data_9G95
# 
_entry.id   9G95 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   9G95         pdb_00009g95 10.2210/pdb9g95/pdb 
WWPDB D_1292140504 ?            ?                   
# 
_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       2025-01-22 
# 
_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                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9G95 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-24 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              james.naismith@mpls.ox.ac.uk 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_last          Naismith 
_pdbx_contact_author.name_mi            H. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6744-5061 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Le Bas, A.'     1 0000-0002-1100-6833 
'El Omari, K.'   2 0000-0003-3506-6045 
'Lee, M.'        3 0000-0001-8447-0314 
'Naismith, J.H.' 4 0000-0001-6744-5061 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Open Biology' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2046-2441 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                240310 
_citation.page_last                 240310 
_citation.title                     'Structure of WzxE the lipid III flippase for Enterobacterial Common Antigen polysaccharide.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1098/rsob.240310 
_citation.pdbx_database_id_PubMed   39772807 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Le Bas, A.'       1  0000-0002-1100-6833 
primary 'Clarke, B.R.'     2  ?                   
primary 'Teelucksingh, T.' 3  ?                   
primary 'Lee, M.'          4  ?                   
primary 'El Omari, K.'     5  ?                   
primary 'Giltrap, A.M.'    6  ?                   
primary 'McMahon, S.A.'    7  ?                   
primary 'Liu, H.'          8  ?                   
primary 'Beale, J.H.'      9  0000-0003-1171-2428 
primary 'Mykhaylyk, V.'    10 ?                   
primary 'Duman, R.'        11 ?                   
primary 'Paterson, N.G.'   12 ?                   
primary 'Ward, P.N.'       13 0000-0003-2546-3426 
primary 'Harrison, P.J.'   14 0000-0001-5167-0547 
primary 'Weckener, M.'     15 ?                   
primary 'Pardon, E.'       16 ?                   
primary 'Steyaert, J.'     17 ?                   
primary 'Liu, H.'          18 ?                   
primary 'Quigley, A.'      19 0000-0002-5022-9845 
primary 'Davis, B.G.'      20 ?                   
primary 'Wagner, A.'       21 ?                   
primary 'Whitfield, C.'    22 ?                   
primary 'Naismith, J.H.'   23 0000-0001-6744-5061 
# 
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 'Lipid III flippase'                                    46130.621 1 ? ? ? ? 
2 polymer     man 'NB10 Nanobody'                                         15132.753 1 ? ? ? ? 
3 non-polymer syn '[(Z)-octadec-9-enyl] (2R)-2,3-bis(oxidanyl)propanoate' 356.540   5 ? ? ? ? 
4 non-polymer syn N-OCTANE                                                114.229   5 ? ? ? ? 
5 non-polymer syn 'SULFATE ION'                                           96.063    2 ? ? ? ? 
6 non-polymer syn 'ZINC ION'                                              65.409    1 ? ? ? ? 
7 non-polymer syn 'CHLORIDE ION'                                          35.453    2 ? ? ? ? 
# 
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 
;MVSLAKASLWTAASTLVKIGAGLLVGKLLAVSFGPAGLGLAANFRQLITVLGVLAGAGIFNGVTKYVAQYHDNPQQLRRV
VGTSSAMVLGFSTLMALVFVLAAAPISQGLFGNTDYQGLVRLVALVQMGIAWGNLLLALMKGFRDAAGNALSLIVGSLIG
VLAYYVSYRLGGYEGALLGLALIPALVVIPAAIMLIKRGVIPLSYLKPSWDNGLAGQLSKFTLMALITSVTLPVAYIMMR
KLLAAQYSWDEVGIWQGVSSISDAYLQFITASFSVYLLPTLSRLTEKRDITREVVKSLKFVLPAVAAASFTVWLLRDFAI
WLLLSNKFTAMRDLFAWQLVGDVLKVGAYVFGYLVIAKASLRFYILAEVSQFTLLMVFAHWLIPAHGALGAAQAYMATYI
VYFSLCCGVFLLWRRRALEENLYFQ
;
;MVSLAKASLWTAASTLVKIGAGLLVGKLLAVSFGPAGLGLAANFRQLITVLGVLAGAGIFNGVTKYVAQYHDNPQQLRRV
VGTSSAMVLGFSTLMALVFVLAAAPISQGLFGNTDYQGLVRLVALVQMGIAWGNLLLALMKGFRDAAGNALSLIVGSLIG
VLAYYVSYRLGGYEGALLGLALIPALVVIPAAIMLIKRGVIPLSYLKPSWDNGLAGQLSKFTLMALITSVTLPVAYIMMR
KLLAAQYSWDEVGIWQGVSSISDAYLQFITASFSVYLLPTLSRLTEKRDITREVVKSLKFVLPAVAAASFTVWLLRDFAI
WLLLSNKFTAMRDLFAWQLVGDVLKVGAYVFGYLVIAKASLRFYILAEVSQFTLLMVFAHWLIPAHGALGAAQAYMATYI
VYFSLCCGVFLLWRRRALEENLYFQ
;
A ? 
2 'polypeptide(L)' no no 
;MAQVQLVESGGGLVQAGGSLGLSCAASGRTFSNYVMAWFRQAPGKEREFVARISESRGTTDYADSVKGRFTISRDNAKNT
IYLQMNSLNPGDTAVYSCAATLPAWTGIIGGRRPGNYPYWGQGTQVTVSSHHHHHHEPEA
;
;MAQVQLVESGGGLVQAGGSLGLSCAASGRTFSNYVMAWFRQAPGKEREFVARISESRGTTDYADSVKGRFTISRDNAKNT
IYLQMNSLNPGDTAVYSCAATLPAWTGIIGGRRPGNYPYWGQGTQVTVSSHHHHHHEPEA
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 '[(Z)-octadec-9-enyl] (2R)-2,3-bis(oxidanyl)propanoate' MPG 
4 N-OCTANE                                                OCT 
5 'SULFATE ION'                                           SO4 
6 'ZINC ION'                                              ZN  
7 'CHLORIDE ION'                                          CL  
# 
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   VAL n 
1 3   SER n 
1 4   LEU n 
1 5   ALA n 
1 6   LYS n 
1 7   ALA n 
1 8   SER n 
1 9   LEU n 
1 10  TRP n 
1 11  THR n 
1 12  ALA n 
1 13  ALA n 
1 14  SER n 
1 15  THR n 
1 16  LEU n 
1 17  VAL n 
1 18  LYS n 
1 19  ILE n 
1 20  GLY n 
1 21  ALA n 
1 22  GLY n 
1 23  LEU n 
1 24  LEU n 
1 25  VAL n 
1 26  GLY n 
1 27  LYS n 
1 28  LEU n 
1 29  LEU n 
1 30  ALA n 
1 31  VAL n 
1 32  SER n 
1 33  PHE n 
1 34  GLY n 
1 35  PRO n 
1 36  ALA n 
1 37  GLY n 
1 38  LEU n 
1 39  GLY n 
1 40  LEU n 
1 41  ALA n 
1 42  ALA n 
1 43  ASN n 
1 44  PHE n 
1 45  ARG n 
1 46  GLN n 
1 47  LEU n 
1 48  ILE n 
1 49  THR n 
1 50  VAL n 
1 51  LEU n 
1 52  GLY n 
1 53  VAL n 
1 54  LEU n 
1 55  ALA n 
1 56  GLY n 
1 57  ALA n 
1 58  GLY n 
1 59  ILE n 
1 60  PHE n 
1 61  ASN n 
1 62  GLY n 
1 63  VAL n 
1 64  THR n 
1 65  LYS n 
1 66  TYR n 
1 67  VAL n 
1 68  ALA n 
1 69  GLN n 
1 70  TYR n 
1 71  HIS n 
1 72  ASP n 
1 73  ASN n 
1 74  PRO n 
1 75  GLN n 
1 76  GLN n 
1 77  LEU n 
1 78  ARG n 
1 79  ARG n 
1 80  VAL n 
1 81  VAL n 
1 82  GLY n 
1 83  THR n 
1 84  SER n 
1 85  SER n 
1 86  ALA n 
1 87  MET n 
1 88  VAL n 
1 89  LEU n 
1 90  GLY n 
1 91  PHE n 
1 92  SER n 
1 93  THR n 
1 94  LEU n 
1 95  MET n 
1 96  ALA n 
1 97  LEU n 
1 98  VAL n 
1 99  PHE n 
1 100 VAL n 
1 101 LEU n 
1 102 ALA n 
1 103 ALA n 
1 104 ALA n 
1 105 PRO n 
1 106 ILE n 
1 107 SER n 
1 108 GLN n 
1 109 GLY n 
1 110 LEU n 
1 111 PHE n 
1 112 GLY n 
1 113 ASN n 
1 114 THR n 
1 115 ASP n 
1 116 TYR n 
1 117 GLN n 
1 118 GLY n 
1 119 LEU n 
1 120 VAL n 
1 121 ARG n 
1 122 LEU n 
1 123 VAL n 
1 124 ALA n 
1 125 LEU n 
1 126 VAL n 
1 127 GLN n 
1 128 MET n 
1 129 GLY n 
1 130 ILE n 
1 131 ALA n 
1 132 TRP n 
1 133 GLY n 
1 134 ASN n 
1 135 LEU n 
1 136 LEU n 
1 137 LEU n 
1 138 ALA n 
1 139 LEU n 
1 140 MET n 
1 141 LYS n 
1 142 GLY n 
1 143 PHE n 
1 144 ARG n 
1 145 ASP n 
1 146 ALA n 
1 147 ALA n 
1 148 GLY n 
1 149 ASN n 
1 150 ALA n 
1 151 LEU n 
1 152 SER n 
1 153 LEU n 
1 154 ILE n 
1 155 VAL n 
1 156 GLY n 
1 157 SER n 
1 158 LEU n 
1 159 ILE n 
1 160 GLY n 
1 161 VAL n 
1 162 LEU n 
1 163 ALA n 
1 164 TYR n 
1 165 TYR n 
1 166 VAL n 
1 167 SER n 
1 168 TYR n 
1 169 ARG n 
1 170 LEU n 
1 171 GLY n 
1 172 GLY n 
1 173 TYR n 
1 174 GLU n 
1 175 GLY n 
1 176 ALA n 
1 177 LEU n 
1 178 LEU n 
1 179 GLY n 
1 180 LEU n 
1 181 ALA n 
1 182 LEU n 
1 183 ILE n 
1 184 PRO n 
1 185 ALA n 
1 186 LEU n 
1 187 VAL n 
1 188 VAL n 
1 189 ILE n 
1 190 PRO n 
1 191 ALA n 
1 192 ALA n 
1 193 ILE n 
1 194 MET n 
1 195 LEU n 
1 196 ILE n 
1 197 LYS n 
1 198 ARG n 
1 199 GLY n 
1 200 VAL n 
1 201 ILE n 
1 202 PRO n 
1 203 LEU n 
1 204 SER n 
1 205 TYR n 
1 206 LEU n 
1 207 LYS n 
1 208 PRO n 
1 209 SER n 
1 210 TRP n 
1 211 ASP n 
1 212 ASN n 
1 213 GLY n 
1 214 LEU n 
1 215 ALA n 
1 216 GLY n 
1 217 GLN n 
1 218 LEU n 
1 219 SER n 
1 220 LYS n 
1 221 PHE n 
1 222 THR n 
1 223 LEU n 
1 224 MET n 
1 225 ALA n 
1 226 LEU n 
1 227 ILE n 
1 228 THR n 
1 229 SER n 
1 230 VAL n 
1 231 THR n 
1 232 LEU n 
1 233 PRO n 
1 234 VAL n 
1 235 ALA n 
1 236 TYR n 
1 237 ILE n 
1 238 MET n 
1 239 MET n 
1 240 ARG n 
1 241 LYS n 
1 242 LEU n 
1 243 LEU n 
1 244 ALA n 
1 245 ALA n 
1 246 GLN n 
1 247 TYR n 
1 248 SER n 
1 249 TRP n 
1 250 ASP n 
1 251 GLU n 
1 252 VAL n 
1 253 GLY n 
1 254 ILE n 
1 255 TRP n 
1 256 GLN n 
1 257 GLY n 
1 258 VAL n 
1 259 SER n 
1 260 SER n 
1 261 ILE n 
1 262 SER n 
1 263 ASP n 
1 264 ALA n 
1 265 TYR n 
1 266 LEU n 
1 267 GLN n 
1 268 PHE n 
1 269 ILE n 
1 270 THR n 
1 271 ALA n 
1 272 SER n 
1 273 PHE n 
1 274 SER n 
1 275 VAL n 
1 276 TYR n 
1 277 LEU n 
1 278 LEU n 
1 279 PRO n 
1 280 THR n 
1 281 LEU n 
1 282 SER n 
1 283 ARG n 
1 284 LEU n 
1 285 THR n 
1 286 GLU n 
1 287 LYS n 
1 288 ARG n 
1 289 ASP n 
1 290 ILE n 
1 291 THR n 
1 292 ARG n 
1 293 GLU n 
1 294 VAL n 
1 295 VAL n 
1 296 LYS n 
1 297 SER n 
1 298 LEU n 
1 299 LYS n 
1 300 PHE n 
1 301 VAL n 
1 302 LEU n 
1 303 PRO n 
1 304 ALA n 
1 305 VAL n 
1 306 ALA n 
1 307 ALA n 
1 308 ALA n 
1 309 SER n 
1 310 PHE n 
1 311 THR n 
1 312 VAL n 
1 313 TRP n 
1 314 LEU n 
1 315 LEU n 
1 316 ARG n 
1 317 ASP n 
1 318 PHE n 
1 319 ALA n 
1 320 ILE n 
1 321 TRP n 
1 322 LEU n 
1 323 LEU n 
1 324 LEU n 
1 325 SER n 
1 326 ASN n 
1 327 LYS n 
1 328 PHE n 
1 329 THR n 
1 330 ALA n 
1 331 MET n 
1 332 ARG n 
1 333 ASP n 
1 334 LEU n 
1 335 PHE n 
1 336 ALA n 
1 337 TRP n 
1 338 GLN n 
1 339 LEU n 
1 340 VAL n 
1 341 GLY n 
1 342 ASP n 
1 343 VAL n 
1 344 LEU n 
1 345 LYS n 
1 346 VAL n 
1 347 GLY n 
1 348 ALA n 
1 349 TYR n 
1 350 VAL n 
1 351 PHE n 
1 352 GLY n 
1 353 TYR n 
1 354 LEU n 
1 355 VAL n 
1 356 ILE n 
1 357 ALA n 
1 358 LYS n 
1 359 ALA n 
1 360 SER n 
1 361 LEU n 
1 362 ARG n 
1 363 PHE n 
1 364 TYR n 
1 365 ILE n 
1 366 LEU n 
1 367 ALA n 
1 368 GLU n 
1 369 VAL n 
1 370 SER n 
1 371 GLN n 
1 372 PHE n 
1 373 THR n 
1 374 LEU n 
1 375 LEU n 
1 376 MET n 
1 377 VAL n 
1 378 PHE n 
1 379 ALA n 
1 380 HIS n 
1 381 TRP n 
1 382 LEU n 
1 383 ILE n 
1 384 PRO n 
1 385 ALA n 
1 386 HIS n 
1 387 GLY n 
1 388 ALA n 
1 389 LEU n 
1 390 GLY n 
1 391 ALA n 
1 392 ALA n 
1 393 GLN n 
1 394 ALA n 
1 395 TYR n 
1 396 MET n 
1 397 ALA n 
1 398 THR n 
1 399 TYR n 
1 400 ILE n 
1 401 VAL n 
1 402 TYR n 
1 403 PHE n 
1 404 SER n 
1 405 LEU n 
1 406 CYS n 
1 407 CYS n 
1 408 GLY n 
1 409 VAL n 
1 410 PHE n 
1 411 LEU n 
1 412 LEU n 
1 413 TRP n 
1 414 ARG n 
1 415 ARG n 
1 416 ARG n 
1 417 ALA n 
1 418 LEU n 
1 419 GLU n 
1 420 GLU n 
1 421 ASN n 
1 422 LEU n 
1 423 TYR n 
1 424 PHE n 
1 425 GLN n 
2 1   MET n 
2 2   ALA n 
2 3   GLN n 
2 4   VAL n 
2 5   GLN n 
2 6   LEU n 
2 7   VAL n 
2 8   GLU n 
2 9   SER n 
2 10  GLY n 
2 11  GLY n 
2 12  GLY n 
2 13  LEU n 
2 14  VAL n 
2 15  GLN n 
2 16  ALA n 
2 17  GLY n 
2 18  GLY n 
2 19  SER n 
2 20  LEU n 
2 21  GLY n 
2 22  LEU n 
2 23  SER n 
2 24  CYS n 
2 25  ALA n 
2 26  ALA n 
2 27  SER n 
2 28  GLY n 
2 29  ARG n 
2 30  THR n 
2 31  PHE n 
2 32  SER n 
2 33  ASN n 
2 34  TYR n 
2 35  VAL n 
2 36  MET n 
2 37  ALA n 
2 38  TRP n 
2 39  PHE n 
2 40  ARG n 
2 41  GLN n 
2 42  ALA n 
2 43  PRO n 
2 44  GLY n 
2 45  LYS n 
2 46  GLU n 
2 47  ARG n 
2 48  GLU n 
2 49  PHE n 
2 50  VAL n 
2 51  ALA n 
2 52  ARG n 
2 53  ILE n 
2 54  SER n 
2 55  GLU n 
2 56  SER n 
2 57  ARG n 
2 58  GLY n 
2 59  THR n 
2 60  THR n 
2 61  ASP n 
2 62  TYR n 
2 63  ALA n 
2 64  ASP n 
2 65  SER n 
2 66  VAL n 
2 67  LYS n 
2 68  GLY n 
2 69  ARG n 
2 70  PHE n 
2 71  THR n 
2 72  ILE n 
2 73  SER n 
2 74  ARG n 
2 75  ASP n 
2 76  ASN n 
2 77  ALA n 
2 78  LYS n 
2 79  ASN n 
2 80  THR n 
2 81  ILE n 
2 82  TYR n 
2 83  LEU n 
2 84  GLN n 
2 85  MET n 
2 86  ASN n 
2 87  SER n 
2 88  LEU n 
2 89  ASN n 
2 90  PRO n 
2 91  GLY n 
2 92  ASP n 
2 93  THR n 
2 94  ALA n 
2 95  VAL n 
2 96  TYR n 
2 97  SER n 
2 98  CYS n 
2 99  ALA n 
2 100 ALA n 
2 101 THR n 
2 102 LEU n 
2 103 PRO n 
2 104 ALA n 
2 105 TRP n 
2 106 THR n 
2 107 GLY n 
2 108 ILE n 
2 109 ILE n 
2 110 GLY n 
2 111 GLY n 
2 112 ARG n 
2 113 ARG n 
2 114 PRO n 
2 115 GLY n 
2 116 ASN n 
2 117 TYR n 
2 118 PRO n 
2 119 TYR n 
2 120 TRP n 
2 121 GLY n 
2 122 GLN n 
2 123 GLY n 
2 124 THR n 
2 125 GLN n 
2 126 VAL n 
2 127 THR n 
2 128 VAL n 
2 129 SER n 
2 130 SER n 
2 131 HIS n 
2 132 HIS n 
2 133 HIS n 
2 134 HIS n 
2 135 HIS n 
2 136 HIS n 
2 137 GLU n 
2 138 PRO n 
2 139 GLU n 
2 140 ALA 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' 1 425 ? ? 'wzxE, wzx, yifJ, b3792, JW3766' ? ? ? ? ? ? 'Escherichia coli' 562  ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ?          C43 ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 140 ? ? ?                                ? ? ? ? ? ? 'Lama glama'       9844 ? ? ? ? ? ? ? ? 
'Escherichia coli'           562    ? ? ? ? ? ? 'wk6(su-)' ?   ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                 ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                                ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                              ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                         ? 'C4 H7 N O4'     133.103 
CL  non-polymer         . 'CHLORIDE ION'                                          ? 'Cl -1'          35.453  
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 
ILE 'L-peptide linking' y ISOLEUCINE                                              ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                                 ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                                  ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                              ? 'C5 H11 N O2 S'  149.211 
MPG non-polymer         . '[(Z)-octadec-9-enyl] (2R)-2,3-bis(oxidanyl)propanoate' ? 'C21 H40 O4'     356.540 
OCT non-polymer         . N-OCTANE                                                ? 'C8 H18'         114.229 
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 
SO4 non-polymer         . 'SULFATE ION'                                           ? 'O4 S -2'        96.063  
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 
ZN  non-polymer         . 'ZINC ION'                                              ? 'Zn 2'           65.409  
# 
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   0   ?   ?   ?   A . n 
A 1 2   VAL 2   1   1   VAL VAL A . n 
A 1 3   SER 3   2   2   SER SER A . n 
A 1 4   LEU 4   3   3   LEU LEU A . n 
A 1 5   ALA 5   4   4   ALA ALA A . n 
A 1 6   LYS 6   5   5   LYS LYS A . n 
A 1 7   ALA 7   6   6   ALA ALA A . n 
A 1 8   SER 8   7   7   SER SER A . n 
A 1 9   LEU 9   8   8   LEU LEU A . n 
A 1 10  TRP 10  9   9   TRP TRP A . n 
A 1 11  THR 11  10  10  THR THR A . n 
A 1 12  ALA 12  11  11  ALA ALA A . n 
A 1 13  ALA 13  12  12  ALA ALA A . n 
A 1 14  SER 14  13  13  SER SER A . n 
A 1 15  THR 15  14  14  THR THR A . n 
A 1 16  LEU 16  15  15  LEU LEU A . n 
A 1 17  VAL 17  16  16  VAL VAL A . n 
A 1 18  LYS 18  17  17  LYS LYS A . n 
A 1 19  ILE 19  18  18  ILE ILE A . n 
A 1 20  GLY 20  19  19  GLY GLY A . n 
A 1 21  ALA 21  20  20  ALA ALA A . n 
A 1 22  GLY 22  21  21  GLY GLY A . n 
A 1 23  LEU 23  22  22  LEU LEU A . n 
A 1 24  LEU 24  23  23  LEU LEU A . n 
A 1 25  VAL 25  24  24  VAL VAL A . n 
A 1 26  GLY 26  25  25  GLY GLY A . n 
A 1 27  LYS 27  26  26  LYS LYS A . n 
A 1 28  LEU 28  27  27  LEU LEU A . n 
A 1 29  LEU 29  28  28  LEU LEU A . n 
A 1 30  ALA 30  29  29  ALA ALA A . n 
A 1 31  VAL 31  30  30  VAL VAL A . n 
A 1 32  SER 32  31  31  SER SER A . n 
A 1 33  PHE 33  32  32  PHE PHE A . n 
A 1 34  GLY 34  33  33  GLY GLY A . n 
A 1 35  PRO 35  34  34  PRO PRO A . n 
A 1 36  ALA 36  35  35  ALA ALA A . n 
A 1 37  GLY 37  36  36  GLY GLY A . n 
A 1 38  LEU 38  37  37  LEU LEU A . n 
A 1 39  GLY 39  38  38  GLY GLY A . n 
A 1 40  LEU 40  39  39  LEU LEU A . n 
A 1 41  ALA 41  40  40  ALA ALA A . n 
A 1 42  ALA 42  41  41  ALA ALA A . n 
A 1 43  ASN 43  42  42  ASN ASN A . n 
A 1 44  PHE 44  43  43  PHE PHE A . n 
A 1 45  ARG 45  44  44  ARG ARG A . n 
A 1 46  GLN 46  45  45  GLN GLN A . n 
A 1 47  LEU 47  46  46  LEU LEU A . n 
A 1 48  ILE 48  47  47  ILE ILE A . n 
A 1 49  THR 49  48  48  THR THR A . n 
A 1 50  VAL 50  49  49  VAL VAL A . n 
A 1 51  LEU 51  50  50  LEU LEU A . n 
A 1 52  GLY 52  51  51  GLY GLY A . n 
A 1 53  VAL 53  52  52  VAL VAL A . n 
A 1 54  LEU 54  53  53  LEU LEU A . n 
A 1 55  ALA 55  54  54  ALA ALA A . n 
A 1 56  GLY 56  55  55  GLY GLY A . n 
A 1 57  ALA 57  56  56  ALA ALA A . n 
A 1 58  GLY 58  57  57  GLY GLY A . n 
A 1 59  ILE 59  58  58  ILE ILE A . n 
A 1 60  PHE 60  59  59  PHE PHE A . n 
A 1 61  ASN 61  60  60  ASN ASN A . n 
A 1 62  GLY 62  61  61  GLY GLY A . n 
A 1 63  VAL 63  62  62  VAL VAL A . n 
A 1 64  THR 64  63  63  THR THR A . n 
A 1 65  LYS 65  64  64  LYS LYS A . n 
A 1 66  TYR 66  65  65  TYR TYR A . n 
A 1 67  VAL 67  66  66  VAL VAL A . n 
A 1 68  ALA 68  67  67  ALA ALA A . n 
A 1 69  GLN 69  68  68  GLN GLN A . n 
A 1 70  TYR 70  69  69  TYR TYR A . n 
A 1 71  HIS 71  70  70  HIS HIS A . n 
A 1 72  ASP 72  71  71  ASP ASP A . n 
A 1 73  ASN 73  72  72  ASN ASN A . n 
A 1 74  PRO 74  73  73  PRO PRO A . n 
A 1 75  GLN 75  74  74  GLN GLN A . n 
A 1 76  GLN 76  75  75  GLN GLN A . n 
A 1 77  LEU 77  76  76  LEU LEU A . n 
A 1 78  ARG 78  77  77  ARG ARG A . n 
A 1 79  ARG 79  78  78  ARG ARG A . n 
A 1 80  VAL 80  79  79  VAL VAL A . n 
A 1 81  VAL 81  80  80  VAL VAL A . n 
A 1 82  GLY 82  81  81  GLY GLY A . n 
A 1 83  THR 83  82  82  THR THR A . n 
A 1 84  SER 84  83  83  SER SER A . n 
A 1 85  SER 85  84  84  SER SER A . n 
A 1 86  ALA 86  85  85  ALA ALA A . n 
A 1 87  MET 87  86  86  MET MET A . n 
A 1 88  VAL 88  87  87  VAL VAL A . n 
A 1 89  LEU 89  88  88  LEU LEU A . n 
A 1 90  GLY 90  89  89  GLY GLY A . n 
A 1 91  PHE 91  90  90  PHE PHE A . n 
A 1 92  SER 92  91  91  SER SER A . n 
A 1 93  THR 93  92  92  THR THR A . n 
A 1 94  LEU 94  93  93  LEU LEU A . n 
A 1 95  MET 95  94  94  MET MET A . n 
A 1 96  ALA 96  95  95  ALA ALA A . n 
A 1 97  LEU 97  96  96  LEU LEU A . n 
A 1 98  VAL 98  97  97  VAL VAL A . n 
A 1 99  PHE 99  98  98  PHE PHE A . n 
A 1 100 VAL 100 99  99  VAL VAL A . n 
A 1 101 LEU 101 100 100 LEU LEU A . n 
A 1 102 ALA 102 101 101 ALA ALA A . n 
A 1 103 ALA 103 102 102 ALA ALA A . n 
A 1 104 ALA 104 103 103 ALA ALA A . n 
A 1 105 PRO 105 104 104 PRO PRO A . n 
A 1 106 ILE 106 105 105 ILE ILE A . n 
A 1 107 SER 107 106 106 SER SER A . n 
A 1 108 GLN 108 107 107 GLN GLN A . n 
A 1 109 GLY 109 108 108 GLY GLY A . n 
A 1 110 LEU 110 109 109 LEU LEU A . n 
A 1 111 PHE 111 110 110 PHE PHE A . n 
A 1 112 GLY 112 111 111 GLY GLY A . n 
A 1 113 ASN 113 112 112 ASN ASN A . n 
A 1 114 THR 114 113 113 THR THR A . n 
A 1 115 ASP 115 114 114 ASP ASP A . n 
A 1 116 TYR 116 115 115 TYR TYR A . n 
A 1 117 GLN 117 116 116 GLN GLN A . n 
A 1 118 GLY 118 117 117 GLY GLY A . n 
A 1 119 LEU 119 118 118 LEU LEU A . n 
A 1 120 VAL 120 119 119 VAL VAL A . n 
A 1 121 ARG 121 120 120 ARG ARG A . n 
A 1 122 LEU 122 121 121 LEU LEU A . n 
A 1 123 VAL 123 122 122 VAL VAL A . n 
A 1 124 ALA 124 123 123 ALA ALA A . n 
A 1 125 LEU 125 124 124 LEU LEU A . n 
A 1 126 VAL 126 125 125 VAL VAL A . n 
A 1 127 GLN 127 126 126 GLN GLN A . n 
A 1 128 MET 128 127 127 MET MET A . n 
A 1 129 GLY 129 128 128 GLY GLY A . n 
A 1 130 ILE 130 129 129 ILE ILE A . n 
A 1 131 ALA 131 130 130 ALA ALA A . n 
A 1 132 TRP 132 131 131 TRP TRP A . n 
A 1 133 GLY 133 132 132 GLY GLY A . n 
A 1 134 ASN 134 133 133 ASN ASN A . n 
A 1 135 LEU 135 134 134 LEU LEU A . n 
A 1 136 LEU 136 135 135 LEU LEU A . n 
A 1 137 LEU 137 136 136 LEU LEU A . n 
A 1 138 ALA 138 137 137 ALA ALA A . n 
A 1 139 LEU 139 138 138 LEU LEU A . n 
A 1 140 MET 140 139 139 MET MET A . n 
A 1 141 LYS 141 140 140 LYS LYS A . n 
A 1 142 GLY 142 141 141 GLY GLY A . n 
A 1 143 PHE 143 142 142 PHE PHE A . n 
A 1 144 ARG 144 143 143 ARG ARG A . n 
A 1 145 ASP 145 144 144 ASP ASP A . n 
A 1 146 ALA 146 145 145 ALA ALA A . n 
A 1 147 ALA 147 146 146 ALA ALA A . n 
A 1 148 GLY 148 147 147 GLY GLY A . n 
A 1 149 ASN 149 148 148 ASN ASN A . n 
A 1 150 ALA 150 149 149 ALA ALA A . n 
A 1 151 LEU 151 150 150 LEU LEU A . n 
A 1 152 SER 152 151 151 SER SER A . n 
A 1 153 LEU 153 152 152 LEU LEU A . n 
A 1 154 ILE 154 153 153 ILE ILE A . n 
A 1 155 VAL 155 154 154 VAL VAL A . n 
A 1 156 GLY 156 155 155 GLY GLY A . n 
A 1 157 SER 157 156 156 SER SER A . n 
A 1 158 LEU 158 157 157 LEU LEU A . n 
A 1 159 ILE 159 158 158 ILE ILE A . n 
A 1 160 GLY 160 159 159 GLY GLY A . n 
A 1 161 VAL 161 160 160 VAL VAL A . n 
A 1 162 LEU 162 161 161 LEU LEU A . n 
A 1 163 ALA 163 162 162 ALA ALA A . n 
A 1 164 TYR 164 163 163 TYR TYR A . n 
A 1 165 TYR 165 164 164 TYR TYR A . n 
A 1 166 VAL 166 165 165 VAL VAL A . n 
A 1 167 SER 167 166 166 SER SER A . n 
A 1 168 TYR 168 167 167 TYR TYR A . n 
A 1 169 ARG 169 168 168 ARG ARG A . n 
A 1 170 LEU 170 169 169 LEU LEU A . n 
A 1 171 GLY 171 170 170 GLY GLY A . n 
A 1 172 GLY 172 171 171 GLY GLY A . n 
A 1 173 TYR 173 172 172 TYR TYR A . n 
A 1 174 GLU 174 173 173 GLU GLU A . n 
A 1 175 GLY 175 174 174 GLY GLY A . n 
A 1 176 ALA 176 175 175 ALA ALA A . n 
A 1 177 LEU 177 176 176 LEU LEU A . n 
A 1 178 LEU 178 177 177 LEU LEU A . n 
A 1 179 GLY 179 178 178 GLY GLY A . n 
A 1 180 LEU 180 179 179 LEU LEU A . n 
A 1 181 ALA 181 180 180 ALA ALA A . n 
A 1 182 LEU 182 181 181 LEU LEU A . n 
A 1 183 ILE 183 182 182 ILE ILE A . n 
A 1 184 PRO 184 183 183 PRO PRO A . n 
A 1 185 ALA 185 184 184 ALA ALA A . n 
A 1 186 LEU 186 185 185 LEU LEU A . n 
A 1 187 VAL 187 186 186 VAL VAL A . n 
A 1 188 VAL 188 187 187 VAL VAL A . n 
A 1 189 ILE 189 188 188 ILE ILE A . n 
A 1 190 PRO 190 189 189 PRO PRO A . n 
A 1 191 ALA 191 190 190 ALA ALA A . n 
A 1 192 ALA 192 191 191 ALA ALA A . n 
A 1 193 ILE 193 192 192 ILE ILE A . n 
A 1 194 MET 194 193 193 MET MET A . n 
A 1 195 LEU 195 194 194 LEU LEU A . n 
A 1 196 ILE 196 195 195 ILE ILE A . n 
A 1 197 LYS 197 196 196 LYS LYS A . n 
A 1 198 ARG 198 197 197 ARG ARG A . n 
A 1 199 GLY 199 198 198 GLY GLY A . n 
A 1 200 VAL 200 199 199 VAL VAL A . n 
A 1 201 ILE 201 200 200 ILE ILE A . n 
A 1 202 PRO 202 201 201 PRO PRO A . n 
A 1 203 LEU 203 202 202 LEU LEU A . n 
A 1 204 SER 204 203 203 SER SER A . n 
A 1 205 TYR 205 204 204 TYR TYR A . n 
A 1 206 LEU 206 205 205 LEU LEU A . n 
A 1 207 LYS 207 206 206 LYS LYS A . n 
A 1 208 PRO 208 207 207 PRO PRO A . n 
A 1 209 SER 209 208 208 SER SER A . n 
A 1 210 TRP 210 209 209 TRP TRP A . n 
A 1 211 ASP 211 210 210 ASP ASP A . n 
A 1 212 ASN 212 211 211 ASN ASN A . n 
A 1 213 GLY 213 212 212 GLY GLY A . n 
A 1 214 LEU 214 213 213 LEU LEU A . n 
A 1 215 ALA 215 214 214 ALA ALA A . n 
A 1 216 GLY 216 215 215 GLY GLY A . n 
A 1 217 GLN 217 216 216 GLN GLN A . n 
A 1 218 LEU 218 217 217 LEU LEU A . n 
A 1 219 SER 219 218 218 SER SER A . n 
A 1 220 LYS 220 219 219 LYS LYS A . n 
A 1 221 PHE 221 220 220 PHE PHE A . n 
A 1 222 THR 222 221 221 THR THR A . n 
A 1 223 LEU 223 222 222 LEU LEU A . n 
A 1 224 MET 224 223 223 MET MET A . n 
A 1 225 ALA 225 224 224 ALA ALA A . n 
A 1 226 LEU 226 225 225 LEU LEU A . n 
A 1 227 ILE 227 226 226 ILE ILE A . n 
A 1 228 THR 228 227 227 THR THR A . n 
A 1 229 SER 229 228 228 SER SER A . n 
A 1 230 VAL 230 229 229 VAL VAL A . n 
A 1 231 THR 231 230 230 THR THR A . n 
A 1 232 LEU 232 231 231 LEU LEU A . n 
A 1 233 PRO 233 232 232 PRO PRO A . n 
A 1 234 VAL 234 233 233 VAL VAL A . n 
A 1 235 ALA 235 234 234 ALA ALA A . n 
A 1 236 TYR 236 235 235 TYR TYR A . n 
A 1 237 ILE 237 236 236 ILE ILE A . n 
A 1 238 MET 238 237 237 MET MET A . n 
A 1 239 MET 239 238 238 MET MET A . n 
A 1 240 ARG 240 239 239 ARG ARG A . n 
A 1 241 LYS 241 240 240 LYS LYS A . n 
A 1 242 LEU 242 241 241 LEU LEU A . n 
A 1 243 LEU 243 242 242 LEU LEU A . n 
A 1 244 ALA 244 243 243 ALA ALA A . n 
A 1 245 ALA 245 244 244 ALA ALA A . n 
A 1 246 GLN 246 245 245 GLN GLN A . n 
A 1 247 TYR 247 246 246 TYR TYR A . n 
A 1 248 SER 248 247 247 SER SER A . n 
A 1 249 TRP 249 248 248 TRP TRP A . n 
A 1 250 ASP 250 249 249 ASP ASP A . n 
A 1 251 GLU 251 250 250 GLU GLU A . n 
A 1 252 VAL 252 251 251 VAL VAL A . n 
A 1 253 GLY 253 252 252 GLY GLY A . n 
A 1 254 ILE 254 253 253 ILE ILE A . n 
A 1 255 TRP 255 254 254 TRP TRP A . n 
A 1 256 GLN 256 255 255 GLN GLN A . n 
A 1 257 GLY 257 256 256 GLY GLY A . n 
A 1 258 VAL 258 257 257 VAL VAL A . n 
A 1 259 SER 259 258 258 SER SER A . n 
A 1 260 SER 260 259 259 SER SER A . n 
A 1 261 ILE 261 260 260 ILE ILE A . n 
A 1 262 SER 262 261 261 SER SER A . n 
A 1 263 ASP 263 262 262 ASP ASP A . n 
A 1 264 ALA 264 263 263 ALA ALA A . n 
A 1 265 TYR 265 264 264 TYR TYR A . n 
A 1 266 LEU 266 265 265 LEU LEU A . n 
A 1 267 GLN 267 266 266 GLN GLN A . n 
A 1 268 PHE 268 267 267 PHE PHE A . n 
A 1 269 ILE 269 268 268 ILE ILE A . n 
A 1 270 THR 270 269 269 THR THR A . n 
A 1 271 ALA 271 270 270 ALA ALA A . n 
A 1 272 SER 272 271 271 SER SER A . n 
A 1 273 PHE 273 272 272 PHE PHE A . n 
A 1 274 SER 274 273 273 SER SER A . n 
A 1 275 VAL 275 274 274 VAL VAL A . n 
A 1 276 TYR 276 275 275 TYR TYR A . n 
A 1 277 LEU 277 276 276 LEU LEU A . n 
A 1 278 LEU 278 277 277 LEU LEU A . n 
A 1 279 PRO 279 278 278 PRO PRO A . n 
A 1 280 THR 280 279 279 THR THR A . n 
A 1 281 LEU 281 280 280 LEU LEU A . n 
A 1 282 SER 282 281 281 SER SER A . n 
A 1 283 ARG 283 282 282 ARG ARG A . n 
A 1 284 LEU 284 283 283 LEU LEU A . n 
A 1 285 THR 285 284 284 THR THR A . n 
A 1 286 GLU 286 285 285 GLU GLU A . n 
A 1 287 LYS 287 286 286 LYS LYS A . n 
A 1 288 ARG 288 287 287 ARG ARG A . n 
A 1 289 ASP 289 288 288 ASP ASP A . n 
A 1 290 ILE 290 289 289 ILE ILE A . n 
A 1 291 THR 291 290 290 THR THR A . n 
A 1 292 ARG 292 291 291 ARG ARG A . n 
A 1 293 GLU 293 292 292 GLU GLU A . n 
A 1 294 VAL 294 293 293 VAL VAL A . n 
A 1 295 VAL 295 294 294 VAL VAL A . n 
A 1 296 LYS 296 295 295 LYS LYS A . n 
A 1 297 SER 297 296 296 SER SER A . n 
A 1 298 LEU 298 297 297 LEU LEU A . n 
A 1 299 LYS 299 298 298 LYS LYS A . n 
A 1 300 PHE 300 299 299 PHE PHE A . n 
A 1 301 VAL 301 300 300 VAL VAL A . n 
A 1 302 LEU 302 301 301 LEU LEU A . n 
A 1 303 PRO 303 302 302 PRO PRO A . n 
A 1 304 ALA 304 303 303 ALA ALA A . n 
A 1 305 VAL 305 304 304 VAL VAL A . n 
A 1 306 ALA 306 305 305 ALA ALA A . n 
A 1 307 ALA 307 306 306 ALA ALA A . n 
A 1 308 ALA 308 307 307 ALA ALA A . n 
A 1 309 SER 309 308 308 SER SER A . n 
A 1 310 PHE 310 309 309 PHE PHE A . n 
A 1 311 THR 311 310 310 THR THR A . n 
A 1 312 VAL 312 311 311 VAL VAL A . n 
A 1 313 TRP 313 312 312 TRP TRP A . n 
A 1 314 LEU 314 313 313 LEU LEU A . n 
A 1 315 LEU 315 314 314 LEU LEU A . n 
A 1 316 ARG 316 315 315 ARG ARG A . n 
A 1 317 ASP 317 316 316 ASP ASP A . n 
A 1 318 PHE 318 317 317 PHE PHE A . n 
A 1 319 ALA 319 318 318 ALA ALA A . n 
A 1 320 ILE 320 319 319 ILE ILE A . n 
A 1 321 TRP 321 320 320 TRP TRP A . n 
A 1 322 LEU 322 321 321 LEU LEU A . n 
A 1 323 LEU 323 322 322 LEU LEU A . n 
A 1 324 LEU 324 323 323 LEU LEU A . n 
A 1 325 SER 325 324 324 SER SER A . n 
A 1 326 ASN 326 325 325 ASN ASN A . n 
A 1 327 LYS 327 326 326 LYS LYS A . n 
A 1 328 PHE 328 327 327 PHE PHE A . n 
A 1 329 THR 329 328 328 THR THR A . n 
A 1 330 ALA 330 329 329 ALA ALA A . n 
A 1 331 MET 331 330 330 MET MET A . n 
A 1 332 ARG 332 331 331 ARG ARG A . n 
A 1 333 ASP 333 332 332 ASP ASP A . n 
A 1 334 LEU 334 333 333 LEU LEU A . n 
A 1 335 PHE 335 334 334 PHE PHE A . n 
A 1 336 ALA 336 335 335 ALA ALA A . n 
A 1 337 TRP 337 336 336 TRP TRP A . n 
A 1 338 GLN 338 337 337 GLN GLN A . n 
A 1 339 LEU 339 338 338 LEU LEU A . n 
A 1 340 VAL 340 339 339 VAL VAL A . n 
A 1 341 GLY 341 340 340 GLY GLY A . n 
A 1 342 ASP 342 341 341 ASP ASP A . n 
A 1 343 VAL 343 342 342 VAL VAL A . n 
A 1 344 LEU 344 343 343 LEU LEU A . n 
A 1 345 LYS 345 344 344 LYS LYS A . n 
A 1 346 VAL 346 345 345 VAL VAL A . n 
A 1 347 GLY 347 346 346 GLY GLY A . n 
A 1 348 ALA 348 347 347 ALA ALA A . n 
A 1 349 TYR 349 348 348 TYR TYR A . n 
A 1 350 VAL 350 349 349 VAL VAL A . n 
A 1 351 PHE 351 350 350 PHE PHE A . n 
A 1 352 GLY 352 351 351 GLY GLY A . n 
A 1 353 TYR 353 352 352 TYR TYR A . n 
A 1 354 LEU 354 353 353 LEU LEU A . n 
A 1 355 VAL 355 354 354 VAL VAL A . n 
A 1 356 ILE 356 355 355 ILE ILE A . n 
A 1 357 ALA 357 356 356 ALA ALA A . n 
A 1 358 LYS 358 357 357 LYS LYS A . n 
A 1 359 ALA 359 358 358 ALA ALA A . n 
A 1 360 SER 360 359 359 SER SER A . n 
A 1 361 LEU 361 360 360 LEU LEU A . n 
A 1 362 ARG 362 361 361 ARG ARG A . n 
A 1 363 PHE 363 362 362 PHE PHE A . n 
A 1 364 TYR 364 363 363 TYR TYR A . n 
A 1 365 ILE 365 364 364 ILE ILE A . n 
A 1 366 LEU 366 365 365 LEU LEU A . n 
A 1 367 ALA 367 366 366 ALA ALA A . n 
A 1 368 GLU 368 367 367 GLU GLU A . n 
A 1 369 VAL 369 368 368 VAL VAL A . n 
A 1 370 SER 370 369 369 SER SER A . n 
A 1 371 GLN 371 370 370 GLN GLN A . n 
A 1 372 PHE 372 371 371 PHE PHE A . n 
A 1 373 THR 373 372 372 THR THR A . n 
A 1 374 LEU 374 373 373 LEU LEU A . n 
A 1 375 LEU 375 374 374 LEU LEU A . n 
A 1 376 MET 376 375 375 MET MET A . n 
A 1 377 VAL 377 376 376 VAL VAL A . n 
A 1 378 PHE 378 377 377 PHE PHE A . n 
A 1 379 ALA 379 378 378 ALA ALA A . n 
A 1 380 HIS 380 379 379 HIS HIS A . n 
A 1 381 TRP 381 380 380 TRP TRP A . n 
A 1 382 LEU 382 381 381 LEU LEU A . n 
A 1 383 ILE 383 382 382 ILE ILE A . n 
A 1 384 PRO 384 383 383 PRO PRO A . n 
A 1 385 ALA 385 384 384 ALA ALA A . n 
A 1 386 HIS 386 385 385 HIS HIS A . n 
A 1 387 GLY 387 386 386 GLY GLY A . n 
A 1 388 ALA 388 387 387 ALA ALA A . n 
A 1 389 LEU 389 388 388 LEU LEU A . n 
A 1 390 GLY 390 389 389 GLY GLY A . n 
A 1 391 ALA 391 390 390 ALA ALA A . n 
A 1 392 ALA 392 391 391 ALA ALA A . n 
A 1 393 GLN 393 392 392 GLN GLN A . n 
A 1 394 ALA 394 393 393 ALA ALA A . n 
A 1 395 TYR 395 394 394 TYR TYR A . n 
A 1 396 MET 396 395 395 MET MET A . n 
A 1 397 ALA 397 396 396 ALA ALA A . n 
A 1 398 THR 398 397 397 THR THR A . n 
A 1 399 TYR 399 398 398 TYR TYR A . n 
A 1 400 ILE 400 399 399 ILE ILE A . n 
A 1 401 VAL 401 400 400 VAL VAL A . n 
A 1 402 TYR 402 401 401 TYR TYR A . n 
A 1 403 PHE 403 402 402 PHE PHE A . n 
A 1 404 SER 404 403 403 SER SER A . n 
A 1 405 LEU 405 404 404 LEU LEU A . n 
A 1 406 CYS 406 405 405 CYS CYS A . n 
A 1 407 CYS 407 406 406 CYS CYS A . n 
A 1 408 GLY 408 407 407 GLY GLY A . n 
A 1 409 VAL 409 408 408 VAL VAL A . n 
A 1 410 PHE 410 409 409 PHE PHE A . n 
A 1 411 LEU 411 410 410 LEU LEU A . n 
A 1 412 LEU 412 411 411 LEU LEU A . n 
A 1 413 TRP 413 412 412 TRP TRP A . n 
A 1 414 ARG 414 413 413 ARG ARG A . n 
A 1 415 ARG 415 414 414 ARG ARG A . n 
A 1 416 ARG 416 415 415 ARG ARG A . n 
A 1 417 ALA 417 416 416 ALA ALA A . n 
A 1 418 LEU 418 417 417 LEU LEU A . n 
A 1 419 GLU 419 418 418 GLU GLU A . n 
A 1 420 GLU 420 419 ?   ?   ?   A . n 
A 1 421 ASN 421 420 ?   ?   ?   A . n 
A 1 422 LEU 422 421 ?   ?   ?   A . n 
A 1 423 TYR 423 422 ?   ?   ?   A . n 
A 1 424 PHE 424 423 ?   ?   ?   A . n 
A 1 425 GLN 425 424 ?   ?   ?   A . n 
B 2 1   MET 1   -1  ?   ?   ?   B . n 
B 2 2   ALA 2   0   ?   ?   ?   B . n 
B 2 3   GLN 3   1   ?   ?   ?   B . n 
B 2 4   VAL 4   2   ?   ?   ?   B . n 
B 2 5   GLN 5   3   3   GLN GLN B . n 
B 2 6   LEU 6   4   4   LEU LEU B . n 
B 2 7   VAL 7   5   5   VAL VAL B . n 
B 2 8   GLU 8   6   6   GLU GLU B . n 
B 2 9   SER 9   7   7   SER SER B . n 
B 2 10  GLY 10  8   8   GLY GLY B . n 
B 2 11  GLY 11  9   9   GLY GLY B . n 
B 2 12  GLY 12  10  10  GLY GLY B . n 
B 2 13  LEU 13  11  11  LEU LEU B . n 
B 2 14  VAL 14  12  12  VAL VAL B . n 
B 2 15  GLN 15  13  13  GLN GLN B . n 
B 2 16  ALA 16  14  14  ALA ALA B . n 
B 2 17  GLY 17  15  15  GLY GLY B . n 
B 2 18  GLY 18  16  16  GLY GLY B . n 
B 2 19  SER 19  17  17  SER SER B . n 
B 2 20  LEU 20  18  18  LEU LEU B . n 
B 2 21  GLY 21  19  19  GLY GLY B . n 
B 2 22  LEU 22  20  20  LEU LEU B . n 
B 2 23  SER 23  21  21  SER SER B . n 
B 2 24  CYS 24  22  22  CYS CYS B . n 
B 2 25  ALA 25  23  23  ALA ALA B . n 
B 2 26  ALA 26  24  24  ALA ALA B . n 
B 2 27  SER 27  25  25  SER SER B . n 
B 2 28  GLY 28  26  26  GLY GLY B . n 
B 2 29  ARG 29  27  27  ARG ARG B . n 
B 2 30  THR 30  28  28  THR THR B . n 
B 2 31  PHE 31  29  29  PHE PHE B . n 
B 2 32  SER 32  30  30  SER SER B . n 
B 2 33  ASN 33  31  31  ASN ASN B . n 
B 2 34  TYR 34  32  32  TYR TYR B . n 
B 2 35  VAL 35  33  33  VAL VAL B . n 
B 2 36  MET 36  34  34  MET MET B . n 
B 2 37  ALA 37  35  35  ALA ALA B . n 
B 2 38  TRP 38  36  36  TRP TRP B . n 
B 2 39  PHE 39  37  37  PHE PHE B . n 
B 2 40  ARG 40  38  38  ARG ARG B . n 
B 2 41  GLN 41  39  39  GLN GLN B . n 
B 2 42  ALA 42  40  40  ALA ALA B . n 
B 2 43  PRO 43  41  41  PRO PRO B . n 
B 2 44  GLY 44  42  42  GLY GLY B . n 
B 2 45  LYS 45  43  43  LYS LYS B . n 
B 2 46  GLU 46  44  44  GLU GLU B . n 
B 2 47  ARG 47  45  45  ARG ARG B . n 
B 2 48  GLU 48  46  46  GLU GLU B . n 
B 2 49  PHE 49  47  47  PHE PHE B . n 
B 2 50  VAL 50  48  48  VAL VAL B . n 
B 2 51  ALA 51  49  49  ALA ALA B . n 
B 2 52  ARG 52  50  50  ARG ARG B . n 
B 2 53  ILE 53  51  51  ILE ILE B . n 
B 2 54  SER 54  52  52  SER SER B . n 
B 2 55  GLU 55  53  53  GLU GLU B . n 
B 2 56  SER 56  54  54  SER SER B . n 
B 2 57  ARG 57  55  55  ARG ARG B . n 
B 2 58  GLY 58  56  56  GLY GLY B . n 
B 2 59  THR 59  57  57  THR THR B . n 
B 2 60  THR 60  58  58  THR THR B . n 
B 2 61  ASP 61  59  59  ASP ASP B . n 
B 2 62  TYR 62  60  60  TYR TYR B . n 
B 2 63  ALA 63  61  61  ALA ALA B . n 
B 2 64  ASP 64  62  62  ASP ASP B . n 
B 2 65  SER 65  63  63  SER SER B . n 
B 2 66  VAL 66  64  64  VAL VAL B . n 
B 2 67  LYS 67  65  65  LYS LYS B . n 
B 2 68  GLY 68  66  66  GLY GLY B . n 
B 2 69  ARG 69  67  67  ARG ARG B . n 
B 2 70  PHE 70  68  68  PHE PHE B . n 
B 2 71  THR 71  69  69  THR THR B . n 
B 2 72  ILE 72  70  70  ILE ILE B . n 
B 2 73  SER 73  71  71  SER SER B . n 
B 2 74  ARG 74  72  72  ARG ARG B . n 
B 2 75  ASP 75  73  73  ASP ASP B . n 
B 2 76  ASN 76  74  74  ASN ASN B . n 
B 2 77  ALA 77  75  75  ALA ALA B . n 
B 2 78  LYS 78  76  76  LYS LYS B . n 
B 2 79  ASN 79  77  77  ASN ASN B . n 
B 2 80  THR 80  78  78  THR THR B . n 
B 2 81  ILE 81  79  79  ILE ILE B . n 
B 2 82  TYR 82  80  80  TYR TYR B . n 
B 2 83  LEU 83  81  81  LEU LEU B . n 
B 2 84  GLN 84  82  82  GLN GLN B . n 
B 2 85  MET 85  83  83  MET MET B . n 
B 2 86  ASN 86  84  84  ASN ASN B . n 
B 2 87  SER 87  85  85  SER SER B . n 
B 2 88  LEU 88  86  86  LEU LEU B . n 
B 2 89  ASN 89  87  87  ASN ASN B . n 
B 2 90  PRO 90  88  88  PRO PRO B . n 
B 2 91  GLY 91  89  89  GLY GLY B . n 
B 2 92  ASP 92  90  90  ASP ASP B . n 
B 2 93  THR 93  91  91  THR THR B . n 
B 2 94  ALA 94  92  92  ALA ALA B . n 
B 2 95  VAL 95  93  93  VAL VAL B . n 
B 2 96  TYR 96  94  94  TYR TYR B . n 
B 2 97  SER 97  95  95  SER SER B . n 
B 2 98  CYS 98  96  96  CYS CYS B . n 
B 2 99  ALA 99  97  97  ALA ALA B . n 
B 2 100 ALA 100 98  98  ALA ALA B . n 
B 2 101 THR 101 99  99  THR THR B . n 
B 2 102 LEU 102 100 100 LEU LEU B . n 
B 2 103 PRO 103 101 101 PRO PRO B . n 
B 2 104 ALA 104 102 102 ALA ALA B . n 
B 2 105 TRP 105 103 103 TRP TRP B . n 
B 2 106 THR 106 104 104 THR THR B . n 
B 2 107 GLY 107 105 105 GLY GLY B . n 
B 2 108 ILE 108 106 106 ILE ILE B . n 
B 2 109 ILE 109 107 107 ILE ILE B . n 
B 2 110 GLY 110 108 108 GLY GLY B . n 
B 2 111 GLY 111 109 109 GLY GLY B . n 
B 2 112 ARG 112 110 110 ARG ARG B . n 
B 2 113 ARG 113 111 111 ARG ARG B . n 
B 2 114 PRO 114 112 112 PRO PRO B . n 
B 2 115 GLY 115 113 113 GLY GLY B . n 
B 2 116 ASN 116 114 114 ASN ASN B . n 
B 2 117 TYR 117 115 115 TYR TYR B . n 
B 2 118 PRO 118 116 116 PRO PRO B . n 
B 2 119 TYR 119 117 117 TYR TYR B . n 
B 2 120 TRP 120 118 118 TRP TRP B . n 
B 2 121 GLY 121 119 119 GLY GLY B . n 
B 2 122 GLN 122 120 120 GLN GLN B . n 
B 2 123 GLY 123 121 121 GLY GLY B . n 
B 2 124 THR 124 122 122 THR THR B . n 
B 2 125 GLN 125 123 123 GLN GLN B . n 
B 2 126 VAL 126 124 124 VAL VAL B . n 
B 2 127 THR 127 125 125 THR THR B . n 
B 2 128 VAL 128 126 126 VAL VAL B . n 
B 2 129 SER 129 127 127 SER SER B . n 
B 2 130 SER 130 128 ?   ?   ?   B . n 
B 2 131 HIS 131 129 ?   ?   ?   B . n 
B 2 132 HIS 132 130 ?   ?   ?   B . n 
B 2 133 HIS 133 131 ?   ?   ?   B . n 
B 2 134 HIS 134 132 ?   ?   ?   B . n 
B 2 135 HIS 135 133 ?   ?   ?   B . n 
B 2 136 HIS 136 134 ?   ?   ?   B . n 
B 2 137 GLU 137 135 ?   ?   ?   B . n 
B 2 138 PRO 138 136 ?   ?   ?   B . n 
B 2 139 GLU 139 137 ?   ?   ?   B . n 
B 2 140 ALA 140 138 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 MPG 1 501 419 MPG MPG A . 
D 3 MPG 1 502 420 MPG MPG A . 
E 3 MPG 1 503 421 MPG MPG A . 
F 3 MPG 1 504 422 MPG MPG A . 
G 3 MPG 1 505 423 MPG MPG A . 
H 4 OCT 1 506 424 OCT OCT A . 
I 4 OCT 1 507 425 OCT OCT A . 
J 4 OCT 1 508 426 OCT OCT A . 
K 4 OCT 1 509 427 OCT OCT A . 
L 4 OCT 1 510 428 OCT OCT A . 
M 5 SO4 1 511 429 SO4 SO4 A . 
N 5 SO4 1 512 430 SO4 SO4 A . 
O 6 ZN  1 513 431 ZN  ZN  A . 
P 7 CL  1 514 432 CL  CL  A . 
Q 7 CL  1 515 433 CL  CL  A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? CRANK2 ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   93.09 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9G95 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     271.540 
_cell.length_a_esd                 ? 
_cell.length_b                     38.450 
_cell.length_b_esd                 ? 
_cell.length_c                     56.960 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9G95 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 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                   9G95 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.42 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.24 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'LIPIDIC CUBIC PHASE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'Na acetate, PEG400, lithium sulfate, zinc chloride, E. coli polar lipids, monoolein' 
_exptl_crystal_grow.pdbx_pH_range   6.4-6.43 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     80 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 12M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-07-26 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   2.7552 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'DIAMOND BEAMLINE I23' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        2.7552 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I23 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9G95 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.80 
_reflns.d_resolution_low                               45.19 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     14932 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                85.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          30.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.91 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.80 
_reflns_shell.d_res_low                                     2.95 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.7 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2147 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               19.6 
_reflns_shell.pdbx_chi_squared                              0.73 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.872 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.9 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_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                                 9G95 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_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                            2.80 
_refine.ls_d_res_low                             44.78 
_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                     14921 
_refine.ls_number_reflns_R_free                  704 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.92 
_refine.ls_percent_reflns_R_free                 4.72 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2383 
_refine.ls_R_factor_R_free                       0.2887 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2359 
_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                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_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                          1.35 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          SAD 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_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             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 31.58 
_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                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.47 
_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                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.80 
_refine_hist.d_res_low                        44.78 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               4310 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4132 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         178 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.002  ? 4387 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.658  ? 5913 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 16.408 ? 1569 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.037  ? 678  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 717  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.80 3.02  . . 160 2773 100.00 . . . . 0.2869 . . . . . . . . . . . 0.3652 
'X-RAY DIFFRACTION' 3.02 3.32  . . 150 2787 100.00 . . . . 0.2756 . . . . . . . . . . . 0.3155 
'X-RAY DIFFRACTION' 3.32 3.80  . . 137 2858 100.00 . . . . 0.2469 . . . . . . . . . . . 0.2920 
'X-RAY DIFFRACTION' 3.80 4.79  . . 122 2852 100.00 . . . . 0.2256 . . . . . . . . . . . 0.2457 
'X-RAY DIFFRACTION' 4.79 44.78 . . 135 2947 100.00 . . . . 0.2177 . . . . . . . . . . . 0.2924 
# 
_struct.entry_id                     9G95 
_struct.title                        'Lipid III flippase WzxE with NB10 nanobody in outward-facing conformation at 2.7552 A' 
_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        9G95 
_struct_keywords.text            
'membrane protein, flippase, cell wall, enterobacterial common antigen, lipid III, 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 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 4 ? 
I N N 4 ? 
J N N 4 ? 
K N N 4 ? 
L N N 4 ? 
M N N 5 ? 
N N N 5 ? 
O N N 6 ? 
P N N 7 ? 
Q N N 7 ? 
# 
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 WZXE_ECOLI P0AAA7 ? 1 
;SLAKASLWTAASTLVKIGAGLLVGKLLAVSFGPAGLGLAANFRQLITVLGVLAGAGIFNGVTKYVAQYHDNPQQLRRVVG
TSSAMVLGFSTLMALVFVLAAAPISQGLFGNTDYQGLVRLVALVQMGIAWGNLLLALMKGFRDAAGNALSLIVGSLIGVL
AYYVSYRLGGYEGALLGLALIPALVVIPAAIMLIKRGVIPLSYLKPSWDNGLAGQLSKFTLMALITSVTLPVAYIMMRKL
LAAQYSWDEVGIWQGVSSISDAYLQFITASFSVYLLPTLSRLTEKRDITREVVKSLKFVLPAVAAASFTVWLLRDFAIWL
LLSNKFTAMRDLFAWQLVGDVLKVGAYVFGYLVIAKASLRFYILAEVSQFTLLMVFAHWLIPAHGALGAAQAYMATYIVY
FSLCCGVFLLWRRRA
;
2 
2 PDB 9G95       9G95   ? 2 ? 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 9G95 A 3 ? 417 ? P0AAA7 2  ? 416 ? 2  416 
2 2 9G95 B 1 ? 140 ? 9G95   -1 ? 138 ? -1 138 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9G95 MET A 1   ? UNP P0AAA7 ? ? 'initiating methionine' 0   1  
1 9G95 VAL A 2   ? UNP P0AAA7 ? ? 'cloning artifact'      1   2  
1 9G95 LEU A 418 ? UNP P0AAA7 ? ? 'expression tag'        417 3  
1 9G95 GLU A 419 ? UNP P0AAA7 ? ? 'expression tag'        418 4  
1 9G95 GLU A 420 ? UNP P0AAA7 ? ? 'expression tag'        419 5  
1 9G95 ASN A 421 ? UNP P0AAA7 ? ? 'expression tag'        420 6  
1 9G95 LEU A 422 ? UNP P0AAA7 ? ? 'expression tag'        421 7  
1 9G95 TYR A 423 ? UNP P0AAA7 ? ? 'expression tag'        422 8  
1 9G95 PHE A 424 ? UNP P0AAA7 ? ? 'expression tag'        423 9  
1 9G95 GLN A 425 ? UNP P0AAA7 ? ? 'expression tag'        424 10 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q 
# 
_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                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_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 SER A 3   ? ALA A 55  ? SER A 2   ALA A 54  1 ? 53 
HELX_P HELX_P2  AA2 ILE A 59  ? TYR A 70  ? ILE A 58  TYR A 69  1 ? 12 
HELX_P HELX_P3  AA3 ASN A 73  ? ALA A 102 ? ASN A 72  ALA A 101 1 ? 30 
HELX_P HELX_P4  AA4 ALA A 102 ? GLY A 112 ? ALA A 101 GLY A 111 1 ? 11 
HELX_P HELX_P5  AA5 TYR A 116 ? PHE A 143 ? TYR A 115 PHE A 142 1 ? 28 
HELX_P HELX_P6  AA6 ASP A 145 ? LEU A 186 ? ASP A 144 LEU A 185 1 ? 42 
HELX_P HELX_P7  AA7 VAL A 187 ? ARG A 198 ? VAL A 186 ARG A 197 1 ? 12 
HELX_P HELX_P8  AA8 PRO A 202 ? LYS A 207 ? PRO A 201 LYS A 206 5 ? 6  
HELX_P HELX_P9  AA9 ASP A 211 ? SER A 229 ? ASP A 210 SER A 228 1 ? 19 
HELX_P HELX_P10 AB1 VAL A 230 ? TYR A 247 ? VAL A 229 TYR A 246 1 ? 18 
HELX_P HELX_P11 AB2 SER A 248 ? THR A 270 ? SER A 247 THR A 269 1 ? 23 
HELX_P HELX_P12 AB3 TYR A 276 ? LEU A 284 ? TYR A 275 LEU A 283 1 ? 9  
HELX_P HELX_P13 AB4 GLU A 286 ? LEU A 315 ? GLU A 285 LEU A 314 1 ? 30 
HELX_P HELX_P14 AB5 LEU A 315 ? LEU A 324 ? LEU A 314 LEU A 323 1 ? 10 
HELX_P HELX_P15 AB6 MET A 331 ? LYS A 358 ? MET A 330 LYS A 357 1 ? 28 
HELX_P HELX_P16 AB7 SER A 360 ? ARG A 415 ? SER A 359 ARG A 414 1 ? 56 
HELX_P HELX_P17 AB8 ASN B 89  ? THR B 93  ? ASN B 87  THR B 91  5 ? 5  
HELX_P HELX_P18 AB9 LEU B 102 ? GLY B 107 ? LEU B 100 GLY B 105 1 ? 6  
HELX_P HELX_P19 AC1 ARG B 113 ? TYR B 117 ? ARG B 111 TYR B 115 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            disulf1 
_struct_conn.conn_type_id                  disulf 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           B 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            24 
_struct_conn.ptnr1_label_atom_id           SG 
_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                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           CYS 
_struct_conn.ptnr2_label_seq_id            98 
_struct_conn.ptnr2_label_atom_id           SG 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            B 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             22 
_struct_conn.ptnr2_auth_asym_id            B 
_struct_conn.ptnr2_auth_comp_id            CYS 
_struct_conn.ptnr2_auth_seq_id             96 
_struct_conn.ptnr2_symmetry                1_555 
_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               2.032 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       24 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     B 
_pdbx_modification_feature.modified_residue_label_seq_id      98 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       B 
_pdbx_modification_feature.auth_seq_id                        22 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      B 
_pdbx_modification_feature.modified_residue_auth_seq_id       96 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 6 ? 
