data_9H8C
# 
_entry.id   9H8C 
# 
_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   9H8C         pdb_00009h8c 10.2210/pdb9h8c/pdb 
WWPDB D_1292142816 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2025-01-22 
2 'Structure model' 1 1 2025-02-05 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9H8C 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-29 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              don.o.somers@gsk.com 
_pdbx_contact_author.name_first         DON 
_pdbx_contact_author.name_last          SOMERS 
_pdbx_contact_author.name_mi            O 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7815-485X 
# 
_audit_author.name               'Somers, D.O.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0001-7815-485X 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            68 
_citation.language                  ? 
_citation.page_first                1883 
_citation.page_last                 1900 
_citation.title                     
;Phenotype-Led Identification of IL-10 Upregulators in Human CD4 + T-cells and Elucidation of Their Pharmacology as Highly Selective CDK8/CDK19 Inhibitors.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c02630 
_citation.pdbx_database_id_PubMed   39780505 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Nicolle, S.'     1  ? 
primary 'Barker, M.'      2  ? 
primary 'Barrett, J.'     3  ? 
primary 'Campbell, M.'    4  ? 
primary 'Wojno-Picon, J.' 5  ? 
primary 'Atkinson, S.J.'  6  ? 
primary 'Aylott, H.'      7  ? 
primary 'Kessedjian, H.'  8  ? 
primary 'He, Y.'          9  ? 
primary 'Messenger, C.'   10 ? 
primary 'Roberts, E.'     11 ? 
primary 'Spitzfaden, C.'  12 ? 
primary 'Le, J.'          13 ? 
primary 'Zinn, N.'        14 ? 
primary 'Werner, T.'      15 ? 
primary 'Dumpelfeld, B.'  16 ? 
primary 'Bantscheff, M.'  17 ? 
primary 'Somers, D.O.'    18 ? 
primary 'Reid, H.'        19 ? 
primary 'Thang, K.'       20 ? 
primary 'Gobbetti, T.'    21 ? 
primary 'Lewis, H.D.'     22 ? 
# 
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 'Cyclin-dependent kinase 8' 48028.863 1   2.7.11.22,2.7.11.23 ? ? ? 
2 polymer     man Cyclin-C 36491.113 1   ?                   ? ? ? 
3 non-polymer syn 1,2-ETHANEDIOL 62.068    1   ?                   ? ? ? 
4 non-polymer nat GLYCEROL 92.094    2   ?                   ? ? ? 
5 non-polymer syn 
'4-[(3~{S})-3-[2-[(3~{R})-3-fluoranylpyrrolidin-1-yl]pyrimidin-4-yl]piperidin-1-yl]carbonyl-1~{H}-pyrrole-2-carbonitrile' 368.408 
1   ?                   ? ? ? 
6 non-polymer syn 'DIMETHYL SULFOXIDE' 78.133    2   ?                   ? ? ? 
7 water       nat water 18.015    275 ?                   ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 
;Cell division protein kinase 8,Mediator complex subunit CDK8,Mediator of RNA polymerase II transcription subunit CDK8,Protein kinase K35
;
2 'SRB11 homolog,hSRB11' 
# 
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 
;GPMDYKDDDDKMDYDFKVKLSSERERVEDLFEYEGCKVGRGTYGHVYKAKRKDGKDDKDYALKQIEGTGISMSACREIAL
LRELKHPNVISLQKVFLSHADRKVWLLFDYAEHDLWHIIKFHRASKANKKPVQLPRGMVKSLLYQILDGIHYLHANWVLH
RDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLT
SEPIFHCRQEDIKTSNPYHHDQLDRIFNVMGFPADKDWEDIKKMPEHSTLMKDFRRNTYTNCSLIKYMEKHKVKPDSKAF
HLLQKLLTMDPIKRITSEQAMQDPYFLEDPLPTSDVFAGCQIPYPKREFLTEEEPDDKGDKKNQQQQQGNNHTNGTGHPG
NQDSSHTQGPPLKK
;
;GPMDYKDDDDKMDYDFKVKLSSERERVEDLFEYEGCKVGRGTYGHVYKAKRKDGKDDKDYALKQIEGTGISMSACREIAL
LRELKHPNVISLQKVFLSHADRKVWLLFDYAEHDLWHIIKFHRASKANKKPVQLPRGMVKSLLYQILDGIHYLHANWVLH
RDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLT
SEPIFHCRQEDIKTSNPYHHDQLDRIFNVMGFPADKDWEDIKKMPEHSTLMKDFRRNTYTNCSLIKYMEKHKVKPDSKAF
HLLQKLLTMDPIKRITSEQAMQDPYFLEDPLPTSDVFAGCQIPYPKREFLTEEEPDDKGDKKNQQQQQGNNHTNGTGHPG
NQDSSHTQGPPLKK
;
A ? 
2 'polypeptide(L)' no no 
;GSGMKETAAAKFERQHMDSPDLGTDDDDKAMAGNFWQSSHYLQWILDKQDLLKERQKDLKFLSEEEYWKLQIFFTNVIQA
LGEHLKLRQQVIATATVYFKRFYARYSLKSIDPVLMAPTCVFLASKVEEFGVVSNTRLIAAATSVLKTRFSYAFPKEFPY
RMNHILECEFYLLELMDCCLIVYHPYRPLLQYVQDMGQEDMLLPLAWRIVNDTYRTDLCLLYPPFMIALACLHVACVVQQ
KDARQWFAELSVDMEKILEIIRVILKLYEQWKNFDERKEMATILSKMPKPKPPPNSEGEQGPNGSQNSSYSQS
;
;GSGMKETAAAKFERQHMDSPDLGTDDDDKAMAGNFWQSSHYLQWILDKQDLLKERQKDLKFLSEEEYWKLQIFFTNVIQA
LGEHLKLRQQVIATATVYFKRFYARYSLKSIDPVLMAPTCVFLASKVEEFGVVSNTRLIAAATSVLKTRFSYAFPKEFPY
RMNHILECEFYLLELMDCCLIVYHPYRPLLQYVQDMGQEDMLLPLAWRIVNDTYRTDLCLLYPPFMIALACLHVACVVQQ
KDARQWFAELSVDMEKILEIIRVILKLYEQWKNFDERKEMATILSKMPKPKPPPNSEGEQGPNGSQNSSYSQS
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 1,2-ETHANEDIOL                                                                                                            EDO   
4 GLYCEROL                                                                                                                  GOL   
5 '4-[(3~{S})-3-[2-[(3~{R})-3-fluoranylpyrrolidin-1-yl]pyrimidin-4-yl]piperidin-1-yl]carbonyl-1~{H}-pyrrole-2-carbonitrile' A1IS8 
6 'DIMETHYL SULFOXIDE'                                                                                                      DMS   
7 water                                                                                                                     HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   MET n 
1 4   ASP n 
1 5   TYR n 
1 6   LYS n 
1 7   ASP n 
1 8   ASP n 
1 9   ASP n 
1 10  ASP n 
1 11  LYS n 
1 12  MET n 
1 13  ASP n 
1 14  TYR n 
1 15  ASP n 
1 16  PHE n 
1 17  LYS n 
1 18  VAL n 
1 19  LYS n 
1 20  LEU n 
1 21  SER n 
1 22  SER n 
1 23  GLU n 
1 24  ARG n 
1 25  GLU n 
1 26  ARG n 
1 27  VAL n 
1 28  GLU n 
1 29  ASP n 
1 30  LEU n 
1 31  PHE n 
1 32  GLU n 
1 33  TYR n 
1 34  GLU n 
1 35  GLY n 
1 36  CYS n 
1 37  LYS n 
1 38  VAL n 
1 39  GLY n 
1 40  ARG n 
1 41  GLY n 
1 42  THR n 
1 43  TYR n 
1 44  GLY n 
1 45  HIS n 
1 46  VAL n 
1 47  TYR n 
1 48  LYS n 
1 49  ALA n 
1 50  LYS n 
1 51  ARG n 
1 52  LYS n 
1 53  ASP n 
1 54  GLY n 
1 55  LYS n 
1 56  ASP n 
1 57  ASP n 
1 58  LYS n 
1 59  ASP n 
1 60  TYR n 
1 61  ALA n 
1 62  LEU n 
1 63  LYS n 
1 64  GLN n 
1 65  ILE n 
1 66  GLU n 
1 67  GLY n 
1 68  THR n 
1 69  GLY n 
1 70  ILE n 
1 71  SER n 
1 72  MET n 
1 73  SER n 
1 74  ALA n 
1 75  CYS n 
1 76  ARG n 
1 77  GLU n 
1 78  ILE n 
1 79  ALA n 
1 80  LEU n 
1 81  LEU n 
1 82  ARG n 
1 83  GLU n 
1 84  LEU n 
1 85  LYS n 
1 86  HIS n 
1 87  PRO n 
1 88  ASN n 
1 89  VAL n 
1 90  ILE n 
1 91  SER n 
1 92  LEU n 
1 93  GLN n 
1 94  LYS n 
1 95  VAL n 
1 96  PHE n 
1 97  LEU n 
1 98  SER n 
1 99  HIS n 
1 100 ALA n 
1 101 ASP n 
1 102 ARG n 
1 103 LYS n 
1 104 VAL n 
1 105 TRP n 
1 106 LEU n 
1 107 LEU n 
1 108 PHE n 
1 109 ASP n 
1 110 TYR n 
1 111 ALA n 
1 112 GLU n 
1 113 HIS n 
1 114 ASP n 
1 115 LEU n 
1 116 TRP n 
1 117 HIS n 
1 118 ILE n 
1 119 ILE n 
1 120 LYS n 
1 121 PHE n 
1 122 HIS n 
1 123 ARG n 
1 124 ALA n 
1 125 SER n 
1 126 LYS n 
1 127 ALA n 
1 128 ASN n 
1 129 LYS n 
1 130 LYS n 
1 131 PRO n 
1 132 VAL n 
1 133 GLN n 
1 134 LEU n 
1 135 PRO n 
1 136 ARG n 
1 137 GLY n 
1 138 MET n 
1 139 VAL n 
1 140 LYS n 
1 141 SER n 
1 142 LEU n 
1 143 LEU n 
1 144 TYR n 
1 145 GLN n 
1 146 ILE n 
1 147 LEU n 
1 148 ASP n 
1 149 GLY n 
1 150 ILE n 
1 151 HIS n 
1 152 TYR n 
1 153 LEU n 
1 154 HIS n 
1 155 ALA n 
1 156 ASN n 
1 157 TRP n 
1 158 VAL n 
1 159 LEU n 
1 160 HIS n 
1 161 ARG n 
1 162 ASP n 
1 163 LEU n 
1 164 LYS n 
1 165 PRO n 
1 166 ALA n 
1 167 ASN n 
1 168 ILE n 
1 169 LEU n 
1 170 VAL n 
1 171 MET n 
1 172 GLY n 
1 173 GLU n 
1 174 GLY n 
1 175 PRO n 
1 176 GLU n 
1 177 ARG n 
1 178 GLY n 
1 179 ARG n 
1 180 VAL n 
1 181 LYS n 
1 182 ILE n 
1 183 ALA n 
1 184 ASP n 
1 185 MET n 
1 186 GLY n 
1 187 PHE n 
1 188 ALA n 
1 189 ARG n 
1 190 LEU n 
1 191 PHE n 
1 192 ASN n 
1 193 SER n 
1 194 PRO n 
1 195 LEU n 
1 196 LYS n 
1 197 PRO n 
1 198 LEU n 
1 199 ALA n 
1 200 ASP n 
1 201 LEU n 
1 202 ASP n 
1 203 PRO n 
1 204 VAL n 
1 205 VAL n 
1 206 VAL n 
1 207 THR n 
1 208 PHE n 
1 209 TRP n 
1 210 TYR n 
1 211 ARG n 
1 212 ALA n 
1 213 PRO n 
1 214 GLU n 
1 215 LEU n 
1 216 LEU n 
1 217 LEU n 
1 218 GLY n 
1 219 ALA n 
1 220 ARG n 
1 221 HIS n 
1 222 TYR n 
1 223 THR n 
1 224 LYS n 
1 225 ALA n 
1 226 ILE n 
1 227 ASP n 
1 228 ILE n 
1 229 TRP n 
1 230 ALA n 
1 231 ILE n 
1 232 GLY n 
1 233 CYS n 
1 234 ILE n 
1 235 PHE n 
1 236 ALA n 
1 237 GLU n 
1 238 LEU n 
1 239 LEU n 
1 240 THR n 
1 241 SER n 
1 242 GLU n 
1 243 PRO n 
1 244 ILE n 
1 245 PHE n 
1 246 HIS n 
1 247 CYS n 
1 248 ARG n 
1 249 GLN n 
1 250 GLU n 
1 251 ASP n 
1 252 ILE n 
1 253 LYS n 
1 254 THR n 
1 255 SER n 
1 256 ASN n 
1 257 PRO n 
1 258 TYR n 
1 259 HIS n 
1 260 HIS n 
1 261 ASP n 
1 262 GLN n 
1 263 LEU n 
1 264 ASP n 
1 265 ARG n 
1 266 ILE n 
1 267 PHE n 
1 268 ASN n 
1 269 VAL n 
1 270 MET n 
1 271 GLY n 
1 272 PHE n 
1 273 PRO n 
1 274 ALA n 
1 275 ASP n 
1 276 LYS n 
1 277 ASP n 
1 278 TRP n 
1 279 GLU n 
1 280 ASP n 
1 281 ILE n 
1 282 LYS n 
1 283 LYS n 
1 284 MET n 
1 285 PRO n 
1 286 GLU n 
1 287 HIS n 
1 288 SER n 
1 289 THR n 
1 290 LEU n 
1 291 MET n 
1 292 LYS n 
1 293 ASP n 
1 294 PHE n 
1 295 ARG n 
1 296 ARG n 
1 297 ASN n 
1 298 THR n 
1 299 TYR n 
1 300 THR n 
1 301 ASN n 
1 302 CYS n 
1 303 SER n 
1 304 LEU n 
1 305 ILE n 
1 306 LYS n 
1 307 TYR n 
1 308 MET n 
1 309 GLU n 
1 310 LYS n 
1 311 HIS n 
1 312 LYS n 
1 313 VAL n 
1 314 LYS n 
1 315 PRO n 
1 316 ASP n 
1 317 SER n 
1 318 LYS n 
1 319 ALA n 
1 320 PHE n 
1 321 HIS n 
1 322 LEU n 
1 323 LEU n 
1 324 GLN n 
1 325 LYS n 
1 326 LEU n 
1 327 LEU n 
1 328 THR n 
1 329 MET n 
1 330 ASP n 
1 331 PRO n 
1 332 ILE n 
1 333 LYS n 
1 334 ARG n 
1 335 ILE n 
1 336 THR n 
1 337 SER n 
1 338 GLU n 
1 339 GLN n 
1 340 ALA n 
1 341 MET n 
1 342 GLN n 
1 343 ASP n 
1 344 PRO n 
1 345 TYR n 
1 346 PHE n 
1 347 LEU n 
1 348 GLU n 
1 349 ASP n 
1 350 PRO n 
1 351 LEU n 
1 352 PRO n 
1 353 THR n 
1 354 SER n 
1 355 ASP n 
1 356 VAL n 
1 357 PHE n 
1 358 ALA n 
1 359 GLY n 
1 360 CYS n 
1 361 GLN n 
1 362 ILE n 
1 363 PRO n 
1 364 TYR n 
1 365 PRO n 
1 366 LYS n 
1 367 ARG n 
1 368 GLU n 
1 369 PHE n 
1 370 LEU n 
1 371 THR n 
1 372 GLU n 
1 373 GLU n 
1 374 GLU n 
1 375 PRO n 
1 376 ASP n 
1 377 ASP n 
1 378 LYS n 
1 379 GLY n 
1 380 ASP n 
1 381 LYS n 
1 382 LYS n 
1 383 ASN n 
1 384 GLN n 
1 385 GLN n 
1 386 GLN n 
1 387 GLN n 
1 388 GLN n 
1 389 GLY n 
1 390 ASN n 
1 391 ASN n 
1 392 HIS n 
1 393 THR n 
1 394 ASN n 
1 395 GLY n 
1 396 THR n 
1 397 GLY n 
1 398 HIS n 
1 399 PRO n 
1 400 GLY n 
1 401 ASN n 
1 402 GLN n 
1 403 ASP n 
1 404 SER n 
1 405 SER n 
1 406 HIS n 
1 407 THR n 
1 408 GLN n 
1 409 GLY n 
1 410 PRO n 
1 411 PRO n 
1 412 LEU n 
1 413 LYS n 
1 414 LYS n 
2 1   GLY n 
2 2   SER n 
2 3   GLY n 
2 4   MET n 
2 5   LYS n 
2 6   GLU n 
2 7   THR n 
2 8   ALA n 
2 9   ALA n 
2 10  ALA n 
2 11  LYS n 
2 12  PHE n 
2 13  GLU n 
2 14  ARG n 
2 15  GLN n 
2 16  HIS n 
2 17  MET n 
2 18  ASP n 
2 19  SER n 
2 20  PRO n 
2 21  ASP n 
2 22  LEU n 
2 23  GLY n 
2 24  THR n 
2 25  ASP n 
2 26  ASP n 
2 27  ASP n 
2 28  ASP n 
2 29  LYS n 
2 30  ALA n 
2 31  MET n 
2 32  ALA n 
2 33  GLY n 
2 34  ASN n 
2 35  PHE n 
2 36  TRP n 
2 37  GLN n 
2 38  SER n 
2 39  SER n 
2 40  HIS n 
2 41  TYR n 
2 42  LEU n 
2 43  GLN n 
2 44  TRP n 
2 45  ILE n 
2 46  LEU n 
2 47  ASP n 
2 48  LYS n 
2 49  GLN n 
2 50  ASP n 
2 51  LEU n 
2 52  LEU n 
2 53  LYS n 
2 54  GLU n 
2 55  ARG n 
2 56  GLN n 
2 57  LYS n 
2 58  ASP n 
2 59  LEU n 
2 60  LYS n 
2 61  PHE n 
2 62  LEU n 
2 63  SER n 
2 64  GLU n 
2 65  GLU n 
2 66  GLU n 
2 67  TYR n 
2 68  TRP n 
2 69  LYS n 
2 70  LEU n 
2 71  GLN n 
2 72  ILE n 
2 73  PHE n 
2 74  PHE n 
2 75  THR n 
2 76  ASN n 
2 77  VAL n 
2 78  ILE n 
2 79  GLN n 
2 80  ALA n 
2 81  LEU n 
2 82  GLY n 
2 83  GLU n 
2 84  HIS n 
2 85  LEU n 
2 86  LYS n 
2 87  LEU n 
2 88  ARG n 
2 89  GLN n 
2 90  GLN n 
2 91  VAL n 
2 92  ILE n 
2 93  ALA n 
2 94  THR n 
2 95  ALA n 
2 96  THR n 
2 97  VAL n 
2 98  TYR n 
2 99  PHE n 
2 100 LYS n 
2 101 ARG n 
2 102 PHE n 
2 103 TYR n 
2 104 ALA n 
2 105 ARG n 
2 106 TYR n 
2 107 SER n 
2 108 LEU n 
2 109 LYS n 
2 110 SER n 
2 111 ILE n 
2 112 ASP n 
2 113 PRO n 
2 114 VAL n 
2 115 LEU n 
2 116 MET n 
2 117 ALA n 
2 118 PRO n 
2 119 THR n 
2 120 CYS n 
2 121 VAL n 
2 122 PHE n 
2 123 LEU n 
2 124 ALA n 
2 125 SER n 
2 126 LYS n 
2 127 VAL n 
2 128 GLU n 
2 129 GLU n 
2 130 PHE n 
2 131 GLY n 
2 132 VAL n 
2 133 VAL n 
2 134 SER n 
2 135 ASN n 
2 136 THR n 
2 137 ARG n 
2 138 LEU n 
2 139 ILE n 
2 140 ALA n 
2 141 ALA n 
2 142 ALA n 
2 143 THR n 
2 144 SER n 
2 145 VAL n 
2 146 LEU n 
2 147 LYS n 
2 148 THR n 
2 149 ARG n 
2 150 PHE n 
2 151 SER n 
2 152 TYR n 
2 153 ALA n 
2 154 PHE n 
2 155 PRO n 
2 156 LYS n 
2 157 GLU n 
2 158 PHE n 
2 159 PRO n 
2 160 TYR n 
2 161 ARG n 
2 162 MET n 
2 163 ASN n 
2 164 HIS n 
2 165 ILE n 
2 166 LEU n 
2 167 GLU n 
2 168 CYS n 
2 169 GLU n 
2 170 PHE n 
2 171 TYR n 
2 172 LEU n 
2 173 LEU n 
2 174 GLU n 
2 175 LEU n 
2 176 MET n 
2 177 ASP n 
2 178 CYS n 
2 179 CYS n 
2 180 LEU n 
2 181 ILE n 
2 182 VAL n 
2 183 TYR n 
2 184 HIS n 
2 185 PRO n 
2 186 TYR n 
2 187 ARG n 
2 188 PRO n 
2 189 LEU n 
2 190 LEU n 
2 191 GLN n 
2 192 TYR n 
2 193 VAL n 
2 194 GLN n 
2 195 ASP n 
2 196 MET n 
2 197 GLY n 
2 198 GLN n 
2 199 GLU n 
2 200 ASP n 
2 201 MET n 
2 202 LEU n 
2 203 LEU n 
2 204 PRO n 
2 205 LEU n 
2 206 ALA n 
2 207 TRP n 
2 208 ARG n 
2 209 ILE n 
2 210 VAL n 
2 211 ASN n 
2 212 ASP n 
2 213 THR n 
2 214 TYR n 
2 215 ARG n 
2 216 THR n 
2 217 ASP n 
2 218 LEU n 
2 219 CYS n 
2 220 LEU n 
2 221 LEU n 
2 222 TYR n 
2 223 PRO n 
2 224 PRO n 
2 225 PHE n 
2 226 MET n 
2 227 ILE n 
2 228 ALA n 
2 229 LEU n 
2 230 ALA n 
2 231 CYS n 
2 232 LEU n 
2 233 HIS n 
2 234 VAL n 
2 235 ALA n 
2 236 CYS n 
2 237 VAL n 
2 238 VAL n 
2 239 GLN n 
2 240 GLN n 
2 241 LYS n 
2 242 ASP n 
2 243 ALA n 
2 244 ARG n 
2 245 GLN n 
2 246 TRP n 
2 247 PHE n 
2 248 ALA n 
2 249 GLU n 
2 250 LEU n 
2 251 SER n 
2 252 VAL n 
2 253 ASP n 
2 254 MET n 
2 255 GLU n 
2 256 LYS n 
2 257 ILE n 
2 258 LEU n 
2 259 GLU n 
2 260 ILE n 
2 261 ILE n 
2 262 ARG n 
2 263 VAL n 
2 264 ILE n 
2 265 LEU n 
2 266 LYS n 
2 267 LEU n 
2 268 TYR n 
2 269 GLU n 
2 270 GLN n 
2 271 TRP n 
2 272 LYS n 
2 273 ASN n 
2 274 PHE n 
2 275 ASP n 
2 276 GLU n 
2 277 ARG n 
2 278 LYS n 
2 279 GLU n 
2 280 MET n 
2 281 ALA n 
2 282 THR n 
2 283 ILE n 
2 284 LEU n 
2 285 SER n 
2 286 LYS n 
2 287 MET n 
2 288 PRO n 
2 289 LYS n 
2 290 PRO n 
2 291 LYS n 
2 292 PRO n 
2 293 PRO n 
2 294 PRO n 
2 295 ASN n 
2 296 SER n 
2 297 GLU n 
2 298 GLY n 
2 299 GLU n 
2 300 GLN n 
2 301 GLY n 
2 302 PRO n 
2 303 ASN n 
2 304 GLY n 
2 305 SER n 
2 306 GLN n 
2 307 ASN n 
2 308 SER n 
2 309 SER n 
2 310 TYR n 
2 311 SER n 
2 312 GLN n 
2 313 SER 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' 1 414 human ? CDK8 ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Spodoptera frugiperda' 7108 ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 313 human ? CCNC ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Spodoptera frugiperda' 7108 ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1IS8 non-polymer         . 
'4-[(3~{S})-3-[2-[(3~{R})-3-fluoranylpyrrolidin-1-yl]pyrimidin-4-yl]piperidin-1-yl]carbonyl-1~{H}-pyrrole-2-carbonitrile' ? 
