 44  ? 177.094 156.791 196.170 1.00 21.87  ? 44  LEU B CA    1 
ATOM   4499  C  C     . LEU B 2 44  ? 178.356 156.783 195.316 1.00 26.35  ? 44  LEU B C     1 
ATOM   4500  O  O     . LEU B 2 44  ? 179.427 156.385 195.787 1.00 33.02  ? 44  LEU B O     1 
ATOM   4501  C  CB    . LEU B 2 44  ? 176.280 155.519 195.934 1.00 29.62  ? 44  LEU B CB    1 
ATOM   4502  C  CG    . LEU B 2 44  ? 176.757 154.259 196.660 1.00 28.51  ? 44  LEU B CG    1 
ATOM   4503  C  CD1   . LEU B 2 44  ? 176.920 154.520 198.149 1.00 30.54  ? 44  LEU B CD1   1 
ATOM   4504  C  CD2   . LEU B 2 44  ? 175.798 153.105 196.415 1.00 28.46  ? 44  LEU B CD2   1 
ATOM   4505  N  N     . LEU B 2 45  ? 178.246 157.212 194.056 1.00 24.72  ? 45  LEU B N     1 
ATOM   4506  C  CA    . LEU B 2 45  ? 179.411 157.236 193.178 1.00 25.99  ? 45  LEU B CA    1 
ATOM   4507  C  C     . LEU B 2 45  ? 180.455 158.231 193.669 1.00 24.46  ? 45  LEU B C     1 
ATOM   4508  O  O     . LEU B 2 45  ? 181.656 157.940 193.654 1.00 33.58  ? 45  LEU B O     1 
ATOM   4509  C  CB    . LEU B 2 45  ? 178.982 157.569 191.750 1.00 29.06  ? 45  LEU B CB    1 
ATOM   4510  C  CG    . LEU B 2 45  ? 180.067 157.470 190.677 1.00 35.05  ? 45  LEU B CG    1 
ATOM   4511  C  CD1   . LEU B 2 45  ? 180.436 156.018 190.417 1.00 28.43  ? 45  LEU B CD1   1 
ATOM   4512  C  CD2   . LEU B 2 45  ? 179.611 158.147 189.395 1.00 28.93  ? 45  LEU B CD2   1 
ATOM   4513  N  N     . THR B 2 46  ? 180.017 159.413 194.109 1.00 25.81  ? 46  THR B N     1 
ATOM   4514  C  CA    . THR B 2 46  ? 180.960 160.401 194.622 1.00 28.27  ? 46  THR B CA    1 
ATOM   4515  C  C     . THR B 2 46  ? 181.536 159.979 195.967 1.00 28.03  ? 46  THR B C     1 
ATOM   4516  O  O     . THR B 2 46  ? 182.698 160.282 196.263 1.00 34.79  ? 46  THR B O     1 
ATOM   4517  C  CB    . THR B 2 46  ? 180.286 161.768 194.738 1.00 32.43  ? 46  THR B CB    1 
ATOM   4518  O  OG1   . THR B 2 46  ? 178.944 161.605 195.215 1.00 36.13  ? 46  THR B OG1   1 
ATOM   4519  C  CG2   . THR B 2 46  ? 180.257 162.463 193.386 1.00 25.86  ? 46  THR B CG2   1 
ATOM   4520  N  N     . THR B 2 47  ? 180.743 159.295 196.795 1.00 30.52  ? 47  THR B N     1 
ATOM   4521  C  CA    . THR B 2 47  ? 181.257 158.786 198.063 1.00 31.80  ? 47  THR B CA    1 
ATOM   4522  C  C     . THR B 2 47  ? 182.351 157.751 197.836 1.00 33.24  ? 47  THR B C     1 
ATOM   4523  O  O     . THR B 2 47  ? 183.397 157.785 198.496 1.00 37.90  ? 47  THR B O     1 
ATOM   4524  C  CB    . THR B 2 47  ? 180.116 158.191 198.890 1.00 30.78  ? 47  THR B CB    1 
ATOM   4525  O  OG1   . THR B 2 47  ? 179.227 159.235 199.303 1.00 35.24  ? 47  THR B OG1   1 
ATOM   4526  C  CG2   . THR B 2 47  ? 180.658 157.479 200.121 1.00 25.28  ? 47  THR B CG2   1 
ATOM   4527  N  N     . CYS B 2 48  ? 182.130 156.824 196.900 1.00 34.17  ? 48  CYS B N     1 
ATOM   4528  C  CA    . CYS B 2 48  ? 183.149 155.827 196.586 1.00 34.10  ? 48  CYS B CA    1 
ATOM   4529  C  C     . CYS B 2 48  ? 184.387 156.476 195.978 1.00 35.29  ? 48  CYS B C     1 
ATOM   4530  O  O     . CYS B 2 48  ? 185.516 156.070 196.275 1.00 37.94  ? 48  CYS B O     1 
ATOM   4531  C  CB    . CYS B 2 48  ? 182.577 154.771 195.641 1.00 32.89  ? 48  CYS B CB    1 
ATOM   4532  S  SG    . CYS B 2 48  ? 181.403 153.634 196.413 1.00 50.24  ? 48  CYS B SG    1 
ATOM   4533  N  N     . ILE B 2 49  ? 184.192 157.477 195.118 1.00 33.24  ? 49  ILE B N     1 
ATOM   4534  C  CA    . ILE B 2 49  ? 185.322 158.176 194.512 1.00 31.00  ? 49  ILE B CA    1 
ATOM   4535  C  C     . ILE B 2 49  ? 186.138 158.897 195.579 1.00 31.65  ? 49  ILE B C     1 
ATOM   4536  O  O     . ILE B 2 49  ? 187.375 158.863 195.565 1.00 38.19  ? 49  ILE B O     1 
ATOM   4537  C  CB    . ILE B 2 49  ? 184.826 159.143 193.421 1.00 35.12  ? 49  ILE B CB    1 
ATOM   4538  C  CG1   . ILE B 2 49  ? 184.579 158.386 192.114 1.00 29.95  ? 49  ILE B CG1   1 
ATOM   4539  C  CG2   . ILE B 2 49  ? 185.819 160.274 193.203 1.00 29.66  ? 49  ILE B CG2   1 
ATOM   4540  C  CD1   . ILE B 2 49  ? 183.778 159.166 191.100 1.00 34.73  ? 49  ILE B CD1   1 
ATOM   4541  N  N     . SER B 2 50  ? 185.460 159.554 196.523 1.00 32.79  ? 50  SER B N     1 
ATOM   4542  C  CA    . SER B 2 50  ? 186.168 160.246 197.596 1.00 30.97  ? 50  SER B CA    1 
ATOM   4543  C  C     . SER B 2 50  ? 186.931 159.265 198.477 1.00 37.78  ? 50  SER B C     1 
ATOM   4544  O  O     . SER B 2 50  ? 188.011 159.587 198.986 1.00 40.60  ? 50  SER B O     1 
ATOM   4545  C  CB    . SER B 2 50  ? 185.185 161.063 198.432 1.00 32.71  ? 50  SER B CB    1 
ATOM   4546  O  OG    . SER B 2 50  ? 185.865 162.040 199.200 1.00 40.03  ? 50  SER B OG    1 
ATOM   4547  N  N     . ILE B 2 51  ? 186.381 158.065 198.673 1.00 37.79  ? 51  ILE B N     1 
ATOM   4548  C  CA    . ILE B 2 51  ? 187.075 157.048 199.458 1.00 36.97  ? 51  ILE B CA    1 
ATOM   4549  C  C     . ILE B 2 51  ? 188.347 156.606 198.744 1.00 39.74  ? 51  ILE B C     1 
ATOM   4550  O  O     . ILE B 2 51  ? 189.390 156.391 199.374 1.00 45.29  ? 51  ILE B O     1 
ATOM   4551  C  CB    . ILE B 2 51  ? 186.132 155.863 199.742 1.00 39.50  ? 51  ILE B CB    1 
ATOM   4552  C  CG1   . ILE B 2 51  ? 185.295 156.138 200.992 1.00 38.14  ? 51  ILE B CG1   1 
ATOM   4553  C  CG2   . ILE B 2 51  ? 186.913 154.567 199.903 1.00 39.72  ? 51  ILE B CG2   1 
ATOM   4554  C  CD1   . ILE B 2 51  ? 184.029 155.315 201.071 1.00 36.69  ? 51  ILE B CD1   1 
ATOM   4555  N  N     . ALA B 2 52  ? 188.286 156.480 197.416 1.00 40.01  ? 52  ALA B N     1 
ATOM   4556  C  CA    . ALA B 2 52  ? 189.461 156.066 196.657 1.00 38.67  ? 52  ALA B CA    1 
ATOM   4557  C  C     . ALA B 2 52  ? 190.549 157.132 196.694 1.00 45.37  ? 52  ALA B C     1 
ATOM   4558  O  O     . ALA B 2 52  ? 191.741 156.810 196.763 1.00 47.32  ? 52  ALA B O     1 
ATOM   4559  C  CB    . ALA B 2 52  ? 189.069 155.747 195.215 1.00 38.04  ? 52  ALA B CB    1 
ATOM   4560  N  N     . MET B 2 53  ? 190.161 158.409 196.647 1.00 40.67  ? 53  MET B N     1 
ATOM   4561  C  CA    . MET B 2 53  ? 191.149 159.480 196.735 1.00 39.25  ? 53  MET B CA    1 
ATOM   4562  C  C     . MET B 2 53  ? 191.768 159.550 198.125 1.00 43.25  ? 53  MET B C     1 
ATOM   4563  O  O     . MET B 2 53  ? 192.968 159.813 198.263 1.00 46.66  ? 53  MET B O     1 
ATOM   4564  C  CB    . MET B 2 53  ? 190.514 160.821 196.365 1.00 40.47  ? 53  MET B CB    1 
ATOM   4565  C  CG    . MET B 2 53  ? 189.957 160.889 194.954 1.00 38.66  ? 53  MET B CG    1 
ATOM   4566  S  SD    . MET B 2 53  ? 189.008 162.395 194.668 1.00 47.71  ? 53  MET B SD    1 
ATOM   4567  C  CE    . MET B 2 53  ? 188.829 162.354 192.888 1.00 42.18  ? 53  MET B CE    1 
ATOM   4568  N  N     . ALA B 2 54  ? 190.963 159.326 199.167 1.00 44.93  ? 54  ALA B N     1 
ATOM   4569  C  CA    . ALA B 2 54  ? 191.489 159.351 200.528 1.00 43.79  ? 54  ALA B CA    1 
ATOM   4570  C  C     . ALA B 2 54  ? 192.498 158.232 200.751 1.00 47.00  ? 54  ALA B C     1 
ATOM   4571  O  O     . ALA B 2 54  ? 193.534 158.439 201.393 1.00 49.21  ? 54  ALA B O     1 
ATOM   4572  C  CB    . ALA B 2 54  ? 190.343 159.252 201.535 1.00 42.72  ? 54  ALA B CB    1 
ATOM   4573  N  N     . SER B 2 55  ? 192.213 157.040 200.227 1.00 50.89  ? 55  SER B N     1 
ATOM   4574  C  CA    . SER B 2 55  ? 193.123 155.910 200.351 1.00 48.05  ? 55  SER B CA    1 
ATOM   4575  C  C     . SER B 2 55  ? 194.323 156.007 199.418 1.00 49.49  ? 55  SER B C     1 
ATOM   4576  O  O     . SER B 2 55  ? 195.249 155.198 199.543 1.00 53.94  ? 55  SER B O     1 
ATOM   4577  C  CB    . SER B 2 55  ? 192.373 154.602 200.086 1.00 47.68  ? 55  SER B CB    1 
ATOM   4578  O  OG    . SER B 2 55  ? 192.241 154.363 198.696 1.00 51.27  ? 55  SER B OG    1 
ATOM   4579  N  N     . GLY B 2 56  ? 194.332 156.966 198.495 1.00 51.92  ? 56  GLY B N     1 
ATOM   4580  C  CA    . GLY B 2 56  ? 195.423 157.120 197.558 1.00 49.99  ? 56  GLY B CA    1 
ATOM   4581  C  C     . GLY B 2 56  ? 195.338 156.254 196.321 1.00 52.49  ? 56  GLY B C     1 
ATOM   4582  O  O     . GLY B 2 56  ? 196.262 156.291 195.497 1.00 54.34  ? 56  GLY B O     1 
ATOM   4583  N  N     . ALA B 2 57  ? 194.265 155.477 196.161 1.00 51.69  ? 57  ALA B N     1 
ATOM   4584  C  CA    . ALA B 2 57  ? 194.139 154.626 194.983 1.00 52.18  ? 57  ALA B CA    1 
ATOM   4585  C  C     . ALA B 2 57  ? 193.876 155.439 193.722 1.00 51.03  ? 57  ALA B C     1 
ATOM   4586  O  O     . ALA B 2 57  ? 194.194 154.985 192.617 1.00 51.91  ? 57  ALA B O     1 
ATOM   4587  C  CB    . ALA B 2 57  ? 193.027 153.599 195.193 1.00 48.55  ? 57  ALA B CB    1 
ATOM   4588  N  N     . MET B 2 58  ? 193.301 156.634 193.862 1.00 53.03  ? 58  MET B N     1 
ATOM   4589  C  CA    . MET B 2 58  ? 192.983 157.483 192.724 1.00 49.25  ? 58  MET B CA    1 
ATOM   4590  C  C     . MET B 2 58  ? 193.425 158.910 193.024 1.00 50.82  ? 58  MET B C     1 
ATOM   4591  O  O     . MET B 2 58  ? 193.091 159.451 194.093 1.00 53.96  ? 58  MET B O     1 
ATOM   4592  C  CB    . MET B 2 58  ? 191.481 157.438 192.412 1.00 49.05  ? 58  MET B CB    1 
ATOM   4593  C  CG    . MET B 2 58  ? 190.956 158.666 191.687 1.00 51.73  ? 58  MET B CG    1 
ATOM   4594  S  SD    . MET B 2 58  ? 189.156 158.696 191.576 1.00 60.78  ? 58  MET B SD    1 
ATOM   4595  C  CE    . MET B 2 58  ? 188.792 156.948 191.437 1.00 49.21  ? 58  MET B CE    1 
ATOM   4596  N  N     . PRO B 2 59  ? 194.180 159.546 192.132 1.00 52.38  ? 59  PRO B N     1 
ATOM   4597  C  CA    . PRO B 2 59  ? 194.581 160.938 192.359 1.00 52.80  ? 59  PRO B CA    1 
ATOM   4598  C  C     . PRO B 2 59  ? 193.384 161.876 192.353 1.00 52.22  ? 59  PRO B C     1 
ATOM   4599  O  O     . PRO B 2 59  ? 192.370 161.640 191.693 1.00 52.78  ? 59  PRO B O     1 
ATOM   4600  C  CB    . PRO B 2 59  ? 195.522 161.241 191.186 1.00 51.95  ? 59  PRO B CB    1 
ATOM   4601  C  CG    . PRO B 2 59  ? 195.266 160.163 190.180 1.00 51.87  ? 59  PRO B CG    1 
ATOM   4602  C  CD    . PRO B 2 59  ? 194.835 158.961 190.951 1.00 50.06  ? 59  PRO B CD    1 
ATOM   4603  N  N     . GLY B 2 60  ? 193.519 162.961 193.107 1.00 45.44  ? 60  GLY B N     1 
ATOM   4604  C  CA    . GLY B 2 60  ? 192.512 163.996 193.178 1.00 44.05  ? 60  GLY B CA    1 
ATOM   4605  C  C     . GLY B 2 60  ? 192.404 164.578 194.570 1.00 43.33  ? 60  GLY B C     1 
ATOM   4606  O  O     . GLY B 2 60  ? 193.171 164.257 195.475 1.00 45.31  ? 60  GLY B O     1 
ATOM   4607  N  N     . ASN B 2 61  ? 191.416 165.455 194.731 1.00 41.63  ? 61  ASN B N     1 
ATOM   4608  C  CA    . ASN B 2 61  ? 191.151 166.109 196.008 1.00 40.52  ? 61  ASN B CA    1 
ATOM   4609  C  C     . ASN B 2 61  ? 190.022 165.362 196.709 1.00 41.36  ? 61  ASN B C     1 
ATOM   4610  O  O     . ASN B 2 61  ? 188.859 165.457 196.303 1.00 44.42  ? 61  ASN B O     1 
ATOM   4611  C  CB    . ASN B 2 61  ? 190.795 167.578 195.799 1.00 37.99  ? 61  ASN B CB    1 
ATOM   4612  C  CG    . ASN B 2 61  ? 190.826 168.375 197.088 1.00 41.14  ? 61  ASN B CG    1 
ATOM   4613  O  OD1   . ASN B 2 61  ? 191.208 167.863 198.139 1.00 45.32  ? 61  ASN B OD1   1 
ATOM   4614  N  ND2   . ASN B 2 61  ? 190.422 169.638 197.012 1.00 41.81  ? 61  ASN B ND2   1 
ATOM   4615  N  N     . ALA B 2 62  ? 190.367 164.617 197.761 1.00 37.23  ? 62  ALA B N     1 
ATOM   4616  C  CA    . ALA B 2 62  ? 189.362 163.843 198.483 1.00 36.67  ? 62  ALA B CA    1 
ATOM   4617  C  C     . ALA B 2 62  ? 188.375 164.750 199.208 1.00 39.08  ? 62  ALA B C     1 
ATOM   4618  O  O     . ALA B 2 62  ? 187.182 164.435 199.290 1.00 41.46  ? 62  ALA B O     1 
ATOM   4619  C  CB    . ALA B 2 62  ? 190.040 162.892 199.468 1.00 36.56  ? 62  ALA B CB    1 
ATOM   4620  N  N     . LEU B 2 63  ? 188.854 165.874 199.747 1.00 36.20  ? 63  LEU B N     1 
ATOM   4621  C  CA    . LEU B 2 63  ? 187.974 166.774 200.487 1.00 36.37  ? 63  LEU B CA    1 
ATOM   4622  C  C     . LEU B 2 63  ? 186.903 167.374 199.585 1.00 38.33  ? 63  LEU B C     1 
ATOM   4623  O  O     . LEU B 2 63  ? 185.738 167.488 199.985 1.00 37.93  ? 63  LEU B O     1 
ATOM   4624  C  CB    . LEU B 2 63  ? 188.794 167.877 201.155 1.00 37.41  ? 63  LEU B CB    1 
ATOM   4625  C  CG    . LEU B 2 63  ? 188.859 167.828 202.682 1.00 41.40  ? 63  LEU B CG    1 
ATOM   4626  C  CD1   . LEU B 2 63  ? 189.654 166.618 203.147 1.00 39.19  ? 63  LEU B CD1   1 
ATOM   4627  C  CD2   . LEU B 2 63  ? 189.453 169.112 203.240 1.00 40.60  ? 63  LEU B CD2   1 
ATOM   4628  N  N     . PHE B 2 64  ? 187.276 167.769 198.365 1.00 33.43  ? 64  PHE B N     1 
ATOM   4629  C  CA    . PHE B 2 64  ? 186.296 168.335 197.444 1.00 26.81  ? 64  PHE B CA    1 
ATOM   4630  C  C     . PHE B 2 64  ? 185.241 167.306 197.059 1.00 27.52  ? 64  PHE B C     1 
ATOM   4631  O  O     . PHE B 2 64  ? 184.048 167.625 196.992 1.00 30.11  ? 64  PHE B O     1 
ATOM   4632  C  CB    . PHE B 2 64  ? 186.995 168.878 196.197 1.00 28.23  ? 64  PHE B CB    1 
ATOM   4633  C  CG    . PHE B 2 64  ? 186.049 169.410 195.158 1.00 29.15  ? 64  PHE B CG    1 
ATOM   4634  C  CD1   . PHE B 2 64  ? 185.355 170.589 195.373 1.00 26.55  ? 64  PHE B CD1   1 
ATOM   4635  C  CD2   . PHE B 2 64  ? 185.854 168.732 193.967 1.00 28.50  ? 64  PHE B CD2   1 
ATOM   4636  C  CE1   . PHE B 2 64  ? 184.484 171.081 194.420 1.00 27.32  ? 64  PHE B CE1   1 
ATOM   4637  C  CE2   . PHE B 2 64  ? 184.984 169.219 193.010 1.00 26.00  ? 64  PHE B CE2   1 
ATOM   4638  C  CZ    . PHE B 2 64  ? 184.299 170.395 193.237 1.00 28.98  ? 64  PHE B CZ    1 
ATOM   4639  N  N     . SER B 2 65  ? 185.661 166.065 196.802 1.00 31.89  ? 65  SER B N     1 
ATOM   4640  C  CA    . SER B 2 65  ? 184.703 165.017 196.469 1.00 27.29  ? 65  SER B CA    1 
ATOM   4641  C  C     . SER B 2 65  ? 183.811 164.688 197.660 1.00 29.32  ? 65  SER B C     1 
ATOM   4642  O  O     . SER B 2 65  ? 182.622 164.391 197.491 1.00 30.72  ? 65  SER B O     1 
ATOM   4643  C  CB    . SER B 2 65  ? 185.437 163.767 195.985 1.00 29.32  ? 65  SER B CB    1 
ATOM   4644  O  OG    . SER B 2 65  ? 186.038 163.985 194.721 1.00 40.57  ? 65  SER B OG    1 
ATOM   4645  N  N     . ALA B 2 66  ? 184.365 164.737 198.873 1.00 28.55  ? 66  ALA B N     1 
ATOM   4646  C  CA    . ALA B 2 66  ? 183.562 164.463 200.060 1.00 23.62  ? 66  ALA B CA    1 
ATOM   4647  C  C     . ALA B 2 66  ? 182.607 165.611 200.355 1.00 27.64  ? 66  ALA B C     1 
ATOM   4648  O  O     . ALA B 2 66  ? 181.560 165.413 200.982 1.00 30.89  ? 66  ALA B O     1 
ATOM   4649  C  CB    . ALA B 2 66  ? 184.470 164.195 201.260 1.00 21.68  ? 66  ALA B CB    1 
ATOM   4650  N  N     . ALA B 2 67  ? 182.944 166.820 199.901 1.00 23.67  ? 67  ALA B N     1 
ATOM   4651  C  CA    . ALA B 2 67  ? 182.044 167.951 200.094 1.00 24.70  ? 67  ALA B CA    1 
ATOM   4652  C  C     . ALA B 2 67  ? 180.882 167.896 199.113 1.00 28.67  ? 67  ALA B C     1 
ATOM   4653  O  O     . ALA B 2 67  ? 179.743 168.223 199.467 1.00 25.99  ? 67  ALA B O     1 
ATOM   4654  C  CB    . ALA B 2 67  ? 182.811 169.265 199.951 1.00 22.75  ? 67  ALA B CB    1 
ATOM   4655  N  N     . ILE B 2 68  ? 181.149 167.479 197.874 1.00 26.11  ? 68  ILE B N     1 
ATOM   4656  C  CA    . ILE B 2 68  ? 180.077 167.323 196.896 1.00 23.39  ? 68  ILE B CA    1 
ATOM   4657  C  C     . ILE B 2 68  ? 179.194 166.137 197.258 1.00 22.55  ? 68  ILE B C     1 
ATOM   4658  O  O     . ILE B 2 68  ? 177.962 166.218 197.188 1.00 24.00  ? 68  ILE B O     1 
ATOM   4659  C  CB    . ILE B 2 68  ? 180.663 167.184 195.479 1.00 22.16  ? 68  ILE B CB    1 
ATOM   4660  C  CG1   . ILE B 2 68  ? 181.479 168.427 195.115 1.00 24.91  ? 68  ILE B CG1   1 
ATOM   4661  C  CG2   . ILE B 2 68  ? 179.556 166.930 194.462 1.00 22.63  ? 68  ILE B CG2   1 
ATOM   4662  C  CD1   . ILE B 2 68  ? 180.657 169.554 194.532 1.00 22.45  ? 68  ILE B CD1   1 
ATOM   4663  N  N     . SER B 2 69  ? 179.808 165.018 197.655 1.00 26.72  ? 69  SER B N     1 
ATOM   4664  C  CA    . SER B 2 69  ? 179.038 163.833 198.017 1.00 24.78  ? 69  SER B CA    1 
ATOM   4665  C  C     . SER B 2 69  ? 178.170 164.088 199.242 1.00 25.14  ? 69  SER B C     1 
ATOM   4666  O  O     . SER B 2 69  ? 177.019 163.640 199.300 1.00 32.63  ? 69  SER B O     1 
ATOM   4667  C  CB    . SER B 2 69  ? 179.978 162.653 198.265 1.00 23.60  ? 69  SER B CB    1 
ATOM   4668  O  OG    . SER B 2 69  ? 179.256 161.497 198.649 1.00 26.16  ? 69  SER B OG    1 
ATOM   4669  N  N     . GLY B 2 70  ? 178.707 164.802 200.234 1.00 22.89  ? 70  GLY B N     1 
ATOM   4670  C  CA    . GLY B 2 70  ? 177.934 165.081 201.433 1.00 19.12  ? 70  GLY B CA    1 
ATOM   4671  C  C     . GLY B 2 70  ? 176.684 165.892 201.152 1.00 23.10  ? 70  GLY B C     1 
ATOM   4672  O  O     . GLY B 2 70  ? 175.613 165.607 201.693 1.00 22.40  ? 70  GLY B O     1 
ATOM   4673  N  N     . TRP B 2 71  ? 176.800 166.912 200.299 1.00 24.88  ? 71  TRP B N     1 
ATOM   4674  C  CA    . TRP B 2 71  ? 175.633 167.717 199.956 1.00 20.63  ? 71  TRP B CA    1 
ATOM   4675  C  C     . TRP B 2 71  ? 174.694 166.972 199.017 1.00 23.23  ? 71  TRP B C     1 
ATOM   4676  O  O     . TRP B 2 71  ? 173.490 167.249 199.001 1.00 25.10  ? 71  TRP B O     1 
ATOM   4677  C  CB    . TRP B 2 71  ? 176.072 169.045 199.342 1.00 14.76  ? 71  TRP B CB    1 
ATOM   4678  C  CG    . TRP B 2 71  ? 176.388 170.085 200.372 1.00 27.31  ? 71  TRP B CG    1 
ATOM   4679  C  CD1   . TRP B 2 71  ? 177.625 170.467 200.800 1.00 15.77  ? 71  TRP B CD1   1 
ATOM   4680  C  CD2   . TRP B 2 71  ? 175.447 170.869 201.115 1.00 23.50  ? 71  TRP B CD2   1 
ATOM   4681  N  NE1   . TRP B 2 71  ? 177.514 171.443 201.759 1.00 22.27  ? 71  TRP B NE1   1 
ATOM   4682  C  CE2   . TRP B 2 71  ? 176.187 171.708 201.971 1.00 26.12  ? 71  TRP B CE2   1 
ATOM   4683  C  CE3   . TRP B 2 71  ? 174.051 170.944 201.137 1.00 22.69  ? 71  TRP B CE3   1 
ATOM   4684  C  CZ2   . TRP B 2 71  ? 175.578 172.612 202.839 1.00 21.38  ? 71  TRP B CZ2   1 
ATOM   4685  C  CZ3   . TRP B 2 71  ? 173.449 171.842 202.000 1.00 23.53  ? 71  TRP B CZ3   1 
ATOM   4686  C  CH2   . TRP B 2 71  ? 174.212 172.663 202.839 1.00 24.11  ? 71  TRP B CH2   1 
ATOM   4687  N  N     . LEU B 2 72  ? 175.223 166.036 198.224 1.00 21.93  ? 72  LEU B N     1 
ATOM   4688  C  CA    . LEU B 2 72  ? 174.358 165.179 197.420 1.00 23.38  ? 72  LEU B CA    1 
ATOM   4689  C  C     . LEU B 2 72  ? 173.492 164.291 198.306 1.00 23.59  ? 72  LEU B C     1 
ATOM   4690  O  O     . LEU B 2 72  ? 172.303 164.097 198.027 1.00 33.61  ? 72  LEU B O     1 
ATOM   4691  C  CB    . LEU B 2 72  ? 175.198 164.334 196.463 1.00 25.03  ? 72  LEU B CB    1 
ATOM   4692  C  CG    . LEU B 2 72  ? 175.710 165.035 195.203 1.00 24.75  ? 72  LEU B CG    1 
ATOM   4693  C  CD1   . LEU B 2 72  ? 176.183 164.017 194.179 1.00 20.84  ? 72  LEU B CD1   1 
ATOM   4694  C  CD2   . LEU B 2 72  ? 174.645 165.945 194.612 1.00 23.78  ? 72  LEU B CD2   1 
ATOM   4695  N  N     . TRP B 2 73  ? 174.073 163.741 199.376 1.00 22.04  ? 73  TRP B N     1 
ATOM   4696  C  CA    . TRP B 2 73  ? 173.283 162.988 200.345 1.00 24.08  ? 73  TRP B CA    1 
ATOM   4697  C  C     . TRP B 2 73  ? 172.291 163.886 201.071 1.00 23.33  ? 73  TRP B C     1 
ATOM   4698  O  O     . TRP B 2 73  ? 171.228 163.422 201.496 1.00 32.29  ? 73  TRP B O     1 
ATOM   4699  C  CB    . TRP B 2 73  ? 174.202 162.293 201.350 1.00 21.12  ? 73  TRP B CB    1 
ATOM   4700  C  CG    . TRP B 2 73  ? 174.910 161.094 200.799 1.00 25.28  ? 73  TRP B CG    1 
ATOM   4701  C  CD1   . TRP B 2 73  ? 176.251 160.958 200.591 1.00 24.59  ? 73  TRP B CD1   1 
ATOM   4702  C  CD2   . TRP B 2 73  ? 174.314 159.856 200.391 1.00 28.51  ? 73  TRP B CD2   1 
ATOM   4703  N  NE1   . TRP B 2 73  ? 176.527 159.716 200.076 1.00 25.77  ? 73  TRP B NE1   1 
ATOM   4704  C  CE2   . TRP B 2 73  ? 175.355 159.019 199.945 1.00 27.29  ? 73  TRP B CE2   1 
ATOM   4705  C  CE3   . TRP B 2 73  ? 173.001 159.376 200.359 1.00 25.87  ? 73  TRP B CE3   1 
ATOM   4706  C  CZ2   . TRP B 2 73  ? 175.125 157.729 199.471 1.00 27.87  ? 73  TRP B CZ2   1 
ATOM   4707  C  CZ3   . TRP B 2 73  ? 172.775 158.095 199.889 1.00 26.72  ? 73  TRP B CZ3   1 
ATOM   4708  C  CH2   . TRP B 2 73  ? 173.831 157.287 199.451 1.00 27.03  ? 73  TRP B CH2   1 
ATOM   4709  N  N     . ILE B 2 74  ? 172.628 165.165 201.242 1.00 28.15  ? 74  ILE B N     1 
ATOM   4710  C  CA    . ILE B 2 74  ? 171.688 166.105 201.843 1.00 24.01  ? 74  ILE B CA    1 
ATOM   4711  C  C     . ILE B 2 74  ? 170.502 166.335 200.913 1.00 22.57  ? 74  ILE B C     1 
ATOM   4712  O  O     . ILE B 2 74  ? 169.358 166.470 201.364 1.00 25.32  ? 74  ILE B O     1 
ATOM   4713  C  CB    . ILE B 2 74  ? 172.410 167.418 202.198 1.00 20.18  ? 74  ILE B CB    1 
ATOM   4714  C  CG1   . ILE B 2 74  ? 173.295 167.218 203.430 1.00 23.40  ? 74  ILE B CG1   1 
ATOM   4715  C  CG2   . ILE B 2 74  ? 171.415 168.541 202.441 1.00 18.67  ? 74  ILE B CG2   1 
ATOM   4716  C  CD1   . ILE B 2 74  ? 174.307 168.321 203.644 1.00 26.63  ? 74  ILE B CD1   1 
ATOM   4717  N  N     . THR B 2 75  ? 170.753 166.370 199.602 1.00 17.97  ? 75  THR B N     1 
ATOM   4718  C  CA    . THR B 2 75  ? 169.678 166.594 198.639 1.00 24.00  ? 75  THR B CA    1 
ATOM   4719  C  C     . THR B 2 75  ? 168.650 165.468 198.682 1.00 22.52  ? 75  THR B C     1 
ATOM   4720  O  O     . THR B 2 75  ? 167.440 165.718 198.675 1.00 26.76  ? 75  THR B O     1 
ATOM   4721  C  CB    . THR B 2 75  ? 170.257 166.739 197.231 1.00 19.74  ? 75  THR B CB    1 
ATOM   4722  O  OG1   . THR B 2 75  ? 171.348 167.667 197.254 1.00 29.56  ? 75  THR B OG1   1 
ATOM   4723  C  CG2   . THR B 2 75  ? 169.194 167.238 196.266 1.00 20.36  ? 75  THR B CG2   1 
ATOM   4724  N  N     . VAL B 2 76  ? 169.113 164.215 198.727 1.00 29.24  ? 76  VAL B N     1 
ATOM   4725  C  CA    . VAL B 2 76  ? 168.172 163.101 198.798 1.00 25.21  ? 76  VAL B CA    1 
ATOM   4726  C  C     . VAL B 2 76  ? 167.510 163.045 200.168 1.00 22.92  ? 76  VAL B C     1 
ATOM   4727  O  O     . VAL B 2 76  ? 166.360 162.607 200.290 1.00 28.27  ? 76  VAL B O     1 
ATOM   4728  C  CB    . VAL B 2 76  ? 168.862 161.769 198.444 1.00 28.69  ? 76  VAL B CB    1 
ATOM   4729  C  CG1   . VAL B 2 76  ? 169.346 161.787 197.006 1.00 29.39  ? 76  VAL B CG1   1 
ATOM   4730  C  CG2   . VAL B 2 76  ? 170.012 161.481 199.388 1.00 32.36  ? 76  VAL B CG2   1 
ATOM   4731  N  N     . LEU B 2 77  ? 168.210 163.486 201.216 1.00 22.74  ? 77  LEU B N     1 
ATOM   4732  C  CA    . LEU B 2 77  ? 167.601 163.527 202.541 1.00 22.54  ? 77  LEU B CA    1 
ATOM   4733  C  C     . LEU B 2 77  ? 166.556 164.632 202.633 1.00 22.05  ? 77  LEU B C     1 
ATOM   4734  O  O     . LEU B 2 77  ? 165.535 164.473 203.312 1.00 30.84  ? 77  LEU B O     1 
ATOM   4735  C  CB    . LEU B 2 77  ? 168.676 163.717 203.610 1.00 26.36  ? 77  LEU B CB    1 
ATOM   4736  C  CG    . LEU B 2 77  ? 168.334 163.202 205.009 1.00 32.75  ? 77  LEU B CG    1 
ATOM   4737  C  CD1   . LEU B 2 77  ? 168.408 161.684 205.061 1.00 28.18  ? 77  LEU B CD1   1 
ATOM   4738  C  CD2   . LEU B 2 77  ? 169.252 163.824 206.050 1.00 30.05  ? 77  LEU B CD2   1 
ATOM   4739  N  N     . PHE B 2 78  ? 166.793 165.758 201.957 1.00 23.22  ? 78  PHE B N     1 
ATOM   4740  C  CA    . PHE B 2 78  ? 165.823 166.847 201.976 1.00 22.97  ? 78  PHE B CA    1 
ATOM   4741  C  C     . PHE B 2 78  ? 164.563 166.475 201.205 1.00 26.39  ? 78  PHE B C     1 
ATOM   4742  O  O     . PHE B 2 78  ? 163.453 166.843 201.604 1.00 27.59  ? 78  PHE B O     1 
ATOM   4743  C  CB    . PHE B 2 78  ? 166.451 168.118 201.405 1.00 26.87  ? 78  PHE B CB    1 
ATOM   4744  C  CG    . PHE B 2 78  ? 167.239 168.910 202.410 1.00 31.16  ? 78  PHE B CG    1 
ATOM   4745  C  CD1   . PHE B 2 78  ? 167.281 168.524 203.739 1.00 29.41  ? 78  PHE B CD1   1 
ATOM   4746  C  CD2   . PHE B 2 78  ? 167.939 170.040 202.024 1.00 26.65  ? 78  PHE B CD2   1 
ATOM   4747  C  CE1   . PHE B 2 78  ? 168.007 169.250 204.664 1.00 27.58  ? 78  PHE B CE1   1 
ATOM   4748  C  CE2   . PHE B 2 78  ? 168.665 170.771 202.944 1.00 29.52  ? 78  PHE B CE2   1 
ATOM   4749  C  CZ    . PHE B 2 78  ? 168.699 170.375 204.266 1.00 30.57  ? 78  PHE B CZ    1 
ATOM   4750  N  N     . ALA B 2 79  ? 164.717 165.751 200.093 1.00 22.66  ? 79  ALA B N     1 
ATOM   4751  C  CA    . ALA B 2 79  ? 163.553 165.305 199.334 1.00 28.23  ? 79  ALA B CA    1 
ATOM   4752  C  C     . ALA B 2 79  ? 162.724 164.304 200.129 1.00 26.47  ? 79  ALA B C     1 
ATOM   4753  O  O     . ALA B 2 79  ? 161.489 164.342 200.092 1.00 33.03  ? 79  ALA B O     1 
ATOM   4754  C  CB    . ALA B 2 79  ? 163.996 164.698 198.003 1.00 20.50  ? 79  ALA B CB    1 
ATOM   4755  N  N     . ASN B 2 80  ? 163.386 163.399 200.854 1.00 25.80  ? 80  ASN B N     1 
ATOM   4756  C  CA    . ASN B 2 80  ? 162.655 162.420 201.651 1.00 29.12  ? 80  ASN B CA    1 
ATOM   4757  C  C     . ASN B 2 80  ? 162.062 163.057 202.901 1.00 30.86  ? 80  ASN B C     1 
ATOM   4758  O  O     . ASN B 2 80  ? 161.093 162.540 203.468 1.00 37.14  ? 80  ASN B O     1 
ATOM   4759  C  CB    . ASN B 2 80  ? 163.572 161.257 202.029 1.00 23.80  ? 80  ASN B CB    1 
ATOM   4760  C  CG    . ASN B 2 80  ? 164.142 160.547 200.820 1.00 32.91  ? 80  ASN B CG    1 
ATOM   4761  O  OD1   . ASN B 2 80  ? 163.571 160.596 199.731 1.00 38.21  ? 80  ASN B OD1   1 
ATOM   4762  N  ND2   . ASN B 2 80  ? 165.275 159.881 201.005 1.00 30.44  ? 80  ASN B ND2   1 
ATOM   4763  N  N     . PHE B 2 81  ? 162.627 164.182 203.343 1.00 32.56  ? 81  PHE B N     1 
ATOM   4764  C  CA    . PHE B 2 81  ? 162.088 164.865 204.514 1.00 29.43  ? 81  PHE B CA    1 
ATOM   4765  C  C     . PHE B 2 81  ? 160.774 165.559 204.184 1.00 32.12  ? 81  PHE B C     1 
ATOM   4766  O  O     . PHE B 2 81  ? 159.843 165.563 204.997 1.00 36.68  ? 81  PHE B O     1 
ATOM   4767  C  CB    . PHE B 2 81  ? 163.113 165.862 205.055 1.00 28.26  ? 81  PHE B CB    1 
ATOM   4768  C  CG    . PHE B 2 81  ? 162.554 166.824 206.065 1.00 31.93  ? 81  PHE B CG    1 
ATOM   4769  C  CD1   . PHE B 2 81  ? 162.406 166.451 207.390 1.00 29.70  ? 81  PHE B CD1   1 
ATOM   4770  C  CD2   . PHE B 2 81  ? 162.196 168.110 205.694 1.00 34.96  ? 81  PHE B CD2   1 
ATOM   4771  C  CE1   . PHE B 2 81  ? 161.897 167.335 208.322 1.00 32.79  ? 81  PHE B CE1   1 
ATOM   4772  C  CE2   . PHE B 2 81  ? 161.687 168.999 206.621 1.00 33.65  ? 81  PHE B CE2   1 
ATOM   4773  C  CZ    . PHE B 2 81  ? 161.539 168.611 207.937 1.00 34.11  ? 81  PHE B CZ    1 
ATOM   4774  N  N     . ALA B 2 82  ? 160.681 166.157 202.993 1.00 33.04  ? 82  ALA B N     1 
ATOM   4775  C  CA    . ALA B 2 82  ? 159.429 166.777 202.573 1.00 29.87  ? 82  ALA B CA    1 
ATOM   4776  C  C     . ALA B 2 82  ? 158.328 165.738 202.407 1.00 36.94  ? 82  ALA B C     1 
ATOM   4777  O  O     . ALA B 2 82  ? 157.177 165.974 202.793 1.00 33.82  ? 82  ALA B O     1 
ATOM   4778  C  CB    . ALA B 2 82  ? 159.638 167.550 201.272 1.00 29.23  ? 82  ALA B CB    1 
ATOM   4779  N  N     . GLU B 2 83  ? 158.662 164.584 201.825 1.00 33.45  ? 83  GLU B N     1 
ATOM   4780  C  CA    . GLU B 2 83  ? 157.680 163.514 201.682 1.00 35.64  ? 83  GLU B CA    1 
ATOM   4781  C  C     . GLU B 2 83  ? 157.244 162.978 203.040 1.00 34.63  ? 83  GLU B C     1 
ATOM   4782  O  O     . GLU B 2 83  ? 156.056 162.717 203.258 1.00 39.60  ? 83  GLU B O     1 
ATOM   4783  C  CB    . GLU B 2 83  ? 158.253 162.393 200.816 1.00 35.87  ? 83  GLU B CB    1 
ATOM   4784  C  CG    . GLU B 2 83  ? 157.441 161.110 200.831 1.00 36.03  ? 83  GLU B CG    1 
ATOM   4785  C  CD    . GLU B 2 83  ? 157.941 160.094 199.823 1.00 44.05  ? 83  GLU B CD    1 
ATOM   4786  O  OE1   . GLU B 2 83  ? 159.102 159.650 199.950 1.00 43.86  ? 83  GLU B OE1   1 
ATOM   4787  O  OE2   . GLU B 2 83  ? 157.174 159.739 198.904 1.00 48.06  ? 83  GLU B OE2   1 
ATOM   4788  N  N     . ALA B 2 84  ? 158.192 162.810 203.965 1.00 35.64  ? 84  ALA B N     1 
ATOM   4789  C  CA    . ALA B 2 84  ? 157.848 162.329 205.299 1.00 36.51  ? 84  ALA B CA    1 
ATOM   4790  C  C     . ALA B 2 84  ? 157.023 163.356 206.063 1.00 38.30  ? 84  ALA B C     1 
ATOM   4791  O  O     . ALA B 2 84  ? 156.118 162.992 206.823 1.00 39.89  ? 84  ALA B O     1 
ATOM   4792  C  CB    . ALA B 2 84  ? 159.116 161.973 206.074 1.00 36.10  ? 84  ALA B CB    1 
ATOM   4793  N  N     . LEU B 2 85  ? 157.326 164.644 205.883 1.00 34.40  ? 85  LEU B N     1 
ATOM   4794  C  CA    . LEU B 2 85  ? 156.556 165.687 206.553 1.00 35.87  ? 85  LEU B CA    1 
ATOM   4795  C  C     . LEU B 2 85  ? 155.107 165.696 206.082 1.00 39.61  ? 85  LEU B C     1 
ATOM   4796  O  O     . LEU B 2 85  ? 154.183 165.819 206.894 1.00 40.51  ? 85  LEU B O     1 
ATOM   4797  C  CB    . LEU B 2 85  ? 157.203 167.051 206.320 1.00 36.44  ? 85  LEU B CB    1 
ATOM   4798  C  CG    . LEU B 2 85  ? 156.964 168.118 207.390 1.00 39.56  ? 85  LEU B CG    1 
ATOM   4799  C  CD1   . LEU B 2 85  ? 157.680 167.766 208.683 1.00 38.15  ? 85  LEU B CD1   1 
ATOM   4800  C  CD2   . LEU B 2 85  ? 157.403 169.482 206.886 1.00 35.63  ? 85  LEU B CD2   1 
ATOM   4801  N  N     . ALA B 2 86  ? 154.888 165.573 204.770 1.00 35.12  ? 86  ALA B N     1 
ATOM   4802  C  CA    . ALA B 2 86  ? 153.524 165.526 204.254 1.00 33.66  ? 86  ALA B CA    1 
ATOM   4803  C  C     . ALA B 2 86  ? 152.805 164.263 204.708 1.00 40.34  ? 86  ALA B C     1 
ATOM   4804  O  O     . ALA B 2 86  ? 151.638 164.317 205.112 1.00 41.92  ? 86  ALA B O     1 
ATOM   4805  C  CB    . ALA B 2 86  ? 153.536 165.620 202.729 1.00 34.33  ? 86  ALA B CB    1 
ATOM   4806  N  N     . GLU B 2 87  ? 153.485 163.115 204.648 1.00 42.96  ? 87  GLU B N     1 
ATOM   4807  C  CA    . GLU B 2 87  ? 152.882 161.872 205.116 1.00 40.46  ? 87  GLU B CA    1 
ATOM   4808  C  C     . GLU B 2 87  ? 152.661 161.898 206.623 1.00 42.32  ? 87  GLU B C     1 
ATOM   4809  O  O     . GLU B 2 87  ? 151.619 161.444 207.110 1.00 46.17  ? 87  GLU B O     1 
ATOM   4810  C  CB    . GLU B 2 87  ? 153.758 160.684 204.720 1.00 39.20  ? 87  GLU B CB    1 
ATOM   4811  C  CG    . GLU B 2 87  ? 153.527 160.188 203.303 1.00 42.62  ? 87  GLU B CG    1 
ATOM   4812  C  CD    . GLU B 2 87  ? 154.677 159.348 202.785 1.00 47.49  ? 87  GLU B CD    1 
ATOM   4813  O  OE1   . GLU B 2 87  ? 155.582 159.022 203.581 1.00 46.73  ? 87  GLU B OE1   1 
ATOM   4814  O  OE2   . GLU B 2 87  ? 154.677 159.015 201.581 1.00 50.97  ? 87  GLU B OE2   1 
ATOM   4815  N  N     . GLY B 2 88  ? 153.629 162.426 207.376 1.00 45.20  ? 88  GLY B N     1 
ATOM   4816  C  CA    . GLY B 2 88  ? 153.476 162.494 208.820 1.00 43.46  ? 88  GLY B CA    1 
ATOM   4817  C  C     . GLY B 2 88  ? 152.313 163.369 209.245 1.00 46.04  ? 88  GLY B C     1 
ATOM   4818  O  O     . GLY B 2 88  ? 151.580 163.033 210.179 1.00 48.62  ? 88  GLY B O     1 
ATOM   4819  N  N     . ARG B 2 89  ? 152.131 164.505 208.569 1.00 49.21  ? 89  ARG B N     1 
ATOM   4820  C  CA    . ARG B 2 89  ? 150.975 165.350 208.849 1.00 49.83  ? 89  ARG B CA    1 
ATOM   4821  C  C     . ARG B 2 89  ? 149.684 164.677 208.400 1.00 50.46  ? 89  ARG B C     1 
ATOM   4822  O  O     . ARG B 2 89  ? 148.620 164.908 208.985 1.00 50.05  ? 89  ARG B O     1 
ATOM   4823  C  CB    . ARG B 2 89  ? 151.142 166.709 208.169 1.00 47.97  ? 89  ARG B CB    1 
ATOM   4824  C  CG    . ARG B 2 89  ? 152.083 167.652 208.898 1.00 51.68  ? 89  ARG B CG    1 
ATOM   4825  C  CD    . ARG B 2 89  ? 152.523 168.803 208.007 1.00 50.38  ? 89  ARG B CD    1 
ATOM   4826  N  NE    . ARG B 2 89  ? 151.428 169.321 207.196 1.00 53.29  ? 89  ARG B NE    1 
ATOM   4827  C  CZ    . ARG B 2 89  ? 150.954 170.556 207.279 1.00 56.13  ? 89  ARG B CZ    1 
ATOM   4828  N  NH1   . ARG B 2 89  ? 151.456 171.433 208.134 1.00 51.88  ? 89  ARG B NH1   1 
ATOM   4829  N  NH2   . ARG B 2 89  ? 149.952 170.922 206.485 1.00 55.48  ? 89  ARG B NH2   1 
ATOM   4830  N  N     . SER B 2 90  ? 149.758 163.843 207.359 1.00 52.57  ? 90  SER B N     1 
ATOM   4831  C  CA    . SER B 2 90  ? 148.572 163.131 206.896 1.00 50.47  ? 90  SER B CA    1 
ATOM   4832  C  C     . SER B 2 90  ? 148.172 162.028 207.870 1.00 51.19  ? 90  SER B C     1 
ATOM   4833  O  O     . SER B 2 90  ? 146.985 161.862 208.173 1.00 53.72  ? 90  SER B O     1 
ATOM   4834  C  CB    . SER B 2 90  ? 148.817 162.554 205.503 1.00 48.66  ? 90  SER B CB    1 
ATOM   4835  O  OG    . SER B 2 90  ? 147.609 162.461 204.769 1.00 54.56  ? 90  SER B OG    1 
ATOM   4836  N  N     . LYS B 2 91  ? 149.147 161.263 208.369 1.00 53.30  ? 91  LYS B N     1 
ATOM   4837  C  CA    . LYS B 2 91  ? 148.831 160.212 209.330 1.00 52.83  ? 91  LYS B CA    1 
ATOM   4838  C  C     . LYS B 2 91  ? 148.426 160.788 210.680 1.00 55.33  ? 91  LYS B C     1 
ATOM   4839  O  O     . LYS B 2 91  ? 147.746 160.112 211.460 1.00 56.12  ? 91  LYS B O     1 
ATOM   4840  C  CB    . LYS B 2 91  ? 150.018 159.261 209.491 1.00 52.23  ? 91  LYS B CB    1 
ATOM   4841  C  CG    . LYS B 2 91  ? 150.200 158.295 208.328 1.00 55.52  ? 91  LYS B CG    1 
ATOM   4842  C  CD    . LYS B 2 91  ? 151.585 157.662 208.327 1.00 58.25  ? 91  LYS B CD    1 
ATOM   4843  C  CE    . LYS B 2 91  ? 152.684 158.710 208.341 1.00 55.59  ? 91  LYS B CE    1 
ATOM   4844  N  NZ    . LYS B 2 91  ? 154.039 158.092 208.339 1.00 54.37  ? 91  LYS B NZ    1 
ATOM   4845  N  N     . ALA B 2 92  ? 148.838 162.023 210.978 1.00 54.04  ? 92  ALA B N     1 
ATOM   4846  C  CA    . ALA B 2 92  ? 148.387 162.674 212.203 1.00 53.42  ? 92  ALA B CA    1 
ATOM   4847  C  C     . ALA B 2 92  ? 146.879 162.891 212.184 1.00 56.82  ? 92  ALA B C     1 
ATOM   4848  O  O     . ALA B 2 92  ? 146.199 162.674 213.193 1.00 61.44  ? 92  ALA B O     1 
ATOM   4849  C  CB    . ALA B 2 92  ? 149.120 164.001 212.395 1.00 54.95  ? 92  ALA B CB    1 
ATOM   4850  N  N     . GLN B 2 93  ? 146.340 163.326 211.042 1.00 57.93  ? 93  GLN B N     1 
ATOM   4851  C  CA    . GLN B 2 93  ? 144.892 163.455 210.910 1.00 56.80  ? 93  GLN B CA    1 
ATOM   4852  C  C     . GLN B 2 93  ? 144.212 162.092 210.949 1.00 56.07  ? 93  GLN B C     1 
ATOM   4853  O  O     . GLN B 2 93  ? 143.134 161.947 211.538 1.00 54.94  ? 93  GLN B O     1 
ATOM   4854  C  CB    . GLN B 2 93  ? 144.548 164.192 209.616 1.00 55.28  ? 93  GLN B CB    1 
ATOM   4855  C  CG    . GLN B 2 93  ? 145.005 165.640 209.583 1.00 56.00  ? 93  GLN B CG    1 
ATOM   4856  C  CD    . GLN B 2 93  ? 144.661 166.328 208.276 1.00 57.26  ? 93  GLN B CD    1 
ATOM   4857  O  OE1   . GLN B 2 93  ? 144.977 165.830 207.197 1.00 55.89  ? 93  GLN B OE1   1 
ATOM   4858  N  NE2   . GLN B 2 93  ? 144.009 167.482 208.368 1.00 57.53  ? 93  GLN B NE2   1 
ATOM   4859  N  N     . ALA B 2 94  ? 144.822 161.085 210.319 1.00 61.79  ? 94  ALA B N     1 
ATOM   4860  C  CA    . ALA B 2 94  ? 144.259 159.739 210.352 1.00 63.03  ? 94  ALA B CA    1 
ATOM   4861  C  C     . ALA B 2 94  ? 144.254 159.177 211.768 1.00 65.08  ? 94  ALA B C     1 
ATOM   4862  O  O     . ALA B 2 94  ? 143.285 158.532 212.185 1.00 66.49  ? 94  ALA B O     1 
ATOM   4863  C  CB    . ALA B 2 94  ? 145.038 158.820 209.412 1.00 63.77  ? 94  ALA B CB    1 
ATOM   4864  N  N     . ASN B 2 95  ? 145.332 159.409 212.523 1.00 65.64  ? 95  ASN B N     1 
ATOM   4865  C  CA    . ASN B 2 95  ? 145.371 158.958 213.910 1.00 66.42  ? 95  ASN B CA    1 
ATOM   4866  C  C     . ASN B 2 95  ? 144.346 159.700 214.758 1.00 67.71  ? 95  ASN B C     1 
ATOM   4867  O  O     . ASN B 2 95  ? 143.764 159.126 215.686 1.00 69.93  ? 95  ASN B O     1 
ATOM   4868  C  CB    . ASN B 2 95  ? 146.776 159.142 214.484 1.00 67.09  ? 95  ASN B CB    1 
ATOM   4869  C  CG    . ASN B 2 95  ? 147.757 158.106 213.969 1.00 68.43  ? 95  ASN B CG    1 
ATOM   4870  O  OD1   . ASN B 2 95  ? 147.384 157.195 213.230 1.00 69.46  ? 95  ASN B OD1   1 
ATOM   4871  N  ND2   . ASN B 2 95  ? 149.019 158.242 214.358 1.00 67.03  ? 95  ASN B ND2   1 
ATOM   4872  N  N     . SER B 2 96  ? 144.081 160.951 214.395 1.00 65.99  ? 96  SER B N     1 
ATOM   4873  C  CA    . SER B 2 96  ? 143.075 161.744 215.138 1.00 65.98  ? 96  SER B CA    1 
ATOM   4874  C  C     . SER B 2 96  ? 141.698 161.111 214.962 1.00 68.21  ? 96  SER B C     1 
ATOM   4875  O  O     . SER B 2 96  ? 140.904 161.162 215.908 1.00 69.60  ? 96  SER B O     1 
ATOM   4876  C  CB    . SER B 2 96  ? 143.068 163.167 214.696 1.00 64.59  ? 96  SER B CB    1 
ATOM   4877  O  OG    . SER B 2 96  ? 141.971 163.862 215.262 1.00 66.56  ? 96  SER B OG    1 
ATOM   4878  N  N     . LEU B 2 97  ? 141.432 160.530 213.798 1.00 84.91  ? 97  LEU B N     1 
ATOM   4879  C  CA    . LEU B 2 97  ? 140.080 159.976 213.533 1.00 80.42  ? 97  LEU B CA    1 
ATOM   4880  C  C     . LEU B 2 97  ? 139.991 158.587 214.148 1.00 75.81  ? 97  LEU B C     1 
ATOM   4881  O  O     . LEU B 2 97  ? 138.947 158.273 214.707 1.00 81.41  ? 97  LEU B O     1 
ATOM   4882  C  CB    . LEU B 2 97  ? 139.810 159.918 212.027 1.00 74.24  ? 97  LEU B CB    1 
ATOM   4883  C  CG    . LEU B 2 97  ? 139.585 161.263 211.344 1.00 72.57  ? 97  LEU B CG    1 
ATOM   4884  C  CD1   . LEU B 2 97  ? 139.370 161.074 209.854 1.00 73.93  ? 97  LEU B CD1   1 
ATOM   4885  C  CD2   . LEU B 2 97  ? 138.400 161.984 211.963 1.00 75.15  ? 97  LEU B CD2   1 
ATOM   4886  N  N     . LYS B 2 98  ? 141.047 157.789 214.067 1.00 81.61  ? 98  LYS B N     1 
ATOM   4887  C  CA    . LYS B 2 98  ? 140.914 156.495 214.728 1.00 81.79  ? 98  LYS B CA    1 
ATOM   4888  C  C     . LYS B 2 98  ? 140.629 156.667 216.214 1.00 84.85  ? 98  LYS B C     1 
ATOM   4889  O  O     . LYS B 2 98  ? 140.164 155.734 216.879 1.00 90.70  ? 98  LYS B O     1 
ATOM   4890  C  CB    . LYS B 2 98  ? 142.180 155.663 214.523 1.00 80.52  ? 98  LYS B CB    1 
ATOM   4891  C  CG    . LYS B 2 98  ? 142.498 155.348 213.072 1.00 82.89  ? 98  LYS B CG    1 
ATOM   4892  C  CD    . LYS B 2 98  ? 143.790 154.557 212.952 1.00 83.14  ? 98  LYS B CD    1 
ATOM   4893  C  CE    . LYS B 2 98  ? 144.113 154.248 211.500 1.00 88.82  ? 98  LYS B CE    1 
ATOM   4894  N  NZ    . LYS B 2 98  ? 145.417 153.546 211.357 1.00 86.63  ? 98  LYS B NZ    1 
ATOM   4895  N  N     . GLY B 2 99  ? 140.900 157.854 216.751 1.00 93.33  ? 99  GLY B N     1 
ATOM   4896  C  CA    . GLY B 2 99  ? 140.742 158.114 218.167 1.00 96.52  ? 99  GLY B CA    1 
ATOM   4897  C  C     . GLY B 2 99  ? 139.305 158.210 218.634 1.00 101.12 ? 99  GLY B C     1 
ATOM   4898  O  O     . GLY B 2 99  ? 139.052 158.279 219.841 1.00 103.46 ? 99  GLY B O     1 
ATOM   4899  N  N     . VAL B 2 100 ? 138.357 158.232 217.697 1.00 110.86 ? 100 VAL B N     1 
ATOM   4900  C  CA    . VAL B 2 100 ? 136.940 158.315 218.037 1.00 110.77 ? 100 VAL B CA    1 
ATOM   4901  C  C     . VAL B 2 100 ? 136.563 157.126 218.911 1.00 112.86 ? 100 VAL B C     1 
ATOM   4902  O  O     . VAL B 2 100 ? 136.941 155.983 218.629 1.00 116.27 ? 100 VAL B O     1 
ATOM   4903  C  CB    . VAL B 2 100 ? 136.055 158.385 216.777 1.00 103.37 ? 100 VAL B CB    1 
ATOM   4904  C  CG1   . VAL B 2 100 ? 136.273 159.704 216.051 1.00 104.14 ? 100 VAL B CG1   1 
ATOM   4905  C  CG2   . VAL B 2 100 ? 136.330 157.209 215.853 1.00 103.68 ? 100 VAL B CG2   1 
ATOM   4906  N  N     . LYS B 2 101 ? 135.833 157.391 219.990 1.00 120.64 ? 101 LYS B N     1 
ATOM   4907  C  CA    . LYS B 2 101 ? 135.506 156.343 220.943 1.00 119.92 ? 101 LYS B CA    1 
ATOM   4908  C  C     . LYS B 2 101 ? 134.338 155.502 220.444 1.00 121.26 ? 101 LYS B C     1 
ATOM   4909  O  O     . LYS B 2 101 ? 133.305 156.028 220.024 1.00 122.85 ? 101 LYS B O     1 
ATOM   4910  C  CB    . LYS B 2 101 ? 135.172 156.952 222.305 1.00 120.33 ? 101 LYS B CB    1 
ATOM   4911  C  CG    . LYS B 2 101 ? 135.170 155.958 223.460 1.00 122.62 ? 101 LYS B CG    1 
ATOM   4912  C  CD    . LYS B 2 101 ? 136.213 154.867 223.269 1.00 124.42 ? 101 LYS B CD    1 
ATOM   4913  C  CE    . LYS B 2 101 ? 135.938 153.677 224.175 1.00 123.81 ? 101 LYS B CE    1 
ATOM   4914  N  NZ    . LYS B 2 101 ? 136.467 152.409 223.600 1.00 121.21 ? 101 LYS B NZ    1 
ATOM   4915  N  N     . LYS B 2 102 ? 134.512 154.185 220.491 1.00 131.52 ? 102 LYS B N     1 
ATOM   4916  C  CA    . LYS B 2 102 ? 133.446 153.233 220.215 1.00 130.86 ? 102 LYS B CA    1 
ATOM   4917  C  C     . LYS B 2 102 ? 132.865 152.764 221.540 1.00 131.89 ? 102 LYS B C     1 
ATOM   4918  O  O     . LYS B 2 102 ? 133.595 152.253 222.396 1.00 132.50 ? 102 LYS B O     1 
ATOM   4919  C  CB    . LYS B 2 102 ? 133.961 152.045 219.400 1.00 131.18 ? 102 LYS B CB    1 
ATOM   4920  C  CG    . LYS B 2 102 ? 134.327 152.389 217.966 1.00 129.47 ? 102 LYS B CG    1 
ATOM   4921  C  CD    . LYS B 2 102 ? 135.548 151.611 217.503 1.00 130.91 ? 102 LYS B CD    1 
ATOM   4922  C  CE    . LYS B 2 102 ? 136.789 152.018 218.279 1.00 130.28 ? 102 LYS B CE    1 
ATOM   4923  N  NZ    . LYS B 2 102 ? 137.091 153.467 218.116 1.00 130.59 ? 102 LYS B NZ    1 
ATOM   4924  N  N     . THR B 2 103 ? 131.552 152.942 221.705 1.00 132.54 ? 103 THR B N     1 
ATOM   4925  C  CA    . THR B 2 103 ? 130.928 152.699 223.003 1.00 132.73 ? 103 THR B CA    1 
ATOM   4926  C  C     . THR B 2 103 ? 131.033 151.235 223.414 1.00 133.21 ? 103 THR B C     1 
ATOM   4927  O  O     . THR B 2 103 ? 131.173 150.931 224.605 1.00 133.63 ? 103 THR B O     1 
ATOM   4928  C  CB    . THR B 2 103 ? 129.464 153.146 222.977 1.00 132.08 ? 103 THR B CB    1 
ATOM   4929  O  OG1   . THR B 2 103 ? 128.819 152.750 224.194 1.00 134.14 ? 103 THR B OG1   1 
ATOM   4930  C  CG2   . THR B 2 103 ? 128.728 152.532 221.792 1.00 131.84 ? 103 THR B CG2   1 
ATOM   4931  N  N     . ALA B 2 104 ? 130.938 150.317 222.448 1.00 134.74 ? 104 ALA B N     1 
ATOM   4932  C  CA    . ALA B 2 104 ? 130.949 148.877 222.693 1.00 134.21 ? 104 ALA B CA    1 
ATOM   4933  C  C     . ALA B 2 104 ? 129.753 148.454 223.540 1.00 137.82 ? 104 ALA B C     1 
ATOM   4934  O  O     . ALA B 2 104 ? 129.656 147.295 223.956 1.00 138.73 ? 104 ALA B O     1 
ATOM   4935  C  CB    . ALA B 2 104 ? 132.260 148.438 223.354 1.00 133.25 ? 104 ALA B CB    1 
ATOM   4936  N  N     . PHE B 2 105 ? 128.839 149.388 223.799 1.00 151.07 ? 105 PHE B N     1 
ATOM   4937  C  CA    . PHE B 2 105 ? 127.620 149.130 224.562 1.00 150.47 ? 105 PHE B CA    1 
ATOM   4938  C  C     . PHE B 2 105 ? 126.449 149.224 223.589 1.00 150.31 ? 105 PHE B C     1 
ATOM   4939  O  O     . PHE B 2 105 ? 125.817 150.271 223.444 1.00 149.72 ? 105 PHE B O     1 
ATOM   4940  C  CB    . PHE B 2 105 ? 127.483 150.119 225.714 1.00 150.81 ? 105 PHE B CB    1 
ATOM   4941  C  CG    . PHE B 2 105 ? 126.624 149.625 226.844 1.00 152.70 ? 105 PHE B CG    1 
ATOM   4942  C  CD1   . PHE B 2 105 ? 126.088 148.349 226.822 1.00 152.51 ? 105 PHE B CD1   1 
ATOM   4943  C  CD2   . PHE B 2 105 ? 126.353 150.442 227.929 1.00 153.63 ? 105 PHE B CD2   1 
ATOM   4944  C  CE1   . PHE B 2 105 ? 125.297 147.896 227.862 1.00 151.64 ? 105 PHE B CE1   1 
ATOM   4945  C  CE2   . PHE B 2 105 ? 125.563 149.995 228.971 1.00 153.30 ? 105 PHE B CE2   1 
ATOM   4946  C  CZ    . PHE B 2 105 ? 125.035 148.720 228.937 1.00 151.73 ? 105 PHE B CZ    1 
ATOM   4947  N  N     . ALA B 2 106 ? 126.160 148.113 222.918 1.00 137.39 ? 106 ALA B N     1 
ATOM   4948  C  CA    . ALA B 2 106 ? 125.094 148.043 221.929 1.00 135.71 ? 106 ALA B CA    1 
ATOM   4949  C  C     . ALA B 2 106 ? 123.948 147.220 222.499 1.00 137.97 ? 106 ALA B C     1 
ATOM   4950  O  O     . ALA B 2 106 ? 124.130 146.045 222.836 1.00 141.41 ? 106 ALA B O     1 
ATOM   4951  C  CB    . ALA B 2 106 ? 125.598 147.433 220.622 1.00 133.81 ? 106 ALA B CB    1 
ATOM   4952  N  N     . ARG B 2 107 ? 122.770 147.837 222.601 1.00 112.59 ? 107 ARG B N     1 
ATOM   4953  C  CA    . ARG B 2 107 ? 121.582 147.159 223.115 1.00 109.13 ? 107 ARG B CA    1 
ATOM   4954  C  C     . ARG B 2 107 ? 120.826 146.561 221.933 1.00 110.09 ? 107 ARG B C     1 
ATOM   4955  O  O     . ARG B 2 107 ? 119.873 147.135 221.402 1.00 118.99 ? 107 ARG B O     1 
ATOM   4956  C  CB    . ARG B 2 107 ? 120.716 148.121 223.916 1.00 108.82 ? 107 ARG B CB    1 
ATOM   4957  C  CG    . ARG B 2 107 ? 121.491 149.224 224.612 1.00 111.03 ? 107 ARG B CG    1 
ATOM   4958  C  CD    . ARG B 2 107 ? 120.598 150.000 225.563 1.00 112.65 ? 107 ARG B CD    1 
ATOM   4959  N  NE    . ARG B 2 107 ? 121.266 151.178 226.103 1.00 114.66 ? 107 ARG B NE    1 
ATOM   4960  C  CZ    . ARG B 2 107 ? 120.775 151.940 227.070 1.00 115.57 ? 107 ARG B CZ    1 
ATOM   4961  N  NH1   . ARG B 2 107 ? 119.608 151.675 227.633 1.00 113.68 ? 107 ARG B NH1   1 
ATOM   4962  N  NH2   . ARG B 2 107 ? 121.472 152.994 227.483 1.00 114.31 ? 107 ARG B NH2   1 
ATOM   4963  N  N     . LYS B 2 108 ? 121.274 145.382 221.515 1.00 109.27 ? 108 LYS B N     1 
ATOM   4964  C  CA    . LYS B 2 108 ? 120.629 144.692 220.407 1.00 110.57 ? 108 LYS B CA    1 
ATOM   4965  C  C     . LYS B 2 108 ? 119.216 144.280 220.796 1.00 116.93 ? 108 LYS B C     1 
ATOM   4966  O  O     . LYS B 2 108 ? 118.967 143.831 221.917 1.00 119.44 ? 108 LYS B O     1 
ATOM   4967  C  CB    . LYS B 2 108 ? 121.445 143.468 219.996 1.00 110.71 ? 108 LYS B CB    1 
ATOM   4968  C  CG    . LYS B 2 108 ? 120.933 142.777 218.744 1.00 108.70 ? 108 LYS B CG    1 
ATOM   4969  C  CD    . LYS B 2 108 ? 121.967 141.817 218.179 1.00 111.87 ? 108 LYS B CD    1 
ATOM   4970  C  CE    . LYS B 2 108 ? 121.472 141.160 216.901 1.00 112.27 ? 108 LYS B CE    1 
ATOM   4971  N  NZ    . LYS B 2 108 ? 122.528 140.333 216.256 1.00 112.19 ? 108 LYS B NZ    1 
ATOM   4972  N  N     . LEU B 2 109 ? 118.285 144.443 219.862 1.00 132.39 ? 109 LEU B N     1 
ATOM   4973  C  CA    . LEU B 2 109 ? 116.882 144.137 220.097 1.00 131.51 ? 109 LEU B CA    1 
ATOM   4974  C  C     . LEU B 2 109 ? 116.504 142.838 219.399 1.00 133.36 ? 109 LEU B C     1 
ATOM   4975  O  O     . LEU B 2 109 ? 116.879 142.607 218.246 1.00 134.46 ? 109 LEU B O     1 
ATOM   4976  C  CB    . LEU B 2 109 ? 115.988 145.277 219.606 1.00 128.22 ? 109 LEU B CB    1 
ATOM   4977  C  CG    . LEU B 2 109 ? 115.668 146.367 220.631 1.00 128.16 ? 109 LEU B CG    1 
ATOM   4978  C  CD1   . LEU B 2 109 ? 114.545 147.267 220.135 1.00 130.50 ? 109 LEU B CD1   1 
ATOM   4979  C  CD2   . LEU B 2 109 ? 115.315 145.758 221.982 1.00 130.81 ? 109 LEU B CD2   1 
ATOM   4980  N  N     . ARG B 2 110 ? 115.765 141.986 220.113 1.00 140.26 ? 110 ARG B N     1 
ATOM   4981  C  CA    . ARG B 2 110 ? 115.323 140.723 219.531 1.00 140.31 ? 110 ARG B CA    1 
ATOM   4982  C  C     . ARG B 2 110 ? 114.374 140.951 218.360 1.00 142.93 ? 110 ARG B C     1 
ATOM   4983  O  O     . ARG B 2 110 ? 114.424 140.225 217.360 1.00 143.16 ? 110 ARG B O     1 
ATOM   4984  C  CB    . ARG B 2 110 ? 114.659 139.857 220.602 1.00 140.14 ? 110 ARG B CB    1 
ATOM   4985  C  CG    . ARG B 2 110 ? 113.764 140.627 221.560 1.00 141.39 ? 110 ARG B CG    1 
ATOM   4986  C  CD    . ARG B 2 110 ? 113.854 140.067 222.972 1.00 143.63 ? 110 ARG B CD    1 
ATOM   4987  N  NE    . ARG B 2 110 ? 115.148 140.336 223.587 1.00 144.32 ? 110 ARG B NE    1 
ATOM   4988  C  CZ    . ARG B 2 110 ? 116.107 139.432 223.740 1.00 142.92 ? 110 ARG B CZ    1 
ATOM   4989  N  NH1   . ARG B 2 110 ? 115.952 138.183 223.331 1.00 141.66 ? 110 ARG B NH1   1 
ATOM   4990  N  NH2   . ARG B 2 110 ? 117.253 139.792 224.310 1.00 141.78 ? 110 ARG B NH2   1 
ATOM   4991  N  N     . GLU B 2 111 ? 113.489 141.938 218.473 1.00 152.26 ? 111 GLU B N     1 
ATOM   4992  C  CA    . GLU B 2 111 ? 112.568 142.294 217.406 1.00 153.13 ? 111 GLU B CA    1 
ATOM   4993  C  C     . GLU B 2 111 ? 112.583 143.798 217.161 1.00 152.04 ? 111 GLU B C     1 
ATOM   4994  O  O     . GLU B 2 111 ? 112.893 144.577 218.067 1.00 152.32 ? 111 GLU B O     1 
ATOM   4995  C  CB    . GLU B 2 111 ? 111.147 141.770 217.709 1.00 152.24 ? 111 GLU B CB    1 
ATOM   4996  C  CG    . GLU B 2 111 ? 110.571 141.978 219.128 1.00 152.72 ? 111 GLU B CG    1 
ATOM   4997  C  CD    . GLU B 2 111 ? 110.044 143.367 219.433 1.00 153.72 ? 111 GLU B CD    1 
ATOM   4998  O  OE1   . GLU B 2 111 ? 110.291 144.309 218.662 1.00 154.35 ? 111 GLU B OE1   1 
ATOM   4999  O  OE2   . GLU B 2 111 ? 109.358 143.513 220.468 1.00 154.18 ? 111 GLU B OE2   1 
ATOM   5000  N  N     . PRO B 2 112 ? 112.287 144.228 215.929 1.00 129.52 ? 112 PRO B N     1 
ATOM   5001  C  CA    . PRO B 2 112 ? 112.489 145.645 215.571 1.00 129.43 ? 112 PRO B CA    1 
ATOM   5002  C  C     . PRO B 2 112 ? 111.674 146.637 216.388 1.00 130.33 ? 112 PRO B C     1 
ATOM   5003  O  O     . PRO B 2 112 ? 112.135 147.767 216.596 1.00 131.13 ? 112 PRO B O     1 
ATOM   5004  C  CB    . PRO B 2 112 ? 112.091 145.683 214.089 1.00 127.49 ? 112 PRO B CB    1 
ATOM   5005  C  CG    . PRO B 2 112 ? 112.289 144.291 213.608 1.00 126.80 ? 112 PRO B CG    1 
ATOM   5006  C  CD    . PRO B 2 112 ? 111.908 143.416 214.760 1.00 128.02 ? 112 PRO B CD    1 
ATOM   5007  N  N     . LYS B 2 113 ? 110.484 146.262 216.850 1.00 127.79 ? 113 LYS B N     1 
ATOM   5008  C  CA    . LYS B 2 113 ? 109.612 147.216 217.524 1.00 126.71 ? 113 LYS B CA    1 
ATOM   5009  C  C     . LYS B 2 113 ? 110.258 147.721 218.810 1.00 124.95 ? 113 LYS B C     1 
ATOM   5010  O  O     . LYS B 2 113 ? 110.857 146.955 219.569 1.00 127.99 ? 113 LYS B O     1 
ATOM   5011  C  CB    . LYS B 2 113 ? 108.254 146.568 217.826 1.00 129.26 ? 113 LYS B CB    1 
ATOM   5012  C  CG    . LYS B 2 113 ? 107.322 147.347 218.774 1.00 126.37 ? 113 LYS B CG    1 
ATOM   5013  C  CD    . LYS B 2 113 ? 107.019 148.811 218.383 1.00 126.39 ? 113 LYS B CD    1 
ATOM   5014  C  CE    . LYS B 2 113 ? 106.853 149.063 216.879 1.00 127.02 ? 113 LYS B CE    1 
ATOM   5015  N  NZ    . LYS B 2 113 ? 106.037 148.025 216.185 1.00 125.53 ? 113 LYS B NZ    1 
ATOM   5016  N  N     . TYR B 2 114 ? 110.142 149.027 219.041 1.00 100.74 ? 114 TYR B N     1 
ATOM   5017  C  CA    . TYR B 2 114 ? 110.675 149.628 220.255 1.00 103.91 ? 114 TYR B CA    1 
ATOM   5018  C  C     . TYR B 2 114 ? 109.975 149.056 221.482 1.00 107.06 ? 114 TYR B C     1 
ATOM   5019  O  O     . TYR B 2 114 ? 108.780 148.749 221.450 1.00 107.44 ? 114 TYR B O     1 
ATOM   5020  C  CB    . TYR B 2 114 ? 110.498 151.146 220.207 1.00 104.12 ? 114 TYR B CB    1 
ATOM   5021  C  CG    . TYR B 2 114 ? 110.947 151.871 221.456 1.00 104.93 ? 114 TYR B CG    1 
ATOM   5022  C  CD1   . TYR B 2 114 ? 112.190 151.624 222.021 1.00 107.47 ? 114 TYR B CD1   1 
ATOM   5023  C  CD2   . TYR B 2 114 ? 110.118 152.796 222.077 1.00 103.05 ? 114 TYR B CD2   1 
ATOM   5024  C  CE1   . TYR B 2 114 ? 112.599 152.285 223.163 1.00 106.23 ? 114 TYR B CE1   1 
ATOM   5025  C  CE2   . TYR B 2 114 ? 110.518 153.460 223.220 1.00 103.62 ? 114 TYR B CE2   1 
ATOM   5026  C  CZ    . TYR B 2 114 ? 111.759 153.201 223.759 1.00 104.45 ? 114 TYR B CZ    1 
ATOM   5027  O  OH    . TYR B 2 114 ? 112.159 153.862 224.898 1.00 103.39 ? 114 TYR B OH    1 
ATOM   5028  N  N     . GLY B 2 115 ? 110.730 148.910 222.569 1.00 118.42 ? 115 GLY B N     1 
ATOM   5029  C  CA    . GLY B 2 115 ? 110.200 148.409 223.819 1.00 117.85 ? 115 GLY B CA    1 
ATOM   5030  C  C     . GLY B 2 115 ? 110.520 146.964 224.131 1.00 117.69 ? 115 GLY B C     1 
ATOM   5031  O  O     . GLY B 2 115 ? 110.058 146.457 225.162 1.00 118.63 ? 115 GLY B O     1 
ATOM   5032  N  N     . ALA B 2 116 ? 111.290 146.285 223.285 1.00 123.18 ? 116 ALA B N     1 
ATOM   5033  C  CA    . ALA B 2 116 ? 111.638 144.896 223.525 1.00 122.71 ? 116 ALA B CA    1 
ATOM   5034  C  C     . ALA B 2 116 ? 112.819 144.793 224.490 1.00 128.22 ? 116 ALA B C     1 
ATOM   5035  O  O     . ALA B 2 116 ? 113.482 145.782 224.822 1.00 130.05 ? 116 ALA B O     1 
ATOM   5036  C  CB    . ALA B 2 116 ? 111.965 144.190 222.210 1.00 121.21 ? 116 ALA B CB    1 
ATOM   5037  N  N     . ALA B 2 117 ? 113.077 143.570 224.945 1.00 142.37 ? 117 ALA B N     1 
ATOM   5038  C  CA    . ALA B 2 117 ? 114.219 143.306 225.809 1.00 142.06 ? 117 ALA B CA    1 
ATOM   5039  C  C     . ALA B 2 117 ? 115.514 143.394 225.014 1.00 142.19 ? 117 ALA B C     1 
ATOM   5040  O  O     . ALA B 2 117 ? 115.597 142.923 223.876 1.00 139.60 ? 117 ALA B O     1 
ATOM   5041  C  CB    . ALA B 2 117 ? 114.094 141.928 226.458 1.00 139.98 ? 117 ALA B CB    1 
ATOM   5042  N  N     . ALA B 2 118 ? 116.528 144.001 225.624 1.00 147.23 ? 118 ALA B N     1 
ATOM   5043  C  CA    . ALA B 2 118 ? 117.818 144.221 224.986 1.00 146.98 ? 118 ALA B CA    1 
ATOM   5044  C  C     . ALA B 2 118 ? 118.892 143.422 225.712 1.00 147.61 ? 118 ALA B C     1 
ATOM   5045  O  O     . ALA B 2 118 ? 118.946 143.425 226.947 1.00 146.71 ? 118 ALA B O     1 
ATOM   5046  C  CB    . ALA B 2 118 ? 118.177 145.708 224.980 1.00 145.54 ? 118 ALA B CB    1 
ATOM   5047  N  N     . ASP B 2 119 ? 119.741 142.744 224.945 1.00 149.42 ? 119 ASP B N     1 
ATOM   5048  C  CA    . ASP B 2 119 ? 120.826 141.938 225.485 1.00 149.82 ? 119 ASP B CA    1 
ATOM   5049  C  C     . ASP B 2 119 ? 122.159 142.634 225.247 1.00 149.51 ? 119 ASP B C     1 
ATOM   5050  O  O     . ASP B 2 119 ? 122.404 143.178 224.165 1.00 148.53 ? 119 ASP B O     1 
ATOM   5051  C  CB    . ASP B 2 119 ? 120.844 140.540 224.857 1.00 149.05 ? 119 ASP B CB    1 
ATOM   5052  C  CG    . ASP B 2 119 ? 120.431 140.549 223.399 1.00 147.84 ? 119 ASP B CG    1 
ATOM   5053  O  OD1   . ASP B 2 119 ? 120.457 141.633 222.781 1.00 148.99 ? 119 ASP B OD1   1 
ATOM   5054  O  OD2   . ASP B 2 119 ? 120.084 139.472 222.869 1.00 148.01 ? 119 ASP B OD2   1 
ATOM   5055  N  N     . LYS B 2 120 ? 123.014 142.621 226.267 1.00 150.26 ? 120 LYS B N     1 
ATOM   5056  C  CA    . LYS B 2 120 ? 124.322 143.258 226.176 1.00 148.51 ? 120 LYS B CA    1 
ATOM   5057  C  C     . LYS B 2 120 ? 125.174 142.547 225.131 1.00 149.45 ? 120 LYS B C     1 
ATOM   5058  O  O     . LYS B 2 120 ? 125.491 141.362 225.277 1.00 150.71 ? 120 LYS B O     1 
ATOM   5059  C  CB    . LYS B 2 120 ? 125.006 143.237 227.542 1.00 150.08 ? 120 LYS B CB    1 
ATOM   5060  C  CG    . LYS B 2 120 ? 126.495 143.573 227.533 1.00 149.60 ? 120 LYS B CG    1 
ATOM   5061  C  CD    . LYS B 2 120 ? 126.801 144.871 226.801 1.00 147.89 ? 120 LYS B CD    1 
ATOM   5062  C  CE    . LYS B 2 120 ? 128.299 145.044 226.615 1.00 146.40 ? 120 LYS B CE    1 
ATOM   5063  N  NZ    . LYS B 2 120 ? 128.622 146.155 225.684 1.00 146.38 ? 120 LYS B NZ    1 
ATOM   5064  N  N     . VAL B 2 121 ? 125.542 143.271 224.079 1.00 142.67 ? 121 VAL B N     1 
ATOM   5065  C  CA    . VAL B 2 121 ? 126.399 142.745 223.019 1.00 144.17 ? 121 VAL B CA    1 
ATOM   5066  C  C     . VAL B 2 121 ? 127.410 143.821 222.638 1.00 144.48 ? 121 VAL B C     1 
ATOM   5067  O  O     . VAL B 2 121 ? 127.020 144.970 222.384 1.00 145.58 ? 121 VAL B O     1 
ATOM   5068  C  CB    . VAL B 2 121 ? 125.576 142.297 221.801 1.00 142.36 ? 121 VAL B CB    1 
ATOM   5069  C  CG1   . VAL B 2 121 ? 126.468 142.153 220.576 1.00 141.01 ? 121 VAL B CG1   1 
ATOM   5070  C  CG2   . VAL B 2 121 ? 124.857 140.987 222.093 1.00 140.57 ? 121 VAL B CG2   1 
ATOM   5071  N  N     . PRO B 2 122 ? 128.703 143.509 222.597 1.00 139.73 ? 122 PRO B N     1 
ATOM   5072  C  CA    . PRO B 2 122 ? 129.692 144.514 222.194 1.00 138.83 ? 122 PRO B CA    1 
ATOM   5073  C  C     . PRO B 2 122 ? 129.511 144.923 220.740 1.00 138.46 ? 122 PRO B C     1 
ATOM   5074  O  O     . PRO B 2 122 ? 128.976 144.181 219.912 1.00 139.28 ? 122 PRO B O     1 
ATOM   5075  C  CB    . PRO B 2 122 ? 131.035 143.808 222.413 1.00 137.11 ? 122 PRO B CB    1 
ATOM   5076  C  CG    . PRO B 2 122 ? 130.731 142.676 223.349 1.00 135.79 ? 122 PRO B CG    1 
ATOM   5077  C  CD    . PRO B 2 122 ? 129.335 142.249 223.017 1.00 137.46 ? 122 PRO B CD    1 
ATOM   5078  N  N     . ALA B 2 123 ? 129.972 146.140 220.441 1.00 127.50 ? 123 ALA B N     1 
ATOM   5079  C  CA    . ALA B 2 123 ? 129.710 146.741 219.136 1.00 127.43 ? 123 ALA B CA    1 
ATOM   5080  C  C     . ALA B 2 123 ? 130.349 145.944 218.004 1.00 128.70 ? 123 ALA B C     1 
ATOM   5081  O  O     . ALA B 2 123 ? 129.781 145.847 216.910 1.00 130.66 ? 123 ALA B O     1 
ATOM   5082  C  CB    . ALA B 2 123 ? 130.206 148.186 219.117 1.00 126.30 ? 123 ALA B CB    1 
ATOM   5083  N  N     . ASP B 2 124 ? 131.533 145.375 218.241 1.00 130.30 ? 124 ASP B N     1 
ATOM   5084  C  CA    . ASP B 2 124 ? 132.259 144.704 217.168 1.00 130.62 ? 124 ASP B CA    1 
ATOM   5085  C  C     . ASP B 2 124 ? 131.518 143.486 216.628 1.00 131.58 ? 124 ASP B C     1 
ATOM   5086  O  O     . ASP B 2 124 ? 131.733 143.110 215.470 1.00 130.16 ? 124 ASP B O     1 
ATOM   5087  C  CB    . ASP B 2 124 ? 133.656 144.302 217.646 1.00 132.30 ? 124 ASP B CB    1 
ATOM   5088  C  CG    . ASP B 2 124 ? 133.623 143.415 218.873 1.00 136.73 ? 124 ASP B CG    1 
ATOM   5089  O  OD1   . ASP B 2 124 ? 133.298 142.218 218.734 1.00 140.47 ? 124 ASP B OD1   1 
ATOM   5090  O  OD2   . ASP B 2 124 ? 133.921 143.915 219.978 1.00 136.73 ? 124 ASP B OD2   1 
ATOM   5091  N  N     . GLN B 2 125 ? 130.654 142.860 217.430 1.00 129.87 ? 125 GLN B N     1 
ATOM   5092  C  CA    . GLN B 2 125 ? 129.884 141.720 216.947 1.00 129.72 ? 125 GLN B CA    1 
ATOM   5093  C  C     . GLN B 2 125 ? 128.737 142.124 216.031 1.00 130.88 ? 125 GLN B C     1 
ATOM   5094  O  O     . GLN B 2 125 ? 128.175 141.258 215.350 1.00 131.03 ? 125 GLN B O     1 
ATOM   5095  C  CB    . GLN B 2 125 ? 129.329 140.907 218.119 1.00 130.52 ? 125 GLN B CB    1 
ATOM   5096  C  CG    . GLN B 2 125 ? 130.317 139.926 218.727 1.00 130.17 ? 125 GLN B CG    1 
ATOM   5097  C  CD    . GLN B 2 125 ? 130.773 140.340 220.108 1.00 130.43 ? 125 GLN B CD    1 
ATOM   5098  O  OE1   . GLN B 2 125 ? 131.154 141.487 220.328 1.00 130.87 ? 125 GLN B OE1   1 
ATOM   5099  N  NE2   . GLN B 2 125 ? 130.734 139.405 221.050 1.00 129.78 ? 125 GLN B NE2   1 
ATOM   5100  N  N     . LEU B 2 126 ? 128.374 143.404 216.001 1.00 118.90 ? 126 LEU B N     1 
ATOM   5101  C  CA    . LEU B 2 126 ? 127.261 143.847 215.173 1.00 116.90 ? 126 LEU B CA    1 
ATOM   5102  C  C     . LEU B 2 126 ? 127.599 143.690 213.696 1.00 114.48 ? 126 LEU B C     1 
ATOM   5103  O  O     . LEU B 2 126 ? 128.697 144.045 213.256 1.00 115.69 ? 126 LEU B O     1 
ATOM   5104  C  CB    . LEU B 2 126 ? 126.916 145.302 215.482 1.00 118.11 ? 126 LEU B CB    1 
ATOM   5105  C  CG    . LEU B 2 126 ? 126.317 145.584 216.860 1.00 116.60 ? 126 LEU B CG    1 
ATOM   5106  C  CD1   . LEU B 2 126 ? 125.957 147.054 216.988 1.00 115.98 ? 126 LEU B CD1   1 
ATOM   5107  C  CD2   . LEU B 2 126 ? 125.100 144.708 217.104 1.00 118.75 ? 126 LEU B CD2   1 
ATOM   5108  N  N     . ARG B 2 127 ? 126.648 143.158 212.930 1.00 112.24 ? 127 ARG B N     1 
ATOM   5109  C  CA    . ARG B 2 127 ? 126.826 142.986 211.494 1.00 115.79 ? 127 ARG B CA    1 
ATOM   5110  C  C     . ARG B 2 127 ? 125.633 143.558 210.741 1.00 118.16 ? 127 ARG B C     1 
ATOM   5111  O  O     . ARG B 2 127 ? 124.773 144.213 211.338 1.00 117.54 ? 127 ARG B O     1 
ATOM   5112  C  CB    . ARG B 2 127 ? 127.021 141.508 211.148 1.00 116.52 ? 127 ARG B CB    1 
ATOM   5113  C  CG    . ARG B 2 127 ? 128.456 141.134 210.818 1.00 116.44 ? 127 ARG B CG    1 
ATOM   5114  C  CD    . ARG B 2 127 ? 129.299 141.023 212.077 1.00 118.37 ? 127 ARG B CD    1 
ATOM   5115  N  NE    . ARG B 2 127 ? 130.726 140.997 211.777 1.00 120.12 ? 127 ARG B NE    1 
ATOM   5116  C  CZ    . ARG B 2 127 ? 131.683 140.992 212.695 1.00 120.61 ? 127 ARG B CZ    1 
ATOM   5117  N  NH1   . ARG B 2 127 ? 131.402 141.014 213.987 1.00 119.63 ? 127 ARG B NH1   1 
ATOM   5118  N  NH2   . ARG B 2 127 ? 132.955 140.966 212.305 1.00 120.02 ? 127 ARG B NH2   1 
ATOM   5119  N  N     . LYS B 2 128 ? 125.575 143.318 209.434 1.00 112.34 ? 128 LYS B N     1 
ATOM   5120  C  CA    . LYS B 2 128 ? 124.480 143.838 208.627 1.00 110.76 ? 128 LYS B CA    1 
ATOM   5121  C  C     . LYS B 2 128 ? 123.158 143.204 209.040 1.00 114.59 ? 128 LYS B C     1 
ATOM   5122  O  O     . LYS B 2 128 ? 123.075 141.997 209.282 1.00 114.50 ? 128 LYS B O     1 
ATOM   5123  C  CB    . LYS B 2 128 ? 124.749 143.577 207.145 1.00 108.26 ? 128 LYS B CB    1 
ATOM   5124  C  CG    . LYS B 2 128 ? 123.899 144.411 206.202 1.00 109.83 ? 128 LYS B CG    1 
ATOM   5125  C  CD    . LYS B 2 128 ? 124.386 144.297 204.765 1.00 112.82 ? 128 LYS B CD    1 
ATOM   5126  C  CE    . LYS B 2 128 ? 125.899 144.421 204.678 1.00 114.96 ? 128 LYS B CE    1 
ATOM   5127  N  NZ    . LYS B 2 128 ? 126.368 144.512 203.269 1.00 116.55 ? 128 LYS B NZ    1 
ATOM   5128  N  N     . GLY B 2 129 ? 122.117 144.030 209.120 1.00 121.21 ? 129 GLY B N     1 
ATOM   5129  C  CA    . GLY B 2 129 ? 120.787 143.563 209.444 1.00 119.12 ? 129 GLY B CA    1 
ATOM   5130  C  C     . GLY B 2 129 ? 120.483 143.420 210.919 1.00 118.14 ? 129 GLY B C     1 
ATOM   5131  O  O     . GLY B 2 129 ? 119.400 142.931 211.264 1.00 121.49 ? 129 GLY B O     1 
ATOM   5132  N  N     . ASP B 2 130 ? 121.391 143.829 211.800 1.00 111.15 ? 130 ASP B N     1 
ATOM   5133  C  CA    . ASP B 2 130 ? 121.179 143.717 213.238 1.00 113.78 ? 130 ASP B CA    1 
ATOM   5134  C  C     . ASP B 2 130 ? 120.525 144.993 213.754 1.00 111.19 ? 130 ASP B C     1 
ATOM   5135  O  O     . ASP B 2 130 ? 121.035 146.095 213.527 1.00 114.03 ? 130 ASP B O     1 
ATOM   5136  C  CB    . ASP B 2 130 ? 122.499 143.458 213.963 1.00 116.54 ? 130 ASP B CB    1 
ATOM   5137  C  CG    . ASP B 2 130 ? 123.257 142.279 213.388 1.00 119.51 ? 130 ASP B CG    1 
ATOM   5138  O  OD1   . ASP B 2 130 ? 122.624 141.428 212.728 1.00 118.90 ? 130 ASP B OD1   1 
ATOM   5139  O  OD2   . ASP B 2 130 ? 124.485 142.201 213.600 1.00 119.79 ? 130 ASP B OD2   1 
ATOM   5140  N  N     . ILE B 2 131 ? 119.401 144.841 214.446 1.00 100.03 ? 131 ILE B N     1 
ATOM   5141  C  CA    . ILE B 2 131 ? 118.686 145.983 215.006 1.00 99.23  ? 131 ILE B CA    1 
ATOM   5142  C  C     . ILE B 2 131 ? 119.254 146.285 216.386 1.00 102.64 ? 131 ILE B C     1 
ATOM   5143  O  O     . ILE B 2 131 ? 119.335 145.400 217.246 1.00 110.54 ? 131 ILE B O     1 
ATOM   5144  C  CB    . ILE B 2 131 ? 117.174 145.706 215.073 1.00 104.22 ? 131 ILE B CB    1 
ATOM   5145  C  CG1   . ILE B 2 131 ? 116.491 146.019 213.737 1.00 109.01 ? 131 ILE B CG1   1 
ATOM   5146  C  CG2   . ILE B 2 131 ? 116.527 146.519 216.184 1.00 106.60 ? 131 ILE B CG2   1 
ATOM   5147  C  CD1   . ILE B 2 131 ? 116.883 145.109 212.590 1.00 108.00 ? 131 ILE B CD1   1 
ATOM   5148  N  N     . VAL B 2 132 ? 119.658 147.535 216.599 1.00 89.37  ? 132 VAL B N     1 
ATOM   5149  C  CA    . VAL B 2 132 ? 120.234 147.970 217.865 1.00 90.26  ? 132 VAL B CA    1 
ATOM   5150  C  C     . VAL B 2 132 ? 119.439 149.162 218.378 1.00 87.13  ? 132 VAL B C     1 
ATOM   5151  O  O     . VAL B 2 132 ? 119.207 150.126 217.639 1.00 92.24  ? 132 VAL B O     1 
ATOM   5152  C  CB    . VAL B 2 132 ? 121.728 148.325 217.726 1.00 88.83  ? 132 VAL B CB    1 
ATOM   5153  C  CG1   . VAL B 2 132 ? 121.974 149.140 216.466 1.00 88.45  ? 132 VAL B CG1   1 
ATOM   5154  C  CG2   . VAL B 2 132 ? 122.214 149.076 218.955 1.00 90.76  ? 132 VAL B CG2   1 
ATOM   5155  N  N     . LEU B 2 133 ? 119.017 149.092 219.635 1.00 91.34  ? 133 LEU B N     1 
ATOM   5156  C  CA    . LEU B 2 133 ? 118.304 150.175 220.291 1.00 88.75  ? 133 LEU B CA    1 
ATOM   5157  C  C     . LEU B 2 133 ? 119.279 151.042 221.076 1.00 89.97  ? 133 LEU B C     1 
ATOM   5158  O  O     . LEU B 2 133 ? 120.186 150.540 221.743 1.00 98.56  ? 133 LEU B O     1 
ATOM   5159  C  CB    . LEU B 2 133 ? 117.223 149.628 221.225 1.00 92.42  ? 133 LEU B CB    1 
ATOM   5160  C  CG    . LEU B 2 133 ? 116.429 150.653 222.036 1.00 94.22  ? 133 LEU B CG    1 
ATOM   5161  C  CD1   . LEU B 2 133 ? 115.692 151.612 221.118 1.00 97.44  ? 133 LEU B CD1   1 
ATOM   5162  C  CD2   . LEU B 2 133 ? 115.460 149.955 222.978 1.00 95.43  ? 133 LEU B CD2   1 
ATOM   5163  N  N     . VAL B 2 134 ? 119.085 152.356 220.986 1.00 85.63  ? 134 VAL B N     1 
ATOM   5164  C  CA    . VAL B 2 134 ? 119.947 153.315 221.663 1.00 86.80  ? 134 VAL B CA    1 
ATOM   5165  C  C     . VAL B 2 134 ? 119.080 154.322 222.407 1.00 92.39  ? 134 VAL B C     1 
ATOM   5166  O  O     . VAL B 2 134 ? 117.927 154.571 222.040 1.00 96.67  ? 134 VAL B O     1 
ATOM   5167  C  CB    . VAL B 2 134 ? 120.903 154.018 220.671 1.00 84.61  ? 134 VAL B CB    1 
ATOM   5168  C  CG1   . VAL B 2 134 ? 120.206 155.168 219.967 1.00 85.64  ? 134 VAL B CG1   1 
ATOM   5169  C  CG2   . VAL B 2 134 ? 122.156 154.499 221.385 1.00 90.61  ? 134 VAL B CG2   1 
ATOM   5170  N  N     . GLU B 2 135 ? 119.641 154.890 223.471 1.00 99.13  ? 135 GLU B N     1 
ATOM   5171  C  CA    . GLU B 2 135 ? 118.963 155.876 224.296 1.00 98.98  ? 135 GLU B CA    1 
ATOM   5172  C  C     . GLU B 2 135 ? 119.760 157.173 224.304 1.00 94.92  ? 135 GLU B C     1 
ATOM   5173  O  O     . GLU B 2 135 ? 120.922 157.214 223.892 1.00 97.03  ? 135 GLU B O     1 
ATOM   5174  C  CB    . GLU B 2 135 ? 118.773 155.371 225.732 1.00 103.57 ? 135 GLU B CB    1 
ATOM   5175  C  CG    . GLU B 2 135 ? 118.043 154.044 225.838 1.00 103.47 ? 135 GLU B CG    1 
ATOM   5176  C  CD    . GLU B 2 135 ? 116.780 154.004 225.003 1.00 103.95 ? 135 GLU B CD    1 
ATOM   5177  O  OE1   . GLU B 2 135 ? 115.910 154.880 225.195 1.00 104.82 ? 135 GLU B OE1   1 
ATOM   5178  O  OE2   . GLU B 2 135 ? 116.655 153.096 224.156 1.00 101.08 ? 135 GLU B OE2   1 
ATOM   5179  N  N     . ALA B 2 136 ? 119.118 158.235 224.787 1.00 95.07  ? 136 ALA B N     1 
ATOM   5180  C  CA    . ALA B 2 136 ? 119.742 159.551 224.792 1.00 100.06 ? 136 ALA B CA    1 
ATOM   5181  C  C     . ALA B 2 136 ? 121.014 159.548 225.631 1.00 100.42 ? 136 ALA B C     1 
ATOM   5182  O  O     . ALA B 2 136 ? 121.078 158.924 226.694 1.00 101.61 ? 136 ALA B O     1 
ATOM   5183  C  CB    . ALA B 2 136 ? 118.764 160.598 225.325 1.00 97.20  ? 136 ALA B CB    1 
ATOM   5184  N  N     . GLY B 2 137 ? 122.034 160.251 225.141 1.00 98.43  ? 137 GLY B N     1 
ATOM   5185  C  CA    . GLY B 2 137 ? 123.308 160.340 225.817 1.00 93.50  ? 137 GLY B CA    1 
ATOM   5186  C  C     . GLY B 2 137 ? 124.312 159.272 225.444 1.00 96.80  ? 137 GLY B C     1 
ATOM   5187  O  O     . GLY B 2 137 ? 125.467 159.352 225.883 1.00 101.33 ? 137 GLY B O     1 
ATOM   5188  N  N     . ASP B 2 138 ? 123.918 158.280 224.651 1.00 102.73 ? 138 ASP B N     1 
ATOM   5189  C  CA    . ASP B 2 138 ? 124.812 157.199 224.271 1.00 102.76 ? 138 ASP B CA    1 
ATOM   5190  C  C     . ASP B 2 138 ? 125.505 157.521 222.948 1.00 104.96 ? 138 ASP B C     1 
ATOM   5191  O  O     . ASP B 2 138 ? 125.334 158.595 222.367 1.00 105.51 ? 138 ASP B O     1 
ATOM   5192  C  CB    . ASP B 2 138 ? 124.045 155.881 224.184 1.00 102.11 ? 138 ASP B CB    1 
ATOM   5193  C  CG    . ASP B 2 138 ? 123.245 155.589 225.437 1.00 110.36 ? 138 ASP B CG    1 
ATOM   5194  O  OD1   . ASP B 2 138 ? 123.125 156.492 226.292 1.00 114.06 ? 138 ASP B OD1   1 
ATOM   5195  O  OD2   . ASP B 2 138 ? 122.738 154.455 225.569 1.00 111.64 ? 138 ASP B OD2   1 
ATOM   5196  N  N     . ILE B 2 139 ? 126.306 156.573 222.467 1.00 100.84 ? 139 ILE B N     1 
ATOM   5197  C  CA    . ILE B 2 139 ? 127.043 156.706 221.216 1.00 98.59  ? 139 ILE B CA    1 
ATOM   5198  C  C     . ILE B 2 139 ? 126.510 155.662 220.245 1.00 96.90  ? 139 ILE B C     1 
ATOM   5199  O  O     . ILE B 2 139 ? 126.307 154.502 220.623 1.00 95.74  ? 139 ILE B O     1 
ATOM   5200  C  CB    . ILE B 2 139 ? 128.561 156.545 221.431 1.00 97.92  ? 139 ILE B CB    1 
ATOM   5201  C  CG1   . ILE B 2 139 ? 129.237 157.906 221.623 1.00 95.07  ? 139 ILE B CG1   1 
ATOM   5202  C  CG2   . ILE B 2 139 ? 129.208 155.814 220.263 1.00 96.84  ? 139 ILE B CG2   1 
ATOM   5203  C  CD1   . ILE B 2 139 ? 128.713 158.713 222.788 1.00 94.03  ? 139 ILE B CD1   1 
ATOM   5204  N  N     . ILE B 2 140 ? 126.264 156.078 219.005 1.00 83.79  ? 140 ILE B N     1 
ATOM   5205  C  CA    . ILE B 2 140 ? 125.766 155.135 217.997 1.00 79.50  ? 140 ILE B CA    1 
ATOM   5206  C  C     . ILE B 2 140 ? 126.821 154.063 217.750 1.00 82.39  ? 140 ILE B C     1 
ATOM   5207  O  O     . ILE B 2 140 ? 127.986 154.395 217.456 1.00 86.49  ? 140 ILE B O     1 
ATOM   5208  C  CB    . ILE B 2 140 ? 125.417 155.873 216.694 1.00 82.35  ? 140 ILE B CB    1 
ATOM   5209  C  CG1   . ILE B 2 140 ? 124.558 157.102 216.992 1.00 79.75  ? 140 ILE B CG1   1 
ATOM   5210  C  CG2   . ILE B 2 140 ? 124.700 154.941 215.732 1.00 86.49  ? 140 ILE B CG2   1 
ATOM   5211  C  CD1   . ILE B 2 140 ? 123.205 156.775 217.579 1.00 83.75  ? 140 ILE B CD1   1 
ATOM   5212  N  N     . PRO B 2 141 ? 126.483 152.779 217.859 1.00 81.35  ? 141 PRO B N     1 
ATOM   5213  C  CA    . PRO B 2 141 ? 127.501 151.730 217.704 1.00 85.09  ? 141 PRO B CA    1 
ATOM   5214  C  C     . PRO B 2 141 ? 128.017 151.587 216.281 1.00 89.22  ? 141 PRO B C     1 
ATOM   5215  O  O     . PRO B 2 141 ? 129.229 151.502 216.064 1.00 89.27  ? 141 PRO B O     1 
ATOM   5216  C  CB    . PRO B 2 141 ? 126.767 150.464 218.161 1.00 88.83  ? 141 PRO B CB    1 
ATOM   5217  C  CG    . PRO B 2 141 ? 125.325 150.763 217.937 1.00 88.30  ? 141 PRO B CG    1 
ATOM   5218  C  CD    . PRO B 2 141 ? 125.165 152.227 218.213 1.00 82.05  ? 141 PRO B CD    1 
ATOM   5219  N  N     . CYS B 2 142 ? 127.114 151.561 215.303 1.00 90.71  ? 142 CYS B N     1 
ATOM   5220  C  CA    . CYS B 2 142 ? 127.505 151.309 213.925 1.00 91.09  ? 142 CYS B CA    1 
ATOM   5221  C  C     . CYS B 2 142 ? 126.628 152.124 212.988 1.00 91.37  ? 142 CYS B C     1 
ATOM   5222  O  O     . CYS B 2 142 ? 125.540 152.575 213.354 1.00 95.62  ? 142 CYS B O     1 
ATOM   5223  C  CB    . CYS B 2 142 ? 127.410 149.819 213.577 1.00 95.45  ? 142 CYS B CB    1 
ATOM   5224  S  SG    . CYS B 2 142 ? 125.719 149.181 213.482 1.00 112.89 ? 142 CYS B SG    1 
ATOM   5225  N  N     . ASP B 2 143 ? 127.123 152.309 211.767 1.00 84.46  ? 143 ASP B N     1 
ATOM   5226  C  CA    . ASP B 2 143 ? 126.358 153.000 210.741 1.00 90.41  ? 143 ASP B CA    1 
ATOM   5227  C  C     . ASP B 2 143 ? 125.139 152.178 210.346 1.00 94.06  ? 143 ASP B C     1 
ATOM   5228  O  O     . ASP B 2 143 ? 125.188 150.946 210.300 1.00 98.69  ? 143 ASP B O     1 
ATOM   5229  C  CB    . ASP B 2 143 ? 127.228 153.263 209.513 1.00 91.12  ? 143 ASP B CB    1 
ATOM   5230  C  CG    . ASP B 2 143 ? 128.510 153.990 209.853 1.00 92.84  ? 143 ASP B CG    1 
ATOM   5231  O  OD1   . ASP B 2 143 ? 128.733 154.280 211.047 1.00 93.09  ? 143 ASP B OD1   1 
ATOM   5232  O  OD2   . ASP B 2 143 ? 129.296 154.269 208.926 1.00 95.84  ? 143 ASP B OD2   1 
ATOM   5233  N  N     . GLY B 2 144 ? 124.043 152.866 210.057 1.00 87.38  ? 144 GLY B N     1 
ATOM   5234  C  CA    . GLY B 2 144 ? 122.830 152.180 209.655 1.00 86.89  ? 144 GLY B CA    1 
ATOM   5235  C  C     . GLY B 2 144 ? 121.733 153.174 209.355 1.00 89.96  ? 144 GLY B C     1 
ATOM   5236  O  O     . GLY B 2 144 ? 121.919 154.392 209.442 1.00 93.11  ? 144 GLY B O     1 
ATOM   5237  N  N     . GLU B 2 145 ? 120.576 152.629 208.997 1.00 91.46  ? 145 GLU B N     1 
ATOM   5238  C  CA    . GLU B 2 145 ? 119.394 153.421 208.689 1.00 87.33  ? 145 GLU B CA    1 
ATOM   5239  C  C     . GLU B 2 145 ? 118.412 153.328 209.847 1.00 83.54  ? 145 GLU B C     1 
ATOM   5240  O  O     . GLU B 2 145 ? 118.088 152.227 210.304 1.00 89.44  ? 145 GLU B O     1 
ATOM   5241  C  CB    . GLU B 2 145 ? 118.735 152.939 207.396 1.00 86.05  ? 145 GLU B CB    1 
ATOM   5242  C  CG    . GLU B 2 145 ? 119.712 152.664 206.265 1.00 93.95  ? 145 GLU B CG    1 
ATOM   5243  C  CD    . GLU B 2 145 ? 120.070 153.914 205.486 1.00 100.89 ? 145 GLU B CD    1 
ATOM   5244  O  OE1   . GLU B 2 145 ? 119.502 154.986 205.783 1.00 102.32 ? 145 GLU B OE1   1 
ATOM   5245  O  OE2   . GLU B 2 145 ? 120.919 153.825 204.575 1.00 102.75 ? 145 GLU B OE2   1 
ATOM   5246  N  N     . VAL B 2 146 ? 117.947 154.483 210.322 1.00 67.37  ? 146 VAL B N     1 
ATOM   5247  C  CA    . VAL B 2 146 ? 116.978 154.505 211.410 1.00 65.40  ? 146 VAL B CA    1 
ATOM   5248  C  C     . VAL B 2 146 ? 115.678 153.875 210.932 1.00 75.38  ? 146 VAL B C     1 
ATOM   5249  O  O     . VAL B 2 146 ? 115.100 154.293 209.920 1.00 88.17  ? 146 VAL B O     1 
ATOM   5250  C  CB    . VAL B 2 146 ? 116.755 155.940 211.905 1.00 68.61  ? 146 VAL B CB    1 
ATOM   5251  C  CG1   . VAL B 2 146 ? 115.591 155.989 212.881 1.00 71.80  ? 146 VAL B CG1   1 
ATOM   5252  C  CG2   . VAL B 2 146 ? 118.020 156.480 212.549 1.00 73.00  ? 146 VAL B CG2   1 
ATOM   5253  N  N     . ILE B 2 147 ? 115.214 152.858 211.656 1.00 77.52  ? 147 ILE B N     1 
ATOM   5254  C  CA    . ILE B 2 147 ? 114.005 152.142 211.269 1.00 76.03  ? 147 ILE B CA    1 
ATOM   5255  C  C     . ILE B 2 147 ? 112.774 152.601 212.044 1.00 75.72  ? 147 ILE B C     1 
ATOM   5256  O  O     . ILE B 2 147 ? 111.646 152.336 211.600 1.00 84.43  ? 147 ILE B O     1 
ATOM   5257  C  CB    . ILE B 2 147 ? 114.201 150.618 211.422 1.00 76.45  ? 147 ILE B CB    1 
ATOM   5258  C  CG1   . ILE B 2 147 ? 113.537 149.874 210.263 1.00 77.17  ? 147 ILE B CG1   1 
ATOM   5259  C  CG2   . ILE B 2 147 ? 113.665 150.128 212.759 1.00 80.35  ? 147 ILE B CG2   1 
ATOM   5260  C  CD1   . ILE B 2 147 ? 114.324 149.932 208.974 1.00 78.51  ? 147 ILE B CD1   1 
ATOM   5261  N  N     . GLU B 2 148 ? 112.952 153.289 213.170 1.00 85.30  ? 148 GLU B N     1 
ATOM   5262  C  CA    . GLU B 2 148 ? 111.827 153.755 213.968 1.00 94.51  ? 148 GLU B CA    1 
ATOM   5263  C  C     . GLU B 2 148 ? 112.319 154.813 214.943 1.00 90.78  ? 148 GLU B C     1 
ATOM   5264  O  O     . GLU B 2 148 ? 113.442 154.726 215.446 1.00 95.18  ? 148 GLU B O     1 
ATOM   5265  C  CB    . GLU B 2 148 ? 111.166 152.598 214.726 1.00 99.76  ? 148 GLU B CB    1 
ATOM   5266  C  CG    . GLU B 2 148 ? 109.829 152.947 215.351 1.00 102.75 ? 148 GLU B CG    1 
ATOM   5267  C  CD    . GLU B 2 148 ? 109.111 151.730 215.894 1.00 106.39 ? 148 GLU B CD    1 
ATOM   5268  O  OE1   . GLU B 2 148 ? 108.895 150.775 215.119 1.00 106.00 ? 148 GLU B OE1   1 
ATOM   5269  O  OE2   . GLU B 2 148 ? 108.764 151.728 217.094 1.00 108.36 ? 148 GLU B OE2   1 
ATOM   5270  N  N     . GLY B 2 149 ? 111.474 155.806 215.202 1.00 78.34  ? 149 GLY B N     1 
ATOM   5271  C  CA    . GLY B 2 149 ? 111.787 156.853 216.150 1.00 72.18  ? 149 GLY B CA    1 
ATOM   5272  C  C     . GLY B 2 149 ? 112.535 158.015 215.523 1.00 77.36  ? 149 GLY B C     1 
ATOM   5273  O  O     . GLY B 2 149 ? 113.026 157.958 214.393 1.00 83.11  ? 149 GLY B O     1 
ATOM   5274  N  N     . GLY B 2 150 ? 112.614 159.100 216.288 1.00 76.14  ? 150 GLY B N     1 
ATOM   5275  C  CA    . GLY B 2 150 ? 113.318 160.290 215.853 1.00 80.19  ? 150 GLY B CA    1 
ATOM   5276  C  C     . GLY B 2 150 ? 113.876 161.086 217.013 1.00 80.29  ? 150 GLY B C     1 
ATOM   5277  O  O     . GLY B 2 150 ? 113.169 161.346 217.990 1.00 83.76  ? 150 GLY B O     1 
ATOM   5278  N  N     . ALA B 2 151 ? 115.142 161.484 216.918 1.00 87.86  ? 151 ALA B N     1 
ATOM   5279  C  CA    . ALA B 2 151 ? 115.798 162.195 218.006 1.00 90.61  ? 151 ALA B CA    1 
ATOM   5280  C  C     . ALA B 2 151 ? 116.955 163.004 217.441 1.00 88.32  ? 151 ALA B C     1 
ATOM   5281  O  O     . ALA B 2 151 ? 117.416 162.772 216.321 1.00 91.13  ? 151 ALA B O     1 
ATOM   5282  C  CB    . ALA B 2 151 ? 116.286 161.228 219.090 1.00 93.46  ? 151 ALA B CB    1 
ATOM   5283  N  N     . SER B 2 152 ? 117.418 163.965 218.236 1.00 87.81  ? 152 SER B N     1 
ATOM   5284  C  CA    . SER B 2 152 ? 118.559 164.784 217.856 1.00 87.55  ? 152 SER B CA    1 
ATOM   5285  C  C     . SER B 2 152 ? 119.851 163.994 218.010 1.00 88.55  ? 152 SER B C     1 
ATOM   5286  O  O     . SER B 2 152 ? 119.995 163.181 218.928 1.00 96.97  ? 152 SER B O     1 
ATOM   5287  C  CB    . SER B 2 152 ? 118.615 166.051 218.708 1.00 88.31  ? 152 SER B CB    1 
ATOM   5288  O  OG    . SER B 2 152 ? 117.426 166.809 218.572 1.00 93.12  ? 152 SER B OG    1 
ATOM   5289  N  N     . VAL B 2 153 ? 120.792 164.232 217.099 1.00 74.18  ? 153 VAL B N     1 
ATOM   5290  C  CA    . VAL B 2 153 ? 122.074 163.541 217.088 1.00 71.88  ? 153 VAL B CA    1 
ATOM   5291  C  C     . VAL B 2 153 ? 123.188 164.574 217.005 1.00 75.97  ? 153 VAL B C     1 
ATOM   5292  O  O     . VAL B 2 153 ? 123.130 165.498 216.186 1.00 82.06  ? 153 VAL B O     1 
ATOM   5293  C  CB    . VAL B 2 153 ? 122.169 162.539 215.918 1.00 72.13  ? 153 VAL B CB    1 
ATOM   5294  C  CG1   . VAL B 2 153 ? 123.594 162.038 215.754 1.00 77.01  ? 153 VAL B CG1   1 
ATOM   5295  C  CG2   . VAL B 2 153 ? 121.218 161.375 216.141 1.00 76.63  ? 153 VAL B CG2   1 
ATOM   5296  N  N     . ASP B 2 154 ? 124.197 164.421 217.858 1.00 86.97  ? 154 ASP B N     1 
ATOM   5297  C  CA    . ASP B 2 154 ? 125.378 165.274 217.853 1.00 89.35  ? 154 ASP B CA    1 
ATOM   5298  C  C     . ASP B 2 154 ? 126.473 164.571 217.062 1.00 91.72  ? 154 ASP B C     1 
ATOM   5299  O  O     . ASP B 2 154 ? 126.894 163.467 217.425 1.00 92.68  ? 154 ASP B O     1 
ATOM   5300  C  CB    . ASP B 2 154 ? 125.846 165.573 219.277 1.00 95.22  ? 154 ASP B CB    1 
ATOM   5301  C  CG    . ASP B 2 154 ? 127.012 166.544 219.321 1.00 97.15  ? 154 ASP B CG    1 
ATOM   5302  O  OD1   . ASP B 2 154 ? 127.355 167.121 218.268 1.00 98.15  ? 154 ASP B OD1   1 
ATOM   5303  O  OD2   . ASP B 2 154 ? 127.589 166.728 220.413 1.00 95.32  ? 154 ASP B OD2   1 
ATOM   5304  N  N     . GLU B 2 155 ? 126.930 165.210 215.986 1.00 87.87  ? 155 GLU B N     1 
ATOM   5305  C  CA    . GLU B 2 155 ? 127.937 164.641 215.100 1.00 83.40  ? 155 GLU B CA    1 
ATOM   5306  C  C     . GLU B 2 155 ? 129.264 165.389 215.185 1.00 86.37  ? 155 GLU B C     1 
ATOM   5307  O  O     . GLU B 2 155 ? 130.029 165.420 214.218 1.00 93.82  ? 155 GLU B O     1 
ATOM   5308  C  CB    . GLU B 2 155 ? 127.427 164.621 213.660 1.00 85.83  ? 155 GLU B CB    1 
ATOM   5309  C  CG    . GLU B 2 155 ? 126.002 164.114 213.518 1.00 93.25  ? 155 GLU B CG    1 
ATOM   5310  C  CD    . GLU B 2 155 ? 125.737 163.490 212.162 1.00 98.61  ? 155 GLU B CD    1 
ATOM   5311  O  OE1   . GLU B 2 155 ? 125.894 164.193 211.142 1.00 96.76  ? 155 GLU B OE1   1 
ATOM   5312  O  OE2   . GLU B 2 155 ? 125.370 162.298 212.117 1.00 100.01 ? 155 GLU B OE2   1 
ATOM   5313  N  N     . SER B 2 156 ? 129.548 165.999 216.338 1.00 84.43  ? 156 SER B N     1 
ATOM   5314  C  CA    . SER B 2 156 ? 130.799 166.728 216.510 1.00 84.09  ? 156 SER B CA    1 
ATOM   5315  C  C     . SER B 2 156 ? 132.017 165.817 216.460 1.00 88.18  ? 156 SER B C     1 
ATOM   5316  O  O     . SER B 2 156 ? 133.126 166.301 216.215 1.00 88.68  ? 156 SER B O     1 
ATOM   5317  C  CB    . SER B 2 156 ? 130.780 167.498 217.830 1.00 86.40  ? 156 SER B CB    1 
ATOM   5318  O  OG    . SER B 2 156 ? 130.444 166.646 218.911 1.00 90.59  ? 156 SER B OG    1 
ATOM   5319  N  N     . ALA B 2 157 ? 131.839 164.515 216.695 1.00 80.10  ? 157 ALA B N     1 