AA3 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU B 6   ? SER B 9   ? LEU B 4   SER B 7   
AA1 2 LEU B 20  ? ALA B 26  ? LEU B 18  ALA B 24  
AA1 3 THR B 80  ? MET B 85  ? THR B 78  MET B 83  
AA1 4 PHE B 70  ? ASP B 75  ? PHE B 68  ASP B 73  
AA2 1 LEU B 13  ? GLN B 15  ? LEU B 11  GLN B 13  
AA2 2 THR B 124 ? SER B 129 ? THR B 122 SER B 127 
AA2 3 ALA B 94  ? THR B 101 ? ALA B 92  THR B 99  
AA2 4 VAL B 35  ? GLN B 41  ? VAL B 33  GLN B 39  
AA2 5 GLU B 48  ? ILE B 53  ? GLU B 46  ILE B 51  
AA2 6 THR B 60  ? TYR B 62  ? THR B 58  TYR B 60  
AA3 1 LEU B 13  ? GLN B 15  ? LEU B 11  GLN B 13  
AA3 2 THR B 124 ? SER B 129 ? THR B 122 SER B 127 
AA3 3 ALA B 94  ? THR B 101 ? ALA B 92  THR B 99  
AA3 4 TYR B 119 ? TRP B 120 ? TYR B 117 TRP B 118 
# 
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 VAL B 7   ? N VAL B 5   O ALA B 25  ? O ALA B 23  
AA1 2 3 N LEU B 20  ? N LEU B 18  O MET B 85  ? O MET B 83  
AA1 3 4 O TYR B 82  ? O TYR B 80  N SER B 73  ? N SER B 71  
AA2 1 2 N VAL B 14  ? N VAL B 12  O THR B 127 ? O THR B 125 
AA2 2 3 O THR B 124 ? O THR B 122 N TYR B 96  ? N TYR B 94  
AA2 3 4 O SER B 97  ? O SER B 95  N PHE B 39  ? N PHE B 37  
AA2 4 5 N TRP B 38  ? N TRP B 36  O ALA B 51  ? O ALA B 49  
AA2 5 6 N ARG B 52  ? N ARG B 50  O ASP B 61  ? O ASP B 59  
AA3 1 2 N VAL B 14  ? N VAL B 12  O THR B 127 ? O THR B 125 
AA3 2 3 O THR B 124 ? O THR B 122 N TYR B 96  ? N TYR B 94  
AA3 3 4 N ALA B 100 ? N ALA B 98  O TYR B 119 ? O TYR B 117 
# 
_pdbx_entry_details.entry_id                   9G95 
_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     N 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER B 25 ? ? -93.28  -158.95 
2 1 ARG B 27 ? ? -140.04 -68.46  
3 1 VAL B 48 ? ? -120.92 -61.95  
4 1 SER B 54 ? ? -115.86 -93.72  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 0   ? A MET 1   
2  1 Y 1 A GLU 419 ? A GLU 420 
3  1 Y 1 A ASN 420 ? A ASN 421 
4  1 Y 1 A LEU 421 ? A LEU 422 
5  1 Y 1 A TYR 422 ? A TYR 423 
6  1 Y 1 A PHE 423 ? A PHE 424 
7  1 Y 1 A GLN 424 ? A GLN 425 
8  1 Y 1 B MET -1  ? B MET 1   
9  1 Y 1 B ALA 0   ? B ALA 2   
10 1 Y 1 B GLN 1   ? B GLN 3   
11 1 Y 1 B VAL 2   ? B VAL 4   
12 1 Y 1 B SER 128 ? B SER 130 
13 1 Y 1 B HIS 129 ? B HIS 131 
14 1 Y 1 B HIS 130 ? B HIS 132 
15 1 Y 1 B HIS 131 ? B HIS 133 
16 1 Y 1 B HIS 132 ? B HIS 134 
17 1 Y 1 B HIS 133 ? B HIS 135 
18 1 Y 1 B HIS 134 ? B HIS 136 
19 1 Y 1 B GLU 135 ? B GLU 137 
20 1 Y 1 B PRO 136 ? B PRO 138 
21 1 Y 1 B GLU 137 ? B GLU 139 
22 1 Y 1 B ALA 138 ? B ALA 140 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
ILE N    N  N N 159 
ILE CA   C  N S 160 
ILE C    C  N N 161 
ILE O    O  N N 162 
ILE CB   C  N S 163 
ILE CG1  C  N N 164 
ILE CG2  C  N N 165 
ILE CD1  C  N N 166 
ILE OXT  O  N N 167 
ILE H    H  N N 168 
ILE H2   H  N N 169 
ILE HA   H  N N 170 
ILE HB   H  N N 171 
ILE HG12 H  N N 172 
ILE HG13 H  N N 173 
ILE HG21 H  N N 174 
ILE HG22 H  N N 175 
ILE HG23 H  N N 176 
ILE HD11 H  N N 177 
ILE HD12 H  N N 178 
ILE HD13 H  N N 179 
ILE HXT  H  N N 180 
LEU N    N  N N 181 
LEU CA   C  N S 182 
LEU C    C  N N 183 
LEU O    O  N N 184 
LEU CB   C  N N 185 
LEU CG   C  N N 186 
LEU CD1  C  N N 187 
LEU CD2  C  N N 188 
LEU OXT  O  N N 189 
LEU H    H  N N 190 
LEU H2   H  N N 191 
LEU HA   H  N N 192 
LEU HB2  H  N N 193 
LEU HB3  H  N N 194 
LEU HG   H  N N 195 
LEU HD11 H  N N 196 
LEU HD12 H  N N 197 
LEU HD13 H  N N 198 
LEU HD21 H  N N 199 
LEU HD22 H  N N 200 
LEU HD23 H  N N 201 
LEU HXT  H  N N 202 
LYS N    N  N N 203 
LYS CA   C  N S 204 
LYS C    C  N N 205 
LYS O    O  N N 206 
LYS CB   C  N N 207 
LYS CG   C  N N 208 
LYS CD   C  N N 209 
LYS CE   C  N N 210 
LYS NZ   N  N N 211 
LYS OXT  O  N N 212 
LYS H    H  N N 213 
LYS H2   H  N N 214 
LYS HA   H  N N 215 
LYS HB2  H  N N 216 
LYS HB3  H  N N 217 
LYS HG2  H  N N 218 
LYS HG3  H  N N 219 
LYS HD2  H  N N 220 
LYS HD3  H  N N 221 
LYS HE2  H  N N 222 
LYS HE3  H  N N 223 
LYS HZ1  H  N N 224 
LYS HZ2  H  N N 225 
LYS HZ3  H  N N 226 
LYS HXT  H  N N 227 
MET N    N  N N 228 
MET CA   C  N S 229 
MET C    C  N N 230 
MET O    O  N N 231 
MET CB   C  N N 232 
MET CG   C  N N 233 
MET SD   S  N N 234 
MET CE   C  N N 235 
MET OXT  O  N N 236 
MET H    H  N N 237 
MET H2   H  N N 238 
MET HA   H  N N 239 
MET HB2  H  N N 240 
MET HB3  H  N N 241 
MET HG2  H  N N 242 
MET HG3  H  N N 243 
MET HE1  H  N N 244 
MET HE2  H  N N 245 
MET HE3  H  N N 246 
MET HXT  H  N N 247 
MPG C2   C  N N 248 
MPG C3   C  N N 249 
MPG C4   C  N N 250 
MPG C5   C  N N 251 
MPG C6   C  N N 252 
MPG C7   C  N N 253 
MPG C8   C  N N 254 
MPG C9   C  N N 255 
MPG C10  C  N N 256 
MPG C11  C  N N 257 
MPG C12  C  N N 258 
MPG C13  C  N N 259 
MPG C14  C  N N 260 
MPG C15  C  N N 261 
MPG C16  C  N N 262 
MPG C17  C  N N 263 
MPG C18  C  N N 264 
MPG O1   O  N N 265 
MPG C1   C  N N 266 
MPG CXD  C  N R 267 
MPG O2   O  N N 268 
MPG C21  C  N N 269 
MPG O3   O  N N 270 
MPG O4   O  N N 271 
MPG CX3  C  N N 272 
MPG H21C H  N N 273 
MPG H22C H  N N 274 
MPG H31C H  N N 275 
MPG H32C H  N N 276 
MPG H41C H  N N 277 
MPG H42C H  N N 278 
MPG H51C H  N N 279 
MPG H52C H  N N 280 
MPG H61C H  N N 281 
MPG H62C H  N N 282 
MPG H71C H  N N 283 
MPG H72C H  N N 284 
MPG H81C H  N N 285 
MPG H82C H  N N 286 
MPG H9   H  N N 287 
MPG H10  H  N N 288 
MPG H111 H  N N 289 
MPG H112 H  N N 290 
MPG H121 H  N N 291 
MPG H122 H  N N 292 
MPG H131 H  N N 293 
MPG H132 H  N N 294 
MPG H141 H  N N 295 
MPG H142 H  N N 296 
MPG H151 H  N N 297 
MPG H152 H  N N 298 
MPG H161 H  N N 299 
MPG H162 H  N N 300 
MPG H171 H  N N 301 
MPG H172 H  N N 302 
MPG H181 H  N N 303 
MPG H182 H  N N 304 
MPG H183 H  N N 305 
MPG HX31 H  N N 306 
MPG HX32 H  N N 307 
MPG HXD  H  N N 308 
MPG H2   H  N N 309 
MPG H211 H  N N 310 
MPG H212 H  N N 311 
MPG H3   H  N N 312 
OCT C1   C  N N 313 
OCT C2   C  N N 314 
OCT C3   C  N N 315 
OCT C4   C  N N 316 
OCT C5   C  N N 317 
OCT C6   C  N N 318 
OCT C7   C  N N 319 
OCT C8   C  N N 320 
OCT H11  H  N N 321 
OCT H12  H  N N 322 
OCT H13  H  N N 323 
OCT H21  H  N N 324 
OCT H22  H  N N 325 
OCT H31  H  N N 326 
OCT H32  H  N N 327 
OCT H41  H  N N 328 
OCT H42  H  N N 329 
OCT H51  H  N N 330 
OCT H52  H  N N 331 
OCT H61  H  N N 332 
OCT H62  H  N N 333 
OCT H71  H  N N 334 
OCT H72  H  N N 335 
OCT H81  H  N N 336 
OCT H82  H  N N 337 
OCT H83  H  N N 338 
PHE N    N  N N 339 
PHE CA   C  N S 340 
PHE C    C  N N 341 
PHE O    O  N N 342 
PHE CB   C  N N 343 
PHE CG   C  Y N 344 
PHE CD1  C  Y N 345 
PHE CD2  C  Y N 346 
PHE CE1  C  Y N 347 
PHE CE2  C  Y N 348 
PHE CZ   C  Y N 349 
PHE OXT  O  N N 350 
PHE H    H  N N 351 
PHE H2   H  N N 352 
PHE HA   H  N N 353 
PHE HB2  H  N N 354 
PHE HB3  H  N N 355 
PHE HD1  H  N N 356 
PHE HD2  H  N N 357 
PHE HE1  H  N N 358 
PHE HE2  H  N N 359 
PHE HZ   H  N N 360 
PHE HXT  H  N N 361 
PRO N    N  N N 362 
PRO CA   C  N S 363 
PRO C    C  N N 364 
PRO O    O  N N 365 
PRO CB   C  N N 366 
PRO CG   C  N N 367 
PRO CD   C  N N 368 
PRO OXT  O  N N 369 
PRO H    H  N N 370 
PRO HA   H  N N 371 
PRO HB2  H  N N 372 
PRO HB3  H  N N 373 
PRO HG2  H  N N 374 
PRO HG3  H  N N 375 
PRO HD2  H  N N 376 
PRO HD3  H  N N 377 
PRO HXT  H  N N 378 
SER N    N  N N 379 
SER CA   C  N S 380 
SER C    C  N N 381 
SER O    O  N N 382 
SER CB   C  N N 383 
SER OG   O  N N 384 
SER OXT  O  N N 385 
SER H    H  N N 386 
SER H2   H  N N 387 
SER HA   H  N N 388 
SER HB2  H  N N 389 
SER HB3  H  N N 390 
SER HG   H  N N 391 
SER HXT  H  N N 392 
SO4 S    S  N N 393 
SO4 O1   O  N N 394 
SO4 O2   O  N N 395 
SO4 O3   O  N N 396 
SO4 O4   O  N N 397 
THR N    N  N N 398 
THR CA   C  N S 399 
THR C    C  N N 400 
THR O    O  N N 401 
THR CB   C  N R 402 
THR OG1  O  N N 403 
THR CG2  C  N N 404 
THR OXT  O  N N 405 
THR H    H  N N 406 
THR H2   H  N N 407 
THR HA   H  N N 408 
THR HB   H  N N 409 
THR HG1  H  N N 410 
THR HG21 H  N N 411 
THR HG22 H  N N 412 
THR HG23 H  N N 413 
THR HXT  H  N N 414 
TRP N    N  N N 415 
TRP CA   C  N S 416 
TRP C    C  N N 417 
TRP O    O  N N 418 
TRP CB   C  N N 419 
TRP CG   C  Y N 420 
TRP CD1  C  Y N 421 
TRP CD2  C  Y N 422 
TRP NE1  N  Y N 423 
TRP CE2  C  Y N 424 
TRP CE3  C  Y N 425 
TRP CZ2  C  Y N 426 
TRP CZ3  C  Y N 427 
TRP CH2  C  Y N 428 
TRP OXT  O  N N 429 
TRP H    H  N N 430 
TRP H2   H  N N 431 
TRP HA   H  N N 432 
TRP HB2  H  N N 433 
TRP HB3  H  N N 434 
TRP HD1  H  N N 435 
TRP HE1  H  N N 436 
TRP HE3  H  N N 437 
TRP HZ2  H  N N 438 
TRP HZ3  H  N N 439 
TRP HH2  H  N N 440 
TRP HXT  H  N N 441 
TYR N    N  N N 442 
TYR CA   C  N S 443 
TYR C    C  N N 444 
TYR O    O  N N 445 
TYR CB   C  N N 446 
TYR CG   C  Y N 447 
TYR CD1  C  Y N 448 
TYR CD2  C  Y N 449 
TYR CE1  C  Y N 450 
TYR CE2  C  Y N 451 
TYR CZ   C  Y N 452 
TYR OH   O  N N 453 
TYR OXT  O  N N 454 
TYR H    H  N N 455 
TYR H2   H  N N 456 
TYR HA   H  N N 457 
TYR HB2  H  N N 458 
TYR HB3  H  N N 459 
TYR HD1  H  N N 460 
TYR HD2  H  N N 461 
TYR HE1  H  N N 462 
TYR HE2  H  N N 463 
TYR HH   H  N N 464 
TYR HXT  H  N N 465 
VAL N    N  N N 466 
VAL CA   C  N S 467 
VAL C    C  N N 468 
VAL O    O  N N 469 
VAL CB   C  N N 470 
VAL CG1  C  N N 471 
VAL CG2  C  N N 472 
VAL OXT  O  N N 473 
VAL H    H  N N 474 
VAL H2   H  N N 475 
VAL HA   H  N N 476 
VAL HB   H  N N 477 
VAL HG11 H  N N 478 
VAL HG12 H  N N 479 
VAL HG13 H  N N 480 
VAL HG21 H  N N 481 
VAL HG22 H  N N 482 
VAL HG23 H  N N 483 
VAL HXT  H  N N 484 
ZN  ZN   ZN N N 485 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
MPG C2  C3   sing N N 235 
MPG C2  C1   sing N N 236 
MPG C3  C4   sing N N 237 
MPG C4  C5   sing N N 238 
MPG C5  C6   sing N N 239 
MPG C6  C7   sing N N 240 
MPG C7  C8   sing N N 241 
MPG C8  C9   sing N N 242 
MPG C9  C10  doub N Z 243 
MPG C10 C11  sing N N 244 
MPG C11 C12  sing N N 245 
MPG C12 C13  sing N N 246 
MPG C13 C14  sing N N 247 
MPG C14 C15  sing N N 248 
MPG C15 C16  sing N N 249 
MPG C16 C17  sing N N 250 
MPG C17 C18  sing N N 251 
MPG O1  C1   sing N N 252 
MPG O1  CX3  sing N N 253 
MPG CXD O2   sing N N 254 
MPG CXD C21  sing N N 255 
MPG CXD CX3  sing N N 256 
MPG C21 O3   sing N N 257 
MPG C2  H21C sing N N 258 
MPG C2  H22C sing N N 259 
MPG C3  H31C sing N N 260 
MPG C3  H32C sing N N 261 
MPG CX3 O4   doub N N 262 
MPG C4  H41C sing N N 263 
MPG C4  H42C sing N N 264 
MPG C5  H51C sing N N 265 
MPG C5  H52C sing N N 266 
MPG C6  H61C sing N N 267 
MPG C6  H62C sing N N 268 
MPG C7  H71C sing N N 269 
MPG C7  H72C sing N N 270 
MPG C8  H81C sing N N 271 
MPG C8  H82C sing N N 272 
MPG C9  H9   sing N N 273 
MPG C10 H10  sing N N 274 
MPG C11 H111 sing N N 275 
MPG C11 H112 sing N N 276 
MPG C12 H121 sing N N 277 
MPG C12 H122 sing N N 278 
MPG C13 H131 sing N N 279 
MPG C13 H132 sing N N 280 
MPG C14 H141 sing N N 281 
MPG C14 H142 sing N N 282 
MPG C15 H151 sing N N 283 
MPG C15 H152 sing N N 284 
MPG C16 H161 sing N N 285 
MPG C16 H162 sing N N 286 
MPG C17 H171 sing N N 287 
MPG C17 H172 sing N N 288 
MPG C18 H181 sing N N 289 
MPG C18 H182 sing N N 290 
MPG C18 H183 sing N N 291 
MPG C1  HX31 sing N N 292 
MPG C1  HX32 sing N N 293 
MPG CXD HXD  sing N N 294 
MPG O2  H2   sing N N 295 
MPG C21 H211 sing N N 296 
MPG C21 H212 sing N N 297 
MPG O3  H3   sing N N 298 
OCT C1  C2   sing N N 299 
OCT C1  H11  sing N N 300 
OCT C1  H12  sing N N 301 
OCT C1  H13  sing N N 302 
OCT C2  C3   sing N N 303 
OCT C2  H21  sing N N 304 
OCT C2  H22  sing N N 305 
OCT C3  C4   sing N N 306 
OCT C3  H31  sing N N 307 
OCT C3  H32  sing N N 308 
OCT C4  C5   sing N N 309 
OCT C4  H41  sing N N 310 
OCT C4  H42  sing N N 311 
OCT C5  C6   sing N N 312 
OCT C5  H51  sing N N 313 
OCT C5  H52  sing N N 314 
OCT C6  C7   sing N N 315 
OCT C6  H61  sing N N 316 
OCT C6  H62  sing N N 317 
OCT C7  C8   sing N N 318 
OCT C7  H71  sing N N 319 
OCT C7  H72  sing N N 320 
OCT C8  H81  sing N N 321 
OCT C8  H82  sing N N 322 
OCT C8  H83  sing N N 323 
PHE N   CA   sing N N 324 
PHE N   H    sing N N 325 
PHE N   H2   sing N N 326 
PHE CA  C    sing N N 327 
PHE CA  CB   sing N N 328 
PHE CA  HA   sing N N 329 
PHE C   O    doub N N 330 
PHE C   OXT  sing N N 331 
PHE CB  CG   sing N N 332 
PHE CB  HB2  sing N N 333 
PHE CB  HB3  sing N N 334 
PHE CG  CD1  doub Y N 335 
PHE CG  CD2  sing Y N 336 
PHE CD1 CE1  sing Y N 337 
PHE CD1 HD1  sing N N 338 
PHE CD2 CE2  doub Y N 339 
PHE CD2 HD2  sing N N 340 
PHE CE1 CZ   doub Y N 341 
PHE CE1 HE1  sing N N 342 
PHE CE2 CZ   sing Y N 343 
PHE CE2 HE2  sing N N 344 
PHE CZ  HZ   sing N N 345 
PHE OXT HXT  sing N N 346 
PRO N   CA   sing N N 347 
PRO N   CD   sing N N 348 
PRO N   H    sing N N 349 
PRO CA  C    sing N N 350 
PRO CA  CB   sing N N 351 
PRO CA  HA   sing N N 352 
PRO C   O    doub N N 353 
PRO C   OXT  sing N N 354 
PRO CB  CG   sing N N 355 
PRO CB  HB2  sing N N 356 
PRO CB  HB3  sing N N 357 
PRO CG  CD   sing N N 358 
PRO CG  HG2  sing N N 359 
PRO CG  HG3  sing N N 360 
PRO CD  HD2  sing N N 361 
PRO CD  HD3  sing N N 362 
PRO OXT HXT  sing N N 363 
SER N   CA   sing N N 364 
SER N   H    sing N N 365 
SER N   H2   sing N N 366 
SER CA  C    sing N N 367 
SER CA  CB   sing N N 368 
SER CA  HA   sing N N 369 
SER C   O    doub N N 370 
SER C   OXT  sing N N 371 
SER CB  OG   sing N N 372 
SER CB  HB2  sing N N 373 
SER CB  HB3  sing N N 374 
SER OG  HG   sing N N 375 
SER OXT HXT  sing N N 376 
SO4 S   O1   doub N N 377 
SO4 S   O2   doub N N 378 
SO4 S   O3   sing N N 379 
SO4 S   O4   sing N N 380 
THR N   CA   sing N N 381 
THR N   H    sing N N 382 
THR N   H2   sing N N 383 
THR CA  C    sing N N 384 
THR CA  CB   sing N N 385 
THR CA  HA   sing N N 386 
THR C   O    doub N N 387 
THR C   OXT  sing N N 388 
THR CB  OG1  sing N N 389 
THR CB  CG2  sing N N 390 
THR CB  HB   sing N N 391 
THR OG1 HG1  sing N N 392 
THR CG2 HG21 sing N N 393 
THR CG2 HG22 sing N N 394 
THR CG2 HG23 sing N N 395 
THR OXT HXT  sing N N 396 
TRP N   CA   sing N N 397 
TRP N   H    sing N N 398 
TRP N   H2   sing N N 399 
TRP CA  C    sing N N 400 
TRP CA  CB   sing N N 401 
TRP CA  HA   sing N N 402 
TRP C   O    doub N N 403 
TRP C   OXT  sing N N 404 
TRP CB  CG   sing N N 405 
TRP CB  HB2  sing N N 406 
TRP CB  HB3  sing N N 407 
TRP CG  CD1  doub Y N 408 
TRP CG  CD2  sing Y N 409 
TRP CD1 NE1  sing Y N 410 
TRP CD1 HD1  sing N N 411 
TRP CD2 CE2  doub Y N 412 
TRP CD2 CE3  sing Y N 413 
TRP NE1 CE2  sing Y N 414 
TRP NE1 HE1  sing N N 415 
TRP CE2 CZ2  sing Y N 416 
TRP CE3 CZ3  doub Y N 417 
TRP CE3 HE3  sing N N 418 
TRP CZ2 CH2  doub Y N 419 
TRP CZ2 HZ2  sing N N 420 
TRP CZ3 CH2  sing Y N 421 
TRP CZ3 HZ3  sing N N 422 
TRP CH2 HH2  sing N N 423 
TRP OXT HXT  sing N N 424 
TYR N   CA   sing N N 425 
TYR N   H    sing N N 426 
TYR N   H2   sing N N 427 
TYR CA  C    sing N N 428 
TYR CA  CB   sing N N 429 
TYR CA  HA   sing N N 430 
TYR C   O    doub N N 431 
TYR C   OXT  sing N N 432 
TYR CB  CG   sing N N 433 
TYR CB  HB2  sing N N 434 
TYR CB  HB3  sing N N 435 
TYR CG  CD1  doub Y N 436 
TYR CG  CD2  sing Y N 437 
TYR CD1 CE1  sing Y N 438 
TYR CD1 HD1  sing N N 439 
TYR CD2 CE2  doub Y N 440 
TYR CD2 HD2  sing N N 441 
TYR CE1 CZ   doub Y N 442 
TYR CE1 HE1  sing N N 443 
TYR CE2 CZ   sing Y N 444 
TYR CE2 HE2  sing N N 445 
TYR CZ  OH   sing N N 446 
TYR OH  HH   sing N N 447 
TYR OXT HXT  sing N N 448 
VAL N   CA   sing N N 449 
VAL N   H    sing N N 450 
VAL N   H2   sing N N 451 
VAL CA  C    sing N N 452 
VAL CA  CB   sing N N 453 
VAL CA  HA   sing N N 454 
VAL C   O    doub N N 455 
VAL C   OXT  sing N N 456 
VAL CB  CG1  sing N N 457 
VAL CB  CG2  sing N N 458 
VAL CB  HB   sing N N 459 
VAL CG1 HG11 sing N N 460 
VAL CG1 HG12 sing N N 461 
VAL CG1 HG13 sing N N 462 
VAL CG2 HG21 sing N N 463 
VAL CG2 HG22 sing N N 464 
VAL CG2 HG23 sing N N 465 
VAL OXT HXT  sing N N 466 
# 
_pdbx_audit_support.funding_organization   'Wellcome Trust' 
_pdbx_audit_support.country                'United Kingdom' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9G95 
_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]   0.003683 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000199 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.026008 
_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]   0.017582 
_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  
CL 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . VAL A 1 2   ? 70.003  5.593   13.550  1.00 56.05  ? 1   VAL A N   1 
ATOM   2    C  CA  . VAL A 1 2   ? 71.442  5.787   13.429  1.00 59.21  ? 1   VAL A CA  1 
ATOM   3    C  C   . VAL A 1 2   ? 71.920  6.670   14.580  1.00 60.40  ? 1   VAL A C   1 
ATOM   4    O  O   . VAL A 1 2   ? 71.151  7.464   15.121  1.00 59.08  ? 1   VAL A O   1 
ATOM   5    C  CB  . VAL A 1 2   ? 71.798  6.393   12.050  1.00 48.40  ? 1   VAL A CB  1 
ATOM   6    C  CG1 . VAL A 1 2   ? 73.306  6.504   11.860  1.00 63.12  ? 1   VAL A CG1 1 
ATOM   7    C  CG2 . VAL A 1 2   ? 71.189  5.552   10.940  1.00 62.56  ? 1   VAL A CG2 1 
ATOM   8    N  N   . SER A 1 3   ? 73.191  6.536   14.947  1.00 47.95  ? 2   SER A N   1 
ATOM   9    C  CA  . SER A 1 3   ? 73.725  7.223   16.114  1.00 52.71  ? 2   SER A CA  1 
ATOM   10   C  C   . SER A 1 3   ? 75.227  7.397   15.940  1.00 51.68  ? 2   SER A C   1 
ATOM   11   O  O   . SER A 1 3   ? 75.849  6.792   15.063  1.00 52.80  ? 2   SER A O   1 
ATOM   12   C  CB  . SER A 1 3   ? 73.409  6.460   17.405  1.00 55.67  ? 2   SER A CB  1 
ATOM   13   O  OG  . SER A 1 3   ? 74.459  5.571   17.746  1.00 58.08  ? 2   SER A OG  1 
ATOM   14   N  N   . LEU A 1 4   ? 75.800  8.241   16.799  1.00 46.89  ? 3   LEU A N   1 
ATOM   15   C  CA  . LEU A 1 4   ? 77.242  8.459   16.787  1.00 44.17  ? 3   LEU A CA  1 
ATOM   16   C  C   . LEU A 1 4   ? 77.996  7.202   17.197  1.00 49.42  ? 3   LEU A C   1 
ATOM   17   O  O   . LEU A 1 4   ? 79.099  6.951   16.699  1.00 49.39  ? 3   LEU A O   1 
ATOM   18   C  CB  . LEU A 1 4   ? 77.601  9.622   17.710  1.00 43.83  ? 3   LEU A CB  1 
ATOM   19   C  CG  . LEU A 1 4   ? 79.059  10.083  17.757  1.00 43.03  ? 3   LEU A CG  1 
ATOM   20   C  CD1 . LEU A 1 4   ? 79.582  10.381  16.358  1.00 46.79  ? 3   LEU A CD1 1 
ATOM   21   C  CD2 . LEU A 1 4   ? 79.207  11.297  18.661  1.00 39.99  ? 3   LEU A CD2 1 
ATOM   22   N  N   . ALA A 1 5   ? 77.421  6.410   18.105  1.00 49.68  ? 4   ALA A N   1 
ATOM   23   C  CA  . ALA A 1 5   ? 78.076  5.189   18.562  1.00 49.52  ? 4   ALA A CA  1 
ATOM   24   C  C   . ALA A 1 5   ? 78.169  4.163   17.439  1.00 53.88  ? 4   ALA A C   1 
ATOM   25   O  O   . ALA A 1 5   ? 79.250  3.630   17.162  1.00 49.52  ? 4   ALA A O   1 
ATOM   26   C  CB  . ALA A 1 5   ? 77.328  4.616   19.767  1.00 51.14  ? 4   ALA A CB  1 
ATOM   27   N  N   . LYS A 1 6   ? 77.041  3.870   16.780  1.00 51.64  ? 5   LYS A N   1 
ATOM   28   C  CA  . LYS A 1 6   ? 77.058  2.916   15.674  1.00 51.34  ? 5   LYS A CA  1 
ATOM   29   C  C   . LYS A 1 6   ? 77.972  3.386   14.550  1.00 47.56  ? 5   LYS A C   1 
ATOM   30   O  O   . LYS A 1 6   ? 78.675  2.575   13.934  1.00 56.22  ? 5   LYS A O   1 
ATOM   31   C  CB  . LYS A 1 6   ? 75.644  2.687   15.138  1.00 56.87  ? 5   LYS A CB  1 
ATOM   32   C  CG  . LYS A 1 6   ? 74.650  2.157   16.155  1.00 50.74  ? 5   LYS A CG  1 
ATOM   33   C  CD  . LYS A 1 6   ? 73.326  2.893   16.046  1.00 62.67  ? 5   LYS A CD  1 
ATOM   34   C  CE  . LYS A 1 6   ? 72.170  1.929   15.863  1.00 72.45  ? 5   LYS A CE  1 
ATOM   35   N  NZ  . LYS A 1 6   ? 70.892  2.496   16.372  1.00 77.90  ? 5   LYS A NZ  1 
ATOM   36   N  N   . ALA A 1 7   ? 77.965  4.688   14.253  1.00 42.73  ? 6   ALA A N   1 
ATOM   37   C  CA  . ALA A 1 7   ? 78.860  5.206   13.224  1.00 48.26  ? 6   ALA A CA  1 
ATOM   38   C  C   . ALA A 1 7   ? 80.317  5.008   13.621  1.00 47.01  ? 6   ALA A C   1 
ATOM   39   O  O   . ALA A 1 7   ? 81.168  4.723   12.770  1.00 43.07  ? 6   ALA A O   1 
ATOM   40   C  CB  . ALA A 1 7   ? 78.568  6.682   12.957  1.00 44.89  ? 6   ALA A CB  1 
ATOM   41   N  N   . SER A 1 8   ? 80.623  5.156   14.913  1.00 46.59  ? 7   SER A N   1 
ATOM   42   C  CA  . SER A 1 8   ? 81.981  4.912   15.384  1.00 44.45  ? 7   SER A CA  1 
ATOM   43   C  C   . SER A 1 8   ? 82.375  3.452   15.207  1.00 48.96  ? 7   SER A C   1 
ATOM   44   O  O   . SER A 1 8   ? 83.546  3.153   14.949  1.00 45.67  ? 7   SER A O   1 
ATOM   45   C  CB  . SER A 1 8   ? 82.115  5.329   16.848  1.00 41.98  ? 7   SER A CB  1 
ATOM   46   O  OG  . SER A 1 8   ? 81.901  6.722   17.001  1.00 49.11  ? 7   SER A OG  1 
ATOM   47   N  N   . LEU A 1 9   ? 81.418  2.533   15.351  1.00 48.09  ? 8   LEU A N   1 
ATOM   48   C  CA  . LEU A 1 9   ? 81.716  1.112   15.199  1.00 49.70  ? 8   LEU A CA  1 
ATOM   49   C  C   . LEU A 1 9   ? 82.088  0.779   13.759  1.00 48.20  ? 8   LEU A C   1 
ATOM   50   O  O   . LEU A 1 9   ? 83.065  0.064   13.507  1.00 47.11  ? 8   LEU A O   1 
ATOM   51   C  CB  . LEU A 1 9   ? 80.516  0.279   15.651  1.00 47.75  ? 8   LEU A CB  1 
ATOM   52   C  CG  . LEU A 1 9   ? 80.802  -1.122  16.189  1.00 55.67  ? 8   LEU A CG  1 
ATOM   53   C  CD1 . LEU A 1 9   ? 81.908  -1.081  17.233  1.00 53.74  ? 8   LEU A CD1 1 
ATOM   54   C  CD2 . LEU A 1 9   ? 79.536  -1.735  16.763  1.00 53.86  ? 8   LEU A CD2 1 
ATOM   55   N  N   . TRP A 1 10  ? 81.311  1.286   12.799  1.00 43.82  ? 9   TRP A N   1 
ATOM   56   C  CA  . TRP A 1 10  ? 81.663  1.127   11.391  1.00 43.94  ? 9   TRP A CA  1 
ATOM   57   C  C   . TRP A 1 10  ? 82.985  1.810   11.068  1.00 41.07  ? 9   TRP A C   1 
ATOM   58   O  O   . TRP A 1 10  ? 83.877  1.208   10.458  1.00 42.98  ? 9   TRP A O   1 
ATOM   59   C  CB  . TRP A 1 10  ? 80.550  1.690   10.505  1.00 45.57  ? 9   TRP A CB  1 
ATOM   60   C  CG  . TRP A 1 10  ? 79.402  0.761   10.283  1.00 44.00  ? 9   TRP A CG  1 
ATOM   61   C  CD1 . TRP A 1 10  ? 78.141  0.873   10.794  1.00 45.92  ? 9   TRP A CD1 1 
ATOM   62   C  CD2 . TRP A 1 10  ? 79.402  -0.417  9.470   1.00 48.43  ? 9   TRP A CD2 1 
ATOM   63   N  NE1 . TRP A 1 10  ? 77.359  -0.168  10.356  1.00 46.08  ? 9   TRP A NE1 1 
ATOM   64   C  CE2 . TRP A 1 10  ? 78.110  -0.974  9.541   1.00 47.51  ? 9   TRP A CE2 1 
ATOM   65   C  CE3 . TRP A 1 10  ? 80.371  -1.057  8.692   1.00 46.36  ? 9   TRP A CE3 1 
ATOM   66   C  CZ2 . TRP A 1 10  ? 77.762  -2.141  8.865   1.00 48.92  ? 9   TRP A CZ2 1 
ATOM   67   C  CZ3 . TRP A 1 10  ? 80.024  -2.214  8.021   1.00 42.08  ? 9   TRP A CZ3 1 
ATOM   68   C  CH2 . TRP A 1 10  ? 78.732  -2.744  8.111   1.00 50.19  ? 9   TRP A CH2 1 
ATOM   69   N  N   . THR A 1 11  ? 83.129  3.073   11.473  1.00 46.26  ? 10  THR A N   1 
ATOM   70   C  CA  . THR A 1 11  ? 84.306  3.847   11.094  1.00 43.33  ? 10  THR A CA  1 
ATOM   71   C  C   . THR A 1 11  ? 85.582  3.318   11.739  1.00 42.20  ? 10  THR A C   1 
ATOM   72   O  O   . THR A 1 11  ? 86.660  3.422   11.142  1.00 43.23  ? 10  THR A O   1 
ATOM   73   C  CB  . THR A 1 11  ? 84.100  5.317   11.460  1.00 41.66  ? 10  THR A CB  1 
ATOM   74   O  OG1 . THR A 1 11  ? 82.799  5.738   11.033  1.00 42.32  ? 10  THR A OG1 1 
ATOM   75   C  CG2 . THR A 1 11  ? 85.127  6.172   10.759  1.00 33.64  ? 10  THR A CG2 1 
ATOM   76   N  N   . ALA A 1 12  ? 85.491  2.751   12.945  1.00 45.14  ? 11  ALA A N   1 
ATOM   77   C  CA  . ALA A 1 12  ? 86.679  2.173   13.568  1.00 44.01  ? 11  ALA A CA  1 
ATOM   78   C  C   . ALA A 1 12  ? 87.202  0.986   12.771  1.00 43.26  ? 11  ALA A C   1 
ATOM   79   O  O   . ALA A 1 12  ? 88.418  0.812   12.627  1.00 43.13  ? 11  ALA A O   1 
ATOM   80   C  CB  . ALA A 1 12  ? 86.375  1.759   15.008  1.00 33.47  ? 11  ALA A CB  1 
ATOM   81   N  N   . ALA A 1 13  ? 86.298  0.159   12.241  1.00 40.43  ? 12  ALA A N   1 
ATOM   82   C  CA  . ALA A 1 13  ? 86.722  -0.991  11.451  1.00 41.65  ? 12  ALA A CA  1 
ATOM   83   C  C   . ALA A 1 13  ? 87.444  -0.561  10.180  1.00 42.35  ? 12  ALA A C   1 
ATOM   84   O  O   . ALA A 1 13  ? 88.486  -1.127  9.828   1.00 44.24  ? 12  ALA A O   1 
ATOM   85   C  CB  . ALA A 1 13  ? 85.516  -1.869  11.113  1.00 44.56  ? 12  ALA A CB  1 
ATOM   86   N  N   . SER A 1 14  ? 86.914  0.446   9.482   1.00 39.26  ? 13  SER A N   1 
ATOM   87   C  CA  . SER A 1 14  ? 87.568  0.921   8.266   1.00 37.09  ? 13  SER A CA  1 
ATOM   88   C  C   . SER A 1 14  ? 88.887  1.624   8.567   1.00 34.96  ? 13  SER A C   1 
ATOM   89   O  O   . SER A 1 14  ? 89.864  1.456   7.828   1.00 41.00  ? 13  SER A O   1 
ATOM   90   C  CB  . SER A 1 14  ? 86.632  1.853   7.496   1.00 38.40  ? 13  SER A CB  1 
ATOM   91   O  OG  . SER A 1 14  ? 86.226  2.949   8.297   1.00 47.95  ? 13  SER A OG  1 
ATOM   92   N  N   . THR A 1 15  ? 88.941  2.415   9.642   1.00 37.53  ? 14  THR A N   1 
ATOM   93   C  CA  . THR A 1 15  ? 90.183  3.106   9.978   1.00 41.57  ? 14  THR A CA  1 
ATOM   94   C  C   . THR A 1 15  ? 91.269  2.128   10.408  1.00 46.13  ? 14  THR A C   1 
ATOM   95   O  O   . THR A 1 15  ? 92.448  2.319   10.086  1.00 48.40  ? 14  THR A O   1 
ATOM   96   C  CB  . THR A 1 15  ? 89.934  4.140   11.075  1.00 40.55  ? 14  THR A CB  1 
ATOM   97   O  OG1 . THR A 1 15  ? 88.822  4.967   10.711  1.00 50.90  ? 14  THR A OG1 1 
ATOM   98   C  CG2 . THR A 1 15  ? 91.160  5.021   11.255  1.00 42.36  ? 14  THR A CG2 1 
ATOM   99   N  N   . LEU A 1 16  ? 90.890  1.067   11.125  1.00 45.60  ? 15  LEU A N   1 
ATOM   100  C  CA  . LEU A 1 16  ? 91.871  0.077   11.558  1.00 47.86  ? 15  LEU A CA  1 
ATOM   101  C  C   . LEU A 1 16  ? 92.468  -0.665  10.369  1.00 51.02  ? 15  LEU A C   1 
ATOM   102  O  O   . LEU A 1 16  ? 93.666  -0.974  10.361  1.00 50.91  ? 15  LEU A O   1 
ATOM   103  C  CB  . LEU A 1 16  ? 91.235  -0.903  12.545  1.00 46.72  ? 15  LEU A CB  1 
ATOM   104  C  CG  . LEU A 1 16  ? 91.133  -0.430  13.998  1.00 43.45  ? 15  LEU A CG  1 
ATOM   105  C  CD1 . LEU A 1 16  ? 90.347  -1.422  14.842  1.00 42.61  ? 15  LEU A CD1 1 
ATOM   106  C  CD2 . LEU A 1 16  ? 92.518  -0.206  14.585  1.00 36.27  ? 15  LEU A CD2 1 
ATOM   107  N  N   . VAL A 1 17  ? 91.649  -0.963  9.358   1.00 50.57  ? 16  VAL A N   1 
ATOM   108  C  CA  . VAL A 1 17  ? 92.166  -1.603  8.153   1.00 45.75  ? 16  VAL A CA  1 
ATOM   109  C  C   . VAL A 1 17  ? 93.104  -0.660  7.410   1.00 45.55  ? 16  VAL A C   1 
ATOM   110  O  O   . VAL A 1 17  ? 94.150  -1.080  6.899   1.00 47.89  ? 16  VAL A O   1 
ATOM   111  C  CB  . VAL A 1 17  ? 91.000  -2.071  7.261   1.00 44.03  ? 16  VAL A CB  1 
ATOM   112  C  CG1 . VAL A 1 17  ? 91.405  -2.078  5.796   1.00 39.75  ? 16  VAL A CG1 1 
ATOM   113  C  CG2 . VAL A 1 17  ? 90.525  -3.449  7.690   1.00 49.98  ? 16  VAL A CG2 1 
ATOM   114  N  N   . LYS A 1 18  ? 92.759  0.629   7.352   1.00 41.09  ? 17  LYS A N   1 
ATOM   115  C  CA  . LYS A 1 18  ? 93.642  1.596   6.707   1.00 47.78  ? 17  LYS A CA  1 
ATOM   116  C  C   . LYS A 1 18  ? 94.969  1.696   7.449   1.00 49.29  ? 17  LYS A C   1 
ATOM   117  O  O   . LYS A 1 18  ? 96.030  1.835   6.829   1.00 42.50  ? 17  LYS A O   1 
ATOM   118  C  CB  . LYS A 1 18  ? 92.960  2.963   6.614   1.00 43.64  ? 17  LYS A CB  1 
ATOM   119  C  CG  . LYS A 1 18  ? 93.906  4.146   6.763   1.00 50.88  ? 17  LYS A CG  1 
ATOM   120  C  CD  . LYS A 1 18  ? 93.265  5.437   6.277   1.00 63.71  ? 17  LYS A CD  1 
ATOM   121  C  CE  . LYS A 1 18  ? 94.174  6.632   6.519   1.00 72.19  ? 17  LYS A CE  1 
ATOM   122  N  NZ  . LYS A 1 18  ? 93.802  7.797   5.666   1.00 67.25  ? 17  LYS A NZ  1 
ATOM   123  N  N   . ILE A 1 19  ? 94.930  1.613   8.780   1.00 49.28  ? 18  ILE A N   1 
ATOM   124  C  CA  . ILE A 1 19  ? 96.161  1.674   9.561   1.00 51.06  ? 18  ILE A CA  1 
ATOM   125  C  C   . ILE A 1 19  ? 96.978  0.406   9.349   1.00 51.52  ? 18  ILE A C   1 
ATOM   126  O  O   . ILE A 1 19  ? 98.191  0.460   9.113   1.00 50.98  ? 18  ILE A O   1 
ATOM   127  C  CB  . ILE A 1 19  ? 95.838  1.898   11.050  1.00 53.59  ? 18  ILE A CB  1 
ATOM   128  C  CG1 . ILE A 1 19  ? 95.576  3.379   11.327  1.00 46.56  ? 18  ILE A CG1 1 
ATOM   129  C  CG2 . ILE A 1 19  ? 96.970  1.389   11.932  1.00 60.05  ? 18  ILE A CG2 1 
ATOM   130  C  CD1 . ILE A 1 19  ? 94.912  3.639   12.661  1.00 39.67  ? 18  ILE A CD1 1 
ATOM   131  N  N   . GLY A 1 20  ? 96.324  -0.756  9.428   1.00 47.50  ? 19  GLY A N   1 
ATOM   132  C  CA  . GLY A 1 20  ? 97.024  -2.008  9.185   1.00 51.12  ? 19  GLY A CA  1 
ATOM   133  C  C   . GLY A 1 20  ? 97.614  -2.089  7.791   1.00 50.98  ? 19  GLY A C   1 
ATOM   134  O  O   . GLY A 1 20  ? 98.730  -2.581  7.606   1.00 52.80  ? 19  GLY A O   1 
ATOM   135  N  N   . ALA A 1 21  ? 96.871  -1.609  6.791   1.00 43.74  ? 20  ALA A N   1 
ATOM   136  C  CA  . ALA A 1 21  ? 97.390  -1.590  5.427   1.00 45.73  ? 20  ALA A CA  1 
ATOM   137  C  C   . ALA A 1 21  ? 98.565  -0.629  5.299   1.00 49.57  ? 20  ALA A C   1 
ATOM   138  O  O   . ALA A 1 21  ? 99.552  -0.934  4.619   1.00 50.26  ? 20  ALA A O   1 
ATOM   139  C  CB  . ALA A 1 21  ? 96.280  -1.218  4.445   1.00 43.41  ? 20  ALA A CB  1 
ATOM   140  N  N   . GLY A 1 22  ? 98.475  0.536   5.943   1.00 48.89  ? 21  GLY A N   1 
ATOM   141  C  CA  . GLY A 1 22  ? 99.572  1.488   5.887   1.00 48.15  ? 21  GLY A CA  1 
ATOM   142  C  C   . GLY A 1 22  ? 100.832 0.964   6.547   1.00 52.99  ? 21  GLY A C   1 
ATOM   143  O  O   . GLY A 1 22  ? 101.936 1.134   6.022   1.00 55.30  ? 21  GLY A O   1 
ATOM   144  N  N   . LEU A 1 23  ? 100.686 0.318   7.707   1.00 48.93  ? 22  LEU A N   1 
ATOM   145  C  CA  . LEU A 1 23  ? 101.843 -0.273  8.370   1.00 52.50  ? 22  LEU A CA  1 
ATOM   146  C  C   . LEU A 1 23  ? 102.463 -1.370  7.516   1.00 56.42  ? 22  LEU A C   1 
ATOM   147  O  O   . LEU A 1 23  ? 103.690 -1.526  7.487   1.00 58.11  ? 22  LEU A O   1 
ATOM   148  C  CB  . LEU A 1 23  ? 101.444 -0.816  9.742   1.00 53.77  ? 22  LEU A CB  1 
ATOM   149  C  CG  . LEU A 1 23  ? 101.012 0.229   10.771  1.00 59.31  ? 22  LEU A CG  1 
ATOM   150  C  CD1 . LEU A 1 23  ? 100.594 -0.436  12.073  1.00 57.25  ? 22  LEU A CD1 1 
ATOM   151  C  CD2 . LEU A 1 23  ? 102.124 1.238   11.008  1.00 56.69  ? 22  LEU A CD2 1 
ATOM   152  N  N   . LEU A 1 24  ? 101.632 -2.144  6.814   1.00 55.34  ? 23  LEU A N   1 
ATOM   153  C  CA  . LEU A 1 24  ? 102.161 -3.189  5.945   1.00 53.62  ? 23  LEU A CA  1 
ATOM   154  C  C   . LEU A 1 24  ? 102.915 -2.584  4.769   1.00 56.48  ? 23  LEU A C   1 
ATOM   155  O  O   . LEU A 1 24  ? 104.038 -2.997  4.458   1.00 59.22  ? 23  LEU A O   1 
ATOM   156  C  CB  . LEU A 1 24  ? 101.022 -4.083  5.453   1.00 56.96  ? 23  LEU A CB  1 
ATOM   157  C  CG  . LEU A 1 24  ? 101.388 -5.272  4.561   1.00 63.08  ? 23  LEU A CG  1 
ATOM   158  C  CD1 . LEU A 1 24  ? 102.557 -6.058  5.142   1.00 64.83  ? 23  LEU A CD1 1 
ATOM   159  C  CD2 . LEU A 1 24  ? 100.180 -6.172  4.351   1.00 55.51  ? 23  LEU A CD2 1 
ATOM   160  N  N   . VAL A 1 25  ? 102.311 -1.598  4.104   1.00 51.58  ? 24  VAL A N   1 
ATOM   161  C  CA  . VAL A 1 25  ? 102.950 -0.985  2.945   1.00 52.33  ? 24  VAL A CA  1 
ATOM   162  C  C   . VAL A 1 25  ? 104.193 -0.208  3.365   1.00 57.20  ? 24  VAL A C   1 
ATOM   163  O  O   . VAL A 1 25  ? 105.224 -0.244  2.682   1.00 53.97  ? 24  VAL A O   1 
ATOM   164  C  CB  . VAL A 1 25  ? 101.941 -0.092  2.199   1.00 45.90  ? 24  VAL A CB  1 
ATOM   165  C  CG1 . VAL A 1 25  ? 102.659 0.884   1.281   1.00 48.95  ? 24  VAL A CG1 1 
ATOM   166  C  CG2 . VAL A 1 25  ? 100.959 -0.947  1.411   1.00 58.12  ? 24  VAL A CG2 1 
ATOM   167  N  N   . GLY A 1 26  ? 104.126 0.485   4.505   1.00 53.20  ? 25  GLY A N   1 
ATOM   168  C  CA  . GLY A 1 26  ? 105.277 1.249   4.960   1.00 53.66  ? 25  GLY A CA  1 
ATOM   169  C  C   . GLY A 1 26  ? 106.479 0.384   5.288   1.00 58.68  ? 25  GLY A C   1 
ATOM   170  O  O   . GLY A 1 26  ? 107.617 0.746   4.980   1.00 63.00  ? 25  GLY A O   1 
ATOM   171  N  N   . LYS A 1 27  ? 106.248 -0.774  5.912   1.00 57.19  ? 26  LYS A N   1 
ATOM   172  C  CA  . LYS A 1 27  ? 107.366 -1.664  6.209   1.00 61.79  ? 26  LYS A CA  1 
ATOM   173  C  C   . LYS A 1 27  ? 107.876 -2.363  4.954   1.00 63.01  ? 26  LYS A C   1 
ATOM   174  O  O   . LYS A 1 27  ? 109.073 -2.654  4.855   1.00 69.06  ? 26  LYS A O   1 
ATOM   175  C  CB  . LYS A 1 27  ? 106.983 -2.659  7.306   1.00 67.41  ? 26  LYS A CB  1 
ATOM   176  C  CG  . LYS A 1 27  ? 107.223 -2.078  8.704   1.00 80.63  ? 26  LYS A CG  1 
ATOM   177  C  CD  . LYS A 1 27  ? 107.110 -3.103  9.825   1.00 94.25  ? 26  LYS A CD  1 
ATOM   178  C  CE  . LYS A 1 27  ? 106.151 -2.635  10.913  1.00 91.45  ? 26  LYS A CE  1 
ATOM   179  N  NZ  . LYS A 1 27  ? 105.204 -3.696  11.350  1.00 82.47  ? 26  LYS A NZ  1 
ATOM   180  N  N   . LEU A 1 28  ? 106.993 -2.641  3.990   1.00 60.89  ? 27  LEU A N   1 
ATOM   181  C  CA  . LEU A 1 28  ? 107.454 -3.170  2.709   1.00 64.34  ? 27  LEU A CA  1 
ATOM   182  C  C   . LEU A 1 28  ? 108.344 -2.161  1.996   1.00 64.32  ? 27  LEU A C   1 
ATOM   183  O  O   . LEU A 1 28  ? 109.349 -2.532  1.379   1.00 64.07  ? 27  LEU A O   1 
ATOM   184  C  CB  . LEU A 1 28  ? 106.262 -3.544  1.826   1.00 59.79  ? 27  LEU A CB  1 
ATOM   185  C  CG  . LEU A 1 28  ? 105.465 -4.804  2.168   1.00 63.02  ? 27  LEU A CG  1 
ATOM   186  C  CD1 . LEU A 1 28  ? 104.128 -4.794  1.445   1.00 62.92  ? 27  LEU A CD1 1 
ATOM   187  C  CD2 . LEU A 1 28  ? 106.256 -6.051  1.810   1.00 68.26  ? 27  LEU A CD2 1 
ATOM   188  N  N   . LEU A 1 29  ? 107.982 -0.878  2.063   1.00 64.48  ? 28  LEU A N   1 
ATOM   189  C  CA  . LEU A 1 29  ? 108.784 0.158   1.422   1.00 64.86  ? 28  LEU A CA  1 
ATOM   190  C  C   . LEU A 1 29  ? 110.125 0.334   2.126   1.00 70.47  ? 28  LEU A C   1 
ATOM   191  O  O   . LEU A 1 29  ? 111.152 0.550   1.472   1.00 69.19  ? 28  LEU A O   1 
ATOM   192  C  CB  . LEU A 1 29  ? 108.010 1.475   1.406   1.00 63.18  ? 28  LEU A CB  1 
ATOM   193  C  CG  . LEU A 1 29  ? 108.571 2.611   0.552   1.00 67.56  ? 28  LEU A CG  1 
ATOM   194  C  CD1 . LEU A 1 29  ? 107.974 2.564   -0.842  1.00 64.98  ? 28  LEU A CD1 1 
ATOM   195  C  CD2 . LEU A 1 29  ? 108.300 3.953   1.211   1.00 66.60  ? 28  LEU A CD2 1 
ATOM   196  N  N   . ALA A 1 30  ? 110.132 0.255   3.458   1.00 70.85  ? 29  ALA A N   1 
ATOM   197  C  CA  . ALA A 1 30  ? 111.374 0.413   4.209   1.00 68.61  ? 29  ALA A CA  1 
ATOM   198  C  C   . ALA A 1 30  ? 112.352 -0.717  3.907   1.00 64.84  ? 29  ALA A C   1 
ATOM   199  O  O   . ALA A 1 30  ? 113.530 -0.473  3.623   1.00 67.06  ? 29  ALA A O   1 
ATOM   200  C  CB  . ALA A 1 30  ? 111.076 0.484   5.707   1.00 61.69  ? 29  ALA A CB  1 
ATOM   201  N  N   . VAL A 1 31  ? 111.879 -1.964  3.972   1.00 60.52  ? 30  VAL A N   1 
ATOM   202  C  CA  . VAL A 1 31  ? 112.743 -3.115  3.719   1.00 64.84  ? 30  VAL A CA  1 
ATOM   203  C  C   . VAL A 1 31  ? 113.242 -3.121  2.280   1.00 69.74  ? 30  VAL A C   1 
ATOM   204  O  O   . VAL A 1 31  ? 114.370 -3.551  2.005   1.00 75.06  ? 30  VAL A O   1 
ATOM   205  C  CB  . VAL A 1 31  ? 111.991 -4.417  4.063   1.00 57.09  ? 30  VAL A CB  1 
ATOM   206  C  CG1 . VAL A 1 31  ? 112.782 -5.641  3.622   1.00 48.41  ? 30  VAL A CG1 1 
ATOM   207  C  CG2 . VAL A 1 31  ? 111.692 -4.479  5.554   1.00 50.38  ? 30  VAL A CG2 1 
ATOM   208  N  N   . SER A 1 32  ? 112.436 -2.617  1.346   1.00 69.81  ? 31  SER A N   1 
ATOM   209  C  CA  . SER A 1 32  ? 112.803 -2.692  -0.063  1.00 69.58  ? 31  SER A CA  1 
ATOM   210  C  C   . SER A 1 32  ? 113.800 -1.607  -0.455  1.00 69.72  ? 31  SER A C   1 
ATOM   211  O  O   . SER A 1 32  ? 114.690 -1.853  -1.277  1.00 76.16  ? 31  SER A O   1 
ATOM   212  C  CB  . SER A 1 32  ? 111.552 -2.606  -0.937  1.00 61.63  ? 31  SER A CB  1 
ATOM   213  O  OG  . SER A 1 32  ? 111.081 -3.900  -1.274  1.00 66.17  ? 31  SER A OG  1 
ATOM   214  N  N   . PHE A 1 33  ? 113.674 -0.405  0.112   1.00 65.92  ? 32  PHE A N   1 
ATOM   215  C  CA  . PHE A 1 33  ? 114.428 0.737   -0.380  1.00 63.82  ? 32  PHE A CA  1 
ATOM   216  C  C   . PHE A 1 33  ? 115.223 1.467   0.696   1.00 70.92  ? 32  PHE A C   1 
ATOM   217  O  O   . PHE A 1 33  ? 115.943 2.416   0.367   1.00 74.57  ? 32  PHE A O   1 
ATOM   218  C  CB  . PHE A 1 33  ? 113.479 1.724   -1.074  1.00 61.83  ? 32  PHE A CB  1 
ATOM   219  C  CG  . PHE A 1 33  ? 112.590 1.076   -2.097  1.00 69.71  ? 32  PHE A CG  1 
ATOM   220  C  CD1 . PHE A 1 33  ? 113.119 0.561   -3.268  1.00 62.24  ? 32  PHE A CD1 1 
ATOM   221  C  CD2 . PHE A 1 33  ? 111.227 0.960   -1.874  1.00 67.67  ? 32  PHE A CD2 1 
ATOM   222  C  CE1 . PHE A 1 33  ? 112.304 -0.046  -4.204  1.00 65.82  ? 32  PHE A CE1 1 
ATOM   223  C  CE2 . PHE A 1 33  ? 110.408 0.355   -2.806  1.00 63.39  ? 32  PHE A CE2 1 
ATOM   224  C  CZ  . PHE A 1 33  ? 110.946 -0.149  -3.972  1.00 64.53  ? 32  PHE A CZ  1 
ATOM   225  N  N   . GLY A 1 34  ? 115.119 1.057   1.959   1.00 72.35  ? 33  GLY A N   1 
ATOM   226  C  CA  . GLY A 1 34  ? 115.953 1.580   3.018   1.00 68.46  ? 33  GLY A CA  1 
ATOM   227  C  C   . GLY A 1 34  ? 115.785 3.067   3.258   1.00 74.51  ? 33  GLY A C   1 
ATOM   228  O  O   . GLY A 1 34  ? 114.838 3.698   2.778   1.00 75.02  ? 33  GLY A O   1 
ATOM   229  N  N   . PRO A 1 35  ? 116.711 3.657   4.023   1.00 78.74  ? 34  PRO A N   1 
ATOM   230  C  CA  . PRO A 1 35  ? 116.588 5.089   4.343   1.00 77.99  ? 34  PRO A CA  1 
ATOM   231  C  C   . PRO A 1 35  ? 116.714 5.989   3.127   1.00 75.16  ? 34  PRO A C   1 
ATOM   232  O  O   . PRO A 1 35  ? 116.139 7.084   3.120   1.00 76.08  ? 34  PRO A O   1 
ATOM   233  C  CB  . PRO A 1 35  ? 117.726 5.327   5.348   1.00 75.70  ? 34  PRO A CB  1 
ATOM   234  C  CG  . PRO A 1 35  ? 118.101 3.962   5.848   1.00 74.69  ? 34  PRO A CG  1 
ATOM   235  C  CD  . PRO A 1 35  ? 117.865 3.040   4.694   1.00 76.23  ? 34  PRO A CD  1 
ATOM   236  N  N   . ALA A 1 36  ? 117.463 5.567   2.105   1.00 73.75  ? 35  ALA A N   1 
ATOM   237  C  CA  . ALA A 1 36  ? 117.575 6.360   0.885   1.00 74.57  ? 35  ALA A CA  1 
ATOM   238  C  C   . ALA A 1 36  ? 116.236 6.452   0.164   1.00 74.86  ? 35  ALA A C   1 
ATOM   239  O  O   . ALA A 1 36  ? 115.861 7.522   -0.330  1.00 71.72  ? 35  ALA A O   1 
ATOM   240  C  CB  . ALA A 1 36  ? 118.642 5.767   -0.034  1.00 71.97  ? 35  ALA A CB  1 
ATOM   241  N  N   . GLY A 1 37  ? 115.506 5.339   0.086   1.00 71.88  ? 36  GLY A N   1 
ATOM   242  C  CA  . GLY A 1 37  ? 114.186 5.372   -0.522  1.00 71.88  ? 36  GLY A CA  1 
ATOM   243  C  C   . GLY A 1 37  ? 113.186 6.173   0.290   1.00 68.94  ? 36  GLY A C   1 
ATOM   244  O  O   . GLY A 1 37  ? 112.332 6.866   -0.271  1.00 61.35  ? 36  GLY A O   1 
ATOM   245  N  N   . LEU A 1 38  ? 113.277 6.093   1.620   1.00 67.14  ? 37  LEU A N   1 
ATOM   246  C  CA  . LEU A 1 38  ? 112.366 6.852   2.471   1.00 61.10  ? 37  LEU A CA  1 
ATOM   247  C  C   . LEU A 1 38  ? 112.625 8.349   2.356   1.00 65.63  ? 37  LEU A C   1 
ATOM   248  O  O   . LEU A 1 38  ? 111.681 9.144   2.277   1.00 66.46  ? 37  LEU A O   1 
ATOM   249  C  CB  . LEU A 1 38  ? 112.500 6.392   3.923   1.00 64.19  ? 37  LEU A CB  1 
ATOM   250  C  CG  . LEU A 1 38  ? 111.875 5.037   4.264   1.00 67.14  ? 37  LEU A CG  1 
ATOM   251  C  CD1 . LEU A 1 38  ? 112.210 4.632   5.692   1.00 61.27  ? 37  LEU A CD1 1 
ATOM   252  C  CD2 . LEU A 1 38  ? 110.370 5.067   4.052   1.00 70.63  ? 37  LEU A CD2 1 
ATOM   253  N  N   . GLY A 1 39  ? 113.897 8.753   2.357   1.00 69.30  ? 38  GLY A N   1 
ATOM   254  C  CA  . GLY A 1 39  ? 114.219 10.166  2.247   1.00 60.64  ? 38  GLY A CA  1 
ATOM   255  C  C   . GLY A 1 39  ? 113.805 10.766  0.918   1.00 63.78  ? 38  GLY A C   1 
ATOM   256  O  O   . GLY A 1 39  ? 113.405 11.931  0.855   1.00 59.24  ? 38  GLY A O   1 
ATOM   257  N  N   . LEU A 1 40  ? 113.895 9.985   -0.158  1.00 65.16  ? 39  LEU A N   1 
ATOM   258  C  CA  . LEU A 1 40  ? 113.456 10.455  -1.465  1.00 64.79  ? 39  LEU A CA  1 
ATOM   259  C  C   . LEU A 1 40  ? 111.941 10.452  -1.612  1.00 64.05  ? 39  LEU A C   1 
ATOM   260  O  O   . LEU A 1 40  ? 111.410 11.200  -2.439  1.00 62.78  ? 39  LEU A O   1 
ATOM   261  C  CB  . LEU A 1 40  ? 114.072 9.589   -2.565  1.00 65.28  ? 39  LEU A CB  1 
ATOM   262  C  CG  . LEU A 1 40  ? 115.379 10.032  -3.221  1.00 60.45  ? 39  LEU A CG  1 
ATOM   263  C  CD1 . LEU A 1 40  ? 115.683 9.142   -4.414  1.00 63.74  ? 39  LEU A CD1 1 
ATOM   264  C  CD2 . LEU A 1 40  ? 115.298 11.486  -3.647  1.00 52.41  ? 39  LEU A CD2 1 
ATOM   265  N  N   . ALA A 1 41  ? 111.235 9.641   -0.827  1.00 61.35  ? 40  ALA A N   1 
ATOM   266  C  CA  . ALA A 1 41  ? 109.783 9.559   -0.896  1.00 61.24  ? 40  ALA A CA  1 
ATOM   267  C  C   . ALA A 1 41  ? 109.076 10.502  0.068   1.00 64.48  ? 40  ALA A C   1 
ATOM   268  O  O   . ALA A 1 41  ? 107.843 10.558  0.055   1.00 64.19  ? 40  ALA A O   1 
ATOM   269  C  CB  . ALA A 1 41  ? 109.325 8.121   -0.629  1.00 54.37  ? 40  ALA A CB  1 
ATOM   270  N  N   . ALA A 1 42  ? 109.815 11.254  0.885   1.00 66.30  ? 41  ALA A N   1 
ATOM   271  C  CA  . ALA A 1 42  ? 109.194 12.037  1.950   1.00 58.28  ? 41  ALA A CA  1 
ATOM   272  C  C   . ALA A 1 42  ? 108.269 13.109  1.384   1.00 63.18  ? 41  ALA A C   1 
ATOM   273  O  O   . ALA A 1 42  ? 107.085 13.177  1.735   1.00 64.80  ? 41  ALA A O   1 
ATOM   274  C  CB  . ALA A 1 42  ? 110.272 12.662  2.836   1.00 55.37  ? 41  ALA A CB  1 
ATOM   275  N  N   . ASN A 1 43  ? 108.798 13.965  0.506   1.00 62.25  ? 42  ASN A N   1 
ATOM   276  C  CA  . ASN A 1 43  ? 107.988 15.037  -0.067  1.00 63.20  ? 42  ASN A CA  1 
ATOM   277  C  C   . ASN A 1 43  ? 106.848 14.483  -0.915  1.00 63.31  ? 42  ASN A C   1 
ATOM   278  O  O   . ASN A 1 43  ? 105.713 14.967  -0.833  1.00 55.64  ? 42  ASN A O   1 
ATOM   279  C  CB  . ASN A 1 43  ? 108.869 15.971  -0.894  1.00 62.72  ? 42  ASN A CB  1 
ATOM   280  C  CG  . ASN A 1 43  ? 109.829 16.774  -0.041  1.00 68.31  ? 42  ASN A CG  1 
ATOM   281  O  OD1 . ASN A 1 43  ? 109.576 17.016  1.139   1.00 65.55  ? 42  ASN A OD1 1 
ATOM   282  N  ND2 . ASN A 1 43  ? 110.941 17.189  -0.635  1.00 68.34  ? 42  ASN A ND2 1 
ATOM   283  N  N   . PHE A 1 44  ? 107.138 13.479  -1.747  1.00 63.99  ? 43  PHE A N   1 
ATOM   284  C  CA  . PHE A 1 44  ? 106.108 12.875  -2.590  1.00 60.64  ? 43  PHE A CA  1 
ATOM   285  C  C   . PHE A 1 44  ? 104.950 12.333  -1.758  1.00 60.43  ? 43  PHE A C   1 
ATOM   286  O  O   . PHE A 1 44  ? 103.783 12.469  -2.144  1.00 59.60  ? 43  PHE A O   1 
ATOM   287  C  CB  . PHE A 1 44  ? 106.724 11.767  -3.446  1.00 60.21  ? 43  PHE A CB  1 
ATOM   288  C  CG  . PHE A 1 44  ? 105.752 11.113  -4.389  1.00 59.99  ? 43  PHE A CG  1 
ATOM   289  C  CD1 . PHE A 1 44  ? 105.484 11.674  -5.627  1.00 54.12  ? 43  PHE A CD1 1 
ATOM   290  C  CD2 . PHE A 1 44  ? 105.118 9.930   -4.045  1.00 59.03  ? 43  PHE A CD2 1 
ATOM   291  C  CE1 . PHE A 1 44  ? 104.594 11.074  -6.499  1.00 57.39  ? 43  PHE A CE1 1 
ATOM   292  C  CE2 . PHE A 1 44  ? 104.228 9.325   -4.913  1.00 55.89  ? 43  PHE A CE2 1 
ATOM   293  C  CZ  . PHE A 1 44  ? 103.966 9.898   -6.141  1.00 56.01  ? 43  PHE A CZ  1 
ATOM   294  N  N   . ARG A 1 45  ? 105.251 11.724  -0.610  1.00 61.24  ? 44  ARG A N   1 
ATOM   295  C  CA  . ARG A 1 45  ? 104.196 11.183  0.243   1.00 62.60  ? 44  ARG A CA  1 
ATOM   296  C  C   . ARG A 1 45  ? 103.373 12.297  0.880   1.00 61.27  ? 44  ARG A C   1 
ATOM   297  O  O   . ARG A 1 45  ? 102.148 12.176  1.002   1.00 63.99  ? 44  ARG A O   1 
ATOM   298  C  CB  . ARG A 1 45  ? 104.798 10.264  1.306   1.00 62.62  ? 44  ARG A CB  1 
ATOM   299  C  CG  . ARG A 1 45  ? 105.309 8.949   0.732   1.00 67.67  ? 44  ARG A CG  1 
ATOM   300  C  CD  . ARG A 1 45  ? 106.212 8.195   1.698   1.00 67.66  ? 44  ARG A CD  1 
ATOM   301  N  NE  . ARG A 1 45  ? 105.466 7.442   2.699   1.00 76.52  ? 44  ARG A NE  1 
ATOM   302  C  CZ  . ARG A 1 45  ? 106.024 6.733   3.670   1.00 76.53  ? 44  ARG A CZ  1 
ATOM   303  N  NH1 . ARG A 1 45  ? 107.339 6.660   3.804   1.00 80.37  ? 44  ARG A NH1 1 
ATOM   304  N  NH2 . ARG A 1 45  ? 105.246 6.075   4.524   1.00 84.89  ? 44  ARG A NH2 1 
ATOM   305  N  N   . GLN A 1 46  ? 104.023 13.388  1.293   1.00 63.21  ? 45  GLN A N   1 
ATOM   306  C  CA  . GLN A 1 46  ? 103.282 14.520  1.839   1.00 60.05  ? 45  GLN A CA  1 
ATOM   307  C  C   . GLN A 1 46  ? 102.387 15.164  0.787   1.00 57.81  ? 45  GLN A C   1 
ATOM   308  O  O   . GLN A 1 46  ? 101.302 15.655  1.117   1.00 58.79  ? 45  GLN A O   1 
ATOM   309  C  CB  . GLN A 1 46  ? 104.257 15.556  2.406   1.00 60.48  ? 45  GLN A CB  1 
ATOM   310  C  CG  . GLN A 1 46  ? 103.657 16.648  3.308   1.00 62.81  ? 45  GLN A CG  1 
ATOM   311  C  CD  . GLN A 1 46  ? 102.614 16.154  4.304   1.00 85.85  ? 45  GLN A CD  1 
ATOM   312  O  OE1 . GLN A 1 46  ? 101.668 16.874  4.627   1.00 83.59  ? 45  GLN A OE1 1 
ATOM   313  N  NE2 . GLN A 1 46  ? 102.821 14.958  4.849   1.00 93.22  ? 45  GLN A NE2 1 
ATOM   314  N  N   . LEU A 1 47  ? 102.823 15.175  -0.475  1.00 64.21  ? 46  LEU A N   1 
ATOM   315  C  CA  . LEU A 1 47  ? 101.963 15.660  -1.551  1.00 63.80  ? 46  LEU A CA  1 
ATOM   316  C  C   . LEU A 1 47  ? 100.721 14.788  -1.706  1.00 62.11  ? 46  LEU A C   1 
ATOM   317  O  O   . LEU A 1 47  ? 99.620  15.301  -1.939  1.00 63.55  ? 46  LEU A O   1 
ATOM   318  C  CB  . LEU A 1 47  ? 102.748 15.721  -2.863  1.00 60.63  ? 46  LEU A CB  1 
ATOM   319  C  CG  . LEU A 1 47  ? 101.926 15.849  -4.148  1.00 60.60  ? 46  LEU A CG  1 
ATOM   320  C  CD1 . LEU A 1 47  ? 101.201 17.188  -4.194  1.00 61.97  ? 46  LEU A CD1 1 
ATOM   321  C  CD2 . LEU A 1 47  ? 102.806 15.671  -5.375  1.00 54.70  ? 46  LEU A CD2 1 
ATOM   322  N  N   . ILE A 1 48  ? 100.878 13.467  -1.583  1.00 60.30  ? 47  ILE A N   1 
ATOM   323  C  CA  . ILE A 1 48  ? 99.733  12.563  -1.684  1.00 57.39  ? 47  ILE A CA  1 
ATOM   324  C  C   . ILE A 1 48  ? 98.724  12.847  -0.578  1.00 61.61  ? 47  ILE A C   1 
ATOM   325  O  O   . ILE A 1 48  ? 97.507  12.815  -0.804  1.00 61.26  ? 47  ILE A O   1 
ATOM   326  C  CB  . ILE A 1 48  ? 100.206 11.097  -1.657  1.00 59.96  ? 47  ILE A CB  1 
ATOM   327  C  CG1 . ILE A 1 48  ? 101.126 10.809  -2.845  1.00 62.07  ? 47  ILE A CG1 1 
ATOM   328  C  CG2 . ILE A 1 48  ? 99.017  10.150  -1.669  1.00 58.16  ? 47  ILE A CG2 1 
ATOM   329  C  CD1 . ILE A 1 48  ? 100.604 11.332  -4.167  1.00 62.70  ? 47  ILE A CD1 1 
ATOM   330  N  N   . THR A 1 49  ? 99.209  13.125  0.633   1.00 62.22  ? 48  THR A N   1 
ATOM   331  C  CA  . THR A 1 49  ? 98.314  13.501  1.723   1.00 63.56  ? 48  THR A CA  1 
ATOM   332  C  C   . THR A 1 49  ? 97.566  14.788  1.390   1.00 60.77  ? 48  THR A C   1 
ATOM   333  O  O   . THR A 1 49  ? 96.345  14.875  1.566   1.00 62.63  ? 48  THR A O   1 
ATOM   334  C  CB  . THR A 1 49  ? 99.102  13.647  3.024   1.00 65.78  ? 48  THR A CB  1 
ATOM   335  O  OG1 . THR A 1 49  ? 99.617  12.369  3.417   1.00 63.96  ? 48  THR A OG1 1 
ATOM   336  C  CG2 . THR A 1 49  ? 98.201  14.168  4.128   1.00 68.74  ? 48  THR A CG2 1 
ATOM   337  N  N   . VAL A 1 50  ? 98.293  15.801  0.911   1.00 62.35  ? 49  VAL A N   1 
ATOM   338  C  CA  . VAL A 1 50  ? 97.687  17.095  0.599   1.00 65.45  ? 49  VAL A CA  1 
ATOM   339  C  C   . VAL A 1 50  ? 96.623  16.943  -0.482  1.00 61.59  ? 49  VAL A C   1 
ATOM   340  O  O   . VAL A 1 50  ? 95.557  17.568  -0.419  1.00 61.60  ? 49  VAL A O   1 
ATOM   341  C  CB  . VAL A 1 50  ? 98.774  18.104  0.181   1.00 60.87  ? 49  VAL A CB  1 
ATOM   342  C  CG1 . VAL A 1 50  ? 98.148  19.343  -0.448  1.00 59.02  ? 49  VAL A CG1 1 
ATOM   343  C  CG2 . VAL A 1 50  ? 99.641  18.479  1.370   1.00 66.26  ? 49  VAL A CG2 1 
ATOM   344  N  N   . LEU A 1 51  ? 96.894  16.106  -1.487  1.00 55.47  ? 50  LEU A N   1 
ATOM   345  C  CA  . LEU A 1 51  ? 95.956  15.914  -2.587  1.00 53.19  ? 50  LEU A CA  1 
ATOM   346  C  C   . LEU A 1 51  ? 94.629  15.320  -2.133  1.00 53.65  ? 50  LEU A C   1 
ATOM   347  O  O   . LEU A 1 51  ? 93.624  15.477  -2.834  1.00 47.73  ? 50  LEU A O   1 
ATOM   348  C  CB  . LEU A 1 51  ? 96.581  15.014  -3.654  1.00 51.61  ? 50  LEU A CB  1 
ATOM   349  C  CG  . LEU A 1 51  ? 97.577  15.659  -4.618  1.00 52.56  ? 50  LEU A CG  1 
ATOM   350  C  CD1 . LEU A 1 51  ? 98.255  14.592  -5.463  1.00 58.12  ? 50  LEU A CD1 1 
ATOM   351  C  CD2 . LEU A 1 51  ? 96.890  16.690  -5.498  1.00 54.47  ? 50  LEU A CD2 1 
ATOM   352  N  N   . GLY A 1 52  ? 94.602  14.637  -0.987  1.00 51.91  ? 51  GLY A N   1 
ATOM   353  C  CA  . GLY A 1 52  ? 93.347  14.103  -0.484  1.00 56.74  ? 51  GLY A CA  1 
ATOM   354  C  C   . GLY A 1 52  ? 92.289  15.159  -0.228  1.00 52.67  ? 51  GLY A C   1 
ATOM   355  O  O   . GLY A 1 52  ? 91.092  14.862  -0.260  1.00 45.06  ? 51  GLY A O   1 
ATOM   356  N  N   . VAL A 1 53  ? 92.705  16.396  0.036   1.00 56.72  ? 52  VAL A N   1 
ATOM   357  C  CA  . VAL A 1 53  ? 91.791  17.521  0.158   1.00 56.50  ? 52  VAL A CA  1 
ATOM   358  C  C   . VAL A 1 53  ? 91.897  18.472  -1.029  1.00 62.02  ? 52  VAL A C   1 
ATOM   359  O  O   . VAL A 1 53  ? 90.890  19.035  -1.468  1.00 59.36  ? 52  VAL A O   1 
ATOM   360  C  CB  . VAL A 1 53  ? 92.030  18.273  1.485   1.00 59.30  ? 52  VAL A CB  1 
ATOM   361  C  CG1 . VAL A 1 53  ? 90.996  19.374  1.673   1.00 64.77  ? 52  VAL A CG1 1 
ATOM   362  C  CG2 . VAL A 1 53  ? 92.007  17.304  2.657   1.00 67.68  ? 52  VAL A CG2 1 
ATOM   363  N  N   . LEU A 1 54  ? 93.104  18.659  -1.568  1.00 60.00  ? 53  LEU A N   1 
ATOM   364  C  CA  . LEU A 1 54  ? 93.300  19.670  -2.603  1.00 58.99  ? 53  LEU A CA  1 
ATOM   365  C  C   . LEU A 1 54  ? 92.693  19.258  -3.939  1.00 58.70  ? 53  LEU A C   1 
ATOM   366  O  O   . LEU A 1 54  ? 92.201  20.116  -4.680  1.00 59.66  ? 53  LEU A O   1 
ATOM   367  C  CB  . LEU A 1 54  ? 94.793  19.959  -2.766  1.00 63.45  ? 53  LEU A CB  1 
ATOM   368  C  CG  . LEU A 1 54  ? 95.220  20.811  -3.963  1.00 67.09  ? 53  LEU A CG  1 
ATOM   369  C  CD1 . LEU A 1 54  ? 94.673  22.227  -3.835  1.00 73.32  ? 53  LEU A CD1 1 
ATOM   370  C  CD2 . LEU A 1 54  ? 96.734  20.822  -4.103  1.00 56.22  ? 53  LEU A CD2 1 
ATOM   371  N  N   . ALA A 1 55  ? 92.706  17.961  -4.260  1.00 61.51  ? 54  ALA A N   1 
ATOM   372  C  CA  . ALA A 1 55  ? 92.292  17.529  -5.593  1.00 60.89  ? 54  ALA A CA  1 
ATOM   373  C  C   . ALA A 1 55  ? 90.837  17.877  -5.884  1.00 65.68  ? 54  ALA A C   1 
ATOM   374  O  O   . ALA A 1 55  ? 90.485  18.142  -7.039  1.00 65.61  ? 54  ALA A O   1 
ATOM   375  C  CB  . ALA A 1 55  ? 92.522  16.027  -5.755  1.00 57.67  ? 54  ALA A CB  1 
ATOM   376  N  N   . GLY A 1 56  ? 89.982  17.881  -4.864  1.00 59.68  ? 55  GLY A N   1 
ATOM   377  C  CA  . GLY A 1 56  ? 88.593  18.252  -5.050  1.00 55.28  ? 55  GLY A CA  1 
ATOM   378  C  C   . GLY A 1 56  ? 88.256  19.635  -4.533  1.00 55.25  ? 55  GLY A C   1 
ATOM   379  O  O   . GLY A 1 56  ? 87.094  19.924  -4.233  1.00 54.77  ? 55  GLY A O   1 
ATOM   380  N  N   . ALA A 1 57  ? 89.271  20.492  -4.419  1.00 54.04  ? 56  ALA A N   1 
ATOM   381  C  CA  . ALA A 1 57  ? 89.125  21.882  -3.990  1.00 51.73  ? 56  ALA A CA  1 
ATOM   382  C  C   . ALA A 1 57  ? 88.523  22.004  -2.592  1.00 52.78  ? 56  ALA A C   1 
ATOM   383  O  O   . ALA A 1 57  ? 87.933  23.036  -2.258  1.00 53.28  ? 56  ALA A O   1 
ATOM   384  C  CB  . ALA A 1 57  ? 88.293  22.693  -4.993  1.00 52.67  ? 56  ALA A CB  1 
ATOM   385  N  N   . GLY A 1 58  ? 88.664  20.968  -1.767  1.00 49.98  ? 57  GLY A N   1 
ATOM   386  C  CA  . GLY A 1 58  ? 88.273  21.045  -0.370  1.00 46.81  ? 57  GLY A CA  1 
ATOM   387  C  C   . GLY A 1 58  ? 86.802  21.281  -0.107  1.00 49.15  ? 57  GLY A C   1 
ATOM   388  O  O   . GLY A 1 58  ? 86.450  21.777  0.966   1.00 45.72  ? 57  GLY A O   1 
ATOM   389  N  N   . ILE A 1 59  ? 85.923  20.953  -1.061  1.00 43.42  ? 58  ILE A N   1 
ATOM   390  C  CA  . ILE A 1 59  ? 84.489  21.164  -0.875  1.00 42.11  ? 58  ILE A CA  1 
ATOM   391  C  C   . ILE A 1 59  ? 83.807  20.005  -0.160  1.00 46.70  ? 58  ILE A C   1 
ATOM   392  O  O   . ILE A 1 59  ? 82.590  20.061  0.063   1.00 47.53  ? 58  ILE A O   1 
ATOM   393  C  CB  . ILE A 1 59  ? 83.784  21.396  -2.227  1.00 46.12  ? 58  ILE A CB  1 
ATOM   394  C  CG1 . ILE A 1 59  ? 83.798  20.112  -3.059  1.00 41.56  ? 58  ILE A CG1 1 
ATOM   395  C  CG2 . ILE A 1 59  ? 84.446  22.531  -2.984  1.00 45.85  ? 58  ILE A CG2 1 
ATOM   396  C  CD1 . ILE A 1 59  ? 82.931  20.175  -4.296  1.00 42.88  ? 58  ILE A CD1 1 
ATOM   397  N  N   . PHE A 1 60  ? 84.552  18.957  0.201   1.00 46.49  ? 59  PHE A N   1 
ATOM   398  C  CA  . PHE A 1 60  ? 83.938  17.689  0.593   1.00 44.13  ? 59  PHE A CA  1 
ATOM   399  C  C   . PHE A 1 60  ? 83.020  17.845  1.802   1.00 43.57  ? 59  PHE A C   1 
ATOM   400  O  O   . PHE A 1 60  ? 81.908  17.304  1.821   1.00 43.40  ? 59  PHE A O   1 
ATOM   401  C  CB  . PHE A 1 60  ? 85.027  16.646  0.841   1.00 42.31  ? 59  PHE A CB  1 
ATOM   402  C  CG  . PHE A 1 60  ? 85.881  16.385  -0.367  1.00 47.93  ? 59  PHE A CG  1 
ATOM   403  C  CD1 . PHE A 1 60  ? 85.315  15.888  -1.530  1.00 43.42  ? 59  PHE A CD1 1 
ATOM   404  C  CD2 . PHE A 1 60  ? 87.239  16.649  -0.350  1.00 46.10  ? 59  PHE A CD2 1 
ATOM   405  C  CE1 . PHE A 1 60  ? 86.087  15.655  -2.650  1.00 42.78  ? 59  PHE A CE1 1 
ATOM   406  C  CE2 . PHE A 1 60  ? 88.018  16.415  -1.468  1.00 51.54  ? 59  PHE A CE2 1 
ATOM   407  C  CZ  . PHE A 1 60  ? 87.440  15.918  -2.620  1.00 39.59  ? 59  PHE A CZ  1 
ATOM   408  N  N   . ASN A 1 61  ? 83.471  18.567  2.832   1.00 43.13  ? 60  ASN A N   1 
ATOM   409  C  CA  . ASN A 1 61  ? 82.610  18.804  3.989   1.00 35.15  ? 60  ASN A CA  1 
ATOM   410  C  C   . ASN A 1 61  ? 81.343  19.553  3.593   1.00 41.79  ? 60  ASN A C   1 
ATOM   411  O  O   . ASN A 1 61  ? 80.269  19.308  4.153   1.00 41.67  ? 60  ASN A O   1 
ATOM   412  C  CB  . ASN A 1 61  ? 83.369  19.564  5.075   1.00 39.41  ? 60  ASN A CB  1 
ATOM   413  C  CG  . ASN A 1 61  ? 84.260  18.660  5.900   1.00 49.93  ? 60  ASN A CG  1 
ATOM   414  O  OD1 . ASN A 1 61  ? 85.246  19.106  6.484   1.00 56.07  ? 60  ASN A OD1 1 
ATOM   415  N  ND2 . ASN A 1 61  ? 83.911  17.380  5.956   1.00 39.94  ? 60  ASN A ND2 1 
ATOM   416  N  N   . GLY A 1 62  ? 81.450  20.476  2.635   1.00 44.02  ? 61  GLY A N   1 
ATOM   417  C  CA  . GLY A 1 62  ? 80.261  21.157  2.149   1.00 36.98  ? 61  GLY A CA  1 
ATOM   418  C  C   . GLY A 1 62  ? 79.327  20.229  1.401   1.00 40.31  ? 61  GLY A C   1 
ATOM   419  O  O   . GLY A 1 62  ? 78.103  20.345  1.511   1.00 40.81  ? 61  GLY A O   1 
ATOM   420  N  N   . VAL A 1 63  ? 79.890  19.305  0.618   1.00 41.77  ? 62  VAL A N   1 
ATOM   421  C  CA  . VAL A 1 63  ? 79.078  18.285  -0.040  1.00 38.66  ? 62  VAL A CA  1 
ATOM   422  C  C   . VAL A 1 63  ? 78.257  17.523  0.990   1.00 39.92  ? 62  VAL A C   1 
ATOM   423  O  O   . VAL A 1 63  ? 77.037  17.381  0.859   1.00 39.52  ? 62  VAL A O   1 
ATOM   424  C  CB  . VAL A 1 63  ? 79.970  17.338  -0.863  1.00 42.95  ? 62  VAL A CB  1 
ATOM   425  C  CG1 . VAL A 1 63  ? 79.148  16.193  -1.428  1.00 37.05  ? 62  VAL A CG1 1 
ATOM   426  C  CG2 . VAL A 1 63  ? 80.666  18.102  -1.976  1.00 48.88  ? 62  VAL A CG2 1 
ATOM   427  N  N   . THR A 1 64  ? 78.920  17.028  2.039   1.00 37.36  ? 63  THR A N   1 
ATOM   428  C  CA  . THR A 1 64  ? 78.216  16.317  3.100   1.00 38.65  ? 63  THR A CA  1 
ATOM   429  C  C   . THR A 1 64  ? 77.171  17.208  3.762   1.00 41.41  ? 63  THR A C   1 
ATOM   430  O  O   . THR A 1 64  ? 76.045  16.768  4.022   1.00 41.12  ? 63  THR A O   1 
ATOM   431  C  CB  . THR A 1 64  ? 79.218  15.802  4.135   1.00 35.17  ? 63  THR A CB  1 
ATOM   432  O  OG1 . THR A 1 64  ? 80.096  14.852  3.520   1.00 44.11  ? 63  THR A OG1 1 
ATOM   433  C  CG2 . THR A 1 64  ? 78.499  15.135  5.295   1.00 34.89  ? 63  THR A CG2 1 
ATOM   434  N  N   . LYS A 1 65  ? 77.528  18.464  4.040   1.00 38.81  ? 64  LYS A N   1 
ATOM   435  C  CA  . LYS A 1 65  ? 76.615  19.364  4.738   1.00 36.10  ? 64  LYS A CA  1 
ATOM   436  C  C   . LYS A 1 65  ? 75.339  19.590  3.936   1.00 38.45  ? 64  LYS A C   1 
ATOM   437  O  O   . LYS A 1 65  ? 74.229  19.475  4.469   1.00 38.05  ? 64  LYS A O   1 
ATOM   438  C  CB  . LYS A 1 65  ? 77.316  20.694  5.029   1.00 41.92  ? 64  LYS A CB  1 
ATOM   439  C  CG  . LYS A 1 65  ? 76.486  21.690  5.832   1.00 43.86  ? 64  LYS A CG  1 
ATOM   440  C  CD  . LYS A 1 65  ? 75.893  22.768  4.931   1.00 51.64  ? 64  LYS A CD  1 
ATOM   441  C  CE  . LYS A 1 65  ? 74.958  23.700  5.691   1.00 39.44  ? 64  LYS A CE  1 
ATOM   442  N  NZ  . LYS A 1 65  ? 73.981  22.956  6.530   1.00 43.48  ? 64  LYS A NZ  1 
ATOM   443  N  N   . TYR A 1 66  ? 75.474  19.905  2.648   1.00 36.18  ? 65  TYR A N   1 
ATOM   444  C  CA  . TYR A 1 66  ? 74.303  20.297  1.875   1.00 39.76  ? 65  TYR A CA  1 
ATOM   445  C  C   . TYR A 1 66  ? 73.514  19.092  1.380   1.00 40.51  ? 65  TYR A C   1 
ATOM   446  O  O   . TYR A 1 66  ? 72.292  19.184  1.220   1.00 42.23  ? 65  TYR A O   1 
ATOM   447  C  CB  . TYR A 1 66  ? 74.724  21.191  0.709   1.00 39.49  ? 65  TYR A CB  1 
ATOM   448  C  CG  . TYR A 1 66  ? 75.118  22.577  1.163   1.00 44.25  ? 65  TYR A CG  1 
ATOM   449  C  CD1 . TYR A 1 66  ? 74.176  23.448  1.695   1.00 42.36  ? 65  TYR A CD1 1 
ATOM   450  C  CD2 . TYR A 1 66  ? 76.437  23.004  1.087   1.00 42.15  ? 65  TYR A CD2 1 
ATOM   451  C  CE1 . TYR A 1 66  ? 74.535  24.711  2.127   1.00 45.12  ? 65  TYR A CE1 1 
ATOM   452  C  CE2 . TYR A 1 66  ? 76.805  24.265  1.514   1.00 43.41  ? 65  TYR A CE2 1 
ATOM   453  C  CZ  . TYR A 1 66  ? 75.850  25.113  2.033   1.00 43.50  ? 65  TYR A CZ  1 
ATOM   454  O  OH  . TYR A 1 66  ? 76.211  26.370  2.456   1.00 46.06  ? 65  TYR A OH  1 
ATOM   455  N  N   . VAL A 1 67  ? 74.183  17.963  1.135   1.00 35.90  ? 66  VAL A N   1 
ATOM   456  C  CA  . VAL A 1 67  ? 73.458  16.731  0.838   1.00 42.94  ? 66  VAL A CA  1 
ATOM   457  C  C   . VAL A 1 67  ? 72.576  16.341  2.017   1.00 40.34  ? 66  VAL A C   1 
ATOM   458  O  O   . VAL A 1 67  ? 71.405  15.978  1.845   1.00 43.35  ? 66  VAL A O   1 
ATOM   459  C  CB  . VAL A 1 67  ? 74.438  15.605  0.460   1.00 45.85  ? 66  VAL A CB  1 
ATOM   460  C  CG1 . VAL A 1 67  ? 73.758  14.251  0.565   1.00 42.02  ? 66  VAL A CG1 1 