'C19 H21 F N6 O' 368.408 
ALA   'L-peptide linking' y ALANINE ?                               'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE ?                               'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE ?                               'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ?                               'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE ?                               'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE' ?                               'C2 H6 O S'      78.133  
EDO   non-polymer         . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL'               'C2 H6 O2'       62.068  
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  
GOL   non-polymer         . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS   'L-peptide linking' y HISTIDINE ?                               'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER ?                               'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE ?                               'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE ?                               'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE ?                               'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE ?                               'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE ?                               'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE ?                               'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE ?                               'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE ?                               'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ?                               'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE ?                               'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE ?                               'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -10 ?   ?   ?   A . n 
A 1 2   PRO 2   -9  ?   ?   ?   A . n 
A 1 3   MET 3   -8  ?   ?   ?   A . n 
A 1 4   ASP 4   -7  ?   ?   ?   A . n 
A 1 5   TYR 5   -6  ?   ?   ?   A . n 
A 1 6   LYS 6   -5  ?   ?   ?   A . n 
A 1 7   ASP 7   -4  ?   ?   ?   A . n 
A 1 8   ASP 8   -3  ?   ?   ?   A . n 
A 1 9   ASP 9   -2  ?   ?   ?   A . n 
A 1 10  ASP 10  -1  ?   ?   ?   A . n 
A 1 11  LYS 11  0   ?   ?   ?   A . n 
A 1 12  MET 12  1   1   MET MET A . n 
A 1 13  ASP 13  2   2   ASP ASP A . n 
A 1 14  TYR 14  3   3   TYR TYR A . n 
A 1 15  ASP 15  4   4   ASP ASP A . n 
A 1 16  PHE 16  5   5   PHE PHE A . n 
A 1 17  LYS 17  6   6   LYS LYS A . n 
A 1 18  VAL 18  7   7   VAL VAL A . n 
A 1 19  LYS 19  8   8   LYS LYS A . n 
A 1 20  LEU 20  9   9   LEU LEU A . n 
A 1 21  SER 21  10  10  SER SER A . n 
A 1 22  SER 22  11  11  SER SER A . n 
A 1 23  GLU 23  12  12  GLU GLU A . n 
A 1 24  ARG 24  13  13  ARG ARG A . n 
A 1 25  GLU 25  14  14  GLU GLU A . n 
A 1 26  ARG 26  15  15  ARG ARG A . n 
A 1 27  VAL 27  16  16  VAL VAL A . n 
A 1 28  GLU 28  17  17  GLU GLU A . n 
A 1 29  ASP 29  18  18  ASP ASP A . n 
A 1 30  LEU 30  19  19  LEU LEU A . n 
A 1 31  PHE 31  20  20  PHE PHE A . n 
A 1 32  GLU 32  21  21  GLU GLU A . n 
A 1 33  TYR 33  22  22  TYR TYR A . n 
A 1 34  GLU 34  23  23  GLU GLU A . n 
A 1 35  GLY 35  24  24  GLY GLY A . n 
A 1 36  CYS 36  25  25  CYS CYS A . n 
A 1 37  LYS 37  26  26  LYS LYS A . n 
A 1 38  VAL 38  27  27  VAL VAL A . n 
A 1 39  GLY 39  28  28  GLY GLY A . n 
A 1 40  ARG 40  29  29  ARG ARG A . n 
A 1 41  GLY 41  30  30  GLY GLY A . n 
A 1 42  THR 42  31  31  THR THR A . n 
A 1 43  TYR 43  32  32  TYR TYR A . n 
A 1 44  GLY 44  33  33  GLY GLY A . n 
A 1 45  HIS 45  34  34  HIS HIS A . n 
A 1 46  VAL 46  35  35  VAL VAL A . n 
A 1 47  TYR 47  36  36  TYR TYR A . n 
A 1 48  LYS 48  37  37  LYS LYS A . n 
A 1 49  ALA 49  38  38  ALA ALA A . n 
A 1 50  LYS 50  39  39  LYS LYS A . n 
A 1 51  ARG 51  40  40  ARG ARG A . n 
A 1 52  LYS 52  41  41  LYS LYS A . n 
A 1 53  ASP 53  42  42  ASP ASP A . n 
A 1 54  GLY 54  43  43  GLY GLY A . n 
A 1 55  LYS 55  44  44  LYS LYS A . n 
A 1 56  ASP 56  45  45  ASP ASP A . n 
A 1 57  ASP 57  46  46  ASP ASP A . n 
A 1 58  LYS 58  47  47  LYS LYS A . n 
A 1 59  ASP 59  48  48  ASP ASP A . n 
A 1 60  TYR 60  49  49  TYR TYR A . n 
A 1 61  ALA 61  50  50  ALA ALA A . n 
A 1 62  LEU 62  51  51  LEU LEU A . n 
A 1 63  LYS 63  52  52  LYS LYS A . n 
A 1 64  GLN 64  53  53  GLN GLN A . n 
A 1 65  ILE 65  54  54  ILE ILE A . n 
A 1 66  GLU 66  55  55  GLU GLU A . n 
A 1 67  GLY 67  56  56  GLY GLY A . n 
A 1 68  THR 68  57  57  THR THR A . n 
A 1 69  GLY 69  58  58  GLY GLY A . n 
A 1 70  ILE 70  59  59  ILE ILE A . n 
A 1 71  SER 71  60  60  SER SER A . n 
A 1 72  MET 72  61  61  MET MET A . n 
A 1 73  SER 73  62  62  SER SER A . n 
A 1 74  ALA 74  63  63  ALA ALA A . n 
A 1 75  CYS 75  64  64  CYS CYS A . n 
A 1 76  ARG 76  65  65  ARG ARG A . n 
A 1 77  GLU 77  66  66  GLU GLU A . n 
A 1 78  ILE 78  67  67  ILE ILE A . n 
A 1 79  ALA 79  68  68  ALA ALA A . n 
A 1 80  LEU 80  69  69  LEU LEU A . n 
A 1 81  LEU 81  70  70  LEU LEU A . n 
A 1 82  ARG 82  71  71  ARG ARG A . n 
A 1 83  GLU 83  72  72  GLU GLU A . n 
A 1 84  LEU 84  73  73  LEU LEU A . n 
A 1 85  LYS 85  74  74  LYS LYS A . n 
A 1 86  HIS 86  75  75  HIS HIS A . n 
A 1 87  PRO 87  76  76  PRO PRO A . n 
A 1 88  ASN 88  77  77  ASN ASN A . n 
A 1 89  VAL 89  78  78  VAL VAL A . n 
A 1 90  ILE 90  79  79  ILE ILE A . n 
A 1 91  SER 91  80  80  SER SER A . n 
A 1 92  LEU 92  81  81  LEU LEU A . n 
A 1 93  GLN 93  82  82  GLN GLN A . n 
A 1 94  LYS 94  83  83  LYS LYS A . n 
A 1 95  VAL 95  84  84  VAL VAL A . n 
A 1 96  PHE 96  85  85  PHE PHE A . n 
A 1 97  LEU 97  86  86  LEU LEU A . n 
A 1 98  SER 98  87  87  SER SER A . n 
A 1 99  HIS 99  88  88  HIS HIS A . n 
A 1 100 ALA 100 89  89  ALA ALA A . n 
A 1 101 ASP 101 90  90  ASP ASP A . n 
A 1 102 ARG 102 91  91  ARG ARG A . n 
A 1 103 LYS 103 92  92  LYS LYS A . n 
A 1 104 VAL 104 93  93  VAL VAL A . n 
A 1 105 TRP 105 94  94  TRP TRP A . n 
A 1 106 LEU 106 95  95  LEU LEU A . n 
A 1 107 LEU 107 96  96  LEU LEU A . n 
A 1 108 PHE 108 97  97  PHE PHE A . n 
A 1 109 ASP 109 98  98  ASP ASP A . n 
A 1 110 TYR 110 99  99  TYR TYR A . n 
A 1 111 ALA 111 100 100 ALA ALA A . n 
A 1 112 GLU 112 101 101 GLU GLU A . n 
A 1 113 HIS 113 102 102 HIS HIS A . n 
A 1 114 ASP 114 103 103 ASP ASP A . n 
A 1 115 LEU 115 104 104 LEU LEU A . n 
A 1 116 TRP 116 105 105 TRP TRP A . n 
A 1 117 HIS 117 106 106 HIS HIS A . n 
A 1 118 ILE 118 107 107 ILE ILE A . n 
A 1 119 ILE 119 108 108 ILE ILE A . n 
A 1 120 LYS 120 109 109 LYS LYS A . n 
A 1 121 PHE 121 110 110 PHE PHE A . n 
A 1 122 HIS 122 111 111 HIS HIS A . n 
A 1 123 ARG 123 112 112 ARG ARG A . n 
A 1 124 ALA 124 113 113 ALA ALA A . n 
A 1 125 SER 125 114 114 SER SER A . n 
A 1 126 LYS 126 115 115 LYS LYS A . n 
A 1 127 ALA 127 116 116 ALA ALA A . n 
A 1 128 ASN 128 117 117 ASN ASN A . n 
A 1 129 LYS 129 118 ?   ?   ?   A . n 
A 1 130 LYS 130 119 ?   ?   ?   A . n 
A 1 131 PRO 131 120 ?   ?   ?   A . n 
A 1 132 VAL 132 121 ?   ?   ?   A . n 
A 1 133 GLN 133 122 ?   ?   ?   A . n 
A 1 134 LEU 134 123 123 LEU LEU A . n 
A 1 135 PRO 135 124 124 PRO PRO A . n 
A 1 136 ARG 136 125 125 ARG ARG A . n 
A 1 137 GLY 137 126 126 GLY GLY A . n 
A 1 138 MET 138 127 127 MET MET A . n 
A 1 139 VAL 139 128 128 VAL VAL A . n 
A 1 140 LYS 140 129 129 LYS LYS A . n 
A 1 141 SER 141 130 130 SER SER A . n 
A 1 142 LEU 142 131 131 LEU LEU A . n 
A 1 143 LEU 143 132 132 LEU LEU A . n 
A 1 144 TYR 144 133 133 TYR TYR A . n 
A 1 145 GLN 145 134 134 GLN GLN A . n 
A 1 146 ILE 146 135 135 ILE ILE A . n 
A 1 147 LEU 147 136 136 LEU LEU A . n 
A 1 148 ASP 148 137 137 ASP ASP A . n 
A 1 149 GLY 149 138 138 GLY GLY A . n 
A 1 150 ILE 150 139 139 ILE ILE A . n 
A 1 151 HIS 151 140 140 HIS HIS A . n 
A 1 152 TYR 152 141 141 TYR TYR A . n 
A 1 153 LEU 153 142 142 LEU LEU A . n 
A 1 154 HIS 154 143 143 HIS HIS A . n 
A 1 155 ALA 155 144 144 ALA ALA A . n 
A 1 156 ASN 156 145 145 ASN ASN A . n 
A 1 157 TRP 157 146 146 TRP TRP A . n 
A 1 158 VAL 158 147 147 VAL VAL A . n 
A 1 159 LEU 159 148 148 LEU LEU A . n 
A 1 160 HIS 160 149 149 HIS HIS A . n 
A 1 161 ARG 161 150 150 ARG ARG A . n 
A 1 162 ASP 162 151 151 ASP ASP A . n 
A 1 163 LEU 163 152 152 LEU LEU A . n 
A 1 164 LYS 164 153 153 LYS LYS A . n 
A 1 165 PRO 165 154 154 PRO PRO A . n 
A 1 166 ALA 166 155 155 ALA ALA A . n 
A 1 167 ASN 167 156 156 ASN ASN A . n 
A 1 168 ILE 168 157 157 ILE ILE A . n 
A 1 169 LEU 169 158 158 LEU LEU A . n 
A 1 170 VAL 170 159 159 VAL VAL A . n 
A 1 171 MET 171 160 160 MET MET A . n 
A 1 172 GLY 172 161 161 GLY GLY A . n 
A 1 173 GLU 173 162 162 GLU GLU A . n 
A 1 174 GLY 174 163 163 GLY GLY A . n 
A 1 175 PRO 175 164 164 PRO PRO A . n 
A 1 176 GLU 176 165 165 GLU GLU A . n 
A 1 177 ARG 177 166 166 ARG ARG A . n 
A 1 178 GLY 178 167 167 GLY GLY A . n 
A 1 179 ARG 179 168 168 ARG ARG A . n 
A 1 180 VAL 180 169 169 VAL VAL A . n 
A 1 181 LYS 181 170 170 LYS LYS A . n 
A 1 182 ILE 182 171 171 ILE ILE A . n 
A 1 183 ALA 183 172 172 ALA ALA A . n 
A 1 184 ASP 184 173 173 ASP ASP A . n 
A 1 185 MET 185 174 174 MET MET A . n 
A 1 186 GLY 186 175 175 GLY GLY A . n 
A 1 187 PHE 187 176 176 PHE PHE A . n 
A 1 188 ALA 188 177 177 ALA ALA A . n 
A 1 189 ARG 189 178 178 ARG ARG A . n 
A 1 190 LEU 190 179 179 LEU LEU A . n 
A 1 191 PHE 191 180 ?   ?   ?   A . n 
A 1 192 ASN 192 181 ?   ?   ?   A . n 
A 1 193 SER 193 182 ?   ?   ?   A . n 
A 1 194 PRO 194 183 ?   ?   ?   A . n 
A 1 195 LEU 195 184 ?   ?   ?   A . n 
A 1 196 LYS 196 185 ?   ?   ?   A . n 
A 1 197 PRO 197 186 ?   ?   ?   A . n 
A 1 198 LEU 198 187 ?   ?   ?   A . n 
A 1 199 ALA 199 188 ?   ?   ?   A . n 
A 1 200 ASP 200 189 ?   ?   ?   A . n 
A 1 201 LEU 201 190 ?   ?   ?   A . n 
A 1 202 ASP 202 191 ?   ?   ?   A . n 
A 1 203 PRO 203 192 ?   ?   ?   A . n 
A 1 204 VAL 204 193 ?   ?   ?   A . n 
A 1 205 VAL 205 194 ?   ?   ?   A . n 
A 1 206 VAL 206 195 195 VAL VAL A . n 
A 1 207 THR 207 196 196 THR THR A . n 
A 1 208 PHE 208 197 197 PHE PHE A . n 
A 1 209 TRP 209 198 198 TRP TRP A . n 
A 1 210 TYR 210 199 199 TYR TYR A . n 
A 1 211 ARG 211 200 200 ARG ARG A . n 
A 1 212 ALA 212 201 201 ALA ALA A . n 
A 1 213 PRO 213 202 202 PRO PRO A . n 
A 1 214 GLU 214 203 203 GLU GLU A . n 
A 1 215 LEU 215 204 204 LEU LEU A . n 
A 1 216 LEU 216 205 205 LEU LEU A . n 
A 1 217 LEU 217 206 206 LEU LEU A . n 
A 1 218 GLY 218 207 207 GLY GLY A . n 
A 1 219 ALA 219 208 208 ALA ALA A . n 
A 1 220 ARG 220 209 209 ARG ARG A . n 
A 1 221 HIS 221 210 210 HIS HIS A . n 
A 1 222 TYR 222 211 211 TYR TYR A . n 
A 1 223 THR 223 212 212 THR THR A . n 
A 1 224 LYS 224 213 213 LYS LYS A . n 
A 1 225 ALA 225 214 214 ALA ALA A . n 
A 1 226 ILE 226 215 215 ILE ILE A . n 
A 1 227 ASP 227 216 216 ASP ASP A . n 
A 1 228 ILE 228 217 217 ILE ILE A . n 
A 1 229 TRP 229 218 218 TRP TRP A . n 
A 1 230 ALA 230 219 219 ALA ALA A . n 
A 1 231 ILE 231 220 220 ILE ILE A . n 
A 1 232 GLY 232 221 221 GLY GLY A . n 
A 1 233 CYS 233 222 222 CYS CYS A . n 
A 1 234 ILE 234 223 223 ILE ILE A . n 
A 1 235 PHE 235 224 224 PHE PHE A . n 
A 1 236 ALA 236 225 225 ALA ALA A . n 
A 1 237 GLU 237 226 226 GLU GLU A . n 
A 1 238 LEU 238 227 227 LEU LEU A . n 
A 1 239 LEU 239 228 228 LEU LEU A . n 
A 1 240 THR 240 229 229 THR THR A . n 
A 1 241 SER 241 230 230 SER SER A . n 
A 1 242 GLU 242 231 231 GLU GLU A . n 
A 1 243 PRO 243 232 232 PRO PRO A . n 
A 1 244 ILE 244 233 233 ILE ILE A . n 
A 1 245 PHE 245 234 234 PHE PHE A . n 
A 1 246 HIS 246 235 235 HIS HIS A . n 
A 1 247 CYS 247 236 236 CYS CYS A . n 
A 1 248 ARG 248 237 237 ARG ARG A . n 
A 1 249 GLN 249 238 238 GLN GLN A . n 
A 1 250 GLU 250 239 ?   ?   ?   A . n 
A 1 251 ASP 251 240 ?   ?   ?   A . n 
A 1 252 ILE 252 241 ?   ?   ?   A . n 
A 1 253 LYS 253 242 ?   ?   ?   A . n 
A 1 254 THR 254 243 ?   ?   ?   A . n 
A 1 255 SER 255 244 244 SER SER A . n 
A 1 256 ASN 256 245 245 ASN ASN A . n 
A 1 257 PRO 257 246 246 PRO PRO A . n 
A 1 258 TYR 258 247 247 TYR TYR A . n 
A 1 259 HIS 259 248 248 HIS HIS A . n 
A 1 260 HIS 260 249 249 HIS HIS A . n 
A 1 261 ASP 261 250 250 ASP ASP A . n 
A 1 262 GLN 262 251 251 GLN GLN A . n 
A 1 263 LEU 263 252 252 LEU LEU A . n 
A 1 264 ASP 264 253 253 ASP ASP A . n 
A 1 265 ARG 265 254 254 ARG ARG A . n 
A 1 266 ILE 266 255 255 ILE ILE A . n 
A 1 267 PHE 267 256 256 PHE PHE A . n 
A 1 268 ASN 268 257 257 ASN ASN A . n 
A 1 269 VAL 269 258 258 VAL VAL A . n 
A 1 270 MET 270 259 259 MET MET A . n 
A 1 271 GLY 271 260 260 GLY GLY A . n 
A 1 272 PHE 272 261 261 PHE PHE A . n 
A 1 273 PRO 273 262 262 PRO PRO A . n 
A 1 274 ALA 274 263 263 ALA ALA A . n 
A 1 275 ASP 275 264 264 ASP ASP A . n 
A 1 276 LYS 276 265 265 LYS LYS A . n 
A 1 277 ASP 277 266 266 ASP ASP A . n 
A 1 278 TRP 278 267 267 TRP TRP A . n 
A 1 279 GLU 279 268 268 GLU GLU A . n 
A 1 280 ASP 280 269 269 ASP ASP A . n 
A 1 281 ILE 281 270 270 ILE ILE A . n 
A 1 282 LYS 282 271 271 LYS LYS A . n 
A 1 283 LYS 283 272 272 LYS LYS A . n 
A 1 284 MET 284 273 273 MET MET A . n 
A 1 285 PRO 285 274 274 PRO PRO A . n 
A 1 286 GLU 286 275 275 GLU GLU A . n 
A 1 287 HIS 287 276 276 HIS HIS A . n 
A 1 288 SER 288 277 277 SER SER A . n 
A 1 289 THR 289 278 278 THR THR A . n 
A 1 290 LEU 290 279 279 LEU LEU A . n 
A 1 291 MET 291 280 280 MET MET A . n 
A 1 292 LYS 292 281 281 LYS LYS A . n 
A 1 293 ASP 293 282 282 ASP ASP A . n 
A 1 294 PHE 294 283 283 PHE PHE A . n 
A 1 295 ARG 295 284 284 ARG ARG A . n 
A 1 296 ARG 296 285 285 ARG ARG A . n 
A 1 297 ASN 297 286 286 ASN ASN A . n 
A 1 298 THR 298 287 287 THR THR A . n 
A 1 299 TYR 299 288 288 TYR TYR A . n 
A 1 300 THR 300 289 289 THR THR A . n 
A 1 301 ASN 301 290 290 ASN ASN A . n 
A 1 302 CYS 302 291 291 CYS CYS A . n 
A 1 303 SER 303 292 292 SER SER A . n 
A 1 304 LEU 304 293 293 LEU LEU A . n 
A 1 305 ILE 305 294 294 ILE ILE A . n 
A 1 306 LYS 306 295 295 LYS LYS A . n 
A 1 307 TYR 307 296 296 TYR TYR A . n 
A 1 308 MET 308 297 297 MET MET A . n 
A 1 309 GLU 309 298 298 GLU GLU A . n 
A 1 310 LYS 310 299 299 LYS LYS A . n 
A 1 311 HIS 311 300 300 HIS HIS A . n 
A 1 312 LYS 312 301 301 LYS LYS A . n 
A 1 313 VAL 313 302 302 VAL VAL A . n 
A 1 314 LYS 314 303 303 LYS LYS A . n 
A 1 315 PRO 315 304 304 PRO PRO A . n 
A 1 316 ASP 316 305 305 ASP ASP A . n 
A 1 317 SER 317 306 306 SER SER A . n 
A 1 318 LYS 318 307 307 LYS LYS A . n 
A 1 319 ALA 319 308 308 ALA ALA A . n 
A 1 320 PHE 320 309 309 PHE PHE A . n 
A 1 321 HIS 321 310 310 HIS HIS A . n 
A 1 322 LEU 322 311 311 LEU LEU A . n 
A 1 323 LEU 323 312 312 LEU LEU A . n 
A 1 324 GLN 324 313 313 GLN GLN A . n 
A 1 325 LYS 325 314 314 LYS LYS A . n 
A 1 326 LEU 326 315 315 LEU LEU A . n 
A 1 327 LEU 327 316 316 LEU LEU A . n 
A 1 328 THR 328 317 317 THR THR A . n 
A 1 329 MET 329 318 318 MET MET A . n 
A 1 330 ASP 330 319 319 ASP ASP A . n 
A 1 331 PRO 331 320 320 PRO PRO A . n 
A 1 332 ILE 332 321 321 ILE ILE A . n 
A 1 333 LYS 333 322 322 LYS LYS A . n 
A 1 334 ARG 334 323 323 ARG ARG A . n 
A 1 335 ILE 335 324 324 ILE ILE A . n 
A 1 336 THR 336 325 325 THR THR A . n 
A 1 337 SER 337 326 326 SER SER A . n 
A 1 338 GLU 338 327 327 GLU GLU A . n 
A 1 339 GLN 339 328 328 GLN GLN A . n 
A 1 340 ALA 340 329 329 ALA ALA A . n 
A 1 341 MET 341 330 330 MET MET A . n 
A 1 342 GLN 342 331 331 GLN GLN A . n 
A 1 343 ASP 343 332 332 ASP ASP A . n 
A 1 344 PRO 344 333 333 PRO PRO A . n 
A 1 345 TYR 345 334 334 TYR TYR A . n 
A 1 346 PHE 346 335 335 PHE PHE A . n 
A 1 347 LEU 347 336 336 LEU LEU A . n 
A 1 348 GLU 348 337 337 GLU GLU A . n 
A 1 349 ASP 349 338 338 ASP ASP A . n 
A 1 350 PRO 350 339 339 PRO PRO A . n 
A 1 351 LEU 351 340 340 LEU LEU A . n 
A 1 352 PRO 352 341 341 PRO PRO A . n 
A 1 353 THR 353 342 342 THR THR A . n 
A 1 354 SER 354 343 343 SER SER A . n 
A 1 355 ASP 355 344 344 ASP ASP A . n 
A 1 356 VAL 356 345 345 VAL VAL A . n 
A 1 357 PHE 357 346 346 PHE PHE A . n 
A 1 358 ALA 358 347 347 ALA ALA A . n 
A 1 359 GLY 359 348 348 GLY GLY A . n 
A 1 360 CYS 360 349 349 CYS CYS A . n 
A 1 361 GLN 361 350 350 GLN GLN A . n 
A 1 362 ILE 362 351 351 ILE ILE A . n 
A 1 363 PRO 363 352 352 PRO PRO A . n 
A 1 364 TYR 364 353 353 TYR TYR A . n 
A 1 365 PRO 365 354 354 PRO PRO A . n 
A 1 366 LYS 366 355 355 LYS LYS A . n 
A 1 367 ARG 367 356 356 ARG ARG A . n 
A 1 368 GLU 368 357 357 GLU GLU A . n 
A 1 369 PHE 369 358 358 PHE PHE A . n 
A 1 370 LEU 370 359 359 LEU LEU A . n 
A 1 371 THR 371 360 360 THR THR A . n 
A 1 372 GLU 372 361 361 GLU GLU A . n 
A 1 373 GLU 373 362 ?   ?   ?   A . n 
A 1 374 GLU 374 363 ?   ?   ?   A . n 
A 1 375 PRO 375 364 ?   ?   ?   A . n 
A 1 376 ASP 376 365 ?   ?   ?   A . n 
A 1 377 ASP 377 366 ?   ?   ?   A . n 
A 1 378 LYS 378 367 ?   ?   ?   A . n 
A 1 379 GLY 379 368 ?   ?   ?   A . n 
A 1 380 ASP 380 369 ?   ?   ?   A . n 
A 1 381 LYS 381 370 ?   ?   ?   A . n 
A 1 382 LYS 382 371 ?   ?   ?   A . n 
A 1 383 ASN 383 372 ?   ?   ?   A . n 
A 1 384 GLN 384 373 ?   ?   ?   A . n 
A 1 385 GLN 385 374 ?   ?   ?   A . n 
A 1 386 GLN 386 375 ?   ?   ?   A . n 
A 1 387 GLN 387 376 ?   ?   ?   A . n 
A 1 388 GLN 388 377 ?   ?   ?   A . n 
A 1 389 GLY 389 378 ?   ?   ?   A . n 
A 1 390 ASN 390 379 ?   ?   ?   A . n 
A 1 391 ASN 391 380 ?   ?   ?   A . n 
A 1 392 HIS 392 381 ?   ?   ?   A . n 
A 1 393 THR 393 382 ?   ?   ?   A . n 
A 1 394 ASN 394 383 ?   ?   ?   A . n 
A 1 395 GLY 395 384 ?   ?   ?   A . n 
A 1 396 THR 396 385 ?   ?   ?   A . n 
A 1 397 GLY 397 386 ?   ?   ?   A . n 
A 1 398 HIS 398 387 ?   ?   ?   A . n 
A 1 399 PRO 399 388 ?   ?   ?   A . n 
A 1 400 GLY 400 389 ?   ?   ?   A . n 
A 1 401 ASN 401 390 ?   ?   ?   A . n 
A 1 402 GLN 402 391 ?   ?   ?   A . n 
A 1 403 ASP 403 392 ?   ?   ?   A . n 
A 1 404 SER 404 393 ?   ?   ?   A . n 
A 1 405 SER 405 394 ?   ?   ?   A . n 
A 1 406 HIS 406 395 ?   ?   ?   A . n 
A 1 407 THR 407 396 ?   ?   ?   A . n 
A 1 408 GLN 408 397 ?   ?   ?   A . n 
A 1 409 GLY 409 398 ?   ?   ?   A . n 
A 1 410 PRO 410 399 ?   ?   ?   A . n 
A 1 411 PRO 411 400 ?   ?   ?   A . n 
A 1 412 LEU 412 401 ?   ?   ?   A . n 
A 1 413 LYS 413 402 ?   ?   ?   A . n 
A 1 414 LYS 414 403 ?   ?   ?   A . n 
B 2 1   GLY 1   -29 ?   ?   ?   B . n 
B 2 2   SER 2   -28 ?   ?   ?   B . n 
B 2 3   GLY 3   -27 ?   ?   ?   B . n 
B 2 4   MET 4   -26 ?   ?   ?   B . n 
B 2 5   LYS 5   -25 ?   ?   ?   B . n 
B 2 6   GLU 6   -24 ?   ?   ?   B . n 
B 2 7   THR 7   -23 ?   ?   ?   B . n 
B 2 8   ALA 8   -22 ?   ?   ?   B . n 
B 2 9   ALA 9   -21 ?   ?   ?   B . n 
B 2 10  ALA 10  -20 ?   ?   ?   B . n 
B 2 11  LYS 11  -19 ?   ?   ?   B . n 
B 2 12  PHE 12  -18 ?   ?   ?   B . n 
B 2 13  GLU 13  -17 ?   ?   ?   B . n 
B 2 14  ARG 14  -16 ?   ?   ?   B . n 
B 2 15  GLN 15  -15 ?   ?   ?   B . n 
B 2 16  HIS 16  -14 ?   ?   ?   B . n 
B 2 17  MET 17  -13 ?   ?   ?   B . n 
B 2 18  ASP 18  -12 ?   ?   ?   B . n 
B 2 19  SER 19  -11 ?   ?   ?   B . n 
B 2 20  PRO 20  -10 ?   ?   ?   B . n 
B 2 21  ASP 21  -9  ?   ?   ?   B . n 
B 2 22  LEU 22  -8  ?   ?   ?   B . n 
B 2 23  GLY 23  -7  ?   ?   ?   B . n 
B 2 24  THR 24  -6  ?   ?   ?   B . n 
B 2 25  ASP 25  -5  ?   ?   ?   B . n 
B 2 26  ASP 26  -4  ?   ?   ?   B . n 
B 2 27  ASP 27  -3  ?   ?   ?   B . n 
B 2 28  ASP 28  -2  ?   ?   ?   B . n 
B 2 29  LYS 29  -1  ?   ?   ?   B . n 
B 2 30  ALA 30  0   0   ALA ALA B . n 
B 2 31  MET 31  1   1   MET MET B . n 
B 2 32  ALA 32  2   2   ALA ALA B . n 
B 2 33  GLY 33  3   3   GLY GLY B . n 
B 2 34  ASN 34  4   4   ASN ASN B . n 
B 2 35  PHE 35  5   5   PHE PHE B . n 
B 2 36  TRP 36  6   6   TRP TRP B . n 
B 2 37  GLN 37  7   7   GLN GLN B . n 
B 2 38  SER 38  8   8   SER SER B . n 
B 2 39  SER 39  9   9   SER SER B . n 
B 2 40  HIS 40  10  10  HIS HIS B . n 
B 2 41  TYR 41  11  11  TYR TYR B . n 
B 2 42  LEU 42  12  12  LEU LEU B . n 
B 2 43  GLN 43  13  13  GLN GLN B . n 
B 2 44  TRP 44  14  14  TRP TRP B . n 
B 2 45  ILE 45  15  15  ILE ILE B . n 
B 2 46  LEU 46  16  16  LEU LEU B . n 
B 2 47  ASP 47  17  17  ASP ASP B . n 
B 2 48  LYS 48  18  18  LYS LYS B . n 
B 2 49  GLN 49  19  19  GLN GLN B . n 
B 2 50  ASP 50  20  20  ASP ASP B . n 
B 2 51  LEU 51  21  21  LEU LEU B . n 
B 2 52  LEU 52  22  22  LEU LEU B . n 
B 2 53  LYS 53  23  23  LYS LYS B . n 
B 2 54  GLU 54  24  24  GLU GLU B . n 
B 2 55  ARG 55  25  25  ARG ARG B . n 
B 2 56  GLN 56  26  26  GLN GLN B . n 
B 2 57  LYS 57  27  27  LYS LYS B . n 
B 2 58  ASP 58  28  28  ASP ASP B . n 
B 2 59  LEU 59  29  29  LEU LEU B . n 
B 2 60  LYS 60  30  30  LYS LYS B . n 
B 2 61  PHE 61  31  31  PHE PHE B . n 
B 2 62  LEU 62  32  32  LEU LEU B . n 
B 2 63  SER 63  33  33  SER SER B . n 
B 2 64  GLU 64  34  34  GLU GLU B . n 
B 2 65  GLU 65  35  35  GLU GLU B . n 
B 2 66  GLU 66  36  36  GLU GLU B . n 
B 2 67  TYR 67  37  37  TYR TYR B . n 
B 2 68  TRP 68  38  38  TRP TRP B . n 
B 2 69  LYS 69  39  39  LYS LYS B . n 
B 2 70  LEU 70  40  40  LEU LEU B . n 
B 2 71  GLN 71  41  41  GLN GLN B . n 
B 2 72  ILE 72  42  42  ILE ILE B . n 
B 2 73  PHE 73  43  43  PHE PHE B . n 
B 2 74  PHE 74  44  44  PHE PHE B . n 
B 2 75  THR 75  45  45  THR THR B . n 
B 2 76  ASN 76  46  46  ASN ASN B . n 
B 2 77  VAL 77  47  47  VAL VAL B . n 
B 2 78  ILE 78  48  48  ILE ILE B . n 
B 2 79  GLN 79  49  49  GLN GLN B . n 
B 2 80  ALA 80  50  50  ALA ALA B . n 
B 2 81  LEU 81  51  51  LEU LEU B . n 
B 2 82  GLY 82  52  52  GLY GLY B . n 
B 2 83  GLU 83  53  53  GLU GLU B . n 
B 2 84  HIS 84  54  54  HIS HIS B . n 
B 2 85  LEU 85  55  55  LEU LEU B . n 
B 2 86  LYS 86  56  56  LYS LYS B . n 
B 2 87  LEU 87  57  57  LEU LEU B . n 
B 2 88  ARG 88  58  58  ARG ARG B . n 
B 2 89  GLN 89  59  59  GLN GLN B . n 
B 2 90  GLN 90  60  60  GLN GLN B . n 
B 2 91  VAL 91  61  61  VAL VAL B . n 
B 2 92  ILE 92  62  62  ILE ILE B . n 
B 2 93  ALA 93  63  63  ALA ALA B . n 
B 2 94  THR 94  64  64  THR THR B . n 
B 2 95  ALA 95  65  65  ALA ALA B . n 
B 2 96  THR 96  66  66  THR THR B . n 
B 2 97  VAL 97  67  67  VAL VAL B . n 
B 2 98  TYR 98  68  68  TYR TYR B . n 
B 2 99  PHE 99  69  69  PHE PHE B . n 
B 2 100 LYS 100 70  70  LYS LYS B . n 
B 2 101 ARG 101 71  71  ARG ARG B . n 
B 2 102 PHE 102 72  72  PHE PHE B . n 
B 2 103 TYR 103 73  73  TYR TYR B . n 
B 2 104 ALA 104 74  74  ALA ALA B . n 
B 2 105 ARG 105 75  75  ARG ARG B . n 
B 2 106 TYR 106 76  76  TYR TYR B . n 
B 2 107 SER 107 77  77  SER SER B . n 
B 2 108 LEU 108 78  78  LEU LEU B . n 
B 2 109 LYS 109 79  79  LYS LYS B . n 
B 2 110 SER 110 80  80  SER SER B . n 
B 2 111 ILE 111 81  81  ILE ILE B . n 
B 2 112 ASP 112 82  82  ASP ASP B . n 
B 2 113 PRO 113 83  83  PRO PRO B . n 
B 2 114 VAL 114 84  84  VAL VAL B . n 
B 2 115 LEU 115 85  85  LEU LEU B . n 
B 2 116 MET 116 86  86  MET MET B . n 
B 2 117 ALA 117 87  87  ALA ALA B . n 
