data_9G97
# 
_entry.id   9G97 
# 
_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   9G97         pdb_00009g97 10.2210/pdb9g97/pdb 
WWPDB D_1292140355 ?            ?                   
# 
_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                        9G97 
_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_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          9G95 
_pdbx_database_related.content_type   unspecified 
# 
_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   7  ? ? ? ? 
4 non-polymer syn '(1R)-2-{[(R)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(DODECANOYLOXY)METHYL]ETHYL (9Z)-OCTADEC-9-ENOATE' 
661.890   1  ? ? ? ? 
5 non-polymer syn N-OCTANE                                                                                                    
114.229   5  ? ? ? ? 
6 non-polymer syn 'CHLORIDE ION'                                                                                              
35.453    3  ? ? ? ? 
7 non-polymer syn 'SULFATE ION'                                                                                               
96.063    2  ? ? ? ? 
8 non-polymer syn 'ZINC ION'                                                                                                  
65.409    1  ? ? ? ? 
9 water       nat water                                                                                                       
18.015    45 ? ? ? ? 
# 
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 '(1R)-2-{[(R)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(DODECANOYLOXY)METHYL]ETHYL (9Z)-OCTADEC-9-ENOATE' LOP 
5 N-OCTANE                                                                                                    OCT 
6 'CHLORIDE ION'                                                                                              CL  
7 'SULFATE ION'                                                                                               SO4 
8 'ZINC ION'                                                                                                  ZN  
9 water                                                                                                       HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   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 
HOH non-polymer         . WATER ?                                        'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE ?                                        'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE ?                                        'C6 H13 N O2'    131.173 
LOP non-polymer         . 
'(1R)-2-{[(R)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(DODECANOYLOXY)METHYL]ETHYL (9Z)-OCTADEC-9-ENOATE' 
'LAURYL OLEYL PHOSPHATIDYL ETHANOLAMINE' 'C35 H68 N O8 P' 661.890 
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 3 MPG 1  506 424 MPG MPG A . 
I 3 MPG 1  507 425 MPG MPG A . 
J 4 LOP 1  508 426 LOP LOP A . 
K 5 OCT 1  509 427 OCT OCT A . 
L 5 OCT 1  510 428 OCT OCT A . 
M 5 OCT 1  511 429 OCT OCT A . 
N 5 OCT 1  512 430 OCT OCT A . 
O 5 OCT 1  513 431 OCT OCT A . 
P 6 CL  1  514 432 CL  CL  A . 
Q 7 SO4 1  515 433 SO4 SO4 A . 
R 7 SO4 1  516 434 SO4 SO4 A . 
S 8 ZN  1  517 435 ZN  ZN  A . 
T 6 CL  1  518 436 CL  CL  A . 
U 6 CL  1  519 437 CL  CL  A . 
V 9 HOH 1  601 13  HOH HOH A . 
V 9 HOH 2  602 39  HOH HOH A . 
V 9 HOH 3  603 33  HOH HOH A . 
V 9 HOH 4  604 12  HOH HOH A . 
V 9 HOH 5  605 22  HOH HOH A . 
V 9 HOH 6  606 3   HOH HOH A . 
V 9 HOH 7  607 16  HOH HOH A . 
V 9 HOH 8  608 8   HOH HOH A . 
V 9 HOH 9  609 45  HOH HOH A . 
V 9 HOH 10 610 28  HOH HOH A . 
V 9 HOH 11 611 1   HOH HOH A . 
V 9 HOH 12 612 20  HOH HOH A . 
V 9 HOH 13 613 34  HOH HOH A . 
V 9 HOH 14 614 26  HOH HOH A . 
V 9 HOH 15 615 10  HOH HOH A . 
V 9 HOH 16 616 19  HOH HOH A . 
V 9 HOH 17 617 32  HOH HOH A . 
V 9 HOH 18 618 5   HOH HOH A . 
V 9 HOH 19 619 6   HOH HOH A . 
V 9 HOH 20 620 2   HOH HOH A . 
V 9 HOH 21 621 44  HOH HOH A . 
V 9 HOH 22 622 35  HOH HOH A . 
V 9 HOH 23 623 9   HOH HOH A . 
V 9 HOH 24 624 17  HOH HOH A . 
V 9 HOH 25 625 37  HOH HOH A . 
V 9 HOH 26 626 14  HOH HOH A . 
V 9 HOH 27 627 4   HOH HOH A . 
V 9 HOH 28 628 18  HOH HOH A . 
V 9 HOH 29 629 27  HOH HOH A . 
V 9 HOH 30 630 7   HOH HOH A . 
V 9 HOH 31 631 29  HOH HOH A . 
V 9 HOH 32 632 21  HOH HOH A . 
V 9 HOH 33 633 11  HOH HOH A . 
V 9 HOH 34 634 23  HOH HOH A . 
V 9 HOH 35 635 36  HOH HOH A . 
V 9 HOH 36 636 40  HOH HOH A . 
V 9 HOH 37 637 25  HOH HOH A . 
V 9 HOH 38 638 31  HOH HOH A . 
V 9 HOH 39 639 38  HOH HOH A . 
V 9 HOH 40 640 15  HOH HOH A . 
V 9 HOH 41 641 24  HOH HOH A . 
V 9 HOH 42 642 41  HOH HOH A . 
V 9 HOH 43 643 42  HOH HOH A . 
W 9 HOH 1  201 43  HOH HOH B . 
W 9 HOH 2  202 30  HOH HOH B . 
# 
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'   ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   93.50 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9G97 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     270.550 
_cell.length_a_esd                 ? 
_cell.length_b                     38.470 
_cell.length_b_esd                 ? 
_cell.length_c                     56.830 
_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                         9G97 
_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                   9G97 
_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             2.41 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.95 
_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              6.43 
_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    'sodium acetate, PEG400, lithium sulfate, zinc chloride, E. coli polar lipids, monoolein' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_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 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-04-25 
_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   0.9688 
_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 I24' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9688 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I24 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9G97 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.31 
_reflns.d_resolution_low                               135.02 
_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                                     25893 
_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                           98.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_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                                   1.0 
_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                                    2.31 
_reflns_shell.d_res_low                                     2.35 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.1 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1276 
_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                               6.4 
_reflns_shell.pdbx_chi_squared                              ? 
_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                                  0.4 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          98.2 
_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                                 9G97 
_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                            2.31 
_refine.ls_d_res_low                             51.19 
_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                     25882 
_refine.ls_number_reflns_R_free                  1311 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.67 
_refine.ls_percent_reflns_R_free                 5.07 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2165 
_refine.ls_R_factor_R_free                       0.2602 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2141 
_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                          1.34 
_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          'MOLECULAR REPLACEMENT' 
_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                 27.11 
_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                            0.32 
_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.pdbx_number_atoms_protein        4132 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         274 
_refine_hist.number_atoms_solvent             45 
_refine_hist.number_atoms_total               4451 
_refine_hist.d_res_high                       2.31 
_refine_hist.d_res_low                        51.19 
# 
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' ? 0.003  ? ?   ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.584  ? ?   ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.731 ? 787 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.039  ? 682 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 716 ? 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' 2.31 2.40  . . 127 2728 98.00 . . . . 0.2759 . . . . . . . . . . . 0.3462 
'X-RAY DIFFRACTION' 2.40 2.51  . . 113 2683 98.00 . . . . 0.2595 . . . . . . . . . . . 0.2895 
'X-RAY DIFFRACTION' 2.51 2.64  . . 137 2706 99.00 . . . . 0.2478 . . . . . . . . . . . 0.3130 
'X-RAY DIFFRACTION' 2.64 2.81  . . 167 2671 99.00 . . . . 0.2293 . . . . . . . . . . . 0.3080 
'X-RAY DIFFRACTION' 2.81 3.03  . . 161 2698 99.00 . . . . 0.2281 . . . . . . . . . . . 0.2523 
'X-RAY DIFFRACTION' 3.03 3.33  . . 163 2702 99.00 . . . . 0.2183 . . . . . . . . . . . 0.2740 
'X-RAY DIFFRACTION' 3.33 3.81  . . 155 2767 99.00 . . . . 0.2059 . . . . . . . . . . . 0.2699 
'X-RAY DIFFRACTION' 3.81 4.80  . . 143 2768 99.00 . . . . 0.1887 . . . . . . . . . . . 0.2660 
'X-RAY DIFFRACTION' 4.80 51.19 . . 145 2848 99.00 . . . . 0.2077 . . . . . . . . . . . 0.2016 
# 
_struct.entry_id                     9G97 
_struct.title                        'Lipid III flippase WzxE with NB10 nanobody in outward-facing conformation at 0.9688 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        9G97 
_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 3 ? 
I N N 3 ? 
J N N 4 ? 
K N N 5 ? 
L N N 5 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
P N N 6 ? 
Q N N 7 ? 
R N N 7 ? 
S N N 8 ? 
T N N 6 ? 
U N N 6 ? 
V N N 9 ? 
W N N 9 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP WZXE_ECOLI P0AAA7 ? 1 
;SLAKASLWTAASTLVKIGAGLLVGKLLAVSFGPAGLGLAANFRQLITVLGVLAGAGIFNGVTKYVAQYHDNPQQLRRVVG
TSSAMVLGFSTLMALVFVLAAAPISQGLFGNTDYQGLVRLVALVQMGIAWGNLLLALMKGFRDAAGNALSLIVGSLIGVL
AYYVSYRLGGYEGALLGLALIPALVVIPAAIMLIKRGVIPLSYLKPSWDNGLAGQLSKFTLMALITSVTLPVAYIMMRKL
LAAQYSWDEVGIWQGVSSISDAYLQFITASFSVYLLPTLSRLTEKRDITREVVKSLKFVLPAVAAASFTVWLLRDFAIWL
LLSNKFTAMRDLFAWQLVGDVLKVGAYVFGYLVIAKASLRFYILAEVSQFTLLMVFAHWLIPAHGALGAAQAYMATYIVY
FSLCCGVFLLWRRRA
;
2 
2 PDB 9G97       9G97   ? 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 9G97 A 3 ? 417 ? P0AAA7 2  ? 416 ? 2  416 
2 2 9G97 B 1 ? 140 ? 9G97   -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 9G97 MET A 1   ? UNP P0AAA7 ? ? 'initiating methionine' 0   1  
1 9G97 VAL A 2   ? UNP P0AAA7 ? ? 'cloning artifact'      1   2  
1 9G97 LEU A 418 ? UNP P0AAA7 ? ? 'expression tag'        417 3  
1 9G97 GLU A 419 ? UNP P0AAA7 ? ? 'expression tag'        418 4  
1 9G97 GLU A 420 ? UNP P0AAA7 ? ? 'expression tag'        419 5  
1 9G97 ASN A 421 ? UNP P0AAA7 ? ? 'expression tag'        420 6  
1 9G97 LEU A 422 ? UNP P0AAA7 ? ? 'expression tag'        421 7  
1 9G97 TYR A 423 ? UNP P0AAA7 ? ? 'expression tag'        422 8  
1 9G97 PHE A 424 ? UNP P0AAA7 ? ? 'expression tag'        423 9  
1 9G97 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,R,S,T,U,V,W 
# 
_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               2.043 
_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 THR B 80  ? O THR B 78  N ASP B 75  ? N ASP B 73  
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                   9G97 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 ASN A 325 ? ? -63.45  76.82   
2 1 PHE A 327 ? ? -123.47 -59.81  
3 1 THR A 328 ? ? 44.78   9.69    
4 1 SER B 25  ? ? -93.14  -159.16 
5 1 ARG B 27  ? ? -140.01 -68.29  
6 1 VAL B 48  ? ? -120.88 -61.87  
7 1 SER B 54  ? ? -116.23 -93.62  
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 90.1855  10.6618 -2.7416  0.2402 ? -0.0076 ? -0.0474 ? 0.2691 ? 0.0094  ? 0.3066 ? 1.5143 ? 
-0.3427 ? 0.1349  ? 0.8828 ? 0.0289  ? 0.9357 ? -0.0040 ? 0.1493  ? 0.0583  ? -0.0541 ? -0.0425 ? -0.0288 ? -0.0892 ? 0.1549 ? 
0.0358 ? 
2 'X-RAY DIFFRACTION' ? refined 92.6316  18.2133 20.2917  0.3344 ? 0.0094  ? -0.0468 ? 0.2673 ? -0.0163 ? 0.3244 ? 1.7006 ? 0.2785 
? 0.1289  ? 2.1960 ? -0.4504 ? 1.5839 ? -0.0279 ? 0.0329  ? 0.0520  ? 0.1904  ? -0.0644 ? -0.2618 ? -0.0506 ? 0.1483 ? 0.0811 ? 
3 'X-RAY DIFFRACTION' ? refined 125.2020 3.3694  -18.6788 0.3095 ? 0.1084  ? 0.0564  ? 0.7765 ? 0.1098  ? 0.6941 ? 2.0491 ? 1.1620 
? -1.1771 ? 2.3386 ? 0.7391  ? 1.8611 ? 0.0263  ? -0.5592 ? -0.3191 ? -0.0810 ? -0.0998 ? -0.4186 ? 0.0542  ? 0.3718 ? 0.0727 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 2 through 232 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 233 through 418 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 5 through 127 )
;
# 
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 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LOP N1   N  N N 206 
LOP C1   C  N N 207 
LOP C2   C  N N 208 
LOP O1   O  N N 209 
LOP P1   P  N R 210 
LOP O2   O  N N 211 
LOP O3   O  N N 212 
LOP O4   O  N N 213 
LOP C3   C  N N 214 
LOP C4   C  N R 215 
LOP C5   C  N N 216 
LOP O5   O  N N 217 
LOP O6   O  N N 218 
LOP C6   C  N N 219 
LOP O7   O  N N 220 
LOP C7   C  N N 221 
LOP C8   C  N N 222 
LOP C9   C  N N 223 
LOP C10  C  N N 224 
LOP C11  C  N N 225 
LOP C12  C  N N 226 
LOP C13  C  N N 227 
LOP C14  C  N N 228 
LOP C15  C  N N 229 
LOP C16  C  N N 230 
LOP C17  C  N N 231 
LOP C18  C  N N 232 
LOP C19  C  N N 233 
LOP C20  C  N N 234 
LOP C21  C  N N 235 
LOP C22  C  N N 236 
LOP C23  C  N N 237 
LOP C24  C  N N 238 
LOP O8   O  N N 239 
LOP C25  C  N N 240 
LOP C26  C  N N 241 
LOP C27  C  N N 242 
LOP C28  C  N N 243 
LOP C29  C  N N 244 
LOP C30  C  N N 245 
LOP C31  C  N N 246 
LOP C32  C  N N 247 
LOP C33  C  N N 248 
LOP C34  C  N N 249 
LOP C35  C  N N 250 
LOP HN11 H  N N 251 
LOP HN12 H  N N 252 
LOP H11  H  N N 253 
LOP H12  H  N N 254 
LOP H21  H  N N 255 
LOP H22  H  N N 256 
LOP HO3  H  N N 257 
LOP H31  H  N N 258 
LOP H32  H  N N 259 
LOP H4   H  N N 260 
LOP H51  H  N N 261 
LOP H52  H  N N 262 
LOP H71  H  N N 263 
LOP H72  H  N N 264 
LOP H81  H  N N 265 
LOP H82  H  N N 266 
LOP H91  H  N N 267 
LOP H92  H  N N 268 
LOP H101 H  N N 269 
LOP H102 H  N N 270 
LOP H111 H  N N 271 
LOP H112 H  N N 272 
LOP H121 H  N N 273 
LOP H122 H  N N 274 
LOP H131 H  N N 275 
LOP H132 H  N N 276 
LOP H14  H  N N 277 
LOP H15  H  N N 278 
LOP H161 H  N N 279 
LOP H162 H  N N 280 
LOP H171 H  N N 281 
LOP H172 H  N N 282 
LOP H181 H  N N 283 
LOP H182 H  N N 284 
LOP H191 H  N N 285 
LOP H192 H  N N 286 
LOP H201 H  N N 287 
LOP H202 H  N N 288 
LOP H211 H  N N 289 
LOP H212 H  N N 290 
LOP H221 H  N N 291 
LOP H222 H  N N 292 
LOP H231 H  N N 293 
LOP H232 H  N N 294 
LOP H233 H  N N 295 
LOP H251 H  N N 296 
LOP H252 H  N N 297 
LOP H261 H  N N 298 
LOP H262 H  N N 299 
LOP H271 H  N N 300 
LOP H272 H  N N 301 
LOP H281 H  N N 302 
LOP H282 H  N N 303 
LOP H291 H  N N 304 
LOP H292 H  N N 305 
LOP H301 H  N N 306 
LOP H302 H  N N 307 
LOP H311 H  N N 308 
LOP H312 H  N N 309 
LOP H321 H  N N 310 
LOP H322 H  N N 311 
LOP H331 H  N N 312 
LOP H332 H  N N 313 
LOP H341 H  N N 314 
LOP H342 H  N N 315 
LOP H351 H  N N 316 
LOP H352 H  N N 317 
LOP H353 H  N N 318 
LYS N    N  N N 319 
LYS CA   C  N S 320 
LYS C    C  N N 321 
LYS O    O  N N 322 
LYS CB   C  N N 323 
LYS CG   C  N N 324 
LYS CD   C  N N 325 
LYS CE   C  N N 326 
LYS NZ   N  N N 327 
LYS OXT  O  N N 328 
LYS H    H  N N 329 
LYS H2   H  N N 330 
LYS HA   H  N N 331 
LYS HB2  H  N N 332 
LYS HB3  H  N N 333 
LYS HG2  H  N N 334 
LYS HG3  H  N N 335 
LYS HD2  H  N N 336 
LYS HD3  H  N N 337 
LYS HE2  H  N N 338 
LYS HE3  H  N N 339 
LYS HZ1  H  N N 340 
LYS HZ2  H  N N 341 
LYS HZ3  H  N N 342 
LYS HXT  H  N N 343 
MET N    N  N N 344 
MET CA   C  N S 345 
MET C    C  N N 346 
MET O    O  N N 347 
MET CB   C  N N 348 
MET CG   C  N N 349 
MET SD   S  N N 350 
MET CE   C  N N 351 
MET OXT  O  N N 352 
MET H    H  N N 353 
MET H2   H  N N 354 
MET HA   H  N N 355 
MET HB2  H  N N 356 
MET HB3  H  N N 357 
MET HG2  H  N N 358 
MET HG3  H  N N 359 
MET HE1  H  N N 360 
MET HE2  H  N N 361 
MET HE3  H  N N 362 
MET HXT  H  N N 363 
MPG C2   C  N N 364 
MPG C3   C  N N 365 
MPG C4   C  N N 366 
MPG C5   C  N N 367 
MPG C6   C  N N 368 
MPG C7   C  N N 369 
MPG C8   C  N N 370 
MPG C9   C  N N 371 
MPG C10  C  N N 372 
MPG C11  C  N N 373 
MPG C12  C  N N 374 
MPG C13  C  N N 375 
MPG C14  C  N N 376 
MPG C15  C  N N 377 
MPG C16  C  N N 378 
MPG C17  C  N N 379 
MPG C18  C  N N 380 
MPG O1   O  N N 381 
MPG C1   C  N N 382 
MPG CXD  C  N R 383 
MPG O2   O  N N 384 
MPG C21  C  N N 385 
MPG O3   O  N N 386 
MPG O4   O  N N 387 
MPG CX3  C  N N 388 
MPG H21C H  N N 389 
MPG H22C H  N N 390 
MPG H31C H  N N 391 
MPG H32C H  N N 392 
MPG H41C H  N N 393 
MPG H42C H  N N 394 
MPG H51C H  N N 395 
MPG H52C H  N N 396 
MPG H61C H  N N 397 
MPG H62C H  N N 398 
MPG H71C H  N N 399 
MPG H72C H  N N 400 
MPG H81C H  N N 401 
MPG H82C H  N N 402 
MPG H9   H  N N 403 
MPG H10  H  N N 404 
MPG H111 H  N N 405 
MPG H112 H  N N 406 
MPG H121 H  N N 407 
MPG H122 H  N N 408 
MPG H131 H  N N 409 
MPG H132 H  N N 410 
MPG H141 H  N N 411 
MPG H142 H  N N 412 
MPG H151 H  N N 413 
MPG H152 H  N N 414 
MPG H161 H  N N 415 
MPG H162 H  N N 416 
MPG H171 H  N N 417 
MPG H172 H  N N 418 
MPG H181 H  N N 419 
MPG H182 H  N N 420 
MPG H183 H  N N 421 
MPG HX31 H  N N 422 
MPG HX32 H  N N 423 
MPG HXD  H  N N 424 
MPG H2   H  N N 425 
MPG H211 H  N N 426 
MPG H212 H  N N 427 
MPG H3   H  N N 428 
OCT C1   C  N N 429 
OCT C2   C  N N 430 
OCT C3   C  N N 431 
OCT C4   C  N N 432 
OCT C5   C  N N 433 
OCT C6   C  N N 434 
OCT C7   C  N N 435 
OCT C8   C  N N 436 
OCT H11  H  N N 437 
OCT H12  H  N N 438 
OCT H13  H  N N 439 
OCT H21  H  N N 440 
OCT H22  H  N N 441 
OCT H31  H  N N 442 
OCT H32  H  N N 443 
OCT H41  H  N N 444 
OCT H42  H  N N 445 
OCT H51  H  N N 446 
OCT H52  H  N N 447 
OCT H61  H  N N 448 
OCT H62  H  N N 449 
OCT H71  H  N N 450 
OCT H72  H  N N 451 
OCT H81  H  N N 452 
OCT H82  H  N N 453 
OCT H83  H  N N 454 
PHE N    N  N N 455 
PHE CA   C  N S 456 
PHE C    C  N N 457 
PHE O    O  N N 458 
PHE CB   C  N N 459 
PHE CG   C  Y N 460 
PHE CD1  C  Y N 461 
PHE CD2  C  Y N 462 
PHE CE1  C  Y N 463 
PHE CE2  C  Y N 464 
PHE CZ   C  Y N 465 
PHE OXT  O  N N 466 
PHE H    H  N N 467 
PHE H2   H  N N 468 
PHE HA   H  N N 469 
PHE HB2  H  N N 470 
PHE HB3  H  N N 471 
PHE HD1  H  N N 472 
PHE HD2  H  N N 473 
PHE HE1  H  N N 474 
PHE HE2  H  N N 475 
PHE HZ   H  N N 476 
PHE HXT  H  N N 477 
PRO N    N  N N 478 
PRO CA   C  N S 479 
PRO C    C  N N 480 
PRO O    O  N N 481 
PRO CB   C  N N 482 
PRO CG   C  N N 483 
PRO CD   C  N N 484 
PRO OXT  O  N N 485 
PRO H    H  N N 486 
PRO HA   H  N N 487 
PRO HB2  H  N N 488 
PRO HB3  H  N N 489 
PRO HG2  H  N N 490 
PRO HG3  H  N N 491 
PRO HD2  H  N N 492 
PRO HD3  H  N N 493 
PRO HXT  H  N N 494 
SER N    N  N N 495 
SER CA   C  N S 496 
SER C    C  N N 497 
SER O    O  N N 498 
SER CB   C  N N 499 
SER OG   O  N N 500 
SER OXT  O  N N 501 
SER H    H  N N 502 
SER H2   H  N N 503 
SER HA   H  N N 504 
SER HB2  H  N N 505 
SER HB3  H  N N 506 
SER HG   H  N N 507 
SER HXT  H  N N 508 
SO4 S    S  N N 509 
SO4 O1   O  N N 510 
SO4 O2   O  N N 511 
SO4 O3   O  N N 512 
SO4 O4   O  N N 513 
THR N    N  N N 514 
THR CA   C  N S 515 
THR C    C  N N 516 
THR O    O  N N 517 
THR CB   C  N R 518 
THR OG1  O  N N 519 
THR CG2  C  N N 520 
THR OXT  O  N N 521 
THR H    H  N N 522 
THR H2   H  N N 523 
THR HA   H  N N 524 
THR HB   H  N N 525 
THR HG1  H  N N 526 
THR HG21 H  N N 527 
THR HG22 H  N N 528 
THR HG23 H  N N 529 
THR HXT  H  N N 530 
TRP N    N  N N 531 
TRP CA   C  N S 532 
TRP C    C  N N 533 
TRP O    O  N N 534 
TRP CB   C  N N 535 
TRP CG   C  Y N 536 
TRP CD1  C  Y N 537 
TRP CD2  C  Y N 538 
TRP NE1  N  Y N 539 
TRP CE2  C  Y N 540 
TRP CE3  C  Y N 541 
TRP CZ2  C  Y N 542 
TRP CZ3  C  Y N 543 
TRP CH2  C  Y N 544 
TRP OXT  O  N N 545 
TRP H    H  N N 546 
TRP H2   H  N N 547 
TRP HA   H  N N 548 
TRP HB2  H  N N 549 
TRP HB3  H  N N 550 
TRP HD1  H  N N 551 
TRP HE1  H  N N 552 
TRP HE3  H  N N 553 
TRP HZ2  H  N N 554 
TRP HZ3  H  N N 555 
TRP HH2  H  N N 556 
TRP HXT  H  N N 557 
TYR N    N  N N 558 
TYR CA   C  N S 559 
TYR C    C  N N 560 
TYR O    O  N N 561 
TYR CB   C  N N 562 
TYR CG   C  Y N 563 
TYR CD1  C  Y N 564 
TYR CD2  C  Y N 565 
TYR CE1  C  Y N 566 
TYR CE2  C  Y N 567 
TYR CZ   C  Y N 568 
TYR OH   O  N N 569 
TYR OXT  O  N N 570 
TYR H    H  N N 571 
TYR H2   H  N N 572 
TYR HA   H  N N 573 
TYR HB2  H  N N 574 
TYR HB3  H  N N 575 
TYR HD1  H  N N 576 
TYR HD2  H  N N 577 
TYR HE1  H  N N 578 
TYR HE2  H  N N 579 
TYR HH   H  N N 580 
TYR HXT  H  N N 581 
VAL N    N  N N 582 
VAL CA   C  N S 583 
VAL C    C  N N 584 
VAL O    O  N N 585 
VAL CB   C  N N 586 
VAL CG1  C  N N 587 
VAL CG2  C  N N 588 
VAL OXT  O  N N 589 
VAL H    H  N N 590 
VAL H2   H  N N 591 
VAL HA   H  N N 592 
VAL HB   H  N N 593 
VAL HG11 H  N N 594 
VAL HG12 H  N N 595 
VAL HG13 H  N N 596 
VAL HG21 H  N N 597 
VAL HG22 H  N N 598 
VAL HG23 H  N N 599 
VAL HXT  H  N N 600 
ZN  ZN   ZN N N 601 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LOP N1  C1   sing N N 194 
LOP N1  HN11 sing N N 195 
LOP N1  HN12 sing N N 196 
LOP C1  C2   sing N N 197 
LOP C1  H11  sing N N 198 
LOP C1  H12  sing N N 199 
LOP C2  O1   sing N N 200 
LOP C2  H21  sing N N 201 
LOP C2  H22  sing N N 202 
LOP O1  P1   sing N N 203 
LOP P1  O2   sing N N 204 
LOP P1  O3   sing N N 205 
LOP P1  O4   doub N N 206 
LOP O2  C3   sing N N 207 
LOP O3  HO3  sing N N 208 
LOP C3  C4   sing N N 209 
LOP C3  H31  sing N N 210 
LOP C3  H32  sing N N 211 
LOP C4  C5   sing N N 212 
LOP C4  O5   sing N N 213 
LOP C4  H4   sing N N 214 
LOP C5  O6   sing N N 215 
LOP C5  H51  sing N N 216 
LOP C5  H52  sing N N 217 
LOP O5  C6   sing N N 218 
LOP O6  C24  sing N N 219 
LOP C6  O7   doub N N 220 
LOP C6  C7   sing N N 221 
LOP C7  C8   sing N N 222 
LOP C7  H71  sing N N 223 
LOP C7  H72  sing N N 224 
LOP C8  C9   sing N N 225 
LOP C8  H81  sing N N 226 
LOP C8  H82  sing N N 227 
LOP C9  C10  sing N N 228 
LOP C9  H91  sing N N 229 
LOP C9  H92  sing N N 230 
LOP C10 C11  sing N N 231 
LOP C10 H101 sing N N 232 
LOP C10 H102 sing N N 233 
LOP C11 C12  sing N N 234 
LOP C11 H111 sing N N 235 
LOP C11 H112 sing N N 236 
LOP C12 C13  sing N N 237 
LOP C12 H121 sing N N 238 
LOP C12 H122 sing N N 239 
LOP C13 C14  sing N N 240 
LOP C13 H131 sing N N 241 
LOP C13 H132 sing N N 242 
LOP C14 C15  doub N Z 243 
LOP C14 H14  sing N N 244 
LOP C15 C16  sing N N 245 
LOP C15 H15  sing N N 246 
LOP C16 C17  sing N N 247 
LOP C16 H161 sing N N 248 
LOP C16 H162 sing N N 249 
LOP C17 C18  sing N N 250 
LOP C17 H171 sing N N 251 
LOP C17 H172 sing N N 252 
LOP C18 C19  sing N N 253 
LOP C18 H181 sing N N 254 
LOP C18 H182 sing N N 255 
LOP C19 C20  sing N N 256 
LOP C19 H191 sing N N 257 
LOP C19 H192 sing N N 258 
LOP C20 C21  sing N N 259 
LOP C20 H201 sing N N 260 
LOP C20 H202 sing N N 261 
LOP C21 C22  sing N N 262 
LOP C21 H211 sing N N 263 
LOP C21 H212 sing N N 264 
LOP C22 C23  sing N N 265 
LOP C22 H221 sing N N 266 
LOP C22 H222 sing N N 267 
LOP C23 H231 sing N N 268 
LOP C23 H232 sing N N 269 
LOP C23 H233 sing N N 270 
LOP C24 O8   doub N N 271 
LOP C24 C25  sing N N 272 
LOP C25 C26  sing N N 273 
LOP C25 H251 sing N N 274 
LOP C25 H252 sing N N 275 
LOP C26 C27  sing N N 276 
LOP C26 H261 sing N N 277 
LOP C26 H262 sing N N 278 
LOP C27 C28  sing N N 279 
LOP C27 H271 sing N N 280 
LOP C27 H272 sing N N 281 
LOP C28 C29  sing N N 282 
LOP C28 H281 sing N N 283 
LOP C28 H282 sing N N 284 
LOP C29 C30  sing N N 285 
LOP C29 H291 sing N N 286 
LOP C29 H292 sing N N 287 
LOP C30 C31  sing N N 288 
LOP C30 H301 sing N N 289 
LOP C30 H302 sing N N 290 
LOP C31 C32  sing N N 291 
LOP C31 H311 sing N N 292 
LOP C31 H312 sing N N 293 
LOP C32 C33  sing N N 294 
LOP C32 H321 sing N N 295 
LOP C32 H322 sing N N 296 
LOP C33 C34  sing N N 297 
LOP C33 H331 sing N N 298 
LOP C33 H332 sing N N 299 
LOP C34 C35  sing N N 300 
LOP C34 H341 sing N N 301 
LOP C34 H342 sing N N 302 
LOP C35 H351 sing N N 303 
LOP C35 H352 sing N N 304 
LOP C35 H353 sing N N 305 
LYS N   CA   sing N N 306 
LYS N   H    sing N N 307 
LYS N   H2   sing N N 308 
LYS CA  C    sing N N 309 
LYS CA  CB   sing N N 310 
LYS CA  HA   sing N N 311 
LYS C   O    doub N N 312 
LYS C   OXT  sing N N 313 
LYS CB  CG   sing N N 314 
LYS CB  HB2  sing N N 315 
LYS CB  HB3  sing N N 316 
LYS CG  CD   sing N N 317 
LYS CG  HG2  sing N N 318 
LYS CG  HG3  sing N N 319 
LYS CD  CE   sing N N 320 
LYS CD  HD2  sing N N 321 
LYS CD  HD3  sing N N 322 
LYS CE  NZ   sing N N 323 
LYS CE  HE2  sing N N 324 
LYS CE  HE3  sing N N 325 
LYS NZ  HZ1  sing N N 326 
LYS NZ  HZ2  sing N N 327 
LYS NZ  HZ3  sing N N 328 
LYS OXT HXT  sing N N 329 
MET N   CA   sing N N 330 
MET N   H    sing N N 331 
MET N   H2   sing N N 332 
MET CA  C    sing N N 333 
MET CA  CB   sing N N 334 
MET CA  HA   sing N N 335 
MET C   O    doub N N 336 
MET C   OXT  sing N N 337 
MET CB  CG   sing N N 338 
MET CB  HB2  sing N N 339 
MET CB  HB3  sing N N 340 
MET CG  SD   sing N N 341 
MET CG  HG2  sing N N 342 
MET CG  HG3  sing N N 343 
MET SD  CE   sing N N 344 
MET CE  HE1  sing N N 345 
MET CE  HE2  sing N N 346 
MET CE  HE3  sing N N 347 
MET OXT HXT  sing N N 348 
MPG C2  C3   sing N N 349 
MPG C2  C1   sing N N 350 
MPG C3  C4   sing N N 351 
MPG C4  C5   sing N N 352 
MPG C5  C6   sing N N 353 
MPG C6  C7   sing N N 354 
MPG C7  C8   sing N N 355 
MPG C8  C9   sing N N 356 
MPG C9  C10  doub N Z 357 
MPG C10 C11  sing N N 358 
MPG C11 C12  sing N N 359 
MPG C12 C13  sing N N 360 
MPG C13 C14  sing N N 361 
MPG C14 C15  sing N N 362 
MPG C15 C16  sing N N 363 
MPG C16 C17  sing N N 364 
MPG C17 C18  sing N N 365 
MPG O1  C1   sing N N 366 
MPG O1  CX3  sing N N 367 
MPG CXD O2   sing N N 368 
MPG CXD C21  sing N N 369 
MPG CXD CX3  sing N N 370 
MPG C21 O3   sing N N 371 
MPG C2  H21C sing N N 372 
MPG C2  H22C sing N N 373 
MPG C3  H31C sing N N 374 
MPG C3  H32C sing N N 375 
MPG CX3 O4   doub N N 376 
MPG C4  H41C sing N N 377 
MPG C4  H42C sing N N 378 
MPG C5  H51C sing N N 379 
MPG C5  H52C sing N N 380 
MPG C6  H61C sing N N 381 
MPG C6  H62C sing N N 382 
MPG C7  H71C sing N N 383 
MPG C7  H72C sing N N 384 
MPG C8  H81C sing N N 385 
MPG C8  H82C sing N N 386 
MPG C9  H9   sing N N 387 
MPG C10 H10  sing N N 388 
MPG C11 H111 sing N N 389 
MPG C11 H112 sing N N 390 
MPG C12 H121 sing N N 391 
MPG C12 H122 sing N N 392 
MPG C13 H131 sing N N 393 
MPG C13 H132 sing N N 394 
MPG C14 H141 sing N N 395 
MPG C14 H142 sing N N 396 
MPG C15 H151 sing N N 397 
MPG C15 H152 sing N N 398 
MPG C16 H161 sing N N 399 
MPG C16 H162 sing N N 400 
MPG C17 H171 sing N N 401 
MPG C17 H172 sing N N 402 
MPG C18 H181 sing N N 403 
MPG C18 H182 sing N N 404 
MPG C18 H183 sing N N 405 
MPG C1  HX31 sing N N 406 
MPG C1  HX32 sing N N 407 
MPG CXD HXD  sing N N 408 
MPG O2  H2   sing N N 409 
MPG C21 H211 sing N N 410 
MPG C21 H212 sing N N 411 
MPG O3  H3   sing N N 412 
OCT C1  C2   sing N N 413 
OCT C1  H11  sing N N 414 
OCT C1  H12  sing N N 415 
OCT C1  H13  sing N N 416 
OCT C2  C3   sing N N 417 
OCT C2  H21  sing N N 418 
OCT C2  H22  sing N N 419 
OCT C3  C4   sing N N 420 
OCT C3  H31  sing N N 421 
OCT C3  H32  sing N N 422 
OCT C4  C5   sing N N 423 
OCT C4  H41  sing N N 424 
OCT C4  H42  sing N N 425 
OCT C5  C6   sing N N 426 
OCT C5  H51  sing N N 427 
OCT C5  H52  sing N N 428 
OCT C6  C7   sing N N 429 
OCT C6  H61  sing N N 430 
OCT C6  H62  sing N N 431 
OCT C7  C8   sing N N 432 
OCT C7  H71  sing N N 433 
OCT C7  H72  sing N N 434 
OCT C8  H81  sing N N 435 
OCT C8  H82  sing N N 436 
OCT C8  H83  sing N N 437 
PHE N   CA   sing N N 438 
PHE N   H    sing N N 439 
PHE N   H2   sing N N 440 
PHE CA  C    sing N N 441 
PHE CA  CB   sing N N 442 
PHE CA  HA   sing N N 443 
PHE C   O    doub N N 444 
PHE C   OXT  sing N N 445 
PHE CB  CG   sing N N 446 
PHE CB  HB2  sing N N 447 
PHE CB  HB3  sing N N 448 
PHE CG  CD1  doub Y N 449 
PHE CG  CD2  sing Y N 450 
PHE CD1 CE1  sing Y N 451 
PHE CD1 HD1  sing N N 452 
PHE CD2 CE2  doub Y N 453 
PHE CD2 HD2  sing N N 454 
PHE CE1 CZ   doub Y N 455 
PHE CE1 HE1  sing N N 456 
PHE CE2 CZ   sing Y N 457 
PHE CE2 HE2  sing N N 458 
PHE CZ  HZ   sing N N 459 
PHE OXT HXT  sing N N 460 
PRO N   CA   sing N N 461 
PRO N   CD   sing N N 462 
PRO N   H    sing N N 463 
PRO CA  C    sing N N 464 
PRO CA  CB   sing N N 465 
PRO CA  HA   sing N N 466 
PRO C   O    doub N N 467 
PRO C   OXT  sing N N 468 
PRO CB  CG   sing N N 469 
PRO CB  HB2  sing N N 470 
PRO CB  HB3  sing N N 471 
PRO CG  CD   sing N N 472 
PRO CG  HG2  sing N N 473 
PRO CG  HG3  sing N N 474 
PRO CD  HD2  sing N N 475 
PRO CD  HD3  sing N N 476 
PRO OXT HXT  sing N N 477 
SER N   CA   sing N N 478 
SER N   H    sing N N 479 
SER N   H2   sing N N 480 
SER CA  C    sing N N 481 
SER CA  CB   sing N N 482 
SER CA  HA   sing N N 483 
SER C   O    doub N N 484 
SER C   OXT  sing N N 485 
SER CB  OG   sing N N 486 
SER CB  HB2  sing N N 487 
SER CB  HB3  sing N N 488 
SER OG  HG   sing N N 489 
SER OXT HXT  sing N N 490 
SO4 S   O1   doub N N 491 
SO4 S   O2   doub N N 492 
SO4 S   O3   sing N N 493 
SO4 S   O4   sing N N 494 
THR N   CA   sing N N 495 
THR N   H    sing N N 496 
THR N   H2   sing N N 497 
THR CA  C    sing N N 498 
THR CA  CB   sing N N 499 
THR CA  HA   sing N N 500 
THR C   O    doub N N 501 
THR C   OXT  sing N N 502 
THR CB  OG1  sing N N 503 
THR CB  CG2  sing N N 504 
THR CB  HB   sing N N 505 
THR OG1 HG1  sing N N 506 
THR CG2 HG21 sing N N 507 
THR CG2 HG22 sing N N 508 
THR CG2 HG23 sing N N 509 
THR OXT HXT  sing N N 510 
TRP N   CA   sing N N 511 
TRP N   H    sing N N 512 
TRP N   H2   sing N N 513 
TRP CA  C    sing N N 514 
TRP CA  CB   sing N N 515 
TRP CA  HA   sing N N 516 
TRP C   O    doub N N 517 
TRP C   OXT  sing N N 518 
TRP CB  CG   sing N N 519 
TRP CB  HB2  sing N N 520 
TRP CB  HB3  sing N N 521 
TRP CG  CD1  doub Y N 522 
TRP CG  CD2  sing Y N 523 
TRP CD1 NE1  sing Y N 524 
TRP CD1 HD1  sing N N 525 
TRP CD2 CE2  doub Y N 526 
TRP CD2 CE3  sing Y N 527 
TRP NE1 CE2  sing Y N 528 
TRP NE1 HE1  sing N N 529 
TRP CE2 CZ2  sing Y N 530 
TRP CE3 CZ3  doub Y N 531 
TRP CE3 HE3  sing N N 532 
TRP CZ2 CH2  doub Y N 533 
TRP CZ2 HZ2  sing N N 534 
TRP CZ3 CH2  sing Y N 535 
TRP CZ3 HZ3  sing N N 536 
TRP CH2 HH2  sing N N 537 
TRP OXT HXT  sing N N 538 
TYR N   CA   sing N N 539 
TYR N   H    sing N N 540 
TYR N   H2   sing N N 541 
TYR CA  C    sing N N 542 
TYR CA  CB   sing N N 543 
TYR CA  HA   sing N N 544 
TYR C   O    doub N N 545 
TYR C   OXT  sing N N 546 
TYR CB  CG   sing N N 547 
TYR CB  HB2  sing N N 548 
TYR CB  HB3  sing N N 549 
TYR CG  CD1  doub Y N 550 
TYR CG  CD2  sing Y N 551 
TYR CD1 CE1  sing Y N 552 
TYR CD1 HD1  sing N N 553 
TYR CD2 CE2  doub Y N 554 
TYR CD2 HD2  sing N N 555 
TYR CE1 CZ   doub Y N 556 
TYR CE1 HE1  sing N N 557 
TYR CE2 CZ   sing Y N 558 
TYR CE2 HE2  sing N N 559 
TYR CZ  OH   sing N N 560 
TYR OH  HH   sing N N 561 
TYR OXT HXT  sing N N 562 
VAL N   CA   sing N N 563 
VAL N   H    sing N N 564 
VAL N   H2   sing N N 565 
VAL CA  C    sing N N 566 
VAL CA  CB   sing N N 567 
VAL CA  HA   sing N N 568 
VAL C   O    doub N N 569 
VAL C   OXT  sing N N 570 
VAL CB  CG1  sing N N 571 
VAL CB  CG2  sing N N 572 
VAL CB  HB   sing N N 573 
VAL CG1 HG11 sing N N 574 
VAL CG1 HG12 sing N N 575 
VAL CG1 HG13 sing N N 576 
VAL CG2 HG21 sing N N 577 
VAL CG2 HG22 sing N N 578 
VAL CG2 HG23 sing N N 579 
VAL OXT HXT  sing N N 580 
# 
_pdbx_audit_support.funding_organization   'Wellcome Trust' 
_pdbx_audit_support.country                'United Kingdom' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   9G95 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9G97 
_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]   0.003696 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000226 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.025994 
_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]   0.017629 
_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  
P  
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   ? 69.706  4.818   13.384  1.00 55.57  ? 1   VAL A N   1 
ATOM   2    C  CA  . VAL A 1 2   ? 71.148  5.023   13.284  1.00 55.47  ? 1   VAL A CA  1 
ATOM   3    C  C   . VAL A 1 2   ? 71.611  5.908   14.439  1.00 49.84  ? 1   VAL A C   1 
ATOM   4    O  O   . VAL A 1 2   ? 70.824  6.683   14.985  1.00 52.86  ? 1   VAL A O   1 
ATOM   5    C  CB  . VAL A 1 2   ? 71.538  5.630   11.927  1.00 50.68  ? 1   VAL A CB  1 
ATOM   6    C  CG1 . VAL A 1 2   ? 71.436  7.142   11.967  1.00 54.01  ? 1   VAL A CG1 1 
ATOM   7    C  CG2 . VAL A 1 2   ? 72.942  5.205   11.540  1.00 59.61  ? 1   VAL A CG2 1 
ATOM   8    N  N   . SER A 1 3   ? 72.884  5.781   14.813  1.00 44.30  ? 2   SER A N   1 
ATOM   9    C  CA  . SER A 1 3   ? 73.416  6.465   15.984  1.00 42.66  ? 2   SER A CA  1 
ATOM   10   C  C   . SER A 1 3   ? 74.917  6.655   15.829  1.00 39.86  ? 2   SER A C   1 
ATOM   11   O  O   . SER A 1 3   ? 75.559  6.040   14.975  1.00 39.75  ? 2   SER A O   1 
ATOM   12   C  CB  . SER A 1 3   ? 73.138  5.684   17.267  1.00 40.14  ? 2   SER A CB  1 
ATOM   13   O  OG  . SER A 1 3   ? 74.236  4.834   17.550  1.00 48.42  ? 2   SER A OG  1 
ATOM   14   N  N   . LEU A 1 4   ? 75.480  7.499   16.696  1.00 36.16  ? 3   LEU A N   1 
ATOM   15   C  CA  . LEU A 1 4   ? 76.923  7.716   16.680  1.00 38.53  ? 3   LEU A CA  1 
ATOM   16   C  C   . LEU A 1 4   ? 77.685  6.465   17.087  1.00 38.37  ? 3   LEU A C   1 
ATOM   17   O  O   . LEU A 1 4   ? 78.780  6.210   16.567  1.00 38.31  ? 3   LEU A O   1 
ATOM   18   C  CB  . LEU A 1 4   ? 77.289  8.877   17.601  1.00 40.97  ? 3   LEU A CB  1 
ATOM   19   C  CG  . LEU A 1 4   ? 78.752  9.312   17.623  1.00 37.07  ? 3   LEU A CG  1 
ATOM   20   C  CD1 . LEU A 1 4   ? 79.263  9.596   16.214  1.00 37.89  ? 3   LEU A CD1 1 
ATOM   21   C  CD2 . LEU A 1 4   ? 78.916  10.533  18.522  1.00 41.08  ? 3   LEU A CD2 1 
ATOM   22   N  N   . ALA A 1 5   ? 77.124  5.672   18.003  1.00 35.58  ? 4   ALA A N   1 
ATOM   23   C  CA  . ALA A 1 5   ? 77.799  4.459   18.449  1.00 39.74  ? 4   ALA A CA  1 
ATOM   24   C  C   . ALA A 1 5   ? 77.884  3.430   17.327  1.00 37.77  ? 4   ALA A C   1 
ATOM   25   O  O   . ALA A 1 5   ? 78.967  2.916   17.030  1.00 42.38  ? 4   ALA A O   1 
ATOM   26   C  CB  . ALA A 1 5   ? 77.083  3.877   19.668  1.00 42.88  ? 4   ALA A CB  1 
ATOM   27   N  N   . LYS A 1 6   ? 76.749  3.117   16.690  1.00 45.17  ? 5   LYS A N   1 
ATOM   28   C  CA  . LYS A 1 6   ? 76.762  2.159   15.585  1.00 42.30  ? 5   LYS A CA  1 
ATOM   29   C  C   . LYS A 1 6   ? 77.641  2.639   14.443  1.00 34.05  ? 5   LYS A C   1 
ATOM   30   O  O   . LYS A 1 6   ? 78.341  1.837   13.815  1.00 43.89  ? 5   LYS A O   1 
ATOM   31   C  CB  . LYS A 1 6   ? 75.348  1.898   15.067  1.00 45.28  ? 5   LYS A CB  1 
ATOM   32   C  CG  . LYS A 1 6   ? 74.385  1.356   16.094  1.00 52.70  ? 5   LYS A CG  1 
ATOM   33   C  CD  . LYS A 1 6   ? 73.060  2.075   15.986  1.00 54.52  ? 5   LYS A CD  1 
ATOM   34   C  CE  . LYS A 1 6   ? 71.911  1.106   15.819  1.00 66.37  ? 5   LYS A CE  1 
ATOM   35   N  NZ  . LYS A 1 6   ? 70.639  1.686   16.340  1.00 72.79  ? 5   LYS A NZ  1 
ATOM   36   N  N   . ALA A 1 7   ? 77.602  3.937   14.140  1.00 34.64  ? 6   ALA A N   1 
ATOM   37   C  CA  . ALA A 1 7   ? 78.467  4.457   13.086  1.00 37.53  ? 6   ALA A CA  1 
ATOM   38   C  C   . ALA A 1 7   ? 79.928  4.281   13.459  1.00 36.71  ? 6   ALA A C   1 
ATOM   39   O  O   . ALA A 1 7   ? 80.767  3.979   12.601  1.00 38.40  ? 6   ALA A O   1 
ATOM   40   C  CB  . ALA A 1 7   ? 78.153  5.929   12.815  1.00 30.80  ? 6   ALA A CB  1 
ATOM   41   N  N   . SER A 1 8   ? 80.246  4.445   14.745  1.00 36.71  ? 7   SER A N   1 
ATOM   42   C  CA  . SER A 1 8   ? 81.610  4.227   15.204  1.00 38.64  ? 7   SER A CA  1 
ATOM   43   C  C   . SER A 1 8   ? 82.021  2.772   15.036  1.00 35.93  ? 7   SER A C   1 
ATOM   44   O  O   . SER A 1 8   ? 83.186  2.486   14.740  1.00 39.55  ? 7   SER A O   1 
ATOM   45   C  CB  . SER A 1 8   ? 81.745  4.654   16.662  1.00 37.65  ? 7   SER A CB  1 
ATOM   46   O  OG  . SER A 1 8   ? 81.505  6.043   16.789  1.00 41.40  ? 7   SER A OG  1 
ATOM   47   N  N   . LEU A 1 9   ? 81.078  1.844   15.202  1.00 38.62  ? 8   LEU A N   1 
ATOM   48   C  CA  . LEU A 1 9   ? 81.401  0.427   15.061  1.00 40.92  ? 8   LEU A CA  1 
ATOM   49   C  C   . LEU A 1 9   ? 81.764  0.085   13.622  1.00 35.92  ? 8   LEU A C   1 
ATOM   50   O  O   . LEU A 1 9   ? 82.757  -0.608  13.370  1.00 36.82  ? 8   LEU A O   1 
ATOM   51   C  CB  . LEU A 1 9   ? 80.228  -0.424  15.537  1.00 41.73  ? 8   LEU A CB  1 
ATOM   52   C  CG  . LEU A 1 9   ? 80.608  -1.800  16.076  1.00 45.78  ? 8   LEU A CG  1 
ATOM   53   C  CD1 . LEU A 1 9   ? 81.743  -1.695  17.089  1.00 43.26  ? 8   LEU A CD1 1 
ATOM   54   C  CD2 . LEU A 1 9   ? 79.388  -2.474  16.686  1.00 43.49  ? 8   LEU A CD2 1 
ATOM   55   N  N   . TRP A 1 10  ? 80.968  0.567   12.664  1.00 36.98  ? 9   TRP A N   1 
ATOM   56   C  CA  . TRP A 1 10  ? 81.311  0.400   11.254  1.00 36.09  ? 9   TRP A CA  1 
ATOM   57   C  C   . TRP A 1 10  ? 82.617  1.110   10.923  1.00 33.92  ? 9   TRP A C   1 
ATOM   58   O  O   . TRP A 1 10  ? 83.515  0.529   10.304  1.00 30.45  ? 9   TRP A O   1 
ATOM   59   C  CB  . TRP A 1 10  ? 80.188  0.940   10.367  1.00 35.54  ? 9   TRP A CB  1 
ATOM   60   C  CG  . TRP A 1 10  ? 79.055  0.000   10.159  1.00 35.65  ? 9   TRP A CG  1 
ATOM   61   C  CD1 . TRP A 1 10  ? 77.796  0.108   10.675  1.00 38.11  ? 9   TRP A CD1 1 
ATOM   62   C  CD2 . TRP A 1 10  ? 79.062  -1.187  9.362   1.00 34.39  ? 9   TRP A CD2 1 
ATOM   63   N  NE1 . TRP A 1 10  ? 77.019  -0.942  10.251  1.00 36.44  ? 9   TRP A NE1 1 
ATOM   64   C  CE2 . TRP A 1 10  ? 77.775  -1.753  9.447   1.00 38.00  ? 9   TRP A CE2 1 
ATOM   65   C  CE3 . TRP A 1 10  ? 80.031  -1.830  8.592   1.00 37.24  ? 9   TRP A CE3 1 
ATOM   66   C  CZ2 . TRP A 1 10  ? 77.434  -2.933  8.792   1.00 40.24  ? 9   TRP A CZ2 1 
ATOM   67   C  CZ3 . TRP A 1 10  ? 79.689  -3.000  7.937   1.00 39.90  ? 9   TRP A CZ3 1 
ATOM   68   C  CH2 . TRP A 1 10  ? 78.404  -3.540  8.043   1.00 41.33  ? 9   TRP A CH2 1 
ATOM   69   N  N   . THR A 1 11  ? 82.736  2.381   11.319  1.00 34.57  ? 10  THR A N   1 
ATOM   70   C  CA  . THR A 1 11  ? 83.907  3.160   10.925  1.00 34.91  ? 10  THR A CA  1 
ATOM   71   C  C   . THR A 1 11  ? 85.185  2.643   11.576  1.00 31.33  ? 10  THR A C   1 
ATOM   72   O  O   . THR A 1 11  ? 86.257  2.737   10.970  1.00 35.29  ? 10  THR A O   1 
ATOM   73   C  CB  . THR A 1 11  ? 83.705  4.647   11.244  1.00 35.04  ? 10  THR A CB  1 
ATOM   74   O  OG1 . THR A 1 11  ? 82.408  5.072   10.803  1.00 32.92  ? 10  THR A OG1 1 
ATOM   75   C  CG2 . THR A 1 11  ? 84.756  5.486   10.545  1.00 34.61  ? 10  THR A CG2 1 
ATOM   76   N  N   . ALA A 1 12  ? 85.103  2.089   12.790  1.00 29.77  ? 11  ALA A N   1 
ATOM   77   C  CA  . ALA A 1 12  ? 86.304  1.523   13.404  1.00 33.46  ? 11  ALA A CA  1 
ATOM   78   C  C   . ALA A 1 12  ? 86.822  0.330   12.606  1.00 33.73  ? 11  ALA A C   1 
ATOM   79   O  O   . ALA A 1 12  ? 88.037  0.159   12.447  1.00 31.35  ? 11  ALA A O   1 
ATOM   80   C  CB  . ALA A 1 12  ? 86.027  1.118   14.850  1.00 26.16  ? 11  ALA A CB  1 
ATOM   81   N  N   . ALA A 1 13  ? 85.914  -0.505  12.093  1.00 32.78  ? 12  ALA A N   1 
ATOM   82   C  CA  . ALA A 1 13  ? 86.337  -1.657  11.304  1.00 32.54  ? 12  ALA A CA  1 
ATOM   83   C  C   . ALA A 1 13  ? 87.046  -1.222  10.026  1.00 33.64  ? 12  ALA A C   1 
ATOM   84   O  O   . ALA A 1 13  ? 88.095  -1.773  9.669   1.00 33.58  ? 12  ALA A O   1 
ATOM   85   C  CB  . ALA A 1 13  ? 85.133  -2.543  10.984  1.00 34.64  ? 12  ALA A CB  1 
ATOM   86   N  N   . SER A 1 14  ? 86.504  -0.223  9.330   1.00 30.45  ? 13  SER A N   1 
ATOM   87   C  CA  . SER A 1 14  ? 87.170  0.240   8.118   1.00 32.07  ? 13  SER A CA  1 
ATOM   88   C  C   . SER A 1 14  ? 88.485  0.946   8.445   1.00 34.56  ? 13  SER A C   1 
ATOM   89   O  O   . SER A 1 14  ? 89.487  0.757   7.747   1.00 33.80  ? 13  SER A O   1 
ATOM   90   C  CB  . SER A 1 14  ? 86.236  1.142   7.307   1.00 32.98  ? 13  SER A CB  1 
ATOM   91   O  OG  . SER A 1 14  ? 85.783  2.254   8.055   1.00 34.26  ? 13  SER A OG  1 
ATOM   92   N  N   . THR A 1 15  ? 88.518  1.738   9.516   1.00 31.30  ? 14  THR A N   1 
ATOM   93   C  CA  . THR A 1 15  ? 89.764  2.417   9.860   1.00 34.15  ? 14  THR A CA  1 
ATOM   94   C  C   . THR A 1 15  ? 90.832  1.422   10.304  1.00 36.11  ? 14  THR A C   1 
ATOM   95   O  O   . THR A 1 15  ? 92.012  1.589   9.980   1.00 37.66  ? 14  THR A O   1 
ATOM   96   C  CB  . THR A 1 15  ? 89.519  3.480   10.936  1.00 37.74  ? 14  THR A CB  1 
ATOM   97   O  OG1 . THR A 1 15  ? 88.427  4.320   10.537  1.00 38.40  ? 14  THR A OG1 1 
ATOM   98   C  CG2 . THR A 1 15  ? 90.747  4.353   11.118  1.00 39.35  ? 14  THR A CG2 1 
ATOM   99   N  N   . LEU A 1 16  ? 90.442  0.364   11.018  1.00 34.35  ? 15  LEU A N   1 
ATOM   100  C  CA  . LEU A 1 16  ? 91.432  -0.621  11.447  1.00 37.89  ? 15  LEU A CA  1 
ATOM   101  C  C   . LEU A 1 16  ? 92.035  -1.359  10.255  1.00 39.29  ? 15  LEU A C   1 
ATOM   102  O  O   . LEU A 1 16  ? 93.237  -1.650  10.240  1.00 41.26  ? 15  LEU A O   1 
ATOM   103  C  CB  . LEU A 1 16  ? 90.804  -1.606  12.435  1.00 36.59  ? 15  LEU A CB  1 
ATOM   104  C  CG  . LEU A 1 16  ? 90.730  -1.083  13.873  1.00 38.61  ? 15  LEU A CG  1 
ATOM   105  C  CD1 . LEU A 1 16  ? 89.963  -2.039  14.758  1.00 36.02  ? 15  LEU A CD1 1 
ATOM   106  C  CD2 . LEU A 1 16  ? 92.128  -0.830  14.427  1.00 33.86  ? 15  LEU A CD2 1 
ATOM   107  N  N   . VAL A 1 17  ? 91.217  -1.669  9.246   1.00 37.12  ? 16  VAL A N   1 
ATOM   108  C  CA  . VAL A 1 17  ? 91.740  -2.303  8.040   1.00 35.60  ? 16  VAL A CA  1 
ATOM   109  C  C   . VAL A 1 17  ? 92.660  -1.344  7.296   1.00 36.75  ? 16  VAL A C   1 
ATOM   110  O  O   . VAL A 1 17  ? 93.712  -1.741  6.781   1.00 38.51  ? 16  VAL A O   1 
ATOM   111  C  CB  . VAL A 1 17  ? 90.582  -2.787  7.148   1.00 39.72  ? 16  VAL A CB  1 
ATOM   112  C  CG1 . VAL A 1 17  ? 90.995  -2.784  5.682   1.00 38.37  ? 16  VAL A CG1 1 
ATOM   113  C  CG2 . VAL A 1 17  ? 90.122  -4.170  7.582   1.00 37.34  ? 16  VAL A CG2 1 
ATOM   114  N  N   . LYS A 1 18  ? 92.291  -0.062  7.242   1.00 35.03  ? 17  LYS A N   1 
ATOM   115  C  CA  . LYS A 1 18  ? 93.156  0.916   6.594   1.00 39.13  ? 17  LYS A CA  1 
ATOM   116  C  C   . LYS A 1 18  ? 94.488  1.038   7.327   1.00 39.39  ? 17  LYS A C   1 
ATOM   117  O  O   . LYS A 1 18  ? 95.544  1.185   6.700   1.00 44.28  ? 17  LYS A O   1 
ATOM   118  C  CB  . LYS A 1 18  ? 92.449  2.270   6.518   1.00 36.64  ? 17  LYS A CB  1 
ATOM   119  C  CG  . LYS A 1 18  ? 93.376  3.459   6.673   1.00 41.50  ? 17  LYS A CG  1 
ATOM   120  C  CD  . LYS A 1 18  ? 92.724  4.739   6.210   1.00 52.30  ? 17  LYS A CD  1 
ATOM   121  C  CE  . LYS A 1 18  ? 93.627  5.928   6.466   1.00 54.91  ? 17  LYS A CE  1 
ATOM   122  N  NZ  . LYS A 1 18  ? 93.240  7.096   5.628   1.00 61.31  ? 17  LYS A NZ  1 
ATOM   123  N  N   . ILE A 1 19  ? 94.462  0.960   8.656   1.00 37.73  ? 18  ILE A N   1 
ATOM   124  C  CA  . ILE A 1 19  ? 95.699  1.047   9.423   1.00 42.66  ? 18  ILE A CA  1 
ATOM   125  C  C   . ILE A 1 19  ? 96.538  -0.208  9.214   1.00 38.69  ? 18  ILE A C   1 
ATOM   126  O  O   . ILE A 1 19  ? 97.744  -0.132  8.957   1.00 45.56  ? 18  ILE A O   1 
ATOM   127  C  CB  . ILE A 1 19  ? 95.392  1.285   10.912  1.00 45.76  ? 18  ILE A CB  1 
ATOM   128  C  CG1 . ILE A 1 19  ? 95.120  2.769   11.164  1.00 41.25  ? 18  ILE A CG1 1 
ATOM   129  C  CG2 . ILE A 1 19  ? 96.558  0.826   11.780  1.00 48.37  ? 18  ILE A CG2 1 
ATOM   130  C  CD1 . ILE A 1 19  ? 94.469  3.045   12.494  1.00 41.74  ? 18  ILE A CD1 1 
ATOM   131  N  N   . GLY A 1 20  ? 95.908  -1.381  9.308   1.00 37.17  ? 19  GLY A N   1 
ATOM   132  C  CA  . GLY A 1 20  ? 96.635  -2.618  9.072   1.00 44.72  ? 19  GLY A CA  1 
ATOM   133  C  C   . GLY A 1 20  ? 97.223  -2.691  7.678   1.00 40.66  ? 19  GLY A C   1 
ATOM   134  O  O   . GLY A 1 20  ? 98.352  -3.151  7.493   1.00 39.13  ? 19  GLY A O   1 
ATOM   135  N  N   . ALA A 1 21  ? 96.468  -2.231  6.677   1.00 41.36  ? 20  ALA A N   1 
ATOM   136  C  CA  . ALA A 1 21  ? 96.988  -2.208  5.313   1.00 42.11  ? 20  ALA A CA  1 
ATOM   137  C  C   . ALA A 1 21  ? 98.140  -1.223  5.185   1.00 43.46  ? 20  ALA A C   1 
ATOM   138  O  O   . ALA A 1 21  ? 99.137  -1.512  4.516   1.00 43.14  ? 20  ALA A O   1 
ATOM   139  C  CB  . ALA A 1 21  ? 95.874  -1.859  4.327   1.00 35.49  ? 20  ALA A CB  1 
ATOM   140  N  N   . GLY A 1 22  ? 98.024  -0.056  5.825   1.00 43.05  ? 21  GLY A N   1 
ATOM   141  C  CA  . GLY A 1 22  ? 99.103  0.915   5.765   1.00 38.36  ? 21  GLY A CA  1 
ATOM   142  C  C   . GLY A 1 22  ? 100.370 0.417   6.431   1.00 43.68  ? 21  GLY A C   1 
ATOM   143  O  O   . GLY A 1 22  ? 101.472 0.606   5.908   1.00 47.27  ? 21  GLY A O   1 
ATOM   144  N  N   . LEU A 1 23  ? 100.233 -0.225  7.595   1.00 42.89  ? 22  LEU A N   1 
ATOM   145  C  CA  . LEU A 1 23  ? 101.392 -0.796  8.271   1.00 45.31  ? 22  LEU A CA  1 
ATOM   146  C  C   . LEU A 1 23  ? 102.034 -1.890  7.430   1.00 44.21  ? 22  LEU A C   1 
ATOM   147  O  O   . LEU A 1 23  ? 103.261 -2.034  7.416   1.00 46.40  ? 22  LEU A O   1 
ATOM   148  C  CB  . LEU A 1 23  ? 100.984 -1.346  9.636   1.00 42.89  ? 22  LEU A CB  1 
ATOM   149  C  CG  . LEU A 1 23  ? 100.525 -0.284  10.635  1.00 52.26  ? 22  LEU A CG  1 
ATOM   150  C  CD1 . LEU A 1 23  ? 100.088 -0.922  11.951  1.00 39.65  ? 22  LEU A CD1 1 
ATOM   151  C  CD2 . LEU A 1 23  ? 101.636 0.730   10.861  1.00 48.64  ? 22  LEU A CD2 1 
ATOM   152  N  N   . LEU A 1 24  ? 101.218 -2.680  6.731   1.00 42.66  ? 23  LEU A N   1 
ATOM   153  C  CA  . LEU A 1 24  ? 101.762 -3.726  5.875   1.00 43.74  ? 23  LEU A CA  1 
ATOM   154  C  C   . LEU A 1 24  ? 102.513 -3.125  4.696   1.00 45.53  ? 23  LEU A C   1 
ATOM   155  O  O   . LEU A 1 24  ? 103.646 -3.523  4.399   1.00 48.39  ? 23  LEU A O   1 
ATOM   156  C  CB  . LEU A 1 24  ? 100.638 -4.646  5.394   1.00 43.21  ? 23  LEU A CB  1 
ATOM   157  C  CG  . LEU A 1 24  ? 101.046 -5.834  4.518   1.00 50.52  ? 23  LEU A CG  1 
ATOM   158  C  CD1 . LEU A 1 24  ? 102.239 -6.576  5.121   1.00 44.41  ? 23  LEU A CD1 1 
ATOM   159  C  CD2 . LEU A 1 24  ? 99.869  -6.777  4.316   1.00 42.49  ? 23  LEU A CD2 1 
ATOM   160  N  N   . VAL A 1 25  ? 101.902 -2.152  4.021   1.00 39.27  ? 24  VAL A N   1 
ATOM   161  C  CA  . VAL A 1 25  ? 102.540 -1.552  2.856   1.00 42.28  ? 24  VAL A CA  1 
ATOM   162  C  C   . VAL A 1 25  ? 103.783 -0.772  3.266   1.00 49.02  ? 24  VAL A C   1 
ATOM   163  O  O   . VAL A 1 25  ? 104.815 -0.817  2.583   1.00 48.99  ? 24  VAL A O   1 
ATOM   164  C  CB  . VAL A 1 25  ? 101.528 -0.675  2.100   1.00 42.52  ? 24  VAL A CB  1 
ATOM   165  C  CG1 . VAL A 1 25  ? 102.243 0.293   1.174   1.00 50.69  ? 24  VAL A CG1 1 
ATOM   166  C  CG2 . VAL A 1 25  ? 100.571 -1.556  1.313   1.00 40.90  ? 24  VAL A CG2 1 
ATOM   167  N  N   . GLY A 1 26  ? 103.717 -0.070  4.399   1.00 45.61  ? 25  GLY A N   1 
ATOM   168  C  CA  . GLY A 1 26  ? 104.869 0.692   4.852   1.00 46.24  ? 25  GLY A CA  1 
ATOM   169  C  C   . GLY A 1 26  ? 106.060 -0.186  5.183   1.00 50.45  ? 25  GLY A C   1 
ATOM   170  O  O   . GLY A 1 26  ? 107.205 0.163   4.880   1.00 46.55  ? 25  GLY A O   1 
ATOM   171  N  N   . LYS A 1 27  ? 105.811 -1.341  5.801   1.00 47.32  ? 26  LYS A N   1 
ATOM   172  C  CA  . LYS A 1 27  ? 106.916 -2.241  6.103   1.00 47.88  ? 26  LYS A CA  1 
ATOM   173  C  C   . LYS A 1 27  ? 107.436 -2.940  4.852   1.00 48.74  ? 26  LYS A C   1 
ATOM   174  O  O   . LYS A 1 27  ? 108.635 -3.216  4.761   1.00 51.79  ? 26  LYS A O   1 
ATOM   175  C  CB  . LYS A 1 27  ? 106.501 -3.244  7.182   1.00 54.49  ? 26  LYS A CB  1 
ATOM   176  C  CG  . LYS A 1 27  ? 106.725 -2.670  8.591   1.00 70.88  ? 26  LYS A CG  1 
ATOM   177  C  CD  . LYS A 1 27  ? 106.586 -3.687  9.731   1.00 80.82  ? 26  LYS A CD  1 
ATOM   178  C  CE  . LYS A 1 27  ? 105.607 -3.211  10.817  1.00 74.49  ? 26  LYS A CE  1 
ATOM   179  N  NZ  . LYS A 1 27  ? 104.632 -4.244  11.270  1.00 71.79  ? 26  LYS A NZ  1 
ATOM   180  N  N   . LEU A 1 28  ? 106.569 -3.213  3.874   1.00 50.14  ? 27  LEU A N   1 
ATOM   181  C  CA  . LEU A 1 28  ? 107.051 -3.745  2.603   1.00 48.60  ? 27  LEU A CA  1 
ATOM   182  C  C   . LEU A 1 28  ? 107.954 -2.740  1.906   1.00 47.84  ? 27  LEU A C   1 
ATOM   183  O  O   . LEU A 1 28  ? 108.981 -3.111  1.326   1.00 51.76  ? 27  LEU A O   1 
ATOM   184  C  CB  . LEU A 1 28  ? 105.875 -4.115  1.697   1.00 48.66  ? 27  LEU A CB  1 
ATOM   185  C  CG  . LEU A 1 28  ? 105.068 -5.373  2.029   1.00 54.14  ? 27  LEU A CG  1 
ATOM   186  C  CD1 . LEU A 1 28  ? 103.737 -5.374  1.287   1.00 45.48  ? 27  LEU A CD1 1 
ATOM   187  C  CD2 . LEU A 1 28  ? 105.864 -6.625  1.698   1.00 55.59  ? 27  LEU A CD2 1 
ATOM   188  N  N   . LEU A 1 29  ? 107.591 -1.458  1.963   1.00 48.44  ? 28  LEU A N   1 
ATOM   189  C  CA  . LEU A 1 29  ? 108.405 -0.428  1.332   1.00 47.60  ? 28  LEU A CA  1 
ATOM   190  C  C   . LEU A 1 29  ? 109.733 -0.255  2.055   1.00 55.04  ? 28  LEU A C   1 
ATOM   191  O  O   . LEU A 1 29  ? 110.773 -0.049  1.416   1.00 56.44  ? 28  LEU A O   1 
ATOM   192  C  CB  . LEU A 1 29  ? 107.639 0.891   1.295   1.00 48.83  ? 28  LEU A CB  1 
ATOM   193  C  CG  . LEU A 1 29  ? 108.251 1.992   0.433   1.00 49.76  ? 28  LEU A CG  1 
ATOM   194  C  CD1 . LEU A 1 29  ? 107.687 1.937   -0.976  1.00 44.19  ? 28  LEU A CD1 1 
ATOM   195  C  CD2 . LEU A 1 29  ? 108.003 3.348   1.065   1.00 50.27  ? 28  LEU A CD2 1 
ATOM   196  N  N   . ALA A 1 30  ? 109.720 -0.331  3.388   1.00 50.35  ? 29  ALA A N   1 
ATOM   197  C  CA  . ALA A 1 30  ? 110.958 -0.173  4.145   1.00 52.70  ? 29  ALA A CA  1 
ATOM   198  C  C   . ALA A 1 30  ? 111.929 -1.305  3.844   1.00 48.70  ? 29  ALA A C   1 
ATOM   199  O  O   . ALA A 1 30  ? 113.104 -1.065  3.545   1.00 52.73  ? 29  ALA A O   1 
ATOM   200  C  CB  . ALA A 1 30  ? 110.657 -0.103  5.640   1.00 50.27  ? 29  ALA A CB  1 
ATOM   201  N  N   . VAL A 1 31  ? 111.449 -2.551  3.906   1.00 45.20  ? 30  VAL A N   1 
ATOM   202  C  CA  . VAL A 1 31  ? 112.310 -3.701  3.651   1.00 52.75  ? 30  VAL A CA  1 
ATOM   203  C  C   . VAL A 1 31  ? 112.812 -3.704  2.210   1.00 54.95  ? 30  VAL A C   1 
ATOM   204  O  O   . VAL A 1 31  ? 113.939 -4.136  1.935   1.00 57.51  ? 30  VAL A O   1 
ATOM   205  C  CB  . VAL A 1 31  ? 111.558 -5.002  4.007   1.00 48.89  ? 30  VAL A CB  1 
ATOM   206  C  CG1 . VAL A 1 31  ? 112.341 -6.228  3.565   1.00 39.87  ? 30  VAL A CG1 1 
ATOM   207  C  CG2 . VAL A 1 31  ? 111.287 -5.058  5.506   1.00 43.61  ? 30  VAL A CG2 1 
ATOM   208  N  N   . SER A 1 32  ? 112.013 -3.194  1.274   1.00 51.57  ? 31  SER A N   1 
ATOM   209  C  CA  . SER A 1 32  ? 112.395 -3.269  -0.131  1.00 45.30  ? 31  SER A CA  1 
ATOM   210  C  C   . SER A 1 32  ? 113.398 -2.188  -0.520  1.00 51.53  ? 31  SER A C   1 
ATOM   211  O  O   . SER A 1 32  ? 114.295 -2.442  -1.331  1.00 52.43  ? 31  SER A O   1 
ATOM   212  C  CB  . SER A 1 32  ? 111.155 -3.176  -1.017  1.00 49.81  ? 31  SER A CB  1 
ATOM   213  O  OG  . SER A 1 32  ? 110.685 -4.466  -1.362  1.00 58.31  ? 31  SER A OG  1 
ATOM   214  N  N   . PHE A 1 33  ? 113.275 -0.981  0.034   1.00 50.95  ? 32  PHE A N   1 
ATOM   215  C  CA  . PHE A 1 33  ? 114.044 0.147   -0.472  1.00 48.68  ? 32  PHE A CA  1 
ATOM   216  C  C   . PHE A 1 33  ? 114.846 0.896   0.584   1.00 54.95  ? 32  PHE A C   1 
ATOM   217  O  O   . PHE A 1 33  ? 115.567 1.837   0.229   1.00 59.55  ? 32  PHE A O   1 
ATOM   218  C  CB  . PHE A 1 33  ? 113.113 1.125   -1.198  1.00 41.22  ? 32  PHE A CB  1 
ATOM   219  C  CG  . PHE A 1 33  ? 112.234 0.464   -2.222  1.00 50.43  ? 32  PHE A CG  1 
ATOM   220  C  CD1 . PHE A 1 33  ? 112.776 -0.076  -3.376  1.00 50.81  ? 32  PHE A CD1 1 
ATOM   221  C  CD2 . PHE A 1 33  ? 110.865 0.367   -2.022  1.00 53.77  ? 32  PHE A CD2 1 
ATOM   222  C  CE1 . PHE A 1 33  ? 111.970 -0.687  -4.318  1.00 50.45  ? 32  PHE A CE1 1 
ATOM   223  C  CE2 . PHE A 1 33  ? 110.056 -0.246  -2.958  1.00 46.23  ? 32  PHE A CE2 1 
ATOM   224  C  CZ  . PHE A 1 33  ? 110.609 -0.774  -4.107  1.00 48.70  ? 32  PHE A CZ  1 
ATOM   225  N  N   . GLY A 1 34  ? 114.744 0.517   1.858   1.00 55.68  ? 33  GLY A N   1 
ATOM   226  C  CA  . GLY A 1 34  ? 115.586 1.063   2.899   1.00 52.79  ? 33  GLY A CA  1 
ATOM   227  C  C   . GLY A 1 34  ? 115.431 2.556   3.108   1.00 54.75  ? 33  GLY A C   1 
ATOM   228  O  O   . GLY A 1 34  ? 114.492 3.186   2.610   1.00 58.34  ? 33  GLY A O   1 
ATOM   229  N  N   . PRO A 1 35  ? 116.366 3.155   3.851   1.00 59.82  ? 34  PRO A N   1 
ATOM   230  C  CA  . PRO A 1 35  ? 116.252 4.593   4.145   1.00 59.23  ? 34  PRO A CA  1 
ATOM   231  C  C   . PRO A 1 35  ? 116.366 5.473   2.914   1.00 57.89  ? 34  PRO A C   1 
ATOM   232  O  O   . PRO A 1 35  ? 115.784 6.566   2.891   1.00 57.97  ? 34  PRO A O   1 
ATOM   233  C  CB  . PRO A 1 35  ? 117.407 4.844   5.127   1.00 59.58  ? 34  PRO A CB  1 
ATOM   234  C  CG  . PRO A 1 35  ? 117.788 3.487   5.647   1.00 62.99  ? 34  PRO A CG  1 
ATOM   235  C  CD  . PRO A 1 35  ? 117.531 2.546   4.511   1.00 56.92  ? 34  PRO A CD  1 
ATOM   236  N  N   . ALA A 1 36  ? 117.103 5.034   1.890   1.00 58.06  ? 35  ALA A N   1 
ATOM   237  C  CA  . ALA A 1 36  ? 117.197 5.816   0.661   1.00 58.22  ? 35  ALA A CA  1 
ATOM   238  C  C   . ALA A 1 36  ? 115.848 5.895   -0.041  1.00 57.17  ? 35  ALA A C   1 
ATOM   239  O  O   . ALA A 1 36  ? 115.452 6.961   -0.529  1.00 57.79  ? 35  ALA A O   1 
ATOM   240  C  CB  . ALA A 1 36  ? 118.250 5.215   -0.266  1.00 53.70  ? 35  ALA A CB  1 
ATOM   241  N  N   . GLY A 1 37  ? 115.127 4.775   -0.100  1.00 52.14  ? 36  GLY A N   1 
ATOM   242  C  CA  . GLY A 1 37  ? 113.797 4.796   -0.686  1.00 53.11  ? 36  GLY A CA  1 
ATOM   243  C  C   . GLY A 1 37  ? 112.803 5.588   0.143   1.00 50.69  ? 36  GLY A C   1 
ATOM   244  O  O   . GLY A 1 37  ? 111.936 6.274   -0.402  1.00 53.25  ? 36  GLY A O   1 
ATOM   245  N  N   . LEU A 1 38  ? 112.914 5.506   1.472   1.00 51.69  ? 37  LEU A N   1 
ATOM   246  C  CA  . LEU A 1 38  ? 112.007 6.261   2.331   1.00 49.96  ? 37  LEU A CA  1 
ATOM   247  C  C   . LEU A 1 38  ? 112.258 7.757   2.216   1.00 53.59  ? 37  LEU A C   1 
ATOM   248  O  O   . LEU A 1 38  ? 111.308 8.545   2.126   1.00 51.17  ? 37  LEU A O   1 
ATOM   249  C  CB  . LEU A 1 38  ? 112.149 5.807   3.782   1.00 51.11  ? 37  LEU A CB  1 
ATOM   250  C  CG  . LEU A 1 38  ? 111.533 4.455   4.147   1.00 52.94  ? 37  LEU A CG  1 
ATOM   251  C  CD1 . LEU A 1 38  ? 111.888 4.075   5.575   1.00 50.76  ? 37  LEU A CD1 1 
ATOM   252  C  CD2 . LEU A 1 38  ? 110.028 4.486   3.964   1.00 43.95  ? 37  LEU A CD2 1 
ATOM   253  N  N   . GLY A 1 39  ? 113.529 8.167   2.211   1.00 49.86  ? 38  GLY A N   1 
ATOM   254  C  CA  . GLY A 1 39  ? 113.836 9.584   2.105   1.00 45.83  ? 38  GLY A CA  1 
ATOM   255  C  C   . GLY A 1 39  ? 113.404 10.178  0.779   1.00 50.53  ? 38  GLY A C   1 
ATOM   256  O  O   . GLY A 1 39  ? 112.986 11.336  0.714   1.00 58.29  ? 38  GLY A O   1 
ATOM   257  N  N   . LEU A 1 40  ? 113.499 9.396   -0.297  1.00 53.50  ? 39  LEU A N   1 
ATOM   258  C  CA  . LEU A 1 40  ? 113.043 9.856   -1.602  1.00 53.10  ? 39  LEU A CA  1 
ATOM   259  C  C   . LEU A 1 40  ? 111.525 9.822   -1.737  1.00 48.11  ? 39  LEU A C   1 
ATOM   260  O  O   . LEU A 1 40  ? 110.977 10.554  -2.565  1.00 52.35  ? 39  LEU A O   1 
ATOM   261  C  CB  . LEU A 1 40  ? 113.676 9.010   -2.711  1.00 47.35  ? 39  LEU A CB  1 
ATOM   262  C  CG  . LEU A 1 40  ? 114.965 9.518   -3.354  1.00 49.74  ? 39  LEU A CG  1 
ATOM   263  C  CD1 . LEU A 1 40  ? 115.312 8.667   -4.558  1.00 49.62  ? 39  LEU A CD1 1 
ATOM   264  C  CD2 . LEU A 1 40  ? 114.853 10.980  -3.750  1.00 51.23  ? 39  LEU A CD2 1 
ATOM   265  N  N   . ALA A 1 41  ? 110.837 9.001   -0.947  1.00 47.74  ? 40  ALA A N   1 
ATOM   266  C  CA  . ALA A 1 41  ? 109.385 8.904   -1.016  1.00 44.89  ? 40  ALA A CA  1 
ATOM   267  C  C   . ALA A 1 41  ? 108.673 9.843   -0.055  1.00 46.02  ? 40  ALA A C   1 
ATOM   268  O  O   . ALA A 1 41  ? 107.442 9.882   -0.061  1.00 55.57  ? 40  ALA A O   1 
ATOM   269  C  CB  . ALA A 1 41  ? 108.934 7.467   -0.735  1.00 41.15  ? 40  ALA A CB  1 
ATOM   270  N  N   . ALA A 1 42  ? 109.406 10.603  0.759   1.00 46.33  ? 41  ALA A N   1 
ATOM   271  C  CA  . ALA A 1 42  ? 108.776 11.382  1.822   1.00 46.51  ? 41  ALA A CA  1 
ATOM   272  C  C   . ALA A 1 42  ? 107.844 12.447  1.255   1.00 48.58  ? 41  ALA A C   1 
ATOM   273  O  O   . ALA A 1 42  ? 106.656 12.499  1.598   1.00 49.91  ? 41  ALA A O   1 
ATOM   274  C  CB  . ALA A 1 42  ? 109.847 12.014  2.712   1.00 45.28  ? 41  ALA A CB  1 
ATOM   275  N  N   . ASN A 1 43  ? 108.368 13.310  0.380   1.00 45.33  ? 42  ASN A N   1 
ATOM   276  C  CA  . ASN A 1 43  ? 107.546 14.373  -0.190  1.00 42.88  ? 42  ASN A CA  1 
ATOM   277  C  C   . ASN A 1 43  ? 106.416 13.806  -1.041  1.00 48.99  ? 42  ASN A C   1 
ATOM   278  O  O   . ASN A 1 43  ? 105.269 14.265  -0.949  1.00 42.59  ? 42  ASN A O   1 
ATOM   279  C  CB  . ASN A 1 43  ? 108.415 15.316  -1.018  1.00 45.18  ? 42  ASN A CB  1 
ATOM   280  C  CG  . ASN A 1 43  ? 109.365 16.127  -0.165  1.00 51.03  ? 42  ASN A CG  1 
ATOM   281  O  OD1 . ASN A 1 43  ? 109.112 16.366  1.016   1.00 56.16  ? 42  ASN A OD1 1 
ATOM   282  N  ND2 . ASN A 1 43  ? 110.478 16.545  -0.757  1.00 50.63  ? 42  ASN A ND2 1 
ATOM   283  N  N   . PHE A 1 44  ? 106.726 12.809  -1.877  1.00 44.94  ? 43  PHE A N   1 
ATOM   284  C  CA  . PHE A 1 44  ? 105.706 12.193  -2.719  1.00 44.93  ? 43  PHE A CA  1 
ATOM   285  C  C   . PHE A 1 44  ? 104.564 11.632  -1.883  1.00 42.07  ? 43  PHE A C   1 
ATOM   286  O  O   . PHE A 1 44  ? 103.394 11.745  -2.265  1.00 45.39  ? 43  PHE A O   1 
ATOM   287  C  CB  . PHE A 1 44  ? 106.328 11.091  -3.576  1.00 40.80  ? 43  PHE A CB  1 
ATOM   288  C  CG  . PHE A 1 44  ? 105.353 10.429  -4.517  1.00 43.33  ? 43  PHE A CG  1 
ATOM   289  C  CD1 . PHE A 1 44  ? 105.076 10.989  -5.753  1.00 46.23  ? 43  PHE A CD1 1 
ATOM   290  C  CD2 . PHE A 1 44  ? 104.721 9.244   -4.170  1.00 38.35  ? 43  PHE A CD2 1 
ATOM   291  C  CE1 . PHE A 1 44  ? 104.190 10.383  -6.625  1.00 43.74  ? 43  PHE A CE1 1 
ATOM   292  C  CE2 . PHE A 1 44  ? 103.829 8.638   -5.034  1.00 38.47  ? 43  PHE A CE2 1 
ATOM   293  C  CZ  . PHE A 1 44  ? 103.562 9.208   -6.260  1.00 42.59  ? 43  PHE A CZ  1 
ATOM   294  N  N   . ARG A 1 45  ? 104.882 11.021  -0.739  1.00 43.36  ? 44  ARG A N   1 
ATOM   295  C  CA  . ARG A 1 45  ? 103.834 10.468  0.111   1.00 46.93  ? 44  ARG A CA  1 
ATOM   296  C  C   . ARG A 1 45  ? 103.007 11.572  0.759   1.00 47.05  ? 44  ARG A C   1 
ATOM   297  O  O   . ARG A 1 45  ? 101.781 11.450  0.869   1.00 51.47  ? 44  ARG A O   1 
ATOM   298  C  CB  . ARG A 1 45  ? 104.441 9.550   1.170   1.00 43.51  ? 44  ARG A CB  1 
ATOM   299  C  CG  . ARG A 1 45  ? 104.963 8.241   0.603   1.00 51.97  ? 44  ARG A CG  1 
ATOM   300  C  CD  . ARG A 1 45  ? 105.863 7.518   1.589   1.00 47.69  ? 44  ARG A CD  1 
ATOM   301  N  NE  . ARG A 1 45  ? 105.081 6.785   2.577   1.00 52.02  ? 44  ARG A NE  1 
ATOM   302  C  CZ  . ARG A 1 45  ? 105.594 6.089   3.582   1.00 54.22  ? 44  ARG A CZ  1 
ATOM   303  N  NH1 . ARG A 1 45  ? 106.902 6.008   3.772   1.00 46.00  ? 44  ARG A NH1 1 
ATOM   304  N  NH2 . ARG A 1 45  ? 104.774 5.457   4.417   1.00 58.51  ? 44  ARG A NH2 1 
ATOM   305  N  N   . GLN A 1 46  ? 103.651 12.657  1.189   1.00 44.29  ? 45  GLN A N   1 
ATOM   306  C  CA  . GLN A 1 46  ? 102.892 13.773  1.741   1.00 42.19  ? 45  GLN A CA  1 
ATOM   307  C  C   . GLN A 1 46  ? 102.009 14.425  0.683   1.00 43.85  ? 45  GLN A C   1 
ATOM   308  O  O   . GLN A 1 46  ? 100.902 14.876  0.997   1.00 47.13  ? 45  GLN A O   1 
ATOM   309  C  CB  . GLN A 1 46  ? 103.847 14.789  2.371   1.00 40.12  ? 45  GLN A CB  1 
ATOM   310  C  CG  . GLN A 1 46  ? 103.215 15.850  3.284   1.00 53.31  ? 45  GLN A CG  1 
ATOM   311  C  CD  . GLN A 1 46  ? 102.122 15.334  4.229   1.00 66.41  ? 45  GLN A CD  1 
ATOM   312  O  OE1 . GLN A 1 46  ? 101.177 16.061  4.534   1.00 66.69  ? 45  GLN A OE1 1 
ATOM   313  N  NE2 . GLN A 1 46  ? 102.280 14.108  4.740   1.00 70.42  ? 45  GLN A NE2 1 
ATOM   314  N  N   . LEU A 1 47  ? 102.462 14.459  -0.572  1.00 42.90  ? 46  LEU A N   1 
ATOM   315  C  CA  . LEU A 1 47  ? 101.611 14.954  -1.651  1.00 41.02  ? 46  LEU A CA  1 
ATOM   316  C  C   . LEU A 1 47  ? 100.376 14.078  -1.827  1.00 43.18  ? 46  LEU A C   1 
ATOM   317  O  O   . LEU A 1 47  ? 99.274  14.593  -2.056  1.00 43.16  ? 46  LEU A O   1 
ATOM   318  C  CB  . LEU A 1 47  ? 102.398 15.030  -2.959  1.00 44.23  ? 46  LEU A CB  1 
ATOM   319  C  CG  . LEU A 1 47  ? 101.556 15.164  -4.234  1.00 46.36  ? 46  LEU A CG  1 
ATOM   320  C  CD1 . LEU A 1 47  ? 100.826 16.494  -4.255  1.00 44.22  ? 46  LEU A CD1 1 
ATOM   321  C  CD2 . LEU A 1 47  ? 102.424 15.016  -5.480  1.00 39.56  ? 46  LEU A CD2 1 
ATOM   322  N  N   . ILE A 1 48  ? 100.534 12.756  -1.718  1.00 41.53  ? 47  ILE A N   1 
ATOM   323  C  CA  . ILE A 1 48  ? 99.384  11.863  -1.837  1.00 41.76  ? 47  ILE A CA  1 
ATOM   324  C  C   . ILE A 1 48  ? 98.376  12.146  -0.730  1.00 45.11  ? 47  ILE A C   1 
ATOM   325  O  O   . ILE A 1 48  ? 97.159  12.131  -0.956  1.00 42.93  ? 47  ILE A O   1 
ATOM   326  C  CB  . ILE A 1 48  ? 99.836  10.391  -1.822  1.00 38.34  ? 47  ILE A CB  1 
ATOM   327  C  CG1 . ILE A 1 48  ? 100.760 10.095  -3.000  1.00 43.68  ? 47  ILE A CG1 1 
ATOM   328  C  CG2 . ILE A 1 48  ? 98.628  9.471   -1.850  1.00 44.11  ? 47  ILE A CG2 1 
ATOM   329  C  CD1 . ILE A 1 48  ? 100.258 10.638  -4.319  1.00 47.25  ? 47  ILE A CD1 1 
ATOM   330  N  N   . THR A 1 49  ? 98.863  12.407  0.484   1.00 46.17  ? 48  THR A N   1 
ATOM   331  C  CA  . THR A 1 49  ? 97.966  12.782  1.571   1.00 44.46  ? 48  THR A CA  1 
ATOM   332  C  C   . THR A 1 49  ? 97.234  14.079  1.244   1.00 44.51  ? 48  THR A C   1 
ATOM   333  O  O   . THR A 1 49  ? 96.008  14.165  1.380   1.00 41.17  ? 48  THR A O   1 
ATOM   334  C  CB  . THR A 1 49  ? 98.756  12.914  2.876   1.00 50.64  ? 48  THR A CB  1 
ATOM   335  O  OG1 . THR A 1 49  ? 99.257  11.628  3.263   1.00 51.93  ? 48  THR A OG1 1 
ATOM   336  C  CG2 . THR A 1 49  ? 97.876  13.463  3.988   1.00 46.13  ? 48  THR A CG2 1 
ATOM   337  N  N   . VAL A 1 50  ? 97.970  15.093  0.783   1.00 39.42  ? 49  VAL A N   1 
ATOM   338  C  CA  . VAL A 1 50  ? 97.355  16.385  0.489   1.00 44.96  ? 49  VAL A CA  1 
ATOM   339  C  C   . VAL A 1 50  ? 96.297  16.242  -0.599  1.00 44.17  ? 49  VAL A C   1 
ATOM   340  O  O   . VAL A 1 50  ? 95.217  16.841  -0.518  1.00 45.98  ? 49  VAL A O   1 
ATOM   341  C  CB  . VAL A 1 50  ? 98.433  17.415  0.103   1.00 42.70  ? 49  VAL A CB  1 
ATOM   342  C  CG1 . VAL A 1 50  ? 97.794  18.645  -0.506  1.00 43.86  ? 49  VAL A CG1 1 
ATOM   343  C  CG2 . VAL A 1 50  ? 99.264  17.791  1.316   1.00 42.13  ? 49  VAL A CG2 1 
ATOM   344  N  N   . LEU A 1 51  ? 96.577  15.428  -1.621  1.00 39.82  ? 50  LEU A N   1 
ATOM   345  C  CA  . LEU A 1 51  ? 95.638  15.250  -2.723  1.00 34.37  ? 50  LEU A CA  1 
ATOM   346  C  C   . LEU A 1 51  ? 94.321  14.626  -2.278  1.00 43.14  ? 50  LEU A C   1 
ATOM   347  O  O   . LEU A 1 51  ? 93.309  14.789  -2.968  1.00 35.15  ? 50  LEU A O   1 
ATOM   348  C  CB  . LEU A 1 51  ? 96.273  14.390  -3.815  1.00 40.09  ? 50  LEU A CB  1 
ATOM   349  C  CG  . LEU A 1 51  ? 97.243  15.120  -4.742  1.00 42.41  ? 50  LEU A CG  1 
ATOM   350  C  CD1 . LEU A 1 51  ? 97.961  14.125  -5.634  1.00 50.15  ? 50  LEU A CD1 1 
ATOM   351  C  CD2 . LEU A 1 51  ? 96.519  16.168  -5.573  1.00 34.82  ? 50  LEU A CD2 1 
ATOM   352  N  N   . GLY A 1 52  ? 94.309  13.912  -1.148  1.00 43.28  ? 51  GLY A N   1 
ATOM   353  C  CA  . GLY A 1 52  ? 93.065  13.349  -0.649  1.00 40.18  ? 51  GLY A CA  1 
ATOM   354  C  C   . GLY A 1 52  ? 92.010  14.400  -0.366  1.00 43.23  ? 51  GLY A C   1 
ATOM   355  O  O   . GLY A 1 52  ? 90.810  14.114  -0.410  1.00 39.20  ? 51  GLY A O   1 
ATOM   356  N  N   . VAL A 1 53  ? 92.436  15.627  -0.082  1.00 40.20  ? 52  VAL A N   1 
ATOM   357  C  CA  . VAL A 1 53  ? 91.516  16.740  0.056   1.00 41.66  ? 52  VAL A CA  1 
ATOM   358  C  C   . VAL A 1 53  ? 91.607  17.712  -1.116  1.00 40.34  ? 52  VAL A C   1 
ATOM   359  O  O   . VAL A 1 53  ? 90.575  18.238  -1.551  1.00 41.59  ? 52  VAL A O   1 
ATOM   360  C  CB  . VAL A 1 53  ? 91.759  17.469  1.391   1.00 42.29  ? 52  VAL A CB  1 
ATOM   361  C  CG1 . VAL A 1 53  ? 90.722  18.558  1.601   1.00 42.27  ? 52  VAL A CG1 1 
ATOM   362  C  CG2 . VAL A 1 53  ? 91.744  16.474  2.536   1.00 47.16  ? 52  VAL A CG2 1 
ATOM   363  N  N   . LEU A 1 54  ? 92.802  17.927  -1.668  1.00 37.76  ? 53  LEU A N   1 
ATOM   364  C  CA  . LEU A 1 54  ? 92.987  18.950  -2.690  1.00 42.14  ? 53  LEU A CA  1 
ATOM   365  C  C   . LEU A 1 54  ? 92.377  18.551  -4.029  1.00 39.34  ? 53  LEU A C   1 
ATOM   366  O  O   . LEU A 1 54  ? 91.887  19.418  -4.760  1.00 42.46  ? 53  LEU A O   1 
ATOM   367  C  CB  . LEU A 1 54  ? 94.480  19.252  -2.852  1.00 38.60  ? 53  LEU A CB  1 
ATOM   368  C  CG  . LEU A 1 54  ? 94.887  20.118  -4.042  1.00 44.54  ? 53  LEU A CG  1 
ATOM   369  C  CD1 . LEU A 1 54  ? 94.318  21.520  -3.881  1.00 51.24  ? 53  LEU A CD1 1 
ATOM   370  C  CD2 . LEU A 1 54  ? 96.404  20.161  -4.196  1.00 39.89  ? 53  LEU A CD2 1 
ATOM   371  N  N   . ALA A 1 55  ? 92.390  17.257  -4.369  1.00 34.44  ? 54  ALA A N   1 
ATOM   372  C  CA  . ALA A 1 55  ? 91.975  16.841  -5.708  1.00 40.72  ? 54  ALA A CA  1 
ATOM   373  C  C   . ALA A 1 55  ? 90.520  17.196  -5.995  1.00 44.24  ? 54  ALA A C   1 
ATOM   374  O  O   . ALA A 1 55  ? 90.167  17.481  -7.146  1.00 44.44  ? 54  ALA A O   1 
ATOM   375  C  CB  . ALA A 1 55  ? 92.195  15.338  -5.893  1.00 36.25  ? 54  ALA A CB  1 
ATOM   376  N  N   . GLY A 1 56  ? 89.667  17.193  -4.973  1.00 36.08  ? 55  GLY A N   1 
ATOM   377  C  CA  . GLY A 1 56  ? 88.282  17.573  -5.162  1.00 37.04  ? 55  GLY A CA  1 
ATOM   378  C  C   . GLY A 1 56  ? 87.966  18.957  -4.633  1.00 41.63  ? 55  GLY A C   1 
ATOM   379  O  O   . GLY A 1 56  ? 86.806  19.252  -4.329  1.00 40.33  ? 55  GLY A O   1 
ATOM   380  N  N   . ALA A 1 57  ? 88.987  19.808  -4.508  1.00 37.36  ? 56  ALA A N   1 
ATOM   381  C  CA  . ALA A 1 57  ? 88.840  21.196  -4.068  1.00 37.63  ? 56  ALA A CA  1 
ATOM   382  C  C   . ALA A 1 57  ? 88.233  21.314  -2.672  1.00 40.55  ? 56  ALA A C   1 
ATOM   383  O  O   . ALA A 1 57  ? 87.640  22.345  -2.339  1.00 39.74  ? 56  ALA A O   1 
ATOM   384  C  CB  . ALA A 1 57  ? 88.021  22.017  -5.073  1.00 38.07  ? 56  ALA A CB  1 
ATOM   385  N  N   . GLY A 1 58  ? 88.371  20.275  -1.847  1.00 43.96  ? 57  GLY A N   1 
ATOM   386  C  CA  . GLY A 1 58  ? 87.978  20.340  -0.450  1.00 40.74  ? 57  GLY A CA  1 
ATOM   387  C  C   . GLY A 1 58  ? 86.506  20.569  -0.177  1.00 38.18  ? 57  GLY A C   1 
ATOM   388  O  O   . GLY A 1 58  ? 86.154  21.036  0.910   1.00 38.81  ? 57  GLY A O   1 
ATOM   389  N  N   . ILE A 1 59  ? 85.624  20.244  -1.128  1.00 31.59  ? 58  ILE A N   1 
ATOM   390  C  CA  . ILE A 1 59  ? 84.195  20.453  -0.927  1.00 34.04  ? 58  ILE A CA  1 
ATOM   391  C  C   . ILE A 1 59  ? 83.528  19.292  -0.208  1.00 29.71  ? 58  ILE A C   1 
ATOM   392  O  O   . ILE A 1 59  ? 82.321  19.359  0.058   1.00 36.70  ? 58  ILE A O   1 
ATOM   393  C  CB  . ILE A 1 59  ? 83.461  20.686  -2.266  1.00 34.62  ? 58  ILE A CB  1 
ATOM   394  C  CG1 . ILE A 1 59  ? 83.456  19.409  -3.104  1.00 28.07  ? 58  ILE A CG1 1 
ATOM   395  C  CG2 . ILE A 1 59  ? 84.086  21.830  -3.042  1.00 34.82  ? 58  ILE A CG2 1 
ATOM   396  C  CD1 . ILE A 1 59  ? 82.557  19.503  -4.313  1.00 36.52  ? 58  ILE A CD1 1 
ATOM   397  N  N   . PHE A 1 60  ? 84.280  18.246  0.145   1.00 30.84  ? 59  PHE A N   1 
ATOM   398  C  CA  . PHE A 1 60  ? 83.662  16.981  0.534   1.00 33.67  ? 59  PHE A CA  1 
ATOM   399  C  C   . PHE A 1 60  ? 82.743  17.140  1.740   1.00 33.49  ? 59  PHE A C   1 
ATOM   400  O  O   . PHE A 1 60  ? 81.610  16.645  1.726   1.00 37.42  ? 59  PHE A O   1 
ATOM   401  C  CB  . PHE A 1 60  ? 84.748  15.935  0.783   1.00 35.79  ? 59  PHE A CB  1 
ATOM   402  C  CG  . PHE A 1 60  ? 85.606  15.671  -0.428  1.00 35.49  ? 59  PHE A CG  1 
ATOM   403  C  CD1 . PHE A 1 60  ? 85.043  15.176  -1.592  1.00 34.61  ? 59  PHE A CD1 1 
ATOM   404  C  CD2 . PHE A 1 60  ? 86.964  15.943  -0.415  1.00 37.57  ? 59  PHE A CD2 1 
ATOM   405  C  CE1 . PHE A 1 60  ? 85.821  14.946  -2.719  1.00 34.45  ? 59  PHE A CE1 1 
ATOM   406  C  CE2 . PHE A 1 60  ? 87.744  15.711  -1.537  1.00 38.40  ? 59  PHE A CE2 1 
ATOM   407  C  CZ  . PHE A 1 60  ? 87.169  15.215  -2.689  1.00 30.75  ? 59  PHE A CZ  1 
ATOM   408  N  N   . ASN A 1 61  ? 83.189  17.857  2.774   1.00 32.07  ? 60  ASN A N   1 
ATOM   409  C  CA  . ASN A 1 61  ? 82.318  18.091  3.925   1.00 34.72  ? 60  ASN A CA  1 
ATOM   410  C  C   . ASN A 1 61  ? 81.054  18.841  3.530   1.00 34.10  ? 60  ASN A C   1 
ATOM   411  O  O   . ASN A 1 61  ? 79.981  18.583  4.090   1.00 28.52  ? 60  ASN A O   1 
ATOM   412  C  CB  . ASN A 1 61  ? 83.063  18.860  5.008   1.00 32.69  ? 60  ASN A CB  1 
ATOM   413  C  CG  . ASN A 1 61  ? 83.952  17.968  5.830   1.00 38.61  ? 60  ASN A CG  1 
ATOM   414  O  OD1 . ASN A 1 61  ? 84.932  18.423  6.419   1.00 41.23  ? 60  ASN A OD1 1 
ATOM   415  N  ND2 . ASN A 1 61  ? 83.623  16.682  5.868   1.00 34.71  ? 60  ASN A ND2 1 
ATOM   416  N  N   . GLY A 1 62  ? 81.157  19.775  2.580   1.00 34.21  ? 61  GLY A N   1 
ATOM   417  C  CA  . GLY A 1 62  ? 79.968  20.457  2.097   1.00 26.88  ? 61  GLY A CA  1 
ATOM   418  C  C   . GLY A 1 62  ? 79.038  19.530  1.339   1.00 27.08  ? 61  GLY A C   1 
ATOM   419  O  O   . GLY A 1 62  ? 77.817  19.631  1.460   1.00 31.12  ? 61  GLY A O   1 
ATOM   420  N  N   . VAL A 1 63  ? 79.600  18.611  0.549   1.00 34.60  ? 62  VAL A N   1 
ATOM   421  C  CA  . VAL A 1 63  ? 78.777  17.600  -0.113  1.00 33.16  ? 62  VAL A CA  1 
ATOM   422  C  C   . VAL A 1 63  ? 77.957  16.841  0.919   1.00 32.47  ? 62  VAL A C   1 
ATOM   423  O  O   . VAL A 1 63  ? 76.731  16.724  0.805   1.00 29.12  ? 62  VAL A O   1 
ATOM   424  C  CB  . VAL A 1 63  ? 79.659  16.646  -0.938  1.00 33.95  ? 62  VAL A CB  1 
ATOM   425  C  CG1 . VAL A 1 63  ? 78.823  15.515  -1.503  1.00 28.57  ? 62  VAL A CG1 1 
ATOM   426  C  CG2 . VAL A 1 63  ? 80.371  17.402  -2.044  1.00 30.10  ? 62  VAL A CG2 1 
ATOM   427  N  N   . THR A 1 64  ? 78.627  16.340  1.959   1.00 31.49  ? 63  THR A N   1 
ATOM   428  C  CA  . THR A 1 64  ? 77.937  15.628  3.027   1.00 33.58  ? 63  THR A CA  1 
ATOM   429  C  C   . THR A 1 64  ? 76.901  16.515  3.707   1.00 32.51  ? 63  THR A C   1 
ATOM   430  O  O   . THR A 1 64  ? 75.769  16.079  3.961   1.00 33.20  ? 63  THR A O   1 
ATOM   431  C  CB  . THR A 1 64  ? 78.957  15.118  4.044   1.00 31.41  ? 63  THR A CB  1 
ATOM   432  O  OG1 . THR A 1 64  ? 79.823  14.173  3.407   1.00 29.22  ? 63  THR A OG1 1 
ATOM   433  C  CG2 . THR A 1 64  ? 78.256  14.445  5.221   1.00 29.78  ? 63  THR A CG2 1 
ATOM   434  N  N   . LYS A 1 65  ? 77.262  17.770  3.986   1.00 32.06  ? 64  LYS A N   1 
ATOM   435  C  CA  . LYS A 1 65  ? 76.358  18.663  4.702   1.00 29.29  ? 64  LYS A CA  1 
ATOM   436  C  C   . LYS A 1 65  ? 75.069  18.887  3.919   1.00 34.14  ? 64  LYS A C   1 
ATOM   437  O  O   . LYS A 1 65  ? 73.967  18.766  4.468   1.00 31.52  ? 64  LYS A O   1 
ATOM   438  C  CB  . LYS A 1 65  ? 77.053  19.996  4.989   1.00 30.21  ? 64  LYS A CB  1 
ATOM   439  C  CG  . LYS A 1 65  ? 76.213  20.977  5.819   1.00 34.79  ? 64  LYS A CG  1 
ATOM   440  C  CD  . LYS A 1 65  ? 75.584  22.062  4.943   1.00 38.65  ? 64  LYS A CD  1 
ATOM   441  C  CE  . LYS A 1 65  ? 74.642  22.975  5.727   1.00 36.99  ? 64  LYS A CE  1 
ATOM   442  N  NZ  . LYS A 1 65  ? 73.672  22.217  6.588   1.00 37.03  ? 64  LYS A NZ  1 
ATOM   443  N  N   . TYR A 1 66  ? 75.186  19.205  2.629   1.00 29.03  ? 65  TYR A N   1 
ATOM   444  C  CA  . TYR A 1 66  ? 74.001  19.599  1.878   1.00 32.83  ? 65  TYR A CA  1 
ATOM   445  C  C   . TYR A 1 66  ? 73.199  18.399  1.395   1.00 31.12  ? 65  TYR A C   1 
ATOM   446  O  O   . TYR A 1 66  ? 71.973  18.496  1.261   1.00 33.82  ? 65  TYR A O   1 
ATOM   447  C  CB  . TYR A 1 66  ? 74.397  20.505  0.711   1.00 30.49  ? 65  TYR A CB  1 
ATOM   448  C  CG  . TYR A 1 66  ? 74.788  21.890  1.170   1.00 32.30  ? 65  TYR A CG  1 
ATOM   449  C  CD1 . TYR A 1 66  ? 73.848  22.750  1.726   1.00 34.76  ? 65  TYR A CD1 1 
ATOM   450  C  CD2 . TYR A 1 66  ? 76.100  22.326  1.080   1.00 31.39  ? 65  TYR A CD2 1 
ATOM   451  C  CE1 . TYR A 1 66  ? 74.206  24.012  2.167   1.00 33.23  ? 65  TYR A CE1 1 
ATOM   452  C  CE2 . TYR A 1 66  ? 76.466  23.587  1.511   1.00 34.99  ? 65  TYR A CE2 1 
ATOM   453  C  CZ  . TYR A 1 66  ? 75.520  24.426  2.053   1.00 35.91  ? 65  TYR A CZ  1 
ATOM   454  O  OH  . TYR A 1 66  ? 75.896  25.681  2.479   1.00 40.18  ? 65  TYR A OH  1 
ATOM   455  N  N   . VAL A 1 67  ? 73.857  17.269  1.138   1.00 32.17  ? 66  VAL A N   1 
ATOM   456  C  CA  . VAL A 1 67  ? 73.117  16.044  0.851   1.00 30.59  ? 66  VAL A CA  1 
ATOM   457  C  C   . VAL A 1 67  ? 72.251  15.669  2.044   1.00 34.26  ? 66  VAL A C   1 
ATOM   458  O  O   . VAL A 1 67  ? 71.068  15.341  1.895   1.00 35.04  ? 66  VAL A O   1 
ATOM   459  C  CB  . VAL A 1 67  ? 74.087  14.913  0.470   1.00 38.12  ? 66  VAL A CB  1 
ATOM   460  C  CG1 . VAL A 1 67  ? 73.400  13.560  0.583   1.00 33.96  ? 66  VAL A CG1 1 
ATOM   461  C  CG2 . VAL A 1 67  ? 74.638  15.140  -0.932  1.00 30.07  ? 66  VAL A CG2 1 
ATOM   462  N  N   . ALA A 1 68  ? 72.820  15.743  3.251   1.00 34.20  ? 67  ALA A N   1 
ATOM   463  C  CA  . ALA A 1 68  ? 72.038  15.519  4.462   1.00 36.49  ? 67  ALA A CA  1 
ATOM   464  C  C   . ALA A 1 68  ? 70.881  16.505  4.572   1.00 38.57  ? 67  ALA A C   1 
ATOM   465  O  O   . ALA A 1 68  ? 69.756  16.118  4.911   1.00 39.89  ? 67  ALA A O   1 
ATOM   466  C  CB  . ALA A 1 68  ? 72.940  15.624  5.691   1.00 33.43  ? 67  ALA A CB  1 
ATOM   467  N  N   . GLN A 1 69  ? 71.140  17.788  4.303   1.00 33.67  ? 68  GLN A N   1 
ATOM   468  C  CA  . GLN A 1 69  ? 70.093  18.789  4.449   1.00 31.75  ? 68  GLN A CA  1 
ATOM   469  C  C   . GLN A 1 69  ? 68.941  18.531  3.491   1.00 36.30  ? 68  GLN A C   1 
ATOM   470  O  O   . GLN A 1 69  ? 67.780  18.770  3.842   1.00 29.86  ? 68  GLN A O   1 
ATOM   471  C  CB  . GLN A 1 69  ? 70.666  20.185  4.231   1.00 33.17  ? 68  GLN A CB  1 
ATOM   472  C  CG  . GLN A 1 69  ? 69.647  21.297  4.362   1.00 37.00  ? 68  GLN A CG  1 
ATOM   473  C  CD  . GLN A 1 69  ? 70.268  22.662  4.191   1.00 36.56  ? 68  GLN A CD  1 
ATOM   474  O  OE1 . GLN A 1 69  ? 71.415  22.883  4.574   1.00 39.26  ? 68  GLN A OE1 1 
ATOM   475  N  NE2 . GLN A 1 69  ? 69.516  23.588  3.611   1.00 35.70  ? 68  GLN A NE2 1 
ATOM   476  N  N   . TYR A 1 70  ? 69.236  18.024  2.293   1.00 34.02  ? 69  TYR A N   1 
ATOM   477  C  CA  . TYR A 1 70  ? 68.236  17.830  1.251   1.00 33.03  ? 69  TYR A CA  1 
ATOM   478  C  C   . TYR A 1 70  ? 67.985  16.355  0.946   1.00 35.17  ? 69  TYR A C   1 
ATOM   479  O  O   . TYR A 1 70  ? 67.531  16.019  -0.149  1.00 33.39  ? 69  TYR A O   1 
ATOM   480  C  CB  . TYR A 1 70  ? 68.648  18.556  -0.030  1.00 35.37  ? 69  TYR A CB  1 
ATOM   481  C  CG  . TYR A 1 70  ? 68.718  20.060  0.096   1.00 35.99  ? 69  TYR A CG  1 
ATOM   482  C  CD1 . TYR A 1 70  ? 67.582  20.803  0.366   1.00 36.67  ? 69  TYR A CD1 1 
ATOM   483  C  CD2 . TYR A 1 70  ? 69.920  20.736  -0.060  1.00 34.12  ? 69  TYR A CD2 1 
ATOM   484  C  CE1 . TYR A 1 70  ? 67.638  22.180  0.481   1.00 36.71  ? 69  TYR A CE1 1 
ATOM   485  C  CE2 . TYR A 1 70  ? 69.985  22.114  0.054   1.00 33.13  ? 69  TYR A CE2 1 
ATOM   486  C  CZ  . TYR A 1 70  ? 68.836  22.827  0.324   1.00 35.67  ? 69  TYR A CZ  1 
ATOM   487  O  OH  . TYR A 1 70  ? 68.883  24.190  0.438   1.00 36.70  ? 69  TYR A OH  1 
ATOM   488  N  N   . HIS A 1 71  ? 68.259  15.462  1.900   1.00 41.30  ? 70  HIS A N   1 
ATOM   489  C  CA  . HIS A 1 71  ? 68.107  14.036  1.619   1.00 47.40  ? 70  HIS A CA  1 
ATOM   490  C  C   . HIS A 1 71  ? 66.657  13.637  1.371   1.00 42.92  ? 70  HIS A C   1 
ATOM   491  O  O   . HIS A 1 71  ? 66.411  12.562  0.814   1.00 47.83  ? 70  HIS A O   1 
ATOM   492  C  CB  . HIS A 1 71  ? 68.703  13.197  2.755   1.00 49.07  ? 70  HIS A CB  1 
ATOM   493  C  CG  . HIS A 1 71  ? 67.757  12.925  3.881   1.00 51.71  ? 70  HIS A CG  1 
ATOM   494  N  ND1 . HIS A 1 71  ? 67.119  13.928  4.579   1.00 55.78  ? 70  HIS A ND1 1 
ATOM   495  C  CD2 . HIS A 1 71  ? 67.352  11.762  4.441   1.00 63.20  ? 70  HIS A CD2 1 
ATOM   496  C  CE1 . HIS A 1 71  ? 66.358  13.394  5.518   1.00 59.51  ? 70  HIS A CE1 1 
ATOM   497  N  NE2 . HIS A 1 71  ? 66.479  12.081  5.454   1.00 72.30  ? 70  HIS A NE2 1 
ATOM   498  N  N   . ASP A 1 72  ? 65.695  14.479  1.749   1.00 38.20  ? 71  ASP A N   1 
ATOM   499  C  CA  . ASP A 1 72  ? 64.292  14.251  1.436   1.00 41.41  ? 71  ASP A CA  1 
ATOM   500  C  C   . ASP A 1 72  ? 63.776  15.228  0.385   1.00 36.95  ? 71  ASP A C   1 
ATOM   501  O  O   . ASP A 1 72  ? 62.570  15.476  0.312   1.00 37.65  ? 71  ASP A O   1 
ATOM   502  C  CB  . ASP A 1 72  ? 63.447  14.330  2.708   1.00 44.40  ? 71  ASP A CB  1 
ATOM   503  C  CG  . ASP A 1 72  ? 63.648  13.125  3.617   1.00 53.06  ? 71  ASP A CG  1 
ATOM   504  O  OD1 . ASP A 1 72  ? 63.997  12.040  3.106   1.00 58.11  ? 71  ASP A OD1 1 
ATOM   505  O  OD2 . ASP A 1 72  ? 63.464  13.263  4.845   1.00 62.32  ? 71  ASP A OD2 1 
ATOM   506  N  N   . ASN A 1 73  ? 64.671  15.782  -0.432  1.00 35.42  ? 72  ASN A N   1 
ATOM   507  C  CA  . ASN A 1 73  ? 64.329  16.773  -1.451  1.00 36.14  ? 72  ASN A CA  1 
ATOM   508  C  C   . ASN A 1 73  ? 64.999  16.345  -2.748  1.00 37.15  ? 72  ASN A C   1 
ATOM   509  O  O   . ASN A 1 73  ? 66.144  16.727  -3.023  1.00 38.46  ? 72  ASN A O   1 
ATOM   510  C  CB  . ASN A 1 73  ? 64.768  18.172  -1.019  1.00 37.17  ? 72  ASN A CB  1 
ATOM   511  C  CG  . ASN A 1 73  ? 64.336  19.260  -1.991  1.00 35.12  ? 72  ASN A CG  1 
ATOM   512  O  OD1 . ASN A 1 73  ? 64.142  19.021  -3.184  1.00 33.14  ? 72  ASN A OD1 1 
ATOM   513  N  ND2 . ASN A 1 73  ? 64.199  20.473  -1.478  1.00 30.38  ? 72  ASN A ND2 1 
ATOM   514  N  N   . PRO A 1 74  ? 64.312  15.556  -3.579  1.00 40.12  ? 73  PRO A N   1 
ATOM   515  C  CA  . PRO A 1 74  ? 64.979  15.011  -4.774  1.00 40.81  ? 73  PRO A CA  1 
ATOM   516  C  C   . PRO A 1 74  ? 65.468  16.081  -5.738  1.00 39.45  ? 73  PRO A C   1 
ATOM   517  O  O   . PRO A 1 74  ? 66.560  15.942  -6.304  1.00 38.59  ? 73  PRO A O   1 
ATOM   518  C  CB  . PRO A 1 74  ? 63.892  14.125  -5.400  1.00 44.34  ? 73  PRO A CB  1 
ATOM   519  C  CG  . PRO A 1 74  ? 62.954  13.814  -4.270  1.00 38.55  ? 73  PRO A CG  1 
ATOM   520  C  CD  . PRO A 1 74  ? 62.939  15.047  -3.430  1.00 33.28  ? 73  PRO A CD  1 
ATOM   521  N  N   . GLN A 1 75  ? 64.696  17.154  -5.929  1.00 35.70  ? 74  GLN A N   1 
ATOM   522  C  CA  . GLN A 1 75  ? 65.080  18.195  -6.879  1.00 35.87  ? 74  GLN A CA  1 
ATOM   523  C  C   . GLN A 1 75  ? 66.359  18.901  -6.445  1.00 35.63  ? 74  GLN A C   1 
ATOM   524  O  O   . GLN A 1 75  ? 67.287  19.074  -7.244  1.00 38.69  ? 74  GLN A O   1 
ATOM   525  C  CB  . GLN A 1 75  ? 63.940  19.201  -7.038  1.00 37.59  ? 74  GLN A CB  1 
ATOM   526  C  CG  . GLN A 1 75  ? 62.726  18.663  -7.773  1.00 38.75  ? 74  GLN A CG  1 
ATOM   527  C  CD  . GLN A 1 75  ? 61.925  17.669  -6.945  1.00 47.75  ? 74  GLN A CD  1 
ATOM   528  O  OE1 . GLN A 1 75  ? 62.016  17.648  -5.715  1.00 45.50  ? 74  GLN A OE1 1 
ATOM   529  N  NE2 . GLN A 1 75  ? 61.141  16.833  -7.620  1.00 48.36  ? 74  GLN A NE2 1 
ATOM   530  N  N   . GLN A 1 76  ? 66.424  19.327  -5.182  1.00 35.94  ? 75  GLN A N   1 
ATOM   531  C  CA  . GLN A 1 76  ? 67.625  19.992  -4.688  1.00 36.26  ? 75  GLN A CA  1 
ATOM   532  C  C   . GLN A 1 76  ? 68.783  19.012  -4.569  1.00 37.98  ? 75  GLN A C   1 
ATOM   533  O  O   . GLN A 1 76  ? 69.938  19.369  -4.837  1.00 33.53  ? 75  GLN A O   1 
ATOM   534  C  CB  . GLN A 1 76  ? 67.345  20.649  -3.337  1.00 38.05  ? 75  GLN A CB  1 
ATOM   535  C  CG  . GLN A 1 76  ? 66.779  22.053  -3.427  1.00 39.25  ? 75  GLN A CG  1 
ATOM   536  C  CD  . GLN A 1 76  ? 67.776  23.055  -3.974  1.00 41.44  ? 75  GLN A CD  1 
ATOM   537  O  OE1 . GLN A 1 76  ? 67.845  23.279  -5.179  1.00 50.38  ? 75  GLN A OE1 1 
ATOM   538  N  NE2 . GLN A 1 76  ? 68.545  23.673  -3.086  1.00 44.20  ? 75  GLN A NE2 1 
ATOM   539  N  N   . LEU A 1 77  ? 68.491  17.774  -4.160  1.00 35.22  ? 76  LEU A N   1 
ATOM   540  C  CA  . LEU A 1 77  ? 69.538  16.767  -4.035  1.00 33.90  ? 76  LEU A CA  1 
ATOM   541  C  C   . LEU A 1 77  ? 70.241  16.546  -5.368  1.00 35.54  ? 76  LEU A C   1 
ATOM   542  O  O   . LEU A 1 77  ? 71.478  16.494  -5.428  1.00 35.95  ? 76  LEU A O   1 
ATOM   543  C  CB  . LEU A 1 77  ? 68.939  15.465  -3.502  1.00 33.26  ? 76  LEU A CB  1 
ATOM   544  C  CG  . LEU A 1 77  ? 69.870  14.381  -2.965  1.00 40.88  ? 76  LEU A CG  1 
ATOM   545  C  CD1 . LEU A 1 77  ? 70.864  14.962  -1.977  1.00 37.36  ? 76  LEU A CD1 1 
ATOM   546  C  CD2 . LEU A 1 77  ? 69.054  13.266  -2.315  1.00 36.76  ? 76  LEU A CD2 1 
ATOM   547  N  N   . ARG A 1 78  ? 69.472  16.447  -6.453  1.00 37.56  ? 77  ARG A N   1 
ATOM   548  C  CA  . ARG A 1 78  ? 70.081  16.317  -7.771  1.00 42.18  ? 77  ARG A CA  1 
ATOM   549  C  C   . ARG A 1 78  ? 70.948  17.530  -8.093  1.00 34.68  ? 77  ARG A C   1 
ATOM   550  O  O   . ARG A 1 78  ? 72.050  17.390  -8.636  1.00 32.08  ? 77  ARG A O   1 
ATOM   551  C  CB  . ARG A 1 78  ? 68.995  16.124  -8.831  1.00 36.14  ? 77  ARG A CB  1 
ATOM   552  C  CG  . ARG A 1 78  ? 69.508  15.550  -10.143 1.00 41.01  ? 77  ARG A CG  1 
ATOM   553  C  CD  . ARG A 1 78  ? 68.599  15.899  -11.305 1.00 43.83  ? 77  ARG A CD  1 
ATOM   554  N  NE  . ARG A 1 78  ? 67.458  14.996  -11.398 1.00 53.03  ? 77  ARG A NE  1 
ATOM   555  C  CZ  . ARG A 1 78  ? 67.484  13.807  -11.987 1.00 56.61  ? 77  ARG A CZ  1 
ATOM   556  N  NH1 . ARG A 1 78  ? 68.586  13.339  -12.552 1.00 49.70  ? 77  ARG A NH1 1 
ATOM   557  N  NH2 . ARG A 1 78  ? 66.378  13.068  -12.007 1.00 53.48  ? 77  ARG A NH2 1 
ATOM   558  N  N   . ARG A 1 79  ? 70.473  18.729  -7.751  1.00 32.71  ? 78  ARG A N   1 
ATOM   559  C  CA  . ARG A 1 79  ? 71.276  19.923  -7.984  1.00 34.11  ? 78  ARG A CA  1 
ATOM   560  C  C   . ARG A 1 79  ? 72.559  19.883  -7.162  1.00 34.82  ? 78  ARG A C   1 
ATOM   561  O  O   . ARG A 1 79  ? 73.637  20.226  -7.661  1.00 35.44  ? 78  ARG A O   1 
ATOM   562  C  CB  . ARG A 1 79  ? 70.457  21.174  -7.660  1.00 36.07  ? 78  ARG A CB  1 
ATOM   563  C  CG  . ARG A 1 79  ? 69.727  21.784  -8.856  1.00 43.85  ? 78  ARG A CG  1 
ATOM   564  C  CD  . ARG A 1 79  ? 68.654  22.787  -8.409  1.00 44.48  ? 78  ARG A CD  1 
ATOM   565  N  NE  . ARG A 1 79  ? 67.330  22.435  -8.913  1.00 50.51  ? 78  ARG A NE  1 
ATOM   566  C  CZ  . ARG A 1 79  ? 66.251  22.273  -8.158  1.00 53.06  ? 78  ARG A CZ  1 
ATOM   567  N  NH1 . ARG A 1 79  ? 66.290  22.441  -6.844  1.00 45.19  ? 78  ARG A NH1 1 
ATOM   568  N  NH2 . ARG A 1 79  ? 65.101  21.935  -8.735  1.00 52.96  ? 78  ARG A NH2 1 
ATOM   569  N  N   . VAL A 1 80  ? 72.464  19.438  -5.905  1.00 31.59  ? 79  VAL A N   1 
ATOM   570  C  CA  . VAL A 1 80  ? 73.635  19.372  -5.035  1.00 29.38  ? 79  VAL A CA  1 
ATOM   571  C  C   . VAL A 1 80  ? 74.677  18.426  -5.619  1.00 31.86  ? 79  VAL A C   1 
ATOM   572  O  O   . VAL A 1 80  ? 75.854  18.779  -5.764  1.00 32.58  ? 79  VAL A O   1 
ATOM   573  C  CB  . VAL A 1 80  ? 73.221  18.944  -3.613  1.00 32.32  ? 79  VAL A CB  1 
ATOM   574  C  CG1 . VAL A 1 80  ? 74.412  18.385  -2.851  1.00 31.59  ? 79  VAL A CG1 1 
ATOM   575  C  CG2 . VAL A 1 80  ? 72.602  20.110  -2.856  1.00 31.38  ? 79  VAL A CG2 1 
ATOM   576  N  N   . VAL A 1 81  ? 74.257  17.206  -5.960  1.00 32.97  ? 80  VAL A N   1 
ATOM   577  C  CA  . VAL A 1 81  ? 75.190  16.204  -6.465  1.00 26.31  ? 80  VAL A CA  1 
ATOM   578  C  C   . VAL A 1 81  ? 75.720  16.602  -7.839  1.00 31.41  ? 80  VAL A C   1 
ATOM   579  O  O   . VAL A 1 81  ? 76.894  16.377  -8.156  1.00 31.67  ? 80  VAL A O   1 
ATOM   580  C  CB  . VAL A 1 81  ? 74.510  14.825  -6.493  1.00 27.92  ? 80  VAL A CB  1 
ATOM   581  C  CG1 . VAL A 1 81  ? 75.440  13.783  -7.075  1.00 28.25  ? 80  VAL A CG1 1 
ATOM   582  C  CG2 . VAL A 1 81  ? 74.061  14.431  -5.092  1.00 25.77  ? 80  VAL A CG2 1 
ATOM   583  N  N   . GLY A 1 82  ? 74.870  17.204  -8.674  1.00 32.97  ? 81  GLY A N   1 
ATOM   584  C  CA  . GLY A 1 82  ? 75.329  17.639  -9.984  1.00 36.32  ? 81  GLY A CA  1 
ATOM   585  C  C   . GLY A 1 82  ? 76.382  18.730  -9.900  1.00 35.99  ? 81  GLY A C   1 
ATOM   586  O  O   . GLY A 1 82  ? 77.409  18.673  -10.585 1.00 34.27  ? 81  GLY A O   1 
ATOM   587  N  N   . THR A 1 83  ? 76.142  19.741  -9.061  1.00 31.86  ? 82  THR A N   1 
ATOM   588  C  CA  . THR A 1 83  ? 77.134  20.798  -8.896  1.00 34.75  ? 82  THR A CA  1 
ATOM   589  C  C   . THR A 1 83  ? 78.411  20.255  -8.265  1.00 34.19  ? 82  THR A C   1 
ATOM   590  O  O   . THR A 1 83  ? 79.518  20.626  -8.676  1.00 33.47  ? 82  THR A O   1 
ATOM   591  C  CB  . THR A 1 83  ? 76.556  21.947  -8.065  1.00 36.05  ? 82  THR A CB  1 
ATOM   592  O  OG1 . THR A 1 83  ? 75.540  22.617  -8.820  1.00 35.97  ? 82  THR A OG1 1 
ATOM   593  C  CG2 . THR A 1 83  ? 77.638  22.959  -7.693  1.00 34.59  ? 82  THR A CG2 1 
ATOM   594  N  N   . SER A 1 84  ? 78.283  19.359  -7.282  1.00 28.95  ? 83  SER A N   1 
ATOM   595  C  CA  . SER A 1 84  ? 79.475  18.767  -6.685  1.00 32.11  ? 83  SER A CA  1 
ATOM   596  C  C   . SER A 1 84  ? 80.267  17.972  -7.716  1.00 36.77  ? 83  SER A C   1 
ATOM   597  O  O   . SER A 1 84  ? 81.504  18.038  -7.750  1.00 33.22  ? 83  SER A O   1 
ATOM   598  C  CB  . SER A 1 84  ? 79.084  17.883  -5.503  1.00 31.63  ? 83  SER A CB  1 
ATOM   599  O  OG  . SER A 1 84  ? 78.334  18.619  -4.553  1.00 33.06  ? 83  SER A OG  1 
ATOM   600  N  N   . SER A 1 85  ? 79.572  17.219  -8.570  1.00 31.19  ? 84  SER A N   1 
ATOM   601  C  CA  . SER A 1 85  ? 80.258  16.483  -9.626  1.00 34.70  ? 84  SER A CA  1 
ATOM   602  C  C   . SER A 1 85  ? 80.982  17.433  -10.573 1.00 34.91  ? 84  SER A C   1 
ATOM   603  O  O   . SER A 1 85  ? 82.136  17.192  -10.943 1.00 35.99  ? 84  SER A O   1 
ATOM   604  C  CB  . SER A 1 85  ? 79.261  15.611  -10.389 1.00 35.23  ? 84  SER A CB  1 
ATOM   605  O  OG  . SER A 1 85  ? 79.744  15.306  -11.687 1.00 40.94  ? 84  SER A OG  1 
ATOM   606  N  N   . ALA A 1 86  ? 80.323  18.529  -10.962 1.00 31.82  ? 85  ALA A N   1 
ATOM   607  C  CA  . ALA A 1 86  ? 80.958  19.507  -11.840 1.00 34.58  ? 85  ALA A CA  1 
ATOM   608  C  C   . ALA A 1 86  ? 82.198  20.110  -11.193 1.00 39.45  ? 85  ALA A C   1 
ATOM   609  O  O   . ALA A 1 86  ? 83.222  20.306  -11.860 1.00 37.77  ? 85  ALA A O   1 
ATOM   610  C  CB  . ALA A 1 86  ? 79.964  20.606  -12.208 1.00 32.77  ? 85  ALA A CB  1 
ATOM   611  N  N   . MET A 1 87  ? 82.131  20.396  -9.890  1.00 34.49  ? 86  MET A N   1 
ATOM   612  C  CA  . MET A 1 87  ? 83.258  21.036  -9.220  1.00 34.80  ? 86  MET A CA  1 
ATOM   613  C  C   . MET A 1 87  ? 84.429  20.075  -9.059  1.00 35.53  ? 86  MET A C   1 
ATOM   614  O  O   . MET A 1 87  ? 85.590  20.468  -9.221  1.00 36.62  ? 86  MET A O   1 
ATOM   615  C  CB  . MET A 1 87  ? 82.814  21.590  -7.868  1.00 31.60  ? 86  MET A CB  1 
ATOM   616  C  CG  . MET A 1 87  ? 81.940  22.831  -7.986  1.00 39.20  ? 86  MET A CG  1 
ATOM   617  S  SD  . MET A 1 87  ? 81.208  23.345  -6.421  1.00 37.72  ? 86  MET A SD  1 
ATOM   618  C  CE  . MET A 1 87  ? 82.575  24.252  -5.706  1.00 34.88  ? 86  MET A CE  1 
ATOM   619  N  N   . VAL A 1 88  ? 84.146  18.810  -8.746  1.00 36.22  ? 87  VAL A N   1 
ATOM   620  C  CA  . VAL A 1 88  ? 85.215  17.827  -8.626  1.00 34.07  ? 87  VAL A CA  1 
ATOM   621  C  C   . VAL A 1 88  ? 85.793  17.502  -9.998  1.00 38.35  ? 87  VAL A C   1 
ATOM   622  O  O   . VAL A 1 88  ? 87.013  17.434  -10.167 1.00 38.48  ? 87  VAL A O   1 
ATOM   623  C  CB  . VAL A 1 88  ? 84.707  16.565  -7.905  1.00 36.72  ? 87  VAL A CB  1 
ATOM   624  C  CG1 . VAL A 1 88  ? 85.690  15.413  -8.078  1.00 40.37  ? 87  VAL A CG1 1 
ATOM   625  C  CG2 . VAL A 1 88  ? 84.474  16.857  -6.428  1.00 35.53  ? 87  VAL A CG2 1 
ATOM   626  N  N   . LEU A 1 89  ? 84.934  17.310  -11.000 1.00 39.55  ? 88  LEU A N   1 
ATOM   627  C  CA  . LEU A 1 89  ? 85.427  17.063  -12.351 1.00 39.16  ? 88  LEU A CA  1 
ATOM   628  C  C   . LEU A 1 89  ? 86.263  18.235  -12.847 1.00 42.55  ? 88  LEU A C   1 
ATOM   629  O  O   . LEU A 1 89  ? 87.378  18.051  -13.350 1.00 36.63  ? 88  LEU A O   1 
ATOM   630  C  CB  . LEU A 1 89  ? 84.260  16.801  -13.304 1.00 41.10  ? 88  LEU A CB  1 
ATOM   631  C  CG  . LEU A 1 89  ? 84.538  17.131  -14.777 1.00 51.80  ? 88  LEU A CG  1 
ATOM   632  C  CD1 . LEU A 1 89  ? 85.306  16.000  -15.459 1.00 54.90  ? 88  LEU A CD1 1 
ATOM   633  C  CD2 . LEU A 1 89  ? 83.252  17.456  -15.537 1.00 54.13  ? 88  LEU A CD2 1 
ATOM   634  N  N   . GLY A 1 90  ? 85.741  19.454  -12.701 1.00 44.05  ? 89  GLY A N   1 
ATOM   635  C  CA  . GLY A 1 90  ? 86.453  20.616  -13.208 1.00 34.77  ? 89  GLY A CA  1 
ATOM   636  C  C   . GLY A 1 90  ? 87.792  20.821  -12.528 1.00 41.27  ? 89  GLY A C   1 
ATOM   637  O  O   . GLY A 1 90  ? 88.805  21.065  -13.184 1.00 47.25  ? 89  GLY A O   1 
ATOM   638  N  N   . PHE A 1 91  ? 87.816  20.722  -11.199 1.00 41.37  ? 90  PHE A N   1 
ATOM   639  C  CA  . PHE A 1 91  ? 89.062  20.971  -10.483 1.00 44.80  ? 90  PHE A CA  1 
ATOM   640  C  C   . PHE A 1 91  ? 90.057  19.838  -10.694 1.00 43.38  ? 90  PHE A C   1 
ATOM   641  O  O   . PHE A 1 91  ? 91.248  20.084  -10.914 1.00 43.55  ? 90  PHE A O   1 
ATOM   642  C  CB  . PHE A 1 91  ? 88.791  21.176  -8.996  1.00 39.07  ? 90  PHE A CB  1 
ATOM   643  C  CG  . PHE A 1 91  ? 89.939  21.789  -8.261  1.00 38.25  ? 90  PHE A CG  1 
ATOM   644  C  CD1 . PHE A 1 91  ? 90.130  23.159  -8.271  1.00 47.13  ? 90  PHE A CD1 1 
ATOM   645  C  CD2 . PHE A 1 91  ? 90.837  20.998  -7.570  1.00 40.54  ? 90  PHE A CD2 1 
ATOM   646  C  CE1 . PHE A 1 91  ? 91.194  23.731  -7.599  1.00 41.26  ? 90  PHE A CE1 1 
ATOM   647  C  CE2 . PHE A 1 91  ? 91.901  21.564  -6.896  1.00 44.34  ? 90  PHE A CE2 1 
ATOM   648  C  CZ  . PHE A 1 91  ? 92.078  22.934  -6.909  1.00 44.90  ? 90  PHE A CZ  1 
ATOM   649  N  N   . SER A 1 92  ? 89.587  18.591  -10.638 1.00 39.93  ? 91  SER A N   1 
ATOM   650  C  CA  . SER A 1 92  ? 90.482  17.459  -10.850 1.00 43.33  ? 91  SER A CA  1 
ATOM   651  C  C   . SER A 1 92  ? 91.070  17.480  -12.255 1.00 39.28  ? 91  SER A C   1 
ATOM   652  O  O   . SER A 1 92  ? 92.235  17.122  -12.451 1.00 37.07  ? 91  SER A O   1 
ATOM   653  C  CB  . SER A 1 92  ? 89.741  16.149  -10.599 1.00 38.54  ? 91  SER A CB  1 
ATOM   654  O  OG  . SER A 1 92  ? 90.642  15.144  -10.180 1.00 54.39  ? 91  SER A OG  1 
ATOM   655  N  N   . THR A 1 93  ? 90.279  17.894  -13.243 1.00 36.25  ? 92  THR A N   1 
ATOM   656  C  CA  . THR A 1 93  ? 90.805  18.032  -14.595 1.00 43.94  ? 92  THR A CA  1 
ATOM   657  C  C   . THR A 1 93  ? 91.865  19.125  -14.655 1.00 50.09  ? 92  THR A C   1 
ATOM   658  O  O   . THR A 1 93  ? 92.942  18.926  -15.229 1.00 46.09  ? 92  THR A O   1 
ATOM   659  C  CB  . THR A 1 93  ? 89.667  18.317  -15.576 1.00 49.38  ? 92  THR A CB  1 
ATOM   660  O  OG1 . THR A 1 93  ? 88.796  17.177  -15.638 1.00 44.18  ? 92  THR A OG1 1 
ATOM   661  C  CG2 . THR A 1 93  ? 90.218  18.613  -16.969 1.00 53.31  ? 92  THR A CG2 1 
ATOM   662  N  N   . LEU A 1 94  ? 91.583  20.282  -14.050 1.00 46.80  ? 93  LEU A N   1 
ATOM   663  C  CA  . LEU A 1 94  ? 92.581  21.344  -13.993 1.00 46.20  ? 93  LEU A CA  1 
ATOM   664  C  C   . LEU A 1 94  ? 93.843  20.868  -13.287 1.00 46.99  ? 93  LEU A C   1 
ATOM   665  O  O   . LEU A 1 94  ? 94.961  21.167  -13.724 1.00 47.58  ? 93  LEU A O   1 
ATOM   666  C  CB  . LEU A 1 94  ? 92.002  22.572  -13.291 1.00 44.20  ? 93  LEU A CB  1 
ATOM   667  C  CG  . LEU A 1 94  ? 91.331  23.628  -14.171 1.00 56.50  ? 93  LEU A CG  1 
ATOM   668  C  CD1 . LEU A 1 94  ? 90.544  22.991  -15.307 1.00 59.97  ? 93  LEU A CD1 1 
ATOM   669  C  CD2 . LEU A 1 94  ? 90.415  24.518  -13.335 1.00 60.13  ? 93  LEU A CD2 1 
ATOM   670  N  N   . MET A 1 95  ? 93.682  20.113  -12.197 1.00 41.89  ? 94  MET A N   1 
ATOM   671  C  CA  . MET A 1 95  ? 94.840  19.584  -11.488 1.00 44.08  ? 94  MET A CA  1 
ATOM   672  C  C   . MET A 1 95  ? 95.642  18.647  -12.378 1.00 44.02  ? 94  MET A C   1 
ATOM   673  O  O   . MET A 1 95  ? 96.877  18.701  -12.400 1.00 49.46  ? 94  MET A O   1 
ATOM   674  C  CB  . MET A 1 95  ? 94.387  18.864  -10.219 1.00 46.52  ? 94  MET A CB  1 
ATOM   675  C  CG  . MET A 1 95  ? 94.173  19.792  -9.041  1.00 49.82  ? 94  MET A CG  1 
ATOM   676  S  SD  . MET A 1 95  ? 95.651  19.933  -8.032  1.00 60.55  ? 94  MET A SD  1 
ATOM   677  C  CE  . MET A 1 95  ? 96.249  21.540  -8.552  1.00 53.09  ? 94  MET A CE  1 
ATOM   678  N  N   . ALA A 1 96  ? 94.953  17.783  -13.126 1.00 41.63  ? 95  ALA A N   1 
ATOM   679  C  CA  . ALA A 1 96  ? 95.639  16.857  -14.017 1.00 43.87  ? 95  ALA A CA  1 
ATOM   680  C  C   . ALA A 1 96  ? 96.453  17.606  -15.065 1.00 47.99  ? 95  ALA A C   1 
ATOM   681  O  O   . ALA A 1 96  ? 97.570  17.196  -15.401 1.00 46.71  ? 95  ALA A O   1 
ATOM   682  C  CB  . ALA A 1 96  ? 94.624  15.925  -14.679 1.00 40.06  ? 95  ALA A CB  1 
ATOM   683  N  N   . LEU A 1 97  ? 95.919  18.719  -15.576 1.00 46.53  ? 96  LEU A N   1 
ATOM   684  C  CA  . LEU A 1 97  ? 96.645  19.506  -16.568 1.00 45.14  ? 96  LEU A CA  1 
ATOM   685  C  C   . LEU A 1 97  ? 97.863  20.184  -15.955 1.00 47.83  ? 96  LEU A C   1 
ATOM   686  O  O   . LEU A 1 97  ? 98.942  20.198  -16.559 1.00 47.93  ? 96  LEU A O   1 
ATOM   687  C  CB  . LEU A 1 97  ? 95.715  20.541  -17.195 1.00 46.99  ? 96  LEU A CB  1 
ATOM   688  C  CG  . LEU A 1 97  ? 94.538  19.961  -17.981 1.00 58.13  ? 96  LEU A CG  1 
ATOM   689  C  CD1 . LEU A 1 97  ? 93.450  21.007  -18.187 1.00 64.80  ? 96  LEU A CD1 1 
ATOM   690  C  CD2 . LEU A 1 97  ? 95.015  19.412  -19.317 1.00 61.85  ? 96  LEU A CD2 1 
ATOM   691  N  N   . VAL A 1 98  ? 97.710  20.750  -14.757 1.00 48.35  ? 97  VAL A N   1 
ATOM   692  C  CA  . VAL A 1 98  ? 98.838  21.385  -14.083 1.00 47.87  ? 97  VAL A CA  1 
ATOM   693  C  C   . VAL A 1 98  ? 99.936  20.364  -13.810 1.00 54.14  ? 97  VAL A C   1 
ATOM   694  O  O   . VAL A 1 98  ? 101.131 20.657  -13.957 1.00 54.02  ? 97  VAL A O   1 
ATOM   695  C  CB  . VAL A 1 98  ? 98.360  22.073  -12.790 1.00 53.11  ? 97  VAL A CB  1 
ATOM   696  C  CG1 . VAL A 1 98  ? 99.500  22.212  -11.794 1.00 58.31  ? 97  VAL A CG1 1 
ATOM   697  C  CG2 . VAL A 1 98  ? 97.765  23.430  -13.111 1.00 51.46  ? 97  VAL A CG2 1 
ATOM   698  N  N   . PHE A 1 99  ? 99.548  19.143  -13.439 1.00 48.91  ? 98  PHE A N   1 
ATOM   699  C  CA  . PHE A 1 99  ? 100.534 18.114  -13.126 1.00 49.96  ? 98  PHE A CA  1 
ATOM   700  C  C   . PHE A 1 99  ? 101.296 17.679  -14.369 1.00 52.06  ? 98  PHE A C   1 
ATOM   701  O  O   . PHE A 1 99  ? 102.524 17.541  -14.338 1.00 52.13  ? 98  PHE A O   1 
ATOM   702  C  CB  . PHE A 1 99  ? 99.850  16.915  -12.478 1.00 47.70  ? 98  PHE A CB  1 
ATOM   703  C  CG  . PHE A 1 99  ? 99.925  16.918  -10.988 1.00 51.38  ? 98  PHE A CG  1 
ATOM   704  C  CD1 . PHE A 1 99  ? 99.502  18.021  -10.268 1.00 46.83  ? 98  PHE A CD1 1 
ATOM   705  C  CD2 . PHE A 1 99  ? 100.416 15.821  -10.302 1.00 53.13  ? 98  PHE A CD2 1 
ATOM   706  C  CE1 . PHE A 1 99  ? 99.571  18.033  -8.894  1.00 48.71  ? 98  PHE A CE1 1 
ATOM   707  C  CE2 . PHE A 1 99  ? 100.482 15.826  -8.924  1.00 54.48  ? 98  PHE A CE2 1 
ATOM   708  C  CZ  . PHE A 1 99  ? 100.059 16.934  -8.220  1.00 49.36  ? 98  PHE A CZ  1 
ATOM   709  N  N   . VAL A 1 100 ? 100.583 17.445  -15.472 1.00 49.91  ? 99  VAL A N   1 
ATOM   710  C  CA  . VAL A 1 100 ? 101.243 16.948  -16.671 1.00 51.85  ? 99  VAL A CA  1 
ATOM   711  C  C   . VAL A 1 100 ? 102.090 18.041  -17.315 1.00 53.95  ? 99  VAL A C   1 
ATOM   712  O  O   . VAL A 1 100 ? 103.172 17.764  -17.847 1.00 52.72  ? 99  VAL A O   1 
ATOM   713  C  CB  . VAL A 1 100 ? 100.199 16.361  -17.644 1.00 55.32  ? 99  VAL A CB  1 
ATOM   714  C  CG1 . VAL A 1 100 ? 99.312  17.450  -18.222 1.00 56.57  ? 99  VAL A CG1 1 
ATOM   715  C  CG2 . VAL A 1 100 ? 100.880 15.584  -18.758 1.00 61.73  ? 99  VAL A CG2 1 
ATOM   716  N  N   . LEU A 1 101 ? 101.642 19.297  -17.246 1.00 55.73  ? 100 LEU A N   1 
ATOM   717  C  CA  . LEU A 1 101 ? 102.388 20.379  -17.878 1.00 57.12  ? 100 LEU A CA  1 
ATOM   718  C  C   . LEU A 1 101 ? 103.660 20.699  -17.104 1.00 56.98  ? 100 LEU A C   1 
ATOM   719  O  O   . LEU A 1 101 ? 104.707 20.969  -17.702 1.00 66.84  ? 100 LEU A O   1 
ATOM   720  C  CB  . LEU A 1 101 ? 101.505 21.621  -18.005 1.00 56.12  ? 100 LEU A CB  1 
ATOM   721  C  CG  . LEU A 1 101 ? 100.918 21.902  -19.394 1.00 59.91  ? 100 LEU A CG  1 
ATOM   722  C  CD1 . LEU A 1 101 ? 102.022 22.190  -20.388 1.00 65.55  ? 100 LEU A CD1 1 
ATOM   723  C  CD2 . LEU A 1 101 ? 100.053 20.745  -19.882 1.00 63.27  ? 100 LEU A CD2 1 