ATOM   461  C  CG2 . VAL A 1 67  ? 74.967  15.816  -0.950  1.00 42.68  ? 66  VAL A CG2 1 
ATOM   462  N  N   . ALA A 1 68  ? 73.122  16.414  3.234   1.00 39.18  ? 67  ALA A N   1 
ATOM   463  C  CA  . ALA A 1 68  ? 72.323  16.173  4.431   1.00 48.08  ? 67  ALA A CA  1 
ATOM   464  C  C   . ALA A 1 68  ? 71.154  17.145  4.527   1.00 44.41  ? 67  ALA A C   1 
ATOM   465  O  O   . ALA A 1 68  ? 70.028  16.743  4.843   1.00 49.42  ? 67  ALA A O   1 
ATOM   466  C  CB  . ALA A 1 68  ? 73.203  16.269  5.676   1.00 42.69  ? 67  ALA A CB  1 
ATOM   467  N  N   . GLN A 1 69  ? 71.404  18.431  4.267   1.00 45.46  ? 68  GLN A N   1 
ATOM   468  C  CA  . GLN A 1 69  ? 70.348  19.429  4.397   1.00 40.38  ? 68  GLN A CA  1 
ATOM   469  C  C   . GLN A 1 69  ? 69.208  19.171  3.422   1.00 44.61  ? 68  GLN A C   1 
ATOM   470  O  O   . GLN A 1 69  ? 68.042  19.417  3.752   1.00 50.42  ? 68  GLN A O   1 
ATOM   471  C  CB  . GLN A 1 69  ? 70.922  20.829  4.186   1.00 40.55  ? 68  GLN A CB  1 
ATOM   472  C  CG  . GLN A 1 69  ? 69.897  21.945  4.301   1.00 47.05  ? 68  GLN A CG  1 
ATOM   473  C  CD  . GLN A 1 69  ? 70.513  23.318  4.138   1.00 39.84  ? 68  GLN A CD  1 
ATOM   474  O  OE1 . GLN A 1 69  ? 71.654  23.550  4.535   1.00 41.33  ? 68  GLN A OE1 1 
ATOM   475  N  NE2 . GLN A 1 69  ? 69.757  24.238  3.550   1.00 43.13  ? 68  GLN A NE2 1 
ATOM   476  N  N   . TYR A 1 70  ? 69.516  18.670  2.225   1.00 42.52  ? 69  TYR A N   1 
ATOM   477  C  CA  . TYR A 1 70  ? 68.521  18.478  1.179   1.00 40.85  ? 69  TYR A CA  1 
ATOM   478  C  C   . TYR A 1 70  ? 68.278  17.005  0.868   1.00 43.93  ? 69  TYR A C   1 
ATOM   479  O  O   . TYR A 1 70  ? 67.844  16.676  -0.240  1.00 51.77  ? 69  TYR A O   1 
ATOM   480  C  CB  . TYR A 1 70  ? 68.938  19.221  -0.091  1.00 42.91  ? 69  TYR A CB  1 
ATOM   481  C  CG  . TYR A 1 70  ? 68.997  20.724  0.061   1.00 47.80  ? 69  TYR A CG  1 
ATOM   482  C  CD1 . TYR A 1 70  ? 67.852  21.460  0.333   1.00 46.71  ? 69  TYR A CD1 1 
ATOM   483  C  CD2 . TYR A 1 70  ? 70.199  21.407  -0.073  1.00 44.77  ? 69  TYR A CD2 1 
ATOM   484  C  CE1 . TYR A 1 70  ? 67.901  22.835  0.471   1.00 44.39  ? 69  TYR A CE1 1 
ATOM   485  C  CE2 . TYR A 1 70  ? 70.258  22.780  0.062   1.00 43.75  ? 69  TYR A CE2 1 
ATOM   486  C  CZ  . TYR A 1 70  ? 69.107  23.489  0.334   1.00 45.28  ? 69  TYR A CZ  1 
ATOM   487  O  OH  . TYR A 1 70  ? 69.163  24.857  0.469   1.00 50.58  ? 69  TYR A OH  1 
ATOM   488  N  N   . HIS A 1 71  ? 68.555  16.106  1.818   1.00 50.29  ? 70  HIS A N   1 
ATOM   489  C  CA  . HIS A 1 71  ? 68.410  14.681  1.541   1.00 55.00  ? 70  HIS A CA  1 
ATOM   490  C  C   . HIS A 1 71  ? 66.960  14.274  1.302   1.00 53.56  ? 70  HIS A C   1 
ATOM   491  O  O   . HIS A 1 71  ? 66.717  13.195  0.752   1.00 57.24  ? 70  HIS A O   1 
ATOM   492  C  CB  . HIS A 1 71  ? 69.015  13.856  2.680   1.00 59.95  ? 70  HIS A CB  1 
ATOM   493  C  CG  . HIS A 1 71  ? 68.071  13.589  3.810   1.00 66.08  ? 70  HIS A CG  1 
ATOM   494  N  ND1 . HIS A 1 71  ? 67.431  14.596  4.500   1.00 68.65  ? 70  HIS A ND1 1 
ATOM   495  C  CD2 . HIS A 1 71  ? 67.666  12.428  4.377   1.00 74.57  ? 70  HIS A CD2 1 
ATOM   496  C  CE1 . HIS A 1 71  ? 66.671  14.067  5.443   1.00 77.79  ? 70  HIS A CE1 1 
ATOM   497  N  NE2 . HIS A 1 71  ? 66.794  12.753  5.388   1.00 87.78  ? 70  HIS A NE2 1 
ATOM   498  N  N   . ASP A 1 72  ? 65.995  15.111  1.691   1.00 49.68  ? 71  ASP A N   1 
ATOM   499  C  CA  . ASP A 1 72  ? 64.588  14.881  1.387   1.00 52.94  ? 71  ASP A CA  1 
ATOM   500  C  C   . ASP A 1 72  ? 64.063  15.866  0.349   1.00 52.98  ? 71  ASP A C   1 
ATOM   501  O  O   . ASP A 1 72  ? 62.854  16.110  0.284   1.00 51.22  ? 71  ASP A O   1 
ATOM   502  C  CB  . ASP A 1 72  ? 63.742  14.952  2.660   1.00 52.90  ? 71  ASP A CB  1 
ATOM   503  C  CG  . ASP A 1 72  ? 63.942  13.750  3.562   1.00 61.17  ? 71  ASP A CG  1 
ATOM   504  O  OD1 . ASP A 1 72  ? 64.293  12.669  3.045   1.00 68.79  ? 71  ASP A OD1 1 
ATOM   505  O  OD2 . ASP A 1 72  ? 63.740  13.886  4.787   1.00 67.87  ? 71  ASP A OD2 1 
ATOM   506  N  N   . ASN A 1 73  ? 64.952  16.433  -0.466  1.00 44.03  ? 72  ASN A N   1 
ATOM   507  C  CA  . ASN A 1 73  ? 64.598  17.430  -1.473  1.00 40.01  ? 72  ASN A CA  1 
ATOM   508  C  C   . ASN A 1 73  ? 65.275  17.000  -2.766  1.00 47.10  ? 72  ASN A C   1 
ATOM   509  O  O   . ASN A 1 73  ? 66.423  17.382  -3.035  1.00 44.24  ? 72  ASN A O   1 
ATOM   510  C  CB  . ASN A 1 73  ? 65.029  18.832  -1.042  1.00 40.59  ? 72  ASN A CB  1 
ATOM   511  C  CG  . ASN A 1 73  ? 64.575  19.920  -2.008  1.00 45.64  ? 72  ASN A CG  1 
ATOM   512  O  OD1 . ASN A 1 73  ? 64.369  19.680  -3.198  1.00 44.60  ? 72  ASN A OD1 1 
ATOM   513  N  ND2 . ASN A 1 73  ? 64.426  21.133  -1.490  1.00 44.99  ? 72  ASN A ND2 1 
ATOM   514  N  N   . PRO A 1 74  ? 64.593  16.206  -3.597  1.00 50.65  ? 73  PRO A N   1 
ATOM   515  C  CA  . PRO A 1 74  ? 65.260  15.657  -4.791  1.00 46.39  ? 73  PRO A CA  1 
ATOM   516  C  C   . PRO A 1 74  ? 65.746  16.724  -5.756  1.00 45.89  ? 73  PRO A C   1 
ATOM   517  O  O   . PRO A 1 74  ? 66.826  16.577  -6.343  1.00 51.23  ? 73  PRO A O   1 
ATOM   518  C  CB  . PRO A 1 74  ? 64.171  14.774  -5.420  1.00 40.32  ? 73  PRO A CB  1 
ATOM   519  C  CG  . PRO A 1 74  ? 63.230  14.466  -4.292  1.00 45.04  ? 73  PRO A CG  1 
ATOM   520  C  CD  . PRO A 1 74  ? 63.217  15.702  -3.449  1.00 39.55  ? 73  PRO A CD  1 
ATOM   521  N  N   . GLN A 1 75  ? 64.972  17.795  -5.943  1.00 45.05  ? 74  GLN A N   1 
ATOM   522  C  CA  . GLN A 1 75  ? 65.354  18.836  -6.894  1.00 47.65  ? 74  GLN A CA  1 
ATOM   523  C  C   . GLN A 1 75  ? 66.634  19.538  -6.453  1.00 46.87  ? 74  GLN A C   1 
ATOM   524  O  O   . GLN A 1 75  ? 67.568  19.706  -7.245  1.00 49.18  ? 74  GLN A O   1 
ATOM   525  C  CB  . GLN A 1 75  ? 64.211  19.839  -7.060  1.00 44.26  ? 74  GLN A CB  1 
ATOM   526  C  CG  . GLN A 1 75  ? 62.995  19.294  -7.802  1.00 41.31  ? 74  GLN A CG  1 
ATOM   527  C  CD  . GLN A 1 75  ? 62.193  18.300  -6.979  1.00 49.41  ? 74  GLN A CD  1 
ATOM   528  O  OE1 . GLN A 1 75  ? 62.279  18.281  -5.750  1.00 47.99  ? 74  GLN A OE1 1 
ATOM   529  N  NE2 . GLN A 1 75  ? 61.414  17.464  -7.655  1.00 51.22  ? 74  GLN A NE2 1 
ATOM   530  N  N   . GLN A 1 76  ? 66.693  19.957  -5.187  1.00 44.54  ? 75  GLN A N   1 
ATOM   531  C  CA  . GLN A 1 76  ? 67.895  20.615  -4.683  1.00 46.89  ? 75  GLN A CA  1 
ATOM   532  C  C   . GLN A 1 76  ? 69.054  19.634  -4.561  1.00 48.55  ? 75  GLN A C   1 
ATOM   533  O  O   . GLN A 1 76  ? 70.210  19.999  -4.810  1.00 45.48  ? 75  GLN A O   1 
ATOM   534  C  CB  . GLN A 1 76  ? 67.608  21.282  -3.339  1.00 47.99  ? 75  GLN A CB  1 
ATOM   535  C  CG  . GLN A 1 76  ? 67.057  22.692  -3.454  1.00 50.31  ? 75  GLN A CG  1 
ATOM   536  C  CD  . GLN A 1 76  ? 68.082  23.667  -4.000  1.00 52.33  ? 75  GLN A CD  1 
ATOM   537  O  OE1 . GLN A 1 76  ? 68.177  23.874  -5.210  1.00 57.34  ? 75  GLN A OE1 1 
ATOM   538  N  NE2 . GLN A 1 76  ? 68.859  24.269  -3.107  1.00 50.36  ? 75  GLN A NE2 1 
ATOM   539  N  N   . LEU A 1 77  ? 68.768  18.392  -4.160  1.00 43.25  ? 76  LEU A N   1 
ATOM   540  C  CA  . LEU A 1 77  ? 69.820  17.387  -4.036  1.00 41.50  ? 76  LEU A CA  1 
ATOM   541  C  C   . LEU A 1 77  ? 70.535  17.169  -5.363  1.00 46.60  ? 76  LEU A C   1 
ATOM   542  O  O   . LEU A 1 77  ? 71.768  17.085  -5.407  1.00 43.33  ? 76  LEU A O   1 
ATOM   543  C  CB  . LEU A 1 77  ? 69.231  16.073  -3.523  1.00 39.41  ? 76  LEU A CB  1 
ATOM   544  C  CG  . LEU A 1 77  ? 70.203  15.015  -3.002  1.00 46.00  ? 76  LEU A CG  1 
ATOM   545  C  CD1 . LEU A 1 77  ? 71.185  15.618  -2.009  1.00 47.99  ? 76  LEU A CD1 1 
ATOM   546  C  CD2 . LEU A 1 77  ? 69.430  13.870  -2.370  1.00 41.03  ? 76  LEU A CD2 1 
ATOM   547  N  N   . ARG A 1 78  ? 69.775  17.070  -6.457  1.00 45.22  ? 77  ARG A N   1 
ATOM   548  C  CA  . ARG A 1 78  ? 70.389  16.943  -7.774  1.00 42.49  ? 77  ARG A CA  1 
ATOM   549  C  C   . ARG A 1 78  ? 71.255  18.153  -8.095  1.00 42.28  ? 77  ARG A C   1 
ATOM   550  O  O   . ARG A 1 78  ? 72.351  18.013  -8.650  1.00 40.26  ? 77  ARG A O   1 
ATOM   551  C  CB  . ARG A 1 78  ? 69.308  16.746  -8.836  1.00 41.20  ? 77  ARG A CB  1 
ATOM   552  C  CG  . ARG A 1 78  ? 69.827  16.182  -10.145 1.00 47.88  ? 77  ARG A CG  1 
ATOM   553  C  CD  . ARG A 1 78  ? 68.912  16.523  -11.307 1.00 47.26  ? 77  ARG A CD  1 
ATOM   554  N  NE  . ARG A 1 78  ? 67.789  15.596  -11.386 1.00 61.96  ? 77  ARG A NE  1 
ATOM   555  C  CZ  . ARG A 1 78  ? 67.843  14.407  -11.972 1.00 65.16  ? 77  ARG A CZ  1 
ATOM   556  N  NH1 . ARG A 1 78  ? 68.954  13.969  -12.542 1.00 61.47  ? 77  ARG A NH1 1 
ATOM   557  N  NH2 . ARG A 1 78  ? 66.760  13.637  -11.980 1.00 63.59  ? 77  ARG A NH2 1 
ATOM   558  N  N   . ARG A 1 79  ? 70.779  19.352  -7.752  1.00 43.70  ? 78  ARG A N   1 
ATOM   559  C  CA  . ARG A 1 79  ? 71.570  20.557  -7.978  1.00 44.68  ? 78  ARG A CA  1 
ATOM   560  C  C   . ARG A 1 79  ? 72.853  20.535  -7.155  1.00 45.05  ? 78  ARG A C   1 
ATOM   561  O  O   . ARG A 1 79  ? 73.921  20.923  -7.645  1.00 46.10  ? 78  ARG A O   1 
ATOM   562  C  CB  . ARG A 1 79  ? 70.736  21.793  -7.643  1.00 46.25  ? 78  ARG A CB  1 
ATOM   563  C  CG  . ARG A 1 79  ? 70.000  22.394  -8.827  1.00 45.95  ? 78  ARG A CG  1 
ATOM   564  C  CD  . ARG A 1 79  ? 68.928  23.370  -8.368  1.00 52.84  ? 78  ARG A CD  1 
ATOM   565  N  NE  . ARG A 1 79  ? 67.603  23.012  -8.861  1.00 54.13  ? 78  ARG A NE  1 
ATOM   566  C  CZ  . ARG A 1 79  ? 66.540  22.834  -8.089  1.00 53.41  ? 78  ARG A CZ  1 
ATOM   567  N  NH1 . ARG A 1 79  ? 66.606  22.988  -6.777  1.00 56.77  ? 78  ARG A NH1 1 
ATOM   568  N  NH2 . ARG A 1 79  ? 65.380  22.501  -8.648  1.00 57.80  ? 78  ARG A NH2 1 
ATOM   569  N  N   . VAL A 1 80  ? 72.765  20.086  -5.900  1.00 42.96  ? 79  VAL A N   1 
ATOM   570  C  CA  . VAL A 1 80  ? 73.939  20.033  -5.031  1.00 41.53  ? 79  VAL A CA  1 
ATOM   571  C  C   . VAL A 1 80  ? 74.991  19.098  -5.618  1.00 41.63  ? 79  VAL A C   1 
ATOM   572  O  O   . VAL A 1 80  ? 76.161  19.467  -5.774  1.00 43.33  ? 79  VAL A O   1 
ATOM   573  C  CB  . VAL A 1 80  ? 73.532  19.602  -3.609  1.00 45.65  ? 79  VAL A CB  1 
ATOM   574  C  CG1 . VAL A 1 80  ? 74.734  19.060  -2.848  1.00 41.54  ? 79  VAL A CG1 1 
ATOM   575  C  CG2 . VAL A 1 80  ? 72.894  20.761  -2.859  1.00 41.02  ? 79  VAL A CG2 1 
ATOM   576  N  N   . VAL A 1 81  ? 74.581  17.875  -5.961  1.00 40.20  ? 80  VAL A N   1 
ATOM   577  C  CA  . VAL A 1 81  ? 75.521  16.881  -6.469  1.00 39.51  ? 80  VAL A CA  1 
ATOM   578  C  C   . VAL A 1 81  ? 76.043  17.289  -7.841  1.00 42.74  ? 80  VAL A C   1 
ATOM   579  O  O   . VAL A 1 81  ? 77.219  17.076  -8.162  1.00 42.24  ? 80  VAL A O   1 
ATOM   580  C  CB  . VAL A 1 81  ? 74.852  15.495  -6.507  1.00 41.04  ? 80  VAL A CB  1 
ATOM   581  C  CG1 . VAL A 1 81  ? 75.794  14.456  -7.092  1.00 43.84  ? 80  VAL A CG1 1 
ATOM   582  C  CG2 . VAL A 1 81  ? 74.393  15.089  -5.116  1.00 39.85  ? 80  VAL A CG2 1 
ATOM   583  N  N   . GLY A 1 82  ? 75.186  17.890  -8.668  1.00 45.44  ? 81  GLY A N   1 
ATOM   584  C  CA  . GLY A 1 82  ? 75.634  18.333  -9.979  1.00 42.17  ? 81  GLY A CA  1 
ATOM   585  C  C   . GLY A 1 82  ? 76.682  19.425  -9.899  1.00 43.84  ? 81  GLY A C   1 
ATOM   586  O  O   . GLY A 1 82  ? 77.703  19.374  -10.589 1.00 47.35  ? 81  GLY A O   1 
ATOM   587  N  N   . THR A 1 83  ? 76.444  20.433  -9.055  1.00 39.17  ? 82  THR A N   1 
ATOM   588  C  CA  . THR A 1 83  ? 77.430  21.496  -8.890  1.00 44.67  ? 82  THR A CA  1 
ATOM   589  C  C   . THR A 1 83  ? 78.714  20.966  -8.260  1.00 46.19  ? 82  THR A C   1 
ATOM   590  O  O   . THR A 1 83  ? 79.817  21.347  -8.673  1.00 44.66  ? 82  THR A O   1 
ATOM   591  C  CB  . THR A 1 83  ? 76.843  22.633  -8.051  1.00 46.51  ? 82  THR A CB  1 
ATOM   592  O  OG1 . THR A 1 83  ? 75.817  23.296  -8.799  1.00 45.49  ? 82  THR A OG1 1 
ATOM   593  C  CG2 . THR A 1 83  ? 77.921  23.648  -7.688  1.00 42.02  ? 82  THR A CG2 1 
ATOM   594  N  N   . SER A 1 84  ? 78.593  20.072  -7.274  1.00 43.43  ? 83  SER A N   1 
ATOM   595  C  CA  . SER A 1 84  ? 79.781  19.481  -6.665  1.00 47.56  ? 83  SER A CA  1 
ATOM   596  C  C   . SER A 1 84  ? 80.579  18.680  -7.684  1.00 52.18  ? 83  SER A C   1 
ATOM   597  O  O   . SER A 1 84  ? 81.815  18.737  -7.700  1.00 48.94  ? 83  SER A O   1 
ATOM   598  C  CB  . SER A 1 84  ? 79.383  18.601  -5.481  1.00 40.24  ? 83  SER A CB  1 
ATOM   599  O  OG  . SER A 1 84  ? 78.629  19.334  -4.533  1.00 43.74  ? 83  SER A OG  1 
ATOM   600  N  N   . SER A 1 85  ? 79.889  17.921  -8.539  1.00 47.38  ? 84  SER A N   1 
ATOM   601  C  CA  . SER A 1 85  ? 80.574  17.177  -9.590  1.00 48.61  ? 84  SER A CA  1 
ATOM   602  C  C   . SER A 1 85  ? 81.297  18.119  -10.544 1.00 46.58  ? 84  SER A C   1 
ATOM   603  O  O   . SER A 1 85  ? 82.443  17.862  -10.932 1.00 56.54  ? 84  SER A O   1 
ATOM   604  C  CB  . SER A 1 85  ? 79.575  16.304  -10.348 1.00 49.97  ? 84  SER A CB  1 
ATOM   605  O  OG  . SER A 1 85  ? 80.053  15.985  -11.642 1.00 49.16  ? 84  SER A OG  1 
ATOM   606  N  N   . ALA A 1 86  ? 80.637  19.211  -10.939 1.00 44.85  ? 85  ALA A N   1 
ATOM   607  C  CA  . ALA A 1 86  ? 81.266  20.186  -11.825 1.00 49.01  ? 85  ALA A CA  1 
ATOM   608  C  C   . ALA A 1 86  ? 82.505  20.801  -11.186 1.00 47.39  ? 85  ALA A C   1 
ATOM   609  O  O   . ALA A 1 86  ? 83.521  21.012  -11.860 1.00 50.39  ? 85  ALA A O   1 
ATOM   610  C  CB  . ALA A 1 86  ? 80.264  21.274  -12.206 1.00 42.12  ? 85  ALA A CB  1 
ATOM   611  N  N   . MET A 1 87  ? 82.442  21.094  -9.885  1.00 45.99  ? 86  MET A N   1 
ATOM   612  C  CA  . MET A 1 87  ? 83.567  21.742  -9.219  1.00 44.96  ? 86  MET A CA  1 
ATOM   613  C  C   . MET A 1 87  ? 84.741  20.784  -9.062  1.00 50.26  ? 86  MET A C   1 
ATOM   614  O  O   . MET A 1 87  ? 85.901  21.183  -9.218  1.00 46.89  ? 86  MET A O   1 
ATOM   615  C  CB  . MET A 1 87  ? 83.135  22.291  -7.860  1.00 39.31  ? 86  MET A CB  1 
ATOM   616  C  CG  . MET A 1 87  ? 82.251  23.524  -7.942  1.00 49.15  ? 86  MET A CG  1 
ATOM   617  S  SD  . MET A 1 87  ? 81.564  23.993  -6.343  1.00 54.78  ? 86  MET A SD  1 
ATOM   618  C  CE  . MET A 1 87  ? 82.943  24.896  -5.642  1.00 44.72  ? 86  MET A CE  1 
ATOM   619  N  N   . VAL A 1 88  ? 84.460  19.517  -8.754  1.00 52.55  ? 87  VAL A N   1 
ATOM   620  C  CA  . VAL A 1 88  ? 85.530  18.533  -8.635  1.00 51.84  ? 87  VAL A CA  1 
ATOM   621  C  C   . VAL A 1 88  ? 86.118  18.218  -10.004 1.00 47.36  ? 87  VAL A C   1 
ATOM   622  O  O   . VAL A 1 88  ? 87.341  18.144  -10.165 1.00 49.39  ? 87  VAL A O   1 
ATOM   623  C  CB  . VAL A 1 88  ? 85.011  17.265  -7.933  1.00 52.54  ? 87  VAL A CB  1 
ATOM   624  C  CG1 . VAL A 1 88  ? 85.994  16.116  -8.107  1.00 49.49  ? 87  VAL A CG1 1 
ATOM   625  C  CG2 . VAL A 1 88  ? 84.759  17.540  -6.460  1.00 48.28  ? 87  VAL A CG2 1 
ATOM   626  N  N   . LEU A 1 89  ? 85.262  18.035  -11.012 1.00 48.02  ? 88  LEU A N   1 
ATOM   627  C  CA  . LEU A 1 89  ? 85.752  17.796  -12.366 1.00 53.42  ? 88  LEU A CA  1 
ATOM   628  C  C   . LEU A 1 89  ? 86.592  18.969  -12.858 1.00 53.76  ? 88  LEU A C   1 
ATOM   629  O  O   . LEU A 1 89  ? 87.699  18.782  -13.376 1.00 53.91  ? 88  LEU A O   1 
ATOM   630  C  CB  . LEU A 1 89  ? 84.579  17.540  -13.314 1.00 61.08  ? 88  LEU A CB  1 
ATOM   631  C  CG  . LEU A 1 89  ? 84.816  17.865  -14.792 1.00 63.06  ? 88  LEU A CG  1 
ATOM   632  C  CD1 . LEU A 1 89  ? 85.566  16.735  -15.488 1.00 69.51  ? 88  LEU A CD1 1 
ATOM   633  C  CD2 . LEU A 1 89  ? 83.505  18.169  -15.504 1.00 64.22  ? 88  LEU A CD2 1 
ATOM   634  N  N   . GLY A 1 90  ? 86.079  20.192  -12.701 1.00 52.14  ? 89  GLY A N   1 
ATOM   635  C  CA  . GLY A 1 90  ? 86.795  21.354  -13.204 1.00 46.64  ? 89  GLY A CA  1 
ATOM   636  C  C   . GLY A 1 90  ? 88.141  21.555  -12.534 1.00 53.74  ? 89  GLY A C   1 
ATOM   637  O  O   . GLY A 1 90  ? 89.149  21.801  -13.200 1.00 57.98  ? 89  GLY A O   1 
ATOM   638  N  N   . PHE A 1 91  ? 88.177  21.450  -11.203 1.00 53.05  ? 90  PHE A N   1 
ATOM   639  C  CA  . PHE A 1 91  ? 89.426  21.691  -10.487 1.00 53.80  ? 90  PHE A CA  1 
ATOM   640  C  C   . PHE A 1 91  ? 90.421  20.557  -10.703 1.00 54.34  ? 90  PHE A C   1 
ATOM   641  O  O   . PHE A 1 91  ? 91.615  20.806  -10.906 1.00 52.48  ? 90  PHE A O   1 
ATOM   642  C  CB  . PHE A 1 91  ? 89.156  21.890  -8.996  1.00 51.13  ? 90  PHE A CB  1 
ATOM   643  C  CG  . PHE A 1 91  ? 90.310  22.497  -8.251  1.00 55.45  ? 90  PHE A CG  1 
ATOM   644  C  CD1 . PHE A 1 91  ? 90.509  23.869  -8.248  1.00 61.31  ? 90  PHE A CD1 1 
ATOM   645  C  CD2 . PHE A 1 91  ? 91.206  21.696  -7.564  1.00 52.78  ? 90  PHE A CD2 1 
ATOM   646  C  CE1 . PHE A 1 91  ? 91.574  24.428  -7.565  1.00 54.36  ? 90  PHE A CE1 1 
ATOM   647  C  CE2 . PHE A 1 91  ? 92.272  22.250  -6.882  1.00 56.01  ? 90  PHE A CE2 1 
ATOM   648  C  CZ  . PHE A 1 91  ? 92.455  23.616  -6.882  1.00 50.81  ? 90  PHE A CZ  1 
ATOM   649  N  N   . SER A 1 92  ? 89.953  19.307  -10.655 1.00 54.96  ? 91  SER A N   1 
ATOM   650  C  CA  . SER A 1 92  ? 90.849  18.174  -10.873 1.00 53.97  ? 91  SER A CA  1 
ATOM   651  C  C   . SER A 1 92  ? 91.438  18.205  -12.277 1.00 51.35  ? 91  SER A C   1 
ATOM   652  O  O   . SER A 1 92  ? 92.604  17.841  -12.478 1.00 50.87  ? 91  SER A O   1 
ATOM   653  C  CB  . SER A 1 92  ? 90.112  16.858  -10.627 1.00 51.09  ? 91  SER A CB  1 
ATOM   654  O  OG  . SER A 1 92  ? 91.007  15.840  -10.214 1.00 63.87  ? 91  SER A OG  1 
ATOM   655  N  N   . THR A 1 93  ? 90.646  18.631  -13.263 1.00 51.05  ? 92  THR A N   1 
ATOM   656  C  CA  . THR A 1 93  ? 91.168  18.781  -14.617 1.00 57.15  ? 92  THR A CA  1 
ATOM   657  C  C   . THR A 1 93  ? 92.232  19.869  -14.671 1.00 59.74  ? 92  THR A C   1 
ATOM   658  O  O   . THR A 1 93  ? 93.298  19.682  -15.271 1.00 53.10  ? 92  THR A O   1 
ATOM   659  C  CB  . THR A 1 93  ? 90.028  19.092  -15.588 1.00 55.37  ? 92  THR A CB  1 
ATOM   660  O  OG1 . THR A 1 93  ? 89.143  17.968  -15.663 1.00 61.26  ? 92  THR A OG1 1 
ATOM   661  C  CG2 . THR A 1 93  ? 90.571  19.405  -16.976 1.00 58.81  ? 92  THR A CG2 1 
ATOM   662  N  N   . LEU A 1 94  ? 91.956  21.022  -14.055 1.00 58.45  ? 93  LEU A N   1 
ATOM   663  C  CA  . LEU A 1 94  ? 92.961  22.078  -13.986 1.00 59.78  ? 93  LEU A CA  1 
ATOM   664  C  C   . LEU A 1 94  ? 94.215  21.587  -13.276 1.00 59.10  ? 93  LEU A C   1 
ATOM   665  O  O   . LEU A 1 94  ? 95.338  21.894  -13.695 1.00 59.58  ? 93  LEU A O   1 
ATOM   666  C  CB  . LEU A 1 94  ? 92.390  23.312  -13.288 1.00 59.93  ? 93  LEU A CB  1 
ATOM   667  C  CG  . LEU A 1 94  ? 91.734  24.388  -14.160 1.00 71.12  ? 93  LEU A CG  1 
ATOM   668  C  CD1 . LEU A 1 94  ? 90.936  23.787  -15.311 1.00 68.08  ? 93  LEU A CD1 1 
ATOM   669  C  CD2 . LEU A 1 94  ? 90.853  25.290  -13.311 1.00 78.05  ? 93  LEU A CD2 1 
ATOM   670  N  N   . MET A 1 95  ? 94.042  20.826  -12.191 1.00 58.26  ? 94  MET A N   1 
ATOM   671  C  CA  . MET A 1 95  ? 95.188  20.274  -11.477 1.00 56.24  ? 94  MET A CA  1 
ATOM   672  C  C   . MET A 1 95  ? 95.984  19.327  -12.363 1.00 57.92  ? 94  MET A C   1 
ATOM   673  O  O   . MET A 1 95  ? 97.221  19.353  -12.359 1.00 59.46  ? 94  MET A O   1 
ATOM   674  C  CB  . MET A 1 95  ? 94.723  19.552  -10.212 1.00 56.28  ? 94  MET A CB  1 
ATOM   675  C  CG  . MET A 1 95  ? 94.510  20.460  -9.015  1.00 57.96  ? 94  MET A CG  1 
ATOM   676  S  SD  . MET A 1 95  ? 95.983  20.583  -7.986  1.00 73.44  ? 94  MET A SD  1 
ATOM   677  C  CE  . MET A 1 95  ? 96.595  22.195  -8.472  1.00 70.39  ? 94  MET A CE  1 
ATOM   678  N  N   . ALA A 1 96  ? 95.290  18.474  -13.122 1.00 54.29  ? 95  ALA A N   1 
ATOM   679  C  CA  . ALA A 1 96  ? 95.976  17.541  -14.010 1.00 57.43  ? 95  ALA A CA  1 
ATOM   680  C  C   . ALA A 1 96  ? 96.811  18.276  -15.050 1.00 62.30  ? 95  ALA A C   1 
ATOM   681  O  O   . ALA A 1 96  ? 97.917  17.840  -15.391 1.00 61.80  ? 95  ALA A O   1 
ATOM   682  C  CB  . ALA A 1 96  ? 94.962  16.621  -14.689 1.00 55.28  ? 95  ALA A CB  1 
ATOM   683  N  N   . LEU A 1 97  ? 96.298  19.395  -15.568 1.00 63.28  ? 96  LEU A N   1 
ATOM   684  C  CA  . LEU A 1 97  ? 97.051  20.164  -16.553 1.00 59.70  ? 96  LEU A CA  1 
ATOM   685  C  C   . LEU A 1 97  ? 98.271  20.823  -15.922 1.00 61.40  ? 96  LEU A C   1 
ATOM   686  O  O   . LEU A 1 97  ? 99.357  20.825  -16.513 1.00 66.58  ? 96  LEU A O   1 
ATOM   687  C  CB  . LEU A 1 97  ? 96.147  21.209  -17.206 1.00 63.33  ? 96  LEU A CB  1 
ATOM   688  C  CG  . LEU A 1 97  ? 94.971  20.653  -18.014 1.00 75.59  ? 96  LEU A CG  1 
ATOM   689  C  CD1 . LEU A 1 97  ? 93.912  21.722  -18.246 1.00 79.68  ? 96  LEU A CD1 1 
ATOM   690  C  CD2 . LEU A 1 97  ? 95.453  20.074  -19.336 1.00 71.94  ? 96  LEU A CD2 1 
ATOM   691  N  N   . VAL A 1 98  ? 98.110  21.398  -14.728 1.00 59.40  ? 97  VAL A N   1 
ATOM   692  C  CA  . VAL A 1 98  ? 99.239  22.016  -14.036 1.00 63.35  ? 97  VAL A CA  1 
ATOM   693  C  C   . VAL A 1 98  ? 100.314 20.978  -13.735 1.00 64.97  ? 97  VAL A C   1 
ATOM   694  O  O   . VAL A 1 98  ? 101.515 21.248  -13.862 1.00 63.22  ? 97  VAL A O   1 
ATOM   695  C  CB  . VAL A 1 98  ? 98.754  22.722  -12.755 1.00 65.11  ? 97  VAL A CB  1 
ATOM   696  C  CG1 . VAL A 1 98  ? 99.884  22.846  -11.740 1.00 56.88  ? 97  VAL A CG1 1 
ATOM   697  C  CG2 . VAL A 1 98  ? 98.172  24.087  -13.089 1.00 57.52  ? 97  VAL A CG2 1 
ATOM   698  N  N   . PHE A 1 99  ? 99.899  19.765  -13.362 1.00 62.22  ? 98  PHE A N   1 
ATOM   699  C  CA  . PHE A 1 99  ? 100.863 18.725  -13.021 1.00 63.00  ? 98  PHE A CA  1 
ATOM   700  C  C   . PHE A 1 99  ? 101.643 18.275  -14.251 1.00 65.46  ? 98  PHE A C   1 
ATOM   701  O  O   . PHE A 1 99  ? 102.870 18.129  -14.201 1.00 65.70  ? 98  PHE A O   1 
ATOM   702  C  CB  . PHE A 1 99  ? 100.144 17.541  -12.375 1.00 59.46  ? 98  PHE A CB  1 
ATOM   703  C  CG  . PHE A 1 99  ? 100.177 17.551  -10.873 1.00 64.20  ? 98  PHE A CG  1 
ATOM   704  C  CD1 . PHE A 1 99  ? 99.747  18.662  -10.165 1.00 66.02  ? 98  PHE A CD1 1 
ATOM   705  C  CD2 . PHE A 1 99  ? 100.636 16.450  -10.169 1.00 67.00  ? 98  PHE A CD2 1 
ATOM   706  C  CE1 . PHE A 1 99  ? 99.772  18.673  -8.783  1.00 65.69  ? 98  PHE A CE1 1 
ATOM   707  C  CE2 . PHE A 1 99  ? 100.665 16.458  -8.786  1.00 71.19  ? 98  PHE A CE2 1 
ATOM   708  C  CZ  . PHE A 1 99  ? 100.233 17.570  -8.093  1.00 67.13  ? 98  PHE A CZ  1 
ATOM   709  N  N   . VAL A 1 100 ? 100.945 18.048  -15.368 1.00 63.95  ? 99  VAL A N   1 
ATOM   710  C  CA  . VAL A 1 100 ? 101.613 17.542  -16.563 1.00 66.84  ? 99  VAL A CA  1 
ATOM   711  C  C   . VAL A 1 100 ? 102.478 18.627  -17.198 1.00 64.19  ? 99  VAL A C   1 
ATOM   712  O  O   . VAL A 1 100 ? 103.547 18.334  -17.748 1.00 53.10  ? 99  VAL A O   1 
ATOM   713  C  CB  . VAL A 1 100 ? 100.579 16.972  -17.558 1.00 59.49  ? 99  VAL A CB  1 
ATOM   714  C  CG1 . VAL A 1 100 ? 99.712  18.076  -18.149 1.00 64.36  ? 99  VAL A CG1 1 
ATOM   715  C  CG2 . VAL A 1 100 ? 101.271 16.190  -18.662 1.00 61.43  ? 99  VAL A CG2 1 
ATOM   716  N  N   . LEU A 1 101 ? 102.044 19.888  -17.130 1.00 64.88  ? 100 LEU A N   1 
ATOM   717  C  CA  . LEU A 1 101 ? 102.803 20.969  -17.750 1.00 65.16  ? 100 LEU A CA  1 
ATOM   718  C  C   . LEU A 1 101 ? 104.070 21.279  -16.964 1.00 60.21  ? 100 LEU A C   1 
ATOM   719  O  O   . LEU A 1 101 ? 105.122 21.550  -17.554 1.00 62.41  ? 100 LEU A O   1 
ATOM   720  C  CB  . LEU A 1 101 ? 101.932 22.219  -17.872 1.00 66.67  ? 100 LEU A CB  1 
ATOM   721  C  CG  . LEU A 1 101 ? 101.345 22.534  -19.250 1.00 71.29  ? 100 LEU A CG  1 
ATOM   722  C  CD1 . LEU A 1 101 ? 102.455 22.830  -20.246 1.00 76.11  ? 100 LEU A CD1 1 
ATOM   723  C  CD2 . LEU A 1 101 ? 100.474 21.389  -19.743 1.00 71.56  ? 100 LEU A CD2 1 
ATOM   724  N  N   . ALA A 1 102 ? 103.993 21.243  -15.637 1.00 60.95  ? 101 ALA A N   1 
ATOM   725  C  CA  . ALA A 1 102 ? 105.120 21.567  -14.769 1.00 60.60  ? 101 ALA A CA  1 
ATOM   726  C  C   . ALA A 1 102 ? 105.674 20.328  -14.074 1.00 57.39  ? 101 ALA A C   1 
ATOM   727  O  O   . ALA A 1 102 ? 106.102 20.386  -12.920 1.00 60.56  ? 101 ALA A O   1 
ATOM   728  C  CB  . ALA A 1 102 ? 104.721 22.620  -13.739 1.00 55.66  ? 101 ALA A CB  1 
ATOM   729  N  N   . ALA A 1 103 ? 105.665 19.188  -14.769 1.00 55.26  ? 102 ALA A N   1 
ATOM   730  C  CA  . ALA A 1 103 ? 106.165 17.957  -14.165 1.00 60.78  ? 102 ALA A CA  1 
ATOM   731  C  C   . ALA A 1 103 ? 107.640 18.066  -13.797 1.00 62.90  ? 102 ALA A C   1 
ATOM   732  O  O   . ALA A 1 103 ? 108.081 17.453  -12.818 1.00 62.93  ? 102 ALA A O   1 
ATOM   733  C  CB  . ALA A 1 103 ? 105.938 16.777  -15.108 1.00 59.65  ? 102 ALA A CB  1 
ATOM   734  N  N   . ALA A 1 104 ? 108.418 18.834  -14.570 1.00 68.28  ? 103 ALA A N   1 
ATOM   735  C  CA  . ALA A 1 104 ? 109.838 18.980  -14.251 1.00 62.87  ? 103 ALA A CA  1 
ATOM   736  C  C   . ALA A 1 104 ? 110.068 19.843  -13.015 1.00 60.17  ? 103 ALA A C   1 
ATOM   737  O  O   . ALA A 1 104 ? 110.802 19.401  -12.112 1.00 61.78  ? 103 ALA A O   1 
ATOM   738  C  CB  . ALA A 1 104 ? 110.601 19.502  -15.475 1.00 64.55  ? 103 ALA A CB  1 
ATOM   739  N  N   . PRO A 1 105 ? 109.506 21.054  -12.896 1.00 61.56  ? 104 PRO A N   1 
ATOM   740  C  CA  . PRO A 1 105 ? 109.687 21.803  -11.640 1.00 62.81  ? 104 PRO A CA  1 
ATOM   741  C  C   . PRO A 1 105 ? 109.103 21.100  -10.427 1.00 68.08  ? 104 PRO A C   1 
ATOM   742  O  O   . PRO A 1 105 ? 109.660 21.218  -9.328  1.00 65.12  ? 104 PRO A O   1 
ATOM   743  C  CB  . PRO A 1 105 ? 108.974 23.135  -11.918 1.00 62.83  ? 104 PRO A CB  1 
ATOM   744  C  CG  . PRO A 1 105 ? 108.965 23.256  -13.400 1.00 70.80  ? 104 PRO A CG  1 
ATOM   745  C  CD  . PRO A 1 105 ? 108.784 21.860  -13.899 1.00 58.19  ? 104 PRO A CD  1 
ATOM   746  N  N   . ILE A 1 106 ? 107.996 20.373  -10.590 1.00 68.27  ? 105 ILE A N   1 
ATOM   747  C  CA  . ILE A 1 106 ? 107.411 19.648  -9.466  1.00 64.66  ? 105 ILE A CA  1 
ATOM   748  C  C   . ILE A 1 106 ? 108.323 18.507  -9.035  1.00 62.84  ? 105 ILE A C   1 
ATOM   749  O  O   . ILE A 1 106 ? 108.545 18.288  -7.838  1.00 65.77  ? 105 ILE A O   1 
ATOM   750  C  CB  . ILE A 1 106 ? 106.000 19.149  -9.828  1.00 58.17  ? 105 ILE A CB  1 
ATOM   751  C  CG1 . ILE A 1 106 ? 105.032 20.328  -9.931  1.00 53.31  ? 105 ILE A CG1 1 
ATOM   752  C  CG2 . ILE A 1 106 ? 105.506 18.142  -8.803  1.00 52.90  ? 105 ILE A CG2 1 
ATOM   753  C  CD1 . ILE A 1 106 ? 103.716 19.979  -10.586 1.00 60.70  ? 105 ILE A CD1 1 
ATOM   754  N  N   . SER A 1 107 ? 108.863 17.761  -10.003 1.00 59.33  ? 106 SER A N   1 
ATOM   755  C  CA  . SER A 1 107 ? 109.819 16.705  -9.684  1.00 62.15  ? 106 SER A CA  1 
ATOM   756  C  C   . SER A 1 107 ? 111.045 17.267  -8.975  1.00 68.98  ? 106 SER A C   1 
ATOM   757  O  O   . SER A 1 107 ? 111.569 16.648  -8.040  1.00 66.40  ? 106 SER A O   1 
ATOM   758  C  CB  . SER A 1 107 ? 110.225 15.963  -10.957 1.00 60.72  ? 106 SER A CB  1 
ATOM   759  O  OG  . SER A 1 107 ? 111.265 15.039  -10.698 1.00 63.46  ? 106 SER A OG  1 
ATOM   760  N  N   . GLN A 1 108 ? 111.523 18.435  -9.412  1.00 68.34  ? 107 GLN A N   1 
ATOM   761  C  CA  . GLN A 1 108 ? 112.681 19.048  -8.769  1.00 68.84  ? 107 GLN A CA  1 
ATOM   762  C  C   . GLN A 1 108 ? 112.388 19.391  -7.313  1.00 68.29  ? 107 GLN A C   1 
ATOM   763  O  O   . GLN A 1 108 ? 113.226 19.165  -6.433  1.00 63.82  ? 107 GLN A O   1 
ATOM   764  C  CB  . GLN A 1 108 ? 113.103 20.300  -9.539  1.00 70.41  ? 107 GLN A CB  1 
ATOM   765  C  CG  . GLN A 1 108 ? 114.311 21.015  -8.957  1.00 72.32  ? 107 GLN A CG  1 
ATOM   766  C  CD  . GLN A 1 108 ? 115.586 20.206  -9.078  1.00 71.68  ? 107 GLN A CD  1 
ATOM   767  O  OE1 . GLN A 1 108 ? 115.835 19.564  -10.099 1.00 67.05  ? 107 GLN A OE1 1 
ATOM   768  N  NE2 . GLN A 1 108 ? 116.405 20.235  -8.033  1.00 66.46  ? 107 GLN A NE2 1 
ATOM   769  N  N   . GLY A 1 109 ? 111.203 19.940  -7.041  1.00 68.27  ? 108 GLY A N   1 
ATOM   770  C  CA  . GLY A 1 109 ? 110.852 20.291  -5.676  1.00 66.78  ? 108 GLY A CA  1 
ATOM   771  C  C   . GLY A 1 109 ? 110.582 19.089  -4.794  1.00 63.70  ? 108 GLY A C   1 
ATOM   772  O  O   . GLY A 1 109 ? 110.726 19.169  -3.570  1.00 61.51  ? 108 GLY A O   1 
ATOM   773  N  N   . LEU A 1 110 ? 110.186 17.966  -5.392  1.00 66.46  ? 109 LEU A N   1 
ATOM   774  C  CA  . LEU A 1 110 ? 109.838 16.770  -4.634  1.00 68.26  ? 109 LEU A CA  1 
ATOM   775  C  C   . LEU A 1 110 ? 111.049 15.884  -4.356  1.00 65.56  ? 109 LEU A C   1 
ATOM   776  O  O   . LEU A 1 110 ? 111.231 15.414  -3.228  1.00 62.20  ? 109 LEU A O   1 
ATOM   777  C  CB  . LEU A 1 110 ? 108.770 15.974  -5.388  1.00 58.94  ? 109 LEU A CB  1 
ATOM   778  C  CG  . LEU A 1 110 ? 107.331 16.481  -5.283  1.00 61.30  ? 109 LEU A CG  1 
ATOM   779  C  CD1 . LEU A 1 110 ? 106.415 15.667  -6.183  1.00 62.48  ? 109 LEU A CD1 1 
ATOM   780  C  CD2 . LEU A 1 110 ? 106.843 16.453  -3.845  1.00 60.92  ? 109 LEU A CD2 1 
ATOM   781  N  N   . PHE A 1 111 ? 111.886 15.655  -5.368  1.00 64.07  ? 110 PHE A N   1 
ATOM   782  C  CA  . PHE A 1 111 ? 112.965 14.680  -5.286  1.00 66.66  ? 110 PHE A CA  1 
ATOM   783  C  C   . PHE A 1 111 ? 114.357 15.282  -5.405  1.00 66.46  ? 110 PHE A C   1 
ATOM   784  O  O   . PHE A 1 111 ? 115.332 14.598  -5.075  1.00 65.44  ? 110 PHE A O   1 
ATOM   785  C  CB  . PHE A 1 111 ? 112.803 13.601  -6.370  1.00 67.02  ? 110 PHE A CB  1 
ATOM   786  C  CG  . PHE A 1 111 ? 111.458 12.934  -6.370  1.00 64.14  ? 110 PHE A CG  1 
ATOM   787  C  CD1 . PHE A 1 111 ? 111.227 11.822  -5.578  1.00 59.88  ? 110 PHE A CD1 1 
ATOM   788  C  CD2 . PHE A 1 111 ? 110.430 13.407  -7.168  1.00 65.91  ? 110 PHE A CD2 1 
ATOM   789  C  CE1 . PHE A 1 111 ? 109.995 11.199  -5.574  1.00 59.71  ? 110 PHE A CE1 1 
ATOM   790  C  CE2 . PHE A 1 111 ? 109.194 12.789  -7.169  1.00 62.81  ? 110 PHE A CE2 1 
ATOM   791  C  CZ  . PHE A 1 111 ? 108.976 11.683  -6.371  1.00 61.19  ? 110 PHE A CZ  1 
ATOM   792  N  N   . GLY A 1 112 ? 114.483 16.526  -5.860  1.00 63.79  ? 111 GLY A N   1 
ATOM   793  C  CA  . GLY A 1 112 ? 115.769 17.170  -6.009  1.00 61.94  ? 111 GLY A CA  1 
ATOM   794  C  C   . GLY A 1 112 ? 116.345 17.112  -7.407  1.00 72.02  ? 111 GLY A C   1 
ATOM   795  O  O   . GLY A 1 112 ? 117.385 17.733  -7.657  1.00 78.48  ? 111 GLY A O   1 
ATOM   796  N  N   . ASN A 1 113 ? 115.707 16.383  -8.319  1.00 73.79  ? 112 ASN A N   1 
ATOM   797  C  CA  . ASN A 1 113 ? 116.111 16.354  -9.716  1.00 67.40  ? 112 ASN A CA  1 
ATOM   798  C  C   . ASN A 1 113 ? 114.863 16.165  -10.571 1.00 66.78  ? 112 ASN A C   1 
ATOM   799  O  O   . ASN A 1 113 ? 113.742 16.091  -10.061 1.00 69.36  ? 112 ASN A O   1 
ATOM   800  C  CB  . ASN A 1 113 ? 117.157 15.261  -9.969  1.00 67.57  ? 112 ASN A CB  1 
ATOM   801  C  CG  . ASN A 1 113 ? 116.678 13.883  -9.556  1.00 66.70  ? 112 ASN A CG  1 
ATOM   802  O  OD1 . ASN A 1 113 ? 115.713 13.354  -10.106 1.00 62.15  ? 112 ASN A OD1 1 
ATOM   803  N  ND2 . ASN A 1 113 ? 117.359 13.292  -8.582  1.00 73.79  ? 112 ASN A ND2 1 
ATOM   804  N  N   . THR A 1 114 ? 115.066 16.088  -11.885 1.00 63.21  ? 113 THR A N   1 
ATOM   805  C  CA  . THR A 1 114 ? 113.971 16.036  -12.844 1.00 61.56  ? 113 THR A CA  1 
ATOM   806  C  C   . THR A 1 114 ? 113.706 14.630  -13.370 1.00 62.25  ? 113 THR A C   1 
ATOM   807  O  O   . THR A 1 114 ? 112.998 14.479  -14.371 1.00 63.40  ? 113 THR A O   1 
ATOM   808  C  CB  . THR A 1 114 ? 114.249 16.986  -14.012 1.00 60.34  ? 113 THR A CB  1 
ATOM   809  O  OG1 . THR A 1 114 ? 115.491 16.637  -14.634 1.00 70.96  ? 113 THR A OG1 1 
ATOM   810  C  CG2 . THR A 1 114 ? 114.324 18.423  -13.516 1.00 56.71  ? 113 THR A CG2 1 
ATOM   811  N  N   . ASP A 1 115 ? 114.245 13.602  -12.719 1.00 59.15  ? 114 ASP A N   1 
ATOM   812  C  CA  . ASP A 1 115 ? 114.158 12.240  -13.228 1.00 65.00  ? 114 ASP A CA  1 
ATOM   813  C  C   . ASP A 1 115 ? 112.806 11.585  -12.978 1.00 63.43  ? 114 ASP A C   1 
ATOM   814  O  O   . ASP A 1 115 ? 112.630 10.415  -13.334 1.00 65.27  ? 114 ASP A O   1 
ATOM   815  C  CB  . ASP A 1 115 ? 115.268 11.380  -12.618 1.00 70.70  ? 114 ASP A CB  1 
ATOM   816  C  CG  . ASP A 1 115 ? 116.651 11.872  -12.990 1.00 74.95  ? 114 ASP A CG  1 
ATOM   817  O  OD1 . ASP A 1 115 ? 116.751 12.705  -13.915 1.00 71.96  ? 114 ASP A OD1 1 
ATOM   818  O  OD2 . ASP A 1 115 ? 117.634 11.421  -12.366 1.00 71.98  ? 114 ASP A OD2 1 
ATOM   819  N  N   . TYR A 1 116 ? 111.850 12.300  -12.388 1.00 66.68  ? 115 TYR A N   1 
ATOM   820  C  CA  . TYR A 1 116 ? 110.574 11.723  -11.982 1.00 64.08  ? 115 TYR A CA  1 
ATOM   821  C  C   . TYR A 1 116 ? 109.403 12.397  -12.692 1.00 56.20  ? 115 TYR A C   1 
ATOM   822  O  O   . TYR A 1 116 ? 108.284 12.422  -12.175 1.00 56.38  ? 115 TYR A O   1 
ATOM   823  C  CB  . TYR A 1 116 ? 110.405 11.791  -10.464 1.00 65.51  ? 115 TYR A CB  1 
ATOM   824  C  CG  . TYR A 1 116 ? 111.456 11.008  -9.707  1.00 61.33  ? 115 TYR A CG  1 
ATOM   825  C  CD1 . TYR A 1 116 ? 112.705 11.556  -9.441  1.00 63.98  ? 115 TYR A CD1 1 
ATOM   826  C  CD2 . TYR A 1 116 ? 111.205 9.712   -9.273  1.00 63.53  ? 115 TYR A CD2 1 
ATOM   827  C  CE1 . TYR A 1 116 ? 113.671 10.839  -8.758  1.00 58.80  ? 115 TYR A CE1 1 
ATOM   828  C  CE2 . TYR A 1 116 ? 112.164 8.988   -8.588  1.00 68.49  ? 115 TYR A CE2 1 
ATOM   829  C  CZ  . TYR A 1 116 ? 113.394 9.556   -8.334  1.00 61.38  ? 115 TYR A CZ  1 
ATOM   830  O  OH  . TYR A 1 116 ? 114.348 8.837   -7.650  1.00 50.81  ? 115 TYR A OH  1 
ATOM   831  N  N   . GLN A 1 117 ? 109.659 12.957  -13.879 1.00 60.89  ? 116 GLN A N   1 
ATOM   832  C  CA  . GLN A 1 117 ? 108.613 13.649  -14.627 1.00 59.20  ? 116 GLN A CA  1 
ATOM   833  C  C   . GLN A 1 117 ? 107.482 12.700  -15.010 1.00 55.62  ? 116 GLN A C   1 
ATOM   834  O  O   . GLN A 1 117 ? 106.304 13.071  -14.953 1.00 55.51  ? 116 GLN A O   1 
ATOM   835  C  CB  . GLN A 1 117 ? 109.212 14.288  -15.880 1.00 65.05  ? 116 GLN A CB  1 
ATOM   836  C  CG  . GLN A 1 117 ? 109.780 15.680  -15.680 1.00 68.56  ? 116 GLN A CG  1 
ATOM   837  C  CD  . GLN A 1 117 ? 110.729 16.082  -16.795 1.00 80.42  ? 116 GLN A CD  1 
ATOM   838  O  OE1 . GLN A 1 117 ? 111.912 16.331  -16.560 1.00 79.28  ? 116 GLN A OE1 1 
ATOM   839  N  NE2 . GLN A 1 117 ? 110.218 16.129  -18.020 1.00 76.45  ? 116 GLN A NE2 1 
ATOM   840  N  N   . GLY A 1 118 ? 107.823 11.476  -15.417 1.00 51.31  ? 117 GLY A N   1 
ATOM   841  C  CA  . GLY A 1 118 ? 106.796 10.515  -15.786 1.00 49.42  ? 117 GLY A CA  1 
ATOM   842  C  C   . GLY A 1 118 ? 105.883 10.153  -14.630 1.00 56.69  ? 117 GLY A C   1 
ATOM   843  O  O   . GLY A 1 118 ? 104.668 10.031  -14.801 1.00 58.37  ? 117 GLY A O   1 
ATOM   844  N  N   . LEU A 1 119 ? 106.457 9.974   -13.437 1.00 56.09  ? 118 LEU A N   1 
ATOM   845  C  CA  . LEU A 1 119 ? 105.644 9.676   -12.262 1.00 50.63  ? 118 LEU A CA  1 
ATOM   846  C  C   . LEU A 1 119 ? 104.716 10.837  -11.923 1.00 56.70  ? 118 LEU A C   1 
ATOM   847  O  O   . LEU A 1 119 ? 103.562 10.626  -11.534 1.00 61.11  ? 118 LEU A O   1 
ATOM   848  C  CB  . LEU A 1 119 ? 106.549 9.343   -11.076 1.00 54.28  ? 118 LEU A CB  1 
ATOM   849  C  CG  . LEU A 1 119 ? 105.893 9.256   -9.697  1.00 57.07  ? 118 LEU A CG  1 
ATOM   850  C  CD1 . LEU A 1 119 ? 104.865 8.133   -9.665  1.00 58.36  ? 118 LEU A CD1 1 
ATOM   851  C  CD2 . LEU A 1 119 ? 106.945 9.059   -8.616  1.00 59.66  ? 118 LEU A CD2 1 
ATOM   852  N  N   . VAL A 1 120 ? 105.203 12.071  -12.069 1.00 51.57  ? 119 VAL A N   1 
ATOM   853  C  CA  . VAL A 1 120 ? 104.369 13.239  -11.805 1.00 53.49  ? 119 VAL A CA  1 
ATOM   854  C  C   . VAL A 1 120 ? 103.225 13.317  -12.808 1.00 59.76  ? 119 VAL A C   1 
ATOM   855  O  O   . VAL A 1 120 ? 102.081 13.623  -12.447 1.00 59.95  ? 119 VAL A O   1 
ATOM   856  C  CB  . VAL A 1 120 ? 105.226 14.518  -11.815 1.00 53.83  ? 119 VAL A CB  1 
ATOM   857  C  CG1 . VAL A 1 120 ? 104.342 15.755  -11.781 1.00 51.42  ? 119 VAL A CG1 1 
ATOM   858  C  CG2 . VAL A 1 120 ? 106.192 14.516  -10.639 1.00 53.21  ? 119 VAL A CG2 1 
ATOM   859  N  N   . ARG A 1 121 ? 103.513 13.042  -14.083 1.00 62.03  ? 120 ARG A N   1 
ATOM   860  C  CA  . ARG A 1 121 ? 102.466 13.055  -15.099 1.00 59.82  ? 120 ARG A CA  1 
ATOM   861  C  C   . ARG A 1 121 ? 101.424 11.973  -14.838 1.00 57.99  ? 120 ARG A C   1 
ATOM   862  O  O   . ARG A 1 121 ? 100.233 12.173  -15.101 1.00 52.82  ? 120 ARG A O   1 
ATOM   863  C  CB  . ARG A 1 121 ? 103.084 12.887  -16.488 1.00 56.28  ? 120 ARG A CB  1 
ATOM   864  C  CG  . ARG A 1 121 ? 103.829 14.116  -16.982 1.00 53.35  ? 120 ARG A CG  1 
ATOM   865  C  CD  . ARG A 1 121 ? 104.180 13.997  -18.456 1.00 51.19  ? 120 ARG A CD  1 
ATOM   866  N  NE  . ARG A 1 121 ? 105.067 12.872  -18.724 1.00 58.62  ? 120 ARG A NE  1 
ATOM   867  C  CZ  . ARG A 1 121 ? 106.384 12.972  -18.835 1.00 58.91  ? 120 ARG A CZ  1 
ATOM   868  N  NH1 . ARG A 1 121 ? 106.999 14.139  -18.730 1.00 54.82  ? 120 ARG A NH1 1 
ATOM   869  N  NH2 . ARG A 1 121 ? 107.102 11.876  -19.065 1.00 57.09  ? 120 ARG A NH2 1 
ATOM   870  N  N   . LEU A 1 122 ? 101.852 10.820  -14.320 1.00 53.33  ? 121 LEU A N   1 
ATOM   871  C  CA  . LEU A 1 122 ? 100.890 9.794   -13.930 1.00 59.60  ? 121 LEU A CA  1 
ATOM   872  C  C   . LEU A 1 122 ? 100.037 10.260  -12.758 1.00 59.62  ? 121 LEU A C   1 
ATOM   873  O  O   . LEU A 1 122 ? 98.819  10.043  -12.746 1.00 57.47  ? 121 LEU A O   1 
ATOM   874  C  CB  . LEU A 1 122 ? 101.612 8.491   -13.586 1.00 61.30  ? 121 LEU A CB  1 
ATOM   875  C  CG  . LEU A 1 122 ? 102.053 7.610   -14.757 1.00 48.43  ? 121 LEU A CG  1 
ATOM   876  C  CD1 . LEU A 1 122 ? 102.134 6.155   -14.325 1.00 46.79  ? 121 LEU A CD1 1 
ATOM   877  C  CD2 . LEU A 1 122 ? 101.103 7.765   -15.935 1.00 51.09  ? 121 LEU A CD2 1 
ATOM   878  N  N   . VAL A 1 123 ? 100.658 10.903  -11.766 1.00 58.95  ? 122 VAL A N   1 
ATOM   879  C  CA  . VAL A 1 123 ? 99.917  11.408  -10.613 1.00 59.76  ? 122 VAL A CA  1 
ATOM   880  C  C   . VAL A 1 123 ? 98.866  12.421  -11.053 1.00 57.25  ? 122 VAL A C   1 
ATOM   881  O  O   . VAL A 1 123 ? 97.803  12.537  -10.428 1.00 49.20  ? 122 VAL A O   1 
ATOM   882  C  CB  . VAL A 1 123 ? 100.901 11.995  -9.578  1.00 60.01  ? 122 VAL A CB  1 
ATOM   883  C  CG1 . VAL A 1 123 ? 100.210 12.977  -8.643  1.00 57.77  ? 122 VAL A CG1 1 
ATOM   884  C  CG2 . VAL A 1 123 ? 101.558 10.875  -8.784  1.00 57.53  ? 122 VAL A CG2 1 
ATOM   885  N  N   . ALA A 1 124 ? 99.129  13.149  -12.144 1.00 57.24  ? 123 ALA A N   1 
ATOM   886  C  CA  . ALA A 1 124 ? 98.144  14.088  -12.672 1.00 56.33  ? 123 ALA A CA  1 
ATOM   887  C  C   . ALA A 1 124 ? 96.829  13.399  -13.007 1.00 57.50  ? 123 ALA A C   1 
ATOM   888  O  O   . ALA A 1 124 ? 95.762  14.013  -12.901 1.00 53.71  ? 123 ALA A O   1 
ATOM   889  C  CB  . ALA A 1 124 ? 98.695  14.786  -13.915 1.00 58.84  ? 123 ALA A CB  1 
ATOM   890  N  N   . LEU A 1 125 ? 96.883  12.134  -13.421 1.00 56.73  ? 124 LEU A N   1 
ATOM   891  C  CA  . LEU A 1 125 ? 95.672  11.365  -13.672 1.00 59.57  ? 124 LEU A CA  1 
ATOM   892  C  C   . LEU A 1 125 ? 95.186  10.638  -12.426 1.00 60.34  ? 124 LEU A C   1 
ATOM   893  O  O   . LEU A 1 125 ? 93.977  10.429  -12.270 1.00 60.26  ? 124 LEU A O   1 
ATOM   894  C  CB  . LEU A 1 125 ? 95.916  10.356  -14.798 1.00 63.09  ? 124 LEU A CB  1 
ATOM   895  C  CG  . LEU A 1 125 ? 96.321  10.946  -16.153 1.00 68.99  ? 124 LEU A CG  1 
ATOM   896  C  CD1 . LEU A 1 125 ? 96.382  9.865   -17.223 1.00 60.88  ? 124 LEU A CD1 1 
ATOM   897  C  CD2 . LEU A 1 125 ? 95.377  12.066  -16.566 1.00 72.37  ? 124 LEU A CD2 1 
ATOM   898  N  N   . VAL A 1 126 ? 96.107  10.246  -11.543 1.00 58.52  ? 125 VAL A N   1 
ATOM   899  C  CA  . VAL A 1 126 ? 95.733  9.534   -10.325 1.00 52.14  ? 125 VAL A CA  1 
ATOM   900  C  C   . VAL A 1 126 ? 94.948  10.441  -9.383  1.00 56.60  ? 125 VAL A C   1 
ATOM   901  O  O   . VAL A 1 126 ? 94.012  9.994   -8.709  1.00 55.56  ? 125 VAL A O   1 
ATOM   902  C  CB  . VAL A 1 126 ? 96.990  8.954   -9.650  1.00 62.46  ? 125 VAL A CB  1 
ATOM   903  C  CG1 . VAL A 1 126 ? 96.627  8.221   -8.374  1.00 58.15  ? 125 VAL A CG1 1 
ATOM   904  C  CG2 . VAL A 1 126 ? 97.708  8.013   -10.602 1.00 63.45  ? 125 VAL A CG2 1 
ATOM   905  N  N   . GLN A 1 127 ? 95.311  11.727  -9.318  1.00 53.36  ? 126 GLN A N   1 
ATOM   906  C  CA  . GLN A 1 127 ? 94.615  12.645  -8.422  1.00 52.56  ? 126 GLN A CA  1 
ATOM   907  C  C   . GLN A 1 127 ? 93.163  12.865  -8.830  1.00 56.06  ? 126 GLN A C   1 
ATOM   908  O  O   . GLN A 1 127 ? 92.352  13.269  -7.990  1.00 52.23  ? 126 GLN A O   1 
ATOM   909  C  CB  . GLN A 1 127 ? 95.350  13.986  -8.347  1.00 49.59  ? 126 GLN A CB  1 
ATOM   910  C  CG  . GLN A 1 127 ? 95.561  14.681  -9.680  1.00 56.69  ? 126 GLN A CG  1 
ATOM   911  C  CD  . GLN A 1 127 ? 94.417  15.609  -10.041 1.00 55.69  ? 126 GLN A CD  1 
ATOM   912  O  OE1 . GLN A 1 127 ? 93.633  16.012  -9.181  1.00 57.47  ? 126 GLN A OE1 1 
ATOM   913  N  NE2 . GLN A 1 127 ? 94.323  15.961  -11.317 1.00 56.97  ? 126 GLN A NE2 1 
ATOM   914  N  N   . MET A 1 128 ? 92.820  12.614  -10.096 1.00 56.21  ? 127 MET A N   1 
ATOM   915  C  CA  . MET A 1 128 ? 91.416  12.626  -10.494 1.00 56.01  ? 127 MET A CA  1 
ATOM   916  C  C   . MET A 1 128 ? 90.632  11.544  -9.762  1.00 53.19  ? 127 MET A C   1 
ATOM   917  O  O   . MET A 1 128 ? 89.515  11.787  -9.292  1.00 49.35  ? 127 MET A O   1 
ATOM   918  C  CB  . MET A 1 128 ? 91.292  12.451  -12.008 1.00 61.70  ? 127 MET A CB  1 
ATOM   919  C  CG  . MET A 1 128 ? 91.307  13.755  -12.792 1.00 62.26  ? 127 MET A CG  1 
ATOM   920  S  SD  . MET A 1 128 ? 91.423  13.487  -14.572 1.00 82.07  ? 127 MET A SD  1 
ATOM   921  C  CE  . MET A 1 128 ? 91.508  15.174  -15.165 1.00 72.73  ? 127 MET A CE  1 
ATOM   922  N  N   . GLY A 1 129 ? 91.201  10.340  -9.659  1.00 51.34  ? 128 GLY A N   1 
ATOM   923  C  CA  . GLY A 1 129 ? 90.555  9.291   -8.889  1.00 46.49  ? 128 GLY A CA  1 
ATOM   924  C  C   . GLY A 1 129 ? 90.468  9.619   -7.413  1.00 46.57  ? 128 GLY A C   1 
ATOM   925  O  O   . GLY A 1 129 ? 89.500  9.248   -6.746  1.00 44.36  ? 128 GLY A O   1 
ATOM   926  N  N   . ILE A 1 130 ? 91.477  10.314  -6.882  1.00 46.97  ? 129 ILE A N   1 
ATOM   927  C  CA  . ILE A 1 130 ? 91.439  10.753  -5.489  1.00 45.99  ? 129 ILE A CA  1 
ATOM   928  C  C   . ILE A 1 130 ? 90.286  11.726  -5.275  1.00 45.72  ? 129 ILE A C   1 
ATOM   929  O  O   . ILE A 1 130 ? 89.487  11.577  -4.342  1.00 43.45  ? 129 ILE A O   1 
ATOM   930  C  CB  . ILE A 1 130 ? 92.785  11.381  -5.085  1.00 46.12  ? 129 ILE A CB  1 
ATOM   931  C  CG1 . ILE A 1 130 ? 93.907  10.345  -5.167  1.00 53.51  ? 129 ILE A CG1 1 
ATOM   932  C  CG2 . ILE A 1 130 ? 92.700  11.969  -3.684  1.00 34.87  ? 129 ILE A CG2 1 
ATOM   933  C  CD1 . ILE A 1 130 ? 95.264  10.879  -4.758  1.00 48.23  ? 129 ILE A CD1 1 
ATOM   934  N  N   . ALA A 1 131 ? 90.187  12.740  -6.138  1.00 40.45  ? 130 ALA A N   1 
ATOM   935  C  CA  . ALA A 1 131 ? 89.128  13.737  -6.008  1.00 44.90  ? 130 ALA A CA  1 
ATOM   936  C  C   . ALA A 1 131 ? 87.751  13.107  -6.177  1.00 46.60  ? 130 ALA A C   1 
ATOM   937  O  O   . ALA A 1 131 ? 86.831  13.378  -5.396  1.00 46.08  ? 130 ALA A O   1 
ATOM   938  C  CB  . ALA A 1 131 ? 89.336  14.857  -7.027  1.00 48.82  ? 130 ALA A CB  1 
ATOM   939  N  N   . TRP A 1 132 ? 87.585  12.264  -7.199  1.00 45.70  ? 131 TRP A N   1 
ATOM   940  C  CA  . TRP A 1 132 ? 86.271  11.682  -7.455  1.00 48.06  ? 131 TRP A CA  1 
ATOM   941  C  C   . TRP A 1 132 ? 85.890  10.677  -6.377  1.00 47.94  ? 131 TRP A C   1 
ATOM   942  O  O   . TRP A 1 132 ? 84.723  10.604  -5.976  1.00 47.35  ? 131 TRP A O   1 
ATOM   943  C  CB  . TRP A 1 132 ? 86.235  11.027  -8.834  1.00 47.65  ? 131 TRP A CB  1 
ATOM   944  C  CG  . TRP A 1 132 ? 84.847  10.924  -9.385  1.00 58.31  ? 131 TRP A CG  1 
ATOM   945  C  CD1 . TRP A 1 132 ? 84.106  9.788   -9.538  1.00 66.08  ? 131 TRP A CD1 1 
ATOM   946  C  CD2 . TRP A 1 132 ? 84.021  12.005  -9.832  1.00 65.03  ? 131 TRP A CD2 1 
ATOM   947  N  NE1 . TRP A 1 132 ? 82.874  10.094  -10.066 1.00 69.38  ? 131 TRP A NE1 1 
ATOM   948  C  CE2 . TRP A 1 132 ? 82.797  11.449  -10.254 1.00 65.91  ? 131 TRP A CE2 1 
ATOM   949  C  CE3 . TRP A 1 132 ? 84.201  13.388  -9.922  1.00 65.04  ? 131 TRP A CE3 1 
ATOM   950  C  CZ2 . TRP A 1 132 ? 81.758  12.229  -10.758 1.00 61.04  ? 131 TRP A CZ2 1 
ATOM   951  C  CZ3 . TRP A 1 132 ? 83.170  14.160  -10.422 1.00 58.88  ? 131 TRP A CZ3 1 
ATOM   952  C  CH2 . TRP A 1 132 ? 81.964  13.579  -10.834 1.00 56.49  ? 131 TRP A CH2 1 
ATOM   953  N  N   . GLY A 1 133 ? 86.856  9.891   -5.900  1.00 41.56  ? 132 GLY A N   1 
ATOM   954  C  CA  . GLY A 1 133 ? 86.574  8.975   -4.809  1.00 36.96  ? 132 GLY A CA  1 
ATOM   955  C  C   . GLY A 1 133 ? 86.154  9.696   -3.542  1.00 42.32  ? 132 GLY A C   1 
ATOM   956  O  O   . GLY A 1 133 ? 85.210  9.283   -2.865  1.00 43.17  ? 132 GLY A O   1 
ATOM   957  N  N   . ASN A 1 134 ? 86.853  10.782  -3.202  1.00 40.60  ? 133 ASN A N   1 
ATOM   958  C  CA  . ASN A 1 134 ? 86.505  11.530  -2.000  1.00 42.40  ? 133 ASN A CA  1 
ATOM   959  C  C   . ASN A 1 134 ? 85.143  12.200  -2.130  1.00 43.29  ? 133 ASN A C   1 
ATOM   960  O  O   . ASN A 1 134 ? 84.450  12.390  -1.123  1.00 44.26  ? 133 ASN A O   1 
ATOM   961  C  CB  . ASN A 1 134 ? 87.584  12.569  -1.699  1.00 44.02  ? 133 ASN A CB  1 
ATOM   962  C  CG  . ASN A 1 134 ? 88.870  11.942  -1.198  1.00 49.51  ? 133 ASN A CG  1 
ATOM   963  O  OD1 . ASN A 1 134 ? 88.937  10.734  -0.974  1.00 58.10  ? 133 ASN A OD1 1 
ATOM   964  N  ND2 . ASN A 1 134 ? 89.901  12.762  -1.027  1.00 47.62  ? 133 ASN A ND2 1 
ATOM   965  N  N   . LEU A 1 135 ? 84.743  12.566  -3.350  1.00 42.61  ? 134 LEU A N   1 
ATOM   966  C  CA  . LEU A 1 135 ? 83.415  13.136  -3.553  1.00 41.13  ? 134 LEU A CA  1 
ATOM   967  C  C   . LEU A 1 135 ? 82.333  12.102  -3.264  1.00 43.92  ? 134 LEU A C   1 
ATOM   968  O  O   . LEU A 1 135 ? 81.347  12.395  -2.576  1.00 40.87  ? 134 LEU A O   1 
ATOM   969  C  CB  . LEU A 1 135 ? 83.282  13.676  -4.978  1.00 42.77  ? 134 LEU A CB  1 
ATOM   970  C  CG  . LEU A 1 135 ? 81.890  14.170  -5.378  1.00 42.80  ? 134 LEU A CG  1 
ATOM   971  C  CD1 . LEU A 1 135 ? 81.508  15.401  -4.571  1.00 44.17  ? 134 LEU A CD1 1 
ATOM   972  C  CD2 . LEU A 1 135 ? 81.822  14.459  -6.870  1.00 46.14  ? 134 LEU A CD2 1 
ATOM   973  N  N   . LEU A 1 136 ? 82.499  10.886  -3.793  1.00 39.41  ? 135 LEU A N   1 
ATOM   974  C  CA  . LEU A 1 136 ? 81.509  9.835   -3.578  1.00 40.97  ? 135 LEU A CA  1 
ATOM   975  C  C   . LEU A 1 136 ? 81.396  9.482   -2.100  1.00 40.96  ? 135 LEU A C   1 
ATOM   976  O  O   . LEU A 1 136 ? 80.293  9.247   -1.593  1.00 46.51  ? 135 LEU A O   1 
ATOM   977  C  CB  . LEU A 1 136 ? 81.869  8.599   -4.403  1.00 48.69  ? 135 LEU A CB  1 
ATOM   978  C  CG  . LEU A 1 136 ? 82.012  8.809   -5.912  1.00 49.88  ? 135 LEU A CG  1 
ATOM   979  C  CD1 . LEU A 1 136 ? 82.482  7.532   -6.585  1.00 40.39  ? 135 LEU A CD1 1 
ATOM   980  C  CD2 . LEU A 1 136 ? 80.704  9.291   -6.523  1.00 50.56  ? 135 LEU A CD2 1 
ATOM   981  N  N   . LEU A 1 137 ? 82.529  9.435   -1.395  1.00 40.23  ? 136 LEU A N   1 
ATOM   982  C  CA  . LEU A 1 137 ? 82.496  9.195   0.044   1.00 43.98  ? 136 LEU A CA  1 
ATOM   983  C  C   . LEU A 1 137 ? 81.761  10.316  0.767   1.00 43.47  ? 136 LEU A C   1 
ATOM   984  O  O   . LEU A 1 137 ? 80.962  10.060  1.675   1.00 44.33  ? 136 LEU A O   1 
ATOM   985  C  CB  . LEU A 1 137 ? 83.918  9.045   0.586   1.00 41.91  ? 136 LEU A CB  1 
ATOM   986  C  CG  . LEU A 1 137 ? 84.708  7.830   0.094   1.00 40.70  ? 136 LEU A CG  1 
ATOM   987  C  CD1 . LEU A 1 137 ? 86.185  7.982   0.420   1.00 48.03  ? 136 LEU A CD1 1 
ATOM   988  C  CD2 . LEU A 1 137 ? 84.149  6.548   0.691   1.00 35.21  ? 136 LEU A CD2 1 
ATOM   989  N  N   . ALA A 1 138 ? 82.027  11.567  0.381   1.00 42.96  ? 137 ALA A N   1 
ATOM   990  C  CA  . ALA A 1 138 ? 81.354  12.703  1.002   1.00 39.69  ? 137 ALA A CA  1 
ATOM   991  C  C   . ALA A 1 138 ? 79.853  12.668  0.748   1.00 47.46  ? 137 ALA A C   1 
ATOM   992  O  O   . ALA A 1 138 ? 79.068  13.085  1.608   1.00 43.83  ? 137 ALA A O   1 
ATOM   993  C  CB  . ALA A 1 138 ? 81.953  14.014  0.493   1.00 38.02  ? 137 ALA A CB  1 
ATOM   994  N  N   . LEU A 1 139 ? 79.436  12.183  -0.424  1.00 41.78  ? 138 LEU A N   1 
ATOM   995  C  CA  . LEU A 1 139 ? 78.013  11.988  -0.686  1.00 42.05  ? 138 LEU A CA  1 
ATOM   996  C  C   . LEU A 1 139 ? 77.403  11.006  0.306   1.00 46.08  ? 138 LEU A C   1 
ATOM   997  O  O   . LEU A 1 139 ? 76.350  11.276  0.895   1.00 44.49  ? 138 LEU A O   1 
ATOM   998  C  CB  . LEU A 1 139 ? 77.807  11.494  -2.117  1.00 43.90  ? 138 LEU A CB  1 
ATOM   999  C  CG  . LEU A 1 139 ? 78.026  12.494  -3.251  1.00 46.22  ? 138 LEU A CG  1 
ATOM   1000 C  CD1 . LEU A 1 139 ? 77.843  11.810  -4.596  1.00 48.32  ? 138 LEU A CD1 1 
ATOM   1001 C  CD2 . LEU A 1 139 ? 77.082  13.673  -3.113  1.00 48.54  ? 138 LEU A CD2 1 
ATOM   1002 N  N   . MET A 1 140 ? 78.049  9.851   0.495   1.00 47.65  ? 139 MET A N   1 
ATOM   1003 C  CA  . MET A 1 140 ? 77.540  8.865   1.443   1.00 43.81  ? 139 MET A CA  1 
ATOM   1004 C  C   . MET A 1 140 ? 77.441  9.449   2.846   1.00 41.01  ? 139 MET A C   1 
ATOM   1005 O  O   . MET A 1 140 ? 76.456  9.213   3.557   1.00 39.06  ? 139 MET A O   1 
ATOM   1006 C  CB  . MET A 1 140 ? 78.432  7.625   1.452   1.00 45.86  ? 139 MET A CB  1 
ATOM   1007 C  CG  . MET A 1 140 ? 78.638  6.981   0.098   1.00 50.97  ? 139 MET A CG  1 
ATOM   1008 S  SD  . MET A 1 140 ? 79.623  5.478   0.234   1.00 61.87  ? 139 MET A SD  1 
ATOM   1009 C  CE  . MET A 1 140 ? 79.873  5.081   -1.491  1.00 48.74  ? 139 MET A CE  1 
ATOM   1010 N  N   . LYS A 1 141 ? 78.456  10.210  3.264   1.00 35.53  ? 140 LYS A N   1 
ATOM   1011 C  CA  . LYS A 1 141 ? 78.416  10.830  4.584   1.00 42.30  ? 140 LYS A CA  1 
ATOM   1012 C  C   . LYS A 1 141 ? 77.258  11.810  4.708   1.00 40.22  ? 140 LYS A C   1 
ATOM   1013 O  O   . LYS A 1 141 ? 76.695  11.968  5.797   1.00 39.75  ? 140 LYS A O   1 
ATOM   1014 C  CB  . LYS A 1 141 ? 79.740  11.537  4.870   1.00 41.27  ? 140 LYS A CB  1 
ATOM   1015 C  CG  . LYS A 1 141 ? 80.934  10.601  4.974   1.00 41.08  ? 140 LYS A CG  1 
ATOM   1016 C  CD  . LYS A 1 141 ? 82.185  11.357  5.388   1.00 40.05  ? 140 LYS A CD  1 
ATOM   1017 C  CE  . LYS A 1 141 ? 83.445  10.643  4.932   1.00 36.37  ? 140 LYS A CE  1 
ATOM   1018 N  NZ  . LYS A 1 141 ? 84.651  11.161  5.630   1.00 43.93  ? 140 LYS A NZ  1 
ATOM   1019 N  N   . GLY A 1 142 ? 76.892  12.479  3.612   1.00 40.64  ? 141 GLY A N   1 
ATOM   1020 C  CA  . GLY A 1 142 ? 75.734  13.354  3.642   1.00 38.45  ? 141 GLY A CA  1 
ATOM   1021 C  C   . GLY A 1 142 ? 74.446  12.613  3.937   1.00 42.90  ? 141 GLY A C   1 
ATOM   1022 O  O   . GLY A 1 142 ? 73.505  13.187  4.491   1.00 51.19  ? 141 GLY A O   1 
ATOM   1023 N  N   . PHE A 1 143 ? 74.387  11.335  3.575   1.00 44.41  ? 142 PHE A N   1 
ATOM   1024 C  CA  . PHE A 1 143 ? 73.261  10.466  3.882   1.00 39.45  ? 142 PHE A CA  1 
ATOM   1025 C  C   . PHE A 1 143 ? 73.454  9.686   5.176   1.00 40.48  ? 142 PHE A C   1 
ATOM   1026 O  O   . PHE A 1 143 ? 72.605  8.852   5.509   1.00 43.81  ? 142 PHE A O   1 
ATOM   1027 C  CB  . PHE A 1 143 ? 73.031  9.494   2.723   1.00 37.95  ? 142 PHE A CB  1 
ATOM   1028 C  CG  . PHE A 1 143 ? 72.282  10.095  1.570   1.00 41.71  ? 142 PHE A CG  1 
ATOM   1029 C  CD1 . PHE A 1 143 ? 70.898  10.107  1.555   1.00 41.66  ? 142 PHE A CD1 1 
ATOM   1030 C  CD2 . PHE A 1 143 ? 72.966  10.660  0.505   1.00 42.12  ? 142 PHE A CD2 1 
ATOM   1031 C  CE1 . PHE A 1 143 ? 70.209  10.663  0.494   1.00 45.67  ? 142 PHE A CE1 1 
ATOM   1032 C  CE2 . PHE A 1 143 ? 72.283  11.215  -0.559  1.00 41.40  ? 142 PHE A CE2 1 
ATOM   1033 C  CZ  . PHE A 1 143 ? 70.902  11.217  -0.563  1.00 47.30  ? 142 PHE A CZ  1 
ATOM   1034 N  N   . ARG A 1 144 ? 74.543  9.942   5.905   1.00 39.08  ? 143 ARG A N   1 
ATOM   1035 C  CA  . ARG A 1 144 ? 74.874  9.233   7.143   1.00 38.38  ? 143 ARG A CA  1 
ATOM   1036 C  C   . ARG A 1 144 ? 75.019  7.730   6.912   1.00 45.83  ? 143 ARG A C   1 
ATOM   1037 O  O   . ARG A 1 144 ? 74.725  6.924   7.798   1.00 39.96  ? 143 ARG A O   1 
ATOM   1038 C  CB  . ARG A 1 144 ? 73.834  9.505   8.235   1.00 33.76  ? 143 ARG A CB  1 
ATOM   1039 C  CG  . ARG A 1 144 ? 73.610  10.979  8.519   1.00 48.35  ? 143 ARG A CG  1 
ATOM   1040 C  CD  . ARG A 1 144 ? 72.960  11.201  9.873   1.00 46.88  ? 143 ARG A CD  1 
ATOM   1041 N  NE  . ARG A 1 144 ? 71.575  10.746  9.887   1.00 49.72  ? 143 ARG A NE  1 
ATOM   1042 C  CZ  . ARG A 1 144 ? 70.746  10.894  10.911  1.00 45.77  ? 143 ARG A CZ  1 
ATOM   1043 N  NH1 . ARG A 1 144 ? 71.124  11.497  12.026  1.00 42.30  ? 143 ARG A NH1 1 
ATOM   1044 N  NH2 . ARG A 1 144 ? 69.507  10.421  10.815  1.00 50.97  ? 143 ARG A NH2 1 
ATOM   1045 N  N   . ASP A 1 145 ? 75.480  7.346   5.719   1.00 43.01  ? 144 ASP A N   1 
ATOM   1046 C  CA  . ASP A 1 145 ? 75.661  5.937   5.365   1.00 38.28  ? 144 ASP A CA  1 
ATOM   1047 C  C   . ASP A 1 145 ? 77.034  5.481   5.851   1.00 43.94  ? 144 ASP A C   1 
ATOM   1048 O  O   . ASP A 1 145 ? 77.998  5.367   5.091   1.00 46.14  ? 144 ASP A O   1 
ATOM   1049 C  CB  . ASP A 1 145 ? 75.494  5.737   3.863   1.00 36.60  ? 144 ASP A CB  1 
ATOM   1050 C  CG  . ASP A 1 145 ? 75.346  4.273   3.477   1.00 43.26  ? 144 ASP A CG  1 
ATOM   1051 O  OD1 . ASP A 1 145 ? 75.524  3.395   4.348   1.00 42.03  ? 144 ASP A OD1 1 
ATOM   1052 O  OD2 . ASP A 1 145 ? 75.046  4.000   2.296   1.00 46.41  ? 144 ASP A OD2 1 
ATOM   1053 N  N   . ALA A 1 146 ? 77.118  5.232   7.161   1.00 47.99  ? 145 ALA A N   1 
ATOM   1054 C  CA  . ALA A 1 146 ? 78.380  4.803   7.754   1.00 42.75  ? 145 ALA A CA  1 
ATOM   1055 C  C   . ALA A 1 146 ? 78.846  3.470   7.182   1.00 42.79  ? 145 ALA A C   1 
ATOM   1056 O  O   . ALA A 1 146 ? 80.053  3.234   7.061   1.00 43.48  ? 145 ALA A O   1 
ATOM   1057 C  CB  . ALA A 1 146 ? 78.244  4.707   9.273   1.00 39.51  ? 145 ALA A CB  1 
ATOM   1058 N  N   . ALA A 1 147 ? 77.908  2.589   6.827   1.00 45.28  ? 146 ALA A N   1 
ATOM   1059 C  CA  . ALA A 1 147 ? 78.281  1.273   6.320   1.00 46.83  ? 146 ALA A CA  1 
ATOM   1060 C  C   . ALA A 1 147 ? 78.840  1.359   4.906   1.00 43.20  ? 146 ALA A C   1 
ATOM   1061 O  O   . ALA A 1 147 ? 79.871  0.750   4.599   1.00 45.27  ? 146 ALA A O   1 
ATOM   1062 C  CB  . ALA A 1 147 ? 77.075  0.334   6.367   1.00 46.29  ? 146 ALA A CB  1 
ATOM   1063 N  N   . GLY A 1 148 ? 78.172  2.111   4.027   1.00 40.12  ? 147 GLY A N   1 
ATOM   1064 C  CA  . GLY A 1 148 ? 78.694  2.292   2.681   1.00 37.58  ? 147 GLY A CA  1 
ATOM   1065 C  C   . GLY A 1 148 ? 80.055  2.961   2.670   1.00 45.66  ? 147 GLY A C   1 
ATOM   1066 O  O   . GLY A 1 148 ? 80.954  2.552   1.929   1.00 42.89  ? 147 GLY A O   1 
ATOM   1067 N  N   . ASN A 1 149 ? 80.218  4.007   3.481   1.00 45.24  ? 148 ASN A N   1 
ATOM   1068 C  CA  . ASN A 1 149 ? 81.509  4.676   3.602   1.00 38.03  ? 148 ASN A CA  1 
ATOM   1069 C  C   . ASN A 1 149 ? 82.588  3.708   4.075   1.00 37.25  ? 148 ASN A C   1 
ATOM   1070 O  O   . ASN A 1 149 ? 83.665  3.617   3.474   1.00 40.51  ? 148 ASN A O   1 
ATOM   1071 C  CB  . ASN A 1 149 ? 81.385  5.868   4.553   1.00 44.82  ? 148 ASN A CB  1 
ATOM   1072 C  CG  . ASN A 1 149 ? 82.713  6.549   4.818   1.00 42.01  ? 148 ASN A CG  1 
ATOM   1073 O  OD1 . ASN A 1 149 ? 83.223  7.289   3.978   1.00 45.47  ? 148 ASN A OD1 1 
ATOM   1074 N  ND2 . ASN A 1 149 ? 83.275  6.310   5.997   1.00 43.59  ? 148 ASN A ND2 1 
ATOM   1075 N  N   . ALA A 1 150 ? 82.312  2.972   5.155   1.00 39.64  ? 149 ALA A N   1 
ATOM   1076 C  CA  . ALA A 1 150 ? 83.311  2.069   5.721   1.00 41.51  ? 149 ALA A CA  1 
ATOM   1077 C  C   . ALA A 1 150 ? 83.639  0.919   4.776   1.00 40.85  ? 149 ALA A C   1 
ATOM   1078 O  O   . ALA A 1 150 ? 84.814  0.582   4.590   1.00 45.02  ? 149 ALA A O   1 
ATOM   1079 C  CB  . ALA A 1 150 ? 82.829  1.533   7.068   1.00 41.96  ? 149 ALA A CB  1 
ATOM   1080 N  N   . LEU A 1 151 ? 82.620  0.304   4.169   1.00 39.16  ? 150 LEU A N   1 
ATOM   1081 C  CA  . LEU A 1 151 ? 82.878  -0.795  3.242   1.00 48.76  ? 150 LEU A CA  1 
ATOM   1082 C  C   . LEU A 1 151 ? 83.691  -0.328  2.042   1.00 43.29  ? 150 LEU A C   1 
ATOM   1083 O  O   . LEU A 1 151 ? 84.562  -1.057  1.552   1.00 42.35  ? 150 LEU A O   1 
ATOM   1084 C  CB  . LEU A 1 151 ? 81.562  -1.430  2.789   1.00 46.54  ? 150 LEU A CB  1 
ATOM   1085 C  CG  . LEU A 1 151 ? 80.811  -2.234  3.851   1.00 53.97  ? 150 LEU A CG  1 
ATOM   1086 C  CD1 . LEU A 1 151 ? 79.324  -2.309  3.533   1.00 51.13  ? 150 LEU A CD1 1 
ATOM   1087 C  CD2 . LEU A 1 151 ? 81.407  -3.627  3.971   1.00 49.77  ? 150 LEU A CD2 1 
ATOM   1088 N  N   . SER A 1 152 ? 83.423  0.885   1.556   1.00 40.84  ? 151 SER A N   1 
ATOM   1089 C  CA  . SER A 1 152 ? 84.182  1.417   0.429   1.00 37.44  ? 151 SER A CA  1 
ATOM   1090 C  C   . SER A 1 152 ? 85.653  1.574   0.793   1.00 43.33  ? 151 SER A C   1 
ATOM   1091 O  O   . SER A 1 152 ? 86.540  1.128   0.055   1.00 43.21  ? 151 SER A O   1 
ATOM   1092 C  CB  . SER A 1 152 ? 83.589  2.753   -0.018  1.00 36.62  ? 151 SER A CB  1 
ATOM   1093 O  OG  . SER A 1 152 ? 82.307  2.577   -0.593  1.00 44.44  ? 151 SER A OG  1 
ATOM   1094 N  N   . LEU A 1 153 ? 85.930  2.211   1.933   1.00 41.19  ? 152 LEU A N   1 
ATOM   1095 C  CA  . LEU A 1 153 ? 87.311  2.415   2.358   1.00 40.35  ? 152 LEU A CA  1 
ATOM   1096 C  C   . LEU A 1 153 ? 88.019  1.090   2.614   1.00 40.63  ? 152 LEU A C   1 
ATOM   1097 O  O   . LEU A 1 153 ? 89.218  0.957   2.340   1.00 41.02  ? 152 LEU A O   1 
ATOM   1098 C  CB  . LEU A 1 153 ? 87.348  3.294   3.607   1.00 42.71  ? 152 LEU A CB  1 
ATOM   1099 C  CG  . LEU A 1 153 ? 86.884  4.739   3.418   1.00 43.80  ? 152 LEU A CG  1 
ATOM   1100 C  CD1 . LEU A 1 153 ? 86.598  5.383   4.763   1.00 43.06  ? 152 LEU A CD1 1 
ATOM   1101 C  CD2 . LEU A 1 153 ? 87.916  5.543   2.642   1.00 36.38  ? 152 LEU A CD2 1 
ATOM   1102 N  N   . ILE A 1 154 ? 87.297  0.097   3.138   1.00 42.01  ? 153 ILE A N   1 