B 2 118 PRO 118 88  88  PRO PRO B . n 
B 2 119 THR 119 89  89  THR THR B . n 
B 2 120 CYS 120 90  90  CYS CYS B . n 
B 2 121 VAL 121 91  91  VAL VAL B . n 
B 2 122 PHE 122 92  92  PHE PHE B . n 
B 2 123 LEU 123 93  93  LEU LEU B . n 
B 2 124 ALA 124 94  94  ALA ALA B . n 
B 2 125 SER 125 95  95  SER SER B . n 
B 2 126 LYS 126 96  96  LYS LYS B . n 
B 2 127 VAL 127 97  97  VAL VAL B . n 
B 2 128 GLU 128 98  98  GLU GLU B . n 
B 2 129 GLU 129 99  99  GLU GLU B . n 
B 2 130 PHE 130 100 100 PHE PHE B . n 
B 2 131 GLY 131 101 101 GLY GLY B . n 
B 2 132 VAL 132 102 102 VAL VAL B . n 
B 2 133 VAL 133 103 103 VAL VAL B . n 
B 2 134 SER 134 104 104 SER SER B . n 
B 2 135 ASN 135 105 105 ASN ASN B . n 
B 2 136 THR 136 106 106 THR THR B . n 
B 2 137 ARG 137 107 107 ARG ARG B . n 
B 2 138 LEU 138 108 108 LEU LEU B . n 
B 2 139 ILE 139 109 109 ILE ILE B . n 
B 2 140 ALA 140 110 110 ALA ALA B . n 
B 2 141 ALA 141 111 111 ALA ALA B . n 
B 2 142 ALA 142 112 112 ALA ALA B . n 
B 2 143 THR 143 113 113 THR THR B . n 
B 2 144 SER 144 114 114 SER SER B . n 
B 2 145 VAL 145 115 115 VAL VAL B . n 
B 2 146 LEU 146 116 116 LEU LEU B . n 
B 2 147 LYS 147 117 117 LYS LYS B . n 
B 2 148 THR 148 118 118 THR THR B . n 
B 2 149 ARG 149 119 119 ARG ARG B . n 
B 2 150 PHE 150 120 120 PHE PHE B . n 
B 2 151 SER 151 121 121 SER SER B . n 
B 2 152 TYR 152 122 122 TYR TYR B . n 
B 2 153 ALA 153 123 123 ALA ALA B . n 
B 2 154 PHE 154 124 124 PHE PHE B . n 
B 2 155 PRO 155 125 125 PRO PRO B . n 
B 2 156 LYS 156 126 126 LYS LYS B . n 
B 2 157 GLU 157 127 127 GLU GLU B . n 
B 2 158 PHE 158 128 128 PHE PHE B . n 
B 2 159 PRO 159 129 129 PRO PRO B . n 
B 2 160 TYR 160 130 130 TYR TYR B . n 
B 2 161 ARG 161 131 131 ARG ARG B . n 
B 2 162 MET 162 132 132 MET MET B . n 
B 2 163 ASN 163 133 133 ASN ASN B . n 
B 2 164 HIS 164 134 134 HIS HIS B . n 
B 2 165 ILE 165 135 135 ILE ILE B . n 
B 2 166 LEU 166 136 136 LEU LEU B . n 
B 2 167 GLU 167 137 137 GLU GLU B . n 
B 2 168 CYS 168 138 138 CYS CYS B . n 
B 2 169 GLU 169 139 139 GLU GLU B . n 
B 2 170 PHE 170 140 140 PHE PHE B . n 
B 2 171 TYR 171 141 141 TYR TYR B . n 
B 2 172 LEU 172 142 142 LEU LEU B . n 
B 2 173 LEU 173 143 143 LEU LEU B . n 
B 2 174 GLU 174 144 144 GLU GLU B . n 
B 2 175 LEU 175 145 145 LEU LEU B . n 
B 2 176 MET 176 146 146 MET MET B . n 
B 2 177 ASP 177 147 147 ASP ASP B . n 
B 2 178 CYS 178 148 148 CYS CYS B . n 
B 2 179 CYS 179 149 149 CYS CYS B . n 
B 2 180 LEU 180 150 150 LEU LEU B . n 
B 2 181 ILE 181 151 151 ILE ILE B . n 
B 2 182 VAL 182 152 152 VAL VAL B . n 
B 2 183 TYR 183 153 153 TYR TYR B . n 
B 2 184 HIS 184 154 154 HIS HIS B . n 
B 2 185 PRO 185 155 155 PRO PRO B . n 
B 2 186 TYR 186 156 156 TYR TYR B . n 
B 2 187 ARG 187 157 157 ARG ARG B . n 
B 2 188 PRO 188 158 158 PRO PRO B . n 
B 2 189 LEU 189 159 159 LEU LEU B . n 
B 2 190 LEU 190 160 160 LEU LEU B . n 
B 2 191 GLN 191 161 161 GLN GLN B . n 
B 2 192 TYR 192 162 162 TYR TYR B . n 
B 2 193 VAL 193 163 163 VAL VAL B . n 
B 2 194 GLN 194 164 164 GLN GLN B . n 
B 2 195 ASP 195 165 165 ASP ASP B . n 
B 2 196 MET 196 166 166 MET MET B . n 
B 2 197 GLY 197 167 167 GLY GLY B . n 
B 2 198 GLN 198 168 168 GLN GLN B . n 
B 2 199 GLU 199 169 169 GLU GLU B . n 
B 2 200 ASP 200 170 170 ASP ASP B . n 
B 2 201 MET 201 171 171 MET MET B . n 
B 2 202 LEU 202 172 172 LEU LEU B . n 
B 2 203 LEU 203 173 173 LEU LEU B . n 
B 2 204 PRO 204 174 174 PRO PRO B . n 
B 2 205 LEU 205 175 175 LEU LEU B . n 
B 2 206 ALA 206 176 176 ALA ALA B . n 
B 2 207 TRP 207 177 177 TRP TRP B . n 
B 2 208 ARG 208 178 178 ARG ARG B . n 
B 2 209 ILE 209 179 179 ILE ILE B . n 
B 2 210 VAL 210 180 180 VAL VAL B . n 
B 2 211 ASN 211 181 181 ASN ASN B . n 
B 2 212 ASP 212 182 182 ASP ASP B . n 
B 2 213 THR 213 183 183 THR THR B . n 
B 2 214 TYR 214 184 184 TYR TYR B . n 
B 2 215 ARG 215 185 185 ARG ARG B . n 
B 2 216 THR 216 186 186 THR THR B . n 
B 2 217 ASP 217 187 187 ASP ASP B . n 
B 2 218 LEU 218 188 188 LEU LEU B . n 
B 2 219 CYS 219 189 189 CYS CYS B . n 
B 2 220 LEU 220 190 190 LEU LEU B . n 
B 2 221 LEU 221 191 191 LEU LEU B . n 
B 2 222 TYR 222 192 192 TYR TYR B . n 
B 2 223 PRO 223 193 193 PRO PRO B . n 
B 2 224 PRO 224 194 194 PRO PRO B . n 
B 2 225 PHE 225 195 195 PHE PHE B . n 
B 2 226 MET 226 196 196 MET MET B . n 
B 2 227 ILE 227 197 197 ILE ILE B . n 
B 2 228 ALA 228 198 198 ALA ALA B . n 
B 2 229 LEU 229 199 199 LEU LEU B . n 
B 2 230 ALA 230 200 200 ALA ALA B . n 
B 2 231 CYS 231 201 201 CYS CYS B . n 
B 2 232 LEU 232 202 202 LEU LEU B . n 
B 2 233 HIS 233 203 203 HIS HIS B . n 
B 2 234 VAL 234 204 204 VAL VAL B . n 
B 2 235 ALA 235 205 205 ALA ALA B . n 
B 2 236 CYS 236 206 206 CYS CYS B . n 
B 2 237 VAL 237 207 207 VAL VAL B . n 
B 2 238 VAL 238 208 208 VAL VAL B . n 
B 2 239 GLN 239 209 209 GLN GLN B . n 
B 2 240 GLN 240 210 210 GLN GLN B . n 
B 2 241 LYS 241 211 211 LYS LYS B . n 
B 2 242 ASP 242 212 212 ASP ASP B . n 
B 2 243 ALA 243 213 213 ALA ALA B . n 
B 2 244 ARG 244 214 214 ARG ARG B . n 
B 2 245 GLN 245 215 215 GLN GLN B . n 
B 2 246 TRP 246 216 216 TRP TRP B . n 
B 2 247 PHE 247 217 217 PHE PHE B . n 
B 2 248 ALA 248 218 218 ALA ALA B . n 
B 2 249 GLU 249 219 219 GLU GLU B . n 
B 2 250 LEU 250 220 220 LEU LEU B . n 
B 2 251 SER 251 221 221 SER SER B . n 
B 2 252 VAL 252 222 222 VAL VAL B . n 
B 2 253 ASP 253 223 223 ASP ASP B . n 
B 2 254 MET 254 224 224 MET MET B . n 
B 2 255 GLU 255 225 225 GLU GLU B . n 
B 2 256 LYS 256 226 226 LYS LYS B . n 
B 2 257 ILE 257 227 227 ILE ILE B . n 
B 2 258 LEU 258 228 228 LEU LEU B . n 
B 2 259 GLU 259 229 229 GLU GLU B . n 
B 2 260 ILE 260 230 230 ILE ILE B . n 
B 2 261 ILE 261 231 231 ILE ILE B . n 
B 2 262 ARG 262 232 232 ARG ARG B . n 
B 2 263 VAL 263 233 233 VAL VAL B . n 
B 2 264 ILE 264 234 234 ILE ILE B . n 
B 2 265 LEU 265 235 235 LEU LEU B . n 
B 2 266 LYS 266 236 236 LYS LYS B . n 
B 2 267 LEU 267 237 237 LEU LEU B . n 
B 2 268 TYR 268 238 238 TYR TYR B . n 
B 2 269 GLU 269 239 239 GLU GLU B . n 
B 2 270 GLN 270 240 240 GLN GLN B . n 
B 2 271 TRP 271 241 241 TRP TRP B . n 
B 2 272 LYS 272 242 242 LYS LYS B . n 
B 2 273 ASN 273 243 243 ASN ASN B . n 
B 2 274 PHE 274 244 244 PHE PHE B . n 
B 2 275 ASP 275 245 245 ASP ASP B . n 
B 2 276 GLU 276 246 246 GLU GLU B . n 
B 2 277 ARG 277 247 247 ARG ARG B . n 
B 2 278 LYS 278 248 248 LYS LYS B . n 
B 2 279 GLU 279 249 249 GLU GLU B . n 
B 2 280 MET 280 250 250 MET MET B . n 
B 2 281 ALA 281 251 251 ALA ALA B . n 
B 2 282 THR 282 252 252 THR THR B . n 
B 2 283 ILE 283 253 253 ILE ILE B . n 
B 2 284 LEU 284 254 254 LEU LEU B . n 
B 2 285 SER 285 255 255 SER SER B . n 
B 2 286 LYS 286 256 256 LYS LYS B . n 
B 2 287 MET 287 257 257 MET MET B . n 
B 2 288 PRO 288 258 258 PRO PRO B . n 
B 2 289 LYS 289 259 259 LYS LYS B . n 
B 2 290 PRO 290 260 260 PRO PRO B . n 
B 2 291 LYS 291 261 261 LYS LYS B . n 
B 2 292 PRO 292 262 262 PRO PRO B . n 
B 2 293 PRO 293 263 263 PRO PRO B . n 
B 2 294 PRO 294 264 264 PRO PRO B . n 
B 2 295 ASN 295 265 265 ASN ASN B . n 
B 2 296 SER 296 266 ?   ?   ?   B . n 
B 2 297 GLU 297 267 ?   ?   ?   B . n 
B 2 298 GLY 298 268 ?   ?   ?   B . n 
B 2 299 GLU 299 269 ?   ?   ?   B . n 
B 2 300 GLN 300 270 ?   ?   ?   B . n 
B 2 301 GLY 301 271 ?   ?   ?   B . n 
B 2 302 PRO 302 272 ?   ?   ?   B . n 
B 2 303 ASN 303 273 ?   ?   ?   B . n 
B 2 304 GLY 304 274 ?   ?   ?   B . n 
B 2 305 SER 305 275 ?   ?   ?   B . n 
B 2 306 GLN 306 276 ?   ?   ?   B . n 
B 2 307 ASN 307 277 ?   ?   ?   B . n 
B 2 308 SER 308 278 ?   ?   ?   B . n 
B 2 309 SER 309 279 ?   ?   ?   B . n 
B 2 310 TYR 310 280 ?   ?   ?   B . n 
B 2 311 SER 311 281 ?   ?   ?   B . n 
B 2 312 GLN 312 282 ?   ?   ?   B . n 
B 2 313 SER 313 283 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IS8 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IS8 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 EDO   1   501 1   EDO   EDO A . 
D 4 GOL   1   502 1   GOL   GOL A . 
E 5 A1IS8 1   503 1   A1IS8 LIG A . 
F 6 DMS   1   301 1   DMS   DMS B . 
G 6 DMS   1   302 2   DMS   DMS B . 
H 4 GOL   1   303 2   GOL   GOL B . 
I 7 HOH   1   601 66  HOH   HOH A . 
I 7 HOH   2   602 6   HOH   HOH A . 
I 7 HOH   3   603 44  HOH   HOH A . 
I 7 HOH   4   604 18  HOH   HOH A . 
I 7 HOH   5   605 111 HOH   HOH A . 
I 7 HOH   6   606 229 HOH   HOH A . 
I 7 HOH   7   607 110 HOH   HOH A . 
I 7 HOH   8   608 45  HOH   HOH A . 
I 7 HOH   9   609 25  HOH   HOH A . 
I 7 HOH   10  610 196 HOH   HOH A . 
I 7 HOH   11  611 16  HOH   HOH A . 
I 7 HOH   12  612 143 HOH   HOH A . 
I 7 HOH   13  613 51  HOH   HOH A . 
I 7 HOH   14  614 119 HOH   HOH A . 
I 7 HOH   15  615 52  HOH   HOH A . 
I 7 HOH   16  616 114 HOH   HOH A . 
I 7 HOH   17  617 174 HOH   HOH A . 
I 7 HOH   18  618 5   HOH   HOH A . 
I 7 HOH   19  619 43  HOH   HOH A . 
I 7 HOH   20  620 175 HOH   HOH A . 
I 7 HOH   21  621 89  HOH   HOH A . 
I 7 HOH   22  622 201 HOH   HOH A . 
I 7 HOH   23  623 247 HOH   HOH A . 
I 7 HOH   24  624 23  HOH   HOH A . 
I 7 HOH   25  625 14  HOH   HOH A . 
I 7 HOH   26  626 178 HOH   HOH A . 
I 7 HOH   27  627 1   HOH   HOH A . 
I 7 HOH   28  628 251 HOH   HOH A . 
I 7 HOH   29  629 2   HOH   HOH A . 
I 7 HOH   30  630 50  HOH   HOH A . 
I 7 HOH   31  631 236 HOH   HOH A . 
I 7 HOH   32  632 19  HOH   HOH A . 
I 7 HOH   33  633 10  HOH   HOH A . 
I 7 HOH   34  634 180 HOH   HOH A . 
I 7 HOH   35  635 69  HOH   HOH A . 
I 7 HOH   36  636 153 HOH   HOH A . 
I 7 HOH   37  637 103 HOH   HOH A . 
I 7 HOH   38  638 13  HOH   HOH A . 
I 7 HOH   39  639 172 HOH   HOH A . 
I 7 HOH   40  640 169 HOH   HOH A . 
I 7 HOH   41  641 17  HOH   HOH A . 
I 7 HOH   42  642 34  HOH   HOH A . 
I 7 HOH   43  643 206 HOH   HOH A . 
I 7 HOH   44  644 240 HOH   HOH A . 
I 7 HOH   45  645 4   HOH   HOH A . 
I 7 HOH   46  646 164 HOH   HOH A . 
I 7 HOH   47  647 104 HOH   HOH A . 
I 7 HOH   48  648 91  HOH   HOH A . 
I 7 HOH   49  649 226 HOH   HOH A . 
I 7 HOH   50  650 171 HOH   HOH A . 
I 7 HOH   51  651 137 HOH   HOH A . 
I 7 HOH   52  652 202 HOH   HOH A . 
I 7 HOH   53  653 56  HOH   HOH A . 
I 7 HOH   54  654 185 HOH   HOH A . 
I 7 HOH   55  655 8   HOH   HOH A . 
I 7 HOH   56  656 48  HOH   HOH A . 
I 7 HOH   57  657 248 HOH   HOH A . 
I 7 HOH   58  658 189 HOH   HOH A . 
I 7 HOH   59  659 200 HOH   HOH A . 
I 7 HOH   60  660 230 HOH   HOH A . 
I 7 HOH   61  661 53  HOH   HOH A . 
I 7 HOH   62  662 177 HOH   HOH A . 
I 7 HOH   63  663 186 HOH   HOH A . 
I 7 HOH   64  664 39  HOH   HOH A . 
I 7 HOH   65  665 11  HOH   HOH A . 
I 7 HOH   66  666 102 HOH   HOH A . 
I 7 HOH   67  667 37  HOH   HOH A . 
I 7 HOH   68  668 195 HOH   HOH A . 
I 7 HOH   69  669 167 HOH   HOH A . 
I 7 HOH   70  670 59  HOH   HOH A . 
I 7 HOH   71  671 31  HOH   HOH A . 
I 7 HOH   72  672 74  HOH   HOH A . 
I 7 HOH   73  673 162 HOH   HOH A . 
I 7 HOH   74  674 244 HOH   HOH A . 
I 7 HOH   75  675 75  HOH   HOH A . 
I 7 HOH   76  676 42  HOH   HOH A . 
I 7 HOH   77  677 141 HOH   HOH A . 
I 7 HOH   78  678 20  HOH   HOH A . 
I 7 HOH   79  679 132 HOH   HOH A . 
I 7 HOH   80  680 269 HOH   HOH A . 
I 7 HOH   81  681 36  HOH   HOH A . 
I 7 HOH   82  682 96  HOH   HOH A . 
I 7 HOH   83  683 157 HOH   HOH A . 
I 7 HOH   84  684 113 HOH   HOH A . 
I 7 HOH   85  685 238 HOH   HOH A . 
I 7 HOH   86  686 182 HOH   HOH A . 
I 7 HOH   87  687 46  HOH   HOH A . 
I 7 HOH   88  688 246 HOH   HOH A . 
I 7 HOH   89  689 208 HOH   HOH A . 
I 7 HOH   90  690 179 HOH   HOH A . 
I 7 HOH   91  691 62  HOH   HOH A . 
I 7 HOH   92  692 225 HOH   HOH A . 
I 7 HOH   93  693 128 HOH   HOH A . 
I 7 HOH   94  694 24  HOH   HOH A . 
I 7 HOH   95  695 209 HOH   HOH A . 
I 7 HOH   96  696 228 HOH   HOH A . 
I 7 HOH   97  697 67  HOH   HOH A . 
I 7 HOH   98  698 231 HOH   HOH A . 
I 7 HOH   99  699 73  HOH   HOH A . 
I 7 HOH   100 700 109 HOH   HOH A . 
I 7 HOH   101 701 223 HOH   HOH A . 
I 7 HOH   102 702 15  HOH   HOH A . 
I 7 HOH   103 703 88  HOH   HOH A . 
I 7 HOH   104 704 116 HOH   HOH A . 
I 7 HOH   105 705 29  HOH   HOH A . 
I 7 HOH   106 706 54  HOH   HOH A . 
I 7 HOH   107 707 107 HOH   HOH A . 
I 7 HOH   108 708 57  HOH   HOH A . 
I 7 HOH   109 709 243 HOH   HOH A . 
I 7 HOH   110 710 93  HOH   HOH A . 
I 7 HOH   111 711 205 HOH   HOH A . 
I 7 HOH   112 712 80  HOH   HOH A . 
I 7 HOH   113 713 194 HOH   HOH A . 
I 7 HOH   114 714 159 HOH   HOH A . 
I 7 HOH   115 715 242 HOH   HOH A . 
I 7 HOH   116 716 68  HOH   HOH A . 
I 7 HOH   117 717 87  HOH   HOH A . 
I 7 HOH   118 718 166 HOH   HOH A . 
I 7 HOH   119 719 252 HOH   HOH A . 
I 7 HOH   120 720 239 HOH   HOH A . 
I 7 HOH   121 721 245 HOH   HOH A . 
I 7 HOH   122 722 64  HOH   HOH A . 
I 7 HOH   123 723 207 HOH   HOH A . 
I 7 HOH   124 724 203 HOH   HOH A . 
I 7 HOH   125 725 187 HOH   HOH A . 
I 7 HOH   126 726 267 HOH   HOH A . 
I 7 HOH   127 727 131 HOH   HOH A . 
I 7 HOH   128 728 264 HOH   HOH A . 
I 7 HOH   129 729 210 HOH   HOH A . 
I 7 HOH   130 730 94  HOH   HOH A . 
I 7 HOH   131 731 146 HOH   HOH A . 
I 7 HOH   132 732 204 HOH   HOH A . 
I 7 HOH   133 733 85  HOH   HOH A . 
I 7 HOH   134 734 227 HOH   HOH A . 
I 7 HOH   135 735 149 HOH   HOH A . 
I 7 HOH   136 736 232 HOH   HOH A . 
I 7 HOH   137 737 188 HOH   HOH A . 
I 7 HOH   138 738 266 HOH   HOH A . 
I 7 HOH   139 739 122 HOH   HOH A . 
I 7 HOH   140 740 249 HOH   HOH A . 
I 7 HOH   141 741 254 HOH   HOH A . 
I 7 HOH   142 742 250 HOH   HOH A . 
I 7 HOH   143 743 237 HOH   HOH A . 
I 7 HOH   144 744 253 HOH   HOH A . 
I 7 HOH   145 745 183 HOH   HOH A . 
I 7 HOH   146 746 211 HOH   HOH A . 
I 7 HOH   147 747 273 HOH   HOH A . 
J 7 HOH   1   401 63  HOH   HOH B . 
J 7 HOH   2   402 130 HOH   HOH B . 
J 7 HOH   3   403 139 HOH   HOH B . 
J 7 HOH   4   404 47  HOH   HOH B . 
J 7 HOH   5   405 35  HOH   HOH B . 
J 7 HOH   6   406 22  HOH   HOH B . 
J 7 HOH   7   407 199 HOH   HOH B . 
J 7 HOH   8   408 3   HOH   HOH B . 
J 7 HOH   9   409 78  HOH   HOH B . 
J 7 HOH   10  410 140 HOH   HOH B . 
J 7 HOH   11  411 274 HOH   HOH B . 
J 7 HOH   12  412 21  HOH   HOH B . 
J 7 HOH   13  413 165 HOH   HOH B . 
J 7 HOH   14  414 268 HOH   HOH B . 
J 7 HOH   15  415 138 HOH   HOH B . 
J 7 HOH   16  416 76  HOH   HOH B . 
J 7 HOH   17  417 32  HOH   HOH B . 
J 7 HOH   18  418 26  HOH   HOH B . 
J 7 HOH   19  419 190 HOH   HOH B . 
J 7 HOH   20  420 40  HOH   HOH B . 
J 7 HOH   21  421 86  HOH   HOH B . 
J 7 HOH   22  422 220 HOH   HOH B . 
J 7 HOH   23  423 27  HOH   HOH B . 
J 7 HOH   24  424 41  HOH   HOH B . 
J 7 HOH   25  425 70  HOH   HOH B . 
J 7 HOH   26  426 120 HOH   HOH B . 
J 7 HOH   27  427 58  HOH   HOH B . 
J 7 HOH   28  428 112 HOH   HOH B . 
J 7 HOH   29  429 99  HOH   HOH B . 
J 7 HOH   30  430 71  HOH   HOH B . 
J 7 HOH   31  431 33  HOH   HOH B . 
J 7 HOH   32  432 28  HOH   HOH B . 
J 7 HOH   33  433 198 HOH   HOH B . 
J 7 HOH   34  434 221 HOH   HOH B . 
J 7 HOH   35  435 158 HOH   HOH B . 
J 7 HOH   36  436 147 HOH   HOH B . 
J 7 HOH   37  437 133 HOH   HOH B . 
J 7 HOH   38  438 160 HOH   HOH B . 
J 7 HOH   39  439 241 HOH   HOH B . 
J 7 HOH   40  440 272 HOH   HOH B . 
J 7 HOH   41  441 105 HOH   HOH B . 
J 7 HOH   42  442 55  HOH   HOH B . 
J 7 HOH   43  443 215 HOH   HOH B . 
J 7 HOH   44  444 100 HOH   HOH B . 
J 7 HOH   45  445 65  HOH   HOH B . 
J 7 HOH   46  446 142 HOH   HOH B . 
J 7 HOH   47  447 9   HOH   HOH B . 
J 7 HOH   48  448 150 HOH   HOH B . 
J 7 HOH   49  449 121 HOH   HOH B . 
J 7 HOH   50  450 155 HOH   HOH B . 
J 7 HOH   51  451 217 HOH   HOH B . 
J 7 HOH   52  452 118 HOH   HOH B . 
J 7 HOH   53  453 219 HOH   HOH B . 
J 7 HOH   54  454 12  HOH   HOH B . 
J 7 HOH   55  455 148 HOH   HOH B . 
J 7 HOH   56  456 216 HOH   HOH B . 
J 7 HOH   57  457 106 HOH   HOH B . 
J 7 HOH   58  458 265 HOH   HOH B . 
J 7 HOH   59  459 191 HOH   HOH B . 
J 7 HOH   60  460 38  HOH   HOH B . 
J 7 HOH   61  461 144 HOH   HOH B . 
J 7 HOH   62  462 83  HOH   HOH B . 
J 7 HOH   63  463 136 HOH   HOH B . 
J 7 HOH   64  464 263 HOH   HOH B . 
J 7 HOH   65  465 61  HOH   HOH B . 
J 7 HOH   66  466 7   HOH   HOH B . 
J 7 HOH   67  467 72  HOH   HOH B . 
J 7 HOH   68  468 224 HOH   HOH B . 
J 7 HOH   69  469 125 HOH   HOH B . 
J 7 HOH   70  470 101 HOH   HOH B . 
J 7 HOH   71  471 168 HOH   HOH B . 
J 7 HOH   72  472 184 HOH   HOH B . 
J 7 HOH   73  473 82  HOH   HOH B . 
J 7 HOH   74  474 258 HOH   HOH B . 
J 7 HOH   75  475 192 HOH   HOH B . 
J 7 HOH   76  476 152 HOH   HOH B . 
J 7 HOH   77  477 97  HOH   HOH B . 
J 7 HOH   78  478 126 HOH   HOH B . 
J 7 HOH   79  479 234 HOH   HOH B . 
J 7 HOH   80  480 30  HOH   HOH B . 
J 7 HOH   81  481 270 HOH   HOH B . 
J 7 HOH   82  482 95  HOH   HOH B . 
J 7 HOH   83  483 161 HOH   HOH B . 
J 7 HOH   84  484 115 HOH   HOH B . 
J 7 HOH   85  485 108 HOH   HOH B . 
J 7 HOH   86  486 134 HOH   HOH B . 
J 7 HOH   87  487 79  HOH   HOH B . 
J 7 HOH   88  488 151 HOH   HOH B . 
J 7 HOH   89  489 181 HOH   HOH B . 
J 7 HOH   90  490 214 HOH   HOH B . 
J 7 HOH   91  491 84  HOH   HOH B . 
J 7 HOH   92  492 81  HOH   HOH B . 
J 7 HOH   93  493 156 HOH   HOH B . 
J 7 HOH   94  494 235 HOH   HOH B . 
J 7 HOH   95  495 90  HOH   HOH B . 
J 7 HOH   96  496 212 HOH   HOH B . 
J 7 HOH   97  497 98  HOH   HOH B . 
J 7 HOH   98  498 49  HOH   HOH B . 
J 7 HOH   99  499 60  HOH   HOH B . 
J 7 HOH   100 500 170 HOH   HOH B . 
J 7 HOH   101 501 163 HOH   HOH B . 
J 7 HOH   102 502 77  HOH   HOH B . 
J 7 HOH   103 503 92  HOH   HOH B . 
J 7 HOH   104 504 256 HOH   HOH B . 
J 7 HOH   105 505 145 HOH   HOH B . 
J 7 HOH   106 506 123 HOH   HOH B . 
J 7 HOH   107 507 135 HOH   HOH B . 
J 7 HOH   108 508 154 HOH   HOH B . 
J 7 HOH   109 509 259 HOH   HOH B . 
J 7 HOH   110 510 193 HOH   HOH B . 
J 7 HOH   111 511 218 HOH   HOH B . 
J 7 HOH   112 512 197 HOH   HOH B . 
J 7 HOH   113 513 271 HOH   HOH B . 
J 7 HOH   114 514 176 HOH   HOH B . 
J 7 HOH   115 515 173 HOH   HOH B . 
J 7 HOH   116 516 260 HOH   HOH B . 
J 7 HOH   117 517 117 HOH   HOH B . 
J 7 HOH   118 518 261 HOH   HOH B . 
J 7 HOH   119 519 124 HOH   HOH B . 
J 7 HOH   120 520 262 HOH   HOH B . 
J 7 HOH   121 521 129 HOH   HOH B . 
J 7 HOH   122 522 257 HOH   HOH B . 
J 7 HOH   123 523 127 HOH   HOH B . 
J 7 HOH   124 524 222 HOH   HOH B . 
J 7 HOH   125 525 255 HOH   HOH B . 
J 7 HOH   126 526 233 HOH   HOH B . 
J 7 HOH   127 527 213 HOH   HOH B . 
J 7 HOH   128 528 275 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       ? ? ? ? ? ? ? ? ? ? ? BUSTER   ? ? ? '2.11.8 (26-JUL-2023)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                      2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS      ? ? ? '(VERSION Jan 10'      3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? '(Version 1.0.5)'      4 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? .                      5 
? phasing          ? ? ? ? ? ? ? ? ? ? ? BUSTER   ? ? ? .                      6 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9H8C 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     71.531 
_cell.length_a_esd                 ? 
_cell.length_b                     69.208 
_cell.length_b_esd                 ? 
_cell.length_c                     168.237 
_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                         9H8C 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   9H8C 
_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             2.46 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.07 
_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          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'PEG3350, MES pH6.5, HEPES pH6.8, Sodium Formate' 
_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 EIGER2 XE 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-02-24 
_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   0.976 
_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 I03' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.976 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I03 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9H8C 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.573 
_reflns.d_resolution_low                               64.004 
_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                                     19966 
_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                           90.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                11.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.2 
_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                                0.218 
_reflns.pdbx_Rpim_I_all                                0.065 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.209 
_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                                    2.573 
_reflns_shell.d_res_low                                     2.838 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.4 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             999 
_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                               12.3 
_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                               2.066 
_reflns_shell.pdbx_Rpim_I_all                               0.585 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.566 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          52.5 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.980 
_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]                            2.05180 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.00000 
_refine.aniso_B[2][2]                            -5.66530 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            3.61350 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               53.53 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.933 
_refine.correlation_coeff_Fo_to_Fc_free          0.889 
_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                                 9H8C 
_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                            2.573 
_refine.ls_d_res_low                             64.00 
_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                     19966 
_refine.ls_number_reflns_R_free                  933 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    73.2 
_refine.ls_percent_reflns_R_free                 4.670 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1924 
_refine.ls_R_factor_R_free                       0.2621 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1889 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.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                          0.000 
_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          'FOURIER SYNTHESIS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.390 
_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                            ? 