ATOM   5320  C  CA    . ALA B 2 157 ? 132.964 163.591 216.623 1.00 75.60  ? 157 ALA B CA    1 
ATOM   5321  C  C     . ALA B 2 157 ? 133.513 163.495 215.205 1.00 70.77  ? 157 ALA B C     1 
ATOM   5322  O  O     . ALA B 2 157 ? 134.731 163.415 215.009 1.00 75.12  ? 157 ALA B O     1 
ATOM   5323  C  CB    . ALA B 2 157 ? 132.546 162.212 217.132 1.00 73.93  ? 157 ALA B CB    1 
ATOM   5324  N  N     . ILE B 2 158 ? 132.635 163.500 214.208 1.00 62.80  ? 158 ILE B N     1 
ATOM   5325  C  CA    . ILE B 2 158 ? 133.031 163.354 212.812 1.00 65.28  ? 158 ILE B CA    1 
ATOM   5326  C  C     . ILE B 2 158 ? 133.088 164.698 212.099 1.00 58.99  ? 158 ILE B C     1 
ATOM   5327  O  O     . ILE B 2 158 ? 134.120 165.068 211.539 1.00 62.57  ? 158 ILE B O     1 
ATOM   5328  C  CB    . ILE B 2 158 ? 132.076 162.378 212.089 1.00 63.09  ? 158 ILE B CB    1 
ATOM   5329  C  CG1   . ILE B 2 158 ? 132.212 160.972 212.672 1.00 64.77  ? 158 ILE B CG1   1 
ATOM   5330  C  CG2   . ILE B 2 158 ? 132.352 162.371 210.595 1.00 59.61  ? 158 ILE B CG2   1 
ATOM   5331  C  CD1   . ILE B 2 158 ? 131.270 159.965 212.056 1.00 65.26  ? 158 ILE B CD1   1 
ATOM   5332  N  N     . THR B 2 159 ? 131.983 165.446 212.111 1.00 62.06  ? 159 THR B N     1 
ATOM   5333  C  CA    . THR B 2 159 ? 131.936 166.704 211.373 1.00 61.39  ? 159 THR B CA    1 
ATOM   5334  C  C     . THR B 2 159 ? 132.751 167.795 212.054 1.00 66.29  ? 159 THR B C     1 
ATOM   5335  O  O     . THR B 2 159 ? 133.166 168.755 211.396 1.00 73.80  ? 159 THR B O     1 
ATOM   5336  C  CB    . THR B 2 159 ? 130.488 167.161 211.202 1.00 69.59  ? 159 THR B CB    1 
ATOM   5337  O  OG1   . THR B 2 159 ? 130.033 167.774 212.414 1.00 81.47  ? 159 THR B OG1   1 
ATOM   5338  C  CG2   . THR B 2 159 ? 129.594 165.977 210.872 1.00 75.46  ? 159 THR B CG2   1 
ATOM   5339  N  N     . GLY B 2 160 ? 132.988 167.674 213.357 1.00 76.38  ? 160 GLY B N     1 
ATOM   5340  C  CA    . GLY B 2 160 ? 133.721 168.682 214.089 1.00 83.07  ? 160 GLY B CA    1 
ATOM   5341  C  C     . GLY B 2 160 ? 132.899 169.856 214.572 1.00 86.61  ? 160 GLY B C     1 
ATOM   5342  O  O     . GLY B 2 160 ? 133.468 170.790 215.150 1.00 87.23  ? 160 GLY B O     1 
ATOM   5343  N  N     . GLU B 2 161 ? 131.587 169.847 214.353 1.00 98.80  ? 161 GLU B N     1 
ATOM   5344  C  CA    . GLU B 2 161 ? 130.704 170.913 214.798 1.00 97.81  ? 161 GLU B CA    1 
ATOM   5345  C  C     . GLU B 2 161 ? 129.636 170.343 215.721 1.00 103.68 ? 161 GLU B C     1 
ATOM   5346  O  O     . GLU B 2 161 ? 129.082 169.270 215.469 1.00 105.22 ? 161 GLU B O     1 
ATOM   5347  C  CB    . GLU B 2 161 ? 130.050 171.627 213.610 1.00 100.26 ? 161 GLU B CB    1 
ATOM   5348  C  CG    . GLU B 2 161 ? 131.045 172.195 212.612 1.00 102.08 ? 161 GLU B CG    1 
ATOM   5349  C  CD    . GLU B 2 161 ? 130.422 173.215 211.681 1.00 107.07 ? 161 GLU B CD    1 
ATOM   5350  O  OE1   . GLU B 2 161 ? 129.203 173.460 211.795 1.00 105.69 ? 161 GLU B OE1   1 
ATOM   5351  O  OE2   . GLU B 2 161 ? 131.151 173.771 210.834 1.00 109.12 ? 161 GLU B OE2   1 
ATOM   5352  N  N     . SER B 2 162 ? 129.347 171.080 216.795 1.00 118.38 ? 162 SER B N     1 
ATOM   5353  C  CA    . SER B 2 162 ? 128.451 170.602 217.839 1.00 118.28 ? 162 SER B CA    1 
ATOM   5354  C  C     . SER B 2 162 ? 126.982 170.900 217.571 1.00 115.42 ? 162 SER B C     1 
ATOM   5355  O  O     . SER B 2 162 ? 126.140 170.563 218.410 1.00 112.45 ? 162 SER B O     1 
ATOM   5356  C  CB    . SER B 2 162 ? 128.843 171.211 219.191 1.00 115.41 ? 162 SER B CB    1 
ATOM   5357  O  OG    . SER B 2 162 ? 129.259 172.557 219.043 1.00 117.16 ? 162 SER B OG    1 
ATOM   5358  N  N     . ALA B 2 163 ? 126.656 171.518 216.442 1.00 105.87 ? 163 ALA B N     1 
ATOM   5359  C  CA    . ALA B 2 163 ? 125.267 171.824 216.139 1.00 103.44 ? 163 ALA B CA    1 
ATOM   5360  C  C     . ALA B 2 163 ? 124.478 170.530 215.951 1.00 105.78 ? 163 ALA B C     1 
ATOM   5361  O  O     . ALA B 2 163 ? 124.865 169.688 215.129 1.00 109.25 ? 163 ALA B O     1 
ATOM   5362  C  CB    . ALA B 2 163 ? 125.172 172.689 214.881 1.00 103.83 ? 163 ALA B CB    1 
ATOM   5363  N  N     . PRO B 2 164 ? 123.386 170.332 216.686 1.00 99.73  ? 164 PRO B N     1 
ATOM   5364  C  CA    . PRO B 2 164 ? 122.626 169.085 216.563 1.00 97.60  ? 164 PRO B CA    1 
ATOM   5365  C  C     . PRO B 2 164 ? 121.940 168.968 215.210 1.00 95.07  ? 164 PRO B C     1 
ATOM   5366  O  O     . PRO B 2 164 ? 121.607 169.958 214.556 1.00 96.61  ? 164 PRO B O     1 
ATOM   5367  C  CB    . PRO B 2 164 ? 121.597 169.180 217.696 1.00 95.09  ? 164 PRO B CB    1 
ATOM   5368  C  CG    . PRO B 2 164 ? 122.134 170.232 218.625 1.00 98.20  ? 164 PRO B CG    1 
ATOM   5369  C  CD    . PRO B 2 164 ? 122.845 171.203 217.740 1.00 98.41  ? 164 PRO B CD    1 
ATOM   5370  N  N     . VAL B 2 165 ? 121.729 167.720 214.797 1.00 80.54  ? 165 VAL B N     1 
ATOM   5371  C  CA    . VAL B 2 165 ? 121.019 167.406 213.567 1.00 82.30  ? 165 VAL B CA    1 
ATOM   5372  C  C     . VAL B 2 165 ? 119.802 166.561 213.917 1.00 81.40  ? 165 VAL B C     1 
ATOM   5373  O  O     . VAL B 2 165 ? 119.664 166.056 215.034 1.00 84.67  ? 165 VAL B O     1 
ATOM   5374  C  CB    . VAL B 2 165 ? 121.911 166.678 212.541 1.00 78.60  ? 165 VAL B CB    1 
ATOM   5375  C  CG1   . VAL B 2 165 ? 123.168 167.484 212.262 1.00 82.00  ? 165 VAL B CG1   1 
ATOM   5376  C  CG2   . VAL B 2 165 ? 122.259 165.284 213.034 1.00 78.80  ? 165 VAL B CG2   1 
ATOM   5377  N  N     . ILE B 2 166 ? 118.911 166.413 212.943 1.00 84.41  ? 166 ILE B N     1 
ATOM   5378  C  CA    . ILE B 2 166 ? 117.666 165.675 213.120 1.00 86.13  ? 166 ILE B CA    1 
ATOM   5379  C  C     . ILE B 2 166 ? 117.771 164.363 212.356 1.00 85.04  ? 166 ILE B C     1 
ATOM   5380  O  O     . ILE B 2 166 ? 118.053 164.356 211.151 1.00 93.14  ? 166 ILE B O     1 
ATOM   5381  C  CB    . ILE B 2 166 ? 116.456 166.494 212.646 1.00 93.19  ? 166 ILE B CB    1 
ATOM   5382  C  CG1   . ILE B 2 166 ? 116.299 167.753 213.499 1.00 93.08  ? 166 ILE B CG1   1 
ATOM   5383  C  CG2   . ILE B 2 166 ? 115.192 165.651 212.696 1.00 88.79  ? 166 ILE B CG2   1 
ATOM   5384  C  CD1   . ILE B 2 166 ? 115.092 168.589 213.136 1.00 93.42  ? 166 ILE B CD1   1 
ATOM   5385  N  N     . ARG B 2 167 ? 117.546 163.253 213.053 1.00 65.74  ? 167 ARG B N     1 
ATOM   5386  C  CA    . ARG B 2 167 ? 117.539 161.927 212.453 1.00 67.80  ? 167 ARG B CA    1 
ATOM   5387  C  C     . ARG B 2 167 ? 116.203 161.260 212.741 1.00 72.44  ? 167 ARG B C     1 
ATOM   5388  O  O     . ARG B 2 167 ? 115.782 161.181 213.900 1.00 74.84  ? 167 ARG B O     1 
ATOM   5389  C  CB    . ARG B 2 167 ? 118.689 161.072 212.989 1.00 70.54  ? 167 ARG B CB    1 
ATOM   5390  C  CG    . ARG B 2 167 ? 120.068 161.608 212.649 1.00 69.30  ? 167 ARG B CG    1 
ATOM   5391  C  CD    . ARG B 2 167 ? 120.325 161.563 211.154 1.00 69.93  ? 167 ARG B CD    1 
ATOM   5392  N  NE    . ARG B 2 167 ? 121.609 162.157 210.804 1.00 73.12  ? 167 ARG B NE    1 
ATOM   5393  C  CZ    . ARG B 2 167 ? 122.089 162.227 209.570 1.00 77.48  ? 167 ARG B CZ    1 
ATOM   5394  N  NH1   . ARG B 2 167 ? 121.415 161.747 208.538 1.00 75.45  ? 167 ARG B NH1   1 
ATOM   5395  N  NH2   . ARG B 2 167 ? 123.275 162.791 209.367 1.00 75.59  ? 167 ARG B NH2   1 
ATOM   5396  N  N     . GLU B 2 168 ? 115.542 160.784 211.690 1.00 90.84  ? 168 GLU B N     1 
ATOM   5397  C  CA    . GLU B 2 168 ? 114.243 160.143 211.827 1.00 89.46  ? 168 GLU B CA    1 
ATOM   5398  C  C     . GLU B 2 168 ? 114.060 159.148 210.691 1.00 94.10  ? 168 GLU B C     1 
ATOM   5399  O  O     . GLU B 2 168 ? 114.712 159.239 209.649 1.00 98.90  ? 168 GLU B O     1 
ATOM   5400  C  CB    . GLU B 2 168 ? 113.107 161.171 211.834 1.00 89.29  ? 168 GLU B CB    1 
ATOM   5401  C  CG    . GLU B 2 168 ? 113.218 162.215 210.738 1.00 94.02  ? 168 GLU B CG    1 
ATOM   5402  C  CD    . GLU B 2 168 ? 111.917 162.953 210.501 1.00 98.69  ? 168 GLU B CD    1 
ATOM   5403  O  OE1   . GLU B 2 168 ? 111.429 163.616 211.440 1.00 99.30  ? 168 GLU B OE1   1 
ATOM   5404  O  OE2   . GLU B 2 168 ? 111.382 162.870 209.376 1.00 101.10 ? 168 GLU B OE2   1 
ATOM   5405  N  N     . SER B 2 169 ? 113.156 158.199 210.904 1.00 86.88  ? 169 SER B N     1 
ATOM   5406  C  CA    . SER B 2 169 ? 112.927 157.124 209.952 1.00 86.17  ? 169 SER B CA    1 
ATOM   5407  C  C     . SER B 2 169 ? 111.953 157.554 208.859 1.00 88.43  ? 169 SER B C     1 
ATOM   5408  O  O     . SER B 2 169 ? 111.148 158.471 209.031 1.00 91.84  ? 169 SER B O     1 
ATOM   5409  C  CB    . SER B 2 169 ? 112.390 155.884 210.665 1.00 87.08  ? 169 SER B CB    1 
ATOM   5410  O  OG    . SER B 2 169 ? 111.162 156.163 211.314 1.00 85.93  ? 169 SER B OG    1 
ATOM   5411  N  N     . GLY B 2 170 ? 112.043 156.870 207.719 1.00 95.62  ? 170 GLY B N     1 
ATOM   5412  C  CA    . GLY B 2 170 ? 111.108 157.049 206.630 1.00 98.20  ? 170 GLY B CA    1 
ATOM   5413  C  C     . GLY B 2 170 ? 111.434 158.157 205.654 1.00 96.43  ? 170 GLY B C     1 
ATOM   5414  O  O     . GLY B 2 170 ? 110.720 158.306 204.654 1.00 96.03  ? 170 GLY B O     1 
ATOM   5415  N  N     . GLY B 2 171 ? 112.481 158.938 205.902 1.00 103.77 ? 171 GLY B N     1 
ATOM   5416  C  CA    . GLY B 2 171 ? 112.833 160.019 205.004 1.00 102.70 ? 171 GLY B CA    1 
ATOM   5417  C  C     . GLY B 2 171 ? 114.292 160.005 204.601 1.00 103.83 ? 171 GLY B C     1 
ATOM   5418  O  O     . GLY B 2 171 ? 114.934 158.950 204.599 1.00 107.82 ? 171 GLY B O     1 
ATOM   5419  N  N     . ASP B 2 172 ? 114.827 161.173 204.255 1.00 93.10  ? 172 ASP B N     1 
ATOM   5420  C  CA    . ASP B 2 172 ? 116.236 161.299 203.911 1.00 94.41  ? 172 ASP B CA    1 
ATOM   5421  C  C     . ASP B 2 172 ? 117.126 161.469 205.134 1.00 93.71  ? 172 ASP B C     1 
ATOM   5422  O  O     . ASP B 2 172 ? 118.349 161.558 204.984 1.00 97.42  ? 172 ASP B O     1 
ATOM   5423  C  CB    . ASP B 2 172 ? 116.441 162.477 202.955 1.00 100.18 ? 172 ASP B CB    1 
ATOM   5424  C  CG    . ASP B 2 172 ? 115.805 162.242 201.599 1.00 103.51 ? 172 ASP B CG    1 
ATOM   5425  O  OD1   . ASP B 2 172 ? 116.096 161.199 200.976 1.00 101.85 ? 172 ASP B OD1   1 
ATOM   5426  O  OD2   . ASP B 2 172 ? 115.014 163.101 201.155 1.00 101.55 ? 172 ASP B OD2   1 
ATOM   5427  N  N     . PHE B 2 173 ? 116.546 161.519 206.332 1.00 78.94  ? 173 PHE B N     1 
ATOM   5428  C  CA    . PHE B 2 173 ? 117.299 161.626 207.572 1.00 79.94  ? 173 PHE B CA    1 
ATOM   5429  C  C     . PHE B 2 173 ? 117.458 160.284 208.273 1.00 82.69  ? 173 PHE B C     1 
ATOM   5430  O  O     . PHE B 2 173 ? 117.858 160.248 209.441 1.00 81.82  ? 173 PHE B O     1 
ATOM   5431  C  CB    . PHE B 2 173 ? 116.626 162.629 208.510 1.00 76.18  ? 173 PHE B CB    1 
ATOM   5432  C  CG    . PHE B 2 173 ? 116.401 163.977 207.893 1.00 77.91  ? 173 PHE B CG    1 
ATOM   5433  C  CD1   . PHE B 2 173 ? 117.469 164.808 207.604 1.00 80.16  ? 173 PHE B CD1   1 
ATOM   5434  C  CD2   . PHE B 2 173 ? 115.121 164.413 207.600 1.00 80.60  ? 173 PHE B CD2   1 
ATOM   5435  C  CE1   . PHE B 2 173 ? 117.264 166.049 207.035 1.00 79.70  ? 173 PHE B CE1   1 
ATOM   5436  C  CE2   . PHE B 2 173 ? 114.910 165.653 207.031 1.00 81.20  ? 173 PHE B CE2   1 
ATOM   5437  C  CZ    . PHE B 2 173 ? 115.983 166.472 206.748 1.00 81.81  ? 173 PHE B CZ    1 
ATOM   5438  N  N     . ALA B 2 174 ? 117.147 159.180 207.590 1.00 82.27  ? 174 ALA B N     1 
ATOM   5439  C  CA    . ALA B 2 174 ? 117.250 157.868 208.216 1.00 79.10  ? 174 ALA B CA    1 
ATOM   5440  C  C     . ALA B 2 174 ? 118.697 157.420 208.364 1.00 85.30  ? 174 ALA B C     1 
ATOM   5441  O  O     . ALA B 2 174 ? 119.016 156.656 209.282 1.00 92.68  ? 174 ALA B O     1 
ATOM   5442  C  CB    . ALA B 2 174 ? 116.457 156.839 207.412 1.00 75.77  ? 174 ALA B CB    1 
ATOM   5443  N  N     . SER B 2 175 ? 119.581 157.876 207.479 1.00 75.07  ? 175 SER B N     1 
ATOM   5444  C  CA    . SER B 2 175 ? 120.974 157.453 207.528 1.00 71.75  ? 175 SER B CA    1 
ATOM   5445  C  C     . SER B 2 175 ? 121.664 158.024 208.760 1.00 70.00  ? 175 SER B C     1 
ATOM   5446  O  O     . SER B 2 175 ? 121.562 159.221 209.045 1.00 73.30  ? 175 SER B O     1 
ATOM   5447  C  CB    . SER B 2 175 ? 121.706 157.892 206.261 1.00 77.52  ? 175 SER B CB    1 
ATOM   5448  O  OG    . SER B 2 175 ? 121.350 157.078 205.158 1.00 82.24  ? 175 SER B OG    1 
ATOM   5449  N  N     . VAL B 2 176 ? 122.367 157.161 209.492 1.00 74.60  ? 176 VAL B N     1 
ATOM   5450  C  CA    . VAL B 2 176 ? 123.132 157.556 210.664 1.00 78.88  ? 176 VAL B CA    1 
ATOM   5451  C  C     . VAL B 2 176 ? 124.511 156.916 210.570 1.00 81.26  ? 176 VAL B C     1 
ATOM   5452  O  O     . VAL B 2 176 ? 124.715 155.921 209.871 1.00 81.68  ? 176 VAL B O     1 
ATOM   5453  C  CB    . VAL B 2 176 ? 122.430 157.163 211.984 1.00 74.33  ? 176 VAL B CB    1 
ATOM   5454  C  CG1   . VAL B 2 176 ? 122.755 155.726 212.361 1.00 77.02  ? 176 VAL B CG1   1 
ATOM   5455  C  CG2   . VAL B 2 176 ? 122.813 158.121 213.101 1.00 77.28  ? 176 VAL B CG2   1 
ATOM   5456  N  N     . THR B 2 177 ? 125.468 157.510 211.277 1.00 74.62  ? 177 THR B N     1 
ATOM   5457  C  CA    . THR B 2 177 ? 126.852 157.061 211.256 1.00 72.33  ? 177 THR B CA    1 
ATOM   5458  C  C     . THR B 2 177 ? 127.331 156.781 212.673 1.00 75.63  ? 177 THR B C     1 
ATOM   5459  O  O     . THR B 2 177 ? 126.964 157.489 213.616 1.00 78.90  ? 177 THR B O     1 
ATOM   5460  C  CB    . THR B 2 177 ? 127.763 158.100 210.593 1.00 70.44  ? 177 THR B CB    1 
ATOM   5461  O  OG1   . THR B 2 177 ? 129.132 157.787 210.875 1.00 78.25  ? 177 THR B OG1   1 
ATOM   5462  C  CG2   . THR B 2 177 ? 127.449 159.495 211.110 1.00 70.14  ? 177 THR B CG2   1 
ATOM   5463  N  N     . GLY B 2 178 ? 128.150 155.741 212.815 1.00 83.46  ? 178 GLY B N     1 
ATOM   5464  C  CA    . GLY B 2 178 ? 128.672 155.387 214.116 1.00 81.16  ? 178 GLY B CA    1 
ATOM   5465  C  C     . GLY B 2 178 ? 129.661 156.408 214.642 1.00 80.04  ? 178 GLY B C     1 
ATOM   5466  O  O     . GLY B 2 178 ? 130.301 157.149 213.897 1.00 84.62  ? 178 GLY B O     1 
ATOM   5467  N  N     . GLY B 2 179 ? 129.785 156.439 215.968 1.00 64.57  ? 179 GLY B N     1 
ATOM   5468  C  CA    . GLY B 2 179 ? 130.645 157.387 216.638 1.00 62.69  ? 179 GLY B CA    1 
ATOM   5469  C  C     . GLY B 2 179 ? 129.981 158.690 217.021 1.00 65.93  ? 179 GLY B C     1 
ATOM   5470  O  O     . GLY B 2 179 ? 130.594 159.491 217.739 1.00 66.62  ? 179 GLY B O     1 
ATOM   5471  N  N     . THR B 2 180 ? 128.756 158.930 216.570 1.00 80.14  ? 180 THR B N     1 
ATOM   5472  C  CA    . THR B 2 180 ? 128.016 160.129 216.929 1.00 81.98  ? 180 THR B CA    1 
ATOM   5473  C  C     . THR B 2 180 ? 127.219 159.894 218.208 1.00 84.91  ? 180 THR B C     1 
ATOM   5474  O  O     . THR B 2 180 ? 126.960 158.757 218.610 1.00 86.52  ? 180 THR B O     1 
ATOM   5475  C  CB    . THR B 2 180 ? 127.080 160.546 215.794 1.00 85.61  ? 180 THR B CB    1 
ATOM   5476  O  OG1   . THR B 2 180 ? 126.243 159.441 215.433 1.00 91.89  ? 180 THR B OG1   1 
ATOM   5477  C  CG2   . THR B 2 180 ? 127.883 160.978 214.579 1.00 81.16  ? 180 THR B CG2   1 
ATOM   5478  N  N     . ARG B 2 181 ? 126.828 160.992 218.848 1.00 93.60  ? 181 ARG B N     1 
ATOM   5479  C  CA    . ARG B 2 181 ? 126.142 160.951 220.133 1.00 92.96  ? 181 ARG B CA    1 
ATOM   5480  C  C     . ARG B 2 181 ? 124.680 161.333 219.945 1.00 95.91  ? 181 ARG B C     1 
ATOM   5481  O  O     . ARG B 2 181 ? 124.376 162.452 219.518 1.00 100.48 ? 181 ARG B O     1 
ATOM   5482  C  CB    . ARG B 2 181 ? 126.814 161.886 221.139 1.00 92.20  ? 181 ARG B CB    1 
ATOM   5483  C  CG    . ARG B 2 181 ? 126.064 162.022 222.453 1.00 94.27  ? 181 ARG B CG    1 
ATOM   5484  C  CD    . ARG B 2 181 ? 126.990 161.829 223.643 1.00 95.78  ? 181 ARG B CD    1 
ATOM   5485  N  NE    . ARG B 2 181 ? 128.158 162.700 223.577 1.00 100.92 ? 181 ARG B NE    1 
ATOM   5486  C  CZ    . ARG B 2 181 ? 128.146 163.994 223.867 1.00 103.42 ? 181 ARG B CZ    1 
ATOM   5487  N  NH1   . ARG B 2 181 ? 127.040 164.605 224.258 1.00 98.72  ? 181 ARG B NH1   1 
ATOM   5488  N  NH2   . ARG B 2 181 ? 129.274 164.691 223.767 1.00 104.31 ? 181 ARG B NH2   1 
ATOM   5489  N  N     . ILE B 2 182 ? 123.781 160.400 220.266 1.00 90.82  ? 182 ILE B N     1 
ATOM   5490  C  CA    . ILE B 2 182 ? 122.359 160.706 220.270 1.00 84.60  ? 182 ILE B CA    1 
ATOM   5491  C  C     . ILE B 2 182 ? 122.043 161.618 221.453 1.00 84.80  ? 182 ILE B C     1 
ATOM   5492  O  O     . ILE B 2 182 ? 122.619 161.487 222.541 1.00 91.42  ? 182 ILE B O     1 
ATOM   5493  C  CB    . ILE B 2 182 ? 121.534 159.409 220.317 1.00 81.41  ? 182 ILE B CB    1 
ATOM   5494  C  CG1   . ILE B 2 182 ? 120.080 159.699 220.689 1.00 86.88  ? 182 ILE B CG1   1 
ATOM   5495  C  CG2   . ILE B 2 182 ? 122.165 158.415 221.274 1.00 91.54  ? 182 ILE B CG2   1 
ATOM   5496  C  CD1   . ILE B 2 182 ? 119.143 158.592 220.334 1.00 95.50  ? 182 ILE B CD1   1 
ATOM   5497  N  N     . LEU B 2 183 ? 121.122 162.555 221.241 1.00 88.45  ? 183 LEU B N     1 
ATOM   5498  C  CA    . LEU B 2 183 ? 120.943 163.655 222.178 1.00 88.96  ? 183 LEU B CA    1 
ATOM   5499  C  C     . LEU B 2 183 ? 119.653 163.609 222.983 1.00 93.38  ? 183 LEU B C     1 
ATOM   5500  O  O     . LEU B 2 183 ? 119.703 163.786 224.203 1.00 91.86  ? 183 LEU B O     1 
ATOM   5501  C  CB    . LEU B 2 183 ? 121.018 164.995 221.430 1.00 92.34  ? 183 LEU B CB    1 
ATOM   5502  C  CG    . LEU B 2 183 ? 122.402 165.644 221.362 1.00 90.29  ? 183 LEU B CG    1 
ATOM   5503  C  CD1   . LEU B 2 183 ? 122.294 167.094 220.918 1.00 92.86  ? 183 LEU B CD1   1 
ATOM   5504  C  CD2   . LEU B 2 183 ? 123.112 165.542 222.702 1.00 88.14  ? 183 LEU B CD2   1 
ATOM   5505  N  N     . SER B 2 184 ? 118.494 163.381 222.361 1.00 103.62 ? 184 SER B N     1 
ATOM   5506  C  CA    . SER B 2 184 ? 117.244 163.774 223.003 1.00 103.89 ? 184 SER B CA    1 
ATOM   5507  C  C     . SER B 2 184 ? 116.389 162.610 223.494 1.00 102.47 ? 184 SER B C     1 
ATOM   5508  O  O     . SER B 2 184 ? 116.160 162.506 224.702 1.00 104.33 ? 184 SER B O     1 
ATOM   5509  C  CB    . SER B 2 184 ? 116.431 164.649 222.037 1.00 104.20 ? 184 SER B CB    1 
ATOM   5510  O  OG    . SER B 2 184 ? 116.080 163.930 220.869 1.00 107.48 ? 184 SER B OG    1 
ATOM   5511  N  N     . ASP B 2 185 ? 115.899 161.724 222.621 1.00 97.61  ? 185 ASP B N     1 
ATOM   5512  C  CA    . ASP B 2 185 ? 114.958 160.704 223.084 1.00 98.20  ? 185 ASP B CA    1 
ATOM   5513  C  C     . ASP B 2 185 ? 115.448 159.278 222.860 1.00 99.04  ? 185 ASP B C     1 
ATOM   5514  O  O     . ASP B 2 185 ? 115.754 158.589 223.836 1.00 105.41 ? 185 ASP B O     1 
ATOM   5515  C  CB    . ASP B 2 185 ? 113.601 160.928 222.413 1.00 98.18  ? 185 ASP B CB    1 
ATOM   5516  C  CG    . ASP B 2 185 ? 113.228 162.395 222.330 1.00 104.87 ? 185 ASP B CG    1 
ATOM   5517  O  OD1   . ASP B 2 185 ? 113.230 163.070 223.381 1.00 109.46 ? 185 ASP B OD1   1 
ATOM   5518  O  OD2   . ASP B 2 185 ? 112.933 162.872 221.215 1.00 103.87 ? 185 ASP B OD2   1 
ATOM   5519  N  N     . TRP B 2 186 ? 115.570 158.826 221.612 1.00 87.71  ? 186 TRP B N     1 
ATOM   5520  C  CA    . TRP B 2 186 ? 115.937 157.448 221.292 1.00 89.50  ? 186 TRP B CA    1 
ATOM   5521  C  C     . TRP B 2 186 ? 115.911 157.278 219.779 1.00 90.76  ? 186 TRP B C     1 
ATOM   5522  O  O     . TRP B 2 186 ? 115.283 158.061 219.062 1.00 99.60  ? 186 TRP B O     1 
ATOM   5523  C  CB    . TRP B 2 186 ? 115.002 156.419 221.945 1.00 88.88  ? 186 TRP B CB    1 
ATOM   5524  C  CG    . TRP B 2 186 ? 113.548 156.638 221.660 1.00 90.45  ? 186 TRP B CG    1 
ATOM   5525  C  CD1   . TRP B 2 186 ? 112.725 157.551 222.251 1.00 91.14  ? 186 TRP B CD1   1 
ATOM   5526  C  CD2   . TRP B 2 186 ? 112.740 155.919 220.721 1.00 93.17  ? 186 TRP B CD2   1 
ATOM   5527  N  NE1   . TRP B 2 186 ? 111.457 157.450 221.734 1.00 93.22  ? 186 TRP B NE1   1 
ATOM   5528  C  CE2   . TRP B 2 186 ? 111.440 156.455 220.793 1.00 93.86  ? 186 TRP B CE2   1 
ATOM   5529  C  CE3   . TRP B 2 186 ? 112.991 154.877 219.824 1.00 93.33  ? 186 TRP B CE3   1 
ATOM   5530  C  CZ2   . TRP B 2 186 ? 110.394 155.984 220.003 1.00 93.68  ? 186 TRP B CZ2   1 
ATOM   5531  C  CZ3   . TRP B 2 186 ? 111.951 154.411 219.041 1.00 95.66  ? 186 TRP B CZ3   1 
ATOM   5532  C  CH2   . TRP B 2 186 ? 110.669 154.964 219.135 1.00 92.26  ? 186 TRP B CH2   1 
ATOM   5533  N  N     . LEU B 2 187 ? 116.589 156.233 219.308 1.00 78.26  ? 187 LEU B N     1 
ATOM   5534  C  CA    . LEU B 2 187 ? 116.501 155.792 217.923 1.00 76.02  ? 187 LEU B CA    1 
ATOM   5535  C  C     . LEU B 2 187 ? 116.583 154.274 217.878 1.00 70.21  ? 187 LEU B C     1 
ATOM   5536  O  O     . LEU B 2 187 ? 117.104 153.631 218.793 1.00 82.17  ? 187 LEU B O     1 
ATOM   5537  C  CB    . LEU B 2 187 ? 117.606 156.393 217.039 1.00 76.06  ? 187 LEU B CB    1 
ATOM   5538  C  CG    . LEU B 2 187 ? 117.860 157.900 217.037 1.00 75.25  ? 187 LEU B CG    1 
ATOM   5539  C  CD1   . LEU B 2 187 ? 119.205 158.203 216.404 1.00 78.54  ? 187 LEU B CD1   1 
ATOM   5540  C  CD2   . LEU B 2 187 ? 116.753 158.619 216.289 1.00 76.71  ? 187 LEU B CD2   1 
ATOM   5541  N  N     . VAL B 2 188 ? 116.057 153.705 216.798 1.00 67.16  ? 188 VAL B N     1 
ATOM   5542  C  CA    . VAL B 2 188 ? 116.152 152.275 216.523 1.00 70.01  ? 188 VAL B CA    1 
ATOM   5543  C  C     . VAL B 2 188 ? 116.865 152.145 215.185 1.00 75.29  ? 188 VAL B C     1 
ATOM   5544  O  O     . VAL B 2 188 ? 116.269 152.376 214.126 1.00 91.30  ? 188 VAL B O     1 
ATOM   5545  C  CB    . VAL B 2 188 ? 114.782 151.590 216.497 1.00 75.46  ? 188 VAL B CB    1 
ATOM   5546  C  CG1   . VAL B 2 188 ? 114.941 150.107 216.198 1.00 74.31  ? 188 VAL B CG1   1 
ATOM   5547  C  CG2   . VAL B 2 188 ? 114.062 151.795 217.818 1.00 77.76  ? 188 VAL B CG2   1 
ATOM   5548  N  N     . ILE B 2 189 ? 118.140 151.771 215.223 1.00 68.95  ? 189 ILE B N     1 
ATOM   5549  C  CA    . ILE B 2 189 ? 118.995 151.750 214.043 1.00 68.38  ? 189 ILE B CA    1 
ATOM   5550  C  C     . ILE B 2 189 ? 119.201 150.309 213.603 1.00 71.21  ? 189 ILE B C     1 
ATOM   5551  O  O     . ILE B 2 189 ? 119.492 149.434 214.428 1.00 86.07  ? 189 ILE B O     1 
ATOM   5552  C  CB    . ILE B 2 189 ? 120.344 152.433 214.323 1.00 68.13  ? 189 ILE B CB    1 
ATOM   5553  C  CG1   . ILE B 2 189 ? 120.125 153.859 214.830 1.00 75.24  ? 189 ILE B CG1   1 
ATOM   5554  C  CG2   . ILE B 2 189 ? 121.212 152.433 213.075 1.00 72.74  ? 189 ILE B CG2   1 
ATOM   5555  C  CD1   . ILE B 2 189 ? 120.382 154.026 216.310 1.00 77.39  ? 189 ILE B CD1   1 
ATOM   5556  N  N     . GLU B 2 190 ? 119.042 150.060 212.307 1.00 85.96  ? 190 GLU B N     1 
ATOM   5557  C  CA    . GLU B 2 190 ? 119.370 148.776 211.705 1.00 89.95  ? 190 GLU B CA    1 
ATOM   5558  C  C     . GLU B 2 190 ? 120.714 148.907 210.999 1.00 96.66  ? 190 GLU B C     1 
ATOM   5559  O  O     . GLU B 2 190 ? 120.839 149.672 210.037 1.00 101.48 ? 190 GLU B O     1 
ATOM   5560  C  CB    . GLU B 2 190 ? 118.285 148.337 210.723 1.00 95.39  ? 190 GLU B CB    1 
ATOM   5561  C  CG    . GLU B 2 190 ? 118.591 147.033 210.006 1.00 100.30 ? 190 GLU B CG    1 
ATOM   5562  C  CD    . GLU B 2 190 ? 118.853 147.230 208.527 1.00 102.47 ? 190 GLU B CD    1 
ATOM   5563  O  OE1   . GLU B 2 190 ? 118.784 148.385 208.058 1.00 102.98 ? 190 GLU B OE1   1 
ATOM   5564  O  OE2   . GLU B 2 190 ? 119.129 146.229 207.833 1.00 101.93 ? 190 GLU B OE2   1 
ATOM   5565  N  N     . CYS B 2 191 ? 121.713 148.169 211.481 1.00 110.48 ? 191 CYS B N     1 
ATOM   5566  C  CA    . CYS B 2 191 ? 123.054 148.264 210.920 1.00 107.05 ? 191 CYS B CA    1 
ATOM   5567  C  C     . CYS B 2 191 ? 123.051 147.856 209.453 1.00 107.25 ? 191 CYS B C     1 
ATOM   5568  O  O     . CYS B 2 191 ? 122.479 146.827 209.081 1.00 112.44 ? 191 CYS B O     1 
ATOM   5569  C  CB    . CYS B 2 191 ? 124.022 147.388 211.715 1.00 106.33 ? 191 CYS B CB    1 
ATOM   5570  S  SG    . CYS B 2 191 ? 125.709 148.032 211.807 1.00 119.99 ? 191 CYS B SG    1 
ATOM   5571  N  N     . SER B 2 192 ? 123.697 148.670 208.616 1.00 99.20  ? 192 SER B N     1 
ATOM   5572  C  CA    . SER B 2 192 ? 123.704 148.453 207.178 1.00 102.68 ? 192 SER B CA    1 
ATOM   5573  C  C     . SER B 2 192 ? 125.051 148.018 206.624 1.00 106.95 ? 192 SER B C     1 
ATOM   5574  O  O     . SER B 2 192 ? 125.094 147.478 205.514 1.00 108.42 ? 192 SER B O     1 
ATOM   5575  C  CB    . SER B 2 192 ? 123.262 149.728 206.445 1.00 103.54 ? 192 SER B CB    1 
ATOM   5576  O  OG    . SER B 2 192 ? 123.994 150.853 206.897 1.00 99.50  ? 192 SER B OG    1 
ATOM   5577  N  N     . VAL B 2 193 ? 126.143 148.239 207.352 1.00 106.19 ? 193 VAL B N     1 
ATOM   5578  C  CA    . VAL B 2 193 ? 127.481 147.897 206.887 1.00 104.87 ? 193 VAL B CA    1 
ATOM   5579  C  C     . VAL B 2 193 ? 128.164 147.036 207.940 1.00 103.70 ? 193 VAL B C     1 
ATOM   5580  O  O     . VAL B 2 193 ? 128.121 147.352 209.134 1.00 102.42 ? 193 VAL B O     1 
ATOM   5581  C  CB    . VAL B 2 193 ? 128.319 149.152 206.574 1.00 105.03 ? 193 VAL B CB    1 
ATOM   5582  C  CG1   . VAL B 2 193 ? 127.783 149.847 205.334 1.00 103.38 ? 193 VAL B CG1   1 
ATOM   5583  C  CG2   . VAL B 2 193 ? 128.315 150.112 207.754 1.00 104.25 ? 193 VAL B CG2   1 
ATOM   5584  N  N     . ASN B 2 194 ? 128.776 145.941 207.497 1.00 112.30 ? 194 ASN B N     1 
ATOM   5585  C  CA    . ASN B 2 194 ? 129.555 145.100 208.385 1.00 112.57 ? 194 ASN B CA    1 
ATOM   5586  C  C     . ASN B 2 194 ? 130.853 145.810 208.767 1.00 113.73 ? 194 ASN B C     1 
ATOM   5587  O  O     . ASN B 2 194 ? 131.288 146.735 208.077 1.00 116.22 ? 194 ASN B O     1 
ATOM   5588  C  CB    . ASN B 2 194 ? 129.855 143.761 207.717 1.00 112.34 ? 194 ASN B CB    1 
ATOM   5589  C  CG    . ASN B 2 194 ? 130.323 143.916 206.284 1.00 115.25 ? 194 ASN B CG    1 
ATOM   5590  O  OD1   . ASN B 2 194 ? 131.397 144.460 206.025 1.00 116.36 ? 194 ASN B OD1   1 
ATOM   5591  N  ND2   . ASN B 2 194 ? 129.518 143.438 205.343 1.00 113.84 ? 194 ASN B ND2   1 
ATOM   5592  N  N     . PRO B 2 195 ? 131.478 145.409 209.875 1.00 117.10 ? 195 PRO B N     1 
ATOM   5593  C  CA    . PRO B 2 195 ? 132.750 146.031 210.263 1.00 116.73 ? 195 PRO B CA    1 
ATOM   5594  C  C     . PRO B 2 195 ? 133.795 145.890 209.165 1.00 117.24 ? 195 PRO B C     1 
ATOM   5595  O  O     . PRO B 2 195 ? 133.889 144.859 208.497 1.00 119.59 ? 195 PRO B O     1 
ATOM   5596  C  CB    . PRO B 2 195 ? 133.149 145.261 211.525 1.00 115.48 ? 195 PRO B CB    1 
ATOM   5597  C  CG    . PRO B 2 195 ? 131.855 144.795 212.093 1.00 119.07 ? 195 PRO B CG    1 
ATOM   5598  C  CD    . PRO B 2 195 ? 130.984 144.482 210.909 1.00 118.01 ? 195 PRO B CD    1 
ATOM   5599  N  N     . GLY B 2 196 ? 134.583 146.949 208.986 1.00 99.11  ? 196 GLY B N     1 
ATOM   5600  C  CA    . GLY B 2 196 ? 135.537 147.044 207.908 1.00 99.67  ? 196 GLY B CA    1 
ATOM   5601  C  C     . GLY B 2 196 ? 135.090 147.916 206.754 1.00 96.48  ? 196 GLY B C     1 
ATOM   5602  O  O     . GLY B 2 196 ? 135.924 148.303 205.927 1.00 96.47  ? 196 GLY B O     1 
ATOM   5603  N  N     . GLU B 2 197 ? 133.797 148.237 206.679 1.00 95.30  ? 197 GLU B N     1 
ATOM   5604  C  CA    . GLU B 2 197 ? 133.260 149.125 205.654 1.00 97.42  ? 197 GLU B CA    1 
ATOM   5605  C  C     . GLU B 2 197 ? 132.559 150.331 206.270 1.00 98.79  ? 197 GLU B C     1 
ATOM   5606  O  O     . GLU B 2 197 ? 131.703 150.947 205.627 1.00 100.62 ? 197 GLU B O     1 
ATOM   5607  C  CB    . GLU B 2 197 ? 132.309 148.363 204.730 1.00 99.80  ? 197 GLU B CB    1 
ATOM   5608  C  CG    . GLU B 2 197 ? 132.256 148.896 203.306 1.00 101.18 ? 197 GLU B CG    1 
ATOM   5609  C  CD    . GLU B 2 197 ? 133.617 149.317 202.790 1.00 104.83 ? 197 GLU B CD    1 
ATOM   5610  O  OE1   . GLU B 2 197 ? 134.489 148.439 202.622 1.00 108.48 ? 197 GLU B OE1   1 
ATOM   5611  O  OE2   . GLU B 2 197 ? 133.816 150.527 202.553 1.00 101.54 ? 197 GLU B OE2   1 
ATOM   5612  N  N     . THR B 2 198 ? 132.905 150.675 207.507 1.00 88.27  ? 198 THR B N     1 
ATOM   5613  C  CA    . THR B 2 198 ? 132.303 151.816 208.178 1.00 87.87  ? 198 THR B CA    1 
ATOM   5614  C  C     . THR B 2 198 ? 132.713 153.113 207.486 1.00 85.36  ? 198 THR B C     1 
ATOM   5615  O  O     . THR B 2 198 ? 133.761 153.193 206.840 1.00 86.64  ? 198 THR B O     1 
ATOM   5616  C  CB    . THR B 2 198 ? 132.725 151.841 209.650 1.00 89.92  ? 198 THR B CB    1 
ATOM   5617  O  OG1   . THR B 2 198 ? 132.571 150.532 210.210 1.00 90.56  ? 198 THR B OG1   1 
ATOM   5618  C  CG2   . THR B 2 198 ? 131.870 152.813 210.450 1.00 91.12  ? 198 THR B CG2   1 
ATOM   5619  N  N     . PHE B 2 199 ? 131.860 154.133 207.611 1.00 66.97  ? 199 PHE B N     1 
ATOM   5620  C  CA    . PHE B 2 199 ? 132.170 155.438 207.036 1.00 67.17  ? 199 PHE B CA    1 
ATOM   5621  C  C     . PHE B 2 199 ? 133.470 155.995 207.603 1.00 75.49  ? 199 PHE B C     1 
ATOM   5622  O  O     . PHE B 2 199 ? 134.208 156.704 206.912 1.00 78.89  ? 199 PHE B O     1 
ATOM   5623  C  CB    . PHE B 2 199 ? 131.017 156.411 207.282 1.00 72.81  ? 199 PHE B CB    1 
ATOM   5624  C  CG    . PHE B 2 199 ? 131.203 157.746 206.623 1.00 69.65  ? 199 PHE B CG    1 
ATOM   5625  C  CD1   . PHE B 2 199 ? 131.428 157.835 205.260 1.00 67.58  ? 199 PHE B CD1   1 
ATOM   5626  C  CD2   . PHE B 2 199 ? 131.158 158.913 207.366 1.00 66.32  ? 199 PHE B CD2   1 
ATOM   5627  C  CE1   . PHE B 2 199 ? 131.602 159.062 204.652 1.00 67.16  ? 199 PHE B CE1   1 
ATOM   5628  C  CE2   . PHE B 2 199 ? 131.331 160.142 206.763 1.00 63.06  ? 199 PHE B CE2   1 
ATOM   5629  C  CZ    . PHE B 2 199 ? 131.553 160.216 205.404 1.00 67.74  ? 199 PHE B CZ    1 
ATOM   5630  N  N     . LEU B 2 200 ? 133.765 155.682 208.868 1.00 79.59  ? 200 LEU B N     1 
ATOM   5631  C  CA    . LEU B 2 200 ? 135.030 156.108 209.457 1.00 67.98  ? 200 LEU B CA    1 
ATOM   5632  C  C     . LEU B 2 200 ? 136.213 155.487 208.727 1.00 66.81  ? 200 LEU B C     1 
ATOM   5633  O  O     . LEU B 2 200 ? 137.240 156.143 208.519 1.00 77.06  ? 200 LEU B O     1 
ATOM   5634  C  CB    . LEU B 2 200 ? 135.068 155.748 210.942 1.00 66.76  ? 200 LEU B CB    1 
ATOM   5635  C  CG    . LEU B 2 200 ? 134.390 156.737 211.891 1.00 71.43  ? 200 LEU B CG    1 
ATOM   5636  C  CD1   . LEU B 2 200 ? 134.014 156.054 213.194 1.00 78.94  ? 200 LEU B CD1   1 
ATOM   5637  C  CD2   . LEU B 2 200 ? 135.291 157.932 212.149 1.00 68.19  ? 200 LEU B CD2   1 
ATOM   5638  N  N     . ASP B 2 201 ? 136.088 154.217 208.335 1.00 72.01  ? 201 ASP B N     1 
ATOM   5639  C  CA    . ASP B 2 201 ? 137.143 153.580 207.553 1.00 75.13  ? 201 ASP B CA    1 
ATOM   5640  C  C     . ASP B 2 201 ? 137.320 154.270 206.207 1.00 74.21  ? 201 ASP B C     1 
ATOM   5641  O  O     . ASP B 2 201 ? 138.425 154.294 205.653 1.00 78.14  ? 201 ASP B O     1 
ATOM   5642  C  CB    . ASP B 2 201 ? 136.830 152.097 207.361 1.00 79.25  ? 201 ASP B CB    1 
ATOM   5643  C  CG    . ASP B 2 201 ? 136.580 151.381 208.672 1.00 88.92  ? 201 ASP B CG    1 
ATOM   5644  O  OD1   . ASP B 2 201 ? 136.696 152.027 209.734 1.00 91.40  ? 201 ASP B OD1   1 
ATOM   5645  O  OD2   . ASP B 2 201 ? 136.266 150.173 208.641 1.00 87.02  ? 201 ASP B OD2   1 
ATOM   5646  N  N     . ARG B 2 202 ? 136.237 154.828 205.660 1.00 74.93  ? 202 ARG B N     1 
ATOM   5647  C  CA    . ARG B 2 202 ? 136.345 155.589 204.420 1.00 77.18  ? 202 ARG B CA    1 
ATOM   5648  C  C     . ARG B 2 202 ? 137.190 156.841 204.619 1.00 80.62  ? 202 ARG B C     1 
ATOM   5649  O  O     . ARG B 2 202 ? 138.007 157.191 203.758 1.00 87.84  ? 202 ARG B O     1 
ATOM   5650  C  CB    . ARG B 2 202 ? 134.951 155.948 203.905 1.00 77.71  ? 202 ARG B CB    1 
ATOM   5651  C  CG    . ARG B 2 202 ? 134.942 156.711 202.594 1.00 80.60  ? 202 ARG B CG    1 
ATOM   5652  C  CD    . ARG B 2 202 ? 133.544 157.206 202.262 1.00 80.91  ? 202 ARG B CD    1 
ATOM   5653  N  NE    . ARG B 2 202 ? 133.561 158.257 201.251 1.00 89.87  ? 202 ARG B NE    1 
ATOM   5654  C  CZ    . ARG B 2 202 ? 132.924 158.189 200.090 1.00 85.52  ? 202 ARG B CZ    1 
ATOM   5655  N  NH1   . ARG B 2 202 ? 132.203 157.131 199.759 1.00 80.49  ? 202 ARG B NH1   1 
ATOM   5656  N  NH2   . ARG B 2 202 ? 133.013 159.208 199.241 1.00 85.35  ? 202 ARG B NH2   1 
ATOM   5657  N  N     . MET B 2 203 ? 136.982 157.468 205.773 1.00 70.38  ? 203 MET B N     1 
ATOM   5658  C  CA    . MET B 2 203 ? 137.723 158.703 206.108 1.00 71.16  ? 203 MET B CA    1 
ATOM   5659  C  C     . MET B 2 203 ? 139.185 158.359 206.388 1.00 72.35  ? 203 MET B C     1 
ATOM   5660  O  O     . MET B 2 203 ? 140.051 159.128 205.963 1.00 69.71  ? 203 MET B O     1 
ATOM   5661  C  CB    . MET B 2 203 ? 137.104 159.342 207.350 1.00 72.76  ? 203 MET B CB    1 
ATOM   5662  C  CG    . MET B 2 203 ? 135.612 159.516 207.264 1.00 71.90  ? 203 MET B CG    1 
ATOM   5663  S  SD    . MET B 2 203 ? 134.968 160.349 208.725 1.00 71.22  ? 203 MET B SD    1 
ATOM   5664  C  CE    . MET B 2 203 ? 135.887 161.884 208.664 1.00 75.32  ? 203 MET B CE    1 
ATOM   5665  N  N     . ILE B 2 204 ? 139.440 157.261 207.095 1.00 71.96  ? 204 ILE B N     1 
ATOM   5666  C  CA    . ILE B 2 204 ? 140.840 156.839 207.361 1.00 71.00  ? 204 ILE B CA    1 
ATOM   5667  C  C     . ILE B 2 204 ? 141.473 156.531 206.013 1.00 70.61  ? 204 ILE B C     1 
ATOM   5668  O  O     . ILE B 2 204 ? 142.414 157.232 205.649 1.00 72.27  ? 204 ILE B O     1 
ATOM   5669  C  CB    . ILE B 2 204 ? 140.921 155.630 208.302 1.00 71.17  ? 204 ILE B CB    1 
ATOM   5670  C  CG1   . ILE B 2 204 ? 140.327 155.934 209.676 1.00 70.26  ? 204 ILE B CG1   1 
ATOM   5671  C  CG2   . ILE B 2 204 ? 142.354 155.140 208.404 1.00 71.47  ? 204 ILE B CG2   1 
ATOM   5672  C  CD1   . ILE B 2 204 ? 140.647 157.312 210.174 1.00 70.48  ? 204 ILE B CD1   1 
ATOM   5673  N  N     . ALA B 2 205 ? 140.971 155.538 205.288 1.00 69.84  ? 205 ALA B N     1 
ATOM   5674  C  CA    . ALA B 2 205 ? 141.672 155.256 204.042 1.00 70.33  ? 205 ALA B CA    1 
ATOM   5675  C  C     . ALA B 2 205 ? 141.877 156.499 203.187 1.00 70.43  ? 205 ALA B C     1 
ATOM   5676  O  O     . ALA B 2 205 ? 142.633 156.441 202.212 1.00 71.28  ? 205 ALA B O     1 
ATOM   5677  C  CB    . ALA B 2 205 ? 140.912 154.199 203.240 1.00 70.52  ? 205 ALA B CB    1 
ATOM   5678  N  N     . MET B 2 206 ? 141.225 157.612 203.526 1.00 65.83  ? 206 MET B N     1 
ATOM   5679  C  CA    . MET B 2 206 ? 141.367 158.827 202.733 1.00 65.40  ? 206 MET B CA    1 
ATOM   5680  C  C     . MET B 2 206 ? 142.725 159.484 202.953 1.00 66.03  ? 206 MET B C     1 
ATOM   5681  O  O     . MET B 2 206 ? 143.297 160.064 202.024 1.00 63.95  ? 206 MET B O     1 
ATOM   5682  C  CB    . MET B 2 206 ? 140.242 159.802 203.071 1.00 62.94  ? 206 MET B CB    1 
ATOM   5683  C  CG    . MET B 2 206 ? 140.096 160.939 202.083 1.00 62.29  ? 206 MET B CG    1 
ATOM   5684  S  SD    . MET B 2 206 ? 139.557 162.465 202.871 1.00 70.43  ? 206 MET B SD    1 
ATOM   5685  C  CE    . MET B 2 206 ? 140.262 163.670 201.755 1.00 59.30  ? 206 MET B CE    1 
ATOM   5686  N  N     . VAL B 2 207 ? 143.258 159.401 204.172 1.00 66.17  ? 207 VAL B N     1 
ATOM   5687  C  CA    . VAL B 2 207 ? 144.492 160.089 204.534 1.00 64.28  ? 207 VAL B CA    1 
ATOM   5688  C  C     . VAL B 2 207 ? 145.579 159.137 204.999 1.00 65.38  ? 207 VAL B C     1 
ATOM   5689  O  O     . VAL B 2 207 ? 146.706 159.585 205.257 1.00 66.16  ? 207 VAL B O     1 
ATOM   5690  C  CB    . VAL B 2 207 ? 144.239 161.168 205.603 1.00 63.87  ? 207 VAL B CB    1 
ATOM   5691  C  CG1   . VAL B 2 207 ? 143.742 162.450 204.953 1.00 64.17  ? 207 VAL B CG1   1 
ATOM   5692  C  CG2   . VAL B 2 207 ? 143.246 160.665 206.639 1.00 64.23  ? 207 VAL B CG2   1 
ATOM   5693  N  N     . GLU B 2 208 ? 145.282 157.842 205.129 1.00 74.86  ? 208 GLU B N     1 
ATOM   5694  C  CA    . GLU B 2 208 ? 146.310 156.886 205.532 1.00 74.04  ? 208 GLU B CA    1 
ATOM   5695  C  C     . GLU B 2 208 ? 147.451 156.856 204.523 1.00 76.84  ? 208 GLU B C     1 
ATOM   5696  O  O     . GLU B 2 208 ? 148.628 156.926 204.896 1.00 78.91  ? 208 GLU B O     1 
ATOM   5697  C  CB    . GLU B 2 208 ? 145.698 155.496 205.701 1.00 73.96  ? 208 GLU B CB    1 
ATOM   5698  C  CG    . GLU B 2 208 ? 146.699 154.424 206.098 1.00 77.86  ? 208 GLU B CG    1 
ATOM   5699  C  CD    . GLU B 2 208 ? 147.522 154.817 207.309 1.00 78.68  ? 208 GLU B CD    1 
ATOM   5700  O  OE1   . GLU B 2 208 ? 146.925 155.143 208.356 1.00 77.42  ? 208 GLU B OE1   1 
ATOM   5701  O  OE2   . GLU B 2 208 ? 148.768 154.800 207.213 1.00 78.05  ? 208 GLU B OE2   1 
ATOM   5702  N  N     . GLY B 2 209 ? 147.119 156.759 203.239 1.00 79.76  ? 209 GLY B N     1 
ATOM   5703  C  CA    . GLY B 2 209 ? 148.118 156.862 202.186 1.00 79.89  ? 209 GLY B CA    1 
ATOM   5704  C  C     . GLY B 2 209 ? 149.207 155.812 202.237 1.00 80.36  ? 209 GLY B C     1 
ATOM   5705  O  O     . GLY B 2 209 ? 150.378 156.126 201.986 1.00 81.67  ? 209 GLY B O     1 
ATOM   5706  N  N     . ALA B 2 210 ? 148.851 154.569 202.566 1.00 79.31  ? 210 ALA B N     1 
ATOM   5707  C  CA    . ALA B 2 210 ? 149.839 153.495 202.560 1.00 80.25  ? 210 ALA B CA    1 
ATOM   5708  C  C     . ALA B 2 210 ? 150.385 153.267 201.156 1.00 81.13  ? 210 ALA B C     1 
ATOM   5709  O  O     . ALA B 2 210 ? 151.580 153.461 200.901 1.00 81.31  ? 210 ALA B O     1 
ATOM   5710  C  CB    . ALA B 2 210 ? 149.224 152.211 203.118 1.00 80.23  ? 210 ALA B CB    1 
ATOM   5711  N  N     . GLN B 2 211 ? 149.521 152.862 200.230 1.00 78.11  ? 211 GLN B N     1 
ATOM   5712  C  CA    . GLN B 2 211 ? 149.866 152.701 198.819 1.00 78.58  ? 211 GLN B CA    1 
ATOM   5713  C  C     . GLN B 2 211 ? 149.065 153.742 198.042 1.00 77.81  ? 211 GLN B C     1 
ATOM   5714  O  O     . GLN B 2 211 ? 147.966 153.462 197.560 1.00 78.20  ? 211 GLN B O     1 
ATOM   5715  C  CB    . GLN B 2 211 ? 149.575 151.278 198.323 1.00 78.66  ? 211 GLN B CB    1 
ATOM   5716  C  CG    . GLN B 2 211 ? 150.646 150.240 198.651 1.00 77.99  ? 211 GLN B CG    1 
ATOM   5717  C  CD    . GLN B 2 211 ? 150.987 150.178 200.128 1.00 79.10  ? 211 GLN B CD    1 
ATOM   5718  O  OE1   . GLN B 2 211 ? 152.016 150.694 200.562 1.00 79.54  ? 211 GLN B OE1   1 
ATOM   5719  N  NE2   . GLN B 2 211 ? 150.121 149.542 200.909 1.00 78.79  ? 211 GLN B NE2   1 
ATOM   5720  N  N     . ARG B 2 212 ? 149.620 154.946 197.926 1.00 66.01  ? 212 ARG B N     1 
ATOM   5721  C  CA    . ARG B 2 212 ? 148.939 156.033 197.237 1.00 65.64  ? 212 ARG B CA    1 
ATOM   5722  C  C     . ARG B 2 212 ? 148.937 155.782 195.734 1.00 64.98  ? 212 ARG B C     1 
ATOM   5723  O  O     . ARG B 2 212 ? 149.960 155.397 195.159 1.00 64.29  ? 212 ARG B O     1 
ATOM   5724  C  CB    . ARG B 2 212 ? 149.610 157.370 197.550 1.00 64.02  ? 212 ARG B CB    1 
ATOM   5725  C  CG    . ARG B 2 212 ? 148.713 158.356 198.282 1.00 63.70  ? 212 ARG B CG    1 
ATOM   5726  C  CD    . ARG B 2 212 ? 149.200 159.788 198.114 1.00 61.73  ? 212 ARG B CD    1 
ATOM   5727  N  NE    . ARG B 2 212 ? 148.839 160.343 196.815 1.00 64.63  ? 212 ARG B NE    1 
ATOM   5728  C  CZ    . ARG B 2 212 ? 149.689 160.941 195.993 1.00 62.92  ? 212 ARG B CZ    1 
ATOM   5729  N  NH1   . ARG B 2 212 ? 150.968 161.083 196.303 1.00 60.78  ? 212 ARG B NH1   1 
ATOM   5730  N  NH2   . ARG B 2 212 ? 149.246 161.412 194.831 1.00 60.22  ? 212 ARG B NH2   1 
ATOM   5731  N  N     . ARG B 2 213 ? 147.787 156.001 195.102 1.00 61.03  ? 213 ARG B N     1 
ATOM   5732  C  CA    . ARG B 2 213 ? 147.645 155.816 193.664 1.00 58.61  ? 213 ARG B CA    1 
ATOM   5733  C  C     . ARG B 2 213 ? 147.902 157.144 192.963 1.00 58.97  ? 213 ARG B C     1 
ATOM   5734  O  O     . ARG B 2 213 ? 147.235 158.144 193.250 1.00 59.84  ? 213 ARG B O     1 
ATOM   5735  C  CB    . ARG B 2 213 ? 146.255 155.284 193.320 1.00 58.63  ? 213 ARG B CB    1 
ATOM   5736  C  CG    . ARG B 2 213 ? 145.884 154.002 194.044 1.00 60.97  ? 213 ARG B CG    1 
ATOM   5737  C  CD    . ARG B 2 213 ? 144.822 154.254 195.101 1.00 62.59  ? 213 ARG B CD    1 
ATOM   5738  N  NE    . ARG B 2 213 ? 143.477 154.223 194.538 1.00 63.54  ? 213 ARG B NE    1 
ATOM   5739  C  CZ    . ARG B 2 213 ? 142.433 154.858 195.054 1.00 62.33  ? 213 ARG B CZ    1 
ATOM   5740  N  NH1   . ARG B 2 213 ? 142.543 155.591 196.150 1.00 60.79  ? 213 ARG B NH1   1 
ATOM   5741  N  NH2   . ARG B 2 213 ? 141.250 154.754 194.456 1.00 61.72  ? 213 ARG B NH2   1 
ATOM   5742  N  N     . LYS B 2 214 ? 148.868 157.151 192.049 1.00 47.76  ? 214 LYS B N     1 
ATOM   5743  C  CA    . LYS B 2 214 ? 149.211 158.370 191.330 1.00 43.74  ? 214 LYS B CA    1 
ATOM   5744  C  C     . LYS B 2 214 ? 148.109 158.730 190.341 1.00 41.74  ? 214 LYS B C     1 
ATOM   5745  O  O     . LYS B 2 214 ? 147.645 157.881 189.574 1.00 41.35  ? 214 LYS B O     1 
ATOM   5746  C  CB    . LYS B 2 214 ? 150.541 158.195 190.600 1.00 41.47  ? 214 LYS B CB    1 
ATOM   5747  C  CG    . LYS B 2 214 ? 151.742 158.072 191.522 1.00 44.21  ? 214 LYS B CG    1 
ATOM   5748  C  CD    . LYS B 2 214 ? 152.907 158.910 191.026 1.00 47.28  ? 214 LYS B CD    1 
ATOM   5749  C  CE    . LYS B 2 214 ? 153.419 158.401 189.688 1.00 47.07  ? 214 LYS B CE    1 
ATOM   5750  N  NZ    . LYS B 2 214 ? 154.654 159.112 189.259 1.00 46.48  ? 214 LYS B NZ    1 
ATOM   5751  N  N     . THR B 2 215 ? 147.692 159.993 190.361 1.00 38.47  ? 215 THR B N     1 
ATOM   5752  C  CA    . THR B 2 215 ? 146.705 160.471 189.411 1.00 35.04  ? 215 THR B CA    1 
ATOM   5753  C  C     . THR B 2 215 ? 147.320 160.551 188.015 1.00 36.26  ? 215 THR B C     1 
ATOM   5754  O  O     . THR B 2 215 ? 148.541 160.637 187.870 1.00 36.62  ? 215 THR B O     1 
ATOM   5755  C  CB    . THR B 2 215 ? 146.174 161.839 189.838 1.00 38.49  ? 215 THR B CB    1 
ATOM   5756  O  OG1   . THR B 2 215 ? 147.209 162.821 189.707 1.00 37.81  ? 215 THR B OG1   1 
ATOM   5757  C  CG2   . THR B 2 215 ? 145.697 161.799 191.283 1.00 34.47  ? 215 THR B CG2   1 
ATOM   5758  N  N     . PRO B 2 216 ? 146.490 160.505 186.967 1.00 37.23  ? 216 PRO B N     1 
ATOM   5759  C  CA    . PRO B 2 216 ? 147.039 160.599 185.603 1.00 30.83  ? 216 PRO B CA    1 
ATOM   5760  C  C     . PRO B 2 216 ? 147.845 161.863 185.359 1.00 29.89  ? 216 PRO B C     1 
ATOM   5761  O  O     . PRO B 2 216 ? 148.789 161.837 184.560 1.00 39.12  ? 216 PRO B O     1 
ATOM   5762  C  CB    . PRO B 2 216 ? 145.790 160.546 184.713 1.00 33.65  ? 216 PRO B CB    1 
ATOM   5763  C  CG    . PRO B 2 216 ? 144.751 159.882 185.538 1.00 32.59  ? 216 PRO B CG    1 
ATOM   5764  C  CD    . PRO B 2 216 ? 145.049 160.194 186.972 1.00 35.53  ? 216 PRO B CD    1 
ATOM   5765  N  N     . ASN B 2 217 ? 147.498 162.973 186.017 1.00 28.82  ? 217 ASN B N     1 
ATOM   5766  C  CA    . ASN B 2 217 ? 148.294 164.188 185.877 1.00 28.07  ? 217 ASN B CA    1 
ATOM   5767  C  C     . ASN B 2 217 ? 149.701 163.995 186.430 1.00 28.03  ? 217 ASN B C     1 
ATOM   5768  O  O     . ASN B 2 217 ? 150.680 164.447 185.825 1.00 28.88  ? 217 ASN B O     1 
ATOM   5769  C  CB    . ASN B 2 217 ? 147.602 165.357 186.576 1.00 28.19  ? 217 ASN B CB    1 
ATOM   5770  C  CG    . ASN B 2 217 ? 148.051 166.700 186.039 1.00 33.03  ? 217 ASN B CG    1 
ATOM   5771  O  OD1   . ASN B 2 217 ? 147.861 167.004 184.861 1.00 37.67  ? 217 ASN B OD1   1 
ATOM   5772  N  ND2   . ASN B 2 217 ? 148.663 167.506 186.897 1.00 36.22  ? 217 ASN B ND2   1 
ATOM   5773  N  N     . GLU B 2 218 ? 149.820 163.337 187.587 1.00 28.15  ? 218 GLU B N     1 
ATOM   5774  C  CA    . GLU B 2 218 ? 151.141 163.054 188.142 1.00 33.15  ? 218 GLU B CA    1 
ATOM   5775  C  C     . GLU B 2 218 ? 151.926 162.110 187.242 1.00 30.83  ? 218 GLU B C     1 
ATOM   5776  O  O     . GLU B 2 218 ? 153.135 162.285 187.050 1.00 34.22  ? 218 GLU B O     1 
ATOM   5777  C  CB    . GLU B 2 218 ? 151.011 162.465 189.547 1.00 31.08  ? 218 GLU B CB    1 
ATOM   5778  C  CG    . GLU B 2 218 ? 150.298 163.363 190.539 1.00 34.87  ? 218 GLU B CG    1 
ATOM   5779  C  CD    . GLU B 2 218 ? 149.965 162.650 191.835 1.00 42.35  ? 218 GLU B CD    1 
ATOM   5780  O  OE1   . GLU B 2 218 ? 150.902 162.177 192.512 1.00 44.70  ? 218 GLU B OE1   1 
ATOM   5781  O  OE2   . GLU B 2 218 ? 148.768 162.562 192.177 1.00 41.51  ? 218 GLU B OE2   1 
ATOM   5782  N  N     . ILE B 2 219 ? 151.256 161.097 186.688 1.00 27.35  ? 219 ILE B N     1 
ATOM   5783  C  CA    . ILE B 2 219 ? 151.925 160.163 185.788 1.00 30.43  ? 219 ILE B CA    1 
ATOM   5784  C  C     . ILE B 2 219 ? 152.408 160.884 184.537 1.00 21.71  ? 219 ILE B C     1 
ATOM   5785  O  O     . ILE B 2 219 ? 153.527 160.656 184.063 1.00 26.69  ? 219 ILE B O     1 
ATOM   5786  C  CB    . ILE B 2 219 ? 150.987 158.990 185.446 1.00 30.57  ? 219 ILE B CB    1 
ATOM   5787  C  CG1   . ILE B 2 219 ? 150.692 158.163 186.699 1.00 32.88  ? 219 ILE B CG1   1 
ATOM   5788  C  CG2   . ILE B 2 219 ? 151.593 158.115 184.358 1.00 26.51  ? 219 ILE B CG2   1 
ATOM   5789  C  CD1   . ILE B 2 219 ? 149.519 157.223 186.550 1.00 29.60  ? 219 ILE B CD1   1 
ATOM   5790  N  N     . ALA B 2 220 ? 151.577 161.773 183.988 1.00 24.64  ? 220 ALA B N     1 
ATOM   5791  C  CA    . ALA B 2 220 ? 151.978 162.523 182.803 1.00 22.39  ? 220 ALA B CA    1 
ATOM   5792  C  C     . ALA B 2 220 ? 153.122 163.479 183.116 1.00 25.78  ? 220 ALA B C     1 
ATOM   5793  O  O     . ALA B 2 220 ? 154.005 163.697 182.278 1.00 20.85  ? 220 ALA B O     1 
ATOM   5794  C  CB    . ALA B 2 220 ? 150.781 163.282 182.232 1.00 17.76  ? 220 ALA B CB    1 
ATOM   5795  N  N     . LEU B 2 221 ? 153.127 164.056 184.319 1.00 24.52  ? 221 LEU B N     1 
ATOM   5796  C  CA    . LEU B 2 221 ? 154.231 164.924 184.714 1.00 20.58  ? 221 LEU B CA    1 
ATOM   5797  C  C     . LEU B 2 221 ? 155.508 164.124 184.932 1.00 26.14  ? 221 LEU B C     1 
ATOM   5798  O  O     . LEU B 2 221 ? 156.606 164.601 184.622 1.00 28.27  ? 221 LEU B O     1 
ATOM   5799  C  CB    . LEU B 2 221 ? 153.866 165.701 185.978 1.00 24.61  ? 221 LEU B CB    1 
ATOM   5800  C  CG    . LEU B 2 221 ? 154.893 166.733 186.450 1.00 25.25  ? 221 LEU B CG    1 
ATOM   5801  C  CD1   . LEU B 2 221 ? 155.320 167.641 185.305 1.00 21.18  ? 221 LEU B CD1   1 
ATOM   5802  C  CD2   . LEU B 2 221 ? 154.353 167.545 187.614 1.00 23.34  ? 221 LEU B CD2   1 
ATOM   5803  N  N     . THR B 2 222 ? 155.384 162.905 185.463 1.00 20.20  ? 222 THR B N     1 
ATOM   5804  C  CA    . THR B 2 222 ? 156.557 162.066 185.683 1.00 18.98  ? 222 THR B CA    1 
ATOM   5805  C  C     . THR B 2 222 ? 157.233 161.707 184.365 1.00 23.84  ? 222 THR B C     1 
ATOM   5806  O  O     . THR B 2 222 ? 158.464 161.610 184.297 1.00 18.08  ? 222 THR B O     1 
ATOM   5807  C  CB    . THR B 2 222 ? 156.163 160.801 186.446 1.00 25.31  ? 222 THR B CB    1 
ATOM   5808  O  OG1   . THR B 2 222 ? 155.356 161.156 187.576 1.00 28.52  ? 222 THR B OG1   1 
ATOM   5809  C  CG2   . THR B 2 222 ? 157.400 160.059 186.930 1.00 24.71  ? 222 THR B CG2   1 
ATOM   5810  N  N     . ILE B 2 223 ? 156.443 161.507 183.307 1.00 26.63  ? 223 ILE B N     1 
ATOM   5811  C  CA    . ILE B 2 223 ? 157.012 161.193 181.999 1.00 20.96  ? 223 ILE B CA    1 
ATOM   5812  C  C     . ILE B 2 223 ? 157.901 162.332 181.517 1.00 18.33  ? 223 ILE B C     1 
ATOM   5813  O  O     . ILE B 2 223 ? 159.014 162.107 181.025 1.00 26.96  ? 223 ILE B O     1 
ATOM   5814  C  CB    . ILE B 2 223 ? 155.891 160.884 180.989 1.00 24.95  ? 223 ILE B CB    1 
ATOM   5815  C  CG1   . ILE B 2 223 ? 155.144 159.612 181.393 1.00 23.84  ? 223 ILE B CG1   1 
ATOM   5816  C  CG2   . ILE B 2 223 ? 156.454 160.750 179.582 1.00 19.60  ? 223 ILE B CG2   1 
ATOM   5817  C  CD1   . ILE B 2 223 ? 153.832 159.418 180.670 1.00 28.97  ? 223 ILE B CD1   1 
ATOM   5818  N  N     . LEU B 2 224 ? 157.426 163.572 181.652 1.00 16.78  ? 224 LEU B N     1 
ATOM   5819  C  CA    . LEU B 2 224 ? 158.232 164.723 181.257 1.00 23.19  ? 224 LEU B CA    1 
ATOM   5820  C  C     . LEU B 2 224 ? 159.474 164.856 182.131 1.00 17.84  ? 224 LEU B C     1 
ATOM   5821  O  O     . LEU B 2 224 ? 160.561 165.167 181.630 1.00 26.95  ? 224 LEU B O     1 
ATOM   5822  C  CB    . LEU B 2 224 ? 157.388 165.996 181.315 1.00 21.87  ? 224 LEU B CB    1 
ATOM   5823  C  CG    . LEU B 2 224 ? 158.140 167.327 181.373 1.00 33.96  ? 224 LEU B CG    1 
ATOM   5824  C  CD1   . LEU B 2 224 ? 158.731 167.667 180.014 1.00 31.89  ? 224 LEU B CD1   1 
ATOM   5825  C  CD2   . LEU B 2 224 ? 157.223 168.440 181.854 1.00 24.79  ? 224 LEU B CD2   1 
ATOM   5826  N  N     . LEU B 2 225 ? 159.332 164.626 183.440 1.00 18.63  ? 225 LEU B N     1 
ATOM   5827  C  CA    . LEU B 2 225 ? 160.481 164.710 184.337 1.00 20.40  ? 225 LEU B CA    1 
ATOM   5828  C  C     . LEU B 2 225 ? 161.523 163.650 184.000 1.00 19.36  ? 225 LEU B C     1 
ATOM   5829  O  O     . LEU B 2 225 ? 162.729 163.918 184.048 1.00 21.37  ? 225 LEU B O     1 
ATOM   5830  C  CB    . LEU B 2 225 ? 160.024 164.575 185.790 1.00 17.88  ? 225 LEU B CB    1 
ATOM   5831  C  CG    . LEU B 2 225 ? 159.170 165.715 186.352 1.00 17.83  ? 225 LEU B CG    1 
ATOM   5832  C  CD1   . LEU B 2 225 ? 159.029 165.585 187.859 1.00 16.63  ? 225 LEU B CD1   1 
ATOM   5833  C  CD2   . LEU B 2 225 ? 159.753 167.070 185.979 1.00 16.50  ? 225 LEU B CD2   1 
ATOM   5834  N  N     . ILE B 2 226 ? 161.076 162.437 183.669 1.00 19.18  ? 226 ILE B N     1 
ATOM   5835  C  CA    . ILE B 2 226 ? 162.003 161.387 183.255 1.00 16.66  ? 226 ILE B CA    1 
ATOM   5836  C  C     . ILE B 2 226 ? 162.691 161.770 181.950 1.00 16.37  ? 226 ILE B C     1 
ATOM   5837  O  O     . ILE B 2 226 ? 163.902 161.577 181.789 1.00 21.53  ? 226 ILE B O     1 
ATOM   5838  C  CB    . ILE B 2 226 ? 161.268 160.039 183.136 1.00 23.50  ? 226 ILE B CB    1 
ATOM   5839  C  CG1   . ILE B 2 226 ? 160.898 159.509 184.522 1.00 20.11  ? 226 ILE B CG1   1 
ATOM   5840  C  CG2   . ILE B 2 226 ? 162.120 159.023 182.391 1.00 21.78  ? 226 ILE B CG2   1 
ATOM   5841  C  CD1   . ILE B 2 226 ? 159.875 158.397 184.496 1.00 19.01  ? 226 ILE B CD1   1 
ATOM   5842  N  N     . ALA B 2 227 ? 161.930 162.321 181.001 1.00 19.11  ? 227 ALA B N     1 
ATOM   5843  C  CA    . ALA B 2 227 ? 162.505 162.703 179.714 1.00 20.01  ? 227 ALA B CA    1 
ATOM   5844  C  C     . ALA B 2 227 ? 163.576 163.774 179.882 1.00 24.01  ? 227 ALA B C     1 
ATOM   5845  O  O     . ALA B 2 227 ? 164.620 163.726 179.222 1.00 22.68  ? 227 ALA B O     1 
ATOM   5846  C  CB    . ALA B 2 227 ? 161.405 163.186 178.770 1.00 18.77  ? 227 ALA B CB    1 
ATOM   5847  N  N     . LEU B 2 228 ? 163.332 164.752 180.757 1.00 20.71  ? 228 LEU B N     1 
ATOM   5848  C  CA    . LEU B 2 228 ? 164.342 165.769 181.030 1.00 20.13  ? 228 LEU B CA    1 
ATOM   5849  C  C     . LEU B 2 228 ? 165.580 165.156 181.672 1.00 22.12  ? 228 LEU B C     1 
ATOM   5850  O  O     . LEU B 2 228 ? 166.711 165.540 181.350 1.00 24.50  ? 228 LEU B O     1 
ATOM   5851  C  CB    . LEU B 2 228 ? 163.758 166.862 181.924 1.00 23.10  ? 228 LEU B CB    1 
ATOM   5852  C  CG    . LEU B 2 228 ? 162.699 167.763 181.286 1.00 29.80  ? 228 LEU B CG    1 
ATOM   5853  C  CD1   . LEU B 2 228 ? 162.340 168.906 182.219 1.00 31.58  ? 228 LEU B CD1   1 
ATOM   5854  C  CD2   . LEU B 2 228 ? 163.181 168.295 179.946 1.00 28.86  ? 228 LEU B CD2   1 
ATOM   5855  N  N     . THR B 2 229 ? 165.384 164.201 182.584 1.00 15.51  ? 229 THR B N     1 
ATOM   5856  C  CA    . THR B 2 229 ? 166.516 163.534 183.220 1.00 22.00  ? 229 THR B CA    1 
ATOM   5857  C  C     . THR B 2 229 ? 167.336 162.750 182.203 1.00 20.97  ? 229 THR B C     1 
ATOM   5858  O  O     . THR B 2 229 ? 168.570 162.719 182.280 1.00 25.93  ? 229 THR B O     1 
ATOM   5859  C  CB    . THR B 2 229 ? 166.019 162.613 184.336 1.00 19.67  ? 229 THR B CB    1 
ATOM   5860  O  OG1   . THR B 2 229 ? 165.247 163.373 185.275 1.00 24.29  ? 229 THR B OG1   1 
ATOM   5861  C  CG2   . THR B 2 229 ? 167.188 161.962 185.062 1.00 9.23   ? 229 THR B CG2   1 
ATOM   5862  N  N     . ILE B 2 230 ? 166.667 162.109 181.242 1.00 22.53  ? 230 ILE B N     1 
ATOM   5863  C  CA    . ILE B 2 230 ? 167.374 161.341 180.219 1.00 21.02  ? 230 ILE B CA    1 
ATOM   5864  C  C     . ILE B 2 230 ? 168.243 162.261 179.371 1.00 23.63  ? 230 ILE B C     1 
ATOM   5865  O  O     . ILE B 2 230 ? 169.413 161.965 179.100 1.00 24.61  ? 230 ILE B O     1 
ATOM   5866  C  CB    . ILE B 2 230 ? 166.372 160.557 179.352 1.00 21.71  ? 230 ILE B CB    1 
ATOM   5867  C  CG1   . ILE B 2 230 ? 165.897 159.303 180.083 1.00 21.70  ? 230 ILE B CG1   1 
ATOM   5868  C  CG2   . ILE B 2 230 ? 166.994 160.185 178.013 1.00 17.84  ? 230 ILE B CG2   1 
ATOM   5869  C  CD1   . ILE B 2 230 ? 164.681 158.657 179.458 1.00 16.10  ? 230 ILE B CD1   1 
ATOM   5870  N  N     . VAL B 2 231 ? 167.684 163.396 178.943 1.00 14.05  ? 231 VAL B N     1 
ATOM   5871  C  CA    . VAL B 2 231 ? 168.419 164.293 178.057 1.00 19.73  ? 231 VAL B CA    1 
ATOM   5872  C  C     . VAL B 2 231 ? 169.584 164.950 178.790 1.00 22.81  ? 231 VAL B C     1 
ATOM   5873  O  O     . VAL B 2 231 ? 170.629 165.220 178.187 1.00 30.68  ? 231 VAL B O     1 
ATOM   5874  C  CB    . VAL B 2 231 ? 167.460 165.327 177.429 1.00 27.20  ? 231 VAL B CB    1 
ATOM   5875  C  CG1   . VAL B 2 231 ? 167.478 166.650 178.186 1.00 20.43  ? 231 VAL B CG1   1 
ATOM   5876  C  CG2   . VAL B 2 231 ? 167.799 165.540 175.962 1.00 24.09  ? 231 VAL B CG2   1 
ATOM   5877  N  N     . PHE B 2 232 ? 169.438 165.213 180.092 1.00 27.18  ? 232 PHE B N     1 
ATOM   5878  C  CA    . PHE B 2 232 ? 170.536 165.795 180.854 1.00 18.96  ? 232 PHE B CA    1 
ATOM   5879  C  C     . PHE B 2 232 ? 171.603 164.763 181.190 1.00 20.84  ? 232 PHE B C     1 
ATOM   5880  O  O     . PHE B 2 232 ? 172.783 165.114 181.302 1.00 26.43  ? 232 PHE B O     1 
ATOM   5881  C  CB    . PHE B 2 232 ? 170.003 166.450 182.129 1.00 19.81  ? 232 PHE B CB    1 
ATOM   5882  C  CG    . PHE B 2 232 ? 169.276 167.740 181.884 1.00 26.39  ? 232 PHE B CG    1 
ATOM   5883  C  CD1   . PHE B 2 232 ? 169.732 168.636 180.931 1.00 25.71  ? 232 PHE B CD1   1 
ATOM   5884  C  CD2   . PHE B 2 232 ? 168.133 168.056 182.600 1.00 23.25  ? 232 PHE B CD2   1 
ATOM   5885  C  CE1   . PHE B 2 232 ? 169.064 169.823 180.699 1.00 24.38  ? 232 PHE B CE1   1 
ATOM   5886  C  CE2   . PHE B 2 232 ? 167.461 169.241 182.372 1.00 24.75  ? 232 PHE B CE2   1 
ATOM   5887  C  CZ    . PHE B 2 232 ? 167.928 170.126 181.421 1.00 27.28  ? 232 PHE B CZ    1 
ATOM   5888  N  N     . LEU B 2 233 ? 171.212 163.499 181.362 1.00 18.70  ? 233 LEU B N     1 
ATOM   5889  C  CA    . LEU B 2 233 ? 172.198 162.442 181.564 1.00 12.10  ? 233 LEU B CA    1 
ATOM   5890  C  C     . LEU B 2 233 ? 173.062 162.255 180.323 1.00 23.65  ? 233 LEU B C     1 
ATOM   5891  O  O     . LEU B 2 233 ? 174.279 162.067 180.429 1.00 23.73  ? 233 LEU B O     1 
ATOM   5892  C  CB    . LEU B 2 233 ? 171.496 161.136 181.939 1.00 17.16  ? 233 LEU B CB    1 
ATOM   5893  C  CG    . LEU B 2 233 ? 172.332 159.854 181.932 1.00 17.94  ? 233 LEU B CG    1 
ATOM   5894  C  CD1   . LEU B 2 233 ? 173.505 159.964 182.895 1.00 22.83  ? 233 LEU B CD1   1 
ATOM   5895  C  CD2   . LEU B 2 233 ? 171.469 158.649 182.272 1.00 24.28  ? 233 LEU B CD2   1 
ATOM   5896  N  N     . LEU B 2 234 ? 172.449 162.302 179.138 1.00 21.62  ? 234 LEU B N     1 
ATOM   5897  C  CA    . LEU B 2 234 ? 173.217 162.192 177.902 1.00 21.60  ? 234 LEU B CA    1 
ATOM   5898  C  C     . LEU B 2 234 ? 174.115 163.406 177.696 1.00 24.02  ? 234 LEU B C     1 
ATOM   5899  O  O     . LEU B 2 234 ? 175.248 163.275 177.222 1.00 29.20  ? 234 LEU B O     1 
ATOM   5900  C  CB    . LEU B 2 234 ? 172.274 162.015 176.712 1.00 13.78  ? 234 LEU B CB    1 
ATOM   5901  C  CG    . LEU B 2 234 ? 171.528 160.683 176.617 1.00 23.76  ? 234 LEU B CG    1 
ATOM   5902  C  CD1   . LEU B 2 234 ? 170.162 160.881 175.980 1.00 23.99  ? 234 LEU B CD1   1 
ATOM   5903  C  CD2   . LEU B 2 234 ? 172.344 159.668 175.837 1.00 26.48  ? 234 LEU B CD2   1 
ATOM   5904  N  N     . ALA B 2 235 ? 173.628 164.597 178.052 1.00 23.42  ? 235 ALA B N     1 
ATOM   5905  C  CA    . ALA B 2 235 ? 174.412 165.808 177.831 1.00 24.16  ? 235 ALA B CA    1 
ATOM   5906  C  C     . ALA B 2 235 ? 175.542 165.931 178.845 1.00 24.01  ? 235 ALA B C     1 
ATOM   5907  O  O     . ALA B 2 235 ? 176.454 166.747 178.673 1.00 34.67  ? 235 ALA B O     1 
ATOM   5908  C  CB    . ALA B 2 235 ? 173.506 167.037 177.883 1.00 16.25  ? 235 ALA B CB    1 
ATOM   5909  N  N     . THR B 2 236 ? 175.502 165.126 179.909 1.00 22.20  ? 236 THR B N     1 
ATOM   5910  C  CA    . THR B 2 236 ? 176.564 165.173 180.907 1.00 18.27  ? 236 THR B CA    1 
ATOM   5911  C  C     . THR B 2 236 ? 177.544 164.021 180.722 1.00 19.34  ? 236 THR B C     1 
ATOM   5912  O  O     . THR B 2 236 ? 178.758 164.201 180.871 1.00 25.58  ? 236 THR B O     1 
ATOM   5913  C  CB    . THR B 2 236 ? 175.965 165.152 182.314 1.00 28.20  ? 236 THR B CB    1 
ATOM   5914  O  OG1   . THR B 2 236 ? 175.079 166.266 182.475 1.00 29.43  ? 236 THR B OG1   1 
ATOM   5915  C  CG2   . THR B 2 236 ? 177.060 165.233 183.363 1.00 26.82  ? 236 THR B CG2   1 
ATOM   5916  N  N     . ALA B 2 237 ? 177.035 162.830 180.398 1.00 25.28  ? 237 ALA B N     1 
ATOM   5917  C  CA    . ALA B 2 237 ? 177.913 161.687 180.168 1.00 25.06  ? 237 ALA B CA    1 
ATOM   5918  C  C     . ALA B 2 237 ? 178.804 161.908 178.953 1.00 26.91  ? 237 ALA B C     1 
ATOM   5919  O  O     . ALA B 2 237 ? 180.002 161.606 178.989 1.00 29.33  ? 237 ALA B O     1 
ATOM   5920  C  CB    . ALA B 2 237 ? 177.084 160.414 180.002 1.00 24.66  ? 237 ALA B CB    1 
ATOM   5921  N  N     . THR B 2 238 ? 178.239 162.439 177.866 1.00 24.85  ? 238 THR B N     1 
ATOM   5922  C  CA    . THR B 2 238 ? 179.016 162.694 176.660 1.00 23.39  ? 238 THR B CA    1 
ATOM   5923  C  C     . THR B 2 238 ? 179.982 163.859 176.819 1.00 25.74  ? 238 THR B C     1 
ATOM   5924  O  O     . THR B 2 238 ? 180.815 164.075 175.932 1.00 31.73  ? 238 THR B O     1 
ATOM   5925  C  CB    . THR B 2 238 ? 178.087 162.959 175.473 1.00 20.01  ? 238 THR B CB    1 
ATOM   5926  O  OG1   . THR B 2 238 ? 177.229 164.067 175.770 1.00 30.48  ? 238 THR B OG1   1 
ATOM   5927  C  CG2   . THR B 2 238 ? 177.241 161.730 175.174 1.00 17.04  ? 238 THR B CG2   1 
ATOM   5928  N  N     . LEU B 2 239 ? 179.886 164.616 177.914 1.00 22.96  ? 239 LEU B N     1 
ATOM   5929  C  CA    . LEU B 2 239 ? 180.821 165.709 178.145 1.00 24.97  ? 239 LEU B CA    1 
ATOM   5930  C  C     . LEU B 2 239 ? 182.232 165.197 178.409 1.00 25.31  ? 239 LEU B C     1 
ATOM   5931  O  O     . LEU B 2 239 ? 183.207 165.868 178.053 1.00 22.68  ? 239 LEU B O     1 
ATOM   5932  C  CB    . LEU B 2 239 ? 180.337 166.570 179.313 1.00 25.25  ? 239 LEU B CB    1 
ATOM   5933  C  CG    . LEU B 2 239 ? 180.794 168.028 179.347 1.00 28.31  ? 239 LEU B CG    1 
ATOM   5934  C  CD1   . LEU B 2 239 ? 180.628 168.674 177.980 1.00 22.27  ? 239 LEU B CD1   1 
ATOM   5935  C  CD2   . LEU B 2 239 ? 180.019 168.799 180.405 1.00 25.84  ? 239 LEU B CD2   1 
ATOM   5936  N  N     . TRP B 2 240 ? 182.361 164.027 179.037 1.00 23.72  ? 240 TRP B N     1 
ATOM   5937  C  CA    . TRP B 2 240 ? 183.688 163.481 179.319 1.00 21.29  ? 240 TRP B CA    1 
ATOM   5938  C  C     . TRP B 2 240 ? 184.495 163.200 178.056 1.00 22.38  ? 240 TRP B C     1 
ATOM   5939  O  O     . TRP B 2 240 ? 185.643 163.671 177.973 1.00 26.96  ? 240 TRP B O     1 
ATOM   5940  C  CB    . TRP B 2 240 ? 183.557 162.233 180.199 1.00 21.18  ? 240 TRP B CB    1 
ATOM   5941  C  CG    . TRP B 2 240 ? 184.858 161.775 180.783 1.00 28.58  ? 240 TRP B CG    1 
ATOM   5942  C  CD1   . TRP B 2 240 ? 185.364 162.095 182.008 1.00 26.79  ? 240 TRP B CD1   1 
ATOM   5943  C  CD2   . TRP B 2 240 ? 185.820 160.911 180.164 1.00 26.64  ? 240 TRP B CD2   1 
ATOM   5944  N  NE1   . TRP B 2 240 ? 186.581 161.486 182.191 1.00 33.39  ? 240 TRP B NE1   1 
ATOM   5945  C  CE2   . TRP B 2 240 ? 186.884 160.754 181.073 1.00 31.18  ? 240 TRP B CE2   1 
ATOM   5946  C  CE3   . TRP B 2 240 ? 185.885 160.257 178.930 1.00 27.63  ? 240 TRP B CE3   1 
ATOM   5947  C  CZ2   . TRP B 2 240 ? 187.999 159.969 180.788 1.00 27.87  ? 240 TRP B CZ2   1 
ATOM   5948  C  CZ3   . TRP B 2 240 ? 186.993 159.479 178.649 1.00 29.80  ? 240 TRP B CZ3   1 
ATOM   5949  C  CH2   . TRP B 2 240 ? 188.035 159.342 179.574 1.00 28.35  ? 240 TRP B CH2   1 
ATOM   5950  N  N     . PRO B 2 241 ? 183.995 162.462 177.056 1.00 27.33  ? 241 PRO B N     1 
ATOM   5951  C  CA    . PRO B 2 241 ? 184.775 162.329 175.815 1.00 20.58  ? 241 PRO B CA    1 
ATOM   5952  C  C     . PRO B 2 241 ? 184.928 163.639 175.065 1.00 21.34  ? 241 PRO B C     1 
ATOM   5953  O  O     . PRO B 2 241 ? 185.924 163.825 174.355 1.00 34.85  ? 241 PRO B O     1 
ATOM   5954  C  CB    . PRO B 2 241 ? 183.979 161.298 175.005 1.00 22.34  ? 241 PRO B CB    1 
ATOM   5955  C  CG    . PRO B 2 241 ? 182.598 161.406 175.515 1.00 27.53  ? 241 PRO B CG    1 
ATOM   5956  C  CD    . PRO B 2 241 ? 182.729 161.708 176.977 1.00 24.98  ? 241 PRO B CD    1 
ATOM   5957  N  N     . PHE B 2 242 ? 183.963 164.552 175.199 1.00 22.94  ? 242 PHE B N     1 
ATOM   5958  C  CA    . PHE B 2 242 ? 184.057 165.843 174.525 1.00 20.61  ? 242 PHE B CA    1 
ATOM   5959  C  C     . PHE B 2 242 ? 185.230 166.658 175.055 1.00 22.35  ? 242 PHE B C     1 
ATOM   5960  O  O     . PHE B 2 242 ? 185.998 167.234 174.275 1.00 30.53  ? 242 PHE B O     1 
ATOM   5961  C  CB    . PHE B 2 242 ? 182.749 166.615 174.697 1.00 19.61  ? 242 PHE B CB    1 
ATOM   5962  C  CG    . PHE B 2 242 ? 181.629 166.121 173.825 1.00 22.66  ? 242 PHE B CG    1 
ATOM   5963  C  CD1   . PHE B 2 242 ? 181.824 165.068 172.946 1.00 20.48  ? 242 PHE B CD1   1 
ATOM   5964  C  CD2   . PHE B 2 242 ? 180.372 166.698 173.901 1.00 14.71  ? 242 PHE B CD2   1 
ATOM   5965  C  CE1   . PHE B 2 242 ? 180.792 164.610 172.151 1.00 19.19  ? 242 PHE B CE1   1 
ATOM   5966  C  CE2   . PHE B 2 242 ? 179.336 166.244 173.109 1.00 22.05  ? 242 PHE B CE2   1 
ATOM   5967  C  CZ    . PHE B 2 242 ? 179.546 165.198 172.233 1.00 24.30  ? 242 PHE B CZ    1 
ATOM   5968  N  N     . SER B 2 243 ? 185.382 166.721 176.378 1.00 24.57  ? 243 SER B N     1 
ATOM   5969  C  CA    . SER B 2 243 ? 186.475 167.460 176.996 1.00 21.02  ? 243 SER B CA    1 
ATOM   5970  C  C     . SER B 2 243 ? 187.809 166.730 176.922 1.00 25.12  ? 243 SER B C     1 
ATOM   5971  O  O     . SER B 2 243 ? 188.855 167.384 176.983 1.00 32.13  ? 243 SER B O     1 
ATOM   5972  C  CB    . SER B 2 243 ? 186.143 167.763 178.460 1.00 22.02  ? 243 SER B CB    1 
ATOM   5973  O  OG    . SER B 2 243 ? 185.695 166.600 179.132 1.00 25.89  ? 243 SER B OG    1 
ATOM   5974  N  N     . ALA B 2 244 ? 187.799 165.400 176.801 1.00 29.87  ? 244 ALA B N     1 
ATOM   5975  C  CA    . ALA B 2 244 ? 189.041 164.638 176.792 1.00 23.71  ? 244 ALA B CA    1 
ATOM   5976  C  C     . ALA B 2 244 ? 189.894 164.921 175.564 1.00 29.38  ? 244 ALA B C     1 
ATOM   5977  O  O     . ALA B 2 244 ? 191.113 164.721 175.614 1.00 41.10  ? 244 ALA B O     1 
ATOM   5978  C  CB    . ALA B 2 244 ? 188.742 163.141 176.879 1.00 20.06  ? 244 ALA B CB    1 
ATOM   5979  N  N     . TRP B 2 245 ? 189.290 165.375 174.468 1.00 30.06  ? 245 TRP B N     1 
ATOM   5980  C  CA    . TRP B 2 245 ? 190.048 165.672 173.260 1.00 30.17  ? 245 TRP B CA    1 
ATOM   5981  C  C     . TRP B 2 245 ? 190.706 167.044 173.300 1.00 33.89  ? 245 TRP B C     1 
ATOM   5982  O  O     . TRP B 2 245 ? 191.792 167.218 172.734 1.00 41.10  ? 245 TRP B O     1 
ATOM   5983  C  CB    . TRP B 2 245 ? 189.142 165.573 172.030 1.00 34.46  ? 245 TRP B CB    1 
ATOM   5984  C  CG    . TRP B 2 245 ? 189.855 165.860 170.750 1.00 34.82  ? 245 TRP B CG    1 
ATOM   5985  C  CD1   . TRP B 2 245 ? 190.736 165.045 170.102 1.00 27.40  ? 245 TRP B CD1   1 
ATOM   5986  C  CD2   . TRP B 2 245 ? 189.757 167.051 169.964 1.00 25.65  ? 245 TRP B CD2   1 
ATOM   5987  N  NE1   . TRP B 2 245 ? 191.190 165.653 168.958 1.00 29.42  ? 245 TRP B NE1   1 
ATOM   5988  C  CE2   . TRP B 2 245 ? 190.603 166.886 168.850 1.00 27.31  ? 245 TRP B CE2   1 
ATOM   5989  C  CE3   . TRP B 2 245 ? 189.033 168.240 170.092 1.00 20.66  ? 245 TRP B CE3   1 
ATOM   5990  C  CZ2   . TRP B 2 245 ? 190.746 167.866 167.872 1.00 26.29  ? 245 TRP B CZ2   1 
ATOM   5991  C  CZ3   . TRP B 2 245 ? 189.175 169.208 169.122 1.00 24.61  ? 245 TRP B CZ3   1 
ATOM   5992  C  CH2   . TRP B 2 245 ? 190.025 169.016 168.025 1.00 29.86  ? 245 TRP B CH2   1 
ATOM   5993  N  N     . GLY B 2 246 ? 190.081 168.019 173.953 1.00 30.97  ? 246 GLY B N     1 
ATOM   5994  C  CA    . GLY B 2 246 ? 190.643 169.348 174.068 1.00 28.98  ? 246 GLY B CA    1 
ATOM   5995  C  C     . GLY B 2 246 ? 191.629 169.541 175.194 1.00 33.57  ? 246 GLY B C     1 
ATOM   5996  O  O     . GLY B 2 246 ? 192.115 170.657 175.397 1.00 34.57  ? 246 GLY B O     1 
ATOM   5997  N  N     . GLY B 2 247 ? 191.941 168.492 175.929 1.00 37.23  ? 247 GLY B N     1 
ATOM   5998  C  CA    . GLY B 2 247 ? 192.852 168.566 177.053 1.00 37.34  ? 247 GLY B CA    1 
ATOM   5999  C  C     . GLY B 2 247 ? 192.526 167.476 178.059 1.00 37.78  ? 247 GLY B C     1 
ATOM   6000  O  O     . GLY B 2 247 ? 192.059 166.400 177.691 1.00 41.65  ? 247 GLY B O     1 
ATOM   6001  N  N     . ASN B 2 248 ? 192.787 167.778 179.328 1.00 42.79  ? 248 ASN B N     1 
ATOM   6002  C  CA    . ASN B 2 248 ? 192.447 166.849 180.396 1.00 39.49  ? 248 ASN B CA    1 
ATOM   6003  C  C     . ASN B 2 248 ? 190.934 166.712 180.514 1.00 36.31  ? 248 ASN B C     1 
ATOM   6004  O  O     . ASN B 2 248 ? 190.195 167.696 180.420 1.00 37.70  ? 248 ASN B O     1 
ATOM   6005  C  CB    . ASN B 2 248 ? 193.040 167.321 181.723 1.00 42.26  ? 248 ASN B CB    1 
ATOM   6006  C  CG    . ASN B 2 248 ? 194.537 167.098 181.804 1.00 45.07  ? 248 ASN B CG    1 
ATOM   6007  O  OD1   . ASN B 2 248 ? 195.010 165.961 181.774 1.00 45.77  ? 248 ASN B OD1   1 
ATOM   6008  N  ND2   . ASN B 2 248 ? 195.293 168.185 181.908 1.00 41.68  ? 248 ASN B ND2   1 
ATOM   6009  N  N     . ALA B 2 249 ? 190.476 165.481 180.716 1.00 33.93  ? 249 ALA B N     1 
ATOM   6010  C  CA    . ALA B 2 249 ? 189.049 165.222 180.831 1.00 27.70  ? 249 ALA B CA    1 
ATOM   6011  C  C     . ALA B 2 249 ? 188.494 165.804 182.127 1.00 28.12  ? 249 ALA B C     1 
ATOM   6012  O  O     . ALA B 2 249 ? 189.180 165.871 183.150 1.00 39.48  ? 249 ALA B O     1 
ATOM   6013  C  CB    . ALA B 2 249 ? 188.772 163.721 180.769 1.00 26.56  ? 249 ALA B CB    1 
ATOM   6014  N  N     . VAL B 2 250 ? 187.233 166.235 182.069 1.00 28.17  ? 250 VAL B N     1 
ATOM   6015  C  CA    . VAL B 2 250 ? 186.564 166.759 183.252 1.00 26.71  ? 250 VAL B CA    1 
ATOM   6016  C  C     . VAL B 2 250 ? 186.386 165.641 184.271 1.00 28.77  ? 250 VAL B C     1 
ATOM   6017  O  O     . VAL B 2 250 ? 186.077 164.494 183.917 1.00 36.45  ? 250 VAL B O     1 
ATOM   6018  C  CB    . VAL B 2 250 ? 185.218 167.400 182.866 1.00 23.98  ? 250 VAL B CB    1 
ATOM   6019  C  CG1   . VAL B 2 250 ? 184.345 166.410 182.108 1.00 30.31  ? 250 VAL B CG1   1 
ATOM   6020  C  CG2   . VAL B 2 250 ? 184.496 167.934 184.096 1.00 27.35  ? 250 VAL B CG2   1 
ATOM   6021  N  N     . SER B 2 251 ? 186.603 165.964 185.543 1.00 24.80  ? 251 SER B N     1 
ATOM   6022  C  CA    . SER B 2 251 ? 186.534 164.962 186.596 1.00 27.69  ? 251 SER B CA    1 
ATOM   6023  C  C     . SER B 2 251 ? 185.117 164.416 186.735 1.00 25.78  ? 251 SER B C     1 
ATOM   6024  O  O     . SER B 2 251 ? 184.130 165.097 186.445 1.00 28.80  ? 251 SER B O     1 
ATOM   6025  C  CB    . SER B 2 251 ? 187.000 165.551 187.927 1.00 23.00  ? 251 SER B CB    1 
ATOM   6026  O  OG    . SER B 2 251 ? 185.956 166.261 188.566 1.00 28.50  ? 251 SER B OG    1 
ATOM   6027  N  N     . VAL B 2 252 ? 185.029 163.160 187.180 1.00 24.61  ? 252 VAL B N     1 
ATOM   6028  C  CA    . VAL B 2 252 ? 183.732 162.506 187.334 1.00 25.16  ? 252 VAL B CA    1 
ATOM   6029  C  C     . VAL B 2 252 ? 182.905 163.202 188.408 1.00 21.25  ? 252 VAL B C     1 
ATOM   6030  O  O     . VAL B 2 252 ? 181.679 163.317 188.290 1.00 30.97  ? 252 VAL B O     1 
ATOM   6031  C  CB    . VAL B 2 252 ? 183.926 161.010 187.645 1.00 26.56  ? 252 VAL B CB    1 
ATOM   6032  C  CG1   . VAL B 2 252 ? 182.583 160.315 187.797 1.00 24.79  ? 252 VAL B CG1   1 
ATOM   6033  C  CG2   . VAL B 2 252 ? 184.752 160.347 186.554 1.00 31.34  ? 252 VAL B CG2   1 
ATOM   6034  N  N     . THR B 2 253 ? 183.561 163.681 189.468 1.00 21.23  ? 253 THR B N     1 
ATOM   6035  C  CA    . THR B 2 253 ? 182.841 164.358 190.543 1.00 21.82  ? 253 THR B CA    1 
ATOM   6036  C  C     . THR B 2 253 ? 182.132 165.608 190.033 1.00 19.62  ? 253 THR B C     1 
ATOM   6037  O  O     . THR B 2 253 ? 180.984 165.876 190.407 1.00 26.91  ? 253 THR B O     1 
ATOM   6038  C  CB    . THR B 2 253 ? 183.805 164.713 191.677 1.00 23.51  ? 253 THR B CB    1 
ATOM   6039  O  OG1   . THR B 2 253 ? 184.373 163.514 192.217 1.00 34.32  ? 253 THR B OG1   1 
ATOM   6040  C  CG2   . THR B 2 253 ? 183.079 165.463 192.785 1.00 20.63  ? 253 THR B CG2   1 
ATOM   6041  N  N     . VAL B 2 254 ? 182.799 166.382 189.175 1.00 22.07  ? 254 VAL B N     1 
ATOM   6042  C  CA    . VAL B 2 254 ? 182.177 167.574 188.606 1.00 21.67  ? 254 VAL B CA    1 
ATOM   6043  C  C     . VAL B 2 254 ? 180.987 167.192 187.735 1.00 20.74  ? 254 VAL B C     1 
ATOM   6044  O  O     . VAL B 2 254 ? 179.930 167.834 187.785 1.00 23.43  ? 254 VAL B O     1 
ATOM   6045  C  CB    . VAL B 2 254 ? 183.218 168.395 187.821 1.00 22.91  ? 254 VAL B CB    1 
ATOM   6046  C  CG1   . VAL B 2 254 ? 182.537 169.461 186.976 1.00 19.53  ? 254 VAL B CG1   1 
ATOM   6047  C  CG2   . VAL B 2 254 ? 184.220 169.026 188.775 1.00 22.31  ? 254 VAL B CG2   1 
ATOM   6048  N  N     . LEU B 2 255 ? 181.136 166.140 186.926 1.00 21.06  ? 255 LEU B N     1 
ATOM   6049  C  CA    . LEU B 2 255 ? 180.045 165.708 186.057 1.00 18.69  ? 255 LEU B CA    1 
ATOM   6050  C  C     . LEU B 2 255 ? 178.834 165.260 186.865 1.00 19.41  ? 255 LEU B C     1 
ATOM   6051  O  O     . LEU B 2 255 ? 177.691 165.566 186.506 1.00 24.79  ? 255 LEU B O     1 
ATOM   6052  C  CB    . LEU B 2 255 ? 180.520 164.584 185.136 1.00 24.84  ? 255 LEU B CB    1 
ATOM   6053  C  CG    . LEU B 2 255 ? 181.431 164.991 183.978 1.00 23.41  ? 255 LEU B CG    1 
ATOM   6054  C  CD1   . LEU B 2 255 ? 181.808 163.780 183.141 1.00 21.54  ? 255 LEU B CD1   1 
ATOM   6055  C  CD2   . LEU B 2 255 ? 180.764 166.054 183.120 1.00 25.20  ? 255 LEU B CD2   1 
ATOM   6056  N  N     . VAL B 2 256 ? 179.063 164.526 187.957 1.00 22.25  ? 256 VAL B N     1 
ATOM   6057  C  CA    . VAL B 2 256 ? 177.956 164.110 188.814 1.00 22.42  ? 256 VAL B CA    1 
ATOM   6058  C  C     . VAL B 2 256 ? 177.273 165.327 189.425 1.00 21.93  ? 256 VAL B C     1 
ATOM   6059  O  O     . VAL B 2 256 ? 176.040 165.402 189.483 1.00 24.96  ? 256 VAL B O     1 
ATOM   6060  C  CB    . VAL B 2 256 ? 178.453 163.132 189.896 1.00 24.32  ? 256 VAL B CB    1 
ATOM   6061  C  CG1   . VAL B 2 256 ? 177.341 162.822 190.883 1.00 16.19  ? 256 VAL B CG1   1 
ATOM   6062  C  CG2   . VAL B 2 256 ? 178.968 161.853 189.257 1.00 25.09  ? 256 VAL B CG2   1 
ATOM   6063  N  N     . ALA B 2 257 ? 178.062 166.301 189.884 1.00 22.83  ? 257 ALA B N     1 
ATOM   6064  C  CA    . ALA B 2 257 ? 177.487 167.519 190.445 1.00 21.67  ? 257 ALA B CA    1 
ATOM   6065  C  C     . ALA B 2 257 ? 176.687 168.285 189.399 1.00 19.75  ? 257 ALA B C     1 
ATOM   6066  O  O     . ALA B 2 257 ? 175.625 168.841 189.703 1.00 26.67  ? 257 ALA B O     1 
ATOM   6067  C  CB    . ALA B 2 257 ? 178.591 168.399 191.029 1.00 6.75   ? 257 ALA B CB    1 
ATOM   6068  N  N     . LEU B 2 258 ? 177.185 168.330 188.161 1.00 12.94  ? 258 LEU B N     1 
ATOM   6069  C  CA    . LEU B 2 258 ? 176.459 169.007 187.091 1.00 20.01  ? 258 LEU B CA    1 
ATOM   6070  C  C     . LEU B 2 258 ? 175.131 168.319 186.794 1.00 21.06  ? 258 LEU B C     1 
ATOM   6071  O  O     . LEU B 2 258 ? 174.119 168.989 186.561 1.00 19.01  ? 258 LEU B O     1 
ATOM   6072  C  CB    . LEU B 2 258 ? 177.323 169.071 185.832 1.00 19.28  ? 258 LEU B CB    1 
ATOM   6073  C  CG    . LEU B 2 258 ? 176.695 169.731 184.601 1.00 26.45  ? 258 LEU B CG    1 
ATOM   6074  C  CD1   . LEU B 2 258 ? 176.408 171.202 184.856 1.00 13.47  ? 258 LEU B CD1   1 
ATOM   6075  C  CD2   . LEU B 2 258 ? 177.591 169.559 183.384 1.00 23.92  ? 258 LEU B CD2   1 
ATOM   6076  N  N     . LEU B 2 259 ? 175.117 166.983 186.792 1.00 18.92  ? 259 LEU B N     1 
ATOM   6077  C  CA    . LEU B 2 259 ? 173.898 166.256 186.452 1.00 15.76  ? 259 LEU B CA    1 
ATOM   6078  C  C     . LEU B 2 259 ? 172.796 166.503 187.475 1.00 17.80  ? 259 LEU B C     1 
ATOM   6079  O  O     . LEU B 2 259 ? 171.632 166.703 187.107 1.00 17.43  ? 259 LEU B O     1 
ATOM   6080  C  CB    . LEU B 2 259 ? 174.191 164.761 186.333 1.00 19.20  ? 259 LEU B CB    1 
ATOM   6081  C  CG    . LEU B 2 259 ? 172.982 163.883 186.006 1.00 17.40  ? 259 LEU B CG    1 
ATOM   6082  C  CD1   . LEU B 2 259 ? 172.378 164.290 184.674 1.00 21.99  ? 259 LEU B CD1   1 
ATOM   6083  C  CD2   . LEU B 2 259 ? 173.360 162.413 185.999 1.00 18.64  ? 259 LEU B CD2   1 
ATOM   6084  N  N     . VAL B 2 260 ? 173.141 166.493 188.765 1.00 24.67  ? 260 VAL B N     1 
ATOM   6085  C  CA    . VAL B 2 260 ? 172.144 166.723 189.808 1.00 15.75  ? 260 VAL B CA    1 
ATOM   6086  C  C     . VAL B 2 260 ? 171.572 168.131 189.705 1.00 20.66  ? 260 VAL B C     1 
ATOM   6087  O  O     . VAL B 2 260 ? 170.359 168.335 189.832 1.00 26.38  ? 260 VAL B O     1 
ATOM   6088  C  CB    . VAL B 2 260 ? 172.752 166.458 191.198 1.00 23.36  ? 260 VAL B CB    1 
ATOM   6089  C  CG1   . VAL B 2 260 ? 171.688 166.585 192.272 1.00 21.61  ? 260 VAL B CG1   1 
ATOM   6090  C  CG2   . VAL B 2 260 ? 173.379 165.075 191.240 1.00 22.96  ? 260 VAL B CG2   1 
ATOM   6091  N  N     . CYS B 2 261 ? 172.434 169.124 189.474 1.00 18.66  ? 261 CYS B N     1 
ATOM   6092  C  CA    . CYS B 2 261 ? 171.969 170.499 189.338 1.00 22.93  ? 261 CYS B CA    1 
ATOM   6093  C  C     . CYS B 2 261 ? 171.091 170.697 188.109 1.00 19.24  ? 261 CYS B C     1 
ATOM   6094  O  O     . CYS B 2 261 ? 170.280 171.628 188.085 1.00 22.44  ? 261 CYS B O     1 
ATOM   6095  C  CB    . CYS B 2 261 ? 173.163 171.454 189.280 1.00 20.62  ? 261 CYS B CB    1 
ATOM   6096  S  SG    . CYS B 2 261 ? 174.142 171.520 190.797 1.00 30.31  ? 261 CYS B SG    1 
ATOM   6097  N  N     . LEU B 2 262 ? 171.230 169.846 187.094 1.00 19.72  ? 262 LEU B N     1 
ATOM   6098  C  CA    . LEU B 2 262 ? 170.468 169.997 185.861 1.00 13.35  ? 262 LEU B CA    1 
ATOM   6099  C  C     . LEU B 2 262 ? 169.129 169.271 185.905 1.00 20.69  ? 262 LEU B C     1 
ATOM   6100  O  O     . LEU B 2 262 ? 168.119 169.816 185.449 1.00 26.48  ? 262 LEU B O     1 
ATOM   6101  C  CB    . LEU B 2 262 ? 171.291 169.495 184.672 1.00 17.58  ? 262 LEU B CB    1 
ATOM   6102  C  CG    . LEU B 2 262 ? 172.381 170.441 184.162 1.00 24.91  ? 262 LEU B CG    1 
ATOM   6103  C  CD1   . LEU B 2 262 ? 173.013 169.892 182.894 1.00 24.61  ? 262 LEU B CD1   1 
ATOM   6104  C  CD2   . LEU B 2 262 ? 171.824 171.837 183.929 1.00 18.66  ? 262 LEU B CD2   1 
ATOM   6105  N  N     . ILE B 2 263 ? 169.095 168.054 186.442 1.00 19.37  ? 263 ILE B N     1 
ATOM   6106  C  CA    . ILE B 2 263 ? 167.870 167.259 186.472 1.00 23.60  ? 263 ILE B CA    1 
ATOM   6107  C  C     . ILE B 2 263 ? 166.858 167.937 187.388 1.00 25.94  ? 263 ILE B C     1 
ATOM   6108  O  O     . ILE B 2 263 ? 167.249 168.590 188.366 1.00 29.28  ? 263 ILE B O     1 
ATOM   6109  C  CB    . ILE B 2 263 ? 168.148 165.813 186.915 1.00 19.97  ? 263 ILE B CB    1 
ATOM   6110  C  CG1   . ILE B 2 263 ? 168.819 165.786 188.289 1.00 23.16  ? 263 ILE B CG1   1 
ATOM   6111  C  CG2   . ILE B 2 263 ? 169.003 165.097 185.882 1.00 16.78  ? 263 ILE B CG2   1 
ATOM   6112  C  CD1   . ILE B 2 263 ? 169.125 164.393 188.790 1.00 17.88  ? 263 ILE B CD1   1 
ATOM   6113  N  N     . PRO B 2 264 ? 165.556 167.819 187.115 1.00 25.08  ? 264 PRO B N     1 
ATOM   6114  C  CA    . PRO B 2 264 ? 164.562 168.532 187.929 1.00 19.85  ? 264 PRO B CA    1 
ATOM   6115  C  C     . PRO B 2 264 ? 164.412 167.951 189.326 1.00 18.43  ? 264 PRO B C     1 
ATOM   6116  O  O     . PRO B 2 264 ? 163.428 167.266 189.622 1.00 22.63  ? 264 PRO B O     1 
ATOM   6117  C  CB    . PRO B 2 264 ? 163.272 168.378 187.114 1.00 24.18  ? 264 PRO B CB    1 
ATOM   6118  C  CG    . PRO B 2 264 ? 163.472 167.124 186.336 1.00 22.30  ? 264 PRO B CG    1 
ATOM   6119  C  CD    . PRO B 2 264 ? 164.934 167.082 186.000 1.00 23.88  ? 264 PRO B CD    1 
ATOM   6120  N  N     . THR B 2 265 ? 165.387 168.224 190.197 1.00 24.69  ? 265 THR B N     1 
ATOM   6121  C  CA    . THR B 2 265 ? 165.334 167.698 191.556 1.00 16.99  ? 265 THR B CA    1 
ATOM   6122  C  C     . THR B 2 265 ? 164.325 168.446 192.417 1.00 16.08  ? 265 THR B C     1 
ATOM   6123  O  O     . THR B 2 265 ? 163.779 167.872 193.366 1.00 25.75  ? 265 THR B O     1 
ATOM   6124  C  CB    . THR B 2 265 ? 166.718 167.761 192.203 1.00 21.35  ? 265 THR B CB    1 
ATOM   6125  O  OG1   . THR B 2 265 ? 167.284 169.062 192.001 1.00 26.05  ? 265 THR B OG1   1 
ATOM   6126  C  CG2   . THR B 2 265 ? 167.636 166.720 191.591 1.00 21.43  ? 265 THR B CG2   1 
ATOM   6127  N  N     . THR B 2 266 ? 164.071 169.721 192.114 1.00 16.99  ? 266 THR B N     1 
ATOM   6128  C  CA    . THR B 2 266 ? 163.161 170.511 192.938 1.00 23.69  ? 266 THR B CA    1 
ATOM   6129  C  C     . THR B 2 266 ? 161.734 169.983 192.846 1.00 21.77  ? 266 THR B C     1 
ATOM   6130  O  O     . THR B 2 266 ? 161.086 169.731 193.868 1.00 26.29  ? 266 THR B O     1 
ATOM   6131  C  CB    . THR B 2 266 ? 163.218 171.981 192.523 1.00 20.57  ? 266 THR B CB    1 
ATOM   6132  O  OG1   . THR B 2 266 ? 164.573 172.444 192.581 1.00 27.85  ? 266 THR B OG1   1 
ATOM   6133  C  CG2   . THR B 2 266 ? 162.360 172.827 193.449 1.00 26.57  ? 266 THR B CG2   1 
ATOM   6134  N  N     . ILE B 2 267 ? 161.228 169.804 191.624 1.00 16.26  ? 267 ILE B N     1 
ATOM   6135  C  CA    . ILE B 2 267 ? 159.883 169.261 191.459 1.00 15.25  ? 267 ILE B CA    1 
ATOM   6136  C  C     . ILE B 2 267 ? 159.876 167.761 191.734 1.00 17.46  ? 267 ILE B C     1 
ATOM   6137  O  O     . ILE B 2 267 ? 158.931 167.230 192.328 1.00 27.60  ? 267 ILE B O     1 
ATOM   6138  C  CB    . ILE B 2 267 ? 159.336 169.594 190.058 1.00 18.63  ? 267 ILE B CB    1 
ATOM   6139  C  CG1   . ILE B 2 267 ? 158.018 168.858 189.799 1.00 20.57  ? 267 ILE B CG1   1 
ATOM   6140  C  CG2   . ILE B 2 267 ? 160.356 169.260 188.983 1.00 14.08  ? 267 ILE B CG2   1 