ATOM   1103 C  CA  . ILE A 1 154 ? 87.905  -1.202  3.417   1.00 37.81  ? 153 ILE A CA  1 
ATOM   1104 C  C   . ILE A 1 154 ? 88.330  -1.882  2.121   1.00 41.32  ? 153 ILE A C   1 
ATOM   1105 O  O   . ILE A 1 154 ? 89.465  -2.355  1.994   1.00 47.85  ? 153 ILE A O   1 
ATOM   1106 C  CB  . ILE A 1 154 ? 86.939  -2.085  4.226   1.00 40.95  ? 153 ILE A CB  1 
ATOM   1107 C  CG1 . ILE A 1 154 ? 86.885  -1.621  5.682   1.00 39.33  ? 153 ILE A CG1 1 
ATOM   1108 C  CG2 . ILE A 1 154 ? 87.357  -3.546  4.148   1.00 41.20  ? 153 ILE A CG2 1 
ATOM   1109 C  CD1 . ILE A 1 154 ? 85.592  -1.972  6.385   1.00 37.09  ? 153 ILE A CD1 1 
ATOM   1110 N  N   . VAL A 1 155 ? 87.421  -1.948  1.145   1.00 37.82  ? 154 VAL A N   1 
ATOM   1111 C  CA  . VAL A 1 155 ? 87.751  -2.541  -0.149  1.00 38.13  ? 154 VAL A CA  1 
ATOM   1112 C  C   . VAL A 1 155 ? 88.910  -1.795  -0.797  1.00 42.01  ? 154 VAL A C   1 
ATOM   1113 O  O   . VAL A 1 155 ? 89.815  -2.406  -1.380  1.00 45.21  ? 154 VAL A O   1 
ATOM   1114 C  CB  . VAL A 1 155 ? 86.508  -2.561  -1.059  1.00 40.16  ? 154 VAL A CB  1 
ATOM   1115 C  CG1 . VAL A 1 155 ? 86.884  -2.977  -2.475  1.00 35.59  ? 154 VAL A CG1 1 
ATOM   1116 C  CG2 . VAL A 1 155 ? 85.444  -3.485  -0.487  1.00 37.71  ? 154 VAL A CG2 1 
ATOM   1117 N  N   . GLY A 1 156 ? 88.913  -0.465  -0.687  1.00 40.99  ? 155 GLY A N   1 
ATOM   1118 C  CA  . GLY A 1 156 ? 89.962  0.321   -1.316  1.00 44.10  ? 155 GLY A CA  1 
ATOM   1119 C  C   . GLY A 1 156 ? 91.330  0.074   -0.709  1.00 47.57  ? 155 GLY A C   1 
ATOM   1120 O  O   . GLY A 1 156 ? 92.331  -0.001  -1.426  1.00 44.28  ? 155 GLY A O   1 
ATOM   1121 N  N   . SER A 1 157 ? 91.397  -0.037  0.620   1.00 42.28  ? 156 SER A N   1 
ATOM   1122 C  CA  . SER A 1 157 ? 92.666  -0.344  1.273   1.00 41.65  ? 156 SER A CA  1 
ATOM   1123 C  C   . SER A 1 157 ? 93.206  -1.695  0.819   1.00 45.74  ? 156 SER A C   1 
ATOM   1124 O  O   . SER A 1 157 ? 94.395  -1.830  0.508   1.00 48.16  ? 156 SER A O   1 
ATOM   1125 C  CB  . SER A 1 157 ? 92.498  -0.313  2.791   1.00 40.16  ? 156 SER A CB  1 
ATOM   1126 O  OG  . SER A 1 157 ? 92.094  0.970   3.236   1.00 43.81  ? 156 SER A OG  1 
ATOM   1127 N  N   . LEU A 1 158 ? 92.343  -2.715  0.783   1.00 48.11  ? 157 LEU A N   1 
ATOM   1128 C  CA  . LEU A 1 158 ? 92.805  -4.058  0.444   1.00 46.09  ? 157 LEU A CA  1 
ATOM   1129 C  C   . LEU A 1 158 ? 93.254  -4.144  -1.011  1.00 50.00  ? 157 LEU A C   1 
ATOM   1130 O  O   . LEU A 1 158 ? 94.290  -4.749  -1.308  1.00 62.16  ? 157 LEU A O   1 
ATOM   1131 C  CB  . LEU A 1 158 ? 91.711  -5.082  0.741   1.00 44.11  ? 157 LEU A CB  1 
ATOM   1132 C  CG  . LEU A 1 158 ? 91.244  -5.128  2.199   1.00 46.67  ? 157 LEU A CG  1 
ATOM   1133 C  CD1 . LEU A 1 158 ? 90.400  -6.364  2.464   1.00 43.77  ? 157 LEU A CD1 1 
ATOM   1134 C  CD2 . LEU A 1 158 ? 92.428  -5.068  3.156   1.00 50.32  ? 157 LEU A CD2 1 
ATOM   1135 N  N   . ILE A 1 159 ? 92.490  -3.552  -1.934  1.00 49.14  ? 158 ILE A N   1 
ATOM   1136 C  CA  . ILE A 1 159 ? 92.930  -3.531  -3.326  1.00 53.50  ? 158 ILE A CA  1 
ATOM   1137 C  C   . ILE A 1 159 ? 94.140  -2.621  -3.484  1.00 48.35  ? 158 ILE A C   1 
ATOM   1138 O  O   . ILE A 1 159 ? 94.957  -2.812  -4.394  1.00 52.66  ? 158 ILE A O   1 
ATOM   1139 C  CB  . ILE A 1 159 ? 91.779  -3.118  -4.264  1.00 54.06  ? 158 ILE A CB  1 
ATOM   1140 C  CG1 . ILE A 1 159 ? 91.399  -1.650  -4.051  1.00 53.49  ? 158 ILE A CG1 1 
ATOM   1141 C  CG2 . ILE A 1 159 ? 90.577  -4.034  -4.070  1.00 54.73  ? 158 ILE A CG2 1 
ATOM   1142 C  CD1 . ILE A 1 159 ? 90.103  -1.247  -4.722  1.00 55.25  ? 158 ILE A CD1 1 
ATOM   1143 N  N   . GLY A 1 160 ? 94.275  -1.618  -2.615  1.00 44.74  ? 159 GLY A N   1 
ATOM   1144 C  CA  . GLY A 1 160 ? 95.439  -0.753  -2.673  1.00 45.66  ? 159 GLY A CA  1 
ATOM   1145 C  C   . GLY A 1 160 ? 96.723  -1.494  -2.351  1.00 53.73  ? 159 GLY A C   1 
ATOM   1146 O  O   . GLY A 1 160 ? 97.747  -1.296  -3.011  1.00 52.54  ? 159 GLY A O   1 
ATOM   1147 N  N   . VAL A 1 161 ? 96.685  -2.357  -1.333  1.00 50.87  ? 160 VAL A N   1 
ATOM   1148 C  CA  . VAL A 1 161 ? 97.855  -3.162  -0.991  1.00 52.62  ? 160 VAL A CA  1 
ATOM   1149 C  C   . VAL A 1 161 ? 98.228  -4.073  -2.153  1.00 58.45  ? 160 VAL A C   1 
ATOM   1150 O  O   . VAL A 1 161 ? 99.408  -4.210  -2.502  1.00 54.58  ? 160 VAL A O   1 
ATOM   1151 C  CB  . VAL A 1 161 ? 97.592  -3.964  0.298   1.00 49.24  ? 160 VAL A CB  1 
ATOM   1152 C  CG1 . VAL A 1 161 ? 98.608  -5.085  0.449   1.00 54.45  ? 160 VAL A CG1 1 
ATOM   1153 C  CG2 . VAL A 1 161 ? 97.624  -3.044  1.507   1.00 52.76  ? 160 VAL A CG2 1 
ATOM   1154 N  N   . LEU A 1 162 ? 97.230  -4.708  -2.773  1.00 56.48  ? 161 LEU A N   1 
ATOM   1155 C  CA  . LEU A 1 162 ? 97.498  -5.545  -3.937  1.00 56.58  ? 161 LEU A CA  1 
ATOM   1156 C  C   . LEU A 1 162 ? 98.109  -4.731  -5.070  1.00 57.77  ? 161 LEU A C   1 
ATOM   1157 O  O   . LEU A 1 162 ? 99.075  -5.167  -5.707  1.00 55.26  ? 161 LEU A O   1 
ATOM   1158 C  CB  . LEU A 1 162 ? 96.208  -6.223  -4.401  1.00 54.20  ? 161 LEU A CB  1 
ATOM   1159 C  CG  . LEU A 1 162 ? 95.505  -7.127  -3.388  1.00 65.30  ? 161 LEU A CG  1 
ATOM   1160 C  CD1 . LEU A 1 162 ? 94.304  -7.807  -4.025  1.00 74.06  ? 161 LEU A CD1 1 
ATOM   1161 C  CD2 . LEU A 1 162 ? 96.472  -8.159  -2.830  1.00 62.34  ? 161 LEU A CD2 1 
ATOM   1162 N  N   . ALA A 1 163 ? 97.553  -3.547  -5.342  1.00 54.81  ? 162 ALA A N   1 
ATOM   1163 C  CA  . ALA A 1 163 ? 98.086  -2.708  -6.410  1.00 54.95  ? 162 ALA A CA  1 
ATOM   1164 C  C   . ALA A 1 163 ? 99.512  -2.263  -6.110  1.00 54.55  ? 162 ALA A C   1 
ATOM   1165 O  O   . ALA A 1 163 ? 100.362 -2.238  -7.008  1.00 56.05  ? 162 ALA A O   1 
ATOM   1166 C  CB  . ALA A 1 163 ? 97.183  -1.497  -6.628  1.00 45.76  ? 162 ALA A CB  1 
ATOM   1167 N  N   . TYR A 1 164 ? 99.793  -1.904  -4.854  1.00 53.33  ? 163 TYR A N   1 
ATOM   1168 C  CA  . TYR A 1 164 ? 101.153 -1.527  -4.481  1.00 55.15  ? 163 TYR A CA  1 
ATOM   1169 C  C   . TYR A 1 164 ? 102.128 -2.677  -4.705  1.00 58.71  ? 163 TYR A C   1 
ATOM   1170 O  O   . TYR A 1 164 ? 103.244 -2.466  -5.193  1.00 56.06  ? 163 TYR A O   1 
ATOM   1171 C  CB  . TYR A 1 164 ? 101.193 -1.062  -3.024  1.00 52.76  ? 163 TYR A CB  1 
ATOM   1172 C  CG  . TYR A 1 164 ? 102.592 -0.884  -2.473  1.00 54.77  ? 163 TYR A CG  1 
ATOM   1173 C  CD1 . TYR A 1 164 ? 103.284 0.307   -2.654  1.00 53.46  ? 163 TYR A CD1 1 
ATOM   1174 C  CD2 . TYR A 1 164 ? 103.218 -1.903  -1.764  1.00 53.47  ? 163 TYR A CD2 1 
ATOM   1175 C  CE1 . TYR A 1 164 ? 104.561 0.476   -2.152  1.00 53.53  ? 163 TYR A CE1 1 
ATOM   1176 C  CE2 . TYR A 1 164 ? 104.495 -1.744  -1.260  1.00 53.80  ? 163 TYR A CE2 1 
ATOM   1177 C  CZ  . TYR A 1 164 ? 105.161 -0.553  -1.456  1.00 59.53  ? 163 TYR A CZ  1 
ATOM   1178 O  OH  . TYR A 1 164 ? 106.433 -0.390  -0.955  1.00 63.35  ? 163 TYR A OH  1 
ATOM   1179 N  N   . TYR A 1 165 ? 101.723 -3.900  -4.352  1.00 59.86  ? 164 TYR A N   1 
ATOM   1180 C  CA  . TYR A 1 165 ? 102.604 -5.051  -4.526  1.00 61.23  ? 164 TYR A CA  1 
ATOM   1181 C  C   . TYR A 1 165 ? 102.960 -5.250  -5.993  1.00 58.19  ? 164 TYR A C   1 
ATOM   1182 O  O   . TYR A 1 165 ? 104.137 -5.381  -6.347  1.00 65.80  ? 164 TYR A O   1 
ATOM   1183 C  CB  . TYR A 1 165 ? 101.955 -6.314  -3.959  1.00 64.34  ? 164 TYR A CB  1 
ATOM   1184 C  CG  . TYR A 1 165 ? 102.923 -7.469  -3.834  1.00 70.47  ? 164 TYR A CG  1 
ATOM   1185 C  CD1 . TYR A 1 165 ? 103.874 -7.501  -2.823  1.00 78.63  ? 164 TYR A CD1 1 
ATOM   1186 C  CD2 . TYR A 1 165 ? 102.908 -8.512  -4.751  1.00 81.30  ? 164 TYR A CD2 1 
ATOM   1187 C  CE1 . TYR A 1 165 ? 104.768 -8.552  -2.714  1.00 85.90  ? 164 TYR A CE1 1 
ATOM   1188 C  CE2 . TYR A 1 165 ? 103.797 -9.566  -4.652  1.00 85.13  ? 164 TYR A CE2 1 
ATOM   1189 C  CZ  . TYR A 1 165 ? 104.725 -9.581  -3.633  1.00 87.35  ? 164 TYR A CZ  1 
ATOM   1190 O  OH  . TYR A 1 165 ? 105.612 -10.628 -3.532  1.00 88.49  ? 164 TYR A OH  1 
ATOM   1191 N  N   . VAL A 1 166 ? 101.947 -5.294  -6.860  1.00 56.27  ? 165 VAL A N   1 
ATOM   1192 C  CA  . VAL A 1 166 ? 102.197 -5.449  -8.290  1.00 57.68  ? 165 VAL A CA  1 
ATOM   1193 C  C   . VAL A 1 166 ? 103.028 -4.285  -8.813  1.00 57.00  ? 165 VAL A C   1 
ATOM   1194 O  O   . VAL A 1 166 ? 103.928 -4.467  -9.643  1.00 62.36  ? 165 VAL A O   1 
ATOM   1195 C  CB  . VAL A 1 166 ? 100.866 -5.582  -9.054  1.00 58.56  ? 165 VAL A CB  1 
ATOM   1196 C  CG1 . VAL A 1 166 ? 101.115 -5.670  -10.555 1.00 52.48  ? 165 VAL A CG1 1 
ATOM   1197 C  CG2 . VAL A 1 166 ? 100.082 -6.789  -8.559  1.00 58.56  ? 165 VAL A CG2 1 
ATOM   1198 N  N   . SER A 1 167 ? 102.746 -3.070  -8.334  1.00 51.63  ? 166 SER A N   1 
ATOM   1199 C  CA  . SER A 1 167 ? 103.391 -1.888  -8.896  1.00 54.65  ? 166 SER A CA  1 
ATOM   1200 C  C   . SER A 1 167 ? 104.884 -1.846  -8.583  1.00 62.88  ? 166 SER A C   1 
ATOM   1201 O  O   . SER A 1 167 ? 105.695 -1.550  -9.468  1.00 57.53  ? 166 SER A O   1 
ATOM   1202 C  CB  . SER A 1 167 ? 102.702 -0.623  -8.385  1.00 46.26  ? 166 SER A CB  1 
ATOM   1203 O  OG  . SER A 1 167 ? 103.136 0.520   -9.103  1.00 51.58  ? 166 SER A OG  1 
ATOM   1204 N  N   . TYR A 1 168 ? 105.276 -2.145  -7.340  1.00 57.45  ? 167 TYR A N   1 
ATOM   1205 C  CA  . TYR A 1 168 ? 106.698 -2.084  -7.018  1.00 54.09  ? 167 TYR A CA  1 
ATOM   1206 C  C   . TYR A 1 168 ? 107.451 -3.306  -7.528  1.00 64.02  ? 167 TYR A C   1 
ATOM   1207 O  O   . TYR A 1 168 ? 108.633 -3.196  -7.874  1.00 65.44  ? 167 TYR A O   1 
ATOM   1208 C  CB  . TYR A 1 168 ? 106.917 -1.912  -5.510  1.00 59.09  ? 167 TYR A CB  1 
ATOM   1209 C  CG  . TYR A 1 168 ? 107.012 -3.189  -4.703  1.00 65.19  ? 167 TYR A CG  1 
ATOM   1210 C  CD1 . TYR A 1 168 ? 108.243 -3.799  -4.481  1.00 65.71  ? 167 TYR A CD1 1 
ATOM   1211 C  CD2 . TYR A 1 168 ? 105.886 -3.766  -4.137  1.00 62.37  ? 167 TYR A CD2 1 
ATOM   1212 C  CE1 . TYR A 1 168 ? 108.345 -4.956  -3.741  1.00 58.83  ? 167 TYR A CE1 1 
ATOM   1213 C  CE2 . TYR A 1 168 ? 105.980 -4.925  -3.391  1.00 69.41  ? 167 TYR A CE2 1 
ATOM   1214 C  CZ  . TYR A 1 168 ? 107.212 -5.516  -3.197  1.00 71.43  ? 167 TYR A CZ  1 
ATOM   1215 O  OH  . TYR A 1 168 ? 107.316 -6.671  -2.457  1.00 84.88  ? 167 TYR A OH  1 
ATOM   1216 N  N   . ARG A 1 169 ? 106.804 -4.474  -7.566  1.00 59.62  ? 168 ARG A N   1 
ATOM   1217 C  CA  . ARG A 1 169 ? 107.457 -5.647  -8.136  1.00 60.22  ? 168 ARG A CA  1 
ATOM   1218 C  C   . ARG A 1 169 ? 107.726 -5.448  -9.621  1.00 65.43  ? 168 ARG A C   1 
ATOM   1219 O  O   . ARG A 1 169 ? 108.752 -5.900  -10.142 1.00 73.95  ? 168 ARG A O   1 
ATOM   1220 C  CB  . ARG A 1 169 ? 106.598 -6.891  -7.909  1.00 61.43  ? 168 ARG A CB  1 
ATOM   1221 C  CG  . ARG A 1 169 ? 106.634 -7.426  -6.486  1.00 69.73  ? 168 ARG A CG  1 
ATOM   1222 C  CD  . ARG A 1 169 ? 108.014 -7.941  -6.120  1.00 65.64  ? 168 ARG A CD  1 
ATOM   1223 N  NE  . ARG A 1 169 ? 108.331 -9.176  -6.830  1.00 72.51  ? 168 ARG A NE  1 
ATOM   1224 C  CZ  . ARG A 1 169 ? 108.671 -10.312 -6.238  1.00 77.87  ? 168 ARG A CZ  1 
ATOM   1225 N  NH1 . ARG A 1 169 ? 108.737 -10.414 -4.921  1.00 80.26  ? 168 ARG A NH1 1 
ATOM   1226 N  NH2 . ARG A 1 169 ? 108.943 -11.377 -6.987  1.00 81.13  ? 168 ARG A NH2 1 
ATOM   1227 N  N   . LEU A 1 170 ? 106.813 -4.770  -10.318 1.00 60.52  ? 169 LEU A N   1 
ATOM   1228 C  CA  . LEU A 1 170 ? 106.989 -4.527  -11.744 1.00 62.43  ? 169 LEU A CA  1 
ATOM   1229 C  C   . LEU A 1 170 ? 107.965 -3.384  -11.997 1.00 65.98  ? 169 LEU A C   1 
ATOM   1230 O  O   . LEU A 1 170 ? 108.923 -3.532  -12.763 1.00 67.58  ? 169 LEU A O   1 
ATOM   1231 C  CB  . LEU A 1 170 ? 105.637 -4.231  -12.396 1.00 60.60  ? 169 LEU A CB  1 
ATOM   1232 C  CG  . LEU A 1 170 ? 104.826 -5.444  -12.856 1.00 68.70  ? 169 LEU A CG  1 
ATOM   1233 C  CD1 . LEU A 1 170 ? 103.568 -5.003  -13.594 1.00 65.59  ? 169 LEU A CD1 1 
ATOM   1234 C  CD2 . LEU A 1 170 ? 105.670 -6.370  -13.720 1.00 59.70  ? 169 LEU A CD2 1 
ATOM   1235 N  N   . GLY A 1 171 ? 107.749 -2.242  -11.346 1.00 63.72  ? 170 GLY A N   1 
ATOM   1236 C  CA  . GLY A 1 171 ? 108.480 -1.036  -11.683 1.00 53.32  ? 170 GLY A CA  1 
ATOM   1237 C  C   . GLY A 1 171 ? 109.427 -0.519  -10.620 1.00 57.04  ? 170 GLY A C   1 
ATOM   1238 O  O   . GLY A 1 171 ? 109.815 0.653   -10.656 1.00 59.13  ? 170 GLY A O   1 
ATOM   1239 N  N   . GLY A 1 172 ? 109.810 -1.375  -9.676  1.00 53.05  ? 171 GLY A N   1 
ATOM   1240 C  CA  . GLY A 1 172 ? 110.812 -0.985  -8.696  1.00 52.48  ? 171 GLY A CA  1 
ATOM   1241 C  C   . GLY A 1 172 ? 110.374 0.178   -7.827  1.00 55.05  ? 171 GLY A C   1 
ATOM   1242 O  O   . GLY A 1 172 ? 109.216 0.279   -7.409  1.00 63.78  ? 171 GLY A O   1 
ATOM   1243 N  N   . TYR A 1 173 ? 111.329 1.068   -7.540  1.00 63.38  ? 172 TYR A N   1 
ATOM   1244 C  CA  . TYR A 1 173 ? 111.083 2.175   -6.619  1.00 59.28  ? 172 TYR A CA  1 
ATOM   1245 C  C   . TYR A 1 173 ? 110.002 3.114   -7.142  1.00 58.13  ? 172 TYR A C   1 
ATOM   1246 O  O   . TYR A 1 173 ? 109.117 3.532   -6.386  1.00 57.21  ? 172 TYR A O   1 
ATOM   1247 C  CB  . TYR A 1 173 ? 112.383 2.940   -6.363  1.00 56.75  ? 172 TYR A CB  1 
ATOM   1248 C  CG  . TYR A 1 173 ? 112.236 4.104   -5.409  1.00 52.54  ? 172 TYR A CG  1 
ATOM   1249 C  CD1 . TYR A 1 173 ? 112.051 3.890   -4.050  1.00 56.06  ? 172 TYR A CD1 1 
ATOM   1250 C  CD2 . TYR A 1 173 ? 112.292 5.415   -5.864  1.00 53.43  ? 172 TYR A CD2 1 
ATOM   1251 C  CE1 . TYR A 1 173 ? 111.918 4.945   -3.171  1.00 53.24  ? 172 TYR A CE1 1 
ATOM   1252 C  CE2 . TYR A 1 173 ? 112.161 6.480   -4.990  1.00 55.82  ? 172 TYR A CE2 1 
ATOM   1253 C  CZ  . TYR A 1 173 ? 111.975 6.237   -3.645  1.00 58.08  ? 172 TYR A CZ  1 
ATOM   1254 O  OH  . TYR A 1 173 ? 111.843 7.288   -2.767  1.00 56.46  ? 172 TYR A OH  1 
ATOM   1255 N  N   . GLU A 1 174 ? 110.065 3.472   -8.426  1.00 55.89  ? 173 GLU A N   1 
ATOM   1256 C  CA  . GLU A 1 174 ? 109.062 4.375   -8.981  1.00 59.88  ? 173 GLU A CA  1 
ATOM   1257 C  C   . GLU A 1 174 ? 107.690 3.713   -9.021  1.00 59.62  ? 173 GLU A C   1 
ATOM   1258 O  O   . GLU A 1 174 ? 106.667 4.378   -8.816  1.00 54.14  ? 173 GLU A O   1 
ATOM   1259 C  CB  . GLU A 1 174 ? 109.481 4.843   -10.375 1.00 57.83  ? 173 GLU A CB  1 
ATOM   1260 C  CG  . GLU A 1 174 ? 110.572 5.905   -10.364 1.00 65.17  ? 173 GLU A CG  1 
ATOM   1261 C  CD  . GLU A 1 174 ? 110.645 6.687   -11.661 1.00 72.52  ? 173 GLU A CD  1 
ATOM   1262 O  OE1 . GLU A 1 174 ? 109.692 7.440   -11.956 1.00 74.50  ? 173 GLU A OE1 1 
ATOM   1263 O  OE2 . GLU A 1 174 ? 111.651 6.546   -12.389 1.00 76.57  ? 173 GLU A OE2 1 
ATOM   1264 N  N   . GLY A 1 175 ? 107.647 2.406   -9.291  1.00 54.33  ? 174 GLY A N   1 
ATOM   1265 C  CA  . GLY A 1 175 ? 106.395 1.677   -9.164  1.00 53.83  ? 174 GLY A CA  1 
ATOM   1266 C  C   . GLY A 1 175 ? 105.852 1.700   -7.747  1.00 56.90  ? 174 GLY A C   1 
ATOM   1267 O  O   . GLY A 1 175 ? 104.638 1.774   -7.538  1.00 55.74  ? 174 GLY A O   1 
ATOM   1268 N  N   . ALA A 1 176 ? 106.744 1.637   -6.756  1.00 51.60  ? 175 ALA A N   1 
ATOM   1269 C  CA  . ALA A 1 176 ? 106.317 1.730   -5.363  1.00 52.26  ? 175 ALA A CA  1 
ATOM   1270 C  C   . ALA A 1 176 ? 105.695 3.089   -5.072  1.00 56.77  ? 175 ALA A C   1 
ATOM   1271 O  O   . ALA A 1 176 ? 104.652 3.181   -4.416  1.00 57.58  ? 175 ALA A O   1 
ATOM   1272 C  CB  . ALA A 1 176 ? 107.499 1.469   -4.430  1.00 50.20  ? 175 ALA A CB  1 
ATOM   1273 N  N   . LEU A 1 177 ? 106.336 4.163   -5.544  1.00 56.60  ? 176 LEU A N   1 
ATOM   1274 C  CA  . LEU A 1 177 ? 105.776 5.498   -5.359  1.00 56.98  ? 176 LEU A CA  1 
ATOM   1275 C  C   . LEU A 1 177 ? 104.414 5.621   -6.030  1.00 58.39  ? 176 LEU A C   1 
ATOM   1276 O  O   . LEU A 1 177 ? 103.488 6.215   -5.466  1.00 57.51  ? 176 LEU A O   1 
ATOM   1277 C  CB  . LEU A 1 177 ? 106.741 6.551   -5.903  1.00 61.00  ? 176 LEU A CB  1 
ATOM   1278 C  CG  . LEU A 1 177 ? 108.133 6.588   -5.268  1.00 60.19  ? 176 LEU A CG  1 
ATOM   1279 C  CD1 . LEU A 1 177 ? 108.930 7.776   -5.784  1.00 56.44  ? 176 LEU A CD1 1 
ATOM   1280 C  CD2 . LEU A 1 177 ? 108.026 6.629   -3.753  1.00 56.47  ? 176 LEU A CD2 1 
ATOM   1281 N  N   . LEU A 1 178 ? 104.280 5.083   -7.246  1.00 55.34  ? 177 LEU A N   1 
ATOM   1282 C  CA  . LEU A 1 178 ? 102.984 5.081   -7.919  1.00 51.22  ? 177 LEU A CA  1 
ATOM   1283 C  C   . LEU A 1 178 ? 101.935 4.348   -7.092  1.00 54.49  ? 177 LEU A C   1 
ATOM   1284 O  O   . LEU A 1 178 ? 100.789 4.802   -6.983  1.00 57.66  ? 177 LEU A O   1 
ATOM   1285 C  CB  . LEU A 1 178 ? 103.114 4.451   -9.306  1.00 52.73  ? 177 LEU A CB  1 
ATOM   1286 C  CG  . LEU A 1 178 ? 101.804 4.059   -9.994  1.00 54.70  ? 177 LEU A CG  1 
ATOM   1287 C  CD1 . LEU A 1 178 ? 101.041 5.295   -10.449 1.00 46.98  ? 177 LEU A CD1 1 
ATOM   1288 C  CD2 . LEU A 1 178 ? 102.058 3.117   -11.163 1.00 52.03  ? 177 LEU A CD2 1 
ATOM   1289 N  N   . GLY A 1 179 ? 102.307 3.206   -6.509  1.00 50.88  ? 178 GLY A N   1 
ATOM   1290 C  CA  . GLY A 1 179 ? 101.386 2.495   -5.637  1.00 52.69  ? 178 GLY A CA  1 
ATOM   1291 C  C   . GLY A 1 179 ? 100.964 3.318   -4.436  1.00 52.61  ? 178 GLY A C   1 
ATOM   1292 O  O   . GLY A 1 179 ? 99.823  3.226   -3.978  1.00 57.33  ? 178 GLY A O   1 
ATOM   1293 N  N   . LEU A 1 180 ? 101.880 4.134   -3.907  1.00 50.24  ? 179 LEU A N   1 
ATOM   1294 C  CA  . LEU A 1 180 ? 101.531 5.013   -2.796  1.00 52.18  ? 179 LEU A CA  1 
ATOM   1295 C  C   . LEU A 1 180 ? 100.473 6.026   -3.211  1.00 53.05  ? 179 LEU A C   1 
ATOM   1296 O  O   . LEU A 1 180 ? 99.564  6.341   -2.434  1.00 55.13  ? 179 LEU A O   1 
ATOM   1297 C  CB  . LEU A 1 180 ? 102.781 5.724   -2.279  1.00 53.03  ? 179 LEU A CB  1 
ATOM   1298 C  CG  . LEU A 1 180 ? 103.774 4.873   -1.487  1.00 54.99  ? 179 LEU A CG  1 
ATOM   1299 C  CD1 . LEU A 1 180 ? 104.927 5.724   -0.976  1.00 58.61  ? 179 LEU A CD1 1 
ATOM   1300 C  CD2 . LEU A 1 180 ? 103.077 4.160   -0.341  1.00 47.36  ? 179 LEU A CD2 1 
ATOM   1301 N  N   . ALA A 1 181 ? 100.578 6.554   -4.433  1.00 52.60  ? 180 ALA A N   1 
ATOM   1302 C  CA  . ALA A 1 181 ? 99.561  7.472   -4.931  1.00 53.58  ? 180 ALA A CA  1 
ATOM   1303 C  C   . ALA A 1 181 ? 98.255  6.751   -5.240  1.00 59.04  ? 180 ALA A C   1 
ATOM   1304 O  O   . ALA A 1 181 ? 97.179  7.352   -5.146  1.00 48.26  ? 180 ALA A O   1 
ATOM   1305 C  CB  . ALA A 1 181 ? 100.072 8.201   -6.173  1.00 49.53  ? 180 ALA A CB  1 
ATOM   1306 N  N   . LEU A 1 182 ? 98.328  5.471   -5.610  1.00 54.91  ? 181 LEU A N   1 
ATOM   1307 C  CA  . LEU A 1 182 ? 97.131  4.715   -5.953  1.00 54.41  ? 181 LEU A CA  1 
ATOM   1308 C  C   . LEU A 1 182 ? 96.344  4.261   -4.732  1.00 55.81  ? 181 LEU A C   1 
ATOM   1309 O  O   . LEU A 1 182 ? 95.172  3.895   -4.878  1.00 58.86  ? 181 LEU A O   1 
ATOM   1310 C  CB  . LEU A 1 182 ? 97.496  3.495   -6.802  1.00 50.82  ? 181 LEU A CB  1 
ATOM   1311 C  CG  . LEU A 1 182 ? 97.884  3.755   -8.259  1.00 58.01  ? 181 LEU A CG  1 
ATOM   1312 C  CD1 . LEU A 1 182 ? 98.688  2.586   -8.804  1.00 57.28  ? 181 LEU A CD1 1 
ATOM   1313 C  CD2 . LEU A 1 182 ? 96.656  4.018   -9.117  1.00 51.91  ? 181 LEU A CD2 1 
ATOM   1314 N  N   . ILE A 1 183 ? 96.957  4.254   -3.551  1.00 53.33  ? 182 ILE A N   1 
ATOM   1315 C  CA  . ILE A 1 183 ? 96.274  3.837   -2.326  1.00 53.26  ? 182 ILE A CA  1 
ATOM   1316 C  C   . ILE A 1 183 ? 94.990  4.649   -2.150  1.00 54.40  ? 182 ILE A C   1 
ATOM   1317 O  O   . ILE A 1 183 ? 93.906  4.050   -2.102  1.00 53.83  ? 182 ILE A O   1 
ATOM   1318 C  CB  . ILE A 1 183 ? 97.193  3.957   -1.094  1.00 55.75  ? 182 ILE A CB  1 
ATOM   1319 C  CG1 . ILE A 1 183 ? 98.346  2.954   -1.159  1.00 58.56  ? 182 ILE A CG1 1 
ATOM   1320 C  CG2 . ILE A 1 183 ? 96.394  3.752   0.184   1.00 59.74  ? 182 ILE A CG2 1 
ATOM   1321 C  CD1 . ILE A 1 183 ? 97.944  1.578   -1.591  1.00 56.63  ? 182 ILE A CD1 1 
ATOM   1322 N  N   . PRO A 1 184 ? 95.030  5.987   -2.057  1.00 55.57  ? 183 PRO A N   1 
ATOM   1323 C  CA  . PRO A 1 184 ? 93.774  6.732   -1.883  1.00 53.34  ? 183 PRO A CA  1 
ATOM   1324 C  C   . PRO A 1 184 ? 92.949  6.884   -3.152  1.00 50.37  ? 183 PRO A C   1 
ATOM   1325 O  O   . PRO A 1 184 ? 91.782  7.286   -3.058  1.00 55.93  ? 183 PRO A O   1 
ATOM   1326 C  CB  . PRO A 1 184 ? 94.247  8.100   -1.376  1.00 44.44  ? 183 PRO A CB  1 
ATOM   1327 C  CG  . PRO A 1 184 ? 95.581  8.269   -1.963  1.00 52.54  ? 183 PRO A CG  1 
ATOM   1328 C  CD  . PRO A 1 184 ? 96.189  6.903   -2.111  1.00 49.42  ? 183 PRO A CD  1 
ATOM   1329 N  N   . ALA A 1 185 ? 93.510  6.600   -4.330  1.00 52.49  ? 184 ALA A N   1 
ATOM   1330 C  CA  . ALA A 1 185 ? 92.762  6.790   -5.570  1.00 53.55  ? 184 ALA A CA  1 
ATOM   1331 C  C   . ALA A 1 185 ? 91.846  5.613   -5.882  1.00 51.86  ? 184 ALA A C   1 
ATOM   1332 O  O   . ALA A 1 185 ? 90.738  5.807   -6.396  1.00 46.48  ? 184 ALA A O   1 
ATOM   1333 C  CB  . ALA A 1 185 ? 93.725  7.024   -6.733  1.00 50.29  ? 184 ALA A CB  1 
ATOM   1334 N  N   . LEU A 1 186 ? 92.284  4.389   -5.580  1.00 51.59  ? 185 LEU A N   1 
ATOM   1335 C  CA  . LEU A 1 186 ? 91.513  3.198   -5.921  1.00 47.21  ? 185 LEU A CA  1 
ATOM   1336 C  C   . LEU A 1 186 ? 90.203  3.085   -5.155  1.00 53.47  ? 185 LEU A C   1 
ATOM   1337 O  O   . LEU A 1 186 ? 89.387  2.221   -5.493  1.00 53.31  ? 185 LEU A O   1 
ATOM   1338 C  CB  . LEU A 1 186 ? 92.356  1.947   -5.688  1.00 51.94  ? 185 LEU A CB  1 
ATOM   1339 C  CG  . LEU A 1 186 ? 93.443  1.726   -6.740  1.00 58.92  ? 185 LEU A CG  1 
ATOM   1340 C  CD1 . LEU A 1 186 ? 94.530  0.831   -6.184  1.00 50.45  ? 185 LEU A CD1 1 
ATOM   1341 C  CD2 . LEU A 1 186 ? 92.862  1.153   -8.027  1.00 57.97  ? 185 LEU A CD2 1 
ATOM   1342 N  N   . VAL A 1 187 ? 89.983  3.919   -4.135  1.00 52.79  ? 186 VAL A N   1 
ATOM   1343 C  CA  . VAL A 1 187 ? 88.710  3.919   -3.423  1.00 51.53  ? 186 VAL A CA  1 
ATOM   1344 C  C   . VAL A 1 187 ? 87.554  4.278   -4.347  1.00 49.40  ? 186 VAL A C   1 
ATOM   1345 O  O   . VAL A 1 187 ? 86.402  3.940   -4.055  1.00 46.49  ? 186 VAL A O   1 
ATOM   1346 C  CB  . VAL A 1 187 ? 88.773  4.878   -2.213  1.00 50.64  ? 186 VAL A CB  1 
ATOM   1347 C  CG1 . VAL A 1 187 ? 88.773  6.329   -2.672  1.00 50.17  ? 186 VAL A CG1 1 
ATOM   1348 C  CG2 . VAL A 1 187 ? 87.626  4.608   -1.246  1.00 40.79  ? 186 VAL A CG2 1 
ATOM   1349 N  N   . VAL A 1 188 ? 87.832  4.965   -5.459  1.00 44.02  ? 187 VAL A N   1 
ATOM   1350 C  CA  . VAL A 1 188 ? 86.770  5.407   -6.359  1.00 44.44  ? 187 VAL A CA  1 
ATOM   1351 C  C   . VAL A 1 188 ? 86.011  4.222   -6.946  1.00 44.58  ? 187 VAL A C   1 
ATOM   1352 O  O   . VAL A 1 188 ? 84.816  4.333   -7.250  1.00 47.95  ? 187 VAL A O   1 
ATOM   1353 C  CB  . VAL A 1 188 ? 87.353  6.317   -7.463  1.00 45.82  ? 187 VAL A CB  1 
ATOM   1354 C  CG1 . VAL A 1 188 ? 88.129  5.505   -8.491  1.00 35.97  ? 187 VAL A CG1 1 
ATOM   1355 C  CG2 . VAL A 1 188 ? 86.247  7.119   -8.134  1.00 47.52  ? 187 VAL A CG2 1 
ATOM   1356 N  N   . ILE A 1 189 ? 86.671  3.080   -7.114  1.00 45.18  ? 188 ILE A N   1 
ATOM   1357 C  CA  . ILE A 1 189 ? 86.035  1.913   -7.724  1.00 46.19  ? 188 ILE A CA  1 
ATOM   1358 C  C   . ILE A 1 189 ? 84.967  1.343   -6.792  1.00 47.47  ? 188 ILE A C   1 
ATOM   1359 O  O   . ILE A 1 189 ? 83.805  1.232   -7.210  1.00 49.70  ? 188 ILE A O   1 
ATOM   1360 C  CB  . ILE A 1 189 ? 87.073  0.849   -8.125  1.00 46.39  ? 188 ILE A CB  1 
ATOM   1361 C  CG1 . ILE A 1 189 ? 87.838  1.286   -9.376  1.00 44.60  ? 188 ILE A CG1 1 
ATOM   1362 C  CG2 . ILE A 1 189 ? 86.403  -0.499  -8.338  1.00 45.34  ? 188 ILE A CG2 1 
ATOM   1363 C  CD1 . ILE A 1 189 ? 89.223  0.688   -9.479  1.00 45.07  ? 188 ILE A CD1 1 
ATOM   1364 N  N   . PRO A 1 190 ? 85.278  0.973   -5.539  1.00 41.62  ? 189 PRO A N   1 
ATOM   1365 C  CA  . PRO A 1 190 ? 84.193  0.500   -4.661  1.00 45.06  ? 189 PRO A CA  1 
ATOM   1366 C  C   . PRO A 1 190 ? 83.197  1.582   -4.290  1.00 48.71  ? 189 PRO A C   1 
ATOM   1367 O  O   . PRO A 1 190 ? 82.003  1.289   -4.155  1.00 42.93  ? 189 PRO A O   1 
ATOM   1368 C  CB  . PRO A 1 190 ? 84.944  -0.026  -3.430  1.00 39.16  ? 189 PRO A CB  1 
ATOM   1369 C  CG  . PRO A 1 190 ? 86.207  0.733   -3.420  1.00 42.21  ? 189 PRO A CG  1 
ATOM   1370 C  CD  . PRO A 1 190 ? 86.583  0.882   -4.858  1.00 43.50  ? 189 PRO A CD  1 
ATOM   1371 N  N   . ALA A 1 191 ? 83.653  2.826   -4.110  1.00 45.96  ? 190 ALA A N   1 
ATOM   1372 C  CA  . ALA A 1 191 ? 82.737  3.906   -3.755  1.00 41.80  ? 190 ALA A CA  1 
ATOM   1373 C  C   . ALA A 1 191 ? 81.664  4.104   -4.819  1.00 43.18  ? 190 ALA A C   1 
ATOM   1374 O  O   . ALA A 1 191 ? 80.483  4.267   -4.494  1.00 42.54  ? 190 ALA A O   1 
ATOM   1375 C  CB  . ALA A 1 191 ? 83.514  5.203   -3.529  1.00 43.84  ? 190 ALA A CB  1 
ATOM   1376 N  N   . ALA A 1 192 ? 82.054  4.093   -6.095  1.00 37.81  ? 191 ALA A N   1 
ATOM   1377 C  CA  . ALA A 1 192 ? 81.065  4.222   -7.161  1.00 44.76  ? 191 ALA A CA  1 
ATOM   1378 C  C   . ALA A 1 192 ? 80.123  3.025   -7.184  1.00 48.49  ? 191 ALA A C   1 
ATOM   1379 O  O   . ALA A 1 192 ? 78.910  3.185   -7.361  1.00 53.41  ? 191 ALA A O   1 
ATOM   1380 C  CB  . ALA A 1 192 ? 81.761  4.387   -8.510  1.00 43.78  ? 191 ALA A CB  1 
ATOM   1381 N  N   . ILE A 1 193 ? 80.667  1.820   -7.009  1.00 47.41  ? 192 ILE A N   1 
ATOM   1382 C  CA  . ILE A 1 193 ? 79.840  0.616   -6.995  1.00 46.98  ? 192 ILE A CA  1 
ATOM   1383 C  C   . ILE A 1 193 ? 78.872  0.648   -5.818  1.00 48.59  ? 192 ILE A C   1 
ATOM   1384 O  O   . ILE A 1 193 ? 77.670  0.403   -5.972  1.00 51.63  ? 192 ILE A O   1 
ATOM   1385 C  CB  . ILE A 1 193 ? 80.727  -0.641  -6.967  1.00 51.71  ? 192 ILE A CB  1 
ATOM   1386 C  CG1 . ILE A 1 193 ? 81.314  -0.902  -8.354  1.00 51.70  ? 192 ILE A CG1 1 
ATOM   1387 C  CG2 . ILE A 1 193 ? 79.931  -1.847  -6.498  1.00 47.63  ? 192 ILE A CG2 1 
ATOM   1388 C  CD1 . ILE A 1 193 ? 82.630  -1.641  -8.332  1.00 47.53  ? 192 ILE A CD1 1 
ATOM   1389 N  N   . MET A 1 194 ? 79.383  0.958   -4.624  1.00 47.99  ? 193 MET A N   1 
ATOM   1390 C  CA  . MET A 1 194 ? 78.547  0.925   -3.427  1.00 48.80  ? 193 MET A CA  1 
ATOM   1391 C  C   . MET A 1 194 ? 77.446  1.977   -3.486  1.00 45.75  ? 193 MET A C   1 
ATOM   1392 O  O   . MET A 1 194 ? 76.312  1.720   -3.068  1.00 48.85  ? 193 MET A O   1 
ATOM   1393 C  CB  . MET A 1 194 ? 79.407  1.123   -2.179  1.00 48.29  ? 193 MET A CB  1 
ATOM   1394 C  CG  . MET A 1 194 ? 80.249  -0.087  -1.812  1.00 48.19  ? 193 MET A CG  1 
ATOM   1395 S  SD  . MET A 1 194 ? 79.277  -1.408  -1.068  1.00 60.15  ? 193 MET A SD  1 
ATOM   1396 C  CE  . MET A 1 194 ? 79.366  -2.647  -2.358  1.00 64.88  ? 193 MET A CE  1 
ATOM   1397 N  N   . LEU A 1 195 ? 77.763  3.170   -3.994  1.00 47.80  ? 194 LEU A N   1 
ATOM   1398 C  CA  . LEU A 1 195 ? 76.774  4.245   -4.041  1.00 47.57  ? 194 LEU A CA  1 
ATOM   1399 C  C   . LEU A 1 195 ? 75.589  3.867   -4.923  1.00 52.79  ? 194 LEU A C   1 
ATOM   1400 O  O   . LEU A 1 195 ? 74.429  4.069   -4.546  1.00 53.52  ? 194 LEU A O   1 
ATOM   1401 C  CB  . LEU A 1 195 ? 77.429  5.533   -4.541  1.00 46.13  ? 194 LEU A CB  1 
ATOM   1402 C  CG  . LEU A 1 195 ? 76.595  6.814   -4.464  1.00 45.61  ? 194 LEU A CG  1 
ATOM   1403 C  CD1 . LEU A 1 195 ? 76.430  7.262   -3.020  1.00 47.75  ? 194 LEU A CD1 1 
ATOM   1404 C  CD2 . LEU A 1 195 ? 77.218  7.915   -5.308  1.00 48.58  ? 194 LEU A CD2 1 
ATOM   1405 N  N   . ILE A 1 196 ? 75.865  3.311   -6.103  1.00 52.46  ? 195 ILE A N   1 
ATOM   1406 C  CA  . ILE A 1 196 ? 74.791  2.960   -7.030  1.00 53.99  ? 195 ILE A CA  1 
ATOM   1407 C  C   . ILE A 1 196 ? 74.050  1.719   -6.550  1.00 50.62  ? 195 ILE A C   1 
ATOM   1408 O  O   . ILE A 1 196 ? 72.815  1.658   -6.604  1.00 56.04  ? 195 ILE A O   1 
ATOM   1409 C  CB  . ILE A 1 196 ? 75.350  2.771   -8.454  1.00 58.45  ? 195 ILE A CB  1 
ATOM   1410 C  CG1 . ILE A 1 196 ? 76.015  4.054   -8.976  1.00 63.00  ? 195 ILE A CG1 1 
ATOM   1411 C  CG2 . ILE A 1 196 ? 74.249  2.315   -9.402  1.00 52.73  ? 195 ILE A CG2 1 
ATOM   1412 C  CD1 . ILE A 1 196 ? 75.454  5.357   -8.416  1.00 57.60  ? 195 ILE A CD1 1 
ATOM   1413 N  N   . LYS A 1 197 ? 74.785  0.710   -6.074  1.00 49.08  ? 196 LYS A N   1 
ATOM   1414 C  CA  . LYS A 1 197 ? 74.150  -0.543  -5.679  1.00 50.28  ? 196 LYS A CA  1 
ATOM   1415 C  C   . LYS A 1 197 ? 73.265  -0.363  -4.452  1.00 48.00  ? 196 LYS A C   1 
ATOM   1416 O  O   . LYS A 1 197 ? 72.217  -1.010  -4.348  1.00 54.31  ? 196 LYS A O   1 
ATOM   1417 C  CB  . LYS A 1 197 ? 75.220  -1.611  -5.439  1.00 51.50  ? 196 LYS A CB  1 
ATOM   1418 C  CG  . LYS A 1 197 ? 74.920  -2.601  -4.324  1.00 59.94  ? 196 LYS A CG  1 
ATOM   1419 C  CD  . LYS A 1 197 ? 76.130  -3.483  -4.048  1.00 64.59  ? 196 LYS A CD  1 
ATOM   1420 C  CE  . LYS A 1 197 ? 76.518  -4.276  -5.290  1.00 69.36  ? 196 LYS A CE  1 
ATOM   1421 N  NZ  . LYS A 1 197 ? 77.941  -4.714  -5.266  1.00 65.15  ? 196 LYS A NZ  1 
ATOM   1422 N  N   . ARG A 1 198 ? 73.650  0.517   -3.529  1.00 46.86  ? 197 ARG A N   1 
ATOM   1423 C  CA  . ARG A 1 198 ? 72.876  0.726   -2.311  1.00 48.65  ? 197 ARG A CA  1 
ATOM   1424 C  C   . ARG A 1 198 ? 71.671  1.636   -2.518  1.00 47.07  ? 197 ARG A C   1 
ATOM   1425 O  O   . ARG A 1 198 ? 70.906  1.844   -1.569  1.00 45.75  ? 197 ARG A O   1 
ATOM   1426 C  CB  . ARG A 1 198 ? 73.769  1.301   -1.208  1.00 45.89  ? 197 ARG A CB  1 
ATOM   1427 C  CG  . ARG A 1 198 ? 74.674  0.282   -0.537  1.00 43.98  ? 197 ARG A CG  1 
ATOM   1428 C  CD  . ARG A 1 198 ? 75.712  0.968   0.342   1.00 46.34  ? 197 ARG A CD  1 
ATOM   1429 N  NE  . ARG A 1 198 ? 75.174  1.345   1.645   1.00 46.76  ? 197 ARG A NE  1 
ATOM   1430 C  CZ  . ARG A 1 198 ? 74.970  0.503   2.649   1.00 44.04  ? 197 ARG A CZ  1 
ATOM   1431 N  NH1 . ARG A 1 198 ? 75.213  -0.792  2.526   1.00 45.36  ? 197 ARG A NH1 1 
ATOM   1432 N  NH2 . ARG A 1 198 ? 74.501  0.970   3.803   1.00 39.01  ? 197 ARG A NH2 1 
ATOM   1433 N  N   . GLY A 1 199 ? 71.482  2.182   -3.718  1.00 45.57  ? 198 GLY A N   1 
ATOM   1434 C  CA  . GLY A 1 199 ? 70.317  3.001   -3.988  1.00 43.18  ? 198 GLY A CA  1 
ATOM   1435 C  C   . GLY A 1 199 ? 70.314  4.354   -3.316  1.00 46.24  ? 198 GLY A C   1 
ATOM   1436 O  O   . GLY A 1 199 ? 69.241  4.927   -3.107  1.00 47.94  ? 198 GLY A O   1 
ATOM   1437 N  N   . VAL A 1 200 ? 71.488  4.884   -2.968  1.00 54.38  ? 199 VAL A N   1 
ATOM   1438 C  CA  . VAL A 1 200 ? 71.559  6.153   -2.245  1.00 61.49  ? 199 VAL A CA  1 
ATOM   1439 C  C   . VAL A 1 200 ? 71.030  7.290   -3.112  1.00 53.40  ? 199 VAL A C   1 
ATOM   1440 O  O   . VAL A 1 200 ? 70.099  8.009   -2.730  1.00 51.09  ? 199 VAL A O   1 
ATOM   1441 C  CB  . VAL A 1 200 ? 73.000  6.422   -1.781  1.00 54.93  ? 199 VAL A CB  1 
ATOM   1442 C  CG1 . VAL A 1 200 ? 73.010  7.369   -0.595  1.00 42.56  ? 199 VAL A CG1 1 
ATOM   1443 C  CG2 . VAL A 1 200 ? 73.698  5.111   -1.443  1.00 49.29  ? 199 VAL A CG2 1 
ATOM   1444 N  N   . ILE A 1 201 ? 71.607  7.458   -4.298  1.00 50.12  ? 200 ILE A N   1 
ATOM   1445 C  CA  . ILE A 1 201 ? 71.134  8.458   -5.253  1.00 52.10  ? 200 ILE A CA  1 
ATOM   1446 C  C   . ILE A 1 201 ? 71.132  7.850   -6.647  1.00 57.06  ? 200 ILE A C   1 
ATOM   1447 O  O   . ILE A 1 201 ? 71.856  6.886   -6.925  1.00 46.53  ? 200 ILE A O   1 
ATOM   1448 C  CB  . ILE A 1 201 ? 72.002  9.734   -5.235  1.00 52.50  ? 200 ILE A CB  1 
ATOM   1449 C  CG1 . ILE A 1 201 ? 73.490  9.375   -5.280  1.00 49.75  ? 200 ILE A CG1 1 
ATOM   1450 C  CG2 . ILE A 1 201 ? 71.671  10.594  -4.025  1.00 50.70  ? 200 ILE A CG2 1 
ATOM   1451 C  CD1 . ILE A 1 201 ? 74.308  10.290  -6.163  1.00 43.25  ? 200 ILE A CD1 1 
ATOM   1452 N  N   . PRO A 1 202 ? 70.329  8.410   -7.550  1.00 58.05  ? 201 PRO A N   1 
ATOM   1453 C  CA  . PRO A 1 202 ? 70.445  8.029   -8.962  1.00 52.79  ? 201 PRO A CA  1 
ATOM   1454 C  C   . PRO A 1 202 ? 71.796  8.424   -9.537  1.00 57.95  ? 201 PRO A C   1 
ATOM   1455 O  O   . PRO A 1 202 ? 72.388  9.439   -9.161  1.00 56.66  ? 201 PRO A O   1 
ATOM   1456 C  CB  . PRO A 1 202 ? 69.301  8.797   -9.637  1.00 52.50  ? 201 PRO A CB  1 
ATOM   1457 C  CG  . PRO A 1 202 ? 68.376  9.189   -8.528  1.00 53.91  ? 201 PRO A CG  1 
ATOM   1458 C  CD  . PRO A 1 202 ? 69.225  9.356   -7.316  1.00 52.60  ? 201 PRO A CD  1 
ATOM   1459 N  N   . LEU A 1 203 ? 72.290  7.585   -10.452 1.00 63.73  ? 202 LEU A N   1 
ATOM   1460 C  CA  . LEU A 1 203 ? 73.574  7.847   -11.093 1.00 59.97  ? 202 LEU A CA  1 
ATOM   1461 C  C   . LEU A 1 203 ? 73.575  9.188   -11.817 1.00 61.08  ? 202 LEU A C   1 
ATOM   1462 O  O   . LEU A 1 203 ? 74.614  9.856   -11.888 1.00 59.31  ? 202 LEU A O   1 
ATOM   1463 C  CB  . LEU A 1 203 ? 73.905  6.713   -12.065 1.00 62.19  ? 202 LEU A CB  1 
ATOM   1464 C  CG  . LEU A 1 203 ? 75.220  6.765   -12.845 1.00 70.20  ? 202 LEU A CG  1 
ATOM   1465 C  CD1 . LEU A 1 203 ? 76.393  7.034   -11.912 1.00 61.67  ? 202 LEU A CD1 1 
ATOM   1466 C  CD2 . LEU A 1 203 ? 75.429  5.471   -13.621 1.00 56.14  ? 202 LEU A CD2 1 
ATOM   1467 N  N   . SER A 1 204 ? 72.424  9.594   -12.362 1.00 60.78  ? 203 SER A N   1 
ATOM   1468 C  CA  . SER A 1 204 ? 72.346  10.818  -13.151 1.00 59.54  ? 203 SER A CA  1 
ATOM   1469 C  C   . SER A 1 204 ? 72.634  12.068  -12.330 1.00 56.87  ? 203 SER A C   1 
ATOM   1470 O  O   . SER A 1 204 ? 72.955  13.111  -12.910 1.00 55.34  ? 203 SER A O   1 
ATOM   1471 C  CB  . SER A 1 204 ? 70.968  10.932  -13.801 1.00 60.03  ? 203 SER A CB  1 
ATOM   1472 O  OG  . SER A 1 204 ? 69.946  10.952  -12.821 1.00 62.01  ? 203 SER A OG  1 
ATOM   1473 N  N   . TYR A 1 205 ? 72.518  11.989  -11.001 1.00 52.55  ? 204 TYR A N   1 
ATOM   1474 C  CA  . TYR A 1 205 ? 72.806  13.147  -10.160 1.00 49.69  ? 204 TYR A CA  1 
ATOM   1475 C  C   . TYR A 1 205 ? 74.239  13.630  -10.335 1.00 49.98  ? 204 TYR A C   1 
ATOM   1476 O  O   . TYR A 1 205 ? 74.522  14.816  -10.133 1.00 52.81  ? 204 TYR A O   1 
ATOM   1477 C  CB  . TYR A 1 205 ? 72.550  12.813  -8.689  1.00 55.41  ? 204 TYR A CB  1 
ATOM   1478 C  CG  . TYR A 1 205 ? 71.101  12.892  -8.259  1.00 48.09  ? 204 TYR A CG  1 
ATOM   1479 C  CD1 . TYR A 1 205 ? 70.073  12.890  -9.193  1.00 52.00  ? 204 TYR A CD1 1 
ATOM   1480 C  CD2 . TYR A 1 205 ? 70.764  12.979  -6.915  1.00 47.23  ? 204 TYR A CD2 1 
ATOM   1481 C  CE1 . TYR A 1 205 ? 68.748  12.965  -8.798  1.00 53.44  ? 204 TYR A CE1 1 
ATOM   1482 C  CE2 . TYR A 1 205 ? 69.443  13.055  -6.512  1.00 51.93  ? 204 TYR A CE2 1 
ATOM   1483 C  CZ  . TYR A 1 205 ? 68.441  13.048  -7.457  1.00 44.89  ? 204 TYR A CZ  1 
ATOM   1484 O  OH  . TYR A 1 205 ? 67.129  13.125  -7.054  1.00 42.51  ? 204 TYR A OH  1 
ATOM   1485 N  N   . LEU A 1 206 ? 75.150  12.733  -10.711 1.00 49.76  ? 205 LEU A N   1 
ATOM   1486 C  CA  . LEU A 1 206 ? 76.568  13.054  -10.821 1.00 46.38  ? 205 LEU A CA  1 
ATOM   1487 C  C   . LEU A 1 206 ? 76.935  13.742  -12.131 1.00 47.46  ? 205 LEU A C   1 
ATOM   1488 O  O   . LEU A 1 206 ? 78.105  14.099  -12.310 1.00 53.29  ? 205 LEU A O   1 
ATOM   1489 C  CB  . LEU A 1 206 ? 77.402  11.781  -10.649 1.00 46.33  ? 205 LEU A CB  1 
ATOM   1490 C  CG  . LEU A 1 206 ? 77.437  11.218  -9.226  1.00 50.72  ? 205 LEU A CG  1 
ATOM   1491 C  CD1 . LEU A 1 206 ? 77.912  9.774   -9.229  1.00 48.74  ? 205 LEU A CD1 1 
ATOM   1492 C  CD2 . LEU A 1 206 ? 78.311  12.081  -8.326  1.00 43.89  ? 205 LEU A CD2 1 
ATOM   1493 N  N   . LYS A 1 207 ? 75.988  13.931  -13.043 1.00 51.90  ? 206 LYS A N   1 
ATOM   1494 C  CA  . LYS A 1 207 ? 76.275  14.686  -14.258 1.00 49.33  ? 206 LYS A CA  1 
ATOM   1495 C  C   . LYS A 1 207 ? 76.579  16.134  -13.893 1.00 49.73  ? 206 LYS A C   1 
ATOM   1496 O  O   . LYS A 1 207 ? 75.806  16.756  -13.155 1.00 50.54  ? 206 LYS A O   1 
ATOM   1497 C  CB  . LYS A 1 207 ? 75.106  14.615  -15.236 1.00 48.83  ? 206 LYS A CB  1 
ATOM   1498 C  CG  . LYS A 1 207 ? 74.847  13.215  -15.778 1.00 64.45  ? 206 LYS A CG  1 
ATOM   1499 C  CD  . LYS A 1 207 ? 73.514  13.137  -16.496 1.00 66.38  ? 206 LYS A CD  1 
ATOM   1500 C  CE  . LYS A 1 207 ? 73.597  12.176  -17.664 1.00 67.39  ? 206 LYS A CE  1 
ATOM   1501 N  NZ  . LYS A 1 207 ? 72.277  11.939  -18.302 1.00 78.26  ? 206 LYS A NZ  1 
ATOM   1502 N  N   . PRO A 1 208 ? 77.691  16.695  -14.367 1.00 48.07  ? 207 PRO A N   1 
ATOM   1503 C  CA  . PRO A 1 208 ? 78.046  18.069  -13.990 1.00 48.62  ? 207 PRO A CA  1 
ATOM   1504 C  C   . PRO A 1 208 ? 76.978  19.072  -14.406 1.00 44.11  ? 207 PRO A C   1 
ATOM   1505 O  O   . PRO A 1 208 ? 76.522  19.087  -15.552 1.00 50.60  ? 207 PRO A O   1 
ATOM   1506 C  CB  . PRO A 1 208 ? 79.369  18.310  -14.729 1.00 48.53  ? 207 PRO A CB  1 
ATOM   1507 C  CG  . PRO A 1 208 ? 79.905  16.952  -15.030 1.00 47.14  ? 207 PRO A CG  1 
ATOM   1508 C  CD  . PRO A 1 208 ? 78.709  16.071  -15.229 1.00 44.04  ? 207 PRO A CD  1 
ATOM   1509 N  N   . SER A 1 209 ? 76.579  19.909  -13.452 1.00 43.48  ? 208 SER A N   1 
ATOM   1510 C  CA  . SER A 1 209 ? 75.726  21.061  -13.696 1.00 43.61  ? 208 SER A CA  1 
ATOM   1511 C  C   . SER A 1 209 ? 76.271  22.223  -12.879 1.00 49.74  ? 208 SER A C   1 
ATOM   1512 O  O   . SER A 1 209 ? 77.162  22.052  -12.044 1.00 49.79  ? 208 SER A O   1 
ATOM   1513 C  CB  . SER A 1 209 ? 74.264  20.771  -13.336 1.00 39.09  ? 208 SER A CB  1 
ATOM   1514 O  OG  . SER A 1 209 ? 74.125  20.498  -11.952 1.00 40.66  ? 208 SER A OG  1 
ATOM   1515 N  N   . TRP A 1 210 ? 75.730  23.417  -13.108 1.00 53.72  ? 209 TRP A N   1 
ATOM   1516 C  CA  . TRP A 1 210 ? 76.181  24.595  -12.380 1.00 48.61  ? 209 TRP A CA  1 
ATOM   1517 C  C   . TRP A 1 210 ? 75.001  25.334  -11.767 1.00 53.49  ? 209 TRP A C   1 
ATOM   1518 O  O   . TRP A 1 210 ? 74.046  25.685  -12.466 1.00 55.21  ? 209 TRP A O   1 
ATOM   1519 C  CB  . TRP A 1 210 ? 76.982  25.537  -13.281 1.00 50.84  ? 209 TRP A CB  1 
ATOM   1520 C  CG  . TRP A 1 210 ? 77.796  26.514  -12.497 1.00 53.55  ? 209 TRP A CG  1 
ATOM   1521 C  CD1 . TRP A 1 210 ? 77.506  27.827  -12.270 1.00 45.11  ? 209 TRP A CD1 1 
ATOM   1522 C  CD2 . TRP A 1 210 ? 79.023  26.249  -11.804 1.00 51.00  ? 209 TRP A CD2 1 
ATOM   1523 N  NE1 . TRP A 1 210 ? 78.483  28.401  -11.494 1.00 45.49  ? 209 TRP A NE1 1 
ATOM   1524 C  CE2 . TRP A 1 210 ? 79.426  27.453  -11.194 1.00 49.93  ? 209 TRP A CE2 1 
ATOM   1525 C  CE3 . TRP A 1 210 ? 79.824  25.113  -11.649 1.00 45.16  ? 209 TRP A CE3 1 
ATOM   1526 C  CZ2 . TRP A 1 210 ? 80.594  27.555  -10.440 1.00 48.85  ? 209 TRP A CZ2 1 
ATOM   1527 C  CZ3 . TRP A 1 210 ? 80.983  25.215  -10.899 1.00 50.21  ? 209 TRP A CZ3 1 
ATOM   1528 C  CH2 . TRP A 1 210 ? 81.356  26.427  -10.304 1.00 54.37  ? 209 TRP A CH2 1 
ATOM   1529 N  N   . ASP A 1 211 ? 75.085  25.575  -10.460 1.00 49.89  ? 210 ASP A N   1 
ATOM   1530 C  CA  . ASP A 1 211 ? 74.156  26.438  -9.742  1.00 43.93  ? 210 ASP A CA  1 
ATOM   1531 C  C   . ASP A 1 211 ? 74.975  27.486  -9.005  1.00 49.64  ? 210 ASP A C   1 
ATOM   1532 O  O   . ASP A 1 211 ? 75.778  27.143  -8.131  1.00 48.91  ? 210 ASP A O   1 
ATOM   1533 C  CB  . ASP A 1 211 ? 73.299  25.629  -8.765  1.00 44.95  ? 210 ASP A CB  1 
ATOM   1534 C  CG  . ASP A 1 211 ? 72.125  26.417  -8.224  1.00 50.45  ? 210 ASP A CG  1 
ATOM   1535 O  OD1 . ASP A 1 211 ? 72.322  27.217  -7.284  1.00 51.15  ? 210 ASP A OD1 1 
ATOM   1536 O  OD2 . ASP A 1 211 ? 71.002  26.225  -8.734  1.00 58.75  ? 210 ASP A OD2 1 
ATOM   1537 N  N   . ASN A 1 212 ? 74.774  28.758  -9.360  1.00 52.98  ? 211 ASN A N   1 
ATOM   1538 C  CA  . ASN A 1 212 ? 75.620  29.822  -8.824  1.00 44.72  ? 211 ASN A CA  1 
ATOM   1539 C  C   . ASN A 1 212 ? 75.517  29.907  -7.306  1.00 46.92  ? 211 ASN A C   1 
ATOM   1540 O  O   . ASN A 1 212 ? 76.533  30.066  -6.617  1.00 47.95  ? 211 ASN A O   1 
ATOM   1541 C  CB  . ASN A 1 212 ? 75.251  31.157  -9.468  1.00 39.45  ? 211 ASN A CB  1 
ATOM   1542 C  CG  . ASN A 1 212 ? 76.033  31.421  -10.737 1.00 52.84  ? 211 ASN A CG  1 
ATOM   1543 O  OD1 . ASN A 1 212 ? 77.128  30.889  -10.923 1.00 53.33  ? 211 ASN A OD1 1 
ATOM   1544 N  ND2 . ASN A 1 212 ? 75.474  32.237  -11.623 1.00 56.15  ? 211 ASN A ND2 1 
ATOM   1545 N  N   . GLY A 1 213 ? 74.303  29.819  -6.768  1.00 47.13  ? 212 GLY A N   1 
ATOM   1546 C  CA  . GLY A 1 213 ? 74.108  29.853  -5.333  1.00 47.37  ? 212 GLY A CA  1 
ATOM   1547 C  C   . GLY A 1 213 ? 74.859  28.751  -4.615  1.00 51.68  ? 212 GLY A C   1 
ATOM   1548 O  O   . GLY A 1 213 ? 75.667  29.022  -3.721  1.00 54.27  ? 212 GLY A O   1 
ATOM   1549 N  N   . LEU A 1 214 ? 74.592  27.497  -4.996  1.00 50.14  ? 213 LEU A N   1 
ATOM   1550 C  CA  . LEU A 1 214 ? 75.244  26.371  -4.335  1.00 46.08  ? 213 LEU A CA  1 
ATOM   1551 C  C   . LEU A 1 214 ? 76.753  26.395  -4.537  1.00 45.02  ? 213 LEU A C   1 
ATOM   1552 O  O   . LEU A 1 214 ? 77.503  25.973  -3.650  1.00 45.63  ? 213 LEU A O   1 
ATOM   1553 C  CB  . LEU A 1 214 ? 74.659  25.053  -4.840  1.00 47.35  ? 213 LEU A CB  1 
ATOM   1554 C  CG  . LEU A 1 214 ? 73.211  24.781  -4.432  1.00 46.61  ? 213 LEU A CG  1 
ATOM   1555 C  CD1 . LEU A 1 214 ? 72.670  23.558  -5.150  1.00 48.35  ? 213 LEU A CD1 1 
ATOM   1556 C  CD2 . LEU A 1 214 ? 73.114  24.610  -2.926  1.00 44.06  ? 213 LEU A CD2 1 
ATOM   1557 N  N   . ALA A 1 215 ? 77.217  26.876  -5.693  1.00 42.50  ? 214 ALA A N   1 
ATOM   1558 C  CA  . ALA A 1 215 ? 78.654  26.988  -5.925  1.00 45.95  ? 214 ALA A CA  1 
ATOM   1559 C  C   . ALA A 1 215 ? 79.288  27.960  -4.939  1.00 49.81  ? 214 ALA A C   1 
ATOM   1560 O  O   . ALA A 1 215 ? 80.339  27.674  -4.353  1.00 45.78  ? 214 ALA A O   1 
ATOM   1561 C  CB  . ALA A 1 215 ? 78.923  27.422  -7.365  1.00 41.05  ? 214 ALA A CB  1 
ATOM   1562 N  N   . GLY A 1 216 ? 78.663  29.126  -4.751  1.00 45.28  ? 215 GLY A N   1 
ATOM   1563 C  CA  . GLY A 1 216 ? 79.141  30.062  -3.750  1.00 45.94  ? 215 GLY A CA  1 
ATOM   1564 C  C   . GLY A 1 216 ? 79.102  29.495  -2.345  1.00 44.01  ? 215 GLY A C   1 
ATOM   1565 O  O   . GLY A 1 216 ? 79.962  29.810  -1.519  1.00 47.78  ? 215 GLY A O   1 
ATOM   1566 N  N   . GLN A 1 217 ? 78.104  28.658  -2.053  1.00 45.80  ? 216 GLN A N   1 
ATOM   1567 C  CA  . GLN A 1 217 ? 78.003  28.074  -0.720  1.00 47.84  ? 216 GLN A CA  1 
ATOM   1568 C  C   . GLN A 1 217 ? 79.069  27.008  -0.503  1.00 46.83  ? 216 GLN A C   1 
ATOM   1569 O  O   . GLN A 1 217 ? 79.672  26.938  0.574   1.00 47.83  ? 216 GLN A O   1 
ATOM   1570 C  CB  . GLN A 1 217 ? 76.607  27.487  -0.517  1.00 46.26  ? 216 GLN A CB  1 
ATOM   1571 C  CG  . GLN A 1 217 ? 75.575  28.485  -0.022  1.00 40.00  ? 216 GLN A CG  1 
ATOM   1572 C  CD  . GLN A 1 217 ? 74.179  27.898  0.013   1.00 45.70  ? 216 GLN A CD  1 
ATOM   1573 O  OE1 . GLN A 1 217 ? 73.698  27.359  -0.983  1.00 56.36  ? 216 GLN A OE1 1 
ATOM   1574 N  NE2 . GLN A 1 217 ? 73.523  27.993  1.164   1.00 46.72  ? 216 GLN A NE2 1 
ATOM   1575 N  N   . LEU A 1 218 ? 79.307  26.163  -1.509  1.00 47.33  ? 217 LEU A N   1 
ATOM   1576 C  CA  . LEU A 1 218 ? 80.378  25.179  -1.400  1.00 48.58  ? 217 LEU A CA  1 
ATOM   1577 C  C   . LEU A 1 218 ? 81.744  25.849  -1.358  1.00 46.10  ? 217 LEU A C   1 
ATOM   1578 O  O   . LEU A 1 218 ? 82.687  25.301  -0.775  1.00 43.48  ? 217 LEU A O   1 
ATOM   1579 C  CB  . LEU A 1 218 ? 80.304  24.189  -2.563  1.00 43.88  ? 217 LEU A CB  1 
ATOM   1580 C  CG  . LEU A 1 218 ? 79.105  23.239  -2.573  1.00 42.62  ? 217 LEU A CG  1 
ATOM   1581 C  CD1 . LEU A 1 218 ? 78.806  22.776  -3.988  1.00 40.28  ? 217 LEU A CD1 1 
ATOM   1582 C  CD2 . LEU A 1 218 ? 79.363  22.050  -1.661  1.00 41.62  ? 217 LEU A CD2 1 
ATOM   1583 N  N   . SER A 1 219 ? 81.867  27.030  -1.973  1.00 47.81  ? 218 SER A N   1 
ATOM   1584 C  CA  . SER A 1 219 ? 83.123  27.771  -1.936  1.00 49.61  ? 218 SER A CA  1 
ATOM   1585 C  C   . SER A 1 219 ? 83.515  28.157  -0.516  1.00 46.13  ? 218 SER A C   1 
ATOM   1586 O  O   . SER A 1 219 ? 84.708  28.278  -0.216  1.00 45.21  ? 218 SER A O   1 
ATOM   1587 C  CB  . SER A 1 219 ? 83.019  29.017  -2.815  1.00 43.96  ? 218 SER A CB  1 
ATOM   1588 O  OG  . SER A 1 219 ? 82.687  28.671  -4.148  1.00 50.64  ? 218 SER A OG  1 
ATOM   1589 N  N   . LYS A 1 220 ? 82.532  28.359  0.367   1.00 45.74  ? 219 LYS A N   1 
ATOM   1590 C  CA  . LYS A 1 220 ? 82.840  28.657  1.762   1.00 47.01  ? 219 LYS A CA  1 
ATOM   1591 C  C   . LYS A 1 220 ? 83.652  27.545  2.408   1.00 46.30  ? 219 LYS A C   1 
ATOM   1592 O  O   . LYS A 1 220 ? 84.526  27.815  3.238   1.00 49.34  ? 219 LYS A O   1 
ATOM   1593 C  CB  . LYS A 1 220 ? 81.549  28.887  2.549   1.00 43.94  ? 219 LYS A CB  1 
ATOM   1594 C  CG  . LYS A 1 220 ? 80.849  30.198  2.241   1.00 45.31  ? 219 LYS A CG  1 
ATOM   1595 C  CD  . LYS A 1 220 ? 79.875  30.567  3.348   1.00 50.12  ? 219 LYS A CD  1 
ATOM   1596 C  CE  . LYS A 1 220 ? 78.784  29.518  3.490   1.00 53.25  ? 219 LYS A CE  1 
ATOM   1597 N  NZ  . LYS A 1 220 ? 77.665  29.988  4.351   1.00 60.32  ? 219 LYS A NZ  1 
ATOM   1598 N  N   . PHE A 1 221 ? 83.399  26.295  2.022   1.00 41.95  ? 220 PHE A N   1 
ATOM   1599 C  CA  . PHE A 1 221 ? 84.151  25.176  2.572   1.00 41.82  ? 220 PHE A CA  1 
ATOM   1600 C  C   . PHE A 1 221 ? 85.537  25.062  1.950   1.00 47.38  ? 220 PHE A C   1 
ATOM   1601 O  O   . PHE A 1 221 ? 86.472  24.597  2.611   1.00 47.95  ? 220 PHE A O   1 
ATOM   1602 C  CB  . PHE A 1 221 ? 83.364  23.879  2.385   1.00 38.88  ? 220 PHE A CB  1 
ATOM   1603 C  CG  . PHE A 1 221 ? 82.071  23.842  3.154   1.00 48.41  ? 220 PHE A CG  1 
ATOM   1604 C  CD1 . PHE A 1 221 ? 80.951  24.518  2.693   1.00 41.72  ? 220 PHE A CD1 1 
ATOM   1605 C  CD2 . PHE A 1 221 ? 81.976  23.134  4.340   1.00 44.47  ? 220 PHE A CD2 1 
ATOM   1606 C  CE1 . PHE A 1 221 ? 79.765  24.485  3.400   1.00 44.56  ? 220 PHE A CE1 1 
ATOM   1607 C  CE2 . PHE A 1 221 ? 80.793  23.100  5.052   1.00 44.82  ? 220 PHE A CE2 1 
ATOM   1608 C  CZ  . PHE A 1 221 ? 79.686  23.775  4.580   1.00 46.26  ? 220 PHE A CZ  1 
ATOM   1609 N  N   . THR A 1 222 ? 85.685  25.472  0.688   1.00 42.82  ? 221 THR A N   1 
ATOM   1610 C  CA  . THR A 1 222 ? 87.016  25.630  0.115   1.00 46.36  ? 221 THR A CA  1 
ATOM   1611 C  C   . THR A 1 222 ? 87.836  26.643  0.905   1.00 47.29  ? 221 THR A C   1 
ATOM   1612 O  O   . THR A 1 222 ? 89.026  26.425  1.164   1.00 47.07  ? 221 THR A O   1 
ATOM   1613 C  CB  . THR A 1 222 ? 86.908  26.061  -1.349  1.00 48.37  ? 221 THR A CB  1 
ATOM   1614 O  OG1 . THR A 1 222 ? 86.191  25.068  -2.091  1.00 51.07  ? 221 THR A OG1 1 
ATOM   1615 C  CG2 . THR A 1 222 ? 88.289  26.247  -1.958  1.00 40.65  ? 221 THR A CG2 1 
ATOM   1616 N  N   . LEU A 1 223 ? 87.216  27.757  1.300   1.00 46.85  ? 222 LEU A N   1 
ATOM   1617 C  CA  . LEU A 1 223 ? 87.954  28.797  2.009   1.00 52.46  ? 222 LEU A CA  1 
ATOM   1618 C  C   . LEU A 1 223 ? 88.359  28.343  3.407   1.00 49.57  ? 222 LEU A C   1 
ATOM   1619 O  O   . LEU A 1 223 ? 89.439  28.703  3.890   1.00 49.28  ? 222 LEU A O   1 
ATOM   1620 C  CB  . LEU A 1 223 ? 87.120  30.076  2.075   1.00 50.85  ? 222 LEU A CB  1 
ATOM   1621 C  CG  . LEU A 1 223 ? 86.682  30.637  0.719   1.00 52.63  ? 222 LEU A CG  1 
ATOM   1622 C  CD1 . LEU A 1 223 ? 85.360  31.376  0.848   1.00 49.71  ? 222 LEU A CD1 1 
ATOM   1623 C  CD2 . LEU A 1 223 ? 87.747  31.541  0.120   1.00 53.37  ? 222 LEU A CD2 1 
ATOM   1624 N  N   . MET A 1 224 ? 87.512  27.553  4.074   1.00 47.83  ? 223 MET A N   1 
ATOM   1625 C  CA  . MET A 1 224 ? 87.915  26.968  5.351   1.00 52.38  ? 223 MET A CA  1 
ATOM   1626 C  C   . MET A 1 224 ? 89.070  25.992  5.173   1.00 47.62  ? 223 MET A C   1 
ATOM   1627 O  O   . MET A 1 224 ? 89.980  25.941  6.008   1.00 49.24  ? 223 MET A O   1 
ATOM   1628 C  CB  . MET A 1 224 ? 86.731  26.289  6.042   1.00 42.92  ? 223 MET A CB  1 
ATOM   1629 C  CG  . MET A 1 224 ? 85.472  27.133  6.101   1.00 46.82  ? 223 MET A CG  1 
ATOM   1630 S  SD  . MET A 1 224 ? 84.135  26.327  7.001   1.00 60.15  ? 223 MET A SD  1 
ATOM   1631 C  CE  . MET A 1 224 ? 84.196  24.696  6.282   1.00 51.67  ? 223 MET A CE  1 
ATOM   1632 N  N   . ALA A 1 225 ? 89.045  25.198  4.099   1.00 45.42  ? 224 ALA A N   1 
ATOM   1633 C  CA  . ALA A 1 225 ? 90.155  24.292  3.824   1.00 46.83  ? 224 ALA A CA  1 
ATOM   1634 C  C   . ALA A 1 225 ? 91.446  25.068  3.601   1.00 50.98  ? 224 ALA A C   1 
ATOM   1635 O  O   . ALA A 1 225 ? 92.519  24.648  4.048   1.00 50.19  ? 224 ALA A O   1 
ATOM   1636 C  CB  . ALA A 1 225 ? 89.835  23.416  2.612   1.00 41.70  ? 224 ALA A CB  1 
ATOM   1637 N  N   . LEU A 1 226 ? 91.359  26.201  2.900   1.00 53.73  ? 225 LEU A N   1 
ATOM   1638 C  CA  . LEU A 1 226 ? 92.536  27.034  2.679   1.00 49.28  ? 225 LEU A CA  1 
ATOM   1639 C  C   . LEU A 1 226 ? 93.073  27.580  3.997   1.00 51.64  ? 225 LEU A C   1 
ATOM   1640 O  O   . LEU A 1 226 ? 94.287  27.572  4.232   1.00 54.14  ? 225 LEU A O   1 
ATOM   1641 C  CB  . LEU A 1 226 ? 92.199  28.173  1.717   1.00 47.94  ? 225 LEU A CB  1 
ATOM   1642 C  CG  . LEU A 1 226 ? 92.587  27.940  0.256   1.00 49.67  ? 225 LEU A CG  1 
ATOM   1643 C  CD1 . LEU A 1 226 ? 92.025  29.038  -0.632  1.00 60.08  ? 225 LEU A CD1 1 
ATOM   1644 C  CD2 . LEU A 1 226 ? 94.099  27.855  0.115   1.00 65.42  ? 225 LEU A CD2 1 
ATOM   1645 N  N   . ILE A 1 227 ? 92.183  28.075  4.861   1.00 45.93  ? 226 ILE A N   1 
ATOM   1646 C  CA  . ILE A 1 227 ? 92.608  28.622  6.147   1.00 48.86  ? 226 ILE A CA  1 
ATOM   1647 C  C   . ILE A 1 227 ? 93.240  27.536  7.008   1.00 54.02  ? 226 ILE A C   1 
ATOM   1648 O  O   . ILE A 1 227 ? 94.270  27.758  7.656   1.00 60.65  ? 226 ILE A O   1 
ATOM   1649 C  CB  . ILE A 1 227 ? 91.418  29.287  6.864   1.00 52.85  ? 226 ILE A CB  1 
ATOM   1650 C  CG1 . ILE A 1 227 ? 90.956  30.529  6.102   1.00 50.85  ? 226 ILE A CG1 1 
ATOM   1651 C  CG2 . ILE A 1 227 ? 91.780  29.638  8.302   1.00 51.27  ? 226 ILE A CG2 1 
ATOM   1652 C  CD1 . ILE A 1 227 ? 89.506  30.880  6.340   1.00 41.15  ? 226 ILE A CD1 1 
ATOM   1653 N  N   . THR A 1 228 ? 92.643  26.342  7.020   1.00 49.03  ? 227 THR A N   1 
ATOM   1654 C  CA  . THR A 1 228 ? 93.135  25.279  7.891   1.00 52.58  ? 227 THR A CA  1 
ATOM   1655 C  C   . THR A 1 228 ? 94.527  24.813  7.479   1.00 54.95  ? 227 THR A C   1 
ATOM   1656 O  O   . THR A 1 228 ? 95.353  24.489  8.341   1.00 60.17  ? 227 THR A O   1 
ATOM   1657 C  CB  . THR A 1 228 ? 92.142  24.112  7.894   1.00 51.64  ? 227 THR A CB  1 
ATOM   1658 O  OG1 . THR A 1 228 ? 92.520  23.169  8.903   1.00 52.05  ? 227 THR A OG1 1 
ATOM   1659 C  CG2 . THR A 1 228 ? 92.098  23.407  6.543   1.00 43.47  ? 227 THR A CG2 1 
ATOM   1660 N  N   . SER A 1 229 ? 94.822  24.814  6.179   1.00 50.05  ? 228 SER A N   1 
ATOM   1661 C  CA  . SER A 1 229 ? 96.122  24.363  5.696   1.00 58.46  ? 228 SER A CA  1 
ATOM   1662 C  C   . SER A 1 229 ? 97.254  25.334  6.014   1.00 55.46  ? 228 SER A C   1 
ATOM   1663 O  O   . SER A 1 229 ? 98.396  25.060  5.627   1.00 56.95  ? 228 SER A O   1 
ATOM   1664 C  CB  . SER A 1 229 ? 96.057  24.129  4.186   1.00 58.05  ? 228 SER A CB  1 
ATOM   1665 O  OG  . SER A 1 229 ? 95.880  25.349  3.486   1.00 59.14  ? 228 SER A OG  1 
ATOM   1666 N  N   . VAL A 1 230 ? 96.984  26.447  6.696   1.00 58.18  ? 229 VAL A N   1 
ATOM   1667 C  CA  . VAL A 1 230 ? 98.019  27.439  6.970   1.00 57.72  ? 229 VAL A CA  1 
ATOM   1668 C  C   . VAL A 1 230 ? 98.206  27.633  8.470   1.00 58.01  ? 229 VAL A C   1 
ATOM   1669 O  O   . VAL A 1 230 ? 99.305  27.432  8.995   1.00 59.31  ? 229 VAL A O   1 
ATOM   1670 C  CB  . VAL A 1 230 ? 97.690  28.778  6.281   1.00 55.71  ? 229 VAL A CB  1 
ATOM   1671 C  CG1 . VAL A 1 230 ? 98.508  29.913  6.887   1.00 53.76  ? 229 VAL A CG1 1 
ATOM   1672 C  CG2 . VAL A 1 230 ? 97.937  28.677  4.782   1.00 55.19  ? 229 VAL A CG2 1 
ATOM   1673 N  N   . THR A 1 231 ? 97.133  28.017  9.166   1.00 52.94  ? 230 THR A N   1 
ATOM   1674 C  CA  . THR A 1 231 ? 97.223  28.567  10.517  1.00 57.36  ? 230 THR A CA  1 
ATOM   1675 C  C   . THR A 1 231 ? 97.973  27.669  11.496  1.00 60.65  ? 230 THR A C   1 
ATOM   1676 O  O   . THR A 1 231 ? 99.068  28.018  11.947  1.00 65.43  ? 230 THR A O   1 
ATOM   1677 C  CB  . THR A 1 231 ? 95.824  28.845  11.067  1.00 57.34  ? 230 THR A CB  1 
ATOM   1678 O  OG1 . THR A 1 231 ? 95.162  27.599  11.317  1.00 55.36  ? 230 THR A OG1 1 
ATOM   1679 C  CG2 . THR A 1 231 ? 95.011  29.663  10.076  1.00 50.02  ? 230 THR A CG2 1 
ATOM   1680 N  N   . LEU A 1 232 ? 97.402  26.514  11.825  1.00 58.44  ? 231 LEU A N   1 
ATOM   1681 C  CA  . LEU A 1 232 ? 98.039  25.628  12.794  1.00 58.18  ? 231 LEU A CA  1 
ATOM   1682 C  C   . LEU A 1 232 ? 99.294  24.957  12.237  1.00 58.23  ? 231 LEU A C   1 
ATOM   1683 O  O   . LEU A 1 232 ? 100.261 24.777  12.987  1.00 58.28  ? 231 LEU A O   1 
ATOM   1684 C  CB  . LEU A 1 232 ? 97.043  24.578  13.296  1.00 64.08  ? 231 LEU A CB  1 
ATOM   1685 C  CG  . LEU A 1 232 ? 95.954  25.123  14.225  1.00 68.74  ? 231 LEU A CG  1 
ATOM   1686 C  CD1 . LEU A 1 232 ? 95.028  24.014  14.708  1.00 71.12  ? 231 LEU A CD1 1 
ATOM   1687 C  CD2 . LEU A 1 232 ? 96.565  25.875  15.399  1.00 67.70  ? 231 LEU A CD2 1 
ATOM   1688 N  N   . PRO A 1 233 ? 99.335  24.558  10.956  1.00 57.04  ? 232 PRO A N   1 
ATOM   1689 C  CA  . PRO A 1 233 ? 100.627 24.129  10.388  1.00 57.90  ? 232 PRO A CA  1 
ATOM   1690 C  C   . PRO A 1 233 ? 101.731 25.159  10.578  1.00 58.92  ? 232 PRO A C   1 
ATOM   1691 O  O   . PRO A 1 233 ? 102.852 24.804  10.966  1.00 59.87  ? 232 PRO A O   1 
ATOM   1692 C  CB  . PRO A 1 233 ? 100.289 23.901  8.911   1.00 51.13  ? 232 PRO A CB  1 
ATOM   1693 C  CG  . PRO A 1 233 ? 98.872  23.484  8.926   1.00 54.58  ? 232 PRO A CG  1 
ATOM   1694 C  CD  . PRO A 1 233 ? 98.215  24.234  10.051  1.00 54.15  ? 232 PRO A CD  1 
ATOM   1695 N  N   . VAL A 1 234 ? 101.440 26.431  10.293  1.00 53.98  ? 233 VAL A N   1 
ATOM   1696 C  CA  . VAL A 1 234 ? 102.372 27.512  10.607  1.00 55.09  ? 233 VAL A CA  1 
ATOM   1697 C  C   . VAL A 1 234 ? 102.728 27.500  12.086  1.00 58.29  ? 233 VAL A C   1 
ATOM   1698 O  O   . VAL A 1 234 ? 103.887 27.713  12.465  1.00 58.54  ? 233 VAL A O   1 
ATOM   1699 C  CB  . VAL A 1 234 ? 101.778 28.869  10.189  1.00 53.96  ? 233 VAL A CB  1 
ATOM   1700 C  CG1 . VAL A 1 234 ? 102.310 29.968  11.082  1.00 52.32  ? 233 VAL A CG1 1 
ATOM   1701 C  CG2 . VAL A 1 234 ? 102.096 29.161  8.733   1.00 51.54  ? 233 VAL A CG2 1 
ATOM   1702 N  N   . ALA A 1 235 ? 101.741 27.233  12.943  1.00 58.56  ? 234 ALA A N   1 
ATOM   1703 C  CA  . ALA A 1 235 ? 101.978 27.255  14.381  1.00 63.47  ? 234 ALA A CA  1 
ATOM   1704 C  C   . ALA A 1 235 ? 102.998 26.201  14.789  1.00 64.88  ? 234 ALA A C   1 
ATOM   1705 O  O   . ALA A 1 235 ? 103.928 26.482  15.554  1.00 60.91  ? 234 ALA A O   1 
ATOM   1706 C  CB  . ALA A 1 235 ? 100.662 27.060  15.134  1.00 57.52  ? 234 ALA A CB  1 
ATOM   1707 N  N   . TYR A 1 236 ? 102.841 24.979  14.287  1.00 61.68  ? 235 TYR A N   1 
ATOM   1708 C  CA  . TYR A 1 236 ? 103.785 23.919  14.608  1.00 61.82  ? 235 TYR A CA  1 
ATOM   1709 C  C   . TYR A 1 236 ? 105.146 24.139  13.958  1.00 64.77  ? 235 TYR A C   1 
ATOM   1710 O  O   . TYR A 1 236 ? 106.147 23.621  14.462  1.00 63.19  ? 235 TYR A O   1 
ATOM   1711 C  CB  . TYR A 1 236 ? 103.205 22.561  14.212  1.00 59.11  ? 235 TYR A CB  1 
ATOM   1712 C  CG  . TYR A 1 236 ? 102.036 22.150  15.080  1.00 67.27  ? 235 TYR A CG  1 
ATOM   1713 C  CD1 . TYR A 1 236 ? 102.240 21.539  16.311  1.00 70.61  ? 235 TYR A CD1 1 
ATOM   1714 C  CD2 . TYR A 1 236 ? 100.728 22.365  14.667  1.00 67.30  ? 235 TYR A CD2 1 
ATOM   1715 C  CE1 . TYR A 1 236 ? 101.175 21.166  17.109  1.00 58.26  ? 235 TYR A CE1 1 
ATOM   1716 C  CE2 . TYR A 1 236 ? 99.657  21.994  15.456  1.00 65.11  ? 235 TYR A CE2 1 
ATOM   1717 C  CZ  . TYR A 1 236 ? 99.886  21.394  16.676  1.00 65.34  ? 235 TYR A CZ  1 
ATOM   1718 O  OH  . TYR A 1 236 ? 98.823  21.020  17.465  1.00 76.73  ? 235 TYR A OH  1 
ATOM   1719 N  N   . ILE A 1 237 ? 105.209 24.894  12.858  1.00 64.05  ? 236 ILE A N   1 
ATOM   1720 C  CA  . ILE A 1 237 ? 106.493 25.141  12.207  1.00 60.89  ? 236 ILE A CA  1 
ATOM   1721 C  C   . ILE A 1 237 ? 107.383 26.009  13.090  1.00 65.80  ? 236 ILE A C   1 
ATOM   1722 O  O   . ILE A 1 237 ? 108.545 25.672  13.346  1.00 76.86  ? 236 ILE A O   1 
ATOM   1723 C  CB  . ILE A 1 237 ? 106.278 25.781  10.823  1.00 65.15  ? 236 ILE A CB  1 
ATOM   1724 C  CG1 . ILE A 1 237 ? 106.107 24.703  9.755   1.00 71.95  ? 236 ILE A CG1 1 
ATOM   1725 C  CG2 . ILE A 1 237 ? 107.448 26.681  10.453  1.00 67.15  ? 236 ILE A CG2 1 
ATOM   1726 C  CD1 . ILE A 1 237 ? 105.877 25.258  8.367   1.00 67.59  ? 236 ILE A CD1 1 
ATOM   1727 N  N   . MET A 1 238 ? 106.857 27.134  13.576  1.00 66.24  ? 237 MET A N   1 
ATOM   1728 C  CA  . MET A 1 238 ? 107.650 27.974  14.464  1.00 69.92  ? 237 MET A CA  1 
ATOM   1729 C  C   . MET A 1 238 ? 107.616 27.501  15.913  1.00 67.09  ? 237 MET A C   1 
ATOM   1730 O  O   . MET A 1 238 ? 108.336 28.061  16.747  1.00 71.73  ? 237 MET A O   1 
ATOM   1731 C  CB  . MET A 1 238 ? 107.219 29.441  14.347  1.00 76.29  ? 237 MET A CB  1 
ATOM   1732 C  CG  . MET A 1 238 ? 105.787 29.726  14.697  1.00 64.28  ? 237 MET A CG  1 
ATOM   1733 S  SD  . MET A 1 238 ? 105.462 31.497  14.835  1.00 74.65  ? 237 MET A SD  1 
ATOM   1734 C  CE  . MET A 1 238 ? 103.910 31.638  13.953  1.00 58.51  ? 237 MET A CE  1 
ATOM   1735 N  N   . MET A 1 239 ? 106.801 26.492  16.231  1.00 66.81  ? 238 MET A N   1 
ATOM   1736 C  CA  . MET A 1 239 ? 107.008 25.739  17.465  1.00 68.54  ? 238 MET A CA  1 
ATOM   1737 C  C   . MET A 1 239 ? 108.288 24.919  17.379  1.00 67.58  ? 238 MET A C   1 
ATOM   1738 O  O   . MET A 1 239 ? 109.079 24.881  18.329  1.00 69.07  ? 238 MET A O   1 
ATOM   1739 C  CB  . MET A 1 239 ? 105.808 24.835  17.740  1.00 63.84  ? 238 MET A CB  1 
ATOM   1740 C  CG  . MET A 1 239 ? 104.900 25.328  18.848  1.00 63.18  ? 238 MET A CG  1 
ATOM   1741 S  SD  . MET A 1 239 ? 103.447 24.282  19.047  1.00 66.44  ? 238 MET A SD  1 
ATOM   1742 C  CE  . MET A 1 239 ? 103.871 23.390  20.541  1.00 71.61  ? 238 MET A CE  1 
ATOM   1743 N  N   . ARG A 1 240 ? 108.501 24.253  16.242  1.00 65.41  ? 239 ARG A N   1 