ATOM   724  N  N   . ALA A 1 102 ? 103.594 20.665  -15.779 1.00 57.62  ? 101 ALA A N   1 
ATOM   725  C  CA  . ALA A 1 102 ? 104.723 20.997  -14.919 1.00 53.45  ? 101 ALA A CA  1 
ATOM   726  C  C   . ALA A 1 102 ? 105.286 19.759  -14.228 1.00 46.00  ? 101 ALA A C   1 
ATOM   727  O  O   . ALA A 1 102 ? 105.729 19.819  -13.082 1.00 48.46  ? 101 ALA A O   1 
ATOM   728  C  CB  . ALA A 1 102 ? 104.321 22.046  -13.886 1.00 53.15  ? 101 ALA A CB  1 
ATOM   729  N  N   . ALA A 1 103 ? 105.281 18.620  -14.922 1.00 45.45  ? 102 ALA A N   1 
ATOM   730  C  CA  . ALA A 1 103 ? 105.789 17.390  -14.319 1.00 48.97  ? 102 ALA A CA  1 
ATOM   731  C  C   . ALA A 1 103 ? 107.265 17.501  -13.947 1.00 54.88  ? 102 ALA A C   1 
ATOM   732  O  O   . ALA A 1 103 ? 107.701 16.886  -12.967 1.00 52.21  ? 102 ALA A O   1 
ATOM   733  C  CB  . ALA A 1 103 ? 105.567 16.210  -15.264 1.00 46.01  ? 102 ALA A CB  1 
ATOM   734  N  N   . ALA A 1 104 ? 108.051 18.276  -14.708 1.00 52.00  ? 103 ALA A N   1 
ATOM   735  C  CA  . ALA A 1 104 ? 109.468 18.412  -14.373 1.00 50.69  ? 103 ALA A CA  1 
ATOM   736  C  C   . ALA A 1 104 ? 109.683 19.254  -13.121 1.00 53.83  ? 103 ALA A C   1 
ATOM   737  O  O   . ALA A 1 104 ? 110.398 18.793  -12.212 1.00 54.75  ? 103 ALA A O   1 
ATOM   738  C  CB  . ALA A 1 104 ? 110.243 18.958  -15.576 1.00 48.39  ? 103 ALA A CB  1 
ATOM   739  N  N   . PRO A 1 105 ? 109.121 20.464  -12.990 1.00 54.26  ? 104 PRO A N   1 
ATOM   740  C  CA  . PRO A 1 105 ? 109.282 21.197  -11.722 1.00 53.60  ? 104 PRO A CA  1 
ATOM   741  C  C   . PRO A 1 105 ? 108.681 20.478  -10.531 1.00 51.77  ? 104 PRO A C   1 
ATOM   742  O  O   . PRO A 1 105 ? 109.215 20.587  -9.419  1.00 51.86  ? 104 PRO A O   1 
ATOM   743  C  CB  . PRO A 1 105 ? 108.566 22.527  -11.990 1.00 57.94  ? 104 PRO A CB  1 
ATOM   744  C  CG  . PRO A 1 105 ? 108.576 22.665  -13.474 1.00 60.20  ? 104 PRO A CG  1 
ATOM   745  C  CD  . PRO A 1 105 ? 108.409 21.277  -13.992 1.00 53.28  ? 104 PRO A CD  1 
ATOM   746  N  N   . ILE A 1 106 ? 107.580 19.751  -10.725 1.00 51.60  ? 105 ILE A N   1 
ATOM   747  C  CA  . ILE A 1 106 ? 106.981 19.014  -9.619  1.00 52.02  ? 105 ILE A CA  1 
ATOM   748  C  C   . ILE A 1 106 ? 107.893 17.875  -9.190  1.00 48.41  ? 105 ILE A C   1 
ATOM   749  O  O   . ILE A 1 106 ? 108.103 17.645  -7.994  1.00 51.36  ? 105 ILE A O   1 
ATOM   750  C  CB  . ILE A 1 106 ? 105.582 18.503  -10.005 1.00 45.41  ? 105 ILE A CB  1 
ATOM   751  C  CG1 . ILE A 1 106 ? 104.599 19.668  -10.116 1.00 48.03  ? 105 ILE A CG1 1 
ATOM   752  C  CG2 . ILE A 1 106 ? 105.097 17.479  -8.993  1.00 42.13  ? 105 ILE A CG2 1 
ATOM   753  C  CD1 . ILE A 1 106 ? 103.286 19.298  -10.801 1.00 46.77  ? 105 ILE A CD1 1 
ATOM   754  N  N   . SER A 1 107 ? 108.448 17.144  -10.156 1.00 50.12  ? 106 SER A N   1 
ATOM   755  C  CA  . SER A 1 107 ? 109.406 16.093  -9.828  1.00 53.86  ? 106 SER A CA  1 
ATOM   756  C  C   . SER A 1 107 ? 110.615 16.666  -9.101  1.00 54.82  ? 106 SER A C   1 
ATOM   757  O  O   . SER A 1 107 ? 111.114 16.066  -8.141  1.00 51.30  ? 106 SER A O   1 
ATOM   758  C  CB  . SER A 1 107 ? 109.834 15.360  -11.101 1.00 50.55  ? 106 SER A CB  1 
ATOM   759  O  OG  . SER A 1 107 ? 110.877 14.441  -10.841 1.00 50.22  ? 106 SER A OG  1 
ATOM   760  N  N   . GLN A 1 108 ? 111.089 17.838  -9.531  1.00 51.84  ? 107 GLN A N   1 
ATOM   761  C  CA  . GLN A 1 108 ? 112.232 18.457  -8.867  1.00 56.47  ? 107 GLN A CA  1 
ATOM   762  C  C   . GLN A 1 108 ? 111.911 18.797  -7.415  1.00 57.19  ? 107 GLN A C   1 
ATOM   763  O  O   . GLN A 1 108 ? 112.733 18.567  -6.518  1.00 56.95  ? 107 GLN A O   1 
ATOM   764  C  CB  . GLN A 1 108 ? 112.668 19.708  -9.627  1.00 54.69  ? 107 GLN A CB  1 
ATOM   765  C  CG  . GLN A 1 108 ? 113.863 20.417  -9.015  1.00 58.42  ? 107 GLN A CG  1 
ATOM   766  C  CD  . GLN A 1 108 ? 115.136 19.599  -9.114  1.00 60.72  ? 107 GLN A CD  1 
ATOM   767  O  OE1 . GLN A 1 108 ? 115.401 18.960  -10.136 1.00 59.35  ? 107 GLN A OE1 1 
ATOM   768  N  NE2 . GLN A 1 108 ? 115.937 19.617  -8.051  1.00 55.98  ? 107 GLN A NE2 1 
ATOM   769  N  N   . GLY A 1 109 ? 110.718 19.338  -7.161  1.00 51.90  ? 108 GLY A N   1 
ATOM   770  C  CA  . GLY A 1 109 ? 110.345 19.687  -5.801  1.00 51.91  ? 108 GLY A CA  1 
ATOM   771  C  C   . GLY A 1 109 ? 110.070 18.496  -4.910  1.00 51.75  ? 108 GLY A C   1 
ATOM   772  O  O   . GLY A 1 109 ? 110.209 18.604  -3.688  1.00 53.41  ? 108 GLY A O   1 
ATOM   773  N  N   . LEU A 1 110 ? 109.688 17.364  -5.493  1.00 52.28  ? 109 LEU A N   1 
ATOM   774  C  CA  . LEU A 1 110 ? 109.340 16.169  -4.734  1.00 46.83  ? 109 LEU A CA  1 
ATOM   775  C  C   . LEU A 1 110 ? 110.556 15.294  -4.439  1.00 54.64  ? 109 LEU A C   1 
ATOM   776  O  O   . LEU A 1 110 ? 110.725 14.816  -3.309  1.00 49.06  ? 109 LEU A O   1 
ATOM   777  C  CB  . LEU A 1 110 ? 108.294 15.351  -5.499  1.00 43.39  ? 109 LEU A CB  1 
ATOM   778  C  CG  . LEU A 1 110 ? 106.841 15.812  -5.436  1.00 44.35  ? 109 LEU A CG  1 
ATOM   779  C  CD1 . LEU A 1 110 ? 105.987 14.959  -6.355  1.00 44.23  ? 109 LEU A CD1 1 
ATOM   780  C  CD2 . LEU A 1 110 ? 106.319 15.743  -4.011  1.00 46.94  ? 109 LEU A CD2 1 
ATOM   781  N  N   . PHE A 1 111 ? 111.406 15.072  -5.450  1.00 48.76  ? 110 PHE A N   1 
ATOM   782  C  CA  . PHE A 1 111 ? 112.491 14.107  -5.361  1.00 53.25  ? 110 PHE A CA  1 
ATOM   783  C  C   . PHE A 1 111 ? 113.881 14.715  -5.470  1.00 48.00  ? 110 PHE A C   1 
ATOM   784  O  O   . PHE A 1 111 ? 114.856 14.032  -5.143  1.00 49.72  ? 110 PHE A O   1 
ATOM   785  C  CB  . PHE A 1 111 ? 112.355 13.035  -6.455  1.00 51.97  ? 110 PHE A CB  1 
ATOM   786  C  CG  . PHE A 1 111 ? 111.015 12.354  -6.487  1.00 49.96  ? 110 PHE A CG  1 
ATOM   787  C  CD1 . PHE A 1 111 ? 110.777 11.232  -5.710  1.00 45.18  ? 110 PHE A CD1 1 
ATOM   788  C  CD2 . PHE A 1 111 ? 110.003 12.820  -7.312  1.00 48.83  ? 110 PHE A CD2 1 
ATOM   789  C  CE1 . PHE A 1 111 ? 109.554 10.597  -5.745  1.00 51.24  ? 110 PHE A CE1 1 
ATOM   790  C  CE2 . PHE A 1 111 ? 108.774 12.189  -7.347  1.00 49.89  ? 110 PHE A CE2 1 
ATOM   791  C  CZ  . PHE A 1 111 ? 108.549 11.075  -6.563  1.00 46.76  ? 110 PHE A CZ  1 
ATOM   792  N  N   . GLY A 1 112 ? 114.005 15.957  -5.929  1.00 51.28  ? 111 GLY A N   1 
ATOM   793  C  CA  . GLY A 1 112 ? 115.294 16.602  -6.061  1.00 54.10  ? 111 GLY A CA  1 
ATOM   794  C  C   . GLY A 1 112 ? 115.899 16.537  -7.446  1.00 56.48  ? 111 GLY A C   1 
ATOM   795  O  O   . GLY A 1 112 ? 116.942 17.159  -7.677  1.00 61.48  ? 111 GLY A O   1 
ATOM   796  N  N   . ASN A 1 113 ? 115.284 15.802  -8.367  1.00 58.81  ? 112 ASN A N   1 
ATOM   797  C  CA  . ASN A 1 113 ? 115.727 15.770  -9.754  1.00 56.35  ? 112 ASN A CA  1 
ATOM   798  C  C   . ASN A 1 113 ? 114.500 15.576  -10.636 1.00 54.28  ? 112 ASN A C   1 
ATOM   799  O  O   . ASN A 1 113 ? 113.368 15.501  -10.153 1.00 53.59  ? 112 ASN A O   1 
ATOM   800  C  CB  . ASN A 1 113 ? 116.782 14.679  -9.978  1.00 51.03  ? 112 ASN A CB  1 
ATOM   801  C  CG  . ASN A 1 113 ? 116.290 13.304  -9.578  1.00 55.45  ? 112 ASN A CG  1 
ATOM   802  O  OD1 . ASN A 1 113 ? 115.337 12.778  -10.157 1.00 54.99  ? 112 ASN A OD1 1 
ATOM   803  N  ND2 . ASN A 1 113 ? 116.932 12.715  -8.577  1.00 56.42  ? 112 ASN A ND2 1 
ATOM   804  N  N   . THR A 1 114 ? 114.733 15.490  -11.943 1.00 53.44  ? 113 THR A N   1 
ATOM   805  C  CA  . THR A 1 114 ? 113.657 15.435  -12.921 1.00 51.39  ? 113 THR A CA  1 
ATOM   806  C  C   . THR A 1 114 ? 113.397 14.023  -13.437 1.00 50.39  ? 113 THR A C   1 
ATOM   807  O  O   . THR A 1 114 ? 112.705 13.860  -14.447 1.00 50.95  ? 113 THR A O   1 
ATOM   808  C  CB  . THR A 1 114 ? 113.973 16.372  -14.088 1.00 52.04  ? 113 THR A CB  1 
ATOM   809  O  OG1 . THR A 1 114 ? 115.227 15.999  -14.673 1.00 62.66  ? 113 THR A OG1 1 
ATOM   810  C  CG2 . THR A 1 114 ? 114.064 17.814  -13.604 1.00 50.95  ? 113 THR A CG2 1 
ATOM   811  N  N   . ASP A 1 115 ? 113.925 13.000  -12.764 1.00 49.07  ? 114 ASP A N   1 
ATOM   812  C  CA  . ASP A 1 115 ? 113.844 11.629  -13.259 1.00 44.17  ? 114 ASP A CA  1 
ATOM   813  C  C   . ASP A 1 115 ? 112.489 10.975  -13.022 1.00 54.29  ? 114 ASP A C   1 
ATOM   814  O  O   . ASP A 1 115 ? 112.320 9.802   -13.373 1.00 57.50  ? 114 ASP A O   1 
ATOM   815  C  CB  . ASP A 1 115 ? 114.935 10.767  -12.615 1.00 50.22  ? 114 ASP A CB  1 
ATOM   816  C  CG  . ASP A 1 115 ? 116.341 11.238  -12.959 1.00 54.61  ? 114 ASP A CG  1 
ATOM   817  O  OD1 . ASP A 1 115 ? 116.497 12.057  -13.889 1.00 55.75  ? 114 ASP A OD1 1 
ATOM   818  O  OD2 . ASP A 1 115 ? 117.292 10.785  -12.290 1.00 59.15  ? 114 ASP A OD2 1 
ATOM   819  N  N   . TYR A 1 116 ? 111.522 11.693  -12.450 1.00 54.83  ? 115 TYR A N   1 
ATOM   820  C  CA  . TYR A 1 116 ? 110.242 11.114  -12.056 1.00 54.03  ? 115 TYR A CA  1 
ATOM   821  C  C   . TYR A 1 116 ? 109.070 11.774  -12.778 1.00 49.90  ? 115 TYR A C   1 
ATOM   822  O  O   . TYR A 1 116 ? 107.942 11.767  -12.280 1.00 50.34  ? 115 TYR A O   1 
ATOM   823  C  CB  . TYR A 1 116 ? 110.063 11.203  -10.540 1.00 50.99  ? 115 TYR A CB  1 
ATOM   824  C  CG  . TYR A 1 116 ? 111.111 10.438  -9.753  1.00 46.35  ? 115 TYR A CG  1 
ATOM   825  C  CD1 . TYR A 1 116 ? 112.358 10.994  -9.483  1.00 53.01  ? 115 TYR A CD1 1 
ATOM   826  C  CD2 . TYR A 1 116 ? 110.854 9.157   -9.286  1.00 46.88  ? 115 TYR A CD2 1 
ATOM   827  C  CE1 . TYR A 1 116 ? 113.318 10.290  -8.767  1.00 44.99  ? 115 TYR A CE1 1 
ATOM   828  C  CE2 . TYR A 1 116 ? 111.802 8.449   -8.573  1.00 41.91  ? 115 TYR A CE2 1 
ATOM   829  C  CZ  . TYR A 1 116 ? 113.030 9.018   -8.315  1.00 47.41  ? 115 TYR A CZ  1 
ATOM   830  O  OH  . TYR A 1 116 ? 113.962 8.305   -7.601  1.00 47.68  ? 115 TYR A OH  1 
ATOM   831  N  N   . GLN A 1 117 ? 109.326 12.335  -13.964 1.00 48.67  ? 116 GLN A N   1 
ATOM   832  C  CA  . GLN A 1 117 ? 108.276 13.017  -14.718 1.00 50.93  ? 116 GLN A CA  1 
ATOM   833  C  C   . GLN A 1 117 ? 107.156 12.061  -15.111 1.00 50.10  ? 116 GLN A C   1 
ATOM   834  O  O   . GLN A 1 117 ? 105.974 12.427  -15.071 1.00 48.45  ? 116 GLN A O   1 
ATOM   835  C  CB  . GLN A 1 117 ? 108.869 13.668  -15.969 1.00 55.75  ? 116 GLN A CB  1 
ATOM   836  C  CG  . GLN A 1 117 ? 109.416 15.067  -15.772 1.00 54.05  ? 116 GLN A CG  1 
ATOM   837  C  CD  . GLN A 1 117 ? 110.360 15.473  -16.893 1.00 64.84  ? 116 GLN A CD  1 
ATOM   838  O  OE1 . GLN A 1 117 ? 111.542 15.736  -16.664 1.00 56.43  ? 116 GLN A OE1 1 
ATOM   839  N  NE2 . GLN A 1 117 ? 109.840 15.517  -18.116 1.00 55.25  ? 116 GLN A NE2 1 
ATOM   840  N  N   . GLY A 1 118 ? 107.509 10.840  -15.517 1.00 50.11  ? 117 GLY A N   1 
ATOM   841  C  CA  . GLY A 1 118 ? 106.489 9.875   -15.894 1.00 46.75  ? 117 GLY A CA  1 
ATOM   842  C  C   . GLY A 1 118 ? 105.575 9.516   -14.740 1.00 46.56  ? 117 GLY A C   1 
ATOM   843  O  O   . GLY A 1 118 ? 104.358 9.401   -14.911 1.00 49.85  ? 117 GLY A O   1 
ATOM   844  N  N   . LEU A 1 119 ? 106.147 9.344   -13.546 1.00 46.45  ? 118 LEU A N   1 
ATOM   845  C  CA  . LEU A 1 119 ? 105.337 9.051   -12.367 1.00 46.32  ? 118 LEU A CA  1 
ATOM   846  C  C   . LEU A 1 119 ? 104.406 10.211  -12.032 1.00 48.08  ? 118 LEU A C   1 
ATOM   847  O  O   . LEU A 1 119 ? 103.255 9.998   -11.631 1.00 45.99  ? 118 LEU A O   1 
ATOM   848  C  CB  . LEU A 1 119 ? 106.247 8.735   -11.183 1.00 42.71  ? 118 LEU A CB  1 
ATOM   849  C  CG  . LEU A 1 119 ? 105.574 8.664   -9.814  1.00 47.26  ? 118 LEU A CG  1 
ATOM   850  C  CD1 . LEU A 1 119 ? 104.547 7.535   -9.786  1.00 36.36  ? 118 LEU A CD1 1 
ATOM   851  C  CD2 . LEU A 1 119 ? 106.622 8.488   -8.722  1.00 44.14  ? 118 LEU A CD2 1 
ATOM   852  N  N   . VAL A 1 120 ? 104.888 11.446  -12.188 1.00 48.89  ? 119 VAL A N   1 
ATOM   853  C  CA  . VAL A 1 120 ? 104.046 12.609  -11.926 1.00 46.14  ? 119 VAL A CA  1 
ATOM   854  C  C   . VAL A 1 120 ? 102.898 12.667  -12.924 1.00 46.12  ? 119 VAL A C   1 
ATOM   855  O  O   . VAL A 1 120 ? 101.751 12.952  -12.557 1.00 48.71  ? 119 VAL A O   1 
ATOM   856  C  CB  . VAL A 1 120 ? 104.891 13.897  -11.954 1.00 45.41  ? 119 VAL A CB  1 
ATOM   857  C  CG1 . VAL A 1 120 ? 103.998 15.126  -11.924 1.00 44.98  ? 119 VAL A CG1 1 
ATOM   858  C  CG2 . VAL A 1 120 ? 105.855 13.914  -10.782 1.00 50.67  ? 119 VAL A CG2 1 
ATOM   859  N  N   . ARG A 1 121 ? 103.183 12.388  -14.197 1.00 47.98  ? 120 ARG A N   1 
ATOM   860  C  CA  . ARG A 1 121 ? 102.124 12.384  -15.200 1.00 50.53  ? 120 ARG A CA  1 
ATOM   861  C  C   . ARG A 1 121 ? 101.100 11.292  -14.919 1.00 47.29  ? 120 ARG A C   1 
ATOM   862  O  O   . ARG A 1 121 ? 99.905  11.487  -15.160 1.00 42.64  ? 120 ARG A O   1 
ATOM   863  C  CB  . ARG A 1 121 ? 102.725 12.222  -16.596 1.00 48.41  ? 120 ARG A CB  1 
ATOM   864  C  CG  . ARG A 1 121 ? 103.448 13.464  -17.103 1.00 50.99  ? 120 ARG A CG  1 
ATOM   865  C  CD  . ARG A 1 121 ? 103.775 13.344  -18.577 1.00 50.44  ? 120 ARG A CD  1 
ATOM   866  N  NE  . ARG A 1 121 ? 104.669 12.224  -18.836 1.00 60.37  ? 120 ARG A NE  1 
ATOM   867  C  CZ  . ARG A 1 121 ? 105.984 12.334  -18.960 1.00 64.66  ? 120 ARG A CZ  1 
ATOM   868  N  NH1 . ARG A 1 121 ? 106.590 13.507  -18.877 1.00 55.19  ? 120 ARG A NH1 1 
ATOM   869  N  NH2 . ARG A 1 121 ? 106.710 11.239  -19.172 1.00 71.09  ? 120 ARG A NH2 1 
ATOM   870  N  N   . LEU A 1 122 ? 101.542 10.144  -14.400 1.00 43.27  ? 121 LEU A N   1 
ATOM   871  C  CA  . LEU A 1 122 ? 100.592 9.114   -13.994 1.00 51.47  ? 121 LEU A CA  1 
ATOM   872  C  C   . LEU A 1 122 ? 99.749  9.579   -12.815 1.00 47.99  ? 121 LEU A C   1 
ATOM   873  O  O   . LEU A 1 122 ? 98.532  9.357   -12.789 1.00 47.85  ? 121 LEU A O   1 
ATOM   874  C  CB  . LEU A 1 122 ? 101.327 7.818   -13.648 1.00 48.27  ? 121 LEU A CB  1 
ATOM   875  C  CG  . LEU A 1 122 ? 101.754 6.949   -14.833 1.00 55.13  ? 121 LEU A CG  1 
ATOM   876  C  CD1 . LEU A 1 122 ? 101.850 5.488   -14.422 1.00 56.08  ? 121 LEU A CD1 1 
ATOM   877  C  CD2 . LEU A 1 122 ? 100.805 7.119   -16.012 1.00 51.72  ? 121 LEU A CD2 1 
ATOM   878  N  N   . VAL A 1 123 ? 100.379 10.232  -11.834 1.00 45.87  ? 122 VAL A N   1 
ATOM   879  C  CA  . VAL A 1 123 ? 99.638  10.732  -10.680 1.00 45.61  ? 122 VAL A CA  1 
ATOM   880  C  C   . VAL A 1 123 ? 98.568  11.731  -11.117 1.00 44.92  ? 122 VAL A C   1 
ATOM   881  O  O   . VAL A 1 123 ? 97.502  11.823  -10.494 1.00 40.77  ? 122 VAL A O   1 
ATOM   882  C  CB  . VAL A 1 123 ? 100.622 11.331  -9.653  1.00 46.86  ? 122 VAL A CB  1 
ATOM   883  C  CG1 . VAL A 1 123 ? 99.923  12.315  -8.717  1.00 53.89  ? 122 VAL A CG1 1 
ATOM   884  C  CG2 . VAL A 1 123 ? 101.285 10.215  -8.858  1.00 42.72  ? 122 VAL A CG2 1 
ATOM   885  N  N   . ALA A 1 124 ? 98.813  12.460  -12.214 1.00 46.39  ? 123 ALA A N   1 
ATOM   886  C  CA  . ALA A 1 124 ? 97.811  13.385  -12.737 1.00 45.96  ? 123 ALA A CA  1 
ATOM   887  C  C   . ALA A 1 124 ? 96.497  12.682  -13.058 1.00 46.70  ? 123 ALA A C   1 
ATOM   888  O  O   . ALA A 1 124 ? 95.425  13.289  -12.948 1.00 37.95  ? 123 ALA A O   1 
ATOM   889  C  CB  . ALA A 1 124 ? 98.343  14.090  -13.985 1.00 44.96  ? 123 ALA A CB  1 
ATOM   890  N  N   . LEU A 1 125 ? 96.554  11.415  -13.466 1.00 42.81  ? 124 LEU A N   1 
ATOM   891  C  CA  . LEU A 1 125 ? 95.338  10.650  -13.698 1.00 43.63  ? 124 LEU A CA  1 
ATOM   892  C  C   . LEU A 1 125 ? 94.857  9.933   -12.446 1.00 45.95  ? 124 LEU A C   1 
ATOM   893  O  O   . LEU A 1 125 ? 93.646  9.747   -12.275 1.00 47.17  ? 124 LEU A O   1 
ATOM   894  C  CB  . LEU A 1 125 ? 95.561  9.635   -14.821 1.00 44.61  ? 124 LEU A CB  1 
ATOM   895  C  CG  . LEU A 1 125 ? 95.947  10.254  -16.170 1.00 57.02  ? 124 LEU A CG  1 
ATOM   896  C  CD1 . LEU A 1 125 ? 95.996  9.198   -17.259 1.00 51.11  ? 124 LEU A CD1 1 
ATOM   897  C  CD2 . LEU A 1 125 ? 94.986  11.376  -16.550 1.00 51.89  ? 124 LEU A CD2 1 
ATOM   898  N  N   . VAL A 1 126 ? 95.778  9.541   -11.562 1.00 41.13  ? 125 VAL A N   1 
ATOM   899  C  CA  . VAL A 1 126 ? 95.396  8.835   -10.343 1.00 39.32  ? 125 VAL A CA  1 
ATOM   900  C  C   . VAL A 1 126 ? 94.607  9.752   -9.413  1.00 44.56  ? 125 VAL A C   1 
ATOM   901  O  O   . VAL A 1 126 ? 93.660  9.314   -8.746  1.00 38.22  ? 125 VAL A O   1 
ATOM   902  C  CB  . VAL A 1 126 ? 96.645  8.261   -9.649  1.00 41.41  ? 125 VAL A CB  1 
ATOM   903  C  CG1 . VAL A 1 126 ? 96.264  7.535   -8.375  1.00 44.08  ? 125 VAL A CG1 1 
ATOM   904  C  CG2 . VAL A 1 126 ? 97.405  7.334   -10.585 1.00 46.48  ? 125 VAL A CG2 1 
ATOM   905  N  N   . GLN A 1 127 ? 94.971  11.038  -9.356  1.00 39.08  ? 126 GLN A N   1 
ATOM   906  C  CA  . GLN A 1 127 ? 94.263  11.955  -8.468  1.00 38.75  ? 126 GLN A CA  1 
ATOM   907  C  C   . GLN A 1 127 ? 92.812  12.166  -8.886  1.00 40.32  ? 126 GLN A C   1 
ATOM   908  O  O   . GLN A 1 127 ? 91.990  12.560  -8.052  1.00 37.72  ? 126 GLN A O   1 
ATOM   909  C  CB  . GLN A 1 127 ? 94.994  13.295  -8.390  1.00 42.01  ? 126 GLN A CB  1 
ATOM   910  C  CG  . GLN A 1 127 ? 95.209  13.967  -9.726  1.00 41.67  ? 126 GLN A CG  1 
ATOM   911  C  CD  . GLN A 1 127 ? 94.064  14.881  -10.096 1.00 44.79  ? 126 GLN A CD  1 
ATOM   912  O  OE1 . GLN A 1 127 ? 93.280  15.288  -9.237  1.00 44.64  ? 126 GLN A OE1 1 
ATOM   913  N  NE2 . GLN A 1 127 ? 93.951  15.202  -11.381 1.00 46.23  ? 126 GLN A NE2 1 
ATOM   914  N  N   . MET A 1 128 ? 92.475  11.912  -10.152 1.00 38.02  ? 127 MET A N   1 
ATOM   915  C  CA  . MET A 1 128 ? 91.071  11.916  -10.548 1.00 38.46  ? 127 MET A CA  1 
ATOM   916  C  C   . MET A 1 128 ? 90.303  10.829  -9.814  1.00 38.53  ? 127 MET A C   1 
ATOM   917  O  O   . MET A 1 128 ? 89.187  11.058  -9.337  1.00 40.82  ? 127 MET A O   1 
ATOM   918  C  CB  . MET A 1 128 ? 90.949  11.732  -12.059 1.00 43.86  ? 127 MET A CB  1 
ATOM   919  C  CG  . MET A 1 128 ? 90.960  13.033  -12.841 1.00 48.64  ? 127 MET A CG  1 
ATOM   920  S  SD  . MET A 1 128 ? 91.081  12.749  -14.612 1.00 68.66  ? 127 MET A SD  1 
ATOM   921  C  CE  . MET A 1 128 ? 91.163  14.433  -15.211 1.00 56.75  ? 127 MET A CE  1 
ATOM   922  N  N   . GLY A 1 129 ? 90.885  9.632   -9.717  1.00 38.22  ? 128 GLY A N   1 
ATOM   923  C  CA  . GLY A 1 129 ? 90.250  8.579   -8.947  1.00 39.06  ? 128 GLY A CA  1 
ATOM   924  C  C   . GLY A 1 129 ? 90.169  8.912   -7.473  1.00 36.57  ? 128 GLY A C   1 
ATOM   925  O  O   . GLY A 1 129 ? 89.195  8.555   -6.805  1.00 37.39  ? 128 GLY A O   1 
ATOM   926  N  N   . ILE A 1 130 ? 91.179  9.613   -6.951  1.00 39.16  ? 129 ILE A N   1 
ATOM   927  C  CA  . ILE A 1 130 ? 91.147  10.057  -5.560  1.00 37.90  ? 129 ILE A CA  1 
ATOM   928  C  C   . ILE A 1 130 ? 89.994  11.027  -5.343  1.00 34.21  ? 129 ILE A C   1 
ATOM   929  O  O   . ILE A 1 130 ? 89.194  10.874  -4.412  1.00 37.01  ? 129 ILE A O   1 
ATOM   930  C  CB  . ILE A 1 130 ? 92.490  10.697  -5.174  1.00 34.50  ? 129 ILE A CB  1 
ATOM   931  C  CG1 . ILE A 1 130 ? 93.610  9.664   -5.265  1.00 33.57  ? 129 ILE A CG1 1 
ATOM   932  C  CG2 . ILE A 1 130 ? 92.401  11.303  -3.780  1.00 30.50  ? 129 ILE A CG2 1 
ATOM   933  C  CD1 . ILE A 1 130 ? 94.967  10.207  -4.874  1.00 34.49  ? 129 ILE A CD1 1 
ATOM   934  N  N   . ALA A 1 131 ? 89.893  12.039  -6.208  1.00 33.01  ? 130 ALA A N   1 
ATOM   935  C  CA  . ALA A 1 131 ? 88.833  13.031  -6.077  1.00 36.17  ? 130 ALA A CA  1 
ATOM   936  C  C   . ALA A 1 131 ? 87.459  12.397  -6.246  1.00 32.18  ? 130 ALA A C   1 
ATOM   937  O  O   . ALA A 1 131 ? 86.551  12.659  -5.452  1.00 33.03  ? 130 ALA A O   1 
ATOM   938  C  CB  . ALA A 1 131 ? 89.030  14.152  -7.095  1.00 36.45  ? 130 ALA A CB  1 
ATOM   939  N  N   . TRP A 1 132 ? 87.288  11.556  -7.267  1.00 30.93  ? 131 TRP A N   1 
ATOM   940  C  CA  . TRP A 1 132 ? 85.971  10.978  -7.516  1.00 34.83  ? 131 TRP A CA  1 
ATOM   941  C  C   . TRP A 1 132 ? 85.593  9.970   -6.437  1.00 35.20  ? 131 TRP A C   1 
ATOM   942  O  O   . TRP A 1 132 ? 84.429  9.909   -6.023  1.00 36.57  ? 131 TRP A O   1 
ATOM   943  C  CB  . TRP A 1 132 ? 85.915  10.332  -8.901  1.00 34.93  ? 131 TRP A CB  1 
ATOM   944  C  CG  . TRP A 1 132 ? 84.517  10.247  -9.425  1.00 43.69  ? 131 TRP A CG  1 
ATOM   945  C  CD1 . TRP A 1 132 ? 83.761  9.119   -9.571  1.00 48.39  ? 131 TRP A CD1 1 
ATOM   946  C  CD2 . TRP A 1 132 ? 83.690  11.340  -9.854  1.00 45.29  ? 131 TRP A CD2 1 
ATOM   947  N  NE1 . TRP A 1 132 ? 82.519  9.441   -10.067 1.00 49.63  ? 131 TRP A NE1 1 
ATOM   948  C  CE2 . TRP A 1 132 ? 82.450  10.797  -10.249 1.00 49.80  ? 131 TRP A CE2 1 
ATOM   949  C  CE3 . TRP A 1 132 ? 83.880  12.721  -9.944  1.00 43.62  ? 131 TRP A CE3 1 
ATOM   950  C  CZ2 . TRP A 1 132 ? 81.407  11.587  -10.728 1.00 45.44  ? 131 TRP A CZ2 1 
ATOM   951  C  CZ3 . TRP A 1 132 ? 82.840  13.504  -10.422 1.00 43.45  ? 131 TRP A CZ3 1 
ATOM   952  C  CH2 . TRP A 1 132 ? 81.622  12.935  -10.805 1.00 39.75  ? 131 TRP A CH2 1 
ATOM   953  N  N   . GLY A 1 133 ? 86.556  9.175   -5.967  1.00 31.91  ? 132 GLY A N   1 
ATOM   954  C  CA  . GLY A 1 133 ? 86.271  8.259   -4.874  1.00 30.44  ? 132 GLY A CA  1 
ATOM   955  C  C   . GLY A 1 133 ? 85.867  8.974   -3.598  1.00 35.24  ? 132 GLY A C   1 
ATOM   956  O  O   . GLY A 1 133 ? 84.919  8.568   -2.918  1.00 36.45  ? 132 GLY A O   1 
ATOM   957  N  N   . ASN A 1 134 ? 86.577  10.048  -3.252  1.00 34.45  ? 133 ASN A N   1 
ATOM   958  C  CA  . ASN A 1 134 ? 86.236  10.778  -2.038  1.00 32.30  ? 133 ASN A CA  1 
ATOM   959  C  C   . ASN A 1 134 ? 84.879  11.451  -2.156  1.00 34.53  ? 133 ASN A C   1 
ATOM   960  O  O   . ASN A 1 134 ? 84.186  11.623  -1.148  1.00 34.81  ? 133 ASN A O   1 
ATOM   961  C  CB  . ASN A 1 134 ? 87.315  11.807  -1.723  1.00 33.28  ? 133 ASN A CB  1 
ATOM   962  C  CG  . ASN A 1 134 ? 88.588  11.163  -1.238  1.00 40.93  ? 133 ASN A CG  1 
ATOM   963  O  OD1 . ASN A 1 134 ? 88.634  9.948   -1.042  1.00 45.16  ? 133 ASN A OD1 1 
ATOM   964  N  ND2 . ASN A 1 134 ? 89.633  11.964  -1.050  1.00 38.40  ? 133 ASN A ND2 1 
ATOM   965  N  N   . LEU A 1 135 ? 84.482  11.831  -3.371  1.00 33.05  ? 134 LEU A N   1 
ATOM   966  C  CA  . LEU A 1 135 ? 83.156  12.410  -3.562  1.00 38.17  ? 134 LEU A CA  1 
ATOM   967  C  C   . LEU A 1 135 ? 82.067  11.382  -3.277  1.00 30.85  ? 134 LEU A C   1 
ATOM   968  O  O   . LEU A 1 135 ? 81.099  11.671  -2.567  1.00 31.81  ? 134 LEU A O   1 
ATOM   969  C  CB  . LEU A 1 135 ? 83.023  12.967  -4.980  1.00 31.06  ? 134 LEU A CB  1 
ATOM   970  C  CG  . LEU A 1 135 ? 81.628  13.467  -5.353  1.00 30.70  ? 134 LEU A CG  1 
ATOM   971  C  CD1 . LEU A 1 135 ? 81.274  14.686  -4.517  1.00 32.30  ? 134 LEU A CD1 1 
ATOM   972  C  CD2 . LEU A 1 135 ? 81.533  13.791  -6.845  1.00 30.76  ? 134 LEU A CD2 1 
ATOM   973  N  N   . LEU A 1 136 ? 82.219  10.169  -3.815  1.00 31.65  ? 135 LEU A N   1 
ATOM   974  C  CA  . LEU A 1 136 ? 81.215  9.130   -3.605  1.00 32.54  ? 135 LEU A CA  1 
ATOM   975  C  C   . LEU A 1 136 ? 81.094  8.766   -2.128  1.00 33.04  ? 135 LEU A C   1 
ATOM   976  O  O   . LEU A 1 136 ? 79.987  8.553   -1.622  1.00 37.22  ? 135 LEU A O   1 
ATOM   977  C  CB  . LEU A 1 136 ? 81.560  7.896   -4.441  1.00 33.02  ? 135 LEU A CB  1 
ATOM   978  C  CG  . LEU A 1 136 ? 81.706  8.117   -5.953  1.00 38.00  ? 135 LEU A CG  1 
ATOM   979  C  CD1 . LEU A 1 136 ? 82.162  6.847   -6.658  1.00 33.07  ? 135 LEU A CD1 1 
ATOM   980  C  CD2 . LEU A 1 136 ? 80.407  8.624   -6.561  1.00 40.45  ? 135 LEU A CD2 1 
ATOM   981  N  N   . LEU A 1 137 ? 82.220  8.695   -1.418  1.00 32.87  ? 136 LEU A N   1 
ATOM   982  C  CA  . LEU A 1 137 ? 82.173  8.442   0.018   1.00 34.06  ? 136 LEU A CA  1 
ATOM   983  C  C   . LEU A 1 137 ? 81.454  9.567   0.748   1.00 35.12  ? 136 LEU A C   1 
ATOM   984  O  O   . LEU A 1 137 ? 80.631  9.315   1.637   1.00 35.04  ? 136 LEU A O   1 
ATOM   985  C  CB  . LEU A 1 137 ? 83.588  8.268   0.571   1.00 31.78  ? 136 LEU A CB  1 
ATOM   986  C  CG  . LEU A 1 137 ? 84.345  7.039   0.059   1.00 34.19  ? 136 LEU A CG  1 
ATOM   987  C  CD1 . LEU A 1 137 ? 85.830  7.140   0.381   1.00 31.51  ? 136 LEU A CD1 1 
ATOM   988  C  CD2 . LEU A 1 137 ? 83.746  5.768   0.633   1.00 29.55  ? 136 LEU A CD2 1 
ATOM   989  N  N   . ALA A 1 138 ? 81.750  10.816  0.377   1.00 34.14  ? 137 ALA A N   1 
ATOM   990  C  CA  . ALA A 1 138 ? 81.100  11.959  1.006   1.00 30.26  ? 137 ALA A CA  1 
ATOM   991  C  C   . ALA A 1 138 ? 79.599  11.960  0.741   1.00 33.91  ? 137 ALA A C   1 
ATOM   992  O  O   . ALA A 1 138 ? 78.815  12.365  1.608   1.00 31.49  ? 137 ALA A O   1 
ATOM   993  C  CB  . ALA A 1 138 ? 81.737  13.254  0.513   1.00 31.10  ? 137 ALA A CB  1 
ATOM   994  N  N   . LEU A 1 139 ? 79.182  11.506  -0.444  1.00 31.60  ? 138 LEU A N   1 
ATOM   995  C  CA  . LEU A 1 139 ? 77.758  11.338  -0.720  1.00 33.20  ? 138 LEU A CA  1 
ATOM   996  C  C   . LEU A 1 139 ? 77.131  10.343  0.242   1.00 34.47  ? 138 LEU A C   1 
ATOM   997  O  O   . LEU A 1 139 ? 76.066  10.599  0.814   1.00 34.22  ? 138 LEU A O   1 
ATOM   998  C  CB  . LEU A 1 139 ? 77.537  10.866  -2.156  1.00 35.30  ? 138 LEU A CB  1 
ATOM   999  C  CG  . LEU A 1 139 ? 77.753  11.826  -3.314  1.00 35.35  ? 138 LEU A CG  1 
ATOM   1000 C  CD1 . LEU A 1 139 ? 77.530  11.075  -4.620  1.00 38.43  ? 138 LEU A CD1 1 
ATOM   1001 C  CD2 . LEU A 1 139 ? 76.807  12.999  -3.202  1.00 32.98  ? 138 LEU A CD2 1 
ATOM   1002 N  N   . MET A 1 140 ? 77.764  9.178   0.403   1.00 34.92  ? 139 MET A N   1 
ATOM   1003 C  CA  . MET A 1 140 ? 77.230  8.181   1.322   1.00 35.80  ? 139 MET A CA  1 
ATOM   1004 C  C   . MET A 1 140 ? 77.125  8.746   2.730   1.00 29.25  ? 139 MET A C   1 
ATOM   1005 O  O   . MET A 1 140 ? 76.125  8.530   3.421   1.00 34.25  ? 139 MET A O   1 
ATOM   1006 C  CB  . MET A 1 140 ? 78.105  6.929   1.315   1.00 32.23  ? 139 MET A CB  1 
ATOM   1007 C  CG  . MET A 1 140 ? 78.324  6.312   -0.050  1.00 32.62  ? 139 MET A CG  1 
ATOM   1008 S  SD  . MET A 1 140 ? 79.290  4.794   0.106   1.00 43.47  ? 139 MET A SD  1 
ATOM   1009 C  CE  . MET A 1 140 ? 79.588  4.392   -1.612  1.00 36.70  ? 139 MET A CE  1 
ATOM   1010 N  N   . LYS A 1 141 ? 78.147  9.482   3.167   1.00 31.78  ? 140 LYS A N   1 
ATOM   1011 C  CA  . LYS A 1 141 ? 78.108  10.089  4.491   1.00 28.73  ? 140 LYS A CA  1 
ATOM   1012 C  C   . LYS A 1 141 ? 76.967  11.086  4.605   1.00 31.05  ? 140 LYS A C   1 
ATOM   1013 O  O   . LYS A 1 141 ? 76.395  11.253  5.690   1.00 33.18  ? 140 LYS A O   1 
ATOM   1014 C  CB  . LYS A 1 141 ? 79.441  10.769  4.801   1.00 30.06  ? 140 LYS A CB  1 
ATOM   1015 C  CG  . LYS A 1 141 ? 80.632  9.815   4.915   1.00 31.33  ? 140 LYS A CG  1 
ATOM   1016 C  CD  . LYS A 1 141 ? 81.875  10.578  5.359   1.00 30.54  ? 140 LYS A CD  1 
ATOM   1017 C  CE  . LYS A 1 141 ? 83.148  9.891   4.930   1.00 34.29  ? 140 LYS A CE  1 
ATOM   1018 N  NZ  . LYS A 1 141 ? 84.329  10.434  5.672   1.00 34.64  ? 140 LYS A NZ  1 
ATOM   1019 N  N   . GLY A 1 142 ? 76.622  11.761  3.502   1.00 31.01  ? 141 GLY A N   1 
ATOM   1020 C  CA  . GLY A 1 142 ? 75.480  12.658  3.527   1.00 29.85  ? 141 GLY A CA  1 
ATOM   1021 C  C   . GLY A 1 142 ? 74.184  11.935  3.826   1.00 34.82  ? 141 GLY A C   1 
ATOM   1022 O  O   . GLY A 1 142 ? 73.248  12.524  4.378   1.00 35.89  ? 141 GLY A O   1 
ATOM   1023 N  N   . PHE A 1 143 ? 74.113  10.652  3.470   1.00 34.60  ? 142 PHE A N   1 
ATOM   1024 C  CA  . PHE A 1 143 ? 72.987  9.787   3.780   1.00 33.41  ? 142 PHE A CA  1 
ATOM   1025 C  C   . PHE A 1 143 ? 73.189  9.016   5.080   1.00 33.73  ? 142 PHE A C   1 
ATOM   1026 O  O   . PHE A 1 143 ? 72.343  8.188   5.434   1.00 34.28  ? 142 PHE A O   1 
ATOM   1027 C  CB  . PHE A 1 143 ? 72.748  8.814   2.623   1.00 35.62  ? 142 PHE A CB  1 
ATOM   1028 C  CG  . PHE A 1 143 ? 71.988  9.415   1.471   1.00 35.93  ? 142 PHE A CG  1 
ATOM   1029 C  CD1 . PHE A 1 143 ? 70.602  9.426   1.472   1.00 36.99  ? 142 PHE A CD1 1 
ATOM   1030 C  CD2 . PHE A 1 143 ? 72.660  9.973   0.392   1.00 31.94  ? 142 PHE A CD2 1 
ATOM   1031 C  CE1 . PHE A 1 143 ? 69.895  9.982   0.420   1.00 39.55  ? 142 PHE A CE1 1 
ATOM   1032 C  CE2 . PHE A 1 143 ? 71.960  10.528  -0.669  1.00 34.99  ? 142 PHE A CE2 1 
ATOM   1033 C  CZ  . PHE A 1 143 ? 70.575  10.534  -0.654  1.00 39.12  ? 142 PHE A CZ  1 
ATOM   1034 N  N   . ARG A 1 144 ? 74.284  9.279   5.799   1.00 30.93  ? 143 ARG A N   1 
ATOM   1035 C  CA  . ARG A 1 144 ? 74.617  8.577   7.042   1.00 34.92  ? 143 ARG A CA  1 
ATOM   1036 C  C   . ARG A 1 144 ? 74.751  7.071   6.816   1.00 34.49  ? 143 ARG A C   1 
ATOM   1037 O  O   . ARG A 1 144 ? 74.442  6.269   7.700   1.00 35.22  ? 143 ARG A O   1 
ATOM   1038 C  CB  . ARG A 1 144 ? 73.587  8.865   8.143   1.00 28.44  ? 143 ARG A CB  1 
ATOM   1039 C  CG  . ARG A 1 144 ? 73.365  10.342  8.435   1.00 34.86  ? 143 ARG A CG  1 
ATOM   1040 C  CD  . ARG A 1 144 ? 72.725  10.574  9.811   1.00 35.03  ? 143 ARG A CD  1 
ATOM   1041 N  NE  . ARG A 1 144 ? 71.339  10.123  9.836   1.00 39.44  ? 143 ARG A NE  1 
ATOM   1042 C  CZ  . ARG A 1 144 ? 70.507  10.269  10.860  1.00 47.31  ? 143 ARG A CZ  1 
ATOM   1043 N  NH1 . ARG A 1 144 ? 70.881  10.870  11.980  1.00 38.84  ? 143 ARG A NH1 1 
ATOM   1044 N  NH2 . ARG A 1 144 ? 69.268  9.798   10.759  1.00 32.51  ? 143 ARG A NH2 1 
ATOM   1045 N  N   . ASP A 1 145 ? 75.204  6.674   5.625   1.00 32.52  ? 144 ASP A N   1 
ATOM   1046 C  CA  . ASP A 1 145 ? 75.372  5.260   5.281   1.00 33.93  ? 144 ASP A CA  1 
ATOM   1047 C  C   . ASP A 1 145 ? 76.743  4.801   5.773   1.00 33.85  ? 144 ASP A C   1 
ATOM   1048 O  O   . ASP A 1 145 ? 77.704  4.670   5.014   1.00 33.32  ? 144 ASP A O   1 
ATOM   1049 C  CB  . ASP A 1 145 ? 75.209  5.053   3.779   1.00 32.80  ? 144 ASP A CB  1 
ATOM   1050 C  CG  . ASP A 1 145 ? 75.046  3.589   3.401   1.00 32.62  ? 144 ASP A CG  1 
ATOM   1051 O  OD1 . ASP A 1 145 ? 75.209  2.714   4.276   1.00 37.28  ? 144 ASP A OD1 1 
ATOM   1052 O  OD2 . ASP A 1 145 ? 74.754  3.310   2.220   1.00 39.42  ? 144 ASP A OD2 1 
ATOM   1053 N  N   . ALA A 1 146 ? 76.829  4.563   7.084   1.00 32.55  ? 145 ALA A N   1 
ATOM   1054 C  CA  . ALA A 1 146 ? 78.097  4.138   7.671   1.00 32.18  ? 145 ALA A CA  1 
ATOM   1055 C  C   . ALA A 1 146 ? 78.561  2.805   7.101   1.00 30.45  ? 145 ALA A C   1 
ATOM   1056 O  O   . ALA A 1 146 ? 79.768  2.577   6.964   1.00 29.91  ? 145 ALA A O   1 
ATOM   1057 C  CB  . ALA A 1 146 ? 77.968  4.048   9.193   1.00 33.40  ? 145 ALA A CB  1 
ATOM   1058 N  N   . ALA A 1 147 ? 77.623  1.922   6.756   1.00 33.03  ? 146 ALA A N   1 
ATOM   1059 C  CA  . ALA A 1 147 ? 77.986  0.602   6.251   1.00 34.92  ? 146 ALA A CA  1 
ATOM   1060 C  C   . ALA A 1 147 ? 78.535  0.686   4.833   1.00 31.64  ? 146 ALA A C   1 
ATOM   1061 O  O   . ALA A 1 147 ? 79.556  0.064   4.517   1.00 34.50  ? 146 ALA A O   1 
ATOM   1062 C  CB  . ALA A 1 147 ? 76.779  -0.339  6.305   1.00 32.57  ? 146 ALA A CB  1 
ATOM   1063 N  N   . GLY A 1 148 ? 77.863  1.442   3.960   1.00 31.83  ? 147 GLY A N   1 
ATOM   1064 C  CA  . GLY A 1 148 ? 78.376  1.625   2.611   1.00 28.66  ? 147 GLY A CA  1 
ATOM   1065 C  C   . GLY A 1 148 ? 79.739  2.286   2.599   1.00 32.82  ? 147 GLY A C   1 
ATOM   1066 O  O   . GLY A 1 148 ? 80.642  1.862   1.871   1.00 33.23  ? 147 GLY A O   1 
ATOM   1067 N  N   . ASN A 1 149 ? 79.910  3.327   3.416   1.00 28.74  ? 148 ASN A N   1 
ATOM   1068 C  CA  . ASN A 1 149 ? 81.205  3.989   3.533   1.00 31.07  ? 148 ASN A CA  1 
ATOM   1069 C  C   . ASN A 1 149 ? 82.277  3.005   3.990   1.00 31.29  ? 148 ASN A C   1 
ATOM   1070 O  O   . ASN A 1 149 ? 83.330  2.876   3.354   1.00 32.17  ? 148 ASN A O   1 
ATOM   1071 C  CB  . ASN A 1 149 ? 81.080  5.175   4.497   1.00 30.23  ? 148 ASN A CB  1 
ATOM   1072 C  CG  . ASN A 1 149 ? 82.407  5.862   4.773   1.00 36.09  ? 148 ASN A CG  1 
ATOM   1073 O  OD1 . ASN A 1 149 ? 82.916  6.613   3.943   1.00 34.74  ? 148 ASN A OD1 1 
ATOM   1074 N  ND2 . ASN A 1 149 ? 82.957  5.629   5.960   1.00 35.11  ? 148 ASN A ND2 1 
ATOM   1075 N  N   . ALA A 1 150 ? 82.001  2.263   5.069   1.00 30.91  ? 149 ALA A N   1 
ATOM   1076 C  CA  . ALA A 1 150 ? 82.994  1.341   5.617   1.00 32.84  ? 149 ALA A CA  1 
ATOM   1077 C  C   . ALA A 1 150 ? 83.293  0.194   4.656   1.00 29.79  ? 149 ALA A C   1 
ATOM   1078 O  O   . ALA A 1 150 ? 84.456  -0.169  4.457   1.00 33.37  ? 149 ALA A O   1 
ATOM   1079 C  CB  . ALA A 1 150 ? 82.517  0.801   6.965   1.00 31.16  ? 149 ALA A CB  1 
ATOM   1080 N  N   . LEU A 1 151 ? 82.261  -0.397  4.056   1.00 31.67  ? 150 LEU A N   1 
ATOM   1081 C  CA  . LEU A 1 151 ? 82.496  -1.490  3.115   1.00 35.85  ? 150 LEU A CA  1 
ATOM   1082 C  C   . LEU A 1 151 ? 83.301  -1.017  1.911   1.00 31.54  ? 150 LEU A C   1 
ATOM   1083 O  O   . LEU A 1 151 ? 84.168  -1.742  1.414   1.00 32.00  ? 150 LEU A O   1 
ATOM   1084 C  CB  . LEU A 1 151 ? 81.163  -2.103  2.678   1.00 28.96  ? 150 LEU A CB  1 
ATOM   1085 C  CG  . LEU A 1 151 ? 80.470  -2.893  3.792   1.00 38.84  ? 150 LEU A CG  1 
ATOM   1086 C  CD1 . LEU A 1 151 ? 78.961  -2.970  3.560   1.00 36.18  ? 150 LEU A CD1 1 
ATOM   1087 C  CD2 . LEU A 1 151 ? 81.064  -4.295  3.947   1.00 37.72  ? 150 LEU A CD2 1 
ATOM   1088 N  N   . SER A 1 152 ? 83.044  0.203   1.439   1.00 32.62  ? 151 SER A N   1 
ATOM   1089 C  CA  . SER A 1 152 ? 83.804  0.725   0.308   1.00 33.92  ? 151 SER A CA  1 
ATOM   1090 C  C   . SER A 1 152 ? 85.279  0.860   0.657   1.00 33.74  ? 151 SER A C   1 
ATOM   1091 O  O   . SER A 1 152 ? 86.149  0.393   -0.088  1.00 31.01  ? 151 SER A O   1 
ATOM   1092 C  CB  . SER A 1 152 ? 83.228  2.066   -0.135  1.00 25.34  ? 151 SER A CB  1 
ATOM   1093 O  OG  . SER A 1 152 ? 81.950  1.876   -0.696  1.00 31.35  ? 151 SER A OG  1 
ATOM   1094 N  N   . LEU A 1 153 ? 85.577  1.494   1.795   1.00 32.19  ? 152 LEU A N   1 
ATOM   1095 C  CA  . LEU A 1 153 ? 86.962  1.680   2.211   1.00 27.65  ? 152 LEU A CA  1 
ATOM   1096 C  C   . LEU A 1 153 ? 87.659  0.349   2.466   1.00 30.20  ? 152 LEU A C   1 
ATOM   1097 O  O   . LEU A 1 153 ? 88.854  0.212   2.175   1.00 30.48  ? 152 LEU A O   1 
ATOM   1098 C  CB  . LEU A 1 153 ? 87.011  2.556   3.462   1.00 31.46  ? 152 LEU A CB  1 
ATOM   1099 C  CG  . LEU A 1 153 ? 86.556  4.006   3.258   1.00 34.20  ? 152 LEU A CG  1 
ATOM   1100 C  CD1 . LEU A 1 153 ? 86.265  4.684   4.588   1.00 34.93  ? 152 LEU A CD1 1 
ATOM   1101 C  CD2 . LEU A 1 153 ? 87.595  4.796   2.463   1.00 31.44  ? 152 LEU A CD2 1 
ATOM   1102 N  N   . ILE A 1 154 ? 86.935  -0.640  2.998   1.00 31.53  ? 153 ILE A N   1 
ATOM   1103 C  CA  . ILE A 1 154 ? 87.551  -1.937  3.268   1.00 33.26  ? 153 ILE A CA  1 
ATOM   1104 C  C   . ILE A 1 154 ? 87.961  -2.612  1.965   1.00 33.95  ? 153 ILE A C   1 
ATOM   1105 O  O   . ILE A 1 154 ? 89.102  -3.064  1.815   1.00 36.09  ? 153 ILE A O   1 
ATOM   1106 C  CB  . ILE A 1 154 ? 86.606  -2.828  4.094   1.00 30.88  ? 153 ILE A CB  1 
ATOM   1107 C  CG1 . ILE A 1 154 ? 86.578  -2.366  5.551   1.00 28.94  ? 153 ILE A CG1 1 
ATOM   1108 C  CG2 . ILE A 1 154 ? 87.050  -4.279  4.013   1.00 32.26  ? 153 ILE A CG2 1 
ATOM   1109 C  CD1 . ILE A 1 154 ? 85.293  -2.724  6.284   1.00 30.48  ? 153 ILE A CD1 1 
ATOM   1110 N  N   . VAL A 1 155 ? 87.043  -2.680  0.999   1.00 31.44  ? 154 VAL A N   1 
ATOM   1111 C  CA  . VAL A 1 155 ? 87.381  -3.273  -0.291  1.00 32.29  ? 154 VAL A CA  1 
ATOM   1112 C  C   . VAL A 1 155 ? 88.534  -2.516  -0.936  1.00 38.32  ? 154 VAL A C   1 
ATOM   1113 O  O   . VAL A 1 155 ? 89.449  -3.118  -1.511  1.00 35.67  ? 154 VAL A O   1 
ATOM   1114 C  CB  . VAL A 1 155 ? 86.142  -3.309  -1.205  1.00 30.04  ? 154 VAL A CB  1 
ATOM   1115 C  CG1 . VAL A 1 155 ? 86.529  -3.723  -2.622  1.00 30.27  ? 154 VAL A CG1 1 
ATOM   1116 C  CG2 . VAL A 1 155 ? 85.113  -4.265  -0.639  1.00 34.52  ? 154 VAL A CG2 1 
ATOM   1117 N  N   . GLY A 1 156 ? 88.520  -1.185  -0.827  1.00 35.81  ? 155 GLY A N   1 
ATOM   1118 C  CA  . GLY A 1 156 ? 89.561  -0.388  -1.450  1.00 34.79  ? 155 GLY A CA  1 
ATOM   1119 C  C   . GLY A 1 156 ? 90.929  -0.611  -0.834  1.00 39.22  ? 155 GLY A C   1 
ATOM   1120 O  O   . GLY A 1 156 ? 91.933  -0.685  -1.548  1.00 38.89  ? 155 GLY A O   1 
ATOM   1121 N  N   . SER A 1 157 ? 90.993  -0.713  0.498   1.00 37.19  ? 156 SER A N   1 
ATOM   1122 C  CA  . SER A 1 157 ? 92.268  -0.999  1.147   1.00 34.31  ? 156 SER A CA  1 
ATOM   1123 C  C   . SER A 1 157 ? 92.817  -2.344  0.694   1.00 35.09  ? 156 SER A C   1 
ATOM   1124 O  O   . SER A 1 157 ? 93.999  -2.458  0.350   1.00 36.45  ? 156 SER A O   1 
ATOM   1125 C  CB  . SER A 1 157 ? 92.114  -0.974  2.667   1.00 32.98  ? 156 SER A CB  1 
ATOM   1126 O  OG  . SER A 1 157 ? 91.693  0.302   3.111   1.00 39.03  ? 156 SER A OG  1 
ATOM   1127 N  N   . LEU A 1 158 ? 91.968  -3.371  0.667   1.00 39.57  ? 157 LEU A N   1 
ATOM   1128 C  CA  . LEU A 1 158 ? 92.448  -4.707  0.330   1.00 37.36  ? 157 LEU A CA  1 
ATOM   1129 C  C   . LEU A 1 158 ? 92.893  -4.782  -1.124  1.00 37.26  ? 157 LEU A C   1 
ATOM   1130 O  O   . LEU A 1 158 ? 93.947  -5.349  -1.426  1.00 42.58  ? 157 LEU A O   1 
ATOM   1131 C  CB  . LEU A 1 158 ? 91.368  -5.744  0.627   1.00 33.89  ? 157 LEU A CB  1 
ATOM   1132 C  CG  . LEU A 1 158 ? 90.917  -5.773  2.091   1.00 38.23  ? 157 LEU A CG  1 
ATOM   1133 C  CD1 . LEU A 1 158 ? 90.085  -7.012  2.393   1.00 42.57  ? 157 LEU A CD1 1 
ATOM   1134 C  CD2 . LEU A 1 158 ? 92.112  -5.704  3.009   1.00 38.81  ? 157 LEU A CD2 1 
ATOM   1135 N  N   . ILE A 1 159 ? 92.119  -4.200  -2.042  1.00 38.20  ? 158 ILE A N   1 
ATOM   1136 C  CA  . ILE A 1 159 ? 92.575  -4.182  -3.426  1.00 41.39  ? 158 ILE A CA  1 
ATOM   1137 C  C   . ILE A 1 159 ? 93.777  -3.259  -3.578  1.00 40.13  ? 158 ILE A C   1 
ATOM   1138 O  O   . ILE A 1 159 ? 94.623  -3.469  -4.455  1.00 40.67  ? 158 ILE A O   1 
ATOM   1139 C  CB  . ILE A 1 159 ? 91.425  -3.794  -4.377  1.00 41.75  ? 158 ILE A CB  1 
ATOM   1140 C  CG1 . ILE A 1 159 ? 91.018  -2.336  -4.182  1.00 42.78  ? 158 ILE A CG1 1 
ATOM   1141 C  CG2 . ILE A 1 159 ? 90.234  -4.713  -4.169  1.00 40.86  ? 158 ILE A CG2 1 
ATOM   1142 C  CD1 . ILE A 1 159 ? 89.709  -1.977  -4.878  1.00 43.53  ? 158 ILE A CD1 1 
ATOM   1143 N  N   . GLY A 1 160 ? 93.894  -2.246  -2.719  1.00 38.00  ? 159 GLY A N   1 
ATOM   1144 C  CA  . GLY A 1 160 ? 95.052  -1.373  -2.787  1.00 37.35  ? 159 GLY A CA  1 
ATOM   1145 C  C   . GLY A 1 160 ? 96.340  -2.098  -2.453  1.00 40.02  ? 159 GLY A C   1 
ATOM   1146 O  O   . GLY A 1 160 ? 97.362  -1.906  -3.117  1.00 43.62  ? 159 GLY A O   1 
ATOM   1147 N  N   . VAL A 1 161 ? 96.308  -2.944  -1.422  1.00 39.55  ? 160 VAL A N   1 
ATOM   1148 C  CA  . VAL A 1 161 ? 97.482  -3.735  -1.070  1.00 37.89  ? 160 VAL A CA  1 
ATOM   1149 C  C   . VAL A 1 161 ? 97.861  -4.665  -2.214  1.00 45.09  ? 160 VAL A C   1 
ATOM   1150 O  O   . VAL A 1 161 ? 99.042  -4.801  -2.562  1.00 43.03  ? 160 VAL A O   1 
ATOM   1151 C  CB  . VAL A 1 161 ? 97.224  -4.513  0.231   1.00 41.03  ? 160 VAL A CB  1 
ATOM   1152 C  CG1 . VAL A 1 161 ? 98.247  -5.626  0.395   1.00 35.06  ? 160 VAL A CG1 1 
ATOM   1153 C  CG2 . VAL A 1 161 ? 97.246  -3.562  1.415   1.00 37.82  ? 160 VAL A CG2 1 
ATOM   1154 N  N   . LEU A 1 162 ? 96.867  -5.321  -2.818  1.00 41.38  ? 161 LEU A N   1 
ATOM   1155 C  CA  . LEU A 1 162 ? 97.153  -6.176  -3.963  1.00 43.57  ? 161 LEU A CA  1 
ATOM   1156 C  C   . LEU A 1 162 ? 97.761  -5.372  -5.106  1.00 45.49  ? 161 LEU A C   1 
ATOM   1157 O  O   . LEU A 1 162 ? 98.762  -5.789  -5.704  1.00 41.77  ? 161 LEU A O   1 
ATOM   1158 C  CB  . LEU A 1 162 ? 95.878  -6.890  -4.413  1.00 43.06  ? 161 LEU A CB  1 
ATOM   1159 C  CG  . LEU A 1 162 ? 95.209  -7.783  -3.361  1.00 47.11  ? 161 LEU A CG  1 
ATOM   1160 C  CD1 . LEU A 1 162 ? 94.016  -8.524  -3.946  1.00 51.79  ? 161 LEU A CD1 1 
ATOM   1161 C  CD2 . LEU A 1 162 ? 96.199  -8.764  -2.747  1.00 44.52  ? 161 LEU A CD2 1 
ATOM   1162 N  N   . ALA A 1 163 ? 97.189  -4.200  -5.404  1.00 43.75  ? 162 ALA A N   1 
ATOM   1163 C  CA  . ALA A 1 163 ? 97.717  -3.373  -6.486  1.00 41.77  ? 162 ALA A CA  1 
ATOM   1164 C  C   . ALA A 1 163 ? 99.136  -2.907  -6.188  1.00 42.09  ? 162 ALA A C   1 
ATOM   1165 O  O   . ALA A 1 163 ? 99.991  -2.890  -7.082  1.00 42.81  ? 162 ALA A O   1 
ATOM   1166 C  CB  . ALA A 1 163 ? 96.804  -2.175  -6.729  1.00 38.28  ? 162 ALA A CB  1 
ATOM   1167 N  N   . TYR A 1 164 ? 99.409  -2.527  -4.936  1.00 39.35  ? 163 TYR A N   1 
ATOM   1168 C  CA  . TYR A 1 164 ? 100.763 -2.132  -4.568  1.00 37.97  ? 163 TYR A CA  1 
ATOM   1169 C  C   . TYR A 1 164 ? 101.750 -3.276  -4.778  1.00 46.60  ? 163 TYR A C   1 
ATOM   1170 O  O   . TYR A 1 164 ? 102.863 -3.058  -5.269  1.00 40.29  ? 163 TYR A O   1 
ATOM   1171 C  CB  . TYR A 1 164 ? 100.800 -1.656  -3.116  1.00 40.98  ? 163 TYR A CB  1 
ATOM   1172 C  CG  . TYR A 1 164 ? 102.199 -1.463  -2.584  1.00 41.96  ? 163 TYR A CG  1 
ATOM   1173 C  CD1 . TYR A 1 164 ? 102.878 -0.267  -2.781  1.00 42.43  ? 163 TYR A CD1 1 
ATOM   1174 C  CD2 . TYR A 1 164 ? 102.848 -2.481  -1.892  1.00 48.10  ? 163 TYR A CD2 1 
ATOM   1175 C  CE1 . TYR A 1 164 ? 104.163 -0.088  -2.299  1.00 42.01  ? 163 TYR A CE1 1 
ATOM   1176 C  CE2 . TYR A 1 164 ? 104.135 -2.314  -1.412  1.00 47.03  ? 163 TYR A CE2 1 
ATOM   1177 C  CZ  . TYR A 1 164 ? 104.786 -1.114  -1.618  1.00 46.57  ? 163 TYR A CZ  1 
ATOM   1178 O  OH  . TYR A 1 164 ? 106.062 -0.941  -1.138  1.00 47.38  ? 163 TYR A OH  1 
ATOM   1179 N  N   . TYR A 1 165 ? 101.361 -4.502  -4.413  1.00 44.34  ? 164 TYR A N   1 
ATOM   1180 C  CA  . TYR A 1 165 ? 102.258 -5.647  -4.571  1.00 45.03  ? 164 TYR A CA  1 
ATOM   1181 C  C   . TYR A 1 165 ? 102.625 -5.864  -6.032  1.00 43.81  ? 164 TYR A C   1 
ATOM   1182 O  O   . TYR A 1 165 ? 103.805 -5.990  -6.376  1.00 46.27  ? 164 TYR A O   1 
ATOM   1183 C  CB  . TYR A 1 165 ? 101.622 -6.917  -4.000  1.00 49.67  ? 164 TYR A CB  1 
ATOM   1184 C  CG  . TYR A 1 165 ? 102.604 -8.057  -3.855  1.00 50.20  ? 164 TYR A CG  1 
ATOM   1185 C  CD1 . TYR A 1 165 ? 103.545 -8.066  -2.839  1.00 58.54  ? 164 TYR A CD1 1 
ATOM   1186 C  CD2 . TYR A 1 165 ? 102.614 -9.106  -4.764  1.00 60.08  ? 164 TYR A CD2 1 
ATOM   1187 C  CE1 . TYR A 1 165 ? 104.455 -9.101  -2.712  1.00 64.23  ? 164 TYR A CE1 1 
ATOM   1188 C  CE2 . TYR A 1 165 ? 103.525 -10.148 -4.647  1.00 66.95  ? 164 TYR A CE2 1 
ATOM   1189 C  CZ  . TYR A 1 165 ? 104.445 -10.137 -3.619  1.00 66.81  ? 164 TYR A CZ  1 
ATOM   1190 O  OH  . TYR A 1 165 ? 105.356 -11.160 -3.486  1.00 69.92  ? 164 TYR A OH  1 
ATOM   1191 N  N   . VAL A 1 166 ? 101.620 -5.935  -6.904  1.00 42.79  ? 165 VAL A N   1 
ATOM   1192 C  CA  . VAL A 1 166 ? 101.885 -6.109  -8.329  1.00 44.78  ? 165 VAL A CA  1 
ATOM   1193 C  C   . VAL A 1 166 ? 102.706 -4.941  -8.860  1.00 41.89  ? 165 VAL A C   1 
ATOM   1194 O  O   . VAL A 1 166 ? 103.638 -5.125  -9.651  1.00 50.54  ? 165 VAL A O   1 
ATOM   1195 C  CB  . VAL A 1 166 ? 100.556 -6.268  -9.092  1.00 46.31  ? 165 VAL A CB  1 
ATOM   1196 C  CG1 . VAL A 1 166 ? 100.797 -6.376  -10.590 1.00 42.72  ? 165 VAL A CG1 1 
ATOM   1197 C  CG2 . VAL A 1 166 ? 99.796  -7.477  -8.572  1.00 43.95  ? 165 VAL A CG2 1 
ATOM   1198 N  N   . SER A 1 167 ? 102.400 -3.725  -8.400  1.00 40.70  ? 166 SER A N   1 
ATOM   1199 C  CA  . SER A 1 167 ? 103.027 -2.535  -8.963  1.00 42.29  ? 166 SER A CA  1 
ATOM   1200 C  C   . SER A 1 167 ? 104.515 -2.470  -8.629  1.00 46.91  ? 166 SER A C   1 
ATOM   1201 O  O   . SER A 1 167 ? 105.338 -2.153  -9.498  1.00 42.09  ? 166 SER A O   1 
ATOM   1202 C  CB  . SER A 1 167 ? 102.306 -1.282  -8.465  1.00 39.95  ? 166 SER A CB  1 
ATOM   1203 O  OG  . SER A 1 167 ? 102.723 -0.135  -9.184  1.00 47.77  ? 166 SER A OG  1 
ATOM   1204 N  N   . TYR A 1 168 ? 104.891 -2.759  -7.383  1.00 39.95  ? 167 TYR A N   1 
ATOM   1205 C  CA  . TYR A 1 168 ? 106.305 -2.677  -7.054  1.00 43.69  ? 167 TYR A CA  1 
ATOM   1206 C  C   . TYR A 1 168 ? 107.072 -3.893  -7.561  1.00 48.34  ? 167 TYR A C   1 
ATOM   1207 O  O   . TYR A 1 168 ? 108.246 -3.769  -7.923  1.00 50.87  ? 167 TYR A O   1 
ATOM   1208 C  CB  . TYR A 1 168 ? 106.485 -2.489  -5.545  1.00 46.41  ? 167 TYR A CB  1 
ATOM   1209 C  CG  . TYR A 1 168 ? 106.570 -3.750  -4.715  1.00 50.25  ? 167 TYR A CG  1 
ATOM   1210 C  CD1 . TYR A 1 168 ? 105.459 -4.227  -4.038  1.00 55.59  ? 167 TYR A CD1 1 
ATOM   1211 C  CD2 . TYR A 1 168 ? 107.776 -4.432  -4.563  1.00 53.10  ? 167 TYR A CD2 1 
ATOM   1212 C  CE1 . TYR A 1 168 ? 105.533 -5.361  -3.263  1.00 57.03  ? 167 TYR A CE1 1 
ATOM   1213 C  CE2 . TYR A 1 168 ? 107.856 -5.572  -3.795  1.00 48.83  ? 167 TYR A CE2 1 
ATOM   1214 C  CZ  . TYR A 1 168 ? 106.733 -6.031  -3.146  1.00 58.03  ? 167 TYR A CZ  1 
ATOM   1215 O  OH  . TYR A 1 168 ? 106.816 -7.163  -2.375  1.00 81.58  ? 167 TYR A OH  1 
ATOM   1216 N  N   . ARG A 1 169 ? 106.435 -5.066  -7.598  1.00 48.58  ? 168 ARG A N   1 
ATOM   1217 C  CA  . ARG A 1 169 ? 107.095 -6.239  -8.164  1.00 45.64  ? 168 ARG A CA  1 
ATOM   1218 C  C   . ARG A 1 169 ? 107.365 -6.045  -9.647  1.00 47.85  ? 168 ARG A C   1 
ATOM   1219 O  O   . ARG A 1 169 ? 108.392 -6.495  -10.163 1.00 58.03  ? 168 ARG A O   1 
ATOM   1220 C  CB  . ARG A 1 169 ? 106.239 -7.487  -7.944  1.00 48.40  ? 168 ARG A CB  1 
ATOM   1221 C  CG  . ARG A 1 169 ? 106.265 -8.025  -6.524  1.00 57.49  ? 168 ARG A CG  1 
ATOM   1222 C  CD  . ARG A 1 169 ? 107.643 -8.528  -6.156  1.00 51.13  ? 168 ARG A CD  1 
ATOM   1223 N  NE  . ARG A 1 169 ? 107.979 -9.756  -6.866  1.00 55.06  ? 168 ARG A NE  1 
ATOM   1224 C  CZ  . ARG A 1 169 ? 108.333 -10.889 -6.276  1.00 67.14  ? 168 ARG A CZ  1 
ATOM   1225 N  NH1 . ARG A 1 169 ? 108.394 -10.993 -4.958  1.00 68.81  ? 168 ARG A NH1 1 
ATOM   1226 N  NH2 . ARG A 1 169 ? 108.640 -11.944 -7.027  1.00 60.15  ? 168 ARG A NH2 1 
ATOM   1227 N  N   . LEU A 1 170 ? 106.454 -5.373  -10.346 1.00 51.88  ? 169 LEU A N   1 
ATOM   1228 C  CA  . LEU A 1 170 ? 106.630 -5.141  -11.774 1.00 48.54  ? 169 LEU A CA  1 
ATOM   1229 C  C   . LEU A 1 170 ? 107.614 -4.007  -12.029 1.00 51.48  ? 169 LEU A C   1 
ATOM   1230 O  O   . LEU A 1 170 ? 108.570 -4.168  -12.795 1.00 47.68  ? 169 LEU A O   1 
ATOM   1231 C  CB  . LEU A 1 170 ? 105.281 -4.829  -12.424 1.00 44.69  ? 169 LEU A CB  1 
ATOM   1232 C  CG  . LEU A 1 170 ? 104.458 -6.031  -12.876 1.00 51.59  ? 169 LEU A CG  1 
ATOM   1233 C  CD1 . LEU A 1 170 ? 103.208 -5.583  -13.610 1.00 47.24  ? 169 LEU A CD1 1 
ATOM   1234 C  CD2 . LEU A 1 170 ? 105.299 -6.943  -13.747 1.00 52.07  ? 169 LEU A CD2 1 
ATOM   1235 N  N   . GLY A 1 171 ? 107.404 -2.862  -11.380 1.00 49.94  ? 170 GLY A N   1 
ATOM   1236 C  CA  . GLY A 1 171 ? 108.139 -1.659  -11.715 1.00 46.04  ? 170 GLY A CA  1 
ATOM   1237 C  C   . GLY A 1 171 ? 109.091 -1.134  -10.661 1.00 48.04  ? 170 GLY A C   1 
ATOM   1238 O  O   . GLY A 1 171 ? 109.466 0.042   -10.706 1.00 49.27  ? 170 GLY A O   1 
ATOM   1239 N  N   . GLY A 1 172 ? 109.487 -1.977  -9.710  1.00 45.03  ? 171 GLY A N   1 
ATOM   1240 C  CA  . GLY A 1 172 ? 110.495 -1.574  -8.739  1.00 45.27  ? 171 GLY A CA  1 
ATOM   1241 C  C   . GLY A 1 172 ? 110.054 -0.402  -7.880  1.00 49.82  ? 171 GLY A C   1 
ATOM   1242 O  O   . GLY A 1 172 ? 108.888 -0.287  -7.481  1.00 49.10  ? 171 GLY A O   1 
ATOM   1243 N  N   . TYR A 1 173 ? 111.006 0.496   -7.599  1.00 48.01  ? 172 TYR A N   1 
ATOM   1244 C  CA  . TYR A 1 173 ? 110.749 1.610   -6.689  1.00 46.92  ? 172 TYR A CA  1 
ATOM   1245 C  C   . TYR A 1 173 ? 109.665 2.537   -7.224  1.00 44.28  ? 172 TYR A C   1 
ATOM   1246 O  O   . TYR A 1 173 ? 108.777 2.956   -6.474  1.00 42.16  ? 172 TYR A O   1 
ATOM   1247 C  CB  . TYR A 1 173 ? 112.037 2.392   -6.441  1.00 41.39  ? 172 TYR A CB  1 
ATOM   1248 C  CG  . TYR A 1 173 ? 111.872 3.565   -5.500  1.00 42.61  ? 172 TYR A CG  1 
ATOM   1249 C  CD1 . TYR A 1 173 ? 111.687 3.367   -4.138  1.00 42.17  ? 172 TYR A CD1 1 
ATOM   1250 C  CD2 . TYR A 1 173 ? 111.902 4.869   -5.972  1.00 40.74  ? 172 TYR A CD2 1 
ATOM   1251 C  CE1 . TYR A 1 173 ? 111.540 4.433   -3.274  1.00 42.76  ? 172 TYR A CE1 1 
ATOM   1252 C  CE2 . TYR A 1 173 ? 111.754 5.943   -5.112  1.00 47.07  ? 172 TYR A CE2 1 
ATOM   1253 C  CZ  . TYR A 1 173 ? 111.576 5.719   -3.764  1.00 45.51  ? 172 TYR A CZ  1 
ATOM   1254 O  OH  . TYR A 1 173 ? 111.432 6.786   -2.908  1.00 48.26  ? 172 TYR A OH  1 
ATOM   1255 N  N   . GLU A 1 174 ? 109.732 2.887   -8.510  1.00 40.64  ? 173 GLU A N   1 
ATOM   1256 C  CA  . GLU A 1 174 ? 108.723 3.779   -9.069  1.00 46.67  ? 173 GLU A CA  1 
ATOM   1257 C  C   . GLU A 1 174 ? 107.357 3.107   -9.115  1.00 45.50  ? 173 GLU A C   1 
ATOM   1258 O  O   . GLU A 1 174 ? 106.335 3.765   -8.883  1.00 39.94  ? 173 GLU A O   1 
ATOM   1259 C  CB  . GLU A 1 174 ? 109.160 4.261   -10.451 1.00 43.75  ? 173 GLU A CB  1 
ATOM   1260 C  CG  . GLU A 1 174 ? 110.235 5.341   -10.374 1.00 49.99  ? 173 GLU A CG  1 
ATOM   1261 C  CD  . GLU A 1 174 ? 110.363 6.171   -11.638 1.00 57.07  ? 173 GLU A CD  1 
ATOM   1262 O  OE1 . GLU A 1 174 ? 111.305 5.925   -12.427 1.00 59.15  ? 173 GLU A OE1 1 
ATOM   1263 O  OE2 . GLU A 1 174 ? 109.519 7.069   -11.847 1.00 57.53  ? 173 GLU A OE2 1 
ATOM   1264 N  N   . GLY A 1 175 ? 107.321 1.802   -9.386  1.00 44.88  ? 174 GLY A N   1 
ATOM   1265 C  CA  . GLY A 1 175 ? 106.075 1.069   -9.263  1.00 40.26  ? 174 GLY A CA  1 
ATOM   1266 C  C   . GLY A 1 175 ? 105.525 1.086   -7.851  1.00 42.89  ? 174 GLY A C   1 
ATOM   1267 O  O   . GLY A 1 175 ? 104.307 1.164   -7.653  1.00 44.03  ? 174 GLY A O   1 
ATOM   1268 N  N   . ALA A 1 176 ? 106.407 1.023   -6.852  1.00 40.01  ? 175 ALA A N   1 
ATOM   1269 C  CA  . ALA A 1 176 ? 105.963 1.111   -5.465  1.00 40.08  ? 175 ALA A CA  1 
ATOM   1270 C  C   . ALA A 1 176 ? 105.333 2.465   -5.171  1.00 40.08  ? 175 ALA A C   1 
ATOM   1271 O  O   . ALA A 1 176 ? 104.270 2.538   -4.540  1.00 40.90  ? 175 ALA A O   1 
ATOM   1272 C  CB  . ALA A 1 176 ? 107.131 0.849   -4.519  1.00 44.68  ? 175 ALA A CB  1 
ATOM   1273 N  N   . LEU A 1 177 ? 105.970 3.550   -5.621  1.00 39.60  ? 176 LEU A N   1 
ATOM   1274 C  CA  . LEU A 1 177 ? 105.394 4.878   -5.427  1.00 41.95  ? 176 LEU A CA  1 
ATOM   1275 C  C   . LEU A 1 177 ? 104.041 5.000   -6.117  1.00 43.30  ? 176 LEU A C   1 
ATOM   1276 O  O   . LEU A 1 177 ? 103.100 5.570   -5.553  1.00 41.54  ? 176 LEU A O   1 
ATOM   1277 C  CB  . LEU A 1 177 ? 106.351 5.950   -5.945  1.00 45.57  ? 176 LEU A CB  1 
ATOM   1278 C  CG  . LEU A 1 177 ? 107.737 6.003   -5.296  1.00 47.55  ? 176 LEU A CG  1 
ATOM   1279 C  CD1 . LEU A 1 177 ? 108.508 7.210   -5.795  1.00 41.13  ? 176 LEU A CD1 1 
ATOM   1280 C  CD2 . LEU A 1 177 ? 107.621 6.023   -3.781  1.00 39.30  ? 176 LEU A CD2 1 
ATOM   1281 N  N   . LEU A 1 178 ? 103.925 4.477   -7.342  1.00 39.55  ? 177 LEU A N   1 
ATOM   1282 C  CA  . LEU A 1 178 ? 102.636 4.483   -8.026  1.00 39.58  ? 177 LEU A CA  1 
ATOM   1283 C  C   . LEU A 1 178 ? 101.586 3.740   -7.211  1.00 43.42  ? 177 LEU A C   1 
ATOM   1284 O  O   . LEU A 1 178 ? 100.446 4.203   -7.085  1.00 43.34  ? 177 LEU A O   1 
ATOM   1285 C  CB  . LEU A 1 178 ? 102.771 3.863   -9.417  1.00 39.55  ? 177 LEU A CB  1 
ATOM   1286 C  CG  . LEU A 1 178 ? 101.467 3.478   -10.117 1.00 45.14  ? 177 LEU A CG  1 
ATOM   1287 C  CD1 . LEU A 1 178 ? 100.699 4.716   -10.576 1.00 41.51  ? 177 LEU A CD1 1 
ATOM   1288 C  CD2 . LEU A 1 178 ? 101.739 2.544   -11.290 1.00 48.94  ? 177 LEU A CD2 1 
ATOM   1289 N  N   . GLY A 1 179 ? 101.959 2.594   -6.637  1.00 39.23  ? 178 GLY A N   1 
ATOM   1290 C  CA  . GLY A 1 179 ? 101.037 1.874   -5.775  1.00 41.60  ? 178 GLY A CA  1 
ATOM   1291 C  C   . GLY A 1 179 ? 100.611 2.690   -4.570  1.00 42.00  ? 178 GLY A C   1 
ATOM   1292 O  O   . GLY A 1 179 ? 99.466  2.598   -4.121  1.00 40.30  ? 178 GLY A O   1 
ATOM   1293 N  N   . LEU A 1 180 ? 101.524 3.502   -4.033  1.00 42.86  ? 179 LEU A N   1 
ATOM   1294 C  CA  . LEU A 1 180 ? 101.168 4.373   -2.918  1.00 39.58  ? 179 LEU A CA  1 
ATOM   1295 C  C   . LEU A 1 180 ? 100.112 5.386   -3.332  1.00 40.72  ? 179 LEU A C   1 
ATOM   1296 O  O   . LEU A 1 180 ? 99.193  5.688   -2.562  1.00 39.98  ? 179 LEU A O   1 
ATOM   1297 C  CB  . LEU A 1 180 ? 102.411 5.084   -2.390  1.00 40.84  ? 179 LEU A CB  1 
ATOM   1298 C  CG  . LEU A 1 180 ? 103.387 4.215   -1.599  1.00 45.71  ? 179 LEU A CG  1 
ATOM   1299 C  CD1 . LEU A 1 180 ? 104.542 5.052   -1.068  1.00 38.09  ? 179 LEU A CD1 1 
ATOM   1300 C  CD2 . LEU A 1 180 ? 102.664 3.508   -0.470  1.00 43.54  ? 179 LEU A CD2 1 
ATOM   1301 N  N   . ALA A 1 181 ? 100.223 5.920   -4.549  1.00 37.04  ? 180 ALA A N   1 
ATOM   1302 C  CA  . ALA A 1 181 ? 99.203  6.839   -5.038  1.00 40.03  ? 180 ALA A CA  1 
ATOM   1303 C  C   . ALA A 1 181 ? 97.901  6.111   -5.350  1.00 41.75  ? 180 ALA A C   1 
ATOM   1304 O  O   . ALA A 1 181 ? 96.817  6.697   -5.239  1.00 40.44  ? 180 ALA A O   1 
ATOM   1305 C  CB  . ALA A 1 181 ? 99.712  7.577   -6.277  1.00 41.31  ? 180 ALA A CB  1 
ATOM   1306 N  N   . LEU A 1 182 ? 97.985  4.837   -5.730  1.00 38.78  ? 181 LEU A N   1 
ATOM   1307 C  CA  . LEU A 1 182 ? 96.795  4.077   -6.075  1.00 38.04  ? 181 LEU A CA  1 
ATOM   1308 C  C   . LEU A 1 182 ? 96.021  3.609   -4.851  1.00 40.26  ? 181 LEU A C   1 
ATOM   1309 O  O   . LEU A 1 182 ? 94.842  3.260   -4.984  1.00 39.37  ? 181 LEU A O   1 
ATOM   1310 C  CB  . LEU A 1 182 ? 97.174  2.871   -6.933  1.00 37.30  ? 181 LEU A CB  1 
ATOM   1311 C  CG  . LEU A 1 182 ? 97.554  3.163   -8.382  1.00 42.12  ? 181 LEU A CG  1 
ATOM   1312 C  CD1 . LEU A 1 182 ? 98.379  2.019   -8.942  1.00 38.54  ? 181 LEU A CD1 1 
ATOM   1313 C  CD2 . LEU A 1 182 ? 96.310  3.396   -9.222  1.00 39.73  ? 181 LEU A CD2 1 
ATOM   1314 N  N   . ILE A 1 183 ? 96.645  3.594   -3.676  1.00 40.16  ? 182 ILE A N   1 
ATOM   1315 C  CA  . ILE A 1 183 ? 95.968  3.166   -2.452  1.00 39.76  ? 182 ILE A CA  1 
ATOM   1316 C  C   . ILE A 1 183 ? 94.685  3.977   -2.269  1.00 40.54  ? 182 ILE A C   1 
ATOM   1317 O  O   . ILE A 1 183 ? 93.600  3.379   -2.245  1.00 39.41  ? 182 ILE A O   1 
ATOM   1318 C  CB  . ILE A 1 183 ? 96.885  3.280   -1.221  1.00 43.25  ? 182 ILE A CB  1 
ATOM   1319 C  CG1 . ILE A 1 183 ? 98.038  2.275   -1.294  1.00 48.44  ? 182 ILE A CG1 1 
ATOM   1320 C  CG2 . ILE A 1 183 ? 96.084  3.082   0.049   1.00 42.62  ? 182 ILE A CG2 1 
ATOM   1321 C  CD1 . ILE A 1 183 ? 97.629  0.909   -1.738  1.00 43.55  ? 182 ILE A CD1 1 
ATOM   1322 N  N   . PRO A 1 184 ? 94.722  5.314   -2.171  1.00 42.21  ? 183 PRO A N   1 
ATOM   1323 C  CA  . PRO A 1 184 ? 93.461  6.050   -1.985  1.00 38.78  ? 183 PRO A CA  1 
ATOM   1324 C  C   . PRO A 1 184 ? 92.612  6.200   -3.242  1.00 34.81  ? 183 PRO A C   1 
ATOM   1325 O  O   . PRO A 1 184 ? 91.432  6.558   -3.123  1.00 44.60  ? 183 PRO A O   1 
ATOM   1326 C  CB  . PRO A 1 184 ? 93.927  7.419   -1.468  1.00 29.56  ? 183 PRO A CB  1 
ATOM   1327 C  CG  . PRO A 1 184 ? 95.263  7.606   -2.056  1.00 36.52  ? 183 PRO A CG  1 
ATOM   1328 C  CD  . PRO A 1 184 ? 95.878  6.236   -2.216  1.00 36.52  ? 183 PRO A CD  1 
ATOM   1329 N  N   . ALA A 1 185 ? 93.149  5.923   -4.427  1.00 35.16  ? 184 ALA A N   1 
ATOM   1330 C  CA  . ALA A 1 185 ? 92.392  6.101   -5.663  1.00 38.78  ? 184 ALA A CA  1 
ATOM   1331 C  C   . ALA A 1 185 ? 91.478  4.924   -5.972  1.00 41.09  ? 184 ALA A C   1 
ATOM   1332 O  O   . ALA A 1 185 ? 90.369  5.119   -6.485  1.00 34.19  ? 184 ALA A O   1 
ATOM   1333 C  CB  . ALA A 1 185 ? 93.337  6.327   -6.843  1.00 34.40  ? 184 ALA A CB  1 
ATOM   1334 N  N   . LEU A 1 186 ? 91.920  3.701   -5.670  1.00 38.68  ? 185 LEU A N   1 
ATOM   1335 C  CA  . LEU A 1 186 ? 91.146  2.513   -6.006  1.00 35.93  ? 185 LEU A CA  1 
ATOM   1336 C  C   . LEU A 1 186 ? 89.843  2.410   -5.228  1.00 36.63  ? 185 LEU A C   1 
ATOM   1337 O  O   . LEU A 1 186 ? 89.017  1.553   -5.556  1.00 41.13  ? 185 LEU A O   1 
ATOM   1338 C  CB  . LEU A 1 186 ? 91.983  1.261   -5.766  1.00 40.47  ? 185 LEU A CB  1 
ATOM   1339 C  CG  . LEU A 1 186 ? 93.066  1.026   -6.813  1.00 40.29  ? 185 LEU A CG  1 
ATOM   1340 C  CD1 . LEU A 1 186 ? 94.145  0.135   -6.248  1.00 40.85  ? 185 LEU A CD1 1 
ATOM   1341 C  CD2 . LEU A 1 186 ? 92.467  0.419   -8.072  1.00 43.89  ? 185 LEU A CD2 1 
ATOM   1342 N  N   . VAL A 1 187 ? 89.636  3.246   -4.207  1.00 37.06  ? 186 VAL A N   1 
ATOM   1343 C  CA  . VAL A 1 187 ? 88.363  3.243   -3.497  1.00 37.37  ? 186 VAL A CA  1 
ATOM   1344 C  C   . VAL A 1 187 ? 87.213  3.606   -4.425  1.00 35.32  ? 186 VAL A C   1 
ATOM   1345 O  O   . VAL A 1 187 ? 86.060  3.245   -4.154  1.00 34.34  ? 186 VAL A O   1 
ATOM   1346 C  CB  . VAL A 1 187 ? 88.416  4.200   -2.286  1.00 32.13  ? 186 VAL A CB  1 
ATOM   1347 C  CG1 . VAL A 1 187 ? 88.412  5.641   -2.749  1.00 33.80  ? 186 VAL A CG1 1 
ATOM   1348 C  CG2 . VAL A 1 187 ? 87.237  3.947   -1.361  1.00 34.59  ? 186 VAL A CG2 1 
ATOM   1349 N  N   . VAL A 1 188 ? 87.502  4.302   -5.531  1.00 35.28  ? 187 VAL A N   1 
ATOM   1350 C  CA  . VAL A 1 188 ? 86.441  4.743   -6.428  1.00 32.43  ? 187 VAL A CA  1 
ATOM   1351 C  C   . VAL A 1 188 ? 85.695  3.556   -7.019  1.00 30.83  ? 187 VAL A C   1 
ATOM   1352 O  O   . VAL A 1 188 ? 84.497  3.653   -7.301  1.00 34.99  ? 187 VAL A O   1 
ATOM   1353 C  CB  . VAL A 1 188 ? 87.011  5.660   -7.529  1.00 34.41  ? 187 VAL A CB  1 
ATOM   1354 C  CG1 . VAL A 1 188 ? 87.793  4.860   -8.576  1.00 35.17  ? 187 VAL A CG1 1 
ATOM   1355 C  CG2 . VAL A 1 188 ? 85.891  6.454   -8.178  1.00 33.84  ? 187 VAL A CG2 1 
ATOM   1356 N  N   . ILE A 1 189 ? 86.361  2.419   -7.192  1.00 32.62  ? 188 ILE A N   1 
ATOM   1357 C  CA  . ILE A 1 189 ? 85.718  1.260   -7.811  1.00 33.09  ? 188 ILE A CA  1 
ATOM   1358 C  C   . ILE A 1 189 ? 84.650  0.688   -6.884  1.00 32.26  ? 188 ILE A C   1 
ATOM   1359 O  O   . ILE A 1 189 ? 83.489  0.572   -7.305  1.00 33.71  ? 188 ILE A O   1 
ATOM   1360 C  CB  . ILE A 1 189 ? 86.743  0.186   -8.209  1.00 31.83  ? 188 ILE A CB  1 
ATOM   1361 C  CG1 . ILE A 1 189 ? 87.518  0.615   -9.453  1.00 37.80  ? 188 ILE A CG1 1 
ATOM   1362 C  CG2 . ILE A 1 189 ? 86.051  -1.148  -8.419  1.00 35.70  ? 188 ILE A CG2 1 
ATOM   1363 C  CD1 . ILE A 1 189 ? 88.883  0.000   -9.536  1.00 40.69  ? 188 ILE A CD1 1 
ATOM   1364 N  N   . PRO A 1 190 ? 84.967  0.310   -5.637  1.00 33.42  ? 189 PRO A N   1 
ATOM   1365 C  CA  . PRO A 1 190 ? 83.897  -0.162  -4.747  1.00 33.33  ? 189 PRO A CA  1 
ATOM   1366 C  C   . PRO A 1 190 ? 82.908  0.921   -4.358  1.00 38.10  ? 189 PRO A C   1 
ATOM   1367 O  O   . PRO A 1 190 ? 81.716  0.622   -4.205  1.00 33.57  ? 189 PRO A O   1 
ATOM   1368 C  CB  . PRO A 1 190 ? 84.664  -0.684  -3.525  1.00 34.98  ? 189 PRO A CB  1 
ATOM   1369 C  CG  . PRO A 1 190 ? 85.926  0.068   -3.529  1.00 32.75  ? 189 PRO A CG  1 
ATOM   1370 C  CD  . PRO A 1 190 ? 86.283  0.212   -4.971  1.00 34.52  ? 189 PRO A CD  1 
ATOM   1371 N  N   . ALA A 1 191 ? 83.364  2.165   -4.178  1.00 35.34  ? 190 ALA A N   1 
ATOM   1372 C  CA  . ALA A 1 191 ? 82.445  3.237   -3.812  1.00 33.49  ? 190 ALA A CA  1 
ATOM   1373 C  C   . ALA A 1 191 ? 81.370  3.417   -4.872  1.00 35.29  ? 190 ALA A C   1 
ATOM   1374 O  O   . ALA A 1 191 ? 80.186  3.562   -4.547  1.00 33.64  ? 190 ALA A O   1 
ATOM   1375 C  CB  . ALA A 1 191 ? 83.204  4.544   -3.594  1.00 29.65  ? 190 ALA A CB  1 
ATOM   1376 N  N   . ALA A 1 192 ? 81.762  3.402   -6.148  1.00 33.66  ? 191 ALA A N   1 
ATOM   1377 C  CA  . ALA A 1 192 ? 80.772  3.517   -7.213  1.00 34.91  ? 191 ALA A CA  1 
ATOM   1378 C  C   . ALA A 1 192 ? 79.841  2.315   -7.225  1.00 34.50  ? 191 ALA A C   1 
ATOM   1379 O  O   . ALA A 1 192 ? 78.624  2.461   -7.394  1.00 40.49  ? 191 ALA A O   1 
ATOM   1380 C  CB  . ALA A 1 192 ? 81.463  3.673   -8.565  1.00 36.81  ? 191 ALA A CB  1 
ATOM   1381 N  N   . ILE A 1 193 ? 80.395  1.116   -7.039  1.00 37.55  ? 192 ILE A N   1 
ATOM   1382 C  CA  . ILE A 1 193 ? 79.572  -0.088  -7.016  1.00 37.92  ? 192 ILE A CA  1 
ATOM   1383 C  C   . ILE A 1 193 ? 78.602  -0.043  -5.841  1.00 37.49  ? 192 ILE A C   1 
ATOM   1384 O  O   . ILE A 1 193 ? 77.399  -0.281  -5.995  1.00 40.45  ? 192 ILE A O   1 
ATOM   1385 C  CB  . ILE A 1 193 ? 80.464  -1.342  -6.969  1.00 42.21  ? 192 ILE A CB  1 
ATOM   1386 C  CG1 . ILE A 1 193 ? 81.061  -1.629  -8.348  1.00 39.09  ? 192 ILE A CG1 1 
ATOM   1387 C  CG2 . ILE A 1 193 ? 79.677  -2.548  -6.475  1.00 46.07  ? 192 ILE A CG2 1 
ATOM   1388 C  CD1 . ILE A 1 193 ? 82.378  -2.362  -8.293  1.00 33.50  ? 192 ILE A CD1 1 
ATOM   1389 N  N   . MET A 1 194 ? 79.111  0.280   -4.650  1.00 38.91  ? 193 MET A N   1 
ATOM   1390 C  CA  . MET A 1 194 ? 78.275  0.263   -3.452  1.00 39.25  ? 193 MET A CA  1 
ATOM   1391 C  C   . MET A 1 194 ? 77.177  1.317   -3.524  1.00 37.82  ? 193 MET A C   1 
ATOM   1392 O  O   . MET A 1 194 ? 76.040  1.063   -3.116  1.00 37.47  ? 193 MET A O   1 
ATOM   1393 C  CB  . MET A 1 194 ? 79.142  0.472   -2.208  1.00 36.97  ? 193 MET A CB  1 
ATOM   1394 C  CG  . MET A 1 194 ? 79.979  -0.744  -1.834  1.00 48.12  ? 193 MET A CG  1 
ATOM   1395 S  SD  . MET A 1 194 ? 79.017  -2.055  -1.069  1.00 61.38  ? 193 MET A SD  1 
ATOM   1396 C  CE  . MET A 1 194 ? 79.089  -3.309  -2.341  1.00 52.11  ? 193 MET A CE  1 
ATOM   1397 N  N   . LEU A 1 195 ? 77.498  2.503   -4.044  1.00 35.79  ? 194 LEU A N   1 
ATOM   1398 C  CA  . LEU A 1 195 ? 76.513  3.577   -4.104  1.00 37.97  ? 194 LEU A CA  1 
ATOM   1399 C  C   . LEU A 1 195 ? 75.327  3.192   -4.983  1.00 42.89  ? 194 LEU A C   1 
ATOM   1400 O  O   . LEU A 1 195 ? 74.168  3.396   -4.604  1.00 43.32  ? 194 LEU A O   1 
ATOM   1401 C  CB  . LEU A 1 195 ? 77.178  4.853   -4.616  1.00 36.45  ? 194 LEU A CB  1 
ATOM   1402 C  CG  . LEU A 1 195 ? 76.368  6.144   -4.563  1.00 40.49  ? 194 LEU A CG  1 
ATOM   1403 C  CD1 . LEU A 1 195 ? 76.206  6.612   -3.123  1.00 43.44  ? 194 LEU A CD1 1 
ATOM   1404 C  CD2 . LEU A 1 195 ? 77.047  7.210   -5.400  1.00 43.61  ? 194 LEU A CD2 1 
ATOM   1405 N  N   . ILE A 1 196 ? 75.598  2.622   -6.157  1.00 42.90  ? 195 ILE A N   1 
ATOM   1406 C  CA  . ILE A 1 196 ? 74.530  2.262   -7.084  1.00 38.42  ? 195 ILE A CA  1 
ATOM   1407 C  C   . ILE A 1 196 ? 73.787  1.027   -6.588  1.00 40.16  ? 195 ILE A C   1 
ATOM   1408 O  O   . ILE A 1 196 ? 72.552  0.963   -6.643  1.00 40.83  ? 195 ILE A O   1 
ATOM   1409 C  CB  . ILE A 1 196 ? 75.108  2.037   -8.497  1.00 47.63  ? 195 ILE A CB  1 
ATOM   1410 C  CG1 . ILE A 1 196 ? 75.804  3.291   -9.050  1.00 49.88  ? 195 ILE A CG1 1 
ATOM   1411 C  CG2 . ILE A 1 196 ? 74.022  1.573   -9.451  1.00 44.46  ? 195 ILE A CG2 1 
ATOM   1412 C  CD1 . ILE A 1 196 ? 75.271  4.632   -8.532  1.00 49.38  ? 195 ILE A CD1 1 
ATOM   1413 N  N   . LYS A 1 197 ? 74.526  0.027   -6.098  1.00 37.24  ? 196 LYS A N   1 
ATOM   1414 C  CA  . LYS A 1 197 ? 73.905  -1.226  -5.683  1.00 39.61  ? 196 LYS A CA  1 
ATOM   1415 C  C   . LYS A 1 197 ? 73.020  -1.039  -4.453  1.00 39.88  ? 196 LYS A C   1 
ATOM   1416 O  O   . LYS A 1 197 ? 71.982  -1.698  -4.324  1.00 37.81  ? 196 LYS A O   1 
ATOM   1417 C  CB  . LYS A 1 197 ? 74.988  -2.277  -5.420  1.00 38.61  ? 196 LYS A CB  1 
ATOM   1418 C  CG  . LYS A 1 197 ? 74.687  -3.248  -4.280  1.00 52.86  ? 196 LYS A CG  1 
ATOM   1419 C  CD  . LYS A 1 197 ? 75.887  -4.133  -3.946  1.00 50.67  ? 196 LYS A CD  1 
ATOM   1420 C  CE  . LYS A 1 197 ? 76.316  -4.976  -5.146  1.00 55.30  ? 196 LYS A CE  1 
ATOM   1421 N  NZ  . LYS A 1 197 ? 77.732  -5.409  -5.048  1.00 55.69  ? 196 LYS A NZ  1 
ATOM   1422 N  N   . ARG A 1 198 ? 73.402  -0.142  -3.546  1.00 37.53  ? 197 ARG A N   1 
ATOM   1423 C  CA  . ARG A 1 198 ? 72.626  0.063   -2.328  1.00 39.92  ? 197 ARG A CA  1 
ATOM   1424 C  C   . ARG A 1 198 ? 71.403  0.948   -2.536  1.00 38.38  ? 197 ARG A C   1 
ATOM   1425 O  O   . ARG A 1 198 ? 70.635  1.138   -1.588  1.00 34.04  ? 197 ARG A O   1 
ATOM   1426 C  CB  . ARG A 1 198 ? 73.514  0.653   -1.228  1.00 39.27  ? 197 ARG A CB  1 
ATOM   1427 C  CG  . ARG A 1 198 ? 74.426  -0.373  -0.563  1.00 34.10  ? 197 ARG A CG  1 
ATOM   1428 C  CD  . ARG A 1 198 ? 75.467  0.300   0.314   1.00 38.34  ? 197 ARG A CD  1 
ATOM   1429 N  NE  . ARG A 1 198 ? 74.941  0.665   1.625   1.00 35.96  ? 197 ARG A NE  1 
ATOM   1430 C  CZ  . ARG A 1 198 ? 74.745  -0.194  2.618   1.00 41.85  ? 197 ARG A CZ  1 
ATOM   1431 N  NH1 . ARG A 1 198 ? 74.982  -1.490  2.468   1.00 32.53  ? 197 ARG A NH1 1 
ATOM   1432 N  NH2 . ARG A 1 198 ? 74.304  0.257   3.789   1.00 33.56  ? 197 ARG A NH2 1 
ATOM   1433 N  N   . GLY A 1 199 ? 71.196  1.480   -3.739  1.00 39.94  ? 198 GLY A N   1 
ATOM   1434 C  CA  . GLY A 1 199 ? 70.015  2.276   -4.011  1.00 36.07  ? 198 GLY A CA  1 
ATOM   1435 C  C   . GLY A 1 199 ? 70.012  3.631   -3.345  1.00 33.51  ? 198 GLY A C   1 
ATOM   1436 O  O   . GLY A 1 199 ? 68.943  4.207   -3.137  1.00 29.68  ? 198 GLY A O   1 
ATOM   1437 N  N   . VAL A 1 200 ? 71.189  4.164   -3.016  1.00 43.61  ? 199 VAL A N   1 
ATOM   1438 C  CA  . VAL A 1 200 ? 71.272  5.437   -2.302  1.00 43.79  ? 199 VAL A CA  1 
ATOM   1439 C  C   . VAL A 1 200 ? 70.730  6.573   -3.166  1.00 37.01  ? 199 VAL A C   1 
ATOM   1440 O  O   . VAL A 1 200 ? 69.817  7.301   -2.762  1.00 42.51  ? 199 VAL A O   1 
ATOM   1441 C  CB  . VAL A 1 200 ? 72.720  5.704   -1.853  1.00 34.75  ? 199 VAL A CB  1 
ATOM   1442 C  CG1 . VAL A 1 200 ? 72.747  6.657   -0.676  1.00 33.11  ? 199 VAL A CG1 1 
ATOM   1443 C  CG2 . VAL A 1 200 ? 73.403  4.392   -1.497  1.00 41.28  ? 199 VAL A CG2 1 
ATOM   1444 N  N   . ILE A 1 201 ? 71.284  6.738   -4.365  1.00 39.80  ? 200 ILE A N   1 
ATOM   1445 C  CA  . ILE A 1 201 ? 70.803  7.730   -5.327  1.00 40.28  ? 200 ILE A CA  1 
ATOM   1446 C  C   . ILE A 1 201 ? 70.785  7.111   -6.716  1.00 36.25  ? 200 ILE A C   1 
ATOM   1447 O  O   . ILE A 1 201 ? 71.492  6.133   -6.991  1.00 36.12  ? 200 ILE A O   1 
ATOM   1448 C  CB  . ILE A 1 201 ? 71.680  8.998   -5.341  1.00 42.35  ? 200 ILE A CB  1 
ATOM   1449 C  CG1 . ILE A 1 201 ? 73.158  8.618   -5.404  1.00 45.97  ? 200 ILE A CG1 1 
ATOM   1450 C  CG2 . ILE A 1 201 ? 71.372  9.888   -4.151  1.00 40.95  ? 200 ILE A CG2 1 
ATOM   1451 C  CD1 . ILE A 1 201 ? 73.979  9.506   -6.317  1.00 43.12  ? 200 ILE A CD1 1 
ATOM   1452 N  N   . PRO A 1 202 ? 69.979  7.667   -7.617  1.00 38.52  ? 201 PRO A N   1 
ATOM   1453 C  CA  . PRO A 1 202 ? 70.093  7.277   -9.024  1.00 42.83  ? 201 PRO A CA  1 
ATOM   1454 C  C   . PRO A 1 202 ? 71.452  7.677   -9.579  1.00 42.56  ? 201 PRO A C   1 
ATOM   1455 O  O   . PRO A 1 202 ? 72.026  8.701   -9.201  1.00 43.28  ? 201 PRO A O   1 
ATOM   1456 C  CB  . PRO A 1 202 ? 68.958  8.051   -9.706  1.00 42.90  ? 201 PRO A CB  1 
ATOM   1457 C  CG  . PRO A 1 202 ? 68.036  8.462   -8.604  1.00 44.67  ? 201 PRO A CG  1 
ATOM   1458 C  CD  . PRO A 1 202 ? 68.885  8.629   -7.391  1.00 38.70  ? 201 PRO A CD  1 
ATOM   1459 N  N   . LEU A 1 203 ? 71.970  6.848   -10.489 1.00 48.31  ? 202 LEU A N   1 
ATOM   1460 C  CA  . LEU A 1 203 ? 73.268  7.137   -11.094 1.00 48.37  ? 202 LEU A CA  1 
ATOM   1461 C  C   . LEU A 1 203 ? 73.269  8.489   -11.796 1.00 46.07  ? 202 LEU A C   1 
ATOM   1462 O  O   . LEU A 1 203 ? 74.293  9.183   -11.801 1.00 45.87  ? 202 LEU A O   1 
ATOM   1463 C  CB  . LEU A 1 203 ? 73.648  6.023   -12.073 1.00 45.59  ? 202 LEU A CB  1 
ATOM   1464 C  CG  . LEU A 1 203 ? 74.987  6.127   -12.806 1.00 61.10  ? 202 LEU A CG  1 
ATOM   1465 C  CD1 . LEU A 1 203 ? 76.122  6.412   -11.827 1.00 59.55  ? 202 LEU A CD1 1 
ATOM   1466 C  CD2 . LEU A 1 203 ? 75.270  4.851   -13.599 1.00 55.60  ? 202 LEU A CD2 1 
ATOM   1467 N  N   . SER A 1 204 ? 72.126  8.895   -12.359 1.00 39.58  ? 203 SER A N   1 
ATOM   1468 C  CA  . SER A 1 204 ? 72.058  10.128  -13.134 1.00 46.44  ? 203 SER A CA  1 
ATOM   1469 C  C   . SER A 1 204 ? 72.330  11.371  -12.294 1.00 43.91  ? 203 SER A C   1 
ATOM   1470 O  O   . SER A 1 204 ? 72.663  12.420  -12.856 1.00 40.67  ? 203 SER A O   1 
ATOM   1471 C  CB  . SER A 1 204 ? 70.690  10.248  -13.806 1.00 45.82  ? 203 SER A CB  1 
ATOM   1472 O  OG  . SER A 1 204 ? 69.655  10.254  -12.843 1.00 53.04  ? 203 SER A OG  1 
ATOM   1473 N  N   . TYR A 1 205 ? 72.201  11.281  -10.967 1.00 40.29  ? 204 TYR A N   1 
ATOM   1474 C  CA  . TYR A 1 205 ? 72.476  12.439  -10.124 1.00 38.93  ? 204 TYR A CA  1 
ATOM   1475 C  C   . TYR A 1 205 ? 73.906  12.928  -10.294 1.00 35.68  ? 204 TYR A C   1 
ATOM   1476 O  O   . TYR A 1 205 ? 74.180  14.117  -10.094 1.00 37.53  ? 204 TYR A O   1 
ATOM   1477 C  CB  . TYR A 1 205 ? 72.219  12.102  -8.656  1.00 37.68  ? 204 TYR A CB  1 
ATOM   1478 C  CG  . TYR A 1 205 ? 70.770  12.171  -8.238  1.00 36.02  ? 204 TYR A CG  1 
ATOM   1479 C  CD1 . TYR A 1 205 ? 69.750  12.163  -9.178  1.00 38.06  ? 204 TYR A CD1 1 
ATOM   1480 C  CD2 . TYR A 1 205 ? 70.420  12.227  -6.895  1.00 40.90  ? 204 TYR A CD2 1 
ATOM   1481 C  CE1 . TYR A 1 205 ? 68.427  12.219  -8.794  1.00 42.51  ? 204 TYR A CE1 1 
ATOM   1482 C  CE2 . TYR A 1 205 ? 69.097  12.281  -6.503  1.00 36.67  ? 204 TYR A CE2 1 
ATOM   1483 C  CZ  . TYR A 1 205 ? 68.109  12.280  -7.456  1.00 37.36  ? 204 TYR A CZ  1 
ATOM   1484 O  OH  . TYR A 1 205 ? 66.794  12.339  -7.072  1.00 43.64  ? 204 TYR A OH  1 
ATOM   1485 N  N   . LEU A 1 206 ? 74.824  12.035  -10.668 1.00 32.52  ? 205 LEU A N   1 
ATOM   1486 C  CA  . LEU A 1 206 ? 76.243  12.354  -10.781 1.00 38.86  ? 205 LEU A CA  1 
ATOM   1487 C  C   . LEU A 1 206 ? 76.611  13.039  -12.093 1.00 36.49  ? 205 LEU A C   1 
ATOM   1488 O  O   . LEU A 1 206 ? 77.781  13.394  -12.278 1.00 35.70  ? 205 LEU A O   1 
ATOM   1489 C  CB  . LEU A 1 206 ? 77.081  11.082  -10.614 1.00 35.31  ? 205 LEU A CB  1 
ATOM   1490 C  CG  . LEU A 1 206 ? 77.114  10.528  -9.185  1.00 45.98  ? 205 LEU A CG  1 
ATOM   1491 C  CD1 . LEU A 1 206 ? 77.586  9.081   -9.162  1.00 40.53  ? 205 LEU A CD1 1 
ATOM   1492 C  CD2 . LEU A 1 206 ? 77.985  11.393  -8.288  1.00 37.74  ? 205 LEU A CD2 1 
ATOM   1493 N  N   . LYS A 1 207 ? 75.665  13.228  -13.003 1.00 36.31  ? 206 LYS A N   1 
ATOM   1494 C  CA  . LYS A 1 207 ? 75.956  13.977  -14.218 1.00 38.06  ? 206 LYS A CA  1 
ATOM   1495 C  C   . LYS A 1 207 ? 76.269  15.424  -13.855 1.00 38.43  ? 206 LYS A C   1 
ATOM   1496 O  O   . LYS A 1 207 ? 75.498  16.051  -13.120 1.00 39.97  ? 206 LYS A O   1 
ATOM   1497 C  CB  . LYS A 1 207 ? 74.780  13.914  -15.184 1.00 34.40  ? 206 LYS A CB  1 
ATOM   1498 C  CG  . LYS A 1 207 ? 74.514  12.514  -15.708 1.00 52.59  ? 206 LYS A CG  1 
ATOM   1499 C  CD  . LYS A 1 207 ? 73.175  12.424  -16.413 1.00 53.61  ? 206 LYS A CD  1 
ATOM   1500 C  CE  . LYS A 1 207 ? 73.242  11.451  -17.574 1.00 58.63  ? 206 LYS A CE  1 
ATOM   1501 N  NZ  . LYS A 1 207 ? 71.898  11.224  -18.176 1.00 68.28  ? 206 LYS A NZ  1 
ATOM   1502 N  N   . PRO A 1 208 ? 77.382  15.978  -14.328 1.00 39.95  ? 207 PRO A N   1 
ATOM   1503 C  CA  . PRO A 1 208 ? 77.741  17.352  -13.950 1.00 38.27  ? 207 PRO A CA  1 
ATOM   1504 C  C   . PRO A 1 208 ? 76.670  18.354  -14.368 1.00 39.00  ? 207 PRO A C   1 
ATOM   1505 O  O   . PRO A 1 208 ? 76.203  18.357  -15.508 1.00 36.97  ? 207 PRO A O   1 
ATOM   1506 C  CB  . PRO A 1 208 ? 79.061  17.590  -14.696 1.00 43.83  ? 207 PRO A CB  1 
ATOM   1507 C  CG  . PRO A 1 208 ? 79.590  16.218  -15.004 1.00 39.16  ? 207 PRO A CG  1 
ATOM   1508 C  CD  . PRO A 1 208 ? 78.392  15.348  -15.196 1.00 32.95  ? 207 PRO A CD  1 
ATOM   1509 N  N   . SER A 1 209 ? 76.268  19.195  -13.418 1.00 39.84  ? 208 SER A N   1 
ATOM   1510 C  CA  . SER A 1 209 ? 75.413  20.344  -13.679 1.00 37.50  ? 208 SER A CA  1 
ATOM   1511 C  C   . SER A 1 209 ? 75.953  21.512  -12.869 1.00 40.58  ? 208 SER A C   1 
ATOM   1512 O  O   . SER A 1 209 ? 76.842  21.349  -12.032 1.00 40.62  ? 208 SER A O   1 
ATOM   1513 C  CB  . SER A 1 209 ? 73.950  20.059  -13.318 1.00 34.42  ? 208 SER A CB  1 
ATOM   1514 O  OG  . SER A 1 209 ? 73.812  19.805  -11.929 1.00 41.51  ? 208 SER A OG  1 
ATOM   1515 N  N   . TRP A 1 210 ? 75.415  22.703  -13.108 1.00 44.89  ? 209 TRP A N   1 
ATOM   1516 C  CA  . TRP A 1 210 ? 75.864  23.882  -12.380 1.00 44.17  ? 209 TRP A CA  1 
ATOM   1517 C  C   . TRP A 1 210 ? 74.685  24.625  -11.776 1.00 46.85  ? 209 TRP A C   1 
ATOM   1518 O  O   . TRP A 1 210 ? 73.736  24.981  -12.482 1.00 48.98  ? 209 TRP A O   1 
ATOM   1519 C  CB  . TRP A 1 210 ? 76.658  24.826  -13.277 1.00 42.41  ? 209 TRP A CB  1 
ATOM   1520 C  CG  . TRP A 1 210 ? 77.466  25.796  -12.487 1.00 42.73  ? 209 TRP A CG  1 
ATOM   1521 C  CD1 . TRP A 1 210 ? 77.172  27.111  -12.248 1.00 38.18  ? 209 TRP A CD1 1 
ATOM   1522 C  CD2 . TRP A 1 210 ? 78.699  25.530  -11.812 1.00 38.32  ? 209 TRP A CD2 1 
ATOM   1523 N  NE1 . TRP A 1 210 ? 78.154  27.680  -11.475 1.00 39.66  ? 209 TRP A NE1 1 
ATOM   1524 C  CE2 . TRP A 1 210 ? 79.103  26.730  -11.193 1.00 37.10  ? 209 TRP A CE2 1 
ATOM   1525 C  CE3 . TRP A 1 210 ? 79.506  24.394  -11.677 1.00 39.70  ? 209 TRP A CE3 1 
ATOM   1526 C  CZ2 . TRP A 1 210 ? 80.278  26.827  -10.452 1.00 38.63  ? 209 TRP A CZ2 1 
ATOM   1527 C  CZ3 . TRP A 1 210 ? 80.669  24.492  -10.942 1.00 35.54  ? 209 TRP A CZ3 1 
ATOM   1528 C  CH2 . TRP A 1 210 ? 81.044  25.699  -10.335 1.00 35.60  ? 209 TRP A CH2 1 
ATOM   1529 N  N   . ASP A 1 211 ? 74.759  24.868  -10.471 1.00 41.07  ? 210 ASP A N   1 
ATOM   1530 C  CA  . ASP A 1 211 ? 73.825  25.743  -9.777  1.00 41.24  ? 210 ASP A CA  1 
ATOM   1531 C  C   . ASP A 1 211 ? 74.646  26.784  -9.035  1.00 39.02  ? 210 ASP A C   1 
ATOM   1532 O  O   . ASP A 1 211 ? 75.439  26.436  -8.155  1.00 35.14  ? 210 ASP A O   1 
ATOM   1533 C  CB  . ASP A 1 211 ? 72.930  24.955  -8.819  1.00 44.09  ? 210 ASP A CB  1 
ATOM   1534 C  CG  . ASP A 1 211 ? 71.758  25.771  -8.313  1.00 49.62  ? 210 ASP A CG  1 
ATOM   1535 O  OD1 . ASP A 1 211 ? 71.955  26.569  -7.371  1.00 50.55  ? 210 ASP A OD1 1 
ATOM   1536 O  OD2 . ASP A 1 211 ? 70.642  25.619  -8.859  1.00 61.91  ? 210 ASP A OD2 1 
ATOM   1537 N  N   . ASN A 1 212 ? 74.466  28.056  -9.401  1.00 40.93  ? 211 ASN A N   1 
ATOM   1538 C  CA  . ASN A 1 212 ? 75.315  29.114  -8.859  1.00 40.35  ? 211 ASN A CA  1 
ATOM   1539 C  C   . ASN A 1 212 ? 75.193  29.211  -7.344  1.00 39.15  ? 211 ASN A C   1 
ATOM   1540 O  O   . ASN A 1 212 ? 76.204  29.352  -6.643  1.00 40.01  ? 211 ASN A O   1 
ATOM   1541 C  CB  . ASN A 1 212 ? 74.961  30.450  -9.509  1.00 37.32  ? 211 ASN A CB  1 
ATOM   1542 C  CG  . ASN A 1 212 ? 75.757  30.706  -10.766 1.00 46.81  ? 211 ASN A CG  1 
ATOM   1543 O  OD1 . ASN A 1 212 ? 76.853  30.165  -10.936 1.00 46.70  ? 211 ASN A OD1 1 
ATOM   1544 N  ND2 . ASN A 1 212 ? 75.217  31.530  -11.655 1.00 50.34  ? 211 ASN A ND2 1 
ATOM   1545 N  N   . GLY A 1 213 ? 73.966  29.137  -6.824  1.00 37.99  ? 212 GLY A N   1 
ATOM   1546 C  CA  . GLY A 1 213 ? 73.781  29.189  -5.385  1.00 33.54  ? 212 GLY A CA  1 
ATOM   1547 C  C   . GLY A 1 213 ? 74.540  28.084  -4.672  1.00 42.59  ? 212 GLY A C   1 
ATOM   1548 O  O   . GLY A 1 213 ? 75.380  28.348  -3.807  1.00 39.35  ? 212 GLY A O   1 
ATOM   1549 N  N   . LEU A 1 214 ? 74.271  26.826  -5.044  1.00 38.36  ? 213 LEU A N   1 
ATOM   1550 C  CA  . LEU A 1 214 ? 74.926  25.702  -4.381  1.00 36.10  ? 213 LEU A CA  1 
ATOM   1551 C  C   . LEU A 1 214 ? 76.432  25.729  -4.586  1.00 37.95  ? 213 LEU A C   1 
ATOM   1552 O  O   . LEU A 1 214 ? 77.183  25.317  -3.696  1.00 39.44  ? 213 LEU A O   1 
ATOM   1553 C  CB  . LEU A 1 214 ? 74.343  24.382  -4.886  1.00 38.22  ? 213 LEU A CB  1 
ATOM   1554 C  CG  . LEU A 1 214 ? 72.895  24.110  -4.479  1.00 43.39  ? 213 LEU A CG  1 
ATOM   1555 C  CD1 . LEU A 1 214 ? 72.371  22.893  -5.200  1.00 43.64  ? 213 LEU A CD1 1 
ATOM   1556 C  CD2 . LEU A 1 214 ? 72.798  23.922  -2.975  1.00 44.01  ? 213 LEU A CD2 1 
ATOM   1557 N  N   . ALA A 1 215 ? 76.891  26.212  -5.742  1.00 34.55  ? 214 ALA A N   1 
ATOM   1558 C  CA  . ALA A 1 215 ? 78.326  26.323  -5.974  1.00 36.22  ? 214 ALA A CA  1 
ATOM   1559 C  C   . ALA A 1 215 ? 78.963  27.289  -4.982  1.00 39.15  ? 214 ALA A C   1 
ATOM   1560 O  O   . ALA A 1 215 ? 80.005  26.988  -4.386  1.00 36.55  ? 214 ALA A O   1 
ATOM   1561 C  CB  . ALA A 1 215 ? 78.593  26.766  -7.411  1.00 35.75  ? 214 ALA A CB  1 
ATOM   1562 N  N   . GLY A 1 216 ? 78.338  28.456  -4.784  1.00 34.86  ? 215 GLY A N   1 
ATOM   1563 C  CA  . GLY A 1 216 ? 78.823  29.383  -3.776  1.00 36.15  ? 215 GLY A CA  1 
ATOM   1564 C  C   . GLY A 1 216 ? 78.792  28.805  -2.375  1.00 37.47  ? 215 GLY A C   1 
ATOM   1565 O  O   . GLY A 1 216 ? 79.669  29.096  -1.557  1.00 39.38  ? 215 GLY A O   1 
ATOM   1566 N  N   . GLN A 1 217 ? 77.800  27.969  -2.079  1.00 34.46  ? 216 GLN A N   1 
ATOM   1567 C  CA  . GLN A 1 217 ? 77.715  27.383  -0.747  1.00 42.37  ? 216 GLN A CA  1 
ATOM   1568 C  C   . GLN A 1 217 ? 78.784  26.319  -0.543  1.00 35.47  ? 216 GLN A C   1 
ATOM   1569 O  O   . GLN A 1 217 ? 79.396  26.245  0.529   1.00 32.17  ? 216 GLN A O   1 
ATOM   1570 C  CB  . GLN A 1 217 ? 76.323  26.801  -0.523  1.00 37.32  ? 216 GLN A CB  1 
ATOM   1571 C  CG  . GLN A 1 217 ? 75.328  27.815  -0.011  1.00 33.93  ? 216 GLN A CG  1 
ATOM   1572 C  CD  . GLN A 1 217 ? 73.934  27.253  0.052   1.00 44.30  ? 216 GLN A CD  1 
ATOM   1573 O  OE1 . GLN A 1 217 ? 73.422  26.719  -0.933  1.00 50.66  ? 216 GLN A OE1 1 
ATOM   1574 N  NE2 . GLN A 1 217 ? 73.309  27.358  1.215   1.00 45.93  ? 216 GLN A NE2 1 
ATOM   1575 N  N   . LEU A 1 218 ? 79.019  25.479  -1.553  1.00 34.29  ? 217 LEU A N   1 
ATOM   1576 C  CA  . LEU A 1 218 ? 80.092  24.500  -1.438  1.00 34.01  ? 217 LEU A CA  1 
ATOM   1577 C  C   . LEU A 1 218 ? 81.456  25.170  -1.382  1.00 35.02  ? 217 LEU A C   1 
ATOM   1578 O  O   . LEU A 1 218 ? 82.385  24.624  -0.776  1.00 33.11  ? 217 LEU A O   1 
ATOM   1579 C  CB  . LEU A 1 218 ? 80.031  23.507  -2.593  1.00 32.67  ? 217 LEU A CB  1 
ATOM   1580 C  CG  . LEU A 1 218 ? 78.816  22.586  -2.542  1.00 34.58  ? 217 LEU A CG  1 
ATOM   1581 C  CD1 . LEU A 1 218 ? 78.474  22.091  -3.933  1.00 36.45  ? 217 LEU A CD1 1 
ATOM   1582 C  CD2 . LEU A 1 218 ? 79.070  21.421  -1.582  1.00 32.17  ? 217 LEU A CD2 1 
ATOM   1583 N  N   . SER A 1 219 ? 81.588  26.355  -1.989  1.00 35.45  ? 218 SER A N   1 
ATOM   1584 C  CA  . SER A 1 219 ? 82.846  27.092  -1.932  1.00 36.43  ? 218 SER A CA  1 
ATOM   1585 C  C   . SER A 1 219 ? 83.221  27.461  -0.504  1.00 36.64  ? 218 SER A C   1 
ATOM   1586 O  O   . SER A 1 219 ? 84.411  27.594  -0.191  1.00 37.59  ? 218 SER A O   1 
ATOM   1587 C  CB  . SER A 1 219 ? 82.755  28.354  -2.788  1.00 34.51  ? 218 SER A CB  1 
ATOM   1588 O  OG  . SER A 1 219 ? 82.430  28.022  -4.125  1.00 45.36  ? 218 SER A OG  1 
ATOM   1589 N  N   . LYS A 1 220 ? 82.230  27.654  0.368   1.00 30.21  ? 219 LYS A N   1 
ATOM   1590 C  CA  . LYS A 1 220 ? 82.532  27.931  1.768   1.00 35.04  ? 219 LYS A CA  1 
ATOM   1591 C  C   . LYS A 1 220 ? 83.336  26.793  2.376   1.00 34.38  ? 219 LYS A C   1 
ATOM   1592 O  O   . LYS A 1 220 ? 84.212  27.018  3.215   1.00 33.25  ? 219 LYS A O   1 
ATOM   1593 C  CB  . LYS A 1 220 ? 81.239  28.153  2.552   1.00 32.60  ? 219 LYS A CB  1 
ATOM   1594 C  CG  . LYS A 1 220 ? 80.550  29.477  2.254   1.00 35.74  ? 219 LYS A CG  1 
ATOM   1595 C  CD  . LYS A 1 220 ? 79.573  29.840  3.361   1.00 37.53  ? 219 LYS A CD  1 
ATOM   1596 C  CE  . LYS A 1 220 ? 78.472  28.787  3.477   1.00 49.12  ? 219 LYS A CE  1 
ATOM   1597 N  NZ  . LYS A 1 220 ? 77.341  29.253  4.340   1.00 50.52  ? 219 LYS A NZ  1 
ATOM   1598 N  N   . PHE A 1 221 ? 83.066  25.564  1.948   1.00 29.19  ? 220 PHE A N   1 
ATOM   1599 C  CA  . PHE A 1 221 ? 83.818  24.431  2.463   1.00 35.83  ? 220 PHE A CA  1 
ATOM   1600 C  C   . PHE A 1 221 ? 85.198  24.342  1.820   1.00 38.51  ? 220 PHE A C   1 
ATOM   1601 O  O   . PHE A 1 221 ? 86.151  23.909  2.477   1.00 38.19  ? 220 PHE A O   1 
ATOM   1602 C  CB  . PHE A 1 221 ? 83.004  23.146  2.278   1.00 28.03  ? 220 PHE A CB  1 
ATOM   1603 C  CG  . PHE A 1 221 ? 81.730  23.128  3.087   1.00 33.53  ? 220 PHE A CG  1 
ATOM   1604 C  CD1 . PHE A 1 221 ? 80.609  23.834  2.668   1.00 32.19  ? 220 PHE A CD1 1 
ATOM   1605 C  CD2 . PHE A 1 221 ? 81.659  22.432  4.284   1.00 33.22  ? 220 PHE A CD2 1 
ATOM   1606 C  CE1 . PHE A 1 221 ? 79.447  23.834  3.422   1.00 34.74  ? 220 PHE A CE1 1 
ATOM   1607 C  CE2 . PHE A 1 221 ? 80.502  22.434  5.045   1.00 33.25  ? 220 PHE A CE2 1 
ATOM   1608 C  CZ  . PHE A 1 221 ? 79.393  23.131  4.611   1.00 35.22  ? 220 PHE A CZ  1 
ATOM   1609 N  N   . THR A 1 222 ? 85.338  24.781  0.566   1.00 34.03  ? 221 THR A N   1 
ATOM   1610 C  CA  . THR A 1 222 ? 86.674  24.958  0.010   1.00 36.86  ? 221 THR A CA  1 
ATOM   1611 C  C   . THR A 1 222 ? 87.473  25.962  0.833   1.00 32.95  ? 221 THR A C   1 
ATOM   1612 O  O   . THR A 1 222 ? 88.656  25.741  1.119   1.00 32.53  ? 221 THR A O   1 
ATOM   1613 C  CB  . THR A 1 222 ? 86.602  25.416  -1.450  1.00 36.16  ? 221 THR A CB  1 
ATOM   1614 O  OG1 . THR A 1 222 ? 85.907  24.441  -2.237  1.00 36.82  ? 221 THR A OG1 1 
ATOM   1615 C  CG2 . THR A 1 222 ? 88.004  25.579  -2.012  1.00 35.94  ? 221 THR A CG2 1 
ATOM   1616 N  N   . LEU A 1 223 ? 86.837  27.064  1.244   1.00 31.20  ? 222 LEU A N   1 
ATOM   1617 C  CA  . LEU A 1 223 ? 87.566  28.089  1.982   1.00 31.47  ? 222 LEU A CA  1 
ATOM   1618 C  C   . LEU A 1 223 ? 87.963  27.605  3.371   1.00 34.76  ? 222 LEU A C   1 
ATOM   1619 O  O   . LEU A 1 223 ? 89.041  27.951  3.860   1.00 38.52  ? 222 LEU A O   1 
ATOM   1620 C  CB  . LEU A 1 223 ? 86.734  29.366  2.069   1.00 37.99  ? 222 LEU A CB  1 
ATOM   1621 C  CG  . LEU A 1 223 ? 86.298  29.979  0.729   1.00 42.41  ? 222 LEU A CG  1 
ATOM   1622 C  CD1 . LEU A 1 223 ? 84.974  30.713  0.882   1.00 45.31  ? 222 LEU A CD1 1 
ATOM   1623 C  CD2 . LEU A 1 223 ? 87.348  30.902  0.154   1.00 36.74  ? 222 LEU A CD2 1 
ATOM   1624 N  N   . MET A 1 224 ? 87.123  26.796  4.018   1.00 32.22  ? 223 MET A N   1 
ATOM   1625 C  CA  . MET A 1 224 ? 87.537  26.194  5.279   1.00 41.84  ? 223 MET A CA  1 
ATOM   1626 C  C   . MET A 1 224 ? 88.704  25.237  5.075   1.00 35.00  ? 223 MET A C   1 
ATOM   1627 O  O   . MET A 1 224 ? 89.635  25.215  5.886   1.00 39.39  ? 223 MET A O   1 
ATOM   1628 C  CB  . MET A 1 224 ? 86.361  25.488  5.959   1.00 36.47  ? 223 MET A CB  1 
ATOM   1629 C  CG  . MET A 1 224 ? 85.112  26.342  6.016   1.00 41.24  ? 223 MET A CG  1 
ATOM   1630 S  SD  . MET A 1 224 ? 83.689  25.630  6.869   1.00 52.20  ? 223 MET A SD  1 
ATOM   1631 C  CE  . MET A 1 224 ? 83.658  24.018  6.174   1.00 34.26  ? 223 MET A CE  1 
ATOM   1632 N  N   . ALA A 1 225 ? 88.688  24.458  3.993   1.00 33.11  ? 224 ALA A N   1 
ATOM   1633 C  CA  . ALA A 1 225 ? 89.818  23.577  3.713   1.00 41.20  ? 224 ALA A CA  1 
ATOM   1634 C  C   . ALA A 1 225 ? 91.098  24.379  3.491   1.00 44.82  ? 224 ALA A C   1 
ATOM   1635 O  O   . ALA A 1 225 ? 92.175  23.992  3.959   1.00 41.61  ? 224 ALA A O   1 
ATOM   1636 C  CB  . ALA A 1 225 ? 89.512  22.700  2.500   1.00 41.77  ? 224 ALA A CB  1 
ATOM   1637 N  N   . LEU A 1 226 ? 90.992  25.509  2.789   1.00 37.51  ? 225 LEU A N   1 
ATOM   1638 C  CA  . LEU A 1 226 ? 92.155  26.358  2.566   1.00 39.47  ? 225 LEU A CA  1 
ATOM   1639 C  C   . LEU A 1 226 ? 92.688  26.921  3.876   1.00 43.58  ? 225 LEU A C   1 
ATOM   1640 O  O   . LEU A 1 226 ? 93.903  26.916  4.112   1.00 49.03  ? 225 LEU A O   1 
ATOM   1641 C  CB  . LEU A 1 226 ? 91.791  27.489  1.609   1.00 40.59  ? 225 LEU A CB  1 
ATOM   1642 C  CG  . LEU A 1 226 ? 92.174  27.266  0.153   1.00 46.51  ? 225 LEU A CG  1 
ATOM   1643 C  CD1 . LEU A 1 226 ? 91.577  28.364  -0.717  1.00 46.01  ? 225 LEU A CD1 1 
ATOM   1644 C  CD2 . LEU A 1 226 ? 93.678  27.221  0.020   1.00 48.58  ? 225 LEU A CD2 1 
ATOM   1645 N  N   . ILE A 1 227 ? 91.796  27.417  4.738   1.00 43.13  ? 226 ILE A N   1 
ATOM   1646 C  CA  . ILE A 1 227 ? 92.226  27.982  6.014   1.00 43.09  ? 226 ILE A CA  1 
ATOM   1647 C  C   . ILE A 1 227 ? 92.869  26.910  6.882   1.00 45.08  ? 226 ILE A C   1 
ATOM   1648 O  O   . ILE A 1 227 ? 93.904  27.140  7.519   1.00 44.51  ? 226 ILE A O   1 
ATOM   1649 C  CB  . ILE A 1 227 ? 91.037  28.646  6.733   1.00 44.76  ? 226 ILE A CB  1 
ATOM   1650 C  CG1 . ILE A 1 227 ? 90.566  29.872  5.958   1.00 39.81  ? 226 ILE A CG1 1 
ATOM   1651 C  CG2 . ILE A 1 227 ? 91.417  29.038  8.154   1.00 40.04  ? 226 ILE A CG2 1 
ATOM   1652 C  CD1 . ILE A 1 227 ? 89.122  30.214  6.196   1.00 40.27  ? 226 ILE A CD1 1 
ATOM   1653 N  N   . THR A 1 228 ? 92.274  25.718  6.909   1.00 42.20  ? 227 THR A N   1 
ATOM   1654 C  CA  . THR A 1 228 ? 92.768  24.665  7.785   1.00 44.97  ? 227 THR A CA  1 
ATOM   1655 C  C   . THR A 1 228 ? 94.153  24.197  7.367   1.00 50.80  ? 227 THR A C   1 
ATOM   1656 O  O   . THR A 1 228 ? 94.988  23.876  8.223   1.00 52.01  ? 227 THR A O   1 
ATOM   1657 C  CB  . THR A 1 228 ? 91.776  23.503  7.794   1.00 48.50  ? 227 THR A CB  1 
ATOM   1658 O  OG1 . THR A 1 228 ? 90.789  23.743  8.802   1.00 49.21  ? 227 THR A OG1 1 
ATOM   1659 C  CG2 . THR A 1 228 ? 92.473  22.175  8.080   1.00 44.17  ? 227 THR A CG2 1 
ATOM   1660 N  N   . SER A 1 229 ? 94.432  24.190  6.067   1.00 51.96  ? 228 SER A N   1 
ATOM   1661 C  CA  . SER A 1 229 ? 95.729  23.732  5.590   1.00 57.66  ? 228 SER A CA  1 
ATOM   1662 C  C   . SER A 1 229 ? 96.862  24.703  5.901   1.00 54.32  ? 228 SER A C   1 
ATOM   1663 O  O   . SER A 1 229 ? 98.002  24.417  5.525   1.00 53.26  ? 228 SER A O   1 
ATOM   1664 C  CB  . SER A 1 229 ? 95.664  23.468  4.083   1.00 58.77  ? 228 SER A CB  1 
ATOM   1665 O  OG  . SER A 1 229 ? 95.487  24.671  3.354   1.00 57.07  ? 228 SER A OG  1 
ATOM   1666 N  N   . VAL A 1 230 ? 96.596  25.823  6.576   1.00 51.17  ? 229 VAL A N   1 
ATOM   1667 C  CA  . VAL A 1 230 ? 97.633  26.815  6.844   1.00 46.16  ? 229 VAL A CA  1 
ATOM   1668 C  C   . VAL A 1 230 ? 97.819  27.009  8.344   1.00 50.16  ? 229 VAL A C   1 
ATOM   1669 O  O   . VAL A 1 230 ? 98.916  26.796  8.868   1.00 53.77  ? 229 VAL A O   1 
ATOM   1670 C  CB  . VAL A 1 230 ? 97.310  28.156  6.157   1.00 45.04  ? 229 VAL A CB  1 
ATOM   1671 C  CG1 . VAL A 1 230 ? 98.133  29.285  6.766   1.00 48.68  ? 229 VAL A CG1 1 
ATOM   1672 C  CG2 . VAL A 1 230 ? 97.570  28.063  4.666   1.00 51.47  ? 229 VAL A CG2 1 
ATOM   1673 N  N   . THR A 1 231 ? 96.748  27.392  9.045   1.00 52.19  ? 230 THR A N   1 
ATOM   1674 C  CA  . THR A 1 231 ? 96.837  27.941  10.397  1.00 56.72  ? 230 THR A CA  1 
ATOM   1675 C  C   . THR A 1 231 ? 97.589  27.052  11.379  1.00 55.47  ? 230 THR A C   1 
ATOM   1676 O  O   . THR A 1 231 ? 98.667  27.421  11.857  1.00 59.47  ? 230 THR A O   1 
ATOM   1677 C  CB  . THR A 1 231 ? 95.442  28.208  10.955  1.00 49.61  ? 230 THR A CB  1 
ATOM   1678 O  OG1 . THR A 1 231 ? 94.802  26.956  11.204  1.00 54.65  ? 230 THR A OG1 1 
ATOM   1679 C  CG2 . THR A 1 231 ? 94.618  29.020  9.971   1.00 46.50  ? 230 THR A CG2 1 
ATOM   1680 N  N   . LEU A 1 232 ? 97.024  25.897  11.705  1.00 46.74  ? 231 LEU A N   1 
ATOM   1681 C  CA  . LEU A 1 232 ? 97.666  25.017  12.675  1.00 54.33  ? 231 LEU A CA  1 
ATOM   1682 C  C   . LEU A 1 232 ? 98.926  24.356  12.113  1.00 54.35  ? 231 LEU A C   1 
ATOM   1683 O  O   . LEU A 1 232 ? 99.895  24.180  12.860  1.00 49.24  ? 231 LEU A O   1 
ATOM   1684 C  CB  . LEU A 1 232 ? 96.677  23.967  13.185  1.00 54.60  ? 231 LEU A CB  1 
ATOM   1685 C  CG  . LEU A 1 232 ? 95.606  24.550  14.114  1.00 58.56  ? 231 LEU A CG  1 
ATOM   1686 C  CD1 . LEU A 1 232 ? 94.668  23.471  14.622  1.00 53.55  ? 231 LEU A CD1 1 
ATOM   1687 C  CD2 . LEU A 1 232 ? 96.246  25.297  15.276  1.00 50.10  ? 231 LEU A CD2 1 
ATOM   1688 N  N   . PRO A 1 233 ? 98.969  23.961  10.831  1.00 52.37  ? 232 PRO A N   1 
ATOM   1689 C  CA  . PRO A 1 233 ? 100.263 23.542  10.259  1.00 42.59  ? 232 PRO A CA  1 
ATOM   1690 C  C   . PRO A 1 233 ? 101.363 24.575  10.451  1.00 52.08  ? 232 PRO A C   1 
ATOM   1691 O  O   . PRO A 1 233 ? 102.487 24.226  10.840  1.00 46.65  ? 232 PRO A O   1 
ATOM   1692 C  CB  . PRO A 1 233 ? 99.927  23.325  8.780   1.00 48.52  ? 232 PRO A CB  1 
ATOM   1693 C  CG  . PRO A 1 233 ? 98.512  22.904  8.791   1.00 51.90  ? 232 PRO A CG  1 
ATOM   1694 C  CD  . PRO A 1 233 ? 97.849  23.641  9.923   1.00 48.88  ? 232 PRO A CD  1 
ATOM   1695 N  N   . VAL A 1 234 ? 101.066 25.848  10.173  1.00 54.44  ? 233 VAL A N   1 
ATOM   1696 C  CA  . VAL A 1 234 ? 102.000 26.923  10.492  1.00 47.32  ? 233 VAL A CA  1 
ATOM   1697 C  C   . VAL A 1 234 ? 102.355 26.885  11.968  1.00 46.22  ? 233 VAL A C   1 
ATOM   1698 O  O   . VAL A 1 234 ? 103.512 27.089  12.354  1.00 48.12  ? 233 VAL A O   1 
ATOM   1699 C  CB  . VAL A 1 234 ? 101.396 28.283  10.103  1.00 47.33  ? 233 VAL A CB  1 
ATOM   1700 C  CG1 . VAL A 1 234 ? 101.938 29.373  11.003  1.00 44.25  ? 233 VAL A CG1 1 
ATOM   1701 C  CG2 . VAL A 1 234 ? 101.669 28.591  8.649   1.00 47.10  ? 233 VAL A CG2 1 
ATOM   1702 N  N   . ALA A 1 235 ? 101.362 26.610  12.813  1.00 45.63  ? 234 ALA A N   1 
ATOM   1703 C  CA  . ALA A 1 235 ? 101.591 26.598  14.250  1.00 50.10  ? 234 ALA A CA  1 
ATOM   1704 C  C   . ALA A 1 235 ? 102.591 25.517  14.641  1.00 49.32  ? 234 ALA A C   1 
ATOM   1705 O  O   . ALA A 1 235 ? 103.530 25.770  15.405  1.00 48.10  ? 234 ALA A O   1 
ATOM   1706 C  CB  . ALA A 1 235 ? 100.265 26.414  14.993  1.00 54.43  ? 234 ALA A CB  1 
ATOM   1707 N  N   . TYR A 1 236 ? 102.413 24.303  14.115  1.00 45.75  ? 235 TYR A N   1 
ATOM   1708 C  CA  . TYR A 1 236 ? 103.342 23.225  14.428  1.00 48.87  ? 235 TYR A CA  1 
ATOM   1709 C  C   . TYR A 1 236 ? 104.708 23.441  13.788  1.00 48.49  ? 235 TYR A C   1 
ATOM   1710 O  O   . TYR A 1 236 ? 105.709 22.943  14.314  1.00 44.96  ? 235 TYR A O   1 
ATOM   1711 C  CB  . TYR A 1 236 ? 102.744 21.881  14.010  1.00 50.45  ? 235 TYR A CB  1 
ATOM   1712 C  CG  . TYR A 1 236 ? 101.561 21.480  14.877  1.00 55.64  ? 235 TYR A CG  1 
ATOM   1713 C  CD1 . TYR A 1 236 ? 101.754 20.848  16.100  1.00 55.39  ? 235 TYR A CD1 1 
ATOM   1714 C  CD2 . TYR A 1 236 ? 100.254 21.741  14.477  1.00 52.62  ? 235 TYR A CD2 1 
ATOM   1715 C  CE1 . TYR A 1 236 ? 100.681 20.489  16.902  1.00 52.85  ? 235 TYR A CE1 1 
ATOM   1716 C  CE2 . TYR A 1 236 ? 99.173  21.383  15.275  1.00 54.75  ? 235 TYR A CE2 1 
ATOM   1717 C  CZ  . TYR A 1 236 ? 99.397  20.758  16.483  1.00 50.82  ? 235 TYR A CZ  1 
ATOM   1718 O  OH  . TYR A 1 236 ? 98.336  20.396  17.280  1.00 58.95  ? 235 TYR A OH  1 
ATOM   1719 N  N   . ILE A 1 237 ? 104.778 24.200  12.692  1.00 50.16  ? 236 ILE A N   1 
ATOM   1720 C  CA  . ILE A 1 237 ? 106.063 24.455  12.048  1.00 43.87  ? 236 ILE A CA  1 
ATOM   1721 C  C   . ILE A 1 237 ? 106.938 25.328  12.933  1.00 49.30  ? 236 ILE A C   1 
ATOM   1722 O  O   . ILE A 1 237 ? 108.106 25.013  13.182  1.00 60.33  ? 236 ILE A O   1 
ATOM   1723 C  CB  . ILE A 1 237 ? 105.862 25.090  10.662  1.00 48.59  ? 236 ILE A CB  1 
ATOM   1724 C  CG1 . ILE A 1 237 ? 105.716 24.002  9.601   1.00 55.42  ? 236 ILE A CG1 1 
ATOM   1725 C  CG2 . ILE A 1 237 ? 107.041 25.989  10.312  1.00 46.52  ? 236 ILE A CG2 1 
ATOM   1726 C  CD1 . ILE A 1 237 ? 105.501 24.543  8.205   1.00 57.71  ? 236 ILE A CD1 1 
ATOM   1727 N  N   . MET A 1 238 ? 106.398 26.443  13.417  1.00 48.73  ? 237 MET A N   1 
ATOM   1728 C  CA  . MET A 1 238 ? 107.199 27.272  14.304  1.00 53.57  ? 237 MET A CA  1 
ATOM   1729 C  C   . MET A 1 238 ? 107.176 26.780  15.746  1.00 51.29  ? 237 MET A C   1 
ATOM   1730 O  O   . MET A 1 238 ? 107.923 27.305  16.577  1.00 51.32  ? 237 MET A O   1 
ATOM   1731 C  CB  . MET A 1 238 ? 106.763 28.740  14.208  1.00 63.77  ? 237 MET A CB  1 
ATOM   1732 C  CG  . MET A 1 238 ? 105.334 29.024  14.583  1.00 58.54  ? 237 MET A CG  1 
ATOM   1733 S  SD  . MET A 1 238 ? 104.976 30.792  14.753  1.00 69.32  ? 237 MET A SD  1 
ATOM   1734 C  CE  . MET A 1 238 ? 103.415 30.927  13.899  1.00 41.73  ? 237 MET A CE  1 
ATOM   1735 N  N   . MET A 1 239 ? 106.363 25.773  16.059  1.00 48.87  ? 238 MET A N   1 
ATOM   1736 C  CA  . MET A 1 239 ? 106.599 25.016  17.282  1.00 49.11  ? 238 MET A CA  1 
ATOM   1737 C  C   . MET A 1 239 ? 107.876 24.198  17.161  1.00 52.84  ? 238 MET A C   1 
ATOM   1738 O  O   . MET A 1 239 ? 108.694 24.167  18.088  1.00 53.61  ? 238 MET A O   1 
ATOM   1739 C  CB  . MET A 1 239 ? 105.409 24.115  17.583  1.00 46.06  ? 238 MET A CB  1 
ATOM   1740 C  CG  . MET A 1 239 ? 104.557 24.625  18.712  1.00 47.27  ? 238 MET A CG  1 
ATOM   1741 S  SD  . MET A 1 239 ? 103.106 23.606  18.969  1.00 51.96  ? 238 MET A SD  1 
ATOM   1742 C  CE  . MET A 1 239 ? 103.572 22.724  20.453  1.00 48.65  ? 238 MET A CE  1 
ATOM   1743 N  N   . ARG A 1 240 ? 108.065 23.533  16.019  1.00 51.96  ? 239 ARG A N   1 
ATOM   1744 C  CA  . ARG A 1 240 ? 109.325 22.846  15.769  1.00 52.07  ? 239 ARG A CA  1 
ATOM   1745 C  C   . ARG A 1 240 ? 110.488 23.828  15.726  1.00 51.16  ? 239 ARG A C   1 
ATOM   1746 O  O   . ARG A 1 240 ? 111.603 23.489  16.136  1.00 52.69  ? 239 ARG A O   1 
ATOM   1747 C  CB  . ARG A 1 240 ? 109.234 22.048  14.468  1.00 47.95  ? 239 ARG A CB  1 
ATOM   1748 C  CG  . ARG A 1 240 ? 110.567 21.562  13.932  1.00 54.45  ? 239 ARG A CG  1 
ATOM   1749 C  CD  . ARG A 1 240 ? 110.380 20.717  12.688  1.00 58.83  ? 239 ARG A CD  1 
ATOM   1750 N  NE  . ARG A 1 240 ? 109.668 21.441  11.642  1.00 66.00  ? 239 ARG A NE  1 
ATOM   1751 C  CZ  . ARG A 1 240 ? 110.178 22.444  10.939  1.00 67.52  ? 239 ARG A CZ  1 
ATOM   1752 N  NH1 . ARG A 1 240 ? 111.415 22.871  11.136  1.00 68.78  ? 239 ARG A NH1 1 
ATOM   1753 N  NH2 . ARG A 1 240 ? 109.428 23.031  10.012  1.00 68.48  ? 239 ARG A NH2 1 
ATOM   1754 N  N   . LYS A 1 241 ? 110.245 25.051  15.250  1.00 51.56  ? 240 LYS A N   1 
ATOM   1755 C  CA  . LYS A 1 241 ? 111.285 26.075  15.250  1.00 53.06  ? 240 LYS A CA  1 
ATOM   1756 C  C   . LYS A 1 241 ? 111.731 26.400  16.671  1.00 55.87  ? 240 LYS A C   1 
ATOM   1757 O  O   . LYS A 1 241 ? 112.932 26.431  16.966  1.00 57.55  ? 240 LYS A O   1 
ATOM   1758 C  CB  . LYS A 1 241 ? 110.772 27.328  14.536  1.00 61.43  ? 240 LYS A CB  1 
ATOM   1759 C  CG  . LYS A 1 241 ? 111.843 28.246  13.973  1.00 63.59  ? 240 LYS A CG  1 
ATOM   1760 C  CD  . LYS A 1 241 ? 112.381 29.196  15.035  1.00 71.29  ? 240 LYS A CD  1 
ATOM   1761 C  CE  . LYS A 1 241 ? 111.256 29.947  15.728  1.00 69.26  ? 240 LYS A CE  1 
ATOM   1762 N  NZ  . LYS A 1 241 ? 111.696 30.527  17.028  1.00 70.79  ? 240 LYS A NZ  1 
ATOM   1763 N  N   . LEU A 1 242 ? 110.771 26.656  17.565  1.00 53.59  ? 241 LEU A N   1 
ATOM   1764 C  CA  . LEU A 1 242 ? 111.097 26.906  18.967  1.00 53.30  ? 241 LEU A CA  1 
ATOM   1765 C  C   . LEU A 1 242 ? 111.861 25.734  19.568  1.00 54.21  ? 241 LEU A C   1 
ATOM   1766 O  O   . LEU A 1 242 ? 112.791 25.926  20.360  1.00 57.80  ? 241 LEU A O   1 
ATOM   1767 C  CB  . LEU A 1 242 ? 109.818 27.158  19.766  1.00 51.63  ? 241 LEU A CB  1 
ATOM   1768 C  CG  . LEU A 1 242 ? 109.249 28.571  19.854  1.00 52.19  ? 241 LEU A CG  1 
ATOM   1769 C  CD1 . LEU A 1 242 ? 107.727 28.518  19.915  1.00 57.33  ? 241 LEU A CD1 1 
ATOM   1770 C  CD2 . LEU A 1 242 ? 109.806 29.290  21.062  1.00 57.51  ? 241 LEU A CD2 1 
ATOM   1771 N  N   . LEU A 1 243 ? 111.471 24.511  19.205  1.00 49.93  ? 242 LEU A N   1 
ATOM   1772 C  CA  . LEU A 1 243 ? 112.138 23.320  19.716  1.00 49.32  ? 242 LEU A CA  1 
ATOM   1773 C  C   . LEU A 1 243 ? 113.596 23.277  19.279  1.00 58.71  ? 242 LEU A C   1 
ATOM   1774 O  O   . LEU A 1 243 ? 114.497 23.071  20.099  1.00 61.71  ? 242 LEU A O   1 
ATOM   1775 C  CB  . LEU A 1 243 ? 111.397 22.073  19.235  1.00 52.97  ? 242 LEU A CB  1 
ATOM   1776 C  CG  . LEU A 1 243 ? 110.556 21.308  20.254  1.00 54.47  ? 242 LEU A CG  1 
ATOM   1777 C  CD1 . LEU A 1 243 ? 110.388 19.870  19.804  1.00 58.34  ? 242 LEU A CD1 1 
ATOM   1778 C  CD2 . LEU A 1 243 ? 111.192 21.366  21.632  1.00 53.24  ? 242 LEU A CD2 1 
ATOM   1779 N  N   . ALA A 1 244 ? 113.848 23.471  17.983  1.00 58.76  ? 243 ALA A N   1 
ATOM   1780 C  CA  . ALA A 1 244 ? 115.214 23.382  17.482  1.00 59.61  ? 243 ALA A CA  1 
ATOM   1781 C  C   . ALA A 1 244 ? 116.076 24.535  17.976  1.00 62.38  ? 243 ALA A C   1 
ATOM   1782 O  O   . ALA A 1 244 ? 117.300 24.391  18.075  1.00 67.69  ? 243 ALA A O   1 
ATOM   1783 C  CB  . ALA A 1 244 ? 115.211 23.341  15.956  1.00 57.73  ? 243 ALA A CB  1 
ATOM   1784 N  N   . ALA A 1 245 ? 115.460 25.676  18.300  1.00 60.67  ? 244 ALA A N   1 
ATOM   1785 C  CA  . ALA A 1 245 ? 116.232 26.851  18.693  1.00 63.87  ? 244 ALA A CA  1 
ATOM   1786 C  C   . ALA A 1 245 ? 117.004 26.621  19.985  1.00 68.93  ? 244 ALA A C   1 
ATOM   1787 O  O   . ALA A 1 245 ? 118.072 27.211  20.185  1.00 71.50  ? 244 ALA A O   1 
ATOM   1788 C  CB  . ALA A 1 245 ? 115.308 28.060  18.840  1.00 63.81  ? 244 ALA A CB  1 
ATOM   1789 N  N   . GLN A 1 246 ? 116.489 25.771  20.870  1.00 64.70  ? 245 GLN A N   1 
ATOM   1790 C  CA  . GLN A 1 246 ? 117.112 25.549  22.162  1.00 66.90  ? 245 GLN A CA  1 
ATOM   1791 C  C   . GLN A 1 246 ? 117.407 24.087  22.452  1.00 69.05  ? 245 GLN A C   1 
ATOM   1792 O  O   . GLN A 1 246 ? 117.924 23.784  23.532  1.00 71.26  ? 245 GLN A O   1 
ATOM   1793 C  CB  . GLN A 1 246 ? 116.226 26.110  23.284  1.00 71.86  ? 245 GLN A CB  1 
ATOM   1794 C  CG  . GLN A 1 246 ? 116.177 27.625  23.339  1.00 85.50  ? 245 GLN A CG  1 
ATOM   1795 C  CD  . GLN A 1 246 ? 115.728 28.136  24.692  1.00 89.92  ? 245 GLN A CD  1 
ATOM   1796 O  OE1 . GLN A 1 246 ? 115.904 27.465  25.709  1.00 86.48  ? 245 GLN A OE1 1 
ATOM   1797 N  NE2 . GLN A 1 246 ? 115.145 29.328  24.711  1.00 92.36  ? 245 GLN A NE2 1 
ATOM   1798 N  N   . TYR A 1 247 ? 117.091 23.175  21.538  1.00 69.16  ? 246 TYR A N   1 
ATOM   1799 C  CA  . TYR A 1 247 ? 117.281 21.755  21.785  1.00 66.06  ? 246 TYR A CA  1 
ATOM   1800 C  C   . TYR A 1 247 ? 117.808 21.088  20.524  1.00 72.10  ? 246 TYR A C   1 
ATOM   1801 O  O   . TYR A 1 247 ? 117.927 21.707  19.462  1.00 68.71  ? 246 TYR A O   1 
ATOM   1802 C  CB  . TYR A 1 247 ? 115.979 21.091  22.253  1.00 61.74  ? 246 TYR A CB  1 
ATOM   1803 C  CG  . TYR A 1 247 ? 115.512 21.585  23.605  1.00 68.85  ? 246 TYR A CG  1 
ATOM   1804 C  CD1 . TYR A 1 247 ? 114.699 22.709  23.715  1.00 64.37  ? 246 TYR A CD1 1 
ATOM   1805 C  CD2 . TYR A 1 247 ? 115.890 20.935  24.770  1.00 70.87  ? 246 TYR A CD2 1 
ATOM   1806 C  CE1 . TYR A 1 247 ? 114.276 23.169  24.948  1.00 60.98  ? 246 TYR A CE1 1 
ATOM   1807 C  CE2 . TYR A 1 247 ? 115.469 21.385  26.009  1.00 69.82  ? 246 TYR A CE2 1 
ATOM   1808 C  CZ  . TYR A 1 247 ? 114.664 22.502  26.092  1.00 64.73  ? 246 TYR A CZ  1 
ATOM   1809 O  OH  . TYR A 1 247 ? 114.248 22.951  27.325  1.00 61.10  ? 246 TYR A OH  1 
ATOM   1810 N  N   . SER A 1 248 ? 118.135 19.807  20.662  1.00 73.03  ? 247 SER A N   1 