ATOM   6141  C  CD1   . ILE B 2 267 ? 156.884 169.304 190.693 1.00 16.76  ? 267 ILE B CD1   1 
ATOM   6142  N  N     . GLY B 2 268 ? 160.932 167.058 191.318 1.00 16.23  ? 268 GLY B N     1 
ATOM   6143  C  CA    . GLY B 2 268 ? 160.984 165.620 191.531 1.00 23.53  ? 268 GLY B CA    1 
ATOM   6144  C  C     . GLY B 2 268 ? 160.986 165.241 192.999 1.00 23.48  ? 268 GLY B C     1 
ATOM   6145  O  O     . GLY B 2 268 ? 160.312 164.292 193.406 1.00 34.03  ? 268 GLY B O     1 
ATOM   6146  N  N     . GLY B 2 269 ? 161.746 165.975 193.815 1.00 20.62  ? 269 GLY B N     1 
ATOM   6147  C  CA    . GLY B 2 269 ? 161.763 165.714 195.243 1.00 21.65  ? 269 GLY B CA    1 
ATOM   6148  C  C     . GLY B 2 269 ? 160.533 166.190 195.983 1.00 20.89  ? 269 GLY B C     1 
ATOM   6149  O  O     . GLY B 2 269 ? 160.276 165.724 197.097 1.00 32.48  ? 269 GLY B O     1 
ATOM   6150  N  N     . LEU B 2 270 ? 159.766 167.106 195.391 1.00 21.30  ? 270 LEU B N     1 
ATOM   6151  C  CA    . LEU B 2 270 ? 158.569 167.645 196.018 1.00 24.03  ? 270 LEU B CA    1 
ATOM   6152  C  C     . LEU B 2 270 ? 157.275 167.106 195.425 1.00 25.59  ? 270 LEU B C     1 
ATOM   6153  O  O     . LEU B 2 270 ? 156.202 167.402 195.962 1.00 30.99  ? 270 LEU B O     1 
ATOM   6154  C  CB    . LEU B 2 270 ? 158.564 169.178 195.921 1.00 22.90  ? 270 LEU B CB    1 
ATOM   6155  C  CG    . LEU B 2 270 ? 159.559 169.931 196.806 1.00 25.61  ? 270 LEU B CG    1 
ATOM   6156  C  CD1   . LEU B 2 270 ? 159.442 171.431 196.590 1.00 24.32  ? 270 LEU B CD1   1 
ATOM   6157  C  CD2   . LEU B 2 270 ? 159.346 169.583 198.267 1.00 26.00  ? 270 LEU B CD2   1 
ATOM   6158  N  N     . LEU B 2 271 ? 157.344 166.326 194.343 1.00 24.19  ? 271 LEU B N     1 
ATOM   6159  C  CA    . LEU B 2 271 ? 156.130 165.865 193.676 1.00 26.56  ? 271 LEU B CA    1 
ATOM   6160  C  C     . LEU B 2 271 ? 155.295 164.971 194.584 1.00 32.13  ? 271 LEU B C     1 
ATOM   6161  O  O     . LEU B 2 271 ? 154.062 165.071 194.603 1.00 30.99  ? 271 LEU B O     1 
ATOM   6162  C  CB    . LEU B 2 271 ? 156.488 165.128 192.386 1.00 30.18  ? 271 LEU B CB    1 
ATOM   6163  C  CG    . LEU B 2 271 ? 155.319 164.687 191.504 1.00 29.73  ? 271 LEU B CG    1 
ATOM   6164  C  CD1   . LEU B 2 271 ? 154.483 165.885 191.083 1.00 31.81  ? 271 LEU B CD1   1 
ATOM   6165  C  CD2   . LEU B 2 271 ? 155.823 163.925 190.288 1.00 30.90  ? 271 LEU B CD2   1 
ATOM   6166  N  N     . SER B 2 272 ? 155.947 164.091 195.346 1.00 26.87  ? 272 SER B N     1 
ATOM   6167  C  CA    . SER B 2 272 ? 155.205 163.168 196.199 1.00 27.52  ? 272 SER B CA    1 
ATOM   6168  C  C     . SER B 2 272 ? 154.634 163.876 197.422 1.00 28.94  ? 272 SER B C     1 
ATOM   6169  O  O     . SER B 2 272 ? 153.833 163.295 198.162 1.00 32.23  ? 272 SER B O     1 
ATOM   6170  C  CB    . SER B 2 272 ? 156.102 162.006 196.622 1.00 30.58  ? 272 SER B CB    1 
ATOM   6171  O  OG    . SER B 2 272 ? 157.062 162.424 197.576 1.00 37.59  ? 272 SER B OG    1 
ATOM   6172  N  N     . ALA B 2 273 ? 155.030 165.129 197.652 1.00 32.08  ? 273 ALA B N     1 
ATOM   6173  C  CA    . ALA B 2 273 ? 154.524 165.853 198.811 1.00 24.16  ? 273 ALA B CA    1 
ATOM   6174  C  C     . ALA B 2 273 ? 153.353 166.756 198.446 1.00 29.55  ? 273 ALA B C     1 
ATOM   6175  O  O     . ALA B 2 273 ? 152.554 167.113 199.319 1.00 30.77  ? 273 ALA B O     1 
ATOM   6176  C  CB    . ALA B 2 273 ? 155.644 166.672 199.453 1.00 24.63  ? 273 ALA B CB    1 
ATOM   6177  N  N     . ILE B 2 274 ? 153.229 167.130 197.171 1.00 22.34  ? 274 ILE B N     1 
ATOM   6178  C  CA    . ILE B 2 274 ? 152.109 167.968 196.747 1.00 26.31  ? 274 ILE B CA    1 
ATOM   6179  C  C     . ILE B 2 274 ? 150.808 167.177 196.792 1.00 29.73  ? 274 ILE B C     1 
ATOM   6180  O  O     . ILE B 2 274 ? 149.765 167.684 197.221 1.00 27.91  ? 274 ILE B O     1 
ATOM   6181  C  CB    . ILE B 2 274 ? 152.371 168.549 195.346 1.00 30.19  ? 274 ILE B CB    1 
ATOM   6182  C  CG1   . ILE B 2 274 ? 153.715 169.280 195.312 1.00 25.13  ? 274 ILE B CG1   1 
ATOM   6183  C  CG2   . ILE B 2 274 ? 151.246 169.485 194.934 1.00 22.86  ? 274 ILE B CG2   1 
ATOM   6184  C  CD1   . ILE B 2 274 ? 154.338 169.352 193.935 1.00 25.72  ? 274 ILE B CD1   1 
ATOM   6185  N  N     . GLY B 2 275 ? 150.849 165.920 196.344 1.00 35.36  ? 275 GLY B N     1 
ATOM   6186  C  CA    . GLY B 2 275 ? 149.645 165.105 196.341 1.00 32.64  ? 275 GLY B CA    1 
ATOM   6187  C  C     . GLY B 2 275 ? 149.110 164.824 197.733 1.00 32.97  ? 275 GLY B C     1 
ATOM   6188  O  O     . GLY B 2 275 ? 147.905 164.930 197.975 1.00 35.95  ? 275 GLY B O     1 
ATOM   6189  N  N     . VAL B 2 276 ? 149.994 164.461 198.665 1.00 32.78  ? 276 VAL B N     1 
ATOM   6190  C  CA    . VAL B 2 276 ? 149.553 164.159 200.024 1.00 33.22  ? 276 VAL B CA    1 
ATOM   6191  C  C     . VAL B 2 276 ? 149.078 165.422 200.731 1.00 30.23  ? 276 VAL B C     1 
ATOM   6192  O  O     . VAL B 2 276 ? 148.087 165.399 201.470 1.00 32.65  ? 276 VAL B O     1 
ATOM   6193  C  CB    . VAL B 2 276 ? 150.675 163.455 200.809 1.00 31.24  ? 276 VAL B CB    1 
ATOM   6194  C  CG1   . VAL B 2 276 ? 150.115 162.800 202.057 1.00 28.99  ? 276 VAL B CG1   1 
ATOM   6195  C  CG2   . VAL B 2 276 ? 151.355 162.416 199.936 1.00 30.01  ? 276 VAL B CG2   1 
ATOM   6196  N  N     . ALA B 2 277 ? 149.776 166.542 200.523 1.00 33.75  ? 277 ALA B N     1 
ATOM   6197  C  CA    . ALA B 2 277 ? 149.361 167.797 201.141 1.00 29.22  ? 277 ALA B CA    1 
ATOM   6198  C  C     . ALA B 2 277 ? 148.005 168.257 200.625 1.00 35.71  ? 277 ALA B C     1 
ATOM   6199  O  O     . ALA B 2 277 ? 147.191 168.771 201.401 1.00 34.20  ? 277 ALA B O     1 
ATOM   6200  C  CB    . ALA B 2 277 ? 150.415 168.878 200.904 1.00 25.11  ? 277 ALA B CB    1 
ATOM   6201  N  N     . GLY B 2 278 ? 147.747 168.091 199.326 1.00 32.40  ? 278 GLY B N     1 
ATOM   6202  C  CA    . GLY B 2 278 ? 146.439 168.437 198.794 1.00 31.58  ? 278 GLY B CA    1 
ATOM   6203  C  C     . GLY B 2 278 ? 145.331 167.577 199.370 1.00 35.98  ? 278 GLY B C     1 
ATOM   6204  O  O     . GLY B 2 278 ? 144.237 168.067 199.658 1.00 36.47  ? 278 GLY B O     1 
ATOM   6205  N  N     . MET B 2 279 ? 145.599 166.280 199.546 1.00 35.70  ? 279 MET B N     1 
ATOM   6206  C  CA    . MET B 2 279 ? 144.620 165.403 200.177 1.00 32.33  ? 279 MET B CA    1 
ATOM   6207  C  C     . MET B 2 279 ? 144.416 165.758 201.644 1.00 38.09  ? 279 MET B C     1 
ATOM   6208  O  O     . MET B 2 279 ? 143.309 165.595 202.171 1.00 42.12  ? 279 MET B O     1 
ATOM   6209  C  CB    . MET B 2 279 ? 145.053 163.944 200.039 1.00 38.46  ? 279 MET B CB    1 
ATOM   6210  C  CG    . MET B 2 279 ? 144.666 163.244 198.728 1.00 42.89  ? 279 MET B CG    1 
ATOM   6211  S  SD    . MET B 2 279 ? 143.005 163.559 198.079 1.00 57.76  ? 279 MET B SD    1 
ATOM   6212  C  CE    . MET B 2 279 ? 143.255 165.015 197.061 1.00 41.66  ? 279 MET B CE    1 
ATOM   6213  N  N     . SER B 2 280 ? 145.464 166.240 202.316 1.00 38.76  ? 280 SER B N     1 
ATOM   6214  C  CA    . SER B 2 280 ? 145.323 166.642 203.711 1.00 35.12  ? 280 SER B CA    1 
ATOM   6215  C  C     . SER B 2 280 ? 144.523 167.933 203.834 1.00 37.63  ? 280 SER B C     1 
ATOM   6216  O  O     . SER B 2 280 ? 143.795 168.128 204.813 1.00 37.67  ? 280 SER B O     1 
ATOM   6217  C  CB    . SER B 2 280 ? 146.700 166.799 204.355 1.00 35.04  ? 280 SER B CB    1 
ATOM   6218  O  OG    . SER B 2 280 ? 147.277 165.537 204.637 1.00 47.24  ? 280 SER B OG    1 
ATOM   6219  N  N     . ARG B 2 281 ? 144.644 168.827 202.849 1.00 33.02  ? 281 ARG B N     1 
ATOM   6220  C  CA    . ARG B 2 281 ? 143.861 170.056 202.868 1.00 36.09  ? 281 ARG B CA    1 
ATOM   6221  C  C     . ARG B 2 281 ? 142.385 169.797 202.601 1.00 37.26  ? 281 ARG B C     1 
ATOM   6222  O  O     . ARG B 2 281 ? 141.544 170.615 202.991 1.00 39.64  ? 281 ARG B O     1 
ATOM   6223  C  CB    . ARG B 2 281 ? 144.421 171.053 201.851 1.00 33.42  ? 281 ARG B CB    1 
ATOM   6224  C  CG    . ARG B 2 281 ? 145.667 171.781 202.338 1.00 34.78  ? 281 ARG B CG    1 
ATOM   6225  C  CD    . ARG B 2 281 ? 146.033 172.957 201.445 1.00 30.10  ? 281 ARG B CD    1 
ATOM   6226  N  NE    . ARG B 2 281 ? 145.860 172.661 200.028 1.00 42.28  ? 281 ARG B NE    1 
ATOM   6227  C  CZ    . ARG B 2 281 ? 146.839 172.278 199.219 1.00 33.33  ? 281 ARG B CZ    1 
ATOM   6228  N  NH1   . ARG B 2 281 ? 148.075 172.116 199.659 1.00 33.36  ? 281 ARG B NH1   1 
ATOM   6229  N  NH2   . ARG B 2 281 ? 146.569 172.052 197.937 1.00 36.78  ? 281 ARG B NH2   1 
ATOM   6230  N  N     . MET B 2 282 ? 142.053 168.685 201.941 1.00 40.04  ? 282 MET B N     1 
ATOM   6231  C  CA    . MET B 2 282 ? 140.656 168.283 201.818 1.00 37.57  ? 282 MET B CA    1 
ATOM   6232  C  C     . MET B 2 282 ? 140.057 167.948 203.178 1.00 38.03  ? 282 MET B C     1 
ATOM   6233  O  O     . MET B 2 282 ? 138.918 168.329 203.474 1.00 43.81  ? 282 MET B O     1 
ATOM   6234  C  CB    . MET B 2 282 ? 140.536 167.087 200.875 1.00 38.76  ? 282 MET B CB    1 
ATOM   6235  C  CG    . MET B 2 282 ? 140.454 167.452 199.411 1.00 39.11  ? 282 MET B CG    1 
ATOM   6236  S  SD    . MET B 2 282 ? 138.896 168.271 199.032 1.00 52.26  ? 282 MET B SD    1 
ATOM   6237  C  CE    . MET B 2 282 ? 139.382 169.261 197.630 1.00 43.14  ? 282 MET B CE    1 
ATOM   6238  N  N     . LEU B 2 283 ? 140.808 167.229 204.016 1.00 42.60  ? 283 LEU B N     1 
ATOM   6239  C  CA    . LEU B 2 283 ? 140.315 166.889 205.347 1.00 42.05  ? 283 LEU B CA    1 
ATOM   6240  C  C     . LEU B 2 283 ? 140.121 168.137 206.197 1.00 44.60  ? 283 LEU B C     1 
ATOM   6241  O  O     . LEU B 2 283 ? 139.155 168.232 206.962 1.00 47.40  ? 283 LEU B O     1 
ATOM   6242  C  CB    . LEU B 2 283 ? 141.273 165.912 206.029 1.00 45.48  ? 283 LEU B CB    1 
ATOM   6243  C  CG    . LEU B 2 283 ? 140.723 165.167 207.248 1.00 48.95  ? 283 LEU B CG    1 
ATOM   6244  C  CD1   . LEU B 2 283 ? 139.256 164.815 207.055 1.00 47.49  ? 283 LEU B CD1   1 
ATOM   6245  C  CD2   . LEU B 2 283 ? 141.540 163.918 207.525 1.00 47.54  ? 283 LEU B CD2   1 
ATOM   6246  N  N     . GLY B 2 284 ? 141.032 169.105 206.079 1.00 40.89  ? 284 GLY B N     1 
ATOM   6247  C  CA    . GLY B 2 284 ? 140.861 170.369 206.771 1.00 41.73  ? 284 GLY B CA    1 
ATOM   6248  C  C     . GLY B 2 284 ? 139.670 171.167 206.287 1.00 42.24  ? 284 GLY B C     1 
ATOM   6249  O  O     . GLY B 2 284 ? 139.201 172.062 206.999 1.00 46.38  ? 284 GLY B O     1 
ATOM   6250  N  N     . ALA B 2 285 ? 139.168 170.865 205.091 1.00 46.52  ? 285 ALA B N     1 
ATOM   6251  C  CA    . ALA B 2 285 ? 137.976 171.499 204.548 1.00 43.93  ? 285 ALA B CA    1 
ATOM   6252  C  C     . ALA B 2 285 ? 136.722 170.664 204.769 1.00 43.89  ? 285 ALA B C     1 
ATOM   6253  O  O     . ALA B 2 285 ? 135.676 170.973 204.191 1.00 51.17  ? 285 ALA B O     1 
ATOM   6254  C  CB    . ALA B 2 285 ? 138.162 171.781 203.056 1.00 42.09  ? 285 ALA B CB    1 
ATOM   6255  N  N     . ASN B 2 286 ? 136.808 169.614 205.590 1.00 48.19  ? 286 ASN B N     1 
ATOM   6256  C  CA    . ASN B 2 286 ? 135.671 168.745 205.903 1.00 46.16  ? 286 ASN B CA    1 
ATOM   6257  C  C     . ASN B 2 286 ? 135.073 168.120 204.644 1.00 45.68  ? 286 ASN B C     1 
ATOM   6258  O  O     . ASN B 2 286 ? 133.854 168.022 204.495 1.00 51.68  ? 286 ASN B O     1 
ATOM   6259  C  CB    . ASN B 2 286 ? 134.601 169.498 206.697 1.00 46.27  ? 286 ASN B CB    1 
ATOM   6260  C  CG    . ASN B 2 286 ? 134.718 169.272 208.191 1.00 48.05  ? 286 ASN B CG    1 
ATOM   6261  O  OD1   . ASN B 2 286 ? 135.633 168.594 208.658 1.00 50.10  ? 286 ASN B OD1   1 
ATOM   6262  N  ND2   . ASN B 2 286 ? 133.788 169.839 208.950 1.00 52.25  ? 286 ASN B ND2   1 
ATOM   6263  N  N     . VAL B 2 287 ? 135.940 167.694 203.729 1.00 42.82  ? 287 VAL B N     1 
ATOM   6264  C  CA    . VAL B 2 287 ? 135.535 167.006 202.508 1.00 46.62  ? 287 VAL B CA    1 
ATOM   6265  C  C     . VAL B 2 287 ? 136.264 165.671 202.453 1.00 45.29  ? 287 VAL B C     1 
ATOM   6266  O  O     . VAL B 2 287 ? 137.493 165.624 202.578 1.00 48.89  ? 287 VAL B O     1 
ATOM   6267  C  CB    . VAL B 2 287 ? 135.833 167.846 201.253 1.00 46.56  ? 287 VAL B CB    1 
ATOM   6268  C  CG1   . VAL B 2 287 ? 135.508 167.054 199.996 1.00 45.12  ? 287 VAL B CG1   1 
ATOM   6269  C  CG2   . VAL B 2 287 ? 135.047 169.146 201.285 1.00 43.67  ? 287 VAL B CG2   1 
ATOM   6270  N  N     . ILE B 2 288 ? 135.508 164.592 202.270 1.00 49.34  ? 288 ILE B N     1 
ATOM   6271  C  CA    . ILE B 2 288 ? 136.051 163.240 202.212 1.00 49.02  ? 288 ILE B CA    1 
ATOM   6272  C  C     . ILE B 2 288 ? 135.988 162.780 200.763 1.00 50.48  ? 288 ILE B C     1 
ATOM   6273  O  O     . ILE B 2 288 ? 134.917 162.417 200.263 1.00 56.56  ? 288 ILE B O     1 
ATOM   6274  C  CB    . ILE B 2 288 ? 135.288 162.278 203.133 1.00 50.94  ? 288 ILE B CB    1 
ATOM   6275  C  CG1   . ILE B 2 288 ? 135.284 162.807 204.568 1.00 52.67  ? 288 ILE B CG1   1 
ATOM   6276  C  CG2   . ILE B 2 288 ? 135.902 160.888 203.078 1.00 53.38  ? 288 ILE B CG2   1 
ATOM   6277  C  CD1   . ILE B 2 288 ? 136.664 163.077 205.117 1.00 53.84  ? 288 ILE B CD1   1 
ATOM   6278  N  N     . ALA B 2 289 ? 137.134 162.785 200.089 1.00 51.09  ? 289 ALA B N     1 
ATOM   6279  C  CA    . ALA B 2 289 ? 137.221 162.403 198.688 1.00 55.66  ? 289 ALA B CA    1 
ATOM   6280  C  C     . ALA B 2 289 ? 137.711 160.967 198.562 1.00 56.41  ? 289 ALA B C     1 
ATOM   6281  O  O     . ALA B 2 289 ? 138.625 160.546 199.277 1.00 58.11  ? 289 ALA B O     1 
ATOM   6282  C  CB    . ALA B 2 289 ? 138.157 163.342 197.924 1.00 54.19  ? 289 ALA B CB    1 
ATOM   6283  N  N     . THR B 2 290 ? 137.090 160.215 197.650 1.00 55.68  ? 290 THR B N     1 
ATOM   6284  C  CA    . THR B 2 290 ? 137.492 158.828 197.438 1.00 57.08  ? 290 THR B CA    1 
ATOM   6285  C  C     . THR B 2 290 ? 138.916 158.739 196.901 1.00 59.88  ? 290 THR B C     1 
ATOM   6286  O  O     . THR B 2 290 ? 139.702 157.892 197.342 1.00 61.29  ? 290 THR B O     1 
ATOM   6287  C  CB    . THR B 2 290 ? 136.514 158.139 196.485 1.00 57.36  ? 290 THR B CB    1 
ATOM   6288  O  OG1   . THR B 2 290 ? 135.204 158.132 197.064 1.00 60.05  ? 290 THR B OG1   1 
ATOM   6289  C  CG2   . THR B 2 290 ? 136.947 156.705 196.217 1.00 57.89  ? 290 THR B CG2   1 
ATOM   6290  N  N     . SER B 2 291 ? 139.270 159.611 195.959 1.00 53.75  ? 291 SER B N     1 
ATOM   6291  C  CA    . SER B 2 291 ? 140.593 159.586 195.355 1.00 53.15  ? 291 SER B CA    1 
ATOM   6292  C  C     . SER B 2 291 ? 140.956 160.986 194.883 1.00 53.15  ? 291 SER B C     1 
ATOM   6293  O  O     . SER B 2 291 ? 140.087 161.819 194.616 1.00 54.49  ? 291 SER B O     1 
ATOM   6294  C  CB    . SER B 2 291 ? 140.661 158.595 194.186 1.00 55.93  ? 291 SER B CB    1 
ATOM   6295  O  OG    . SER B 2 291 ? 139.769 158.968 193.150 1.00 57.64  ? 291 SER B OG    1 
ATOM   6296  N  N     . GLY B 2 292 ? 142.264 161.235 194.789 1.00 43.65  ? 292 GLY B N     1 
ATOM   6297  C  CA    . GLY B 2 292 ? 142.750 162.517 194.309 1.00 40.17  ? 292 GLY B CA    1 
ATOM   6298  C  C     . GLY B 2 292 ? 142.407 162.809 192.864 1.00 41.58  ? 292 GLY B C     1 
ATOM   6299  O  O     . GLY B 2 292 ? 142.387 163.979 192.468 1.00 44.26  ? 292 GLY B O     1 
ATOM   6300  N  N     . ARG B 2 293 ? 142.143 161.772 192.065 1.00 47.13  ? 293 ARG B N     1 
ATOM   6301  C  CA    . ARG B 2 293 ? 141.797 161.981 190.662 1.00 50.46  ? 293 ARG B CA    1 
ATOM   6302  C  C     . ARG B 2 293 ? 140.495 162.760 190.523 1.00 47.49  ? 293 ARG B C     1 
ATOM   6303  O  O     . ARG B 2 293 ? 140.382 163.642 189.663 1.00 50.35  ? 293 ARG B O     1 
ATOM   6304  C  CB    . ARG B 2 293 ? 141.702 160.636 189.942 1.00 48.74  ? 293 ARG B CB    1 
ATOM   6305  C  CG    . ARG B 2 293 ? 141.318 160.736 188.475 1.00 46.69  ? 293 ARG B CG    1 
ATOM   6306  C  CD    . ARG B 2 293 ? 140.533 159.513 188.027 1.00 50.81  ? 293 ARG B CD    1 
ATOM   6307  N  NE    . ARG B 2 293 ? 141.404 158.459 187.520 1.00 52.45  ? 293 ARG B NE    1 
ATOM   6308  C  CZ    . ARG B 2 293 ? 141.481 158.097 186.247 1.00 53.99  ? 293 ARG B CZ    1 
ATOM   6309  N  NH1   . ARG B 2 293 ? 140.750 158.687 185.316 1.00 51.04  ? 293 ARG B NH1   1 
ATOM   6310  N  NH2   . ARG B 2 293 ? 142.312 157.118 185.900 1.00 52.16  ? 293 ARG B NH2   1 
ATOM   6311  N  N     . ALA B 2 294 ? 139.501 162.449 191.358 1.00 44.60  ? 294 ALA B N     1 
ATOM   6312  C  CA    . ALA B 2 294 ? 138.240 163.183 191.313 1.00 45.91  ? 294 ALA B CA    1 
ATOM   6313  C  C     . ALA B 2 294 ? 138.428 164.631 191.748 1.00 44.01  ? 294 ALA B C     1 
ATOM   6314  O  O     . ALA B 2 294 ? 137.741 165.529 191.248 1.00 46.86  ? 294 ALA B O     1 
ATOM   6315  C  CB    . ALA B 2 294 ? 137.196 162.489 192.187 1.00 45.12  ? 294 ALA B CB    1 
ATOM   6316  N  N     . VAL B 2 295 ? 139.346 164.874 192.685 1.00 42.81  ? 295 VAL B N     1 
ATOM   6317  C  CA    . VAL B 2 295 ? 139.624 166.240 193.122 1.00 44.56  ? 295 VAL B CA    1 
ATOM   6318  C  C     . VAL B 2 295 ? 140.204 167.061 191.979 1.00 41.24  ? 295 VAL B C     1 
ATOM   6319  O  O     . VAL B 2 295 ? 139.813 168.215 191.762 1.00 44.20  ? 295 VAL B O     1 
ATOM   6320  C  CB    . VAL B 2 295 ? 140.563 166.228 194.342 1.00 44.50  ? 295 VAL B CB    1 
ATOM   6321  C  CG1   . VAL B 2 295 ? 140.839 167.645 194.808 1.00 41.08  ? 295 VAL B CG1   1 
ATOM   6322  C  CG2   . VAL B 2 295 ? 139.957 165.405 195.464 1.00 42.02  ? 295 VAL B CG2   1 
ATOM   6323  N  N     . GLU B 2 296 ? 141.145 166.483 191.231 1.00 42.51  ? 296 GLU B N     1 
ATOM   6324  C  CA    . GLU B 2 296 ? 141.758 167.210 190.124 1.00 43.27  ? 296 GLU B CA    1 
ATOM   6325  C  C     . GLU B 2 296 ? 140.771 167.440 188.987 1.00 45.02  ? 296 GLU B C     1 
ATOM   6326  O  O     . GLU B 2 296 ? 140.960 168.357 188.181 1.00 48.23  ? 296 GLU B O     1 
ATOM   6327  C  CB    . GLU B 2 296 ? 142.987 166.456 189.622 1.00 43.95  ? 296 GLU B CB    1 
ATOM   6328  C  CG    . GLU B 2 296 ? 144.217 166.642 190.493 1.00 46.42  ? 296 GLU B CG    1 
ATOM   6329  C  CD    . GLU B 2 296 ? 145.297 165.623 190.199 1.00 49.61  ? 296 GLU B CD    1 
ATOM   6330  O  OE1   . GLU B 2 296 ? 145.417 165.201 189.030 1.00 49.41  ? 296 GLU B OE1   1 
ATOM   6331  O  OE2   . GLU B 2 296 ? 146.027 165.243 191.138 1.00 48.09  ? 296 GLU B OE2   1 
ATOM   6332  N  N     . ALA B 2 297 ? 139.718 166.624 188.906 1.00 46.27  ? 297 ALA B N     1 
ATOM   6333  C  CA    . ALA B 2 297 ? 138.688 166.834 187.897 1.00 46.01  ? 297 ALA B CA    1 
ATOM   6334  C  C     . ALA B 2 297 ? 137.816 168.043 188.206 1.00 44.29  ? 297 ALA B C     1 
ATOM   6335  O  O     . ALA B 2 297 ? 137.146 168.555 187.304 1.00 49.19  ? 297 ALA B O     1 
ATOM   6336  C  CB    . ALA B 2 297 ? 137.818 165.584 187.763 1.00 44.88  ? 297 ALA B CB    1 
ATOM   6337  N  N     . ALA B 2 298 ? 137.812 168.510 189.457 1.00 43.07  ? 298 ALA B N     1 
ATOM   6338  C  CA    . ALA B 2 298 ? 137.023 169.677 189.830 1.00 42.29  ? 298 ALA B CA    1 
ATOM   6339  C  C     . ALA B 2 298 ? 137.597 170.977 189.285 1.00 45.32  ? 298 ALA B C     1 
ATOM   6340  O  O     . ALA B 2 298 ? 136.920 172.008 189.355 1.00 47.60  ? 298 ALA B O     1 
ATOM   6341  C  CB    . ALA B 2 298 ? 136.903 169.765 191.352 1.00 41.74  ? 298 ALA B CB    1 
ATOM   6342  N  N     . GLY B 2 299 ? 138.815 170.960 188.754 1.00 44.25  ? 299 GLY B N     1 
ATOM   6343  C  CA    . GLY B 2 299 ? 139.384 172.140 188.141 1.00 40.78  ? 299 GLY B CA    1 
ATOM   6344  C  C     . GLY B 2 299 ? 138.925 172.412 186.730 1.00 42.50  ? 299 GLY B C     1 
ATOM   6345  O  O     . GLY B 2 299 ? 139.311 173.429 186.146 1.00 45.43  ? 299 GLY B O     1 
ATOM   6346  N  N     . ASP B 2 300 ? 138.105 171.529 186.161 1.00 47.84  ? 300 ASP B N     1 
ATOM   6347  C  CA    . ASP B 2 300 ? 137.613 171.683 184.801 1.00 46.21  ? 300 ASP B CA    1 
ATOM   6348  C  C     . ASP B 2 300 ? 136.094 171.741 184.711 1.00 47.23  ? 300 ASP B C     1 
ATOM   6349  O  O     . ASP B 2 300 ? 135.562 171.841 183.599 1.00 50.68  ? 300 ASP B O     1 
ATOM   6350  C  CB    . ASP B 2 300 ? 138.128 170.537 183.918 1.00 45.43  ? 300 ASP B CB    1 
ATOM   6351  C  CG    . ASP B 2 300 ? 139.509 170.808 183.358 1.00 49.27  ? 300 ASP B CG    1 
ATOM   6352  O  OD1   . ASP B 2 300 ? 140.493 170.689 184.118 1.00 50.96  ? 300 ASP B OD1   1 
ATOM   6353  O  OD2   . ASP B 2 300 ? 139.612 171.140 182.159 1.00 49.44  ? 300 ASP B OD2   1 
ATOM   6354  N  N     . VAL B 2 301 ? 135.381 171.678 185.836 1.00 47.83  ? 301 VAL B N     1 
ATOM   6355  C  CA    . VAL B 2 301 ? 133.925 171.684 185.795 1.00 50.64  ? 301 VAL B CA    1 
ATOM   6356  C  C     . VAL B 2 301 ? 133.426 173.068 185.403 1.00 50.01  ? 301 VAL B C     1 
ATOM   6357  O  O     . VAL B 2 301 ? 133.939 174.094 185.871 1.00 52.30  ? 301 VAL B O     1 
ATOM   6358  C  CB    . VAL B 2 301 ? 133.339 171.241 187.148 1.00 47.58  ? 301 VAL B CB    1 
ATOM   6359  C  CG1   . VAL B 2 301 ? 133.584 169.758 187.371 1.00 49.32  ? 301 VAL B CG1   1 
ATOM   6360  C  CG2   . VAL B 2 301 ? 133.924 172.061 188.285 1.00 50.47  ? 301 VAL B CG2   1 
ATOM   6361  N  N     . ASP B 2 302 ? 132.420 173.102 184.527 1.00 55.82  ? 302 ASP B N     1 
ATOM   6362  C  CA    . ASP B 2 302 ? 131.834 174.351 184.066 1.00 57.22  ? 302 ASP B CA    1 
ATOM   6363  C  C     . ASP B 2 302 ? 130.394 174.557 184.506 1.00 56.59  ? 302 ASP B C     1 
ATOM   6364  O  O     . ASP B 2 302 ? 129.918 175.697 184.469 1.00 57.32  ? 302 ASP B O     1 
ATOM   6365  C  CB    . ASP B 2 302 ? 131.897 174.440 182.532 1.00 56.77  ? 302 ASP B CB    1 
ATOM   6366  C  CG    . ASP B 2 302 ? 133.268 174.100 181.986 1.00 62.20  ? 302 ASP B CG    1 
ATOM   6367  O  OD1   . ASP B 2 302 ? 134.224 174.853 182.270 1.00 62.06  ? 302 ASP B OD1   1 
ATOM   6368  O  OD2   . ASP B 2 302 ? 133.393 173.080 181.274 1.00 59.48  ? 302 ASP B OD2   1 
ATOM   6369  N  N     . VAL B 2 303 ? 129.692 173.504 184.918 1.00 57.17  ? 303 VAL B N     1 
ATOM   6370  C  CA    . VAL B 2 303 ? 128.312 173.601 185.376 1.00 57.92  ? 303 VAL B CA    1 
ATOM   6371  C  C     . VAL B 2 303 ? 128.176 172.817 186.675 1.00 56.85  ? 303 VAL B C     1 
ATOM   6372  O  O     . VAL B 2 303 ? 128.782 171.750 186.831 1.00 56.60  ? 303 VAL B O     1 
ATOM   6373  C  CB    . VAL B 2 303 ? 127.313 173.098 184.312 1.00 54.88  ? 303 VAL B CB    1 
ATOM   6374  C  CG1   . VAL B 2 303 ? 127.371 171.582 184.165 1.00 55.86  ? 303 VAL B CG1   1 
ATOM   6375  C  CG2   . VAL B 2 303 ? 125.900 173.555 184.651 1.00 56.25  ? 303 VAL B CG2   1 
ATOM   6376  N  N     . LEU B 2 304 ? 127.423 173.369 187.622 1.00 50.99  ? 304 LEU B N     1 
ATOM   6377  C  CA    . LEU B 2 304 ? 127.146 172.720 188.895 1.00 50.79  ? 304 LEU B CA    1 
ATOM   6378  C  C     . LEU B 2 304 ? 125.648 172.475 189.023 1.00 52.22  ? 304 LEU B C     1 
ATOM   6379  O  O     . LEU B 2 304 ? 124.848 173.403 188.863 1.00 54.53  ? 304 LEU B O     1 
ATOM   6380  C  CB    . LEU B 2 304 ? 127.649 173.570 190.064 1.00 52.18  ? 304 LEU B CB    1 
ATOM   6381  C  CG    . LEU B 2 304 ? 127.153 173.196 191.463 1.00 49.91  ? 304 LEU B CG    1 
ATOM   6382  C  CD1   . LEU B 2 304 ? 127.645 171.815 191.863 1.00 49.74  ? 304 LEU B CD1   1 
ATOM   6383  C  CD2   . LEU B 2 304 ? 127.588 174.237 192.483 1.00 50.50  ? 304 LEU B CD2   1 
ATOM   6384  N  N     . LEU B 2 305 ? 125.275 171.232 189.311 1.00 54.77  ? 305 LEU B N     1 
ATOM   6385  C  CA    . LEU B 2 305 ? 123.881 170.854 189.502 1.00 55.11  ? 305 LEU B CA    1 
ATOM   6386  C  C     . LEU B 2 305 ? 123.608 170.670 190.988 1.00 55.07  ? 305 LEU B C     1 
ATOM   6387  O  O     . LEU B 2 305 ? 124.311 169.911 191.664 1.00 58.97  ? 305 LEU B O     1 
ATOM   6388  C  CB    . LEU B 2 305 ? 123.552 169.569 188.740 1.00 56.97  ? 305 LEU B CB    1 
ATOM   6389  C  CG    . LEU B 2 305 ? 123.742 169.575 187.221 1.00 59.35  ? 305 LEU B CG    1 
ATOM   6390  C  CD1   . LEU B 2 305 ? 122.945 168.449 186.586 1.00 58.08  ? 305 LEU B CD1   1 
ATOM   6391  C  CD2   . LEU B 2 305 ? 123.344 170.912 186.621 1.00 56.12  ? 305 LEU B CD2   1 
ATOM   6392  N  N     . LEU B 2 306 ? 122.590 171.359 191.491 1.00 55.20  ? 306 LEU B N     1 
ATOM   6393  C  CA    . LEU B 2 306 ? 122.270 171.312 192.913 1.00 59.02  ? 306 LEU B CA    1 
ATOM   6394  C  C     . LEU B 2 306 ? 120.829 170.888 193.163 1.00 58.33  ? 306 LEU B C     1 
ATOM   6395  O  O     . LEU B 2 306 ? 119.918 171.285 192.438 1.00 63.20  ? 306 LEU B O     1 
ATOM   6396  C  CB    . LEU B 2 306 ? 122.526 172.674 193.562 1.00 58.22  ? 306 LEU B CB    1 
ATOM   6397  C  CG    . LEU B 2 306 ? 123.871 173.343 193.278 1.00 59.18  ? 306 LEU B CG    1 
ATOM   6398  C  CD1   . LEU B 2 306 ? 123.707 174.477 192.277 1.00 58.36  ? 306 LEU B CD1   1 
ATOM   6399  C  CD2   . LEU B 2 306 ? 124.498 173.847 194.567 1.00 59.92  ? 306 LEU B CD2   1 
HETATM 6400  N  N     . PHD B 2 307 ? 120.632 170.077 194.197 1.00 65.76  ? 307 PHD B N     1 
HETATM 6401  C  CA    . PHD B 2 307 ? 119.301 169.694 194.625 1.00 65.23  ? 307 PHD B CA    1 
HETATM 6402  C  C     . PHD B 2 307 ? 118.710 170.839 195.499 1.00 66.08  ? 307 PHD B C     1 
HETATM 6403  O  O     . PHD B 2 307 ? 119.488 171.632 196.112 1.00 70.33  ? 307 PHD B O     1 
HETATM 6404  C  CB    . PHD B 2 307 ? 119.264 168.383 195.425 1.00 65.38  ? 307 PHD B CB    1 
HETATM 6405  C  CG    . PHD B 2 307 ? 117.900 167.855 195.819 1.00 69.08  ? 307 PHD B CG    1 
HETATM 6406  O  OD1   . PHD B 2 307 ? 117.684 166.576 195.655 1.00 70.56  ? 307 PHD B OD1   1 
HETATM 6407  O  OD2   . PHD B 2 307 ? 116.967 168.542 196.285 1.00 73.29  ? 307 PHD B OD2   1 
HETATM 6408  P  P     . PHD B 2 307 ? 117.095 165.666 197.069 1.00 75.53  ? 307 PHD B P     1 
HETATM 6409  O  OP1   . PHD B 2 307 ? 117.110 164.235 196.618 1.00 71.07  ? 307 PHD B OP1   1 
HETATM 6410  O  OP2   . PHD B 2 307 ? 118.236 166.025 197.988 1.00 66.17  ? 307 PHD B OP2   1 
HETATM 6411  O  OP3   . PHD B 2 307 ? 115.788 166.289 197.464 1.00 69.61  ? 307 PHD B OP3   1 
ATOM   6412  N  N     . LYS B 2 308 ? 117.386 170.931 195.559 1.00 65.15  ? 308 LYS B N     1 
ATOM   6413  C  CA    . LYS B 2 308 ? 116.735 171.965 196.353 1.00 66.56  ? 308 LYS B CA    1 
ATOM   6414  C  C     . LYS B 2 308 ? 116.569 171.526 197.804 1.00 66.77  ? 308 LYS B C     1 
ATOM   6415  O  O     . LYS B 2 308 ? 117.292 171.988 198.687 1.00 68.47  ? 308 LYS B O     1 
ATOM   6416  C  CB    . LYS B 2 308 ? 115.373 172.325 195.757 1.00 66.09  ? 308 LYS B CB    1 
ATOM   6417  C  CG    . LYS B 2 308 ? 114.843 173.676 196.208 1.00 66.58  ? 308 LYS B CG    1 
ATOM   6418  C  CD    . LYS B 2 308 ? 113.651 173.524 197.135 1.00 69.03  ? 308 LYS B CD    1 
ATOM   6419  C  CE    . LYS B 2 308 ? 112.444 172.974 196.396 1.00 67.40  ? 308 LYS B CE    1 
ATOM   6420  N  NZ    . LYS B 2 308 ? 111.298 172.739 197.316 1.00 68.68  ? 308 LYS B NZ    1 
ATOM   6421  N  N     . THR B 2 309 ? 115.612 170.634 198.045 1.00 65.55  ? 309 THR B N     1 
ATOM   6422  C  CA    . THR B 2 309 ? 115.334 170.153 199.392 1.00 65.90  ? 309 THR B CA    1 
ATOM   6423  C  C     . THR B 2 309 ? 116.474 169.258 199.862 1.00 65.74  ? 309 THR B C     1 
ATOM   6424  O  O     . THR B 2 309 ? 116.878 168.331 199.152 1.00 66.18  ? 309 THR B O     1 
ATOM   6425  C  CB    . THR B 2 309 ? 114.008 169.397 199.428 1.00 65.91  ? 309 THR B CB    1 
ATOM   6426  O  OG1   . THR B 2 309 ? 112.988 170.187 198.804 1.00 67.62  ? 309 THR B OG1   1 
ATOM   6427  C  CG2   . THR B 2 309 ? 113.602 169.102 200.865 1.00 65.68  ? 309 THR B CG2   1 
ATOM   6428  N  N     . GLY B 2 310 ? 116.992 169.534 201.058 1.00 63.41  ? 310 GLY B N     1 
ATOM   6429  C  CA    . GLY B 2 310 ? 118.077 168.771 201.626 1.00 64.90  ? 310 GLY B CA    1 
ATOM   6430  C  C     . GLY B 2 310 ? 119.460 169.322 201.351 1.00 64.55  ? 310 GLY B C     1 
ATOM   6431  O  O     . GLY B 2 310 ? 120.326 169.247 202.229 1.00 65.02  ? 310 GLY B O     1 
ATOM   6432  N  N     . THR B 2 311 ? 119.654 169.886 200.154 1.00 62.34  ? 311 THR B N     1 
ATOM   6433  C  CA    . THR B 2 311 ? 120.979 170.445 199.769 1.00 62.56  ? 311 THR B CA    1 
ATOM   6434  C  C     . THR B 2 311 ? 120.953 171.972 199.905 1.00 61.96  ? 311 THR B C     1 
ATOM   6435  O  O     . THR B 2 311 ? 121.680 172.494 200.770 1.00 65.68  ? 311 THR B O     1 
ATOM   6436  C  CB    . THR B 2 311 ? 121.368 170.005 198.352 1.00 61.14  ? 311 THR B CB    1 
ATOM   6437  O  OG1   . THR B 2 311 ? 121.291 168.580 198.295 1.00 62.04  ? 311 THR B OG1   1 
ATOM   6438  C  CG2   . THR B 2 311 ? 122.756 170.458 197.956 1.00 61.35  ? 311 THR B CG2   1 
ATOM   6439  N  N     . ILE B 2 312 ? 120.154 172.654 199.078 1.00 31.32  ? 312 ILE B N     1 
ATOM   6440  C  CA    . ILE B 2 312 ? 120.055 174.144 199.139 1.00 37.33  ? 312 ILE B CA    1 
ATOM   6441  C  C     . ILE B 2 312 ? 119.291 174.529 200.409 1.00 43.53  ? 312 ILE B C     1 
ATOM   6442  O  O     . ILE B 2 312 ? 119.809 175.365 201.174 1.00 60.10  ? 312 ILE B O     1 
ATOM   6443  C  CB    . ILE B 2 312 ? 119.388 174.699 197.864 1.00 26.94  ? 312 ILE B CB    1 
ATOM   6444  C  CG1   . ILE B 2 312 ? 120.330 174.623 196.660 1.00 33.15  ? 312 ILE B CG1   1 
ATOM   6445  C  CG2   . ILE B 2 312 ? 118.870 176.112 198.089 1.00 35.65  ? 312 ILE B CG2   1 
ATOM   6446  C  CD1   . ILE B 2 312 ? 120.351 175.873 195.813 1.00 47.86  ? 312 ILE B CD1   1 
ATOM   6447  N  N     . THR B 2 313 ? 118.109 173.943 200.622 1.00 45.73  ? 313 THR B N     1 
ATOM   6448  C  CA    . THR B 2 313 ? 117.338 174.207 201.825 1.00 44.86  ? 313 THR B CA    1 
ATOM   6449  C  C     . THR B 2 313 ? 117.675 173.169 202.886 1.00 52.54  ? 313 THR B C     1 
ATOM   6450  O  O     . THR B 2 313 ? 118.235 172.111 202.588 1.00 55.29  ? 313 THR B O     1 
ATOM   6451  C  CB    . THR B 2 313 ? 115.834 174.188 201.538 1.00 47.52  ? 313 THR B CB    1 
ATOM   6452  O  OG1   . THR B 2 313 ? 115.427 172.858 201.197 1.00 53.91  ? 313 THR B OG1   1 
ATOM   6453  C  CG2   . THR B 2 313 ? 115.500 175.123 200.389 1.00 53.06  ? 313 THR B CG2   1 
ATOM   6454  N  N     . LEU B 2 314 ? 117.324 173.481 204.133 1.00 63.45  ? 314 LEU B N     1 
ATOM   6455  C  CA    . LEU B 2 314 ? 117.613 172.578 205.240 1.00 60.92  ? 314 LEU B CA    1 
ATOM   6456  C  C     . LEU B 2 314 ? 116.752 171.324 205.221 1.00 55.60  ? 314 LEU B C     1 
ATOM   6457  O  O     . LEU B 2 314 ? 117.013 170.406 206.005 1.00 60.79  ? 314 LEU B O     1 
ATOM   6458  C  CB    . LEU B 2 314 ? 117.430 173.306 206.573 1.00 59.95  ? 314 LEU B CB    1 
ATOM   6459  C  CG    . LEU B 2 314 ? 118.461 174.386 206.898 1.00 71.75  ? 314 LEU B CG    1 
ATOM   6460  C  CD1   . LEU B 2 314 ? 117.921 175.348 207.943 1.00 73.62  ? 314 LEU B CD1   1 
ATOM   6461  C  CD2   . LEU B 2 314 ? 119.764 173.759 207.367 1.00 68.89  ? 314 LEU B CD2   1 
ATOM   6462  N  N     . GLY B 2 315 ? 115.744 171.259 204.356 1.00 50.36  ? 315 GLY B N     1 
ATOM   6463  C  CA    . GLY B 2 315 ? 114.832 170.140 204.402 1.00 53.63  ? 315 GLY B CA    1 
ATOM   6464  C  C     . GLY B 2 315 ? 113.889 170.282 205.585 1.00 59.04  ? 315 GLY B C     1 
ATOM   6465  O  O     . GLY B 2 315 ? 113.665 171.375 206.115 1.00 76.57  ? 315 GLY B O     1 
ATOM   6466  N  N     . ASN B 2 316 ? 113.340 169.143 206.004 1.00 59.64  ? 316 ASN B N     1 
ATOM   6467  C  CA    . ASN B 2 316 ? 112.422 169.085 207.140 1.00 69.88  ? 316 ASN B CA    1 
ATOM   6468  C  C     . ASN B 2 316 ? 111.268 170.067 206.957 1.00 71.16  ? 316 ASN B C     1 
ATOM   6469  O  O     . ASN B 2 316 ? 110.993 170.914 207.809 1.00 72.49  ? 316 ASN B O     1 
ATOM   6470  C  CB    . ASN B 2 316 ? 113.164 169.345 208.453 1.00 67.39  ? 316 ASN B CB    1 
ATOM   6471  C  CG    . ASN B 2 316 ? 112.462 168.739 209.649 1.00 79.39  ? 316 ASN B CG    1 
ATOM   6472  O  OD1   . ASN B 2 316 ? 112.166 167.545 209.670 1.00 83.96  ? 316 ASN B OD1   1 
ATOM   6473  N  ND2   . ASN B 2 316 ? 112.192 169.562 210.655 1.00 79.68  ? 316 ASN B ND2   1 
ATOM   6474  N  N     . ARG B 2 317 ? 110.597 169.954 205.813 1.00 73.36  ? 317 ARG B N     1 
ATOM   6475  C  CA    . ARG B 2 317 ? 109.510 170.865 205.478 1.00 71.25  ? 317 ARG B CA    1 
ATOM   6476  C  C     . ARG B 2 317 ? 108.372 170.728 206.479 1.00 71.92  ? 317 ARG B C     1 
ATOM   6477  O  O     . ARG B 2 317 ? 107.837 169.634 206.681 1.00 77.99  ? 317 ARG B O     1 
ATOM   6478  C  CB    . ARG B 2 317 ? 109.015 170.585 204.061 1.00 67.43  ? 317 ARG B CB    1 
ATOM   6479  C  CG    . ARG B 2 317 ? 109.769 171.345 202.985 1.00 67.48  ? 317 ARG B CG    1 
ATOM   6480  C  CD    . ARG B 2 317 ? 109.255 171.005 201.599 1.00 70.98  ? 317 ARG B CD    1 
ATOM   6481  N  NE    . ARG B 2 317 ? 109.434 169.595 201.280 1.00 65.78  ? 317 ARG B NE    1 
ATOM   6482  C  CZ    . ARG B 2 317 ? 109.583 169.119 200.052 1.00 68.23  ? 317 ARG B CZ    1 
ATOM   6483  N  NH1   . ARG B 2 317 ? 109.582 169.916 198.997 1.00 68.44  ? 317 ARG B NH1   1 
ATOM   6484  N  NH2   . ARG B 2 317 ? 109.740 167.810 199.878 1.00 66.93  ? 317 ARG B NH2   1 
ATOM   6485  N  N     . GLN B 2 318 ? 108.006 171.842 207.105 1.00 77.48  ? 318 GLN B N     1 
ATOM   6486  C  CA    . GLN B 2 318 ? 106.963 171.876 208.120 1.00 78.76  ? 318 GLN B CA    1 
ATOM   6487  C  C     . GLN B 2 318 ? 105.742 172.598 207.569 1.00 83.08  ? 318 GLN B C     1 
ATOM   6488  O  O     . GLN B 2 318 ? 105.865 173.691 207.005 1.00 85.93  ? 318 GLN B O     1 
ATOM   6489  C  CB    . GLN B 2 318 ? 107.457 172.570 209.390 1.00 79.20  ? 318 GLN B CB    1 
ATOM   6490  C  CG    . GLN B 2 318 ? 108.745 171.996 209.956 1.00 82.78  ? 318 GLN B CG    1 
ATOM   6491  C  CD    . GLN B 2 318 ? 108.527 170.698 210.708 1.00 86.03  ? 318 GLN B CD    1 
ATOM   6492  O  OE1   . GLN B 2 318 ? 108.327 169.644 210.106 1.00 91.91  ? 318 GLN B OE1   1 
ATOM   6493  N  NE2   . GLN B 2 318 ? 108.565 170.770 212.033 1.00 82.84  ? 318 GLN B NE2   1 
ATOM   6494  N  N     . ALA B 2 319 ? 104.573 171.986 207.729 1.00 77.25  ? 319 ALA B N     1 
ATOM   6495  C  CA    . ALA B 2 319 ? 103.334 172.626 207.313 1.00 73.75  ? 319 ALA B CA    1 
ATOM   6496  C  C     . ALA B 2 319 ? 103.050 173.843 208.183 1.00 79.82  ? 319 ALA B C     1 
ATOM   6497  O  O     . ALA B 2 319 ? 103.238 173.813 209.402 1.00 85.60  ? 319 ALA B O     1 
ATOM   6498  C  CB    . ALA B 2 319 ? 102.172 171.638 207.390 1.00 74.10  ? 319 ALA B CB    1 
ATOM   6499  N  N     . SER B 2 320 ? 102.594 174.921 207.549 1.00 91.31  ? 320 SER B N     1 
ATOM   6500  C  CA    . SER B 2 320 ? 102.344 176.182 208.234 1.00 94.20  ? 320 SER B CA    1 
ATOM   6501  C  C     . SER B 2 320 ? 100.863 176.473 208.422 1.00 97.04  ? 320 SER B C     1 
ATOM   6502  O  O     . SER B 2 320 ? 100.425 176.749 209.543 1.00 100.63 ? 320 SER B O     1 
ATOM   6503  C  CB    . SER B 2 320 ? 103.004 177.335 207.465 1.00 93.87  ? 320 SER B CB    1 
ATOM   6504  O  OG    . SER B 2 320 ? 102.301 177.618 206.269 1.00 97.97  ? 320 SER B OG    1 
ATOM   6505  N  N     . GLU B 2 321 ? 100.075 176.419 207.351 1.00 107.33 ? 321 GLU B N     1 
ATOM   6506  C  CA    . GLU B 2 321 ? 98.659  176.743 207.424 1.00 109.17 ? 321 GLU B CA    1 
ATOM   6507  C  C     . GLU B 2 321 ? 97.862  175.757 206.584 1.00 111.14 ? 321 GLU B C     1 
ATOM   6508  O  O     . GLU B 2 321 ? 98.373  175.176 205.623 1.00 108.96 ? 321 GLU B O     1 
ATOM   6509  C  CB    . GLU B 2 321 ? 98.384  178.175 206.947 1.00 109.78 ? 321 GLU B CB    1 
ATOM   6510  C  CG    . GLU B 2 321 ? 99.042  178.522 205.623 1.00 111.88 ? 321 GLU B CG    1 
ATOM   6511  C  CD    . GLU B 2 321 ? 98.923  179.993 205.281 1.00 114.52 ? 321 GLU B CD    1 
ATOM   6512  O  OE1   . GLU B 2 321 ? 98.153  180.702 205.962 1.00 114.82 ? 321 GLU B OE1   1 
ATOM   6513  O  OE2   . GLU B 2 321 ? 99.599  180.441 204.331 1.00 112.81 ? 321 GLU B OE2   1 
ATOM   6514  N  N     . PHE B 2 322 ? 96.599  175.576 206.962 1.00 110.95 ? 322 PHE B N     1 
ATOM   6515  C  CA    . PHE B 2 322 ? 95.663  174.727 206.230 1.00 109.36 ? 322 PHE B CA    1 
ATOM   6516  C  C     . PHE B 2 322 ? 94.740  175.639 205.429 1.00 113.30 ? 322 PHE B C     1 
ATOM   6517  O  O     . PHE B 2 322 ? 93.805  176.228 205.975 1.00 114.33 ? 322 PHE B O     1 
ATOM   6518  C  CB    . PHE B 2 322 ? 94.874  173.837 207.185 1.00 108.57 ? 322 PHE B CB    1 
ATOM   6519  C  CG    . PHE B 2 322 ? 95.581  172.566 207.554 1.00 111.24 ? 322 PHE B CG    1 
ATOM   6520  C  CD1   . PHE B 2 322 ? 95.797  171.578 206.608 1.00 112.44 ? 322 PHE B CD1   1 
ATOM   6521  C  CD2   . PHE B 2 322 ? 96.025  172.356 208.848 1.00 112.61 ? 322 PHE B CD2   1 
ATOM   6522  C  CE1   . PHE B 2 322 ? 96.444  170.406 206.945 1.00 109.91 ? 322 PHE B CE1   1 
ATOM   6523  C  CE2   . PHE B 2 322 ? 96.674  171.186 209.191 1.00 113.62 ? 322 PHE B CE2   1 
ATOM   6524  C  CZ    . PHE B 2 322 ? 96.884  170.210 208.238 1.00 111.49 ? 322 PHE B CZ    1 
ATOM   6525  N  N     . ILE B 2 323 ? 95.007  175.755 204.131 1.00 106.35 ? 323 ILE B N     1 
ATOM   6526  C  CA    . ILE B 2 323 ? 94.203  176.587 203.237 1.00 103.34 ? 323 ILE B CA    1 
ATOM   6527  C  C     . ILE B 2 323 ? 93.112  175.702 202.639 1.00 105.17 ? 323 ILE B C     1 
ATOM   6528  O  O     . ILE B 2 323 ? 93.431  174.793 201.854 1.00 101.43 ? 323 ILE B O     1 
ATOM   6529  C  CB    . ILE B 2 323 ? 95.062  177.225 202.139 1.00 99.99  ? 323 ILE B CB    1 
ATOM   6530  C  CG1   . ILE B 2 323 ? 96.196  178.043 202.760 1.00 100.56 ? 323 ILE B CG1   1 
ATOM   6531  C  CG2   . ILE B 2 323 ? 94.206  178.097 201.237 1.00 101.28 ? 323 ILE B CG2   1 
ATOM   6532  C  CD1   . ILE B 2 323 ? 95.721  179.143 203.682 1.00 100.67 ? 323 ILE B CD1   1 
ATOM   6533  N  N     . PRO B 2 324 ? 91.842  175.924 202.968 1.00 117.82 ? 324 PRO B N     1 
ATOM   6534  C  CA    . PRO B 2 324 ? 90.775  175.066 202.452 1.00 115.18 ? 324 PRO B CA    1 
ATOM   6535  C  C     . PRO B 2 324 ? 90.186  175.579 201.148 1.00 112.91 ? 324 PRO B C     1 
ATOM   6536  O  O     . PRO B 2 324 ? 90.202  176.773 200.844 1.00 114.10 ? 324 PRO B O     1 
ATOM   6537  C  CB    . PRO B 2 324 ? 89.734  175.117 203.578 1.00 115.31 ? 324 PRO B CB    1 
ATOM   6538  C  CG    . PRO B 2 324 ? 89.891  176.495 204.145 1.00 115.17 ? 324 PRO B CG    1 
ATOM   6539  C  CD    . PRO B 2 324 ? 91.335  176.911 203.938 1.00 115.43 ? 324 PRO B CD    1 
ATOM   6540  N  N     . ALA B 2 325 ? 89.657  174.638 200.371 1.00 116.10 ? 325 ALA B N     1 
ATOM   6541  C  CA    . ALA B 2 325 ? 88.986  174.980 199.129 1.00 117.89 ? 325 ALA B CA    1 
ATOM   6542  C  C     . ALA B 2 325 ? 87.607  175.570 199.418 1.00 124.83 ? 325 ALA B C     1 
ATOM   6543  O  O     . ALA B 2 325 ? 87.095  175.513 200.540 1.00 128.66 ? 325 ALA B O     1 
ATOM   6544  C  CB    . ALA B 2 325 ? 88.863  173.752 198.230 1.00 116.96 ? 325 ALA B CB    1 
ATOM   6545  N  N     . GLN B 2 326 ? 87.007  176.154 198.383 1.00 132.34 ? 326 GLN B N     1 
ATOM   6546  C  CA    . GLN B 2 326 ? 85.671  176.720 198.518 1.00 130.48 ? 326 GLN B CA    1 
ATOM   6547  C  C     . GLN B 2 326 ? 84.664  175.627 198.849 1.00 129.73 ? 326 GLN B C     1 
ATOM   6548  O  O     . GLN B 2 326 ? 84.656  174.561 198.227 1.00 128.65 ? 326 GLN B O     1 
ATOM   6549  C  CB    . GLN B 2 326 ? 85.270  177.443 197.233 1.00 129.04 ? 326 GLN B CB    1 
ATOM   6550  C  CG    . GLN B 2 326 ? 84.285  178.601 197.415 1.00 130.73 ? 326 GLN B CG    1 
ATOM   6551  C  CD    . GLN B 2 326 ? 84.705  179.599 198.486 1.00 133.32 ? 326 GLN B CD    1 
ATOM   6552  O  OE1   . GLN B 2 326 ? 84.593  179.336 199.684 1.00 131.87 ? 326 GLN B OE1   1 
ATOM   6553  N  NE2   . GLN B 2 326 ? 85.191  180.756 198.051 1.00 131.96 ? 326 GLN B NE2   1 
ATOM   6554  N  N     . GLY B 2 327 ? 83.811  175.896 199.835 1.00 130.05 ? 327 GLY B N     1 
ATOM   6555  C  CA    . GLY B 2 327 ? 82.846  174.923 200.297 1.00 131.39 ? 327 GLY B CA    1 
ATOM   6556  C  C     . GLY B 2 327 ? 83.374  173.921 201.299 1.00 133.67 ? 327 GLY B C     1 
ATOM   6557  O  O     . GLY B 2 327 ? 82.612  173.047 201.733 1.00 134.06 ? 327 GLY B O     1 
ATOM   6558  N  N     . VAL B 2 328 ? 84.646  174.012 201.679 1.00 124.55 ? 328 VAL B N     1 
ATOM   6559  C  CA    . VAL B 2 328 ? 85.255  173.116 202.653 1.00 121.78 ? 328 VAL B CA    1 
ATOM   6560  C  C     . VAL B 2 328 ? 85.803  173.957 203.796 1.00 122.13 ? 328 VAL B C     1 
ATOM   6561  O  O     . VAL B 2 328 ? 86.514  174.941 203.562 1.00 122.46 ? 328 VAL B O     1 
ATOM   6562  C  CB    . VAL B 2 328 ? 86.370  172.260 202.025 1.00 124.39 ? 328 VAL B CB    1 
ATOM   6563  C  CG1   . VAL B 2 328 ? 86.862  171.219 203.019 1.00 123.60 ? 328 VAL B CG1   1 
ATOM   6564  C  CG2   . VAL B 2 328 ? 85.882  171.596 200.749 1.00 125.23 ? 328 VAL B CG2   1 
ATOM   6565  N  N     . ASP B 2 329 ? 85.468  173.575 205.024 1.00 135.48 ? 329 ASP B N     1 
ATOM   6566  C  CA    . ASP B 2 329 ? 85.982  174.266 206.194 1.00 137.50 ? 329 ASP B CA    1 
ATOM   6567  C  C     . ASP B 2 329 ? 87.364  173.730 206.566 1.00 139.33 ? 329 ASP B C     1 
ATOM   6568  O  O     . ASP B 2 329 ? 87.804  172.677 206.095 1.00 139.06 ? 329 ASP B O     1 
ATOM   6569  C  CB    . ASP B 2 329 ? 85.014  174.124 207.368 1.00 137.59 ? 329 ASP B CB    1 
ATOM   6570  C  CG    . ASP B 2 329 ? 84.648  172.681 207.649 1.00 139.69 ? 329 ASP B CG    1 
ATOM   6571  O  OD1   . ASP B 2 329 ? 85.501  171.939 208.179 1.00 141.16 ? 329 ASP B OD1   1 
ATOM   6572  O  OD2   . ASP B 2 329 ? 83.504  172.286 207.339 1.00 140.07 ? 329 ASP B OD2   1 
ATOM   6573  N  N     . GLU B 2 330 ? 88.056  174.479 207.427 1.00 139.15 ? 330 GLU B N     1 
ATOM   6574  C  CA    . GLU B 2 330 ? 89.386  174.068 207.864 1.00 136.58 ? 330 GLU B CA    1 
ATOM   6575  C  C     . GLU B 2 330 ? 89.331  172.775 208.668 1.00 138.05 ? 330 GLU B C     1 
ATOM   6576  O  O     . GLU B 2 330 ? 90.267  171.968 208.620 1.00 138.21 ? 330 GLU B O     1 
ATOM   6577  C  CB    . GLU B 2 330 ? 90.037  175.182 208.683 1.00 136.96 ? 330 GLU B CB    1 
ATOM   6578  C  CG    . GLU B 2 330 ? 91.555  175.117 208.724 1.00 140.12 ? 330 GLU B CG    1 
ATOM   6579  C  CD    . GLU B 2 330 ? 92.162  176.225 209.563 1.00 141.80 ? 330 GLU B CD    1 
ATOM   6580  O  OE1   . GLU B 2 330 ? 91.931  177.409 209.243 1.00 140.92 ? 330 GLU B OE1   1 
ATOM   6581  O  OE2   . GLU B 2 330 ? 92.871  175.910 210.542 1.00 141.56 ? 330 GLU B OE2   1 
ATOM   6582  N  N     . LYS B 2 331 ? 88.247  172.566 209.418 1.00 138.41 ? 331 LYS B N     1 
ATOM   6583  C  CA    . LYS B 2 331 ? 88.106  171.341 210.199 1.00 137.68 ? 331 LYS B CA    1 
ATOM   6584  C  C     . LYS B 2 331 ? 88.058  170.115 209.295 1.00 136.89 ? 331 LYS B C     1 
ATOM   6585  O  O     . LYS B 2 331 ? 88.699  169.097 209.582 1.00 137.54 ? 331 LYS B O     1 
ATOM   6586  C  CB    . LYS B 2 331 ? 86.851  171.427 211.071 1.00 134.96 ? 331 LYS B CB    1 
ATOM   6587  C  CG    . LYS B 2 331 ? 86.333  170.100 211.611 1.00 135.80 ? 331 LYS B CG    1 
ATOM   6588  C  CD    . LYS B 2 331 ? 87.345  169.414 212.515 1.00 137.45 ? 331 LYS B CD    1 
ATOM   6589  C  CE    . LYS B 2 331 ? 87.306  167.905 212.336 1.00 137.28 ? 331 LYS B CE    1 
ATOM   6590  N  NZ    . LYS B 2 331 ? 87.860  167.478 211.023 1.00 137.24 ? 331 LYS B NZ    1 
ATOM   6591  N  N     . THR B 2 332 ? 87.310  170.195 208.192 1.00 126.08 ? 332 THR B N     1 
ATOM   6592  C  CA    . THR B 2 332 ? 87.234  169.068 207.268 1.00 125.94 ? 332 THR B CA    1 
ATOM   6593  C  C     . THR B 2 332 ? 88.572  168.825 206.580 1.00 125.61 ? 332 THR B C     1 
ATOM   6594  O  O     . THR B 2 332 ? 88.936  167.675 206.306 1.00 127.99 ? 332 THR B O     1 
ATOM   6595  C  CB    . THR B 2 332 ? 86.135  169.309 206.233 1.00 128.19 ? 332 THR B CB    1 
ATOM   6596  O  OG1   . THR B 2 332 ? 84.931  169.710 206.897 1.00 132.53 ? 332 THR B OG1   1 
ATOM   6597  C  CG2   . THR B 2 332 ? 85.865  168.041 205.435 1.00 127.07 ? 332 THR B CG2   1 
ATOM   6598  N  N     . LEU B 2 333 ? 89.314  169.896 206.290 1.00 116.00 ? 333 LEU B N     1 
ATOM   6599  C  CA    . LEU B 2 333 ? 90.599  169.749 205.613 1.00 119.16 ? 333 LEU B CA    1 
ATOM   6600  C  C     . LEU B 2 333 ? 91.591  168.965 206.463 1.00 121.87 ? 333 LEU B C     1 
ATOM   6601  O  O     . LEU B 2 333 ? 92.329  168.117 205.946 1.00 120.62 ? 333 LEU B O     1 
ATOM   6602  C  CB    . LEU B 2 333 ? 91.165  171.124 205.263 1.00 118.85 ? 333 LEU B CB    1 
ATOM   6603  C  CG    . LEU B 2 333 ? 92.399  171.128 204.361 1.00 116.68 ? 333 LEU B CG    1 
ATOM   6604  C  CD1   . LEU B 2 333 ? 92.047  170.592 202.986 1.00 115.58 ? 333 LEU B CD1   1 
ATOM   6605  C  CD2   . LEU B 2 333 ? 92.989  172.525 204.260 1.00 118.58 ? 333 LEU B CD2   1 
ATOM   6606  N  N     . ALA B 2 334 ? 91.625  169.236 207.769 1.00 130.28 ? 334 ALA B N     1 
ATOM   6607  C  CA    . ALA B 2 334 ? 92.585  168.565 208.641 1.00 127.18 ? 334 ALA B CA    1 
ATOM   6608  C  C     . ALA B 2 334 ? 92.291  167.075 208.755 1.00 128.42 ? 334 ALA B C     1 
ATOM   6609  O  O     . ALA B 2 334 ? 93.218  166.260 208.839 1.00 130.17 ? 334 ALA B O     1 
ATOM   6610  C  CB    . ALA B 2 334 ? 92.585  169.218 210.022 1.00 125.85 ? 334 ALA B CB    1 
ATOM   6611  N  N     . ASP B 2 335 ? 91.009  166.699 208.770 1.00 128.63 ? 335 ASP B N     1 
ATOM   6612  C  CA    . ASP B 2 335 ? 90.654  165.290 208.909 1.00 129.33 ? 335 ASP B CA    1 
ATOM   6613  C  C     . ASP B 2 335 ? 91.183  164.467 207.742 1.00 129.88 ? 335 ASP B C     1 
ATOM   6614  O  O     . ASP B 2 335 ? 91.713  163.368 207.938 1.00 130.65 ? 335 ASP B O     1 
ATOM   6615  C  CB    . ASP B 2 335 ? 89.138  165.140 209.027 1.00 131.53 ? 335 ASP B CB    1 
ATOM   6616  C  CG    . ASP B 2 335 ? 88.693  163.692 209.005 1.00 134.67 ? 335 ASP B CG    1 
ATOM   6617  O  OD1   . ASP B 2 335 ? 89.123  162.923 209.890 1.00 135.01 ? 335 ASP B OD1   1 
ATOM   6618  O  OD2   . ASP B 2 335 ? 87.913  163.322 208.102 1.00 136.47 ? 335 ASP B OD2   1 
ATOM   6619  N  N     . ALA B 2 336 ? 91.046  164.982 206.518 1.00 123.77 ? 336 ALA B N     1 
ATOM   6620  C  CA    . ALA B 2 336 ? 91.603  164.286 205.364 1.00 126.06 ? 336 ALA B CA    1 
ATOM   6621  C  C     . ALA B 2 336 ? 93.126  164.306 205.392 1.00 130.47 ? 336 ALA B C     1 
ATOM   6622  O  O     . ALA B 2 336 ? 93.773  163.326 205.004 1.00 131.16 ? 336 ALA B O     1 
ATOM   6623  C  CB    . ALA B 2 336 ? 91.081  164.910 204.071 1.00 126.99 ? 336 ALA B CB    1 
ATOM   6624  N  N     . ALA B 2 337 ? 93.714  165.416 205.842 1.00 124.09 ? 337 ALA B N     1 
ATOM   6625  C  CA    . ALA B 2 337 ? 95.168  165.510 205.915 1.00 120.48 ? 337 ALA B CA    1 
ATOM   6626  C  C     . ALA B 2 337 ? 95.738  164.517 206.920 1.00 118.26 ? 337 ALA B C     1 
ATOM   6627  O  O     . ALA B 2 337 ? 96.776  163.894 206.667 1.00 119.23 ? 337 ALA B O     1 
ATOM   6628  C  CB    . ALA B 2 337 ? 95.582  166.937 206.273 1.00 118.05 ? 337 ALA B CB    1 
ATOM   6629  N  N     . GLN B 2 338 ? 95.076  164.361 208.070 1.00 115.73 ? 338 GLN B N     1 
ATOM   6630  C  CA    . GLN B 2 338 ? 95.554  163.419 209.077 1.00 115.17 ? 338 GLN B CA    1 
ATOM   6631  C  C     . GLN B 2 338 ? 95.509  161.986 208.563 1.00 115.84 ? 338 GLN B C     1 
ATOM   6632  O  O     . GLN B 2 338 ? 96.431  161.201 208.813 1.00 120.99 ? 338 GLN B O     1 
ATOM   6633  C  CB    . GLN B 2 338 ? 94.729  163.548 210.357 1.00 116.43 ? 338 GLN B CB    1 
ATOM   6634  C  CG    . GLN B 2 338 ? 95.095  164.736 211.224 1.00 116.94 ? 338 GLN B CG    1 
ATOM   6635  C  CD    . GLN B 2 338 ? 95.010  164.417 212.703 1.00 123.12 ? 338 GLN B CD    1 
ATOM   6636  O  OE1   . GLN B 2 338 ? 95.121  163.259 213.106 1.00 124.64 ? 338 GLN B OE1   1 
ATOM   6637  N  NE2   . GLN B 2 338 ? 94.811  165.443 213.521 1.00 124.04 ? 338 GLN B NE2   1 
ATOM   6638  N  N     . LEU B 2 339 ? 94.441  161.627 207.847 1.00 119.20 ? 339 LEU B N     1 
ATOM   6639  C  CA    . LEU B 2 339 ? 94.291  160.253 207.376 1.00 121.35 ? 339 LEU B CA    1 
ATOM   6640  C  C     . LEU B 2 339 ? 95.422  159.859 206.437 1.00 123.06 ? 339 LEU B C     1 
ATOM   6641  O  O     . LEU B 2 339 ? 95.973  158.757 206.543 1.00 127.55 ? 339 LEU B O     1 
ATOM   6642  C  CB    . LEU B 2 339 ? 92.939  160.082 206.685 1.00 120.85 ? 339 LEU B CB    1 
ATOM   6643  C  CG    . LEU B 2 339 ? 91.703  160.113 207.585 1.00 122.14 ? 339 LEU B CG    1 
ATOM   6644  C  CD1   . LEU B 2 339 ? 90.435  159.960 206.761 1.00 123.64 ? 339 LEU B CD1   1 
ATOM   6645  C  CD2   . LEU B 2 339 ? 91.792  159.024 208.638 1.00 121.65 ? 339 LEU B CD2   1 
ATOM   6646  N  N     . ALA B 2 340 ? 95.788  160.747 205.513 1.00 113.64 ? 340 ALA B N     1 
ATOM   6647  C  CA    . ALA B 2 340 ? 96.833  160.445 204.545 1.00 115.40 ? 340 ALA B CA    1 
ATOM   6648  C  C     . ALA B 2 340 ? 98.233  160.492 205.141 1.00 116.27 ? 340 ALA B C     1 
ATOM   6649  O  O     . ALA B 2 340 ? 99.183  160.063 204.478 1.00 115.51 ? 340 ALA B O     1 
ATOM   6650  C  CB    . ALA B 2 340 ? 96.749  161.413 203.363 1.00 116.54 ? 340 ALA B CB    1 
ATOM   6651  N  N     . SER B 2 341 ? 98.387  160.995 206.366 1.00 114.32 ? 341 SER B N     1 
ATOM   6652  C  CA    . SER B 2 341 ? 99.699  161.139 206.985 1.00 112.62 ? 341 SER B CA    1 
ATOM   6653  C  C     . SER B 2 341 ? 99.828  160.371 208.294 1.00 114.30 ? 341 SER B C     1 
ATOM   6654  O  O     . SER B 2 341 ? 100.774 160.619 209.051 1.00 116.99 ? 341 SER B O     1 
ATOM   6655  C  CB    . SER B 2 341 ? 100.011 162.620 207.219 1.00 114.16 ? 341 SER B CB    1 
ATOM   6656  O  OG    . SER B 2 341 ? 99.616  163.403 206.106 1.00 112.96 ? 341 SER B OG    1 
ATOM   6657  N  N     . LEU B 2 342 ? 98.906  159.451 208.586 1.00 122.42 ? 342 LEU B N     1 
ATOM   6658  C  CA    . LEU B 2 342 ? 98.994  158.685 209.826 1.00 122.75 ? 342 LEU B CA    1 
ATOM   6659  C  C     . LEU B 2 342 ? 100.248 157.819 209.850 1.00 125.20 ? 342 LEU B C     1 
ATOM   6660  O  O     . LEU B 2 342 ? 100.965 157.770 210.856 1.00 125.83 ? 342 LEU B O     1 
ATOM   6661  C  CB    . LEU B 2 342 ? 97.742  157.825 210.004 1.00 122.12 ? 342 LEU B CB    1 
ATOM   6662  C  CG    . LEU B 2 342 ? 96.511  158.514 210.594 1.00 124.91 ? 342 LEU B CG    1 
ATOM   6663  C  CD1   . LEU B 2 342 ? 95.348  157.539 210.691 1.00 126.95 ? 342 LEU B CD1   1 
ATOM   6664  C  CD2   . LEU B 2 342 ? 96.830  159.113 211.955 1.00 126.27 ? 342 LEU B CD2   1 
ATOM   6665  N  N     . ALA B 2 343 ? 100.529 157.127 208.747 1.00 120.32 ? 343 ALA B N     1 
ATOM   6666  C  CA    . ALA B 2 343 ? 101.699 156.269 208.640 1.00 121.57 ? 343 ALA B CA    1 
ATOM   6667  C  C     . ALA B 2 343 ? 102.799 156.879 207.781 1.00 121.74 ? 343 ALA B C     1 
ATOM   6668  O  O     . ALA B 2 343 ? 103.782 156.197 207.476 1.00 120.53 ? 343 ALA B O     1 
ATOM   6669  C  CB    . ALA B 2 343 ? 101.303 154.899 208.085 1.00 118.10 ? 343 ALA B CB    1 
ATOM   6670  N  N     . ASP B 2 344 ? 102.658 158.141 207.384 1.00 117.82 ? 344 ASP B N     1 
ATOM   6671  C  CA    . ASP B 2 344 ? 103.679 158.804 206.580 1.00 114.43 ? 344 ASP B CA    1 
ATOM   6672  C  C     . ASP B 2 344 ? 104.842 159.207 207.477 1.00 114.45 ? 344 ASP B C     1 
ATOM   6673  O  O     . ASP B 2 344 ? 104.708 160.103 208.317 1.00 112.20 ? 344 ASP B O     1 
ATOM   6674  C  CB    . ASP B 2 344 ? 103.091 160.018 205.869 1.00 116.55 ? 344 ASP B CB    1 
ATOM   6675  C  CG    . ASP B 2 344 ? 103.694 160.237 204.497 1.00 118.00 ? 344 ASP B CG    1 
ATOM   6676  O  OD1   . ASP B 2 344 ? 104.474 159.372 204.045 1.00 117.45 ? 344 ASP B OD1   1 
ATOM   6677  O  OD2   . ASP B 2 344 ? 103.390 161.273 203.870 1.00 118.06 ? 344 ASP B OD2   1 
ATOM   6678  N  N     . GLU B 2 345 ? 105.983 158.549 207.302 1.00 111.35 ? 345 GLU B N     1 
ATOM   6679  C  CA    . GLU B 2 345 ? 107.171 158.824 208.097 1.00 108.34 ? 345 GLU B CA    1 
ATOM   6680  C  C     . GLU B 2 345 ? 108.047 159.915 207.496 1.00 109.11 ? 345 GLU B C     1 
ATOM   6681  O  O     . GLU B 2 345 ? 109.061 160.277 208.101 1.00 108.83 ? 345 GLU B O     1 
ATOM   6682  C  CB    . GLU B 2 345 ? 107.990 157.543 208.276 1.00 107.55 ? 345 GLU B CB    1 
ATOM   6683  C  CG    . GLU B 2 345 ? 107.454 156.607 209.346 1.00 109.25 ? 345 GLU B CG    1 
ATOM   6684  C  CD    . GLU B 2 345 ? 107.347 157.274 210.703 1.00 114.01 ? 345 GLU B CD    1 
ATOM   6685  O  OE1   . GLU B 2 345 ? 108.366 157.816 211.181 1.00 116.05 ? 345 GLU B OE1   1 
ATOM   6686  O  OE2   . GLU B 2 345 ? 106.246 157.257 211.291 1.00 113.74 ? 345 GLU B OE2   1 
ATOM   6687  N  N     . THR B 2 346 ? 107.685 160.442 206.329 1.00 94.99  ? 346 THR B N     1 
ATOM   6688  C  CA    . THR B 2 346 ? 108.440 161.532 205.737 1.00 90.68  ? 346 THR B CA    1 
ATOM   6689  C  C     . THR B 2 346 ? 108.305 162.788 206.596 1.00 89.40  ? 346 THR B C     1 
ATOM   6690  O  O     . THR B 2 346 ? 107.298 162.970 207.284 1.00 92.80  ? 346 THR B O     1 
ATOM   6691  C  CB    . THR B 2 346 ? 107.947 161.816 204.320 1.00 85.78  ? 346 THR B CB    1 
ATOM   6692  O  OG1   . THR B 2 346 ? 106.592 162.278 204.367 1.00 90.89  ? 346 THR B OG1   1 
ATOM   6693  C  CG2   . THR B 2 346 ? 108.019 160.558 203.469 1.00 89.81  ? 346 THR B CG2   1 
ATOM   6694  N  N     . PRO B 2 347 ? 109.314 163.667 206.582 1.00 80.73  ? 347 PRO B N     1 
ATOM   6695  C  CA    . PRO B 2 347 ? 109.229 164.878 207.418 1.00 76.34  ? 347 PRO B CA    1 
ATOM   6696  C  C     . PRO B 2 347 ? 108.009 165.728 207.119 1.00 82.34  ? 347 PRO B C     1 
ATOM   6697  O  O     . PRO B 2 347 ? 107.446 166.340 208.035 1.00 86.59  ? 347 PRO B O     1 
ATOM   6698  C  CB    . PRO B 2 347 ? 110.536 165.619 207.096 1.00 78.76  ? 347 PRO B CB    1 
ATOM   6699  C  CG    . PRO B 2 347 ? 111.026 165.021 205.816 1.00 84.45  ? 347 PRO B CG    1 
ATOM   6700  C  CD    . PRO B 2 347 ? 110.583 163.597 205.841 1.00 87.58  ? 347 PRO B CD    1 
ATOM   6701  N  N     . GLU B 2 348 ? 107.585 165.787 205.856 1.00 88.52  ? 348 GLU B N     1 
ATOM   6702  C  CA    . GLU B 2 348 ? 106.350 166.491 205.528 1.00 86.06  ? 348 GLU B CA    1 
ATOM   6703  C  C     . GLU B 2 348 ? 105.142 165.802 206.150 1.00 84.64  ? 348 GLU B C     1 
ATOM   6704  O  O     . GLU B 2 348 ? 104.239 166.470 206.665 1.00 85.57  ? 348 GLU B O     1 
ATOM   6705  C  CB    . GLU B 2 348 ? 106.190 166.591 204.011 1.00 84.32  ? 348 GLU B CB    1 
ATOM   6706  C  CG    . GLU B 2 348 ? 107.308 167.352 203.320 1.00 90.42  ? 348 GLU B CG    1 
ATOM   6707  C  CD    . GLU B 2 348 ? 108.398 166.438 202.799 1.00 93.64  ? 348 GLU B CD    1 
ATOM   6708  O  OE1   . GLU B 2 348 ? 108.242 165.203 202.906 1.00 97.07  ? 348 GLU B OE1   1 
ATOM   6709  O  OE2   . GLU B 2 348 ? 109.412 166.953 202.285 1.00 92.54  ? 348 GLU B OE2   1 
ATOM   6710  N  N     . GLY B 2 349 ? 105.112 164.468 206.116 1.00 91.48  ? 349 GLY B N     1 
ATOM   6711  C  CA    . GLY B 2 349 ? 103.970 163.747 206.655 1.00 88.73  ? 349 GLY B CA    1 
ATOM   6712  C  C     . GLY B 2 349 ? 103.793 163.944 208.148 1.00 88.34  ? 349 GLY B C     1 
ATOM   6713  O  O     . GLY B 2 349 ? 102.674 164.135 208.630 1.00 93.71  ? 349 GLY B O     1 
ATOM   6714  N  N     . ARG B 2 350 ? 104.893 163.895 208.903 1.00 85.63  ? 350 ARG B N     1 
ATOM   6715  C  CA    . ARG B 2 350 ? 104.805 164.087 210.347 1.00 87.90  ? 350 ARG B CA    1 
ATOM   6716  C  C     . ARG B 2 350 ? 104.341 165.496 210.690 1.00 90.71  ? 350 ARG B C     1 
ATOM   6717  O  O     . ARG B 2 350 ? 103.565 165.690 211.633 1.00 96.54  ? 350 ARG B O     1 
ATOM   6718  C  CB    . ARG B 2 350 ? 106.154 163.789 211.002 1.00 88.11  ? 350 ARG B CB    1 
ATOM   6719  C  CG    . ARG B 2 350 ? 106.877 162.593 210.408 1.00 90.29  ? 350 ARG B CG    1 
ATOM   6720  C  CD    . ARG B 2 350 ? 108.316 162.524 210.882 1.00 91.18  ? 350 ARG B CD    1 
ATOM   6721  N  NE    . ARG B 2 350 ? 108.443 161.780 212.129 1.00 92.44  ? 350 ARG B NE    1 
ATOM   6722  C  CZ    . ARG B 2 350 ? 109.139 160.660 212.264 1.00 91.57  ? 350 ARG B CZ    1 
ATOM   6723  N  NH1   . ARG B 2 350 ? 109.787 160.121 211.244 1.00 91.58  ? 350 ARG B NH1   1 
ATOM   6724  N  NH2   . ARG B 2 350 ? 109.186 160.065 213.453 1.00 89.90  ? 350 ARG B NH2   1 
ATOM   6725  N  N     . SER B 2 351 ? 104.811 166.495 209.939 1.00 84.85  ? 351 SER B N     1 
ATOM   6726  C  CA    . SER B 2 351 ? 104.386 167.868 210.185 1.00 85.25  ? 351 SER B CA    1 
ATOM   6727  C  C     . SER B 2 351 ? 102.900 168.057 209.913 1.00 95.40  ? 351 SER B C     1 
ATOM   6728  O  O     . SER B 2 351 ? 102.252 168.879 210.571 1.00 98.37  ? 351 SER B O     1 
ATOM   6729  C  CB    . SER B 2 351 ? 105.209 168.832 209.331 1.00 86.32  ? 351 SER B CB    1 
ATOM   6730  O  OG    . SER B 2 351 ? 105.053 168.550 207.952 1.00 88.30  ? 351 SER B OG    1 
ATOM   6731  N  N     . ILE B 2 352 ? 102.347 167.319 208.948 1.00 100.02 ? 352 ILE B N     1 
ATOM   6732  C  CA    . ILE B 2 352 ? 100.918 167.416 208.658 1.00 94.40  ? 352 ILE B CA    1 
ATOM   6733  C  C     . ILE B 2 352 ? 100.101 166.967 209.862 1.00 94.51  ? 352 ILE B C     1 
ATOM   6734  O  O     . ILE B 2 352 ? 99.141  167.632 210.269 1.00 96.17  ? 352 ILE B O     1 
ATOM   6735  C  CB    . ILE B 2 352 ? 100.569 166.594 207.404 1.00 94.88  ? 352 ILE B CB    1 
ATOM   6736  C  CG1   . ILE B 2 352 ? 101.213 167.208 206.161 1.00 96.70  ? 352 ILE B CG1   1 
ATOM   6737  C  CG2   . ILE B 2 352 ? 99.064  166.497 207.233 1.00 98.51  ? 352 ILE B CG2   1 
ATOM   6738  C  CD1   . ILE B 2 352 ? 100.762 168.616 205.878 1.00 98.29  ? 352 ILE B CD1   1 
ATOM   6739  N  N     . VAL B 2 353 ? 100.474 165.830 210.452 1.00 96.27  ? 353 VAL B N     1 
ATOM   6740  C  CA    . VAL B 2 353 ? 99.745  165.315 211.605 1.00 99.36  ? 353 VAL B CA    1 
ATOM   6741  C  C     . VAL B 2 353 ? 99.905  166.243 212.802 1.00 100.90 ? 353 VAL B C     1 
ATOM   6742  O  O     . VAL B 2 353 ? 98.930  166.556 213.496 1.00 106.34 ? 353 VAL B O     1 
ATOM   6743  C  CB    . VAL B 2 353 ? 100.208 163.882 211.928 1.00 96.24  ? 353 VAL B CB    1 
ATOM   6744  C  CG1   . VAL B 2 353 ? 99.949  163.547 213.389 1.00 98.52  ? 353 VAL B CG1   1 
ATOM   6745  C  CG2   . VAL B 2 353 ? 99.510  162.886 211.018 1.00 96.01  ? 353 VAL B CG2   1 
ATOM   6746  N  N     . ILE B 2 354 ? 101.131 166.708 213.055 1.00 105.23 ? 354 ILE B N     1 
ATOM   6747  C  CA    . ILE B 2 354 ? 101.394 167.527 214.236 1.00 106.22 ? 354 ILE B CA    1 
ATOM   6748  C  C     . ILE B 2 354 ? 100.619 168.837 214.171 1.00 107.79 ? 354 ILE B C     1 
ATOM   6749  O  O     . ILE B 2 354 ? 100.010 169.264 215.160 1.00 110.11 ? 354 ILE B O     1 
ATOM   6750  C  CB    . ILE B 2 354 ? 102.907 167.768 214.389 1.00 107.13 ? 354 ILE B CB    1 
ATOM   6751  C  CG1   . ILE B 2 354 ? 103.605 166.488 214.852 1.00 106.03 ? 354 ILE B CG1   1 
ATOM   6752  C  CG2   . ILE B 2 354 ? 103.177 168.904 215.363 1.00 107.90 ? 354 ILE B CG2   1 
ATOM   6753  C  CD1   . ILE B 2 354 ? 105.115 166.567 214.813 1.00 104.20 ? 354 ILE B CD1   1 
ATOM   6754  N  N     . LEU B 2 355 ? 100.621 169.492 213.007 1.00 109.02 ? 355 LEU B N     1 
ATOM   6755  C  CA    . LEU B 2 355 ? 99.952  170.785 212.881 1.00 108.66 ? 355 LEU B CA    1 
ATOM   6756  C  C     . LEU B 2 355 ? 98.446  170.669 213.079 1.00 111.06 ? 355 LEU B C     1 
ATOM   6757  O  O     . LEU B 2 355 ? 97.805  171.626 213.529 1.00 114.65 ? 355 LEU B O     1 
ATOM   6758  C  CB    . LEU B 2 355 ? 100.259 171.404 211.517 1.00 108.99 ? 355 LEU B CB    1 
ATOM   6759  C  CG    . LEU B 2 355 ? 99.619  172.764 211.223 1.00 108.57 ? 355 LEU B CG    1 
ATOM   6760  C  CD1   . LEU B 2 355 ? 100.121 173.816 212.201 1.00 108.73 ? 355 LEU B CD1   1 
ATOM   6761  C  CD2   . LEU B 2 355 ? 99.878  173.193 209.789 1.00 108.95 ? 355 LEU B CD2   1 
ATOM   6762  N  N     . ALA B 2 356 ? 97.862  169.515 212.754 1.00 115.17 ? 356 ALA B N     1 
ATOM   6763  C  CA    . ALA B 2 356 ? 96.415  169.373 212.858 1.00 116.47 ? 356 ALA B CA    1 
ATOM   6764  C  C     . ALA B 2 356 ? 95.954  169.240 214.305 1.00 117.06 ? 356 ALA B C     1 
ATOM   6765  O  O     . ALA B 2 356 ? 94.799  169.553 214.611 1.00 120.36 ? 356 ALA B O     1 
ATOM   6766  C  CB    . ALA B 2 356 ? 95.947  168.172 212.039 1.00 116.44 ? 356 ALA B CB    1 
ATOM   6767  N  N     . LYS B 2 357 ? 96.831  168.783 215.203 1.00 126.70 ? 357 LYS B N     1 
ATOM   6768  C  CA    . LYS B 2 357 ? 96.411  168.514 216.576 1.00 126.92 ? 357 LYS B CA    1 
ATOM   6769  C  C     . LYS B 2 357 ? 96.022  169.794 217.306 1.00 128.66 ? 357 LYS B C     1 
ATOM   6770  O  O     . LYS B 2 357 ? 94.947  169.869 217.913 1.00 131.87 ? 357 LYS B O     1 
ATOM   6771  C  CB    . LYS B 2 357 ? 97.519  167.781 217.334 1.00 127.30 ? 357 LYS B CB    1 
ATOM   6772  C  CG    . LYS B 2 357 ? 98.180  166.661 216.552 1.00 128.56 ? 357 LYS B CG    1 
ATOM   6773  C  CD    . LYS B 2 357 ? 97.165  165.624 216.097 1.00 128.30 ? 357 LYS B CD    1 
ATOM   6774  C  CE    . LYS B 2 357 ? 96.572  164.872 217.276 1.00 130.86 ? 357 LYS B CE    1 
ATOM   6775  N  NZ    . LYS B 2 357 ? 95.592  163.840 216.838 1.00 129.75 ? 357 LYS B NZ    1 
ATOM   6776  N  N     . GLN B 2 358 ? 96.883  170.814 217.265 1.00 127.31 ? 358 GLN B N     1 
ATOM   6777  C  CA    . GLN B 2 358 ? 96.580  172.049 217.981 1.00 128.76 ? 358 GLN B CA    1 
ATOM   6778  C  C     . GLN B 2 358 ? 95.415  172.793 217.339 1.00 129.75 ? 358 GLN B C     1 
ATOM   6779  O  O     . GLN B 2 358 ? 94.604  173.407 218.041 1.00 132.15 ? 358 GLN B O     1 
ATOM   6780  C  CB    . GLN B 2 358 ? 97.818  172.945 218.057 1.00 127.90 ? 358 GLN B CB    1 
ATOM   6781  C  CG    . GLN B 2 358 ? 99.127  172.196 218.247 1.00 127.64 ? 358 GLN B CG    1 
ATOM   6782  C  CD    . GLN B 2 358 ? 99.836  171.927 216.939 1.00 129.00 ? 358 GLN B CD    1 
ATOM   6783  O  OE1   . GLN B 2 358 ? 99.202  171.810 215.893 1.00 130.16 ? 358 GLN B OE1   1 
ATOM   6784  N  NE2   . GLN B 2 358 ? 101.159 171.825 216.990 1.00 126.18 ? 358 GLN B NE2   1 
ATOM   6785  N  N     . ARG B 2 359 ? 95.320  172.757 216.008 1.00 125.95 ? 359 ARG B N     1 
ATOM   6786  C  CA    . ARG B 2 359 ? 94.204  173.410 215.331 1.00 127.35 ? 359 ARG B CA    1 
ATOM   6787  C  C     . ARG B 2 359 ? 92.880  172.746 215.691 1.00 129.77 ? 359 ARG B C     1 
ATOM   6788  O  O     . ARG B 2 359 ? 91.895  173.425 216.003 1.00 128.24 ? 359 ARG B O     1 
ATOM   6789  C  CB    . ARG B 2 359 ? 94.427  173.393 213.819 1.00 126.80 ? 359 ARG B CB    1 
ATOM   6790  C  CG    . ARG B 2 359 ? 95.409  174.442 213.327 1.00 126.06 ? 359 ARG B CG    1 
ATOM   6791  C  CD    . ARG B 2 359 ? 94.970  175.838 213.736 1.00 128.05 ? 359 ARG B CD    1 
ATOM   6792  N  NE    . ARG B 2 359 ? 95.885  176.863 213.249 1.00 130.52 ? 359 ARG B NE    1 
ATOM   6793  C  CZ    . ARG B 2 359 ? 95.687  177.584 212.154 1.00 129.46 ? 359 ARG B CZ    1 
ATOM   6794  N  NH1   . ARG B 2 359 ? 94.611  177.418 211.402 1.00 128.24 ? 359 ARG B NH1   1 
ATOM   6795  N  NH2   . ARG B 2 359 ? 96.591  178.495 211.805 1.00 128.45 ? 359 ARG B NH2   1 
ATOM   6796  N  N     . PHE B 2 360 ? 92.839  171.415 215.655 1.00 136.46 ? 360 PHE B N     1 
ATOM   6797  C  CA    . PHE B 2 360 ? 91.646  170.655 216.014 1.00 133.44 ? 360 PHE B CA    1 
ATOM   6798  C  C     . PHE B 2 360 ? 92.080  169.394 216.743 1.00 133.75 ? 360 PHE B C     1 
ATOM   6799  O  O     . PHE B 2 360 ? 92.731  168.528 216.152 1.00 135.67 ? 360 PHE B O     1 
ATOM   6800  C  CB    . PHE B 2 360 ? 90.809  170.300 214.779 1.00 134.05 ? 360 PHE B CB    1 
ATOM   6801  C  CG    . PHE B 2 360 ? 90.798  171.367 213.722 1.00 134.87 ? 360 PHE B CG    1 
ATOM   6802  C  CD1   . PHE B 2 360 ? 89.868  172.392 213.765 1.00 134.21 ? 360 PHE B CD1   1 
ATOM   6803  C  CD2   . PHE B 2 360 ? 91.713  171.343 212.683 1.00 134.03 ? 360 PHE B CD2   1 
ATOM   6804  C  CE1   . PHE B 2 360 ? 89.853  173.376 212.795 1.00 134.31 ? 360 PHE B CE1   1 
ATOM   6805  C  CE2   . PHE B 2 360 ? 91.703  172.324 211.709 1.00 134.49 ? 360 PHE B CE2   1 
ATOM   6806  C  CZ    . PHE B 2 360 ? 90.772  173.341 211.766 1.00 135.86 ? 360 PHE B CZ    1 
ATOM   6807  N  N     . ASN B 2 361 ? 91.710  169.286 218.018 1.00 139.17 ? 361 ASN B N     1 
ATOM   6808  C  CA    . ASN B 2 361 ? 92.120  168.150 218.833 1.00 141.35 ? 361 ASN B CA    1 
ATOM   6809  C  C     . ASN B 2 361 ? 91.337  166.899 218.456 1.00 142.88 ? 361 ASN B C     1 
ATOM   6810  O  O     . ASN B 2 361 ? 90.431  166.481 219.184 1.00 143.08 ? 361 ASN B O     1 
ATOM   6811  C  CB    . ASN B 2 361 ? 91.938  168.466 220.318 1.00 141.26 ? 361 ASN B CB    1 
ATOM   6812  C  CG    . ASN B 2 361 ? 92.060  169.947 220.616 1.00 141.94 ? 361 ASN B CG    1 
ATOM   6813  O  OD1   . ASN B 2 361 ? 93.116  170.547 220.416 1.00 141.79 ? 361 ASN B OD1   1 
ATOM   6814  N  ND2   . ASN B 2 361 ? 90.976  170.546 221.095 1.00 142.63 ? 361 ASN B ND2   1 
ATOM   6815  N  N     . LEU B 2 362 ? 91.680  166.298 217.321 1.00 146.51 ? 362 LEU B N     1 
ATOM   6816  C  CA    . LEU B 2 362 ? 90.999  165.092 216.874 1.00 145.97 ? 362 LEU B CA    1 
ATOM   6817  C  C     . LEU B 2 362 ? 91.519  163.871 217.624 1.00 147.07 ? 362 LEU B C     1 
ATOM   6818  O  O     . LEU B 2 362 ? 92.662  163.836 218.086 1.00 145.77 ? 362 LEU B O     1 
ATOM   6819  C  CB    . LEU B 2 362 ? 91.188  164.899 215.369 1.00 144.76 ? 362 LEU B CB    1 
ATOM   6820  C  CG    . LEU B 2 362 ? 90.683  166.016 214.453 1.00 144.48 ? 362 LEU B CG    1 
ATOM   6821  C  CD1   . LEU B 2 362 ? 90.478  165.493 213.040 1.00 144.83 ? 362 LEU B CD1   1 
ATOM   6822  C  CD2   . LEU B 2 362 ? 89.395  166.620 214.994 1.00 144.97 ? 362 LEU B CD2   1 
ATOM   6823  N  N     . ARG B 2 363 ? 90.660  162.862 217.744 1.00 169.52 ? 363 ARG B N     1 
ATOM   6824  C  CA    . ARG B 2 363 ? 91.061  161.615 218.380 1.00 170.61 ? 363 ARG B CA    1 
ATOM   6825  C  C     . ARG B 2 363 ? 92.107  160.904 217.528 1.00 171.08 ? 363 ARG B C     1 
ATOM   6826  O  O     . ARG B 2 363 ? 92.028  160.889 216.297 1.00 172.78 ? 363 ARG B O     1 
ATOM   6827  C  CB    . ARG B 2 363 ? 89.833  160.730 218.634 1.00 170.18 ? 363 ARG B CB    1 
ATOM   6828  C  CG    . ARG B 2 363 ? 89.122  160.167 217.402 1.00 171.12 ? 363 ARG B CG    1 
ATOM   6829  C  CD    . ARG B 2 363 ? 89.674  158.821 216.950 1.00 171.00 ? 363 ARG B CD    1 
ATOM   6830  N  NE    . ARG B 2 363 ? 89.099  158.403 215.677 1.00 172.56 ? 363 ARG B NE    1 
ATOM   6831  C  CZ    . ARG B 2 363 ? 89.309  157.223 215.110 1.00 171.51 ? 363 ARG B CZ    1 
ATOM   6832  N  NH1   . ARG B 2 363 ? 90.071  156.307 215.683 1.00 169.39 ? 363 ARG B NH1   1 
ATOM   6833  N  NH2   . ARG B 2 363 ? 88.738  156.955 213.939 1.00 170.74 ? 363 ARG B NH2   1 
ATOM   6834  N  N     . GLU B 2 364 ? 93.105  160.325 218.197 1.00 171.90 ? 364 GLU B N     1 
ATOM   6835  C  CA    . GLU B 2 364 ? 94.283  159.777 217.523 1.00 171.50 ? 364 GLU B CA    1 
ATOM   6836  C  C     . GLU B 2 364 ? 93.941  158.408 216.941 1.00 172.00 ? 364 GLU B C     1 
ATOM   6837  O  O     . GLU B 2 364 ? 94.047  157.368 217.595 1.00 170.87 ? 364 GLU B O     1 
ATOM   6838  C  CB    . GLU B 2 364 ? 95.464  159.701 218.484 1.00 171.64 ? 364 GLU B CB    1 
ATOM   6839  C  CG    . GLU B 2 364 ? 96.073  161.050 218.853 1.00 171.99 ? 364 GLU B CG    1 
ATOM   6840  C  CD    . GLU B 2 364 ? 95.172  161.884 219.745 1.00 172.34 ? 364 GLU B CD    1 
ATOM   6841  O  OE1   . GLU B 2 364 ? 94.326  161.299 220.453 1.00 172.65 ? 364 GLU B OE1   1 
ATOM   6842  O  OE2   . GLU B 2 364 ? 95.311  163.125 219.738 1.00 172.38 ? 364 GLU B OE2   1 
ATOM   6843  N  N     . ARG B 2 365 ? 93.522  158.419 215.679 1.00 173.86 ? 365 ARG B N     1 
ATOM   6844  C  CA    . ARG B 2 365 ? 93.273  157.174 214.968 1.00 173.72 ? 365 ARG B CA    1 
ATOM   6845  C  C     . ARG B 2 365 ? 94.589  156.481 214.636 1.00 172.70 ? 365 ARG B C     1 
ATOM   6846  O  O     . ARG B 2 365 ? 95.609  157.132 214.393 1.00 171.46 ? 365 ARG B O     1 
ATOM   6847  C  CB    . ARG B 2 365 ? 92.488  157.433 213.683 1.00 172.52 ? 365 ARG B CB    1 
ATOM   6848  C  CG    . ARG B 2 365 ? 92.742  158.790 213.049 1.00 172.20 ? 365 ARG B CG    1 
ATOM   6849  C  CD    . ARG B 2 365 ? 91.542  159.250 212.231 1.00 171.14 ? 365 ARG B CD    1 
ATOM   6850  N  NE    . ARG B 2 365 ? 90.459  159.782 213.049 1.00 172.54 ? 365 ARG B NE    1 
ATOM   6851  C  CZ    . ARG B 2 365 ? 90.487  160.958 213.661 1.00 171.76 ? 365 ARG B CZ    1 
ATOM   6852  N  NH1   . ARG B 2 365 ? 91.534  161.762 213.570 1.00 172.14 ? 365 ARG B NH1   1 
ATOM   6853  N  NH2   . ARG B 2 365 ? 89.433  161.343 214.375 1.00 169.59 ? 365 ARG B NH2   1 
ATOM   6854  N  N     . ASP B 2 366 ? 94.563  155.154 214.630 1.00 180.03 ? 366 ASP B N     1 
ATOM   6855  C  CA    . ASP B 2 366 ? 95.704  154.353 214.215 1.00 179.05 ? 366 ASP B CA    1 
ATOM   6856  C  C     . ASP B 2 366 ? 95.357  153.555 212.961 1.00 179.67 ? 366 ASP B C     1 
ATOM   6857  O  O     . ASP B 2 366 ? 94.189  153.358 212.620 1.00 180.32 ? 366 ASP B O     1 
ATOM   6858  C  CB    . ASP B 2 366 ? 96.157  153.426 215.348 1.00 179.69 ? 366 ASP B CB    1 
ATOM   6859  C  CG    . ASP B 2 366 ? 94.996  152.804 216.094 1.00 180.02 ? 366 ASP B CG    1 
ATOM   6860  O  OD1   . ASP B 2 366 ? 94.220  153.555 216.722 1.00 179.66 ? 366 ASP B OD1   1 
ATOM   6861  O  OD2   . ASP B 2 366 ? 94.864  151.563 216.061 1.00 180.32 ? 366 ASP B OD2   1 
ATOM   6862  N  N     . VAL B 2 367 ? 96.403  153.103 212.265 1.00 180.98 ? 367 VAL B N     1 
ATOM   6863  C  CA    . VAL B 2 367 ? 96.210  152.441 210.978 1.00 181.47 ? 367 VAL B CA    1 
ATOM   6864  C  C     . VAL B 2 367 ? 95.446  151.131 211.147 1.00 181.91 ? 367 VAL B C     1 
ATOM   6865  O  O     . VAL B 2 367 ? 94.549  150.816 210.356 1.00 181.26 ? 367 VAL B O     1 
ATOM   6866  C  CB    . VAL B 2 367 ? 97.566  152.232 210.275 1.00 180.90 ? 367 VAL B CB    1 
ATOM   6867  C  CG1   . VAL B 2 367 ? 98.590  151.640 211.233 1.00 180.97 ? 367 VAL B CG1   1 
ATOM   6868  C  CG2   . VAL B 2 367 ? 97.403  151.351 209.044 1.00 180.16 ? 367 VAL B CG2   1 
ATOM   6869  N  N     . GLN B 2 368 ? 95.777  150.351 212.180 1.00 186.14 ? 368 GLN B N     1 
ATOM   6870  C  CA    . GLN B 2 368 ? 95.094  149.075 212.376 1.00 185.88 ? 368 GLN B CA    1 
ATOM   6871  C  C     . GLN B 2 368 ? 93.649  149.271 212.820 1.00 184.75 ? 368 GLN B C     1 
ATOM   6872  O  O     . GLN B 2 368 ? 92.805  148.401 212.575 1.00 184.45 ? 368 GLN B O     1 
ATOM   6873  C  CB    . GLN B 2 368 ? 95.848  148.210 213.389 1.00 185.53 ? 368 GLN B CB    1 
ATOM   6874  C  CG    . GLN B 2 368 ? 96.018  148.820 214.777 1.00 184.88 ? 368 GLN B CG    1 
ATOM   6875  C  CD    . GLN B 2 368 ? 97.160  149.816 214.861 1.00 185.10 ? 368 GLN B CD    1 
ATOM   6876  O  OE1   . GLN B 2 368 ? 97.313  150.680 213.999 1.00 185.96 ? 368 GLN B OE1   1 
ATOM   6877  N  NE2   . GLN B 2 368 ? 97.971  149.697 215.906 1.00 184.73 ? 368 GLN B NE2   1 
ATOM   6878  N  N     . SER B 2 369 ? 93.344  150.396 213.472 1.00 176.13 ? 369 SER B N     1 
ATOM   6879  C  CA    . SER B 2 369 ? 91.971  150.653 213.895 1.00 175.29 ? 369 SER B CA    1 
ATOM   6880  C  C     . SER B 2 369 ? 91.052  150.901 212.707 1.00 176.46 ? 369 SER B C     1 
ATOM   6881  O  O     . SER B 2 369 ? 89.858  150.590 212.773 1.00 178.73 ? 369 SER B O     1 
ATOM   6882  C  CB    . SER B 2 369 ? 91.925  151.843 214.852 1.00 174.95 ? 369 SER B CB    1 
ATOM   6883  O  OG    . SER B 2 369 ? 92.417  153.017 214.228 1.00 175.30 ? 369 SER B OG    1 
ATOM   6884  N  N     . LEU B 2 370 ? 91.580  151.465 211.623 1.00 171.68 ? 370 LEU B N     1 
ATOM   6885  C  CA    . LEU B 2 370 ? 90.783  151.741 210.436 1.00 171.60 ? 370 LEU B CA    1 
ATOM   6886  C  C     . LEU B 2 370 ? 90.736  150.573 209.461 1.00 171.73 ? 370 LEU B C     1 
ATOM   6887  O  O     . LEU B 2 370 ? 89.944  150.616 208.513 1.00 171.15 ? 370 LEU B O     1 
ATOM   6888  C  CB    . LEU B 2 370 ? 91.323  152.982 209.718 1.00 169.35 ? 370 LEU B CB    1 
ATOM   6889  C  CG    . LEU B 2 370 ? 91.246  154.291 210.505 1.00 169.64 ? 370 LEU B CG    1 
ATOM   6890  C  CD1   . LEU B 2 370 ? 91.824  155.440 209.696 1.00 169.36 ? 370 LEU B CD1   1 
ATOM   6891  C  CD2   . LEU B 2 370 ? 89.813  154.588 210.919 1.00 169.65 ? 370 LEU B CD2   1 
ATOM   6892  N  N     . HIS B 2 371 ? 91.545  149.535 209.680 1.00 171.73 ? 371 HIS B N     1 
ATOM   6893  C  CA    . HIS B 2 371 ? 91.608  148.368 208.797 1.00 170.74 ? 371 HIS B CA    1 
ATOM   6894  C  C     . HIS B 2 371 ? 91.818  148.787 207.343 1.00 171.31 ? 371 HIS B C     1 
ATOM   6895  O  O     . HIS B 2 371 ? 91.141  148.315 206.427 1.00 171.06 ? 371 HIS B O     1 
ATOM   6896  C  CB    . HIS B 2 371 ? 90.359  147.496 208.943 1.00 171.36 ? 371 HIS B CB    1 
ATOM   6897  C  CG    . HIS B 2 371 ? 89.683  147.620 210.273 1.00 172.97 ? 371 HIS B CG    1 
ATOM   6898  N  ND1   . HIS B 2 371 ? 90.350  147.443 211.466 1.00 172.59 ? 371 HIS B ND1   1 
ATOM   6899  C  CD2   . HIS B 2 371 ? 88.400  147.904 210.598 1.00 172.91 ? 371 HIS B CD2   1 
ATOM   6900  C  CE1   . HIS B 2 371 ? 89.506  147.610 212.469 1.00 172.91 ? 371 HIS B CE1   1 
ATOM   6901  N  NE2   . HIS B 2 371 ? 88.317  147.892 211.969 1.00 172.78 ? 371 HIS B NE2   1 
ATOM   6902  N  N     . ALA B 2 372 ? 92.773  149.689 207.136 1.00 155.31 ? 372 ALA B N     1 
ATOM   6903  C  CA    . ALA B 2 372 ? 93.062  150.233 205.820 1.00 154.04 ? 372 ALA B CA    1 
ATOM   6904  C  C     . ALA B 2 372 ? 94.558  150.156 205.547 1.00 153.34 ? 372 ALA B C     1 
ATOM   6905  O  O     . ALA B 2 372 ? 95.371  149.938 206.450 1.00 153.39 ? 372 ALA B O     1 
ATOM   6906  C  CB    . ALA B 2 372 ? 92.574  151.682 205.694 1.00 152.76 ? 372 ALA B CB    1 
ATOM   6907  N  N     . THR B 2 373 ? 94.913  150.340 204.281 1.00 152.46 ? 373 THR B N     1 
ATOM   6908  C  CA    . THR B 2 373 ? 96.296  150.336 203.833 1.00 154.73 ? 373 THR B CA    1 
ATOM   6909  C  C     . THR B 2 373 ? 96.722  151.749 203.456 1.00 153.11 ? 373 THR B C     1 
ATOM   6910  O  O     . THR B 2 373 ? 95.893  152.634 203.230 1.00 153.35 ? 373 THR B O     1 
ATOM   6911  C  CB    . THR B 2 373 ? 96.487  149.395 202.638 1.00 154.79 ? 373 THR B CB    1 
ATOM   6912  O  OG1   . THR B 2 373 ? 95.742  149.887 201.517 1.00 154.63 ? 373 THR B OG1   1 
ATOM   6913  C  CG2   . THR B 2 373 ? 96.007  147.994 202.982 1.00 151.64 ? 373 THR B CG2   1 
ATOM   6914  N  N     . PHE B 2 374 ? 98.035  151.953 203.397 1.00 129.59 ? 374 PHE B N     1 
ATOM   6915  C  CA    . PHE B 2 374 ? 98.610  153.254 203.092 1.00 127.58 ? 374 PHE B CA    1 
ATOM   6916  C  C     . PHE B 2 374 ? 99.475  153.160 201.845 1.00 126.92 ? 374 PHE B C     1 
ATOM   6917  O  O     . PHE B 2 374 ? 100.167 152.159 201.630 1.00 128.85 ? 374 PHE B O     1 
ATOM   6918  C  CB    . PHE B 2 374 ? 99.450  153.786 204.258 1.00 130.02 ? 374 PHE B CB    1 
ATOM   6919  C  CG    . PHE B 2 374 ? 98.641  154.434 205.343 1.00 132.76 ? 374 PHE B CG    1 
ATOM   6920  C  CD1   . PHE B 2 374 ? 97.633  153.736 205.986 1.00 132.62 ? 374 PHE B CD1   1 
ATOM   6921  C  CD2   . PHE B 2 374 ? 98.878  155.748 205.709 1.00 132.39 ? 374 PHE B CD2   1 
ATOM   6922  C  CE1   . PHE B 2 374 ? 96.887  154.331 206.983 1.00 133.16 ? 374 PHE B CE1   1 
ATOM   6923  C  CE2   . PHE B 2 374 ? 98.134  156.348 206.704 1.00 132.92 ? 374 PHE B CE2   1 
ATOM   6924  C  CZ    . PHE B 2 374 ? 97.136  155.639 207.341 1.00 134.34 ? 374 PHE B CZ    1 
ATOM   6925  N  N     . VAL B 2 375 ? 99.430  154.206 201.025 1.00 106.73 ? 375 VAL B N     1 
ATOM   6926  C  CA    . VAL B 2 375 ? 100.278 154.314 199.842 1.00 107.10 ? 375 VAL B CA    1 
ATOM   6927  C  C     . VAL B 2 375 ? 101.503 155.140 200.227 1.00 109.91 ? 375 VAL B C     1 
ATOM   6928  O  O     . VAL B 2 375 ? 101.359 156.342 200.507 1.00 114.51 ? 375 VAL B O     1 
ATOM   6929  C  CB    . VAL B 2 375 ? 99.527  154.953 198.668 1.00 105.10 ? 375 VAL B CB    1 
ATOM   6930  C  CG1   . VAL B 2 375 ? 100.450 155.106 197.469 1.00 104.13 ? 375 VAL B CG1   1 
ATOM   6931  C  CG2   . VAL B 2 375 ? 98.307  154.121 198.305 1.00 108.97 ? 375 VAL B CG2   1 
ATOM   6932  N  N     . PRO B 2 376 ? 102.697 154.554 200.265 1.00 98.70  ? 376 PRO B N     1 
ATOM   6933  C  CA    . PRO B 2 376 ? 103.883 155.328 200.643 1.00 97.30  ? 376 PRO B CA    1 
ATOM   6934  C  C     . PRO B 2 376 ? 104.238 156.361 199.587 1.00 97.96  ? 376 PRO B C     1 
ATOM   6935  O  O     . PRO B 2 376 ? 103.970 156.187 198.395 1.00 99.66  ? 376 PRO B O     1 
ATOM   6936  C  CB    . PRO B 2 376 ? 104.976 154.263 200.769 1.00 94.99  ? 376 PRO B CB    1 
ATOM   6937  C  CG    . PRO B 2 376 ? 104.530 153.165 199.866 1.00 94.88  ? 376 PRO B CG    1 
ATOM   6938  C  CD    . PRO B 2 376 ? 103.026 153.160 199.921 1.00 97.99  ? 376 PRO B CD    1 
ATOM   6939  N  N     . PHE B 2 377 ? 104.848 157.452 200.042 1.00 85.49  ? 377 PHE B N     1 
ATOM   6940  C  CA    . PHE B 2 377 ? 105.283 158.498 199.130 1.00 83.72  ? 377 PHE B CA    1 
ATOM   6941  C  C     . PHE B 2 377 ? 106.409 157.987 198.240 1.00 86.02  ? 377 PHE B C     1 
ATOM   6942  O  O     . PHE B 2 377 ? 107.330 157.309 198.702 1.00 87.44  ? 377 PHE B O     1 
ATOM   6943  C  CB    . PHE B 2 377 ? 105.744 159.727 199.910 1.00 85.52  ? 377 PHE B CB    1 
ATOM   6944  C  CG    . PHE B 2 377 ? 106.433 160.759 199.064 1.00 84.97  ? 377 PHE B CG    1 
ATOM   6945  C  CD1   . PHE B 2 377 ? 105.709 161.549 198.187 1.00 81.98  ? 377 PHE B CD1   1 
ATOM   6946  C  CD2   . PHE B 2 377 ? 107.804 160.937 199.143 1.00 89.33  ? 377 PHE B CD2   1 
ATOM   6947  C  CE1   . PHE B 2 377 ? 106.339 162.498 197.407 1.00 81.23  ? 377 PHE B CE1   1 
ATOM   6948  C  CE2   . PHE B 2 377 ? 108.439 161.884 198.364 1.00 91.34  ? 377 PHE B CE2   1 
ATOM   6949  C  CZ    . PHE B 2 377 ? 107.706 162.666 197.495 1.00 87.42  ? 377 PHE B CZ    1 
ATOM   6950  N  N     . THR B 2 378 ? 106.329 158.315 196.953 1.00 96.28  ? 378 THR B N     1 
ATOM   6951  C  CA    . THR B 2 378 ? 107.323 157.888 195.981 1.00 98.05  ? 378 THR B CA    1 
ATOM   6952  C  C     . THR B 2 378 ? 107.695 159.072 195.103 1.00 99.01  ? 378 THR B C     1 
ATOM   6953  O  O     . THR B 2 378 ? 106.843 159.902 194.776 1.00 98.79  ? 378 THR B O     1 
ATOM   6954  C  CB    . THR B 2 378 ? 106.802 156.727 195.122 1.00 102.39 ? 378 THR B CB    1 
ATOM   6955  O  OG1   . THR B 2 378 ? 106.343 155.672 195.975 1.00 106.24 ? 378 THR B OG1   1 
ATOM   6956  C  CG2   . THR B 2 378 ? 107.899 156.187 194.217 1.00 100.40 ? 378 THR B CG2   1 
ATOM   6957  N  N     . ALA B 2 379 ? 108.975 159.148 194.731 1.00 112.03 ? 379 ALA B N     1 
ATOM   6958  C  CA    . ALA B 2 379 ? 109.438 160.246 193.889 1.00 112.68 ? 379 ALA B CA    1 
ATOM   6959  C  C     . ALA B 2 379 ? 108.753 160.230 192.529 1.00 111.62 ? 379 ALA B C     1 
ATOM   6960  O  O     . ALA B 2 379 ? 108.396 161.285 191.992 1.00 112.32 ? 379 ALA B O     1 
ATOM   6961  C  CB    . ALA B 2 379 ? 110.956 160.179 193.726 1.00 113.82 ? 379 ALA B CB    1 