ATOM   1744 C  CA  . ARG A 1 240 ? 109.761 23.562  15.996  1.00 70.33  ? 239 ARG A CA  1 
ATOM   1745 C  C   . ARG A 1 240 ? 110.923 24.548  15.971  1.00 71.09  ? 239 ARG A C   1 
ATOM   1746 O  O   . ARG A 1 240 ? 112.043 24.199  16.361  1.00 70.98  ? 239 ARG A O   1 
ATOM   1747 C  CB  . ARG A 1 240 ? 109.663 22.754  14.700  1.00 72.71  ? 239 ARG A CB  1 
ATOM   1748 C  CG  . ARG A 1 240 ? 110.981 22.250  14.142  1.00 71.90  ? 239 ARG A CG  1 
ATOM   1749 C  CD  . ARG A 1 240 ? 110.750 21.389  12.906  1.00 71.48  ? 239 ARG A CD  1 
ATOM   1750 N  NE  . ARG A 1 240 ? 110.016 22.081  11.852  1.00 80.52  ? 239 ARG A NE  1 
ATOM   1751 C  CZ  . ARG A 1 240 ? 110.504 23.060  11.102  1.00 82.76  ? 239 ARG A CZ  1 
ATOM   1752 N  NH1 . ARG A 1 240 ? 111.744 23.496  11.252  1.00 86.94  ? 239 ARG A NH1 1 
ATOM   1753 N  NH2 . ARG A 1 240 ? 109.732 23.606  10.166  1.00 83.38  ? 239 ARG A NH2 1 
ATOM   1754 N  N   . LYS A 1 241 ? 110.672 25.780  15.519  1.00 73.70  ? 240 LYS A N   1 
ATOM   1755 C  CA  . LYS A 1 241 ? 111.701 26.816  15.540  1.00 72.83  ? 240 LYS A CA  1 
ATOM   1756 C  C   . LYS A 1 241 ? 112.150 27.100  16.968  1.00 63.95  ? 240 LYS A C   1 
ATOM   1757 O  O   . LYS A 1 241 ? 113.352 27.138  17.257  1.00 67.59  ? 240 LYS A O   1 
ATOM   1758 C  CB  . LYS A 1 241 ? 111.151 28.087  14.888  1.00 76.93  ? 240 LYS A CB  1 
ATOM   1759 C  CG  . LYS A 1 241 ? 112.098 29.270  14.747  1.00 86.85  ? 240 LYS A CG  1 
ATOM   1760 C  CD  . LYS A 1 241 ? 111.493 30.466  14.052  1.00 99.87  ? 240 LYS A CD  1 
ATOM   1761 C  CE  . LYS A 1 241 ? 112.515 31.597  13.987  1.00 102.76 ? 240 LYS A CE  1 
ATOM   1762 N  NZ  . LYS A 1 241 ? 111.965 32.805  13.308  1.00 108.01 ? 240 LYS A NZ  1 
ATOM   1763 N  N   . LEU A 1 242 ? 111.193 27.319  17.873  1.00 70.18  ? 241 LEU A N   1 
ATOM   1764 C  CA  . LEU A 1 242 ? 111.534 27.520  19.278  1.00 69.55  ? 241 LEU A CA  1 
ATOM   1765 C  C   . LEU A 1 242 ? 112.301 26.327  19.838  1.00 72.73  ? 241 LEU A C   1 
ATOM   1766 O  O   . LEU A 1 242 ? 113.243 26.494  20.622  1.00 74.50  ? 241 LEU A O   1 
ATOM   1767 C  CB  . LEU A 1 242 ? 110.266 27.763  20.095  1.00 63.57  ? 241 LEU A CB  1 
ATOM   1768 C  CG  . LEU A 1 242 ? 109.765 29.203  20.193  1.00 66.79  ? 241 LEU A CG  1 
ATOM   1769 C  CD1 . LEU A 1 242 ? 108.247 29.220  20.262  1.00 75.14  ? 241 LEU A CD1 1 
ATOM   1770 C  CD2 . LEU A 1 242 ? 110.371 29.900  21.400  1.00 73.28  ? 241 LEU A CD2 1 
ATOM   1771 N  N   . LEU A 1 243 ? 111.907 25.112  19.446  1.00 69.84  ? 242 LEU A N   1 
ATOM   1772 C  CA  . LEU A 1 243 ? 112.581 23.911  19.929  1.00 68.33  ? 242 LEU A CA  1 
ATOM   1773 C  C   . LEU A 1 243 ? 114.038 23.866  19.485  1.00 72.91  ? 242 LEU A C   1 
ATOM   1774 O  O   . LEU A 1 243 ? 114.941 23.650  20.302  1.00 75.37  ? 242 LEU A O   1 
ATOM   1775 C  CB  . LEU A 1 243 ? 111.835 22.671  19.439  1.00 71.57  ? 242 LEU A CB  1 
ATOM   1776 C  CG  . LEU A 1 243 ? 111.005 21.889  20.458  1.00 71.88  ? 242 LEU A CG  1 
ATOM   1777 C  CD1 . LEU A 1 243 ? 110.829 20.459  19.990  1.00 67.53  ? 242 LEU A CD1 1 
ATOM   1778 C  CD2 . LEU A 1 243 ? 111.654 21.931  21.833  1.00 67.97  ? 242 LEU A CD2 1 
ATOM   1779 N  N   . ALA A 1 244 ? 114.288 24.072  18.190  1.00 74.91  ? 243 ALA A N   1 
ATOM   1780 C  CA  . ALA A 1 244 ? 115.655 23.981  17.690  1.00 72.33  ? 243 ALA A CA  1 
ATOM   1781 C  C   . ALA A 1 244 ? 116.518 25.131  18.191  1.00 75.46  ? 243 ALA A C   1 
ATOM   1782 O  O   . ALA A 1 244 ? 117.743 24.989  18.283  1.00 76.05  ? 243 ALA A O   1 
ATOM   1783 C  CB  . ALA A 1 244 ? 115.655 23.948  16.163  1.00 66.98  ? 243 ALA A CB  1 
ATOM   1784 N  N   . ALA A 1 245 ? 115.901 26.270  18.515  1.00 75.88  ? 244 ALA A N   1 
ATOM   1785 C  CA  . ALA A 1 245 ? 116.666 27.445  18.920  1.00 76.53  ? 244 ALA A CA  1 
ATOM   1786 C  C   . ALA A 1 245 ? 117.420 27.213  20.223  1.00 79.82  ? 244 ALA A C   1 
ATOM   1787 O  O   . ALA A 1 245 ? 118.484 27.806  20.437  1.00 78.57  ? 244 ALA A O   1 
ATOM   1788 C  CB  . ALA A 1 245 ? 115.740 28.654  19.053  1.00 69.21  ? 244 ALA A CB  1 
ATOM   1789 N  N   . GLN A 1 246 ? 116.894 26.360  21.103  1.00 79.37  ? 245 GLN A N   1 
ATOM   1790 C  CA  . GLN A 1 246 ? 117.502 26.141  22.405  1.00 80.21  ? 245 GLN A CA  1 
ATOM   1791 C  C   . GLN A 1 246 ? 117.803 24.680  22.705  1.00 83.78  ? 245 GLN A C   1 
ATOM   1792 O  O   . GLN A 1 246 ? 118.317 24.384  23.789  1.00 86.31  ? 245 GLN A O   1 
ATOM   1793 C  CB  . GLN A 1 246 ? 116.593 26.701  23.510  1.00 75.46  ? 245 GLN A CB  1 
ATOM   1794 C  CG  . GLN A 1 246 ? 116.533 28.215  23.555  1.00 82.72  ? 245 GLN A CG  1 
ATOM   1795 C  CD  . GLN A 1 246 ? 116.053 28.740  24.891  1.00 94.95  ? 245 GLN A CD  1 
ATOM   1796 O  OE1 . GLN A 1 246 ? 116.207 28.086  25.924  1.00 93.23  ? 245 GLN A OE1 1 
ATOM   1797 N  NE2 . GLN A 1 246 ? 115.455 29.925  24.877  1.00 90.08  ? 245 GLN A NE2 1 
ATOM   1798 N  N   . TYR A 1 247 ? 117.499 23.763  21.791  1.00 80.41  ? 246 TYR A N   1 
ATOM   1799 C  CA  . TYR A 1 247 ? 117.694 22.342  22.032  1.00 77.01  ? 246 TYR A CA  1 
ATOM   1800 C  C   . TYR A 1 247 ? 118.226 21.690  20.764  1.00 80.03  ? 246 TYR A C   1 
ATOM   1801 O  O   . TYR A 1 247 ? 118.333 22.320  19.709  1.00 83.58  ? 246 TYR A O   1 
ATOM   1802 C  CB  . TYR A 1 247 ? 116.397 21.668  22.501  1.00 78.00  ? 246 TYR A CB  1 
ATOM   1803 C  CG  . TYR A 1 247 ? 115.924 22.145  23.857  1.00 69.77  ? 246 TYR A CG  1 
ATOM   1804 C  CD1 . TYR A 1 247 ? 115.102 23.259  23.977  1.00 68.92  ? 246 TYR A CD1 1 
ATOM   1805 C  CD2 . TYR A 1 247 ? 116.307 21.487  25.018  1.00 76.49  ? 246 TYR A CD2 1 
ATOM   1806 C  CE1 . TYR A 1 247 ? 114.672 23.701  25.215  1.00 72.91  ? 246 TYR A CE1 1 
ATOM   1807 C  CE2 . TYR A 1 247 ? 115.881 21.921  26.260  1.00 71.88  ? 246 TYR A CE2 1 
ATOM   1808 C  CZ  . TYR A 1 247 ? 115.064 23.027  26.352  1.00 65.83  ? 246 TYR A CZ  1 
ATOM   1809 O  OH  . TYR A 1 247 ? 114.640 23.462  27.587  1.00 58.49  ? 246 TYR A OH  1 
ATOM   1810 N  N   . SER A 1 248 ? 118.564 20.411  20.883  1.00 86.18  ? 247 SER A N   1 
ATOM   1811 C  CA  . SER A 1 248 ? 119.135 19.655  19.782  1.00 93.96  ? 247 SER A CA  1 
ATOM   1812 C  C   . SER A 1 248 ? 118.043 19.208  18.811  1.00 95.63  ? 247 SER A C   1 
ATOM   1813 O  O   . SER A 1 248 ? 116.845 19.286  19.096  1.00 94.64  ? 247 SER A O   1 
ATOM   1814 C  CB  . SER A 1 248 ? 119.910 18.448  20.311  1.00 98.82  ? 247 SER A CB  1 
ATOM   1815 O  OG  . SER A 1 248 ? 119.044 17.524  20.948  1.00 96.07  ? 247 SER A OG  1 
ATOM   1816 N  N   . TRP A 1 249 ? 118.475 18.737  17.640  1.00 96.05  ? 248 TRP A N   1 
ATOM   1817 C  CA  . TRP A 1 249 ? 117.539 18.145  16.693  1.00 100.91 ? 248 TRP A CA  1 
ATOM   1818 C  C   . TRP A 1 249 ? 116.945 16.850  17.226  1.00 95.00  ? 248 TRP A C   1 
ATOM   1819 O  O   . TRP A 1 249 ? 115.852 16.461  16.802  1.00 87.31  ? 248 TRP A O   1 
ATOM   1820 C  CB  . TRP A 1 249 ? 118.230 17.897  15.350  1.00 107.18 ? 248 TRP A CB  1 
ATOM   1821 C  CG  . TRP A 1 249 ? 118.645 19.151  14.636  1.00 111.34 ? 248 TRP A CG  1 
ATOM   1822 C  CD1 . TRP A 1 249 ? 119.912 19.515  14.288  1.00 117.24 ? 248 TRP A CD1 1 
ATOM   1823 C  CD2 . TRP A 1 249 ? 117.782 20.189  14.151  1.00 117.50 ? 248 TRP A CD2 1 
ATOM   1824 N  NE1 . TRP A 1 249 ? 119.896 20.724  13.635  1.00 118.52 ? 248 TRP A NE1 1 
ATOM   1825 C  CE2 . TRP A 1 249 ? 118.600 21.158  13.536  1.00 116.08 ? 248 TRP A CE2 1 
ATOM   1826 C  CE3 . TRP A 1 249 ? 116.399 20.397  14.185  1.00 112.70 ? 248 TRP A CE3 1 
ATOM   1827 C  CZ2 . TRP A 1 249 ? 118.082 22.316  12.960  1.00 112.05 ? 248 TRP A CZ2 1 
ATOM   1828 C  CZ3 . TRP A 1 249 ? 115.887 21.546  13.611  1.00 106.68 ? 248 TRP A CZ3 1 
ATOM   1829 C  CH2 . TRP A 1 249 ? 116.726 22.491  13.008  1.00 110.40 ? 248 TRP A CH2 1 
ATOM   1830 N  N   . ASP A 1 250 ? 117.645 16.178  18.142  1.00 91.95  ? 249 ASP A N   1 
ATOM   1831 C  CA  . ASP A 1 250 ? 117.105 14.971  18.758  1.00 95.20  ? 249 ASP A CA  1 
ATOM   1832 C  C   . ASP A 1 250 ? 115.824 15.279  19.524  1.00 87.32  ? 249 ASP A C   1 
ATOM   1833 O  O   . ASP A 1 250 ? 114.805 14.602  19.347  1.00 86.62  ? 249 ASP A O   1 
ATOM   1834 C  CB  . ASP A 1 250 ? 118.150 14.344  19.682  1.00 101.61 ? 249 ASP A CB  1 
ATOM   1835 C  CG  . ASP A 1 250 ? 118.842 13.153  19.052  1.00 103.85 ? 249 ASP A CG  1 
ATOM   1836 O  OD1 . ASP A 1 250 ? 118.634 12.914  17.845  1.00 100.69 ? 249 ASP A OD1 1 
ATOM   1837 O  OD2 . ASP A 1 250 ? 119.594 12.455  19.766  1.00 106.07 ? 249 ASP A OD2 1 
ATOM   1838 N  N   . GLU A 1 251 ? 115.852 16.316  20.366  1.00 86.68  ? 250 GLU A N   1 
ATOM   1839 C  CA  . GLU A 1 251 ? 114.647 16.725  21.084  1.00 83.12  ? 250 GLU A CA  1 
ATOM   1840 C  C   . GLU A 1 251 ? 113.550 17.159  20.120  1.00 77.98  ? 250 GLU A C   1 
ATOM   1841 O  O   . GLU A 1 251 ? 112.362 16.939  20.381  1.00 73.67  ? 250 GLU A O   1 
ATOM   1842 C  CB  . GLU A 1 251 ? 114.975 17.847  22.068  1.00 78.99  ? 250 GLU A CB  1 
ATOM   1843 C  CG  . GLU A 1 251 ? 113.894 18.078  23.111  1.00 66.03  ? 250 GLU A CG  1 
ATOM   1844 C  CD  . GLU A 1 251 ? 114.448 18.199  24.515  1.00 65.38  ? 250 GLU A CD  1 
ATOM   1845 O  OE1 . GLU A 1 251 ? 115.629 17.851  24.723  1.00 79.85  ? 250 GLU A OE1 1 
ATOM   1846 O  OE2 . GLU A 1 251 ? 113.699 18.638  25.412  1.00 64.17  ? 250 GLU A OE2 1 
ATOM   1847 N  N   . VAL A 1 252 ? 113.929 17.792  19.008  1.00 80.45  ? 251 VAL A N   1 
ATOM   1848 C  CA  . VAL A 1 252 ? 112.948 18.158  17.990  1.00 80.75  ? 251 VAL A CA  1 
ATOM   1849 C  C   . VAL A 1 252 ? 112.280 16.904  17.441  1.00 80.92  ? 251 VAL A C   1 
ATOM   1850 O  O   . VAL A 1 252 ? 111.056 16.855  17.267  1.00 77.76  ? 251 VAL A O   1 
ATOM   1851 C  CB  . VAL A 1 252 ? 113.616 18.983  16.873  1.00 87.48  ? 251 VAL A CB  1 
ATOM   1852 C  CG1 . VAL A 1 252 ? 112.810 18.896  15.583  1.00 88.40  ? 251 VAL A CG1 1 
ATOM   1853 C  CG2 . VAL A 1 252 ? 113.792 20.429  17.309  1.00 84.11  ? 251 VAL A CG2 1 
ATOM   1854 N  N   . GLY A 1 253 ? 113.076 15.867  17.176  1.00 81.31  ? 252 GLY A N   1 
ATOM   1855 C  CA  . GLY A 1 253 ? 112.519 14.613  16.698  1.00 72.08  ? 252 GLY A CA  1 
ATOM   1856 C  C   . GLY A 1 253 ? 111.603 13.959  17.714  1.00 74.99  ? 252 GLY A C   1 
ATOM   1857 O  O   . GLY A 1 253 ? 110.603 13.337  17.349  1.00 85.23  ? 252 GLY A O   1 
ATOM   1858 N  N   . ILE A 1 254 ? 111.946 14.068  19.002  1.00 77.31  ? 253 ILE A N   1 
ATOM   1859 C  CA  . ILE A 1 254 ? 111.090 13.512  20.048  1.00 80.95  ? 253 ILE A CA  1 
ATOM   1860 C  C   . ILE A 1 254 ? 109.698 14.131  19.968  1.00 79.78  ? 253 ILE A C   1 
ATOM   1861 O  O   . ILE A 1 254 ? 108.680 13.429  20.009  1.00 76.45  ? 253 ILE A O   1 
ATOM   1862 C  CB  . ILE A 1 254 ? 111.722 13.741  21.438  1.00 83.75  ? 253 ILE A CB  1 
ATOM   1863 C  CG1 . ILE A 1 254 ? 112.537 12.532  21.901  1.00 87.39  ? 253 ILE A CG1 1 
ATOM   1864 C  CG2 . ILE A 1 254 ? 110.664 14.063  22.483  1.00 89.03  ? 253 ILE A CG2 1 
ATOM   1865 C  CD1 . ILE A 1 254 ? 113.775 12.287  21.095  1.00 94.10  ? 253 ILE A CD1 1 
ATOM   1866 N  N   . TRP A 1 255 ? 109.638 15.458  19.832  1.00 78.74  ? 254 TRP A N   1 
ATOM   1867 C  CA  . TRP A 1 255 ? 108.357 16.157  19.787  1.00 75.66  ? 254 TRP A CA  1 
ATOM   1868 C  C   . TRP A 1 255 ? 107.610 15.873  18.489  1.00 72.60  ? 254 TRP A C   1 
ATOM   1869 O  O   . TRP A 1 255 ? 106.402 15.611  18.506  1.00 70.76  ? 254 TRP A O   1 
ATOM   1870 C  CB  . TRP A 1 255 ? 108.579 17.657  19.974  1.00 74.66  ? 254 TRP A CB  1 
ATOM   1871 C  CG  . TRP A 1 255 ? 107.506 18.520  19.389  1.00 72.48  ? 254 TRP A CG  1 
ATOM   1872 C  CD1 . TRP A 1 255 ? 107.624 19.373  18.331  1.00 71.66  ? 254 TRP A CD1 1 
ATOM   1873 C  CD2 . TRP A 1 255 ? 106.151 18.624  19.840  1.00 66.97  ? 254 TRP A CD2 1 
ATOM   1874 N  NE1 . TRP A 1 255 ? 106.425 19.998  18.092  1.00 72.70  ? 254 TRP A NE1 1 
ATOM   1875 C  CE2 . TRP A 1 255 ? 105.504 19.556  19.004  1.00 68.17  ? 254 TRP A CE2 1 
ATOM   1876 C  CE3 . TRP A 1 255 ? 105.420 18.017  20.866  1.00 68.95  ? 254 TRP A CE3 1 
ATOM   1877 C  CZ2 . TRP A 1 255 ? 104.162 19.895  19.163  1.00 69.55  ? 254 TRP A CZ2 1 
ATOM   1878 C  CZ3 . TRP A 1 255 ? 104.088 18.356  21.023  1.00 72.97  ? 254 TRP A CZ3 1 
ATOM   1879 C  CH2 . TRP A 1 255 ? 103.473 19.286  20.176  1.00 71.35  ? 254 TRP A CH2 1 
ATOM   1880 N  N   . GLN A 1 256 ? 108.314 15.922  17.356  1.00 71.48  ? 255 GLN A N   1 
ATOM   1881 C  CA  . GLN A 1 256 ? 107.683 15.656  16.068  1.00 72.43  ? 255 GLN A CA  1 
ATOM   1882 C  C   . GLN A 1 256 ? 107.091 14.252  16.013  1.00 74.98  ? 255 GLN A C   1 
ATOM   1883 O  O   . GLN A 1 256 ? 106.004 14.052  15.457  1.00 75.53  ? 255 GLN A O   1 
ATOM   1884 C  CB  . GLN A 1 256 ? 108.699 15.853  14.943  1.00 75.80  ? 255 GLN A CB  1 
ATOM   1885 C  CG  . GLN A 1 256 ? 109.121 17.299  14.731  1.00 81.79  ? 255 GLN A CG  1 
ATOM   1886 C  CD  . GLN A 1 256 ? 109.231 17.667  13.264  1.00 87.29  ? 255 GLN A CD  1 
ATOM   1887 O  OE1 . GLN A 1 256 ? 110.331 17.808  12.730  1.00 83.73  ? 255 GLN A OE1 1 
ATOM   1888 N  NE2 . GLN A 1 256 ? 108.089 17.825  12.605  1.00 90.63  ? 255 GLN A NE2 1 
ATOM   1889 N  N   . GLY A 1 257 ? 107.793 13.265  16.572  1.00 78.25  ? 256 GLY A N   1 
ATOM   1890 C  CA  . GLY A 1 257 ? 107.229 11.927  16.644  1.00 77.18  ? 256 GLY A CA  1 
ATOM   1891 C  C   . GLY A 1 257 ? 105.946 11.861  17.452  1.00 74.40  ? 256 GLY A C   1 
ATOM   1892 O  O   . GLY A 1 257 ? 104.977 11.222  17.037  1.00 72.98  ? 256 GLY A O   1 
ATOM   1893 N  N   . VAL A 1 258 ? 105.924 12.511  18.619  1.00 73.42  ? 257 VAL A N   1 
ATOM   1894 C  CA  . VAL A 1 258 ? 104.711 12.545  19.437  1.00 71.94  ? 257 VAL A CA  1 
ATOM   1895 C  C   . VAL A 1 258 ? 103.569 13.211  18.680  1.00 74.57  ? 257 VAL A C   1 
ATOM   1896 O  O   . VAL A 1 258 ? 102.450 12.688  18.624  1.00 69.34  ? 257 VAL A O   1 
ATOM   1897 C  CB  . VAL A 1 258 ? 104.978 13.253  20.777  1.00 76.44  ? 257 VAL A CB  1 
ATOM   1898 C  CG1 . VAL A 1 258 ? 103.678 13.430  21.548  1.00 75.11  ? 257 VAL A CG1 1 
ATOM   1899 C  CG2 . VAL A 1 258 ? 105.956 12.463  21.594  1.00 75.41  ? 257 VAL A CG2 1 
ATOM   1900 N  N   . SER A 1 259 ? 103.835 14.379  18.091  1.00 74.08  ? 258 SER A N   1 
ATOM   1901 C  CA  . SER A 1 259 ? 102.776 15.135  17.429  1.00 69.10  ? 258 SER A CA  1 
ATOM   1902 C  C   . SER A 1 259 ? 102.195 14.359  16.255  1.00 74.77  ? 258 SER A C   1 
ATOM   1903 O  O   . SER A 1 259 ? 100.972 14.279  16.094  1.00 73.72  ? 258 SER A O   1 
ATOM   1904 C  CB  . SER A 1 259 ? 103.313 16.489  16.967  1.00 71.98  ? 258 SER A CB  1 
ATOM   1905 O  OG  . SER A 1 259 ? 104.234 17.016  17.903  1.00 81.66  ? 258 SER A OG  1 
ATOM   1906 N  N   . SER A 1 260 ? 103.060 13.780  15.420  1.00 75.20  ? 259 SER A N   1 
ATOM   1907 C  CA  . SER A 1 260 ? 102.576 13.087  14.231  1.00 75.00  ? 259 SER A CA  1 
ATOM   1908 C  C   . SER A 1 260 ? 101.767 11.847  14.598  1.00 72.87  ? 259 SER A C   1 
ATOM   1909 O  O   . SER A 1 260 ? 100.741 11.562  13.969  1.00 77.24  ? 259 SER A O   1 
ATOM   1910 C  CB  . SER A 1 260 ? 103.752 12.722  13.323  1.00 71.72  ? 259 SER A CB  1 
ATOM   1911 O  OG  . SER A 1 260 ? 104.136 11.369  13.493  1.00 75.21  ? 259 SER A OG  1 
ATOM   1912 N  N   . ILE A 1 261 ? 102.208 11.097  15.612  1.00 69.78  ? 260 ILE A N   1 
ATOM   1913 C  CA  . ILE A 1 261 ? 101.444 9.927   16.040  1.00 69.19  ? 260 ILE A CA  1 
ATOM   1914 C  C   . ILE A 1 261 ? 100.184 10.342  16.793  1.00 71.05  ? 260 ILE A C   1 
ATOM   1915 O  O   . ILE A 1 261 ? 99.168  9.636   16.753  1.00 70.43  ? 260 ILE A O   1 
ATOM   1916 C  CB  . ILE A 1 261 ? 102.327 8.978   16.874  1.00 78.09  ? 260 ILE A CB  1 
ATOM   1917 C  CG1 . ILE A 1 261 ? 101.644 7.622   17.033  1.00 77.45  ? 260 ILE A CG1 1 
ATOM   1918 C  CG2 . ILE A 1 261 ? 102.618 9.555   18.247  1.00 76.83  ? 260 ILE A CG2 1 
ATOM   1919 C  CD1 . ILE A 1 261 ? 102.598 6.468   16.938  1.00 76.32  ? 260 ILE A CD1 1 
ATOM   1920 N  N   . SER A 1 262 ? 100.221 11.481  17.491  1.00 72.32  ? 261 SER A N   1 
ATOM   1921 C  CA  . SER A 1 262 ? 99.030  11.970  18.179  1.00 68.30  ? 261 SER A CA  1 
ATOM   1922 C  C   . SER A 1 262 ? 97.990  12.471  17.186  1.00 69.74  ? 261 SER A C   1 
ATOM   1923 O  O   . SER A 1 262 ? 96.785  12.293  17.395  1.00 61.14  ? 261 SER A O   1 
ATOM   1924 C  CB  . SER A 1 262 ? 99.405  13.072  19.168  1.00 67.09  ? 261 SER A CB  1 
ATOM   1925 O  OG  . SER A 1 262 ? 98.275  13.848  19.523  1.00 68.05  ? 261 SER A OG  1 
ATOM   1926 N  N   . ASP A 1 263 ? 98.441  13.107  16.101  1.00 69.66  ? 262 ASP A N   1 
ATOM   1927 C  CA  . ASP A 1 263 ? 97.521  13.535  15.053  1.00 67.76  ? 262 ASP A CA  1 
ATOM   1928 C  C   . ASP A 1 263 ? 96.848  12.338  14.392  1.00 66.92  ? 262 ASP A C   1 
ATOM   1929 O  O   . ASP A 1 263 ? 95.641  12.365  14.125  1.00 56.98  ? 262 ASP A O   1 
ATOM   1930 C  CB  . ASP A 1 263 ? 98.264  14.378  14.018  1.00 67.92  ? 262 ASP A CB  1 
ATOM   1931 C  CG  . ASP A 1 263 ? 98.712  15.717  14.571  1.00 84.50  ? 262 ASP A CG  1 
ATOM   1932 O  OD1 . ASP A 1 263 ? 98.108  16.186  15.559  1.00 96.55  ? 262 ASP A OD1 1 
ATOM   1933 O  OD2 . ASP A 1 263 ? 99.671  16.298  14.021  1.00 97.81  ? 262 ASP A OD2 1 
ATOM   1934 N  N   . ALA A 1 264 ? 97.615  11.280  14.114  1.00 63.74  ? 263 ALA A N   1 
ATOM   1935 C  CA  . ALA A 1 264 ? 97.024  10.063  13.567  1.00 60.48  ? 263 ALA A CA  1 
ATOM   1936 C  C   . ALA A 1 264 ? 96.036  9.448   14.550  1.00 58.17  ? 263 ALA A C   1 
ATOM   1937 O  O   . ALA A 1 264 ? 95.002  8.902   14.146  1.00 59.23  ? 263 ALA A O   1 
ATOM   1938 C  CB  . ALA A 1 264 ? 98.121  9.061   13.208  1.00 57.48  ? 263 ALA A CB  1 
ATOM   1939 N  N   . TYR A 1 265 ? 96.346  9.520   15.846  1.00 57.35  ? 264 TYR A N   1 
ATOM   1940 C  CA  . TYR A 1 265 ? 95.413  9.052   16.865  1.00 61.44  ? 264 TYR A CA  1 
ATOM   1941 C  C   . TYR A 1 265 ? 94.127  9.869   16.839  1.00 58.34  ? 264 TYR A C   1 
ATOM   1942 O  O   . TYR A 1 265 ? 93.027  9.318   16.963  1.00 50.61  ? 264 TYR A O   1 
ATOM   1943 C  CB  . TYR A 1 265 ? 96.084  9.126   18.238  1.00 63.95  ? 264 TYR A CB  1 
ATOM   1944 C  CG  . TYR A 1 265 ? 95.212  8.741   19.411  1.00 61.21  ? 264 TYR A CG  1 
ATOM   1945 C  CD1 . TYR A 1 265 ? 94.690  7.460   19.527  1.00 60.25  ? 264 TYR A CD1 1 
ATOM   1946 C  CD2 . TYR A 1 265 ? 94.933  9.656   20.419  1.00 59.16  ? 264 TYR A CD2 1 
ATOM   1947 C  CE1 . TYR A 1 265 ? 93.903  7.104   20.607  1.00 57.55  ? 264 TYR A CE1 1 
ATOM   1948 C  CE2 . TYR A 1 265 ? 94.148  9.310   21.502  1.00 58.11  ? 264 TYR A CE2 1 
ATOM   1949 C  CZ  . TYR A 1 265 ? 93.636  8.034   21.591  1.00 57.74  ? 264 TYR A CZ  1 
ATOM   1950 O  OH  . TYR A 1 265 ? 92.852  7.686   22.667  1.00 60.22  ? 264 TYR A OH  1 
ATOM   1951 N  N   . LEU A 1 266 ? 94.250  11.189  16.681  1.00 64.11  ? 265 LEU A N   1 
ATOM   1952 C  CA  . LEU A 1 266 ? 93.077  12.055  16.616  1.00 59.81  ? 265 LEU A CA  1 
ATOM   1953 C  C   . LEU A 1 266 ? 92.232  11.759  15.383  1.00 60.77  ? 265 LEU A C   1 
ATOM   1954 O  O   . LEU A 1 266 ? 90.999  11.705  15.463  1.00 56.90  ? 265 LEU A O   1 
ATOM   1955 C  CB  . LEU A 1 266 ? 93.519  13.518  16.613  1.00 61.97  ? 265 LEU A CB  1 
ATOM   1956 C  CG  . LEU A 1 266 ? 93.735  14.208  17.958  1.00 63.44  ? 265 LEU A CG  1 
ATOM   1957 C  CD1 . LEU A 1 266 ? 94.068  15.670  17.737  1.00 67.34  ? 265 LEU A CD1 1 
ATOM   1958 C  CD2 . LEU A 1 266 ? 92.505  14.066  18.832  1.00 58.69  ? 265 LEU A CD2 1 
ATOM   1959 N  N   . GLN A 1 267 ? 92.880  11.571  14.230  1.00 61.67  ? 266 GLN A N   1 
ATOM   1960 C  CA  . GLN A 1 267 ? 92.151  11.283  12.998  1.00 58.06  ? 266 GLN A CA  1 
ATOM   1961 C  C   . GLN A 1 267 ? 91.384  9.969   13.095  1.00 55.85  ? 266 GLN A C   1 
ATOM   1962 O  O   . GLN A 1 267 ? 90.270  9.853   12.572  1.00 62.69  ? 266 GLN A O   1 
ATOM   1963 C  CB  . GLN A 1 267 ? 93.118  11.258  11.814  1.00 60.43  ? 266 GLN A CB  1 
ATOM   1964 C  CG  . GLN A 1 267 ? 93.730  12.614  11.493  1.00 65.73  ? 266 GLN A CG  1 
ATOM   1965 C  CD  . GLN A 1 267 ? 94.739  12.547  10.363  1.00 83.20  ? 266 GLN A CD  1 
ATOM   1966 O  OE1 . GLN A 1 267 ? 95.335  11.500  10.107  1.00 82.68  ? 266 GLN A OE1 1 
ATOM   1967 N  NE2 . GLN A 1 267 ? 94.933  13.667  9.677   1.00 96.25  ? 266 GLN A NE2 1 
ATOM   1968 N  N   . PHE A 1 268 ? 91.966  8.967   13.756  1.00 54.27  ? 267 PHE A N   1 
ATOM   1969 C  CA  . PHE A 1 268 ? 91.268  7.697   13.934  1.00 56.29  ? 267 PHE A CA  1 
ATOM   1970 C  C   . PHE A 1 268 ? 90.070  7.853   14.862  1.00 54.36  ? 267 PHE A C   1 
ATOM   1971 O  O   . PHE A 1 268 ? 89.005  7.272   14.617  1.00 50.25  ? 267 PHE A O   1 
ATOM   1972 C  CB  . PHE A 1 268 ? 92.238  6.643   14.473  1.00 54.31  ? 267 PHE A CB  1 
ATOM   1973 C  CG  . PHE A 1 268 ? 91.577  5.552   15.273  1.00 59.44  ? 267 PHE A CG  1 
ATOM   1974 C  CD1 . PHE A 1 268 ? 90.818  4.575   14.650  1.00 57.82  ? 267 PHE A CD1 1 
ATOM   1975 C  CD2 . PHE A 1 268 ? 91.727  5.498   16.649  1.00 69.57  ? 267 PHE A CD2 1 
ATOM   1976 C  CE1 . PHE A 1 268 ? 90.213  3.572   15.383  1.00 58.86  ? 267 PHE A CE1 1 
ATOM   1977 C  CE2 . PHE A 1 268 ? 91.125  4.497   17.388  1.00 66.20  ? 267 PHE A CE2 1 
ATOM   1978 C  CZ  . PHE A 1 268 ? 90.367  3.533   16.754  1.00 62.34  ? 267 PHE A CZ  1 
ATOM   1979 N  N   . ILE A 1 269 ? 90.222  8.643   15.923  1.00 55.92  ? 268 ILE A N   1 
ATOM   1980 C  CA  . ILE A 1 269 ? 89.205  8.713   16.964  1.00 55.98  ? 268 ILE A CA  1 
ATOM   1981 C  C   . ILE A 1 269 ? 87.999  9.532   16.514  1.00 55.57  ? 268 ILE A C   1 
ATOM   1982 O  O   . ILE A 1 269 ? 86.853  9.196   16.835  1.00 57.43  ? 268 ILE A O   1 
ATOM   1983 C  CB  . ILE A 1 269 ? 89.833  9.276   18.252  1.00 58.60  ? 268 ILE A CB  1 
ATOM   1984 C  CG1 . ILE A 1 269 ? 90.742  8.229   18.907  1.00 59.08  ? 268 ILE A CG1 1 
ATOM   1985 C  CG2 . ILE A 1 269 ? 88.767  9.772   19.203  1.00 60.97  ? 268 ILE A CG2 1 
ATOM   1986 C  CD1 . ILE A 1 269 ? 90.052  7.368   19.945  1.00 61.24  ? 268 ILE A CD1 1 
ATOM   1987 N  N   . THR A 1 270 ? 88.222  10.594  15.741  1.00 54.24  ? 269 THR A N   1 
ATOM   1988 C  CA  . THR A 1 270 ? 87.147  11.486  15.324  1.00 50.32  ? 269 THR A CA  1 
ATOM   1989 C  C   . THR A 1 270 ? 86.706  11.255  13.884  1.00 49.70  ? 269 THR A C   1 
ATOM   1990 O  O   . THR A 1 270 ? 86.009  12.103  13.318  1.00 43.01  ? 269 THR A O   1 
ATOM   1991 C  CB  . THR A 1 270 ? 87.576  12.943  15.509  1.00 54.28  ? 269 THR A CB  1 
ATOM   1992 O  OG1 . THR A 1 270 ? 88.595  13.269  14.556  1.00 56.31  ? 269 THR A OG1 1 
ATOM   1993 C  CG2 . THR A 1 270 ? 88.123  13.154  16.911  1.00 54.94  ? 269 THR A CG2 1 
ATOM   1994 N  N   . ALA A 1 271 ? 87.103  10.135  13.279  1.00 47.40  ? 270 ALA A N   1 
ATOM   1995 C  CA  . ALA A 1 271 ? 86.779  9.887   11.877  1.00 41.63  ? 270 ALA A CA  1 
ATOM   1996 C  C   . ALA A 1 271 ? 85.275  9.775   11.646  1.00 44.58  ? 270 ALA A C   1 
ATOM   1997 O  O   . ALA A 1 271 ? 84.791  10.100  10.555  1.00 43.46  ? 270 ALA A O   1 
ATOM   1998 C  CB  . ALA A 1 271 ? 87.495  8.628   11.392  1.00 44.59  ? 270 ALA A CB  1 
ATOM   1999 N  N   . SER A 1 272 ? 84.521  9.314   12.646  1.00 44.70  ? 271 SER A N   1 
ATOM   2000 C  CA  . SER A 1 272 ? 83.070  9.219   12.531  1.00 43.04  ? 271 SER A CA  1 
ATOM   2001 C  C   . SER A 1 272 ? 82.354  10.552  12.720  1.00 40.98  ? 271 SER A C   1 
ATOM   2002 O  O   . SER A 1 272 ? 81.131  10.603  12.553  1.00 43.78  ? 271 SER A O   1 
ATOM   2003 C  CB  . SER A 1 272 ? 82.526  8.209   13.544  1.00 41.46  ? 271 SER A CB  1 
ATOM   2004 O  OG  . SER A 1 272 ? 82.452  8.777   14.840  1.00 45.56  ? 271 SER A OG  1 
ATOM   2005 N  N   . PHE A 1 273 ? 83.073  11.622  13.065  1.00 38.32  ? 272 PHE A N   1 
ATOM   2006 C  CA  . PHE A 1 273 ? 82.431  12.924  13.219  1.00 42.53  ? 272 PHE A CA  1 
ATOM   2007 C  C   . PHE A 1 273 ? 81.852  13.411  11.896  1.00 41.18  ? 272 PHE A C   1 
ATOM   2008 O  O   . PHE A 1 273 ? 80.700  13.853  11.832  1.00 43.15  ? 272 PHE A O   1 
ATOM   2009 C  CB  . PHE A 1 273 ? 83.418  13.942  13.793  1.00 42.76  ? 272 PHE A CB  1 
ATOM   2010 C  CG  . PHE A 1 273 ? 83.615  13.829  15.282  1.00 48.22  ? 272 PHE A CG  1 
ATOM   2011 C  CD1 . PHE A 1 273 ? 83.562  12.598  15.920  1.00 46.34  ? 272 PHE A CD1 1 
ATOM   2012 C  CD2 . PHE A 1 273 ? 83.846  14.961  16.046  1.00 48.46  ? 272 PHE A CD2 1 
ATOM   2013 C  CE1 . PHE A 1 273 ? 83.741  12.500  17.288  1.00 43.82  ? 272 PHE A CE1 1 
ATOM   2014 C  CE2 . PHE A 1 273 ? 84.025  14.870  17.414  1.00 45.18  ? 272 PHE A CE2 1 
ATOM   2015 C  CZ  . PHE A 1 273 ? 83.973  13.638  18.035  1.00 47.09  ? 272 PHE A CZ  1 
ATOM   2016 N  N   . SER A 1 274 ? 82.638  13.333  10.821  1.00 43.03  ? 273 SER A N   1 
ATOM   2017 C  CA  . SER A 1 274 ? 82.139  13.746  9.516   1.00 45.49  ? 273 SER A CA  1 
ATOM   2018 C  C   . SER A 1 274 ? 81.123  12.759  8.957   1.00 47.12  ? 273 SER A C   1 
ATOM   2019 O  O   . SER A 1 274 ? 80.346  13.123  8.068   1.00 48.61  ? 273 SER A O   1 
ATOM   2020 C  CB  . SER A 1 274 ? 83.299  13.911  8.534   1.00 40.37  ? 273 SER A CB  1 
ATOM   2021 O  OG  . SER A 1 274 ? 83.810  12.650  8.138   1.00 46.68  ? 273 SER A OG  1 
ATOM   2022 N  N   . VAL A 1 275 ? 81.113  11.525  9.459   1.00 41.79  ? 274 VAL A N   1 
ATOM   2023 C  CA  . VAL A 1 275 ? 80.187  10.518  8.955   1.00 39.70  ? 274 VAL A CA  1 
ATOM   2024 C  C   . VAL A 1 275 ? 78.807  10.687  9.583   1.00 43.77  ? 274 VAL A C   1 
ATOM   2025 O  O   . VAL A 1 275 ? 77.784  10.551  8.902   1.00 43.67  ? 274 VAL A O   1 
ATOM   2026 C  CB  . VAL A 1 275 ? 80.766  9.112   9.203   1.00 44.39  ? 274 VAL A CB  1 
ATOM   2027 C  CG1 . VAL A 1 275 ? 79.697  8.048   9.032   1.00 46.13  ? 274 VAL A CG1 1 
ATOM   2028 C  CG2 . VAL A 1 275 ? 81.942  8.852   8.272   1.00 45.43  ? 274 VAL A CG2 1 
ATOM   2029 N  N   . TYR A 1 276 ? 78.750  10.999  10.878  1.00 41.56  ? 275 TYR A N   1 
ATOM   2030 C  CA  . TYR A 1 276 ? 77.483  11.160  11.583  1.00 43.68  ? 275 TYR A CA  1 
ATOM   2031 C  C   . TYR A 1 276 ? 77.254  12.577  12.084  1.00 44.73  ? 275 TYR A C   1 
ATOM   2032 O  O   . TYR A 1 276 ? 76.186  13.149  11.836  1.00 43.36  ? 275 TYR A O   1 
ATOM   2033 C  CB  . TYR A 1 276 ? 77.389  10.182  12.765  1.00 38.28  ? 275 TYR A CB  1 
ATOM   2034 C  CG  . TYR A 1 276 ? 76.189  10.450  13.648  1.00 43.33  ? 275 TYR A CG  1 
ATOM   2035 C  CD1 . TYR A 1 276 ? 74.940  9.941   13.322  1.00 43.74  ? 275 TYR A CD1 1 
ATOM   2036 C  CD2 . TYR A 1 276 ? 76.303  11.220  14.800  1.00 44.43  ? 275 TYR A CD2 1 
ATOM   2037 C  CE1 . TYR A 1 276 ? 73.839  10.187  14.118  1.00 46.05  ? 275 TYR A CE1 1 
ATOM   2038 C  CE2 . TYR A 1 276 ? 75.208  11.472  15.601  1.00 46.18  ? 275 TYR A CE2 1 
ATOM   2039 C  CZ  . TYR A 1 276 ? 73.978  10.952  15.256  1.00 45.48  ? 275 TYR A CZ  1 
ATOM   2040 O  OH  . TYR A 1 276 ? 72.882  11.198  16.048  1.00 53.13  ? 275 TYR A OH  1 
ATOM   2041 N  N   . LEU A 1 277 ? 78.212  13.148  12.819  1.00 41.16  ? 276 LEU A N   1 
ATOM   2042 C  CA  . LEU A 1 277 ? 77.957  14.399  13.529  1.00 41.22  ? 276 LEU A CA  1 
ATOM   2043 C  C   . LEU A 1 277 ? 77.701  15.549  12.564  1.00 44.52  ? 276 LEU A C   1 
ATOM   2044 O  O   . LEU A 1 277 ? 76.767  16.336  12.763  1.00 46.06  ? 276 LEU A O   1 
ATOM   2045 C  CB  . LEU A 1 277 ? 79.126  14.726  14.456  1.00 40.53  ? 276 LEU A CB  1 
ATOM   2046 C  CG  . LEU A 1 277 ? 78.867  15.798  15.516  1.00 44.94  ? 276 LEU A CG  1 
ATOM   2047 C  CD1 . LEU A 1 277 ? 77.591  15.492  16.285  1.00 43.42  ? 276 LEU A CD1 1 
ATOM   2048 C  CD2 . LEU A 1 277 ? 80.055  15.912  16.458  1.00 39.81  ? 276 LEU A CD2 1 
ATOM   2049 N  N   . LEU A 1 278 ? 78.520  15.666  11.519  1.00 44.03  ? 277 LEU A N   1 
ATOM   2050 C  CA  . LEU A 1 278 ? 78.355  16.763  10.567  1.00 39.45  ? 277 LEU A CA  1 
ATOM   2051 C  C   . LEU A 1 278 ? 77.013  16.714  9.844   1.00 40.54  ? 277 LEU A C   1 
ATOM   2052 O  O   . LEU A 1 278 ? 76.313  17.742  9.828   1.00 44.79  ? 277 LEU A O   1 
ATOM   2053 C  CB  . LEU A 1 278 ? 79.535  16.766  9.586   1.00 44.75  ? 277 LEU A CB  1 
ATOM   2054 C  CG  . LEU A 1 278 ? 79.414  17.569  8.288   1.00 38.49  ? 277 LEU A CG  1 
ATOM   2055 C  CD1 . LEU A 1 278 ? 79.162  19.043  8.568   1.00 35.48  ? 277 LEU A CD1 1 
ATOM   2056 C  CD2 . LEU A 1 278 ? 80.657  17.387  7.432   1.00 33.27  ? 277 LEU A CD2 1 
ATOM   2057 N  N   . PRO A 1 279 ? 76.590  15.599  9.232   1.00 43.25  ? 278 PRO A N   1 
ATOM   2058 C  CA  . PRO A 1 279 ? 75.270  15.606  8.577   1.00 48.63  ? 278 PRO A CA  1 
ATOM   2059 C  C   . PRO A 1 279 ? 74.110  15.789  9.543   1.00 48.89  ? 278 PRO A C   1 
ATOM   2060 O  O   . PRO A 1 279 ? 73.122  16.451  9.198   1.00 51.43  ? 278 PRO A O   1 
ATOM   2061 C  CB  . PRO A 1 279 ? 75.215  14.238  7.881   1.00 46.83  ? 278 PRO A CB  1 
ATOM   2062 C  CG  . PRO A 1 279 ? 76.194  13.400  8.602   1.00 38.97  ? 278 PRO A CG  1 
ATOM   2063 C  CD  . PRO A 1 279 ? 77.282  14.311  9.043   1.00 42.67  ? 278 PRO A CD  1 
ATOM   2064 N  N   . THR A 1 280 ? 74.194  15.205  10.741  1.00 45.16  ? 279 THR A N   1 
ATOM   2065 C  CA  . THR A 1 280 ? 73.112  15.338  11.712  1.00 45.50  ? 279 THR A CA  1 
ATOM   2066 C  C   . THR A 1 280 ? 72.912  16.793  12.121  1.00 47.17  ? 279 THR A C   1 
ATOM   2067 O  O   . THR A 1 280 ? 71.794  17.318  12.068  1.00 48.87  ? 279 THR A O   1 
ATOM   2068 C  CB  . THR A 1 280 ? 73.391  14.468  12.938  1.00 43.52  ? 279 THR A CB  1 
ATOM   2069 O  OG1 . THR A 1 280 ? 73.345  13.086  12.565  1.00 35.32  ? 279 THR A OG1 1 
ATOM   2070 C  CG2 . THR A 1 280 ? 72.351  14.726  14.018  1.00 41.74  ? 279 THR A CG2 1 
ATOM   2071 N  N   . LEU A 1 281 ? 73.990  17.460  12.541  1.00 42.41  ? 280 LEU A N   1 
ATOM   2072 C  CA  . LEU A 1 281 ? 73.894  18.862  12.932  1.00 42.71  ? 280 LEU A CA  1 
ATOM   2073 C  C   . LEU A 1 281 ? 73.515  19.762  11.764  1.00 44.61  ? 280 LEU A C   1 
ATOM   2074 O  O   . LEU A 1 281 ? 72.965  20.846  11.985  1.00 40.04  ? 280 LEU A O   1 
ATOM   2075 C  CB  . LEU A 1 281 ? 75.214  19.327  13.548  1.00 34.77  ? 280 LEU A CB  1 
ATOM   2076 C  CG  . LEU A 1 281 ? 75.625  18.718  14.889  1.00 37.66  ? 280 LEU A CG  1 
ATOM   2077 C  CD1 . LEU A 1 281 ? 77.054  19.107  15.228  1.00 36.00  ? 280 LEU A CD1 1 
ATOM   2078 C  CD2 . LEU A 1 281 ? 74.673  19.153  15.992  1.00 39.99  ? 280 LEU A CD2 1 
ATOM   2079 N  N   . SER A 1 282 ? 73.800  19.342  10.528  1.00 44.73  ? 281 SER A N   1 
ATOM   2080 C  CA  . SER A 1 282 ? 73.398  20.134  9.369   1.00 45.84  ? 281 SER A CA  1 
ATOM   2081 C  C   . SER A 1 282 ? 71.882  20.198  9.243   1.00 44.73  ? 281 SER A C   1 
ATOM   2082 O  O   . SER A 1 282 ? 71.326  21.241  8.878   1.00 49.72  ? 281 SER A O   1 
ATOM   2083 C  CB  . SER A 1 282 ? 74.017  19.554  8.098   1.00 44.26  ? 281 SER A CB  1 
ATOM   2084 O  OG  . SER A 1 282 ? 73.593  20.270  6.950   1.00 42.03  ? 281 SER A OG  1 
ATOM   2085 N  N   . ARG A 1 283 ? 71.195  19.095  9.547   1.00 40.15  ? 282 ARG A N   1 
ATOM   2086 C  CA  . ARG A 1 283 ? 69.747  19.049  9.384   1.00 45.49  ? 282 ARG A CA  1 
ATOM   2087 C  C   . ARG A 1 283 ? 69.025  19.815  10.483  1.00 46.03  ? 282 ARG A C   1 
ATOM   2088 O  O   . ARG A 1 283 ? 67.913  20.307  10.262  1.00 48.93  ? 282 ARG A O   1 
ATOM   2089 C  CB  . ARG A 1 283 ? 69.273  17.595  9.358   1.00 55.20  ? 282 ARG A CB  1 
ATOM   2090 C  CG  . ARG A 1 283 ? 69.721  16.819  8.130   1.00 60.80  ? 282 ARG A CG  1 
ATOM   2091 C  CD  . ARG A 1 283 ? 69.117  15.423  8.100   1.00 76.95  ? 282 ARG A CD  1 
ATOM   2092 N  NE  . ARG A 1 283 ? 69.861  14.529  7.220   1.00 94.22  ? 282 ARG A NE  1 
ATOM   2093 C  CZ  . ARG A 1 283 ? 69.792  13.206  7.261   1.00 105.04 ? 282 ARG A CZ  1 
ATOM   2094 N  NH1 . ARG A 1 283 ? 69.003  12.580  8.119   1.00 116.09 ? 282 ARG A NH1 1 
ATOM   2095 N  NH2 . ARG A 1 283 ? 70.529  12.491  6.415   1.00 98.41  ? 282 ARG A NH2 1 
ATOM   2096 N  N   . LEU A 1 284 ? 69.636  19.932  11.659  1.00 45.33  ? 283 LEU A N   1 
ATOM   2097 C  CA  . LEU A 1 284 ? 69.000  20.562  12.806  1.00 43.91  ? 283 LEU A CA  1 
ATOM   2098 C  C   . LEU A 1 284 ? 69.264  22.061  12.786  1.00 52.36  ? 283 LEU A C   1 
ATOM   2099 O  O   . LEU A 1 284 ? 70.387  22.503  12.527  1.00 55.93  ? 283 LEU A O   1 
ATOM   2100 C  CB  . LEU A 1 284 ? 69.512  19.957  14.114  1.00 40.40  ? 283 LEU A CB  1 
ATOM   2101 C  CG  . LEU A 1 284 ? 69.429  18.435  14.245  1.00 39.04  ? 283 LEU A CG  1 
ATOM   2102 C  CD1 . LEU A 1 284 ? 70.255  17.956  15.429  1.00 40.56  ? 283 LEU A CD1 1 
ATOM   2103 C  CD2 . LEU A 1 284 ? 67.985  17.981  14.378  1.00 32.06  ? 283 LEU A CD2 1 
ATOM   2104 N  N   . THR A 1 285 ? 68.223  22.843  13.070  1.00 54.14  ? 284 THR A N   1 
ATOM   2105 C  CA  . THR A 1 285 ? 68.346  24.294  13.020  1.00 58.22  ? 284 THR A CA  1 
ATOM   2106 C  C   . THR A 1 285 ? 67.895  24.916  14.335  1.00 61.81  ? 284 THR A C   1 
ATOM   2107 O  O   . THR A 1 285 ? 68.376  25.988  14.715  1.00 64.25  ? 284 THR A O   1 
ATOM   2108 C  CB  . THR A 1 285 ? 67.529  24.872  11.859  1.00 62.70  ? 284 THR A CB  1 
ATOM   2109 O  OG1 . THR A 1 285 ? 66.130  24.732  12.140  1.00 67.74  ? 284 THR A OG1 1 
ATOM   2110 C  CG2 . THR A 1 285 ? 67.853  24.152  10.557  1.00 57.70  ? 284 THR A CG2 1 
ATOM   2111 N  N   . GLU A 1 286 ? 66.967  24.264  15.030  1.00 58.79  ? 285 GLU A N   1 
ATOM   2112 C  CA  . GLU A 1 286 ? 66.499  24.785  16.306  1.00 59.65  ? 285 GLU A CA  1 
ATOM   2113 C  C   . GLU A 1 286 ? 67.568  24.608  17.376  1.00 51.39  ? 285 GLU A C   1 
ATOM   2114 O  O   . GLU A 1 286 ? 68.266  23.592  17.421  1.00 54.57  ? 285 GLU A O   1 
ATOM   2115 C  CB  . GLU A 1 286 ? 65.197  24.109  16.731  1.00 60.29  ? 285 GLU A CB  1 
ATOM   2116 C  CG  . GLU A 1 286 ? 64.017  24.474  15.850  1.00 61.44  ? 285 GLU A CG  1 
ATOM   2117 C  CD  . GLU A 1 286 ? 63.587  25.921  16.031  1.00 69.74  ? 285 GLU A CD  1 
ATOM   2118 O  OE1 . GLU A 1 286 ? 62.891  26.220  17.025  1.00 77.13  ? 285 GLU A OE1 1 
ATOM   2119 O  OE2 . GLU A 1 286 ? 63.949  26.759  15.178  1.00 70.57  ? 285 GLU A OE2 1 
ATOM   2120 N  N   . LYS A 1 287 ? 67.690  25.613  18.244  1.00 53.40  ? 286 LYS A N   1 
ATOM   2121 C  CA  . LYS A 1 287 ? 68.744  25.605  19.252  1.00 54.09  ? 286 LYS A CA  1 
ATOM   2122 C  C   . LYS A 1 287 ? 68.543  24.489  20.270  1.00 54.96  ? 286 LYS A C   1 
ATOM   2123 O  O   . LYS A 1 287 ? 69.524  23.930  20.773  1.00 51.56  ? 286 LYS A O   1 
ATOM   2124 C  CB  . LYS A 1 287 ? 68.815  26.968  19.935  1.00 55.56  ? 286 LYS A CB  1 
ATOM   2125 C  CG  . LYS A 1 287 ? 69.525  28.013  19.089  1.00 59.40  ? 286 LYS A CG  1 
ATOM   2126 C  CD  . LYS A 1 287 ? 69.561  29.368  19.764  1.00 60.80  ? 286 LYS A CD  1 
ATOM   2127 C  CE  . LYS A 1 287 ? 70.311  30.385  18.916  1.00 58.07  ? 286 LYS A CE  1 
ATOM   2128 N  NZ  . LYS A 1 287 ? 70.885  29.784  17.681  1.00 62.40  ? 286 LYS A NZ  1 
ATOM   2129 N  N   . ARG A 1 288 ? 67.291  24.157  20.593  1.00 55.15  ? 287 ARG A N   1 
ATOM   2130 C  CA  . ARG A 1 288 ? 67.039  23.046  21.505  1.00 59.97  ? 287 ARG A CA  1 
ATOM   2131 C  C   . ARG A 1 288 ? 67.517  21.728  20.904  1.00 56.62  ? 287 ARG A C   1 
ATOM   2132 O  O   . ARG A 1 288 ? 68.137  20.911  21.595  1.00 56.70  ? 287 ARG A O   1 
ATOM   2133 C  CB  . ARG A 1 288 ? 65.549  22.969  21.840  1.00 63.30  ? 287 ARG A CB  1 
ATOM   2134 C  CG  . ARG A 1 288 ? 65.095  23.907  22.948  1.00 69.51  ? 287 ARG A CG  1 
ATOM   2135 C  CD  . ARG A 1 288 ? 64.664  25.257  22.389  1.00 76.61  ? 287 ARG A CD  1 
ATOM   2136 N  NE  . ARG A 1 288 ? 64.832  26.333  23.360  1.00 74.16  ? 287 ARG A NE  1 
ATOM   2137 C  CZ  . ARG A 1 288 ? 64.523  27.602  23.134  1.00 67.40  ? 287 ARG A CZ  1 
ATOM   2138 N  NH1 . ARG A 1 288 ? 64.026  27.997  21.973  1.00 67.88  ? 287 ARG A NH1 1 
ATOM   2139 N  NH2 . ARG A 1 288 ? 64.712  28.498  24.100  1.00 68.10  ? 287 ARG A NH2 1 
ATOM   2140 N  N   . ASP A 1 289 ? 67.238  21.506  19.617  1.00 54.79  ? 288 ASP A N   1 
ATOM   2141 C  CA  . ASP A 1 289 ? 67.650  20.263  18.969  1.00 54.85  ? 288 ASP A CA  1 
ATOM   2142 C  C   . ASP A 1 289 ? 69.166  20.178  18.841  1.00 48.57  ? 288 ASP A C   1 
ATOM   2143 O  O   . ASP A 1 289 ? 69.749  19.102  19.016  1.00 48.57  ? 288 ASP A O   1 
ATOM   2144 C  CB  . ASP A 1 289 ? 66.992  20.142  17.595  1.00 56.93  ? 288 ASP A CB  1 
ATOM   2145 C  CG  . ASP A 1 289 ? 65.480  20.121  17.673  1.00 63.93  ? 288 ASP A CG  1 
ATOM   2146 O  OD1 . ASP A 1 289 ? 64.944  19.803  18.756  1.00 74.31  ? 288 ASP A OD1 1 
ATOM   2147 O  OD2 . ASP A 1 289 ? 64.827  20.419  16.651  1.00 69.43  ? 288 ASP A OD2 1 
ATOM   2148 N  N   . ILE A 1 290 ? 69.819  21.299  18.527  1.00 45.55  ? 289 ILE A N   1 
ATOM   2149 C  CA  . ILE A 1 290 ? 71.274  21.307  18.400  1.00 46.84  ? 289 ILE A CA  1 
ATOM   2150 C  C   . ILE A 1 290 ? 71.928  21.020  19.746  1.00 50.50  ? 289 ILE A C   1 
ATOM   2151 O  O   . ILE A 1 290 ? 72.867  20.221  19.840  1.00 49.43  ? 289 ILE A O   1 
ATOM   2152 C  CB  . ILE A 1 290 ? 71.752  22.649  17.816  1.00 50.52  ? 289 ILE A CB  1 
ATOM   2153 C  CG1 . ILE A 1 290 ? 71.262  22.813  16.375  1.00 48.62  ? 289 ILE A CG1 1 
ATOM   2154 C  CG2 . ILE A 1 290 ? 73.267  22.768  17.903  1.00 45.56  ? 289 ILE A CG2 1 
ATOM   2155 C  CD1 . ILE A 1 290 ? 71.510  24.192  15.799  1.00 48.29  ? 289 ILE A CD1 1 
ATOM   2156 N  N   . THR A 1 291 ? 71.447  21.676  20.805  1.00 51.47  ? 290 THR A N   1 
ATOM   2157 C  CA  . THR A 1 291 ? 71.988  21.445  22.141  1.00 46.78  ? 290 THR A CA  1 
ATOM   2158 C  C   . THR A 1 291 ? 71.856  19.981  22.545  1.00 49.62  ? 290 THR A C   1 
ATOM   2159 O  O   . THR A 1 291 ? 72.807  19.379  23.057  1.00 54.18  ? 290 THR A O   1 
ATOM   2160 C  CB  . THR A 1 291 ? 71.291  22.348  23.156  1.00 53.94  ? 290 THR A CB  1 
ATOM   2161 O  OG1 . THR A 1 291 ? 71.507  23.717  22.800  1.00 55.02  ? 290 THR A OG1 1 
ATOM   2162 C  CG2 . THR A 1 291 ? 71.844  22.104  24.553  1.00 43.91  ? 290 THR A CG2 1 
ATOM   2163 N  N   . ARG A 1 292 ? 70.672  19.398  22.333  1.00 44.19  ? 291 ARG A N   1 
ATOM   2164 C  CA  . ARG A 1 292 ? 70.460  17.994  22.674  1.00 47.31  ? 291 ARG A CA  1 
ATOM   2165 C  C   . ARG A 1 292 ? 71.472  17.092  21.981  1.00 47.44  ? 291 ARG A C   1 
ATOM   2166 O  O   . ARG A 1 292 ? 72.018  16.170  22.598  1.00 51.54  ? 291 ARG A O   1 
ATOM   2167 C  CB  . ARG A 1 292 ? 69.041  17.574  22.289  1.00 52.01  ? 291 ARG A CB  1 
ATOM   2168 C  CG  . ARG A 1 292 ? 68.451  16.475  23.152  1.00 68.02  ? 291 ARG A CG  1 
ATOM   2169 C  CD  . ARG A 1 292 ? 67.092  16.038  22.622  1.00 65.32  ? 291 ARG A CD  1 
ATOM   2170 N  NE  . ARG A 1 292 ? 66.105  17.112  22.621  1.00 79.69  ? 291 ARG A NE  1 
ATOM   2171 C  CZ  . ARG A 1 292 ? 65.470  17.547  23.701  1.00 89.19  ? 291 ARG A CZ  1 
ATOM   2172 N  NH1 . ARG A 1 292 ? 65.686  17.014  24.892  1.00 90.17  ? 291 ARG A NH1 1 
ATOM   2173 N  NH2 . ARG A 1 292 ? 64.586  18.534  23.580  1.00 89.30  ? 291 ARG A NH2 1 
ATOM   2174 N  N   . GLU A 1 293 ? 71.736  17.343  20.698  1.00 47.32  ? 292 GLU A N   1 
ATOM   2175 C  CA  . GLU A 1 293 ? 72.662  16.493  19.957  1.00 47.10  ? 292 GLU A CA  1 
ATOM   2176 C  C   . GLU A 1 293 ? 74.104  16.725  20.396  1.00 51.77  ? 292 GLU A C   1 
ATOM   2177 O  O   . GLU A 1 293 ? 74.887  15.774  20.503  1.00 46.79  ? 292 GLU A O   1 
ATOM   2178 C  CB  . GLU A 1 293 ? 72.506  16.741  18.457  1.00 40.31  ? 292 GLU A CB  1 
ATOM   2179 C  CG  . GLU A 1 293 ? 73.297  15.784  17.586  1.00 46.81  ? 292 GLU A CG  1 
ATOM   2180 C  CD  . GLU A 1 293 ? 72.777  14.362  17.670  1.00 54.72  ? 292 GLU A CD  1 
ATOM   2181 O  OE1 . GLU A 1 293 ? 71.555  14.183  17.864  1.00 47.54  ? 292 GLU A OE1 1 
ATOM   2182 O  OE2 . GLU A 1 293 ? 73.593  13.424  17.548  1.00 54.91  ? 292 GLU A OE2 1 
ATOM   2183 N  N   . VAL A 1 294 ? 74.473  17.984  20.648  1.00 52.08  ? 293 VAL A N   1 
ATOM   2184 C  CA  . VAL A 1 294 ? 75.819  18.295  21.125  1.00 50.28  ? 293 VAL A CA  1 
ATOM   2185 C  C   . VAL A 1 294 ? 76.061  17.677  22.498  1.00 48.18  ? 293 VAL A C   1 
ATOM   2186 O  O   . VAL A 1 294 ? 77.102  17.057  22.745  1.00 49.97  ? 293 VAL A O   1 
ATOM   2187 C  CB  . VAL A 1 294 ? 76.041  19.819  21.145  1.00 49.91  ? 293 VAL A CB  1 
ATOM   2188 C  CG1 . VAL A 1 294 ? 77.283  20.168  21.954  1.00 48.03  ? 293 VAL A CG1 1 
ATOM   2189 C  CG2 . VAL A 1 294 ? 76.151  20.361  19.727  1.00 40.14  ? 293 VAL A CG2 1 
ATOM   2190 N  N   . VAL A 1 295 ? 75.104  17.846  23.413  1.00 46.47  ? 294 VAL A N   1 
ATOM   2191 C  CA  . VAL A 1 295 ? 75.234  17.270  24.751  1.00 50.83  ? 294 VAL A CA  1 
ATOM   2192 C  C   . VAL A 1 295 ? 75.348  15.751  24.677  1.00 46.85  ? 294 VAL A C   1 
ATOM   2193 O  O   . VAL A 1 295 ? 76.205  15.143  25.329  1.00 46.79  ? 294 VAL A O   1 
ATOM   2194 C  CB  . VAL A 1 295 ? 74.053  17.706  25.639  1.00 46.25  ? 294 VAL A CB  1 
ATOM   2195 C  CG1 . VAL A 1 295 ? 73.955  16.819  26.869  1.00 36.63  ? 294 VAL A CG1 1 
ATOM   2196 C  CG2 . VAL A 1 295 ? 74.204  19.164  26.043  1.00 37.14  ? 294 VAL A CG2 1 
ATOM   2197 N  N   . LYS A 1 296 ? 74.483  15.115  23.882  1.00 47.20  ? 295 LYS A N   1 
ATOM   2198 C  CA  . LYS A 1 296 ? 74.519  13.660  23.764  1.00 46.51  ? 295 LYS A CA  1 
ATOM   2199 C  C   . LYS A 1 296 ? 75.847  13.182  23.190  1.00 44.47  ? 295 LYS A C   1 
ATOM   2200 O  O   . LYS A 1 296 ? 76.392  12.163  23.630  1.00 52.26  ? 295 LYS A O   1 
ATOM   2201 C  CB  . LYS A 1 296 ? 73.358  13.167  22.900  1.00 44.53  ? 295 LYS A CB  1 
ATOM   2202 C  CG  . LYS A 1 296 ? 73.335  11.655  22.719  1.00 49.42  ? 295 LYS A CG  1 
ATOM   2203 C  CD  . LYS A 1 296 ? 72.027  11.168  22.115  1.00 47.05  ? 295 LYS A CD  1 
ATOM   2204 C  CE  . LYS A 1 296 ? 71.764  11.814  20.764  1.00 58.35  ? 295 LYS A CE  1 
ATOM   2205 N  NZ  . LYS A 1 296 ? 70.787  11.032  19.956  1.00 62.35  ? 295 LYS A NZ  1 
ATOM   2206 N  N   . SER A 1 297 ? 76.380  13.905  22.204  1.00 44.37  ? 296 SER A N   1 
ATOM   2207 C  CA  . SER A 1 297 ? 77.666  13.540  21.618  1.00 45.07  ? 296 SER A CA  1 
ATOM   2208 C  C   . SER A 1 297 ? 78.792  13.661  22.637  1.00 46.32  ? 296 SER A C   1 
ATOM   2209 O  O   . SER A 1 297 ? 79.618  12.751  22.780  1.00 48.03  ? 296 SER A O   1 
ATOM   2210 C  CB  . SER A 1 297 ? 77.952  14.416  20.398  1.00 44.81  ? 296 SER A CB  1 
ATOM   2211 O  OG  . SER A 1 297 ? 77.036  14.150  19.350  1.00 53.82  ? 296 SER A OG  1 
ATOM   2212 N  N   . LEU A 1 298 ? 78.840  14.785  23.357  1.00 50.65  ? 297 LEU A N   1 
ATOM   2213 C  CA  . LEU A 1 298 ? 79.887  14.988  24.354  1.00 49.87  ? 297 LEU A CA  1 
ATOM   2214 C  C   . LEU A 1 298 ? 79.804  13.952  25.469  1.00 46.28  ? 297 LEU A C   1 
ATOM   2215 O  O   . LEU A 1 298 ? 80.834  13.494  25.977  1.00 45.66  ? 297 LEU A O   1 
ATOM   2216 C  CB  . LEU A 1 298 ? 79.800  16.406  24.920  1.00 42.21  ? 297 LEU A CB  1 
ATOM   2217 C  CG  . LEU A 1 298 ? 80.333  17.519  24.015  1.00 43.05  ? 297 LEU A CG  1 
ATOM   2218 C  CD1 . LEU A 1 298 ? 79.921  18.888  24.538  1.00 41.34  ? 297 LEU A CD1 1 
ATOM   2219 C  CD2 . LEU A 1 298 ? 81.846  17.427  23.878  1.00 45.53  ? 297 LEU A CD2 1 
ATOM   2220 N  N   . LYS A 1 299 ? 78.588  13.575  25.871  1.00 43.38  ? 298 LYS A N   1 
ATOM   2221 C  CA  . LYS A 1 299 ? 78.434  12.572  26.918  1.00 47.11  ? 298 LYS A CA  1 
ATOM   2222 C  C   . LYS A 1 299 ? 78.950  11.204  26.490  1.00 51.90  ? 298 LYS A C   1 
ATOM   2223 O  O   . LYS A 1 299 ? 79.283  10.383  27.351  1.00 48.21  ? 298 LYS A O   1 
ATOM   2224 C  CB  . LYS A 1 299 ? 76.969  12.473  27.347  1.00 46.06  ? 298 LYS A CB  1 
ATOM   2225 C  CG  . LYS A 1 299 ? 76.592  13.476  28.424  1.00 49.88  ? 298 LYS A CG  1 
ATOM   2226 C  CD  . LYS A 1 299 ? 75.090  13.680  28.514  1.00 52.70  ? 298 LYS A CD  1 
ATOM   2227 C  CE  . LYS A 1 299 ? 74.685  14.073  29.929  1.00 70.13  ? 298 LYS A CE  1 
ATOM   2228 N  NZ  . LYS A 1 299 ? 73.860  13.031  30.606  1.00 81.93  ? 298 LYS A NZ  1 
ATOM   2229 N  N   . PHE A 1 300 ? 79.026  10.943  25.186  1.00 49.63  ? 299 PHE A N   1 
ATOM   2230 C  CA  . PHE A 1 300 ? 79.537  9.678   24.672  1.00 50.58  ? 299 PHE A CA  1 
ATOM   2231 C  C   . PHE A 1 300 ? 81.023  9.733   24.342  1.00 53.87  ? 299 PHE A C   1 
ATOM   2232 O  O   . PHE A 1 300 ? 81.763  8.797   24.662  1.00 57.59  ? 299 PHE A O   1 
ATOM   2233 C  CB  . PHE A 1 300 ? 78.764  9.256   23.420  1.00 46.39  ? 299 PHE A CB  1 
ATOM   2234 C  CG  . PHE A 1 300 ? 79.487  8.231   22.584  1.00 53.25  ? 299 PHE A CG  1 
ATOM   2235 C  CD1 . PHE A 1 300 ? 79.606  6.921   23.018  1.00 48.62  ? 299 PHE A CD1 1 
ATOM   2236 C  CD2 . PHE A 1 300 ? 80.054  8.582   21.368  1.00 50.75  ? 299 PHE A CD2 1 
ATOM   2237 C  CE1 . PHE A 1 300 ? 80.273  5.978   22.256  1.00 48.56  ? 299 PHE A CE1 1 
ATOM   2238 C  CE2 . PHE A 1 300 ? 80.722  7.644   20.600  1.00 50.85  ? 299 PHE A CE2 1 
ATOM   2239 C  CZ  . PHE A 1 300 ? 80.832  6.341   21.044  1.00 49.03  ? 299 PHE A CZ  1 
ATOM   2240 N  N   . VAL A 1 301 ? 81.476  10.813  23.707  1.00 47.64  ? 300 VAL A N   1 
ATOM   2241 C  CA  . VAL A 1 301 ? 82.824  10.823  23.154  1.00 55.29  ? 300 VAL A CA  1 
ATOM   2242 C  C   . VAL A 1 301 ? 83.865  11.104  24.234  1.00 58.60  ? 300 VAL A C   1 
ATOM   2243 O  O   . VAL A 1 301 ? 84.962  10.537  24.206  1.00 52.66  ? 300 VAL A O   1 
ATOM   2244 C  CB  . VAL A 1 301 ? 82.906  11.822  21.981  1.00 54.00  ? 300 VAL A CB  1 
ATOM   2245 C  CG1 . VAL A 1 301 ? 83.006  13.265  22.468  1.00 56.91  ? 300 VAL A CG1 1 
ATOM   2246 C  CG2 . VAL A 1 301 ? 84.059  11.463  21.057  1.00 56.39  ? 300 VAL A CG2 1 
ATOM   2247 N  N   . LEU A 1 302 ? 83.551  11.962  25.207  1.00 53.28  ? 301 LEU A N   1 
ATOM   2248 C  CA  . LEU A 1 302 ? 84.539  12.282  26.236  1.00 52.52  ? 301 LEU A CA  1 
ATOM   2249 C  C   . LEU A 1 302 ? 84.899  11.077  27.097  1.00 52.17  ? 301 LEU A C   1 
ATOM   2250 O  O   . LEU A 1 302 ? 86.101  10.832  27.299  1.00 49.44  ? 301 LEU A O   1 
ATOM   2251 C  CB  . LEU A 1 302 ? 84.056  13.464  27.084  1.00 51.95  ? 301 LEU A CB  1 
ATOM   2252 C  CG  . LEU A 1 302 ? 84.184  14.841  26.433  1.00 50.30  ? 301 LEU A CG  1 
ATOM   2253 C  CD1 . LEU A 1 302 ? 83.592  15.916  27.328  1.00 58.91  ? 301 LEU A CD1 1 
ATOM   2254 C  CD2 . LEU A 1 302 ? 85.640  15.142  26.121  1.00 59.27  ? 301 LEU A CD2 1 
ATOM   2255 N  N   . PRO A 1 303 ? 83.952  10.294  27.632  1.00 51.37  ? 302 PRO A N   1 
ATOM   2256 C  CA  . PRO A 1 303 ? 84.363  9.100   28.388  1.00 58.53  ? 302 PRO A CA  1 
ATOM   2257 C  C   . PRO A 1 303 ? 85.021  8.044   27.519  1.00 56.68  ? 302 PRO A C   1 
ATOM   2258 O  O   . PRO A 1 303 ? 85.912  7.332   27.998  1.00 58.24  ? 302 PRO A O   1 
ATOM   2259 C  CB  . PRO A 1 303 ? 83.048  8.588   28.996  1.00 59.00  ? 302 PRO A CB  1 
ATOM   2260 C  CG  . PRO A 1 303 ? 82.101  9.738   28.907  1.00 55.95  ? 302 PRO A CG  1 
ATOM   2261 C  CD  . PRO A 1 303 ? 82.488  10.462  27.661  1.00 54.19  ? 302 PRO A CD  1 
ATOM   2262 N  N   . ALA A 1 304 ? 84.610  7.924   26.255  1.00 50.35  ? 303 ALA A N   1 
ATOM   2263 C  CA  . ALA A 1 304 ? 85.198  6.918   25.378  1.00 52.93  ? 303 ALA A CA  1 
ATOM   2264 C  C   . ALA A 1 304 ? 86.648  7.255   25.050  1.00 59.01  ? 303 ALA A C   1 
ATOM   2265 O  O   . ALA A 1 304 ? 87.525  6.384   25.097  1.00 59.94  ? 303 ALA A O   1 
ATOM   2266 C  CB  . ALA A 1 304 ? 84.369  6.791   24.099  1.00 47.16  ? 303 ALA A CB  1 
ATOM   2267 N  N   . VAL A 1 305 ? 86.919  8.517   24.714  1.00 57.97  ? 304 VAL A N   1 
ATOM   2268 C  CA  . VAL A 1 305 ? 88.282  8.914   24.373  1.00 57.97  ? 304 VAL A CA  1 
ATOM   2269 C  C   . VAL A 1 305 ? 89.168  8.918   25.613  1.00 55.61  ? 304 VAL A C   1 
ATOM   2270 O  O   . VAL A 1 305 ? 90.353  8.571   25.544  1.00 60.44  ? 304 VAL A O   1 
ATOM   2271 C  CB  . VAL A 1 305 ? 88.270  10.284  23.673  1.00 59.02  ? 304 VAL A CB  1 
ATOM   2272 C  CG1 . VAL A 1 305 ? 89.687  10.763  23.394  1.00 57.70  ? 304 VAL A CG1 1 
ATOM   2273 C  CG2 . VAL A 1 305 ? 87.467  10.203  22.391  1.00 58.26  ? 304 VAL A CG2 1 
ATOM   2274 N  N   . ALA A 1 306 ? 88.611  9.297   26.766  1.00 53.80  ? 305 ALA A N   1 
ATOM   2275 C  CA  . ALA A 1 306 ? 89.385  9.274   28.004  1.00 53.53  ? 305 ALA A CA  1 
ATOM   2276 C  C   . ALA A 1 306 ? 89.794  7.853   28.367  1.00 55.52  ? 305 ALA A C   1 
ATOM   2277 O  O   . ALA A 1 306 ? 90.950  7.599   28.725  1.00 48.81  ? 305 ALA A O   1 
ATOM   2278 C  CB  . ALA A 1 306 ? 88.586  9.916   29.139  1.00 48.70  ? 305 ALA A CB  1 
ATOM   2279 N  N   . ALA A 1 307 ? 88.849  6.911   28.294  1.00 55.20  ? 306 ALA A N   1 
ATOM   2280 C  CA  . ALA A 1 307 ? 89.180  5.513   28.549  1.00 53.83  ? 306 ALA A CA  1 
ATOM   2281 C  C   . ALA A 1 307 ? 90.225  5.007   27.563  1.00 52.09  ? 306 ALA A C   1 
ATOM   2282 O  O   . ALA A 1 307 ? 91.183  4.329   27.955  1.00 52.43  ? 306 ALA A O   1 
ATOM   2283 C  CB  . ALA A 1 307 ? 87.917  4.655   28.482  1.00 47.44  ? 306 ALA A CB  1 
ATOM   2284 N  N   . ALA A 1 308 ? 90.056  5.321   26.276  1.00 49.87  ? 307 ALA A N   1 
ATOM   2285 C  CA  . ALA A 1 308 ? 91.014  4.872   25.272  1.00 49.95  ? 307 ALA A CA  1 
ATOM   2286 C  C   . ALA A 1 308 ? 92.381  5.514   25.480  1.00 54.20  ? 307 ALA A C   1 
ATOM   2287 O  O   . ALA A 1 308 ? 93.413  4.844   25.357  1.00 52.13  ? 307 ALA A O   1 
ATOM   2288 C  CB  . ALA A 1 308 ? 90.487  5.172   23.871  1.00 46.78  ? 307 ALA A CB  1 
ATOM   2289 N  N   . SER A 1 309 ? 92.409  6.812   25.797  1.00 53.17  ? 308 SER A N   1 
ATOM   2290 C  CA  . SER A 1 309 ? 93.682  7.505   25.960  1.00 52.70  ? 308 SER A CA  1 
ATOM   2291 C  C   . SER A 1 309 ? 94.401  7.069   27.229  1.00 52.10  ? 308 SER A C   1 
ATOM   2292 O  O   . SER A 1 309 ? 95.636  7.030   27.259  1.00 51.67  ? 308 SER A O   1 
ATOM   2293 C  CB  . SER A 1 309 ? 93.458  9.017   25.970  1.00 56.26  ? 308 SER A CB  1 
ATOM   2294 O  OG  . SER A 1 309 ? 92.931  9.460   24.731  1.00 56.03  ? 308 SER A OG  1 
ATOM   2295 N  N   . PHE A 1 310 ? 93.651  6.737   28.281  1.00 48.02  ? 309 PHE A N   1 
ATOM   2296 C  CA  . PHE A 1 310 ? 94.269  6.204   29.490  1.00 51.07  ? 309 PHE A CA  1 
ATOM   2297 C  C   . PHE A 1 310 ? 94.909  4.849   29.224  1.00 57.45  ? 309 PHE A C   1 
ATOM   2298 O  O   . PHE A 1 310 ? 96.002  4.561   29.726  1.00 60.70  ? 309 PHE A O   1 
ATOM   2299 C  CB  . PHE A 1 310 ? 93.230  6.105   30.606  1.00 50.99  ? 309 PHE A CB  1 
ATOM   2300 C  CG  . PHE A 1 310 ? 93.771  5.548   31.889  1.00 53.84  ? 309 PHE A CG  1 
ATOM   2301 C  CD1 . PHE A 1 310 ? 94.808  6.185   32.550  1.00 56.61  ? 309 PHE A CD1 1 
ATOM   2302 C  CD2 . PHE A 1 310 ? 93.237  4.396   32.441  1.00 58.44  ? 309 PHE A CD2 1 
ATOM   2303 C  CE1 . PHE A 1 310 ? 95.309  5.679   33.735  1.00 55.79  ? 309 PHE A CE1 1 
ATOM   2304 C  CE2 . PHE A 1 310 ? 93.732  3.886   33.626  1.00 64.51  ? 309 PHE A CE2 1 
ATOM   2305 C  CZ  . PHE A 1 310 ? 94.770  4.528   34.274  1.00 57.57  ? 309 PHE A CZ  1 
ATOM   2306 N  N   . THR A 1 311 ? 94.236  4.002   28.442  1.00 48.65  ? 310 THR A N   1 
ATOM   2307 C  CA  . THR A 1 311 ? 94.818  2.722   28.051  1.00 51.82  ? 310 THR A CA  1 
ATOM   2308 C  C   . THR A 1 311 ? 96.108  2.925   27.265  1.00 56.61  ? 310 THR A C   1 
ATOM   2309 O  O   . THR A 1 311 ? 97.102  2.225   27.496  1.00 58.73  ? 310 THR A O   1 
ATOM   2310 C  CB  . THR A 1 311 ? 93.810  1.920   27.227  1.00 54.79  ? 310 THR A CB  1 
ATOM   2311 O  OG1 . THR A 1 311 ? 92.599  1.757   27.976  1.00 55.90  ? 310 THR A OG1 1 
ATOM   2312 C  CG2 . THR A 1 311 ? 94.372  0.552   26.881  1.00 54.14  ? 310 THR A CG2 1 
ATOM   2313 N  N   . VAL A 1 312 ? 96.107  3.877   26.329  1.00 54.12  ? 311 VAL A N   1 
ATOM   2314 C  CA  . VAL A 1 312 ? 97.301  4.150   25.532  1.00 52.02  ? 311 VAL A CA  1 
ATOM   2315 C  C   . VAL A 1 312 ? 98.452  4.594   26.425  1.00 57.23  ? 311 VAL A C   1 
ATOM   2316 O  O   . VAL A 1 312 ? 99.596  4.152   26.253  1.00 59.66  ? 311 VAL A O   1 
ATOM   2317 C  CB  . VAL A 1 312 ? 96.988  5.196   24.445  1.00 50.60  ? 311 VAL A CB  1 
ATOM   2318 C  CG1 . VAL A 1 312 ? 98.271  5.691   23.793  1.00 53.65  ? 311 VAL A CG1 1 
ATOM   2319 C  CG2 . VAL A 1 312 ? 96.054  4.608   23.400  1.00 47.86  ? 311 VAL A CG2 1 
ATOM   2320 N  N   . TRP A 1 313 ? 98.174  5.473   27.393  1.00 54.27  ? 312 TRP A N   1 
ATOM   2321 C  CA  . TRP A 1 313 ? 99.232  5.934   28.287  1.00 59.54  ? 312 TRP A CA  1 
ATOM   2322 C  C   . TRP A 1 313 ? 99.789  4.786   29.120  1.00 60.45  ? 312 TRP A C   1 
ATOM   2323 O  O   . TRP A 1 313 ? 100.996 4.732   29.385  1.00 63.75  ? 312 TRP A O   1 
ATOM   2324 C  CB  . TRP A 1 313 ? 98.713  7.052   29.191  1.00 59.09  ? 312 TRP A CB  1 
ATOM   2325 C  CG  . TRP A 1 313 ? 99.687  7.451   30.256  1.00 58.54  ? 312 TRP A CG  1 
ATOM   2326 C  CD1 . TRP A 1 313 ? 100.734 8.317   30.127  1.00 59.89  ? 312 TRP A CD1 1 
ATOM   2327 C  CD2 . TRP A 1 313 ? 99.701  7.006   31.618  1.00 57.27  ? 312 TRP A CD2 1 
ATOM   2328 N  NE1 . TRP A 1 313 ? 101.403 8.434   31.321  1.00 60.69  ? 312 TRP A NE1 1 
ATOM   2329 C  CE2 . TRP A 1 313 ? 100.788 7.640   32.253  1.00 57.89  ? 312 TRP A CE2 1 
ATOM   2330 C  CE3 . TRP A 1 313 ? 98.901  6.133   32.361  1.00 56.12  ? 312 TRP A CE3 1 
ATOM   2331 C  CZ2 . TRP A 1 313 ? 101.094 7.429   33.596  1.00 57.44  ? 312 TRP A CZ2 1 
ATOM   2332 C  CZ3 . TRP A 1 313 ? 99.207  5.924   33.694  1.00 59.91  ? 312 TRP A CZ3 1 
ATOM   2333 C  CH2 . TRP A 1 313 ? 100.295 6.570   34.297  1.00 64.87  ? 312 TRP A CH2 1 
ATOM   2334 N  N   . LEU A 1 314 ? 98.924  3.866   29.553  1.00 52.89  ? 313 LEU A N   1 
ATOM   2335 C  CA  . LEU A 1 314 ? 99.400  2.702   30.294  1.00 58.15  ? 313 LEU A CA  1 
ATOM   2336 C  C   . LEU A 1 314 ? 100.347 1.864   29.445  1.00 64.24  ? 313 LEU A C   1 
ATOM   2337 O  O   . LEU A 1 314 ? 101.315 1.292   29.959  1.00 70.13  ? 313 LEU A O   1 
ATOM   2338 C  CB  . LEU A 1 314 ? 98.222  1.855   30.774  1.00 63.61  ? 313 LEU A CB  1 
ATOM   2339 C  CG  . LEU A 1 314 ? 97.374  2.436   31.905  1.00 59.26  ? 313 LEU A CG  1 
ATOM   2340 C  CD1 . LEU A 1 314 ? 96.019  1.749   31.958  1.00 57.14  ? 313 LEU A CD1 1 
ATOM   2341 C  CD2 . LEU A 1 314 ? 98.098  2.322   33.238  1.00 47.99  ? 313 LEU A CD2 1 
ATOM   2342 N  N   . LEU A 1 315 ? 100.082 1.780   28.142  1.00 60.53  ? 314 LEU A N   1 
ATOM   2343 C  CA  . LEU A 1 315 ? 100.890 0.993   27.221  1.00 62.70  ? 314 LEU A CA  1 
ATOM   2344 C  C   . LEU A 1 315 ? 101.764 1.875   26.332  1.00 62.48  ? 314 LEU A C   1 
ATOM   2345 O  O   . LEU A 1 315 ? 102.053 1.514   25.189  1.00 61.84  ? 314 LEU A O   1 
ATOM   2346 C  CB  . LEU A 1 315 ? 99.992  0.108   26.358  1.00 67.16  ? 314 LEU A CB  1 
ATOM   2347 C  CG  . LEU A 1 315 ? 99.122  -0.930  27.070  1.00 69.67  ? 314 LEU A CG  1 
ATOM   2348 C  CD1 . LEU A 1 315 ? 98.313  -1.731  26.059  1.00 67.86  ? 314 LEU A CD1 1 
ATOM   2349 C  CD2 . LEU A 1 315 ? 99.975  -1.849  27.929  1.00 70.55  ? 314 LEU A CD2 1 
ATOM   2350 N  N   . ARG A 1 316 ? 102.181 3.040   26.841  1.00 67.40  ? 315 ARG A N   1 
ATOM   2351 C  CA  . ARG A 1 316 ? 102.971 3.959   26.025  1.00 64.82  ? 315 ARG A CA  1 
ATOM   2352 C  C   . ARG A 1 316 ? 104.277 3.325   25.564  1.00 65.28  ? 315 ARG A C   1 
ATOM   2353 O  O   . ARG A 1 316 ? 104.736 3.594   24.448  1.00 70.21  ? 315 ARG A O   1 
ATOM   2354 C  CB  . ARG A 1 316 ? 103.244 5.261   26.785  1.00 64.89  ? 315 ARG A CB  1 
ATOM   2355 C  CG  . ARG A 1 316 ? 103.972 5.127   28.116  1.00 66.67  ? 315 ARG A CG  1 
ATOM   2356 C  CD  . ARG A 1 316 ? 103.765 6.384   28.958  1.00 64.81  ? 315 ARG A CD  1 
ATOM   2357 N  NE  . ARG A 1 316 ? 104.568 6.396   30.176  1.00 60.93  ? 315 ARG A NE  1 
ATOM   2358 C  CZ  . ARG A 1 316 ? 104.292 5.693   31.266  1.00 55.55  ? 315 ARG A CZ  1 
ATOM   2359 N  NH1 . ARG A 1 316 ? 103.234 4.902   31.329  1.00 53.91  ? 315 ARG A NH1 1 
ATOM   2360 N  NH2 . ARG A 1 316 ? 105.096 5.791   32.321  1.00 61.73  ? 315 ARG A NH2 1 
ATOM   2361 N  N   . ASP A 1 317 ? 104.885 2.477   26.397  1.00 66.81  ? 316 ASP A N   1 
ATOM   2362 C  CA  . ASP A 1 317 ? 106.113 1.802   25.992  1.00 67.68  ? 316 ASP A CA  1 
ATOM   2363 C  C   . ASP A 1 317 ? 105.851 0.793   24.882  1.00 63.71  ? 316 ASP A C   1 
ATOM   2364 O  O   . ASP A 1 317 ? 106.664 0.648   23.962  1.00 60.32  ? 316 ASP A O   1 
ATOM   2365 C  CB  . ASP A 1 317 ? 106.757 1.119   27.198  1.00 71.04  ? 316 ASP A CB  1 
ATOM   2366 C  CG  . ASP A 1 317 ? 107.585 2.074   28.033  1.00 77.43  ? 316 ASP A CG  1 
ATOM   2367 O  OD1 . ASP A 1 317 ? 108.027 3.109   27.490  1.00 76.92  ? 316 ASP A OD1 1 
ATOM   2368 O  OD2 . ASP A 1 317 ? 107.797 1.790   29.231  1.00 83.65  ? 316 ASP A OD2 1 
ATOM   2369 N  N   . PHE A 1 318 ? 104.719 0.089   24.945  1.00 63.73  ? 317 PHE A N   1 
ATOM   2370 C  CA  . PHE A 1 318 ? 104.356 -0.816  23.860  1.00 60.88  ? 317 PHE A CA  1 
ATOM   2371 C  C   . PHE A 1 318 ? 103.995 -0.049  22.594  1.00 62.60  ? 317 PHE A C   1 
ATOM   2372 O  O   . PHE A 1 318 ? 104.349 -0.469  21.486  1.00 61.90  ? 317 PHE A O   1 
ATOM   2373 C  CB  . PHE A 1 318 ? 103.199 -1.713  24.295  1.00 58.66  ? 317 PHE A CB  1 
ATOM   2374 C  CG  . PHE A 1 318 ? 102.539 -2.440  23.162  1.00 69.83  ? 317 PHE A CG  1 
ATOM   2375 C  CD1 . PHE A 1 318 ? 103.091 -3.603  22.655  1.00 65.07  ? 317 PHE A CD1 1 
ATOM   2376 C  CD2 . PHE A 1 318 ? 101.358 -1.966  22.611  1.00 66.40  ? 317 PHE A CD2 1 
ATOM   2377 C  CE1 . PHE A 1 318 ? 102.486 -4.272  21.613  1.00 66.19  ? 317 PHE A CE1 1 
ATOM   2378 C  CE2 . PHE A 1 318 ? 100.748 -2.632  21.569  1.00 61.89  ? 317 PHE A CE2 1 
ATOM   2379 C  CZ  . PHE A 1 318 ? 101.310 -3.787  21.070  1.00 69.64  ? 317 PHE A CZ  1 
ATOM   2380 N  N   . ALA A 1 319 ? 103.279 1.068   22.736  1.00 62.71  ? 318 ALA A N   1 
ATOM   2381 C  CA  . ALA A 1 319 ? 102.913 1.867   21.571  1.00 61.07  ? 318 ALA A CA  1 
ATOM   2382 C  C   . ALA A 1 319 ? 104.147 2.432   20.877  1.00 69.48  ? 318 ALA A C   1 
ATOM   2383 O  O   . ALA A 1 319 ? 104.204 2.490   19.643  1.00 68.16  ? 318 ALA A O   1 
ATOM   2384 C  CB  . ALA A 1 319 ? 101.963 2.992   21.980  1.00 62.65  ? 318 ALA A CB  1 
ATOM   2385 N  N   . ILE A 1 320 ? 105.148 2.846   21.655  1.00 69.48  ? 319 ILE A N   1 