ATOM   1811 C  CA  . SER A 1 248 ? 118.703 19.031  19.575  1.00 75.12  ? 247 SER A CA  1 
ATOM   1812 C  C   . SER A 1 248 ? 117.613 18.582  18.606  1.00 74.35  ? 247 SER A C   1 
ATOM   1813 O  O   . SER A 1 248 ? 116.414 18.669  18.885  1.00 74.22  ? 247 SER A O   1 
ATOM   1814 C  CB  . SER A 1 248 ? 119.452 17.818  20.126  1.00 80.02  ? 247 SER A CB  1 
ATOM   1815 O  OG  . SER A 1 248 ? 118.559 16.918  20.763  1.00 72.40  ? 247 SER A OG  1 
ATOM   1816 N  N   . TRP A 1 249 ? 118.051 18.095  17.443  1.00 76.20  ? 248 TRP A N   1 
ATOM   1817 C  CA  . TRP A 1 249 ? 117.126 17.498  16.490  1.00 80.03  ? 248 TRP A CA  1 
ATOM   1818 C  C   . TRP A 1 249 ? 116.520 16.205  17.019  1.00 76.79  ? 248 TRP A C   1 
ATOM   1819 O  O   . TRP A 1 249 ? 115.426 15.823  16.586  1.00 67.12  ? 248 TRP A O   1 
ATOM   1820 C  CB  . TRP A 1 249 ? 117.837 17.245  15.158  1.00 81.88  ? 248 TRP A CB  1 
ATOM   1821 C  CG  . TRP A 1 249 ? 118.263 18.503  14.449  1.00 92.18  ? 248 TRP A CG  1 
ATOM   1822 C  CD1 . TRP A 1 249 ? 119.539 18.863  14.116  1.00 98.23  ? 248 TRP A CD1 1 
ATOM   1823 C  CD2 . TRP A 1 249 ? 117.413 19.558  13.974  1.00 92.59  ? 248 TRP A CD2 1 
ATOM   1824 N  NE1 . TRP A 1 249 ? 119.536 20.078  13.472  1.00 101.41 ? 248 TRP A NE1 1 
ATOM   1825 C  CE2 . TRP A 1 249 ? 118.244 20.525  13.372  1.00 97.09  ? 248 TRP A CE2 1 
ATOM   1826 C  CE3 . TRP A 1 249 ? 116.031 19.779  14.002  1.00 91.76  ? 248 TRP A CE3 1 
ATOM   1827 C  CZ2 . TRP A 1 249 ? 117.740 21.695  12.803  1.00 92.72  ? 248 TRP A CZ2 1 
ATOM   1828 C  CZ3 . TRP A 1 249 ? 115.532 20.941  13.436  1.00 88.07  ? 248 TRP A CZ3 1 
ATOM   1829 C  CH2 . TRP A 1 249 ? 116.385 21.885  12.846  1.00 88.51  ? 248 TRP A CH2 1 
ATOM   1830 N  N   . ASP A 1 250 ? 117.207 15.528  17.946  1.00 64.07  ? 249 ASP A N   1 
ATOM   1831 C  CA  . ASP A 1 250 ? 116.653 14.324  18.554  1.00 69.75  ? 249 ASP A CA  1 
ATOM   1832 C  C   . ASP A 1 250 ? 115.366 14.635  19.303  1.00 65.00  ? 249 ASP A C   1 
ATOM   1833 O  O   . ASP A 1 250 ? 114.352 13.952  19.126  1.00 58.95  ? 249 ASP A O   1 
ATOM   1834 C  CB  . ASP A 1 250 ? 117.677 13.689  19.491  1.00 70.34  ? 249 ASP A CB  1 
ATOM   1835 C  CG  . ASP A 1 250 ? 118.363 12.497  18.871  1.00 84.46  ? 249 ASP A CG  1 
ATOM   1836 O  OD1 . ASP A 1 250 ? 118.873 11.637  19.623  1.00 87.24  ? 249 ASP A OD1 1 
ATOM   1837 O  OD2 . ASP A 1 250 ? 118.382 12.417  17.625  1.00 87.15  ? 249 ASP A OD2 1 
ATOM   1838 N  N   . GLU A 1 251 ? 115.393 15.668  20.149  1.00 66.03  ? 250 GLU A N   1 
ATOM   1839 C  CA  . GLU A 1 251 ? 114.184 16.084  20.850  1.00 68.18  ? 250 GLU A CA  1 
ATOM   1840 C  C   . GLU A 1 251 ? 113.107 16.535  19.873  1.00 57.50  ? 250 GLU A C   1 
ATOM   1841 O  O   . GLU A 1 251 ? 111.913 16.313  20.109  1.00 56.26  ? 250 GLU A O   1 
ATOM   1842 C  CB  . GLU A 1 251 ? 114.509 17.202  21.838  1.00 66.55  ? 250 GLU A CB  1 
ATOM   1843 C  CG  . GLU A 1 251 ? 113.420 17.432  22.862  1.00 63.02  ? 250 GLU A CG  1 
ATOM   1844 C  CD  . GLU A 1 251 ? 113.955 17.544  24.266  1.00 58.12  ? 250 GLU A CD  1 
ATOM   1845 O  OE1 . GLU A 1 251 ? 115.131 17.189  24.480  1.00 66.76  ? 250 GLU A OE1 1 
ATOM   1846 O  OE2 . GLU A 1 251 ? 113.199 17.985  25.156  1.00 54.17  ? 250 GLU A OE2 1 
ATOM   1847 N  N   . VAL A 1 252 ? 113.510 17.176  18.774  1.00 58.54  ? 251 VAL A N   1 
ATOM   1848 C  CA  . VAL A 1 252 ? 112.551 17.565  17.745  1.00 60.80  ? 251 VAL A CA  1 
ATOM   1849 C  C   . VAL A 1 252 ? 111.877 16.331  17.164  1.00 55.05  ? 251 VAL A C   1 
ATOM   1850 O  O   . VAL A 1 252 ? 110.655 16.302  16.969  1.00 53.32  ? 251 VAL A O   1 
ATOM   1851 C  CB  . VAL A 1 252 ? 113.251 18.396  16.652  1.00 66.38  ? 251 VAL A CB  1 
ATOM   1852 C  CG1 . VAL A 1 252 ? 112.470 18.331  15.344  1.00 62.86  ? 251 VAL A CG1 1 
ATOM   1853 C  CG2 . VAL A 1 252 ? 113.435 19.837  17.108  1.00 65.28  ? 251 VAL A CG2 1 
ATOM   1854 N  N   . GLY A 1 253 ? 112.662 15.288  16.888  1.00 54.78  ? 252 GLY A N   1 
ATOM   1855 C  CA  . GLY A 1 253 ? 112.087 14.056  16.377  1.00 54.78  ? 252 GLY A CA  1 
ATOM   1856 C  C   . GLY A 1 253 ? 111.153 13.390  17.368  1.00 58.54  ? 252 GLY A C   1 
ATOM   1857 O  O   . GLY A 1 253 ? 110.129 12.822  16.977  1.00 55.98  ? 252 GLY A O   1 
ATOM   1858 N  N   . ILE A 1 254 ? 111.490 13.451  18.661  1.00 59.85  ? 253 ILE A N   1 
ATOM   1859 C  CA  . ILE A 1 254 ? 110.623 12.883  19.694  1.00 61.50  ? 253 ILE A CA  1 
ATOM   1860 C  C   . ILE A 1 254 ? 109.247 13.535  19.635  1.00 51.90  ? 253 ILE A C   1 
ATOM   1861 O  O   . ILE A 1 254 ? 108.213 12.858  19.663  1.00 54.98  ? 253 ILE A O   1 
ATOM   1862 C  CB  . ILE A 1 254 ? 111.258 13.048  21.090  1.00 61.14  ? 253 ILE A CB  1 
ATOM   1863 C  CG1 . ILE A 1 254 ? 112.034 11.797  21.506  1.00 65.37  ? 253 ILE A CG1 1 
ATOM   1864 C  CG2 . ILE A 1 254 ? 110.200 13.346  22.146  1.00 58.42  ? 253 ILE A CG2 1 
ATOM   1865 C  CD1 . ILE A 1 254 ? 113.257 11.542  20.683  1.00 72.50  ? 253 ILE A CD1 1 
ATOM   1866 N  N   . TRP A 1 255 ? 109.217 14.865  19.533  1.00 53.10  ? 254 TRP A N   1 
ATOM   1867 C  CA  . TRP A 1 255 ? 107.947 15.582  19.513  1.00 51.94  ? 254 TRP A CA  1 
ATOM   1868 C  C   . TRP A 1 255 ? 107.191 15.327  18.216  1.00 49.66  ? 254 TRP A C   1 
ATOM   1869 O  O   . TRP A 1 255 ? 105.983 15.064  18.238  1.00 45.94  ? 254 TRP A O   1 
ATOM   1870 C  CB  . TRP A 1 255 ? 108.195 17.078  19.714  1.00 50.56  ? 254 TRP A CB  1 
ATOM   1871 C  CG  . TRP A 1 255 ? 107.125 17.968  19.145  1.00 47.55  ? 254 TRP A CG  1 
ATOM   1872 C  CD1 . TRP A 1 255 ? 107.247 18.832  18.093  1.00 46.64  ? 254 TRP A CD1 1 
ATOM   1873 C  CD2 . TRP A 1 255 ? 105.777 18.089  19.606  1.00 41.44  ? 254 TRP A CD2 1 
ATOM   1874 N  NE1 . TRP A 1 255 ? 106.057 19.476  17.869  1.00 47.71  ? 254 TRP A NE1 1 
ATOM   1875 C  CE2 . TRP A 1 255 ? 105.137 19.037  18.784  1.00 49.74  ? 254 TRP A CE2 1 
ATOM   1876 C  CE3 . TRP A 1 255 ? 105.044 17.479  20.628  1.00 49.26  ? 254 TRP A CE3 1 
ATOM   1877 C  CZ2 . TRP A 1 255 ? 103.801 19.395  18.956  1.00 53.62  ? 254 TRP A CZ2 1 
ATOM   1878 C  CZ3 . TRP A 1 255 ? 103.712 17.834  20.796  1.00 50.50  ? 254 TRP A CZ3 1 
ATOM   1879 C  CH2 . TRP A 1 255 ? 103.108 18.783  19.966  1.00 54.58  ? 254 TRP A CH2 1 
ATOM   1880 N  N   . GLN A 1 256 ? 107.887 15.393  17.079  1.00 46.58  ? 255 GLN A N   1 
ATOM   1881 C  CA  . GLN A 1 256 ? 107.237 15.144  15.798  1.00 51.39  ? 255 GLN A CA  1 
ATOM   1882 C  C   . GLN A 1 256 ? 106.654 13.738  15.740  1.00 48.95  ? 255 GLN A C   1 
ATOM   1883 O  O   . GLN A 1 256 ? 105.549 13.536  15.221  1.00 47.26  ? 255 GLN A O   1 
ATOM   1884 C  CB  . GLN A 1 256 ? 108.232 15.362  14.664  1.00 54.29  ? 255 GLN A CB  1 
ATOM   1885 C  CG  . GLN A 1 256 ? 108.629 16.812  14.486  1.00 58.72  ? 255 GLN A CG  1 
ATOM   1886 C  CD  . GLN A 1 256 ? 108.706 17.212  13.031  1.00 64.09  ? 255 GLN A CD  1 
ATOM   1887 O  OE1 . GLN A 1 256 ? 109.796 17.381  12.477  1.00 57.94  ? 255 GLN A OE1 1 
ATOM   1888 N  NE2 . GLN A 1 256 ? 107.543 17.366  12.399  1.00 63.38  ? 255 GLN A NE2 1 
ATOM   1889 N  N   . GLY A 1 257 ? 107.380 12.755  16.274  1.00 49.83  ? 256 GLY A N   1 
ATOM   1890 C  CA  . GLY A 1 257 ? 106.835 11.411  16.353  1.00 50.24  ? 256 GLY A CA  1 
ATOM   1891 C  C   . GLY A 1 257 ? 105.576 11.344  17.197  1.00 49.94  ? 256 GLY A C   1 
ATOM   1892 O  O   . GLY A 1 257 ? 104.593 10.708  16.809  1.00 55.23  ? 256 GLY A O   1 
ATOM   1893 N  N   . VAL A 1 258 ? 105.587 12.002  18.361  1.00 51.21  ? 257 VAL A N   1 
ATOM   1894 C  CA  . VAL A 1 258 ? 104.395 12.033  19.207  1.00 47.15  ? 257 VAL A CA  1 
ATOM   1895 C  C   . VAL A 1 258 ? 103.241 12.683  18.460  1.00 46.77  ? 257 VAL A C   1 
ATOM   1896 O  O   . VAL A 1 258 ? 102.126 12.151  18.419  1.00 50.90  ? 257 VAL A O   1 
ATOM   1897 C  CB  . VAL A 1 258 ? 104.677 12.769  20.531  1.00 50.50  ? 257 VAL A CB  1 
ATOM   1898 C  CG1 . VAL A 1 258 ? 103.401 12.940  21.326  1.00 47.48  ? 257 VAL A CG1 1 
ATOM   1899 C  CG2 . VAL A 1 258 ? 105.655 12.030  21.368  1.00 63.73  ? 257 VAL A CG2 1 
ATOM   1900 N  N   . SER A 1 259 ? 103.493 13.846  17.854  1.00 45.55  ? 258 SER A N   1 
ATOM   1901 C  CA  . SER A 1 259 ? 102.416 14.580  17.197  1.00 51.82  ? 258 SER A CA  1 
ATOM   1902 C  C   . SER A 1 259 ? 101.828 13.785  16.038  1.00 51.31  ? 258 SER A C   1 
ATOM   1903 O  O   . SER A 1 259 ? 100.603 13.681  15.908  1.00 47.82  ? 258 SER A O   1 
ATOM   1904 C  CB  . SER A 1 259 ? 102.924 15.936  16.713  1.00 46.23  ? 258 SER A CB  1 
ATOM   1905 O  OG  . SER A 1 259 ? 103.847 16.481  17.632  1.00 54.48  ? 258 SER A OG  1 
ATOM   1906 N  N   . SER A 1 260 ? 102.683 13.204  15.192  1.00 52.71  ? 259 SER A N   1 
ATOM   1907 C  CA  . SER A 1 260 ? 102.182 12.499  14.017  1.00 49.62  ? 259 SER A CA  1 
ATOM   1908 C  C   . SER A 1 260 ? 101.384 11.259  14.411  1.00 49.27  ? 259 SER A C   1 
ATOM   1909 O  O   . SER A 1 260 ? 100.334 10.982  13.818  1.00 49.10  ? 259 SER A O   1 
ATOM   1910 C  CB  . SER A 1 260 ? 103.341 12.146  13.080  1.00 50.93  ? 259 SER A CB  1 
ATOM   1911 O  OG  . SER A 1 260 ? 103.757 10.801  13.234  1.00 59.64  ? 259 SER A OG  1 
ATOM   1912 N  N   . ILE A 1 261 ? 101.841 10.518  15.427  1.00 43.63  ? 260 ILE A N   1 
ATOM   1913 C  CA  . ILE A 1 261 ? 101.075 9.354   15.867  1.00 44.60  ? 260 ILE A CA  1 
ATOM   1914 C  C   . ILE A 1 261 ? 99.821  9.782   16.622  1.00 51.13  ? 260 ILE A C   1 
ATOM   1915 O  O   . ILE A 1 261 ? 98.796  9.088   16.579  1.00 48.98  ? 260 ILE A O   1 
ATOM   1916 C  CB  . ILE A 1 261 ? 101.944 8.400   16.710  1.00 53.60  ? 260 ILE A CB  1 
ATOM   1917 C  CG1 . ILE A 1 261 ? 101.236 7.058   16.871  1.00 49.39  ? 260 ILE A CG1 1 
ATOM   1918 C  CG2 . ILE A 1 261 ? 102.244 8.979   18.088  1.00 55.41  ? 260 ILE A CG2 1 
ATOM   1919 C  CD1 . ILE A 1 261 ? 102.156 5.886   16.785  1.00 56.93  ? 260 ILE A CD1 1 
ATOM   1920 N  N   . SER A 1 262 ? 99.866  10.927  17.309  1.00 47.94  ? 261 SER A N   1 
ATOM   1921 C  CA  . SER A 1 262 ? 98.674  11.418  17.992  1.00 49.16  ? 261 SER A CA  1 
ATOM   1922 C  C   . SER A 1 262 ? 97.631  11.911  16.992  1.00 47.48  ? 261 SER A C   1 
ATOM   1923 O  O   . SER A 1 262 ? 96.426  11.717  17.195  1.00 43.27  ? 261 SER A O   1 
ATOM   1924 C  CB  . SER A 1 262 ? 99.057  12.525  18.974  1.00 45.85  ? 261 SER A CB  1 
ATOM   1925 O  OG  . SER A 1 262 ? 97.935  13.310  19.329  1.00 48.96  ? 261 SER A OG  1 
ATOM   1926 N  N   . ASP A 1 263 ? 98.077  12.545  15.904  1.00 46.57  ? 262 ASP A N   1 
ATOM   1927 C  CA  . ASP A 1 263 ? 97.154  12.959  14.852  1.00 50.50  ? 262 ASP A CA  1 
ATOM   1928 C  C   . ASP A 1 263 ? 96.495  11.756  14.191  1.00 50.17  ? 262 ASP A C   1 
ATOM   1929 O  O   . ASP A 1 263 ? 95.288  11.776  13.921  1.00 39.92  ? 262 ASP A O   1 
ATOM   1930 C  CB  . ASP A 1 263 ? 97.889  13.801  13.811  1.00 50.92  ? 262 ASP A CB  1 
ATOM   1931 C  CG  . ASP A 1 263 ? 98.322  15.140  14.356  1.00 62.91  ? 262 ASP A CG  1 
ATOM   1932 O  OD1 . ASP A 1 263 ? 97.708  15.604  15.341  1.00 70.71  ? 262 ASP A OD1 1 
ATOM   1933 O  OD2 . ASP A 1 263 ? 99.277  15.729  13.805  1.00 71.43  ? 262 ASP A OD2 1 
ATOM   1934 N  N   . ALA A 1 264 ? 97.274  10.706  13.910  1.00 44.74  ? 263 ALA A N   1 
ATOM   1935 C  CA  . ALA A 1 264 ? 96.693  9.485   13.362  1.00 46.18  ? 263 ALA A CA  1 
ATOM   1936 C  C   . ALA A 1 264 ? 95.714  8.855   14.346  1.00 45.41  ? 263 ALA A C   1 
ATOM   1937 O  O   . ALA A 1 264 ? 94.680  8.308   13.944  1.00 42.38  ? 263 ALA A O   1 
ATOM   1938 C  CB  . ALA A 1 264 ? 97.798  8.496   12.990  1.00 40.68  ? 263 ALA A CB  1 
ATOM   1939 N  N   . TYR A 1 265 ? 96.025  8.920   15.641  1.00 42.00  ? 264 TYR A N   1 
ATOM   1940 C  CA  . TYR A 1 265 ? 95.096  8.432   16.655  1.00 43.68  ? 264 TYR A CA  1 
ATOM   1941 C  C   . TYR A 1 265 ? 93.798  9.231   16.641  1.00 41.30  ? 264 TYR A C   1 
ATOM   1942 O  O   . TYR A 1 265 ? 92.708  8.661   16.755  1.00 39.04  ? 264 TYR A O   1 
ATOM   1943 C  CB  . TYR A 1 265 ? 95.763  8.503   18.027  1.00 43.32  ? 264 TYR A CB  1 
ATOM   1944 C  CG  . TYR A 1 265 ? 94.912  8.103   19.211  1.00 48.85  ? 264 TYR A CG  1 
ATOM   1945 C  CD1 . TYR A 1 265 ? 94.405  6.813   19.334  1.00 48.21  ? 264 TYR A CD1 1 
ATOM   1946 C  CD2 . TYR A 1 265 ? 94.651  9.010   20.232  1.00 46.39  ? 264 TYR A CD2 1 
ATOM   1947 C  CE1 . TYR A 1 265 ? 93.644  6.446   20.439  1.00 44.82  ? 264 TYR A CE1 1 
ATOM   1948 C  CE2 . TYR A 1 265 ? 93.897  8.653   21.334  1.00 42.39  ? 264 TYR A CE2 1 
ATOM   1949 C  CZ  . TYR A 1 265 ? 93.396  7.374   21.433  1.00 41.51  ? 264 TYR A CZ  1 
ATOM   1950 O  OH  . TYR A 1 265 ? 92.645  7.035   22.535  1.00 41.82  ? 264 TYR A OH  1 
ATOM   1951 N  N   . LEU A 1 266 ? 93.902  10.556  16.500  1.00 42.13  ? 265 LEU A N   1 
ATOM   1952 C  CA  . LEU A 1 266 ? 92.718  11.410  16.450  1.00 39.33  ? 265 LEU A CA  1 
ATOM   1953 C  C   . LEU A 1 266 ? 91.872  11.116  15.219  1.00 41.66  ? 265 LEU A C   1 
ATOM   1954 O  O   . LEU A 1 266 ? 90.639  11.057  15.303  1.00 44.76  ? 265 LEU A O   1 
ATOM   1955 C  CB  . LEU A 1 266 ? 93.140  12.879  16.452  1.00 41.98  ? 265 LEU A CB  1 
ATOM   1956 C  CG  . LEU A 1 266 ? 93.353  13.562  17.797  1.00 45.35  ? 265 LEU A CG  1 
ATOM   1957 C  CD1 . LEU A 1 266 ? 93.662  15.029  17.580  1.00 54.47  ? 265 LEU A CD1 1 
ATOM   1958 C  CD2 . LEU A 1 266 ? 92.131  13.397  18.676  1.00 44.55  ? 265 LEU A CD2 1 
ATOM   1959 N  N   . GLN A 1 267 ? 92.518  10.948  14.062  1.00 41.28  ? 266 GLN A N   1 
ATOM   1960 C  CA  . GLN A 1 267 ? 91.789  10.658  12.832  1.00 43.40  ? 266 GLN A CA  1 
ATOM   1961 C  C   . GLN A 1 267 ? 91.049  9.333   12.930  1.00 42.19  ? 266 GLN A C   1 
ATOM   1962 O  O   . GLN A 1 267 ? 89.935  9.196   12.413  1.00 46.87  ? 266 GLN A O   1 
ATOM   1963 C  CB  . GLN A 1 267 ? 92.748  10.642  11.643  1.00 46.67  ? 266 GLN A CB  1 
ATOM   1964 C  CG  . GLN A 1 267 ? 93.155  12.019  11.161  1.00 54.69  ? 266 GLN A CG  1 
ATOM   1965 C  CD  . GLN A 1 267 ? 93.040  12.159  9.659   1.00 75.55  ? 266 GLN A CD  1 
ATOM   1966 O  OE1 . GLN A 1 267 ? 92.480  13.135  9.155   1.00 76.47  ? 266 GLN A OE1 1 
ATOM   1967 N  NE2 . GLN A 1 267 ? 93.561  11.174  8.931   1.00 79.88  ? 266 GLN A NE2 1 
ATOM   1968 N  N   . PHE A 1 268 ? 91.656  8.342   13.582  1.00 43.56  ? 267 PHE A N   1 
ATOM   1969 C  CA  . PHE A 1 268 ? 90.983  7.061   13.761  1.00 44.44  ? 267 PHE A CA  1 
ATOM   1970 C  C   . PHE A 1 268 ? 89.792  7.203   14.700  1.00 40.04  ? 267 PHE A C   1 
ATOM   1971 O  O   . PHE A 1 268 ? 88.722  6.641   14.444  1.00 46.14  ? 267 PHE A O   1 
ATOM   1972 C  CB  . PHE A 1 268 ? 91.984  6.019   14.274  1.00 42.58  ? 267 PHE A CB  1 
ATOM   1973 C  CG  . PHE A 1 268 ? 91.365  4.904   15.080  1.00 43.58  ? 267 PHE A CG  1 
ATOM   1974 C  CD1 . PHE A 1 268 ? 90.614  3.915   14.473  1.00 43.95  ? 267 PHE A CD1 1 
ATOM   1975 C  CD2 . PHE A 1 268 ? 91.557  4.839   16.448  1.00 53.63  ? 267 PHE A CD2 1 
ATOM   1976 C  CE1 . PHE A 1 268 ? 90.053  2.887   15.214  1.00 39.32  ? 267 PHE A CE1 1 
ATOM   1977 C  CE2 . PHE A 1 268 ? 90.998  3.814   17.197  1.00 54.72  ? 267 PHE A CE2 1 
ATOM   1978 C  CZ  . PHE A 1 268 ? 90.244  2.840   16.575  1.00 45.03  ? 267 PHE A CZ  1 
ATOM   1979 N  N   . ILE A 1 269 ? 89.944  7.994   15.763  1.00 42.88  ? 268 ILE A N   1 
ATOM   1980 C  CA  . ILE A 1 269 ? 88.941  8.060   16.822  1.00 36.19  ? 268 ILE A CA  1 
ATOM   1981 C  C   . ILE A 1 269 ? 87.723  8.867   16.391  1.00 44.25  ? 268 ILE A C   1 
ATOM   1982 O  O   . ILE A 1 269 ? 86.591  8.549   16.772  1.00 43.70  ? 268 ILE A O   1 
ATOM   1983 C  CB  . ILE A 1 269 ? 89.578  8.634   18.101  1.00 43.30  ? 268 ILE A CB  1 
ATOM   1984 C  CG1 . ILE A 1 269 ? 90.501  7.594   18.737  1.00 42.33  ? 268 ILE A CG1 1 
ATOM   1985 C  CG2 . ILE A 1 269 ? 88.516  9.108   19.071  1.00 45.40  ? 268 ILE A CG2 1 
ATOM   1986 C  CD1 . ILE A 1 269 ? 89.825  6.743   19.774  1.00 44.31  ? 268 ILE A CD1 1 
ATOM   1987 N  N   . THR A 1 270 ? 87.924  9.925   15.609  1.00 37.64  ? 269 THR A N   1 
ATOM   1988 C  CA  . THR A 1 270 ? 86.835  10.803  15.205  1.00 42.16  ? 269 THR A CA  1 
ATOM   1989 C  C   . THR A 1 270 ? 86.380  10.553  13.772  1.00 38.90  ? 269 THR A C   1 
ATOM   1990 O  O   . THR A 1 270 ? 85.651  11.377  13.210  1.00 38.10  ? 269 THR A O   1 
ATOM   1991 C  CB  . THR A 1 270 ? 87.245  12.267  15.371  1.00 36.64  ? 269 THR A CB  1 
ATOM   1992 O  OG1 . THR A 1 270 ? 88.243  12.596  14.396  1.00 40.07  ? 269 THR A OG1 1 
ATOM   1993 C  CG2 . THR A 1 270 ? 87.798  12.504  16.765  1.00 39.66  ? 269 THR A CG2 1 
ATOM   1994 N  N   . ALA A 1 271 ? 86.785  9.430   13.175  1.00 38.91  ? 270 ALA A N   1 
ATOM   1995 C  CA  . ALA A 1 271 ? 86.449  9.172   11.779  1.00 35.77  ? 270 ALA A CA  1 
ATOM   1996 C  C   . ALA A 1 271 ? 84.943  9.053   11.566  1.00 36.45  ? 270 ALA A C   1 
ATOM   1997 O  O   . ALA A 1 271 ? 84.444  9.393   10.487  1.00 35.41  ? 270 ALA A O   1 
ATOM   1998 C  CB  . ALA A 1 271 ? 87.165  7.913   11.296  1.00 35.38  ? 270 ALA A CB  1 
ATOM   1999 N  N   . SER A 1 272 ? 84.202  8.595   12.574  1.00 34.64  ? 271 SER A N   1 
ATOM   2000 C  CA  . SER A 1 272 ? 82.750  8.505   12.467  1.00 35.42  ? 271 SER A CA  1 
ATOM   2001 C  C   . SER A 1 272 ? 82.048  9.843   12.663  1.00 30.21  ? 271 SER A C   1 
ATOM   2002 O  O   . SER A 1 272 ? 80.826  9.908   12.497  1.00 29.68  ? 271 SER A O   1 
ATOM   2003 C  CB  . SER A 1 272 ? 82.209  7.502   13.483  1.00 32.02  ? 271 SER A CB  1 
ATOM   2004 O  OG  . SER A 1 272 ? 82.150  8.090   14.766  1.00 35.73  ? 271 SER A OG  1 
ATOM   2005 N  N   . PHE A 1 273 ? 82.776  10.904  13.004  1.00 28.34  ? 272 PHE A N   1 
ATOM   2006 C  CA  . PHE A 1 273 ? 82.145  12.210  13.162  1.00 32.31  ? 272 PHE A CA  1 
ATOM   2007 C  C   . PHE A 1 273 ? 81.567  12.699  11.840  1.00 31.91  ? 272 PHE A C   1 
ATOM   2008 O  O   . PHE A 1 273 ? 80.416  13.145  11.779  1.00 33.99  ? 272 PHE A O   1 
ATOM   2009 C  CB  . PHE A 1 273 ? 83.151  13.222  13.712  1.00 31.41  ? 272 PHE A CB  1 
ATOM   2010 C  CG  . PHE A 1 273 ? 83.376  13.114  15.193  1.00 35.67  ? 272 PHE A CG  1 
ATOM   2011 C  CD1 . PHE A 1 273 ? 83.328  11.884  15.831  1.00 35.09  ? 272 PHE A CD1 1 
ATOM   2012 C  CD2 . PHE A 1 273 ? 83.650  14.244  15.948  1.00 36.61  ? 272 PHE A CD2 1 
ATOM   2013 C  CE1 . PHE A 1 273 ? 83.546  11.782  17.194  1.00 39.64  ? 272 PHE A CE1 1 
ATOM   2014 C  CE2 . PHE A 1 273 ? 83.866  14.147  17.317  1.00 38.17  ? 272 PHE A CE2 1 
ATOM   2015 C  CZ  . PHE A 1 273 ? 83.817  12.912  17.937  1.00 28.93  ? 272 PHE A CZ  1 
ATOM   2016 N  N   . SER A 1 274 ? 82.349  12.619  10.766  1.00 30.31  ? 273 SER A N   1 
ATOM   2017 C  CA  . SER A 1 274 ? 81.851  13.037  9.462   1.00 34.61  ? 273 SER A CA  1 
ATOM   2018 C  C   . SER A 1 274 ? 80.833  12.058  8.898   1.00 34.54  ? 273 SER A C   1 
ATOM   2019 O  O   . SER A 1 274 ? 80.065  12.429  8.005   1.00 35.70  ? 273 SER A O   1 
ATOM   2020 C  CB  . SER A 1 274 ? 83.009  13.192  8.477   1.00 33.26  ? 273 SER A CB  1 
ATOM   2021 O  OG  . SER A 1 274 ? 83.499  11.924  8.084   1.00 26.87  ? 273 SER A OG  1 
ATOM   2022 N  N   . VAL A 1 275 ? 80.822  10.820  9.395   1.00 32.60  ? 274 VAL A N   1 
ATOM   2023 C  CA  . VAL A 1 275 ? 79.898  9.809   8.895   1.00 29.29  ? 274 VAL A CA  1 
ATOM   2024 C  C   . VAL A 1 275 ? 78.522  9.973   9.529   1.00 31.00  ? 274 VAL A C   1 
ATOM   2025 O  O   . VAL A 1 275 ? 77.493  9.807   8.862   1.00 28.88  ? 274 VAL A O   1 
ATOM   2026 C  CB  . VAL A 1 275 ? 80.475  8.406   9.153   1.00 28.76  ? 274 VAL A CB  1 
ATOM   2027 C  CG1 . VAL A 1 275 ? 79.404  7.356   8.987   1.00 33.87  ? 274 VAL A CG1 1 
ATOM   2028 C  CG2 . VAL A 1 275 ? 81.652  8.124   8.228   1.00 32.51  ? 274 VAL A CG2 1 
ATOM   2029 N  N   . TYR A 1 276 ? 78.478  10.284  10.823  1.00 29.19  ? 275 TYR A N   1 
ATOM   2030 C  CA  . TYR A 1 276 ? 77.220  10.441  11.540  1.00 33.55  ? 275 TYR A CA  1 
ATOM   2031 C  C   . TYR A 1 276 ? 76.993  11.859  12.042  1.00 32.08  ? 275 TYR A C   1 
ATOM   2032 O  O   . TYR A 1 276 ? 75.930  12.437  11.792  1.00 33.46  ? 275 TYR A O   1 
ATOM   2033 C  CB  . TYR A 1 276 ? 77.151  9.468   12.730  1.00 30.64  ? 275 TYR A CB  1 
ATOM   2034 C  CG  . TYR A 1 276 ? 75.960  9.745   13.613  1.00 32.12  ? 275 TYR A CG  1 
ATOM   2035 C  CD1 . TYR A 1 276 ? 74.713  9.228   13.302  1.00 36.96  ? 275 TYR A CD1 1 
ATOM   2036 C  CD2 . TYR A 1 276 ? 76.072  10.555  14.737  1.00 35.36  ? 275 TYR A CD2 1 
ATOM   2037 C  CE1 . TYR A 1 276 ? 73.611  9.494   14.092  1.00 42.25  ? 275 TYR A CE1 1 
ATOM   2038 C  CE2 . TYR A 1 276 ? 74.975  10.831  15.530  1.00 38.00  ? 275 TYR A CE2 1 
ATOM   2039 C  CZ  . TYR A 1 276 ? 73.748  10.296  15.202  1.00 39.19  ? 275 TYR A CZ  1 
ATOM   2040 O  OH  . TYR A 1 276 ? 72.650  10.559  15.983  1.00 43.41  ? 275 TYR A OH  1 
ATOM   2041 N  N   . LEU A 1 277 ? 77.954  12.432  12.767  1.00 29.13  ? 276 LEU A N   1 
ATOM   2042 C  CA  . LEU A 1 277 ? 77.700  13.682  13.478  1.00 32.73  ? 276 LEU A CA  1 
ATOM   2043 C  C   . LEU A 1 277 ? 77.438  14.832  12.512  1.00 31.88  ? 276 LEU A C   1 
ATOM   2044 O  O   . LEU A 1 277 ? 76.503  15.617  12.709  1.00 32.89  ? 276 LEU A O   1 
ATOM   2045 C  CB  . LEU A 1 277 ? 78.875  14.008  14.399  1.00 31.36  ? 276 LEU A CB  1 
ATOM   2046 C  CG  . LEU A 1 277 ? 78.625  15.071  15.458  1.00 32.13  ? 276 LEU A CG  1 
ATOM   2047 C  CD1 . LEU A 1 277 ? 77.350  14.758  16.233  1.00 34.77  ? 276 LEU A CD1 1 
ATOM   2048 C  CD2 . LEU A 1 277 ? 79.826  15.167  16.384  1.00 35.14  ? 276 LEU A CD2 1 
ATOM   2049 N  N   . LEU A 1 278 ? 78.256  14.951  11.464  1.00 29.72  ? 277 LEU A N   1 
ATOM   2050 C  CA  . LEU A 1 278 ? 78.086  16.051  10.514  1.00 34.92  ? 277 LEU A CA  1 
ATOM   2051 C  C   . LEU A 1 278 ? 76.743  16.000  9.794   1.00 32.36  ? 277 LEU A C   1 
ATOM   2052 O  O   . LEU A 1 278 ? 76.036  17.020  9.793   1.00 30.62  ? 277 LEU A O   1 
ATOM   2053 C  CB  . LEU A 1 278 ? 79.263  16.075  9.527   1.00 30.79  ? 277 LEU A CB  1 
ATOM   2054 C  CG  . LEU A 1 278 ? 79.120  16.889  8.234   1.00 32.68  ? 277 LEU A CG  1 
ATOM   2055 C  CD1 . LEU A 1 278 ? 78.849  18.344  8.533   1.00 33.05  ? 277 LEU A CD1 1 
ATOM   2056 C  CD2 . LEU A 1 278 ? 80.364  16.762  7.361   1.00 27.90  ? 277 LEU A CD2 1 
ATOM   2057 N  N   . PRO A 1 279 ? 76.324  14.886  9.177   1.00 33.46  ? 278 PRO A N   1 
ATOM   2058 C  CA  . PRO A 1 279 ? 75.003  14.899  8.525   1.00 33.21  ? 278 PRO A CA  1 
ATOM   2059 C  C   . PRO A 1 279 ? 73.849  15.081  9.499   1.00 33.79  ? 278 PRO A C   1 
ATOM   2060 O  O   . PRO A 1 279 ? 72.866  15.754  9.164   1.00 36.68  ? 278 PRO A O   1 
ATOM   2061 C  CB  . PRO A 1 279 ? 74.945  13.537  7.816   1.00 31.01  ? 278 PRO A CB  1 
ATOM   2062 C  CG  . PRO A 1 279 ? 75.925  12.692  8.526   1.00 29.09  ? 278 PRO A CG  1 
ATOM   2063 C  CD  . PRO A 1 279 ? 77.017  13.600  8.974   1.00 28.24  ? 278 PRO A CD  1 
ATOM   2064 N  N   . THR A 1 280 ? 73.935  14.494  10.697  1.00 34.05  ? 279 THR A N   1 
ATOM   2065 C  CA  . THR A 1 280 ? 72.853  14.631  11.669  1.00 35.41  ? 279 THR A CA  1 
ATOM   2066 C  C   . THR A 1 280 ? 72.661  16.088  12.072  1.00 32.54  ? 279 THR A C   1 
ATOM   2067 O  O   . THR A 1 280 ? 71.549  16.620  12.014  1.00 37.31  ? 279 THR A O   1 
ATOM   2068 C  CB  . THR A 1 280 ? 73.134  13.768  12.904  1.00 35.05  ? 279 THR A CB  1 
ATOM   2069 O  OG1 . THR A 1 280 ? 73.091  12.378  12.552  1.00 31.05  ? 279 THR A OG1 1 
ATOM   2070 C  CG2 . THR A 1 280 ? 72.108  14.043  13.997  1.00 34.37  ? 279 THR A CG2 1 
ATOM   2071 N  N   . LEU A 1 281 ? 73.739  16.752  12.487  1.00 32.45  ? 280 LEU A N   1 
ATOM   2072 C  CA  . LEU A 1 281 ? 73.653  18.158  12.872  1.00 33.15  ? 280 LEU A CA  1 
ATOM   2073 C  C   . LEU A 1 281 ? 73.282  19.047  11.696  1.00 35.86  ? 280 LEU A C   1 
ATOM   2074 O  O   . LEU A 1 281 ? 72.743  20.140  11.899  1.00 29.84  ? 280 LEU A O   1 
ATOM   2075 C  CB  . LEU A 1 281 ? 74.981  18.628  13.468  1.00 30.97  ? 280 LEU A CB  1 
ATOM   2076 C  CG  . LEU A 1 281 ? 75.418  18.038  14.809  1.00 34.67  ? 280 LEU A CG  1 
ATOM   2077 C  CD1 . LEU A 1 281 ? 76.863  18.437  15.124  1.00 28.49  ? 280 LEU A CD1 1 
ATOM   2078 C  CD2 . LEU A 1 281 ? 74.486  18.475  15.917  1.00 35.56  ? 280 LEU A CD2 1 
ATOM   2079 N  N   . SER A 1 282 ? 73.565  18.606  10.471  1.00 33.92  ? 281 SER A N   1 
ATOM   2080 C  CA  . SER A 1 282 ? 73.171  19.389  9.309   1.00 35.03  ? 281 SER A CA  1 
ATOM   2081 C  C   . SER A 1 282 ? 71.655  19.462  9.195   1.00 33.24  ? 281 SER A C   1 
ATOM   2082 O  O   . SER A 1 282 ? 71.103  20.509  8.843   1.00 36.47  ? 281 SER A O   1 
ATOM   2083 C  CB  . SER A 1 282 ? 73.787  18.794  8.043   1.00 32.46  ? 281 SER A CB  1 
ATOM   2084 O  OG  . SER A 1 282 ? 73.372  19.501  6.885   1.00 31.65  ? 281 SER A OG  1 
ATOM   2085 N  N   . ARG A 1 283 ? 70.965  18.368  9.517   1.00 33.61  ? 282 ARG A N   1 
ATOM   2086 C  CA  . ARG A 1 283 ? 69.516  18.333  9.363   1.00 37.21  ? 282 ARG A CA  1 
ATOM   2087 C  C   . ARG A 1 283 ? 68.805  19.118  10.455  1.00 36.69  ? 282 ARG A C   1 
ATOM   2088 O  O   . ARG A 1 283 ? 67.694  19.604  10.231  1.00 47.58  ? 282 ARG A O   1 
ATOM   2089 C  CB  . ARG A 1 283 ? 69.020  16.886  9.358   1.00 44.08  ? 282 ARG A CB  1 
ATOM   2090 C  CG  . ARG A 1 283 ? 69.445  16.094  8.136   1.00 46.51  ? 282 ARG A CG  1 
ATOM   2091 C  CD  . ARG A 1 283 ? 68.822  14.710  8.117   1.00 57.39  ? 282 ARG A CD  1 
ATOM   2092 N  NE  . ARG A 1 283 ? 69.558  13.811  7.237   1.00 71.71  ? 282 ARG A NE  1 
ATOM   2093 C  CZ  . ARG A 1 283 ? 69.484  12.488  7.276   1.00 73.67  ? 282 ARG A CZ  1 
ATOM   2094 N  NH1 . ARG A 1 283 ? 68.694  11.863  8.136   1.00 69.76  ? 282 ARG A NH1 1 
ATOM   2095 N  NH2 . ARG A 1 283 ? 70.217  11.772  6.425   1.00 58.38  ? 282 ARG A NH2 1 
ATOM   2096 N  N   . LEU A 1 284 ? 69.421  19.251  11.627  1.00 42.11  ? 283 LEU A N   1 
ATOM   2097 C  CA  . LEU A 1 284 ? 68.795  19.897  12.774  1.00 43.39  ? 283 LEU A CA  1 
ATOM   2098 C  C   . LEU A 1 284 ? 69.048  21.401  12.754  1.00 47.89  ? 283 LEU A C   1 
ATOM   2099 O  O   . LEU A 1 284 ? 70.163  21.856  12.485  1.00 49.71  ? 283 LEU A O   1 
ATOM   2100 C  CB  . LEU A 1 284 ? 69.322  19.303  14.081  1.00 34.54  ? 283 LEU A CB  1 
ATOM   2101 C  CG  . LEU A 1 284 ? 69.242  17.782  14.228  1.00 34.93  ? 283 LEU A CG  1 
ATOM   2102 C  CD1 . LEU A 1 284 ? 70.083  17.307  15.407  1.00 33.94  ? 283 LEU A CD1 1 
ATOM   2103 C  CD2 . LEU A 1 284 ? 67.801  17.321  14.370  1.00 33.51  ? 283 LEU A CD2 1 
ATOM   2104 N  N   . THR A 1 285 ? 68.003  22.172  13.042  1.00 47.74  ? 284 THR A N   1 
ATOM   2105 C  CA  . THR A 1 285 ? 68.112  23.624  12.992  1.00 50.40  ? 284 THR A CA  1 
ATOM   2106 C  C   . THR A 1 285 ? 67.657  24.258  14.299  1.00 50.51  ? 284 THR A C   1 
ATOM   2107 O  O   . THR A 1 285 ? 68.127  25.340  14.666  1.00 50.39  ? 284 THR A O   1 
ATOM   2108 C  CB  . THR A 1 285 ? 67.295  24.182  11.824  1.00 57.68  ? 284 THR A CB  1 
ATOM   2109 O  OG1 . THR A 1 285 ? 65.897  24.024  12.101  1.00 56.03  ? 284 THR A OG1 1 
ATOM   2110 C  CG2 . THR A 1 285 ? 67.642  23.461  10.523  1.00 59.06  ? 284 THR A CG2 1 
ATOM   2111 N  N   . GLU A 1 286 ? 66.735  23.600  14.996  1.00 47.38  ? 285 GLU A N   1 
ATOM   2112 C  CA  . GLU A 1 286 ? 66.244  24.120  16.264  1.00 46.37  ? 285 GLU A CA  1 
ATOM   2113 C  C   . GLU A 1 286 ? 67.309  23.974  17.342  1.00 42.90  ? 285 GLU A C   1 
ATOM   2114 O  O   . GLU A 1 286 ? 68.026  22.973  17.399  1.00 42.84  ? 285 GLU A O   1 
ATOM   2115 C  CB  . GLU A 1 286 ? 64.967  23.395  16.683  1.00 48.32  ? 285 GLU A CB  1 
ATOM   2116 C  CG  . GLU A 1 286 ? 63.764  23.689  15.798  1.00 51.12  ? 285 GLU A CG  1 
ATOM   2117 C  CD  . GLU A 1 286 ? 63.250  25.110  15.959  1.00 57.31  ? 285 GLU A CD  1 
ATOM   2118 O  OE1 . GLU A 1 286 ? 62.535  25.379  16.949  1.00 64.13  ? 285 GLU A OE1 1 
ATOM   2119 O  OE2 . GLU A 1 286 ? 63.560  25.958  15.093  1.00 58.04  ? 285 GLU A OE2 1 
ATOM   2120 N  N   . LYS A 1 287 ? 67.409  24.986  18.202  1.00 40.24  ? 286 LYS A N   1 
ATOM   2121 C  CA  . LYS A 1 287 ? 68.466  24.986  19.205  1.00 44.78  ? 286 LYS A CA  1 
ATOM   2122 C  C   . LYS A 1 287 ? 68.281  23.871  20.229  1.00 42.60  ? 286 LYS A C   1 
ATOM   2123 O  O   . LYS A 1 287 ? 69.269  23.301  20.702  1.00 39.36  ? 286 LYS A O   1 
ATOM   2124 C  CB  . LYS A 1 287 ? 68.534  26.352  19.885  1.00 45.71  ? 286 LYS A CB  1 
ATOM   2125 C  CG  . LYS A 1 287 ? 69.240  27.404  19.040  1.00 49.32  ? 286 LYS A CG  1 
ATOM   2126 C  CD  . LYS A 1 287 ? 69.262  28.755  19.733  1.00 57.28  ? 286 LYS A CD  1 
ATOM   2127 C  CE  . LYS A 1 287 ? 70.005  29.792  18.902  1.00 54.74  ? 286 LYS A CE  1 
ATOM   2128 N  NZ  . LYS A 1 287 ? 70.580  29.197  17.670  1.00 58.08  ? 286 LYS A NZ  1 
ATOM   2129 N  N   . ARG A 1 288 ? 67.036  23.533  20.569  1.00 43.94  ? 287 ARG A N   1 
ATOM   2130 C  CA  . ARG A 1 288 ? 66.812  22.421  21.488  1.00 47.52  ? 287 ARG A CA  1 
ATOM   2131 C  C   . ARG A 1 288 ? 67.290  21.104  20.883  1.00 46.53  ? 287 ARG A C   1 
ATOM   2132 O  O   . ARG A 1 288 ? 67.943  20.303  21.562  1.00 41.83  ? 287 ARG A O   1 
ATOM   2133 C  CB  . ARG A 1 288 ? 65.332  22.337  21.863  1.00 48.16  ? 287 ARG A CB  1 
ATOM   2134 C  CG  . ARG A 1 288 ? 64.910  23.273  22.986  1.00 59.08  ? 287 ARG A CG  1 
ATOM   2135 C  CD  . ARG A 1 288 ? 64.454  24.635  22.448  1.00 70.10  ? 287 ARG A CD  1 
ATOM   2136 N  NE  . ARG A 1 288 ? 64.655  25.705  23.419  1.00 67.67  ? 287 ARG A NE  1 
ATOM   2137 C  CZ  . ARG A 1 288 ? 64.338  26.977  23.220  1.00 61.17  ? 287 ARG A CZ  1 
ATOM   2138 N  NH1 . ARG A 1 288 ? 63.799  27.386  22.085  1.00 65.04  ? 287 ARG A NH1 1 
ATOM   2139 N  NH2 . ARG A 1 288 ? 64.563  27.860  24.188  1.00 66.97  ? 287 ARG A NH2 1 
ATOM   2140 N  N   . ASP A 1 289 ? 66.991  20.871  19.600  1.00 45.47  ? 288 ASP A N   1 
ATOM   2141 C  CA  . ASP A 1 289 ? 67.401  19.625  18.956  1.00 37.47  ? 288 ASP A CA  1 
ATOM   2142 C  C   . ASP A 1 289 ? 68.913  19.546  18.808  1.00 36.62  ? 288 ASP A C   1 
ATOM   2143 O  O   . ASP A 1 289 ? 69.504  18.475  18.978  1.00 40.88  ? 288 ASP A O   1 
ATOM   2144 C  CB  . ASP A 1 289 ? 66.730  19.491  17.591  1.00 36.79  ? 288 ASP A CB  1 
ATOM   2145 C  CG  . ASP A 1 289 ? 65.217  19.465  17.684  1.00 49.01  ? 288 ASP A CG  1 
ATOM   2146 O  OD1 . ASP A 1 289 ? 64.694  19.152  18.777  1.00 54.72  ? 288 ASP A OD1 1 
ATOM   2147 O  OD2 . ASP A 1 289 ? 64.552  19.767  16.664  1.00 48.77  ? 288 ASP A OD2 1 
ATOM   2148 N  N   . ILE A 1 290 ? 69.554  20.664  18.474  1.00 35.79  ? 289 ILE A N   1 
ATOM   2149 C  CA  . ILE A 1 290 ? 71.004  20.665  18.331  1.00 39.41  ? 289 ILE A CA  1 
ATOM   2150 C  C   . ILE A 1 290 ? 71.667  20.392  19.675  1.00 37.25  ? 289 ILE A C   1 
ATOM   2151 O  O   . ILE A 1 290 ? 72.588  19.574  19.774  1.00 40.68  ? 289 ILE A O   1 
ATOM   2152 C  CB  . ILE A 1 290 ? 71.474  21.995  17.714  1.00 40.03  ? 289 ILE A CB  1 
ATOM   2153 C  CG1 . ILE A 1 290 ? 70.960  22.121  16.277  1.00 37.25  ? 289 ILE A CG1 1 
ATOM   2154 C  CG2 . ILE A 1 290 ? 72.987  22.107  17.761  1.00 32.17  ? 289 ILE A CG2 1 
ATOM   2155 C  CD1 . ILE A 1 290 ? 71.189  23.476  15.659  1.00 37.91  ? 289 ILE A CD1 1 
ATOM   2156 N  N   . THR A 1 291 ? 71.197  21.061  20.731  1.00 39.77  ? 290 THR A N   1 
ATOM   2157 C  CA  . THR A 1 291 ? 71.749  20.846  22.064  1.00 36.62  ? 290 THR A CA  1 
ATOM   2158 C  C   . THR A 1 291 ? 71.621  19.387  22.483  1.00 40.26  ? 290 THR A C   1 
ATOM   2159 O  O   . THR A 1 291 ? 72.589  18.784  22.963  1.00 40.93  ? 290 THR A O   1 
ATOM   2160 C  CB  . THR A 1 291 ? 71.043  21.761  23.066  1.00 43.57  ? 290 THR A CB  1 
ATOM   2161 O  OG1 . THR A 1 291 ? 71.250  23.126  22.687  1.00 41.38  ? 290 THR A OG1 1 
ATOM   2162 C  CG2 . THR A 1 291 ? 71.586  21.550  24.478  1.00 38.87  ? 290 THR A CG2 1 
ATOM   2163 N  N   . ARG A 1 292 ? 70.436  18.801  22.291  1.00 37.64  ? 291 ARG A N   1 
ATOM   2164 C  CA  . ARG A 1 292 ? 70.221  17.401  22.643  1.00 38.58  ? 291 ARG A CA  1 
ATOM   2165 C  C   . ARG A 1 292 ? 71.220  16.491  21.940  1.00 39.35  ? 291 ARG A C   1 
ATOM   2166 O  O   . ARG A 1 292 ? 71.773  15.572  22.555  1.00 42.52  ? 291 ARG A O   1 
ATOM   2167 C  CB  . ARG A 1 292 ? 68.786  16.995  22.299  1.00 47.87  ? 291 ARG A CB  1 
ATOM   2168 C  CG  . ARG A 1 292 ? 68.205  15.905  23.190  1.00 60.60  ? 291 ARG A CG  1 
ATOM   2169 C  CD  . ARG A 1 292 ? 66.817  15.464  22.721  1.00 63.55  ? 291 ARG A CD  1 
ATOM   2170 N  NE  . ARG A 1 292 ? 65.843  16.552  22.750  1.00 64.54  ? 291 ARG A NE  1 
ATOM   2171 C  CZ  . ARG A 1 292 ? 65.259  17.017  23.848  1.00 77.73  ? 291 ARG A CZ  1 
ATOM   2172 N  NH1 . ARG A 1 292 ? 65.518  16.506  25.043  1.00 73.68  ? 291 ARG A NH1 1 
ATOM   2173 N  NH2 . ARG A 1 292 ? 64.389  18.018  23.745  1.00 75.34  ? 291 ARG A NH2 1 
ATOM   2174 N  N   . GLU A 1 293 ? 71.475  16.734  20.652  1.00 38.50  ? 292 GLU A N   1 
ATOM   2175 C  CA  . GLU A 1 293 ? 72.389  15.868  19.912  1.00 40.36  ? 292 GLU A CA  1 
ATOM   2176 C  C   . GLU A 1 293 ? 73.834  16.089  20.350  1.00 39.81  ? 292 GLU A C   1 
ATOM   2177 O  O   . GLU A 1 293 ? 74.605  15.130  20.480  1.00 40.09  ? 292 GLU A O   1 
ATOM   2178 C  CB  . GLU A 1 293 ? 72.230  16.105  18.410  1.00 37.20  ? 292 GLU A CB  1 
ATOM   2179 C  CG  . GLU A 1 293 ? 73.009  15.132  17.529  1.00 40.01  ? 292 GLU A CG  1 
ATOM   2180 C  CD  . GLU A 1 293 ? 72.486  13.701  17.608  1.00 49.08  ? 292 GLU A CD  1 
ATOM   2181 O  OE1 . GLU A 1 293 ? 73.316  12.764  17.572  1.00 45.77  ? 292 GLU A OE1 1 
ATOM   2182 O  OE2 . GLU A 1 293 ? 71.251  13.512  17.708  1.00 47.09  ? 292 GLU A OE2 1 
ATOM   2183 N  N   . VAL A 1 294 ? 74.210  17.344  20.596  1.00 38.99  ? 293 VAL A N   1 
ATOM   2184 C  CA  . VAL A 1 294 ? 75.553  17.649  21.077  1.00 36.16  ? 293 VAL A CA  1 
ATOM   2185 C  C   . VAL A 1 294 ? 75.783  17.035  22.453  1.00 37.40  ? 293 VAL A C   1 
ATOM   2186 O  O   . VAL A 1 294 ? 76.815  16.398  22.698  1.00 38.55  ? 293 VAL A O   1 
ATOM   2187 C  CB  . VAL A 1 294 ? 75.770  19.173  21.087  1.00 35.58  ? 293 VAL A CB  1 
ATOM   2188 C  CG1 . VAL A 1 294 ? 77.003  19.538  21.899  1.00 36.70  ? 293 VAL A CG1 1 
ATOM   2189 C  CG2 . VAL A 1 294 ? 75.872  19.703  19.666  1.00 35.53  ? 293 VAL A CG2 1 
ATOM   2190 N  N   . VAL A 1 295 ? 74.828  17.207  23.370  1.00 36.42  ? 294 VAL A N   1 
ATOM   2191 C  CA  . VAL A 1 295 ? 74.966  16.619  24.701  1.00 38.79  ? 294 VAL A CA  1 
ATOM   2192 C  C   . VAL A 1 295 ? 75.073  15.101  24.603  1.00 40.91  ? 294 VAL A C   1 
ATOM   2193 O  O   . VAL A 1 295 ? 75.944  14.483  25.228  1.00 40.40  ? 294 VAL A O   1 
ATOM   2194 C  CB  . VAL A 1 295 ? 73.794  17.049  25.605  1.00 38.54  ? 294 VAL A CB  1 
ATOM   2195 C  CG1 . VAL A 1 295 ? 73.702  16.146  26.832  1.00 38.74  ? 294 VAL A CG1 1 
ATOM   2196 C  CG2 . VAL A 1 295 ? 73.944  18.509  26.026  1.00 32.88  ? 294 VAL A CG2 1 
ATOM   2197 N  N   . LYS A 1 296 ? 74.200  14.476  23.805  1.00 43.21  ? 295 LYS A N   1 
ATOM   2198 C  CA  . LYS A 1 296 ? 74.236  13.022  23.670  1.00 39.20  ? 295 LYS A CA  1 
ATOM   2199 C  C   . LYS A 1 296 ? 75.559  12.558  23.083  1.00 41.21  ? 295 LYS A C   1 
ATOM   2200 O  O   . LYS A 1 296 ? 76.113  11.539  23.511  1.00 43.48  ? 295 LYS A O   1 
ATOM   2201 C  CB  . LYS A 1 296 ? 73.073  12.538  22.803  1.00 38.23  ? 295 LYS A CB  1 
ATOM   2202 C  CG  . LYS A 1 296 ? 73.045  11.029  22.599  1.00 43.76  ? 295 LYS A CG  1 
ATOM   2203 C  CD  . LYS A 1 296 ? 71.728  10.563  21.995  1.00 44.22  ? 295 LYS A CD  1 
ATOM   2204 C  CE  . LYS A 1 296 ? 71.469  11.241  20.659  1.00 53.65  ? 295 LYS A CE  1 
ATOM   2205 N  NZ  . LYS A 1 296 ? 70.483  10.500  19.819  1.00 55.65  ? 295 LYS A NZ  1 
ATOM   2206 N  N   . SER A 1 297 ? 76.081  13.296  22.102  1.00 39.79  ? 296 SER A N   1 
ATOM   2207 C  CA  . SER A 1 297 ? 77.366  12.946  21.507  1.00 37.58  ? 296 SER A CA  1 
ATOM   2208 C  C   . SER A 1 297 ? 78.495  13.067  22.522  1.00 38.42  ? 296 SER A C   1 
ATOM   2209 O  O   . SER A 1 297 ? 79.327  12.161  22.649  1.00 39.45  ? 296 SER A O   1 
ATOM   2210 C  CB  . SER A 1 297 ? 77.635  13.832  20.293  1.00 37.51  ? 296 SER A CB  1 
ATOM   2211 O  OG  . SER A 1 297 ? 76.712  13.553  19.257  1.00 37.77  ? 296 SER A OG  1 
ATOM   2212 N  N   . LEU A 1 298 ? 78.543  14.185  23.251  1.00 39.28  ? 297 LEU A N   1 
ATOM   2213 C  CA  . LEU A 1 298 ? 79.596  14.372  24.244  1.00 39.22  ? 297 LEU A CA  1 
ATOM   2214 C  C   . LEU A 1 298 ? 79.507  13.320  25.343  1.00 41.34  ? 297 LEU A C   1 
ATOM   2215 O  O   . LEU A 1 298 ? 80.532  12.827  25.825  1.00 46.07  ? 297 LEU A O   1 
ATOM   2216 C  CB  . LEU A 1 298 ? 79.521  15.783  24.833  1.00 29.78  ? 297 LEU A CB  1 
ATOM   2217 C  CG  . LEU A 1 298 ? 80.057  16.904  23.939  1.00 36.53  ? 297 LEU A CG  1 
ATOM   2218 C  CD1 . LEU A 1 298 ? 79.659  18.265  24.479  1.00 38.84  ? 297 LEU A CD1 1 
ATOM   2219 C  CD2 . LEU A 1 298 ? 81.573  16.812  23.788  1.00 35.24  ? 297 LEU A CD2 1 
ATOM   2220 N  N   . LYS A 1 299 ? 78.290  12.950  25.742  1.00 40.65  ? 298 LYS A N   1 
ATOM   2221 C  CA  . LYS A 1 299 ? 78.126  11.933  26.775  1.00 40.90  ? 298 LYS A CA  1 
ATOM   2222 C  C   . LYS A 1 299 ? 78.627  10.568  26.326  1.00 46.46  ? 298 LYS A C   1 
ATOM   2223 O  O   . LYS A 1 299 ? 78.946  9.729   27.175  1.00 41.41  ? 298 LYS A O   1 
ATOM   2224 C  CB  . LYS A 1 299 ? 76.660  11.835  27.195  1.00 39.28  ? 298 LYS A CB  1 
ATOM   2225 C  CG  . LYS A 1 299 ? 76.267  12.814  28.285  1.00 40.38  ? 298 LYS A CG  1 
ATOM   2226 C  CD  . LYS A 1 299 ? 74.758  13.001  28.338  1.00 46.11  ? 298 LYS A CD  1 
ATOM   2227 C  CE  . LYS A 1 299 ? 74.291  13.357  29.736  1.00 58.20  ? 298 LYS A CE  1 
ATOM   2228 N  NZ  . LYS A 1 299 ? 73.453  12.288  30.355  1.00 75.66  ? 298 LYS A NZ  1 
ATOM   2229 N  N   . PHE A 1 300 ? 78.699  10.324  25.018  1.00 37.42  ? 299 PHE A N   1 
ATOM   2230 C  CA  . PHE A 1 300 ? 79.198  9.053   24.510  1.00 43.86  ? 299 PHE A CA  1 
ATOM   2231 C  C   . PHE A 1 300 ? 80.686  9.103   24.193  1.00 49.16  ? 299 PHE A C   1 
ATOM   2232 O  O   . PHE A 1 300 ? 81.425  8.169   24.530  1.00 49.34  ? 299 PHE A O   1 
ATOM   2233 C  CB  . PHE A 1 300 ? 78.434  8.640   23.250  1.00 41.91  ? 299 PHE A CB  1 
ATOM   2234 C  CG  . PHE A 1 300 ? 79.149  7.603   22.422  1.00 47.62  ? 299 PHE A CG  1 
ATOM   2235 C  CD1 . PHE A 1 300 ? 79.246  6.289   22.855  1.00 51.66  ? 299 PHE A CD1 1 
ATOM   2236 C  CD2 . PHE A 1 300 ? 79.738  7.947   21.216  1.00 43.49  ? 299 PHE A CD2 1 
ATOM   2237 C  CE1 . PHE A 1 300 ? 79.905  5.338   22.094  1.00 46.01  ? 299 PHE A CE1 1 
ATOM   2238 C  CE2 . PHE A 1 300 ? 80.399  7.000   20.452  1.00 41.79  ? 299 PHE A CE2 1 
ATOM   2239 C  CZ  . PHE A 1 300 ? 80.481  5.696   20.890  1.00 42.75  ? 299 PHE A CZ  1 
ATOM   2240 N  N   . VAL A 1 301 ? 81.141  10.182  23.557  1.00 41.97  ? 300 VAL A N   1 
ATOM   2241 C  CA  . VAL A 1 301 ? 82.493  10.190  23.020  1.00 42.95  ? 300 VAL A CA  1 
ATOM   2242 C  C   . VAL A 1 301 ? 83.534  10.486  24.103  1.00 46.62  ? 300 VAL A C   1 
ATOM   2243 O  O   . VAL A 1 301 ? 84.625  9.905   24.083  1.00 44.49  ? 300 VAL A O   1 
ATOM   2244 C  CB  . VAL A 1 301 ? 82.570  11.176  21.839  1.00 47.83  ? 300 VAL A CB  1 
ATOM   2245 C  CG1 . VAL A 1 301 ? 82.654  12.626  22.316  1.00 40.53  ? 300 VAL A CG1 1 
ATOM   2246 C  CG2 . VAL A 1 301 ? 83.721  10.817  20.923  1.00 52.30  ? 300 VAL A CG2 1 
ATOM   2247 N  N   . LEU A 1 302 ? 83.227  11.361  25.074  1.00 41.90  ? 301 LEU A N   1 
ATOM   2248 C  CA  . LEU A 1 302 ? 84.229  11.686  26.091  1.00 41.62  ? 301 LEU A CA  1 
ATOM   2249 C  C   . LEU A 1 302 ? 84.586  10.482  26.960  1.00 45.73  ? 301 LEU A C   1 
ATOM   2250 O  O   . LEU A 1 302 ? 85.788  10.223  27.150  1.00 43.03  ? 301 LEU A O   1 
ATOM   2251 C  CB  . LEU A 1 302 ? 83.759  12.878  26.931  1.00 40.60  ? 301 LEU A CB  1 
ATOM   2252 C  CG  . LEU A 1 302 ? 83.866  14.274  26.302  1.00 40.31  ? 301 LEU A CG  1 
ATOM   2253 C  CD1 . LEU A 1 302 ? 83.276  15.331  27.224  1.00 51.21  ? 301 LEU A CD1 1 
ATOM   2254 C  CD2 . LEU A 1 302 ? 85.305  14.619  25.968  1.00 44.20  ? 301 LEU A CD2 1 
ATOM   2255 N  N   . PRO A 1 303 ? 83.638  9.713   27.510  1.00 43.61  ? 302 PRO A N   1 
ATOM   2256 C  CA  . PRO A 1 303 ? 84.049  8.525   28.273  1.00 45.22  ? 302 PRO A CA  1 
ATOM   2257 C  C   . PRO A 1 303 ? 84.688  7.458   27.406  1.00 43.34  ? 302 PRO A C   1 
ATOM   2258 O  O   . PRO A 1 303 ? 85.580  6.743   27.881  1.00 43.80  ? 302 PRO A O   1 
ATOM   2259 C  CB  . PRO A 1 303 ? 82.737  8.026   28.899  1.00 48.27  ? 302 PRO A CB  1 
ATOM   2260 C  CG  . PRO A 1 303 ? 81.797  9.183   28.808  1.00 53.09  ? 302 PRO A CG  1 
ATOM   2261 C  CD  . PRO A 1 303 ? 82.177  9.892   27.552  1.00 43.61  ? 302 PRO A CD  1 
ATOM   2262 N  N   . ALA A 1 304 ? 84.260  7.328   26.150  1.00 41.69  ? 303 ALA A N   1 
ATOM   2263 C  CA  . ALA A 1 304 ? 84.834  6.311   25.277  1.00 43.76  ? 303 ALA A CA  1 
ATOM   2264 C  C   . ALA A 1 304 ? 86.279  6.642   24.926  1.00 46.01  ? 303 ALA A C   1 
ATOM   2265 O  O   . ALA A 1 304 ? 87.159  5.774   24.980  1.00 45.90  ? 303 ALA A O   1 
ATOM   2266 C  CB  . ALA A 1 304 ? 83.990  6.169   24.011  1.00 41.31  ? 303 ALA A CB  1 
ATOM   2267 N  N   . VAL A 1 305 ? 86.544  7.899   24.569  1.00 42.67  ? 304 VAL A N   1 
ATOM   2268 C  CA  . VAL A 1 305 ? 87.903  8.284   24.206  1.00 41.43  ? 304 VAL A CA  1 
ATOM   2269 C  C   . VAL A 1 305 ? 88.800  8.299   25.437  1.00 43.02  ? 304 VAL A C   1 
ATOM   2270 O  O   . VAL A 1 305 ? 89.986  7.954   25.361  1.00 44.77  ? 304 VAL A O   1 
ATOM   2271 C  CB  . VAL A 1 305 ? 87.898  9.643   23.487  1.00 40.55  ? 304 VAL A CB  1 
ATOM   2272 C  CG1 . VAL A 1 305 ? 89.314  10.095  23.196  1.00 39.98  ? 304 VAL A CG1 1 
ATOM   2273 C  CG2 . VAL A 1 305 ? 87.102  9.550   22.206  1.00 51.06  ? 304 VAL A CG2 1 
ATOM   2274 N  N   . ALA A 1 306 ? 88.253  8.694   26.591  1.00 39.65  ? 305 ALA A N   1 
ATOM   2275 C  CA  . ALA A 1 306 ? 89.039  8.679   27.821  1.00 42.68  ? 305 ALA A CA  1 
ATOM   2276 C  C   . ALA A 1 306 ? 89.444  7.260   28.196  1.00 45.14  ? 305 ALA A C   1 
ATOM   2277 O  O   . ALA A 1 306 ? 90.607  7.005   28.531  1.00 45.04  ? 305 ALA A O   1 
ATOM   2278 C  CB  . ALA A 1 306 ? 88.257  9.332   28.959  1.00 37.37  ? 305 ALA A CB  1 
ATOM   2279 N  N   . ALA A 1 307 ? 88.497  6.322   28.147  1.00 44.86  ? 306 ALA A N   1 
ATOM   2280 C  CA  . ALA A 1 307 ? 88.834  4.929   28.417  1.00 41.74  ? 306 ALA A CA  1 
ATOM   2281 C  C   . ALA A 1 307 ? 89.868  4.418   27.423  1.00 42.99  ? 306 ALA A C   1 
ATOM   2282 O  O   . ALA A 1 307 ? 90.846  3.769   27.811  1.00 46.32  ? 306 ALA A O   1 
ATOM   2283 C  CB  . ALA A 1 307 ? 87.576  4.064   28.377  1.00 40.33  ? 306 ALA A CB  1 
ATOM   2284 N  N   . ALA A 1 308 ? 89.681  4.719   26.137  1.00 39.07  ? 307 ALA A N   1 
ATOM   2285 C  CA  . ALA A 1 308 ? 90.633  4.255   25.135  1.00 42.51  ? 307 ALA A CA  1 
ATOM   2286 C  C   . ALA A 1 308 ? 92.003  4.898   25.330  1.00 44.38  ? 307 ALA A C   1 
ATOM   2287 O  O   . ALA A 1 308 ? 93.033  4.224   25.219  1.00 48.19  ? 307 ALA A O   1 
ATOM   2288 C  CB  . ALA A 1 308 ? 90.098  4.533   23.732  1.00 39.89  ? 307 ALA A CB  1 
ATOM   2289 N  N   . SER A 1 309 ? 92.038  6.195   25.632  1.00 41.06  ? 308 SER A N   1 
ATOM   2290 C  CA  . SER A 1 309 ? 93.322  6.867   25.775  1.00 37.48  ? 308 SER A CA  1 
ATOM   2291 C  C   . SER A 1 309 ? 94.049  6.433   27.037  1.00 42.77  ? 308 SER A C   1 
ATOM   2292 O  O   . SER A 1 309 ? 95.284  6.380   27.050  1.00 44.64  ? 308 SER A O   1 
ATOM   2293 C  CB  . SER A 1 309 ? 93.122  8.377   25.762  1.00 41.32  ? 308 SER A CB  1 
ATOM   2294 O  OG  . SER A 1 309 ? 92.595  8.781   24.511  1.00 45.29  ? 308 SER A OG  1 
ATOM   2295 N  N   . PHE A 1 310 ? 93.311  6.123   28.103  1.00 42.53  ? 309 PHE A N   1 
ATOM   2296 C  CA  . PHE A 1 310 ? 93.941  5.590   29.304  1.00 41.45  ? 309 PHE A CA  1 
ATOM   2297 C  C   . PHE A 1 310 ? 94.552  4.224   29.034  1.00 44.30  ? 309 PHE A C   1 
ATOM   2298 O  O   . PHE A 1 310 ? 95.654  3.923   29.510  1.00 48.88  ? 309 PHE A O   1 
ATOM   2299 C  CB  . PHE A 1 310 ? 92.919  5.509   30.434  1.00 45.97  ? 309 PHE A CB  1 
ATOM   2300 C  CG  . PHE A 1 310 ? 93.468  4.952   31.710  1.00 43.54  ? 309 PHE A CG  1 
ATOM   2301 C  CD1 . PHE A 1 310 ? 94.521  5.572   32.356  1.00 46.02  ? 309 PHE A CD1 1 
ATOM   2302 C  CD2 . PHE A 1 310 ? 92.923  3.809   32.268  1.00 50.42  ? 309 PHE A CD2 1 
ATOM   2303 C  CE1 . PHE A 1 310 ? 95.026  5.062   33.537  1.00 46.73  ? 309 PHE A CE1 1 
ATOM   2304 C  CE2 . PHE A 1 310 ? 93.420  3.291   33.449  1.00 53.73  ? 309 PHE A CE2 1 
ATOM   2305 C  CZ  . PHE A 1 310 ? 94.475  3.920   34.086  1.00 52.25  ? 309 PHE A CZ  1 
ATOM   2306 N  N   . THR A 1 311 ? 93.848  3.386   28.273  1.00 42.56  ? 310 THR A N   1 
ATOM   2307 C  CA  . THR A 1 311 ? 94.407  2.099   27.884  1.00 42.93  ? 310 THR A CA  1 
ATOM   2308 C  C   . THR A 1 311 ? 95.683  2.283   27.075  1.00 46.79  ? 310 THR A C   1 
ATOM   2309 O  O   . THR A 1 311 ? 96.681  1.588   27.305  1.00 40.42  ? 310 THR A O   1 
ATOM   2310 C  CB  . THR A 1 311 ? 93.375  1.301   27.086  1.00 47.41  ? 310 THR A CB  1 
ATOM   2311 O  OG1 . THR A 1 311 ? 92.177  1.159   27.860  1.00 45.15  ? 310 THR A OG1 1 
ATOM   2312 C  CG2 . THR A 1 311 ? 93.919  -0.079  26.741  1.00 40.60  ? 310 THR A CG2 1 
ATOM   2313 N  N   . VAL A 1 312 ? 95.672  3.227   26.129  1.00 44.97  ? 311 VAL A N   1 
ATOM   2314 C  CA  . VAL A 1 312 ? 96.853  3.481   25.310  1.00 42.16  ? 311 VAL A CA  1 
ATOM   2315 C  C   . VAL A 1 312 ? 98.018  3.923   26.183  1.00 45.14  ? 311 VAL A C   1 
ATOM   2316 O  O   . VAL A 1 312 ? 99.155  3.464   26.009  1.00 45.97  ? 311 VAL A O   1 
ATOM   2317 C  CB  . VAL A 1 312 ? 96.540  4.523   24.220  1.00 47.94  ? 311 VAL A CB  1 
ATOM   2318 C  CG1 . VAL A 1 312 ? 97.830  4.992   23.549  1.00 44.60  ? 311 VAL A CG1 1 
ATOM   2319 C  CG2 . VAL A 1 312 ? 95.574  3.954   23.194  1.00 35.85  ? 311 VAL A CG2 1 
ATOM   2320 N  N   . TRP A 1 313 ? 97.756  4.813   27.143  1.00 44.35  ? 312 TRP A N   1 
ATOM   2321 C  CA  . TRP A 1 313 ? 98.827  5.274   28.019  1.00 45.18  ? 312 TRP A CA  1 
ATOM   2322 C  C   . TRP A 1 313 ? 99.389  4.132   28.858  1.00 46.60  ? 312 TRP A C   1 
ATOM   2323 O  O   . TRP A 1 313 ? 100.599 4.073   29.105  1.00 45.88  ? 312 TRP A O   1 
ATOM   2324 C  CB  . TRP A 1 313 ? 98.331  6.405   28.917  1.00 43.88  ? 312 TRP A CB  1 
ATOM   2325 C  CG  . TRP A 1 313 ? 99.332  6.780   29.949  1.00 47.68  ? 312 TRP A CG  1 
ATOM   2326 C  CD1 . TRP A 1 313 ? 100.395 7.623   29.796  1.00 47.99  ? 312 TRP A CD1 1 
ATOM   2327 C  CD2 . TRP A 1 313 ? 99.387  6.304   31.296  1.00 51.76  ? 312 TRP A CD2 1 
ATOM   2328 N  NE1 . TRP A 1 313 ? 101.105 7.706   30.969  1.00 54.07  ? 312 TRP A NE1 1 
ATOM   2329 C  CE2 . TRP A 1 313 ? 100.505 6.907   31.907  1.00 56.60  ? 312 TRP A CE2 1 
ATOM   2330 C  CE3 . TRP A 1 313 ? 98.595  5.430   32.047  1.00 48.58  ? 312 TRP A CE3 1 
ATOM   2331 C  CZ2 . TRP A 1 313 ? 100.850 6.666   33.235  1.00 62.37  ? 312 TRP A CZ2 1 
ATOM   2332 C  CZ3 . TRP A 1 313 ? 98.938  5.192   33.364  1.00 55.70  ? 312 TRP A CZ3 1 
ATOM   2333 C  CH2 . TRP A 1 313 ? 100.058 5.807   33.945  1.00 60.77  ? 312 TRP A CH2 1 
ATOM   2334 N  N   . LEU A 1 314 ? 98.527  3.218   29.313  1.00 44.21  ? 313 LEU A N   1 
ATOM   2335 C  CA  . LEU A 1 314 ? 99.012  2.065   30.066  1.00 47.15  ? 313 LEU A CA  1 
ATOM   2336 C  C   . LEU A 1 314 ? 99.955  1.218   29.220  1.00 43.07  ? 313 LEU A C   1 
ATOM   2337 O  O   . LEU A 1 314 ? 100.934 0.661   29.732  1.00 41.98  ? 313 LEU A O   1 
ATOM   2338 C  CB  . LEU A 1 314 ? 97.837  1.218   30.559  1.00 44.13  ? 313 LEU A CB  1 
ATOM   2339 C  CG  . LEU A 1 314 ? 96.981  1.797   31.686  1.00 48.72  ? 313 LEU A CG  1 
ATOM   2340 C  CD1 . LEU A 1 314 ? 95.631  1.103   31.739  1.00 47.24  ? 313 LEU A CD1 1 
ATOM   2341 C  CD2 . LEU A 1 314 ? 97.696  1.682   33.019  1.00 45.49  ? 313 LEU A CD2 1 
ATOM   2342 N  N   . LEU A 1 315 ? 99.679  1.114   27.922  1.00 38.58  ? 314 LEU A N   1 
ATOM   2343 C  CA  . LEU A 1 315 ? 100.487 0.317   27.012  1.00 42.88  ? 314 LEU A CA  1 
ATOM   2344 C  C   . LEU A 1 315 ? 101.350 1.189   26.105  1.00 47.60  ? 314 LEU A C   1 
ATOM   2345 O  O   . LEU A 1 315 ? 101.645 0.806   24.970  1.00 42.86  ? 314 LEU A O   1 
ATOM   2346 C  CB  . LEU A 1 315 ? 99.599  -0.603  26.176  1.00 48.66  ? 314 LEU A CB  1 
ATOM   2347 C  CG  . LEU A 1 315 ? 98.759  -1.634  26.925  1.00 43.55  ? 314 LEU A CG  1 
ATOM   2348 C  CD1 . LEU A 1 315 ? 97.970  -2.458  25.929  1.00 53.99  ? 314 LEU A CD1 1 
ATOM   2349 C  CD2 . LEU A 1 315 ? 99.643  -2.528  27.778  1.00 44.43  ? 314 LEU A CD2 1 
ATOM   2350 N  N   . ARG A 1 316 ? 101.764 2.363   26.598  1.00 44.23  ? 315 ARG A N   1 
ATOM   2351 C  CA  . ARG A 1 316 ? 102.540 3.278   25.768  1.00 46.15  ? 315 ARG A CA  1 
ATOM   2352 C  C   . ARG A 1 316 ? 103.842 2.647   25.292  1.00 49.01  ? 315 ARG A C   1 
ATOM   2353 O  O   . ARG A 1 316 ? 104.276 2.905   24.164  1.00 50.02  ? 315 ARG A O   1 
ATOM   2354 C  CB  . ARG A 1 316 ? 102.817 4.584   26.521  1.00 45.40  ? 315 ARG A CB  1 
ATOM   2355 C  CG  . ARG A 1 316 ? 103.561 4.457   27.843  1.00 46.22  ? 315 ARG A CG  1 
ATOM   2356 C  CD  . ARG A 1 316 ? 103.350 5.724   28.684  1.00 47.33  ? 315 ARG A CD  1 
ATOM   2357 N  NE  . ARG A 1 316 ? 104.167 5.741   29.892  1.00 47.67  ? 315 ARG A NE  1 
ATOM   2358 C  CZ  . ARG A 1 316 ? 103.907 5.033   30.983  1.00 44.67  ? 315 ARG A CZ  1 
ATOM   2359 N  NH1 . ARG A 1 316 ? 102.854 4.237   31.056  1.00 45.63  ? 315 ARG A NH1 1 
ATOM   2360 N  NH2 . ARG A 1 316 ? 104.729 5.120   32.024  1.00 53.59  ? 315 ARG A NH2 1 
ATOM   2361 N  N   . ASP A 1 317 ? 104.467 1.807   26.123  1.00 44.34  ? 316 ASP A N   1 
ATOM   2362 C  CA  . ASP A 1 317 ? 105.689 1.137   25.696  1.00 44.54  ? 316 ASP A CA  1 
ATOM   2363 C  C   . ASP A 1 317 ? 105.405 0.121   24.596  1.00 47.33  ? 316 ASP A C   1 
ATOM   2364 O  O   . ASP A 1 317 ? 106.207 -0.039  23.668  1.00 50.26  ? 316 ASP A O   1 
ATOM   2365 C  CB  . ASP A 1 317 ? 106.369 0.457   26.883  1.00 49.59  ? 316 ASP A CB  1 
ATOM   2366 C  CG  . ASP A 1 317 ? 107.220 1.412   27.702  1.00 52.78  ? 316 ASP A CG  1 
ATOM   2367 O  OD1 . ASP A 1 317 ? 107.653 1.015   28.803  1.00 60.62  ? 316 ASP A OD1 1 
ATOM   2368 O  OD2 . ASP A 1 317 ? 107.437 2.561   27.260  1.00 50.70  ? 316 ASP A OD2 1 
ATOM   2369 N  N   . PHE A 1 318 ? 104.279 -0.587  24.686  1.00 44.14  ? 317 PHE A N   1 
ATOM   2370 C  CA  . PHE A 1 318 ? 103.908 -1.491  23.603  1.00 48.65  ? 317 PHE A CA  1 
ATOM   2371 C  C   . PHE A 1 318 ? 103.526 -0.714  22.347  1.00 44.88  ? 317 PHE A C   1 
ATOM   2372 O  O   . PHE A 1 318 ? 103.875 -1.117  21.231  1.00 45.78  ? 317 PHE A O   1 
ATOM   2373 C  CB  . PHE A 1 318 ? 102.764 -2.401  24.043  1.00 46.27  ? 317 PHE A CB  1 
ATOM   2374 C  CG  . PHE A 1 318 ? 102.104 -3.127  22.910  1.00 41.68  ? 317 PHE A CG  1 
ATOM   2375 C  CD1 . PHE A 1 318 ? 102.663 -4.283  22.393  1.00 46.68  ? 317 PHE A CD1 1 
ATOM   2376 C  CD2 . PHE A 1 318 ? 100.930 -2.646  22.353  1.00 45.05  ? 317 PHE A CD2 1 
ATOM   2377 C  CE1 . PHE A 1 318 ? 102.061 -4.952  21.345  1.00 44.80  ? 317 PHE A CE1 1 
ATOM   2378 C  CE2 . PHE A 1 318 ? 100.324 -3.306  21.302  1.00 50.62  ? 317 PHE A CE2 1 
ATOM   2379 C  CZ  . PHE A 1 318 ? 100.890 -4.463  20.798  1.00 48.78  ? 317 PHE A CZ  1 
ATOM   2380 N  N   . ALA A 1 319 ? 102.808 0.400   22.509  1.00 40.94  ? 318 ALA A N   1 
ATOM   2381 C  CA  . ALA A 1 319 ? 102.421 1.206   21.354  1.00 44.49  ? 318 ALA A CA  1 
ATOM   2382 C  C   . ALA A 1 319 ? 103.643 1.773   20.643  1.00 54.28  ? 318 ALA A C   1 
ATOM   2383 O  O   . ALA A 1 319 ? 103.681 1.838   19.408  1.00 51.54  ? 318 ALA A O   1 
ATOM   2384 C  CB  . ALA A 1 319 ? 101.485 2.332   21.790  1.00 43.52  ? 318 ALA A CB  1 
ATOM   2385 N  N   . ILE A 1 320 ? 104.654 2.184   21.408  1.00 55.28  ? 319 ILE A N   1 
ATOM   2386 C  CA  . ILE A 1 320 ? 105.893 2.677   20.816  1.00 56.34  ? 319 ILE A CA  1 
ATOM   2387 C  C   . ILE A 1 320 ? 106.641 1.555   20.108  1.00 53.11  ? 319 ILE A C   1 
ATOM   2388 O  O   . ILE A 1 320 ? 107.086 1.716   18.965  1.00 52.02  ? 319 ILE A O   1 
ATOM   2389 C  CB  . ILE A 1 320 ? 106.757 3.352   21.898  1.00 54.45  ? 319 ILE A CB  1 
ATOM   2390 C  CG1 . ILE A 1 320 ? 106.170 4.720   22.254  1.00 55.46  ? 319 ILE A CG1 1 
ATOM   2391 C  CG2 . ILE A 1 320 ? 108.229 3.402   21.484  1.00 60.13  ? 319 ILE A CG2 1 
ATOM   2392 C  CD1 . ILE A 1 320 ? 106.858 5.407   23.400  1.00 51.66  ? 319 ILE A CD1 1 
ATOM   2393 N  N   . TRP A 1 321 ? 106.787 0.403   20.766  1.00 49.34  ? 320 TRP A N   1 
ATOM   2394 C  CA  . TRP A 1 321 ? 107.512 -0.710  20.162  1.00 49.37  ? 320 TRP A CA  1 
ATOM   2395 C  C   . TRP A 1 321 ? 106.823 -1.229  18.904  1.00 48.42  ? 320 TRP A C   1 
ATOM   2396 O  O   . TRP A 1 321 ? 107.492 -1.724  17.991  1.00 59.19  ? 320 TRP A O   1 
ATOM   2397 C  CB  . TRP A 1 321 ? 107.670 -1.842  21.176  1.00 54.92  ? 320 TRP A CB  1 
ATOM   2398 C  CG  . TRP A 1 321 ? 108.082 -3.144  20.559  1.00 53.70  ? 320 TRP A CG  1 
ATOM   2399 C  CD1 . TRP A 1 321 ? 109.346 -3.527  20.222  1.00 53.93  ? 320 TRP A CD1 1 
ATOM   2400 C  CD2 . TRP A 1 321 ? 107.222 -4.227  20.183  1.00 50.56  ? 320 TRP A CD2 1 
ATOM   2401 N  NE1 . TRP A 1 321 ? 109.330 -4.784  19.671  1.00 60.42  ? 320 TRP A NE1 1 
ATOM   2402 C  CE2 . TRP A 1 321 ? 108.037 -5.236  19.635  1.00 62.24  ? 320 TRP A CE2 1 
ATOM   2403 C  CE3 . TRP A 1 321 ? 105.843 -4.442  20.261  1.00 56.89  ? 320 TRP A CE3 1 
ATOM   2404 C  CZ2 . TRP A 1 321 ? 107.519 -6.444  19.170  1.00 64.34  ? 320 TRP A CZ2 1 
ATOM   2405 C  CZ3 . TRP A 1 321 ? 105.330 -5.643  19.797  1.00 57.40  ? 320 TRP A CZ3 1 
ATOM   2406 C  CH2 . TRP A 1 321 ? 106.166 -6.627  19.258  1.00 59.70  ? 320 TRP A CH2 1 
ATOM   2407 N  N   . LEU A 1 322 ? 105.499 -1.132  18.831  1.00 54.93  ? 321 LEU A N   1 
ATOM   2408 C  CA  . LEU A 1 322 ? 104.795 -1.687  17.684  1.00 57.50  ? 321 LEU A CA  1 
ATOM   2409 C  C   . LEU A 1 322 ? 104.663 -0.690  16.539  1.00 53.44  ? 321 LEU A C   1 
ATOM   2410 O  O   . LEU A 1 322 ? 104.891 -1.049  15.380  1.00 54.23  ? 321 LEU A O   1 
ATOM   2411 C  CB  . LEU A 1 322 ? 103.408 -2.180  18.105  1.00 53.19  ? 321 LEU A CB  1 
ATOM   2412 C  CG  . LEU A 1 322 ? 102.496 -2.711  16.998  1.00 51.27  ? 321 LEU A CG  1 
ATOM   2413 C  CD1 . LEU A 1 322 ? 102.490 -4.230  16.984  1.00 53.25  ? 321 LEU A CD1 1 
ATOM   2414 C  CD2 . LEU A 1 322 ? 101.092 -2.170  17.181  1.00 55.55  ? 321 LEU A CD2 1 
ATOM   2415 N  N   . LEU A 1 323 ? 104.313 0.559   16.837  1.00 55.37  ? 322 LEU A N   1 
ATOM   2416 C  CA  . LEU A 1 323 ? 103.932 1.502   15.795  1.00 60.71  ? 322 LEU A CA  1 
ATOM   2417 C  C   . LEU A 1 323 ? 105.094 2.321   15.253  1.00 68.31  ? 322 LEU A C   1 
ATOM   2418 O  O   . LEU A 1 323 ? 105.008 2.816   14.123  1.00 70.87  ? 322 LEU A O   1 
ATOM   2419 C  CB  . LEU A 1 323 ? 102.853 2.452   16.321  1.00 50.02  ? 322 LEU A CB  1 
ATOM   2420 C  CG  . LEU A 1 323 ? 101.432 1.889   16.320  1.00 56.34  ? 322 LEU A CG  1 
ATOM   2421 C  CD1 . LEU A 1 323 ? 100.585 2.583   17.367  1.00 57.16  ? 322 LEU A CD1 1 
ATOM   2422 C  CD2 . LEU A 1 323 ? 100.807 2.028   14.943  1.00 67.48  ? 322 LEU A CD2 1 
ATOM   2423 N  N   . LEU A 1 324 ? 106.171 2.476   16.012  1.00 65.62  ? 323 LEU A N   1 
ATOM   2424 C  CA  . LEU A 1 324 ? 107.233 3.391   15.631  1.00 83.93  ? 323 LEU A CA  1 
ATOM   2425 C  C   . LEU A 1 324 ? 108.585 2.691   15.646  1.00 86.84  ? 323 LEU A C   1 
ATOM   2426 O  O   . LEU A 1 324 ? 108.786 1.696   16.348  1.00 80.39  ? 323 LEU A O   1 
ATOM   2427 C  CB  . LEU A 1 324 ? 107.254 4.597   16.558  1.00 80.02  ? 323 LEU A CB  1 
ATOM   2428 C  CG  . LEU A 1 324 ? 106.131 5.625   16.406  1.00 74.55  ? 323 LEU A CG  1 
ATOM   2429 C  CD1 . LEU A 1 324 ? 105.630 6.088   17.766  1.00 69.61  ? 323 LEU A CD1 1 
ATOM   2430 C  CD2 . LEU A 1 324 ? 106.606 6.810   15.577  1.00 81.59  ? 323 LEU A CD2 1 
ATOM   2431 N  N   . SER A 1 325 ? 109.512 3.230   14.856  1.00 96.63  ? 324 SER A N   1 
ATOM   2432 C  CA  . SER A 1 325 ? 110.855 2.671   14.767  1.00 105.76 ? 324 SER A CA  1 
ATOM   2433 C  C   . SER A 1 325 ? 111.611 2.941   16.061  1.00 110.60 ? 324 SER A C   1 
ATOM   2434 O  O   . SER A 1 325 ? 111.735 4.095   16.487  1.00 110.95 ? 324 SER A O   1 
ATOM   2435 C  CB  . SER A 1 325 ? 111.596 3.268   13.572  1.00 104.16 ? 324 SER A CB  1 
ATOM   2436 O  OG  . SER A 1 325 ? 112.993 3.314   13.804  1.00 113.05 ? 324 SER A OG  1 
ATOM   2437 N  N   . ASN A 1 326 ? 112.111 1.876   16.688  1.00 120.32 ? 325 ASN A N   1 
ATOM   2438 C  CA  . ASN A 1 326 ? 112.814 1.999   17.959  1.00 118.14 ? 325 ASN A CA  1 
ATOM   2439 C  C   . ASN A 1 326 ? 114.084 2.823   17.802  1.00 118.81 ? 325 ASN A C   1 
ATOM   2440 O  O   . ASN A 1 326 ? 115.190 2.275   17.755  1.00 127.83 ? 325 ASN A O   1 
ATOM   2441 C  CB  . ASN A 1 326 ? 113.146 0.621   18.536  1.00 120.42 ? 325 ASN A CB  1 
ATOM   2442 C  CG  . ASN A 1 326 ? 113.394 0.663   20.032  1.00 123.13 ? 325 ASN A CG  1 
ATOM   2443 O  OD1 . ASN A 1 326 ? 114.338 1.302   20.497  1.00 118.74 ? 325 ASN A OD1 1 
ATOM   2444 N  ND2 . ASN A 1 326 ? 112.542 -0.012  20.793  1.00 122.32 ? 325 ASN A ND2 1 
ATOM   2445 N  N   . LYS A 1 327 ? 113.932 4.142   17.713  1.00 117.21 ? 326 LYS A N   1 
ATOM   2446 C  CA  . LYS A 1 327 ? 115.066 5.050   17.682  1.00 119.81 ? 326 LYS A CA  1 
ATOM   2447 C  C   . LYS A 1 327 ? 114.935 6.173   18.693  1.00 123.19 ? 326 LYS A C   1 
ATOM   2448 O  O   . LYS A 1 327 ? 115.845 7.003   18.797  1.00 128.03 ? 326 LYS A O   1 
ATOM   2449 C  CB  . LYS A 1 327 ? 115.248 5.645   16.279  1.00 118.21 ? 326 LYS A CB  1 
ATOM   2450 C  CG  . LYS A 1 327 ? 114.178 6.645   15.876  1.00 113.07 ? 326 LYS A CG  1 
ATOM   2451 C  CD  . LYS A 1 327 ? 114.531 7.316   14.555  1.00 106.84 ? 326 LYS A CD  1 
ATOM   2452 C  CE  . LYS A 1 327 ? 113.767 8.618   14.376  1.00 102.44 ? 326 LYS A CE  1 
ATOM   2453 N  NZ  . LYS A 1 327 ? 114.343 9.458   13.289  1.00 94.98  ? 326 LYS A NZ  1 
ATOM   2454 N  N   . PHE A 1 328 ? 113.846 6.214   19.449  1.00 126.10 ? 327 PHE A N   1 
ATOM   2455 C  CA  . PHE A 1 328 ? 113.675 7.267   20.434  1.00 126.06 ? 327 PHE A CA  1 
ATOM   2456 C  C   . PHE A 1 328 ? 113.458 6.681   21.825  1.00 127.56 ? 327 PHE A C   1 
ATOM   2457 O  O   . PHE A 1 328 ? 114.270 6.898   22.730  1.00 121.58 ? 327 PHE A O   1 
ATOM   2458 C  CB  . PHE A 1 328 ? 112.546 8.204   19.964  1.00 124.37 ? 327 PHE A CB  1 
ATOM   2459 C  CG  . PHE A 1 328 ? 111.259 7.510   19.543  1.00 126.78 ? 327 PHE A CG  1 
ATOM   2460 C  CD1 . PHE A 1 328 ? 110.341 7.027   20.475  1.00 123.33 ? 327 PHE A CD1 1 
ATOM   2461 C  CD2 . PHE A 1 328 ? 110.994 7.349   18.194  1.00 119.96 ? 327 PHE A CD2 1 
ATOM   2462 C  CE1 . PHE A 1 328 ? 109.173 6.394   20.044  1.00 124.02 ? 327 PHE A CE1 1 
ATOM   2463 C  CE2 . PHE A 1 328 ? 109.829 6.736   17.772  1.00 111.49 ? 327 PHE A CE2 1 
ATOM   2464 C  CZ  . PHE A 1 328 ? 108.926 6.261   18.709  1.00 113.58 ? 327 PHE A CZ  1 
ATOM   2465 N  N   . THR A 1 329 ? 112.399 5.889   21.971  1.00 126.58 ? 328 THR A N   1 
ATOM   2466 C  CA  . THR A 1 329 ? 111.866 5.287   23.193  1.00 123.10 ? 328 THR A CA  1 
ATOM   2467 C  C   . THR A 1 329 ? 111.790 6.247   24.379  1.00 124.73 ? 328 THR A C   1 
ATOM   2468 O  O   . THR A 1 329 ? 111.477 5.815   25.489  1.00 126.53 ? 328 THR A O   1 
ATOM   2469 C  CB  . THR A 1 329 ? 112.635 4.005   23.567  1.00 119.73 ? 328 THR A CB  1 
ATOM   2470 O  OG1 . THR A 1 329 ? 114.030 4.284   23.709  1.00 114.51 ? 328 THR A OG1 1 
ATOM   2471 C  CG2 . THR A 1 329 ? 112.466 2.950   22.498  1.00 119.43 ? 328 THR A CG2 1 
ATOM   2472 N  N   . ALA A 1 330 ? 112.011 7.541   24.162  1.00 106.43 ? 329 ALA A N   1 
ATOM   2473 C  CA  . ALA A 1 330 ? 111.837 8.549   25.195  1.00 91.01  ? 329 ALA A CA  1 
ATOM   2474 C  C   . ALA A 1 330 ? 110.489 9.261   25.116  1.00 79.58  ? 329 ALA A C   1 
ATOM   2475 O  O   . ALA A 1 330 ? 110.182 10.073  25.996  1.00 67.64  ? 329 ALA A O   1 
ATOM   2476 C  CB  . ALA A 1 330 ? 112.964 9.581   25.127  1.00 75.17  ? 329 ALA A CB  1 
ATOM   2477 N  N   . MET A 1 331 ? 109.686 8.998   24.076  1.00 74.97  ? 330 MET A N   1 
ATOM   2478 C  CA  . MET A 1 331 ? 108.377 9.645   23.956  1.00 69.86  ? 330 MET A CA  1 
ATOM   2479 C  C   . MET A 1 331 ? 107.345 9.155   24.969  1.00 65.20  ? 330 MET A C   1 
ATOM   2480 O  O   . MET A 1 331 ? 106.267 9.751   25.040  1.00 63.53  ? 330 MET A O   1 
ATOM   2481 C  CB  . MET A 1 331 ? 107.794 9.508   22.534  1.00 76.05  ? 330 MET A CB  1 
ATOM   2482 C  CG  . MET A 1 331 ? 108.532 10.263  21.445  1.00 81.28  ? 330 MET A CG  1 
ATOM   2483 S  SD  . MET A 1 331 ? 108.288 9.647   19.754  1.00 98.39  ? 330 MET A SD  1 
ATOM   2484 C  CE  . MET A 1 331 ? 106.564 9.146   19.801  1.00 75.98  ? 330 MET A CE  1 
ATOM   2485 N  N   . ARG A 1 332 ? 107.637 8.128   25.773  1.00 61.25  ? 331 ARG A N   1 
ATOM   2486 C  CA  . ARG A 1 332 ? 106.625 7.614   26.698  1.00 51.82  ? 331 ARG A CA  1 
ATOM   2487 C  C   . ARG A 1 332 ? 106.171 8.684   27.688  1.00 55.04  ? 331 ARG A C   1 
ATOM   2488 O  O   . ARG A 1 332 ? 104.990 8.742   28.055  1.00 58.24  ? 331 ARG A O   1 
ATOM   2489 C  CB  . ARG A 1 332 ? 107.161 6.394   27.444  1.00 50.65  ? 331 ARG A CB  1 
ATOM   2490 C  CG  . ARG A 1 332 ? 108.484 6.644   28.131  1.00 52.46  ? 331 ARG A CG  1 
ATOM   2491 C  CD  . ARG A 1 332 ? 109.160 5.346   28.506  1.00 53.34  ? 331 ARG A CD  1 
ATOM   2492 N  NE  . ARG A 1 332 ? 108.237 4.429   29.162  1.00 49.40  ? 331 ARG A NE  1 
ATOM   2493 C  CZ  . ARG A 1 332 ? 108.090 4.324   30.474  1.00 51.78  ? 331 ARG A CZ  1 
ATOM   2494 N  NH1 . ARG A 1 332 ? 108.791 5.070   31.311  1.00 52.70  ? 331 ARG A NH1 1 
ATOM   2495 N  NH2 . ARG A 1 332 ? 107.217 3.447   30.961  1.00 52.32  ? 331 ARG A NH2 1 
ATOM   2496 N  N   . ASP A 1 333 ? 107.090 9.547   28.124  1.00 56.16  ? 332 ASP A N   1 
ATOM   2497 C  CA  . ASP A 1 333 ? 106.725 10.603  29.061  1.00 56.24  ? 332 ASP A CA  1 
ATOM   2498 C  C   . ASP A 1 333 ? 105.818 11.649  28.428  1.00 53.82  ? 332 ASP A C   1 
ATOM   2499 O  O   . ASP A 1 333 ? 105.094 12.343  29.150  1.00 50.08  ? 332 ASP A O   1 
ATOM   2500 C  CB  . ASP A 1 333 ? 107.985 11.259  29.621  1.00 54.77  ? 332 ASP A CB  1 
ATOM   2501 C  CG  . ASP A 1 333 ? 108.874 10.270  30.351  1.00 67.42  ? 332 ASP A CG  1 
ATOM   2502 O  OD1 . ASP A 1 333 ? 108.329 9.431   31.104  1.00 60.30  ? 332 ASP A OD1 1 
ATOM   2503 O  OD2 . ASP A 1 333 ? 110.112 10.328  30.174  1.00 71.79  ? 332 ASP A OD2 1 
ATOM   2504 N  N   . LEU A 1 334 ? 105.825 11.762  27.101  1.00 51.20  ? 333 LEU A N   1 
ATOM   2505 C  CA  . LEU A 1 334 ? 104.956 12.706  26.413  1.00 48.70  ? 333 LEU A CA  1 
ATOM   2506 C  C   . LEU A 1 334 ? 103.539 12.182  26.219  1.00 47.12  ? 333 LEU A C   1 
ATOM   2507 O  O   . LEU A 1 334 ? 102.648 12.977  25.904  1.00 46.27  ? 333 LEU A O   1 
ATOM   2508 C  CB  . LEU A 1 334 ? 105.554 13.065  25.051  1.00 48.44  ? 333 LEU A CB  1 
ATOM   2509 C  CG  . LEU A 1 334 ? 106.459 14.296  25.013  1.00 47.77  ? 333 LEU A CG  1 
ATOM   2510 C  CD1 . LEU A 1 334 ? 107.774 14.019  25.711  1.00 46.32  ? 333 LEU A CD1 1 
ATOM   2511 C  CD2 . LEU A 1 334 ? 106.699 14.737  23.580  1.00 50.06  ? 333 LEU A CD2 1 
ATOM   2512 N  N   . PHE A 1 335 ? 103.307 10.879  26.409  1.00 42.25  ? 334 PHE A N   1 
ATOM   2513 C  CA  . PHE A 1 335 ? 102.018 10.290  26.049  1.00 48.60  ? 334 PHE A CA  1 
ATOM   2514 C  C   . PHE A 1 335 ? 100.890 10.845  26.910  1.00 39.96  ? 334 PHE A C   1 
ATOM   2515 O  O   . PHE A 1 335 ? 99.834  11.231  26.394  1.00 40.25  ? 334 PHE A O   1 
ATOM   2516 C  CB  . PHE A 1 335 ? 102.078 8.768   26.176  1.00 47.22  ? 334 PHE A CB  1 
ATOM   2517 C  CG  . PHE A 1 335 ? 102.450 8.061   24.904  1.00 50.08  ? 334 PHE A CG  1 
ATOM   2518 C  CD1 . PHE A 1 335 ? 103.608 8.394   24.222  1.00 47.62  ? 334 PHE A CD1 1 
ATOM   2519 C  CD2 . PHE A 1 335 ? 101.645 7.052   24.398  1.00 52.87  ? 334 PHE A CD2 1 
ATOM   2520 C  CE1 . PHE A 1 335 ? 103.955 7.736   23.059  1.00 53.34  ? 334 PHE A CE1 1 
ATOM   2521 C  CE2 . PHE A 1 335 ? 101.987 6.388   23.236  1.00 41.43  ? 334 PHE A CE2 1 
ATOM   2522 C  CZ  . PHE A 1 335 ? 103.142 6.730   22.566  1.00 52.36  ? 334 PHE A CZ  1 
ATOM   2523 N  N   . ALA A 1 336 ? 101.105 10.893  28.226  1.00 45.28  ? 335 ALA A N   1 
ATOM   2524 C  CA  . ALA A 1 336 ? 100.061 11.304  29.159  1.00 45.99  ? 335 ALA A CA  1 
ATOM   2525 C  C   . ALA A 1 336 ? 99.511  12.679  28.809  1.00 41.09  ? 335 ALA A C   1 
ATOM   2526 O  O   . ALA A 1 336 ? 98.307  12.849  28.595  1.00 39.48  ? 335 ALA A O   1 
ATOM   2527 C  CB  . ALA A 1 336 ? 100.616 11.296  30.581  1.00 47.35  ? 335 ALA A CB  1 
ATOM   2528 N  N   . TRP A 1 337 ? 100.386 13.681  28.754  1.00 43.75  ? 336 TRP A N   1 
ATOM   2529 C  CA  . TRP A 1 337 ? 99.950  15.029  28.416  1.00 38.62  ? 336 TRP A CA  1 
ATOM   2530 C  C   . TRP A 1 337 ? 99.246  15.050  27.067  1.00 42.97  ? 336 TRP A C   1 
ATOM   2531 O  O   . TRP A 1 337 ? 98.133  15.574  26.943  1.00 40.43  ? 336 TRP A O   1 
ATOM   2532 C  CB  . TRP A 1 337 ? 101.149 15.972  28.417  1.00 43.36  ? 336 TRP A CB  1 
ATOM   2533 C  CG  . TRP A 1 337 ? 101.944 15.895  29.678  1.00 49.71  ? 336 TRP A CG  1 
ATOM   2534 C  CD1 . TRP A 1 337 ? 102.968 15.034  29.953  1.00 49.42  ? 336 TRP A CD1 1 
ATOM   2535 C  CD2 . TRP A 1 337 ? 101.789 16.719  30.837  1.00 50.48  ? 336 TRP A CD2 1 
ATOM   2536 N  NE1 . TRP A 1 337 ? 103.457 15.270  31.213  1.00 54.08  ? 336 TRP A NE1 1 
ATOM   2537 C  CE2 . TRP A 1 337 ? 102.749 16.300  31.777  1.00 55.20  ? 336 TRP A CE2 1 
ATOM   2538 C  CE3 . TRP A 1 337 ? 100.931 17.771  31.171  1.00 43.94  ? 336 TRP A CE3 1 
ATOM   2539 C  CZ2 . TRP A 1 337 ? 102.873 16.894  33.029  1.00 56.88  ? 336 TRP A CZ2 1 
ATOM   2540 C  CZ3 . TRP A 1 337 ? 101.058 18.360  32.409  1.00 46.46  ? 336 TRP A CZ3 1 
ATOM   2541 C  CH2 . TRP A 1 337 ? 102.020 17.921  33.324  1.00 58.33  ? 336 TRP A CH2 1 
ATOM   2542 N  N   . GLN A 1 338 ? 99.875  14.458  26.048  1.00 41.44  ? 337 GLN A N   1 
ATOM   2543 C  CA  . GLN A 1 338 ? 99.294  14.463  24.710  1.00 39.05  ? 337 GLN A CA  1 
ATOM   2544 C  C   . GLN A 1 338 ? 97.935  13.773  24.694  1.00 41.39  ? 337 GLN A C   1 
ATOM   2545 O  O   . GLN A 1 338 ? 96.989  14.260  24.060  1.00 38.61  ? 337 GLN A O   1 
ATOM   2546 C  CB  . GLN A 1 338 ? 100.255 13.794  23.729  1.00 40.42  ? 337 GLN A CB  1 
ATOM   2547 C  CG  . GLN A 1 338 ? 99.840  13.903  22.277  1.00 44.27  ? 337 GLN A CG  1 
ATOM   2548 C  CD  . GLN A 1 338 ? 100.281 15.210  21.642  1.00 46.77  ? 337 GLN A CD  1 
ATOM   2549 O  OE1 . GLN A 1 338 ? 101.064 15.968  22.221  1.00 43.71  ? 337 GLN A OE1 1 
ATOM   2550 N  NE2 . GLN A 1 338 ? 99.774  15.484  20.446  1.00 48.73  ? 337 GLN A NE2 1 
ATOM   2551 N  N   . LEU A 1 339 ? 97.813  12.645  25.400  1.00 43.60  ? 338 LEU A N   1 
ATOM   2552 C  CA  . LEU A 1 339 ? 96.564  11.888  25.386  1.00 40.38  ? 338 LEU A CA  1 
ATOM   2553 C  C   . LEU A 1 339 ? 95.441  12.653  26.076  1.00 41.42  ? 338 LEU A C   1 
ATOM   2554 O  O   . LEU A 1 339 ? 94.282  12.588  25.649  1.00 39.39  ? 338 LEU A O   1 
ATOM   2555 C  CB  . LEU A 1 339 ? 96.775  10.523  26.040  1.00 38.20  ? 338 LEU A CB  1 
ATOM   2556 C  CG  . LEU A 1 339 ? 97.468  9.495   25.147  1.00 39.26  ? 338 LEU A CG  1 
ATOM   2557 C  CD1 . LEU A 1 339 ? 97.825  8.241   25.925  1.00 38.71  ? 338 LEU A CD1 1 
ATOM   2558 C  CD2 . LEU A 1 339 ? 96.592  9.162   23.954  1.00 40.62  ? 338 LEU A CD2 1 
ATOM   2559 N  N   . VAL A 1 340 ? 95.761  13.377  27.150  1.00 40.50  ? 339 VAL A N   1 
ATOM   2560 C  CA  . VAL A 1 340 ? 94.762  14.217  27.801  1.00 39.65  ? 339 VAL A CA  1 
ATOM   2561 C  C   . VAL A 1 340 ? 94.285  15.300  26.842  1.00 40.43  ? 339 VAL A C   1 
ATOM   2562 O  O   . VAL A 1 340 ? 93.080  15.533  26.682  1.00 37.29  ? 339 VAL A O   1 
ATOM   2563 C  CB  . VAL A 1 340 ? 95.333  14.822  29.093  1.00 36.03  ? 339 VAL A CB  1 
ATOM   2564 C  CG1 . VAL A 1 340 ? 94.413  15.907  29.608  1.00 40.16  ? 339 VAL A CG1 1 
ATOM   2565 C  CG2 . VAL A 1 340 ? 95.536  13.743  30.134  1.00 37.95  ? 339 VAL A CG2 1 
ATOM   2566 N  N   . GLY A 1 341 ? 95.229  15.981  26.189  1.00 34.09  ? 340 GLY A N   1 
ATOM   2567 C  CA  . GLY A 1 341 ? 94.853  16.954  25.182  1.00 38.49  ? 340 GLY A CA  1 
ATOM   2568 C  C   . GLY A 1 341 ? 94.007  16.353  24.080  1.00 38.50  ? 340 GLY A C   1 
ATOM   2569 O  O   . GLY A 1 341 ? 93.082  17.001  23.580  1.00 36.58  ? 340 GLY A O   1 
ATOM   2570 N  N   . ASP A 1 342 ? 94.293  15.100  23.704  1.00 38.62  ? 341 ASP A N   1 
ATOM   2571 C  CA  . ASP A 1 342 ? 93.508  14.442  22.664  1.00 36.40  ? 341 ASP A CA  1 
ATOM   2572 C  C   . ASP A 1 342 ? 92.069  14.219  23.111  1.00 36.80  ? 341 ASP A C   1 
ATOM   2573 O  O   . ASP A 1 342 ? 91.134  14.392  22.320  1.00 37.27  ? 341 ASP A O   1 
ATOM   2574 C  CB  . ASP A 1 342 ? 94.155  13.117  22.271  1.00 36.44  ? 341 ASP A CB  1 
ATOM   2575 C  CG  . ASP A 1 342 ? 95.368  13.307  21.391  1.00 40.79  ? 341 ASP A CG  1 
ATOM   2576 O  OD1 . ASP A 1 342 ? 95.587  14.440  20.916  1.00 40.62  ? 341 ASP A OD1 1 
ATOM   2577 O  OD2 . ASP A 1 342 ? 96.105  12.327  21.172  1.00 49.61  ? 341 ASP A OD2 1 
ATOM   2578 N  N   . VAL A 1 343 ? 91.871  13.839  24.376  1.00 36.16  ? 342 VAL A N   1 
ATOM   2579 C  CA  . VAL A 1 343 ? 90.518  13.609  24.878  1.00 36.87  ? 342 VAL A CA  1 
ATOM   2580 C  C   . VAL A 1 343 ? 89.699  14.887  24.775  1.00 36.63  ? 342 VAL A C   1 
ATOM   2581 O  O   . VAL A 1 343 ? 88.583  14.893  24.242  1.00 37.32  ? 342 VAL A O   1 
ATOM   2582 C  CB  . VAL A 1 343 ? 90.557  13.082  26.324  1.00 36.74  ? 342 VAL A CB  1 
ATOM   2583 C  CG1 . VAL A 1 343 ? 89.176  13.181  26.951  1.00 40.06  ? 342 VAL A CG1 1 
ATOM   2584 C  CG2 . VAL A 1 343 ? 91.067  11.651  26.365  1.00 32.60  ? 342 VAL A CG2 1 
ATOM   2585 N  N   . LEU A 1 344 ? 90.257  15.998  25.259  1.00 35.08  ? 343 LEU A N   1 
ATOM   2586 C  CA  . LEU A 1 344 ? 89.548  17.266  25.177  1.00 37.06  ? 343 LEU A CA  1 
ATOM   2587 C  C   . LEU A 1 344 ? 89.424  17.759  23.741  1.00 36.30  ? 343 LEU A C   1 
ATOM   2588 O  O   . LEU A 1 344 ? 88.449  18.440  23.408  1.00 40.43  ? 343 LEU A O   1 
ATOM   2589 C  CB  . LEU A 1 344 ? 90.250  18.301  26.046  1.00 38.53  ? 343 LEU A CB  1 
ATOM   2590 C  CG  . LEU A 1 344 ? 89.893  18.065  27.509  1.00 41.39  ? 343 LEU A CG  1 
ATOM   2591 C  CD1 . LEU A 1 344 ? 91.122  18.208  28.369  1.00 47.10  ? 343 LEU A CD1 1 
ATOM   2592 C  CD2 . LEU A 1 344 ? 88.806  19.018  27.943  1.00 44.24  ? 343 LEU A CD2 1 
ATOM   2593 N  N   . LYS A 1 345 ? 90.387  17.431  22.878  1.00 35.06  ? 344 LYS A N   1 
ATOM   2594 C  CA  . LYS A 1 345 ? 90.273  17.834  21.478  1.00 37.08  ? 344 LYS A CA  1 
ATOM   2595 C  C   . LYS A 1 345 ? 89.134  17.097  20.792  1.00 36.47  ? 344 LYS A C   1 
ATOM   2596 O  O   . LYS A 1 345 ? 88.409  17.684  19.979  1.00 33.87  ? 344 LYS A O   1 
ATOM   2597 C  CB  . LYS A 1 345 ? 91.586  17.585  20.739  1.00 36.78  ? 344 LYS A CB  1 
ATOM   2598 C  CG  . LYS A 1 345 ? 91.614  18.143  19.320  1.00 42.21  ? 344 LYS A CG  1 
ATOM   2599 C  CD  . LYS A 1 345 ? 93.048  18.325  18.844  1.00 44.58  ? 344 LYS A CD  1 
ATOM   2600 C  CE  . LYS A 1 345 ? 93.119  18.734  17.394  1.00 44.22  ? 344 LYS A CE  1 
ATOM   2601 N  NZ  . LYS A 1 345 ? 94.501  18.543  16.873  1.00 56.66  ? 344 LYS A NZ  1 
ATOM   2602 N  N   . VAL A 1 346 ? 88.962  15.810  21.109  1.00 34.24  ? 345 VAL A N   1 
ATOM   2603 C  CA  . VAL A 1 346 ? 87.820  15.062  20.592  1.00 35.26  ? 345 VAL A CA  1 
ATOM   2604 C  C   . VAL A 1 346 ? 86.522  15.715  21.042  1.00 34.55  ? 345 VAL A C   1 
ATOM   2605 O  O   . VAL A 1 346 ? 85.591  15.895  20.249  1.00 32.75  ? 345 VAL A O   1 
ATOM   2606 C  CB  . VAL A 1 346 ? 87.892  13.589  21.037  1.00 36.60  ? 345 VAL A CB  1 
ATOM   2607 C  CG1 . VAL A 1 346 ? 86.561  12.915  20.819  1.00 34.89  ? 345 VAL A CG1 1 
ATOM   2608 C  CG2 . VAL A 1 346 ? 88.976  12.857  20.283  1.00 33.16  ? 345 VAL A CG2 1 
ATOM   2609 N  N   . GLY A 1 347 ? 86.447  16.092  22.321  1.00 38.22  ? 346 GLY A N   1 
ATOM   2610 C  CA  . GLY A 1 347 ? 85.298  16.845  22.793  1.00 35.28  ? 346 GLY A CA  1 
ATOM   2611 C  C   . GLY A 1 347 ? 85.120  18.150  22.044  1.00 32.64  ? 346 GLY A C   1 
ATOM   2612 O  O   . GLY A 1 347 ? 83.999  18.547  21.726  1.00 37.60  ? 346 GLY A O   1 
ATOM   2613 N  N   . ALA A 1 348 ? 86.225  18.825  21.736  1.00 32.97  ? 347 ALA A N   1 
ATOM   2614 C  CA  . ALA A 1 348 ? 86.133  20.069  20.985  1.00 34.02  ? 347 ALA A CA  1 
ATOM   2615 C  C   . ALA A 1 348 ? 85.733  19.821  19.538  1.00 37.73  ? 347 ALA A C   1 
ATOM   2616 O  O   . ALA A 1 348 ? 85.168  20.714  18.897  1.00 37.22  ? 347 ALA A O   1 
ATOM   2617 C  CB  . ALA A 1 348 ? 87.460  20.824  21.053  1.00 34.64  ? 347 ALA A CB  1 
ATOM   2618 N  N   . TYR A 1 349 ? 86.011  18.622  19.007  1.00 36.73  ? 348 TYR A N   1 
ATOM   2619 C  CA  . TYR A 1 349 ? 85.586  18.297  17.646  1.00 36.65  ? 348 TYR A CA  1 
ATOM   2620 C  C   . TYR A 1 349 ? 84.071  18.270  17.523  1.00 36.53  ? 348 TYR A C   1 
ATOM   2621 O  O   . TYR A 1 349 ? 83.532  18.583  16.456  1.00 37.63  ? 348 TYR A O   1 
ATOM   2622 C  CB  . TYR A 1 349 ? 86.150  16.946  17.210  1.00 36.01  ? 348 TYR A CB  1 
ATOM   2623 C  CG  . TYR A 1 349 ? 87.530  17.000  16.603  1.00 36.93  ? 348 TYR A CG  1 
ATOM   2624 C  CD1 . TYR A 1 349 ? 88.365  18.083  16.829  1.00 41.82  ? 348 TYR A CD1 1 
ATOM   2625 C  CD2 . TYR A 1 349 ? 88.007  15.954  15.822  1.00 40.59  ? 348 TYR A CD2 1 
ATOM   2626 C  CE1 . TYR A 1 349 ? 89.633  18.135  16.286  1.00 45.84  ? 348 TYR A CE1 1 
ATOM   2627 C  CE2 . TYR A 1 349 ? 89.278  15.995  15.272  1.00 47.19  ? 348 TYR A CE2 1 
ATOM   2628 C  CZ  . TYR A 1 349 ? 90.085  17.091  15.512  1.00 47.16  ? 348 TYR A CZ  1 
ATOM   2629 O  OH  . TYR A 1 349 ? 91.348  17.146  14.981  1.00 49.94  ? 348 TYR A OH  1 
ATOM   2630 N  N   . VAL A 1 350 ? 83.371  17.886  18.594  1.00 32.85  ? 349 VAL A N   1 
ATOM   2631 C  CA  . VAL A 1 350 ? 81.912  17.838  18.550  1.00 31.71  ? 349 VAL A CA  1 
ATOM   2632 C  C   . VAL A 1 350 ? 81.345  19.215  18.226  1.00 35.62  ? 349 VAL A C   1 
ATOM   2633 O  O   . VAL A 1 350 ? 80.457  19.356  17.376  1.00 34.76  ? 349 VAL A O   1 
ATOM   2634 C  CB  . VAL A 1 350 ? 81.353  17.288  19.875  1.00 33.72  ? 349 VAL A CB  1 
ATOM   2635 C  CG1 . VAL A 1 350 ? 79.843  17.391  19.885  1.00 26.19  ? 349 VAL A CG1 1 
ATOM   2636 C  CG2 . VAL A 1 350 ? 81.791  15.841  20.074  1.00 31.52  ? 349 VAL A CG2 1 
ATOM   2637 N  N   . PHE A 1 351 ? 81.861  20.254  18.885  1.00 33.65  ? 350 PHE A N   1 
ATOM   2638 C  CA  . PHE A 1 351 ? 81.458  21.612  18.539  1.00 36.71  ? 350 PHE A CA  1 
ATOM   2639 C  C   . PHE A 1 351 ? 81.969  22.009  17.159  1.00 38.15  ? 350 PHE A C   1 
ATOM   2640 O  O   . PHE A 1 351 ? 81.287  22.741  16.431  1.00 37.21  ? 350 PHE A O   1 
ATOM   2641 C  CB  . PHE A 1 351 ? 81.958  22.596  19.597  1.00 33.23  ? 350 PHE A CB  1 
ATOM   2642 C  CG  . PHE A 1 351 ? 81.438  22.314  20.985  1.00 36.85  ? 350 PHE A CG  1 
ATOM   2643 C  CD1 . PHE A 1 351 ? 80.148  22.666  21.344  1.00 33.20  ? 350 PHE A CD1 1 
ATOM   2644 C  CD2 . PHE A 1 351 ? 82.248  21.706  21.931  1.00 35.93  ? 350 PHE A CD2 1 
ATOM   2645 C  CE1 . PHE A 1 351 ? 79.673  22.412  22.617  1.00 36.12  ? 350 PHE A CE1 1 
ATOM   2646 C  CE2 . PHE A 1 351 ? 81.779  21.450  23.206  1.00 37.25  ? 350 PHE A CE2 1 
ATOM   2647 C  CZ  . PHE A 1 351 ? 80.489  21.803  23.549  1.00 35.34  ? 350 PHE A CZ  1 
ATOM   2648 N  N   . GLY A 1 352 ? 83.160  21.537  16.782  1.00 35.09  ? 351 GLY A N   1 
ATOM   2649 C  CA  . GLY A 1 352 ? 83.704  21.889  15.480  1.00 34.75  ? 351 GLY A CA  1 
ATOM   2650 C  C   . GLY A 1 352 ? 82.880  21.344  14.328  1.00 34.65  ? 351 GLY A C   1 
ATOM   2651 O  O   . GLY A 1 352 ? 82.678  22.026  13.321  1.00 35.81  ? 351 GLY A O   1 
ATOM   2652 N  N   . TYR A 1 353 ? 82.394  20.105  14.457  1.00 35.66  ? 352 TYR A N   1 
ATOM   2653 C  CA  . TYR A 1 353 ? 81.557  19.539  13.405  1.00 36.97  ? 352 TYR A CA  1 
ATOM   2654 C  C   . TYR A 1 353 ? 80.195  20.213  13.357  1.00 34.72  ? 352 TYR A C   1 
ATOM   2655 O  O   . TYR A 1 353 ? 79.555  20.240  12.299  1.00 31.54  ? 352 TYR A O   1 
ATOM   2656 C  CB  . TYR A 1 353 ? 81.411  18.028  13.595  1.00 33.31  ? 352 TYR A CB  1 
ATOM   2657 C  CG  . TYR A 1 353 ? 82.532  17.263  12.941  1.00 32.98  ? 352 TYR A CG  1 
ATOM   2658 C  CD1 . TYR A 1 353 ? 83.720  17.020  13.620  1.00 34.08  ? 352 TYR A CD1 1 
ATOM   2659 C  CD2 . TYR A 1 353 ? 82.419  16.812  11.633  1.00 35.28  ? 352 TYR A CD2 1 
ATOM   2660 C  CE1 . TYR A 1 353 ? 84.761  16.335  13.016  1.00 35.35  ? 352 TYR A CE1 1 
ATOM   2661 C  CE2 . TYR A 1 353 ? 83.455  16.123  11.020  1.00 35.54  ? 352 TYR A CE2 1 
ATOM   2662 C  CZ  . TYR A 1 353 ? 84.622  15.887  11.716  1.00 35.59  ? 352 TYR A CZ  1 
ATOM   2663 O  OH  . TYR A 1 353 ? 85.655  15.204  11.114  1.00 41.73  ? 352 TYR A OH  1 
ATOM   2664 N  N   . LEU A 1 354 ? 79.742  20.773  14.482  1.00 34.22  ? 353 LEU A N   1 
ATOM   2665 C  CA  . LEU A 1 354 ? 78.541  21.599  14.452  1.00 35.83  ? 353 LEU A CA  1 
ATOM   2666 C  C   . LEU A 1 354 ? 78.745  22.812  13.557  1.00 34.50  ? 353 LEU A C   1 
ATOM   2667 O  O   . LEU A 1 354 ? 77.885  23.130  12.725  1.00 32.64  ? 353 LEU A O   1 
ATOM   2668 C  CB  . LEU A 1 354 ? 78.158  22.028  15.868  1.00 31.29  ? 353 LEU A CB  1 
ATOM   2669 C  CG  . LEU A 1 354 ? 77.058  23.084  15.998  1.00 32.94  ? 353 LEU A CG  1 
ATOM   2670 C  CD1 . LEU A 1 354 ? 75.794  22.664  15.259  1.00 30.28  ? 353 LEU A CD1 1 
ATOM   2671 C  CD2 . LEU A 1 354 ? 76.757  23.350  17.477  1.00 32.42  ? 353 LEU A CD2 1 
ATOM   2672 N  N   . VAL A 1 355 ? 79.888  23.488  13.700  1.00 31.57  ? 354 VAL A N   1 
ATOM   2673 C  CA  . VAL A 1 355 ? 80.204  24.612  12.823  1.00 34.29  ? 354 VAL A CA  1 
ATOM   2674 C  C   . VAL A 1 355 ? 80.223  24.159  11.367  1.00 37.03  ? 354 VAL A C   1 
ATOM   2675 O  O   . VAL A 1 355 ? 79.676  24.834  10.485  1.00 36.95  ? 354 VAL A O   1 
ATOM   2676 C  CB  . VAL A 1 355 ? 81.541  25.254  13.237  1.00 36.50  ? 354 VAL A CB  1 
ATOM   2677 C  CG1 . VAL A 1 355 ? 82.020  26.226  12.168  1.00 30.70  ? 354 VAL A CG1 1 
ATOM   2678 C  CG2 . VAL A 1 355 ? 81.411  25.944  14.595  1.00 39.38  ? 354 VAL A CG2 1 
ATOM   2679 N  N   . ILE A 1 356 ? 80.839  23.002  11.094  1.00 32.31  ? 355 ILE A N   1 
ATOM   2680 C  CA  . ILE A 1 356 ? 80.800  22.442  9.744   1.00 34.94  ? 355 ILE A CA  1 
ATOM   2681 C  C   . ILE A 1 356 ? 79.361  22.187  9.317   1.00 33.70  ? 355 ILE A C   1 
ATOM   2682 O  O   . ILE A 1 356 ? 78.958  22.531  8.199   1.00 37.44  ? 355 ILE A O   1 
ATOM   2683 C  CB  . ILE A 1 356 ? 81.638  21.151  9.662   1.00 37.61  ? 355 ILE A CB  1 
ATOM   2684 C  CG1 . ILE A 1 356 ? 83.025  21.366  10.262  1.00 42.13  ? 355 ILE A CG1 1 
ATOM   2685 C  CG2 . ILE A 1 356 ? 81.751  20.666  8.217   1.00 28.21  ? 355 ILE A CG2 1 
ATOM   2686 C  CD1 . ILE A 1 356 ? 84.000  21.973  9.310   1.00 43.35  ? 355 ILE A CD1 1 
ATOM   2687 N  N   . ALA A 1 357 ? 78.563  21.588  10.202  1.00 35.26  ? 356 ALA A N   1 
ATOM   2688 C  CA  . ALA A 1 357 ? 77.193  21.228  9.847   1.00 36.57  ? 356 ALA A CA  1 
ATOM   2689 C  C   . ALA A 1 357 ? 76.339  22.452  9.540   1.00 33.27  ? 356 ALA A C   1 
ATOM   2690 O  O   . ALA A 1 357 ? 75.389  22.359  8.755   1.00 34.29  ? 356 ALA A O   1 
ATOM   2691 C  CB  . ALA A 1 357 ? 76.560  20.412  10.970  1.00 33.40  ? 356 ALA A CB  1 
ATOM   2692 N  N   . LYS A 1 358 ? 76.651  23.593  10.144  1.00 34.06  ? 357 LYS A N   1 
ATOM   2693 C  CA  . LYS A 1 358 ? 75.946  24.831  9.858   1.00 35.66  ? 357 LYS A CA  1 
ATOM   2694 C  C   . LYS A 1 358 ? 76.643  25.668  8.797   1.00 36.15  ? 357 LYS A C   1 
ATOM   2695 O  O   . LYS A 1 358 ? 76.197  26.787  8.526   1.00 38.32  ? 357 LYS A O   1 
ATOM   2696 C  CB  . LYS A 1 358 ? 75.780  25.649  11.141  1.00 35.43  ? 357 LYS A CB  1 
ATOM   2697 C  CG  . LYS A 1 358 ? 74.752  25.064  12.106  1.00 44.04  ? 357 LYS A CG  1 
ATOM   2698 C  CD  . LYS A 1 358 ? 73.451  24.728  11.382  1.00 46.06  ? 357 LYS A CD  1 
ATOM   2699 C  CE  . LYS A 1 358 ? 73.009  23.287  11.634  1.00 35.23  ? 357 LYS A CE  1 
ATOM   2700 N  NZ  . LYS A 1 358 ? 71.800  22.931  10.836  1.00 35.20  ? 357 LYS A NZ  1 
ATOM   2701 N  N   . ALA A 1 359 ? 77.724  25.154  8.202   1.00 35.60  ? 358 ALA A N   1 
ATOM   2702 C  CA  . ALA A 1 359 ? 78.476  25.862  7.161   1.00 36.62  ? 358 ALA A CA  1 
ATOM   2703 C  C   . ALA A 1 359 ? 78.879  27.263  7.610   1.00 35.43  ? 358 ALA A C   1 
ATOM   2704 O  O   . ALA A 1 359 ? 78.987  28.185  6.798   1.00 34.07  ? 358 ALA A O   1 
ATOM   2705 C  CB  . ALA A 1 359 ? 77.684  25.930  5.852   1.00 31.54  ? 358 ALA A CB  1 
ATOM   2706 N  N   . SER A 1 360 ? 79.085  27.447  8.910   1.00 37.24  ? 359 SER A N   1 
ATOM   2707 C  CA  . SER A 1 360 ? 79.424  28.770  9.422   1.00 31.22  ? 359 SER A CA  1 
ATOM   2708 C  C   . SER A 1 360 ? 80.899  29.020  9.166   1.00 37.02  ? 359 SER A C   1 
ATOM   2709 O  O   . SER A 1 360 ? 81.762  28.599  9.940   1.00 35.65  ? 359 SER A O   1 
ATOM   2710 C  CB  . SER A 1 360 ? 79.099  28.893  10.901  1.00 32.81  ? 359 SER A CB  1 
ATOM   2711 O  OG  . SER A 1 360 ? 79.537  30.154  11.372  1.00 41.65  ? 359 SER A OG  1 
ATOM   2712 N  N   . LEU A 1 361 ? 81.190  29.706  8.064   1.00 38.65  ? 360 LEU A N   1 
ATOM   2713 C  CA  . LEU A 1 361 ? 82.559  30.115  7.797   1.00 39.84  ? 360 LEU A CA  1 
ATOM   2714 C  C   . LEU A 1 361 ? 83.087  31.043  8.887   1.00 42.00  ? 360 LEU A C   1 
ATOM   2715 O  O   . LEU A 1 361 ? 84.273  30.976  9.235   1.00 42.59  ? 360 LEU A O   1 
ATOM   2716 C  CB  . LEU A 1 361 ? 82.639  30.782  6.421   1.00 35.48  ? 360 LEU A CB  1 
ATOM   2717 C  CG  . LEU A 1 361 ? 84.033  31.110  5.894   1.00 37.21  ? 360 LEU A CG  1 
ATOM   2718 C  CD1 . LEU A 1 361 ? 84.987  29.970  6.180   1.00 39.03  ? 360 LEU A CD1 1 
ATOM   2719 C  CD2 . LEU A 1 361 ? 83.982  31.416  4.404   1.00 41.02  ? 360 LEU A CD2 1 
ATOM   2720 N  N   . ARG A 1 362 ? 82.231  31.900  9.457   1.00 36.12  ? 361 ARG A N   1 
ATOM   2721 C  CA  . ARG A 1 362 ? 82.731  32.848  10.449  1.00 38.37  ? 361 ARG A CA  1 
ATOM   2722 C  C   . ARG A 1 362 ? 83.131  32.143  11.739  1.00 38.86  ? 361 ARG A C   1 
ATOM   2723 O  O   . ARG A 1 362 ? 84.192  32.435  12.302  1.00 41.54  ? 361 ARG A O   1 
ATOM   2724 C  CB  . ARG A 1 362 ? 81.702  33.948  10.722  1.00 38.45  ? 361 ARG A CB  1 
ATOM   2725 C  CG  . ARG A 1 362 ? 80.395  33.492  11.330  1.00 41.94  ? 361 ARG A CG  1 
ATOM   2726 C  CD  . ARG A 1 362 ? 79.627  34.666  11.929  1.00 40.49  ? 361 ARG A CD  1 
ATOM   2727 N  NE  . ARG A 1 362 ? 78.283  34.256  12.317  1.00 44.65  ? 361 ARG A NE  1 
ATOM   2728 C  CZ  . ARG A 1 362 ? 77.407  35.022  12.953  1.00 48.67  ? 361 ARG A CZ  1 
ATOM   2729 N  NH1 . ARG A 1 362 ? 77.692  36.271  13.291  1.00 47.16  ? 361 ARG A NH1 1 
ATOM   2730 N  NH2 . ARG A 1 362 ? 76.212  34.522  13.256  1.00 52.98  ? 361 ARG A NH2 1 
ATOM   2731 N  N   . PHE A 1 363 ? 82.313  31.199  12.217  1.00 35.49  ? 362 PHE A N   1 
ATOM   2732 C  CA  . PHE A 1 363 ? 82.693  30.473  13.423  1.00 36.55  ? 362 PHE A CA  1 
ATOM   2733 C  C   . PHE A 1 363 ? 83.861  29.535  13.158  1.00 33.90  ? 362 PHE A C   1 
ATOM   2734 O  O   . PHE A 1 363 ? 84.664  29.280  14.062  1.00 34.24  ? 362 PHE A O   1 
ATOM   2735 C  CB  . PHE A 1 363 ? 81.496  29.709  13.990  1.00 37.85  ? 362 PHE A CB  1 
ATOM   2736 C  CG  . PHE A 1 363 ? 80.705  30.499  14.991  1.00 34.51  ? 362 PHE A CG  1 
ATOM   2737 C  CD1 . PHE A 1 363 ? 81.239  30.803  16.227  1.00 32.79  ? 362 PHE A CD1 1 
ATOM   2738 C  CD2 . PHE A 1 363 ? 79.440  30.972  14.678  1.00 39.14  ? 362 PHE A CD2 1 
ATOM   2739 C  CE1 . PHE A 1 363 ? 80.519  31.548  17.146  1.00 41.64  ? 362 PHE A CE1 1 
ATOM   2740 C  CE2 . PHE A 1 363 ? 78.716  31.718  15.590  1.00 38.54  ? 362 PHE A CE2 1 
ATOM   2741 C  CZ  . PHE A 1 363 ? 79.257  32.006  16.826  1.00 40.21  ? 362 PHE A CZ  1 
ATOM   2742 N  N   . TYR A 1 364 ? 83.984  29.032  11.926  1.00 33.70  ? 363 TYR A N   1 
ATOM   2743 C  CA  . TYR A 1 364 ? 85.136  28.206  11.580  1.00 33.15  ? 363 TYR A CA  1 
ATOM   2744 C  C   . TYR A 1 364 ? 86.433  28.993  11.711  1.00 33.72  ? 363 TYR A C   1 
ATOM   2745 O  O   . TYR A 1 364 ? 87.411  28.500  12.285  1.00 31.82  ? 363 TYR A O   1 
ATOM   2746 C  CB  . TYR A 1 364 ? 84.979  27.655  10.164  1.00 36.43  ? 363 TYR A CB  1 
ATOM   2747 C  CG  . TYR A 1 364 ? 85.951  26.550  9.818   1.00 38.61  ? 363 TYR A CG  1 
ATOM   2748 C  CD1 . TYR A 1 364 ? 87.214  26.838  9.315   1.00 38.94  ? 363 TYR A CD1 1 
ATOM   2749 C  CD2 . TYR A 1 364 ? 85.603  25.218  9.985   1.00 39.63  ? 363 TYR A CD2 1 
ATOM   2750 C  CE1 . TYR A 1 364 ? 88.105  25.829  8.994   1.00 41.78  ? 363 TYR A CE1 1 
ATOM   2751 C  CE2 . TYR A 1 364 ? 86.488  24.205  9.667   1.00 41.46  ? 363 TYR A CE2 1 
ATOM   2752 C  CZ  . TYR A 1 364 ? 87.732  24.514  9.170   1.00 41.37  ? 363 TYR A CZ  1 
ATOM   2753 O  OH  . TYR A 1 364 ? 88.598  23.497  8.856   1.00 43.98  ? 363 TYR A OH  1 
ATOM   2754 N  N   . ILE A 1 365 ? 86.454  30.226  11.194  1.00 37.27  ? 364 ILE A N   1 
ATOM   2755 C  CA  . ILE A 1 365 ? 87.632  31.079  11.328  1.00 33.93  ? 364 ILE A CA  1 
ATOM   2756 C  C   . ILE A 1 365 ? 87.940  31.335  12.796  1.00 35.74  ? 364 ILE A C   1 
ATOM   2757 O  O   . ILE A 1 365 ? 89.098  31.265  13.225  1.00 38.13  ? 364 ILE A O   1 
ATOM   2758 C  CB  . ILE A 1 365 ? 87.426  32.398  10.562  1.00 31.05  ? 364 ILE A CB  1 
ATOM   2759 C  CG1 . ILE A 1 365 ? 87.478  32.148  9.060   1.00 31.05  ? 364 ILE A CG1 1 
ATOM   2760 C  CG2 . ILE A 1 365 ? 88.468  33.427  10.971  1.00 32.18  ? 364 ILE A CG2 1 
ATOM   2761 C  CD1 . ILE A 1 365 ? 86.634  33.097  8.273   1.00 32.17  ? 364 ILE A CD1 1 
ATOM   2762 N  N   . LEU A 1 366 ? 86.912  31.633  13.591  1.00 34.72  ? 365 LEU A N   1 
ATOM   2763 C  CA  . LEU A 1 366 ? 87.143  31.944  14.997  1.00 36.88  ? 365 LEU A CA  1 
ATOM   2764 C  C   . LEU A 1 366 ? 87.660  30.726  15.750  1.00 36.11  ? 365 LEU A C   1 
ATOM   2765 O  O   . LEU A 1 366 ? 88.534  30.850  16.614  1.00 39.43  ? 365 LEU A O   1 
ATOM   2766 C  CB  . LEU A 1 366 ? 85.859  32.472  15.633  1.00 36.27  ? 365 LEU A CB  1 
ATOM   2767 C  CG  . LEU A 1 366 ? 85.312  33.764  15.017  1.00 45.73  ? 365 LEU A CG  1 
ATOM   2768 C  CD1 . LEU A 1 366 ? 84.073  34.248  15.761  1.00 49.51  ? 365 LEU A CD1 1 
ATOM   2769 C  CD2 . LEU A 1 366 ? 86.373  34.849  14.978  1.00 39.24  ? 365 LEU A CD2 1 
ATOM   2770 N  N   . ALA A 1 367 ? 87.142  29.540  15.430  1.00 33.34  ? 366 ALA A N   1 
ATOM   2771 C  CA  . ALA A 1 367 ? 87.640  28.325  16.068  1.00 39.24  ? 366 ALA A CA  1 
ATOM   2772 C  C   . ALA A 1 367 ? 89.101  28.077  15.717  1.00 40.22  ? 366 ALA A C   1 
ATOM   2773 O  O   . ALA A 1 367 ? 89.896  27.680  16.576  1.00 43.17  ? 366 ALA A O   1 
ATOM   2774 C  CB  . ALA A 1 367 ? 86.784  27.127  15.657  1.00 35.41  ? 366 ALA A CB  1 
ATOM   2775 N  N   . GLU A 1 368 ? 89.475  28.317  14.458  1.00 40.54  ? 367 GLU A N   1 
ATOM   2776 C  CA  . GLU A 1 368 ? 90.840  28.047  14.022  1.00 36.36  ? 367 GLU A CA  1 
ATOM   2777 C  C   . GLU A 1 368 ? 91.826  29.041  14.626  1.00 40.49  ? 367 GLU A C   1 
ATOM   2778 O  O   . GLU A 1 368 ? 92.888  28.645  15.121  1.00 37.43  ? 367 GLU A O   1 
ATOM   2779 C  CB  . GLU A 1 368 ? 90.905  28.070  12.497  1.00 37.34  ? 367 GLU A CB  1 
ATOM   2780 C  CG  . GLU A 1 368 ? 91.873  27.071  11.894  1.00 45.75  ? 367 GLU A CG  1 
ATOM   2781 C  CD  . GLU A 1 368 ? 91.285  25.678  11.717  1.00 48.25  ? 367 GLU A CD  1 
ATOM   2782 O  OE1 . GLU A 1 368 ? 90.194  25.406  12.257  1.00 59.24  ? 367 GLU A OE1 1 
ATOM   2783 O  OE2 . GLU A 1 368 ? 91.922  24.851  11.033  1.00 53.60  ? 367 GLU A OE2 1 
ATOM   2784 N  N   . VAL A 1 369 ? 91.488  30.333  14.601  1.00 38.80  ? 368 VAL A N   1 
ATOM   2785 C  CA  . VAL A 1 369 ? 92.363  31.344  15.189  1.00 38.21  ? 368 VAL A CA  1 
ATOM   2786 C  C   . VAL A 1 369 ? 92.499  31.130  16.695  1.00 37.41  ? 368 VAL A C   1 
ATOM   2787 O  O   . VAL A 1 369 ? 93.581  31.321  17.266  1.00 36.58  ? 368 VAL A O   1 
ATOM   2788 C  CB  . VAL A 1 369 ? 91.843  32.754  14.854  1.00 38.10  ? 368 VAL A CB  1 
ATOM   2789 C  CG1 . VAL A 1 369 ? 92.639  33.815  15.598  1.00 40.05  ? 368 VAL A CG1 1 
ATOM   2790 C  CG2 . VAL A 1 369 ? 91.910  33.000  13.351  1.00 38.70  ? 368 VAL A CG2 1 
ATOM   2791 N  N   . SER A 1 370 ? 91.416  30.719  17.360  1.00 33.12  ? 369 SER A N   1 
ATOM   2792 C  CA  . SER A 1 370 ? 91.486  30.428  18.792  1.00 34.69  ? 369 SER A CA  1 
ATOM   2793 C  C   . SER A 1 370 ? 92.477  29.311  19.072  1.00 37.56  ? 369 SER A C   1 
ATOM   2794 O  O   . SER A 1 370 ? 93.296  29.408  19.993  1.00 39.27  ? 369 SER A O   1 
ATOM   2795 C  CB  . SER A 1 370 ? 90.106  30.047  19.336  1.00 33.92  ? 369 SER A CB  1 
ATOM   2796 O  OG  . SER A 1 370 ? 89.228  31.152  19.359  1.00 38.30  ? 369 SER A OG  1 
ATOM   2797 N  N   . GLN A 1 371 ? 92.409  28.230  18.291  1.00 37.30  ? 370 GLN A N   1 
ATOM   2798 C  CA  . GLN A 1 371 ? 93.325  27.117  18.499  1.00 39.05  ? 370 GLN A CA  1 
ATOM   2799 C  C   . GLN A 1 371 ? 94.761  27.530  18.224  1.00 38.75  ? 370 GLN A C   1 
ATOM   2800 O  O   . GLN A 1 371 ? 95.676  27.155  18.966  1.00 40.78  ? 370 GLN A O   1 
ATOM   2801 C  CB  . GLN A 1 371 ? 92.930  25.942  17.612  1.00 42.69  ? 370 GLN A CB  1 
ATOM   2802 C  CG  . GLN A 1 371 ? 91.788  25.121  18.171  1.00 41.52  ? 370 GLN A CG  1 
ATOM   2803 C  CD  . GLN A 1 371 ? 91.227  24.160  17.149  1.00 44.50  ? 370 GLN A CD  1 
ATOM   2804 O  OE1 . GLN A 1 371 ? 91.782  23.081  16.926  1.00 46.61  ? 370 GLN A OE1 1 
ATOM   2805 N  NE2 . GLN A 1 371 ? 90.120  24.547  16.517  1.00 38.64  ? 370 GLN A NE2 1 
ATOM   2806 N  N   . PHE A 1 372 ? 94.975  28.308  17.162  1.00 37.87  ? 371 PHE A N   1 
ATOM   2807 C  CA  . PHE A 1 372 ? 96.323  28.739  16.809  1.00 38.66  ? 371 PHE A CA  1 
ATOM   2808 C  C   . PHE A 1 372 ? 96.923  29.601  17.911  1.00 40.55  ? 371 PHE A C   1 
ATOM   2809 O  O   . PHE A 1 372 ? 98.046  29.357  18.369  1.00 38.72  ? 371 PHE A O   1 
ATOM   2810 C  CB  . PHE A 1 372 ? 96.287  29.498  15.480  1.00 41.53  ? 371 PHE A CB  1 
ATOM   2811 C  CG  . PHE A 1 372 ? 97.566  30.223  15.151  1.00 42.26  ? 371 PHE A CG  1 
ATOM   2812 C  CD1 . PHE A 1 372 ? 98.564  29.597  14.424  1.00 47.31  ? 371 PHE A CD1 1 
ATOM   2813 C  CD2 . PHE A 1 372 ? 97.765  31.534  15.559  1.00 38.60  ? 371 PHE A CD2 1 
ATOM   2814 C  CE1 . PHE A 1 372 ? 99.738  30.260  14.115  1.00 46.71  ? 371 PHE A CE1 1 
ATOM   2815 C  CE2 . PHE A 1 372 ? 98.933  32.201  15.254  1.00 44.37  ? 371 PHE A CE2 1 
ATOM   2816 C  CZ  . PHE A 1 372 ? 99.922  31.565  14.531  1.00 48.34  ? 371 PHE A CZ  1 
ATOM   2817 N  N   . THR A 1 373 ? 96.181  30.620  18.347  1.00 38.94  ? 372 THR A N   1 
ATOM   2818 C  CA  . THR A 1 373 ? 96.709  31.557  19.332  1.00 39.46  ? 372 THR A CA  1 
ATOM   2819 C  C   . THR A 1 373 ? 96.966  30.870  20.665  1.00 38.68  ? 372 THR A C   1 
ATOM   2820 O  O   . THR A 1 373 ? 98.009  31.095  21.288  1.00 40.82  ? 372 THR A O   1 
ATOM   2821 C  CB  . THR A 1 373 ? 95.747  32.731  19.512  1.00 36.66  ? 372 THR A CB  1 
ATOM   2822 O  OG1 . THR A 1 373 ? 95.373  33.246  18.227  1.00 38.10  ? 372 THR A OG1 1 
ATOM   2823 C  CG2 . THR A 1 373 ? 96.408  33.836  20.317  1.00 41.23  ? 372 THR A CG2 1 
ATOM   2824 N  N   . LEU A 1 374 ? 96.030  30.028  21.114  1.00 39.76  ? 373 LEU A N   1 
ATOM   2825 C  CA  . LEU A 1 374 ? 96.236  29.291  22.358  1.00 39.88  ? 373 LEU A CA  1 
ATOM   2826 C  C   . LEU A 1 374 ? 97.462  28.395  22.264  1.00 38.85  ? 373 LEU A C   1 
ATOM   2827 O  O   . LEU A 1 374 ? 98.303  28.387  23.171  1.00 36.96  ? 373 LEU A O   1 
ATOM   2828 C  CB  . LEU A 1 374 ? 94.992  28.469  22.702  1.00 31.36  ? 373 LEU A CB  1 
ATOM   2829 C  CG  . LEU A 1 374 ? 93.832  29.305  23.256  1.00 39.71  ? 373 LEU A CG  1 
ATOM   2830 C  CD1 . LEU A 1 374 ? 92.553  28.487  23.396  1.00 29.63  ? 373 LEU A CD1 1 
ATOM   2831 C  CD2 . LEU A 1 374 ? 94.226  29.943  24.585  1.00 34.29  ? 373 LEU A CD2 1 
ATOM   2832 N  N   . LEU A 1 375 ? 97.587  27.644  21.166  1.00 40.78  ? 374 LEU A N   1 
ATOM   2833 C  CA  . LEU A 1 375 ? 98.771  26.814  20.964  1.00 39.97  ? 374 LEU A CA  1 
ATOM   2834 C  C   . LEU A 1 375 ? 100.040 27.651  21.020  1.00 40.02  ? 374 LEU A C   1 
ATOM   2835 O  O   . LEU A 1 375 ? 101.049 27.229  21.595  1.00 42.18  ? 374 LEU A O   1 
ATOM   2836 C  CB  . LEU A 1 375 ? 98.669  26.070  19.630  1.00 38.03  ? 374 LEU A CB  1 
ATOM   2837 C  CG  . LEU A 1 375 ? 99.471  24.780  19.453  1.00 39.08  ? 374 LEU A CG  1 
ATOM   2838 C  CD1 . LEU A 1 375 ? 99.219  23.813  20.595  1.00 44.48  ? 374 LEU A CD1 1 
ATOM   2839 C  CD2 . LEU A 1 375 ? 99.119  24.129  18.125  1.00 49.15  ? 374 LEU A CD2 1 
ATOM   2840 N  N   . MET A 1 376 ? 99.993  28.862  20.467  1.00 39.79  ? 375 MET A N   1 
ATOM   2841 C  CA  . MET A 1 376 ? 101.182 29.703  20.435  1.00 38.96  ? 375 MET A CA  1 
ATOM   2842 C  C   . MET A 1 376 ? 101.516 30.275  21.800  1.00 42.70  ? 375 MET A C   1 
ATOM   2843 O  O   . MET A 1 376 ? 102.694 30.383  22.160  1.00 45.50  ? 375 MET A O   1 
ATOM   2844 C  CB  . MET A 1 376 ? 101.000 30.821  19.421  1.00 44.68  ? 375 MET A CB  1 
ATOM   2845 C  CG  . MET A 1 376 ? 101.160 30.276  18.064  1.00 49.25  ? 375 MET A CG  1 
ATOM   2846 S  SD  . MET A 1 376 ? 102.548 29.158  18.270  1.00 67.31  ? 375 MET A SD  1 
ATOM   2847 C  CE  . MET A 1 376 ? 102.697 28.576  16.626  1.00 58.67  ? 375 MET A CE  1 
ATOM   2848 N  N   . VAL A 1 377 ? 100.503 30.691  22.555  1.00 39.28  ? 376 VAL A N   1 
ATOM   2849 C  CA  . VAL A 1 377 ? 100.763 31.219  23.889  1.00 43.35  ? 376 VAL A CA  1 
ATOM   2850 C  C   . VAL A 1 377 ? 101.395 30.145  24.759  1.00 39.09  ? 376 VAL A C   1 
ATOM   2851 O  O   . VAL A 1 377 ? 102.387 30.385  25.458  1.00 40.25  ? 376 VAL A O   1 
ATOM   2852 C  CB  . VAL A 1 377 ? 99.464  31.765  24.508  1.00 42.67  ? 376 VAL A CB  1 
ATOM   2853 C  CG1 . VAL A 1 377 ? 99.679  32.107  25.970  1.00 40.23  ? 376 VAL A CG1 1 
ATOM   2854 C  CG2 . VAL A 1 377 ? 98.994  32.987  23.738  1.00 42.99  ? 376 VAL A CG2 1 
ATOM   2855 N  N   . PHE A 1 378 ? 100.861 28.930  24.693  1.00 41.37  ? 377 PHE A N   1 
ATOM   2856 C  CA  . PHE A 1 378 ? 101.344 27.871  25.564  1.00 41.49  ? 377 PHE A CA  1 
ATOM   2857 C  C   . PHE A 1 378 ? 102.696 27.344  25.101  1.00 48.26  ? 377 PHE A C   1 
ATOM   2858 O  O   . PHE A 1 378 ? 103.580 27.086  25.928  1.00 43.29  ? 377 PHE A O   1 
ATOM   2859 C  CB  . PHE A 1 378 ? 100.299 26.760  25.641  1.00 40.01  ? 377 PHE A CB  1 
ATOM   2860 C  CG  . PHE A 1 378 ? 99.174  27.061  26.603  1.00 42.61  ? 377 PHE A CG  1 
ATOM   2861 C  CD1 . PHE A 1 378 ? 99.447  27.432  27.911  1.00 35.15  ? 377 PHE A CD1 1 
ATOM   2862 C  CD2 . PHE A 1 378 ? 97.849  26.988  26.195  1.00 41.02  ? 377 PHE A CD2 1 
ATOM   2863 C  CE1 . PHE A 1 378 ? 98.424  27.706  28.797  1.00 35.82  ? 377 PHE A CE1 1 
ATOM   2864 C  CE2 . PHE A 1 378 ? 96.824  27.262  27.077  1.00 34.09  ? 377 PHE A CE2 1 
ATOM   2865 C  CZ  . PHE A 1 378 ? 97.113  27.623  28.379  1.00 39.02  ? 377 PHE A CZ  1 
ATOM   2866 N  N   . ALA A 1 379 ? 102.886 27.203  23.786  1.00 46.09  ? 378 ALA A N   1 
ATOM   2867 C  CA  . ALA A 1 379 ? 104.168 26.724  23.276  1.00 47.12  ? 378 ALA A CA  1 
ATOM   2868 C  C   . ALA A 1 379 ? 105.288 27.709  23.587  1.00 44.15  ? 378 ALA A C   1 
ATOM   2869 O  O   . ALA A 1 379 ? 106.361 27.315  24.058  1.00 45.04  ? 378 ALA A O   1 
ATOM   2870 C  CB  . ALA A 1 379 ? 104.074 26.465  21.772  1.00 43.75  ? 378 ALA A CB  1 
ATOM   2871 N  N   . HIS A 1 380 ? 105.056 28.999  23.334  1.00 44.84  ? 379 HIS A N   1 
ATOM   2872 C  CA  . HIS A 1 380 ? 106.060 30.020  23.624  1.00 46.11  ? 379 HIS A CA  1 
ATOM   2873 C  C   . HIS A 1 380 ? 106.423 30.056  25.103  1.00 44.98  ? 379 HIS A C   1 
ATOM   2874 O  O   . HIS A 1 380 ? 107.532 30.469  25.455  1.00 53.26  ? 379 HIS A O   1 
ATOM   2875 C  CB  . HIS A 1 380 ? 105.549 31.384  23.144  1.00 51.29  ? 379 HIS A CB  1 
ATOM   2876 C  CG  . HIS A 1 380 ? 106.260 32.559  23.740  1.00 49.33  ? 379 HIS A CG  1 
ATOM   2877 N  ND1 . HIS A 1 380 ? 107.433 33.062  23.220  1.00 56.20  ? 379 HIS A ND1 1 
ATOM   2878 C  CD2 . HIS A 1 380 ? 105.952 33.344  24.799  1.00 52.29  ? 379 HIS A CD2 1 
ATOM   2879 C  CE1 . HIS A 1 380 ? 107.823 34.100  23.938  1.00 57.04  ? 379 HIS A CE1 1 
ATOM   2880 N  NE2 . HIS A 1 380 ? 106.941 34.292  24.904  1.00 58.56  ? 379 HIS A NE2 1 
ATOM   2881 N  N   . TRP A 1 381 ? 105.523 29.600  25.971  1.00 49.13  ? 380 TRP A N   1 
ATOM   2882 C  CA  . TRP A 1 381 ? 105.792 29.551  27.402  1.00 43.73  ? 380 TRP A CA  1 
ATOM   2883 C  C   . TRP A 1 381 ? 106.524 28.268  27.794  1.00 50.04  ? 380 TRP A C   1 
ATOM   2884 O  O   . TRP A 1 381 ? 107.553 28.317  28.477  1.00 48.85  ? 380 TRP A O   1 
ATOM   2885 C  CB  . TRP A 1 381 ? 104.474 29.680  28.173  1.00 48.80  ? 380 TRP A CB  1 
ATOM   2886 C  CG  . TRP A 1 381 ? 104.591 29.406  29.639  1.00 43.81  ? 380 TRP A CG  1 
ATOM   2887 C  CD1 . TRP A 1 381 ? 105.646 29.714  30.448  1.00 48.52  ? 380 TRP A CD1 1 
ATOM   2888 C  CD2 . TRP A 1 381 ? 103.618 28.766  30.475  1.00 44.95  ? 380 TRP A CD2 1 
ATOM   2889 N  NE1 . TRP A 1 381 ? 105.391 29.304  31.734  1.00 46.57  ? 380 TRP A NE1 1 
ATOM   2890 C  CE2 . TRP A 1 381 ? 104.152 28.721  31.778  1.00 49.86  ? 380 TRP A CE2 1 
ATOM   2891 C  CE3 . TRP A 1 381 ? 102.348 28.227  30.249  1.00 48.84  ? 380 TRP A CE3 1 
ATOM   2892 C  CZ2 . TRP A 1 381 ? 103.462 28.158  32.850  1.00 49.35  ? 380 TRP A CZ2 1 
ATOM   2893 C  CZ3 . TRP A 1 381 ? 101.664 27.669  31.315  1.00 43.77  ? 380 TRP A CZ3 1 
ATOM   2894 C  CH2 . TRP A 1 381 ? 102.222 27.639  32.598  1.00 45.65  ? 380 TRP A CH2 1 
ATOM   2895 N  N   . LEU A 1 382 ? 106.018 27.112  27.360  1.00 45.41  ? 381 LEU A N   1 
ATOM   2896 C  CA  . LEU A 1 382 ? 106.460 25.835  27.911  1.00 43.82  ? 381 LEU A CA  1 
ATOM   2897 C  C   . LEU A 1 382 ? 107.585 25.172  27.127  1.00 51.56  ? 381 LEU A C   1 