_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_analyze.entry_id                        9H8C 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.32 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.573 
_refine_hist.d_res_low                        64.00 
_refine_hist.number_atoms_solvent             275 
_refine_hist.number_atoms_total               5313 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4987 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         51 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007 ? 5200 ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 0.88  ? 7019 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1850 ? t_dihedral_angle_d        2.00  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_incorr_chiral_ct        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_pseud_angle             ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_trig_c_planes           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 867  ? t_gen_planes              5.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 5200 ? t_it                      10.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_nbd                     ?     ?            
'X-RAY DIFFRACTION' ? 2.75  ? ?    ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 18.85 ? ?    ? t_other_torsion           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_improper_torsion        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 642  ? t_chiral_improper_torsion 5.00  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? 3    ? t_sum_occupancies         1.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_distance        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_angle           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_torsion         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 4486 ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.573 
_refine_ls_shell.d_res_low                        2.77 
_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             406 
_refine_ls_shell.percent_reflns_obs               8.15 
_refine_ls_shell.percent_reflns_R_free            6.67 
_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                  0.2526 
_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                  0.3298 
# 
_struct.entry_id                     9H8C 
_struct.title                        'Human CDK8/Cyclin-C complex with inhibitor 2-9' 
_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        9H8C 
_struct_keywords.text            
'Kinase, Inhibitor, CDK8, Cyclin Dependent Kinase, Cyclin, Transcription-Transferase-Inhibitor Complex, TRANSCRIPTION' 
_struct_keywords.pdbx_keywords   TRANSCRIPTION 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
G N N 6 ? 
H N N 4 ? 
I N N 7 ? 
J N N 7 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP CDK8_HUMAN P49336 ? 1 
;MDYDFKVKLSSERERVEDLFEYEGCKVGRGTYGHVYKAKRKDGKDDKDYALKQIEGTGISMSACREIALLRELKHPNVIS
LQKVFLSHADRKVWLLFDYAEHDLWHIIKFHRASKANKKPVQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVM
GEGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQED
IKTSNPYHHDQLDRIFNVMGFPADKDWEDIKKMPEHSTLMKDFRRNTYTNCSLIKYMEKHKVKPDSKAFHLLQKLLTMDP
IKRITSEQAMQDPYFLEDPLPTSDVFAGCQIPYPKREFLTEEEPDDKGDKKNQQQQQGNNHTNGTGHPGNQDSSHTQGPP
LKK
;
1 
2 UNP CCNC_HUMAN P24863 ? 2 
;MAGNFWQSSHYLQWILDKQDLLKERQKDLKFLSEEEYWKLQIFFTNVIQALGEHLKLRQQVIATATVYFKRFYARYSLKS
IDPVLMAPTCVFLASKVEEFGVVSNTRLIAAATSVLKTRFSYAFPKEFPYRMNHILECEFYLLELMDCCLIVYHPYRPLL
QYVQDMGQEDMLLPLAWRIVNDTYRTDLCLLYPPFMIALACLHVACVVQQKDARQWFAELSVDMEKILEIIRVILKLYEQ
WKNFDERKEMATILSKMPKPKPPPNSEGEQGPNGSQNSSYSQS
;
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 9H8C A 12 ? 414 ? P49336 1 ? 403 ? 1 403 
2 2 9H8C B 31 ? 313 ? P24863 1 ? 283 ? 1 283 
# 
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 9H8C GLY A 1  ? UNP P49336 ? ? 'expression tag' -10 1  
1 9H8C PRO A 2  ? UNP P49336 ? ? 'expression tag' -9  2  
1 9H8C MET A 3  ? UNP P49336 ? ? 'expression tag' -8  3  
1 9H8C ASP A 4  ? UNP P49336 ? ? 'expression tag' -7  4  
1 9H8C TYR A 5  ? UNP P49336 ? ? 'expression tag' -6  5  
1 9H8C LYS A 6  ? UNP P49336 ? ? 'expression tag' -5  6  
1 9H8C ASP A 7  ? UNP P49336 ? ? 'expression tag' -4  7  
1 9H8C ASP A 8  ? UNP P49336 ? ? 'expression tag' -3  8  
1 9H8C ASP A 9  ? UNP P49336 ? ? 'expression tag' -2  9  
1 9H8C ASP A 10 ? UNP P49336 ? ? 'expression tag' -1  10 
1 9H8C LYS A 11 ? UNP P49336 ? ? 'expression tag' 0   11 
2 9H8C GLY B 1  ? UNP P24863 ? ? 'expression tag' -29 12 
2 9H8C SER B 2  ? UNP P24863 ? ? 'expression tag' -28 13 
2 9H8C GLY B 3  ? UNP P24863 ? ? 'expression tag' -27 14 
2 9H8C MET B 4  ? UNP P24863 ? ? 'expression tag' -26 15 
2 9H8C LYS B 5  ? UNP P24863 ? ? 'expression tag' -25 16 
2 9H8C GLU B 6  ? UNP P24863 ? ? 'expression tag' -24 17 
2 9H8C THR B 7  ? UNP P24863 ? ? 'expression tag' -23 18 
2 9H8C ALA B 8  ? UNP P24863 ? ? 'expression tag' -22 19 
2 9H8C ALA B 9  ? UNP P24863 ? ? 'expression tag' -21 20 
2 9H8C ALA B 10 ? UNP P24863 ? ? 'expression tag' -20 21 
2 9H8C LYS B 11 ? UNP P24863 ? ? 'expression tag' -19 22 
2 9H8C PHE B 12 ? UNP P24863 ? ? 'expression tag' -18 23 
2 9H8C GLU B 13 ? UNP P24863 ? ? 'expression tag' -17 24 
2 9H8C ARG B 14 ? UNP P24863 ? ? 'expression tag' -16 25 
2 9H8C GLN B 15 ? UNP P24863 ? ? 'expression tag' -15 26 
2 9H8C HIS B 16 ? UNP P24863 ? ? 'expression tag' -14 27 
2 9H8C MET B 17 ? UNP P24863 ? ? 'expression tag' -13 28 
2 9H8C ASP B 18 ? UNP P24863 ? ? 'expression tag' -12 29 
2 9H8C SER B 19 ? UNP P24863 ? ? 'expression tag' -11 30 
2 9H8C PRO B 20 ? UNP P24863 ? ? 'expression tag' -10 31 
2 9H8C ASP B 21 ? UNP P24863 ? ? 'expression tag' -9  32 
2 9H8C LEU B 22 ? UNP P24863 ? ? 'expression tag' -8  33 
2 9H8C GLY B 23 ? UNP P24863 ? ? 'expression tag' -7  34 
2 9H8C THR B 24 ? UNP P24863 ? ? 'expression tag' -6  35 
2 9H8C ASP B 25 ? UNP P24863 ? ? 'expression tag' -5  36 
2 9H8C ASP B 26 ? UNP P24863 ? ? 'expression tag' -4  37 
2 9H8C ASP B 27 ? UNP P24863 ? ? 'expression tag' -3  38 
2 9H8C ASP B 28 ? UNP P24863 ? ? 'expression tag' -2  39 
2 9H8C LYS B 29 ? UNP P24863 ? ? 'expression tag' -1  40 
2 9H8C ALA B 30 ? UNP P24863 ? ? 'expression tag' 0   41 
# 
_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 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4300  ? 
1 MORE         -20   ? 
1 'SSA (A^2)'  28050 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_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 ASP A 13  ? ARG A 24  ? ASP A 2   ARG A 13  1 ? 12 
HELX_P HELX_P2  AA2 ARG A 26  ? LEU A 30  ? ARG A 15  LEU A 19  1 ? 5  
HELX_P HELX_P3  AA3 SER A 71  ? ARG A 82  ? SER A 60  ARG A 71  1 ? 12 
HELX_P HELX_P4  AA4 LEU A 115 ? ASN A 128 ? LEU A 104 ASN A 117 1 ? 14 
HELX_P HELX_P5  AA5 GLY A 137 ? ASN A 156 ? GLY A 126 ASN A 145 1 ? 20 
HELX_P HELX_P6  AA6 LYS A 164 ? ALA A 166 ? LYS A 153 ALA A 155 5 ? 3  
HELX_P HELX_P7  AA7 GLU A 214 ? GLY A 218 ? GLU A 203 GLY A 207 5 ? 5  
HELX_P HELX_P8  AA8 THR A 223 ? SER A 241 ? THR A 212 SER A 230 1 ? 19 
HELX_P HELX_P9  AA9 HIS A 259 ? GLY A 271 ? HIS A 248 GLY A 260 1 ? 13 
HELX_P HELX_P10 AB1 ALA A 274 ? LYS A 282 ? ALA A 263 LYS A 271 5 ? 9  
HELX_P HELX_P11 AB2 GLU A 286 ? PHE A 294 ? GLU A 275 PHE A 283 1 ? 9  
HELX_P HELX_P12 AB3 ARG A 295 ? THR A 300 ? ARG A 284 THR A 289 5 ? 6  
HELX_P HELX_P13 AB4 SER A 303 ? HIS A 311 ? SER A 292 HIS A 300 1 ? 9  
HELX_P HELX_P14 AB5 SER A 317 ? LEU A 327 ? SER A 306 LEU A 316 1 ? 11 
HELX_P HELX_P15 AB6 ASP A 330 ? ARG A 334 ? ASP A 319 ARG A 323 5 ? 5  
HELX_P HELX_P16 AB7 THR A 336 ? GLN A 342 ? THR A 325 GLN A 331 1 ? 7  
HELX_P HELX_P17 AB8 ASP A 343 ? LEU A 347 ? ASP A 332 LEU A 336 5 ? 5  
HELX_P HELX_P18 AB9 ASN B 34  ? GLN B 37  ? ASN B 4   GLN B 7   5 ? 4  
HELX_P HELX_P19 AC1 SER B 38  ? TRP B 44  ? SER B 8   TRP B 14  1 ? 7  
HELX_P HELX_P20 AC2 ASP B 47  ? GLN B 56  ? ASP B 17  GLN B 26  1 ? 10 
HELX_P HELX_P21 AC3 SER B 63  ? LEU B 85  ? SER B 33  LEU B 55  1 ? 23 
HELX_P HELX_P22 AC4 ARG B 88  ? TYR B 106 ? ARG B 58  TYR B 76  1 ? 19 
HELX_P HELX_P23 AC5 ASP B 112 ? GLU B 128 ? ASP B 82  GLU B 98  1 ? 17 
HELX_P HELX_P24 AC6 SER B 134 ? ARG B 149 ? SER B 104 ARG B 119 1 ? 16 
HELX_P HELX_P25 AC7 ARG B 161 ? LEU B 175 ? ARG B 131 LEU B 145 1 ? 15 
HELX_P HELX_P26 AC8 PRO B 185 ? GLY B 197 ? PRO B 155 GLY B 167 1 ? 13 
HELX_P HELX_P27 AC9 GLN B 198 ? THR B 213 ? GLN B 168 THR B 183 1 ? 16 
HELX_P HELX_P28 AD1 TYR B 214 ? LEU B 221 ? TYR B 184 LEU B 191 5 ? 8  
HELX_P HELX_P29 AD2 PRO B 223 ? GLN B 239 ? PRO B 193 GLN B 209 1 ? 17 
HELX_P HELX_P30 AD3 ALA B 243 ? GLU B 249 ? ALA B 213 GLU B 219 1 ? 7  
HELX_P HELX_P31 AD4 ASP B 253 ? ASN B 273 ? ASP B 223 ASN B 243 1 ? 21 
HELX_P HELX_P32 AD5 ASP B 275 ? MET B 287 ? ASP B 245 MET B 257 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          ASP 
_struct_mon_prot_cis.label_seq_id           349 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           ASP 
_struct_mon_prot_cis.auth_seq_id            338 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    350 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     339 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -1.54 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 PHE A 31  ? GLU A 32  ? PHE A 20  GLU A 21  
AA1 2 GLY A 44  ? ARG A 51  ? GLY A 33  ARG A 40  
AA1 3 LYS A 37  ? GLY A 41  ? LYS A 26  GLY A 30  
AA2 1 PHE A 31  ? GLU A 32  ? PHE A 20  GLU A 21  
AA2 2 GLY A 44  ? ARG A 51  ? GLY A 33  ARG A 40  
AA2 3 TYR A 60  ? ILE A 65  ? TYR A 49  ILE A 54  
AA2 4 LYS A 103 ? ASP A 109 ? LYS A 92  ASP A 98  
AA2 5 LEU A 92  ? SER A 98  ? LEU A 81  SER A 87  
AA3 1 HIS A 113 ? ASP A 114 ? HIS A 102 ASP A 103 
AA3 2 ILE A 168 ? VAL A 170 ? ILE A 157 VAL A 159 
AA3 3 VAL A 180 ? ILE A 182 ? VAL A 169 ILE A 171 
# 
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 GLU A 32  ? N GLU A 21  O LYS A 50  ? O LYS A 39  
AA1 2 3 O VAL A 46  ? O VAL A 35  N GLY A 39  ? N GLY A 28  
AA2 1 2 N GLU A 32  ? N GLU A 21  O LYS A 50  ? O LYS A 39  
AA2 2 3 N ALA A 49  ? N ALA A 38  O TYR A 60  ? O TYR A 49  
AA2 3 4 N ILE A 65  ? N ILE A 54  O VAL A 104 ? O VAL A 93  
AA2 4 5 O TRP A 105 ? O TRP A 94  N PHE A 96  ? N PHE A 85  
AA3 1 2 N HIS A 113 ? N HIS A 102 O VAL A 170 ? O VAL A 159 
AA3 2 3 N LEU A 169 ? N LEU A 158 O LYS A 181 ? O LYS A 170 
# 
_pdbx_entry_details.entry_id                   9H8C 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ARG A 13  ? ? -47.62  109.46 
2  1 TYR A 22  ? ? -145.37 -12.43 
3  1 LYS A 44  ? ? -82.90  49.42  
4  1 ASP A 45  ? ? -160.75 -63.66 
5  1 ASP A 46  ? ? 71.98   -0.89  
6  1 ARG A 125 ? ? 3.83    -77.35 
7  1 ARG A 150 ? ? 76.46   -12.96 
8  1 ASP A 151 ? ? -151.67 32.67  
9  1 ASP A 173 ? ? 68.83   82.68  
10 1 SER A 230 ? ? 85.19   -11.68 
11 1 PHE A 234 ? ? -108.71 40.38  
12 1 TRP A 267 ? ? -162.14 83.12  
13 1 ILE A 351 ? ? -48.85  108.10 
# 
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 1.4726  68.9206 57.5333 0.0427  ? -0.0093 ? -0.0738 ? -0.1457 ? 0.0186  ? 0.0533  ? 0.1240 ? 
-1.2911 ? -1.3112 ? 1.9272 ? 0.7534  ? 0.9355 ? 0.1742  ? -0.0724 ? 0.1363  ? -0.2754 ? -0.1746 ? 0.0016  ? -0.1173 ? -0.1164 ? 
0.0003  ? 
2 'X-RAY DIFFRACTION' ? refined 10.5243 40.1021 56.4537 0.0245  ? -0.0160 ? -0.0173 ? -0.0927 ? -0.0053 ? -0.0527 ? 1.0415 ? 
0.2582  ? -0.0469 ? 1.6511 ? -0.4424 ? 0.4846 ? 0.0013  ? 0.0903  ? -0.0511 ? -0.0936 ? 0.0492  ? 0.0381  ? 0.0209  ? -0.0184 ? 
-0.0505 ? 
3 'X-RAY DIFFRACTION' ? refined -3.9012 68.2971 86.5482 -0.0326 ? -0.0456 ? 0.0498  ? -0.1315 ? 0.0122  ? 0.0355  ? 0.6327 ? 
-0.4337 ? 0.0874  ? 0.4199 ? 0.0646  ? 1.6199 ? -0.0075 ? -0.0573 ? 0.0630  ? -0.0874 ? 0.1434  ? -0.0092 ? -0.0121 ? 0.0681  ? 
-0.1359 ? 
# 
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 ? ? ? ? ? ? ? ? ? ? ? '{ A|0 - A|100 }'  
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? '{ A|101 - A|362}' 
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? '{ B|* }'          
# 
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 GLY -10 ? A GLY 1   
2   1 Y 1 A PRO -9  ? A PRO 2   
3   1 Y 1 A MET -8  ? A MET 3   
4   1 Y 1 A ASP -7  ? A ASP 4   
5   1 Y 1 A TYR -6  ? A TYR 5   
6   1 Y 1 A LYS -5  ? A LYS 6   
7   1 Y 1 A ASP -4  ? A ASP 7   
8   1 Y 1 A ASP -3  ? A ASP 8   
9   1 Y 1 A ASP -2  ? A ASP 9   
10  1 Y 1 A ASP -1  ? A ASP 10  
11  1 Y 1 A LYS 0   ? A LYS 11  
12  1 Y 1 A LYS 118 ? A LYS 129 
13  1 Y 1 A LYS 119 ? A LYS 130 
14  1 Y 1 A PRO 120 ? A PRO 131 
15  1 Y 1 A VAL 121 ? A VAL 132 
16  1 Y 1 A GLN 122 ? A GLN 133 
17  1 Y 1 A PHE 180 ? A PHE 191 
18  1 Y 1 A ASN 181 ? A ASN 192 
19  1 Y 1 A SER 182 ? A SER 193 
20  1 Y 1 A PRO 183 ? A PRO 194 
21  1 Y 1 A LEU 184 ? A LEU 195 
22  1 Y 1 A LYS 185 ? A LYS 196 
23  1 Y 1 A PRO 186 ? A PRO 197 
24  1 Y 1 A LEU 187 ? A LEU 198 
25  1 Y 1 A ALA 188 ? A ALA 199 
26  1 Y 1 A ASP 189 ? A ASP 200 
27  1 Y 1 A LEU 190 ? A LEU 201 
28  1 Y 1 A ASP 191 ? A ASP 202 
29  1 Y 1 A PRO 192 ? A PRO 203 
30  1 Y 1 A VAL 193 ? A VAL 204 
31  1 Y 1 A VAL 194 ? A VAL 205 
32  1 Y 1 A GLU 239 ? A GLU 250 
33  1 Y 1 A ASP 240 ? A ASP 251 
34  1 Y 1 A ILE 241 ? A ILE 252 
35  1 Y 1 A LYS 242 ? A LYS 253 
36  1 Y 1 A THR 243 ? A THR 254 
37  1 Y 1 A GLU 362 ? A GLU 373 
38  1 Y 1 A GLU 363 ? A GLU 374 
39  1 Y 1 A PRO 364 ? A PRO 375 
40  1 Y 1 A ASP 365 ? A ASP 376 
41  1 Y 1 A ASP 366 ? A ASP 377 
42  1 Y 1 A LYS 367 ? A LYS 378 
43  1 Y 1 A GLY 368 ? A GLY 379 
44  1 Y 1 A ASP 369 ? A ASP 380 
45  1 Y 1 A LYS 370 ? A LYS 381 
46  1 Y 1 A LYS 371 ? A LYS 382 
47  1 Y 1 A ASN 372 ? A ASN 383 
48  1 Y 1 A GLN 373 ? A GLN 384 
49  1 Y 1 A GLN 374 ? A GLN 385 
50  1 Y 1 A GLN 375 ? A GLN 386 
51  1 Y 1 A GLN 376 ? A GLN 387 
52  1 Y 1 A GLN 377 ? A GLN 388 
53  1 Y 1 A GLY 378 ? A GLY 389 
54  1 Y 1 A ASN 379 ? A ASN 390 
55  1 Y 1 A ASN 380 ? A ASN 391 
56  1 Y 1 A HIS 381 ? A HIS 392 
57  1 Y 1 A THR 382 ? A THR 393 
58  1 Y 1 A ASN 383 ? A ASN 394 
59  1 Y 1 A GLY 384 ? A GLY 395 
60  1 Y 1 A THR 385 ? A THR 396 
61  1 Y 1 A GLY 386 ? A GLY 397 
62  1 Y 1 A HIS 387 ? A HIS 398 
63  1 Y 1 A PRO 388 ? A PRO 399 
64  1 Y 1 A GLY 389 ? A GLY 400 
65  1 Y 1 A ASN 390 ? A ASN 401 
66  1 Y 1 A GLN 391 ? A GLN 402 
67  1 Y 1 A ASP 392 ? A ASP 403 
68  1 Y 1 A SER 393 ? A SER 404 
69  1 Y 1 A SER 394 ? A SER 405 
70  1 Y 1 A HIS 395 ? A HIS 406 
71  1 Y 1 A THR 396 ? A THR 407 
72  1 Y 1 A GLN 397 ? A GLN 408 
73  1 Y 1 A GLY 398 ? A GLY 409 
74  1 Y 1 A PRO 399 ? A PRO 410 
75  1 Y 1 A PRO 400 ? A PRO 411 
76  1 Y 1 A LEU 401 ? A LEU 412 
77  1 Y 1 A LYS 402 ? A LYS 413 
78  1 Y 1 A LYS 403 ? A LYS 414 
79  1 Y 1 B GLY -29 ? B GLY 1   
80  1 Y 1 B SER -28 ? B SER 2   
81  1 Y 1 B GLY -27 ? B GLY 3   
82  1 Y 1 B MET -26 ? B MET 4   
83  1 Y 1 B LYS -25 ? B LYS 5   
84  1 Y 1 B GLU -24 ? B GLU 6   
85  1 Y 1 B THR -23 ? B THR 7   
86  1 Y 1 B ALA -22 ? B ALA 8   
87  1 Y 1 B ALA -21 ? B ALA 9   
88  1 Y 1 B ALA -20 ? B ALA 10  
89  1 Y 1 B LYS -19 ? B LYS 11  
90  1 Y 1 B PHE -18 ? B PHE 12  
91  1 Y 1 B GLU -17 ? B GLU 13  
92  1 Y 1 B ARG -16 ? B ARG 14  
93  1 Y 1 B GLN -15 ? B GLN 15  
94  1 Y 1 B HIS -14 ? B HIS 16  
95  1 Y 1 B MET -13 ? B MET 17  
96  1 Y 1 B ASP -12 ? B ASP 18  
97  1 Y 1 B SER -11 ? B SER 19  
98  1 Y 1 B PRO -10 ? B PRO 20  
99  1 Y 1 B ASP -9  ? B ASP 21  
100 1 Y 1 B LEU -8  ? B LEU 22  
101 1 Y 1 B GLY -7  ? B GLY 23  
102 1 Y 1 B THR -6  ? B THR 24  
103 1 Y 1 B ASP -5  ? B ASP 25  
104 1 Y 1 B ASP -4  ? B ASP 26  
105 1 Y 1 B ASP -3  ? B ASP 27  
106 1 Y 1 B ASP -2  ? B ASP 28  
107 1 Y 1 B LYS -1  ? B LYS 29  
108 1 Y 1 B SER 266 ? B SER 296 
109 1 Y 1 B GLU 267 ? B GLU 297 
110 1 Y 1 B GLY 268 ? B GLY 298 
111 1 Y 1 B GLU 269 ? B GLU 299 
112 1 Y 1 B GLN 270 ? B GLN 300 
113 1 Y 1 B GLY 271 ? B GLY 301 
114 1 Y 1 B PRO 272 ? B PRO 302 
115 1 Y 1 B ASN 273 ? B ASN 303 
116 1 Y 1 B GLY 274 ? B GLY 304 
117 1 Y 1 B SER 275 ? B SER 305 
118 1 Y 1 B GLN 276 ? B GLN 306 
119 1 Y 1 B ASN 277 ? B ASN 307 
120 1 Y 1 B SER 278 ? B SER 308 
121 1 Y 1 B SER 279 ? B SER 309 
122 1 Y 1 B TYR 280 ? B TYR 310 
123 1 Y 1 B SER 281 ? B SER 311 
124 1 Y 1 B GLN 282 ? B GLN 312 
125 1 Y 1 B SER 283 ? B SER 313 
# 
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 
A1IS8 N1   N Y N 1   
A1IS8 N3   N N N 2   
A1IS8 C4   C Y N 3   
A1IS8 C5   C Y N 4   
A1IS8 C6   C Y N 5   
A1IS8 C7   C Y N 6   
A1IS8 C8   C N S 7   
A1IS8 C10  C N N 8   
A1IS8 C13  C N N 9   
A1IS8 C15  C Y N 10  
A1IS8 C17  C Y N 11  
A1IS8 N5   N N N 12  
A1IS8 C18  C N N 13  
A1IS8 C16  C Y N 14  
A1IS8 N4   N Y N 15  
A1IS8 C14  C Y N 16  
A1IS8 O    O N N 17  
A1IS8 C11  C N N 18  
A1IS8 C9   C N N 19  
A1IS8 C12  C N N 20  
A1IS8 N2   N Y N 21  
A1IS8 N    N N N 22  
A1IS8 C2   C N N 23  
A1IS8 C1   C N N 24  
A1IS8 C3   C N N 25  
A1IS8 C    C N R 26  
A1IS8 F    F N N 27  
A1IS8 H1   H N N 28  
A1IS8 H2   H N N 29  
A1IS8 H3   H N N 30  
A1IS8 H4   H N N 31  
A1IS8 H5   H N N 32  
A1IS8 H6   H N N 33  
A1IS8 H7   H N N 34  
A1IS8 H8   H N N 35  
A1IS8 H9   H N N 36  
A1IS8 H10  H N N 37  
A1IS8 H11  H N N 38  
A1IS8 H12  H N N 39  
A1IS8 H13  H N N 40  
A1IS8 H14  H N N 41  
A1IS8 H15  H N N 42  
A1IS8 H16  H N N 43  
A1IS8 H17  H N N 44  
A1IS8 H18  H N N 45  
A1IS8 H19  H N N 46  
A1IS8 H20  H N N 47  
A1IS8 H21  H N N 48  
ALA   N    N N N 49  
ALA   CA   C N S 50  
ALA   C    C N N 51  
ALA   O    O N N 52  
ALA   CB   C N N 53  
ALA   OXT  O N N 54  
ALA   H    H N N 55  
ALA   H2   H N N 56  
ALA   HA   H N N 57  
ALA   HB1  H N N 58  
ALA   HB2  H N N 59  
ALA   HB3  H N N 60  
ALA   HXT  H N N 61  
ARG   N    N N N 62  
ARG   CA   C N S 63  
ARG   C    C N N 64  
ARG   O    O N N 65  
ARG   CB   C N N 66  
ARG   CG   C N N 67  
ARG   CD   C N N 68  
ARG   NE   N N N 69  
ARG   CZ   C N N 70  
ARG   NH1  N N N 71  
ARG   NH2  N N N 72  
ARG   OXT  O N N 73  
ARG   H    H N N 74  
ARG   H2   H N N 75  
ARG   HA   H N N 76  
ARG   HB2  H N N 77  
ARG   HB3  H N N 78  
ARG   HG2  H N N 79  
ARG   HG3  H N N 80  
ARG   HD2  H N N 81  
ARG   HD3  H N N 82  
ARG   HE   H N N 83  
ARG   HH11 H N N 84  
ARG   HH12 H N N 85  
ARG   HH21 H N N 86  
ARG   HH22 H N N 87  
ARG   HXT  H N N 88  
ASN   N    N N N 89  
ASN   CA   C N S 90  
ASN   C    C N N 91  
ASN   O    O N N 92  
ASN   CB   C N N 93  
ASN   CG   C N N 94  
ASN   OD1  O N N 95  
ASN   ND2  N N N 96  
ASN   OXT  O N N 97  
ASN   H    H N N 98  
ASN   H2   H N N 99  
ASN   HA   H N N 100 
ASN   HB2  H N N 101 
ASN   HB3  H N N 102 
ASN   HD21 H N N 103 
ASN   HD22 H N N 104 
ASN   HXT  H N N 105 
ASP   N    N N N 106 
ASP   CA   C N S 107 
ASP   C    C N N 108 
ASP   O    O N N 109 
ASP   CB   C N N 110 
ASP   CG   C N N 111 
ASP   OD1  O N N 112 
ASP   OD2  O N N 113 
ASP   OXT  O N N 114 
ASP   H    H N N 115 
ASP   H2   H N N 116 
ASP   HA   H N N 117 
ASP   HB2  H N N 118 
ASP   HB3  H N N 119 
ASP   HD2  H N N 120 
ASP   HXT  H N N 121 
CYS   N    N N N 122 
CYS   CA   C N R 123 
CYS   C    C N N 124 
CYS   O    O N N 125 
CYS   CB   C N N 126 
CYS   SG   S N N 127 
CYS   OXT  O N N 128 
CYS   H    H N N 129 
CYS   H2   H N N 130 
CYS   HA   H N N 131 
CYS   HB2  H N N 132 
CYS   HB3  H N N 133 
CYS   HG   H N N 134 
CYS   HXT  H N N 135 
DMS   S    S N N 136 
DMS   O    O N N 137 
DMS   C1   C N N 138 
DMS   C2   C N N 139 
DMS   H11  H N N 140 
DMS   H12  H N N 141 
DMS   H13  H N N 142 
DMS   H21  H N N 143 
DMS   H22  H N N 144 
DMS   H23  H N N 145 
EDO   C1   C N N 146 
EDO   O1   O N N 147 
EDO   C2   C N N 148 