ATOM   6962  N  N     . GLN B 2 380 ? 108.571 159.042 191.947 1.00 114.49 ? 380 GLN B N     1 
ATOM   6963  C  CA    . GLN B 2 380 ? 107.902 158.951 190.653 1.00 113.73 ? 380 GLN B CA    1 
ATOM   6964  C  C     . GLN B 2 380 ? 106.420 159.287 190.769 1.00 114.81 ? 380 GLN B C     1 
ATOM   6965  O  O     . GLN B 2 380 ? 105.877 160.019 189.932 1.00 115.47 ? 380 GLN B O     1 
ATOM   6966  C  CB    . GLN B 2 380 ? 108.088 157.556 190.054 1.00 112.23 ? 380 GLN B CB    1 
ATOM   6967  C  CG    . GLN B 2 380 ? 109.499 157.241 189.560 1.00 112.89 ? 380 GLN B CG    1 
ATOM   6968  C  CD    . GLN B 2 380 ? 110.528 157.188 190.673 1.00 117.14 ? 380 GLN B CD    1 
ATOM   6969  O  OE1   . GLN B 2 380 ? 110.193 156.963 191.836 1.00 118.61 ? 380 GLN B OE1   1 
ATOM   6970  N  NE2   . GLN B 2 380 ? 111.791 157.396 190.320 1.00 116.58 ? 380 GLN B NE2   1 
ATOM   6971  N  N     . SER B 2 381 ? 105.748 158.763 191.797 1.00 108.98 ? 381 SER B N     1 
ATOM   6972  C  CA    . SER B 2 381 ? 104.313 158.992 191.933 1.00 109.12 ? 381 SER B CA    1 
ATOM   6973  C  C     . SER B 2 381 ? 104.012 160.429 192.338 1.00 107.96 ? 381 SER B C     1 
ATOM   6974  O  O     . SER B 2 381 ? 103.012 161.006 191.896 1.00 109.80 ? 381 SER B O     1 
ATOM   6975  C  CB    . SER B 2 381 ? 103.717 158.016 192.947 1.00 107.35 ? 381 SER B CB    1 
ATOM   6976  O  OG    . SER B 2 381 ? 104.126 158.338 194.264 1.00 109.24 ? 381 SER B OG    1 
ATOM   6977  N  N     . ARG B 2 382 ? 104.859 161.017 193.186 1.00 102.05 ? 382 ARG B N     1 
ATOM   6978  C  CA    . ARG B 2 382 ? 104.671 162.376 193.697 1.00 99.74  ? 382 ARG B CA    1 
ATOM   6979  C  C     . ARG B 2 382 ? 103.349 162.524 194.445 1.00 97.46  ? 382 ARG B C     1 
ATOM   6980  O  O     . ARG B 2 382 ? 102.761 163.607 194.478 1.00 96.79  ? 382 ARG B O     1 
ATOM   6981  C  CB    . ARG B 2 382 ? 104.765 163.416 192.575 1.00 98.04  ? 382 ARG B CB    1 
ATOM   6982  C  CG    . ARG B 2 382 ? 106.109 163.460 191.874 1.00 101.26 ? 382 ARG B CG    1 
ATOM   6983  C  CD    . ARG B 2 382 ? 106.000 164.127 190.515 1.00 101.86 ? 382 ARG B CD    1 
ATOM   6984  N  NE    . ARG B 2 382 ? 105.634 165.533 190.625 1.00 104.44 ? 382 ARG B NE    1 
ATOM   6985  C  CZ    . ARG B 2 382 ? 106.499 166.537 190.588 1.00 107.11 ? 382 ARG B CZ    1 
ATOM   6986  N  NH1   . ARG B 2 382 ? 107.796 166.326 190.439 1.00 106.81 ? 382 ARG B NH1   1 
ATOM   6987  N  NH2   . ARG B 2 382 ? 106.051 167.784 190.701 1.00 105.52 ? 382 ARG B NH2   1 
ATOM   6988  N  N     . MET B 2 383 ? 102.871 161.440 195.051 1.00 97.14  ? 383 MET B N     1 
ATOM   6989  C  CA    . MET B 2 383 ? 101.616 161.479 195.788 1.00 96.80  ? 383 MET B CA    1 
ATOM   6990  C  C     . MET B 2 383 ? 101.598 160.347 196.804 1.00 101.03 ? 383 MET B C     1 
ATOM   6991  O  O     . MET B 2 383 ? 102.336 159.366 196.683 1.00 104.51 ? 383 MET B O     1 
ATOM   6992  C  CB    . MET B 2 383 ? 100.409 161.382 194.849 1.00 101.07 ? 383 MET B CB    1 
ATOM   6993  C  CG    . MET B 2 383 ? 100.088 159.969 194.391 1.00 104.12 ? 383 MET B CG    1 
ATOM   6994  S  SD    . MET B 2 383 ? 98.565  159.872 193.432 1.00 111.19 ? 383 MET B SD    1 
ATOM   6995  C  CE    . MET B 2 383 ? 98.570  161.467 192.618 1.00 104.37 ? 383 MET B CE    1 
ATOM   6996  N  N     . SER B 2 384 ? 100.740 160.502 197.809 1.00 95.99  ? 384 SER B N     1 
ATOM   6997  C  CA    . SER B 2 384 ? 100.567 159.492 198.843 1.00 96.47  ? 384 SER B CA    1 
ATOM   6998  C  C     . SER B 2 384 ? 99.208  159.698 199.494 1.00 101.04 ? 384 SER B C     1 
ATOM   6999  O  O     . SER B 2 384 ? 98.610  160.772 199.395 1.00 102.33 ? 384 SER B O     1 
ATOM   7000  C  CB    . SER B 2 384 ? 101.685 159.558 199.888 1.00 98.17  ? 384 SER B CB    1 
ATOM   7001  O  OG    . SER B 2 384 ? 101.682 160.807 200.557 1.00 98.42  ? 384 SER B OG    1 
ATOM   7002  N  N     . GLY B 2 385 ? 98.728  158.657 200.162 1.00 111.58 ? 385 GLY B N     1 
ATOM   7003  C  CA    . GLY B 2 385 ? 97.439  158.737 200.815 1.00 111.17 ? 385 GLY B CA    1 
ATOM   7004  C  C     . GLY B 2 385 ? 97.019  157.388 201.362 1.00 112.25 ? 385 GLY B C     1 
ATOM   7005  O  O     . GLY B 2 385 ? 97.788  156.424 201.357 1.00 109.46 ? 385 GLY B O     1 
ATOM   7006  N  N     . ILE B 2 386 ? 95.776  157.347 201.833 1.00 130.14 ? 386 ILE B N     1 
ATOM   7007  C  CA    . ILE B 2 386 ? 95.186  156.160 202.438 1.00 129.74 ? 386 ILE B CA    1 
ATOM   7008  C  C     . ILE B 2 386 ? 93.978  155.747 201.609 1.00 128.61 ? 386 ILE B C     1 
ATOM   7009  O  O     . ILE B 2 386 ? 93.112  156.577 201.308 1.00 128.03 ? 386 ILE B O     1 
ATOM   7010  C  CB    . ILE B 2 386 ? 94.782  156.412 203.902 1.00 125.81 ? 386 ILE B CB    1 
ATOM   7011  C  CG1   . ILE B 2 386 ? 93.845  155.310 204.399 1.00 125.54 ? 386 ILE B CG1   1 
ATOM   7012  C  CG2   . ILE B 2 386 ? 94.124  157.774 204.047 1.00 124.63 ? 386 ILE B CG2   1 
ATOM   7013  C  CD1   . ILE B 2 386 ? 93.678  155.282 205.900 1.00 126.13 ? 386 ILE B CD1   1 
ATOM   7014  N  N     . ASN B 2 387 ? 93.928  154.470 201.230 1.00 139.60 ? 387 ASN B N     1 
ATOM   7015  C  CA    . ASN B 2 387 ? 92.773  153.913 200.528 1.00 140.06 ? 387 ASN B CA    1 
ATOM   7016  C  C     . ASN B 2 387 ? 91.895  153.171 201.536 1.00 140.03 ? 387 ASN B C     1 
ATOM   7017  O  O     . ASN B 2 387 ? 91.823  151.942 201.571 1.00 140.40 ? 387 ASN B O     1 
ATOM   7018  C  CB    . ASN B 2 387 ? 93.226  153.030 199.362 1.00 138.78 ? 387 ASN B CB    1 
ATOM   7019  C  CG    . ASN B 2 387 ? 94.085  151.854 199.801 1.00 139.77 ? 387 ASN B CG    1 
ATOM   7020  O  OD1   . ASN B 2 387 ? 94.443  151.727 200.971 1.00 140.45 ? 387 ASN B OD1   1 
ATOM   7021  N  ND2   . ASN B 2 387 ? 94.418  150.985 198.854 1.00 139.50 ? 387 ASN B ND2   1 
ATOM   7022  N  N     . ILE B 2 388 ? 91.195  153.952 202.357 1.00 147.53 ? 388 ILE B N     1 
ATOM   7023  C  CA    . ILE B 2 388 ? 90.284  153.409 203.359 1.00 148.14 ? 388 ILE B CA    1 
ATOM   7024  C  C     . ILE B 2 388 ? 89.079  152.811 202.645 1.00 151.11 ? 388 ILE B C     1 
ATOM   7025  O  O     . ILE B 2 388 ? 88.918  152.984 201.432 1.00 151.85 ? 388 ILE B O     1 
ATOM   7026  C  CB    . ILE B 2 388 ? 89.869  154.486 204.382 1.00 147.57 ? 388 ILE B CB    1 
ATOM   7027  C  CG1   . ILE B 2 388 ? 89.648  153.860 205.761 1.00 147.97 ? 388 ILE B CG1   1 
ATOM   7028  C  CG2   . ILE B 2 388 ? 88.622  155.231 203.923 1.00 146.74 ? 388 ILE B CG2   1 
ATOM   7029  C  CD1   . ILE B 2 388 ? 89.158  154.838 206.805 1.00 146.10 ? 388 ILE B CD1   1 
ATOM   7030  N  N     . ASP B 2 389 ? 88.245  152.075 203.380 1.00 171.11 ? 389 ASP B N     1 
ATOM   7031  C  CA    . ASP B 2 389 ? 87.075  151.444 202.784 1.00 170.52 ? 389 ASP B CA    1 
ATOM   7032  C  C     . ASP B 2 389 ? 86.188  152.480 202.105 1.00 170.08 ? 389 ASP B C     1 
ATOM   7033  O  O     . ASP B 2 389 ? 85.864  153.518 202.689 1.00 170.04 ? 389 ASP B O     1 
ATOM   7034  C  CB    . ASP B 2 389 ? 86.285  150.688 203.856 1.00 170.44 ? 389 ASP B CB    1 
ATOM   7035  C  CG    . ASP B 2 389 ? 85.892  151.572 205.023 1.00 170.83 ? 389 ASP B CG    1 
ATOM   7036  O  OD1   . ASP B 2 389 ? 86.791  152.180 205.640 1.00 171.45 ? 389 ASP B OD1   1 
ATOM   7037  O  OD2   . ASP B 2 389 ? 84.682  151.660 205.323 1.00 170.09 ? 389 ASP B OD2   1 
ATOM   7038  N  N     . ASN B 2 390 ? 85.820  152.194 200.854 1.00 167.85 ? 390 ASN B N     1 
ATOM   7039  C  CA    . ASN B 2 390 ? 84.969  153.058 200.040 1.00 168.88 ? 390 ASN B CA    1 
ATOM   7040  C  C     . ASN B 2 390 ? 85.625  154.410 199.779 1.00 168.97 ? 390 ASN B C     1 
ATOM   7041  O  O     . ASN B 2 390 ? 86.004  154.712 198.642 1.00 167.52 ? 390 ASN B O     1 
ATOM   7042  C  CB    . ASN B 2 390 ? 83.599  153.245 200.699 1.00 168.62 ? 390 ASN B CB    1 
ATOM   7043  C  CG    . ASN B 2 390 ? 82.798  154.367 200.068 1.00 168.87 ? 390 ASN B CG    1 
ATOM   7044  O  OD1   . ASN B 2 390 ? 82.389  155.310 200.746 1.00 169.37 ? 390 ASN B OD1   1 
ATOM   7045  N  ND2   . ASN B 2 390 ? 82.568  154.270 198.764 1.00 168.97 ? 390 ASN B ND2   1 
ATOM   7046  N  N     . ARG B 2 391 ? 85.761  155.228 200.820 1.00 149.77 ? 391 ARG B N     1 
ATOM   7047  C  CA    . ARG B 2 391 ? 86.330  156.559 200.666 1.00 147.93 ? 391 ARG B CA    1 
ATOM   7048  C  C     . ARG B 2 391 ? 87.813  156.477 200.321 1.00 148.48 ? 391 ARG B C     1 
ATOM   7049  O  O     . ARG B 2 391 ? 88.533  155.601 200.805 1.00 146.75 ? 391 ARG B O     1 
ATOM   7050  C  CB    . ARG B 2 391 ? 86.128  157.365 201.949 1.00 144.89 ? 391 ARG B CB    1 
ATOM   7051  C  CG    . ARG B 2 391 ? 86.587  158.811 201.871 1.00 144.83 ? 391 ARG B CG    1 
ATOM   7052  C  CD    . ARG B 2 391 ? 85.866  159.665 202.900 1.00 144.99 ? 391 ARG B CD    1 
ATOM   7053  N  NE    . ARG B 2 391 ? 86.192  159.271 204.265 1.00 144.37 ? 391 ARG B NE    1 
ATOM   7054  C  CZ    . ARG B 2 391 ? 86.652  160.097 205.194 1.00 144.57 ? 391 ARG B CZ    1 
ATOM   7055  N  NH1   . ARG B 2 391 ? 86.854  161.379 204.940 1.00 144.13 ? 391 ARG B NH1   1 
ATOM   7056  N  NH2   . ARG B 2 391 ? 86.913  159.625 206.410 1.00 145.76 ? 391 ARG B NH2   1 
ATOM   7057  N  N     . MET B 2 392 ? 88.269  157.394 199.471 1.00 142.67 ? 392 MET B N     1 
ATOM   7058  C  CA    . MET B 2 392 ? 89.667  157.464 199.066 1.00 138.22 ? 392 MET B CA    1 
ATOM   7059  C  C     . MET B 2 392 ? 90.223  158.839 199.404 1.00 138.05 ? 392 MET B C     1 
ATOM   7060  O  O     . MET B 2 392 ? 89.631  159.860 199.039 1.00 138.50 ? 392 MET B O     1 
ATOM   7061  C  CB    . MET B 2 392 ? 89.824  157.180 197.570 1.00 138.86 ? 392 MET B CB    1 
ATOM   7062  C  CG    . MET B 2 392 ? 91.127  156.487 197.206 1.00 137.19 ? 392 MET B CG    1 
ATOM   7063  S  SD    . MET B 2 392 ? 91.325  156.252 195.430 1.00 145.12 ? 392 MET B SD    1 
ATOM   7064  C  CE    . MET B 2 392 ? 91.115  157.930 194.841 1.00 137.73 ? 392 MET B CE    1 
ATOM   7065  N  N     . ILE B 2 393 ? 91.358  158.861 200.099 1.00 116.54 ? 393 ILE B N     1 
ATOM   7066  C  CA    . ILE B 2 393 ? 92.040  160.092 200.480 1.00 113.09 ? 393 ILE B CA    1 
ATOM   7067  C  C     . ILE B 2 393 ? 93.438  160.064 199.881 1.00 111.03 ? 393 ILE B C     1 
ATOM   7068  O  O     . ILE B 2 393 ? 94.159  159.069 200.024 1.00 113.26 ? 393 ILE B O     1 
ATOM   7069  C  CB    . ILE B 2 393 ? 92.108  160.260 202.009 1.00 114.69 ? 393 ILE B CB    1 
ATOM   7070  C  CG1   . ILE B 2 393 ? 90.800  159.804 202.661 1.00 117.69 ? 393 ILE B CG1   1 
ATOM   7071  C  CG2   . ILE B 2 393 ? 92.423  161.704 202.373 1.00 112.84 ? 393 ILE B CG2   1 
ATOM   7072  C  CD1   . ILE B 2 393 ? 89.686  160.822 202.579 1.00 118.27 ? 393 ILE B CD1   1 
ATOM   7073  N  N     . ARG B 2 394 ? 93.818  161.150 199.212 1.00 94.57  ? 394 ARG B N     1 
ATOM   7074  C  CA    . ARG B 2 394 ? 95.120  161.227 198.568 1.00 96.28  ? 394 ARG B CA    1 
ATOM   7075  C  C     . ARG B 2 394 ? 95.646  162.652 198.656 1.00 99.02  ? 394 ARG B C     1 
ATOM   7076  O  O     . ARG B 2 394 ? 94.874  163.614 198.697 1.00 98.08  ? 394 ARG B O     1 
ATOM   7077  C  CB    . ARG B 2 394 ? 95.048  160.780 197.103 1.00 99.57  ? 394 ARG B CB    1 
ATOM   7078  C  CG    . ARG B 2 394 ? 96.142  159.808 196.697 1.00 97.77  ? 394 ARG B CG    1 
ATOM   7079  C  CD    . ARG B 2 394 ? 95.969  158.468 197.391 1.00 98.62  ? 394 ARG B CD    1 
ATOM   7080  N  NE    . ARG B 2 394 ? 96.770  157.423 196.766 1.00 101.07 ? 394 ARG B NE    1 
ATOM   7081  C  CZ    . ARG B 2 394 ? 96.319  156.586 195.842 1.00 99.24  ? 394 ARG B CZ    1 
ATOM   7082  N  NH1   . ARG B 2 394 ? 95.070  156.642 195.409 1.00 101.10 ? 394 ARG B NH1   1 
ATOM   7083  N  NH2   . ARG B 2 394 ? 97.142  155.670 195.339 1.00 98.88  ? 394 ARG B NH2   1 
ATOM   7084  N  N     . LYS B 2 395 ? 96.972  162.774 198.688 1.00 94.86  ? 395 LYS B N     1 
ATOM   7085  C  CA    . LYS B 2 395 ? 97.643  164.064 198.693 1.00 92.16  ? 395 LYS B CA    1 
ATOM   7086  C  C     . LYS B 2 395 ? 98.953  163.943 197.930 1.00 90.60  ? 395 LYS B C     1 
ATOM   7087  O  O     . LYS B 2 395 ? 99.521  162.854 197.814 1.00 90.33  ? 395 LYS B O     1 
ATOM   7088  C  CB    . LYS B 2 395 ? 97.906  164.565 200.119 1.00 85.79  ? 395 LYS B CB    1 
ATOM   7089  C  CG    . LYS B 2 395 ? 98.857  163.690 200.917 1.00 90.28  ? 395 LYS B CG    1 
ATOM   7090  C  CD    . LYS B 2 395 ? 99.577  164.490 201.989 1.00 93.99  ? 395 LYS B CD    1 
ATOM   7091  C  CE    . LYS B 2 395 ? 100.369 163.583 202.915 1.00 91.02  ? 395 LYS B CE    1 
ATOM   7092  N  NZ    . LYS B 2 395 ? 101.114 162.537 202.163 1.00 88.14  ? 395 LYS B NZ    1 
ATOM   7093  N  N     . GLY B 2 396 ? 99.429  165.069 197.409 1.00 80.19  ? 396 GLY B N     1 
ATOM   7094  C  CA    . GLY B 2 396 ? 100.667 165.057 196.653 1.00 80.41  ? 396 GLY B CA    1 
ATOM   7095  C  C     . GLY B 2 396 ? 100.869 166.365 195.915 1.00 82.27  ? 396 GLY B C     1 
ATOM   7096  O  O     . GLY B 2 396 ? 100.275 167.388 196.260 1.00 78.81  ? 396 GLY B O     1 
ATOM   7097  N  N     . SER B 2 397 ? 101.720 166.307 194.894 1.00 94.20  ? 397 SER B N     1 
ATOM   7098  C  CA    . SER B 2 397 ? 102.039 167.486 194.105 1.00 90.48  ? 397 SER B CA    1 
ATOM   7099  C  C     . SER B 2 397 ? 100.821 167.950 193.312 1.00 91.75  ? 397 SER B C     1 
ATOM   7100  O  O     . SER B 2 397 ? 99.880  167.192 193.059 1.00 100.74 ? 397 SER B O     1 
ATOM   7101  C  CB    . SER B 2 397 ? 103.202 167.197 193.157 1.00 93.01  ? 397 SER B CB    1 
ATOM   7102  O  OG    . SER B 2 397 ? 103.666 168.386 192.543 1.00 95.10  ? 397 SER B OG    1 
ATOM   7103  N  N     . VAL B 2 398 ? 100.849 169.226 192.921 1.00 92.31  ? 398 VAL B N     1 
ATOM   7104  C  CA    . VAL B 2 398 ? 99.726  169.809 192.191 1.00 95.51  ? 398 VAL B CA    1 
ATOM   7105  C  C     . VAL B 2 398 ? 99.540  169.107 190.851 1.00 93.67  ? 398 VAL B C     1 
ATOM   7106  O  O     . VAL B 2 398 ? 98.418  168.764 190.461 1.00 104.49 ? 398 VAL B O     1 
ATOM   7107  C  CB    . VAL B 2 398 ? 99.935  171.323 192.010 1.00 92.47  ? 398 VAL B CB    1 
ATOM   7108  C  CG1   . VAL B 2 398 ? 98.651  171.981 191.530 1.00 94.87  ? 398 VAL B CG1   1 
ATOM   7109  C  CG2   . VAL B 2 398 ? 100.411 171.948 193.309 1.00 96.17  ? 398 VAL B CG2   1 
ATOM   7110  N  N     . ASP B 2 399 ? 100.639 168.886 190.126 1.00 94.12  ? 399 ASP B N     1 
ATOM   7111  C  CA    . ASP B 2 399 ? 100.546 168.215 188.834 1.00 100.83 ? 399 ASP B CA    1 
ATOM   7112  C  C     . ASP B 2 399 ? 100.088 166.770 188.989 1.00 105.71 ? 399 ASP B C     1 
ATOM   7113  O  O     . ASP B 2 399 ? 99.270  166.285 188.199 1.00 110.75 ? 399 ASP B O     1 
ATOM   7114  C  CB    . ASP B 2 399 ? 101.891 168.279 188.110 1.00 102.95 ? 399 ASP B CB    1 
ATOM   7115  C  CG    . ASP B 2 399 ? 103.033 167.754 188.956 1.00 109.43 ? 399 ASP B CG    1 
ATOM   7116  O  OD1   . ASP B 2 399 ? 103.581 168.530 189.766 1.00 111.70 ? 399 ASP B OD1   1 
ATOM   7117  O  OD2   . ASP B 2 399 ? 103.383 166.564 188.810 1.00 112.21 ? 399 ASP B OD2   1 
ATOM   7118  N  N     . ALA B 2 400 ? 100.608 166.064 189.996 1.00 97.69  ? 400 ALA B N     1 
ATOM   7119  C  CA    . ALA B 2 400 ? 100.217 164.674 190.204 1.00 97.01  ? 400 ALA B CA    1 
ATOM   7120  C  C     . ALA B 2 400 ? 98.749  164.561 190.596 1.00 99.79  ? 400 ALA B C     1 
ATOM   7121  O  O     . ALA B 2 400 ? 98.041  163.667 190.119 1.00 105.10 ? 400 ALA B O     1 
ATOM   7122  C  CB    . ALA B 2 400 ? 101.107 164.031 191.267 1.00 98.58  ? 400 ALA B CB    1 
ATOM   7123  N  N     . ILE B 2 401 ? 98.276  165.454 191.468 1.00 100.89 ? 401 ILE B N     1 
ATOM   7124  C  CA    . ILE B 2 401 ? 96.882  165.401 191.897 1.00 102.28 ? 401 ILE B CA    1 
ATOM   7125  C  C     . ILE B 2 401 ? 95.953  165.788 190.753 1.00 105.42 ? 401 ILE B C     1 
ATOM   7126  O  O     . ILE B 2 401 ? 94.919  165.146 190.532 1.00 106.60 ? 401 ILE B O     1 
ATOM   7127  C  CB    . ILE B 2 401 ? 96.671  166.294 193.133 1.00 98.93  ? 401 ILE B CB    1 
ATOM   7128  C  CG1   . ILE B 2 401 ? 97.311  165.653 194.364 1.00 100.04 ? 401 ILE B CG1   1 
ATOM   7129  C  CG2   . ILE B 2 401 ? 95.191  166.533 193.378 1.00 103.68 ? 401 ILE B CG2   1 
ATOM   7130  C  CD1   . ILE B 2 401 ? 96.827  164.247 194.639 1.00 98.86  ? 401 ILE B CD1   1 
ATOM   7131  N  N     . ARG B 2 402 ? 96.305  166.837 190.005 1.00 105.34 ? 402 ARG B N     1 
ATOM   7132  C  CA    . ARG B 2 402 ? 95.462  167.269 188.894 1.00 100.48 ? 402 ARG B CA    1 
ATOM   7133  C  C     . ARG B 2 402 ? 95.337  166.178 187.839 1.00 103.67 ? 402 ARG B C     1 
ATOM   7134  O  O     . ARG B 2 402 ? 94.240  165.922 187.328 1.00 111.99 ? 402 ARG B O     1 
ATOM   7135  C  CB    . ARG B 2 402 ? 96.019  168.553 188.279 1.00 101.53 ? 402 ARG B CB    1 
ATOM   7136  C  CG    . ARG B 2 402 ? 95.612  168.775 186.831 1.00 102.18 ? 402 ARG B CG    1 
ATOM   7137  C  CD    . ARG B 2 402 ? 96.243  170.033 186.258 1.00 103.72 ? 402 ARG B CD    1 
ATOM   7138  N  NE    . ARG B 2 402 ? 95.790  171.235 186.948 1.00 105.02 ? 402 ARG B NE    1 
ATOM   7139  C  CZ    . ARG B 2 402 ? 96.597  172.165 187.440 1.00 106.57 ? 402 ARG B CZ    1 
ATOM   7140  N  NH1   . ARG B 2 402 ? 97.911  172.067 187.334 1.00 106.93 ? 402 ARG B NH1   1 
ATOM   7141  N  NH2   . ARG B 2 402 ? 96.070  173.222 188.052 1.00 103.56 ? 402 ARG B NH2   1 
ATOM   7142  N  N     . ARG B 2 403 ? 96.449  165.521 187.502 1.00 108.12 ? 403 ARG B N     1 
ATOM   7143  C  CA    . ARG B 2 403 ? 96.393  164.428 186.536 1.00 111.72 ? 403 ARG B CA    1 
ATOM   7144  C  C     . ARG B 2 403 ? 95.545  163.275 187.058 1.00 115.18 ? 403 ARG B C     1 
ATOM   7145  O  O     . ARG B 2 403 ? 94.757  162.685 186.310 1.00 121.58 ? 403 ARG B O     1 
ATOM   7146  C  CB    . ARG B 2 403 ? 97.806  163.950 186.204 1.00 110.84 ? 403 ARG B CB    1 
ATOM   7147  C  CG    . ARG B 2 403 ? 97.853  162.679 185.374 1.00 111.23 ? 403 ARG B CG    1 
ATOM   7148  C  CD    . ARG B 2 403 ? 98.967  161.756 185.840 1.00 112.19 ? 403 ARG B CD    1 
ATOM   7149  N  NE    . ARG B 2 403 ? 100.206 162.480 186.098 1.00 116.30 ? 403 ARG B NE    1 
ATOM   7150  C  CZ    . ARG B 2 403 ? 101.019 162.939 185.156 1.00 117.16 ? 403 ARG B CZ    1 
ATOM   7151  N  NH1   . ARG B 2 403 ? 100.760 162.760 183.871 1.00 118.59 ? 403 ARG B NH1   1 
ATOM   7152  N  NH2   . ARG B 2 403 ? 102.121 163.594 185.512 1.00 113.71 ? 403 ARG B NH2   1 
ATOM   7153  N  N     . HIS B 2 404 ? 95.694  162.939 188.341 1.00 105.50 ? 404 HIS B N     1 
ATOM   7154  C  CA    . HIS B 2 404 ? 94.878  161.882 188.930 1.00 105.91 ? 404 HIS B CA    1 
ATOM   7155  C  C     . HIS B 2 404 ? 93.407  162.277 188.972 1.00 109.86 ? 404 HIS B C     1 
ATOM   7156  O  O     . HIS B 2 404 ? 92.528  161.443 188.722 1.00 111.64 ? 404 HIS B O     1 
ATOM   7157  C  CB    . HIS B 2 404 ? 95.389  161.547 190.331 1.00 104.52 ? 404 HIS B CB    1 
ATOM   7158  C  CG    . HIS B 2 404 ? 94.353  160.943 191.225 1.00 107.53 ? 404 HIS B CG    1 
ATOM   7159  N  ND1   . HIS B 2 404 ? 93.590  161.693 192.095 1.00 110.88 ? 404 HIS B ND1   1 
ATOM   7160  C  CD2   . HIS B 2 404 ? 93.955  159.659 191.388 1.00 108.44 ? 404 HIS B CD2   1 
ATOM   7161  C  CE1   . HIS B 2 404 ? 92.766  160.897 192.753 1.00 109.26 ? 404 HIS B CE1   1 
ATOM   7162  N  NE2   . HIS B 2 404 ? 92.968  159.658 192.343 1.00 110.37 ? 404 HIS B NE2   1 
ATOM   7163  N  N     . VAL B 2 405 ? 93.119  163.539 189.293 1.00 117.61 ? 405 VAL B N     1 
ATOM   7164  C  CA    . VAL B 2 405 ? 91.735  164.001 189.345 1.00 118.40 ? 405 VAL B CA    1 
ATOM   7165  C  C     . VAL B 2 405 ? 91.106  163.960 187.957 1.00 121.19 ? 405 VAL B C     1 
ATOM   7166  O  O     . VAL B 2 405 ? 89.971  163.500 187.785 1.00 122.83 ? 405 VAL B O     1 
ATOM   7167  C  CB    . VAL B 2 405 ? 91.663  165.411 189.959 1.00 117.25 ? 405 VAL B CB    1 
ATOM   7168  C  CG1   . VAL B 2 405 ? 90.369  166.106 189.562 1.00 118.23 ? 405 VAL B CG1   1 
ATOM   7169  C  CG2   . VAL B 2 405 ? 91.784  165.334 191.472 1.00 117.32 ? 405 VAL B CG2   1 
ATOM   7170  N  N     . GLU B 2 406 ? 91.836  164.436 186.944 1.00 127.86 ? 406 GLU B N     1 
ATOM   7171  C  CA    . GLU B 2 406 ? 91.295  164.457 185.589 1.00 126.06 ? 406 GLU B CA    1 
ATOM   7172  C  C     . GLU B 2 406 ? 91.018  163.048 185.079 1.00 127.06 ? 406 GLU B C     1 
ATOM   7173  O  O     . GLU B 2 406 ? 89.992  162.805 184.432 1.00 128.12 ? 406 GLU B O     1 
ATOM   7174  C  CB    . GLU B 2 406 ? 92.253  165.188 184.649 1.00 125.74 ? 406 GLU B CB    1 
ATOM   7175  C  CG    . GLU B 2 406 ? 92.325  166.694 184.867 1.00 125.73 ? 406 GLU B CG    1 
ATOM   7176  C  CD    . GLU B 2 406 ? 91.015  167.281 185.355 1.00 126.61 ? 406 GLU B CD    1 
ATOM   7177  O  OE1   . GLU B 2 406 ? 90.126  167.534 184.514 1.00 128.82 ? 406 GLU B OE1   1 
ATOM   7178  O  OE2   . GLU B 2 406 ? 90.877  167.500 186.577 1.00 124.72 ? 406 GLU B OE2   1 
ATOM   7179  N  N     . ALA B 2 407 ? 91.925  162.107 185.352 1.00 127.22 ? 407 ALA B N     1 
ATOM   7180  C  CA    . ALA B 2 407 ? 91.702  160.727 184.934 1.00 128.96 ? 407 ALA B CA    1 
ATOM   7181  C  C     . ALA B 2 407 ? 90.483  160.130 185.627 1.00 131.57 ? 407 ALA B C     1 
ATOM   7182  O  O     . ALA B 2 407 ? 89.668  159.452 184.992 1.00 132.12 ? 407 ALA B O     1 
ATOM   7183  C  CB    . ALA B 2 407 ? 92.946  159.885 185.214 1.00 125.79 ? 407 ALA B CB    1 
ATOM   7184  N  N     . ASN B 2 408 ? 90.343  160.371 186.932 1.00 131.90 ? 408 ASN B N     1 
ATOM   7185  C  CA    . ASN B 2 408 ? 89.173  159.882 187.654 1.00 131.50 ? 408 ASN B CA    1 
ATOM   7186  C  C     . ASN B 2 408 ? 87.925  160.655 187.242 1.00 132.12 ? 408 ASN B C     1 
ATOM   7187  O  O     . ASN B 2 408 ? 86.878  160.061 186.957 1.00 131.04 ? 408 ASN B O     1 
ATOM   7188  C  CB    . ASN B 2 408 ? 89.414  159.988 189.163 1.00 130.23 ? 408 ASN B CB    1 
ATOM   7189  C  CG    . ASN B 2 408 ? 88.324  159.319 189.993 1.00 129.38 ? 408 ASN B CG    1 
ATOM   7190  O  OD1   . ASN B 2 408 ? 87.167  159.226 189.583 1.00 129.54 ? 408 ASN B OD1   1 
ATOM   7191  N  ND2   . ASN B 2 408 ? 88.699  158.848 191.176 1.00 128.07 ? 408 ASN B ND2   1 
ATOM   7192  N  N     . GLY B 2 409 ? 88.021  161.973 187.195 1.00 134.42 ? 409 GLY B N     1 
ATOM   7193  C  CA    . GLY B 2 409 ? 86.895  162.828 186.863 1.00 131.47 ? 409 GLY B CA    1 
ATOM   7194  C  C     . GLY B 2 409 ? 86.888  164.046 187.764 1.00 132.69 ? 409 GLY B C     1 
ATOM   7195  O  O     . GLY B 2 409 ? 87.362  164.018 188.901 1.00 133.22 ? 409 GLY B O     1 
ATOM   7196  N  N     . GLY B 2 410 ? 86.339  165.138 187.252 1.00 138.23 ? 410 GLY B N     1 
ATOM   7197  C  CA    . GLY B 2 410 ? 86.285  166.395 187.970 1.00 138.68 ? 410 GLY B CA    1 
ATOM   7198  C  C     . GLY B 2 410 ? 87.239  167.418 187.377 1.00 140.80 ? 410 GLY B C     1 
ATOM   7199  O  O     . GLY B 2 410 ? 88.037  167.132 186.483 1.00 140.26 ? 410 GLY B O     1 
ATOM   7200  N  N     . HIS B 2 411 ? 87.133  168.636 187.903 1.00 150.70 ? 411 HIS B N     1 
ATOM   7201  C  CA    . HIS B 2 411 ? 87.930  169.758 187.435 1.00 151.34 ? 411 HIS B CA    1 
ATOM   7202  C  C     . HIS B 2 411 ? 88.447  170.534 188.637 1.00 149.04 ? 411 HIS B C     1 
ATOM   7203  O  O     . HIS B 2 411 ? 87.752  170.675 189.648 1.00 148.95 ? 411 HIS B O     1 
ATOM   7204  C  CB    . HIS B 2 411 ? 87.103  170.656 186.499 1.00 150.13 ? 411 HIS B CB    1 
ATOM   7205  C  CG    . HIS B 2 411 ? 87.551  172.084 186.462 1.00 153.47 ? 411 HIS B CG    1 
ATOM   7206  N  ND1   . HIS B 2 411 ? 86.713  173.132 186.776 1.00 152.69 ? 411 HIS B ND1   1 
ATOM   7207  C  CD2   . HIS B 2 411 ? 88.737  172.640 186.118 1.00 152.89 ? 411 HIS B CD2   1 
ATOM   7208  C  CE1   . HIS B 2 411 ? 87.369  174.271 186.646 1.00 151.29 ? 411 HIS B CE1   1 
ATOM   7209  N  NE2   . HIS B 2 411 ? 88.600  174.000 186.249 1.00 151.85 ? 411 HIS B NE2   1 
ATOM   7210  N  N     . PHE B 2 412 ? 89.671  171.037 188.520 1.00 124.72 ? 412 PHE B N     1 
ATOM   7211  C  CA    . PHE B 2 412 ? 90.275  171.788 189.615 1.00 127.22 ? 412 PHE B CA    1 
ATOM   7212  C  C     . PHE B 2 412 ? 89.537  173.106 189.813 1.00 129.97 ? 412 PHE B C     1 
ATOM   7213  O  O     . PHE B 2 412 ? 89.387  173.876 188.857 1.00 128.72 ? 412 PHE B O     1 
ATOM   7214  C  CB    . PHE B 2 412 ? 91.754  172.055 189.338 1.00 129.10 ? 412 PHE B CB    1 
ATOM   7215  C  CG    . PHE B 2 412 ? 92.687  171.154 190.095 1.00 128.50 ? 412 PHE B CG    1 
ATOM   7216  C  CD1   . PHE B 2 412 ? 92.332  169.848 190.384 1.00 130.73 ? 412 PHE B CD1   1 
ATOM   7217  C  CD2   . PHE B 2 412 ? 93.919  171.619 190.524 1.00 121.84 ? 412 PHE B CD2   1 
ATOM   7218  C  CE1   . PHE B 2 412 ? 93.191  169.021 191.082 1.00 127.96 ? 412 PHE B CE1   1 
ATOM   7219  C  CE2   . PHE B 2 412 ? 94.781  170.799 191.222 1.00 124.76 ? 412 PHE B CE2   1 
ATOM   7220  C  CZ    . PHE B 2 412 ? 94.417  169.498 191.501 1.00 127.20 ? 412 PHE B CZ    1 
ATOM   7221  N  N     . PRO B 2 413 ? 89.068  173.404 191.024 1.00 140.26 ? 413 PRO B N     1 
ATOM   7222  C  CA    . PRO B 2 413 ? 88.382  174.679 191.256 1.00 137.76 ? 413 PRO B CA    1 
ATOM   7223  C  C     . PRO B 2 413 ? 89.293  175.862 190.966 1.00 138.51 ? 413 PRO B C     1 
ATOM   7224  O  O     . PRO B 2 413 ? 90.510  175.802 191.154 1.00 140.88 ? 413 PRO B O     1 
ATOM   7225  C  CB    . PRO B 2 413 ? 88.001  174.615 192.740 1.00 137.63 ? 413 PRO B CB    1 
ATOM   7226  C  CG    . PRO B 2 413 ? 87.994  173.157 193.068 1.00 139.16 ? 413 PRO B CG    1 
ATOM   7227  C  CD    . PRO B 2 413 ? 89.067  172.546 192.220 1.00 139.77 ? 413 PRO B CD    1 
ATOM   7228  N  N     . THR B 2 414 ? 88.679  176.947 190.487 1.00 140.08 ? 414 THR B N     1 
ATOM   7229  C  CA    . THR B 2 414 ? 89.442  178.139 190.130 1.00 142.74 ? 414 THR B CA    1 
ATOM   7230  C  C     . THR B 2 414 ? 90.147  178.727 191.347 1.00 144.72 ? 414 THR B C     1 
ATOM   7231  O  O     . THR B 2 414 ? 91.312  179.135 191.262 1.00 144.59 ? 414 THR B O     1 
ATOM   7232  C  CB    . THR B 2 414 ? 88.517  179.172 189.484 1.00 141.36 ? 414 THR B CB    1 
ATOM   7233  O  OG1   . THR B 2 414 ? 88.246  178.788 188.130 1.00 142.33 ? 414 THR B OG1   1 
ATOM   7234  C  CG2   . THR B 2 414 ? 89.152  180.555 189.492 1.00 140.56 ? 414 THR B CG2   1 
ATOM   7235  N  N     . ASP B 2 415 ? 89.462  178.767 192.492 1.00 147.70 ? 415 ASP B N     1 
ATOM   7236  C  CA    . ASP B 2 415 ? 90.078  179.293 193.706 1.00 148.22 ? 415 ASP B CA    1 
ATOM   7237  C  C     . ASP B 2 415 ? 91.267  178.443 194.135 1.00 148.39 ? 415 ASP B C     1 
ATOM   7238  O  O     . ASP B 2 415 ? 92.270  178.971 194.630 1.00 148.01 ? 415 ASP B O     1 
ATOM   7239  C  CB    . ASP B 2 415 ? 89.042  179.375 194.827 1.00 146.77 ? 415 ASP B CB    1 
ATOM   7240  C  CG    . ASP B 2 415 ? 88.213  178.112 194.947 1.00 147.23 ? 415 ASP B CG    1 
ATOM   7241  O  OD1   . ASP B 2 415 ? 88.702  177.132 195.546 1.00 148.67 ? 415 ASP B OD1   1 
ATOM   7242  O  OD2   . ASP B 2 415 ? 87.072  178.099 194.440 1.00 146.33 ? 415 ASP B OD2   1 
ATOM   7243  N  N     . VAL B 2 416 ? 91.172  177.123 193.956 1.00 138.09 ? 416 VAL B N     1 
ATOM   7244  C  CA    . VAL B 2 416 ? 92.270  176.236 194.332 1.00 134.72 ? 416 VAL B CA    1 
ATOM   7245  C  C     . VAL B 2 416 ? 93.516  176.548 193.513 1.00 134.54 ? 416 VAL B C     1 
ATOM   7246  O  O     . VAL B 2 416 ? 94.630  176.608 194.047 1.00 135.43 ? 416 VAL B O     1 
ATOM   7247  C  CB    . VAL B 2 416 ? 91.844  174.765 194.175 1.00 133.65 ? 416 VAL B CB    1 
ATOM   7248  C  CG1   . VAL B 2 416 ? 93.036  173.839 194.361 1.00 134.07 ? 416 VAL B CG1   1 
ATOM   7249  C  CG2   . VAL B 2 416 ? 90.747  174.427 195.167 1.00 134.35 ? 416 VAL B CG2   1 
ATOM   7250  N  N     . ASP B 2 417 ? 93.349  176.756 192.204 1.00 128.98 ? 417 ASP B N     1 
ATOM   7251  C  CA    . ASP B 2 417 ? 94.492  177.080 191.356 1.00 128.70 ? 417 ASP B CA    1 
ATOM   7252  C  C     . ASP B 2 417 ? 95.125  178.403 191.769 1.00 129.37 ? 417 ASP B C     1 
ATOM   7253  O  O     . ASP B 2 417 ? 96.354  178.539 191.765 1.00 132.82 ? 417 ASP B O     1 
ATOM   7254  C  CB    . ASP B 2 417 ? 94.063  177.121 189.890 1.00 130.06 ? 417 ASP B CB    1 
ATOM   7255  C  CG    . ASP B 2 417 ? 94.555  175.921 189.107 1.00 133.24 ? 417 ASP B CG    1 
ATOM   7256  O  OD1   . ASP B 2 417 ? 94.861  174.886 189.735 1.00 129.99 ? 417 ASP B OD1   1 
ATOM   7257  O  OD2   . ASP B 2 417 ? 94.635  176.011 187.865 1.00 134.61 ? 417 ASP B OD2   1 
ATOM   7258  N  N     . GLN B 2 418 ? 94.301  179.392 192.120 1.00 126.15 ? 418 GLN B N     1 
ATOM   7259  C  CA    . GLN B 2 418 ? 94.835  180.653 192.623 1.00 127.77 ? 418 GLN B CA    1 
ATOM   7260  C  C     . GLN B 2 418 ? 95.565  180.443 193.945 1.00 128.69 ? 418 GLN B C     1 
ATOM   7261  O  O     . GLN B 2 418 ? 96.628  181.032 194.177 1.00 131.48 ? 418 GLN B O     1 
ATOM   7262  C  CB    . GLN B 2 418 ? 93.702  181.674 192.771 1.00 127.77 ? 418 GLN B CB    1 
ATOM   7263  C  CG    . GLN B 2 418 ? 94.130  183.121 193.039 1.00 128.86 ? 418 GLN B CG    1 
ATOM   7264  C  CD    . GLN B 2 418 ? 94.695  183.343 194.431 1.00 131.26 ? 418 GLN B CD    1 
ATOM   7265  O  OE1   . GLN B 2 418 ? 94.134  182.876 195.422 1.00 132.01 ? 418 GLN B OE1   1 
ATOM   7266  N  NE2   . GLN B 2 418 ? 95.811  184.058 194.510 1.00 128.79 ? 418 GLN B NE2   1 
ATOM   7267  N  N     . LYS B 2 419 ? 95.008  179.605 194.824 1.00 118.73 ? 419 LYS B N     1 
ATOM   7268  C  CA    . LYS B 2 419 ? 95.657  179.332 196.103 1.00 117.12 ? 419 LYS B CA    1 
ATOM   7269  C  C     . LYS B 2 419 ? 97.002  178.644 195.906 1.00 119.37 ? 419 LYS B C     1 
ATOM   7270  O  O     . LYS B 2 419 ? 97.964  178.930 196.629 1.00 119.48 ? 419 LYS B O     1 
ATOM   7271  C  CB    . LYS B 2 419 ? 94.744  178.482 196.985 1.00 116.36 ? 419 LYS B CB    1 
ATOM   7272  C  CG    . LYS B 2 419 ? 93.560  179.238 197.565 1.00 119.14 ? 419 LYS B CG    1 
ATOM   7273  C  CD    . LYS B 2 419 ? 92.392  178.306 197.840 1.00 121.93 ? 419 LYS B CD    1 
ATOM   7274  C  CE    . LYS B 2 419 ? 91.139  179.086 198.202 1.00 122.46 ? 419 LYS B CE    1 
ATOM   7275  N  NZ    . LYS B 2 419 ? 89.957  178.196 198.361 1.00 120.45 ? 419 LYS B NZ    1 
ATOM   7276  N  N     . VAL B 2 420 ? 97.087  177.728 194.938 1.00 107.57 ? 420 VAL B N     1 
ATOM   7277  C  CA    . VAL B 2 420 ? 98.347  177.039 194.668 1.00 105.06 ? 420 VAL B CA    1 
ATOM   7278  C  C     . VAL B 2 420 ? 99.419  178.039 194.255 1.00 106.17 ? 420 VAL B C     1 
ATOM   7279  O  O     . VAL B 2 420 ? 100.559 177.989 194.731 1.00 109.42 ? 420 VAL B O     1 
ATOM   7280  C  CB    . VAL B 2 420 ? 98.145  175.954 193.596 1.00 102.13 ? 420 VAL B CB    1 
ATOM   7281  C  CG1   . VAL B 2 420 ? 99.484  175.494 193.044 1.00 102.01 ? 420 VAL B CG1   1 
ATOM   7282  C  CG2   . VAL B 2 420 ? 97.374  174.780 194.170 1.00 102.19 ? 420 VAL B CG2   1 
ATOM   7283  N  N     . ASP B 2 421 ? 99.065  178.969 193.365 1.00 113.23 ? 421 ASP B N     1 
ATOM   7284  C  CA    . ASP B 2 421 ? 100.021 179.985 192.938 1.00 111.45 ? 421 ASP B CA    1 
ATOM   7285  C  C     . ASP B 2 421 ? 100.414 180.894 194.095 1.00 110.81 ? 421 ASP B C     1 
ATOM   7286  O  O     . ASP B 2 421 ? 101.578 181.298 194.209 1.00 114.19 ? 421 ASP B O     1 
ATOM   7287  C  CB    . ASP B 2 421 ? 99.435  180.803 191.788 1.00 115.70 ? 421 ASP B CB    1 
ATOM   7288  C  CG    . ASP B 2 421 ? 99.564  180.103 190.451 1.00 118.20 ? 421 ASP B CG    1 
ATOM   7289  O  OD1   . ASP B 2 421 ? 99.587  178.854 190.433 1.00 116.00 ? 421 ASP B OD1   1 
ATOM   7290  O  OD2   . ASP B 2 421 ? 99.641  180.801 189.418 1.00 120.47 ? 421 ASP B OD2   1 
ATOM   7291  N  N     . GLN B 2 422 ? 99.455  181.233 194.959 1.00 108.06 ? 422 GLN B N     1 
ATOM   7292  C  CA    . GLN B 2 422 ? 99.741  182.134 196.072 1.00 107.58 ? 422 GLN B CA    1 
ATOM   7293  C  C     . GLN B 2 422 ? 100.731 181.508 197.047 1.00 111.35 ? 422 GLN B C     1 
ATOM   7294  O  O     . GLN B 2 422 ? 101.712 182.145 197.447 1.00 112.89 ? 422 GLN B O     1 
ATOM   7295  C  CB    . GLN B 2 422 ? 98.439  182.509 196.783 1.00 109.87 ? 422 GLN B CB    1 
ATOM   7296  C  CG    . GLN B 2 422 ? 98.408  183.922 197.355 1.00 112.07 ? 422 GLN B CG    1 
ATOM   7297  C  CD    . GLN B 2 422 ? 98.885  183.998 198.795 1.00 114.80 ? 422 GLN B CD    1 
ATOM   7298  O  OE1   . GLN B 2 422 ? 99.787  183.270 199.206 1.00 115.25 ? 422 GLN B OE1   1 
ATOM   7299  N  NE2   . GLN B 2 422 ? 98.276  184.888 199.570 1.00 112.83 ? 422 GLN B NE2   1 
ATOM   7300  N  N     . VAL B 2 423 ? 100.493 180.253 197.439 1.00 99.58  ? 423 VAL B N     1 
ATOM   7301  C  CA    . VAL B 2 423 ? 101.363 179.609 198.415 1.00 94.17  ? 423 VAL B CA    1 
ATOM   7302  C  C     . VAL B 2 423 ? 102.710 179.227 197.816 1.00 95.98  ? 423 VAL B C     1 
ATOM   7303  O  O     . VAL B 2 423 ? 103.671 179.001 198.560 1.00 102.17 ? 423 VAL B O     1 
ATOM   7304  C  CB    . VAL B 2 423 ? 100.675 178.373 199.024 1.00 90.35  ? 423 VAL B CB    1 
ATOM   7305  C  CG1   . VAL B 2 423 ? 99.370  178.770 199.693 1.00 96.59  ? 423 VAL B CG1   1 
ATOM   7306  C  CG2   . VAL B 2 423 ? 100.436 177.320 197.960 1.00 94.45  ? 423 VAL B CG2   1 
ATOM   7307  N  N     . ALA B 2 424 ? 102.809 179.140 196.492 1.00 91.18  ? 424 ALA B N     1 
ATOM   7308  C  CA    . ALA B 2 424 ? 104.078 178.853 195.840 1.00 87.73  ? 424 ALA B CA    1 
ATOM   7309  C  C     . ALA B 2 424 ? 104.876 180.107 195.514 1.00 89.45  ? 424 ALA B C     1 
ATOM   7310  O  O     . ALA B 2 424 ? 106.033 179.994 195.096 1.00 90.98  ? 424 ALA B O     1 
ATOM   7311  C  CB    . ALA B 2 424 ? 103.845 178.050 194.556 1.00 88.71  ? 424 ALA B CB    1 
ATOM   7312  N  N     . ARG B 2 425 ? 104.290 181.293 195.692 1.00 99.46  ? 425 ARG B N     1 
ATOM   7313  C  CA    . ARG B 2 425 ? 105.000 182.524 195.364 1.00 98.90  ? 425 ARG B CA    1 
ATOM   7314  C  C     . ARG B 2 425 ? 106.097 182.824 196.378 1.00 101.49 ? 425 ARG B C     1 
ATOM   7315  O  O     . ARG B 2 425 ? 107.216 183.189 195.998 1.00 103.72 ? 425 ARG B O     1 
ATOM   7316  C  CB    . ARG B 2 425 ? 104.015 183.688 195.276 1.00 98.96  ? 425 ARG B CB    1 
ATOM   7317  C  CG    . ARG B 2 425 ? 104.528 184.873 194.475 1.00 101.04 ? 425 ARG B CG    1 
ATOM   7318  C  CD    . ARG B 2 425 ? 104.437 184.613 192.981 1.00 100.89 ? 425 ARG B CD    1 
ATOM   7319  N  NE    . ARG B 2 425 ? 103.116 184.140 192.586 1.00 104.86 ? 425 ARG B NE    1 
ATOM   7320  C  CZ    . ARG B 2 425 ? 102.786 183.788 191.351 1.00 105.62 ? 425 ARG B CZ    1 
ATOM   7321  N  NH1   . ARG B 2 425 ? 103.660 183.845 190.359 1.00 100.84 ? 425 ARG B NH1   1 
ATOM   7322  N  NH2   . ARG B 2 425 ? 101.548 183.370 191.104 1.00 107.41 ? 425 ARG B NH2   1 
ATOM   7323  N  N     . GLN B 2 426 ? 105.799 182.680 197.671 1.00 97.34  ? 426 GLN B N     1 
ATOM   7324  C  CA    . GLN B 2 426 ? 106.805 182.972 198.688 1.00 101.40 ? 426 GLN B CA    1 
ATOM   7325  C  C     . GLN B 2 426 ? 107.882 181.897 198.743 1.00 102.93 ? 426 GLN B C     1 
ATOM   7326  O  O     . GLN B 2 426 ? 109.039 182.198 199.056 1.00 104.35 ? 426 GLN B O     1 
ATOM   7327  C  CB    . GLN B 2 426 ? 106.146 183.135 200.058 1.00 98.56  ? 426 GLN B CB    1 
ATOM   7328  C  CG    . GLN B 2 426 ? 104.752 183.735 200.013 1.00 97.67  ? 426 GLN B CG    1 
ATOM   7329  C  CD    . GLN B 2 426 ? 103.668 182.681 200.050 1.00 104.21 ? 426 GLN B CD    1 
ATOM   7330  O  OE1   . GLN B 2 426 ? 103.750 181.670 199.357 1.00 106.67 ? 426 GLN B OE1   1 
ATOM   7331  N  NE2   . GLN B 2 426 ? 102.644 182.912 200.863 1.00 104.36 ? 426 GLN B NE2   1 
ATOM   7332  N  N     . GLY B 2 427 ? 107.530 180.648 198.448 1.00 88.22  ? 427 GLY B N     1 
ATOM   7333  C  CA    . GLY B 2 427 ? 108.510 179.581 198.437 1.00 87.06  ? 427 GLY B CA    1 
ATOM   7334  C  C     . GLY B 2 427 ? 108.002 178.273 199.007 1.00 88.66  ? 427 GLY B C     1 
ATOM   7335  O  O     . GLY B 2 427 ? 108.653 177.235 198.865 1.00 93.59  ? 427 GLY B O     1 
ATOM   7336  N  N     . ALA B 2 428 ? 106.842 178.309 199.656 1.00 76.48  ? 428 ALA B N     1 
ATOM   7337  C  CA    . ALA B 2 428 ? 106.272 177.098 200.227 1.00 73.12  ? 428 ALA B CA    1 
ATOM   7338  C  C     . ALA B 2 428 ? 105.817 176.149 199.126 1.00 73.78  ? 428 ALA B C     1 
ATOM   7339  O  O     . ALA B 2 428 ? 105.206 176.565 198.138 1.00 86.67  ? 428 ALA B O     1 
ATOM   7340  C  CB    . ALA B 2 428 ? 105.100 177.443 201.143 1.00 72.88  ? 428 ALA B CB    1 
ATOM   7341  N  N     . THR B 2 429 ? 106.121 174.869 199.299 1.00 69.77  ? 429 THR B N     1 
ATOM   7342  C  CA    . THR B 2 429 ? 105.708 173.862 198.331 1.00 72.16  ? 429 THR B CA    1 
ATOM   7343  C  C     . THR B 2 429 ? 104.241 173.515 198.548 1.00 74.85  ? 429 THR B C     1 
ATOM   7344  O  O     . THR B 2 429 ? 103.865 173.134 199.662 1.00 84.70  ? 429 THR B O     1 
ATOM   7345  C  CB    . THR B 2 429 ? 106.565 172.610 198.455 1.00 74.88  ? 429 THR B CB    1 
ATOM   7346  O  OG1   . THR B 2 429 ? 106.044 171.774 199.496 1.00 78.66  ? 429 THR B OG1   1 
ATOM   7347  C  CG2   . THR B 2 429 ? 108.003 172.980 198.779 1.00 74.50  ? 429 THR B CG2   1 
ATOM   7348  N  N     . PRO B 2 430 ? 103.388 173.631 197.530 1.00 74.42  ? 430 PRO B N     1 
ATOM   7349  C  CA    . PRO B 2 430 ? 101.958 173.359 197.727 1.00 72.19  ? 430 PRO B CA    1 
ATOM   7350  C  C     . PRO B 2 430 ? 101.666 171.867 197.649 1.00 76.88  ? 430 PRO B C     1 
ATOM   7351  O  O     . PRO B 2 430 ? 102.054 171.193 196.693 1.00 80.72  ? 430 PRO B O     1 
ATOM   7352  C  CB    . PRO B 2 430 ? 101.285 174.117 196.574 1.00 78.18  ? 430 PRO B CB    1 
ATOM   7353  C  CG    . PRO B 2 430 ? 102.409 174.728 195.750 1.00 76.16  ? 430 PRO B CG    1 
ATOM   7354  C  CD    . PRO B 2 430 ? 103.680 174.059 196.155 1.00 82.50  ? 430 PRO B CD    1 
ATOM   7355  N  N     . LEU B 2 431 ? 100.979 171.356 198.666 1.00 79.08  ? 431 LEU B N     1 
ATOM   7356  C  CA    . LEU B 2 431 ? 100.489 169.984 198.682 1.00 79.09  ? 431 LEU B CA    1 
ATOM   7357  C  C     . LEU B 2 431 ? 98.974  170.018 198.546 1.00 83.70  ? 431 LEU B C     1 
ATOM   7358  O  O     . LEU B 2 431 ? 98.287  170.616 199.381 1.00 88.20  ? 431 LEU B O     1 
ATOM   7359  C  CB    . LEU B 2 431 ? 100.895 169.264 199.967 1.00 79.34  ? 431 LEU B CB    1 
ATOM   7360  C  CG    . LEU B 2 431 ? 102.244 168.542 199.979 1.00 81.49  ? 431 LEU B CG    1 
ATOM   7361  C  CD1   . LEU B 2 431 ? 102.304 167.556 201.133 1.00 81.93  ? 431 LEU B CD1   1 
ATOM   7362  C  CD2   . LEU B 2 431 ? 102.499 167.839 198.657 1.00 80.02  ? 431 LEU B CD2   1 
ATOM   7363  N  N     . VAL B 2 432 ? 98.458  169.378 197.503 1.00 93.95  ? 432 VAL B N     1 
ATOM   7364  C  CA    . VAL B 2 432 ? 97.026  169.338 197.234 1.00 94.18  ? 432 VAL B CA    1 
ATOM   7365  C  C     . VAL B 2 432 ? 96.487  168.011 197.744 1.00 94.76  ? 432 VAL B C     1 
ATOM   7366  O  O     . VAL B 2 432 ? 96.968  166.943 197.348 1.00 99.15  ? 432 VAL B O     1 
ATOM   7367  C  CB    . VAL B 2 432 ? 96.728  169.519 195.738 1.00 93.66  ? 432 VAL B CB    1 
ATOM   7368  C  CG1   . VAL B 2 432 ? 95.228  169.586 195.503 1.00 91.27  ? 432 VAL B CG1   1 
ATOM   7369  C  CG2   . VAL B 2 432 ? 97.412  170.767 195.209 1.00 97.21  ? 432 VAL B CG2   1 
ATOM   7370  N  N     . VAL B 2 433 ? 95.488  168.075 198.619 1.00 94.74  ? 433 VAL B N     1 
ATOM   7371  C  CA    . VAL B 2 433 ? 94.862  166.894 199.201 1.00 95.82  ? 433 VAL B CA    1 
ATOM   7372  C  C     . VAL B 2 433 ? 93.483  166.729 198.580 1.00 100.17 ? 433 VAL B C     1 
ATOM   7373  O  O     . VAL B 2 433 ? 92.694  167.681 198.536 1.00 103.06 ? 433 VAL B O     1 
ATOM   7374  C  CB    . VAL B 2 433 ? 94.780  166.994 200.735 1.00 97.78  ? 433 VAL B CB    1 
ATOM   7375  C  CG1   . VAL B 2 433 ? 94.240  168.351 201.156 1.00 100.00 ? 433 VAL B CG1   1 
ATOM   7376  C  CG2   . VAL B 2 433 ? 93.918  165.874 201.296 1.00 100.01 ? 433 VAL B CG2   1 
ATOM   7377  N  N     . VAL B 2 434 ? 93.199  165.527 198.087 1.00 108.63 ? 434 VAL B N     1 
ATOM   7378  C  CA    . VAL B 2 434 ? 91.940  165.221 197.422 1.00 108.16 ? 434 VAL B CA    1 
ATOM   7379  C  C     . VAL B 2 434 ? 91.245  164.101 198.183 1.00 110.74 ? 434 VAL B C     1 
ATOM   7380  O  O     . VAL B 2 434 ? 91.901  163.234 198.772 1.00 113.25 ? 434 VAL B O     1 
ATOM   7381  C  CB    . VAL B 2 434 ? 92.157  164.843 195.940 1.00 107.19 ? 434 VAL B CB    1 
ATOM   7382  C  CG1   . VAL B 2 434 ? 92.581  163.387 195.796 1.00 104.65 ? 434 VAL B CG1   1 
ATOM   7383  C  CG2   . VAL B 2 434 ? 90.900  165.119 195.131 1.00 109.29 ? 434 VAL B CG2   1 
ATOM   7384  N  N     . GLU B 2 435 ? 89.918  164.146 198.201 1.00 122.12 ? 435 GLU B N     1 
ATOM   7385  C  CA    . GLU B 2 435 ? 89.089  163.120 198.826 1.00 121.94 ? 435 GLU B CA    1 
ATOM   7386  C  C     . GLU B 2 435 ? 88.261  162.478 197.719 1.00 122.73 ? 435 GLU B C     1 
ATOM   7387  O  O     . GLU B 2 435 ? 87.263  163.047 197.269 1.00 123.70 ? 435 GLU B O     1 
ATOM   7388  C  CB    . GLU B 2 435 ? 88.210  163.718 199.920 1.00 122.59 ? 435 GLU B CB    1 
ATOM   7389  C  CG    . GLU B 2 435 ? 87.249  162.732 200.560 1.00 124.47 ? 435 GLU B CG    1 
ATOM   7390  C  CD    . GLU B 2 435 ? 86.442  163.354 201.682 1.00 125.51 ? 435 GLU B CD    1 
ATOM   7391  O  OE1   . GLU B 2 435 ? 85.729  164.346 201.423 1.00 125.83 ? 435 GLU B OE1   1 
ATOM   7392  O  OE2   . GLU B 2 435 ? 86.523  162.853 202.823 1.00 125.75 ? 435 GLU B OE2   1 
ATOM   7393  N  N     . GLY B 2 436 ? 88.677  161.292 197.283 1.00 122.72 ? 436 GLY B N     1 
ATOM   7394  C  CA    . GLY B 2 436 ? 88.050  160.663 196.139 1.00 124.57 ? 436 GLY B CA    1 
ATOM   7395  C  C     . GLY B 2 436 ? 88.289  161.462 194.876 1.00 127.34 ? 436 GLY B C     1 
ATOM   7396  O  O     . GLY B 2 436 ? 89.406  161.486 194.349 1.00 129.61 ? 436 GLY B O     1 
ATOM   7397  N  N     . SER B 2 437 ? 87.244  162.121 194.377 1.00 122.96 ? 437 SER B N     1 
ATOM   7398  C  CA    . SER B 2 437 ? 87.360  163.017 193.233 1.00 121.64 ? 437 SER B CA    1 
ATOM   7399  C  C     . SER B 2 437 ? 87.055  164.464 193.597 1.00 120.36 ? 437 SER B C     1 
ATOM   7400  O  O     . SER B 2 437 ? 86.864  165.291 192.698 1.00 119.53 ? 437 SER B O     1 
ATOM   7401  C  CB    . SER B 2 437 ? 86.439  162.556 192.100 1.00 122.64 ? 437 SER B CB    1 
ATOM   7402  O  OG    . SER B 2 437 ? 85.081  162.812 192.413 1.00 126.45 ? 437 SER B OG    1 
ATOM   7403  N  N     . ARG B 2 438 ? 87.002  164.792 194.885 1.00 116.84 ? 438 ARG B N     1 
ATOM   7404  C  CA    . ARG B 2 438 ? 86.656  166.128 195.353 1.00 118.02 ? 438 ARG B CA    1 
ATOM   7405  C  C     . ARG B 2 438 ? 87.884  166.769 195.987 1.00 120.93 ? 438 ARG B C     1 
ATOM   7406  O  O     . ARG B 2 438 ? 88.445  166.230 196.947 1.00 121.21 ? 438 ARG B O     1 
ATOM   7407  C  CB    . ARG B 2 438 ? 85.502  166.068 196.353 1.00 117.35 ? 438 ARG B CB    1 
ATOM   7408  C  CG    . ARG B 2 438 ? 85.090  167.415 196.922 1.00 118.62 ? 438 ARG B CG    1 
ATOM   7409  C  CD    . ARG B 2 438 ? 83.764  167.305 197.660 1.00 118.92 ? 438 ARG B CD    1 
ATOM   7410  N  NE    . ARG B 2 438 ? 83.590  168.360 198.653 1.00 119.53 ? 438 ARG B NE    1 
ATOM   7411  C  CZ    . ARG B 2 438 ? 83.236  169.606 198.368 1.00 123.59 ? 438 ARG B CZ    1 
ATOM   7412  N  NH1   . ARG B 2 438 ? 83.018  169.996 197.123 1.00 122.85 ? 438 ARG B NH1   1 
ATOM   7413  N  NH2   . ARG B 2 438 ? 83.094  170.482 199.359 1.00 122.71 ? 438 ARG B NH2   1 
ATOM   7414  N  N     . VAL B 2 439 ? 88.290  167.919 195.456 1.00 118.00 ? 439 VAL B N     1 
ATOM   7415  C  CA    . VAL B 2 439 ? 89.436  168.648 195.989 1.00 115.59 ? 439 VAL B CA    1 
ATOM   7416  C  C     . VAL B 2 439 ? 89.014  169.375 197.257 1.00 117.47 ? 439 VAL B C     1 
ATOM   7417  O  O     . VAL B 2 439 ? 88.007  170.094 197.270 1.00 119.48 ? 439 VAL B O     1 
ATOM   7418  C  CB    . VAL B 2 439 ? 89.991  169.627 194.943 1.00 114.87 ? 439 VAL B CB    1 
ATOM   7419  C  CG1   . VAL B 2 439 ? 91.093  170.482 195.548 1.00 115.67 ? 439 VAL B CG1   1 
ATOM   7420  C  CG2   . VAL B 2 439 ? 90.504  168.869 193.729 1.00 114.30 ? 439 VAL B CG2   1 
ATOM   7421  N  N     . LEU B 2 440 ? 89.783  169.192 198.329 1.00 106.17 ? 440 LEU B N     1 
ATOM   7422  C  CA    . LEU B 2 440 ? 89.443  169.761 199.627 1.00 107.51 ? 440 LEU B CA    1 
ATOM   7423  C  C     . LEU B 2 440 ? 90.245  171.007 199.975 1.00 107.77 ? 440 LEU B C     1 
ATOM   7424  O  O     . LEU B 2 440 ? 89.766  171.835 200.756 1.00 107.95 ? 440 LEU B O     1 
ATOM   7425  C  CB    . LEU B 2 440 ? 89.641  168.716 200.730 1.00 107.99 ? 440 LEU B CB    1 
ATOM   7426  C  CG    . LEU B 2 440 ? 88.729  167.488 200.682 1.00 108.94 ? 440 LEU B CG    1 
ATOM   7427  C  CD1   . LEU B 2 440 ? 88.656  166.825 202.047 1.00 106.00 ? 440 LEU B CD1   1 
ATOM   7428  C  CD2   . LEU B 2 440 ? 87.338  167.861 200.192 1.00 111.14 ? 440 LEU B CD2   1 
ATOM   7429  N  N     . GLY B 2 441 ? 91.440  171.162 199.425 1.00 106.56 ? 441 GLY B N     1 
ATOM   7430  C  CA    . GLY B 2 441 ? 92.249  172.326 199.715 1.00 107.73 ? 441 GLY B CA    1 
ATOM   7431  C  C     . GLY B 2 441 ? 93.716  172.039 199.459 1.00 106.03 ? 441 GLY B C     1 
ATOM   7432  O  O     . GLY B 2 441 ? 94.078  171.031 198.853 1.00 104.46 ? 441 GLY B O     1 
ATOM   7433  N  N     . VAL B 2 442 ? 94.553  172.960 199.939 1.00 94.36  ? 442 VAL B N     1 
ATOM   7434  C  CA    . VAL B 2 442 ? 95.996  172.872 199.771 1.00 93.10  ? 442 VAL B CA    1 
ATOM   7435  C  C     . VAL B 2 442 ? 96.671  173.103 201.116 1.00 97.34  ? 442 VAL B C     1 
ATOM   7436  O  O     . VAL B 2 442 ? 96.121  173.741 202.016 1.00 100.18 ? 442 VAL B O     1 
ATOM   7437  C  CB    . VAL B 2 442 ? 96.526  173.878 198.727 1.00 91.75  ? 442 VAL B CB    1 
ATOM   7438  C  CG1   . VAL B 2 442 ? 96.034  173.508 197.339 1.00 95.65  ? 442 VAL B CG1   1 
ATOM   7439  C  CG2   . VAL B 2 442 ? 96.101  175.291 199.090 1.00 90.61  ? 442 VAL B CG2   1 
ATOM   7440  N  N     . ILE B 2 443 ? 97.884  172.569 201.241 1.00 92.35  ? 443 ILE B N     1 
ATOM   7441  C  CA    . ILE B 2 443 ? 98.697  172.706 202.443 1.00 87.68  ? 443 ILE B CA    1 
ATOM   7442  C  C     . ILE B 2 443 ? 100.026 173.334 202.051 1.00 83.49  ? 443 ILE B C     1 
ATOM   7443  O  O     . ILE B 2 443 ? 100.669 172.889 201.094 1.00 86.26  ? 443 ILE B O     1 
ATOM   7444  C  CB    . ILE B 2 443 ? 98.923  171.353 203.142 1.00 83.98  ? 443 ILE B CB    1 
ATOM   7445  C  CG1   . ILE B 2 443 ? 97.832  170.354 202.754 1.00 88.62  ? 443 ILE B CG1   1 
ATOM   7446  C  CG2   . ILE B 2 443 ? 98.962  171.539 204.648 1.00 85.84  ? 443 ILE B CG2   1 
ATOM   7447  C  CD1   . ILE B 2 443 ? 98.126  168.935 203.182 1.00 85.71  ? 443 ILE B CD1   1 
ATOM   7448  N  N     . ALA B 2 444 ? 100.434 174.362 202.789 1.00 75.18  ? 444 ALA B N     1 
ATOM   7449  C  CA    . ALA B 2 444 ? 101.676 175.076 202.527 1.00 79.16  ? 444 ALA B CA    1 
ATOM   7450  C  C     . ALA B 2 444 ? 102.767 174.538 203.443 1.00 81.72  ? 444 ALA B C     1 
ATOM   7451  O  O     . ALA B 2 444 ? 102.612 174.544 204.669 1.00 90.91  ? 444 ALA B O     1 
ATOM   7452  C  CB    . ALA B 2 444 ? 101.495 176.580 202.732 1.00 79.01  ? 444 ALA B CB    1 
ATOM   7453  N  N     . LEU B 2 445 ? 103.865 174.077 202.849 1.00 69.34  ? 445 LEU B N     1 
ATOM   7454  C  CA    . LEU B 2 445 ? 105.002 173.534 203.586 1.00 68.99  ? 445 LEU B CA    1 
ATOM   7455  C  C     . LEU B 2 445 ? 106.134 174.552 203.542 1.00 73.57  ? 445 LEU B C     1 
ATOM   7456  O  O     . LEU B 2 445 ? 106.748 174.760 202.490 1.00 80.48  ? 445 LEU B O     1 
ATOM   7457  C  CB    . LEU B 2 445 ? 105.447 172.198 202.999 1.00 68.46  ? 445 LEU B CB    1 
ATOM   7458  C  CG    . LEU B 2 445 ? 104.387 171.107 202.856 1.00 61.09  ? 445 LEU B CG    1 
ATOM   7459  C  CD1   . LEU B 2 445 ? 104.941 169.946 202.053 1.00 67.81  ? 445 LEU B CD1   1 
ATOM   7460  C  CD2   . LEU B 2 445 ? 103.913 170.637 204.219 1.00 68.95  ? 445 LEU B CD2   1 
ATOM   7461  N  N     . LYS B 2 446 ? 106.411 175.180 204.680 1.00 78.58  ? 446 LYS B N     1 
ATOM   7462  C  CA    . LYS B 2 446 ? 107.485 176.156 204.761 1.00 77.97  ? 446 LYS B CA    1 
ATOM   7463  C  C     . LYS B 2 446 ? 108.843 175.466 204.756 1.00 81.69  ? 446 LYS B C     1 
ATOM   7464  O  O     . LYS B 2 446 ? 109.012 174.370 205.298 1.00 85.77  ? 446 LYS B O     1 
ATOM   7465  C  CB    . LYS B 2 446 ? 107.341 177.012 206.019 1.00 81.13  ? 446 LYS B CB    1 
ATOM   7466  C  CG    . LYS B 2 446 ? 106.259 178.071 205.926 1.00 84.57  ? 446 LYS B CG    1 
ATOM   7467  C  CD    . LYS B 2 446 ? 106.603 179.117 204.879 1.00 85.48  ? 446 LYS B CD    1 
ATOM   7468  C  CE    . LYS B 2 446 ? 105.637 180.290 204.935 1.00 88.51  ? 446 LYS B CE    1 
ATOM   7469  N  NZ    . LYS B 2 446 ? 105.640 180.946 206.271 1.00 87.71  ? 446 LYS B NZ    1 
ATOM   7470  N  N     . ASP B 2 447 ? 109.817 176.124 204.132 1.00 80.50  ? 447 ASP B N     1 
ATOM   7471  C  CA    . ASP B 2 447 ? 111.181 175.624 204.078 1.00 82.82  ? 447 ASP B CA    1 
ATOM   7472  C  C     . ASP B 2 447 ? 112.140 176.766 204.380 1.00 83.59  ? 447 ASP B C     1 
ATOM   7473  O  O     . ASP B 2 447 ? 111.824 177.940 204.174 1.00 88.77  ? 447 ASP B O     1 
ATOM   7474  C  CB    . ASP B 2 447 ? 111.503 175.001 202.714 1.00 80.62  ? 447 ASP B CB    1 
ATOM   7475  C  CG    . ASP B 2 447 ? 112.562 173.923 202.802 1.00 83.59  ? 447 ASP B CG    1 
ATOM   7476  O  OD1   . ASP B 2 447 ? 113.265 173.863 203.832 1.00 81.47  ? 447 ASP B OD1   1 
ATOM   7477  O  OD2   . ASP B 2 447 ? 112.692 173.134 201.843 1.00 87.11  ? 447 ASP B OD2   1 
ATOM   7478  N  N     . ILE B 2 448 ? 113.321 176.408 204.874 1.00 62.85  ? 448 ILE B N     1 
ATOM   7479  C  CA    . ILE B 2 448 ? 114.339 177.373 205.273 1.00 61.03  ? 448 ILE B CA    1 
ATOM   7480  C  C     . ILE B 2 448 ? 115.528 177.228 204.335 1.00 62.67  ? 448 ILE B C     1 
ATOM   7481  O  O     . ILE B 2 448 ? 116.089 176.135 204.195 1.00 65.55  ? 448 ILE B O     1 
ATOM   7482  C  CB    . ILE B 2 448 ? 114.765 177.175 206.735 1.00 61.14  ? 448 ILE B CB    1 
ATOM   7483  C  CG1   . ILE B 2 448 ? 113.542 177.183 207.652 1.00 67.23  ? 448 ILE B CG1   1 
ATOM   7484  C  CG2   . ILE B 2 448 ? 115.751 178.254 207.151 1.00 60.10  ? 448 ILE B CG2   1 
ATOM   7485  C  CD1   . ILE B 2 448 ? 113.846 176.780 209.076 1.00 69.59  ? 448 ILE B CD1   1 
ATOM   7486  N  N     . VAL B 2 449 ? 115.913 178.329 203.700 1.00 55.08  ? 449 VAL B N     1 
ATOM   7487  C  CA    . VAL B 2 449 ? 117.071 178.358 202.815 1.00 47.60  ? 449 VAL B CA    1 
ATOM   7488  C  C     . VAL B 2 449 ? 118.317 178.600 203.655 1.00 54.50  ? 449 VAL B C     1 
ATOM   7489  O  O     . VAL B 2 449 ? 118.323 179.466 204.538 1.00 67.67  ? 449 VAL B O     1 
ATOM   7490  C  CB    . VAL B 2 449 ? 116.912 179.442 201.736 1.00 45.15  ? 449 VAL B CB    1 
ATOM   7491  C  CG1   . VAL B 2 449 ? 118.127 179.468 200.823 1.00 48.96  ? 449 VAL B CG1   1 
ATOM   7492  C  CG2   . VAL B 2 449 ? 115.643 179.207 200.934 1.00 46.64  ? 449 VAL B CG2   1 
ATOM   7493  N  N     . LYS B 2 450 ? 119.369 177.830 203.388 1.00 41.02  ? 450 LYS B N     1 
ATOM   7494  C  CA    . LYS B 2 450 ? 120.604 177.957 204.145 1.00 41.88  ? 450 LYS B CA    1 
ATOM   7495  C  C     . LYS B 2 450 ? 121.208 179.346 203.958 1.00 50.88  ? 450 LYS B C     1 
ATOM   7496  O  O     . LYS B 2 450 ? 121.155 179.940 202.878 1.00 57.42  ? 450 LYS B O     1 
ATOM   7497  C  CB    . LYS B 2 450 ? 121.601 176.880 203.719 1.00 32.77  ? 450 LYS B CB    1 
ATOM   7498  C  CG    . LYS B 2 450 ? 121.179 175.471 204.101 1.00 36.29  ? 450 LYS B CG    1 
ATOM   7499  C  CD    . LYS B 2 450 ? 122.188 174.439 203.634 1.00 39.77  ? 450 LYS B CD    1 
ATOM   7500  C  CE    . LYS B 2 450 ? 121.716 173.030 203.950 1.00 42.48  ? 450 LYS B CE    1 
ATOM   7501  N  NZ    . LYS B 2 450 ? 122.534 171.999 203.258 1.00 45.84  ? 450 LYS B NZ    1 
ATOM   7502  N  N     . GLY B 2 451 ? 121.786 179.866 205.036 1.00 53.90  ? 451 GLY B N     1 
ATOM   7503  C  CA    . GLY B 2 451 ? 122.309 181.217 205.061 1.00 53.10  ? 451 GLY B CA    1 
ATOM   7504  C  C     . GLY B 2 451 ? 123.666 181.334 204.394 1.00 54.72  ? 451 GLY B C     1 
ATOM   7505  O  O     . GLY B 2 451 ? 124.492 180.427 204.465 1.00 57.48  ? 451 GLY B O     1 
ATOM   7506  N  N     . GLY B 2 452 ? 123.886 182.473 203.739 1.00 63.96  ? 452 GLY B N     1 
ATOM   7507  C  CA    . GLY B 2 452 ? 125.134 182.747 203.062 1.00 66.70  ? 452 GLY B CA    1 
ATOM   7508  C  C     . GLY B 2 452 ? 125.279 182.102 201.703 1.00 60.09  ? 452 GLY B C     1 
ATOM   7509  O  O     . GLY B 2 452 ? 126.328 182.266 201.067 1.00 68.16  ? 452 GLY B O     1 
ATOM   7510  N  N     . ILE B 2 453 ? 124.263 181.374 201.237 1.00 45.98  ? 453 ILE B N     1 
ATOM   7511  C  CA    . ILE B 2 453 ? 124.369 180.678 199.958 1.00 45.66  ? 453 ILE B CA    1 
ATOM   7512  C  C     . ILE B 2 453 ? 124.379 181.671 198.802 1.00 58.18  ? 453 ILE B C     1 
ATOM   7513  O  O     . ILE B 2 453 ? 124.945 181.397 197.736 1.00 67.93  ? 453 ILE B O     1 
ATOM   7514  C  CB    . ILE B 2 453 ? 123.235 179.642 199.821 1.00 47.85  ? 453 ILE B CB    1 
ATOM   7515  C  CG1   . ILE B 2 453 ? 123.568 178.623 198.731 1.00 56.70  ? 453 ILE B CG1   1 
ATOM   7516  C  CG2   . ILE B 2 453 ? 121.901 180.319 199.547 1.00 58.32  ? 453 ILE B CG2   1 
ATOM   7517  C  CD1   . ILE B 2 453 ? 122.519 177.549 198.566 1.00 64.21  ? 453 ILE B CD1   1 
ATOM   7518  N  N     . LYS B 2 454 ? 123.848 182.871 199.009 1.00 64.02  ? 454 LYS B N     1 
ATOM   7519  C  CA    . LYS B 2 454 ? 123.748 183.807 197.860 1.00 61.44  ? 454 LYS B CA    1 
ATOM   7520  C  C     . LYS B 2 454 ? 125.138 184.296 197.474 1.00 59.37  ? 454 LYS B C     1 
ATOM   7521  O  O     . LYS B 2 454 ? 125.467 184.255 196.290 1.00 70.16  ? 454 LYS B O     1 
ATOM   7522  C  CB    . LYS B 2 454 ? 122.850 184.992 198.200 1.00 64.34  ? 454 LYS B CB    1 
ATOM   7523  C  CG    . LYS B 2 454 ? 122.830 186.105 197.164 1.00 67.12  ? 454 LYS B CG    1 
ATOM   7524  C  CD    . LYS B 2 454 ? 121.717 185.953 196.155 1.00 65.58  ? 454 LYS B CD    1 
ATOM   7525  C  CE    . LYS B 2 454 ? 120.689 187.060 196.245 1.00 68.18  ? 454 LYS B CE    1 
ATOM   7526  N  NZ    . LYS B 2 454 ? 119.322 186.564 195.961 1.00 70.32  ? 454 LYS B NZ    1 
ATOM   7527  N  N     . GLU B 2 455 ? 125.913 184.741 198.450 1.00 61.02  ? 455 GLU B N     1 
ATOM   7528  C  CA    . GLU B 2 455 ? 127.270 185.264 198.188 1.00 60.62  ? 455 GLU B CA    1 
ATOM   7529  C  C     . GLU B 2 455 ? 128.187 184.138 197.723 1.00 61.79  ? 455 GLU B C     1 
ATOM   7530  O  O     . GLU B 2 455 ? 129.003 184.395 196.844 1.00 61.06  ? 455 GLU B O     1 
ATOM   7531  C  CB    . GLU B 2 455 ? 127.819 185.886 199.463 1.00 60.47  ? 455 GLU B CB    1 
ATOM   7532  C  CG    . GLU B 2 455 ? 127.135 187.183 199.840 1.00 63.46  ? 455 GLU B CG    1 
ATOM   7533  C  CD    . GLU B 2 455 ? 125.833 187.014 200.604 1.00 65.61  ? 455 GLU B CD    1 
ATOM   7534  O  OE1   . GLU B 2 455 ? 125.513 185.870 200.977 1.00 65.17  ? 455 GLU B OE1   1 
ATOM   7535  O  OE2   . GLU B 2 455 ? 125.140 188.028 200.817 1.00 65.05  ? 455 GLU B OE2   1 
ATOM   7536  N  N     . ARG B 2 456 ? 128.085 182.955 198.318 1.00 58.67  ? 456 ARG B N     1 
ATOM   7537  C  CA    . ARG B 2 456 ? 128.897 181.856 197.805 1.00 55.02  ? 456 ARG B CA    1 
ATOM   7538  C  C     . ARG B 2 456 ? 128.595 181.577 196.338 1.00 54.32  ? 456 ARG B C     1 
ATOM   7539  O  O     . ARG B 2 456 ? 129.510 181.305 195.551 1.00 56.76  ? 456 ARG B O     1 
ATOM   7540  C  CB    . ARG B 2 456 ? 128.674 180.603 198.651 1.00 51.62  ? 456 ARG B CB    1 
ATOM   7541  C  CG    . ARG B 2 456 ? 129.052 180.767 200.113 1.00 52.63  ? 456 ARG B CG    1 
ATOM   7542  C  CD    . ARG B 2 456 ? 130.520 180.447 200.341 1.00 53.54  ? 456 ARG B CD    1 
ATOM   7543  N  NE    . ARG B 2 456 ? 130.863 179.111 199.869 1.00 55.78  ? 456 ARG B NE    1 
ATOM   7544  C  CZ    . ARG B 2 456 ? 131.866 178.383 200.339 1.00 54.65  ? 456 ARG B CZ    1 
ATOM   7545  N  NH1   . ARG B 2 456 ? 132.657 178.835 201.299 1.00 55.18  ? 456 ARG B NH1   1 
ATOM   7546  N  NH2   . ARG B 2 456 ? 132.082 177.172 199.835 1.00 55.48  ? 456 ARG B NH2   1 
ATOM   7547  N  N     . PHE B 2 457 ? 127.318 181.631 195.951 1.00 56.64  ? 457 PHE B N     1 
ATOM   7548  C  CA    . PHE B 2 457 ? 126.960 181.411 194.553 1.00 56.40  ? 457 PHE B CA    1 
ATOM   7549  C  C     . PHE B 2 457 ? 127.513 182.514 193.659 1.00 57.74  ? 457 PHE B C     1 
ATOM   7550  O  O     . PHE B 2 457 ? 127.818 182.274 192.485 1.00 58.31  ? 457 PHE B O     1 
ATOM   7551  C  CB    . PHE B 2 457 ? 125.442 181.306 194.411 1.00 56.87  ? 457 PHE B CB    1 
ATOM   7552  C  CG    . PHE B 2 457 ? 124.909 179.921 194.637 1.00 57.80  ? 457 PHE B CG    1 
ATOM   7553  C  CD1   . PHE B 2 457 ? 125.621 178.813 194.210 1.00 58.48  ? 457 PHE B CD1   1 
ATOM   7554  C  CD2   . PHE B 2 457 ? 123.702 179.725 195.285 1.00 57.95  ? 457 PHE B CD2   1 
ATOM   7555  C  CE1   . PHE B 2 457 ? 125.135 177.537 194.416 1.00 58.00  ? 457 PHE B CE1   1 
ATOM   7556  C  CE2   . PHE B 2 457 ? 123.212 178.451 195.497 1.00 58.92  ? 457 PHE B CE2   1 
ATOM   7557  C  CZ    . PHE B 2 457 ? 123.929 177.356 195.062 1.00 60.62  ? 457 PHE B CZ    1 
ATOM   7558  N  N     . ALA B 2 458 ? 127.643 183.731 194.193 1.00 58.16  ? 458 ALA B N     1 
ATOM   7559  C  CA    . ALA B 2 458 ? 128.277 184.805 193.436 1.00 58.57  ? 458 ALA B CA    1 
ATOM   7560  C  C     . ALA B 2 458 ? 129.737 184.481 193.146 1.00 59.29  ? 458 ALA B C     1 
ATOM   7561  O  O     . ALA B 2 458 ? 130.246 184.785 192.061 1.00 59.38  ? 458 ALA B O     1 
ATOM   7562  C  CB    . ALA B 2 458 ? 128.158 186.126 194.195 1.00 57.12  ? 458 ALA B CB    1 
ATOM   7563  N  N     . GLN B 2 459 ? 130.428 183.868 194.111 1.00 55.62  ? 459 GLN B N     1 
ATOM   7564  C  CA    . GLN B 2 459 ? 131.808 183.451 193.887 1.00 52.45  ? 459 GLN B CA    1 
ATOM   7565  C  C     . GLN B 2 459 ? 131.893 182.389 192.799 1.00 53.41  ? 459 GLN B C     1 
ATOM   7566  O  O     . GLN B 2 459 ? 132.837 182.380 192.000 1.00 57.38  ? 459 GLN B O     1 
ATOM   7567  C  CB    . GLN B 2 459 ? 132.415 182.935 195.192 1.00 52.30  ? 459 GLN B CB    1 
ATOM   7568  C  CG    . GLN B 2 459 ? 133.884 183.274 195.375 1.00 55.54  ? 459 GLN B CG    1 
ATOM   7569  C  CD    . GLN B 2 459 ? 134.498 182.570 196.568 1.00 55.87  ? 459 GLN B CD    1 
ATOM   7570  O  OE1   . GLN B 2 459 ? 133.818 182.289 197.555 1.00 55.37  ? 459 GLN B OE1   1 
ATOM   7571  N  NE2   . GLN B 2 459 ? 135.790 182.280 196.483 1.00 55.44  ? 459 GLN B NE2   1 
ATOM   7572  N  N     . LEU B 2 460 ? 130.917 181.478 192.756 1.00 52.36  ? 460 LEU B N     1 
ATOM   7573  C  CA    . LEU B 2 460 ? 130.896 180.464 191.707 1.00 50.90  ? 460 LEU B CA    1 
ATOM   7574  C  C     . LEU B 2 460 ? 130.662 181.091 190.338 1.00 54.38  ? 460 LEU B C     1 
ATOM   7575  O  O     . LEU B 2 460 ? 131.219 180.632 189.334 1.00 54.53  ? 460 LEU B O     1 
ATOM   7576  C  CB    . LEU B 2 460 ? 129.823 179.418 192.009 1.00 53.26  ? 460 LEU B CB    1 
ATOM   7577  C  CG    . LEU B 2 460 ? 130.208 178.325 193.007 1.00 53.07  ? 460 LEU B CG    1 
ATOM   7578  C  CD1   . LEU B 2 460 ? 128.970 177.618 193.536 1.00 55.03  ? 460 LEU B CD1   1 
ATOM   7579  C  CD2   . LEU B 2 460 ? 131.167 177.330 192.374 1.00 52.07  ? 460 LEU B CD2   1 
ATOM   7580  N  N     . ARG B 2 461 ? 129.833 182.137 190.277 1.00 58.93  ? 461 ARG B N     1 
ATOM   7581  C  CA    . ARG B 2 461 ? 129.612 182.836 189.014 1.00 57.65  ? 461 ARG B CA    1 
ATOM   7582  C  C     . ARG B 2 461 ? 130.899 183.475 188.507 1.00 56.63  ? 461 ARG B C     1 
ATOM   7583  O  O     . ARG B 2 461 ? 131.206 183.410 187.311 1.00 58.08  ? 461 ARG B O     1 
ATOM   7584  C  CB    . ARG B 2 461 ? 128.521 183.893 189.181 1.00 57.76  ? 461 ARG B CB    1 
ATOM   7585  C  CG    . ARG B 2 461 ? 127.954 184.412 187.868 1.00 59.02  ? 461 ARG B CG    1 
ATOM   7586  C  CD    . ARG B 2 461 ? 126.535 184.953 188.020 1.00 56.56  ? 461 ARG B CD    1 
ATOM   7587  N  NE    . ARG B 2 461 ? 125.619 183.991 188.624 1.00 57.72  ? 461 ARG B NE    1 
ATOM   7588  C  CZ    . ARG B 2 461 ? 125.246 184.006 189.896 1.00 57.88  ? 461 ARG B CZ    1 
ATOM   7589  N  NH1   . ARG B 2 461 ? 125.687 184.928 190.736 1.00 57.73  ? 461 ARG B NH1   1 
ATOM   7590  N  NH2   . ARG B 2 461 ? 124.407 183.073 190.337 1.00 58.53  ? 461 ARG B NH2   1 
ATOM   7591  N  N     . LYS B 2 462 ? 131.662 184.102 189.405 1.00 52.63  ? 462 LYS B N     1 
ATOM   7592  C  CA    . LYS B 2 462 ? 132.940 184.693 189.027 1.00 55.93  ? 462 LYS B CA    1 
ATOM   7593  C  C     . LYS B 2 462 ? 133.942 183.640 188.573 1.00 56.60  ? 462 LYS B C     1 
ATOM   7594  O  O     . LYS B 2 462 ? 134.836 183.946 187.776 1.00 58.63  ? 462 LYS B O     1 
ATOM   7595  C  CB    . LYS B 2 462 ? 133.500 185.498 190.204 1.00 55.65  ? 462 LYS B CB    1 
ATOM   7596  C  CG    . LYS B 2 462 ? 134.884 186.091 189.983 1.00 57.10  ? 462 LYS B CG    1 
ATOM   7597  C  CD    . LYS B 2 462 ? 135.136 187.268 190.912 1.00 56.19  ? 462 LYS B CD    1 
ATOM   7598  C  CE    . LYS B 2 462 ? 134.733 186.945 192.343 1.00 57.63  ? 462 LYS B CE    1 
ATOM   7599  N  NZ    . LYS B 2 462 ? 135.807 186.222 193.077 1.00 57.97  ? 462 LYS B NZ    1 
ATOM   7600  N  N     . MET B 2 463 ? 133.797 182.403 189.042 1.00 55.11  ? 463 MET B N     1 
ATOM   7601  C  CA    . MET B 2 463 ? 134.721 181.325 188.720 1.00 51.68  ? 463 MET B CA    1 
ATOM   7602  C  C     . MET B 2 463 ? 134.401 180.644 187.397 1.00 52.15  ? 463 MET B C     1 
ATOM   7603  O  O     . MET B 2 463 ? 135.073 179.669 187.042 1.00 54.42  ? 463 MET B O     1 
ATOM   7604  C  CB    . MET B 2 463 ? 134.713 180.292 189.846 1.00 50.44  ? 463 MET B CB    1 
ATOM   7605  C  CG    . MET B 2 463 ? 135.738 180.560 190.925 1.00 53.29  ? 463 MET B CG    1 
ATOM   7606  S  SD    . MET B 2 463 ? 135.498 179.520 192.373 1.00 58.36  ? 463 MET B SD    1 
ATOM   7607  C  CE    . MET B 2 463 ? 136.402 180.466 193.590 1.00 50.95  ? 463 MET B CE    1 
ATOM   7608  N  N     . GLY B 2 464 ? 133.401 181.127 186.663 1.00 50.25  ? 464 GLY B N     1 
ATOM   7609  C  CA    . GLY B 2 464 ? 132.998 180.505 185.420 1.00 51.06  ? 464 GLY B CA    1 
ATOM   7610  C  C     . GLY B 2 464 ? 132.212 179.223 185.569 1.00 51.92  ? 464 GLY B C     1 
ATOM   7611  O  O     . GLY B 2 464 ? 132.172 178.428 184.624 1.00 54.79  ? 464 GLY B O     1 
ATOM   7612  N  N     . ILE B 2 465 ? 131.584 178.997 186.719 1.00 55.09  ? 465 ILE B N     1 
ATOM   7613  C  CA    . ILE B 2 465 ? 130.803 177.792 186.973 1.00 55.61  ? 465 ILE B CA    1 
ATOM   7614  C  C     . ILE B 2 465 ? 129.329 178.167 187.003 1.00 54.38  ? 465 ILE B C     1 
ATOM   7615  O  O     . ILE B 2 465 ? 128.918 179.045 187.773 1.00 55.10  ? 465 ILE B O     1 
ATOM   7616  C  CB    . ILE B 2 465 ? 131.228 177.119 188.289 1.00 53.64  ? 465 ILE B CB    1 
ATOM   7617  C  CG1   . ILE B 2 465 ? 132.667 176.610 188.188 1.00 53.60  ? 465 ILE B CG1   1 
ATOM   7618  C  CG2   . ILE B 2 465 ? 130.279 175.982 188.639 1.00 51.35  ? 465 ILE B CG2   1 
ATOM   7619  C  CD1   . ILE B 2 465 ? 133.200 176.024 189.476 1.00 50.46  ? 465 ILE B CD1   1 
ATOM   7620  N  N     . LYS B 2 466 ? 128.534 177.506 186.167 1.00 56.69  ? 466 LYS B N     1 
ATOM   7621  C  CA    . LYS B 2 466 ? 127.100 177.748 186.104 1.00 58.53  ? 466 LYS B CA    1 
ATOM   7622  C  C     . LYS B 2 466 ? 126.386 176.867 187.121 1.00 58.42  ? 466 LYS B C     1 
ATOM   7623  O  O     . LYS B 2 466 ? 126.607 175.653 187.164 1.00 61.06  ? 466 LYS B O     1 
ATOM   7624  C  CB    . LYS B 2 466 ? 126.569 177.475 184.696 1.00 57.46  ? 466 LYS B CB    1 
ATOM   7625  C  CG    . LYS B 2 466 ? 125.053 177.445 184.596 1.00 59.79  ? 466 LYS B CG    1 
ATOM   7626  C  CD    . LYS B 2 466 ? 124.602 177.117 183.182 1.00 59.12  ? 466 LYS B CD    1 
ATOM   7627  C  CE    . LYS B 2 466 ? 123.104 177.312 183.021 1.00 61.34  ? 466 LYS B CE    1 
ATOM   7628  N  NZ    . LYS B 2 466 ? 122.784 178.446 182.112 1.00 62.41  ? 466 LYS B NZ    1 
ATOM   7629  N  N     . THR B 2 467 ? 125.533 177.479 187.936 1.00 56.92  ? 467 THR B N     1 
ATOM   7630  C  CA    . THR B 2 467 ? 124.791 176.769 188.968 1.00 57.87  ? 467 THR B CA    1 
ATOM   7631  C  C     . THR B 2 467 ? 123.355 176.554 188.509 1.00 58.27  ? 467 THR B C     1 
ATOM   7632  O  O     . THR B 2 467 ? 122.659 177.513 188.161 1.00 60.46  ? 467 THR B O     1 
ATOM   7633  C  CB    . THR B 2 467 ? 124.814 177.541 190.288 1.00 58.90  ? 467 THR B CB    1 
ATOM   7634  O  OG1   . THR B 2 467 ? 124.309 178.865 190.079 1.00 60.70  ? 467 THR B OG1   1 
ATOM   7635  C  CG2   . THR B 2 467 ? 126.233 177.624 190.829 1.00 56.87  ? 467 THR B CG2   1 
ATOM   7636  N  N     . VAL B 2 468 ? 122.919 175.296 188.510 1.00 57.95  ? 468 VAL B N     1 
ATOM   7637  C  CA    . VAL B 2 468 ? 121.575 174.918 188.092 1.00 57.87  ? 468 VAL B CA    1 
ATOM   7638  C  C     . VAL B 2 468 ? 120.918 174.151 189.230 1.00 57.72  ? 468 VAL B C     1 
ATOM   7639  O  O     . VAL B 2 468 ? 121.508 173.211 189.774 1.00 63.27  ? 468 VAL B O     1 
ATOM   7640  C  CB    . VAL B 2 468 ? 121.593 174.076 186.803 1.00 60.26  ? 468 VAL B CB    1 
ATOM   7641  C  CG1   . VAL B 2 468 ? 120.178 173.694 186.397 1.00 60.37  ? 468 VAL B CG1   1 
ATOM   7642  C  CG2   . VAL B 2 468 ? 122.287 174.833 185.682 1.00 59.85  ? 468 VAL B CG2   1 
ATOM   7643  N  N     . MET B 2 469 ? 119.700 174.553 189.585 1.00 61.40  ? 469 MET B N     1 
ATOM   7644  C  CA    . MET B 2 469 ? 118.947 173.936 190.671 1.00 61.62  ? 469 MET B CA    1 
ATOM   7645  C  C     . MET B 2 469 ? 117.927 172.971 190.078 1.00 62.15  ? 469 MET B C     1 
ATOM   7646  O  O     . MET B 2 469 ? 116.938 173.397 189.473 1.00 66.12  ? 469 MET B O     1 
ATOM   7647  C  CB    . MET B 2 469 ? 118.262 175.001 191.523 1.00 61.92  ? 469 MET B CB    1 
ATOM   7648  C  CG    . MET B 2 469 ? 117.738 174.490 192.851 1.00 63.61  ? 469 MET B CG    1 
ATOM   7649  S  SD    . MET B 2 469 ? 116.284 175.400 193.401 1.00 69.08  ? 469 MET B SD    1 
ATOM   7650  C  CE    . MET B 2 469 ? 117.052 176.703 194.357 1.00 65.92  ? 469 MET B CE    1 
ATOM   7651  N  N     . ILE B 2 470 ? 118.161 171.675 190.260 1.00 63.12  ? 470 ILE B N     1 
ATOM   7652  C  CA    . ILE B 2 470 ? 117.266 170.634 189.770 1.00 63.26  ? 470 ILE B CA    1 
ATOM   7653  C  C     . ILE B 2 470 ? 116.408 170.148 190.929 1.00 65.40  ? 470 ILE B C     1 
ATOM   7654  O  O     . ILE B 2 470 ? 116.928 169.807 191.999 1.00 68.72  ? 470 ILE B O     1 
ATOM   7655  C  CB    . ILE B 2 470 ? 118.051 169.473 189.136 1.00 63.69  ? 470 ILE B CB    1 
ATOM   7656  C  CG1   . ILE B 2 470 ? 119.289 169.141 189.971 1.00 65.72  ? 470 ILE B CG1   1 
ATOM   7657  C  CG2   . ILE B 2 470 ? 118.451 169.819 187.712 1.00 66.28  ? 470 ILE B CG2   1 
ATOM   7658  C  CD1   . ILE B 2 470 ? 120.032 167.915 189.493 1.00 65.77  ? 470 ILE B CD1   1 
ATOM   7659  N  N     . THR B 2 471 ? 115.093 170.123 190.722 1.00 69.89  ? 471 THR B N     1 
ATOM   7660  C  CA    . THR B 2 471 ? 114.166 169.703 191.761 1.00 70.30  ? 471 THR B CA    1 
ATOM   7661  C  C     . THR B 2 471 ? 112.893 169.173 191.120 1.00 70.56  ? 471 THR B C     1 
ATOM   7662  O  O     . THR B 2 471 ? 112.542 169.548 189.998 1.00 73.19  ? 471 THR B O     1 
ATOM   7663  C  CB    . THR B 2 471 ? 113.827 170.853 192.718 1.00 72.69  ? 471 THR B CB    1 
ATOM   7664  O  OG1   . THR B 2 471 ? 112.737 170.467 193.565 1.00 72.75  ? 471 THR B OG1   1 
ATOM   7665  C  CG2   . THR B 2 471 ? 113.436 172.098 191.935 1.00 71.10  ? 471 THR B CG2   1 
ATOM   7666  N  N     . GLY B 2 472 ? 112.209 168.293 191.844 1.00 71.98  ? 472 GLY B N     1 
ATOM   7667  C  CA    . GLY B 2 472 ? 110.920 167.780 191.439 1.00 73.04  ? 472 GLY B CA    1 
ATOM   7668  C  C     . GLY B 2 472 ? 109.735 168.556 191.960 1.00 73.72  ? 472 GLY B C     1 
ATOM   7669  O  O     . GLY B 2 472 ? 108.594 168.106 191.812 1.00 76.33  ? 472 GLY B O     1 
ATOM   7670  N  N     . ASP B 2 473 ? 109.968 169.716 192.567 1.00 74.20  ? 473 ASP B N     1 
ATOM   7671  C  CA    . ASP B 2 473 ? 108.906 170.497 193.177 1.00 75.08  ? 473 ASP B CA    1 
ATOM   7672  C  C     . ASP B 2 473 ? 108.158 171.311 192.122 1.00 77.10  ? 473 ASP B C     1 
ATOM   7673  O  O     . ASP B 2 473 ? 108.463 171.270 190.927 1.00 78.00  ? 473 ASP B O     1 
ATOM   7674  C  CB    . ASP B 2 473 ? 109.477 171.415 194.258 1.00 75.26  ? 473 ASP B CB    1 
ATOM   7675  C  CG    . ASP B 2 473 ? 108.486 171.694 195.371 1.00 76.87  ? 473 ASP B CG    1 
ATOM   7676  O  OD1   . ASP B 2 473 ? 107.387 171.100 195.353 1.00 74.64  ? 473 ASP B OD1   1 
ATOM   7677  O  OD2   . ASP B 2 473 ? 108.806 172.507 196.263 1.00 77.98  ? 473 ASP B OD2   1 
ATOM   7678  N  N     . ASN B 2 474 ? 107.157 172.057 192.587 1.00 77.64  ? 474 ASN B N     1 
ATOM   7679  C  CA    . ASN B 2 474 ? 106.350 172.884 191.701 1.00 76.83  ? 474 ASN B CA    1 
ATOM   7680  C  C     . ASN B 2 474 ? 107.196 174.001 191.098 1.00 77.14  ? 474 ASN B C     1 
ATOM   7681  O  O     . ASN B 2 474 ? 108.132 174.507 191.722 1.00 78.27  ? 474 ASN B O     1 
ATOM   7682  C  CB    . ASN B 2 474 ? 105.157 173.459 192.473 1.00 76.16  ? 474 ASN B CB    1 
ATOM   7683  C  CG    . ASN B 2 474 ? 104.496 174.620 191.759 1.00 78.41  ? 474 ASN B CG    1 
ATOM   7684  O  OD1   . ASN B 2 474 ? 104.411 175.724 192.295 1.00 78.33  ? 474 ASN B OD1   1 
ATOM   7685  N  ND2   . ASN B 2 474 ? 104.008 174.372 190.548 1.00 77.86  ? 474 ASN B ND2   1 
ATOM   7686  N  N     . ARG B 2 475 ? 106.866 174.372 189.858 1.00 77.98  ? 475 ARG B N     1 
ATOM   7687  C  CA    . ARG B 2 475 ? 107.639 175.389 189.151 1.00 77.34  ? 475 ARG B CA    1 
ATOM   7688  C  C     . ARG B 2 475 ? 107.547 176.747 189.836 1.00 76.41  ? 475 ARG B C     1 
ATOM   7689  O  O     . ARG B 2 475 ? 108.546 177.471 189.924 1.00 76.98  ? 475 ARG B O     1 
ATOM   7690  C  CB    . ARG B 2 475 ? 107.168 175.488 187.700 1.00 77.58  ? 475 ARG B CB    1 
ATOM   7691  C  CG    . ARG B 2 475 ? 108.021 176.399 186.831 1.00 78.29  ? 475 ARG B CG    1 
ATOM   7692  C  CD    . ARG B 2 475 ? 108.368 175.737 185.507 1.00 78.44  ? 475 ARG B CD    1 
ATOM   7693  N  NE    . ARG B 2 475 ? 107.178 175.304 184.784 1.00 79.12  ? 475 ARG B NE    1 
ATOM   7694  C  CZ    . ARG B 2 475 ? 106.935 174.052 184.423 1.00 79.18  ? 475 ARG B CZ    1 
ATOM   7695  N  NH1   . ARG B 2 475 ? 107.783 173.075 184.702 1.00 78.09  ? 475 ARG B NH1   1 
ATOM   7696  N  NH2   . ARG B 2 475 ? 105.813 173.772 183.767 1.00 78.91  ? 475 ARG B NH2   1 
ATOM   7697  N  N     . LEU B 2 476 ? 106.357 177.117 190.315 1.00 74.70  ? 476 LEU B N     1 
ATOM   7698  C  CA    . LEU B 2 476 ? 106.175 178.444 190.898 1.00 75.83  ? 476 LEU B CA    1 
ATOM   7699  C  C     . LEU B 2 476 ? 107.004 178.618 192.166 1.00 76.33  ? 476 LEU B C     1 
ATOM   7700  O  O     . LEU B 2 476 ? 107.635 179.664 192.363 1.00 75.94  ? 476 LEU B O     1 
ATOM   7701  C  CB    . LEU B 2 476 ? 104.695 178.694 191.186 1.00 75.55  ? 476 LEU B CB    1 
ATOM   7702  C  CG    . LEU B 2 476 ? 103.893 179.342 190.057 1.00 75.66  ? 476 LEU B CG    1 
ATOM   7703  C  CD1   . LEU B 2 476 ? 102.473 179.646 190.511 1.00 75.73  ? 476 LEU B CD1   1 
ATOM   7704  C  CD2   . LEU B 2 476 ? 104.584 180.605 189.565 1.00 74.41  ? 476 LEU B CD2   1 
ATOM   7705  N  N     . THR B 2 477 ? 107.017 177.609 193.039 1.00 74.25  ? 477 THR B N     1 
ATOM   7706  C  CA    . THR B 2 477 ? 107.785 177.718 194.275 1.00 73.65  ? 477 THR B CA    1 
ATOM   7707  C  C     . THR B 2 477 ? 109.282 177.564 194.035 1.00 73.44  ? 477 THR B C     1 
ATOM   7708  O  O     . THR B 2 477 ? 110.084 178.113 194.798 1.00 73.92  ? 477 THR B O     1 
ATOM   7709  C  CB    . THR B 2 477 ? 107.305 176.686 195.299 1.00 73.46  ? 477 THR B CB    1 
ATOM   7710  O  OG1   . THR B 2 477 ? 108.123 176.759 196.474 1.00 74.09  ? 477 THR B OG1   1 
ATOM   7711  C  CG2   . THR B 2 477 ? 107.375 175.280 194.727 1.00 72.45  ? 477 THR B CG2   1 
ATOM   7712  N  N     . ALA B 2 478 ? 109.675 176.825 192.994 1.00 70.27  ? 478 ALA B N     1 
ATOM   7713  C  CA    . ALA B 2 478 ? 111.093 176.679 192.683 1.00 69.16  ? 478 ALA B CA    1 
ATOM   7714  C  C     . ALA B 2 478 ? 111.708 178.011 192.274 1.00 69.43  ? 478 ALA B C     1 
ATOM   7715  O  O     . ALA B 2 478 ? 112.851 178.314 192.637 1.00 70.01  ? 478 ALA B O     1 
ATOM   7716  C  CB    . ALA B 2 478 ? 111.286 175.636 191.583 1.00 68.36  ? 478 ALA B CB    1 
ATOM   7717  N  N     . ALA B 2 479 ? 110.968 178.817 191.509 1.00 69.80  ? 479 ALA B N     1 
ATOM   7718  C  CA    . ALA B 2 479 ? 111.479 180.117 191.089 1.00 69.02  ? 479 ALA B CA    1 
ATOM   7719  C  C     . ALA B 2 479 ? 111.683 181.043 192.281 1.00 68.26  ? 479 ALA B C     1 
ATOM   7720  O  O     . ALA B 2 479 ? 112.654 181.809 192.322 1.00 67.20  ? 479 ALA B O     1 
ATOM   7721  C  CB    . ALA B 2 479 ? 110.531 180.752 190.072 1.00 67.64  ? 479 ALA B CB    1 
ATOM   7722  N  N     . ALA B 2 480 ? 110.779 180.989 193.262 1.00 68.43  ? 480 ALA B N     1 
ATOM   7723  C  CA    . ALA B 2 480 ? 110.914 181.850 194.433 1.00 69.76  ? 480 ALA B CA    1 
ATOM   7724  C  C     . ALA B 2 480 ? 112.060 181.392 195.326 1.00 69.78  ? 480 ALA B C     1 
ATOM   7725  O  O     . ALA B 2 480 ? 112.578 182.171 196.134 1.00 70.12  ? 480 ALA B O     1 
ATOM   7726  C  CB    . ALA B 2 480 ? 109.601 181.882 195.215 1.00 68.19  ? 480 ALA B CB    1 
ATOM   7727  N  N     . ILE B 2 481 ? 112.475 180.132 195.188 1.00 67.55  ? 481 ILE B N     1 
ATOM   7728  C  CA    . ILE B 2 481 ? 113.618 179.641 195.952 1.00 66.60  ? 481 ILE B CA    1 
ATOM   7729  C  C     . ILE B 2 481 ? 114.907 179.862 195.170 1.00 67.80  ? 481 ILE B C     1 
ATOM   7730  O  O     . ILE B 2 481 ? 115.959 180.157 195.750 1.00 68.59  ? 481 ILE B O     1 
ATOM   7731  C  CB    . ILE B 2 481 ? 113.415 178.159 196.318 1.00 67.77  ? 481 ILE B CB    1 
ATOM   7732  C  CG1   . ILE B 2 481 ? 112.206 177.999 197.242 1.00 67.10  ? 481 ILE B CG1   1 
ATOM   7733  C  CG2   . ILE B 2 481 ? 114.659 177.588 196.982 1.00 67.16  ? 481 ILE B CG2   1 
ATOM   7734  C  CD1   . ILE B 2 481 ? 112.455 178.454 198.665 1.00 67.32  ? 481 ILE B CD1   1 
ATOM   7735  N  N     . ALA B 2 482 ? 114.842 179.738 193.842 1.00 66.94  ? 482 ALA B N     1 
ATOM   7736  C  CA    . ALA B 2 482 ? 116.015 180.000 193.015 1.00 66.03  ? 482 ALA B CA    1 
ATOM   7737  C  C     . ALA B 2 482 ? 116.445 181.458 193.113 1.00 67.56  ? 482 ALA B C     1 
ATOM   7738  O  O     . ALA B 2 482 ? 117.643 181.762 193.116 1.00 67.90  ? 482 ALA B O     1 
ATOM   7739  C  CB    . ALA B 2 482 ? 115.729 179.620 191.563 1.00 66.59  ? 482 ALA B CB    1 
ATOM   7740  N  N     . ALA B 2 483 ? 115.479 182.377 193.198 1.00 68.39  ? 483 ALA B N     1 
ATOM   7741  C  CA    . ALA B 2 483 ? 115.821 183.789 193.332 1.00 67.50  ? 483 ALA B CA    1 
ATOM   7742  C  C     . ALA B 2 483 ? 116.201 184.127 194.767 1.00 67.76  ? 483 ALA B C     1 
ATOM   7743  O  O     . ALA B 2 483 ? 116.792 185.181 195.030 1.00 68.01  ? 483 ALA B O     1 
ATOM   7744  C  CB    . ALA B 2 483 ? 114.655 184.659 192.863 1.00 67.49  ? 483 ALA B CB    1 
ATOM   7745  N  N     . GLU B 2 484 ? 115.869 183.244 195.712 1.00 68.69  ? 484 GLU B N     1 
ATOM   7746  C  CA    . GLU B 2 484 ? 116.268 183.450 197.098 1.00 68.81  ? 484 GLU B CA    1 
ATOM   7747  C  C     . GLU B 2 484 ? 117.618 182.818 197.407 1.00 69.94  ? 484 GLU B C     1 
ATOM   7748  O  O     . GLU B 2 484 ? 118.119 182.971 198.525 1.00 70.87  ? 484 GLU B O     1 
ATOM   7749  C  CB    . GLU B 2 484 ? 115.203 182.889 198.042 1.00 69.48  ? 484 GLU B CB    1 
ATOM   7750  C  CG    . GLU B 2 484 ? 115.031 183.683 199.327 1.00 70.19  ? 484 GLU B CG    1 
ATOM   7751  C  CD    . GLU B 2 484 ? 114.467 182.846 200.458 1.00 72.15  ? 484 GLU B CD    1 
ATOM   7752  O  OE1   . GLU B 2 484 ? 113.228 182.712 200.539 1.00 70.42  ? 484 GLU B OE1   1 
ATOM   7753  O  OE2   . GLU B 2 484 ? 115.262 182.323 201.266 1.00 72.37  ? 484 GLU B OE2   1 
ATOM   7754  N  N     . ALA B 2 485 ? 118.214 182.116 196.444 1.00 68.14  ? 485 ALA B N     1 
ATOM   7755  C  CA    . ALA B 2 485 ? 119.514 181.484 196.619 1.00 65.36  ? 485 ALA B CA    1 
ATOM   7756  C  C     . ALA B 2 485 ? 120.581 182.062 195.702 1.00 66.34  ? 485 ALA B C     1 
ATOM   7757  O  O     . ALA B 2 485 ? 121.767 182.031 196.044 1.00 67.02  ? 485 ALA B O     1 
ATOM   7758  C  CB    . ALA B 2 485 ? 119.405 179.974 196.386 1.00 63.78  ? 485 ALA B CB    1 
ATOM   7759  N  N     . GLY B 2 486 ? 120.189 182.596 194.550 1.00 63.17  ? 486 GLY B N     1 
ATOM   7760  C  CA    . GLY B 2 486 ? 121.125 183.191 193.621 1.00 63.15  ? 486 GLY B CA    1 
ATOM   7761  C  C     . GLY B 2 486 ? 121.643 182.283 192.528 1.00 63.06  ? 486 GLY B C     1 
ATOM   7762  O  O     . GLY B 2 486 ? 122.647 182.625 191.893 1.00 64.10  ? 486 GLY B O     1 
ATOM   7763  N  N     . VAL B 2 487 ? 120.999 181.139 192.286 1.00 61.97  ? 487 VAL B N     1 
ATOM   7764  C  CA    . VAL B 2 487 ? 121.439 180.253 191.217 1.00 62.61  ? 487 VAL B CA    1 
ATOM   7765  C  C     . VAL B 2 487 ? 121.125 180.883 189.865 1.00 64.14  ? 487 VAL B C     1 
ATOM   7766  O  O     . VAL B 2 487 ? 120.276 181.777 189.747 1.00 64.78  ? 487 VAL B O     1 
ATOM   7767  C  CB    . VAL B 2 487 ? 120.785 178.865 191.347 1.00 62.30  ? 487 VAL B CB    1 
ATOM   7768  C  CG1   . VAL B 2 487 ? 121.053 178.277 192.721 1.00 61.51  ? 487 VAL B CG1   1 
ATOM   7769  C  CG2   . VAL B 2 487 ? 119.292 178.953 191.079 1.00 63.09  ? 487 VAL B CG2   1 
ATOM   7770  N  N     . ASP B 2 488 ? 121.822 180.413 188.828 1.00 63.89  ? 488 ASP B N     1 
ATOM   7771  C  CA    . ASP B 2 488 ? 121.612 180.959 187.491 1.00 62.19  ? 488 ASP B CA    1 
ATOM   7772  C  C     . ASP B 2 488 ? 120.291 180.487 186.898 1.00 62.61  ? 488 ASP B C     1 
ATOM   7773  O  O     . ASP B 2 488 ? 119.430 181.305 186.553 1.00 65.62  ? 488 ASP B O     1 
ATOM   7774  C  CB    . ASP B 2 488 ? 122.777 180.575 186.578 1.00 62.78  ? 488 ASP B CB    1 
ATOM   7775  C  CG    . ASP B 2 488 ? 124.070 181.266 186.961 1.00 62.56  ? 488 ASP B CG    1 
ATOM   7776  O  OD1   . ASP B 2 488 ? 124.120 182.512 186.902 1.00 62.41  ? 488 ASP B OD1   1 
ATOM   7777  O  OD2   . ASP B 2 488 ? 125.039 180.562 187.317 1.00 64.09  ? 488 ASP B OD2   1 
ATOM   7778  N  N     . ASP B 2 489 ? 120.112 179.174 186.770 1.00 64.76  ? 489 ASP B N     1 
ATOM   7779  C  CA    . ASP B 2 489 ? 118.919 178.603 186.166 1.00 65.81  ? 489 ASP B CA    1 
ATOM   7780  C  C     . ASP B 2 489 ? 118.436 177.451 187.036 1.00 66.78  ? 489 ASP B C     1 
ATOM   7781  O  O     . ASP B 2 489 ? 119.162 176.957 187.901 1.00 68.79  ? 489 ASP B O     1 
ATOM   7782  C  CB    . ASP B 2 489 ? 119.202 178.138 184.728 1.00 65.26  ? 489 ASP B CB    1 
ATOM   7783  C  CG    . ASP B 2 489 ? 117.953 177.690 183.995 1.00 67.60  ? 489 ASP B CG    1 