ATOM   2898 O  O   . LEU A 1 382 ? 108.368 24.415  27.713  1.00 51.21  ? 381 LEU A O   1 
ATOM   2899 C  CB  . LEU A 1 382 ? 105.279 24.866  27.995  1.00 44.95  ? 381 LEU A CB  1 
ATOM   2900 C  CG  . LEU A 1 382 ? 104.216 25.215  29.039  1.00 52.99  ? 381 LEU A CG  1 
ATOM   2901 C  CD1 . LEU A 1 382 ? 102.823 24.917  28.501  1.00 40.28  ? 381 LEU A CD1 1 
ATOM   2902 C  CD2 . LEU A 1 382 ? 104.469 24.472  30.346  1.00 49.88  ? 381 LEU A CD2 1 
ATOM   2903 N  N   . ILE A 1 383 ? 107.680 25.411  25.823  1.00 50.79  ? 382 ILE A N   1 
ATOM   2904 C  CA  . ILE A 1 383 ? 108.697 24.755  24.999  1.00 46.97  ? 382 ILE A CA  1 
ATOM   2905 C  C   . ILE A 1 383 ? 110.102 25.218  25.379  1.00 51.91  ? 382 ILE A C   1 
ATOM   2906 O  O   . ILE A 1 383 ? 110.987 24.366  25.556  1.00 52.75  ? 382 ILE A O   1 
ATOM   2907 C  CB  . ILE A 1 383 ? 108.435 24.980  23.501  1.00 49.30  ? 382 ILE A CB  1 
ATOM   2908 C  CG1 . ILE A 1 383 ? 107.258 24.121  23.028  1.00 51.68  ? 382 ILE A CG1 1 
ATOM   2909 C  CG2 . ILE A 1 383 ? 109.691 24.677  22.693  1.00 50.20  ? 382 ILE A CG2 1 
ATOM   2910 C  CD1 . ILE A 1 383 ? 107.050 24.124  21.525  1.00 45.32  ? 382 ILE A CD1 1 
ATOM   2911 N  N   . PRO A 1 384 ? 110.380 26.524  25.508  1.00 54.72  ? 383 PRO A N   1 
ATOM   2912 C  CA  . PRO A 1 384 ? 111.758 26.933  25.833  1.00 52.64  ? 383 PRO A CA  1 
ATOM   2913 C  C   . PRO A 1 384 ? 112.248 26.401  27.162  1.00 55.14  ? 383 PRO A C   1 
ATOM   2914 O  O   . PRO A 1 384 ? 113.464 26.343  27.380  1.00 61.99  ? 383 PRO A O   1 
ATOM   2915 C  CB  . PRO A 1 384 ? 111.681 28.466  25.844  1.00 58.01  ? 383 PRO A CB  1 
ATOM   2916 C  CG  . PRO A 1 384 ? 110.502 28.790  25.012  1.00 53.04  ? 383 PRO A CG  1 
ATOM   2917 C  CD  . PRO A 1 384 ? 109.519 27.703  25.295  1.00 49.78  ? 383 PRO A CD  1 
ATOM   2918 N  N   . ALA A 1 385 ? 111.347 26.001  28.054  1.00 50.97  ? 384 ALA A N   1 
ATOM   2919 C  CA  . ALA A 1 385 ? 111.744 25.489  29.356  1.00 51.21  ? 384 ALA A CA  1 
ATOM   2920 C  C   . ALA A 1 385 ? 111.765 23.969  29.435  1.00 55.15  ? 384 ALA A C   1 
ATOM   2921 O  O   . ALA A 1 385 ? 112.598 23.416  30.158  1.00 63.39  ? 384 ALA A O   1 
ATOM   2922 C  CB  . ALA A 1 385 ? 110.811 26.034  30.442  1.00 53.98  ? 384 ALA A CB  1 
ATOM   2923 N  N   . HIS A 1 386 ? 110.888 23.272  28.706  1.00 53.58  ? 385 HIS A N   1 
ATOM   2924 C  CA  . HIS A 1 386 ? 110.742 21.831  28.880  1.00 50.06  ? 385 HIS A CA  1 
ATOM   2925 C  C   . HIS A 1 386 ? 110.823 21.042  27.579  1.00 51.90  ? 385 HIS A C   1 
ATOM   2926 O  O   . HIS A 1 386 ? 110.522 19.843  27.583  1.00 52.58  ? 385 HIS A O   1 
ATOM   2927 C  CB  . HIS A 1 386 ? 109.425 21.519  29.595  1.00 49.33  ? 385 HIS A CB  1 
ATOM   2928 C  CG  . HIS A 1 386 ? 109.371 22.041  30.995  1.00 58.28  ? 385 HIS A CG  1 
ATOM   2929 N  ND1 . HIS A 1 386 ? 108.214 22.524  31.568  1.00 56.74  ? 385 HIS A ND1 1 
ATOM   2930 C  CD2 . HIS A 1 386 ? 110.337 22.166  31.934  1.00 55.05  ? 385 HIS A CD2 1 
ATOM   2931 C  CE1 . HIS A 1 386 ? 108.470 22.919  32.802  1.00 52.62  ? 385 HIS A CE1 1 
ATOM   2932 N  NE2 . HIS A 1 386 ? 109.750 22.711  33.050  1.00 55.26  ? 385 HIS A NE2 1 
ATOM   2933 N  N   . GLY A 1 387 ? 111.214 21.671  26.474  1.00 50.84  ? 386 GLY A N   1 
ATOM   2934 C  CA  . GLY A 1 387 ? 111.476 20.921  25.259  1.00 49.87  ? 386 GLY A CA  1 
ATOM   2935 C  C   . GLY A 1 387 ? 110.252 20.188  24.754  1.00 51.15  ? 386 GLY A C   1 
ATOM   2936 O  O   . GLY A 1 387 ? 109.130 20.706  24.773  1.00 52.27  ? 386 GLY A O   1 
ATOM   2937 N  N   . ALA A 1 388 ? 110.470 18.951  24.296  1.00 52.49  ? 387 ALA A N   1 
ATOM   2938 C  CA  . ALA A 1 388 ? 109.385 18.176  23.706  1.00 47.84  ? 387 ALA A CA  1 
ATOM   2939 C  C   . ALA A 1 388 ? 108.294 17.892  24.726  1.00 51.79  ? 387 ALA A C   1 
ATOM   2940 O  O   . ALA A 1 388 ? 107.111 17.822  24.372  1.00 45.40  ? 387 ALA A O   1 
ATOM   2941 C  CB  . ALA A 1 388 ? 109.920 16.871  23.119  1.00 48.51  ? 387 ALA A CB  1 
ATOM   2942 N  N   . LEU A 1 389 ? 108.670 17.724  25.996  1.00 46.99  ? 388 LEU A N   1 
ATOM   2943 C  CA  . LEU A 1 389 ? 107.662 17.563  27.035  1.00 45.56  ? 388 LEU A CA  1 
ATOM   2944 C  C   . LEU A 1 389 ? 106.826 18.829  27.174  1.00 43.36  ? 388 LEU A C   1 
ATOM   2945 O  O   . LEU A 1 389 ? 105.604 18.760  27.346  1.00 49.87  ? 388 LEU A O   1 
ATOM   2946 C  CB  . LEU A 1 389 ? 108.327 17.196  28.362  1.00 51.32  ? 388 LEU A CB  1 
ATOM   2947 C  CG  . LEU A 1 389 ? 107.424 17.191  29.598  1.00 55.37  ? 388 LEU A CG  1 
ATOM   2948 C  CD1 . LEU A 1 389 ? 106.433 16.032  29.548  1.00 52.14  ? 388 LEU A CD1 1 
ATOM   2949 C  CD2 . LEU A 1 389 ? 108.252 17.125  30.865  1.00 57.85  ? 388 LEU A CD2 1 
ATOM   2950 N  N   . GLY A 1 390 ? 107.467 19.995  27.079  1.00 45.76  ? 389 GLY A N   1 
ATOM   2951 C  CA  . GLY A 1 390 ? 106.716 21.240  27.086  1.00 48.60  ? 389 GLY A CA  1 
ATOM   2952 C  C   . GLY A 1 390 ? 105.785 21.370  25.893  1.00 48.87  ? 389 GLY A C   1 
ATOM   2953 O  O   . GLY A 1 390 ? 104.670 21.883  26.019  1.00 43.30  ? 389 GLY A O   1 
ATOM   2954 N  N   . ALA A 1 391 ? 106.226 20.907  24.721  1.00 44.54  ? 390 ALA A N   1 
ATOM   2955 C  CA  . ALA A 1 391 ? 105.360 20.941  23.547  1.00 46.03  ? 390 ALA A CA  1 
ATOM   2956 C  C   . ALA A 1 391 ? 104.114 20.090  23.761  1.00 43.54  ? 390 ALA A C   1 
ATOM   2957 O  O   . ALA A 1 391 ? 103.013 20.472  23.345  1.00 44.73  ? 390 ALA A O   1 
ATOM   2958 C  CB  . ALA A 1 391 ? 106.130 20.479  22.310  1.00 41.70  ? 390 ALA A CB  1 
ATOM   2959 N  N   . ALA A 1 392 ? 104.266 18.936  24.422  1.00 44.11  ? 391 ALA A N   1 
ATOM   2960 C  CA  . ALA A 1 392 ? 103.108 18.109  24.747  1.00 42.87  ? 391 ALA A CA  1 
ATOM   2961 C  C   . ALA A 1 392 ? 102.240 18.771  25.809  1.00 42.62  ? 391 ALA A C   1 
ATOM   2962 O  O   . ALA A 1 392 ? 101.007 18.709  25.740  1.00 41.97  ? 391 ALA A O   1 
ATOM   2963 C  CB  . ALA A 1 392 ? 103.558 16.725  25.212  1.00 42.13  ? 391 ALA A CB  1 
ATOM   2964 N  N   . GLN A 1 393 ? 102.869 19.402  26.802  1.00 41.50  ? 392 GLN A N   1 
ATOM   2965 C  CA  . GLN A 1 393 ? 102.110 20.140  27.805  1.00 41.16  ? 392 GLN A CA  1 
ATOM   2966 C  C   . GLN A 1 393 ? 101.370 21.315  27.181  1.00 40.81  ? 392 GLN A C   1 
ATOM   2967 O  O   . GLN A 1 393 ? 100.215 21.586  27.527  1.00 42.47  ? 392 GLN A O   1 
ATOM   2968 C  CB  . GLN A 1 393 ? 103.045 20.625  28.906  1.00 49.47  ? 392 GLN A CB  1 
ATOM   2969 C  CG  . GLN A 1 393 ? 103.657 19.519  29.735  1.00 45.17  ? 392 GLN A CG  1 
ATOM   2970 C  CD  . GLN A 1 393 ? 104.840 20.010  30.538  1.00 48.90  ? 392 GLN A CD  1 
ATOM   2971 O  OE1 . GLN A 1 393 ? 105.492 20.982  30.164  1.00 52.65  ? 392 GLN A OE1 1 
ATOM   2972 N  NE2 . GLN A 1 393 ? 105.114 19.350  31.654  1.00 47.96  ? 392 GLN A NE2 1 
ATOM   2973 N  N   . ALA A 1 394 ? 102.024 22.029  26.261  1.00 39.88  ? 393 ALA A N   1 
ATOM   2974 C  CA  . ALA A 1 394 ? 101.378 23.153  25.592  1.00 39.00  ? 393 ALA A CA  1 
ATOM   2975 C  C   . ALA A 1 394 ? 100.166 22.693  24.800  1.00 41.15  ? 393 ALA A C   1 
ATOM   2976 O  O   . ALA A 1 394 ? 99.115  23.343  24.824  1.00 37.20  ? 393 ALA A O   1 
ATOM   2977 C  CB  . ALA A 1 394 ? 102.375 23.861  24.674  1.00 39.54  ? 393 ALA A CB  1 
ATOM   2978 N  N   . TYR A 1 395 ? 100.303 21.574  24.087  1.00 40.77  ? 394 TYR A N   1 
ATOM   2979 C  CA  . TYR A 1 395 ? 99.181  21.002  23.355  1.00 36.85  ? 394 TYR A CA  1 
ATOM   2980 C  C   . TYR A 1 395 ? 98.033  20.648  24.293  1.00 36.88  ? 394 TYR A C   1 
ATOM   2981 O  O   . TYR A 1 395 ? 96.867  20.932  23.994  1.00 38.76  ? 394 TYR A O   1 
ATOM   2982 C  CB  . TYR A 1 395 ? 99.665  19.774  22.587  1.00 41.88  ? 394 TYR A CB  1 
ATOM   2983 C  CG  . TYR A 1 395 ? 98.582  18.952  21.941  1.00 36.53  ? 394 TYR A CG  1 
ATOM   2984 C  CD1 . TYR A 1 395 ? 98.104  19.273  20.682  1.00 42.11  ? 394 TYR A CD1 1 
ATOM   2985 C  CD2 . TYR A 1 395 ? 98.051  17.841  22.582  1.00 41.00  ? 394 TYR A CD2 1 
ATOM   2986 C  CE1 . TYR A 1 395 ? 97.117  18.519  20.078  1.00 42.67  ? 394 TYR A CE1 1 
ATOM   2987 C  CE2 . TYR A 1 395 ? 97.063  17.079  21.986  1.00 41.56  ? 394 TYR A CE2 1 
ATOM   2988 C  CZ  . TYR A 1 395 ? 96.601  17.426  20.734  1.00 40.89  ? 394 TYR A CZ  1 
ATOM   2989 O  OH  . TYR A 1 395 ? 95.623  16.677  20.131  1.00 48.03  ? 394 TYR A OH  1 
ATOM   2990 N  N   . MET A 1 396 ? 98.342  20.038  25.441  1.00 37.40  ? 395 MET A N   1 
ATOM   2991 C  CA  . MET A 1 396 ? 97.293  19.666  26.388  1.00 38.08  ? 395 MET A CA  1 
ATOM   2992 C  C   . MET A 1 396 ? 96.630  20.896  26.987  1.00 39.54  ? 395 MET A C   1 
ATOM   2993 O  O   . MET A 1 396 ? 95.396  20.990  27.030  1.00 36.89  ? 395 MET A O   1 
ATOM   2994 C  CB  . MET A 1 396 ? 97.858  18.790  27.504  1.00 34.47  ? 395 MET A CB  1 
ATOM   2995 C  CG  . MET A 1 396 ? 96.880  18.613  28.654  1.00 39.31  ? 395 MET A CG  1 
ATOM   2996 S  SD  . MET A 1 396 ? 97.600  17.843  30.115  1.00 51.11  ? 395 MET A SD  1 
ATOM   2997 C  CE  . MET A 1 396 ? 97.724  19.251  31.215  1.00 44.88  ? 395 MET A CE  1 
ATOM   2998 N  N   . ALA A 1 397 ? 97.432  21.838  27.487  1.00 35.54  ? 396 ALA A N   1 
ATOM   2999 C  CA  . ALA A 1 397 ? 96.857  23.056  28.040  1.00 38.51  ? 396 ALA A CA  1 
ATOM   3000 C  C   . ALA A 1 397 ? 96.024  23.785  26.995  1.00 41.81  ? 396 ALA A C   1 
ATOM   3001 O  O   . ALA A 1 397 ? 94.959  24.333  27.310  1.00 42.20  ? 396 ALA A O   1 
ATOM   3002 C  CB  . ALA A 1 397 ? 97.960  23.961  28.583  1.00 39.08  ? 396 ALA A CB  1 
ATOM   3003 N  N   . THR A 1 398 ? 96.479  23.774  25.739  1.00 37.42  ? 397 THR A N   1 
ATOM   3004 C  CA  . THR A 1 398 ? 95.748  24.452  24.674  1.00 38.42  ? 397 THR A CA  1 
ATOM   3005 C  C   . THR A 1 398 ? 94.324  23.926  24.558  1.00 41.85  ? 397 THR A C   1 
ATOM   3006 O  O   . THR A 1 398 ? 93.372  24.708  24.449  1.00 39.05  ? 397 THR A O   1 
ATOM   3007 C  CB  . THR A 1 398 ? 96.481  24.289  23.340  1.00 39.26  ? 397 THR A CB  1 
ATOM   3008 O  OG1 . THR A 1 398 ? 97.693  25.055  23.359  1.00 37.56  ? 397 THR A OG1 1 
ATOM   3009 C  CG2 . THR A 1 398 ? 95.605  24.759  22.183  1.00 31.88  ? 397 THR A CG2 1 
ATOM   3010 N  N   . TYR A 1 399 ? 94.150  22.608  24.598  1.00 37.29  ? 398 TYR A N   1 
ATOM   3011 C  CA  . TYR A 1 399 ? 92.823  22.065  24.350  1.00 41.28  ? 398 TYR A CA  1 
ATOM   3012 C  C   . TYR A 1 399 ? 91.986  21.921  25.618  1.00 38.94  ? 398 TYR A C   1 
ATOM   3013 O  O   . TYR A 1 399 ? 90.760  21.797  25.517  1.00 40.07  ? 398 TYR A O   1 
ATOM   3014 C  CB  . TYR A 1 399 ? 92.951  20.746  23.578  1.00 41.18  ? 398 TYR A CB  1 
ATOM   3015 C  CG  . TYR A 1 399 ? 93.255  21.034  22.115  1.00 38.11  ? 398 TYR A CG  1 
ATOM   3016 C  CD1 . TYR A 1 399 ? 92.239  21.369  21.229  1.00 40.00  ? 398 TYR A CD1 1 
ATOM   3017 C  CD2 . TYR A 1 399 ? 94.562  21.049  21.640  1.00 37.17  ? 398 TYR A CD2 1 
ATOM   3018 C  CE1 . TYR A 1 399 ? 92.502  21.666  19.904  1.00 38.26  ? 398 TYR A CE1 1 
ATOM   3019 C  CE2 . TYR A 1 399 ? 94.836  21.345  20.307  1.00 40.41  ? 398 TYR A CE2 1 
ATOM   3020 C  CZ  . TYR A 1 399 ? 93.799  21.655  19.447  1.00 41.37  ? 398 TYR A CZ  1 
ATOM   3021 O  OH  . TYR A 1 399 ? 94.050  21.957  18.127  1.00 39.69  ? 398 TYR A OH  1 
ATOM   3022 N  N   . ILE A 1 400 ? 92.599  21.987  26.803  1.00 41.42  ? 399 ILE A N   1 
ATOM   3023 C  CA  . ILE A 1 400 ? 91.825  22.234  28.018  1.00 41.53  ? 399 ILE A CA  1 
ATOM   3024 C  C   . ILE A 1 400 ? 91.104  23.573  27.909  1.00 39.12  ? 399 ILE A C   1 
ATOM   3025 O  O   . ILE A 1 400 ? 89.883  23.663  28.080  1.00 40.84  ? 399 ILE A O   1 
ATOM   3026 C  CB  . ILE A 1 400 ? 92.733  22.193  29.261  1.00 40.17  ? 399 ILE A CB  1 
ATOM   3027 C  CG1 . ILE A 1 400 ? 93.224  20.777  29.537  1.00 42.38  ? 399 ILE A CG1 1 
ATOM   3028 C  CG2 . ILE A 1 400 ? 91.997  22.731  30.477  1.00 40.42  ? 399 ILE A CG2 1 
ATOM   3029 C  CD1 . ILE A 1 400 ? 94.314  20.717  30.595  1.00 48.02  ? 399 ILE A CD1 1 
ATOM   3030 N  N   . VAL A 1 401 ? 91.856  24.635  27.609  1.00 39.33  ? 400 VAL A N   1 
ATOM   3031 C  CA  . VAL A 1 401 ? 91.262  25.961  27.481  1.00 35.75  ? 400 VAL A CA  1 
ATOM   3032 C  C   . VAL A 1 401 ? 90.321  26.015  26.286  1.00 37.69  ? 400 VAL A C   1 
ATOM   3033 O  O   . VAL A 1 401 ? 89.255  26.637  26.348  1.00 38.49  ? 400 VAL A O   1 
ATOM   3034 C  CB  . VAL A 1 401 ? 92.364  27.033  27.380  1.00 36.66  ? 400 VAL A CB  1 
ATOM   3035 C  CG1 . VAL A 1 401 ? 91.759  28.398  27.076  1.00 36.93  ? 400 VAL A CG1 1 
ATOM   3036 C  CG2 . VAL A 1 401 ? 93.175  27.083  28.663  1.00 40.77  ? 400 VAL A CG2 1 
ATOM   3037 N  N   . TYR A 1 402 ? 90.691  25.368  25.180  1.00 34.15  ? 401 TYR A N   1 
ATOM   3038 C  CA  . TYR A 1 402 ? 89.878  25.492  23.976  1.00 37.67  ? 401 TYR A CA  1 
ATOM   3039 C  C   . TYR A 1 402 ? 88.533  24.796  24.139  1.00 42.17  ? 401 TYR A C   1 
ATOM   3040 O  O   . TYR A 1 402 ? 87.497  25.340  23.735  1.00 38.32  ? 401 TYR A O   1 
ATOM   3041 C  CB  . TYR A 1 402 ? 90.622  24.942  22.764  1.00 32.66  ? 401 TYR A CB  1 
ATOM   3042 C  CG  . TYR A 1 402 ? 89.793  25.009  21.508  1.00 36.52  ? 401 TYR A CG  1 
ATOM   3043 C  CD1 . TYR A 1 402 ? 89.320  26.224  21.030  1.00 35.93  ? 401 TYR A CD1 1 
ATOM   3044 C  CD2 . TYR A 1 402 ? 89.467  23.858  20.810  1.00 39.50  ? 401 TYR A CD2 1 
ATOM   3045 C  CE1 . TYR A 1 402 ? 88.557  26.288  19.881  1.00 37.71  ? 401 TYR A CE1 1 
ATOM   3046 C  CE2 . TYR A 1 402 ? 88.702  23.909  19.662  1.00 35.72  ? 401 TYR A CE2 1 
ATOM   3047 C  CZ  . TYR A 1 402 ? 88.252  25.127  19.202  1.00 38.94  ? 401 TYR A CZ  1 
ATOM   3048 O  OH  . TYR A 1 402 ? 87.488  25.177  18.066  1.00 38.92  ? 401 TYR A OH  1 
ATOM   3049 N  N   . PHE A 1 403 ? 88.525  23.597  24.733  1.00 40.70  ? 402 PHE A N   1 
ATOM   3050 C  CA  . PHE A 1 403 ? 87.263  22.908  24.986  1.00 41.24  ? 402 PHE A CA  1 
ATOM   3051 C  C   . PHE A 1 403 ? 86.372  23.720  25.913  1.00 34.25  ? 402 PHE A C   1 
ATOM   3052 O  O   . PHE A 1 403 ? 85.167  23.852  25.669  1.00 36.37  ? 402 PHE A O   1 
ATOM   3053 C  CB  . PHE A 1 403 ? 87.521  21.520  25.573  1.00 39.72  ? 402 PHE A CB  1 
ATOM   3054 C  CG  . PHE A 1 403 ? 86.267  20.764  25.921  1.00 37.54  ? 402 PHE A CG  1 
ATOM   3055 C  CD1 . PHE A 1 403 ? 85.537  20.121  24.936  1.00 35.64  ? 402 PHE A CD1 1 
ATOM   3056 C  CD2 . PHE A 1 403 ? 85.823  20.688  27.232  1.00 35.88  ? 402 PHE A CD2 1 
ATOM   3057 C  CE1 . PHE A 1 403 ? 84.386  19.422  25.247  1.00 38.83  ? 402 PHE A CE1 1 
ATOM   3058 C  CE2 . PHE A 1 403 ? 84.674  19.986  27.549  1.00 41.77  ? 402 PHE A CE2 1 
ATOM   3059 C  CZ  . PHE A 1 403 ? 83.954  19.353  26.553  1.00 38.28  ? 402 PHE A CZ  1 
ATOM   3060 N  N   . SER A 1 404 ? 86.948  24.269  26.986  1.00 37.43  ? 403 SER A N   1 
ATOM   3061 C  CA  . SER A 1 404 ? 86.187  25.145  27.871  1.00 40.71  ? 403 SER A CA  1 
ATOM   3062 C  C   . SER A 1 404 ? 85.629  26.339  27.108  1.00 37.87  ? 403 SER A C   1 
ATOM   3063 O  O   . SER A 1 404 ? 84.453  26.690  27.262  1.00 39.92  ? 403 SER A O   1 
ATOM   3064 C  CB  . SER A 1 404 ? 87.065  25.619  29.030  1.00 37.39  ? 403 SER A CB  1 
ATOM   3065 O  OG  . SER A 1 404 ? 87.392  24.550  29.894  1.00 40.27  ? 403 SER A OG  1 
ATOM   3066 N  N   . LEU A 1 405 ? 86.457  26.971  26.275  1.00 37.21  ? 404 LEU A N   1 
ATOM   3067 C  CA  . LEU A 1 405 ? 85.975  28.072  25.449  1.00 35.44  ? 404 LEU A CA  1 
ATOM   3068 C  C   . LEU A 1 405 ? 84.845  27.619  24.529  1.00 38.24  ? 404 LEU A C   1 
ATOM   3069 O  O   . LEU A 1 405 ? 83.852  28.335  24.359  1.00 36.92  ? 404 LEU A O   1 
ATOM   3070 C  CB  . LEU A 1 405 ? 87.132  28.656  24.642  1.00 35.37  ? 404 LEU A CB  1 
ATOM   3071 C  CG  . LEU A 1 405 ? 86.758  29.731  23.623  1.00 48.51  ? 404 LEU A CG  1 
ATOM   3072 C  CD1 . LEU A 1 405 ? 86.095  30.914  24.319  1.00 35.36  ? 404 LEU A CD1 1 
ATOM   3073 C  CD2 . LEU A 1 405 ? 87.995  30.180  22.866  1.00 47.53  ? 404 LEU A CD2 1 
ATOM   3074 N  N   . CYS A 1 406 ? 84.975  26.427  23.935  1.00 37.54  ? 405 CYS A N   1 
ATOM   3075 C  CA  . CYS A 1 406 ? 83.917  25.893  23.080  1.00 39.82  ? 405 CYS A CA  1 
ATOM   3076 C  C   . CYS A 1 406 ? 82.609  25.752  23.844  1.00 40.30  ? 405 CYS A C   1 
ATOM   3077 O  O   . CYS A 1 406 ? 81.538  26.097  23.329  1.00 44.08  ? 405 CYS A O   1 
ATOM   3078 C  CB  . CYS A 1 406 ? 84.327  24.531  22.511  1.00 44.35  ? 405 CYS A CB  1 
ATOM   3079 S  SG  . CYS A 1 406 ? 85.363  24.562  21.026  1.00 42.32  ? 405 CYS A SG  1 
ATOM   3080 N  N   . CYS A 1 407 ? 82.675  25.213  25.065  1.00 36.88  ? 406 CYS A N   1 
ATOM   3081 C  CA  . CYS A 1 407 ? 81.477  25.086  25.887  1.00 36.09  ? 406 CYS A CA  1 
ATOM   3082 C  C   . CYS A 1 407 ? 80.861  26.453  26.154  1.00 40.86  ? 406 CYS A C   1 
ATOM   3083 O  O   . CYS A 1 407 ? 79.659  26.659  25.948  1.00 39.44  ? 406 CYS A O   1 
ATOM   3084 C  CB  . CYS A 1 407 ? 81.816  24.388  27.205  1.00 38.26  ? 406 CYS A CB  1 
ATOM   3085 S  SG  . CYS A 1 407 ? 82.296  22.650  27.059  1.00 43.78  ? 406 CYS A SG  1 
ATOM   3086 N  N   . GLY A 1 408 ? 81.682  27.406  26.596  1.00 34.72  ? 407 GLY A N   1 
ATOM   3087 C  CA  . GLY A 1 408 ? 81.166  28.728  26.906  1.00 38.65  ? 407 GLY A CA  1 
ATOM   3088 C  C   . GLY A 1 408 ? 80.552  29.419  25.703  1.00 39.58  ? 407 GLY A C   1 
ATOM   3089 O  O   . GLY A 1 408 ? 79.490  30.038  25.807  1.00 43.43  ? 407 GLY A O   1 
ATOM   3090 N  N   . VAL A 1 409 ? 81.205  29.322  24.544  1.00 37.11  ? 408 VAL A N   1 
ATOM   3091 C  CA  . VAL A 1 409 ? 80.657  29.958  23.350  1.00 41.04  ? 408 VAL A CA  1 
ATOM   3092 C  C   . VAL A 1 409 ? 79.373  29.257  22.918  1.00 45.65  ? 408 VAL A C   1 
ATOM   3093 O  O   . VAL A 1 409 ? 78.423  29.899  22.452  1.00 39.28  ? 408 VAL A O   1 
ATOM   3094 C  CB  . VAL A 1 409 ? 81.707  29.982  22.228  1.00 41.94  ? 408 VAL A CB  1 
ATOM   3095 C  CG1 . VAL A 1 409 ? 81.089  30.457  20.921  1.00 44.65  ? 408 VAL A CG1 1 
ATOM   3096 C  CG2 . VAL A 1 409 ? 82.864  30.876  22.623  1.00 47.04  ? 408 VAL A CG2 1 
ATOM   3097 N  N   . PHE A 1 410 ? 79.311  27.936  23.091  1.00 39.09  ? 409 PHE A N   1 
ATOM   3098 C  CA  . PHE A 1 410 ? 78.077  27.226  22.783  1.00 37.01  ? 409 PHE A CA  1 
ATOM   3099 C  C   . PHE A 1 410 ? 76.945  27.662  23.706  1.00 44.54  ? 409 PHE A C   1 
ATOM   3100 O  O   . PHE A 1 410 ? 75.804  27.835  23.262  1.00 47.21  ? 409 PHE A O   1 
ATOM   3101 C  CB  . PHE A 1 410 ? 78.290  25.719  22.882  1.00 37.41  ? 409 PHE A CB  1 
ATOM   3102 C  CG  . PHE A 1 410 ? 77.061  24.929  22.577  1.00 40.10  ? 409 PHE A CG  1 
ATOM   3103 C  CD1 . PHE A 1 410 ? 76.729  24.625  21.269  1.00 38.28  ? 409 PHE A CD1 1 
ATOM   3104 C  CD2 . PHE A 1 410 ? 76.218  24.512  23.592  1.00 39.33  ? 409 PHE A CD2 1 
ATOM   3105 C  CE1 . PHE A 1 410 ? 75.590  23.912  20.979  1.00 34.39  ? 409 PHE A CE1 1 
ATOM   3106 C  CE2 . PHE A 1 410 ? 75.075  23.801  23.305  1.00 39.02  ? 409 PHE A CE2 1 
ATOM   3107 C  CZ  . PHE A 1 410 ? 74.761  23.501  21.998  1.00 38.88  ? 409 PHE A CZ  1 
ATOM   3108 N  N   . LEU A 1 411 ? 77.239  27.840  24.996  1.00 42.90  ? 410 LEU A N   1 
ATOM   3109 C  CA  . LEU A 1 411 ? 76.206  28.277  25.930  1.00 44.02  ? 410 LEU A CA  1 
ATOM   3110 C  C   . LEU A 1 411 ? 75.698  29.667  25.573  1.00 43.53  ? 410 LEU A C   1 
ATOM   3111 O  O   . LEU A 1 411 ? 74.492  29.925  25.624  1.00 46.33  ? 410 LEU A O   1 
ATOM   3112 C  CB  . LEU A 1 411 ? 76.742  28.251  27.361  1.00 45.37  ? 410 LEU A CB  1 
ATOM   3113 C  CG  . LEU A 1 411 ? 76.818  26.868  28.016  1.00 49.97  ? 410 LEU A CG  1 
ATOM   3114 C  CD1 . LEU A 1 411 ? 76.817  26.992  29.538  1.00 50.52  ? 410 LEU A CD1 1 
ATOM   3115 C  CD2 . LEU A 1 411 ? 75.676  25.976  27.541  1.00 46.95  ? 410 LEU A CD2 1 
ATOM   3116 N  N   . LEU A 1 412 ? 76.602  30.577  25.202  1.00 45.55  ? 411 LEU A N   1 
ATOM   3117 C  CA  . LEU A 1 412 ? 76.177  31.911  24.789  1.00 43.46  ? 411 LEU A CA  1 
ATOM   3118 C  C   . LEU A 1 412 ? 75.339  31.852  23.517  1.00 47.45  ? 411 LEU A C   1 
ATOM   3119 O  O   . LEU A 1 412 ? 74.352  32.584  23.382  1.00 47.11  ? 411 LEU A O   1 
ATOM   3120 C  CB  . LEU A 1 412 ? 77.395  32.814  24.586  1.00 44.62  ? 411 LEU A CB  1 
ATOM   3121 C  CG  . LEU A 1 412 ? 78.129  33.239  25.859  1.00 40.21  ? 411 LEU A CG  1 
ATOM   3122 C  CD1 . LEU A 1 412 ? 79.441  33.894  25.509  1.00 39.93  ? 411 LEU A CD1 1 
ATOM   3123 C  CD2 . LEU A 1 412 ? 77.273  34.175  26.703  1.00 45.30  ? 411 LEU A CD2 1 
ATOM   3124 N  N   . TRP A 1 413 ? 75.713  30.981  22.577  1.00 45.39  ? 412 TRP A N   1 
ATOM   3125 C  CA  . TRP A 1 413 ? 74.954  30.849  21.337  1.00 40.38  ? 412 TRP A CA  1 
ATOM   3126 C  C   . TRP A 1 413 ? 73.597  30.206  21.588  1.00 45.97  ? 412 TRP A C   1 
ATOM   3127 O  O   . TRP A 1 413 ? 72.579  30.658  21.050  1.00 43.86  ? 412 TRP A O   1 
ATOM   3128 C  CB  . TRP A 1 413 ? 75.761  30.035  20.329  1.00 40.17  ? 412 TRP A CB  1 
ATOM   3129 C  CG  . TRP A 1 413 ? 74.989  29.539  19.147  1.00 45.40  ? 412 TRP A CG  1 
ATOM   3130 C  CD1 . TRP A 1 413 ? 74.787  30.194  17.963  1.00 49.71  ? 412 TRP A CD1 1 
ATOM   3131 C  CD2 . TRP A 1 413 ? 74.343  28.268  19.016  1.00 50.49  ? 412 TRP A CD2 1 
ATOM   3132 N  NE1 . TRP A 1 413 ? 74.049  29.412  17.108  1.00 45.97  ? 412 TRP A NE1 1 
ATOM   3133 C  CE2 . TRP A 1 413 ? 73.763  28.225  17.731  1.00 53.34  ? 412 TRP A CE2 1 
ATOM   3134 C  CE3 . TRP A 1 413 ? 74.191  27.165  19.863  1.00 48.68  ? 412 TRP A CE3 1 
ATOM   3135 C  CZ2 . TRP A 1 413 ? 73.043  27.123  17.274  1.00 48.02  ? 412 TRP A CZ2 1 
ATOM   3136 C  CZ3 . TRP A 1 413 ? 73.474  26.074  19.408  1.00 46.61  ? 412 TRP A CZ3 1 
ATOM   3137 C  CH2 . TRP A 1 413 ? 72.909  26.060  18.124  1.00 46.89  ? 412 TRP A CH2 1 
ATOM   3138 N  N   . ARG A 1 414 ? 73.564  29.161  22.420  1.00 48.43  ? 413 ARG A N   1 
ATOM   3139 C  CA  . ARG A 1 414 ? 72.316  28.457  22.700  1.00 48.20  ? 413 ARG A CA  1 
ATOM   3140 C  C   . ARG A 1 414 ? 71.328  29.347  23.445  1.00 45.17  ? 413 ARG A C   1 
ATOM   3141 O  O   . ARG A 1 414 ? 70.116  29.268  23.213  1.00 51.29  ? 413 ARG A O   1 
ATOM   3142 C  CB  . ARG A 1 414 ? 72.607  27.184  23.498  1.00 44.29  ? 413 ARG A CB  1 
ATOM   3143 C  CG  . ARG A 1 414 ? 71.443  26.666  24.312  1.00 46.63  ? 413 ARG A CG  1 
ATOM   3144 C  CD  . ARG A 1 414 ? 70.416  26.010  23.418  1.00 48.11  ? 413 ARG A CD  1 
ATOM   3145 N  NE  . ARG A 1 414 ? 69.324  25.413  24.178  1.00 55.39  ? 413 ARG A NE  1 
ATOM   3146 C  CZ  . ARG A 1 414 ? 68.071  25.848  24.156  1.00 57.68  ? 413 ARG A CZ  1 
ATOM   3147 N  NH1 . ARG A 1 414 ? 67.715  26.899  23.433  1.00 51.67  ? 413 ARG A NH1 1 
ATOM   3148 N  NH2 . ARG A 1 414 ? 67.153  25.216  24.882  1.00 63.42  ? 413 ARG A NH2 1 
ATOM   3149 N  N   . ARG A 1 415 ? 71.819  30.200  24.340  1.00 47.57  ? 414 ARG A N   1 
ATOM   3150 C  CA  . ARG A 1 415 ? 70.942  31.124  25.046  1.00 49.26  ? 414 ARG A CA  1 
ATOM   3151 C  C   . ARG A 1 415 ? 70.700  32.414  24.268  1.00 54.91  ? 414 ARG A C   1 
ATOM   3152 O  O   . ARG A 1 415 ? 69.937  33.266  24.736  1.00 54.49  ? 414 ARG A O   1 
ATOM   3153 C  CB  . ARG A 1 415 ? 71.515  31.415  26.440  1.00 52.65  ? 414 ARG A CB  1 
ATOM   3154 C  CG  . ARG A 1 415 ? 72.250  32.746  26.591  1.00 63.25  ? 414 ARG A CG  1 
ATOM   3155 C  CD  . ARG A 1 415 ? 72.387  33.142  28.064  1.00 78.84  ? 414 ARG A CD  1 
ATOM   3156 N  NE  . ARG A 1 415 ? 73.378  34.189  28.307  1.00 80.67  ? 414 ARG A NE  1 
ATOM   3157 C  CZ  . ARG A 1 415 ? 73.309  35.432  27.842  1.00 81.61  ? 414 ARG A CZ  1 
ATOM   3158 N  NH1 . ARG A 1 415 ? 72.265  35.859  27.149  1.00 75.04  ? 414 ARG A NH1 1 
ATOM   3159 N  NH2 . ARG A 1 415 ? 74.301  36.280  28.108  1.00 81.31  ? 414 ARG A NH2 1 
ATOM   3160 N  N   . ARG A 1 416 ? 71.310  32.559  23.087  1.00 49.97  ? 415 ARG A N   1 
ATOM   3161 C  CA  . ARG A 1 416 ? 71.118  33.714  22.204  1.00 54.29  ? 415 ARG A CA  1 
ATOM   3162 C  C   . ARG A 1 416 ? 71.550  35.011  22.892  1.00 55.93  ? 415 ARG A C   1 
ATOM   3163 O  O   . ARG A 1 416 ? 70.779  35.960  23.046  1.00 61.51  ? 415 ARG A O   1 
ATOM   3164 C  CB  . ARG A 1 416 ? 69.666  33.797  21.716  1.00 57.43  ? 415 ARG A CB  1 
ATOM   3165 C  CG  . ARG A 1 416 ? 69.096  32.467  21.236  1.00 56.93  ? 415 ARG A CG  1 
ATOM   3166 C  CD  . ARG A 1 416 ? 67.624  32.583  20.849  1.00 60.67  ? 415 ARG A CD  1 
ATOM   3167 N  NE  . ARG A 1 416 ? 67.058  31.289  20.483  1.00 67.81  ? 415 ARG A NE  1 
ATOM   3168 C  CZ  . ARG A 1 416 ? 66.025  30.720  21.091  1.00 64.74  ? 415 ARG A CZ  1 
ATOM   3169 N  NH1 . ARG A 1 416 ? 65.400  31.313  22.096  1.00 66.14  ? 415 ARG A NH1 1 
ATOM   3170 N  NH2 . ARG A 1 416 ? 65.606  29.526  20.680  1.00 59.47  ? 415 ARG A NH2 1 
ATOM   3171 N  N   . ALA A 1 417 ? 72.826  35.039  23.287  1.00 63.10  ? 416 ALA A N   1 
ATOM   3172 C  CA  . ALA A 1 417 ? 73.352  36.166  24.051  1.00 61.61  ? 416 ALA A CA  1 
ATOM   3173 C  C   . ALA A 1 417 ? 73.403  37.447  23.228  1.00 62.30  ? 416 ALA A C   1 
ATOM   3174 O  O   . ALA A 1 417 ? 73.319  38.543  23.793  1.00 65.28  ? 416 ALA A O   1 
ATOM   3175 C  CB  . ALA A 1 417 ? 74.741  35.826  24.589  1.00 60.16  ? 416 ALA A CB  1 
ATOM   3176 N  N   . LEU A 1 418 ? 73.542  37.338  21.909  1.00 66.93  ? 417 LEU A N   1 
ATOM   3177 C  CA  . LEU A 1 418 ? 73.643  38.503  21.039  1.00 67.48  ? 417 LEU A CA  1 
ATOM   3178 C  C   . LEU A 1 418 ? 72.291  38.994  20.534  1.00 71.10  ? 417 LEU A C   1 
ATOM   3179 O  O   . LEU A 1 418 ? 72.245  39.989  19.803  1.00 75.37  ? 417 LEU A O   1 
ATOM   3180 C  CB  . LEU A 1 418 ? 74.553  38.194  19.843  1.00 65.57  ? 417 LEU A CB  1 
ATOM   3181 C  CG  . LEU A 1 418 ? 76.057  38.061  20.097  1.00 58.74  ? 417 LEU A CG  1 
ATOM   3182 C  CD1 . LEU A 1 418 ? 76.834  38.257  18.802  1.00 54.67  ? 417 LEU A CD1 1 
ATOM   3183 C  CD2 . LEU A 1 418 ? 76.524  39.046  21.158  1.00 52.71  ? 417 LEU A CD2 1 
ATOM   3184 N  N   . GLU A 1 419 ? 71.198  38.331  20.897  1.00 69.64  ? 418 GLU A N   1 
ATOM   3185 C  CA  . GLU A 1 419 ? 69.876  38.737  20.429  1.00 74.20  ? 418 GLU A CA  1 
ATOM   3186 C  C   . GLU A 1 419 ? 69.102  39.482  21.516  1.00 75.69  ? 418 GLU A C   1 
ATOM   3187 O  O   . GLU A 1 419 ? 68.370  40.433  21.235  1.00 81.15  ? 418 GLU A O   1 
ATOM   3188 C  CB  . GLU A 1 419 ? 69.078  37.521  19.953  1.00 72.89  ? 418 GLU A CB  1 
ATOM   3189 C  CG  . GLU A 1 419 ? 69.886  36.531  19.123  1.00 73.42  ? 418 GLU A CG  1 
ATOM   3190 C  CD  . GLU A 1 419 ? 70.129  37.013  17.703  1.00 77.63  ? 418 GLU A CD  1 
ATOM   3191 O  OE1 . GLU A 1 419 ? 69.388  37.909  17.241  1.00 81.09  ? 418 GLU A OE1 1 
ATOM   3192 O  OE2 . GLU A 1 419 ? 71.060  36.495  17.048  1.00 75.29  ? 418 GLU A OE2 1 
ATOM   3193 N  N   . GLN B 2 5   ? 129.668 8.230   -4.910  1.00 81.06  ? 3   GLN B N   1 
ATOM   3194 C  CA  . GLN B 2 5   ? 129.713 6.777   -5.028  1.00 76.00  ? 3   GLN B CA  1 
ATOM   3195 C  C   . GLN B 2 5   ? 130.064 6.342   -6.450  1.00 78.25  ? 3   GLN B C   1 
ATOM   3196 O  O   . GLN B 2 5   ? 130.518 5.218   -6.665  1.00 80.37  ? 3   GLN B O   1 
ATOM   3197 C  CB  . GLN B 2 5   ? 128.376 6.163   -4.607  1.00 69.61  ? 3   GLN B CB  1 
ATOM   3198 C  CG  . GLN B 2 5   ? 128.496 4.768   -4.016  1.00 78.50  ? 3   GLN B CG  1 
ATOM   3199 C  CD  . GLN B 2 5   ? 127.209 3.977   -4.121  1.00 65.09  ? 3   GLN B CD  1 
ATOM   3200 O  OE1 . GLN B 2 5   ? 126.373 4.248   -4.977  1.00 65.09  ? 3   GLN B OE1 1 
ATOM   3201 N  NE2 . GLN B 2 5   ? 127.047 2.991   -3.250  1.00 69.27  ? 3   GLN B NE2 1 
ATOM   3202 N  N   . LEU B 2 6   ? 129.855 7.233   -7.420  1.00 70.22  ? 4   LEU B N   1 
ATOM   3203 C  CA  . LEU B 2 6   ? 130.135 6.946   -8.821  1.00 70.23  ? 4   LEU B CA  1 
ATOM   3204 C  C   . LEU B 2 6   ? 130.898 8.103   -9.449  1.00 66.83  ? 4   LEU B C   1 
ATOM   3205 O  O   . LEU B 2 6   ? 130.545 9.269   -9.255  1.00 67.91  ? 4   LEU B O   1 
ATOM   3206 C  CB  . LEU B 2 6   ? 128.842 6.692   -9.610  1.00 69.94  ? 4   LEU B CB  1 
ATOM   3207 C  CG  . LEU B 2 6   ? 127.994 5.477   -9.228  1.00 66.27  ? 4   LEU B CG  1 
ATOM   3208 C  CD1 . LEU B 2 6   ? 126.597 5.599   -9.817  1.00 65.08  ? 4   LEU B CD1 1 
ATOM   3209 C  CD2 . LEU B 2 6   ? 128.658 4.190   -9.685  1.00 63.38  ? 4   LEU B CD2 1 
ATOM   3210 N  N   . VAL B 2 7   ? 131.944 7.772   -10.207 1.00 75.08  ? 5   VAL B N   1 
ATOM   3211 C  CA  . VAL B 2 7   ? 132.750 8.756   -10.922 1.00 80.77  ? 5   VAL B CA  1 
ATOM   3212 C  C   . VAL B 2 7   ? 132.941 8.281   -12.358 1.00 81.49  ? 5   VAL B C   1 
ATOM   3213 O  O   . VAL B 2 7   ? 133.102 7.081   -12.614 1.00 71.40  ? 5   VAL B O   1 
ATOM   3214 C  CB  . VAL B 2 7   ? 134.107 9.006   -10.225 1.00 73.90  ? 5   VAL B CB  1 
ATOM   3215 C  CG1 . VAL B 2 7   ? 135.155 7.982   -10.648 1.00 80.70  ? 5   VAL B CG1 1 
ATOM   3216 C  CG2 . VAL B 2 7   ? 134.595 10.417  -10.513 1.00 85.86  ? 5   VAL B CG2 1 
ATOM   3217 N  N   . GLU B 2 8   ? 132.902 9.222   -13.297 1.00 97.68  ? 6   GLU B N   1 
ATOM   3218 C  CA  . GLU B 2 8   ? 132.937 8.922   -14.719 1.00 89.25  ? 6   GLU B CA  1 
ATOM   3219 C  C   . GLU B 2 8   ? 134.261 9.362   -15.330 1.00 94.47  ? 6   GLU B C   1 
ATOM   3220 O  O   . GLU B 2 8   ? 134.923 10.277  -14.833 1.00 103.18 ? 6   GLU B O   1 
ATOM   3221 C  CB  . GLU B 2 8   ? 131.781 9.607   -15.456 1.00 86.23  ? 6   GLU B CB  1 
ATOM   3222 C  CG  . GLU B 2 8   ? 130.450 8.891   -15.328 1.00 85.37  ? 6   GLU B CG  1 
ATOM   3223 C  CD  . GLU B 2 8   ? 129.464 9.656   -14.465 1.00 93.99  ? 6   GLU B CD  1 
ATOM   3224 O  OE1 . GLU B 2 8   ? 129.866 10.675  -13.865 1.00 98.76  ? 6   GLU B OE1 1 
ATOM   3225 O  OE2 . GLU B 2 8   ? 128.290 9.241   -14.384 1.00 87.18  ? 6   GLU B OE2 1 
ATOM   3226 N  N   . SER B 2 9   ? 134.634 8.696   -16.419 1.00 78.59  ? 7   SER B N   1 
ATOM   3227 C  CA  . SER B 2 9   ? 135.843 9.021   -17.156 1.00 74.91  ? 7   SER B CA  1 
ATOM   3228 C  C   . SER B 2 9   ? 135.601 8.725   -18.627 1.00 78.07  ? 7   SER B C   1 
ATOM   3229 O  O   . SER B 2 9   ? 134.752 7.900   -18.976 1.00 71.80  ? 7   SER B O   1 
ATOM   3230 C  CB  . SER B 2 9   ? 137.050 8.231   -16.639 1.00 75.09  ? 7   SER B CB  1 
ATOM   3231 O  OG  . SER B 2 9   ? 138.098 8.212   -17.592 1.00 89.50  ? 7   SER B OG  1 
ATOM   3232 N  N   . GLY B 2 10  ? 136.354 9.409   -19.485 1.00 81.73  ? 8   GLY B N   1 
ATOM   3233 C  CA  . GLY B 2 10  ? 136.209 9.277   -20.921 1.00 74.06  ? 8   GLY B CA  1 
ATOM   3234 C  C   . GLY B 2 10  ? 135.292 10.336  -21.499 1.00 73.33  ? 8   GLY B C   1 
ATOM   3235 O  O   . GLY B 2 10  ? 134.707 11.165  -20.795 1.00 73.40  ? 8   GLY B O   1 
ATOM   3236 N  N   . GLY B 2 11  ? 135.173 10.301  -22.820 1.00 73.76  ? 9   GLY B N   1 
ATOM   3237 C  CA  . GLY B 2 11  ? 134.317 11.225  -23.531 1.00 78.38  ? 9   GLY B CA  1 
ATOM   3238 C  C   . GLY B 2 11  ? 135.028 12.507  -23.925 1.00 72.75  ? 9   GLY B C   1 
ATOM   3239 O  O   . GLY B 2 11  ? 136.166 12.780  -23.540 1.00 71.83  ? 9   GLY B O   1 
ATOM   3240 N  N   . GLY B 2 12  ? 134.321 13.312  -24.704 1.00 71.85  ? 10  GLY B N   1 
ATOM   3241 C  CA  . GLY B 2 12  ? 134.830 14.552  -25.239 1.00 72.14  ? 10  GLY B CA  1 
ATOM   3242 C  C   . GLY B 2 12  ? 134.337 14.742  -26.655 1.00 70.19  ? 10  GLY B C   1 
ATOM   3243 O  O   . GLY B 2 12  ? 133.407 14.075  -27.104 1.00 72.67  ? 10  GLY B O   1 
ATOM   3244 N  N   . LEU B 2 13  ? 134.969 15.674  -27.364 1.00 70.62  ? 11  LEU B N   1 
ATOM   3245 C  CA  . LEU B 2 13  ? 134.632 15.928  -28.758 1.00 66.74  ? 11  LEU B CA  1 
ATOM   3246 C  C   . LEU B 2 13  ? 135.208 14.822  -29.634 1.00 72.79  ? 11  LEU B C   1 
ATOM   3247 O  O   . LEU B 2 13  ? 136.427 14.626  -29.677 1.00 72.35  ? 11  LEU B O   1 
ATOM   3248 C  CB  . LEU B 2 13  ? 135.171 17.290  -29.188 1.00 80.34  ? 11  LEU B CB  1 
ATOM   3249 C  CG  . LEU B 2 13  ? 134.633 17.925  -30.476 1.00 80.53  ? 11  LEU B CG  1 
ATOM   3250 C  CD1 . LEU B 2 13  ? 133.152 17.639  -30.662 1.00 71.26  ? 11  LEU B CD1 1 
ATOM   3251 C  CD2 . LEU B 2 13  ? 134.911 19.425  -30.505 1.00 81.34  ? 11  LEU B CD2 1 
ATOM   3252 N  N   . VAL B 2 14  ? 134.339 14.101  -30.335 1.00 72.92  ? 12  VAL B N   1 
ATOM   3253 C  CA  . VAL B 2 14  ? 134.751 12.990  -31.183 1.00 74.40  ? 12  VAL B CA  1 
ATOM   3254 C  C   . VAL B 2 14  ? 134.153 13.178  -32.569 1.00 77.26  ? 12  VAL B C   1 
ATOM   3255 O  O   . VAL B 2 14  ? 133.034 13.685  -32.713 1.00 70.25  ? 12  VAL B O   1 
ATOM   3256 C  CB  . VAL B 2 14  ? 134.333 11.631  -30.579 1.00 73.38  ? 12  VAL B CB  1 
ATOM   3257 C  CG1 . VAL B 2 14  ? 132.819 11.523  -30.505 1.00 73.51  ? 12  VAL B CG1 1 
ATOM   3258 C  CG2 . VAL B 2 14  ? 134.922 10.477  -31.379 1.00 70.17  ? 12  VAL B CG2 1 
ATOM   3259 N  N   . GLN B 2 15  ? 134.909 12.785  -33.590 1.00 80.83  ? 13  GLN B N   1 
ATOM   3260 C  CA  . GLN B 2 15  ? 134.416 12.856  -34.957 1.00 83.13  ? 13  GLN B CA  1 
ATOM   3261 C  C   . GLN B 2 15  ? 133.323 11.817  -35.175 1.00 81.01  ? 13  GLN B C   1 
ATOM   3262 O  O   . GLN B 2 15  ? 133.394 10.700  -34.655 1.00 79.89  ? 13  GLN B O   1 
ATOM   3263 C  CB  . GLN B 2 15  ? 135.564 12.639  -35.943 1.00 78.86  ? 13  GLN B CB  1 
ATOM   3264 C  CG  . GLN B 2 15  ? 135.184 12.828  -37.402 1.00 84.84  ? 13  GLN B CG  1 
ATOM   3265 C  CD  . GLN B 2 15  ? 136.272 12.364  -38.354 1.00 91.41  ? 13  GLN B CD  1 
ATOM   3266 O  OE1 . GLN B 2 15  ? 137.451 12.322  -37.998 1.00 95.98  ? 13  GLN B OE1 1 
ATOM   3267 N  NE2 . GLN B 2 15  ? 135.879 12.005  -39.572 1.00 89.43  ? 13  GLN B NE2 1 
ATOM   3268 N  N   . ALA B 2 16  ? 132.297 12.200  -35.936 1.00 76.30  ? 14  ALA B N   1 
ATOM   3269 C  CA  . ALA B 2 16  ? 131.212 11.281  -36.252 1.00 66.41  ? 14  ALA B CA  1 
ATOM   3270 C  C   . ALA B 2 16  ? 131.746 10.049  -36.970 1.00 77.27  ? 14  ALA B C   1 
ATOM   3271 O  O   . ALA B 2 16  ? 132.485 10.158  -37.954 1.00 85.66  ? 14  ALA B O   1 
ATOM   3272 C  CB  . ALA B 2 16  ? 130.160 11.979  -37.111 1.00 66.58  ? 14  ALA B CB  1 
ATOM   3273 N  N   . GLY B 2 17  ? 131.369 8.874   -36.471 1.00 75.51  ? 15  GLY B N   1 
ATOM   3274 C  CA  . GLY B 2 17  ? 131.846 7.613   -36.982 1.00 75.34  ? 15  GLY B CA  1 
ATOM   3275 C  C   . GLY B 2 17  ? 132.941 6.977   -36.152 1.00 86.53  ? 15  GLY B C   1 
ATOM   3276 O  O   . GLY B 2 17  ? 133.126 5.757   -36.226 1.00 86.69  ? 15  GLY B O   1 
ATOM   3277 N  N   . GLY B 2 18  ? 133.666 7.769   -35.362 1.00 99.47  ? 16  GLY B N   1 
ATOM   3278 C  CA  . GLY B 2 18  ? 134.727 7.226   -34.547 1.00 100.92 ? 16  GLY B CA  1 
ATOM   3279 C  C   . GLY B 2 18  ? 134.213 6.539   -33.297 1.00 94.62  ? 16  GLY B C   1 
ATOM   3280 O  O   . GLY B 2 18  ? 133.089 6.754   -32.845 1.00 84.43  ? 16  GLY B O   1 
ATOM   3281 N  N   . SER B 2 19  ? 135.065 5.693   -32.731 1.00 94.75  ? 17  SER B N   1 
ATOM   3282 C  CA  . SER B 2 19  ? 134.724 4.958   -31.526 1.00 85.94  ? 17  SER B CA  1 
ATOM   3283 C  C   . SER B 2 19  ? 135.010 5.803   -30.286 1.00 84.86  ? 17  SER B C   1 
ATOM   3284 O  O   . SER B 2 19  ? 135.703 6.820   -30.339 1.00 87.80  ? 17  SER B O   1 
ATOM   3285 C  CB  . SER B 2 19  ? 135.498 3.642   -31.469 1.00 88.30  ? 17  SER B CB  1 
ATOM   3286 O  OG  . SER B 2 19  ? 135.174 2.816   -32.574 1.00 96.93  ? 17  SER B OG  1 
ATOM   3287 N  N   . LEU B 2 20  ? 134.460 5.365   -29.154 1.00 80.70  ? 18  LEU B N   1 
ATOM   3288 C  CA  . LEU B 2 20  ? 134.646 6.062   -27.889 1.00 71.80  ? 18  LEU B CA  1 
ATOM   3289 C  C   . LEU B 2 20  ? 134.434 5.066   -26.759 1.00 72.68  ? 18  LEU B C   1 
ATOM   3290 O  O   . LEU B 2 20  ? 133.583 4.179   -26.860 1.00 72.44  ? 18  LEU B O   1 
ATOM   3291 C  CB  . LEU B 2 20  ? 133.680 7.248   -27.772 1.00 73.67  ? 18  LEU B CB  1 
ATOM   3292 C  CG  . LEU B 2 20  ? 133.983 8.419   -26.831 1.00 77.94  ? 18  LEU B CG  1 
ATOM   3293 C  CD1 . LEU B 2 20  ? 133.945 8.028   -25.364 1.00 79.62  ? 18  LEU B CD1 1 
ATOM   3294 C  CD2 . LEU B 2 20  ? 135.333 9.015   -27.181 1.00 75.31  ? 18  LEU B CD2 1 
ATOM   3295 N  N   . GLY B 2 21  ? 135.219 5.208   -25.695 1.00 75.99  ? 19  GLY B N   1 
ATOM   3296 C  CA  . GLY B 2 21  ? 135.073 4.338   -24.546 1.00 74.22  ? 19  GLY B CA  1 
ATOM   3297 C  C   . GLY B 2 21  ? 134.861 5.086   -23.247 1.00 68.86  ? 19  GLY B C   1 
ATOM   3298 O  O   . GLY B 2 21  ? 135.754 5.801   -22.786 1.00 80.73  ? 19  GLY B O   1 
ATOM   3299 N  N   . LEU B 2 22  ? 133.683 4.935   -22.650 1.00 63.77  ? 20  LEU B N   1 
ATOM   3300 C  CA  . LEU B 2 22  ? 133.386 5.507   -21.347 1.00 60.75  ? 20  LEU B CA  1 
ATOM   3301 C  C   . LEU B 2 22  ? 133.580 4.458   -20.263 1.00 61.19  ? 20  LEU B C   1 
ATOM   3302 O  O   . LEU B 2 22  ? 133.352 3.266   -20.480 1.00 69.38  ? 20  LEU B O   1 
ATOM   3303 C  CB  . LEU B 2 22  ? 131.956 6.048   -21.290 1.00 65.71  ? 20  LEU B CB  1 
ATOM   3304 C  CG  . LEU B 2 22  ? 131.555 7.135   -22.286 1.00 67.52  ? 20  LEU B CG  1 
ATOM   3305 C  CD1 . LEU B 2 22  ? 130.086 7.480   -22.105 1.00 57.10  ? 20  LEU B CD1 1 
ATOM   3306 C  CD2 . LEU B 2 22  ? 132.422 8.371   -22.122 1.00 65.48  ? 20  LEU B CD2 1 
ATOM   3307 N  N   . SER B 2 23  ? 134.004 4.913   -19.088 1.00 54.91  ? 21  SER B N   1 
ATOM   3308 C  CA  . SER B 2 23  ? 134.191 4.034   -17.945 1.00 60.13  ? 21  SER B CA  1 
ATOM   3309 C  C   . SER B 2 23  ? 133.668 4.726   -16.697 1.00 61.33  ? 21  SER B C   1 
ATOM   3310 O  O   . SER B 2 23  ? 133.696 5.955   -16.591 1.00 66.66  ? 21  SER B O   1 
ATOM   3311 C  CB  . SER B 2 23  ? 135.665 3.646   -17.756 1.00 62.52  ? 21  SER B CB  1 
ATOM   3312 O  OG  . SER B 2 23  ? 136.366 4.647   -17.041 1.00 71.99  ? 21  SER B OG  1 
ATOM   3313 N  N   . CYS B 2 24  ? 133.186 3.926   -15.751 1.00 56.54  ? 22  CYS B N   1 
ATOM   3314 C  CA  . CYS B 2 24  ? 132.635 4.448   -14.508 1.00 68.26  ? 22  CYS B CA  1 
ATOM   3315 C  C   . CYS B 2 24  ? 133.140 3.601   -13.350 1.00 66.37  ? 22  CYS B C   1 
ATOM   3316 O  O   . CYS B 2 24  ? 133.012 2.374   -13.374 1.00 64.55  ? 22  CYS B O   1 
ATOM   3317 C  CB  . CYS B 2 24  ? 131.097 4.462   -14.546 1.00 65.00  ? 22  CYS B CB  1 
ATOM   3318 S  SG  . CYS B 2 24  ? 130.287 4.910   -12.986 1.00 78.38  ? 22  CYS B SG  1 
ATOM   3319 N  N   . ALA B 2 25  ? 133.724 4.255   -12.351 1.00 60.21  ? 23  ALA B N   1 
ATOM   3320 C  CA  . ALA B 2 25  ? 134.229 3.581   -11.165 1.00 71.17  ? 23  ALA B CA  1 
ATOM   3321 C  C   . ALA B 2 25  ? 133.283 3.803   -9.992  1.00 75.49  ? 23  ALA B C   1 
ATOM   3322 O  O   . ALA B 2 25  ? 132.648 4.854   -9.873  1.00 74.92  ? 23  ALA B O   1 
ATOM   3323 C  CB  . ALA B 2 25  ? 135.632 4.079   -10.808 1.00 64.84  ? 23  ALA B CB  1 
ATOM   3324 N  N   . ALA B 2 26  ? 133.192 2.798   -9.121  1.00 71.36  ? 24  ALA B N   1 
ATOM   3325 C  CA  . ALA B 2 26  ? 132.296 2.839   -7.974  1.00 77.75  ? 24  ALA B CA  1 
ATOM   3326 C  C   . ALA B 2 26  ? 133.067 2.566   -6.690  1.00 94.93  ? 24  ALA B C   1 
ATOM   3327 O  O   . ALA B 2 26  ? 133.981 1.736   -6.666  1.00 94.89  ? 24  ALA B O   1 
ATOM   3328 C  CB  . ALA B 2 26  ? 131.159 1.824   -8.118  1.00 84.19  ? 24  ALA B CB  1 
ATOM   3329 N  N   . SER B 2 27  ? 132.687 3.265   -5.625  1.00 98.64  ? 25  SER B N   1 
ATOM   3330 C  CA  . SER B 2 27  ? 133.306 3.092   -4.319  1.00 106.49 ? 25  SER B CA  1 
ATOM   3331 C  C   . SER B 2 27  ? 132.500 2.067   -3.518  1.00 115.15 ? 25  SER B C   1 
ATOM   3332 O  O   . SER B 2 27  ? 131.758 1.261   -4.087  1.00 113.66 ? 25  SER B O   1 
ATOM   3333 C  CB  . SER B 2 27  ? 133.411 4.447   -3.612  1.00 108.66 ? 25  SER B CB  1 
ATOM   3334 O  OG  . SER B 2 27  ? 132.125 4.975   -3.330  1.00 114.86 ? 25  SER B OG  1 
ATOM   3335 N  N   . GLY B 2 28  ? 132.635 2.082   -2.195  1.00 135.04 ? 26  GLY B N   1 
ATOM   3336 C  CA  . GLY B 2 28  ? 131.857 1.200   -1.348  1.00 124.13 ? 26  GLY B CA  1 
ATOM   3337 C  C   . GLY B 2 28  ? 132.467 -0.174  -1.158  1.00 127.50 ? 26  GLY B C   1 
ATOM   3338 O  O   . GLY B 2 28  ? 133.692 -0.319  -1.103  1.00 132.19 ? 26  GLY B O   1 
ATOM   3339 N  N   . ARG B 2 29  ? 131.613 -1.192  -1.056  1.00 117.51 ? 27  ARG B N   1 
ATOM   3340 C  CA  . ARG B 2 29  ? 132.065 -2.558  -0.825  1.00 117.95 ? 27  ARG B CA  1 
ATOM   3341 C  C   . ARG B 2 29  ? 131.244 -3.534  -1.657  1.00 109.86 ? 27  ARG B C   1 
ATOM   3342 O  O   . ARG B 2 29  ? 131.761 -4.149  -2.596  1.00 110.12 ? 27  ARG B O   1 
ATOM   3343 C  CB  . ARG B 2 29  ? 131.968 -2.906  0.663   1.00 116.89 ? 27  ARG B CB  1 
ATOM   3344 C  CG  . ARG B 2 29  ? 133.296 -3.236  1.329   1.00 111.73 ? 27  ARG B CG  1 
ATOM   3345 C  CD  . ARG B 2 29  ? 133.111 -3.447  2.826   1.00 111.18 ? 27  ARG B CD  1 
ATOM   3346 N  NE  . ARG B 2 29  ? 134.105 -4.354  3.386   1.00 111.86 ? 27  ARG B NE  1 
ATOM   3347 C  CZ  . ARG B 2 29  ? 134.112 -4.774  4.645   1.00 112.67 ? 27  ARG B CZ  1 
ATOM   3348 N  NH1 . ARG B 2 29  ? 133.186 -4.387  5.508   1.00 107.92 ? 27  ARG B NH1 1 
ATOM   3349 N  NH2 . ARG B 2 29  ? 135.071 -5.603  5.048   1.00 110.63 ? 27  ARG B NH2 1 
ATOM   3350 N  N   . THR B 2 30  ? 129.964 -3.681  -1.317  1.00 109.08 ? 28  THR B N   1 
ATOM   3351 C  CA  . THR B 2 30  ? 129.062 -4.542  -2.075  1.00 102.99 ? 28  THR B CA  1 
ATOM   3352 C  C   . THR B 2 30  ? 128.810 -3.916  -3.439  1.00 99.01  ? 28  THR B C   1 
ATOM   3353 O  O   . THR B 2 30  ? 128.098 -2.913  -3.551  1.00 102.52 ? 28  THR B O   1 
ATOM   3354 C  CB  . THR B 2 30  ? 127.754 -4.745  -1.314  1.00 99.41  ? 28  THR B CB  1 
ATOM   3355 O  OG1 . THR B 2 30  ? 127.956 -5.703  -0.266  1.00 100.53 ? 28  THR B OG1 1 
ATOM   3356 C  CG2 . THR B 2 30  ? 126.661 -5.261  -2.241  1.00 99.17  ? 28  THR B CG2 1 
ATOM   3357 N  N   . PHE B 2 31  ? 129.410 -4.490  -4.471  1.00 93.96  ? 29  PHE B N   1 
ATOM   3358 C  CA  . PHE B 2 31  ? 129.267 -3.997  -5.833  1.00 89.79  ? 29  PHE B CA  1 
ATOM   3359 C  C   . PHE B 2 31  ? 128.633 -5.013  -6.764  1.00 89.37  ? 29  PHE B C   1 
ATOM   3360 O  O   . PHE B 2 31  ? 127.858 -4.634  -7.649  1.00 80.28  ? 29  PHE B O   1 
ATOM   3361 C  CB  . PHE B 2 31  ? 130.640 -3.580  -6.390  1.00 91.69  ? 29  PHE B CB  1 
ATOM   3362 C  CG  . PHE B 2 31  ? 130.601 -3.111  -7.818  1.00 83.25  ? 29  PHE B CG  1 
ATOM   3363 C  CD1 . PHE B 2 31  ? 130.211 -1.819  -8.126  1.00 82.11  ? 29  PHE B CD1 1 
ATOM   3364 C  CD2 . PHE B 2 31  ? 130.955 -3.963  -8.853  1.00 80.45  ? 29  PHE B CD2 1 
ATOM   3365 C  CE1 . PHE B 2 31  ? 130.172 -1.385  -9.439  1.00 83.15  ? 29  PHE B CE1 1 
ATOM   3366 C  CE2 . PHE B 2 31  ? 130.918 -3.535  -10.168 1.00 81.67  ? 29  PHE B CE2 1 
ATOM   3367 C  CZ  . PHE B 2 31  ? 130.529 -2.244  -10.461 1.00 79.81  ? 29  PHE B CZ  1 
ATOM   3368 N  N   . SER B 2 32  ? 128.942 -6.298  -6.586  1.00 90.11  ? 30  SER B N   1 
ATOM   3369 C  CA  . SER B 2 32  ? 128.393 -7.339  -7.443  1.00 89.70  ? 30  SER B CA  1 
ATOM   3370 C  C   . SER B 2 32  ? 126.888 -7.499  -7.286  1.00 90.68  ? 30  SER B C   1 
ATOM   3371 O  O   . SER B 2 32  ? 126.278 -8.214  -8.085  1.00 93.76  ? 30  SER B O   1 
ATOM   3372 C  CB  . SER B 2 32  ? 129.086 -8.672  -7.156  1.00 82.96  ? 30  SER B CB  1 
ATOM   3373 O  OG  . SER B 2 32  ? 129.040 -8.980  -5.774  1.00 74.95  ? 30  SER B OG  1 
ATOM   3374 N  N   . ASN B 2 33  ? 126.280 -6.863  -6.288  1.00 85.90  ? 31  ASN B N   1 
ATOM   3375 C  CA  . ASN B 2 33  ? 124.842 -6.945  -6.077  1.00 87.36  ? 31  ASN B CA  1 
ATOM   3376 C  C   . ASN B 2 33  ? 124.090 -5.748  -6.641  1.00 83.76  ? 31  ASN B C   1 
ATOM   3377 O  O   . ASN B 2 33  ? 122.856 -5.725  -6.585  1.00 79.62  ? 31  ASN B O   1 
ATOM   3378 C  CB  . ASN B 2 33  ? 124.541 -7.093  -4.584  1.00 89.61  ? 31  ASN B CB  1 
ATOM   3379 C  CG  . ASN B 2 33  ? 125.209 -8.310  -3.982  1.00 98.64  ? 31  ASN B CG  1 
ATOM   3380 O  OD1 . ASN B 2 33  ? 125.777 -8.248  -2.891  1.00 94.16  ? 31  ASN B OD1 1 
ATOM   3381 N  ND2 . ASN B 2 33  ? 125.156 -9.427  -4.700  1.00 102.17 ? 31  ASN B ND2 1 
ATOM   3382 N  N   . TYR B 2 34  ? 124.796 -4.764  -7.190  1.00 78.41  ? 32  TYR B N   1 
ATOM   3383 C  CA  . TYR B 2 34  ? 124.175 -3.576  -7.755  1.00 73.60  ? 32  TYR B CA  1 
ATOM   3384 C  C   . TYR B 2 34  ? 124.004 -3.756  -9.255  1.00 72.29  ? 32  TYR B C   1 
ATOM   3385 O  O   . TYR B 2 34  ? 124.955 -4.119  -9.953  1.00 72.88  ? 32  TYR B O   1 
ATOM   3386 C  CB  . TYR B 2 34  ? 125.017 -2.331  -7.475  1.00 69.17  ? 32  TYR B CB  1 
ATOM   3387 C  CG  . TYR B 2 34  ? 124.782 -1.721  -6.112  1.00 78.06  ? 32  TYR B CG  1 
ATOM   3388 C  CD1 . TYR B 2 34  ? 123.854 -0.702  -5.935  1.00 70.89  ? 32  TYR B CD1 1 
ATOM   3389 C  CD2 . TYR B 2 34  ? 125.496 -2.157  -5.003  1.00 82.06  ? 32  TYR B CD2 1 
ATOM   3390 C  CE1 . TYR B 2 34  ? 123.641 -0.139  -4.686  1.00 71.54  ? 32  TYR B CE1 1 
ATOM   3391 C  CE2 . TYR B 2 34  ? 125.289 -1.601  -3.752  1.00 77.69  ? 32  TYR B CE2 1 
ATOM   3392 C  CZ  . TYR B 2 34  ? 124.363 -0.593  -3.599  1.00 75.47  ? 32  TYR B CZ  1 
ATOM   3393 O  OH  . TYR B 2 34  ? 124.160 -0.041  -2.353  1.00 78.23  ? 32  TYR B OH  1 
ATOM   3394 N  N   . VAL B 2 35  ? 122.791 -3.511  -9.748  1.00 73.00  ? 33  VAL B N   1 
ATOM   3395 C  CA  . VAL B 2 35  ? 122.592 -3.421  -11.187 1.00 69.39  ? 33  VAL B CA  1 
ATOM   3396 C  C   . VAL B 2 35  ? 123.192 -2.111  -11.681 1.00 64.07  ? 33  VAL B C   1 
ATOM   3397 O  O   . VAL B 2 35  ? 123.043 -1.054  -11.050 1.00 62.39  ? 33  VAL B O   1 
ATOM   3398 C  CB  . VAL B 2 35  ? 121.099 -3.557  -11.546 1.00 70.67  ? 33  VAL B CB  1 
ATOM   3399 C  CG1 . VAL B 2 35  ? 120.352 -2.274  -11.317 1.00 64.38  ? 33  VAL B CG1 1 
ATOM   3400 C  CG2 . VAL B 2 35  ? 120.939 -3.980  -12.990 1.00 71.75  ? 33  VAL B CG2 1 
ATOM   3401 N  N   . MET B 2 36  ? 123.923 -2.183  -12.787 1.00 61.31  ? 34  MET B N   1 
ATOM   3402 C  CA  . MET B 2 36  ? 124.640 -1.041  -13.331 1.00 60.28  ? 34  MET B CA  1 
ATOM   3403 C  C   . MET B 2 36  ? 124.010 -0.614  -14.649 1.00 58.01  ? 34  MET B C   1 
ATOM   3404 O  O   . MET B 2 36  ? 123.540 -1.448  -15.429 1.00 57.86  ? 34  MET B O   1 
ATOM   3405 C  CB  . MET B 2 36  ? 126.119 -1.376  -13.547 1.00 62.74  ? 34  MET B CB  1 
ATOM   3406 C  CG  . MET B 2 36  ? 126.931 -1.570  -12.269 1.00 67.93  ? 34  MET B CG  1 
ATOM   3407 S  SD  . MET B 2 36  ? 126.435 -0.526  -10.888 1.00 71.15  ? 34  MET B SD  1 
ATOM   3408 C  CE  . MET B 2 36  ? 127.166 1.036   -11.379 1.00 58.17  ? 34  MET B CE  1 
ATOM   3409 N  N   . ALA B 2 37  ? 124.011 0.692   -14.902 1.00 51.39  ? 35  ALA B N   1 
ATOM   3410 C  CA  . ALA B 2 37  ? 123.339 1.197   -16.087 1.00 55.51  ? 35  ALA B CA  1 
ATOM   3411 C  C   . ALA B 2 37  ? 123.986 2.488   -16.558 1.00 55.41  ? 35  ALA B C   1 
ATOM   3412 O  O   . ALA B 2 37  ? 124.625 3.208   -15.785 1.00 48.92  ? 35  ALA B O   1 
ATOM   3413 C  CB  . ALA B 2 37  ? 121.845 1.431   -15.830 1.00 52.16  ? 35  ALA B CB  1 
ATOM   3414 N  N   . TRP B 2 38  ? 123.803 2.770   -17.843 1.00 49.97  ? 36  TRP B N   1 
ATOM   3415 C  CA  . TRP B 2 38  ? 124.181 4.037   -18.446 1.00 52.91  ? 36  TRP B CA  1 
ATOM   3416 C  C   . TRP B 2 38  ? 122.921 4.780   -18.862 1.00 49.80  ? 36  TRP B C   1 
ATOM   3417 O  O   . TRP B 2 38  ? 122.008 4.185   -19.441 1.00 51.18  ? 36  TRP B O   1 
ATOM   3418 C  CB  . TRP B 2 38  ? 125.085 3.826   -19.660 1.00 53.63  ? 36  TRP B CB  1 
ATOM   3419 C  CG  . TRP B 2 38  ? 126.509 3.518   -19.332 1.00 56.21  ? 36  TRP B CG  1 
ATOM   3420 C  CD1 . TRP B 2 38  ? 127.129 2.307   -19.435 1.00 62.63  ? 36  TRP B CD1 1 
ATOM   3421 C  CD2 . TRP B 2 38  ? 127.506 4.441   -18.877 1.00 57.53  ? 36  TRP B CD2 1 
ATOM   3422 N  NE1 . TRP B 2 38  ? 128.448 2.416   -19.069 1.00 61.60  ? 36  TRP B NE1 1 
ATOM   3423 C  CE2 . TRP B 2 38  ? 128.704 3.716   -18.718 1.00 61.77  ? 36  TRP B CE2 1 
ATOM   3424 C  CE3 . TRP B 2 38  ? 127.501 5.808   -18.585 1.00 55.91  ? 36  TRP B CE3 1 
ATOM   3425 C  CZ2 . TRP B 2 38  ? 129.884 4.309   -18.272 1.00 56.06  ? 36  TRP B CZ2 1 
ATOM   3426 C  CZ3 . TRP B 2 38  ? 128.675 6.397   -18.148 1.00 62.45  ? 36  TRP B CZ3 1 
ATOM   3427 C  CH2 . TRP B 2 38  ? 129.849 5.647   -17.992 1.00 58.35  ? 36  TRP B CH2 1 
ATOM   3428 N  N   . PHE B 2 39  ? 122.872 6.068   -18.552 1.00 51.23  ? 37  PHE B N   1 
ATOM   3429 C  CA  . PHE B 2 39  ? 121.839 6.960   -19.041 1.00 45.19  ? 37  PHE B CA  1 
ATOM   3430 C  C   . PHE B 2 39  ? 122.508 8.138   -19.736 1.00 50.65  ? 37  PHE B C   1 
ATOM   3431 O  O   . PHE B 2 39  ? 123.691 8.415   -19.525 1.00 52.60  ? 37  PHE B O   1 
ATOM   3432 C  CB  . PHE B 2 39  ? 120.934 7.452   -17.902 1.00 48.95  ? 37  PHE B CB  1 
ATOM   3433 C  CG  . PHE B 2 39  ? 120.112 6.364   -17.258 1.00 53.57  ? 37  PHE B CG  1 
ATOM   3434 C  CD1 . PHE B 2 39  ? 120.682 5.477   -16.357 1.00 51.15  ? 37  PHE B CD1 1 
ATOM   3435 C  CD2 . PHE B 2 39  ? 118.767 6.227   -17.564 1.00 50.36  ? 37  PHE B CD2 1 
ATOM   3436 C  CE1 . PHE B 2 39  ? 119.924 4.483   -15.768 1.00 50.47  ? 37  PHE B CE1 1 
ATOM   3437 C  CE2 . PHE B 2 39  ? 118.007 5.229   -16.985 1.00 51.48  ? 37  PHE B CE2 1 
ATOM   3438 C  CZ  . PHE B 2 39  ? 118.586 4.359   -16.084 1.00 52.52  ? 37  PHE B CZ  1 
ATOM   3439 N  N   . ARG B 2 40  ? 121.748 8.829   -20.579 1.00 51.08  ? 38  ARG B N   1 
ATOM   3440 C  CA  . ARG B 2 40  ? 122.253 10.018  -21.247 1.00 51.07  ? 38  ARG B CA  1 
ATOM   3441 C  C   . ARG B 2 40  ? 121.165 11.079  -21.276 1.00 57.55  ? 38  ARG B C   1 
ATOM   3442 O  O   . ARG B 2 40  ? 119.970 10.769  -21.231 1.00 60.47  ? 38  ARG B O   1 
ATOM   3443 C  CB  . ARG B 2 40  ? 122.750 9.708   -22.669 1.00 53.32  ? 38  ARG B CB  1 
ATOM   3444 C  CG  . ARG B 2 40  ? 121.670 9.621   -23.731 1.00 57.04  ? 38  ARG B CG  1 
ATOM   3445 C  CD  . ARG B 2 40  ? 122.258 9.161   -25.062 1.00 58.20  ? 38  ARG B CD  1 
ATOM   3446 N  NE  . ARG B 2 40  ? 121.232 8.715   -25.996 1.00 61.59  ? 38  ARG B NE  1 
ATOM   3447 C  CZ  . ARG B 2 40  ? 121.477 8.212   -27.199 1.00 67.71  ? 38  ARG B CZ  1 
ATOM   3448 N  NH1 . ARG B 2 40  ? 122.714 8.066   -27.651 1.00 67.08  ? 38  ARG B NH1 1 
ATOM   3449 N  NH2 . ARG B 2 40  ? 120.457 7.849   -27.972 1.00 70.69  ? 38  ARG B NH2 1 
ATOM   3450 N  N   . GLN B 2 41  ? 121.595 12.339  -21.330 1.00 51.88  ? 39  GLN B N   1 
ATOM   3451 C  CA  . GLN B 2 41  ? 120.685 13.482  -21.324 1.00 61.33  ? 39  GLN B CA  1 
ATOM   3452 C  C   . GLN B 2 41  ? 121.210 14.509  -22.315 1.00 61.73  ? 39  GLN B C   1 
ATOM   3453 O  O   . GLN B 2 41  ? 122.264 15.110  -22.087 1.00 61.58  ? 39  GLN B O   1 
ATOM   3454 C  CB  . GLN B 2 41  ? 120.559 14.087  -19.924 1.00 62.00  ? 39  GLN B CB  1 
ATOM   3455 C  CG  . GLN B 2 41  ? 119.791 15.406  -19.885 1.00 65.32  ? 39  GLN B CG  1 
ATOM   3456 C  CD  . GLN B 2 41  ? 119.013 15.605  -18.596 1.00 66.02  ? 39  GLN B CD  1 
ATOM   3457 O  OE1 . GLN B 2 41  ? 119.519 15.343  -17.505 1.00 73.77  ? 39  GLN B OE1 1 
ATOM   3458 N  NE2 . GLN B 2 41  ? 117.779 16.079  -18.716 1.00 68.97  ? 39  GLN B NE2 1 
ATOM   3459 N  N   . ALA B 2 42  ? 120.484 14.704  -23.407 1.00 68.42  ? 40  ALA B N   1 
ATOM   3460 C  CA  . ALA B 2 42  ? 120.871 15.657  -24.435 1.00 79.66  ? 40  ALA B CA  1 
ATOM   3461 C  C   . ALA B 2 42  ? 120.352 17.046  -24.097 1.00 87.06  ? 40  ALA B C   1 
ATOM   3462 O  O   . ALA B 2 42  ? 119.368 17.191  -23.367 1.00 83.64  ? 40  ALA B O   1 
ATOM   3463 C  CB  . ALA B 2 42  ? 120.331 15.209  -25.792 1.00 80.50  ? 40  ALA B CB  1 
ATOM   3464 N  N   . PRO B 2 43  ? 121.004 18.098  -24.604 1.00 110.81 ? 41  PRO B N   1 
ATOM   3465 C  CA  . PRO B 2 43  ? 120.534 19.461  -24.319 1.00 113.67 ? 41  PRO B CA  1 
ATOM   3466 C  C   . PRO B 2 43  ? 119.148 19.731  -24.883 1.00 115.10 ? 41  PRO B C   1 
ATOM   3467 O  O   . PRO B 2 43  ? 118.963 19.798  -26.103 1.00 117.63 ? 41  PRO B O   1 
ATOM   3468 C  CB  . PRO B 2 43  ? 121.595 20.348  -24.988 1.00 116.37 ? 41  PRO B CB  1 
ATOM   3469 C  CG  . PRO B 2 43  ? 122.261 19.464  -25.995 1.00 116.12 ? 41  PRO B CG  1 
ATOM   3470 C  CD  . PRO B 2 43  ? 122.249 18.097  -25.390 1.00 112.05 ? 41  PRO B CD  1 
ATOM   3471 N  N   . GLY B 2 44  ? 118.165 19.884  -23.999 1.00 87.39  ? 42  GLY B N   1 
ATOM   3472 C  CA  . GLY B 2 44  ? 116.790 20.117  -24.389 1.00 76.47  ? 42  GLY B CA  1 
ATOM   3473 C  C   . GLY B 2 44  ? 115.850 18.970  -24.096 1.00 73.41  ? 42  GLY B C   1 
ATOM   3474 O  O   . GLY B 2 44  ? 114.632 19.149  -24.217 1.00 74.67  ? 42  GLY B O   1 
ATOM   3475 N  N   . LYS B 2 45  ? 116.364 17.805  -23.721 1.00 77.98  ? 43  LYS B N   1 
ATOM   3476 C  CA  . LYS B 2 45  ? 115.549 16.635  -23.419 1.00 69.27  ? 43  LYS B CA  1 
ATOM   3477 C  C   . LYS B 2 45  ? 115.837 16.158  -21.996 1.00 69.16  ? 43  LYS B C   1 
ATOM   3478 O  O   . LYS B 2 45  ? 116.605 16.771  -21.253 1.00 72.95  ? 43  LYS B O   1 
ATOM   3479 C  CB  . LYS B 2 45  ? 115.799 15.523  -24.442 1.00 73.24  ? 43  LYS B CB  1 
ATOM   3480 C  CG  . LYS B 2 45  ? 116.177 16.029  -25.829 1.00 74.78  ? 43  LYS B CG  1 
ATOM   3481 C  CD  . LYS B 2 45  ? 116.896 14.962  -26.641 1.00 77.72  ? 43  LYS B CD  1 
ATOM   3482 C  CE  . LYS B 2 45  ? 116.076 13.685  -26.731 1.00 81.95  ? 43  LYS B CE  1 
ATOM   3483 N  NZ  . LYS B 2 45  ? 114.902 13.835  -27.636 1.00 73.13  ? 43  LYS B NZ  1 
ATOM   3484 N  N   . GLU B 2 46  ? 115.201 15.051  -21.619 1.00 73.41  ? 44  GLU B N   1 
ATOM   3485 C  CA  . GLU B 2 46  ? 115.333 14.484  -20.287 1.00 65.93  ? 44  GLU B CA  1 
ATOM   3486 C  C   . GLU B 2 46  ? 116.260 13.270  -20.319 1.00 65.83  ? 44  GLU B C   1 
ATOM   3487 O  O   . GLU B 2 46  ? 116.740 12.843  -21.371 1.00 60.69  ? 44  GLU B O   1 
ATOM   3488 C  CB  . GLU B 2 46  ? 113.957 14.118  -19.723 1.00 77.70  ? 44  GLU B CB  1 
ATOM   3489 C  CG  . GLU B 2 46  ? 113.044 13.389  -20.704 1.00 79.27  ? 44  GLU B CG  1 
ATOM   3490 C  CD  . GLU B 2 46  ? 111.597 13.327  -20.228 1.00 94.14  ? 44  GLU B CD  1 
ATOM   3491 O  OE1 . GLU B 2 46  ? 111.369 13.348  -19.000 1.00 85.60  ? 44  GLU B OE1 1 
ATOM   3492 O  OE2 . GLU B 2 46  ? 110.687 13.253  -21.083 1.00 96.91  ? 44  GLU B OE2 1 
ATOM   3493 N  N   . ARG B 2 47  ? 116.518 12.710  -19.139 1.00 66.32  ? 45  ARG B N   1 
ATOM   3494 C  CA  . ARG B 2 47  ? 117.385 11.544  -19.026 1.00 64.34  ? 45  ARG B CA  1 
ATOM   3495 C  C   . ARG B 2 47  ? 116.739 10.351  -19.721 1.00 68.36  ? 45  ARG B C   1 
ATOM   3496 O  O   . ARG B 2 47  ? 115.606 9.978   -19.400 1.00 70.58  ? 45  ARG B O   1 
ATOM   3497 C  CB  . ARG B 2 47  ? 117.653 11.226  -17.557 1.00 57.11  ? 45  ARG B CB  1 
ATOM   3498 C  CG  . ARG B 2 47  ? 119.010 11.674  -17.046 1.00 57.68  ? 45  ARG B CG  1 
ATOM   3499 C  CD  . ARG B 2 47  ? 119.087 11.522  -15.538 1.00 61.57  ? 45  ARG B CD  1 
ATOM   3500 N  NE  . ARG B 2 47  ? 120.374 11.928  -14.986 1.00 64.54  ? 45  ARG B NE  1 
ATOM   3501 C  CZ  . ARG B 2 47  ? 120.576 12.226  -13.710 1.00 69.16  ? 45  ARG B CZ  1 
ATOM   3502 N  NH1 . ARG B 2 47  ? 119.586 12.204  -12.833 1.00 58.46  ? 45  ARG B NH1 1 
ATOM   3503 N  NH2 . ARG B 2 47  ? 121.802 12.550  -13.304 1.00 68.95  ? 45  ARG B NH2 1 
ATOM   3504 N  N   . GLU B 2 48  ? 117.453 9.761   -20.677 1.00 58.50  ? 46  GLU B N   1 
ATOM   3505 C  CA  . GLU B 2 48  ? 116.982 8.589   -21.395 1.00 55.44  ? 46  GLU B CA  1 
ATOM   3506 C  C   . GLU B 2 48  ? 117.914 7.413   -21.129 1.00 55.73  ? 46  GLU B C   1 
ATOM   3507 O  O   . GLU B 2 48  ? 119.115 7.585   -20.906 1.00 52.79  ? 46  GLU B O   1 
ATOM   3508 C  CB  . GLU B 2 48  ? 116.869 8.863   -22.910 1.00 61.03  ? 46  GLU B CB  1 
ATOM   3509 C  CG  . GLU B 2 48  ? 118.147 8.599   -23.708 1.00 68.54  ? 46  GLU B CG  1 
ATOM   3510 C  CD  . GLU B 2 48  ? 118.034 9.001   -25.177 1.00 76.93  ? 46  GLU B CD  1 
ATOM   3511 O  OE1 . GLU B 2 48  ? 118.116 10.212  -25.479 1.00 80.18  ? 46  GLU B OE1 1 
ATOM   3512 O  OE2 . GLU B 2 48  ? 117.878 8.103   -26.032 1.00 81.44  ? 46  GLU B OE2 1 
ATOM   3513 N  N   . PHE B 2 49  ? 117.337 6.216   -21.133 1.00 55.15  ? 47  PHE B N   1 
ATOM   3514 C  CA  . PHE B 2 49  ? 118.100 4.996   -20.912 1.00 52.75  ? 47  PHE B CA  1 
ATOM   3515 C  C   . PHE B 2 49  ? 119.016 4.713   -22.097 1.00 50.64  ? 47  PHE B C   1 
ATOM   3516 O  O   . PHE B 2 49  ? 118.668 4.966   -23.254 1.00 57.60  ? 47  PHE B O   1 
ATOM   3517 C  CB  . PHE B 2 49  ? 117.149 3.820   -20.693 1.00 47.68  ? 47  PHE B CB  1 
ATOM   3518 C  CG  . PHE B 2 49  ? 117.822 2.476   -20.671 1.00 46.76  ? 47  PHE B CG  1 
ATOM   3519 C  CD1 . PHE B 2 49  ? 118.323 1.965   -19.489 1.00 49.26  ? 47  PHE B CD1 1 
ATOM   3520 C  CD2 . PHE B 2 49  ? 117.919 1.706   -21.820 1.00 50.33  ? 47  PHE B CD2 1 
ATOM   3521 C  CE1 . PHE B 2 49  ? 118.924 0.726   -19.450 1.00 51.20  ? 47  PHE B CE1 1 
ATOM   3522 C  CE2 . PHE B 2 49  ? 118.517 0.459   -21.786 1.00 57.86  ? 47  PHE B CE2 1 
ATOM   3523 C  CZ  . PHE B 2 49  ? 119.022 -0.029  -20.597 1.00 54.08  ? 47  PHE B CZ  1 
ATOM   3524 N  N   . VAL B 2 50  ? 120.196 4.164   -21.797 1.00 52.33  ? 48  VAL B N   1 
ATOM   3525 C  CA  . VAL B 2 50  ? 121.181 3.814   -22.817 1.00 47.87  ? 48  VAL B CA  1 
ATOM   3526 C  C   . VAL B 2 50  ? 121.493 2.323   -22.757 1.00 53.57  ? 48  VAL B C   1 
ATOM   3527 O  O   . VAL B 2 50  ? 121.259 1.587   -23.723 1.00 49.39  ? 48  VAL B O   1 
ATOM   3528 C  CB  . VAL B 2 50  ? 122.465 4.645   -22.654 1.00 49.56  ? 48  VAL B CB  1 
ATOM   3529 C  CG1 . VAL B 2 50  ? 123.504 4.231   -23.688 1.00 49.21  ? 48  VAL B CG1 1 
ATOM   3530 C  CG2 . VAL B 2 50  ? 122.151 6.123   -22.765 1.00 56.28  ? 48  VAL B CG2 1 
ATOM   3531 N  N   . ALA B 2 51  ? 122.028 1.869   -21.627 1.00 52.68  ? 49  ALA B N   1 
ATOM   3532 C  CA  . ALA B 2 51  ? 122.397 0.471   -21.472 1.00 47.96  ? 49  ALA B CA  1 
ATOM   3533 C  C   . ALA B 2 51  ? 122.366 0.103   -19.997 1.00 54.39  ? 49  ALA B C   1 
ATOM   3534 O  O   . ALA B 2 51  ? 122.449 0.966   -19.119 1.00 54.78  ? 49  ALA B O   1 
ATOM   3535 C  CB  . ALA B 2 51  ? 123.778 0.182   -22.064 1.00 49.66  ? 49  ALA B CB  1 
ATOM   3536 N  N   . ARG B 2 52  ? 122.240 -1.197  -19.735 1.00 52.00  ? 50  ARG B N   1 
ATOM   3537 C  CA  . ARG B 2 52  ? 122.181 -1.699  -18.371 1.00 57.61  ? 50  ARG B CA  1 
ATOM   3538 C  C   . ARG B 2 52  ? 122.756 -3.105  -18.326 1.00 58.45  ? 50  ARG B C   1 
ATOM   3539 O  O   . ARG B 2 52  ? 122.464 -3.933  -19.191 1.00 56.19  ? 50  ARG B O   1 
ATOM   3540 C  CB  . ARG B 2 52  ? 120.746 -1.711  -17.827 1.00 56.94  ? 50  ARG B CB  1 
ATOM   3541 C  CG  . ARG B 2 52  ? 120.536 -2.669  -16.654 1.00 59.98  ? 50  ARG B CG  1 
ATOM   3542 C  CD  . ARG B 2 52  ? 119.115 -2.614  -16.116 1.00 58.72  ? 50  ARG B CD  1 
ATOM   3543 N  NE  . ARG B 2 52  ? 118.376 -3.828  -16.439 1.00 57.38  ? 50  ARG B NE  1 
ATOM   3544 C  CZ  . ARG B 2 52  ? 117.466 -3.913  -17.399 1.00 57.84  ? 50  ARG B CZ  1 
ATOM   3545 N  NH1 . ARG B 2 52  ? 117.127 -2.860  -18.125 1.00 52.35  ? 50  ARG B NH1 1 
ATOM   3546 N  NH2 . ARG B 2 52  ? 116.883 -5.085  -17.639 1.00 60.21  ? 50  ARG B NH2 1 
ATOM   3547 N  N   . ILE B 2 53  ? 123.577 -3.361  -17.315 1.00 54.31  ? 51  ILE B N   1 
ATOM   3548 C  CA  . ILE B 2 53  ? 124.098 -4.690  -17.039 1.00 62.61  ? 51  ILE B CA  1 
ATOM   3549 C  C   . ILE B 2 53  ? 123.626 -5.102  -15.651 1.00 70.47  ? 51  ILE B C   1 
ATOM   3550 O  O   . ILE B 2 53  ? 123.558 -4.276  -14.733 1.00 67.91  ? 51  ILE B O   1 
ATOM   3551 C  CB  . ILE B 2 53  ? 125.638 -4.739  -17.170 1.00 64.11  ? 51  ILE B CB  1 
ATOM   3552 C  CG1 . ILE B 2 53  ? 126.103 -6.145  -17.549 1.00 66.23  ? 51  ILE B CG1 1 
ATOM   3553 C  CG2 . ILE B 2 53  ? 126.334 -4.238  -15.912 1.00 70.21  ? 51  ILE B CG2 1 
ATOM   3554 C  CD1 . ILE B 2 53  ? 127.607 -6.295  -17.569 1.00 68.68  ? 51  ILE B CD1 1 
ATOM   3555 N  N   . SER B 2 54  ? 123.254 -6.369  -15.513 1.00 72.13  ? 52  SER B N   1 
ATOM   3556 C  CA  . SER B 2 54  ? 122.659 -6.833  -14.274 1.00 77.71  ? 52  SER B CA  1 
ATOM   3557 C  C   . SER B 2 54  ? 123.743 -7.145  -13.251 1.00 76.37  ? 52  SER B C   1 
ATOM   3558 O  O   . SER B 2 54  ? 124.944 -7.038  -13.517 1.00 72.73  ? 52  SER B O   1 
ATOM   3559 C  CB  . SER B 2 54  ? 121.785 -8.059  -14.522 1.00 80.07  ? 52  SER B CB  1 
ATOM   3560 O  OG  . SER B 2 54  ? 122.526 -9.247  -14.311 1.00 94.74  ? 52  SER B OG  1 
ATOM   3561 N  N   . GLU B 2 55  ? 123.304 -7.540  -12.061 1.00 77.57  ? 53  GLU B N   1 
ATOM   3562 C  CA  . GLU B 2 55  ? 124.211 -7.891  -10.980 1.00 83.56  ? 53  GLU B CA  1 
ATOM   3563 C  C   . GLU B 2 55  ? 124.411 -9.389  -10.834 1.00 85.33  ? 53  GLU B C   1 
ATOM   3564 O  O   . GLU B 2 55  ? 125.261 -9.812  -10.043 1.00 99.07  ? 53  GLU B O   1 
ATOM   3565 C  CB  . GLU B 2 55  ? 123.694 -7.317  -9.655  1.00 83.70  ? 53  GLU B CB  1 
ATOM   3566 C  CG  . GLU B 2 55  ? 122.647 -8.177  -8.954  1.00 81.04  ? 53  GLU B CG  1 
ATOM   3567 C  CD  . GLU B 2 55  ? 121.273 -8.062  -9.583  1.00 82.84  ? 53  GLU B CD  1 
ATOM   3568 O  OE1 . GLU B 2 55  ? 121.093 -7.188  -10.455 1.00 87.66  ? 53  GLU B OE1 1 
ATOM   3569 O  OE2 . GLU B 2 55  ? 120.372 -8.839  -9.202  1.00 81.62  ? 53  GLU B OE2 1 
ATOM   3570 N  N   . SER B 2 56  ? 123.662 -10.200 -11.583 1.00 84.49  ? 54  SER B N   1 
ATOM   3571 C  CA  . SER B 2 56  ? 123.667 -11.639 -11.377 1.00 95.91  ? 54  SER B CA  1 
ATOM   3572 C  C   . SER B 2 56  ? 124.220 -12.299 -12.627 1.00 100.21 ? 54  SER B C   1 
ATOM   3573 O  O   . SER B 2 56  ? 125.453 -12.441 -12.760 1.00 104.05 ? 54  SER B O   1 
ATOM   3574 C  CB  . SER B 2 56  ? 122.264 -12.134 -10.994 1.00 98.53  ? 54  SER B CB  1 
ATOM   3575 O  OG  . SER B 2 56  ? 121.345 -11.960 -12.054 1.00 102.58 ? 54  SER B OG  1 
ATOM   3576 N  N   . ARG B 2 57  ? 123.376 -12.715 -13.572 1.00 99.83  ? 55  ARG B N   1 
ATOM   3577 C  CA  . ARG B 2 57  ? 123.791 -13.484 -14.731 1.00 106.62 ? 55  ARG B CA  1 
ATOM   3578 C  C   . ARG B 2 57  ? 124.564 -12.667 -15.757 1.00 109.23 ? 55  ARG B C   1 
ATOM   3579 O  O   . ARG B 2 57  ? 124.902 -13.215 -16.811 1.00 112.94 ? 55  ARG B O   1 
ATOM   3580 C  CB  . ARG B 2 57  ? 122.558 -14.116 -15.376 1.00 106.48 ? 55  ARG B CB  1 
ATOM   3581 C  CG  . ARG B 2 57  ? 121.441 -14.429 -14.371 1.00 110.01 ? 55  ARG B CG  1 
ATOM   3582 C  CD  . ARG B 2 57  ? 120.070 -14.541 -15.038 1.00 115.67 ? 55  ARG B CD  1 
ATOM   3583 N  NE  . ARG B 2 57  ? 118.986 -14.197 -14.123 1.00 116.65 ? 55  ARG B NE  1 
ATOM   3584 C  CZ  . ARG B 2 57  ? 117.695 -14.305 -14.410 1.00 114.62 ? 55  ARG B CZ  1 
ATOM   3585 N  NH1 . ARG B 2 57  ? 117.282 -14.756 -15.584 1.00 117.26 ? 55  ARG B NH1 1 
ATOM   3586 N  NH2 . ARG B 2 57  ? 116.795 -13.955 -13.495 1.00 106.96 ? 55  ARG B NH2 1 
ATOM   3587 N  N   . GLY B 2 58  ? 124.848 -11.393 -15.492 1.00 121.26 ? 56  GLY B N   1 
ATOM   3588 C  CA  . GLY B 2 58  ? 125.513 -10.559 -16.473 1.00 114.63 ? 56  GLY B CA  1 
ATOM   3589 C  C   . GLY B 2 58  ? 124.659 -10.169 -17.659 1.00 112.50 ? 56  GLY B C   1 
ATOM   3590 O  O   . GLY B 2 58  ? 125.198 -9.841  -18.720 1.00 105.28 ? 56  GLY B O   1 
ATOM   3591 N  N   . THR B 2 59  ? 123.337 -10.201 -17.513 1.00 94.02  ? 57  THR B N   1 
ATOM   3592 C  CA  . THR B 2 59  ? 122.456 -9.849  -18.616 1.00 86.68  ? 57  THR B CA  1 
ATOM   3593 C  C   . THR B 2 59  ? 122.599 -8.373  -18.965 1.00 75.66  ? 57  THR B C   1 
ATOM   3594 O  O   . THR B 2 59  ? 122.961 -7.543  -18.128 1.00 75.02  ? 57  THR B O   1 
ATOM   3595 C  CB  . THR B 2 59  ? 121.002 -10.165 -18.267 1.00 83.43  ? 57  THR B CB  1 
ATOM   3596 O  OG1 . THR B 2 59  ? 120.773 -9.907  -16.877 1.00 88.12  ? 57  THR B OG1 1 
ATOM   3597 C  CG2 . THR B 2 59  ? 120.691 -11.623 -18.561 1.00 92.75  ? 57  THR B CG2 1 
ATOM   3598 N  N   . THR B 2 60  ? 122.315 -8.050  -20.222 1.00 70.82  ? 58  THR B N   1 
ATOM   3599 C  CA  . THR B 2 60  ? 122.455 -6.691  -20.716 1.00 64.99  ? 58  THR B CA  1 
ATOM   3600 C  C   . THR B 2 60  ? 121.150 -6.238  -21.352 1.00 70.20  ? 58  THR B C   1 
ATOM   3601 O  O   . THR B 2 60  ? 120.357 -7.050  -21.838 1.00 70.35  ? 58  THR B O   1 
ATOM   3602 C  CB  . THR B 2 60  ? 123.603 -6.572  -21.730 1.00 69.20  ? 58  THR B CB  1 
ATOM   3603 O  OG1 . THR B 2 60  ? 123.658 -7.754  -22.536 1.00 78.75  ? 58  THR B OG1 1 
ATOM   3604 C  CG2 . THR B 2 60  ? 124.931 -6.402  -21.010 1.00 62.72  ? 58  THR B CG2 1 
ATOM   3605 N  N   . ASP B 2 61  ? 120.930 -4.926  -21.325 1.00 63.03  ? 59  ASP B N   1 
ATOM   3606 C  CA  . ASP B 2 61  ? 119.782 -4.300  -21.961 1.00 58.37  ? 59  ASP B CA  1 
ATOM   3607 C  C   . ASP B 2 61  ? 120.256 -3.027  -22.642 1.00 60.41  ? 59  ASP B C   1 
ATOM   3608 O  O   . ASP B 2 61  ? 121.104 -2.310  -22.104 1.00 55.44  ? 59  ASP B O   1 
ATOM   3609 C  CB  . ASP B 2 61  ? 118.675 -3.987  -20.946 1.00 62.98  ? 59  ASP B CB  1 
ATOM   3610 C  CG  . ASP B 2 61  ? 117.323 -3.762  -21.601 1.00 66.25  ? 59  ASP B CG  1 
ATOM   3611 O  OD1 . ASP B 2 61  ? 117.066 -4.355  -22.671 1.00 69.97  ? 59  ASP B OD1 1 
ATOM   3612 O  OD2 . ASP B 2 61  ? 116.515 -2.990  -21.039 1.00 66.26  ? 59  ASP B OD2 1 
ATOM   3613 N  N   . TYR B 2 62  ? 119.716 -2.757  -23.830 1.00 60.00  ? 60  TYR B N   1 
ATOM   3614 C  CA  . TYR B 2 62  ? 120.128 -1.611  -24.627 1.00 55.61  ? 60  TYR B CA  1 
ATOM   3615 C  C   . TYR B 2 62  ? 118.905 -0.926  -25.214 1.00 59.68  ? 60  TYR B C   1 
ATOM   3616 O  O   . TYR B 2 62  ? 117.966 -1.592  -25.661 1.00 55.36  ? 60  TYR B O   1 
ATOM   3617 C  CB  . TYR B 2 62  ? 121.069 -2.025  -25.767 1.00 57.33  ? 60  TYR B CB  1 
ATOM   3618 C  CG  . TYR B 2 62  ? 122.320 -2.739  -25.319 1.00 56.45  ? 60  TYR B CG  1 
ATOM   3619 C  CD1 . TYR B 2 62  ? 123.465 -2.031  -24.991 1.00 48.94  ? 60  TYR B CD1 1 
ATOM   3620 C  CD2 . TYR B 2 62  ? 122.354 -4.124  -25.224 1.00 63.02  ? 60  TYR B CD2 1 
ATOM   3621 C  CE1 . TYR B 2 62  ? 124.612 -2.683  -24.581 1.00 61.78  ? 60  TYR B CE1 1 
ATOM   3622 C  CE2 . TYR B 2 62  ? 123.496 -4.787  -24.813 1.00 57.64  ? 60  TYR B CE2 1 
ATOM   3623 C  CZ  . TYR B 2 62  ? 124.624 -4.063  -24.491 1.00 64.24  ? 60  TYR B CZ  1 
ATOM   3624 O  OH  . TYR B 2 62  ? 125.769 -4.718  -24.084 1.00 65.53  ? 60  TYR B OH  1 
ATOM   3625 N  N   . ALA B 2 63  ? 118.920 0.404   -25.209 1.00 60.88  ? 61  ALA B N   1 
ATOM   3626 C  CA  . ALA B 2 63  ? 117.932 1.146   -25.976 1.00 55.21  ? 61  ALA B CA  1 
ATOM   3627 C  C   . ALA B 2 63  ? 118.091 0.827   -27.459 1.00 62.62  ? 61  ALA B C   1 
ATOM   3628 O  O   . ALA B 2 63  ? 119.197 0.574   -27.948 1.00 68.12  ? 61  ALA B O   1 
ATOM   3629 C  CB  . ALA B 2 63  ? 118.081 2.647   -25.733 1.00 49.30  ? 61  ALA B CB  1 
ATOM   3630 N  N   . ASP B 2 64  ? 116.965 0.828   -28.176 1.00 62.93  ? 62  ASP B N   1 
ATOM   3631 C  CA  . ASP B 2 64  ? 116.973 0.464   -29.590 1.00 65.16  ? 62  ASP B CA  1 
ATOM   3632 C  C   . ASP B 2 64  ? 117.847 1.385   -30.427 1.00 70.47  ? 62  ASP B C   1 
ATOM   3633 O  O   . ASP B 2 64  ? 118.257 0.999   -31.526 1.00 78.89  ? 62  ASP B O   1 
ATOM   3634 C  CB  . ASP B 2 64  ? 115.548 0.470   -30.141 1.00 67.02  ? 62  ASP B CB  1 
ATOM   3635 C  CG  . ASP B 2 64  ? 114.752 -0.731  -29.692 1.00 71.00  ? 62  ASP B CG  1 
ATOM   3636 O  OD1 . ASP B 2 64  ? 113.572 -0.850  -30.083 1.00 65.77  ? 62  ASP B OD1 1 
ATOM   3637 O  OD2 . ASP B 2 64  ? 115.314 -1.560  -28.946 1.00 78.57  ? 62  ASP B OD2 1 
ATOM   3638 N  N   . SER B 2 65  ? 118.143 2.589   -29.937 1.00 67.98  ? 63  SER B N   1 
ATOM   3639 C  CA  . SER B 2 65  ? 118.966 3.516   -30.698 1.00 76.83  ? 63  SER B CA  1 
ATOM   3640 C  C   . SER B 2 65  ? 120.444 3.179   -30.639 1.00 67.60  ? 63  SER B C   1 
ATOM   3641 O  O   . SER B 2 65  ? 121.198 3.612   -31.517 1.00 70.60  ? 63  SER B O   1 
ATOM   3642 C  CB  . SER B 2 65  ? 118.745 4.949   -30.211 1.00 77.19  ? 63  SER B CB  1 
ATOM   3643 O  OG  . SER B 2 65  ? 118.863 5.029   -28.805 1.00 73.56  ? 63  SER B OG  1 
ATOM   3644 N  N   . VAL B 2 66  ? 120.872 2.422   -29.633 1.00 63.02  ? 64  VAL B N   1 
ATOM   3645 C  CA  . VAL B 2 66  ? 122.274 2.079   -29.458 1.00 65.20  ? 64  VAL B CA  1 
ATOM   3646 C  C   . VAL B 2 66  ? 122.536 0.588   -29.584 1.00 68.01  ? 64  VAL B C   1 
ATOM   3647 O  O   . VAL B 2 66  ? 123.693 0.165   -29.472 1.00 72.73  ? 64  VAL B O   1 
ATOM   3648 C  CB  . VAL B 2 66  ? 122.813 2.603   -28.112 1.00 67.10  ? 64  VAL B CB  1 
ATOM   3649 C  CG1 . VAL B 2 66  ? 122.362 4.041   -27.881 1.00 66.39  ? 64  VAL B CG1 1 
ATOM   3650 C  CG2 . VAL B 2 66  ? 122.355 1.706   -26.971 1.00 58.52  ? 64  VAL B CG2 1 
ATOM   3651 N  N   . LYS B 2 67  ? 121.507 -0.223  -29.822 1.00 74.74  ? 65  LYS B N   1 
ATOM   3652 C  CA  . LYS B 2 67  ? 121.715 -1.659  -29.956 1.00 77.69  ? 65  LYS B CA  1 
ATOM   3653 C  C   . LYS B 2 67  ? 122.546 -1.960  -31.197 1.00 75.79  ? 65  LYS B C   1 
ATOM   3654 O  O   . LYS B 2 67  ? 122.322 -1.388  -32.266 1.00 77.52  ? 65  LYS B O   1 
ATOM   3655 C  CB  . LYS B 2 67  ? 120.368 -2.386  -30.015 1.00 79.91  ? 65  LYS B CB  1 
ATOM   3656 C  CG  . LYS B 2 67  ? 119.469 -1.953  -31.160 1.00 88.93  ? 65  LYS B CG  1 
ATOM   3657 C  CD  . LYS B 2 67  ? 118.329 -2.932  -31.378 1.00 93.47  ? 65  LYS B CD  1 
ATOM   3658 C  CE  . LYS B 2 67  ? 117.772 -2.800  -32.787 1.00 94.08  ? 65  LYS B CE  1 
ATOM   3659 N  NZ  . LYS B 2 67  ? 116.592 -3.680  -33.004 1.00 106.80 ? 65  LYS B NZ  1 
ATOM   3660 N  N   . GLY B 2 68  ? 123.527 -2.842  -31.045 1.00 69.28  ? 66  GLY B N   1 
ATOM   3661 C  CA  . GLY B 2 68  ? 124.480 -3.134  -32.092 1.00 76.33  ? 66  GLY B CA  1 
ATOM   3662 C  C   . GLY B 2 68  ? 125.629 -2.148  -32.185 1.00 61.53  ? 66  GLY B C   1 
ATOM   3663 O  O   . GLY B 2 68  ? 126.733 -2.533  -32.582 1.00 72.57  ? 66  GLY B O   1 
ATOM   3664 N  N   . ARG B 2 69  ? 125.398 -0.888  -31.821 1.00 69.43  ? 67  ARG B N   1 
ATOM   3665 C  CA  . ARG B 2 69  ? 126.454 0.119   -31.837 1.00 64.90  ? 67  ARG B CA  1 
ATOM   3666 C  C   . ARG B 2 69  ? 127.157 0.237   -30.492 1.00 67.91  ? 67  ARG B C   1 
ATOM   3667 O  O   . ARG B 2 69  ? 128.385 0.372   -30.443 1.00 69.58  ? 67  ARG B O   1 
ATOM   3668 C  CB  . ARG B 2 69  ? 125.885 1.484   -32.235 1.00 64.84  ? 67  ARG B CB  1 
ATOM   3669 C  CG  . ARG B 2 69  ? 125.201 1.504   -33.592 1.00 65.44  ? 67  ARG B CG  1 
ATOM   3670 C  CD  . ARG B 2 69  ? 124.881 2.924   -34.033 1.00 69.75  ? 67  ARG B CD  1 
ATOM   3671 N  NE  . ARG B 2 69  ? 123.895 3.560   -33.167 1.00 71.12  ? 67  ARG B NE  1 
ATOM   3672 C  CZ  . ARG B 2 69  ? 124.144 4.620   -32.412 1.00 67.06  ? 67  ARG B CZ  1 
ATOM   3673 N  NH1 . ARG B 2 69  ? 125.344 5.176   -32.377 1.00 64.51  ? 67  ARG B NH1 1 
ATOM   3674 N  NH2 . ARG B 2 69  ? 123.165 5.137   -31.674 1.00 64.45  ? 67  ARG B NH2 1 
ATOM   3675 N  N   . PHE B 2 70  ? 126.399 0.186   -29.400 1.00 63.79  ? 68  PHE B N   1 
ATOM   3676 C  CA  . PHE B 2 70  ? 126.936 0.349   -28.058 1.00 62.36  ? 68  PHE B CA  1 
ATOM   3677 C  C   . PHE B 2 70  ? 126.969 -0.998  -27.347 1.00 65.34  ? 68  PHE B C   1 
ATOM   3678 O  O   . PHE B 2 70  ? 126.091 -1.842  -27.543 1.00 69.26  ? 68  PHE B O   1 
ATOM   3679 C  CB  . PHE B 2 70  ? 126.103 1.337   -27.233 1.00 62.61  ? 68  PHE B CB  1 
ATOM   3680 C  CG  . PHE B 2 70  ? 126.237 2.777   -27.663 1.00 64.11  ? 68  PHE B CG  1 
ATOM   3681 C  CD1 . PHE B 2 70  ? 126.602 3.112   -28.957 1.00 57.59  ? 68  PHE B CD1 1 
ATOM   3682 C  CD2 . PHE B 2 70  ? 125.980 3.800   -26.764 1.00 62.60  ? 68  PHE B CD2 1 
ATOM   3683 C  CE1 . PHE B 2 70  ? 126.712 4.432   -29.346 1.00 59.63  ? 68  PHE B CE1 1 
ATOM   3684 C  CE2 . PHE B 2 70  ? 126.090 5.125   -27.147 1.00 58.93  ? 68  PHE B CE2 1 
ATOM   3685 C  CZ  . PHE B 2 70  ? 126.457 5.441   -28.439 1.00 59.84  ? 68  PHE B CZ  1 
ATOM   3686 N  N   . THR B 2 71  ? 127.987 -1.188  -26.510 1.00 60.11  ? 69  THR B N   1 
ATOM   3687 C  CA  . THR B 2 71  ? 128.135 -2.414  -25.732 1.00 58.26  ? 69  THR B CA  1 
ATOM   3688 C  C   . THR B 2 71  ? 128.547 -2.051  -24.315 1.00 54.89  ? 69  THR B C   1 
ATOM   3689 O  O   . THR B 2 71  ? 129.563 -1.380  -24.117 1.00 64.18  ? 69  THR B O   1 
ATOM   3690 C  CB  . THR B 2 71  ? 129.169 -3.352  -26.362 1.00 62.59  ? 69  THR B CB  1 
ATOM   3691 O  OG1 . THR B 2 71  ? 128.640 -3.903  -27.574 1.00 69.11  ? 69  THR B OG1 1 
ATOM   3692 C  CG2 . THR B 2 71  ? 129.512 -4.481  -25.407 1.00 60.00  ? 69  THR B CG2 1 
ATOM   3693 N  N   . ILE B 2 72  ? 127.766 -2.496  -23.335 1.00 61.68  ? 70  ILE B N   1 
ATOM   3694 C  CA  . ILE B 2 72  ? 128.066 -2.269  -21.925 1.00 63.32  ? 70  ILE B CA  1 
ATOM   3695 C  C   . ILE B 2 72  ? 128.665 -3.542  -21.345 1.00 63.75  ? 70  ILE B C   1 
ATOM   3696 O  O   . ILE B 2 72  ? 128.257 -4.657  -21.699 1.00 69.33  ? 70  ILE B O   1 
ATOM   3697 C  CB  . ILE B 2 72  ? 126.810 -1.835  -21.141 1.00 57.56  ? 70  ILE B CB  1 
ATOM   3698 C  CG1 . ILE B 2 72  ? 127.152 -1.582  -19.671 1.00 57.99  ? 70  ILE B CG1 1 
ATOM   3699 C  CG2 . ILE B 2 72  ? 125.716 -2.881  -21.246 1.00 57.39  ? 70  ILE B CG2 1 
ATOM   3700 C  CD1 . ILE B 2 72  ? 125.955 -1.375  -18.783 1.00 49.86  ? 70  ILE B CD1 1 
ATOM   3701 N  N   . SER B 2 73  ? 129.647 -3.378  -20.462 1.00 65.64  ? 71  SER B N   1 
ATOM   3702 C  CA  . SER B 2 73  ? 130.298 -4.491  -19.790 1.00 67.74  ? 71  SER B CA  1 
ATOM   3703 C  C   . SER B 2 73  ? 130.675 -4.055  -18.384 1.00 68.78  ? 71  SER B C   1 
ATOM   3704 O  O   . SER B 2 73  ? 130.706 -2.863  -18.071 1.00 69.98  ? 71  SER B O   1 
ATOM   3705 C  CB  . SER B 2 73  ? 131.545 -4.963  -20.550 1.00 74.53  ? 71  SER B CB  1 
ATOM   3706 O  OG  . SER B 2 73  ? 132.620 -4.054  -20.377 1.00 71.92  ? 71  SER B OG  1 
ATOM   3707 N  N   . ARG B 2 74  ? 130.968 -5.034  -17.532 1.00 70.87  ? 72  ARG B N   1 
ATOM   3708 C  CA  . ARG B 2 74  ? 131.338 -4.750  -16.156 1.00 72.51  ? 72  ARG B CA  1 
ATOM   3709 C  C   . ARG B 2 74  ? 132.471 -5.669  -15.727 1.00 78.56  ? 72  ARG B C   1 
ATOM   3710 O  O   . ARG B 2 74  ? 132.651 -6.760  -16.272 1.00 80.55  ? 72  ARG B O   1 
ATOM   3711 C  CB  . ARG B 2 74  ? 130.137 -4.898  -15.214 1.00 69.51  ? 72  ARG B CB  1 
ATOM   3712 C  CG  . ARG B 2 74  ? 129.930 -6.290  -14.653 1.00 74.51  ? 72  ARG B CG  1 
ATOM   3713 C  CD  . ARG B 2 74  ? 128.561 -6.409  -13.987 1.00 75.00  ? 72  ARG B CD  1 
ATOM   3714 N  NE  . ARG B 2 74  ? 128.566 -5.891  -12.624 1.00 77.83  ? 72  ARG B NE  1 
ATOM   3715 C  CZ  . ARG B 2 74  ? 127.501 -5.402  -12.003 1.00 74.49  ? 72  ARG B CZ  1 
ATOM   3716 N  NH1 . ARG B 2 74  ? 126.322 -5.339  -12.599 1.00 70.20  ? 72  ARG B NH1 1 
ATOM   3717 N  NH2 . ARG B 2 74  ? 127.622 -4.967  -10.751 1.00 71.89  ? 72  ARG B NH2 1 
ATOM   3718 N  N   . ASP B 2 75  ? 133.247 -5.203  -14.752 1.00 76.73  ? 73  ASP B N   1 
ATOM   3719 C  CA  . ASP B 2 75  ? 134.317 -5.990  -14.149 1.00 83.33  ? 73  ASP B CA  1 
ATOM   3720 C  C   . ASP B 2 75  ? 134.193 -5.876  -12.638 1.00 82.30  ? 73  ASP B C   1 
ATOM   3721 O  O   . ASP B 2 75  ? 134.522 -4.834  -12.061 1.00 82.75  ? 73  ASP B O   1 
ATOM   3722 C  CB  . ASP B 2 75  ? 135.693 -5.522  -14.616 1.00 83.24  ? 73  ASP B CB  1 
ATOM   3723 C  CG  . ASP B 2 75  ? 136.816 -6.161  -13.826 1.00 98.77  ? 73  ASP B CG  1 
ATOM   3724 O  OD1 . ASP B 2 75  ? 137.268 -7.259  -14.216 1.00 106.68 ? 73  ASP B OD1 1 
ATOM   3725 O  OD2 . ASP B 2 75  ? 137.241 -5.572  -12.809 1.00 97.62  ? 73  ASP B OD2 1 
ATOM   3726 N  N   . ASN B 2 76  ? 133.722 -6.944  -12.000 1.00 84.09  ? 74  ASN B N   1 
ATOM   3727 C  CA  . ASN B 2 76  ? 133.555 -6.945  -10.554 1.00 85.25  ? 74  ASN B CA  1 
ATOM   3728 C  C   . ASN B 2 76  ? 134.875 -7.062  -9.805  1.00 93.41  ? 74  ASN B C   1 
ATOM   3729 O  O   . ASN B 2 76  ? 134.876 -6.972  -8.572  1.00 97.02  ? 74  ASN B O   1 
ATOM   3730 C  CB  . ASN B 2 76  ? 132.615 -8.078  -10.138 1.00 82.36  ? 74  ASN B CB  1 
ATOM   3731 C  CG  . ASN B 2 76  ? 131.179 -7.823  -10.558 1.00 83.21  ? 74  ASN B CG  1 
ATOM   3732 O  OD1 . ASN B 2 76  ? 130.714 -6.683  -10.555 1.00 77.88  ? 74  ASN B OD1 1 
ATOM   3733 N  ND2 . ASN B 2 76  ? 130.468 -8.884  -10.921 1.00 82.54  ? 74  ASN B ND2 1 
ATOM   3734 N  N   . ALA B 2 77  ? 135.990 -7.262  -10.512 1.00 92.32  ? 75  ALA B N   1 
ATOM   3735 C  CA  . ALA B 2 77  ? 137.288 -7.289  -9.849  1.00 96.14  ? 75  ALA B CA  1 
ATOM   3736 C  C   . ALA B 2 77  ? 137.716 -5.890  -9.423  1.00 96.63  ? 75  ALA B C   1 
ATOM   3737 O  O   . ALA B 2 77  ? 138.209 -5.697  -8.306  1.00 95.61  ? 75  ALA B O   1 
ATOM   3738 C  CB  . ALA B 2 77  ? 138.335 -7.918  -10.769 1.00 93.82  ? 75  ALA B CB  1 
ATOM   3739 N  N   . LYS B 2 78  ? 137.529 -4.903  -10.297 1.00 94.91  ? 76  LYS B N   1 
ATOM   3740 C  CA  . LYS B 2 78  ? 137.867 -3.519  -10.000 1.00 97.09  ? 76  LYS B CA  1 
ATOM   3741 C  C   . LYS B 2 78  ? 136.645 -2.655  -9.728  1.00 90.32  ? 76  LYS B C   1 
ATOM   3742 O  O   . LYS B 2 78  ? 136.797 -1.452  -9.493  1.00 89.76  ? 76  LYS B O   1 
ATOM   3743 C  CB  . LYS B 2 78  ? 138.679 -2.916  -11.152 1.00 96.81  ? 76  LYS B CB  1 
ATOM   3744 C  CG  . LYS B 2 78  ? 139.723 -3.853  -11.732 1.00 103.84 ? 76  LYS B CG  1 
ATOM   3745 C  CD  . LYS B 2 78  ? 140.567 -3.155  -12.788 1.00 114.16 ? 76  LYS B CD  1 
ATOM   3746 C  CE  . LYS B 2 78  ? 139.764 -2.893  -14.053 1.00 108.57 ? 76  LYS B CE  1 
ATOM   3747 N  NZ  . LYS B 2 78  ? 139.516 -4.145  -14.822 1.00 107.47 ? 76  LYS B NZ  1 
ATOM   3748 N  N   . ASN B 2 79  ? 135.443 -3.235  -9.750  1.00 88.60  ? 77  ASN B N   1 
ATOM   3749 C  CA  . ASN B 2 79  ? 134.197 -2.502  -9.517  1.00 88.73  ? 77  ASN B CA  1 
ATOM   3750 C  C   . ASN B 2 79  ? 134.032 -1.352  -10.512 1.00 85.38  ? 77  ASN B C   1 
ATOM   3751 O  O   . ASN B 2 79  ? 133.726 -0.216  -10.145 1.00 79.17  ? 77  ASN B O   1 
ATOM   3752 C  CB  . ASN B 2 79  ? 134.101 -1.994  -8.073  1.00 86.39  ? 77  ASN B CB  1 
ATOM   3753 C  CG  . ASN B 2 79  ? 134.381 -3.076  -7.045  1.00 93.31  ? 77  ASN B CG  1 
ATOM   3754 O  OD1 . ASN B 2 79  ? 134.519 -4.253  -7.379  1.00 93.96  ? 77  ASN B OD1 1 
ATOM   3755 N  ND2 . ASN B 2 79  ? 134.439 -2.679  -5.779  1.00 95.80  ? 77  ASN B ND2 1 
ATOM   3756 N  N   . THR B 2 80  ? 134.240 -1.657  -11.789 1.00 79.15  ? 78  THR B N   1 
ATOM   3757 C  CA  . THR B 2 80  ? 134.062 -0.680  -12.850 1.00 80.20  ? 78  THR B CA  1 
ATOM   3758 C  C   . THR B 2 80  ? 133.138 -1.245  -13.920 1.00 75.94  ? 78  THR B C   1 
ATOM   3759 O  O   . THR B 2 80  ? 132.989 -2.460  -14.070 1.00 78.58  ? 78  THR B O   1 
ATOM   3760 C  CB  . THR B 2 80  ? 135.396 -0.271  -13.493 1.00 81.20  ? 78  THR B CB  1 
ATOM   3761 O  OG1 . THR B 2 80  ? 135.702 -1.173  -14.562 1.00 87.18  ? 78  THR B OG1 1 
ATOM   3762 C  CG2 . THR B 2 80  ? 136.525 -0.290  -12.476 1.00 86.83  ? 78  THR B CG2 1 
ATOM   3763 N  N   . ILE B 2 81  ? 132.513 -0.336  -14.662 1.00 74.20  ? 79  ILE B N   1 
ATOM   3764 C  CA  . ILE B 2 81  ? 131.671 -0.678  -15.799 1.00 71.74  ? 79  ILE B CA  1 
ATOM   3765 C  C   . ILE B 2 81  ? 132.078 0.201   -16.969 1.00 69.82  ? 79  ILE B C   1 
ATOM   3766 O  O   . ILE B 2 81  ? 132.573 1.318   -16.789 1.00 66.96  ? 79  ILE B O   1 
ATOM   3767 C  CB  . ILE B 2 81  ? 130.166 -0.528  -15.474 1.00 67.23  ? 79  ILE B CB  1 
ATOM   3768 C  CG1 . ILE B 2 81  ? 129.827 0.918   -15.123 1.00 70.55  ? 79  ILE B CG1 1 
ATOM   3769 C  CG2 . ILE B 2 81  ? 129.760 -1.438  -14.341 1.00 74.05  ? 79  ILE B CG2 1 
ATOM   3770 C  CD1 . ILE B 2 81  ? 128.963 1.585   -16.131 1.00 66.88  ? 79  ILE B CD1 1 
ATOM   3771 N  N   . TYR B 2 82  ? 131.882 -0.317  -18.176 1.00 68.68  ? 80  TYR B N   1 
ATOM   3772 C  CA  . TYR B 2 82  ? 132.351 0.340   -19.384 1.00 68.10  ? 80  TYR B CA  1 
ATOM   3773 C  C   . TYR B 2 82  ? 131.222 0.442   -20.394 1.00 66.77  ? 80  TYR B C   1 
ATOM   3774 O  O   . TYR B 2 82  ? 130.256 -0.326  -20.364 1.00 66.85  ? 80  TYR B O   1 
ATOM   3775 C  CB  . TYR B 2 82  ? 133.524 -0.411  -20.019 1.00 72.00  ? 80  TYR B CB  1 
ATOM   3776 C  CG  . TYR B 2 82  ? 134.634 -0.761  -19.060 1.00 81.31  ? 80  TYR B CG  1 
ATOM   3777 C  CD1 . TYR B 2 82  ? 134.616 -1.957  -18.352 1.00 83.77  ? 80  TYR B CD1 1 
ATOM   3778 C  CD2 . TYR B 2 82  ? 135.712 0.096   -18.878 1.00 82.83  ? 80  TYR B CD2 1 
ATOM   3779 C  CE1 . TYR B 2 82  ? 135.638 -2.284  -17.479 1.00 92.97  ? 80  TYR B CE1 1 
ATOM   3780 C  CE2 . TYR B 2 82  ? 136.737 -0.221  -18.009 1.00 95.91  ? 80  TYR B CE2 1 
ATOM   3781 C  CZ  . TYR B 2 82  ? 136.697 -1.413  -17.314 1.00 99.47  ? 80  TYR B CZ  1 
ATOM   3782 O  OH  . TYR B 2 82  ? 137.717 -1.732  -16.446 1.00 105.53 ? 80  TYR B OH  1 
ATOM   3783 N  N   . LEU B 2 83  ? 131.364 1.403   -21.303 1.00 63.73  ? 81  LEU B N   1 
ATOM   3784 C  CA  . LEU B 2 83  ? 130.456 1.552   -22.434 1.00 65.81  ? 81  LEU B CA  1 
ATOM   3785 C  C   . LEU B 2 83  ? 131.282 1.836   -23.679 1.00 66.39  ? 81  LEU B C   1 
ATOM   3786 O  O   . LEU B 2 83  ? 131.861 2.918   -23.814 1.00 60.72  ? 81  LEU B O   1 
ATOM   3787 C  CB  . LEU B 2 83  ? 129.432 2.661   -22.195 1.00 64.13  ? 81  LEU B CB  1 
ATOM   3788 C  CG  . LEU B 2 83  ? 128.269 2.678   -23.189 1.00 55.16  ? 81  LEU B CG  1 
ATOM   3789 C  CD1 . LEU B 2 83  ? 127.234 1.615   -22.844 1.00 60.26  ? 81  LEU B CD1 1 
ATOM   3790 C  CD2 . LEU B 2 83  ? 127.637 4.059   -23.238 1.00 53.16  ? 81  LEU B CD2 1 
ATOM   3791 N  N   . GLN B 2 84  ? 131.339 0.858   -24.577 1.00 62.87  ? 82  GLN B N   1 
ATOM   3792 C  CA  . GLN B 2 84  ? 131.950 1.031   -25.885 1.00 56.71  ? 82  GLN B CA  1 
ATOM   3793 C  C   . GLN B 2 84  ? 130.915 1.593   -26.848 1.00 62.08  ? 82  GLN B C   1 
ATOM   3794 O  O   . GLN B 2 84  ? 129.820 1.039   -26.978 1.00 60.71  ? 82  GLN B O   1 
ATOM   3795 C  CB  . GLN B 2 84  ? 132.478 -0.303  -26.403 1.00 60.11  ? 82  GLN B CB  1 
ATOM   3796 C  CG  . GLN B 2 84  ? 132.889 -0.251  -27.846 1.00 68.77  ? 82  GLN B CG  1 
ATOM   3797 C  CD  . GLN B 2 84  ? 134.141 0.569   -28.027 1.00 66.74  ? 82  GLN B CD  1 
ATOM   3798 O  OE1 . GLN B 2 84  ? 135.017 0.571   -27.164 1.00 68.18  ? 82  GLN B OE1 1 
ATOM   3799 N  NE2 . GLN B 2 84  ? 134.233 1.277   -29.146 1.00 71.08  ? 82  GLN B NE2 1 
ATOM   3800 N  N   . MET B 2 85  ? 131.261 2.687   -27.523 1.00 59.56  ? 83  MET B N   1 
ATOM   3801 C  CA  . MET B 2 85  ? 130.340 3.376   -28.425 1.00 67.03  ? 83  MET B CA  1 
ATOM   3802 C  C   . MET B 2 85  ? 130.958 3.477   -29.817 1.00 69.05  ? 83  MET B C   1 
ATOM   3803 O  O   . MET B 2 85  ? 131.853 4.297   -30.047 1.00 70.91  ? 83  MET B O   1 
ATOM   3804 C  CB  . MET B 2 85  ? 129.980 4.759   -27.880 1.00 65.19  ? 83  MET B CB  1 
ATOM   3805 C  CG  . MET B 2 85  ? 129.522 4.758   -26.423 1.00 67.46  ? 83  MET B CG  1 
ATOM   3806 S  SD  . MET B 2 85  ? 129.999 6.234   -25.498 1.00 63.73  ? 83  MET B SD  1 
ATOM   3807 C  CE  . MET B 2 85  ? 128.782 7.398   -26.098 1.00 49.50  ? 83  MET B CE  1 
ATOM   3808 N  N   . ASN B 2 86  ? 130.472 2.655   -30.743 1.00 68.65  ? 84  ASN B N   1 
ATOM   3809 C  CA  . ASN B 2 86  ? 130.912 2.668   -32.129 1.00 63.89  ? 84  ASN B CA  1 
ATOM   3810 C  C   . ASN B 2 86  ? 129.833 3.273   -33.018 1.00 71.10  ? 84  ASN B C   1 
ATOM   3811 O  O   . ASN B 2 86  ? 128.650 3.303   -32.665 1.00 72.60  ? 84  ASN B O   1 
ATOM   3812 C  CB  . ASN B 2 86  ? 131.246 1.255   -32.618 1.00 66.16  ? 84  ASN B CB  1 
ATOM   3813 C  CG  . ASN B 2 86  ? 131.794 0.371   -31.520 1.00 65.36  ? 84  ASN B CG  1 
ATOM   3814 O  OD1 . ASN B 2 86  ? 132.912 0.570   -31.051 1.00 70.45  ? 84  ASN B OD1 1 
ATOM   3815 N  ND2 . ASN B 2 86  ? 131.011 -0.616  -31.108 1.00 68.38  ? 84  ASN B ND2 1 
ATOM   3816 N  N   . SER B 2 87  ? 130.262 3.754   -34.187 1.00 69.48  ? 85  SER B N   1 
ATOM   3817 C  CA  . SER B 2 87  ? 129.366 4.353   -35.177 1.00 69.80  ? 85  SER B CA  1 
ATOM   3818 C  C   . SER B 2 87  ? 128.585 5.519   -34.574 1.00 69.91  ? 85  SER B C   1 
ATOM   3819 O  O   . SER B 2 87  ? 127.354 5.568   -34.621 1.00 73.15  ? 85  SER B O   1 
ATOM   3820 C  CB  . SER B 2 87  ? 128.420 3.305   -35.768 1.00 68.31  ? 85  SER B CB  1 
ATOM   3821 O  OG  . SER B 2 87  ? 129.031 2.624   -36.849 1.00 73.86  ? 85  SER B OG  1 
ATOM   3822 N  N   . LEU B 2 88  ? 129.320 6.470   -34.006 1.00 71.24  ? 86  LEU B N   1 
ATOM   3823 C  CA  . LEU B 2 88  ? 128.703 7.587   -33.305 1.00 70.24  ? 86  LEU B CA  1 
ATOM   3824 C  C   . LEU B 2 88  ? 128.093 8.564   -34.302 1.00 65.06  ? 86  LEU B C   1 
ATOM   3825 O  O   . LEU B 2 88  ? 128.796 9.105   -35.160 1.00 72.72  ? 86  LEU B O   1 
ATOM   3826 C  CB  . LEU B 2 88  ? 129.735 8.290   -32.428 1.00 73.28  ? 86  LEU B CB  1 
ATOM   3827 C  CG  . LEU B 2 88  ? 130.029 7.617   -31.085 1.00 69.13  ? 86  LEU B CG  1 
ATOM   3828 C  CD1 . LEU B 2 88  ? 131.256 8.223   -30.428 1.00 70.00  ? 86  LEU B CD1 1 
ATOM   3829 C  CD2 . LEU B 2 88  ? 128.821 7.726   -30.176 1.00 65.52  ? 86  LEU B CD2 1 
ATOM   3830 N  N   . ASN B 2 89  ? 126.792 8.785   -34.188 1.00 64.43  ? 87  ASN B N   1 
ATOM   3831 C  CA  . ASN B 2 89  ? 126.071 9.765   -34.981 1.00 64.92  ? 87  ASN B CA  1 
ATOM   3832 C  C   . ASN B 2 89  ? 125.801 11.013  -34.154 1.00 68.29  ? 87  ASN B C   1 
ATOM   3833 O  O   . ASN B 2 89  ? 125.889 10.983  -32.923 1.00 70.85  ? 87  ASN B O   1 
ATOM   3834 C  CB  . ASN B 2 89  ? 124.754 9.167   -35.495 1.00 67.95  ? 87  ASN B CB  1 
ATOM   3835 C  CG  . ASN B 2 89  ? 123.769 8.871   -34.386 1.00 68.00  ? 87  ASN B CG  1 
ATOM   3836 O  OD1 . ASN B 2 89  ? 122.797 9.603   -34.191 1.00 74.46  ? 87  ASN B OD1 1 
ATOM   3837 N  ND2 . ASN B 2 89  ? 124.009 7.788   -33.656 1.00 66.37  ? 87  ASN B ND2 1 
ATOM   3838 N  N   . PRO B 2 90  ? 125.497 12.146  -34.798 1.00 70.23  ? 88  PRO B N   1 
ATOM   3839 C  CA  . PRO B 2 90  ? 125.267 13.386  -34.033 1.00 69.15  ? 88  PRO B CA  1 
ATOM   3840 C  C   . PRO B 2 90  ? 124.165 13.284  -32.991 1.00 69.89  ? 88  PRO B C   1 
ATOM   3841 O  O   . PRO B 2 90  ? 124.183 14.054  -32.021 1.00 65.31  ? 88  PRO B O   1 
ATOM   3842 C  CB  . PRO B 2 90  ? 124.913 14.405  -35.123 1.00 74.55  ? 88  PRO B CB  1 
ATOM   3843 C  CG  . PRO B 2 90  ? 125.617 13.902  -36.334 1.00 78.20  ? 88  PRO B CG  1 
ATOM   3844 C  CD  . PRO B 2 90  ? 125.565 12.401  -36.248 1.00 73.26  ? 88  PRO B CD  1 
ATOM   3845 N  N   . GLY B 2 91  ? 123.213 12.365  -33.150 1.00 71.42  ? 89  GLY B N   1 
ATOM   3846 C  CA  . GLY B 2 91  ? 122.175 12.185  -32.153 1.00 64.77  ? 89  GLY B CA  1 
ATOM   3847 C  C   . GLY B 2 91  ? 122.660 11.626  -30.832 1.00 63.89  ? 89  GLY B C   1 
ATOM   3848 O  O   . GLY B 2 91  ? 121.884 11.602  -29.872 1.00 69.27  ? 89  GLY B O   1 
ATOM   3849 N  N   . ASP B 2 92  ? 123.911 11.180  -30.759 1.00 63.09  ? 90  ASP B N   1 
ATOM   3850 C  CA  . ASP B 2 92  ? 124.472 10.629  -29.533 1.00 64.29  ? 90  ASP B CA  1 
ATOM   3851 C  C   . ASP B 2 92  ? 125.100 11.686  -28.636 1.00 64.81  ? 90  ASP B C   1 
ATOM   3852 O  O   . ASP B 2 92  ? 125.553 11.355  -27.535 1.00 63.82  ? 90  ASP B O   1 
ATOM   3853 C  CB  . ASP B 2 92  ? 125.515 9.559   -29.870 1.00 61.82  ? 90  ASP B CB  1 
ATOM   3854 C  CG  . ASP B 2 92  ? 124.910 8.363   -30.575 1.00 60.94  ? 90  ASP B CG  1 
ATOM   3855 O  OD1 . ASP B 2 92  ? 123.688 8.146   -30.433 1.00 72.52  ? 90  ASP B OD1 1 
ATOM   3856 O  OD2 . ASP B 2 92  ? 125.653 7.645   -31.273 1.00 63.20  ? 90  ASP B OD2 1 
ATOM   3857 N  N   . THR B 2 93  ? 125.140 12.941  -29.074 1.00 66.49  ? 91  THR B N   1 
ATOM   3858 C  CA  . THR B 2 93  ? 125.702 14.011  -28.261 1.00 64.11  ? 91  THR B CA  1 
ATOM   3859 C  C   . THR B 2 93  ? 124.829 14.244  -27.035 1.00 57.82  ? 91  THR B C   1 
ATOM   3860 O  O   . THR B 2 93  ? 123.661 14.629  -27.158 1.00 61.13  ? 91  THR B O   1 
ATOM   3861 C  CB  . THR B 2 93  ? 125.825 15.293  -29.081 1.00 67.01  ? 91  THR B CB  1 
ATOM   3862 O  OG1 . THR B 2 93  ? 126.866 15.142  -30.054 1.00 65.85  ? 91  THR B OG1 1 
ATOM   3863 C  CG2 . THR B 2 93  ? 126.150 16.471  -28.176 1.00 63.07  ? 91  THR B CG2 1 
ATOM   3864 N  N   . ALA B 2 94  ? 125.393 14.012  -25.854 1.00 56.65  ? 92  ALA B N   1 
ATOM   3865 C  CA  . ALA B 2 94  ? 124.661 14.172  -24.606 1.00 55.90  ? 92  ALA B CA  1 
ATOM   3866 C  C   . ALA B 2 94  ? 125.646 14.084  -23.450 1.00 59.45  ? 92  ALA B C   1 
ATOM   3867 O  O   . ALA B 2 94  ? 126.831 13.793  -23.635 1.00 61.85  ? 92  ALA B O   1 
ATOM   3868 C  CB  . ALA B 2 94  ? 123.562 13.116  -24.458 1.00 56.22  ? 92  ALA B CB  1 
ATOM   3869 N  N   . VAL B 2 95  ? 125.138 14.351  -22.253 1.00 55.54  ? 93  VAL B N   1 
ATOM   3870 C  CA  . VAL B 2 95  ? 125.864 14.082  -21.019 1.00 56.66  ? 93  VAL B CA  1 
ATOM   3871 C  C   . VAL B 2 95  ? 125.524 12.662  -20.596 1.00 54.29  ? 93  VAL B C   1 
ATOM   3872 O  O   . VAL B 2 95  ? 124.349 12.316  -20.441 1.00 51.13  ? 93  VAL B O   1 
ATOM   3873 C  CB  . VAL B 2 95  ? 125.499 15.090  -19.919 1.00 57.08  ? 93  VAL B CB  1 
ATOM   3874 C  CG1 . VAL B 2 95  ? 125.965 14.584  -18.558 1.00 55.88  ? 93  VAL B CG1 1 
ATOM   3875 C  CG2 . VAL B 2 95  ? 126.093 16.449  -20.229 1.00 52.69  ? 93  VAL B CG2 1 
ATOM   3876 N  N   . TYR B 2 96  ? 126.544 11.837  -20.422 1.00 54.67  ? 94  TYR B N   1 
ATOM   3877 C  CA  . TYR B 2 96  ? 126.357 10.434  -20.088 1.00 57.15  ? 94  TYR B CA  1 
ATOM   3878 C  C   . TYR B 2 96  ? 126.616 10.225  -18.603 1.00 52.23  ? 94  TYR B C   1 
ATOM   3879 O  O   . TYR B 2 96  ? 127.601 10.734  -18.062 1.00 67.65  ? 94  TYR B O   1 
ATOM   3880 C  CB  . TYR B 2 96  ? 127.277 9.555   -20.934 1.00 46.78  ? 94  TYR B CB  1 
ATOM   3881 C  CG  . TYR B 2 96  ? 126.809 9.424   -22.367 1.00 55.10  ? 94  TYR B CG  1 
ATOM   3882 C  CD1 . TYR B 2 96  ? 126.886 10.497  -23.248 1.00 49.62  ? 94  TYR B CD1 1 
ATOM   3883 C  CD2 . TYR B 2 96  ? 126.262 8.232   -22.830 1.00 53.82  ? 94  TYR B CD2 1 
ATOM   3884 C  CE1 . TYR B 2 96  ? 126.448 10.383  -24.553 1.00 51.11  ? 94  TYR B CE1 1 
ATOM   3885 C  CE2 . TYR B 2 96  ? 125.823 8.107   -24.135 1.00 54.61  ? 94  TYR B CE2 1 
ATOM   3886 C  CZ  . TYR B 2 96  ? 125.919 9.185   -24.993 1.00 57.71  ? 94  TYR B CZ  1 
ATOM   3887 O  OH  . TYR B 2 96  ? 125.478 9.061   -26.292 1.00 59.63  ? 94  TYR B OH  1 
ATOM   3888 N  N   . SER B 2 97  ? 125.729 9.481   -17.949 1.00 50.63  ? 95  SER B N   1 
ATOM   3889 C  CA  . SER B 2 97  ? 125.819 9.239   -16.517 1.00 55.98  ? 95  SER B CA  1 
ATOM   3890 C  C   . SER B 2 97  ? 125.640 7.756   -16.242 1.00 61.26  ? 95  SER B C   1 
ATOM   3891 O  O   . SER B 2 97  ? 124.751 7.118   -16.815 1.00 52.47  ? 95  SER B O   1 
ATOM   3892 C  CB  . SER B 2 97  ? 124.763 10.047  -15.754 1.00 61.10  ? 95  SER B CB  1 
ATOM   3893 O  OG  . SER B 2 97  ? 124.925 11.438  -15.967 1.00 69.76  ? 95  SER B OG  1 
ATOM   3894 N  N   . CYS B 2 98  ? 126.486 7.211   -15.373 1.00 63.76  ? 96  CYS B N   1 
ATOM   3895 C  CA  . CYS B 2 98  ? 126.315 5.854   -14.879 1.00 60.41  ? 96  CYS B CA  1 
ATOM   3896 C  C   . CYS B 2 98  ? 125.457 5.878   -13.621 1.00 58.21  ? 96  CYS B C   1 
ATOM   3897 O  O   . CYS B 2 98  ? 125.477 6.842   -12.852 1.00 60.96  ? 96  CYS B O   1 
ATOM   3898 C  CB  . CYS B 2 98  ? 127.667 5.197   -14.583 1.00 58.34  ? 96  CYS B CB  1 
ATOM   3899 S  SG  . CYS B 2 98  ? 128.744 6.151   -13.487 1.00 92.58  ? 96  CYS B SG  1 
ATOM   3900 N  N   . ALA B 2 99  ? 124.698 4.805   -13.418 1.00 56.33  ? 97  ALA B N   1 
ATOM   3901 C  CA  . ALA B 2 99  ? 123.777 4.727   -12.294 1.00 54.17  ? 97  ALA B CA  1 
ATOM   3902 C  C   . ALA B 2 99  ? 123.868 3.355   -11.644 1.00 53.87  ? 97  ALA B C   1 
ATOM   3903 O  O   . ALA B 2 99  ? 124.130 2.349   -12.309 1.00 59.83  ? 97  ALA B O   1 
ATOM   3904 C  CB  . ALA B 2 99  ? 122.336 5.005   -12.733 1.00 52.71  ? 97  ALA B CB  1 
ATOM   3905 N  N   . ALA B 2 100 ? 123.644 3.326   -10.333 1.00 51.69  ? 98  ALA B N   1 
ATOM   3906 C  CA  . ALA B 2 100 ? 123.671 2.095   -9.561  1.00 56.06  ? 98  ALA B CA  1 
ATOM   3907 C  C   . ALA B 2 100 ? 122.422 2.004   -8.704  1.00 62.64  ? 98  ALA B C   1 
ATOM   3908 O  O   . ALA B 2 100 ? 121.946 3.013   -8.172  1.00 60.89  ? 98  ALA B O   1 
ATOM   3909 C  CB  . ALA B 2 100 ? 124.911 2.017   -8.669  1.00 59.43  ? 98  ALA B CB  1 
ATOM   3910 N  N   . THR B 2 101 ? 121.897 0.789   -8.574  1.00 60.01  ? 99  THR B N   1 
ATOM   3911 C  CA  . THR B 2 101 ? 120.761 0.537   -7.704  1.00 58.75  ? 99  THR B CA  1 
ATOM   3912 C  C   . THR B 2 101 ? 120.651 -0.961  -7.461  1.00 67.41  ? 99  THR B C   1 
ATOM   3913 O  O   . THR B 2 101 ? 121.271 -1.770  -8.157  1.00 62.60  ? 99  THR B O   1 
ATOM   3914 C  CB  . THR B 2 101 ? 119.460 1.090   -8.295  1.00 60.37  ? 99  THR B CB  1 
ATOM   3915 O  OG1 . THR B 2 101 ? 118.462 1.161   -7.270  1.00 56.11  ? 99  THR B OG1 1 
ATOM   3916 C  CG2 . THR B 2 101 ? 118.964 0.208   -9.412  1.00 54.31  ? 99  THR B CG2 1 
ATOM   3917 N  N   . LEU B 2 102 ? 119.856 -1.315  -6.446  1.00 63.08  ? 100 LEU B N   1 
ATOM   3918 C  CA  . LEU B 2 102 ? 119.607 -2.708  -6.114  1.00 66.63  ? 100 LEU B CA  1 
ATOM   3919 C  C   . LEU B 2 102 ? 118.497 -3.273  -7.001  1.00 62.44  ? 100 LEU B C   1 
ATOM   3920 O  O   . LEU B 2 102 ? 117.624 -2.532  -7.460  1.00 62.08  ? 100 LEU B O   1 
ATOM   3921 C  CB  . LEU B 2 102 ? 119.218 -2.840  -4.645  1.00 60.16  ? 100 LEU B CB  1 
ATOM   3922 C  CG  . LEU B 2 102 ? 120.338 -2.607  -3.628  1.00 63.67  ? 100 LEU B CG  1 
ATOM   3923 C  CD1 . LEU B 2 102 ? 119.963 -3.176  -2.273  1.00 63.30  ? 100 LEU B CD1 1 
ATOM   3924 C  CD2 . LEU B 2 102 ? 121.647 -3.203  -4.114  1.00 67.65  ? 100 LEU B CD2 1 
ATOM   3925 N  N   . PRO B 2 103 ? 118.514 -4.584  -7.263  1.00 62.88  ? 101 PRO B N   1 
ATOM   3926 C  CA  . PRO B 2 103 ? 117.507 -5.163  -8.170  1.00 61.85  ? 101 PRO B CA  1 
ATOM   3927 C  C   . PRO B 2 103 ? 116.076 -4.998  -7.688  1.00 60.53  ? 101 PRO B C   1 
ATOM   3928 O  O   . PRO B 2 103 ? 115.154 -5.047  -8.512  1.00 57.50  ? 101 PRO B O   1 
ATOM   3929 C  CB  . PRO B 2 103 ? 117.907 -6.644  -8.243  1.00 65.85  ? 101 PRO B CB  1 
ATOM   3930 C  CG  . PRO B 2 103 ? 118.770 -6.876  -7.043  1.00 70.50  ? 101 PRO B CG  1 
ATOM   3931 C  CD  . PRO B 2 103 ? 119.489 -5.587  -6.805  1.00 69.30  ? 101 PRO B CD  1 
ATOM   3932 N  N   . ALA B 2 104 ? 115.855 -4.805  -6.387  1.00 58.93  ? 102 ALA B N   1 
ATOM   3933 C  CA  . ALA B 2 104 ? 114.506 -4.532  -5.911  1.00 55.99  ? 102 ALA B CA  1 
ATOM   3934 C  C   . ALA B 2 104 ? 114.005 -3.169  -6.369  1.00 56.50  ? 102 ALA B C   1 
ATOM   3935 O  O   . ALA B 2 104 ? 112.790 -2.956  -6.429  1.00 53.71  ? 102 ALA B O   1 
ATOM   3936 C  CB  . ALA B 2 104 ? 114.451 -4.625  -4.386  1.00 58.00  ? 102 ALA B CB  1 
ATOM   3937 N  N   . TRP B 2 105 ? 114.910 -2.246  -6.698  1.00 59.02  ? 103 TRP B N   1 
ATOM   3938 C  CA  . TRP B 2 105 ? 114.493 -0.939  -7.188  1.00 55.13  ? 103 TRP B CA  1 
ATOM   3939 C  C   . TRP B 2 105 ? 114.063 -0.979  -8.648  1.00 53.53  ? 103 TRP B C   1 
ATOM   3940 O  O   . TRP B 2 105 ? 113.279 -0.128  -9.078  1.00 49.48  ? 103 TRP B O   1 
ATOM   3941 C  CB  . TRP B 2 105 ? 115.622 0.075   -7.024  1.00 52.11  ? 103 TRP B CB  1 
ATOM   3942 C  CG  . TRP B 2 105 ? 115.867 0.495   -5.616  1.00 53.64  ? 103 TRP B CG  1 
ATOM   3943 C  CD1 . TRP B 2 105 ? 116.207 -0.309  -4.569  1.00 55.54  ? 103 TRP B CD1 1 
ATOM   3944 C  CD2 . TRP B 2 105 ? 115.804 1.829   -5.098  1.00 53.63  ? 103 TRP B CD2 1 
ATOM   3945 N  NE1 . TRP B 2 105 ? 116.352 0.441   -3.427  1.00 56.72  ? 103 TRP B NE1 1 
ATOM   3946 C  CE2 . TRP B 2 105 ? 116.113 1.757   -3.725  1.00 55.55  ? 103 TRP B CE2 1 
ATOM   3947 C  CE3 . TRP B 2 105 ? 115.516 3.076   -5.661  1.00 52.37  ? 103 TRP B CE3 1 
ATOM   3948 C  CZ2 . TRP B 2 105 ? 116.143 2.883   -2.907  1.00 56.20  ? 103 TRP B CZ2 1 
ATOM   3949 C  CZ3 . TRP B 2 105 ? 115.542 4.192   -4.848  1.00 53.02  ? 103 TRP B CZ3 1 
ATOM   3950 C  CH2 . TRP B 2 105 ? 115.856 4.089   -3.487  1.00 54.89  ? 103 TRP B CH2 1 
ATOM   3951 N  N   . THR B 2 106 ? 114.574 -1.935  -9.424  1.00 54.48  ? 104 THR B N   1 
ATOM   3952 C  CA  . THR B 2 106 ? 114.215 -2.038  -10.832 1.00 49.29  ? 104 THR B CA  1 
ATOM   3953 C  C   . THR B 2 106 ? 113.006 -2.926  -11.070 1.00 52.56  ? 104 THR B C   1 
ATOM   3954 O  O   . THR B 2 106 ? 112.264 -2.700  -12.031 1.00 52.78  ? 104 THR B O   1 
ATOM   3955 C  CB  . THR B 2 106 ? 115.390 -2.580  -11.652 1.00 57.24  ? 104 THR B CB  1 
ATOM   3956 O  OG1 . THR B 2 106 ? 115.602 -3.962  -11.329 1.00 59.12  ? 104 THR B OG1 1 
ATOM   3957 C  CG2 . THR B 2 106 ? 116.651 -1.784  -11.374 1.00 49.24  ? 104 THR B CG2 1 
ATOM   3958 N  N   . GLY B 2 107 ? 112.792 -3.931  -10.226 1.00 52.82  ? 105 GLY B N   1 
ATOM   3959 C  CA  . GLY B 2 107 ? 111.677 -4.820  -10.466 1.00 53.68  ? 105 GLY B CA  1 
ATOM   3960 C  C   . GLY B 2 107 ? 111.877 -5.652  -11.724 1.00 55.35  ? 105 GLY B C   1 
ATOM   3961 O  O   . GLY B 2 107 ? 112.999 -5.923  -12.161 1.00 53.64  ? 105 GLY B O   1 
ATOM   3962 N  N   . ILE B 2 108 ? 110.760 -6.059  -12.317 1.00 59.70  ? 106 ILE B N   1 
ATOM   3963 C  CA  . ILE B 2 108 ? 110.799 -6.945  -13.473 1.00 54.04  ? 106 ILE B CA  1 
ATOM   3964 C  C   . ILE B 2 108 ? 110.926 -6.164  -14.774 1.00 52.14  ? 106 ILE B C   1 
ATOM   3965 O  O   . ILE B 2 108 ? 111.590 -6.614  -15.709 1.00 56.19  ? 106 ILE B O   1 
ATOM   3966 C  CB  . ILE B 2 108 ? 109.554 -7.855  -13.470 1.00 56.16  ? 106 ILE B CB  1 
ATOM   3967 C  CG1 . ILE B 2 108 ? 109.748 -8.996  -12.474 1.00 58.82  ? 106 ILE B CG1 1 
ATOM   3968 C  CG2 . ILE B 2 108 ? 109.276 -8.410  -14.857 1.00 57.42  ? 106 ILE B CG2 1 
ATOM   3969 C  CD1 . ILE B 2 108 ? 108.470 -9.487  -11.851 1.00 54.62  ? 106 ILE B CD1 1 
ATOM   3970 N  N   . ILE B 2 109 ? 110.319 -4.983  -14.864 1.00 52.86  ? 107 ILE B N   1 
ATOM   3971 C  CA  . ILE B 2 109 ? 110.304 -4.260  -16.130 1.00 54.32  ? 107 ILE B CA  1 
ATOM   3972 C  C   . ILE B 2 109 ? 110.631 -2.788  -15.925 1.00 52.52  ? 107 ILE B C   1 
ATOM   3973 O  O   . ILE B 2 109 ? 110.400 -1.966  -16.818 1.00 56.47  ? 107 ILE B O   1 
ATOM   3974 C  CB  . ILE B 2 109 ? 108.946 -4.414  -16.839 1.00 57.15  ? 107 ILE B CB  1 
ATOM   3975 C  CG1 . ILE B 2 109 ? 107.794 -4.253  -15.851 1.00 50.70  ? 107 ILE B CG1 1 
ATOM   3976 C  CG2 . ILE B 2 109 ? 108.853 -5.766  -17.522 1.00 60.78  ? 107 ILE B CG2 1 
ATOM   3977 C  CD1 . ILE B 2 109 ? 106.438 -4.240  -16.518 1.00 57.72  ? 107 ILE B CD1 1 
ATOM   3978 N  N   . GLY B 2 110 ? 111.175 -2.438  -14.765 1.00 51.71  ? 108 GLY B N   1 
ATOM   3979 C  CA  . GLY B 2 110 ? 111.463 -1.044  -14.496 1.00 45.81  ? 108 GLY B CA  1 
ATOM   3980 C  C   . GLY B 2 110 ? 112.932 -0.695  -14.605 1.00 48.87  ? 108 GLY B C   1 
ATOM   3981 O  O   . GLY B 2 110 ? 113.369 0.341   -14.098 1.00 53.99  ? 108 GLY B O   1 
ATOM   3982 N  N   . GLY B 2 111 ? 113.706 -1.551  -15.272 1.00 51.87  ? 109 GLY B N   1 
ATOM   3983 C  CA  . GLY B 2 111 ? 115.139 -1.342  -15.379 1.00 51.54  ? 109 GLY B CA  1 