EDO   O2   O N N 149 
EDO   H11  H N N 150 
EDO   H12  H N N 151 
EDO   HO1  H N N 152 
EDO   H21  H N N 153 
EDO   H22  H N N 154 
EDO   HO2  H N N 155 
GLN   N    N N N 156 
GLN   CA   C N S 157 
GLN   C    C N N 158 
GLN   O    O N N 159 
GLN   CB   C N N 160 
GLN   CG   C N N 161 
GLN   CD   C N N 162 
GLN   OE1  O N N 163 
GLN   NE2  N N N 164 
GLN   OXT  O N N 165 
GLN   H    H N N 166 
GLN   H2   H N N 167 
GLN   HA   H N N 168 
GLN   HB2  H N N 169 
GLN   HB3  H N N 170 
GLN   HG2  H N N 171 
GLN   HG3  H N N 172 
GLN   HE21 H N N 173 
GLN   HE22 H N N 174 
GLN   HXT  H N N 175 
GLU   N    N N N 176 
GLU   CA   C N S 177 
GLU   C    C N N 178 
GLU   O    O N N 179 
GLU   CB   C N N 180 
GLU   CG   C N N 181 
GLU   CD   C N N 182 
GLU   OE1  O N N 183 
GLU   OE2  O N N 184 
GLU   OXT  O N N 185 
GLU   H    H N N 186 
GLU   H2   H N N 187 
GLU   HA   H N N 188 
GLU   HB2  H N N 189 
GLU   HB3  H N N 190 
GLU   HG2  H N N 191 
GLU   HG3  H N N 192 
GLU   HE2  H N N 193 
GLU   HXT  H N N 194 
GLY   N    N N N 195 
GLY   CA   C N N 196 
GLY   C    C N N 197 
GLY   O    O N N 198 
GLY   OXT  O N N 199 
GLY   H    H N N 200 
GLY   H2   H N N 201 
GLY   HA2  H N N 202 
GLY   HA3  H N N 203 
GLY   HXT  H N N 204 
GOL   C1   C N N 205 
GOL   O1   O N N 206 
GOL   C2   C N N 207 
GOL   O2   O N N 208 
GOL   C3   C N N 209 
GOL   O3   O N N 210 
GOL   H11  H N N 211 
GOL   H12  H N N 212 
GOL   HO1  H N N 213 
GOL   H2   H N N 214 
GOL   HO2  H N N 215 
GOL   H31  H N N 216 
GOL   H32  H N N 217 
GOL   HO3  H N N 218 
HIS   N    N N N 219 
HIS   CA   C N S 220 
HIS   C    C N N 221 
HIS   O    O N N 222 
HIS   CB   C N N 223 
HIS   CG   C Y N 224 
HIS   ND1  N Y N 225 
HIS   CD2  C Y N 226 
HIS   CE1  C Y N 227 
HIS   NE2  N Y N 228 
HIS   OXT  O N N 229 
HIS   H    H N N 230 
HIS   H2   H N N 231 
HIS   HA   H N N 232 
HIS   HB2  H N N 233 
HIS   HB3  H N N 234 
HIS   HD1  H N N 235 
HIS   HD2  H N N 236 
HIS   HE1  H N N 237 
HIS   HE2  H N N 238 
HIS   HXT  H N N 239 
HOH   O    O N N 240 
HOH   H1   H N N 241 
HOH   H2   H N N 242 
ILE   N    N N N 243 
ILE   CA   C N S 244 
ILE   C    C N N 245 
ILE   O    O N N 246 
ILE   CB   C N S 247 
ILE   CG1  C N N 248 
ILE   CG2  C N N 249 
ILE   CD1  C N N 250 
ILE   OXT  O N N 251 
ILE   H    H N N 252 
ILE   H2   H N N 253 
ILE   HA   H N N 254 
ILE   HB   H N N 255 
ILE   HG12 H N N 256 
ILE   HG13 H N N 257 
ILE   HG21 H N N 258 
ILE   HG22 H N N 259 
ILE   HG23 H N N 260 
ILE   HD11 H N N 261 
ILE   HD12 H N N 262 
ILE   HD13 H N N 263 
ILE   HXT  H N N 264 
LEU   N    N N N 265 
LEU   CA   C N S 266 
LEU   C    C N N 267 
LEU   O    O N N 268 
LEU   CB   C N N 269 
LEU   CG   C N N 270 
LEU   CD1  C N N 271 
LEU   CD2  C N N 272 
LEU   OXT  O N N 273 
LEU   H    H N N 274 
LEU   H2   H N N 275 
LEU   HA   H N N 276 
LEU   HB2  H N N 277 
LEU   HB3  H N N 278 
LEU   HG   H N N 279 
LEU   HD11 H N N 280 
LEU   HD12 H N N 281 
LEU   HD13 H N N 282 
LEU   HD21 H N N 283 
LEU   HD22 H N N 284 
LEU   HD23 H N N 285 
LEU   HXT  H N N 286 
LYS   N    N N N 287 
LYS   CA   C N S 288 
LYS   C    C N N 289 
LYS   O    O N N 290 
LYS   CB   C N N 291 
LYS   CG   C N N 292 
LYS   CD   C N N 293 
LYS   CE   C N N 294 
LYS   NZ   N N N 295 
LYS   OXT  O N N 296 
LYS   H    H N N 297 
LYS   H2   H N N 298 
LYS   HA   H N N 299 
LYS   HB2  H N N 300 
LYS   HB3  H N N 301 
LYS   HG2  H N N 302 
LYS   HG3  H N N 303 
LYS   HD2  H N N 304 
LYS   HD3  H N N 305 
LYS   HE2  H N N 306 
LYS   HE3  H N N 307 
LYS   HZ1  H N N 308 
LYS   HZ2  H N N 309 
LYS   HZ3  H N N 310 
LYS   HXT  H N N 311 
MET   N    N N N 312 
MET   CA   C N S 313 
MET   C    C N N 314 
MET   O    O N N 315 
MET   CB   C N N 316 
MET   CG   C N N 317 
MET   SD   S N N 318 
MET   CE   C N N 319 
MET   OXT  O N N 320 
MET   H    H N N 321 
MET   H2   H N N 322 
MET   HA   H N N 323 
MET   HB2  H N N 324 
MET   HB3  H N N 325 
MET   HG2  H N N 326 
MET   HG3  H N N 327 
MET   HE1  H N N 328 
MET   HE2  H N N 329 
MET   HE3  H N N 330 
MET   HXT  H N N 331 
PHE   N    N N N 332 
PHE   CA   C N S 333 
PHE   C    C N N 334 
PHE   O    O N N 335 
PHE   CB   C N N 336 
PHE   CG   C Y N 337 
PHE   CD1  C Y N 338 
PHE   CD2  C Y N 339 
PHE   CE1  C Y N 340 
PHE   CE2  C Y N 341 
PHE   CZ   C Y N 342 
PHE   OXT  O N N 343 
PHE   H    H N N 344 
PHE   H2   H N N 345 
PHE   HA   H N N 346 
PHE   HB2  H N N 347 
PHE   HB3  H N N 348 
PHE   HD1  H N N 349 
PHE   HD2  H N N 350 
PHE   HE1  H N N 351 
PHE   HE2  H N N 352 
PHE   HZ   H N N 353 
PHE   HXT  H N N 354 
PRO   N    N N N 355 
PRO   CA   C N S 356 
PRO   C    C N N 357 
PRO   O    O N N 358 
PRO   CB   C N N 359 
PRO   CG   C N N 360 
PRO   CD   C N N 361 
PRO   OXT  O N N 362 
PRO   H    H N N 363 
PRO   HA   H N N 364 
PRO   HB2  H N N 365 
PRO   HB3  H N N 366 
PRO   HG2  H N N 367 
PRO   HG3  H N N 368 
PRO   HD2  H N N 369 
PRO   HD3  H N N 370 
PRO   HXT  H N N 371 
SER   N    N N N 372 
SER   CA   C N S 373 
SER   C    C N N 374 
SER   O    O N N 375 
SER   CB   C N N 376 
SER   OG   O N N 377 
SER   OXT  O N N 378 
SER   H    H N N 379 
SER   H2   H N N 380 
SER   HA   H N N 381 
SER   HB2  H N N 382 
SER   HB3  H N N 383 
SER   HG   H N N 384 
SER   HXT  H N N 385 
THR   N    N N N 386 
THR   CA   C N S 387 
THR   C    C N N 388 
THR   O    O N N 389 
THR   CB   C N R 390 
THR   OG1  O N N 391 
THR   CG2  C N N 392 
THR   OXT  O N N 393 
THR   H    H N N 394 
THR   H2   H N N 395 
THR   HA   H N N 396 
THR   HB   H N N 397 
THR   HG1  H N N 398 
THR   HG21 H N N 399 
THR   HG22 H N N 400 
THR   HG23 H N N 401 
THR   HXT  H N N 402 
TRP   N    N N N 403 
TRP   CA   C N S 404 
TRP   C    C N N 405 
TRP   O    O N N 406 
TRP   CB   C N N 407 
TRP   CG   C Y N 408 
TRP   CD1  C Y N 409 
TRP   CD2  C Y N 410 
TRP   NE1  N Y N 411 
TRP   CE2  C Y N 412 
TRP   CE3  C Y N 413 
TRP   CZ2  C Y N 414 
TRP   CZ3  C Y N 415 
TRP   CH2  C Y N 416 
TRP   OXT  O N N 417 
TRP   H    H N N 418 
TRP   H2   H N N 419 
TRP   HA   H N N 420 
TRP   HB2  H N N 421 
TRP   HB3  H N N 422 
TRP   HD1  H N N 423 
TRP   HE1  H N N 424 
TRP   HE3  H N N 425 
TRP   HZ2  H N N 426 
TRP   HZ3  H N N 427 
TRP   HH2  H N N 428 
TRP   HXT  H N N 429 
TYR   N    N N N 430 
TYR   CA   C N S 431 
TYR   C    C N N 432 
TYR   O    O N N 433 
TYR   CB   C N N 434 
TYR   CG   C Y N 435 
TYR   CD1  C Y N 436 
TYR   CD2  C Y N 437 
TYR   CE1  C Y N 438 
TYR   CE2  C Y N 439 
TYR   CZ   C Y N 440 
TYR   OH   O N N 441 
TYR   OXT  O N N 442 
TYR   H    H N N 443 
TYR   H2   H N N 444 
TYR   HA   H N N 445 
TYR   HB2  H N N 446 
TYR   HB3  H N N 447 
TYR   HD1  H N N 448 
TYR   HD2  H N N 449 
TYR   HE1  H N N 450 
TYR   HE2  H N N 451 
TYR   HH   H N N 452 
TYR   HXT  H N N 453 
VAL   N    N N N 454 
VAL   CA   C N S 455 
VAL   C    C N N 456 
VAL   O    O N N 457 
VAL   CB   C N N 458 
VAL   CG1  C N N 459 
VAL   CG2  C N N 460 
VAL   OXT  O N N 461 
VAL   H    H N N 462 
VAL   H2   H N N 463 
VAL   HA   H N N 464 
VAL   HB   H N N 465 
VAL   HG11 H N N 466 
VAL   HG12 H N N 467 
VAL   HG13 H N N 468 
VAL   HG21 H N N 469 
VAL   HG22 H N N 470 
VAL   HG23 H N N 471 
VAL   HXT  H N N 472 
# 
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 
A1IS8 C10 C9   sing N N 1   
A1IS8 C10 C11  sing N N 2   
A1IS8 C9  C8   sing N N 3   
A1IS8 C11 N3   sing N N 4   
A1IS8 C6  C7   doub Y N 5   
A1IS8 C6  C5   sing Y N 6   
A1IS8 C8  C7   sing N N 7   
A1IS8 C8  C12  sing N N 8   
A1IS8 N3  C12  sing N N 9   
A1IS8 N3  C13  sing N N 10  
A1IS8 C7  N2   sing Y N 11  
A1IS8 C5  N1   doub Y N 12  
A1IS8 O   C13  doub N N 13  
A1IS8 C13 C14  sing N N 14  
A1IS8 N2  C4   doub Y N 15  
A1IS8 N1  C4   sing Y N 16  
A1IS8 C4  N    sing N N 17  
A1IS8 C14 C17  sing Y N 18  
A1IS8 C14 C15  doub Y N 19  
A1IS8 C17 C16  doub Y N 20  
A1IS8 C15 N4   sing Y N 21  
A1IS8 N   C3   sing N N 22  
A1IS8 N   C2   sing N N 23  
A1IS8 C16 N4   sing Y N 24  
A1IS8 C16 C18  sing N N 25  
A1IS8 C3  C    sing N N 26  
A1IS8 C2  C1   sing N N 27  
A1IS8 C18 N5   trip N N 28  
A1IS8 F   C    sing N N 29  
A1IS8 C   C1   sing N N 30  
A1IS8 C5  H1   sing N N 31  
A1IS8 C6  H2   sing N N 32  
A1IS8 C8  H3   sing N N 33  
A1IS8 C10 H4   sing N N 34  
A1IS8 C10 H5   sing N N 35  
A1IS8 C15 H6   sing N N 36  
A1IS8 C17 H7   sing N N 37  
A1IS8 N4  H8   sing N N 38  
A1IS8 C11 H9   sing N N 39  
A1IS8 C11 H10  sing N N 40  
A1IS8 C9  H11  sing N N 41  
A1IS8 C9  H12  sing N N 42  
A1IS8 C12 H13  sing N N 43  
A1IS8 C12 H14  sing N N 44  
A1IS8 C2  H15  sing N N 45  
A1IS8 C2  H16  sing N N 46  
A1IS8 C1  H17  sing N N 47  
A1IS8 C1  H18  sing N N 48  
A1IS8 C3  H19  sing N N 49  
A1IS8 C3  H20  sing N N 50  
A1IS8 C   H21  sing N N 51  
ALA   N   CA   sing N N 52  
ALA   N   H    sing N N 53  
ALA   N   H2   sing N N 54  
ALA   CA  C    sing N N 55  
ALA   CA  CB   sing N N 56  
ALA   CA  HA   sing N N 57  
ALA   C   O    doub N N 58  
ALA   C   OXT  sing N N 59  
ALA   CB  HB1  sing N N 60  
ALA   CB  HB2  sing N N 61  
ALA   CB  HB3  sing N N 62  
ALA   OXT HXT  sing N N 63  
ARG   N   CA   sing N N 64  
ARG   N   H    sing N N 65  
ARG   N   H2   sing N N 66  
ARG   CA  C    sing N N 67  
ARG   CA  CB   sing N N 68  
ARG   CA  HA   sing N N 69  
ARG   C   O    doub N N 70  
ARG   C   OXT  sing N N 71  
ARG   CB  CG   sing N N 72  
ARG   CB  HB2  sing N N 73  
ARG   CB  HB3  sing N N 74  
ARG   CG  CD   sing N N 75  
ARG   CG  HG2  sing N N 76  
ARG   CG  HG3  sing N N 77  
ARG   CD  NE   sing N N 78  
ARG   CD  HD2  sing N N 79  
ARG   CD  HD3  sing N N 80  
ARG   NE  CZ   sing N N 81  
ARG   NE  HE   sing N N 82  
ARG   CZ  NH1  sing N N 83  
ARG   CZ  NH2  doub N N 84  
ARG   NH1 HH11 sing N N 85  
ARG   NH1 HH12 sing N N 86  
ARG   NH2 HH21 sing N N 87  
ARG   NH2 HH22 sing N N 88  
ARG   OXT HXT  sing N N 89  
ASN   N   CA   sing N N 90  
ASN   N   H    sing N N 91  
ASN   N   H2   sing N N 92  
ASN   CA  C    sing N N 93  
ASN   CA  CB   sing N N 94  
ASN   CA  HA   sing N N 95  
ASN   C   O    doub N N 96  
ASN   C   OXT  sing N N 97  
ASN   CB  CG   sing N N 98  
ASN   CB  HB2  sing N N 99  
ASN   CB  HB3  sing N N 100 
ASN   CG  OD1  doub N N 101 
ASN   CG  ND2  sing N N 102 
ASN   ND2 HD21 sing N N 103 
ASN   ND2 HD22 sing N N 104 
ASN   OXT HXT  sing N N 105 
ASP   N   CA   sing N N 106 
ASP   N   H    sing N N 107 
ASP   N   H2   sing N N 108 
ASP   CA  C    sing N N 109 
ASP   CA  CB   sing N N 110 
ASP   CA  HA   sing N N 111 
ASP   C   O    doub N N 112 
ASP   C   OXT  sing N N 113 
ASP   CB  CG   sing N N 114 
ASP   CB  HB2  sing N N 115 
ASP   CB  HB3  sing N N 116 
ASP   CG  OD1  doub N N 117 
ASP   CG  OD2  sing N N 118 
ASP   OD2 HD2  sing N N 119 
ASP   OXT HXT  sing N N 120 
CYS   N   CA   sing N N 121 
CYS   N   H    sing N N 122 
CYS   N   H2   sing N N 123 
CYS   CA  C    sing N N 124 
CYS   CA  CB   sing N N 125 
CYS   CA  HA   sing N N 126 
CYS   C   O    doub N N 127 
CYS   C   OXT  sing N N 128 
CYS   CB  SG   sing N N 129 
CYS   CB  HB2  sing N N 130 
CYS   CB  HB3  sing N N 131 
CYS   SG  HG   sing N N 132 
CYS   OXT HXT  sing N N 133 
DMS   S   O    doub N N 134 
DMS   S   C1   sing N N 135 
DMS   S   C2   sing N N 136 
DMS   C1  H11  sing N N 137 
DMS   C1  H12  sing N N 138 
DMS   C1  H13  sing N N 139 
DMS   C2  H21  sing N N 140 
DMS   C2  H22  sing N N 141 
DMS   C2  H23  sing N N 142 
EDO   C1  O1   sing N N 143 
EDO   C1  C2   sing N N 144 
EDO   C1  H11  sing N N 145 
EDO   C1  H12  sing N N 146 
EDO   O1  HO1  sing N N 147 
EDO   C2  O2   sing N N 148 
EDO   C2  H21  sing N N 149 
EDO   C2  H22  sing N N 150 
EDO   O2  HO2  sing N N 151 
GLN   N   CA   sing N N 152 
GLN   N   H    sing N N 153 
GLN   N   H2   sing N N 154 
GLN   CA  C    sing N N 155 
GLN   CA  CB   sing N N 156 
GLN   CA  HA   sing N N 157 
GLN   C   O    doub N N 158 
GLN   C   OXT  sing N N 159 
GLN   CB  CG   sing N N 160 
GLN   CB  HB2  sing N N 161 
GLN   CB  HB3  sing N N 162 
GLN   CG  CD   sing N N 163 
GLN   CG  HG2  sing N N 164 
GLN   CG  HG3  sing N N 165 
GLN   CD  OE1  doub N N 166 
GLN   CD  NE2  sing N N 167 
GLN   NE2 HE21 sing N N 168 
GLN   NE2 HE22 sing N N 169 
GLN   OXT HXT  sing N N 170 
GLU   N   CA   sing N N 171 
GLU   N   H    sing N N 172 
GLU   N   H2   sing N N 173 
GLU   CA  C    sing N N 174 
GLU   CA  CB   sing N N 175 
GLU   CA  HA   sing N N 176 
GLU   C   O    doub N N 177 
GLU   C   OXT  sing N N 178 
GLU   CB  CG   sing N N 179 
GLU   CB  HB2  sing N N 180 
GLU   CB  HB3  sing N N 181 
GLU   CG  CD   sing N N 182 
GLU   CG  HG2  sing N N 183 
GLU   CG  HG3  sing N N 184 
GLU   CD  OE1  doub N N 185 
GLU   CD  OE2  sing N N 186 
GLU   OE2 HE2  sing N N 187 
GLU   OXT HXT  sing N N 188 
GLY   N   CA   sing N N 189 
GLY   N   H    sing N N 190 
GLY   N   H2   sing N N 191 
GLY   CA  C    sing N N 192 
GLY   CA  HA2  sing N N 193 
GLY   CA  HA3  sing N N 194 
GLY   C   O    doub N N 195 
GLY   C   OXT  sing N N 196 
GLY   OXT HXT  sing N N 197 
GOL   C1  O1   sing N N 198 
GOL   C1  C2   sing N N 199 
GOL   C1  H11  sing N N 200 
GOL   C1  H12  sing N N 201 
GOL   O1  HO1  sing N N 202 
GOL   C2  O2   sing N N 203 
GOL   C2  C3   sing N N 204 
GOL   C2  H2   sing N N 205 
GOL   O2  HO2  sing N N 206 
GOL   C3  O3   sing N N 207 
GOL   C3  H31  sing N N 208 
GOL   C3  H32  sing N N 209 
GOL   O3  HO3  sing N N 210 
HIS   N   CA   sing N N 211 
HIS   N   H    sing N N 212 
HIS   N   H2   sing N N 213 
HIS   CA  C    sing N N 214 
HIS   CA  CB   sing N N 215 
HIS   CA  HA   sing N N 216 
HIS   C   O    doub N N 217 
HIS   C   OXT  sing N N 218 
HIS   CB  CG   sing N N 219 
HIS   CB  HB2  sing N N 220 
HIS   CB  HB3  sing N N 221 
HIS   CG  ND1  sing Y N 222 
HIS   CG  CD2  doub Y N 223 
HIS   ND1 CE1  doub Y N 224 
HIS   ND1 HD1  sing N N 225 
HIS   CD2 NE2  sing Y N 226 
HIS   CD2 HD2  sing N N 227 
HIS   CE1 NE2  sing Y N 228 
HIS   CE1 HE1  sing N N 229 
HIS   NE2 HE2  sing N N 230 
HIS   OXT HXT  sing N N 231 
HOH   O   H1   sing N N 232 
HOH   O   H2   sing N N 233 
ILE   N   CA   sing N N 234 
ILE   N   H    sing N N 235 
ILE   N   H2   sing N N 236 
ILE   CA  C    sing N N 237 
ILE   CA  CB   sing N N 238 
ILE   CA  HA   sing N N 239 
ILE   C   O    doub N N 240 
ILE   C   OXT  sing N N 241 
ILE   CB  CG1  sing N N 242 
ILE   CB  CG2  sing N N 243 
ILE   CB  HB   sing N N 244 
ILE   CG1 CD1  sing N N 245 
ILE   CG1 HG12 sing N N 246 
ILE   CG1 HG13 sing N N 247 
ILE   CG2 HG21 sing N N 248 
ILE   CG2 HG22 sing N N 249 
ILE   CG2 HG23 sing N N 250 
ILE   CD1 HD11 sing N N 251 
ILE   CD1 HD12 sing N N 252 
ILE   CD1 HD13 sing N N 253 
ILE   OXT HXT  sing N N 254 
LEU   N   CA   sing N N 255 
LEU   N   H    sing N N 256 
LEU   N   H2   sing N N 257 
LEU   CA  C    sing N N 258 
LEU   CA  CB   sing N N 259 
LEU   CA  HA   sing N N 260 
LEU   C   O    doub N N 261 
LEU   C   OXT  sing N N 262 
LEU   CB  CG   sing N N 263 
LEU   CB  HB2  sing N N 264 
LEU   CB  HB3  sing N N 265 
LEU   CG  CD1  sing N N 266 
LEU   CG  CD2  sing N N 267 
LEU   CG  HG   sing N N 268 
LEU   CD1 HD11 sing N N 269 
LEU   CD1 HD12 sing N N 270 
LEU   CD1 HD13 sing N N 271 
LEU   CD2 HD21 sing N N 272 
LEU   CD2 HD22 sing N N 273 
LEU   CD2 HD23 sing N N 274 
LEU   OXT HXT  sing N N 275 
LYS   N   CA   sing N N 276 
LYS   N   H    sing N N 277 
LYS   N   H2   sing N N 278 
LYS   CA  C    sing N N 279 
LYS   CA  CB   sing N N 280 
LYS   CA  HA   sing N N 281 
LYS   C   O    doub N N 282 
LYS   C   OXT  sing N N 283 
LYS   CB  CG   sing N N 284 
LYS   CB  HB2  sing N N 285 
LYS   CB  HB3  sing N N 286 
LYS   CG  CD   sing N N 287 
LYS   CG  HG2  sing N N 288 
LYS   CG  HG3  sing N N 289 
LYS   CD  CE   sing N N 290 
LYS   CD  HD2  sing N N 291 
LYS   CD  HD3  sing N N 292 
LYS   CE  NZ   sing N N 293 
LYS   CE  HE2  sing N N 294 
LYS   CE  HE3  sing N N 295 
LYS   NZ  HZ1  sing N N 296 
LYS   NZ  HZ2  sing N N 297 
LYS   NZ  HZ3  sing N N 298 
LYS   OXT HXT  sing N N 299 
MET   N   CA   sing N N 300 
MET   N   H    sing N N 301 
MET   N   H2   sing N N 302 
MET   CA  C    sing N N 303 
MET   CA  CB   sing N N 304 
MET   CA  HA   sing N N 305 
MET   C   O    doub N N 306 
MET   C   OXT  sing N N 307 
MET   CB  CG   sing N N 308 
MET   CB  HB2  sing N N 309 
MET   CB  HB3  sing N N 310 
MET   CG  SD   sing N N 311 
MET   CG  HG2  sing N N 312 
MET   CG  HG3  sing N N 313 
MET   SD  CE   sing N N 314 
MET   CE  HE1  sing N N 315 
MET   CE  HE2  sing N N 316 
MET   CE  HE3  sing N N 317 
MET   OXT HXT  sing N N 318 
PHE   N   CA   sing N N 319 
PHE   N   H    sing N N 320 
PHE   N   H2   sing N N 321 
PHE   CA  C    sing N N 322 
PHE   CA  CB   sing N N 323 
PHE   CA  HA   sing N N 324 
PHE   C   O    doub N N 325 
PHE   C   OXT  sing N N 326 
PHE   CB  CG   sing N N 327 
PHE   CB  HB2  sing N N 328 
PHE   CB  HB3  sing N N 329 
PHE   CG  CD1  doub Y N 330 
PHE   CG  CD2  sing Y N 331 
PHE   CD1 CE1  sing Y N 332 
PHE   CD1 HD1  sing N N 333 
PHE   CD2 CE2  doub Y N 334 
PHE   CD2 HD2  sing N N 335 
PHE   CE1 CZ   doub Y N 336 
PHE   CE1 HE1  sing N N 337 
PHE   CE2 CZ   sing Y N 338 
PHE   CE2 HE2  sing N N 339 
PHE   CZ  HZ   sing N N 340 
PHE   OXT HXT  sing N N 341 
PRO   N   CA   sing N N 342 
PRO   N   CD   sing N N 343 
PRO   N   H    sing N N 344 
PRO   CA  C    sing N N 345 
PRO   CA  CB   sing N N 346 
PRO   CA  HA   sing N N 347 
PRO   C   O    doub N N 348 
PRO   C   OXT  sing N N 349 
PRO   CB  CG   sing N N 350 
PRO   CB  HB2  sing N N 351 
PRO   CB  HB3  sing N N 352 
PRO   CG  CD   sing N N 353 
PRO   CG  HG2  sing N N 354 
PRO   CG  HG3  sing N N 355 
PRO   CD  HD2  sing N N 356 
PRO   CD  HD3  sing N N 357 
PRO   OXT HXT  sing N N 358 
SER   N   CA   sing N N 359 
SER   N   H    sing N N 360 
SER   N   H2   sing N N 361 
SER   CA  C    sing N N 362 
SER   CA  CB   sing N N 363 
SER   CA  HA   sing N N 364 
SER   C   O    doub N N 365 
SER   C   OXT  sing N N 366 
SER   CB  OG   sing N N 367 
SER   CB  HB2  sing N N 368 
SER   CB  HB3  sing N N 369 
SER   OG  HG   sing N N 370 
SER   OXT HXT  sing N N 371 
THR   N   CA   sing N N 372 
THR   N   H    sing N N 373 
THR   N   H2   sing N N 374 
THR   CA  C    sing N N 375 
THR   CA  CB   sing N N 376 
THR   CA  HA   sing N N 377 
THR   C   O    doub N N 378 
THR   C   OXT  sing N N 379 
THR   CB  OG1  sing N N 380 
THR   CB  CG2  sing N N 381 
THR   CB  HB   sing N N 382 
THR   OG1 HG1  sing N N 383 
THR   CG2 HG21 sing N N 384 
THR   CG2 HG22 sing N N 385 
THR   CG2 HG23 sing N N 386 
THR   OXT HXT  sing N N 387 
TRP   N   CA   sing N N 388 
TRP   N   H    sing N N 389 
TRP   N   H2   sing N N 390 
TRP   CA  C    sing N N 391 
TRP   CA  CB   sing N N 392 
TRP   CA  HA   sing N N 393 
TRP   C   O    doub N N 394 
TRP   C   OXT  sing N N 395 
TRP   CB  CG   sing N N 396 
TRP   CB  HB2  sing N N 397 
TRP   CB  HB3  sing N N 398 
TRP   CG  CD1  doub Y N 399 
TRP   CG  CD2  sing Y N 400 
TRP   CD1 NE1  sing Y N 401 
TRP   CD1 HD1  sing N N 402 
TRP   CD2 CE2  doub Y N 403 
TRP   CD2 CE3  sing Y N 404 
TRP   NE1 CE2  sing Y N 405 
TRP   NE1 HE1  sing N N 406 
TRP   CE2 CZ2  sing Y N 407 
TRP   CE3 CZ3  doub Y N 408 
TRP   CE3 HE3  sing N N 409 
TRP   CZ2 CH2  doub Y N 410 
TRP   CZ2 HZ2  sing N N 411 
TRP   CZ3 CH2  sing Y N 412 
TRP   CZ3 HZ3  sing N N 413 
TRP   CH2 HH2  sing N N 414 
TRP   OXT HXT  sing N N 415 
TYR   N   CA   sing N N 416 
TYR   N   H    sing N N 417 
TYR   N   H2   sing N N 418 
TYR   CA  C    sing N N 419 
TYR   CA  CB   sing N N 420 
TYR   CA  HA   sing N N 421 
TYR   C   O    doub N N 422 
TYR   C   OXT  sing N N 423 