ATOM   7784  O  OD1   . ASP B 2 489 ? 117.210 178.560 183.493 1.00 67.66  ? 489 ASP B OD1   1 
ATOM   7785  O  OD2   . ASP B 2 489 ? 117.714 176.467 183.924 1.00 67.90  ? 489 ASP B OD2   1 
ATOM   7786  N  N     . PHE B 2 490 ? 117.191 177.033 186.813 1.00 66.20  ? 490 PHE B N     1 
ATOM   7787  C  CA    . PHE B 2 490 ? 116.612 175.932 187.567 1.00 64.58  ? 490 PHE B CA    1 
ATOM   7788  C  C     . PHE B 2 490 ? 115.867 175.001 186.621 1.00 66.17  ? 490 PHE B C     1 
ATOM   7789  O  O     . PHE B 2 490 ? 115.688 175.303 185.439 1.00 68.74  ? 490 PHE B O     1 
ATOM   7790  C  CB    . PHE B 2 490 ? 115.663 176.427 188.670 1.00 65.73  ? 490 PHE B CB    1 
ATOM   7791  C  CG    . PHE B 2 490 ? 114.585 177.353 188.178 1.00 67.90  ? 490 PHE B CG    1 
ATOM   7792  C  CD1   . PHE B 2 490 ? 113.374 176.850 187.729 1.00 67.03  ? 490 PHE B CD1   1 
ATOM   7793  C  CD2   . PHE B 2 490 ? 114.778 178.724 188.171 1.00 67.05  ? 490 PHE B CD2   1 
ATOM   7794  C  CE1   . PHE B 2 490 ? 112.379 177.696 187.278 1.00 68.34  ? 490 PHE B CE1   1 
ATOM   7795  C  CE2   . PHE B 2 490 ? 113.786 179.575 187.721 1.00 67.84  ? 490 PHE B CE2   1 
ATOM   7796  C  CZ    . PHE B 2 490 ? 112.585 179.060 187.274 1.00 69.07  ? 490 PHE B CZ    1 
ATOM   7797  N  N     . LEU B 2 491 ? 115.429 173.865 187.161 1.00 66.69  ? 491 LEU B N     1 
ATOM   7798  C  CA    . LEU B 2 491 ? 114.669 172.861 186.416 1.00 65.99  ? 491 LEU B CA    1 
ATOM   7799  C  C     . LEU B 2 491 ? 113.720 172.193 187.406 1.00 67.39  ? 491 LEU B C     1 
ATOM   7800  O  O     . LEU B 2 491 ? 114.121 171.310 188.169 1.00 68.14  ? 491 LEU B O     1 
ATOM   7801  C  CB    . LEU B 2 491 ? 115.594 171.850 185.741 1.00 65.46  ? 491 LEU B CB    1 
ATOM   7802  C  CG    . LEU B 2 491 ? 114.917 170.648 185.077 1.00 67.52  ? 491 LEU B CG    1 
ATOM   7803  C  CD1   . LEU B 2 491 ? 114.489 170.990 183.658 1.00 68.79  ? 491 LEU B CD1   1 
ATOM   7804  C  CD2   . LEU B 2 491 ? 115.834 169.434 185.086 1.00 66.69  ? 491 LEU B CD2   1 
ATOM   7805  N  N     . ALA B 2 492 ? 112.462 172.621 187.393 1.00 72.86  ? 492 ALA B N     1 
ATOM   7806  C  CA    . ALA B 2 492 ? 111.462 172.108 188.312 1.00 72.26  ? 492 ALA B CA    1 
ATOM   7807  C  C     . ALA B 2 492 ? 110.701 170.941 187.688 1.00 72.45  ? 492 ALA B C     1 
ATOM   7808  O  O     . ALA B 2 492 ? 110.763 170.696 186.481 1.00 73.77  ? 492 ALA B O     1 
ATOM   7809  C  CB    . ALA B 2 492 ? 110.497 173.217 188.725 1.00 71.89  ? 492 ALA B CB    1 
ATOM   7810  N  N     . GLU B 2 493 ? 109.970 170.218 188.540 1.00 75.58  ? 493 GLU B N     1 
ATOM   7811  C  CA    . GLU B 2 493 ? 109.205 169.039 188.129 1.00 76.40  ? 493 GLU B CA    1 
ATOM   7812  C  C     . GLU B 2 493 ? 110.098 168.026 187.419 1.00 76.55  ? 493 GLU B C     1 
ATOM   7813  O  O     . GLU B 2 493 ? 109.735 167.457 186.387 1.00 77.52  ? 493 GLU B O     1 
ATOM   7814  C  CB    . GLU B 2 493 ? 108.015 169.431 187.250 1.00 76.86  ? 493 GLU B CB    1 
ATOM   7815  C  CG    . GLU B 2 493 ? 106.790 169.879 188.028 1.00 77.81  ? 493 GLU B CG    1 
ATOM   7816  C  CD    . GLU B 2 493 ? 106.341 171.276 187.650 1.00 79.15  ? 493 GLU B CD    1 
ATOM   7817  O  OE1   . GLU B 2 493 ? 106.581 171.686 186.495 1.00 79.49  ? 493 GLU B OE1   1 
ATOM   7818  O  OE2   . GLU B 2 493 ? 105.749 171.964 188.508 1.00 78.34  ? 493 GLU B OE2   1 
ATOM   7819  N  N     . ALA B 2 494 ? 111.281 167.799 187.981 1.00 72.48  ? 494 ALA B N     1 
ATOM   7820  C  CA    . ALA B 2 494 ? 112.270 166.905 187.397 1.00 72.72  ? 494 ALA B CA    1 
ATOM   7821  C  C     . ALA B 2 494 ? 112.211 165.557 188.104 1.00 73.45  ? 494 ALA B C     1 
ATOM   7822  O  O     . ALA B 2 494 ? 112.518 165.463 189.297 1.00 74.59  ? 494 ALA B O     1 
ATOM   7823  C  CB    . ALA B 2 494 ? 113.672 167.504 187.496 1.00 73.37  ? 494 ALA B CB    1 
ATOM   7824  N  N     . THR B 2 495 ? 111.814 164.523 187.368 1.00 73.95  ? 495 THR B N     1 
ATOM   7825  C  CA    . THR B 2 495 ? 111.823 163.173 187.896 1.00 73.89  ? 495 THR B CA    1 
ATOM   7826  C  C     . THR B 2 495 ? 113.268 162.709 188.083 1.00 74.40  ? 495 THR B C     1 
ATOM   7827  O  O     . THR B 2 495 ? 114.187 163.252 187.465 1.00 74.46  ? 495 THR B O     1 
ATOM   7828  C  CB    . THR B 2 495 ? 111.057 162.238 186.956 1.00 75.13  ? 495 THR B CB    1 
ATOM   7829  O  OG1   . THR B 2 495 ? 110.581 161.095 187.679 1.00 74.61  ? 495 THR B OG1   1 
ATOM   7830  C  CG2   . THR B 2 495 ? 111.936 161.773 185.806 1.00 74.13  ? 495 THR B CG2   1 
ATOM   7831  N  N     . PRO B 2 496 ? 113.502 161.729 188.965 1.00 74.63  ? 496 PRO B N     1 
ATOM   7832  C  CA    . PRO B 2 496 ? 114.882 161.248 189.156 1.00 74.86  ? 496 PRO B CA    1 
ATOM   7833  C  C     . PRO B 2 496 ? 115.535 160.747 187.879 1.00 74.15  ? 496 PRO B C     1 
ATOM   7834  O  O     . PRO B 2 496 ? 116.762 160.830 187.744 1.00 74.82  ? 496 PRO B O     1 
ATOM   7835  C  CB    . PRO B 2 496 ? 114.717 160.128 190.192 1.00 73.66  ? 496 PRO B CB    1 
ATOM   7836  C  CG    . PRO B 2 496 ? 113.515 160.526 190.969 1.00 74.12  ? 496 PRO B CG    1 
ATOM   7837  C  CD    . PRO B 2 496 ? 112.589 161.199 189.994 1.00 74.16  ? 496 PRO B CD    1 
ATOM   7838  N  N     . GLU B 2 497 ? 114.750 160.229 186.931 1.00 74.13  ? 497 GLU B N     1 
ATOM   7839  C  CA    . GLU B 2 497 ? 115.323 159.813 185.656 1.00 74.43  ? 497 GLU B CA    1 
ATOM   7840  C  C     . GLU B 2 497 ? 115.617 161.006 184.755 1.00 74.98  ? 497 GLU B C     1 
ATOM   7841  O  O     . GLU B 2 497 ? 116.318 160.861 183.747 1.00 74.39  ? 497 GLU B O     1 
ATOM   7842  C  CB    . GLU B 2 497 ? 114.384 158.835 184.951 1.00 73.70  ? 497 GLU B CB    1 
ATOM   7843  C  CG    . GLU B 2 497 ? 114.524 157.396 185.418 1.00 74.91  ? 497 GLU B CG    1 
ATOM   7844  C  CD    . GLU B 2 497 ? 113.688 157.100 186.648 1.00 76.58  ? 497 GLU B CD    1 
ATOM   7845  O  OE1   . GLU B 2 497 ? 114.239 157.143 187.768 1.00 76.22  ? 497 GLU B OE1   1 
ATOM   7846  O  OE2   . GLU B 2 497 ? 112.480 156.823 186.494 1.00 76.28  ? 497 GLU B OE2   1 
ATOM   7847  N  N     . ALA B 2 498 ? 115.096 162.187 185.097 1.00 73.78  ? 498 ALA B N     1 
ATOM   7848  C  CA    . ALA B 2 498 ? 115.356 163.371 184.285 1.00 72.33  ? 498 ALA B CA    1 
ATOM   7849  C  C     . ALA B 2 498 ? 116.654 164.052 184.701 1.00 73.66  ? 498 ALA B C     1 
ATOM   7850  O  O     . ALA B 2 498 ? 117.360 164.619 183.859 1.00 75.94  ? 498 ALA B O     1 
ATOM   7851  C  CB    . ALA B 2 498 ? 114.183 164.346 184.381 1.00 70.73  ? 498 ALA B CB    1 
ATOM   7852  N  N     . LYS B 2 499 ? 116.980 164.013 185.995 1.00 72.05  ? 499 LYS B N     1 
ATOM   7853  C  CA    . LYS B 2 499 ? 118.256 164.554 186.451 1.00 70.89  ? 499 LYS B CA    1 
ATOM   7854  C  C     . LYS B 2 499 ? 119.422 163.777 185.854 1.00 71.01  ? 499 LYS B C     1 
ATOM   7855  O  O     . LYS B 2 499 ? 120.437 164.367 185.465 1.00 70.90  ? 499 LYS B O     1 
ATOM   7856  C  CB    . LYS B 2 499 ? 118.323 164.536 187.978 1.00 71.06  ? 499 LYS B CB    1 
ATOM   7857  C  CG    . LYS B 2 499 ? 117.168 165.248 188.663 1.00 71.59  ? 499 LYS B CG    1 
ATOM   7858  C  CD    . LYS B 2 499 ? 116.988 164.758 190.091 1.00 71.65  ? 499 LYS B CD    1 
ATOM   7859  C  CE    . LYS B 2 499 ? 115.631 165.158 190.648 1.00 72.57  ? 499 LYS B CE    1 
ATOM   7860  N  NZ    . LYS B 2 499 ? 115.644 166.540 191.202 1.00 73.70  ? 499 LYS B NZ    1 
ATOM   7861  N  N     . LEU B 2 500 ? 119.295 162.450 185.778 1.00 69.38  ? 500 LEU B N     1 
ATOM   7862  C  CA    . LEU B 2 500 ? 120.330 161.640 185.142 1.00 69.28  ? 500 LEU B CA    1 
ATOM   7863  C  C     . LEU B 2 500 ? 120.469 161.988 183.666 1.00 70.15  ? 500 LEU B C     1 
ATOM   7864  O  O     . LEU B 2 500 ? 121.584 162.028 183.132 1.00 71.19  ? 500 LEU B O     1 
ATOM   7865  C  CB    . LEU B 2 500 ? 120.012 160.155 185.318 1.00 68.46  ? 500 LEU B CB    1 
ATOM   7866  C  CG    . LEU B 2 500 ? 121.033 159.162 184.760 1.00 69.83  ? 500 LEU B CG    1 
ATOM   7867  C  CD1   . LEU B 2 500 ? 122.288 159.145 185.617 1.00 70.32  ? 500 LEU B CD1   1 
ATOM   7868  C  CD2   . LEU B 2 500 ? 120.430 157.769 184.658 1.00 69.87  ? 500 LEU B CD2   1 
ATOM   7869  N  N     . ALA B 2 501 ? 119.346 162.234 182.988 1.00 68.78  ? 501 ALA B N     1 
ATOM   7870  C  CA    . ALA B 2 501 ? 119.395 162.614 181.580 1.00 69.07  ? 501 ALA B CA    1 
ATOM   7871  C  C     . ALA B 2 501 ? 120.084 163.960 181.393 1.00 68.83  ? 501 ALA B C     1 
ATOM   7872  O  O     . ALA B 2 501 ? 120.836 164.151 180.430 1.00 70.94  ? 501 ALA B O     1 
ATOM   7873  C  CB    . ALA B 2 501 ? 117.983 162.647 180.996 1.00 69.79  ? 501 ALA B CB    1 
ATOM   7874  N  N     . LEU B 2 502 ? 119.832 164.908 182.299 1.00 67.46  ? 502 LEU B N     1 
ATOM   7875  C  CA    . LEU B 2 502 ? 120.453 166.225 182.187 1.00 67.96  ? 502 LEU B CA    1 
ATOM   7876  C  C     . LEU B 2 502 ? 121.968 166.138 182.327 1.00 68.82  ? 502 LEU B C     1 
ATOM   7877  O  O     . LEU B 2 502 ? 122.705 166.825 181.609 1.00 69.26  ? 502 LEU B O     1 
ATOM   7878  C  CB    . LEU B 2 502 ? 119.870 167.171 183.236 1.00 66.99  ? 502 LEU B CB    1 
ATOM   7879  C  CG    . LEU B 2 502 ? 120.210 168.653 183.069 1.00 67.56  ? 502 LEU B CG    1 
ATOM   7880  C  CD1   . LEU B 2 502 ? 119.815 169.143 181.684 1.00 67.16  ? 502 LEU B CD1   1 
ATOM   7881  C  CD2   . LEU B 2 502 ? 119.535 169.484 184.148 1.00 67.84  ? 502 LEU B CD2   1 
ATOM   7882  N  N     . ILE B 2 503 ? 122.451 165.308 183.253 1.00 68.10  ? 503 ILE B N     1 
ATOM   7883  C  CA    . ILE B 2 503 ? 123.892 165.135 183.418 1.00 67.07  ? 503 ILE B CA    1 
ATOM   7884  C  C     . ILE B 2 503 ? 124.501 164.517 182.167 1.00 68.18  ? 503 ILE B C     1 
ATOM   7885  O  O     . ILE B 2 503 ? 125.566 164.941 181.701 1.00 70.36  ? 503 ILE B O     1 
ATOM   7886  C  CB    . ILE B 2 503 ? 124.190 164.292 184.672 1.00 66.25  ? 503 ILE B CB    1 
ATOM   7887  C  CG1   . ILE B 2 503 ? 123.595 164.961 185.911 1.00 66.15  ? 503 ILE B CG1   1 
ATOM   7888  C  CG2   . ILE B 2 503 ? 125.689 164.089 184.836 1.00 66.67  ? 503 ILE B CG2   1 
ATOM   7889  C  CD1   . ILE B 2 503 ? 124.000 164.315 187.212 1.00 68.07  ? 503 ILE B CD1   1 
ATOM   7890  N  N     . ARG B 2 504 ? 123.837 163.505 181.603 1.00 69.94  ? 504 ARG B N     1 
ATOM   7891  C  CA    . ARG B 2 504 ? 124.316 162.907 180.361 1.00 70.14  ? 504 ARG B CA    1 
ATOM   7892  C  C     . ARG B 2 504 ? 124.256 163.904 179.210 1.00 69.15  ? 504 ARG B C     1 
ATOM   7893  O  O     . ARG B 2 504 ? 125.145 163.921 178.351 1.00 70.62  ? 504 ARG B O     1 
ATOM   7894  C  CB    . ARG B 2 504 ? 123.503 161.655 180.033 1.00 69.54  ? 504 ARG B CB    1 
ATOM   7895  C  CG    . ARG B 2 504 ? 123.688 160.518 181.025 1.00 68.99  ? 504 ARG B CG    1 
ATOM   7896  C  CD    . ARG B 2 504 ? 124.054 159.224 180.317 1.00 70.80  ? 504 ARG B CD    1 
ATOM   7897  N  NE    . ARG B 2 504 ? 124.226 158.117 181.251 1.00 71.93  ? 504 ARG B NE    1 
ATOM   7898  C  CZ    . ARG B 2 504 ? 123.229 157.434 181.797 1.00 71.25  ? 504 ARG B CZ    1 
ATOM   7899  N  NH1   . ARG B 2 504 ? 121.966 157.715 181.522 1.00 70.57  ? 504 ARG B NH1   1 
ATOM   7900  N  NH2   . ARG B 2 504 ? 123.507 156.442 182.638 1.00 70.93  ? 504 ARG B NH2   1 
ATOM   7901  N  N     . GLN B 2 505 ? 123.211 164.735 179.171 1.00 66.94  ? 505 GLN B N     1 
ATOM   7902  C  CA    . GLN B 2 505 ? 123.114 165.751 178.128 1.00 67.07  ? 505 GLN B CA    1 
ATOM   7903  C  C     . GLN B 2 505 ? 124.256 166.755 178.227 1.00 68.56  ? 505 GLN B C     1 
ATOM   7904  O  O     . GLN B 2 505 ? 124.851 167.133 177.211 1.00 71.59  ? 505 GLN B O     1 
ATOM   7905  C  CB    . GLN B 2 505 ? 121.764 166.463 178.213 1.00 66.67  ? 505 GLN B CB    1 
ATOM   7906  C  CG    . GLN B 2 505 ? 121.643 167.678 177.308 1.00 69.64  ? 505 GLN B CG    1 
ATOM   7907  C  CD    . GLN B 2 505 ? 120.676 168.714 177.845 1.00 69.94  ? 505 GLN B CD    1 
ATOM   7908  O  OE1   . GLN B 2 505 ? 119.522 168.408 178.143 1.00 71.54  ? 505 GLN B OE1   1 
ATOM   7909  N  NE2   . GLN B 2 505 ? 121.143 169.951 177.971 1.00 68.76  ? 505 GLN B NE2   1 
ATOM   7910  N  N     . TYR B 2 506 ? 124.575 167.200 179.445 1.00 69.36  ? 506 TYR B N     1 
ATOM   7911  C  CA    . TYR B 2 506 ? 125.704 168.106 179.629 1.00 67.82  ? 506 TYR B CA    1 
ATOM   7912  C  C     . TYR B 2 506 ? 127.023 167.419 179.296 1.00 67.26  ? 506 TYR B C     1 
ATOM   7913  O  O     . TYR B 2 506 ? 127.913 168.029 178.693 1.00 68.63  ? 506 TYR B O     1 
ATOM   7914  C  CB    . TYR B 2 506 ? 125.723 168.640 181.060 1.00 66.89  ? 506 TYR B CB    1 
ATOM   7915  C  CG    . TYR B 2 506 ? 124.918 169.904 181.262 1.00 67.21  ? 506 TYR B CG    1 
ATOM   7916  C  CD1   . TYR B 2 506 ? 125.344 171.113 180.730 1.00 67.58  ? 506 TYR B CD1   1 
ATOM   7917  C  CD2   . TYR B 2 506 ? 123.738 169.889 181.993 1.00 67.53  ? 506 TYR B CD2   1 
ATOM   7918  C  CE1   . TYR B 2 506 ? 124.614 172.272 180.914 1.00 67.16  ? 506 TYR B CE1   1 
ATOM   7919  C  CE2   . TYR B 2 506 ? 123.001 171.043 182.183 1.00 68.08  ? 506 TYR B CE2   1 
ATOM   7920  C  CZ    . TYR B 2 506 ? 123.444 172.231 181.641 1.00 67.99  ? 506 TYR B CZ    1 
ATOM   7921  O  OH    . TYR B 2 506 ? 122.713 173.382 181.828 1.00 69.50  ? 506 TYR B OH    1 
ATOM   7922  N  N     . GLN B 2 507 ? 127.167 166.149 179.682 1.00 66.88  ? 507 GLN B N     1 
ATOM   7923  C  CA    . GLN B 2 507 ? 128.384 165.406 179.380 1.00 68.11  ? 507 GLN B CA    1 
ATOM   7924  C  C     . GLN B 2 507 ? 128.508 165.070 177.900 1.00 71.87  ? 507 GLN B C     1 
ATOM   7925  O  O     . GLN B 2 507 ? 129.613 164.764 177.439 1.00 71.71  ? 507 GLN B O     1 
ATOM   7926  C  CB    . GLN B 2 507 ? 128.436 164.120 180.208 1.00 66.98  ? 507 GLN B CB    1 
ATOM   7927  C  CG    . GLN B 2 507 ? 128.842 164.328 181.657 1.00 68.17  ? 507 GLN B CG    1 
ATOM   7928  C  CD    . GLN B 2 507 ? 128.759 163.053 182.474 1.00 70.43  ? 507 GLN B CD    1 
ATOM   7929  O  OE1   . GLN B 2 507 ? 128.267 162.029 182.001 1.00 71.81  ? 507 GLN B OE1   1 
ATOM   7930  N  NE2   . GLN B 2 507 ? 129.244 163.110 183.709 1.00 69.48  ? 507 GLN B NE2   1 
ATOM   7931  N  N     . ALA B 2 508 ? 127.404 165.110 177.151 1.00 72.02  ? 508 ALA B N     1 
ATOM   7932  C  CA    . ALA B 2 508 ? 127.466 164.816 175.722 1.00 70.50  ? 508 ALA B CA    1 
ATOM   7933  C  C     . ALA B 2 508 ? 128.318 165.840 174.984 1.00 71.71  ? 508 ALA B C     1 
ATOM   7934  O  O     . ALA B 2 508 ? 129.097 165.485 174.091 1.00 70.85  ? 508 ALA B O     1 
ATOM   7935  C  CB    . ALA B 2 508 ? 126.056 164.763 175.135 1.00 69.44  ? 508 ALA B CB    1 
ATOM   7936  N  N     . GLU B 2 509 ? 128.185 167.119 175.342 1.00 67.86  ? 509 GLU B N     1 
ATOM   7937  C  CA    . GLU B 2 509 ? 128.977 168.169 174.716 1.00 68.95  ? 509 GLU B CA    1 
ATOM   7938  C  C     . GLU B 2 509 ? 130.442 168.134 175.133 1.00 70.41  ? 509 GLU B C     1 
ATOM   7939  O  O     . GLU B 2 509 ? 131.251 168.857 174.543 1.00 70.94  ? 509 GLU B O     1 
ATOM   7940  C  CB    . GLU B 2 509 ? 128.379 169.540 175.039 1.00 69.08  ? 509 GLU B CB    1 
ATOM   7941  C  CG    . GLU B 2 509 ? 126.882 169.515 175.298 1.00 69.79  ? 509 GLU B CG    1 
ATOM   7942  C  CD    . GLU B 2 509 ? 126.377 170.799 175.925 1.00 72.32  ? 509 GLU B CD    1 
ATOM   7943  O  OE1   . GLU B 2 509 ? 125.478 170.726 176.789 1.00 70.67  ? 509 GLU B OE1   1 
ATOM   7944  O  OE2   . GLU B 2 509 ? 126.878 171.881 175.554 1.00 72.07  ? 509 GLU B OE2   1 
ATOM   7945  N  N     . GLY B 2 510 ? 130.800 167.320 176.124 1.00 69.23  ? 510 GLY B N     1 
ATOM   7946  C  CA    . GLY B 2 510 ? 132.168 167.213 176.582 1.00 68.60  ? 510 GLY B CA    1 
ATOM   7947  C  C     . GLY B 2 510 ? 132.486 167.974 177.850 1.00 69.33  ? 510 GLY B C     1 
ATOM   7948  O  O     . GLY B 2 510 ? 133.624 167.894 178.329 1.00 67.02  ? 510 GLY B O     1 
ATOM   7949  N  N     . ARG B 2 511 ? 131.526 168.704 178.408 1.00 67.49  ? 511 ARG B N     1 
ATOM   7950  C  CA    . ARG B 2 511 ? 131.759 169.457 179.628 1.00 68.06  ? 511 ARG B CA    1 
ATOM   7951  C  C     . ARG B 2 511 ? 131.776 168.528 180.839 1.00 69.08  ? 511 ARG B C     1 
ATOM   7952  O  O     . ARG B 2 511 ? 131.263 167.406 180.807 1.00 69.63  ? 511 ARG B O     1 
ATOM   7953  C  CB    . ARG B 2 511 ? 130.687 170.531 179.810 1.00 66.31  ? 511 ARG B CB    1 
ATOM   7954  C  CG    . ARG B 2 511 ? 130.447 171.385 178.576 1.00 68.16  ? 511 ARG B CG    1 
ATOM   7955  C  CD    . ARG B 2 511 ? 129.209 172.251 178.740 1.00 68.20  ? 511 ARG B CD    1 
ATOM   7956  N  NE    . ARG B 2 511 ? 129.290 173.102 179.921 1.00 68.66  ? 511 ARG B NE    1 
ATOM   7957  C  CZ    . ARG B 2 511 ? 128.322 173.910 180.330 1.00 70.15  ? 511 ARG B CZ    1 
ATOM   7958  N  NH1   . ARG B 2 511 ? 127.176 174.003 179.675 1.00 70.75  ? 511 ARG B NH1   1 
ATOM   7959  N  NH2   . ARG B 2 511 ? 128.508 174.644 181.423 1.00 68.70  ? 511 ARG B NH2   1 
ATOM   7960  N  N     . LEU B 2 512 ? 132.380 169.015 181.919 1.00 62.43  ? 512 LEU B N     1 
ATOM   7961  C  CA    . LEU B 2 512 ? 132.430 168.294 183.183 1.00 58.88  ? 512 LEU B CA    1 
ATOM   7962  C  C     . LEU B 2 512 ? 131.326 168.811 184.095 1.00 58.15  ? 512 LEU B C     1 
ATOM   7963  O  O     . LEU B 2 512 ? 131.175 170.025 184.268 1.00 59.36  ? 512 LEU B O     1 
ATOM   7964  C  CB    . LEU B 2 512 ? 133.796 168.452 183.852 1.00 59.33  ? 512 LEU B CB    1 
ATOM   7965  C  CG    . LEU B 2 512 ? 134.891 167.503 183.360 1.00 60.69  ? 512 LEU B CG    1 
ATOM   7966  C  CD1   . LEU B 2 512 ? 135.762 168.181 182.314 1.00 59.24  ? 512 LEU B CD1   1 
ATOM   7967  C  CD2   . LEU B 2 512 ? 135.734 167.003 184.523 1.00 57.86  ? 512 LEU B CD2   1 
ATOM   7968  N  N     . VAL B 2 513 ? 130.559 167.891 184.673 1.00 56.66  ? 513 VAL B N     1 
ATOM   7969  C  CA    . VAL B 2 513 ? 129.372 168.219 185.453 1.00 58.48  ? 513 VAL B CA    1 
ATOM   7970  C  C     . VAL B 2 513 ? 129.654 167.937 186.921 1.00 56.42  ? 513 VAL B C     1 
ATOM   7971  O  O     . VAL B 2 513 ? 130.097 166.838 187.276 1.00 57.15  ? 513 VAL B O     1 
ATOM   7972  C  CB    . VAL B 2 513 ? 128.146 167.425 184.971 1.00 58.48  ? 513 VAL B CB    1 
ATOM   7973  C  CG1   . VAL B 2 513 ? 126.870 168.016 185.550 1.00 55.54  ? 513 VAL B CG1   1 
ATOM   7974  C  CG2   . VAL B 2 513 ? 128.095 167.407 183.455 1.00 58.35  ? 513 VAL B CG2   1 
ATOM   7975  N  N     . ALA B 2 514 ? 129.401 168.929 187.768 1.00 52.03  ? 514 ALA B N     1 
ATOM   7976  C  CA    . ALA B 2 514 ? 129.464 168.774 189.214 1.00 52.81  ? 514 ALA B CA    1 
ATOM   7977  C  C     . ALA B 2 514 ? 128.046 168.667 189.755 1.00 53.45  ? 514 ALA B C     1 
ATOM   7978  O  O     . ALA B 2 514 ? 127.207 169.532 189.483 1.00 55.12  ? 514 ALA B O     1 
ATOM   7979  C  CB    . ALA B 2 514 ? 130.199 169.948 189.864 1.00 50.98  ? 514 ALA B CB    1 
ATOM   7980  N  N     . MET B 2 515 ? 127.779 167.606 190.511 1.00 54.57  ? 515 MET B N     1 
ATOM   7981  C  CA    . MET B 2 515 ? 126.449 167.343 191.041 1.00 56.50  ? 515 MET B CA    1 
ATOM   7982  C  C     . MET B 2 515 ? 126.519 167.151 192.547 1.00 56.81  ? 515 MET B C     1 
ATOM   7983  O  O     . MET B 2 515 ? 127.360 166.400 193.049 1.00 61.12  ? 515 MET B O     1 
ATOM   7984  C  CB    . MET B 2 515 ? 125.824 166.105 190.385 1.00 57.84  ? 515 MET B CB    1 
ATOM   7985  C  CG    . MET B 2 515 ? 124.624 165.545 191.128 1.00 57.66  ? 515 MET B CG    1 
ATOM   7986  S  SD    . MET B 2 515 ? 123.103 166.438 190.764 1.00 69.17  ? 515 MET B SD    1 
ATOM   7987  C  CE    . MET B 2 515 ? 121.902 165.425 191.623 1.00 59.25  ? 515 MET B CE    1 
ATOM   7988  N  N     . THR B 2 516 ? 125.634 167.838 193.264 1.00 55.49  ? 516 THR B N     1 
ATOM   7989  C  CA    . THR B 2 516 ? 125.498 167.676 194.704 1.00 57.08  ? 516 THR B CA    1 
ATOM   7990  C  C     . THR B 2 516 ? 124.069 167.261 195.027 1.00 56.59  ? 516 THR B C     1 
ATOM   7991  O  O     . THR B 2 516 ? 123.114 167.760 194.424 1.00 61.40  ? 516 THR B O     1 
ATOM   7992  C  CB    . THR B 2 516 ? 125.884 168.965 195.456 1.00 57.55  ? 516 THR B CB    1 
ATOM   7993  O  OG1   . THR B 2 516 ? 125.825 168.734 196.869 1.00 62.96  ? 516 THR B OG1   1 
ATOM   7994  C  CG2   . THR B 2 516 ? 124.969 170.124 195.085 1.00 59.14  ? 516 THR B CG2   1 
ATOM   7995  N  N     . GLY B 2 517 ? 123.929 166.324 195.963 1.00 54.95  ? 517 GLY B N     1 
ATOM   7996  C  CA    . GLY B 2 517 ? 122.621 165.784 196.287 1.00 58.17  ? 517 GLY B CA    1 
ATOM   7997  C  C     . GLY B 2 517 ? 122.590 165.231 197.693 1.00 58.90  ? 517 GLY B C     1 
ATOM   7998  O  O     . GLY B 2 517 ? 123.624 164.945 198.301 1.00 59.17  ? 517 GLY B O     1 
ATOM   7999  N  N     . ASP B 2 518 ? 121.375 165.084 198.204 1.00 66.62  ? 518 ASP B N     1 
ATOM   8000  C  CA    . ASP B 2 518 ? 121.148 164.612 199.566 1.00 65.50  ? 518 ASP B CA    1 
ATOM   8001  C  C     . ASP B 2 518 ? 120.257 163.379 199.630 1.00 67.09  ? 518 ASP B C     1 
ATOM   8002  O  O     . ASP B 2 518 ? 120.497 162.501 200.462 1.00 67.07  ? 518 ASP B O     1 
ATOM   8003  C  CB    . ASP B 2 518 ? 120.541 165.758 200.408 1.00 64.76  ? 518 ASP B CB    1 
ATOM   8004  C  CG    . ASP B 2 518 ? 120.178 165.330 201.821 1.00 69.36  ? 518 ASP B CG    1 
ATOM   8005  O  OD1   . ASP B 2 518 ? 119.179 164.602 202.001 1.00 69.08  ? 518 ASP B OD1   1 
ATOM   8006  O  OD2   . ASP B 2 518 ? 120.897 165.731 202.761 1.00 70.31  ? 518 ASP B OD2   1 
ATOM   8007  N  N     . GLY B 2 519 ? 119.238 163.289 198.774 1.00 73.25  ? 519 GLY B N     1 
ATOM   8008  C  CA    . GLY B 2 519 ? 118.281 162.206 198.862 1.00 70.18  ? 519 GLY B CA    1 
ATOM   8009  C  C     . GLY B 2 519 ? 118.765 160.913 198.232 1.00 70.02  ? 519 GLY B C     1 
ATOM   8010  O  O     . GLY B 2 519 ? 119.827 160.838 197.614 1.00 71.42  ? 519 GLY B O     1 
ATOM   8011  N  N     . THR B 2 520 ? 117.948 159.869 198.403 1.00 72.75  ? 520 THR B N     1 
ATOM   8012  C  CA    . THR B 2 520 ? 118.291 158.556 197.864 1.00 73.48  ? 520 THR B CA    1 
ATOM   8013  C  C     . THR B 2 520 ? 118.102 158.497 196.354 1.00 73.10  ? 520 THR B C     1 
ATOM   8014  O  O     . THR B 2 520 ? 118.821 157.759 195.669 1.00 73.07  ? 520 THR B O     1 
ATOM   8015  C  CB    . THR B 2 520 ? 117.451 157.470 198.538 1.00 73.61  ? 520 THR B CB    1 
ATOM   8016  O  OG1   . THR B 2 520 ? 117.207 157.829 199.903 1.00 74.27  ? 520 THR B OG1   1 
ATOM   8017  C  CG2   . THR B 2 520 ? 118.177 156.135 198.494 1.00 73.34  ? 520 THR B CG2   1 
ATOM   8018  N  N     . ASN B 2 521 ? 117.145 159.258 195.817 1.00 71.84  ? 521 ASN B N     1 
ATOM   8019  C  CA    . ASN B 2 521 ? 116.899 159.242 194.380 1.00 71.81  ? 521 ASN B CA    1 
ATOM   8020  C  C     . ASN B 2 521 ? 118.030 159.880 193.586 1.00 72.91  ? 521 ASN B C     1 
ATOM   8021  O  O     . ASN B 2 521 ? 118.059 159.739 192.359 1.00 74.48  ? 521 ASN B O     1 
ATOM   8022  C  CB    . ASN B 2 521 ? 115.582 159.948 194.061 1.00 72.37  ? 521 ASN B CB    1 
ATOM   8023  C  CG    . ASN B 2 521 ? 115.405 161.235 194.843 1.00 72.73  ? 521 ASN B CG    1 
ATOM   8024  O  OD1   . ASN B 2 521 ? 116.374 161.813 195.335 1.00 72.58  ? 521 ASN B OD1   1 
ATOM   8025  N  ND2   . ASN B 2 521 ? 114.163 161.690 194.960 1.00 72.08  ? 521 ASN B ND2   1 
ATOM   8026  N  N     . ASP B 2 522 ? 118.951 160.580 194.248 1.00 69.56  ? 522 ASP B N     1 
ATOM   8027  C  CA    . ASP B 2 522 ? 120.089 161.189 193.571 1.00 68.13  ? 522 ASP B CA    1 
ATOM   8028  C  C     . ASP B 2 522 ? 121.253 160.223 193.378 1.00 68.05  ? 522 ASP B C     1 
ATOM   8029  O  O     . ASP B 2 522 ? 122.222 160.581 192.701 1.00 70.82  ? 522 ASP B O     1 
ATOM   8030  C  CB    . ASP B 2 522 ? 120.568 162.416 194.355 1.00 68.57  ? 522 ASP B CB    1 
ATOM   8031  C  CG    . ASP B 2 522 ? 119.536 163.526 194.385 1.00 70.67  ? 522 ASP B CG    1 
ATOM   8032  O  OD1   . ASP B 2 522 ? 118.650 163.538 193.509 1.00 71.71  ? 522 ASP B OD1   1 
ATOM   8033  O  OD2   . ASP B 2 522 ? 119.610 164.391 195.282 1.00 69.61  ? 522 ASP B OD2   1 
ATOM   8034  N  N     . ALA B 2 523 ? 121.186 159.021 193.959 1.00 66.75  ? 523 ALA B N     1 
ATOM   8035  C  CA    . ALA B 2 523 ? 122.304 158.084 193.852 1.00 67.04  ? 523 ALA B CA    1 
ATOM   8036  C  C     . ALA B 2 523 ? 122.621 157.709 192.411 1.00 68.81  ? 523 ALA B C     1 
ATOM   8037  O  O     . ALA B 2 523 ? 123.811 157.697 192.049 1.00 70.26  ? 523 ALA B O     1 
ATOM   8038  C  CB    . ALA B 2 523 ? 122.026 156.845 194.711 1.00 68.50  ? 523 ALA B CB    1 
ATOM   8039  N  N     . PRO B 2 524 ? 121.647 157.389 191.551 1.00 69.60  ? 524 PRO B N     1 
ATOM   8040  C  CA    . PRO B 2 524 ? 121.969 157.203 190.117 1.00 68.60  ? 524 PRO B CA    1 
ATOM   8041  C  C     . PRO B 2 524 ? 122.608 158.412 189.450 1.00 67.07  ? 524 PRO B C     1 
ATOM   8042  O  O     . PRO B 2 524 ? 123.485 158.241 188.595 1.00 67.69  ? 524 PRO B O     1 
ATOM   8043  C  CB    . PRO B 2 524 ? 120.564 156.911 189.591 1.00 67.38  ? 524 PRO B CB    1 
ATOM   8044  C  CG    . PRO B 2 524 ? 119.850 157.590 190.818 1.00 67.47  ? 524 PRO B CG    1 
ATOM   8045  C  CD    . PRO B 2 524 ? 120.290 156.787 191.732 1.00 67.94  ? 524 PRO B CD    1 
ATOM   8046  N  N     . ALA B 2 525 ? 122.196 159.631 189.808 1.00 65.41  ? 525 ALA B N     1 
ATOM   8047  C  CA    . ALA B 2 525 ? 122.759 160.814 189.164 1.00 66.97  ? 525 ALA B CA    1 
ATOM   8048  C  C     . ALA B 2 525 ? 124.082 161.214 189.800 1.00 67.54  ? 525 ALA B C     1 
ATOM   8049  O  O     . ALA B 2 525 ? 124.843 162.000 189.224 1.00 66.48  ? 525 ALA B O     1 
ATOM   8050  C  CB    . ALA B 2 525 ? 121.765 161.971 189.221 1.00 64.80  ? 525 ALA B CB    1 
ATOM   8051  N  N     . LEU B 2 526 ? 124.377 160.680 190.986 1.00 63.21  ? 526 LEU B N     1 
ATOM   8052  C  CA    . LEU B 2 526 ? 125.650 160.987 191.628 1.00 60.39  ? 526 LEU B CA    1 
ATOM   8053  C  C     . LEU B 2 526 ? 126.772 160.105 191.098 1.00 62.19  ? 526 LEU B C     1 
ATOM   8054  O  O     . LEU B 2 526 ? 127.933 160.527 191.088 1.00 65.09  ? 526 LEU B O     1 
ATOM   8055  C  CB    . LEU B 2 526 ? 125.532 160.844 193.145 1.00 62.89  ? 526 LEU B CB    1 
ATOM   8056  C  CG    . LEU B 2 526 ? 124.887 162.023 193.879 1.00 61.69  ? 526 LEU B CG    1 
ATOM   8057  C  CD1   . LEU B 2 526 ? 124.529 161.644 195.306 1.00 60.84  ? 526 LEU B CD1   1 
ATOM   8058  C  CD2   . LEU B 2 526 ? 125.782 163.253 193.856 1.00 61.31  ? 526 LEU B CD2   1 
ATOM   8059  N  N     . ALA B 2 527 ? 126.454 158.888 190.651 1.00 64.27  ? 527 ALA B N     1 
ATOM   8060  C  CA    . ALA B 2 527 ? 127.480 158.018 190.093 1.00 65.90  ? 527 ALA B CA    1 
ATOM   8061  C  C     . ALA B 2 527 ? 127.810 158.370 188.650 1.00 66.63  ? 527 ALA B C     1 
ATOM   8062  O  O     . ALA B 2 527 ? 128.777 157.833 188.098 1.00 67.26  ? 527 ALA B O     1 
ATOM   8063  C  CB    . ALA B 2 527 ? 127.043 156.556 190.188 1.00 65.80  ? 527 ALA B CB    1 
ATOM   8064  N  N     . GLN B 2 528 ? 127.035 159.258 188.030 1.00 64.44  ? 528 GLN B N     1 
ATOM   8065  C  CA    . GLN B 2 528 ? 127.270 159.643 186.645 1.00 65.00  ? 528 GLN B CA    1 
ATOM   8066  C  C     . GLN B 2 528 ? 128.116 160.901 186.519 1.00 67.38  ? 528 GLN B C     1 
ATOM   8067  O  O     . GLN B 2 528 ? 128.944 160.993 185.604 1.00 68.08  ? 528 GLN B O     1 
ATOM   8068  C  CB    . GLN B 2 528 ? 125.935 159.850 185.924 1.00 66.11  ? 528 GLN B CB    1 
ATOM   8069  C  CG    . GLN B 2 528 ? 126.063 160.089 184.430 1.00 67.69  ? 528 GLN B CG    1 
ATOM   8070  C  CD    . GLN B 2 528 ? 126.919 159.042 183.744 1.00 67.64  ? 528 GLN B CD    1 
ATOM   8071  O  OE1   . GLN B 2 528 ? 126.622 157.849 183.796 1.00 68.69  ? 528 GLN B OE1   1 
ATOM   8072  N  NE2   . GLN B 2 528 ? 127.992 159.486 183.101 1.00 65.51  ? 528 GLN B NE2   1 
ATOM   8073  N  N     . ALA B 2 529 ? 127.929 161.867 187.413 1.00 63.58  ? 529 ALA B N     1 
ATOM   8074  C  CA    . ALA B 2 529 ? 128.690 163.106 187.349 1.00 62.02  ? 529 ALA B CA    1 
ATOM   8075  C  C     . ALA B 2 529 ? 130.159 162.853 187.663 1.00 61.45  ? 529 ALA B C     1 
ATOM   8076  O  O     . ALA B 2 529 ? 130.498 161.999 188.488 1.00 62.33  ? 529 ALA B O     1 
ATOM   8077  C  CB    . ALA B 2 529 ? 128.113 164.134 188.321 1.00 59.73  ? 529 ALA B CB    1 
ATOM   8078  N  N     . ASP B 2 530 ? 131.035 163.605 186.992 1.00 59.74  ? 530 ASP B N     1 
ATOM   8079  C  CA    . ASP B 2 530 ? 132.469 163.457 187.223 1.00 59.20  ? 530 ASP B CA    1 
ATOM   8080  C  C     . ASP B 2 530 ? 132.845 163.875 188.639 1.00 59.35  ? 530 ASP B C     1 
ATOM   8081  O  O     . ASP B 2 530 ? 133.660 163.216 189.295 1.00 59.13  ? 530 ASP B O     1 
ATOM   8082  C  CB    . ASP B 2 530 ? 133.252 164.273 186.195 1.00 58.38  ? 530 ASP B CB    1 
ATOM   8083  C  CG    . ASP B 2 530 ? 132.901 163.902 184.768 1.00 62.10  ? 530 ASP B CG    1 
ATOM   8084  O  OD1   . ASP B 2 530 ? 133.453 162.904 184.259 1.00 63.60  ? 530 ASP B OD1   1 
ATOM   8085  O  OD2   . ASP B 2 530 ? 132.076 164.610 184.154 1.00 62.27  ? 530 ASP B OD2   1 
ATOM   8086  N  N     . VAL B 2 531 ? 132.264 164.968 189.125 1.00 55.05  ? 531 VAL B N     1 
ATOM   8087  C  CA    . VAL B 2 531 ? 132.473 165.444 190.487 1.00 51.10  ? 531 VAL B CA    1 
ATOM   8088  C  C     . VAL B 2 531 ? 131.138 165.373 191.211 1.00 49.97  ? 531 VAL B C     1 
ATOM   8089  O  O     . VAL B 2 531 ? 130.186 166.071 190.840 1.00 53.93  ? 531 VAL B O     1 
ATOM   8090  C  CB    . VAL B 2 531 ? 133.040 166.871 190.517 1.00 52.08  ? 531 VAL B CB    1 
ATOM   8091  C  CG1   . VAL B 2 531 ? 133.354 167.285 191.946 1.00 52.04  ? 531 VAL B CG1   1 
ATOM   8092  C  CG2   . VAL B 2 531 ? 134.286 166.962 189.651 1.00 53.07  ? 531 VAL B CG2   1 
ATOM   8093  N  N     . ALA B 2 532 ? 131.066 164.532 192.239 1.00 53.36  ? 532 ALA B N     1 
ATOM   8094  C  CA    . ALA B 2 532 ? 129.843 164.335 193.002 1.00 51.57  ? 532 ALA B CA    1 
ATOM   8095  C  C     . ALA B 2 532 ? 130.128 164.563 194.477 1.00 55.03  ? 532 ALA B C     1 
ATOM   8096  O  O     . ALA B 2 532 ? 131.023 163.929 195.045 1.00 61.81  ? 532 ALA B O     1 
ATOM   8097  C  CB    . ALA B 2 532 ? 129.274 162.932 192.780 1.00 52.75  ? 532 ALA B CB    1 
ATOM   8098  N  N     . VAL B 2 533 ? 129.367 165.463 195.093 1.00 46.90  ? 533 VAL B N     1 
ATOM   8099  C  CA    . VAL B 2 533 ? 129.506 165.792 196.506 1.00 50.79  ? 533 VAL B CA    1 
ATOM   8100  C  C     . VAL B 2 533 ? 128.206 165.429 197.207 1.00 49.78  ? 533 VAL B C     1 
ATOM   8101  O  O     . VAL B 2 533 ? 127.129 165.878 196.799 1.00 52.72  ? 533 VAL B O     1 
ATOM   8102  C  CB    . VAL B 2 533 ? 129.847 167.279 196.714 1.00 48.37  ? 533 VAL B CB    1 
ATOM   8103  C  CG1   . VAL B 2 533 ? 130.097 167.563 198.186 1.00 49.60  ? 533 VAL B CG1   1 
ATOM   8104  C  CG2   . VAL B 2 533 ? 131.055 167.669 195.877 1.00 49.27  ? 533 VAL B CG2   1 
ATOM   8105  N  N     . ALA B 2 534 ? 128.307 164.619 198.255 1.00 54.04  ? 534 ALA B N     1 
ATOM   8106  C  CA    . ALA B 2 534 ? 127.151 164.161 199.014 1.00 51.52  ? 534 ALA B CA    1 
ATOM   8107  C  C     . ALA B 2 534 ? 127.172 164.786 200.401 1.00 53.13  ? 534 ALA B C     1 
ATOM   8108  O  O     . ALA B 2 534 ? 128.204 164.766 201.080 1.00 58.87  ? 534 ALA B O     1 
ATOM   8109  C  CB    . ALA B 2 534 ? 127.135 162.635 199.119 1.00 50.28  ? 534 ALA B CB    1 
ATOM   8110  N  N     . MET B 2 535 ? 126.037 165.343 200.813 1.00 52.94  ? 535 MET B N     1 
ATOM   8111  C  CA    . MET B 2 535 ? 125.923 165.907 202.150 1.00 54.14  ? 535 MET B CA    1 
ATOM   8112  C  C     . MET B 2 535 ? 126.016 164.812 203.205 1.00 55.47  ? 535 MET B C     1 
ATOM   8113  O  O     . MET B 2 535 ? 125.544 163.689 203.004 1.00 57.95  ? 535 MET B O     1 
ATOM   8114  C  CB    . MET B 2 535 ? 124.605 166.669 202.297 1.00 56.24  ? 535 MET B CB    1 
ATOM   8115  C  CG    . MET B 2 535 ? 124.167 167.428 201.051 1.00 55.01  ? 535 MET B CG    1 
ATOM   8116  S  SD    . MET B 2 535 ? 124.935 169.058 200.908 1.00 61.16  ? 535 MET B SD    1 
ATOM   8117  C  CE    . MET B 2 535 ? 126.426 168.684 199.989 1.00 55.46  ? 535 MET B CE    1 
ATOM   8118  N  N     . ASN B 2 536 ? 126.635 165.148 204.339 1.00 57.69  ? 536 ASN B N     1 
ATOM   8119  C  CA    . ASN B 2 536 ? 126.764 164.191 205.430 1.00 58.71  ? 536 ASN B CA    1 
ATOM   8120  C  C     . ASN B 2 536 ? 125.441 163.954 206.146 1.00 61.53  ? 536 ASN B C     1 
ATOM   8121  O  O     . ASN B 2 536 ? 125.300 162.947 206.848 1.00 61.45  ? 536 ASN B O     1 
ATOM   8122  C  CB    . ASN B 2 536 ? 127.822 164.675 206.425 1.00 57.52  ? 536 ASN B CB    1 
ATOM   8123  C  CG    . ASN B 2 536 ? 128.143 163.642 207.486 1.00 60.21  ? 536 ASN B CG    1 
ATOM   8124  O  OD1   . ASN B 2 536 ? 128.752 162.611 207.202 1.00 62.60  ? 536 ASN B OD1   1 
ATOM   8125  N  ND2   . ASN B 2 536 ? 127.735 163.916 208.720 1.00 60.22  ? 536 ASN B ND2   1 
ATOM   8126  N  N     . SER B 2 537 ? 124.469 164.846 205.975 1.00 62.34  ? 537 SER B N     1 
ATOM   8127  C  CA    . SER B 2 537 ? 123.156 164.700 206.585 1.00 62.84  ? 537 SER B CA    1 
ATOM   8128  C  C     . SER B 2 537 ? 122.180 163.929 205.707 1.00 62.64  ? 537 SER B C     1 
ATOM   8129  O  O     . SER B 2 537 ? 121.019 163.761 206.095 1.00 65.91  ? 537 SER B O     1 
ATOM   8130  C  CB    . SER B 2 537 ? 122.572 166.078 206.914 1.00 61.91  ? 537 SER B CB    1 
ATOM   8131  O  OG    . SER B 2 537 ? 122.706 166.964 205.817 1.00 63.32  ? 537 SER B OG    1 
ATOM   8132  N  N     . GLY B 2 538 ? 122.618 163.457 204.542 1.00 61.28  ? 538 GLY B N     1 
ATOM   8133  C  CA    . GLY B 2 538 ? 121.768 162.711 203.641 1.00 60.96  ? 538 GLY B CA    1 
ATOM   8134  C  C     . GLY B 2 538 ? 121.780 161.224 203.934 1.00 65.02  ? 538 GLY B C     1 
ATOM   8135  O  O     . GLY B 2 538 ? 122.116 160.771 205.030 1.00 66.60  ? 538 GLY B O     1 
ATOM   8136  N  N     . THR B 2 539 ? 121.401 160.452 202.920 1.00 69.70  ? 539 THR B N     1 
ATOM   8137  C  CA    . THR B 2 539 ? 121.324 159.008 203.054 1.00 69.41  ? 539 THR B CA    1 
ATOM   8138  C  C     . THR B 2 539 ? 122.676 158.365 202.757 1.00 68.86  ? 539 THR B C     1 
ATOM   8139  O  O     . THR B 2 539 ? 123.577 158.981 202.181 1.00 69.01  ? 539 THR B O     1 
ATOM   8140  C  CB    . THR B 2 539 ? 120.257 158.437 202.120 1.00 69.37  ? 539 THR B CB    1 
ATOM   8141  O  OG1   . THR B 2 539 ? 120.658 158.630 200.758 1.00 70.00  ? 539 THR B OG1   1 
ATOM   8142  C  CG2   . THR B 2 539 ? 118.924 159.133 202.352 1.00 68.94  ? 539 THR B CG2   1 
ATOM   8143  N  N     . GLN B 2 540 ? 122.808 157.099 203.162 1.00 67.92  ? 540 GLN B N     1 
ATOM   8144  C  CA    . GLN B 2 540 ? 124.055 156.377 202.934 1.00 68.10  ? 540 GLN B CA    1 
ATOM   8145  C  C     . GLN B 2 540 ? 124.231 156.004 201.468 1.00 71.25  ? 540 GLN B C     1 
ATOM   8146  O  O     . GLN B 2 540 ? 125.366 155.908 200.988 1.00 72.04  ? 540 GLN B O     1 
ATOM   8147  C  CB    . GLN B 2 540 ? 124.103 155.125 203.810 1.00 68.49  ? 540 GLN B CB    1 
ATOM   8148  C  CG    . GLN B 2 540 ? 125.474 154.471 203.889 1.00 69.92  ? 540 GLN B CG    1 
ATOM   8149  C  CD    . GLN B 2 540 ? 126.509 155.365 204.544 1.00 72.47  ? 540 GLN B CD    1 
ATOM   8150  O  OE1   . GLN B 2 540 ? 127.572 155.620 203.979 1.00 71.18  ? 540 GLN B OE1   1 
ATOM   8151  N  NE2   . GLN B 2 540 ? 126.201 155.846 205.742 1.00 69.68  ? 540 GLN B NE2   1 
ATOM   8152  N  N     . ALA B 2 541 ? 123.129 155.787 200.747 1.00 68.12  ? 541 ALA B N     1 
ATOM   8153  C  CA    . ALA B 2 541 ? 123.227 155.446 199.331 1.00 68.54  ? 541 ALA B CA    1 
ATOM   8154  C  C     . ALA B 2 541 ? 123.848 156.584 198.530 1.00 69.36  ? 541 ALA B C     1 
ATOM   8155  O  O     . ALA B 2 541 ? 124.670 156.348 197.638 1.00 69.74  ? 541 ALA B O     1 
ATOM   8156  C  CB    . ALA B 2 541 ? 121.846 155.091 198.780 1.00 67.69  ? 541 ALA B CB    1 
ATOM   8157  N  N     . ALA B 2 542 ? 123.463 157.825 198.834 1.00 67.35  ? 542 ALA B N     1 
ATOM   8158  C  CA    . ALA B 2 542 ? 124.034 158.970 198.131 1.00 65.71  ? 542 ALA B CA    1 
ATOM   8159  C  C     . ALA B 2 542 ? 125.498 159.174 198.500 1.00 65.10  ? 542 ALA B C     1 
ATOM   8160  O  O     . ALA B 2 542 ? 126.298 159.615 197.666 1.00 65.89  ? 542 ALA B O     1 
ATOM   8161  C  CB    . ALA B 2 542 ? 123.222 160.229 198.434 1.00 64.02  ? 542 ALA B CB    1 
ATOM   8162  N  N     . LYS B 2 543 ? 125.867 158.866 199.746 1.00 64.23  ? 543 LYS B N     1 
ATOM   8163  C  CA    . LYS B 2 543 ? 127.246 159.065 200.182 1.00 63.31  ? 543 LYS B CA    1 
ATOM   8164  C  C     . LYS B 2 543 ? 128.200 158.118 199.464 1.00 66.95  ? 543 LYS B C     1 
ATOM   8165  O  O     . LYS B 2 543 ? 129.336 158.492 199.149 1.00 69.28  ? 543 LYS B O     1 
ATOM   8166  C  CB    . LYS B 2 543 ? 127.348 158.883 201.696 1.00 63.75  ? 543 LYS B CB    1 
ATOM   8167  C  CG    . LYS B 2 543 ? 126.694 159.993 202.503 1.00 65.12  ? 543 LYS B CG    1 
ATOM   8168  C  CD    . LYS B 2 543 ? 127.072 159.902 203.972 1.00 64.41  ? 543 LYS B CD    1 
ATOM   8169  C  CE    . LYS B 2 543 ? 125.916 160.320 204.866 1.00 65.86  ? 543 LYS B CE    1 
ATOM   8170  N  NZ    . LYS B 2 543 ? 126.224 160.110 206.308 1.00 65.93  ? 543 LYS B NZ    1 
ATOM   8171  N  N     . GLU B 2 544 ? 127.758 156.887 199.196 1.00 69.04  ? 544 GLU B N     1 
ATOM   8172  C  CA    . GLU B 2 544 ? 128.630 155.927 198.528 1.00 69.23  ? 544 GLU B CA    1 
ATOM   8173  C  C     . GLU B 2 544 ? 128.618 156.110 197.016 1.00 67.96  ? 544 GLU B C     1 
ATOM   8174  O  O     . GLU B 2 544 ? 129.647 155.907 196.361 1.00 68.11  ? 544 GLU B O     1 
ATOM   8175  C  CB    . GLU B 2 544 ? 128.221 154.500 198.893 1.00 68.06  ? 544 GLU B CB    1 
ATOM   8176  C  CG    . GLU B 2 544 ? 128.663 154.065 200.282 1.00 70.10  ? 544 GLU B CG    1 
ATOM   8177  C  CD    . GLU B 2 544 ? 130.103 153.586 200.313 1.00 71.92  ? 544 GLU B CD    1 
ATOM   8178  O  OE1   . GLU B 2 544 ? 130.640 153.390 201.424 1.00 71.05  ? 544 GLU B OE1   1 
ATOM   8179  O  OE2   . GLU B 2 544 ? 130.696 153.407 199.229 1.00 71.28  ? 544 GLU B OE2   1 
ATOM   8180  N  N     . ALA B 2 545 ? 127.471 156.486 196.445 1.00 65.05  ? 545 ALA B N     1 
ATOM   8181  C  CA    . ALA B 2 545 ? 127.407 156.739 195.009 1.00 66.77  ? 545 ALA B CA    1 
ATOM   8182  C  C     . ALA B 2 545 ? 128.264 157.932 194.608 1.00 67.35  ? 545 ALA B C     1 
ATOM   8183  O  O     . ALA B 2 545 ? 128.929 157.894 193.567 1.00 68.03  ? 545 ALA B O     1 
ATOM   8184  C  CB    . ALA B 2 545 ? 125.958 156.957 194.577 1.00 63.72  ? 545 ALA B CB    1 
ATOM   8185  N  N     . GLY B 2 546 ? 128.261 158.995 195.414 1.00 60.83  ? 546 GLY B N     1 
ATOM   8186  C  CA    . GLY B 2 546 ? 129.029 160.175 195.084 1.00 59.91  ? 546 GLY B CA    1 
ATOM   8187  C  C     . GLY B 2 546 ? 130.522 159.988 195.274 1.00 60.41  ? 546 GLY B C     1 
ATOM   8188  O  O     . GLY B 2 546 ? 130.985 159.129 196.024 1.00 62.73  ? 546 GLY B O     1 
ATOM   8189  N  N     . ASN B 2 547 ? 131.288 160.822 194.567 1.00 58.21  ? 547 ASN B N     1 
ATOM   8190  C  CA    . ASN B 2 547 ? 132.743 160.765 194.674 1.00 55.46  ? 547 ASN B CA    1 
ATOM   8191  C  C     . ASN B 2 547 ? 133.223 161.284 196.024 1.00 56.81  ? 547 ASN B C     1 
ATOM   8192  O  O     . ASN B 2 547 ? 134.074 160.659 196.668 1.00 57.39  ? 547 ASN B O     1 
ATOM   8193  C  CB    . ASN B 2 547 ? 133.386 161.560 193.538 1.00 52.54  ? 547 ASN B CB    1 
ATOM   8194  C  CG    . ASN B 2 547 ? 133.629 160.719 192.302 1.00 56.69  ? 547 ASN B CG    1 
ATOM   8195  O  OD1   . ASN B 2 547 ? 133.877 159.517 192.394 1.00 63.58  ? 547 ASN B OD1   1 
ATOM   8196  N  ND2   . ASN B 2 547 ? 133.562 161.348 191.135 1.00 56.13  ? 547 ASN B ND2   1 
ATOM   8197  N  N     . MET B 2 548 ? 132.695 162.423 196.467 1.00 52.06  ? 548 MET B N     1 
ATOM   8198  C  CA    . MET B 2 548 ? 133.123 163.049 197.708 1.00 49.15  ? 548 MET B CA    1 
ATOM   8199  C  C     . MET B 2 548 ? 131.932 163.238 198.637 1.00 50.04  ? 548 MET B C     1 
ATOM   8200  O  O     . MET B 2 548 ? 130.776 163.268 198.207 1.00 53.78  ? 548 MET B O     1 
ATOM   8201  C  CB    . MET B 2 548 ? 133.805 164.401 197.455 1.00 51.75  ? 548 MET B CB    1 
ATOM   8202  C  CG    . MET B 2 548 ? 134.807 164.391 196.314 1.00 53.80  ? 548 MET B CG    1 
ATOM   8203  S  SD    . MET B 2 548 ? 134.940 165.990 195.495 1.00 55.94  ? 548 MET B SD    1 
ATOM   8204  C  CE    . MET B 2 548 ? 135.885 165.542 194.042 1.00 52.61  ? 548 MET B CE    1 
ATOM   8205  N  N     . VAL B 2 549 ? 132.236 163.364 199.926 1.00 51.82  ? 549 VAL B N     1 
ATOM   8206  C  CA    . VAL B 2 549 ? 131.243 163.608 200.964 1.00 50.92  ? 549 VAL B CA    1 
ATOM   8207  C  C     . VAL B 2 549 ? 131.638 164.875 201.709 1.00 51.41  ? 549 VAL B C     1 
ATOM   8208  O  O     . VAL B 2 549 ? 132.779 165.000 202.167 1.00 55.33  ? 549 VAL B O     1 
ATOM   8209  C  CB    . VAL B 2 549 ? 131.126 162.419 201.935 1.00 52.23  ? 549 VAL B CB    1 
ATOM   8210  C  CG1   . VAL B 2 549 ? 130.063 162.696 202.987 1.00 50.44  ? 549 VAL B CG1   1 
ATOM   8211  C  CG2   . VAL B 2 549 ? 130.811 161.139 201.177 1.00 52.54  ? 549 VAL B CG2   1 
ATOM   8212  N  N     . ASP B 2 550 ? 130.697 165.807 201.831 1.00 47.53  ? 550 ASP B N     1 
ATOM   8213  C  CA    . ASP B 2 550 ? 130.923 167.061 202.537 1.00 47.93  ? 550 ASP B CA    1 
ATOM   8214  C  C     . ASP B 2 550 ? 130.387 166.930 203.957 1.00 52.94  ? 550 ASP B C     1 
ATOM   8215  O  O     . ASP B 2 550 ? 129.187 166.707 204.154 1.00 56.81  ? 550 ASP B O     1 
ATOM   8216  C  CB    . ASP B 2 550 ? 130.252 168.226 201.811 1.00 49.21  ? 550 ASP B CB    1 
ATOM   8217  C  CG    . ASP B 2 550 ? 130.282 169.509 202.618 1.00 53.51  ? 550 ASP B CG    1 
ATOM   8218  O  OD1   . ASP B 2 550 ? 131.323 169.796 203.245 1.00 55.01  ? 550 ASP B OD1   1 
ATOM   8219  O  OD2   . ASP B 2 550 ? 129.265 170.232 202.623 1.00 56.80  ? 550 ASP B OD2   1 
ATOM   8220  N  N     . LEU B 2 551 ? 131.276 167.072 204.941 1.00 52.43  ? 551 LEU B N     1 
ATOM   8221  C  CA    . LEU B 2 551 ? 130.891 166.913 206.337 1.00 51.21  ? 551 LEU B CA    1 
ATOM   8222  C  C     . LEU B 2 551 ? 130.080 168.088 206.867 1.00 52.70  ? 551 LEU B C     1 
ATOM   8223  O  O     . LEU B 2 551 ? 129.344 167.922 207.845 1.00 56.88  ? 551 LEU B O     1 
ATOM   8224  C  CB    . LEU B 2 551 ? 132.136 166.716 207.204 1.00 50.30  ? 551 LEU B CB    1 
ATOM   8225  C  CG    . LEU B 2 551 ? 132.910 165.417 206.975 1.00 53.41  ? 551 LEU B CG    1 
ATOM   8226  C  CD1   . LEU B 2 551 ? 134.259 165.463 207.677 1.00 51.08  ? 551 LEU B CD1   1 
ATOM   8227  C  CD2   . LEU B 2 551 ? 132.099 164.217 207.439 1.00 52.30  ? 551 LEU B CD2   1 
ATOM   8228  N  N     . ASP B 2 552 ? 130.195 169.261 206.251 1.00 52.97  ? 552 ASP B N     1 
ATOM   8229  C  CA    . ASP B 2 552 ? 129.475 170.446 206.699 1.00 54.75  ? 552 ASP B CA    1 
ATOM   8230  C  C     . ASP B 2 552 ? 128.121 170.613 206.021 1.00 56.69  ? 552 ASP B C     1 
ATOM   8231  O  O     . ASP B 2 552 ? 127.404 171.568 206.340 1.00 58.23  ? 552 ASP B O     1 
ATOM   8232  C  CB    . ASP B 2 552 ? 130.325 171.698 206.461 1.00 54.82  ? 552 ASP B CB    1 
ATOM   8233  C  CG    . ASP B 2 552 ? 131.294 171.968 207.594 1.00 58.27  ? 552 ASP B CG    1 
ATOM   8234  O  OD1   . ASP B 2 552 ? 130.841 172.084 208.752 1.00 56.04  ? 552 ASP B OD1   1 
ATOM   8235  O  OD2   . ASP B 2 552 ? 132.510 172.065 207.328 1.00 59.70  ? 552 ASP B OD2   1 
ATOM   8236  N  N     . SER B 2 553 ? 127.755 169.707 205.111 1.00 53.64  ? 553 SER B N     1 
ATOM   8237  C  CA    . SER B 2 553 ? 126.494 169.785 204.369 1.00 53.18  ? 553 SER B CA    1 
ATOM   8238  C  C     . SER B 2 553 ? 126.329 171.146 203.695 1.00 54.26  ? 553 SER B C     1 
ATOM   8239  O  O     . SER B 2 553 ? 125.262 171.761 203.746 1.00 55.20  ? 553 SER B O     1 
ATOM   8240  C  CB    . SER B 2 553 ? 125.299 169.476 205.274 1.00 53.32  ? 553 SER B CB    1 
ATOM   8241  O  OG    . SER B 2 553 ? 125.390 168.166 205.806 1.00 57.90  ? 553 SER B OG    1 
ATOM   8242  N  N     . ASN B 2 554 ? 127.395 171.617 203.053 1.00 50.32  ? 554 ASN B N     1 
ATOM   8243  C  CA    . ASN B 2 554 ? 127.380 172.914 202.392 1.00 48.91  ? 554 ASN B CA    1 
ATOM   8244  C  C     . ASN B 2 554 ? 127.090 172.728 200.909 1.00 51.56  ? 554 ASN B C     1 
ATOM   8245  O  O     . ASN B 2 554 ? 127.881 172.077 200.213 1.00 53.05  ? 554 ASN B O     1 
ATOM   8246  C  CB    . ASN B 2 554 ? 128.710 173.624 202.575 1.00 51.49  ? 554 ASN B CB    1 
ATOM   8247  C  CG    . ASN B 2 554 ? 128.587 175.131 202.465 1.00 53.62  ? 554 ASN B CG    1 
ATOM   8248  O  OD1   . ASN B 2 554 ? 127.553 175.653 202.051 1.00 54.61  ? 554 ASN B OD1   1 
ATOM   8249  N  ND2   . ASN B 2 554 ? 129.648 175.838 202.835 1.00 55.22  ? 554 ASN B ND2   1 
ATOM   8250  N  N     . PRO B 2 555 ? 125.980 173.259 200.391 1.00 52.98  ? 555 PRO B N     1 
ATOM   8251  C  CA    . PRO B 2 555 ? 125.715 173.134 198.948 1.00 50.89  ? 555 PRO B CA    1 
ATOM   8252  C  C     . PRO B 2 555 ? 126.773 173.790 198.081 1.00 49.18  ? 555 PRO B C     1 
ATOM   8253  O  O     . PRO B 2 555 ? 126.984 173.355 196.942 1.00 52.43  ? 555 PRO B O     1 
ATOM   8254  C  CB    . PRO B 2 555 ? 124.347 173.813 198.786 1.00 50.87  ? 555 PRO B CB    1 
ATOM   8255  C  CG    . PRO B 2 555 ? 124.234 174.724 199.965 1.00 48.59  ? 555 PRO B CG    1 
ATOM   8256  C  CD    . PRO B 2 555 ? 124.920 174.008 201.086 1.00 50.69  ? 555 PRO B CD    1 
ATOM   8257  N  N     . THR B 2 556 ? 127.446 174.827 198.582 1.00 49.94  ? 556 THR B N     1 
ATOM   8258  C  CA    . THR B 2 556 ? 128.476 175.536 197.835 1.00 51.25  ? 556 THR B CA    1 
ATOM   8259  C  C     . THR B 2 556 ? 129.882 175.082 198.211 1.00 47.91  ? 556 THR B C     1 
ATOM   8260  O  O     . THR B 2 556 ? 130.831 175.869 198.130 1.00 52.65  ? 556 THR B O     1 
ATOM   8261  C  CB    . THR B 2 556 ? 128.337 177.044 198.041 1.00 50.65  ? 556 THR B CB    1 
ATOM   8262  O  OG1   . THR B 2 556 ? 128.311 177.335 199.444 1.00 49.25  ? 556 THR B OG1   1 
ATOM   8263  C  CG2   . THR B 2 556 ? 127.052 177.550 197.405 1.00 51.26  ? 556 THR B CG2   1 
ATOM   8264  N  N     . LYS B 2 557 ? 130.037 173.822 198.621 1.00 44.89  ? 557 LYS B N     1 
ATOM   8265  C  CA    . LYS B 2 557 ? 131.349 173.310 198.995 1.00 45.22  ? 557 LYS B CA    1 
ATOM   8266  C  C     . LYS B 2 557 ? 132.244 173.046 197.793 1.00 46.77  ? 557 LYS B C     1 
ATOM   8267  O  O     . LYS B 2 557 ? 133.434 172.771 197.979 1.00 44.86  ? 557 LYS B O     1 
ATOM   8268  C  CB    . LYS B 2 557 ? 131.199 172.030 199.819 1.00 45.07  ? 557 LYS B CB    1 
ATOM   8269  C  CG    . LYS B 2 557 ? 132.300 171.831 200.844 1.00 48.53  ? 557 LYS B CG    1 
ATOM   8270  C  CD    . LYS B 2 557 ? 132.258 172.920 201.903 1.00 46.51  ? 557 LYS B CD    1 
ATOM   8271  C  CE    . LYS B 2 557 ? 133.317 172.697 202.966 1.00 47.17  ? 557 LYS B CE    1 
ATOM   8272  N  NZ    . LYS B 2 557 ? 132.784 172.909 204.339 1.00 51.88  ? 557 LYS B NZ    1 
ATOM   8273  N  N     . LEU B 2 558 ? 131.706 173.122 196.573 1.00 43.80  ? 558 LEU B N     1 
ATOM   8274  C  CA    . LEU B 2 558 ? 132.518 172.928 195.378 1.00 37.63  ? 558 LEU B CA    1 
ATOM   8275  C  C     . LEU B 2 558 ? 133.607 173.986 195.246 1.00 40.10  ? 558 LEU B C     1 
ATOM   8276  O  O     . LEU B 2 558 ? 134.621 173.736 194.585 1.00 41.92  ? 558 LEU B O     1 
ATOM   8277  C  CB    . LEU B 2 558 ? 131.620 172.931 194.137 1.00 38.28  ? 558 LEU B CB    1 
ATOM   8278  C  CG    . LEU B 2 558 ? 132.267 172.707 192.769 1.00 44.13  ? 558 LEU B CG    1 
ATOM   8279  C  CD1   . LEU B 2 558 ? 132.749 171.271 192.630 1.00 41.16  ? 558 LEU B CD1   1 
ATOM   8280  C  CD2   . LEU B 2 558 ? 131.299 173.063 191.652 1.00 41.31  ? 558 LEU B CD2   1 
ATOM   8281  N  N     . ILE B 2 559 ? 133.424 175.154 195.866 1.00 38.03  ? 559 ILE B N     1 
ATOM   8282  C  CA    . ILE B 2 559 ? 134.437 176.204 195.797 1.00 42.40  ? 559 ILE B CA    1 
ATOM   8283  C  C     . ILE B 2 559 ? 135.741 175.732 196.428 1.00 41.55  ? 559 ILE B C     1 
ATOM   8284  O  O     . ILE B 2 559 ? 136.827 175.932 195.870 1.00 43.88  ? 559 ILE B O     1 
ATOM   8285  C  CB    . ILE B 2 559 ? 133.917 177.490 196.467 1.00 40.63  ? 559 ILE B CB    1 
ATOM   8286  C  CG1   . ILE B 2 559 ? 132.686 178.016 195.728 1.00 44.89  ? 559 ILE B CG1   1 
ATOM   8287  C  CG2   . ILE B 2 559 ? 135.007 178.549 196.515 1.00 40.98  ? 559 ILE B CG2   1 
ATOM   8288  C  CD1   . ILE B 2 559 ? 131.826 178.944 196.556 1.00 42.09  ? 559 ILE B CD1   1 
ATOM   8289  N  N     . GLU B 2 560 ? 135.655 175.094 197.598 1.00 37.23  ? 560 GLU B N     1 
ATOM   8290  C  CA    . GLU B 2 560 ? 136.857 174.582 198.250 1.00 32.88  ? 560 GLU B CA    1 
ATOM   8291  C  C     . GLU B 2 560 ? 137.476 173.441 197.453 1.00 33.49  ? 560 GLU B C     1 
ATOM   8292  O  O     . GLU B 2 560 ? 138.704 173.313 197.395 1.00 34.08  ? 560 GLU B O     1 
ATOM   8293  C  CB    . GLU B 2 560 ? 136.532 174.130 199.674 1.00 39.13  ? 560 GLU B CB    1 
ATOM   8294  C  CG    . GLU B 2 560 ? 136.548 175.248 200.706 1.00 41.17  ? 560 GLU B CG    1 
ATOM   8295  C  CD    . GLU B 2 560 ? 135.488 176.301 200.450 1.00 42.79  ? 560 GLU B CD    1 
ATOM   8296  O  OE1   . GLU B 2 560 ? 134.305 175.932 200.299 1.00 42.11  ? 560 GLU B OE1   1 
ATOM   8297  O  OE2   . GLU B 2 560 ? 135.837 177.499 200.400 1.00 45.10  ? 560 GLU B OE2   1 
ATOM   8298  N  N     . VAL B 2 561 ? 136.643 172.601 196.835 1.00 41.01  ? 561 VAL B N     1 
ATOM   8299  C  CA    . VAL B 2 561 ? 137.164 171.507 196.022 1.00 36.24  ? 561 VAL B CA    1 
ATOM   8300  C  C     . VAL B 2 561 ? 137.885 172.050 194.795 1.00 37.76  ? 561 VAL B C     1 
ATOM   8301  O  O     . VAL B 2 561 ? 138.922 171.518 194.382 1.00 37.89  ? 561 VAL B O     1 
ATOM   8302  C  CB    . VAL B 2 561 ? 136.030 170.540 195.636 1.00 38.16  ? 561 VAL B CB    1 
ATOM   8303  C  CG1   . VAL B 2 561 ? 136.599 169.287 194.990 1.00 35.85  ? 561 VAL B CG1   1 
ATOM   8304  C  CG2   . VAL B 2 561 ? 135.200 170.183 196.858 1.00 38.49  ? 561 VAL B CG2   1 
ATOM   8305  N  N     . VAL B 2 562 ? 137.348 173.112 194.193 1.00 37.26  ? 562 VAL B N     1 
ATOM   8306  C  CA    . VAL B 2 562 ? 138.015 173.747 193.060 1.00 36.41  ? 562 VAL B CA    1 
ATOM   8307  C  C     . VAL B 2 562 ? 139.352 174.340 193.492 1.00 35.28  ? 562 VAL B C     1 
ATOM   8308  O  O     . VAL B 2 562 ? 140.355 174.227 192.777 1.00 35.76  ? 562 VAL B O     1 
ATOM   8309  C  CB    . VAL B 2 562 ? 137.094 174.807 192.429 1.00 38.64  ? 562 VAL B CB    1 
ATOM   8310  C  CG1   . VAL B 2 562 ? 137.886 175.750 191.536 1.00 37.89  ? 562 VAL B CG1   1 
ATOM   8311  C  CG2   . VAL B 2 562 ? 135.978 174.136 191.644 1.00 32.65  ? 562 VAL B CG2   1 
ATOM   8312  N  N     . HIS B 2 563 ? 139.384 174.987 194.661 1.00 36.00  ? 563 HIS B N     1 
ATOM   8313  C  CA    . HIS B 2 563 ? 140.621 175.564 195.181 1.00 33.12  ? 563 HIS B CA    1 
ATOM   8314  C  C     . HIS B 2 563 ? 141.741 174.532 195.228 1.00 36.07  ? 563 HIS B C     1 
ATOM   8315  O  O     . HIS B 2 563 ? 142.773 174.682 194.566 1.00 39.81  ? 563 HIS B O     1 
ATOM   8316  C  CB    . HIS B 2 563 ? 140.382 176.146 196.576 1.00 36.99  ? 563 HIS B CB    1 
ATOM   8317  C  CG    . HIS B 2 563 ? 139.688 177.471 196.573 1.00 42.19  ? 563 HIS B CG    1 
ATOM   8318  N  ND1   . HIS B 2 563 ? 139.587 178.264 197.696 1.00 46.67  ? 563 HIS B ND1   1 
ATOM   8319  C  CD2   . HIS B 2 563 ? 139.057 178.142 195.580 1.00 35.19  ? 563 HIS B CD2   1 
ATOM   8320  C  CE1   . HIS B 2 563 ? 138.924 179.365 197.394 1.00 41.97  ? 563 HIS B CE1   1 
ATOM   8321  N  NE2   . HIS B 2 563 ? 138.592 179.317 196.117 1.00 38.17  ? 563 HIS B NE2   1 
ATOM   8322  N  N     . ILE B 2 564 ? 141.549 173.468 196.011 1.00 33.61  ? 564 ILE B N     1 
ATOM   8323  C  CA    . ILE B 2 564 ? 142.607 172.482 196.207 1.00 35.26  ? 564 ILE B CA    1 
ATOM   8324  C  C     . ILE B 2 564 ? 142.902 171.737 194.911 1.00 30.32  ? 564 ILE B C     1 
ATOM   8325  O  O     . ILE B 2 564 ? 144.065 171.465 194.588 1.00 35.52  ? 564 ILE B O     1 
ATOM   8326  C  CB    . ILE B 2 564 ? 142.233 171.521 197.350 1.00 33.53  ? 564 ILE B CB    1 
ATOM   8327  C  CG1   . ILE B 2 564 ? 142.095 172.295 198.664 1.00 34.00  ? 564 ILE B CG1   1 
ATOM   8328  C  CG2   . ILE B 2 564 ? 143.266 170.414 197.486 1.00 35.20  ? 564 ILE B CG2   1 
ATOM   8329  C  CD1   . ILE B 2 564 ? 141.227 171.612 199.695 1.00 33.87  ? 564 ILE B CD1   1 
ATOM   8330  N  N     . GLY B 2 565 ? 141.860 171.392 194.150 1.00 25.10  ? 565 GLY B N     1 
ATOM   8331  C  CA    . GLY B 2 565 ? 142.076 170.698 192.891 1.00 26.97  ? 565 GLY B CA    1 
ATOM   8332  C  C     . GLY B 2 565 ? 142.922 171.497 191.918 1.00 32.19  ? 565 GLY B C     1 
ATOM   8333  O  O     . GLY B 2 565 ? 143.817 170.954 191.266 1.00 32.91  ? 565 GLY B O     1 
ATOM   8334  N  N     . LYS B 2 566 ? 142.653 172.799 191.809 1.00 31.75  ? 566 LYS B N     1 
ATOM   8335  C  CA    . LYS B 2 566 ? 143.481 173.653 190.966 1.00 27.32  ? 566 LYS B CA    1 
ATOM   8336  C  C     . LYS B 2 566 ? 144.830 173.941 191.614 1.00 26.27  ? 566 LYS B C     1 
ATOM   8337  O  O     . LYS B 2 566 ? 145.831 174.103 190.907 1.00 27.85  ? 566 LYS B O     1 
ATOM   8338  C  CB    . LYS B 2 566 ? 142.749 174.959 190.658 1.00 28.39  ? 566 LYS B CB    1 
ATOM   8339  C  CG    . LYS B 2 566 ? 141.674 174.826 189.594 1.00 32.06  ? 566 LYS B CG    1 
ATOM   8340  C  CD    . LYS B 2 566 ? 141.047 176.171 189.269 1.00 29.19  ? 566 LYS B CD    1 
ATOM   8341  C  CE    . LYS B 2 566 ? 140.273 176.117 187.963 1.00 34.06  ? 566 LYS B CE    1 
ATOM   8342  N  NZ    . LYS B 2 566 ? 141.159 176.315 186.783 1.00 33.34  ? 566 LYS B NZ    1 
ATOM   8343  N  N     . GLN B 2 567 ? 144.875 174.010 192.947 1.00 30.43  ? 567 GLN B N     1 
ATOM   8344  C  CA    . GLN B 2 567 ? 146.133 174.281 193.637 1.00 27.85  ? 567 GLN B CA    1 
ATOM   8345  C  C     . GLN B 2 567 ? 147.155 173.181 193.382 1.00 29.84  ? 567 GLN B C     1 
ATOM   8346  O  O     . GLN B 2 567 ? 148.338 173.463 193.159 1.00 33.66  ? 567 GLN B O     1 
ATOM   8347  C  CB    . GLN B 2 567 ? 145.888 174.439 195.138 1.00 30.31  ? 567 GLN B CB    1 
ATOM   8348  C  CG    . GLN B 2 567 ? 145.606 175.865 195.576 1.00 30.40  ? 567 GLN B CG    1 
ATOM   8349  C  CD    . GLN B 2 567 ? 145.457 175.993 197.079 1.00 37.79  ? 567 GLN B CD    1 
ATOM   8350  O  OE1   . GLN B 2 567 ? 144.946 175.092 197.743 1.00 36.29  ? 567 GLN B OE1   1 
ATOM   8351  N  NE2   . GLN B 2 567 ? 145.904 177.119 197.623 1.00 41.20  ? 567 GLN B NE2   1 
ATOM   8352  N  N     . MET B 2 568 ? 146.720 171.919 193.420 1.00 30.43  ? 568 MET B N     1 
ATOM   8353  C  CA    . MET B 2 568 ? 147.641 170.812 193.178 1.00 30.69  ? 568 MET B CA    1 
ATOM   8354  C  C     . MET B 2 568 ? 148.204 170.861 191.764 1.00 29.26  ? 568 MET B C     1 
ATOM   8355  O  O     . MET B 2 568 ? 149.405 170.653 191.559 1.00 34.84  ? 568 MET B O     1 
ATOM   8356  C  CB    . MET B 2 568 ? 146.938 169.479 193.431 1.00 30.25  ? 568 MET B CB    1 
ATOM   8357  C  CG    . MET B 2 568 ? 146.558 169.241 194.883 1.00 32.15  ? 568 MET B CG    1 
ATOM   8358  S  SD    . MET B 2 568 ? 146.145 167.518 195.218 1.00 47.32  ? 568 MET B SD    1 
ATOM   8359  C  CE    . MET B 2 568 ? 144.557 167.388 194.400 1.00 34.02  ? 568 MET B CE    1 
ATOM   8360  N  N     . LEU B 2 569 ? 147.350 171.131 190.773 1.00 28.21  ? 569 LEU B N     1 
ATOM   8361  C  CA    . LEU B 2 569 ? 147.826 171.253 189.399 1.00 29.01  ? 569 LEU B CA    1 
ATOM   8362  C  C     . LEU B 2 569 ? 148.748 172.456 189.238 1.00 25.70  ? 569 LEU B C     1 
ATOM   8363  O  O     . LEU B 2 569 ? 149.780 172.368 188.563 1.00 23.93  ? 569 LEU B O     1 
ATOM   8364  C  CB    . LEU B 2 569 ? 146.640 171.354 188.441 1.00 29.24  ? 569 LEU B CB    1 
ATOM   8365  C  CG    . LEU B 2 569 ? 146.386 170.159 187.521 1.00 34.66  ? 569 LEU B CG    1 
ATOM   8366  C  CD1   . LEU B 2 569 ? 146.018 168.928 188.330 1.00 28.79  ? 569 LEU B CD1   1 
ATOM   8367  C  CD2   . LEU B 2 569 ? 145.298 170.480 186.508 1.00 30.59  ? 569 LEU B CD2   1 
ATOM   8368  N  N     . MET B 2 570 ? 148.389 173.587 189.848 1.00 24.10  ? 570 MET B N     1 
ATOM   8369  C  CA    . MET B 2 570 ? 149.201 174.793 189.720 1.00 26.56  ? 570 MET B CA    1 
ATOM   8370  C  C     . MET B 2 570 ? 150.553 174.632 190.405 1.00 29.86  ? 570 MET B C     1 
ATOM   8371  O  O     . MET B 2 570 ? 151.575 175.090 189.883 1.00 27.50  ? 570 MET B O     1 
ATOM   8372  C  CB    . MET B 2 570 ? 148.446 175.992 190.292 1.00 26.46  ? 570 MET B CB    1 
ATOM   8373  C  CG    . MET B 2 570 ? 147.338 176.505 189.390 1.00 28.69  ? 570 MET B CG    1 
ATOM   8374  S  SD    . MET B 2 570 ? 146.941 178.235 189.691 1.00 36.12  ? 570 MET B SD    1 
ATOM   8375  C  CE    . MET B 2 570 ? 146.020 178.106 191.221 1.00 33.39  ? 570 MET B CE    1 
ATOM   8376  N  N     . THR B 2 571 ? 150.577 173.991 191.576 1.00 27.87  ? 571 THR B N     1 
ATOM   8377  C  CA    . THR B 2 571 ? 151.841 173.780 192.275 1.00 22.24  ? 571 THR B CA    1 
ATOM   8378  C  C     . THR B 2 571 ? 152.778 172.892 191.468 1.00 25.09  ? 571 THR B C     1 
ATOM   8379  O  O     . THR B 2 571 ? 153.984 173.153 191.396 1.00 27.88  ? 571 THR B O     1 
ATOM   8380  C  CB    . THR B 2 571 ? 151.587 173.173 193.655 1.00 25.55  ? 571 THR B CB    1 
ATOM   8381  O  OG1   . THR B 2 571 ? 150.471 173.828 194.270 1.00 31.21  ? 571 THR B OG1   1 
ATOM   8382  C  CG2   . THR B 2 571 ? 152.814 173.331 194.540 1.00 24.73  ? 571 THR B CG2   1 
ATOM   8383  N  N     . ARG B 2 572 ? 152.242 171.833 190.856 1.00 23.49  ? 572 ARG B N     1 
ATOM   8384  C  CA    . ARG B 2 572 ? 153.071 170.956 190.036 1.00 29.72  ? 572 ARG B CA    1 
ATOM   8385  C  C     . ARG B 2 572 ? 153.608 171.689 188.813 1.00 24.32  ? 572 ARG B C     1 
ATOM   8386  O  O     . ARG B 2 572 ? 154.794 171.574 188.482 1.00 30.17  ? 572 ARG B O     1 
ATOM   8387  C  CB    . ARG B 2 572 ? 152.271 169.724 189.617 1.00 24.18  ? 572 ARG B CB    1 
ATOM   8388  C  CG    . ARG B 2 572 ? 151.956 168.770 190.757 1.00 30.82  ? 572 ARG B CG    1 
ATOM   8389  C  CD    . ARG B 2 572 ? 151.156 167.573 190.269 1.00 26.11  ? 572 ARG B CD    1 
ATOM   8390  N  NE    . ARG B 2 572 ? 150.556 166.833 191.371 1.00 30.98  ? 572 ARG B NE    1 
ATOM   8391  C  CZ    . ARG B 2 572 ? 149.275 166.496 191.438 1.00 34.09  ? 572 ARG B CZ    1 
ATOM   8392  N  NH1   . ARG B 2 572 ? 148.426 166.815 190.475 1.00 30.32  ? 572 ARG B NH1   1 
ATOM   8393  N  NH2   . ARG B 2 572 ? 148.836 165.820 192.496 1.00 30.59  ? 572 ARG B NH2   1 
ATOM   8394  N  N     . GLY B 2 573 ? 152.749 172.446 188.127 1.00 18.57  ? 573 GLY B N     1 
ATOM   8395  C  CA    . GLY B 2 573 ? 153.195 173.176 186.952 1.00 21.64  ? 573 GLY B CA    1 
ATOM   8396  C  C     . GLY B 2 573 ? 154.174 174.288 187.279 1.00 22.99  ? 573 GLY B C     1 
ATOM   8397  O  O     . GLY B 2 573 ? 155.177 174.467 186.584 1.00 29.42  ? 573 GLY B O     1 
ATOM   8398  N  N     . SER B 2 574 ? 153.893 175.056 188.336 1.00 23.54  ? 574 SER B N     1 
ATOM   8399  C  CA    . SER B 2 574 ? 154.773 176.160 188.706 1.00 20.08  ? 574 SER B CA    1 
ATOM   8400  C  C     . SER B 2 574 ? 156.142 175.658 189.147 1.00 25.22  ? 574 SER B C     1 
ATOM   8401  O  O     . SER B 2 574 ? 157.170 176.234 188.773 1.00 28.84  ? 574 SER B O     1 
ATOM   8402  C  CB    . SER B 2 574 ? 154.129 176.998 189.809 1.00 23.26  ? 574 SER B CB    1 
ATOM   8403  O  OG    . SER B 2 574 ? 152.903 177.558 189.373 1.00 35.19  ? 574 SER B OG    1 
ATOM   8404  N  N     . LEU B 2 575 ? 156.176 174.590 189.946 1.00 27.56  ? 575 LEU B N     1 
ATOM   8405  C  CA    . LEU B 2 575 ? 157.453 174.050 190.400 1.00 21.22  ? 575 LEU B CA    1 
ATOM   8406  C  C     . LEU B 2 575 ? 158.235 173.421 189.255 1.00 22.73  ? 575 LEU B C     1 
ATOM   8407  O  O     . LEU B 2 575 ? 159.469 173.490 189.239 1.00 30.36  ? 575 LEU B O     1 
ATOM   8408  C  CB    . LEU B 2 575 ? 157.226 173.032 191.518 1.00 25.75  ? 575 LEU B CB    1 
ATOM   8409  C  CG    . LEU B 2 575 ? 156.904 173.615 192.897 1.00 24.50  ? 575 LEU B CG    1 
ATOM   8410  C  CD1   . LEU B 2 575 ? 157.038 172.554 193.976 1.00 26.88  ? 575 LEU B CD1   1 
ATOM   8411  C  CD2   . LEU B 2 575 ? 157.795 174.809 193.202 1.00 23.52  ? 575 LEU B CD2   1 
ATOM   8412  N  N     . THR B 2 576 ? 157.542 172.799 188.297 1.00 21.94  ? 576 THR B N     1 
ATOM   8413  C  CA    . THR B 2 576 ? 158.225 172.251 187.130 1.00 21.78  ? 576 THR B CA    1 
ATOM   8414  C  C     . THR B 2 576 ? 158.872 173.357 186.305 1.00 25.69  ? 576 THR B C     1 
ATOM   8415  O  O     . THR B 2 576 ? 160.028 173.232 185.883 1.00 26.04  ? 576 THR B O     1 
ATOM   8416  C  CB    . THR B 2 576 ? 157.245 171.447 186.274 1.00 22.25  ? 576 THR B CB    1 
ATOM   8417  O  OG1   . THR B 2 576 ? 156.742 170.340 187.033 1.00 26.58  ? 576 THR B OG1   1 
ATOM   8418  C  CG2   . THR B 2 576 ? 157.933 170.924 185.023 1.00 17.86  ? 576 THR B CG2   1 
ATOM   8419  N  N     . THR B 2 577 ? 158.144 174.452 186.073 1.00 24.81  ? 577 THR B N     1 
ATOM   8420  C  CA    . THR B 2 577 ? 158.716 175.589 185.360 1.00 18.82  ? 577 THR B CA    1 
ATOM   8421  C  C     . THR B 2 577 ? 159.855 176.215 186.155 1.00 23.42  ? 577 THR B C     1 
ATOM   8422  O  O     . THR B 2 577 ? 160.867 176.637 185.582 1.00 28.55  ? 577 THR B O     1 
ATOM   8423  C  CB    . THR B 2 577 ? 157.628 176.624 185.068 1.00 24.44  ? 577 THR B CB    1 
ATOM   8424  O  OG1   . THR B 2 577 ? 156.589 176.020 184.288 1.00 33.90  ? 577 THR B OG1   1 
ATOM   8425  C  CG2   . THR B 2 577 ? 158.200 177.808 184.302 1.00 26.28  ? 577 THR B CG2   1 
ATOM   8426  N  N     . PHE B 2 578 ? 159.706 176.279 187.480 1.00 22.42  ? 578 PHE B N     1 
ATOM   8427  C  CA    . PHE B 2 578 ? 160.761 176.825 188.327 1.00 25.89  ? 578 PHE B CA    1 
ATOM   8428  C  C     . PHE B 2 578 ? 162.035 175.994 188.231 1.00 24.85  ? 578 PHE B C     1 
ATOM   8429  O  O     . PHE B 2 578 ? 163.139 176.545 188.139 1.00 23.97  ? 578 PHE B O     1 
ATOM   8430  C  CB    . PHE B 2 578 ? 160.273 176.897 189.774 1.00 17.76  ? 578 PHE B CB    1 
ATOM   8431  C  CG    . PHE B 2 578 ? 161.213 177.612 190.701 1.00 25.68  ? 578 PHE B CG    1 
ATOM   8432  C  CD1   . PHE B 2 578 ? 161.264 178.995 190.726 1.00 30.94  ? 578 PHE B CD1   1 
ATOM   8433  C  CD2   . PHE B 2 578 ? 162.040 176.900 191.554 1.00 24.29  ? 578 PHE B CD2   1 
ATOM   8434  C  CE1   . PHE B 2 578 ? 162.124 179.655 191.582 1.00 28.31  ? 578 PHE B CE1   1 
ATOM   8435  C  CE2   . PHE B 2 578 ? 162.903 177.555 192.411 1.00 26.33  ? 578 PHE B CE2   1 
ATOM   8436  C  CZ    . PHE B 2 578 ? 162.945 178.934 192.425 1.00 26.76  ? 578 PHE B CZ    1 
ATOM   8437  N  N     . SER B 2 579 ? 161.903 174.665 188.249 1.00 23.67  ? 579 SER B N     1 
ATOM   8438  C  CA    . SER B 2 579 ? 163.078 173.799 188.215 1.00 24.03  ? 579 SER B CA    1 
ATOM   8439  C  C     . SER B 2 579 ? 163.818 173.909 186.887 1.00 26.29  ? 579 SER B C     1 
ATOM   8440  O  O     . SER B 2 579 ? 165.052 173.981 186.863 1.00 29.85  ? 579 SER B O     1 
ATOM   8441  C  CB    . SER B 2 579 ? 162.671 172.350 188.481 1.00 17.54  ? 579 SER B CB    1 
ATOM   8442  O  OG    . SER B 2 579 ? 161.683 172.273 189.493 1.00 32.89  ? 579 SER B OG    1 
ATOM   8443  N  N     . ILE B 2 580 ? 163.084 173.910 185.772 1.00 23.96  ? 580 ILE B N     1 
ATOM   8444  C  CA    . ILE B 2 580 ? 163.723 173.992 184.462 1.00 26.48  ? 580 ILE B CA    1 
ATOM   8445  C  C     . ILE B 2 580 ? 164.410 175.339 184.281 1.00 28.13  ? 580 ILE B C     1 
ATOM   8446  O  O     . ILE B 2 580 ? 165.540 175.413 183.784 1.00 32.74  ? 580 ILE B O     1 
ATOM   8447  C  CB    . ILE B 2 580 ? 162.694 173.724 183.349 1.00 23.83  ? 580 ILE B CB    1 
ATOM   8448  C  CG1   . ILE B 2 580 ? 162.058 172.346 183.535 1.00 27.76  ? 580 ILE B CG1   1 
ATOM   8449  C  CG2   . ILE B 2 580 ? 163.348 173.826 181.981 1.00 27.41  ? 580 ILE B CG2   1 
ATOM   8450  C  CD1   . ILE B 2 580 ? 160.733 172.184 182.827 1.00 31.77  ? 580 ILE B CD1   1 
ATOM   8451  N  N     . ALA B 2 581 ? 163.745 176.426 184.682 1.00 26.27  ? 581 ALA B N     1 
ATOM   8452  C  CA    . ALA B 2 581 ? 164.346 177.749 184.572 1.00 24.89  ? 581 ALA B CA    1 
ATOM   8453  C  C     . ALA B 2 581 ? 165.539 177.923 185.503 1.00 26.90  ? 581 ALA B C     1 
ATOM   8454  O  O     . ALA B 2 581 ? 166.351 178.828 185.286 1.00 29.86  ? 581 ALA B O     1 
ATOM   8455  C  CB    . ALA B 2 581 ? 163.301 178.828 184.859 1.00 21.01  ? 581 ALA B CB    1 
ATOM   8456  N  N     . ASN B 2 582 ? 165.665 177.076 186.527 1.00 23.38  ? 582 ASN B N     1 
ATOM   8457  C  CA    . ASN B 2 582 ? 166.797 177.165 187.441 1.00 21.68  ? 582 ASN B CA    1 
ATOM   8458  C  C     . ASN B 2 582 ? 168.098 176.700 186.799 1.00 27.91  ? 582 ASN B C     1 
ATOM   8459  O  O     . ASN B 2 582 ? 169.174 176.985 187.335 1.00 35.18  ? 582 ASN B O     1 
ATOM   8460  C  CB    . ASN B 2 582 ? 166.521 176.338 188.699 1.00 22.37  ? 582 ASN B CB    1 
ATOM   8461  C  CG    . ASN B 2 582 ? 165.749 177.110 189.753 1.00 28.68  ? 582 ASN B CG    1 
ATOM   8462  O  OD1   . ASN B 2 582 ? 165.243 178.201 189.496 1.00 33.80  ? 582 ASN B OD1   1 
ATOM   8463  N  ND2   . ASN B 2 582 ? 165.656 176.543 190.949 1.00 34.23  ? 582 ASN B ND2   1 
ATOM   8464  N  N     . ASP B 2 583 ? 168.024 175.996 185.667 1.00 20.95  ? 583 ASP B N     1 
ATOM   8465  C  CA    . ASP B 2 583 ? 169.220 175.442 185.042 1.00 22.01  ? 583 ASP B CA    1 
ATOM   8466  C  C     . ASP B 2 583 ? 170.065 176.498 184.342 1.00 27.02  ? 583 ASP B C     1 
ATOM   8467  O  O     . ASP B 2 583 ? 171.245 176.246 184.075 1.00 34.51  ? 583 ASP B O     1 
ATOM   8468  C  CB    . ASP B 2 583 ? 168.833 174.356 184.038 1.00 24.66  ? 583 ASP B CB    1 
ATOM   8469  C  CG    . ASP B 2 583 ? 168.323 173.096 184.707 1.00 28.33  ? 583 ASP B CG    1 
ATOM   8470  O  OD1   . ASP B 2 583 ? 168.335 173.033 185.954 1.00 30.20  ? 583 ASP B OD1   1 
ATOM   8471  O  OD2   . ASP B 2 583 ? 167.909 172.170 183.981 1.00 28.51  ? 583 ASP B OD2   1 
ATOM   8472  N  N     . VAL B 2 584 ? 169.492 177.662 184.030 1.00 28.16  ? 584 VAL B N     1 
ATOM   8473  C  CA    . VAL B 2 584 ? 170.237 178.688 183.303 1.00 25.08  ? 584 VAL B CA    1 
ATOM   8474  C  C     . VAL B 2 584 ? 171.407 179.191 184.140 1.00 23.16  ? 584 VAL B C     1 
ATOM   8475  O  O     . VAL B 2 584 ? 172.532 179.336 183.646 1.00 26.73  ? 584 VAL B O     1 
ATOM   8476  C  CB    . VAL B 2 584 ? 169.301 179.836 182.886 1.00 26.75  ? 584 VAL B CB    1 
ATOM   8477  C  CG1   . VAL B 2 584 ? 170.106 181.028 182.390 1.00 26.22  ? 584 VAL B CG1   1 
ATOM   8478  C  CG2   . VAL B 2 584 ? 168.330 179.363 181.816 1.00 27.21  ? 584 VAL B CG2   1 
ATOM   8479  N  N     . ALA B 2 585 ? 171.163 179.457 185.425 1.00 23.45  ? 585 ALA B N     1 
ATOM   8480  C  CA    . ALA B 2 585 ? 172.239 179.921 186.293 1.00 23.80  ? 585 ALA B CA    1 
ATOM   8481  C  C     . ALA B 2 585 ? 173.201 178.795 186.651 1.00 24.94  ? 585 ALA B C     1 
ATOM   8482  O  O     . ALA B 2 585 ? 174.377 179.055 186.930 1.00 29.38  ? 585 ALA B O     1 
ATOM   8483  C  CB    . ALA B 2 585 ? 171.663 180.550 187.560 1.00 20.33  ? 585 ALA B CB    1 
ATOM   8484  N  N     . LYS B 2 586 ? 172.725 177.548 186.653 1.00 22.96  ? 586 LYS B N     1 
ATOM   8485  C  CA    . LYS B 2 586 ? 173.614 176.419 186.912 1.00 24.80  ? 586 LYS B CA    1 
ATOM   8486  C  C     . LYS B 2 586 ? 174.661 176.284 185.814 1.00 30.72  ? 586 LYS B C     1 
ATOM   8487  O  O     . LYS B 2 586 ? 175.815 175.932 186.086 1.00 28.91  ? 586 LYS B O     1 
ATOM   8488  C  CB    . LYS B 2 586 ? 172.805 175.129 187.041 1.00 27.60  ? 586 LYS B CB    1 
ATOM   8489  C  CG    . LYS B 2 586 ? 171.768 175.147 188.151 1.00 27.09  ? 586 LYS B CG    1 
ATOM   8490  C  CD    . LYS B 2 586 ? 172.422 175.065 189.520 1.00 27.98  ? 586 LYS B CD    1 
ATOM   8491  C  CE    . LYS B 2 586 ? 171.414 175.313 190.628 1.00 31.79  ? 586 LYS B CE    1 
ATOM   8492  N  NZ    . LYS B 2 586 ? 170.091 174.703 190.319 1.00 29.83  ? 586 LYS B NZ    1 
ATOM   8493  N  N     . TYR B 2 587 ? 174.274 176.553 184.565 1.00 26.10  ? 587 TYR B N     1 
ATOM   8494  C  CA    . TYR B 2 587 ? 175.231 176.491 183.465 1.00 24.71  ? 587 TYR B CA    1 
ATOM   8495  C  C     . TYR B 2 587 ? 176.264 177.605 183.569 1.00 22.02  ? 587 TYR B C     1 
ATOM   8496  O  O     . TYR B 2 587 ? 177.446 177.397 183.274 1.00 24.58  ? 587 TYR B O     1 
ATOM   8497  C  CB    . TYR B 2 587 ? 174.495 176.565 182.128 1.00 22.11  ? 587 TYR B CB    1 
ATOM   8498  C  CG    . TYR B 2 587 ? 174.089 175.218 181.576 1.00 23.67  ? 587 TYR B CG    1 
ATOM   8499  C  CD1   . TYR B 2 587 ? 174.875 174.093 181.786 1.00 25.83  ? 587 TYR B CD1   1 
ATOM   8500  C  CD2   . TYR B 2 587 ? 172.918 175.071 180.846 1.00 20.87  ? 587 TYR B CD2   1 
ATOM   8501  C  CE1   . TYR B 2 587 ? 174.507 172.860 181.283 1.00 23.43  ? 587 TYR B CE1   1 
ATOM   8502  C  CE2   . TYR B 2 587 ? 172.542 173.843 180.339 1.00 20.56  ? 587 TYR B CE2   1 
ATOM   8503  C  CZ    . TYR B 2 587 ? 173.339 172.742 180.560 1.00 20.78  ? 587 TYR B CZ    1 
ATOM   8504  O  OH    . TYR B 2 587 ? 172.965 171.518 180.055 1.00 26.14  ? 587 TYR B OH    1 
ATOM   8505  N  N     . PHE B 2 588 ? 175.837 178.798 183.991 1.00 16.21  ? 588 PHE B N     1 
ATOM   8506  C  CA    . PHE B 2 588 ? 176.762 179.918 184.115 1.00 23.40  ? 588 PHE B CA    1 
ATOM   8507  C  C     . PHE B 2 588 ? 177.700 179.769 185.304 1.00 20.60  ? 588 PHE B C     1 
ATOM   8508  O  O     . PHE B 2 588 ? 178.695 180.496 185.387 1.00 32.42  ? 588 PHE B O     1 
ATOM   8509  C  CB    . PHE B 2 588 ? 175.985 181.231 184.228 1.00 25.35  ? 588 PHE B CB    1 
ATOM   8510  C  CG    . PHE B 2 588 ? 175.625 181.838 182.903 1.00 32.34  ? 588 PHE B CG    1 
ATOM   8511  C  CD1   . PHE B 2 588 ? 176.606 182.369 182.081 1.00 27.01  ? 588 PHE B CD1   1 
ATOM   8512  C  CD2   . PHE B 2 588 ? 174.308 181.878 182.478 1.00 28.15  ? 588 PHE B CD2   1 
ATOM   8513  C  CE1   . PHE B 2 588 ? 176.279 182.929 180.861 1.00 24.23  ? 588 PHE B CE1   1 
ATOM   8514  C  CE2   . PHE B 2 588 ? 173.974 182.437 181.259 1.00 24.82  ? 588 PHE B CE2   1 
ATOM   8515  C  CZ    . PHE B 2 588 ? 174.962 182.963 180.450 1.00 26.49  ? 588 PHE B CZ    1 
ATOM   8516  N  N     . ALA B 2 589 ? 177.412 178.847 186.221 1.00 23.25  ? 589 ALA B N     1 
ATOM   8517  C  CA    . ALA B 2 589 ? 178.236 178.654 187.407 1.00 22.39  ? 589 ALA B CA    1 
ATOM   8518  C  C     . ALA B 2 589 ? 179.148 177.440 187.322 1.00 28.15  ? 589 ALA B C     1 
ATOM   8519  O  O     . ALA B 2 589 ? 180.214 177.439 187.945 1.00 34.30  ? 589 ALA B O     1 
ATOM   8520  C  CB    . ALA B 2 589 ? 177.351 178.523 188.651 1.00 22.87  ? 589 ALA B CB    1 
ATOM   8521  N  N     . ILE B 2 590 ? 178.767 176.415 186.566 1.00 24.05  ? 590 ILE B N     1 
ATOM   8522  C  CA    . ILE B 2 590 ? 179.516 175.168 186.516 1.00 26.55  ? 590 ILE B CA    1 
ATOM   8523  C  C     . ILE B 2 590 ? 180.353 175.058 185.247 1.00 26.57  ? 590 ILE B C     1 
ATOM   8524  O  O     . ILE B 2 590 ? 181.505 174.629 185.303 1.00 31.42  ? 590 ILE B O     1 
ATOM   8525  C  CB    . ILE B 2 590 ? 178.560 173.964 186.660 1.00 26.91  ? 590 ILE B CB    1 
ATOM   8526  C  CG1   . ILE B 2 590 ? 177.804 174.043 187.988 1.00 29.98  ? 590 ILE B CG1   1 
ATOM   8527  C  CG2   . ILE B 2 590 ? 179.330 172.656 186.566 1.00 24.93  ? 590 ILE B CG2   1 
ATOM   8528  C  CD1   . ILE B 2 590 ? 176.700 173.019 188.127 1.00 24.21  ? 590 ILE B CD1   1 
ATOM   8529  N  N     . ILE B 2 591 ? 179.790 175.438 184.096 1.00 21.36  ? 591 ILE B N     1 
ATOM   8530  C  CA    . ILE B 2 591 ? 180.519 175.297 182.832 1.00 26.40  ? 591 ILE B CA    1 
ATOM   8531  C  C     . ILE B 2 591 ? 181.831 176.075 182.833 1.00 27.39  ? 591 ILE B C     1 
ATOM   8532  O  O     . ILE B 2 591 ? 182.865 175.496 182.462 1.00 28.88  ? 591 ILE B O     1 
ATOM   8533  C  CB    . ILE B 2 591 ? 179.607 175.668 181.649 1.00 22.79  ? 591 ILE B CB    1 
ATOM   8534  C  CG1   . ILE B 2 591 ? 178.489 174.636 181.487 1.00 24.96  ? 591 ILE B CG1   1 
ATOM   8535  C  CG2   . ILE B 2 591 ? 180.415 175.787 180.366 1.00 24.35  ? 591 ILE B CG2   1 
ATOM   8536  C  CD1   . ILE B 2 591 ? 178.979 173.207 181.401 1.00 28.00  ? 591 ILE B CD1   1 
ATOM   8537  N  N     . PRO B 2 592 ? 181.876 177.358 183.219 1.00 31.61  ? 592 PRO B N     1 
ATOM   8538  C  CA    . PRO B 2 592 ? 183.187 178.020 183.330 1.00 24.44  ? 592 PRO B CA    1 
ATOM   8539  C  C     . PRO B 2 592 ? 184.104 177.364 184.346 1.00 25.25  ? 592 PRO B C     1 
ATOM   8540  O  O     . PRO B 2 592 ? 185.324 177.330 184.139 1.00 28.73  ? 592 PRO B O     1 
ATOM   8541  C  CB    . PRO B 2 592 ? 182.825 179.455 183.740 1.00 20.92  ? 592 PRO B CB    1 
ATOM   8542  C  CG    . PRO B 2 592 ? 181.417 179.633 183.307 1.00 25.27  ? 592 PRO B CG    1 
ATOM   8543  C  CD    . PRO B 2 592 ? 180.775 178.299 183.496 1.00 24.56  ? 592 PRO B CD    1 
ATOM   8544  N  N     . ALA B 2 593 ? 183.551 176.841 185.442 1.00 24.08  ? 593 ALA B N     1 
ATOM   8545  C  CA    . ALA B 2 593 ? 184.369 176.204 186.467 1.00 23.55  ? 593 ALA B CA    1 
ATOM   8546  C  C     . ALA B 2 593 ? 184.859 174.829 186.031 1.00 23.44  ? 593 ALA B C     1 
ATOM   8547  O  O     . ALA B 2 593 ? 185.992 174.445 186.342 1.00 32.10  ? 593 ALA B O     1 
ATOM   8548  C  CB    . ALA B 2 593 ? 183.579 176.095 187.771 1.00 25.53  ? 593 ALA B CB    1 
ATOM   8549  N  N     . ALA B 2 594 ? 184.019 174.074 185.319 1.00 19.81  ? 594 ALA B N     1 
ATOM   8550  C  CA    . ALA B 2 594 ? 184.380 172.711 184.939 1.00 26.68  ? 594 ALA B CA    1 
ATOM   8551  C  C     . ALA B 2 594 ? 185.584 172.690 184.006 1.00 28.36  ? 594 ALA B C     1 
ATOM   8552  O  O     . ALA B 2 594 ? 186.468 171.836 184.141 1.00 29.98  ? 594 ALA B O     1 
ATOM   8553  C  CB    . ALA B 2 594 ? 183.186 172.014 184.289 1.00 23.81  ? 594 ALA B CB    1 
ATOM   8554  N  N     . PHE B 2 595 ? 185.636 173.618 183.055 1.00 27.13  ? 595 PHE B N     1 
ATOM   8555  C  CA    . PHE B 2 595 ? 186.695 173.671 182.053 1.00 28.13  ? 595 PHE B CA    1 
ATOM   8556  C  C     . PHE B 2 595 ? 187.613 174.871 182.270 1.00 32.31  ? 595 PHE B C     1 
ATOM   8557  O  O     . PHE B 2 595 ? 188.055 175.514 181.317 1.00 41.43  ? 595 PHE B O     1 
ATOM   8558  C  CB    . PHE B 2 595 ? 186.103 173.696 180.648 1.00 27.22  ? 595 PHE B CB    1 
ATOM   8559  C  CG    . PHE B 2 595 ? 184.968 172.733 180.455 1.00 28.91  ? 595 PHE B CG    1 
ATOM   8560  C  CD1   . PHE B 2 595 ? 185.207 171.373 180.359 1.00 29.82  ? 595 PHE B CD1   1 
ATOM   8561  C  CD2   . PHE B 2 595 ? 183.663 173.186 180.377 1.00 28.27  ? 595 PHE B CD2   1 
ATOM   8562  C  CE1   . PHE B 2 595 ? 184.166 170.483 180.184 1.00 33.08  ? 595 PHE B CE1   1 
ATOM   8563  C  CE2   . PHE B 2 595 ? 182.618 172.301 180.202 1.00 32.55  ? 595 PHE B CE2   1 
ATOM   8564  C  CZ    . PHE B 2 595 ? 182.870 170.948 180.106 1.00 30.99  ? 595 PHE B CZ    1 
ATOM   8565  N  N     . ALA B 2 596 ? 187.906 175.184 183.534 1.00 34.53  ? 596 ALA B N     1 
ATOM   8566  C  CA    . ALA B 2 596 ? 188.802 176.296 183.829 1.00 33.72  ? 596 ALA B CA    1 
ATOM   8567  C  C     . ALA B 2 596 ? 190.225 176.015 183.364 1.00 37.31  ? 596 ALA B C     1 
ATOM   8568  O  O     . ALA B 2 596 ? 190.963 176.949 183.034 1.00 38.28  ? 596 ALA B O     1 
ATOM   8569  C  CB    . ALA B 2 596 ? 188.786 176.603 185.326 1.00 31.15  ? 596 ALA B CB    1 
ATOM   8570  N  N     . ALA B 2 597 ? 190.626 174.744 183.330 1.00 39.12  ? 597 ALA B N     1 
ATOM   8571  C  CA    . ALA B 2 597 ? 191.971 174.379 182.905 1.00 39.81  ? 597 ALA B CA    1 
ATOM   8572  C  C     . ALA B 2 597 ? 192.011 173.884 181.464 1.00 40.71  ? 597 ALA B C     1 
ATOM   8573  O  O     . ALA B 2 597 ? 193.001 174.110 180.761 1.00 44.62  ? 597 ALA B O     1 
ATOM   8574  C  CB    . ALA B 2 597 ? 192.545 173.310 183.837 1.00 36.32  ? 597 ALA B CB    1 
ATOM   8575  N  N     . THR B 2 598 ? 190.953 173.211 181.009 1.00 37.44  ? 598 THR B N     1 
ATOM   8576  C  CA    . THR B 2 598 ? 190.934 172.699 179.643 1.00 38.07  ? 598 THR B CA    1 
ATOM   8577  C  C     . THR B 2 598 ? 190.700 173.821 178.639 1.00 39.64  ? 598 THR B C     1 
ATOM   8578  O  O     . THR B 2 598 ? 191.181 173.763 177.502 1.00 44.38  ? 598 THR B O     1 
ATOM   8579  C  CB    . THR B 2 598 ? 189.860 171.621 179.499 1.00 41.84  ? 598 THR B CB    1 
ATOM   8580  O  OG1   . THR B 2 598 ? 188.615 172.230 179.137 1.00 42.51  ? 598 THR B OG1   1 
ATOM   8581  C  CG2   . THR B 2 598 ? 189.682 170.872 180.809 1.00 41.46  ? 598 THR B CG2   1 
ATOM   8582  N  N     . TYR B 2 599 ? 189.966 174.855 179.045 1.00 31.04  ? 599 TYR B N     1 
ATOM   8583  C  CA    . TYR B 2 599 ? 189.643 175.994 178.187 1.00 29.40  ? 599 TYR B CA    1 
ATOM   8584  C  C     . TYR B 2 599 ? 189.560 177.240 179.057 1.00 35.86  ? 599 TYR B C     1 
ATOM   8585  O  O     . TYR B 2 599 ? 188.471 177.636 179.495 1.00 34.87  ? 599 TYR B O     1 
ATOM   8586  C  CB    . TYR B 2 599 ? 188.339 175.764 177.423 1.00 32.07  ? 599 TYR B CB    1 
ATOM   8587  C  CG    . TYR B 2 599 ? 188.496 174.940 176.166 1.00 33.44  ? 599 TYR B CG    1 
ATOM   8588  C  CD1   . TYR B 2 599 ? 189.416 175.297 175.188 1.00 34.92  ? 599 TYR B CD1   1 
ATOM   8589  C  CD2   . TYR B 2 599 ? 187.723 173.807 175.954 1.00 31.87  ? 599 TYR B CD2   1 
ATOM   8590  C  CE1   . TYR B 2 599 ? 189.563 174.547 174.038 1.00 33.70  ? 599 TYR B CE1   1 
ATOM   8591  C  CE2   . TYR B 2 599 ? 187.862 173.051 174.807 1.00 30.59  ? 599 TYR B CE2   1 
ATOM   8592  C  CZ    . TYR B 2 599 ? 188.783 173.425 173.852 1.00 38.14  ? 599 TYR B CZ    1 
ATOM   8593  O  OH    . TYR B 2 599 ? 188.925 172.675 172.707 1.00 41.41  ? 599 TYR B OH    1 
ATOM   8594  N  N     . PRO B 2 600 ? 190.697 177.884 179.332 1.00 34.36  ? 600 PRO B N     1 
ATOM   8595  C  CA    . PRO B 2 600 ? 190.675 179.086 180.181 1.00 29.48  ? 600 PRO B CA    1 
ATOM   8596  C  C     . PRO B 2 600 ? 189.878 180.237 179.593 1.00 29.87  ? 600 PRO B C     1 
ATOM   8597  O  O     . PRO B 2 600 ? 189.438 181.112 180.348 1.00 32.76  ? 600 PRO B O     1 
ATOM   8598  C  CB    . PRO B 2 600 ? 192.162 179.449 180.322 1.00 30.11  ? 600 PRO B CB    1 
ATOM   8599  C  CG    . PRO B 2 600 ? 192.916 178.228 179.878 1.00 31.89  ? 600 PRO B CG    1 
ATOM   8600  C  CD    . PRO B 2 600 ? 192.053 177.560 178.863 1.00 33.79  ? 600 PRO B CD    1 
ATOM   8601  N  N     . GLN B 2 601 ? 189.680 180.267 178.273 1.00 33.30  ? 601 GLN B N     1 
ATOM   8602  C  CA    . GLN B 2 601 ? 188.906 181.338 177.655 1.00 22.83  ? 601 GLN B CA    1 
ATOM   8603  C  C     . GLN B 2 601 ? 187.437 181.302 178.055 1.00 30.12  ? 601 GLN B C     1 
ATOM   8604  O  O     . GLN B 2 601 ? 186.744 182.313 177.906 1.00 38.68  ? 601 GLN B O     1 