ATOM   3984 C  C   . GLY B 2 111 ? 115.550 -0.159  -16.232 1.00 51.48  ? 109 GLY B C   1 
ATOM   3985 O  O   . GLY B 2 111 ? 116.716 0.245   -16.172 1.00 51.78  ? 109 GLY B O   1 
ATOM   3986 N  N   . ARG B 2 112 ? 114.626 0.404   -17.012 1.00 47.56  ? 110 ARG B N   1 
ATOM   3987 C  CA  . ARG B 2 112 ? 114.911 1.514   -17.912 1.00 51.20  ? 110 ARG B CA  1 
ATOM   3988 C  C   . ARG B 2 112 ? 114.584 2.878   -17.316 1.00 55.53  ? 110 ARG B C   1 
ATOM   3989 O  O   . ARG B 2 112 ? 114.894 3.898   -17.943 1.00 53.33  ? 110 ARG B O   1 
ATOM   3990 C  CB  . ARG B 2 112 ? 114.118 1.351   -19.213 1.00 56.71  ? 110 ARG B CB  1 
ATOM   3991 C  CG  . ARG B 2 112 ? 114.322 0.025   -19.916 1.00 56.34  ? 110 ARG B CG  1 
ATOM   3992 C  CD  . ARG B 2 112 ? 115.074 0.226   -21.196 1.00 59.58  ? 110 ARG B CD  1 
ATOM   3993 N  NE  . ARG B 2 112 ? 115.148 -0.971  -22.022 1.00 68.02  ? 110 ARG B NE  1 
ATOM   3994 C  CZ  . ARG B 2 112 ? 114.575 -1.097  -23.211 1.00 63.64  ? 110 ARG B CZ  1 
ATOM   3995 N  NH1 . ARG B 2 112 ? 113.860 -0.117  -23.741 1.00 67.32  ? 110 ARG B NH1 1 
ATOM   3996 N  NH2 . ARG B 2 112 ? 114.731 -2.230  -23.889 1.00 65.43  ? 110 ARG B NH2 1 
ATOM   3997 N  N   . ARG B 2 113 ? 113.948 2.925   -16.146 1.00 52.63  ? 111 ARG B N   1 
ATOM   3998 C  CA  . ARG B 2 113 ? 113.510 4.188   -15.564 1.00 51.10  ? 111 ARG B CA  1 
ATOM   3999 C  C   . ARG B 2 113 ? 114.627 4.786   -14.720 1.00 51.40  ? 111 ARG B C   1 
ATOM   4000 O  O   . ARG B 2 113 ? 115.077 4.141   -13.762 1.00 49.08  ? 111 ARG B O   1 
ATOM   4001 C  CB  . ARG B 2 113 ? 112.264 3.989   -14.714 1.00 47.87  ? 111 ARG B CB  1 
ATOM   4002 C  CG  . ARG B 2 113 ? 110.952 3.973   -15.507 1.00 54.31  ? 111 ARG B CG  1 
ATOM   4003 C  CD  . ARG B 2 113 ? 110.975 4.967   -16.679 1.00 61.61  ? 111 ARG B CD  1 
ATOM   4004 N  NE  . ARG B 2 113 ? 110.459 6.286   -16.323 1.00 66.02  ? 111 ARG B NE  1 
ATOM   4005 C  CZ  . ARG B 2 113 ? 110.545 7.360   -17.098 1.00 67.24  ? 111 ARG B CZ  1 
ATOM   4006 N  NH1 . ARG B 2 113 ? 111.138 7.315   -18.280 1.00 68.59  ? 111 ARG B NH1 1 
ATOM   4007 N  NH2 . ARG B 2 113 ? 110.024 8.510   -16.677 1.00 48.24  ? 111 ARG B NH2 1 
ATOM   4008 N  N   . PRO B 2 114 ? 115.093 6.001   -15.021 1.00 50.99  ? 112 PRO B N   1 
ATOM   4009 C  CA  . PRO B 2 114 ? 116.192 6.580   -14.231 1.00 54.82  ? 112 PRO B CA  1 
ATOM   4010 C  C   . PRO B 2 114 ? 115.813 6.863   -12.790 1.00 49.79  ? 112 PRO B C   1 
ATOM   4011 O  O   . PRO B 2 114 ? 116.701 6.900   -11.928 1.00 49.39  ? 112 PRO B O   1 
ATOM   4012 C  CB  . PRO B 2 114 ? 116.527 7.873   -14.986 1.00 50.94  ? 112 PRO B CB  1 
ATOM   4013 C  CG  . PRO B 2 114 ? 115.255 8.230   -15.692 1.00 55.92  ? 112 PRO B CG  1 
ATOM   4014 C  CD  . PRO B 2 114 ? 114.588 6.928   -16.048 1.00 44.97  ? 112 PRO B CD  1 
ATOM   4015 N  N   . GLY B 2 115 ? 114.529 7.055   -12.498 1.00 45.38  ? 113 GLY B N   1 
ATOM   4016 C  CA  . GLY B 2 115 ? 114.092 7.233   -11.125 1.00 46.28  ? 113 GLY B CA  1 
ATOM   4017 C  C   . GLY B 2 115 ? 114.228 5.998   -10.260 1.00 49.80  ? 113 GLY B C   1 
ATOM   4018 O  O   . GLY B 2 115 ? 114.084 6.104   -9.037  1.00 50.31  ? 113 GLY B O   1 
ATOM   4019 N  N   . ASN B 2 116 ? 114.491 4.837   -10.859 1.00 48.01  ? 114 ASN B N   1 
ATOM   4020 C  CA  . ASN B 2 116 ? 114.756 3.617   -10.110 1.00 47.54  ? 114 ASN B CA  1 
ATOM   4021 C  C   . ASN B 2 116 ? 116.223 3.463   -9.728  1.00 50.94  ? 114 ASN B C   1 
ATOM   4022 O  O   . ASN B 2 116 ? 116.601 2.418   -9.187  1.00 51.47  ? 114 ASN B O   1 
ATOM   4023 C  CB  . ASN B 2 116 ? 114.305 2.397   -10.918 1.00 47.51  ? 114 ASN B CB  1 
ATOM   4024 C  CG  . ASN B 2 116 ? 112.805 2.202   -10.886 1.00 48.27  ? 114 ASN B CG  1 
ATOM   4025 O  OD1 . ASN B 2 116 ? 112.143 2.590   -9.926  1.00 48.62  ? 114 ASN B OD1 1 
ATOM   4026 N  ND2 . ASN B 2 116 ? 112.259 1.602   -11.938 1.00 46.43  ? 114 ASN B ND2 1 
ATOM   4027 N  N   . TYR B 2 117 ? 117.054 4.465   -10.000 1.00 48.01  ? 115 TYR B N   1 
ATOM   4028 C  CA  . TYR B 2 117 ? 118.469 4.445   -9.625  1.00 54.72  ? 115 TYR B CA  1 
ATOM   4029 C  C   . TYR B 2 117 ? 118.747 5.651   -8.743  1.00 54.33  ? 115 TYR B C   1 
ATOM   4030 O  O   . TYR B 2 117 ? 118.806 6.789   -9.244  1.00 58.41  ? 115 TYR B O   1 
ATOM   4031 C  CB  . TYR B 2 117 ? 119.377 4.462   -10.857 1.00 52.55  ? 115 TYR B CB  1 
ATOM   4032 C  CG  . TYR B 2 117 ? 119.193 3.292   -11.805 1.00 52.71  ? 115 TYR B CG  1 
ATOM   4033 C  CD1 . TYR B 2 117 ? 118.088 3.223   -12.646 1.00 47.98  ? 115 TYR B CD1 1 
ATOM   4034 C  CD2 . TYR B 2 117 ? 120.133 2.267   -11.871 1.00 50.00  ? 115 TYR B CD2 1 
ATOM   4035 C  CE1 . TYR B 2 117 ? 117.910 2.166   -13.510 1.00 46.22  ? 115 TYR B CE1 1 
ATOM   4036 C  CE2 . TYR B 2 117 ? 119.965 1.199   -12.738 1.00 48.07  ? 115 TYR B CE2 1 
ATOM   4037 C  CZ  . TYR B 2 117 ? 118.847 1.156   -13.557 1.00 55.39  ? 115 TYR B CZ  1 
ATOM   4038 O  OH  . TYR B 2 117 ? 118.652 0.106   -14.429 1.00 52.36  ? 115 TYR B OH  1 
ATOM   4039 N  N   . PRO B 2 118 ? 118.916 5.468   -7.431  1.00 56.95  ? 116 PRO B N   1 
ATOM   4040 C  CA  . PRO B 2 118 ? 119.173 6.617   -6.555  1.00 51.93  ? 116 PRO B CA  1 
ATOM   4041 C  C   . PRO B 2 118 ? 120.618 7.082   -6.547  1.00 54.84  ? 116 PRO B C   1 
ATOM   4042 O  O   . PRO B 2 118 ? 120.884 8.199   -6.083  1.00 64.55  ? 116 PRO B O   1 
ATOM   4043 C  CB  . PRO B 2 118 ? 118.758 6.095   -5.175  1.00 56.75  ? 116 PRO B CB  1 
ATOM   4044 C  CG  . PRO B 2 118 ? 119.030 4.633   -5.244  1.00 56.44  ? 116 PRO B CG  1 
ATOM   4045 C  CD  . PRO B 2 118 ? 118.795 4.211   -6.674  1.00 52.19  ? 116 PRO B CD  1 
ATOM   4046 N  N   . TYR B 2 119 ? 121.553 6.279   -7.047  1.00 53.03  ? 117 TYR B N   1 
ATOM   4047 C  CA  . TYR B 2 119 ? 122.973 6.607   -7.030  1.00 56.10  ? 117 TYR B CA  1 
ATOM   4048 C  C   . TYR B 2 119 ? 123.438 6.952   -8.439  1.00 58.96  ? 117 TYR B C   1 
ATOM   4049 O  O   . TYR B 2 119 ? 123.234 6.171   -9.376  1.00 59.20  ? 117 TYR B O   1 
ATOM   4050 C  CB  . TYR B 2 119 ? 123.785 5.445   -6.456  1.00 58.90  ? 117 TYR B CB  1 
ATOM   4051 C  CG  . TYR B 2 119 ? 123.214 4.925   -5.155  1.00 60.77  ? 117 TYR B CG  1 
ATOM   4052 C  CD1 . TYR B 2 119 ? 123.023 5.773   -4.071  1.00 60.06  ? 117 TYR B CD1 1 
ATOM   4053 C  CD2 . TYR B 2 119 ? 122.843 3.592   -5.017  1.00 62.79  ? 117 TYR B CD2 1 
ATOM   4054 C  CE1 . TYR B 2 119 ? 122.487 5.306   -2.880  1.00 64.45  ? 117 TYR B CE1 1 
ATOM   4055 C  CE2 . TYR B 2 119 ? 122.307 3.116   -3.830  1.00 62.83  ? 117 TYR B CE2 1 
ATOM   4056 C  CZ  . TYR B 2 119 ? 122.133 3.978   -2.765  1.00 63.32  ? 117 TYR B CZ  1 
ATOM   4057 O  OH  . TYR B 2 119 ? 121.603 3.512   -1.583  1.00 68.66  ? 117 TYR B OH  1 
ATOM   4058 N  N   . TRP B 2 120 ? 124.066 8.116   -8.581  1.00 54.97  ? 118 TRP B N   1 
ATOM   4059 C  CA  . TRP B 2 120 ? 124.413 8.667   -9.880  1.00 55.25  ? 118 TRP B CA  1 
ATOM   4060 C  C   . TRP B 2 120 ? 125.858 9.143   -9.882  1.00 67.54  ? 118 TRP B C   1 
ATOM   4061 O  O   . TRP B 2 120 ? 126.466 9.373   -8.833  1.00 73.27  ? 118 TRP B O   1 
ATOM   4062 C  CB  . TRP B 2 120 ? 123.483 9.830   -10.244 1.00 55.84  ? 118 TRP B CB  1 
ATOM   4063 C  CG  . TRP B 2 120 ? 122.118 9.379   -10.646 1.00 60.06  ? 118 TRP B CG  1 
ATOM   4064 C  CD1 . TRP B 2 120 ? 120.995 9.377   -9.872  1.00 57.12  ? 118 TRP B CD1 1 
ATOM   4065 C  CD2 . TRP B 2 120 ? 121.725 8.876   -11.927 1.00 61.32  ? 118 TRP B CD2 1 
ATOM   4066 N  NE1 . TRP B 2 120 ? 119.930 8.892   -10.588 1.00 59.27  ? 118 TRP B NE1 1 
ATOM   4067 C  CE2 . TRP B 2 120 ? 120.351 8.581   -11.854 1.00 55.80  ? 118 TRP B CE2 1 
ATOM   4068 C  CE3 . TRP B 2 120 ? 122.404 8.645   -13.129 1.00 62.91  ? 118 TRP B CE3 1 
ATOM   4069 C  CZ2 . TRP B 2 120 ? 119.642 8.064   -12.934 1.00 53.19  ? 118 TRP B CZ2 1 
ATOM   4070 C  CZ3 . TRP B 2 120 ? 121.696 8.135   -14.202 1.00 56.74  ? 118 TRP B CZ3 1 
ATOM   4071 C  CH2 . TRP B 2 120 ? 120.329 7.852   -14.096 1.00 53.11  ? 118 TRP B CH2 1 
ATOM   4072 N  N   . GLY B 2 121 ? 126.407 9.283   -11.090 1.00 69.04  ? 119 GLY B N   1 
ATOM   4073 C  CA  . GLY B 2 121 ? 127.679 9.936   -11.290 1.00 69.92  ? 119 GLY B CA  1 
ATOM   4074 C  C   . GLY B 2 121 ? 127.494 11.390  -11.700 1.00 73.91  ? 119 GLY B C   1 
ATOM   4075 O  O   . GLY B 2 121 ? 126.386 11.879  -11.899 1.00 73.94  ? 119 GLY B O   1 
ATOM   4076 N  N   . GLN B 2 122 ? 128.624 12.085  -11.824 1.00 73.57  ? 120 GLN B N   1 
ATOM   4077 C  CA  . GLN B 2 122 ? 128.581 13.498  -12.180 1.00 77.13  ? 120 GLN B CA  1 
ATOM   4078 C  C   . GLN B 2 122 ? 128.216 13.720  -13.642 1.00 72.55  ? 120 GLN B C   1 
ATOM   4079 O  O   . GLN B 2 122 ? 127.715 14.796  -13.986 1.00 70.90  ? 120 GLN B O   1 
ATOM   4080 C  CB  . GLN B 2 122 ? 129.926 14.160  -11.863 1.00 82.24  ? 120 GLN B CB  1 
ATOM   4081 C  CG  . GLN B 2 122 ? 130.937 14.133  -13.004 1.00 89.04  ? 120 GLN B CG  1 
ATOM   4082 C  CD  . GLN B 2 122 ? 131.846 12.916  -12.955 1.00 91.27  ? 120 GLN B CD  1 
ATOM   4083 O  OE1 . GLN B 2 122 ? 131.707 12.058  -12.080 1.00 87.45  ? 120 GLN B OE1 1 
ATOM   4084 N  NE2 . GLN B 2 122 ? 132.785 12.837  -13.896 1.00 84.12  ? 120 GLN B NE2 1 
ATOM   4085 N  N   . GLY B 2 123 ? 128.442 12.731  -14.503 1.00 72.81  ? 121 GLY B N   1 
ATOM   4086 C  CA  . GLY B 2 123 ? 128.177 12.886  -15.918 1.00 66.76  ? 121 GLY B CA  1 
ATOM   4087 C  C   . GLY B 2 123 ? 129.376 13.379  -16.704 1.00 72.76  ? 121 GLY B C   1 
ATOM   4088 O  O   . GLY B 2 123 ? 130.045 14.334  -16.298 1.00 75.83  ? 121 GLY B O   1 
ATOM   4089 N  N   . THR B 2 124 ? 129.663 12.733  -17.832 1.00 64.85  ? 122 THR B N   1 
ATOM   4090 C  CA  . THR B 2 124 ? 130.731 13.152  -18.727 1.00 66.90  ? 122 THR B CA  1 
ATOM   4091 C  C   . THR B 2 124 ? 130.142 13.545  -20.073 1.00 60.74  ? 122 THR B C   1 
ATOM   4092 O  O   . THR B 2 124 ? 129.220 12.896  -20.572 1.00 60.79  ? 122 THR B O   1 
ATOM   4093 C  CB  . THR B 2 124 ? 131.775 12.045  -18.915 1.00 63.62  ? 122 THR B CB  1 
ATOM   4094 O  OG1 . THR B 2 124 ? 132.685 12.420  -19.955 1.00 69.60  ? 122 THR B OG1 1 
ATOM   4095 C  CG2 . THR B 2 124 ? 131.104 10.728  -19.277 1.00 65.43  ? 122 THR B CG2 1 
ATOM   4096 N  N   . GLN B 2 125 ? 130.678 14.612  -20.657 1.00 62.49  ? 123 GLN B N   1 
ATOM   4097 C  CA  . GLN B 2 125 ? 130.155 15.132  -21.911 1.00 58.04  ? 123 GLN B CA  1 
ATOM   4098 C  C   . GLN B 2 125 ? 130.688 14.338  -23.096 1.00 61.65  ? 123 GLN B C   1 
ATOM   4099 O  O   . GLN B 2 125 ? 131.875 14.004  -23.159 1.00 69.94  ? 123 GLN B O   1 
ATOM   4100 C  CB  . GLN B 2 125 ? 130.517 16.610  -22.066 1.00 60.74  ? 123 GLN B CB  1 
ATOM   4101 C  CG  . GLN B 2 125 ? 130.160 17.205  -23.419 1.00 60.86  ? 123 GLN B CG  1 
ATOM   4102 C  CD  . GLN B 2 125 ? 128.674 17.137  -23.708 1.00 60.86  ? 123 GLN B CD  1 
ATOM   4103 O  OE1 . GLN B 2 125 ? 127.853 17.195  -22.796 1.00 63.00  ? 123 GLN B OE1 1 
ATOM   4104 N  NE2 . GLN B 2 125 ? 128.320 17.014  -24.982 1.00 64.59  ? 123 GLN B NE2 1 
ATOM   4105 N  N   . VAL B 2 126 ? 129.796 14.032  -24.034 1.00 61.24  ? 124 VAL B N   1 
ATOM   4106 C  CA  . VAL B 2 126 ? 130.141 13.391  -25.297 1.00 58.38  ? 124 VAL B CA  1 
ATOM   4107 C  C   . VAL B 2 126 ? 129.548 14.239  -26.410 1.00 60.33  ? 124 VAL B C   1 
ATOM   4108 O  O   . VAL B 2 126 ? 128.324 14.397  -26.487 1.00 65.42  ? 124 VAL B O   1 
ATOM   4109 C  CB  . VAL B 2 126 ? 129.617 11.947  -25.381 1.00 58.72  ? 124 VAL B CB  1 
ATOM   4110 C  CG1 . VAL B 2 126 ? 129.597 11.468  -26.824 1.00 60.44  ? 124 VAL B CG1 1 
ATOM   4111 C  CG2 . VAL B 2 126 ? 130.465 11.023  -24.522 1.00 61.16  ? 124 VAL B CG2 1 
ATOM   4112 N  N   . THR B 2 127 ? 130.407 14.791  -27.263 1.00 63.39  ? 125 THR B N   1 
ATOM   4113 C  CA  . THR B 2 127 ? 129.982 15.632  -28.375 1.00 67.35  ? 125 THR B CA  1 
ATOM   4114 C  C   . THR B 2 127 ? 130.447 15.000  -29.677 1.00 66.49  ? 125 THR B C   1 
ATOM   4115 O  O   . THR B 2 127 ? 131.653 14.887  -29.921 1.00 67.66  ? 125 THR B O   1 
ATOM   4116 C  CB  . THR B 2 127 ? 130.533 17.054  -28.239 1.00 65.72  ? 125 THR B CB  1 
ATOM   4117 O  OG1 . THR B 2 127 ? 130.308 17.534  -26.906 1.00 66.80  ? 125 THR B OG1 1 
ATOM   4118 C  CG2 . THR B 2 127 ? 129.854 17.985  -29.231 1.00 64.17  ? 125 THR B CG2 1 
ATOM   4119 N  N   . VAL B 2 128 ? 129.494 14.589  -30.505 1.00 63.35  ? 126 VAL B N   1 
ATOM   4120 C  CA  . VAL B 2 128 ? 129.780 13.967  -31.791 1.00 70.67  ? 126 VAL B CA  1 
ATOM   4121 C  C   . VAL B 2 128 ? 129.656 15.043  -32.861 1.00 74.04  ? 126 VAL B C   1 
ATOM   4122 O  O   . VAL B 2 128 ? 128.549 15.486  -33.185 1.00 74.42  ? 126 VAL B O   1 
ATOM   4123 C  CB  . VAL B 2 128 ? 128.838 12.789  -32.067 1.00 71.07  ? 126 VAL B CB  1 
ATOM   4124 C  CG1 . VAL B 2 128 ? 129.143 12.176  -33.424 1.00 67.87  ? 126 VAL B CG1 1 
ATOM   4125 C  CG2 . VAL B 2 128 ? 128.957 11.750  -30.967 1.00 66.28  ? 126 VAL B CG2 1 
ATOM   4126 N  N   . SER B 2 129 ? 130.791 15.468  -33.407 1.00 73.61  ? 127 SER B N   1 
ATOM   4127 C  CA  . SER B 2 129 ? 130.817 16.503  -34.434 1.00 69.07  ? 127 SER B CA  1 
ATOM   4128 C  C   . SER B 2 129 ? 130.087 16.056  -35.697 1.00 75.19  ? 127 SER B C   1 
ATOM   4129 O  O   . SER B 2 129 ? 130.493 15.095  -36.350 1.00 74.11  ? 127 SER B O   1 
ATOM   4130 C  CB  . SER B 2 129 ? 132.259 16.874  -34.771 1.00 69.06  ? 127 SER B CB  1 
ATOM   4131 O  OG  . SER B 2 129 ? 132.865 15.860  -35.553 1.00 72.73  ? 127 SER B OG  1 
HETATM 4132 C  C2  . MPG C 3 .   ? 82.417  26.251  18.666  1.00 45.94  ? 501 MPG A C2  1 
HETATM 4133 C  C3  . MPG C 3 .   ? 81.352  26.347  19.759  1.00 44.92  ? 501 MPG A C3  1 
HETATM 4134 C  C4  . MPG C 3 .   ? 79.950  26.153  19.176  1.00 46.56  ? 501 MPG A C4  1 
HETATM 4135 C  C5  . MPG C 3 .   ? 79.313  27.481  18.744  1.00 39.14  ? 501 MPG A C5  1 
HETATM 4136 C  C6  . MPG C 3 .   ? 77.986  27.275  17.996  1.00 43.41  ? 501 MPG A C6  1 
HETATM 4137 C  C7  . MPG C 3 .   ? 78.157  27.319  16.467  1.00 42.35  ? 501 MPG A C7  1 
HETATM 4138 C  C8  . MPG C 3 .   ? 76.810  27.238  15.726  1.00 47.69  ? 501 MPG A C8  1 
HETATM 4139 C  C9  . MPG C 3 .   ? 76.797  27.913  14.387  1.00 48.77  ? 501 MPG A C9  1 
HETATM 4140 C  C10 . MPG C 3 .   ? 76.227  29.109  14.203  1.00 54.33  ? 501 MPG A C10 1 
HETATM 4141 C  C11 . MPG C 3 .   ? 75.716  29.568  12.870  1.00 52.94  ? 501 MPG A C11 1 
HETATM 4142 C  C12 . MPG C 3 .   ? 74.204  29.348  12.702  1.00 59.04  ? 501 MPG A C12 1 
HETATM 4143 C  C13 . MPG C 3 .   ? 73.419  29.910  13.895  1.00 65.29  ? 501 MPG A C13 1 
HETATM 4144 C  C14 . MPG C 3 .   ? 71.938  29.510  13.849  1.00 66.85  ? 501 MPG A C14 1 
HETATM 4145 C  C15 . MPG C 3 .   ? 71.768  28.065  13.373  1.00 64.21  ? 501 MPG A C15 1 
HETATM 4146 C  C16 . MPG C 3 .   ? 70.321  27.587  13.513  1.00 67.08  ? 501 MPG A C16 1 
HETATM 4147 C  C17 . MPG C 3 .   ? 69.755  27.169  12.155  1.00 64.99  ? 501 MPG A C17 1 
HETATM 4148 C  C18 . MPG C 3 .   ? 69.855  28.287  11.130  1.00 57.95  ? 501 MPG A C18 1 
HETATM 4149 O  O1  . MPG C 3 .   ? 84.214  27.788  18.569  1.00 49.69  ? 501 MPG A O1  1 
HETATM 4150 C  C1  . MPG C 3 .   ? 82.843  27.660  18.238  1.00 47.62  ? 501 MPG A C1  1 
HETATM 4151 C  CXD . MPG C 3 .   ? 85.304  29.858  19.119  1.00 47.47  ? 501 MPG A CXD 1 
HETATM 4152 O  O2  . MPG C 3 .   ? 86.115  30.149  20.215  1.00 60.66  ? 501 MPG A O2  1 
HETATM 4153 C  C21 . MPG C 3 .   ? 84.304  31.028  18.962  1.00 56.77  ? 501 MPG A C21 1 
HETATM 4154 O  O3  . MPG C 3 .   ? 85.061  32.166  19.259  1.00 52.89  ? 501 MPG A O3  1 
HETATM 4155 O  O4  . MPG C 3 .   ? 84.196  28.401  20.728  1.00 62.56  ? 501 MPG A O4  1 
HETATM 4156 C  CX3 . MPG C 3 .   ? 84.525  28.635  19.579  1.00 49.58  ? 501 MPG A CX3 1 
HETATM 4157 C  C2  . MPG D 3 .   ? 90.348  9.006   3.027   1.00 71.19  ? 502 MPG A C2  1 
HETATM 4158 C  C3  . MPG D 3 .   ? 89.546  10.257  3.392   1.00 66.51  ? 502 MPG A C3  1 
HETATM 4159 C  C4  . MPG D 3 .   ? 89.935  11.464  2.533   1.00 53.13  ? 502 MPG A C4  1 
HETATM 4160 C  C5  . MPG D 3 .   ? 88.744  12.413  2.343   1.00 48.96  ? 502 MPG A C5  1 
HETATM 4161 C  C6  . MPG D 3 .   ? 89.032  13.841  2.829   1.00 39.76  ? 502 MPG A C6  1 
HETATM 4162 C  C7  . MPG D 3 .   ? 87.748  14.685  2.906   1.00 44.78  ? 502 MPG A C7  1 
HETATM 4163 C  C8  . MPG D 3 .   ? 86.748  14.152  3.948   1.00 44.35  ? 502 MPG A C8  1 
HETATM 4164 C  C9  . MPG D 3 .   ? 86.837  14.846  5.276   1.00 44.52  ? 502 MPG A C9  1 
HETATM 4165 C  C10 . MPG D 3 .   ? 86.566  14.240  6.436   1.00 42.24  ? 502 MPG A C10 1 
HETATM 4166 C  C11 . MPG D 3 .   ? 87.079  14.791  7.734   1.00 44.87  ? 502 MPG A C11 1 
HETATM 4167 C  C12 . MPG D 3 .   ? 86.712  16.269  7.949   1.00 51.39  ? 502 MPG A C12 1 
HETATM 4168 C  C13 . MPG D 3 .   ? 87.781  17.060  8.716   1.00 50.97  ? 502 MPG A C13 1 
HETATM 4169 C  C14 . MPG D 3 .   ? 87.421  18.544  8.872   1.00 48.92  ? 502 MPG A C14 1 
HETATM 4170 C  C15 . MPG D 3 .   ? 87.833  19.356  7.640   1.00 54.11  ? 502 MPG A C15 1 
HETATM 4171 C  C16 . MPG D 3 .   ? 87.118  20.707  7.551   1.00 54.77  ? 502 MPG A C16 1 
HETATM 4172 C  C17 . MPG D 3 .   ? 87.261  21.322  6.157   1.00 57.10  ? 502 MPG A C17 1 
HETATM 4173 C  C18 . MPG D 3 .   ? 85.948  21.340  5.389   1.00 47.33  ? 502 MPG A C18 1 
HETATM 4174 O  O1  . MPG D 3 .   ? 90.399  7.963   5.164   1.00 68.47  ? 502 MPG A O1  1 
HETATM 4175 C  C1  . MPG D 3 .   ? 89.860  7.816   3.862   1.00 68.56  ? 502 MPG A C1  1 
HETATM 4176 C  CXD . MPG D 3 .   ? 90.294  7.226   7.445   1.00 59.93  ? 502 MPG A CXD 1 
HETATM 4177 O  O2  . MPG D 3 .   ? 89.274  6.875   8.329   1.00 66.18  ? 502 MPG A O2  1 
HETATM 4178 C  C21 . MPG D 3 .   ? 91.063  8.421   8.058   1.00 66.92  ? 502 MPG A C21 1 
HETATM 4179 O  O3  . MPG D 3 .   ? 91.573  7.889   9.247   1.00 56.43  ? 502 MPG A O3  1 
HETATM 4180 O  O4  . MPG D 3 .   ? 88.362  7.796   6.068   1.00 55.40  ? 502 MPG A O4  1 
HETATM 4181 C  CX3 . MPG D 3 .   ? 89.562  7.685   6.192   1.00 54.13  ? 502 MPG A CX3 1 
HETATM 4182 C  C2  . MPG E 3 .   ? 107.018 -7.284  9.057   1.00 82.54  ? 503 MPG A C2  1 
HETATM 4183 C  C3  . MPG E 3 .   ? 105.583 -7.271  9.589   1.00 64.04  ? 503 MPG A C3  1 
HETATM 4184 C  C4  . MPG E 3 .   ? 104.635 -6.477  8.684   1.00 62.81  ? 503 MPG A C4  1 
HETATM 4185 C  C5  . MPG E 3 .   ? 103.189 -6.483  9.200   1.00 63.19  ? 503 MPG A C5  1 
HETATM 4186 C  C6  . MPG E 3 .   ? 102.416 -5.164  9.035   1.00 54.72  ? 503 MPG A C6  1 
HETATM 4187 C  C7  . MPG E 3 .   ? 101.221 -5.047  9.998   1.00 51.73  ? 503 MPG A C7  1 
HETATM 4188 C  C8  . MPG E 3 .   ? 100.214 -6.204  9.851   1.00 51.01  ? 503 MPG A C8  1 
HETATM 4189 C  C9  . MPG E 3 .   ? 98.785  -5.887  10.181  1.00 49.92  ? 503 MPG A C9  1 
HETATM 4190 C  C10 . MPG E 3 .   ? 98.315  -5.973  11.430  1.00 52.29  ? 503 MPG A C10 1 
HETATM 4191 C  C11 . MPG E 3 .   ? 96.855  -6.078  11.753  1.00 44.95  ? 503 MPG A C11 1 
HETATM 4192 C  C12 . MPG E 3 .   ? 96.397  -5.145  12.888  1.00 55.37  ? 503 MPG A C12 1 
HETATM 4193 C  C13 . MPG E 3 .   ? 96.062  -3.732  12.389  1.00 52.53  ? 503 MPG A C13 1 
HETATM 4194 C  C14 . MPG E 3 .   ? 95.580  -2.810  13.516  1.00 53.61  ? 503 MPG A C14 1 
HETATM 4195 C  C15 . MPG E 3 .   ? 96.713  -2.396  14.459  1.00 46.43  ? 503 MPG A C15 1 
HETATM 4196 C  C16 . MPG E 3 .   ? 96.165  -1.865  15.786  1.00 52.53  ? 503 MPG A C16 1 
HETATM 4197 C  C17 . MPG E 3 .   ? 97.293  -1.354  16.684  1.00 55.53  ? 503 MPG A C17 1 
HETATM 4198 C  C18 . MPG E 3 .   ? 96.796  -1.009  18.079  1.00 43.52  ? 503 MPG A C18 1 
HETATM 4199 O  O1  . MPG E 3 .   ? 109.309 -7.610  9.651   1.00 87.39  ? 503 MPG A O1  1 
HETATM 4200 C  C1  . MPG E 3 .   ? 107.987 -7.866  10.094  1.00 80.22  ? 503 MPG A C1  1 
HETATM 4201 C  CXD . MPG E 3 .   ? 111.688 -8.028  9.766   1.00 81.36  ? 503 MPG A CXD 1 
HETATM 4202 O  O2  . MPG E 3 .   ? 112.112 -7.608  11.026  1.00 80.07  ? 503 MPG A O2  1 
HETATM 4203 C  C21 . MPG E 3 .   ? 111.669 -6.799  8.827   1.00 80.31  ? 503 MPG A C21 1 
HETATM 4204 O  O3  . MPG E 3 .   ? 112.989 -6.342  8.868   1.00 77.64  ? 503 MPG A O3  1 
HETATM 4205 O  O4  . MPG E 3 .   ? 109.966 -9.606  10.437  1.00 86.07  ? 503 MPG A O4  1 
HETATM 4206 C  CX3 . MPG E 3 .   ? 110.261 -8.510  9.997   1.00 87.32  ? 503 MPG A CX3 1 
HETATM 4207 C  C2  . MPG F 3 .   ? 94.594  20.644  1.391   1.00 57.60  ? 504 MPG A C2  1 
HETATM 4208 C  C3  . MPG F 3 .   ? 93.651  21.840  1.264   1.00 50.40  ? 504 MPG A C3  1 
HETATM 4209 C  C4  . MPG F 3 .   ? 93.196  22.045  -0.183  1.00 51.32  ? 504 MPG A C4  1 
HETATM 4210 C  C5  . MPG F 3 .   ? 91.857  22.791  -0.236  1.00 46.22  ? 504 MPG A C5  1 
HETATM 4211 C  C6  . MPG F 3 .   ? 91.371  23.057  -1.670  1.00 47.74  ? 504 MPG A C6  1 
HETATM 4212 C  C7  . MPG F 3 .   ? 92.098  24.236  -2.340  1.00 47.34  ? 504 MPG A C7  1 
HETATM 4213 C  C8  . MPG F 3 .   ? 91.439  24.719  -3.646  1.00 44.09  ? 504 MPG A C8  1 
HETATM 4214 C  C9  . MPG F 3 .   ? 92.027  25.993  -4.178  1.00 47.57  ? 504 MPG A C9  1 
HETATM 4215 C  C10 . MPG F 3 .   ? 92.869  26.000  -5.217  1.00 60.26  ? 504 MPG A C10 1 
HETATM 4216 C  C11 . MPG F 3 .   ? 94.271  26.530  -5.143  1.00 67.07  ? 504 MPG A C11 1 
HETATM 4217 C  C12 . MPG F 3 .   ? 95.330  25.519  -4.670  1.00 62.89  ? 504 MPG A C12 1 
HETATM 4218 C  C13 . MPG F 3 .   ? 95.475  25.492  -3.141  1.00 56.40  ? 504 MPG A C13 1 
HETATM 4219 C  C14 . MPG F 3 .   ? 96.601  24.556  -2.684  1.00 62.33  ? 504 MPG A C14 1 
HETATM 4220 C  C15 . MPG F 3 .   ? 96.646  24.419  -1.160  1.00 58.22  ? 504 MPG A C15 1 
HETATM 4221 C  C16 . MPG F 3 .   ? 97.789  23.506  -0.708  1.00 65.17  ? 504 MPG A C16 1 
HETATM 4222 C  C17 . MPG F 3 .   ? 97.772  23.309  0.809   1.00 59.05  ? 504 MPG A C17 1 
HETATM 4223 C  C18 . MPG F 3 .   ? 98.841  22.324  1.252   1.00 56.27  ? 504 MPG A C18 1 
HETATM 4224 O  O1  . MPG F 3 .   ? 95.483  19.082  2.952   1.00 68.14  ? 504 MPG A O1  1 
HETATM 4225 C  C1  . MPG F 3 .   ? 94.642  20.218  2.863   1.00 66.86  ? 504 MPG A C1  1 
HETATM 4226 C  CXD . MPG F 3 .   ? 96.481  17.269  4.173   1.00 71.46  ? 504 MPG A CXD 1 
HETATM 4227 O  O2  . MPG F 3 .   ? 95.846  16.373  5.032   1.00 77.34  ? 504 MPG A O2  1 
HETATM 4228 C  C21 . MPG F 3 .   ? 97.811  17.716  4.826   1.00 73.28  ? 504 MPG A C21 1 
HETATM 4229 O  O3  . MPG F 3 .   ? 98.420  16.528  5.242   1.00 74.86  ? 504 MPG A O3  1 
HETATM 4230 O  O4  . MPG F 3 .   ? 94.900  18.870  5.107   1.00 75.65  ? 504 MPG A O4  1 
HETATM 4231 C  CX3 . MPG F 3 .   ? 95.543  18.468  4.159   1.00 74.03  ? 504 MPG A CX3 1 
HETATM 4232 C  C2  . MPG G 3 .   ? 100.201 3.618   3.717   1.00 65.84  ? 505 MPG A C2  1 
HETATM 4233 C  C3  . MPG G 3 .   ? 101.630 4.048   4.053   1.00 56.43  ? 505 MPG A C3  1 
HETATM 4234 C  C4  . MPG G 3 .   ? 101.933 3.803   5.534   1.00 63.74  ? 505 MPG A C4  1 
HETATM 4235 C  C5  . MPG G 3 .   ? 102.044 5.098   6.351   1.00 62.39  ? 505 MPG A C5  1 
HETATM 4236 C  C6  . MPG G 3 .   ? 100.691 5.796   6.562   1.00 71.98  ? 505 MPG A C6  1 
HETATM 4237 C  C7  . MPG G 3 .   ? 100.670 7.231   6.007   1.00 72.44  ? 505 MPG A C7  1 
HETATM 4238 C  C8  . MPG G 3 .   ? 101.838 8.097   6.516   1.00 75.97  ? 505 MPG A C8  1 
HETATM 4239 C  C9  . MPG G 3 .   ? 102.342 9.110   5.528   1.00 72.41  ? 505 MPG A C9  1 
HETATM 4240 C  C10 . MPG G 3 .   ? 103.637 9.355   5.299   1.00 69.98  ? 505 MPG A C10 1 
HETATM 4241 C  C11 . MPG G 3 .   ? 104.763 8.513   5.825   1.00 66.44  ? 505 MPG A C11 1 
HETATM 4242 C  C12 . MPG G 3 .   ? 105.235 8.845   7.251   1.00 70.21  ? 505 MPG A C12 1 
HETATM 4243 C  C13 . MPG G 3 .   ? 105.357 10.355  7.496   1.00 79.41  ? 505 MPG A C13 1 
HETATM 4244 C  C14 . MPG G 3 .   ? 104.431 10.813  8.629   1.00 72.25  ? 505 MPG A C14 1 
HETATM 4245 C  C15 . MPG G 3 .   ? 103.849 12.201  8.350   1.00 76.35  ? 505 MPG A C15 1 
HETATM 4246 C  C16 . MPG G 3 .   ? 102.686 12.522  9.291   1.00 68.63  ? 505 MPG A C16 1 
HETATM 4247 C  C17 . MPG G 3 .   ? 101.396 12.732  8.498   1.00 71.52  ? 505 MPG A C17 1 
HETATM 4248 C  C18 . MPG G 3 .   ? 100.933 11.451  7.823   1.00 72.75  ? 505 MPG A C18 1 
HETATM 4249 O  O1  . MPG G 3 .   ? 100.549 4.800   1.722   1.00 69.20  ? 505 MPG A O1  1 
HETATM 4250 C  C1  . MPG G 3 .   ? 99.999  3.586   2.198   1.00 55.77  ? 505 MPG A C1  1 
HETATM 4251 C  CXD . MPG G 3 .   ? 99.760  7.042   1.986   1.00 72.18  ? 505 MPG A CXD 1 
HETATM 4252 O  O2  . MPG G 3 .   ? 99.106  7.929   1.132   1.00 74.36  ? 505 MPG A O2  1 
HETATM 4253 C  C21 . MPG G 3 .   ? 101.248 7.458   2.071   1.00 69.26  ? 505 MPG A C21 1 
HETATM 4254 O  O3  . MPG G 3 .   ? 101.185 8.740   2.628   1.00 71.49  ? 505 MPG A O3  1 
HETATM 4255 O  O4  . MPG G 3 .   ? 98.901  5.451   0.338   1.00 54.43  ? 505 MPG A O4  1 
HETATM 4256 C  CX3 . MPG G 3 .   ? 99.668  5.713   1.250   1.00 66.65  ? 505 MPG A CX3 1 
HETATM 4257 C  C2  . MPG H 3 .   ? 100.840 4.538   11.287  1.00 73.21  ? 506 MPG A C2  1 
HETATM 4258 C  C3  . MPG H 3 .   ? 100.331 5.198   12.568  1.00 63.74  ? 506 MPG A C3  1 
HETATM 4259 C  C4  . MPG H 3 .   ? 98.983  4.621   13.007  1.00 54.35  ? 506 MPG A C4  1 
HETATM 4260 C  C5  . MPG H 3 .   ? 98.597  5.136   14.401  1.00 53.32  ? 506 MPG A C5  1 
HETATM 4261 C  C6  . MPG H 3 .   ? 97.080  5.169   14.650  1.00 56.63  ? 506 MPG A C6  1 
HETATM 4262 C  C7  . MPG H 3 .   ? 96.575  3.918   15.390  1.00 52.64  ? 506 MPG A C7  1 
HETATM 4263 C  C8  . MPG H 3 .   ? 95.263  4.156   16.161  1.00 50.59  ? 506 MPG A C8  1 
HETATM 4264 C  C9  . MPG H 3 .   ? 94.741  2.940   16.870  1.00 54.66  ? 506 MPG A C9  1 
HETATM 4265 C  C10 . MPG H 3 .   ? 94.888  2.752   18.186  1.00 61.44  ? 506 MPG A C10 1 
HETATM 4266 C  C11 . MPG H 3 .   ? 95.816  3.573   19.034  1.00 60.57  ? 506 MPG A C11 1 
HETATM 4267 C  C12 . MPG H 3 .   ? 97.304  3.196   18.942  1.00 60.96  ? 506 MPG A C12 1 
HETATM 4268 C  C13 . MPG H 3 .   ? 98.210  4.117   19.772  1.00 53.82  ? 506 MPG A C13 1 
HETATM 4269 C  C14 . MPG H 3 .   ? 98.337  5.532   19.193  1.00 51.79  ? 506 MPG A C14 1 
HETATM 4270 C  C15 . MPG H 3 .   ? 98.867  6.516   20.242  1.00 53.18  ? 506 MPG A C15 1 
HETATM 4271 C  C16 . MPG H 3 .   ? 98.915  7.952   19.717  1.00 51.65  ? 506 MPG A C16 1 
HETATM 4272 C  C17 . MPG H 3 .   ? 98.637  8.954   20.838  1.00 44.95  ? 506 MPG A C17 1 
HETATM 4273 C  C18 . MPG H 3 .   ? 99.889  9.274   21.639  1.00 39.37  ? 506 MPG A C18 1 
HETATM 4274 O  O1  . MPG H 3 .   ? 103.121 5.225   11.436  1.00 85.48  ? 506 MPG A O1  1 
HETATM 4275 C  C1  . MPG H 3 .   ? 101.945 5.400   10.665  1.00 82.90  ? 506 MPG A C1  1 
HETATM 4276 C  CXD . MPG H 3 .   ? 105.444 5.681   11.866  1.00 91.99  ? 506 MPG A CXD 1 
HETATM 4277 O  O2  . MPG H 3 .   ? 106.136 6.868   11.629  1.00 94.04  ? 506 MPG A O2  1 
HETATM 4278 C  C21 . MPG H 3 .   ? 106.330 4.504   11.391  1.00 94.29  ? 506 MPG A C21 1 
HETATM 4279 O  O3  . MPG H 3 .   ? 107.605 4.803   11.882  1.00 94.94  ? 506 MPG A O3  1 
HETATM 4280 O  O4  . MPG H 3 .   ? 104.264 6.287   9.823   1.00 88.92  ? 506 MPG A O4  1 
HETATM 4281 C  CX3 . MPG H 3 .   ? 104.249 5.776   10.927  1.00 90.50  ? 506 MPG A CX3 1 
HETATM 4282 C  C2  . MPG I 3 .   ? 91.066  17.694  9.747   1.00 64.07  ? 507 MPG A C2  1 
HETATM 4283 C  C3  . MPG I 3 .   ? 91.325  18.599  10.953  1.00 64.11  ? 507 MPG A C3  1 
HETATM 4284 C  C4  . MPG I 3 .   ? 90.016  19.128  11.547  1.00 57.77  ? 507 MPG A C4  1 
HETATM 4285 C  C5  . MPG I 3 .   ? 89.188  18.035  12.237  1.00 52.48  ? 507 MPG A C5  1 
HETATM 4286 C  C6  . MPG I 3 .   ? 88.022  18.606  13.063  1.00 49.31  ? 507 MPG A C6  1 
HETATM 4287 C  C7  . MPG I 3 .   ? 87.254  19.719  12.327  1.00 43.98  ? 507 MPG A C7  1 
HETATM 4288 C  C8  . MPG I 3 .   ? 86.339  20.550  13.244  1.00 47.49  ? 507 MPG A C8  1 
HETATM 4289 C  C9  . MPG I 3 .   ? 86.399  22.033  13.012  1.00 43.00  ? 507 MPG A C9  1 
HETATM 4290 C  C10 . MPG I 3 .   ? 87.330  22.823  13.557  1.00 53.35  ? 507 MPG A C10 1 
HETATM 4291 C  C11 . MPG I 3 .   ? 87.793  22.712  14.980  1.00 64.79  ? 507 MPG A C11 1 
HETATM 4292 C  C12 . MPG I 3 .   ? 88.904  21.688  15.278  1.00 60.87  ? 507 MPG A C12 1 
HETATM 4293 C  C13 . MPG I 3 .   ? 90.156  21.855  14.404  1.00 58.66  ? 507 MPG A C13 1 
HETATM 4294 C  C14 . MPG I 3 .   ? 91.239  20.818  14.732  1.00 57.58  ? 507 MPG A C14 1 
HETATM 4295 C  C15 . MPG I 3 .   ? 92.395  20.843  13.726  1.00 65.51  ? 507 MPG A C15 1 
HETATM 4296 C  C16 . MPG I 3 .   ? 93.335  19.642  13.861  1.00 55.85  ? 507 MPG A C16 1 
HETATM 4297 C  C17 . MPG I 3 .   ? 94.740  19.969  13.352  1.00 56.72  ? 507 MPG A C17 1 
HETATM 4298 C  C18 . MPG I 3 .   ? 94.704  20.646  11.992  1.00 58.11  ? 507 MPG A C18 1 
HETATM 4299 O  O1  . MPG I 3 .   ? 93.260  16.798  9.628   1.00 88.89  ? 507 MPG A O1  1 
HETATM 4300 C  C1  . MPG I 3 .   ? 92.327  17.563  8.886   1.00 76.61  ? 507 MPG A C1  1 
HETATM 4301 C  CXD . MPG I 3 .   ? 95.506  16.389  10.347  1.00 87.35  ? 507 MPG A CXD 1 
HETATM 4302 O  O2  . MPG I 3 .   ? 96.596  17.258  10.319  1.00 90.30  ? 507 MPG A O2  1 
HETATM 4303 C  C21 . MPG I 3 .   ? 95.956  15.007  9.817   1.00 84.93  ? 507 MPG A C21 1 
HETATM 4304 O  O3  . MPG I 3 .   ? 97.043  14.671  10.629  1.00 85.13  ? 507 MPG A O3  1 
HETATM 4305 O  O4  . MPG I 3 .   ? 94.903  17.546  8.286   1.00 85.88  ? 507 MPG A O4  1 
HETATM 4306 C  CX3 . MPG I 3 .   ? 94.563  16.977  9.307   1.00 88.28  ? 507 MPG A CX3 1 
HETATM 4307 N  N1  . LOP J 4 .   ? 104.479 6.874   37.650  1.00 77.47  ? 508 LOP A N1  1 
HETATM 4308 C  C1  . LOP J 4 .   ? 104.346 6.988   36.194  1.00 83.42  ? 508 LOP A C1  1 
HETATM 4309 C  C2  . LOP J 4 .   ? 104.237 8.424   35.750  1.00 93.60  ? 508 LOP A C2  1 
HETATM 4310 O  O1  . LOP J 4 .   ? 104.111 8.501   34.300  1.00 103.13 ? 508 LOP A O1  1 
HETATM 4311 P  P1  . LOP J 4 .   ? 104.006 9.941   33.592  1.00 121.09 ? 508 LOP A P1  1 
HETATM 4312 O  O2  . LOP J 4 .   ? 102.661 10.557  34.219  1.00 89.86  ? 508 LOP A O2  1 
HETATM 4313 O  O3  . LOP J 4 .   ? 105.162 10.782  34.064  1.00 109.78 ? 508 LOP A O3  1 
HETATM 4314 O  O4  . LOP J 4 .   ? 103.783 9.737   32.118  1.00 86.17  ? 508 LOP A O4  1 
HETATM 4315 C  C3  . LOP J 4 .   ? 102.251 11.899  33.834  1.00 80.70  ? 508 LOP A C3  1 
HETATM 4316 C  C4  . LOP J 4 .   ? 100.926 12.312  34.440  1.00 80.38  ? 508 LOP A C4  1 
HETATM 4317 C  C5  . LOP J 4 .   ? 100.576 13.750  34.128  1.00 72.26  ? 508 LOP A C5  1 
HETATM 4318 O  O5  . LOP J 4 .   ? 99.820  11.456  34.026  1.00 87.37  ? 508 LOP A O5  1 
HETATM 4319 O  O6  . LOP J 4 .   ? 99.148  13.942  34.243  1.00 77.33  ? 508 LOP A O6  1 
HETATM 4320 C  C6  . LOP J 4 .   ? 99.665  10.248  34.600  1.00 80.59  ? 508 LOP A C6  1 
HETATM 4321 O  O7  . LOP J 4 .   ? 100.406 9.810   35.443  1.00 86.64  ? 508 LOP A O7  1 
HETATM 4322 C  C7  . LOP J 4 .   ? 98.434  9.530   34.114  1.00 65.45  ? 508 LOP A C7  1 
HETATM 4323 C  C8  . LOP J 4 .   ? 98.267  9.563   32.625  1.00 62.19  ? 508 LOP A C8  1 
HETATM 4324 C  C9  . LOP J 4 .   ? 96.914  9.035   32.182  1.00 56.98  ? 508 LOP A C9  1 
HETATM 4325 C  C10 . LOP J 4 .   ? 96.542  9.372   30.758  1.00 50.63  ? 508 LOP A C10 1 
HETATM 4326 C  C11 . LOP J 4 .   ? 95.083  9.140   30.448  1.00 55.22  ? 508 LOP A C11 1 
HETATM 4327 C  C12 . LOP J 4 .   ? 94.584  9.832   29.188  1.00 48.41  ? 508 LOP A C12 1 
HETATM 4328 C  C13 . LOP J 4 .   ? 93.091  9.881   29.084  1.00 50.27  ? 508 LOP A C13 1 
HETATM 4329 C  C14 . LOP J 4 .   ? 92.449  10.447  30.313  1.00 49.72  ? 508 LOP A C14 1 
HETATM 4330 C  C15 . LOP J 4 .   ? 91.749  11.551  30.407  1.00 58.38  ? 508 LOP A C15 1 
HETATM 4331 C  C16 . LOP J 4 .   ? 91.156  12.068  31.682  1.00 55.73  ? 508 LOP A C16 1 
HETATM 4332 C  C17 . LOP J 4 .   ? 90.589  13.455  31.582  1.00 61.14  ? 508 LOP A C17 1 
HETATM 4333 C  C18 . LOP J 4 .   ? 89.281  13.566  30.813  1.00 60.21  ? 508 LOP A C18 1 
HETATM 4334 C  C19 . LOP J 4 .   ? 88.645  14.937  30.881  1.00 58.61  ? 508 LOP A C19 1 
HETATM 4335 C  C20 . LOP J 4 .   ? 87.215  14.991  30.392  1.00 58.20  ? 508 LOP A C20 1 
HETATM 4336 C  C21 . LOP J 4 .   ? 86.522  16.307  30.659  1.00 55.52  ? 508 LOP A C21 1 
HETATM 4337 C  C22 . LOP J 4 .   ? 85.054  16.334  30.322  1.00 56.92  ? 508 LOP A C22 1 
HETATM 4338 C  C23 . LOP J 4 .   ? 84.374  17.629  30.700  1.00 60.16  ? 508 LOP A C23 1 
HETATM 4339 C  C24 . LOP J 4 .   ? 98.721  15.189  34.069  1.00 73.28  ? 508 LOP A C24 1 
HETATM 4340 O  O8  . LOP J 4 .   ? 99.462  16.118  33.888  1.00 78.56  ? 508 LOP A O8  1 
HETATM 4341 C  C25 . LOP J 4 .   ? 97.220  15.282  34.079  1.00 68.60  ? 508 LOP A C25 1 
HETATM 4342 C  C26 . LOP J 4 .   ? 96.724  16.689  33.924  1.00 67.33  ? 508 LOP A C26 1 
HETATM 4343 C  C27 . LOP J 4 .   ? 95.222  16.764  33.701  1.00 73.67  ? 508 LOP A C27 1 
HETATM 4344 C  C28 . LOP J 4 .   ? 94.692  18.171  33.546  1.00 70.07  ? 508 LOP A C28 1 
HETATM 4345 C  C29 . LOP J 4 .   ? 93.308  18.255  32.944  1.00 70.63  ? 508 LOP A C29 1 
HETATM 4346 C  C30 . LOP J 4 .   ? 92.204  17.676  33.792  1.00 68.56  ? 508 LOP A C30 1 
HETATM 4347 C  C31 . LOP J 4 .   ? 90.839  17.706  33.137  1.00 68.76  ? 508 LOP A C31 1 
HETATM 4348 C  C32 . LOP J 4 .   ? 90.382  19.080  32.692  1.00 61.45  ? 508 LOP A C32 1 
HETATM 4349 C  C33 . LOP J 4 .   ? 88.997  19.109  32.078  1.00 69.38  ? 508 LOP A C33 1 
HETATM 4350 C  C34 . LOP J 4 .   ? 88.544  20.460  31.572  1.00 61.74  ? 508 LOP A C34 1 
HETATM 4351 C  C35 . LOP J 4 .   ? 87.145  20.486  30.993  1.00 49.44  ? 508 LOP A C35 1 
HETATM 4352 C  C1  . OCT K 5 .   ? 83.547  24.188  -14.243 1.00 51.55  ? 509 OCT A C1  1 
HETATM 4353 C  C2  . OCT K 5 .   ? 83.717  24.059  -12.748 1.00 48.96  ? 509 OCT A C2  1 
HETATM 4354 C  C3  . OCT K 5 .   ? 85.112  24.350  -12.255 1.00 43.92  ? 509 OCT A C3  1 
HETATM 4355 C  C4  . OCT K 5 .   ? 85.254  24.265  -10.752 1.00 51.41  ? 509 OCT A C4  1 
HETATM 4356 C  C5  . OCT K 5 .   ? 86.629  24.611  -10.234 1.00 51.88  ? 509 OCT A C5  1 
HETATM 4357 C  C6  . OCT K 5 .   ? 86.758  24.546  -8.728  1.00 57.03  ? 509 OCT A C6  1 
HETATM 4358 C  C7  . OCT K 5 .   ? 85.920  25.546  -7.976  1.00 57.88  ? 509 OCT A C7  1 
HETATM 4359 C  C8  . OCT K 5 .   ? 86.084  25.486  -6.474  1.00 54.16  ? 509 OCT A C8  1 
HETATM 4360 C  C1  . OCT L 5 .   ? 95.433  -7.966  1.420   1.00 41.10  ? 510 OCT A C1  1 
HETATM 4361 C  C2  . OCT L 5 .   ? 95.010  -8.089  2.868   1.00 44.58  ? 510 OCT A C2  1 
HETATM 4362 C  C3  . OCT L 5 .   ? 95.530  -6.982  3.753   1.00 48.58  ? 510 OCT A C3  1 
HETATM 4363 C  C4  . OCT L 5 .   ? 95.144  -7.049  5.211   1.00 44.09  ? 510 OCT A C4  1 
HETATM 4364 C  C5  . OCT L 5 .   ? 95.659  -5.891  6.034   1.00 45.31  ? 510 OCT A C5  1 
HETATM 4365 C  C6  . OCT L 5 .   ? 95.295  -5.950  7.497   1.00 40.98  ? 510 OCT A C6  1 
HETATM 4366 C  C7  . OCT L 5 .   ? 93.817  -5.993  7.769   1.00 40.71  ? 510 OCT A C7  1 
HETATM 4367 C  C8  . OCT L 5 .   ? 93.481  -6.005  9.243   1.00 49.33  ? 510 OCT A C8  1 
HETATM 4368 C  C1  . OCT M 5 .   ? 73.722  23.612  -16.766 1.00 54.93  ? 511 OCT A C1  1 
HETATM 4369 C  C2  . OCT M 5 .   ? 75.156  23.489  -16.309 1.00 60.15  ? 511 OCT A C2  1 
HETATM 4370 C  C3  . OCT M 5 .   ? 75.951  22.457  -17.066 1.00 54.64  ? 511 OCT A C3  1 
HETATM 4371 C  C4  . OCT M 5 .   ? 77.345  22.216  -16.537 1.00 47.41  ? 511 OCT A C4  1 
HETATM 4372 C  C5  . OCT M 5 .   ? 78.119  21.174  -17.307 1.00 46.34  ? 511 OCT A C5  1 
HETATM 4373 C  C6  . OCT M 5 .   ? 79.479  20.854  -16.735 1.00 51.99  ? 511 OCT A C6  1 
HETATM 4374 C  C7  . OCT M 5 .   ? 80.453  22.003  -16.680 1.00 49.40  ? 511 OCT A C7  1 
HETATM 4375 C  C8  . OCT M 5 .   ? 81.816  21.600  -16.165 1.00 48.65  ? 511 OCT A C8  1 
HETATM 4376 C  C1  . OCT N 5 .   ? 75.460  -4.304  16.549  1.00 48.76  ? 512 OCT A C1  1 
HETATM 4377 C  C2  . OCT N 5 .   ? 75.447  -4.044  18.038  1.00 48.63  ? 512 OCT A C2  1 
HETATM 4378 C  C3  . OCT N 5 .   ? 76.716  -4.450  18.744  1.00 47.77  ? 512 OCT A C3  1 
HETATM 4379 C  C4  . OCT N 5 .   ? 76.679  -4.278  20.243  1.00 49.96  ? 512 OCT A C4  1 
HETATM 4380 C  C5  . OCT N 5 .   ? 77.969  -4.631  20.949  1.00 49.54  ? 512 OCT A C5  1 
HETATM 4381 C  C6  . OCT N 5 .   ? 79.154  -3.758  20.586  1.00 45.26  ? 512 OCT A C6  1 
HETATM 4382 C  C7  . OCT N 5 .   ? 80.413  -4.094  21.354  1.00 51.20  ? 512 OCT A C7  1 
HETATM 4383 C  C8  . OCT N 5 .   ? 81.664  -3.350  20.940  1.00 44.70  ? 512 OCT A C8  1 
HETATM 4384 C  C1  . OCT O 5 .   ? 82.078  9.994   -13.882 1.00 52.81  ? 513 OCT A C1  1 
HETATM 4385 C  C2  . OCT O 5 .   ? 83.520  9.681   -14.211 1.00 52.24  ? 513 OCT A C2  1 
HETATM 4386 C  C3  . OCT O 5 .   ? 84.422  9.587   -13.007 1.00 51.42  ? 513 OCT A C3  1 
HETATM 4387 C  C4  . OCT O 5 .   ? 85.866  9.284   -13.329 1.00 55.99  ? 513 OCT A C4  1 
HETATM 4388 C  C5  . OCT O 5 .   ? 86.772  9.236   -12.124 1.00 49.52  ? 513 OCT A C5  1 
HETATM 4389 C  C6  . OCT O 5 .   ? 88.233  9.019   -12.439 1.00 51.27  ? 513 OCT A C6  1 
HETATM 4390 C  C7  . OCT O 5 .   ? 88.558  7.689   -13.069 1.00 58.64  ? 513 OCT A C7  1 
HETATM 4391 C  C8  . OCT O 5 .   ? 90.013  7.548   -13.451 1.00 45.63  ? 513 OCT A C8  1 
HETATM 4392 CL CL  . CL  P 6 .   ? 84.342  7.625   19.440  1.00 67.44  ? 514 CL  A CL  1 
HETATM 4393 S  S   . SO4 Q 7 .   ? 66.791  30.642  16.516  1.00 77.38  ? 515 SO4 A S   1 
HETATM 4394 O  O1  . SO4 Q 7 .   ? 67.638  29.547  16.038  1.00 71.56  ? 515 SO4 A O1  1 
HETATM 4395 O  O2  . SO4 Q 7 .   ? 66.687  31.664  15.479  1.00 69.11  ? 515 SO4 A O2  1 
HETATM 4396 O  O3  . SO4 Q 7 .   ? 65.460  30.136  16.838  1.00 74.13  ? 515 SO4 A O3  1 
HETATM 4397 O  O4  . SO4 Q 7 .   ? 67.362  31.226  17.727  1.00 77.48  ? 515 SO4 A O4  1 
HETATM 4398 S  S   . SO4 R 7 .   ? 108.122 2.910   34.203  1.00 64.01  ? 516 SO4 A S   1 
HETATM 4399 O  O1  . SO4 R 7 .   ? 108.535 1.964   33.168  1.00 59.57  ? 516 SO4 A O1  1 
HETATM 4400 O  O2  . SO4 R 7 .   ? 106.991 2.360   34.946  1.00 61.39  ? 516 SO4 A O2  1 
HETATM 4401 O  O3  . SO4 R 7 .   ? 109.240 3.132   35.113  1.00 68.39  ? 516 SO4 A O3  1 
HETATM 4402 O  O4  . SO4 R 7 .   ? 107.743 4.181   33.591  1.00 58.83  ? 516 SO4 A O4  1 
HETATM 4403 ZN ZN  . ZN  S 8 .   ? 74.274  29.783  6.902   1.00 65.05  ? 517 ZN  A ZN  1 
HETATM 4404 CL CL  . CL  T 6 .   ? 75.116  32.502  7.064   1.00 56.67  ? 518 CL  A CL  1 
HETATM 4405 CL CL  . CL  U 6 .   ? 73.899  27.432  4.784   1.00 91.69  ? 519 CL  A CL  1 
HETATM 4406 O  O   . HOH V 9 .   ? 96.055  21.024  17.321  1.00 48.52  ? 601 HOH A O   1 
HETATM 4407 O  O   . HOH V 9 .   ? 81.434  4.082   7.742   1.00 34.90  ? 602 HOH A O   1 
HETATM 4408 O  O   . HOH V 9 .   ? 61.736  13.588  6.559   1.00 40.74  ? 603 HOH A O   1 
HETATM 4409 O  O   . HOH V 9 .   ? 74.897  11.526  19.064  1.00 42.93  ? 604 HOH A O   1 
HETATM 4410 O  O   . HOH V 9 .   ? 66.985  18.832  6.246   1.00 39.17  ? 605 HOH A O   1 
HETATM 4411 O  O   . HOH V 9 .   ? 109.399 12.558  -2.553  1.00 41.58  ? 606 HOH A O   1 
HETATM 4412 O  O   . HOH V 9 .   ? 87.928  14.716  12.278  1.00 50.28  ? 607 HOH A O   1 
HETATM 4413 O  O   . HOH V 9 .   ? 68.363  22.959  25.334  1.00 53.04  ? 608 HOH A O   1 
HETATM 4414 O  O   . HOH V 9 .   ? 103.544 -1.140  27.119  1.00 52.67  ? 609 HOH A O   1 
HETATM 4415 O  O   . HOH V 9 .   ? 86.321  22.707  17.677  1.00 44.24  ? 610 HOH A O   1 
HETATM 4416 O  O   . HOH V 9 .   ? 69.870  -2.072  -2.821  1.00 34.52  ? 611 HOH A O   1 
HETATM 4417 O  O   . HOH V 9 .   ? 93.931  9.623   6.040   1.00 71.43  ? 612 HOH A O   1 
HETATM 4418 O  O   . HOH V 9 .   ? 103.486 0.851   28.990  1.00 40.76  ? 613 HOH A O   1 
HETATM 4419 O  O   . HOH V 9 .   ? 68.742  9.543   6.568   1.00 57.30  ? 614 HOH A O   1 
HETATM 4420 O  O   . HOH V 9 .   ? 105.231 17.783  -19.567 1.00 57.29  ? 615 HOH A O   1 
HETATM 4421 O  O   . HOH V 9 .   ? 71.499  28.925  -8.613  1.00 47.09  ? 616 HOH A O   1 
HETATM 4422 O  O   . HOH V 9 .   ? 119.687 12.716  -8.421  1.00 55.79  ? 617 HOH A O   1 
HETATM 4423 O  O   . HOH V 9 .   ? 87.305  4.730   13.038  1.00 36.38  ? 618 HOH A O   1 
HETATM 4424 O  O   . HOH V 9 .   ? 87.141  4.706   8.120   1.00 42.49  ? 619 HOH A O   1 
HETATM 4425 O  O   . HOH V 9 .   ? 85.151  12.401  10.689  1.00 39.45  ? 620 HOH A O   1 
HETATM 4426 O  O   . HOH V 9 .   ? 85.340  12.136  1.339   1.00 38.52  ? 621 HOH A O   1 
HETATM 4427 O  O   . HOH V 9 .   ? 74.150  9.225   18.439  1.00 42.80  ? 622 HOH A O   1 
HETATM 4428 O  O   . HOH V 9 .   ? 72.899  16.100  -11.590 1.00 46.14  ? 623 HOH A O   1 
HETATM 4429 O  O   . HOH V 9 .   ? 85.641  9.310   7.933   1.00 40.26  ? 624 HOH A O   1 
HETATM 4430 O  O   . HOH V 9 .   ? 107.570 -3.306  -1.645  1.00 43.28  ? 625 HOH A O   1 
HETATM 4431 O  O   . HOH V 9 .   ? 85.791  18.962  3.203   1.00 44.93  ? 626 HOH A O   1 
HETATM 4432 O  O   . HOH V 9 .   ? 94.897  10.465  -0.354  1.00 36.47  ? 627 HOH A O   1 
HETATM 4433 O  O   . HOH V 9 .   ? 85.405  6.735   6.982   1.00 35.67  ? 628 HOH A O   1 
HETATM 4434 O  O   . HOH V 9 .   ? 65.564  21.065  14.088  1.00 43.32  ? 629 HOH A O   1 
HETATM 4435 O  O   . HOH V 9 .   ? 85.029  6.991   14.845  1.00 39.48  ? 630 HOH A O   1 
HETATM 4436 O  O   . HOH V 9 .   ? 111.127 13.512  -0.743  1.00 52.85  ? 631 HOH A O   1 
HETATM 4437 O  O   . HOH V 9 .   ? 82.704  14.311  4.416   1.00 34.27  ? 632 HOH A O   1 
HETATM 4438 O  O   . HOH V 9 .   ? 70.607  3.403   -7.593  1.00 46.74  ? 633 HOH A O   1 
HETATM 4439 O  O   . HOH V 9 .   ? 85.543  8.011   4.499   1.00 43.97  ? 634 HOH A O   1 
HETATM 4440 O  O   . HOH V 9 .   ? 119.300 15.345  -7.530  1.00 67.65  ? 635 HOH A O   1 
HETATM 4441 O  O   . HOH V 9 .   ? 69.904  10.319  14.743  1.00 51.76  ? 636 HOH A O   1 
HETATM 4442 O  O   . HOH V 9 .   ? 94.052  6.827   10.777  1.00 47.99  ? 637 HOH A O   1 
HETATM 4443 O  O   . HOH V 9 .   ? 84.105  12.463  3.281   1.00 36.22  ? 638 HOH A O   1 
HETATM 4444 O  O   . HOH V 9 .   ? 109.871 8.844   33.844  1.00 65.99  ? 639 HOH A O   1 
HETATM 4445 O  O   . HOH V 9 .   ? 74.617  2.357   8.125   1.00 42.40  ? 640 HOH A O   1 
HETATM 4446 O  O   . HOH V 9 .   ? 120.300 25.636  17.464  1.00 67.30  ? 641 HOH A O   1 
HETATM 4447 O  O   . HOH V 9 .   ? 117.591 17.512  -12.845 1.00 52.67  ? 642 HOH A O   1 
HETATM 4448 O  O   . HOH V 9 .   ? 87.690  10.650  8.192   1.00 49.52  ? 643 HOH A O   1 
HETATM 4449 O  O   . HOH W 9 .   ? 125.987 -0.419  -0.671  1.00 74.89  ? 201 HOH B O   1 
HETATM 4450 O  O   . HOH W 9 .   ? 129.662 -2.224  -32.903 1.00 65.85  ? 202 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
8    N N   . SER A 3   ? 0.5081 0.5616 0.6135 0.0227  0.0221  0.0240  2   SER A N   
9    C CA  . SER A 3   ? 0.4925 0.5486 0.5797 0.0279  0.0236  0.0228  2   SER A CA  
10   C C   . SER A 3   ? 0.4642 0.5115 0.5389 0.0276  0.0163  0.0207  2   SER A C   
11   O O   . SER A 3   ? 0.4634 0.5038 0.5431 0.0237  0.0119  0.0223  2   SER A O   
12   C CB  . SER A 3   ? 0.4590 0.5238 0.5422 0.0295  0.0327  0.0320  2   SER A CB  
13   O OG  . SER A 3   ? 0.5679 0.6278 0.6439 0.0282  0.0313  0.0387  2   SER A OG  
14   N N   . LEU A 4   ? 0.4222 0.4707 0.4809 0.0320  0.0150  0.0167  3   LEU A N   
15   C CA  . LEU A 4   ? 0.4580 0.5002 0.5055 0.0316  0.0081  0.0147  3   LEU A CA  
16   C C   . LEU A 4   ? 0.4569 0.4995 0.5016 0.0304  0.0096  0.0239  3   LEU A C   
17   O O   . LEU A 4   ? 0.4585 0.4952 0.5020 0.0283  0.0039  0.0240  3   LEU A O   
18   C CB  . LEU A 4   ? 0.4935 0.5376 0.5254 0.0365  0.0062  0.0076  3   LEU A CB  
19   C CG  . LEU A 4   ? 0.4494 0.4882 0.4709 0.0359  -0.0017 0.0038  3   LEU A CG  
20   C CD1 . LEU A 4   ? 0.4600 0.4896 0.4901 0.0312  -0.0085 0.0007  3   LEU A CD1 
21   C CD2 . LEU A 4   ? 0.5040 0.5445 0.5122 0.0406  -0.0039 -0.0049 3   LEU A CD2 
22   N N   . ALA A 5   ? 0.4193 0.4690 0.4635 0.0321  0.0174  0.0322  4   ALA A N   
23   C CA  . ALA A 5   ? 0.4730 0.5222 0.5146 0.0316  0.0191  0.0423  4   ALA A CA  
24   C C   . ALA A 5   ? 0.4454 0.4871 0.5028 0.0262  0.0174  0.0460  4   ALA A C   
25   O O   . ALA A 5   ? 0.5062 0.5424 0.5618 0.0254  0.0128  0.0479  4   ALA A O   
26   C CB  . ALA A 5   ? 0.5108 0.5694 0.5488 0.0344  0.0286  0.0515  4   ALA A CB  
27   N N   . LYS A 6   ? 0.5337 0.5756 0.6071 0.0229  0.0209  0.0465  5   LYS A N   
28   C CA  . LYS A 6   ? 0.4946 0.5293 0.5833 0.0180  0.0187  0.0484  5   LYS A CA  
29   C C   . LYS A 6   ? 0.3928 0.4204 0.4806 0.0167  0.0098  0.0404  5   LYS A C   
30   O O   . LYS A 6   ? 0.5180 0.5394 0.6103 0.0147  0.0066  0.0421  5   LYS A O   
31   C CB  . LYS A 6   ? 0.5255 0.5631 0.6319 0.0146  0.0227  0.0484  5   LYS A CB  
32   C CG  . LYS A 6   ? 0.6152 0.6612 0.7260 0.0149  0.0325  0.0572  5   LYS A CG  
33   C CD  . LYS A 6   ? 0.6326 0.6870 0.7519 0.0150  0.0359  0.0525  5   LYS A CD  
34   C CE  . LYS A 6   ? 0.7744 0.8328 0.9144 0.0102  0.0419  0.0587  5   LYS A CE  
35   N NZ  . LYS A 6   ? 0.8498 0.9211 0.9949 0.0120  0.0489  0.0580  5   LYS A NZ  
36   N N   . ALA A 7   ? 0.4019 0.4301 0.4843 0.0180  0.0060  0.0318  6   ALA A N   
37   C CA  . ALA A 7   ? 0.4409 0.4631 0.5220 0.0166  -0.0018 0.0253  6   ALA A CA  
38   C C   . ALA A 7   ? 0.4348 0.4550 0.5051 0.0178  -0.0052 0.0271  6   ALA A C   
39   O O   . ALA A 7   ? 0.4568 0.4725 0.5297 0.0160  -0.0098 0.0259  6   ALA A O   
40   C CB  . ALA A 7   ? 0.3568 0.3792 0.4340 0.0179  -0.0048 0.0171  6   ALA A CB  
41   N N   . SER A 8   ? 0.4372 0.4620 0.4955 0.0213  -0.0031 0.0299  7   SER A N   
42   C CA  . SER A 8   ? 0.4650 0.4896 0.5135 0.0229  -0.0066 0.0320  7   SER A CA  
43   C C   . SER A 8   ? 0.4293 0.4511 0.4845 0.0222  -0.0054 0.0400  7   SER A C   
44   O O   . SER A 8   ? 0.4765 0.4962 0.5299 0.0224  -0.0100 0.0400  7   SER A O   
45   C CB  . SER A 8   ? 0.4551 0.4865 0.4890 0.0274  -0.0047 0.0332  7   SER A CB  
46   O OG  . SER A 8   ? 0.5042 0.5368 0.5320 0.0285  -0.0069 0.0243  7   SER A OG  
47   N N   . LEU A 9   ? 0.4606 0.4821 0.5246 0.0212  0.0007  0.0466  8   LEU A N   
48   C CA  . LEU A 9   ? 0.4887 0.5056 0.5605 0.0204  0.0019  0.0543  8   LEU A CA  
49   C C   . LEU A 9   ? 0.4240 0.4340 0.5066 0.0174  -0.0030 0.0493  8   LEU A C   
50   O O   . LEU A 9   ? 0.4365 0.4429 0.5198 0.0184  -0.0059 0.0513  8   LEU A O   
51   C CB  . LEU A 9   ? 0.4957 0.5134 0.5766 0.0191  0.0098  0.0626  8   LEU A CB  
52   C CG  . LEU A 9   ? 0.5473 0.5614 0.6307 0.0202  0.0127  0.0740  8   LEU A CG  
53   C CD1 . LEU A 9   ? 0.5199 0.5376 0.5864 0.0255  0.0108  0.0781  8   LEU A CD1 
54   C CD2 . LEU A 9   ? 0.5148 0.5311 0.6067 0.0184  0.0214  0.0830  8   LEU A CD2 
55   N N   . TRP A 10  ? 0.4351 0.4442 0.5259 0.0144  -0.0039 0.0427  9   TRP A N   
56   C CA  . TRP A 10  ? 0.4228 0.4270 0.5214 0.0121  -0.0089 0.0369  9   TRP A CA  
57   C C   . TRP A 10  ? 0.3983 0.4031 0.4873 0.0135  -0.0147 0.0323  9   TRP A C   
58   O O   . TRP A 10  ? 0.3546 0.3566 0.4459 0.0138  -0.0178 0.0318  9   TRP A O   
59   C CB  . TRP A 10  ? 0.4129 0.4176 0.5199 0.0093  -0.0093 0.0308  9   TRP A CB  
60   C CG  . TRP A 10  ? 0.4097 0.4130 0.5317 0.0066  -0.0057 0.0334  9   TRP A CG  
61   C CD1 . TRP A 10  ? 0.4374 0.4454 0.5654 0.0055  -0.0005 0.0357  9   TRP A CD1 
62   C CD2 . TRP A 10  ? 0.3916 0.3890 0.5261 0.0043  -0.0070 0.0334  9   TRP A CD2 
63   N NE1 . TRP A 10  ? 0.4115 0.4170 0.5559 0.0020  0.0014  0.0376  9   TRP A NE1 
64   C CE2 . TRP A 10  ? 0.4323 0.4306 0.5808 0.0012  -0.0028 0.0359  9   TRP A CE2 
65   C CE3 . TRP A 10  ? 0.4291 0.4210 0.5649 0.0049  -0.0112 0.0311  9   TRP A CE3 
66   C CZ2 . TRP A 10  ? 0.4574 0.4500 0.6215 -0.0019 -0.0034 0.0358  9   TRP A CZ2 
67   C CZ3 . TRP A 10  ? 0.4601 0.4460 0.6101 0.0026  -0.0117 0.0305  9   TRP A CZ3 
68   C CH2 . TRP A 10  ? 0.4735 0.4593 0.6376 -0.0010 -0.0081 0.0327  9   TRP A CH2 
69   N N   . THR A 11  ? 0.4086 0.4172 0.4877 0.0144  -0.0162 0.0286  10  THR A N   
70   C CA  . THR A 11  ? 0.4149 0.4242 0.4873 0.0144  -0.0217 0.0240  10  THR A CA  
71   C C   . THR A 11  ? 0.3708 0.3822 0.4372 0.0169  -0.0233 0.0280  10  THR A C   
72   O O   . THR A 11  ? 0.4209 0.4328 0.4871 0.0166  -0.0275 0.0256  10  THR A O   
73   C CB  . THR A 11  ? 0.4185 0.4299 0.4830 0.0145  -0.0233 0.0189  10  THR A CB  
74   O OG1 . THR A 11  ? 0.3901 0.4003 0.4605 0.0133  -0.0213 0.0161  10  THR A OG1 
75   C CG2 . THR A 11  ? 0.4142 0.4251 0.4756 0.0129  -0.0289 0.0141  10  THR A CG2 
76   N N   . ALA A 12  ? 0.3520 0.3655 0.4137 0.0197  -0.0200 0.0346  11  ALA A N   
77   C CA  . ALA A 12  ? 0.3997 0.4156 0.4560 0.0229  -0.0220 0.0390  11  ALA A CA  
78   C C   . ALA A 12  ? 0.4013 0.4127 0.4674 0.0230  -0.0228 0.0415  11  ALA A C   
79   O O   . ALA A 12  ? 0.3709 0.3845 0.4357 0.0248  -0.0267 0.0411  11  ALA A O   
80   C CB  . ALA A 12  ? 0.3087 0.3279 0.3573 0.0264  -0.0180 0.0467  11  ALA A CB  
81   N N   . ALA A 13  ? 0.3876 0.3932 0.4646 0.0214  -0.0194 0.0434  12  ALA A N   
82   C CA  . ALA A 13  ? 0.3832 0.3833 0.4701 0.0218  -0.0205 0.0443  12  ALA A CA  
83   C C   . ALA A 13  ? 0.3960 0.3971 0.4850 0.0207  -0.0252 0.0362  12  ALA A C   
84   O O   . ALA A 13  ? 0.3945 0.3958 0.4854 0.0231  -0.0277 0.0360  12  ALA A O   
85   C CB  . ALA A 13  ? 0.4078 0.4012 0.5070 0.0194  -0.0164 0.0465  12  ALA A CB  
86   N N   . SER A 14  ? 0.3553 0.3576 0.4440 0.0175  -0.0262 0.0298  13  SER A N   
87   C CA  . SER A 14  ? 0.3750 0.3790 0.4646 0.0165  -0.0301 0.0233  13  SER A CA  
88   C C   . SER A 14  ? 0.4070 0.4174 0.4886 0.0176  -0.0333 0.0228  13  SER A C   
89   O O   . SER A 14  ? 0.3957 0.4090 0.4794 0.0185  -0.0358 0.0208  13  SER A O   
90   C CB  . SER A 14  ? 0.3863 0.3897 0.4772 0.0131  -0.0305 0.0179  13  SER A CB  
91   O OG  . SER A 14  ? 0.4041 0.4096 0.4880 0.0123  -0.0299 0.0178  13  SER A OG  
92   N N   . THR A 15  ? 0.3674 0.3811 0.4405 0.0177  -0.0335 0.0242  14  THR A N   
93   C CA  . THR A 15  ? 0.4034 0.4237 0.4704 0.0182  -0.0374 0.0230  14  THR A CA  
94   C C   . THR A 15  ? 0.4269 0.4505 0.4947 0.0223  -0.0385 0.0275  14  THR A C   
95   O O   . THR A 15  ? 0.4444 0.4738 0.5129 0.0227  -0.0418 0.0257  14  THR A O   
96   C CB  . THR A 15  ? 0.4513 0.4740 0.5088 0.0178  -0.0380 0.0222  14  THR A CB  
97   O OG1 . THR A 15  ? 0.4608 0.4796 0.5187 0.0150  -0.0366 0.0183  14  THR A OG1 
98   C CG2 . THR A 15  ? 0.4710 0.5000 0.5241 0.0169  -0.0429 0.0191  14  THR A CG2 
99   N N   . LEU A 16  ? 0.4055 0.4256 0.4741 0.0254  -0.0355 0.0338  15  LEU A N   
100  C CA  . LEU A 16  ? 0.4493 0.4716 0.5189 0.0301  -0.0368 0.0389  15  LEU A CA  
101  C C   . LEU A 16  ? 0.4642 0.4849 0.5436 0.0311  -0.0379 0.0363  15  LEU A C   
102  O O   . LEU A 16  ? 0.4869 0.5133 0.5675 0.0344  -0.0407 0.0368  15  LEU A O   
103  C CB  . LEU A 16  ? 0.4347 0.4522 0.5035 0.0331  -0.0330 0.0475  15  LEU A CB  
104  C CG  . LEU A 16  ? 0.4626 0.4855 0.5190 0.0349  -0.0327 0.0515  15  LEU A CG  
105  C CD1 . LEU A 16  ? 0.4315 0.4500 0.4873 0.0374  -0.0276 0.0612  15  LEU A CD1 
106  C CD2 . LEU A 16  ? 0.4015 0.4335 0.4516 0.0383  -0.0381 0.0516  15  LEU A CD2 
107  N N   . VAL A 17  ? 0.4366 0.4507 0.5232 0.0288  -0.0358 0.0330  16  VAL A N   
108  C CA  . VAL A 17  ? 0.4150 0.4282 0.5097 0.0301  -0.0369 0.0289  16  VAL A CA  
109  C C   . VAL A 17  ? 0.4273 0.4495 0.5198 0.0286  -0.0398 0.0234  16  VAL A C   
110  O O   . VAL A 17  ? 0.4466 0.4739 0.5428 0.0315  -0.0413 0.0219  16  VAL A O   
111  C CB  . VAL A 17  ? 0.4675 0.4722 0.5697 0.0279  -0.0348 0.0256  16  VAL A CB  
112  C CG1 . VAL A 17  ? 0.4482 0.4551 0.5546 0.0278  -0.0366 0.0181  16  VAL A CG1 
113  C CG2 . VAL A 17  ? 0.4378 0.4334 0.5473 0.0303  -0.0324 0.0309  16  VAL A CG2 
114  N N   . LYS A 18  ? 0.4065 0.4310 0.4935 0.0241  -0.0404 0.0208  17  LYS A N   
115  C CA  . LYS A 18  ? 0.4562 0.4888 0.5418 0.0218  -0.0428 0.0169  17  LYS A CA  
116  C C   . LYS A 18  ? 0.4569 0.4988 0.5408 0.0238  -0.0456 0.0190  17  LYS A C   
117  O O   . LYS A 18  ? 0.5151 0.5651 0.6023 0.0239  -0.0471 0.0171  17  LYS A O   
118  C CB  . LYS A 18  ? 0.4267 0.4580 0.5074 0.0168  -0.0431 0.0144  17  LYS A CB  
119  C CG  . LYS A 18  ? 0.4869 0.5257 0.5641 0.0139  -0.0461 0.0131  17  LYS A CG  
120  C CD  . LYS A 18  ? 0.6256 0.6614 0.7002 0.0092  -0.0464 0.0102  17  LYS A CD  
121  C CE  . LYS A 18  ? 0.6574 0.6990 0.7299 0.0057  -0.0497 0.0090  17  LYS A CE  
122  N NZ  . LYS A 18  ? 0.7395 0.7781 0.8118 0.0011  -0.0500 0.0069  17  LYS A NZ  
123  N N   . ILE A 19  ? 0.4377 0.4795 0.5164 0.0256  -0.0463 0.0232  18  ILE A N   
124  C CA  . ILE A 19  ? 0.4975 0.5489 0.5744 0.0280  -0.0499 0.0250  18  ILE A CA  
125  C C   . ILE A 19  ? 0.4441 0.4983 0.5278 0.0339  -0.0502 0.0276  18  ILE A C   
126  O O   . ILE A 19  ? 0.5263 0.5908 0.6140 0.0351  -0.0527 0.0262  18  ILE A O   
127  C CB  . ILE A 19  ? 0.5399 0.5912 0.6077 0.0293  -0.0509 0.0285  18  ILE A CB  
128  C CG1 . ILE A 19  ? 0.4843 0.5371 0.5460 0.0242  -0.0527 0.0240  18  ILE A CG1 
129  C CG2 . ILE A 19  ? 0.5703 0.6305 0.6369 0.0342  -0.0545 0.0322  18  ILE A CG2 
130  C CD1 . ILE A 19  ? 0.4943 0.5455 0.5460 0.0255  -0.0524 0.0259  18  ILE A CD1 
131  N N   . GLY A 20  ? 0.4269 0.4720 0.5133 0.0375  -0.0474 0.0312  19  GLY A N   
132  C CA  . GLY A 20  ? 0.5200 0.5653 0.6137 0.0436  -0.0477 0.0333  19  GLY A CA  
133  C C   . GLY A 20  ? 0.4647 0.5144 0.5658 0.0437  -0.0476 0.0271  19  GLY A C   
134  O O   . GLY A 20  ? 0.4410 0.4985 0.5473 0.0482  -0.0492 0.0269  19  GLY A O   
135  N N   . ALA A 21  ? 0.4748 0.5205 0.5763 0.0391  -0.0456 0.0221  20  ALA A N   
136  C CA  . ALA A 21  ? 0.4808 0.5319 0.5872 0.0392  -0.0452 0.0163  20  ALA A CA  
137  C C   . ALA A 21  ? 0.4932 0.5589 0.5991 0.0371  -0.0472 0.0151  20  ALA A C   
138  O O   . ALA A 21  ? 0.4842 0.5591 0.5957 0.0401  -0.0472 0.0130  20  ALA A O   
139  C CB  . ALA A 21  ? 0.3995 0.4440 0.5050 0.0349  -0.0432 0.0118  20  ALA A CB  
140  N N   . GLY A 22  ? 0.4893 0.5573 0.5893 0.0319  -0.0488 0.0163  21  GLY A N   
141  C CA  . GLY A 22  ? 0.4251 0.5061 0.5262 0.0288  -0.0511 0.0152  21  GLY A CA  
142  C C   . GLY A 22  ? 0.4875 0.5794 0.5929 0.0336  -0.0539 0.0176  21  GLY A C   
143  O O   . GLY A 22  ? 0.5265 0.6313 0.6382 0.0337  -0.0546 0.0160  21  GLY A O   
144  N N   . LEU A 23  ? 0.4799 0.5677 0.5822 0.0379  -0.0555 0.0218  22  LEU A N   
145  C CA  . LEU A 23  ? 0.5058 0.6037 0.6119 0.0438  -0.0588 0.0247  22  LEU A CA  
146  C C   . LEU A 23  ? 0.4877 0.5888 0.6032 0.0501  -0.0571 0.0237  22  LEU A C   
147  O O   . LEU A 23  ? 0.5087 0.6235 0.6309 0.0536  -0.0593 0.0236  22  LEU A O   
148  C CB  . LEU A 23  ? 0.4795 0.5711 0.5790 0.0478  -0.0603 0.0305  22  LEU A CB  
149  C CG  . LEU A 23  ? 0.6017 0.6930 0.6912 0.0431  -0.0626 0.0308  22  LEU A CG  
150  C CD1 . LEU A 23  ? 0.4463 0.5323 0.5280 0.0480  -0.0631 0.0374  22  LEU A CD1 
151  C CD2 . LEU A 23  ? 0.5503 0.6565 0.6414 0.0399  -0.0675 0.0277  22  LEU A CD2 
152  N N   . LEU A 24  ? 0.4716 0.5607 0.5885 0.0520  -0.0535 0.0224  23  LEU A N   
153  C CA  . LEU A 24  ? 0.4819 0.5727 0.6074 0.0586  -0.0520 0.0199  23  LEU A CA  
154  C C   . LEU A 24  ? 0.4985 0.6028 0.6285 0.0564  -0.0506 0.0144  23  LEU A C   
155  O O   . LEU A 24  ? 0.5281 0.6447 0.6657 0.0615  -0.0510 0.0133  23  LEU A O   
156  C CB  . LEU A 24  ? 0.4805 0.5545 0.6067 0.0603  -0.0490 0.0185  23  LEU A CB  
157  C CG  . LEU A 24  ? 0.5707 0.6432 0.7056 0.0676  -0.0477 0.0145  23  LEU A CG  
158  C CD1 . LEU A 24  ? 0.4888 0.5689 0.6299 0.0760  -0.0502 0.0180  23  LEU A CD1 
159  C CD2 . LEU A 24  ? 0.4747 0.5287 0.6110 0.0687  -0.0459 0.0137  23  LEU A CD2 
160  N N   . VAL A 25  ? 0.4213 0.5241 0.5468 0.0490  -0.0488 0.0116  24  VAL A N   
161  C CA  . VAL A 25  ? 0.4541 0.5694 0.5829 0.0466  -0.0467 0.0078  24  VAL A CA  
162  C C   . VAL A 25  ? 0.5322 0.6648 0.6654 0.0441  -0.0490 0.0097  24  VAL A C   
163  O O   . VAL A 25  ? 0.5244 0.6719 0.6650 0.0461  -0.0476 0.0080  24  VAL A O   
164  C CB  . VAL A 25  ? 0.4616 0.5701 0.5839 0.0395  -0.0446 0.0057  24  VAL A CB  
165  C CG1 . VAL A 25  ? 0.5597 0.6823 0.6840 0.0351  -0.0428 0.0045  24  VAL A CG1 
166  C CG2 . VAL A 25  ? 0.4453 0.5420 0.5666 0.0428  -0.0423 0.0018  24  VAL A CG2 
167  N N   . GLY A 26  ? 0.4907 0.6224 0.6200 0.0400  -0.0528 0.0128  25  GLY A N   
168  C CA  . GLY A 26  ? 0.4915 0.6394 0.6260 0.0371  -0.0560 0.0138  25  GLY A CA  
169  C C   . GLY A 26  ? 0.5376 0.6983 0.6809 0.0450  -0.0580 0.0149  25  GLY A C   
170  O O   . GLY A 26  ? 0.4793 0.6579 0.6316 0.0441  -0.0585 0.0142  25  GLY A O   
171  N N   . LYS A 27  ? 0.5014 0.6536 0.6431 0.0529  -0.0591 0.0172  26  LYS A N   
172  C CA  . LYS A 27  ? 0.5018 0.6652 0.6522 0.0617  -0.0613 0.0186  26  LYS A CA  
173  C C   . LYS A 27  ? 0.5077 0.6776 0.6668 0.0671  -0.0571 0.0147  26  LYS A C   
174  O O   . LYS A 27  ? 0.5372 0.7240 0.7065 0.0720  -0.0580 0.0143  26  LYS A O   
175  C CB  . LYS A 27  ? 0.5909 0.7424 0.7369 0.0687  -0.0638 0.0235  26  LYS A CB  
176  C CG  . LYS A 27  ? 0.7988 0.9550 0.9393 0.0668  -0.0696 0.0275  26  LYS A CG  
177  C CD  . LYS A 27  ? 0.9285 1.0773 1.0650 0.0751  -0.0724 0.0339  26  LYS A CD  
178  C CE  . LYS A 27  ? 0.8563 0.9946 0.9793 0.0711  -0.0738 0.0374  26  LYS A CE  
179  N NZ  . LYS A 27  ? 0.8300 0.9505 0.9474 0.0759  -0.0713 0.0432  26  LYS A NZ  
180  N N   . LEU A 28  ? 0.5304 0.6886 0.6860 0.0666  -0.0525 0.0113  27  LEU A N   
181  C CA  . LEU A 28  ? 0.5062 0.6720 0.6685 0.0714  -0.0483 0.0062  27  LEU A CA  
182  C C   . LEU A 28  ? 0.4880 0.6743 0.6555 0.0662  -0.0463 0.0049  27  LEU A C   
183  O O   . LEU A 28  ? 0.5291 0.7316 0.7059 0.0716  -0.0443 0.0027  27  LEU A O   
184  C CB  . LEU A 28  ? 0.5142 0.6641 0.6706 0.0711  -0.0447 0.0020  27  LEU A CB  
185  C CG  . LEU A 28  ? 0.5904 0.7210 0.7458 0.0773  -0.0454 0.0020  27  LEU A CG  
186  C CD1 . LEU A 28  ? 0.4879 0.6032 0.6367 0.0735  -0.0429 -0.0019 27  LEU A CD1 
187  C CD2 . LEU A 28  ? 0.6043 0.7387 0.7691 0.0886  -0.0450 -0.0010 27  LEU A CD2 
188  N N   . LEU A 29  ? 0.4974 0.6835 0.6597 0.0558  -0.0466 0.0065  28  LEU A N   
189  C CA  . LEU A 29  ? 0.4788 0.6831 0.6467 0.0495  -0.0445 0.0065  28  LEU A CA  
190  C C   . LEU A 29  ? 0.5629 0.7864 0.7420 0.0502  -0.0483 0.0086  28  LEU A C   
191  O O   . LEU A 29  ? 0.5706 0.8140 0.7599 0.0502  -0.0456 0.0080  28  LEU A O   
192  C CB  . LEU A 29  ? 0.4995 0.6961 0.6597 0.0383  -0.0446 0.0081  28  LEU A CB  
193  C CG  . LEU A 29  ? 0.5047 0.7161 0.6698 0.0307  -0.0413 0.0090  28  LEU A CG  
194  C CD1 . LEU A 29  ? 0.4371 0.6453 0.5967 0.0311  -0.0353 0.0069  28  LEU A CD1 
195  C CD2 . LEU A 29  ? 0.5134 0.7207 0.6760 0.0200  -0.0447 0.0117  28  LEU A CD2 
196  N N   . ALA A 30  ? 0.5056 0.7246 0.6830 0.0511  -0.0544 0.0112  29  ALA A N   
197  C CA  . ALA A 30  ? 0.5257 0.7634 0.7134 0.0521  -0.0592 0.0128  29  ALA A CA  
198  C C   . ALA A 30  ? 0.4669 0.7179 0.6656 0.0633  -0.0581 0.0118  29  ALA A C   
199  O O   . ALA A 30  ? 0.5062 0.7797 0.7177 0.0632  -0.0577 0.0113  29  ALA A O   
200  C CB  . ALA A 30  ? 0.4997 0.7293 0.6809 0.0520  -0.0662 0.0156  29  ALA A CB  
201  N N   . VAL A 31  ? 0.4283 0.6657 0.6233 0.0729  -0.0575 0.0114  30  VAL A N   
202  C CA  . VAL A 31  ? 0.5172 0.7646 0.7225 0.0849  -0.0568 0.0100  30  VAL A CA  
203  C C   . VAL A 31  ? 0.5382 0.7991 0.7506 0.0860  -0.0499 0.0053  30  VAL A C   
204  O O   . VAL A 31  ? 0.5600 0.8402 0.7850 0.0930  -0.0490 0.0039  30  VAL A O   
205  C CB  . VAL A 31  ? 0.4773 0.7035 0.6770 0.0941  -0.0576 0.0108  30  VAL A CB  
206  C CG1 . VAL A 31  ? 0.3570 0.5903 0.5675 0.1071  -0.0562 0.0082  30  VAL A CG1 
207  C CG2 . VAL A 31  ? 0.4152 0.6328 0.6089 0.0944  -0.0641 0.0169  30  VAL A CG2 
208  N N   . SER A 32  ? 0.5007 0.7535 0.7052 0.0796  -0.0449 0.0030  31  SER A N   
209  C CA  . SER A 32  ? 0.4159 0.6808 0.6245 0.0817  -0.0380 -0.0014 31  SER A CA  
210  C C   . SER A 32  ? 0.4835 0.7733 0.7013 0.0744  -0.0356 0.0005  31  SER A C   
211  O O   . SER A 32  ? 0.4852 0.7946 0.7125 0.0792  -0.0308 -0.0019 31  SER A O   
212  C CB  . SER A 32  ? 0.4830 0.7306 0.6790 0.0784  -0.0339 -0.0044 31  SER A CB  
213  O OG  . SER A 32  ? 0.5958 0.8303 0.7895 0.0885  -0.0330 -0.0094 31  SER A OG  
214  N N   . PHE A 33  ? 0.4766 0.7664 0.6926 0.0628  -0.0385 0.0046  32  PHE A N   
215  C CA  . PHE A 33  ? 0.4384 0.7484 0.6628 0.0538  -0.0356 0.0068  32  PHE A CA  
216  C C   . PHE A 33  ? 0.5102 0.8328 0.7448 0.0474  -0.0419 0.0100  32  PHE A C   
217  O O   . PHE A 33  ? 0.5593 0.8996 0.8038 0.0392  -0.0399 0.0121  32  PHE A O   
218  C CB  . PHE A 33  ? 0.3513 0.6500 0.5649 0.0438  -0.0318 0.0080  32  PHE A CB  
219  C CG  . PHE A 33  ? 0.4759 0.7620 0.6784 0.0493  -0.0266 0.0042  32  PHE A CG  
220  C CD1 . PHE A 33  ? 0.4745 0.7751 0.6810 0.0561  -0.0200 0.0010  32  PHE A CD1 
221  C CD2 . PHE A 33  ? 0.5312 0.7920 0.7199 0.0482  -0.0286 0.0033  32  PHE A CD2 
222  C CE1 . PHE A 33  ? 0.4771 0.7666 0.6731 0.0614  -0.0161 -0.0038 32  PHE A CE1 
223  C CE2 . PHE A 33  ? 0.4422 0.6923 0.6219 0.0530  -0.0248 -0.0010 32  PHE A CE2 
224  C CZ  . PHE A 33  ? 0.4678 0.7319 0.6508 0.0596  -0.0189 -0.0049 32  PHE A CZ  
225  N N   . GLY A 34  ? 0.5228 0.8373 0.7554 0.0509  -0.0495 0.0106  33  GLY A N   
226  C CA  . GLY A 34  ? 0.4783 0.8068 0.7207 0.0469  -0.0566 0.0124  33  GLY A CA  
227  C C   . GLY A 34  ? 0.5036 0.8314 0.7454 0.0324  -0.0586 0.0139  33  GLY A C   
228  O O   . GLY A 34  ? 0.5576 0.8700 0.7891 0.0255  -0.0553 0.0144  33  GLY A O   
229  N N   . PRO A 35  ? 0.5581 0.9027 0.8121 0.0276  -0.0647 0.0145  34  PRO A N   
230  C CA  . PRO A 35  ? 0.5509 0.8936 0.8059 0.0136  -0.0677 0.0151  34  PRO A CA  
231  C C   . PRO A 35  ? 0.5300 0.8790 0.7907 0.0041  -0.0600 0.0172  34  PRO A C   
232  O O   . PRO A 35  ? 0.5365 0.8738 0.7921 -0.0066 -0.0604 0.0182  34  PRO A O   
233  C CB  . PRO A 35  ? 0.5437 0.9069 0.8134 0.0121  -0.0761 0.0142  34  PRO A CB  
234  C CG  . PRO A 35  ? 0.5847 0.9534 0.8552 0.0266  -0.0791 0.0138  34  PRO A CG  
235  C CD  . PRO A 35  ? 0.5100 0.8751 0.7776 0.0350  -0.0699 0.0141  34  PRO A CD  
236  N N   . ALA A 36  ? 0.5225 0.8901 0.7935 0.0081  -0.0528 0.0182  35  ALA A N   
237  C CA  . ALA A 36  ? 0.5209 0.8953 0.7958 -0.0001 -0.0445 0.0214  35  ALA A CA  
238  C C   . ALA A 36  ? 0.5220 0.8723 0.7779 -0.0007 -0.0396 0.0219  35  ALA A C   
239  O O   . ALA A 36  ? 0.5329 0.8769 0.7861 -0.0111 -0.0370 0.0252  35  ALA A O   
240  C CB  . ALA A 36  ? 0.4504 0.8511 0.7389 0.0061  -0.0372 0.0220  35  ALA A CB  
241  N N   . GLY A 37  ? 0.4670 0.8034 0.7105 0.0103  -0.0388 0.0189  36  GLY A N   
242  C CA  . GLY A 37  ? 0.4927 0.8065 0.7189 0.0100  -0.0354 0.0186  36  GLY A CA  
243  C C   . GLY A 37  ? 0.4728 0.7647 0.6886 0.0026  -0.0411 0.0191  36  GLY A C   
244  O O   . GLY A 37  ? 0.5127 0.7912 0.7193 -0.0033 -0.0384 0.0207  36  GLY A O   
245  N N   . LEU A 38  ? 0.4862 0.7749 0.7030 0.0034  -0.0491 0.0176  37  LEU A N   
246  C CA  . LEU A 38  ? 0.4740 0.7434 0.6808 -0.0029 -0.0546 0.0172  37  LEU A CA  
247  C C   . LEU A 38  ? 0.5167 0.7895 0.7301 -0.0162 -0.0553 0.0193  37  LEU A C   
248  O O   . LEU A 38  ? 0.4949 0.7503 0.6990 -0.0223 -0.0552 0.0200  37  LEU A O   
249  C CB  . LEU A 38  ? 0.4895 0.7573 0.6952 0.0018  -0.0628 0.0152  37  LEU A CB  
250  C CG  . LEU A 38  ? 0.5199 0.7759 0.7157 0.0136  -0.0631 0.0143  37  LEU A CG  
251  C CD1 . LEU A 38  ? 0.4914 0.7500 0.6874 0.0182  -0.0712 0.0139  37  LEU A CD1 
252  C CD2 . LEU A 38  ? 0.4195 0.6510 0.5995 0.0128  -0.0607 0.0140  37  LEU A CD2 
253  N N   . GLY A 39  ? 0.4562 0.7512 0.6869 -0.0208 -0.0562 0.0205  38  GLY A N   
254  C CA  . GLY A 39  ? 0.4012 0.6994 0.6407 -0.0342 -0.0571 0.0228  38  GLY A CA  
255  C C   . GLY A 39  ? 0.4634 0.7569 0.6997 -0.0396 -0.0488 0.0276  38  GLY A C   
256  O O   . GLY A 39  ? 0.5657 0.8483 0.8008 -0.0495 -0.0495 0.0298  38  GLY A O   
257  N N   . LEU A 40  ? 0.4989 0.8006 0.7334 -0.0327 -0.0408 0.0293  39  LEU A N   
258  C CA  . LEU A 40  ? 0.4968 0.7949 0.7257 -0.0361 -0.0328 0.0340  39  LEU A CA  
259  C C   . LEU A 40  ? 0.4490 0.7206 0.6583 -0.0338 -0.0329 0.0327  39  LEU A C   
260  O O   . LEU A 40  ? 0.5072 0.7712 0.7108 -0.0391 -0.0288 0.0369  39  LEU A O   
261  C CB  . LEU A 40  ? 0.4164 0.7338 0.6491 -0.0286 -0.0244 0.0350  39  LEU A CB  
262  C CG  . LEU A 40  ? 0.4315 0.7760 0.6823 -0.0346 -0.0190 0.0402  39  LEU A CG  
263  C CD1 . LEU A 40  ? 0.4251 0.7854 0.6747 -0.0257 -0.0097 0.0405  39  LEU A CD1 
264  C CD2 . LEU A 40  ? 0.4508 0.7911 0.7048 -0.0485 -0.0171 0.0472  39  LEU A CD2 
265  N N   . ALA A 41  ? 0.4521 0.7102 0.6516 -0.0261 -0.0374 0.0276  40  ALA A N   
266  C CA  . ALA A 41  ? 0.4294 0.6639 0.6122 -0.0238 -0.0376 0.0262  40  ALA A CA  
267  C C   . ALA A 41  ? 0.4512 0.6683 0.6291 -0.0305 -0.0439 0.0254  40  ALA A C   
268  O O   . ALA A 41  ? 0.5827 0.7808 0.7479 -0.0292 -0.0441 0.0244  40  ALA A O   
269  C CB  . ALA A 41  ? 0.3866 0.6151 0.5618 -0.0119 -0.0383 0.0216  40  ALA A CB  
270  N N   . ALA A 42  ? 0.4495 0.6731 0.6378 -0.0375 -0.0491 0.0253  41  ALA A N   
271  C CA  . ALA A 42  ? 0.4588 0.6663 0.6421 -0.0423 -0.0559 0.0226  41  ALA A CA  
272  C C   . ALA A 42  ? 0.4928 0.6837 0.6694 -0.0490 -0.0539 0.0253  41  ALA A C   
273  O O   . ALA A 42  ? 0.5201 0.6922 0.6842 -0.0468 -0.0556 0.0230  41  ALA A O   
274  C CB  . ALA A 42  ? 0.4346 0.6543 0.6317 -0.0487 -0.0622 0.0210  41  ALA A CB  
275  N N   . ASN A 43  ? 0.4462 0.6444 0.6317 -0.0570 -0.0501 0.0307  42  ASN A N   
276  C CA  . ASN A 43  ? 0.4222 0.6047 0.6022 -0.0632 -0.0485 0.0344  42  ASN A CA  
277  C C   . ASN A 43  ? 0.5081 0.6800 0.6732 -0.0562 -0.0437 0.0355  42  ASN A C   
278  O O   . ASN A 43  ? 0.4366 0.5896 0.5918 -0.0566 -0.0453 0.0348  42  ASN A O   
279  C CB  . ASN A 43  ? 0.4431 0.6371 0.6364 -0.0729 -0.0446 0.0416  42  ASN A CB  
280  C CG  . ASN A 43  ? 0.5096 0.7105 0.7189 -0.0821 -0.0505 0.0402  42  ASN A CG  
281  O OD1 . ASN A 43  ? 0.5784 0.7695 0.7860 -0.0828 -0.0582 0.0338  42  ASN A OD1 
282  N ND2 . ASN A 43  ? 0.4933 0.7122 0.7184 -0.0892 -0.0469 0.0459  42  ASN A ND2 
283  N N   . PHE A 44  ? 0.4531 0.6375 0.6171 -0.0495 -0.0380 0.0365  43  PHE A N   
284  C CA  . PHE A 44  ? 0.4602 0.6362 0.6108 -0.0426 -0.0341 0.0362  43  PHE A CA  
285  C C   . PHE A 44  ? 0.4333 0.5919 0.5733 -0.0369 -0.0385 0.0304  43  PHE A C   
286  O O   . PHE A 44  ? 0.4835 0.6279 0.6131 -0.0353 -0.0378 0.0304  43  PHE A O   
287  C CB  . PHE A 44  ? 0.4017 0.5948 0.5537 -0.0353 -0.0284 0.0360  43  PHE A CB  
288  C CG  . PHE A 44  ? 0.4405 0.6264 0.5794 -0.0282 -0.0248 0.0346  43  PHE A CG  
289  C CD1 . PHE A 44  ? 0.4786 0.6656 0.6122 -0.0305 -0.0199 0.0398  43  PHE A CD1 
290  C CD2 . PHE A 44  ? 0.3822 0.5606 0.5144 -0.0194 -0.0266 0.0282  43  PHE A CD2 
291  C CE1 . PHE A 44  ? 0.4529 0.6346 0.5743 -0.0237 -0.0175 0.0376  43  PHE A CE1 
292  C CE2 . PHE A 44  ? 0.3893 0.5614 0.5110 -0.0135 -0.0241 0.0260  43  PHE A CE2 
293  C CZ  . PHE A 44  ? 0.4427 0.6169 0.5587 -0.0155 -0.0199 0.0301  43  PHE A CZ  
294  N N   . ARG A 45  ? 0.4481 0.6086 0.5909 -0.0336 -0.0428 0.0260  44  ARG A N   
295  C CA  . ARG A 45  ? 0.5016 0.6469 0.6347 -0.0283 -0.0462 0.0216  44  ARG A CA  
296  C C   . ARG A 45  ? 0.5100 0.6392 0.6385 -0.0338 -0.0502 0.0210  44  ARG A C   
297  O O   . ARG A 45  ? 0.5741 0.6885 0.6929 -0.0309 -0.0505 0.0193  44  ARG A O   
298  C CB  . ARG A 45  ? 0.4547 0.6070 0.5914 -0.0229 -0.0497 0.0184  44  ARG A CB  
299  C CG  . ARG A 45  ? 0.5571 0.7209 0.6965 -0.0148 -0.0460 0.0178  44  ARG A CG  
300  C CD  . ARG A 45  ? 0.4973 0.6714 0.6433 -0.0103 -0.0497 0.0161  44  ARG A CD  
301  N NE  . ARG A 45  ? 0.5591 0.7205 0.6971 -0.0046 -0.0529 0.0139  44  ARG A NE  
302  C CZ  . ARG A 45  ? 0.5844 0.7508 0.7248 0.0005  -0.0567 0.0131  44  ARG A CZ  
303  N NH1 . ARG A 45  ? 0.4707 0.6550 0.6221 0.0010  -0.0585 0.0135  44  ARG A NH1 
304  N NH2 . ARG A 45  ? 0.6458 0.7996 0.7778 0.0054  -0.0586 0.0125  44  ARG A NH2 
305  N N   . GLN A 46  ? 0.4715 0.6033 0.6079 -0.0418 -0.0534 0.0218  45  GLN A N   
306  C CA  . GLN A 46  ? 0.4516 0.5673 0.5841 -0.0469 -0.0572 0.0205  45  GLN A CA  
307  C C   . GLN A 46  ? 0.4780 0.5827 0.6052 -0.0490 -0.0537 0.0245  45  GLN A C   
308  O O   . GLN A 46  ? 0.5274 0.6161 0.6471 -0.0486 -0.0557 0.0226  45  GLN A O   
309  C CB  . GLN A 46  ? 0.4199 0.5408 0.5636 -0.0553 -0.0619 0.0198  45  GLN A CB  
310  C CG  . GLN A 46  ? 0.5933 0.6983 0.7339 -0.0594 -0.0676 0.0157  45  GLN A CG  
311  C CD  . GLN A 46  ? 0.7673 0.8606 0.8952 -0.0522 -0.0700 0.0103  45  GLN A CD  
312  O OE1 . GLN A 46  ? 0.7781 0.8559 0.9000 -0.0532 -0.0717 0.0080  45  GLN A OE1 
313  N NE2 . GLN A 46  ? 0.8167 0.9176 0.9413 -0.0449 -0.0700 0.0086  45  GLN A NE2 
314  N N   . LEU A 47  ? 0.4618 0.5758 0.5923 -0.0506 -0.0485 0.0301  46  LEU A N   
315  C CA  . LEU A 47  ? 0.4433 0.5483 0.5671 -0.0512 -0.0451 0.0346  46  LEU A CA  
316  C C   . LEU A 47  ? 0.4775 0.5736 0.5894 -0.0429 -0.0443 0.0313  46  LEU A C   
317  O O   . LEU A 47  ? 0.4842 0.5666 0.5892 -0.0428 -0.0449 0.0319  46  LEU A O   
318  C CB  . LEU A 47  ? 0.4777 0.5970 0.6059 -0.0535 -0.0391 0.0415  46  LEU A CB  
319  C CG  . LEU A 47  ? 0.5095 0.6237 0.6281 -0.0512 -0.0350 0.0461  46  LEU A CG  
320  C CD1 . LEU A 47  ? 0.4886 0.5861 0.6053 -0.0568 -0.0374 0.0499  46  LEU A CD1 
321  C CD2 . LEU A 47  ? 0.4166 0.5485 0.5380 -0.0517 -0.0284 0.0524  46  LEU A CD2 
322  N N   . ILE A 48  ? 0.4546 0.5582 0.5650 -0.0359 -0.0431 0.0277  47  ILE A N   
323  C CA  . ILE A 48  ? 0.4635 0.5586 0.5647 -0.0287 -0.0426 0.0242  47  ILE A CA  
324  C C   . ILE A 48  ? 0.5124 0.5923 0.6092 -0.0284 -0.0467 0.0207  47  ILE A C   
325  O O   . ILE A 48  ? 0.4907 0.5597 0.5807 -0.0260 -0.0466 0.0197  47  ILE A O   
326  C CB  . ILE A 48  ? 0.4165 0.5213 0.5190 -0.0216 -0.0409 0.0210  47  ILE A CB  
327  C CG1 . ILE A 48  ? 0.4776 0.5984 0.5837 -0.0206 -0.0361 0.0236  47  ILE A CG1 
328  C CG2 . ILE A 48  ? 0.4954 0.5901 0.5904 -0.0151 -0.0409 0.0171  47  ILE A CG2 
329  C CD1 . ILE A 48  ? 0.5253 0.6447 0.6255 -0.0219 -0.0328 0.0273  47  ILE A CD1 
330  N N   . THR A 49  ? 0.5245 0.6046 0.6251 -0.0307 -0.0505 0.0186  48  THR A N   
331  C CA  . THR A 49  ? 0.5089 0.5759 0.6047 -0.0304 -0.0541 0.0150  48  THR A CA  
332  C C   . THR A 49  ? 0.5141 0.5691 0.6079 -0.0348 -0.0550 0.0165  48  THR A C   
333  O O   . THR A 49  ? 0.4778 0.5213 0.5653 -0.0321 -0.0554 0.0147  48  THR A O   
334  C CB  . THR A 49  ? 0.5844 0.6558 0.6840 -0.0320 -0.0584 0.0121  48  THR A CB  
335  O OG1 . THR A 49  ? 0.5974 0.6781 0.6978 -0.0263 -0.0579 0.0111  48  THR A OG1 
336  C CG2 . THR A 49  ? 0.5334 0.5922 0.6272 -0.0318 -0.0620 0.0080  48  THR A CG2 
337  N N   . VAL A 50  ? 0.4467 0.5043 0.5468 -0.0417 -0.0553 0.0202  49  VAL A N   
338  C CA  . VAL A 50  ? 0.5214 0.5663 0.6206 -0.0460 -0.0565 0.0224  49  VAL A CA  
339  C C   . VAL A 50  ? 0.5156 0.5549 0.6078 -0.0422 -0.0534 0.0254  49  VAL A C   
340  O O   . VAL A 50  ? 0.5443 0.5704 0.6323 -0.0413 -0.0550 0.0246  49  VAL A O   
341  C CB  . VAL A 50  ? 0.4881 0.5375 0.5970 -0.0546 -0.0567 0.0273  49  VAL A CB  
342  C CG1 . VAL A 50  ? 0.5075 0.5434 0.6156 -0.0584 -0.0569 0.0317  49  VAL A CG1 
343  C CG2 . VAL A 50  ? 0.4775 0.5295 0.5937 -0.0589 -0.0616 0.0227  49  VAL A CG2 
344  N N   . LEU A 51  ? 0.4574 0.5072 0.5483 -0.0394 -0.0493 0.0283  50  LEU A N   
345  C CA  . LEU A 51  ? 0.3918 0.4383 0.4757 -0.0356 -0.0470 0.0305  50  LEU A CA  
346  C C   . LEU A 51  ? 0.5078 0.5455 0.5857 -0.0296 -0.0484 0.0251  50  LEU A C   
347  O O   . LEU A 51  ? 0.4103 0.4420 0.4833 -0.0271 -0.0483 0.0261  50  LEU A O   
348  C CB  . LEU A 51  ? 0.4597 0.5207 0.5429 -0.0330 -0.0426 0.0328  50  LEU A CB  
349  C CG  . LEU A 51  ? 0.4846 0.5548 0.5718 -0.0383 -0.0395 0.0404  50  LEU A CG  
350  C CD1 . LEU A 51  ? 0.5773 0.6642 0.6640 -0.0345 -0.0348 0.0409  50  LEU A CD1 
351  C CD2 . LEU A 51  ? 0.3931 0.4541 0.4756 -0.0403 -0.0394 0.0466  50  LEU A CD2 
352  N N   . GLY A 52  ? 0.5093 0.5470 0.5881 -0.0271 -0.0498 0.0199  51  GLY A N   
353  C CA  . GLY A 52  ? 0.4741 0.5040 0.5485 -0.0222 -0.0506 0.0157  51  GLY A CA  
354  C C   . GLY A 52  ? 0.5178 0.5349 0.5899 -0.0231 -0.0528 0.0152  51  GLY A C   
355  O O   . GLY A 52  ? 0.4696 0.4811 0.5386 -0.0191 -0.0527 0.0132  51  GLY A O   
356  N N   . VAL A 53  ? 0.4801 0.4924 0.5549 -0.0281 -0.0549 0.0168  52  VAL A N   
357  C CA  . VAL A 53  ? 0.5034 0.5028 0.5768 -0.0287 -0.0572 0.0165  52  VAL A CA  
358  C C   . VAL A 53  ? 0.4875 0.4836 0.5617 -0.0320 -0.0569 0.0232  52  VAL A C   
359  O O   . VAL A 53  ? 0.5071 0.4947 0.5786 -0.0298 -0.0577 0.0244  52  VAL A O   
360  C CB  . VAL A 53  ? 0.5128 0.5060 0.5882 -0.0312 -0.0605 0.0121  52  VAL A CB  
361  C CG1 . VAL A 53  ? 0.5176 0.4968 0.5918 -0.0305 -0.0628 0.0105  52  VAL A CG1 
362  C CG2 . VAL A 53  ? 0.5736 0.5716 0.6468 -0.0276 -0.0605 0.0069  52  VAL A CG2 
363  N N   . LEU A 54  ? 0.4508 0.4547 0.5290 -0.0369 -0.0555 0.0281  53  LEU A N   
364  C CA  . LEU A 54  ? 0.5070 0.5077 0.5865 -0.0410 -0.0548 0.0359  53  LEU A CA  
365  C C   . LEU A 54  ? 0.4724 0.4769 0.5454 -0.0366 -0.0522 0.0403  53  LEU A C   
366  O O   . LEU A 54  ? 0.5151 0.5124 0.5860 -0.0371 -0.0528 0.0460  53  LEU A O   
367  C CB  . LEU A 54  ? 0.4566 0.4666 0.5435 -0.0480 -0.0534 0.0404  53  LEU A CB  
368  C CG  . LEU A 54  ? 0.5309 0.5416 0.6198 -0.0526 -0.0510 0.0506  53  LEU A CG  
369  C CD1 . LEU A 54  ? 0.6210 0.6140 0.7119 -0.0558 -0.0544 0.0531  53  LEU A CD1 
370  C CD2 . LEU A 54  ? 0.4647 0.4887 0.5622 -0.0592 -0.0485 0.0547  53  LEU A CD2 
371  N N   . ALA A 55  ? 0.4079 0.4233 0.4775 -0.0321 -0.0499 0.0375  54  ALA A N   
372  C CA  . ALA A 55  ? 0.4877 0.5087 0.5509 -0.0281 -0.0478 0.0407  54  ALA A CA  
373  C C   . ALA A 55  ? 0.5372 0.5480 0.5956 -0.0240 -0.0504 0.0402  54  ALA A C   
374  O O   . ALA A 55  ? 0.5411 0.5532 0.5942 -0.0222 -0.0500 0.0454  54  ALA A O   
375  C CB  . ALA A 55  ? 0.4277 0.4604 0.4891 -0.0235 -0.0456 0.0357  54  ALA A CB  
376  N N   . GLY A 56  ? 0.4364 0.4381 0.4963 -0.0220 -0.0531 0.0343  55  GLY A N   
377  C CA  . GLY A 56  ? 0.4524 0.4454 0.5096 -0.0179 -0.0557 0.0335  55  GLY A CA  
378  C C   . GLY A 56  ? 0.5142 0.4934 0.5743 -0.0203 -0.0584 0.0354  55  GLY A C   
379  O O   . GLY A 56  ? 0.5004 0.4716 0.5603 -0.0164 -0.0607 0.0325  55  GLY A O   
380  N N   . ALA A 57  ? 0.4597 0.4362 0.5234 -0.0264 -0.0581 0.0399  56  ALA A N   
381  C CA  . ALA A 57  ? 0.4667 0.4288 0.5343 -0.0294 -0.0610 0.0417  56  ALA A CA  
382  C C   . ALA A 57  ? 0.5058 0.4595 0.5756 -0.0274 -0.0636 0.0328  56  ALA A C   
383  O O   . ALA A 57  ? 0.4992 0.4398 0.5708 -0.0268 -0.0664 0.0321  56  ALA A O   
384  C CB  . ALA A 57  ? 0.4759 0.4302 0.5404 -0.0268 -0.0624 0.0486  56  ALA A CB  
385  N N   . GLY A 58  ? 0.5466 0.5078 0.6160 -0.0259 -0.0625 0.0261  57  GLY A N   
386  C CA  . GLY A 58  ? 0.5072 0.4630 0.5777 -0.0243 -0.0642 0.0182  57  GLY A CA  
387  C C   . GLY A 58  ? 0.4779 0.4259 0.5467 -0.0183 -0.0654 0.0145  57  GLY A C   
388  O O   . GLY A 58  ? 0.4879 0.4290 0.5577 -0.0170 -0.0670 0.0086  57  GLY A O   
389  N N   . ILE A 59  ? 0.3944 0.3446 0.4612 -0.0142 -0.0648 0.0173  58  ILE A N   
390  C CA  . ILE A 59  ? 0.4272 0.3719 0.4942 -0.0082 -0.0660 0.0139  58  ILE A CA  
391  C C   . ILE A 59  ? 0.3700 0.3220 0.4369 -0.0044 -0.0639 0.0078  58  ILE A C   
392  O O   . ILE A 59  ? 0.4587 0.4085 0.5271 0.0004  -0.0643 0.0047  58  ILE A O   
393  C CB  . ILE A 59  ? 0.4351 0.3795 0.5007 -0.0051 -0.0672 0.0195  58  ILE A CB  
394  C CG1 . ILE A 59  ? 0.3487 0.3061 0.4116 -0.0038 -0.0653 0.0205  58  ILE A CG1 
395  C CG2 . ILE A 59  ? 0.4402 0.3772 0.5055 -0.0088 -0.0687 0.0275  58  ILE A CG2 
396  C CD1 . ILE A 59  ? 0.4561 0.4150 0.5167 0.0005  -0.0672 0.0240  58  ILE A CD1 
397  N N   . PHE A 60  ? 0.3817 0.3424 0.4477 -0.0064 -0.0616 0.0065  59  PHE A N   
398  C CA  . PHE A 60  ? 0.4149 0.3829 0.4815 -0.0032 -0.0592 0.0030  59  PHE A CA  
399  C C   . PHE A 60  ? 0.4133 0.3779 0.4811 0.0002  -0.0586 -0.0023 59  PHE A C   
400  O O   . PHE A 60  ? 0.4614 0.4287 0.5316 0.0041  -0.0575 -0.0040 59  PHE A O   
401  C CB  . PHE A 60  ? 0.4393 0.4155 0.5051 -0.0057 -0.0572 0.0031  59  PHE A CB  
402  C CG  . PHE A 60  ? 0.4340 0.4157 0.4988 -0.0080 -0.0569 0.0076  59  PHE A CG  
403  C CD1 . PHE A 60  ? 0.4218 0.4075 0.4859 -0.0056 -0.0568 0.0090  59  PHE A CD1 
404  C CD2 . PHE A 60  ? 0.4595 0.4437 0.5243 -0.0125 -0.0569 0.0101  59  PHE A CD2 
405  C CE1 . PHE A 60  ? 0.4183 0.4104 0.4803 -0.0070 -0.0562 0.0127  59  PHE A CE1 
406  C CE2 . PHE A 60  ? 0.4680 0.4590 0.5320 -0.0143 -0.0558 0.0144  59  PHE A CE2 
407  C CZ  . PHE A 60  ? 0.3705 0.3654 0.4323 -0.0113 -0.0553 0.0157  59  PHE A CZ  
408  N N   . ASN A 61  ? 0.3976 0.3569 0.4640 -0.0010 -0.0595 -0.0051 60  ASN A N   
409  C CA  . ASN A 61  ? 0.4321 0.3889 0.4983 0.0030  -0.0586 -0.0106 60  ASN A CA  
410  C C   . ASN A 61  ? 0.4251 0.3762 0.4943 0.0073  -0.0598 -0.0114 60  ASN A C   
411  O O   . ASN A 61  ? 0.3529 0.3067 0.4240 0.0118  -0.0577 -0.0147 60  ASN A O   
412  C CB  . ASN A 61  ? 0.4090 0.3606 0.4723 0.0012  -0.0603 -0.0146 60  ASN A CB  
413  C CG  . ASN A 61  ? 0.4825 0.4419 0.5426 -0.0006 -0.0588 -0.0155 60  ASN A CG  
414  O OD1 . ASN A 61  ? 0.5168 0.4748 0.5751 -0.0036 -0.0612 -0.0176 60  ASN A OD1 
415  N ND2 . ASN A 61  ? 0.4302 0.3981 0.4905 0.0012  -0.0553 -0.0139 60  ASN A ND2 
416  N N   . GLY A 62  ? 0.4286 0.3724 0.4987 0.0063  -0.0629 -0.0078 61  GLY A N   
417  C CA  . GLY A 62  ? 0.3364 0.2753 0.4097 0.0111  -0.0646 -0.0076 61  GLY A CA  
418  C C   . GLY A 62  ? 0.3349 0.2830 0.4111 0.0141  -0.0635 -0.0061 61  GLY A C   
419  O O   . GLY A 62  ? 0.3844 0.3335 0.4647 0.0192  -0.0634 -0.0086 61  GLY A O   
420  N N   . VAL A 63  ? 0.4282 0.3835 0.5028 0.0111  -0.0628 -0.0026 62  VAL A N   
421  C CA  . VAL A 63  ? 0.4059 0.3703 0.4837 0.0134  -0.0621 -0.0026 62  VAL A CA  
422  C C   . VAL A 63  ? 0.3939 0.3636 0.4762 0.0158  -0.0588 -0.0074 62  VAL A C   
423  O O   . VAL A 63  ? 0.3483 0.3216 0.4364 0.0196  -0.0589 -0.0092 62  VAL A O   
424  C CB  . VAL A 63  ? 0.4146 0.3857 0.4897 0.0100  -0.0616 0.0002  62  VAL A CB  
425  C CG1 . VAL A 63  ? 0.3421 0.3220 0.4213 0.0122  -0.0613 -0.0016 62  VAL A CG1 
426  C CG2 . VAL A 63  ? 0.3684 0.3362 0.4390 0.0081  -0.0641 0.0059  62  VAL A CG2 
427  N N   . THR A 64  ? 0.3817 0.3529 0.4617 0.0136  -0.0558 -0.0091 63  THR A N   
428  C CA  . THR A 64  ? 0.4054 0.3819 0.4886 0.0156  -0.0518 -0.0123 63  THR A CA  
429  C C   . THR A 64  ? 0.3920 0.3657 0.4777 0.0203  -0.0514 -0.0158 63  THR A C   
430  O O   . THR A 64  ? 0.3965 0.3764 0.4886 0.0233  -0.0489 -0.0174 63  THR A O   
431  C CB  . THR A 64  ? 0.3792 0.3569 0.4574 0.0130  -0.0493 -0.0125 63  THR A CB  
432  O OG1 . THR A 64  ? 0.3504 0.3319 0.4279 0.0096  -0.0493 -0.0096 63  THR A OG1 
433  C CG2 . THR A 64  ? 0.3560 0.3391 0.4362 0.0153  -0.0446 -0.0145 63  THR A CG2 
434  N N   . LYS A 65  ? 0.3907 0.3551 0.4725 0.0209  -0.0538 -0.0173 64  LYS A N   
435  C CA  . LYS A 65  ? 0.3561 0.3170 0.4398 0.0262  -0.0534 -0.0218 64  LYS A CA  
436  C C   . LYS A 65  ? 0.4142 0.3772 0.5056 0.0307  -0.0548 -0.0213 64  LYS A C   
437  O O   . LYS A 65  ? 0.3773 0.3462 0.4742 0.0352  -0.0520 -0.0245 64  LYS A O   
438  C CB  . LYS A 65  ? 0.3734 0.3219 0.4524 0.0257  -0.0568 -0.0238 64  LYS A CB  
439  C CG  . LYS A 65  ? 0.4326 0.3762 0.5130 0.0319  -0.0567 -0.0301 64  LYS A CG  
440  C CD  . LYS A 65  ? 0.4829 0.4177 0.5680 0.0354  -0.0609 -0.0289 64  LYS A CD  
441  C CE  . LYS A 65  ? 0.4624 0.3929 0.5502 0.0428  -0.0606 -0.0357 64  LYS A CE  
442  N NZ  . LYS A 65  ? 0.4577 0.4013 0.5481 0.0472  -0.0549 -0.0396 64  LYS A NZ  
443  N N   . TYR A 66  ? 0.3504 0.3101 0.4423 0.0298  -0.0591 -0.0171 65  TYR A N   
444  C CA  . TYR A 66  ? 0.3960 0.3570 0.4945 0.0349  -0.0617 -0.0167 65  TYR A CA  
445  C C   . TYR A 66  ? 0.3677 0.3417 0.4731 0.0351  -0.0604 -0.0164 65  TYR A C   
446  O O   . TYR A 66  ? 0.3974 0.3768 0.5110 0.0399  -0.0610 -0.0182 65  TYR A O   
447  C CB  . TYR A 66  ? 0.3702 0.3224 0.4657 0.0345  -0.0670 -0.0116 65  TYR A CB  
448  C CG  . TYR A 66  ? 0.3989 0.3369 0.4916 0.0356  -0.0689 -0.0124 65  TYR A CG  
449  C CD1 . TYR A 66  ? 0.4300 0.3633 0.5273 0.0421  -0.0695 -0.0168 65  TYR A CD1 
450  C CD2 . TYR A 66  ? 0.3921 0.3216 0.4788 0.0300  -0.0701 -0.0095 65  TYR A CD2 
451  C CE1 . TYR A 66  ? 0.4161 0.3349 0.5115 0.0432  -0.0717 -0.0187 65  TYR A CE1 
452  C CE2 . TYR A 66  ? 0.4427 0.3583 0.5286 0.0302  -0.0724 -0.0108 65  TYR A CE2 
453  C CZ  . TYR A 66  ? 0.4550 0.3644 0.5449 0.0369  -0.0734 -0.0157 65  TYR A CZ  
454  O OH  . TYR A 66  ? 0.5143 0.4085 0.6039 0.0371  -0.0761 -0.0180 65  TYR A OH  
455  N N   . VAL A 67  ? 0.3799 0.3592 0.4834 0.0302  -0.0590 -0.0147 66  VAL A N   
456  C CA  . VAL A 67  ? 0.3535 0.3440 0.4648 0.0298  -0.0576 -0.0156 66  VAL A CA  
457  C C   . VAL A 67  ? 0.3954 0.3923 0.5139 0.0318  -0.0524 -0.0189 66  VAL A C   
458  O O   . VAL A 67  ? 0.3990 0.4043 0.5280 0.0343  -0.0520 -0.0205 66  VAL A O   
459  C CB  . VAL A 67  ? 0.4491 0.4423 0.5569 0.0245  -0.0568 -0.0138 66  VAL A CB  
460  C CG1 . VAL A 67  ? 0.3901 0.3930 0.5071 0.0234  -0.0543 -0.0156 66  VAL A CG1 
461  C CG2 . VAL A 67  ? 0.3496 0.3407 0.4522 0.0236  -0.0617 -0.0108 66  VAL A CG2 
462  N N   . ALA A 68  ? 0.3975 0.3914 0.5104 0.0309  -0.0483 -0.0199 67  ALA A N   
463  C CA  . ALA A 68  ? 0.4229 0.4231 0.5404 0.0336  -0.0427 -0.0225 67  ALA A CA  
464  C C   . ALA A 68  ? 0.4469 0.4480 0.5704 0.0400  -0.0434 -0.0257 67  ALA A C   
465  O O   . ALA A 68  ? 0.4569 0.4682 0.5905 0.0426  -0.0399 -0.0271 67  ALA A O   
466  C CB  . ALA A 68  ? 0.3887 0.3850 0.4964 0.0325  -0.0393 -0.0233 67  ALA A CB  
467  N N   . GLN A 69  ? 0.3900 0.3807 0.5086 0.0428  -0.0477 -0.0267 68  GLN A N   
468  C CA  . GLN A 69  ? 0.3640 0.3542 0.4883 0.0500  -0.0486 -0.0301 68  GLN A CA  
469  C C   . GLN A 69  ? 0.4147 0.4137 0.5509 0.0526  -0.0511 -0.0291 68  GLN A C   
470  O O   . GLN A 69  ? 0.3276 0.3339 0.4731 0.0582  -0.0492 -0.0321 68  GLN A O   
471  C CB  . GLN A 69  ? 0.3893 0.3643 0.5067 0.0520  -0.0535 -0.0307 68  GLN A CB  
472  C CG  . GLN A 69  ? 0.4369 0.4090 0.5601 0.0602  -0.0550 -0.0344 68  GLN A CG  
473  C CD  . GLN A 69  ? 0.4390 0.3938 0.5562 0.0617  -0.0599 -0.0346 68  GLN A CD  
474  O OE1 . GLN A 69  ? 0.4791 0.4251 0.5876 0.0571  -0.0602 -0.0348 68  GLN A OE1 
475  N NE2 . GLN A 69  ? 0.4280 0.3779 0.5508 0.0680  -0.0640 -0.0344 68  GLN A NE2 
476  N N   . TYR A 70  ? 0.3855 0.3853 0.5216 0.0490  -0.0553 -0.0254 69  TYR A N   
477  C CA  . TYR A 70  ? 0.3670 0.3751 0.5131 0.0515  -0.0594 -0.0249 69  TYR A CA  
478  C C   . TYR A 70  ? 0.3877 0.4075 0.5412 0.0467  -0.0579 -0.0247 69  TYR A C   
479  O O   . TYR A 70  ? 0.3614 0.3869 0.5203 0.0468  -0.0627 -0.0243 69  TYR A O   
480  C CB  . TYR A 70  ? 0.4013 0.4012 0.5413 0.0524  -0.0667 -0.0211 69  TYR A CB  
481  C CG  . TYR A 70  ? 0.4148 0.4021 0.5505 0.0574  -0.0692 -0.0207 69  TYR A CG  
482  C CD1 . TYR A 70  ? 0.4199 0.4092 0.5641 0.0651  -0.0699 -0.0236 69  TYR A CD1 
483  C CD2 . TYR A 70  ? 0.3995 0.3730 0.5240 0.0545  -0.0710 -0.0174 69  TYR A CD2 
484  C CE1 . TYR A 70  ? 0.4259 0.4020 0.5670 0.0702  -0.0726 -0.0236 69  TYR A CE1 
485  C CE2 . TYR A 70  ? 0.3921 0.3525 0.5141 0.0586  -0.0736 -0.0170 69  TYR A CE2 
486  C CZ  . TYR A 70  ? 0.4214 0.3823 0.5515 0.0667  -0.0745 -0.0203 69  TYR A CZ  
487  O OH  . TYR A 70  ? 0.4398 0.3863 0.5683 0.0713  -0.0774 -0.0203 69  TYR A OH  
488  N N   . HIS A 71  ? 0.4640 0.4873 0.6179 0.0427  -0.0515 -0.0251 70  HIS A N   
489  C CA  . HIS A 71  ? 0.5359 0.5679 0.6974 0.0377  -0.0502 -0.0247 70  HIS A CA  
490  C C   . HIS A 71  ? 0.4688 0.5142 0.6476 0.0396  -0.0506 -0.0269 70  HIS A C   
491  O O   . HIS A 71  ? 0.5261 0.5782 0.7132 0.0357  -0.0518 -0.0274 70  HIS A O   
492  C CB  . HIS A 71  ? 0.5580 0.5901 0.7165 0.0336  -0.0431 -0.0234 70  HIS A CB  
493  C CG  . HIS A 71  ? 0.5851 0.6265 0.7531 0.0351  -0.0362 -0.0242 70  HIS A CG  
494  N ND1 . HIS A 71  ? 0.6360 0.6789 0.8047 0.0412  -0.0339 -0.0266 70  HIS A ND1 
495  C CD2 . HIS A 71  ? 0.7247 0.7747 0.9020 0.0316  -0.0305 -0.0227 70  HIS A CD2 
496  C CE1 . HIS A 71  ? 0.6767 0.7302 0.8543 0.0415  -0.0268 -0.0265 70  HIS A CE1 
497  N NE2 . HIS A 71  ? 0.8354 0.8932 1.0186 0.0354  -0.0245 -0.0235 70  HIS A NE2 
498  N N   . ASP A 72  ? 0.4054 0.4551 0.5908 0.0457  -0.0498 -0.0289 71  ASP A N   
499  C CA  . ASP A 72  ? 0.4356 0.4993 0.6387 0.0482  -0.0510 -0.0311 71  ASP A CA  
500  C C   . ASP A 72  ? 0.3787 0.4419 0.5832 0.0544  -0.0592 -0.0320 71  ASP A C   
501  O O   . ASP A 72  ? 0.3793 0.4535 0.5977 0.0591  -0.0603 -0.0343 71  ASP A O   
502  C CB  . ASP A 72  ? 0.4673 0.5400 0.6796 0.0511  -0.0430 -0.0325 71  ASP A CB  
503  C CG  . ASP A 72  ? 0.5744 0.6519 0.7897 0.0448  -0.0349 -0.0304 71  ASP A CG  
504  O OD1 . ASP A 72  ? 0.6374 0.7152 0.8552 0.0384  -0.0364 -0.0289 71  ASP A OD1 
505  O OD2 . ASP A 72  ? 0.6908 0.7716 0.9055 0.0468  -0.0272 -0.0302 71  ASP A OD2 
506  N N   . ASN A 73  ? 0.3679 0.4194 0.5587 0.0545  -0.0648 -0.0297 72  ASN A N   
507  C CA  . ASN A 73  ? 0.3783 0.4272 0.5676 0.0605  -0.0726 -0.0287 72  ASN A CA  
508  C C   . ASN A 73  ? 0.3945 0.4411 0.5758 0.0571  -0.0788 -0.0264 72  ASN A C   
509  O O   . ASN A 73  ? 0.4200 0.4546 0.5866 0.0552  -0.0798 -0.0229 72  ASN A O   
510  C CB  . ASN A 73  ? 0.3994 0.4342 0.5787 0.0654  -0.0725 -0.0272 72  ASN A CB  
511  C CG  . ASN A 73  ? 0.3748 0.4059 0.5537 0.0724  -0.0802 -0.0251 72  ASN A CG  
512  O OD1 . ASN A 73  ? 0.3480 0.3839 0.5275 0.0727  -0.0867 -0.0233 72  ASN A OD1 
513  N ND2 . ASN A 73  ? 0.3184 0.3403 0.4956 0.0786  -0.0799 -0.0255 72  ASN A ND2 
514  N N   . PRO A 74  ? 0.4249 0.4837 0.6160 0.0562  -0.0832 -0.0287 73  PRO A N   
515  C CA  . PRO A 74  ? 0.4367 0.4946 0.6192 0.0531  -0.0886 -0.0278 73  PRO A CA  
516  C C   . PRO A 74  ? 0.4269 0.4763 0.5957 0.0574  -0.0946 -0.0230 73  PRO A C   
517  O O   . PRO A 74  ? 0.4227 0.4655 0.5781 0.0542  -0.0955 -0.0201 73  PRO A O   
518  C CB  . PRO A 74  ? 0.4709 0.5447 0.6691 0.0527  -0.0931 -0.0326 73  PRO A CB  
519  C CG  . PRO A 74  ? 0.3891 0.4715 0.6044 0.0522  -0.0870 -0.0354 73  PRO A CG  
520  C CD  . PRO A 74  ? 0.3263 0.4011 0.5372 0.0576  -0.0832 -0.0329 73  PRO A CD  
521  N N   . GLN A 75  ? 0.3782 0.4277 0.5505 0.0648  -0.0985 -0.0215 74  GLN A N   
522  C CA  . GLN A 75  ? 0.3872 0.4283 0.5473 0.0693  -0.1044 -0.0156 74  GLN A CA  
523  C C   . GLN A 75  ? 0.3945 0.4185 0.5405 0.0666  -0.1004 -0.0106 74  GLN A C   
524  O O   . GLN A 75  ? 0.4397 0.4576 0.5727 0.0647  -0.1026 -0.0055 74  GLN A O   
525  C CB  . GLN A 75  ? 0.4054 0.4492 0.5738 0.0784  -0.1090 -0.0149 74  GLN A CB  
526  C CG  . GLN A 75  ? 0.4098 0.4715 0.5911 0.0818  -0.1154 -0.0189 74  GLN A CG  
527  C CD  . GLN A 75  ? 0.5134 0.5884 0.7127 0.0784  -0.1108 -0.0260 74  GLN A CD  
528  O OE1 . GLN A 75  ? 0.4848 0.5561 0.6878 0.0763  -0.1028 -0.0274 74  GLN A OE1 
529  N NE2 . GLN A 75  ? 0.5121 0.6029 0.7226 0.0778  -0.1159 -0.0304 74  GLN A NE2 
530  N N   . GLN A 76  ? 0.4000 0.4170 0.5486 0.0666  -0.0946 -0.0122 75  GLN A N   
531  C CA  . GLN A 76  ? 0.4132 0.4146 0.5501 0.0637  -0.0913 -0.0087 75  GLN A CA  
532  C C   . GLN A 76  ? 0.4375 0.4386 0.5669 0.0554  -0.0874 -0.0087 75  GLN A C   
533  O O   . GLN A 76  ? 0.3881 0.3796 0.5061 0.0522  -0.0873 -0.0041 75  GLN A O   
534  C CB  . GLN A 76  ? 0.4362 0.4316 0.5778 0.0663  -0.0866 -0.0121 75  GLN A CB  
535  C CG  . GLN A 76  ? 0.4536 0.4405 0.5971 0.0744  -0.0904 -0.0105 75  GLN A CG  
536  C CD  . GLN A 76  ? 0.4909 0.4612 0.6225 0.0736  -0.0935 -0.0036 75  GLN A CD  
537  O OE1 . GLN A 76  ? 0.6058 0.5757 0.7328 0.0749  -0.0989 0.0025  75  GLN A OE1 
538  N NE2 . GLN A 76  ? 0.5318 0.4889 0.6587 0.0713  -0.0901 -0.0044 75  GLN A NE2 
539  N N   . LEU A 77  ? 0.3966 0.4081 0.5334 0.0520  -0.0841 -0.0134 76  LEU A N   
540  C CA  . LEU A 77  ? 0.3819 0.3933 0.5128 0.0450  -0.0806 -0.0136 76  LEU A CA  
541  C C   . LEU A 77  ? 0.4058 0.4175 0.5273 0.0433  -0.0850 -0.0103 76  LEU A C   
542  O O   . LEU A 77  ? 0.4164 0.4219 0.5277 0.0392  -0.0831 -0.0074 76  LEU A O   
543  C CB  . LEU A 77  ? 0.3664 0.3887 0.5087 0.0422  -0.0771 -0.0185 76  LEU A CB  
544  C CG  . LEU A 77  ? 0.4642 0.4857 0.6034 0.0357  -0.0721 -0.0191 76  LEU A CG  
545  C CD1 . LEU A 77  ? 0.4261 0.4371 0.5561 0.0341  -0.0677 -0.0169 76  LEU A CD1 
546  C CD2 . LEU A 77  ? 0.4042 0.4355 0.5571 0.0337  -0.0683 -0.0229 76  LEU A CD2 
547  N N   . ARG A 78  ? 0.4276 0.4475 0.5521 0.0469  -0.0911 -0.0108 77  ARG A N   
548  C CA  . ARG A 78  ? 0.4891 0.5106 0.6030 0.0466  -0.0954 -0.0077 77  ARG A CA  
549  C C   . ARG A 78  ? 0.4022 0.4119 0.5037 0.0475  -0.0959 0.0003  77  ARG A C   
550  O O   . ARG A 78  ? 0.3736 0.3811 0.4643 0.0441  -0.0950 0.0039  77  ARG A O   
551  C CB  . ARG A 78  ? 0.4071 0.4400 0.5261 0.0514  -0.1026 -0.0100 77  ARG A CB  
552  C CG  . ARG A 78  ? 0.4701 0.5089 0.5791 0.0508  -0.1068 -0.0097 77  ARG A CG  
553  C CD  . ARG A 78  ? 0.5030 0.5504 0.6119 0.0573  -0.1153 -0.0092 77  ARG A CD  
554  N NE  . ARG A 78  ? 0.6103 0.6710 0.7337 0.0580  -0.1190 -0.0177 77  ARG A NE  
555  C CZ  . ARG A 78  ? 0.6522 0.7220 0.7768 0.0554  -0.1214 -0.0243 77  ARG A CZ  
556  N NH1 . ARG A 78  ? 0.5696 0.6376 0.6812 0.0527  -0.1203 -0.0237 77  ARG A NH1 
557  N NH2 . ARG A 78  ? 0.6034 0.6848 0.7438 0.0555  -0.1251 -0.0320 77  ARG A NH2 
558  N N   . ARG A 79  ? 0.3791 0.3811 0.4828 0.0518  -0.0970 0.0032  78  ARG A N   
559  C CA  . ARG A 79  ? 0.4044 0.3934 0.4983 0.0520  -0.0975 0.0111  78  ARG A CA  
560  C C   . ARG A 79  ? 0.4178 0.3983 0.5068 0.0453  -0.0916 0.0117  78  ARG A C   
561  O O   . ARG A 79  ? 0.4307 0.4058 0.5102 0.0421  -0.0911 0.0179  78  ARG A O   
562  C CB  . ARG A 79  ? 0.4300 0.4110 0.5294 0.0584  -0.0999 0.0129  78  ARG A CB  
563  C CG  . ARG A 79  ? 0.5282 0.5119 0.6261 0.0654  -0.1071 0.0180  78  ARG A CG  
564  C CD  . ARG A 79  ? 0.5347 0.5134 0.6419 0.0730  -0.1096 0.0174  78  ARG A CD  
565  N NE  . ARG A 79  ? 0.6033 0.5963 0.7196 0.0792  -0.1147 0.0139  78  ARG A NE  
566  C CZ  . ARG A 79  ? 0.6286 0.6286 0.7590 0.0828  -0.1138 0.0069  78  ARG A CZ  
567  N NH1 . ARG A 79  ? 0.5290 0.5232 0.6648 0.0814  -0.1078 0.0026  78  ARG A NH1 
568  N NH2 . ARG A 79  ? 0.6194 0.6339 0.7588 0.0879  -0.1191 0.0042  78  ARG A NH2 
569  N N   . VAL A 80  ? 0.3747 0.3554 0.4703 0.0431  -0.0870 0.0057  79  VAL A N   
570  C CA  . VAL A 80  ? 0.3504 0.3242 0.4416 0.0373  -0.0821 0.0056  79  VAL A CA  
571  C C   . VAL A 80  ? 0.3822 0.3615 0.4667 0.0322  -0.0807 0.0070  79  VAL A C   
572  O O   . VAL A 80  ? 0.3956 0.3693 0.4728 0.0283  -0.0794 0.0115  79  VAL A O   
573  C CB  . VAL A 80  ? 0.3846 0.3601 0.4832 0.0370  -0.0776 -0.0011 79  VAL A CB  
574  C CG1 . VAL A 80  ? 0.3775 0.3512 0.4715 0.0309  -0.0730 -0.0019 79  VAL A CG1 
575  C CG2 . VAL A 80  ? 0.3741 0.3414 0.4766 0.0417  -0.0779 -0.0025 79  VAL A CG2 
576  N N   . VAL A 81  ? 0.3913 0.3819 0.4794 0.0321  -0.0809 0.0028  80  VAL A N   
577  C CA  . VAL A 81  ? 0.3069 0.3029 0.3897 0.0281  -0.0794 0.0026  80  VAL A CA  
578  C C   . VAL A 81  ? 0.3745 0.3716 0.4474 0.0289  -0.0826 0.0084  80  VAL A C   
579  O O   . VAL A 81  ? 0.3800 0.3775 0.4457 0.0254  -0.0804 0.0112  80  VAL A O   
580  C CB  . VAL A 81  ? 0.3213 0.3276 0.4118 0.0280  -0.0795 -0.0041 80  VAL A CB  
581  C CG1 . VAL A 81  ? 0.3257 0.3368 0.4110 0.0249  -0.0785 -0.0052 80  VAL A CG1 
582  C CG2 . VAL A 81  ? 0.2913 0.2969 0.3911 0.0268  -0.0752 -0.0081 80  VAL A CG2 
583  N N   . GLY A 82  ? 0.3939 0.3926 0.4662 0.0340  -0.0877 0.0109  81  GLY A N   
584  C CA  . GLY A 82  ? 0.4394 0.4397 0.5010 0.0354  -0.0905 0.0177  81  GLY A CA  
585  C C   . GLY A 82  ? 0.4410 0.4304 0.4960 0.0325  -0.0882 0.0263  81  GLY A C   
586  O O   . GLY A 82  ? 0.4214 0.4130 0.4677 0.0298  -0.0865 0.0312  81  GLY A O   
587  N N   . THR A 83  ? 0.3909 0.3687 0.4507 0.0329  -0.0879 0.0278  82  THR A N   
588  C CA  . THR A 83  ? 0.4329 0.3990 0.4886 0.0293  -0.0861 0.0352  82  THR A CA  
589  C C   . THR A 83  ? 0.4260 0.3926 0.4806 0.0223  -0.0810 0.0335  82  THR A C   
590  O O   . THR A 83  ? 0.4194 0.3840 0.4685 0.0182  -0.0792 0.0401  82  THR A O   
591  C CB  . THR A 83  ? 0.4516 0.4044 0.5137 0.0317  -0.0874 0.0352  82  THR A CB  
592  O OG1 . THR A 83  ? 0.4508 0.4024 0.5133 0.0385  -0.0925 0.0391  82  THR A OG1 
593  C CG2 . THR A 83  ? 0.4382 0.3777 0.4984 0.0266  -0.0855 0.0408  82  THR A CG2 
594  N N   . SER A 84  ? 0.3565 0.3267 0.4166 0.0210  -0.0785 0.0252  83  SER A N   
595  C CA  . SER A 84  ? 0.3965 0.3683 0.4555 0.0153  -0.0742 0.0236  83  SER A CA  
596  C C   . SER A 84  ? 0.4542 0.4361 0.5068 0.0136  -0.0730 0.0258  83  SER A C   
597  O O   . SER A 84  ? 0.4103 0.3925 0.4596 0.0091  -0.0702 0.0294  83  SER A O   
598  C CB  . SER A 84  ? 0.3873 0.3617 0.4528 0.0151  -0.0719 0.0154  83  SER A CB  
599  O OG  . SER A 84  ? 0.4062 0.3729 0.4768 0.0174  -0.0724 0.0128  83  SER A OG  
600  N N   . SER A 85  ? 0.3809 0.3720 0.4321 0.0175  -0.0753 0.0232  84  SER A N   
601  C CA  . SER A 85  ? 0.4243 0.4255 0.4684 0.0171  -0.0746 0.0242  84  SER A CA  
602  C C   . SER A 85  ? 0.4303 0.4304 0.4658 0.0163  -0.0744 0.0343  84  SER A C   
603  O O   . SER A 85  ? 0.4439 0.4491 0.4746 0.0132  -0.0710 0.0373  84  SER A O   
604  C CB  . SER A 85  ? 0.4278 0.4384 0.4722 0.0219  -0.0782 0.0185  84  SER A CB  
605  O OG  . SER A 85  ? 0.5003 0.5200 0.5351 0.0234  -0.0790 0.0208  84  SER A OG  
606  N N   . ALA A 86  ? 0.3938 0.3875 0.4278 0.0193  -0.0778 0.0402  85  ALA A N   
607  C CA  . ALA A 86  ? 0.4321 0.4233 0.4585 0.0183  -0.0775 0.0516  85  ALA A CA  
608  C C   . ALA A 86  ? 0.4954 0.4793 0.5241 0.0113  -0.0732 0.0563  85  ALA A C   
609  O O   . ALA A 86  ? 0.4745 0.4626 0.4978 0.0081  -0.0702 0.0637  85  ALA A O   
610  C CB  . ALA A 86  ? 0.4119 0.3952 0.4380 0.0231  -0.0822 0.0572  85  ALA A CB  
611  N N   . MET A 87  ? 0.4331 0.4073 0.4702 0.0088  -0.0728 0.0518  86  MET A N   
612  C CA  . MET A 87  ? 0.4383 0.4052 0.4787 0.0020  -0.0700 0.0552  86  MET A CA  
613  C C   . MET A 87  ? 0.4443 0.4216 0.4843 -0.0023 -0.0657 0.0525  86  MET A C   
614  O O   . MET A 87  ? 0.4578 0.4360 0.4976 -0.0077 -0.0629 0.0585  86  MET A O   
615  C CB  . MET A 87  ? 0.3992 0.3537 0.4476 0.0015  -0.0714 0.0497  86  MET A CB  
616  C CG  . MET A 87  ? 0.4992 0.4408 0.5492 0.0051  -0.0752 0.0538  86  MET A CG  
617  S SD  . MET A 87  ? 0.4818 0.4111 0.5404 0.0068  -0.0769 0.0449  86  MET A SD  
618  C CE  . MET A 87  ? 0.4484 0.3667 0.5103 -0.0015 -0.0755 0.0474  86  MET A CE  
619  N N   . VAL A 88  ? 0.4500 0.4354 0.4909 -0.0001 -0.0651 0.0438  87  VAL A N   
620  C CA  . VAL A 88  ? 0.4196 0.4148 0.4604 -0.0030 -0.0614 0.0410  87  VAL A CA  
621  C C   . VAL A 88  ? 0.4725 0.4793 0.5056 -0.0020 -0.0595 0.0459  87  VAL A C   
622  O O   . VAL A 88  ? 0.4723 0.4852 0.5048 -0.0059 -0.0558 0.0494  87  VAL A O   
623  C CB  . VAL A 88  ? 0.4505 0.4495 0.4951 -0.0005 -0.0613 0.0310  87  VAL A CB  
624  C CG1 . VAL A 88  ? 0.4934 0.5034 0.5370 -0.0016 -0.0581 0.0283  87  VAL A CG1 
625  C CG2 . VAL A 88  ? 0.4363 0.4261 0.4874 -0.0022 -0.0616 0.0270  87  VAL A CG2 
626  N N   . LEU A 89  ? 0.4883 0.4993 0.5152 0.0034  -0.0621 0.0460  88  LEU A N   
627  C CA  . LEU A 89  ? 0.4824 0.5053 0.5001 0.0052  -0.0605 0.0506  88  LEU A CA  
628  C C   . LEU A 89  ? 0.5272 0.5480 0.5417 0.0012  -0.0580 0.0631  88  LEU A C   
629  O O   . LEU A 89  ? 0.4499 0.4804 0.4613 -0.0014 -0.0535 0.0672  88  LEU A O   
630  C CB  . LEU A 89  ? 0.5077 0.5350 0.5190 0.0121  -0.0650 0.0485  88  LEU A CB  
631  C CG  . LEU A 89  ? 0.6443 0.6805 0.6433 0.0147  -0.0646 0.0567  88  LEU A CG  
632  C CD1 . LEU A 89  ? 0.6804 0.7321 0.6735 0.0162  -0.0613 0.0522  88  LEU A CD1 
633  C CD2 . LEU A 89  ? 0.6757 0.7116 0.6693 0.0212  -0.0706 0.0578  88  LEU A CD2 
634  N N   . GLY A 90  ? 0.5498 0.5579 0.5660 0.0005  -0.0606 0.0695  89  GLY A N   
635  C CA  . GLY A 90  ? 0.4342 0.4384 0.4485 -0.0036 -0.0585 0.0825  89  GLY A CA  
636  C C   . GLY A 90  ? 0.5141 0.5179 0.5359 -0.0117 -0.0541 0.0844  89  GLY A C   
637  O O   . GLY A 90  ? 0.5882 0.5995 0.6077 -0.0154 -0.0498 0.0929  89  GLY A O   
638  N N   . PHE A 91  ? 0.5149 0.5111 0.5457 -0.0145 -0.0551 0.0766  90  PHE A N   
639  C CA  . PHE A 91  ? 0.5558 0.5517 0.5945 -0.0221 -0.0522 0.0778  90  PHE A CA  
640  C C   . PHE A 91  ? 0.5326 0.5454 0.5703 -0.0229 -0.0478 0.0747  90  PHE A C   
641  O O   . PHE A 91  ? 0.5315 0.5512 0.5721 -0.0283 -0.0438 0.0807  90  PHE A O   
642  C CB  . PHE A 91  ? 0.4844 0.4685 0.5315 -0.0240 -0.0550 0.0697  90  PHE A CB  
643  C CG  . PHE A 91  ? 0.4723 0.4530 0.5281 -0.0321 -0.0538 0.0717  90  PHE A CG  
644  C CD1 . PHE A 91  ? 0.5874 0.5556 0.6478 -0.0370 -0.0550 0.0793  90  PHE A CD1 
645  C CD2 . PHE A 91  ? 0.4968 0.4866 0.5568 -0.0348 -0.0518 0.0658  90  PHE A CD2 
646  C CE1 . PHE A 91  ? 0.5109 0.4762 0.5808 -0.0452 -0.0545 0.0802  90  PHE A CE1 
647  C CE2 . PHE A 91  ? 0.5426 0.5307 0.6113 -0.0424 -0.0514 0.0670  90  PHE A CE2 
648  C CZ  . PHE A 91  ? 0.5519 0.5279 0.6260 -0.0479 -0.0529 0.0738  90  PHE A CZ  
649  N N   . SER A 92  ? 0.4875 0.5074 0.5222 -0.0174 -0.0484 0.0653  91  SER A N   
650  C CA  . SER A 92  ? 0.5257 0.5607 0.5597 -0.0170 -0.0445 0.0615  91  SER A CA  
651  C C   . SER A 92  ? 0.4728 0.5208 0.4990 -0.0160 -0.0406 0.0692  91  SER A C   
652  O O   . SER A 92  ? 0.4401 0.5002 0.4681 -0.0184 -0.0360 0.0708  91  SER A O   
653  C CB  . SER A 92  ? 0.4646 0.5024 0.4973 -0.0110 -0.0464 0.0504  91  SER A CB  
654  O OG  . SER A 92  ? 0.6610 0.7078 0.6976 -0.0116 -0.0436 0.0451  91  SER A OG  
655  N N   . THR A 93  ? 0.4378 0.4846 0.4550 -0.0120 -0.0424 0.0742  92  THR A N   
656  C CA  . THR A 93  ? 0.5340 0.5934 0.5421 -0.0108 -0.0385 0.0828  92  THR A CA  
657  C C   . THR A 93  ? 0.6105 0.6693 0.6234 -0.0186 -0.0342 0.0953  92  THR A C   
658  O O   . THR A 93  ? 0.5554 0.6286 0.5672 -0.0206 -0.0284 0.0999  92  THR A O   
659  C CB  . THR A 93  ? 0.6072 0.6649 0.6042 -0.0045 -0.0422 0.0860  92  THR A CB  
660  O OG1 . THR A 93  ? 0.5412 0.6027 0.5348 0.0023  -0.0459 0.0738  92  THR A OG1 
661  C CG2 . THR A 93  ? 0.6564 0.7269 0.6422 -0.0032 -0.0379 0.0968  92  THR A CG2 
662  N N   . LEU A 94  ? 0.5721 0.6144 0.5915 -0.0233 -0.0370 0.1005  93  LEU A N   
663  C CA  . LEU A 94  ? 0.5630 0.6025 0.5899 -0.0319 -0.0336 0.1116  93  LEU A CA  