ATOM   2386 C  CA  . ILE A 1 320 ? 106.391 3.346   21.073  1.00 70.11  ? 319 ILE A CA  1 
ATOM   2387 C  C   . ILE A 1 320 ? 107.146 2.225   20.367  1.00 68.73  ? 319 ILE A C   1 
ATOM   2388 O  O   . ILE A 1 320 ? 107.607 2.387   19.231  1.00 70.99  ? 319 ILE A O   1 
ATOM   2389 C  CB  . ILE A 1 320 ? 107.256 4.010   22.161  1.00 71.63  ? 319 ILE A CB  1 
ATOM   2390 C  CG1 . ILE A 1 320 ? 106.685 5.377   22.543  1.00 71.28  ? 319 ILE A CG1 1 
ATOM   2391 C  CG2 . ILE A 1 320 ? 108.701 4.137   21.698  1.00 75.02  ? 319 ILE A CG2 1 
ATOM   2392 C  CD1 . ILE A 1 320 ? 107.401 6.033   23.706  1.00 80.88  ? 319 ILE A CD1 1 
ATOM   2393 N  N   . TRP A 1 321 ? 107.285 1.073   21.027  1.00 63.65  ? 320 TRP A N   1 
ATOM   2394 C  CA  . TRP A 1 321 ? 108.019 -0.040  20.430  1.00 69.80  ? 320 TRP A CA  1 
ATOM   2395 C  C   . TRP A 1 321 ? 107.352 -0.569  19.165  1.00 67.72  ? 320 TRP A C   1 
ATOM   2396 O  O   . TRP A 1 321 ? 108.041 -1.046  18.256  1.00 69.73  ? 320 TRP A O   1 
ATOM   2397 C  CB  . TRP A 1 321 ? 108.172 -1.167  21.452  1.00 70.77  ? 320 TRP A CB  1 
ATOM   2398 C  CG  . TRP A 1 321 ? 108.592 -2.470  20.847  1.00 73.61  ? 320 TRP A CG  1 
ATOM   2399 C  CD1 . TRP A 1 321 ? 109.860 -2.855  20.523  1.00 72.63  ? 320 TRP A CD1 1 
ATOM   2400 C  CD2 . TRP A 1 321 ? 107.736 -3.559  20.477  1.00 74.06  ? 320 TRP A CD2 1 
ATOM   2401 N  NE1 . TRP A 1 321 ? 109.848 -4.118  19.983  1.00 65.50  ? 320 TRP A NE1 1 
ATOM   2402 C  CE2 . TRP A 1 321 ? 108.555 -4.571  19.943  1.00 66.82  ? 320 TRP A CE2 1 
ATOM   2403 C  CE3 . TRP A 1 321 ? 106.356 -3.775  20.549  1.00 73.46  ? 320 TRP A CE3 1 
ATOM   2404 C  CZ2 . TRP A 1 321 ? 108.042 -5.782  19.483  1.00 70.21  ? 320 TRP A CZ2 1 
ATOM   2405 C  CZ3 . TRP A 1 321 ? 105.848 -4.978  20.093  1.00 72.27  ? 320 TRP A CZ3 1 
ATOM   2406 C  CH2 . TRP A 1 321 ? 106.689 -5.966  19.567  1.00 68.61  ? 320 TRP A CH2 1 
ATOM   2407 N  N   . LEU A 1 322 ? 106.026 -0.486  19.077  1.00 70.71  ? 321 LEU A N   1 
ATOM   2408 C  CA  . LEU A 1 322 ? 105.316 -1.050  17.934  1.00 71.75  ? 321 LEU A CA  1 
ATOM   2409 C  C   . LEU A 1 322 ? 105.165 -0.069  16.777  1.00 71.63  ? 321 LEU A C   1 
ATOM   2410 O  O   . LEU A 1 322 ? 105.382 -0.440  15.619  1.00 77.06  ? 321 LEU A O   1 
ATOM   2411 C  CB  . LEU A 1 322 ? 103.935 -1.547  18.375  1.00 68.79  ? 321 LEU A CB  1 
ATOM   2412 C  CG  . LEU A 1 322 ? 103.000 -2.094  17.294  1.00 67.01  ? 321 LEU A CG  1 
ATOM   2413 C  CD1 . LEU A 1 322 ? 103.007 -3.615  17.302  1.00 65.51  ? 321 LEU A CD1 1 
ATOM   2414 C  CD2 . LEU A 1 322 ? 101.588 -1.561  17.483  1.00 71.15  ? 321 LEU A CD2 1 
ATOM   2415 N  N   . LEU A 1 323 ? 104.807 1.180   17.065  1.00 75.14  ? 322 LEU A N   1 
ATOM   2416 C  CA  . LEU A 1 323 ? 104.404 2.113   16.022  1.00 81.24  ? 322 LEU A CA  1 
ATOM   2417 C  C   . LEU A 1 323 ? 105.546 2.946   15.454  1.00 82.75  ? 322 LEU A C   1 
ATOM   2418 O  O   . LEU A 1 323 ? 105.432 3.428   14.320  1.00 84.68  ? 322 LEU A O   1 
ATOM   2419 C  CB  . LEU A 1 323 ? 103.316 3.048   16.557  1.00 75.69  ? 322 LEU A CB  1 
ATOM   2420 C  CG  . LEU A 1 323 ? 101.891 2.495   16.588  1.00 71.27  ? 322 LEU A CG  1 
ATOM   2421 C  CD1 . LEU A 1 323 ? 101.068 3.205   17.648  1.00 69.97  ? 322 LEU A CD1 1 
ATOM   2422 C  CD2 . LEU A 1 323 ? 101.236 2.628   15.223  1.00 75.08  ? 322 LEU A CD2 1 
ATOM   2423 N  N   . LEU A 1 324 ? 106.639 3.123   16.191  1.00 85.52  ? 323 LEU A N   1 
ATOM   2424 C  CA  . LEU A 1 324 ? 107.688 4.050   15.793  1.00 97.76  ? 323 LEU A CA  1 
ATOM   2425 C  C   . LEU A 1 324 ? 109.039 3.349   15.789  1.00 109.77 ? 323 LEU A C   1 
ATOM   2426 O  O   . LEU A 1 324 ? 109.250 2.355   16.489  1.00 104.58 ? 323 LEU A O   1 
ATOM   2427 C  CB  . LEU A 1 324 ? 107.741 5.268   16.727  1.00 95.55  ? 323 LEU A CB  1 
ATOM   2428 C  CG  . LEU A 1 324 ? 106.611 6.292   16.605  1.00 90.37  ? 323 LEU A CG  1 
ATOM   2429 C  CD1 . LEU A 1 324 ? 106.162 6.751   17.984  1.00 78.19  ? 323 LEU A CD1 1 
ATOM   2430 C  CD2 . LEU A 1 324 ? 107.050 7.478   15.764  1.00 94.93  ? 323 LEU A CD2 1 
ATOM   2431 N  N   . SER A 1 325 ? 109.987 3.894   15.034  1.00 123.24 ? 324 SER A N   1 
ATOM   2432 C  CA  . SER A 1 325 ? 111.332 3.330   15.037  1.00 128.58 ? 324 SER A CA  1 
ATOM   2433 C  C   . SER A 1 325 ? 111.996 3.605   16.375  1.00 133.88 ? 324 SER A C   1 
ATOM   2434 O  O   . SER A 1 325 ? 111.899 4.713   16.902  1.00 139.15 ? 324 SER A O   1 
ATOM   2435 C  CB  . SER A 1 325 ? 112.171 3.920   13.908  1.00 130.32 ? 324 SER A CB  1 
ATOM   2436 O  OG  . SER A 1 325 ? 113.491 3.405   13.940  1.00 138.32 ? 324 SER A OG  1 
ATOM   2437 N  N   . ASN A 1 326 ? 112.671 2.603   16.927  1.00 140.42 ? 325 ASN A N   1 
ATOM   2438 C  CA  . ASN A 1 326 ? 113.307 2.765   18.231  1.00 144.16 ? 325 ASN A CA  1 
ATOM   2439 C  C   . ASN A 1 326 ? 114.572 3.604   18.139  1.00 148.84 ? 325 ASN A C   1 
ATOM   2440 O  O   . ASN A 1 326 ? 115.677 3.092   18.310  1.00 156.37 ? 325 ASN A O   1 
ATOM   2441 C  CB  . ASN A 1 326 ? 113.622 1.404   18.850  1.00 143.24 ? 325 ASN A CB  1 
ATOM   2442 C  CG  . ASN A 1 326 ? 114.011 1.511   20.310  1.00 142.36 ? 325 ASN A CG  1 
ATOM   2443 O  OD1 . ASN A 1 326 ? 113.546 2.398   21.024  1.00 138.42 ? 325 ASN A OD1 1 
ATOM   2444 N  ND2 . ASN A 1 326 ? 114.864 0.600   20.763  1.00 138.45 ? 325 ASN A ND2 1 
ATOM   2445 N  N   . LYS A 1 327 ? 114.414 4.892   17.870  1.00 149.77 ? 326 LYS A N   1 
ATOM   2446 C  CA  . LYS A 1 327 ? 115.562 5.794   17.792  1.00 154.05 ? 326 LYS A CA  1 
ATOM   2447 C  C   . LYS A 1 327 ? 115.357 6.864   18.832  1.00 157.23 ? 326 LYS A C   1 
ATOM   2448 O  O   . LYS A 1 327 ? 116.167 7.782   18.953  1.00 160.41 ? 326 LYS A O   1 
ATOM   2449 C  CB  . LYS A 1 327 ? 115.665 6.424   16.411  1.00 154.25 ? 326 LYS A CB  1 
ATOM   2450 C  CG  . LYS A 1 327 ? 116.000 5.445   15.303  1.00 152.56 ? 326 LYS A CG  1 
ATOM   2451 C  CD  . LYS A 1 327 ? 116.059 6.151   13.960  1.00 144.45 ? 326 LYS A CD  1 
ATOM   2452 C  CE  . LYS A 1 327 ? 116.419 5.185   12.844  1.00 139.59 ? 326 LYS A CE  1 
ATOM   2453 N  NZ  . LYS A 1 327 ? 116.455 5.864   11.520  1.00 142.01 ? 326 LYS A NZ  1 
ATOM   2454 N  N   . PHE A 1 328 ? 114.277 6.748   19.591  1.00 156.40 ? 327 PHE A N   1 
ATOM   2455 C  CA  . PHE A 1 328 ? 113.935 7.724   20.611  1.00 154.38 ? 327 PHE A CA  1 
ATOM   2456 C  C   . PHE A 1 328 ? 112.834 7.117   21.470  1.00 153.97 ? 327 PHE A C   1 
ATOM   2457 O  O   . PHE A 1 328 ? 111.807 6.664   20.958  1.00 148.82 ? 327 PHE A O   1 
ATOM   2458 C  CB  . PHE A 1 328 ? 113.581 9.077   19.978  1.00 156.52 ? 327 PHE A CB  1 
ATOM   2459 C  CG  . PHE A 1 328 ? 112.610 8.997   18.837  1.00 158.25 ? 327 PHE A CG  1 
ATOM   2460 C  CD1 . PHE A 1 328 ? 111.263 8.829   19.053  1.00 160.75 ? 327 PHE A CD1 1 
ATOM   2461 C  CD2 . PHE A 1 328 ? 113.057 9.156   17.535  1.00 159.71 ? 327 PHE A CD2 1 
ATOM   2462 C  CE1 . PHE A 1 328 ? 110.380 8.771   17.996  1.00 165.31 ? 327 PHE A CE1 1 
ATOM   2463 C  CE2 . PHE A 1 328 ? 112.178 9.108   16.474  1.00 158.06 ? 327 PHE A CE2 1 
ATOM   2464 C  CZ  . PHE A 1 328 ? 110.835 8.916   16.708  1.00 160.60 ? 327 PHE A CZ  1 
ATOM   2465 N  N   . THR A 1 329 ? 113.093 7.082   22.777  1.00 149.96 ? 328 THR A N   1 
ATOM   2466 C  CA  . THR A 1 329 ? 112.272 6.419   23.784  1.00 137.75 ? 328 THR A CA  1 
ATOM   2467 C  C   . THR A 1 329 ? 112.051 7.280   25.021  1.00 128.11 ? 328 THR A C   1 
ATOM   2468 O  O   . THR A 1 329 ? 111.551 6.773   26.033  1.00 121.86 ? 328 THR A O   1 
ATOM   2469 C  CB  . THR A 1 329 ? 112.876 5.084   24.181  1.00 137.76 ? 328 THR A CB  1 
ATOM   2470 O  OG1 . THR A 1 329 ? 114.205 5.312   24.633  1.00 142.15 ? 328 THR A OG1 1 
ATOM   2471 C  CG2 . THR A 1 329 ? 112.905 4.133   22.996  1.00 134.19 ? 328 THR A CG2 1 
ATOM   2472 N  N   . ALA A 1 330 ? 112.375 8.560   24.959  1.00 124.61 ? 329 ALA A N   1 
ATOM   2473 C  CA  . ALA A 1 330 ? 112.125 9.489   26.046  1.00 115.16 ? 329 ALA A CA  1 
ATOM   2474 C  C   . ALA A 1 330 ? 110.805 10.211  25.867  1.00 104.53 ? 329 ALA A C   1 
ATOM   2475 O  O   . ALA A 1 330 ? 110.412 10.992  26.740  1.00 95.12  ? 329 ALA A O   1 
ATOM   2476 C  CB  . ALA A 1 330 ? 113.265 10.501  26.156  1.00 107.31 ? 329 ALA A CB  1 
ATOM   2477 N  N   . MET A 1 331 ? 110.119 9.979   24.748  1.00 101.75 ? 330 MET A N   1 
ATOM   2478 C  CA  . MET A 1 331 ? 108.830 10.617  24.537  1.00 97.78  ? 330 MET A CA  1 
ATOM   2479 C  C   . MET A 1 331 ? 107.771 10.052  25.469  1.00 83.81  ? 330 MET A C   1 
ATOM   2480 O  O   . MET A 1 331 ? 106.644 10.553  25.463  1.00 84.51  ? 330 MET A O   1 
ATOM   2481 C  CB  . MET A 1 331 ? 108.317 10.384  23.128  1.00 103.66 ? 330 MET A CB  1 
ATOM   2482 C  CG  . MET A 1 331 ? 109.070 11.016  22.010  1.00 111.92 ? 330 MET A CG  1 
ATOM   2483 S  SD  . MET A 1 331 ? 108.658 10.062  20.544  1.00 129.04 ? 330 MET A SD  1 
ATOM   2484 C  CE  . MET A 1 331 ? 108.640 8.390   21.220  1.00 124.68 ? 330 MET A CE  1 
ATOM   2485 N  N   . ARG A 1 332 ? 108.090 9.004   26.236  1.00 83.96  ? 331 ARG A N   1 
ATOM   2486 C  CA  . ARG A 1 332 ? 107.090 8.396   27.104  1.00 78.58  ? 331 ARG A CA  1 
ATOM   2487 C  C   . ARG A 1 332 ? 106.580 9.421   28.104  1.00 75.14  ? 331 ARG A C   1 
ATOM   2488 O  O   . ARG A 1 332 ? 105.397 9.422   28.464  1.00 74.14  ? 331 ARG A O   1 
ATOM   2489 C  CB  . ARG A 1 332 ? 107.679 7.179   27.812  1.00 80.41  ? 331 ARG A CB  1 
ATOM   2490 C  CG  . ARG A 1 332 ? 108.968 7.470   28.547  1.00 84.33  ? 331 ARG A CG  1 
ATOM   2491 C  CD  . ARG A 1 332 ? 109.696 6.185   28.879  1.00 75.73  ? 331 ARG A CD  1 
ATOM   2492 N  NE  . ARG A 1 332 ? 108.803 5.193   29.466  1.00 74.36  ? 331 ARG A NE  1 
ATOM   2493 C  CZ  . ARG A 1 332 ? 108.633 5.021   30.769  1.00 69.02  ? 331 ARG A CZ  1 
ATOM   2494 N  NH1 . ARG A 1 332 ? 109.281 5.763   31.653  1.00 70.89  ? 331 ARG A NH1 1 
ATOM   2495 N  NH2 . ARG A 1 332 ? 107.793 4.083   31.197  1.00 69.03  ? 331 ARG A NH2 1 
ATOM   2496 N  N   . ASP A 1 333 ? 107.468 10.304  28.560  1.00 80.75  ? 332 ASP A N   1 
ATOM   2497 C  CA  . ASP A 1 333 ? 107.086 11.346  29.496  1.00 80.69  ? 332 ASP A CA  1 
ATOM   2498 C  C   . ASP A 1 333 ? 106.169 12.367  28.836  1.00 76.07  ? 332 ASP A C   1 
ATOM   2499 O  O   . ASP A 1 333 ? 105.439 13.077  29.537  1.00 70.00  ? 332 ASP A O   1 
ATOM   2500 C  CB  . ASP A 1 333 ? 108.339 12.035  30.035  1.00 80.95  ? 332 ASP A CB  1 
ATOM   2501 C  CG  . ASP A 1 333 ? 109.270 11.073  30.746  1.00 90.07  ? 332 ASP A CG  1 
ATOM   2502 O  OD1 . ASP A 1 333 ? 108.776 10.215  31.509  1.00 83.24  ? 332 ASP A OD1 1 
ATOM   2503 O  OD2 . ASP A 1 333 ? 110.497 11.166  30.530  1.00 94.27  ? 332 ASP A OD2 1 
ATOM   2504 N  N   . LEU A 1 334 ? 106.199 12.459  27.503  1.00 75.44  ? 333 LEU A N   1 
ATOM   2505 C  CA  . LEU A 1 334 ? 105.334 13.369  26.766  1.00 74.33  ? 333 LEU A CA  1 
ATOM   2506 C  C   . LEU A 1 334 ? 103.933 12.813  26.544  1.00 68.86  ? 333 LEU A C   1 
ATOM   2507 O  O   . LEU A 1 334 ? 103.036 13.581  26.179  1.00 70.22  ? 333 LEU A O   1 
ATOM   2508 C  CB  . LEU A 1 334 ? 105.962 13.696  25.408  1.00 71.58  ? 333 LEU A CB  1 
ATOM   2509 C  CG  . LEU A 1 334 ? 106.869 14.921  25.283  1.00 71.25  ? 333 LEU A CG  1 
ATOM   2510 C  CD1 . LEU A 1 334 ? 108.187 14.678  25.999  1.00 72.07  ? 333 LEU A CD1 1 
ATOM   2511 C  CD2 . LEU A 1 334 ? 107.109 15.250  23.818  1.00 73.88  ? 333 LEU A CD2 1 
ATOM   2512 N  N   . PHE A 1 335 ? 103.724 11.509  26.747  1.00 67.98  ? 334 PHE A N   1 
ATOM   2513 C  CA  . PHE A 1 335 ? 102.450 10.897  26.376  1.00 66.29  ? 334 PHE A CA  1 
ATOM   2514 C  C   . PHE A 1 335 ? 101.313 11.443  27.229  1.00 59.15  ? 334 PHE A C   1 
ATOM   2515 O  O   . PHE A 1 335 ? 100.248 11.795  26.709  1.00 58.31  ? 334 PHE A O   1 
ATOM   2516 C  CB  . PHE A 1 335 ? 102.527 9.373   26.488  1.00 66.78  ? 334 PHE A CB  1 
ATOM   2517 C  CG  . PHE A 1 335 ? 102.911 8.687   25.205  1.00 67.85  ? 334 PHE A CG  1 
ATOM   2518 C  CD1 . PHE A 1 335 ? 104.069 9.036   24.530  1.00 70.01  ? 334 PHE A CD1 1 
ATOM   2519 C  CD2 . PHE A 1 335 ? 102.096 7.707   24.660  1.00 65.73  ? 334 PHE A CD2 1 
ATOM   2520 C  CE1 . PHE A 1 335 ? 104.417 8.406   23.348  1.00 72.25  ? 334 PHE A CE1 1 
ATOM   2521 C  CE2 . PHE A 1 335 ? 102.437 7.074   23.479  1.00 64.11  ? 334 PHE A CE2 1 
ATOM   2522 C  CZ  . PHE A 1 335 ? 103.598 7.425   22.821  1.00 67.99  ? 334 PHE A CZ  1 
ATOM   2523 N  N   . ALA A 1 336 ? 101.523 11.502  28.546  1.00 62.70  ? 335 ALA A N   1 
ATOM   2524 C  CA  . ALA A 1 336 ? 100.471 11.910  29.473  1.00 56.57  ? 335 ALA A CA  1 
ATOM   2525 C  C   . ALA A 1 336 ? 99.913  13.279  29.104  1.00 57.41  ? 335 ALA A C   1 
ATOM   2526 O  O   . ALA A 1 336 ? 98.704  13.438  28.899  1.00 61.55  ? 335 ALA A O   1 
ATOM   2527 C  CB  . ALA A 1 336 ? 101.009 11.910  30.904  1.00 51.93  ? 335 ALA A CB  1 
ATOM   2528 N  N   . TRP A 1 337 ? 100.785 14.287  29.036  1.00 52.60  ? 336 TRP A N   1 
ATOM   2529 C  CA  . TRP A 1 337 ? 100.349 15.634  28.682  1.00 53.83  ? 336 TRP A CA  1 
ATOM   2530 C  C   . TRP A 1 337 ? 99.640  15.649  27.331  1.00 55.54  ? 336 TRP A C   1 
ATOM   2531 O  O   . TRP A 1 337 ? 98.543  16.204  27.199  1.00 56.16  ? 336 TRP A O   1 
ATOM   2532 C  CB  . TRP A 1 337 ? 101.550 16.581  28.678  1.00 59.38  ? 336 TRP A CB  1 
ATOM   2533 C  CG  . TRP A 1 337 ? 102.355 16.525  29.945  1.00 65.15  ? 336 TRP A CG  1 
ATOM   2534 C  CD1 . TRP A 1 337 ? 103.384 15.672  30.223  1.00 65.26  ? 336 TRP A CD1 1 
ATOM   2535 C  CD2 . TRP A 1 337 ? 102.195 17.351  31.105  1.00 61.82  ? 336 TRP A CD2 1 
ATOM   2536 N  NE1 . TRP A 1 337 ? 103.875 15.917  31.482  1.00 63.30  ? 336 TRP A NE1 1 
ATOM   2537 C  CE2 . TRP A 1 337 ? 103.163 16.942  32.045  1.00 62.51  ? 336 TRP A CE2 1 
ATOM   2538 C  CE3 . TRP A 1 337 ? 101.330 18.396  31.441  1.00 60.86  ? 336 TRP A CE3 1 
ATOM   2539 C  CZ2 . TRP A 1 337 ? 103.288 17.542  33.296  1.00 59.75  ? 336 TRP A CZ2 1 
ATOM   2540 C  CZ3 . TRP A 1 337 ? 101.456 18.990  32.684  1.00 58.23  ? 336 TRP A CZ3 1 
ATOM   2541 C  CH2 . TRP A 1 337 ? 102.428 18.561  33.596  1.00 61.66  ? 336 TRP A CH2 1 
ATOM   2542 N  N   . GLN A 1 338 ? 100.259 15.047  26.310  1.00 54.09  ? 337 GLN A N   1 
ATOM   2543 C  CA  . GLN A 1 338 ? 99.671  15.044  24.972  1.00 58.15  ? 337 GLN A CA  1 
ATOM   2544 C  C   . GLN A 1 338 ? 98.308  14.360  24.955  1.00 59.29  ? 337 GLN A C   1 
ATOM   2545 O  O   . GLN A 1 338 ? 97.372  14.840  24.305  1.00 56.16  ? 337 GLN A O   1 
ATOM   2546 C  CB  . GLN A 1 338 ? 100.618 14.360  23.986  1.00 58.51  ? 337 GLN A CB  1 
ATOM   2547 C  CG  . GLN A 1 338 ? 100.187 14.463  22.532  1.00 59.73  ? 337 GLN A CG  1 
ATOM   2548 C  CD  . GLN A 1 338 ? 100.629 15.760  21.885  1.00 67.86  ? 337 GLN A CD  1 
ATOM   2549 O  OE1 . GLN A 1 338 ? 101.422 16.512  22.453  1.00 71.48  ? 337 GLN A OE1 1 
ATOM   2550 N  NE2 . GLN A 1 338 ? 100.119 16.029  20.689  1.00 69.80  ? 337 GLN A NE2 1 
ATOM   2551 N  N   . LEU A 1 339 ? 98.177  13.235  25.663  1.00 56.64  ? 338 LEU A N   1 
ATOM   2552 C  CA  . LEU A 1 339 ? 96.923  12.487  25.645  1.00 54.97  ? 338 LEU A CA  1 
ATOM   2553 C  C   . LEU A 1 339 ? 95.800  13.259  26.328  1.00 54.61  ? 338 LEU A C   1 
ATOM   2554 O  O   . LEU A 1 339 ? 94.643  13.190  25.895  1.00 53.21  ? 338 LEU A O   1 
ATOM   2555 C  CB  . LEU A 1 339 ? 97.117  11.117  26.293  1.00 57.59  ? 338 LEU A CB  1 
ATOM   2556 C  CG  . LEU A 1 339 ? 97.804  10.099  25.380  1.00 53.18  ? 338 LEU A CG  1 
ATOM   2557 C  CD1 . LEU A 1 339 ? 98.153  8.832   26.133  1.00 51.34  ? 338 LEU A CD1 1 
ATOM   2558 C  CD2 . LEU A 1 339 ? 96.920  9.786   24.182  1.00 53.65  ? 338 LEU A CD2 1 
ATOM   2559 N  N   . VAL A 1 340 ? 96.117  13.988  27.400  1.00 57.85  ? 339 VAL A N   1 
ATOM   2560 C  CA  . VAL A 1 340 ? 95.114  14.834  28.044  1.00 58.82  ? 339 VAL A CA  1 
ATOM   2561 C  C   . VAL A 1 340 ? 94.635  15.910  27.078  1.00 55.42  ? 339 VAL A C   1 
ATOM   2562 O  O   . VAL A 1 340 ? 93.430  16.144  26.927  1.00 52.68  ? 339 VAL A O   1 
ATOM   2563 C  CB  . VAL A 1 340 ? 95.681  15.447  29.337  1.00 60.21  ? 339 VAL A CB  1 
ATOM   2564 C  CG1 . VAL A 1 340 ? 94.760  16.541  29.851  1.00 58.50  ? 339 VAL A CG1 1 
ATOM   2565 C  CG2 . VAL A 1 340 ? 95.877  14.373  30.394  1.00 54.16  ? 339 VAL A CG2 1 
ATOM   2566 N  N   . GLY A 1 341 ? 95.576  16.588  26.419  1.00 54.37  ? 340 GLY A N   1 
ATOM   2567 C  CA  . GLY A 1 341 ? 95.207  17.558  25.401  1.00 56.32  ? 340 GLY A CA  1 
ATOM   2568 C  C   . GLY A 1 341 ? 94.363  16.961  24.291  1.00 59.99  ? 340 GLY A C   1 
ATOM   2569 O  O   . GLY A 1 341 ? 93.469  17.620  23.755  1.00 54.89  ? 340 GLY A O   1 
ATOM   2570 N  N   . ASP A 1 342 ? 94.643  15.707  23.922  1.00 58.62  ? 341 ASP A N   1 
ATOM   2571 C  CA  . ASP A 1 342 ? 93.864  15.053  22.874  1.00 52.98  ? 341 ASP A CA  1 
ATOM   2572 C  C   . ASP A 1 342 ? 92.416  14.842  23.298  1.00 54.00  ? 341 ASP A C   1 
ATOM   2573 O  O   . ASP A 1 342 ? 91.497  15.012  22.489  1.00 56.73  ? 341 ASP A O   1 
ATOM   2574 C  CB  . ASP A 1 342 ? 94.504  13.718  22.497  1.00 50.85  ? 341 ASP A CB  1 
ATOM   2575 C  CG  . ASP A 1 342 ? 95.735  13.885  21.633  1.00 61.35  ? 341 ASP A CG  1 
ATOM   2576 O  OD1 . ASP A 1 342 ? 95.979  15.012  21.155  1.00 65.43  ? 341 ASP A OD1 1 
ATOM   2577 O  OD2 . ASP A 1 342 ? 96.454  12.885  21.424  1.00 66.02  ? 341 ASP A OD2 1 
ATOM   2578 N  N   . VAL A 1 343 ? 92.194  14.464  24.559  1.00 53.42  ? 342 VAL A N   1 
ATOM   2579 C  CA  . VAL A 1 343 ? 90.833  14.242  25.045  1.00 55.29  ? 342 VAL A CA  1 
ATOM   2580 C  C   . VAL A 1 343 ? 90.016  15.523  24.936  1.00 51.61  ? 342 VAL A C   1 
ATOM   2581 O  O   . VAL A 1 343 ? 88.897  15.527  24.407  1.00 49.57  ? 342 VAL A O   1 
ATOM   2582 C  CB  . VAL A 1 343 ? 90.859  13.713  26.490  1.00 52.16  ? 342 VAL A CB  1 
ATOM   2583 C  CG1 . VAL A 1 343 ? 89.476  13.812  27.116  1.00 46.10  ? 342 VAL A CG1 1 
ATOM   2584 C  CG2 . VAL A 1 343 ? 91.364  12.280  26.522  1.00 47.84  ? 342 VAL A CG2 1 
ATOM   2585 N  N   . LEU A 1 344 ? 90.569  16.633  25.427  1.00 48.98  ? 343 LEU A N   1 
ATOM   2586 C  CA  . LEU A 1 344 ? 89.868  17.909  25.349  1.00 51.21  ? 343 LEU A CA  1 
ATOM   2587 C  C   . LEU A 1 344 ? 89.758  18.410  23.914  1.00 51.36  ? 343 LEU A C   1 
ATOM   2588 O  O   . LEU A 1 344 ? 88.795  19.110  23.579  1.00 50.36  ? 343 LEU A O   1 
ATOM   2589 C  CB  . LEU A 1 344 ? 90.568  18.935  26.235  1.00 48.26  ? 343 LEU A CB  1 
ATOM   2590 C  CG  . LEU A 1 344 ? 90.238  18.742  27.716  1.00 51.57  ? 343 LEU A CG  1 
ATOM   2591 C  CD1 . LEU A 1 344 ? 91.478  18.894  28.570  1.00 54.88  ? 343 LEU A CD1 1 
ATOM   2592 C  CD2 . LEU A 1 344 ? 89.154  19.711  28.163  1.00 53.57  ? 343 LEU A CD2 1 
ATOM   2593 N  N   . LYS A 1 345 ? 90.727  18.076  23.058  1.00 54.84  ? 344 LYS A N   1 
ATOM   2594 C  CA  . LYS A 1 345 ? 90.631  18.478  21.659  1.00 51.12  ? 344 LYS A CA  1 
ATOM   2595 C  C   . LYS A 1 345 ? 89.492  17.747  20.962  1.00 49.42  ? 344 LYS A C   1 
ATOM   2596 O  O   . LYS A 1 345 ? 88.783  18.333  20.135  1.00 50.79  ? 344 LYS A O   1 
ATOM   2597 C  CB  . LYS A 1 345 ? 91.955  18.215  20.940  1.00 47.69  ? 344 LYS A CB  1 
ATOM   2598 C  CG  . LYS A 1 345 ? 92.011  18.765  19.524  1.00 51.34  ? 344 LYS A CG  1 
ATOM   2599 C  CD  . LYS A 1 345 ? 93.445  18.935  19.057  1.00 52.90  ? 344 LYS A CD  1 
ATOM   2600 C  CE  . LYS A 1 345 ? 93.513  19.341  17.595  1.00 57.57  ? 344 LYS A CE  1 
ATOM   2601 N  NZ  . LYS A 1 345 ? 94.882  19.157  17.038  1.00 64.90  ? 344 LYS A NZ  1 
ATOM   2602 N  N   . VAL A 1 346 ? 89.309  16.463  21.279  1.00 46.78  ? 345 VAL A N   1 
ATOM   2603 C  CA  . VAL A 1 346 ? 88.169  15.712  20.759  1.00 49.22  ? 345 VAL A CA  1 
ATOM   2604 C  C   . VAL A 1 346 ? 86.863  16.361  21.196  1.00 49.96  ? 345 VAL A C   1 
ATOM   2605 O  O   . VAL A 1 346 ? 85.932  16.520  20.396  1.00 50.12  ? 345 VAL A O   1 
ATOM   2606 C  CB  . VAL A 1 346 ? 88.249  14.241  21.208  1.00 46.82  ? 345 VAL A CB  1 
ATOM   2607 C  CG1 . VAL A 1 346 ? 86.920  13.553  20.987  1.00 51.06  ? 345 VAL A CG1 1 
ATOM   2608 C  CG2 . VAL A 1 346 ? 89.349  13.514  20.460  1.00 49.66  ? 345 VAL A CG2 1 
ATOM   2609 N  N   . GLY A 1 347 ? 86.774  16.747  22.471  1.00 48.39  ? 346 GLY A N   1 
ATOM   2610 C  CA  . GLY A 1 347 ? 85.614  17.493  22.931  1.00 47.88  ? 346 GLY A CA  1 
ATOM   2611 C  C   . GLY A 1 347 ? 85.421  18.790  22.170  1.00 46.15  ? 346 GLY A C   1 
ATOM   2612 O  O   . GLY A 1 347 ? 84.291  19.182  21.870  1.00 46.29  ? 346 GLY A O   1 
ATOM   2613 N  N   . ALA A 1 348 ? 86.520  19.479  21.855  1.00 44.55  ? 347 ALA A N   1 
ATOM   2614 C  CA  . ALA A 1 348 ? 86.427  20.714  21.090  1.00 46.03  ? 347 ALA A CA  1 
ATOM   2615 C  C   . ALA A 1 348 ? 86.038  20.460  19.639  1.00 47.24  ? 347 ALA A C   1 
ATOM   2616 O  O   . ALA A 1 348 ? 85.476  21.353  18.996  1.00 50.53  ? 347 ALA A O   1 
ATOM   2617 C  CB  . ALA A 1 348 ? 87.751  21.475  21.154  1.00 52.89  ? 347 ALA A CB  1 
ATOM   2618 N  N   . TYR A 1 349 ? 86.319  19.264  19.114  1.00 46.04  ? 348 TYR A N   1 
ATOM   2619 C  CA  . TYR A 1 349 ? 85.907  18.935  17.753  1.00 48.34  ? 348 TYR A CA  1 
ATOM   2620 C  C   . TYR A 1 349 ? 84.391  18.911  17.617  1.00 48.07  ? 348 TYR A C   1 
ATOM   2621 O  O   . TYR A 1 349 ? 83.862  19.218  16.542  1.00 51.05  ? 348 TYR A O   1 
ATOM   2622 C  CB  . TYR A 1 349 ? 86.490  17.585  17.335  1.00 49.52  ? 348 TYR A CB  1 
ATOM   2623 C  CG  . TYR A 1 349 ? 87.879  17.649  16.741  1.00 47.89  ? 348 TYR A CG  1 
ATOM   2624 C  CD1 . TYR A 1 349 ? 88.706  18.743  16.960  1.00 49.07  ? 348 TYR A CD1 1 
ATOM   2625 C  CD2 . TYR A 1 349 ? 88.364  16.608  15.959  1.00 49.36  ? 348 TYR A CD2 1 
ATOM   2626 C  CE1 . TYR A 1 349 ? 89.976  18.800  16.412  1.00 49.70  ? 348 TYR A CE1 1 
ATOM   2627 C  CE2 . TYR A 1 349 ? 89.631  16.655  15.411  1.00 51.14  ? 348 TYR A CE2 1 
ATOM   2628 C  CZ  . TYR A 1 349 ? 90.433  17.752  15.639  1.00 56.58  ? 348 TYR A CZ  1 
ATOM   2629 O  OH  . TYR A 1 349 ? 91.696  17.799  15.096  1.00 60.99  ? 348 TYR A OH  1 
ATOM   2630 N  N   . VAL A 1 350 ? 83.681  18.532  18.683  1.00 44.29  ? 349 VAL A N   1 
ATOM   2631 C  CA  . VAL A 1 350 ? 82.221  18.486  18.635  1.00 48.42  ? 349 VAL A CA  1 
ATOM   2632 C  C   . VAL A 1 350 ? 81.657  19.863  18.308  1.00 47.75  ? 349 VAL A C   1 
ATOM   2633 O  O   . VAL A 1 350 ? 80.763  20.006  17.466  1.00 44.03  ? 349 VAL A O   1 
ATOM   2634 C  CB  . VAL A 1 350 ? 81.659  17.945  19.962  1.00 45.25  ? 349 VAL A CB  1 
ATOM   2635 C  CG1 . VAL A 1 350 ? 80.141  18.046  19.978  1.00 45.58  ? 349 VAL A CG1 1 
ATOM   2636 C  CG2 . VAL A 1 350 ? 82.107  16.508  20.180  1.00 39.85  ? 349 VAL A CG2 1 
ATOM   2637 N  N   . PHE A 1 351 ? 82.175  20.900  18.970  1.00 48.59  ? 350 PHE A N   1 
ATOM   2638 C  CA  . PHE A 1 351 ? 81.778  22.262  18.632  1.00 48.60  ? 350 PHE A CA  1 
ATOM   2639 C  C   . PHE A 1 351 ? 82.289  22.673  17.257  1.00 48.96  ? 350 PHE A C   1 
ATOM   2640 O  O   . PHE A 1 351 ? 81.611  23.423  16.545  1.00 48.94  ? 350 PHE A O   1 
ATOM   2641 C  CB  . PHE A 1 351 ? 82.277  23.237  19.699  1.00 50.38  ? 350 PHE A CB  1 
ATOM   2642 C  CG  . PHE A 1 351 ? 81.753  22.949  21.078  1.00 50.38  ? 350 PHE A CG  1 
ATOM   2643 C  CD1 . PHE A 1 351 ? 80.461  23.303  21.434  1.00 49.27  ? 350 PHE A CD1 1 
ATOM   2644 C  CD2 . PHE A 1 351 ? 82.557  22.331  22.023  1.00 50.22  ? 350 PHE A CD2 1 
ATOM   2645 C  CE1 . PHE A 1 351 ? 79.980  23.040  22.704  1.00 47.92  ? 350 PHE A CE1 1 
ATOM   2646 C  CE2 . PHE A 1 351 ? 82.081  22.067  23.294  1.00 49.41  ? 350 PHE A CE2 1 
ATOM   2647 C  CZ  . PHE A 1 351 ? 80.792  22.422  23.635  1.00 40.40  ? 350 PHE A CZ  1 
ATOM   2648 N  N   . GLY A 1 352 ? 83.477  22.203  16.871  1.00 45.86  ? 351 GLY A N   1 
ATOM   2649 C  CA  . GLY A 1 352 ? 84.019  22.570  15.572  1.00 44.11  ? 351 GLY A CA  1 
ATOM   2650 C  C   . GLY A 1 352 ? 83.194  22.044  14.413  1.00 44.70  ? 351 GLY A C   1 
ATOM   2651 O  O   . GLY A 1 352 ? 82.982  22.746  13.422  1.00 44.41  ? 351 GLY A O   1 
ATOM   2652 N  N   . TYR A 1 353 ? 82.708  20.805  14.524  1.00 45.83  ? 352 TYR A N   1 
ATOM   2653 C  CA  . TYR A 1 353 ? 81.871  20.246  13.467  1.00 42.02  ? 352 TYR A CA  1 
ATOM   2654 C  C   . TYR A 1 353 ? 80.503  20.913  13.417  1.00 45.41  ? 352 TYR A C   1 
ATOM   2655 O  O   . TYR A 1 353 ? 79.860  20.922  12.361  1.00 46.16  ? 352 TYR A O   1 
ATOM   2656 C  CB  . TYR A 1 353 ? 81.733  18.735  13.646  1.00 44.58  ? 352 TYR A CB  1 
ATOM   2657 C  CG  . TYR A 1 353 ? 82.850  17.959  12.989  1.00 43.23  ? 352 TYR A CG  1 
ATOM   2658 C  CD1 . TYR A 1 353 ? 84.037  17.706  13.663  1.00 45.08  ? 352 TYR A CD1 1 
ATOM   2659 C  CD2 . TYR A 1 353 ? 82.721  17.487  11.689  1.00 45.42  ? 352 TYR A CD2 1 
ATOM   2660 C  CE1 . TYR A 1 353 ? 85.064  17.001  13.061  1.00 49.75  ? 352 TYR A CE1 1 
ATOM   2661 C  CE2 . TYR A 1 353 ? 83.742  16.781  11.079  1.00 48.75  ? 352 TYR A CE2 1 
ATOM   2662 C  CZ  . TYR A 1 353 ? 84.911  16.541  11.770  1.00 48.59  ? 352 TYR A CZ  1 
ATOM   2663 O  OH  . TYR A 1 353 ? 85.930  15.838  11.168  1.00 48.04  ? 352 TYR A OH  1 
ATOM   2664 N  N   . LEU A 1 354 ? 80.040  21.465  14.540  1.00 43.34  ? 353 LEU A N   1 
ATOM   2665 C  CA  . LEU A 1 354 ? 78.832  22.284  14.519  1.00 43.94  ? 353 LEU A CA  1 
ATOM   2666 C  C   . LEU A 1 354 ? 79.026  23.506  13.628  1.00 46.27  ? 353 LEU A C   1 
ATOM   2667 O  O   . LEU A 1 354 ? 78.151  23.849  12.824  1.00 44.25  ? 353 LEU A O   1 
ATOM   2668 C  CB  . LEU A 1 354 ? 78.455  22.699  15.943  1.00 43.60  ? 353 LEU A CB  1 
ATOM   2669 C  CG  . LEU A 1 354 ? 77.347  23.743  16.109  1.00 42.36  ? 353 LEU A CG  1 
ATOM   2670 C  CD1 . LEU A 1 354 ? 76.078  23.312  15.384  1.00 41.78  ? 353 LEU A CD1 1 
ATOM   2671 C  CD2 . LEU A 1 354 ? 77.067  24.010  17.583  1.00 45.01  ? 353 LEU A CD2 1 
ATOM   2672 N  N   . VAL A 1 355 ? 80.170  24.182  13.770  1.00 43.06  ? 354 VAL A N   1 
ATOM   2673 C  CA  . VAL A 1 355 ? 80.491  25.315  12.906  1.00 48.67  ? 354 VAL A CA  1 
ATOM   2674 C  C   . VAL A 1 355 ? 80.509  24.886  11.443  1.00 47.93  ? 354 VAL A C   1 
ATOM   2675 O  O   . VAL A 1 355 ? 79.985  25.588  10.568  1.00 48.30  ? 354 VAL A O   1 
ATOM   2676 C  CB  . VAL A 1 355 ? 81.833  25.941  13.331  1.00 47.60  ? 354 VAL A CB  1 
ATOM   2677 C  CG1 . VAL A 1 355 ? 82.323  26.924  12.283  1.00 40.64  ? 354 VAL A CG1 1 
ATOM   2678 C  CG2 . VAL A 1 355 ? 81.696  26.621  14.686  1.00 55.42  ? 354 VAL A CG2 1 
ATOM   2679 N  N   . ILE A 1 356 ? 81.118  23.732  11.153  1.00 43.71  ? 355 ILE A N   1 
ATOM   2680 C  CA  . ILE A 1 356 ? 81.085  23.185  9.797   1.00 43.76  ? 355 ILE A CA  1 
ATOM   2681 C  C   . ILE A 1 356 ? 79.647  22.938  9.359   1.00 46.48  ? 355 ILE A C   1 
ATOM   2682 O  O   . ILE A 1 356 ? 79.251  23.280  8.238   1.00 45.88  ? 355 ILE A O   1 
ATOM   2683 C  CB  . ILE A 1 356 ? 81.922  21.896  9.715   1.00 47.27  ? 355 ILE A CB  1 
ATOM   2684 C  CG1 . ILE A 1 356 ? 83.308  22.109  10.322  1.00 48.16  ? 355 ILE A CG1 1 
ATOM   2685 C  CG2 . ILE A 1 356 ? 82.022  21.414  8.274   1.00 40.30  ? 355 ILE A CG2 1 
ATOM   2686 C  CD1 . ILE A 1 356 ? 84.291  22.724  9.369   1.00 49.86  ? 355 ILE A CD1 1 
ATOM   2687 N  N   . ALA A 1 357 ? 78.847  22.330  10.239  1.00 42.89  ? 356 ALA A N   1 
ATOM   2688 C  CA  . ALA A 1 357 ? 77.478  21.974  9.882   1.00 43.51  ? 356 ALA A CA  1 
ATOM   2689 C  C   . ALA A 1 357 ? 76.629  23.202  9.590   1.00 46.34  ? 356 ALA A C   1 
ATOM   2690 O  O   . ALA A 1 357 ? 75.677  23.125  8.805   1.00 47.30  ? 356 ALA A O   1 
ATOM   2691 C  CB  . ALA A 1 357 ? 76.844  21.146  10.997  1.00 45.42  ? 356 ALA A CB  1 
ATOM   2692 N  N   . LYS A 1 358 ? 76.949  24.336  10.206  1.00 48.67  ? 357 LYS A N   1 
ATOM   2693 C  CA  . LYS A 1 358 ? 76.246  25.582  9.938   1.00 46.38  ? 357 LYS A CA  1 
ATOM   2694 C  C   . LYS A 1 358 ? 76.941  26.429  8.880   1.00 46.08  ? 357 LYS A C   1 
ATOM   2695 O  O   . LYS A 1 358 ? 76.492  27.549  8.613   1.00 44.73  ? 357 LYS A O   1 
ATOM   2696 C  CB  . LYS A 1 358 ? 76.101  26.391  11.231  1.00 41.92  ? 357 LYS A CB  1 
ATOM   2697 C  CG  . LYS A 1 358 ? 75.093  25.819  12.219  1.00 45.01  ? 357 LYS A CG  1 
ATOM   2698 C  CD  . LYS A 1 358 ? 73.767  25.486  11.552  1.00 52.69  ? 357 LYS A CD  1 
ATOM   2699 C  CE  . LYS A 1 358 ? 73.347  24.053  11.845  1.00 47.83  ? 357 LYS A CE  1 
ATOM   2700 N  NZ  . LYS A 1 358 ? 72.107  23.662  11.116  1.00 45.71  ? 357 LYS A NZ  1 
ATOM   2701 N  N   . ALA A 1 359 ? 78.016  25.915  8.276   1.00 42.49  ? 358 ALA A N   1 
ATOM   2702 C  CA  . ALA A 1 359 ? 78.771  26.619  7.236   1.00 46.35  ? 358 ALA A CA  1 
ATOM   2703 C  C   . ALA A 1 359 ? 79.192  28.018  7.681   1.00 50.81  ? 358 ALA A C   1 
ATOM   2704 O  O   . ALA A 1 359 ? 79.332  28.929  6.862   1.00 51.13  ? 358 ALA A O   1 
ATOM   2705 C  CB  . ALA A 1 359 ? 77.976  26.689  5.929   1.00 47.27  ? 358 ALA A CB  1 
ATOM   2706 N  N   . SER A 1 360 ? 79.407  28.201  8.982   1.00 44.46  ? 359 SER A N   1 
ATOM   2707 C  CA  . SER A 1 360 ? 79.764  29.513  9.514   1.00 37.56  ? 359 SER A CA  1 
ATOM   2708 C  C   . SER A 1 360 ? 81.245  29.747  9.255   1.00 46.14  ? 359 SER A C   1 
ATOM   2709 O  O   . SER A 1 360 ? 82.103  29.309  10.024  1.00 50.95  ? 359 SER A O   1 
ATOM   2710 C  CB  . SER A 1 360 ? 79.439  29.602  11.000  1.00 44.79  ? 359 SER A CB  1 
ATOM   2711 O  OG  . SER A 1 360 ? 79.875  30.838  11.539  1.00 49.38  ? 359 SER A OG  1 
ATOM   2712 N  N   . LEU A 1 361 ? 81.546  30.445  8.158   1.00 48.82  ? 360 LEU A N   1 
ATOM   2713 C  CA  . LEU A 1 361 ? 82.922  30.840  7.883   1.00 52.60  ? 360 LEU A CA  1 
ATOM   2714 C  C   . LEU A 1 361 ? 83.478  31.748  8.972   1.00 52.94  ? 360 LEU A C   1 
ATOM   2715 O  O   . LEU A 1 361 ? 84.671  31.674  9.290   1.00 52.91  ? 360 LEU A O   1 
ATOM   2716 C  CB  . LEU A 1 361 ? 83.003  31.524  6.518   1.00 50.49  ? 360 LEU A CB  1 
ATOM   2717 C  CG  . LEU A 1 361 ? 84.395  31.848  5.971   1.00 50.91  ? 360 LEU A CG  1 
ATOM   2718 C  CD1 . LEU A 1 361 ? 85.359  30.701  6.217   1.00 49.71  ? 360 LEU A CD1 1 
ATOM   2719 C  CD2 . LEU A 1 361 ? 84.316  32.170  4.488   1.00 46.75  ? 360 LEU A CD2 1 
ATOM   2720 N  N   . ARG A 1 362 ? 82.639  32.609  9.552   1.00 46.28  ? 361 ARG A N   1 
ATOM   2721 C  CA  . ARG A 1 362 ? 83.132  33.553  10.550  1.00 51.07  ? 361 ARG A CA  1 
ATOM   2722 C  C   . ARG A 1 362 ? 83.525  32.846  11.844  1.00 53.30  ? 361 ARG A C   1 
ATOM   2723 O  O   . ARG A 1 362 ? 84.578  33.144  12.419  1.00 53.83  ? 361 ARG A O   1 
ATOM   2724 C  CB  . ARG A 1 362 ? 82.091  34.647  10.802  1.00 50.82  ? 361 ARG A CB  1 
ATOM   2725 C  CG  . ARG A 1 362 ? 80.771  34.175  11.388  1.00 47.15  ? 361 ARG A CG  1 
ATOM   2726 C  CD  . ARG A 1 362 ? 79.984  35.339  11.968  1.00 48.58  ? 361 ARG A CD  1 
ATOM   2727 N  NE  . ARG A 1 362 ? 78.629  34.952  12.343  1.00 46.36  ? 361 ARG A NE  1 
ATOM   2728 C  CZ  . ARG A 1 362 ? 77.767  35.749  12.959  1.00 45.31  ? 361 ARG A CZ  1 
ATOM   2729 N  NH1 . ARG A 1 362 ? 78.082  36.993  13.280  1.00 47.40  ? 361 ARG A NH1 1 
ATOM   2730 N  NH2 . ARG A 1 362 ? 76.557  35.285  13.261  1.00 53.82  ? 361 ARG A NH2 1 
ATOM   2731 N  N   . PHE A 1 363 ? 82.704  31.902  12.315  1.00 49.92  ? 362 PHE A N   1 
ATOM   2732 C  CA  . PHE A 1 363 ? 83.065  31.165  13.522  1.00 49.56  ? 362 PHE A CA  1 
ATOM   2733 C  C   . PHE A 1 363 ? 84.229  30.218  13.270  1.00 48.27  ? 362 PHE A C   1 
ATOM   2734 O  O   . PHE A 1 363 ? 85.006  29.935  14.190  1.00 46.81  ? 362 PHE A O   1 
ATOM   2735 C  CB  . PHE A 1 363 ? 81.859  30.390  14.055  1.00 47.81  ? 362 PHE A CB  1 
ATOM   2736 C  CG  . PHE A 1 363 ? 81.037  31.158  15.051  1.00 49.60  ? 362 PHE A CG  1 
ATOM   2737 C  CD1 . PHE A 1 363 ? 81.542  31.445  16.309  1.00 45.60  ? 362 PHE A CD1 1 
ATOM   2738 C  CD2 . PHE A 1 363 ? 79.760  31.592  14.732  1.00 49.46  ? 362 PHE A CD2 1 
ATOM   2739 C  CE1 . PHE A 1 363 ? 80.791  32.149  17.231  1.00 53.62  ? 362 PHE A CE1 1 
ATOM   2740 C  CE2 . PHE A 1 363 ? 79.003  32.298  15.650  1.00 51.30  ? 362 PHE A CE2 1 
ATOM   2741 C  CZ  . PHE A 1 363 ? 79.519  32.577  16.901  1.00 52.14  ? 362 PHE A CZ  1 
ATOM   2742 N  N   . TYR A 1 364 ? 84.363  29.720  12.040  1.00 47.26  ? 363 TYR A N   1 
ATOM   2743 C  CA  . TYR A 1 364 ? 85.509  28.885  11.696  1.00 44.16  ? 363 TYR A CA  1 
ATOM   2744 C  C   . TYR A 1 364 ? 86.812  29.660  11.839  1.00 46.16  ? 363 TYR A C   1 
ATOM   2745 O  O   . TYR A 1 364 ? 87.793  29.151  12.394  1.00 44.94  ? 363 TYR A O   1 
ATOM   2746 C  CB  . TYR A 1 364 ? 85.349  28.340  10.277  1.00 45.20  ? 363 TYR A CB  1 
ATOM   2747 C  CG  . TYR A 1 364 ? 86.317  27.232  9.938   1.00 46.22  ? 363 TYR A CG  1 
ATOM   2748 C  CD1 . TYR A 1 364 ? 87.582  27.517  9.438   1.00 49.05  ? 363 TYR A CD1 1 
ATOM   2749 C  CD2 . TYR A 1 364 ? 85.973  25.903  10.131  1.00 39.47  ? 363 TYR A CD2 1 
ATOM   2750 C  CE1 . TYR A 1 364 ? 88.472  26.507  9.131   1.00 50.85  ? 363 TYR A CE1 1 
ATOM   2751 C  CE2 . TYR A 1 364 ? 86.857  24.889  9.827   1.00 49.13  ? 363 TYR A CE2 1 
ATOM   2752 C  CZ  . TYR A 1 364 ? 88.102  25.194  9.327   1.00 50.10  ? 363 TYR A CZ  1 
ATOM   2753 O  OH  . TYR A 1 364 ? 88.976  24.177  9.024   1.00 52.02  ? 363 TYR A OH  1 
ATOM   2754 N  N   . ILE A 1 365 ? 86.842  30.894  11.330  1.00 50.41  ? 364 ILE A N   1 
ATOM   2755 C  CA  . ILE A 1 365 ? 88.027  31.735  11.474  1.00 47.55  ? 364 ILE A CA  1 
ATOM   2756 C  C   . ILE A 1 365 ? 88.332  31.979  12.946  1.00 48.74  ? 364 ILE A C   1 
ATOM   2757 O  O   . ILE A 1 365 ? 89.485  31.876  13.382  1.00 46.41  ? 364 ILE A O   1 
ATOM   2758 C  CB  . ILE A 1 365 ? 87.832  33.060  10.713  1.00 42.37  ? 364 ILE A CB  1 
ATOM   2759 C  CG1 . ILE A 1 365 ? 87.885  32.823  9.204   1.00 47.04  ? 364 ILE A CG1 1 
ATOM   2760 C  CG2 . ILE A 1 365 ? 88.864  34.091  11.145  1.00 39.05  ? 364 ILE A CG2 1 
ATOM   2761 C  CD1 . ILE A 1 365 ? 87.043  33.795  8.413   1.00 43.46  ? 364 ILE A CD1 1 
ATOM   2762 N  N   . LEU A 1 366 ? 87.301  32.287  13.738  1.00 45.79  ? 365 LEU A N   1 
ATOM   2763 C  CA  . LEU A 1 366 ? 87.518  32.587  15.150  1.00 49.66  ? 365 LEU A CA  1 
ATOM   2764 C  C   . LEU A 1 366 ? 88.008  31.360  15.908  1.00 51.51  ? 365 LEU A C   1 
ATOM   2765 O  O   . LEU A 1 366 ? 88.861  31.474  16.796  1.00 52.44  ? 365 LEU A O   1 
ATOM   2766 C  CB  . LEU A 1 366 ? 86.237  33.139  15.775  1.00 54.23  ? 365 LEU A CB  1 
ATOM   2767 C  CG  . LEU A 1 366 ? 85.727  34.446  15.167  1.00 55.78  ? 365 LEU A CG  1 
ATOM   2768 C  CD1 . LEU A 1 366 ? 84.493  34.945  15.899  1.00 61.05  ? 365 LEU A CD1 1 
ATOM   2769 C  CD2 . LEU A 1 366 ? 86.827  35.495  15.200  1.00 52.55  ? 365 LEU A CD2 1 
ATOM   2770 N  N   . ALA A 1 367 ? 87.477  30.180  15.577  1.00 54.73  ? 366 ALA A N   1 
ATOM   2771 C  CA  . ALA A 1 367 ? 87.949  28.957  16.217  1.00 49.93  ? 366 ALA A CA  1 
ATOM   2772 C  C   . ALA A 1 367 ? 89.411  28.695  15.879  1.00 48.24  ? 366 ALA A C   1 
ATOM   2773 O  O   . ALA A 1 367 ? 90.192  28.272  16.739  1.00 52.20  ? 366 ALA A O   1 
ATOM   2774 C  CB  . ALA A 1 367 ? 87.076  27.775  15.795  1.00 49.66  ? 366 ALA A CB  1 
ATOM   2775 N  N   . GLU A 1 368 ? 89.795  28.940  14.626  1.00 47.86  ? 367 GLU A N   1 
ATOM   2776 C  CA  . GLU A 1 368 ? 91.161  28.669  14.193  1.00 43.68  ? 367 GLU A CA  1 
ATOM   2777 C  C   . GLU A 1 368 ? 92.139  29.662  14.811  1.00 49.91  ? 367 GLU A C   1 
ATOM   2778 O  O   . GLU A 1 368 ? 93.211  29.277  15.293  1.00 49.32  ? 367 GLU A O   1 
ATOM   2779 C  CB  . GLU A 1 368 ? 91.235  28.705  12.666  1.00 40.87  ? 367 GLU A CB  1 
ATOM   2780 C  CG  . GLU A 1 368 ? 92.204  27.706  12.064  1.00 53.69  ? 367 GLU A CG  1 
ATOM   2781 C  CD  . GLU A 1 368 ? 91.602  26.324  11.881  1.00 55.16  ? 367 GLU A CD  1 
ATOM   2782 O  OE1 . GLU A 1 368 ? 90.504  26.071  12.418  1.00 61.34  ? 367 GLU A OE1 1 
ATOM   2783 O  OE2 . GLU A 1 368 ? 92.228  25.490  11.193  1.00 62.40  ? 367 GLU A OE2 1 
ATOM   2784 N  N   . VAL A 1 369 ? 91.788  30.951  14.794  1.00 53.18  ? 368 VAL A N   1 
ATOM   2785 C  CA  . VAL A 1 369 ? 92.646  31.975  15.388  1.00 49.92  ? 368 VAL A CA  1 
ATOM   2786 C  C   . VAL A 1 369 ? 92.785  31.761  16.892  1.00 48.01  ? 368 VAL A C   1 
ATOM   2787 O  O   . VAL A 1 369 ? 93.859  31.981  17.466  1.00 51.09  ? 368 VAL A O   1 
ATOM   2788 C  CB  . VAL A 1 369 ? 92.102  33.380  15.061  1.00 46.94  ? 368 VAL A CB  1 
ATOM   2789 C  CG1 . VAL A 1 369 ? 92.883  34.449  15.812  1.00 47.27  ? 368 VAL A CG1 1 
ATOM   2790 C  CG2 . VAL A 1 369 ? 92.158  33.634  13.562  1.00 52.42  ? 368 VAL A CG2 1 
ATOM   2791 N  N   . SER A 1 370 ? 91.708  31.329  17.553  1.00 44.07  ? 369 SER A N   1 
ATOM   2792 C  CA  . SER A 1 370 ? 91.786  31.040  18.983  1.00 41.75  ? 369 SER A CA  1 
ATOM   2793 C  C   . SER A 1 370 ? 92.805  29.943  19.263  1.00 48.43  ? 369 SER A C   1 
ATOM   2794 O  O   . SER A 1 370 ? 93.631  30.063  20.175  1.00 54.39  ? 369 SER A O   1 
ATOM   2795 C  CB  . SER A 1 370 ? 90.410  30.641  19.519  1.00 42.74  ? 369 SER A CB  1 
ATOM   2796 O  OG  . SER A 1 370 ? 89.521  31.744  19.534  1.00 50.28  ? 369 SER A OG  1 
ATOM   2797 N  N   . GLN A 1 371 ? 92.760  28.862  18.482  1.00 49.39  ? 370 GLN A N   1 
ATOM   2798 C  CA  . GLN A 1 371 ? 93.698  27.761  18.678  1.00 47.43  ? 370 GLN A CA  1 
ATOM   2799 C  C   . GLN A 1 371 ? 95.131  28.195  18.393  1.00 49.02  ? 370 GLN A C   1 
ATOM   2800 O  O   . GLN A 1 371 ? 96.057  27.822  19.123  1.00 57.21  ? 370 GLN A O   1 
ATOM   2801 C  CB  . GLN A 1 371 ? 93.310  26.580  17.788  1.00 51.02  ? 370 GLN A CB  1 
ATOM   2802 C  CG  . GLN A 1 371 ? 92.180  25.725  18.341  1.00 50.52  ? 370 GLN A CG  1 
ATOM   2803 C  CD  . GLN A 1 371 ? 91.628  24.755  17.314  1.00 54.11  ? 370 GLN A CD  1 
ATOM   2804 O  OE1 . GLN A 1 371 ? 92.198  23.689  17.082  1.00 55.88  ? 370 GLN A OE1 1 
ATOM   2805 N  NE2 . GLN A 1 371 ? 90.515  25.125  16.688  1.00 44.24  ? 370 GLN A NE2 1 
ATOM   2806 N  N   . PHE A 1 372 ? 95.334  28.984  17.335  1.00 51.83  ? 371 PHE A N   1 
ATOM   2807 C  CA  . PHE A 1 372 ? 96.679  29.426  16.977  1.00 58.11  ? 371 PHE A CA  1 
ATOM   2808 C  C   . PHE A 1 372 ? 97.287  30.283  18.081  1.00 59.68  ? 371 PHE A C   1 
ATOM   2809 O  O   . PHE A 1 372 ? 98.417  30.041  18.522  1.00 56.86  ? 371 PHE A O   1 
ATOM   2810 C  CB  . PHE A 1 372 ? 96.637  30.191  15.650  1.00 56.63  ? 371 PHE A CB  1 
ATOM   2811 C  CG  . PHE A 1 372 ? 97.914  30.918  15.317  1.00 57.63  ? 371 PHE A CG  1 
ATOM   2812 C  CD1 . PHE A 1 372 ? 98.911  30.283  14.596  1.00 57.68  ? 371 PHE A CD1 1 
ATOM   2813 C  CD2 . PHE A 1 372 ? 98.111  32.235  15.705  1.00 62.47  ? 371 PHE A CD2 1 
ATOM   2814 C  CE1 . PHE A 1 372 ? 100.084 30.939  14.280  1.00 57.97  ? 371 PHE A CE1 1 
ATOM   2815 C  CE2 . PHE A 1 372 ? 99.284  32.896  15.393  1.00 60.73  ? 371 PHE A CE2 1 
ATOM   2816 C  CZ  . PHE A 1 372 ? 100.271 32.247  14.679  1.00 61.88  ? 371 PHE A CZ  1 
ATOM   2817 N  N   . THR A 1 373 ? 96.547  31.297  18.537  1.00 56.09  ? 372 THR A N   1 
ATOM   2818 C  CA  . THR A 1 373 ? 97.082  32.228  19.528  1.00 57.39  ? 372 THR A CA  1 
ATOM   2819 C  C   . THR A 1 373 ? 97.355  31.530  20.854  1.00 54.08  ? 372 THR A C   1 
ATOM   2820 O  O   . THR A 1 373 ? 98.399  31.752  21.478  1.00 58.15  ? 372 THR A O   1 
ATOM   2821 C  CB  . THR A 1 373 ? 96.115  33.395  19.728  1.00 63.94  ? 372 THR A CB  1 
ATOM   2822 O  OG1 . THR A 1 373 ? 95.728  33.921  18.453  1.00 59.26  ? 372 THR A OG1 1 
ATOM   2823 C  CG2 . THR A 1 373 ? 96.771  34.496  20.548  1.00 57.52  ? 372 THR A CG2 1 
ATOM   2824 N  N   . LEU A 1 374 ? 96.427  30.680  21.298  1.00 55.58  ? 373 LEU A N   1 
ATOM   2825 C  CA  . LEU A 1 374 ? 96.627  29.927  22.533  1.00 57.59  ? 373 LEU A CA  1 
ATOM   2826 C  C   . LEU A 1 374 ? 97.858  29.035  22.436  1.00 52.99  ? 373 LEU A C   1 
ATOM   2827 O  O   . LEU A 1 374 ? 98.676  28.983  23.362  1.00 54.35  ? 373 LEU A O   1 
ATOM   2828 C  CB  . LEU A 1 374 ? 95.381  29.101  22.852  1.00 51.27  ? 373 LEU A CB  1 
ATOM   2829 C  CG  . LEU A 1 374 ? 94.196  29.892  23.407  1.00 50.12  ? 373 LEU A CG  1 
ATOM   2830 C  CD1 . LEU A 1 374 ? 92.960  29.014  23.496  1.00 47.85  ? 373 LEU A CD1 1 
ATOM   2831 C  CD2 . LEU A 1 374 ? 94.540  30.482  24.767  1.00 46.98  ? 373 LEU A CD2 1 
ATOM   2832 N  N   . LEU A 1 375 ? 97.993  28.308  21.325  1.00 53.28  ? 374 LEU A N   1 
ATOM   2833 C  CA  . LEU A 1 375 ? 99.178  27.484  21.113  1.00 54.87  ? 374 LEU A CA  1 
ATOM   2834 C  C   . LEU A 1 375 ? 100.452 28.316  21.199  1.00 59.24  ? 374 LEU A C   1 
ATOM   2835 O  O   . LEU A 1 375 ? 101.464 27.860  21.742  1.00 60.98  ? 374 LEU A O   1 
ATOM   2836 C  CB  . LEU A 1 375 ? 99.086  26.783  19.757  1.00 51.01  ? 374 LEU A CB  1 
ATOM   2837 C  CG  . LEU A 1 375 ? 99.890  25.499  19.552  1.00 57.80  ? 374 LEU A CG  1 
ATOM   2838 C  CD1 . LEU A 1 375 ? 99.616  24.507  20.671  1.00 65.37  ? 374 LEU A CD1 1 
ATOM   2839 C  CD2 . LEU A 1 375 ? 99.572  24.883  18.197  1.00 60.73  ? 374 LEU A CD2 1 
ATOM   2840 N  N   . MET A 1 376 ? 100.417 29.543  20.676  1.00 59.39  ? 375 MET A N   1 
ATOM   2841 C  CA  . MET A 1 376 ? 101.609 30.385  20.669  1.00 55.55  ? 375 MET A CA  1 
ATOM   2842 C  C   . MET A 1 376 ? 101.942 30.933  22.049  1.00 57.10  ? 375 MET A C   1 
ATOM   2843 O  O   . MET A 1 376 ? 103.118 30.997  22.425  1.00 62.48  ? 375 MET A O   1 
ATOM   2844 C  CB  . MET A 1 376 ? 101.441 31.520  19.665  1.00 64.33  ? 375 MET A CB  1 
ATOM   2845 C  CG  . MET A 1 376 ? 101.618 31.023  18.276  1.00 64.60  ? 375 MET A CG  1 
ATOM   2846 S  SD  . MET A 1 376 ? 103.003 29.885  18.373  1.00 70.33  ? 375 MET A SD  1 
ATOM   2847 C  CE  . MET A 1 376 ? 103.107 29.409  16.680  1.00 68.75  ? 375 MET A CE  1 
ATOM   2848 N  N   . VAL A 1 377 ? 100.931 31.341  22.816  1.00 58.93  ? 376 VAL A N   1 
ATOM   2849 C  CA  . VAL A 1 377 ? 101.195 31.850  24.158  1.00 60.69  ? 376 VAL A CA  1 
ATOM   2850 C  C   . VAL A 1 377 ? 101.834 30.767  25.015  1.00 60.92  ? 376 VAL A C   1 
ATOM   2851 O  O   . VAL A 1 377 ? 102.813 31.013  25.731  1.00 59.58  ? 376 VAL A O   1 
ATOM   2852 C  CB  . VAL A 1 377 ? 99.897  32.384  24.793  1.00 55.78  ? 376 VAL A CB  1 
ATOM   2853 C  CG1 . VAL A 1 377 ? 100.119 32.707  26.262  1.00 53.20  ? 376 VAL A CG1 1 
ATOM   2854 C  CG2 . VAL A 1 377 ? 99.405  33.610  24.045  1.00 56.72  ? 376 VAL A CG2 1 
ATOM   2855 N  N   . PHE A 1 378 ? 101.306 29.547  24.937  1.00 60.35  ? 377 PHE A N   1 
ATOM   2856 C  CA  . PHE A 1 378 ? 101.787 28.469  25.790  1.00 60.43  ? 377 PHE A CA  1 
ATOM   2857 C  C   . PHE A 1 378 ? 103.140 27.942  25.320  1.00 59.44  ? 377 PHE A C   1 
ATOM   2858 O  O   . PHE A 1 378 ? 104.008 27.632  26.144  1.00 53.11  ? 377 PHE A O   1 
ATOM   2859 C  CB  . PHE A 1 378 ? 100.745 27.353  25.834  1.00 50.33  ? 377 PHE A CB  1 
ATOM   2860 C  CG  . PHE A 1 378 ? 99.608  27.632  26.779  1.00 51.51  ? 377 PHE A CG  1 
ATOM   2861 C  CD1 . PHE A 1 378 ? 99.851  27.987  28.095  1.00 47.20  ? 377 PHE A CD1 1 
ATOM   2862 C  CD2 . PHE A 1 378 ? 98.294  27.560  26.342  1.00 52.79  ? 377 PHE A CD2 1 
ATOM   2863 C  CE1 . PHE A 1 378 ? 98.805  28.252  28.961  1.00 44.88  ? 377 PHE A CE1 1 
ATOM   2864 C  CE2 . PHE A 1 378 ? 97.244  27.823  27.203  1.00 47.82  ? 377 PHE A CE2 1 
ATOM   2865 C  CZ  . PHE A 1 378 ? 97.500  28.169  28.513  1.00 45.00  ? 377 PHE A CZ  1 
ATOM   2866 N  N   . ALA A 1 379 ? 103.333 27.821  24.003  1.00 55.93  ? 378 ALA A N   1 
ATOM   2867 C  CA  . ALA A 1 379 ? 104.612 27.347  23.478  1.00 57.74  ? 378 ALA A CA  1 
ATOM   2868 C  C   . ALA A 1 379 ? 105.735 28.325  23.800  1.00 60.35  ? 378 ALA A C   1 
ATOM   2869 O  O   . ALA A 1 379 ? 106.816 27.924  24.244  1.00 62.27  ? 378 ALA A O   1 
ATOM   2870 C  CB  . ALA A 1 379 ? 104.514 27.116  21.971  1.00 57.32  ? 378 ALA A CB  1 
ATOM   2871 N  N   . HIS A 1 380 ? 105.498 29.619  23.568  1.00 62.99  ? 379 HIS A N   1 
ATOM   2872 C  CA  . HIS A 1 380 ? 106.504 30.631  23.870  1.00 67.75  ? 379 HIS A CA  1 
ATOM   2873 C  C   . HIS A 1 380 ? 106.875 30.642  25.346  1.00 62.69  ? 379 HIS A C   1 
ATOM   2874 O  O   . HIS A 1 380 ? 107.985 31.058  25.696  1.00 69.08  ? 379 HIS A O   1 
ATOM   2875 C  CB  . HIS A 1 380 ? 105.986 32.004  23.429  1.00 66.98  ? 379 HIS A CB  1 
ATOM   2876 C  CG  . HIS A 1 380 ? 106.706 33.161  24.046  1.00 68.88  ? 379 HIS A CG  1 
ATOM   2877 N  ND1 . HIS A 1 380 ? 107.874 33.676  23.526  1.00 74.59  ? 379 HIS A ND1 1 
ATOM   2878 C  CD2 . HIS A 1 380 ? 106.415 33.914  25.134  1.00 64.17  ? 379 HIS A CD2 1 
ATOM   2879 C  CE1 . HIS A 1 380 ? 108.275 34.691  24.271  1.00 76.49  ? 379 HIS A CE1 1 
ATOM   2880 N  NE2 . HIS A 1 380 ? 107.407 34.856  25.253  1.00 70.45  ? 379 HIS A NE2 1 
ATOM   2881 N  N   . TRP A 1 381 ? 105.981 30.178  26.216  1.00 61.19  ? 380 TRP A N   1 
ATOM   2882 C  CA  . TRP A 1 381 ? 106.260 30.103  27.644  1.00 63.33  ? 380 TRP A CA  1 
ATOM   2883 C  C   . TRP A 1 381 ? 106.977 28.810  28.025  1.00 67.06  ? 380 TRP A C   1 
ATOM   2884 O  O   . TRP A 1 381 ? 108.012 28.849  28.698  1.00 65.39  ? 380 TRP A O   1 
ATOM   2885 C  CB  . TRP A 1 381 ? 104.953 30.251  28.430  1.00 62.93  ? 380 TRP A CB  1 
ATOM   2886 C  CG  . TRP A 1 381 ? 105.064 29.956  29.900  1.00 67.43  ? 380 TRP A CG  1 
ATOM   2887 C  CD1 . TRP A 1 381 ? 106.123 30.225  30.720  1.00 63.12  ? 380 TRP A CD1 1 
ATOM   2888 C  CD2 . TRP A 1 381 ? 104.063 29.348  30.726  1.00 67.35  ? 380 TRP A CD2 1 
ATOM   2889 N  NE1 . TRP A 1 381 ? 105.846 29.812  32.001  1.00 68.14  ? 380 TRP A NE1 1 
ATOM   2890 C  CE2 . TRP A 1 381 ? 104.587 29.272  32.032  1.00 66.13  ? 380 TRP A CE2 1 
ATOM   2891 C  CE3 . TRP A 1 381 ? 102.776 28.858  30.486  1.00 64.39  ? 380 TRP A CE3 1 
ATOM   2892 C  CZ2 . TRP A 1 381 ? 103.869 28.726  33.094  1.00 59.73  ? 380 TRP A CZ2 1 
ATOM   2893 C  CZ3 . TRP A 1 381 ? 102.064 28.316  31.541  1.00 70.17  ? 380 TRP A CZ3 1 
ATOM   2894 C  CH2 . TRP A 1 381 ? 102.612 28.254  32.829  1.00 66.72  ? 380 TRP A CH2 1 
ATOM   2895 N  N   . LEU A 1 382 ? 106.457 27.662  27.587  1.00 66.00  ? 381 LEU A N   1 
ATOM   2896 C  CA  . LEU A 1 382 ? 106.888 26.379  28.132  1.00 62.16  ? 381 LEU A CA  1 
ATOM   2897 C  C   . LEU A 1 382 ? 108.004 25.717  27.336  1.00 66.36  ? 381 LEU A C   1 
ATOM   2898 O  O   . LEU A 1 382 ? 108.793 24.960  27.914  1.00 67.81  ? 381 LEU A O   1 
ATOM   2899 C  CB  . LEU A 1 382 ? 105.695 25.424  28.224  1.00 58.60  ? 381 LEU A CB  1 
ATOM   2900 C  CG  . LEU A 1 382 ? 104.643 25.781  29.277  1.00 69.09  ? 381 LEU A CG  1 
ATOM   2901 C  CD1 . LEU A 1 382 ? 103.244 25.499  28.755  1.00 63.27  ? 381 LEU A CD1 1 
ATOM   2902 C  CD2 . LEU A 1 382 ? 104.898 25.020  30.569  1.00 68.80  ? 381 LEU A CD2 1 
ATOM   2903 N  N   . ILE A 1 383 ? 108.093 25.968  26.034  1.00 64.60  ? 382 ILE A N   1 
ATOM   2904 C  CA  . ILE A 1 383 ? 109.106 25.313  25.205  1.00 67.73  ? 382 ILE A CA  1 
ATOM   2905 C  C   . ILE A 1 383 ? 110.504 25.783  25.604  1.00 68.68  ? 382 ILE A C   1 
ATOM   2906 O  O   . ILE A 1 383 ? 111.389 24.933  25.791  1.00 66.20  ? 382 ILE A O   1 
ATOM   2907 C  CB  . ILE A 1 383 ? 108.843 25.545  23.706  1.00 65.82  ? 382 ILE A CB  1 
ATOM   2908 C  CG1 . ILE A 1 383 ? 107.662 24.693  23.235  1.00 63.63  ? 382 ILE A CG1 1 
ATOM   2909 C  CG2 . ILE A 1 383 ? 110.087 25.230  22.887  1.00 63.96  ? 382 ILE A CG2 1 
ATOM   2910 C  CD1 . ILE A 1 383 ? 107.456 24.705  21.735  1.00 63.82  ? 382 ILE A CD1 1 
ATOM   2911 N  N   . PRO A 1 384 ? 110.774 27.090  25.744  1.00 71.67  ? 383 PRO A N   1 
ATOM   2912 C  CA  . PRO A 1 384 ? 112.145 27.505  26.093  1.00 70.36  ? 383 PRO A CA  1 
ATOM   2913 C  C   . PRO A 1 384 ? 112.625 26.979  27.434  1.00 71.55  ? 383 PRO A C   1 
ATOM   2914 O  O   . PRO A 1 384 ? 113.840 26.938  27.665  1.00 77.29  ? 383 PRO A O   1 
ATOM   2915 C  CB  . PRO A 1 384 ? 112.060 29.038  26.100  1.00 71.67  ? 383 PRO A CB  1 
ATOM   2916 C  CG  . PRO A 1 384 ? 110.895 29.359  25.247  1.00 73.44  ? 383 PRO A CG  1 
ATOM   2917 C  CD  . PRO A 1 384 ? 109.912 28.266  25.516  1.00 68.93  ? 383 PRO A CD  1 
ATOM   2918 N  N   . ALA A 1 385 ? 111.720 26.572  28.322  1.00 65.90  ? 384 ALA A N   1 
ATOM   2919 C  CA  . ALA A 1 385 ? 112.113 26.072  29.631  1.00 68.44  ? 384 ALA A CA  1 
ATOM   2920 C  C   . ALA A 1 385 ? 112.153 24.553  29.718  1.00 71.26  ? 384 ALA A C   1 
ATOM   2921 O  O   . ALA A 1 385 ? 112.981 24.013  30.458  1.00 74.14  ? 384 ALA A O   1 
ATOM   2922 C  CB  . ALA A 1 385 ? 111.167 26.614  30.709  1.00 66.51  ? 384 ALA A CB  1 
ATOM   2923 N  N   . HIS A 1 386 ? 111.289 23.846  28.984  1.00 67.23  ? 385 HIS A N   1 
ATOM   2924 C  CA  . HIS A 1 386 ? 111.158 22.404  29.151  1.00 59.56  ? 385 HIS A CA  1 
ATOM   2925 C  C   . HIS A 1 386 ? 111.254 21.628  27.843  1.00 57.07  ? 385 HIS A C   1 
ATOM   2926 O  O   . HIS A 1 386 ? 110.983 20.422  27.840  1.00 57.09  ? 385 HIS A O   1 
ATOM   2927 C  CB  . HIS A 1 386 ? 109.843 22.055  29.856  1.00 61.87  ? 385 HIS A CB  1 
ATOM   2928 C  CG  . HIS A 1 386 ? 109.761 22.555  31.263  1.00 70.30  ? 385 HIS A CG  1 
ATOM   2929 N  ND1 . HIS A 1 386 ? 108.585 22.999  31.829  1.00 75.15  ? 385 HIS A ND1 1 
ATOM   2930 C  CD2 . HIS A 1 386 ? 110.711 22.685  32.220  1.00 71.80  ? 385 HIS A CD2 1 
ATOM   2931 C  CE1 . HIS A 1 386 ? 108.813 23.376  33.074  1.00 71.86  ? 385 HIS A CE1 1 
ATOM   2932 N  NE2 . HIS A 1 386 ? 110.095 23.197  33.336  1.00 80.30  ? 385 HIS A NE2 1 
ATOM   2933 N  N   . GLY A 1 387 ? 111.643 22.272  26.744  1.00 57.00  ? 386 GLY A N   1 
ATOM   2934 C  CA  . GLY A 1 387 ? 111.913 21.528  25.523  1.00 56.27  ? 386 GLY A CA  1 
ATOM   2935 C  C   . GLY A 1 387 ? 110.689 20.793  25.018  1.00 59.82  ? 386 GLY A C   1 
ATOM   2936 O  O   . GLY A 1 387 ? 109.568 21.314  25.030  1.00 62.81  ? 386 GLY A O   1 
ATOM   2937 N  N   . ALA A 1 388 ? 110.906 19.556  24.560  1.00 61.28  ? 387 ALA A N   1 
ATOM   2938 C  CA  . ALA A 1 388 ? 109.819 18.779  23.974  1.00 64.29  ? 387 ALA A CA  1 
ATOM   2939 C  C   . ALA A 1 388 ? 108.724 18.496  24.991  1.00 61.92  ? 387 ALA A C   1 
ATOM   2940 O  O   . ALA A 1 388 ? 107.545 18.415  24.628  1.00 60.18  ? 387 ALA A O   1 
ATOM   2941 C  CB  . ALA A 1 388 ? 110.355 17.473  23.393  1.00 59.53  ? 387 ALA A CB  1 
ATOM   2942 N  N   . LEU A 1 389 ? 109.090 18.334  26.265  1.00 59.57  ? 388 LEU A N   1 
ATOM   2943 C  CA  . LEU A 1 389 ? 108.078 18.176  27.303  1.00 60.92  ? 388 LEU A CA  1 
ATOM   2944 C  C   . LEU A 1 389 ? 107.236 19.438  27.430  1.00 62.96  ? 388 LEU A C   1 
ATOM   2945 O  O   . LEU A 1 389 ? 106.016 19.364  27.616  1.00 60.89  ? 388 LEU A O   1 
ATOM   2946 C  CB  . LEU A 1 389 ? 108.742 17.834  28.637  1.00 64.58  ? 388 LEU A CB  1 
ATOM   2947 C  CG  . LEU A 1 389 ? 107.843 17.834  29.876  1.00 63.72  ? 388 LEU A CG  1 
ATOM   2948 C  CD1 . LEU A 1 389 ? 106.865 16.668  29.845  1.00 64.47  ? 388 LEU A CD1 1 
ATOM   2949 C  CD2 . LEU A 1 389 ? 108.681 17.806  31.145  1.00 69.52  ? 388 LEU A CD2 1 
ATOM   2950 N  N   . GLY A 1 390 ? 107.871 20.607  27.326  1.00 60.42  ? 389 GLY A N   1 
ATOM   2951 C  CA  . GLY A 1 390 ? 107.116 21.849  27.321  1.00 62.52  ? 389 GLY A CA  1 
ATOM   2952 C  C   . GLY A 1 390 ? 106.190 21.962  26.125  1.00 58.20  ? 389 GLY A C   1 
ATOM   2953 O  O   . GLY A 1 390 ? 105.077 22.482  26.238  1.00 55.66  ? 389 GLY A O   1 
ATOM   2954 N  N   . ALA A 1 391 ? 106.640 21.487  24.960  1.00 59.49  ? 390 ALA A N   1 
ATOM   2955 C  CA  . ALA A 1 391 ? 105.784 21.500  23.778  1.00 62.10  ? 390 ALA A CA  1 
ATOM   2956 C  C   . ALA A 1 391 ? 104.541 20.645  23.988  1.00 60.31  ? 390 ALA A C   1 
ATOM   2957 O  O   . ALA A 1 391 ? 103.445 21.008  23.544  1.00 57.72  ? 390 ALA A O   1 
ATOM   2958 C  CB  . ALA A 1 391 ? 106.568 21.019  22.556  1.00 56.23  ? 390 ALA A CB  1 
ATOM   2959 N  N   . ALA A 1 392 ? 104.692 19.501  24.660  1.00 57.44  ? 391 ALA A N   1 
ATOM   2960 C  CA  . ALA A 1 392 ? 103.532 18.677  24.982  1.00 57.97  ? 391 ALA A CA  1 
ATOM   2961 C  C   . ALA A 1 392 ? 102.658 19.349  26.032  1.00 57.15  ? 391 ALA A C   1 
ATOM   2962 O  O   . ALA A 1 392 ? 101.425 19.284  25.957  1.00 56.51  ? 391 ALA A O   1 
ATOM   2963 C  CB  . ALA A 1 392 ? 103.980 17.295  25.456  1.00 63.09  ? 391 ALA A CB  1 
ATOM   2964 N  N   . GLN A 1 393 ? 103.279 19.990  27.026  1.00 59.64  ? 392 GLN A N   1 
ATOM   2965 C  CA  . GLN A 1 393 ? 102.516 20.737  28.020  1.00 58.11  ? 392 GLN A CA  1 
ATOM   2966 C  C   . GLN A 1 393 ? 101.779 21.908  27.383  1.00 50.04  ? 392 GLN A C   1 
ATOM   2967 O  O   . GLN A 1 393 ? 100.623 22.184  27.726  1.00 45.41  ? 392 GLN A O   1 
ATOM   2968 C  CB  . GLN A 1 393 ? 103.446 21.228  29.129  1.00 65.25  ? 392 GLN A CB  1 
ATOM   2969 C  CG  . GLN A 1 393 ? 104.051 20.119  29.972  1.00 69.01  ? 392 GLN A CG  1 
ATOM   2970 C  CD  . GLN A 1 393 ? 105.233 20.596  30.790  1.00 71.32  ? 392 GLN A CD  1 
ATOM   2971 O  OE1 . GLN A 1 393 ? 105.902 21.564  30.427  1.00 71.58  ? 392 GLN A OE1 1 
ATOM   2972 N  NE2 . GLN A 1 393 ? 105.499 19.917  31.900  1.00 69.65  ? 392 GLN A NE2 1 
ATOM   2973 N  N   . ALA A 1 394 ? 102.437 22.617  26.462  1.00 59.62  ? 393 ALA A N   1 
ATOM   2974 C  CA  . ALA A 1 394 ? 101.791 23.733  25.780  1.00 57.64  ? 393 ALA A CA  1 
ATOM   2975 C  C   . ALA A 1 394 ? 100.584 23.264  24.978  1.00 58.28  ? 393 ALA A C   1 
ATOM   2976 O  O   . ALA A 1 394 ? 99.532  23.912  24.987  1.00 52.33  ? 393 ALA A O   1 
ATOM   2977 C  CB  . ALA A 1 394 ? 102.793 24.447  24.874  1.00 51.26  ? 393 ALA A CB  1 
ATOM   2978 N  N   . TYR A 1 395 ? 100.726 22.140  24.272  1.00 56.59  ? 394 TYR A N   1 
ATOM   2979 C  CA  . TYR A 1 395 ? 99.608  21.565  23.531  1.00 47.68  ? 394 TYR A CA  1 
ATOM   2980 C  C   . TYR A 1 395 ? 98.446  21.217  24.454  1.00 53.30  ? 394 TYR A C   1 
ATOM   2981 O  O   . TYR A 1 395 ? 97.283  21.483  24.128  1.00 53.78  ? 394 TYR A O   1 
ATOM   2982 C  CB  . TYR A 1 395 ? 100.084 20.333  22.760  1.00 59.32  ? 394 TYR A CB  1 
ATOM   2983 C  CG  . TYR A 1 395 ? 98.983  19.525  22.108  1.00 55.86  ? 394 TYR A CG  1 
ATOM   2984 C  CD1 . TYR A 1 395 ? 98.508  19.858  20.847  1.00 54.16  ? 394 TYR A CD1 1 
ATOM   2985 C  CD2 . TYR A 1 395 ? 98.437  18.416  22.743  1.00 58.84  ? 394 TYR A CD2 1 
ATOM   2986 C  CE1 . TYR A 1 395 ? 97.508  19.122  20.243  1.00 60.27  ? 394 TYR A CE1 1 
ATOM   2987 C  CE2 . TYR A 1 395 ? 97.436  17.673  22.145  1.00 61.60  ? 394 TYR A CE2 1 
ATOM   2988 C  CZ  . TYR A 1 395 ? 96.976  18.030  20.895  1.00 60.81  ? 394 TYR A CZ  1 
ATOM   2989 O  OH  . TYR A 1 395 ? 95.982  17.293  20.295  1.00 60.51  ? 394 TYR A OH  1 
ATOM   2990 N  N   . MET A 1 396 ? 98.739  20.616  25.609  1.00 55.23  ? 395 MET A N   1 
ATOM   2991 C  CA  . MET A 1 396 ? 97.678  20.246  26.542  1.00 52.93  ? 395 MET A CA  1 
ATOM   2992 C  C   . MET A 1 396 ? 96.997  21.479  27.124  1.00 55.47  ? 395 MET A C   1 
ATOM   2993 O  O   . MET A 1 396 ? 95.764  21.574  27.130  1.00 55.46  ? 395 MET A O   1 
ATOM   2994 C  CB  . MET A 1 396 ? 98.244  19.379  27.665  1.00 51.60  ? 395 MET A CB  1 
ATOM   2995 C  CG  . MET A 1 396 ? 97.276  19.182  28.821  1.00 60.35  ? 395 MET A CG  1 
ATOM   2996 S  SD  . MET A 1 396 ? 98.032  18.423  30.268  1.00 63.21  ? 395 MET A SD  1 
ATOM   2997 C  CE  . MET A 1 396 ? 98.137  19.840  31.361  1.00 56.23  ? 395 MET A CE  1 
ATOM   2998 N  N   . ALA A 1 397 ? 97.788  22.428  27.631  1.00 54.24  ? 396 ALA A N   1 
ATOM   2999 C  CA  . ALA A 1 397 ? 97.224  23.659  28.177  1.00 51.56  ? 396 ALA A CA  1 
ATOM   3000 C  C   . ALA A 1 397 ? 96.404  24.410  27.136  1.00 51.39  ? 396 ALA A C   1 
ATOM   3001 O  O   . ALA A 1 397 ? 95.368  25.003  27.461  1.00 51.19  ? 396 ALA A O   1 
ATOM   3002 C  CB  . ALA A 1 397 ? 98.340  24.548  28.725  1.00 46.58  ? 396 ALA A CB  1 
ATOM   3003 N  N   . THR A 1 398 ? 96.856  24.401  25.879  1.00 44.50  ? 397 THR A N   1 
ATOM   3004 C  CA  . THR A 1 398 ? 96.140  25.103  24.817  1.00 51.94  ? 397 THR A CA  1 
ATOM   3005 C  C   . THR A 1 398 ? 94.704  24.611  24.691  1.00 54.57  ? 397 THR A C   1 
ATOM   3006 O  O   . THR A 1 398 ? 93.767  25.411  24.580  1.00 56.54  ? 397 THR A O   1 
ATOM   3007 C  CB  . THR A 1 398 ? 96.880  24.931  23.490  1.00 53.61  ? 397 THR A CB  1 
ATOM   3008 O  OG1 . THR A 1 398 ? 98.107  25.669  23.526  1.00 57.53  ? 397 THR A OG1 1 
ATOM   3009 C  CG2 . THR A 1 398 ? 96.029  25.429  22.329  1.00 51.93  ? 397 THR A CG2 1 
ATOM   3010 N  N   . TYR A 1 399 ? 94.506  23.296  24.715  1.00 53.61  ? 398 TYR A N   1 
ATOM   3011 C  CA  . TYR A 1 399 ? 93.184  22.745  24.462  1.00 54.07  ? 398 TYR A CA  1 
ATOM   3012 C  C   . TYR A 1 399 ? 92.352  22.583  25.727  1.00 53.80  ? 398 TYR A C   1 
ATOM   3013 O  O   . TYR A 1 399 ? 91.133  22.399  25.630  1.00 51.08  ? 398 TYR A O   1 
ATOM   3014 C  CB  . TYR A 1 399 ? 93.314  21.420  23.709  1.00 46.85  ? 398 TYR A CB  1 
ATOM   3015 C  CG  . TYR A 1 399 ? 93.636  21.668  22.253  1.00 51.48  ? 398 TYR A CG  1 
ATOM   3016 C  CD1 . TYR A 1 399 ? 92.636  21.990  21.343  1.00 52.29  ? 398 TYR A CD1 1 
ATOM   3017 C  CD2 . TYR A 1 399 ? 94.948  21.634  21.800  1.00 48.38  ? 398 TYR A CD2 1 
ATOM   3018 C  CE1 . TYR A 1 399 ? 92.933  22.240  20.014  1.00 48.04  ? 398 TYR A CE1 1 
ATOM   3019 C  CE2 . TYR A 1 399 ? 95.254  21.883  20.476  1.00 51.51  ? 398 TYR A CE2 1 
ATOM   3020 C  CZ  . TYR A 1 399 ? 94.245  22.186  19.587  1.00 54.91  ? 398 TYR A CZ  1 
ATOM   3021 O  OH  . TYR A 1 399 ? 94.551  22.436  18.268  1.00 57.50  ? 398 TYR A OH  1 
ATOM   3022 N  N   . ILE A 1 400 ? 92.977  22.646  26.905  1.00 56.77  ? 399 ILE A N   1 
ATOM   3023 C  CA  . ILE A 1 400 ? 92.218  22.873  28.133  1.00 56.51  ? 399 ILE A CA  1 
ATOM   3024 C  C   . ILE A 1 400 ? 91.478  24.201  28.048  1.00 51.51  ? 399 ILE A C   1 
ATOM   3025 O  O   . ILE A 1 400 ? 90.262  24.274  28.258  1.00 50.33  ? 399 ILE A O   1 
ATOM   3026 C  CB  . ILE A 1 400 ? 93.147  22.830  29.360  1.00 59.58  ? 399 ILE A CB  1 