ATOM   8605  C  CB    . GLN B 2 601 ? 189.030 181.266 176.132 1.00 25.71  ? 601 GLN B CB    1 
ATOM   8606  C  CG    . GLN B 2 601 ? 188.317 180.076 175.510 1.00 22.56  ? 601 GLN B CG    1 
ATOM   8607  C  CD    . GLN B 2 601 ? 189.264 178.943 175.171 1.00 27.37  ? 601 GLN B CD    1 
ATOM   8608  O  OE1   . GLN B 2 601 ? 189.942 178.404 176.045 1.00 34.50  ? 601 GLN B OE1   1 
ATOM   8609  N  NE2   . GLN B 2 601 ? 189.309 178.568 173.899 1.00 29.97  ? 601 GLN B NE2   1 
ATOM   8610  N  N     . LEU B 2 602 ? 186.948 180.168 178.562 1.00 20.13  ? 602 LEU B N     1 
ATOM   8611  C  CA    . LEU B 2 602 ? 185.548 180.056 178.949 1.00 24.59  ? 602 LEU B CA    1 
ATOM   8612  C  C     . LEU B 2 602 ? 185.236 180.781 180.252 1.00 27.81  ? 602 LEU B C     1 
ATOM   8613  O  O     . LEU B 2 602 ? 184.061 180.869 180.623 1.00 31.17  ? 602 LEU B O     1 
ATOM   8614  C  CB    . LEU B 2 602 ? 185.150 178.584 179.072 1.00 29.36  ? 602 LEU B CB    1 
ATOM   8615  C  CG    . LEU B 2 602 ? 184.904 177.842 177.756 1.00 27.68  ? 602 LEU B CG    1 
ATOM   8616  C  CD1   . LEU B 2 602 ? 184.794 176.343 177.996 1.00 26.02  ? 602 LEU B CD1   1 
ATOM   8617  C  CD2   . LEU B 2 602 ? 183.672 178.372 177.044 1.00 26.04  ? 602 LEU B CD2   1 
ATOM   8618  N  N     . ASN B 2 603 ? 186.251 181.296 180.951 1.00 27.81  ? 603 ASN B N     1 
ATOM   8619  C  CA    . ASN B 2 603 ? 186.017 182.027 182.190 1.00 24.85  ? 603 ASN B CA    1 
ATOM   8620  C  C     . ASN B 2 603 ? 185.261 183.330 181.961 1.00 28.32  ? 603 ASN B C     1 
ATOM   8621  O  O     . ASN B 2 603 ? 184.747 183.911 182.922 1.00 34.07  ? 603 ASN B O     1 
ATOM   8622  C  CB    . ASN B 2 603 ? 187.350 182.309 182.889 1.00 26.42  ? 603 ASN B CB    1 
ATOM   8623  C  CG    . ASN B 2 603 ? 187.170 182.887 184.280 1.00 36.76  ? 603 ASN B CG    1 
ATOM   8624  O  OD1   . ASN B 2 603 ? 187.569 184.019 184.551 1.00 38.69  ? 603 ASN B OD1   1 
ATOM   8625  N  ND2   . ASN B 2 603 ? 186.563 182.109 185.170 1.00 36.19  ? 603 ASN B ND2   1 
ATOM   8626  N  N     . ALA B 2 604 ? 185.176 183.797 180.713 1.00 27.00  ? 604 ALA B N     1 
ATOM   8627  C  CA    . ALA B 2 604 ? 184.415 185.004 180.414 1.00 24.79  ? 604 ALA B CA    1 
ATOM   8628  C  C     . ALA B 2 604 ? 182.924 184.830 180.676 1.00 28.77  ? 604 ALA B C     1 
ATOM   8629  O  O     . ALA B 2 604 ? 182.207 185.831 180.781 1.00 26.76  ? 604 ALA B O     1 
ATOM   8630  C  CB    . ALA B 2 604 ? 184.641 185.423 178.961 1.00 25.29  ? 604 ALA B CB    1 
ATOM   8631  N  N     . LEU B 2 605 ? 182.444 183.593 180.783 1.00 30.55  ? 605 LEU B N     1 
ATOM   8632  C  CA    . LEU B 2 605 ? 181.048 183.321 181.098 1.00 26.58  ? 605 LEU B CA    1 
ATOM   8633  C  C     . LEU B 2 605 ? 180.768 183.329 182.595 1.00 29.33  ? 605 LEU B C     1 
ATOM   8634  O  O     . LEU B 2 605 ? 179.616 183.132 182.995 1.00 36.96  ? 605 LEU B O     1 
ATOM   8635  C  CB    . LEU B 2 605 ? 180.621 181.976 180.503 1.00 28.75  ? 605 LEU B CB    1 
ATOM   8636  C  CG    . LEU B 2 605 ? 181.006 181.716 179.046 1.00 34.19  ? 605 LEU B CG    1 
ATOM   8637  C  CD1   . LEU B 2 605 ? 181.071 180.224 178.775 1.00 32.52  ? 605 LEU B CD1   1 
ATOM   8638  C  CD2   . LEU B 2 605 ? 180.030 182.396 178.100 1.00 27.00  ? 605 LEU B CD2   1 
ATOM   8639  N  N     . ASN B 2 606 ? 181.786 183.547 183.428 1.00 25.00  ? 606 ASN B N     1 
ATOM   8640  C  CA    . ASN B 2 606 ? 181.608 183.650 184.877 1.00 29.49  ? 606 ASN B CA    1 
ATOM   8641  C  C     . ASN B 2 606 ? 181.036 185.030 185.210 1.00 30.55  ? 606 ASN B C     1 
ATOM   8642  O  O     . ASN B 2 606 ? 181.690 185.899 185.790 1.00 35.30  ? 606 ASN B O     1 
ATOM   8643  C  CB    . ASN B 2 606 ? 182.926 183.397 185.595 1.00 28.12  ? 606 ASN B CB    1 
ATOM   8644  C  CG    . ASN B 2 606 ? 182.749 183.171 187.084 1.00 31.83  ? 606 ASN B CG    1 
ATOM   8645  O  OD1   . ASN B 2 606 ? 181.635 182.966 187.565 1.00 42.40  ? 606 ASN B OD1   1 
ATOM   8646  N  ND2   . ASN B 2 606 ? 183.851 183.209 187.822 1.00 23.76  ? 606 ASN B ND2   1 
ATOM   8647  N  N     . ILE B 2 607 ? 179.773 185.220 184.820 1.00 28.47  ? 607 ILE B N     1 
ATOM   8648  C  CA    . ILE B 2 607 ? 179.124 186.516 184.990 1.00 31.33  ? 607 ILE B CA    1 
ATOM   8649  C  C     . ILE B 2 607 ? 178.892 186.816 186.466 1.00 29.79  ? 607 ILE B C     1 
ATOM   8650  O  O     . ILE B 2 607 ? 178.881 187.981 186.881 1.00 38.80  ? 607 ILE B O     1 
ATOM   8651  C  CB    . ILE B 2 607 ? 177.812 186.567 184.186 1.00 34.51  ? 607 ILE B CB    1 
ATOM   8652  C  CG1   . ILE B 2 607 ? 176.957 185.332 184.474 1.00 32.38  ? 607 ILE B CG1   1 
ATOM   8653  C  CG2   . ILE B 2 607 ? 178.106 186.678 182.698 1.00 33.80  ? 607 ILE B CG2   1 
ATOM   8654  C  CD1   . ILE B 2 607 ? 175.561 185.416 183.904 1.00 31.46  ? 607 ILE B CD1   1 
ATOM   8655  N  N     . MET B 2 608 ? 178.704 185.777 187.282 1.00 30.51  ? 608 MET B N     1 
ATOM   8656  C  CA    . MET B 2 608 ? 178.512 185.977 188.713 1.00 28.78  ? 608 MET B CA    1 
ATOM   8657  C  C     . MET B 2 608 ? 179.815 186.249 189.450 1.00 33.40  ? 608 MET B C     1 
ATOM   8658  O  O     . MET B 2 608 ? 179.773 186.541 190.650 1.00 35.55  ? 608 MET B O     1 
ATOM   8659  C  CB    . MET B 2 608 ? 177.816 184.761 189.328 1.00 27.76  ? 608 MET B CB    1 
ATOM   8660  C  CG    . MET B 2 608 ? 176.411 184.521 188.805 1.00 32.33  ? 608 MET B CG    1 
ATOM   8661  S  SD    . MET B 2 608 ? 175.542 183.233 189.719 1.00 45.87  ? 608 MET B SD    1 
ATOM   8662  C  CE    . MET B 2 608 ? 175.765 181.837 188.621 1.00 25.67  ? 608 MET B CE    1 
ATOM   8663  N  N     . CYS B 2 609 ? 180.958 186.165 188.764 1.00 34.88  ? 609 CYS B N     1 
ATOM   8664  C  CA    . CYS B 2 609 ? 182.270 186.428 189.357 1.00 34.43  ? 609 CYS B CA    1 
ATOM   8665  C  C     . CYS B 2 609 ? 182.497 185.568 190.600 1.00 36.19  ? 609 CYS B C     1 
ATOM   8666  O  O     . CYS B 2 609 ? 182.865 186.059 191.669 1.00 44.37  ? 609 CYS B O     1 
ATOM   8667  C  CB    . CYS B 2 609 ? 182.440 187.915 189.676 1.00 36.06  ? 609 CYS B CB    1 
ATOM   8668  S  SG    . CYS B 2 609 ? 182.212 189.009 188.255 1.00 50.75  ? 609 CYS B SG    1 
ATOM   8669  N  N     . LEU B 2 610 ? 182.271 184.267 190.448 1.00 28.87  ? 610 LEU B N     1 
ATOM   8670  C  CA    . LEU B 2 610 ? 182.438 183.341 191.556 1.00 30.89  ? 610 LEU B CA    1 
ATOM   8671  C  C     . LEU B 2 610 ? 183.915 183.198 191.910 1.00 35.01  ? 610 LEU B C     1 
ATOM   8672  O  O     . LEU B 2 610 ? 184.796 183.295 191.052 1.00 37.72  ? 610 LEU B O     1 
ATOM   8673  C  CB    . LEU B 2 610 ? 181.828 181.985 191.205 1.00 31.52  ? 610 LEU B CB    1 
ATOM   8674  C  CG    . LEU B 2 610 ? 180.322 182.059 190.931 1.00 33.31  ? 610 LEU B CG    1 
ATOM   8675  C  CD1   . LEU B 2 610 ? 179.779 180.745 190.398 1.00 31.48  ? 610 LEU B CD1   1 
ATOM   8676  C  CD2   . LEU B 2 610 ? 179.563 182.488 192.178 1.00 26.95  ? 610 LEU B CD2   1 
ATOM   8677  N  N     . HIS B 2 611 ? 184.177 182.971 193.200 1.00 36.61  ? 611 HIS B N     1 
ATOM   8678  C  CA    . HIS B 2 611 ? 185.540 183.038 193.720 1.00 32.24  ? 611 HIS B CA    1 
ATOM   8679  C  C     . HIS B 2 611 ? 186.445 182.000 193.065 1.00 35.63  ? 611 HIS B C     1 
ATOM   8680  O  O     . HIS B 2 611 ? 187.437 182.343 192.413 1.00 36.96  ? 611 HIS B O     1 
ATOM   8681  C  CB    . HIS B 2 611 ? 185.525 182.858 195.239 1.00 33.93  ? 611 HIS B CB    1 
ATOM   8682  C  CG    . HIS B 2 611 ? 186.836 183.160 195.897 1.00 37.89  ? 611 HIS B CG    1 
ATOM   8683  N  ND1   . HIS B 2 611 ? 187.712 182.175 196.298 1.00 37.45  ? 611 HIS B ND1   1 
ATOM   8684  C  CD2   . HIS B 2 611 ? 187.420 184.337 196.222 1.00 35.66  ? 611 HIS B CD2   1 
ATOM   8685  C  CE1   . HIS B 2 611 ? 188.779 182.732 196.842 1.00 37.20  ? 611 HIS B CE1   1 
ATOM   8686  N  NE2   . HIS B 2 611 ? 188.627 184.043 196.808 1.00 40.06  ? 611 HIS B NE2   1 
ATOM   8687  N  N     . SER B 2 612 ? 186.120 180.723 193.230 1.00 38.46  ? 612 SER B N     1 
ATOM   8688  C  CA    . SER B 2 612 ? 186.976 179.649 192.756 1.00 28.62  ? 612 SER B CA    1 
ATOM   8689  C  C     . SER B 2 612 ? 186.170 178.660 191.929 1.00 34.40  ? 612 SER B C     1 
ATOM   8690  O  O     . SER B 2 612 ? 184.957 178.529 192.118 1.00 38.72  ? 612 SER B O     1 
ATOM   8691  C  CB    . SER B 2 612 ? 187.636 178.914 193.933 1.00 26.63  ? 612 SER B CB    1 
ATOM   8692  O  OG    . SER B 2 612 ? 188.887 178.366 193.560 1.00 39.98  ? 612 SER B OG    1 
ATOM   8693  N  N     . PRO B 2 613 ? 186.817 177.962 190.989 1.00 30.98  ? 613 PRO B N     1 
ATOM   8694  C  CA    . PRO B 2 613 ? 186.104 176.898 190.262 1.00 30.39  ? 613 PRO B CA    1 
ATOM   8695  C  C     . PRO B 2 613 ? 185.537 175.829 191.178 1.00 29.75  ? 613 PRO B C     1 
ATOM   8696  O  O     . PRO B 2 613 ? 184.434 175.327 190.930 1.00 30.55  ? 613 PRO B O     1 
ATOM   8697  C  CB    . PRO B 2 613 ? 187.178 176.335 189.321 1.00 30.75  ? 613 PRO B CB    1 
ATOM   8698  C  CG    . PRO B 2 613 ? 188.171 177.432 189.167 1.00 27.20  ? 613 PRO B CG    1 
ATOM   8699  C  CD    . PRO B 2 613 ? 188.170 178.196 190.456 1.00 26.33  ? 613 PRO B CD    1 
ATOM   8700  N  N     . ASP B 2 614 ? 186.265 175.463 192.236 1.00 28.20  ? 614 ASP B N     1 
ATOM   8701  C  CA    . ASP B 2 614 ? 185.729 174.516 193.207 1.00 30.28  ? 614 ASP B CA    1 
ATOM   8702  C  C     . ASP B 2 614 ? 184.574 175.127 193.992 1.00 33.57  ? 614 ASP B C     1 
ATOM   8703  O  O     . ASP B 2 614 ? 183.573 174.453 194.260 1.00 39.38  ? 614 ASP B O     1 
ATOM   8704  C  CB    . ASP B 2 614 ? 186.835 174.048 194.152 1.00 30.77  ? 614 ASP B CB    1 
ATOM   8705  C  CG    . ASP B 2 614 ? 187.556 172.817 193.641 1.00 37.61  ? 614 ASP B CG    1 
ATOM   8706  O  OD1   . ASP B 2 614 ? 187.117 172.252 192.617 1.00 35.77  ? 614 ASP B OD1   1 
ATOM   8707  O  OD2   . ASP B 2 614 ? 188.560 172.414 194.263 1.00 38.61  ? 614 ASP B OD2   1 
ATOM   8708  N  N     . SER B 2 615 ? 184.697 176.402 194.370 1.00 24.60  ? 615 SER B N     1 
ATOM   8709  C  CA    . SER B 2 615 ? 183.612 177.069 195.081 1.00 31.51  ? 615 SER B CA    1 
ATOM   8710  C  C     . SER B 2 615 ? 182.409 177.302 194.177 1.00 26.45  ? 615 SER B C     1 
ATOM   8711  O  O     . SER B 2 615 ? 181.274 177.368 194.663 1.00 29.56  ? 615 SER B O     1 
ATOM   8712  C  CB    . SER B 2 615 ? 184.100 178.395 195.662 1.00 30.67  ? 615 SER B CB    1 
ATOM   8713  O  OG    . SER B 2 615 ? 184.072 179.423 194.688 1.00 27.70  ? 615 SER B OG    1 
ATOM   8714  N  N     . ALA B 2 616 ? 182.635 177.430 192.869 1.00 27.14  ? 616 ALA B N     1 
ATOM   8715  C  CA    . ALA B 2 616 ? 181.526 177.630 191.942 1.00 22.14  ? 616 ALA B CA    1 
ATOM   8716  C  C     . ALA B 2 616 ? 180.655 176.384 191.848 1.00 24.60  ? 616 ALA B C     1 
ATOM   8717  O  O     . ALA B 2 616 ? 179.422 176.478 191.837 1.00 28.77  ? 616 ALA B O     1 
ATOM   8718  C  CB    . ALA B 2 616 ? 182.062 178.015 190.564 1.00 20.25  ? 616 ALA B CB    1 
ATOM   8719  N  N     . ILE B 2 617 ? 181.279 175.208 191.778 1.00 26.40  ? 617 ILE B N     1 
ATOM   8720  C  CA    . ILE B 2 617 ? 180.520 173.964 191.698 1.00 23.54  ? 617 ILE B CA    1 
ATOM   8721  C  C     . ILE B 2 617 ? 179.835 173.669 193.027 1.00 22.50  ? 617 ILE B C     1 
ATOM   8722  O  O     . ILE B 2 617 ? 178.681 173.226 193.061 1.00 28.55  ? 617 ILE B O     1 
ATOM   8723  C  CB    . ILE B 2 617 ? 181.442 172.812 191.258 1.00 27.09  ? 617 ILE B CB    1 
ATOM   8724  C  CG1   . ILE B 2 617 ? 181.878 173.012 189.806 1.00 29.06  ? 617 ILE B CG1   1 
ATOM   8725  C  CG2   . ILE B 2 617 ? 180.743 171.472 191.414 1.00 21.92  ? 617 ILE B CG2   1 
ATOM   8726  C  CD1   . ILE B 2 617 ? 183.279 172.525 189.517 1.00 28.06  ? 617 ILE B CD1   1 
ATOM   8727  N  N     . LEU B 2 618 ? 180.532 173.912 194.141 1.00 27.78  ? 618 LEU B N     1 
ATOM   8728  C  CA    . LEU B 2 618 ? 179.944 173.669 195.455 1.00 27.08  ? 618 LEU B CA    1 
ATOM   8729  C  C     . LEU B 2 618 ? 178.731 174.557 195.696 1.00 22.02  ? 618 LEU B C     1 
ATOM   8730  O  O     . LEU B 2 618 ? 177.717 174.101 196.237 1.00 31.17  ? 618 LEU B O     1 
ATOM   8731  C  CB    . LEU B 2 618 ? 180.992 173.888 196.546 1.00 25.66  ? 618 LEU B CB    1 
ATOM   8732  C  CG    . LEU B 2 618 ? 180.812 173.095 197.842 1.00 27.66  ? 618 LEU B CG    1 
ATOM   8733  C  CD1   . LEU B 2 618 ? 180.610 171.617 197.555 1.00 29.76  ? 618 LEU B CD1   1 
ATOM   8734  C  CD2   . LEU B 2 618 ? 181.999 173.307 198.770 1.00 29.14  ? 618 LEU B CD2   1 
ATOM   8735  N  N     . SER B 2 619 ? 178.813 175.830 195.300 1.00 21.31  ? 619 SER B N     1 
ATOM   8736  C  CA    . SER B 2 619 ? 177.704 176.750 195.531 1.00 20.25  ? 619 SER B CA    1 
ATOM   8737  C  C     . SER B 2 619 ? 176.464 176.331 194.751 1.00 19.85  ? 619 SER B C     1 
ATOM   8738  O  O     . SER B 2 619 ? 175.336 176.503 195.227 1.00 17.19  ? 619 SER B O     1 
ATOM   8739  C  CB    . SER B 2 619 ? 178.119 178.173 195.160 1.00 18.33  ? 619 SER B CB    1 
ATOM   8740  O  OG    . SER B 2 619 ? 179.217 178.601 195.945 1.00 30.51  ? 619 SER B OG    1 
ATOM   8741  N  N     . ALA B 2 620 ? 176.653 175.784 193.549 1.00 20.19  ? 620 ALA B N     1 
ATOM   8742  C  CA    . ALA B 2 620 ? 175.515 175.298 192.776 1.00 22.29  ? 620 ALA B CA    1 
ATOM   8743  C  C     . ALA B 2 620 ? 174.890 174.070 193.427 1.00 20.64  ? 620 ALA B C     1 
ATOM   8744  O  O     . ALA B 2 620 ? 173.662 173.922 193.440 1.00 25.54  ? 620 ALA B O     1 
ATOM   8745  C  CB    . ALA B 2 620 ? 175.947 174.987 191.343 1.00 11.65  ? 620 ALA B CB    1 
ATOM   8746  N  N     . VAL B 2 621 ? 175.720 173.177 193.969 1.00 13.23  ? 621 VAL B N     1 
ATOM   8747  C  CA    . VAL B 2 621 ? 175.200 171.984 194.630 1.00 15.06  ? 621 VAL B CA    1 
ATOM   8748  C  C     . VAL B 2 621 ? 174.480 172.356 195.920 1.00 23.35  ? 621 VAL B C     1 
ATOM   8749  O  O     . VAL B 2 621 ? 173.414 171.812 196.231 1.00 27.80  ? 621 VAL B O     1 
ATOM   8750  C  CB    . VAL B 2 621 ? 176.337 170.977 194.880 1.00 24.14  ? 621 VAL B CB    1 
ATOM   8751  C  CG1   . VAL B 2 621 ? 175.844 169.809 195.723 1.00 18.25  ? 621 VAL B CG1   1 
ATOM   8752  C  CG2   . VAL B 2 621 ? 176.904 170.482 193.561 1.00 19.19  ? 621 VAL B CG2   1 
ATOM   8753  N  N     . ILE B 2 622 ? 175.049 173.286 196.692 1.00 19.61  ? 622 ILE B N     1 
ATOM   8754  C  CA    . ILE B 2 622 ? 174.421 173.705 197.943 1.00 18.43  ? 622 ILE B CA    1 
ATOM   8755  C  C     . ILE B 2 622 ? 173.074 174.362 197.670 1.00 19.54  ? 622 ILE B C     1 
ATOM   8756  O  O     . ILE B 2 622 ? 172.084 174.094 198.363 1.00 22.23  ? 622 ILE B O     1 
ATOM   8757  C  CB    . ILE B 2 622 ? 175.362 174.638 198.728 1.00 23.80  ? 622 ILE B CB    1 
ATOM   8758  C  CG1   . ILE B 2 622 ? 176.594 173.869 199.209 1.00 20.82  ? 622 ILE B CG1   1 
ATOM   8759  C  CG2   . ILE B 2 622 ? 174.636 175.262 199.909 1.00 21.86  ? 622 ILE B CG2   1 
ATOM   8760  C  CD1   . ILE B 2 622 ? 177.579 174.712 199.986 1.00 21.31  ? 622 ILE B CD1   1 
ATOM   8761  N  N     . PHE B 2 623 ? 173.010 175.229 196.656 1.00 22.13  ? 623 PHE B N     1 
ATOM   8762  C  CA    . PHE B 2 623 ? 171.738 175.845 196.291 1.00 20.69  ? 623 PHE B CA    1 
ATOM   8763  C  C     . PHE B 2 623 ? 170.732 174.801 195.828 1.00 20.73  ? 623 PHE B C     1 
ATOM   8764  O  O     . PHE B 2 623 ? 169.533 174.914 196.113 1.00 21.28  ? 623 PHE B O     1 
ATOM   8765  C  CB    . PHE B 2 623 ? 171.947 176.898 195.203 1.00 15.81  ? 623 PHE B CB    1 
ATOM   8766  C  CG    . PHE B 2 623 ? 170.692 177.633 194.829 1.00 26.15  ? 623 PHE B CG    1 
ATOM   8767  C  CD1   . PHE B 2 623 ? 170.244 178.700 195.589 1.00 26.55  ? 623 PHE B CD1   1 
ATOM   8768  C  CD2   . PHE B 2 623 ? 169.950 177.245 193.725 1.00 22.22  ? 623 PHE B CD2   1 
ATOM   8769  C  CE1   . PHE B 2 623 ? 169.086 179.372 195.249 1.00 24.89  ? 623 PHE B CE1   1 
ATOM   8770  C  CE2   . PHE B 2 623 ? 168.791 177.912 193.382 1.00 23.52  ? 623 PHE B CE2   1 
ATOM   8771  C  CZ    . PHE B 2 623 ? 168.358 178.976 194.146 1.00 26.28  ? 623 PHE B CZ    1 
ATOM   8772  N  N     . ASN B 2 624 ? 171.200 173.781 195.106 1.00 24.62  ? 624 ASN B N     1 
ATOM   8773  C  CA    . ASN B 2 624 ? 170.306 172.731 194.632 1.00 21.27  ? 624 ASN B CA    1 
ATOM   8774  C  C     . ASN B 2 624 ? 169.639 171.998 195.788 1.00 21.90  ? 624 ASN B C     1 
ATOM   8775  O  O     . ASN B 2 624 ? 168.455 171.653 195.703 1.00 25.70  ? 624 ASN B O     1 
ATOM   8776  C  CB    . ASN B 2 624 ? 171.078 171.750 193.749 1.00 22.89  ? 624 ASN B CB    1 
ATOM   8777  C  CG    . ASN B 2 624 ? 170.167 170.850 192.943 1.00 25.86  ? 624 ASN B CG    1 
ATOM   8778  O  OD1   . ASN B 2 624 ? 169.585 171.272 191.946 1.00 30.52  ? 624 ASN B OD1   1 
ATOM   8779  N  ND2   . ASN B 2 624 ? 170.041 169.600 193.371 1.00 27.93  ? 624 ASN B ND2   1 
ATOM   8780  N  N     . ALA B 2 625 ? 170.378 171.742 196.866 1.00 21.04  ? 625 ALA B N     1 
ATOM   8781  C  CA    . ALA B 2 625 ? 169.812 171.101 198.045 1.00 18.41  ? 625 ALA B CA    1 
ATOM   8782  C  C     . ALA B 2 625 ? 168.948 172.048 198.869 1.00 22.32  ? 625 ALA B C     1 
ATOM   8783  O  O     . ALA B 2 625 ? 167.887 171.648 199.359 1.00 22.07  ? 625 ALA B O     1 
ATOM   8784  C  CB    . ALA B 2 625 ? 170.930 170.528 198.920 1.00 17.93  ? 625 ALA B CB    1 
ATOM   8785  N  N     . LEU B 2 626 ? 169.375 173.304 199.023 1.00 22.84  ? 626 LEU B N     1 
ATOM   8786  C  CA    . LEU B 2 626 ? 168.666 174.222 199.910 1.00 22.53  ? 626 LEU B CA    1 
ATOM   8787  C  C     . LEU B 2 626 ? 167.355 174.706 199.306 1.00 23.10  ? 626 LEU B C     1 
ATOM   8788  O  O     . LEU B 2 626 ? 166.428 175.051 200.047 1.00 29.24  ? 626 LEU B O     1 
ATOM   8789  C  CB    . LEU B 2 626 ? 169.558 175.414 200.256 1.00 23.36  ? 626 LEU B CB    1 
ATOM   8790  C  CG    . LEU B 2 626 ? 170.715 175.146 201.219 1.00 25.34  ? 626 LEU B CG    1 
ATOM   8791  C  CD1   . LEU B 2 626 ? 171.470 176.431 201.520 1.00 22.91  ? 626 LEU B CD1   1 
ATOM   8792  C  CD2   . LEU B 2 626 ? 170.212 174.502 202.501 1.00 24.27  ? 626 LEU B CD2   1 
ATOM   8793  N  N     . ILE B 2 627 ? 167.253 174.741 197.975 1.00 26.94  ? 627 ILE B N     1 
ATOM   8794  C  CA    . ILE B 2 627 ? 166.024 175.220 197.349 1.00 18.48  ? 627 ILE B CA    1 
ATOM   8795  C  C     . ILE B 2 627 ? 164.867 174.265 197.623 1.00 20.84  ? 627 ILE B C     1 
ATOM   8796  O  O     . ILE B 2 627 ? 163.706 174.689 197.683 1.00 26.05  ? 627 ILE B O     1 
ATOM   8797  C  CB    . ILE B 2 627 ? 166.242 175.444 195.839 1.00 21.42  ? 627 ILE B CB    1 
ATOM   8798  C  CG1   . ILE B 2 627 ? 165.063 176.208 195.231 1.00 21.24  ? 627 ILE B CG1   1 
ATOM   8799  C  CG2   . ILE B 2 627 ? 166.458 174.124 195.114 1.00 23.49  ? 627 ILE B CG2   1 
ATOM   8800  C  CD1   . ILE B 2 627 ? 164.796 177.544 195.888 1.00 24.21  ? 627 ILE B CD1   1 
ATOM   8801  N  N     . ILE B 2 628 ? 165.155 172.974 197.800 1.00 29.54  ? 628 ILE B N     1 
ATOM   8802  C  CA    . ILE B 2 628 ? 164.102 172.010 198.105 1.00 20.10  ? 628 ILE B CA    1 
ATOM   8803  C  C     . ILE B 2 628 ? 163.504 172.292 199.478 1.00 25.63  ? 628 ILE B C     1 
ATOM   8804  O  O     . ILE B 2 628 ? 162.279 172.331 199.645 1.00 28.20  ? 628 ILE B O     1 
ATOM   8805  C  CB    . ILE B 2 628 ? 164.647 170.573 198.012 1.00 27.02  ? 628 ILE B CB    1 
ATOM   8806  C  CG1   . ILE B 2 628 ? 164.907 170.193 196.553 1.00 30.81  ? 628 ILE B CG1   1 
ATOM   8807  C  CG2   . ILE B 2 628 ? 163.685 169.588 198.659 1.00 21.84  ? 628 ILE B CG2   1 
ATOM   8808  C  CD1   . ILE B 2 628 ? 165.936 169.098 196.384 1.00 25.25  ? 628 ILE B CD1   1 
ATOM   8809  N  N     . VAL B 2 629 ? 164.361 172.494 200.482 1.00 27.00  ? 629 VAL B N     1 
ATOM   8810  C  CA    . VAL B 2 629 ? 163.876 172.755 201.833 1.00 28.95  ? 629 VAL B CA    1 
ATOM   8811  C  C     . VAL B 2 629 ? 163.181 174.111 201.909 1.00 25.08  ? 629 VAL B C     1 
ATOM   8812  O  O     . VAL B 2 629 ? 162.216 174.279 202.666 1.00 29.70  ? 629 VAL B O     1 
ATOM   8813  C  CB    . VAL B 2 629 ? 165.034 172.632 202.846 1.00 26.66  ? 629 VAL B CB    1 
ATOM   8814  C  CG1   . VAL B 2 629 ? 165.307 173.956 203.553 1.00 28.17  ? 629 VAL B CG1   1 
ATOM   8815  C  CG2   . VAL B 2 629 ? 164.737 171.534 203.855 1.00 26.74  ? 629 VAL B CG2   1 
ATOM   8816  N  N     . PHE B 2 630 ? 163.646 175.096 201.135 1.00 28.31  ? 630 PHE B N     1 
ATOM   8817  C  CA    . PHE B 2 630 ? 163.033 176.418 201.165 1.00 26.65  ? 630 PHE B CA    1 
ATOM   8818  C  C     . PHE B 2 630 ? 161.658 176.439 200.511 1.00 27.43  ? 630 PHE B C     1 
ATOM   8819  O  O     . PHE B 2 630 ? 160.846 177.311 200.836 1.00 34.85  ? 630 PHE B O     1 
ATOM   8820  C  CB    . PHE B 2 630 ? 163.947 177.439 200.486 1.00 26.53  ? 630 PHE B CB    1 
ATOM   8821  C  CG    . PHE B 2 630 ? 164.854 178.167 201.438 1.00 35.20  ? 630 PHE B CG    1 
ATOM   8822  C  CD1   . PHE B 2 630 ? 166.079 177.631 201.796 1.00 34.91  ? 630 PHE B CD1   1 
ATOM   8823  C  CD2   . PHE B 2 630 ? 164.480 179.388 201.974 1.00 31.79  ? 630 PHE B CD2   1 
ATOM   8824  C  CE1   . PHE B 2 630 ? 166.915 178.299 202.671 1.00 38.19  ? 630 PHE B CE1   1 
ATOM   8825  C  CE2   . PHE B 2 630 ? 165.311 180.060 202.850 1.00 33.78  ? 630 PHE B CE2   1 
ATOM   8826  C  CZ    . PHE B 2 630 ? 166.530 179.515 203.199 1.00 36.76  ? 630 PHE B CZ    1 
ATOM   8827  N  N     . LEU B 2 631 ? 161.377 175.506 199.603 1.00 28.28  ? 631 LEU B N     1 
ATOM   8828  C  CA    . LEU B 2 631 ? 160.086 175.425 198.936 1.00 29.51  ? 631 LEU B CA    1 
ATOM   8829  C  C     . LEU B 2 631 ? 159.161 174.396 199.572 1.00 26.66  ? 631 LEU B C     1 
ATOM   8830  O  O     . LEU B 2 631 ? 158.112 174.083 199.000 1.00 34.55  ? 631 LEU B O     1 
ATOM   8831  C  CB    . LEU B 2 631 ? 160.275 175.110 197.451 1.00 26.66  ? 631 LEU B CB    1 
ATOM   8832  C  CG    . LEU B 2 631 ? 160.942 176.201 196.611 1.00 29.42  ? 631 LEU B CG    1 
ATOM   8833  C  CD1   . LEU B 2 631 ? 160.998 175.793 195.150 1.00 27.92  ? 631 LEU B CD1   1 
ATOM   8834  C  CD2   . LEU B 2 631 ? 160.211 177.524 196.773 1.00 27.19  ? 631 LEU B CD2   1 
ATOM   8835  N  N     . ILE B 2 632 ? 159.529 173.859 200.736 1.00 26.38  ? 632 ILE B N     1 
ATOM   8836  C  CA    . ILE B 2 632 ? 158.651 172.912 201.427 1.00 29.89  ? 632 ILE B CA    1 
ATOM   8837  C  C     . ILE B 2 632 ? 157.319 173.545 201.819 1.00 31.86  ? 632 ILE B C     1 
ATOM   8838  O  O     . ILE B 2 632 ? 156.271 172.929 201.563 1.00 30.22  ? 632 ILE B O     1 
ATOM   8839  C  CB    . ILE B 2 632 ? 159.389 172.283 202.622 1.00 30.37  ? 632 ILE B CB    1 
ATOM   8840  C  CG1   . ILE B 2 632 ? 160.233 171.095 202.158 1.00 28.78  ? 632 ILE B CG1   1 
ATOM   8841  C  CG2   . ILE B 2 632 ? 158.404 171.844 203.696 1.00 27.82  ? 632 ILE B CG2   1 
ATOM   8842  C  CD1   . ILE B 2 632 ? 161.119 170.517 203.236 1.00 27.06  ? 632 ILE B CD1   1 
ATOM   8843  N  N     . PRO B 2 633 ? 157.271 174.736 202.434 1.00 33.15  ? 633 PRO B N     1 
ATOM   8844  C  CA    . PRO B 2 633 ? 155.955 175.330 202.734 1.00 27.66  ? 633 PRO B CA    1 
ATOM   8845  C  C     . PRO B 2 633 ? 155.116 175.594 201.497 1.00 27.96  ? 633 PRO B C     1 
ATOM   8846  O  O     . PRO B 2 633 ? 153.884 175.502 201.567 1.00 38.04  ? 633 PRO B O     1 
ATOM   8847  C  CB    . PRO B 2 633 ? 156.304 176.632 203.470 1.00 26.34  ? 633 PRO B CB    1 
ATOM   8848  C  CG    . PRO B 2 633 ? 157.720 176.499 203.880 1.00 32.53  ? 633 PRO B CG    1 
ATOM   8849  C  CD    . PRO B 2 633 ? 158.373 175.604 202.889 1.00 28.21  ? 633 PRO B CD    1 
ATOM   8850  N  N     . LEU B 2 634 ? 155.742 175.928 200.367 1.00 30.29  ? 634 LEU B N     1 
ATOM   8851  C  CA    . LEU B 2 634 ? 154.985 176.129 199.136 1.00 27.69  ? 634 LEU B CA    1 
ATOM   8852  C  C     . LEU B 2 634 ? 154.331 174.833 198.672 1.00 33.46  ? 634 LEU B C     1 
ATOM   8853  O  O     . LEU B 2 634 ? 153.181 174.840 198.221 1.00 35.10  ? 634 LEU B O     1 
ATOM   8854  C  CB    . LEU B 2 634 ? 155.892 176.696 198.045 1.00 31.96  ? 634 LEU B CB    1 
ATOM   8855  C  CG    . LEU B 2 634 ? 155.206 177.085 196.734 1.00 33.70  ? 634 LEU B CG    1 
ATOM   8856  C  CD1   . LEU B 2 634 ? 154.317 178.302 196.933 1.00 30.16  ? 634 LEU B CD1   1 
ATOM   8857  C  CD2   . LEU B 2 634 ? 156.235 177.341 195.644 1.00 32.52  ? 634 LEU B CD2   1 
ATOM   8858  N  N     . ALA B 2 635 ? 155.050 173.713 198.768 1.00 27.47  ? 635 ALA B N     1 
ATOM   8859  C  CA    . ALA B 2 635 ? 154.476 172.432 198.371 1.00 25.85  ? 635 ALA B CA    1 
ATOM   8860  C  C     . ALA B 2 635 ? 153.371 171.999 199.327 1.00 30.41  ? 635 ALA B C     1 
ATOM   8861  O  O     . ALA B 2 635 ? 152.363 171.424 198.900 1.00 30.25  ? 635 ALA B O     1 
ATOM   8862  C  CB    . ALA B 2 635 ? 155.569 171.367 198.295 1.00 28.99  ? 635 ALA B CB    1 
ATOM   8863  N  N     . LEU B 2 636 ? 153.544 172.261 200.625 1.00 35.91  ? 636 LEU B N     1 
ATOM   8864  C  CA    . LEU B 2 636 ? 152.537 171.857 201.601 1.00 30.10  ? 636 LEU B CA    1 
ATOM   8865  C  C     . LEU B 2 636 ? 151.282 172.715 201.495 1.00 28.89  ? 636 LEU B C     1 
ATOM   8866  O  O     . LEU B 2 636 ? 150.163 172.207 201.638 1.00 35.37  ? 636 LEU B O     1 
ATOM   8867  C  CB    . LEU B 2 636 ? 153.117 171.928 203.013 1.00 31.66  ? 636 LEU B CB    1 
ATOM   8868  C  CG    . LEU B 2 636 ? 154.252 170.952 203.332 1.00 36.89  ? 636 LEU B CG    1 
ATOM   8869  C  CD1   . LEU B 2 636 ? 154.524 170.916 204.828 1.00 36.88  ? 636 LEU B CD1   1 
ATOM   8870  C  CD2   . LEU B 2 636 ? 153.933 169.560 202.809 1.00 31.78  ? 636 LEU B CD2   1 
ATOM   8871  N  N     . LYS B 2 637 ? 151.444 174.015 201.251 1.00 26.06  ? 637 LYS B N     1 
ATOM   8872  C  CA    . LYS B 2 637 ? 150.303 174.917 201.159 1.00 29.97  ? 637 LYS B CA    1 
ATOM   8873  C  C     . LYS B 2 637 ? 149.748 175.030 199.747 1.00 32.83  ? 637 LYS B C     1 
ATOM   8874  O  O     . LYS B 2 637 ? 148.537 175.216 199.580 1.00 38.13  ? 637 LYS B O     1 
ATOM   8875  C  CB    . LYS B 2 637 ? 150.690 176.310 201.665 1.00 30.31  ? 637 LYS B CB    1 
ATOM   8876  C  CG    . LYS B 2 637 ? 150.581 176.473 203.171 1.00 32.60  ? 637 LYS B CG    1 
ATOM   8877  C  CD    . LYS B 2 637 ? 151.860 177.046 203.758 1.00 38.82  ? 637 LYS B CD    1 
ATOM   8878  C  CE    . LYS B 2 637 ? 151.898 178.559 203.623 1.00 39.57  ? 637 LYS B CE    1 
ATOM   8879  N  NZ    . LYS B 2 637 ? 153.287 179.089 203.699 1.00 40.17  ? 637 LYS B NZ    1 
ATOM   8880  N  N     . GLY B 2 638 ? 150.596 174.924 198.733 1.00 29.35  ? 638 GLY B N     1 
ATOM   8881  C  CA    . GLY B 2 638 ? 150.163 175.045 197.358 1.00 21.36  ? 638 GLY B CA    1 
ATOM   8882  C  C     . GLY B 2 638 ? 150.256 176.470 196.839 1.00 31.15  ? 638 GLY B C     1 
ATOM   8883  O  O     . GLY B 2 638 ? 150.323 177.440 197.593 1.00 32.69  ? 638 GLY B O     1 
ATOM   8884  N  N     . VAL B 2 639 ? 150.262 176.585 195.512 1.00 36.49  ? 639 VAL B N     1 
ATOM   8885  C  CA    . VAL B 2 639 ? 150.280 177.894 194.871 1.00 32.16  ? 639 VAL B CA    1 
ATOM   8886  C  C     . VAL B 2 639 ? 148.949 178.588 195.121 1.00 39.85  ? 639 VAL B C     1 
ATOM   8887  O  O     . VAL B 2 639 ? 147.878 177.992 194.948 1.00 44.33  ? 639 VAL B O     1 
ATOM   8888  C  CB    . VAL B 2 639 ? 150.570 177.752 193.369 1.00 34.37  ? 639 VAL B CB    1 
ATOM   8889  C  CG1   . VAL B 2 639 ? 150.234 179.040 192.632 1.00 37.27  ? 639 VAL B CG1   1 
ATOM   8890  C  CG2   . VAL B 2 639 ? 152.025 177.370 193.145 1.00 35.78  ? 639 VAL B CG2   1 
ATOM   8891  N  N     . SER B 2 640 ? 149.011 179.851 195.541 1.00 38.98  ? 640 SER B N     1 
ATOM   8892  C  CA    . SER B 2 640 ? 147.803 180.594 195.875 1.00 42.65  ? 640 SER B CA    1 
ATOM   8893  C  C     . SER B 2 640 ? 146.888 180.715 194.663 1.00 42.64  ? 640 SER B C     1 
ATOM   8894  O  O     . SER B 2 640 ? 147.335 181.043 193.560 1.00 47.69  ? 640 SER B O     1 
ATOM   8895  C  CB    . SER B 2 640 ? 148.168 181.981 196.404 1.00 42.73  ? 640 SER B CB    1 
ATOM   8896  O  OG    . SER B 2 640 ? 148.063 182.958 195.384 1.00 46.39  ? 640 SER B OG    1 
ATOM   8897  N  N     . TYR B 2 641 ? 145.604 180.448 194.875 1.00 45.69  ? 641 TYR B N     1 
ATOM   8898  C  CA    . TYR B 2 641 ? 144.603 180.496 193.819 1.00 44.73  ? 641 TYR B CA    1 
ATOM   8899  C  C     . TYR B 2 641 ? 143.923 181.858 193.796 1.00 46.82  ? 641 TYR B C     1 
ATOM   8900  O  O     . TYR B 2 641 ? 143.603 182.423 194.846 1.00 49.39  ? 641 TYR B O     1 
ATOM   8901  C  CB    . TYR B 2 641 ? 143.557 179.395 194.012 1.00 44.71  ? 641 TYR B CB    1 
ATOM   8902  C  CG    . TYR B 2 641 ? 142.350 179.529 193.112 1.00 47.36  ? 641 TYR B CG    1 
ATOM   8903  C  CD1   . TYR B 2 641 ? 142.418 179.185 191.770 1.00 45.58  ? 641 TYR B CD1   1 
ATOM   8904  C  CD2   . TYR B 2 641 ? 141.141 180.003 193.606 1.00 46.70  ? 641 TYR B CD2   1 
ATOM   8905  C  CE1   . TYR B 2 641 ? 141.317 179.308 190.944 1.00 46.12  ? 641 TYR B CE1   1 
ATOM   8906  C  CE2   . TYR B 2 641 ? 140.035 180.130 192.788 1.00 45.23  ? 641 TYR B CE2   1 
ATOM   8907  C  CZ    . TYR B 2 641 ? 140.129 179.780 191.458 1.00 47.56  ? 641 TYR B CZ    1 
ATOM   8908  O  OH    . TYR B 2 641 ? 139.030 179.904 190.640 1.00 48.27  ? 641 TYR B OH    1 
ATOM   8909  N  N     . LYS B 2 642 ? 143.704 182.379 192.591 1.00 47.83  ? 642 LYS B N     1 
ATOM   8910  C  CA    . LYS B 2 642 ? 142.996 183.633 192.397 1.00 44.53  ? 642 LYS B CA    1 
ATOM   8911  C  C     . LYS B 2 642 ? 141.985 183.483 191.268 1.00 46.79  ? 642 LYS B C     1 
ATOM   8912  O  O     . LYS B 2 642 ? 142.296 182.892 190.227 1.00 48.80  ? 642 LYS B O     1 
ATOM   8913  C  CB    . LYS B 2 642 ? 143.967 184.779 192.077 1.00 46.75  ? 642 LYS B CB    1 
ATOM   8914  C  CG    . LYS B 2 642 ? 144.556 185.453 193.306 1.00 48.96  ? 642 LYS B CG    1 
ATOM   8915  C  CD    . LYS B 2 642 ? 146.037 185.146 193.453 1.00 49.42  ? 642 LYS B CD    1 
ATOM   8916  C  CE    . LYS B 2 642 ? 146.613 185.802 194.698 1.00 51.16  ? 642 LYS B CE    1 
ATOM   8917  N  NZ    . LYS B 2 642 ? 145.985 185.278 195.942 1.00 49.49  ? 642 LYS B NZ    1 
ATOM   8918  N  N     . PRO B 2 643 ? 140.770 184.004 191.443 1.00 49.20  ? 643 PRO B N     1 
ATOM   8919  C  CA    . PRO B 2 643 ? 139.754 183.878 190.389 1.00 44.64  ? 643 PRO B CA    1 
ATOM   8920  C  C     . PRO B 2 643 ? 140.042 184.774 189.194 1.00 44.46  ? 643 PRO B C     1 
ATOM   8921  O  O     . PRO B 2 643 ? 139.407 185.820 189.024 1.00 50.59  ? 643 PRO B O     1 
ATOM   8922  C  CB    . PRO B 2 643 ? 138.460 184.287 191.101 1.00 44.26  ? 643 PRO B CB    1 
ATOM   8923  C  CG    . PRO B 2 643 ? 138.911 185.198 192.192 1.00 46.58  ? 643 PRO B CG    1 
ATOM   8924  C  CD    . PRO B 2 643 ? 140.249 184.682 192.642 1.00 46.72  ? 643 PRO B CD    1 
ATOM   8925  N  N     . LEU B 2 644 ? 140.996 184.372 188.362 1.00 42.08  ? 644 LEU B N     1 
ATOM   8926  C  CA    . LEU B 2 644 ? 141.386 185.122 187.179 1.00 38.95  ? 644 LEU B CA    1 
ATOM   8927  C  C     . LEU B 2 644 ? 141.098 184.300 185.929 1.00 35.16  ? 644 LEU B C     1 
ATOM   8928  O  O     . LEU B 2 644 ? 140.768 183.114 185.996 1.00 42.12  ? 644 LEU B O     1 
ATOM   8929  C  CB    . LEU B 2 644 ? 142.870 185.505 187.231 1.00 39.00  ? 644 LEU B CB    1 
ATOM   8930  C  CG    . LEU B 2 644 ? 143.295 186.463 188.345 1.00 43.06  ? 644 LEU B CG    1 
ATOM   8931  C  CD1   . LEU B 2 644 ? 144.782 186.324 188.630 1.00 36.90  ? 644 LEU B CD1   1 
ATOM   8932  C  CD2   . LEU B 2 644 ? 142.945 187.896 187.983 1.00 42.16  ? 644 LEU B CD2   1 
ATOM   8933  N  N     . THR B 2 645 ? 141.229 184.951 184.776 1.00 33.68  ? 645 THR B N     1 
ATOM   8934  C  CA    . THR B 2 645 ? 141.061 184.260 183.509 1.00 31.70  ? 645 THR B CA    1 
ATOM   8935  C  C     . THR B 2 645 ? 142.259 183.350 183.243 1.00 32.73  ? 645 THR B C     1 
ATOM   8936  O  O     . THR B 2 645 ? 143.295 183.423 183.911 1.00 36.46  ? 645 THR B O     1 
ATOM   8937  C  CB    . THR B 2 645 ? 140.885 185.259 182.365 1.00 36.40  ? 645 THR B CB    1 
ATOM   8938  O  OG1   . THR B 2 645 ? 142.114 185.963 182.148 1.00 38.53  ? 645 THR B OG1   1 
ATOM   8939  C  CG2   . THR B 2 645 ? 139.786 186.258 182.694 1.00 35.69  ? 645 THR B CG2   1 
ATOM   8940  N  N     . ALA B 2 646 ? 142.102 182.472 182.250 1.00 32.68  ? 646 ALA B N     1 
ATOM   8941  C  CA    . ALA B 2 646 ? 143.171 181.536 181.920 1.00 30.39  ? 646 ALA B CA    1 
ATOM   8942  C  C     . ALA B 2 646 ? 144.413 182.264 181.422 1.00 31.19  ? 646 ALA B C     1 
ATOM   8943  O  O     . ALA B 2 646 ? 145.540 181.886 181.760 1.00 36.84  ? 646 ALA B O     1 
ATOM   8944  C  CB    . ALA B 2 646 ? 142.683 180.528 180.880 1.00 27.03  ? 646 ALA B CB    1 
ATOM   8945  N  N     . SER B 2 647 ? 144.228 183.318 180.623 1.00 34.08  ? 647 SER B N     1 
ATOM   8946  C  CA    . SER B 2 647 ? 145.376 184.050 180.098 1.00 31.77  ? 647 SER B CA    1 
ATOM   8947  C  C     . SER B 2 647 ? 145.990 184.955 181.159 1.00 32.26  ? 647 SER B C     1 
ATOM   8948  O  O     . SER B 2 647 ? 147.133 185.405 181.013 1.00 32.56  ? 647 SER B O     1 
ATOM   8949  C  CB    . SER B 2 647 ? 144.965 184.865 178.873 1.00 32.86  ? 647 SER B CB    1 
ATOM   8950  O  OG    . SER B 2 647 ? 144.833 184.039 177.730 1.00 40.79  ? 647 SER B OG    1 
ATOM   8951  N  N     . ALA B 2 648 ? 145.254 185.225 182.239 1.00 28.96  ? 648 ALA B N     1 
ATOM   8952  C  CA    . ALA B 2 648 ? 145.796 186.065 183.301 1.00 27.17  ? 648 ALA B CA    1 
ATOM   8953  C  C     . ALA B 2 648 ? 146.432 185.220 184.396 1.00 33.63  ? 648 ALA B C     1 
ATOM   8954  O  O     . ALA B 2 648 ? 147.426 185.631 185.007 1.00 30.34  ? 648 ALA B O     1 
ATOM   8955  C  CB    . ALA B 2 648 ? 144.699 186.959 183.878 1.00 26.36  ? 648 ALA B CB    1 
ATOM   8956  N  N     . MET B 2 649 ? 145.872 184.039 184.660 1.00 35.98  ? 649 MET B N     1 
ATOM   8957  C  CA    . MET B 2 649 ? 146.479 183.138 185.634 1.00 31.59  ? 649 MET B CA    1 
ATOM   8958  C  C     . MET B 2 649 ? 147.798 182.580 185.112 1.00 32.69  ? 649 MET B C     1 
ATOM   8959  O  O     . MET B 2 649 ? 148.764 182.440 185.871 1.00 28.23  ? 649 MET B O     1 
ATOM   8960  C  CB    . MET B 2 649 ? 145.507 182.008 185.974 1.00 31.22  ? 649 MET B CB    1 
ATOM   8961  C  CG    . MET B 2 649 ? 146.048 180.943 186.923 1.00 35.03  ? 649 MET B CG    1 
ATOM   8962  S  SD    . MET B 2 649 ? 145.972 181.406 188.671 1.00 51.80  ? 649 MET B SD    1 
ATOM   8963  C  CE    . MET B 2 649 ? 147.476 182.354 188.888 1.00 32.26  ? 649 MET B CE    1 
ATOM   8964  N  N     . LEU B 2 650 ? 147.854 182.254 183.818 1.00 26.64  ? 650 LEU B N     1 
ATOM   8965  C  CA    . LEU B 2 650 ? 149.105 181.804 183.218 1.00 29.22  ? 650 LEU B CA    1 
ATOM   8966  C  C     . LEU B 2 650 ? 150.149 182.913 183.225 1.00 28.25  ? 650 LEU B C     1 
ATOM   8967  O  O     . LEU B 2 650 ? 151.332 182.663 183.484 1.00 26.75  ? 650 LEU B O     1 
ATOM   8968  C  CB    . LEU B 2 650 ? 148.857 181.315 181.791 1.00 24.48  ? 650 LEU B CB    1 
ATOM   8969  C  CG    . LEU B 2 650 ? 150.081 180.834 181.008 1.00 27.63  ? 650 LEU B CG    1 
ATOM   8970  C  CD1   . LEU B 2 650 ? 150.790 179.712 181.748 1.00 28.65  ? 650 LEU B CD1   1 
ATOM   8971  C  CD2   . LEU B 2 650 ? 149.687 180.393 179.606 1.00 29.16  ? 650 LEU B CD2   1 
ATOM   8972  N  N     . ARG B 2 651 ? 149.728 184.146 182.933 1.00 30.02  ? 651 ARG B N     1 
ATOM   8973  C  CA    . ARG B 2 651 ? 150.662 185.267 182.912 1.00 27.38  ? 651 ARG B CA    1 
ATOM   8974  C  C     . ARG B 2 651 ? 151.264 185.513 184.290 1.00 31.12  ? 651 ARG B C     1 
ATOM   8975  O  O     . ARG B 2 651 ? 152.469 185.758 184.415 1.00 36.61  ? 651 ARG B O     1 
ATOM   8976  C  CB    . ARG B 2 651 ? 149.953 186.523 182.405 1.00 28.01  ? 651 ARG B CB    1 
ATOM   8977  C  CG    . ARG B 2 651 ? 150.886 187.632 181.956 1.00 36.05  ? 651 ARG B CG    1 
ATOM   8978  C  CD    . ARG B 2 651 ? 150.126 188.927 181.710 1.00 37.17  ? 651 ARG B CD    1 
ATOM   8979  N  NE    . ARG B 2 651 ? 149.038 188.758 180.755 1.00 41.03  ? 651 ARG B NE    1 
ATOM   8980  C  CZ    . ARG B 2 651 ? 147.751 188.790 181.074 1.00 40.89  ? 651 ARG B CZ    1 
ATOM   8981  N  NH1   . ARG B 2 651 ? 147.352 188.994 182.318 1.00 37.94  ? 651 ARG B NH1   1 
ATOM   8982  N  NH2   . ARG B 2 651 ? 146.841 188.614 180.120 1.00 31.19  ? 651 ARG B NH2   1 
ATOM   8983  N  N     . ARG B 2 652 ? 150.437 185.453 185.337 1.00 29.64  ? 652 ARG B N     1 
ATOM   8984  C  CA    . ARG B 2 652 ? 150.938 185.676 186.690 1.00 28.16  ? 652 ARG B CA    1 
ATOM   8985  C  C     . ARG B 2 652 ? 151.859 184.545 187.132 1.00 30.10  ? 652 ARG B C     1 
ATOM   8986  O  O     . ARG B 2 652 ? 152.880 184.789 187.786 1.00 32.28  ? 652 ARG B O     1 
ATOM   8987  C  CB    . ARG B 2 652 ? 149.765 185.837 187.660 1.00 28.82  ? 652 ARG B CB    1 
ATOM   8988  C  CG    . ARG B 2 652 ? 149.934 185.116 188.989 1.00 29.15  ? 652 ARG B CG    1 
ATOM   8989  C  CD    . ARG B 2 652 ? 148.998 185.681 190.045 1.00 32.96  ? 652 ARG B CD    1 
ATOM   8990  N  NE    . ARG B 2 652 ? 149.174 185.028 191.337 1.00 40.81  ? 652 ARG B NE    1 
ATOM   8991  C  CZ    . ARG B 2 652 ? 149.694 185.613 192.407 1.00 41.09  ? 652 ARG B CZ    1 
ATOM   8992  N  NH1   . ARG B 2 652 ? 150.098 186.872 192.379 1.00 39.92  ? 652 ARG B NH1   1 
ATOM   8993  N  NH2   . ARG B 2 652 ? 149.810 184.917 193.534 1.00 40.10  ? 652 ARG B NH2   1 
ATOM   8994  N  N     . ASN B 2 653 ? 151.521 183.302 186.781 1.00 30.69  ? 653 ASN B N     1 
ATOM   8995  C  CA    . ASN B 2 653 ? 152.351 182.171 187.185 1.00 29.41  ? 653 ASN B CA    1 
ATOM   8996  C  C     . ASN B 2 653 ? 153.665 182.148 186.415 1.00 30.80  ? 653 ASN B C     1 
ATOM   8997  O  O     . ASN B 2 653 ? 154.692 181.705 186.943 1.00 31.32  ? 653 ASN B O     1 
ATOM   8998  C  CB    . ASN B 2 653 ? 151.588 180.862 186.986 1.00 27.39  ? 653 ASN B CB    1 
ATOM   8999  C  CG    . ASN B 2 653 ? 150.733 180.499 188.183 1.00 30.89  ? 653 ASN B CG    1 
ATOM   9000  O  OD1   . ASN B 2 653 ? 151.036 180.877 189.314 1.00 35.85  ? 653 ASN B OD1   1 
ATOM   9001  N  ND2   . ASN B 2 653 ? 149.656 179.762 187.940 1.00 35.63  ? 653 ASN B ND2   1 
ATOM   9002  N  N     . LEU B 2 654 ? 153.654 182.621 185.167 1.00 30.77  ? 654 LEU B N     1 
ATOM   9003  C  CA    . LEU B 2 654 ? 154.885 182.664 184.386 1.00 32.09  ? 654 LEU B CA    1 
ATOM   9004  C  C     . LEU B 2 654 ? 155.790 183.806 184.829 1.00 33.18  ? 654 LEU B C     1 
ATOM   9005  O  O     . LEU B 2 654 ? 156.984 183.809 184.511 1.00 40.53  ? 654 LEU B O     1 
ATOM   9006  C  CB    . LEU B 2 654 ? 154.558 182.794 182.898 1.00 30.63  ? 654 LEU B CB    1 
ATOM   9007  C  CG    . LEU B 2 654 ? 154.320 181.494 182.128 1.00 29.54  ? 654 LEU B CG    1 
ATOM   9008  C  CD1   . LEU B 2 654 ? 154.175 181.776 180.642 1.00 33.50  ? 654 LEU B CD1   1 
ATOM   9009  C  CD2   . LEU B 2 654 ? 155.447 180.506 182.380 1.00 26.99  ? 654 LEU B CD2   1 
ATOM   9010  N  N     . TRP B 2 655 ? 155.244 184.779 185.561 1.00 29.94  ? 655 TRP B N     1 
ATOM   9011  C  CA    . TRP B 2 655 ? 156.058 185.892 186.035 1.00 34.57  ? 655 TRP B CA    1 
ATOM   9012  C  C     . TRP B 2 655 ? 156.689 185.589 187.388 1.00 34.23  ? 655 TRP B C     1 
ATOM   9013  O  O     . TRP B 2 655 ? 157.779 186.088 187.689 1.00 42.06  ? 655 TRP B O     1 
ATOM   9014  C  CB    . TRP B 2 655 ? 155.208 187.161 186.112 1.00 33.38  ? 655 TRP B CB    1 
ATOM   9015  C  CG    . TRP B 2 655 ? 155.888 188.317 186.779 1.00 38.74  ? 655 TRP B CG    1 
ATOM   9016  C  CD1   . TRP B 2 655 ? 155.818 188.661 188.098 1.00 40.41  ? 655 TRP B CD1   1 
ATOM   9017  C  CD2   . TRP B 2 655 ? 156.734 189.290 186.155 1.00 40.69  ? 655 TRP B CD2   1 
ATOM   9018  N  NE1   . TRP B 2 655 ? 156.573 189.784 188.335 1.00 42.49  ? 655 TRP B NE1   1 
ATOM   9019  C  CE2   . TRP B 2 655 ? 157.145 190.190 187.158 1.00 42.52  ? 655 TRP B CE2   1 
ATOM   9020  C  CE3   . TRP B 2 655 ? 157.185 189.486 184.846 1.00 36.07  ? 655 TRP B CE3   1 
ATOM   9021  C  CZ2   . TRP B 2 655 ? 157.985 191.269 186.894 1.00 38.27  ? 655 TRP B CZ2   1 
ATOM   9022  C  CZ3   . TRP B 2 655 ? 158.019 190.558 184.586 1.00 36.92  ? 655 TRP B CZ3   1 
ATOM   9023  C  CH2   . TRP B 2 655 ? 158.411 191.436 185.604 1.00 40.35  ? 655 TRP B CH2   1 
ATOM   9024  N  N     . ILE B 2 656 ? 156.029 184.771 188.207 1.00 32.39  ? 656 ILE B N     1 
ATOM   9025  C  CA    . ILE B 2 656 ? 156.545 184.465 189.537 1.00 27.42  ? 656 ILE B CA    1 
ATOM   9026  C  C     . ILE B 2 656 ? 157.519 183.296 189.483 1.00 32.38  ? 656 ILE B C     1 
ATOM   9027  O  O     . ILE B 2 656 ? 158.583 183.324 190.113 1.00 36.26  ? 656 ILE B O     1 
ATOM   9028  C  CB    . ILE B 2 656 ? 155.381 184.183 190.505 1.00 31.07  ? 656 ILE B CB    1 
ATOM   9029  C  CG1   . ILE B 2 656 ? 154.524 185.436 190.692 1.00 33.20  ? 656 ILE B CG1   1 
ATOM   9030  C  CG2   . ILE B 2 656 ? 155.904 183.686 191.844 1.00 23.30  ? 656 ILE B CG2   1 
ATOM   9031  C  CD1   . ILE B 2 656 ? 153.271 185.200 191.505 1.00 31.49  ? 656 ILE B CD1   1 
ATOM   9032  N  N     . TYR B 2 657 ? 157.178 182.256 188.726 1.00 32.27  ? 657 TYR B N     1 
ATOM   9033  C  CA    . TYR B 2 657 ? 157.978 181.039 188.685 1.00 30.64  ? 657 TYR B CA    1 
ATOM   9034  C  C     . TYR B 2 657 ? 158.780 180.887 187.402 1.00 26.69  ? 657 TYR B C     1 
ATOM   9035  O  O     . TYR B 2 657 ? 159.804 180.196 187.406 1.00 31.36  ? 657 TYR B O     1 
ATOM   9036  C  CB    . TYR B 2 657 ? 157.077 179.814 188.873 1.00 25.59  ? 657 TYR B CB    1 
ATOM   9037  C  CG    . TYR B 2 657 ? 156.246 179.877 190.134 1.00 29.50  ? 657 TYR B CG    1 
ATOM   9038  C  CD1   . TYR B 2 657 ? 156.757 179.436 191.348 1.00 23.85  ? 657 TYR B CD1   1 
ATOM   9039  C  CD2   . TYR B 2 657 ? 154.957 180.392 190.115 1.00 28.31  ? 657 TYR B CD2   1 
ATOM   9040  C  CE1   . TYR B 2 657 ? 156.004 179.498 192.504 1.00 27.50  ? 657 TYR B CE1   1 
ATOM   9041  C  CE2   . TYR B 2 657 ? 154.196 180.456 191.266 1.00 25.83  ? 657 TYR B CE2   1 
ATOM   9042  C  CZ    . TYR B 2 657 ? 154.725 180.009 192.458 1.00 26.68  ? 657 TYR B CZ    1 
ATOM   9043  O  OH    . TYR B 2 657 ? 153.972 180.072 193.607 1.00 39.75  ? 657 TYR B OH    1 
ATOM   9044  N  N     . GLY B 2 658 ? 158.346 181.508 186.310 1.00 32.04  ? 658 GLY B N     1 
ATOM   9045  C  CA    . GLY B 2 658 ? 159.120 181.491 185.085 1.00 32.07  ? 658 GLY B CA    1 
ATOM   9046  C  C     . GLY B 2 658 ? 160.283 182.458 185.140 1.00 32.25  ? 658 GLY B C     1 
ATOM   9047  O  O     . GLY B 2 658 ? 161.445 182.047 185.070 1.00 37.17  ? 658 GLY B O     1 
ATOM   9048  N  N     . LEU B 2 659 ? 159.981 183.752 185.267 1.00 32.36  ? 659 LEU B N     1 
ATOM   9049  C  CA    . LEU B 2 659 ? 161.040 184.745 185.420 1.00 35.30  ? 659 LEU B CA    1 
ATOM   9050  C  C     . LEU B 2 659 ? 161.740 184.600 186.765 1.00 32.65  ? 659 LEU B C     1 
ATOM   9051  O  O     . LEU B 2 659 ? 162.961 184.769 186.857 1.00 33.71  ? 659 LEU B O     1 
ATOM   9052  C  CB    . LEU B 2 659 ? 160.471 186.154 185.260 1.00 33.94  ? 659 LEU B CB    1 
ATOM   9053  C  CG    . LEU B 2 659 ? 161.482 187.294 185.407 1.00 35.50  ? 659 LEU B CG    1 
ATOM   9054  C  CD1   . LEU B 2 659 ? 162.318 187.439 184.145 1.00 33.86  ? 659 LEU B CD1   1 
ATOM   9055  C  CD2   . LEU B 2 659 ? 160.783 188.602 185.746 1.00 34.57  ? 659 LEU B CD2   1 
ATOM   9056  N  N     . GLY B 2 660 ? 160.981 184.294 187.820 1.00 30.62  ? 660 GLY B N     1 
ATOM   9057  C  CA    . GLY B 2 660 ? 161.590 184.106 189.127 1.00 24.39  ? 660 GLY B CA    1 
ATOM   9058  C  C     . GLY B 2 660 ? 162.562 182.943 189.155 1.00 31.31  ? 660 GLY B C     1 
ATOM   9059  O  O     . GLY B 2 660 ? 163.587 182.995 189.838 1.00 36.61  ? 660 GLY B O     1 
ATOM   9060  N  N     . GLY B 2 661 ? 162.258 181.880 188.409 1.00 30.82  ? 661 GLY B N     1 
ATOM   9061  C  CA    . GLY B 2 661 ? 163.173 180.755 188.338 1.00 25.62  ? 661 GLY B CA    1 
ATOM   9062  C  C     . GLY B 2 661 ? 164.444 181.071 187.578 1.00 26.94  ? 661 GLY B C     1 
ATOM   9063  O  O     . GLY B 2 661 ? 165.461 180.395 187.755 1.00 36.14  ? 661 GLY B O     1 
ATOM   9064  N  N     . LEU B 2 662 ? 164.408 182.092 186.720 1.00 28.05  ? 662 LEU B N     1 
ATOM   9065  C  CA    . LEU B 2 662 ? 165.605 182.492 185.990 1.00 30.07  ? 662 LEU B CA    1 
ATOM   9066  C  C     . LEU B 2 662 ? 166.551 183.312 186.859 1.00 31.69  ? 662 LEU B C     1 
ATOM   9067  O  O     . LEU B 2 662 ? 167.769 183.278 186.653 1.00 39.97  ? 662 LEU B O     1 
ATOM   9068  C  CB    . LEU B 2 662 ? 165.221 183.285 184.742 1.00 31.77  ? 662 LEU B CB    1 
ATOM   9069  C  CG    . LEU B 2 662 ? 164.624 182.510 183.567 1.00 38.73  ? 662 LEU B CG    1 
ATOM   9070  C  CD1   . LEU B 2 662 ? 164.377 183.445 182.395 1.00 38.04  ? 662 LEU B CD1   1 
ATOM   9071  C  CD2   . LEU B 2 662 ? 165.529 181.360 183.160 1.00 38.18  ? 662 LEU B CD2   1 
ATOM   9072  N  N     . LEU B 2 663 ? 166.018 184.047 187.834 1.00 27.62  ? 663 LEU B N     1 
ATOM   9073  C  CA    . LEU B 2 663 ? 166.806 185.018 188.585 1.00 28.95  ? 663 LEU B CA    1 
ATOM   9074  C  C     . LEU B 2 663 ? 167.169 184.562 189.990 1.00 31.26  ? 663 LEU B C     1 
ATOM   9075  O  O     . LEU B 2 663 ? 168.199 184.995 190.518 1.00 40.84  ? 663 LEU B O     1 
ATOM   9076  C  CB    . LEU B 2 663 ? 166.052 186.349 188.678 1.00 29.73  ? 663 LEU B CB    1 
ATOM   9077  C  CG    . LEU B 2 663 ? 165.540 186.939 187.363 1.00 34.33  ? 663 LEU B CG    1 
ATOM   9078  C  CD1   . LEU B 2 663 ? 164.705 188.184 187.624 1.00 32.73  ? 663 LEU B CD1   1 
ATOM   9079  C  CD2   . LEU B 2 663 ? 166.696 187.250 186.425 1.00 34.08  ? 663 LEU B CD2   1 
ATOM   9080  N  N     . VAL B 2 664 ? 166.349 183.713 190.614 1.00 29.27  ? 664 VAL B N     1 
ATOM   9081  C  CA    . VAL B 2 664 ? 166.633 183.277 191.984 1.00 25.79  ? 664 VAL B CA    1 
ATOM   9082  C  C     . VAL B 2 664 ? 167.965 182.542 192.098 1.00 31.47  ? 664 VAL B C     1 
ATOM   9083  O  O     . VAL B 2 664 ? 168.749 182.872 193.003 1.00 34.75  ? 664 VAL B O     1 
ATOM   9084  C  CB    . VAL B 2 664 ? 165.452 182.457 192.533 1.00 29.22  ? 664 VAL B CB    1 
ATOM   9085  C  CG1   . VAL B 2 664 ? 165.892 181.610 193.717 1.00 29.52  ? 664 VAL B CG1   1 
ATOM   9086  C  CG2   . VAL B 2 664 ? 164.312 183.378 192.935 1.00 32.33  ? 664 VAL B CG2   1 
ATOM   9087  N  N     . PRO B 2 665 ? 168.287 181.555 191.249 1.00 31.11  ? 665 PRO B N     1 
ATOM   9088  C  CA    . PRO B 2 665 ? 169.582 180.869 191.408 1.00 23.11  ? 665 PRO B CA    1 
ATOM   9089  C  C     . PRO B 2 665 ? 170.784 181.785 191.254 1.00 23.02  ? 665 PRO B C     1 
ATOM   9090  O  O     . PRO B 2 665 ? 171.818 181.537 191.886 1.00 30.64  ? 665 PRO B O     1 
ATOM   9091  C  CB    . PRO B 2 665 ? 169.550 179.791 190.316 1.00 25.57  ? 665 PRO B CB    1 
ATOM   9092  C  CG    . PRO B 2 665 ? 168.122 179.611 189.991 1.00 27.04  ? 665 PRO B CG    1 
ATOM   9093  C  CD    . PRO B 2 665 ? 167.496 180.953 190.161 1.00 24.62  ? 665 PRO B CD    1 
ATOM   9094  N  N     . PHE B 2 666 ? 170.688 182.830 190.428 1.00 32.11  ? 666 PHE B N     1 
ATOM   9095  C  CA    . PHE B 2 666 ? 171.804 183.761 190.289 1.00 30.94  ? 666 PHE B CA    1 
ATOM   9096  C  C     . PHE B 2 666 ? 172.119 184.441 191.615 1.00 30.40  ? 666 PHE B C     1 
ATOM   9097  O  O     . PHE B 2 666 ? 173.288 184.556 192.001 1.00 36.01  ? 666 PHE B O     1 
ATOM   9098  C  CB    . PHE B 2 666 ? 171.492 184.803 189.215 1.00 25.20  ? 666 PHE B CB    1 
ATOM   9099  C  CG    . PHE B 2 666 ? 171.752 184.329 187.814 1.00 31.16  ? 666 PHE B CG    1 
ATOM   9100  C  CD1   . PHE B 2 666 ? 173.046 184.165 187.352 1.00 28.09  ? 666 PHE B CD1   1 
ATOM   9101  C  CD2   . PHE B 2 666 ? 170.701 184.055 186.957 1.00 26.68  ? 666 PHE B CD2   1 
ATOM   9102  C  CE1   . PHE B 2 666 ? 173.286 183.731 186.063 1.00 30.20  ? 666 PHE B CE1   1 
ATOM   9103  C  CE2   . PHE B 2 666 ? 170.934 183.620 185.667 1.00 24.27  ? 666 PHE B CE2   1 
ATOM   9104  C  CZ    . PHE B 2 666 ? 172.228 183.459 185.219 1.00 28.00  ? 666 PHE B CZ    1 
ATOM   9105  N  N     . ILE B 2 667 ? 171.087 184.898 192.326 1.00 23.94  ? 667 ILE B N     1 
ATOM   9106  C  CA    . ILE B 2 667 ? 171.297 185.500 193.638 1.00 29.05  ? 667 ILE B CA    1 
ATOM   9107  C  C     . ILE B 2 667 ? 171.697 184.440 194.656 1.00 33.18  ? 667 ILE B C     1 
ATOM   9108  O  O     . ILE B 2 667 ? 172.608 184.651 195.465 1.00 32.19  ? 667 ILE B O     1 
ATOM   9109  C  CB    . ILE B 2 667 ? 170.036 186.265 194.079 1.00 27.98  ? 667 ILE B CB    1 
ATOM   9110  C  CG1   . ILE B 2 667 ? 169.695 187.360 193.068 1.00 30.98  ? 667 ILE B CG1   1 
ATOM   9111  C  CG2   . ILE B 2 667 ? 170.227 186.860 195.465 1.00 27.13  ? 667 ILE B CG2   1 
ATOM   9112  C  CD1   . ILE B 2 667 ? 168.234 187.752 193.062 1.00 33.17  ? 667 ILE B CD1   1 
ATOM   9113  N  N     . GLY B 2 668 ? 171.030 183.284 194.629 1.00 30.29  ? 668 GLY B N     1 
ATOM   9114  C  CA    . GLY B 2 668 ? 171.285 182.266 195.637 1.00 24.72  ? 668 GLY B CA    1 
ATOM   9115  C  C     . GLY B 2 668 ? 172.688 181.694 195.569 1.00 23.47  ? 668 GLY B C     1 
ATOM   9116  O  O     . GLY B 2 668 ? 173.341 181.507 196.598 1.00 27.95  ? 668 GLY B O     1 
ATOM   9117  N  N     . ILE B 2 669 ? 173.169 181.402 194.359 1.00 24.29  ? 669 ILE B N     1 
ATOM   9118  C  CA    . ILE B 2 669 ? 174.520 180.869 194.209 1.00 28.37  ? 669 ILE B CA    1 
ATOM   9119  C  C     . ILE B 2 669 ? 175.555 181.916 194.604 1.00 24.88  ? 669 ILE B C     1 
ATOM   9120  O  O     . ILE B 2 669 ? 176.567 181.598 195.240 1.00 34.16  ? 669 ILE B O     1 
ATOM   9121  C  CB    . ILE B 2 669 ? 174.737 180.359 192.771 1.00 28.93  ? 669 ILE B CB    1 
ATOM   9122  C  CG1   . ILE B 2 669 ? 173.885 179.114 192.514 1.00 25.42  ? 669 ILE B CG1   1 
ATOM   9123  C  CG2   . ILE B 2 669 ? 176.205 180.052 192.519 1.00 22.90  ? 669 ILE B CG2   1 
ATOM   9124  C  CD1   . ILE B 2 669 ? 173.603 178.855 191.051 1.00 23.57  ? 669 ILE B CD1   1 
ATOM   9125  N  N     . LYS B 2 670 ? 175.315 183.179 194.244 1.00 25.04  ? 670 LYS B N     1 
ATOM   9126  C  CA    . LYS B 2 670 ? 176.253 184.243 194.588 1.00 28.88  ? 670 LYS B CA    1 
ATOM   9127  C  C     . LYS B 2 670 ? 176.360 184.425 196.098 1.00 28.94  ? 670 LYS B C     1 
ATOM   9128  O  O     . LYS B 2 670 ? 177.462 184.602 196.631 1.00 31.35  ? 670 LYS B O     1 
ATOM   9129  C  CB    . LYS B 2 670 ? 175.828 185.551 193.920 1.00 28.85  ? 670 LYS B CB    1 
ATOM   9130  C  CG    . LYS B 2 670 ? 176.825 186.689 194.074 1.00 28.55  ? 670 LYS B CG    1 
ATOM   9131  C  CD    . LYS B 2 670 ? 178.240 186.239 193.746 1.00 27.92  ? 670 LYS B CD    1 
ATOM   9132  C  CE    . LYS B 2 670 ? 179.219 187.398 193.823 1.00 31.42  ? 670 LYS B CE    1 
ATOM   9133  N  NZ    . LYS B 2 670 ? 180.598 186.986 193.441 1.00 31.15  ? 670 LYS B NZ    1 
ATOM   9134  N  N     . VAL B 2 671 ? 175.227 184.391 196.803 1.00 24.22  ? 671 VAL B N     1 
ATOM   9135  C  CA    . VAL B 2 671 ? 175.248 184.546 198.255 1.00 29.39  ? 671 VAL B CA    1 
ATOM   9136  C  C     . VAL B 2 671 ? 175.972 183.377 198.910 1.00 30.18  ? 671 VAL B C     1 
ATOM   9137  O  O     . VAL B 2 671 ? 176.772 183.565 199.835 1.00 36.00  ? 671 VAL B O     1 
ATOM   9138  C  CB    . VAL B 2 671 ? 173.815 184.704 198.796 1.00 27.73  ? 671 VAL B CB    1 
ATOM   9139  C  CG1   . VAL B 2 671 ? 173.810 184.655 200.315 1.00 31.65  ? 671 VAL B CG1   1 
ATOM   9140  C  CG2   . VAL B 2 671 ? 173.206 186.008 198.307 1.00 29.50  ? 671 VAL B CG2   1 
ATOM   9141  N  N     . ILE B 2 672 ? 175.704 182.154 198.447 1.00 24.69  ? 672 ILE B N     1 
ATOM   9142  C  CA    . ILE B 2 672 ? 176.371 180.981 199.006 1.00 28.73  ? 672 ILE B CA    1 
ATOM   9143  C  C     . ILE B 2 672 ? 177.872 181.048 198.753 1.00 30.51  ? 672 ILE B C     1 
ATOM   9144  O  O     . ILE B 2 672 ? 178.681 180.746 199.640 1.00 34.19  ? 672 ILE B O     1 
ATOM   9145  C  CB    . ILE B 2 672 ? 175.753 179.693 198.431 1.00 29.18  ? 672 ILE B CB    1 
ATOM   9146  C  CG1   . ILE B 2 672 ? 174.342 179.488 198.987 1.00 24.22  ? 672 ILE B CG1   1 
ATOM   9147  C  CG2   . ILE B 2 672 ? 176.629 178.489 198.743 1.00 21.27  ? 672 ILE B CG2   1 
ATOM   9148  C  CD1   . ILE B 2 672 ? 173.511 178.510 198.191 1.00 27.58  ? 672 ILE B CD1   1 
ATOM   9149  N  N     . ASP B 2 673 ? 178.268 181.447 197.542 1.00 27.88  ? 673 ASP B N     1 
ATOM   9150  C  CA    . ASP B 2 673 ? 179.687 181.577 197.229 1.00 26.60  ? 673 ASP B CA    1 
ATOM   9151  C  C     . ASP B 2 673 ? 180.351 182.637 198.099 1.00 29.65  ? 673 ASP B C     1 
ATOM   9152  O  O     . ASP B 2 673 ? 181.482 182.451 198.562 1.00 37.00  ? 673 ASP B O     1 
ATOM   9153  C  CB    . ASP B 2 673 ? 179.869 181.906 195.748 1.00 29.44  ? 673 ASP B CB    1 
ATOM   9154  C  CG    . ASP B 2 673 ? 181.233 181.505 195.224 1.00 35.10  ? 673 ASP B CG    1 
ATOM   9155  O  OD1   . ASP B 2 673 ? 182.171 182.324 195.313 1.00 39.13  ? 673 ASP B OD1   1 
ATOM   9156  O  OD2   . ASP B 2 673 ? 181.367 180.370 194.720 1.00 38.62  ? 673 ASP B OD2   1 
ATOM   9157  N  N     . LEU B 2 674 ? 179.666 183.760 198.325 1.00 28.85  ? 674 LEU B N     1 
ATOM   9158  C  CA    . LEU B 2 674 ? 180.213 184.800 199.190 1.00 32.74  ? 674 LEU B CA    1 
ATOM   9159  C  C     . LEU B 2 674 ? 180.358 184.306 200.624 1.00 34.63  ? 674 LEU B C     1 
ATOM   9160  O  O     . LEU B 2 674 ? 181.346 184.617 201.299 1.00 38.74  ? 674 LEU B O     1 
ATOM   9161  C  CB    . LEU B 2 674 ? 179.328 186.045 199.137 1.00 31.39  ? 674 LEU B CB    1 
ATOM   9162  C  CG    . LEU B 2 674 ? 179.487 186.939 197.907 1.00 34.66  ? 674 LEU B CG    1 
ATOM   9163  C  CD1   . LEU B 2 674 ? 178.408 188.010 197.879 1.00 31.66  ? 674 LEU B CD1   1 
ATOM   9164  C  CD2   . LEU B 2 674 ? 180.872 187.566 197.874 1.00 35.56  ? 674 LEU B CD2   1 
ATOM   9165  N  N     . LEU B 2 675 ? 179.376 183.542 201.110 1.00 29.36  ? 675 LEU B N     1 
ATOM   9166  C  CA    . LEU B 2 675 ? 179.452 183.012 202.468 1.00 36.10  ? 675 LEU B CA    1 
ATOM   9167  C  C     . LEU B 2 675 ? 180.614 182.039 202.619 1.00 38.87  ? 675 LEU B C     1 
ATOM   9168  O  O     . LEU B 2 675 ? 181.313 182.050 203.639 1.00 44.10  ? 675 LEU B O     1 
ATOM   9169  C  CB    . LEU B 2 675 ? 178.133 182.334 202.841 1.00 34.49  ? 675 LEU B CB    1 
ATOM   9170  C  CG    . LEU B 2 675 ? 176.972 183.263 203.202 1.00 39.49  ? 675 LEU B CG    1 
ATOM   9171  C  CD1   . LEU B 2 675 ? 175.714 182.459 203.491 1.00 35.47  ? 675 LEU B CD1   1 
ATOM   9172  C  CD2   . LEU B 2 675 ? 177.337 184.140 204.389 1.00 39.34  ? 675 LEU B CD2   1 
ATOM   9173  N  N     . LEU B 2 676 ? 180.832 181.184 201.616 1.00 38.27  ? 676 LEU B N     1 
ATOM   9174  C  CA    . LEU B 2 676 ? 181.945 180.241 201.674 1.00 36.62  ? 676 LEU B CA    1 
ATOM   9175  C  C     . LEU B 2 676 ? 183.283 180.969 201.703 1.00 36.17  ? 676 LEU B C     1 
ATOM   9176  O  O     . LEU B 2 676 ? 184.200 180.569 202.429 1.00 41.05  ? 676 LEU B O     1 
ATOM   9177  C  CB    . LEU B 2 676 ? 181.882 179.281 200.487 1.00 35.29  ? 676 LEU B CB    1 
ATOM   9178  C  CG    . LEU B 2 676 ? 180.743 178.260 200.477 1.00 36.69  ? 676 LEU B CG    1 
ATOM   9179  C  CD1   . LEU B 2 676 ? 180.420 177.836 199.054 1.00 33.98  ? 676 LEU B CD1   1 
ATOM   9180  C  CD2   . LEU B 2 676 ? 181.094 177.053 201.332 1.00 38.11  ? 676 LEU B CD2   1 
ATOM   9181  N  N     . THR B 2 677 ? 183.416 182.034 200.909 1.00 39.21  ? 677 THR B N     1 
ATOM   9182  C  CA    . THR B 2 677 ? 184.657 182.803 200.898 1.00 41.62  ? 677 THR B CA    1 
ATOM   9183  C  C     . THR B 2 677 ? 184.902 183.478 202.242 1.00 38.96  ? 677 THR B C     1 
ATOM   9184  O  O     . THR B 2 677 ? 186.038 183.513 202.730 1.00 44.38  ? 677 THR B O     1 
ATOM   9185  C  CB    . THR B 2 677 ? 184.620 183.842 199.777 1.00 39.77  ? 677 THR B CB    1 
ATOM   9186  O  OG1   . THR B 2 677 ? 184.140 183.231 198.573 1.00 37.99  ? 677 THR B OG1   1 
ATOM   9187  C  CG2   . THR B 2 677 ? 186.009 184.411 199.532 1.00 38.74  ? 677 THR B CG2   1 
ATOM   9188  N  N     . VAL B 2 678 ? 183.848 184.026 202.853 1.00 41.60  ? 678 VAL B N     1 
ATOM   9189  C  CA    . VAL B 2 678 ? 183.997 184.704 204.138 1.00 44.94  ? 678 VAL B CA    1 
ATOM   9190  C  C     . VAL B 2 678 ? 184.412 183.716 205.221 1.00 46.52  ? 678 VAL B C     1 
ATOM   9191  O  O     . VAL B 2 678 ? 185.307 183.996 206.029 1.00 49.12  ? 678 VAL B O     1 
ATOM   9192  C  CB    . VAL B 2 678 ? 182.693 185.440 204.503 1.00 44.57  ? 678 VAL B CB    1 
ATOM   9193  C  CG1   . VAL B 2 678 ? 182.537 185.552 206.013 1.00 46.82  ? 678 VAL B CG1   1 
ATOM   9194  C  CG2   . VAL B 2 678 ? 182.663 186.816 203.857 1.00 44.14  ? 678 VAL B CG2   1 
ATOM   9195  N  N     . CYS B 2 679 ? 183.781 182.540 205.249 1.00 49.30  ? 679 CYS B N     1 
ATOM   9196  C  CA    . CYS B 2 679 ? 184.100 181.537 206.257 1.00 48.38  ? 679 CYS B CA    1 
ATOM   9197  C  C     . CYS B 2 679 ? 185.464 180.895 206.046 1.00 49.64  ? 679 CYS B C     1 
ATOM   9198  O  O     . CYS B 2 679 ? 185.942 180.192 206.943 1.00 54.63  ? 679 CYS B O     1 
ATOM   9199  C  CB    . CYS B 2 679 ? 183.020 180.453 206.279 1.00 50.17  ? 679 CYS B CB    1 
ATOM   9200  S  SG    . CYS B 2 679 ? 181.370 181.050 206.715 1.00 61.87  ? 679 CYS B SG    1 
ATOM   9201  N  N     . GLY B 2 680 ? 186.098 181.112 204.896 1.00 49.78  ? 680 GLY B N     1 
ATOM   9202  C  CA    . GLY B 2 680 ? 187.400 180.539 204.631 1.00 48.02  ? 680 GLY B CA    1 
ATOM   9203  C  C     . GLY B 2 680 ? 187.389 179.096 204.184 1.00 50.80  ? 680 GLY B C     1 
ATOM   9204  O  O     . GLY B 2 680 ? 188.462 178.489 204.086 1.00 53.88  ? 680 GLY B O     1 
ATOM   9205  N  N     . LEU B 2 681 ? 186.214 178.524 203.912 1.00 49.93  ? 681 LEU B N     1 
ATOM   9206  C  CA    . LEU B 2 681 ? 186.154 177.137 203.464 1.00 48.79  ? 681 LEU B CA    1 
ATOM   9207  C  C     . LEU B 2 681 ? 186.703 176.976 202.053 1.00 48.72  ? 681 LEU B C     1 
ATOM   9208  O  O     . LEU B 2 681 ? 187.263 175.924 201.724 1.00 53.28  ? 681 LEU B O     1 
ATOM   9209  C  CB    . LEU B 2 681 ? 184.717 176.623 203.537 1.00 48.42  ? 681 LEU B CB    1 
ATOM   9210  C  CG    . LEU B 2 681 ? 183.982 176.859 204.858 1.00 49.16  ? 681 LEU B CG    1 
ATOM   9211  C  CD1   . LEU B 2 681 ? 182.535 176.406 204.756 1.00 46.89  ? 681 LEU B CD1   1 
ATOM   9212  C  CD2   . LEU B 2 681 ? 184.689 176.148 206.001 1.00 48.67  ? 681 LEU B CD2   1 
ATOM   9213  N  N     . VAL B 2 682 ? 186.554 177.994 201.212 1.00 48.11  ? 682 VAL B N     1 
ATOM   9214  C  CA    . VAL B 2 682 ? 187.041 177.933 199.841 1.00 49.04  ? 682 VAL B CA    1 
ATOM   9215  C  C     . VAL B 2 682 ? 188.118 178.986 199.613 1.00 47.95  ? 682 VAL B C     1 
ATOM   9216  O  O     . VAL B 2 682 ? 188.219 179.958 200.362 1.00 56.10  ? 682 VAL B O     1 
ATOM   9217  C  CB    . VAL B 2 682 ? 185.892 178.107 198.836 1.00 48.46  ? 682 VAL B CB    1 
ATOM   9218  C  CG1   . VAL B 2 682 ? 184.858 177.006 199.016 1.00 45.68  ? 682 VAL B CG1   1 
ATOM   9219  C  CG2   . VAL B 2 682 ? 185.254 179.479 198.994 1.00 46.55  ? 682 VAL B CG2   1 
ATOM   9220  N  N     . GLY C 3 3   ? 147.640 143.966 150.263 1.00 45.93  ? 3   GLY C N     1 
ATOM   9221  C  CA    . GLY C 3 3   ? 147.982 145.374 150.189 1.00 44.73  ? 3   GLY C CA    1 
ATOM   9222  C  C     . GLY C 3 3   ? 149.286 145.638 149.462 1.00 49.95  ? 3   GLY C C     1 
ATOM   9223  O  O     . GLY C 3 3   ? 149.826 146.743 149.519 1.00 49.47  ? 3   GLY C O     1 
ATOM   9224  N  N     . LEU C 3 4   ? 149.798 144.615 148.779 1.00 46.42  ? 4   LEU C N     1 
ATOM   9225  C  CA    . LEU C 3 4   ? 151.044 144.740 148.034 1.00 38.97  ? 4   LEU C CA    1 
ATOM   9226  C  C     . LEU C 3 4   ? 150.853 145.433 146.690 1.00 41.79  ? 4   LEU C C     1 
ATOM   9227  O  O     . LEU C 3 4   ? 151.747 146.155 146.236 1.00 44.64  ? 4   LEU C O     1 
ATOM   9228  C  CB    . LEU C 3 4   ? 151.670 143.359 147.819 1.00 43.62  ? 4   LEU C CB    1 
ATOM   9229  C  CG    . LEU C 3 4   ? 153.198 143.302 147.800 1.00 43.33  ? 4   LEU C CG    1 
ATOM   9230  C  CD1   . LEU C 3 4   ? 153.774 143.882 149.082 1.00 43.93  ? 4   LEU C CD1   1 
ATOM   9231  C  CD2   . LEU C 3 4   ? 153.679 141.875 147.588 1.00 43.03  ? 4   LEU C CD2   1 
ATOM   9232  N  N     . ARG C 3 5   ? 149.708 145.221 146.041 1.00 39.95  ? 5   ARG C N     1 
ATOM   9233  C  CA    . ARG C 3 5   ? 149.465 145.851 144.744 1.00 39.19  ? 5   ARG C CA    1 
ATOM   9234  C  C     . ARG C 3 5   ? 149.435 147.374 144.821 1.00 38.82  ? 5   ARG C C     1 
ATOM   9235  O  O     . ARG C 3 5   ? 150.078 148.020 143.976 1.00 40.93  ? 5   ARG C O     1 
ATOM   9236  C  CB    . ARG C 3 5   ? 148.178 145.290 144.131 1.00 38.61  ? 5   ARG C CB    1 
ATOM   9237  C  CG    . ARG C 3 5   ? 147.905 145.771 142.713 1.00 39.77  ? 5   ARG C CG    1 
ATOM   9238  C  CD    . ARG C 3 5   ? 146.421 145.997 142.474 1.00 40.23  ? 5   ARG C CD    1 
ATOM   9239  N  NE    . ARG C 3 5   ? 146.177 146.803 141.284 1.00 41.71  ? 5   ARG C NE    1 
ATOM   9240  C  CZ    . ARG C 3 5   ? 145.093 146.712 140.526 1.00 41.82  ? 5   ARG C CZ    1 
ATOM   9241  N  NH1   . ARG C 3 5   ? 144.124 145.856 140.806 1.00 41.75  ? 5   ARG C NH1   1 
ATOM   9242  N  NH2   . ARG C 3 5   ? 144.978 147.499 139.460 1.00 40.68  ? 5   ARG C NH2   1 
ATOM   9243  N  N     . PRO C 3 6   ? 148.720 148.011 145.761 1.00 40.70  ? 6   PRO C N     1 
ATOM   9244  C  CA    . PRO C 3 6   ? 148.797 149.481 145.836 1.00 35.80  ? 6   PRO C CA    1 
ATOM   9245  C  C     . PRO C 3 6   ? 150.196 150.000 146.117 1.00 32.28  ? 6   PRO C C     1 
ATOM   9246  O  O     . PRO C 3 6   ? 150.572 151.062 145.606 1.00 33.77  ? 6   PRO C O     1 
ATOM   9247  C  CB    . PRO C 3 6   ? 147.823 149.826 146.972 1.00 33.77  ? 6   PRO C CB    1 
ATOM   9248  C  CG    . PRO C 3 6   ? 146.906 148.662 147.056 1.00 35.77  ? 6   PRO C CG    1 
ATOM   9249  C  CD    . PRO C 3 6   ? 147.753 147.475 146.736 1.00 37.08  ? 6   PRO C CD    1 
ATOM   9250  N  N     . ALA C 3 7   ? 150.982 149.278 146.920 1.00 33.13  ? 7   ALA C N     1 
ATOM   9251  C  CA    . ALA C 3 7   ? 152.333 149.732 147.234 1.00 24.72  ? 7   ALA C CA    1 
ATOM   9252  C  C     . ALA C 3 7   ? 153.243 149.658 146.015 1.00 28.20  ? 7   ALA C C     1 
ATOM   9253  O  O     . ALA C 3 7   ? 153.997 150.599 145.739 1.00 29.11  ? 7   ALA C O     1 
ATOM   9254  C  CB    . ALA C 3 7   ? 152.909 148.906 148.384 1.00 26.83  ? 7   ALA C CB    1 
ATOM   9255  N  N     . LEU C 3 8   ? 153.192 148.547 145.278 1.00 31.69  ? 8   LEU C N     1 
ATOM   9256  C  CA    . LEU C 3 8   ? 154.050 148.392 144.108 1.00 28.91  ? 8   LEU C CA    1 
ATOM   9257  C  C     . LEU C 3 8   ? 153.636 149.333 142.984 1.00 27.12  ? 8   LEU C C     1 
ATOM   9258  O  O     . LEU C 3 8   ? 154.492 149.898 142.293 1.00 28.82  ? 8   LEU C O     1 
ATOM   9259  C  CB    . LEU C 3 8   ? 154.024 146.941 143.629 1.00 31.40  ? 8   LEU C CB    1 
ATOM   9260  C  CG    . LEU C 3 8   ? 155.110 146.015 144.178 1.00 34.47  ? 8   LEU C CG    1 
ATOM   9261  C  CD1   . LEU C 3 8   ? 155.156 144.717 143.387 1.00 35.81  ? 8   LEU C CD1   1 
ATOM   9262  C  CD2   . LEU C 3 8   ? 156.465 146.703 144.159 1.00 31.46  ? 8   LEU C CD2   1 
ATOM   9263  N  N     . SER C 3 9   ? 152.329 149.516 142.785 1.00 25.85  ? 9   SER C N     1 
ATOM   9264  C  CA    . SER C 3 9   ? 151.862 150.339 141.675 1.00 25.14  ? 9   SER C CA    1 
ATOM   9265  C  C     . SER C 3 9   ? 152.122 151.818 141.930 1.00 30.86  ? 9   SER C C     1 
ATOM   9266  O  O     . SER C 3 9   ? 152.402 152.573 140.992 1.00 34.91  ? 9   SER C O     1 
ATOM   9267  C  CB    . SER C 3 9   ? 150.374 150.093 141.427 1.00 29.15  ? 9   SER C CB    1 
ATOM   9268  O  OG    . SER C 3 9   ? 150.105 148.711 141.270 1.00 41.40  ? 9   SER C OG    1 
ATOM   9269  N  N     . THR C 3 10  ? 152.044 152.250 143.191 1.00 24.94  ? 10  THR C N     1 
ATOM   9270  C  CA    . THR C 3 10  ? 152.269 153.659 143.497 1.00 21.75  ? 10  THR C CA    1 
ATOM   9271  C  C     . THR C 3 10  ? 153.742 154.023 143.361 1.00 21.24  ? 10  THR C C     1 
ATOM   9272  O  O     . THR C 3 10  ? 154.080 155.088 142.832 1.00 29.05  ? 10  THR C O     1 
ATOM   9273  C  CB    . THR C 3 10  ? 151.767 153.981 144.905 1.00 26.55  ? 10  THR C CB    1 
ATOM   9274  O  OG1   . THR C 3 10  ? 150.411 153.537 145.045 1.00 30.44  ? 10  THR C OG1   1 
ATOM   9275  C  CG2   . THR C 3 10  ? 151.832 155.478 145.167 1.00 24.14  ? 10  THR C CG2   1 
ATOM   9276  N  N     . PHE C 3 11  ? 154.634 153.145 143.826 1.00 23.00  ? 11  PHE C N     1 
ATOM   9277  C  CA    . PHE C 3 11  ? 156.062 153.431 143.746 1.00 21.71  ? 11  PHE C CA    1 
ATOM   9278  C  C     . PHE C 3 11  ? 156.552 153.412 142.303 1.00 17.24  ? 11  PHE C C     1 
ATOM   9279  O  O     . PHE C 3 11  ? 157.324 154.287 141.894 1.00 24.09  ? 11  PHE C O     1 
ATOM   9280  C  CB    . PHE C 3 11  ? 156.845 152.424 144.589 1.00 17.06  ? 11  PHE C CB    1 
ATOM   9281  C  CG    . PHE C 3 11  ? 158.332 152.494 144.392 1.00 16.14  ? 11  PHE C CG    1 
ATOM   9282  C  CD1   . PHE C 3 11  ? 159.075 153.502 144.982 1.00 17.75  ? 11  PHE C CD1   1 
ATOM   9283  C  CD2   . PHE C 3 11  ? 158.987 151.555 143.613 1.00 18.62  ? 11  PHE C CD2   1 
ATOM   9284  C  CE1   . PHE C 3 11  ? 160.443 153.570 144.803 1.00 24.21  ? 11  PHE C CE1   1 
ATOM   9285  C  CE2   . PHE C 3 11  ? 160.355 151.618 143.429 1.00 23.06  ? 11  PHE C CE2   1 
ATOM   9286  C  CZ    . PHE C 3 11  ? 161.083 152.628 144.025 1.00 22.98  ? 11  PHE C CZ    1 
ATOM   9287  N  N     . ILE C 3 12  ? 156.117 152.422 141.521 1.00 22.16  ? 12  ILE C N     1 
ATOM   9288  C  CA    . ILE C 3 12  ? 156.571 152.309 140.138 1.00 22.00  ? 12  ILE C CA    1 
ATOM   9289  C  C     . ILE C 3 12  ? 156.058 153.478 139.305 1.00 17.88  ? 12  ILE C C     1 
ATOM   9290  O  O     . ILE C 3 12  ? 156.806 154.074 138.521 1.00 26.29  ? 12  ILE C O     1 
ATOM   9291  C  CB    . ILE C 3 12  ? 156.141 150.954 139.547 1.00 23.84  ? 12  ILE C CB    1 
ATOM   9292  C  CG1   . ILE C 3 12  ? 157.019 149.831 140.101 1.00 21.16  ? 12  ILE C CG1   1 
ATOM   9293  C  CG2   . ILE C 3 12  ? 156.211 150.981 138.028 1.00 15.95  ? 12  ILE C CG2   1 
ATOM   9294  C  CD1   . ILE C 3 12  ? 156.431 148.450 139.915 1.00 25.15  ? 12  ILE C CD1   1 
ATOM   9295  N  N     . PHE C 3 13  ? 154.778 153.827 139.461 1.00 22.65  ? 13  PHE C N     1 
ATOM   9296  C  CA    . PHE C 3 13  ? 154.217 154.934 138.692 1.00 21.59  ? 13  PHE C CA    1 
ATOM   9297  C  C     . PHE C 3 13  ? 154.887 156.254 139.053 1.00 17.11  ? 13  PHE C C     1 
ATOM   9298  O  O     . PHE C 3 13  ? 155.200 157.061 138.171 1.00 21.24  ? 13  PHE C O     1 
ATOM   9299  C  CB    . PHE C 3 13  ? 152.708 155.021 138.916 1.00 15.20  ? 13  PHE C CB    1 
ATOM   9300  C  CG    . PHE C 3 13  ? 152.075 156.237 138.304 1.00 24.20  ? 13  PHE C CG    1 
ATOM   9301  C  CD1   . PHE C 3 13  ? 151.958 156.354 136.929 1.00 22.63  ? 13  PHE C CD1   1 
ATOM   9302  C  CD2   . PHE C 3 13  ? 151.602 157.265 139.101 1.00 19.85  ? 13  PHE C CD2   1 
ATOM   9303  C  CE1   . PHE C 3 13  ? 151.378 157.471 136.362 1.00 22.77  ? 13  PHE C CE1   1 
ATOM   9304  C  CE2   . PHE C 3 13  ? 151.022 158.386 138.539 1.00 17.92  ? 13  PHE C CE2   1 
ATOM   9305  C  CZ    . PHE C 3 13  ? 150.910 158.489 137.168 1.00 21.44  ? 13  PHE C CZ    1 
ATOM   9306  N  N     . LEU C 3 14  ? 155.115 156.492 140.347 1.00 21.80  ? 14  LEU C N     1 
ATOM   9307  C  CA    . LEU C 3 14  ? 155.771 157.727 140.762 1.00 17.17  ? 14  LEU C CA    1 
ATOM   9308  C  C     . LEU C 3 14  ? 157.232 157.757 140.334 1.00 17.63  ? 14  LEU C C     1 
ATOM   9309  O  O     . LEU C 3 14  ? 157.761 158.828 140.016 1.00 23.42  ? 14  LEU C O     1 
ATOM   9310  C  CB    . LEU C 3 14  ? 155.652 157.905 142.276 1.00 17.07  ? 14  LEU C CB    1 
ATOM   9311  C  CG    . LEU C 3 14  ? 154.299 158.413 142.780 1.00 24.39  ? 14  LEU C CG    1 
ATOM   9312  C  CD1   . LEU C 3 14  ? 154.347 158.693 144.274 1.00 17.23  ? 14  LEU C CD1   1 
ATOM   9313  C  CD2   . LEU C 3 14  ? 153.867 159.653 142.011 1.00 22.03  ? 14  LEU C CD2   1 
ATOM   9314  N  N     . LEU C 3 15  ? 157.899 156.600 140.323 1.00 13.00  ? 15  LEU C N     1 
ATOM   9315  C  CA    . LEU C 3 15  ? 159.272 156.541 139.834 1.00 18.79  ? 15  LEU C CA    1 
ATOM   9316  C  C     . LEU C 3 15  ? 159.346 156.910 138.357 1.00 22.30  ? 15  LEU C C     1 
ATOM   9317  O  O     . LEU C 3 15  ? 160.253 157.635 137.934 1.00 26.81  ? 15  LEU C O     1 
ATOM   9318  C  CB    . LEU C 3 15  ? 159.852 155.146 140.072 1.00 22.91  ? 15  LEU C CB    1 
ATOM   9319  C  CG    . LEU C 3 15  ? 160.970 154.673 139.139 1.00 28.80  ? 15  LEU C CG    1 
ATOM   9320  C  CD1   . LEU C 3 15  ? 162.297 155.311 139.515 1.00 22.26  ? 15  LEU C CD1   1 
ATOM   9321  C  CD2   . LEU C 3 15  ? 161.076 153.156 139.156 1.00 25.94  ? 15  LEU C CD2   1 
ATOM   9322  N  N     . LEU C 3 16  ? 158.397 156.418 137.557 1.00 17.12  ? 16  LEU C N     1 
ATOM   9323  C  CA    . LEU C 3 16  ? 158.382 156.749 136.136 1.00 17.47  ? 16  LEU C CA    1 
ATOM   9324  C  C     . LEU C 3 16  ? 158.079 158.224 135.900 1.00 16.74  ? 16  LEU C C     1 
ATOM   9325  O  O     . LEU C 3 16  ? 158.678 158.842 135.013 1.00 25.31  ? 16  LEU C O     1 
ATOM   9326  C  CB    . LEU C 3 16  ? 157.363 155.876 135.405 1.00 19.62  ? 16  LEU C CB    1 
ATOM   9327  C  CG    . LEU C 3 16  ? 157.708 154.390 135.289 1.00 26.62  ? 16  LEU C CG    1 
ATOM   9328  C  CD1   . LEU C 3 16  ? 156.589 153.628 134.596 1.00 24.30  ? 16  LEU C CD1   1 
ATOM   9329  C  CD2   . LEU C 3 16  ? 159.025 154.201 134.554 1.00 23.49  ? 16  LEU C CD2   1 
ATOM   9330  N  N     . ILE C 3 17  ? 157.156 158.800 136.670 1.00 12.11  ? 17  ILE C N     1 
ATOM   9331  C  CA    . ILE C 3 17  ? 156.788 160.199 136.478 1.00 18.45  ? 17  ILE C CA    1 
ATOM   9332  C  C     . ILE C 3 17  ? 157.926 161.123 136.895 1.00 18.26  ? 17  ILE C C     1 
ATOM   9333  O  O     . ILE C 3 17  ? 158.302 162.042 136.159 1.00 19.50  ? 17  ILE C O     1 
ATOM   9334  C  CB    . ILE C 3 17  ? 155.493 160.519 137.246 1.00 21.32  ? 17  ILE C CB    1 
ATOM   9335  C  CG1   . ILE C 3 17  ? 154.301 159.804 136.607 1.00 20.61  ? 17  ILE C CG1   1 
ATOM   9336  C  CG2   . ILE C 3 17  ? 155.256 162.021 137.297 1.00 22.23  ? 17  ILE C CG2   1 
ATOM   9337  C  CD1   . ILE C 3 17  ? 154.035 160.218 135.179 1.00 23.12  ? 17  ILE C CD1   1 
ATOM   9338  N  N     . THR C 3 18  ? 158.497 160.890 138.078 1.00 8.40   ? 18  THR C N     1 
ATOM   9339  C  CA    . THR C 3 18  ? 159.527 161.779 138.602 1.00 12.79  ? 18  THR C CA    1 
ATOM   9340  C  C     . THR C 3 18  ? 160.905 161.507 138.015 1.00 15.52  ? 18  THR C C     1 
ATOM   9341  O  O     . THR C 3 18  ? 161.743 162.414 137.996 1.00 19.42  ? 18  THR C O     1 
ATOM   9342  C  CB    . THR C 3 18  ? 159.594 161.672 140.128 1.00 16.32  ? 18  THR C CB    1 
ATOM   9343  O  OG1   . THR C 3 18  ? 159.934 160.331 140.501 1.00 23.28  ? 18  THR C OG1   1 
ATOM   9344  C  CG2   . THR C 3 18  ? 158.257 162.044 140.749 1.00 11.20  ? 18  THR C CG2   1 
ATOM   9345  N  N     . GLY C 3 19  ? 161.161 160.291 137.540 1.00 20.80  ? 19  GLY C N     1 
ATOM   9346  C  CA    . GLY C 3 19  ? 162.479 159.953 137.041 1.00 13.86  ? 19  GLY C CA    1 
ATOM   9347  C  C     . GLY C 3 19  ? 162.580 159.808 135.536 1.00 18.07  ? 19  GLY C C     1 
ATOM   9348  O  O     . GLY C 3 19  ? 163.687 159.766 134.993 1.00 29.10  ? 19  GLY C O     1 
ATOM   9349  N  N     . GLY C 3 20  ? 161.443 159.731 134.848 1.00 12.35  ? 20  GLY C N     1 
ATOM   9350  C  CA    . GLY C 3 20  ? 161.471 159.528 133.413 1.00 21.09  ? 20  GLY C CA    1 
ATOM   9351  C  C     . GLY C 3 20  ? 160.541 160.423 132.620 1.00 26.67  ? 20  GLY C C     1 
ATOM   9352  O  O     . GLY C 3 20  ? 160.600 160.444 131.387 1.00 41.30  ? 20  GLY C O     1 
ATOM   9353  N  N     . VAL C 3 21  ? 159.684 161.169 133.306 1.00 21.66  ? 21  VAL C N     1 
ATOM   9354  C  CA    . VAL C 3 21  ? 158.752 162.087 132.657 1.00 17.12  ? 21  VAL C CA    1 
ATOM   9355  C  C     . VAL C 3 21  ? 159.041 163.531 133.039 1.00 17.21  ? 21  VAL C C     1 
ATOM   9356  O  O     . VAL C 3 21  ? 159.123 164.405 132.175 1.00 24.50  ? 21  VAL C O     1 
ATOM   9357  C  CB    . VAL C 3 21  ? 157.294 161.699 132.993 1.00 21.36  ? 21  VAL C CB    1 
ATOM   9358  C  CG1   . VAL C 3 21  ? 156.330 162.752 132.469 1.00 13.57  ? 21  VAL C CG1   1 
ATOM   9359  C  CG2   . VAL C 3 21  ? 156.962 160.332 132.417 1.00 21.08  ? 21  VAL C CG2   1 
ATOM   9360  N  N     . TYR C 3 22  ? 159.191 163.798 134.336 1.00 16.14  ? 22  TYR C N     1 
ATOM   9361  C  CA    . TYR C 3 22  ? 159.551 165.142 134.783 1.00 12.15  ? 22  TYR C CA    1 
ATOM   9362  C  C     . TYR C 3 22  ? 160.887 165.613 134.221 1.00 16.63  ? 22  TYR C C     1 
ATOM   9363  O  O     . TYR C 3 22  ? 160.947 166.743 133.706 1.00 19.82  ? 22  TYR C O     1 
ATOM   9364  C  CB    . TYR C 3 22  ? 159.530 165.190 136.316 1.00 14.74  ? 22  TYR C CB    1 
ATOM   9365  C  CG    . TYR C 3 22  ? 160.230 166.391 136.911 1.00 14.48  ? 22  TYR C CG    1 
ATOM   9366  C  CD1   . TYR C 3 22  ? 159.714 167.670 136.752 1.00 16.88  ? 22  TYR C CD1   1 
ATOM   9367  C  CD2   . TYR C 3 22  ? 161.403 166.244 137.640 1.00 13.45  ? 22  TYR C CD2   1 
ATOM   9368  C  CE1   . TYR C 3 22  ? 160.348 168.769 137.298 1.00 14.97  ? 22  TYR C CE1   1 
ATOM   9369  C  CE2   . TYR C 3 22  ? 162.045 167.337 138.189 1.00 12.56  ? 22  TYR C CE2   1 
ATOM   9370  C  CZ    . TYR C 3 22  ? 161.512 168.597 138.015 1.00 14.61  ? 22  TYR C CZ    1 
ATOM   9371  O  OH    . TYR C 3 22  ? 162.146 169.689 138.560 1.00 16.97  ? 22  TYR C OH    1 
ATOM   9372  N  N     . PRO C 3 23  ? 161.979 164.838 134.276 1.00 22.60  ? 23  PRO C N     1 
ATOM   9373  C  CA    . PRO C 3 23  ? 163.230 165.328 133.674 1.00 17.43  ? 23  PRO C CA    1 
ATOM   9374  C  C     . PRO C 3 23  ? 163.178 165.415 132.160 1.00 15.89  ? 23  PRO C C     1 
ATOM   9375  O  O     . PRO C 3 23  ? 163.785 166.327 131.585 1.00 25.50  ? 23  PRO C O     1 
ATOM   9376  C  CB    . PRO C 3 23  ? 164.272 164.305 134.145 1.00 17.72  ? 23  PRO C CB    1 
ATOM   9377  C  CG    . PRO C 3 23  ? 163.490 163.065 134.367 1.00 16.42  ? 23  PRO C CG    1 
ATOM   9378  C  CD    . PRO C 3 23  ? 162.171 163.519 134.910 1.00 14.64  ? 23  PRO C CD    1 
ATOM   9379  N  N     . LEU C 3 24  ? 162.480 164.491 131.495 1.00 21.55  ? 24  LEU C N     1 
ATOM   9380  C  CA    . LEU C 3 24  ? 162.378 164.547 130.040 1.00 20.06  ? 24  LEU C CA    1 
ATOM   9381  C  C     . LEU C 3 24  ? 161.629 165.794 129.588 1.00 21.22  ? 24  LEU C C     1 
ATOM   9382  O  O     . LEU C 3 24  ? 162.037 166.460 128.629 1.00 28.58  ? 24  LEU C O     1 
ATOM   9383  C  CB    . LEU C 3 24  ? 161.693 163.287 129.512 1.00 22.32  ? 24  LEU C CB    1 
ATOM   9384  C  CG    . LEU C 3 24  ? 161.312 163.290 128.030 1.00 26.61  ? 24  LEU C CG    1 
ATOM   9385  C  CD1   . LEU C 3 24  ? 162.557 163.305 127.156 1.00 23.59  ? 24  LEU C CD1   1 
ATOM   9386  C  CD2   . LEU C 3 24  ? 160.433 162.095 127.696 1.00 23.36  ? 24  LEU C CD2   1 
ATOM   9387  N  N     . LEU C 3 25  ? 160.529 166.126 130.268 1.00 21.66  ? 25  LEU C N     1 
ATOM   9388  C  CA    . LEU C 3 25  ? 159.791 167.340 129.934 1.00 23.88  ? 25  LEU C CA    1 
ATOM   9389  C  C     . LEU C 3 25  ? 160.630 168.583 130.197 1.00 21.30  ? 25  LEU C C     1 
ATOM   9390  O  O     . LEU C 3 25  ? 160.615 169.531 129.404 1.00 24.31  ? 25  LEU C O     1 
ATOM   9391  C  CB    . LEU C 3 25  ? 158.485 167.393 130.726 1.00 22.43  ? 25  LEU C CB    1 
ATOM   9392  C  CG    . LEU C 3 25  ? 157.516 168.523 130.378 1.00 29.95  ? 25  LEU C CG    1 
ATOM   9393  C  CD1   . LEU C 3 25  ? 157.275 168.587 128.877 1.00 25.18  ? 25  LEU C CD1   1 
ATOM   9394  C  CD2   . LEU C 3 25  ? 156.205 168.353 131.128 1.00 22.24  ? 25  LEU C CD2   1 
ATOM   9395  N  N     . THR C 3 26  ? 161.366 168.599 131.312 1.00 12.94  ? 26  THR C N     1 
ATOM   9396  C  CA    . THR C 3 26  ? 162.229 169.736 131.616 1.00 22.21  ? 26  THR C CA    1 
ATOM   9397  C  C     . THR C 3 26  ? 163.328 169.890 130.572 1.00 18.36  ? 26  THR C C     1 
ATOM   9398  O  O     . THR C 3 26  ? 163.632 171.008 130.139 1.00 29.18  ? 26  THR C O     1 
ATOM   9399  C  CB    . THR C 3 26  ? 162.837 169.577 133.010 1.00 17.62  ? 26  THR C CB    1 
ATOM   9400  O  OG1   . THR C 3 26  ? 161.796 169.337 133.964 1.00 25.54  ? 26  THR C OG1   1 
ATOM   9401  C  CG2   . THR C 3 26  ? 163.600 170.831 133.406 1.00 19.75  ? 26  THR C CG2   1 
ATOM   9402  N  N     . THR C 3 27  ? 163.938 168.777 130.159 1.00 13.21  ? 27  THR C N     1 
ATOM   9403  C  CA    . THR C 3 27  ? 164.999 168.841 129.160 1.00 17.65  ? 27  THR C CA    1 
ATOM   9404  C  C     . THR C 3 27  ? 164.466 169.302 127.809 1.00 19.25  ? 27  THR C C     1 
ATOM   9405  O  O     . THR C 3 27  ? 165.091 170.132 127.140 1.00 27.37  ? 27  THR C O     1 
ATOM   9406  C  CB    . THR C 3 27  ? 165.681 167.478 129.029 1.00 24.25  ? 27  THR C CB    1 
ATOM   9407  O  OG1   . THR C 3 27  ? 166.107 167.030 130.321 1.00 27.02  ? 27  THR C OG1   1 
ATOM   9408  C  CG2   . THR C 3 27  ? 166.888 167.571 128.108 1.00 13.01  ? 27  THR C CG2   1 
ATOM   9409  N  N     . VAL C 3 28  ? 163.310 168.779 127.393 1.00 22.09  ? 28  VAL C N     1 
ATOM   9410  C  CA    . VAL C 3 28  ? 162.745 169.152 126.099 1.00 22.40  ? 28  VAL C CA    1 
ATOM   9411  C  C     . VAL C 3 28  ? 162.375 170.630 126.085 1.00 20.22  ? 28  VAL C C     1 
ATOM   9412  O  O     . VAL C 3 28  ? 162.664 171.351 125.123 1.00 26.49  ? 28  VAL C O     1 
ATOM   9413  C  CB    . VAL C 3 28  ? 161.535 168.261 125.766 1.00 25.73  ? 28  VAL C CB    1 
ATOM   9414  C  CG1   . VAL C 3 28  ? 160.708 168.874 124.645 1.00 23.18  ? 28  VAL C CG1   1 
ATOM   9415  C  CG2   . VAL C 3 28  ? 161.994 166.862 125.389 1.00 17.95  ? 28  VAL C CG2   1 
ATOM   9416  N  N     . LEU C 3 29  ? 161.740 171.107 127.157 1.00 25.27  ? 29  LEU C N     1 
ATOM   9417  C  CA    . LEU C 3 29  ? 161.338 172.508 127.212 1.00 20.35  ? 29  LEU C CA    1 
ATOM   9418  C  C     . LEU C 3 29  ? 162.542 173.423 127.405 1.00 19.12  ? 29  LEU C C     1 
ATOM   9419  O  O     . LEU C 3 29  ? 162.588 174.523 126.844 1.00 24.22  ? 29  LEU C O     1 
ATOM   9420  C  CB    . LEU C 3 29  ? 160.319 172.717 128.332 1.00 22.17  ? 29  LEU C CB    1 
ATOM   9421  C  CG    . LEU C 3 29  ? 158.886 172.266 128.040 1.00 23.84  ? 29  LEU C CG    1 
ATOM   9422  C  CD1   . LEU C 3 29  ? 158.017 172.409 129.280 1.00 24.16  ? 29  LEU C CD1   1 
ATOM   9423  C  CD2   . LEU C 3 29  ? 158.298 173.044 126.875 1.00 26.00  ? 29  LEU C CD2   1 
ATOM   9424  N  N     . GLY C 3 30  ? 163.524 172.986 128.196 1.00 27.26  ? 30  GLY C N     1 
ATOM   9425  C  CA    . GLY C 3 30  ? 164.707 173.804 128.409 1.00 18.87  ? 30  GLY C CA    1 