TYR   CB  CG   sing N N 424 
TYR   CB  HB2  sing N N 425 
TYR   CB  HB3  sing N N 426 
TYR   CG  CD1  doub Y N 427 
TYR   CG  CD2  sing Y N 428 
TYR   CD1 CE1  sing Y N 429 
TYR   CD1 HD1  sing N N 430 
TYR   CD2 CE2  doub Y N 431 
TYR   CD2 HD2  sing N N 432 
TYR   CE1 CZ   doub Y N 433 
TYR   CE1 HE1  sing N N 434 
TYR   CE2 CZ   sing Y N 435 
TYR   CE2 HE2  sing N N 436 
TYR   CZ  OH   sing N N 437 
TYR   OH  HH   sing N N 438 
TYR   OXT HXT  sing N N 439 
VAL   N   CA   sing N N 440 
VAL   N   H    sing N N 441 
VAL   N   H2   sing N N 442 
VAL   CA  C    sing N N 443 
VAL   CA  CB   sing N N 444 
VAL   CA  HA   sing N N 445 
VAL   C   O    doub N N 446 
VAL   C   OXT  sing N N 447 
VAL   CB  CG1  sing N N 448 
VAL   CB  CG2  sing N N 449 
VAL   CB  HB   sing N N 450 
VAL   CG1 HG11 sing N N 451 
VAL   CG1 HG12 sing N N 452 
VAL   CG1 HG13 sing N N 453 
VAL   CG2 HG21 sing N N 454 
VAL   CG2 HG22 sing N N 455 
VAL   CG2 HG23 sing N N 456 
VAL   OXT HXT  sing N N 457 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9H8C 
_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]   0.013980 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014449 
_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]   0.005944 
_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 
F 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . MET   A 1 12  ? -15.749 81.012 71.966  1.00 60.33  ? 1   MET   A N   1 
ATOM   2    C CA  . MET   A 1 12  ? -14.320 81.323 71.916  1.00 60.72  ? 1   MET   A CA  1 
ATOM   3    C C   . MET   A 1 12  ? -14.063 82.839 71.902  1.00 59.62  ? 1   MET   A C   1 
ATOM   4    O O   . MET   A 1 12  ? -14.893 83.599 71.393  1.00 59.93  ? 1   MET   A O   1 
ATOM   5    C CB  . MET   A 1 12  ? -13.683 80.664 70.690  1.00 62.53  ? 1   MET   A CB  1 
ATOM   6    C CG  . MET   A 1 12  ? -12.412 79.941 71.002  1.00 67.30  ? 1   MET   A CG  1 
ATOM   7    S SD  . MET   A 1 12  ? -12.277 78.400 70.059  1.00 80.76  ? 1   MET   A SD  1 
ATOM   8    C CE  . MET   A 1 12  ? -13.307 77.296 71.054  1.00 79.13  ? 1   MET   A CE  1 
ATOM   9    N N   . ASP   A 1 13  ? -12.923 83.285 72.462  1.00 58.09  ? 2   ASP   A N   1 
ATOM   10   C CA  . ASP   A 1 13  ? -12.598 84.707 72.475  1.00 56.96  ? 2   ASP   A CA  1 
ATOM   11   C C   . ASP   A 1 13  ? -12.294 85.135 71.046  1.00 56.20  ? 2   ASP   A C   1 
ATOM   12   O O   . ASP   A 1 13  ? -11.521 84.465 70.363  1.00 56.43  ? 2   ASP   A O   1 
ATOM   13   C CB  . ASP   A 1 13  ? -11.403 84.991 73.389  1.00 57.90  ? 2   ASP   A CB  1 
ATOM   14   C CG  . ASP   A 1 13  ? -11.006 86.454 73.451  1.00 61.31  ? 2   ASP   A CG  1 
ATOM   15   O OD1 . ASP   A 1 13  ? -11.721 87.234 74.114  1.00 62.22  ? 2   ASP   A OD1 1 
ATOM   16   O OD2 . ASP   A 1 13  ? -9.974  86.813 72.852  1.00 62.41  ? 2   ASP   A OD2 1 
ATOM   17   N N   . TYR   A 1 14  ? -12.950 86.203 70.573  1.00 55.17  ? 3   TYR   A N   1 
ATOM   18   C CA  . TYR   A 1 14  ? -12.765 86.681 69.212  1.00 54.49  ? 3   TYR   A CA  1 
ATOM   19   C C   . TYR   A 1 14  ? -11.338 87.141 68.984  1.00 53.73  ? 3   TYR   A C   1 
ATOM   20   O O   . TYR   A 1 14  ? -10.737 86.763 67.981  1.00 53.52  ? 3   TYR   A O   1 
ATOM   21   C CB  . TYR   A 1 14  ? -13.764 87.797 68.861  1.00 54.38  ? 3   TYR   A CB  1 
ATOM   22   C CG  . TYR   A 1 14  ? -13.543 88.375 67.480  1.00 55.19  ? 3   TYR   A CG  1 
ATOM   23   C CD1 . TYR   A 1 14  ? -13.985 87.707 66.348  1.00 56.18  ? 3   TYR   A CD1 1 
ATOM   24   C CD2 . TYR   A 1 14  ? -12.823 89.548 67.303  1.00 56.17  ? 3   TYR   A CD2 1 
ATOM   25   C CE1 . TYR   A 1 14  ? -13.772 88.225 65.078  1.00 57.34  ? 3   TYR   A CE1 1 
ATOM   26   C CE2 . TYR   A 1 14  ? -12.574 90.058 66.037  1.00 57.21  ? 3   TYR   A CE2 1 
ATOM   27   C CZ  . TYR   A 1 14  ? -13.064 89.402 64.926  1.00 58.48  ? 3   TYR   A CZ  1 
ATOM   28   O OH  . TYR   A 1 14  ? -12.840 89.919 63.672  1.00 60.61  ? 3   TYR   A OH  1 
ATOM   29   N N   . ASP   A 1 15  ? -10.789 87.934 69.913  1.00 53.07  ? 4   ASP   A N   1 
ATOM   30   C CA  . ASP   A 1 15  ? -9.431  88.459 69.778  1.00 52.88  ? 4   ASP   A CA  1 
ATOM   31   C C   . ASP   A 1 15  ? -8.384  87.343 69.682  1.00 51.54  ? 4   ASP   A C   1 
ATOM   32   O O   . ASP   A 1 15  ? -7.451  87.422 68.882  1.00 51.10  ? 4   ASP   A O   1 
ATOM   33   C CB  . ASP   A 1 15  ? -9.123  89.474 70.902  1.00 54.95  ? 4   ASP   A CB  1 
ATOM   34   C CG  . ASP   A 1 15  ? -10.045 90.691 70.916  1.00 60.24  ? 4   ASP   A CG  1 
ATOM   35   O OD1 . ASP   A 1 15  ? -10.936 90.779 70.036  1.00 60.75  ? 4   ASP   A OD1 1 
ATOM   36   O OD2 . ASP   A 1 15  ? -9.867  91.561 71.798  1.00 63.18  ? 4   ASP   A OD2 1 
ATOM   37   N N   . PHE   A 1 16  ? -8.594  86.282 70.449  1.00 50.77  ? 5   PHE   A N   1 
ATOM   38   C CA  . PHE   A 1 16  ? -7.747  85.099 70.458  1.00 50.43  ? 5   PHE   A CA  1 
ATOM   39   C C   . PHE   A 1 16  ? -7.920  84.334 69.143  1.00 49.38  ? 5   PHE   A C   1 
ATOM   40   O O   . PHE   A 1 16  ? -6.928  83.885 68.576  1.00 49.72  ? 5   PHE   A O   1 
ATOM   41   C CB  . PHE   A 1 16  ? -8.128  84.248 71.669  1.00 50.80  ? 5   PHE   A CB  1 
ATOM   42   C CG  . PHE   A 1 16  ? -7.706  82.803 71.710  1.00 52.08  ? 5   PHE   A CG  1 
ATOM   43   C CD1 . PHE   A 1 16  ? -6.425  82.451 72.099  1.00 53.04  ? 5   PHE   A CD1 1 
ATOM   44   C CD2 . PHE   A 1 16  ? -8.627  81.792 71.500  1.00 53.13  ? 5   PHE   A CD2 1 
ATOM   45   C CE1 . PHE   A 1 16  ? -6.068  81.117 72.233  1.00 53.80  ? 5   PHE   A CE1 1 
ATOM   46   C CE2 . PHE   A 1 16  ? -8.255  80.458 71.601  1.00 53.98  ? 5   PHE   A CE2 1 
ATOM   47   C CZ  . PHE   A 1 16  ? -6.988  80.130 71.994  1.00 53.65  ? 5   PHE   A CZ  1 
ATOM   48   N N   . LYS   A 1 17  ? -9.162  84.248 68.630  1.00 48.05  ? 6   LYS   A N   1 
ATOM   49   C CA  . LYS   A 1 17  ? -9.475  83.582 67.375  1.00 47.68  ? 6   LYS   A CA  1 
ATOM   50   C C   . LYS   A 1 17  ? -8.825  84.248 66.156  1.00 47.29  ? 6   LYS   A C   1 
ATOM   51   O O   . LYS   A 1 17  ? -8.162  83.556 65.389  1.00 47.78  ? 6   LYS   A O   1 
ATOM   52   C CB  . LYS   A 1 17  ? -10.995 83.422 67.186  1.00 49.62  ? 6   LYS   A CB  1 
ATOM   53   C CG  . LYS   A 1 17  ? -11.372 82.548 65.990  1.00 54.04  ? 6   LYS   A CG  1 
ATOM   54   C CD  . LYS   A 1 17  ? -12.852 82.651 65.592  1.00 59.15  ? 6   LYS   A CD  1 
ATOM   55   C CE  . LYS   A 1 17  ? -13.112 82.290 64.126  1.00 63.18  ? 6   LYS   A CE  1 
ATOM   56   N NZ  . LYS   A 1 17  ? -12.509 83.266 63.157  1.00 64.93  ? 6   LYS   A NZ  1 
ATOM   57   N N   . VAL   A 1 18  ? -8.979  85.573 65.980  1.00 46.64  ? 7   VAL   A N   1 
ATOM   58   C CA  . VAL   A 1 18  ? -8.367  86.279 64.842  1.00 46.50  ? 7   VAL   A CA  1 
ATOM   59   C C   . VAL   A 1 18  ? -6.834  86.281 64.886  1.00 45.80  ? 7   VAL   A C   1 
ATOM   60   O O   . VAL   A 1 18  ? -6.200  86.168 63.838  1.00 45.43  ? 7   VAL   A O   1 
ATOM   61   C CB  . VAL   A 1 18  ? -8.908  87.721 64.606  1.00 47.51  ? 7   VAL   A CB  1 
ATOM   62   C CG1 . VAL   A 1 18  ? -10.297 87.704 63.991  1.00 48.06  ? 7   VAL   A CG1 1 
ATOM   63   C CG2 . VAL   A 1 18  ? -8.870  88.569 65.871  1.00 48.09  ? 7   VAL   A CG2 1 
ATOM   64   N N   . LYS   A 1 19  ? -6.247  86.417 66.084  1.00 45.65  ? 8   LYS   A N   1 
ATOM   65   C CA  . LYS   A 1 19  ? -4.798  86.426 66.235  1.00 46.26  ? 8   LYS   A CA  1 
ATOM   66   C C   . LYS   A 1 19  ? -4.231  85.071 65.848  1.00 47.41  ? 8   LYS   A C   1 
ATOM   67   O O   . LYS   A 1 19  ? -3.271  85.028 65.078  1.00 48.07  ? 8   LYS   A O   1 
ATOM   68   C CB  . LYS   A 1 19  ? -4.387  86.887 67.654  1.00 47.37  ? 8   LYS   A CB  1 
ATOM   69   C CG  . LYS   A 1 19  ? -3.246  86.139 68.331  1.00 50.10  ? 8   LYS   A CG  1 
ATOM   70   C CD  . LYS   A 1 19  ? -2.149  87.053 68.776  1.00 54.13  ? 8   LYS   A CD  1 
ATOM   71   C CE  . LYS   A 1 19  ? -0.982  86.978 67.824  1.00 58.16  ? 8   LYS   A CE  1 
ATOM   72   N NZ  . LYS   A 1 19  ? -0.565  85.574 67.586  1.00 60.52  ? 8   LYS   A NZ  1 
ATOM   73   N N   . LEU   A 1 20  ? -4.837  83.967 66.328  1.00 47.46  ? 9   LEU   A N   1 
ATOM   74   C CA  . LEU   A 1 20  ? -4.348  82.637 65.958  1.00 48.18  ? 9   LEU   A CA  1 
ATOM   75   C C   . LEU   A 1 20  ? -4.507  82.378 64.485  1.00 49.69  ? 9   LEU   A C   1 
ATOM   76   O O   . LEU   A 1 20  ? -3.624  81.777 63.886  1.00 50.05  ? 9   LEU   A O   1 
ATOM   77   C CB  . LEU   A 1 20  ? -5.042  81.530 66.728  1.00 47.53  ? 9   LEU   A CB  1 
ATOM   78   C CG  . LEU   A 1 20  ? -4.708  81.427 68.176  1.00 47.86  ? 9   LEU   A CG  1 
ATOM   79   C CD1 . LEU   A 1 20  ? -5.552  80.379 68.792  1.00 48.50  ? 9   LEU   A CD1 1 
ATOM   80   C CD2 . LEU   A 1 20  ? -3.243  81.137 68.381  1.00 47.76  ? 9   LEU   A CD2 1 
ATOM   81   N N   . SER   A 1 21  ? -5.629  82.823 63.903  1.00 50.33  ? 10  SER   A N   1 
ATOM   82   C CA  . SER   A 1 21  ? -5.904  82.674 62.489  1.00 51.50  ? 10  SER   A CA  1 
ATOM   83   C C   . SER   A 1 21  ? -4.828  83.393 61.648  1.00 52.66  ? 10  SER   A C   1 
ATOM   84   O O   . SER   A 1 21  ? -4.366  82.850 60.642  1.00 53.06  ? 10  SER   A O   1 
ATOM   85   C CB  . SER   A 1 21  ? -7.287  83.228 62.171  1.00 52.72  ? 10  SER   A CB  1 
ATOM   86   O OG  . SER   A 1 21  ? -7.844  82.580 61.039  1.00 55.13  ? 10  SER   A OG  1 
ATOM   87   N N   . SER   A 1 22  ? -4.416  84.594 62.070  1.00 52.91  ? 11  SER   A N   1 
ATOM   88   C CA  . SER   A 1 22  ? -3.400  85.349 61.358  1.00 53.88  ? 11  SER   A CA  1 
ATOM   89   C C   . SER   A 1 22  ? -2.016  84.708 61.480  1.00 55.35  ? 11  SER   A C   1 
ATOM   90   O O   . SER   A 1 22  ? -1.229  84.779 60.536  1.00 56.13  ? 11  SER   A O   1 
ATOM   91   C CB  . SER   A 1 22  ? -3.352  86.782 61.866  1.00 54.97  ? 11  SER   A CB  1 
ATOM   92   O OG  . SER   A 1 22  ? -2.340  87.519 61.201  1.00 57.12  ? 11  SER   A OG  1 
ATOM   93   N N   . GLU   A 1 23  ? -1.705  84.115 62.627  1.00 55.62  ? 12  GLU   A N   1 
ATOM   94   C CA  . GLU   A 1 23  ? -0.413  83.476 62.815  1.00 56.74  ? 12  GLU   A CA  1 
ATOM   95   C C   . GLU   A 1 23  ? -0.353  82.124 62.078  1.00 57.33  ? 12  GLU   A C   1 
ATOM   96   O O   . GLU   A 1 23  ? 0.696   81.760 61.551  1.00 57.87  ? 12  GLU   A O   1 
ATOM   97   C CB  . GLU   A 1 23  ? -0.140  83.278 64.309  1.00 60.13  ? 12  GLU   A CB  1 
ATOM   98   C CG  . GLU   A 1 23  ? -0.077  84.569 65.092  1.00 67.70  ? 12  GLU   A CG  1 
ATOM   99   C CD  . GLU   A 1 23  ? 1.193   85.387 64.936  1.00 79.09  ? 12  GLU   A CD  1 
ATOM   100  O OE1 . GLU   A 1 23  ? 2.221   84.822 64.492  1.00 81.65  ? 12  GLU   A OE1 1 
ATOM   101  O OE2 . GLU   A 1 23  ? 1.164   86.595 65.271  1.00 82.63  ? 12  GLU   A OE2 1 
ATOM   102  N N   . ARG   A 1 24  ? -1.481  81.389 62.056  1.00 56.90  ? 13  ARG   A N   1 
ATOM   103  C CA  . ARG   A 1 24  ? -1.637  80.052 61.485  1.00 56.72  ? 13  ARG   A CA  1 
ATOM   104  C C   . ARG   A 1 24  ? -1.064  79.879 60.093  1.00 57.84  ? 13  ARG   A C   1 
ATOM   105  O O   . ARG   A 1 24  ? -1.623  80.391 59.130  1.00 58.12  ? 13  ARG   A O   1 
ATOM   106  C CB  . ARG   A 1 24  ? -3.111  79.619 61.503  1.00 56.40  ? 13  ARG   A CB  1 
ATOM   107  C CG  . ARG   A 1 24  ? -3.336  78.097 61.469  1.00 56.36  ? 13  ARG   A CG  1 
ATOM   108  C CD  . ARG   A 1 24  ? -4.275  77.600 62.563  1.00 56.12  ? 13  ARG   A CD  1 
ATOM   109  N NE  . ARG   A 1 24  ? -5.548  78.322 62.567  1.00 56.93  ? 13  ARG   A NE  1 
ATOM   110  C CZ  . ARG   A 1 24  ? -6.234  78.635 63.663  1.00 57.91  ? 13  ARG   A CZ  1 
ATOM   111  N NH1 . ARG   A 1 24  ? -5.788  78.272 64.860  1.00 56.93  ? 13  ARG   A NH1 1 
ATOM   112  N NH2 . ARG   A 1 24  ? -7.371  79.313 63.570  1.00 57.52  ? 13  ARG   A NH2 1 
ATOM   113  N N   . GLU   A 1 25  ? 0.041   79.119 59.993  1.00 58.33  ? 14  GLU   A N   1 
ATOM   114  C CA  . GLU   A 1 25  ? 0.701   78.780 58.735  1.00 58.92  ? 14  GLU   A CA  1 
ATOM   115  C C   . GLU   A 1 25  ? -0.176  77.802 57.972  1.00 58.61  ? 14  GLU   A C   1 
ATOM   116  O O   . GLU   A 1 25  ? -0.541  76.754 58.511  1.00 58.63  ? 14  GLU   A O   1 
ATOM   117  C CB  . GLU   A 1 25  ? 2.025   78.057 58.999  1.00 61.87  ? 14  GLU   A CB  1 
ATOM   118  C CG  . GLU   A 1 25  ? 3.061   78.835 59.782  1.00 68.02  ? 14  GLU   A CG  1 
ATOM   119  C CD  . GLU   A 1 25  ? 4.289   78.015 60.142  1.00 76.69  ? 14  GLU   A CD  1 
ATOM   120  O OE1 . GLU   A 1 25  ? 4.249   76.768 60.006  1.00 78.22  ? 14  GLU   A OE1 1 
ATOM   121  O OE2 . GLU   A 1 25  ? 5.297   78.625 60.566  1.00 79.75  ? 14  GLU   A OE2 1 
ATOM   122  N N   . ARG   A 1 26  ? -0.457  78.104 56.711  1.00 58.11  ? 15  ARG   A N   1 
ATOM   123  C CA  . ARG   A 1 26  ? -1.272  77.243 55.885  1.00 58.40  ? 15  ARG   A CA  1 
ATOM   124  C C   . ARG   A 1 26  ? -0.409  76.379 54.987  1.00 58.01  ? 15  ARG   A C   1 
ATOM   125  O O   . ARG   A 1 26  ? 0.552   76.888 54.421  1.00 57.90  ? 15  ARG   A O   1 
ATOM   126  C CB  . ARG   A 1 26  ? -2.258  78.087 55.089  1.00 60.63  ? 15  ARG   A CB  1 
ATOM   127  C CG  . ARG   A 1 26  ? -3.531  78.318 55.878  1.00 65.59  ? 15  ARG   A CG  1 
ATOM   128  C CD  . ARG   A 1 26  ? -4.252  79.588 55.498  1.00 70.79  ? 15  ARG   A CD  1 
ATOM   129  N NE  . ARG   A 1 26  ? -4.573  79.634 54.073  1.00 75.41  ? 15  ARG   A NE  1 
ATOM   130  C CZ  . ARG   A 1 26  ? -5.060  80.700 53.446  1.00 78.66  ? 15  ARG   A CZ  1 
ATOM   131  N NH1 . ARG   A 1 26  ? -5.312  80.651 52.143  1.00 78.72  ? 15  ARG   A NH1 1 
ATOM   132  N NH2 . ARG   A 1 26  ? -5.279  81.832 54.112  1.00 78.50  ? 15  ARG   A NH2 1 
ATOM   133  N N   . VAL   A 1 27  ? -0.731  75.062 54.874  1.00 57.65  ? 16  VAL   A N   1 
ATOM   134  C CA  . VAL   A 1 27  ? 0.038   74.115 54.060  1.00 57.66  ? 16  VAL   A CA  1 
ATOM   135  C C   . VAL   A 1 27  ? 0.077   74.552 52.594  1.00 57.97  ? 16  VAL   A C   1 
ATOM   136  O O   . VAL   A 1 27  ? 1.152   74.589 51.996  1.00 58.25  ? 16  VAL   A O   1 
ATOM   137  C CB  . VAL   A 1 27  ? -0.409  72.627 54.235  1.00 58.07  ? 16  VAL   A CB  1 
ATOM   138  C CG1 . VAL   A 1 27  ? -1.800  72.361 53.655  1.00 58.61  ? 16  VAL   A CG1 1 
ATOM   139  C CG2 . VAL   A 1 27  ? 0.614   71.659 53.644  1.00 58.13  ? 16  VAL   A CG2 1 
ATOM   140  N N   . GLU   A 1 28  ? -1.074  74.964 52.046  1.00 57.80  ? 17  GLU   A N   1 
ATOM   141  C CA  . GLU   A 1 28  ? -1.187  75.371 50.649  1.00 58.16  ? 17  GLU   A CA  1 
ATOM   142  C C   . GLU   A 1 28  ? -0.562  76.735 50.344  1.00 58.76  ? 17  GLU   A C   1 
ATOM   143  O O   . GLU   A 1 28  ? -0.381  77.072 49.180  1.00 59.44  ? 17  GLU   A O   1 
ATOM   144  C CB  . GLU   A 1 28  ? -2.641  75.304 50.173  1.00 59.63  ? 17  GLU   A CB  1 
ATOM   145  C CG  . GLU   A 1 28  ? -3.519  76.423 50.699  1.00 62.64  ? 17  GLU   A CG  1 
ATOM   146  C CD  . GLU   A 1 28  ? -4.026  76.247 52.114  1.00 65.65  ? 17  GLU   A CD  1 
ATOM   147  O OE1 . GLU   A 1 28  ? -3.953  75.115 52.642  1.00 65.41  ? 17  GLU   A OE1 1 
ATOM   148  O OE2 . GLU   A 1 28  ? -4.513  77.243 52.693  1.00 67.68  ? 17  GLU   A OE2 1 
ATOM   149  N N   . ASP   A 1 29  ? -0.237  77.517 51.366  1.00 58.36  ? 18  ASP   A N   1 
ATOM   150  C CA  . ASP   A 1 29  ? 0.448   78.791 51.184  1.00 58.28  ? 18  ASP   A CA  1 
ATOM   151  C C   . ASP   A 1 29  ? 1.959   78.595 51.278  1.00 57.99  ? 18  ASP   A C   1 
ATOM   152  O O   . ASP   A 1 29  ? 2.708   79.322 50.638  1.00 58.01  ? 18  ASP   A O   1 
ATOM   153  C CB  . ASP   A 1 29  ? 0.009   79.793 52.252  1.00 59.86  ? 18  ASP   A CB  1 
ATOM   154  C CG  . ASP   A 1 29  ? -1.377  80.356 52.046  1.00 64.50  ? 18  ASP   A CG  1 
ATOM   155  O OD1 . ASP   A 1 29  ? -1.878  80.307 50.899  1.00 65.04  ? 18  ASP   A OD1 1 
ATOM   156  O OD2 . ASP   A 1 29  ? -1.952  80.867 53.019  1.00 66.99  ? 18  ASP   A OD2 1 
ATOM   157  N N   . LEU   A 1 30  ? 2.409   77.637 52.098  1.00 57.74  ? 19  LEU   A N   1 
ATOM   158  C CA  . LEU   A 1 30  ? 3.820   77.376 52.308  1.00 58.12  ? 19  LEU   A CA  1 
ATOM   159  C C   . LEU   A 1 30  ? 4.448   76.452 51.262  1.00 58.24  ? 19  LEU   A C   1 
ATOM   160  O O   . LEU   A 1 30  ? 5.636   76.603 50.976  1.00 58.47  ? 19  LEU   A O   1 
ATOM   161  C CB  . LEU   A 1 30  ? 4.049   76.817 53.726  1.00 58.39  ? 19  LEU   A CB  1 
ATOM   162  C CG  . LEU   A 1 30  ? 4.520   77.833 54.772  1.00 59.88  ? 19  LEU   A CG  1 
ATOM   163  C CD1 . LEU   A 1 30  ? 3.370   78.373 55.564  1.00 60.24  ? 19  LEU   A CD1 1 
ATOM   164  C CD2 . LEU   A 1 30  ? 5.512   77.215 55.719  1.00 60.76  ? 19  LEU   A CD2 1 
ATOM   165  N N   . PHE   A 1 31  ? 3.672   75.517 50.677  1.00 57.79  ? 20  PHE   A N   1 
ATOM   166  C CA  . PHE   A 1 31  ? 4.247   74.560 49.734  1.00 57.91  ? 20  PHE   A CA  1 
ATOM   167  C C   . PHE   A 1 31  ? 3.533   74.392 48.388  1.00 58.03  ? 20  PHE   A C   1 
ATOM   168  O O   . PHE   A 1 31  ? 2.322   74.590 48.273  1.00 58.01  ? 20  PHE   A O   1 
ATOM   169  C CB  . PHE   A 1 31  ? 4.364   73.174 50.409  1.00 57.86  ? 20  PHE   A CB  1 
ATOM   170  C CG  . PHE   A 1 31  ? 5.241   73.135 51.639  1.00 58.41  ? 20  PHE   A CG  1 
ATOM   171  C CD1 . PHE   A 1 31  ? 6.604   72.947 51.529  1.00 59.04  ? 20  PHE   A CD1 1 
ATOM   172  C CD2 . PHE   A 1 31  ? 4.700   73.303 52.901  1.00 59.19  ? 20  PHE   A CD2 1 
ATOM   173  C CE1 . PHE   A 1 31  ? 7.409   72.930 52.660  1.00 59.77  ? 20  PHE   A CE1 1 
ATOM   174  C CE2 . PHE   A 1 31  ? 5.512   73.295 54.028  1.00 59.77  ? 20  PHE   A CE2 1 
ATOM   175  C CZ  . PHE   A 1 31  ? 6.861   73.118 53.899  1.00 59.48  ? 20  PHE   A CZ  1 
ATOM   176  N N   . GLU   A 1 32  ? 4.308   73.954 47.381  1.00 58.08  ? 21  GLU   A N   1 
ATOM   177  C CA  . GLU   A 1 32  ? 3.838   73.586 46.056  1.00 58.95  ? 21  GLU   A CA  1 
ATOM   178  C C   . GLU   A 1 32  ? 3.866   72.066 46.002  1.00 59.50  ? 21  GLU   A C   1 
ATOM   179  O O   . GLU   A 1 32  ? 4.939   71.464 46.072  1.00 59.47  ? 21  GLU   A O   1 
ATOM   180  C CB  . GLU   A 1 32  ? 4.759   74.121 44.970  1.00 61.52  ? 21  GLU   A CB  1 
ATOM   181  C CG  . GLU   A 1 32  ? 4.106   74.041 43.604  1.00 65.78  ? 21  GLU   A CG  1 
ATOM   182  C CD  . GLU   A 1 32  ? 2.957   75.018 43.478  1.00 70.09  ? 21  GLU   A CD  1 
ATOM   183  O OE1 . GLU   A 1 32  ? 3.203   76.234 43.645  1.00 71.57  ? 21  GLU   A OE1 1 
ATOM   184  O OE2 . GLU   A 1 32  ? 1.811   74.571 43.241  1.00 70.72  ? 21  GLU   A OE2 1 
ATOM   185  N N   . TYR   A 1 33  ? 2.692   71.440 45.901  1.00 59.71  ? 22  TYR   A N   1 
ATOM   186  C CA  . TYR   A 1 33  ? 2.589   69.986 45.924  1.00 60.27  ? 22  TYR   A CA  1 
ATOM   187  C C   . TYR   A 1 33  ? 1.485   69.440 45.032  1.00 61.29  ? 22  TYR   A C   1 
ATOM   188  O O   . TYR   A 1 33  ? 1.430   68.227 44.854  1.00 61.45  ? 22  TYR   A O   1 
ATOM   189  C CB  . TYR   A 1 33  ? 2.336   69.512 47.364  1.00 60.14  ? 22  TYR   A CB  1 
ATOM   190  C CG  . TYR   A 1 33  ? 1.102   70.126 48.007  1.00 60.72  ? 22  TYR   A CG  1 
ATOM   191  C CD1 . TYR   A 1 33  ? -0.147  69.533 47.872  1.00 61.48  ? 22  TYR   A CD1 1 
ATOM   192  C CD2 . TYR   A 1 33  ? 1.194   71.271 48.788  1.00 61.31  ? 22  TYR   A CD2 1 
ATOM   193  C CE1 . TYR   A 1 33  ? -1.278  70.094 48.448  1.00 62.25  ? 22  TYR   A CE1 1 
ATOM   194  C CE2 . TYR   A 1 33  ? 0.075   71.821 49.397  1.00 62.13  ? 22  TYR   A CE2 1 
ATOM   195  C CZ  . TYR   A 1 33  ? -1.161  71.228 49.228  1.00 63.14  ? 22  TYR   A CZ  1 
ATOM   196  O OH  . TYR   A 1 33  ? -2.279  71.769 49.824  1.00 64.79  ? 22  TYR   A OH  1 
ATOM   197  N N   . GLU   A 1 34  ? 0.568   70.295 44.526  1.00 61.90  ? 23  GLU   A N   1 