ATOM   3027 C  CG1 . ILE A 1 400 ? 93.658  21.412  29.607  1.00 60.12  ? 399 ILE A CG1 1 
ATOM   3028 C  CG2 . ILE A 1 400 ? 92.421  23.348  30.592  1.00 56.21  ? 399 ILE A CG2 1 
ATOM   3029 C  CD1 . ILE A 1 400 ? 94.758  21.331  30.639  1.00 55.25  ? 399 ILE A CD1 1 
ATOM   3030 N  N   . VAL A 1 401 ? 92.212  25.273  27.745  1.00 51.15  ? 400 VAL A N   1 
ATOM   3031 C  CA  . VAL A 1 401 ? 91.610  26.598  27.636  1.00 49.10  ? 400 VAL A CA  1 
ATOM   3032 C  C   . VAL A 1 401 ? 90.648  26.659  26.456  1.00 51.43  ? 400 VAL A C   1 
ATOM   3033 O  O   . VAL A 1 401 ? 89.579  27.276  26.541  1.00 53.42  ? 400 VAL A O   1 
ATOM   3034 C  CB  . VAL A 1 401 ? 92.712  27.668  27.529  1.00 51.24  ? 400 VAL A CB  1 
ATOM   3035 C  CG1 . VAL A 1 401 ? 92.109  29.037  27.247  1.00 46.34  ? 400 VAL A CG1 1 
ATOM   3036 C  CG2 . VAL A 1 401 ? 93.551  27.694  28.800  1.00 51.47  ? 400 VAL A CG2 1 
ATOM   3037 N  N   . TYR A 1 402 ? 91.002  26.019  25.339  1.00 46.66  ? 401 TYR A N   1 
ATOM   3038 C  CA  . TYR A 1 402 ? 90.184  26.136  24.136  1.00 49.65  ? 401 TYR A CA  1 
ATOM   3039 C  C   . TYR A 1 402 ? 88.838  25.438  24.300  1.00 53.55  ? 401 TYR A C   1 
ATOM   3040 O  O   . TYR A 1 402 ? 87.804  25.973  23.882  1.00 50.93  ? 401 TYR A O   1 
ATOM   3041 C  CB  . TYR A 1 402 ? 90.934  25.573  22.931  1.00 47.83  ? 401 TYR A CB  1 
ATOM   3042 C  CG  . TYR A 1 402 ? 90.132  25.614  21.651  1.00 53.70  ? 401 TYR A CG  1 
ATOM   3043 C  CD1 . TYR A 1 402 ? 89.667  26.818  21.138  1.00 47.04  ? 401 TYR A CD1 1 
ATOM   3044 C  CD2 . TYR A 1 402 ? 89.833  24.448  20.960  1.00 55.57  ? 401 TYR A CD2 1 
ATOM   3045 C  CE1 . TYR A 1 402 ? 88.934  26.859  19.968  1.00 50.21  ? 401 TYR A CE1 1 
ATOM   3046 C  CE2 . TYR A 1 402 ? 89.098  24.479  19.792  1.00 51.11  ? 401 TYR A CE2 1 
ATOM   3047 C  CZ  . TYR A 1 402 ? 88.652  25.686  19.300  1.00 51.28  ? 401 TYR A CZ  1 
ATOM   3048 O  OH  . TYR A 1 402 ? 87.916  25.714  18.139  1.00 53.30  ? 401 TYR A OH  1 
ATOM   3049 N  N   . PHE A 1 403 ? 88.829  24.242  24.894  1.00 52.08  ? 402 PHE A N   1 
ATOM   3050 C  CA  . PHE A 1 403 ? 87.562  23.559  25.143  1.00 49.26  ? 402 PHE A CA  1 
ATOM   3051 C  C   . PHE A 1 403 ? 86.671  24.374  26.070  1.00 51.05  ? 402 PHE A C   1 
ATOM   3052 O  O   . PHE A 1 403 ? 85.464  24.502  25.830  1.00 46.09  ? 402 PHE A O   1 
ATOM   3053 C  CB  . PHE A 1 403 ? 87.813  22.168  25.727  1.00 48.79  ? 402 PHE A CB  1 
ATOM   3054 C  CG  . PHE A 1 403 ? 86.554  21.421  26.069  1.00 47.40  ? 402 PHE A CG  1 
ATOM   3055 C  CD1 . PHE A 1 403 ? 85.821  20.783  25.082  1.00 50.47  ? 402 PHE A CD1 1 
ATOM   3056 C  CD2 . PHE A 1 403 ? 86.100  21.361  27.378  1.00 47.87  ? 402 PHE A CD2 1 
ATOM   3057 C  CE1 . PHE A 1 403 ? 84.660  20.097  25.392  1.00 48.97  ? 402 PHE A CE1 1 
ATOM   3058 C  CE2 . PHE A 1 403 ? 84.940  20.677  27.694  1.00 50.01  ? 402 PHE A CE2 1 
ATOM   3059 C  CZ  . PHE A 1 403 ? 84.220  20.044  26.700  1.00 42.68  ? 402 PHE A CZ  1 
ATOM   3060 N  N   . SER A 1 404 ? 87.245  24.921  27.144  1.00 52.32  ? 403 SER A N   1 
ATOM   3061 C  CA  . SER A 1 404 ? 86.485  25.798  28.030  1.00 51.29  ? 403 SER A CA  1 
ATOM   3062 C  C   . SER A 1 404 ? 85.929  26.994  27.270  1.00 49.23  ? 403 SER A C   1 
ATOM   3063 O  O   . SER A 1 404 ? 84.758  27.358  27.431  1.00 49.40  ? 403 SER A O   1 
ATOM   3064 C  CB  . SER A 1 404 ? 87.366  26.260  29.191  1.00 46.08  ? 403 SER A CB  1 
ATOM   3065 O  OG  . SER A 1 404 ? 87.685  25.180  30.049  1.00 44.80  ? 403 SER A OG  1 
ATOM   3066 N  N   . LEU A 1 405 ? 86.761  27.623  26.437  1.00 47.40  ? 404 LEU A N   1 
ATOM   3067 C  CA  . LEU A 1 405 ? 86.291  28.728  25.608  1.00 47.31  ? 404 LEU A CA  1 
ATOM   3068 C  C   . LEU A 1 405 ? 85.163  28.287  24.683  1.00 53.62  ? 404 LEU A C   1 
ATOM   3069 O  O   . LEU A 1 405 ? 84.181  29.015  24.500  1.00 53.12  ? 404 LEU A O   1 
ATOM   3070 C  CB  . LEU A 1 405 ? 87.455  29.305  24.803  1.00 52.81  ? 404 LEU A CB  1 
ATOM   3071 C  CG  . LEU A 1 405 ? 87.116  30.388  23.780  1.00 60.38  ? 404 LEU A CG  1 
ATOM   3072 C  CD1 . LEU A 1 405 ? 86.471  31.578  24.471  1.00 52.95  ? 404 LEU A CD1 1 
ATOM   3073 C  CD2 . LEU A 1 405 ? 88.362  30.815  23.021  1.00 62.62  ? 404 LEU A CD2 1 
ATOM   3074 N  N   . CYS A 1 406 ? 85.289  27.095  24.090  1.00 56.26  ? 405 CYS A N   1 
ATOM   3075 C  CA  . CYS A 1 406 ? 84.231  26.573  23.228  1.00 51.82  ? 405 CYS A CA  1 
ATOM   3076 C  C   . CYS A 1 406 ? 82.916  26.441  23.984  1.00 52.75  ? 405 CYS A C   1 
ATOM   3077 O  O   . CYS A 1 406 ? 81.854  26.810  23.468  1.00 56.75  ? 405 CYS A O   1 
ATOM   3078 C  CB  . CYS A 1 406 ? 84.648  25.225  22.642  1.00 54.53  ? 405 CYS A CB  1 
ATOM   3079 S  SG  . CYS A 1 406 ? 85.684  25.338  21.164  1.00 58.95  ? 405 CYS A SG  1 
ATOM   3080 N  N   . CYS A 1 407 ? 82.965  25.901  25.204  1.00 52.66  ? 406 CYS A N   1 
ATOM   3081 C  CA  . CYS A 1 407 ? 81.758  25.785  26.017  1.00 47.46  ? 406 CYS A CA  1 
ATOM   3082 C  C   . CYS A 1 407 ? 81.149  27.155  26.285  1.00 51.03  ? 406 CYS A C   1 
ATOM   3083 O  O   . CYS A 1 407 ? 79.944  27.360  26.098  1.00 47.97  ? 406 CYS A O   1 
ATOM   3084 C  CB  . CYS A 1 407 ? 82.076  25.069  27.330  1.00 47.93  ? 406 CYS A CB  1 
ATOM   3085 S  SG  . CYS A 1 407 ? 82.525  23.329  27.139  1.00 56.08  ? 406 CYS A SG  1 
ATOM   3086 N  N   . GLY A 1 408 ? 81.972  28.107  26.732  1.00 45.13  ? 407 GLY A N   1 
ATOM   3087 C  CA  . GLY A 1 408 ? 81.459  29.432  27.039  1.00 50.69  ? 407 GLY A CA  1 
ATOM   3088 C  C   . GLY A 1 408 ? 80.855  30.125  25.832  1.00 50.31  ? 407 GLY A C   1 
ATOM   3089 O  O   . GLY A 1 408 ? 79.797  30.752  25.931  1.00 47.43  ? 407 GLY A O   1 
ATOM   3090 N  N   . VAL A 1 409 ? 81.517  30.024  24.677  1.00 45.12  ? 408 VAL A N   1 
ATOM   3091 C  CA  . VAL A 1 409 ? 80.990  30.654  23.469  1.00 47.32  ? 408 VAL A CA  1 
ATOM   3092 C  C   . VAL A 1 409 ? 79.711  29.958  23.018  1.00 53.89  ? 408 VAL A C   1 
ATOM   3093 O  O   . VAL A 1 409 ? 78.775  30.604  22.529  1.00 52.07  ? 408 VAL A O   1 
ATOM   3094 C  CB  . VAL A 1 409 ? 82.058  30.662  22.360  1.00 50.92  ? 408 VAL A CB  1 
ATOM   3095 C  CG1 . VAL A 1 409 ? 81.463  31.130  21.039  1.00 49.55  ? 408 VAL A CG1 1 
ATOM   3096 C  CG2 . VAL A 1 409 ? 83.223  31.553  22.756  1.00 55.09  ? 408 VAL A CG2 1 
ATOM   3097 N  N   . PHE A 1 410 ? 79.639  28.636  23.192  1.00 51.14  ? 409 PHE A N   1 
ATOM   3098 C  CA  . PHE A 1 410 ? 78.409  27.921  22.869  1.00 50.68  ? 409 PHE A CA  1 
ATOM   3099 C  C   . PHE A 1 410 ? 77.268  28.359  23.775  1.00 52.66  ? 409 PHE A C   1 
ATOM   3100 O  O   . PHE A 1 410 ? 76.132  28.531  23.318  1.00 52.87  ? 409 PHE A O   1 
ATOM   3101 C  CB  . PHE A 1 410 ? 78.623  26.412  22.977  1.00 50.37  ? 409 PHE A CB  1 
ATOM   3102 C  CG  . PHE A 1 410 ? 77.397  25.606  22.662  1.00 47.19  ? 409 PHE A CG  1 
ATOM   3103 C  CD1 . PHE A 1 410 ? 77.077  25.289  21.353  1.00 50.98  ? 409 PHE A CD1 1 
ATOM   3104 C  CD2 . PHE A 1 410 ? 76.561  25.168  23.676  1.00 45.60  ? 409 PHE A CD2 1 
ATOM   3105 C  CE1 . PHE A 1 410 ? 75.948  24.550  21.062  1.00 51.29  ? 409 PHE A CE1 1 
ATOM   3106 C  CE2 . PHE A 1 410 ? 75.431  24.431  23.392  1.00 47.32  ? 409 PHE A CE2 1 
ATOM   3107 C  CZ  . PHE A 1 410 ? 75.124  24.120  22.083  1.00 50.50  ? 409 PHE A CZ  1 
ATOM   3108 N  N   . LEU A 1 411 ? 77.552  28.543  25.066  1.00 56.66  ? 410 LEU A N   1 
ATOM   3109 C  CA  . LEU A 1 411 ? 76.514  28.983  25.991  1.00 58.01  ? 410 LEU A CA  1 
ATOM   3110 C  C   . LEU A 1 411 ? 76.005  30.371  25.626  1.00 53.88  ? 410 LEU A C   1 
ATOM   3111 O  O   . LEU A 1 411 ? 74.796  30.629  25.678  1.00 54.90  ? 410 LEU A O   1 
ATOM   3112 C  CB  . LEU A 1 411 ? 77.044  28.964  27.423  1.00 65.63  ? 410 LEU A CB  1 
ATOM   3113 C  CG  . LEU A 1 411 ? 77.126  27.591  28.093  1.00 65.91  ? 410 LEU A CG  1 
ATOM   3114 C  CD1 . LEU A 1 411 ? 77.120  27.740  29.605  1.00 61.91  ? 410 LEU A CD1 1 
ATOM   3115 C  CD2 . LEU A 1 411 ? 75.992  26.688  27.632  1.00 62.15  ? 410 LEU A CD2 1 
ATOM   3116 N  N   . LEU A 1 412 ? 76.911  31.280  25.255  1.00 51.60  ? 411 LEU A N   1 
ATOM   3117 C  CA  . LEU A 1 412 ? 76.488  32.611  24.834  1.00 56.67  ? 411 LEU A CA  1 
ATOM   3118 C  C   . LEU A 1 412 ? 75.656  32.545  23.559  1.00 61.78  ? 411 LEU A C   1 
ATOM   3119 O  O   . LEU A 1 412 ? 74.678  33.286  23.404  1.00 62.16  ? 411 LEU A O   1 
ATOM   3120 C  CB  . LEU A 1 412 ? 77.711  33.510  24.636  1.00 55.69  ? 411 LEU A CB  1 
ATOM   3121 C  CG  . LEU A 1 412 ? 78.448  33.950  25.905  1.00 54.54  ? 411 LEU A CG  1 
ATOM   3122 C  CD1 . LEU A 1 412 ? 79.783  34.610  25.578  1.00 49.66  ? 411 LEU A CD1 1 
ATOM   3123 C  CD2 . LEU A 1 412 ? 77.575  34.894  26.722  1.00 51.50  ? 411 LEU A CD2 1 
ATOM   3124 N  N   . TRP A 1 413 ? 76.039  31.671  22.627  1.00 56.33  ? 412 TRP A N   1 
ATOM   3125 C  CA  . TRP A 1 413 ? 75.285  31.529  21.385  1.00 52.81  ? 412 TRP A CA  1 
ATOM   3126 C  C   . TRP A 1 413 ? 73.929  30.870  21.618  1.00 56.42  ? 412 TRP A C   1 
ATOM   3127 O  O   . TRP A 1 413 ? 72.915  31.304  21.057  1.00 54.07  ? 412 TRP A O   1 
ATOM   3128 C  CB  . TRP A 1 413 ? 76.104  30.723  20.383  1.00 52.64  ? 412 TRP A CB  1 
ATOM   3129 C  CG  . TRP A 1 413 ? 75.333  30.227  19.205  1.00 57.89  ? 412 TRP A CG  1 
ATOM   3130 C  CD1 . TRP A 1 413 ? 75.128  30.883  18.027  1.00 58.61  ? 412 TRP A CD1 1 
ATOM   3131 C  CD2 . TRP A 1 413 ? 74.666  28.965  19.083  1.00 57.53  ? 412 TRP A CD2 1 
ATOM   3132 N  NE1 . TRP A 1 413 ? 74.379  30.107  17.177  1.00 55.14  ? 412 TRP A NE1 1 
ATOM   3133 C  CE2 . TRP A 1 413 ? 74.081  28.925  17.802  1.00 54.47  ? 412 TRP A CE2 1 
ATOM   3134 C  CE3 . TRP A 1 413 ? 74.507  27.865  19.932  1.00 54.14  ? 412 TRP A CE3 1 
ATOM   3135 C  CZ2 . TRP A 1 413 ? 73.350  27.829  17.350  1.00 56.56  ? 412 TRP A CZ2 1 
ATOM   3136 C  CZ3 . TRP A 1 413 ? 73.779  26.780  19.481  1.00 55.41  ? 412 TRP A CZ3 1 
ATOM   3137 C  CH2 . TRP A 1 413 ? 73.210  26.769  18.202  1.00 56.31  ? 412 TRP A CH2 1 
ATOM   3138 N  N   . ARG A 1 414 ? 73.894  29.819  22.442  1.00 58.55  ? 413 ARG A N   1 
ATOM   3139 C  CA  . ARG A 1 414 ? 72.646  29.104  22.695  1.00 57.08  ? 413 ARG A CA  1 
ATOM   3140 C  C   . ARG A 1 414 ? 71.643  29.978  23.429  1.00 58.72  ? 413 ARG A C   1 
ATOM   3141 O  O   . ARG A 1 414 ? 70.438  29.908  23.164  1.00 62.63  ? 413 ARG A O   1 
ATOM   3142 C  CB  . ARG A 1 414 ? 72.926  27.825  23.482  1.00 56.25  ? 413 ARG A CB  1 
ATOM   3143 C  CG  . ARG A 1 414 ? 71.736  27.307  24.270  1.00 55.67  ? 413 ARG A CG  1 
ATOM   3144 C  CD  . ARG A 1 414 ? 70.720  26.674  23.347  1.00 59.56  ? 413 ARG A CD  1 
ATOM   3145 N  NE  . ARG A 1 414 ? 69.616  26.085  24.091  1.00 71.70  ? 413 ARG A NE  1 
ATOM   3146 C  CZ  . ARG A 1 414 ? 68.376  26.550  24.058  1.00 66.51  ? 413 ARG A CZ  1 
ATOM   3147 N  NH1 . ARG A 1 414 ? 68.057  27.618  23.345  1.00 59.60  ? 413 ARG A NH1 1 
ATOM   3148 N  NH2 . ARG A 1 414 ? 67.436  25.940  24.774  1.00 67.54  ? 413 ARG A NH2 1 
ATOM   3149 N  N   . ARG A 1 415 ? 72.124  30.821  24.329  1.00 61.20  ? 414 ARG A N   1 
ATOM   3150 C  CA  . ARG A 1 415 ? 71.278  31.748  25.056  1.00 65.56  ? 414 ARG A CA  1 
ATOM   3151 C  C   . ARG A 1 415 ? 71.020  33.059  24.318  1.00 70.19  ? 414 ARG A C   1 
ATOM   3152 O  O   . ARG A 1 415 ? 70.300  33.917  24.846  1.00 69.99  ? 414 ARG A O   1 
ATOM   3153 C  CB  . ARG A 1 415 ? 71.877  31.999  26.443  1.00 63.91  ? 414 ARG A CB  1 
ATOM   3154 C  CG  . ARG A 1 415 ? 72.675  33.269  26.634  1.00 74.17  ? 414 ARG A CG  1 
ATOM   3155 C  CD  . ARG A 1 415 ? 72.763  33.563  28.129  1.00 93.02  ? 414 ARG A CD  1 
ATOM   3156 N  NE  . ARG A 1 415 ? 73.797  34.515  28.507  1.00 90.28  ? 414 ARG A NE  1 
ATOM   3157 C  CZ  . ARG A 1 415 ? 73.835  35.780  28.123  1.00 94.97  ? 414 ARG A CZ  1 
ATOM   3158 N  NH1 . ARG A 1 415 ? 72.874  36.307  27.384  1.00 91.37  ? 414 ARG A NH1 1 
ATOM   3159 N  NH2 . ARG A 1 415 ? 74.832  36.552  28.540  1.00 96.55  ? 414 ARG A NH2 1 
ATOM   3160 N  N   . ARG A 1 416 ? 71.598  33.237  23.127  1.00 67.05  ? 415 ARG A N   1 
ATOM   3161 C  CA  . ARG A 1 416 ? 71.369  34.405  22.272  1.00 66.69  ? 415 ARG A CA  1 
ATOM   3162 C  C   . ARG A 1 416 ? 71.772  35.701  22.980  1.00 72.44  ? 415 ARG A C   1 
ATOM   3163 O  O   . ARG A 1 416 ? 70.976  36.627  23.160  1.00 74.17  ? 415 ARG A O   1 
ATOM   3164 C  CB  . ARG A 1 416 ? 69.912  34.443  21.785  1.00 56.44  ? 415 ARG A CB  1 
ATOM   3165 C  CG  . ARG A 1 416 ? 69.392  33.091  21.259  1.00 58.01  ? 415 ARG A CG  1 
ATOM   3166 C  CD  . ARG A 1 416 ? 67.909  33.116  20.867  1.00 65.37  ? 415 ARG A CD  1 
ATOM   3167 N  NE  . ARG A 1 416 ? 67.435  31.796  20.456  1.00 70.93  ? 415 ARG A NE  1 
ATOM   3168 C  CZ  . ARG A 1 416 ? 66.449  31.120  21.031  1.00 70.54  ? 415 ARG A CZ  1 
ATOM   3169 N  NH1 . ARG A 1 416 ? 65.778  31.612  22.058  1.00 66.90  ? 415 ARG A NH1 1 
ATOM   3170 N  NH2 . ARG A 1 416 ? 66.115  29.926  20.548  1.00 67.23  ? 415 ARG A NH2 1 
ATOM   3171 N  N   . ALA A 1 417 ? 73.045  35.748  23.374  1.00 76.32  ? 416 ALA A N   1 
ATOM   3172 C  CA  . ALA A 1 417 ? 73.549  36.875  24.150  1.00 71.95  ? 416 ALA A CA  1 
ATOM   3173 C  C   . ALA A 1 417 ? 73.585  38.157  23.335  1.00 75.23  ? 416 ALA A C   1 
ATOM   3174 O  O   . ALA A 1 417 ? 73.448  39.250  23.894  1.00 75.03  ? 416 ALA A O   1 
ATOM   3175 C  CB  . ALA A 1 417 ? 74.936  36.554  24.705  1.00 69.29  ? 416 ALA A CB  1 
ATOM   3176 N  N   . LEU A 1 418 ? 73.730  38.043  22.019  1.00 81.31  ? 417 LEU A N   1 
ATOM   3177 C  CA  . LEU A 1 418 ? 73.834  39.196  21.139  1.00 75.38  ? 417 LEU A CA  1 
ATOM   3178 C  C   . LEU A 1 418 ? 72.488  39.694  20.628  1.00 77.99  ? 417 LEU A C   1 
ATOM   3179 O  O   . LEU A 1 418 ? 72.457  40.679  19.885  1.00 76.17  ? 417 LEU A O   1 
ATOM   3180 C  CB  . LEU A 1 418 ? 74.747  38.867  19.952  1.00 71.21  ? 417 LEU A CB  1 
ATOM   3181 C  CG  . LEU A 1 418 ? 76.241  38.742  20.269  1.00 64.39  ? 417 LEU A CG  1 
ATOM   3182 C  CD1 . LEU A 1 418 ? 77.087  38.912  19.012  1.00 60.78  ? 417 LEU A CD1 1 
ATOM   3183 C  CD2 . LEU A 1 418 ? 76.653  39.739  21.342  1.00 63.39  ? 417 LEU A CD2 1 
ATOM   3184 N  N   . GLU A 1 419 ? 71.384  39.052  21.000  1.00 81.96  ? 418 GLU A N   1 
ATOM   3185 C  CA  . GLU A 1 419 ? 70.072  39.478  20.522  1.00 80.57  ? 418 GLU A CA  1 
ATOM   3186 C  C   . GLU A 1 419 ? 69.328  40.255  21.606  1.00 83.59  ? 418 GLU A C   1 
ATOM   3187 O  O   . GLU A 1 419 ? 68.618  41.223  21.329  1.00 90.37  ? 418 GLU A O   1 
ATOM   3188 C  CB  . GLU A 1 419 ? 69.238  38.275  20.078  1.00 81.44  ? 418 GLU A CB  1 
ATOM   3189 C  CG  . GLU A 1 419 ? 70.007  37.241  19.274  1.00 83.18  ? 418 GLU A CG  1 
ATOM   3190 C  CD  . GLU A 1 419 ? 70.264  37.678  17.845  1.00 94.32  ? 418 GLU A CD  1 
ATOM   3191 O  OE1 . GLU A 1 419 ? 69.557  38.588  17.361  1.00 93.43  ? 418 GLU A OE1 1 
ATOM   3192 O  OE2 . GLU A 1 419 ? 71.170  37.105  17.204  1.00 88.12  ? 418 GLU A OE2 1 
ATOM   3193 N  N   . GLN B 2 5   ? 130.166 8.712   -4.822  1.00 87.31  ? 3   GLN B N   1 
ATOM   3194 C  CA  . GLN B 2 5   ? 130.213 7.260   -4.967  1.00 89.48  ? 3   GLN B CA  1 
ATOM   3195 C  C   . GLN B 2 5   ? 130.557 6.830   -6.390  1.00 87.12  ? 3   GLN B C   1 
ATOM   3196 O  O   . GLN B 2 5   ? 131.002 5.705   -6.611  1.00 85.15  ? 3   GLN B O   1 
ATOM   3197 C  CB  . GLN B 2 5   ? 128.879 6.633   -4.556  1.00 88.80  ? 3   GLN B CB  1 
ATOM   3198 C  CG  . GLN B 2 5   ? 129.001 5.223   -3.995  1.00 91.39  ? 3   GLN B CG  1 
ATOM   3199 C  CD  . GLN B 2 5   ? 127.709 4.440   -4.118  1.00 81.75  ? 3   GLN B CD  1 
ATOM   3200 O  OE1 . GLN B 2 5   ? 126.870 4.736   -4.968  1.00 81.41  ? 3   GLN B OE1 1 
ATOM   3201 N  NE2 . GLN B 2 5   ? 127.541 3.434   -3.267  1.00 86.12  ? 3   GLN B NE2 1 
ATOM   3202 N  N   . LEU B 2 6   ? 130.348 7.724   -7.354  1.00 83.40  ? 4   LEU B N   1 
ATOM   3203 C  CA  . LEU B 2 6   ? 130.619 7.435   -8.756  1.00 84.88  ? 4   LEU B CA  1 
ATOM   3204 C  C   . LEU B 2 6   ? 131.388 8.586   -9.386  1.00 82.88  ? 4   LEU B C   1 
ATOM   3205 O  O   . LEU B 2 6   ? 131.048 9.755   -9.176  1.00 78.02  ? 4   LEU B O   1 
ATOM   3206 C  CB  . LEU B 2 6   ? 129.317 7.193   -9.528  1.00 88.63  ? 4   LEU B CB  1 
ATOM   3207 C  CG  . LEU B 2 6   ? 128.481 5.981   -9.115  1.00 85.56  ? 4   LEU B CG  1 
ATOM   3208 C  CD1 . LEU B 2 6   ? 127.074 6.092   -9.675  1.00 80.90  ? 4   LEU B CD1 1 
ATOM   3209 C  CD2 . LEU B 2 6   ? 129.142 4.691   -9.573  1.00 84.27  ? 4   LEU B CD2 1 
ATOM   3210 N  N   . VAL B 2 7   ? 132.425 8.251   -10.150 1.00 84.41  ? 5   VAL B N   1 
ATOM   3211 C  CA  . VAL B 2 7   ? 133.231 9.230   -10.869 1.00 87.86  ? 5   VAL B CA  1 
ATOM   3212 C  C   . VAL B 2 7   ? 133.406 8.747   -12.303 1.00 91.19  ? 5   VAL B C   1 
ATOM   3213 O  O   . VAL B 2 7   ? 133.523 7.542   -12.556 1.00 84.45  ? 5   VAL B O   1 
ATOM   3214 C  CB  . VAL B 2 7   ? 134.595 9.477   -10.180 1.00 84.51  ? 5   VAL B CB  1 
ATOM   3215 C  CG1 . VAL B 2 7   ? 135.635 8.447   -10.603 1.00 91.22  ? 5   VAL B CG1 1 
ATOM   3216 C  CG2 . VAL B 2 7   ? 135.086 10.888  -10.471 1.00 83.47  ? 5   VAL B CG2 1 
ATOM   3217 N  N   . GLU B 2 8   ? 133.367 9.684   -13.245 1.00 95.57  ? 6   GLU B N   1 
ATOM   3218 C  CA  . GLU B 2 8   ? 133.390 9.378   -14.667 1.00 92.72  ? 6   GLU B CA  1 
ATOM   3219 C  C   . GLU B 2 8   ? 134.712 9.810   -15.289 1.00 91.58  ? 6   GLU B C   1 
ATOM   3220 O  O   . GLU B 2 8   ? 135.384 10.721  -14.797 1.00 95.96  ? 6   GLU B O   1 
ATOM   3221 C  CB  . GLU B 2 8   ? 132.231 10.060  -15.402 1.00 94.02  ? 6   GLU B CB  1 
ATOM   3222 C  CG  . GLU B 2 8   ? 130.893 9.350   -15.266 1.00 91.49  ? 6   GLU B CG  1 
ATOM   3223 C  CD  . GLU B 2 8   ? 129.907 10.119  -14.407 1.00 92.47  ? 6   GLU B CD  1 
ATOM   3224 O  OE1 . GLU B 2 8   ? 130.306 11.140  -13.811 1.00 94.80  ? 6   GLU B OE1 1 
ATOM   3225 O  OE2 . GLU B 2 8   ? 128.731 9.704   -14.333 1.00 89.60  ? 6   GLU B OE2 1 
ATOM   3226 N  N   . SER B 2 9   ? 135.075 9.141   -16.381 1.00 87.64  ? 7   SER B N   1 
ATOM   3227 C  CA  . SER B 2 9   ? 136.284 9.471   -17.120 1.00 94.27  ? 7   SER B CA  1 
ATOM   3228 C  C   . SER B 2 9   ? 136.047 9.187   -18.596 1.00 91.20  ? 7   SER B C   1 
ATOM   3229 O  O   . SER B 2 9   ? 135.205 8.358   -18.956 1.00 83.13  ? 7   SER B O   1 
ATOM   3230 C  CB  . SER B 2 9   ? 137.493 8.679   -16.607 1.00 94.39  ? 7   SER B CB  1 
ATOM   3231 O  OG  . SER B 2 9   ? 138.543 8.665   -17.560 1.00 105.30 ? 7   SER B OG  1 
ATOM   3232 N  N   . GLY B 2 10  ? 136.799 9.882   -19.445 1.00 96.52  ? 8   GLY B N   1 
ATOM   3233 C  CA  . GLY B 2 10  ? 136.638 9.746   -20.878 1.00 87.80  ? 8   GLY B CA  1 
ATOM   3234 C  C   . GLY B 2 10  ? 135.709 10.796  -21.453 1.00 87.25  ? 8   GLY B C   1 
ATOM   3235 O  O   . GLY B 2 10  ? 135.124 11.624  -20.749 1.00 91.60  ? 8   GLY B O   1 
ATOM   3236 N  N   . GLY B 2 11  ? 135.573 10.757  -22.776 1.00 90.24  ? 9   GLY B N   1 
ATOM   3237 C  CA  . GLY B 2 11  ? 134.703 11.667  -23.489 1.00 91.94  ? 9   GLY B CA  1 
ATOM   3238 C  C   . GLY B 2 11  ? 135.386 12.956  -23.909 1.00 85.71  ? 9   GLY B C   1 
ATOM   3239 O  O   . GLY B 2 11  ? 136.527 13.254  -23.547 1.00 94.81  ? 9   GLY B O   1 
ATOM   3240 N  N   . GLY B 2 12  ? 134.652 13.739  -24.691 1.00 81.50  ? 10  GLY B N   1 
ATOM   3241 C  CA  . GLY B 2 12  ? 135.139 14.980  -25.245 1.00 88.26  ? 10  GLY B CA  1 
ATOM   3242 C  C   . GLY B 2 12  ? 134.634 15.164  -26.660 1.00 94.04  ? 10  GLY B C   1 
ATOM   3243 O  O   . GLY B 2 12  ? 133.709 14.484  -27.103 1.00 91.39  ? 10  GLY B O   1 
ATOM   3244 N  N   . LEU B 2 13  ? 135.255 16.102  -27.373 1.00 96.47  ? 11  LEU B N   1 
ATOM   3245 C  CA  . LEU B 2 13  ? 134.918 16.369  -28.766 1.00 94.73  ? 11  LEU B CA  1 
ATOM   3246 C  C   . LEU B 2 13  ? 135.492 15.277  -29.660 1.00 97.20  ? 11  LEU B C   1 
ATOM   3247 O  O   . LEU B 2 13  ? 136.713 15.090  -29.715 1.00 99.67  ? 11  LEU B O   1 
ATOM   3248 C  CB  . LEU B 2 13  ? 135.450 17.738  -29.186 1.00 103.63 ? 11  LEU B CB  1 
ATOM   3249 C  CG  . LEU B 2 13  ? 134.906 18.365  -30.474 1.00 110.30 ? 11  LEU B CG  1 
ATOM   3250 C  CD1 . LEU B 2 13  ? 133.431 18.061  -30.653 1.00 104.25 ? 11  LEU B CD1 1 
ATOM   3251 C  CD2 . LEU B 2 13  ? 135.150 19.868  -30.491 1.00 120.42 ? 11  LEU B CD2 1 
ATOM   3252 N  N   . VAL B 2 14  ? 134.618 14.565  -30.367 1.00 93.59  ? 12  VAL B N   1 
ATOM   3253 C  CA  . VAL B 2 14  ? 135.020 13.469  -31.238 1.00 91.02  ? 12  VAL B CA  1 
ATOM   3254 C  C   . VAL B 2 14  ? 134.400 13.689  -32.612 1.00 93.84  ? 12  VAL B C   1 
ATOM   3255 O  O   . VAL B 2 14  ? 133.276 14.192  -32.727 1.00 95.48  ? 12  VAL B O   1 
ATOM   3256 C  CB  . VAL B 2 14  ? 134.614 12.097  -30.649 1.00 91.65  ? 12  VAL B CB  1 
ATOM   3257 C  CG1 . VAL B 2 14  ? 133.101 11.973  -30.549 1.00 98.98  ? 12  VAL B CG1 1 
ATOM   3258 C  CG2 . VAL B 2 14  ? 135.196 10.955  -31.478 1.00 91.76  ? 12  VAL B CG2 1 
ATOM   3259 N  N   . GLN B 2 15  ? 135.143 13.325  -33.652 1.00 93.64  ? 13  GLN B N   1 
ATOM   3260 C  CA  . GLN B 2 15  ? 134.643 13.421  -35.016 1.00 100.96 ? 13  GLN B CA  1 
ATOM   3261 C  C   . GLN B 2 15  ? 133.558 12.374  -35.245 1.00 98.91  ? 13  GLN B C   1 
ATOM   3262 O  O   . GLN B 2 15  ? 133.645 11.251  -34.741 1.00 96.58  ? 13  GLN B O   1 
ATOM   3263 C  CB  . GLN B 2 15  ? 135.790 13.259  -36.014 1.00 98.48  ? 13  GLN B CB  1 
ATOM   3264 C  CG  . GLN B 2 15  ? 135.402 13.486  -37.467 1.00 99.47  ? 13  GLN B CG  1 
ATOM   3265 C  CD  . GLN B 2 15  ? 136.496 13.079  -38.437 1.00 109.21 ? 13  GLN B CD  1 
ATOM   3266 O  OE1 . GLN B 2 15  ? 137.676 13.051  -38.085 1.00 109.31 ? 13  GLN B OE1 1 
ATOM   3267 N  NE2 . GLN B 2 15  ? 136.112 12.789  -39.675 1.00 113.02 ? 13  GLN B NE2 1 
ATOM   3268 N  N   . ALA B 2 16  ? 132.525 12.751  -35.999 1.00 94.62  ? 14  ALA B N   1 
ATOM   3269 C  CA  . ALA B 2 16  ? 131.446 11.821  -36.313 1.00 93.73  ? 14  ALA B CA  1 
ATOM   3270 C  C   . ALA B 2 16  ? 131.980 10.588  -37.030 1.00 96.93  ? 14  ALA B C   1 
ATOM   3271 O  O   . ALA B 2 16  ? 132.710 10.693  -38.020 1.00 103.03 ? 14  ALA B O   1 
ATOM   3272 C  CB  . ALA B 2 16  ? 130.387 12.510  -37.172 1.00 89.74  ? 14  ALA B CB  1 
ATOM   3273 N  N   . GLY B 2 17  ? 131.603 9.412   -36.524 1.00 97.48  ? 15  GLY B N   1 
ATOM   3274 C  CA  . GLY B 2 17  ? 132.075 8.143   -37.025 1.00 98.79  ? 15  GLY B CA  1 
ATOM   3275 C  C   . GLY B 2 17  ? 133.167 7.504   -36.190 1.00 98.33  ? 15  GLY B C   1 
ATOM   3276 O  O   . GLY B 2 17  ? 133.350 6.283   -36.266 1.00 95.63  ? 15  GLY B O   1 
ATOM   3277 N  N   . GLY B 2 18  ? 133.899 8.296   -35.401 1.00 97.73  ? 16  GLY B N   1 
ATOM   3278 C  CA  . GLY B 2 18  ? 134.956 7.748   -34.580 1.00 98.90  ? 16  GLY B CA  1 
ATOM   3279 C  C   . GLY B 2 18  ? 134.440 7.074   -33.322 1.00 94.95  ? 16  GLY B C   1 
ATOM   3280 O  O   . GLY B 2 18  ? 133.318 7.299   -32.871 1.00 96.37  ? 16  GLY B O   1 
ATOM   3281 N  N   . SER B 2 19  ? 135.287 6.224   -32.752 1.00 93.91  ? 17  SER B N   1 
ATOM   3282 C  CA  . SER B 2 19  ? 134.954 5.495   -31.539 1.00 92.43  ? 17  SER B CA  1 
ATOM   3283 C  C   . SER B 2 19  ? 135.258 6.334   -30.298 1.00 91.35  ? 17  SER B C   1 
ATOM   3284 O  O   . SER B 2 19  ? 135.954 7.350   -30.353 1.00 94.05  ? 17  SER B O   1 
ATOM   3285 C  CB  . SER B 2 19  ? 135.715 4.169   -31.493 1.00 91.64  ? 17  SER B CB  1 
ATOM   3286 O  OG  . SER B 2 19  ? 135.364 3.347   -32.593 1.00 99.70  ? 17  SER B OG  1 
ATOM   3287 N  N   . LEU B 2 20  ? 134.714 5.895   -29.164 1.00 94.64  ? 18  LEU B N   1 
ATOM   3288 C  CA  . LEU B 2 20  ? 134.919 6.581   -27.897 1.00 87.81  ? 18  LEU B CA  1 
ATOM   3289 C  C   . LEU B 2 20  ? 134.703 5.573   -26.777 1.00 83.32  ? 18  LEU B C   1 
ATOM   3290 O  O   . LEU B 2 20  ? 133.830 4.707   -26.877 1.00 81.64  ? 18  LEU B O   1 
ATOM   3291 C  CB  . LEU B 2 20  ? 133.967 7.780   -27.761 1.00 91.68  ? 18  LEU B CB  1 
ATOM   3292 C  CG  . LEU B 2 20  ? 134.273 8.955   -26.819 1.00 95.82  ? 18  LEU B CG  1 
ATOM   3293 C  CD1 . LEU B 2 20  ? 134.238 8.573   -25.347 1.00 92.15  ? 18  LEU B CD1 1 
ATOM   3294 C  CD2 . LEU B 2 20  ? 135.619 9.574   -27.174 1.00 91.85  ? 18  LEU B CD2 1 
ATOM   3295 N  N   . GLY B 2 21  ? 135.501 5.690   -25.718 1.00 82.01  ? 19  GLY B N   1 
ATOM   3296 C  CA  . GLY B 2 21  ? 135.369 4.812   -24.572 1.00 81.47  ? 19  GLY B CA  1 
ATOM   3297 C  C   . GLY B 2 21  ? 135.187 5.543   -23.258 1.00 81.44  ? 19  GLY B C   1 
ATOM   3298 O  O   . GLY B 2 21  ? 136.096 6.241   -22.799 1.00 86.28  ? 19  GLY B O   1 
ATOM   3299 N  N   . LEU B 2 22  ? 134.019 5.390   -22.643 1.00 78.26  ? 20  LEU B N   1 
ATOM   3300 C  CA  . LEU B 2 22  ? 133.744 5.946   -21.327 1.00 75.66  ? 20  LEU B CA  1 
ATOM   3301 C  C   . LEU B 2 22  ? 133.944 4.894   -20.243 1.00 74.72  ? 20  LEU B C   1 
ATOM   3302 O  O   . LEU B 2 22  ? 133.704 3.702   -20.453 1.00 75.96  ? 20  LEU B O   1 
ATOM   3303 C  CB  . LEU B 2 22  ? 132.321 6.501   -21.249 1.00 82.15  ? 20  LEU B CB  1 
ATOM   3304 C  CG  . LEU B 2 22  ? 131.957 7.608   -22.237 1.00 82.82  ? 20  LEU B CG  1 
ATOM   3305 C  CD1 . LEU B 2 22  ? 130.500 8.001   -22.080 1.00 79.45  ? 20  LEU B CD1 1 
ATOM   3306 C  CD2 . LEU B 2 22  ? 132.858 8.811   -22.024 1.00 78.58  ? 20  LEU B CD2 1 
ATOM   3307 N  N   . SER B 2 23  ? 134.383 5.353   -19.073 1.00 70.87  ? 21  SER B N   1 
ATOM   3308 C  CA  . SER B 2 23  ? 134.581 4.489   -17.921 1.00 76.62  ? 21  SER B CA  1 
ATOM   3309 C  C   . SER B 2 23  ? 134.071 5.203   -16.678 1.00 74.42  ? 21  SER B C   1 
ATOM   3310 O  O   . SER B 2 23  ? 134.113 6.433   -16.588 1.00 77.96  ? 21  SER B O   1 
ATOM   3311 C  CB  . SER B 2 23  ? 136.056 4.101   -17.740 1.00 86.75  ? 21  SER B CB  1 
ATOM   3312 O  OG  . SER B 2 23  ? 136.770 5.109   -17.046 1.00 90.30  ? 21  SER B OG  1 
ATOM   3313 N  N   . CYS B 2 24  ? 133.597 4.415   -15.717 1.00 78.12  ? 22  CYS B N   1 
ATOM   3314 C  CA  . CYS B 2 24  ? 133.050 4.932   -14.471 1.00 83.14  ? 22  CYS B CA  1 
ATOM   3315 C  C   . CYS B 2 24  ? 133.567 4.094   -13.314 1.00 76.94  ? 22  CYS B C   1 
ATOM   3316 O  O   . CYS B 2 24  ? 133.435 2.867   -13.327 1.00 77.18  ? 22  CYS B O   1 
ATOM   3317 C  CB  . CYS B 2 24  ? 131.516 4.920   -14.509 1.00 92.91  ? 22  CYS B CB  1 
ATOM   3318 S  SG  . CYS B 2 24  ? 130.664 5.343   -12.966 1.00 99.28  ? 22  CYS B SG  1 
ATOM   3319 N  N   . ALA B 2 25  ? 134.152 4.756   -12.320 1.00 74.31  ? 23  ALA B N   1 
ATOM   3320 C  CA  . ALA B 2 25  ? 134.668 4.088   -11.136 1.00 84.59  ? 23  ALA B CA  1 
ATOM   3321 C  C   . ALA B 2 25  ? 133.727 4.307   -9.960  1.00 90.27  ? 23  ALA B C   1 
ATOM   3322 O  O   . ALA B 2 25  ? 133.093 5.358   -9.834  1.00 92.22  ? 23  ALA B O   1 
ATOM   3323 C  CB  . ALA B 2 25  ? 136.068 4.598   -10.786 1.00 88.02  ? 23  ALA B CB  1 
ATOM   3324 N  N   . ALA B 2 26  ? 133.646 3.301   -9.092  1.00 87.07  ? 24  ALA B N   1 
ATOM   3325 C  CA  . ALA B 2 26  ? 132.756 3.337   -7.942  1.00 95.24  ? 24  ALA B CA  1 
ATOM   3326 C  C   . ALA B 2 26  ? 133.537 3.063   -6.667  1.00 101.07 ? 24  ALA B C   1 
ATOM   3327 O  O   . ALA B 2 26  ? 134.452 2.234   -6.652  1.00 104.51 ? 24  ALA B O   1 
ATOM   3328 C  CB  . ALA B 2 26  ? 131.620 2.319   -8.086  1.00 96.99  ? 24  ALA B CB  1 
ATOM   3329 N  N   . SER B 2 27  ? 133.164 3.759   -5.598  1.00 103.06 ? 25  SER B N   1 
ATOM   3330 C  CA  . SER B 2 27  ? 133.789 3.583   -4.296  1.00 106.17 ? 25  SER B CA  1 
ATOM   3331 C  C   . SER B 2 27  ? 132.979 2.559   -3.499  1.00 108.47 ? 25  SER B C   1 
ATOM   3332 O  O   . SER B 2 27  ? 132.235 1.757   -4.069  1.00 107.34 ? 25  SER B O   1 
ATOM   3333 C  CB  . SER B 2 27  ? 133.906 4.934   -3.582  1.00 104.43 ? 25  SER B CB  1 
ATOM   3334 O  OG  . SER B 2 27  ? 132.628 5.468   -3.289  1.00 102.77 ? 25  SER B OG  1 
ATOM   3335 N  N   . GLY B 2 28  ? 133.114 2.573   -2.177  1.00 113.20 ? 26  GLY B N   1 
ATOM   3336 C  CA  . GLY B 2 28  ? 132.334 1.693   -1.334  1.00 110.42 ? 26  GLY B CA  1 
ATOM   3337 C  C   . GLY B 2 28  ? 132.941 0.320   -1.148  1.00 114.47 ? 26  GLY B C   1 
ATOM   3338 O  O   . GLY B 2 28  ? 134.167 0.168   -1.112  1.00 123.02 ? 26  GLY B O   1 
ATOM   3339 N  N   . ARG B 2 29  ? 132.084 -0.695  -1.049  1.00 106.37 ? 27  ARG B N   1 
ATOM   3340 C  CA  . ARG B 2 29  ? 132.531 -2.061  -0.815  1.00 113.41 ? 27  ARG B CA  1 
ATOM   3341 C  C   . ARG B 2 29  ? 131.715 -3.041  -1.646  1.00 110.90 ? 27  ARG B C   1 
ATOM   3342 O  O   . ARG B 2 29  ? 132.235 -3.661  -2.580  1.00 110.75 ? 27  ARG B O   1 
ATOM   3343 C  CB  . ARG B 2 29  ? 132.413 -2.379  0.677   1.00 108.18 ? 27  ARG B CB  1 
ATOM   3344 C  CG  . ARG B 2 29  ? 133.722 -2.697  1.371   1.00 105.93 ? 27  ARG B CG  1 
ATOM   3345 C  CD  . ARG B 2 29  ? 133.498 -2.863  2.869   1.00 104.43 ? 27  ARG B CD  1 
ATOM   3346 N  NE  . ARG B 2 29  ? 134.462 -3.754  3.503   1.00 108.72 ? 27  ARG B NE  1 
ATOM   3347 C  CZ  . ARG B 2 29  ? 134.417 -4.116  4.778   1.00 106.75 ? 27  ARG B CZ  1 
ATOM   3348 N  NH1 . ARG B 2 29  ? 133.465 -3.681  5.588   1.00 100.74 ? 27  ARG B NH1 1 
ATOM   3349 N  NH2 . ARG B 2 29  ? 135.359 -4.925  5.257   1.00 108.19 ? 27  ARG B NH2 1 
ATOM   3350 N  N   . THR B 2 30  ? 130.437 -3.188  -1.307  1.00 112.52 ? 28  THR B N   1 
ATOM   3351 C  CA  . THR B 2 30  ? 129.532 -4.047  -2.060  1.00 108.67 ? 28  THR B CA  1 
ATOM   3352 C  C   . THR B 2 30  ? 129.279 -3.415  -3.424  1.00 102.50 ? 28  THR B C   1 
ATOM   3353 O  O   . THR B 2 30  ? 128.589 -2.396  -3.527  1.00 104.26 ? 28  THR B O   1 
ATOM   3354 C  CB  . THR B 2 30  ? 128.231 -4.251  -1.287  1.00 108.17 ? 28  THR B CB  1 
ATOM   3355 O  OG1 . THR B 2 30  ? 128.444 -5.206  -0.239  1.00 104.61 ? 28  THR B OG1 1 
ATOM   3356 C  CG2 . THR B 2 30  ? 127.133 -4.773  -2.202  1.00 115.14 ? 28  THR B CG2 1 
ATOM   3357 N  N   . PHE B 2 31  ? 129.870 -3.987  -4.466  1.00 106.79 ? 29  PHE B N   1 
ATOM   3358 C  CA  . PHE B 2 31  ? 129.713 -3.475  -5.822  1.00 105.49 ? 29  PHE B CA  1 
ATOM   3359 C  C   . PHE B 2 31  ? 129.062 -4.478  -6.757  1.00 104.51 ? 29  PHE B C   1 
ATOM   3360 O  O   . PHE B 2 31  ? 128.282 -4.086  -7.629  1.00 98.80  ? 29  PHE B O   1 
ATOM   3361 C  CB  . PHE B 2 31  ? 131.080 -3.053  -6.390  1.00 100.13 ? 29  PHE B CB  1 
ATOM   3362 C  CG  . PHE B 2 31  ? 131.024 -2.561  -7.811  1.00 96.38  ? 29  PHE B CG  1 
ATOM   3363 C  CD1 . PHE B 2 31  ? 130.633 -1.261  -8.090  1.00 95.07  ? 29  PHE B CD1 1 
ATOM   3364 C  CD2 . PHE B 2 31  ? 131.369 -3.391  -8.866  1.00 94.44  ? 29  PHE B CD2 1 
ATOM   3365 C  CE1 . PHE B 2 31  ? 130.582 -0.800  -9.392  1.00 89.43  ? 29  PHE B CE1 1 
ATOM   3366 C  CE2 . PHE B 2 31  ? 131.318 -2.935  -10.172 1.00 90.65  ? 29  PHE B CE2 1 
ATOM   3367 C  CZ  . PHE B 2 31  ? 130.925 -1.638  -10.434 1.00 87.86  ? 29  PHE B CZ  1 
ATOM   3368 N  N   . SER B 2 32  ? 129.365 -5.768  -6.598  1.00 106.47 ? 30  SER B N   1 
ATOM   3369 C  CA  . SER B 2 32  ? 128.800 -6.802  -7.456  1.00 110.80 ? 30  SER B CA  1 
ATOM   3370 C  C   . SER B 2 32  ? 127.295 -6.966  -7.282  1.00 114.29 ? 30  SER B C   1 
ATOM   3371 O  O   . SER B 2 32  ? 126.677 -7.679  -8.078  1.00 115.82 ? 30  SER B O   1 
ATOM   3372 C  CB  . SER B 2 32  ? 129.497 -8.138  -7.193  1.00 111.36 ? 30  SER B CB  1 
ATOM   3373 O  OG  . SER B 2 32  ? 129.475 -8.460  -5.813  1.00 113.88 ? 30  SER B OG  1 
ATOM   3374 N  N   . ASN B 2 33  ? 126.695 -6.341  -6.270  1.00 115.20 ? 31  ASN B N   1 
ATOM   3375 C  CA  . ASN B 2 33  ? 125.259 -6.427  -6.044  1.00 114.88 ? 31  ASN B CA  1 
ATOM   3376 C  C   . ASN B 2 33  ? 124.503 -5.225  -6.590  1.00 105.43 ? 31  ASN B C   1 
ATOM   3377 O  O   . ASN B 2 33  ? 123.271 -5.194  -6.508  1.00 103.87 ? 31  ASN B O   1 
ATOM   3378 C  CB  . ASN B 2 33  ? 124.964 -6.592  -4.549  1.00 121.09 ? 31  ASN B CB  1 
ATOM   3379 C  CG  . ASN B 2 33  ? 125.633 -7.816  -3.956  1.00 125.84 ? 31  ASN B CG  1 
ATOM   3380 O  OD1 . ASN B 2 33  ? 126.201 -7.761  -2.866  1.00 124.77 ? 31  ASN B OD1 1 
ATOM   3381 N  ND2 . ASN B 2 33  ? 125.576 -8.928  -4.679  1.00 126.30 ? 31  ASN B ND2 1 
ATOM   3382 N  N   . TYR B 2 34  ? 125.205 -4.238  -7.137  1.00 98.04  ? 32  TYR B N   1 
ATOM   3383 C  CA  . TYR B 2 34  ? 124.587 -3.043  -7.692  1.00 89.03  ? 32  TYR B CA  1 
ATOM   3384 C  C   . TYR B 2 34  ? 124.413 -3.226  -9.193  1.00 83.33  ? 32  TYR B C   1 
ATOM   3385 O  O   . TYR B 2 34  ? 125.364 -3.595  -9.890  1.00 91.13  ? 32  TYR B O   1 
ATOM   3386 C  CB  . TYR B 2 34  ? 125.438 -1.803  -7.413  1.00 84.29  ? 32  TYR B CB  1 
ATOM   3387 C  CG  . TYR B 2 34  ? 125.230 -1.189  -6.047  1.00 88.15  ? 32  TYR B CG  1 
ATOM   3388 C  CD1 . TYR B 2 34  ? 125.940 -1.646  -4.945  1.00 95.00  ? 32  TYR B CD1 1 
ATOM   3389 C  CD2 . TYR B 2 34  ? 124.334 -0.145  -5.862  1.00 90.60  ? 32  TYR B CD2 1 
ATOM   3390 C  CE1 . TYR B 2 34  ? 125.758 -1.087  -3.695  1.00 91.62  ? 32  TYR B CE1 1 
ATOM   3391 C  CE2 . TYR B 2 34  ? 124.145 0.421   -4.614  1.00 94.94  ? 32  TYR B CE2 1 
ATOM   3392 C  CZ  . TYR B 2 34  ? 124.860 -0.054  -3.535  1.00 97.09  ? 32  TYR B CZ  1 
ATOM   3393 O  OH  . TYR B 2 34  ? 124.680 0.502   -2.289  1.00 97.14  ? 32  TYR B OH  1 
ATOM   3394 N  N   . VAL B 2 35  ? 123.201 -2.978  -9.687  1.00 87.78  ? 33  VAL B N   1 
ATOM   3395 C  CA  . VAL B 2 35  ? 123.002 -2.896  -11.127 1.00 88.70  ? 33  VAL B CA  1 
ATOM   3396 C  C   . VAL B 2 35  ? 123.603 -1.594  -11.642 1.00 76.42  ? 33  VAL B C   1 
ATOM   3397 O  O   . VAL B 2 35  ? 123.469 -0.530  -11.020 1.00 72.22  ? 33  VAL B O   1 
ATOM   3398 C  CB  . VAL B 2 35  ? 121.508 -3.035  -11.481 1.00 87.71  ? 33  VAL B CB  1 
ATOM   3399 C  CG1 . VAL B 2 35  ? 120.754 -1.744  -11.252 1.00 74.79  ? 33  VAL B CG1 1 
ATOM   3400 C  CG2 . VAL B 2 35  ? 121.339 -3.479  -12.921 1.00 84.43  ? 33  VAL B CG2 1 
ATOM   3401 N  N   . MET B 2 36  ? 124.326 -1.683  -12.753 1.00 75.85  ? 34  MET B N   1 
ATOM   3402 C  CA  . MET B 2 36  ? 125.038 -0.545  -13.313 1.00 72.31  ? 34  MET B CA  1 
ATOM   3403 C  C   . MET B 2 36  ? 124.390 -0.140  -14.630 1.00 70.69  ? 34  MET B C   1 
ATOM   3404 O  O   . MET B 2 36  ? 123.920 -0.987  -15.395 1.00 72.63  ? 34  MET B O   1 
ATOM   3405 C  CB  . MET B 2 36  ? 126.517 -0.881  -13.531 1.00 76.07  ? 34  MET B CB  1 
ATOM   3406 C  CG  . MET B 2 36  ? 127.323 -1.059  -12.249 1.00 75.40  ? 34  MET B CG  1 
ATOM   3407 S  SD  . MET B 2 36  ? 126.826 0.009   -10.887 1.00 84.66  ? 34  MET B SD  1 
ATOM   3408 C  CE  . MET B 2 36  ? 127.562 1.564   -11.388 1.00 67.09  ? 34  MET B CE  1 
ATOM   3409 N  N   . ALA B 2 37  ? 124.378 1.163   -14.897 1.00 61.81  ? 35  ALA B N   1 
ATOM   3410 C  CA  . ALA B 2 37  ? 123.693 1.664   -16.078 1.00 67.09  ? 35  ALA B CA  1 
ATOM   3411 C  C   . ALA B 2 37  ? 124.340 2.958   -16.547 1.00 65.12  ? 35  ALA B C   1 
ATOM   3412 O  O   . ALA B 2 37  ? 124.977 3.679   -15.773 1.00 60.48  ? 35  ALA B O   1 
ATOM   3413 C  CB  . ALA B 2 37  ? 122.199 1.885   -15.810 1.00 69.19  ? 35  ALA B CB  1 
ATOM   3414 N  N   . TRP B 2 38  ? 124.152 3.247   -17.831 1.00 62.61  ? 36  TRP B N   1 
ATOM   3415 C  CA  . TRP B 2 38  ? 124.535 4.520   -18.425 1.00 67.31  ? 36  TRP B CA  1 
ATOM   3416 C  C   . TRP B 2 38  ? 123.280 5.276   -18.829 1.00 67.74  ? 36  TRP B C   1 
ATOM   3417 O  O   . TRP B 2 38  ? 122.366 4.697   -19.427 1.00 65.65  ? 36  TRP B O   1 
ATOM   3418 C  CB  . TRP B 2 38  ? 125.430 4.314   -19.649 1.00 73.66  ? 36  TRP B CB  1 
ATOM   3419 C  CG  . TRP B 2 38  ? 126.849 3.994   -19.324 1.00 72.66  ? 36  TRP B CG  1 
ATOM   3420 C  CD1 . TRP B 2 38  ? 127.460 2.781   -19.435 1.00 76.27  ? 36  TRP B CD1 1 
ATOM   3421 C  CD2 . TRP B 2 38  ? 127.848 4.906   -18.850 1.00 69.72  ? 36  TRP B CD2 1 
ATOM   3422 N  NE1 . TRP B 2 38  ? 128.776 2.878   -19.056 1.00 83.63  ? 36  TRP B NE1 1 
ATOM   3423 C  CE2 . TRP B 2 38  ? 129.039 4.172   -18.691 1.00 82.36  ? 36  TRP B CE2 1 
ATOM   3424 C  CE3 . TRP B 2 38  ? 127.849 6.270   -18.542 1.00 72.59  ? 36  TRP B CE3 1 
ATOM   3425 C  CZ2 . TRP B 2 38  ? 130.221 4.755   -18.234 1.00 72.19  ? 36  TRP B CZ2 1 
ATOM   3426 C  CZ3 . TRP B 2 38  ? 129.023 6.847   -18.090 1.00 80.34  ? 36  TRP B CZ3 1 
ATOM   3427 C  CH2 . TRP B 2 38  ? 130.192 6.091   -17.941 1.00 75.38  ? 36  TRP B CH2 1 
ATOM   3428 N  N   . PHE B 2 39  ? 123.240 6.564   -18.503 1.00 67.37  ? 37  PHE B N   1 
ATOM   3429 C  CA  . PHE B 2 39  ? 122.203 7.461   -18.982 1.00 62.61  ? 37  PHE B CA  1 
ATOM   3430 C  C   . PHE B 2 39  ? 122.863 8.648   -19.667 1.00 67.67  ? 37  PHE B C   1 
ATOM   3431 O  O   . PHE B 2 39  ? 124.044 8.934   -19.455 1.00 71.62  ? 37  PHE B O   1 
ATOM   3432 C  CB  . PHE B 2 39  ? 121.295 7.937   -17.838 1.00 66.37  ? 37  PHE B CB  1 
ATOM   3433 C  CG  . PHE B 2 39  ? 120.481 6.838   -17.211 1.00 67.73  ? 37  PHE B CG  1 
ATOM   3434 C  CD1 . PHE B 2 39  ? 121.063 5.949   -16.321 1.00 66.90  ? 37  PHE B CD1 1 
ATOM   3435 C  CD2 . PHE B 2 39  ? 119.139 6.689   -17.518 1.00 65.79  ? 37  PHE B CD2 1 
ATOM   3436 C  CE1 . PHE B 2 39  ? 120.321 4.938   -15.745 1.00 68.95  ? 37  PHE B CE1 1 
ATOM   3437 C  CE2 . PHE B 2 39  ? 118.392 5.677   -16.945 1.00 61.97  ? 37  PHE B CE2 1 
ATOM   3438 C  CZ  . PHE B 2 39  ? 118.983 4.801   -16.057 1.00 64.72  ? 37  PHE B CZ  1 
ATOM   3439 N  N   . ARG B 2 40  ? 122.090 9.339   -20.501 1.00 69.92  ? 38  ARG B N   1 
ATOM   3440 C  CA  . ARG B 2 40  ? 122.577 10.539  -21.163 1.00 71.24  ? 38  ARG B CA  1 
ATOM   3441 C  C   . ARG B 2 40  ? 121.481 11.593  -21.182 1.00 71.76  ? 38  ARG B C   1 
ATOM   3442 O  O   . ARG B 2 40  ? 120.288 11.276  -21.152 1.00 73.36  ? 38  ARG B O   1 
ATOM   3443 C  CB  . ARG B 2 40  ? 123.064 10.228  -22.587 1.00 68.22  ? 38  ARG B CB  1 
ATOM   3444 C  CG  . ARG B 2 40  ? 121.962 10.127  -23.630 1.00 72.83  ? 38  ARG B CG  1 
ATOM   3445 C  CD  . ARG B 2 40  ? 122.528 9.667   -24.965 1.00 70.47  ? 38  ARG B CD  1 
ATOM   3446 N  NE  . ARG B 2 40  ? 121.490 9.206   -25.880 1.00 74.64  ? 38  ARG B NE  1 
ATOM   3447 C  CZ  . ARG B 2 40  ? 121.726 8.699   -27.082 1.00 81.51  ? 38  ARG B CZ  1 
ATOM   3448 N  NH1 . ARG B 2 40  ? 122.958 8.565   -27.547 1.00 82.71  ? 38  ARG B NH1 1 
ATOM   3449 N  NH2 . ARG B 2 40  ? 120.701 8.309   -27.835 1.00 83.92  ? 38  ARG B NH2 1 
ATOM   3450 N  N   . GLN B 2 41  ? 121.903 12.856  -21.224 1.00 72.67  ? 39  GLN B N   1 
ATOM   3451 C  CA  . GLN B 2 41  ? 120.988 13.995  -21.212 1.00 77.97  ? 39  GLN B CA  1 
ATOM   3452 C  C   . GLN B 2 41  ? 121.517 15.037  -22.188 1.00 76.95  ? 39  GLN B C   1 
ATOM   3453 O  O   . GLN B 2 41  ? 122.566 15.641  -21.944 1.00 76.03  ? 39  GLN B O   1 
ATOM   3454 C  CB  . GLN B 2 41  ? 120.843 14.579  -19.805 1.00 78.80  ? 39  GLN B CB  1 
ATOM   3455 C  CG  . GLN B 2 41  ? 120.072 15.891  -19.748 1.00 81.02  ? 39  GLN B CG  1 
ATOM   3456 C  CD  . GLN B 2 41  ? 119.286 16.054  -18.458 1.00 77.52  ? 39  GLN B CD  1 
ATOM   3457 O  OE1 . GLN B 2 41  ? 119.787 15.768  -17.370 1.00 72.82  ? 39  GLN B OE1 1 
ATOM   3458 N  NE2 . GLN B 2 41  ? 118.052 16.530  -18.574 1.00 77.88  ? 39  GLN B NE2 1 
ATOM   3459 N  N   . ALA B 2 42  ? 120.798 15.243  -23.288 1.00 79.05  ? 40  ALA B N   1 
ATOM   3460 C  CA  . ALA B 2 42  ? 121.195 16.212  -24.296 1.00 87.81  ? 40  ALA B CA  1 
ATOM   3461 C  C   . ALA B 2 42  ? 120.664 17.600  -23.944 1.00 93.13  ? 40  ALA B C   1 
ATOM   3462 O  O   . ALA B 2 42  ? 119.666 17.724  -23.227 1.00 95.36  ? 40  ALA B O   1 
ATOM   3463 C  CB  . ALA B 2 42  ? 120.678 15.792  -25.670 1.00 96.03  ? 40  ALA B CB  1 
ATOM   3464 N  N   . PRO B 2 43  ? 121.316 18.669  -24.424 1.00 102.24 ? 41  PRO B N   1 
ATOM   3465 C  CA  . PRO B 2 43  ? 120.830 20.022  -24.120 1.00 108.57 ? 41  PRO B CA  1 
ATOM   3466 C  C   . PRO B 2 43  ? 119.451 20.291  -24.698 1.00 106.69 ? 41  PRO B C   1 
ATOM   3467 O  O   . PRO B 2 43  ? 119.285 20.385  -25.918 1.00 104.82 ? 41  PRO B O   1 
ATOM   3468 C  CB  . PRO B 2 43  ? 121.892 20.932  -24.753 1.00 110.97 ? 41  PRO B CB  1 
ATOM   3469 C  CG  . PRO B 2 43  ? 122.577 20.078  -25.766 1.00 110.96 ? 41  PRO B CG  1 
ATOM   3470 C  CD  . PRO B 2 43  ? 122.570 18.697  -25.195 1.00 104.68 ? 41  PRO B CD  1 
ATOM   3471 N  N   . GLY B 2 44  ? 118.456 20.419  -23.823 1.00 99.95  ? 42  GLY B N   1 
ATOM   3472 C  CA  . GLY B 2 44  ? 117.081 20.650  -24.217 1.00 93.92  ? 42  GLY B CA  1 
ATOM   3473 C  C   . GLY B 2 44  ? 116.136 19.498  -23.956 1.00 97.28  ? 42  GLY B C   1 
ATOM   3474 O  O   . GLY B 2 44  ? 114.920 19.679  -24.096 1.00 93.18  ? 42  GLY B O   1 
ATOM   3475 N  N   . LYS B 2 45  ? 116.643 18.322  -23.603 1.00 92.57  ? 43  LYS B N   1 
ATOM   3476 C  CA  . LYS B 2 45  ? 115.821 17.151  -23.325 1.00 83.96  ? 43  LYS B CA  1 
ATOM   3477 C  C   . LYS B 2 45  ? 116.117 16.649  -21.912 1.00 81.83  ? 43  LYS B C   1 
ATOM   3478 O  O   . LYS B 2 45  ? 116.903 17.245  -21.170 1.00 82.14  ? 43  LYS B O   1 
ATOM   3479 C  CB  . LYS B 2 45  ? 116.052 16.058  -24.374 1.00 91.91  ? 43  LYS B CB  1 
ATOM   3480 C  CG  . LYS B 2 45  ? 116.417 16.583  -25.756 1.00 102.84 ? 43  LYS B CG  1 
ATOM   3481 C  CD  . LYS B 2 45  ? 117.112 15.512  -26.581 1.00 109.33 ? 43  LYS B CD  1 
ATOM   3482 C  CE  . LYS B 2 45  ? 116.267 14.244  -26.669 1.00 113.30 ? 43  LYS B CE  1 
ATOM   3483 N  NZ  . LYS B 2 45  ? 115.079 14.400  -27.557 1.00 103.76 ? 43  LYS B NZ  1 
ATOM   3484 N  N   . GLU B 2 46  ? 115.480 15.539  -21.542 1.00 82.50  ? 44  GLU B N   1 
ATOM   3485 C  CA  . GLU B 2 46  ? 115.634 14.965  -20.215 1.00 79.45  ? 44  GLU B CA  1 
ATOM   3486 C  C   . GLU B 2 46  ? 116.559 13.754  -20.278 1.00 81.65  ? 44  GLU B C   1 
ATOM   3487 O  O   . GLU B 2 46  ? 117.019 13.339  -21.345 1.00 81.94  ? 44  GLU B O   1 
ATOM   3488 C  CB  . GLU B 2 46  ? 114.282 14.577  -19.609 1.00 84.79  ? 44  GLU B CB  1 
ATOM   3489 C  CG  . GLU B 2 46  ? 113.329 13.831  -20.527 1.00 88.33  ? 44  GLU B CG  1 
ATOM   3490 C  CD  . GLU B 2 46  ? 111.920 13.773  -19.960 1.00 99.80  ? 44  GLU B CD  1 
ATOM   3491 O  OE1 . GLU B 2 46  ? 111.772 13.815  -18.718 1.00 90.51  ? 44  GLU B OE1 1 
ATOM   3492 O  OE2 . GLU B 2 46  ? 110.961 13.692  -20.753 1.00 97.43  ? 44  GLU B OE2 1 
ATOM   3493 N  N   . ARG B 2 47  ? 116.835 13.187  -19.107 1.00 76.08  ? 45  ARG B N   1 
ATOM   3494 C  CA  . ARG B 2 47  ? 117.701 12.019  -19.004 1.00 76.64  ? 45  ARG B CA  1 
ATOM   3495 C  C   . ARG B 2 47  ? 117.047 10.829  -19.695 1.00 78.03  ? 45  ARG B C   1 
ATOM   3496 O  O   . ARG B 2 47  ? 115.918 10.452  -19.361 1.00 81.31  ? 45  ARG B O   1 
ATOM   3497 C  CB  . ARG B 2 47  ? 117.974 11.696  -17.539 1.00 76.57  ? 45  ARG B CB  1 
ATOM   3498 C  CG  . ARG B 2 47  ? 119.331 12.146  -17.031 1.00 76.03  ? 45  ARG B CG  1 
ATOM   3499 C  CD  . ARG B 2 47  ? 119.407 11.983  -15.522 1.00 75.79  ? 45  ARG B CD  1 
ATOM   3500 N  NE  . ARG B 2 47  ? 120.692 12.392  -14.968 1.00 78.59  ? 45  ARG B NE  1 
ATOM   3501 C  CZ  . ARG B 2 47  ? 120.892 12.679  -13.689 1.00 85.02  ? 45  ARG B CZ  1 
ATOM   3502 N  NH1 . ARG B 2 47  ? 119.905 12.641  -12.809 1.00 80.90  ? 45  ARG B NH1 1 
ATOM   3503 N  NH2 . ARG B 2 47  ? 122.112 13.024  -13.284 1.00 88.32  ? 45  ARG B NH2 1 
ATOM   3504 N  N   . GLU B 2 48  ? 117.753 10.238  -20.655 1.00 75.55  ? 46  GLU B N   1 
ATOM   3505 C  CA  . GLU B 2 48  ? 117.276 9.067   -21.375 1.00 73.64  ? 46  GLU B CA  1 
ATOM   3506 C  C   . GLU B 2 48  ? 118.201 7.885   -21.114 1.00 70.84  ? 46  GLU B C   1 
ATOM   3507 O  O   . GLU B 2 48  ? 119.405 8.049   -20.892 1.00 70.86  ? 46  GLU B O   1 
ATOM   3508 C  CB  . GLU B 2 48  ? 117.168 9.343   -22.886 1.00 67.71  ? 46  GLU B CB  1 
ATOM   3509 C  CG  . GLU B 2 48  ? 118.437 9.079   -23.685 1.00 80.05  ? 46  GLU B CG  1 
ATOM   3510 C  CD  . GLU B 2 48  ? 118.305 9.487   -25.143 1.00 86.02  ? 46  GLU B CD  1 
ATOM   3511 O  OE1 . GLU B 2 48  ? 118.381 10.699  -25.437 1.00 87.77  ? 46  GLU B OE1 1 
ATOM   3512 O  OE2 . GLU B 2 48  ? 118.123 8.593   -25.997 1.00 82.96  ? 46  GLU B OE2 1 
ATOM   3513 N  N   . PHE B 2 49  ? 117.616 6.691   -21.123 1.00 73.51  ? 47  PHE B N   1 
ATOM   3514 C  CA  . PHE B 2 49  ? 118.381 5.472   -20.900 1.00 64.06  ? 47  PHE B CA  1 
ATOM   3515 C  C   . PHE B 2 49  ? 119.305 5.192   -22.079 1.00 65.60  ? 47  PHE B C   1 
ATOM   3516 O  O   . PHE B 2 49  ? 118.964 5.456   -23.235 1.00 67.36  ? 47  PHE B O   1 
ATOM   3517 C  CB  . PHE B 2 49  ? 117.427 4.298   -20.681 1.00 67.37  ? 47  PHE B CB  1 
ATOM   3518 C  CG  . PHE B 2 49  ? 118.101 2.955   -20.651 1.00 62.71  ? 47  PHE B CG  1 
ATOM   3519 C  CD1 . PHE B 2 49  ? 118.597 2.447   -19.464 1.00 58.72  ? 47  PHE B CD1 1 
ATOM   3520 C  CD2 . PHE B 2 49  ? 118.226 2.195   -21.805 1.00 65.31  ? 47  PHE B CD2 1 
ATOM   3521 C  CE1 . PHE B 2 49  ? 119.209 1.213   -19.425 1.00 63.72  ? 47  PHE B CE1 1 
ATOM   3522 C  CE2 . PHE B 2 49  ? 118.837 0.958   -21.772 1.00 68.61  ? 47  PHE B CE2 1 
ATOM   3523 C  CZ  . PHE B 2 49  ? 119.328 0.466   -20.580 1.00 70.64  ? 47  PHE B CZ  1 
ATOM   3524 N  N   . VAL B 2 50  ? 120.483 4.645   -21.779 1.00 68.89  ? 48  VAL B N   1 
ATOM   3525 C  CA  . VAL B 2 50  ? 121.460 4.306   -22.808 1.00 65.93  ? 48  VAL B CA  1 
ATOM   3526 C  C   . VAL B 2 50  ? 121.771 2.816   -22.755 1.00 66.20  ? 48  VAL B C   1 
ATOM   3527 O  O   . VAL B 2 50  ? 121.520 2.082   -23.718 1.00 65.57  ? 48  VAL B O   1 
ATOM   3528 C  CB  . VAL B 2 50  ? 122.746 5.137   -22.652 1.00 62.70  ? 48  VAL B CB  1 
ATOM   3529 C  CG1 . VAL B 2 50  ? 123.770 4.729   -23.699 1.00 73.32  ? 48  VAL B CG1 1 
ATOM   3530 C  CG2 . VAL B 2 50  ? 122.433 6.618   -22.754 1.00 66.77  ? 48  VAL B CG2 1 
ATOM   3531 N  N   . ALA B 2 51  ? 122.315 2.358   -21.630 1.00 63.21  ? 49  ALA B N   1 
ATOM   3532 C  CA  . ALA B 2 51  ? 122.689 0.961   -21.476 1.00 63.22  ? 49  ALA B CA  1 
ATOM   3533 C  C   . ALA B 2 51  ? 122.666 0.599   -20.000 1.00 64.45  ? 49  ALA B C   1 
ATOM   3534 O  O   . ALA B 2 51  ? 122.746 1.467   -19.127 1.00 67.62  ? 49  ALA B O   1 
ATOM   3535 C  CB  . ALA B 2 51  ? 124.069 0.674   -22.079 1.00 74.63  ? 49  ALA B CB  1 
ATOM   3536 N  N   . ARG B 2 52  ? 122.548 -0.699  -19.730 1.00 67.50  ? 50  ARG B N   1 
ATOM   3537 C  CA  . ARG B 2 52  ? 122.497 -1.200  -18.365 1.00 73.66  ? 50  ARG B CA  1 
ATOM   3538 C  C   . ARG B 2 52  ? 123.083 -2.602  -18.325 1.00 72.88  ? 50  ARG B C   1 
ATOM   3539 O  O   . ARG B 2 52  ? 122.775 -3.435  -19.180 1.00 64.72  ? 50  ARG B O   1 
ATOM   3540 C  CB  . ARG B 2 52  ? 121.060 -1.225  -17.824 1.00 75.83  ? 50  ARG B CB  1 
ATOM   3541 C  CG  . ARG B 2 52  ? 120.857 -2.176  -16.651 1.00 74.24  ? 50  ARG B CG  1 
ATOM   3542 C  CD  . ARG B 2 52  ? 119.435 -2.141  -16.116 1.00 78.39  ? 50  ARG B CD  1 
ATOM   3543 N  NE  . ARG B 2 52  ? 118.710 -3.366  -16.432 1.00 77.92  ? 50  ARG B NE  1 
ATOM   3544 C  CZ  . ARG B 2 52  ? 117.801 -3.476  -17.391 1.00 70.91  ? 50  ARG B CZ  1 
ATOM   3545 N  NH1 . ARG B 2 52  ? 117.445 -2.437  -18.129 1.00 76.35  ? 50  ARG B NH1 1 
ATOM   3546 N  NH2 . ARG B 2 52  ? 117.229 -4.656  -17.610 1.00 73.97  ? 50  ARG B NH2 1 
ATOM   3547 N  N   . ILE B 2 53  ? 123.915 -2.857  -17.318 1.00 71.42  ? 51  ILE B N   1 
ATOM   3548 C  CA  . ILE B 2 53  ? 124.451 -4.184  -17.044 1.00 79.81  ? 51  ILE B CA  1 
ATOM   3549 C  C   . ILE B 2 53  ? 123.986 -4.598  -15.656 1.00 82.74  ? 51  ILE B C   1 
ATOM   3550 O  O   . ILE B 2 53  ? 123.919 -3.772  -14.738 1.00 81.26  ? 51  ILE B O   1 
ATOM   3551 C  CB  . ILE B 2 53  ? 125.992 -4.231  -17.170 1.00 89.33  ? 51  ILE B CB  1 
ATOM   3552 C  CG1 . ILE B 2 53  ? 126.454 -5.642  -17.544 1.00 92.20  ? 51  ILE B CG1 1 
ATOM   3553 C  CG2 . ILE B 2 53  ? 126.684 -3.735  -15.903 1.00 86.00  ? 51  ILE B CG2 1 
ATOM   3554 C  CD1 . ILE B 2 53  ? 127.958 -5.812  -17.564 1.00 89.93  ? 51  ILE B CD1 1 
ATOM   3555 N  N   . SER B 2 54  ? 123.627 -5.870  -15.515 1.00 90.20  ? 52  SER B N   1 
ATOM   3556 C  CA  . SER B 2 54  ? 123.034 -6.351  -14.279 1.00 94.88  ? 52  SER B CA  1 
ATOM   3557 C  C   . SER B 2 54  ? 124.114 -6.655  -13.246 1.00 95.65  ? 52  SER B C   1 
ATOM   3558 O  O   . SER B 2 54  ? 125.316 -6.525  -13.496 1.00 93.42  ? 52  SER B O   1 
ATOM   3559 C  CB  . SER B 2 54  ? 122.175 -7.584  -14.547 1.00 95.30  ? 52  SER B CB  1 
ATOM   3560 O  OG  . SER B 2 54  ? 122.919 -8.774  -14.353 1.00 103.63 ? 52  SER B OG  1 
ATOM   3561 N  N   . GLU B 2 55  ? 123.669 -7.064  -12.060 1.00 99.74  ? 53  GLU B N   1 
ATOM   3562 C  CA  . GLU B 2 55  ? 124.559 -7.413  -10.964 1.00 103.25 ? 53  GLU B CA  1 
ATOM   3563 C  C   . GLU B 2 55  ? 124.769 -8.914  -10.830 1.00 107.35 ? 53  GLU B C   1 
ATOM   3564 O  O   . GLU B 2 55  ? 125.598 -9.339  -10.018 1.00 111.45 ? 53  GLU B O   1 
ATOM   3565 C  CB  . GLU B 2 55  ? 124.029 -6.842  -9.641  1.00 101.42 ? 53  GLU B CB  1 
ATOM   3566 C  CG  . GLU B 2 55  ? 122.973 -7.690  -8.945  1.00 102.99 ? 53  GLU B CG  1 
ATOM   3567 C  CD  . GLU B 2 55  ? 121.602 -7.564  -9.583  1.00 101.65 ? 53  GLU B CD  1 
ATOM   3568 O  OE1 . GLU B 2 55  ? 121.429 -6.691  -10.460 1.00 101.24 ? 53  GLU B OE1 1 
ATOM   3569 O  OE2 . GLU B 2 55  ? 120.694 -8.333  -9.201  1.00 101.19 ? 53  GLU B OE2 1 
ATOM   3570 N  N   . SER B 2 56  ? 124.048 -9.722  -11.604 1.00 104.21 ? 54  SER B N   1 
ATOM   3571 C  CA  . SER B 2 56  ? 124.067 -11.165 -11.421 1.00 105.36 ? 54  SER B CA  1 
ATOM   3572 C  C   . SER B 2 56  ? 124.660 -11.827 -12.657 1.00 107.53 ? 54  SER B C   1 
ATOM   3573 O  O   . SER B 2 56  ? 125.884 -11.965 -12.761 1.00 107.80 ? 54  SER B O   1 
ATOM   3574 C  CB  . SER B 2 56  ? 122.655 -11.684 -11.135 1.00 110.72 ? 54  SER B CB  1 
ATOM   3575 O  OG  . SER B 2 56  ? 121.803 -11.498 -12.253 1.00 114.27 ? 54  SER B OG  1 
ATOM   3576 N  N   . ARG B 2 57  ? 123.811 -12.237 -13.599 1.00 106.79 ? 55  ARG B N   1 
ATOM   3577 C  CA  . ARG B 2 57  ? 124.260 -13.004 -14.756 1.00 113.85 ? 55  ARG B CA  1 
ATOM   3578 C  C   . ARG B 2 57  ? 125.036 -12.167 -15.770 1.00 110.77 ? 55  ARG B C   1 
ATOM   3579 O  O   . ARG B 2 57  ? 125.424 -12.702 -16.817 1.00 109.21 ? 55  ARG B O   1 
ATOM   3580 C  CB  . ARG B 2 57  ? 123.054 -13.656 -15.437 1.00 117.22 ? 55  ARG B CB  1 
ATOM   3581 C  CG  . ARG B 2 57  ? 121.915 -13.999 -14.478 1.00 123.71 ? 55  ARG B CG  1 
ATOM   3582 C  CD  . ARG B 2 57  ? 120.578 -14.130 -15.206 1.00 129.93 ? 55  ARG B CD  1 
ATOM   3583 N  NE  . ARG B 2 57  ? 119.446 -13.819 -14.337 1.00 137.76 ? 55  ARG B NE  1 
ATOM   3584 C  CZ  . ARG B 2 57  ? 118.172 -13.949 -14.683 1.00 139.29 ? 55  ARG B CZ  1 
ATOM   3585 N  NH1 . ARG B 2 57  ? 117.820 -14.392 -15.878 1.00 138.94 ? 55  ARG B NH1 1 
ATOM   3586 N  NH2 . ARG B 2 57  ? 117.225 -13.628 -13.804 1.00 131.42 ? 55  ARG B NH2 1 
ATOM   3587 N  N   . GLY B 2 58  ? 125.284 -10.889 -15.491 1.00 110.47 ? 56  GLY B N   1 
ATOM   3588 C  CA  . GLY B 2 58  ? 125.948 -10.036 -16.458 1.00 104.40 ? 56  GLY B CA  1 
ATOM   3589 C  C   . GLY B 2 58  ? 125.102 -9.666  -17.654 1.00 102.95 ? 56  GLY B C   1 
ATOM   3590 O  O   . GLY B 2 58  ? 125.650 -9.320  -18.703 1.00 96.48  ? 56  GLY B O   1 
ATOM   3591 N  N   . THR B 2 59  ? 123.778 -9.734  -17.528 1.00 101.43 ? 57  THR B N   1 
ATOM   3592 C  CA  . THR B 2 59  ? 122.896 -9.401  -18.637 1.00 94.91  ? 57  THR B CA  1 
ATOM   3593 C  C   . THR B 2 59  ? 122.997 -7.919  -18.979 1.00 89.76  ? 57  THR B C   1 
ATOM   3594 O  O   . THR B 2 59  ? 123.323 -7.081  -18.132 1.00 87.29  ? 57  THR B O   1 
ATOM   3595 C  CB  . THR B 2 59  ? 121.447 -9.766  -18.306 1.00 100.61 ? 57  THR B CB  1 
ATOM   3596 O  OG1 . THR B 2 59  ? 121.193 -9.526  -16.916 1.00 104.57 ? 57  THR B OG1 1 
ATOM   3597 C  CG2 . THR B 2 59  ? 121.181 -11.231 -18.621 1.00 102.33 ? 57  THR B CG2 1 
ATOM   3598 N  N   . THR B 2 60  ? 122.710 -7.598  -20.238 1.00 86.62  ? 58  THR B N   1 
ATOM   3599 C  CA  . THR B 2 60  ? 122.814 -6.235  -20.732 1.00 82.88  ? 58  THR B CA  1 
ATOM   3600 C  C   . THR B 2 60  ? 121.501 -5.808  -21.371 1.00 80.96  ? 58  THR B C   1 
ATOM   3601 O  O   . THR B 2 60  ? 120.735 -6.632  -21.878 1.00 81.83  ? 58  THR B O   1 
ATOM   3602 C  CB  . THR B 2 60  ? 123.956 -6.090  -21.750 1.00 82.33  ? 58  THR B CB  1 
ATOM   3603 O  OG1 . THR B 2 60  ? 124.033 -7.272  -22.557 1.00 89.46  ? 58  THR B OG1 1 
ATOM   3604 C  CG2 . THR B 2 60  ? 125.282 -5.888  -21.036 1.00 72.18  ? 58  THR B CG2 1 
ATOM   3605 N  N   . ASP B 2 61  ? 121.254 -4.500  -21.340 1.00 77.27  ? 59  ASP B N   1 
ATOM   3606 C  CA  . ASP B 2 61  ? 120.096 -3.889  -21.975 1.00 73.99  ? 59  ASP B CA  1 
ATOM   3607 C  C   . ASP B 2 61  ? 120.548 -2.605  -22.650 1.00 70.03  ? 59  ASP B C   1 
ATOM   3608 O  O   . ASP B 2 61  ? 121.385 -1.876  -22.110 1.00 67.47  ? 59  ASP B O   1 
ATOM   3609 C  CB  . ASP B 2 61  ? 118.978 -3.597  -20.963 1.00 69.76  ? 59  ASP B CB  1 
ATOM   3610 C  CG  . ASP B 2 61  ? 117.627 -3.390  -21.628 1.00 76.01  ? 59  ASP B CG  1 
ATOM   3611 O  OD1 . ASP B 2 61  ? 117.394 -3.984  -22.703 1.00 83.14  ? 59  ASP B OD1 1 
ATOM   3612 O  OD2 . ASP B 2 61  ? 116.799 -2.634  -21.077 1.00 73.13  ? 59  ASP B OD2 1 
ATOM   3613 N  N   . TYR B 2 62  ? 120.001 -2.336  -23.832 1.00 67.50  ? 60  TYR B N   1 
ATOM   3614 C  CA  . TYR B 2 62  ? 120.401 -1.178  -24.615 1.00 72.38  ? 60  TYR B CA  1 
ATOM   3615 C  C   . TYR B 2 62  ? 119.179 -0.488  -25.197 1.00 72.26  ? 60  TYR B C   1 
ATOM   3616 O  O   . TYR B 2 62  ? 118.242 -1.145  -25.659 1.00 77.93  ? 60  TYR B O   1 
ATOM   3617 C  CB  . TYR B 2 62  ? 121.357 -1.562  -25.754 1.00 79.48  ? 60  TYR B CB  1 
ATOM   3618 C  CG  . TYR B 2 62  ? 122.620 -2.256  -25.300 1.00 72.18  ? 60  TYR B CG  1 
ATOM   3619 C  CD1 . TYR B 2 62  ? 123.749 -1.525  -24.956 1.00 69.09  ? 60  TYR B CD1 1 
ATOM   3620 C  CD2 . TYR B 2 62  ? 122.686 -3.640  -25.219 1.00 76.55  ? 60  TYR B CD2 1 
ATOM   3621 C  CE1 . TYR B 2 62  ? 124.908 -2.152  -24.541 1.00 75.97  ? 60  TYR B CE1 1 
ATOM   3622 C  CE2 . TYR B 2 62  ? 123.842 -4.277  -24.806 1.00 76.54  ? 60  TYR B CE2 1 
ATOM   3623 C  CZ  . TYR B 2 62  ? 124.949 -3.528  -24.467 1.00 80.75  ? 60  TYR B CZ  1 
ATOM   3624 O  OH  . TYR B 2 62  ? 126.102 -4.157  -24.056 1.00 84.35  ? 60  TYR B OH  1 
ATOM   3625 N  N   . ALA B 2 63  ? 119.206 0.842   -25.173 1.00 73.15  ? 61  ALA B N   1 
ATOM   3626 C  CA  . ALA B 2 63  ? 118.234 1.623   -25.919 1.00 74.28  ? 61  ALA B CA  1 
ATOM   3627 C  C   . ALA B 2 63  ? 118.377 1.333   -27.406 1.00 80.18  ? 61  ALA B C   1 
ATOM   3628 O  O   . ALA B 2 63  ? 119.471 1.063   -27.908 1.00 89.66  ? 61  ALA B O   1 
ATOM   3629 C  CB  . ALA B 2 63  ? 118.417 3.116   -25.649 1.00 69.56  ? 61  ALA B CB  1 
ATOM   3630 N  N   . ASP B 2 64  ? 117.247 1.387   -28.113 1.00 83.22  ? 62  ASP B N   1 
ATOM   3631 C  CA  . ASP B 2 64  ? 117.238 1.049   -29.530 1.00 88.56  ? 62  ASP B CA  1 
ATOM   3632 C  C   . ASP B 2 64  ? 118.151 1.950   -30.351 1.00 89.81  ? 62  ASP B C   1 
ATOM   3633 O  O   . ASP B 2 64  ? 118.547 1.564   -31.457 1.00 92.63  ? 62  ASP B O   1 
ATOM   3634 C  CB  . ASP B 2 64  ? 115.808 1.130   -30.066 1.00 90.20  ? 62  ASP B CB  1 
ATOM   3635 C  CG  . ASP B 2 64  ? 114.955 -0.042  -29.626 1.00 90.21  ? 62  ASP B CG  1 
ATOM   3636 O  OD1 . ASP B 2 64  ? 115.498 -0.964  -28.981 1.00 99.54  ? 62  ASP B OD1 1 
ATOM   3637 O  OD2 . ASP B 2 64  ? 113.742 -0.039  -29.922 1.00 92.71  ? 62  ASP B OD2 1 
ATOM   3638 N  N   . SER B 2 65  ? 118.498 3.133   -29.840 1.00 94.60  ? 63  SER B N   1 
ATOM   3639 C  CA  . SER B 2 65  ? 119.363 4.041   -30.581 1.00 93.50  ? 63  SER B CA  1 
ATOM   3640 C  C   . SER B 2 65  ? 120.830 3.654   -30.528 1.00 86.31  ? 63  SER B C   1 
ATOM   3641 O  O   . SER B 2 65  ? 121.596 4.066   -31.405 1.00 85.85  ? 63  SER B O   1 
ATOM   3642 C  CB  . SER B 2 65  ? 119.214 5.467   -30.040 1.00 91.68  ? 63  SER B CB  1 
ATOM   3643 O  OG  . SER B 2 65  ? 119.346 5.498   -28.631 1.00 90.90  ? 63  SER B OG  1 
ATOM   3644 N  N   . VAL B 2 66  ? 121.240 2.877   -29.530 1.00 80.80  ? 64  VAL B N   1 
ATOM   3645 C  CA  . VAL B 2 66  ? 122.635 2.498   -29.371 1.00 85.25  ? 64  VAL B CA  1 
ATOM   3646 C  C   . VAL B 2 66  ? 122.868 1.002   -29.497 1.00 85.43  ? 64  VAL B C   1 
ATOM   3647 O  O   . VAL B 2 66  ? 124.017 0.560   -29.392 1.00 89.01  ? 64  VAL B O   1 
ATOM   3648 C  CB  . VAL B 2 66  ? 123.197 3.019   -28.033 1.00 85.93  ? 64  VAL B CB  1 
ATOM   3649 C  CG1 . VAL B 2 66  ? 122.784 4.468   -27.814 1.00 82.19  ? 64  VAL B CG1 1 
ATOM   3650 C  CG2 . VAL B 2 66  ? 122.727 2.147   -26.882 1.00 84.61  ? 64  VAL B CG2 1 
ATOM   3651 N  N   . LYS B 2 67  ? 121.824 0.206   -29.717 1.00 83.75  ? 65  LYS B N   1 
ATOM   3652 C  CA  . LYS B 2 67  ? 122.020 -1.232  -29.844 1.00 86.20  ? 65  LYS B CA  1 
ATOM   3653 C  C   . LYS B 2 67  ? 122.832 -1.541  -31.096 1.00 88.10  ? 65  LYS B C   1 
ATOM   3654 O  O   . LYS B 2 67  ? 122.577 -0.989  -32.172 1.00 89.25  ? 65  LYS B O   1 
ATOM   3655 C  CB  . LYS B 2 67  ? 120.677 -1.963  -29.867 1.00 88.82  ? 65  LYS B CB  1 
ATOM   3656 C  CG  . LYS B 2 67  ? 119.733 -1.562  -30.987 1.00 95.39  ? 65  LYS B CG  1 
ATOM   3657 C  CD  . LYS B 2 67  ? 118.607 -2.577  -31.124 1.00 100.97 ? 65  LYS B CD  1 
ATOM   3658 C  CE  . LYS B 2 67  ? 117.963 -2.520  -32.499 1.00 107.78 ? 65  LYS B CE  1 
ATOM   3659 N  NZ  . LYS B 2 67  ? 116.802 -3.449  -32.603 1.00 111.94 ? 65  LYS B NZ  1 
ATOM   3660 N  N   . GLY B 2 68  ? 123.813 -2.425  -30.949 1.00 90.23  ? 66  GLY B N   1 
ATOM   3661 C  CA  . GLY B 2 68  ? 124.751 -2.724  -32.011 1.00 93.62  ? 66  GLY B CA  1 
ATOM   3662 C  C   . GLY B 2 68  ? 125.892 -1.731  -32.115 1.00 87.11  ? 66  GLY B C   1 
ATOM   3663 O  O   . GLY B 2 68  ? 127.000 -2.100  -32.515 1.00 95.91  ? 66  GLY B O   1 
ATOM   3664 N  N   . ARG B 2 69  ? 125.643 -0.471  -31.751 1.00 85.97  ? 67  ARG B N   1 
ATOM   3665 C  CA  . ARG B 2 69  ? 126.693 0.541   -31.777 1.00 86.66  ? 67  ARG B CA  1 
ATOM   3666 C  C   . ARG B 2 69  ? 127.405 0.677   -30.436 1.00 88.18  ? 67  ARG B C   1 
ATOM   3667 O  O   . ARG B 2 69  ? 128.632 0.822   -30.399 1.00 91.08  ? 67  ARG B O   1 
ATOM   3668 C  CB  . ARG B 2 69  ? 126.121 1.899   -32.197 1.00 85.97  ? 67  ARG B CB  1 