ATOM   9426  C  C     . GLY C 3 30  ? 165.542 173.973 127.154 1.00 14.66  ? 30  GLY C C     1 
ATOM   9427  O  O     . GLY C 3 30  ? 166.010 175.075 126.854 1.00 29.63  ? 30  GLY C O     1 
ATOM   9428  N  N     . GLN C 3 31  ? 165.742 172.887 126.404 1.00 19.10  ? 31  GLN C N     1 
ATOM   9429  C  CA    . GLN C 3 31  ? 166.522 172.964 125.174 1.00 21.59  ? 31  GLN C CA    1 
ATOM   9430  C  C     . GLN C 3 31  ? 165.794 173.723 124.074 1.00 22.54  ? 31  GLN C C     1 
ATOM   9431  O  O     . GLN C 3 31  ? 166.447 174.287 123.189 1.00 32.19  ? 31  GLN C O     1 
ATOM   9432  C  CB    . GLN C 3 31  ? 166.874 171.558 124.684 1.00 21.90  ? 31  GLN C CB    1 
ATOM   9433  C  CG    . GLN C 3 31  ? 167.816 170.793 125.600 1.00 23.15  ? 31  GLN C CG    1 
ATOM   9434  C  CD    . GLN C 3 31  ? 169.264 171.195 125.416 1.00 27.00  ? 31  GLN C CD    1 
ATOM   9435  O  OE1   . GLN C 3 31  ? 169.658 171.670 124.352 1.00 34.52  ? 31  GLN C OE1   1 
ATOM   9436  N  NE2   . GLN C 3 31  ? 170.067 171.005 126.456 1.00 25.21  ? 31  GLN C NE2   1 
ATOM   9437  N  N     . TRP C 3 32  ? 164.461 173.748 124.107 1.00 23.83  ? 32  TRP C N     1 
ATOM   9438  C  CA    . TRP C 3 32  ? 163.696 174.449 123.082 1.00 17.01  ? 32  TRP C CA    1 
ATOM   9439  C  C     . TRP C 3 32  ? 163.677 175.953 123.333 1.00 19.16  ? 32  TRP C C     1 
ATOM   9440  O  O     . TRP C 3 32  ? 163.844 176.743 122.397 1.00 25.32  ? 32  TRP C O     1 
ATOM   9441  C  CB    . TRP C 3 32  ? 162.273 173.888 123.032 1.00 23.23  ? 32  TRP C CB    1 
ATOM   9442  C  CG    . TRP C 3 32  ? 161.340 174.595 122.090 1.00 25.20  ? 32  TRP C CG    1 
ATOM   9443  C  CD1   . TRP C 3 32  ? 161.674 175.283 120.960 1.00 28.58  ? 32  TRP C CD1   1 
ATOM   9444  C  CD2   . TRP C 3 32  ? 159.914 174.678 122.202 1.00 32.16  ? 32  TRP C CD2   1 
ATOM   9445  N  NE1   . TRP C 3 32  ? 160.545 175.789 120.363 1.00 32.71  ? 32  TRP C NE1   1 
ATOM   9446  C  CE2   . TRP C 3 32  ? 159.452 175.431 121.106 1.00 29.83  ? 32  TRP C CE2   1 
ATOM   9447  C  CE3   . TRP C 3 32  ? 158.984 174.187 123.124 1.00 32.71  ? 32  TRP C CE3   1 
ATOM   9448  C  CZ2   . TRP C 3 32  ? 158.100 175.706 120.906 1.00 28.46  ? 32  TRP C CZ2   1 
ATOM   9449  C  CZ3   . TRP C 3 32  ? 157.643 174.460 122.923 1.00 33.14  ? 32  TRP C CZ3   1 
ATOM   9450  C  CH2   . TRP C 3 32  ? 157.214 175.213 121.824 1.00 29.30  ? 32  TRP C CH2   1 
ATOM   9451  N  N     . TRP C 3 33  ? 163.489 176.366 124.586 1.00 22.59  ? 33  TRP C N     1 
ATOM   9452  C  CA    . TRP C 3 33  ? 163.345 177.779 124.913 1.00 19.49  ? 33  TRP C CA    1 
ATOM   9453  C  C     . TRP C 3 33  ? 164.679 178.463 125.189 1.00 16.67  ? 33  TRP C C     1 
ATOM   9454  O  O     . TRP C 3 33  ? 164.891 179.598 124.748 1.00 29.30  ? 33  TRP C O     1 
ATOM   9455  C  CB    . TRP C 3 33  ? 162.418 177.943 126.120 1.00 18.15  ? 33  TRP C CB    1 
ATOM   9456  C  CG    . TRP C 3 33  ? 160.988 177.615 125.821 1.00 18.75  ? 33  TRP C CG    1 
ATOM   9457  C  CD1   . TRP C 3 33  ? 160.406 177.534 124.589 1.00 25.74  ? 33  TRP C CD1   1 
ATOM   9458  C  CD2   . TRP C 3 33  ? 159.960 177.308 126.770 1.00 22.16  ? 33  TRP C CD2   1 
ATOM   9459  N  NE1   . TRP C 3 33  ? 159.079 177.205 124.713 1.00 28.71  ? 33  TRP C NE1   1 
ATOM   9460  C  CE2   . TRP C 3 33  ? 158.780 177.059 126.042 1.00 29.07  ? 33  TRP C CE2   1 
ATOM   9461  C  CE3   . TRP C 3 33  ? 159.922 177.223 128.165 1.00 24.07  ? 33  TRP C CE3   1 
ATOM   9462  C  CZ2   . TRP C 3 33  ? 157.576 176.731 126.661 1.00 22.60  ? 33  TRP C CZ2   1 
ATOM   9463  C  CZ3   . TRP C 3 33  ? 158.726 176.897 128.777 1.00 27.40  ? 33  TRP C CZ3   1 
ATOM   9464  C  CH2   . TRP C 3 33  ? 157.570 176.655 128.026 1.00 26.90  ? 33  TRP C CH2   1 
ATOM   9465  N  N     . PHE C 3 34  ? 165.586 177.802 125.906 1.00 22.36  ? 34  PHE C N     1 
ATOM   9466  C  CA    . PHE C 3 34  ? 166.880 178.377 126.276 1.00 20.40  ? 34  PHE C CA    1 
ATOM   9467  C  C     . PHE C 3 34  ? 167.994 177.393 125.940 1.00 18.58  ? 34  PHE C C     1 
ATOM   9468  O  O     . PHE C 3 34  ? 168.627 176.822 126.836 1.00 25.90  ? 34  PHE C O     1 
ATOM   9469  C  CB    . PHE C 3 34  ? 166.902 178.743 127.761 1.00 17.55  ? 34  PHE C CB    1 
ATOM   9470  C  CG    . PHE C 3 34  ? 165.561 179.150 128.304 1.00 22.83  ? 34  PHE C CG    1 
ATOM   9471  C  CD1   . PHE C 3 34  ? 164.986 180.356 127.936 1.00 13.69  ? 34  PHE C CD1   1 
ATOM   9472  C  CD2   . PHE C 3 34  ? 164.870 178.323 129.173 1.00 19.94  ? 34  PHE C CD2   1 
ATOM   9473  C  CE1   . PHE C 3 34  ? 163.751 180.730 128.429 1.00 16.75  ? 34  PHE C CE1   1 
ATOM   9474  C  CE2   . PHE C 3 34  ? 163.635 178.692 129.671 1.00 11.19  ? 34  PHE C CE2   1 
ATOM   9475  C  CZ    . PHE C 3 34  ? 163.075 179.898 129.298 1.00 9.29   ? 34  PHE C CZ    1 
ATOM   9476  N  N     . PRO C 3 35  ? 168.255 177.163 124.647 1.00 26.36  ? 35  PRO C N     1 
ATOM   9477  C  CA    . PRO C 3 35  ? 169.313 176.201 124.286 1.00 17.17  ? 35  PRO C CA    1 
ATOM   9478  C  C     . PRO C 3 35  ? 170.691 176.594 124.788 1.00 19.80  ? 35  PRO C C     1 
ATOM   9479  O  O     . PRO C 3 35  ? 171.468 175.718 125.188 1.00 25.50  ? 35  PRO C O     1 
ATOM   9480  C  CB    . PRO C 3 35  ? 169.259 176.175 122.751 1.00 10.24  ? 35  PRO C CB    1 
ATOM   9481  C  CG    . PRO C 3 35  ? 168.520 177.411 122.359 1.00 19.45  ? 35  PRO C CG    1 
ATOM   9482  C  CD    . PRO C 3 35  ? 167.562 177.694 123.462 1.00 22.40  ? 35  PRO C CD    1 
ATOM   9483  N  N     . TRP C 3 36  ? 171.020 177.888 124.780 1.00 22.94  ? 36  TRP C N     1 
ATOM   9484  C  CA    . TRP C 3 36  ? 172.376 178.305 125.128 1.00 16.69  ? 36  TRP C CA    1 
ATOM   9485  C  C     . TRP C 3 36  ? 172.657 178.110 126.613 1.00 18.55  ? 36  TRP C C     1 
ATOM   9486  O  O     . TRP C 3 36  ? 173.706 177.573 126.988 1.00 24.43  ? 36  TRP C O     1 
ATOM   9487  C  CB    . TRP C 3 36  ? 172.598 179.763 124.726 1.00 14.25  ? 36  TRP C CB    1 
ATOM   9488  C  CG    . TRP C 3 36  ? 174.013 180.223 124.906 1.00 21.24  ? 36  TRP C CG    1 
ATOM   9489  C  CD1   . TRP C 3 36  ? 175.109 179.787 124.221 1.00 19.40  ? 36  TRP C CD1   1 
ATOM   9490  C  CD2   . TRP C 3 36  ? 174.485 181.211 125.830 1.00 20.78  ? 36  TRP C CD2   1 
ATOM   9491  N  NE1   . TRP C 3 36  ? 176.234 180.440 124.662 1.00 22.62  ? 36  TRP C NE1   1 
ATOM   9492  C  CE2   . TRP C 3 36  ? 175.878 181.321 125.649 1.00 18.12  ? 36  TRP C CE2   1 
ATOM   9493  C  CE3   . TRP C 3 36  ? 173.865 182.014 126.793 1.00 21.06  ? 36  TRP C CE3   1 
ATOM   9494  C  CZ2   . TRP C 3 36  ? 176.661 182.199 126.395 1.00 19.88  ? 36  TRP C CZ2   1 
ATOM   9495  C  CZ3   . TRP C 3 36  ? 174.645 182.886 127.532 1.00 19.61  ? 36  TRP C CZ3   1 
ATOM   9496  C  CH2   . TRP C 3 36  ? 176.027 182.971 127.329 1.00 18.39  ? 36  TRP C CH2   1 
ATOM   9497  N  N     . GLN C 3 37  ? 171.736 178.545 127.475 1.00 14.23  ? 37  GLN C N     1 
ATOM   9498  C  CA    . GLN C 3 37  ? 171.942 178.393 128.912 1.00 17.48  ? 37  GLN C CA    1 
ATOM   9499  C  C     . GLN C 3 37  ? 171.907 176.927 129.326 1.00 22.70  ? 37  GLN C C     1 
ATOM   9500  O  O     . GLN C 3 37  ? 172.690 176.500 130.183 1.00 25.41  ? 37  GLN C O     1 
ATOM   9501  C  CB    . GLN C 3 37  ? 170.893 179.191 129.684 1.00 18.49  ? 37  GLN C CB    1 
ATOM   9502  C  CG    . GLN C 3 37  ? 170.794 180.655 129.289 1.00 15.36  ? 37  GLN C CG    1 
ATOM   9503  C  CD    . GLN C 3 37  ? 169.765 180.899 128.203 1.00 16.87  ? 37  GLN C CD    1 
ATOM   9504  O  OE1   . GLN C 3 37  ? 169.898 180.408 127.083 1.00 27.62  ? 37  GLN C OE1   1 
ATOM   9505  N  NE2   . GLN C 3 37  ? 168.729 181.662 128.531 1.00 14.98  ? 37  GLN C NE2   1 
ATOM   9506  N  N     . ALA C 3 38  ? 171.006 176.141 128.732 1.00 18.96  ? 38  ALA C N     1 
ATOM   9507  C  CA    . ALA C 3 38  ? 170.881 174.735 129.095 1.00 17.52  ? 38  ALA C CA    1 
ATOM   9508  C  C     . ALA C 3 38  ? 172.105 173.918 128.704 1.00 17.95  ? 38  ALA C C     1 
ATOM   9509  O  O     . ALA C 3 38  ? 172.321 172.842 129.270 1.00 17.89  ? 38  ALA C O     1 
ATOM   9510  C  CB    . ALA C 3 38  ? 169.631 174.133 128.451 1.00 14.73  ? 38  ALA C CB    1 
ATOM   9511  N  N     . ASN C 3 39  ? 172.907 174.401 127.757 1.00 15.79  ? 39  ASN C N     1 
ATOM   9512  C  CA    . ASN C 3 39  ? 174.084 173.687 127.287 1.00 14.12  ? 39  ASN C CA    1 
ATOM   9513  C  C     . ASN C 3 39  ? 175.375 174.189 127.923 1.00 15.80  ? 39  ASN C C     1 
ATOM   9514  O  O     . ASN C 3 39  ? 176.460 173.773 127.507 1.00 25.63  ? 39  ASN C O     1 
ATOM   9515  C  CB    . ASN C 3 39  ? 174.179 173.776 125.763 1.00 18.47  ? 39  ASN C CB    1 
ATOM   9516  C  CG    . ASN C 3 39  ? 173.093 172.980 125.068 1.00 24.46  ? 39  ASN C CG    1 
ATOM   9517  O  OD1   . ASN C 3 39  ? 172.938 171.783 125.305 1.00 24.16  ? 39  ASN C OD1   1 
ATOM   9518  N  ND2   . ASN C 3 39  ? 172.333 173.642 124.203 1.00 30.20  ? 39  ASN C ND2   1 
ATOM   9519  N  N     . GLY C 3 40  ? 175.284 175.073 128.915 1.00 17.68  ? 40  GLY C N     1 
ATOM   9520  C  CA    . GLY C 3 40  ? 176.445 175.529 129.654 1.00 15.57  ? 40  GLY C CA    1 
ATOM   9521  C  C     . GLY C 3 40  ? 176.867 176.958 129.399 1.00 14.37  ? 40  GLY C C     1 
ATOM   9522  O  O     . GLY C 3 40  ? 177.887 177.384 129.955 1.00 27.44  ? 40  GLY C O     1 
ATOM   9523  N  N     . SER C 3 41  ? 176.119 177.716 128.594 1.00 18.69  ? 41  SER C N     1 
ATOM   9524  C  CA    . SER C 3 41  ? 176.469 179.099 128.263 1.00 13.89  ? 41  SER C CA    1 
ATOM   9525  C  C     . SER C 3 41  ? 177.897 179.188 127.728 1.00 17.32  ? 41  SER C C     1 
ATOM   9526  O  O     . SER C 3 41  ? 178.684 180.048 128.130 1.00 21.62  ? 41  SER C O     1 
ATOM   9527  C  CB    . SER C 3 41  ? 176.278 180.021 129.469 1.00 16.46  ? 41  SER C CB    1 
ATOM   9528  O  OG    . SER C 3 41  ? 174.992 179.858 130.040 1.00 26.81  ? 41  SER C OG    1 
ATOM   9529  N  N     . LEU C 3 42  ? 178.232 178.280 126.816 1.00 21.03  ? 42  LEU C N     1 
ATOM   9530  C  CA    . LEU C 3 42  ? 179.596 178.179 126.318 1.00 24.07  ? 42  LEU C CA    1 
ATOM   9531  C  C     . LEU C 3 42  ? 179.955 179.377 125.449 1.00 21.49  ? 42  LEU C C     1 
ATOM   9532  O  O     . LEU C 3 42  ? 179.139 179.865 124.661 1.00 22.89  ? 42  LEU C O     1 
ATOM   9533  C  CB    . LEU C 3 42  ? 179.772 176.887 125.522 1.00 21.27  ? 42  LEU C CB    1 
ATOM   9534  C  CG    . LEU C 3 42  ? 179.471 175.586 126.269 1.00 21.47  ? 42  LEU C CG    1 
ATOM   9535  C  CD1   . LEU C 3 42  ? 179.661 174.385 125.356 1.00 25.48  ? 42  LEU C CD1   1 
ATOM   9536  C  CD2   . LEU C 3 42  ? 180.343 175.467 127.507 1.00 18.92  ? 42  LEU C CD2   1 
ATOM   9537  N  N     . ILE C 3 43  ? 181.189 179.849 125.597 1.00 22.48  ? 43  ILE C N     1 
ATOM   9538  C  CA    . ILE C 3 43  ? 181.739 180.912 124.765 1.00 25.74  ? 43  ILE C CA    1 
ATOM   9539  C  C     . ILE C 3 43  ? 182.607 180.261 123.698 1.00 29.15  ? 43  ILE C C     1 
ATOM   9540  O  O     . ILE C 3 43  ? 183.560 179.540 124.017 1.00 33.05  ? 43  ILE C O     1 
ATOM   9541  C  CB    . ILE C 3 43  ? 182.546 181.919 125.599 1.00 27.44  ? 43  ILE C CB    1 
ATOM   9542  C  CG1   . ILE C 3 43  ? 181.644 182.605 126.627 1.00 25.13  ? 43  ILE C CG1   1 
ATOM   9543  C  CG2   . ILE C 3 43  ? 183.210 182.947 124.695 1.00 26.03  ? 43  ILE C CG2   1 
ATOM   9544  C  CD1   . ILE C 3 43  ? 182.394 183.183 127.807 1.00 26.79  ? 43  ILE C CD1   1 
ATOM   9545  N  N     . ARG C 3 44  ? 182.278 180.507 122.433 1.00 39.20  ? 44  ARG C N     1 
ATOM   9546  C  CA    . ARG C 3 44  ? 182.950 179.871 121.309 1.00 38.60  ? 44  ARG C CA    1 
ATOM   9547  C  C     . ARG C 3 44  ? 183.526 180.923 120.376 1.00 42.84  ? 44  ARG C C     1 
ATOM   9548  O  O     . ARG C 3 44  ? 182.843 181.891 120.023 1.00 48.79  ? 44  ARG C O     1 
ATOM   9549  C  CB    . ARG C 3 44  ? 181.989 178.966 120.532 1.00 40.19  ? 44  ARG C CB    1 
ATOM   9550  C  CG    . ARG C 3 44  ? 181.984 177.516 120.977 1.00 40.76  ? 44  ARG C CG    1 
ATOM   9551  C  CD    . ARG C 3 44  ? 181.006 176.702 120.146 1.00 40.04  ? 44  ARG C CD    1 
ATOM   9552  N  NE    . ARG C 3 44  ? 180.121 175.890 120.972 1.00 40.53  ? 44  ARG C NE    1 
ATOM   9553  C  CZ    . ARG C 3 44  ? 180.243 174.580 121.134 1.00 43.65  ? 44  ARG C CZ    1 
ATOM   9554  N  NH1   . ARG C 3 44  ? 181.205 173.896 120.535 1.00 41.74  ? 44  ARG C NH1   1 
ATOM   9555  N  NH2   . ARG C 3 44  ? 179.378 173.939 121.915 1.00 39.21  ? 44  ARG C NH2   1 
ATOM   9556  N  N     . GLU C 3 45  ? 184.782 180.732 119.984 1.00 51.40  ? 45  GLU C N     1 
ATOM   9557  C  CA    . GLU C 3 45  ? 185.397 181.442 118.865 1.00 54.09  ? 45  GLU C CA    1 
ATOM   9558  C  C     . GLU C 3 45  ? 185.893 180.351 117.920 1.00 56.19  ? 45  GLU C C     1 
ATOM   9559  O  O     . GLU C 3 45  ? 186.559 179.403 118.343 1.00 56.99  ? 45  GLU C O     1 
ATOM   9560  C  CB    . GLU C 3 45  ? 186.519 182.401 119.331 1.00 54.65  ? 45  GLU C CB    1 
ATOM   9561  C  CG    . GLU C 3 45  ? 187.747 181.745 119.955 1.00 55.43  ? 45  GLU C CG    1 
ATOM   9562  C  CD    . GLU C 3 45  ? 188.802 181.351 118.935 1.00 58.89  ? 45  GLU C CD    1 
ATOM   9563  O  OE1   . GLU C 3 45  ? 188.581 181.569 117.726 1.00 58.58  ? 45  GLU C OE1   1 
ATOM   9564  O  OE2   . GLU C 3 45  ? 189.856 180.822 119.346 1.00 58.13  ? 45  GLU C OE2   1 
ATOM   9565  N  N     . GLY C 3 46  ? 185.546 180.471 116.648 1.00 56.80  ? 46  GLY C N     1 
ATOM   9566  C  CA    . GLY C 3 46  ? 185.834 179.430 115.677 1.00 57.22  ? 46  GLY C CA    1 
ATOM   9567  C  C     . GLY C 3 46  ? 185.146 178.123 116.051 1.00 57.59  ? 46  GLY C C     1 
ATOM   9568  O  O     . GLY C 3 46  ? 183.950 178.104 116.337 1.00 58.65  ? 46  GLY C O     1 
ATOM   9569  N  N     . ASP C 3 47  ? 185.910 177.032 116.049 1.00 60.07  ? 47  ASP C N     1 
ATOM   9570  C  CA    . ASP C 3 47  ? 185.393 175.713 116.386 1.00 61.11  ? 47  ASP C CA    1 
ATOM   9571  C  C     . ASP C 3 47  ? 185.852 175.227 117.756 1.00 63.45  ? 47  ASP C C     1 
ATOM   9572  O  O     . ASP C 3 47  ? 185.673 174.047 118.074 1.00 64.93  ? 47  ASP C O     1 
ATOM   9573  C  CB    . ASP C 3 47  ? 185.794 174.701 115.310 1.00 62.65  ? 47  ASP C CB    1 
ATOM   9574  C  CG    . ASP C 3 47  ? 187.233 174.245 115.443 1.00 61.71  ? 47  ASP C CG    1 
ATOM   9575  O  OD1   . ASP C 3 47  ? 188.135 175.109 115.456 1.00 62.22  ? 47  ASP C OD1   1 
ATOM   9576  O  OD2   . ASP C 3 47  ? 187.464 173.021 115.535 1.00 63.73  ? 47  ASP C OD2   1 
ATOM   9577  N  N     . THR C 3 48  ? 186.430 176.102 118.575 1.00 51.95  ? 48  THR C N     1 
ATOM   9578  C  CA    . THR C 3 48  ? 186.948 175.724 119.882 1.00 49.76  ? 48  THR C CA    1 
ATOM   9579  C  C     . THR C 3 48  ? 186.233 176.500 120.981 1.00 49.70  ? 48  THR C C     1 
ATOM   9580  O  O     . THR C 3 48  ? 186.039 177.715 120.887 1.00 50.25  ? 48  THR C O     1 
ATOM   9581  C  CB    . THR C 3 48  ? 188.465 175.958 119.975 1.00 52.66  ? 48  THR C CB    1 
ATOM   9582  O  OG1   . THR C 3 48  ? 188.898 175.778 121.330 1.00 49.88  ? 48  THR C OG1   1 
ATOM   9583  C  CG2   . THR C 3 48  ? 188.833 177.358 119.505 1.00 49.37  ? 48  THR C CG2   1 
ATOM   9584  N  N     . VAL C 3 49  ? 185.828 175.776 122.020 1.00 41.61  ? 49  VAL C N     1 
ATOM   9585  C  CA    . VAL C 3 49  ? 185.167 176.368 123.177 1.00 34.61  ? 49  VAL C CA    1 
ATOM   9586  C  C     . VAL C 3 49  ? 186.228 177.007 124.064 1.00 31.48  ? 49  VAL C C     1 
ATOM   9587  O  O     . VAL C 3 49  ? 187.171 176.337 124.499 1.00 37.81  ? 49  VAL C O     1 
ATOM   9588  C  CB    . VAL C 3 49  ? 184.360 175.317 123.954 1.00 34.88  ? 49  VAL C CB    1 
ATOM   9589  C  CG1   . VAL C 3 49  ? 183.737 175.935 125.197 1.00 33.79  ? 49  VAL C CG1   1 
ATOM   9590  C  CG2   . VAL C 3 49  ? 183.292 174.705 123.061 1.00 32.61  ? 49  VAL C CG2   1 
ATOM   9591  N  N     . ARG C 3 50  ? 186.074 178.300 124.336 1.00 31.51  ? 50  ARG C N     1 
ATOM   9592  C  CA    . ARG C 3 50  ? 187.022 179.034 125.164 1.00 31.02  ? 50  ARG C CA    1 
ATOM   9593  C  C     . ARG C 3 50  ? 186.633 179.060 126.635 1.00 30.74  ? 50  ARG C C     1 
ATOM   9594  O  O     . ARG C 3 50  ? 187.389 179.601 127.449 1.00 36.24  ? 50  ARG C O     1 
ATOM   9595  C  CB    . ARG C 3 50  ? 187.174 180.468 124.649 1.00 32.51  ? 50  ARG C CB    1 
ATOM   9596  C  CG    . ARG C 3 50  ? 187.877 180.568 123.309 1.00 38.76  ? 50  ARG C CG    1 
ATOM   9597  C  CD    . ARG C 3 50  ? 189.138 179.721 123.283 1.00 38.62  ? 50  ARG C CD    1 
ATOM   9598  N  NE    . ARG C 3 50  ? 190.303 180.453 123.763 1.00 38.37  ? 50  ARG C NE    1 
ATOM   9599  C  CZ    . ARG C 3 50  ? 191.510 180.378 123.218 1.00 40.12  ? 50  ARG C CZ    1 
ATOM   9600  N  NH1   . ARG C 3 50  ? 191.747 179.610 122.168 1.00 39.47  ? 50  ARG C NH1   1 
ATOM   9601  N  NH2   . ARG C 3 50  ? 192.503 181.092 123.741 1.00 39.65  ? 50  ARG C NH2   1 
ATOM   9602  N  N     . GLY C 3 51  ? 185.490 178.498 126.995 1.00 27.77  ? 51  GLY C N     1 
ATOM   9603  C  CA    . GLY C 3 51  ? 185.046 178.456 128.367 1.00 23.67  ? 51  GLY C CA    1 
ATOM   9604  C  C     . GLY C 3 51  ? 183.556 178.691 128.451 1.00 23.48  ? 51  GLY C C     1 
ATOM   9605  O  O     . GLY C 3 51  ? 182.863 178.805 127.441 1.00 28.78  ? 51  GLY C O     1 
ATOM   9606  N  N     . SER C 3 52  ? 183.063 178.760 129.682 1.00 27.15  ? 52  SER C N     1 
ATOM   9607  C  CA    . SER C 3 52  ? 181.665 179.043 129.962 1.00 17.80  ? 52  SER C CA    1 
ATOM   9608  C  C     . SER C 3 52  ? 181.547 180.411 130.619 1.00 20.80  ? 52  SER C C     1 
ATOM   9609  O  O     . SER C 3 52  ? 182.407 180.804 131.413 1.00 23.10  ? 52  SER C O     1 
ATOM   9610  C  CB    . SER C 3 52  ? 181.055 177.970 130.869 1.00 15.99  ? 52  SER C CB    1 
ATOM   9611  O  OG    . SER C 3 52  ? 179.859 178.431 131.472 1.00 25.10  ? 52  SER C OG    1 
ATOM   9612  N  N     . ALA C 3 53  ? 180.478 181.134 130.282 1.00 22.75  ? 53  ALA C N     1 
ATOM   9613  C  CA    . ALA C 3 53  ? 180.256 182.458 130.850 1.00 21.38  ? 53  ALA C CA    1 
ATOM   9614  C  C     . ALA C 3 53  ? 179.969 182.421 132.345 1.00 17.05  ? 53  ALA C C     1 
ATOM   9615  O  O     . ALA C 3 53  ? 180.009 183.474 132.990 1.00 23.30  ? 53  ALA C O     1 
ATOM   9616  C  CB    . ALA C 3 53  ? 179.107 183.156 130.121 1.00 22.30  ? 53  ALA C CB    1 
ATOM   9617  N  N     . LEU C 3 54  ? 179.684 181.248 132.909 1.00 14.42  ? 54  LEU C N     1 
ATOM   9618  C  CA    . LEU C 3 54  ? 179.386 181.116 134.328 1.00 23.31  ? 54  LEU C CA    1 
ATOM   9619  C  C     . LEU C 3 54  ? 180.516 180.481 135.127 1.00 11.66  ? 54  LEU C C     1 
ATOM   9620  O  O     . LEU C 3 54  ? 180.488 180.544 136.361 1.00 26.23  ? 54  LEU C O     1 
ATOM   9621  C  CB    . LEU C 3 54  ? 178.107 180.293 134.523 1.00 18.43  ? 54  LEU C CB    1 
ATOM   9622  C  CG    . LEU C 3 54  ? 176.839 180.837 133.864 1.00 17.26  ? 54  LEU C CG    1 
ATOM   9623  C  CD1   . LEU C 3 54  ? 175.631 180.015 134.275 1.00 16.72  ? 54  LEU C CD1   1 
ATOM   9624  C  CD2   . LEU C 3 54  ? 176.640 182.301 134.218 1.00 23.87  ? 54  LEU C CD2   1 
ATOM   9625  N  N     . ILE C 3 55  ? 181.502 179.879 134.468 1.00 13.87  ? 55  ILE C N     1 
ATOM   9626  C  CA    . ILE C 3 55  ? 182.589 179.172 135.135 1.00 13.80  ? 55  ILE C CA    1 
ATOM   9627  C  C     . ILE C 3 55  ? 183.846 180.025 135.053 1.00 13.90  ? 55  ILE C C     1 
ATOM   9628  O  O     . ILE C 3 55  ? 184.267 180.420 133.959 1.00 28.42  ? 55  ILE C O     1 
ATOM   9629  C  CB    . ILE C 3 55  ? 182.824 177.784 134.515 1.00 19.97  ? 55  ILE C CB    1 
ATOM   9630  C  CG1   . ILE C 3 55  ? 181.528 176.972 134.519 1.00 17.32  ? 55  ILE C CG1   1 
ATOM   9631  C  CG2   . ILE C 3 55  ? 183.924 177.045 135.261 1.00 14.78  ? 55  ILE C CG2   1 
ATOM   9632  C  CD1   . ILE C 3 55  ? 180.935 176.771 135.896 1.00 9.79   ? 55  ILE C CD1   1 
ATOM   9633  N  N     . GLY C 3 56  ? 184.446 180.304 136.210 1.00 21.09  ? 56  GLY C N     1 
ATOM   9634  C  CA    . GLY C 3 56  ? 185.658 181.090 136.242 1.00 12.67  ? 56  GLY C CA    1 
ATOM   9635  C  C     . GLY C 3 56  ? 186.880 180.305 135.804 1.00 17.93  ? 56  GLY C C     1 
ATOM   9636  O  O     . GLY C 3 56  ? 186.901 179.075 135.795 1.00 28.22  ? 56  GLY C O     1 
ATOM   9637  N  N     . GLN C 3 57  ? 187.919 181.046 135.431 1.00 19.01  ? 57  GLN C N     1 
ATOM   9638  C  CA    . GLN C 3 57  ? 189.174 180.462 134.985 1.00 22.23  ? 57  GLN C CA    1 
ATOM   9639  C  C     . GLN C 3 57  ? 190.321 181.037 135.802 1.00 23.99  ? 57  GLN C C     1 
ATOM   9640  O  O     . GLN C 3 57  ? 190.182 182.058 136.481 1.00 27.83  ? 57  GLN C O     1 
ATOM   9641  C  CB    . GLN C 3 57  ? 189.413 180.711 133.490 1.00 16.91  ? 57  GLN C CB    1 
ATOM   9642  C  CG    . GLN C 3 57  ? 188.482 179.932 132.578 1.00 15.00  ? 57  GLN C CG    1 
ATOM   9643  C  CD    . GLN C 3 57  ? 188.530 180.420 131.145 1.00 23.78  ? 57  GLN C CD    1 
ATOM   9644  O  OE1   . GLN C 3 57  ? 189.363 181.253 130.790 1.00 32.66  ? 57  GLN C OE1   1 
ATOM   9645  N  NE2   . GLN C 3 57  ? 187.634 179.904 130.314 1.00 23.20  ? 57  GLN C NE2   1 
ATOM   9646  N  N     . ASN C 3 58  ? 191.464 180.361 135.730 1.00 27.12  ? 58  ASN C N     1 
ATOM   9647  C  CA    . ASN C 3 58  ? 192.663 180.770 136.454 1.00 18.83  ? 58  ASN C CA    1 
ATOM   9648  C  C     . ASN C 3 58  ? 193.480 181.702 135.566 1.00 26.05  ? 58  ASN C C     1 
ATOM   9649  O  O     . ASN C 3 58  ? 194.134 181.255 134.619 1.00 35.92  ? 58  ASN C O     1 
ATOM   9650  C  CB    . ASN C 3 58  ? 193.479 179.549 136.869 1.00 25.32  ? 58  ASN C CB    1 
ATOM   9651  C  CG    . ASN C 3 58  ? 194.621 179.901 137.801 1.00 23.92  ? 58  ASN C CG    1 
ATOM   9652  O  OD1   . ASN C 3 58  ? 194.494 180.779 138.654 1.00 34.99  ? 58  ASN C OD1   1 
ATOM   9653  N  ND2   . ASN C 3 58  ? 195.747 179.217 137.641 1.00 34.59  ? 58  ASN C ND2   1 
ATOM   9654  N  N     . PHE C 3 59  ? 193.441 182.996 135.871 1.00 24.62  ? 59  PHE C N     1 
ATOM   9655  C  CA    . PHE C 3 59  ? 194.213 183.998 135.150 1.00 27.59  ? 59  PHE C CA    1 
ATOM   9656  C  C     . PHE C 3 59  ? 195.438 184.380 135.970 1.00 29.72  ? 59  PHE C C     1 
ATOM   9657  O  O     . PHE C 3 59  ? 195.314 184.757 137.140 1.00 38.14  ? 59  PHE C O     1 
ATOM   9658  C  CB    . PHE C 3 59  ? 193.364 185.237 134.857 1.00 25.60  ? 59  PHE C CB    1 
ATOM   9659  C  CG    . PHE C 3 59  ? 192.254 184.993 133.876 1.00 25.89  ? 59  PHE C CG    1 
ATOM   9660  C  CD1   . PHE C 3 59  ? 192.501 185.001 132.514 1.00 21.96  ? 59  PHE C CD1   1 
ATOM   9661  C  CD2   . PHE C 3 59  ? 190.963 184.752 134.316 1.00 22.95  ? 59  PHE C CD2   1 
ATOM   9662  C  CE1   . PHE C 3 59  ? 191.482 184.776 131.609 1.00 24.11  ? 59  PHE C CE1   1 
ATOM   9663  C  CE2   . PHE C 3 59  ? 189.940 184.526 133.416 1.00 22.20  ? 59  PHE C CE2   1 
ATOM   9664  C  CZ    . PHE C 3 59  ? 190.200 184.538 132.060 1.00 16.62  ? 59  PHE C CZ    1 
ATOM   9665  N  N     . THR C 3 60  ? 196.617 184.280 135.355 1.00 33.96  ? 60  THR C N     1 
ATOM   9666  C  CA    . THR C 3 60  ? 197.870 184.580 136.031 1.00 28.99  ? 60  THR C CA    1 
ATOM   9667  C  C     . THR C 3 60  ? 198.724 185.618 135.318 1.00 31.24  ? 60  THR C C     1 
ATOM   9668  O  O     . THR C 3 60  ? 199.790 185.970 135.836 1.00 39.89  ? 60  THR C O     1 
ATOM   9669  C  CB    . THR C 3 60  ? 198.705 183.301 136.212 1.00 34.35  ? 60  THR C CB    1 
ATOM   9670  O  OG1   . THR C 3 60  ? 198.884 182.660 134.944 1.00 42.92  ? 60  THR C OG1   1 
ATOM   9671  C  CG2   . THR C 3 60  ? 198.012 182.341 137.168 1.00 32.39  ? 60  THR C CG2   1 
ATOM   9672  N  N     . GLY C 3 61  ? 198.297 186.119 134.162 1.00 31.53  ? 61  GLY C N     1 
ATOM   9673  C  CA    . GLY C 3 61  ? 199.108 187.069 133.432 1.00 31.51  ? 61  GLY C CA    1 
ATOM   9674  C  C     . GLY C 3 61  ? 199.037 188.466 134.017 1.00 34.42  ? 61  GLY C C     1 
ATOM   9675  O  O     . GLY C 3 61  ? 198.284 188.753 134.948 1.00 35.53  ? 61  GLY C O     1 
ATOM   9676  N  N     . ASN C 3 62  ? 199.846 189.359 133.443 1.00 33.52  ? 62  ASN C N     1 
ATOM   9677  C  CA    . ASN C 3 62  ? 199.885 190.734 133.927 1.00 32.08  ? 62  ASN C CA    1 
ATOM   9678  C  C     . ASN C 3 62  ? 198.849 191.605 133.231 1.00 33.70  ? 62  ASN C C     1 
ATOM   9679  O  O     . ASN C 3 62  ? 198.367 192.581 133.817 1.00 38.13  ? 62  ASN C O     1 
ATOM   9680  C  CB    . ASN C 3 62  ? 201.284 191.320 133.737 1.00 31.80  ? 62  ASN C CB    1 
ATOM   9681  C  CG    . ASN C 3 62  ? 201.678 192.261 134.856 1.00 35.12  ? 62  ASN C CG    1 
ATOM   9682  O  OD1   . ASN C 3 62  ? 201.814 193.467 134.650 1.00 39.50  ? 62  ASN C OD1   1 
ATOM   9683  N  ND2   . ASN C 3 62  ? 201.863 191.713 136.052 1.00 37.68  ? 62  ASN C ND2   1 
ATOM   9684  N  N     . GLY C 3 63  ? 198.495 191.274 131.994 1.00 29.82  ? 63  GLY C N     1 
ATOM   9685  C  CA    . GLY C 3 63  ? 197.495 192.001 131.245 1.00 28.56  ? 63  GLY C CA    1 
ATOM   9686  C  C     . GLY C 3 63  ? 196.077 191.514 131.432 1.00 30.47  ? 63  GLY C C     1 
ATOM   9687  O  O     . GLY C 3 63  ? 195.175 191.994 130.737 1.00 36.17  ? 63  GLY C O     1 
ATOM   9688  N  N     . TYR C 3 64  ? 195.847 190.578 132.347 1.00 31.77  ? 64  TYR C N     1 
ATOM   9689  C  CA    . TYR C 3 64  ? 194.530 190.009 132.588 1.00 25.11  ? 64  TYR C CA    1 
ATOM   9690  C  C     . TYR C 3 64  ? 194.038 190.397 133.975 1.00 23.85  ? 64  TYR C C     1 
ATOM   9691  O  O     . TYR C 3 64  ? 194.826 190.483 134.922 1.00 30.52  ? 64  TYR C O     1 
ATOM   9692  C  CB    . TYR C 3 64  ? 194.559 188.483 132.464 1.00 23.70  ? 64  TYR C CB    1 
ATOM   9693  C  CG    . TYR C 3 64  ? 194.561 187.975 131.041 1.00 29.11  ? 64  TYR C CG    1 
ATOM   9694  C  CD1   . TYR C 3 64  ? 193.608 188.405 130.127 1.00 27.34  ? 64  TYR C CD1   1 
ATOM   9695  C  CD2   . TYR C 3 64  ? 195.517 187.065 130.612 1.00 30.40  ? 64  TYR C CD2   1 
ATOM   9696  C  CE1   . TYR C 3 64  ? 193.609 187.941 128.825 1.00 31.88  ? 64  TYR C CE1   1 
ATOM   9697  C  CE2   . TYR C 3 64  ? 195.526 186.597 129.314 1.00 30.43  ? 64  TYR C CE2   1 
ATOM   9698  C  CZ    . TYR C 3 64  ? 194.571 187.038 128.425 1.00 28.77  ? 64  TYR C CZ    1 
ATOM   9699  O  OH    . TYR C 3 64  ? 194.578 186.573 127.131 1.00 33.03  ? 64  TYR C OH    1 
ATOM   9700  N  N     . PHE C 3 65  ? 192.735 190.638 134.088 1.00 28.41  ? 65  PHE C N     1 
ATOM   9701  C  CA    . PHE C 3 65  ? 192.128 190.833 135.396 1.00 21.42  ? 65  PHE C CA    1 
ATOM   9702  C  C     . PHE C 3 65  ? 192.095 189.511 136.152 1.00 20.82  ? 65  PHE C C     1 
ATOM   9703  O  O     . PHE C 3 65  ? 191.706 188.474 135.607 1.00 30.32  ? 65  PHE C O     1 
ATOM   9704  C  CB    . PHE C 3 65  ? 190.715 191.398 135.250 1.00 19.54  ? 65  PHE C CB    1 
ATOM   9705  C  CG    . PHE C 3 65  ? 190.680 192.861 134.914 1.00 21.79  ? 65  PHE C CG    1 
ATOM   9706  C  CD1   . PHE C 3 65  ? 190.682 193.816 135.917 1.00 24.41  ? 65  PHE C CD1   1 
ATOM   9707  C  CD2   . PHE C 3 65  ? 190.650 193.282 133.595 1.00 24.35  ? 65  PHE C CD2   1 
ATOM   9708  C  CE1   . PHE C 3 65  ? 190.651 195.163 135.611 1.00 22.53  ? 65  PHE C CE1   1 
ATOM   9709  C  CE2   . PHE C 3 65  ? 190.620 194.628 133.283 1.00 25.70  ? 65  PHE C CE2   1 
ATOM   9710  C  CZ    . PHE C 3 65  ? 190.620 195.569 134.292 1.00 24.85  ? 65  PHE C CZ    1 
ATOM   9711  N  N     . HIS C 3 66  ? 192.508 189.549 137.415 1.00 22.32  ? 66  HIS C N     1 
ATOM   9712  C  CA    . HIS C 3 66  ? 192.635 188.350 138.233 1.00 16.36  ? 66  HIS C CA    1 
ATOM   9713  C  C     . HIS C 3 66  ? 191.414 188.197 139.128 1.00 17.68  ? 66  HIS C C     1 
ATOM   9714  O  O     . HIS C 3 66  ? 190.961 189.167 139.744 1.00 26.61  ? 66  HIS C O     1 
ATOM   9715  C  CB    . HIS C 3 66  ? 193.907 188.403 139.080 1.00 19.37  ? 66  HIS C CB    1 
ATOM   9716  C  CG    . HIS C 3 66  ? 195.169 188.338 138.278 1.00 22.47  ? 66  HIS C CG    1 
ATOM   9717  N  ND1   . HIS C 3 66  ? 196.411 188.574 138.824 1.00 27.51  ? 66  HIS C ND1   1 
ATOM   9718  C  CD2   . HIS C 3 66  ? 195.380 188.063 136.969 1.00 17.53  ? 66  HIS C CD2   1 
ATOM   9719  C  CE1   . HIS C 3 66  ? 197.333 188.448 137.887 1.00 26.20  ? 66  HIS C CE1   1 
ATOM   9720  N  NE2   . HIS C 3 66  ? 196.734 188.138 136.752 1.00 29.49  ? 66  HIS C NE2   1 
ATOM   9721  N  N     . GLY C 3 67  ? 190.883 186.977 139.192 1.00 21.80  ? 67  GLY C N     1 
ATOM   9722  C  CA    . GLY C 3 67  ? 189.745 186.672 140.030 1.00 14.74  ? 67  GLY C CA    1 
ATOM   9723  C  C     . GLY C 3 67  ? 190.152 186.239 141.425 1.00 13.91  ? 67  GLY C C     1 
ATOM   9724  O  O     . GLY C 3 67  ? 191.310 186.340 141.835 1.00 27.28  ? 67  GLY C O     1 
ATOM   9725  N  N     . ARG C 3 68  ? 189.164 185.743 142.165 1.00 15.08  ? 68  ARG C N     1 
ATOM   9726  C  CA    . ARG C 3 68  ? 189.387 185.305 143.529 1.00 15.14  ? 68  ARG C CA    1 
ATOM   9727  C  C     . ARG C 3 68  ? 190.158 183.986 143.556 1.00 16.47  ? 68  ARG C C     1 
ATOM   9728  O  O     . ARG C 3 68  ? 190.155 183.232 142.580 1.00 29.78  ? 68  ARG C O     1 
ATOM   9729  C  CB    . ARG C 3 68  ? 188.054 185.149 144.255 1.00 20.23  ? 68  ARG C CB    1 
ATOM   9730  C  CG    . ARG C 3 68  ? 187.188 186.394 144.226 1.00 18.21  ? 68  ARG C CG    1 
ATOM   9731  C  CD    . ARG C 3 68  ? 185.944 186.212 145.071 1.00 19.87  ? 68  ARG C CD    1 
ATOM   9732  N  NE    . ARG C 3 68  ? 186.267 185.899 146.458 1.00 12.85  ? 68  ARG C NE    1 
ATOM   9733  C  CZ    . ARG C 3 68  ? 185.433 185.313 147.305 1.00 20.38  ? 68  ARG C CZ    1 
ATOM   9734  N  NH1   . ARG C 3 68  ? 184.211 184.963 146.941 1.00 22.01  ? 68  ARG C NH1   1 
ATOM   9735  N  NH2   . ARG C 3 68  ? 185.836 185.071 148.549 1.00 11.84  ? 68  ARG C NH2   1 
ATOM   9736  N  N     . PRO C 3 69  ? 190.841 183.695 144.664 1.00 20.81  ? 69  PRO C N     1 
ATOM   9737  C  CA    . PRO C 3 69  ? 191.517 182.399 144.792 1.00 19.40  ? 69  PRO C CA    1 
ATOM   9738  C  C     . PRO C 3 69  ? 190.529 181.245 144.711 1.00 16.32  ? 69  PRO C C     1 
ATOM   9739  O  O     . PRO C 3 69  ? 189.370 181.359 145.115 1.00 21.13  ? 69  PRO C O     1 
ATOM   9740  C  CB    . PRO C 3 69  ? 192.169 182.477 146.176 1.00 22.99  ? 69  PRO C CB    1 
ATOM   9741  C  CG    . PRO C 3 69  ? 192.383 183.930 146.401 1.00 24.83  ? 69  PRO C CG    1 
ATOM   9742  C  CD    . PRO C 3 69  ? 191.215 184.620 145.749 1.00 21.66  ? 69  PRO C CD    1 
ATOM   9743  N  N     . SER C 3 70  ? 191.002 180.125 144.173 1.00 15.09  ? 70  SER C N     1 
ATOM   9744  C  CA    . SER C 3 70  ? 190.196 178.921 144.012 1.00 16.94  ? 70  SER C CA    1 
ATOM   9745  C  C     . SER C 3 70  ? 190.866 177.776 144.757 1.00 20.99  ? 70  SER C C     1 
ATOM   9746  O  O     . SER C 3 70  ? 192.013 177.427 144.460 1.00 26.19  ? 70  SER C O     1 
ATOM   9747  C  CB    . SER C 3 70  ? 190.021 178.574 142.532 1.00 12.61  ? 70  SER C CB    1 
ATOM   9748  O  OG    . SER C 3 70  ? 189.579 177.239 142.370 1.00 17.39  ? 70  SER C OG    1 
ATOM   9749  N  N     . ALA C 3 71  ? 190.155 177.202 145.722 1.00 20.22  ? 71  ALA C N     1 
ATOM   9750  C  CA    . ALA C 3 71  ? 190.678 176.094 146.521 1.00 24.98  ? 71  ALA C CA    1 
ATOM   9751  C  C     . ALA C 3 71  ? 190.184 174.752 145.981 1.00 21.14  ? 71  ALA C C     1 
ATOM   9752  O  O     . ALA C 3 71  ? 189.574 173.951 146.688 1.00 35.75  ? 71  ALA C O     1 
ATOM   9753  C  CB    . ALA C 3 71  ? 190.295 176.276 147.986 1.00 17.83  ? 71  ALA C CB    1 
ATOM   9754  N  N     . THR C 3 72  ? 190.463 174.507 144.706 1.00 34.31  ? 72  THR C N     1 
ATOM   9755  C  CA    . THR C 3 72  ? 190.125 173.232 144.093 1.00 26.33  ? 72  THR C CA    1 
ATOM   9756  C  C     . THR C 3 72  ? 191.227 172.210 144.365 1.00 26.31  ? 72  THR C C     1 
ATOM   9757  O  O     . THR C 3 72  ? 192.333 172.551 144.792 1.00 42.37  ? 72  THR C O     1 
ATOM   9758  C  CB    . THR C 3 72  ? 189.899 173.388 142.589 1.00 30.88  ? 72  THR C CB    1 
ATOM   9759  O  OG1   . THR C 3 72  ? 190.934 174.204 142.032 1.00 40.06  ? 72  THR C OG1   1 
ATOM   9760  C  CG2   . THR C 3 72  ? 188.554 174.044 142.321 1.00 18.57  ? 72  THR C CG2   1 
ATOM   9761  N  N     . ALA C 3 73  ? 190.907 170.940 144.110 1.00 29.78  ? 73  ALA C N     1 
ATOM   9762  C  CA    . ALA C 3 73  ? 191.773 169.850 144.551 1.00 34.40  ? 73  ALA C CA    1 
ATOM   9763  C  C     . ALA C 3 73  ? 193.107 169.850 143.809 1.00 38.83  ? 73  ALA C C     1 
ATOM   9764  O  O     . ALA C 3 73  ? 194.168 170.029 144.417 1.00 46.69  ? 73  ALA C O     1 
ATOM   9765  C  CB    . ALA C 3 73  ? 191.057 168.511 144.371 1.00 32.04  ? 73  ALA C CB    1 
ATOM   9766  N  N     . GLU C 3 74  ? 193.074 169.649 142.491 1.00 37.76  ? 74  GLU C N     1 
ATOM   9767  C  CA    . GLU C 3 74  ? 194.314 169.475 141.739 1.00 37.00  ? 74  GLU C CA    1 
ATOM   9768  C  C     . GLU C 3 74  ? 194.948 170.815 141.380 1.00 35.97  ? 74  GLU C C     1 
ATOM   9769  O  O     . GLU C 3 74  ? 196.076 171.111 141.789 1.00 42.40  ? 74  GLU C O     1 
ATOM   9770  C  CB    . GLU C 3 74  ? 194.049 168.646 140.479 1.00 36.77  ? 74  GLU C CB    1 
ATOM   9771  C  CG    . GLU C 3 74  ? 193.481 167.264 140.759 1.00 37.77  ? 74  GLU C CG    1 
ATOM   9772  C  CD    . GLU C 3 74  ? 192.638 166.735 139.615 1.00 45.57  ? 74  GLU C CD    1 
ATOM   9773  O  OE1   . GLU C 3 74  ? 193.197 166.497 138.525 1.00 47.16  ? 74  GLU C OE1   1 
ATOM   9774  O  OE2   . GLU C 3 74  ? 191.417 166.557 139.807 1.00 47.09  ? 74  GLU C OE2   1 
ATOM   9775  N  N     . MET C 3 75  ? 194.240 171.633 140.616 1.00 36.11  ? 75  MET C N     1 
ATOM   9776  C  CA    . MET C 3 75  ? 194.709 172.934 140.173 1.00 26.34  ? 75  MET C CA    1 
ATOM   9777  C  C     . MET C 3 75  ? 193.629 173.968 140.438 1.00 28.62  ? 75  MET C C     1 
ATOM   9778  O  O     . MET C 3 75  ? 192.445 173.626 140.535 1.00 40.30  ? 75  MET C O     1 
ATOM   9779  C  CB    . MET C 3 75  ? 195.065 172.916 138.678 1.00 27.75  ? 75  MET C CB    1 
ATOM   9780  C  CG    . MET C 3 75  ? 193.870 172.760 137.754 1.00 31.11  ? 75  MET C CG    1 
ATOM   9781  S  SD    . MET C 3 75  ? 193.326 171.050 137.597 1.00 53.08  ? 75  MET C SD    1 
ATOM   9782  C  CE    . MET C 3 75  ? 192.580 171.082 135.969 1.00 36.37  ? 75  MET C CE    1 
ATOM   9783  N  N     . PRO C 3 76  ? 194.003 175.240 140.583 1.00 29.29  ? 76  PRO C N     1 
ATOM   9784  C  CA    . PRO C 3 76  ? 192.989 176.280 140.797 1.00 23.95  ? 76  PRO C CA    1 
ATOM   9785  C  C     . PRO C 3 76  ? 191.997 176.336 139.644 1.00 20.49  ? 76  PRO C C     1 
ATOM   9786  O  O     . PRO C 3 76  ? 192.360 176.164 138.478 1.00 25.60  ? 76  PRO C O     1 
ATOM   9787  C  CB    . PRO C 3 76  ? 193.813 177.571 140.901 1.00 22.12  ? 76  PRO C CB    1 
ATOM   9788  C  CG    . PRO C 3 76  ? 195.170 177.226 140.370 1.00 26.53  ? 76  PRO C CG    1 
ATOM   9789  C  CD    . PRO C 3 76  ? 195.370 175.778 140.664 1.00 28.76  ? 76  PRO C CD    1 
ATOM   9790  N  N     . TYR C 3 77  ? 190.731 176.576 139.990 1.00 20.99  ? 77  TYR C N     1 
ATOM   9791  C  CA    . TYR C 3 77  ? 189.627 176.633 139.032 1.00 13.59  ? 77  TYR C CA    1 
ATOM   9792  C  C     . TYR C 3 77  ? 189.516 175.328 138.240 1.00 15.78  ? 77  TYR C C     1 
ATOM   9793  O  O     . TYR C 3 77  ? 189.584 175.300 137.010 1.00 15.77  ? 77  TYR C O     1 
ATOM   9794  C  CB    . TYR C 3 77  ? 189.770 177.843 138.102 1.00 13.84  ? 77  TYR C CB    1 
ATOM   9795  C  CG    . TYR C 3 77  ? 189.509 179.162 138.789 1.00 21.67  ? 77  TYR C CG    1 
ATOM   9796  C  CD1   . TYR C 3 77  ? 188.214 179.630 138.965 1.00 17.74  ? 77  TYR C CD1   1 
ATOM   9797  C  CD2   . TYR C 3 77  ? 190.557 179.934 139.275 1.00 17.19  ? 77  TYR C CD2   1 
ATOM   9798  C  CE1   . TYR C 3 77  ? 187.969 180.833 139.597 1.00 18.39  ? 77  TYR C CE1   1 
ATOM   9799  C  CE2   . TYR C 3 77  ? 190.322 181.138 139.908 1.00 19.89  ? 77  TYR C CE2   1 
ATOM   9800  C  CZ    . TYR C 3 77  ? 189.026 181.582 140.067 1.00 32.14  ? 77  TYR C CZ    1 
ATOM   9801  O  OH    . TYR C 3 77  ? 188.788 182.781 140.697 1.00 29.18  ? 77  TYR C OH    1 
ATOM   9802  N  N     . ASN C 3 78  ? 189.337 174.235 138.982 1.00 12.91  ? 78  ASN C N     1 
ATOM   9803  C  CA    . ASN C 3 78  ? 189.153 172.920 138.389 1.00 18.63  ? 78  ASN C CA    1 
ATOM   9804  C  C     . ASN C 3 78  ? 187.686 172.535 138.494 1.00 17.08  ? 78  ASN C C     1 
ATOM   9805  O  O     . ASN C 3 78  ? 187.209 172.255 139.604 1.00 20.75  ? 78  ASN C O     1 
ATOM   9806  C  CB    . ASN C 3 78  ? 190.030 171.884 139.090 1.00 22.77  ? 78  ASN C CB    1 
ATOM   9807  C  CG    . ASN C 3 78  ? 189.810 170.478 138.565 1.00 19.94  ? 78  ASN C CG    1 
ATOM   9808  O  OD1   . ASN C 3 78  ? 189.389 170.284 137.425 1.00 30.44  ? 78  ASN C OD1   1 
ATOM   9809  N  ND2   . ASN C 3 78  ? 190.099 169.486 139.398 1.00 22.90  ? 78  ASN C ND2   1 
ATOM   9810  N  N     . PRO C 3 79  ? 186.935 172.502 137.388 1.00 18.23  ? 79  PRO C N     1 
ATOM   9811  C  CA    . PRO C 3 79  ? 185.505 172.170 137.486 1.00 20.92  ? 79  PRO C CA    1 
ATOM   9812  C  C     . PRO C 3 79  ? 185.236 170.719 137.839 1.00 22.74  ? 79  PRO C C     1 
ATOM   9813  O  O     . PRO C 3 79  ? 184.106 170.395 138.222 1.00 37.08  ? 79  PRO C O     1 
ATOM   9814  C  CB    . PRO C 3 79  ? 184.958 172.518 136.091 1.00 21.02  ? 79  PRO C CB    1 
ATOM   9815  C  CG    . PRO C 3 79  ? 186.117 173.096 135.311 1.00 24.80  ? 79  PRO C CG    1 
ATOM   9816  C  CD    . PRO C 3 79  ? 187.372 172.685 135.997 1.00 10.55  ? 79  PRO C CD    1 
ATOM   9817  N  N     . GLN C 3 80  ? 186.228 169.836 137.725 1.00 21.55  ? 80  GLN C N     1 
ATOM   9818  C  CA    . GLN C 3 80  ? 186.051 168.444 138.117 1.00 17.90  ? 80  GLN C CA    1 
ATOM   9819  C  C     . GLN C 3 80  ? 186.079 168.243 139.626 1.00 15.65  ? 80  GLN C C     1 
ATOM   9820  O  O     . GLN C 3 80  ? 185.617 167.202 140.103 1.00 29.25  ? 80  GLN C O     1 
ATOM   9821  C  CB    . GLN C 3 80  ? 187.123 167.571 137.459 1.00 19.44  ? 80  GLN C CB    1 
ATOM   9822  C  CG    . GLN C 3 80  ? 186.955 167.433 135.957 1.00 20.29  ? 80  GLN C CG    1 
ATOM   9823  C  CD    . GLN C 3 80  ? 185.580 166.922 135.576 1.00 21.74  ? 80  GLN C CD    1 
ATOM   9824  O  OE1   . GLN C 3 80  ? 185.117 165.907 136.096 1.00 32.33  ? 80  GLN C OE1   1 
ATOM   9825  N  NE2   . GLN C 3 80  ? 184.913 167.631 134.674 1.00 20.29  ? 80  GLN C NE2   1 
ATOM   9826  N  N     . ALA C 3 81  ? 186.620 169.194 140.382 1.00 14.89  ? 81  ALA C N     1 
ATOM   9827  C  CA    . ALA C 3 81  ? 186.590 169.144 141.840 1.00 18.11  ? 81  ALA C CA    1 
ATOM   9828  C  C     . ALA C 3 81  ? 186.138 170.491 142.393 1.00 20.48  ? 81  ALA C C     1 
ATOM   9829  O  O     . ALA C 3 81  ? 186.947 171.345 142.757 1.00 34.99  ? 81  ALA C O     1 
ATOM   9830  C  CB    . ALA C 3 81  ? 187.952 168.743 142.402 1.00 21.68  ? 81  ALA C CB    1 
ATOM   9831  N  N     . SER C 3 82  ? 184.825 170.687 142.476 1.00 20.53  ? 82  SER C N     1 
ATOM   9832  C  CA    . SER C 3 82  ? 184.295 171.950 142.970 1.00 18.07  ? 82  SER C CA    1 
ATOM   9833  C  C     . SER C 3 82  ? 184.180 171.923 144.489 1.00 14.41  ? 82  SER C C     1 
ATOM   9834  O  O     . SER C 3 82  ? 183.766 170.923 145.080 1.00 24.58  ? 82  SER C O     1 
ATOM   9835  C  CB    . SER C 3 82  ? 182.932 172.237 142.339 1.00 15.54  ? 82  SER C CB    1 
ATOM   9836  O  OG    . SER C 3 82  ? 181.940 171.363 142.849 1.00 18.20  ? 82  SER C OG    1 
ATOM   9837  N  N     . GLY C 3 83  ? 184.562 173.021 145.120 1.00 17.36  ? 83  GLY C N     1 
ATOM   9838  C  CA    . GLY C 3 83  ? 184.459 173.131 146.561 1.00 17.26  ? 83  GLY C CA    1 
ATOM   9839  C  C     . GLY C 3 83  ? 185.302 174.269 147.083 1.00 15.05  ? 83  GLY C C     1 
ATOM   9840  O  O     . GLY C 3 83  ? 186.078 174.892 146.358 1.00 25.32  ? 83  GLY C O     1 
ATOM   9841  N  N     . GLY C 3 84  ? 185.132 174.535 148.379 1.00 29.01  ? 84  GLY C N     1 
ATOM   9842  C  CA    . GLY C 3 84  ? 185.879 175.567 149.060 1.00 16.77  ? 84  GLY C CA    1 
ATOM   9843  C  C     . GLY C 3 84  ? 187.045 175.007 149.863 1.00 18.32  ? 84  GLY C C     1 
ATOM   9844  O  O     . GLY C 3 84  ? 187.317 173.810 149.886 1.00 34.23  ? 84  GLY C O     1 
ATOM   9845  N  N     . SER C 3 85  ? 187.745 175.923 150.536 1.00 22.84  ? 85  SER C N     1 
ATOM   9846  C  CA    . SER C 3 85  ? 188.870 175.519 151.374 1.00 16.95  ? 85  SER C CA    1 
ATOM   9847  C  C     . SER C 3 85  ? 188.402 174.929 152.697 1.00 20.55  ? 85  SER C C     1 
ATOM   9848  O  O     . SER C 3 85  ? 189.089 174.073 153.267 1.00 20.19  ? 85  SER C O     1 
ATOM   9849  C  CB    . SER C 3 85  ? 189.795 176.711 151.622 1.00 11.77  ? 85  SER C CB    1 
ATOM   9850  O  OG    . SER C 3 85  ? 189.254 177.584 152.597 1.00 18.78  ? 85  SER C OG    1 
ATOM   9851  N  N     . ASN C 3 86  ? 187.245 175.372 153.196 1.00 18.32  ? 86  ASN C N     1 
ATOM   9852  C  CA    . ASN C 3 86  ? 186.698 174.915 154.474 1.00 15.92  ? 86  ASN C CA    1 
ATOM   9853  C  C     . ASN C 3 86  ? 187.673 175.170 155.621 1.00 21.24  ? 86  ASN C C     1 
ATOM   9854  O  O     . ASN C 3 86  ? 187.751 174.399 156.579 1.00 30.08  ? 86  ASN C O     1 
ATOM   9855  C  CB    . ASN C 3 86  ? 186.301 173.438 154.413 1.00 18.83  ? 86  ASN C CB    1 
ATOM   9856  C  CG    . ASN C 3 86  ? 185.214 173.171 153.395 1.00 16.64  ? 86  ASN C CG    1 
ATOM   9857  O  OD1   . ASN C 3 86  ? 184.139 173.766 153.449 1.00 20.75  ? 86  ASN C OD1   1 
ATOM   9858  N  ND2   . ASN C 3 86  ? 185.489 172.273 152.457 1.00 15.27  ? 86  ASN C ND2   1 
ATOM   9859  N  N     . LEU C 3 87  ? 188.420 176.266 155.526 1.00 16.24  ? 87  LEU C N     1 
ATOM   9860  C  CA    . LEU C 3 87  ? 189.382 176.636 156.553 1.00 16.31  ? 87  LEU C CA    1 
ATOM   9861  C  C     . LEU C 3 87  ? 188.712 177.541 157.579 1.00 11.54  ? 87  LEU C C     1 
ATOM   9862  O  O     . LEU C 3 87  ? 188.034 178.508 157.217 1.00 22.64  ? 87  LEU C O     1 
ATOM   9863  C  CB    . LEU C 3 87  ? 190.592 177.335 155.934 1.00 23.17  ? 87  LEU C CB    1 
ATOM   9864  C  CG    . LEU C 3 87  ? 191.586 176.416 155.222 1.00 21.45  ? 87  LEU C CG    1 
ATOM   9865  C  CD1   . LEU C 3 87  ? 192.625 177.228 154.466 1.00 19.11  ? 87  LEU C CD1   1 
ATOM   9866  C  CD2   . LEU C 3 87  ? 192.250 175.467 156.208 1.00 13.59  ? 87  LEU C CD2   1 
ATOM   9867  N  N     . ALA C 3 88  ? 188.904 177.222 158.855 1.00 20.34  ? 88  ALA C N     1 
ATOM   9868  C  CA    . ALA C 3 88  ? 188.268 177.976 159.922 1.00 11.73  ? 88  ALA C CA    1 
ATOM   9869  C  C     . ALA C 3 88  ? 188.992 179.297 160.162 1.00 15.35  ? 88  ALA C C     1 
ATOM   9870  O  O     . ALA C 3 88  ? 190.141 179.495 159.756 1.00 19.14  ? 88  ALA C O     1 
ATOM   9871  C  CB    . ALA C 3 88  ? 188.235 177.157 161.212 1.00 10.26  ? 88  ALA C CB    1 
ATOM   9872  N  N     . VAL C 3 89  ? 188.291 180.211 160.836 1.00 26.27  ? 89  VAL C N     1 
ATOM   9873  C  CA    . VAL C 3 89  ? 188.880 181.499 161.191 1.00 18.67  ? 89  VAL C CA    1 
ATOM   9874  C  C     . VAL C 3 89  ? 190.074 181.304 162.116 1.00 24.33  ? 89  VAL C C     1 
ATOM   9875  O  O     . VAL C 3 89  ? 191.118 181.948 161.954 1.00 32.08  ? 89  VAL C O     1 
ATOM   9876  C  CB    . VAL C 3 89  ? 187.815 182.413 161.824 1.00 31.13  ? 89  VAL C CB    1 
ATOM   9877  C  CG1   . VAL C 3 89  ? 188.415 183.757 162.194 1.00 24.15  ? 89  VAL C CG1   1 
ATOM   9878  C  CG2   . VAL C 3 89  ? 186.641 182.595 160.874 1.00 28.98  ? 89  VAL C CG2   1 
ATOM   9879  N  N     . SER C 3 90  ? 189.943 180.412 163.097 1.00 28.97  ? 90  SER C N     1 
ATOM   9880  C  CA    . SER C 3 90  ? 191.002 180.163 164.067 1.00 24.99  ? 90  SER C CA    1 
ATOM   9881  C  C     . SER C 3 90  ? 192.136 179.308 163.515 1.00 21.78  ? 90  SER C C     1 
ATOM   9882  O  O     . SER C 3 90  ? 193.161 179.165 164.190 1.00 39.49  ? 90  SER C O     1 
ATOM   9883  C  CB    . SER C 3 90  ? 190.420 179.494 165.316 1.00 22.81  ? 90  SER C CB    1 
ATOM   9884  O  OG    . SER C 3 90  ? 189.568 178.418 164.965 1.00 23.03  ? 90  SER C OG    1 
ATOM   9885  N  N     . ASN C 3 91  ? 191.984 178.740 162.327 1.00 15.83  ? 91  ASN C N     1 
ATOM   9886  C  CA    . ASN C 3 91  ? 193.029 177.896 161.756 1.00 21.76  ? 91  ASN C CA    1 
ATOM   9887  C  C     . ASN C 3 91  ? 194.213 178.754 161.330 1.00 23.54  ? 91  ASN C C     1 
ATOM   9888  O  O     . ASN C 3 91  ? 194.044 179.657 160.499 1.00 36.14  ? 91  ASN C O     1 
ATOM   9889  C  CB    . ASN C 3 91  ? 192.478 177.112 160.566 1.00 20.88  ? 91  ASN C CB    1 
ATOM   9890  C  CG    . ASN C 3 91  ? 193.324 175.901 160.216 1.00 25.79  ? 91  ASN C CG    1 
ATOM   9891  O  OD1   . ASN C 3 91  ? 194.495 175.816 160.582 1.00 31.40  ? 91  ASN C OD1   1 
ATOM   9892  N  ND2   . ASN C 3 91  ? 192.728 174.952 159.504 1.00 27.17  ? 91  ASN C ND2   1 
ATOM   9893  N  N     . PRO C 3 92  ? 195.415 178.521 161.864 1.00 30.45  ? 92  PRO C N     1 
ATOM   9894  C  CA    . PRO C 3 92  ? 196.573 179.332 161.450 1.00 29.44  ? 92  PRO C CA    1 
ATOM   9895  C  C     . PRO C 3 92  ? 196.956 179.154 159.992 1.00 25.96  ? 92  PRO C C     1 
ATOM   9896  O  O     . PRO C 3 92  ? 197.656 180.016 159.444 1.00 27.80  ? 92  PRO C O     1 
ATOM   9897  C  CB    . PRO C 3 92  ? 197.690 178.852 162.387 1.00 20.86  ? 92  PRO C CB    1 
ATOM   9898  C  CG    . PRO C 3 92  ? 197.258 177.493 162.831 1.00 31.62  ? 92  PRO C CG    1 
ATOM   9899  C  CD    . PRO C 3 92  ? 195.764 177.558 162.921 1.00 27.47  ? 92  PRO C CD    1 
ATOM   9900  N  N     . GLU C 3 93  ? 196.528 178.068 159.345 1.00 25.75  ? 93  GLU C N     1 
ATOM   9901  C  CA    . GLU C 3 93  ? 196.860 177.872 157.937 1.00 27.85  ? 93  GLU C CA    1 
ATOM   9902  C  C     . GLU C 3 93  ? 196.138 178.883 157.055 1.00 27.39  ? 93  GLU C C     1 
ATOM   9903  O  O     . GLU C 3 93  ? 196.618 179.225 155.968 1.00 31.06  ? 93  GLU C O     1 
ATOM   9904  C  CB    . GLU C 3 93  ? 196.517 176.445 157.510 1.00 25.75  ? 93  GLU C CB    1 
ATOM   9905  C  CG    . GLU C 3 93  ? 197.118 175.368 158.399 1.00 32.36  ? 93  GLU C CG    1 
ATOM   9906  C  CD    . GLU C 3 93  ? 198.535 174.996 158.000 1.00 40.96  ? 93  GLU C CD    1 
ATOM   9907  O  OE1   . GLU C 3 93  ? 199.129 175.709 157.165 1.00 43.25  ? 93  GLU C OE1   1 
ATOM   9908  O  OE2   . GLU C 3 93  ? 199.054 173.988 158.524 1.00 37.82  ? 93  GLU C OE2   1 
ATOM   9909  N  N     . LEU C 3 94  ? 194.982 179.375 157.507 1.00 22.14  ? 94  LEU C N     1 
ATOM   9910  C  CA    . LEU C 3 94  ? 194.268 180.395 156.747 1.00 25.32  ? 94  LEU C CA    1 
ATOM   9911  C  C     . LEU C 3 94  ? 195.006 181.727 156.789 1.00 23.59  ? 94  LEU C C     1 
ATOM   9912  O  O     . LEU C 3 94  ? 195.078 182.438 155.779 1.00 28.48  ? 94  LEU C O     1 
ATOM   9913  C  CB    . LEU C 3 94  ? 192.845 180.550 157.284 1.00 21.29  ? 94  LEU C CB    1 
ATOM   9914  C  CG    . LEU C 3 94  ? 191.940 181.536 156.544 1.00 21.01  ? 94  LEU C CG    1 
ATOM   9915  C  CD1   . LEU C 3 94  ? 191.815 181.158 155.077 1.00 27.17  ? 94  LEU C CD1   1 
ATOM   9916  C  CD2   . LEU C 3 94  ? 190.571 181.606 157.202 1.00 27.01  ? 94  LEU C CD2   1 
ATOM   9917  N  N     . ASP C 3 95  ? 195.559 182.082 157.951 1.00 21.11  ? 95  ASP C N     1 
ATOM   9918  C  CA    . ASP C 3 95  ? 196.334 183.314 158.058 1.00 23.13  ? 95  ASP C CA    1 
ATOM   9919  C  C     . ASP C 3 95  ? 197.580 183.258 157.185 1.00 25.92  ? 95  ASP C C     1 
ATOM   9920  O  O     . ASP C 3 95  ? 197.967 184.262 156.574 1.00 30.17  ? 95  ASP C O     1 
ATOM   9921  C  CB    . ASP C 3 95  ? 196.710 183.572 159.517 1.00 25.02  ? 95  ASP C CB    1 
ATOM   9922  C  CG    . ASP C 3 95  ? 195.500 183.645 160.427 1.00 42.22  ? 95  ASP C CG    1 
ATOM   9923  O  OD1   . ASP C 3 95  ? 194.443 184.132 159.975 1.00 42.26  ? 95  ASP C OD1   1 
ATOM   9924  O  OD2   . ASP C 3 95  ? 195.606 183.213 161.594 1.00 45.48  ? 95  ASP C OD2   1 
ATOM   9925  N  N     . LYS C 3 96  ? 198.230 182.093 157.124 1.00 28.12  ? 96  LYS C N     1 
ATOM   9926  C  CA    . LYS C 3 96  ? 199.407 181.943 156.274 1.00 29.01  ? 96  LYS C CA    1 
ATOM   9927  C  C     . LYS C 3 96  ? 199.056 182.134 154.804 1.00 28.74  ? 96  LYS C C     1 
ATOM   9928  O  O     . LYS C 3 96  ? 199.794 182.794 154.063 1.00 30.74  ? 96  LYS C O     1 
ATOM   9929  C  CB    . LYS C 3 96  ? 200.040 180.570 156.500 1.00 28.28  ? 96  LYS C CB    1 
ATOM   9930  C  CG    . LYS C 3 96  ? 201.472 180.451 156.000 1.00 32.11  ? 96  LYS C CG    1 
ATOM   9931  C  CD    . LYS C 3 96  ? 201.836 179.012 155.644 1.00 35.68  ? 96  LYS C CD    1 
ATOM   9932  C  CE    . LYS C 3 96  ? 201.554 178.031 156.778 1.00 38.92  ? 96  LYS C CE    1 
ATOM   9933  N  NZ    . LYS C 3 96  ? 201.841 178.582 158.135 1.00 39.75  ? 96  LYS C NZ    1 
ATOM   9934  N  N     . LEU C 3 97  ? 197.936 181.557 154.362 1.00 28.14  ? 97  LEU C N     1 
ATOM   9935  C  CA    . LEU C 3 97  ? 197.521 181.707 152.971 1.00 23.39  ? 97  LEU C CA    1 
ATOM   9936  C  C     . LEU C 3 97  ? 197.164 183.152 152.647 1.00 25.68  ? 97  LEU C C     1 
ATOM   9937  O  O     . LEU C 3 97  ? 197.514 183.658 151.575 1.00 27.41  ? 97  LEU C O     1 
ATOM   9938  C  CB    . LEU C 3 97  ? 196.338 180.785 152.675 1.00 24.92  ? 97  LEU C CB    1 
ATOM   9939  C  CG    . LEU C 3 97  ? 196.672 179.340 152.304 1.00 28.50  ? 97  LEU C CG    1 
ATOM   9940  C  CD1   . LEU C 3 97  ? 195.435 178.465 152.409 1.00 24.93  ? 97  LEU C CD1   1 
ATOM   9941  C  CD2   . LEU C 3 97  ? 197.266 179.267 150.908 1.00 27.51  ? 97  LEU C CD2   1 
ATOM   9942  N  N     . ILE C 3 98  ? 196.462 183.830 153.559 1.00 23.57  ? 98  ILE C N     1 
ATOM   9943  C  CA    . ILE C 3 98  ? 196.056 185.212 153.311 1.00 23.92  ? 98  ILE C CA    1 
ATOM   9944  C  C     . ILE C 3 98  ? 197.276 186.120 153.222 1.00 22.93  ? 98  ILE C C     1 
ATOM   9945  O  O     . ILE C 3 98  ? 197.353 186.996 152.352 1.00 29.21  ? 98  ILE C O     1 
ATOM   9946  C  CB    . ILE C 3 98  ? 195.072 185.682 154.399 1.00 27.59  ? 98  ILE C CB    1 
ATOM   9947  C  CG1   . ILE C 3 98  ? 193.694 185.058 154.175 1.00 29.45  ? 98  ILE C CG1   1 
ATOM   9948  C  CG2   . ILE C 3 98  ? 194.960 187.198 154.402 1.00 23.46  ? 98  ILE C CG2   1 
ATOM   9949  C  CD1   . ILE C 3 98  ? 192.813 185.070 155.403 1.00 29.52  ? 98  ILE C CD1   1 
ATOM   9950  N  N     . ALA C 3 99  ? 198.248 185.924 154.117 1.00 26.04  ? 99  ALA C N     1 
ATOM   9951  C  CA    . ALA C 3 99  ? 199.457 186.742 154.091 1.00 23.19  ? 99  ALA C CA    1 
ATOM   9952  C  C     . ALA C 3 99  ? 200.228 186.549 152.792 1.00 23.07  ? 99  ALA C C     1 
ATOM   9953  O  O     . ALA C 3 99  ? 200.771 187.511 152.235 1.00 29.49  ? 99  ALA C O     1 
ATOM   9954  C  CB    . ALA C 3 99  ? 200.341 186.412 155.294 1.00 24.40  ? 99  ALA C CB    1 
ATOM   9955  N  N     . ALA C 3 100 ? 200.297 185.311 152.299 1.00 21.82  ? 100 ALA C N     1 
ATOM   9956  C  CA    . ALA C 3 100 ? 200.968 185.058 151.028 1.00 24.24  ? 100 ALA C CA    1 
ATOM   9957  C  C     . ALA C 3 100 ? 200.241 185.736 149.872 1.00 22.88  ? 100 ALA C C     1 
ATOM   9958  O  O     . ALA C 3 100 ? 200.880 186.305 148.979 1.00 28.07  ? 100 ALA C O     1 
ATOM   9959  C  CB    . ALA C 3 100 ? 201.083 183.555 150.783 1.00 22.81  ? 100 ALA C CB    1 
ATOM   9960  N  N     . ARG C 3 101 ? 198.907 185.685 149.870 1.00 18.30  ? 101 ARG C N     1 
ATOM   9961  C  CA    . ARG C 3 101 ? 198.143 186.328 148.805 1.00 20.73  ? 101 ARG C CA    1 
ATOM   9962  C  C     . ARG C 3 101 ? 198.250 187.846 148.882 1.00 21.79  ? 101 ARG C C     1 
ATOM   9963  O  O     . ARG C 3 101 ? 198.311 188.521 147.849 1.00 30.30  ? 101 ARG C O     1 
ATOM   9964  C  CB    . ARG C 3 101 ? 196.681 185.887 148.864 1.00 15.12  ? 101 ARG C CB    1 
ATOM   9965  C  CG    . ARG C 3 101 ? 196.455 184.432 148.493 1.00 19.29  ? 101 ARG C CG    1 
ATOM   9966  C  CD    . ARG C 3 101 ? 195.081 183.957 148.929 1.00 17.55  ? 101 ARG C CD    1 
ATOM   9967  N  NE    . ARG C 3 101 ? 194.954 182.506 148.853 1.00 26.96  ? 101 ARG C NE    1 
ATOM   9968  C  CZ    . ARG C 3 101 ? 194.033 181.800 149.493 1.00 20.50  ? 101 ARG C CZ    1 
ATOM   9969  N  NH1   . ARG C 3 101 ? 193.136 182.379 150.274 1.00 13.34  ? 101 ARG C NH1   1 
ATOM   9970  N  NH2   . ARG C 3 101 ? 194.010 180.479 149.345 1.00 25.20  ? 101 ARG C NH2   1 
ATOM   9971  N  N     . VAL C 3 102 ? 198.265 188.400 150.097 1.00 22.29  ? 102 VAL C N     1 
ATOM   9972  C  CA    . VAL C 3 102 ? 198.398 189.847 150.252 1.00 22.19  ? 102 VAL C CA    1 
ATOM   9973  C  C     . VAL C 3 102 ? 199.751 190.316 149.730 1.00 24.96  ? 102 VAL C C     1 
ATOM   9974  O  O     . VAL C 3 102 ? 199.842 191.316 149.007 1.00 26.72  ? 102 VAL C O     1 
ATOM   9975  C  CB    . VAL C 3 102 ? 198.186 190.247 151.725 1.00 24.83  ? 102 VAL C CB    1 
ATOM   9976  C  CG1   . VAL C 3 102 ? 198.821 191.601 152.012 1.00 21.83  ? 102 VAL C CG1   1 
ATOM   9977  C  CG2   . VAL C 3 102 ? 196.703 190.267 152.061 1.00 25.86  ? 102 VAL C CG2   1 
ATOM   9978  N  N     . ALA C 3 103 ? 200.821 189.598 150.082 1.00 24.99  ? 103 ALA C N     1 
ATOM   9979  C  CA    . ALA C 3 103 ? 202.152 189.973 149.613 1.00 23.44  ? 103 ALA C CA    1 
ATOM   9980  C  C     . ALA C 3 103 ? 202.268 189.832 148.100 1.00 25.52  ? 103 ALA C C     1 
ATOM   9981  O  O     . ALA C 3 103 ? 202.866 190.686 147.434 1.00 33.19  ? 103 ALA C O     1 
ATOM   9982  C  CB    . ALA C 3 103 ? 203.213 189.126 150.315 1.00 19.79  ? 103 ALA C CB    1 
ATOM   9983  N  N     . ALA C 3 104 ? 201.709 188.756 147.539 1.00 29.34  ? 104 ALA C N     1 
ATOM   9984  C  CA    . ALA C 3 104 ? 201.776 188.554 146.095 1.00 22.14  ? 104 ALA C CA    1 
ATOM   9985  C  C     . ALA C 3 104 ? 201.010 189.638 145.346 1.00 24.45  ? 104 ALA C C     1 
ATOM   9986  O  O     . ALA C 3 104 ? 201.485 190.152 144.327 1.00 31.13  ? 104 ALA C O     1 
ATOM   9987  C  CB    . ALA C 3 104 ? 201.240 187.169 145.733 1.00 16.18  ? 104 ALA C CB    1 
ATOM   9988  N  N     . LEU C 3 105 ? 199.819 189.995 145.833 1.00 21.71  ? 105 LEU C N     1 
ATOM   9989  C  CA    . LEU C 3 105 ? 199.039 191.043 145.182 1.00 22.16  ? 105 LEU C CA    1 
ATOM   9990  C  C     . LEU C 3 105 ? 199.706 192.404 145.333 1.00 24.67  ? 105 LEU C C     1 
ATOM   9991  O  O     . LEU C 3 105 ? 199.669 193.225 144.409 1.00 31.22  ? 105 LEU C O     1 
ATOM   9992  C  CB    . LEU C 3 105 ? 197.621 191.074 145.752 1.00 20.61  ? 105 LEU C CB    1 
ATOM   9993  C  CG    . LEU C 3 105 ? 196.663 189.992 145.253 1.00 28.41  ? 105 LEU C CG    1 
ATOM   9994  C  CD1   . LEU C 3 105 ? 195.615 189.674 146.306 1.00 24.94  ? 105 LEU C CD1   1 
ATOM   9995  C  CD2   . LEU C 3 105 ? 196.006 190.419 143.951 1.00 22.76  ? 105 LEU C CD2   1 
ATOM   9996  N  N     . ARG C 3 106 ? 200.313 192.663 146.493 1.00 29.27  ? 106 ARG C N     1 
ATOM   9997  C  CA    . ARG C 3 106 ? 200.962 193.950 146.722 1.00 23.32  ? 106 ARG C CA    1 
ATOM   9998  C  C     . ARG C 3 106 ? 202.141 194.149 145.777 1.00 25.72  ? 106 ARG C C     1 
ATOM   9999  O  O     . ARG C 3 106 ? 202.341 195.247 145.245 1.00 32.72  ? 106 ARG C O     1 
ATOM   10000 C  CB    . ARG C 3 106 ? 201.415 194.050 148.178 1.00 22.57  ? 106 ARG C CB    1 
ATOM   10001 C  CG    . ARG C 3 106 ? 200.433 194.769 149.086 1.00 23.96  ? 106 ARG C CG    1 
ATOM   10002 C  CD    . ARG C 3 106 ? 200.898 194.736 150.531 1.00 25.69  ? 106 ARG C CD    1 
ATOM   10003 N  NE    . ARG C 3 106 ? 199.976 195.434 151.419 1.00 27.68  ? 106 ARG C NE    1 
ATOM   10004 C  CZ    . ARG C 3 106 ? 199.904 195.237 152.728 1.00 23.25  ? 106 ARG C CZ    1 
ATOM   10005 N  NH1   . ARG C 3 106 ? 200.693 194.370 153.341 1.00 28.50  ? 106 ARG C NH1   1 
ATOM   10006 N  NH2   . ARG C 3 106 ? 199.019 195.928 153.441 1.00 28.88  ? 106 ARG C NH2   1 
ATOM   10007 N  N     . ALA C 3 107 ? 202.934 193.098 145.560 1.00 28.02  ? 107 ALA C N     1 
ATOM   10008 C  CA    . ALA C 3 107 ? 204.076 193.205 144.658 1.00 28.19  ? 107 ALA C CA    1 
ATOM   10009 C  C     . ALA C 3 107 ? 203.629 193.350 143.209 1.00 30.86  ? 107 ALA C C     1 
ATOM   10010 O  O     . ALA C 3 107 ? 204.262 194.069 142.428 1.00 36.61  ? 107 ALA C O     1 
ATOM   10011 C  CB    . ALA C 3 107 ? 204.988 191.989 144.820 1.00 27.01  ? 107 ALA C CB    1 
ATOM   10012 N  N     . ALA C 3 108 ? 202.541 192.676 142.830 1.00 32.17  ? 108 ALA C N     1 
ATOM   10013 C  CA    . ALA C 3 108 ? 202.069 192.739 141.452 1.00 26.76  ? 108 ALA C CA    1 
ATOM   10014 C  C     . ALA C 3 108 ? 201.285 194.011 141.163 1.00 27.71  ? 108 ALA C C     1 
ATOM   10015 O  O     . ALA C 3 108 ? 201.037 194.318 139.992 1.00 31.96  ? 108 ALA C O     1 
ATOM   10016 C  CB    . ALA C 3 108 ? 201.208 191.516 141.134 1.00 21.34  ? 108 ALA C CB    1 
ATOM   10017 N  N     . ASN C 3 109 ? 200.894 194.757 142.193 1.00 30.07  ? 109 ASN C N     1 
ATOM   10018 C  CA    . ASN C 3 109 ? 200.149 196.005 142.038 1.00 25.16  ? 109 ASN C CA    1 
ATOM   10019 C  C     . ASN C 3 109 ? 200.825 197.090 142.867 1.00 29.43  ? 109 ASN C C     1 
ATOM   10020 O  O     . ASN C 3 109 ? 200.304 197.516 143.904 1.00 39.36  ? 109 ASN C O     1 
ATOM   10021 C  CB    . ASN C 3 109 ? 198.688 195.825 142.452 1.00 26.94  ? 109 ASN C CB    1 
ATOM   10022 C  CG    . ASN C 3 109 ? 198.000 194.708 141.691 1.00 27.95  ? 109 ASN C CG    1 
ATOM   10023 O  OD1   . ASN C 3 109 ? 197.403 194.933 140.640 1.00 32.22  ? 109 ASN C OD1   1 
ATOM   10024 N  ND2   . ASN C 3 109 ? 198.084 193.493 142.221 1.00 21.68  ? 109 ASN C ND2   1 
ATOM   10025 N  N     . PRO C 3 110 ? 201.995 197.563 142.432 1.00 35.06  ? 110 PRO C N     1 
ATOM   10026 C  CA    . PRO C 3 110 ? 202.704 198.578 143.225 1.00 35.41  ? 110 PRO C CA    1 
ATOM   10027 C  C     . PRO C 3 110 ? 202.103 199.966 143.106 1.00 34.96  ? 110 PRO C C     1 
ATOM   10028 O  O     . PRO C 3 110 ? 202.402 200.834 143.936 1.00 40.72  ? 110 PRO C O     1 
ATOM   10029 C  CB    . PRO C 3 110 ? 204.124 198.521 142.652 1.00 37.19  ? 110 PRO C CB    1 
ATOM   10030 C  CG    . PRO C 3 110 ? 203.906 198.176 141.217 1.00 35.26  ? 110 PRO C CG    1 
ATOM   10031 C  CD    . PRO C 3 110 ? 202.710 197.246 141.182 1.00 35.26  ? 110 PRO C CD    1 
ATOM   10032 N  N     . ASP C 3 111 ? 201.263 200.204 142.102 1.00 35.38  ? 111 ASP C N     1 
ATOM   10033 C  CA    . ASP C 3 111 ? 200.634 201.502 141.902 1.00 35.84  ? 111 ASP C CA    1 
ATOM   10034 C  C     . ASP C 3 111 ? 199.237 201.584 142.502 1.00 39.53  ? 111 ASP C C     1 
ATOM   10035 O  O     . ASP C 3 111 ? 198.566 202.606 142.333 1.00 42.20  ? 111 ASP C O     1 
ATOM   10036 C  CB    . ASP C 3 111 ? 200.573 201.833 140.407 1.00 38.17  ? 111 ASP C CB    1 
ATOM   10037 C  CG    . ASP C 3 111 ? 201.936 201.795 139.747 1.00 42.39  ? 111 ASP C CG    1 
ATOM   10038 O  OD1   . ASP C 3 111 ? 202.760 202.690 140.031 1.00 45.77  ? 111 ASP C OD1   1 
ATOM   10039 O  OD2   . ASP C 3 111 ? 202.184 200.872 138.944 1.00 44.74  ? 111 ASP C OD2   1 
ATOM   10040 N  N     . ALA C 3 112 ? 198.786 200.541 143.190 1.00 35.46  ? 112 ALA C N     1 
ATOM   10041 C  CA    . ALA C 3 112 ? 197.477 200.541 143.820 1.00 33.56  ? 112 ALA C CA    1 
ATOM   10042 C  C     . ALA C 3 112 ? 197.609 200.772 145.323 1.00 37.69  ? 112 ALA C C     1 
ATOM   10043 O  O     . ALA C 3 112 ? 198.708 200.866 145.873 1.00 42.80  ? 112 ALA C O     1 
ATOM   10044 C  CB    . ALA C 3 112 ? 196.748 199.227 143.540 1.00 31.05  ? 112 ALA C CB    1 
ATOM   10045 N  N     . SER C 3 113 ? 196.462 200.866 145.989 1.00 35.42  ? 113 SER C N     1 
ATOM   10046 C  CA    . SER C 3 113 ? 196.449 201.066 147.430 1.00 33.56  ? 113 SER C CA    1 
ATOM   10047 C  C     . SER C 3 113 ? 196.967 199.826 148.149 1.00 32.36  ? 113 SER C C     1 
ATOM   10048 O  O     . SER C 3 113 ? 196.772 198.692 147.704 1.00 36.84  ? 113 SER C O     1 
ATOM   10049 C  CB    . SER C 3 113 ? 195.037 201.399 147.910 1.00 33.56  ? 113 SER C CB    1 
ATOM   10050 O  OG    . SER C 3 113 ? 194.805 200.880 149.207 1.00 36.83  ? 113 SER C OG    1 
ATOM   10051 N  N     . ALA C 3 114 ? 197.643 200.056 149.278 1.00 38.48  ? 114 ALA C N     1 
ATOM   10052 C  CA    . ALA C 3 114 ? 198.174 198.952 150.069 1.00 30.71  ? 114 ALA C CA    1 
ATOM   10053 C  C     . ALA C 3 114 ? 197.075 198.086 150.670 1.00 29.26  ? 114 ALA C C     1 
ATOM   10054 O  O     . ALA C 3 114 ? 197.329 196.919 150.988 1.00 33.24  ? 114 ALA C O     1 
ATOM   10055 C  CB    . ALA C 3 114 ? 199.080 199.485 151.178 1.00 33.23  ? 114 ALA C CB    1 
ATOM   10056 N  N     . SER C 3 115 ? 195.868 198.623 150.832 1.00 32.70  ? 115 SER C N     1 
ATOM   10057 C  CA    . SER C 3 115 ? 194.743 197.870 151.384 1.00 30.56  ? 115 SER C CA    1 
ATOM   10058 C  C     . SER C 3 115 ? 194.139 197.031 150.265 1.00 34.21  ? 115 SER C C     1 
ATOM   10059 O  O     . SER C 3 115 ? 193.376 197.532 149.436 1.00 36.05  ? 115 SER C O     1 
ATOM   10060 C  CB    . SER C 3 115 ? 193.714 198.812 151.999 1.00 34.77  ? 115 SER C CB    1 
ATOM   10061 O  OG    . SER C 3 115 ? 194.062 199.144 153.331 1.00 39.69  ? 115 SER C OG    1 
ATOM   10062 N  N     . VAL C 3 116 ? 194.484 195.750 150.242 1.00 27.91  ? 116 VAL C N     1 
ATOM   10063 C  CA    . VAL C 3 116 ? 193.989 194.847 149.196 1.00 32.46  ? 116 VAL C CA    1 
ATOM   10064 C  C     . VAL C 3 116 ? 192.515 194.550 149.444 1.00 23.13  ? 116 VAL C C     1 
ATOM   10065 O  O     . VAL C 3 116 ? 192.115 194.363 150.607 1.00 29.72  ? 116 VAL C O     1 
ATOM   10066 C  CB    . VAL C 3 116 ? 194.818 193.560 149.176 1.00 29.99  ? 116 VAL C CB    1 
ATOM   10067 C  CG1   . VAL C 3 116 ? 194.299 192.598 148.120 1.00 27.89  ? 116 VAL C CG1   1 
ATOM   10068 C  CG2   . VAL C 3 116 ? 196.286 193.881 148.936 1.00 26.72  ? 116 VAL C CG2   1 
ATOM   10069 N  N     . PRO C 3 117 ? 191.673 194.517 148.410 1.00 31.93  ? 117 PRO C N     1 
ATOM   10070 C  CA    . PRO C 3 117 ? 190.277 194.110 148.614 1.00 22.65  ? 117 PRO C CA    1 
ATOM   10071 C  C     . PRO C 3 117 ? 190.190 192.702 149.186 1.00 23.35  ? 117 PRO C C     1 
ATOM   10072 O  O     . PRO C 3 117 ? 190.986 191.822 148.852 1.00 27.16  ? 117 PRO C O     1 
ATOM   10073 C  CB    . PRO C 3 117 ? 189.667 194.190 147.207 1.00 25.46  ? 117 PRO C CB    1 
ATOM   10074 C  CG    . PRO C 3 117 ? 190.810 194.437 146.268 1.00 29.82  ? 117 PRO C CG    1 
ATOM   10075 C  CD    . PRO C 3 117 ? 191.906 195.053 147.061 1.00 25.99  ? 117 PRO C CD    1 
ATOM   10076 N  N     . VAL C 3 118 ? 189.203 192.500 150.062 1.00 17.07  ? 118 VAL C N     1 
ATOM   10077 C  CA    . VAL C 3 118 ? 189.118 191.261 150.830 1.00 21.36  ? 118 VAL C CA    1 
ATOM   10078 C  C     . VAL C 3 118 ? 188.824 190.071 149.921 1.00 20.53  ? 118 VAL C C     1 
ATOM   10079 O  O     . VAL C 3 118 ? 189.321 188.962 150.152 1.00 22.39  ? 118 VAL C O     1 
ATOM   10080 C  CB    . VAL C 3 118 ? 188.068 191.406 151.949 1.00 25.13  ? 118 VAL C CB    1 
ATOM   10081 C  CG1   . VAL C 3 118 ? 186.732 191.869 151.382 1.00 23.60  ? 118 VAL C CG1   1 
ATOM   10082 C  CG2   . VAL C 3 118 ? 187.911 190.102 152.720 1.00 28.22  ? 118 VAL C CG2   1 
ATOM   10083 N  N     . GLU C 3 119 ? 188.021 190.275 148.873 1.00 27.45  ? 119 GLU C N     1 
ATOM   10084 C  CA    . GLU C 3 119 ? 187.621 189.155 148.026 1.00 21.69  ? 119 GLU C CA    1 
ATOM   10085 C  C     . GLU C 3 119 ? 188.798 188.571 147.253 1.00 17.60  ? 119 GLU C C     1 
ATOM   10086 O  O     . GLU C 3 119 ? 188.790 187.378 146.929 1.00 23.10  ? 119 GLU C O     1 
ATOM   10087 C  CB    . GLU C 3 119 ? 186.519 189.590 147.062 1.00 19.61  ? 119 GLU C CB    1 
ATOM   10088 C  CG    . GLU C 3 119 ? 186.709 190.979 146.488 1.00 31.53  ? 119 GLU C CG    1 
ATOM   10089 C  CD    . GLU C 3 119 ? 185.431 191.542 145.903 1.00 34.28  ? 119 GLU C CD    1 
ATOM   10090 O  OE1   . GLU C 3 119 ? 184.776 190.834 145.110 1.00 40.00  ? 119 GLU C OE1   1 
ATOM   10091 O  OE2   . GLU C 3 119 ? 185.080 192.691 146.241 1.00 33.22  ? 119 GLU C OE2   1 
ATOM   10092 N  N     . LEU C 3 120 ? 189.815 189.381 146.953 1.00 19.20  ? 120 LEU C N     1 
ATOM   10093 C  CA    . LEU C 3 120 ? 190.957 188.891 146.190 1.00 19.56  ? 120 LEU C CA    1 
ATOM   10094 C  C     . LEU C 3 120 ? 191.915 188.049 147.024 1.00 17.67  ? 120 LEU C C     1 
ATOM   10095 O  O     . LEU C 3 120 ? 192.820 187.431 146.453 1.00 21.86  ? 120 LEU C O     1 
ATOM   10096 C  CB    . LEU C 3 120 ? 191.716 190.062 145.563 1.00 18.99  ? 120 LEU C CB    1 
ATOM   10097 C  CG    . LEU C 3 120 ? 190.970 190.860 144.491 1.00 23.91  ? 120 LEU C CG    1 
ATOM   10098 C  CD1   . LEU C 3 120 ? 191.869 191.936 143.901 1.00 20.83  ? 120 LEU C CD1   1 
ATOM   10099 C  CD2   . LEU C 3 120 ? 190.444 189.939 143.401 1.00 19.21  ? 120 LEU C CD2   1 
ATOM   10100 N  N     . VAL C 3 121 ? 191.749 188.010 148.345 1.00 20.18  ? 121 VAL C N     1 
ATOM   10101 C  CA    . VAL C 3 121 ? 192.591 187.197 149.215 1.00 20.42  ? 121 VAL C CA    1 
ATOM   10102 C  C     . VAL C 3 121 ? 191.829 186.050 149.852 1.00 18.60  ? 121 VAL C C     1 
ATOM   10103 O  O     . VAL C 3 121 ? 192.434 185.248 150.580 1.00 27.51  ? 121 VAL C O     1 
ATOM   10104 C  CB    . VAL C 3 121 ? 193.272 188.053 150.301 1.00 22.95  ? 121 VAL C CB    1 
ATOM   10105 C  CG1   . VAL C 3 121 ? 193.930 189.273 149.679 1.00 23.78  ? 121 VAL C CG1   1 
ATOM   10106 C  CG2   . VAL C 3 121 ? 192.270 188.463 151.369 1.00 20.55  ? 121 VAL C CG2   1 
ATOM   10107 N  N     . THR C 3 122 ? 190.527 185.939 149.606 1.00 20.22  ? 122 THR C N     1 
ATOM   10108 C  CA    . THR C 3 122 ? 189.699 184.889 150.183 1.00 23.26  ? 122 THR C CA    1 
ATOM   10109 C  C     . THR C 3 122 ? 189.175 183.984 149.076 1.00 19.67  ? 122 THR C C     1 
ATOM   10110 O  O     . THR C 3 122 ? 188.681 184.469 148.053 1.00 24.78  ? 122 THR C O     1 
ATOM   10111 C  CB    . THR C 3 122 ? 188.531 185.481 150.975 1.00 22.49  ? 122 THR C CB    1 
ATOM   10112 O  OG1   . THR C 3 122 ? 187.925 186.539 150.222 1.00 27.26  ? 122 THR C OG1   1 
ATOM   10113 C  CG2   . THR C 3 122 ? 189.015 186.028 152.309 1.00 18.86  ? 122 THR C CG2   1 
ATOM   10114 N  N     . ALA C 3 123 ? 189.287 182.675 149.283 1.00 16.80  ? 123 ALA C N     1 
ATOM   10115 C  CA    . ALA C 3 123 ? 188.771 181.716 148.319 1.00 13.08  ? 123 ALA C CA    1 
ATOM   10116 C  C     . ALA C 3 123 ? 187.247 181.674 148.364 1.00 14.96  ? 123 ALA C C     1 
ATOM   10117 O  O     . ALA C 3 123 ? 186.626 181.900 149.405 1.00 23.30  ? 123 ALA C O     1 
ATOM   10118 C  CB    . ALA C 3 123 ? 189.344 180.325 148.587 1.00 16.53  ? 123 ALA C CB    1 
ATOM   10119 N  N     . SER C 3 124 ? 186.647 181.382 147.214 1.00 13.55  ? 124 SER C N     1 
ATOM   10120 C  CA    . SER C 3 124 ? 185.199 181.322 147.106 1.00 15.19  ? 124 SER C CA    1 
ATOM   10121 C  C     . SER C 3 124 ? 184.671 179.997 147.654 1.00 7.29   ? 124 SER C C     1 
ATOM   10122 O  O     . SER C 3 124 ? 185.428 179.092 148.014 1.00 23.99  ? 124 SER C O     1 
ATOM   10123 C  CB    . SER C 3 124 ? 184.764 181.513 145.654 1.00 12.74  ? 124 SER C CB    1 
ATOM   10124 O  OG    . SER C 3 124 ? 185.070 180.371 144.875 1.00 24.72  ? 124 SER C OG    1 
ATOM   10125 N  N     . ALA C 3 125 ? 183.342 179.890 147.712 1.00 9.89   ? 125 ALA C N     1 
ATOM   10126 C  CA    . ALA C 3 125 ? 182.722 178.690 148.267 1.00 20.78  ? 125 ALA C CA    1 
ATOM   10127 C  C     . ALA C 3 125 ? 182.690 177.554 147.252 1.00 3.49   ? 125 ALA C C     1 
ATOM   10128 O  O     . ALA C 3 125 ? 182.481 176.393 147.621 1.00 18.59  ? 125 ALA C O     1 
ATOM   10129 C  CB    . ALA C 3 125 ? 181.308 179.006 148.752 1.00 15.69  ? 125 ALA C CB    1 
ATOM   10130 N  N     . SER C 3 126 ? 182.903 177.863 145.975 1.00 5.58   ? 126 SER C N     1 
ATOM   10131 C  CA    . SER C 3 126 ? 182.811 176.852 144.931 1.00 13.19  ? 126 SER C CA    1 
ATOM   10132 C  C     . SER C 3 126 ? 184.129 176.613 144.210 1.00 15.31  ? 126 SER C C     1 
ATOM   10133 O  O     . SER C 3 126 ? 184.290 175.562 143.579 1.00 20.70  ? 126 SER C O     1 
ATOM   10134 C  CB    . SER C 3 126 ? 181.746 177.247 143.903 1.00 12.61  ? 126 SER C CB    1 
ATOM   10135 O  OG    . SER C 3 126 ? 182.104 178.441 143.229 1.00 15.37  ? 126 SER C OG    1 
ATOM   10136 N  N     . GLY C 3 127 ? 185.067 177.553 144.285 1.00 12.15  ? 127 GLY C N     1 
ATOM   10137 C  CA    . GLY C 3 127 ? 186.310 177.442 143.556 1.00 8.77   ? 127 GLY C CA    1 
ATOM   10138 C  C     . GLY C 3 127 ? 186.204 177.740 142.078 1.00 12.08  ? 127 GLY C C     1 
ATOM   10139 O  O     . GLY C 3 127 ? 187.199 177.586 141.360 1.00 14.82  ? 127 GLY C O     1 
ATOM   10140 N  N     . LEU C 3 128 ? 185.032 178.158 141.600 1.00 12.16  ? 128 LEU C N     1 
ATOM   10141 C  CA    . LEU C 3 128 ? 184.816 178.493 140.198 1.00 21.47  ? 128 LEU C CA    1 
ATOM   10142 C  C     . LEU C 3 128 ? 184.170 179.866 140.066 1.00 10.90  ? 128 LEU C C     1 
ATOM   10143 O  O     . LEU C 3 128 ? 183.413 180.117 139.125 1.00 26.02  ? 128 LEU C O     1 
ATOM   10144 C  CB    . LEU C 3 128 ? 183.964 177.429 139.507 1.00 21.76  ? 128 LEU C CB    1 
ATOM   10145 C  CG    . LEU C 3 128 ? 184.391 175.975 139.724 1.00 19.20  ? 128 LEU C CG    1 
ATOM   10146 C  CD1   . LEU C 3 128 ? 183.241 175.020 139.439 1.00 19.07  ? 128 LEU C CD1   1 
ATOM   10147 C  CD2   . LEU C 3 128 ? 185.601 175.640 138.866 1.00 13.11  ? 128 LEU C CD2   1 
ATOM   10148 N  N     . ASP C 3 129 ? 184.465 180.764 141.003 1.00 26.33  ? 129 ASP C N     1 
ATOM   10149 C  CA    . ASP C 3 129 ? 183.868 182.093 141.002 1.00 20.02  ? 129 ASP C CA    1 
ATOM   10150 C  C     . ASP C 3 129 ? 184.411 182.908 139.836 1.00 14.47  ? 129 ASP C C     1 
ATOM   10151 O  O     . ASP C 3 129 ? 185.608 183.209 139.781 1.00 29.12  ? 129 ASP C O     1 
ATOM   10152 C  CB    . ASP C 3 129 ? 184.148 182.797 142.327 1.00 20.89  ? 129 ASP C CB    1 
ATOM   10153 C  CG    . ASP C 3 129 ? 183.157 183.905 142.622 1.00 20.94  ? 129 ASP C CG    1 
ATOM   10154 O  OD1   . ASP C 3 129 ? 182.442 184.334 141.693 1.00 27.94  ? 129 ASP C OD1   1 
ATOM   10155 O  OD2   . ASP C 3 129 ? 183.093 184.349 143.788 1.00 26.04  ? 129 ASP C OD2   1 
ATOM   10156 N  N     . ASN C 3 130 ? 183.530 183.262 138.907 1.00 18.87  ? 130 ASN C N     1 
ATOM   10157 C  CA    . ASN C 3 130 ? 183.878 184.074 137.751 1.00 16.30  ? 130 ASN C CA    1 
ATOM   10158 C  C     . ASN C 3 130 ? 183.656 185.561 137.998 1.00 16.88  ? 130 ASN C C     1 
ATOM   10159 O  O     . ASN C 3 130 ? 183.848 186.368 137.083 1.00 27.12  ? 130 ASN C O     1 
ATOM   10160 C  CB    . ASN C 3 130 ? 183.068 183.613 136.534 1.00 9.23   ? 130 ASN C CB    1 
ATOM   10161 C  CG    . ASN C 3 130 ? 183.609 184.158 135.228 1.00 23.92  ? 130 ASN C CG    1 
ATOM   10162 O  OD1   . ASN C 3 130 ? 184.818 184.188 135.008 1.00 26.95  ? 130 ASN C OD1   1 
ATOM   10163 N  ND2   . ASN C 3 130 ? 182.711 184.596 134.354 1.00 21.30  ? 130 ASN C ND2   1 
ATOM   10164 N  N     . ASN C 3 131 ? 183.270 185.941 139.211 1.00 19.57  ? 131 ASN C N     1 
ATOM   10165 C  CA    . ASN C 3 131 ? 182.816 187.291 139.499 1.00 25.61  ? 131 ASN C CA    1 
ATOM   10166 C  C     . ASN C 3 131 ? 183.649 187.929 140.601 1.00 26.71  ? 131 ASN C C     1 
ATOM   10167 O  O     . ASN C 3 131 ? 184.030 187.269 141.572 1.00 36.50  ? 131 ASN C O     1 
ATOM   10168 C  CB    . ASN C 3 131 ? 181.342 187.287 139.910 1.00 14.68  ? 131 ASN C CB    1 
ATOM   10169 C  CG    . ASN C 3 131 ? 180.445 186.682 138.853 1.00 18.59  ? 131 ASN C CG    1 
ATOM   10170 O  OD1   . ASN C 3 131 ? 180.399 187.153 137.717 1.00 25.49  ? 131 ASN C OD1   1 
ATOM   10171 N  ND2   . ASN C 3 131 ? 179.720 185.633 139.223 1.00 33.83  ? 131 ASN C ND2   1 
ATOM   10172 N  N     . ILE C 3 132 ? 183.932 189.221 140.430 1.00 22.98  ? 132 ILE C N     1 
ATOM   10173 C  CA    . ILE C 3 132 ? 184.448 190.079 141.486 1.00 20.32  ? 132 ILE C CA    1 
ATOM   10174 C  C     . ILE C 3 132 ? 183.662 191.382 141.440 1.00 20.25  ? 132 ILE C C     1 
ATOM   10175 O  O     . ILE C 3 132 ? 183.044 191.726 140.431 1.00 28.47  ? 132 ILE C O     1 
ATOM   10176 C  CB    . ILE C 3 132 ? 185.963 190.358 141.354 1.00 28.26  ? 132 ILE C CB    1 
ATOM   10177 C  CG1   . ILE C 3 132 ? 186.293 190.886 139.957 1.00 32.02  ? 132 ILE C CG1   1 
ATOM   10178 C  CG2   . ILE C 3 132 ? 186.773 189.109 141.675 1.00 24.16  ? 132 ILE C CG2   1 
ATOM   10179 C  CD1   . ILE C 3 132 ? 187.753 191.230 139.765 1.00 18.60  ? 132 ILE C CD1   1 
ATOM   10180 N  N     . THR C 3 133 ? 183.685 192.106 142.554 1.00 22.96  ? 133 THR C N     1 
ATOM   10181 C  CA    . THR C 3 133 ? 182.976 193.373 142.617 1.00 22.01  ? 133 THR C CA    1 
ATOM   10182 C  C     . THR C 3 133 ? 183.672 194.416 141.741 1.00 21.43  ? 133 THR C C     1 
ATOM   10183 O  O     . THR C 3 133 ? 184.877 194.322 141.491 1.00 25.18  ? 133 THR C O     1 
ATOM   10184 C  CB    . THR C 3 133 ? 182.892 193.875 144.056 1.00 23.32  ? 133 THR C CB    1 
ATOM   10185 O  OG1   . THR C 3 133 ? 184.211 194.008 144.599 1.00 31.20  ? 133 THR C OG1   1 
ATOM   10186 C  CG2   . THR C 3 133 ? 182.084 192.910 144.911 1.00 15.62  ? 133 THR C CG2   1 
ATOM   10187 N  N     . PRO C 3 134 ? 182.926 195.404 141.241 1.00 32.31  ? 134 PRO C N     1 
ATOM   10188 C  CA    . PRO C 3 134 ? 183.556 196.453 140.420 1.00 29.39  ? 134 PRO C CA    1 
ATOM   10189 C  C     . PRO C 3 134 ? 184.696 197.174 141.119 1.00 23.79  ? 134 PRO C C     1 
ATOM   10190 O  O     . PRO C 3 134 ? 185.692 197.511 140.467 1.00 30.06  ? 134 PRO C O     1 
ATOM   10191 C  CB    . PRO C 3 134 ? 182.396 197.410 140.116 1.00 24.84  ? 134 PRO C CB    1 
ATOM   10192 C  CG    . PRO C 3 134 ? 181.158 196.606 140.279 1.00 26.01  ? 134 PRO C CG    1 
ATOM   10193 C  CD    . PRO C 3 134 ? 181.456 195.412 141.138 1.00 22.24  ? 134 PRO C CD    1 
ATOM   10194 N  N     . GLN C 3 135 ? 184.578 197.429 142.425 1.00 21.96  ? 135 GLN C N     1 
ATOM   10195 C  CA    . GLN C 3 135 ? 185.671 198.067 143.152 1.00 24.59  ? 135 GLN C CA    1 
ATOM   10196 C  C     . GLN C 3 135 ? 186.897 197.164 143.214 1.00 29.81  ? 135 GLN C C     1 
ATOM   10197 O  O     . GLN C 3 135 ? 188.034 197.646 143.159 1.00 31.73  ? 135 GLN C O     1 
ATOM   10198 C  CB    . GLN C 3 135 ? 185.221 198.467 144.559 1.00 27.18  ? 135 GLN C CB    1 
ATOM   10199 C  CG    . GLN C 3 135 ? 184.192 197.548 145.198 1.00 33.24  ? 135 GLN C CG    1 
ATOM   10200 C  CD    . GLN C 3 135 ? 182.768 197.936 144.839 1.00 38.64  ? 135 GLN C CD    1 
ATOM   10201 O  OE1   . GLN C 3 135 ? 182.358 199.080 145.036 1.00 36.16  ? 135 GLN C OE1   1 
ATOM   10202 N  NE2   . GLN C 3 135 ? 182.007 196.985 144.313 1.00 35.74  ? 135 GLN C NE2   1 
ATOM   10203 N  N     . ALA C 3 136 ? 186.688 195.853 143.346 1.00 23.66  ? 136 ALA C N     1 
ATOM   10204 C  CA    . ALA C 3 136 ? 187.813 194.924 143.310 1.00 21.79  ? 136 ALA C CA    1 
ATOM   10205 C  C     . ALA C 3 136 ? 188.488 194.930 141.944 1.00 26.76  ? 136 ALA C C     1 
ATOM   10206 O  O     . ALA C 3 136 ? 189.720 194.876 141.854 1.00 28.30  ? 136 ALA C O     1 
ATOM   10207 C  CB    . ALA C 3 136 ? 187.347 193.515 143.674 1.00 22.33  ? 136 ALA C CB    1 
ATOM   10208 N  N     . ALA C 3 137 ? 187.696 194.990 140.870 1.00 23.04  ? 137 ALA C N     1 
ATOM   10209 C  CA    . ALA C 3 137 ? 188.266 195.050 139.528 1.00 18.73  ? 137 ALA C CA    1 
ATOM   10210 C  C     . ALA C 3 137 ? 188.996 196.366 139.291 1.00 23.69  ? 137 ALA C C     1 
ATOM   10211 O  O     . ALA C 3 137 ? 190.059 196.387 138.660 1.00 31.21  ? 137 ALA C O     1 
ATOM   10212 C  CB    . ALA C 3 137 ? 187.170 194.847 138.483 1.00 18.05  ? 137 ALA C CB    1 
ATOM   10213 N  N     . ALA C 3 138 ? 188.438 197.476 139.782 1.00 27.28  ? 138 ALA C N     1 
ATOM   10214 C  CA    . ALA C 3 138 ? 189.074 198.777 139.609 1.00 26.56  ? 138 ALA C CA    1 
ATOM   10215 C  C     . ALA C 3 138 ? 190.401 198.878 140.349 1.00 28.47  ? 138 ALA C C     1 
ATOM   10216 O  O     . ALA C 3 138 ? 191.254 199.682 139.959 1.00 31.59  ? 138 ALA C O     1 
ATOM   10217 C  CB    . ALA C 3 138 ? 188.134 199.890 140.075 1.00 20.92  ? 138 ALA C CB    1 
ATOM   10218 N  N     . TRP C 3 139 ? 190.592 198.086 141.407 1.00 28.49  ? 139 TRP C N     1 
ATOM   10219 C  CA    . TRP C 3 139 ? 191.859 198.096 142.129 1.00 23.06  ? 139 TRP C CA    1 
ATOM   10220 C  C     . TRP C 3 139 ? 193.003 197.579 141.266 1.00 23.42  ? 139 TRP C C     1 
ATOM   10221 O  O     . TRP C 3 139 ? 194.158 197.966 141.472 1.00 33.14  ? 139 TRP C O     1 
ATOM   10222 C  CB    . TRP C 3 139 ? 191.732 197.266 143.407 1.00 22.67  ? 139 TRP C CB    1 
ATOM   10223 C  CG    . TRP C 3 139 ? 192.966 197.248 144.256 1.00 25.97  ? 139 TRP C CG    1 
ATOM   10224 C  CD1   . TRP C 3 139 ? 193.343 198.185 145.173 1.00 20.87  ? 139 TRP C CD1   1 
ATOM   10225 C  CD2   . TRP C 3 139 ? 193.979 196.235 144.278 1.00 28.90  ? 139 TRP C CD2   1 
ATOM   10226 N  NE1   . TRP C 3 139 ? 194.530 197.822 145.761 1.00 28.94  ? 139 TRP C NE1   1 
ATOM   10227 C  CE2   . TRP C 3 139 ? 194.941 196.628 145.229 1.00 27.19  ? 139 TRP C CE2   1 
ATOM   10228 C  CE3   . TRP C 3 139 ? 194.167 195.036 143.585 1.00 20.99  ? 139 TRP C CE3   1 
ATOM   10229 C  CZ2   . TRP C 3 139 ? 196.074 195.866 145.503 1.00 25.11  ? 139 TRP C CZ2   1 
ATOM   10230 C  CZ3   . TRP C 3 139 ? 195.292 194.281 143.859 1.00 21.87  ? 139 TRP C CZ3   1 
ATOM   10231 C  CH2   . TRP C 3 139 ? 196.230 194.698 144.809 1.00 23.75  ? 139 TRP C CH2   1 
ATOM   10232 N  N     . GLN C 3 140 ? 192.703 196.716 140.298 1.00 22.40  ? 140 GLN C N     1 
ATOM   10233 C  CA    . GLN C 3 140 ? 193.704 196.154 139.401 1.00 23.54  ? 140 GLN C CA    1 
ATOM   10234 C  C     . GLN C 3 140 ? 193.895 196.975 138.133 1.00 27.00  ? 140 GLN C C     1 
ATOM   10235 O  O     . GLN C 3 140 ? 194.674 196.570 137.264 1.00 31.70  ? 140 GLN C O     1 
ATOM   10236 C  CB    . GLN C 3 140 ? 193.322 194.719 139.025 1.00 19.84  ? 140 GLN C CB    1 
ATOM   10237 C  CG    . GLN C 3 140 ? 192.549 193.979 140.102 1.00 23.05  ? 140 GLN C CG    1 
ATOM   10238 C  CD    . GLN C 3 140 ? 192.381 192.506 139.792 1.00 20.53  ? 140 GLN C CD    1 
ATOM   10239 O  OE1   . GLN C 3 140 ? 193.321 191.839 139.363 1.00 26.01  ? 140 GLN C OE1   1 
ATOM   10240 N  NE2   . GLN C 3 140 ? 191.177 191.991 140.008 1.00 25.30  ? 140 GLN C NE2   1 
ATOM   10241 N  N     . ILE C 3 141 ? 193.199 198.107 138.004 1.00 26.76  ? 141 ILE C N     1 
ATOM   10242 C  CA    . ILE C 3 141 ? 193.280 198.894 136.771 1.00 27.01  ? 141 ILE C CA    1 
ATOM   10243 C  C     . ILE C 3 141 ? 194.692 199.397 136.487 1.00 30.85  ? 141 ILE C C     1 
ATOM   10244 O  O     . ILE C 3 141 ? 195.156 199.248 135.345 1.00 34.13  ? 141 ILE C O     1 
ATOM   10245 C  CB    . ILE C 3 141 ? 192.241 200.030 136.803 1.00 28.40  ? 141 ILE C CB    1 
ATOM   10246 C  CG1   . ILE C 3 141 ? 190.882 199.521 136.318 1.00 28.99  ? 141 ILE C CG1   1 
ATOM   10247 C  CG2   . ILE C 3 141 ? 192.695 201.202 135.947 1.00 28.08  ? 141 ILE C CG2   1 