664  C C   . LEU A 94  ? 0.5665 0.6152 0.6036 -0.0376 -0.0300 0.1074  93  LEU A C   
665  O O   . LEU A 94  ? 0.5694 0.6284 0.6101 -0.0429 -0.0246 0.1159  93  LEU A O   
666  C CB  . LEU A 94  ? 0.5425 0.5605 0.5763 -0.0354 -0.0383 0.1148  93  LEU A CB  
667  C CG  . LEU A 94  ? 0.7035 0.7122 0.7309 -0.0335 -0.0398 0.1269  93  LEU A CG  
668  C CD1 . LEU A 94  ? 0.7491 0.7681 0.7615 -0.0242 -0.0405 0.1269  93  LEU A CD1 
669  C CD2 . LEU A 94  ? 0.7548 0.7415 0.7883 -0.0335 -0.0460 0.1247  93  LEU A CD2 
670  N N   . MET A 95  ? 0.5011 0.5473 0.5433 -0.0363 -0.0329 0.0950  94  MET A N   
671  C CA  . MET A 95  ? 0.5226 0.5781 0.5741 -0.0405 -0.0303 0.0905  94  MET A CA  
672  C C   . MET A 95  ? 0.5163 0.5930 0.5634 -0.0375 -0.0245 0.0910  94  MET A C   
673  O O   . MET A 95  ? 0.5788 0.6672 0.6333 -0.0426 -0.0200 0.0949  94  MET A O   
674  C CB  . MET A 95  ? 0.5543 0.6034 0.6097 -0.0380 -0.0345 0.0777  94  MET A CB  
675  C CG  . MET A 95  ? 0.5990 0.6315 0.6626 -0.0431 -0.0389 0.0763  94  MET A CG  
676  S SD  . MET A 95  ? 0.7284 0.7665 0.8057 -0.0514 -0.0380 0.0749  94  MET A SD  
677  C CE  . MET A 95  ? 0.6336 0.6658 0.7178 -0.0607 -0.0366 0.0883  94  MET A CE  
678  N N   . ALA A 96  ? 0.4878 0.5704 0.5236 -0.0292 -0.0247 0.0864  95  ALA A N   
679  C CA  . ALA A 96  ? 0.5114 0.6138 0.5417 -0.0250 -0.0195 0.0852  95  ALA A CA  
680  C C   . ALA A 96  ? 0.5606 0.6743 0.5884 -0.0286 -0.0133 0.0987  95  ALA A C   
681  O O   . ALA A 96  ? 0.5378 0.6688 0.5684 -0.0295 -0.0074 0.1001  95  ALA A O   
682  C CB  . ALA A 96  ? 0.4664 0.5710 0.4847 -0.0155 -0.0220 0.0774  95  ALA A CB  
683  N N   . LEU A 97  ? 0.5468 0.6511 0.5699 -0.0305 -0.0143 0.1093  96  LEU A N   
684  C CA  . LEU A 97  ? 0.5269 0.6407 0.5476 -0.0344 -0.0081 0.1242  96  LEU A CA  
685  C C   . LEU A 97  ? 0.5550 0.6704 0.5919 -0.0451 -0.0046 0.1306  96  LEU A C   
686  O O   . LEU A 97  ? 0.5497 0.6824 0.5890 -0.0481 0.0027  0.1380  96  LEU A O   
687  C CB  . LEU A 97  ? 0.5573 0.6585 0.5695 -0.0335 -0.0108 0.1346  96  LEU A CB  
688  C CG  . LEU A 97  ? 0.7034 0.8060 0.6993 -0.0230 -0.0144 0.1296  96  LEU A CG  
689  C CD1 . LEU A 97  ? 0.7951 0.8806 0.7863 -0.0220 -0.0195 0.1374  96  LEU A CD1 
690  C CD2 . LEU A 97  ? 0.7476 0.8722 0.7303 -0.0176 -0.0083 0.1333  96  LEU A CD2 
691  N N   . VAL A 98  ? 0.5635 0.6618 0.6120 -0.0508 -0.0097 0.1275  97  VAL A N   
692  C CA  . VAL A 98  ? 0.5515 0.6507 0.6167 -0.0613 -0.0078 0.1318  97  VAL A CA  
693  C C   . VAL A 98  ? 0.6221 0.7411 0.6940 -0.0611 -0.0040 0.1249  97  VAL A C   
694  O O   . VAL A 98  ? 0.6127 0.7449 0.6951 -0.0678 0.0013  0.1318  97  VAL A O   
695  C CB  . VAL A 98  ? 0.6221 0.6992 0.6967 -0.0659 -0.0152 0.1267  97  VAL A CB  
696  C CG1 . VAL A 98  ? 0.6809 0.7619 0.7726 -0.0744 -0.0152 0.1238  97  VAL A CG1 
697  C CG2 . VAL A 98  ? 0.6073 0.6666 0.6812 -0.0694 -0.0172 0.1377  97  VAL A CG2 
698  N N   . PHE A 99  ? 0.5566 0.6784 0.6235 -0.0532 -0.0065 0.1117  98  PHE A N   
699  C CA  . PHE A 99  ? 0.5619 0.7010 0.6354 -0.0517 -0.0036 0.1046  98  PHE A CA  
700  C C   . PHE A 99  ? 0.5825 0.7446 0.6509 -0.0486 0.0047  0.1100  98  PHE A C   
701  O O   . PHE A 99  ? 0.5743 0.7532 0.6533 -0.0523 0.0096  0.1121  98  PHE A O   
702  C CB  . PHE A 99  ? 0.5363 0.6707 0.6054 -0.0436 -0.0083 0.0901  98  PHE A CB  
703  C CG  . PHE A 99  ? 0.5827 0.7068 0.6625 -0.0472 -0.0137 0.0830  98  PHE A CG  
704  C CD1 . PHE A 99  ? 0.5295 0.6358 0.6141 -0.0534 -0.0183 0.0856  98  PHE A CD1 
705  C CD2 . PHE A 99  ? 0.6006 0.7328 0.6852 -0.0437 -0.0143 0.0737  98  PHE A CD2 
706  C CE1 . PHE A 99  ? 0.5533 0.6513 0.6463 -0.0561 -0.0233 0.0784  98  PHE A CE1 
707  C CE2 . PHE A 99  ? 0.6177 0.7414 0.7107 -0.0464 -0.0193 0.0677  98  PHE A CE2 
708  C CZ  . PHE A 99  ? 0.5573 0.6644 0.6539 -0.0526 -0.0238 0.0698  98  PHE A CZ  
709  N N   . VAL A 100 ? 0.5598 0.7243 0.6121 -0.0414 0.0062  0.1117  99  VAL A N   
710  C CA  . VAL A 100 ? 0.5792 0.7666 0.6243 -0.0369 0.0140  0.1153  99  VAL A CA  
711  C C   . VAL A 100 ? 0.6010 0.7978 0.6510 -0.0451 0.0211  0.1320  99  VAL A C   
712  O O   . VAL A 100 ? 0.5768 0.7959 0.6304 -0.0454 0.0289  0.1357  99  VAL A O   
713  C CB  . VAL A 100 ? 0.6295 0.8171 0.6551 -0.0264 0.0127  0.1111  99  VAL A CB  
714  C CG1 . VAL A 100 ? 0.6527 0.8277 0.6689 -0.0279 0.0106  0.1220  99  VAL A CG1 
715  C CG2 . VAL A 100 ? 0.7053 0.9176 0.7226 -0.0197 0.0202  0.1105  99  VAL A CG2 
716  N N   . LEU A 101 ? 0.6285 0.8087 0.6801 -0.0519 0.0187  0.1424  100 LEU A N   
717  C CA  . LEU A 101 ? 0.6421 0.8293 0.6990 -0.0602 0.0253  0.1597  100 LEU A CA  
718  C C   . LEU A 101 ? 0.6306 0.8249 0.7094 -0.0707 0.0278  0.1617  100 LEU A C   
719  O O   . LEU A 101 ? 0.7470 0.9601 0.8325 -0.0755 0.0362  0.1721  100 LEU A O   
720  C CB  . LEU A 101 ? 0.6381 0.8031 0.6912 -0.0640 0.0214  0.1702  100 LEU A CB  
721  C CG  . LEU A 101 ? 0.6911 0.8599 0.7253 -0.0582 0.0247  0.1812  100 LEU A CG  
722  C CD1 . LEU A 101 ? 0.7549 0.9461 0.7897 -0.0619 0.0356  0.1957  100 LEU A CD1 
723  C CD2 . LEU A 101 ? 0.7380 0.9120 0.7540 -0.0450 0.0219  0.1690  100 LEU A CD2 
724  N N   . ALA A 102 ? 0.6393 0.8204 0.7298 -0.0741 0.0207  0.1518  101 ALA A N   
725  C CA  . ALA A 102 ? 0.5776 0.7640 0.6894 -0.0840 0.0210  0.1521  101 ALA A CA  
726  C C   . ALA A 102 ? 0.4769 0.6765 0.5943 -0.0792 0.0200  0.1381  101 ALA A C   
727  O O   . ALA A 102 ? 0.5045 0.7004 0.6363 -0.0843 0.0153  0.1321  101 ALA A O   
728  C CB  . ALA A 102 ? 0.5786 0.7402 0.7005 -0.0924 0.0132  0.1521  101 ALA A CB  
729  N N   . ALA A 103 ? 0.4686 0.6837 0.5746 -0.0688 0.0240  0.1328  102 ALA A N   
730  C CA  . ALA A 103 ? 0.5076 0.7342 0.6186 -0.0630 0.0230  0.1199  102 ALA A CA  
731  C C   . ALA A 103 ? 0.5696 0.8151 0.7006 -0.0701 0.0269  0.1227  102 ALA A C   
732  O O   . ALA A 103 ? 0.5315 0.7799 0.6724 -0.0691 0.0230  0.1130  102 ALA A O   
733  C CB  . ALA A 103 ? 0.4708 0.7107 0.5666 -0.0506 0.0271  0.1140  102 ALA A CB  
734  N N   . ALA A 104 ? 0.5261 0.7857 0.6641 -0.0774 0.0346  0.1363  103 ALA A N   
735  C CA  . ALA A 104 ? 0.4957 0.7751 0.6550 -0.0849 0.0384  0.1392  103 ALA A CA  
736  C C   . ALA A 104 ? 0.5344 0.7996 0.7113 -0.0961 0.0308  0.1384  103 ALA A C   
737  O O   . ALA A 104 ? 0.5387 0.8123 0.7292 -0.0970 0.0275  0.1302  103 ALA A O   
738  C CB  . ALA A 104 ? 0.4586 0.7589 0.6210 -0.0895 0.0496  0.1545  103 ALA A CB  
739  N N   . PRO A 105 ? 0.5467 0.7907 0.7243 -0.1044 0.0273  0.1458  104 PRO A N   
740  C CA  . PRO A 105 ? 0.5378 0.7673 0.7315 -0.1141 0.0190  0.1422  104 PRO A CA  
741  C C   . PRO A 105 ? 0.5205 0.7370 0.7095 -0.1075 0.0097  0.1263  104 PRO A C   
742  O O   . PRO A 105 ? 0.5171 0.7332 0.7204 -0.1126 0.0039  0.1200  104 PRO A O   
743  C CB  . PRO A 105 ? 0.6012 0.8080 0.7921 -0.1213 0.0174  0.1526  104 PRO A CB  
744  C CG  . PRO A 105 ? 0.6295 0.8476 0.8104 -0.1194 0.0273  0.1662  104 PRO A CG  
745  C CD  . PRO A 105 ? 0.5418 0.7752 0.7073 -0.1057 0.0308  0.1583  104 PRO A CD  
746  N N   . ILE A 106 ? 0.5282 0.7345 0.6978 -0.0965 0.0079  0.1200  105 ILE A N   
747  C CA  . ILE A 106 ? 0.5389 0.7336 0.7040 -0.0901 0.0000  0.1060  105 ILE A CA  
748  C C   . ILE A 106 ? 0.4841 0.6988 0.6566 -0.0853 0.0007  0.0981  105 ILE A C   
749  O O   . ILE A 106 ? 0.5199 0.7315 0.7000 -0.0859 -0.0058 0.0898  105 ILE A O   
750  C CB  . ILE A 106 ? 0.4669 0.6471 0.6112 -0.0801 -0.0016 0.1019  105 ILE A CB  
751  C CG1 . ILE A 106 ? 0.5096 0.6670 0.6483 -0.0844 -0.0047 0.1079  105 ILE A CG1 
752  C CG2 . ILE A 106 ? 0.4290 0.6026 0.5692 -0.0725 -0.0077 0.0883  105 ILE A CG2 
753  C CD1 . ILE A 106 ? 0.5035 0.6508 0.6229 -0.0752 -0.0050 0.1067  105 ILE A CD1 
754  N N   . SER A 107 ? 0.4994 0.7355 0.6694 -0.0797 0.0086  0.1004  106 SER A N   
755  C CA  . SER A 107 ? 0.5370 0.7936 0.7158 -0.0747 0.0099  0.0936  106 SER A CA  
756  C C   . SER A 107 ? 0.5377 0.8061 0.7389 -0.0848 0.0083  0.0957  106 SER A C   
757  O O   . SER A 107 ? 0.4885 0.7626 0.6982 -0.0825 0.0035  0.0875  106 SER A O   
758  C CB  . SER A 107 ? 0.4899 0.7682 0.6627 -0.0673 0.0194  0.0963  106 SER A CB  
759  O OG  . SER A 107 ? 0.4749 0.7747 0.6586 -0.0627 0.0212  0.0906  106 SER A OG  
760  N N   . GLN A 108 ? 0.4954 0.7672 0.7070 -0.0962 0.0119  0.1070  107 GLN A N   
761  C CA  . GLN A 108 ? 0.5426 0.8255 0.7776 -0.1071 0.0099  0.1091  107 GLN A CA  
762  C C   . GLN A 108 ? 0.5564 0.8205 0.7960 -0.1108 -0.0016 0.1003  107 GLN A C   
763  O O   . GLN A 108 ? 0.5449 0.8200 0.7990 -0.1128 -0.0062 0.0943  107 GLN A O   
764  C CB  . GLN A 108 ? 0.5153 0.8021 0.7606 -0.1193 0.0159  0.1237  107 GLN A CB  
765  C CG  . GLN A 108 ? 0.5496 0.8484 0.8216 -0.1321 0.0139  0.1262  107 GLN A CG  
766  C CD  . GLN A 108 ? 0.5631 0.8948 0.8491 -0.1293 0.0188  0.1244  107 GLN A CD  
767  O OE1 . GLN A 108 ? 0.5416 0.8919 0.8215 -0.1224 0.0284  0.1284  107 GLN A OE1 
768  N NE2 . GLN A 108 ? 0.4941 0.8340 0.7990 -0.1342 0.0121  0.1179  107 GLN A NE2 
769  N N   . GLY A 109 ? 0.5026 0.7395 0.7299 -0.1111 -0.0066 0.0991  108 GLY A N   
770  C CA  . GLY A 109 ? 0.5079 0.7269 0.7377 -0.1139 -0.0171 0.0904  108 GLY A CA  
771  C C   . GLY A 109 ? 0.5085 0.7271 0.7305 -0.1032 -0.0222 0.0781  108 GLY A C   
772  O O   . GLY A 109 ? 0.5292 0.7428 0.7572 -0.1053 -0.0304 0.0706  108 GLY A O   
773  N N   . LEU A 110 ? 0.5180 0.7418 0.7268 -0.0919 -0.0179 0.0760  109 LEU A N   
774  C CA  . LEU A 110 ? 0.4523 0.6739 0.6531 -0.0814 -0.0221 0.0656  109 LEU A CA  
775  C C   . LEU A 110 ? 0.5391 0.7848 0.7520 -0.0779 -0.0213 0.0623  109 LEU A C   
776  O O   . LEU A 110 ? 0.4677 0.7129 0.6834 -0.0749 -0.0280 0.0548  109 LEU A O   
777  C CB  . LEU A 110 ? 0.4176 0.6315 0.5995 -0.0710 -0.0184 0.0643  109 LEU A CB  
778  C CG  . LEU A 110 ? 0.4431 0.6314 0.6107 -0.0703 -0.0217 0.0636  109 LEU A CG  
779  C CD1 . LEU A 110 ? 0.4477 0.6335 0.5994 -0.0605 -0.0177 0.0625  109 LEU A CD1 
780  C CD2 . LEU A 110 ? 0.4815 0.6548 0.6474 -0.0692 -0.0302 0.0551  109 LEU A CD2 
781  N N   . PHE A 111 ? 0.4550 0.7227 0.6748 -0.0776 -0.0132 0.0680  110 PHE A N   
782  C CA  . PHE A 111 ? 0.5004 0.7923 0.7305 -0.0719 -0.0112 0.0647  110 PHE A CA  
783  C C   . PHE A 111 ? 0.4186 0.7340 0.6711 -0.0812 -0.0085 0.0704  110 PHE A C   
784  O O   . PHE A 111 ? 0.4296 0.7655 0.6941 -0.0774 -0.0088 0.0669  110 PHE A O   
785  C CB  . PHE A 111 ? 0.4845 0.7860 0.7040 -0.0606 -0.0034 0.0643  110 PHE A CB  
786  C CG  . PHE A 111 ? 0.4728 0.7534 0.6720 -0.0516 -0.0055 0.0586  110 PHE A CG  
787  C CD1 . PHE A 111 ? 0.4153 0.6911 0.6103 -0.0422 -0.0103 0.0498  110 PHE A CD1 
788  C CD2 . PHE A 111 ? 0.4679 0.7344 0.6529 -0.0524 -0.0027 0.0627  110 PHE A CD2 
789  C CE1 . PHE A 111 ? 0.5037 0.7610 0.6822 -0.0347 -0.0119 0.0450  110 PHE A CE1 
790  C CE2 . PHE A 111 ? 0.4929 0.7417 0.6611 -0.0445 -0.0050 0.0572  110 PHE A CE2 
791  C CZ  . PHE A 111 ? 0.4556 0.6998 0.6212 -0.0360 -0.0094 0.0482  110 PHE A CZ  
792  N N   . GLY A 112 ? 0.4584 0.7719 0.7180 -0.0931 -0.0059 0.0793  111 GLY A N   
793  C CA  . GLY A 112 ? 0.4791 0.8146 0.7618 -0.1034 -0.0029 0.0856  111 GLY A CA  
794  C C   . GLY A 112 ? 0.5008 0.8584 0.7869 -0.1033 0.0094  0.0952  111 GLY A C   
795  O O   . GLY A 112 ? 0.5510 0.9278 0.8572 -0.1130 0.0133  0.1023  111 GLY A O   
796  N N   . ASN A 113 ? 0.5368 0.8933 0.8043 -0.0927 0.0156  0.0953  112 ASN A N   
797  C CA  . ASN A 113 ? 0.4993 0.8758 0.7661 -0.0915 0.0277  0.1043  112 ASN A CA  
798  C C   . ASN A 113 ? 0.4870 0.8470 0.7284 -0.0842 0.0309  0.1056  112 ASN A C   
799  O O   . ASN A 113 ? 0.4915 0.8259 0.7188 -0.0810 0.0239  0.0999  112 ASN A O   
800  C CB  . ASN A 113 ? 0.4187 0.8254 0.6947 -0.0828 0.0329  0.1002  112 ASN A CB  
801  C CG  . ASN A 113 ? 0.4812 0.8814 0.7442 -0.0678 0.0285  0.0875  112 ASN A CG  
802  O OD1 . ASN A 113 ? 0.4864 0.8740 0.7288 -0.0592 0.0303  0.0848  112 ASN A OD1 
803  N ND2 . ASN A 113 ? 0.4867 0.8951 0.7620 -0.0648 0.0225  0.0800  112 ASN A ND2 
804  N N   . THR A 114 ? 0.4728 0.8491 0.7087 -0.0814 0.0416  0.1131  113 THR A N   
805  C CA  . THR A 114 ? 0.4587 0.8228 0.6713 -0.0754 0.0450  0.1157  113 THR A CA  
806  C C   . THR A 114 ? 0.4484 0.8200 0.6462 -0.0596 0.0477  0.1060  113 THR A C   
807  O O   . THR A 114 ? 0.4627 0.8313 0.6420 -0.0535 0.0519  0.1079  113 THR A O   
808  C CB  . THR A 114 ? 0.4629 0.8382 0.6762 -0.0827 0.0549  0.1314  113 THR A CB  
809  O OG1 . THR A 114 ? 0.5821 0.9909 0.8076 -0.0814 0.0645  0.1348  113 THR A OG1 
810  C CG2 . THR A 114 ? 0.4487 0.8112 0.6759 -0.0986 0.0516  0.1411  113 THR A CG2 
811  N N   . ASP A 115 ? 0.4260 0.8068 0.6315 -0.0525 0.0447  0.0955  114 ASP A N   
812  C CA  . ASP A 115 ? 0.3646 0.7543 0.5595 -0.0375 0.0475  0.0860  114 ASP A CA  
813  C C   . ASP A 115 ? 0.5078 0.8713 0.6837 -0.0293 0.0406  0.0766  114 ASP A C   
814  O O   . ASP A 115 ? 0.5501 0.9174 0.7173 -0.0170 0.0417  0.0676  114 ASP A O   
815  C CB  . ASP A 115 ? 0.4293 0.8379 0.6409 -0.0325 0.0467  0.0788  114 ASP A CB  
816  C CG  . ASP A 115 ? 0.4680 0.9073 0.6998 -0.0390 0.0545  0.0871  114 ASP A CG  
817  O OD1 . ASP A 115 ? 0.4796 0.9280 0.7105 -0.0455 0.0626  0.0984  114 ASP A OD1 
818  O OD2 . ASP A 115 ? 0.5144 0.9695 0.7637 -0.0374 0.0526  0.0827  114 ASP A OD2 
819  N N   . TYR A 116 ? 0.5251 0.8628 0.6952 -0.0357 0.0336  0.0782  115 TYR A N   
820  C CA  . TYR A 116 ? 0.5280 0.8415 0.6833 -0.0291 0.0266  0.0694  115 TYR A CA  
821  C C   . TYR A 116 ? 0.4868 0.7838 0.6253 -0.0308 0.0268  0.0745  115 TYR A C   
822  O O   . TYR A 116 ? 0.5031 0.7770 0.6326 -0.0298 0.0200  0.0701  115 TYR A O   
823  C CB  . TYR A 116 ? 0.4922 0.7897 0.6555 -0.0330 0.0170  0.0647  115 TYR A CB  
824  C CG  . TYR A 116 ? 0.4236 0.7360 0.6017 -0.0296 0.0153  0.0590  115 TYR A CG  
825  C CD1 . TYR A 116 ? 0.4952 0.8265 0.6924 -0.0372 0.0171  0.0641  115 TYR A CD1 
826  C CD2 . TYR A 116 ? 0.4332 0.7410 0.6072 -0.0187 0.0117  0.0487  115 TYR A CD2 
827  C CE1 . TYR A 116 ? 0.3840 0.7301 0.5951 -0.0334 0.0150  0.0589  115 TYR A CE1 
828  C CE2 . TYR A 116 ? 0.3614 0.6824 0.5486 -0.0147 0.0098  0.0442  115 TYR A CE2 
829  C CZ  . TYR A 116 ? 0.4184 0.7590 0.6238 -0.0217 0.0113  0.0492  115 TYR A CZ  
830  O OH  . TYR A 116 ? 0.4126 0.7674 0.6315 -0.0171 0.0087  0.0446  115 TYR A OH  
831  N N   . GLN A 117 ? 0.4685 0.7782 0.6027 -0.0330 0.0347  0.0840  116 GLN A N   
832  C CA  . GLN A 117 ? 0.5071 0.8029 0.6254 -0.0343 0.0350  0.0903  116 GLN A CA  
833  C C   . GLN A 117 ? 0.5061 0.7914 0.6060 -0.0228 0.0320  0.0803  116 GLN A C   
834  O O   . GLN A 117 ? 0.4956 0.7604 0.5849 -0.0233 0.0269  0.0803  116 GLN A O   
835  C CB  . GLN A 117 ? 0.5624 0.8771 0.6789 -0.0375 0.0450  0.1030  116 GLN A CB  
836  C CG  . GLN A 117 ? 0.5363 0.8509 0.6666 -0.0517 0.0467  0.1168  116 GLN A CG  
837  C CD  . GLN A 117 ? 0.6633 1.0036 0.7969 -0.0545 0.0583  0.1292  116 GLN A CD  
838  O OE1 . GLN A 117 ? 0.5445 0.9025 0.6971 -0.0614 0.0625  0.1340  116 GLN A OE1 
839  N NE2 . GLN A 117 ? 0.5469 0.8904 0.6619 -0.0492 0.0635  0.1347  116 GLN A NE2 
840  N N   . GLY A 118 ? 0.5024 0.8020 0.5994 -0.0123 0.0350  0.0714  117 GLY A N   
841  C CA  . GLY A 118 ? 0.4683 0.7582 0.5497 -0.0017 0.0317  0.0608  117 GLY A CA  
842  C C   . GLY A 118 ? 0.4736 0.7394 0.5559 -0.0014 0.0222  0.0526  117 GLY A C   
843  O O   . GLY A 118 ? 0.5248 0.7745 0.5949 0.0016  0.0178  0.0489  117 GLY A O   
844  N N   . LEU A 119 ? 0.4680 0.7322 0.5648 -0.0043 0.0189  0.0500  118 LEU A N   
845  C CA  . LEU A 119 ? 0.4732 0.7158 0.5709 -0.0044 0.0104  0.0435  118 LEU A CA  
846  C C   . LEU A 119 ? 0.5034 0.7266 0.5970 -0.0124 0.0061  0.0495  118 LEU A C   
847  O O   . LEU A 119 ? 0.4854 0.6901 0.5720 -0.0102 0.0005  0.0445  118 LEU A O   
848  C CB  . LEU A 119 ? 0.4206 0.6680 0.5340 -0.0060 0.0080  0.0410  118 LEU A CB  
849  C CG  . LEU A 119 ? 0.4844 0.7114 0.5999 -0.0078 -0.0002 0.0368  118 LEU A CG  
850  C CD1 . LEU A 119 ? 0.3539 0.5679 0.4598 0.0013  -0.0034 0.0274  118 LEU A CD1 
851  C CD2 . LEU A 119 ? 0.4371 0.6723 0.5677 -0.0097 -0.0024 0.0357  118 LEU A CD2 
852  N N   . VAL A 120 ? 0.5104 0.7377 0.6095 -0.0217 0.0087  0.0603  119 VAL A N   
853  C CA  . VAL A 120 ? 0.4830 0.6913 0.5789 -0.0290 0.0048  0.0663  119 VAL A CA  
854  C C   . VAL A 120 ? 0.4910 0.6914 0.5701 -0.0244 0.0049  0.0672  119 VAL A C   
855  O O   . VAL A 120 ? 0.5321 0.7132 0.6053 -0.0246 -0.0007 0.0654  119 VAL A O   
856  C CB  . VAL A 120 ? 0.4680 0.6826 0.5749 -0.0401 0.0078  0.0779  119 VAL A CB  
857  C CG1 . VAL A 120 ? 0.4706 0.6654 0.5731 -0.0465 0.0044  0.0848  119 VAL A CG1 
858  C CG2 . VAL A 120 ? 0.5271 0.7467 0.6513 -0.0453 0.0052  0.0755  119 VAL A CG2 
859  N N   . ARG A 121 ? 0.5119 0.7282 0.5829 -0.0196 0.0113  0.0698  120 ARG A N   
860  C CA  . ARG A 121 ? 0.5516 0.7626 0.6057 -0.0143 0.0109  0.0701  120 ARG A CA  
861  C C   . ARG A 121 ? 0.5166 0.7162 0.5639 -0.0060 0.0051  0.0570  120 ARG A C   
862  O O   . ARG A 121 ? 0.4654 0.6517 0.5028 -0.0043 0.0009  0.0561  120 ARG A O   
863  C CB  . ARG A 121 ? 0.5202 0.7531 0.5662 -0.0100 0.0191  0.0745  120 ARG A CB  
864  C CG  . ARG A 121 ? 0.5485 0.7906 0.5984 -0.0185 0.0253  0.0903  120 ARG A CG  
865  C CD  . ARG A 121 ? 0.5388 0.8012 0.5764 -0.0132 0.0334  0.0955  120 ARG A CD  
866  N NE  . ARG A 121 ? 0.6566 0.9401 0.6970 -0.0060 0.0384  0.0873  120 ARG A NE  
867  C CZ  . ARG A 121 ? 0.7002 1.0047 0.7520 -0.0092 0.0460  0.0929  120 ARG A CZ  
868  N NH1 . ARG A 121 ? 0.5756 0.8834 0.6378 -0.0203 0.0497  0.1070  120 ARG A NH1 
869  N NH2 . ARG A 121 ? 0.7747 1.0976 0.8289 -0.0011 0.0500  0.0840  120 ARG A NH2 
870  N N   . LEU A 122 ? 0.4620 0.6665 0.5155 -0.0011 0.0045  0.0472  121 LEU A N   
871  C CA  . LEU A 122 ? 0.5713 0.7632 0.6211 0.0055  -0.0011 0.0355  121 LEU A CA  
872  C C   . LEU A 122 ? 0.5330 0.7038 0.5867 0.0004  -0.0077 0.0354  121 LEU A C   
873  O O   . LEU A 122 ? 0.5378 0.6952 0.5849 0.0032  -0.0123 0.0308  121 LEU A O   
874  C CB  . LEU A 122 ? 0.5255 0.7262 0.5824 0.0118  -0.0001 0.0263  121 LEU A CB  
875  C CG  . LEU A 122 ? 0.6089 0.8268 0.6591 0.0207  0.0049  0.0209  121 LEU A CG  
876  C CD1 . LEU A 122 ? 0.6198 0.8364 0.6746 0.0288  0.0028  0.0086  121 LEU A CD1 
877  C CD2 . LEU A 122 ? 0.5716 0.7879 0.6057 0.0242  0.0046  0.0206  121 LEU A CD2 
878  N N   . VAL A 123 ? 0.5031 0.6718 0.5680 -0.0069 -0.0084 0.0401  122 VAL A N   
879  C CA  . VAL A 123 ? 0.5049 0.6549 0.5730 -0.0114 -0.0143 0.0396  122 VAL A CA  
880  C C   . VAL A 123 ? 0.5031 0.6406 0.5629 -0.0141 -0.0164 0.0449  122 VAL A C   
881  O O   . VAL A 123 ? 0.4565 0.5781 0.5145 -0.0139 -0.0214 0.0416  122 VAL A O   
882  C CB  . VAL A 123 ? 0.5157 0.6679 0.5968 -0.0188 -0.0147 0.0433  122 VAL A CB  
883  C CG1 . VAL A 123 ? 0.6103 0.7443 0.6930 -0.0250 -0.0200 0.0453  122 VAL A CG1 
884  C CG2 . VAL A 123 ? 0.4586 0.6171 0.5473 -0.0147 -0.0155 0.0362  122 VAL A CG2 
885  N N   . ALA A 124 ? 0.5209 0.6663 0.5756 -0.0160 -0.0123 0.0535  123 ALA A N   
886  C CA  . ALA A 124 ? 0.5219 0.6563 0.5682 -0.0174 -0.0144 0.0593  123 ALA A CA  
887  C C   . ALA A 124 ? 0.5371 0.6638 0.5734 -0.0099 -0.0184 0.0515  123 ALA A C   
888  O O   . ALA A 124 ? 0.4322 0.5450 0.4648 -0.0106 -0.0226 0.0530  123 ALA A O   
889  C CB  . ALA A 124 ? 0.5070 0.6535 0.5479 -0.0191 -0.0086 0.0703  123 ALA A CB  
890  N N   . LEU A 125 ? 0.4861 0.6217 0.5188 -0.0026 -0.0174 0.0428  124 LEU A N   
891  C CA  . LEU A 125 ? 0.5012 0.6297 0.5270 0.0039  -0.0219 0.0341  124 LEU A CA  
892  C C   . LEU A 125 ? 0.5318 0.6486 0.5655 0.0043  -0.0261 0.0257  124 LEU A C   
893  O O   . LEU A 125 ? 0.5517 0.6574 0.5830 0.0064  -0.0306 0.0212  124 LEU A O   
894  C CB  . LEU A 125 ? 0.5114 0.6543 0.5294 0.0117  -0.0193 0.0279  124 LEU A CB  
895  C CG  . LEU A 125 ? 0.6675 0.8240 0.6749 0.0126  -0.0146 0.0361  124 LEU A CG  
896  C CD1 . LEU A 125 ? 0.5913 0.7613 0.5892 0.0216  -0.0130 0.0277  124 LEU A CD1 
897  C CD2 . LEU A 125 ? 0.6082 0.7551 0.6082 0.0102  -0.0177 0.0441  124 LEU A CD2 
898  N N   . VAL A 126 ? 0.4666 0.5863 0.5098 0.0026  -0.0246 0.0242  125 VAL A N   
899  C CA  . VAL A 126 ? 0.4448 0.5543 0.4947 0.0033  -0.0281 0.0175  125 VAL A CA  
900  C C   . VAL A 126 ? 0.5156 0.6099 0.5676 -0.0017 -0.0318 0.0206  125 VAL A C   
901  O O   . VAL A 126 ? 0.4385 0.5220 0.4916 0.0000  -0.0353 0.0155  125 VAL A O   
902  C CB  . VAL A 126 ? 0.4656 0.5832 0.5245 0.0032  -0.0258 0.0162  125 VAL A CB  
903  C CG1 . VAL A 126 ? 0.5010 0.6082 0.5657 0.0044  -0.0293 0.0107  125 VAL A CG1 
904  C CG2 . VAL A 126 ? 0.5252 0.6582 0.5825 0.0093  -0.0219 0.0123  125 VAL A CG2 
905  N N   . GLN A 127 ? 0.4462 0.5393 0.4993 -0.0079 -0.0311 0.0288  126 GLN A N   
906  C CA  . GLN A 127 ? 0.4463 0.5246 0.5015 -0.0122 -0.0348 0.0308  126 GLN A CA  
907  C C   . GLN A 127 ? 0.4716 0.5402 0.5203 -0.0093 -0.0379 0.0297  126 GLN A C   
908  O O   . GLN A 127 ? 0.4421 0.4984 0.4927 -0.0105 -0.0412 0.0283  126 GLN A O   
909  C CB  . GLN A 127 ? 0.4864 0.5646 0.5454 -0.0195 -0.0337 0.0395  126 GLN A CB  
910  C CG  . GLN A 127 ? 0.4817 0.5666 0.5351 -0.0205 -0.0305 0.0477  126 GLN A CG  
911  C CD  . GLN A 127 ? 0.5273 0.5999 0.5747 -0.0206 -0.0334 0.0517  126 GLN A CD  
912  O OE1 . GLN A 127 ? 0.5293 0.5879 0.5790 -0.0216 -0.0375 0.0493  126 GLN A OE1 
913  N NE2 . GLN A 127 ? 0.5463 0.6246 0.5856 -0.0189 -0.0314 0.0579  126 GLN A NE2 
914  N N   . MET A 128 ? 0.4430 0.5178 0.4837 -0.0051 -0.0371 0.0298  127 MET A N   
915  C CA  . MET A 128 ? 0.4528 0.5204 0.4882 -0.0015 -0.0409 0.0272  127 MET A CA  
916  C C   . MET A 128 ? 0.4540 0.5162 0.4936 0.0017  -0.0435 0.0178  127 MET A C   
917  O O   . MET A 128 ? 0.4860 0.5382 0.5270 0.0020  -0.0469 0.0160  127 MET A O   
918  C CB  . MET A 128 ? 0.5211 0.5987 0.5466 0.0030  -0.0400 0.0282  127 MET A CB  
919  C CG  . MET A 128 ? 0.5837 0.6614 0.6030 0.0007  -0.0393 0.0389  127 MET A CG  
920  S SD  . MET A 128 ? 0.8366 0.9298 0.8423 0.0064  -0.0372 0.0409  127 MET A SD  
921  C CE  . MET A 128 ? 0.6885 0.7787 0.6892 0.0022  -0.0359 0.0565  127 MET A CE  
922  N N   . GLY A 129 ? 0.4470 0.5158 0.4893 0.0044  -0.0418 0.0120  128 GLY A N   
923  C CA  . GLY A 129 ? 0.4579 0.5207 0.5056 0.0067  -0.0438 0.0044  128 GLY A CA  
924  C C   . GLY A 129 ? 0.4273 0.4808 0.4813 0.0030  -0.0445 0.0058  128 GLY A C   
925  O O   . GLY A 129 ? 0.4393 0.4849 0.4965 0.0039  -0.0466 0.0022  128 GLY A O   
926  N N   . ILE A 130 ? 0.4588 0.5141 0.5150 -0.0012 -0.0428 0.0108  129 ILE A N   
927  C CA  . ILE A 130 ? 0.4440 0.4913 0.5048 -0.0045 -0.0440 0.0116  129 ILE A CA  
928  C C   . ILE A 130 ? 0.4013 0.4379 0.4604 -0.0058 -0.0466 0.0130  129 ILE A C   
929  O O   . ILE A 130 ? 0.4386 0.4677 0.5001 -0.0051 -0.0481 0.0100  129 ILE A O   
930  C CB  . ILE A 130 ? 0.3981 0.4506 0.4621 -0.0091 -0.0425 0.0161  129 ILE A CB  
931  C CG1 . ILE A 130 ? 0.3815 0.4455 0.4487 -0.0068 -0.0400 0.0141  129 ILE A CG1 
932  C CG2 . ILE A 130 ? 0.3491 0.3932 0.4165 -0.0124 -0.0447 0.0161  129 ILE A CG2 
933  C CD1 . ILE A 130 ? 0.3889 0.4604 0.4612 -0.0113 -0.0388 0.0181  129 ILE A CD1 
934  N N   . ALA A 131 ? 0.3877 0.4238 0.4427 -0.0073 -0.0470 0.0181  130 ALA A N   
935  C CA  . ALA A 131 ? 0.4315 0.4574 0.4854 -0.0078 -0.0497 0.0199  130 ALA A CA  
936  C C   . ALA A 131 ? 0.3820 0.4052 0.4354 -0.0032 -0.0519 0.0148  130 ALA A C   
937  O O   . ALA A 131 ? 0.3946 0.4098 0.4507 -0.0028 -0.0536 0.0127  130 ALA A O   
938  C CB  . ALA A 131 ? 0.4364 0.4625 0.4860 -0.0097 -0.0497 0.0274  130 ALA A CB  
939  N N   . TRP A 132 ? 0.3648 0.3952 0.4151 0.0004  -0.0518 0.0121  131 TRP A N   
940  C CA  . TRP A 132 ? 0.4145 0.4432 0.4657 0.0042  -0.0545 0.0069  131 TRP A CA  
941  C C   . TRP A 132 ? 0.4179 0.4435 0.4762 0.0047  -0.0541 0.0012  131 TRP A C   
942  O O   . TRP A 132 ? 0.4355 0.4564 0.4978 0.0058  -0.0559 -0.0014 131 TRP A O   
943  C CB  . TRP A 132 ? 0.4146 0.4522 0.4605 0.0080  -0.0553 0.0043  131 TRP A CB  
944  C CG  . TRP A 132 ? 0.5260 0.5624 0.5717 0.0113  -0.0595 0.0009  131 TRP A CG  
945  C CD1 . TRP A 132 ? 0.5834 0.6217 0.6334 0.0141  -0.0616 -0.0071 131 TRP A CD1 
946  C CD2 . TRP A 132 ? 0.5484 0.5814 0.5909 0.0122  -0.0625 0.0051  131 TRP A CD2 
947  N NE1 . TRP A 132 ? 0.5993 0.6371 0.6492 0.0164  -0.0659 -0.0084 131 TRP A NE1 
948  C CE2 . TRP A 132 ? 0.6042 0.6389 0.6492 0.0158  -0.0666 -0.0008 131 TRP A CE2 
949  C CE3 . TRP A 132 ? 0.5301 0.5585 0.5689 0.0104  -0.0625 0.0135  131 TRP A CE3 
950  C CZ2 . TRP A 132 ? 0.5500 0.5832 0.5934 0.0183  -0.0707 0.0013  131 TRP A CZ2 
951  C CZ3 . TRP A 132 ? 0.5296 0.5548 0.5664 0.0131  -0.0664 0.0160  131 TRP A CZ3 
952  C CH2 . TRP A 132 ? 0.4811 0.5093 0.5200 0.0172  -0.0705 0.0100  131 TRP A CH2 
953  N N   . GLY A 133 ? 0.3743 0.4032 0.4350 0.0041  -0.0516 -0.0002 132 GLY A N   
954  C CA  . GLY A 133 ? 0.3547 0.3800 0.4217 0.0045  -0.0508 -0.0038 132 GLY A CA  
955  C C   . GLY A 133 ? 0.4172 0.4352 0.4864 0.0024  -0.0508 -0.0018 132 GLY A C   
956  O O   . GLY A 133 ? 0.4325 0.4466 0.5060 0.0033  -0.0508 -0.0042 132 GLY A O   
957  N N   . ASN A 134 ? 0.4087 0.4252 0.4752 -0.0005 -0.0505 0.0023  133 ASN A N   
958  C CA  . ASN A 134 ? 0.3833 0.3930 0.4510 -0.0020 -0.0509 0.0029  133 ASN A CA  
959  C C   . ASN A 134 ? 0.4134 0.4173 0.4814 -0.0006 -0.0527 0.0023  133 ASN A C   
960  O O   . ASN A 134 ? 0.4176 0.4171 0.4879 0.0000  -0.0524 0.0007  133 ASN A O   
961  C CB  . ASN A 134 ? 0.3967 0.4055 0.4624 -0.0058 -0.0511 0.0064  133 ASN A CB  
962  C CG  . ASN A 134 ? 0.4910 0.5060 0.5581 -0.0070 -0.0496 0.0065  133 ASN A CG  
963  O OD1 . ASN A 134 ? 0.5429 0.5612 0.6119 -0.0044 -0.0483 0.0042  133 ASN A OD1 
964  N ND2 . ASN A 134 ? 0.4584 0.4749 0.5256 -0.0108 -0.0500 0.0092  133 ASN A ND2 
965  N N   . LEU A 135 ? 0.3949 0.4001 0.4606 0.0005  -0.0545 0.0036  134 LEU A N   
966  C CA  . LEU A 135 ? 0.4608 0.4618 0.5278 0.0028  -0.0568 0.0029  134 LEU A CA  
967  C C   . LEU A 135 ? 0.3654 0.3683 0.4384 0.0052  -0.0566 -0.0019 134 LEU A C   
968  O O   . LEU A 135 ? 0.3774 0.3768 0.4544 0.0064  -0.0567 -0.0033 134 LEU A O   
969  C CB  . LEU A 135 ? 0.3715 0.3746 0.4339 0.0040  -0.0592 0.0061  134 LEU A CB  
970  C CG  . LEU A 135 ? 0.3674 0.3679 0.4313 0.0074  -0.0624 0.0054  134 LEU A CG  
971  C CD1 . LEU A 135 ? 0.3902 0.3815 0.4557 0.0070  -0.0630 0.0073  134 LEU A CD1 
972  C CD2 . LEU A 135 ? 0.3686 0.3733 0.4267 0.0095  -0.0651 0.0087  134 LEU A CD2 
973  N N   . LEU A 136 ? 0.3732 0.3817 0.4477 0.0060  -0.0563 -0.0047 135 LEU A N   
974  C CA  . LEU A 136 ? 0.3815 0.3913 0.4637 0.0074  -0.0563 -0.0092 135 LEU A CA  
975  C C   . LEU A 136 ? 0.3873 0.3940 0.4742 0.0063  -0.0530 -0.0092 135 LEU A C   
976  O O   . LEU A 136 ? 0.4382 0.4443 0.5316 0.0071  -0.0524 -0.0109 135 LEU A O   
977  C CB  . LEU A 136 ? 0.3854 0.4004 0.4686 0.0083  -0.0568 -0.0129 135 LEU A CB  
978  C CG  . LEU A 136 ? 0.4489 0.4691 0.5259 0.0102  -0.0598 -0.0135 135 LEU A CG  
979  C CD1 . LEU A 136 ? 0.3847 0.4099 0.4621 0.0116  -0.0600 -0.0185 135 LEU A CD1 
980  C CD2 . LEU A 136 ? 0.4792 0.5002 0.5576 0.0122  -0.0638 -0.0148 135 LEU A CD2 
981  N N   . LEU A 137 ? 0.3865 0.3922 0.4701 0.0048  -0.0508 -0.0071 136 LEU A N   
982  C CA  . LEU A 137 ? 0.4017 0.4051 0.4874 0.0043  -0.0479 -0.0064 136 LEU A CA  
983  C C   . LEU A 137 ? 0.4166 0.4163 0.5014 0.0048  -0.0478 -0.0059 136 LEU A C   
984  O O   . LEU A 137 ? 0.4144 0.4138 0.5032 0.0057  -0.0455 -0.0066 136 LEU A O   
985  C CB  . LEU A 137 ? 0.3739 0.3781 0.4554 0.0031  -0.0466 -0.0043 136 LEU A CB  
986  C CG  . LEU A 137 ? 0.4026 0.4106 0.4860 0.0037  -0.0460 -0.0050 136 LEU A CG  
987  C CD1 . LEU A 137 ? 0.3691 0.3797 0.4485 0.0027  -0.0456 -0.0028 136 LEU A CD1 
988  C CD2 . LEU A 137 ? 0.3419 0.3487 0.4321 0.0048  -0.0440 -0.0060 136 LEU A CD2 
989  N N   . ALA A 138 ? 0.4068 0.4035 0.4867 0.0042  -0.0501 -0.0047 137 ALA A N   
990  C CA  . ALA A 138 ? 0.3595 0.3514 0.4388 0.0053  -0.0505 -0.0051 137 ALA A CA  
991  C C   . ALA A 138 ? 0.4034 0.3963 0.4887 0.0081  -0.0511 -0.0070 137 ALA A C   
992  O O   . ALA A 138 ? 0.3724 0.3639 0.4600 0.0100  -0.0496 -0.0085 137 ALA A O   
993  C CB  . ALA A 138 ? 0.3734 0.3606 0.4478 0.0039  -0.0533 -0.0029 137 ALA A CB  
994  N N   . LEU A 139 ? 0.3720 0.3686 0.4602 0.0088  -0.0532 -0.0076 138 LEU A N   
995  C CA  . LEU A 139 ? 0.3886 0.3883 0.4844 0.0113  -0.0542 -0.0100 138 LEU A CA  
996  C C   . LEU A 139 ? 0.4011 0.4039 0.5046 0.0110  -0.0504 -0.0116 138 LEU A C   
997  O O   . LEU A 139 ? 0.3955 0.3998 0.5049 0.0128  -0.0489 -0.0127 138 LEU A O   
998  C CB  . LEU A 139 ? 0.4133 0.4175 0.5103 0.0119  -0.0579 -0.0111 138 LEU A CB  
999  C CG  . LEU A 139 ? 0.4166 0.4197 0.5068 0.0132  -0.0619 -0.0087 138 LEU A CG  
1000 C CD1 . LEU A 139 ? 0.4532 0.4630 0.5440 0.0143  -0.0651 -0.0111 138 LEU A CD1 
1001 C CD2 . LEU A 139 ? 0.3871 0.3868 0.4791 0.0162  -0.0639 -0.0079 138 LEU A CD2 
1002 N N   . MET A 140 ? 0.4060 0.4103 0.5105 0.0089  -0.0484 -0.0114 139 MET A N   
1003 C CA  . MET A 140 ? 0.4139 0.4204 0.5260 0.0083  -0.0443 -0.0114 139 MET A CA  
1004 C C   . MET A 140 ? 0.3324 0.3375 0.4416 0.0092  -0.0404 -0.0097 139 MET A C   
1005 O O   . MET A 140 ? 0.3924 0.4006 0.5084 0.0101  -0.0372 -0.0097 139 MET A O   
1006 C CB  . MET A 140 ? 0.3686 0.3749 0.4810 0.0064  -0.0430 -0.0106 139 MET A CB  
1007 C CG  . MET A 140 ? 0.3725 0.3804 0.4866 0.0062  -0.0466 -0.0135 139 MET A CG  
1008 S SD  . MET A 140 ? 0.5096 0.5163 0.6257 0.0050  -0.0447 -0.0132 139 MET A SD  
1009 C CE  . MET A 140 ? 0.4233 0.4325 0.5385 0.0059  -0.0495 -0.0183 139 MET A CE  
1010 N N   . LYS A 141 ? 0.3690 0.3702 0.4684 0.0091  -0.0408 -0.0085 140 LYS A N   
1011 C CA  . LYS A 141 ? 0.3322 0.3322 0.4273 0.0105  -0.0380 -0.0082 140 LYS A CA  
1012 C C   . LYS A 141 ? 0.3607 0.3605 0.4586 0.0135  -0.0382 -0.0106 140 LYS A C   
1013 O O   . LYS A 141 ? 0.3868 0.3887 0.4852 0.0156  -0.0345 -0.0113 140 LYS A O   
1014 C CB  . LYS A 141 ? 0.3536 0.3495 0.4389 0.0094  -0.0398 -0.0077 140 LYS A CB  
1015 C CG  . LYS A 141 ? 0.3701 0.3675 0.4528 0.0074  -0.0392 -0.0053 140 LYS A CG  
1016 C CD  . LYS A 141 ? 0.3636 0.3587 0.4381 0.0062  -0.0411 -0.0052 140 LYS A CD  
1017 C CE  . LYS A 141 ? 0.4108 0.4082 0.4841 0.0042  -0.0421 -0.0032 140 LYS A CE  
1018 N NZ  . LYS A 141 ? 0.4173 0.4147 0.4844 0.0030  -0.0435 -0.0031 140 LYS A NZ  
1019 N N   . GLY A 142 ? 0.3601 0.3582 0.4597 0.0143  -0.0425 -0.0118 141 GLY A N   
1020 C CA  . GLY A 142 ? 0.3441 0.3423 0.4478 0.0179  -0.0432 -0.0139 141 GLY A CA  
1021 C C   . GLY A 142 ? 0.4007 0.4068 0.5155 0.0192  -0.0398 -0.0148 141 GLY A C   
1022 O O   . GLY A 142 ? 0.4122 0.4207 0.5308 0.0228  -0.0380 -0.0167 141 GLY A O   
1023 N N   . PHE A 143 ? 0.3943 0.4049 0.5154 0.0164  -0.0388 -0.0138 142 PHE A N   
1024 C CA  . PHE A 143 ? 0.3725 0.3908 0.5062 0.0161  -0.0353 -0.0139 142 PHE A CA  
1025 C C   . PHE A 143 ? 0.3761 0.3962 0.5093 0.0148  -0.0287 -0.0109 142 PHE A C   
1026 O O   . PHE A 143 ? 0.3773 0.4037 0.5214 0.0137  -0.0247 -0.0095 142 PHE A O   
1027 C CB  . PHE A 143 ? 0.3966 0.4179 0.5388 0.0136  -0.0386 -0.0150 142 PHE A CB  
1028 C CG  . PHE A 143 ? 0.3982 0.4222 0.5449 0.0158  -0.0443 -0.0180 142 PHE A CG  
1029 C CD1 . PHE A 143 ? 0.4047 0.4365 0.5643 0.0175  -0.0440 -0.0199 142 PHE A CD1 
1030 C CD2 . PHE A 143 ? 0.3520 0.3716 0.4900 0.0165  -0.0498 -0.0183 142 PHE A CD2 
1031 C CE1 . PHE A 143 ? 0.4347 0.4698 0.5983 0.0202  -0.0500 -0.0225 142 PHE A CE1 
1032 C CE2 . PHE A 143 ? 0.3887 0.4111 0.5295 0.0192  -0.0553 -0.0202 142 PHE A CE2 
1033 C CZ  . PHE A 143 ? 0.4343 0.4644 0.5878 0.0213  -0.0558 -0.0224 142 PHE A CZ  
1034 N N   . ARG A 144 ? 0.3463 0.3616 0.4674 0.0149  -0.0276 -0.0093 143 ARG A N   
1035 C CA  . ARG A 144 ? 0.3971 0.4142 0.5152 0.0143  -0.0220 -0.0057 143 ARG A CA  
1036 C C   . ARG A 144 ? 0.3889 0.4071 0.5145 0.0108  -0.0204 -0.0023 143 ARG A C   
1037 O O   . ARG A 144 ? 0.3958 0.4173 0.5252 0.0102  -0.0148 0.0018  143 ARG A O   
1038 C CB  . ARG A 144 ? 0.3121 0.3355 0.4330 0.0173  -0.0162 -0.0055 143 ARG A CB  
1039 C CG  . ARG A 144 ? 0.3961 0.4179 0.5106 0.0217  -0.0177 -0.0100 143 ARG A CG  
1040 C CD  . ARG A 144 ? 0.3968 0.4250 0.5093 0.0255  -0.0111 -0.0100 143 ARG A CD  
1041 N NE  . ARG A 144 ? 0.4446 0.4825 0.5715 0.0261  -0.0065 -0.0089 143 ARG A NE  
1042 C CZ  . ARG A 144 ? 0.5408 0.5872 0.6695 0.0295  0.0001  -0.0087 143 ARG A CZ  
1043 N NH1 . ARG A 144 ? 0.4379 0.4841 0.5536 0.0334  0.0028  -0.0102 143 ARG A NH1 
1044 N NH2 . ARG A 144 ? 0.3450 0.4012 0.4892 0.0292  0.0041  -0.0074 143 ARG A NH2 
1045 N N   . ASP A 145 ? 0.3643 0.3794 0.4920 0.0087  -0.0252 -0.0039 144 ASP A N   
1046 C CA  . ASP A 145 ? 0.3798 0.3944 0.5151 0.0058  -0.0247 -0.0021 144 ASP A CA  
1047 C C   . ASP A 145 ? 0.3833 0.3936 0.5093 0.0056  -0.0239 0.0012  144 ASP A C   
1048 O O   . ASP A 145 ? 0.3790 0.3862 0.5008 0.0051  -0.0277 -0.0003 144 ASP A O   
1049 C CB  . ASP A 145 ? 0.3636 0.3779 0.5047 0.0047  -0.0304 -0.0066 144 ASP A CB  
1050 C CG  . ASP A 145 ? 0.3577 0.3716 0.5100 0.0018  -0.0301 -0.0067 144 ASP A CG  
1051 O OD1 . ASP A 145 ? 0.4162 0.4286 0.5715 0.0005  -0.0255 -0.0021 144 ASP A OD1 
1052 O OD2 . ASP A 145 ? 0.4416 0.4563 0.5998 0.0011  -0.0348 -0.0114 144 ASP A OD2 
1053 N N   . ALA A 146 ? 0.3675 0.3791 0.4902 0.0064  -0.0189 0.0059  145 ALA A N   
1054 C CA  . ALA A 146 ? 0.3667 0.3755 0.4806 0.0069  -0.0184 0.0094  145 ALA A CA  
1055 C C   . ALA A 146 ? 0.3437 0.3491 0.4643 0.0051  -0.0193 0.0110  145 ALA A C   
1056 O O   . ALA A 146 ? 0.3396 0.3425 0.4542 0.0057  -0.0216 0.0115  145 ALA A O   
1057 C CB  . ALA A 146 ? 0.3828 0.3947 0.4916 0.0087  -0.0128 0.0147  145 ALA A CB  
1058 N N   . ALA A 147 ? 0.3718 0.3773 0.5060 0.0029  -0.0178 0.0113  146 ALA A N   
1059 C CA  . ALA A 147 ? 0.3946 0.3955 0.5368 0.0014  -0.0187 0.0120  146 ALA A CA  
1060 C C   . ALA A 147 ? 0.3540 0.3531 0.4953 0.0015  -0.0249 0.0052  146 ALA A C   
1061 O O   . ALA A 147 ? 0.3921 0.3877 0.5312 0.0023  -0.0266 0.0050  146 ALA A O   
1062 C CB  . ALA A 147 ? 0.3592 0.3605 0.5178 -0.0017 -0.0156 0.0137  146 ALA A CB  
1063 N N   . GLY A 148 ? 0.3547 0.3568 0.4977 0.0011  -0.0281 -0.0002 147 GLY A N   
1064 C CA  . GLY A 148 ? 0.3157 0.3174 0.4558 0.0017  -0.0336 -0.0059 147 GLY A CA  
1065 C C   . GLY A 148 ? 0.3731 0.3742 0.4997 0.0035  -0.0350 -0.0050 147 GLY A C   
1066 O O   . GLY A 148 ? 0.3794 0.3796 0.5037 0.0042  -0.0373 -0.0071 147 GLY A O   
1067 N N   . ASN A 149 ? 0.3239 0.3260 0.4421 0.0042  -0.0336 -0.0024 148 ASN A N   
1068 C CA  . ASN A 149 ? 0.3571 0.3591 0.4643 0.0051  -0.0349 -0.0014 148 ASN A CA  
1069 C C   . ASN A 149 ? 0.3606 0.3615 0.4667 0.0058  -0.0337 0.0016  148 ASN A C   
1070 O O   . ASN A 149 ? 0.3725 0.3742 0.4756 0.0064  -0.0359 0.0003  148 ASN A O   
1071 C CB  . ASN A 149 ? 0.3487 0.3512 0.4488 0.0056  -0.0337 0.0001  148 ASN A CB  
1072 C CG  . ASN A 149 ? 0.4262 0.4287 0.5164 0.0057  -0.0354 0.0009  148 ASN A CG  
1073 O OD1 . ASN A 149 ? 0.4101 0.4126 0.4970 0.0050  -0.0386 -0.0010 148 ASN A OD1 
1074 N ND2 . ASN A 149 ? 0.4150 0.4182 0.5010 0.0066  -0.0334 0.0040  148 ASN A ND2 
1075 N N   . ALA A 150 ? 0.3552 0.3549 0.4644 0.0062  -0.0299 0.0060  149 ALA A N   
1076 C CA  . ALA A 150 ? 0.3805 0.3788 0.4886 0.0077  -0.0289 0.0099  149 ALA A CA  
1077 C C   . ALA A 150 ? 0.3403 0.3356 0.4561 0.0080  -0.0305 0.0075  149 ALA A C   
1078 O O   . ALA A 150 ? 0.3864 0.3820 0.4995 0.0100  -0.0319 0.0075  149 ALA A O   
1079 C CB  . ALA A 150 ? 0.3590 0.3565 0.4684 0.0082  -0.0242 0.0164  149 ALA A CB  
1080 N N   . LEU A 151 ? 0.3613 0.3543 0.4876 0.0064  -0.0305 0.0047  150 LEU A N   
1081 C CA  . LEU A 151 ? 0.4129 0.4024 0.5468 0.0070  -0.0326 0.0007  150 LEU A CA  
1082 C C   . LEU A 151 ? 0.3592 0.3523 0.4869 0.0084  -0.0366 -0.0052 150 LEU A C   
1083 O O   . LEU A 151 ? 0.3651 0.3572 0.4936 0.0108  -0.0378 -0.0074 150 LEU A O   
1084 C CB  . LEU A 151 ? 0.3221 0.3092 0.4691 0.0043  -0.0327 -0.0024 150 LEU A CB  
1085 C CG  . LEU A 151 ? 0.4455 0.4288 0.6014 0.0026  -0.0280 0.0044  150 LEU A CG  
1086 C CD1 . LEU A 151 ? 0.4073 0.3919 0.5755 -0.0011 -0.0274 0.0022  150 LEU A CD1 
1087 C CD2 . LEU A 151 ? 0.4316 0.4074 0.5942 0.0037  -0.0273 0.0068  150 LEU A CD2 
1088 N N   . SER A 152 ? 0.3735 0.3708 0.4950 0.0075  -0.0383 -0.0073 151 SER A N   
1089 C CA  . SER A 152 ? 0.3908 0.3923 0.5058 0.0087  -0.0413 -0.0113 151 SER A CA  
1090 C C   . SER A 152 ? 0.3899 0.3940 0.4981 0.0103  -0.0407 -0.0084 151 SER A C   
1091 O O   . SER A 152 ? 0.3547 0.3612 0.4624 0.0124  -0.0417 -0.0111 151 SER A O   
1092 C CB  . SER A 152 ? 0.2828 0.2873 0.3927 0.0074  -0.0430 -0.0122 151 SER A CB  
1093 O OG  . SER A 152 ? 0.3567 0.3608 0.4737 0.0066  -0.0446 -0.0160 151 SER A OG  
1094 N N   . LEU A 153 ? 0.3717 0.3762 0.4750 0.0096  -0.0391 -0.0034 152 LEU A N   
1095 C CA  . LEU A 153 ? 0.3148 0.3230 0.4127 0.0108  -0.0391 -0.0008 152 LEU A CA  
1096 C C   . LEU A 153 ? 0.3460 0.3529 0.4485 0.0139  -0.0383 0.0004  152 LEU A C   
1097 O O   . LEU A 153 ? 0.3486 0.3602 0.4495 0.0159  -0.0392 0.0000  152 LEU A O   
1098 C CB  . LEU A 153 ? 0.3648 0.3735 0.4570 0.0096  -0.0383 0.0032  152 LEU A CB  
1099 C CG  . LEU A 153 ? 0.4010 0.4102 0.4883 0.0071  -0.0396 0.0019  152 LEU A CG  
1100 C CD1 . LEU A 153 ? 0.4121 0.4201 0.4949 0.0067  -0.0385 0.0043  152 LEU A CD1 
1101 C CD2 . LEU A 153 ? 0.3658 0.3796 0.4490 0.0060  -0.0418 0.0008  152 LEU A CD2 
1102 N N   . ILE A 154 ? 0.3627 0.3635 0.4719 0.0144  -0.0365 0.0023  153 ILE A N   
1103 C CA  . ILE A 154 ? 0.3839 0.3814 0.4983 0.0176  -0.0359 0.0042  153 ILE A CA  
1104 C C   . ILE A 154 ? 0.3910 0.3888 0.5100 0.0199  -0.0378 -0.0024 153 ILE A C   
1105 O O   . ILE A 154 ? 0.4173 0.4179 0.5360 0.0235  -0.0384 -0.0027 153 ILE A O   
1106 C CB  . ILE A 154 ? 0.3538 0.3438 0.4756 0.0170  -0.0332 0.0087  153 ILE A CB  
1107 C CG1 . ILE A 154 ? 0.3308 0.3224 0.4462 0.0168  -0.0307 0.0162  153 ILE A CG1 
1108 C CG2 . ILE A 154 ? 0.3707 0.3546 0.5006 0.0203  -0.0331 0.0093  153 ILE A CG2 
1109 C CD1 . ILE A 154 ? 0.3502 0.3372 0.4708 0.0147  -0.0271 0.0205  153 ILE A CD1 
1110 N N   . VAL A 155 ? 0.3587 0.3545 0.4815 0.0183  -0.0391 -0.0082 154 VAL A N   
1111 C CA  . VAL A 155 ? 0.3680 0.3650 0.4936 0.0209  -0.0412 -0.0158 154 VAL A CA  
1112 C C   . VAL A 155 ? 0.4441 0.4508 0.5611 0.0226  -0.0419 -0.0172 154 VAL A C   
1113 O O   . VAL A 155 ? 0.4092 0.4190 0.5271 0.0266  -0.0423 -0.0206 154 VAL A O   
1114 C CB  . VAL A 155 ? 0.3388 0.3339 0.4687 0.0187  -0.0433 -0.0221 154 VAL A CB  
1115 C CG1 . VAL A 155 ? 0.3407 0.3391 0.4702 0.0219  -0.0460 -0.0310 154 VAL A CG1 
1116 C CG2 . VAL A 155 ? 0.3947 0.3806 0.5363 0.0168  -0.0424 -0.0211 154 VAL A CG2 
1117 N N   . GLY A 156 ? 0.4132 0.4250 0.5226 0.0196  -0.0419 -0.0145 155 GLY A N   
1118 C CA  . GLY A 156 ? 0.3994 0.4205 0.5020 0.0200  -0.0421 -0.0148 155 GLY A CA  
1119 C C   . GLY A 156 ? 0.4540 0.4798 0.5564 0.0224  -0.0412 -0.0114 155 GLY A C   
1120 O O   . GLY A 156 ? 0.4474 0.4812 0.5489 0.0249  -0.0410 -0.0135 155 GLY A O   
1121 N N   . SER A 157 ? 0.4292 0.4516 0.5324 0.0220  -0.0405 -0.0060 156 SER A N   
1122 C CA  . SER A 157 ? 0.3908 0.4183 0.4945 0.0248  -0.0404 -0.0027 156 SER A CA  
1123 C C   . SER A 157 ? 0.3987 0.4255 0.5089 0.0304  -0.0402 -0.0057 156 SER A C   
1124 O O   . SER A 157 ? 0.4129 0.4483 0.5237 0.0336  -0.0402 -0.0067 156 SER A O   
1125 C CB  . SER A 157 ? 0.3757 0.3994 0.4780 0.0242  -0.0400 0.0035  156 SER A CB  
1126 O OG  . SER A 157 ? 0.4540 0.4788 0.5502 0.0198  -0.0404 0.0052  156 SER A OG  
1127 N N   . LEU A 158 ? 0.4569 0.4735 0.5731 0.0318  -0.0400 -0.0075 157 LEU A N   
1128 C CA  . LEU A 158 ? 0.4275 0.4409 0.5510 0.0374  -0.0402 -0.0107 157 LEU A CA  
1129 C C   . LEU A 158 ? 0.4242 0.4443 0.5473 0.0401  -0.0408 -0.0190 157 LEU A C   
1130 O O   . LEU A 158 ? 0.4890 0.5142 0.6146 0.0455  -0.0406 -0.0212 157 LEU A O   
1131 C CB  . LEU A 158 ? 0.3855 0.3853 0.5169 0.0372  -0.0400 -0.0107 157 LEU A CB  
1132 C CG  . LEU A 158 ? 0.4424 0.4363 0.5740 0.0351  -0.0385 -0.0015 157 LEU A CG  
1133 C CD1 . LEU A 158 ? 0.4982 0.4791 0.6401 0.0355  -0.0377 -0.0001 157 LEU A CD1 
1134 C CD2 . LEU A 158 ? 0.4490 0.4487 0.5770 0.0385  -0.0385 0.0048  157 LEU A CD2 
1135 N N   . ILE A 159 ? 0.4369 0.4581 0.5563 0.0370  -0.0414 -0.0236 158 ILE A N   
1136 C CA  . ILE A 159 ? 0.4755 0.5051 0.5921 0.0399  -0.0417 -0.0309 158 ILE A CA  
1137 C C   . ILE A 159 ? 0.4569 0.5004 0.5676 0.0398  -0.0401 -0.0277 158 ILE A C   
1138 O O   . ILE A 159 ? 0.4608 0.5137 0.5707 0.0440  -0.0391 -0.0319 158 ILE A O   
1139 C CB  . ILE A 159 ? 0.4816 0.5096 0.5950 0.0370  -0.0433 -0.0362 158 ILE A CB  
1140 C CG1 . ILE A 159 ? 0.4959 0.5274 0.6020 0.0313  -0.0431 -0.0307 158 ILE A CG1 
1141 C CG2 . ILE A 159 ? 0.4718 0.4870 0.5935 0.0362  -0.0451 -0.0393 158 ILE A CG2 
1142 C CD1 . ILE A 159 ? 0.5071 0.5356 0.6114 0.0287  -0.0452 -0.0344 158 ILE A CD1 
1143 N N   . GLY A 160 ? 0.4304 0.4759 0.5376 0.0352  -0.0398 -0.0205 159 GLY A N   
1144 C CA  . GLY A 160 ? 0.4190 0.4773 0.5229 0.0342  -0.0386 -0.0172 159 GLY A CA  
1145 C C   . GLY A 160 ? 0.4487 0.5138 0.5580 0.0394  -0.0380 -0.0167 159 GLY A C   
1146 O O   . GLY A 160 ? 0.4900 0.5681 0.5994 0.0414  -0.0364 -0.0179 159 GLY A O   
1147 N N   . VAL A 161 ? 0.4437 0.5010 0.5580 0.0421  -0.0389 -0.0142 160 VAL A N   
1148 C CA  . VAL A 161 ? 0.4189 0.4818 0.5391 0.0482  -0.0389 -0.0135 160 VAL A CA  
1149 C C   . VAL A 161 ? 0.5077 0.5735 0.6319 0.0549  -0.0378 -0.0212 160 VAL A C   
1150 O O   . VAL A 161 ? 0.4766 0.5549 0.6035 0.0593  -0.0367 -0.0225 160 VAL A O   
1151 C CB  . VAL A 161 ? 0.4609 0.5130 0.5849 0.0502  -0.0402 -0.0085 160 VAL A CB  
1152 C CG1 . VAL A 161 ? 0.3821 0.4367 0.5134 0.0584  -0.0405 -0.0088 160 VAL A CG1 
1153 C CG2 . VAL A 161 ? 0.4212 0.4752 0.5404 0.0454  -0.0412 -0.0013 160 VAL A CG2 
1154 N N   . LEU A 162 ? 0.4640 0.5191 0.5890 0.0558  -0.0384 -0.0271 161 LEU A N   
1155 C CA  . LEU A 162 ? 0.4901 0.5475 0.6179 0.0623  -0.0379 -0.0363 161 LEU A CA  
1156 C C   . LEU A 162 ? 0.5110 0.5849 0.6324 0.0622  -0.0357 -0.0394 161 LEU A C   
1157 O O   . LEU A 162 ? 0.4595 0.5443 0.5833 0.0685  -0.0339 -0.0434 161 LEU A O   
1158 C CB  . LEU A 162 ? 0.4876 0.5308 0.6175 0.0621  -0.0397 -0.0427 161 LEU A CB  
1159 C CG  . LEU A 162 ? 0.5420 0.5683 0.6797 0.0618  -0.0412 -0.0392 161 LEU A CG  
1160 C CD1 . LEU A 162 ? 0.6039 0.6176 0.7461 0.0612  -0.0432 -0.0468 161 LEU A CD1 
1161 C CD2 . LEU A 162 ? 0.5072 0.5319 0.6525 0.0689  -0.0411 -0.0371 161 LEU A CD2 
1162 N N   . ALA A 163 ? 0.4907 0.5672 0.6044 0.0554  -0.0355 -0.0368 162 ALA A N   
1163 C CA  . ALA A 163 ? 0.4627 0.5544 0.5699 0.0547  -0.0330 -0.0378 162 ALA A CA  
1164 C C   . ALA A 163 ? 0.4608 0.5678 0.5706 0.0550  -0.0305 -0.0326 162 ALA A C   
1165 O O   . ALA A 163 ? 0.4652 0.5870 0.5744 0.0586  -0.0274 -0.0353 162 ALA A O   
1166 C CB  . ALA A 163 ? 0.4219 0.5114 0.5210 0.0473  -0.0336 -0.0345 162 ALA A CB  
1167 N N   . TYR A 164 ? 0.4257 0.5306 0.5389 0.0514  -0.0318 -0.0254 163 TYR A N   
1168 C CA  . TYR A 164 ? 0.4017 0.5216 0.5194 0.0515  -0.0304 -0.0210 163 TYR A CA  
1169 C C   . TYR A 164 ? 0.5059 0.6335 0.6311 0.0608  -0.0292 -0.0253 163 TYR A C   
1170 O O   . TYR A 164 ? 0.4191 0.5643 0.5473 0.0629  -0.0263 -0.0253 163 TYR A O   
1171 C CB  . TYR A 164 ? 0.4408 0.5560 0.5603 0.0469  -0.0331 -0.0139 163 TYR A CB  
1172 C CG  . TYR A 164 ? 0.4460 0.5761 0.5722 0.0479  -0.0331 -0.0103 163 TYR A CG  
1173 C CD1 . TYR A 164 ? 0.4474 0.5910 0.5737 0.0418  -0.0318 -0.0066 163 TYR A CD1 
1174 C CD2 . TYR A 164 ? 0.5211 0.6521 0.6545 0.0549  -0.0346 -0.0103 163 TYR A CD2 
1175 C CE1 . TYR A 164 ? 0.4344 0.5931 0.5688 0.0422  -0.0322 -0.0037 163 TYR A CE1 
1176 C CE2 . TYR A 164 ? 0.5000 0.6464 0.6405 0.0562  -0.0352 -0.0073 163 TYR A CE2 
1177 C CZ  . TYR A 164 ? 0.4892 0.6499 0.6305 0.0495  -0.0340 -0.0043 163 TYR A CZ  
1178 O OH  . TYR A 164 ? 0.4911 0.6682 0.6411 0.0503  -0.0350 -0.0017 163 TYR A OH  
1179 N N   . TYR A 165 ? 0.4802 0.5949 0.6095 0.0666  -0.0312 -0.0289 164 TYR A N   
1180 C CA  . TYR A 165 ? 0.4846 0.6043 0.6219 0.0765  -0.0305 -0.0333 164 TYR A CA  
1181 C C   . TYR A 165 ? 0.4659 0.5972 0.6014 0.0816  -0.0271 -0.0416 164 TYR A C   
1182 O O   . TYR A 165 ? 0.4900 0.6380 0.6301 0.0868  -0.0244 -0.0429 164 TYR A O   
1183 C CB  . TYR A 165 ? 0.5481 0.6489 0.6903 0.0813  -0.0334 -0.0355 164 TYR A CB  
1184 C CG  . TYR A 165 ? 0.5506 0.6545 0.7024 0.0916  -0.0335 -0.0381 164 TYR A CG  
1185 C CD1 . TYR A 165 ? 0.6520 0.7629 0.8096 0.0937  -0.0347 -0.0311 164 TYR A CD1 
1186 C CD2 . TYR A 165 ? 0.6757 0.7763 0.8309 0.0998  -0.0328 -0.0480 164 TYR A CD2 
1187 C CE1 . TYR A 165 ? 0.7198 0.8340 0.8867 0.1040  -0.0351 -0.0331 164 TYR A CE1 
1188 C CE2 . TYR A 165 ? 0.7588 0.8617 0.9235 0.1101  -0.0330 -0.0508 164 TYR A CE2 
1189 C CZ  . TYR A 165 ? 0.7527 0.8625 0.9234 0.1123  -0.0341 -0.0429 164 TYR A CZ  
1190 O OH  . TYR A 165 ? 0.7877 0.9003 0.9685 0.1233  -0.0346 -0.0451 164 TYR A OH  
1191 N N   . VAL A 166 ? 0.4578 0.5813 0.5865 0.0806  -0.0273 -0.0477 165 VAL A N   
1192 C CA  . VAL A 166 ? 0.4807 0.6155 0.6051 0.0858  -0.0242 -0.0561 165 VAL A CA  
1193 C C   . VAL A 166 ? 0.4385 0.5945 0.5588 0.0821  -0.0198 -0.0511 165 VAL A C   
1194 O O   . VAL A 166 ? 0.5420 0.7150 0.6633 0.0880  -0.0158 -0.0548 165 VAL A O   
1195 C CB  . VAL A 166 ? 0.5066 0.6295 0.6236 0.0844  -0.0263 -0.0631 165 VAL A CB  
1196 C CG1 . VAL A 166 ? 0.4591 0.5949 0.5693 0.0900  -0.0235 -0.0720 165 VAL A CG1 
1197 C CG2 . VAL A 166 ? 0.4813 0.5836 0.6052 0.0875  -0.0304 -0.0679 165 VAL A CG2 
1198 N N   . SER A 167 ? 0.4250 0.5803 0.5413 0.0723  -0.0203 -0.0423 166 SER A N   
1199 C CA  . SER A 167 ? 0.4405 0.6134 0.5531 0.0673  -0.0162 -0.0367 166 SER A CA  
1200 C C   . SER A 167 ? 0.4896 0.6808 0.6119 0.0693  -0.0135 -0.0330 166 SER A C   
1201 O O   . SER A 167 ? 0.4222 0.6328 0.5444 0.0708  -0.0084 -0.0329 166 SER A O   
1202 C CB  . SER A 167 ? 0.4151 0.5801 0.5226 0.0566  -0.0182 -0.0286 166 SER A CB  
1203 O OG  . SER A 167 ? 0.5109 0.6901 0.6141 0.0515  -0.0143 -0.0233 166 SER A OG  
1204 N N   . TYR A 168 ? 0.4001 0.5869 0.5310 0.0694  -0.0166 -0.0297 167 TYR A N   
1205 C CA  . TYR A 168 ? 0.4378 0.6434 0.5790 0.0713  -0.0148 -0.0264 167 TYR A CA  
1206 C C   . TYR A 168 ? 0.4914 0.7062 0.6391 0.0834  -0.0125 -0.0339 167 TYR A C   
1207 O O   . TYR A 168 ? 0.5139 0.7504 0.6685 0.0862  -0.0085 -0.0332 167 TYR A O   
1208 C CB  . TYR A 168 ? 0.4721 0.6717 0.6195 0.0675  -0.0196 -0.0201 167 TYR A CB  
1209 C CG  . TYR A 168 ? 0.5218 0.7120 0.6756 0.0758  -0.0231 -0.0225 167 TYR A CG  
1210 C CD1 . TYR A 168 ? 0.5983 0.7660 0.7479 0.0754  -0.0270 -0.0226 167 TYR A CD1 
1211 C CD2 . TYR A 168 ? 0.5497 0.7538 0.7142 0.0840  -0.0225 -0.0238 167 TYR A CD2 
1212 C CE1 . TYR A 168 ? 0.6177 0.7760 0.7732 0.0826  -0.0300 -0.0232 167 TYR A CE1 
1213 C CE2 . TYR A 168 ? 0.4968 0.6913 0.6671 0.0920  -0.0260 -0.0249 167 TYR A CE2 
1214 C CZ  . TYR A 168 ? 0.6228 0.7939 0.7883 0.0911  -0.0296 -0.0242 167 TYR A CZ  
1215 O OH  . TYR A 168 ? 0.9225 1.0833 1.0939 0.0988  -0.0328 -0.0239 167 TYR A OH  
1216 N N   . ARG A 169 ? 0.4999 0.6989 0.6468 0.0907  -0.0149 -0.0413 168 ARG A N   
1217 C CA  . ARG A 169 ? 0.4585 0.6644 0.6113 0.1029  -0.0130 -0.0498 168 ARG A CA  
1218 C C   . ARG A 169 ? 0.4831 0.7054 0.6297 0.1060  -0.0071 -0.0557 168 ARG A C   
1219 O O   . ARG A 169 ? 0.6041 0.8441 0.7566 0.1143  -0.0031 -0.0599 168 ARG A O   
1220 C CB  . ARG A 169 ? 0.5009 0.6837 0.6542 0.1090  -0.0171 -0.0568 168 ARG A CB  
1221 C CG  . ARG A 169 ? 0.6177 0.7874 0.7791 0.1100  -0.0218 -0.0514 168 ARG A CG  
1222 C CD  . ARG A 169 ? 0.5283 0.7129 0.7015 0.1183  -0.0212 -0.0505 168 ARG A CD  
1223 N NE  . ARG A 169 ? 0.5764 0.7610 0.7547 0.1309  -0.0199 -0.0609 168 ARG A NE  
1224 C CZ  . ARG A 169 ? 0.7288 0.9052 0.9169 0.1402  -0.0227 -0.0624 168 ARG A CZ  
1225 N NH1 . ARG A 169 ? 0.7511 0.9192 0.9441 0.1387  -0.0269 -0.0536 168 ARG A NH1 
1226 N NH2 . ARG A 169 ? 0.6388 0.8153 0.8314 0.1518  -0.0214 -0.0731 168 ARG A NH2 
1227 N N   . LEU A 170 ? 0.5397 0.7574 0.6741 0.0999  -0.0064 -0.0558 169 LEU A N   
1228 C CA  . LEU A 170 ? 0.4950 0.7284 0.6211 0.1028  -0.0009 -0.0605 169 LEU A CA  
1229 C C   . LEU A 170 ? 0.5236 0.7809 0.6514 0.0973  0.0049  -0.0515 169 LEU A C   
1230 O O   . LEU A 170 ? 0.4676 0.7464 0.5978 0.1034  0.0108  -0.0541 169 LEU A O   
1231 C CB  . LEU A 170 ? 0.4552 0.6754 0.5675 0.0986  -0.0029 -0.0632 169 LEU A CB  
1232 C CG  . LEU A 170 ? 0.5487 0.7537 0.6579 0.1065  -0.0064 -0.0762 169 LEU A CG  
1233 C CD1 . LEU A 170 ? 0.5009 0.6975 0.5967 0.1020  -0.0084 -0.0785 169 LEU A CD1 
1234 C CD2 . LEU A 170 ? 0.5494 0.7685 0.6606 0.1189  -0.0026 -0.0868 169 LEU A CD2 
1235 N N   . GLY A 171 ? 0.5054 0.7593 0.6328 0.0857  0.0034  -0.0409 170 GLY A N   
1236 C CA  . GLY A 171 ? 0.4491 0.7226 0.5775 0.0784  0.0085  -0.0318 170 GLY A CA  
1237 C C   . GLY A 171 ? 0.4669 0.7493 0.6090 0.0728  0.0077  -0.0237 170 GLY A C   
1238 O O   . GLY A 171 ? 0.4785 0.7713 0.6223 0.0636  0.0102  -0.0149 170 GLY A O   
1239 N N   . GLY A 172 ? 0.4267 0.7051 0.5790 0.0783  0.0037  -0.0264 171 GLY A N   
1240 C CA  . GLY A 172 ? 0.4215 0.7114 0.5873 0.0745  0.0023  -0.0198 171 GLY A CA  
1241 C C   . GLY A 172 ? 0.4828 0.7628 0.6472 0.0617  -0.0017 -0.0114 171 GLY A C   
1242 O O   . GLY A 172 ? 0.4840 0.7420 0.6395 0.0582  -0.0060 -0.0115 171 GLY A O   
1243 N N   . TYR A 173 ? 0.4509 0.7480 0.6252 0.0547  -0.0004 -0.0046 172 TYR A N   
1244 C CA  . TYR A 173 ? 0.4395 0.7284 0.6147 0.0430  -0.0049 0.0024  172 TYR A CA  
1245 C C   . TYR A 173 ? 0.4149 0.6904 0.5772 0.0350  -0.0040 0.0055  172 TYR A C   
1246 O O   . TYR A 173 ? 0.3962 0.6526 0.5529 0.0297  -0.0092 0.0070  172 TYR A O   
1247 C CB  . TYR A 173 ? 0.3571 0.6686 0.5470 0.0368  -0.0035 0.0082  172 TYR A CB  
1248 C CG  . TYR A 173 ? 0.3743 0.6782 0.5665 0.0247  -0.0087 0.0141  172 TYR A CG  
1249 C CD1 . TYR A 173 ? 0.3721 0.6642 0.5660 0.0247  -0.0165 0.0131  172 TYR A CD1 
1250 C CD2 . TYR A 173 ? 0.3492 0.6572 0.5416 0.0136  -0.0057 0.0207  172 TYR A CD2 
1251 C CE1 . TYR A 173 ? 0.3813 0.6669 0.5767 0.0144  -0.0215 0.0170  172 TYR A CE1 
1252 C CE2 . TYR A 173 ? 0.4311 0.7310 0.6263 0.0028  -0.0109 0.0249  172 TYR A CE2 
1253 C CZ  . TYR A 173 ? 0.4145 0.7035 0.6110 0.0035  -0.0189 0.0223  172 TYR A CZ  
1254 O OH  . TYR A 173 ? 0.4513 0.7324 0.6498 -0.0066 -0.0243 0.0252  172 TYR A OH  
1255 N N   . GLU A 174 ? 0.3670 0.6531 0.5241 0.0345  0.0026  0.0068  173 GLU A N   
1256 C CA  . GLU A 174 ? 0.4514 0.7256 0.5961 0.0277  0.0033  0.0105  173 GLU A CA  
1257 C C   . GLU A 174 ? 0.4483 0.7002 0.5803 0.0326  -0.0004 0.0041  173 GLU A C   
1258 O O   . GLU A 174 ? 0.3861 0.6211 0.5105 0.0266  -0.0037 0.0067  173 GLU A O   
1259 C CB  . GLU A 174 ? 0.4095 0.7018 0.5509 0.0269  0.0115  0.0144  173 GLU A CB  
1260 C CG  . GLU A 174 ? 0.4784 0.7887 0.6323 0.0175  0.0149  0.0237  173 GLU A CG  
1261 C CD  . GLU A 174 ? 0.5658 0.8884 0.7142 0.0133  0.0226  0.0311  173 GLU A CD  
1262 O OE1 . GLU A 174 ? 0.5827 0.9291 0.7358 0.0173  0.0300  0.0318  173 GLU A OE1 
1263 O OE2 . GLU A 174 ? 0.5793 0.8880 0.7184 0.0064  0.0214  0.0364  173 GLU A OE2 
1264 N N   . GLY A 175 ? 0.4410 0.6924 0.5720 0.0435  -0.0002 -0.0044 174 GLY A N   
1265 C CA  . GLY A 175 ? 0.3925 0.6224 0.5149 0.0476  -0.0044 -0.0108 174 GLY A CA  
1266 C C   . GLY A 175 ? 0.4309 0.6428 0.5560 0.0438  -0.0110 -0.0091 174 GLY A C   
1267 O O   . GLY A 175 ? 0.4540 0.6475 0.5715 0.0415  -0.0143 -0.0100 174 GLY A O   
1268 N N   . ALA A 176 ? 0.3887 0.6069 0.5247 0.0434  -0.0129 -0.0064 175 ALA A N   
1269 C CA  . ALA A 176 ? 0.3939 0.5973 0.5315 0.0400  -0.0190 -0.0041 175 ALA A CA  
1270 C C   . ALA A 176 ? 0.3984 0.5936 0.5307 0.0292  -0.0207 0.0015  175 ALA A C   
1271 O O   . ALA A 176 ? 0.4168 0.5939 0.5433 0.0270  -0.0245 0.0014  175 ALA A O   
1272 C CB  . ALA A 176 ? 0.4444 0.6592 0.5941 0.0420  -0.0210 -0.0023 175 ALA A CB  
1273 N N   . LEU A 177 ? 0.3871 0.5953 0.5222 0.0223  -0.0178 0.0068  176 LEU A N   
1274 C CA  . LEU A 177 ? 0.4212 0.6207 0.5522 0.0123  -0.0194 0.0121  176 LEU A CA  
1275 C C   . LEU A 177 ? 0.4475 0.6321 0.5658 0.0124  -0.0191 0.0107  176 LEU A C   
1276 O O   . LEU A 177 ? 0.4320 0.6009 0.5455 0.0078  -0.0227 0.0120  176 LEU A O   
1277 C CB  . LEU A 177 ? 0.4592 0.6755 0.5967 0.0051  -0.0156 0.0185  176 LEU A CB  
1278 C CG  . LEU A 177 ? 0.4735 0.7071 0.6259 0.0035  -0.0162 0.0202  176 LEU A CG  
1279 C CD1 . LEU A 177 ? 0.3851 0.6329 0.5448 -0.0058 -0.0126 0.0274  176 LEU A CD1 
1280 C CD2 . LEU A 177 ? 0.3715 0.5949 0.5270 0.0017  -0.0236 0.0191  176 LEU A CD2 
1281 N N   . LEU A 178 ? 0.3998 0.5902 0.5126 0.0179  -0.0150 0.0076  177 LEU A N   
1282 C CA  . LEU A 178 ? 0.4084 0.5861 0.5095 0.0189  -0.0155 0.0053  177 LEU A CA  
1283 C C   . LEU A 178 ? 0.4639 0.6228 0.5630 0.0218  -0.0205 0.0002  177 LEU A C   
1284 O O   . LEU A 178 ? 0.4698 0.6146 0.5625 0.0185  -0.0231 0.0010  177 LEU A O   
1285 C CB  . LEU A 178 ? 0.4062 0.5947 0.5017 0.0259  -0.0110 0.0009  177 LEU A CB  
1286 C CG  . LEU A 178 ? 0.4847 0.6613 0.5690 0.0295  -0.0127 -0.0045 177 LEU A CG  
1287 C CD1 . LEU A 178 ? 0.4434 0.6145 0.5193 0.0228  -0.0130 0.0017  177 LEU A CD1 
1288 C CD2 . LEU A 178 ? 0.5305 0.7182 0.6107 0.0385  -0.0093 -0.0119 177 LEU A CD2 
1289 N N   . GLY A 179 ? 0.4089 0.5678 0.5140 0.0281  -0.0217 -0.0042 178 GLY A N   
1290 C CA  . GLY A 179 ? 0.4449 0.5864 0.5494 0.0303  -0.0258 -0.0074 178 GLY A CA  
1291 C C   . GLY A 179 ? 0.4533 0.5848 0.5578 0.0235  -0.0294 -0.0025 178 GLY A C   
1292 O O   . GLY A 179 ? 0.4380 0.5545 0.5386 0.0226  -0.0319 -0.0035 178 GLY A O   
1293 N N   . LEU A 180 ? 0.4595 0.6000 0.5690 0.0186  -0.0296 0.0024  179 LEU A N   
1294 C CA  . LEU A 180 ? 0.4210 0.5528 0.5300 0.0122  -0.0332 0.0060  179 LEU A CA  
1295 C C   . LEU A 180 ? 0.4413 0.5630 0.5427 0.0067  -0.0334 0.0078  179 LEU A C   
1296 O O   . LEU A 180 ? 0.4375 0.5460 0.5356 0.0045  -0.0364 0.0079  179 LEU A O   
1297 C CB  . LEU A 180 ? 0.4301 0.5747 0.5469 0.0077  -0.0340 0.0098  179 LEU A CB  
1298 C CG  . LEU A 180 ? 0.4862 0.6395 0.6110 0.0128  -0.0356 0.0087  179 LEU A CG  
1299 C CD1 . LEU A 180 ? 0.3824 0.5491 0.5158 0.0072  -0.0372 0.0120  179 LEU A CD1 
1300 C CD2 . LEU A 180 ? 0.4645 0.6038 0.5861 0.0164  -0.0393 0.0073  179 LEU A CD2 
1301 N N   . ALA A 181 ? 0.3933 0.5219 0.4920 0.0050  -0.0302 0.0095  180 ALA A N   
1302 C CA  . ALA A 181 ? 0.4369 0.5560 0.5282 0.0008  -0.0306 0.0117  180 ALA A CA  
1303 C C   . ALA A 181 ? 0.4645 0.5722 0.5494 0.0055  -0.0318 0.0068  180 ALA A C   
1304 O O   . ALA A 181 ? 0.4534 0.5496 0.5337 0.0029  -0.0339 0.0076  180 ALA A O   
1305 C CB  . ALA A 181 ? 0.4500 0.5803 0.5395 -0.0018 -0.0266 0.0162  180 ALA A CB  
1306 N N   . LEU A 182 ? 0.4257 0.5365 0.5114 0.0124  -0.0307 0.0013  181 LEU A N   
1307 C CA  . LEU A 182 ? 0.4211 0.5217 0.5027 0.0165  -0.0322 -0.0041 181 LEU A CA  
1308 C C   . LEU A 182 ? 0.4528 0.5399 0.5372 0.0165  -0.0353 -0.0054 181 LEU A C   
1309 O O   . LEU A 182 ? 0.4454 0.5227 0.5276 0.0177  -0.0368 -0.0086 181 LEU A O   
1310 C CB  . LEU A 182 ? 0.4091 0.5169 0.4914 0.0239  -0.0303 -0.0105 181 LEU A CB  
1311 C CG  . LEU A 182 ? 0.4678 0.5884 0.5443 0.0255  -0.0270 -0.0109 181 LEU A CG  
1312 C CD1 . LEU A 182 ? 0.4179 0.5490 0.4973 0.0332  -0.0246 -0.0170 181 LEU A CD1 
1313 C CD2 . LEU A 182 ? 0.4425 0.5565 0.5104 0.0256  -0.0288 -0.0132 181 LEU A CD2 
1314 N N   . ILE A 183 ? 0.4498 0.5372 0.5390 0.0154  -0.0361 -0.0027 182 ILE A N   
1315 C CA  . ILE A 183 ? 0.4480 0.5239 0.5387 0.0158  -0.0384 -0.0027 182 ILE A CA  
1316 C C   . ILE A 183 ? 0.4631 0.5284 0.5491 0.0117  -0.0398 -0.0017 182 ILE A C   
1317 O O   . ILE A 183 ? 0.4517 0.5082 0.5375 0.0135  -0.0405 -0.0044 182 ILE A O   
1318 C CB  . ILE A 183 ? 0.4897 0.5694 0.5842 0.0149  -0.0396 0.0007  182 ILE A CB  
1319 C CG1 . ILE A 183 ? 0.5502 0.6396 0.6508 0.0205  -0.0386 -0.0006 182 ILE A CG1 
1320 C CG2 . ILE A 183 ? 0.4858 0.5542 0.5793 0.0147  -0.0415 0.0018  182 ILE A CG2 
1321 C CD1 . ILE A 183 ? 0.4893 0.5736 0.5918 0.0270  -0.0378 -0.0052 182 ILE A CD1 
1322 N N   . PRO A 184 ? 0.4849 0.5506 0.5681 0.0063  -0.0405 0.0019  183 PRO A N   
1323 C CA  . PRO A 184 ? 0.4463 0.5016 0.5257 0.0036  -0.0419 0.0023  183 PRO A CA  
1324 C C   . PRO A 184 ? 0.3978 0.4515 0.4733 0.0043  -0.0418 0.0006  183 PRO A C   
1325 O O   . PRO A 184 ? 0.5252 0.5706 0.5989 0.0034  -0.0432 0.0001  183 PRO A O   
1326 C CB  . PRO A 184 ? 0.3295 0.3854 0.4082 -0.0020 -0.0430 0.0062  183 PRO A CB  
1327 C CG  . PRO A 184 ? 0.4127 0.4808 0.4940 -0.0032 -0.0415 0.0083  183 PRO A CG  
1328 C CD  . PRO A 184 ? 0.4093 0.4844 0.4940 0.0023  -0.0400 0.0056  183 PRO A CD  
1329 N N   . ALA A 185 ? 0.3998 0.4623 0.4739 0.0064  -0.0401 -0.0005 184 ALA A N   
1330 C CA  . ALA A 185 ? 0.4474 0.5100 0.5162 0.0075  -0.0404 -0.0020 184 ALA A CA  
1331 C C   . ALA A 185 ? 0.4777 0.5359 0.5477 0.0120  -0.0417 -0.0087 184 ALA A C   
1332 O O   . ALA A 185 ? 0.3926 0.4466 0.4600 0.0123  -0.0437 -0.0105 184 ALA A O   
1333 C CB  . ALA A 185 ? 0.3888 0.4639 0.4542 0.0083  -0.0378 -0.0004 184 ALA A CB  
1334 N N   . LEU A 186 ? 0.4451 0.5043 0.5201 0.0157  -0.0410 -0.0125 185 LEU A N   
1335 C CA  . LEU A 186 ? 0.4110 0.4654 0.4889 0.0196  -0.0424 -0.0193 185 LEU A CA  
1336 C C   . LEU A 186 ? 0.4223 0.4654 0.5039 0.0176  -0.0443 -0.0196 185 LEU A C   
1337 O O   . LEU A 186 ? 0.4796 0.5184 0.5649 0.0197  -0.0459 -0.0251 185 LEU A O   
1338 C CB  . LEU A 186 ? 0.4659 0.5222 0.5495 0.0240  -0.0412 -0.0225 185 LEU A CB  
1339 C CG  . LEU A 186 ? 0.4603 0.5291 0.5414 0.0279  -0.0391 -0.0252 185 LEU A CG  
1340 C CD1 . LEU A 186 ? 0.4642 0.5360 0.5518 0.0317  -0.0377 -0.0258 185 LEU A CD1 
1341 C CD2 . LEU A 186 ? 0.5066 0.5764 0.5846 0.0319  -0.0405 -0.0333 185 LEU A CD2 
1342 N N   . VAL A 187 ? 0.4293 0.4681 0.5106 0.0139  -0.0442 -0.0143 186 VAL A N   
1343 C CA  . VAL A 187 ? 0.4351 0.4651 0.5196 0.0123  -0.0453 -0.0142 186 VAL A CA  
1344 C C   . VAL A 187 ? 0.4100 0.4391 0.4929 0.0121  -0.0476 -0.0171 186 VAL A C   
1345 O O   . VAL A 187 ? 0.3977 0.4213 0.4856 0.0118  -0.0487 -0.0193 186 VAL A O   
1346 C CB  . VAL A 187 ? 0.3703 0.3973 0.4533 0.0090  -0.0447 -0.0088 186 VAL A CB  
1347 C CG1 . VAL A 187 ? 0.3928 0.4214 0.4700 0.0062  -0.0456 -0.0061 186 VAL A CG1 
1348 C CG2 . VAL A 187 ? 0.4026 0.4220 0.4897 0.0084  -0.0446 -0.0087 186 VAL A CG2 
1349 N N   . VAL A 188 ? 0.4097 0.4449 0.4859 0.0124  -0.0483 -0.0169 187 VAL A N   
1350 C CA  . VAL A 188 ? 0.3745 0.4097 0.4479 0.0129  -0.0511 -0.0188 187 VAL A CA  
1351 C C   . VAL A 188 ? 0.3528 0.3876 0.4309 0.0158  -0.0534 -0.0267 187 VAL A C   
1352 O O   . VAL A 188 ? 0.4055 0.4383 0.4858 0.0157  -0.0563 -0.0292 187 VAL A O   
1353 C CB  . VAL A 188 ? 0.4002 0.4427 0.4645 0.0131  -0.0511 -0.0158 187 VAL A CB  
1354 C CG1 . VAL A 188 ? 0.4079 0.4593 0.4690 0.0169  -0.0502 -0.0201 187 VAL A CG1 
1355 C CG2 . VAL A 188 ? 0.3947 0.4359 0.4554 0.0132  -0.0543 -0.0152 187 VAL A CG2 
1356 N N   . ILE A 189 ? 0.3740 0.4106 0.4549 0.0184  -0.0524 -0.0311 188 ILE A N   
1357 C CA  . ILE A 189 ? 0.3786 0.4139 0.4648 0.0211  -0.0551 -0.0397 188 ILE A CA  
1358 C C   . ILE A 189 ? 0.3674 0.3937 0.4647 0.0188  -0.0558 -0.0405 188 ILE A C   
1359 O O   . ILE A 189 ? 0.3848 0.4101 0.4861 0.0183  -0.0591 -0.0447 188 ILE A O   
1360 C CB  . ILE A 189 ? 0.3614 0.3997 0.4483 0.0252  -0.0539 -0.0447 188 ILE A CB  
1361 C CG1 . ILE A 189 ? 0.4367 0.4864 0.5130 0.0283  -0.0534 -0.0461 188 ILE A CG1 
1362 C CG2 . ILE A 189 ? 0.4091 0.4419 0.5053 0.0270  -0.0566 -0.0536 188 ILE A CG2 
1363 C CD1 . ILE A 189 ? 0.4716 0.5268 0.5477 0.0318  -0.0503 -0.0473 188 ILE A CD1 
1364 N N   . PRO A 190 ? 0.3822 0.4029 0.4849 0.0173  -0.0529 -0.0362 189 PRO A N   
1365 C CA  . PRO A 190 ? 0.3801 0.3934 0.4929 0.0149  -0.0527 -0.0354 189 PRO A CA  
1366 C C   . PRO A 190 ? 0.4408 0.4540 0.5528 0.0120  -0.0530 -0.0317 189 PRO A C   
1367 O O   . PRO A 190 ? 0.3815 0.3921 0.5020 0.0105  -0.0541 -0.0337 189 PRO A O   
1368 C CB  . PRO A 190 ? 0.4015 0.4104 0.5171 0.0149  -0.0490 -0.0302 189 PRO A CB  
1369 C CG  . PRO A 190 ? 0.3745 0.3892 0.4807 0.0158  -0.0477 -0.0266 189 PRO A CG  
1370 C CD  . PRO A 190 ? 0.3965 0.4181 0.4970 0.0182  -0.0497 -0.0318 189 PRO A CD  
1371 N N   . ALA A 191 ? 0.4080 0.4238 0.5111 0.0113  -0.0520 -0.0266 190 ALA A N   
1372 C CA  . ALA A 191 ? 0.3851 0.3999 0.4874 0.0094  -0.0524 -0.0236 190 ALA A CA  
1373 C C   . ALA A 191 ? 0.4065 0.4241 0.5104 0.0103  -0.0565 -0.0282 190 ALA A C   
1374 O O   . ALA A 191 ? 0.3838 0.4002 0.4943 0.0092  -0.0573 -0.0286 190 ALA A O   
1375 C CB  . ALA A 191 ? 0.3392 0.3552 0.4321 0.0086  -0.0515 -0.0183 190 ALA A CB  
1376 N N   . ALA A 192 ? 0.3861 0.4089 0.4839 0.0125  -0.0592 -0.0317 191 ALA A N   
1377 C CA  . ALA A 192 ? 0.4005 0.4273 0.4988 0.0140  -0.0639 -0.0365 191 ALA A CA  
1378 C C   . ALA A 192 ? 0.3916 0.4168 0.5025 0.0136  -0.0660 -0.0434 191 ALA A C   
1379 O O   . ALA A 192 ? 0.4648 0.4915 0.5821 0.0130  -0.0691 -0.0457 191 ALA A O   
1380 C CB  . ALA A 192 ? 0.4258 0.4594 0.5134 0.0171  -0.0659 -0.0387 191 ALA A CB  
1381 N N   . ILE A 193 ? 0.4295 0.4517 0.5454 0.0137  -0.0646 -0.0467 192 ILE A N   
1382 C CA  . ILE A 193 ? 0.4307 0.4497 0.5604 0.0126  -0.0665 -0.0530 192 ILE A CA  
1383 C C   . ILE A 193 ? 0.4229 0.4379 0.5636 0.0088  -0.0641 -0.0485 192 ILE A C   
1384 O O   . ILE A 193 ? 0.4564 0.4728 0.6077 0.0072  -0.0668 -0.0522 192 ILE A O   
1385 C CB  . ILE A 193 ? 0.4855 0.5000 0.6184 0.0139  -0.0651 -0.0565 192 ILE A CB  
1386 C CG1 . ILE A 193 ? 0.4467 0.4669 0.5718 0.0182  -0.0685 -0.0644 192 ILE A CG1 
1387 C CG2 . ILE A 193 ? 0.5311 0.5387 0.6807 0.0113  -0.0654 -0.0597 192 ILE A CG2 
1388 C CD1 . ILE A 193 ? 0.3773 0.3956 0.4999 0.0211  -0.0658 -0.0653 192 ILE A CD1 
1389 N N   . MET A 194 ? 0.4429 0.4541 0.5812 0.0076  -0.0589 -0.0406 193 MET A N   
1390 C CA  . MET A 194 ? 0.4451 0.4535 0.5925 0.0047  -0.0555 -0.0360 193 MET A CA  
1391 C C   . MET A 194 ? 0.4253 0.4383 0.5735 0.0043  -0.0571 -0.0353 193 MET A C   
1392 O O   . MET A 194 ? 0.4164 0.4304 0.5767 0.0022  -0.0565 -0.0356 193 MET A O   
1393 C CB  . MET A 194 ? 0.4194 0.4241 0.5611 0.0045  -0.0502 -0.0282 193 MET A CB  
1394 C CG  . MET A 194 ? 0.5612 0.5608 0.7063 0.0050  -0.0482 -0.0275 193 MET A CG  
1395 S SD  . MET A 194 ? 0.7253 0.7189 0.8879 0.0019  -0.0457 -0.0263 193 MET A SD  
1396 C CE  . MET A 194 ? 0.6061 0.5969 0.7770 0.0028  -0.0506 -0.0363 193 MET A CE  
1397 N N   . LEU A 195 ? 0.4024 0.4185 0.5388 0.0064  -0.0589 -0.0341 194 LEU A N   
1398 C CA  . LEU A 195 ? 0.4288 0.4483 0.5656 0.0069  -0.0606 -0.0330 194 LEU A CA  
1399 C C   . LEU A 195 ? 0.4861 0.5109 0.6327 0.0071  -0.0657 -0.0395 194 LEU A C   
1400 O O   . LEU A 195 ? 0.4873 0.5149 0.6438 0.0063  -0.0658 -0.0394 194 LEU A O   
1401 C CB  . LEU A 195 ? 0.4141 0.4344 0.5366 0.0091  -0.0620 -0.0300 194 LEU A CB  
1402 C CG  . LEU A 195 ? 0.4652 0.4868 0.5864 0.0105  -0.0635 -0.0276 194 LEU A CG  
1403 C CD1 . LEU A 195 ? 0.5031 0.5209 0.6264 0.0094  -0.0586 -0.0232 194 LEU A CD1 
1404 C CD2 . LEU A 195 ? 0.5090 0.5309 0.6171 0.0125  -0.0659 -0.0249 194 LEU A CD2 
1405 N N   . ILE A 196 ? 0.4861 0.5134 0.6306 0.0085  -0.0703 -0.0457 195 ILE A N   
1406 C CA  . ILE A 196 ? 0.4246 0.4578 0.5775 0.0090  -0.0764 -0.0531 195 ILE A CA  
1407 C C   . ILE A 196 ? 0.4410 0.4725 0.6124 0.0052  -0.0757 -0.0569 195 ILE A C   
1408 O O   . ILE A 196 ? 0.4435 0.4800 0.6278 0.0037  -0.0783 -0.0597 195 ILE A O   
1409 C CB  . ILE A 196 ? 0.5432 0.5802 0.6863 0.0123  -0.0816 -0.0593 195 ILE A CB  
1410 C CG1 . ILE A 196 ? 0.5768 0.6163 0.7022 0.0156  -0.0819 -0.0542 195 ILE A CG1 
1411 C CG2 . ILE A 196 ? 0.4979 0.5417 0.6497 0.0130  -0.0889 -0.0683 195 ILE A CG2 
1412 C CD1 . ILE A 196 ? 0.5711 0.6104 0.6947 0.0159  -0.0808 -0.0470 195 ILE A CD1 
1413 N N   . LYS A 197 ? 0.4054 0.4300 0.5794 0.0035  -0.0722 -0.0565 196 LYS A N   
1414 C CA  . LYS A 197 ? 0.4305 0.4517 0.6227 -0.0005 -0.0714 -0.0594 196 LYS A CA  
1415 C C   . LYS A 197 ? 0.4300 0.4517 0.6335 -0.0039 -0.0663 -0.0527 196 LYS A C   
1416 O O   . LYS A 197 ? 0.3973 0.4208 0.6184 -0.0075 -0.0670 -0.0552 196 LYS A O   
1417 C CB  . LYS A 197 ? 0.4209 0.4336 0.6123 -0.0006 -0.0687 -0.0594 196 LYS A CB  
1418 C CG  . LYS A 197 ? 0.5988 0.6045 0.8052 -0.0049 -0.0637 -0.0550 196 LYS A CG  
1419 C CD  . LYS A 197 ? 0.5750 0.5717 0.7784 -0.0037 -0.0609 -0.0533 196 LYS A CD  
1420 C CE  . LYS A 197 ? 0.6342 0.6289 0.8382 -0.0014 -0.0665 -0.0641 196 LYS A CE  
1421 N NZ  . LYS A 197 ? 0.6439 0.6330 0.8390 0.0021  -0.0643 -0.0627 196 LYS A NZ  
1422 N N   . ARG A 198 ? 0.4039 0.4245 0.5977 -0.0028 -0.0611 -0.0445 197 ARG A N   
1423 C CA  . ARG A 198 ? 0.4308 0.4527 0.6332 -0.0051 -0.0554 -0.0382 197 ARG A CA  
1424 C C   . ARG A 198 ? 0.4065 0.4374 0.6145 -0.0043 -0.0577 -0.0396 197 ARG A C   
1425 O O   . ARG A 198 ? 0.3477 0.3817 0.5640 -0.0057 -0.0529 -0.0353 197 ARG A O   
1426 C CB  . ARG A 198 ? 0.4282 0.4460 0.6179 -0.0037 -0.0494 -0.0301 197 ARG A CB  
1427 C CG  . ARG A 198 ? 0.3653 0.3755 0.5548 -0.0050 -0.0454 -0.0264 197 ARG A CG  
1428 C CD  . ARG A 198 ? 0.4249 0.4324 0.5994 -0.0029 -0.0414 -0.0199 197 ARG A CD  
1429 N NE  . ARG A 198 ? 0.3936 0.4028 0.5698 -0.0035 -0.0355 -0.0135 197 ARG A NE  
1430 C CZ  . ARG A 198 ? 0.4664 0.4735 0.6503 -0.0057 -0.0301 -0.0081 197 ARG A CZ  
1431 N NH1 . ARG A 198 ? 0.3473 0.3489 0.5397 -0.0076 -0.0302 -0.0082 197 ARG A NH1 
1432 N NH2 . ARG A 198 ? 0.3607 0.3710 0.5435 -0.0054 -0.0245 -0.0023 197 ARG A NH2 
1433 N N   . GLY A 199 ? 0.4261 0.4618 0.6296 -0.0015 -0.0647 -0.0453 198 GLY A N   
1434 C CA  . GLY A 199 ? 0.3721 0.4166 0.5818 0.0000  -0.0678 -0.0467 198 GLY A CA  
1435 C C   . GLY A 199 ? 0.3427 0.3875 0.5430 0.0032  -0.0644 -0.0407 198 GLY A C   
1436 O O   . GLY A 199 ? 0.2892 0.3407 0.4978 0.0043  -0.0646 -0.0404 198 GLY A O   
1437 N N   . VAL A 200 ? 0.4783 0.5161 0.6624 0.0047  -0.0617 -0.0363 199 VAL A N   
1438 C CA  . VAL A 200 ? 0.4841 0.5204 0.6595 0.0074  -0.0587 -0.0312 199 VAL A CA  
1439 C C   . VAL A 200 ? 0.3980 0.4383 0.5698 0.0116  -0.0643 -0.0328 199 VAL A C   
1440 O O   . VAL A 200 ? 0.4645 0.5088 0.6419 0.0137  -0.0636 -0.0319 199 VAL A O   
1441 C CB  . VAL A 200 ? 0.3773 0.4056 0.5374 0.0075  -0.0556 -0.0271 199 VAL A CB  
1442 C CG1 . VAL A 200 ? 0.3590 0.3849 0.5140 0.0089  -0.0509 -0.0225 199 VAL A CG1 
1443 C CG2 . VAL A 200 ? 0.4604 0.4849 0.6232 0.0044  -0.0526 -0.0267 199 VAL A CG2 
1444 N N   . ILE A 201 ? 0.4367 0.4766 0.5990 0.0132  -0.0699 -0.0348 200 ILE A N   
1445 C CA  . ILE A 201 ? 0.4429 0.4866 0.6008 0.0175  -0.0759 -0.0355 200 ILE A CA  
1446 C C   . ILE A 201 ? 0.3904 0.4393 0.5475 0.0182  -0.0827 -0.0410 200 ILE A C   
1447 O O   . ILE A 201 ? 0.3900 0.4371 0.5453 0.0159  -0.0824 -0.0439 200 ILE A O   
1448 C CB  . ILE A 201 ? 0.4767 0.5136 0.6187 0.0200  -0.0753 -0.0298 200 ILE A CB  
1449 C CG1 . ILE A 201 ? 0.5282 0.5594 0.6589 0.0177  -0.0730 -0.0281 200 ILE A CG1 
1450 C CG2 . ILE A 201 ? 0.4598 0.4929 0.6032 0.0211  -0.0709 -0.0262 200 ILE A CG2 
1451 C CD1 . ILE A 201 ? 0.4978 0.5268 0.6138 0.0199  -0.0758 -0.0247 200 ILE A CD1 
1452 N N   . PRO A 202 ? 0.4166 0.4723 0.5746 0.0220  -0.0892 -0.0430 201 PRO A N   
1453 C CA  . PRO A 202 ? 0.4712 0.5323 0.6238 0.0238  -0.0963 -0.0480 201 PRO A CA  
1454 C C   . PRO A 202 ? 0.4759 0.5318 0.6092 0.0252  -0.0955 -0.0441 201 PRO A C   
1455 O O   . PRO A 202 ? 0.4903 0.5401 0.6142 0.0261  -0.0923 -0.0369 201 PRO A O   
1456 C CB  . PRO A 202 ? 0.4682 0.5376 0.6242 0.0285  -0.1031 -0.0488 201 PRO A CB  
1457 C CG  . PRO A 202 ? 0.4859 0.5560 0.6553 0.0282  -0.0995 -0.0466 201 PRO A CG  
1458 C CD  . PRO A 202 ? 0.4153 0.4751 0.5799 0.0254  -0.0908 -0.0412 201 PRO A CD  
1459 N N   . LEU A 203 ? 0.5494 0.6083 0.6777 0.0252  -0.0984 -0.0494 202 LEU A N   
1460 C CA  . LEU A 203 ? 0.5568 0.6133 0.6676 0.0267  -0.0971 -0.0460 202 LEU A CA  
1461 C C   . LEU A 203 ? 0.5314 0.5894 0.6298 0.0310  -0.1000 -0.0394 202 LEU A C   
1462 O O   . LEU A 203 ? 0.5344 0.5877 0.6208 0.0309  -0.0966 -0.0324 202 LEU A O   
1463 C CB  . LEU A 203 ? 0.5209 0.5824 0.6287 0.0274  -0.1005 -0.0543 202 LEU A CB  
1464 C CG  . LEU A 203 ? 0.7230 0.7849 0.8137 0.0293  -0.0988 -0.0521 202 LEU A CG  
1465 C CD1 . LEU A 203 ? 0.7074 0.7609 0.7944 0.0262  -0.0910 -0.0448 202 LEU A CD1 
1466 C CD2 . LEU A 203 ? 0.6518 0.7185 0.7423 0.0303  -0.1017 -0.0623 202 LEU A CD2 
1467 N N   . SER A 204 ? 0.4457 0.5102 0.5480 0.0346  -0.1064 -0.0410 203 SER A N   
1468 C CA  . SER A 204 ? 0.5359 0.6019 0.6265 0.0395  -0.1100 -0.0343 203 SER A CA  
1469 C C   . SER A 204 ? 0.5081 0.5641 0.5963 0.0391  -0.1054 -0.0248 203 SER A C   
1470 O O   . SER A 204 ? 0.4716 0.5253 0.5483 0.0420  -0.1066 -0.0173 203 SER A O   
1471 C CB  . SER A 204 ? 0.5227 0.5984 0.6201 0.0439  -0.1183 -0.0384 203 SER A CB  
1472 O OG  . SER A 204 ? 0.6083 0.6837 0.7232 0.0425  -0.1175 -0.0402 203 SER A OG  
1473 N N   . TYR A 205 ? 0.4608 0.5107 0.5594 0.0356  -0.1002 -0.0250 204 TYR A N   
1474 C CA  . TYR A 205 ? 0.4477 0.4878 0.5438 0.0354  -0.0962 -0.0177 204 TYR A CA  
1475 C C   . TYR A 205 ? 0.4133 0.4468 0.4955 0.0336  -0.0928 -0.0111 204 TYR A C   
1476 O O   . TYR A 205 ? 0.4410 0.4669 0.5182 0.0343  -0.0918 -0.0041 204 TYR A O   
1477 C CB  . TYR A 205 ? 0.4292 0.4654 0.5371 0.0321  -0.0907 -0.0199 204 TYR A CB  
1478 C CG  . TYR A 205 ? 0.4018 0.4429 0.5241 0.0344  -0.0925 -0.0231 204 TYR A CG  
1479 C CD1 . TYR A 205 ? 0.4229 0.4734 0.5500 0.0383  -0.0995 -0.0261 204 TYR A CD1 
1480 C CD2 . TYR A 205 ? 0.4615 0.4996 0.5928 0.0328  -0.0871 -0.0233 204 TYR A CD2 
1481 C CE1 . TYR A 205 ? 0.4721 0.5289 0.6141 0.0404  -0.1011 -0.0292 204 TYR A CE1 
1482 C CE2 . TYR A 205 ? 0.4012 0.4456 0.5465 0.0351  -0.0880 -0.0261 204 TYR A CE2 
1483 C CZ  . TYR A 205 ? 0.4047 0.4586 0.5562 0.0387  -0.0949 -0.0290 204 TYR A CZ  
1484 O OH  . TYR A 205 ? 0.4764 0.5382 0.6435 0.0410  -0.0957 -0.0319 204 TYR A OH  
1485 N N   . LEU A 206 ? 0.3741 0.4106 0.4509 0.0312  -0.0910 -0.0135 205 LEU A N   
1486 C CA  . LEU A 206 ? 0.4595 0.4920 0.5251 0.0289  -0.0871 -0.0078 205 LEU A CA  
1487 C C   . LEU A 206 ? 0.4326 0.4687 0.4851 0.0320  -0.0900 -0.0020 205 LEU A C   
1488 O O   . LEU A 206 ? 0.4262 0.4603 0.4699 0.0299  -0.0864 0.0038  205 LEU A O   
1489 C CB  . LEU A 206 ? 0.4133 0.4485 0.4796 0.0258  -0.0836 -0.0129 205 LEU A CB  
1490 C CG  . LEU A 206 ? 0.5470 0.5768 0.6234 0.0221  -0.0791 -0.0154 205 LEU A CG  
1491 C CD1 . LEU A 206 ? 0.4757 0.5087 0.5554 0.0204  -0.0774 -0.0215 205 LEU A CD1 
1492 C CD2 . LEU A 206 ? 0.4465 0.4681 0.5193 0.0194  -0.0747 -0.0089 205 LEU A CD2 
1493 N N   . LYS A 207 ? 0.4288 0.4711 0.4798 0.0368  -0.0961 -0.0029 206 LYS A N   
1494 C CA  . LYS A 207 ? 0.4544 0.4999 0.4917 0.0404  -0.0988 0.0043  206 LYS A CA  
1495 C C   . LYS A 207 ? 0.4638 0.4983 0.4982 0.0397  -0.0967 0.0153  206 LYS A C   
1496 O O   . LYS A 207 ? 0.4828 0.5103 0.5256 0.0405  -0.0979 0.0159  206 LYS A O   
1497 C CB  . LYS A 207 ? 0.4051 0.4599 0.4419 0.0464  -0.1068 0.0011  206 LYS A CB  
1498 C CG  . LYS A 207 ? 0.6311 0.6968 0.6702 0.0472  -0.1098 -0.0105 206 LYS A CG  
1499 C CD  . LYS A 207 ? 0.6397 0.7146 0.6827 0.0524  -0.1186 -0.0155 206 LYS A CD  
1500 C CE  . LYS A 207 ? 0.7016 0.7888 0.7373 0.0551  -0.1231 -0.0237 206 LYS A CE  
1501 N NZ  . LYS A 207 ? 0.8184 0.9156 0.8603 0.0597  -0.1325 -0.0307 206 LYS A NZ  
1502 N N   . PRO A 208 ? 0.4872 0.5200 0.5108 0.0380  -0.0936 0.0238  207 PRO A N   
1503 C CA  . PRO A 208 ? 0.4703 0.4911 0.4928 0.0362  -0.0917 0.0341  207 PRO A CA  
1504 C C   . PRO A 208 ? 0.4807 0.4979 0.5032 0.0419  -0.0974 0.0392  207 PRO A C   
1505 O O   . PRO A 208 ? 0.4548 0.4803 0.4697 0.0472  -0.1021 0.0412  207 PRO A O   
1506 C CB  . PRO A 208 ? 0.5436 0.5672 0.5545 0.0337  -0.0878 0.0423  207 PRO A CB  
1507 C CG  . PRO A 208 ? 0.4814 0.5167 0.4897 0.0330  -0.0858 0.0343  207 PRO A CG  
1508 C CD  . PRO A 208 ? 0.3989 0.4410 0.4119 0.0373  -0.0912 0.0240  207 PRO A CD  
1509 N N   . SER A 209 ? 0.4926 0.4977 0.5235 0.0415  -0.0972 0.0408  208 SER A N   
1510 C CA  . SER A 209 ? 0.4648 0.4634 0.4966 0.0469  -0.1019 0.0469  208 SER A CA  
1511 C C   . SER A 209 ? 0.5084 0.4904 0.5432 0.0435  -0.0988 0.0533  208 SER A C   
1512 O O   . SER A 209 ? 0.5097 0.4869 0.5469 0.0372  -0.0937 0.0514  208 SER A O   
1513 C CB  . SER A 209 ? 0.4208 0.4234 0.4636 0.0520  -0.1065 0.0387  208 SER A CB  
1514 O OG  . SER A 209 ? 0.5086 0.5060 0.5627 0.0487  -0.1028 0.0316  208 SER A OG  
1515 N N   . TRP A 210 ? 0.5660 0.5387 0.6010 0.0480  -0.1024 0.0607  209 TRP A N   
1516 C CA  . TRP A 210 ? 0.5614 0.5166 0.6001 0.0451  -0.1004 0.0661  209 TRP A CA  
1517 C C   . TRP A 210 ? 0.5951 0.5416 0.6435 0.0511  -0.1042 0.0634  209 TRP A C   
1518 O O   . TRP A 210 ? 0.6214 0.5704 0.6692 0.0586  -0.1097 0.0666  209 TRP A O   
1519 C CB  . TRP A 210 ? 0.5443 0.4929 0.5740 0.0436  -0.1001 0.0804  209 TRP A CB  
1520 C CG  . TRP A 210 ? 0.5525 0.4841 0.5869 0.0377  -0.0969 0.0847  209 TRP A CG  
1521 C CD1 . TRP A 210 ? 0.4990 0.4135 0.5381 0.0397  -0.0994 0.0906  209 TRP A CD1 
1522 C CD2 . TRP A 210 ? 0.4966 0.4268 0.5326 0.0288  -0.0913 0.0826  209 TRP A CD2 
1523 N NE1 . TRP A 210 ? 0.5204 0.4224 0.5640 0.0321  -0.0958 0.0918  209 TRP A NE1 
1524 C CE2 . TRP A 210 ? 0.4853 0.3974 0.5270 0.0254  -0.0910 0.0871  209 TRP A CE2 
1525 C CE3 . TRP A 210 ? 0.5108 0.4530 0.5445 0.0239  -0.0870 0.0772  209 TRP A CE3 
1526 C CZ2 . TRP A 210 ? 0.5051 0.4122 0.5504 0.0167  -0.0868 0.0860  209 TRP A CZ2 
1527 C CZ3 . TRP A 210 ? 0.4587 0.3961 0.4956 0.0159  -0.0826 0.0769  209 TRP A CZ3 
1528 C CH2 . TRP A 210 ? 0.4631 0.3838 0.5059 0.0122  -0.0827 0.0811  209 TRP A CH2 
1529 N N   . ASP A 211 ? 0.5222 0.4592 0.5790 0.0485  -0.1015 0.0574  210 ASP A N   
1530 C CA  . ASP A 211 ? 0.5249 0.4514 0.5907 0.0540  -0.1040 0.0548  210 ASP A CA  
1531 C C   . ASP A 211 ? 0.5023 0.4104 0.5698 0.0495  -0.1017 0.0578  210 ASP A C   
1532 O O   . ASP A 211 ? 0.4532 0.3599 0.5220 0.0429  -0.0974 0.0526  210 ASP A O   
1533 C CB  . ASP A 211 ? 0.5550 0.4899 0.6303 0.0562  -0.1030 0.0423  210 ASP A CB  
1534 C CG  . ASP A 211 ? 0.6240 0.5525 0.7087 0.0640  -0.1060 0.0394  210 ASP A CG  
1535 O OD1 . ASP A 211 ? 0.6391 0.5538 0.7276 0.0635  -0.1043 0.0375  210 ASP A OD1 
1536 O OD2 . ASP A 211 ? 0.7753 0.7131 0.8638 0.0710  -0.1104 0.0385  210 ASP A OD2 
1537 N N   . ASN A 212 ? 0.5311 0.4250 0.5990 0.0531  -0.1052 0.0661  211 ASN A N   
1538 C CA  . ASN A 212 ? 0.5293 0.4043 0.5994 0.0481  -0.1037 0.0699  211 ASN A CA  
1539 C C   . ASN A 212 ? 0.5137 0.3819 0.5921 0.0473  -0.1019 0.0578  211 ASN A C   
1540 O O   . ASN A 212 ? 0.5266 0.3880 0.6056 0.0398  -0.0989 0.0558  211 ASN A O   
1541 C CB  . ASN A 212 ? 0.4958 0.3557 0.5666 0.0532  -0.1083 0.0807  211 ASN A CB  
1542 C CG  . ASN A 212 ? 0.6191 0.4790 0.6804 0.0496  -0.1081 0.0957  211 ASN A CG  
1543 O OD1 . ASN A 212 ? 0.6172 0.4839 0.6734 0.0415  -0.1037 0.0979  211 ASN A OD1 
1544 N ND2 . ASN A 212 ? 0.6667 0.5201 0.7259 0.0561  -0.1126 0.1066  211 ASN A ND2 
1545 N N   . GLY A 213 ? 0.4957 0.3670 0.5807 0.0551  -0.1036 0.0497  212 GLY A N   
1546 C CA  . GLY A 213 ? 0.4386 0.3056 0.5302 0.0554  -0.1013 0.0380  212 GLY A CA  
1547 C C   . GLY A 213 ? 0.5506 0.4280 0.6397 0.0479  -0.0961 0.0314  212 GLY A C   
1548 O O   . GLY A 213 ? 0.5122 0.3815 0.6014 0.0425  -0.0939 0.0279  212 GLY A O   
1549 N N   . LEU A 214 ? 0.4917 0.3869 0.5787 0.0477  -0.0945 0.0296  213 LEU A N   
1550 C CA  . LEU A 214 ? 0.4605 0.3655 0.5457 0.0415  -0.0897 0.0238  213 LEU A CA  
1551 C C   . LEU A 214 ? 0.4872 0.3883 0.5663 0.0328  -0.0878 0.0291  213 LEU A C   
1552 O O   . LEU A 214 ? 0.5060 0.4080 0.5847 0.0276  -0.0845 0.0241  213 LEU A O   
1553 C CB  . LEU A 214 ? 0.4813 0.4044 0.5665 0.0430  -0.0891 0.0216  213 LEU A CB  
1554 C CG  . LEU A 214 ? 0.5414 0.4721 0.6351 0.0501  -0.0899 0.0148  213 LEU A CG  
1555 C CD1 . LEU A 214 ? 0.5386 0.4861 0.6333 0.0506  -0.0905 0.0136  213 LEU A CD1 
1556 C CD2 . LEU A 214 ? 0.5480 0.4780 0.6462 0.0494  -0.0854 0.0060  213 LEU A CD2 
1557 N N   . ALA A 215 ? 0.4470 0.3446 0.5213 0.0314  -0.0898 0.0396  214 ALA A N   
1558 C CA  . ALA A 215 ? 0.4704 0.3653 0.5404 0.0230  -0.0875 0.0455  214 ALA A CA  
1559 C C   . ALA A 215 ? 0.5113 0.3905 0.5859 0.0189  -0.0874 0.0433  214 ALA A C   
1560 O O   . ALA A 215 ? 0.4779 0.3586 0.5523 0.0119  -0.0847 0.0406  214 ALA A O   
1561 C CB  . ALA A 215 ? 0.4666 0.3609 0.5308 0.0229  -0.0892 0.0582  214 ALA A CB  
1562 N N   . GLY A 216 ? 0.4604 0.3245 0.5396 0.0234  -0.0909 0.0437  215 GLY A N   
1563 C CA  . GLY A 216 ? 0.4803 0.3287 0.5646 0.0202  -0.0916 0.0394  215 GLY A CA  
1564 C C   . GLY A 216 ? 0.4948 0.3480 0.5807 0.0200  -0.0893 0.0263  215 GLY A C   
1565 O O   . GLY A 216 ? 0.5206 0.3677 0.6080 0.0144  -0.0888 0.0221  215 GLY A O   
1566 N N   . GLN A 217 ? 0.4528 0.3179 0.5387 0.0260  -0.0879 0.0199  216 GLN A N   
1567 C CA  . GLN A 217 ? 0.5508 0.4216 0.6375 0.0263  -0.0851 0.0088  216 GLN A CA  
1568 C C   . GLN A 217 ? 0.4611 0.3431 0.5435 0.0190  -0.0816 0.0085  216 GLN A C   
1569 O O   . GLN A 217 ? 0.4197 0.3007 0.5017 0.0157  -0.0803 0.0021  216 GLN A O   
1570 C CB  . GLN A 217 ? 0.4825 0.3634 0.5719 0.0344  -0.0840 0.0034  216 GLN A CB  
1571 C CG  . GLN A 217 ? 0.4411 0.3118 0.5361 0.0423  -0.0863 -0.0016 216 GLN A CG  
1572 C CD  . GLN A 217 ? 0.5669 0.4499 0.6663 0.0502  -0.0851 -0.0055 216 GLN A CD  
1573 O OE1 . GLN A 217 ? 0.6441 0.5366 0.7442 0.0519  -0.0862 -0.0005 216 GLN A OE1 
1574 N NE2 . GLN A 217 ? 0.5861 0.4700 0.6888 0.0550  -0.0830 -0.0150 216 GLN A NE2 
1575 N N   . LEU A 218 ? 0.4436 0.3366 0.5226 0.0169  -0.0804 0.0148  217 LEU A N   
1576 C CA  . LEU A 218 ? 0.4378 0.3409 0.5135 0.0105  -0.0773 0.0148  217 LEU A CA  
1577 C C   . LEU A 218 ? 0.4532 0.3486 0.5287 0.0029  -0.0778 0.0185  217 LEU A C   
1578 O O   . LEU A 218 ? 0.4274 0.3284 0.5021 -0.0021 -0.0758 0.0155  217 LEU A O   
1579 C CB  . LEU A 218 ? 0.4176 0.3337 0.4899 0.0107  -0.0761 0.0199  217 LEU A CB  
1580 C CG  . LEU A 218 ? 0.4378 0.3640 0.5119 0.0165  -0.0754 0.0150  217 LEU A CG  
1581 C CD1 . LEU A 218 ? 0.4596 0.3943 0.5310 0.0184  -0.0768 0.0203  217 LEU A CD1 
1582 C CD2 . LEU A 218 ? 0.4042 0.3395 0.4786 0.0145  -0.0716 0.0085  217 LEU A CD2 
1583 N N   . SER A 219 ? 0.4622 0.3450 0.5397 0.0018  -0.0806 0.0252  218 SER A N   
1584 C CA  . SER A 219 ? 0.4766 0.3513 0.5564 -0.0062 -0.0812 0.0290  218 SER A CA  
1585 C C   . SER A 219 ? 0.4804 0.3482 0.5636 -0.0084 -0.0823 0.0191  218 SER A C   
1586 O O   . SER A 219 ? 0.4919 0.3594 0.5771 -0.0159 -0.0823 0.0192  218 SER A O   
1587 C CB  . SER A 219 ? 0.4562 0.3164 0.5385 -0.0064 -0.0841 0.0384  218 SER A CB  
1588 O OG  . SER A 219 ? 0.5927 0.4605 0.6702 -0.0038 -0.0833 0.0478  218 SER A OG  
1589 N N   . LYS A 220 ? 0.4002 0.2634 0.4842 -0.0017 -0.0834 0.0102  219 LYS A N   
1590 C CA  . LYS A 220 ? 0.4626 0.3212 0.5478 -0.0027 -0.0844 -0.0004 219 LYS A CA  
1591 C C   . LYS A 220 ? 0.4505 0.3237 0.5321 -0.0066 -0.0816 -0.0038 219 LYS A C   
1592 O O   . LYS A 220 ? 0.4366 0.3078 0.5191 -0.0112 -0.0829 -0.0089 219 LYS A O   
1593 C CB  . LYS A 220 ? 0.4327 0.2877 0.5181 0.0064  -0.0848 -0.0093 219 LYS A CB  
1594 C CG  . LYS A 220 ? 0.4767 0.3143 0.5670 0.0109  -0.0886 -0.0083 219 LYS A CG  
1595 C CD  . LYS A 220 ? 0.5004 0.3338 0.5917 0.0191  -0.0891 -0.0199 219 LYS A CD  
1596 C CE  . LYS A 220 ? 0.6426 0.4920 0.7315 0.0260  -0.0851 -0.0223 219 LYS A CE  
1597 N NZ  . LYS A 220 ? 0.6609 0.5068 0.7519 0.0353  -0.0851 -0.0319 219 LYS A NZ  
1598 N N   . PHE A 221 ? 0.3811 0.2689 0.4591 -0.0048 -0.0780 -0.0012 220 PHE A N   
1599 C CA  . PHE A 221 ? 0.4619 0.3629 0.5368 -0.0079 -0.0753 -0.0035 220 PHE A CA  
1600 C C   . PHE A 221 ? 0.4940 0.3989 0.5702 -0.0159 -0.0752 0.0032  220 PHE A C   
1601 O O   . PHE A 221 ? 0.4880 0.3993 0.5639 -0.0199 -0.0748 0.0003  220 PHE A O   
1602 C CB  . PHE A 221 ? 0.3597 0.2735 0.4319 -0.0031 -0.0718 -0.0037 220 PHE A CB  
1603 C CG  . PHE A 221 ? 0.4296 0.3425 0.5018 0.0041  -0.0710 -0.0106 220 PHE A CG  
1604 C CD1 . PHE A 221 ? 0.4141 0.3200 0.4891 0.0096  -0.0726 -0.0102 220 PHE A CD1 
1605 C CD2 . PHE A 221 ? 0.4242 0.3442 0.4939 0.0058  -0.0685 -0.0170 220 PHE A CD2 
1606 C CE1 . PHE A 221 ? 0.4456 0.3525 0.5219 0.0164  -0.0713 -0.0166 220 PHE A CE1 
1607 C CE2 . PHE A 221 ? 0.4242 0.3450 0.4941 0.0124  -0.0669 -0.0229 220 PHE A CE2 
1608 C CZ  . PHE A 221 ? 0.4499 0.3647 0.5236 0.0177  -0.0681 -0.0230 220 PHE A CZ  
1609 N N   . THR A 222 ? 0.4378 0.3397 0.5154 -0.0180 -0.0755 0.0124  221 THR A N   
1610 C CA  . THR A 222 ? 0.4719 0.3764 0.5521 -0.0260 -0.0751 0.0190  221 THR A CA  
1611 C C   . THR A 222 ? 0.4239 0.3182 0.5099 -0.0318 -0.0784 0.0154  221 THR A C   
1612 O O   . THR A 222 ? 0.4154 0.3165 0.5042 -0.0381 -0.0781 0.0151  221 THR A O   
1613 C CB  . THR A 222 ? 0.4639 0.3659 0.5439 -0.0268 -0.0746 0.0303  221 THR A CB  
1614 O OG1 . THR A 222 ? 0.4706 0.3833 0.5450 -0.0214 -0.0723 0.0325  221 THR A OG1 
1615 C CG2 . THR A 222 ? 0.4586 0.3652 0.5419 -0.0352 -0.0731 0.0379  221 THR A CG2 
1616 N N   . LEU A 223 ? 0.4061 0.2844 0.4948 -0.0295 -0.0818 0.0117  222 LEU A N   
1617 C CA  . LEU A 223 ? 0.4112 0.2781 0.5064 -0.0352 -0.0858 0.0073  222 LEU A CA  
1618 C C   . LEU A 223 ? 0.4513 0.3249 0.5446 -0.0353 -0.0868 -0.0041 222 LEU A C   
1619 O O   . LEU A 223 ? 0.4974 0.3705 0.5957 -0.0421 -0.0894 -0.0068 222 LEU A O   
1620 C CB  . LEU A 223 ? 0.4992 0.3463 0.5978 -0.0316 -0.0895 0.0053  222 LEU A CB  
1621 C CG  . LEU A 223 ? 0.5574 0.3961 0.6577 -0.0308 -0.0892 0.0174  222 LEU A CG  
1622 C CD1 . LEU A 223 ? 0.5988 0.4236 0.6993 -0.0221 -0.0918 0.0137  222 LEU A CD1 
1623 C CD2 . LEU A 223 ? 0.4860 0.3157 0.5943 -0.0402 -0.0907 0.0261  222 LEU A CD2 
1624 N N   . MET A 224 ? 0.4191 0.2996 0.5055 -0.0278 -0.0849 -0.0105 223 MET A N   
1625 C CA  . MET A 224 ? 0.5392 0.4283 0.6221 -0.0274 -0.0852 -0.0194 223 MET A CA  
1626 C C   . MET A 224 ? 0.4475 0.3518 0.5306 -0.0328 -0.0833 -0.0152 223 MET A C   
1627 O O   . MET A 224 ? 0.5013 0.4099 0.5857 -0.0367 -0.0857 -0.0201 223 MET A O   
1628 C CB  . MET A 224 ? 0.4719 0.3661 0.5476 -0.0185 -0.0825 -0.0253 223 MET A CB  
1629 C CG  . MET A 224 ? 0.5362 0.4179 0.6126 -0.0120 -0.0836 -0.0288 223 MET A CG  
1630 S SD  . MET A 224 ? 0.6748 0.5637 0.7449 -0.0016 -0.0799 -0.0357 223 MET A SD  
1631 C CE  . MET A 224 ? 0.4427 0.3486 0.5104 -0.0020 -0.0747 -0.0279 223 MET A CE  
1632 N N   . ALA A 225 ? 0.4210 0.3340 0.5030 -0.0327 -0.0794 -0.0066 224 ALA A N   
1633 C CA  . ALA A 225 ? 0.5183 0.4457 0.6013 -0.0371 -0.0774 -0.0025 224 ALA A CA  
1634 C C   . ALA A 225 ? 0.5620 0.4876 0.6534 -0.0462 -0.0799 0.0007  224 ALA A C   
1635 O O   . ALA A 225 ? 0.5172 0.4527 0.6113 -0.0503 -0.0807 -0.0012 224 ALA A O   
1636 C CB  . ALA A 225 ? 0.5236 0.4594 0.6039 -0.0348 -0.0730 0.0053  224 ALA A CB  
1637 N N   . LEU A 226 ? 0.4720 0.3850 0.5684 -0.0495 -0.0813 0.0058  225 LEU A N   
1638 C CA  . LEU A 226 ? 0.4944 0.4044 0.6008 -0.0590 -0.0834 0.0096  225 LEU A CA  
1639 C C   . LEU A 226 ? 0.5466 0.4519 0.6574 -0.0623 -0.0889 -0.0009 225 LEU A C   
1640 O O   . LEU A 226 ? 0.6107 0.5238 0.7285 -0.0694 -0.0905 -0.0012 225 LEU A O   
1641 C CB  . LEU A 226 ? 0.5122 0.4073 0.6227 -0.0611 -0.0839 0.0179  225 LEU A CB  
1642 C CG  . LEU A 226 ? 0.5843 0.4872 0.6955 -0.0640 -0.0793 0.0313  225 LEU A CG  
1643 C CD1 . LEU A 226 ? 0.5828 0.4698 0.6958 -0.0641 -0.0799 0.0398  225 LEU A CD1 
1644 C CD2 . LEU A 226 ? 0.6041 0.5180 0.7238 -0.0734 -0.0783 0.0353  225 LEU A CD2 
1645 N N   . ILE A 227 ? 0.5461 0.4394 0.6532 -0.0570 -0.0921 -0.0101 226 ILE A N   
1646 C CA  . ILE A 227 ? 0.5463 0.4349 0.6561 -0.0591 -0.0978 -0.0217 226 ILE A CA  
1647 C C   . ILE A 227 ? 0.5671 0.4733 0.6723 -0.0582 -0.0978 -0.0270 226 ILE A C   
1648 O O   . ILE A 227 ? 0.5567 0.4669 0.6675 -0.0640 -0.1021 -0.0319 226 ILE A O   
1649 C CB  . ILE A 227 ? 0.5740 0.4477 0.6790 -0.0518 -0.1004 -0.0309 226 ILE A CB  
1650 C CG1 . ILE A 227 ? 0.5155 0.3698 0.6272 -0.0532 -0.1018 -0.0260 226 ILE A CG1 
1651 C CG2 . ILE A 227 ? 0.5151 0.3867 0.6197 -0.0522 -0.1061 -0.0448 226 ILE A CG2 
1652 C CD1 . ILE A 227 ? 0.5270 0.3701 0.6330 -0.0434 -0.1018 -0.0309 226 ILE A CD1 
1653 N N   . THR A 228 ? 0.5303 0.4470 0.6260 -0.0511 -0.0932 -0.0259 227 THR A N   
1654 C CA  . THR A 228 ? 0.5620 0.4940 0.6525 -0.0490 -0.0931 -0.0303 227 THR A CA  
1655 C C   . THR A 228 ? 0.6290 0.5747 0.7266 -0.0558 -0.0928 -0.0247 227 THR A C   
1656 O O   . THR A 228 ? 0.6409 0.5963 0.7390 -0.0572 -0.0960 -0.0298 227 THR A O   
1657 C CB  . THR A 228 ? 0.6079 0.5465 0.6885 -0.0404 -0.0878 -0.0288 227 THR A CB  
1658 O OG1 . THR A 228 ? 0.6214 0.5536 0.6949 -0.0337 -0.0888 -0.0374 227 THR A OG1 
1659 C CG2 . THR A 228 ? 0.5482 0.5041 0.6259 -0.0395 -0.0857 -0.0271 227 THR A CG2 
1660 N N   . SER A 229 ? 0.6412 0.5887 0.7443 -0.0597 -0.0893 -0.0144 228 SER A N   
1661 C CA  . SER A 229 ? 0.7061 0.6682 0.8165 -0.0656 -0.0881 -0.0088 228 SER A CA  
1662 C C   . SER A 229 ? 0.6602 0.6210 0.7829 -0.0751 -0.0933 -0.0110 228 SER A C   
1663 O O   . SER A 229 ? 0.6395 0.6137 0.7704 -0.0807 -0.0924 -0.0064 228 SER A O   
1664 C CB  . SER A 229 ? 0.7187 0.6839 0.8303 -0.0665 -0.0823 0.0027  228 SER A CB  
1665 O OG  . SER A 229 ? 0.6997 0.6515 0.8170 -0.0713 -0.0829 0.0079  228 SER A OG  
1666 N N   . VAL A 230 ? 0.6244 0.5703 0.7495 -0.0771 -0.0988 -0.0184 229 VAL A N   
1667 C CA  . VAL A 230 ? 0.5574 0.5004 0.6960 -0.0870 -0.1045 -0.0212 229 VAL A CA  
1668 C C   . VAL A 230 ? 0.6090 0.5518 0.7453 -0.0856 -0.1118 -0.0353 229 VAL A C   
1669 O O   . VAL A 230 ? 0.6482 0.6040 0.7908 -0.0901 -0.1155 -0.0387 229 VAL A O   
1670 C CB  . VAL A 230 ? 0.5472 0.4706 0.6938 -0.0922 -0.1054 -0.0168 229 VAL A CB  
1671 C CG1 . VAL A 230 ? 0.5913 0.5071 0.7514 -0.1015 -0.1129 -0.0235 229 VAL A CG1 
1672 C CG2 . VAL A 230 ? 0.6256 0.5532 0.7770 -0.0962 -0.0990 -0.0017 229 VAL A CG2 
1673 N N   . THR A 231 ? 0.6421 0.5716 0.7693 -0.0789 -0.1138 -0.0437 230 THR A N   
1674 C CA  . THR A 231 ? 0.7016 0.6266 0.8270 -0.0781 -0.1215 -0.0582 230 THR A CA  
1675 C C   . THR A 231 ? 0.6810 0.6249 0.8017 -0.0762 -0.1242 -0.0640 230 THR A C   
1676 O O   . THR A 231 ? 0.7267 0.6764 0.8567 -0.0830 -0.1307 -0.0692 230 THR A O   
1677 C CB  . THR A 231 ? 0.6199 0.5317 0.7333 -0.0686 -0.1211 -0.0655 230 THR A CB  
1678 O OG1 . THR A 231 ? 0.6844 0.6078 0.7842 -0.0594 -0.1157 -0.0638 230 THR A OG1 
1679 C CG2 . THR A 231 ? 0.5853 0.4789 0.7027 -0.0689 -0.1185 -0.0592 230 THR A CG2 
1680 N N   . LEU A 232 ? 0.5718 0.5253 0.6789 -0.0671 -0.1198 -0.0630 231 LEU A N   
1681 C CA  . LEU A 232 ? 0.6640 0.6349 0.7654 -0.0641 -0.1224 -0.0675 231 LEU A CA  
1682 C C   . LEU A 232 ? 0.6553 0.6432 0.7666 -0.0697 -0.1215 -0.0596 231 LEU A C   
1683 O O   . LEU A 232 ? 0.5855 0.5858 0.6998 -0.0717 -0.1271 -0.0647 231 LEU A O   
1684 C CB  . LEU A 232 ? 0.6715 0.6468 0.7563 -0.0528 -0.1175 -0.0675 231 LEU A CB  
1685 C CG  . LEU A 232 ? 0.7291 0.6928 0.8032 -0.0462 -0.1193 -0.0779 231 LEU A CG  
1686 C CD1 . LEU A 232 ? 0.6686 0.6386 0.7276 -0.0359 -0.1136 -0.0765 231 LEU A CD1 
1687 C CD2 . LEU A 232 ? 0.6219 0.5857 0.6962 -0.0483 -0.1286 -0.0911 231 LEU A CD2 
1688 N N   . PRO A 233 ? 0.6277 0.6180 0.7442 -0.0719 -0.1148 -0.0477 232 PRO A N   
1689 C CA  . PRO A 233 ? 0.4944 0.5009 0.6228 -0.0781 -0.1142 -0.0411 232 PRO A CA  
1690 C C   . PRO A 233 ? 0.6091 0.6163 0.7533 -0.0888 -0.1212 -0.0452 232 PRO A C   
1691 O O   . PRO A 233 ? 0.5324 0.5562 0.6838 -0.0918 -0.1249 -0.0469 232 PRO A O   
1692 C CB  . PRO A 233 ? 0.5696 0.5737 0.7003 -0.0790 -0.1061 -0.0290 232 PRO A CB  
1693 C CG  . PRO A 233 ? 0.6203 0.6150 0.7367 -0.0699 -0.1020 -0.0291 232 PRO A CG  
1694 C CD  . PRO A 233 ? 0.5882 0.5706 0.6983 -0.0671 -0.1073 -0.0402 232 PRO A CD  
1695 N N   . VAL A 234 ? 0.6272 0.6879 0.7534 -0.0424 -0.0052 0.0654  233 VAL A N   
1696 C CA  . VAL A 234 ? 0.5285 0.5928 0.6764 -0.0534 -0.0115 0.0749  233 VAL A CA  
1697 C C   . VAL A 234 ? 0.5129 0.5708 0.6726 -0.0546 -0.0258 0.0696  233 VAL A C   
1698 O O   . VAL A 234 ? 0.5239 0.5951 0.7094 -0.0610 -0.0299 0.0749  233 VAL A O   
1699 C CB  . VAL A 234 ? 0.5379 0.5855 0.6749 -0.0611 -0.0156 0.0823  233 VAL A CB  
1700 C CG1 . VAL A 234 ? 0.4969 0.5346 0.6497 -0.0714 -0.0288 0.0863  233 VAL A CG1 
1701 C CG2 . VAL A 234 ? 0.5311 0.5917 0.6667 -0.0651 -0.0024 0.0935  233 VAL A CG2 
1702 N N   . ALA A 235 ? 0.5182 0.5565 0.6590 -0.0489 -0.0338 0.0595  234 ALA A N   
1703 C CA  . ALA A 235 ? 0.5763 0.6054 0.7217 -0.0503 -0.0477 0.0541  234 ALA A CA  
1704 C C   . ALA A 235 ? 0.5534 0.6021 0.7182 -0.0464 -0.0474 0.0533  234 ALA A C   
1705 O O   . ALA A 235 ? 0.5296 0.5842 0.7137 -0.0526 -0.0576 0.0564  234 ALA A O   
1706 C CB  . ALA A 235 ? 0.6477 0.6535 0.7670 -0.0439 -0.0531 0.0436  234 ALA A CB  
1707 N N   . TYR A 236 ? 0.5063 0.5648 0.6670 -0.0362 -0.0363 0.0494  235 TYR A N   
1708 C CA  . TYR A 236 ? 0.5333 0.6095 0.7139 -0.0306 -0.0350 0.0489  235 TYR A CA  
1709 C C   . TYR A 236 ? 0.5088 0.6120 0.7215 -0.0352 -0.0283 0.0590  235 TYR A C   
1710 O O   . TYR A 236 ? 0.4504 0.5695 0.6884 -0.0338 -0.0324 0.0615  235 TYR A O   
1711 C CB  . TYR A 236 ? 0.5580 0.6340 0.7249 -0.0184 -0.0245 0.0412  235 TYR A CB  
1712 C CG  . TYR A 236 ? 0.6397 0.6928 0.7814 -0.0141 -0.0322 0.0320  235 TYR A CG  
1713 C CD1 . TYR A 236 ? 0.6373 0.6856 0.7817 -0.0111 -0.0425 0.0288  235 TYR A CD1 
1714 C CD2 . TYR A 236 ? 0.6152 0.6527 0.7314 -0.0133 -0.0293 0.0277  235 TYR A CD2 
1715 C CE1 . TYR A 236 ? 0.6195 0.6478 0.7406 -0.0078 -0.0480 0.0214  235 TYR A CE1 
1716 C CE2 . TYR A 236 ? 0.6549 0.6742 0.7512 -0.0096 -0.0349 0.0201  235 TYR A CE2 
1717 C CZ  . TYR A 236 ? 0.6061 0.6207 0.7042 -0.0071 -0.0435 0.0169  235 TYR A CZ  
1718 O OH  . TYR A 236 ? 0.7216 0.7189 0.7994 -0.0040 -0.0476 0.0102  235 TYR A OH  
1719 N N   . ILE A 237 ? 0.5278 0.6372 0.7411 -0.0411 -0.0185 0.0661  236 ILE A N   
1720 C CA  . ILE A 237 ? 0.4287 0.5652 0.6730 -0.0464 -0.0102 0.0768  236 ILE A CA  
1721 C C   . ILE A 237 ? 0.4876 0.6282 0.7572 -0.0583 -0.0257 0.0838  236 ILE A C   
1722 O O   . ILE A 237 ? 0.6087 0.7726 0.9111 -0.0592 -0.0268 0.0890  236 ILE A O   
1723 C CB  . ILE A 237 ? 0.4905 0.6307 0.7252 -0.0508 0.0040  0.0836  236 ILE A CB  
1724 C CG1 . ILE A 237 ? 0.5768 0.7277 0.8011 -0.0398 0.0230  0.0791  236 ILE A CG1 
1725 C CG2 . ILE A 237 ? 0.4474 0.6075 0.7125 -0.0629 0.0064  0.0975  236 ILE A CG2 
1726 C CD1 . ILE A 237 ? 0.6095 0.7639 0.8194 -0.0440 0.0372  0.0858  236 ILE A CD1 
1727 N N   . MET A 238 ? 0.4927 0.6105 0.7485 -0.0676 -0.0381 0.0840  237 MET A N   
1728 C CA  . MET A 238 ? 0.5469 0.6650 0.8236 -0.0800 -0.0545 0.0891  237 MET A CA  
1729 C C   . MET A 238 ? 0.5225 0.6304 0.7958 -0.0770 -0.0714 0.0810  237 MET A C   
1730 O O   . MET A 238 ? 0.5166 0.6262 0.8073 -0.0870 -0.0869 0.0843  237 MET A O   
1731 C CB  . MET A 238 ? 0.6870 0.7836 0.9522 -0.0921 -0.0608 0.0930  237 MET A CB  
1732 C CG  . MET A 238 ? 0.6441 0.7074 0.8726 -0.0876 -0.0658 0.0831  237 MET A CG  
1733 S SD  . MET A 238 ? 0.7930 0.8278 1.0130 -0.1014 -0.0766 0.0870  237 MET A SD  
1734 C CE  . MET A 238 ? 0.4609 0.4767 0.6478 -0.0923 -0.0661 0.0839  237 MET A CE  
1735 N N   . MET A 239 ? 0.5026 0.6003 0.7539 -0.0645 -0.0693 0.0710  238 MET A N   
1736 C CA  . MET A 239 ? 0.5055 0.6016 0.7591 -0.0603 -0.0822 0.0661  238 MET A CA  
1737 C C   . MET A 239 ? 0.5298 0.6577 0.8200 -0.0566 -0.0793 0.0728  238 MET A C   
1738 O O   . MET A 239 ? 0.5305 0.6662 0.8402 -0.0610 -0.0946 0.0760  238 MET A O   
1739 C CB  . MET A 239 ? 0.4834 0.5611 0.7056 -0.0483 -0.0792 0.0552  238 MET A CB  
1740 C CG  . MET A 239 ? 0.5178 0.5661 0.7123 -0.0516 -0.0931 0.0476  238 MET A CG  
1741 S SD  . MET A 239 ? 0.5947 0.6243 0.7551 -0.0387 -0.0871 0.0364  238 MET A SD  
1742 C CE  . MET A 239 ? 0.5530 0.5810 0.7144 -0.0361 -0.1021 0.0342  238 MET A CE  
1743 N N   . ARG A 240 ? 0.5091 0.6558 0.8092 -0.0483 -0.0600 0.0749  239 ARG A N   
1744 C CA  . ARG A 240 ? 0.4867 0.6658 0.8257 -0.0439 -0.0541 0.0818  239 ARG A CA  
1745 C C   . ARG A 240 ? 0.4565 0.6565 0.8308 -0.0579 -0.0597 0.0939  239 ARG A C   
1746 O O   . ARG A 240 ? 0.4558 0.6798 0.8662 -0.0581 -0.0659 0.1003  239 ARG A O   
1747 C CB  . ARG A 240 ? 0.4306 0.6226 0.7688 -0.0327 -0.0300 0.0803  239 ARG A CB  
1748 C CG  . ARG A 240 ? 0.4869 0.7148 0.8674 -0.0286 -0.0186 0.0883  239 ARG A CG  
1749 C CD  . ARG A 240 ? 0.5422 0.7780 0.9150 -0.0165 0.0060  0.0839  239 ARG A CD  
1750 N NE  . ARG A 240 ? 0.6453 0.8711 0.9914 -0.0222 0.0176  0.0839  239 ARG A NE  
1751 C CZ  . ARG A 240 ? 0.6556 0.8953 1.0147 -0.0333 0.0242  0.0943  239 ARG A CZ  
1752 N NH1 . ARG A 240 ? 0.6491 0.9147 1.0494 -0.0408 0.0214  0.1054  239 ARG A NH1 
1753 N NH2 . ARG A 240 ? 0.6811 0.9088 1.0119 -0.0376 0.0335  0.0946  239 ARG A NH2 
1754 N N   . LYS A 241 ? 0.4673 0.6584 0.8333 -0.0701 -0.0586 0.0980  240 LYS A N   
1755 C CA  . LYS A 241 ? 0.4701 0.6775 0.8684 -0.0858 -0.0653 0.1098  240 LYS A CA  
1756 C C   . LYS A 241 ? 0.5045 0.7054 0.9128 -0.0946 -0.0913 0.1096  240 LYS A C   
1757 O O   . LYS A 241 ? 0.5040 0.7309 0.9519 -0.1009 -0.0990 0.1185  240 LYS A O   
1758 C CB  . LYS A 241 ? 0.5868 0.7787 0.9686 -0.0968 -0.0605 0.1137  240 LYS A CB  
1759 C CG  . LYS A 241 ? 0.5950 0.8094 1.0115 -0.1117 -0.0574 0.1285  240 LYS A CG  
1760 C CD  . LYS A 241 ? 0.6901 0.8967 1.1218 -0.1281 -0.0814 0.1319  240 LYS A CD  
1761 C CE  . LYS A 241 ? 0.6922 0.8555 1.0839 -0.1321 -0.0956 0.1222  240 LYS A CE  
1762 N NZ  . LYS A 241 ? 0.7129 0.8647 1.1120 -0.1444 -0.1210 0.1205  240 LYS A NZ  
1763 N N   . LEU A 242 ? 0.4991 0.6657 0.8714 -0.0954 -0.1051 0.0995  241 LEU A N   
1764 C CA  . LEU A 242 ? 0.4984 0.6547 0.8719 -0.1032 -0.1300 0.0973  241 LEU A CA  
1765 C C   . LEU A 242 ? 0.4948 0.6733 0.8917 -0.0947 -0.1364 0.0993  241 LEU A C   
1766 O O   . LEU A 242 ? 0.5280 0.7183 0.9496 -0.1036 -0.1549 0.1049  241 LEU A O   
1767 C CB  . LEU A 242 ? 0.5063 0.6224 0.8328 -0.1017 -0.1389 0.0845  241 LEU A CB  
1768 C CG  . LEU A 242 ? 0.5300 0.6173 0.8357 -0.1140 -0.1451 0.0818  241 LEU A CG  
1769 C CD1 . LEU A 242 ? 0.6202 0.6763 0.8820 -0.1048 -0.1389 0.0701  241 LEU A CD1 
1770 C CD2 . LEU A 242 ? 0.6001 0.6760 0.9091 -0.1282 -0.1697 0.0809  241 LEU A CD2 
1771 N N   . LEU A 243 ? 0.4415 0.6247 0.8309 -0.0776 -0.1224 0.0950  242 LEU A N   
1772 C CA  . LEU A 243 ? 0.4201 0.6222 0.8316 -0.0673 -0.1272 0.0972  242 LEU A CA  
1773 C C   . LEU A 243 ? 0.5072 0.7502 0.9734 -0.0702 -0.1243 0.1102  242 LEU A C   
1774 O O   . LEU A 243 ? 0.5306 0.7895 1.0248 -0.0731 -0.1416 0.1163  242 LEU A O   
1775 C CB  . LEU A 243 ? 0.4743 0.6710 0.8672 -0.0490 -0.1101 0.0898  242 LEU A CB  
1776 C CG  . LEU A 243 ? 0.5129 0.6839 0.8729 -0.0411 -0.1203 0.0808  242 LEU A CG  
1777 C CD1 . LEU A 243 ? 0.5592 0.7366 0.9208 -0.0233 -0.1055 0.0777  242 LEU A CD1 
1778 C CD2 . LEU A 243 ? 0.4941 0.6651 0.8635 -0.0476 -0.1460 0.0845  242 LEU A CD2 
1779 N N   . ALA A 244 ? 0.4962 0.7578 0.9786 -0.0695 -0.1025 0.1151  243 ALA A N   
1780 C CA  . ALA A 244 ? 0.4750 0.7785 1.0113 -0.0710 -0.0957 0.1276  243 ALA A CA  
1781 C C   . ALA A 244 ? 0.4971 0.8117 1.0614 -0.0913 -0.1143 0.1377  243 ALA A C   
1782 O O   . ALA A 244 ? 0.5364 0.8858 1.1498 -0.0939 -0.1186 0.1486  243 ALA A O   
1783 C CB  . ALA A 244 ? 0.4445 0.7633 0.9858 -0.0659 -0.0661 0.1300  243 ALA A CB  
1784 N N   . ALA A 245 ? 0.4949 0.7800 1.0302 -0.1057 -0.1257 0.1342  244 ALA A N   
1785 C CA  . ALA A 245 ? 0.5254 0.8168 1.0848 -0.1267 -0.1429 0.1430  244 ALA A CA  
1786 C C   . ALA A 245 ? 0.5792 0.8796 1.1601 -0.1316 -0.1702 0.1457  244 ALA A C   
1787 O O   . ALA A 245 ? 0.5908 0.9141 1.2117 -0.1464 -0.1826 0.1566  244 ALA A O   
1788 C CB  . ALA A 245 ? 0.5511 0.8028 1.0705 -0.1391 -0.1498 0.1366  244 ALA A CB  
1789 N N   . GLN A 246 ? 0.5399 0.8232 1.0952 -0.1203 -0.1805 0.1368  245 GLN A N   
1790 C CA  . GLN A 246 ? 0.5622 0.8496 1.1300 -0.1251 -0.2083 0.1392  245 GLN A CA  
1791 C C   . GLN A 246 ? 0.5785 0.8836 1.1614 -0.1065 -0.2074 0.1407  245 GLN A C   
1792 O O   . GLN A 246 ? 0.6017 0.9112 1.1947 -0.1088 -0.2312 0.1440  245 GLN A O   
1793 C CB  . GLN A 246 ? 0.6569 0.8998 1.1735 -0.1332 -0.2287 0.1275  245 GLN A CB  
1794 C CG  . GLN A 246 ? 0.8389 1.0631 1.3465 -0.1541 -0.2382 0.1267  245 GLN A CG  
1795 C CD  . GLN A 246 ? 0.9200 1.1077 1.3889 -0.1639 -0.2641 0.1167  245 GLN A CD  
1796 O OE1 . GLN A 246 ? 0.8788 1.0656 1.3414 -0.1602 -0.2813 0.1152  245 GLN A OE1 
1797 N NE2 . GLN A 246 ? 0.9706 1.1267 1.4119 -0.1762 -0.2667 0.1100  245 GLN A NE2 
1798 N N   . TYR A 247 ? 0.5771 0.8906 1.1603 -0.0884 -0.1817 0.1385  246 TYR A N   
1799 C CA  . TYR A 247 ? 0.5301 0.8551 1.1247 -0.0696 -0.1796 0.1389  246 TYR A CA  
1800 C C   . TYR A 247 ? 0.5838 0.9414 1.2143 -0.0561 -0.1517 0.1439  246 TYR A C   
1801 O O   . TYR A 247 ? 0.5336 0.9030 1.1742 -0.0614 -0.1332 0.1466  246 TYR A O   
1802 C CB  . TYR A 247 ? 0.5065 0.7932 1.0463 -0.0587 -0.1791 0.1258  246 TYR A CB  
1803 C CG  . TYR A 247 ? 0.6186 0.8746 1.1229 -0.0697 -0.2059 0.1207  246 TYR A CG  
1804 C CD1 . TYR A 247 ? 0.5844 0.8102 1.0511 -0.0825 -0.2089 0.1126  246 TYR A CD1 
1805 C CD2 . TYR A 247 ? 0.6430 0.8994 1.1505 -0.0671 -0.2279 0.1240  246 TYR A CD2 
1806 C CE1 . TYR A 247 ? 0.5626 0.7592 0.9949 -0.0920 -0.2316 0.1066  246 TYR A CE1 
1807 C CE2 . TYR A 247 ? 0.6514 0.8790 1.1223 -0.0775 -0.2516 0.1188  246 TYR A CE2 
1808 C CZ  . TYR A 247 ? 0.6096 0.8072 1.0426 -0.0898 -0.2526 0.1094  246 TYR A CZ  
1809 O OH  . TYR A 247 ? 0.5863 0.7541 0.9811 -0.0996 -0.2746 0.1029  246 TYR A OH  
1810 N N   . SER A 248 ? 0.5851 0.9560 1.2338 -0.0384 -0.1486 0.1453  247 SER A N   
1811 C CA  . SER A 248 ? 0.5897 0.9909 1.2737 -0.0231 -0.1224 0.1489  247 SER A CA  
1812 C C   . SER A 248 ? 0.6008 0.9796 1.2445 -0.0115 -0.0961 0.1365  247 SER A C   
1813 O O   . SER A 248 ? 0.6288 0.9703 1.2208 -0.0127 -0.0996 0.1258  247 SER A O   