ATOM   3669 C  CG  . ARG B 2 69  ? 125.440 1.897   -33.557 1.00 88.57  ? 67  ARG B CG  1 
ATOM   3670 C  CD  . ARG B 2 69  ? 125.116 3.310   -34.031 1.00 88.79  ? 67  ARG B CD  1 
ATOM   3671 N  NE  . ARG B 2 69  ? 124.128 3.980   -33.194 1.00 87.74  ? 67  ARG B NE  1 
ATOM   3672 C  CZ  . ARG B 2 69  ? 124.373 5.063   -32.469 1.00 85.85  ? 67  ARG B CZ  1 
ATOM   3673 N  NH1 . ARG B 2 69  ? 125.574 5.619   -32.439 1.00 86.55  ? 67  ARG B NH1 1 
ATOM   3674 N  NH2 . ARG B 2 69  ? 123.389 5.602   -31.754 1.00 90.15  ? 67  ARG B NH2 1 
ATOM   3675 N  N   . PHE B 2 70  ? 126.662 0.636   -29.333 1.00 86.95  ? 68  PHE B N   1 
ATOM   3676 C  CA  . PHE B 2 70  ? 127.221 0.814   -28.001 1.00 87.52  ? 68  PHE B CA  1 
ATOM   3677 C  C   . PHE B 2 70  ? 127.265 -0.526  -27.279 1.00 81.67  ? 68  PHE B C   1 
ATOM   3678 O  O   . PHE B 2 70  ? 126.389 -1.377  -27.459 1.00 83.30  ? 68  PHE B O   1 
ATOM   3679 C  CB  . PHE B 2 70  ? 126.410 1.818   -27.169 1.00 85.24  ? 68  PHE B CB  1 
ATOM   3680 C  CG  . PHE B 2 70  ? 126.548 3.258   -27.615 1.00 80.98  ? 68  PHE B CG  1 
ATOM   3681 C  CD1 . PHE B 2 70  ? 126.894 3.580   -28.917 1.00 80.53  ? 68  PHE B CD1 1 
ATOM   3682 C  CD2 . PHE B 2 70  ? 126.309 4.291   -26.722 1.00 82.16  ? 68  PHE B CD2 1 
ATOM   3683 C  CE1 . PHE B 2 70  ? 127.009 4.897   -29.318 1.00 82.48  ? 68  PHE B CE1 1 
ATOM   3684 C  CE2 . PHE B 2 70  ? 126.421 5.612   -27.118 1.00 86.63  ? 68  PHE B CE2 1 
ATOM   3685 C  CZ  . PHE B 2 70  ? 126.773 5.915   -28.417 1.00 83.71  ? 68  PHE B CZ  1 
ATOM   3686 N  N   . THR B 2 71  ? 128.295 -0.708  -26.455 1.00 81.54  ? 69  THR B N   1 
ATOM   3687 C  CA  . THR B 2 71  ? 128.455 -1.929  -25.672 1.00 78.18  ? 69  THR B CA  1 
ATOM   3688 C  C   . THR B 2 71  ? 128.886 -1.559  -24.262 1.00 78.72  ? 69  THR B C   1 
ATOM   3689 O  O   . THR B 2 71  ? 129.903 -0.883  -24.081 1.00 78.84  ? 69  THR B O   1 
ATOM   3690 C  CB  . THR B 2 71  ? 129.481 -2.868  -26.314 1.00 79.95  ? 69  THR B CB  1 
ATOM   3691 O  OG1 . THR B 2 71  ? 128.937 -3.426  -27.517 1.00 79.38  ? 69  THR B OG1 1 
ATOM   3692 C  CG2 . THR B 2 71  ? 129.845 -3.993  -25.356 1.00 82.27  ? 69  THR B CG2 1 
ATOM   3693 N  N   . ILE B 2 72  ? 128.116 -2.000  -23.270 1.00 78.16  ? 70  ILE B N   1 
ATOM   3694 C  CA  . ILE B 2 72  ? 128.428 -1.770  -21.864 1.00 75.32  ? 70  ILE B CA  1 
ATOM   3695 C  C   . ILE B 2 72  ? 129.031 -3.040  -21.280 1.00 74.42  ? 70  ILE B C   1 
ATOM   3696 O  O   . ILE B 2 72  ? 128.623 -4.156  -21.625 1.00 78.98  ? 70  ILE B O   1 
ATOM   3697 C  CB  . ILE B 2 72  ? 127.176 -1.326  -21.081 1.00 76.07  ? 70  ILE B CB  1 
ATOM   3698 C  CG1 . ILE B 2 72  ? 127.513 -1.064  -19.611 1.00 76.63  ? 70  ILE B CG1 1 
ATOM   3699 C  CG2 . ILE B 2 72  ? 126.070 -2.362  -21.196 1.00 71.92  ? 70  ILE B CG2 1 
ATOM   3700 C  CD1 . ILE B 2 72  ? 126.298 -0.846  -18.737 1.00 71.65  ? 70  ILE B CD1 1 
ATOM   3701 N  N   . SER B 2 73  ? 130.019 -2.870  -20.404 1.00 76.48  ? 71  SER B N   1 
ATOM   3702 C  CA  . SER B 2 73  ? 130.667 -3.988  -19.736 1.00 83.78  ? 71  SER B CA  1 
ATOM   3703 C  C   . SER B 2 73  ? 131.054 -3.551  -18.332 1.00 85.57  ? 71  SER B C   1 
ATOM   3704 O  O   . SER B 2 73  ? 131.077 -2.358  -18.019 1.00 81.53  ? 71  SER B O   1 
ATOM   3705 C  CB  . SER B 2 73  ? 131.896 -4.478  -20.512 1.00 91.46  ? 71  SER B CB  1 
ATOM   3706 O  OG  . SER B 2 73  ? 132.985 -3.582  -20.363 1.00 90.20  ? 71  SER B OG  1 
ATOM   3707 N  N   . ARG B 2 74  ? 131.347 -4.532  -17.481 1.00 86.83  ? 72  ARG B N   1 
ATOM   3708 C  CA  . ARG B 2 74  ? 131.726 -4.249  -16.106 1.00 87.55  ? 72  ARG B CA  1 
ATOM   3709 C  C   . ARG B 2 74  ? 132.859 -5.171  -15.681 1.00 94.29  ? 72  ARG B C   1 
ATOM   3710 O  O   . ARG B 2 74  ? 133.027 -6.268  -16.219 1.00 96.56  ? 72  ARG B O   1 
ATOM   3711 C  CB  . ARG B 2 74  ? 130.525 -4.399  -15.159 1.00 91.30  ? 72  ARG B CB  1 
ATOM   3712 C  CG  . ARG B 2 74  ? 130.315 -5.796  -14.599 1.00 93.44  ? 72  ARG B CG  1 
ATOM   3713 C  CD  . ARG B 2 74  ? 128.953 -5.907  -13.935 1.00 95.85  ? 72  ARG B CD  1 
ATOM   3714 N  NE  . ARG B 2 74  ? 128.963 -5.385  -12.574 1.00 96.98  ? 72  ARG B NE  1 
ATOM   3715 C  CZ  . ARG B 2 74  ? 127.899 -4.892  -11.955 1.00 91.02  ? 72  ARG B CZ  1 
ATOM   3716 N  NH1 . ARG B 2 74  ? 126.720 -4.829  -12.551 1.00 90.70  ? 72  ARG B NH1 1 
ATOM   3717 N  NH2 . ARG B 2 74  ? 128.023 -4.444  -10.709 1.00 87.17  ? 72  ARG B NH2 1 
ATOM   3718 N  N   . ASP B 2 75  ? 133.642 -4.702  -14.711 1.00 94.61  ? 73  ASP B N   1 
ATOM   3719 C  CA  . ASP B 2 75  ? 134.717 -5.482  -14.104 1.00 94.38  ? 73  ASP B CA  1 
ATOM   3720 C  C   . ASP B 2 75  ? 134.595 -5.347  -12.594 1.00 94.83  ? 73  ASP B C   1 
ATOM   3721 O  O   . ASP B 2 75  ? 134.925 -4.297  -12.033 1.00 92.20  ? 73  ASP B O   1 
ATOM   3722 C  CB  . ASP B 2 75  ? 136.089 -5.013  -14.592 1.00 104.86 ? 73  ASP B CB  1 
ATOM   3723 C  CG  . ASP B 2 75  ? 137.230 -5.635  -13.810 1.00 107.08 ? 73  ASP B CG  1 
ATOM   3724 O  OD1 . ASP B 2 75  ? 137.686 -6.734  -14.191 1.00 107.50 ? 73  ASP B OD1 1 
ATOM   3725 O  OD2 . ASP B 2 75  ? 137.676 -5.023  -12.817 1.00 101.72 ? 73  ASP B OD2 1 
ATOM   3726 N  N   . ASN B 2 76  ? 134.125 -6.408  -11.936 1.00 95.67  ? 74  ASN B N   1 
ATOM   3727 C  CA  . ASN B 2 76  ? 133.960 -6.384  -10.489 1.00 101.14 ? 74  ASN B CA  1 
ATOM   3728 C  C   . ASN B 2 76  ? 135.280 -6.489  -9.736  1.00 104.88 ? 74  ASN B C   1 
ATOM   3729 O  O   . ASN B 2 76  ? 135.278 -6.378  -8.506  1.00 106.26 ? 74  ASN B O   1 
ATOM   3730 C  CB  . ASN B 2 76  ? 133.025 -7.514  -10.052 1.00 106.29 ? 74  ASN B CB  1 
ATOM   3731 C  CG  . ASN B 2 76  ? 131.587 -7.277  -10.475 1.00 102.73 ? 74  ASN B CG  1 
ATOM   3732 O  OD1 . ASN B 2 76  ? 131.113 -6.141  -10.495 1.00 99.31  ? 74  ASN B OD1 1 
ATOM   3733 N  ND2 . ASN B 2 76  ? 130.884 -8.352  -10.814 1.00 96.28  ? 74  ASN B ND2 1 
ATOM   3734 N  N   . ALA B 2 77  ? 136.398 -6.700  -10.436 1.00 107.47 ? 75  ALA B N   1 
ATOM   3735 C  CA  . ALA B 2 77  ? 137.696 -6.721  -9.768  1.00 102.66 ? 75  ALA B CA  1 
ATOM   3736 C  C   . ALA B 2 77  ? 138.134 -5.321  -9.355  1.00 103.46 ? 75  ALA B C   1 
ATOM   3737 O  O   . ALA B 2 77  ? 138.630 -5.124  -8.239  1.00 103.94 ? 75  ALA B O   1 
ATOM   3738 C  CB  . ALA B 2 77  ? 138.742 -7.364  -10.677 1.00 104.59 ? 75  ALA B CB  1 
ATOM   3739 N  N   . LYS B 2 78  ? 137.957 -4.337  -10.235 1.00 103.43 ? 76  LYS B N   1 
ATOM   3740 C  CA  . LYS B 2 78  ? 138.310 -2.955  -9.945  1.00 105.60 ? 76  LYS B CA  1 
ATOM   3741 C  C   . LYS B 2 78  ? 137.096 -2.078  -9.677  1.00 99.58  ? 76  LYS B C   1 
ATOM   3742 O  O   . LYS B 2 78  ? 137.258 -0.873  -9.453  1.00 95.96  ? 76  LYS B O   1 
ATOM   3743 C  CB  . LYS B 2 78  ? 139.133 -2.363  -11.096 1.00 109.27 ? 76  LYS B CB  1 
ATOM   3744 C  CG  . LYS B 2 78  ? 140.175 -3.309  -11.668 1.00 113.35 ? 76  LYS B CG  1 
ATOM   3745 C  CD  . LYS B 2 78  ? 141.025 -2.616  -12.720 1.00 119.40 ? 76  LYS B CD  1 
ATOM   3746 C  CE  . LYS B 2 78  ? 140.228 -2.352  -13.987 1.00 117.15 ? 76  LYS B CE  1 
ATOM   3747 N  NZ  . LYS B 2 78  ? 139.978 -3.604  -14.750 1.00 119.60 ? 76  LYS B NZ  1 
ATOM   3748 N  N   . ASN B 2 79  ? 135.891 -2.651  -9.691  1.00 101.50 ? 77  ASN B N   1 
ATOM   3749 C  CA  . ASN B 2 79  ? 134.646 -1.916  -9.463  1.00 94.94  ? 77  ASN B CA  1 
ATOM   3750 C  C   . ASN B 2 79  ? 134.478 -0.778  -10.468 1.00 92.11  ? 77  ASN B C   1 
ATOM   3751 O  O   . ASN B 2 79  ? 134.179 0.363   -10.109 1.00 88.50  ? 77  ASN B O   1 
ATOM   3752 C  CB  . ASN B 2 79  ? 134.562 -1.391  -8.025  1.00 92.38  ? 77  ASN B CB  1 
ATOM   3753 C  CG  . ASN B 2 79  ? 134.846 -2.464  -6.993  1.00 95.73  ? 77  ASN B CG  1 
ATOM   3754 O  OD1 . ASN B 2 79  ? 134.975 -3.643  -7.323  1.00 93.82  ? 77  ASN B OD1 1 
ATOM   3755 N  ND2 . ASN B 2 79  ? 134.936 -2.060  -5.731  1.00 99.69  ? 77  ASN B ND2 1 
ATOM   3756 N  N   . THR B 2 80  ? 134.682 -1.097  -11.744 1.00 90.73  ? 78  THR B N   1 
ATOM   3757 C  CA  . THR B 2 80  ? 134.498 -0.135  -12.819 1.00 91.12  ? 78  THR B CA  1 
ATOM   3758 C  C   . THR B 2 80  ? 133.571 -0.720  -13.876 1.00 87.44  ? 78  THR B C   1 
ATOM   3759 O  O   . THR B 2 80  ? 133.434 -1.939  -14.012 1.00 86.83  ? 78  THR B O   1 
ATOM   3760 C  CB  . THR B 2 80  ? 135.833 0.274   -13.467 1.00 98.92  ? 78  THR B CB  1 
ATOM   3761 O  OG1 . THR B 2 80  ? 136.155 -0.640  -14.522 1.00 101.76 ? 78  THR B OG1 1 
ATOM   3762 C  CG2 . THR B 2 80  ? 136.960 0.286   -12.445 1.00 92.69  ? 78  THR B CG2 1 
ATOM   3763 N  N   . ILE B 2 81  ? 132.934 0.176   -14.627 1.00 84.99  ? 79  ILE B N   1 
ATOM   3764 C  CA  . ILE B 2 81  ? 132.082 -0.176  -15.755 1.00 87.84  ? 79  ILE B CA  1 
ATOM   3765 C  C   . ILE B 2 81  ? 132.466 0.696   -16.942 1.00 84.67  ? 79  ILE B C   1 
ATOM   3766 O  O   . ILE B 2 81  ? 132.947 1.822   -16.778 1.00 81.02  ? 79  ILE B O   1 
ATOM   3767 C  CB  . ILE B 2 81  ? 130.581 -0.038  -15.404 1.00 85.72  ? 79  ILE B CB  1 
ATOM   3768 C  CG1 . ILE B 2 81  ? 130.232 1.406   -15.039 1.00 85.77  ? 79  ILE B CG1 1 
ATOM   3769 C  CG2 . ILE B 2 81  ? 130.209 -0.971  -14.270 1.00 81.78  ? 79  ILE B CG2 1 
ATOM   3770 C  CD1 . ILE B 2 81  ? 129.335 2.083   -16.028 1.00 81.19  ? 79  ILE B CD1 1 
ATOM   3771 N  N   . TYR B 2 82  ? 132.256 0.167   -18.147 1.00 84.06  ? 80  TYR B N   1 
ATOM   3772 C  CA  . TYR B 2 82  ? 132.707 0.819   -19.368 1.00 81.26  ? 80  TYR B CA  1 
ATOM   3773 C  C   . TYR B 2 82  ? 131.568 0.917   -20.375 1.00 80.81  ? 80  TYR B C   1 
ATOM   3774 O  O   . TYR B 2 82  ? 130.597 0.158   -20.326 1.00 80.39  ? 80  TYR B O   1 
ATOM   3775 C  CB  . TYR B 2 82  ? 133.880 0.065   -20.011 1.00 91.94  ? 80  TYR B CB  1 
ATOM   3776 C  CG  . TYR B 2 82  ? 135.007 -0.274  -19.062 1.00 100.37 ? 80  TYR B CG  1 
ATOM   3777 C  CD1 . TYR B 2 82  ? 135.011 -1.471  -18.358 1.00 99.66  ? 80  TYR B CD1 1 
ATOM   3778 C  CD2 . TYR B 2 82  ? 136.073 0.597   -18.881 1.00 105.91 ? 80  TYR B CD2 1 
ATOM   3779 C  CE1 . TYR B 2 82  ? 136.041 -1.787  -17.494 1.00 103.46 ? 80  TYR B CE1 1 
ATOM   3780 C  CE2 . TYR B 2 82  ? 137.108 0.290   -18.018 1.00 112.44 ? 80  TYR B CE2 1 
ATOM   3781 C  CZ  . TYR B 2 82  ? 137.087 -0.904  -17.329 1.00 112.34 ? 80  TYR B CZ  1 
ATOM   3782 O  OH  . TYR B 2 82  ? 138.114 -1.216  -16.469 1.00 120.70 ? 80  TYR B OH  1 
ATOM   3783 N  N   . LEU B 2 83  ? 131.702 1.876   -21.292 1.00 79.32  ? 81  LEU B N   1 
ATOM   3784 C  CA  . LEU B 2 83  ? 130.786 2.024   -22.422 1.00 82.09  ? 81  LEU B CA  1 
ATOM   3785 C  C   . LEU B 2 83  ? 131.597 2.311   -23.678 1.00 79.09  ? 81  LEU B C   1 
ATOM   3786 O  O   . LEU B 2 83  ? 132.164 3.398   -23.817 1.00 70.71  ? 81  LEU B O   1 
ATOM   3787 C  CB  . LEU B 2 83  ? 129.763 3.132   -22.173 1.00 76.81  ? 81  LEU B CB  1 
ATOM   3788 C  CG  . LEU B 2 83  ? 128.587 3.170   -23.153 1.00 65.32  ? 81  LEU B CG  1 
ATOM   3789 C  CD1 . LEU B 2 83  ? 127.550 2.112   -22.813 1.00 77.69  ? 81  LEU B CD1 1 
ATOM   3790 C  CD2 . LEU B 2 83  ? 127.956 4.554   -23.174 1.00 68.76  ? 81  LEU B CD2 1 
ATOM   3791 N  N   . GLN B 2 84  ? 131.654 1.340   -24.586 1.00 79.40  ? 82  GLN B N   1 
ATOM   3792 C  CA  . GLN B 2 84  ? 132.255 1.532   -25.900 1.00 76.40  ? 82  GLN B CA  1 
ATOM   3793 C  C   . GLN B 2 84  ? 131.210 2.093   -26.856 1.00 80.23  ? 82  GLN B C   1 
ATOM   3794 O  O   . GLN B 2 84  ? 130.120 1.529   -26.988 1.00 81.88  ? 82  GLN B O   1 
ATOM   3795 C  CB  . GLN B 2 84  ? 132.815 0.215   -26.437 1.00 79.29  ? 82  GLN B CB  1 
ATOM   3796 C  CG  . GLN B 2 84  ? 133.227 0.272   -27.897 1.00 86.08  ? 82  GLN B CG  1 
ATOM   3797 C  CD  . GLN B 2 84  ? 134.464 1.119   -28.114 1.00 90.27  ? 82  GLN B CD  1 
ATOM   3798 O  OE1 . GLN B 2 84  ? 135.360 1.156   -27.270 1.00 94.90  ? 82  GLN B OE1 1 
ATOM   3799 N  NE2 . GLN B 2 84  ? 134.519 1.808   -29.247 1.00 90.06  ? 82  GLN B NE2 1 
ATOM   3800 N  N   . MET B 2 85  ? 131.543 3.196   -27.526 1.00 84.64  ? 83  MET B N   1 
ATOM   3801 C  CA  . MET B 2 85  ? 130.613 3.887   -28.417 1.00 86.47  ? 83  MET B CA  1 
ATOM   3802 C  C   . MET B 2 85  ? 131.225 3.996   -29.809 1.00 91.61  ? 83  MET B C   1 
ATOM   3803 O  O   . MET B 2 85  ? 132.119 4.818   -30.037 1.00 96.04  ? 83  MET B O   1 
ATOM   3804 C  CB  . MET B 2 85  ? 130.267 5.272   -27.872 1.00 86.69  ? 83  MET B CB  1 
ATOM   3805 C  CG  . MET B 2 85  ? 129.832 5.278   -26.415 1.00 82.79  ? 83  MET B CG  1 
ATOM   3806 S  SD  . MET B 2 85  ? 130.347 6.773   -25.549 1.00 83.14  ? 83  MET B SD  1 
ATOM   3807 C  CE  . MET B 2 85  ? 129.130 7.942   -26.149 1.00 69.02  ? 83  MET B CE  1 
ATOM   3808 N  N   . ASN B 2 86  ? 130.737 3.176   -30.737 1.00 88.29  ? 84  ASN B N   1 
ATOM   3809 C  CA  . ASN B 2 86  ? 131.167 3.193   -32.127 1.00 87.75  ? 84  ASN B CA  1 
ATOM   3810 C  C   . ASN B 2 86  ? 130.080 3.794   -33.010 1.00 91.37  ? 84  ASN B C   1 
ATOM   3811 O  O   . ASN B 2 86  ? 128.899 3.822   -32.649 1.00 96.94  ? 84  ASN B O   1 
ATOM   3812 C  CB  . ASN B 2 86  ? 131.514 1.783   -32.618 1.00 89.77  ? 84  ASN B CB  1 
ATOM   3813 C  CG  . ASN B 2 86  ? 132.086 0.909   -31.522 1.00 88.73  ? 84  ASN B CG  1 
ATOM   3814 O  OD1 . ASN B 2 86  ? 133.208 1.123   -31.066 1.00 85.91  ? 84  ASN B OD1 1 
ATOM   3815 N  ND2 . ASN B 2 86  ? 131.314 -0.082  -31.092 1.00 92.11  ? 84  ASN B ND2 1 
ATOM   3816 N  N   . SER B 2 87  ? 130.501 4.275   -34.182 1.00 92.03  ? 85  SER B N   1 
ATOM   3817 C  CA  . SER B 2 87  ? 129.601 4.873   -35.172 1.00 95.71  ? 85  SER B CA  1 
ATOM   3818 C  C   . SER B 2 87  ? 128.819 6.041   -34.572 1.00 91.12  ? 85  SER B C   1 
ATOM   3819 O  O   . SER B 2 87  ? 127.588 6.087   -34.614 1.00 84.92  ? 85  SER B O   1 
ATOM   3820 C  CB  . SER B 2 87  ? 128.657 3.822   -35.762 1.00 90.65  ? 85  SER B CB  1 
ATOM   3821 O  OG  . SER B 2 87  ? 129.264 3.136   -36.844 1.00 89.82  ? 85  SER B OG  1 
ATOM   3822 N  N   . LEU B 2 88  ? 129.554 6.996   -34.008 1.00 92.05  ? 86  LEU B N   1 
ATOM   3823 C  CA  . LEU B 2 88  ? 128.937 8.117   -33.311 1.00 92.49  ? 86  LEU B CA  1 
ATOM   3824 C  C   . LEU B 2 88  ? 128.324 9.094   -34.307 1.00 89.83  ? 86  LEU B C   1 
ATOM   3825 O  O   . LEU B 2 88  ? 129.024 9.636   -35.170 1.00 91.16  ? 86  LEU B O   1 
ATOM   3826 C  CB  . LEU B 2 88  ? 129.972 8.817   -32.434 1.00 94.37  ? 86  LEU B CB  1 
ATOM   3827 C  CG  . LEU B 2 88  ? 130.260 8.139   -31.093 1.00 92.17  ? 86  LEU B CG  1 
ATOM   3828 C  CD1 . LEU B 2 88  ? 131.489 8.742   -30.437 1.00 89.15  ? 86  LEU B CD1 1 
ATOM   3829 C  CD2 . LEU B 2 88  ? 129.053 8.240   -30.172 1.00 95.14  ? 86  LEU B CD2 1 
ATOM   3830 N  N   . ASN B 2 89  ? 127.019 9.316   -34.189 1.00 93.62  ? 87  ASN B N   1 
ATOM   3831 C  CA  . ASN B 2 89  ? 126.287 10.294  -34.975 1.00 94.64  ? 87  ASN B CA  1 
ATOM   3832 C  C   . ASN B 2 89  ? 126.014 11.540  -34.142 1.00 95.04  ? 87  ASN B C   1 
ATOM   3833 O  O   . ASN B 2 89  ? 126.105 11.506  -32.911 1.00 94.30  ? 87  ASN B O   1 
ATOM   3834 C  CB  . ASN B 2 89  ? 124.967 9.692   -35.477 1.00 92.78  ? 87  ASN B CB  1 
ATOM   3835 C  CG  . ASN B 2 89  ? 123.994 9.391   -34.355 1.00 97.76  ? 87  ASN B CG  1 
ATOM   3836 O  OD1 . ASN B 2 89  ? 123.024 10.120  -34.146 1.00 101.05 ? 87  ASN B OD1 1 
ATOM   3837 N  ND2 . ASN B 2 89  ? 124.243 8.306   -33.631 1.00 95.79  ? 87  ASN B ND2 1 
ATOM   3838 N  N   . PRO B 2 90  ? 125.700 12.672  -34.782 1.00 97.10  ? 88  PRO B N   1 
ATOM   3839 C  CA  . PRO B 2 90  ? 125.465 13.908  -34.012 1.00 98.72  ? 88  PRO B CA  1 
ATOM   3840 C  C   . PRO B 2 90  ? 124.366 13.793  -32.967 1.00 96.12  ? 88  PRO B C   1 
ATOM   3841 O  O   . PRO B 2 90  ? 124.376 14.562  -31.997 1.00 93.65  ? 88  PRO B O   1 
ATOM   3842 C  CB  . PRO B 2 90  ? 125.098 14.928  -35.097 1.00 100.16 ? 88  PRO B CB  1 
ATOM   3843 C  CG  . PRO B 2 90  ? 125.798 14.437  -36.312 1.00 103.23 ? 88  PRO B CG  1 
ATOM   3844 C  CD  . PRO B 2 90  ? 125.758 12.934  -36.232 1.00 100.32 ? 88  PRO B CD  1 
ATOM   3845 N  N   . GLY B 2 91  ? 123.420 12.868  -33.129 1.00 95.29  ? 89  GLY B N   1 
ATOM   3846 C  CA  . GLY B 2 91  ? 122.380 12.675  -32.131 1.00 89.15  ? 89  GLY B CA  1 
ATOM   3847 C  C   . GLY B 2 91  ? 122.862 12.113  -30.809 1.00 87.72  ? 89  GLY B C   1 
ATOM   3848 O  O   . GLY B 2 91  ? 122.080 12.075  -29.853 1.00 91.20  ? 89  GLY B O   1 
ATOM   3849 N  N   . ASP B 2 92  ? 124.115 11.671  -30.732 1.00 87.81  ? 90  ASP B N   1 
ATOM   3850 C  CA  . ASP B 2 92  ? 124.679 11.119  -29.508 1.00 82.95  ? 90  ASP B CA  1 
ATOM   3851 C  C   . ASP B 2 92  ? 125.307 12.175  -28.609 1.00 82.67  ? 90  ASP B C   1 
ATOM   3852 O  O   . ASP B 2 92  ? 125.767 11.839  -27.513 1.00 77.45  ? 90  ASP B O   1 
ATOM   3853 C  CB  . ASP B 2 92  ? 125.723 10.048  -29.843 1.00 84.47  ? 90  ASP B CB  1 
ATOM   3854 C  CG  . ASP B 2 92  ? 125.122 8.849   -30.546 1.00 87.52  ? 90  ASP B CG  1 
ATOM   3855 O  OD1 . ASP B 2 92  ? 123.901 8.627   -30.406 1.00 92.60  ? 90  ASP B OD1 1 
ATOM   3856 O  OD2 . ASP B 2 92  ? 125.871 8.127   -31.237 1.00 89.29  ? 90  ASP B OD2 1 
ATOM   3857 N  N   . THR B 2 93  ? 125.346 13.434  -29.042 1.00 84.23  ? 91  THR B N   1 
ATOM   3858 C  CA  . THR B 2 93  ? 125.913 14.499  -28.225 1.00 80.82  ? 91  THR B CA  1 
ATOM   3859 C  C   . THR B 2 93  ? 125.050 14.734  -26.991 1.00 71.70  ? 91  THR B C   1 
ATOM   3860 O  O   . THR B 2 93  ? 123.885 15.133  -27.104 1.00 71.44  ? 91  THR B O   1 
ATOM   3861 C  CB  . THR B 2 93  ? 126.037 15.784  -29.040 1.00 81.69  ? 91  THR B CB  1 
ATOM   3862 O  OG1 . THR B 2 93  ? 127.074 15.634  -30.016 1.00 91.63  ? 91  THR B OG1 1 
ATOM   3863 C  CG2 . THR B 2 93  ? 126.375 16.957  -28.131 1.00 81.01  ? 91  THR B CG2 1 
ATOM   3864 N  N   . ALA B 2 94  ? 125.625 14.495  -25.816 1.00 69.16  ? 92  ALA B N   1 
ATOM   3865 C  CA  . ALA B 2 94  ? 124.921 14.652  -24.549 1.00 69.89  ? 92  ALA B CA  1 
ATOM   3866 C  C   . ALA B 2 94  ? 125.937 14.547  -23.421 1.00 69.03  ? 92  ALA B C   1 
ATOM   3867 O  O   . ALA B 2 94  ? 127.110 14.233  -23.642 1.00 71.30  ? 92  ALA B O   1 
ATOM   3868 C  CB  . ALA B 2 94  ? 123.815 13.606  -24.381 1.00 73.14  ? 92  ALA B CB  1 
ATOM   3869 N  N   . VAL B 2 95  ? 125.468 14.811  -22.207 1.00 66.49  ? 93  VAL B N   1 
ATOM   3870 C  CA  . VAL B 2 95  ? 126.229 14.527  -20.997 1.00 65.28  ? 93  VAL B CA  1 
ATOM   3871 C  C   . VAL B 2 95  ? 125.893 13.106  -20.568 1.00 65.38  ? 93  VAL B C   1 
ATOM   3872 O  O   . VAL B 2 95  ? 124.722 12.775  -20.357 1.00 70.84  ? 93  VAL B O   1 
ATOM   3873 C  CB  . VAL B 2 95  ? 125.907 15.532  -19.881 1.00 62.13  ? 93  VAL B CB  1 
ATOM   3874 C  CG1 . VAL B 2 95  ? 126.410 15.016  -18.540 1.00 56.82  ? 93  VAL B CG1 1 
ATOM   3875 C  CG2 . VAL B 2 95  ? 126.514 16.888  -20.195 1.00 52.11  ? 93  VAL B CG2 1 
ATOM   3876 N  N   . TYR B 2 96  ? 126.914 12.267  -20.428 1.00 61.93  ? 94  TYR B N   1 
ATOM   3877 C  CA  . TYR B 2 96  ? 126.719 10.863  -20.096 1.00 64.66  ? 94  TYR B CA  1 
ATOM   3878 C  C   . TYR B 2 96  ? 127.017 10.653  -18.618 1.00 69.24  ? 94  TYR B C   1 
ATOM   3879 O  O   . TYR B 2 96  ? 128.029 11.143  -18.107 1.00 73.62  ? 94  TYR B O   1 
ATOM   3880 C  CB  . TYR B 2 96  ? 127.616 9.977   -20.961 1.00 60.53  ? 94  TYR B CB  1 
ATOM   3881 C  CG  . TYR B 2 96  ? 127.136 9.852   -22.392 1.00 56.89  ? 94  TYR B CG  1 
ATOM   3882 C  CD1 . TYR B 2 96  ? 127.222 10.929  -23.267 1.00 50.14  ? 94  TYR B CD1 1 
ATOM   3883 C  CD2 . TYR B 2 96  ? 126.600 8.663   -22.868 1.00 57.88  ? 94  TYR B CD2 1 
ATOM   3884 C  CE1 . TYR B 2 96  ? 126.787 10.827  -24.572 1.00 52.14  ? 94  TYR B CE1 1 
ATOM   3885 C  CE2 . TYR B 2 96  ? 126.162 8.551   -24.177 1.00 58.32  ? 94  TYR B CE2 1 
ATOM   3886 C  CZ  . TYR B 2 96  ? 126.259 9.637   -25.023 1.00 62.03  ? 94  TYR B CZ  1 
ATOM   3887 O  OH  . TYR B 2 96  ? 125.825 9.536   -26.325 1.00 65.60  ? 94  TYR B OH  1 
ATOM   3888 N  N   . SER B 2 97  ? 126.135 9.924   -17.940 1.00 70.99  ? 95  SER B N   1 
ATOM   3889 C  CA  . SER B 2 97  ? 126.249 9.680   -16.510 1.00 68.75  ? 95  SER B CA  1 
ATOM   3890 C  C   . SER B 2 97  ? 126.049 8.203   -16.210 1.00 72.09  ? 95  SER B C   1 
ATOM   3891 O  O   . SER B 2 97  ? 125.140 7.566   -16.751 1.00 74.06  ? 95  SER B O   1 
ATOM   3892 C  CB  . SER B 2 97  ? 125.228 10.512  -15.725 1.00 78.54  ? 95  SER B CB  1 
ATOM   3893 O  OG  . SER B 2 97  ? 125.423 11.898  -15.946 1.00 83.51  ? 95  SER B OG  1 
ATOM   3894 N  N   . CYS B 2 98  ? 126.905 7.663   -15.349 1.00 76.71  ? 96  CYS B N   1 
ATOM   3895 C  CA  . CYS B 2 98  ? 126.724 6.317   -14.828 1.00 73.30  ? 96  CYS B CA  1 
ATOM   3896 C  C   . CYS B 2 98  ? 125.889 6.354   -13.554 1.00 73.57  ? 96  CYS B C   1 
ATOM   3897 O  O   . CYS B 2 98  ? 125.929 7.321   -12.788 1.00 70.93  ? 96  CYS B O   1 
ATOM   3898 C  CB  . CYS B 2 98  ? 128.080 5.659   -14.566 1.00 74.49  ? 96  CYS B CB  1 
ATOM   3899 S  SG  . CYS B 2 98  ? 129.200 6.636   -13.528 1.00 92.78  ? 96  CYS B SG  1 
ATOM   3900 N  N   . ALA B 2 99  ? 125.123 5.286   -13.338 1.00 74.99  ? 97  ALA B N   1 
ATOM   3901 C  CA  . ALA B 2 99  ? 124.212 5.200   -12.206 1.00 71.78  ? 97  ALA B CA  1 
ATOM   3902 C  C   . ALA B 2 99  ? 124.300 3.822   -11.567 1.00 65.50  ? 97  ALA B C   1 
ATOM   3903 O  O   . ALA B 2 99  ? 124.552 2.820   -12.242 1.00 67.23  ? 97  ALA B O   1 
ATOM   3904 C  CB  . ALA B 2 99  ? 122.767 5.490   -12.631 1.00 69.31  ? 97  ALA B CB  1 
ATOM   3905 N  N   . ALA B 2 100 ? 124.085 3.784   -10.254 1.00 66.64  ? 98  ALA B N   1 
ATOM   3906 C  CA  . ALA B 2 100 ? 124.106 2.549   -9.482  1.00 73.00  ? 98  ALA B CA  1 
ATOM   3907 C  C   . ALA B 2 100 ? 122.860 2.469   -8.613  1.00 77.56  ? 98  ALA B C   1 
ATOM   3908 O  O   . ALA B 2 100 ? 122.405 3.482   -8.074  1.00 74.45  ? 98  ALA B O   1 
ATOM   3909 C  CB  . ALA B 2 100 ? 125.359 2.460   -8.604  1.00 75.94  ? 98  ALA B CB  1 
ATOM   3910 N  N   . THR B 2 101 ? 122.317 1.260   -8.475  1.00 71.36  ? 99  THR B N   1 
ATOM   3911 C  CA  . THR B 2 101 ? 121.181 1.022   -7.594  1.00 80.90  ? 99  THR B CA  1 
ATOM   3912 C  C   . THR B 2 101 ? 121.061 -0.477  -7.352  1.00 84.28  ? 99  THR B C   1 
ATOM   3913 O  O   . THR B 2 101 ? 121.659 -1.292  -8.058  1.00 82.61  ? 99  THR B O   1 
ATOM   3914 C  CB  . THR B 2 101 ? 119.878 1.587   -8.169  1.00 77.10  ? 99  THR B CB  1 
ATOM   3915 O  OG1 . THR B 2 101 ? 118.899 1.665   -7.127  1.00 75.42  ? 99  THR B OG1 1 
ATOM   3916 C  CG2 . THR B 2 101 ? 119.342 0.692   -9.261  1.00 71.18  ? 99  THR B CG2 1 
ATOM   3917 N  N   . LEU B 2 102 ? 120.270 -0.827  -6.336  1.00 82.67  ? 100 LEU B N   1 
ATOM   3918 C  CA  . LEU B 2 102 ? 120.003 -2.212  -5.981  1.00 80.36  ? 100 LEU B CA  1 
ATOM   3919 C  C   . LEU B 2 102 ? 118.886 -2.787  -6.853  1.00 78.14  ? 100 LEU B C   1 
ATOM   3920 O  O   . LEU B 2 102 ? 118.015 -2.051  -7.323  1.00 76.97  ? 100 LEU B O   1 
ATOM   3921 C  CB  . LEU B 2 102 ? 119.614 -2.307  -4.508  1.00 79.31  ? 100 LEU B CB  1 
ATOM   3922 C  CG  . LEU B 2 102 ? 120.750 -2.063  -3.510  1.00 83.57  ? 100 LEU B CG  1 
ATOM   3923 C  CD1 . LEU B 2 102 ? 120.396 -2.588  -2.126  1.00 80.07  ? 100 LEU B CD1 1 
ATOM   3924 C  CD2 . LEU B 2 102 ? 122.039 -2.695  -4.010  1.00 91.19  ? 100 LEU B CD2 1 
ATOM   3925 N  N   . PRO B 2 103 ? 118.894 -4.105  -7.087  1.00 78.29  ? 101 PRO B N   1 
ATOM   3926 C  CA  . PRO B 2 103 ? 117.883 -4.698  -7.980  1.00 76.79  ? 101 PRO B CA  1 
ATOM   3927 C  C   . PRO B 2 103 ? 116.449 -4.521  -7.507  1.00 78.95  ? 101 PRO B C   1 
ATOM   3928 O  O   . PRO B 2 103 ? 115.531 -4.593  -8.333  1.00 76.88  ? 101 PRO B O   1 
ATOM   3929 C  CB  . PRO B 2 103 ? 118.276 -6.183  -8.023  1.00 78.71  ? 101 PRO B CB  1 
ATOM   3930 C  CG  . PRO B 2 103 ? 119.137 -6.396  -6.820  1.00 85.39  ? 101 PRO B CG  1 
ATOM   3931 C  CD  . PRO B 2 103 ? 119.862 -5.106  -6.609  1.00 80.32  ? 101 PRO B CD  1 
ATOM   3932 N  N   . ALA B 2 104 ? 116.221 -4.299  -6.211  1.00 75.20  ? 102 ALA B N   1 
ATOM   3933 C  CA  . ALA B 2 104 ? 114.872 -4.015  -5.736  1.00 73.61  ? 102 ALA B CA  1 
ATOM   3934 C  C   . ALA B 2 104 ? 114.363 -2.662  -6.216  1.00 72.09  ? 102 ALA B C   1 
ATOM   3935 O  O   . ALA B 2 104 ? 113.147 -2.451  -6.263  1.00 69.32  ? 102 ALA B O   1 
ATOM   3936 C  CB  . ALA B 2 104 ? 114.825 -4.078  -4.209  1.00 71.22  ? 102 ALA B CB  1 
ATOM   3937 N  N   . TRP B 2 105 ? 115.264 -1.743  -6.566  1.00 66.48  ? 103 TRP B N   1 
ATOM   3938 C  CA  . TRP B 2 105 ? 114.853 -0.441  -7.075  1.00 66.49  ? 103 TRP B CA  1 
ATOM   3939 C  C   . TRP B 2 105 ? 114.416 -0.495  -8.533  1.00 68.48  ? 103 TRP B C   1 
ATOM   3940 O  O   . TRP B 2 105 ? 113.633 0.356   -8.967  1.00 67.21  ? 103 TRP B O   1 
ATOM   3941 C  CB  . TRP B 2 105 ? 115.991 0.565   -6.918  1.00 62.24  ? 103 TRP B CB  1 
ATOM   3942 C  CG  . TRP B 2 105 ? 116.232 0.996   -5.505  1.00 61.71  ? 103 TRP B CG  1 
ATOM   3943 C  CD1 . TRP B 2 105 ? 116.559 0.197   -4.448  1.00 64.22  ? 103 TRP B CD1 1 
ATOM   3944 C  CD2 . TRP B 2 105 ? 116.178 2.333   -4.997  1.00 58.09  ? 103 TRP B CD2 1 
ATOM   3945 N  NE1 . TRP B 2 105 ? 116.705 0.954   -3.310  1.00 62.51  ? 103 TRP B NE1 1 
ATOM   3946 C  CE2 . TRP B 2 105 ? 116.477 2.269   -3.621  1.00 61.99  ? 103 TRP B CE2 1 
ATOM   3947 C  CE3 . TRP B 2 105 ? 115.905 3.578   -5.570  1.00 53.30  ? 103 TRP B CE3 1 
ATOM   3948 C  CZ2 . TRP B 2 105 ? 116.510 3.402   -2.811  1.00 60.12  ? 103 TRP B CZ2 1 
ATOM   3949 C  CZ3 . TRP B 2 105 ? 115.937 4.702   -4.765  1.00 51.11  ? 103 TRP B CZ3 1 
ATOM   3950 C  CH2 . TRP B 2 105 ? 116.237 4.606   -3.401  1.00 56.88  ? 103 TRP B CH2 1 
ATOM   3951 N  N   . THR B 2 106 ? 114.914 -1.462  -9.303  1.00 71.13  ? 104 THR B N   1 
ATOM   3952 C  CA  . THR B 2 106 ? 114.548 -1.574  -10.711 1.00 70.90  ? 104 THR B CA  1 
ATOM   3953 C  C   . THR B 2 106 ? 113.329 -2.453  -10.949 1.00 64.43  ? 104 THR B C   1 
ATOM   3954 O  O   . THR B 2 106 ? 112.584 -2.213  -11.905 1.00 64.76  ? 104 THR B O   1 
ATOM   3955 C  CB  . THR B 2 106 ? 115.722 -2.128  -11.524 1.00 72.23  ? 104 THR B CB  1 
ATOM   3956 O  OG1 . THR B 2 106 ? 115.930 -3.506  -11.187 1.00 66.24  ? 104 THR B OG1 1 
ATOM   3957 C  CG2 . THR B 2 106 ? 116.987 -1.340  -11.237 1.00 67.48  ? 104 THR B CG2 1 
ATOM   3958 N  N   . GLY B 2 107 ? 113.100 -3.456  -10.105 1.00 61.98  ? 105 GLY B N   1 
ATOM   3959 C  CA  . GLY B 2 107 ? 111.975 -4.336  -10.347 1.00 64.19  ? 105 GLY B CA  1 
ATOM   3960 C  C   . GLY B 2 107 ? 112.162 -5.177  -11.600 1.00 66.99  ? 105 GLY B C   1 
ATOM   3961 O  O   . GLY B 2 107 ? 113.281 -5.464  -12.036 1.00 68.36  ? 105 GLY B O   1 
ATOM   3962 N  N   . ILE B 2 108 ? 111.037 -5.573  -12.192 1.00 68.95  ? 106 ILE B N   1 
ATOM   3963 C  CA  . ILE B 2 108 ? 111.071 -6.467  -13.343 1.00 66.95  ? 106 ILE B CA  1 
ATOM   3964 C  C   . ILE B 2 108 ? 111.210 -5.717  -14.668 1.00 66.70  ? 106 ILE B C   1 
ATOM   3965 O  O   . ILE B 2 108 ? 111.896 -6.196  -15.578 1.00 73.33  ? 106 ILE B O   1 
ATOM   3966 C  CB  . ILE B 2 108 ? 109.816 -7.361  -13.334 1.00 63.19  ? 106 ILE B CB  1 
ATOM   3967 C  CG1 . ILE B 2 108 ? 109.984 -8.499  -12.325 1.00 58.29  ? 106 ILE B CG1 1 
ATOM   3968 C  CG2 . ILE B 2 108 ? 109.531 -7.932  -14.716 1.00 62.36  ? 106 ILE B CG2 1 
ATOM   3969 C  CD1 . ILE B 2 108 ? 108.685 -8.966  -11.707 1.00 66.52  ? 106 ILE B CD1 1 
ATOM   3970 N  N   . ILE B 2 109 ? 110.613 -4.532  -14.793 1.00 69.52  ? 107 ILE B N   1 
ATOM   3971 C  CA  . ILE B 2 109 ? 110.601 -3.830  -16.074 1.00 68.19  ? 107 ILE B CA  1 
ATOM   3972 C  C   . ILE B 2 109 ? 110.942 -2.359  -15.883 1.00 61.87  ? 107 ILE B C   1 
ATOM   3973 O  O   . ILE B 2 109 ? 110.714 -1.538  -16.779 1.00 72.90  ? 107 ILE B O   1 
ATOM   3974 C  CB  . ILE B 2 109 ? 109.243 -3.987  -16.783 1.00 71.48  ? 107 ILE B CB  1 
ATOM   3975 C  CG1 . ILE B 2 109 ? 108.092 -3.796  -15.794 1.00 68.74  ? 107 ILE B CG1 1 
ATOM   3976 C  CG2 . ILE B 2 109 ? 109.144 -5.351  -17.450 1.00 72.45  ? 107 ILE B CG2 1 
ATOM   3977 C  CD1 . ILE B 2 109 ? 106.726 -3.782  -16.446 1.00 68.12  ? 107 ILE B CD1 1 
ATOM   3978 N  N   . GLY B 2 110 ? 111.492 -2.012  -14.723 1.00 61.15  ? 108 GLY B N   1 
ATOM   3979 C  CA  . GLY B 2 110 ? 111.805 -0.625  -14.442 1.00 55.83  ? 108 GLY B CA  1 
ATOM   3980 C  C   . GLY B 2 110 ? 113.281 -0.300  -14.549 1.00 67.40  ? 108 GLY B C   1 
ATOM   3981 O  O   . GLY B 2 110 ? 113.736 0.720   -14.023 1.00 72.17  ? 108 GLY B O   1 
ATOM   3982 N  N   . GLY B 2 111 ? 114.042 -1.163  -15.223 1.00 67.52  ? 109 GLY B N   1 
ATOM   3983 C  CA  . GLY B 2 111 ? 115.477 -0.968  -15.333 1.00 71.73  ? 109 GLY B CA  1 
ATOM   3984 C  C   . GLY B 2 111 ? 115.880 0.215   -16.187 1.00 72.11  ? 109 GLY B C   1 
ATOM   3985 O  O   . GLY B 2 111 ? 117.046 0.622   -16.148 1.00 73.77  ? 109 GLY B O   1 
ATOM   3986 N  N   . ARG B 2 112 ? 114.945 0.772   -16.953 1.00 68.80  ? 110 ARG B N   1 
ATOM   3987 C  CA  . ARG B 2 112 ? 115.208 1.883   -17.854 1.00 60.62  ? 110 ARG B CA  1 
ATOM   3988 C  C   . ARG B 2 112 ? 114.877 3.239   -17.248 1.00 60.35  ? 110 ARG B C   1 
ATOM   3989 O  O   . ARG B 2 112 ? 115.196 4.265   -17.859 1.00 64.11  ? 110 ARG B O   1 
ATOM   3990 C  CB  . ARG B 2 112 ? 114.409 1.717   -19.152 1.00 67.37  ? 110 ARG B CB  1 
ATOM   3991 C  CG  . ARG B 2 112 ? 114.611 0.399   -19.878 1.00 66.04  ? 110 ARG B CG  1 
ATOM   3992 C  CD  . ARG B 2 112 ? 115.357 0.630   -21.174 1.00 68.99  ? 110 ARG B CD  1 
ATOM   3993 N  NE  . ARG B 2 112 ? 115.419 -0.558  -22.016 1.00 77.33  ? 110 ARG B NE  1 
ATOM   3994 C  CZ  . ARG B 2 112 ? 114.827 -0.660  -23.197 1.00 73.69  ? 110 ARG B CZ  1 
ATOM   3995 N  NH1 . ARG B 2 112 ? 114.110 0.333   -23.697 1.00 68.32  ? 110 ARG B NH1 1 
ATOM   3996 N  NH2 . ARG B 2 112 ? 114.956 -1.786  -23.893 1.00 71.94  ? 110 ARG B NH2 1 
ATOM   3997 N  N   . ARG B 2 113 ? 114.265 3.274   -16.066 1.00 64.72  ? 111 ARG B N   1 
ATOM   3998 C  CA  . ARG B 2 113 ? 113.817 4.528   -15.482 1.00 71.68  ? 111 ARG B CA  1 
ATOM   3999 C  C   . ARG B 2 113 ? 114.945 5.150   -14.672 1.00 65.66  ? 111 ARG B C   1 
ATOM   4000 O  O   . ARG B 2 113 ? 115.437 4.514   -13.730 1.00 65.39  ? 111 ARG B O   1 
ATOM   4001 C  CB  . ARG B 2 113 ? 112.617 4.289   -14.581 1.00 63.27  ? 111 ARG B CB  1 
ATOM   4002 C  CG  . ARG B 2 113 ? 111.352 3.843   -15.298 1.00 60.92  ? 111 ARG B CG  1 
ATOM   4003 C  CD  . ARG B 2 113 ? 110.171 3.665   -14.365 1.00 72.19  ? 111 ARG B CD  1 
ATOM   4004 N  NE  . ARG B 2 113 ? 108.984 3.171   -15.051 1.00 81.01  ? 111 ARG B NE  1 
ATOM   4005 C  CZ  . ARG B 2 113 ? 107.862 2.827   -14.435 1.00 88.86  ? 111 ARG B CZ  1 
ATOM   4006 N  NH1 . ARG B 2 113 ? 107.747 2.897   -13.118 1.00 86.97  ? 111 ARG B NH1 1 
ATOM   4007 N  NH2 . ARG B 2 113 ? 106.835 2.387   -15.155 1.00 82.30  ? 111 ARG B NH2 1 
ATOM   4008 N  N   . PRO B 2 114 ? 115.385 6.373   -14.991 1.00 60.59  ? 112 PRO B N   1 
ATOM   4009 C  CA  . PRO B 2 114 ? 116.493 6.975   -14.229 1.00 64.32  ? 112 PRO B CA  1 
ATOM   4010 C  C   . PRO B 2 114 ? 116.152 7.273   -12.780 1.00 68.45  ? 112 PRO B C   1 
ATOM   4011 O  O   . PRO B 2 114 ? 117.065 7.336   -11.948 1.00 69.29  ? 112 PRO B O   1 
ATOM   4012 C  CB  . PRO B 2 114 ? 116.795 8.263   -15.005 1.00 62.33  ? 112 PRO B CB  1 
ATOM   4013 C  CG  . PRO B 2 114 ? 115.516 8.598   -15.685 1.00 65.28  ? 112 PRO B CG  1 
ATOM   4014 C  CD  . PRO B 2 114 ? 114.854 7.287   -16.016 1.00 66.74  ? 112 PRO B CD  1 
ATOM   4015 N  N   . GLY B 2 115 ? 114.874 7.457   -12.453 1.00 67.41  ? 113 GLY B N   1 
ATOM   4016 C  CA  . GLY B 2 115 ? 114.453 7.654   -11.077 1.00 64.41  ? 113 GLY B CA  1 
ATOM   4017 C  C   . GLY B 2 115 ? 114.613 6.441   -10.188 1.00 67.20  ? 113 GLY B C   1 
ATOM   4018 O  O   . GLY B 2 115 ? 114.481 6.569   -8.966  1.00 65.23  ? 113 GLY B O   1 
ATOM   4019 N  N   . ASN B 2 116 ? 114.887 5.275   -10.766 1.00 60.91  ? 114 ASN B N   1 
ATOM   4020 C  CA  . ASN B 2 116 ? 115.168 4.065   -10.008 1.00 65.27  ? 114 ASN B CA  1 
ATOM   4021 C  C   . ASN B 2 116 ? 116.637 3.929   -9.625  1.00 67.63  ? 114 ASN B C   1 
ATOM   4022 O  O   . ASN B 2 116 ? 117.024 2.897   -9.068  1.00 68.70  ? 114 ASN B O   1 
ATOM   4023 C  CB  . ASN B 2 116 ? 114.725 2.839   -10.810 1.00 68.21  ? 114 ASN B CB  1 
ATOM   4024 C  CG  . ASN B 2 116 ? 113.224 2.636   -10.775 1.00 64.65  ? 114 ASN B CG  1 
ATOM   4025 O  OD1 . ASN B 2 116 ? 112.557 3.024   -9.816  1.00 64.16  ? 114 ASN B OD1 1 
ATOM   4026 N  ND2 . ASN B 2 116 ? 112.684 2.020   -11.821 1.00 60.03  ? 114 ASN B ND2 1 
ATOM   4027 N  N   . TYR B 2 117 ? 117.455 4.937   -9.901  1.00 67.19  ? 115 TYR B N   1 
ATOM   4028 C  CA  . TYR B 2 117 ? 118.869 4.930   -9.527  1.00 66.07  ? 115 TYR B CA  1 
ATOM   4029 C  C   . TYR B 2 117 ? 119.162 6.134   -8.642  1.00 67.11  ? 115 TYR B C   1 
ATOM   4030 O  O   . TYR B 2 117 ? 119.220 7.270   -9.150  1.00 71.34  ? 115 TYR B O   1 
ATOM   4031 C  CB  . TYR B 2 117 ? 119.758 4.954   -10.772 1.00 71.14  ? 115 TYR B CB  1 
ATOM   4032 C  CG  . TYR B 2 117 ? 119.568 3.779   -11.715 1.00 68.54  ? 115 TYR B CG  1 
ATOM   4033 C  CD1 . TYR B 2 117 ? 118.453 3.694   -12.541 1.00 66.03  ? 115 TYR B CD1 1 
ATOM   4034 C  CD2 . TYR B 2 117 ? 120.513 2.763   -11.788 1.00 66.67  ? 115 TYR B CD2 1 
ATOM   4035 C  CE1 . TYR B 2 117 ? 118.278 2.626   -13.403 1.00 60.64  ? 115 TYR B CE1 1 
ATOM   4036 C  CE2 . TYR B 2 117 ? 120.346 1.691   -12.646 1.00 67.47  ? 115 TYR B CE2 1 
ATOM   4037 C  CZ  . TYR B 2 117 ? 119.228 1.628   -13.452 1.00 69.17  ? 115 TYR B CZ  1 
ATOM   4038 O  OH  . TYR B 2 117 ? 119.059 0.563   -14.308 1.00 73.10  ? 115 TYR B OH  1 
ATOM   4039 N  N   . PRO B 2 118 ? 119.346 5.958   -7.328  1.00 61.90  ? 116 PRO B N   1 
ATOM   4040 C  CA  . PRO B 2 118 ? 119.615 7.117   -6.465  1.00 62.92  ? 116 PRO B CA  1 
ATOM   4041 C  C   . PRO B 2 118 ? 121.060 7.580   -6.475  1.00 72.31  ? 116 PRO B C   1 
ATOM   4042 O  O   . PRO B 2 118 ? 121.329 8.700   -6.022  1.00 78.94  ? 116 PRO B O   1 
ATOM   4043 C  CB  . PRO B 2 118 ? 119.216 6.613   -5.072  1.00 62.17  ? 116 PRO B CB  1 
ATOM   4044 C  CG  . PRO B 2 118 ? 119.488 5.150   -5.128  1.00 62.48  ? 116 PRO B CG  1 
ATOM   4045 C  CD  . PRO B 2 118 ? 119.235 4.709   -6.554  1.00 61.71  ? 116 PRO B CD  1 
ATOM   4046 N  N   . TYR B 2 119 ? 121.990 6.773   -6.974  1.00 73.57  ? 117 TYR B N   1 
ATOM   4047 C  CA  . TYR B 2 119 ? 123.408 7.105   -6.971  1.00 73.50  ? 117 TYR B CA  1 
ATOM   4048 C  C   . TYR B 2 119 ? 123.863 7.441   -8.384  1.00 76.71  ? 117 TYR B C   1 
ATOM   4049 O  O   . TYR B 2 119 ? 123.654 6.655   -9.315  1.00 74.51  ? 117 TYR B O   1 
ATOM   4050 C  CB  . TYR B 2 119 ? 124.237 5.960   -6.388  1.00 76.31  ? 117 TYR B CB  1 
ATOM   4051 C  CG  . TYR B 2 119 ? 123.699 5.450   -5.070  1.00 75.88  ? 117 TYR B CG  1 
ATOM   4052 C  CD1 . TYR B 2 119 ? 123.523 6.314   -3.996  1.00 77.08  ? 117 TYR B CD1 1 
ATOM   4053 C  CD2 . TYR B 2 119 ? 123.370 4.113   -4.897  1.00 76.72  ? 117 TYR B CD2 1 
ATOM   4054 C  CE1 . TYR B 2 119 ? 123.033 5.861   -2.786  1.00 82.30  ? 117 TYR B CE1 1 
ATOM   4055 C  CE2 . TYR B 2 119 ? 122.879 3.650   -3.688  1.00 79.95  ? 117 TYR B CE2 1 
ATOM   4056 C  CZ  . TYR B 2 119 ? 122.713 4.529   -2.637  1.00 85.90  ? 117 TYR B CZ  1 
ATOM   4057 O  OH  . TYR B 2 119 ? 122.227 4.079   -1.431  1.00 89.66  ? 117 TYR B OH  1 
ATOM   4058 N  N   . TRP B 2 120 ? 124.488 8.606   -8.534  1.00 75.50  ? 118 TRP B N   1 
ATOM   4059 C  CA  . TRP B 2 120 ? 124.827 9.157   -9.834  1.00 76.69  ? 118 TRP B CA  1 
ATOM   4060 C  C   . TRP B 2 120 ? 126.274 9.632   -9.835  1.00 86.51  ? 118 TRP B C   1 
ATOM   4061 O  O   . TRP B 2 120 ? 126.878 9.865   -8.785  1.00 83.17  ? 118 TRP B O   1 
ATOM   4062 C  CB  . TRP B 2 120 ? 123.893 10.320  -10.191 1.00 73.37  ? 118 TRP B CB  1 
ATOM   4063 C  CG  . TRP B 2 120 ? 122.518 9.881   -10.581 1.00 82.13  ? 118 TRP B CG  1 
ATOM   4064 C  CD1 . TRP B 2 120 ? 121.405 9.886   -9.791  1.00 75.33  ? 118 TRP B CD1 1 
ATOM   4065 C  CD2 . TRP B 2 120 ? 122.101 9.390   -11.860 1.00 81.09  ? 118 TRP B CD2 1 
ATOM   4066 N  NE1 . TRP B 2 120 ? 120.324 9.416   -10.494 1.00 76.16  ? 118 TRP B NE1 1 
ATOM   4067 C  CE2 . TRP B 2 120 ? 120.723 9.107   -11.768 1.00 74.35  ? 118 TRP B CE2 1 
ATOM   4068 C  CE3 . TRP B 2 120 ? 122.758 9.158   -13.072 1.00 79.93  ? 118 TRP B CE3 1 
ATOM   4069 C  CZ2 . TRP B 2 120 ? 119.991 8.605   -12.841 1.00 75.39  ? 118 TRP B CZ2 1 
ATOM   4070 C  CZ3 . TRP B 2 120 ? 122.029 8.659   -14.136 1.00 75.76  ? 118 TRP B CZ3 1 
ATOM   4071 C  CH2 . TRP B 2 120 ? 120.660 8.389   -14.013 1.00 76.56  ? 118 TRP B CH2 1 
ATOM   4072 N  N   . GLY B 2 121 ? 126.823 9.775   -11.042 1.00 85.80  ? 119 GLY B N   1 
ATOM   4073 C  CA  . GLY B 2 121 ? 128.099 10.424  -11.240 1.00 82.42  ? 119 GLY B CA  1 
ATOM   4074 C  C   . GLY B 2 121 ? 127.936 11.883  -11.642 1.00 81.97  ? 119 GLY B C   1 
ATOM   4075 O  O   . GLY B 2 121 ? 126.837 12.390  -11.846 1.00 87.61  ? 119 GLY B O   1 
ATOM   4076 N  N   . GLN B 2 122 ? 129.079 12.560  -11.763 1.00 87.27  ? 120 GLN B N   1 
ATOM   4077 C  CA  . GLN B 2 122 ? 129.059 13.976  -12.110 1.00 87.83  ? 120 GLN B CA  1 
ATOM   4078 C  C   . GLN B 2 122 ? 128.691 14.209  -13.569 1.00 86.65  ? 120 GLN B C   1 
ATOM   4079 O  O   . GLN B 2 122 ? 128.219 15.299  -13.908 1.00 78.12  ? 120 GLN B O   1 
ATOM   4080 C  CB  . GLN B 2 122 ? 130.414 14.616  -11.795 1.00 94.84  ? 120 GLN B CB  1 
ATOM   4081 C  CG  . GLN B 2 122 ? 131.418 14.577  -12.936 1.00 102.76 ? 120 GLN B CG  1 
ATOM   4082 C  CD  . GLN B 2 122 ? 132.303 13.346  -12.891 1.00 108.22 ? 120 GLN B CD  1 
ATOM   4083 O  OE1 . GLN B 2 122 ? 132.151 12.490  -12.019 1.00 105.78 ? 120 GLN B OE1 1 
ATOM   4084 N  NE2 . GLN B 2 122 ? 133.237 13.253  -13.831 1.00 109.72 ? 120 GLN B NE2 1 
ATOM   4085 N  N   . GLY B 2 123 ? 128.896 13.218  -14.435 1.00 86.68  ? 121 GLY B N   1 
ATOM   4086 C  CA  . GLY B 2 123 ? 128.621 13.382  -15.849 1.00 83.00  ? 121 GLY B CA  1 
ATOM   4087 C  C   . GLY B 2 123 ? 129.810 13.861  -16.654 1.00 83.73  ? 121 GLY B C   1 
ATOM   4088 O  O   . GLY B 2 123 ? 130.496 14.808  -16.258 1.00 83.54  ? 121 GLY B O   1 
ATOM   4089 N  N   . THR B 2 124 ? 130.068 13.211  -17.786 1.00 77.55  ? 122 THR B N   1 
ATOM   4090 C  CA  . THR B 2 124 ? 131.124 13.614  -18.702 1.00 77.36  ? 122 THR B CA  1 
ATOM   4091 C  C   . THR B 2 124 ? 130.512 14.013  -20.038 1.00 71.19  ? 122 THR B C   1 
ATOM   4092 O  O   . THR B 2 124 ? 129.568 13.376  -20.516 1.00 70.30  ? 122 THR B O   1 
ATOM   4093 C  CB  . THR B 2 124 ? 132.152 12.491  -18.903 1.00 83.00  ? 122 THR B CB  1 
ATOM   4094 O  OG1 . THR B 2 124 ? 133.052 12.845  -19.961 1.00 85.81  ? 122 THR B OG1 1 
ATOM   4095 C  CG2 . THR B 2 124 ? 131.462 11.176  -19.240 1.00 79.05  ? 122 THR B CG2 1 
ATOM   4096 N  N   . GLN B 2 125 ? 131.050 15.073  -20.632 1.00 76.69  ? 123 GLN B N   1 
ATOM   4097 C  CA  . GLN B 2 125 ? 130.512 15.599  -21.877 1.00 72.86  ? 123 GLN B CA  1 
ATOM   4098 C  C   . GLN B 2 125 ? 131.016 14.802  -23.072 1.00 73.61  ? 123 GLN B C   1 
ATOM   4099 O  O   . GLN B 2 125 ? 132.198 14.458  -23.157 1.00 79.47  ? 123 GLN B O   1 
ATOM   4100 C  CB  . GLN B 2 125 ? 130.887 17.073  -22.039 1.00 69.24  ? 123 GLN B CB  1 
ATOM   4101 C  CG  . GLN B 2 125 ? 130.515 17.674  -23.390 1.00 69.20  ? 123 GLN B CG  1 
ATOM   4102 C  CD  . GLN B 2 125 ? 129.024 17.628  -23.668 1.00 75.79  ? 123 GLN B CD  1 
ATOM   4103 O  OE1 . GLN B 2 125 ? 128.207 17.697  -22.751 1.00 82.35  ? 123 GLN B OE1 1 
ATOM   4104 N  NE2 . GLN B 2 125 ? 128.663 17.509  -24.940 1.00 75.07  ? 123 GLN B NE2 1 
ATOM   4105 N  N   . VAL B 2 126 ? 130.104 14.505  -23.995 1.00 70.54  ? 124 VAL B N   1 
ATOM   4106 C  CA  . VAL B 2 126 ? 130.431 13.865  -25.263 1.00 70.73  ? 124 VAL B CA  1 
ATOM   4107 C  C   . VAL B 2 126 ? 129.826 14.719  -26.368 1.00 77.01  ? 124 VAL B C   1 
ATOM   4108 O  O   . VAL B 2 126 ? 128.601 14.884  -26.427 1.00 77.68  ? 124 VAL B O   1 
ATOM   4109 C  CB  . VAL B 2 126 ? 129.910 12.421  -25.340 1.00 66.34  ? 124 VAL B CB  1 
ATOM   4110 C  CG1 . VAL B 2 126 ? 129.874 11.943  -26.786 1.00 66.07  ? 124 VAL B CG1 1 
ATOM   4111 C  CG2 . VAL B 2 126 ? 130.772 11.501  -24.489 1.00 72.81  ? 124 VAL B CG2 1 
ATOM   4112 N  N   . THR B 2 127 ? 130.676 15.270  -27.230 1.00 84.53  ? 125 THR B N   1 
ATOM   4113 C  CA  . THR B 2 127 ? 130.240 16.118  -28.333 1.00 87.21  ? 125 THR B CA  1 
ATOM   4114 C  C   . THR B 2 127 ? 130.684 15.490  -29.645 1.00 88.54  ? 125 THR B C   1 
ATOM   4115 O  O   . THR B 2 127 ? 131.887 15.366  -29.902 1.00 95.95  ? 125 THR B O   1 
ATOM   4116 C  CB  . THR B 2 127 ? 130.804 17.535  -28.199 1.00 85.75  ? 125 THR B CB  1 
ATOM   4117 O  OG1 . THR B 2 127 ? 130.602 18.009  -26.862 1.00 80.93  ? 125 THR B OG1 1 
ATOM   4118 C  CG2 . THR B 2 127 ? 130.107 18.476  -29.171 1.00 87.90  ? 125 THR B CG2 1 
ATOM   4119 N  N   . VAL B 2 128 ? 129.719 15.088  -30.464 1.00 88.56  ? 126 VAL B N   1 
ATOM   4120 C  CA  . VAL B 2 128 ? 129.982 14.471  -31.759 1.00 95.00  ? 126 VAL B CA  1 
ATOM   4121 C  C   . VAL B 2 128 ? 129.850 15.554  -32.822 1.00 102.08 ? 126 VAL B C   1 
ATOM   4122 O  O   . VAL B 2 128 ? 128.740 16.003  -33.129 1.00 98.34  ? 126 VAL B O   1 
ATOM   4123 C  CB  . VAL B 2 128 ? 129.030 13.300  -32.031 1.00 89.99  ? 126 VAL B CB  1 
ATOM   4124 C  CG1 . VAL B 2 128 ? 129.313 12.695  -33.397 1.00 94.71  ? 126 VAL B CG1 1 
ATOM   4125 C  CG2 . VAL B 2 128 ? 129.160 12.249  -30.940 1.00 89.26  ? 126 VAL B CG2 1 
ATOM   4126 N  N   . SER B 2 129 ? 130.979 15.975  -33.383 1.00 103.08 ? 127 SER B N   1 
ATOM   4127 C  CA  . SER B 2 129 ? 130.993 17.017  -34.407 1.00 102.52 ? 127 SER B CA  1 
ATOM   4128 C  C   . SER B 2 129 ? 130.240 16.580  -35.660 1.00 105.92 ? 127 SER B C   1 
ATOM   4129 O  O   . SER B 2 129 ? 130.669 15.669  -36.368 1.00 101.41 ? 127 SER B O   1 
ATOM   4130 C  CB  . SER B 2 129 ? 132.431 17.396  -34.765 1.00 99.39  ? 127 SER B CB  1 
ATOM   4131 O  OG  . SER B 2 129 ? 133.039 16.393  -35.561 1.00 104.04 ? 127 SER B OG  1 
HETATM 4132 C  C2  . MPG C 3 .   ? 82.879  27.017  18.744  1.00 55.79  ? 501 MPG A C2  1 
HETATM 4133 C  C3  . MPG C 3 .   ? 81.770  27.130  19.785  1.00 59.25  ? 501 MPG A C3  1 
HETATM 4134 C  C4  . MPG C 3 .   ? 80.360  26.898  19.255  1.00 55.11  ? 501 MPG A C4  1 
HETATM 4135 C  C5  . MPG C 3 .   ? 79.721  28.202  18.791  1.00 56.62  ? 501 MPG A C5  1 
HETATM 4136 C  C6  . MPG C 3 .   ? 78.382  28.018  18.095  1.00 57.62  ? 501 MPG A C6  1 
HETATM 4137 C  C7  . MPG C 3 .   ? 78.456  28.003  16.574  1.00 56.10  ? 501 MPG A C7  1 
HETATM 4138 C  C8  . MPG C 3 .   ? 77.042  27.944  16.006  1.00 62.88  ? 501 MPG A C8  1 
HETATM 4139 C  C9  . MPG C 3 .   ? 76.864  28.555  14.654  1.00 65.51  ? 501 MPG A C9  1 
HETATM 4140 C  C10 . MPG C 3 .   ? 76.327  29.741  14.378  1.00 67.37  ? 501 MPG A C10 1 
HETATM 4141 C  C11 . MPG C 3 .   ? 76.090  30.344  13.031  1.00 68.07  ? 501 MPG A C11 1 
HETATM 4142 C  C12 . MPG C 3 .   ? 74.625  30.059  12.690  1.00 75.47  ? 501 MPG A C12 1 
HETATM 4143 C  C13 . MPG C 3 .   ? 73.754  30.495  13.865  1.00 84.50  ? 501 MPG A C13 1 
HETATM 4144 C  C14 . MPG C 3 .   ? 72.283  30.098  13.813  1.00 89.20  ? 501 MPG A C14 1 
HETATM 4145 C  C15 . MPG C 3 .   ? 72.063  28.691  13.271  1.00 91.35  ? 501 MPG A C15 1 
HETATM 4146 C  C16 . MPG C 3 .   ? 70.622  28.209  13.401  1.00 93.89  ? 501 MPG A C16 1 
HETATM 4147 C  C17 . MPG C 3 .   ? 69.980  27.852  12.067  1.00 90.84  ? 501 MPG A C17 1 
HETATM 4148 C  C18 . MPG C 3 .   ? 70.020  28.996  11.064  1.00 82.14  ? 501 MPG A C18 1 
HETATM 4149 O  O1  . MPG C 3 .   ? 84.673  28.602  18.643  1.00 66.51  ? 501 MPG A O1  1 
HETATM 4150 C  C1  . MPG C 3 .   ? 83.301  28.393  18.271  1.00 58.94  ? 501 MPG A C1  1 
HETATM 4151 C  CXD . MPG C 3 .   ? 85.615  30.678  19.273  1.00 68.15  ? 501 MPG A CXD 1 
HETATM 4152 O  O2  . MPG C 3 .   ? 86.577  31.034  20.218  1.00 73.53  ? 501 MPG A O2  1 
HETATM 4153 C  C21 . MPG C 3 .   ? 84.583  31.779  19.037  1.00 67.24  ? 501 MPG A C21 1 
HETATM 4154 O  O3  . MPG C 3 .   ? 85.223  33.023  19.168  1.00 59.29  ? 501 MPG A O3  1 
HETATM 4155 O  O4  . MPG C 3 .   ? 84.612  29.125  20.821  1.00 81.06  ? 501 MPG A O4  1 
HETATM 4156 C  CX3 . MPG C 3 .   ? 84.912  29.387  19.681  1.00 72.16  ? 501 MPG A CX3 1 
HETATM 4157 C  C2  . MPG D 3 .   ? 90.847  9.636   3.103   1.00 88.76  ? 502 MPG A C2  1 
HETATM 4158 C  C3  . MPG D 3 .   ? 89.963  10.830  3.447   1.00 89.20  ? 502 MPG A C3  1 
HETATM 4159 C  C4  . MPG D 3 .   ? 90.258  12.075  2.622   1.00 74.94  ? 502 MPG A C4  1 
HETATM 4160 C  C5  . MPG D 3 .   ? 89.040  12.965  2.405   1.00 63.10  ? 502 MPG A C5  1 
HETATM 4161 C  C6  . MPG D 3 .   ? 89.360  14.346  2.951   1.00 58.00  ? 502 MPG A C6  1 
HETATM 4162 C  C7  . MPG D 3 .   ? 88.201  15.320  3.102   1.00 61.02  ? 502 MPG A C7  1 
HETATM 4163 C  C8  . MPG D 3 .   ? 87.165  14.846  4.122   1.00 58.91  ? 502 MPG A C8  1 
HETATM 4164 C  C9  . MPG D 3 .   ? 87.447  15.469  5.448   1.00 66.18  ? 502 MPG A C9  1 
HETATM 4165 C  C10 . MPG D 3 .   ? 87.200  14.954  6.652   1.00 58.93  ? 502 MPG A C10 1 
HETATM 4166 C  C11 . MPG D 3 .   ? 87.545  15.578  7.967   1.00 56.99  ? 502 MPG A C11 1 
HETATM 4167 C  C12 . MPG D 3 .   ? 87.022  17.004  8.098   1.00 58.07  ? 502 MPG A C12 1 
HETATM 4168 C  C13 . MPG D 3 .   ? 87.983  17.846  8.928   1.00 51.34  ? 502 MPG A C13 1 
HETATM 4169 C  C14 . MPG D 3 .   ? 87.557  19.301  9.048   1.00 55.90  ? 502 MPG A C14 1 
HETATM 4170 C  C15 . MPG D 3 .   ? 88.041  20.091  7.837   1.00 69.79  ? 502 MPG A C15 1 
HETATM 4171 C  C16 . MPG D 3 .   ? 87.334  21.420  7.605   1.00 74.85  ? 502 MPG A C16 1 
HETATM 4172 C  C17 . MPG D 3 .   ? 87.597  21.978  6.210   1.00 77.27  ? 502 MPG A C17 1 
HETATM 4173 C  C18 . MPG D 3 .   ? 86.379  21.958  5.294   1.00 66.82  ? 502 MPG A C18 1 
HETATM 4174 O  O1  . MPG D 3 .   ? 90.924  8.598   5.261   1.00 84.73  ? 502 MPG A O1  1 
HETATM 4175 C  C1  . MPG D 3 .   ? 90.426  8.433   3.919   1.00 83.03  ? 502 MPG A C1  1 
HETATM 4176 C  CXD . MPG D 3 .   ? 90.807  7.929   7.537   1.00 79.25  ? 502 MPG A CXD 1 
HETATM 4177 O  O2  . MPG D 3 .   ? 89.885  7.512   8.497   1.00 85.45  ? 502 MPG A O2  1 
HETATM 4178 C  C21 . MPG D 3 .   ? 91.726  9.042   8.038   1.00 81.22  ? 502 MPG A C21 1 
HETATM 4179 O  O3  . MPG D 3 .   ? 92.223  8.664   9.297   1.00 76.33  ? 502 MPG A O3  1 
HETATM 4180 O  O4  . MPG D 3 .   ? 88.894  8.471   6.184   1.00 83.28  ? 502 MPG A O4  1 
HETATM 4181 C  CX3 . MPG D 3 .   ? 90.091  8.364   6.262   1.00 72.66  ? 502 MPG A CX3 1 
HETATM 4182 C  C2  . MPG E 3 .   ? 107.470 -6.673  9.181   1.00 110.32 ? 503 MPG A C2  1 
HETATM 4183 C  C3  . MPG E 3 .   ? 106.036 -6.625  9.705   1.00 101.45 ? 503 MPG A C3  1 
HETATM 4184 C  C4  . MPG E 3 .   ? 105.088 -5.832  8.807   1.00 97.91  ? 503 MPG A C4  1 
HETATM 4185 C  C5  . MPG E 3 .   ? 103.654 -5.817  9.331   1.00 91.61  ? 503 MPG A C5  1 
HETATM 4186 C  C6  . MPG E 3 .   ? 102.875 -4.515  9.173   1.00 72.67  ? 503 MPG A C6  1 
HETATM 4187 C  C7  . MPG E 3 .   ? 101.701 -4.407  10.144  1.00 70.74  ? 503 MPG A C7  1 
HETATM 4188 C  C8  . MPG E 3 .   ? 100.746 -5.590  9.977   1.00 62.39  ? 503 MPG A C8  1 
HETATM 4189 C  C9  . MPG E 3 .   ? 99.295  -5.382  10.292  1.00 62.81  ? 503 MPG A C9  1 
HETATM 4190 C  C10 . MPG E 3 .   ? 98.674  -5.488  11.471  1.00 63.69  ? 503 MPG A C10 1 
HETATM 4191 C  C11 . MPG E 3 .   ? 97.204  -5.314  11.723  1.00 60.21  ? 503 MPG A C11 1 
HETATM 4192 C  C12 . MPG E 3 .   ? 96.769  -4.453  12.913  1.00 63.69  ? 503 MPG A C12 1 
HETATM 4193 C  C13 . MPG E 3 .   ? 96.726  -2.979  12.538  1.00 63.93  ? 503 MPG A C13 1 
HETATM 4194 C  C14 . MPG E 3 .   ? 96.271  -2.026  13.636  1.00 56.27  ? 503 MPG A C14 1 
HETATM 4195 C  C15 . MPG E 3 .   ? 97.272  -1.809  14.760  1.00 61.94  ? 503 MPG A C15 1 
HETATM 4196 C  C16 . MPG E 3 .   ? 96.614  -1.221  16.000  1.00 64.03  ? 503 MPG A C16 1 
HETATM 4197 C  C17 . MPG E 3 .   ? 97.614  -0.896  17.101  1.00 67.38  ? 503 MPG A C17 1 
HETATM 4198 C  C18 . MPG E 3 .   ? 96.942  -0.497  18.408  1.00 66.98  ? 503 MPG A C18 1 
HETATM 4199 O  O1  . MPG E 3 .   ? 109.768 -7.024  9.754   1.00 120.23 ? 503 MPG A O1  1 
HETATM 4200 C  C1  . MPG E 3 .   ? 108.422 -7.254  10.207  1.00 112.69 ? 503 MPG A C1  1 
HETATM 4201 C  CXD . MPG E 3 .   ? 112.075 -7.504  9.636   1.00 110.55 ? 503 MPG A CXD 1 
HETATM 4202 O  O2  . MPG E 3 .   ? 112.766 -7.410  10.845  1.00 110.46 ? 503 MPG A O2  1 
HETATM 4203 C  C21 . MPG E 3 .   ? 112.038 -6.189  8.861   1.00 105.23 ? 503 MPG A C21 1 
HETATM 4204 O  O3  . MPG E 3 .   ? 113.310 -5.601  8.946   1.00 108.11 ? 503 MPG A O3  1 
HETATM 4205 O  O4  . MPG E 3 .   ? 110.378 -9.152  10.090  1.00 112.21 ? 503 MPG A O4  1 
HETATM 4206 C  CX3 . MPG E 3 .   ? 110.651 -8.002  9.856   1.00 114.96 ? 503 MPG A CX3 1 
HETATM 4207 C  C2  . MPG F 3 .   ? 94.823  21.134  1.278   1.00 76.19  ? 504 MPG A C2  1 
HETATM 4208 C  C3  . MPG F 3 .   ? 94.118  22.450  0.964   1.00 74.85  ? 504 MPG A C3  1 
HETATM 4209 C  C4  . MPG F 3 .   ? 93.360  22.544  -0.359  1.00 75.25  ? 504 MPG A C4  1 
HETATM 4210 C  C5  . MPG F 3 .   ? 92.291  23.623  -0.231  1.00 57.91  ? 504 MPG A C5  1 
HETATM 4211 C  C6  . MPG F 3 .   ? 91.397  23.973  -1.419  1.00 54.22  ? 504 MPG A C6  1 
HETATM 4212 C  C7  . MPG F 3 .   ? 92.201  24.838  -2.382  1.00 55.11  ? 504 MPG A C7  1 
HETATM 4213 C  C8  . MPG F 3 .   ? 91.521  25.616  -3.517  1.00 55.61  ? 504 MPG A C8  1 
HETATM 4214 C  C9  . MPG F 3 .   ? 92.674  26.429  -3.999  1.00 67.27  ? 504 MPG A C9  1 
HETATM 4215 C  C10 . MPG F 3 .   ? 93.454  26.328  -5.079  1.00 83.87  ? 504 MPG A C10 1 
HETATM 4216 C  C11 . MPG F 3 .   ? 94.688  27.139  -5.308  1.00 77.15  ? 504 MPG A C11 1 
HETATM 4217 C  C12 . MPG F 3 .   ? 95.669  26.206  -4.588  1.00 76.90  ? 504 MPG A C12 1 
HETATM 4218 C  C13 . MPG F 3 .   ? 95.889  26.353  -3.088  1.00 78.01  ? 504 MPG A C13 1 
HETATM 4219 C  C14 . MPG F 3 .   ? 96.955  25.373  -2.614  1.00 80.60  ? 504 MPG A C14 1 
HETATM 4220 C  C15 . MPG F 3 .   ? 97.131  25.335  -1.102  1.00 86.41  ? 504 MPG A C15 1 
HETATM 4221 C  C16 . MPG F 3 .   ? 98.216  24.350  -0.682  1.00 88.64  ? 504 MPG A C16 1 
HETATM 4222 C  C17 . MPG F 3 .   ? 98.384  24.192  0.825   1.00 79.57  ? 504 MPG A C17 1 
HETATM 4223 C  C18 . MPG F 3 .   ? 99.407  23.121  1.183   1.00 80.71  ? 504 MPG A C18 1 
HETATM 4224 O  O1  . MPG F 3 .   ? 95.770  19.762  3.001   1.00 103.29 ? 504 MPG A O1  1 
HETATM 4225 C  C1  . MPG F 3 .   ? 95.133  21.028  2.756   1.00 88.79  ? 504 MPG A C1  1 
HETATM 4226 C  CXD . MPG F 3 .   ? 96.624  17.982  4.284   1.00 103.29 ? 504 MPG A CXD 1 
HETATM 4227 O  O2  . MPG F 3 .   ? 95.997  17.066  5.128   1.00 100.82 ? 504 MPG A O2  1 
HETATM 4228 C  C21 . MPG F 3 .   ? 98.079  18.245  4.672   1.00 100.74 ? 504 MPG A C21 1 
HETATM 4229 O  O3  . MPG F 3 .   ? 98.583  17.119  5.343   1.00 98.47  ? 504 MPG A O3  1 
HETATM 4230 O  O4  . MPG F 3 .   ? 95.476  19.890  5.217   1.00 107.93 ? 504 MPG A O4  1 
HETATM 4231 C  CX3 . MPG F 3 .   ? 95.894  19.321  4.240   1.00 103.35 ? 504 MPG A CX3 1 
HETATM 4232 C  C2  . MPG G 3 .   ? 100.584 4.233   3.783   1.00 70.90  ? 505 MPG A C2  1 
HETATM 4233 C  C3  . MPG G 3 .   ? 101.996 4.676   4.152   1.00 72.72  ? 505 MPG A C3  1 
HETATM 4234 C  C4  . MPG G 3 .   ? 102.307 4.416   5.619   1.00 80.96  ? 505 MPG A C4  1 
HETATM 4235 C  C5  . MPG G 3 .   ? 102.396 5.691   6.449   1.00 89.06  ? 505 MPG A C5  1 
HETATM 4236 C  C6  . MPG G 3 .   ? 101.058 6.380   6.687   1.00 91.97  ? 505 MPG A C6  1 
HETATM 4237 C  C7  . MPG G 3 .   ? 101.041 7.812   6.162   1.00 97.91  ? 505 MPG A C7  1 
HETATM 4238 C  C8  . MPG G 3 .   ? 102.239 8.587   6.714   1.00 101.63 ? 505 MPG A C8  1 
HETATM 4239 C  C9  . MPG G 3 .   ? 102.792 9.617   5.780   1.00 102.62 ? 505 MPG A C9  1 
HETATM 4240 C  C10 . MPG G 3 .   ? 104.084 9.833   5.537   1.00 100.16 ? 505 MPG A C10 1 
HETATM 4241 C  C11 . MPG G 3 .   ? 105.236 9.045   6.080   1.00 99.59  ? 505 MPG A C11 1 
HETATM 4242 C  C12 . MPG G 3 .   ? 105.718 9.475   7.467   1.00 106.70 ? 505 MPG A C12 1 
HETATM 4243 C  C13 . MPG G 3 .   ? 105.816 10.982  7.644   1.00 112.46 ? 505 MPG A C13 1 
HETATM 4244 C  C14 . MPG G 3 .   ? 104.915 11.504  8.756   1.00 106.86 ? 505 MPG A C14 1 
HETATM 4245 C  C15 . MPG G 3 .   ? 104.311 12.867  8.443   1.00 110.91 ? 505 MPG A C15 1 
HETATM 4246 C  C16 . MPG G 3 .   ? 103.170 13.250  9.377   1.00 111.51 ? 505 MPG A C16 1 
HETATM 4247 C  C17 . MPG G 3 .   ? 101.843 13.439  8.650   1.00 115.97 ? 505 MPG A C17 1 
HETATM 4248 C  C18 . MPG G 3 .   ? 101.296 12.151  8.050   1.00 113.02 ? 505 MPG A C18 1 
HETATM 4249 O  O1  . MPG G 3 .   ? 100.909 5.467   1.786   1.00 87.50  ? 505 MPG A O1  1 
HETATM 4250 C  C1  . MPG G 3 .   ? 100.384 4.227   2.285   1.00 69.62  ? 505 MPG A C1  1 
HETATM 4251 C  CXD . MPG G 3 .   ? 100.130 7.677   2.026   1.00 88.28  ? 505 MPG A CXD 1 
HETATM 4252 O  O2  . MPG G 3 .   ? 99.395  8.651   1.349   1.00 91.14  ? 505 MPG A O2  1 
HETATM 4253 C  C21 . MPG G 3 .   ? 101.591 8.064   2.245   1.00 91.25  ? 505 MPG A C21 1 
HETATM 4254 O  O3  . MPG G 3 .   ? 101.624 9.376   2.741   1.00 88.35  ? 505 MPG A O3  1 
HETATM 4255 O  O4  . MPG G 3 .   ? 99.291  6.122   0.391   1.00 68.09  ? 505 MPG A O4  1 
HETATM 4256 C  CX3 . MPG G 3 .   ? 100.051 6.342   1.298   1.00 80.01  ? 505 MPG A CX3 1 
HETATM 4257 C  C1  . OCT H 4 .   ? 83.657  25.027  -14.385 1.00 64.27  ? 506 OCT A C1  1 
HETATM 4258 C  C2  . OCT H 4 .   ? 83.935  24.731  -12.917 1.00 60.69  ? 506 OCT A C2  1 
HETATM 4259 C  C3  . OCT H 4 .   ? 85.358  25.086  -12.499 1.00 54.32  ? 506 OCT A C3  1 
HETATM 4260 C  C4  . OCT H 4 .   ? 85.628  24.857  -11.017 1.00 57.13  ? 506 OCT A C4  1 
HETATM 4261 C  C5  . OCT H 4 .   ? 86.914  25.515  -10.529 1.00 58.54  ? 506 OCT A C5  1 
HETATM 4262 C  C6  . OCT H 4 .   ? 87.139  25.378  -9.028  1.00 59.95  ? 506 OCT A C6  1 
HETATM 4263 C  C7  . OCT H 4 .   ? 86.094  26.098  -8.184  1.00 56.97  ? 506 OCT A C7  1 
HETATM 4264 C  C8  . OCT H 4 .   ? 86.468  26.159  -6.709  1.00 67.62  ? 506 OCT A C8  1 
HETATM 4265 C  C1  . OCT I 4 .   ? 95.812  -7.429  1.480   1.00 58.63  ? 507 OCT A C1  1 
HETATM 4266 C  C2  . OCT I 4 .   ? 95.318  -7.451  2.921   1.00 54.80  ? 507 OCT A C2  1 
HETATM 4267 C  C3  . OCT I 4 .   ? 95.887  -6.311  3.758   1.00 53.16  ? 507 OCT A C3  1 
HETATM 4268 C  C4  . OCT I 4 .   ? 95.492  -6.372  5.228   1.00 50.37  ? 507 OCT A C4  1 
HETATM 4269 C  C5  . OCT I 4 .   ? 95.935  -5.144  6.016   1.00 43.94  ? 507 OCT A C5  1 
HETATM 4270 C  C6  . OCT I 4 .   ? 95.700  -5.257  7.518   1.00 47.65  ? 507 OCT A C6  1 
HETATM 4271 C  C7  . OCT I 4 .   ? 94.229  -5.368  7.903   1.00 51.97  ? 507 OCT A C7  1 
HETATM 4272 C  C8  . OCT I 4 .   ? 93.990  -5.119  9.387   1.00 54.29  ? 507 OCT A C8  1 
HETATM 4273 C  C1  . OCT J 4 .   ? 73.837  24.365  -16.776 1.00 46.38  ? 508 OCT A C1  1 
HETATM 4274 C  C2  . OCT J 4 .   ? 75.292  24.277  -16.332 1.00 68.01  ? 508 OCT A C2  1 
HETATM 4275 C  C3  . OCT J 4 .   ? 76.085  23.234  -17.111 1.00 65.45  ? 508 OCT A C3  1 
HETATM 4276 C  C4  . OCT J 4 .   ? 77.501  23.026  -16.588 1.00 52.18  ? 508 OCT A C4  1 
HETATM 4277 C  C5  . OCT J 4 .   ? 78.311  22.049  -17.432 1.00 57.61  ? 508 OCT A C5  1 
HETATM 4278 C  C6  . OCT J 4 .   ? 79.595  21.579  -16.760 1.00 61.60  ? 508 OCT A C6  1 
HETATM 4279 C  C7  . OCT J 4 .   ? 80.637  22.678  -16.593 1.00 57.78  ? 508 OCT A C7  1 
HETATM 4280 C  C8  . OCT J 4 .   ? 81.992  22.139  -16.149 1.00 56.60  ? 508 OCT A C8  1 
HETATM 4281 C  C1  . OCT K 4 .   ? 75.608  -3.502  16.693  1.00 57.98  ? 509 OCT A C1  1 
HETATM 4282 C  C2  . OCT K 4 .   ? 75.616  -3.321  18.205  1.00 59.59  ? 509 OCT A C2  1 
HETATM 4283 C  C3  . OCT K 4 .   ? 76.945  -3.708  18.842  1.00 58.95  ? 509 OCT A C3  1 
HETATM 4284 C  C4  . OCT K 4 .   ? 76.972  -3.477  20.347  1.00 59.00  ? 509 OCT A C4  1 
HETATM 4285 C  C5  . OCT K 4 .   ? 78.313  -3.807  20.992  1.00 55.06  ? 509 OCT A C5  1 
HETATM 4286 C  C6  . OCT K 4 .   ? 79.421  -2.826  20.625  1.00 58.11  ? 509 OCT A C6  1 
HETATM 4287 C  C7  . OCT K 4 .   ? 80.697  -3.030  21.435  1.00 68.74  ? 509 OCT A C7  1 
HETATM 4288 C  C8  . OCT K 4 .   ? 81.786  -2.027  21.079  1.00 47.25  ? 509 OCT A C8  1 
HETATM 4289 C  C1  . OCT L 4 .   ? 82.409  10.455  -13.834 1.00 70.49  ? 510 OCT A C1  1 
HETATM 4290 C  C2  . OCT L 4 .   ? 83.858  10.141  -14.177 1.00 77.60  ? 510 OCT A C2  1 
HETATM 4291 C  C3  . OCT L 4 .   ? 84.771  10.186  -12.959 1.00 65.81  ? 510 OCT A C3  1 
HETATM 4292 C  C4  . OCT L 4 .   ? 86.226  9.875   -13.286 1.00 62.77  ? 510 OCT A C4  1 
HETATM 4293 C  C5  . OCT L 4 .   ? 87.109  9.884   -12.045 1.00 66.13  ? 510 OCT A C5  1 
HETATM 4294 C  C6  . OCT L 4 .   ? 88.584  9.599   -12.293 1.00 61.72  ? 510 OCT A C6  1 
HETATM 4295 C  C7  . OCT L 4 .   ? 88.865  8.253   -12.949 1.00 67.09  ? 510 OCT A C7  1 
HETATM 4296 C  C8  . OCT L 4 .   ? 90.361  8.025   -13.116 1.00 65.26  ? 510 OCT A C8  1 
HETATM 4297 S  S   . SO4 M 5 .   ? 67.040  31.371  16.481  1.00 78.84  ? 511 SO4 A S   1 
HETATM 4298 O  O1  . SO4 M 5 .   ? 67.671  30.101  16.132  1.00 79.96  ? 511 SO4 A O1  1 
HETATM 4299 O  O2  . SO4 M 5 .   ? 67.190  32.309  15.372  1.00 78.54  ? 511 SO4 A O2  1 
HETATM 4300 O  O3  . SO4 M 5 .   ? 65.621  31.154  16.749  1.00 75.59  ? 511 SO4 A O3  1 
HETATM 4301 O  O4  . SO4 M 5 .   ? 67.677  31.922  17.673  1.00 74.23  ? 511 SO4 A O4  1 
HETATM 4302 S  S   . SO4 N 5 .   ? 108.459 3.889   34.673  1.00 98.36  ? 512 SO4 A S   1 
HETATM 4303 O  O1  . SO4 N 5 .   ? 109.003 2.900   33.747  1.00 80.34  ? 512 SO4 A O1  1 
HETATM 4304 O  O2  . SO4 N 5 .   ? 107.237 3.368   35.281  1.00 95.98  ? 512 SO4 A O2  1 
HETATM 4305 O  O3  . SO4 N 5 .   ? 109.441 4.167   35.717  1.00 88.57  ? 512 SO4 A O3  1 
HETATM 4306 O  O4  . SO4 N 5 .   ? 108.154 5.119   33.948  1.00 84.06  ? 512 SO4 A O4  1 
HETATM 4307 ZN ZN  . ZN  O 6 .   ? 74.501  30.019  6.929   1.00 87.70  ? 513 ZN  A ZN  1 
HETATM 4308 CL CL  . CL  P 7 .   ? 75.375  32.751  7.449   1.00 77.82  ? 514 CL  A CL  1 
HETATM 4309 CL CL  . CL  Q 7 .   ? 74.213  27.419  4.631   1.00 72.18  ? 515 CL  A CL  1 
# 