ATOM   10248 C  CD1   . ILE C 3 141 ? 189.783 200.557 136.388 1.00 26.74  ? 141 ILE C CD1   1 
ATOM   10249 N  N     . PRO C 3 142 ? 195.423 199.993 137.444 1.00 29.54  ? 142 PRO C N     1 
ATOM   10250 C  CA    . PRO C 3 142 ? 196.771 200.489 137.103 1.00 28.45  ? 142 PRO C CA    1 
ATOM   10251 C  C     . PRO C 3 142 ? 197.715 199.407 136.606 1.00 30.36  ? 142 PRO C C     1 
ATOM   10252 O  O     . PRO C 3 142 ? 198.569 199.684 135.754 1.00 30.07  ? 142 PRO C O     1 
ATOM   10253 C  CB    . PRO C 3 142 ? 197.262 201.115 138.417 1.00 27.02  ? 142 PRO C CB    1 
ATOM   10254 C  CG    . PRO C 3 142 ? 196.387 200.554 139.477 1.00 33.41  ? 142 PRO C CG    1 
ATOM   10255 C  CD    . PRO C 3 142 ? 195.063 200.334 138.832 1.00 28.81  ? 142 PRO C CD    1 
ATOM   10256 N  N     . ARG C 3 143 ? 197.592 198.179 137.114 1.00 26.55  ? 143 ARG C N     1 
ATOM   10257 C  CA    . ARG C 3 143 ? 198.437 197.096 136.620 1.00 22.17  ? 143 ARG C CA    1 
ATOM   10258 C  C     . ARG C 3 143 ? 198.044 196.692 135.204 1.00 27.76  ? 143 ARG C C     1 
ATOM   10259 O  O     . ARG C 3 143 ? 198.911 196.486 134.347 1.00 31.53  ? 143 ARG C O     1 
ATOM   10260 C  CB    . ARG C 3 143 ? 198.359 195.895 137.562 1.00 24.94  ? 143 ARG C CB    1 
ATOM   10261 C  CG    . ARG C 3 143 ? 198.836 194.592 136.941 1.00 27.07  ? 143 ARG C CG    1 
ATOM   10262 C  CD    . ARG C 3 143 ? 198.694 193.429 137.906 1.00 26.66  ? 143 ARG C CD    1 
ATOM   10263 N  NE    . ARG C 3 143 ? 197.300 193.055 138.112 1.00 26.90  ? 143 ARG C NE    1 
ATOM   10264 C  CZ    . ARG C 3 143 ? 196.610 192.262 137.303 1.00 25.81  ? 143 ARG C CZ    1 
ATOM   10265 N  NH1   . ARG C 3 143 ? 197.155 191.742 136.215 1.00 26.87  ? 143 ARG C NH1   1 
ATOM   10266 N  NH2   . ARG C 3 143 ? 195.343 191.983 137.593 1.00 26.28  ? 143 ARG C NH2   1 
ATOM   10267 N  N     . VAL C 3 144 ? 196.741 196.578 134.939 1.00 33.27  ? 144 VAL C N     1 
ATOM   10268 C  CA    . VAL C 3 144 ? 196.279 196.187 133.611 1.00 34.17  ? 144 VAL C CA    1 
ATOM   10269 C  C     . VAL C 3 144 ? 196.526 197.306 132.605 1.00 33.79  ? 144 VAL C C     1 
ATOM   10270 O  O     . VAL C 3 144 ? 196.901 197.051 131.454 1.00 34.58  ? 144 VAL C O     1 
ATOM   10271 C  CB    . VAL C 3 144 ? 194.794 195.783 133.663 1.00 34.54  ? 144 VAL C CB    1 
ATOM   10272 C  CG1   . VAL C 3 144 ? 194.282 195.445 132.272 1.00 29.27  ? 144 VAL C CG1   1 
ATOM   10273 C  CG2   . VAL C 3 144 ? 194.598 194.608 134.607 1.00 29.46  ? 144 VAL C CG2   1 
ATOM   10274 N  N     . ALA C 3 145 ? 196.321 198.559 133.021 1.00 35.67  ? 145 ALA C N     1 
ATOM   10275 C  CA    . ALA C 3 145 ? 196.490 199.684 132.105 1.00 34.02  ? 145 ALA C CA    1 
ATOM   10276 C  C     . ALA C 3 145 ? 197.925 199.786 131.605 1.00 38.78  ? 145 ALA C C     1 
ATOM   10277 O  O     . ALA C 3 145 ? 198.160 200.030 130.416 1.00 46.36  ? 145 ALA C O     1 
ATOM   10278 C  CB    . ALA C 3 145 ? 196.070 200.984 132.789 1.00 34.52  ? 145 ALA C CB    1 
ATOM   10279 N  N     . LYS C 3 146 ? 198.900 199.604 132.497 1.00 41.17  ? 146 LYS C N     1 
ATOM   10280 C  CA    . LYS C 3 146 ? 200.298 199.688 132.088 1.00 41.20  ? 146 LYS C CA    1 
ATOM   10281 C  C     . LYS C 3 146 ? 200.697 198.492 131.233 1.00 43.24  ? 146 LYS C C     1 
ATOM   10282 O  O     . LYS C 3 146 ? 201.418 198.645 130.239 1.00 44.10  ? 146 LYS C O     1 
ATOM   10283 C  CB    . LYS C 3 146 ? 201.194 199.799 133.322 1.00 41.16  ? 146 LYS C CB    1 
ATOM   10284 C  CG    . LYS C 3 146 ? 202.593 199.230 133.141 1.00 43.94  ? 146 LYS C CG    1 
ATOM   10285 C  CD    . LYS C 3 146 ? 203.438 199.417 134.393 1.00 44.69  ? 146 LYS C CD    1 
ATOM   10286 C  CE    . LYS C 3 146 ? 203.235 200.795 135.005 1.00 46.09  ? 146 LYS C CE    1 
ATOM   10287 N  NZ    . LYS C 3 146 ? 204.027 200.970 136.254 1.00 48.38  ? 146 LYS C NZ    1 
ATOM   10288 N  N     . ALA C 3 147 ? 200.236 197.294 131.600 1.00 41.83  ? 147 ALA C N     1 
ATOM   10289 C  CA    . ALA C 3 147 ? 200.600 196.095 130.852 1.00 39.55  ? 147 ALA C CA    1 
ATOM   10290 C  C     . ALA C 3 147 ? 200.022 196.115 129.442 1.00 38.22  ? 147 ALA C C     1 
ATOM   10291 O  O     . ALA C 3 147 ? 200.698 195.725 128.483 1.00 44.69  ? 147 ALA C O     1 
ATOM   10292 C  CB    . ALA C 3 147 ? 200.137 194.848 131.604 1.00 37.59  ? 147 ALA C CB    1 
ATOM   10293 N  N     . ARG C 3 148 ? 198.777 196.561 129.295 1.00 40.69  ? 148 ARG C N     1 
ATOM   10294 C  CA    . ARG C 3 148 ? 198.095 196.563 128.008 1.00 38.73  ? 148 ARG C CA    1 
ATOM   10295 C  C     . ARG C 3 148 ? 198.201 197.891 127.272 1.00 44.89  ? 148 ARG C C     1 
ATOM   10296 O  O     . ARG C 3 148 ? 197.619 198.029 126.192 1.00 49.60  ? 148 ARG C O     1 
ATOM   10297 C  CB    . ARG C 3 148 ? 196.620 196.195 128.194 1.00 41.37  ? 148 ARG C CB    1 
ATOM   10298 C  CG    . ARG C 3 148 ? 196.394 194.756 128.618 1.00 40.78  ? 148 ARG C CG    1 
ATOM   10299 C  CD    . ARG C 3 148 ? 195.456 194.043 127.662 1.00 40.34  ? 148 ARG C CD    1 
ATOM   10300 N  NE    . ARG C 3 148 ? 195.297 192.635 128.005 1.00 39.90  ? 148 ARG C NE    1 
ATOM   10301 C  CZ    . ARG C 3 148 ? 195.434 191.635 127.147 1.00 41.74  ? 148 ARG C CZ    1 
ATOM   10302 N  NH1   . ARG C 3 148 ? 195.727 191.851 125.875 1.00 46.72  ? 148 ARG C NH1   1 
ATOM   10303 N  NH2   . ARG C 3 148 ? 195.272 190.386 127.574 1.00 40.71  ? 148 ARG C NH2   1 
ATOM   10304 N  N     . ASN C 3 149 ? 198.926 198.864 127.827 1.00 44.67  ? 149 ASN C N     1 
ATOM   10305 C  CA    . ASN C 3 149 ? 199.080 200.187 127.223 1.00 45.77  ? 149 ASN C CA    1 
ATOM   10306 C  C     . ASN C 3 149 ? 197.715 200.827 126.969 1.00 47.16  ? 149 ASN C C     1 
ATOM   10307 O  O     . ASN C 3 149 ? 197.393 201.262 125.861 1.00 51.69  ? 149 ASN C O     1 
ATOM   10308 C  CB    . ASN C 3 149 ? 199.909 200.110 125.937 1.00 46.42  ? 149 ASN C CB    1 
ATOM   10309 C  CG    . ASN C 3 149 ? 200.362 201.475 125.445 1.00 50.19  ? 149 ASN C CG    1 
ATOM   10310 O  OD1   . ASN C 3 149 ? 199.958 202.510 125.976 1.00 52.33  ? 149 ASN C OD1   1 
ATOM   10311 N  ND2   . ASN C 3 149 ? 201.208 201.481 124.422 1.00 49.95  ? 149 ASN C ND2   1 
ATOM   10312 N  N     . LEU C 3 150 ? 196.900 200.868 128.019 1.00 44.39  ? 150 LEU C N     1 
ATOM   10313 C  CA    . LEU C 3 150 ? 195.573 201.460 127.966 1.00 44.74  ? 150 LEU C CA    1 
ATOM   10314 C  C     . LEU C 3 150 ? 195.452 202.514 129.057 1.00 48.68  ? 150 LEU C C     1 
ATOM   10315 O  O     . LEU C 3 150 ? 196.247 202.556 129.999 1.00 52.65  ? 150 LEU C O     1 
ATOM   10316 C  CB    . LEU C 3 150 ? 194.473 200.401 128.131 1.00 46.76  ? 150 LEU C CB    1 
ATOM   10317 C  CG    . LEU C 3 150 ? 194.346 199.361 127.016 1.00 46.99  ? 150 LEU C CG    1 
ATOM   10318 C  CD1   . LEU C 3 150 ? 193.496 198.185 127.473 1.00 45.45  ? 150 LEU C CD1   1 
ATOM   10319 C  CD2   . LEU C 3 150 ? 193.767 199.988 125.759 1.00 47.23  ? 150 LEU C CD2   1 
ATOM   10320 N  N     . SER C 3 151 ? 194.452 203.374 128.915 1.00 45.08  ? 151 SER C N     1 
ATOM   10321 C  CA    . SER C 3 151 ? 194.191 204.422 129.890 1.00 48.39  ? 151 SER C CA    1 
ATOM   10322 C  C     . SER C 3 151 ? 193.130 203.971 130.888 1.00 49.39  ? 151 SER C C     1 
ATOM   10323 O  O     . SER C 3 151 ? 192.461 202.950 130.712 1.00 52.60  ? 151 SER C O     1 
ATOM   10324 C  CB    . SER C 3 151 ? 193.760 205.716 129.191 1.00 50.87  ? 151 SER C CB    1 
ATOM   10325 O  OG    . SER C 3 151 ? 192.631 205.501 128.365 1.00 51.65  ? 151 SER C OG    1 
ATOM   10326 N  N     . VAL C 3 152 ? 192.988 204.756 131.957 1.00 50.35  ? 152 VAL C N     1 
ATOM   10327 C  CA    . VAL C 3 152 ? 192.019 204.431 132.999 1.00 47.86  ? 152 VAL C CA    1 
ATOM   10328 C  C     . VAL C 3 152 ? 190.596 204.555 132.469 1.00 48.62  ? 152 VAL C C     1 
ATOM   10329 O  O     . VAL C 3 152 ? 189.703 203.801 132.873 1.00 51.52  ? 152 VAL C O     1 
ATOM   10330 C  CB    . VAL C 3 152 ? 192.243 205.326 134.232 1.00 47.81  ? 152 VAL C CB    1 
ATOM   10331 C  CG1   . VAL C 3 152 ? 191.594 204.709 135.460 1.00 47.17  ? 152 VAL C CG1   1 
ATOM   10332 C  CG2   . VAL C 3 152 ? 193.729 205.544 134.464 1.00 47.46  ? 152 VAL C CG2   1 
ATOM   10333 N  N     . GLU C 3 153 ? 190.360 205.509 131.565 1.00 50.88  ? 153 GLU C N     1 
ATOM   10334 C  CA    . GLU C 3 153 ? 189.005 205.759 131.082 1.00 50.45  ? 153 GLU C CA    1 
ATOM   10335 C  C     . GLU C 3 153 ? 188.445 204.557 130.329 1.00 50.89  ? 153 GLU C C     1 
ATOM   10336 O  O     . GLU C 3 153 ? 187.278 204.191 130.513 1.00 51.99  ? 153 GLU C O     1 
ATOM   10337 C  CB    . GLU C 3 153 ? 188.989 207.002 130.193 1.00 51.81  ? 153 GLU C CB    1 
ATOM   10338 C  CG    . GLU C 3 153 ? 189.443 208.273 130.893 1.00 54.35  ? 153 GLU C CG    1 
ATOM   10339 C  CD    . GLU C 3 153 ? 190.939 208.496 130.786 1.00 55.97  ? 153 GLU C CD    1 
ATOM   10340 O  OE1   . GLU C 3 153 ? 191.449 208.591 129.650 1.00 56.95  ? 153 GLU C OE1   1 
ATOM   10341 O  OE2   . GLU C 3 153 ? 191.606 208.577 131.839 1.00 52.39  ? 153 GLU C OE2   1 
ATOM   10342 N  N     . GLN C 3 154 ? 189.259 203.929 129.476 1.00 46.04  ? 154 GLN C N     1 
ATOM   10343 C  CA    . GLN C 3 154 ? 188.769 202.796 128.697 1.00 45.99  ? 154 GLN C CA    1 
ATOM   10344 C  C     . GLN C 3 154 ? 188.539 201.570 129.574 1.00 45.97  ? 154 GLN C C     1 
ATOM   10345 O  O     . GLN C 3 154 ? 187.595 200.806 129.344 1.00 47.99  ? 154 GLN C O     1 
ATOM   10346 C  CB    . GLN C 3 154 ? 189.743 202.469 127.565 1.00 43.12  ? 154 GLN C CB    1 
ATOM   10347 C  CG    . GLN C 3 154 ? 190.462 203.675 126.992 1.00 45.80  ? 154 GLN C CG    1 
ATOM   10348 C  CD    . GLN C 3 154 ? 191.578 203.290 126.042 1.00 49.60  ? 154 GLN C CD    1 
ATOM   10349 O  OE1   . GLN C 3 154 ? 192.742 203.623 126.265 1.00 54.73  ? 154 GLN C OE1   1 
ATOM   10350 N  NE2   . GLN C 3 154 ? 191.228 202.584 124.974 1.00 48.71  ? 154 GLN C NE2   1 
ATOM   10351 N  N     . LEU C 3 155 ? 189.394 201.361 130.578 1.00 39.73  ? 155 LEU C N     1 
ATOM   10352 C  CA    . LEU C 3 155 ? 189.238 200.195 131.442 1.00 39.46  ? 155 LEU C CA    1 
ATOM   10353 C  C     . LEU C 3 155 ? 187.994 200.310 132.315 1.00 41.34  ? 155 LEU C C     1 
ATOM   10354 O  O     . LEU C 3 155 ? 187.329 199.304 132.589 1.00 46.99  ? 155 LEU C O     1 
ATOM   10355 C  CB    . LEU C 3 155 ? 190.485 200.005 132.304 1.00 38.75  ? 155 LEU C CB    1 
ATOM   10356 C  CG    . LEU C 3 155 ? 191.704 199.421 131.590 1.00 38.70  ? 155 LEU C CG    1 
ATOM   10357 C  CD1   . LEU C 3 155 ? 192.859 199.256 132.560 1.00 42.36  ? 155 LEU C CD1   1 
ATOM   10358 C  CD2   . LEU C 3 155 ? 191.359 198.096 130.931 1.00 36.68  ? 155 LEU C CD2   1 
ATOM   10359 N  N     . THR C 3 156 ? 187.668 201.523 132.768 1.00 35.52  ? 156 THR C N     1 
ATOM   10360 C  CA    . THR C 3 156 ? 186.458 201.707 133.563 1.00 38.09  ? 156 THR C CA    1 
ATOM   10361 C  C     . THR C 3 156 ? 185.209 201.455 132.728 1.00 41.27  ? 156 THR C C     1 
ATOM   10362 O  O     . THR C 3 156 ? 184.226 200.890 133.222 1.00 41.07  ? 156 THR C O     1 
ATOM   10363 C  CB    . THR C 3 156 ? 186.425 203.114 134.163 1.00 40.56  ? 156 THR C CB    1 
ATOM   10364 O  OG1   . THR C 3 156 ? 186.597 204.085 133.124 1.00 50.80  ? 156 THR C OG1   1 
ATOM   10365 C  CG2   . THR C 3 156 ? 187.526 203.280 135.198 1.00 40.47  ? 156 THR C CG2   1 
ATOM   10366 N  N     . GLN C 3 157 ? 185.229 201.866 131.458 1.00 39.42  ? 157 GLN C N     1 
ATOM   10367 C  CA    . GLN C 3 157 ? 184.086 201.620 130.585 1.00 38.68  ? 157 GLN C CA    1 
ATOM   10368 C  C     . GLN C 3 157 ? 183.968 200.142 130.235 1.00 40.75  ? 157 GLN C C     1 
ATOM   10369 O  O     . GLN C 3 157 ? 182.856 199.612 130.125 1.00 41.84  ? 157 GLN C O     1 
ATOM   10370 C  CB    . GLN C 3 157 ? 184.202 202.466 129.318 1.00 41.17  ? 157 GLN C CB    1 
ATOM   10371 C  CG    . GLN C 3 157 ? 184.147 203.964 129.566 1.00 43.51  ? 157 GLN C CG    1 
ATOM   10372 C  CD    . GLN C 3 157 ? 184.149 204.769 128.281 1.00 47.30  ? 157 GLN C CD    1 
ATOM   10373 O  OE1   . GLN C 3 157 ? 184.140 204.209 127.185 1.00 48.33  ? 157 GLN C OE1   1 
ATOM   10374 N  NE2   . GLN C 3 157 ? 184.158 206.090 128.410 1.00 45.84  ? 157 GLN C NE2   1 
ATOM   10375 N  N     . LEU C 3 158 ? 185.102 199.460 130.056 1.00 34.88  ? 158 LEU C N     1 
ATOM   10376 C  CA    . LEU C 3 158 ? 185.063 198.033 129.755 1.00 35.14  ? 158 LEU C CA    1 
ATOM   10377 C  C     . LEU C 3 158 ? 184.605 197.225 130.962 1.00 33.24  ? 158 LEU C C     1 
ATOM   10378 O  O     . LEU C 3 158 ? 183.885 196.231 130.814 1.00 39.23  ? 158 LEU C O     1 
ATOM   10379 C  CB    . LEU C 3 158 ? 186.436 197.560 129.279 1.00 34.12  ? 158 LEU C CB    1 
ATOM   10380 C  CG    . LEU C 3 158 ? 186.438 196.349 128.345 1.00 38.78  ? 158 LEU C CG    1 
ATOM   10381 C  CD1   . LEU C 3 158 ? 185.709 196.667 127.050 1.00 39.58  ? 158 LEU C CD1   1 
ATOM   10382 C  CD2   . LEU C 3 158 ? 187.858 195.893 128.066 1.00 40.90  ? 158 LEU C CD2   1 
ATOM   10383 N  N     . ILE C 3 159 ? 185.018 197.631 132.165 1.00 31.05  ? 159 ILE C N     1 
ATOM   10384 C  CA    . ILE C 3 159 ? 184.555 196.958 133.375 1.00 29.46  ? 159 ILE C CA    1 
ATOM   10385 C  C     . ILE C 3 159 ? 183.057 197.167 133.556 1.00 34.65  ? 159 ILE C C     1 
ATOM   10386 O  O     . ILE C 3 159 ? 182.318 196.231 133.886 1.00 36.61  ? 159 ILE C O     1 
ATOM   10387 C  CB    . ILE C 3 159 ? 185.352 197.449 134.599 1.00 28.50  ? 159 ILE C CB    1 
ATOM   10388 C  CG1   . ILE C 3 159 ? 186.720 196.767 134.654 1.00 35.04  ? 159 ILE C CG1   1 
ATOM   10389 C  CG2   . ILE C 3 159 ? 184.582 197.193 135.885 1.00 32.06  ? 159 ILE C CG2   1 
ATOM   10390 C  CD1   . ILE C 3 159 ? 187.709 197.457 135.567 1.00 26.39  ? 159 ILE C CD1   1 
ATOM   10391 N  N     . ALA C 3 160 ? 182.585 198.396 133.332 1.00 37.50  ? 160 ALA C N     1 
ATOM   10392 C  CA    . ALA C 3 160 ? 181.160 198.682 133.463 1.00 34.39  ? 160 ALA C CA    1 
ATOM   10393 C  C     . ALA C 3 160 ? 180.338 197.956 132.407 1.00 36.57  ? 160 ALA C C     1 
ATOM   10394 O  O     . ALA C 3 160 ? 179.192 197.574 132.672 1.00 42.16  ? 160 ALA C O     1 
ATOM   10395 C  CB    . ALA C 3 160 ? 180.917 200.189 133.380 1.00 33.49  ? 160 ALA C CB    1 
ATOM   10396 N  N     . LYS C 3 161 ? 180.898 197.761 131.211 1.00 31.12  ? 161 LYS C N     1 
ATOM   10397 C  CA    . LYS C 3 161 ? 180.170 197.060 130.158 1.00 27.35  ? 161 LYS C CA    1 
ATOM   10398 C  C     . LYS C 3 161 ? 179.910 195.608 130.541 1.00 32.25  ? 161 LYS C C     1 
ATOM   10399 O  O     . LYS C 3 161 ? 178.860 195.046 130.204 1.00 41.74  ? 161 LYS C O     1 
ATOM   10400 C  CB    . LYS C 3 161 ? 180.946 197.146 128.843 1.00 31.59  ? 161 LYS C CB    1 
ATOM   10401 C  CG    . LYS C 3 161 ? 180.417 196.248 127.736 1.00 36.20  ? 161 LYS C CG    1 
ATOM   10402 C  CD    . LYS C 3 161 ? 181.376 196.198 126.559 1.00 35.59  ? 161 LYS C CD    1 
ATOM   10403 C  CE    . LYS C 3 161 ? 180.679 195.712 125.299 1.00 36.28  ? 161 LYS C CE    1 
ATOM   10404 N  NZ    . LYS C 3 161 ? 181.398 194.569 124.670 1.00 42.99  ? 161 LYS C NZ    1 
ATOM   10405 N  N     . TYR C 3 162 ? 180.850 194.985 131.253 1.00 32.04  ? 162 TYR C N     1 
ATOM   10406 C  CA    . TYR C 3 162 ? 180.716 193.605 131.701 1.00 30.10  ? 162 TYR C CA    1 
ATOM   10407 C  C     . TYR C 3 162 ? 180.396 193.509 133.189 1.00 25.24  ? 162 TYR C C     1 
ATOM   10408 O  O     . TYR C 3 162 ? 180.804 192.551 133.855 1.00 28.49  ? 162 TYR C O     1 
ATOM   10409 C  CB    . TYR C 3 162 ? 181.983 192.820 131.367 1.00 30.57  ? 162 TYR C CB    1 
ATOM   10410 C  CG    . TYR C 3 162 ? 182.221 192.698 129.881 1.00 32.93  ? 162 TYR C CG    1 
ATOM   10411 C  CD1   . TYR C 3 162 ? 181.536 191.756 129.125 1.00 30.08  ? 162 TYR C CD1   1 
ATOM   10412 C  CD2   . TYR C 3 162 ? 183.113 193.538 129.229 1.00 29.31  ? 162 TYR C CD2   1 
ATOM   10413 C  CE1   . TYR C 3 162 ? 181.742 191.646 127.765 1.00 32.70  ? 162 TYR C CE1   1 
ATOM   10414 C  CE2   . TYR C 3 162 ? 183.324 193.436 127.869 1.00 31.08  ? 162 TYR C CE2   1 
ATOM   10415 C  CZ    . TYR C 3 162 ? 182.636 192.488 127.142 1.00 31.38  ? 162 TYR C CZ    1 
ATOM   10416 O  OH    . TYR C 3 162 ? 182.842 192.380 125.787 1.00 39.58  ? 162 TYR C OH    1 
ATOM   10417 N  N     . SER C 3 163 ? 179.670 194.487 133.723 1.00 35.29  ? 163 SER C N     1 
ATOM   10418 C  CA    . SER C 3 163 ? 179.231 194.489 135.111 1.00 30.94  ? 163 SER C CA    1 
ATOM   10419 C  C     . SER C 3 163 ? 177.718 194.339 135.157 1.00 32.12  ? 163 SER C C     1 
ATOM   10420 O  O     . SER C 3 163 ? 176.998 195.036 134.434 1.00 45.16  ? 163 SER C O     1 
ATOM   10421 C  CB    . SER C 3 163 ? 179.658 195.774 135.824 1.00 33.05  ? 163 SER C CB    1 
ATOM   10422 O  OG    . SER C 3 163 ? 181.061 195.956 135.757 1.00 40.01  ? 163 SER C OG    1 
ATOM   10423 N  N     . GLN C 3 164 ? 177.241 193.429 136.000 1.00 33.01  ? 164 GLN C N     1 
ATOM   10424 C  CA    . GLN C 3 164 ? 175.820 193.156 136.143 1.00 38.58  ? 164 GLN C CA    1 
ATOM   10425 C  C     . GLN C 3 164 ? 175.380 193.421 137.576 1.00 34.46  ? 164 GLN C C     1 
ATOM   10426 O  O     . GLN C 3 164 ? 176.120 193.164 138.530 1.00 37.23  ? 164 GLN C O     1 
ATOM   10427 C  CB    . GLN C 3 164 ? 175.489 191.709 135.756 1.00 34.61  ? 164 GLN C CB    1 
ATOM   10428 C  CG    . GLN C 3 164 ? 175.287 191.500 134.264 1.00 41.73  ? 164 GLN C CG    1 
ATOM   10429 C  CD    . GLN C 3 164 ? 174.756 190.118 133.934 1.00 47.06  ? 164 GLN C CD    1 
ATOM   10430 O  OE1   . GLN C 3 164 ? 174.841 189.197 134.746 1.00 45.20  ? 164 GLN C OE1   1 
ATOM   10431 N  NE2   . GLN C 3 164 ? 174.205 189.967 132.735 1.00 43.12  ? 164 GLN C NE2   1 
ATOM   10432 N  N     . GLN C 3 165 ? 174.166 193.941 137.717 1.00 39.82  ? 165 GLN C N     1 
ATOM   10433 C  CA    . GLN C 3 165 ? 173.578 194.241 139.011 1.00 39.23  ? 165 GLN C CA    1 
ATOM   10434 C  C     . GLN C 3 165 ? 172.226 193.556 139.133 1.00 39.12  ? 165 GLN C C     1 
ATOM   10435 O  O     . GLN C 3 165 ? 171.529 193.367 138.131 1.00 45.41  ? 165 GLN C O     1 
ATOM   10436 C  CB    . GLN C 3 165 ? 173.412 195.755 139.205 1.00 36.93  ? 165 GLN C CB    1 
ATOM   10437 C  CG    . GLN C 3 165 ? 174.725 196.515 139.285 1.00 40.91  ? 165 GLN C CG    1 
ATOM   10438 C  CD    . GLN C 3 165 ? 175.106 197.164 137.969 1.00 46.37  ? 165 GLN C CD    1 
ATOM   10439 O  OE1   . GLN C 3 165 ? 174.252 197.683 137.250 1.00 51.35  ? 165 GLN C OE1   1 
ATOM   10440 N  NE2   . GLN C 3 165 ? 176.393 197.136 137.646 1.00 42.94  ? 165 GLN C NE2   1 
ATOM   10441 N  N     . PRO C 3 166 ? 171.827 193.174 140.350 1.00 38.43  ? 166 PRO C N     1 
ATOM   10442 C  CA    . PRO C 3 166 ? 170.545 192.476 140.518 1.00 36.05  ? 166 PRO C CA    1 
ATOM   10443 C  C     . PRO C 3 166 ? 169.350 193.409 140.392 1.00 36.75  ? 166 PRO C C     1 
ATOM   10444 O  O     . PRO C 3 166 ? 169.514 194.622 140.229 1.00 39.26  ? 166 PRO C O     1 
ATOM   10445 C  CB    . PRO C 3 166 ? 170.647 191.881 141.932 1.00 33.07  ? 166 PRO C CB    1 
ATOM   10446 C  CG    . PRO C 3 166 ? 172.073 192.118 142.380 1.00 34.73  ? 166 PRO C CG    1 
ATOM   10447 C  CD    . PRO C 3 166 ? 172.544 193.311 141.626 1.00 35.62  ? 166 PRO C CD    1 
ATOM   10448 N  N     . LEU C 3 167 ? 168.141 192.844 140.459 1.00 40.95  ? 167 LEU C N     1 
ATOM   10449 C  CA    . LEU C 3 167 ? 166.934 193.659 140.362 1.00 41.19  ? 167 LEU C CA    1 
ATOM   10450 C  C     . LEU C 3 167 ? 166.846 194.651 141.515 1.00 39.14  ? 167 LEU C C     1 
ATOM   10451 O  O     . LEU C 3 167 ? 166.499 195.821 141.313 1.00 40.64  ? 167 LEU C O     1 
ATOM   10452 C  CB    . LEU C 3 167 ? 165.697 192.762 140.329 1.00 43.46  ? 167 LEU C CB    1 
ATOM   10453 C  CG    . LEU C 3 167 ? 164.918 192.721 139.013 1.00 44.27  ? 167 LEU C CG    1 
ATOM   10454 C  CD1   . LEU C 3 167 ? 165.825 192.312 137.862 1.00 42.27  ? 167 LEU C CD1   1 
ATOM   10455 C  CD2   . LEU C 3 167 ? 163.729 191.780 139.125 1.00 42.61  ? 167 LEU C CD2   1 
ATOM   10456 N  N     . VAL C 3 168 ? 167.156 194.203 142.729 1.00 37.89  ? 168 VAL C N     1 
ATOM   10457 C  CA    . VAL C 3 168 ? 167.229 195.075 143.891 1.00 32.07  ? 168 VAL C CA    1 
ATOM   10458 C  C     . VAL C 3 168 ? 168.613 194.922 144.509 1.00 36.67  ? 168 VAL C C     1 
ATOM   10459 O  O     . VAL C 3 168 ? 169.339 193.961 144.243 1.00 45.14  ? 168 VAL C O     1 
ATOM   10460 C  CB    . VAL C 3 168 ? 166.124 194.783 144.928 1.00 37.25  ? 168 VAL C CB    1 
ATOM   10461 C  CG1   . VAL C 3 168 ? 164.758 194.753 144.257 1.00 33.70  ? 168 VAL C CG1   1 
ATOM   10462 C  CG2   . VAL C 3 168 ? 166.397 193.481 145.645 1.00 35.85  ? 168 VAL C CG2   1 
ATOM   10463 N  N     . LYS C 3 169 ? 168.974 195.893 145.349 1.00 39.44  ? 169 LYS C N     1 
ATOM   10464 C  CA    . LYS C 3 169 ? 170.360 196.006 145.790 1.00 35.35  ? 169 LYS C CA    1 
ATOM   10465 C  C     . LYS C 3 169 ? 170.688 195.064 146.942 1.00 34.99  ? 169 LYS C C     1 
ATOM   10466 O  O     . LYS C 3 169 ? 171.868 194.855 147.243 1.00 41.56  ? 169 LYS C O     1 
ATOM   10467 C  CB    . LYS C 3 169 ? 170.658 197.450 146.192 1.00 39.21  ? 169 LYS C CB    1 
ATOM   10468 C  CG    . LYS C 3 169 ? 172.047 197.931 145.811 1.00 40.73  ? 169 LYS C CG    1 
ATOM   10469 C  CD    . LYS C 3 169 ? 172.066 199.437 145.603 1.00 42.55  ? 169 LYS C CD    1 
ATOM   10470 C  CE    . LYS C 3 169 ? 171.943 200.179 146.924 1.00 41.21  ? 169 LYS C CE    1 
ATOM   10471 N  NZ    . LYS C 3 169 ? 173.085 199.889 147.833 1.00 44.24  ? 169 LYS C NZ    1 
ATOM   10472 N  N     . TYR C 3 170 ? 169.683 194.484 147.595 1.00 26.67  ? 170 TYR C N     1 
ATOM   10473 C  CA    . TYR C 3 170 ? 169.938 193.716 148.808 1.00 26.60  ? 170 TYR C CA    1 
ATOM   10474 C  C     . TYR C 3 170 ? 169.866 192.206 148.606 1.00 27.43  ? 170 TYR C C     1 
ATOM   10475 O  O     . TYR C 3 170 ? 170.183 191.462 149.540 1.00 28.13  ? 170 TYR C O     1 
ATOM   10476 C  CB    . TYR C 3 170 ? 168.967 194.132 149.921 1.00 24.85  ? 170 TYR C CB    1 
ATOM   10477 C  CG    . TYR C 3 170 ? 167.562 194.446 149.463 1.00 27.74  ? 170 TYR C CG    1 
ATOM   10478 C  CD1   . TYR C 3 170 ? 166.600 193.449 149.383 1.00 24.95  ? 170 TYR C CD1   1 
ATOM   10479 C  CD2   . TYR C 3 170 ? 167.191 195.743 149.132 1.00 25.82  ? 170 TYR C CD2   1 
ATOM   10480 C  CE1   . TYR C 3 170 ? 165.313 193.730 148.974 1.00 28.96  ? 170 TYR C CE1   1 
ATOM   10481 C  CE2   . TYR C 3 170 ? 165.905 196.034 148.721 1.00 30.15  ? 170 TYR C CE2   1 
ATOM   10482 C  CZ    . TYR C 3 170 ? 164.970 195.024 148.644 1.00 28.06  ? 170 TYR C CZ    1 
ATOM   10483 O  OH    . TYR C 3 170 ? 163.688 195.307 148.236 1.00 34.25  ? 170 TYR C OH    1 
ATOM   10484 N  N     . ILE C 3 171 ? 169.464 191.728 147.425 1.00 27.16  ? 171 ILE C N     1 
ATOM   10485 C  CA    . ILE C 3 171 ? 169.456 190.294 147.153 1.00 17.68  ? 171 ILE C CA    1 
ATOM   10486 C  C     . ILE C 3 171 ? 170.762 189.813 146.544 1.00 25.82  ? 171 ILE C C     1 
ATOM   10487 O  O     . ILE C 3 171 ? 171.001 188.599 146.488 1.00 29.06  ? 171 ILE C O     1 
ATOM   10488 C  CB    . ILE C 3 171 ? 168.277 189.894 146.242 1.00 23.48  ? 171 ILE C CB    1 
ATOM   10489 C  CG1   . ILE C 3 171 ? 168.358 190.628 144.903 1.00 30.93  ? 171 ILE C CG1   1 
ATOM   10490 C  CG2   . ILE C 3 171 ? 166.950 190.154 146.940 1.00 20.58  ? 171 ILE C CG2   1 
ATOM   10491 C  CD1   . ILE C 3 171 ? 167.958 189.776 143.719 1.00 18.65  ? 171 ILE C CD1   1 
ATOM   10492 N  N     . GLY C 3 172 ? 171.608 190.721 146.084 1.00 23.61  ? 172 GLY C N     1 
ATOM   10493 C  CA    . GLY C 3 172 ? 172.867 190.325 145.498 1.00 19.02  ? 172 GLY C CA    1 
ATOM   10494 C  C     . GLY C 3 172 ? 173.846 191.474 145.469 1.00 21.09  ? 172 GLY C C     1 
ATOM   10495 O  O     . GLY C 3 172 ? 173.517 192.604 145.832 1.00 33.93  ? 172 GLY C O     1 
ATOM   10496 N  N     . GLN C 3 173 ? 175.063 191.166 145.036 1.00 23.44  ? 173 GLN C N     1 
ATOM   10497 C  CA    . GLN C 3 173 ? 176.130 192.142 144.915 1.00 24.32  ? 173 GLN C CA    1 
ATOM   10498 C  C     . GLN C 3 173 ? 176.411 192.418 143.447 1.00 24.33  ? 173 GLN C C     1 
ATOM   10499 O  O     . GLN C 3 173 ? 176.291 191.518 142.609 1.00 31.15  ? 173 GLN C O     1 
ATOM   10500 C  CB    . GLN C 3 173 ? 177.412 191.644 145.598 1.00 27.49  ? 173 GLN C CB    1 
ATOM   10501 C  CG    . GLN C 3 173 ? 177.634 192.201 146.993 1.00 29.05  ? 173 GLN C CG    1 
ATOM   10502 C  CD    . GLN C 3 173 ? 179.028 191.918 147.519 1.00 34.61  ? 173 GLN C CD    1 
ATOM   10503 O  OE1   . GLN C 3 173 ? 179.491 192.561 148.460 1.00 33.34  ? 173 GLN C OE1   1 
ATOM   10504 N  NE2   . GLN C 3 173 ? 179.703 190.947 146.914 1.00 35.57  ? 173 GLN C NE2   1 
ATOM   10505 N  N     . PRO C 3 174 ? 176.778 193.651 143.102 1.00 27.79  ? 174 PRO C N     1 
ATOM   10506 C  CA    . PRO C 3 174 ? 177.221 193.922 141.730 1.00 29.24  ? 174 PRO C CA    1 
ATOM   10507 C  C     . PRO C 3 174 ? 178.534 193.208 141.447 1.00 27.91  ? 174 PRO C C     1 
ATOM   10508 O  O     . PRO C 3 174 ? 179.449 193.204 142.274 1.00 25.09  ? 174 PRO C O     1 
ATOM   10509 C  CB    . PRO C 3 174 ? 177.372 195.445 141.705 1.00 22.33  ? 174 PRO C CB    1 
ATOM   10510 C  CG    . PRO C 3 174 ? 177.720 195.791 143.114 1.00 29.39  ? 174 PRO C CG    1 
ATOM   10511 C  CD    . PRO C 3 174 ? 176.916 194.837 143.967 1.00 20.41  ? 174 PRO C CD    1 
ATOM   10512 N  N     . VAL C 3 175 ? 178.620 192.589 140.269 1.00 21.94  ? 175 VAL C N     1 
ATOM   10513 C  CA    . VAL C 3 175 ? 179.741 191.723 139.932 1.00 24.78  ? 175 VAL C CA    1 
ATOM   10514 C  C     . VAL C 3 175 ? 180.197 191.993 138.505 1.00 26.38  ? 175 VAL C C     1 
ATOM   10515 O  O     . VAL C 3 175 ? 179.477 192.578 137.694 1.00 29.93  ? 175 VAL C O     1 
ATOM   10516 C  CB    . VAL C 3 175 ? 179.385 190.231 140.103 1.00 26.91  ? 175 VAL C CB    1 
ATOM   10517 C  CG1   . VAL C 3 175 ? 179.442 189.844 141.570 1.00 22.09  ? 175 VAL C CG1   1 
ATOM   10518 C  CG2   . VAL C 3 175 ? 178.013 189.939 139.516 1.00 19.59  ? 175 VAL C CG2   1 
ATOM   10519 N  N     . VAL C 3 176 ? 181.416 191.550 138.209 1.00 26.62  ? 176 VAL C N     1 
ATOM   10520 C  CA    . VAL C 3 176 ? 182.030 191.696 136.895 1.00 25.56  ? 176 VAL C CA    1 
ATOM   10521 C  C     . VAL C 3 176 ? 182.358 190.307 136.365 1.00 23.02  ? 176 VAL C C     1 
ATOM   10522 O  O     . VAL C 3 176 ? 182.955 189.492 137.077 1.00 33.28  ? 176 VAL C O     1 
ATOM   10523 C  CB    . VAL C 3 176 ? 183.298 192.568 136.952 1.00 27.31  ? 176 VAL C CB    1 
ATOM   10524 C  CG1   . VAL C 3 176 ? 183.813 192.850 135.549 1.00 31.13  ? 176 VAL C CG1   1 
ATOM   10525 C  CG2   . VAL C 3 176 ? 183.021 193.866 137.694 1.00 28.97  ? 176 VAL C CG2   1 
ATOM   10526 N  N     . ASN C 3 177 ? 181.968 190.041 135.121 1.00 20.65  ? 177 ASN C N     1 
ATOM   10527 C  CA    . ASN C 3 177 ? 182.277 188.772 134.465 1.00 22.36  ? 177 ASN C CA    1 
ATOM   10528 C  C     . ASN C 3 177 ? 183.748 188.789 134.067 1.00 20.20  ? 177 ASN C C     1 
ATOM   10529 O  O     . ASN C 3 177 ? 184.136 189.451 133.103 1.00 29.62  ? 177 ASN C O     1 
ATOM   10530 C  CB    . ASN C 3 177 ? 181.372 188.558 133.257 1.00 19.48  ? 177 ASN C CB    1 
ATOM   10531 C  CG    . ASN C 3 177 ? 181.269 187.100 132.857 1.00 25.79  ? 177 ASN C CG    1 
ATOM   10532 O  OD1   . ASN C 3 177 ? 182.265 186.379 132.832 1.00 30.62  ? 177 ASN C OD1   1 
ATOM   10533 N  ND2   . ASN C 3 177 ? 180.058 186.658 132.542 1.00 23.13  ? 177 ASN C ND2   1 
ATOM   10534 N  N     . ILE C 3 178 ? 184.573 188.052 134.814 1.00 8.77   ? 178 ILE C N     1 
ATOM   10535 C  CA    . ILE C 3 178 ? 186.018 188.104 134.608 1.00 15.25  ? 178 ILE C CA    1 
ATOM   10536 C  C     . ILE C 3 178 ? 186.401 187.479 133.271 1.00 22.41  ? 178 ILE C C     1 
ATOM   10537 O  O     . ILE C 3 178 ? 187.206 188.041 132.519 1.00 26.59  ? 178 ILE C O     1 
ATOM   10538 C  CB    . ILE C 3 178 ? 186.745 187.427 135.784 1.00 22.23  ? 178 ILE C CB    1 
ATOM   10539 C  CG1   . ILE C 3 178 ? 186.709 188.329 137.018 1.00 20.67  ? 178 ILE C CG1   1 
ATOM   10540 C  CG2   . ILE C 3 178 ? 188.181 187.095 135.411 1.00 17.61  ? 178 ILE C CG2   1 
ATOM   10541 C  CD1   . ILE C 3 178 ? 186.682 187.571 138.322 1.00 22.06  ? 178 ILE C CD1   1 
ATOM   10542 N  N     . VAL C 3 179 ? 185.837 186.311 132.954 1.00 17.23  ? 179 VAL C N     1 
ATOM   10543 C  CA    . VAL C 3 179 ? 186.191 185.624 131.713 1.00 19.60  ? 179 VAL C CA    1 
ATOM   10544 C  C     . VAL C 3 179 ? 185.788 186.465 130.506 1.00 21.00  ? 179 VAL C C     1 
ATOM   10545 O  O     . VAL C 3 179 ? 186.562 186.630 129.555 1.00 21.79  ? 179 VAL C O     1 
ATOM   10546 C  CB    . VAL C 3 179 ? 185.551 184.224 131.671 1.00 19.59  ? 179 VAL C CB    1 
ATOM   10547 C  CG1   . VAL C 3 179 ? 185.319 183.777 130.235 1.00 21.03  ? 179 VAL C CG1   1 
ATOM   10548 C  CG2   . VAL C 3 179 ? 186.427 183.220 132.403 1.00 16.66  ? 179 VAL C CG2   1 
ATOM   10549 N  N     . GLU C 3 180 ? 184.572 187.015 130.531 1.00 23.14  ? 180 GLU C N     1 
ATOM   10550 C  CA    . GLU C 3 180 ? 184.114 187.845 129.421 1.00 23.16  ? 180 GLU C CA    1 
ATOM   10551 C  C     . GLU C 3 180 ? 184.927 189.130 129.316 1.00 25.63  ? 180 GLU C C     1 
ATOM   10552 O  O     . GLU C 3 180 ? 185.258 189.571 128.209 1.00 27.49  ? 180 GLU C O     1 
ATOM   10553 C  CB    . GLU C 3 180 ? 182.627 188.158 129.581 1.00 28.84  ? 180 GLU C CB    1 
ATOM   10554 C  CG    . GLU C 3 180 ? 181.713 186.989 129.256 1.00 29.32  ? 180 GLU C CG    1 
ATOM   10555 C  CD    . GLU C 3 180 ? 180.247 187.375 129.267 1.00 35.41  ? 180 GLU C CD    1 
ATOM   10556 O  OE1   . GLU C 3 180 ? 179.949 188.587 129.272 1.00 40.16  ? 180 GLU C OE1   1 
ATOM   10557 O  OE2   . GLU C 3 180 ? 179.393 186.464 129.270 1.00 39.46  ? 180 GLU C OE2   1 
ATOM   10558 N  N     . LEU C 3 181 ? 185.247 189.750 130.454 1.00 23.39  ? 181 LEU C N     1 
ATOM   10559 C  CA    . LEU C 3 181 ? 186.046 190.971 130.434 1.00 24.24  ? 181 LEU C CA    1 
ATOM   10560 C  C     . LEU C 3 181 ? 187.451 190.706 129.905 1.00 28.61  ? 181 LEU C C     1 
ATOM   10561 O  O     . LEU C 3 181 ? 187.981 191.495 129.114 1.00 28.24  ? 181 LEU C O     1 
ATOM   10562 C  CB    . LEU C 3 181 ? 186.102 191.582 131.834 1.00 25.71  ? 181 LEU C CB    1 
ATOM   10563 C  CG    . LEU C 3 181 ? 187.089 192.724 132.087 1.00 29.84  ? 181 LEU C CG    1 
ATOM   10564 C  CD1   . LEU C 3 181 ? 186.844 193.881 131.130 1.00 22.22  ? 181 LEU C CD1   1 
ATOM   10565 C  CD2   . LEU C 3 181 ? 187.002 193.193 133.531 1.00 23.15  ? 181 LEU C CD2   1 
ATOM   10566 N  N     . ASN C 3 182 ? 188.071 189.604 130.333 1.00 24.60  ? 182 ASN C N     1 
ATOM   10567 C  CA    . ASN C 3 182 ? 189.410 189.277 129.855 1.00 24.42  ? 182 ASN C CA    1 
ATOM   10568 C  C     . ASN C 3 182 ? 189.399 188.919 128.374 1.00 27.23  ? 182 ASN C C     1 
ATOM   10569 O  O     . ASN C 3 182 ? 190.334 189.260 127.641 1.00 32.90  ? 182 ASN C O     1 
ATOM   10570 C  CB    . ASN C 3 182 ? 190.002 188.137 130.683 1.00 25.34  ? 182 ASN C CB    1 
ATOM   10571 C  CG    . ASN C 3 182 ? 190.645 188.624 131.967 1.00 23.73  ? 182 ASN C CG    1 
ATOM   10572 O  OD1   . ASN C 3 182 ? 191.190 189.726 132.022 1.00 26.45  ? 182 ASN C OD1   1 
ATOM   10573 N  ND2   . ASN C 3 182 ? 190.585 187.803 133.008 1.00 25.23  ? 182 ASN C ND2   1 
ATOM   10574 N  N     . LEU C 3 183 ? 188.355 188.222 127.918 1.00 27.41  ? 183 LEU C N     1 
ATOM   10575 C  CA    . LEU C 3 183 ? 188.247 187.898 126.499 1.00 30.00  ? 183 LEU C CA    1 
ATOM   10576 C  C     . LEU C 3 183 ? 188.113 189.159 125.655 1.00 30.36  ? 183 LEU C C     1 
ATOM   10577 O  O     . LEU C 3 183 ? 188.731 189.271 124.590 1.00 36.78  ? 183 LEU C O     1 
ATOM   10578 C  CB    . LEU C 3 183 ? 187.061 186.963 126.262 1.00 27.92  ? 183 LEU C CB    1 
ATOM   10579 C  CG    . LEU C 3 183 ? 187.354 185.464 126.342 1.00 30.09  ? 183 LEU C CG    1 
ATOM   10580 C  CD1   . LEU C 3 183 ? 186.089 184.688 126.672 1.00 30.30  ? 183 LEU C CD1   1 
ATOM   10581 C  CD2   . LEU C 3 183 ? 187.974 184.965 125.046 1.00 33.87  ? 183 LEU C CD2   1 
ATOM   10582 N  N     . ALA C 3 184 ? 187.305 190.119 126.113 1.00 27.62  ? 184 ALA C N     1 
ATOM   10583 C  CA    . ALA C 3 184 ? 187.193 191.389 125.405 1.00 32.22  ? 184 ALA C CA    1 
ATOM   10584 C  C     . ALA C 3 184 ? 188.487 192.188 125.479 1.00 36.00  ? 184 ALA C C     1 
ATOM   10585 O  O     . ALA C 3 184 ? 188.769 192.994 124.585 1.00 39.56  ? 184 ALA C O     1 
ATOM   10586 C  CB    . ALA C 3 184 ? 186.034 192.207 125.970 1.00 27.15  ? 184 ALA C CB    1 
ATOM   10587 N  N     . LEU C 3 185 ? 189.278 191.983 126.534 1.00 37.96  ? 185 LEU C N     1 
ATOM   10588 C  CA    . LEU C 3 185 ? 190.561 192.666 126.644 1.00 35.33  ? 185 LEU C CA    1 
ATOM   10589 C  C     . LEU C 3 185 ? 191.525 192.199 125.561 1.00 36.79  ? 185 LEU C C     1 
ATOM   10590 O  O     . LEU C 3 185 ? 192.399 192.959 125.126 1.00 42.34  ? 185 LEU C O     1 
ATOM   10591 C  CB    . LEU C 3 185 ? 191.154 192.433 128.033 1.00 35.69  ? 185 LEU C CB    1 
ATOM   10592 C  CG    . LEU C 3 185 ? 192.002 193.545 128.650 1.00 41.27  ? 185 LEU C CG    1 
ATOM   10593 C  CD1   . LEU C 3 185 ? 191.359 194.905 128.440 1.00 38.48  ? 185 LEU C CD1   1 
ATOM   10594 C  CD2   . LEU C 3 185 ? 192.216 193.276 130.129 1.00 39.47  ? 185 LEU C CD2   1 
ATOM   10595 N  N     . ASP C 3 186 ? 191.382 190.950 125.113 1.00 42.23  ? 186 ASP C N     1 
ATOM   10596 C  CA    . ASP C 3 186 ? 192.229 190.450 124.035 1.00 42.48  ? 186 ASP C CA    1 
ATOM   10597 C  C     . ASP C 3 186 ? 191.822 191.047 122.694 1.00 47.75  ? 186 ASP C C     1 
ATOM   10598 O  O     . ASP C 3 186 ? 192.678 191.352 121.856 1.00 54.48  ? 186 ASP C O     1 
ATOM   10599 C  CB    . ASP C 3 186 ? 192.165 188.924 123.984 1.00 40.47  ? 186 ASP C CB    1 
ATOM   10600 C  CG    . ASP C 3 186 ? 193.064 188.269 125.013 1.00 47.79  ? 186 ASP C CG    1 
ATOM   10601 O  OD1   . ASP C 3 186 ? 193.903 188.975 125.609 1.00 49.13  ? 186 ASP C OD1   1 
ATOM   10602 O  OD2   . ASP C 3 186 ? 192.931 187.045 125.226 1.00 49.46  ? 186 ASP C OD2   1 
ATOM   10603 N  N     . LYS C 3 187 ? 190.516 191.217 122.471 1.00 50.08  ? 187 LYS C N     1 
ATOM   10604 C  CA    . LYS C 3 187 ? 190.050 191.813 121.223 1.00 47.23  ? 187 LYS C CA    1 
ATOM   10605 C  C     . LYS C 3 187 ? 190.437 193.285 121.135 1.00 51.67  ? 187 LYS C C     1 
ATOM   10606 O  O     . LYS C 3 187 ? 190.785 193.777 120.055 1.00 56.21  ? 187 LYS C O     1 
ATOM   10607 C  CB    . LYS C 3 187 ? 188.537 191.647 121.095 1.00 47.38  ? 187 LYS C CB    1 
ATOM   10608 C  CG    . LYS C 3 187 ? 188.082 190.206 120.942 1.00 48.18  ? 187 LYS C CG    1 
ATOM   10609 C  CD    . LYS C 3 187 ? 186.613 190.051 121.298 1.00 53.24  ? 187 LYS C CD    1 
ATOM   10610 C  CE    . LYS C 3 187 ? 186.166 188.604 121.178 1.00 53.17  ? 187 LYS C CE    1 
ATOM   10611 N  NZ    . LYS C 3 187 ? 187.197 187.660 121.692 1.00 49.68  ? 187 LYS C NZ    1 
ATOM   10612 N  N     . LEU C 3 188 ? 190.377 194.003 122.259 1.00 53.89  ? 188 LEU C N     1 
ATOM   10613 C  CA    . LEU C 3 188 ? 190.762 195.411 122.258 1.00 52.58  ? 188 LEU C CA    1 
ATOM   10614 C  C     . LEU C 3 188 ? 192.247 195.575 121.959 1.00 58.28  ? 188 LEU C C     1 
ATOM   10615 O  O     . LEU C 3 188 ? 192.649 196.516 121.265 1.00 60.51  ? 188 LEU C O     1 
ATOM   10616 C  CB    . LEU C 3 188 ? 190.411 196.052 123.601 1.00 51.45  ? 188 LEU C CB    1 
ATOM   10617 C  CG    . LEU C 3 188 ? 190.260 197.575 123.614 1.00 54.94  ? 188 LEU C CG    1 
ATOM   10618 C  CD1   . LEU C 3 188 ? 189.437 198.047 122.424 1.00 57.03  ? 188 LEU C CD1   1 
ATOM   10619 C  CD2   . LEU C 3 188 ? 189.640 198.044 124.921 1.00 55.80  ? 188 LEU C CD2   1 
ATOM   10620 N  N     . ASP C 3 189 ? 193.078 194.666 122.475 1.00 61.21  ? 189 ASP C N     1 
ATOM   10621 C  CA    . ASP C 3 189 ? 194.509 194.737 122.205 1.00 60.55  ? 189 ASP C CA    1 
ATOM   10622 C  C     . ASP C 3 189 ? 194.831 194.321 120.776 1.00 62.19  ? 189 ASP C C     1 
ATOM   10623 O  O     . ASP C 3 189 ? 195.877 194.704 120.240 1.00 64.52  ? 189 ASP C O     1 
ATOM   10624 C  CB    . ASP C 3 189 ? 195.272 193.863 123.201 1.00 59.71  ? 189 ASP C CB    1 
ATOM   10625 C  CG    . ASP C 3 189 ? 196.676 194.369 123.468 1.00 62.88  ? 189 ASP C CG    1 
ATOM   10626 O  OD1   . ASP C 3 189 ? 197.484 194.424 122.518 1.00 62.34  ? 189 ASP C OD1   1 
ATOM   10627 O  OD2   . ASP C 3 189 ? 196.972 194.711 124.632 1.00 61.39  ? 189 ASP C OD2   1 
ATOM   10628 N  N     . GLU C 3 190 ? 193.951 193.550 120.145 1.00 65.67  ? 190 GLU C N     1 
ATOM   10629 C  CA    . GLU C 3 190 ? 194.161 193.110 118.771 1.00 67.87  ? 190 GLU C CA    1 
ATOM   10630 C  C     . GLU C 3 190 ? 193.729 194.186 117.781 1.00 68.91  ? 190 GLU C C     1 
ATOM   10631 O  O     . GLU C 3 190 ? 194.561 194.791 117.104 1.00 70.77  ? 190 GLU C O     1 
ATOM   10632 C  CB    . GLU C 3 190 ? 193.400 191.810 118.502 1.00 66.50  ? 190 GLU C CB    1 
ATOM   10633 C  CG    . GLU C 3 190 ? 193.885 191.050 117.278 1.00 68.83  ? 190 GLU C CG    1 
ATOM   10634 C  CD    . GLU C 3 190 ? 195.198 190.332 117.520 1.00 71.24  ? 190 GLU C CD    1 
ATOM   10635 O  OE1   . GLU C 3 190 ? 195.436 189.896 118.666 1.00 70.61  ? 190 GLU C OE1   1 
ATOM   10636 O  OE2   . GLU C 3 190 ? 195.992 190.205 116.565 1.00 70.90  ? 190 GLU C OE2   1 
ATOM   10637 N  N     . MET D 4 1   ? 191.198 150.103 175.242 1.00 72.30  ? 1   MET D N     1 
ATOM   10638 C  CA    . MET D 4 1   ? 190.438 151.117 175.963 1.00 71.41  ? 1   MET D CA    1 
ATOM   10639 C  C     . MET D 4 1   ? 190.694 151.024 177.464 1.00 71.77  ? 1   MET D C     1 
ATOM   10640 O  O     . MET D 4 1   ? 190.928 149.938 177.996 1.00 72.26  ? 1   MET D O     1 
ATOM   10641 C  CB    . MET D 4 1   ? 188.942 150.974 175.671 1.00 69.66  ? 1   MET D CB    1 
ATOM   10642 C  CG    . MET D 4 1   ? 188.126 152.219 175.980 1.00 71.86  ? 1   MET D CG    1 
ATOM   10643 S  SD    . MET D 4 1   ? 187.805 153.223 174.517 1.00 81.61  ? 1   MET D SD    1 
ATOM   10644 C  CE    . MET D 4 1   ? 188.891 154.615 174.816 1.00 70.74  ? 1   MET D CE    1 
ATOM   10645 N  N     . SER D 4 2   ? 190.650 152.169 178.139 1.00 63.41  ? 2   SER D N     1 
ATOM   10646 C  CA    . SER D 4 2   ? 190.894 152.207 179.573 1.00 63.39  ? 2   SER D CA    1 
ATOM   10647 C  C     . SER D 4 2   ? 189.784 151.486 180.330 1.00 62.46  ? 2   SER D C     1 
ATOM   10648 O  O     . SER D 4 2   ? 188.638 151.411 179.880 1.00 62.26  ? 2   SER D O     1 
ATOM   10649 C  CB    . SER D 4 2   ? 191.001 153.653 180.057 1.00 63.28  ? 2   SER D CB    1 
ATOM   10650 O  OG    . SER D 4 2   ? 191.170 153.711 181.463 1.00 65.88  ? 2   SER D OG    1 
ATOM   10651 N  N     . ALA D 4 3   ? 190.141 150.946 181.499 1.00 59.67  ? 3   ALA D N     1 
ATOM   10652 C  CA    . ALA D 4 3   ? 189.160 150.229 182.305 1.00 56.75  ? 3   ALA D CA    1 
ATOM   10653 C  C     . ALA D 4 3   ? 188.152 151.178 182.938 1.00 56.70  ? 3   ALA D C     1 
ATOM   10654 O  O     . ALA D 4 3   ? 187.062 150.750 183.335 1.00 56.53  ? 3   ALA D O     1 
ATOM   10655 C  CB    . ALA D 4 3   ? 189.864 149.406 183.384 1.00 56.57  ? 3   ALA D CB    1 
ATOM   10656 N  N     . GLY D 4 4   ? 188.490 152.465 183.037 1.00 53.70  ? 4   GLY D N     1 
ATOM   10657 C  CA    . GLY D 4 4   ? 187.541 153.428 183.565 1.00 50.99  ? 4   GLY D CA    1 
ATOM   10658 C  C     . GLY D 4 4   ? 186.531 153.885 182.534 1.00 49.38  ? 4   GLY D C     1 
ATOM   10659 O  O     . GLY D 4 4   ? 185.416 154.280 182.886 1.00 52.31  ? 4   GLY D O     1 
ATOM   10660 N  N     . VAL D 4 5   ? 186.901 153.841 181.254 1.00 48.67  ? 5   VAL D N     1 
ATOM   10661 C  CA    . VAL D 4 5   ? 185.957 154.180 180.195 1.00 47.46  ? 5   VAL D CA    1 
ATOM   10662 C  C     . VAL D 4 5   ? 184.884 153.106 180.069 1.00 50.54  ? 5   VAL D C     1 
ATOM   10663 O  O     . VAL D 4 5   ? 183.699 153.412 179.894 1.00 51.20  ? 5   VAL D O     1 
ATOM   10664 C  CB    . VAL D 4 5   ? 186.702 154.397 178.866 1.00 50.44  ? 5   VAL D CB    1 
ATOM   10665 C  CG1   . VAL D 4 5   ? 185.746 154.891 177.798 1.00 47.49  ? 5   VAL D CG1   1 
ATOM   10666 C  CG2   . VAL D 4 5   ? 187.843 155.382 179.056 1.00 49.34  ? 5   VAL D CG2   1 
ATOM   10667 N  N     . ILE D 4 6   ? 185.280 151.833 180.149 1.00 48.93  ? 6   ILE D N     1 
ATOM   10668 C  CA    . ILE D 4 6   ? 184.319 150.741 180.007 1.00 48.75  ? 6   ILE D CA    1 
ATOM   10669 C  C     . ILE D 4 6   ? 183.297 150.782 181.135 1.00 48.05  ? 6   ILE D C     1 
ATOM   10670 O  O     . ILE D 4 6   ? 182.086 150.692 180.902 1.00 47.78  ? 6   ILE D O     1 
ATOM   10671 C  CB    . ILE D 4 6   ? 185.048 149.386 179.952 1.00 51.68  ? 6   ILE D CB    1 
ATOM   10672 C  CG1   . ILE D 4 6   ? 185.667 149.170 178.570 1.00 49.79  ? 6   ILE D CG1   1 
ATOM   10673 C  CG2   . ILE D 4 6   ? 184.098 148.248 180.295 1.00 50.05  ? 6   ILE D CG2   1 
ATOM   10674 C  CD1   . ILE D 4 6   ? 187.099 148.686 178.612 1.00 51.54  ? 6   ILE D CD1   1 
ATOM   10675 N  N     . THR D 4 7   ? 183.766 150.938 182.376 1.00 45.58  ? 7   THR D N     1 
ATOM   10676 C  CA    . THR D 4 7   ? 182.843 150.978 183.506 1.00 45.97  ? 7   THR D CA    1 
ATOM   10677 C  C     . THR D 4 7   ? 182.020 152.260 183.515 1.00 44.98  ? 7   THR D C     1 
ATOM   10678 O  O     . THR D 4 7   ? 180.999 152.334 184.208 1.00 46.18  ? 7   THR D O     1 
ATOM   10679 C  CB    . THR D 4 7   ? 183.605 150.828 184.823 1.00 45.42  ? 7   THR D CB    1 
ATOM   10680 O  OG1   . THR D 4 7   ? 182.672 150.720 185.906 1.00 46.07  ? 7   THR D OG1   1 
ATOM   10681 C  CG2   . THR D 4 7   ? 184.505 152.027 185.061 1.00 46.28  ? 7   THR D CG2   1 
ATOM   10682 N  N     . GLY D 4 8   ? 182.442 153.274 182.759 1.00 42.49  ? 8   GLY D N     1 
ATOM   10683 C  CA    . GLY D 4 8   ? 181.655 154.493 182.674 1.00 40.78  ? 8   GLY D CA    1 
ATOM   10684 C  C     . GLY D 4 8   ? 180.616 154.440 181.571 1.00 40.16  ? 8   GLY D C     1 
ATOM   10685 O  O     . GLY D 4 8   ? 179.669 155.229 181.560 1.00 41.76  ? 8   GLY D O     1 
ATOM   10686 N  N     . VAL D 4 9   ? 180.777 153.509 180.628 1.00 39.72  ? 9   VAL D N     1 
ATOM   10687 C  CA    . VAL D 4 9   ? 179.811 153.382 179.542 1.00 38.34  ? 9   VAL D CA    1 
ATOM   10688 C  C     . VAL D 4 9   ? 178.641 152.501 179.965 1.00 38.78  ? 9   VAL D C     1 
ATOM   10689 O  O     . VAL D 4 9   ? 177.477 152.822 179.697 1.00 37.04  ? 9   VAL D O     1 
ATOM   10690 C  CB    . VAL D 4 9   ? 180.502 152.845 178.274 1.00 40.11  ? 9   VAL D CB    1 
ATOM   10691 C  CG1   . VAL D 4 9   ? 179.473 152.381 177.258 1.00 40.25  ? 9   VAL D CG1   1 
ATOM   10692 C  CG2   . VAL D 4 9   ? 181.399 153.914 177.670 1.00 38.16  ? 9   VAL D CG2   1 
ATOM   10693 N  N     . LEU D 4 10  ? 178.927 151.381 180.636 1.00 42.13  ? 10  LEU D N     1 
ATOM   10694 C  CA    . LEU D 4 10  ? 177.855 150.508 181.104 1.00 38.50  ? 10  LEU D CA    1 
ATOM   10695 C  C     . LEU D 4 10  ? 176.974 151.210 182.128 1.00 39.72  ? 10  LEU D C     1 
ATOM   10696 O  O     . LEU D 4 10  ? 175.749 151.049 182.115 1.00 39.87  ? 10  LEU D O     1 
ATOM   10697 C  CB    . LEU D 4 10  ? 178.431 149.219 181.691 1.00 40.65  ? 10  LEU D CB    1 
ATOM   10698 C  CG    . LEU D 4 10  ? 179.709 148.653 181.071 1.00 44.21  ? 10  LEU D CG    1 
ATOM   10699 C  CD1   . LEU D 4 10  ? 180.383 147.683 182.028 1.00 42.67  ? 10  LEU D CD1   1 
ATOM   10700 C  CD2   . LEU D 4 10  ? 179.411 147.980 179.740 1.00 41.03  ? 10  LEU D CD2   1 
ATOM   10701 N  N     . LEU D 4 11  ? 177.579 151.994 183.025 1.00 34.45  ? 11  LEU D N     1 
ATOM   10702 C  CA    . LEU D 4 11  ? 176.797 152.700 184.035 1.00 36.15  ? 11  LEU D CA    1 
ATOM   10703 C  C     . LEU D 4 11  ? 175.806 153.662 183.392 1.00 38.93  ? 11  LEU D C     1 
ATOM   10704 O  O     . LEU D 4 11  ? 174.649 153.749 183.818 1.00 41.47  ? 11  LEU D O     1 
ATOM   10705 C  CB    . LEU D 4 11  ? 177.724 153.447 184.993 1.00 37.05  ? 11  LEU D CB    1 
ATOM   10706 C  CG    . LEU D 4 11  ? 177.043 154.302 186.065 1.00 36.80  ? 11  LEU D CG    1 
ATOM   10707 C  CD1   . LEU D 4 11  ? 176.065 153.471 186.883 1.00 36.41  ? 11  LEU D CD1   1 
ATOM   10708 C  CD2   . LEU D 4 11  ? 178.075 154.961 186.966 1.00 38.87  ? 11  LEU D CD2   1 
ATOM   10709 N  N     . VAL D 4 12  ? 176.243 154.392 182.364 1.00 29.29  ? 12  VAL D N     1 
ATOM   10710 C  CA    . VAL D 4 12  ? 175.332 155.278 181.645 1.00 35.14  ? 12  VAL D CA    1 
ATOM   10711 C  C     . VAL D 4 12  ? 174.268 154.467 180.917 1.00 35.11  ? 12  VAL D C     1 
ATOM   10712 O  O     . VAL D 4 12  ? 173.091 154.848 180.879 1.00 37.19  ? 12  VAL D O     1 
ATOM   10713 C  CB    . VAL D 4 12  ? 176.122 156.184 180.681 1.00 34.39  ? 12  VAL D CB    1 
ATOM   10714 C  CG1   . VAL D 4 12  ? 175.178 157.023 179.835 1.00 31.19  ? 12  VAL D CG1   1 
ATOM   10715 C  CG2   . VAL D 4 12  ? 177.072 157.076 181.460 1.00 37.60  ? 12  VAL D CG2   1 
ATOM   10716 N  N     . PHE D 4 13  ? 174.662 153.333 180.329 1.00 36.00  ? 13  PHE D N     1 
ATOM   10717 C  CA    . PHE D 4 13  ? 173.701 152.493 179.621 1.00 33.22  ? 13  PHE D CA    1 
ATOM   10718 C  C     . PHE D 4 13  ? 172.660 151.914 180.572 1.00 33.62  ? 13  PHE D C     1 
ATOM   10719 O  O     . PHE D 4 13  ? 171.469 151.867 180.242 1.00 34.67  ? 13  PHE D O     1 
ATOM   10720 C  CB    . PHE D 4 13  ? 174.430 151.374 178.877 1.00 36.65  ? 13  PHE D CB    1 
ATOM   10721 C  CG    . PHE D 4 13  ? 174.970 151.789 177.539 1.00 42.45  ? 13  PHE D CG    1 
ATOM   10722 C  CD1   . PHE D 4 13  ? 174.516 152.942 176.921 1.00 37.88  ? 13  PHE D CD1   1 
ATOM   10723 C  CD2   . PHE D 4 13  ? 175.929 151.024 176.896 1.00 44.72  ? 13  PHE D CD2   1 
ATOM   10724 C  CE1   . PHE D 4 13  ? 175.011 153.327 175.691 1.00 39.69  ? 13  PHE D CE1   1 
ATOM   10725 C  CE2   . PHE D 4 13  ? 176.427 151.403 175.663 1.00 41.92  ? 13  PHE D CE2   1 
ATOM   10726 C  CZ    . PHE D 4 13  ? 175.967 152.557 175.060 1.00 41.91  ? 13  PHE D CZ    1 
ATOM   10727 N  N     . LEU D 4 14  ? 173.088 151.459 181.753 1.00 29.21  ? 14  LEU D N     1 
ATOM   10728 C  CA    . LEU D 4 14  ? 172.136 150.936 182.728 1.00 32.39  ? 14  LEU D CA    1 
ATOM   10729 C  C     . LEU D 4 14  ? 171.187 152.023 183.217 1.00 33.56  ? 14  LEU D C     1 
ATOM   10730 O  O     . LEU D 4 14  ? 169.983 151.785 183.357 1.00 36.98  ? 14  LEU D O     1 
ATOM   10731 C  CB    . LEU D 4 14  ? 172.874 150.300 183.906 1.00 33.65  ? 14  LEU D CB    1 
ATOM   10732 C  CG    . LEU D 4 14  ? 173.775 149.100 183.606 1.00 37.92  ? 14  LEU D CG    1 
ATOM   10733 C  CD1   . LEU D 4 14  ? 174.650 148.775 184.806 1.00 33.27  ? 14  LEU D CD1   1 
ATOM   10734 C  CD2   . LEU D 4 14  ? 172.944 147.893 183.201 1.00 36.88  ? 14  LEU D CD2   1 
ATOM   10735 N  N     . LEU D 4 15  ? 171.712 153.221 183.487 1.00 28.73  ? 15  LEU D N     1 
ATOM   10736 C  CA    . LEU D 4 15  ? 170.858 154.317 183.934 1.00 29.35  ? 15  LEU D CA    1 
ATOM   10737 C  C     . LEU D 4 15  ? 169.868 154.726 182.850 1.00 24.96  ? 15  LEU D C     1 
ATOM   10738 O  O     . LEU D 4 15  ? 168.693 154.981 183.142 1.00 32.39  ? 15  LEU D O     1 
ATOM   10739 C  CB    . LEU D 4 15  ? 171.711 155.511 184.362 1.00 32.27  ? 15  LEU D CB    1 
ATOM   10740 C  CG    . LEU D 4 15  ? 172.511 155.342 185.655 1.00 32.65  ? 15  LEU D CG    1 
ATOM   10741 C  CD1   . LEU D 4 15  ? 173.138 156.661 186.069 1.00 28.06  ? 15  LEU D CD1   1 
ATOM   10742 C  CD2   . LEU D 4 15  ? 171.632 154.789 186.767 1.00 29.88  ? 15  LEU D CD2   1 
ATOM   10743 N  N     . LEU D 4 16  ? 170.322 154.802 181.597 1.00 28.76  ? 16  LEU D N     1 
ATOM   10744 C  CA    . LEU D 4 16  ? 169.413 155.132 180.503 1.00 23.42  ? 16  LEU D CA    1 
ATOM   10745 C  C     . LEU D 4 16  ? 168.341 154.062 180.337 1.00 28.66  ? 16  LEU D C     1 
ATOM   10746 O  O     . LEU D 4 16  ? 167.164 154.380 180.130 1.00 31.58  ? 16  LEU D O     1 
ATOM   10747 C  CB    . LEU D 4 16  ? 170.193 155.314 179.201 1.00 26.02  ? 16  LEU D CB    1 
ATOM   10748 C  CG    . LEU D 4 16  ? 170.898 156.658 179.011 1.00 29.00  ? 16  LEU D CG    1 
ATOM   10749 C  CD1   . LEU D 4 16  ? 172.044 156.525 178.021 1.00 33.10  ? 16  LEU D CD1   1 
ATOM   10750 C  CD2   . LEU D 4 16  ? 169.913 157.725 178.560 1.00 29.26  ? 16  LEU D CD2   1 
ATOM   10751 N  N     . GLY D 4 17  ? 168.729 152.789 180.424 1.00 31.35  ? 17  GLY D N     1 
ATOM   10752 C  CA    . GLY D 4 17  ? 167.747 151.721 180.334 1.00 23.94  ? 17  GLY D CA    1 
ATOM   10753 C  C     . GLY D 4 17  ? 166.753 151.748 181.479 1.00 22.34  ? 17  GLY D C     1 
ATOM   10754 O  O     . GLY D 4 17  ? 165.563 151.487 181.287 1.00 27.48  ? 17  GLY D O     1 
ATOM   10755 N  N     . TYR D 4 18  ? 167.229 152.060 182.686 1.00 24.61  ? 18  TYR D N     1 
ATOM   10756 C  CA    . TYR D 4 18  ? 166.330 152.178 183.830 1.00 25.70  ? 18  TYR D CA    1 
ATOM   10757 C  C     . TYR D 4 18  ? 165.353 153.333 183.647 1.00 28.82  ? 18  TYR D C     1 
ATOM   10758 O  O     . TYR D 4 18  ? 164.164 153.206 183.962 1.00 27.69  ? 18  TYR D O     1 
ATOM   10759 C  CB    . TYR D 4 18  ? 167.143 152.356 185.113 1.00 26.67  ? 18  TYR D CB    1 
ATOM   10760 C  CG    . TYR D 4 18  ? 166.366 152.960 186.261 1.00 27.83  ? 18  TYR D CG    1 
ATOM   10761 C  CD1   . TYR D 4 18  ? 165.417 152.218 186.949 1.00 31.12  ? 18  TYR D CD1   1 
ATOM   10762 C  CD2   . TYR D 4 18  ? 166.587 154.272 186.660 1.00 27.46  ? 18  TYR D CD2   1 
ATOM   10763 C  CE1   . TYR D 4 18  ? 164.706 152.765 188.000 1.00 30.96  ? 18  TYR D CE1   1 
ATOM   10764 C  CE2   . TYR D 4 18  ? 165.880 154.829 187.710 1.00 25.04  ? 18  TYR D CE2   1 
ATOM   10765 C  CZ    . TYR D 4 18  ? 164.942 154.070 188.376 1.00 31.70  ? 18  TYR D CZ    1 
ATOM   10766 O  OH    . TYR D 4 18  ? 164.236 154.617 189.422 1.00 29.60  ? 18  TYR D OH    1 
ATOM   10767 N  N     . LEU D 4 19  ? 165.836 154.470 183.142 1.00 25.06  ? 19  LEU D N     1 
ATOM   10768 C  CA    . LEU D 4 19  ? 164.959 155.618 182.932 1.00 23.96  ? 19  LEU D CA    1 
ATOM   10769 C  C     . LEU D 4 19  ? 163.994 155.377 181.777 1.00 23.63  ? 19  LEU D C     1 
ATOM   10770 O  O     . LEU D 4 19  ? 162.824 155.771 181.848 1.00 30.82  ? 19  LEU D O     1 
ATOM   10771 C  CB    . LEU D 4 19  ? 165.792 156.875 182.685 1.00 23.95  ? 19  LEU D CB    1 
ATOM   10772 C  CG    . LEU D 4 19  ? 166.600 157.404 183.871 1.00 28.36  ? 19  LEU D CG    1 
ATOM   10773 C  CD1   . LEU D 4 19  ? 167.670 158.375 183.397 1.00 21.72  ? 19  LEU D CD1   1 
ATOM   10774 C  CD2   . LEU D 4 19  ? 165.689 158.063 184.894 1.00 18.93  ? 19  LEU D CD2   1 
ATOM   10775 N  N     . VAL D 4 20  ? 164.467 154.741 180.702 1.00 28.17  ? 20  VAL D N     1 
ATOM   10776 C  CA    . VAL D 4 20  ? 163.587 154.418 179.582 1.00 26.11  ? 20  VAL D CA    1 
ATOM   10777 C  C     . VAL D 4 20  ? 162.499 153.449 180.027 1.00 28.46  ? 20  VAL D C     1 
ATOM   10778 O  O     . VAL D 4 20  ? 161.325 153.599 179.668 1.00 25.63  ? 20  VAL D O     1 
ATOM   10779 C  CB    . VAL D 4 20  ? 164.405 153.858 178.402 1.00 25.73  ? 20  VAL D CB    1 
ATOM   10780 C  CG1   . VAL D 4 20  ? 163.510 153.087 177.443 1.00 28.67  ? 20  VAL D CG1   1 
ATOM   10781 C  CG2   . VAL D 4 20  ? 165.119 154.985 177.671 1.00 27.22  ? 20  VAL D CG2   1 
ATOM   10782 N  N     . TYR D 4 21  ? 162.872 152.442 180.821 1.00 24.25  ? 21  TYR D N     1 
ATOM   10783 C  CA    . TYR D 4 21  ? 161.881 151.522 181.368 1.00 29.49  ? 21  TYR D CA    1 
ATOM   10784 C  C     . TYR D 4 21  ? 160.900 152.249 182.278 1.00 28.48  ? 21  TYR D C     1 
ATOM   10785 O  O     . TYR D 4 21  ? 159.698 151.958 182.268 1.00 29.53  ? 21  TYR D O     1 
ATOM   10786 C  CB    . TYR D 4 21  ? 162.581 150.388 182.119 1.00 27.04  ? 21  TYR D CB    1 
ATOM   10787 C  CG    . TYR D 4 21  ? 161.651 149.498 182.914 1.00 30.21  ? 21  TYR D CG    1 
ATOM   10788 C  CD1   . TYR D 4 21  ? 161.005 148.425 182.315 1.00 31.30  ? 21  TYR D CD1   1 
ATOM   10789 C  CD2   . TYR D 4 21  ? 161.420 149.729 184.265 1.00 34.44  ? 21  TYR D CD2   1 
ATOM   10790 C  CE1   . TYR D 4 21  ? 160.156 147.609 183.036 1.00 32.36  ? 21  TYR D CE1   1 
ATOM   10791 C  CE2   . TYR D 4 21  ? 160.572 148.919 184.994 1.00 33.89  ? 21  TYR D CE2   1 
ATOM   10792 C  CZ    . TYR D 4 21  ? 159.943 147.860 184.374 1.00 34.50  ? 21  TYR D CZ    1 
ATOM   10793 O  OH    . TYR D 4 21  ? 159.098 147.050 185.096 1.00 42.35  ? 21  TYR D OH    1 
ATOM   10794 N  N     . ALA D 4 22  ? 161.396 153.194 183.081 1.00 28.08  ? 22  ALA D N     1 
ATOM   10795 C  CA    . ALA D 4 22  ? 160.513 153.964 183.952 1.00 28.08  ? 22  ALA D CA    1 
ATOM   10796 C  C     . ALA D 4 22  ? 159.544 154.817 183.143 1.00 30.44  ? 22  ALA D C     1 
ATOM   10797 O  O     . ALA D 4 22  ? 158.371 154.950 183.509 1.00 33.73  ? 22  ALA D O     1 
ATOM   10798 C  CB    . ALA D 4 22  ? 161.338 154.835 184.899 1.00 27.05  ? 22  ALA D CB    1 
ATOM   10799 N  N     . LEU D 4 23  ? 160.018 155.413 182.046 1.00 29.21  ? 23  LEU D N     1 
ATOM   10800 C  CA    . LEU D 4 23  ? 159.141 156.221 181.204 1.00 27.27  ? 23  LEU D CA    1 
ATOM   10801 C  C     . LEU D 4 23  ? 158.051 155.371 180.562 1.00 26.97  ? 23  LEU D C     1 
ATOM   10802 O  O     . LEU D 4 23  ? 156.892 155.794 180.478 1.00 31.28  ? 23  LEU D O     1 
ATOM   10803 C  CB    . LEU D 4 23  ? 159.960 156.943 180.134 1.00 25.55  ? 23  LEU D CB    1 
ATOM   10804 C  CG    . LEU D 4 23  ? 159.249 158.046 179.346 1.00 28.03  ? 23  LEU D CG    1 
ATOM   10805 C  CD1   . LEU D 4 23  ? 160.162 159.248 179.165 1.00 24.94  ? 23  LEU D CD1   1 
ATOM   10806 C  CD2   . LEU D 4 23  ? 158.772 157.529 177.996 1.00 27.39  ? 23  LEU D CD2   1 
ATOM   10807 N  N     . ILE D 4 24  ? 158.406 154.173 180.096 1.00 30.01  ? 24  ILE D N     1 
ATOM   10808 C  CA    . ILE D 4 24  ? 157.423 153.294 179.469 1.00 29.51  ? 24  ILE D CA    1 
ATOM   10809 C  C     . ILE D 4 24  ? 156.395 152.824 180.492 1.00 28.26  ? 24  ILE D C     1 
ATOM   10810 O  O     . ILE D 4 24  ? 155.205 152.690 180.183 1.00 39.10  ? 24  ILE D O     1 
ATOM   10811 C  CB    . ILE D 4 24  ? 158.135 152.112 178.783 1.00 32.77  ? 24  ILE D CB    1 
ATOM   10812 C  CG1   . ILE D 4 24  ? 158.863 152.589 177.525 1.00 30.05  ? 24  ILE D CG1   1 
ATOM   10813 C  CG2   . ILE D 4 24  ? 157.150 151.005 178.436 1.00 30.53  ? 24  ILE D CG2   1 
ATOM   10814 C  CD1   . ILE D 4 24  ? 159.929 151.633 177.036 1.00 32.56  ? 24  ILE D CD1   1 
ATOM   10815 N  N     . ASN D 4 25  ? 156.830 152.593 181.730 1.00 31.08  ? 25  ASN D N     1 
ATOM   10816 C  CA    . ASN D 4 25  ? 155.947 152.090 182.775 1.00 30.51  ? 25  ASN D CA    1 
ATOM   10817 C  C     . ASN D 4 25  ? 155.758 153.130 183.872 1.00 34.68  ? 25  ASN D C     1 
ATOM   10818 O  O     . ASN D 4 25  ? 155.841 152.808 185.062 1.00 42.04  ? 25  ASN D O     1 
ATOM   10819 C  CB    . ASN D 4 25  ? 156.502 150.790 183.363 1.00 31.59  ? 25  ASN D CB    1 
ATOM   10820 C  CG    . ASN D 4 25  ? 156.686 149.709 182.316 1.00 34.81  ? 25  ASN D CG    1 
ATOM   10821 O  OD1   . ASN D 4 25  ? 157.647 149.730 181.547 1.00 37.55  ? 25  ASN D OD1   1 
ATOM   10822 N  ND2   . ASN D 4 25  ? 155.761 148.758 182.280 1.00 40.60  ? 25  ASN D ND2   1 
ATOM   10823 N  N     . ALA D 4 26  ? 155.510 154.382 183.478 1.00 33.13  ? 26  ALA D N     1 
ATOM   10824 C  CA    . ALA D 4 26  ? 155.378 155.467 184.445 1.00 36.80  ? 26  ALA D CA    1 
ATOM   10825 C  C     . ALA D 4 26  ? 154.201 155.272 185.392 1.00 36.24  ? 26  ALA D C     1 
ATOM   10826 O  O     . ALA D 4 26  ? 154.174 155.893 186.461 1.00 39.30  ? 26  ALA D O     1 
ATOM   10827 C  CB    . ALA D 4 26  ? 155.241 156.804 183.717 1.00 32.64  ? 26  ALA D CB    1 
ATOM   10828 N  N     . GLU D 4 27  ? 153.227 154.435 185.026 1.00 42.45  ? 27  GLU D N     1 
ATOM   10829 C  CA    . GLU D 4 27  ? 152.118 154.157 185.932 1.00 44.02  ? 27  GLU D CA    1 
ATOM   10830 C  C     . GLU D 4 27  ? 152.604 153.473 187.204 1.00 46.94  ? 27  GLU D C     1 
ATOM   10831 O  O     . GLU D 4 27  ? 152.145 153.795 188.306 1.00 50.04  ? 27  GLU D O     1 
ATOM   10832 C  CB    . GLU D 4 27  ? 151.067 153.299 185.227 1.00 40.63  ? 27  GLU D CB    1 
ATOM   10833 C  CG    . GLU D 4 27  ? 150.153 154.080 184.296 1.00 44.33  ? 27  GLU D CG    1 
ATOM   10834 C  CD    . GLU D 4 27  ? 150.676 154.134 182.874 1.00 48.72  ? 27  GLU D CD    1 
ATOM   10835 O  OE1   . GLU D 4 27  ? 151.770 153.587 182.620 1.00 47.74  ? 27  GLU D OE1   1 
ATOM   10836 O  OE2   . GLU D 4 27  ? 149.993 154.724 182.011 1.00 47.37  ? 27  GLU D OE2   1 
ATOM   10837 N  N     . ALA D 4 28  ? 153.535 152.527 187.072 1.00 44.14  ? 28  ALA D N     1 
ATOM   10838 C  CA    . ALA D 4 28  ? 154.092 151.846 188.233 1.00 42.01  ? 28  ALA D CA    1 
ATOM   10839 C  C     . ALA D 4 28  ? 155.098 152.701 188.992 1.00 43.65  ? 28  ALA D C     1 
ATOM   10840 O  O     . ALA D 4 28  ? 155.361 152.425 190.168 1.00 49.69  ? 28  ALA D O     1 
ATOM   10841 C  CB    . ALA D 4 28  ? 154.753 150.533 187.809 1.00 39.91  ? 28  ALA D CB    1 
ATOM   10842 N  N     . PHE D 4 29  ? 155.662 153.722 188.356 1.00 42.74  ? 29  PHE D N     1 
ATOM   10843 C  CA    . PHE D 4 29  ? 156.638 154.586 189.008 1.00 41.37  ? 29  PHE D CA    1 
ATOM   10844 C  C     . PHE D 4 29  ? 155.996 155.891 189.465 1.00 46.51  ? 29  PHE D C     1 
ATOM   10845 O  O     . PHE D 4 29  ? 155.557 156.011 190.609 1.00 53.93  ? 29  PHE D O     1 
ATOM   10846 C  CB    . PHE D 4 29  ? 157.811 154.877 188.069 1.00 40.33  ? 29  PHE D CB    1 
ATOM   10847 C  CG    . PHE D 4 29  ? 158.775 153.734 187.931 1.00 42.71  ? 29  PHE D CG    1 
ATOM   10848 C  CD1   . PHE D 4 29  ? 158.514 152.692 187.056 1.00 39.92  ? 29  PHE D CD1   1 
ATOM   10849 C  CD2   . PHE D 4 29  ? 159.942 153.700 188.676 1.00 39.27  ? 29  PHE D CD2   1 
ATOM   10850 C  CE1   . PHE D 4 29  ? 159.399 151.639 186.927 1.00 40.89  ? 29  PHE D CE1   1 
ATOM   10851 C  CE2   . PHE D 4 29  ? 160.830 152.650 188.551 1.00 40.10  ? 29  PHE D CE2   1 
ATOM   10852 C  CZ    . PHE D 4 29  ? 160.559 151.618 187.676 1.00 42.31  ? 29  PHE D CZ    1 
HETATM 10853 K  K     . K   E 5 .   ? 167.525 167.632 153.787 1.00 17.86  ? 601 K   A K     1 
HETATM 10854 N  N     . 9Y0 F 6 .   ? 147.507 184.131 174.796 1.00 50.48  ? 602 9Y0 A N     1 
HETATM 10855 C  C     . 9Y0 F 6 .   ? 151.229 190.893 175.510 1.00 50.65  ? 602 9Y0 A C     1 
HETATM 10856 O  O     . 9Y0 F 6 .   ? 146.588 189.134 175.305 1.00 50.72  ? 602 9Y0 A O     1 
HETATM 10857 C  C1    . 9Y0 F 6 .   ? 151.051 189.449 175.930 1.00 48.91  ? 602 9Y0 A C1    1 
HETATM 10858 C  C10   . 9Y0 F 6 .   ? 153.156 190.927 181.104 1.00 50.74  ? 602 9Y0 A C10   1 
HETATM 10859 C  C11   . 9Y0 F 6 .   ? 154.309 190.085 181.635 1.00 48.50  ? 602 9Y0 A C11   1 
HETATM 10860 C  C12   . 9Y0 F 6 .   ? 154.335 188.672 181.047 1.00 47.86  ? 602 9Y0 A C12   1 
HETATM 10861 C  C13   . 9Y0 F 6 .   ? 155.737 188.195 180.829 1.00 49.80  ? 602 9Y0 A C13   1 
HETATM 10862 C  C14   . 9Y0 F 6 .   ? 156.276 187.039 181.215 1.00 48.06  ? 602 9Y0 A C14   1 
HETATM 10863 C  C15   . 9Y0 F 6 .   ? 157.683 186.583 180.985 1.00 47.44  ? 602 9Y0 A C15   1 
HETATM 10864 C  C16   . 9Y0 F 6 .   ? 158.072 185.386 181.849 1.00 44.35  ? 602 9Y0 A C16   1 
HETATM 10865 C  C17   . 9Y0 F 6 .   ? 159.470 184.874 181.531 1.00 48.44  ? 602 9Y0 A C17   1 
HETATM 10866 C  C18   . 9Y0 F 6 .   ? 159.649 183.391 181.820 1.00 46.93  ? 602 9Y0 A C18   1 
HETATM 10867 C  C19   . 9Y0 F 6 .   ? 160.964 182.836 181.286 1.00 48.94  ? 602 9Y0 A C19   1 
HETATM 10868 C  C2    . 9Y0 F 6 .   ? 149.773 189.163 176.700 1.00 44.98  ? 602 9Y0 A C2    1 
HETATM 10869 C  C20   . 9Y0 F 6 .   ? 161.023 181.315 181.289 1.00 50.46  ? 602 9Y0 A C20   1 
HETATM 10870 C  C21   . 9Y0 F 6 .   ? 153.301 188.646 176.104 1.00 49.09  ? 602 9Y0 A C21   1 
HETATM 10871 C  C22   . 9Y0 F 6 .   ? 154.289 188.113 177.104 1.00 47.47  ? 602 9Y0 A C22   1 
HETATM 10872 C  C23   . 9Y0 F 6 .   ? 155.045 186.885 176.624 1.00 46.38  ? 602 9Y0 A C23   1 
HETATM 10873 C  C24   . 9Y0 F 6 .   ? 155.701 186.141 177.781 1.00 48.83  ? 602 9Y0 A C24   1 
HETATM 10874 C  C25   . 9Y0 F 6 .   ? 156.402 184.860 177.344 1.00 48.14  ? 602 9Y0 A C25   1 
HETATM 10875 C  C26   . 9Y0 F 6 .   ? 156.813 183.980 178.517 1.00 46.11  ? 602 9Y0 A C26   1 
HETATM 10876 C  C27   . 9Y0 F 6 .   ? 157.499 182.689 178.092 1.00 43.35  ? 602 9Y0 A C27   1 
HETATM 10877 C  C28   . 9Y0 F 6 .   ? 157.639 181.688 179.230 1.00 47.12  ? 602 9Y0 A C28   1 
HETATM 10878 C  C29   . 9Y0 F 6 .   ? 158.363 180.410 178.827 1.00 46.09  ? 602 9Y0 A C29   1 
HETATM 10879 C  C3    . 9Y0 F 6 .   ? 146.306 186.263 175.085 1.00 51.88  ? 602 9Y0 A C3    1 
HETATM 10880 C  C30   . 9Y0 F 6 .   ? 158.226 179.293 179.852 1.00 47.54  ? 602 9Y0 A C30   1 
HETATM 10881 C  C31   . 9Y0 F 6 .   ? 158.985 178.031 179.464 1.00 46.97  ? 602 9Y0 A C31   1 
HETATM 10882 C  C32   . 9Y0 F 6 .   ? 158.520 176.787 180.210 1.00 48.38  ? 602 9Y0 A C32   1 
HETATM 10883 C  C33   . 9Y0 F 6 .   ? 159.294 175.540 179.804 1.00 43.54  ? 602 9Y0 A C33   1 
HETATM 10884 C  C34   . 9Y0 F 6 .   ? 158.605 174.232 180.168 1.00 45.64  ? 602 9Y0 A C34   1 
HETATM 10885 C  C35   . 9Y0 F 6 .   ? 159.265 173.019 179.522 1.00 49.27  ? 602 9Y0 A C35   1 
HETATM 10886 C  C36   . 9Y0 F 6 .   ? 158.561 171.709 179.845 1.00 46.25  ? 602 9Y0 A C36   1 
HETATM 10887 C  C37   . 9Y0 F 6 .   ? 162.380 180.763 180.868 1.00 51.16  ? 602 9Y0 A C37   1 
HETATM 10888 C  C38   . 9Y0 F 6 .   ? 162.865 181.329 179.541 1.00 47.09  ? 602 9Y0 A C38   1 
HETATM 10889 C  C4    . 9Y0 F 6 .   ? 147.295 185.466 174.262 1.00 50.78  ? 602 9Y0 A C4    1 
HETATM 10890 C  C5    . 9Y0 F 6 .   ? 151.675 192.978 176.530 1.00 54.37  ? 602 9Y0 A C5    1 
HETATM 10891 C  C6    . 9Y0 F 6 .   ? 151.846 193.616 177.879 1.00 50.04  ? 602 9Y0 A C6    1 
HETATM 10892 C  C7    . 9Y0 F 6 .   ? 152.774 192.850 178.808 1.00 51.68  ? 602 9Y0 A C7    1 
HETATM 10893 C  C8    . 9Y0 F 6 .   ? 152.561 193.246 180.264 1.00 49.04  ? 602 9Y0 A C8    1 
HETATM 10894 C  C9    . 9Y0 F 6 .   ? 153.402 192.425 181.231 1.00 49.96  ? 602 9Y0 A C9    1 
HETATM 10895 O  O1    . 9Y0 F 6 .   ? 146.945 186.771 176.240 1.00 53.90  ? 602 9Y0 A O1    1 
HETATM 10896 O  O2    . 9Y0 F 6 .   ? 147.100 188.712 177.822 1.00 57.43  ? 602 9Y0 A O2    1 
HETATM 10897 O  O3    . 9Y0 F 6 .   ? 148.893 188.308 176.014 1.00 53.34  ? 602 9Y0 A O3    1 
HETATM 10898 O  O4    . 9Y0 F 6 .   ? 151.590 193.568 175.480 1.00 54.50  ? 602 9Y0 A O4    1 
HETATM 10899 O  O5    . 9Y0 F 6 .   ? 151.627 191.658 176.638 1.00 56.08  ? 602 9Y0 A O5    1 
HETATM 10900 O  O6    . 9Y0 F 6 .   ? 153.476 188.674 174.912 1.00 53.55  ? 602 9Y0 A O6    1 
HETATM 10901 O  O7    . 9Y0 F 6 .   ? 152.199 189.086 176.707 1.00 50.56  ? 602 9Y0 A O7    1 
HETATM 10902 P  P     . 9Y0 F 6 .   ? 147.287 188.357 176.381 1.00 73.92  ? 602 9Y0 A P     1 
HETATM 10903 C  C     . 9Y0 G 6 .   ? 188.202 158.222 184.825 1.00 42.16  ? 701 9Y0 B C     1 
HETATM 10904 O  O     . 9Y0 G 6 .   ? 191.779 160.645 186.393 1.00 47.20  ? 701 9Y0 B O     1 
HETATM 10905 C  C1    . 9Y0 G 6 .   ? 188.104 158.386 186.327 1.00 43.90  ? 701 9Y0 B C1    1 
HETATM 10906 C  C10   . 9Y0 G 6 .   ? 182.873 158.283 179.524 1.00 45.43  ? 701 9Y0 B C10   1 
HETATM 10907 C  C11   . 9Y0 G 6 .   ? 181.394 158.592 179.329 1.00 41.06  ? 701 9Y0 B C11   1 
HETATM 10908 C  C12   . 9Y0 G 6 .   ? 180.653 157.509 178.541 1.00 41.45  ? 701 9Y0 B C12   1 
HETATM 10909 C  C13   . 9Y0 G 6 .   ? 179.215 157.860 178.308 1.00 43.67  ? 701 9Y0 B C13   1 
HETATM 10910 C  C14   . 9Y0 G 6 .   ? 178.619 158.100 177.140 1.00 41.39  ? 701 9Y0 B C14   1 
HETATM 10911 C  C15   . 9Y0 G 6 .   ? 179.236 158.084 175.776 1.00 42.94  ? 701 9Y0 B C15   1 
HETATM 10912 C  C16   . 9Y0 G 6 .   ? 178.775 156.897 174.931 1.00 45.04  ? 701 9Y0 B C16   1 
HETATM 10913 C  C17   . 9Y0 G 6 .   ? 179.407 156.883 173.545 1.00 41.74  ? 701 9Y0 B C17   1 
HETATM 10914 C  C18   . 9Y0 G 6 .   ? 179.602 155.481 172.980 1.00 43.18  ? 701 9Y0 B C18   1 
HETATM 10915 C  C19   . 9Y0 G 6 .   ? 178.300 154.764 172.643 1.00 44.33  ? 701 9Y0 B C19   1 
HETATM 10916 C  C2    . 9Y0 G 6 .   ? 189.335 158.978 186.994 1.00 44.01  ? 701 9Y0 B C2    1 
HETATM 10917 C  C20   . 9Y0 G 6 .   ? 177.689 155.217 171.323 1.00 42.91  ? 701 9Y0 B C20   1 
HETATM 10918 C  C21   . 9Y0 G 6 .   ? 186.927 157.025 187.889 1.00 47.01  ? 701 9Y0 B C21   1 
HETATM 10919 C  C22   . 9Y0 G 6 .   ? 186.518 155.601 188.159 1.00 42.90  ? 701 9Y0 B C22   1 
HETATM 10920 C  C23   . 9Y0 G 6 .   ? 185.174 155.225 187.557 1.00 44.40  ? 701 9Y0 B C23   1 
HETATM 10921 C  C24   . 9Y0 G 6 .   ? 185.065 155.623 186.090 1.00 47.17  ? 701 9Y0 B C24   1 
HETATM 10922 C  C25   . 9Y0 G 6 .   ? 183.630 155.820 185.612 1.00 44.44  ? 701 9Y0 B C25   1 
HETATM 10923 C  C26   . 9Y0 G 6 .   ? 182.574 155.690 186.702 1.00 41.17  ? 701 9Y0 B C26   1 
HETATM 10924 C  C27   . 9Y0 G 6 .   ? 181.359 156.584 186.482 1.00 42.49  ? 701 9Y0 B C27   1 
HETATM 10925 C  C28   . 9Y0 G 6 .   ? 181.312 157.282 185.128 1.00 43.89  ? 701 9Y0 B C28   1 
HETATM 10926 C  C29   . 9Y0 G 6 .   ? 180.631 158.642 185.206 1.00 45.29  ? 701 9Y0 B C29   1 
HETATM 10927 C  C30   . 9Y0 G 6 .   ? 180.014 159.115 183.897 1.00 43.20  ? 701 9Y0 B C30   1 
HETATM 10928 C  C31   . 9Y0 G 6 .   ? 179.270 160.434 184.062 1.00 40.19  ? 701 9Y0 B C31   1 
HETATM 10929 C  C32   . 9Y0 G 6 .   ? 177.792 160.242 184.374 1.00 42.62  ? 701 9Y0 B C32   1 
HETATM 10930 C  C33   . 9Y0 G 6 .   ? 177.207 161.372 185.210 1.00 39.76  ? 701 9Y0 B C33   1 
HETATM 10931 C  C34   . 9Y0 G 6 .   ? 176.635 160.899 186.541 1.00 49.13  ? 701 9Y0 B C34   1 
HETATM 10932 C  C35   . 9Y0 G 6 .   ? 175.777 159.645 186.428 1.00 44.18  ? 701 9Y0 B C35   1 
HETATM 10933 C  C36   . 9Y0 G 6 .   ? 175.218 159.191 187.769 1.00 39.95  ? 701 9Y0 B C36   1 
HETATM 10934 C  C37   . 9Y0 G 6 .   ? 176.635 154.257 170.783 1.00 44.74  ? 701 9Y0 B C37   1 
HETATM 10935 C  C38   . 9Y0 G 6 .   ? 176.038 154.716 169.460 1.00 43.30  ? 701 9Y0 B C38   1 
HETATM 10936 C  C5    . 9Y0 G 6 .   ? 186.795 157.574 183.054 1.00 45.45  ? 701 9Y0 B C5    1 
HETATM 10937 C  C6    . 9Y0 G 6 .   ? 185.362 157.474 182.614 1.00 40.80  ? 701 9Y0 B C6    1 
HETATM 10938 C  C7    . 9Y0 G 6 .   ? 184.552 158.751 182.770 1.00 42.15  ? 701 9Y0 B C7    1 
HETATM 10939 C  C8    . 9Y0 G 6 .   ? 183.230 158.696 182.009 1.00 42.88  ? 701 9Y0 B C8    1 
HETATM 10940 C  C9    . 9Y0 G 6 .   ? 183.193 157.671 180.881 1.00 42.46  ? 701 9Y0 B C9    1 
HETATM 10941 O  O1    . 9Y0 G 6 .   ? 192.859 158.436 185.658 1.00 49.16  ? 701 9Y0 B O1    1 
HETATM 10942 O  O2    . 9Y0 G 6 .   ? 192.511 158.832 188.113 1.00 51.32  ? 701 9Y0 B O2    1 
HETATM 10943 O  O3    . 9Y0 G 6 .   ? 190.531 158.420 186.510 1.00 48.52  ? 701 9Y0 B O3    1 
HETATM 10944 O  O4    . 9Y0 G 6 .   ? 187.747 157.217 182.404 1.00 50.94  ? 701 9Y0 B O4    1 
HETATM 10945 O  O5    . 9Y0 G 6 .   ? 186.902 158.107 184.263 1.00 43.73  ? 701 9Y0 B O5    1 
HETATM 10946 O  O6    . 9Y0 G 6 .   ? 186.529 157.984 188.501 1.00 50.12  ? 701 9Y0 B O6    1 
HETATM 10947 O  O7    . 9Y0 G 6 .   ? 187.790 157.101 186.880 1.00 48.30  ? 701 9Y0 B O7    1 
HETATM 10948 P  P     . 9Y0 G 6 .   ? 191.956 159.205 186.774 1.00 68.40  ? 701 9Y0 B P     1 
HETATM 10949 P  PB    . ADP H 7 .   ? 112.007 167.724 196.521 1.00 84.15  ? 702 ADP B PB    1 
HETATM 10950 O  O1B   . ADP H 7 .   ? 113.298 167.013 196.197 1.00 80.91  ? 702 ADP B O1B   1 
HETATM 10951 O  O2B   . ADP H 7 .   ? 111.335 167.264 197.793 1.00 80.98  ? 702 ADP B O2B   1 
HETATM 10952 O  O3B   . ADP H 7 .   ? 112.058 169.224 196.359 1.00 80.59  ? 702 ADP B O3B   1 
HETATM 10953 P  PA    . ADP H 7 .   ? 110.549 165.720 195.185 1.00 87.51  ? 702 ADP B PA    1 
HETATM 10954 O  O1A   . ADP H 7 .   ? 110.802 165.295 193.758 1.00 81.91  ? 702 ADP B O1A   1 
HETATM 10955 O  O2A   . ADP H 7 .   ? 111.078 164.884 196.326 1.00 80.81  ? 702 ADP B O2A   1 
HETATM 10956 O  O3A   . ADP H 7 .   ? 110.996 167.256 195.362 1.00 80.90  ? 702 ADP B O3A   1 
HETATM 10957 O  "O5'" . ADP H 7 .   ? 108.964 165.878 195.398 1.00 82.14  ? 702 ADP B "O5'" 1 
HETATM 10958 C  "C5'" . ADP H 7 .   ? 108.038 165.676 194.336 1.00 79.99  ? 702 ADP B "C5'" 1 
HETATM 10959 C  "C4'" . ADP H 7 .   ? 106.730 166.328 194.757 1.00 80.44  ? 702 ADP B "C4'" 1 
HETATM 10960 O  "O4'" . ADP H 7 .   ? 106.045 165.478 195.676 1.00 83.13  ? 702 ADP B "O4'" 1 
HETATM 10961 C  "C3'" . ADP H 7 .   ? 106.981 167.652 195.465 1.00 79.54  ? 702 ADP B "C3'" 1 
HETATM 10962 O  "O3'" . ADP H 7 .   ? 106.494 168.739 194.673 1.00 82.25  ? 702 ADP B "O3'" 1 
HETATM 10963 C  "C2'" . ADP H 7 .   ? 106.221 167.581 196.775 1.00 79.56  ? 702 ADP B "C2'" 1 
HETATM 10964 O  "O2'" . ADP H 7 .   ? 105.275 168.651 196.855 1.00 79.66  ? 702 ADP B "O2'" 1 
HETATM 10965 C  "C1'" . ADP H 7 .   ? 105.506 166.239 196.758 1.00 81.84  ? 702 ADP B "C1'" 1 
HETATM 10966 N  N9    . ADP H 7 .   ? 105.726 165.519 198.036 1.00 81.82  ? 702 ADP B N9    1 
HETATM 10967 C  C8    . ADP H 7 .   ? 106.856 165.533 198.768 1.00 80.23  ? 702 ADP B C8    1 
HETATM 10968 N  N7    . ADP H 7 .   ? 106.725 164.773 199.885 1.00 81.49  ? 702 ADP B N7    1 
HETATM 10969 C  C5    . ADP H 7 .   ? 105.482 164.257 199.878 1.00 80.73  ? 702 ADP B C5    1 
HETATM 10970 C  C6    . ADP H 7 .   ? 104.688 163.368 200.759 1.00 81.15  ? 702 ADP B C6    1 
HETATM 10971 N  N6    . ADP H 7 .   ? 105.211 162.865 201.902 1.00 81.35  ? 702 ADP B N6    1 
HETATM 10972 N  N1    . ADP H 7 .   ? 103.423 163.077 200.383 1.00 81.12  ? 702 ADP B N1    1 
HETATM 10973 C  C2    . ADP H 7 .   ? 102.890 163.570 199.250 1.00 80.81  ? 702 ADP B C2    1 
HETATM 10974 N  N3    . ADP H 7 .   ? 103.551 164.381 198.405 1.00 80.64  ? 702 ADP B N3    1 
HETATM 10975 C  C4    . ADP H 7 .   ? 104.826 164.757 198.660 1.00 81.00  ? 702 ADP B C4    1 
HETATM 10976 MG MG    . MG  I 8 .   ? 114.732 167.734 194.944 1.00 68.90  ? 703 MG  B MG    1 
HETATM 10977 K  K     . K   J 5 .   ? 168.330 170.535 189.739 1.00 40.71  ? 704 K   B K     1 
HETATM 10978 MG MG    . MG  K 8 .   ? 111.862 164.719 198.365 1.00 70.71  ? 705 MG  B MG    1 
HETATM 10979 O  O     . HOH L 9 .   ? 164.652 163.853 162.749 1.00 19.70  ? 701 HOH A O     1 
HETATM 10980 O  O     . HOH L 9 .   ? 179.490 165.826 153.454 1.00 36.46  ? 702 HOH A O     1 
HETATM 10981 O  O     . HOH L 9 .   ? 177.725 182.325 148.891 1.00 10.61  ? 703 HOH A O     1 
HETATM 10982 O  O     . HOH L 9 .   ? 174.840 171.119 151.591 1.00 13.47  ? 704 HOH A O     1 
HETATM 10983 O  O     . HOH L 9 .   ? 169.260 167.647 168.205 1.00 31.86  ? 705 HOH A O     1 
HETATM 10984 O  O     . HOH L 9 .   ? 169.259 177.630 141.062 1.00 17.96  ? 706 HOH A O     1 
HETATM 10985 O  O     . HOH L 9 .   ? 163.492 164.015 168.330 1.00 24.35  ? 707 HOH A O     1 
HETATM 10986 O  O     . HOH L 9 .   ? 159.185 174.000 150.313 1.00 14.59  ? 708 HOH A O     1 
HETATM 10987 O  O     . HOH L 9 .   ? 176.612 169.063 146.941 1.00 17.51  ? 709 HOH A O     1 
HETATM 10988 O  O     . HOH L 9 .   ? 161.820 167.545 165.540 1.00 26.02  ? 710 HOH A O     1 
HETATM 10989 O  O     . HOH L 9 .   ? 163.680 166.522 169.532 1.00 37.90  ? 711 HOH A O     1 
HETATM 10990 O  O     . HOH L 9 .   ? 161.950 169.277 159.962 1.00 22.64  ? 712 HOH A O     1 
HETATM 10991 O  O     . HOH L 9 .   ? 164.611 167.125 155.484 1.00 7.12   ? 713 HOH A O     1 
HETATM 10992 O  O     . HOH L 9 .   ? 160.914 168.988 162.751 1.00 28.90  ? 714 HOH A O     1 
HETATM 10993 O  O     . HOH L 9 .   ? 182.019 180.914 154.447 1.00 20.96  ? 715 HOH A O     1 
HETATM 10994 O  O     . HOH L 9 .   ? 166.227 165.385 137.520 1.00 25.53  ? 716 HOH A O     1 
HETATM 10995 O  O     . HOH L 9 .   ? 160.639 165.808 155.326 1.00 24.77  ? 717 HOH A O     1 
HETATM 10996 O  O     . HOH L 9 .   ? 156.614 171.431 157.767 1.00 18.81  ? 718 HOH A O     1 
HETATM 10997 O  O     . HOH L 9 .   ? 160.384 168.282 167.685 1.00 35.52  ? 719 HOH A O     1 
HETATM 10998 O  O     . HOH L 9 .   ? 176.699 167.115 153.328 1.00 29.11  ? 720 HOH A O     1 
HETATM 10999 O  O     . HOH L 9 .   ? 174.839 164.472 143.428 1.00 9.94   ? 721 HOH A O     1 
HETATM 11000 O  O     . HOH L 9 .   ? 164.284 154.843 145.080 1.00 20.77  ? 722 HOH A O     1 
HETATM 11001 O  O     . HOH L 9 .   ? 160.890 162.531 160.828 1.00 21.66  ? 723 HOH A O     1 
HETATM 11002 O  O     . HOH L 9 .   ? 162.750 164.578 159.202 1.00 21.71  ? 724 HOH A O     1 
HETATM 11003 O  O     . HOH L 9 .   ? 144.447 163.837 149.730 1.00 24.18  ? 725 HOH A O     1 
HETATM 11004 O  O     . HOH L 9 .   ? 161.513 174.688 177.692 1.00 44.74  ? 726 HOH A O     1 
HETATM 11005 O  O     . HOH L 9 .   ? 161.416 159.965 154.222 1.00 15.27  ? 727 HOH A O     1 
HETATM 11006 O  O     . HOH L 9 .   ? 164.279 172.705 171.193 1.00 28.76  ? 728 HOH A O     1 
HETATM 11007 O  O     . HOH L 9 .   ? 173.551 168.378 151.484 1.00 17.77  ? 729 HOH A O     1 
HETATM 11008 O  O     . HOH L 9 .   ? 169.136 165.044 137.645 1.00 18.77  ? 730 HOH A O     1 
HETATM 11009 O  O     . HOH L 9 .   ? 165.046 174.840 163.375 1.00 12.08  ? 731 HOH A O     1 
HETATM 11010 O  O     . HOH L 9 .   ? 177.546 171.234 153.283 1.00 21.14  ? 732 HOH A O     1 
HETATM 11011 O  O     . HOH L 9 .   ? 175.582 169.201 175.487 1.00 15.49  ? 733 HOH A O     1 
HETATM 11012 O  O     . HOH L 9 .   ? 160.560 155.710 148.773 1.00 19.98  ? 734 HOH A O     1 
HETATM 11013 O  O     . HOH L 9 .   ? 171.095 168.414 152.332 1.00 3.68   ? 735 HOH A O     1 
HETATM 11014 O  O     . HOH L 9 .   ? 163.870 167.159 160.890 1.00 32.41  ? 736 HOH A O     1 
HETATM 11015 O  O     . HOH L 9 .   ? 161.018 158.019 150.614 1.00 23.55  ? 737 HOH A O     1 
HETATM 11016 O  O     . HOH L 9 .   ? 164.610 166.629 163.680 1.00 24.15  ? 738 HOH A O     1 
HETATM 11017 O  O     . HOH L 9 .   ? 174.840 178.653 153.247 1.00 15.26  ? 739 HOH A O     1 
HETATM 11018 O  O     . HOH L 9 .   ? 178.878 174.047 153.856 1.00 21.69  ? 740 HOH A O     1 
HETATM 11019 O  O     . HOH L 9 .   ? 163.413 166.470 157.969 1.00 28.63  ? 741 HOH A O     1 
HETATM 11020 O  O     . HOH L 9 .   ? 177.630 166.307 145.095 1.00 19.22  ? 742 HOH A O     1 
HETATM 11021 O  O     . HOH L 9 .   ? 183.210 163.680 152.876 1.00 25.64  ? 743 HOH A O     1 
HETATM 11022 O  O     . HOH L 9 .   ? 165.472 156.051 143.222 1.00 25.30  ? 744 HOH A O     1 
HETATM 11023 O  O     . HOH L 9 .   ? 165.790 168.330 169.434 1.00 38.70  ? 745 HOH A O     1 
HETATM 11024 O  O     . HOH L 9 .   ? 156.240 173.961 159.030 1.00 23.80  ? 746 HOH A O     1 
HETATM 11025 O  O     . HOH L 9 .   ? 166.726 170.488 178.266 1.00 40.99  ? 747 HOH A O     1 
HETATM 11026 O  O     . HOH L 9 .   ? 178.559 168.110 148.800 1.00 34.46  ? 748 HOH A O     1 
HETATM 11027 O  O     . HOH L 9 .   ? 163.265 165.540 165.545 1.00 29.29  ? 749 HOH A O     1 
HETATM 11028 O  O     . HOH L 9 .   ? 150.843 161.757 162.092 1.00 37.69  ? 750 HOH A O     1 
HETATM 11029 O  O     . HOH L 9 .   ? 181.584 166.470 154.462 1.00 32.95  ? 751 HOH A O     1 
HETATM 11030 O  O     . HOH L 9 .   ? 177.460 170.321 149.730 1.00 31.99  ? 752 HOH A O     1 
HETATM 11031 O  O     . HOH L 9 .   ? 162.599 168.330 168.455 1.00 30.97  ? 753 HOH A O     1 
HETATM 11032 O  O     . HOH L 9 .   ? 156.239 162.074 161.865 1.00 40.66  ? 754 HOH A O     1 
HETATM 11033 O  O     . HOH L 9 .   ? 161.820 164.610 161.863 1.00 33.83  ? 755 HOH A O     1 
HETATM 11034 O  O     . HOH L 9 .   ? 153.122 165.152 167.294 1.00 35.11  ? 756 HOH A O     1 
HETATM 11035 O  O     . HOH L 9 .   ? 166.316 169.419 172.051 1.00 38.49  ? 757 HOH A O     1 
HETATM 11036 O  O     . HOH L 9 .   ? 164.886 167.883 173.277 1.00 47.29  ? 758 HOH A O     1 
HETATM 11037 O  O     . HOH L 9 .   ? 149.730 169.328 162.762 1.00 42.71  ? 759 HOH A O     1 
HETATM 11038 O  O     . HOH M 9 .   ? 146.404 164.558 193.335 1.00 46.80  ? 801 HOH B O     1 
HETATM 11039 O  O     . HOH M 9 .   ? 165.790 174.135 191.376 1.00 34.78  ? 802 HOH B O     1 
HETATM 11040 O  O     . HOH M 9 .   ? 158.152 164.990 198.090 1.00 32.86  ? 803 HOH B O     1 
HETATM 11041 O  O     . HOH M 9 .   ? 168.127 173.909 191.654 1.00 28.82  ? 804 HOH B O     1 
HETATM 11042 O  O     . HOH M 9 .   ? 172.245 169.192 195.470 1.00 23.26  ? 805 HOH B O     1 
HETATM 11043 O  O     . HOH M 9 .   ? 166.544 170.932 193.582 1.00 23.05  ? 806 HOH B O     1 
HETATM 11044 O  O     . HOH M 9 .   ? 160.136 161.820 189.829 1.00 38.41  ? 807 HOH B O     1 
HETATM 11045 O  O     . HOH M 9 .   ? 151.795 164.983 193.405 1.00 31.41  ? 808 HOH B O     1 
HETATM 11046 O  O     . HOH M 9 .   ? 158.752 163.488 195.298 1.00 22.15  ? 809 HOH B O     1 
HETATM 11047 O  O     . HOH M 9 .   ? 168.330 173.576 188.789 1.00 32.50  ? 810 HOH B O     1 
HETATM 11048 O  O     . HOH M 9 .   ? 149.990 170.687 198.036 1.00 30.42  ? 811 HOH B O     1 
HETATM 11049 O  O     . HOH M 9 .   ? 168.379 180.419 186.131 1.00 26.57  ? 812 HOH B O     1 
HETATM 11050 O  O     . HOH M 9 .   ? 159.034 154.380 197.160 1.00 50.70  ? 813 HOH B O     1 
HETATM 11051 O  O     . HOH M 9 .   ? 148.800 171.951 196.229 1.00 34.81  ? 814 HOH B O     1 
HETATM 11052 O  O     . HOH M 9 .   ? 165.926 171.270 186.658 1.00 31.83  ? 815 HOH B O     1 
HETATM 11053 O  O     . HOH M 9 .   ? 177.397 167.179 175.910 1.00 27.11  ? 816 HOH B O     1 
HETATM 11054 O  O     . HOH M 9 .   ? 165.540 171.537 189.918 1.00 19.88  ? 817 HOH B O     1 
HETATM 11055 O  O     . HOH M 9 .   ? 174.911 168.543 180.522 1.00 43.46  ? 818 HOH B O     1 
HETATM 11056 O  O     . HOH M 9 .   ? 150.002 166.803 204.599 1.00 42.42  ? 819 HOH B O     1 
HETATM 11057 O  O     . HOH M 9 .   ? 160.371 162.750 197.529 1.00 36.26  ? 820 HOH B O     1 
HETATM 11058 O  O     . HOH M 9 .   ? 160.890 178.184 182.384 1.00 44.25  ? 821 HOH B O     1 
HETATM 11059 O  O     . HOH M 9 .   ? 157.034 164.948 178.099 1.00 39.99  ? 822 HOH B O     1 
HETATM 11060 O  O     . HOH M 9 .   ? 163.532 166.435 176.700 1.00 39.93  ? 823 HOH B O     1 
HETATM 11061 O  O     . HOH M 9 .   ? 181.287 169.260 183.842 1.00 45.40  ? 824 HOH B O     1 
HETATM 11062 O  O     . HOH M 9 .   ? 160.929 166.451 176.953 1.00 40.83  ? 825 HOH B O     1 
HETATM 11063 O  O     . HOH M 9 .   ? 161.633 168.629 176.997 1.00 43.85  ? 826 HOH B O     1 
HETATM 11064 O  O     . HOH N 9 .   ? 164.317 162.804 137.617 1.00 26.27  ? 301 HOH C O     1 
HETATM 11065 O  O     . HOH N 9 .   ? 187.323 177.636 146.893 1.00 21.14  ? 302 HOH C O     1 
HETATM 11066 O  O     . HOH N 9 .   ? 174.642 177.684 131.584 1.00 18.78  ? 303 HOH C O     1 
HETATM 11067 O  O     . HOH N 9 .   ? 186.931 178.618 150.611 1.00 23.09  ? 304 HOH C O     1 
HETATM 11068 O  O     . HOH N 9 .   ? 181.598 173.911 154.822 1.00 15.11  ? 305 HOH C O     1 
# 