ATOM   198  C CA  . GLU   A 1 34  ? -0.548  69.815 43.701  1.00 62.85  ? 23  GLU   A CA  1 
ATOM   199  C C   . GLU   A 1 34  ? -0.094  69.159 42.408  1.00 62.54  ? 23  GLU   A C   1 
ATOM   200  O O   . GLU   A 1 34  ? 0.677   69.733 41.643  1.00 62.90  ? 23  GLU   A O   1 
ATOM   201  C CB  . GLU   A 1 34  ? -1.576  70.913 43.437  1.00 66.19  ? 23  GLU   A CB  1 
ATOM   202  C CG  . GLU   A 1 34  ? -2.852  70.740 44.239  1.00 72.55  ? 23  GLU   A CG  1 
ATOM   203  C CD  . GLU   A 1 34  ? -3.895  71.788 43.905  1.00 80.70  ? 23  GLU   A CD  1 
ATOM   204  O OE1 . GLU   A 1 34  ? -4.547  71.663 42.841  1.00 81.65  ? 23  GLU   A OE1 1 
ATOM   205  O OE2 . GLU   A 1 34  ? -4.047  72.745 44.701  1.00 83.90  ? 23  GLU   A OE2 1 
ATOM   206  N N   . GLY   A 1 35  ? -0.550  67.938 42.201  1.00 61.66  ? 24  GLY   A N   1 
ATOM   207  C CA  . GLY   A 1 35  ? -0.136  67.151 41.051  1.00 61.46  ? 24  GLY   A CA  1 
ATOM   208  C C   . GLY   A 1 35  ? 1.040   66.244 41.368  1.00 60.79  ? 24  GLY   A C   1 
ATOM   209  O O   . GLY   A 1 35  ? 1.208   65.195 40.739  1.00 60.81  ? 24  GLY   A O   1 
ATOM   210  N N   . CYS   A 1 36  ? 1.850   66.620 42.374  1.00 59.86  ? 25  CYS   A N   1 
ATOM   211  C CA  . CYS   A 1 36  ? 3.023   65.856 42.772  1.00 59.14  ? 25  CYS   A CA  1 
ATOM   212  C C   . CYS   A 1 36  ? 2.726   64.795 43.842  1.00 58.90  ? 25  CYS   A C   1 
ATOM   213  O O   . CYS   A 1 36  ? 3.457   64.728 44.829  1.00 59.87  ? 25  CYS   A O   1 
ATOM   214  C CB  . CYS   A 1 36  ? 4.169   66.777 43.196  1.00 59.19  ? 25  CYS   A CB  1 
ATOM   215  S SG  . CYS   A 1 36  ? 4.127   68.428 42.453  1.00 60.91  ? 25  CYS   A SG  1 
ATOM   216  N N   . LYS   A 1 37  ? 1.705   63.930 43.647  1.00 57.44  ? 26  LYS   A N   1 
ATOM   217  C CA  . LYS   A 1 37  ? 1.420   62.881 44.634  1.00 56.44  ? 26  LYS   A CA  1 
ATOM   218  C C   . LYS   A 1 37  ? 2.239   61.621 44.326  1.00 55.90  ? 26  LYS   A C   1 
ATOM   219  O O   . LYS   A 1 37  ? 2.102   61.059 43.253  1.00 56.23  ? 26  LYS   A O   1 
ATOM   220  C CB  . LYS   A 1 37  ? -0.080  62.569 44.695  1.00 57.45  ? 26  LYS   A CB  1 
ATOM   221  C CG  . LYS   A 1 37  ? -0.455  61.618 45.831  1.00 60.43  ? 26  LYS   A CG  1 
ATOM   222  C CD  . LYS   A 1 37  ? -1.891  61.080 45.732  1.00 63.85  ? 26  LYS   A CD  1 
ATOM   223  C CE  . LYS   A 1 37  ? -2.941  62.171 45.732  1.00 66.73  ? 26  LYS   A CE  1 
ATOM   224  N NZ  . LYS   A 1 37  ? -4.306  61.628 45.958  1.00 68.39  ? 26  LYS   A NZ  1 
ATOM   225  N N   . VAL   A 1 38  ? 3.090   61.177 45.252  1.00 55.01  ? 27  VAL   A N   1 
ATOM   226  C CA  . VAL   A 1 38  ? 3.924   59.986 45.040  1.00 54.43  ? 27  VAL   A CA  1 
ATOM   227  C C   . VAL   A 1 38  ? 3.387   58.702 45.724  1.00 54.40  ? 27  VAL   A C   1 
ATOM   228  O O   . VAL   A 1 38  ? 3.891   57.607 45.471  1.00 54.55  ? 27  VAL   A O   1 
ATOM   229  C CB  . VAL   A 1 38  ? 5.374   60.277 45.470  1.00 54.72  ? 27  VAL   A CB  1 
ATOM   230  C CG1 . VAL   A 1 38  ? 5.964   61.409 44.641  1.00 55.51  ? 27  VAL   A CG1 1 
ATOM   231  C CG2 . VAL   A 1 38  ? 5.442   60.611 46.958  1.00 54.81  ? 27  VAL   A CG2 1 
ATOM   232  N N   . GLY   A 1 39  ? 2.408   58.848 46.607  1.00 53.96  ? 28  GLY   A N   1 
ATOM   233  C CA  . GLY   A 1 39  ? 1.844   57.723 47.332  1.00 53.91  ? 28  GLY   A CA  1 
ATOM   234  C C   . GLY   A 1 39  ? 0.408   57.941 47.751  1.00 53.98  ? 28  GLY   A C   1 
ATOM   235  O O   . GLY   A 1 39  ? -0.017  59.068 48.023  1.00 53.78  ? 28  GLY   A O   1 
ATOM   236  N N   . ARG   A 1 40  ? -0.344  56.846 47.824  1.00 54.21  ? 29  ARG   A N   1 
ATOM   237  C CA  . ARG   A 1 40  ? -1.746  56.878 48.220  1.00 54.96  ? 29  ARG   A CA  1 
ATOM   238  C C   . ARG   A 1 40  ? -2.112  55.557 48.895  1.00 55.31  ? 29  ARG   A C   1 
ATOM   239  O O   . ARG   A 1 40  ? -1.821  54.487 48.357  1.00 55.73  ? 29  ARG   A O   1 
ATOM   240  C CB  . ARG   A 1 40  ? -2.629  57.150 46.993  1.00 56.45  ? 29  ARG   A CB  1 
ATOM   241  C CG  . ARG   A 1 40  ? -4.121  56.979 47.227  1.00 60.07  ? 29  ARG   A CG  1 
ATOM   242  C CD  . ARG   A 1 40  ? -4.699  57.930 48.253  1.00 63.97  ? 29  ARG   A CD  1 
ATOM   243  N NE  . ARG   A 1 40  ? -5.993  57.435 48.721  1.00 67.52  ? 29  ARG   A NE  1 
ATOM   244  C CZ  . ARG   A 1 40  ? -6.637  57.890 49.788  1.00 69.78  ? 29  ARG   A CZ  1 
ATOM   245  N NH1 . ARG   A 1 40  ? -6.111  58.859 50.527  1.00 69.58  ? 29  ARG   A NH1 1 
ATOM   246  N NH2 . ARG   A 1 40  ? -7.803  57.367 50.138  1.00 70.01  ? 29  ARG   A NH2 1 
ATOM   247  N N   . GLY   A 1 41  ? -2.705  55.638 50.077  1.00 54.98  ? 30  GLY   A N   1 
ATOM   248  C CA  . GLY   A 1 41  ? -3.105  54.450 50.818  1.00 55.39  ? 30  GLY   A CA  1 
ATOM   249  C C   . GLY   A 1 41  ? -3.957  54.774 52.024  1.00 55.82  ? 30  GLY   A C   1 
ATOM   250  O O   . GLY   A 1 41  ? -4.515  55.875 52.109  1.00 56.17  ? 30  GLY   A O   1 
ATOM   251  N N   . THR   A 1 42  ? -4.045  53.827 52.979  1.00 55.66  ? 31  THR   A N   1 
ATOM   252  C CA  . THR   A 1 42  ? -4.819  53.983 54.225  1.00 55.91  ? 31  THR   A CA  1 
ATOM   253  C C   . THR   A 1 42  ? -4.314  55.135 55.081  1.00 55.59  ? 31  THR   A C   1 
ATOM   254  O O   . THR   A 1 42  ? -5.076  55.705 55.851  1.00 56.00  ? 31  THR   A O   1 
ATOM   255  C CB  . THR   A 1 42  ? -4.729  52.716 55.053  1.00 57.72  ? 31  THR   A CB  1 
ATOM   256  O OG1 . THR   A 1 42  ? -3.343  52.461 55.306  1.00 59.55  ? 31  THR   A OG1 1 
ATOM   257  C CG2 . THR   A 1 42  ? -5.371  51.525 54.364  1.00 57.93  ? 31  THR   A CG2 1 
ATOM   258  N N   . TYR   A 1 43  ? -3.013  55.429 54.989  1.00 54.92  ? 32  TYR   A N   1 
ATOM   259  C CA  . TYR   A 1 43  ? -2.332  56.536 55.665  1.00 54.44  ? 32  TYR   A CA  1 
ATOM   260  C C   . TYR   A 1 43  ? -2.722  57.910 55.093  1.00 55.29  ? 32  TYR   A C   1 
ATOM   261  O O   . TYR   A 1 43  ? -2.448  58.928 55.726  1.00 55.95  ? 32  TYR   A O   1 
ATOM   262  C CB  . TYR   A 1 43  ? -0.810  56.363 55.537  1.00 53.42  ? 32  TYR   A CB  1 
ATOM   263  C CG  . TYR   A 1 43  ? -0.328  56.196 54.110  1.00 52.53  ? 32  TYR   A CG  1 
ATOM   264  C CD1 . TYR   A 1 43  ? -0.270  54.942 53.517  1.00 52.48  ? 32  TYR   A CD1 1 
ATOM   265  C CD2 . TYR   A 1 43  ? 0.099   57.287 53.366  1.00 52.73  ? 32  TYR   A CD2 1 
ATOM   266  C CE1 . TYR   A 1 43  ? 0.160   54.783 52.208  1.00 52.92  ? 32  TYR   A CE1 1 
ATOM   267  C CE2 . TYR   A 1 43  ? 0.529   57.140 52.055  1.00 53.38  ? 32  TYR   A CE2 1 
ATOM   268  C CZ  . TYR   A 1 43  ? 0.555   55.884 51.476  1.00 53.97  ? 32  TYR   A CZ  1 
ATOM   269  O OH  . TYR   A 1 43  ? 1.013   55.728 50.191  1.00 55.18  ? 32  TYR   A OH  1 
ATOM   270  N N   . GLY   A 1 44  ? -3.291  57.941 53.892  1.00 55.23  ? 33  GLY   A N   1 
ATOM   271  C CA  . GLY   A 1 44  ? -3.676  59.184 53.246  1.00 55.77  ? 33  GLY   A CA  1 
ATOM   272  C C   . GLY   A 1 44  ? -2.947  59.425 51.943  1.00 55.98  ? 33  GLY   A C   1 
ATOM   273  O O   . GLY   A 1 44  ? -2.793  58.508 51.131  1.00 56.49  ? 33  GLY   A O   1 
ATOM   274  N N   . HIS   A 1 45  ? -2.482  60.659 51.736  1.00 55.35  ? 34  HIS   A N   1 
ATOM   275  C CA  . HIS   A 1 45  ? -1.815  61.028 50.492  1.00 55.16  ? 34  HIS   A CA  1 
ATOM   276  C C   . HIS   A 1 45  ? -0.444  61.601 50.778  1.00 54.46  ? 34  HIS   A C   1 
ATOM   277  O O   . HIS   A 1 45  ? -0.327  62.490 51.602  1.00 54.25  ? 34  HIS   A O   1 
ATOM   278  C CB  . HIS   A 1 45  ? -2.635  62.098 49.740  1.00 56.27  ? 34  HIS   A CB  1 
ATOM   279  C CG  . HIS   A 1 45  ? -4.124  61.921 49.802  1.00 59.45  ? 34  HIS   A CG  1 
ATOM   280  N ND1 . HIS   A 1 45  ? -4.842  61.460 48.713  1.00 61.75  ? 34  HIS   A ND1 1 
ATOM   281  C CD2 . HIS   A 1 45  ? -4.981  62.157 50.823  1.00 60.72  ? 34  HIS   A CD2 1 
ATOM   282  C CE1 . HIS   A 1 45  ? -6.106  61.429 49.106  1.00 62.31  ? 34  HIS   A CE1 1 
ATOM   283  N NE2 . HIS   A 1 45  ? -6.238  61.837 50.370  1.00 61.96  ? 34  HIS   A NE2 1 
ATOM   284  N N   . VAL   A 1 46  ? 0.587   61.129 50.080  1.00 54.08  ? 35  VAL   A N   1 
ATOM   285  C CA  . VAL   A 1 46  ? 1.937   61.674 50.235  1.00 53.81  ? 35  VAL   A CA  1 
ATOM   286  C C   . VAL   A 1 46  ? 2.306   62.439 48.950  1.00 53.79  ? 35  VAL   A C   1 
ATOM   287  O O   . VAL   A 1 46  ? 1.993   61.997 47.844  1.00 53.77  ? 35  VAL   A O   1 
ATOM   288  C CB  . VAL   A 1 46  ? 2.986   60.602 50.632  1.00 53.83  ? 35  VAL   A CB  1 
ATOM   289  C CG1 . VAL   A 1 46  ? 4.385   61.193 50.700  1.00 53.98  ? 35  VAL   A CG1 1 
ATOM   290  C CG2 . VAL   A 1 46  ? 2.627   59.976 51.965  1.00 54.21  ? 35  VAL   A CG2 1 
ATOM   291  N N   . TYR   A 1 47  ? 2.920   63.615 49.108  1.00 53.38  ? 36  TYR   A N   1 
ATOM   292  C CA  . TYR   A 1 47  ? 3.310   64.477 48.008  1.00 53.19  ? 36  TYR   A CA  1 
ATOM   293  C C   . TYR   A 1 47  ? 4.786   64.818 48.085  1.00 52.98  ? 36  TYR   A C   1 
ATOM   294  O O   . TYR   A 1 47  ? 5.343   64.902 49.172  1.00 52.76  ? 36  TYR   A O   1 
ATOM   295  C CB  . TYR   A 1 47  ? 2.525   65.800 48.084  1.00 53.40  ? 36  TYR   A CB  1 
ATOM   296  C CG  . TYR   A 1 47  ? 1.019   65.658 48.066  1.00 54.68  ? 36  TYR   A CG  1 
ATOM   297  C CD1 . TYR   A 1 47  ? 0.308   65.431 49.237  1.00 55.86  ? 36  TYR   A CD1 1 
ATOM   298  C CD2 . TYR   A 1 47  ? 0.297   65.836 46.893  1.00 55.54  ? 36  TYR   A CD2 1 
ATOM   299  C CE1 . TYR   A 1 47  ? -1.073  65.300 49.227  1.00 56.94  ? 36  TYR   A CE1 1 
ATOM   300  C CE2 . TYR   A 1 47  ? -1.086  65.728 46.875  1.00 56.57  ? 36  TYR   A CE2 1 
ATOM   301  C CZ  . TYR   A 1 47  ? -1.770  65.454 48.044  1.00 57.95  ? 36  TYR   A CZ  1 
ATOM   302  O OH  . TYR   A 1 47  ? -3.142  65.343 48.044  1.00 60.07  ? 36  TYR   A OH  1 
ATOM   303  N N   . LYS   A 1 48  ? 5.406   65.085 46.937  1.00 53.17  ? 37  LYS   A N   1 
ATOM   304  C CA  . LYS   A 1 48  ? 6.773   65.589 46.859  1.00 54.02  ? 37  LYS   A CA  1 
ATOM   305  C C   . LYS   A 1 48  ? 6.540   67.101 46.763  1.00 55.78  ? 37  LYS   A C   1 
ATOM   306  O O   . LYS   A 1 48  ? 5.964   67.579 45.781  1.00 56.26  ? 37  LYS   A O   1 
ATOM   307  C CB  . LYS   A 1 48  ? 7.471   65.067 45.590  1.00 54.85  ? 37  LYS   A CB  1 
ATOM   308  C CG  . LYS   A 1 48  ? 8.941   65.458 45.461  1.00 57.13  ? 37  LYS   A CG  1 
ATOM   309  C CD  . LYS   A 1 48  ? 9.368   65.454 43.995  1.00 60.51  ? 37  LYS   A CD  1 
ATOM   310  C CE  . LYS   A 1 48  ? 10.862  65.372 43.782  1.00 63.91  ? 37  LYS   A CE  1 
ATOM   311  N NZ  . LYS   A 1 48  ? 11.204  64.986 42.379  1.00 65.72  ? 37  LYS   A NZ  1 
ATOM   312  N N   . ALA   A 1 49  ? 6.881   67.839 47.817  1.00 56.56  ? 38  ALA   A N   1 
ATOM   313  C CA  . ALA   A 1 49  ? 6.618   69.266 47.896  1.00 57.85  ? 38  ALA   A CA  1 
ATOM   314  C C   . ALA   A 1 49  ? 7.883   70.152 47.778  1.00 59.40  ? 38  ALA   A C   1 
ATOM   315  O O   . ALA   A 1 49  ? 9.003   69.676 47.935  1.00 59.74  ? 38  ALA   A O   1 
ATOM   316  C CB  . ALA   A 1 49  ? 5.847   69.567 49.178  1.00 57.78  ? 38  ALA   A CB  1 
ATOM   317  N N   . LYS   A 1 50  ? 7.691   71.428 47.437  1.00 60.20  ? 39  LYS   A N   1 
ATOM   318  C CA  . LYS   A 1 50  ? 8.748   72.430 47.300  1.00 61.35  ? 39  LYS   A CA  1 
ATOM   319  C C   . LYS   A 1 50  ? 8.271   73.717 47.986  1.00 61.73  ? 39  LYS   A C   1 
ATOM   320  O O   . LYS   A 1 50  ? 7.102   74.065 47.870  1.00 61.40  ? 39  LYS   A O   1 
ATOM   321  C CB  . LYS   A 1 50  ? 9.031   72.703 45.807  1.00 63.63  ? 39  LYS   A CB  1 
ATOM   322  C CG  . LYS   A 1 50  ? 10.164  71.872 45.206  1.00 67.61  ? 39  LYS   A CG  1 
ATOM   323  C CD  . LYS   A 1 50  ? 11.530  72.522 45.453  1.00 71.38  ? 39  LYS   A CD  1 
ATOM   324  C CE  . LYS   A 1 50  ? 12.559  72.115 44.424  1.00 74.62  ? 39  LYS   A CE  1 
ATOM   325  N NZ  . LYS   A 1 50  ? 12.340  70.725 43.944  1.00 76.61  ? 39  LYS   A NZ  1 
ATOM   326  N N   . ARG   A 1 51  ? 9.157   74.418 48.694  1.00 62.53  ? 40  ARG   A N   1 
ATOM   327  C CA  . ARG   A 1 51  ? 8.780   75.646 49.401  1.00 64.12  ? 40  ARG   A CA  1 
ATOM   328  C C   . ARG   A 1 51  ? 8.458   76.826 48.478  1.00 64.83  ? 40  ARG   A C   1 
ATOM   329  O O   . ARG   A 1 51  ? 9.240   77.150 47.580  1.00 65.13  ? 40  ARG   A O   1 
ATOM   330  C CB  . ARG   A 1 51  ? 9.860   76.051 50.406  1.00 66.46  ? 40  ARG   A CB  1 
ATOM   331  C CG  . ARG   A 1 51  ? 10.239  74.930 51.339  1.00 71.41  ? 40  ARG   A CG  1 
ATOM   332  C CD  . ARG   A 1 51  ? 10.100  75.381 52.767  1.00 76.47  ? 40  ARG   A CD  1 
ATOM   333  N NE  . ARG   A 1 51  ? 11.210  76.248 53.143  1.00 80.89  ? 40  ARG   A NE  1 
ATOM   334  C CZ  . ARG   A 1 51  ? 11.114  77.268 53.985  1.00 84.47  ? 40  ARG   A CZ  1 
ATOM   335  N NH1 . ARG   A 1 51  ? 12.182  78.002 54.271  1.00 85.28  ? 40  ARG   A NH1 1 
ATOM   336  N NH2 . ARG   A 1 51  ? 9.942   77.582 54.531  1.00 84.34  ? 40  ARG   A NH2 1 
ATOM   337  N N   . LYS   A 1 52  ? 7.319   77.491 48.728  1.00 64.89  ? 41  LYS   A N   1 
ATOM   338  C CA  . LYS   A 1 52  ? 6.884   78.644 47.945  1.00 65.43  ? 41  LYS   A CA  1 
ATOM   339  C C   . LYS   A 1 52  ? 7.802   79.852 48.120  1.00 67.02  ? 41  LYS   A C   1 
ATOM   340  O O   . LYS   A 1 52  ? 7.879   80.689 47.222  1.00 67.18  ? 41  LYS   A O   1 
ATOM   341  C CB  . LYS   A 1 52  ? 5.457   79.031 48.333  1.00 65.83  ? 41  LYS   A CB  1 
ATOM   342  C CG  . LYS   A 1 52  ? 4.441   77.963 48.011  1.00 68.28  ? 41  LYS   A CG  1 
ATOM   343  C CD  . LYS   A 1 52  ? 3.898   78.102 46.616  1.00 71.18  ? 41  LYS   A CD  1 
ATOM   344  C CE  . LYS   A 1 52  ? 2.403   78.265 46.658  1.00 73.88  ? 41  LYS   A CE  1 
ATOM   345  N NZ  . LYS   A 1 52  ? 1.770   77.200 47.464  1.00 75.38  ? 41  LYS   A NZ  1 
ATOM   346  N N   . ASP   A 1 53  ? 8.477   79.964 49.278  1.00 68.08  ? 42  ASP   A N   1 
ATOM   347  C CA  . ASP   A 1 53  ? 9.359   81.099 49.559  1.00 69.47  ? 42  ASP   A CA  1 
ATOM   348  C C   . ASP   A 1 53  ? 10.752  81.003 48.917  1.00 70.56  ? 42  ASP   A C   1 
ATOM   349  O O   . ASP   A 1 53  ? 11.477  81.989 48.900  1.00 70.62  ? 42  ASP   A O   1 
ATOM   350  C CB  . ASP   A 1 53  ? 9.467   81.353 51.066  1.00 71.13  ? 42  ASP   A CB  1 
ATOM   351  C CG  . ASP   A 1 53  ? 9.809   80.135 51.882  1.00 74.96  ? 42  ASP   A CG  1 
ATOM   352  O OD1 . ASP   A 1 53  ? 10.618  79.309 51.402  1.00 75.86  ? 42  ASP   A OD1 1 
ATOM   353  O OD2 . ASP   A 1 53  ? 9.286   80.017 53.010  1.00 76.52  ? 42  ASP   A OD2 1 
ATOM   354  N N   . GLY   A 1 54  ? 11.117  79.829 48.417  1.00 71.40  ? 43  GLY   A N   1 
ATOM   355  C CA  . GLY   A 1 54  ? 12.374  79.620 47.709  1.00 72.71  ? 43  GLY   A CA  1 
ATOM   356  C C   . GLY   A 1 54  ? 13.663  79.718 48.501  1.00 73.68  ? 43  GLY   A C   1 
ATOM   357  O O   . GLY   A 1 54  ? 14.745  79.498 47.943  1.00 73.96  ? 43  GLY   A O   1 
ATOM   358  N N   . LYS   A 1 55  ? 13.577  80.029 49.800  1.00 73.87  ? 44  LYS   A N   1 
ATOM   359  C CA  . LYS   A 1 55  ? 14.769  80.107 50.645  1.00 74.70  ? 44  LYS   A CA  1 
ATOM   360  C C   . LYS   A 1 55  ? 15.149  78.699 51.124  1.00 75.19  ? 44  LYS   A C   1 
ATOM   361  O O   . LYS   A 1 55  ? 15.361  78.488 52.321  1.00 75.58  ? 44  LYS   A O   1 
ATOM   362  C CB  . LYS   A 1 55  ? 14.552  81.066 51.841  1.00 76.93  ? 44  LYS   A CB  1 
ATOM   363  C CG  . LYS   A 1 55  ? 13.099  81.222 52.303  1.00 80.79  ? 44  LYS   A CG  1 
ATOM   364  C CD  . LYS   A 1 55  ? 12.975  81.458 53.803  1.00 84.72  ? 44  LYS   A CD  1 
ATOM   365  C CE  . LYS   A 1 55  ? 11.953  82.520 54.138  1.00 87.83  ? 44  LYS   A CE  1 
ATOM   366  N NZ  . LYS   A 1 55  ? 12.445  83.883 53.802  1.00 89.59  ? 44  LYS   A NZ  1 
ATOM   367  N N   . ASP   A 1 56  ? 15.223  77.730 50.187  1.00 74.92  ? 45  ASP   A N   1 
ATOM   368  C CA  . ASP   A 1 56  ? 15.504  76.343 50.525  1.00 74.89  ? 45  ASP   A CA  1 
ATOM   369  C C   . ASP   A 1 56  ? 16.004  75.493 49.342  1.00 74.35  ? 45  ASP   A C   1 
ATOM   370  O O   . ASP   A 1 56  ? 17.131  74.992 49.408  1.00 74.56  ? 45  ASP   A O   1 
ATOM   371  C CB  . ASP   A 1 56  ? 14.248  75.706 51.149  1.00 76.96  ? 45  ASP   A CB  1 
ATOM   372  C CG  . ASP   A 1 56  ? 14.516  74.779 52.310  1.00 81.91  ? 45  ASP   A CG  1 
ATOM   373  O OD1 . ASP   A 1 56  ? 15.185  75.212 53.281  1.00 82.57  ? 45  ASP   A OD1 1 
ATOM   374  O OD2 . ASP   A 1 56  ? 14.028  73.643 52.274  1.00 84.22  ? 45  ASP   A OD2 1 
ATOM   375  N N   . ASP   A 1 57  ? 15.158  75.299 48.286  1.00 73.43  ? 46  ASP   A N   1 
ATOM   376  C CA  . ASP   A 1 57  ? 15.408  74.437 47.108  1.00 72.92  ? 46  ASP   A CA  1 
ATOM   377  C C   . ASP   A 1 57  ? 15.336  72.910 47.443  1.00 70.95  ? 46  ASP   A C   1 
ATOM   378  O O   . ASP   A 1 57  ? 15.475  72.071 46.551  1.00 71.08  ? 46  ASP   A O   1 
ATOM   379  C CB  . ASP   A 1 57  ? 16.722  74.804 46.373  1.00 75.82  ? 46  ASP   A CB  1 
ATOM   380  C CG  . ASP   A 1 57  ? 17.111  73.872 45.231  1.00 82.35  ? 46  ASP   A CG  1 
ATOM   381  O OD1 . ASP   A 1 57  ? 16.205  73.448 44.471  1.00 83.41  ? 46  ASP   A OD1 1 
ATOM   382  O OD2 . ASP   A 1 57  ? 18.314  73.539 45.118  1.00 85.28  ? 46  ASP   A OD2 1 
ATOM   383  N N   . LYS   A 1 58  ? 15.086  72.559 48.706  1.00 68.93  ? 47  LYS   A N   1 
ATOM   384  C CA  . LYS   A 1 58  ? 15.011  71.168 49.120  1.00 67.40  ? 47  LYS   A CA  1 
ATOM   385  C C   . LYS   A 1 58  ? 13.671  70.532 48.746  1.00 65.36  ? 47  LYS   A C   1 
ATOM   386  O O   . LYS   A 1 58  ? 12.694  71.234 48.484  1.00 65.36  ? 47  LYS   A O   1 
ATOM   387  C CB  . LYS   A 1 58  ? 15.275  71.062 50.629  1.00 69.32  ? 47  LYS   A CB  1 
ATOM   388  C CG  . LYS   A 1 58  ? 16.571  71.740 51.061  1.00 73.84  ? 47  LYS   A CG  1 
ATOM   389  C CD  . LYS   A 1 58  ? 16.728  71.761 52.576  1.00 78.90  ? 47  LYS   A CD  1 
ATOM   390  C CE  . LYS   A 1 58  ? 16.981  70.391 53.149  1.00 83.25  ? 47  LYS   A CE  1 
ATOM   391  N NZ  . LYS   A 1 58  ? 16.258  70.184 54.431  1.00 85.54  ? 47  LYS   A NZ  1 
ATOM   392  N N   . ASP   A 1 59  ? 13.634  69.197 48.710  1.00 63.54  ? 48  ASP   A N   1 
ATOM   393  C CA  . ASP   A 1 59  ? 12.419  68.437 48.427  1.00 62.14  ? 48  ASP   A CA  1 
ATOM   394  C C   . ASP   A 1 59  ? 11.847  67.910 49.747  1.00 60.06  ? 48  ASP   A C   1 
ATOM   395  O O   . ASP   A 1 59  ? 12.601  67.446 50.607  1.00 60.16  ? 48  ASP   A O   1 
ATOM   396  C CB  . ASP   A 1 59  ? 12.709  67.272 47.462  1.00 63.96  ? 48  ASP   A CB  1 
ATOM   397  C CG  . ASP   A 1 59  ? 12.710  67.661 45.996  1.00 68.90  ? 48  ASP   A CG  1 
ATOM   398  O OD1 . ASP   A 1 59  ? 12.007  68.631 45.638  1.00 70.17  ? 48  ASP   A OD1 1 
ATOM   399  O OD2 . ASP   A 1 59  ? 13.399  66.990 45.207  1.00 70.93  ? 48  ASP   A OD2 1 
ATOM   400  N N   . TYR   A 1 60  ? 10.521  67.974 49.912  1.00 58.01  ? 49  TYR   A N   1 
ATOM   401  C CA  . TYR   A 1 60  ? 9.875   67.511 51.141  1.00 56.24  ? 49  TYR   A CA  1 
ATOM   402  C C   . TYR   A 1 60  ? 8.797   66.495 50.866  1.00 54.35  ? 49  TYR   A C   1 
ATOM   403  O O   . TYR   A 1 60  ? 8.200   66.511 49.807  1.00 54.53  ? 49  TYR   A O   1 
ATOM   404  C CB  . TYR   A 1 60  ? 9.219   68.692 51.861  1.00 56.11  ? 49  TYR   A CB  1 
ATOM   405  C CG  . TYR   A 1 60  ? 10.201  69.652 52.485  1.00 56.70  ? 49  TYR   A CG  1 
ATOM   406  C CD1 . TYR   A 1 60  ? 10.627  70.778 51.802  1.00 57.40  ? 49  TYR   A CD1 1 
ATOM   407  C CD2 . TYR   A 1 60  ? 10.700  69.436 53.762  1.00 57.65  ? 49  TYR   A CD2 1 
ATOM   408  C CE1 . TYR   A 1 60  ? 11.535  71.660 52.367  1.00 58.54  ? 49  TYR   A CE1 1 
ATOM   409  C CE2 . TYR   A 1 60  ? 11.603  70.314 54.342  1.00 58.64  ? 49  TYR   A CE2 1 