1814 C CB  . SER A 248 ? 0.6333 1.0544 1.3525 -0.0074 -0.1300 0.1548  247 SER A CB  
1815 O OG  . SER A 248 ? 0.5610 0.9495 1.2402 0.0041  -0.1361 0.1457  247 SER A OG  
1816 N N   . TRP A 249 ? 0.6079 1.0110 1.2764 -0.0002 -0.0692 0.1379  248 TRP A N   
1817 C CA  . TRP A 249 ? 0.6745 1.0588 1.3075 0.0122  -0.0445 0.1260  248 TRP A CA  
1818 C C   . TRP A 249 ? 0.6484 1.0101 1.2594 0.0288  -0.0478 0.1172  248 TRP A C   
1819 O O   . TRP A 249 ? 0.5493 0.8834 1.1174 0.0349  -0.0361 0.1054  248 TRP A O   
1820 C CB  . TRP A 249 ? 0.6768 1.0928 1.3413 0.0204  -0.0148 0.1294  248 TRP A CB  
1821 C CG  . TRP A 249 ? 0.7963 1.2310 1.4752 0.0038  -0.0069 0.1378  248 TRP A CG  
1822 C CD1 . TRP A 249 ? 0.8406 1.3173 1.5745 -0.0011 -0.0010 0.1512  248 TRP A CD1 
1823 C CD2 . TRP A 249 ? 0.8222 1.2344 1.4616 -0.0102 -0.0038 0.1346  248 TRP A CD2 
1824 N NE1 . TRP A 249 ? 0.8811 1.3616 1.6105 -0.0183 0.0056  0.1568  248 TRP A NE1 
1825 C CE2 . TRP A 249 ? 0.8591 1.2995 1.5305 -0.0237 0.0037  0.1469  248 TRP A CE2 
1826 C CE3 . TRP A 249 ? 0.8442 1.2158 1.4263 -0.0125 -0.0067 0.1235  248 TRP A CE3 
1827 C CZ2 . TRP A 249 ? 0.8166 1.2435 1.4629 -0.0392 0.0077  0.1486  248 TRP A CZ2 
1828 C CZ3 . TRP A 249 ? 0.8090 1.1690 1.3682 -0.0268 -0.0028 0.1249  248 TRP A CZ3 
1829 C CH2 . TRP A 249 ? 0.7955 1.1817 1.3857 -0.0399 0.0040  0.1375  248 TRP A CH2 
1830 N N   . ASP A 250 ? 0.4738 0.8468 1.1138 0.0357  -0.0643 0.1236  249 ASP A N   
1831 C CA  . ASP A 250 ? 0.5604 0.9101 1.1797 0.0502  -0.0699 0.1172  249 ASP A CA  
1832 C C   . ASP A 250 ? 0.5329 0.8413 1.0954 0.0416  -0.0844 0.1087  249 ASP A C   
1833 O O   . ASP A 250 ? 0.4777 0.7589 1.0033 0.0502  -0.0754 0.0981  249 ASP A O   
1834 C CB  . ASP A 250 ? 0.5469 0.9169 1.2089 0.0570  -0.0885 0.1283  249 ASP A CB  
1835 C CG  . ASP A 250 ? 0.7061 1.0974 1.4058 0.0785  -0.0698 0.1298  249 ASP A CG  
1836 O OD1 . ASP A 250 ? 0.7313 1.1283 1.4551 0.0895  -0.0831 0.1362  249 ASP A OD1 
1837 O OD2 . ASP A 250 ? 0.7354 1.1365 1.4392 0.0848  -0.0417 0.1245  249 ASP A OD2 
1838 N N   . GLU A 251 ? 0.5501 0.8535 1.1054 0.0244  -0.1066 0.1129  250 GLU A N   
1839 C CA  . GLU A 251 ? 0.6078 0.8730 1.1097 0.0159  -0.1186 0.1044  250 GLU A CA  
1840 C C   . GLU A 251 ? 0.4908 0.7373 0.9566 0.0137  -0.0991 0.0942  250 GLU A C   
1841 O O   . GLU A 251 ? 0.5001 0.7154 0.9223 0.0156  -0.0988 0.0846  250 GLU A O   
1842 C CB  . GLU A 251 ? 0.5874 0.8512 1.0898 -0.0025 -0.1443 0.1100  250 GLU A CB  
1843 C CG  . GLU A 251 ? 0.5727 0.7981 1.0235 -0.0087 -0.1597 0.1020  250 GLU A CG  
1844 C CD  . GLU A 251 ? 0.5096 0.7339 0.9647 -0.0164 -0.1894 0.1084  250 GLU A CD  
1845 O OE1 . GLU A 251 ? 0.5945 0.8479 1.0942 -0.0139 -0.1989 0.1196  250 GLU A OE1 
1846 O OE2 . GLU A 251 ? 0.4832 0.6780 0.8970 -0.0248 -0.2033 0.1023  250 GLU A OE2 
1847 N N   . VAL A 252 ? 0.4913 0.7575 0.9754 0.0093  -0.0828 0.0970  251 VAL A N   
1848 C CA  . VAL A 252 ? 0.5358 0.7867 0.9876 0.0078  -0.0642 0.0889  251 VAL A CA  
1849 C C   . VAL A 252 ? 0.4735 0.7124 0.9059 0.0244  -0.0470 0.0793  251 VAL A C   
1850 O O   . VAL A 252 ? 0.4744 0.6862 0.8653 0.0247  -0.0424 0.0697  251 VAL A O   
1851 C CB  . VAL A 252 ? 0.5891 0.8661 1.0668 0.0004  -0.0495 0.0959  251 VAL A CB  
1852 C CG1 . VAL A 252 ? 0.5565 0.8245 1.0073 0.0050  -0.0251 0.0886  251 VAL A CG1 
1853 C CG2 . VAL A 252 ? 0.5751 0.8503 1.0549 -0.0194 -0.0657 0.1022  251 VAL A CG2 
1854 N N   . GLY A 253 ? 0.4530 0.7116 0.9167 0.0385  -0.0376 0.0817  252 GLY A N   
1855 C CA  . GLY A 253 ? 0.4633 0.7083 0.9097 0.0543  -0.0221 0.0719  252 GLY A CA  
1856 C C   . GLY A 253 ? 0.5322 0.7457 0.9465 0.0578  -0.0362 0.0659  252 GLY A C   
1857 O O   . GLY A 253 ? 0.5184 0.7089 0.8996 0.0633  -0.0264 0.0556  252 GLY A O   
1858 N N   . ILE A 254 ? 0.5463 0.7585 0.9693 0.0538  -0.0594 0.0726  253 ILE A N   
1859 C CA  . ILE A 254 ? 0.5878 0.7703 0.9786 0.0555  -0.0732 0.0684  253 ILE A CA  
1860 C C   . ILE A 254 ? 0.4911 0.6461 0.8346 0.0464  -0.0719 0.0593  253 ILE A C   
1861 O O   . ILE A 254 ? 0.5484 0.6794 0.8611 0.0516  -0.0673 0.0512  253 ILE A O   
1862 C CB  . ILE A 254 ? 0.5773 0.7639 0.9820 0.0500  -0.0997 0.0781  253 ILE A CB  
1863 C CG1 . ILE A 254 ? 0.6174 0.8145 1.0519 0.0645  -0.1044 0.0847  253 ILE A CG1 
1864 C CG2 . ILE A 254 ? 0.5683 0.7232 0.9282 0.0415  -0.1152 0.0737  253 ILE A CG2 
1865 C CD1 . ILE A 254 ? 0.6789 0.9112 1.1645 0.0734  -0.0917 0.0909  253 ILE A CD1 
1866 N N   . TRP A 255 ? 0.5067 0.6649 0.8459 0.0325  -0.0756 0.0610  254 TRP A N   
1867 C CA  . TRP A 255 ? 0.5141 0.6471 0.8121 0.0243  -0.0752 0.0533  254 TRP A CA  
1868 C C   . TRP A 255 ? 0.4925 0.6205 0.7739 0.0296  -0.0535 0.0455  254 TRP A C   
1869 O O   . TRP A 255 ? 0.4645 0.5691 0.7121 0.0310  -0.0510 0.0374  254 TRP A O   
1870 C CB  . TRP A 255 ? 0.4946 0.6313 0.7953 0.0087  -0.0851 0.0575  254 TRP A CB  
1871 C CG  . TRP A 255 ? 0.4722 0.5919 0.7424 0.0019  -0.0776 0.0513  254 TRP A CG  
1872 C CD1 . TRP A 255 ? 0.4552 0.5849 0.7319 -0.0041 -0.0665 0.0536  254 TRP A CD1 
1873 C CD2 . TRP A 255 ? 0.4180 0.5085 0.6482 0.0006  -0.0809 0.0430  254 TRP A CD2 
1874 N NE1 . TRP A 255 ? 0.4871 0.5949 0.7306 -0.0085 -0.0639 0.0475  254 TRP A NE1 
1875 C CE2 . TRP A 255 ? 0.5297 0.6143 0.7458 -0.0054 -0.0722 0.0406  254 TRP A CE2 
1876 C CE3 . TRP A 255 ? 0.5321 0.6018 0.7379 0.0039  -0.0897 0.0382  254 TRP A CE3 
1877 C CZ2 . TRP A 255 ? 0.5986 0.6586 0.7801 -0.0072 -0.0723 0.0333  254 TRP A CZ2 
1878 C CZ3 . TRP A 255 ? 0.5674 0.6132 0.7380 0.0015  -0.0884 0.0306  254 TRP A CZ3 
1879 C CH2 . TRP A 255 ? 0.6239 0.6657 0.7842 -0.0035 -0.0799 0.0280  254 TRP A CH2 
1880 N N   . GLN A 256 ? 0.4383 0.5885 0.7428 0.0322  -0.0378 0.0481  255 GLN A N   
1881 C CA  . GLN A 256 ? 0.5068 0.6525 0.7933 0.0368  -0.0176 0.0407  255 GLN A CA  
1882 C C   . GLN A 256 ? 0.4860 0.6164 0.7575 0.0496  -0.0110 0.0321  255 GLN A C   
1883 O O   . GLN A 256 ? 0.4810 0.5933 0.7214 0.0502  -0.0035 0.0236  255 GLN A O   
1884 C CB  . GLN A 256 ? 0.5247 0.6985 0.8396 0.0380  -0.0011 0.0457  255 GLN A CB  
1885 C CG  . GLN A 256 ? 0.5734 0.7594 0.8984 0.0236  -0.0047 0.0540  255 GLN A CG  
1886 C CD  . GLN A 256 ? 0.6379 0.8358 0.9613 0.0220  0.0159  0.0548  255 GLN A CD  
1887 O OE1 . GLN A 256 ? 0.5401 0.7656 0.8958 0.0218  0.0258  0.0623  255 GLN A OE1 
1888 N NE2 . GLN A 256 ? 0.6480 0.8261 0.9340 0.0207  0.0224  0.0477  255 GLN A NE2 
1889 N N   . GLY A 257 ? 0.4873 0.6243 0.7819 0.0595  -0.0147 0.0348  256 GLY A N   
1890 C CA  . GLY A 257 ? 0.5031 0.6219 0.7839 0.0710  -0.0106 0.0274  256 GLY A CA  
1891 C C   . GLY A 257 ? 0.5207 0.6108 0.7658 0.0662  -0.0224 0.0230  256 GLY A C   
1892 O O   . GLY A 257 ? 0.6025 0.6739 0.8222 0.0695  -0.0147 0.0143  256 GLY A O   
1893 N N   . VAL A 258 ? 0.5390 0.6254 0.7814 0.0577  -0.0408 0.0288  257 VAL A N   
1894 C CA  . VAL A 258 ? 0.5076 0.5681 0.7156 0.0527  -0.0504 0.0249  257 VAL A CA  
1895 C C   . VAL A 258 ? 0.5157 0.5654 0.6959 0.0466  -0.0414 0.0174  257 VAL A C   
1896 O O   . VAL A 258 ? 0.5827 0.6136 0.7375 0.0483  -0.0378 0.0106  257 VAL A O   
1897 C CB  . VAL A 258 ? 0.5507 0.6096 0.7584 0.0439  -0.0708 0.0315  257 VAL A CB  
1898 C CG1 . VAL A 258 ? 0.5336 0.5665 0.7038 0.0385  -0.0775 0.0266  257 VAL A CG1 
1899 C CG2 . VAL A 258 ? 0.7078 0.7746 0.9389 0.0498  -0.0825 0.0395  257 VAL A CG2 
1900 N N   . SER A 259 ? 0.4943 0.5561 0.6803 0.0391  -0.0383 0.0196  258 SER A N   
1901 C CA  . SER A 259 ? 0.5854 0.6372 0.7463 0.0331  -0.0320 0.0145  258 SER A CA  
1902 C C   . SER A 259 ? 0.5841 0.6322 0.7331 0.0397  -0.0161 0.0071  258 SER A C   
1903 O O   . SER A 259 ? 0.5543 0.5858 0.6771 0.0383  -0.0146 0.0009  258 SER A O   
1904 C CB  . SER A 259 ? 0.5064 0.5719 0.6783 0.0241  -0.0316 0.0200  258 SER A CB  
1905 O OG  . SER A 259 ? 0.6015 0.6755 0.7931 0.0187  -0.0454 0.0273  258 SER A OG  
1906 N N   . SER A 260 ? 0.5904 0.6537 0.7585 0.0469  -0.0041 0.0072  259 SER A N   
1907 C CA  . SER A 260 ? 0.5576 0.6161 0.7115 0.0524  0.0114  -0.0011 259 SER A CA  
1908 C C   . SER A 260 ? 0.5656 0.6032 0.7033 0.0585  0.0099  -0.0085 259 SER A C   
1909 O O   . SER A 260 ? 0.5761 0.6003 0.6893 0.0574  0.0152  -0.0161 259 SER A O   
1910 C CB  . SER A 260 ? 0.5594 0.6385 0.7372 0.0595  0.0261  0.0000  259 SER A CB  
1911 O OG  . SER A 260 ? 0.6669 0.7431 0.8562 0.0717  0.0301  -0.0038 259 SER A OG  
1912 N N   . ILE A 261 ? 0.4909 0.5250 0.6417 0.0641  0.0015  -0.0055 260 ILE A N   
1913 C CA  . ILE A 261 ? 0.5156 0.5281 0.6510 0.0688  -0.0006 -0.0109 260 ILE A CA  
1914 C C   . ILE A 261 ? 0.6124 0.6082 0.7220 0.0602  -0.0105 -0.0117 260 ILE A C   
1915 O O   . ILE A 261 ? 0.5975 0.5760 0.6874 0.0604  -0.0086 -0.0178 260 ILE A O   
1916 C CB  . ILE A 261 ? 0.6222 0.6350 0.7793 0.0778  -0.0068 -0.0060 260 ILE A CB  
1917 C CG1 . ILE A 261 ? 0.5815 0.5711 0.7242 0.0837  -0.0052 -0.0120 260 ILE A CG1 
1918 C CG2 . ILE A 261 ? 0.6425 0.6574 0.8056 0.0723  -0.0246 0.0035  260 ILE A CG2 
1919 C CD1 . ILE A 261 ? 0.6689 0.6596 0.8345 0.0970  -0.0005 -0.0116 260 ILE A CD1 
1920 N N   . SER A 262 ? 0.5705 0.5711 0.6800 0.0523  -0.0205 -0.0060 261 SER A N   
1921 C CA  . SER A 262 ? 0.5990 0.5845 0.6843 0.0450  -0.0277 -0.0075 261 SER A CA  
1922 C C   . SER A 262 ? 0.5845 0.5670 0.6523 0.0408  -0.0196 -0.0133 261 SER A C   
1923 O O   . SER A 262 ? 0.5423 0.5110 0.5906 0.0383  -0.0204 -0.0173 261 SER A O   
1924 C CB  . SER A 262 ? 0.5547 0.5439 0.6437 0.0382  -0.0402 -0.0012 261 SER A CB  
1925 O OG  . SER A 262 ? 0.6054 0.5828 0.6721 0.0314  -0.0433 -0.0038 261 SER A OG  
1926 N N   . ASP A 263 ? 0.5660 0.5623 0.6412 0.0396  -0.0119 -0.0128 262 ASP A N   
1927 C CA  . ASP A 263 ? 0.6220 0.6162 0.6803 0.0359  -0.0049 -0.0171 262 ASP A CA  
1928 C C   . ASP A 263 ? 0.6254 0.6098 0.6709 0.0403  0.0026  -0.0253 262 ASP A C   
1929 O O   . ASP A 263 ? 0.5049 0.4800 0.5319 0.0365  0.0025  -0.0294 262 ASP A O   
1930 C CB  . ASP A 263 ? 0.6186 0.6295 0.6866 0.0337  0.0022  -0.0134 262 ASP A CB  
1931 C CG  . ASP A 263 ? 0.7650 0.7825 0.8427 0.0269  -0.0060 -0.0057 262 ASP A CG  
1932 O OD1 . ASP A 263 ? 0.8705 0.8768 0.9395 0.0231  -0.0162 -0.0053 262 ASP A OD1 
1933 O OD2 . ASP A 263 ? 0.8624 0.8956 0.9561 0.0250  -0.0019 -0.0003 262 ASP A OD2 
1934 N N   . ALA A 264 ? 0.5524 0.5386 0.6088 0.0481  0.0091  -0.0279 263 ALA A N   
1935 C CA  . ALA A 264 ? 0.5793 0.5523 0.6231 0.0521  0.0155  -0.0368 263 ALA A CA  
1936 C C   . ALA A 264 ? 0.5793 0.5342 0.6120 0.0503  0.0072  -0.0381 263 ALA A C   
1937 O O   . ALA A 264 ? 0.5505 0.4934 0.5665 0.0479  0.0091  -0.0445 263 ALA A O   
1938 C CB  . ALA A 264 ? 0.5031 0.4796 0.5629 0.0623  0.0242  -0.0394 263 ALA A CB  
1939 N N   . TYR A 265 ? 0.5338 0.4869 0.5750 0.0507  -0.0022 -0.0315 264 TYR A N   
1940 C CA  . TYR A 265 ? 0.5645 0.5015 0.5936 0.0480  -0.0093 -0.0312 264 TYR A CA  
1941 C C   . TYR A 265 ? 0.5409 0.4752 0.5530 0.0397  -0.0113 -0.0326 264 TYR A C   
1942 O O   . TYR A 265 ? 0.5204 0.4430 0.5198 0.0370  -0.0113 -0.0359 264 TYR A O   
1943 C CB  . TYR A 265 ? 0.5568 0.4937 0.5955 0.0493  -0.0195 -0.0231 264 TYR A CB  
1944 C CG  . TYR A 265 ? 0.6367 0.5579 0.6614 0.0460  -0.0265 -0.0210 264 TYR A CG  
1945 C CD1 . TYR A 265 ? 0.6359 0.5414 0.6544 0.0483  -0.0247 -0.0233 264 TYR A CD1 
1946 C CD2 . TYR A 265 ? 0.6081 0.5292 0.6252 0.0405  -0.0346 -0.0165 264 TYR A CD2 
1947 C CE1 . TYR A 265 ? 0.6017 0.4937 0.6075 0.0445  -0.0302 -0.0199 264 TYR A CE1 
1948 C CE2 . TYR A 265 ? 0.5669 0.4742 0.5694 0.0375  -0.0394 -0.0143 264 TYR A CE2 
1949 C CZ  . TYR A 265 ? 0.5620 0.4558 0.5593 0.0393  -0.0370 -0.0153 264 TYR A CZ  
1950 O OH  . TYR A 265 ? 0.5751 0.4562 0.5578 0.0356  -0.0407 -0.0118 264 TYR A OH  
1951 N N   . LEU A 266 ? 0.5473 0.4926 0.5609 0.0358  -0.0130 -0.0294 265 LEU A N   
1952 C CA  . LEU A 266 ? 0.5167 0.4603 0.5174 0.0295  -0.0146 -0.0301 265 LEU A CA  
1953 C C   . LEU A 266 ? 0.5498 0.4928 0.5404 0.0278  -0.0085 -0.0359 265 LEU A C   
1954 O O   . LEU A 266 ? 0.5944 0.5315 0.5746 0.0239  -0.0100 -0.0379 265 LEU A O   
1955 C CB  . LEU A 266 ? 0.5451 0.4987 0.5511 0.0263  -0.0175 -0.0254 265 LEU A CB  
1956 C CG  . LEU A 266 ? 0.5886 0.5387 0.5958 0.0242  -0.0263 -0.0210 265 LEU A CG  
1957 C CD1 . LEU A 266 ? 0.7002 0.6576 0.7119 0.0201  -0.0285 -0.0176 265 LEU A CD1 
1958 C CD2 . LEU A 266 ? 0.5874 0.5252 0.5801 0.0222  -0.0288 -0.0228 265 LEU A CD2 
1959 N N   . GLN A 267 ? 0.5417 0.4917 0.5351 0.0303  -0.0016 -0.0385 266 GLN A N   
1960 C CA  . GLN A 267 ? 0.5734 0.5219 0.5537 0.0280  0.0034  -0.0445 266 GLN A CA  
1961 C C   . GLN A 267 ? 0.5657 0.4996 0.5376 0.0281  0.0034  -0.0511 266 GLN A C   
1962 O O   . GLN A 267 ? 0.6303 0.5604 0.5902 0.0230  0.0023  -0.0548 266 GLN A O   
1963 C CB  . GLN A 267 ? 0.6112 0.5687 0.5935 0.0312  0.0123  -0.0465 266 GLN A CB  
1964 C CG  . GLN A 267 ? 0.7067 0.6784 0.6927 0.0282  0.0131  -0.0400 266 GLN A CG  
1965 C CD  . GLN A 267 ? 0.9737 0.9503 0.9463 0.0262  0.0203  -0.0428 266 GLN A CD  
1966 O OE1 . GLN A 267 ? 0.9865 0.9677 0.9512 0.0209  0.0177  -0.0387 266 GLN A OE1 
1967 N NE2 . GLN A 267 ? 1.0305 1.0052 0.9993 0.0308  0.0295  -0.0500 266 GLN A NE2 
1968 N N   . PHE A 268 ? 0.5834 0.5090 0.5628 0.0333  0.0039  -0.0518 267 PHE A N   
1969 C CA  . PHE A 268 ? 0.6024 0.5115 0.5748 0.0328  0.0034  -0.0570 267 PHE A CA  
1970 C C   . PHE A 268 ? 0.5501 0.4539 0.5174 0.0265  -0.0032 -0.0536 267 PHE A C   
1971 O O   . PHE A 268 ? 0.6329 0.5288 0.5913 0.0213  -0.0039 -0.0576 267 PHE A O   
1972 C CB  . PHE A 268 ? 0.5780 0.4785 0.5613 0.0408  0.0051  -0.0570 267 PHE A CB  
1973 C CG  . PHE A 268 ? 0.5980 0.4801 0.5777 0.0397  0.0013  -0.0572 267 PHE A CG  
1974 C CD1 . PHE A 268 ? 0.6110 0.4786 0.5802 0.0368  0.0037  -0.0652 267 PHE A CD1 
1975 C CD2 . PHE A 268 ? 0.7245 0.6030 0.7103 0.0407  -0.0051 -0.0490 267 PHE A CD2 
1976 C CE1 . PHE A 268 ? 0.5590 0.4088 0.5259 0.0346  0.0003  -0.0643 267 PHE A CE1 
1977 C CE2 . PHE A 268 ? 0.7455 0.6067 0.7269 0.0390  -0.0080 -0.0476 267 PHE A CE2 
1978 C CZ  . PHE A 268 ? 0.6303 0.4773 0.6035 0.0358  -0.0051 -0.0549 267 PHE A CZ  
1979 N N   . ILE A 269 ? 0.5827 0.4914 0.5552 0.0263  -0.0079 -0.0463 268 ILE A N   
1980 C CA  . ILE A 269 ? 0.5015 0.4046 0.4690 0.0217  -0.0122 -0.0429 268 ILE A CA  
1981 C C   . ILE A 269 ? 0.6031 0.5132 0.5650 0.0158  -0.0125 -0.0437 268 ILE A C   
1982 O O   . ILE A 269 ? 0.5989 0.5047 0.5568 0.0112  -0.0134 -0.0437 268 ILE A O   
1983 C CB  . ILE A 269 ? 0.5898 0.4941 0.5615 0.0237  -0.0169 -0.0361 268 ILE A CB  
1984 C CG1 . ILE A 269 ? 0.5785 0.4739 0.5559 0.0288  -0.0187 -0.0336 268 ILE A CG1 
1985 C CG2 . ILE A 269 ? 0.6198 0.5216 0.5837 0.0189  -0.0193 -0.0332 268 ILE A CG2 
1986 C CD1 . ILE A 269 ? 0.6108 0.4920 0.5807 0.0264  -0.0211 -0.0307 268 ILE A CD1 
1987 N N   . THR A 270 ? 0.5151 0.4367 0.4782 0.0158  -0.0119 -0.0434 269 THR A N   
1988 C CA  . THR A 270 ? 0.5711 0.4999 0.5310 0.0115  -0.0134 -0.0425 269 THR A CA  
1989 C C   . THR A 270 ? 0.5307 0.4628 0.4845 0.0086  -0.0121 -0.0471 269 THR A C   
1990 O O   . THR A 270 ? 0.5183 0.4586 0.4706 0.0056  -0.0143 -0.0452 269 THR A O   
1991 C CB  . THR A 270 ? 0.4969 0.4340 0.4611 0.0127  -0.0150 -0.0377 269 THR A CB  
1992 O OG1 . THR A 270 ? 0.5374 0.4812 0.5037 0.0145  -0.0127 -0.0376 269 THR A OG1 
1993 C CG2 . THR A 270 ? 0.5357 0.4680 0.5030 0.0148  -0.0174 -0.0343 269 THR A CG2 
1994 N N   . ALA A 271 ? 0.5348 0.4596 0.4841 0.0095  -0.0091 -0.0530 270 ALA A N   
1995 C CA  . ALA A 271 ? 0.4980 0.4240 0.4370 0.0064  -0.0080 -0.0587 270 ALA A CA  
1996 C C   . ALA A 271 ? 0.5077 0.4344 0.4427 -0.0010 -0.0133 -0.0595 270 ALA A C   
1997 O O   . ALA A 271 ? 0.4952 0.4280 0.4224 -0.0049 -0.0157 -0.0608 270 ALA A O   
1998 C CB  . ALA A 271 ? 0.4985 0.4132 0.4325 0.0095  -0.0029 -0.0665 270 ALA A CB  
1999 N N   . SER A 272 ? 0.4846 0.4062 0.4253 -0.0035 -0.0154 -0.0579 271 SER A N   
2000 C CA  . SER A 272 ? 0.4928 0.4182 0.4346 -0.0109 -0.0200 -0.0575 271 SER A CA  
2001 C C   . SER A 272 ? 0.4194 0.3594 0.3690 -0.0110 -0.0228 -0.0505 271 SER A C   
2002 O O   . SER A 272 ? 0.4088 0.3558 0.3629 -0.0162 -0.0268 -0.0491 271 SER A O   
2003 C CB  . SER A 272 ? 0.4516 0.3671 0.3979 -0.0140 -0.0197 -0.0573 271 SER A CB  
2004 O OG  . SER A 272 ? 0.4951 0.4137 0.4488 -0.0112 -0.0181 -0.0506 271 SER A OG  
2005 N N   . PHE A 273 ? 0.3933 0.3377 0.3458 -0.0054 -0.0210 -0.0462 272 PHE A N   
2006 C CA  . PHE A 273 ? 0.4376 0.3928 0.3973 -0.0045 -0.0233 -0.0402 272 PHE A CA  
2007 C C   . PHE A 273 ? 0.4303 0.3951 0.3872 -0.0077 -0.0281 -0.0391 272 PHE A C   
2008 O O   . PHE A 273 ? 0.4510 0.4247 0.4156 -0.0099 -0.0321 -0.0355 272 PHE A O   
2009 C CB  . PHE A 273 ? 0.4256 0.3805 0.3875 0.0011  -0.0212 -0.0367 272 PHE A CB  
2010 C CG  . PHE A 273 ? 0.4809 0.4287 0.4457 0.0036  -0.0189 -0.0358 272 PHE A CG  
2011 C CD1 . PHE A 273 ? 0.4772 0.4163 0.4397 0.0022  -0.0173 -0.0383 272 PHE A CD1 
2012 C CD2 . PHE A 273 ? 0.4918 0.4398 0.4595 0.0069  -0.0190 -0.0324 272 PHE A CD2 
2013 C CE1 . PHE A 273 ? 0.5373 0.4694 0.4994 0.0040  -0.0158 -0.0364 272 PHE A CE1 
2014 C CE2 . PHE A 273 ? 0.5146 0.4549 0.4807 0.0085  -0.0175 -0.0320 272 PHE A CE2 
2015 C CZ  . PHE A 273 ? 0.4011 0.3342 0.3639 0.0070  -0.0160 -0.0336 272 PHE A CZ  
2016 N N   . SER A 274 ? 0.4140 0.3777 0.3598 -0.0078 -0.0275 -0.0415 273 SER A N   
2017 C CA  . SER A 274 ? 0.4682 0.4398 0.4068 -0.0115 -0.0327 -0.0399 273 SER A CA  
2018 C C   . SER A 274 ? 0.4693 0.4403 0.4029 -0.0187 -0.0381 -0.0448 273 SER A C   
2019 O O   . SER A 274 ? 0.4822 0.4617 0.4127 -0.0230 -0.0454 -0.0421 273 SER A O   
2020 C CB  . SER A 274 ? 0.4561 0.4264 0.3814 -0.0100 -0.0290 -0.0413 273 SER A CB  
2021 O OG  . SER A 274 ? 0.3820 0.3428 0.2960 -0.0111 -0.0250 -0.0504 273 SER A OG  
2022 N N   . VAL A 275 ? 0.4483 0.4089 0.3813 -0.0208 -0.0357 -0.0512 274 VAL A N   
2023 C CA  . VAL A 275 ? 0.4090 0.3665 0.3376 -0.0291 -0.0412 -0.0565 274 VAL A CA  
2024 C C   . VAL A 275 ? 0.4212 0.3891 0.3674 -0.0332 -0.0462 -0.0511 274 VAL A C   
2025 O O   . VAL A 275 ? 0.3914 0.3667 0.3391 -0.0406 -0.0545 -0.0508 274 VAL A O   
2026 C CB  . VAL A 275 ? 0.4105 0.3502 0.3321 -0.0297 -0.0364 -0.0652 274 VAL A CB  
2027 C CG1 . VAL A 275 ? 0.4769 0.4115 0.3983 -0.0394 -0.0424 -0.0697 274 VAL A CG1 
2028 C CG2 . VAL A 275 ? 0.4666 0.3978 0.3707 -0.0263 -0.0315 -0.0721 274 VAL A CG2 
2029 N N   . TYR A 276 ? 0.3933 0.3625 0.3532 -0.0287 -0.0411 -0.0466 275 TYR A N   
2030 C CA  . TYR A 276 ? 0.4391 0.4188 0.4169 -0.0314 -0.0426 -0.0415 275 TYR A CA  
2031 C C   . TYR A 276 ? 0.4125 0.4038 0.4024 -0.0244 -0.0409 -0.0340 275 TYR A C   
2032 O O   . TYR A 276 ? 0.4207 0.4266 0.4239 -0.0257 -0.0457 -0.0289 275 TYR A O   
2033 C CB  . TYR A 276 ? 0.4041 0.3740 0.3861 -0.0331 -0.0368 -0.0430 275 TYR A CB  
2034 C CG  . TYR A 276 ? 0.4125 0.3947 0.4133 -0.0347 -0.0350 -0.0369 275 TYR A CG  
2035 C CD1 . TYR A 276 ? 0.4665 0.4586 0.4792 -0.0436 -0.0402 -0.0357 275 TYR A CD1 
2036 C CD2 . TYR A 276 ? 0.4507 0.4352 0.4576 -0.0274 -0.0280 -0.0326 275 TYR A CD2 
2037 C CE1 . TYR A 276 ? 0.5220 0.5282 0.5550 -0.0446 -0.0370 -0.0296 275 TYR A CE1 
2038 C CE2 . TYR A 276 ? 0.4747 0.4708 0.4982 -0.0278 -0.0242 -0.0277 275 TYR A CE2 
2039 C CZ  . TYR A 276 ? 0.4811 0.4892 0.5190 -0.0361 -0.0281 -0.0258 275 TYR A CZ  
2040 O OH  . TYR A 276 ? 0.5232 0.5456 0.5806 -0.0363 -0.0228 -0.0205 275 TYR A OH  
2041 N N   . LEU A 277 ? 0.3785 0.3630 0.3652 -0.0171 -0.0347 -0.0332 276 LEU A N   
2042 C CA  . LEU A 277 ? 0.4184 0.4094 0.4159 -0.0107 -0.0321 -0.0277 276 LEU A CA  
2043 C C   . LEU A 277 ? 0.4030 0.4041 0.4041 -0.0086 -0.0380 -0.0227 276 LEU A C   
2044 O O   . LEU A 277 ? 0.4072 0.4189 0.4234 -0.0059 -0.0393 -0.0175 276 LEU A O   
2045 C CB  . LEU A 277 ? 0.4072 0.3866 0.3978 -0.0048 -0.0261 -0.0287 276 LEU A CB  
2046 C CG  . LEU A 277 ? 0.4140 0.3945 0.4123 0.0011  -0.0220 -0.0255 276 LEU A CG  
2047 C CD1 . LEU A 277 ? 0.4412 0.4285 0.4512 -0.0004 -0.0183 -0.0243 276 LEU A CD1 
2048 C CD2 . LEU A 277 ? 0.4596 0.4272 0.4483 0.0046  -0.0182 -0.0274 276 LEU A CD2 
2049 N N   . LEU A 278 ? 0.3811 0.3792 0.3689 -0.0093 -0.0412 -0.0235 277 LEU A N   
2050 C CA  . LEU A 278 ? 0.4440 0.4501 0.4326 -0.0079 -0.0471 -0.0171 277 LEU A CA  
2051 C C   . LEU A 278 ? 0.4042 0.4239 0.4016 -0.0124 -0.0560 -0.0134 277 LEU A C   
2052 O O   . LEU A 278 ? 0.3741 0.4035 0.3859 -0.0085 -0.0595 -0.0060 277 LEU A O   
2053 C CB  . LEU A 278 ? 0.3998 0.4001 0.3701 -0.0089 -0.0472 -0.0184 277 LEU A CB  
2054 C CG  . LEU A 278 ? 0.4234 0.4309 0.3875 -0.0102 -0.0542 -0.0118 277 LEU A CG  
2055 C CD1 . LEU A 278 ? 0.4223 0.4338 0.3998 -0.0044 -0.0559 -0.0027 277 LEU A CD1 
2056 C CD2 . LEU A 278 ? 0.3713 0.3729 0.3158 -0.0116 -0.0510 -0.0139 277 LEU A CD2 
2057 N N   . PRO A 279 ? 0.4198 0.4408 0.4108 -0.0206 -0.0609 -0.0179 278 PRO A N   
2058 C CA  . PRO A 279 ? 0.4079 0.4439 0.4099 -0.0258 -0.0714 -0.0134 278 PRO A CA  
2059 C C   . PRO A 279 ? 0.4023 0.4503 0.4314 -0.0238 -0.0697 -0.0093 278 PRO A C   
2060 O O   . PRO A 279 ? 0.4278 0.4916 0.4740 -0.0227 -0.0769 -0.0017 278 PRO A O   
2061 C CB  . PRO A 279 ? 0.3869 0.4174 0.3739 -0.0360 -0.0761 -0.0214 278 PRO A CB  
2062 C CG  . PRO A 279 ? 0.3716 0.3853 0.3485 -0.0347 -0.0658 -0.0296 278 PRO A CG  
2063 C CD  . PRO A 279 ? 0.3636 0.3719 0.3375 -0.0255 -0.0581 -0.0272 278 PRO A CD  
2064 N N   . THR A 280 ? 0.4061 0.4478 0.4400 -0.0229 -0.0601 -0.0135 279 THR A N   
2065 C CA  . THR A 280 ? 0.4111 0.4647 0.4695 -0.0210 -0.0559 -0.0097 279 THR A CA  
2066 C C   . THR A 280 ? 0.3683 0.4280 0.4401 -0.0103 -0.0528 -0.0034 279 THR A C   
2067 O O   . THR A 280 ? 0.4154 0.4921 0.5100 -0.0080 -0.0559 0.0029  279 THR A O   
2068 C CB  . THR A 280 ? 0.4111 0.4539 0.4666 -0.0221 -0.0452 -0.0147 279 THR A CB  
2069 O OG1 . THR A 280 ? 0.3651 0.4020 0.4125 -0.0324 -0.0486 -0.0198 279 THR A OG1 
2070 C CG2 . THR A 280 ? 0.3910 0.4456 0.4692 -0.0190 -0.0377 -0.0106 279 THR A CG2 
2071 N N   . LEU A 281 ? 0.3759 0.4217 0.4353 -0.0034 -0.0469 -0.0051 280 LEU A N   
2072 C CA  . LEU A 281 ? 0.3810 0.4279 0.4507 0.0066  -0.0441 -0.0003 280 LEU A CA  
2073 C C   . LEU A 281 ? 0.4100 0.4664 0.4861 0.0082  -0.0547 0.0076  280 LEU A C   
2074 O O   . LEU A 281 ? 0.3265 0.3882 0.4192 0.0163  -0.0543 0.0133  280 LEU A O   
2075 C CB  . LEU A 281 ? 0.3649 0.3935 0.4183 0.0112  -0.0377 -0.0040 280 LEU A CB  
2076 C CG  . LEU A 281 ? 0.4178 0.4354 0.4642 0.0116  -0.0277 -0.0102 280 LEU A CG  
2077 C CD1 . LEU A 281 ? 0.3506 0.3517 0.3803 0.0143  -0.0254 -0.0131 280 LEU A CD1 
2078 C CD2 . LEU A 281 ? 0.4222 0.4448 0.4840 0.0173  -0.0196 -0.0095 280 LEU A CD2 
2079 N N   . SER A 282 ? 0.3898 0.4471 0.4519 0.0011  -0.0640 0.0081  281 SER A N   
2080 C CA  . SER A 282 ? 0.3997 0.4660 0.4651 0.0015  -0.0754 0.0170  281 SER A CA  
2081 C C   . SER A 282 ? 0.3611 0.4482 0.4535 0.0015  -0.0824 0.0234  281 SER A C   
2082 O O   . SER A 282 ? 0.3941 0.4900 0.5018 0.0076  -0.0883 0.0327  281 SER A O   
2083 C CB  . SER A 282 ? 0.3770 0.4392 0.4172 -0.0070 -0.0830 0.0151  281 SER A CB  
2084 O OG  . SER A 282 ? 0.3638 0.4348 0.4039 -0.0078 -0.0951 0.0247  281 SER A OG  
2085 N N   . ARG A 283 ? 0.3602 0.4558 0.4612 -0.0053 -0.0818 0.0192  282 ARG A N   
2086 C CA  . ARG A 283 ? 0.3886 0.5071 0.5183 -0.0070 -0.0890 0.0258  282 ARG A CA  
2087 C C   . ARG A 283 ? 0.3692 0.4969 0.5281 0.0041  -0.0792 0.0295  282 ARG A C   
2088 O O   . ARG A 283 ? 0.4910 0.6387 0.6781 0.0074  -0.0852 0.0379  282 ARG A O   
2089 C CB  . ARG A 283 ? 0.4734 0.5975 0.6039 -0.0195 -0.0915 0.0204  282 ARG A CB  
2090 C CG  . ARG A 283 ? 0.5152 0.6323 0.6196 -0.0308 -0.1031 0.0163  282 ARG A CG  
2091 C CD  . ARG A 283 ? 0.6504 0.7719 0.7582 -0.0437 -0.1069 0.0111  282 ARG A CD  
2092 N NE  . ARG A 283 ? 0.8479 0.9533 0.9234 -0.0530 -0.1126 0.0027  282 ARG A NE  
2093 C CZ  . ARG A 283 ? 0.8778 0.9755 0.9458 -0.0638 -0.1131 -0.0054 282 ARG A CZ  
2094 N NH1 . ARG A 283 ? 0.8181 0.9237 0.9087 -0.0680 -0.1090 -0.0051 282 ARG A NH1 
2095 N NH2 . ARG A 283 ? 0.7002 0.7810 0.7371 -0.0704 -0.1173 -0.0140 282 ARG A NH2 
2096 N N   . LEU A 284 ? 0.4448 0.5581 0.5971 0.0100  -0.0643 0.0233  283 LEU A N   
2097 C CA  . LEU A 284 ? 0.4516 0.5704 0.6265 0.0204  -0.0523 0.0244  283 LEU A CA  
2098 C C   . LEU A 284 ? 0.5099 0.6214 0.6884 0.0329  -0.0517 0.0287  283 LEU A C   
2099 O O   . LEU A 284 ? 0.5466 0.6396 0.7024 0.0339  -0.0532 0.0271  283 LEU A O   
2100 C CB  . LEU A 284 ? 0.3484 0.4534 0.5106 0.0200  -0.0372 0.0155  283 LEU A CB  
2101 C CG  . LEU A 284 ? 0.3551 0.4615 0.5106 0.0077  -0.0365 0.0111  283 LEU A CG  
2102 C CD1 . LEU A 284 ? 0.3555 0.4428 0.4913 0.0079  -0.0238 0.0035  283 LEU A CD1 
2103 C CD2 . LEU A 284 ? 0.3187 0.4497 0.5049 0.0038  -0.0364 0.0158  283 LEU A CD2 
2104 N N   . THR A 285 ? 0.4930 0.6190 0.7019 0.0425  -0.0493 0.0346  284 THR A N   
2105 C CA  . THR A 285 ? 0.5271 0.6451 0.7427 0.0551  -0.0494 0.0393  284 THR A CA  
2106 C C   . THR A 285 ? 0.5238 0.6396 0.7558 0.0675  -0.0330 0.0354  284 THR A C   
2107 O O   . THR A 285 ? 0.5299 0.6279 0.7567 0.0773  -0.0283 0.0338  284 THR A O   
2108 C CB  . THR A 285 ? 0.6061 0.7421 0.8435 0.0572  -0.0649 0.0520  284 THR A CB  
2109 O OG1 . THR A 285 ? 0.5641 0.7265 0.8384 0.0605  -0.0633 0.0565  284 THR A OG1 
2110 C CG2 . THR A 285 ? 0.6290 0.7680 0.8470 0.0438  -0.0809 0.0550  284 THR A CG2 
2111 N N   . GLU A 286 ? 0.4719 0.6050 0.7232 0.0667  -0.0240 0.0337  285 GLU A N   
2112 C CA  . GLU A 286 ? 0.4549 0.5870 0.7200 0.0783  -0.0062 0.0293  285 GLU A CA  
2113 C C   . GLU A 286 ? 0.4307 0.5362 0.6629 0.0775  0.0060  0.0178  285 GLU A C   
2114 O O   . GLU A 286 ? 0.4405 0.5383 0.6490 0.0661  0.0046  0.0134  285 GLU A O   
2115 C CB  . GLU A 286 ? 0.4601 0.6205 0.7553 0.0763  0.0010  0.0318  285 GLU A CB  
2116 C CG  . GLU A 286 ? 0.4724 0.6624 0.8074 0.0794  -0.0102 0.0438  285 GLU A CG  
2117 C CD  . GLU A 286 ? 0.5420 0.7334 0.9019 0.0978  -0.0056 0.0480  285 GLU A CD  
2118 O OE1 . GLU A 286 ? 0.6186 0.8184 0.9996 0.1079  0.0117  0.0453  285 GLU A OE1 
2119 O OE2 . GLU A 286 ? 0.5547 0.7380 0.9127 0.1024  -0.0187 0.0541  285 GLU A OE2 
2120 N N   . LYS A 287 ? 0.4024 0.4930 0.6333 0.0897  0.0175  0.0129  286 LYS A N   
2121 C CA  . LYS A 287 ? 0.4798 0.5436 0.6778 0.0889  0.0267  0.0022  286 LYS A CA  
2122 C C   . LYS A 287 ? 0.4537 0.5217 0.6432 0.0825  0.0391  -0.0034 286 LYS A C   
2123 O O   . LYS A 287 ? 0.4284 0.4792 0.5880 0.0753  0.0401  -0.0093 286 LYS A O   
2124 C CB  . LYS A 287 ? 0.4980 0.5433 0.6957 0.1030  0.0355  -0.0027 286 LYS A CB  
2125 C CG  . LYS A 287 ? 0.5507 0.5800 0.7434 0.1062  0.0230  0.0012  286 LYS A CG  
2126 C CD  . LYS A 287 ? 0.6584 0.6665 0.8516 0.1199  0.0315  -0.0043 286 LYS A CD  
2127 C CE  . LYS A 287 ? 0.6339 0.6241 0.8218 0.1216  0.0187  0.0007  286 LYS A CE  
2128 N NZ  . LYS A 287 ? 0.6759 0.6745 0.8563 0.1093  0.0028  0.0091  286 LYS A NZ  
2129 N N   . ARG A 288 ? 0.4538 0.5453 0.6703 0.0848  0.0483  -0.0004 287 ARG A N   
2130 C CA  . ARG A 288 ? 0.5001 0.5965 0.7091 0.0773  0.0600  -0.0036 287 ARG A CA  
2131 C C   . ARG A 288 ? 0.4911 0.5896 0.6873 0.0613  0.0485  -0.0014 287 ARG A C   
2132 O O   . ARG A 288 ? 0.4445 0.5295 0.6154 0.0541  0.0531  -0.0062 287 ARG A O   
2133 C CB  . ARG A 288 ? 0.4867 0.6114 0.7318 0.0821  0.0721  0.0008  287 ARG A CB  
2134 C CG  . ARG A 288 ? 0.6255 0.7445 0.8747 0.0969  0.0917  -0.0052 287 ARG A CG  
2135 C CD  . ARG A 288 ? 0.7554 0.8778 1.0303 0.1121  0.0885  -0.0022 287 ARG A CD  
2136 N NE  . ARG A 288 ? 0.7363 0.8363 0.9984 0.1259  0.1032  -0.0118 287 ARG A NE  
2137 C CZ  . ARG A 288 ? 0.6496 0.7451 0.9296 0.1411  0.1040  -0.0116 287 ARG A CZ  
2138 N NH1 . ARG A 288 ? 0.6819 0.7949 0.9943 0.1450  0.0905  -0.0008 287 ARG A NH1 
2139 N NH2 . ARG A 288 ? 0.7364 0.8079 1.0003 0.1526  0.1183  -0.0224 287 ARG A NH2 
2140 N N   . ASP A 289 ? 0.4673 0.5810 0.6795 0.0559  0.0330  0.0057  288 ASP A N   
2141 C CA  . ASP A 289 ? 0.3700 0.4841 0.5697 0.0412  0.0223  0.0065  288 ASP A CA  
2142 C C   . ASP A 289 ? 0.3800 0.4673 0.5440 0.0380  0.0165  0.0009  288 ASP A C   
2143 O O   . ASP A 289 ? 0.4432 0.5217 0.5884 0.0286  0.0160  -0.0023 288 ASP A O   
2144 C CB  . ASP A 289 ? 0.3470 0.4819 0.5689 0.0363  0.0063  0.0145  288 ASP A CB  
2145 C CG  . ASP A 289 ? 0.4783 0.6435 0.7402 0.0381  0.0101  0.0213  288 ASP A CG  
2146 O OD1 . ASP A 289 ? 0.5459 0.7172 0.8162 0.0392  0.0261  0.0196  288 ASP A OD1 
2147 O OD2 . ASP A 289 ? 0.4613 0.6452 0.7466 0.0382  -0.0029 0.0291  288 ASP A OD2 
2148 N N   . ILE A 290 ? 0.3763 0.4511 0.5327 0.0457  0.0121  0.0003  289 ILE A N   
2149 C CA  . ILE A 290 ? 0.4397 0.4918 0.5661 0.0426  0.0071  -0.0041 289 ILE A CA  
2150 C C   . ILE A 290 ? 0.4254 0.4598 0.5301 0.0428  0.0184  -0.0115 289 ILE A C   
2151 O O   . ILE A 290 ? 0.4796 0.5027 0.5634 0.0356  0.0160  -0.0146 289 ILE A O   
2152 C CB  . ILE A 290 ? 0.4506 0.4939 0.5763 0.0501  0.0004  -0.0017 289 ILE A CB  
2153 C CG1 . ILE A 290 ? 0.4048 0.4642 0.5462 0.0479  -0.0132 0.0069  289 ILE A CG1 
2154 C CG2 . ILE A 290 ? 0.3679 0.3888 0.4655 0.0474  -0.0023 -0.0062 289 ILE A CG2 
2155 C CD1 . ILE A 290 ? 0.4141 0.4670 0.5592 0.0557  -0.0196 0.0120  289 ILE A CD1 
2156 N N   . THR A 291 ? 0.4568 0.4884 0.5657 0.0515  0.0309  -0.0145 290 THR A N   
2157 C CA  . THR A 291 ? 0.4304 0.4450 0.5158 0.0514  0.0414  -0.0214 290 THR A CA  
2158 C C   . THR A 291 ? 0.4770 0.4966 0.5562 0.0414  0.0449  -0.0207 290 THR A C   
2159 O O   . THR A 291 ? 0.4990 0.5027 0.5536 0.0362  0.0439  -0.0239 290 THR A O   
2160 C CB  . THR A 291 ? 0.5169 0.5299 0.6088 0.0624  0.0557  -0.0251 290 THR A CB  
2161 O OG1 . THR A 291 ? 0.4907 0.4945 0.5871 0.0717  0.0517  -0.0260 290 THR A OG1 
2162 C CG2 . THR A 291 ? 0.4732 0.4674 0.5362 0.0617  0.0663  -0.0325 290 THR A CG2 
2163 N N   . ARG A 292 ? 0.4286 0.4701 0.5313 0.0383  0.0481  -0.0158 291 ARG A N   
2164 C CA  . ARG A 292 ? 0.4402 0.4861 0.5395 0.0277  0.0512  -0.0141 291 ARG A CA  
2165 C C   . ARG A 292 ? 0.4591 0.4943 0.5419 0.0184  0.0386  -0.0145 291 ARG A C   
2166 O O   . ARG A 292 ? 0.5093 0.5324 0.5737 0.0124  0.0409  -0.0160 291 ARG A O   
2167 C CB  . ARG A 292 ? 0.5377 0.6112 0.6699 0.0244  0.0536  -0.0077 291 ARG A CB  
2168 C CG  . ARG A 292 ? 0.6965 0.7759 0.8299 0.0166  0.0648  -0.0056 291 ARG A CG  
2169 C CD  . ARG A 292 ? 0.7120 0.8209 0.8817 0.0114  0.0650  0.0016  291 ARG A CD  
2170 N NE  . ARG A 292 ? 0.7085 0.8369 0.9070 0.0227  0.0719  0.0040  291 ARG A NE  
2171 C CZ  . ARG A 292 ? 0.8718 1.0052 1.0764 0.0307  0.0906  0.0029  291 ARG A CZ  
2172 N NH1 . ARG A 292 ? 0.8323 0.9531 1.0140 0.0278  0.1042  0.0002  291 ARG A NH1 
2173 N NH2 . ARG A 292 ? 0.8259 0.9769 1.0597 0.0423  0.0961  0.0049  291 ARG A NH2 
2174 N N   . GLU A 293 ? 0.4451 0.4840 0.5336 0.0176  0.0256  -0.0131 292 GLU A N   
2175 C CA  . GLU A 293 ? 0.4769 0.5063 0.5502 0.0096  0.0153  -0.0144 292 GLU A CA  
2176 C C   . GLU A 293 ? 0.4859 0.4933 0.5335 0.0123  0.0149  -0.0190 292 GLU A C   
2177 O O   . GLU A 293 ? 0.4982 0.4944 0.5305 0.0068  0.0129  -0.0208 292 GLU A O   
2178 C CB  . GLU A 293 ? 0.4299 0.4697 0.5137 0.0079  0.0026  -0.0116 292 GLU A CB  
2179 C CG  . GLU A 293 ? 0.4731 0.5049 0.5422 -0.0005 -0.0067 -0.0139 292 GLU A CG  
2180 C CD  . GLU A 293 ? 0.5859 0.6207 0.6581 -0.0108 -0.0066 -0.0140 292 GLU A CD  
2181 O OE1 . GLU A 293 ? 0.5546 0.5747 0.6096 -0.0157 -0.0083 -0.0177 292 GLU A OE1 
2182 O OE2 . GLU A 293 ? 0.5480 0.5999 0.6413 -0.0141 -0.0047 -0.0101 292 GLU A OE2 
2183 N N   . VAL A 294 ? 0.4789 0.4795 0.5229 0.0207  0.0163  -0.0206 293 VAL A N   
2184 C CA  . VAL A 294 ? 0.4570 0.4381 0.4789 0.0226  0.0151  -0.0246 293 VAL A CA  
2185 C C   . VAL A 294 ? 0.4817 0.4518 0.4875 0.0209  0.0231  -0.0271 293 VAL A C   
2186 O O   . VAL A 294 ? 0.5059 0.4638 0.4952 0.0172  0.0196  -0.0283 293 VAL A O   
2187 C CB  . VAL A 294 ? 0.4512 0.4264 0.4742 0.0309  0.0148  -0.0258 293 VAL A CB  
2188 C CG1 . VAL A 294 ? 0.4794 0.4345 0.4806 0.0320  0.0147  -0.0303 293 VAL A CG1 
2189 C CG2 . VAL A 294 ? 0.4448 0.4270 0.4781 0.0313  0.0048  -0.0218 293 VAL A CG2 
2190 N N   . VAL A 295 ? 0.4663 0.4410 0.4766 0.0237  0.0343  -0.0272 294 VAL A N   
2191 C CA  . VAL A 295 ? 0.5057 0.4701 0.4979 0.0215  0.0426  -0.0286 294 VAL A CA  
2192 C C   . VAL A 295 ? 0.5334 0.4983 0.5227 0.0121  0.0400  -0.0251 294 VAL A C   
2193 O O   . VAL A 295 ? 0.5384 0.4886 0.5079 0.0091  0.0384  -0.0254 294 VAL A O   
2194 C CB  . VAL A 295 ? 0.4978 0.4697 0.4968 0.0262  0.0573  -0.0291 294 VAL A CB  
2195 C CG1 . VAL A 295 ? 0.5083 0.4737 0.4900 0.0212  0.0667  -0.0280 294 VAL A CG1 
2196 C CG2 . VAL A 295 ? 0.4312 0.3936 0.4245 0.0361  0.0610  -0.0347 294 VAL A CG2 
2197 N N   . LYS A 296 ? 0.5505 0.5312 0.5599 0.0072  0.0384  -0.0214 295 LYS A N   
2198 C CA  . LYS A 296 ? 0.5010 0.4798 0.5085 -0.0023 0.0357  -0.0187 295 LYS A CA  
2199 C C   . LYS A 296 ? 0.5357 0.5005 0.5297 -0.0040 0.0250  -0.0209 295 LYS A C   
2200 O O   . LYS A 296 ? 0.5725 0.5253 0.5542 -0.0084 0.0242  -0.0199 295 LYS A O   
2201 C CB  . LYS A 296 ? 0.4741 0.4721 0.5063 -0.0082 0.0338  -0.0153 295 LYS A CB  
2202 C CG  . LYS A 296 ? 0.5460 0.5397 0.5769 -0.0190 0.0303  -0.0132 295 LYS A CG  
2203 C CD  . LYS A 296 ? 0.5368 0.5503 0.5930 -0.0265 0.0294  -0.0095 295 LYS A CD  
2204 C CE  . LYS A 296 ? 0.6469 0.6737 0.7177 -0.0243 0.0193  -0.0106 295 LYS A CE  
2205 N NZ  . LYS A 296 ? 0.6607 0.7024 0.7512 -0.0345 0.0126  -0.0079 295 LYS A NZ  
2206 N N   . SER A 297 ? 0.5161 0.4827 0.5131 -0.0002 0.0174  -0.0232 296 SER A N   
2207 C CA  . SER A 297 ? 0.4953 0.4510 0.4814 -0.0009 0.0091  -0.0253 296 SER A CA  
2208 C C   . SER A 297 ? 0.5174 0.4573 0.4852 0.0021  0.0098  -0.0264 296 SER A C   
2209 O O   . SER A 297 ? 0.5368 0.4664 0.4955 -0.0003 0.0066  -0.0262 296 SER A O   
2210 C CB  . SER A 297 ? 0.4901 0.4524 0.4828 0.0023  0.0024  -0.0264 296 SER A CB  
2211 O OG  . SER A 297 ? 0.4841 0.4600 0.4910 -0.0018 -0.0011 -0.0250 296 SER A OG  
2212 N N   . LEU A 298 ? 0.5310 0.4682 0.4935 0.0075  0.0134  -0.0278 297 LEU A N   
2213 C CA  . LEU A 298 ? 0.5415 0.4636 0.4853 0.0093  0.0122  -0.0290 297 LEU A CA  
2214 C C   . LEU A 298 ? 0.5753 0.4892 0.5064 0.0054  0.0165  -0.0263 297 LEU A C   
2215 O O   . LEU A 298 ? 0.6434 0.5455 0.5614 0.0045  0.0116  -0.0251 297 LEU A O   
2216 C CB  . LEU A 298 ? 0.4247 0.3433 0.3636 0.0150  0.0154  -0.0322 297 LEU A CB  
2217 C CG  . LEU A 298 ? 0.5072 0.4273 0.4534 0.0186  0.0090  -0.0339 297 LEU A CG  
2218 C CD1 . LEU A 298 ? 0.5384 0.4542 0.4830 0.0243  0.0135  -0.0372 297 LEU A CD1 
2219 C CD2 . LEU A 298 ? 0.4964 0.4079 0.4345 0.0172  0.0001  -0.0339 297 LEU A CD2 
2220 N N   . LYS A 299 ? 0.5625 0.4834 0.4987 0.0029  0.0254  -0.0241 298 LYS A N   
2221 C CA  . LYS A 299 ? 0.5723 0.4854 0.4961 -0.0019 0.0303  -0.0199 298 LYS A CA  
2222 C C   . LYS A 299 ? 0.6443 0.5515 0.5693 -0.0073 0.0238  -0.0167 298 LYS A C   
2223 O O   . LYS A 299 ? 0.5889 0.4843 0.5002 -0.0104 0.0243  -0.0124 298 LYS A O   
2224 C CB  . LYS A 299 ? 0.5450 0.4697 0.4779 -0.0042 0.0425  -0.0175 298 LYS A CB  
2225 C CG  . LYS A 299 ? 0.5633 0.4864 0.4846 0.0009  0.0529  -0.0200 298 LYS A CG  
2226 C CD  . LYS A 299 ? 0.6236 0.5646 0.5636 0.0012  0.0655  -0.0185 298 LYS A CD  
2227 C CE  . LYS A 299 ? 0.7840 0.7205 0.7070 0.0036  0.0800  -0.0191 298 LYS A CE  
2228 N NZ  . LYS A 299 ? 1.0027 0.9451 0.9269 -0.0040 0.0904  -0.0119 298 LYS A NZ  
2229 N N   . PHE A 300 ? 0.5229 0.4365 0.4625 -0.0082 0.0178  -0.0186 299 PHE A N   
2230 C CA  . PHE A 300 ? 0.6068 0.5125 0.5471 -0.0123 0.0122  -0.0174 299 PHE A CA  
2231 C C   . PHE A 300 ? 0.6791 0.5758 0.6131 -0.0078 0.0041  -0.0195 299 PHE A C   
2232 O O   . PHE A 300 ? 0.6878 0.5720 0.6149 -0.0084 0.0009  -0.0169 299 PHE A O   
2233 C CB  . PHE A 300 ? 0.5731 0.4892 0.5302 -0.0168 0.0104  -0.0192 299 PHE A CB  
2234 C CG  . PHE A 300 ? 0.6488 0.5552 0.6054 -0.0189 0.0037  -0.0214 299 PHE A CG  
2235 C CD1 . PHE A 300 ? 0.7062 0.5988 0.6580 -0.0236 0.0038  -0.0183 299 PHE A CD1 
2236 C CD2 . PHE A 300 ? 0.5941 0.5040 0.5542 -0.0159 -0.0018 -0.0264 299 PHE A CD2 
2237 C CE1 . PHE A 300 ? 0.6383 0.5199 0.5900 -0.0243 -0.0014 -0.0214 299 PHE A CE1 
2238 C CE2 . PHE A 300 ? 0.5764 0.4767 0.5348 -0.0169 -0.0060 -0.0297 299 PHE A CE2 
2239 C CZ  . PHE A 300 ? 0.5947 0.4804 0.5494 -0.0206 -0.0057 -0.0278 299 PHE A CZ  
2240 N N   . VAL A 301 ? 0.5845 0.4878 0.5225 -0.0031 0.0010  -0.0232 300 VAL A N   
2241 C CA  . VAL A 301 ? 0.5986 0.4976 0.5357 0.0004  -0.0058 -0.0248 300 VAL A CA  
2242 C C   . VAL A 301 ? 0.6522 0.5417 0.5773 0.0035  -0.0091 -0.0227 300 VAL A C   
2243 O O   . VAL A 301 ? 0.6277 0.5108 0.5520 0.0052  -0.0143 -0.0213 300 VAL A O   
2244 C CB  . VAL A 301 ? 0.6537 0.5637 0.6000 0.0029  -0.0079 -0.0283 300 VAL A CB  
2245 C CG1 . VAL A 301 ? 0.5613 0.4737 0.5050 0.0065  -0.0075 -0.0287 300 VAL A CG1 
2246 C CG2 . VAL A 301 ? 0.7100 0.6185 0.6589 0.0048  -0.0124 -0.0301 300 VAL A CG2 
2247 N N   . LEU A 302 ? 0.5961 0.4842 0.5116 0.0042  -0.0064 -0.0225 301 LEU A N   
2248 C CA  . LEU A 302 ? 0.6005 0.4789 0.5021 0.0059  -0.0115 -0.0210 301 LEU A CA  
2249 C C   . LEU A 302 ? 0.6599 0.5269 0.5509 0.0038  -0.0137 -0.0153 301 LEU A C   
2250 O O   . LEU A 302 ? 0.6280 0.4896 0.5174 0.0057  -0.0219 -0.0129 301 LEU A O   
2251 C CB  . LEU A 302 ? 0.5918 0.4684 0.4822 0.0069  -0.0077 -0.0237 301 LEU A CB  
2252 C CG  . LEU A 302 ? 0.5837 0.4661 0.4819 0.0101  -0.0090 -0.0283 301 LEU A CG  
2253 C CD1 . LEU A 302 ? 0.7276 0.6047 0.6135 0.0117  -0.0037 -0.0319 301 LEU A CD1 
2254 C CD2 . LEU A 302 ? 0.6325 0.5133 0.5336 0.0110  -0.0189 -0.0281 301 LEU A CD2 
2255 N N   . PRO A 303 ? 0.6362 0.4996 0.5213 -0.0001 -0.0072 -0.0120 302 PRO A N   
2256 C CA  . PRO A 303 ? 0.6641 0.5147 0.5392 -0.0022 -0.0103 -0.0050 302 PRO A CA  
2257 C C   . PRO A 303 ? 0.6367 0.4845 0.5253 -0.0010 -0.0153 -0.0038 302 PRO A C   
2258 O O   . PRO A 303 ? 0.6476 0.4850 0.5317 0.0005  -0.0219 0.0015  302 PRO A O   
2259 C CB  . PRO A 303 ? 0.7054 0.5547 0.5738 -0.0077 -0.0003 -0.0015 302 PRO A CB  
2260 C CG  . PRO A 303 ? 0.7616 0.6227 0.6329 -0.0068 0.0078  -0.0069 302 PRO A CG  
2261 C CD  . PRO A 303 ? 0.6327 0.5035 0.5206 -0.0029 0.0032  -0.0130 302 PRO A CD  
2262 N N   . ALA A 304 ? 0.6079 0.4639 0.5121 -0.0014 -0.0127 -0.0087 303 ALA A N   
2263 C CA  . ALA A 304 ? 0.6322 0.4835 0.5468 0.0000  -0.0161 -0.0096 303 ALA A CA  
2264 C C   . ALA A 304 ? 0.6583 0.5113 0.5785 0.0067  -0.0228 -0.0108 303 ALA A C   
2265 O O   . ALA A 304 ? 0.6587 0.5032 0.5821 0.0100  -0.0272 -0.0079 303 ALA A O   
2266 C CB  . ALA A 304 ? 0.5948 0.4540 0.5210 -0.0029 -0.0121 -0.0154 303 ALA A CB  
2267 N N   . VAL A 305 ? 0.6113 0.4755 0.5345 0.0087  -0.0236 -0.0146 304 VAL A N   
2268 C CA  . VAL A 305 ? 0.5915 0.4600 0.5227 0.0138  -0.0294 -0.0150 304 VAL A CA  
2269 C C   . VAL A 305 ? 0.6164 0.4781 0.5399 0.0153  -0.0370 -0.0089 304 VAL A C   
2270 O O   . VAL A 305 ? 0.6356 0.4975 0.5681 0.0196  -0.0430 -0.0062 304 VAL A O   
2271 C CB  . VAL A 305 ? 0.5743 0.4555 0.5108 0.0143  -0.0284 -0.0195 304 VAL A CB  
2272 C CG1 . VAL A 305 ? 0.5621 0.4490 0.5080 0.0182  -0.0339 -0.0187 304 VAL A CG1 
2273 C CG2 . VAL A 305 ? 0.7029 0.5909 0.6463 0.0129  -0.0229 -0.0244 304 VAL A CG2 
2274 N N   . ALA A 306 ? 0.5813 0.4374 0.4878 0.0118  -0.0370 -0.0065 305 ALA A N   
2275 C CA  . ALA A 306 ? 0.6263 0.4744 0.5208 0.0120  -0.0456 -0.0005 305 ALA A CA  
2276 C C   . ALA A 306 ? 0.6609 0.4984 0.5558 0.0134  -0.0494 0.0070  305 ALA A C   
2277 O O   . ALA A 306 ? 0.6587 0.4945 0.5581 0.0169  -0.0590 0.0121  305 ALA A O   
2278 C CB  . ALA A 306 ? 0.5685 0.4109 0.4404 0.0078  -0.0429 -0.0005 305 ALA A CB  
2279 N N   . ALA A 307 ? 0.6608 0.4910 0.5527 0.0107  -0.0425 0.0083  306 ALA A N   
2280 C CA  . ALA A 307 ? 0.6250 0.4423 0.5185 0.0120  -0.0458 0.0155  306 ALA A CA  
2281 C C   . ALA A 307 ? 0.6327 0.4528 0.5477 0.0191  -0.0492 0.0136  306 ALA A C   
2282 O O   . ALA A 307 ? 0.6753 0.4891 0.5955 0.0239  -0.0569 0.0202  306 ALA A O   
2283 C CB  . ALA A 307 ? 0.6114 0.4206 0.5005 0.0064  -0.0373 0.0165  306 ALA A CB  
2284 N N   . ALA A 308 ? 0.5756 0.4057 0.5034 0.0204  -0.0432 0.0047  307 ALA A N   
2285 C CA  . ALA A 308 ? 0.6118 0.4449 0.5583 0.0274  -0.0438 0.0016  307 ALA A CA  
2286 C C   . ALA A 308 ? 0.6288 0.4722 0.5855 0.0328  -0.0515 0.0046  307 ALA A C   
2287 O O   . ALA A 308 ? 0.6727 0.5148 0.6436 0.0398  -0.0554 0.0079  307 ALA A O   
2288 C CB  . ALA A 308 ? 0.5735 0.4153 0.5269 0.0265  -0.0357 -0.0084 307 ALA A CB  
2289 N N   . SER A 309 ? 0.5851 0.4386 0.5363 0.0297  -0.0540 0.0036  308 SER A N   
2290 C CA  . SER A 309 ? 0.5324 0.3966 0.4949 0.0329  -0.0622 0.0064  308 SER A CA  
2291 C C   . SER A 309 ? 0.6034 0.4601 0.5614 0.0341  -0.0740 0.0163  308 SER A C   
2292 O O   . SER A 309 ? 0.6189 0.4832 0.5940 0.0390  -0.0817 0.0207  308 SER A O   
2293 C CB  . SER A 309 ? 0.5798 0.4535 0.5366 0.0282  -0.0623 0.0023  308 SER A CB  
2294 O OG  . SER A 309 ? 0.6252 0.5070 0.5885 0.0279  -0.0530 -0.0051 308 SER A OG  
2295 N N   . PHE A 310 ? 0.6125 0.4554 0.5482 0.0295  -0.0756 0.0206  309 PHE A N   
2296 C CA  . PHE A 310 ? 0.6044 0.4381 0.5323 0.0302  -0.0874 0.0313  309 PHE A CA  
2297 C C   . PHE A 310 ? 0.6369 0.4644 0.5820 0.0377  -0.0894 0.0372  309 PHE A C   
2298 O O   . PHE A 310 ? 0.6909 0.5199 0.6466 0.0425  -0.1009 0.0455  309 PHE A O   
2299 C CB  . PHE A 310 ? 0.6765 0.4960 0.5740 0.0231  -0.0862 0.0348  309 PHE A CB  
2300 C CG  . PHE A 310 ? 0.6540 0.4623 0.5380 0.0227  -0.0986 0.0469  309 PHE A CG  
2301 C CD1 . PHE A 310 ? 0.6839 0.4976 0.5670 0.0228  -0.1129 0.0511  309 PHE A CD1 
2302 C CD2 . PHE A 310 ? 0.7507 0.5426 0.6226 0.0214  -0.0969 0.0548  309 PHE A CD2 
2303 C CE1 . PHE A 310 ? 0.7010 0.5044 0.5699 0.0220  -0.1262 0.0631  309 PHE A CE1 
2304 C CE2 . PHE A 310 ? 0.8011 0.5817 0.6585 0.0208  -0.1090 0.0675  309 PHE A CE2 
2305 C CZ  . PHE A 310 ? 0.7812 0.5678 0.6364 0.0213  -0.1242 0.0717  309 PHE A CZ  
2306 N N   . THR A 311 ? 0.6160 0.4360 0.5651 0.0389  -0.0789 0.0329  310 THR A N   
2307 C CA  . THR A 311 ? 0.6178 0.4293 0.5840 0.0470  -0.0793 0.0362  310 THR A CA  
2308 C C   . THR A 311 ? 0.6521 0.4792 0.6464 0.0561  -0.0809 0.0338  310 THR A C   
2309 O O   . THR A 311 ? 0.5665 0.3920 0.5773 0.0642  -0.0880 0.0412  310 THR A O   
2310 C CB  . THR A 311 ? 0.6791 0.4792 0.6432 0.0451  -0.0675 0.0294  310 THR A CB  
2311 O OG1 . THR A 311 ? 0.6620 0.4505 0.6029 0.0359  -0.0653 0.0327  310 THR A OG1 
2312 C CG2 . THR A 311 ? 0.5922 0.3786 0.5717 0.0536  -0.0677 0.0320  310 THR A CG2 
2313 N N   . VAL A 312 ? 0.6214 0.4646 0.6227 0.0550  -0.0740 0.0244  311 VAL A N   
2314 C CA  . VAL A 312 ? 0.5711 0.4315 0.5992 0.0627  -0.0733 0.0223  311 VAL A CA  
2315 C C   . VAL A 312 ? 0.6018 0.4728 0.6407 0.0644  -0.0875 0.0321  311 VAL A C   
2316 O O   . VAL A 312 ? 0.6010 0.4800 0.6657 0.0734  -0.0912 0.0368  311 VAL A O   
2317 C CB  . VAL A 312 ? 0.6391 0.5140 0.6684 0.0592  -0.0639 0.0121  311 VAL A CB  
2318 C CG1 . VAL A 312 ? 0.5812 0.4765 0.6370 0.0652  -0.0637 0.0121  311 VAL A CG1 
2319 C CG2 . VAL A 312 ? 0.4910 0.3572 0.5138 0.0586  -0.0514 0.0026  311 VAL A CG2 
2320 N N   . TRP A 313 ? 0.5980 0.4691 0.6180 0.0559  -0.0960 0.0352  312 TRP A N   
2321 C CA  . TRP A 313 ? 0.6031 0.4831 0.6304 0.0556  -0.1117 0.0441  312 TRP A CA  
2322 C C   . TRP A 313 ? 0.6230 0.4928 0.6548 0.0614  -0.1226 0.0562  312 TRP A C   
2323 O O   . TRP A 313 ? 0.6024 0.4840 0.6568 0.0666  -0.1339 0.0641  312 TRP A O   
2324 C CB  . TRP A 313 ? 0.5965 0.4738 0.5969 0.0448  -0.1182 0.0434  312 TRP A CB  
2325 C CG  . TRP A 313 ? 0.6425 0.5247 0.6445 0.0428  -0.1365 0.0525  312 TRP A CG  
2326 C CD1 . TRP A 313 ? 0.6333 0.5342 0.6560 0.0418  -0.1449 0.0536  312 TRP A CD1 
2327 C CD2 . TRP A 313 ? 0.7053 0.5739 0.6875 0.0404  -0.1500 0.0626  312 TRP A CD2 
2328 N NE1 . TRP A 313 ? 0.7123 0.6123 0.7298 0.0388  -0.1639 0.0633  312 TRP A NE1 
2329 C CE2 . TRP A 313 ? 0.7599 0.6397 0.7509 0.0381  -0.1675 0.0690  312 TRP A CE2 
2330 C CE3 . TRP A 313 ? 0.6803 0.5282 0.6373 0.0393  -0.1492 0.0676  312 TRP A CE3 
2331 C CZ2 . TRP A 313 ? 0.8419 0.7125 0.8154 0.0349  -0.1851 0.0798  312 TRP A CZ2 
2332 C CZ3 . TRP A 313 ? 0.7796 0.6181 0.7187 0.0363  -0.1652 0.0790  312 TRP A CZ3 
2333 C CH2 . TRP A 313 ? 0.8377 0.6873 0.7839 0.0343  -0.1835 0.0848  312 TRP A CH2 
2334 N N   . LEU A 314 ? 0.6064 0.4549 0.6185 0.0604  -0.1200 0.0589  313 LEU A N   
2335 C CA  . LEU A 314 ? 0.6466 0.4827 0.6625 0.0662  -0.1300 0.0716  313 LEU A CA  
2336 C C   . LEU A 314 ? 0.5807 0.4229 0.6329 0.0796  -0.1272 0.0725  313 LEU A C   
2337 O O   . LEU A 314 ? 0.5605 0.4043 0.6303 0.0870  -0.1393 0.0839  313 LEU A O   
2338 C CB  . LEU A 314 ? 0.6253 0.4367 0.6146 0.0618  -0.1252 0.0740  313 LEU A CB  
2339 C CG  . LEU A 314 ? 0.6988 0.5014 0.6508 0.0501  -0.1287 0.0767  313 LEU A CG  
2340 C CD1 . LEU A 314 ? 0.6931 0.4769 0.6248 0.0450  -0.1173 0.0753  313 LEU A CD1 
2341 C CD2 . LEU A 314 ? 0.6631 0.4610 0.6044 0.0492  -0.1474 0.0912  313 LEU A CD2 
2342 N N   . LEU A 315 ? 0.5187 0.3645 0.5825 0.0833  -0.1112 0.0604  314 LEU A N   
2343 C CA  . LEU A 315 ? 0.5612 0.4113 0.6568 0.0965  -0.1049 0.0585  314 LEU A CA  
2344 C C   . LEU A 315 ? 0.6033 0.4810 0.7243 0.1000  -0.1000 0.0526  314 LEU A C   
2345 O O   . LEU A 315 ? 0.5354 0.4180 0.6752 0.1084  -0.0871 0.0448  314 LEU A O   
2346 C CB  . LEU A 315 ? 0.6433 0.4742 0.7314 0.0985  -0.0902 0.0489  314 LEU A CB  
2347 C CG  . LEU A 315 ? 0.5950 0.3974 0.6624 0.0953  -0.0930 0.0550  314 LEU A CG  
2348 C CD1 . LEU A 315 ? 0.7340 0.5195 0.7979 0.0964  -0.0786 0.0438  314 LEU A CD1 
2349 C CD2 . LEU A 315 ? 0.6045 0.3981 0.6857 0.1042  -0.1061 0.0701  314 LEU A CD2 
2350 N N   . ARG A 316 ? 0.5549 0.4499 0.6757 0.0930  -0.1098 0.0562  315 ARG A N   
2351 C CA  . ARG A 316 ? 0.5625 0.4838 0.7070 0.0940  -0.1052 0.0519  315 ARG A CA  
2352 C C   . ARG A 316 ? 0.5801 0.5165 0.7654 0.1079  -0.1040 0.0563  315 ARG A C   
2353 O O   . ARG A 316 ? 0.5808 0.5337 0.7862 0.1125  -0.0911 0.0493  315 ARG A O   
2354 C CB  . ARG A 316 ? 0.5510 0.4851 0.6889 0.0834  -0.1185 0.0562  315 ARG A CB  
2355 C CG  . ARG A 316 ? 0.5600 0.4947 0.7015 0.0828  -0.1396 0.0701  315 ARG A CG  
2356 C CD  . ARG A 316 ? 0.5813 0.5176 0.6996 0.0691  -0.1514 0.0706  315 ARG A CD  
2357 N NE  . ARG A 316 ? 0.5836 0.5228 0.7047 0.0671  -0.1735 0.0834  315 ARG A NE  
2358 C CZ  . ARG A 316 ? 0.5589 0.4796 0.6589 0.0667  -0.1845 0.0921  315 ARG A CZ  
2359 N NH1 . ARG A 316 ? 0.5866 0.4846 0.6627 0.0678  -0.1751 0.0898  315 ARG A NH1 
2360 N NH2 . ARG A 316 ? 0.6693 0.5947 0.7722 0.0644  -0.2062 0.1041  315 ARG A NH2 
2361 N N   . ASP A 317 ? 0.5184 0.4496 0.7167 0.1153  -0.1166 0.0683  316 ASP A N   
2362 C CA  . ASP A 317 ? 0.5021 0.4476 0.7427 0.1304  -0.1150 0.0731  316 ASP A CA  
2363 C C   . ASP A 317 ? 0.5398 0.4723 0.7860 0.1415  -0.0955 0.0626  316 ASP A C   
2364 O O   . ASP A 317 ? 0.5612 0.5100 0.8383 0.1524  -0.0841 0.0586  316 ASP A O   
2365 C CB  . ASP A 317 ? 0.5634 0.5047 0.8160 0.1360  -0.1348 0.0897  316 ASP A CB  
2366 C CG  . ASP A 317 ? 0.5922 0.5564 0.8568 0.1292  -0.1543 0.1004  316 ASP A CG  
2367 O OD1 . ASP A 317 ? 0.6921 0.6522 0.9589 0.1304  -0.1737 0.1146  316 ASP A OD1 
2368 O OD2 . ASP A 317 ? 0.5570 0.5420 0.8273 0.1217  -0.1511 0.0951  316 ASP A OD2 
2369 N N   . PHE A 318 ? 0.5193 0.4221 0.7358 0.1387  -0.0913 0.0579  317 PHE A N   
2370 C CA  . PHE A 318 ? 0.5812 0.4688 0.7983 0.1469  -0.0734 0.0459  317 PHE A CA  
2371 C C   . PHE A 318 ? 0.5319 0.4313 0.7418 0.1420  -0.0568 0.0310  317 PHE A C   
2372 O O   . PHE A 318 ? 0.5373 0.4400 0.7619 0.1515  -0.0414 0.0216  317 PHE A O   
2373 C CB  . PHE A 318 ? 0.5724 0.4256 0.7600 0.1427  -0.0744 0.0453  317 PHE A CB  
2374 C CG  . PHE A 318 ? 0.5231 0.3582 0.7024 0.1460  -0.0570 0.0304  317 PHE A CG  
2375 C CD1 . PHE A 318 ? 0.5834 0.4066 0.7836 0.1612  -0.0496 0.0275  317 PHE A CD1 
2376 C CD2 . PHE A 318 ? 0.5771 0.4068 0.7280 0.1339  -0.0485 0.0189  317 PHE A CD2 
2377 C CE1 . PHE A 318 ? 0.5694 0.3736 0.7590 0.1633  -0.0342 0.0123  317 PHE A CE1 
2378 C CE2 . PHE A 318 ? 0.6561 0.4692 0.7979 0.1355  -0.0344 0.0050  317 PHE A CE2 
2379 C CZ  . PHE A 318 ? 0.6315 0.4309 0.7911 0.1498  -0.0273 0.0011  317 PHE A CZ  
2380 N N   . ALA A 319 ? 0.4881 0.3931 0.6743 0.1275  -0.0595 0.0287  318 ALA A N   
2381 C CA  . ALA A 319 ? 0.5321 0.4481 0.7104 0.1222  -0.0456 0.0166  318 ALA A CA  
2382 C C   . ALA A 319 ? 0.6354 0.5810 0.8458 0.1286  -0.0394 0.0169  318 ALA A C   
2383 O O   . ALA A 319 ? 0.5976 0.5498 0.8110 0.1317  -0.0231 0.0066  318 ALA A O   
2384 C CB  . ALA A 319 ? 0.5289 0.4453 0.6793 0.1066  -0.0513 0.0161  318 ALA A CB  
2385 N N   . ILE A 320 ? 0.6340 0.5982 0.8682 0.1299  -0.0524 0.0290  319 ILE A N   
2386 C CA  . ILE A 320 ? 0.6252 0.6202 0.8954 0.1357  -0.0473 0.0314  319 ILE A CA  
2387 C C   . ILE A 320 ? 0.5745 0.5709 0.8727 0.1533  -0.0345 0.0285  319 ILE A C   
2388 O O   . ILE A 320 ? 0.5506 0.5626 0.8634 0.1586  -0.0175 0.0213  319 ILE A O   
2389 C CB  . ILE A 320 ? 0.5886 0.6024 0.8780 0.1314  -0.0670 0.0457  319 ILE A CB  
2390 C CG1 . ILE A 320 ? 0.6086 0.6253 0.8733 0.1142  -0.0746 0.0451  319 ILE A CG1 
2391 C CG2 . ILE A 320 ? 0.6339 0.6792 0.9714 0.1413  -0.0639 0.0518  319 ILE A CG2 
2392 C CD1 . ILE A 320 ? 0.5527 0.5822 0.8280 0.1075  -0.0959 0.0574  319 ILE A CD1 
2393 N N   . TRP A 321 ? 0.5299 0.5092 0.8354 0.1631  -0.0418 0.0343  320 TRP A N   
2394 C CA  . TRP A 321 ? 0.5214 0.4993 0.8552 0.1816  -0.0299 0.0315  320 TRP A CA  
2395 C C   . TRP A 321 ? 0.5217 0.4819 0.8359 0.1848  -0.0084 0.0137  320 TRP A C   
2396 O O   . TRP A 321 ? 0.6486 0.6157 0.9847 0.1983  0.0079  0.0070  320 TRP A O   
2397 C CB  . TRP A 321 ? 0.5956 0.5537 0.9372 0.1904  -0.0436 0.0420  320 TRP A CB  
2398 C CG  . TRP A 321 ? 0.5780 0.5228 0.9397 0.2093  -0.0305 0.0365  320 TRP A CG  
2399 C CD1 . TRP A 321 ? 0.5591 0.5239 0.9661 0.2265  -0.0243 0.0401  320 TRP A CD1 
2400 C CD2 . TRP A 321 ? 0.5582 0.4664 0.8963 0.2130  -0.0214 0.0257  320 TRP A CD2 
2401 N NE1 . TRP A 321 ? 0.6476 0.5886 1.0594 0.2418  -0.0112 0.0316  320 TRP A NE1 
2402 C CE2 . TRP A 321 ? 0.6969 0.6018 1.0659 0.2332  -0.0098 0.0225  320 TRP A CE2 
2403 C CE3 . TRP A 321 ? 0.6627 0.5407 0.9581 0.2009  -0.0219 0.0186  320 TRP A CE3 
2404 C CZ2 . TRP A 321 ? 0.7397 0.6091 1.0957 0.2412  0.0005  0.0115  320 TRP A CZ2 
2405 C CZ3 . TRP A 321 ? 0.6838 0.5289 0.9680 0.2077  -0.0123 0.0087  320 TRP A CZ3 
2406 C CH2 . TRP A 321 ? 0.7053 0.5447 1.0183 0.2274  -0.0016 0.0048  320 TRP A CH2 
2407 N N   . LEU A 322 ? 0.6253 0.5631 0.8987 0.1727  -0.0079 0.0058  321 LEU A N   
2408 C CA  . LEU A 322 ? 0.6710 0.5899 0.9238 0.1744  0.0097  -0.0109 321 LEU A CA  
2409 C C   . LEU A 322 ? 0.6167 0.5539 0.8598 0.1676  0.0234  -0.0205 321 LEU A C   
2410 O O   . LEU A 322 ? 0.6259 0.5632 0.8713 0.1754  0.0414  -0.0322 321 LEU A O   
2411 C CB  . LEU A 322 ? 0.6396 0.5256 0.8559 0.1647  0.0035  -0.0144 321 LEU A CB  
2412 C CG  . LEU A 322 ? 0.6311 0.4955 0.8216 0.1628  0.0180  -0.0316 321 LEU A CG  
2413 C CD1 . LEU A 322 ? 0.6653 0.4990 0.8590 0.1741  0.0213  -0.0358 321 LEU A CD1 
2414 C CD2 . LEU A 322 ? 0.7005 0.5547 0.8555 0.1452  0.0123  -0.0341 321 LEU A CD2 
2415 N N   . LEU A 323 ? 0.6403 0.5919 0.8718 0.1534  0.0154  -0.0158 322 LEU A N   
2416 C CA  . LEU A 323 ? 0.7093 0.6725 0.9248 0.1449  0.0265  -0.0241 322 LEU A CA  
2417 C C   . LEU A 323 ? 0.7848 0.7818 1.0289 0.1479  0.0341  -0.0201 322 LEU A C   
2418 O O   . LEU A 323 ? 0.8172 0.8232 1.0523 0.1452  0.0485  -0.0279 322 LEU A O   
2419 C CB  . LEU A 323 ? 0.5848 0.5436 0.7721 0.1281  0.0152  -0.0217 322 LEU A CB  
2420 C CG  . LEU A 323 ? 0.6859 0.6155 0.8392 0.1217  0.0144  -0.0296 322 LEU A CG  
2421 C CD1 . LEU A 323 ? 0.7039 0.6290 0.8390 0.1089  -0.0002 -0.0228 322 LEU A CD1 
2422 C CD2 . LEU A 323 ? 0.8348 0.7615 0.9678 0.1183  0.0288  -0.0430 322 LEU A CD2 
2423 N N   . LEU A 324 ? 0.7329 0.7493 1.0111 0.1528  0.0247  -0.0075 323 LEU A N   
2424 C CA  . LEU A 324 ? 0.9436 0.9946 1.2509 0.1525  0.0295  -0.0015 323 LEU A CA  
2425 C C   . LEU A 324 ? 0.9596 1.0280 1.3120 0.1691  0.0341  0.0042  323 LEU A C   
2426 O O   . LEU A 324 ? 0.8782 0.9337 1.2424 0.1791  0.0262  0.0081  323 LEU A O   
2427 C CB  . LEU A 324 ? 0.8895 0.9533 1.1974 0.1385  0.0110  0.0098  323 LEU A CB  
2428 C CG  . LEU A 324 ? 0.8354 0.8906 1.1068 0.1224  0.0088  0.0054  323 LEU A CG  
2429 C CD1 . LEU A 324 ? 0.7809 0.8260 1.0381 0.1121  -0.0127 0.0129  323 LEU A CD1 
2430 C CD2 . LEU A 324 ? 0.9128 0.9935 1.1939 0.1157  0.0176  0.0067  323 LEU A CD2 
2431 N N   . SER A 325 ? 1.0646 1.1633 1.4436 0.1721  0.0475  0.0054  324 SER A N   
2432 C CA  . SER A 325 ? 1.1566 1.2778 1.5839 0.1883  0.0544  0.0110  324 SER A CA  
2433 C C   . SER A 325 ? 1.2016 1.3398 1.6611 0.1868  0.0312  0.0284  324 SER A C   
2434 O O   . SER A 325 ? 1.1996 1.3547 1.6612 0.1725  0.0190  0.0367  324 SER A O   
2435 C CB  . SER A 325 ? 1.1201 1.2714 1.5662 0.1900  0.0761  0.0084  324 SER A CB  
2436 O OG  . SER A 325 ? 1.2031 1.3888 1.7036 0.1988  0.0759  0.0204  324 SER A OG  
2437 N N   . ASN A 326 ? 1.3185 1.4509 1.8021 0.2012  0.0243  0.0339  325 ASN A N   
2438 C CA  . ASN A 326 ? 1.2767 1.4231 1.7891 0.2004  0.0000  0.0511  325 ASN A CA  
2439 C C   . ASN A 326 ? 1.2545 1.4456 1.8139 0.1995  0.0005  0.0616  325 ASN A C   
2440 O O   . ASN A 326 ? 1.3456 1.5586 1.9528 0.2147  0.0043  0.0684  325 ASN A O   
2441 C CB  . ASN A 326 ? 1.3041 1.4356 1.8356 0.2180  -0.0060 0.0558  325 ASN A CB  
2442 C CG  . ASN A 326 ? 1.3353 1.4673 1.8757 0.2134  -0.0359 0.0726  325 ASN A CG  
2443 O OD1 . ASN A 326 ? 1.2577 1.4212 1.8324 0.2102  -0.0486 0.0855  325 ASN A OD1 
2444 N ND2 . ASN A 326 ? 1.3474 1.4444 1.8560 0.2120  -0.0478 0.0729  325 ASN A ND2 
2445 N N   . LYS A 327 ? 1.2335 1.4383 1.7815 0.1817  -0.0032 0.0632  326 LYS A N   
2446 C CA  . LYS A 327 ? 1.2385 1.4845 1.8291 0.1766  -0.0061 0.0745  326 LYS A CA  
2447 C C   . LYS A 327 ? 1.2836 1.5329 1.8639 0.1569  -0.0318 0.0839  326 LYS A C   
2448 O O   . LYS A 327 ? 1.3228 1.6045 1.9373 0.1497  -0.0383 0.0942  326 LYS A O   
2449 C CB  . LYS A 327 ? 1.2108 1.4757 1.8049 0.1747  0.0205  0.0671  326 LYS A CB  
2450 C CG  . LYS A 327 ? 1.1669 1.4161 1.7130 0.1568  0.0229  0.0593  326 LYS A CG  
2451 C CD  . LYS A 327 ? 1.0778 1.3499 1.6319 0.1540  0.0469  0.0559  326 LYS A CD  
2452 C CE  . LYS A 327 ? 1.0357 1.3012 1.5552 0.1336  0.0427  0.0546  326 LYS A CE  
2453 N NZ  . LYS A 327 ? 0.9266 1.2202 1.4618 0.1282  0.0613  0.0569  326 LYS A NZ  
2454 N N   . PHE A 328 ? 1.3465 1.5632 1.8815 0.1479  -0.0462 0.0806  327 PHE A N   
2455 C CA  . PHE A 328 ? 1.3510 1.5671 1.8717 0.1297  -0.0697 0.0876  327 PHE A CA  
2456 C C   . PHE A 328 ? 1.3807 1.5770 1.8892 0.1305  -0.0940 0.0946  327 PHE A C   
2457 O O   . PHE A 328 ? 1.2911 1.5036 1.8249 0.1273  -0.1152 0.1075  327 PHE A O   
2458 C CB  . PHE A 328 ? 1.3505 1.5493 1.8258 0.1151  -0.0625 0.0770  327 PHE A CB  
2459 C CG  . PHE A 328 ? 1.4066 1.5717 1.8387 0.1195  -0.0500 0.0636  327 PHE A CG  
2460 C CD1 . PHE A 328 ? 1.3845 1.5187 1.7829 0.1177  -0.0632 0.0621  327 PHE A CD1 
2461 C CD2 . PHE A 328 ? 1.3224 1.4877 1.7480 0.1247  -0.0251 0.0529  327 PHE A CD2 
2462 C CE1 . PHE A 328 ? 1.4147 1.5202 1.7772 0.1205  -0.0516 0.0503  327 PHE A CE1 
2463 C CE2 . PHE A 328 ? 1.2378 1.3733 1.6249 0.1273  -0.0151 0.0406  327 PHE A CE2 
2464 C CZ  . PHE A 328 ? 1.2838 1.3902 1.6415 0.1250  -0.0287 0.0396  327 PHE A CZ  
2465 N N   . THR A 329 ? 1.3923 1.5541 1.8630 0.1347  -0.0909 0.0867  328 THR A N   
2466 C CA  . THR A 329 ? 1.3653 1.5005 1.8114 0.1341  -0.1099 0.0914  328 THR A CA  
2467 C C   . THR A 329 ? 1.3920 1.5261 1.8210 0.1174  -0.1348 0.0988  328 THR A C   
2468 O O   . THR A 329 ? 1.4277 1.5427 1.8370 0.1160  -0.1522 0.1046  328 THR A O   
2469 C CB  . THR A 329 ? 1.3109 1.4486 1.7898 0.1518  -0.1152 0.1006  328 THR A CB  
2470 O OG1 . THR A 329 ? 1.2151 1.3896 1.7462 0.1553  -0.1240 0.1131  328 THR A OG1 
2471 C CG2 . THR A 329 ? 1.3085 1.4363 1.7930 0.1683  -0.0906 0.0904  328 THR A CG2 
2472 N N   . ALA A 330 ? 1.1533 1.3046 1.5858 0.1041  -0.1363 0.0982  329 ALA A N   
2473 C CA  . ALA A 330 ? 0.9671 1.1131 1.3779 0.0871  -0.1580 0.1020  329 ALA A CA  
2474 C C   . ALA A 330 ? 0.8478 0.9681 1.2080 0.0754  -0.1519 0.0901  329 ALA A C   
2475 O O   . ALA A 330 ? 0.7080 0.8183 1.0436 0.0620  -0.1681 0.0910  329 ALA A O   
2476 C CB  . ALA A 330 ? 0.7428 0.9223 1.1908 0.0783  -0.1665 0.1097  329 ALA A CB  
2477 N N   . MET A 331 ? 0.7982 0.9079 1.1426 0.0802  -0.1294 0.0789  330 MET A N   
2478 C CA  . MET A 331 ? 0.7557 0.8429 1.0557 0.0702  -0.1236 0.0684  330 MET A CA  
2479 C C   . MET A 331 ? 0.7202 0.7766 0.9804 0.0682  -0.1327 0.0667  330 MET A C   
2480 O O   . MET A 331 ? 0.7166 0.7557 0.9416 0.0595  -0.1298 0.0591  330 MET A O   
2481 C CB  . MET A 331 ? 0.8366 0.9222 1.1307 0.0750  -0.0985 0.0575  330 MET A CB  
2482 C CG  . MET A 331 ? 0.8847 0.9974 1.2064 0.0732  -0.0865 0.0576  330 MET A CG  
2483 S SD  . MET A 331 ? 1.0996 1.2152 1.4237 0.0841  -0.0569 0.0473  330 MET A SD  
2484 C CE  . MET A 331 ? 0.8453 0.9234 1.1182 0.0829  -0.0528 0.0358  330 MET A CE  
2485 N N   . ARG A 332 ? 0.6709 0.7203 0.9360 0.0758  -0.1435 0.0745  331 ARG A N   
2486 C CA  . ARG A 332 ? 0.5743 0.5941 0.8004 0.0735  -0.1502 0.0739  331 ARG A CA  
2487 C C   . ARG A 332 ? 0.6289 0.6389 0.8234 0.0585  -0.1645 0.0736  331 ARG A C   
2488 O O   . ARG A 332 ? 0.6900 0.6770 0.8459 0.0534  -0.1614 0.0676  331 ARG A O   
2489 C CB  . ARG A 332 ? 0.5568 0.5719 0.7958 0.0835  -0.1616 0.0850  331 ARG A CB  
2490 C CG  . ARG A 332 ? 0.5621 0.5989 0.8320 0.0830  -0.1820 0.0981  331 ARG A CG  
2491 C CD  . ARG A 332 ? 0.5650 0.6023 0.8594 0.0970  -0.1894 0.1094  331 ARG A CD  
2492 N NE  . ARG A 332 ? 0.5371 0.5426 0.7971 0.0990  -0.1912 0.1104  331 ARG A NE  
2493 C CZ  . ARG A 332 ? 0.5802 0.5713 0.8157 0.0929  -0.2110 0.1197  331 ARG A CZ  
2494 N NH1 . ARG A 332 ? 0.5865 0.5904 0.8256 0.0842  -0.2324 0.1279  331 ARG A NH1 
2495 N NH2 . ARG A 332 ? 0.6066 0.5692 0.8119 0.0947  -0.2096 0.1209  331 ARG A NH2 
2496 N N   . ASP A 333 ? 0.6319 0.6590 0.8428 0.0511  -0.1798 0.0797  332 ASP A N   
2497 C CA  . ASP A 333 ? 0.6470 0.6629 0.8271 0.0367  -0.1937 0.0780  332 ASP A CA  
2498 C C   . ASP A 333 ? 0.6257 0.6344 0.7847 0.0289  -0.1802 0.0658  332 ASP A C   
2499 O O   . ASP A 333 ? 0.5960 0.5868 0.7200 0.0194  -0.1860 0.0611  332 ASP A O   
2500 C CB  . ASP A 333 ? 0.6134 0.6492 0.8184 0.0298  -0.2145 0.0871  332 ASP A CB  
2501 C CG  . ASP A 333 ? 0.7641 0.8074 0.9901 0.0373  -0.2310 0.1008  332 ASP A CG  
2502 O OD1 . ASP A 333 ? 0.6896 0.7118 0.8896 0.0410  -0.2357 0.1037  332 ASP A OD1 
2503 O OD2 . ASP A 333 ? 0.7957 0.8665 1.0654 0.0395  -0.2392 0.1095  332 ASP A OD2 
2504 N N   . LEU A 334 ? 0.5819 0.6033 0.7602 0.0332  -0.1620 0.0608  333 LEU A N   
2505 C CA  . LEU A 334 ? 0.5585 0.5735 0.7185 0.0268  -0.1494 0.0507  333 LEU A CA  
2506 C C   . LEU A 334 ? 0.5563 0.5494 0.6846 0.0301  -0.1362 0.0424  333 LEU A C   
2507 O O   . LEU A 334 ? 0.5552 0.5396 0.6632 0.0243  -0.1288 0.0347  333 LEU A O   
2508 C CB  . LEU A 334 ? 0.5369 0.5750 0.7286 0.0291  -0.1359 0.0499  333 LEU A CB  
2509 C CG  . LEU A 334 ? 0.5154 0.5715 0.7280 0.0189  -0.1446 0.0542  333 LEU A CG  
2510 C CD1 . LEU A 334 ? 0.4808 0.5548 0.7243 0.0194  -0.1619 0.0655  333 LEU A CD1 
2511 C CD2 . LEU A 334 ? 0.5316 0.6054 0.7651 0.0198  -0.1270 0.0522  333 LEU A CD2 
2512 N N   . PHE A 335 ? 0.4987 0.4828 0.6240 0.0389  -0.1337 0.0444  334 PHE A N   
2513 C CA  . PHE A 335 ? 0.5930 0.5591 0.6942 0.0418  -0.1200 0.0369  334 PHE A CA  
2514 C C   . PHE A 335 ? 0.5030 0.4493 0.5661 0.0332  -0.1235 0.0329  334 PHE A C   
2515 O O   . PHE A 335 ? 0.5145 0.4536 0.5612 0.0306  -0.1120 0.0248  334 PHE A O   
2516 C CB  . PHE A 335 ? 0.5764 0.5347 0.6832 0.0521  -0.1185 0.0410  334 PHE A CB  
2517 C CG  . PHE A 335 ? 0.6006 0.5692 0.7329 0.0623  -0.1039 0.0379  334 PHE A CG  
2518 C CD1 . PHE A 335 ? 0.5501 0.5430 0.7163 0.0659  -0.1018 0.0404  334 PHE A CD1 
2519 C CD2 . PHE A 335 ? 0.6446 0.5981 0.7662 0.0679  -0.0919 0.0323  334 PHE A CD2 
2520 C CE1 . PHE A 335 ? 0.6126 0.6143 0.7998 0.0759  -0.0866 0.0367  334 PHE A CE1 
2521 C CE2 . PHE A 335 ? 0.4909 0.4510 0.6322 0.0774  -0.0783 0.0278  334 PHE A CE2 
2522 C CZ  . PHE A 335 ? 0.6107 0.5948 0.7838 0.0819  -0.0749 0.0297  334 PHE A CZ  
2523 N N   . ALA A 336 ? 0.5780 0.5158 0.6266 0.0289  -0.1394 0.0386  335 ALA A N   
2524 C CA  . ALA A 336 ? 0.6065 0.5243 0.6166 0.0217  -0.1417 0.0349  335 ALA A CA  
2525 C C   . ALA A 336 ? 0.5481 0.4654 0.5476 0.0145  -0.1362 0.0260  335 ALA A C   
2526 O O   . ALA A 336 ? 0.5377 0.4445 0.5179 0.0136  -0.1246 0.0189  335 ALA A O   
2527 C CB  . ALA A 336 ? 0.6305 0.5415 0.6271 0.0173  -0.1612 0.0426  335 ALA A CB  
2528 N N   . TRP A 337 ? 0.5732 0.5020 0.5871 0.0093  -0.1449 0.0269  336 TRP A N   
2529 C CA  . TRP A 337 ? 0.5117 0.4382 0.5175 0.0025  -0.1408 0.0194  336 TRP A CA  
2530 C C   . TRP A 337 ? 0.5624 0.4941 0.5760 0.0066  -0.1225 0.0139  336 TRP A C   
2531 O O   . TRP A 337 ? 0.5404 0.4612 0.5345 0.0047  -0.1142 0.0069  336 TRP A O   
2532 C CB  . TRP A 337 ? 0.5604 0.5002 0.5868 -0.0041 -0.1530 0.0228  336 TRP A CB  
2533 C CG  . TRP A 337 ? 0.6434 0.5805 0.6648 -0.0087 -0.1734 0.0290  336 TRP A CG  
2534 C CD1 . TRP A 337 ? 0.6281 0.5780 0.6716 -0.0046 -0.1839 0.0391  336 TRP A CD1 
2535 C CD2 . TRP A 337 ? 0.6687 0.5888 0.6606 -0.0182 -0.1865 0.0256  336 TRP A CD2 
2536 N NE1 . TRP A 337 ? 0.6942 0.6371 0.7235 -0.0117 -0.2043 0.0432  336 TRP A NE1 
2537 C CE2 . TRP A 337 ? 0.7260 0.6498 0.7217 -0.0206 -0.2060 0.0343  336 TRP A CE2 
2538 C CE3 . TRP A 337 ? 0.6020 0.5034 0.5643 -0.0246 -0.1835 0.0157  336 TRP A CE3 
2539 C CZ2 . TRP A 337 ? 0.7616 0.6703 0.7291 -0.0301 -0.2232 0.0330  336 TRP A CZ2 
2540 C CZ3 . TRP A 337 ? 0.6483 0.5338 0.5834 -0.0331 -0.1988 0.0133  336 TRP A CZ3 
2541 C CH2 . TRP A 337 ? 0.7971 0.6859 0.7332 -0.0365 -0.2188 0.0217  336 TRP A CH2 
2542 N N   . GLN A 338 ? 0.5282 0.4765 0.5699 0.0128  -0.1159 0.0170  337 GLN A N   
2543 C CA  . GLN A 338 ? 0.4943 0.4478 0.5416 0.0161  -0.0995 0.0119  337 GLN A CA  
2544 C C   . GLN A 338 ? 0.5364 0.4750 0.5613 0.0192  -0.0901 0.0067  337 GLN A C   
2545 O O   . GLN A 338 ? 0.5054 0.4408 0.5208 0.0177  -0.0807 0.0009  337 GLN A O   
2546 C CB  . GLN A 338 ? 0.4951 0.4674 0.5732 0.0230  -0.0936 0.0156  337 GLN A CB  
2547 C CG  . GLN A 338 ? 0.5401 0.5192 0.6229 0.0253  -0.0776 0.0107  337 GLN A CG  
2548 C CD  . GLN A 338 ? 0.5640 0.5552 0.6580 0.0189  -0.0766 0.0117  337 GLN A CD  
2549 O OE1 . GLN A 338 ? 0.5201 0.5168 0.6239 0.0130  -0.0878 0.0163  337 GLN A OE1 
2550 N NE2 . GLN A 338 ? 0.5884 0.5829 0.6802 0.0193  -0.0639 0.0080  337 GLN A NE2 
2551 N N   . LEU A 339 ? 0.5699 0.4994 0.5873 0.0229  -0.0931 0.0095  338 LEU A N   
2552 C CA  . LEU A 339 ? 0.5395 0.4558 0.5388 0.0248  -0.0842 0.0057  338 LEU A CA  
2553 C C   . LEU A 339 ? 0.5659 0.4695 0.5383 0.0188  -0.0836 0.0014  338 LEU A C   
2554 O O   . LEU A 339 ? 0.5450 0.4439 0.5078 0.0187  -0.0734 -0.0035 338 LEU A O   
2555 C CB  . LEU A 339 ? 0.5150 0.4232 0.5133 0.0296  -0.0884 0.0114  338 LEU A CB  
2556 C CG  . LEU A 339 ? 0.5175 0.4338 0.5403 0.0381  -0.0833 0.0130  338 LEU A CG  
2557 C CD1 . LEU A 339 ? 0.5133 0.4201 0.5373 0.0431  -0.0901 0.0203  338 LEU A CD1 
2558 C CD2 . LEU A 339 ? 0.5358 0.4507 0.5568 0.0399  -0.0686 0.0051  338 LEU A CD2 
2559 N N   . VAL A 340 ? 0.5602 0.4582 0.5206 0.0139  -0.0944 0.0030  339 VAL A N   
2560 C CA  . VAL A 340 ? 0.5620 0.4475 0.4970 0.0090  -0.0925 -0.0024 339 VAL A CA  
2561 C C   . VAL A 340 ? 0.5682 0.4589 0.5091 0.0078  -0.0847 -0.0084 339 VAL A C   
2562 O O   . VAL A 340 ? 0.5341 0.4192 0.4636 0.0079  -0.0754 -0.0133 339 VAL A O   
2563 C CB  . VAL A 340 ? 0.5243 0.4012 0.4435 0.0036  -0.1065 -0.0008 339 VAL A CB  
2564 C CG1 . VAL A 340 ? 0.5889 0.4529 0.4839 -0.0006 -0.1031 -0.0084 339 VAL A CG1 
2565 C CG2 . VAL A 340 ? 0.5555 0.4243 0.4622 0.0045  -0.1139 0.0060  339 VAL A CG2 
2566 N N   . GLY A 341 ? 0.4774 0.3798 0.4379 0.0064  -0.0885 -0.0070 340 GLY A N   
2567 C CA  . GLY A 341 ? 0.5292 0.4366 0.4965 0.0052  -0.0814 -0.0107 340 GLY A CA  
2568 C C   . GLY A 341 ? 0.5264 0.4388 0.4978 0.0096  -0.0687 -0.0128 340 GLY A C   
2569 O O   . GLY A 341 ? 0.5044 0.4149 0.4707 0.0090  -0.0621 -0.0166 340 GLY A O   
2570 N N   . ASP A 342 ? 0.5230 0.4408 0.5035 0.0141  -0.0658 -0.0105 341 ASP A N   
2571 C CA  . ASP A 342 ? 0.4934 0.4140 0.4757 0.0174  -0.0549 -0.0135 341 ASP A CA  
2572 C C   . ASP A 342 ? 0.5082 0.4177 0.4723 0.0165  -0.0503 -0.0169 341 ASP A C   
2573 O O   . ASP A 342 ? 0.5138 0.4257 0.4768 0.0163  -0.0431 -0.0202 341 ASP A O   
2574 C CB  . ASP A 342 ? 0.4883 0.4133 0.4828 0.0226  -0.0531 -0.0114 341 ASP A CB  
2575 C CG  . ASP A 342 ? 0.5311 0.4714 0.5474 0.0247  -0.0522 -0.0091 341 ASP A CG  
2576 O OD1 . ASP A 342 ? 0.5248 0.4726 0.5461 0.0212  -0.0521 -0.0088 341 ASP A OD1 
2577 O OD2 . ASP A 342 ? 0.6370 0.5816 0.6662 0.0302  -0.0511 -0.0072 341 ASP A OD2 
2578 N N   . VAL A 343 ? 0.5085 0.4070 0.4584 0.0155  -0.0544 -0.0154 342 VAL A N   
2579 C CA  . VAL A 343 ? 0.5258 0.4154 0.4595 0.0143  -0.0486 -0.0178 342 VAL A CA  
2580 C C   . VAL A 343 ? 0.5246 0.4142 0.4530 0.0126  -0.0448 -0.0222 342 VAL A C   
2581 O O   . VAL A 343 ? 0.5323 0.4245 0.4611 0.0129  -0.0372 -0.0247 342 VAL A O   
2582 C CB  . VAL A 343 ? 0.5338 0.4114 0.4507 0.0129  -0.0535 -0.0144 342 VAL A CB  
2583 C CG1 . VAL A 343 ? 0.5843 0.4542 0.4837 0.0109  -0.0460 -0.0170 342 VAL A CG1 
2584 C CG2 . VAL A 343 ? 0.4802 0.3558 0.4029 0.0156  -0.0557 -0.0093 342 VAL A CG2 
2585 N N   . LEU A 344 ? 0.5073 0.3937 0.4320 0.0106  -0.0510 -0.0229 343 LEU A N   
2586 C CA  . LEU A 344 ? 0.5346 0.4182 0.4551 0.0099  -0.0477 -0.0272 343 LEU A CA  
2587 C C   . LEU A 344 ? 0.5159 0.4105 0.4528 0.0110  -0.0439 -0.0272 343 LEU A C   
2588 O O   . LEU A 344 ? 0.5685 0.4628 0.5047 0.0120  -0.0387 -0.0296 343 LEU A O   
2589 C CB  . LEU A 344 ? 0.5593 0.4336 0.4709 0.0068  -0.0562 -0.0287 343 LEU A CB  
2590 C CG  . LEU A 344 ? 0.6083 0.4686 0.4957 0.0057  -0.0573 -0.0305 343 LEU A CG  
2591 C CD1 . LEU A 344 ? 0.6850 0.5394 0.5654 0.0017  -0.0706 -0.0285 343 LEU A CD1 
2592 C CD2 . LEU A 344 ? 0.6522 0.5028 0.5259 0.0066  -0.0503 -0.0371 343 LEU A CD2 
2593 N N   . LYS A 345 ? 0.4920 0.3966 0.4434 0.0111  -0.0461 -0.0239 344 LYS A N   
2594 C CA  . LYS A 345 ? 0.5102 0.4251 0.4735 0.0115  -0.0419 -0.0233 344 LYS A CA  
2595 C C   . LYS A 345 ? 0.5017 0.4202 0.4639 0.0134  -0.0346 -0.0250 344 LYS A C   
2596 O O   . LYS A 345 ? 0.4664 0.3892 0.4313 0.0134  -0.0315 -0.0253 344 LYS A O   
2597 C CB  . LYS A 345 ? 0.4980 0.4236 0.4760 0.0114  -0.0439 -0.0197 344 LYS A CB  
2598 C CG  . LYS A 345 ? 0.5603 0.4959 0.5475 0.0109  -0.0395 -0.0181 344 LYS A CG  
2599 C CD  . LYS A 345 ? 0.5819 0.5280 0.5841 0.0095  -0.0415 -0.0138 344 LYS A CD  
2600 C CE  . LYS A 345 ? 0.5717 0.5281 0.5804 0.0088  -0.0355 -0.0114 344 LYS A CE  
2601 N NZ  . LYS A 345 ? 0.7196 0.6889 0.7441 0.0086  -0.0340 -0.0074 344 LYS A NZ  
2602 N N   . VAL A 346 ? 0.4753 0.3915 0.4341 0.0144  -0.0329 -0.0255 345 VAL A N   
2603 C CA  . VAL A 346 ? 0.4881 0.4061 0.4455 0.0145  -0.0272 -0.0274 345 VAL A CA  
2604 C C   . VAL A 346 ? 0.4818 0.3974 0.4336 0.0139  -0.0242 -0.0288 345 VAL A C   
2605 O O   . VAL A 346 ? 0.4553 0.3775 0.4117 0.0137  -0.0210 -0.0295 345 VAL A O   
2606 C CB  . VAL A 346 ? 0.5080 0.4204 0.4622 0.0148  -0.0266 -0.0272 345 VAL A CB  
2607 C CG1 . VAL A 346 ? 0.4874 0.3993 0.4389 0.0129  -0.0216 -0.0290 345 VAL A CG1 
2608 C CG2 . VAL A 346 ? 0.4602 0.3763 0.4232 0.0171  -0.0272 -0.0268 345 VAL A CG2 
2609 N N   . GLY A 347 ? 0.5346 0.4412 0.4764 0.0139  -0.0250 -0.0294 346 GLY A N   
2610 C CA  . GLY A 347 ? 0.4996 0.4040 0.4370 0.0148  -0.0205 -0.0315 346 GLY A CA  
2611 C C   . GLY A 347 ? 0.4622 0.3705 0.4076 0.0164  -0.0210 -0.0318 346 GLY A C   
2612 O O   . GLY A 347 ? 0.5217 0.4346 0.4722 0.0182  -0.0167 -0.0322 346 GLY A O   
2613 N N   . ALA A 348 ? 0.4657 0.3730 0.4141 0.0156  -0.0266 -0.0306 347 ALA A N   
2614 C CA  . ALA A 348 ? 0.4758 0.3851 0.4316 0.0163  -0.0277 -0.0294 347 ALA A CA  
2615 C C   . ALA A 348 ? 0.5153 0.4371 0.4811 0.0164  -0.0260 -0.0264 347 ALA A C   
2616 O O   . ALA A 348 ? 0.5061 0.4305 0.4776 0.0177  -0.0258 -0.0244 347 ALA A O   
2617 C CB  . ALA A 348 ? 0.4847 0.3896 0.4420 0.0138  -0.0342 -0.0279 347 ALA A CB  
2618 N N   . TYR A 349 ? 0.5001 0.4284 0.4670 0.0150  -0.0252 -0.0261 348 TYR A N   
2619 C CA  . TYR A 349 ? 0.4940 0.4325 0.4659 0.0142  -0.0239 -0.0247 348 TYR A CA  
2620 C C   . TYR A 349 ? 0.4904 0.4329 0.4646 0.0149  -0.0217 -0.0251 348 TYR A C   
2621 O O   . TYR A 349 ? 0.5001 0.4505 0.4790 0.0145  -0.0229 -0.0226 348 TYR A O   
2622 C CB  . TYR A 349 ? 0.4855 0.4266 0.4561 0.0130  -0.0228 -0.0262 348 TYR A CB  
2623 C CG  . TYR A 349 ? 0.4949 0.4394 0.4689 0.0129  -0.0236 -0.0245 348 TYR A CG  
2624 C CD1 . TYR A 349 ? 0.5557 0.4995 0.5337 0.0124  -0.0265 -0.0214 348 TYR A CD1 
2625 C CD2 . TYR A 349 ? 0.5400 0.4883 0.5140 0.0130  -0.0209 -0.0263 348 TYR A CD2 
2626 C CE1 . TYR A 349 ? 0.6026 0.5523 0.5870 0.0117  -0.0264 -0.0188 348 TYR A CE1 
2627 C CE2 . TYR A 349 ? 0.6201 0.5736 0.5992 0.0137  -0.0196 -0.0247 348 TYR A CE2 
2628 C CZ  . TYR A 349 ? 0.6169 0.5725 0.6025 0.0128  -0.0223 -0.0203 348 TYR A CZ  
2629 O OH  . TYR A 349 ? 0.6466 0.6101 0.6406 0.0129  -0.0204 -0.0177 348 TYR A OH  
2630 N N   . VAL A 350 ? 0.4462 0.3845 0.4176 0.0157  -0.0185 -0.0274 349 VAL A N   
2631 C CA  . VAL A 350 ? 0.4274 0.3723 0.4050 0.0162  -0.0155 -0.0271 349 VAL A CA  
2632 C C   . VAL A 350 ? 0.4733 0.4212 0.4588 0.0199  -0.0162 -0.0247 349 VAL A C   
2633 O O   . VAL A 350 ? 0.4559 0.4142 0.4508 0.0200  -0.0176 -0.0218 349 VAL A O   
2634 C CB  . VAL A 350 ? 0.4562 0.3961 0.4290 0.0163  -0.0101 -0.0293 349 VAL A CB  
2635 C CG1 . VAL A 350 ? 0.3541 0.3035 0.3374 0.0173  -0.0057 -0.0283 349 VAL A CG1 
2636 C CG2 . VAL A 350 ? 0.4316 0.3679 0.3981 0.0125  -0.0101 -0.0301 349 VAL A CG2 
2637 N N   . PHE A 351 ? 0.4529 0.3907 0.4349 0.0228  -0.0164 -0.0255 350 PHE A N   
2638 C CA  . PHE A 351 ? 0.4894 0.4264 0.4791 0.0267  -0.0177 -0.0230 350 PHE A CA  
2639 C C   . PHE A 351 ? 0.5045 0.4470 0.4982 0.0246  -0.0234 -0.0175 350 PHE A C   
2640 O O   . PHE A 351 ? 0.4878 0.4355 0.4904 0.0270  -0.0255 -0.0128 350 PHE A O   
2641 C CB  . PHE A 351 ? 0.4529 0.3741 0.4355 0.0293  -0.0169 -0.0264 350 PHE A CB  
2642 C CG  . PHE A 351 ? 0.5038 0.4182 0.4782 0.0315  -0.0103 -0.0320 350 PHE A CG  
2643 C CD1 . PHE A 351 ? 0.4541 0.3716 0.4356 0.0369  -0.0035 -0.0332 350 PHE A CD1 
2644 C CD2 . PHE A 351 ? 0.4999 0.4056 0.4596 0.0283  -0.0108 -0.0352 350 PHE A CD2 
2645 C CE1 . PHE A 351 ? 0.4961 0.4078 0.4684 0.0388  0.0046  -0.0382 350 PHE A CE1 
2646 C CE2 . PHE A 351 ? 0.5227 0.4214 0.4712 0.0297  -0.0045 -0.0396 350 PHE A CE2 
2647 C CZ  . PHE A 351 ? 0.4958 0.3973 0.4495 0.0348  0.0040  -0.0413 350 PHE A CZ  
2648 N N   . GLY A 352 ? 0.4679 0.4100 0.4555 0.0205  -0.0256 -0.0172 351 GLY A N   
2649 C CA  . GLY A 352 ? 0.4611 0.4088 0.4504 0.0181  -0.0292 -0.0118 351 GLY A CA  
2650 C C   . GLY A 352 ? 0.4552 0.4150 0.4464 0.0167  -0.0304 -0.0093 351 GLY A C   
2651 O O   . GLY A 352 ? 0.4675 0.4318 0.4611 0.0164  -0.0339 -0.0033 351 GLY A O   
2652 N N   . TYR A 353 ? 0.4673 0.4314 0.4564 0.0151  -0.0285 -0.0135 352 TYR A N   
2653 C CA  . TYR A 353 ? 0.4800 0.4547 0.4700 0.0124  -0.0312 -0.0122 352 TYR A CA  
2654 C C   . TYR A 353 ? 0.4452 0.4268 0.4472 0.0152  -0.0336 -0.0081 352 TYR A C   
2655 O O   . TYR A 353 ? 0.4010 0.3921 0.4055 0.0132  -0.0389 -0.0040 352 TYR A O   
2656 C CB  . TYR A 353 ? 0.4350 0.4101 0.4205 0.0090  -0.0290 -0.0180 352 TYR A CB  
2657 C CG  . TYR A 353 ? 0.4351 0.4076 0.4102 0.0063  -0.0281 -0.0208 352 TYR A CG  
2658 C CD1 . TYR A 353 ? 0.4525 0.4175 0.4248 0.0079  -0.0248 -0.0231 352 TYR A CD1 
2659 C CD2 . TYR A 353 ? 0.4649 0.4427 0.4330 0.0026  -0.0306 -0.0211 352 TYR A CD2 
2660 C CE1 . TYR A 353 ? 0.4709 0.4351 0.4372 0.0069  -0.0228 -0.0255 352 TYR A CE1 
2661 C CE2 . TYR A 353 ? 0.4724 0.4474 0.4305 0.0014  -0.0277 -0.0247 352 TYR A CE2 
2662 C CZ  . TYR A 353 ? 0.4748 0.4436 0.4338 0.0041  -0.0232 -0.0268 352 TYR A CZ  
2663 O OH  . TYR A 353 ? 0.5551 0.5226 0.5076 0.0042  -0.0191 -0.0302 352 TYR A OH  
2664 N N   . LEU A 354 ? 0.4379 0.4150 0.4473 0.0201  -0.0299 -0.0093 353 LEU A N   
2665 C CA  . LEU A 354 ? 0.4512 0.4348 0.4754 0.0249  -0.0310 -0.0050 353 LEU A CA  
2666 C C   . LEU A 354 ? 0.4338 0.4164 0.4607 0.0270  -0.0368 0.0024  353 LEU A C   
2667 O O   . LEU A 354 ? 0.4036 0.3965 0.4399 0.0279  -0.0424 0.0088  353 LEU A O   
2668 C CB  . LEU A 354 ? 0.3945 0.3710 0.4234 0.0307  -0.0238 -0.0090 353 LEU A CB  
2669 C CG  . LEU A 354 ? 0.4084 0.3888 0.4542 0.0383  -0.0227 -0.0054 353 LEU A CG  
2670 C CD1 . LEU A 354 ? 0.3628 0.3629 0.4249 0.0375  -0.0263 -0.0005 353 LEU A CD1 
2671 C CD2 . LEU A 354 ? 0.4047 0.3765 0.4507 0.0439  -0.0129 -0.0116 353 LEU A CD2 
2672 N N   . VAL A 355 ? 0.4034 0.3737 0.4225 0.0271  -0.0364 0.0026  354 VAL A N   
2673 C CA  . VAL A 355 ? 0.4383 0.4060 0.4587 0.0276  -0.0417 0.0108  354 VAL A CA  
2674 C C   . VAL A 355 ? 0.4713 0.4502 0.4856 0.0222  -0.0471 0.0164  354 VAL A C   
2675 O O   . VAL A 355 ? 0.4670 0.4508 0.4860 0.0232  -0.0533 0.0250  354 VAL A O   
2676 C CB  . VAL A 355 ? 0.4733 0.4268 0.4868 0.0262  -0.0403 0.0100  354 VAL A CB  
2677 C CG1 . VAL A 355 ? 0.4005 0.3522 0.4137 0.0243  -0.0453 0.0198  354 VAL A CG1 
2678 C CG2 . VAL A 355 ? 0.5132 0.4529 0.5304 0.0315  -0.0367 0.0047  354 VAL A CG2 
2679 N N   . ILE A 356 ? 0.4144 0.3964 0.4169 0.0167  -0.0451 0.0114  355 ILE A N   
2680 C CA  . ILE A 356 ? 0.4479 0.4389 0.4407 0.0115  -0.0493 0.0143  355 ILE A CA  
2681 C C   . ILE A 356 ? 0.4258 0.4283 0.4264 0.0114  -0.0554 0.0167  355 ILE A C   
2682 O O   . ILE A 356 ? 0.4718 0.4811 0.4697 0.0094  -0.0629 0.0241  355 ILE A O   
2683 C CB  . ILE A 356 ? 0.4862 0.4764 0.4662 0.0070  -0.0446 0.0063  355 ILE A CB  
2684 C CG1 . ILE A 356 ? 0.5472 0.5287 0.5249 0.0077  -0.0391 0.0043  355 ILE A CG1 
2685 C CG2 . ILE A 356 ? 0.3699 0.3664 0.3354 0.0017  -0.0476 0.0080  355 ILE A CG2 
2686 C CD1 . ILE A 356 ? 0.5647 0.5468 0.5355 0.0051  -0.0389 0.0106  355 ILE A CD1 
2687 N N   . ALA A 357 ? 0.4410 0.4467 0.4518 0.0130  -0.0528 0.0113  356 ALA A N   
2688 C CA  . ALA A 357 ? 0.4495 0.4688 0.4713 0.0117  -0.0586 0.0135  356 ALA A CA  
2689 C C   . ALA A 357 ? 0.4002 0.4259 0.4381 0.0174  -0.0647 0.0235  356 ALA A C   
2690 O O   . ALA A 357 ? 0.4064 0.4452 0.4514 0.0153  -0.0735 0.0290  356 ALA A O   
2691 C CB  . ALA A 357 ? 0.4052 0.4268 0.4369 0.0122  -0.0527 0.0068  356 ALA A CB  
2692 N N   . LYS A 358 ? 0.4114 0.4272 0.4556 0.0244  -0.0611 0.0260  357 LYS A N   
2693 C CA  . LYS A 358 ? 0.4255 0.4438 0.4854 0.0311  -0.0665 0.0357  357 LYS A CA  
2694 C C   . LYS A 358 ? 0.4374 0.4496 0.4864 0.0293  -0.0729 0.0450  357 LYS A C   
2695 O O   . LYS A 358 ? 0.4615 0.4724 0.5222 0.0350  -0.0779 0.0545  357 LYS A O   
2696 C CB  . LYS A 358 ? 0.4216 0.4298 0.4947 0.0404  -0.0585 0.0325  357 LYS A CB  
2697 C CG  . LYS A 358 ? 0.5225 0.5400 0.6107 0.0438  -0.0521 0.0267  357 LYS A CG  
2698 C CD  . LYS A 358 ? 0.5350 0.5742 0.6409 0.0430  -0.0598 0.0332  357 LYS A CD  
2699 C CE  . LYS A 358 ? 0.3940 0.4447 0.4998 0.0358  -0.0574 0.0269  357 LYS A CE  
2700 N NZ  . LYS A 358 ? 0.3807 0.4531 0.5036 0.0327  -0.0672 0.0335  357 LYS A NZ  
2701 N N   . ALA A 359 ? 0.4389 0.4474 0.4665 0.0218  -0.0720 0.0431  358 ALA A N   
2702 C CA  . ALA A 359 ? 0.4575 0.4615 0.4726 0.0186  -0.0761 0.0523  358 ALA A CA  
2703 C C   . ALA A 359 ? 0.4442 0.4341 0.4677 0.0242  -0.0747 0.0581  358 ALA A C   
2704 O O   . ALA A 359 ? 0.4287 0.4154 0.4505 0.0239  -0.0806 0.0699  358 ALA A O   
2705 C CB  . ALA A 359 ? 0.3902 0.4059 0.4022 0.0158  -0.0877 0.0625  358 ALA A CB  
2706 N N   . SER A 360 ? 0.4678 0.4477 0.4994 0.0288  -0.0674 0.0501  359 SER A N   
2707 C CA  . SER A 360 ? 0.3947 0.3581 0.4335 0.0337  -0.0664 0.0536  359 SER A CA  
2708 C C   . SER A 360 ? 0.4758 0.4298 0.5010 0.0269  -0.0644 0.0552  359 SER A C   
2709 O O   . SER A 360 ? 0.4621 0.4105 0.4819 0.0244  -0.0583 0.0463  359 SER A O   
2710 C CB  . SER A 360 ? 0.4143 0.3690 0.4632 0.0406  -0.0595 0.0435  359 SER A CB  
2711 O OG  . SER A 360 ? 0.5314 0.4670 0.5839 0.0442  -0.0589 0.0453  359 SER A OG  
2712 N N   . LEU A 361 ? 0.4983 0.4515 0.5187 0.0236  -0.0697 0.0676  360 LEU A N   
2713 C CA  . LEU A 361 ? 0.5192 0.4643 0.5304 0.0169  -0.0671 0.0712  360 LEU A CA  
2714 C C   . LEU A 361 ? 0.5499 0.4762 0.5698 0.0193  -0.0648 0.0680  360 LEU A C   
2715 O O   . LEU A 361 ? 0.5605 0.4820 0.5758 0.0137  -0.0609 0.0645  360 LEU A O   
2716 C CB  . LEU A 361 ? 0.4655 0.4125 0.4699 0.0130  -0.0731 0.0870  360 LEU A CB  
2717 C CG  . LEU A 361 ? 0.4922 0.4354 0.4864 0.0044  -0.0694 0.0931  360 LEU A CG  
2718 C CD1 . LEU A 361 ? 0.5153 0.4664 0.5014 -0.0001 -0.0609 0.0819  360 LEU A CD1 
2719 C CD2 . LEU A 361 ? 0.5426 0.4920 0.5242 -0.0004 -0.0741 0.1081  360 LEU A CD2 
2720 N N   . ARG A 362 ? 0.4747 0.3900 0.5077 0.0275  -0.0673 0.0686  361 ARG A N   
2721 C CA  . ARG A 362 ? 0.5086 0.4024 0.5468 0.0292  -0.0656 0.0646  361 ARG A CA  
2722 C C   . ARG A 362 ? 0.5171 0.4082 0.5514 0.0290  -0.0593 0.0492  361 ARG A C   
2723 O O   . ARG A 362 ? 0.5562 0.4356 0.5866 0.0239  -0.0583 0.0457  361 ARG A O   
2724 C CB  . ARG A 362 ? 0.5093 0.3899 0.5618 0.0394  -0.0687 0.0680  361 ARG A CB  
2725 C CG  . ARG A 362 ? 0.5474 0.4363 0.6099 0.0493  -0.0658 0.0606  361 ARG A CG  
2726 C CD  . ARG A 362 ? 0.5299 0.4013 0.6075 0.0606  -0.0656 0.0604  361 ARG A CD  
2727 N NE  . ARG A 362 ? 0.5737 0.4579 0.6649 0.0706  -0.0623 0.0561  361 ARG A NE  
2728 C CZ  . ARG A 362 ? 0.6228 0.4969 0.7296 0.0827  -0.0591 0.0535  361 ARG A CZ  
2729 N NH1 . ARG A 362 ? 0.6115 0.4593 0.7211 0.0870  -0.0595 0.0539  361 ARG A NH1 
2730 N NH2 . ARG A 362 ? 0.6670 0.5577 0.7882 0.0908  -0.0550 0.0502  361 ARG A NH2 
2731 N N   . PHE A 363 ? 0.4705 0.3724 0.5056 0.0336  -0.0557 0.0410  362 PHE A N   
2732 C CA  . PHE A 363 ? 0.4869 0.3860 0.5160 0.0329  -0.0501 0.0280  362 PHE A CA  
2733 C C   . PHE A 363 ? 0.4537 0.3617 0.4726 0.0242  -0.0489 0.0265  362 PHE A C   
2734 O O   . PHE A 363 ? 0.4619 0.3633 0.4758 0.0215  -0.0469 0.0191  362 PHE A O   
2735 C CB  . PHE A 363 ? 0.4987 0.4073 0.5321 0.0394  -0.0459 0.0210  362 PHE A CB  
2736 C CG  . PHE A 363 ? 0.4582 0.3535 0.4995 0.0486  -0.0424 0.0158  362 PHE A CG  
2737 C CD1 . PHE A 363 ? 0.4450 0.3225 0.4784 0.0489  -0.0387 0.0060  362 PHE A CD1 
2738 C CD2 . PHE A 363 ? 0.5099 0.4103 0.5667 0.0572  -0.0430 0.0207  362 PHE A CD2 
2739 C CE1 . PHE A 363 ? 0.5604 0.4237 0.5981 0.0578  -0.0340 -0.0002 362 PHE A CE1 
2740 C CE2 . PHE A 363 ? 0.5036 0.3917 0.5689 0.0671  -0.0380 0.0153  362 PHE A CE2 
2741 C CZ  . PHE A 363 ? 0.5349 0.4035 0.5893 0.0675  -0.0327 0.0042  362 PHE A CZ  
2742 N N   . TYR A 364 ? 0.4476 0.3701 0.4628 0.0201  -0.0504 0.0334  363 TYR A N   
2743 C CA  . TYR A 364 ? 0.4407 0.3713 0.4476 0.0130  -0.0478 0.0322  363 TYR A CA  
2744 C C   . TYR A 364 ? 0.4506 0.3719 0.4588 0.0075  -0.0485 0.0358  363 TYR A C   
2745 O O   . TYR A 364 ? 0.4268 0.3487 0.4336 0.0040  -0.0462 0.0304  363 TYR A O   
2746 C CB  . TYR A 364 ? 0.4795 0.4251 0.4796 0.0100  -0.0485 0.0387  363 TYR A CB  
2747 C CG  . TYR A 364 ? 0.5069 0.4621 0.4982 0.0049  -0.0436 0.0348  363 TYR A CG  
2748 C CD1 . TYR A 364 ? 0.5111 0.4677 0.5006 -0.0007 -0.0411 0.0401  363 TYR A CD1 
2749 C CD2 . TYR A 364 ? 0.5188 0.4816 0.5053 0.0060  -0.0408 0.0262  363 TYR A CD2 
2750 C CE1 . TYR A 364 ? 0.5457 0.5120 0.5296 -0.0037 -0.0352 0.0363  363 TYR A CE1 
2751 C CE2 . TYR A 364 ? 0.5420 0.5116 0.5215 0.0028  -0.0359 0.0222  363 TYR A CE2 
2752 C CZ  . TYR A 364 ? 0.5405 0.5123 0.5191 -0.0013 -0.0327 0.0270  363 TYR A CZ  
2753 O OH  . TYR A 364 ? 0.5725 0.5520 0.5466 -0.0029 -0.0264 0.0227  363 TYR A OH  
2754 N N   . ILE A 365 ? 0.4970 0.4095 0.5095 0.0063  -0.0523 0.0456  364 ILE A N   
2755 C CA  . ILE A 365 ? 0.4570 0.3594 0.4729 -0.0002 -0.0537 0.0500  364 ILE A CA  
2756 C C   . ILE A 365 ? 0.4842 0.3714 0.5025 0.0006  -0.0547 0.0397  364 ILE A C   
2757 O O   . ILE A 365 ? 0.5143 0.4007 0.5338 -0.0058 -0.0551 0.0377  364 ILE A O   
2758 C CB  . ILE A 365 ? 0.4224 0.3149 0.4426 -0.0013 -0.0582 0.0630  364 ILE A CB  
2759 C CG1 . ILE A 365 ? 0.4194 0.3272 0.4331 -0.0051 -0.0574 0.0746  364 ILE A CG1 
2760 C CG2 . ILE A 365 ? 0.4400 0.3167 0.4661 -0.0081 -0.0607 0.0661  364 ILE A CG2 
2761 C CD1 . ILE A 365 ? 0.4352 0.3366 0.4506 -0.0023 -0.0630 0.0869  364 ILE A CD1 
2762 N N   . LEU A 366 ? 0.4749 0.3505 0.4938 0.0084  -0.0552 0.0331  365 LEU A N   
2763 C CA  . LEU A 366 ? 0.5088 0.3673 0.5253 0.0092  -0.0559 0.0227  365 LEU A CA  
2764 C C   . LEU A 366 ? 0.4981 0.3657 0.5080 0.0072  -0.0533 0.0137  365 LEU A C   
2765 O O   . LEU A 366 ? 0.5442 0.4029 0.5512 0.0026  -0.0561 0.0087  365 LEU A O   
2766 C CB  . LEU A 366 ? 0.5049 0.3505 0.5227 0.0193  -0.0544 0.0172  365 LEU A CB  
2767 C CG  . LEU A 366 ? 0.6259 0.4590 0.6525 0.0230  -0.0577 0.0260  365 LEU A CG  
2768 C CD1 . LEU A 366 ? 0.6767 0.4974 0.7070 0.0346  -0.0547 0.0192  365 LEU A CD1 
2769 C CD2 . LEU A 366 ? 0.5492 0.3646 0.5773 0.0151  -0.0630 0.0308  365 LEU A CD2 
2770 N N   . ALA A 367 ? 0.4583 0.3428 0.4656 0.0102  -0.0492 0.0121  366 ALA A N   
2771 C CA  . ALA A 367 ? 0.5324 0.4247 0.5340 0.0086  -0.0470 0.0050  366 ALA A CA  
2772 C C   . ALA A 367 ? 0.5411 0.4411 0.5459 0.0009  -0.0486 0.0089  366 ALA A C   
2773 O O   . ALA A 367 ? 0.5796 0.4778 0.5828 -0.0018 -0.0504 0.0041  366 ALA A O   
2774 C CB  . ALA A 367 ? 0.4797 0.3869 0.4790 0.0124  -0.0425 0.0034  366 ALA A CB  
2775 N N   . GLU A 368 ? 0.5404 0.4498 0.5500 -0.0026 -0.0478 0.0184  367 GLU A N   
2776 C CA  . GLU A 368 ? 0.4822 0.4023 0.4972 -0.0093 -0.0470 0.0228  367 GLU A CA  
2777 C C   . GLU A 368 ? 0.5356 0.4448 0.5579 -0.0158 -0.0526 0.0247  367 GLU A C   
2778 O O   . GLU A 368 ? 0.4933 0.4079 0.5210 -0.0200 -0.0543 0.0230  367 GLU A O   
2779 C CB  . GLU A 368 ? 0.4903 0.4230 0.5056 -0.0114 -0.0432 0.0324  367 GLU A CB  
2780 C CG  . GLU A 368 ? 0.5903 0.5408 0.6072 -0.0140 -0.0373 0.0332  367 GLU A CG  
2781 C CD  . GLU A 368 ? 0.6220 0.5811 0.6303 -0.0087 -0.0328 0.0261  367 GLU A CD  
2782 O OE1 . GLU A 368 ? 0.7650 0.7178 0.7680 -0.0039 -0.0347 0.0202  367 GLU A OE1 
2783 O OE2 . GLU A 368 ? 0.6856 0.6577 0.6932 -0.0096 -0.0268 0.0262  367 GLU A OE2 
2784 N N   . VAL A 369 ? 0.5191 0.4124 0.5428 -0.0170 -0.0565 0.0286  368 VAL A N   
2785 C CA  . VAL A 369 ? 0.5142 0.3936 0.5441 -0.0244 -0.0631 0.0298  368 VAL A CA  
2786 C C   . VAL A 369 ? 0.5100 0.3777 0.5337 -0.0238 -0.0676 0.0180  368 VAL A C   
2787 O O   . VAL A 369 ? 0.4985 0.3641 0.5273 -0.0314 -0.0735 0.0175  368 VAL A O   
2788 C CB  . VAL A 369 ? 0.5185 0.3792 0.5499 -0.0247 -0.0662 0.0358  368 VAL A CB  
2789 C CG1 . VAL A 369 ? 0.5482 0.3895 0.5842 -0.0328 -0.0739 0.0348  368 VAL A CG1 
2790 C CG2 . VAL A 369 ? 0.5206 0.3931 0.5568 -0.0275 -0.0629 0.0497  368 VAL A CG2 
2791 N N   . SER A 370 ? 0.4616 0.3227 0.4740 -0.0153 -0.0652 0.0091  369 SER A N   
2792 C CA  . SER A 370 ? 0.4885 0.3388 0.4907 -0.0146 -0.0684 -0.0018 369 SER A CA  
2793 C C   . SER A 370 ? 0.5188 0.3849 0.5235 -0.0183 -0.0699 -0.0023 369 SER A C   
2794 O O   . SER A 370 ? 0.5432 0.4028 0.5461 -0.0237 -0.0772 -0.0057 369 SER A O   
2795 C CB  . SER A 370 ? 0.4845 0.3292 0.4752 -0.0048 -0.0629 -0.0098 369 SER A CB  
2796 O OG  . SER A 370 ? 0.5460 0.3735 0.5357 -0.0002 -0.0621 -0.0110 369 SER A OG  
2797 N N   . GLN A 371 ? 0.5075 0.3936 0.5160 -0.0152 -0.0636 0.0010  370 GLN A N   
2798 C CA  . GLN A 371 ? 0.5233 0.4241 0.5364 -0.0168 -0.0641 0.0008  370 GLN A CA  
2799 C C   . GLN A 371 ? 0.5115 0.4205 0.5404 -0.0254 -0.0688 0.0077  370 GLN A C   
2800 O O   . GLN A 371 ? 0.5345 0.4470 0.5681 -0.0288 -0.0748 0.0065  370 GLN A O   
2801 C CB  . GLN A 371 ? 0.5636 0.4812 0.5772 -0.0116 -0.0557 0.0021  370 GLN A CB  
2802 C CG  . GLN A 371 ? 0.5544 0.4678 0.5553 -0.0048 -0.0523 -0.0051 370 GLN A CG  
2803 C CD  . GLN A 371 ? 0.5877 0.5145 0.5886 -0.0009 -0.0451 -0.0039 370 GLN A CD  
2804 O OE1 . GLN A 371 ? 0.6098 0.5475 0.6136 -0.0003 -0.0425 -0.0041 370 GLN A OE1 
2805 N NE2 . GLN A 371 ? 0.5150 0.4405 0.5128 0.0019  -0.0423 -0.0027 370 GLN A NE2 
2806 N N   . PHE A 372 ? 0.4960 0.4089 0.5341 -0.0293 -0.0665 0.0161  371 PHE A N   
2807 C CA  . PHE A 372 ? 0.4968 0.4197 0.5526 -0.0383 -0.0695 0.0243  371 PHE A CA  
2808 C C   . PHE A 372 ? 0.5252 0.4325 0.5831 -0.0461 -0.0814 0.0217  371 PHE A C   
2809 O O   . PHE A 372 ? 0.4948 0.4115 0.5648 -0.0518 -0.0874 0.0232  371 PHE A O   
2810 C CB  . PHE A 372 ? 0.5297 0.4569 0.5915 -0.0415 -0.0642 0.0346  371 PHE A CB  
2811 C CG  . PHE A 372 ? 0.5302 0.4647 0.6107 -0.0525 -0.0670 0.0442  371 PHE A CG  
2812 C CD1 . PHE A 372 ? 0.5808 0.5404 0.6765 -0.0549 -0.0603 0.0509  371 PHE A CD1 
2813 C CD2 . PHE A 372 ? 0.4891 0.4049 0.5728 -0.0606 -0.0757 0.0466  371 PHE A CD2 
2814 C CE1 . PHE A 372 ? 0.5632 0.5323 0.6792 -0.0656 -0.0619 0.0607  371 PHE A CE1 
2815 C CE2 . PHE A 372 ? 0.5535 0.4764 0.6562 -0.0722 -0.0786 0.0562  371 PHE A CE2 
2816 C CZ  . PHE A 372 ? 0.5886 0.5397 0.7085 -0.0750 -0.0715 0.0639  371 PHE A CZ  
2817 N N   . THR A 373 ? 0.5167 0.3996 0.5632 -0.0462 -0.0853 0.0176  372 THR A N   
2818 C CA  . THR A 373 ? 0.5300 0.3937 0.5754 -0.0544 -0.0969 0.0141  372 THR A CA  
2819 C C   . THR A 373 ? 0.5246 0.3850 0.5599 -0.0539 -0.1040 0.0049  372 THR A C   
2820 O O   . THR A 373 ? 0.5494 0.4095 0.5919 -0.0631 -0.1148 0.0054  372 THR A O   
2821 C CB  . THR A 373 ? 0.5079 0.3436 0.5413 -0.0524 -0.0979 0.0100  372 THR A CB  
2822 O OG1 . THR A 373 ? 0.5223 0.3619 0.5636 -0.0513 -0.0914 0.0199  372 THR A OG1 
2823 C CG2 . THR A 373 ? 0.5732 0.3869 0.6064 -0.0628 -0.1100 0.0070  372 THR A CG2 
2824 N N   . LEU A 374 ? 0.5444 0.4029 0.5633 -0.0441 -0.0987 -0.0026 373 LEU A N   
2825 C CA  . LEU A 374 ? 0.5510 0.4065 0.5579 -0.0435 -0.1048 -0.0099 373 LEU A CA  
2826 C C   . LEU A 374 ? 0.5242 0.4032 0.5486 -0.0471 -0.1087 -0.0035 373 LEU A C   
2827 O O   . LEU A 374 ? 0.5007 0.3776 0.5258 -0.0534 -0.1206 -0.0047 373 LEU A O   
2828 C CB  . LEU A 374 ? 0.4502 0.3023 0.4390 -0.0327 -0.0964 -0.0168 373 LEU A CB  
2829 C CG  . LEU A 374 ? 0.5705 0.3977 0.5405 -0.0286 -0.0939 -0.0254 373 LEU A CG  
2830 C CD1 . LEU A 374 ? 0.4463 0.2754 0.4041 -0.0182 -0.0835 -0.0300 373 LEU A CD1 
2831 C CD2 . LEU A 374 ? 0.5147 0.3194 0.4686 -0.0346 -0.1046 -0.0336 373 LEU A CD2 
2832 N N   . LEU A 375 ? 0.5364 0.4378 0.5753 -0.0428 -0.0992 0.0032  374 LEU A N   
2833 C CA  . LEU A 375 ? 0.5117 0.4365 0.5707 -0.0446 -0.1008 0.0094  374 LEU A CA  
2834 C C   . LEU A 375 ? 0.5038 0.4339 0.5829 -0.0563 -0.1107 0.0159  374 LEU A C   
2835 O O   . LEU A 375 ? 0.5233 0.4644 0.6150 -0.0600 -0.1196 0.0182  374 LEU A O   
2836 C CB  . LEU A 375 ? 0.4768 0.4217 0.5464 -0.0384 -0.0871 0.0145  374 LEU A CB  
2837 C CG  . LEU A 375 ? 0.4778 0.4447 0.5625 -0.0343 -0.0840 0.0175  374 LEU A CG  
2838 C CD1 . LEU A 375 ? 0.5528 0.5127 0.6246 -0.0291 -0.0893 0.0113  374 LEU A CD1 
2839 C CD2 . LEU A 375 ? 0.6000 0.5803 0.6872 -0.0277 -0.0692 0.0195  374 LEU A CD2 
2840 N N   . MET A 376 ? 0.5024 0.4240 0.5854 -0.0627 -0.1103 0.0194  375 MET A N   
2841 C CA  . MET A 376 ? 0.4831 0.4099 0.5873 -0.0755 -0.1193 0.0267  375 MET A CA  
2842 C C   . MET A 376 ? 0.5401 0.4474 0.6351 -0.0836 -0.1364 0.0203  375 MET A C   
2843 O O   . MET A 376 ? 0.5656 0.4838 0.6794 -0.0932 -0.1476 0.0250  375 MET A O   
2844 C CB  . MET A 376 ? 0.5554 0.4767 0.6654 -0.0805 -0.1139 0.0334  375 MET A CB  
2845 C CG  . MET A 376 ? 0.6005 0.5466 0.7242 -0.0764 -0.0997 0.0423  375 MET A CG  
2846 S SD  . MET A 376 ? 0.8102 0.7875 0.9597 -0.0772 -0.1016 0.0464  375 MET A SD  
2847 C CE  . MET A 376 ? 0.6878 0.6915 0.8500 -0.0719 -0.0823 0.0550  375 MET A CE  
2848 N N   . VAL A 377 ? 0.5156 0.3945 0.5823 -0.0804 -0.1386 0.0095  376 VAL A N   
2849 C CA  . VAL A 377 ? 0.5793 0.4366 0.6312 -0.0880 -0.1543 0.0016  376 VAL A CA  
2850 C C   . VAL A 377 ? 0.5212 0.3912 0.5729 -0.0875 -0.1630 0.0008  376 VAL A C   
2851 O O   . VAL A 377 ? 0.5331 0.4040 0.5922 -0.0980 -0.1789 0.0021  376 VAL A O   
2852 C CB  . VAL A 377 ? 0.5923 0.4171 0.6119 -0.0823 -0.1516 -0.0108 376 VAL A CB  
2853 C CG1 . VAL A 377 ? 0.5764 0.3782 0.5740 -0.0888 -0.1664 -0.0210 376 VAL A CG1 
2854 C CG2 . VAL A 377 ? 0.6003 0.4099 0.6232 -0.0840 -0.1465 -0.0088 376 VAL A CG2 
2855 N N   . PHE A 378 ? 0.5487 0.4296 0.5937 -0.0757 -0.1536 -0.0003 377 PHE A N   
2856 C CA  . PHE A 378 ? 0.5481 0.4379 0.5904 -0.0739 -0.1617 -0.0005 377 PHE A CA  
2857 C C   . PHE A 378 ? 0.6116 0.5323 0.6896 -0.0774 -0.1659 0.0109  377 PHE A C   
2858 O O   . PHE A 378 ? 0.5446 0.4711 0.6291 -0.0829 -0.1810 0.0132  377 PHE A O   
2859 C CB  . PHE A 378 ? 0.5357 0.4246 0.5598 -0.0608 -0.1501 -0.0049 377 PHE A CB  
2860 C CG  . PHE A 378 ? 0.5903 0.4506 0.5782 -0.0581 -0.1499 -0.0164 377 PHE A CG  
2861 C CD1 . PHE A 378 ? 0.5088 0.3506 0.4762 -0.0649 -0.1644 -0.0225 377 PHE A CD1 
2862 C CD2 . PHE A 378 ? 0.5771 0.4297 0.5517 -0.0489 -0.1351 -0.0211 377 PHE A CD2 
2863 C CE1 . PHE A 378 ? 0.5375 0.3532 0.4702 -0.0620 -0.1620 -0.0336 377 PHE A CE1 
2864 C CE2 . PHE A 378 ? 0.5074 0.3361 0.4517 -0.0457 -0.1330 -0.0313 377 PHE A CE2 
2865 C CZ  . PHE A 378 ? 0.5834 0.3932 0.5059 -0.0519 -0.1455 -0.0379 377 PHE A CZ  
2866 N N   . ALA A 379 ? 0.5694 0.5108 0.6711 -0.0743 -0.1529 0.0185  378 ALA A N   
2867 C CA  . ALA A 379 ? 0.5599 0.5325 0.6979 -0.0766 -0.1538 0.0293  378 ALA A CA  
2868 C C   . ALA A 379 ? 0.5143 0.4905 0.6726 -0.0918 -0.1691 0.0348  378 ALA A C   
2869 O O   . ALA A 379 ? 0.5126 0.5065 0.6924 -0.0959 -0.1808 0.0404  378 ALA A O   
2870 C CB  . ALA A 379 ? 0.5055 0.4969 0.6598 -0.0706 -0.1348 0.0351  378 ALA A CB  
2871 N N   . HIS A 380 ? 0.5303 0.4898 0.6836 -0.1008 -0.1701 0.0337  379 HIS A N   
2872 C CA  . HIS A 380 ? 0.5403 0.4997 0.7119 -0.1172 -0.1853 0.0385  379 HIS A CA  
2873 C C   . HIS A 380 ? 0.5351 0.4808 0.6931 -0.1241 -0.2070 0.0324  379 HIS A C   
2874 O O   . HIS A 380 ? 0.6294 0.5848 0.8096 -0.1372 -0.2227 0.0382  379 HIS A O   
2875 C CB  . HIS A 380 ? 0.6163 0.5530 0.7792 -0.1243 -0.1820 0.0372  379 HIS A CB  
2876 C CG  . HIS A 380 ? 0.5941 0.5167 0.7633 -0.1418 -0.2001 0.0376  379 HIS A CG  
2877 N ND1 . HIS A 380 ? 0.6620 0.6052 0.8680 -0.1550 -0.2047 0.0499  379 HIS A ND1 
2878 C CD2 . HIS A 380 ? 0.6517 0.5404 0.7946 -0.1489 -0.2144 0.0267  379 HIS A CD2 
2879 C CE1 . HIS A 380 ? 0.6807 0.6031 0.8836 -0.1703 -0.2225 0.0469  379 HIS A CE1 
2880 N NE2 . HIS A 380 ? 0.7245 0.6125 0.8880 -0.1667 -0.2288 0.0322  379 HIS A NE2 
2881 N N   . TRP A 381 ? 0.6067 0.5312 0.7288 -0.1161 -0.2082 0.0216  380 TRP A N   
2882 C CA  . TRP A 381 ? 0.5496 0.4597 0.6523 -0.1220 -0.2281 0.0155  380 TRP A CA  
2883 C C   . TRP A 381 ? 0.6158 0.5514 0.7340 -0.1172 -0.2348 0.0224  380 TRP A C   
2884 O O   . TRP A 381 ? 0.5933 0.5376 0.7252 -0.1271 -0.2544 0.0268  380 TRP A O   
2885 C CB  . TRP A 381 ? 0.6412 0.5164 0.6967 -0.1158 -0.2248 0.0012  380 TRP A CB  
2886 C CG  . TRP A 381 ? 0.5921 0.4522 0.6201 -0.1193 -0.2419 -0.0055 380 TRP A CG  
2887 C CD1 . TRP A 381 ? 0.6498 0.5105 0.6833 -0.1328 -0.2648 -0.0035 380 TRP A CD1 
2888 C CD2 . TRP A 381 ? 0.6254 0.4677 0.6148 -0.1100 -0.2380 -0.0145 380 TRP A CD2 
2889 N NE1 . TRP A 381 ? 0.6427 0.4861 0.6407 -0.1323 -0.2759 -0.0109 380 TRP A NE1 
2890 C CE2 . TRP A 381 ? 0.6975 0.5293 0.6678 -0.1183 -0.2589 -0.0176 380 TRP A CE2 
2891 C CE3 . TRP A 381 ? 0.6836 0.5188 0.6533 -0.0961 -0.2192 -0.0197 380 TRP A CE3 
2892 C CZ2 . TRP A 381 ? 0.7106 0.5242 0.6405 -0.1130 -0.2601 -0.0252 380 TRP A CZ2 
2893 C CZ3 . TRP A 381 ? 0.6371 0.4556 0.5702 -0.0912 -0.2200 -0.0272 380 TRP A CZ3 
2894 C CH2 . TRP A 381 ? 0.6715 0.4791 0.5841 -0.0994 -0.2397 -0.0298 380 TRP A CH2 
2895 N N   . LEU A 382 ? 0.5535 0.5009 0.6711 -0.1022 -0.2197 0.0237  381 LEU A N   
2896 C CA  . LEU A 382 ? 0.5263 0.4892 0.6497 -0.0953 -0.2259 0.0282  381 LEU A CA  
2897 C C   . LEU A 382 ? 0.5957 0.5969 0.7666 -0.0925 -0.2229 0.0411  381 LEU A C   
2898 O O   . LEU A 382 ? 0.5812 0.5976 0.7669 -0.0912 -0.2352 0.0474  381 LEU A O   
2899 C CB  . LEU A 382 ? 0.5537 0.5054 0.6489 -0.0809 -0.2121 0.0221  381 LEU A CB  
2900 C CG  . LEU A 382 ? 0.6827 0.5999 0.7306 -0.0816 -0.2156 0.0099  381 LEU A CG  
2901 C CD1 . LEU A 382 ? 0.5320 0.4384 0.5601 -0.0702 -0.1947 0.0035  381 LEU A CD1 
2902 C CD2 . LEU A 382 ? 0.6514 0.5630 0.6807 -0.0818 -0.2312 0.0101  381 LEU A CD2 
2903 N N   . ILE A 383 ? 0.5727 0.5898 0.7673 -0.0907 -0.2064 0.0457  382 ILE A N   
2904 C CA  . ILE A 383 ? 0.4972 0.5512 0.7361 -0.0865 -0.1995 0.0571  382 ILE A CA  
2905 C C   . ILE A 383 ? 0.5413 0.6155 0.8155 -0.0994 -0.2180 0.0666  382 ILE A C   
2906 O O   . ILE A 383 ? 0.5339 0.6335 0.8370 -0.0949 -0.2237 0.0747  382 ILE A O   
2907 C CB  . ILE A 383 ? 0.5192 0.5839 0.7703 -0.0827 -0.1768 0.0594  382 ILE A CB  
2908 C CG1 . ILE A 383 ? 0.5610 0.6156 0.7870 -0.0677 -0.1590 0.0523  382 ILE A CG1 
2909 C CG2 . ILE A 383 ? 0.5015 0.6046 0.8011 -0.0826 -0.1709 0.0716  382 ILE A CG2 
2910 C CD1 . ILE A 383 ? 0.4727 0.5400 0.7094 -0.0628 -0.1371 0.0550  382 ILE A CD1 
2911 N N   . PRO A 384 ? 0.5794 0.6443 0.8554 -0.1156 -0.2283 0.0667  383 PRO A N   
2912 C CA  . PRO A 384 ? 0.5332 0.6202 0.8469 -0.1293 -0.2467 0.0767  383 PRO A CA  
2913 C C   . PRO A 384 ? 0.5663 0.6529 0.8758 -0.1313 -0.2706 0.0772  383 PRO A C   
2914 O O   . PRO A 384 ? 0.6312 0.7448 0.9793 -0.1385 -0.2852 0.0878  383 PRO A O   
2915 C CB  . PRO A 384 ? 0.6112 0.6771 0.9160 -0.1466 -0.2539 0.0736  383 PRO A CB  
2916 C CG  . PRO A 384 ? 0.5631 0.6095 0.8425 -0.1395 -0.2325 0.0669  383 PRO A CG  
2917 C CD  . PRO A 384 ? 0.5359 0.5712 0.7844 -0.1224 -0.2237 0.0588  383 PRO A CD  
2918 N N   . ALA A 385 ? 0.5379 0.5961 0.8025 -0.1252 -0.2753 0.0671  384 ALA A N   
2919 C CA  . ALA A 385 ? 0.5455 0.6004 0.7998 -0.1273 -0.2985 0.0680  384 ALA A CA  
2920 C C   . ALA A 385 ? 0.5879 0.6583 0.8493 -0.1104 -0.2932 0.0731  384 ALA A C   
2921 O O   . ALA A 385 ? 0.6818 0.7670 0.9597 -0.1114 -0.3119 0.0812  384 ALA A O   
2922 C CB  . ALA A 385 ? 0.6137 0.6260 0.8112 -0.1329 -0.3086 0.0541  384 ALA A CB  
2923 N N   . HIS A 386 ? 0.5729 0.6398 0.8232 -0.0951 -0.2694 0.0692  385 HIS A N   
2924 C CA  . HIS A 386 ? 0.5264 0.5998 0.7759 -0.0794 -0.2648 0.0721  385 HIS A CA  
2925 C C   . HIS A 386 ? 0.5317 0.6287 0.8114 -0.0653 -0.2408 0.0764  385 HIS A C   
2926 O O   . HIS A 386 ? 0.5416 0.6391 0.8172 -0.0513 -0.2334 0.0769  385 HIS A O   
2927 C CB  . HIS A 386 ? 0.5468 0.5854 0.7419 -0.0743 -0.2620 0.0612  385 HIS A CB  
2928 C CG  . HIS A 386 ? 0.6794 0.6943 0.8406 -0.0857 -0.2851 0.0569  385 HIS A CG  
2929 N ND1 . HIS A 386 ? 0.6883 0.6682 0.7992 -0.0881 -0.2825 0.0442  385 HIS A ND1 
2930 C CD2 . HIS A 386 ? 0.6335 0.6548 0.8032 -0.0956 -0.3114 0.0632  385 HIS A CD2 
2931 C CE1 . HIS A 386 ? 0.6494 0.6135 0.7363 -0.0988 -0.3051 0.0420  385 HIS A CE1 
2932 N NE2 . HIS A 386 ? 0.6635 0.6518 0.7844 -0.1041 -0.3240 0.0535  385 HIS A NE2 
2933 N N   . GLY A 387 ? 0.5029 0.6179 0.8109 -0.0691 -0.2284 0.0794  386 GLY A N   
2934 C CA  . GLY A 387 ? 0.4722 0.6122 0.8105 -0.0564 -0.2066 0.0840  386 GLY A CA  
2935 C C   . GLY A 387 ? 0.5045 0.6267 0.8122 -0.0430 -0.1867 0.0750  386 GLY A C   
2936 O O   . GLY A 387 ? 0.5403 0.6357 0.8102 -0.0457 -0.1818 0.0656  386 GLY A O   
2937 N N   . ALA A 388 ? 0.5105 0.6477 0.8361 -0.0282 -0.1753 0.0780  387 ALA A N   
2938 C CA  . ALA A 388 ? 0.4650 0.5873 0.7655 -0.0160 -0.1562 0.0698  387 ALA A CA  
2939 C C   . ALA A 388 ? 0.5405 0.6308 0.7963 -0.0152 -0.1644 0.0624  387 ALA A C   
2940 O O   . ALA A 388 ? 0.4761 0.5472 0.7018 -0.0118 -0.1517 0.0537  387 ALA A O   
2941 C CB  . ALA A 388 ? 0.4574 0.5995 0.7861 -0.0005 -0.1443 0.0738  387 ALA A CB  
2942 N N   . LEU A 389 ? 0.4831 0.5681 0.7341 -0.0188 -0.1855 0.0663  388 LEU A N   
2943 C CA  . LEU A 389 ? 0.4901 0.5446 0.6962 -0.0197 -0.1931 0.0598  388 LEU A CA  
2944 C C   . LEU A 389 ? 0.4801 0.5129 0.6546 -0.0306 -0.1929 0.0507  388 LEU A C   
2945 O O   . LEU A 389 ? 0.5823 0.5917 0.7210 -0.0280 -0.1852 0.0422  388 LEU A O   
2946 C CB  . LEU A 389 ? 0.5633 0.6172 0.7693 -0.0225 -0.2170 0.0669  388 LEU A CB  
2947 C CG  . LEU A 389 ? 0.6415 0.6641 0.7984 -0.0263 -0.2272 0.0611  388 LEU A CG  
2948 C CD1 . LEU A 389 ? 0.6124 0.6207 0.7478 -0.0141 -0.2136 0.0580  388 LEU A CD1 
2949 C CD2 . LEU A 389 ? 0.6725 0.6963 0.8294 -0.0327 -0.2539 0.0689  388 LEU A CD2 
2950 N N   . GLY A 390 ? 0.5031 0.5433 0.6924 -0.0426 -0.2010 0.0526  389 GLY A N   
2951 C CA  . GLY A 390 ? 0.5550 0.5737 0.7180 -0.0520 -0.1995 0.0441  389 GLY A CA  
2952 C C   . GLY A 390 ? 0.5618 0.5769 0.7181 -0.0461 -0.1766 0.0388  389 GLY A C   
2953 O O   . GLY A 390 ? 0.5099 0.5013 0.6342 -0.0471 -0.1716 0.0301  389 GLY A O   
2954 N N   . ALA A 391 ? 0.4891 0.5278 0.6753 -0.0395 -0.1625 0.0441  390 ALA A N   
2955 C CA  . ALA A 391 ? 0.5117 0.5476 0.6897 -0.0340 -0.1417 0.0396  390 ALA A CA  
2956 C C   . ALA A 391 ? 0.4968 0.5140 0.6436 -0.0244 -0.1340 0.0319  390 ALA A C   
2957 O O   . ALA A 391 ? 0.5240 0.5267 0.6489 -0.0237 -0.1241 0.0254  390 ALA A O   
2958 C CB  . ALA A 391 ? 0.4356 0.5001 0.6486 -0.0283 -0.1279 0.0462  390 ALA A CB  
2959 N N   . ALA A 392 ? 0.5042 0.5218 0.6500 -0.0174 -0.1390 0.0336  391 ALA A N   
2960 C CA  . ALA A 392 ? 0.5044 0.5034 0.6210 -0.0100 -0.1329 0.0274  391 ALA A CA  
2961 C C   . ALA A 392 ? 0.5217 0.4952 0.6025 -0.0164 -0.1411 0.0210  391 ALA A C   
2962 O O   . ALA A 392 ? 0.5270 0.4849 0.5830 -0.0134 -0.1315 0.0142  391 ALA A O   
2963 C CB  . ALA A 392 ? 0.4902 0.4946 0.6158 -0.0014 -0.1369 0.0323  391 ALA A CB  
2964 N N   . GLN A 393 ? 0.5099 0.4791 0.5878 -0.0252 -0.1587 0.0229  392 GLN A N   
2965 C CA  . GLN A 393 ? 0.5260 0.4695 0.5682 -0.0315 -0.1658 0.0155  392 GLN A CA  
2966 C C   . GLN A 393 ? 0.5279 0.4613 0.5613 -0.0353 -0.1564 0.0087  392 GLN A C   
2967 O O   . GLN A 393 ? 0.5654 0.4786 0.5696 -0.0340 -0.1507 0.0007  392 GLN A O   
2968 C CB  . GLN A 393 ? 0.6325 0.5735 0.6736 -0.0414 -0.1878 0.0184  392 GLN A CB  
2969 C CG  . GLN A 393 ? 0.5752 0.5220 0.6191 -0.0380 -0.2000 0.0257  392 GLN A CG  
2970 C CD  . GLN A 393 ? 0.6169 0.5696 0.6713 -0.0485 -0.2232 0.0312  392 GLN A CD  
2971 O OE1 . GLN A 393 ? 0.6549 0.6164 0.7290 -0.0572 -0.2283 0.0322  392 GLN A OE1 
2972 N NE2 . GLN A 393 ? 0.6115 0.5589 0.6521 -0.0485 -0.2384 0.0354  392 GLN A NE2 
2973 N N   . ALA A 394 ? 0.5025 0.4503 0.5622 -0.0397 -0.1544 0.0126  393 ALA A N   
2974 C CA  . ALA A 394 ? 0.4966 0.4349 0.5503 -0.0430 -0.1462 0.0082  393 ALA A CA  
2975 C C   . ALA A 394 ? 0.5284 0.4638 0.5714 -0.0336 -0.1283 0.0043  393 ALA A C   
2976 O O   . ALA A 394 ? 0.4910 0.4089 0.5137 -0.0334 -0.1231 -0.0022 393 ALA A O   
2977 C CB  . ALA A 394 ? 0.4866 0.4432 0.5725 -0.0497 -0.1463 0.0156  393 ALA A CB  
2978 N N   . TYR A 395 ? 0.5132 0.4653 0.5705 -0.0256 -0.1191 0.0081  394 TYR A N   
2979 C CA  . TYR A 395 ? 0.4679 0.4175 0.5147 -0.0176 -0.1040 0.0043  394 TYR A CA  
2980 C C   . TYR A 395 ? 0.4849 0.4147 0.5018 -0.0145 -0.1038 -0.0025 394 TYR A C   
2981 O O   . TYR A 395 ? 0.5166 0.4368 0.5192 -0.0122 -0.0950 -0.0075 394 TYR A O   
2982 C CB  . TYR A 395 ? 0.5190 0.4873 0.5849 -0.0101 -0.0961 0.0085  394 TYR A CB  
2983 C CG  . TYR A 395 ? 0.4562 0.4211 0.5105 -0.0025 -0.0828 0.0041  394 TYR A CG  
2984 C CD1 . TYR A 395 ? 0.5246 0.4946 0.5810 -0.0015 -0.0713 0.0032  394 TYR A CD1 
2985 C CD2 . TYR A 395 ? 0.5202 0.4765 0.5612 0.0029  -0.0826 0.0016  394 TYR A CD2 
2986 C CE1 . TYR A 395 ? 0.5362 0.5032 0.5819 0.0043  -0.0610 -0.0009 394 TYR A CE1 
2987 C CE2 . TYR A 395 ? 0.5314 0.4844 0.5632 0.0084  -0.0715 -0.0023 394 TYR A CE2 
2988 C CZ  . TYR A 395 ? 0.5202 0.4788 0.5545 0.0089  -0.0612 -0.0040 394 TYR A CZ  
2989 O OH  . TYR A 395 ? 0.6147 0.5703 0.6398 0.0131  -0.0519 -0.0080 394 TYR A OH  
2990 N N   . MET A 396 ? 0.4963 0.4207 0.5042 -0.0146 -0.1136 -0.0018 395 MET A N   
2991 C CA  . MET A 396 ? 0.5208 0.4270 0.4991 -0.0123 -0.1125 -0.0072 395 MET A CA  
2992 C C   . MET A 396 ? 0.5529 0.4401 0.5093 -0.0173 -0.1145 -0.0144 395 MET A C   
2993 O O   . MET A 396 ? 0.5287 0.4051 0.4679 -0.0139 -0.1049 -0.0201 395 MET A O   
2994 C CB  . MET A 396 ? 0.4780 0.3818 0.4497 -0.0122 -0.1237 -0.0033 395 MET A CB  
2995 C CG  . MET A 396 ? 0.5577 0.4411 0.4950 -0.0122 -0.1237 -0.0082 395 MET A CG  
2996 S SD  . MET A 396 ? 0.7139 0.5910 0.6372 -0.0144 -0.1402 -0.0025 395 MET A SD  
2997 C CE  . MET A 396 ? 0.6496 0.5084 0.5471 -0.0246 -0.1529 -0.0091 395 MET A CE  
2998 N N   . ALA A 397 ? 0.5035 0.3859 0.4609 -0.0253 -0.1271 -0.0144 396 ALA A N   
2999 C CA  . ALA A 397 ? 0.5552 0.4164 0.4914 -0.0298 -0.1289 -0.0224 396 ALA A CA  
3000 C C   . ALA A 397 ? 0.5955 0.4556 0.5375 -0.0269 -0.1163 -0.0250 396 ALA A C   
3001 O O   . ALA A 397 ? 0.6124 0.4559 0.5351 -0.0246 -0.1102 -0.0324 396 ALA A O   
3002 C CB  . ALA A 397 ? 0.5628 0.4194 0.5026 -0.0403 -0.1455 -0.0218 396 ALA A CB  
3003 N N   . THR A 398 ? 0.5250 0.4033 0.4934 -0.0264 -0.1118 -0.0186 397 THR A N   
3004 C CA  . THR A 398 ? 0.5359 0.4142 0.5098 -0.0241 -0.1013 -0.0191 397 THR A CA  
3005 C C   . THR A 398 ? 0.5853 0.4593 0.5453 -0.0158 -0.0893 -0.0235 397 THR A C   
3006 O O   . THR A 398 ? 0.5565 0.4190 0.5080 -0.0139 -0.0840 -0.0278 397 THR A O   
3007 C CB  . THR A 398 ? 0.5300 0.4303 0.5312 -0.0246 -0.0972 -0.0107 397 THR A CB  
3008 O OG1 . THR A 398 ? 0.5018 0.4063 0.5189 -0.0335 -0.1072 -0.0060 397 THR A OG1 
3009 C CG2 . THR A 398 ? 0.4356 0.3368 0.4388 -0.0213 -0.0861 -0.0101 397 THR A CG2 
3010 N N   . TYR A 399 ? 0.5250 0.4078 0.4840 -0.0110 -0.0852 -0.0222 398 TYR A N   
3011 C CA  . TYR A 399 ? 0.5790 0.4605 0.5291 -0.0046 -0.0740 -0.0253 398 TYR A CA  
3012 C C   . TYR A 399 ? 0.5627 0.4283 0.4883 -0.0030 -0.0730 -0.0314 398 TYR A C   
3013 O O   . TYR A 399 ? 0.5801 0.4433 0.4990 0.0014  -0.0635 -0.0344 398 TYR A O   
3014 C CB  . TYR A 399 ? 0.5685 0.4660 0.5303 -0.0007 -0.0686 -0.0212 398 TYR A CB  
3015 C CG  . TYR A 399 ? 0.5187 0.4301 0.4991 -0.0007 -0.0640 -0.0171 398 TYR A CG  
3016 C CD1 . TYR A 399 ? 0.5426 0.4550 0.5222 0.0017  -0.0562 -0.0180 398 TYR A CD1 
3017 C CD2 . TYR A 399 ? 0.4967 0.4205 0.4951 -0.0035 -0.0678 -0.0117 398 TYR A CD2 
3018 C CE1 . TYR A 399 ? 0.5125 0.4363 0.5049 0.0010  -0.0524 -0.0137 398 TYR A CE1 
3019 C CE2 . TYR A 399 ? 0.5289 0.4652 0.5415 -0.0040 -0.0621 -0.0076 398 TYR A CE2 
3020 C CZ  . TYR A 399 ? 0.5431 0.4783 0.5505 -0.0020 -0.0547 -0.0086 398 TYR A CZ  
3021 O OH  . TYR A 399 ? 0.5146 0.4611 0.5322 -0.0030 -0.0494 -0.0039 398 TYR A OH  
3022 N N   . ILE A 400 ? 0.6021 0.4574 0.5141 -0.0070 -0.0827 -0.0329 399 ILE A N   
3023 C CA  . ILE A 400 ? 0.6189 0.4558 0.5034 -0.0066 -0.0813 -0.0399 399 ILE A CA  
3024 C C   . ILE A 400 ? 0.5941 0.4185 0.4738 -0.0058 -0.0766 -0.0465 399 ILE A C   
3025 O O   . ILE A 400 ? 0.6211 0.4396 0.4909 -0.0006 -0.0659 -0.0511 399 ILE A O   
3026 C CB  . ILE A 400 ? 0.6104 0.4372 0.4788 -0.0124 -0.0948 -0.0403 399 ILE A CB  
3027 C CG1 . ILE A 400 ? 0.6344 0.4709 0.5050 -0.0115 -0.0985 -0.0333 399 ILE A CG1 
3028 C CG2 . ILE A 400 ? 0.6316 0.4364 0.4678 -0.0129 -0.0929 -0.0492 399 ILE A CG2 
3029 C CD1 . ILE A 400 ? 0.7111 0.5419 0.5715 -0.0175 -0.1150 -0.0310 399 ILE A CD1 
3030 N N   . VAL A 401 ? 0.5952 0.4156 0.4838 -0.0107 -0.0843 -0.0463 400 VAL A N   
3031 C CA  . VAL A 401 ? 0.5557 0.3614 0.4411 -0.0098 -0.0810 -0.0520 400 VAL A CA  
3032 C C   . VAL A 401 ? 0.5714 0.3879 0.4728 -0.0032 -0.0696 -0.0490 400 VAL A C   
3033 O O   . VAL A 401 ? 0.5867 0.3934 0.4824 0.0021  -0.0618 -0.0539 400 VAL A O   
3034 C CB  . VAL A 401 ? 0.5670 0.3656 0.4603 -0.0181 -0.0930 -0.0511 400 VAL A CB  
3035 C CG1 . VAL A 401 ? 0.5758 0.3582 0.4692 -0.0166 -0.0893 -0.0556 400 VAL A CG1 
3036 C CG2 . VAL A 401 ? 0.6296 0.4153 0.5043 -0.0254 -0.1060 -0.0552 400 VAL A CG2 
3037 N N   . TYR A 402 ? 0.5131 0.3500 0.4344 -0.0032 -0.0685 -0.0409 401 TYR A N   
3038 C CA  . TYR A 402 ? 0.5500 0.3966 0.4847 0.0016  -0.0600 -0.0375 401 TYR A CA  
3039 C C   . TYR A 402 ? 0.6084 0.4577 0.5362 0.0085  -0.0499 -0.0405 401 TYR A C   
3040 O O   . TYR A 402 ? 0.5588 0.4068 0.4903 0.0133  -0.0435 -0.0414 401 TYR A O   
3041 C CB  . TYR A 402 ? 0.4737 0.3401 0.4272 -0.0005 -0.0607 -0.0292 401 TYR A CB  
3042 C CG  . TYR A 402 ? 0.5161 0.3922 0.4794 0.0035  -0.0534 -0.0255 401 TYR A CG  
3043 C CD1 . TYR A 402 ? 0.5097 0.3784 0.4770 0.0044  -0.0527 -0.0243 401 TYR A CD1 
3044 C CD2 . TYR A 402 ? 0.5473 0.4386 0.5151 0.0062  -0.0480 -0.0232 401 TYR A CD2 
3045 C CE1 . TYR A 402 ? 0.5263 0.4044 0.5021 0.0079  -0.0478 -0.0196 401 TYR A CE1 
3046 C CE2 . TYR A 402 ? 0.4942 0.3942 0.4688 0.0088  -0.0430 -0.0199 401 TYR A CE2 
3047 C CZ  . TYR A 402 ? 0.5355 0.4298 0.5140 0.0096  -0.0434 -0.0176 401 TYR A CZ  
3048 O OH  . TYR A 402 ? 0.5303 0.4336 0.5149 0.0120  -0.0401 -0.0131 401 TYR A OH  
3049 N N   . PHE A 403 ? 0.5912 0.4448 0.5107 0.0087  -0.0486 -0.0410 402 PHE A N   
3050 C CA  . PHE A 403 ? 0.5991 0.4553 0.5127 0.0136  -0.0390 -0.0432 402 PHE A CA  
3051 C C   . PHE A 403 ? 0.5204 0.3612 0.4196 0.0171  -0.0336 -0.0504 402 PHE A C   
3052 O O   . PHE A 403 ? 0.5444 0.3888 0.4486 0.0225  -0.0245 -0.0515 402 PHE A O   
3053 C CB  . PHE A 403 ? 0.5812 0.4411 0.4868 0.0122  -0.0395 -0.0416 402 PHE A CB  
3054 C CG  . PHE A 403 ? 0.5549 0.4170 0.4544 0.0155  -0.0296 -0.0429 402 PHE A CG  
3055 C CD1 . PHE A 403 ? 0.5215 0.3976 0.4351 0.0173  -0.0240 -0.0399 402 PHE A CD1 
3056 C CD2 . PHE A 403 ? 0.5446 0.3950 0.4235 0.0158  -0.0260 -0.0470 402 PHE A CD2 
3057 C CE1 . PHE A 403 ? 0.5617 0.4412 0.4727 0.0190  -0.0155 -0.0403 402 PHE A CE1 
3058 C CE2 . PHE A 403 ? 0.6192 0.4733 0.4944 0.0180  -0.0157 -0.0471 402 PHE A CE2 
3059 C CZ  . PHE A 403 ? 0.5640 0.4333 0.4570 0.0193  -0.0107 -0.0435 402 PHE A CZ  
3060 N N   . SER A 404 ? 0.5723 0.3959 0.4538 0.0141  -0.0391 -0.0556 403 SER A N   
3061 C CA  . SER A 404 ? 0.6251 0.4310 0.4905 0.0178  -0.0332 -0.0643 403 SER A CA  
3062 C C   . SER A 404 ? 0.5856 0.3881 0.4652 0.0224  -0.0299 -0.0652 403 SER A C   
3063 O O   . SER A 404 ? 0.6124 0.4122 0.4921 0.0297  -0.0194 -0.0691 403 SER A O   
3064 C CB  . SER A 404 ? 0.5975 0.3834 0.4398 0.0122  -0.0423 -0.0702 403 SER A CB  
3065 O OG  . SER A 404 ? 0.6392 0.4261 0.4648 0.0090  -0.0448 -0.0691 403 SER A OG  
3066 N N   . LEU A 405 ? 0.5724 0.3758 0.4658 0.0186  -0.0384 -0.0608 404 LEU A N   
3067 C CA  . LEU A 405 ? 0.5462 0.3463 0.4541 0.0226  -0.0365 -0.0593 404 LEU A CA  
3068 C C   . LEU A 405 ? 0.5700 0.3885 0.4944 0.0291  -0.0280 -0.0541 404 LEU A C   
3069 O O   . LEU A 405 ? 0.5523 0.3669 0.4834 0.0363  -0.0219 -0.0555 404 LEU A O   
3070 C CB  . LEU A 405 ? 0.5411 0.3417 0.4611 0.0156  -0.0469 -0.0530 404 LEU A CB  
3071 C CG  . LEU A 405 ? 0.7029 0.5011 0.6390 0.0185  -0.0463 -0.0483 404 LEU A CG  
3072 C CD1 . LEU A 405 ? 0.5474 0.3211 0.4751 0.0240  -0.0431 -0.0567 404 LEU A CD1 
3073 C CD2 . LEU A 405 ? 0.6862 0.4867 0.6333 0.0099  -0.0557 -0.0407 404 LEU A CD2 
3074 N N   . CYS A 406 ? 0.5523 0.3904 0.4837 0.0268  -0.0281 -0.0482 405 CYS A N   
3075 C CA  . CYS A 406 ? 0.5707 0.4263 0.5161 0.0312  -0.0218 -0.0436 405 CYS A CA  
3076 C C   . CYS A 406 ? 0.5784 0.4331 0.5198 0.0378  -0.0113 -0.0487 405 CYS A C   
3077 O O   . CYS A 406 ? 0.6192 0.4811 0.5746 0.0438  -0.0062 -0.0467 405 CYS A O   
3078 C CB  . CYS A 406 ? 0.6212 0.4936 0.5702 0.0269  -0.0235 -0.0388 405 CYS A CB  
3079 S SG  . CYS A 406 ? 0.5875 0.4709 0.5495 0.0221  -0.0306 -0.0307 405 CYS A SG  
3080 N N   . CYS A 407 ? 0.5437 0.3909 0.4668 0.0366  -0.0080 -0.0543 406 CYS A N   
3081 C CA  . CYS A 407 ? 0.5357 0.3820 0.4534 0.0423  0.0039  -0.0591 406 CYS A CA  
3082 C C   . CYS A 407 ? 0.6001 0.4330 0.5193 0.0500  0.0091  -0.0648 406 CYS A C   
3083 O O   . CYS A 407 ? 0.5745 0.4159 0.5080 0.0575  0.0181  -0.0643 406 CYS A O   
3084 C CB  . CYS A 407 ? 0.5746 0.4118 0.4674 0.0387  0.0059  -0.0637 406 CYS A CB  
3085 S SG  . CYS A 407 ? 0.6401 0.4914 0.5320 0.0317  0.0021  -0.0568 406 CYS A SG  
3086 N N   . GLY A 408 ? 0.5337 0.3452 0.4400 0.0482  0.0031  -0.0701 407 GLY A N   
3087 C CA  . GLY A 408 ? 0.5897 0.3835 0.4955 0.0557  0.0078  -0.0768 407 GLY A CA  
3088 C C   . GLY A 408 ? 0.5895 0.3918 0.5225 0.0618  0.0076  -0.0701 407 GLY A C   
3089 O O   . GLY A 408 ? 0.6359 0.4360 0.5784 0.0718  0.0167  -0.0728 407 GLY A O   
3090 N N   . VAL A 409 ? 0.5504 0.3630 0.4965 0.0563  -0.0025 -0.0607 408 VAL A N   
3091 C CA  . VAL A 409 ? 0.5898 0.4104 0.5592 0.0611  -0.0042 -0.0527 408 VAL A CA  
3092 C C   . VAL A 409 ? 0.6348 0.4788 0.6209 0.0668  0.0031  -0.0482 408 VAL A C   
3093 O O   . VAL A 409 ? 0.5466 0.3948 0.5510 0.0752  0.0061  -0.0449 408 VAL A O   
3094 C CB  . VAL A 409 ? 0.5972 0.4233 0.5729 0.0529  -0.0158 -0.0435 408 VAL A CB  
3095 C CG1 . VAL A 409 ? 0.6208 0.4579 0.6179 0.0570  -0.0180 -0.0333 408 VAL A CG1 
3096 C CG2 . VAL A 409 ? 0.6731 0.4765 0.6377 0.0473  -0.0232 -0.0469 408 VAL A CG2 
3097 N N   . PHE A 410 ? 0.5482 0.4075 0.5297 0.0622  0.0056  -0.0477 409 PHE A N   
3098 C CA  . PHE A 410 ? 0.5093 0.3903 0.5067 0.0660  0.0122  -0.0440 409 PHE A CA  
3099 C C   . PHE A 410 ? 0.6046 0.4823 0.6053 0.0758  0.0253  -0.0502 409 PHE A C   
3100 O O   . PHE A 410 ? 0.6260 0.5184 0.6494 0.0828  0.0298  -0.0461 409 PHE A O   
3101 C CB  . PHE A 410 ? 0.5124 0.4063 0.5026 0.0582  0.0123  -0.0428 409 PHE A CB  
3102 C CG  . PHE A 410 ? 0.5338 0.4495 0.5405 0.0598  0.0181  -0.0389 409 PHE A CG  
3103 C CD1 . PHE A 410 ? 0.4991 0.4323 0.5232 0.0577  0.0114  -0.0309 409 PHE A CD1 
3104 C CD2 . PHE A 410 ? 0.5236 0.4424 0.5282 0.0627  0.0301  -0.0431 409 PHE A CD2 
3105 C CE1 . PHE A 410 ? 0.4375 0.3910 0.4780 0.0578  0.0149  -0.0273 409 PHE A CE1 
3106 C CE2 . PHE A 410 ? 0.5063 0.4468 0.5294 0.0630  0.0351  -0.0386 409 PHE A CE2 
3107 C CZ  . PHE A 410 ? 0.4925 0.4504 0.5344 0.0603  0.0267  -0.0309 409 PHE A CZ  
3108 N N   . LEU A 411 ? 0.5976 0.4567 0.5759 0.0764  0.0316  -0.0601 410 LEU A N   
3109 C CA  . LEU A 411 ? 0.6134 0.4678 0.5916 0.0862  0.0464  -0.0673 410 LEU A CA  
3110 C C   . LEU A 411 ? 0.6047 0.4498 0.5996 0.0972  0.0477  -0.0681 410 LEU A C   
3111 O O   . LEU A 411 ? 0.6301 0.4857 0.6444 0.1075  0.0583  -0.0678 410 LEU A O   
3112 C CB  . LEU A 411 ? 0.6487 0.4815 0.5936 0.0838  0.0517  -0.0783 410 LEU A CB  
3113 C CG  . LEU A 411 ? 0.7090 0.5513 0.6385 0.0764  0.0555  -0.0777 410 LEU A CG  
3114 C CD1 . LEU A 411 ? 0.7326 0.5559 0.6312 0.0777  0.0658  -0.0885 410 LEU A CD1 
3115 C CD2 . LEU A 411 ? 0.6532 0.5241 0.6067 0.0778  0.0628  -0.0701 410 LEU A CD2 
3116 N N   . LEU A 412 ? 0.6384 0.4643 0.6280 0.0952  0.0371  -0.0682 411 LEU A N   
3117 C CA  . LEU A 412 ? 0.6103 0.4248 0.6163 0.1052  0.0369  -0.0674 411 LEU A CA  
3118 C C   . LEU A 412 ? 0.6415 0.4809 0.6804 0.1096  0.0334  -0.0545 411 LEU A C   
3119 O O   . LEU A 412 ? 0.6296 0.4708 0.6896 0.1218  0.0392  -0.0531 411 LEU A O   
3120 C CB  . LEU A 412 ? 0.6373 0.4265 0.6314 0.0995  0.0248  -0.0684 411 LEU A CB  
3121 C CG  . LEU A 412 ? 0.6018 0.3610 0.5651 0.0966  0.0266  -0.0823 411 LEU A CG  
3122 C CD1 . LEU A 412 ? 0.6072 0.3477 0.5624 0.0873  0.0120  -0.0806 411 LEU A CD1 
3123 C CD2 . LEU A 412 ? 0.6736 0.4133 0.6344 0.1099  0.0396  -0.0936 411 LEU A CD2 
3124 N N   . TRP A 413 ? 0.6075 0.4662 0.6508 0.1001  0.0238  -0.0449 412 TRP A N   
3125 C CA  . TRP A 413 ? 0.5272 0.4096 0.5976 0.1024  0.0185  -0.0327 412 TRP A CA  
3126 C C   . TRP A 413 ? 0.5839 0.4899 0.6728 0.1083  0.0289  -0.0321 412 TRP A C   
3127 O O   . TRP A 413 ? 0.5437 0.4628 0.6599 0.1172  0.0294  -0.0255 412 TRP A O   
3128 C CB  . TRP A 413 ? 0.5223 0.4165 0.5875 0.0900  0.0066  -0.0248 412 TRP A CB  
3129 C CG  . TRP A 413 ? 0.5726 0.4932 0.6590 0.0894  0.0010  -0.0137 412 TRP A CG  
3130 C CD1 . TRP A 413 ? 0.6205 0.5461 0.7220 0.0915  -0.0085 -0.0029 412 TRP A CD1 
3131 C CD2 . TRP A 413 ? 0.6270 0.5715 0.7199 0.0852  0.0033  -0.0121 412 TRP A CD2 
3132 N NE1 . TRP A 413 ? 0.5599 0.5114 0.6756 0.0889  -0.0130 0.0049  412 TRP A NE1 
3133 C CE2 . TRP A 413 ? 0.6506 0.6139 0.7622 0.0847  -0.0059 -0.0010 412 TRP A CE2 
3134 C CE3 . TRP A 413 ? 0.6050 0.5558 0.6890 0.0812  0.0115  -0.0184 412 TRP A CE3 
3135 C CZ2 . TRP A 413 ? 0.5717 0.5592 0.6936 0.0798  -0.0076 0.0027  412 TRP A CZ2 
3136 C CZ3 . TRP A 413 ? 0.5668 0.5414 0.6627 0.0765  0.0107  -0.0139 412 TRP A CZ3 
3137 C CH2 . TRP A 413 ? 0.5581 0.5506 0.6729 0.0756  0.0009  -0.0041 412 TRP A CH2 
3138 N N   . ARG A 414 ? 0.6175 0.5295 0.6932 0.1034  0.0369  -0.0379 413 ARG A N   
3139 C CA  . ARG A 414 ? 0.6009 0.5365 0.6942 0.1069  0.0475  -0.0367 413 ARG A CA  
3140 C C   . ARG A 414 ? 0.5592 0.4909 0.6661 0.1216  0.0618  -0.0420 413 ARG A C   
3141 O O   . ARG A 414 ? 0.6192 0.5739 0.7557 0.1285  0.0676  -0.0367 413 ARG A O   
3142 C CB  . ARG A 414 ? 0.5571 0.4957 0.6300 0.0976  0.0531  -0.0412 413 ARG A CB  
3143 C CG  . ARG A 414 ? 0.5782 0.5322 0.6614 0.1017  0.0691  -0.0433 413 ARG A CG  
3144 C CD  . ARG A 414 ? 0.5757 0.5616 0.6908 0.1001  0.0663  -0.0330 413 ARG A CD  
3145 N NE  . ARG A 414 ? 0.6579 0.6614 0.7853 0.1021  0.0817  -0.0337 413 ARG A NE  
3146 C CZ  . ARG A 414 ? 0.6700 0.6922 0.8296 0.1122  0.0906  -0.0306 413 ARG A CZ  
3147 N NH1 . ARG A 414 ? 0.5854 0.6099 0.7679 0.1223  0.0848  -0.0264 413 ARG A NH1 
3148 N NH2 . ARG A 414 ? 0.7332 0.7728 0.9036 0.1124  0.1057  -0.0307 413 ARG A NH2 
3149 N N   . ARG A 415 ? 0.6060 0.5090 0.6924 0.1266  0.0678  -0.0527 414 ARG A N   
3150 C CA  . ARG A 415 ? 0.6264 0.5216 0.7235 0.1419  0.0825  -0.0595 414 ARG A CA  
3151 C C   . ARG A 415 ? 0.6933 0.5803 0.8128 0.1526  0.0760  -0.0546 414 ARG A C   
3152 O O   . ARG A 415 ? 0.6859 0.5659 0.8187 0.1673  0.0878  -0.0598 414 ARG A O   
3153 C CB  . ARG A 415 ? 0.6912 0.5569 0.7523 0.1423  0.0927  -0.0749 414 ARG A CB  
3154 C CG  . ARG A 415 ? 0.8422 0.6724 0.8888 0.1465  0.0876  -0.0824 414 ARG A CG  
3155 C CD  . ARG A 415 ? 1.0592 0.8620 1.0745 0.1505  0.1014  -0.0993 414 ARG A CD  
3156 N NE  . ARG A 415 ? 1.1022 0.8678 1.0949 0.1491  0.0933  -0.1077 414 ARG A NE  
3157 C CZ  . ARG A 415 ? 1.1153 0.8632 1.1223 0.1579  0.0894  -0.1077 414 ARG A CZ  
3158 N NH1 . ARG A 415 ? 1.0145 0.7780 1.0586 0.1707  0.0933  -0.0998 414 ARG A NH1 
3159 N NH2 . ARG A 415 ? 1.1306 0.8438 1.1150 0.1536  0.0809  -0.1154 414 ARG A NH2 
3160 N N   . ARG A 416 ? 0.6287 0.5167 0.7531 0.1460  0.0583  -0.0444 415 ARG A N   
3161 C CA  . ARG A 416 ? 0.6786 0.5599 0.8243 0.1544  0.0498  -0.0364 415 ARG A CA  
3162 C C   . ARG A 416 ? 0.7166 0.5600 0.8484 0.1624  0.0540  -0.0469 415 ARG A C   
3163 O O   . ARG A 416 ? 0.7836 0.6192 0.9344 0.1776  0.0612  -0.0485 415 ARG A O   
3164 C CB  . ARG A 416 ? 0.6956 0.6045 0.8818 0.1663  0.0536  -0.0274 415 ARG A CB  
3165 C CG  . ARG A 416 ? 0.6726 0.6183 0.8724 0.1580  0.0512  -0.0194 415 ARG A CG  
3166 C CD  . ARG A 416 ? 0.6959 0.6707 0.9387 0.1695  0.0548  -0.0106 415 ARG A CD  
3167 N NE  . ARG A 416 ? 0.7708 0.7795 1.0261 0.1601  0.0525  -0.0040 415 ARG A NE  
3168 C CZ  . ARG A 416 ? 0.7179 0.7497 0.9925 0.1638  0.0663  -0.0056 415 ARG A CZ  
3169 N NH1 . ARG A 416 ? 0.7341 0.7608 1.0180 0.1779  0.0850  -0.0136 415 ARG A NH1 
3170 N NH2 . ARG A 416 ? 0.6381 0.6984 0.9229 0.1528  0.0618  0.0009  415 ARG A NH2 
3171 N N   . ALA A 417 ? 0.8262 0.6457 0.9254 0.1516  0.0486  -0.0540 416 ALA A N   
3172 C CA  . ALA A 417 ? 0.8264 0.6074 0.9070 0.1560  0.0515  -0.0659 416 ALA A CA  
3173 C C   . ALA A 417 ? 0.8351 0.5992 0.9329 0.1624  0.0421  -0.0584 416 ALA A C   
3174 O O   . ALA A 417 ? 0.8840 0.6182 0.9783 0.1721  0.0476  -0.0675 416 ALA A O   
3175 C CB  . ALA A 417 ? 0.8262 0.5892 0.8705 0.1408  0.0450  -0.0732 416 ALA A CB  
3176 N N   . LEU A 418 ? 0.8827 0.6633 0.9969 0.1571  0.0281  -0.0420 417 LEU A N   
3177 C CA  . LEU A 418 ? 0.8899 0.6551 1.0191 0.1616  0.0178  -0.0320 417 LEU A CA  
3178 C C   . LEU A 418 ? 0.9187 0.6980 1.0846 0.1782  0.0208  -0.0231 417 LEU A C   
3179 O O   . LEU A 418 ? 0.9721 0.7387 1.1531 0.1837  0.0122  -0.0132 417 LEU A O   
3180 C CB  . LEU A 418 ? 0.8638 0.6383 0.9891 0.1467  0.0011  -0.0179 417 LEU A CB  
3181 C CG  . LEU A 418 ? 0.7932 0.5501 0.8887 0.1309  -0.0053 -0.0230 417 LEU A CG  
3182 C CD1 . LEU A 418 ? 0.7397 0.4997 0.8379 0.1206  -0.0202 -0.0074 417 LEU A CD1 
3183 C CD2 . LEU A 418 ? 0.7354 0.4532 0.8140 0.1336  -0.0011 -0.0373 417 LEU A CD2 
3184 N N   . GLU A 419 ? 0.8859 0.6917 1.0683 0.1861  0.0324  -0.0253 418 GLU A N   
3185 C CA  . GLU A 419 ? 0.9244 0.7483 1.1464 0.2022  0.0350  -0.0159 418 GLU A CA  
3186 C C   . GLU A 419 ? 0.9456 0.7534 1.1768 0.2206  0.0535  -0.0292 418 GLU A C   
3187 O O   . GLU A 419 ? 1.0070 0.8095 1.2666 0.2367  0.0546  -0.0240 418 GLU A O   
3188 C CB  . GLU A 419 ? 0.8866 0.7552 1.1279 0.1985  0.0344  -0.0070 418 GLU A CB  
3189 C CG  . GLU A 419 ? 0.8939 0.7772 1.1184 0.1792  0.0201  0.0010  418 GLU A CG  
3190 C CD  . GLU A 419 ? 0.9433 0.8283 1.1778 0.1759  0.0014  0.0183  418 GLU A CD  
3191 O OE1 . GLU A 419 ? 0.9781 0.8628 1.2402 0.1889  -0.0019 0.0275  418 GLU A OE1 
3192 O OE2 . GLU A 419 ? 0.9197 0.8064 1.1344 0.1606  -0.0095 0.0231  418 GLU A OE2 
3210 N N   . VAL B 7   ? 0.5299 1.3482 0.9744 0.0248  -0.0134 0.1105  5   VAL B N   
3211 C CA  . VAL B 7   ? 0.5975 1.4173 1.0540 0.0174  -0.0014 0.0906  5   VAL B CA  
3212 C C   . VAL B 7   ? 0.6132 1.3970 1.0860 0.0341  0.0105  0.0914  5   VAL B C   
3213 O O   . VAL B 7   ? 0.4802 1.2611 0.9715 0.0515  0.0056  0.1096  5   VAL B O   
3214 C CB  . VAL B 7   ? 0.4833 1.3615 0.9631 0.0077  -0.0115 0.0899  5   VAL B CB  
3215 C CG1 . VAL B 7   ? 0.5498 1.4465 1.0699 0.0260  -0.0179 0.1061  5   VAL B CG1 
3216 C CG2 . VAL B 7   ? 0.6346 1.5162 1.1116 -0.0110 0.0027  0.0626  5   VAL B CG2 
3217 N N   . GLU B 8   ? 0.8312 1.5850 1.2952 0.0281  0.0272  0.0715  6   GLU B N   
3218 C CA  . GLU B 8   ? 0.7359 1.4492 1.2061 0.0401  0.0405  0.0694  6   GLU B CA  
3219 C C   . GLU B 8   ? 0.7895 1.5162 1.2837 0.0356  0.0504  0.0577  6   GLU B C   
3220 O O   . GLU B 8   ? 0.8889 1.6451 1.3865 0.0199  0.0514  0.0446  6   GLU B O   
3221 C CB  . GLU B 8   ? 0.7255 1.3875 1.1633 0.0377  0.0522  0.0573  6   GLU B CB  
3222 C CG  . GLU B 8   ? 0.7281 1.3668 1.1490 0.0471  0.0463  0.0686  6   GLU B CG  
3223 C CD  . GLU B 8   ? 0.8451 1.4846 1.2413 0.0354  0.0433  0.0610  6   GLU B CD  
3224 O OE1 . GLU B 8   ? 0.8996 1.5604 1.2922 0.0197  0.0451  0.0483  6   GLU B OE1 
3225 O OE2 . GLU B 8   ? 0.7704 1.3897 1.1522 0.0409  0.0405  0.0661  6   GLU B OE2 
3226 N N   . SER B 9   ? 0.5902 1.2948 1.1010 0.0480  0.0594  0.0610  7   SER B N   
3227 C CA  . SER B 9   ? 0.5336 1.2447 1.0679 0.0441  0.0722  0.0487  7   SER B CA  
3228 C C   . SER B 9   ? 0.5937 1.2524 1.1202 0.0518  0.0889  0.0450  7   SER B C   
3229 O O   . SER B 9   ? 0.5272 1.1574 1.0435 0.0639  0.0870  0.0567  7   SER B O   
3230 C CB  . SER B 9   ? 0.5031 1.2662 1.0837 0.0513  0.0620  0.0597  7   SER B CB  
3231 O OG  . SER B 9   ? 0.6770 1.4381 1.2855 0.0522  0.0771  0.0495  7   SER B OG  
3232 N N   . GLY B 10  ? 0.6431 1.2894 1.1730 0.0428  0.1060  0.0279  8   GLY B N   
3233 C CA  . GLY B 10  ? 0.5670 1.1626 1.0842 0.0459  0.1235  0.0220  8   GLY B CA  
3234 C C   . GLY B 10  ? 0.5891 1.1374 1.0598 0.0369  0.1321  0.0108  8   GLY B C   
3235 O O   . GLY B 10  ? 0.5954 1.1477 1.0456 0.0292  0.1258  0.0070  8   GLY B O   
3236 N N   . GLY B 11  ? 0.6154 1.1175 1.0695 0.0377  0.1471  0.0054  9   GLY B N   
3237 C CA  . GLY B 11  ? 0.7052 1.1581 1.1148 0.0315  0.1545  -0.0025 9   GLY B CA  
3238 C C   . GLY B 11  ? 0.6419 1.0828 1.0395 0.0149  0.1710  -0.0211 9   GLY B C   
3239 O O   . GLY B 11  ? 0.6099 1.0853 1.0341 0.0059  0.1764  -0.0303 9   GLY B O   
3240 N N   . GLY B 12  ? 0.6607 1.0517 1.0175 0.0106  0.1789  -0.0264 10  GLY B N   
3241 C CA  . GLY B 12  ? 0.6795 1.0455 1.0161 -0.0048 0.1968  -0.0427 10  GLY B CA  
3242 C C   . GLY B 12  ? 0.6885 0.9925 0.9860 -0.0045 0.2078  -0.0431 10  GLY B C   
3243 O O   . GLY B 12  ? 0.7321 1.0143 1.0149 0.0071  0.1989  -0.0316 10  GLY B O   
3244 N N   . LEU B 13  ? 0.7097 0.9853 0.9884 -0.0187 0.2275  -0.0569 11  LEU B N   
3245 C CA  . LEU B 13  ? 0.6947 0.9094 0.9317 -0.0211 0.2392  -0.0574 11  LEU B CA  
3246 C C   . LEU B 13  ? 0.7685 0.9789 1.0182 -0.0195 0.2477  -0.0568 11  LEU B C   
3247 O O   . LEU B 13  ? 0.7456 0.9785 1.0247 -0.0277 0.2614  -0.0674 11  LEU B O   
3248 C CB  . LEU B 13  ? 0.8860 1.0696 1.0969 -0.0383 0.2594  -0.0723 11  LEU B CB  
3249 C CG  . LEU B 13  ? 0.9297 1.0439 1.0861 -0.0418 0.2693  -0.0708 11  LEU B CG  
3250 C CD1 . LEU B 13  ? 0.8279 0.9196 0.9599 -0.0256 0.2493  -0.0540 11  LEU B CD1 
3251 C CD2 . LEU B 13  ? 0.9578 1.0440 1.0888 -0.0562 0.2854  -0.0826 11  LEU B CD2 
3252 N N   . VAL B 14  ? 0.7862 0.9689 1.0156 -0.0098 0.2406  -0.0457 12  VAL B N   
3253 C CA  . VAL B 14  ? 0.8040 0.9793 1.0435 -0.0087 0.2497  -0.0454 12  VAL B CA  
3254 C C   . VAL B 14  ? 0.8780 0.9926 1.0651 -0.0135 0.2571  -0.0446 12  VAL B C   
3255 O O   . VAL B 14  ? 0.8101 0.8977 0.9612 -0.0086 0.2449  -0.0366 12  VAL B O   
3256 C CB  . VAL B 14  ? 0.7688 0.9778 1.0415 0.0075  0.2335  -0.0323 12  VAL B CB  
3257 C CG1 . VAL B 14  ? 0.7854 0.9772 1.0306 0.0183  0.2147  -0.0196 12  VAL B CG1 
3258 C CG2 . VAL B 14  ? 0.7236 0.9279 1.0144 0.0077  0.2467  -0.0342 12  VAL B CG2 
3259 N N   . GLN B 15  ? 0.9313 1.0254 1.1144 -0.0235 0.2771  -0.0533 13  GLN B N   
3260 C CA  . GLN B 15  ? 0.9967 1.0341 1.1277 -0.0304 0.2847  -0.0527 13  GLN B CA  
3261 C C   . GLN B 15  ? 0.9732 1.0070 1.0977 -0.0179 0.2686  -0.0398 13  GLN B C   
3262 O O   . GLN B 15  ? 0.9339 1.0025 1.0991 -0.0082 0.2632  -0.0357 13  GLN B O   
3263 C CB  . GLN B 15  ? 0.9490 0.9677 1.0795 -0.0468 0.3128  -0.0674 13  GLN B CB  
3264 C CG  . GLN B 15  ? 1.0655 1.0226 1.1354 -0.0586 0.3233  -0.0684 13  GLN B CG  
3265 C CD  . GLN B 15  ? 1.1527 1.0942 1.2262 -0.0753 0.3523  -0.0839 13  GLN B CD  
3266 O OE1 . GLN B 15  ? 1.1868 1.1570 1.3031 -0.0812 0.3683  -0.0969 13  GLN B OE1 
3267 N NE2 . GLN B 15  ? 1.1569 1.0545 1.1866 -0.0839 0.3596  -0.0835 13  GLN B NE2 
3268 N N   . ALA B 16  ? 0.9447 0.9365 1.0178 -0.0181 0.2606  -0.0330 14  ALA B N   
3269 C CA  . ALA B 16  ? 0.8247 0.8114 0.8874 -0.0088 0.2460  -0.0228 14  ALA B CA  
3270 C C   . ALA B 16  ? 0.9587 0.9431 1.0342 -0.0149 0.2617  -0.0288 14  ALA B C   
3271 O O   . ALA B 16  ? 1.0813 1.0364 1.1369 -0.0306 0.2833  -0.0394 14  ALA B O   
3272 C CB  . ALA B 16  ? 0.8619 0.8025 0.8652 -0.0104 0.2361  -0.0160 14  ALA B CB  
3273 N N   . GLY B 17  ? 0.9156 0.9291 1.0243 -0.0032 0.2526  -0.0227 15  GLY B N   
3274 C CA  . GLY B 17  ? 0.9059 0.9212 1.0355 -0.0067 0.2680  -0.0280 15  GLY B CA  
3275 C C   . GLY B 17  ? 1.0123 1.0703 1.2050 -0.0010 0.2770  -0.0313 15  GLY B C   
3276 O O   . GLY B 17  ? 1.0009 1.0697 1.2231 0.0030  0.2844  -0.0312 15  GLY B O   
3277 N N   . GLY B 18  ? 1.1605 1.2436 1.3754 -0.0006 0.2766  -0.0340 16  GLY B N   
3278 C CA  . GLY B 18  ? 1.1435 1.2716 1.4193 0.0052  0.2823  -0.0362 16  GLY B CA  
3279 C C   . GLY B 18  ? 1.0383 1.2077 1.3490 0.0236  0.2608  -0.0214 16  GLY B C   
3280 O O   . GLY B 18  ? 0.9164 1.0849 1.2064 0.0309  0.2410  -0.0114 16  GLY B O   
3281 N N   . SER B 19  ? 1.0095 1.2155 1.3751 0.0312  0.2654  -0.0200 17  SER B N   
3282 C CA  . SER B 19  ? 0.8735 1.1184 1.2735 0.0481  0.2467  -0.0048 17  SER B CA  
3283 C C   . SER B 19  ? 0.8413 1.1257 1.2572 0.0507  0.2317  -0.0017 17  SER B C   
3284 O O   . SER B 19  ? 0.8791 1.1661 1.2909 0.0398  0.2390  -0.0130 17  SER B O   
3285 C CB  . SER B 19  ? 0.8794 1.1443 1.3312 0.0566  0.2574  -0.0022 17  SER B CB  
3286 O OG  . SER B 19  ? 1.0060 1.2341 1.4428 0.0528  0.2728  -0.0062 17  SER B OG  
3287 N N   . LEU B 20  ? 0.7731 1.0876 1.2056 0.0636  0.2117  0.0129  18  LEU B N   
3288 C CA  . LEU B 20  ? 0.6426 0.9969 1.0887 0.0650  0.1964  0.0164  18  LEU B CA  
3289 C C   . LEU B 20  ? 0.6309 1.0216 1.1090 0.0800  0.1800  0.0336  18  LEU B C   
3290 O O   . LEU B 20  ? 0.6352 1.0110 1.1063 0.0885  0.1756  0.0434  18  LEU B O   
3291 C CB  . LEU B 20  ? 0.6878 1.0227 1.0887 0.0586  0.1869  0.0138  18  LEU B CB  
3292 C CG  . LEU B 20  ? 0.7325 1.0943 1.1348 0.0518  0.1798  0.0088  18  LEU B CG  
3293 C CD1 . LEU B 20  ? 0.7276 1.1386 1.1590 0.0602  0.1613  0.0205  18  LEU B CD1 
3294 C CD2 . LEU B 20  ? 0.6914 1.0609 1.1091 0.0398  0.1969  -0.0061 18  LEU B CD2 
3295 N N   . GLY B 21  ? 0.6457 1.0838 1.1576 0.0823  0.1712  0.0371  19  GLY B N   
3296 C CA  . GLY B 21  ? 0.6025 1.0759 1.1415 0.0957  0.1542  0.0553  19  GLY B CA  
3297 C C   . GLY B 21  ? 0.5251 1.0328 1.0586 0.0925  0.1355  0.0592  19  GLY B C   
3298 O O   . GLY B 21  ? 0.6594 1.1988 1.2091 0.0849  0.1346  0.0518  19  GLY B O   
3299 N N   . LEU B 22  ? 0.4700 0.9723 0.9808 0.0965  0.1218  0.0691  20  LEU B N   
3300 C CA  . LEU B 22  ? 0.4231 0.9572 0.9279 0.0928  0.1048  0.0734  20  LEU B CA  
3301 C C   . LEU B 22  ? 0.4069 0.9778 0.9404 0.1043  0.0903  0.0931  20  LEU B C   
3302 O O   . LEU B 22  ? 0.5106 1.0698 1.0558 0.1167  0.0915  0.1055  20  LEU B O   
3303 C CB  . LEU B 22  ? 0.5089 1.0156 0.9721 0.0890  0.0996  0.0710  20  LEU B CB  
3304 C CG  . LEU B 22  ? 0.5562 1.0233 0.9859 0.0794  0.1106  0.0549  20  LEU B CG  
3305 C CD1 . LEU B 22  ? 0.4421 0.8882 0.8394 0.0796  0.1025  0.0557  20  LEU B CD1 
3306 C CD2 . LEU B 22  ? 0.5250 1.0070 0.9560 0.0662  0.1164  0.0410  20  LEU B CD2 
3307 N N   . SER B 23  ? 0.3095 0.9242 0.8526 0.0992  0.0768  0.0960  21  SER B N   
3308 C CA  . SER B 23  ? 0.3560 1.0078 0.9211 0.1087  0.0602  0.1164  21  SER B CA  
3309 C C   . SER B 23  ? 0.3704 1.0466 0.9132 0.0981  0.0450  0.1173  21  SER B C   
3310 O O   . SER B 23  ? 0.4419 1.1226 0.9682 0.0831  0.0477  0.1007  21  SER B O   
3311 C CB  . SER B 23  ? 0.3566 1.0495 0.9696 0.1146  0.0581  0.1215  21  SER B CB  
3312 O OG  . SER B 23  ? 0.4608 1.1952 1.0792 0.1014  0.0507  0.1123  21  SER B OG  
3313 N N   . CYS B 24  ? 0.3057 0.9955 0.8471 0.1050  0.0309  0.1362  22  CYS B N   
3314 C CA  . CYS B 24  ? 0.4543 1.1664 0.9728 0.0939  0.0173  0.1379  22  CYS B CA  
3315 C C   . CYS B 24  ? 0.4102 1.1638 0.9477 0.1006  -0.0007 0.1606  22  CYS B C   
3316 O O   . CYS B 24  ? 0.3863 1.1302 0.9359 0.1162  -0.0032 0.1798  22  CYS B O   
3317 C CB  . CYS B 24  ? 0.4375 1.1124 0.9199 0.0919  0.0198  0.1357  22  CYS B CB  
3318 S SG  . CYS B 24  ? 0.6084 1.3066 1.0630 0.0781  0.0059  0.1380  22  CYS B SG  
3319 N N   . ALA B 25  ? 0.3164 1.1155 0.8557 0.0884  -0.0129 0.1588  23  ALA B N   
3320 C CA  . ALA B 25  ? 0.4387 1.2769 0.9886 0.0921  -0.0330 0.1798  23  ALA B CA  
3321 C C   . ALA B 25  ? 0.5014 1.3505 1.0166 0.0798  -0.0438 0.1850  23  ALA B C   
3322 O O   . ALA B 25  ? 0.5066 1.3461 0.9937 0.0628  -0.0374 0.1655  23  ALA B O   
3323 C CB  . ALA B 25  ? 0.3383 1.2158 0.9096 0.0848  -0.0408 0.1727  23  ALA B CB  
3324 N N   . ALA B 26  ? 0.4444 1.3078 0.9592 0.0880  -0.0589 0.2105  24  ALA B N   
3325 C CA  . ALA B 26  ? 0.5363 1.4037 1.0141 0.0757  -0.0682 0.2166  24  ALA B CA  
3326 C C   . ALA B 26  ? 0.7345 1.6553 1.2172 0.0720  -0.0911 0.2360  24  ALA B C   
3327 O O   . ALA B 26  ? 0.7247 1.6504 1.2302 0.0869  -0.0998 0.2526  24  ALA B O   
3328 C CB  . ALA B 26  ? 0.6380 1.4621 1.0989 0.0866  -0.0628 0.2295  24  ALA B CB  
3329 N N   . SER B 27  ? 0.7852 1.7271 1.2356 0.0500  -0.0985 0.2293  25  SER B N   
3330 C CA  . SER B 27  ? 0.8693 1.8619 1.3149 0.0421  -0.1215 0.2466  25  SER B CA  
3331 C C   . SER B 27  ? 0.9931 1.9705 1.4114 0.0464  -0.1303 0.2720  25  SER B C   
3332 O O   . SER B 27  ? 0.9901 1.9221 1.4063 0.0612  -0.1197 0.2799  25  SER B O   
3333 C CB  . SER B 27  ? 0.8927 1.9185 1.3173 0.0126  -0.1229 0.2234  25  SER B CB  
3334 O OG  . SER B 27  ? 0.9950 1.9901 1.3790 -0.0039 -0.1108 0.2081  25  SER B OG  
3335 N N   . GLY B 28  ? 1.2407 2.2548 1.6355 0.0319  -0.1488 0.2843  26  GLY B N   
3336 C CA  . GLY B 28  ? 1.1187 2.1170 1.4807 0.0319  -0.1560 0.3072  26  GLY B CA  
3337 C C   . GLY B 28  ? 1.1521 2.1573 1.5351 0.0565  -0.1723 0.3451  26  GLY B C   
3338 O O   . GLY B 28  ? 1.1974 2.2212 1.6040 0.0647  -0.1826 0.3510  26  GLY B O   
3339 N N   . ARG B 29  ? 1.0455 2.0099 1.4095 0.0662  -0.1676 0.3633  27  ARG B N   
3340 C CA  . ARG B 29  ? 1.0467 2.0088 1.4262 0.0897  -0.1806 0.4011  27  ARG B CA  
3341 C C   . ARG B 29  ? 0.9629 1.8646 1.3467 0.1078  -0.1609 0.4068  27  ARG B C   
3342 O O   . ARG B 29  ? 0.9568 1.8449 1.3824 0.1315  -0.1544 0.4134  27  ARG B O   
3343 C CB  . ARG B 29  ? 1.0400 2.0224 1.3789 0.0772  -0.2009 0.4252  27  ARG B CB  
3344 C CG  . ARG B 29  ? 0.9619 1.9708 1.3123 0.0830  -0.2210 0.4418  27  ARG B CG  
3345 C CD  . ARG B 29  ? 0.9645 1.9923 1.2675 0.0662  -0.2403 0.4627  27  ARG B CD  
3346 N NE  . ARG B 29  ? 0.9671 2.0014 1.2815 0.0821  -0.2585 0.4911  27  ARG B NE  
3347 C CZ  . ARG B 29  ? 0.9863 2.0313 1.2633 0.0729  -0.2766 0.5146  27  ARG B CZ  
3348 N NH1 . ARG B 29  ? 0.9428 1.9921 1.1656 0.0459  -0.2779 0.5127  27  ARG B NH1 
3349 N NH2 . ARG B 29  ? 0.9531 2.0038 1.2468 0.0905  -0.2935 0.5398  27  ARG B NH2 
3350 N N   . THR B 30  ? 0.9792 1.8449 1.3206 0.0953  -0.1498 0.4024  28  THR B N   
3351 C CA  . THR B 30  ? 0.9210 1.7297 1.2624 0.1081  -0.1295 0.4035  28  THR B CA  
3352 C C   . THR B 30  ? 0.8706 1.6575 1.2339 0.1104  -0.1092 0.3720  28  THR B C   
3353 O O   . THR B 30  ? 0.9236 1.7052 1.2667 0.0918  -0.0996 0.3437  28  THR B O   
3354 C CB  . THR B 30  ? 0.9018 1.6827 1.1926 0.0907  -0.1226 0.4031  28  THR B CB  
3355 O OG1 . THR B 30  ? 0.9206 1.7066 1.1925 0.0948  -0.1381 0.4387  28  THR B OG1 
3356 C CG2 . THR B 30  ? 0.9173 1.6427 1.2079 0.0973  -0.0979 0.3911  28  THR B CG2 
3357 N N   . PHE B 31  ? 0.7971 1.5712 1.2015 0.1329  -0.1024 0.3771  29  PHE B N   
3358 C CA  . PHE B 31  ? 0.7451 1.4969 1.1695 0.1360  -0.0836 0.3502  29  PHE B CA  
3359 C C   . PHE B 31  ? 0.7542 1.4548 1.1868 0.1509  -0.0646 0.3529  29  PHE B C   
3360 O O   . PHE B 31  ? 0.6511 1.3221 1.0770 0.1458  -0.0477 0.3289  29  PHE B O   
3361 C CB  . PHE B 31  ? 0.7439 1.5285 1.2115 0.1452  -0.0890 0.3464  29  PHE B CB  
3362 C CG  . PHE B 31  ? 0.6389 1.3991 1.1253 0.1482  -0.0694 0.3206  29  PHE B CG  
3363 C CD1 . PHE B 31  ? 0.6300 1.3903 1.0994 0.1304  -0.0625 0.2910  29  PHE B CD1 
3364 C CD2 . PHE B 31  ? 0.6006 1.3358 1.1202 0.1681  -0.0572 0.3262  29  PHE B CD2 
3365 C CE1 . PHE B 31  ? 0.6471 1.3829 1.1294 0.1329  -0.0456 0.2693  29  PHE B CE1 
3366 C CE2 . PHE B 31  ? 0.6197 1.3316 1.1517 0.1686  -0.0392 0.3026  29  PHE B CE2 
3367 C CZ  . PHE B 31  ? 0.6028 1.3148 1.1147 0.1512  -0.0344 0.2751  29  PHE B CZ  
3368 N N   . SER B 32  ? 0.7625 1.4518 1.2094 0.1689  -0.0669 0.3817  30  SER B N   
3369 C CA  . SER B 32  ? 0.7706 1.4110 1.2265 0.1821  -0.0470 0.3844  30  SER B CA  
3370 C C   . SER B 32  ? 0.8086 1.4127 1.2241 0.1686  -0.0347 0.3745  30  SER B C   
3371 O O   . SER B 32  ? 0.8599 1.4233 1.2794 0.1752  -0.0161 0.3700  30  SER B O   
3372 C CB  . SER B 32  ? 0.6784 1.3148 1.1588 0.2042  -0.0519 0.4191  30  SER B CB  
3373 O OG  . SER B 32  ? 0.5804 1.2332 1.0342 0.2000  -0.0699 0.4445  30  SER B OG  
3374 N N   . ASN B 33  ? 0.7556 1.3744 1.1338 0.1489  -0.0435 0.3695  31  ASN B N   
3375 C CA  . ASN B 33  ? 0.7962 1.3846 1.1384 0.1345  -0.0314 0.3578  31  ASN B CA  
3376 C C   . ASN B 33  ? 0.7546 1.3407 1.0871 0.1193  -0.0228 0.3224  31  ASN B C   
3377 O O   . ASN B 33  ? 0.7179 1.2810 1.0264 0.1078  -0.0120 0.3086  31  ASN B O   
3378 C CB  . ASN B 33  ? 0.8328 1.4340 1.1381 0.1212  -0.0436 0.3746  31  ASN B CB  
3379 C CG  . ASN B 33  ? 0.9457 1.5455 1.2566 0.1370  -0.0532 0.4129  31  ASN B CG  
3380 O OD1 . ASN B 33  ? 0.8830 1.5139 1.1806 0.1329  -0.0730 0.4329  31  ASN B OD1 
3381 N ND2 . ASN B 33  ? 0.9958 1.5593 1.3268 0.1551  -0.0392 0.4237  31  ASN B ND2 
3382 N N   . TYR B 34  ? 0.6729 1.2815 1.0247 0.1194  -0.0267 0.3074  32  TYR B N   
3383 C CA  . TYR B 34  ? 0.6158 1.2209 0.9598 0.1068  -0.0191 0.2760  32  TYR B CA  
3384 C C   . TYR B 34  ? 0.6028 1.1772 0.9668 0.1180  -0.0038 0.2628  32  TYR B C   
3385 O O   . TYR B 34  ? 0.6002 1.1754 0.9934 0.1325  -0.0026 0.2701  32  TYR B O   
3386 C CB  . TYR B 34  ? 0.5448 1.1893 0.8941 0.0979  -0.0302 0.2661  32  TYR B CB  
3387 C CG  . TYR B 34  ? 0.6581 1.3298 0.9780 0.0780  -0.0409 0.2655  32  TYR B CG  
3388 C CD1 . TYR B 34  ? 0.5757 1.2440 0.8736 0.0596  -0.0342 0.2404  32  TYR B CD1 
3389 C CD2 . TYR B 34  ? 0.7008 1.4019 1.0152 0.0772  -0.0575 0.2900  32  TYR B CD2 
3390 C CE1 . TYR B 34  ? 0.5851 1.2772 0.8559 0.0392  -0.0413 0.2377  32  TYR B CE1 
3391 C CE2 . TYR B 34  ? 0.6474 1.3736 0.9310 0.0561  -0.0668 0.2887  32  TYR B CE2 
3392 C CZ  . TYR B 34  ? 0.6282 1.3493 0.8900 0.0363  -0.0574 0.2614  32  TYR B CZ  
3393 O OH  . TYR B 34  ? 0.6654 1.4105 0.8964 0.0134  -0.0641 0.2581  32  TYR B OH  
3394 N N   . VAL B 35  ? 0.6254 1.1739 0.9742 0.1106  0.0078  0.2429  33  VAL B N   
3395 C CA  . VAL B 35  ? 0.5835 1.1071 0.9460 0.1174  0.0201  0.2269  33  VAL B CA  
3396 C C   . VAL B 35  ? 0.5078 1.0483 0.8782 0.1136  0.0167  0.2103  33  VAL B C   
3397 O O   . VAL B 35  ? 0.4845 1.0450 0.8411 0.1006  0.0102  0.1997  33  VAL B O   
3398 C CB  . VAL B 35  ? 0.6151 1.1098 0.9601 0.1108  0.0312  0.2113  33  VAL B CB  
3399 C CG1 . VAL B 35  ? 0.5378 1.0418 0.8664 0.0964  0.0288  0.1894  33  VAL B CG1 
3400 C CG2 . VAL B 35  ? 0.6341 1.0996 0.9925 0.1198  0.0438  0.2025  33  VAL B CG2 
3401 N N   . MET B 36  ? 0.4684 1.0002 0.8607 0.1240  0.0226  0.2078  34  MET B N   
3402 C CA  . MET B 36  ? 0.4482 0.9929 0.8491 0.1210  0.0215  0.1937  34  MET B CA  
3403 C C   . MET B 36  ? 0.4317 0.9454 0.8269 0.1205  0.0331  0.1739  34  MET B C   
3404 O O   . MET B 36  ? 0.4386 0.9241 0.8357 0.1270  0.0427  0.1743  34  MET B O   
3405 C CB  . MET B 36  ? 0.4633 1.0256 0.8949 0.1317  0.0193  0.2058  34  MET B CB  
3406 C CG  . MET B 36  ? 0.5133 1.1146 0.9531 0.1321  0.0038  0.2251  34  MET B CG  
3407 S SD  . MET B 36  ? 0.5548 1.1847 0.9640 0.1120  -0.0088 0.2187  34  MET B SD  
3408 C CE  . MET B 36  ? 0.3820 1.0302 0.7982 0.1024  -0.0075 0.1957  34  MET B CE  
3409 N N   . ALA B 37  ? 0.3490 0.8675 0.7361 0.1121  0.0323  0.1567  35  ALA B N   
3410 C CA  . ALA B 37  ? 0.4141 0.9034 0.7915 0.1113  0.0407  0.1394  35  ALA B CA  
3411 C C   . ALA B 37  ? 0.4113 0.9055 0.7886 0.1062  0.0416  0.1261  35  ALA B C   
3412 O O   . ALA B 37  ? 0.3190 0.8409 0.6988 0.0993  0.0357  0.1254  35  ALA B O   
3413 C CB  . ALA B 37  ? 0.3825 0.8601 0.7394 0.1048  0.0401  0.1297  35  ALA B CB  
3414 N N   . TRP B 38  ? 0.3534 0.8196 0.7256 0.1083  0.0498  0.1153  36  TRP B N   
3415 C CA  . TRP B 38  ? 0.3948 0.8553 0.7603 0.1028  0.0530  0.1014  36  TRP B CA  
3416 C C   . TRP B 38  ? 0.3702 0.8081 0.7139 0.0995  0.0530  0.0885  36  TRP B C   
3417 O O   . TRP B 38  ? 0.3970 0.8138 0.7337 0.1038  0.0545  0.0879  36  TRP B O   
3418 C CB  . TRP B 38  ? 0.4062 0.8503 0.7813 0.1073  0.0629  0.0999  36  TRP B CB  
3419 C CG  . TRP B 38  ? 0.4215 0.8914 0.8227 0.1097  0.0636  0.1080  36  TRP B CG  
3420 C CD1 . TRP B 38  ? 0.4937 0.9675 0.9183 0.1191  0.0668  0.1207  36  TRP B CD1 
3421 C CD2 . TRP B 38  ? 0.4265 0.9229 0.8363 0.1026  0.0615  0.1032  36  TRP B CD2 
3422 N NE1 . TRP B 38  ? 0.4625 0.9658 0.9121 0.1198  0.0653  0.1249  36  TRP B NE1 
3423 C CE2 . TRP B 38  ? 0.4626 0.9816 0.9030 0.1088  0.0618  0.1136  36  TRP B CE2 
3424 C CE3 . TRP B 38  ? 0.4083 0.9117 0.8044 0.0913  0.0603  0.0903  36  TRP B CE3 
3425 C CZ2 . TRP B 38  ? 0.3733 0.9254 0.8314 0.1036  0.0594  0.1110  36  TRP B CZ2 
3426 C CZ3 . TRP B 38  ? 0.4762 1.0095 0.8873 0.0846  0.0599  0.0869  36  TRP B CZ3 
3427 C CH2 . TRP B 38  ? 0.4053 0.9645 0.8473 0.0905  0.0586  0.0970  36  TRP B CH2 
3428 N N   . PHE B 39  ? 0.3894 0.8330 0.7243 0.0918  0.0515  0.0779  37  PHE B N   
3429 C CA  . PHE B 39  ? 0.3259 0.7473 0.6438 0.0902  0.0519  0.0656  37  PHE B CA  
3430 C C   . PHE B 39  ? 0.4019 0.8102 0.7125 0.0866  0.0579  0.0564  37  PHE B C   
3431 O O   . PHE B 39  ? 0.4184 0.8422 0.7379 0.0820  0.0613  0.0567  37  PHE B O   
3432 C CB  . PHE B 39  ? 0.3697 0.8063 0.6837 0.0839  0.0469  0.0604  37  PHE B CB  
3433 C CG  . PHE B 39  ? 0.4247 0.8692 0.7415 0.0858  0.0428  0.0675  37  PHE B CG  
3434 C CD1 . PHE B 39  ? 0.3834 0.8509 0.7090 0.0847  0.0400  0.0806  37  PHE B CD1 
3435 C CD2 . PHE B 39  ? 0.3913 0.8201 0.7021 0.0885  0.0419  0.0614  37  PHE B CD2 
3436 C CE1 . PHE B 39  ? 0.3742 0.8446 0.6991 0.0855  0.0380  0.0876  37  PHE B CE1 
3437 C CE2 . PHE B 39  ? 0.4027 0.8375 0.7157 0.0885  0.0404  0.0662  37  PHE B CE2 
3438 C CZ  . PHE B 39  ? 0.4078 0.8613 0.7262 0.0865  0.0393  0.0794  37  PHE B CZ  
3439 N N   . ARG B 40  ? 0.4222 0.8017 0.7168 0.0885  0.0590  0.0484  38  ARG B N   
3440 C CA  . ARG B 40  ? 0.4322 0.7931 0.7152 0.0847  0.0655  0.0401  38  ARG B CA  
3441 C C   . ARG B 40  ? 0.5240 0.8685 0.7942 0.0851  0.0631  0.0316  38  ARG B C   
3442 O O   . ARG B 40  ? 0.5624 0.9034 0.8318 0.0905  0.0563  0.0318  38  ARG B O   
3443 C CB  . ARG B 40  ? 0.4732 0.8060 0.7469 0.0882  0.0719  0.0418  38  ARG B CB  
3444 C CG  . ARG B 40  ? 0.5368 0.8381 0.7921 0.0944  0.0683  0.0412  38  ARG B CG  
3445 C CD  . ARG B 40  ? 0.5635 0.8397 0.8080 0.0948  0.0758  0.0428  38  ARG B CD  
3446 N NE  . ARG B 40  ? 0.6194 0.8727 0.8480 0.0997  0.0708  0.0437  38  ARG B NE  
3447 C CZ  . ARG B 40  ? 0.7093 0.9390 0.9243 0.0987  0.0766  0.0442  38  ARG B CZ  
3448 N NH1 . ARG B 40  ? 0.7026 0.9266 0.9197 0.0936  0.0890  0.0435  38  ARG B NH1 
3449 N NH2 . ARG B 40  ? 0.7579 0.9707 0.9574 0.1016  0.0702  0.0442  38  ARG B NH2 
3450 N N   . GLN B 41  ? 0.4578 0.7929 0.7203 0.0791  0.0696  0.0235  39  GLN B N   
3451 C CA  . GLN B 41  ? 0.5864 0.9042 0.8397 0.0800  0.0694  0.0155  39  GLN B CA  
3452 C C   . GLN B 41  ? 0.6085 0.8931 0.8438 0.0786  0.0780  0.0116  39  GLN B C   
3453 O O   . GLN B 41  ? 0.6048 0.8946 0.8405 0.0690  0.0878  0.0063  39  GLN B O   
3454 C CB  . GLN B 41  ? 0.5825 0.9267 0.8467 0.0709  0.0713  0.0076  39  GLN B CB  
3455 C CG  . GLN B 41  ? 0.6328 0.9578 0.8913 0.0709  0.0751  -0.0026 39  GLN B CG  
3456 C CD  . GLN B 41  ? 0.6296 0.9781 0.9008 0.0654  0.0743  -0.0101 39  GLN B CD  
3457 O OE1 . GLN B 41  ? 0.7145 1.0950 0.9934 0.0543  0.0757  -0.0117 39  GLN B OE1 
3458 N NE2 . GLN B 41  ? 0.6712 1.0047 0.9448 0.0727  0.0720  -0.0151 39  GLN B NE2 
3459 N N   . ALA B 42  ? 0.7100 0.9612 0.9285 0.0874  0.0741  0.0141  40  ALA B N   
3460 C CA  . ALA B 42  ? 0.8725 1.0860 1.0681 0.0866  0.0816  0.0126  40  ALA B CA  
3461 C C   . ALA B 42  ? 0.9723 1.1713 1.1644 0.0867  0.0850  0.0056  40  ALA B C   
3462 O O   . ALA B 42  ? 0.9201 1.1322 1.1258 0.0908  0.0789  0.0026  40  ALA B O   
3463 C CB  . ALA B 42  ? 0.8997 1.0834 1.0754 0.0954  0.0745  0.0201  40  ALA B CB  
3464 N N   . PRO B 43  ? 1.2883 1.4587 1.4631 0.0814  0.0969  0.0019  41  PRO B N   
3465 C CA  . PRO B 43  ? 1.3319 1.4834 1.5036 0.0818  0.1028  -0.0047 41  PRO B CA  
3466 C C   . PRO B 43  ? 1.3600 1.4875 1.5258 0.0975  0.0907  0.0012  41  PRO B C   
3467 O O   . PRO B 43  ? 1.4112 1.5049 1.5533 0.1050  0.0858  0.0098  41  PRO B O   
3468 C CB  . PRO B 43  ? 1.3841 1.5039 1.5337 0.0728  0.1189  -0.0080 41  PRO B CB  
3469 C CG  . PRO B 43  ? 1.3884 1.4999 1.5239 0.0722  0.1176  -0.0007 41  PRO B CG  
3470 C CD  . PRO B 43  ? 1.3146 1.4688 1.4738 0.0734  0.1080  0.0021  41  PRO B CD  
3471 N N   . GLY B 44  ? 0.9956 1.1418 1.1831 0.1021  0.0856  -0.0036 42  GLY B N   
3472 C CA  . GLY B 44  ? 0.8611 0.9926 1.0517 0.1177  0.0732  0.0004  42  GLY B CA  
3473 C C   . GLY B 44  ? 0.8064 0.9677 1.0153 0.1243  0.0583  0.0024  42  GLY B C   
3474 O O   . GLY B 44  ? 0.8199 0.9779 1.0393 0.1364  0.0480  0.0029  42  GLY B O   
3475 N N   . LYS B 45  ? 0.8528 1.0428 1.0675 0.1169  0.0573  0.0035  43  LYS B N   
3476 C CA  . LYS B 45  ? 0.7284 0.9449 0.9587 0.1211  0.0459  0.0051  43  LYS B CA  
3477 C C   . LYS B 45  ? 0.7077 0.9624 0.9575 0.1101  0.0514  -0.0011 43  LYS B C   
3478 O O   . LYS B 45  ? 0.7523 1.0153 1.0043 0.0993  0.0625  -0.0073 43  LYS B O   
3479 C CB  . LYS B 45  ? 0.7857 0.9956 1.0014 0.1237  0.0390  0.0147  43  LYS B CB  
3480 C CG  . LYS B 45  ? 0.8282 0.9985 1.0145 0.1271  0.0392  0.0211  43  LYS B CG  
3481 C CD  . LYS B 45  ? 0.8717 1.0380 1.0435 0.1230  0.0400  0.0272  43  LYS B CD  
3482 C CE  . LYS B 45  ? 0.9159 1.1005 1.0975 0.1273  0.0290  0.0296  43  LYS B CE  
3483 N NZ  . LYS B 45  ? 0.8134 0.9812 0.9842 0.1375  0.0148  0.0326  43  LYS B NZ  
3484 N N   . GLU B 46  ? 0.7497 1.0275 1.0120 0.1117  0.0436  0.0004  44  GLU B N   
3485 C CA  . GLU B 46  ? 0.6385 0.9508 0.9158 0.1017  0.0470  -0.0033 44  GLU B CA  
3486 C C   . GLU B 46  ? 0.6338 0.9596 0.9076 0.0977  0.0466  0.0061  44  GLU B C   
3487 O O   . GLU B 46  ? 0.5783 0.8871 0.8403 0.1020  0.0452  0.0134  44  GLU B O   
3488 C CB  . GLU B 46  ? 0.7768 1.1043 1.0712 0.1051  0.0412  -0.0089 44  GLU B CB  
3489 C CG  . GLU B 46  ? 0.8001 1.1180 1.0939 0.1168  0.0296  -0.0042 44  GLU B CG  
3490 C CD  . GLU B 46  ? 0.9771 1.3084 1.2913 0.1205  0.0249  -0.0131 44  GLU B CD  
3491 O OE1 . GLU B 46  ? 0.8573 1.2102 1.1848 0.1116  0.0313  -0.0212 44  GLU B OE1 
3492 O OE2 . GLU B 46  ? 1.0146 1.3360 1.3313 0.1315  0.0148  -0.0127 44  GLU B OE2 
3493 N N   . ARG B 47  ? 0.6266 0.9824 0.9107 0.0889  0.0484  0.0060  45  ARG B N   
3494 C CA  . ARG B 47  ? 0.5963 0.9669 0.8814 0.0865  0.0478  0.0164  45  ARG B CA  
3495 C C   . ARG B 47  ? 0.6498 1.0128 0.9349 0.0951  0.0416  0.0230  45  ARG B C   
3496 O O   . ARG B 47  ? 0.6736 1.0426 0.9653 0.0971  0.0374  0.0197  45  ARG B O   
3497 C CB  . ARG B 47  ? 0.4907 0.8947 0.7847 0.0759  0.0490  0.0165  45  ARG B CB  
3498 C CG  . ARG B 47  ? 0.4925 0.9126 0.7864 0.0661  0.0540  0.0169  45  ARG B CG  
3499 C CD  . ARG B 47  ? 0.5289 0.9825 0.8279 0.0541  0.0535  0.0159  45  ARG B CD  
3500 N NE  . ARG B 47  ? 0.5591 1.0340 0.8590 0.0434  0.0564  0.0158  45  ARG B NE  
3501 C CZ  . ARG B 47  ? 0.6080 1.1115 0.9081 0.0291  0.0571  0.0113  45  ARG B CZ  
3502 N NH1 . ARG B 47  ? 0.4703 0.9821 0.7687 0.0230  0.0570  0.0060  45  ARG B NH1 
3503 N NH2 . ARG B 47  ? 0.5973 1.1230 0.8994 0.0194  0.0584  0.0112  45  ARG B NH2 
3504 N N   . GLU B 48  ? 0.5316 0.8813 0.8098 0.0987  0.0427  0.0306  46  GLU B N   
3505 C CA  . GLU B 48  ? 0.4961 0.8374 0.7731 0.1045  0.0395  0.0358  46  GLU B CA  
3506 C C   . GLU B 48  ? 0.4929 0.8469 0.7776 0.1028  0.0437  0.0458  46  GLU B C   
3507 O O   . GLU B 48  ? 0.4519 0.8140 0.7401 0.0994  0.0482  0.0494  46  GLU B O   
3508 C CB  . GLU B 48  ? 0.5827 0.8929 0.8432 0.1101  0.0382  0.0352  46  GLU B CB  
3509 C CG  . GLU B 48  ? 0.6851 0.9820 0.9373 0.1082  0.0458  0.0404  46  GLU B CG  
3510 C CD  . GLU B 48  ? 0.8099 1.0736 1.0397 0.1109  0.0453  0.0392  46  GLU B CD  
3511 O OE1 . GLU B 48  ? 0.8606 1.1080 1.0780 0.1109  0.0455  0.0359  46  GLU B OE1 
3512 O OE2 . GLU B 48  ? 0.8730 1.1255 1.0959 0.1120  0.0454  0.0417  46  GLU B OE2 
3513 N N   . PHE B 49  ? 0.4833 0.8394 0.7727 0.1053  0.0425  0.0499  47  PHE B N   
3514 C CA  . PHE B 49  ? 0.4471 0.8115 0.7456 0.1057  0.0471  0.0607  47  PHE B CA  
3515 C C   . PHE B 49  ? 0.4278 0.7734 0.7228 0.1083  0.0536  0.0637  47  PHE B C   
3516 O O   . PHE B 49  ? 0.5284 0.8504 0.8096 0.1098  0.0540  0.0583  47  PHE B O   
3517 C CB  . PHE B 49  ? 0.3810 0.7469 0.6836 0.1069  0.0468  0.0629  47  PHE B CB  
3518 C CG  . PHE B 49  ? 0.3663 0.7327 0.6778 0.1091  0.0532  0.0746  47  PHE B CG  
3519 C CD1 . PHE B 49  ? 0.3876 0.7747 0.7094 0.1079  0.0531  0.0854  47  PHE B CD1 
3520 C CD2 . PHE B 49  ? 0.4192 0.7647 0.7286 0.1121  0.0597  0.0751  47  PHE B CD2 
3521 C CE1 . PHE B 49  ? 0.4090 0.7950 0.7413 0.1120  0.0589  0.0980  47  PHE B CE1 
3522 C CE2 . PHE B 49  ? 0.5113 0.8552 0.8320 0.1148  0.0679  0.0854  47  PHE B CE2 
3523 C CZ  . PHE B 49  ? 0.4525 0.8162 0.7861 0.1159  0.0672  0.0976  47  PHE B CZ  
3524 N N   . VAL B 50  ? 0.4411 0.7980 0.7491 0.1086  0.0588  0.0724  48  VAL B N   
3525 C CA  . VAL B 50  ? 0.3890 0.7308 0.6988 0.1102  0.0678  0.0743  48  VAL B CA  
3526 C C   . VAL B 50  ? 0.4552 0.7994 0.7810 0.1144  0.0738  0.0843  48  VAL B C   
3527 O O   . VAL B 50  ? 0.4108 0.7335 0.7322 0.1156  0.0809  0.0826  48  VAL B O   
3528 C CB  . VAL B 50  ? 0.4049 0.7574 0.7208 0.1069  0.0708  0.0736  48  VAL B CB  
3529 C CG1 . VAL B 50  ? 0.4036 0.7414 0.7246 0.1076  0.0823  0.0740  48  VAL B CG1 
3530 C CG2 . VAL B 50  ? 0.4982 0.8428 0.7973 0.1023  0.0677  0.0633  48  VAL B CG2 
3531 N N   . ALA B 51  ? 0.4295 0.7989 0.7730 0.1164  0.0715  0.0950  49  ALA B N   
3532 C CA  . ALA B 51  ? 0.3634 0.7344 0.7244 0.1222  0.0774  0.1071  49  ALA B CA  
3533 C C   . ALA B 51  ? 0.4329 0.8304 0.8031 0.1232  0.0695  0.1193  49  ALA B C   
3534 O O   . ALA B 51  ? 0.4319 0.8511 0.7986 0.1184  0.0608  0.1182  49  ALA B O   
3535 C CB  . ALA B 51  ? 0.3793 0.7488 0.7585 0.1258  0.0868  0.1107  49  ALA B CB  
3536 N N   . ARG B 52  ? 0.4007 0.7945 0.7805 0.1285  0.0737  0.1308  50  ARG B N   
3537 C CA  . ARG B 52  ? 0.4633 0.8776 0.8479 0.1294  0.0669  0.1450  50  ARG B CA  
3538 C C   . ARG B 52  ? 0.4693 0.8782 0.8734 0.1389  0.0741  0.1617  50  ARG B C   
3539 O O   . ARG B 52  ? 0.4485 0.8314 0.8550 0.1419  0.0863  0.1593  50  ARG B O   
3540 C CB  . ARG B 52  ? 0.4623 0.8727 0.8283 0.1229  0.0636  0.1395  50  ARG B CB  
3541 C CG  . ARG B 52  ? 0.4975 0.9168 0.8648 0.1235  0.0618  0.1552  50  ARG B CG  
3542 C CD  . ARG B 52  ? 0.4886 0.9046 0.8379 0.1148  0.0608  0.1467  50  ARG B CD  
3543 N NE  . ARG B 52  ? 0.4795 0.8727 0.8278 0.1164  0.0712  0.1485  50  ARG B NE  
3544 C CZ  . ARG B 52  ? 0.4936 0.8674 0.8366 0.1141  0.0776  0.1333  50  ARG B CZ  
3545 N NH1 . ARG B 52  ? 0.4264 0.7993 0.7635 0.1116  0.0733  0.1171  50  ARG B NH1 
3546 N NH2 . ARG B 52  ? 0.5300 0.8847 0.8730 0.1140  0.0886  0.1346  50  ARG B NH2 
3547 N N   . ILE B 53  ? 0.4039 0.8374 0.8221 0.1434  0.0668  0.1786  51  ILE B N   
3548 C CA  . ILE B 53  ? 0.5035 0.9339 0.9415 0.1544  0.0714  0.1984  51  ILE B CA  
3549 C C   . ILE B 53  ? 0.6026 1.0457 1.0294 0.1525  0.0621  0.2136  51  ILE B C   
3550 O O   . ILE B 53  ? 0.5660 1.0341 0.9801 0.1445  0.0493  0.2129  51  ILE B O   
3551 C CB  . ILE B 53  ? 0.5060 0.9546 0.9755 0.1638  0.0707  0.2078  51  ILE B CB  
3552 C CG1 . ILE B 53  ? 0.5302 0.9611 1.0253 0.1770  0.0833  0.2217  51  ILE B CG1 
3553 C CG2 . ILE B 53  ? 0.5679 1.0570 1.0426 0.1632  0.0532  0.2200  51  ILE B CG2 
3554 C CD1 . ILE B 53  ? 0.5417 0.9937 1.0741 0.1881  0.0823  0.2323  51  ILE B CD1 
3555 N N   . SER B 54  ? 0.6295 1.0527 1.0583 0.1581  0.0703  0.2260  52  SER B N   
3556 C CA  . SER B 54  ? 0.7042 1.1320 1.1166 0.1545  0.0643  0.2396  52  SER B CA  
3557 C C   . SER B 54  ? 0.6738 1.1278 1.1000 0.1628  0.0519  0.2651  52  SER B C   
3558 O O   . SER B 54  ? 0.6134 1.0838 1.0662 0.1723  0.0483  0.2715  52  SER B O   
3559 C CB  . SER B 54  ? 0.7474 1.1408 1.1540 0.1557  0.0796  0.2422  52  SER B CB  
3560 O OG  . SER B 54  ? 0.9294 1.3143 1.3558 0.1693  0.0846  0.2658  52  SER B OG  
3561 N N   . GLU B 55  ? 0.6937 1.1525 1.1011 0.1586  0.0451  0.2798  53  GLU B N   
3562 C CA  . GLU B 55  ? 0.7588 1.2426 1.1736 0.1656  0.0308  0.3068  53  GLU B CA  
3563 C C   . GLU B 55  ? 0.7848 1.2458 1.2117 0.1801  0.0382  0.3322  53  GLU B C   
3564 O O   . GLU B 55  ? 0.9489 1.4287 1.3868 0.1899  0.0258  0.3583  53  GLU B O   
3565 C CB  . GLU B 55  ? 0.7644 1.2694 1.1466 0.1500  0.0173  0.3089  53  GLU B CB  
3566 C CG  . GLU B 55  ? 0.7478 1.2286 1.1028 0.1440  0.0237  0.3182  53  GLU B CG  
3567 C CD  . GLU B 55  ? 0.7851 1.2377 1.1247 0.1333  0.0395  0.2929  53  GLU B CD  
3568 O OE1 . GLU B 55  ? 0.8434 1.2979 1.1892 0.1299  0.0423  0.2691  53  GLU B OE1 
3569 O OE2 . GLU B 55  ? 0.7837 1.2126 1.1047 0.1281  0.0488  0.2968  53  GLU B OE2 
3570 N N   . SER B 56  ? 0.7878 1.2090 1.2136 0.1818  0.0581  0.3254  54  SER B N   
3571 C CA  . SER B 56  ? 0.9393 1.3327 1.3719 0.1931  0.0685  0.3480  54  SER B CA  
3572 C C   . SER B 56  ? 0.9897 1.3607 1.4570 0.2068  0.0859  0.3448  54  SER B C   
3573 O O   . SER B 56  ? 1.0218 1.4086 1.5231 0.2219  0.0811  0.3582  54  SER B O   
3574 C CB  . SER B 56  ? 0.9934 1.3582 1.3921 0.1802  0.0793  0.3432  54  SER B CB  
3575 O OG  . SER B 56  ? 1.0535 1.3968 1.4474 0.1712  0.0951  0.3145  54  SER B OG  
3576 N N   . ARG B 57  ? 0.9984 1.3346 1.4603 0.2013  0.1068  0.3264  55  ARG B N   
3577 C CA  . ARG B 57  ? 1.0835 1.3933 1.5743 0.2113  0.1271  0.3227  55  ARG B CA  
3578 C C   . ARG B 57  ? 1.1043 1.4292 1.6167 0.2130  0.1267  0.3055  55  ARG B C   
3579 O O   . ARG B 57  ? 1.1511 1.4541 1.6859 0.2185  0.1452  0.2986  55  ARG B O   
3580 C CB  . ARG B 57  ? 1.1006 1.3715 1.5736 0.2008  0.1488  0.3057  55  ARG B CB  
3581 C CG  . ARG B 57  ? 1.1596 1.4210 1.5991 0.1902  0.1474  0.3111  55  ARG B CG  
3582 C CD  . ARG B 57  ? 1.2464 1.4834 1.6652 0.1741  0.1633  0.2846  55  ARG B CD  
3583 N NE  . ARG B 57  ? 1.2674 1.5111 1.6536 0.1595  0.1559  0.2799  55  ARG B NE  
3584 C CZ  . ARG B 57  ? 1.2532 1.4810 1.6208 0.1448  0.1672  0.2589  55  ARG B CZ  
3585 N NH1 . ARG B 57  ? 1.2919 1.4966 1.6669 0.1415  0.1853  0.2408  55  ARG B NH1 
3586 N NH2 . ARG B 57  ? 1.1619 1.3987 1.5033 0.1318  0.1606  0.2549  55  ARG B NH2 
3587 N N   . GLY B 58  ? 1.2475 1.6068 1.7529 0.2069  0.1083  0.2977  56  GLY B N   
3588 C CA  . GLY B 58  ? 1.1546 1.5249 1.6758 0.2061  0.1095  0.2800  56  GLY B CA  
3589 C C   . GLY B 58  ? 1.1415 1.4882 1.6448 0.1938  0.1223  0.2517  56  GLY B C   
3590 O O   . GLY B 58  ? 1.0470 1.3894 1.5638 0.1940  0.1304  0.2382  56  GLY B O   
3591 N N   . THR B 59  ? 0.9224 1.2544 1.3956 0.1825  0.1242  0.2424  57  THR B N   
3592 C CA  . THR B 59  ? 0.8416 1.1541 1.2978 0.1711  0.1337  0.2167  57  THR B CA  
3593 C C   . THR B 59  ? 0.6985 1.0308 1.1454 0.1644  0.1215  0.2007  57  THR B C   
3594 O O   . THR B 59  ? 0.6816 1.0429 1.1261 0.1638  0.1052  0.2061  57  THR B O   
3595 C CB  . THR B 59  ? 0.8140 1.1124 1.2437 0.1607  0.1364  0.2100  57  THR B CB  
3596 O OG1 . THR B 59  ? 0.8707 1.1898 1.2878 0.1587  0.1216  0.2227  57  THR B OG1 
3597 C CG2 . THR B 59  ? 0.9407 1.2064 1.3771 0.1633  0.1571  0.2153  57  THR B CG2 
3598 N N   . THR B 60  ? 0.6452 0.9603 1.0852 0.1583  0.1303  0.1809  58  THR B N   
3599 C CA  . THR B 60  ? 0.5710 0.8976 1.0007 0.1523  0.1215  0.1660  58  THR B CA  
3600 C C   . THR B 60  ? 0.6509 0.9630 1.0535 0.1414  0.1214  0.1466  58  THR B C   
3601 O O   . THR B 60  ? 0.6622 0.9526 1.0583 0.1379  0.1323  0.1408  58  THR B O   
3602 C CB  . THR B 60  ? 0.6201 0.9411 1.0679 0.1560  0.1309  0.1616  58  THR B CB  
3603 O OG1 . THR B 60  ? 0.7466 1.0397 1.2059 0.1585  0.1508  0.1609  58  THR B OG1 
3604 C CG2 . THR B 60  ? 0.5198 0.8689 0.9943 0.1652  0.1236  0.1765  58  THR B CG2 
3605 N N   . ASP B 61  ? 0.5604 0.8858 0.9486 0.1361  0.1089  0.1366  59  ASP B N   
3606 C CA  . ASP B 61  ? 0.5124 0.8276 0.8779 0.1278  0.1058  0.1191  59  ASP B CA  
3607 C C   . ASP B 61  ? 0.5401 0.8570 0.8980 0.1258  0.1005  0.1095  59  ASP B C   
3608 O O   . ASP B 61  ? 0.4686 0.8041 0.8339 0.1277  0.0940  0.1145  59  ASP B O   
3609 C CB  . ASP B 61  ? 0.5701 0.8989 0.9242 0.1232  0.0954  0.1173  59  ASP B CB  
3610 C CG  . ASP B 61  ? 0.6207 0.9381 0.9585 0.1165  0.0944  0.1004  59  ASP B CG  
3611 O OD1 . ASP B 61  ? 0.6757 0.9727 1.0102 0.1146  0.1038  0.0932  59  ASP B OD1 
3612 O OD2 . ASP B 61  ? 0.6192 0.9495 0.9488 0.1126  0.0843  0.0936  59  ASP B OD2 
3613 N N   . TYR B 62  ? 0.5470 0.8440 0.8886 0.1209  0.1034  0.0958  60  TYR B N   
3614 C CA  . TYR B 62  ? 0.4974 0.7886 0.8271 0.1183  0.1004  0.0873  60  TYR B CA  
3615 C C   . TYR B 62  ? 0.5599 0.8414 0.8662 0.1134  0.0921  0.0747  60  TYR B C   
3616 O O   . TYR B 62  ? 0.5111 0.7820 0.8102 0.1104  0.0945  0.0691  60  TYR B O   
3617 C CB  . TYR B 62  ? 0.5243 0.7960 0.8579 0.1175  0.1150  0.0852  60  TYR B CB  
3618 C CG  . TYR B 62  ? 0.5004 0.7816 0.8630 0.1241  0.1240  0.0970  60  TYR B CG  
3619 C CD1 . TYR B 62  ? 0.3953 0.6934 0.7708 0.1265  0.1214  0.1007  60  TYR B CD1 
3620 C CD2 . TYR B 62  ? 0.5804 0.8544 0.9596 0.1281  0.1354  0.1044  60  TYR B CD2 
3621 C CE1 . TYR B 62  ? 0.5434 0.8543 0.9498 0.1337  0.1278  0.1119  60  TYR B CE1 
3622 C CE2 . TYR B 62  ? 0.4992 0.7822 0.9087 0.1364  0.1428  0.1170  60  TYR B CE2 
3623 C CZ  . TYR B 62  ? 0.5711 0.8744 0.9953 0.1397  0.1379  0.1209  60  TYR B CZ  
3624 O OH  . TYR B 62  ? 0.5717 0.8879 1.0302 0.1492  0.1435  0.1336  60  TYR B OH  
3625 N N   . ALA B 63  ? 0.5773 0.8630 0.8728 0.1127  0.0827  0.0703  61  ALA B N   
3626 C CA  . ALA B 63  ? 0.5168 0.7900 0.7910 0.1101  0.0747  0.0599  61  ALA B CA  
3627 C C   . ALA B 63  ? 0.6249 0.8715 0.8830 0.1060  0.0824  0.0546  61  ALA B C   
3628 O O   . ALA B 63  ? 0.6968 0.9334 0.9580 0.1046  0.0941  0.0567  61  ALA B O   
3629 C CB  . ALA B 63  ? 0.4428 0.7207 0.7095 0.1108  0.0659  0.0574  61  ALA B CB  
3630 N N   . ASP B 64  ? 0.6376 0.8745 0.8790 0.1031  0.0761  0.0467  62  ASP B N   
3631 C CA  . ASP B 64  ? 0.6806 0.8932 0.9022 0.0966  0.0826  0.0407  62  ASP B CA  
3632 C C   . ASP B 64  ? 0.7603 0.9542 0.9631 0.0941  0.0849  0.0402  62  ASP B C   
3633 O O   . ASP B 64  ? 0.8790 1.0516 1.0669 0.0869  0.0954  0.0362  62  ASP B O   
3634 C CB  . ASP B 64  ? 0.7097 0.9206 0.9161 0.0939  0.0712  0.0325  62  ASP B CB  
3635 C CG  . ASP B 64  ? 0.7516 0.9736 0.9726 0.0918  0.0752  0.0295  62  ASP B CG  
3636 O OD1 . ASP B 64  ? 0.6869 0.9120 0.9000 0.0886  0.0668  0.0212  62  ASP B OD1 
3637 O OD2 . ASP B 64  ? 0.8389 1.0667 1.0798 0.0934  0.0868  0.0357  62  ASP B OD2 
3638 N N   . SER B 65  ? 0.7269 0.9269 0.9290 0.0983  0.0773  0.0429  63  SER B N   
3639 C CA  . SER B 65  ? 0.8522 1.0322 1.0350 0.0949  0.0811  0.0418  63  SER B CA  
3640 C C   . SER B 65  ? 0.7304 0.9100 0.9281 0.0923  0.0977  0.0440  63  SER B C   
3641 O O   . SER B 65  ? 0.7810 0.9396 0.9619 0.0862  0.1065  0.0408  63  SER B O   
3642 C CB  . SER B 65  ? 0.8572 1.0414 1.0344 0.0994  0.0694  0.0427  63  SER B CB  
3643 O OG  . SER B 65  ? 0.7930 1.0052 0.9966 0.1040  0.0670  0.0460  63  SER B OG  
3644 N N   . VAL B 66  ? 0.6544 0.8568 0.8832 0.0967  0.1023  0.0496  64  VAL B N   
3645 C CA  . VAL B 66  ? 0.6730 0.8812 0.9233 0.0966  0.1160  0.0528  64  VAL B CA  
3646 C C   . VAL B 66  ? 0.7024 0.9095 0.9722 0.0973  0.1291  0.0553  64  VAL B C   
3647 O O   . VAL B 66  ? 0.7526 0.9652 1.0456 0.0988  0.1412  0.0584  64  VAL B O   
3648 C CB  . VAL B 66  ? 0.6795 0.9176 0.9522 0.1018  0.1097  0.0591  64  VAL B CB  
3649 C CG1 . VAL B 66  ? 0.6763 0.9149 0.9312 0.1008  0.0980  0.0554  64  VAL B CG1 
3650 C CG2 . VAL B 66  ? 0.5557 0.8174 0.8504 0.1081  0.1045  0.0675  64  VAL B CG2 
3651 N N   . LYS B 67  ? 0.7922 0.9925 1.0552 0.0962  0.1280  0.0534  65  LYS B N   
3652 C CA  . LYS B 67  ? 0.8252 1.0204 1.1061 0.0961  0.1431  0.0551  65  LYS B CA  
3653 C C   . LYS B 67  ? 0.8115 0.9821 1.0862 0.0881  0.1618  0.0476  65  LYS B C   
3654 O O   . LYS B 67  ? 0.8508 1.0005 1.0940 0.0789  0.1618  0.0386  65  LYS B O   
3655 C CB  . LYS B 67  ? 0.8575 1.0493 1.1293 0.0938  0.1394  0.0517  65  LYS B CB  
3656 C CG  . LYS B 67  ? 0.9894 1.1631 1.2265 0.0848  0.1335  0.0405  65  LYS B CG  
3657 C CD  . LYS B 67  ? 1.0493 1.2200 1.2822 0.0800  0.1348  0.0346  65  LYS B CD  
3658 C CE  . LYS B 67  ? 1.0749 1.2250 1.2746 0.0684  0.1342  0.0229  65  LYS B CE  
3659 N NZ  . LYS B 67  ? 1.2371 1.3885 1.4325 0.0620  0.1341  0.0150  65  LYS B NZ  
3660 N N   . GLY B 68  ? 0.7182 0.8910 1.0233 0.0914  0.1782  0.0516  66  GLY B N   
3661 C CA  . GLY B 68  ? 0.8137 0.9659 1.1206 0.0840  0.1990  0.0436  66  GLY B CA  
3662 C C   . GLY B 68  ? 0.6236 0.7800 0.9344 0.0831  0.2011  0.0420  66  GLY B C   
3663 O O   . GLY B 68  ? 0.7582 0.9094 1.0898 0.0812  0.2197  0.0386  66  GLY B O   
3664 N N   . ARG B 69  ? 0.7263 0.8919 1.0198 0.0838  0.1842  0.0433  67  ARG B N   
3665 C CA  . ARG B 69  ? 0.6665 0.8366 0.9628 0.0816  0.1868  0.0407  67  ARG B CA  
3666 C C   . ARG B 69  ? 0.6799 0.8868 1.0135 0.0922  0.1798  0.0506  67  ARG B C   
3667 O O   . ARG B 69  ? 0.6897 0.9069 1.0470 0.0921  0.1896  0.0491  67  ARG B O   
3668 C CB  . ARG B 69  ? 0.6839 0.8401 0.9396 0.0755  0.1746  0.0360  67  ARG B CB  
3669 C CG  . ARG B 69  ? 0.7171 0.8382 0.9310 0.0646  0.1780  0.0276  67  ARG B CG  
3670 C CD  . ARG B 69  ? 0.7899 0.8945 0.9656 0.0599  0.1675  0.0251  67  ARG B CD  
3671 N NE  . ARG B 69  ? 0.8025 0.9238 0.9759 0.0689  0.1458  0.0315  67  ARG B NE  
3672 C CZ  . ARG B 69  ? 0.7450 0.8795 0.9235 0.0729  0.1381  0.0341  67  ARG B CZ  
3673 N NH1 . ARG B 69  ? 0.7098 0.8450 0.8963 0.0688  0.1491  0.0310  67  ARG B NH1 
3674 N NH2 . ARG B 69  ? 0.7081 0.8559 0.8849 0.0800  0.1204  0.0381  67  ARG B NH2 
3675 N N   . PHE B 70  ? 0.6190 0.8470 0.9580 0.1001  0.1631  0.0600  68  PHE B N   
3676 C CA  . PHE B 70  ? 0.5792 0.8432 0.9470 0.1083  0.1536  0.0701  68  PHE B CA  
3677 C C   . PHE B 70  ? 0.6019 0.8802 1.0005 0.1182  0.1553  0.0826  68  PHE B C   
3678 O O   . PHE B 70  ? 0.6590 0.9228 1.0499 0.1190  0.1574  0.0839  68  PHE B O   
3679 C CB  . PHE B 70  ? 0.5837 0.8614 0.9339 0.1084  0.1346  0.0717  68  PHE B CB  
3680 C CG  . PHE B 70  ? 0.6142 0.8817 0.9401 0.1007  0.1325  0.0621  68  PHE B CG  
3681 C CD1 . PHE B 70  ? 0.5482 0.7858 0.8542 0.0926  0.1449  0.0523  68  PHE B CD1 
3682 C CD2 . PHE B 70  ? 0.5906 0.8762 0.9118 0.1006  0.1196  0.0627  68  PHE B CD2 
3683 C CE1 . PHE B 70  ? 0.5868 0.8110 0.8679 0.0856  0.1439  0.0449  68  PHE B CE1 
3684 C CE2 . PHE B 70  ? 0.5556 0.8285 0.8549 0.0938  0.1197  0.0541  68  PHE B CE2 
3685 C CZ  . PHE B 70  ? 0.5845 0.8258 0.8633 0.0869  0.1315  0.0461  68  PHE B CZ  
3686 N N   . THR B 71  ? 0.5145 0.8216 0.9479 0.1256  0.1541  0.0920  69  THR B N   
3687 C CA  . THR B 71  ? 0.4760 0.7975 0.9400 0.1369  0.1542  0.1073  69  THR B CA  
3688 C C   . THR B 71  ? 0.4143 0.7756 0.8956 0.1430  0.1375  0.1197  69  THR B C   
3689 O O   . THR B 71  ? 0.5196 0.9026 1.0165 0.1420  0.1357  0.1178  69  THR B O   
3690 C CB  . THR B 71  ? 0.5226 0.8362 1.0195 0.1415  0.1739  0.1077  69  THR B CB  
3691 O OG1 . THR B 71  ? 0.6237 0.8997 1.1026 0.1345  0.1903  0.0968  69  THR B OG1 
3692 C CG2 . THR B 71  ? 0.4714 0.8037 1.0048 0.1559  0.1720  0.1268  69  THR B CG2 
3693 N N   . ILE B 72  ? 0.4984 0.8696 0.9757 0.1475  0.1260  0.1316  70  ILE B N   
3694 C CA  . ILE B 72  ? 0.5028 0.9110 0.9920 0.1516  0.1097  0.1447  70  ILE B CA  
3695 C C   . ILE B 72  ? 0.4931 0.9131 1.0161 0.1647  0.1114  0.1641  70  ILE B C   
3696 O O   . ILE B 72  ? 0.5703 0.9665 1.0973 0.1699  0.1222  0.1689  70  ILE B O   
3697 C CB  . ILE B 72  ? 0.4385 0.8500 0.8986 0.1462  0.0962  0.1448  70  ILE B CB  
3698 C CG1 . ILE B 72  ? 0.4283 0.8780 0.8968 0.1475  0.0803  0.1574  70  ILE B CG1 
3699 C CG2 . ILE B 72  ? 0.4475 0.8356 0.8974 0.1485  0.1010  0.1487  70  ILE B CG2 
3700 C CD1 . ILE B 72  ? 0.3326 0.7858 0.7762 0.1419  0.0697  0.1587  70  ILE B CD1 
3701 N N   . SER B 73  ? 0.4964 0.9533 1.0444 0.1701  0.1008  0.1752  71  SER B N   
3702 C CA  . SER B 73  ? 0.5063 0.9792 1.0884 0.1845  0.0985  0.1969  71  SER B CA  
3703 C C   . SER B 73  ? 0.5035 1.0200 1.0898 0.1852  0.0768  0.2103  71  SER B C   
3704 O O   . SER B 73  ? 0.5174 1.0535 1.0879 0.1741  0.0674  0.1998  71  SER B O   
3705 C CB  . SER B 73  ? 0.5782 1.0516 1.2019 0.1930  0.1129  0.1959  71  SER B CB  
3706 O OG  . SER B 73  ? 0.5312 1.0342 1.1671 0.1884  0.1053  0.1885  71  SER B OG  
3707 N N   . ARG B 74  ? 0.5195 1.0487 1.1245 0.1973  0.0693  0.2334  72  ARG B N   
3708 C CA  . ARG B 74  ? 0.5282 1.0959 1.1312 0.1963  0.0471  0.2473  72  ARG B CA  
3709 C C   . ARG B 74  ? 0.5914 1.1692 1.2243 0.2091  0.0413  0.2647  72  ARG B C   
3710 O O   . ARG B 74  ? 0.6193 1.1702 1.2709 0.2204  0.0544  0.2711  72  ARG B O   
3711 C CB  . ARG B 74  ? 0.5011 1.0673 1.0728 0.1921  0.0379  0.2579  72  ARG B CB  
3712 C CG  . ARG B 74  ? 0.5659 1.1204 1.1448 0.2051  0.0375  0.2832  72  ARG B CG  
3713 C CD  . ARG B 74  ? 0.5913 1.1291 1.1291 0.1955  0.0344  0.2850  72  ARG B CD  
3714 N NE  . ARG B 74  ? 0.6216 1.1940 1.1418 0.1877  0.0140  0.2950  72  ARG B NE  
3715 C CZ  . ARG B 74  ? 0.5927 1.1622 1.0752 0.1729  0.0095  0.2876  72  ARG B CZ  
3716 N NH1 . ARG B 74  ? 0.5568 1.0932 1.0174 0.1655  0.0222  0.2708  72  ARG B NH1 
3717 N NH2 . ARG B 74  ? 0.5540 1.1562 1.0214 0.1645  -0.0079 0.2966  72  ARG B NH2 
3718 N N   . ASP B 75  ? 0.5532 1.1710 1.1913 0.2069  0.0220  0.2713  73  ASP B N   
3719 C CA  . ASP B 75  ? 0.6220 1.2566 1.2875 0.2192  0.0115  0.2898  73  ASP B CA  
3720 C C   . ASP B 75  ? 0.6034 1.2716 1.2518 0.2164  -0.0124 0.3093  73  ASP B C   
3721 O O   . ASP B 75  ? 0.6000 1.3042 1.2398 0.2043  -0.0261 0.3013  73  ASP B O   
3722 C CB  . ASP B 75  ? 0.6038 1.2587 1.3003 0.2190  0.0122  0.2755  73  ASP B CB  
3723 C CG  . ASP B 75  ? 0.7819 1.4638 1.5070 0.2309  -0.0032 0.2938  73  ASP B CG  
3724 O OD1 . ASP B 75  ? 0.8796 1.5420 1.6319 0.2458  0.0057  0.3032  73  ASP B OD1 
3725 O OD2 . ASP B 75  ? 0.7552 1.4781 1.4757 0.2250  -0.0241 0.2987  73  ASP B OD2 
3726 N N   . ASN B 76  ? 0.6321 1.2881 1.2746 0.2264  -0.0163 0.3346  74  ASN B N   
3727 C CA  . ASN B 76  ? 0.6438 1.3289 1.2663 0.2233  -0.0384 0.3557  74  ASN B CA  
3728 C C   . ASN B 76  ? 0.7284 1.4488 1.3718 0.2290  -0.0576 0.3683  74  ASN B C   
3729 O O   . ASN B 76  ? 0.7706 1.5199 1.3959 0.2243  -0.0781 0.3850  74  ASN B O   
3730 C CB  . ASN B 76  ? 0.6210 1.2790 1.2293 0.2323  -0.0350 0.3800  74  ASN B CB  
3731 C CG  . ASN B 76  ? 0.6479 1.2825 1.2311 0.2239  -0.0214 0.3686  74  ASN B CG  
3732 O OD1 . ASN B 76  ? 0.5815 1.2320 1.1454 0.2084  -0.0239 0.3497  74  ASN B OD1 
3733 N ND2 . ASN B 76  ? 0.6516 1.2483 1.2361 0.2341  -0.0061 0.3790  74  ASN B ND2 
3734 N N   . ALA B 77  ? 0.7021 1.4225 1.3832 0.2382  -0.0515 0.3602  75  ALA B N   
3735 C CA  . ALA B 77  ? 0.7294 1.4882 1.4352 0.2436  -0.0703 0.3690  75  ALA B CA  
3736 C C   . ALA B 77  ? 0.7238 1.5270 1.4208 0.2256  -0.0836 0.3513  75  ALA B C   
3737 O O   . ALA B 77  ? 0.6995 1.5416 1.3917 0.2219  -0.1061 0.3633  75  ALA B O   
3738 C CB  . ALA B 77  ? 0.6884 1.4355 1.4408 0.2587  -0.0581 0.3635  75  ALA B CB  
3739 N N   . LYS B 78  ? 0.7050 1.5025 1.3986 0.2134  -0.0694 0.3229  76  LYS B N   
3740 C CA  . LYS B 78  ? 0.7231 1.5579 1.4081 0.1948  -0.0775 0.3034  76  LYS B CA  
3741 C C   . LYS B 78  ? 0.6525 1.4842 1.2950 0.1771  -0.0759 0.2946  76  LYS B C   
3742 O O   . LYS B 78  ? 0.6397 1.4989 1.2718 0.1597  -0.0798 0.2770  76  LYS B O   
3743 C CB  . LYS B 78  ? 0.7100 1.5442 1.4244 0.1925  -0.0623 0.2765  76  LYS B CB  
3744 C CG  . LYS B 78  ? 0.7861 1.6137 1.5455 0.2108  -0.0567 0.2807  76  LYS B CG  
3745 C CD  . LYS B 78  ? 0.9057 1.7387 1.6931 0.2056  -0.0418 0.2525  76  LYS B CD  
3746 C CE  . LYS B 78  ? 0.8544 1.6438 1.6268 0.2003  -0.0163 0.2349  76  LYS B CE  
3747 N NZ  . LYS B 78  ? 0.8508 1.5973 1.6352 0.2159  -0.0005 0.2439  76  LYS B NZ  
3748 N N   . ASN B 79  ? 0.6489 1.4488 1.2686 0.1806  -0.0692 0.3055  77  ASN B N   
3749 C CA  . ASN B 79  ? 0.6641 1.4604 1.2468 0.1654  -0.0667 0.2969  77  ASN B CA  
3750 C C   . ASN B 79  ? 0.6253 1.4126 1.2061 0.1539  -0.0512 0.2662  77  ASN B C   
3751 O O   . ASN B 79  ? 0.5466 1.3543 1.1074 0.1364  -0.0543 0.2518  77  ASN B O   
3752 C CB  . ASN B 79  ? 0.6292 1.4667 1.1866 0.1509  -0.0877 0.3057  77  ASN B CB  
3753 C CG  . ASN B 79  ? 0.7134 1.5617 1.2702 0.1614  -0.1050 0.3377  77  ASN B CG  
3754 O OD1 . ASN B 79  ? 0.7245 1.5463 1.2994 0.1805  -0.1002 0.3545  77  ASN B OD1 
3755 N ND2 . ASN B 79  ? 0.7400 1.6260 1.2739 0.1479  -0.1244 0.3461  77  ASN B ND2 
3756 N N   . THR B 80  ? 0.5502 1.3058 1.1512 0.1632  -0.0333 0.2563  78  THR B N   
3757 C CA  . THR B 80  ? 0.5695 1.3106 1.1672 0.1540  -0.0172 0.2299  78  THR B CA  
3758 C C   . THR B 80  ? 0.5334 1.2268 1.1250 0.1614  0.0014  0.2271  78  THR B C   
3759 O O   . THR B 80  ? 0.5714 1.2421 1.1723 0.1751  0.0054  0.2424  78  THR B O   
3760 C CB  . THR B 80  ? 0.5674 1.3215 1.1962 0.1539  -0.0117 0.2153  78  THR B CB  
3761 O OG1 . THR B 80  ? 0.6460 1.3681 1.2985 0.1678  0.0036  0.2159  78  THR B OG1 
3762 C CG2 . THR B 80  ? 0.6177 1.4167 1.2649 0.1538  -0.0310 0.2245  78  THR B CG2 
3763 N N   . ILE B 81  ? 0.5217 1.2002 1.0973 0.1518  0.0131  0.2074  79  ILE B N   
3764 C CA  . ILE B 81  ? 0.5111 1.1406 1.0740 0.1547  0.0305  0.1988  79  ILE B CA  
3765 C C   . ILE B 81  ? 0.4911 1.1064 1.0555 0.1476  0.0447  0.1758  79  ILE B C   
3766 O O   . ILE B 81  ? 0.4482 1.0856 1.0102 0.1363  0.0415  0.1632  79  ILE B O   
3767 C CB  . ILE B 81  ? 0.4758 1.0816 0.9972 0.1467  0.0286  0.1956  79  ILE B CB  
3768 C CG1 . ILE B 81  ? 0.5225 1.1398 1.0181 0.1296  0.0238  0.1781  79  ILE B CG1 
3769 C CG2 . ILE B 81  ? 0.5603 1.1761 1.0771 0.1520  0.0170  0.2179  79  ILE B CG2 
3770 C CD1 . ILE B 81  ? 0.4965 1.0763 0.9681 0.1232  0.0358  0.1583  79  ILE B CD1 
3771 N N   . TYR B 82  ? 0.4886 1.0657 1.0553 0.1528  0.0615  0.1700  80  TYR B N   
3772 C CA  . TYR B 82  ? 0.4868 1.0461 1.0547 0.1466  0.0769  0.1503  80  TYR B CA  
3773 C C   . TYR B 82  ? 0.4972 1.0087 1.0309 0.1417  0.0881  0.1385  80  TYR B C   
3774 O O   . TYR B 82  ? 0.5094 1.0005 1.0302 0.1463  0.0879  0.1459  80  TYR B O   
3775 C CB  . TYR B 82  ? 0.5206 1.0838 1.1314 0.1566  0.0889  0.1531  80  TYR B CB  
3776 C CG  . TYR B 82  ? 0.6135 1.2182 1.2579 0.1636  0.0754  0.1657  80  TYR B CG  
3777 C CD1 . TYR B 82  ? 0.6413 1.2466 1.2951 0.1760  0.0658  0.1862  80  TYR B CD1 
3778 C CD2 . TYR B 82  ? 0.6162 1.2537 1.2771 0.1561  0.0718  0.1552  80  TYR B CD2 
3779 C CE1 . TYR B 82  ? 0.7389 1.3768 1.4169 0.1819  0.0511  0.1975  80  TYR B CE1 
3780 C CE2 . TYR B 82  ? 0.7617 1.4343 1.4483 0.1610  0.0571  0.1640  80  TYR B CE2 
3781 C CZ  . TYR B 82  ? 0.8040 1.4766 1.4988 0.1745  0.0459  0.1859  80  TYR B CZ  
3782 O OH  . TYR B 82  ? 0.8605 1.5684 1.5806 0.1805  0.0299  0.1966  80  TYR B OH  
3783 N N   . LEU B 83  ? 0.4695 0.9636 0.9882 0.1317  0.0979  0.1199  81  LEU B N   
3784 C CA  . LEU B 83  ? 0.5213 0.9706 1.0085 0.1269  0.1083  0.1085  81  LEU B CA  
3785 C C   . LEU B 83  ? 0.5334 0.9637 1.0256 0.1219  0.1259  0.0948  81  LEU B C   
3786 O O   . LEU B 83  ? 0.4608 0.8978 0.9484 0.1127  0.1283  0.0834  81  LEU B O   
3787 C CB  . LEU B 83  ? 0.5150 0.9562 0.9653 0.1178  0.0997  0.1002  81  LEU B CB  
3788 C CG  . LEU B 83  ? 0.4261 0.8255 0.8443 0.1155  0.1049  0.0926  81  LEU B CG  
3789 C CD1 . LEU B 83  ? 0.4937 0.8870 0.9090 0.1222  0.1001  0.1027  81  LEU B CD1 
3790 C CD2 . LEU B 83  ? 0.4141 0.8040 0.8019 0.1066  0.1000  0.0812  81  LEU B CD2 
3791 N N   . GLN B 84  ? 0.4942 0.8996 0.9950 0.1264  0.1401  0.0951  82  GLN B N   
3792 C CA  . GLN B 84  ? 0.4253 0.8052 0.9243 0.1194  0.1596  0.0807  82  GLN B CA  
3793 C C   . GLN B 84  ? 0.5228 0.8619 0.9739 0.1097  0.1629  0.0697  82  GLN B C   
3794 O O   . GLN B 84  ? 0.5175 0.8387 0.9505 0.1123  0.1592  0.0738  82  GLN B O   
3795 C CB  . GLN B 84  ? 0.4606 0.8320 0.9913 0.1273  0.1751  0.0848  82  GLN B CB  
3796 C CG  . GLN B 84  ? 0.5843 0.9223 1.1064 0.1176  0.1977  0.0684  82  GLN B CG  
3797 C CD  . GLN B 84  ? 0.5476 0.9013 1.0869 0.1106  0.2057  0.0572  82  GLN B CD  
3798 O OE1 . GLN B 84  ? 0.5394 0.9337 1.1173 0.1173  0.1990  0.0635  82  GLN B OE1 
3799 N NE2 . GLN B 84  ? 0.6228 0.9453 1.1327 0.0963  0.2198  0.0406  82  GLN B NE2 
3800 N N   . MET B 85  ? 0.5026 0.8272 0.9331 0.0984  0.1697  0.0561  83  MET B N   
3801 C CA  . MET B 85  ? 0.6257 0.9122 1.0088 0.0897  0.1706  0.0474  83  MET B CA  
3802 C C   . MET B 85  ? 0.6662 0.9206 1.0368 0.0794  0.1912  0.0346  83  MET B C   
3803 O O   . MET B 85  ? 0.6892 0.9444 1.0607 0.0712  0.2000  0.0253  83  MET B O   
3804 C CB  . MET B 85  ? 0.6075 0.9006 0.9687 0.0851  0.1582  0.0444  83  MET B CB  
3805 C CG  . MET B 85  ? 0.6202 0.9482 0.9948 0.0922  0.1400  0.0548  83  MET B CG  
3806 S SD  . MET B 85  ? 0.5643 0.9186 0.9385 0.0847  0.1331  0.0489  83  MET B SD  
3807 C CE  . MET B 85  ? 0.4130 0.7289 0.7389 0.0790  0.1298  0.0412  83  MET B CE  
3808 N N   . ASN B 86  ? 0.6754 0.9007 1.0322 0.0778  0.2003  0.0328  84  ASN B N   
3809 C CA  . ASN B 86  ? 0.6330 0.8236 0.9710 0.0655  0.2207  0.0201  84  ASN B CA  
3810 C C   . ASN B 86  ? 0.7551 0.9086 1.0375 0.0570  0.2155  0.0159  84  ASN B C   
3811 O O   . ASN B 86  ? 0.7795 0.9338 1.0452 0.0625  0.1982  0.0228  84  ASN B O   
3812 C CB  . ASN B 86  ? 0.6556 0.8394 1.0189 0.0674  0.2377  0.0193  84  ASN B CB  
3813 C CG  . ASN B 86  ? 0.6147 0.8362 1.0324 0.0823  0.2348  0.0309  84  ASN B CG  
3814 O OD1 . ASN B 86  ? 0.6586 0.9068 1.1114 0.0852  0.2382  0.0306  84  ASN B OD1 
3815 N ND2 . ASN B 86  ? 0.6498 0.8739 1.0746 0.0915  0.2282  0.0413  84  ASN B ND2 
3816 N N   . SER B 87  ? 0.7550 0.8761 1.0090 0.0430  0.2309  0.0045  85  SER B N   
3817 C CA  . SER B 87  ? 0.7904 0.8732 0.9884 0.0339  0.2265  0.0014  85  SER B CA  
3818 C C   . SER B 87  ? 0.7973 0.8847 0.9744 0.0392  0.2051  0.0077  85  SER B C   
3819 O O   . SER B 87  ? 0.8485 0.9284 1.0026 0.0434  0.1890  0.0131  85  SER B O   
3820 C CB  . SER B 87  ? 0.7813 0.8492 0.9652 0.0334  0.2254  0.0026  85  SER B CB  
3821 O OG  . SER B 87  ? 0.8609 0.9052 1.0404 0.0210  0.2491  -0.0078 85  SER B OG  
3822 N N   . LEU B 88  ? 0.8062 0.9067 0.9938 0.0383  0.2061  0.0056  86  LEU B N   
3823 C CA  . LEU B 88  ? 0.7957 0.9027 0.9702 0.0430  0.1891  0.0102  86  LEU B CA  
3824 C C   . LEU B 88  ? 0.7622 0.8264 0.8833 0.0358  0.1869  0.0083  86  LEU B C   
3825 O O   . LEU B 88  ? 0.8765 0.9123 0.9744 0.0235  0.2024  0.0007  86  LEU B O   
3826 C CB  . LEU B 88  ? 0.8163 0.9502 1.0179 0.0417  0.1934  0.0065  86  LEU B CB  
3827 C CG  . LEU B 88  ? 0.7310 0.9141 0.9815 0.0520  0.1855  0.0130  86  LEU B CG  
3828 C CD1 . LEU B 88  ? 0.7238 0.9346 1.0015 0.0474  0.1924  0.0070  86  LEU B CD1 
3829 C CD2 . LEU B 88  ? 0.6815 0.8793 0.9287 0.0617  0.1642  0.0222  86  LEU B CD2 
3830 N N   . ASN B 89  ? 0.7622 0.8215 0.8643 0.0434  0.1678  0.0155  87  ASN B N   
3831 C CA  . ASN B 89  ? 0.7964 0.8191 0.8512 0.0405  0.1606  0.0172  87  ASN B CA  
3832 C C   . ASN B 89  ? 0.8366 0.8661 0.8921 0.0464  0.1507  0.0197  87  ASN B C   
3833 O O   . ASN B 89  ? 0.8453 0.9109 0.9359 0.0529  0.1457  0.0205  87  ASN B O   
3834 C CB  . ASN B 89  ? 0.8442 0.8581 0.8797 0.0454  0.1455  0.0227  87  ASN B CB  
3835 C CG  . ASN B 89  ? 0.8246 0.8719 0.8872 0.0591  0.1271  0.0286  87  ASN B CG  
3836 O OD1 . ASN B 89  ? 0.9117 0.9558 0.9616 0.0662  0.1110  0.0330  87  ASN B OD1 
3837 N ND2 . ASN B 89  ? 0.7811 0.8592 0.8813 0.0629  0.1302  0.0289  87  ASN B ND2 
3838 N N   . PRO B 90  ? 0.8863 0.8798 0.9024 0.0434  0.1489  0.0210  88  PRO B N   
3839 C CA  . PRO B 90  ? 0.8713 0.8673 0.8889 0.0483  0.1428  0.0222  88  PRO B CA  
3840 C C   . PRO B 90  ? 0.8627 0.8887 0.9039 0.0621  0.1235  0.0275  88  PRO B C   
3841 O O   . PRO B 90  ? 0.7943 0.8358 0.8514 0.0648  0.1220  0.0257  88  PRO B O   
3842 C CB  . PRO B 90  ? 0.9734 0.9189 0.9403 0.0449  0.1424  0.0258  88  PRO B CB  
3843 C CG  . PRO B 90  ? 1.0373 0.9557 0.9783 0.0315  0.1575  0.0219  88  PRO B CG  
3844 C CD  . PRO B 90  ? 0.9564 0.9031 0.9242 0.0331  0.1562  0.0205  88  PRO B CD  
3845 N N   . GLY B 91  ? 0.8784 0.9131 0.9222 0.0691  0.1103  0.0324  89  GLY B N   
3846 C CA  . GLY B 91  ? 0.7763 0.8405 0.8442 0.0806  0.0941  0.0357  89  GLY B CA  
3847 C C   . GLY B 91  ? 0.7370 0.8439 0.8467 0.0817  0.0970  0.0335  89  GLY B C   
3848 O O   . GLY B 91  ? 0.7906 0.9219 0.9193 0.0890  0.0858  0.0351  89  GLY B O   
3849 N N   . ASP B 92  ? 0.7183 0.8355 0.8431 0.0745  0.1115  0.0301  90  ASP B N   
3850 C CA  . ASP B 92  ? 0.7066 0.8655 0.8705 0.0758  0.1129  0.0301  90  ASP B CA  
3851 C C   . ASP B 92  ? 0.7044 0.8788 0.8792 0.0715  0.1167  0.0253  90  ASP B C   
3852 O O   . ASP B 92  ? 0.6695 0.8811 0.8744 0.0717  0.1157  0.0257  90  ASP B O   
3853 C CB  . ASP B 92  ? 0.6672 0.8335 0.8480 0.0718  0.1257  0.0293  90  ASP B CB  
3854 C CG  . ASP B 92  ? 0.6613 0.8173 0.8368 0.0747  0.1239  0.0328  90  ASP B CG  
3855 O OD1 . ASP B 92  ? 0.8096 0.9669 0.9790 0.0811  0.1102  0.0366  90  ASP B OD1 
3856 O OD2 . ASP B 92  ? 0.6919 0.8388 0.8706 0.0696  0.1375  0.0302  90  ASP B OD2 
3857 N N   . THR B 93  ? 0.7435 0.8896 0.8932 0.0670  0.1214  0.0209  91  THR B N   
3858 C CA  . THR B 93  ? 0.7067 0.8646 0.8647 0.0608  0.1275  0.0141  91  THR B CA  
3859 C C   . THR B 93  ? 0.6129 0.7971 0.7870 0.0667  0.1151  0.0153  91  THR B C   
3860 O O   . THR B 93  ? 0.6644 0.8327 0.8255 0.0741  0.1054  0.0180  91  THR B O   
3861 C CB  . THR B 93  ? 0.7690 0.8837 0.8933 0.0550  0.1368  0.0098  91  THR B CB  
3862 O OG1 . THR B 93  ? 0.7654 0.8597 0.8769 0.0454  0.1524  0.0059  91  THR B OG1 
3863 C CG2 . THR B 93  ? 0.7133 0.8379 0.8452 0.0488  0.1430  0.0018  91  THR B CG2 
3864 N N   . ALA B 94  ? 0.5749 0.8000 0.7776 0.0630  0.1154  0.0130  92  ALA B N   
3865 C CA  . ALA B 94  ? 0.5515 0.8038 0.7688 0.0654  0.1056  0.0129  92  ALA B CA  
3866 C C   . ALA B 94  ? 0.5738 0.8686 0.8164 0.0569  0.1087  0.0095  92  ALA B C   
3867 O O   . ALA B 94  ? 0.5969 0.9027 0.8503 0.0516  0.1166  0.0081  92  ALA B O   
3868 C CB  . ALA B 94  ? 0.5505 0.8116 0.7742 0.0759  0.0921  0.0212  92  ALA B CB  
3869 N N   . VAL B 95  ? 0.5125 0.8325 0.7651 0.0549  0.1024  0.0074  93  VAL B N   
3870 C CA  . VAL B 95  ? 0.5039 0.8697 0.7792 0.0473  0.1006  0.0067  93  VAL B CA  
3871 C C   . VAL B 95  ? 0.4615 0.8497 0.7517 0.0559  0.0890  0.0193  93  VAL B C   
3872 O O   . VAL B 95  ? 0.4250 0.8072 0.7107 0.0626  0.0810  0.0231  93  VAL B O   
3873 C CB  . VAL B 95  ? 0.5044 0.8849 0.7793 0.0380  0.1014  -0.0029 93  VAL B CB  
3874 C CG1 . VAL B 95  ? 0.4661 0.8966 0.7606 0.0307  0.0948  -0.0006 93  VAL B CG1 
3875 C CG2 . VAL B 95  ? 0.4589 0.8207 0.7225 0.0273  0.1160  -0.0159 93  VAL B CG2 
3876 N N   . TYR B 96  ? 0.4514 0.8647 0.7610 0.0558  0.0888  0.0255  94  TYR B N   
3877 C CA  . TYR B 96  ? 0.4722 0.9026 0.7965 0.0646  0.0799  0.0390  94  TYR B CA  
3878 C C   . TYR B 96  ? 0.3900 0.8648 0.7296 0.0594  0.0714  0.0434  94  TYR B C   
3879 O O   . TYR B 96  ? 0.5730 1.0744 0.9228 0.0501  0.0732  0.0387  94  TYR B O   
3880 C CB  . TYR B 96  ? 0.3380 0.7639 0.6756 0.0700  0.0857  0.0447  94  TYR B CB  
3881 C CG  . TYR B 96  ? 0.4641 0.8462 0.7831 0.0751  0.0923  0.0429  94  TYR B CG  
3882 C CD1 . TYR B 96  ? 0.4124 0.7634 0.7097 0.0695  0.1012  0.0326  94  TYR B CD1 
3883 C CD2 . TYR B 96  ? 0.4512 0.8219 0.7718 0.0842  0.0899  0.0514  94  TYR B CD2 
3884 C CE1 . TYR B 96  ? 0.4516 0.7629 0.7276 0.0729  0.1055  0.0321  94  TYR B CE1 
3885 C CE2 . TYR B 96  ? 0.4804 0.8132 0.7814 0.0865  0.0952  0.0489  94  TYR B CE2 
3886 C CZ  . TYR B 96  ? 0.5370 0.8410 0.8149 0.0809  0.1021  0.0398  94  TYR B CZ  
3887 O OH  . TYR B 96  ? 0.5815 0.8482 0.8360 0.0821  0.1059  0.0385  94  TYR B OH  
3888 N N   . SER B 97  ? 0.3671 0.8500 0.7067 0.0641  0.0622  0.0520  95  SER B N   
3889 C CA  . SER B 97  ? 0.4194 0.9407 0.7669 0.0582  0.0534  0.0576  95  SER B CA  
3890 C C   . SER B 97  ? 0.4801 1.0097 0.8379 0.0682  0.0460  0.0749  95  SER B C   
3891 O O   . SER B 97  ? 0.3794 0.8836 0.7308 0.0766  0.0468  0.0782  95  SER B O   
3892 C CB  . SER B 97  ? 0.4894 1.0106 0.8216 0.0495  0.0521  0.0480  95  SER B CB  
3893 O OG  . SER B 97  ? 0.6053 1.1164 0.9289 0.0404  0.0607  0.0322  95  SER B OG  
3894 N N   . CYS B 98  ? 0.4946 1.0597 0.8682 0.0671  0.0388  0.0861  96  CYS B N   
3895 C CA  . CYS B 98  ? 0.4464 1.0207 0.8283 0.0758  0.0314  0.1045  96  CYS B CA  
3896 C C   . CYS B 98  ? 0.4186 1.0075 0.7855 0.0675  0.0237  0.1066  96  CYS B C   
3897 O O   . CYS B 98  ? 0.4501 1.0579 0.8081 0.0538  0.0219  0.0968  96  CYS B O   
3898 C CB  . CYS B 98  ? 0.4013 1.0060 0.8094 0.0809  0.0262  0.1182  96  CYS B CB  
3899 S SG  . CYS B 98  ? 0.8161 1.4703 1.2311 0.0661  0.0182  0.1135  96  CYS B SG  
3900 N N   . ALA B 99  ? 0.3993 0.9781 0.7627 0.0743  0.0212  0.1182  97  ALA B N   
3901 C CA  . ALA B 99  ? 0.3744 0.9621 0.7215 0.0657  0.0164  0.1195  97  ALA B CA  
3902 C C   . ALA B 99  ? 0.3663 0.9631 0.7174 0.0721  0.0098  0.1415  97  ALA B C   
3903 O O   . ALA B 99  ? 0.4422 1.0243 0.8068 0.0858  0.0124  0.1530  97  ALA B O   
3904 C CB  . ALA B 99  ? 0.3706 0.9285 0.7036 0.0648  0.0231  0.1061  97  ALA B CB  
3905 N N   . ALA B 100 ? 0.3358 0.9547 0.6735 0.0613  0.0024  0.1471  98  ALA B N   
3906 C CA  . ALA B 100 ? 0.3893 1.0156 0.7251 0.0656  -0.0044 0.1695  98  ALA B CA  
3907 C C   . ALA B 100 ? 0.4832 1.1030 0.7939 0.0539  -0.0028 0.1659  98  ALA B C   
3908 O O   . ALA B 100 ? 0.4627 1.0916 0.7592 0.0384  -0.0013 0.1494  98  ALA B O   
3909 C CB  . ALA B 100 ? 0.4160 1.0823 0.7596 0.0634  -0.0180 0.1852  98  ALA B CB  
3910 N N   . THR B 101 ? 0.4570 1.0598 0.7634 0.0606  -0.0011 0.1802  99  THR B N   
3911 C CA  . THR B 101 ? 0.4511 1.0474 0.7339 0.0488  0.0017  0.1784  99  THR B CA  
3912 C C   . THR B 101 ? 0.5663 1.1483 0.8466 0.0577  0.0019  0.2013  99  THR B C   
3913 O O   . THR B 101 ? 0.5026 1.0740 0.8020 0.0743  0.0026  0.2151  99  THR B O   
3914 C CB  . THR B 101 ? 0.4808 1.0538 0.7590 0.0444  0.0132  0.1541  99  THR B CB  
3915 O OG1 . THR B 101 ? 0.4333 1.0086 0.6902 0.0284  0.0163  0.1475  99  THR B OG1 
3916 C CG2 . THR B 101 ? 0.4111 0.9524 0.7000 0.0585  0.0213  0.1554  99  THR B CG2 
3917 N N   . LEU B 102 ? 0.5203 1.1003 0.7762 0.0455  0.0032  0.2047  100 LEU B N   
3918 C CA  . LEU B 102 ? 0.5739 1.1356 0.8219 0.0513  0.0057  0.2257  100 LEU B CA  
3919 C C   . LEU B 102 ? 0.5316 1.0573 0.7836 0.0561  0.0213  0.2140  100 LEU B C   
3920 O O   . LEU B 102 ? 0.5292 1.0483 0.7812 0.0495  0.0283  0.1893  100 LEU B O   
3921 C CB  . LEU B 102 ? 0.4990 1.0718 0.7151 0.0337  0.0017  0.2338  100 LEU B CB  
3922 C CG  . LEU B 102 ? 0.5341 1.1431 0.7419 0.0286  -0.0158 0.2518  100 LEU B CG  
3923 C CD1 . LEU B 102 ? 0.5405 1.1514 0.7131 0.0142  -0.0191 0.2674  100 LEU B CD1 
3924 C CD2 . LEU B 102 ? 0.5725 1.1902 0.8079 0.0500  -0.0258 0.2745  100 LEU B CD2 
3925 N N   . PRO B 103 ? 0.5432 1.0458 0.8000 0.0676  0.0270  0.2313  101 PRO B N   
3926 C CA  . PRO B 103 ? 0.5394 1.0094 0.8010 0.0710  0.0426  0.2188  101 PRO B CA  
3927 C C   . PRO B 103 ? 0.5321 0.9940 0.7737 0.0542  0.0513  0.2009  101 PRO B C   
3928 O O   . PRO B 103 ? 0.4975 0.9415 0.7458 0.0543  0.0618  0.1824  101 PRO B O   
3929 C CB  . PRO B 103 ? 0.5953 1.0440 0.8627 0.0839  0.0478  0.2437  101 PRO B CB  
3930 C CG  . PRO B 103 ? 0.6509 1.1198 0.9079 0.0838  0.0344  0.2702  101 PRO B CG  
3931 C CD  . PRO B 103 ? 0.6223 1.1276 0.8831 0.0789  0.0200  0.2628  101 PRO B CD  
3932 N N   . ALA B 104 ? 0.5154 0.9910 0.7329 0.0389  0.0476  0.2048  102 ALA B N   
3933 C CA  . ALA B 104 ? 0.4853 0.9556 0.6865 0.0213  0.0575  0.1843  102 ALA B CA  
3934 C C   . ALA B 104 ? 0.4839 0.9667 0.6959 0.0158  0.0576  0.1553  102 ALA B C   
3935 O O   . ALA B 104 ? 0.4515 0.9267 0.6625 0.0067  0.0675  0.1340  102 ALA B O   
3936 C CB  . ALA B 104 ? 0.5174 0.9988 0.6875 0.0040  0.0547  0.1950  102 ALA B CB  
3937 N N   . TRP B 105 ? 0.5058 1.0071 0.7296 0.0215  0.0473  0.1540  103 TRP B N   
3938 C CA  . TRP B 105 ? 0.4505 0.9594 0.6847 0.0181  0.0481  0.1284  103 TRP B CA  
3939 C C   . TRP B 105 ? 0.4300 0.9194 0.6843 0.0314  0.0528  0.1168  103 TRP B C   
3940 O O   . TRP B 105 ? 0.3767 0.8652 0.6382 0.0287  0.0557  0.0948  103 TRP B O   
3941 C CB  . TRP B 105 ? 0.4030 0.9364 0.6406 0.0177  0.0374  0.1304  103 TRP B CB  
3942 C CG  . TRP B 105 ? 0.4212 0.9788 0.6380 -0.0001 0.0327  0.1334  103 TRP B CG  
3943 C CD1 . TRP B 105 ? 0.4494 1.0143 0.6463 -0.0065 0.0280  0.1545  103 TRP B CD1 
3944 C CD2 . TRP B 105 ? 0.4162 0.9933 0.6281 -0.0151 0.0328  0.1149  103 TRP B CD2 
3945 N NE1 . TRP B 105 ? 0.4626 1.0522 0.6402 -0.0259 0.0242  0.1498  103 TRP B NE1 
3946 C CE2 . TRP B 105 ? 0.4419 1.0394 0.6294 -0.0321 0.0282  0.1244  103 TRP B CE2 
3947 C CE3 . TRP B 105 ? 0.3958 0.9735 0.6207 -0.0161 0.0370  0.0915  103 TRP B CE3 
3948 C CZ2 . TRP B 105 ? 0.4466 1.0661 0.6227 -0.0517 0.0289  0.1092  103 TRP B CZ2 
3949 C CZ3 . TRP B 105 ? 0.4004 0.9976 0.6163 -0.0339 0.0387  0.0770  103 TRP B CZ3 
3950 C CH2 . TRP B 105 ? 0.4250 1.0435 0.6169 -0.0523 0.0353  0.0848  103 TRP B CH2 
3951 N N   . THR B 106 ? 0.4443 0.9180 0.7078 0.0456  0.0536  0.1312  104 THR B N   
3952 C CA  . THR B 106 ? 0.3796 0.8346 0.6585 0.0562  0.0583  0.1206  104 THR B CA  
3953 C C   . THR B 106 ? 0.4281 0.8636 0.7053 0.0532  0.0694  0.1128  104 THR B C   
3954 O O   . THR B 106 ? 0.4308 0.8572 0.7174 0.0558  0.0725  0.0958  104 THR B O   
3955 C CB  . THR B 106 ? 0.4788 0.9261 0.7702 0.0711  0.0563  0.1364  104 THR B CB  
3956 O OG1 . THR B 106 ? 0.5074 0.9423 0.7965 0.0751  0.0615  0.1560  104 THR B OG1 
3957 C CG2 . THR B 106 ? 0.3687 0.8381 0.6641 0.0732  0.0458  0.1441  104 THR B CG2 
3958 N N   . GLY B 107 ? 0.4378 0.8666 0.7024 0.0473  0.0755  0.1248  105 GLY B N   
3959 C CA  . GLY B 107 ? 0.4557 0.8650 0.7190 0.0431  0.0884  0.1163  105 GLY B CA  
3960 C C   . GLY B 107 ? 0.4796 0.8675 0.7559 0.0554  0.0943  0.1196  105 GLY B C   
3961 O O   . GLY B 107 ? 0.4567 0.8408 0.7405 0.0673  0.0909  0.1354  105 GLY B O   
3962 N N   . ILE B 108 ? 0.5376 0.9129 0.8178 0.0512  0.1041  0.1027  106 ILE B N   
3963 C CA  . ILE B 108 ? 0.4700 0.8238 0.7594 0.0588  0.1125  0.1029  106 ILE B CA  
3964 C C   . ILE B 108 ? 0.4409 0.7978 0.7425 0.0664  0.1053  0.0903  106 ILE B C   
3965 O O   . ILE B 108 ? 0.4945 0.8377 0.8028 0.0751  0.1084  0.0964  106 ILE B O   
3966 C CB  . ILE B 108 ? 0.5028 0.8421 0.7889 0.0484  0.1276  0.0906  106 ILE B CB  
3967 C CG1 . ILE B 108 ? 0.5462 0.8699 0.8185 0.0443  0.1385  0.1100  106 ILE B CG1 
3968 C CG2 . ILE B 108 ? 0.5205 0.8438 0.8172 0.0523  0.1351  0.0801  106 ILE B CG2 
3969 C CD1 . ILE B 108 ? 0.4986 0.8161 0.7608 0.0283  0.1515  0.0969  106 ILE B CD1 
3970 N N   . ILE B 109 ? 0.4437 0.8167 0.7479 0.0631  0.0966  0.0729  107 ILE B N   
3971 C CA  . ILE B 109 ? 0.4597 0.8322 0.7720 0.0699  0.0897  0.0614  107 ILE B CA  
3972 C C   . ILE B 109 ? 0.4309 0.8205 0.7442 0.0720  0.0772  0.0576  107 ILE B C   
3973 O O   . ILE B 109 ? 0.4793 0.8692 0.7971 0.0763  0.0704  0.0463  107 ILE B O   
3974 C CB  . ILE B 109 ? 0.4947 0.8644 0.8123 0.0649  0.0929  0.0403  107 ILE B CB  
3975 C CG1 . ILE B 109 ? 0.4082 0.7912 0.7268 0.0538  0.0956  0.0275  107 ILE B CG1 
3976 C CG2 . ILE B 109 ? 0.5477 0.8969 0.8649 0.0640  0.1057  0.0421  107 ILE B CG2 
3977 C CD1 . ILE B 109 ? 0.4922 0.8794 0.8214 0.0494  0.0964  0.0048  107 ILE B CD1 
3978 N N   . GLY B 110 ? 0.4180 0.8209 0.7257 0.0684  0.0743  0.0671  108 GLY B N   
3979 C CA  . GLY B 110 ? 0.3379 0.7566 0.6462 0.0679  0.0651  0.0616  108 GLY B CA  
3980 C C   . GLY B 110 ? 0.3756 0.7979 0.6836 0.0747  0.0596  0.0759  108 GLY B C   
3981 O O   . GLY B 110 ? 0.4359 0.8732 0.7423 0.0718  0.0538  0.0742  108 GLY B O   
3982 N N   . GLY B 111 ? 0.4167 0.8259 0.7282 0.0830  0.0627  0.0886  109 GLY B N   
3983 C CA  . GLY B 111 ? 0.4095 0.8238 0.7250 0.0896  0.0588  0.1019  109 GLY B CA  
3984 C C   . GLY B 111 ? 0.4080 0.8222 0.7260 0.0931  0.0537  0.0925  109 GLY B C   
3985 O O   . GLY B 111 ? 0.4076 0.8305 0.7293 0.0959  0.0505  0.1003  109 GLY B O   
3986 N N   . ARG B 112 ? 0.3621 0.7668 0.6781 0.0930  0.0528  0.0765  110 ARG B N   
3987 C CA  . ARG B 112 ? 0.4106 0.8094 0.7252 0.0967  0.0485  0.0685  110 ARG B CA  
3988 C C   . ARG B 112 ? 0.4618 0.8734 0.7746 0.0919  0.0432  0.0581  110 ARG B C   
3989 O O   . ARG B 112 ? 0.4368 0.8422 0.7473 0.0946  0.0405  0.0527  110 ARG B O   
3990 C CB  . ARG B 112 ? 0.4878 0.8672 0.7998 0.1003  0.0490  0.0588  110 ARG B CB  
3991 C CG  . ARG B 112 ? 0.4879 0.8518 0.8009 0.1029  0.0569  0.0652  110 ARG B CG  
3992 C CD  . ARG B 112 ? 0.5359 0.8831 0.8447 0.1074  0.0584  0.0654  110 ARG B CD  
3993 N NE  . ARG B 112 ? 0.6485 0.9783 0.9576 0.1081  0.0680  0.0676  110 ARG B NE  
3994 C CZ  . ARG B 112 ? 0.6013 0.9152 0.9016 0.1067  0.0689  0.0580  110 ARG B CZ  
3995 N NH1 . ARG B 112 ? 0.6514 0.9644 0.9422 0.1065  0.0589  0.0475  110 ARG B NH1 
3996 N NH2 . ARG B 112 ? 0.6290 0.9273 0.9298 0.1053  0.0802  0.0592  110 ARG B NH2 
3997 N N   . ARG B 113 ? 0.4200 0.8468 0.7330 0.0839  0.0435  0.0545  111 ARG B N   
3998 C CA  . ARG B 113 ? 0.3968 0.8345 0.7102 0.0780  0.0414  0.0420  111 ARG B CA  
3999 C C   . ARG B 113 ? 0.3963 0.8505 0.7062 0.0720  0.0405  0.0479  111 ARG B C   
4000 O O   . ARG B 113 ? 0.3632 0.8318 0.6697 0.0663  0.0408  0.0588  111 ARG B O   
4001 C CB  . ARG B 113 ? 0.3522 0.7986 0.6681 0.0700  0.0444  0.0322  111 ARG B CB  
4002 C CG  . ARG B 113 ? 0.4342 0.8707 0.7584 0.0745  0.0437  0.0187  111 ARG B CG  
4003 C CD  . ARG B 113 ? 0.5301 0.9541 0.8567 0.0841  0.0376  0.0129  111 ARG B CD  
4004 N NE  . ARG B 113 ? 0.5816 1.0115 0.9154 0.0825  0.0365  -0.0002 111 ARG B NE  
4005 C CZ  . ARG B 113 ? 0.6007 1.0191 0.9351 0.0900  0.0321  -0.0042 111 ARG B CZ  
4006 N NH1 . ARG B 113 ? 0.6266 1.0274 0.9521 0.0982  0.0280  0.0034  111 ARG B NH1 
4007 N NH2 . ARG B 113 ? 0.3556 0.7782 0.6992 0.0886  0.0333  -0.0162 111 ARG B NH2 
4008 N N   . PRO B 114 ? 0.3915 0.8447 0.7013 0.0723  0.0395  0.0414  112 PRO B N   
4009 C CA  . PRO B 114 ? 0.4347 0.9063 0.7418 0.0645  0.0393  0.0450  112 PRO B CA  
4010 C C   . PRO B 114 ? 0.3652 0.8582 0.6683 0.0504  0.0409  0.0396  112 PRO B C   
4011 O O   . PRO B 114 ? 0.3548 0.8684 0.6533 0.0420  0.0392  0.0466  112 PRO B O   
4012 C CB  . PRO B 114 ? 0.3896 0.8495 0.6965 0.0670  0.0406  0.0355  112 PRO B CB  
4013 C CG  . PRO B 114 ? 0.4583 0.8993 0.7673 0.0732  0.0404  0.0244  112 PRO B CG  
4014 C CD  . PRO B 114 ? 0.3208 0.7558 0.6319 0.0788  0.0385  0.0301  112 PRO B CD  
4015 N N   . GLY B 115 ? 0.3097 0.7998 0.6146 0.0465  0.0442  0.0269  113 GLY B N   
4016 C CA  . GLY B 115 ? 0.3168 0.8252 0.6164 0.0310  0.0481  0.0203  113 GLY B CA  
4017 C C   . GLY B 115 ? 0.3610 0.8804 0.6508 0.0250  0.0469  0.0346  113 GLY B C   
4018 O O   . GLY B 115 ? 0.3653 0.9013 0.6451 0.0097  0.0495  0.0319  113 GLY B O   
4019 N N   . ASN B 116 ? 0.3413 0.8504 0.6326 0.0358  0.0439  0.0496  114 ASN B N   
4020 C CA  . ASN B 116 ? 0.3362 0.8517 0.6183 0.0326  0.0428  0.0669  114 ASN B CA  
4021 C C   . ASN B 116 ? 0.3748 0.9068 0.6539 0.0333  0.0356  0.0848  114 ASN B C   
4022 O O   . ASN B 116 ? 0.3820 0.9185 0.6552 0.0339  0.0328  0.1031  114 ASN B O   
4023 C CB  . ASN B 116 ? 0.3411 0.8357 0.6283 0.0437  0.0454  0.0738  114 ASN B CB  
4024 C CG  . ASN B 116 ? 0.3533 0.8390 0.6416 0.0389  0.0523  0.0588  114 ASN B CG  
4025 O OD1 . ASN B 116 ? 0.3562 0.8524 0.6386 0.0257  0.0562  0.0484  114 ASN B OD1 
4026 N ND2 . ASN B 116 ? 0.3333 0.8009 0.6298 0.0484  0.0545  0.0561  114 ASN B ND2 
4027 N N   . TYR B 117 ? 0.3330 0.8741 0.6172 0.0335  0.0328  0.0801  115 TYR B N   
4028 C CA  . TYR B 117 ? 0.4104 0.9729 0.6958 0.0330  0.0255  0.0941  115 TYR B CA  
4029 C C   . TYR B 117 ? 0.4004 0.9861 0.6779 0.0164  0.0251  0.0824  115 TYR B C   
4030 O O   . TYR B 117 ? 0.4518 1.0331 0.7344 0.0151  0.0293  0.0668  115 TYR B O   
4031 C CB  . TYR B 117 ? 0.3812 0.9338 0.6817 0.0472  0.0246  0.0983  115 TYR B CB  
4032 C CG  . TYR B 117 ? 0.3884 0.9173 0.6969 0.0620  0.0271  0.1081  115 TYR B CG  
4033 C CD1 . TYR B 117 ? 0.3371 0.8406 0.6452 0.0665  0.0329  0.0969  115 TYR B CD1 
4034 C CD2 . TYR B 117 ? 0.3497 0.8826 0.6677 0.0711  0.0241  0.1279  115 TYR B CD2 
4035 C CE1 . TYR B 117 ? 0.3198 0.8026 0.6336 0.0772  0.0365  0.1037  115 TYR B CE1 
4036 C CE2 . TYR B 117 ? 0.3305 0.8398 0.6562 0.0831  0.0293  0.1351  115 TYR B CE2 
4037 C CZ  . TYR B 117 ? 0.4329 0.9170 0.7549 0.0849  0.0359  0.1222  115 TYR B CZ  
4038 O OH  . TYR B 117 ? 0.4001 0.8614 0.7281 0.0942  0.0424  0.1270  115 TYR B OH  
4039 N N   . PRO B 118 ? 0.4304 1.0398 0.6938 0.0024  0.0210  0.0890  116 PRO B N   
4040 C CA  . PRO B 118 ? 0.3621 0.9949 0.6162 -0.0166 0.0220  0.0758  116 PRO B CA  
4041 C C   . PRO B 118 ? 0.3885 1.0457 0.6494 -0.0179 0.0149  0.0809  116 PRO B C   
4042 O O   . PRO B 118 ? 0.5078 1.1811 0.7640 -0.0332 0.0183  0.0658  116 PRO B O   
4043 C CB  . PRO B 118 ? 0.4254 1.0731 0.6579 -0.0325 0.0201  0.0821  116 PRO B CB  
4044 C CG  . PRO B 118 ? 0.4231 1.0656 0.6557 -0.0194 0.0124  0.1079  116 PRO B CG  
4045 C CD  . PRO B 118 ? 0.3725 0.9858 0.6246 0.0015  0.0164  0.1083  116 PRO B CD  
4046 N N   . TYR B 119 ? 0.3602 1.0209 0.6338 -0.0031 0.0067  0.0998  117 TYR B N   
4047 C CA  . TYR B 119 ? 0.3864 1.0742 0.6710 -0.0037 -0.0005 0.1051  117 TYR B CA  
4048 C C   . TYR B 119 ? 0.4226 1.0911 0.7265 0.0102  0.0052  0.0988  117 TYR B C   
4049 O O   . TYR B 119 ? 0.4309 1.0742 0.7443 0.0269  0.0072  0.1067  117 TYR B O   
4050 C CB  . TYR B 119 ? 0.4132 1.1234 0.7012 0.0025  -0.0144 0.1320  117 TYR B CB  
4051 C CG  . TYR B 119 ? 0.4414 1.1626 0.7051 -0.0099 -0.0197 0.1415  117 TYR B CG  
4052 C CD1 . TYR B 119 ? 0.4319 1.1752 0.6750 -0.0337 -0.0194 0.1288  117 TYR B CD1 
4053 C CD2 . TYR B 119 ? 0.4731 1.1802 0.7326 0.0005  -0.0230 0.1622  117 TYR B CD2 
4054 C CE1 . TYR B 119 ? 0.4934 1.2450 0.7103 -0.0475 -0.0229 0.1367  117 TYR B CE1 
4055 C CE2 . TYR B 119 ? 0.4801 1.1937 0.7135 -0.0122 -0.0265 0.1712  117 TYR B CE2 
4056 C CZ  . TYR B 119 ? 0.4862 1.2223 0.6974 -0.0365 -0.0268 0.1585  117 TYR B CZ  
4057 O OH  . TYR B 119 ? 0.5621 1.3032 0.7436 -0.0515 -0.0291 0.1667  117 TYR B OH  
4058 N N   . TRP B 120 ? 0.3672 1.0465 0.6749 0.0015  0.0091  0.0840  118 TRP B N   
4059 C CA  . TRP B 120 ? 0.3741 1.0312 0.6940 0.0106  0.0172  0.0746  118 TRP B CA  
4060 C C   . TRP B 120 ? 0.5163 1.2008 0.8492 0.0057  0.0150  0.0734  118 TRP B C   
4061 O O   . TRP B 120 ? 0.5770 1.2992 0.9078 -0.0081 0.0080  0.0743  118 TRP B O   
4062 C CB  . TRP B 120 ? 0.3936 1.0248 0.7034 0.0046  0.0291  0.0527  118 TRP B CB  
4063 C CG  . TRP B 120 ? 0.4589 1.0599 0.7633 0.0136  0.0319  0.0522  118 TRP B CG  
4064 C CD1 . TRP B 120 ? 0.4254 1.0260 0.7191 0.0056  0.0335  0.0465  118 TRP B CD1 
4065 C CD2 . TRP B 120 ? 0.4837 1.0524 0.7938 0.0306  0.0341  0.0558  118 TRP B CD2 
4066 N NE1 . TRP B 120 ? 0.4616 1.0337 0.7567 0.0175  0.0359  0.0462  118 TRP B NE1 
4067 C CE2 . TRP B 120 ? 0.4212 0.9737 0.7251 0.0326  0.0356  0.0522  118 TRP B CE2 
4068 C CE3 . TRP B 120 ? 0.5061 1.0587 0.8256 0.0428  0.0357  0.0605  118 TRP B CE3 
4069 C CZ2 . TRP B 120 ? 0.3969 0.9204 0.7035 0.0463  0.0370  0.0534  118 TRP B CZ2 
4070 C CZ3 . TRP B 120 ? 0.4385 0.9597 0.7577 0.0555  0.0379  0.0620  118 TRP B CZ3 
4071 C CH2 . TRP B 120 ? 0.3990 0.9071 0.7118 0.0572  0.0378  0.0586  118 TRP B CH2 
4072 N N   . GLY B 121 ? 0.5370 1.2031 0.8832 0.0160  0.0213  0.0704  119 GLY B N   
4073 C CA  . GLY B 121 ? 0.5371 1.2230 0.8964 0.0100  0.0238  0.0634  119 GLY B CA  
4074 C C   . GLY B 121 ? 0.5976 1.2644 0.9462 -0.0010 0.0377  0.0403  119 GLY B C   
4075 O O   . GLY B 121 ? 0.6129 1.2502 0.9465 -0.0015 0.0445  0.0310  119 GLY B O   
4076 N N   . GLN B 122 ? 0.5842 1.2685 0.9427 -0.0097 0.0424  0.0310  120 GLN B N   
4077 C CA  . GLN B 122 ? 0.6392 1.3044 0.9872 -0.0215 0.0575  0.0092  120 GLN B CA  
4078 C C   . GLN B 122 ? 0.5996 1.2143 0.9427 -0.0090 0.0684  0.0056  120 GLN B C   
4079 O O   . GLN B 122 ? 0.5928 1.1791 0.9219 -0.0144 0.0801  -0.0089 120 GLN B O   
4080 C CB  . GLN B 122 ? 0.6885 1.3882 1.0481 -0.0366 0.0607  -0.0010 120 GLN B CB  
4081 C CG  . GLN B 122 ? 0.7726 1.4621 1.1484 -0.0295 0.0681  -0.0024 120 GLN B CG  
4082 C CD  . GLN B 122 ? 0.7812 1.5027 1.1839 -0.0185 0.0553  0.0153  120 GLN B CD  
4083 O OE1 . GLN B 122 ? 0.7220 1.4713 1.1293 -0.0147 0.0397  0.0311  120 GLN B OE1 
4084 N NE2 . GLN B 122 ? 0.6863 1.4026 1.1071 -0.0133 0.0629  0.0129  120 GLN B NE2 
4085 N N   . GLY B 123 ? 0.6037 1.2057 0.9571 0.0072  0.0652  0.0187  121 GLY B N   
4086 C CA  . GLY B 123 ? 0.5449 1.1009 0.8906 0.0170  0.0749  0.0157  121 GLY B CA  
4087 C C   . GLY B 123 ? 0.6199 1.1716 0.9732 0.0127  0.0861  0.0075  121 GLY B C   
4088 O O   . GLY B 123 ? 0.6528 1.2212 1.0072 -0.0023 0.0929  -0.0058 121 GLY B O   
4089 N N   . THR B 124 ? 0.5255 1.0548 0.8838 0.0240  0.0898  0.0136  122 THR B N   
4090 C CA  . THR B 124 ? 0.5532 1.0720 0.9168 0.0197  0.1030  0.0048  122 THR B CA  
4091 C C   . THR B 124 ? 0.5021 0.9649 0.8408 0.0244  0.1135  0.0006  122 THR B C   
4092 O O   . THR B 124 ? 0.5142 0.9528 0.8430 0.0363  0.1083  0.0097  122 THR B O   
4093 C CB  . THR B 124 ? 0.4935 1.0367 0.8870 0.0269  0.1005  0.0143  122 THR B CB  
4094 O OG1 . THR B 124 ? 0.5739 1.0997 0.9708 0.0226  0.1162  0.0040  122 THR B OG1 
4095 C CG2 . THR B 124 ? 0.5204 1.0490 0.9165 0.0436  0.0932  0.0306  122 THR B CG2 
4096 N N   . GLN B 125 ? 0.5349 0.9773 0.8622 0.0142  0.1284  -0.0131 123 GLN B N   
4097 C CA  . GLN B 125 ? 0.5064 0.8936 0.8051 0.0171  0.1380  -0.0163 123 GLN B CA  
4098 C C   . GLN B 125 ? 0.5578 0.9260 0.8587 0.0230  0.1442  -0.0119 123 GLN B C   
4099 O O   . GLN B 125 ? 0.6480 1.0380 0.9713 0.0186  0.1508  -0.0150 123 GLN B O   
4100 C CB  . GLN B 125 ? 0.5526 0.9204 0.8348 0.0030  0.1534  -0.0321 123 GLN B CB  
4101 C CG  . GLN B 125 ? 0.5845 0.8931 0.8346 0.0051  0.1643  -0.0341 123 GLN B CG  
4102 C CD  . GLN B 125 ? 0.6011 0.8802 0.8313 0.0182  0.1534  -0.0248 123 GLN B CD  
4103 O OE1 . GLN B 125 ? 0.6204 0.9166 0.8566 0.0214  0.1433  -0.0231 123 GLN B OE1 
4104 N NE2 . GLN B 125 ? 0.6704 0.9064 0.8771 0.0249  0.1555  -0.0197 123 GLN B NE2 
4105 N N   . VAL B 126 ? 0.5731 0.9018 0.8519 0.0323  0.1423  -0.0055 124 VAL B N   
4106 C CA  . VAL B 126 ? 0.5479 0.8498 0.8204 0.0354  0.1505  -0.0033 124 VAL B CA  
4107 C C   . VAL B 126 ? 0.6042 0.8519 0.8363 0.0336  0.1573  -0.0068 124 VAL B C   
4108 O O   . VAL B 126 ? 0.6811 0.9099 0.8946 0.0412  0.1470  -0.0012 124 VAL B O   
4109 C CB  . VAL B 126 ? 0.5459 0.8549 0.8302 0.0482  0.1402  0.0096  124 VAL B CB  
4110 C CG1 . VAL B 126 ? 0.5868 0.8566 0.8530 0.0498  0.1492  0.0101  124 VAL B CG1 
4111 C CG2 . VAL B 126 ? 0.5476 0.9041 0.8720 0.0507  0.1364  0.0149  124 VAL B CG2 
4112 N N   . THR B 127 ? 0.6556 0.8786 0.8744 0.0234  0.1744  -0.0157 125 THR B N   
4113 C CA  . THR B 127 ? 0.7382 0.9063 0.9147 0.0204  0.1819  -0.0177 125 THR B CA  
4114 C C   . THR B 127 ? 0.7409 0.8814 0.9039 0.0175  0.1926  -0.0177 125 THR B C   
4115 O O   . THR B 127 ? 0.7486 0.8968 0.9255 0.0077  0.2083  -0.0265 125 THR B O   
4116 C CB  . THR B 127 ? 0.7260 0.8808 0.8903 0.0074  0.1961  -0.0298 125 THR B CB  
4117 O OG1 . THR B 127 ? 0.7221 0.9107 0.9052 0.0068  0.1890  -0.0327 125 THR B OG1 
4118 C CG2 . THR B 127 ? 0.7413 0.8372 0.8597 0.0074  0.2003  -0.0278 125 THR B CG2 
4119 N N   . VAL B 128 ? 0.7200 0.8302 0.8570 0.0250  0.1848  -0.0091 126 VAL B N   
4120 C CA  . VAL B 128 ? 0.8286 0.9094 0.9470 0.0207  0.1947  -0.0094 126 VAL B CA  
4121 C C   . VAL B 128 ? 0.9060 0.9323 0.9750 0.0125  0.2037  -0.0117 126 VAL B C   
4122 O O   . VAL B 128 ? 0.9296 0.9293 0.9687 0.0195  0.1913  -0.0036 126 VAL B O   
4123 C CB  . VAL B 128 ? 0.8331 0.9155 0.9516 0.0316  0.1812  0.0006  126 VAL B CB  
4124 C CG1 . VAL B 128 ? 0.8104 0.8612 0.9071 0.0242  0.1935  -0.0017 126 VAL B CG1 
4125 C CG2 . VAL B 128 ? 0.7403 0.8726 0.9053 0.0398  0.1733  0.0045  126 VAL B CG2 
4126 N N   . SER B 129 ? 0.9089 0.9185 0.9697 -0.0022 0.2252  -0.0225 127 SER B N   
4127 C CA  . SER B 129 ? 0.8865 0.8407 0.8973 -0.0123 0.2369  -0.0248 127 SER B CA  
4128 C C   . SER B 129 ? 0.9911 0.9051 0.9605 -0.0108 0.2317  -0.0162 127 SER B C   
4129 O O   . SER B 129 ? 0.9771 0.8900 0.9488 -0.0163 0.2399  -0.0193 127 SER B O   
4130 C CB  . SER B 129 ? 0.8878 0.8350 0.9013 -0.0305 0.2637  -0.0401 127 SER B CB  
4131 O OG  . SER B 129 ? 0.9333 0.8783 0.9519 -0.0369 0.2752  -0.0446 127 SER B OG  
# 