ATOM   410  C CZ  . TYR   A 1 60  ? 12.021  71.430 53.642  1.00 59.72  ? 49  TYR   A CZ  1 
ATOM   411  O OH  . TYR   A 1 60  ? 12.909  72.318 54.219  1.00 61.18  ? 49  TYR   A OH  1 
ATOM   412  N N   . ALA   A 1 61  ? 8.540   65.612 51.815  1.00 52.58  ? 50  ALA   A N   1 
ATOM   413  C CA  . ALA   A 1 61  ? 7.436   64.677 51.729  1.00 51.51  ? 50  ALA   A CA  1 
ATOM   414  C C   . ALA   A 1 61  ? 6.340   65.330 52.559  1.00 50.89  ? 50  ALA   A C   1 
ATOM   415  O O   . ALA   A 1 61  ? 6.564   65.701 53.710  1.00 50.95  ? 50  ALA   A O   1 
ATOM   416  C CB  . ALA   A 1 61  ? 7.822   63.347 52.323  1.00 51.38  ? 50  ALA   A CB  1 
ATOM   417  N N   . LEU   A 1 62  ? 5.183   65.555 51.957  1.00 50.29  ? 51  LEU   A N   1 
ATOM   418  C CA  . LEU   A 1 62  ? 4.067   66.225 52.625  1.00 50.21  ? 51  LEU   A CA  1 
ATOM   419  C C   . LEU   A 1 62  ? 2.907   65.239 52.681  1.00 49.81  ? 51  LEU   A C   1 
ATOM   420  O O   . LEU   A 1 62  ? 2.442   64.822 51.627  1.00 50.23  ? 51  LEU   A O   1 
ATOM   421  C CB  . LEU   A 1 62  ? 3.672   67.450 51.771  1.00 50.34  ? 51  LEU   A CB  1 
ATOM   422  C CG  . LEU   A 1 62  ? 3.081   68.671 52.464  1.00 51.60  ? 51  LEU   A CG  1 
ATOM   423  C CD1 . LEU   A 1 62  ? 3.964   69.147 53.594  1.00 52.58  ? 51  LEU   A CD1 1 
ATOM   424  C CD2 . LEU   A 1 62  ? 2.937   69.797 51.488  1.00 51.77  ? 51  LEU   A CD2 1 
ATOM   425  N N   . LYS   A 1 63  ? 2.444   64.859 53.877  1.00 48.91  ? 52  LYS   A N   1 
ATOM   426  C CA  . LYS   A 1 63  ? 1.361   63.893 53.970  1.00 49.06  ? 52  LYS   A CA  1 
ATOM   427  C C   . LYS   A 1 63  ? 0.044   64.442 54.504  1.00 49.62  ? 52  LYS   A C   1 
ATOM   428  O O   . LYS   A 1 63  ? 0.004   64.885 55.634  1.00 49.78  ? 52  LYS   A O   1 
ATOM   429  C CB  . LYS   A 1 63  ? 1.798   62.664 54.794  1.00 50.22  ? 52  LYS   A CB  1 
ATOM   430  C CG  . LYS   A 1 63  ? 0.730   61.575 54.880  1.00 52.64  ? 52  LYS   A CG  1 
ATOM   431  C CD  . LYS   A 1 63  ? 1.250   60.270 55.455  1.00 55.74  ? 52  LYS   A CD  1 
ATOM   432  C CE  . LYS   A 1 63  ? 1.669   60.368 56.896  1.00 58.05  ? 52  LYS   A CE  1 
ATOM   433  N NZ  . LYS   A 1 63  ? 1.933   59.021 57.449  1.00 59.39  ? 52  LYS   A NZ  1 
ATOM   434  N N   . GLN   A 1 64  ? -1.051  64.334 53.732  1.00 50.09  ? 53  GLN   A N   1 
ATOM   435  C CA  . GLN   A 1 64  ? -2.373  64.679 54.245  1.00 51.23  ? 53  GLN   A CA  1 
ATOM   436  C C   . GLN   A 1 64  ? -2.901  63.363 54.809  1.00 52.41  ? 53  GLN   A C   1 
ATOM   437  O O   . GLN   A 1 64  ? -2.999  62.378 54.070  1.00 52.30  ? 53  GLN   A O   1 
ATOM   438  C CB  . GLN   A 1 64  ? -3.324  65.190 53.152  1.00 52.85  ? 53  GLN   A CB  1 
ATOM   439  C CG  . GLN   A 1 64  ? -4.682  65.639 53.713  1.00 56.77  ? 53  GLN   A CG  1 
ATOM   440  C CD  . GLN   A 1 64  ? -5.785  65.707 52.670  1.00 63.23  ? 53  GLN   A CD  1 
ATOM   441  O OE1 . GLN   A 1 64  ? -6.228  64.694 52.122  1.00 65.03  ? 53  GLN   A OE1 1 
ATOM   442  N NE2 . GLN   A 1 64  ? -6.284  66.906 52.385  1.00 65.15  ? 53  GLN   A NE2 1 
ATOM   443  N N   . ILE   A 1 65  ? -3.203  63.328 56.120  1.00 53.14  ? 54  ILE   A N   1 
ATOM   444  C CA  . ILE   A 1 65  ? -3.690  62.119 56.774  1.00 54.16  ? 54  ILE   A CA  1 
ATOM   445  C C   . ILE   A 1 65  ? -5.108  61.769 56.328  1.00 54.97  ? 54  ILE   A C   1 
ATOM   446  O O   . ILE   A 1 65  ? -5.916  62.667 56.085  1.00 55.54  ? 54  ILE   A O   1 
ATOM   447  C CB  . ILE   A 1 65  ? -3.554  62.234 58.314  1.00 54.88  ? 54  ILE   A CB  1 
ATOM   448  C CG1 . ILE   A 1 65  ? -2.096  62.559 58.704  1.00 55.92  ? 54  ILE   A CG1 1 
ATOM   449  C CG2 . ILE   A 1 65  ? -4.033  60.956 59.009  1.00 55.51  ? 54  ILE   A CG2 1 
ATOM   450  C CD1 . ILE   A 1 65  ? -1.879  62.834 60.163  1.00 57.24  ? 54  ILE   A CD1 1 
ATOM   451  N N   . GLU   A 1 66  ? -5.393  60.467 56.182  1.00 54.86  ? 55  GLU   A N   1 
ATOM   452  C CA  . GLU   A 1 66  ? -6.697  59.963 55.767  1.00 55.39  ? 55  GLU   A CA  1 
ATOM   453  C C   . GLU   A 1 66  ? -7.806  60.390 56.733  1.00 55.60  ? 55  GLU   A C   1 
ATOM   454  O O   . GLU   A 1 66  ? -7.636  60.283 57.950  1.00 55.68  ? 55  GLU   A O   1 
ATOM   455  C CB  . GLU   A 1 66  ? -6.647  58.433 55.684  1.00 57.87  ? 55  GLU   A CB  1 
ATOM   456  C CG  . GLU   A 1 66  ? -7.961  57.777 55.297  1.00 63.68  ? 55  GLU   A CG  1 
ATOM   457  C CD  . GLU   A 1 66  ? -8.322  57.968 53.838  1.00 70.90  ? 55  GLU   A CD  1 
ATOM   458  O OE1 . GLU   A 1 66  ? -7.511  57.557 52.977  1.00 72.92  ? 55  GLU   A OE1 1 
ATOM   459  O OE2 . GLU   A 1 66  ? -9.401  58.539 53.553  1.00 72.52  ? 55  GLU   A OE2 1 
ATOM   460  N N   . GLY   A 1 67  ? -8.915  60.881 56.173  1.00 55.57  ? 56  GLY   A N   1 
ATOM   461  C CA  . GLY   A 1 67  ? -10.095 61.296 56.921  1.00 56.06  ? 56  GLY   A CA  1 
ATOM   462  C C   . GLY   A 1 67  ? -9.989  62.652 57.584  1.00 56.34  ? 56  GLY   A C   1 
ATOM   463  O O   . GLY   A 1 67  ? -8.920  63.267 57.579  1.00 56.64  ? 56  GLY   A O   1 
ATOM   464  N N   . THR   A 1 68  ? -11.085 63.123 58.183  1.00 56.19  ? 57  THR   A N   1 
ATOM   465  C CA  . THR   A 1 68  ? -11.070 64.412 58.870  1.00 56.78  ? 57  THR   A CA  1 
ATOM   466  C C   . THR   A 1 68  ? -10.963 64.247 60.393  1.00 56.26  ? 57  THR   A C   1 
ATOM   467  O O   . THR   A 1 68  ? -11.472 63.286 60.961  1.00 56.65  ? 57  THR   A O   1 
ATOM   468  C CB  . THR   A 1 68  ? -12.254 65.277 58.424  1.00 58.86  ? 57  THR   A CB  1 
ATOM   469  O OG1 . THR   A 1 68  ? -13.475 64.666 58.841  1.00 60.33  ? 57  THR   A OG1 1 
ATOM   470  C CG2 . THR   A 1 68  ? -12.271 65.480 56.919  1.00 59.34  ? 57  THR   A CG2 1 
ATOM   471  N N   . GLY   A 1 69  ? -10.277 65.179 61.031  1.00 55.38  ? 58  GLY   A N   1 
ATOM   472  C CA  . GLY   A 1 69  ? -10.083 65.179 62.471  1.00 55.07  ? 58  GLY   A CA  1 
ATOM   473  C C   . GLY   A 1 69  ? -8.891  64.370 62.928  1.00 54.27  ? 58  GLY   A C   1 
ATOM   474  O O   . GLY   A 1 69  ? -8.131  63.856 62.105  1.00 54.30  ? 58  GLY   A O   1 
ATOM   475  N N   . ILE   A 1 70  ? -8.708  64.270 64.252  1.00 53.45  ? 59  ILE   A N   1 
ATOM   476  C CA  . ILE   A 1 70  ? -7.604  63.497 64.799  1.00 53.26  ? 59  ILE   A CA  1 
ATOM   477  C C   . ILE   A 1 70  ? -8.069  62.073 65.043  1.00 53.28  ? 59  ILE   A C   1 
ATOM   478  O O   . ILE   A 1 70  ? -8.688  61.771 66.064  1.00 53.49  ? 59  ILE   A O   1 
ATOM   479  C CB  . ILE   A 1 70  ? -6.926  64.161 66.027  1.00 53.67  ? 59  ILE   A CB  1 
ATOM   480  C CG1 . ILE   A 1 70  ? -6.200  65.425 65.598  1.00 55.01  ? 59  ILE   A CG1 1 
ATOM   481  C CG2 . ILE   A 1 70  ? -5.929  63.230 66.710  1.00 53.97  ? 59  ILE   A CG2 1 
ATOM   482  C CD1 . ILE   A 1 70  ? -6.901  66.660 65.930  1.00 56.69  ? 59  ILE   A CD1 1 
ATOM   483  N N   . SER   A 1 71  ? -7.825  61.203 64.057  1.00 52.72  ? 60  SER   A N   1 
ATOM   484  C CA  . SER   A 1 71  ? -8.178  59.794 64.152  1.00 52.67  ? 60  SER   A CA  1 
ATOM   485  C C   . SER   A 1 71  ? -7.229  59.110 65.134  1.00 52.37  ? 60  SER   A C   1 
ATOM   486  O O   . SER   A 1 71  ? -6.208  59.694 65.494  1.00 52.65  ? 60  SER   A O   1 
ATOM   487  C CB  . SER   A 1 71  ? -8.036  59.141 62.779  1.00 54.36  ? 60  SER   A CB  1 
ATOM   488  O OG  . SER   A 1 71  ? -6.766  59.385 62.190  1.00 56.46  ? 60  SER   A OG  1 
ATOM   489  N N   . MET   A 1 72  ? -7.499  57.853 65.528  1.00 51.71  ? 61  MET   A N   1 
ATOM   490  C CA  . MET   A 1 72  ? -6.570  57.117 66.390  1.00 51.73  ? 61  MET   A CA  1 
ATOM   491  C C   . MET   A 1 72  ? -5.199  56.992 65.702  1.00 51.53  ? 61  MET   A C   1 
ATOM   492  O O   . MET   A 1 72  ? -4.163  57.248 66.310  1.00 51.52  ? 61  MET   A O   1 
ATOM   493  C CB  . MET   A 1 72  ? -7.131  55.734 66.687  1.00 52.72  ? 61  MET   A CB  1 
ATOM   494  C CG  . MET   A 1 72  ? -8.329  55.785 67.559  1.00 55.38  ? 61  MET   A CG  1 
ATOM   495  S SD  . MET   A 1 72  ? -7.837  56.181 69.229  1.00 59.37  ? 61  MET   A SD  1 
ATOM   496  C CE  . MET   A 1 72  ? -7.378  54.519 69.811  1.00 56.84  ? 61  MET   A CE  1 
ATOM   497  N N   . SER   A 1 73  ? -5.232  56.691 64.404  1.00 51.18  ? 62  SER   A N   1 
ATOM   498  C CA  . SER   A 1 73  ? -4.080  56.567 63.542  1.00 51.19  ? 62  SER   A CA  1 
ATOM   499  C C   . SER   A 1 73  ? -3.292  57.882 63.500  1.00 50.07  ? 62  SER   A C   1 
ATOM   500  O O   . SER   A 1 73  ? -2.093  57.859 63.752  1.00 50.35  ? 62  SER   A O   1 
ATOM   501  C CB  . SER   A 1 73  ? -4.536  56.135 62.149  1.00 53.82  ? 62  SER   A CB  1 
ATOM   502  O OG  . SER   A 1 73  ? -3.596  56.413 61.121  1.00 57.73  ? 62  SER   A OG  1 
ATOM   503  N N   . ALA   A 1 74  ? -3.954  59.020 63.205  1.00 48.75  ? 63  ALA   A N   1 
ATOM   504  C CA  . ALA   A 1 74  ? -3.288  60.330 63.151  1.00 47.93  ? 63  ALA   A CA  1 
ATOM   505  C C   . ALA   A 1 74  ? -2.723  60.734 64.497  1.00 47.27  ? 63  ALA   A C   1 
ATOM   506  O O   . ALA   A 1 74  ? -1.655  61.331 64.578  1.00 47.42  ? 63  ALA   A O   1 
ATOM   507  C CB  . ALA   A 1 74  ? -4.251  61.397 62.665  1.00 47.86  ? 63  ALA   A CB  1 
ATOM   508  N N   . CYS   A 1 75  ? -3.441  60.391 65.553  1.00 46.56  ? 64  CYS   A N   1 
ATOM   509  C CA  . CYS   A 1 75  ? -3.099  60.660 66.930  1.00 46.21  ? 64  CYS   A CA  1 
ATOM   510  C C   . CYS   A 1 75  ? -1.800  59.963 67.270  1.00 44.65  ? 64  CYS   A C   1 
ATOM   511  O O   . CYS   A 1 75  ? -0.895  60.604 67.771  1.00 44.11  ? 64  CYS   A O   1 
ATOM   512  C CB  . CYS   A 1 75  ? -4.238  60.185 67.823  1.00 47.68  ? 64  CYS   A CB  1 
ATOM   513  S SG  . CYS   A 1 75  ? -4.265  60.950 69.448  1.00 53.25  ? 64  CYS   A SG  1 
ATOM   514  N N   . ARG   A 1 76  ? -1.698  58.667 66.919  1.00 43.99  ? 65  ARG   A N   1 
ATOM   515  C CA  . ARG   A 1 76  ? -0.550  57.806 67.169  1.00 43.65  ? 65  ARG   A CA  1 
ATOM   516  C C   . ARG   A 1 76  ? 0.661   58.278 66.446  1.00 43.17  ? 65  ARG   A C   1 
ATOM   517  O O   . ARG   A 1 76  ? 1.735   58.298 67.049  1.00 43.42  ? 65  ARG   A O   1 
ATOM   518  C CB  . ARG   A 1 76  ? -0.836  56.344 66.766  1.00 44.98  ? 65  ARG   A CB  1 
ATOM   519  C CG  . ARG   A 1 76  ? 0.299   55.393 67.146  1.00 46.93  ? 65  ARG   A CG  1 
ATOM   520  C CD  . ARG   A 1 76  ? 0.037   53.937 66.828  1.00 49.25  ? 65  ARG   A CD  1 
ATOM   521  N NE  . ARG   A 1 76  ? 0.982   53.085 67.557  1.00 50.85  ? 65  ARG   A NE  1 
ATOM   522  C CZ  . ARG   A 1 76  ? 1.989   52.421 66.998  1.00 50.55  ? 65  ARG   A CZ  1 
ATOM   523  N NH1 . ARG   A 1 76  ? 2.169   52.455 65.678  1.00 48.46  ? 65  ARG   A NH1 1 
ATOM   524  N NH2 . ARG   A 1 76  ? 2.810   51.696 67.751  1.00 49.20  ? 65  ARG   A NH2 1 
ATOM   525  N N   . GLU   A 1 77  ? 0.517   58.646 65.156  1.00 42.38  ? 66  GLU   A N   1 
ATOM   526  C CA  . GLU   A 1 77  ? 1.676   59.094 64.396  1.00 41.92  ? 66  GLU   A CA  1 
ATOM   527  C C   . GLU   A 1 77  ? 2.204   60.404 64.904  1.00 41.16  ? 66  GLU   A C   1 
ATOM   528  O O   . GLU   A 1 77  ? 3.412   60.550 65.058  1.00 41.41  ? 66  GLU   A O   1 
ATOM   529  C CB  . GLU   A 1 77  ? 1.423   59.163 62.894  1.00 43.88  ? 66  GLU   A CB  1 
ATOM   530  C CG  . GLU   A 1 77  ? 2.728   58.893 62.179  1.00 49.44  ? 66  GLU   A CG  1 
ATOM   531  C CD  . GLU   A 1 77  ? 2.701   58.965 60.673  1.00 58.18  ? 66  GLU   A CD  1 
ATOM   532  O OE1 . GLU   A 1 77  ? 1.589   59.084 60.113  1.00 61.20  ? 66  GLU   A OE1 1 
ATOM   533  O OE2 . GLU   A 1 77  ? 3.786   58.868 60.049  1.00 60.54  ? 66  GLU   A OE2 1 
ATOM   534  N N   . ILE   A 1 78  ? 1.309   61.344 65.205  1.00 40.15  ? 67  ILE   A N   1 
ATOM   535  C CA  . ILE   A 1 78  ? 1.716   62.639 65.725  1.00 39.67  ? 67  ILE   A CA  1 
ATOM   536  C C   . ILE   A 1 78  ? 2.355   62.474 67.100  1.00 40.18  ? 67  ILE   A C   1 
ATOM   537  O O   . ILE   A 1 78  ? 3.446   62.993 67.318  1.00 41.09  ? 67  ILE   A O   1 
ATOM   538  C CB  . ILE   A 1 78  ? 0.532   63.641 65.729  1.00 39.21  ? 67  ILE   A CB  1 
ATOM   539  C CG1 . ILE   A 1 78  ? 0.162   64.051 64.296  1.00 39.47  ? 67  ILE   A CG1 1 
ATOM   540  C CG2 . ILE   A 1 78  ? 0.830   64.866 66.596  1.00 39.37  ? 67  ILE   A CG2 1 
ATOM   541  C CD1 . ILE   A 1 78  ? -1.107  64.778 64.188  1.00 40.38  ? 67  ILE   A CD1 1 
ATOM   542  N N   . ALA   A 1 79  ? 1.713   61.726 68.004  1.00 39.33  ? 68  ALA   A N   1 
ATOM   543  C CA  . ALA   A 1 79  ? 2.243   61.566 69.350  1.00 39.32  ? 68  ALA   A CA  1 
ATOM   544  C C   . ALA   A 1 79  ? 3.601   60.898 69.359  1.00 39.57  ? 68  ALA   A C   1 
ATOM   545  O O   . ALA   A 1 79  ? 4.490   61.368 70.059  1.00 39.98  ? 68  ALA   A O   1 
ATOM   546  C CB  . ALA   A 1 79  ? 1.262   60.818 70.239  1.00 39.06  ? 68  ALA   A CB  1 
ATOM   547  N N   . LEU   A 1 80  ? 3.784   59.840 68.561  1.00 39.25  ? 69  LEU   A N   1 
ATOM   548  C CA  . LEU   A 1 80  ? 5.055   59.124 68.541  1.00 39.28  ? 69  LEU   A CA  1 
ATOM   549  C C   . LEU   A 1 80  ? 6.173   59.871 67.801  1.00 40.08  ? 69  LEU   A C   1 
ATOM   550  O O   . LEU   A 1 80  ? 7.272   60.034 68.349  1.00 40.28  ? 69  LEU   A O   1 
ATOM   551  C CB  . LEU   A 1 80  ? 4.883   57.705 68.001  1.00 38.82  ? 69  LEU   A CB  1 
ATOM   552  C CG  . LEU   A 1 80  ? 4.129   56.731 68.915  1.00 39.43  ? 69  LEU   A CG  1 
ATOM   553  C CD1 . LEU   A 1 80  ? 3.934   55.380 68.240  1.00 39.32  ? 69  LEU   A CD1 1 
ATOM   554  C CD2 . LEU   A 1 80  ? 4.843   56.555 70.239  1.00 39.64  ? 69  LEU   A CD2 1 
ATOM   555  N N   . LEU   A 1 81  ? 5.890   60.359 66.584  1.00 40.03  ? 70  LEU   A N   1 
ATOM   556  C CA  . LEU   A 1 81  ? 6.895   61.083 65.795  1.00 40.36  ? 70  LEU   A CA  1 
ATOM   557  C C   . LEU   A 1 81  ? 7.427   62.333 66.475  1.00 40.78  ? 70  LEU   A C   1 
ATOM   558  O O   . LEU   A 1 81  ? 8.545   62.764 66.197  1.00 41.19  ? 70  LEU   A O   1 
ATOM   559  C CB  . LEU   A 1 81  ? 6.349   61.458 64.415  1.00 40.22  ? 70  LEU   A CB  1 
ATOM   560  C CG  . LEU   A 1 81  ? 6.290   60.338 63.401  1.00 40.71  ? 70  LEU   A CG  1 
ATOM   561  C CD1 . LEU   A 1 81  ? 5.659   60.824 62.143  1.00 40.79  ? 70  LEU   A CD1 1 
ATOM   562  C CD2 . LEU   A 1 81  ? 7.676   59.796 63.110  1.00 41.10  ? 70  LEU   A CD2 1 
ATOM   563  N N   . ARG   A 1 82  ? 6.612   62.924 67.337  1.00 40.34  ? 71  ARG   A N   1 
ATOM   564  C CA  . ARG   A 1 82  ? 6.932   64.108 68.107  1.00 40.22  ? 71  ARG   A CA  1 
ATOM   565  C C   . ARG   A 1 82  ? 8.036   63.822 69.146  1.00 40.17  ? 71  ARG   A C   1 
ATOM   566  O O   . ARG   A 1 82  ? 8.803   64.715 69.501  1.00 40.16  ? 71  ARG   A O   1 
ATOM   567  C CB  . ARG   A 1 82  ? 5.639   64.551 68.797  1.00 41.54  ? 71  ARG   A CB  1 
ATOM   568  C CG  . ARG   A 1 82  ? 5.662   65.911 69.419  1.00 45.30  ? 71  ARG   A CG  1 
ATOM   569  C CD  . ARG   A 1 82  ? 6.005   67.008 68.433  1.00 48.93  ? 71  ARG   A CD  1 
ATOM   570  N NE  . ARG   A 1 82  ? 6.102   68.296 69.111  1.00 52.64  ? 71  ARG   A NE  1 
ATOM   571  C CZ  . ARG   A 1 82  ? 7.171   68.721 69.777  1.00 55.31  ? 71  ARG   A CZ  1 
ATOM   572  N NH1 . ARG   A 1 82  ? 7.162   69.906 70.366  1.00 54.87  ? 71  ARG   A NH1 1 
ATOM   573  N NH2 . ARG   A 1 82  ? 8.257   67.960 69.862  1.00 55.66  ? 71  ARG   A NH2 1 
ATOM   574  N N   . GLU   A 1 83  ? 8.126   62.574 69.616  1.00 40.08  ? 72  GLU   A N   1 
ATOM   575  C CA  . GLU   A 1 83  ? 9.085   62.177 70.629  1.00 40.45  ? 72  GLU   A CA  1 
ATOM   576  C C   . GLU   A 1 83  ? 10.271  61.412 70.059  1.00 41.11  ? 72  GLU   A C   1 
ATOM   577  O O   . GLU   A 1 83  ? 11.330  61.410 70.678  1.00 41.39  ? 72  GLU   A O   1 
ATOM   578  C CB  . GLU   A 1 83  ? 8.395   61.283 71.673  1.00 41.90  ? 72  GLU   A CB  1 
ATOM   579  C CG  . GLU   A 1 83  ? 7.050   61.779 72.159  1.00 44.81  ? 72  GLU   A CG  1 
ATOM   580  C CD  . GLU   A 1 83  ? 7.094   63.001 73.053  1.00 48.43  ? 72  GLU   A CD  1 
ATOM   581  O OE1 . GLU   A 1 83  ? 7.861   62.983 74.042  1.00 50.31  ? 72  GLU   A OE1 1 
ATOM   582  O OE2 . GLU   A 1 83  ? 6.342   63.966 72.782  1.00 48.08  ? 72  GLU   A OE2 1 
ATOM   583  N N   . LEU   A 1 84  ? 10.088  60.698 68.942  1.00 41.28  ? 73  LEU   A N   1 
ATOM   584  C CA  . LEU   A 1 84  ? 11.161  59.869 68.395  1.00 41.75  ? 73  LEU   A CA  1 
ATOM   585  C C   . LEU   A 1 84  ? 12.256  60.656 67.659  1.00 42.02  ? 73  LEU   A C   1 
ATOM   586  O O   . LEU   A 1 84  ? 11.958  61.480 66.797  1.00 42.02  ? 73  LEU   A O   1 
ATOM   587  C CB  . LEU   A 1 84  ? 10.588  58.758 67.505  1.00 41.96  ? 73  LEU   A CB  1 
ATOM   588  C CG  . LEU   A 1 84  ? 9.632   57.787 68.194  1.00 43.54  ? 73  LEU   A CG  1 
ATOM   589  C CD1 . LEU   A 1 84  ? 8.702   57.134 67.196  1.00 44.22  ? 73  LEU   A CD1 1 
ATOM   590  C CD2 . LEU   A 1 84  ? 10.382  56.717 68.961  1.00 44.09  ? 73  LEU   A CD2 1 
ATOM   591  N N   . LYS   A 1 85  ? 13.531  60.377 67.999  1.00 41.90  ? 74  LYS   A N   1 
ATOM   592  C CA  . LYS   A 1 85  ? 14.718  60.970 67.375  1.00 41.96  ? 74  LYS   A CA  1 
ATOM   593  C C   . LYS   A 1 85  ? 15.779  59.884 67.107  1.00 41.30  ? 74  LYS   A C   1 
ATOM   594  O O   . LYS   A 1 85  ? 16.540  59.518 67.999  1.00 41.30  ? 74  LYS   A O   1 
ATOM   595  C CB  . LYS   A 1 85  ? 15.311  62.116 68.223  1.00 44.10  ? 74  LYS   A CB  1 
ATOM   596  C CG  . LYS   A 1 85  ? 16.470  62.868 67.541  1.00 49.01  ? 74  LYS   A CG  1 
ATOM   597  C CD  . LYS   A 1 85  ? 17.014  64.055 68.370  1.00 55.24  ? 74  LYS   A CD  1 
ATOM   598  C CE  . LYS   A 1 85  ? 16.906  65.405 67.646  1.00 60.24  ? 74  LYS   A CE  1 
ATOM   599  N NZ  . LYS   A 1 85  ? 17.244  66.591 68.513  1.00 61.70  ? 74  LYS   A NZ  1 
ATOM   600  N N   . HIS   A 1 86  ? 15.827  59.381 65.872  1.00 40.60  ? 75  HIS   A N   1 
ATOM   601  C CA  . HIS   A 1 86  ? 16.798  58.375 65.453  1.00 40.53  ? 75  HIS   A CA  1 
ATOM   602  C C   . HIS   A 1 86  ? 17.110  58.570 63.980  1.00 40.20  ? 75  HIS   A C   1 
ATOM   603  O O   . HIS   A 1 86  ? 16.205  58.853 63.204  1.00 40.05  ? 75  HIS   A O   1 
ATOM   604  C CB  . HIS   A 1 86  ? 16.264  56.949 65.688  1.00 41.37  ? 75  HIS   A CB  1 
ATOM   605  C CG  . HIS   A 1 86  ? 17.322  55.903 65.543  1.00 43.63  ? 75  HIS   A CG  1 
ATOM   606  N ND1 . HIS   A 1 86  ? 17.607  55.334 64.315  1.00 45.55  ? 75  HIS   A ND1 1 
ATOM   607  C CD2 . HIS   A 1 86  ? 18.201  55.427 66.457  1.00 44.67  ? 75  HIS   A CD2 1 
ATOM   608  C CE1 . HIS   A 1 86  ? 18.633  54.524 64.521  1.00 46.04  ? 75  HIS   A CE1 1 
ATOM   609  N NE2 . HIS   A 1 86  ? 19.021  54.538 65.797  1.00 45.73  ? 75  HIS   A NE2 1 
ATOM   610  N N   . PRO   A 1 87  ? 18.380  58.417 63.556  1.00 40.22  ? 76  PRO   A N   1 
ATOM   611  C CA  . PRO   A 1 87  ? 18.710  58.617 62.128  1.00 40.13  ? 76  PRO   A CA  1 
ATOM   612  C C   . PRO   A 1 87  ? 18.027  57.643 61.149  1.00 39.71  ? 76  PRO   A C   1 
ATOM   613  O O   . PRO   A 1 87  ? 17.901  57.940 59.957  1.00 39.54  ? 76  PRO   A O   1 
ATOM   614  C CB  . PRO   A 1 87  ? 20.235  58.462 62.095  1.00 40.65  ? 76  PRO   A CB  1 
ATOM   615  C CG  . PRO   A 1 87  ? 20.565  57.684 63.324  1.00 41.09  ? 76  PRO   A CG  1 
ATOM   616  C CD  . PRO   A 1 87  ? 19.590  58.128 64.351  1.00 39.65  ? 76  PRO   A CD  1 
ATOM   617  N N   . ASN   A 1 88  ? 17.570  56.488 61.655  1.00 38.78  ? 77  ASN   A N   1 
ATOM   618  C CA  . ASN   A 1 88  ? 16.899  55.506 60.820  1.00 38.18  ? 77  ASN   A CA  1 
ATOM   619  C C   . ASN   A 1 88  ? 15.365  55.517 60.963  1.00 37.84  ? 77  ASN   A C   1 
ATOM   620  O O   . ASN   A 1 88  ? 14.708  54.591 60.506  1.00 38.01  ? 77  ASN   A O   1 
ATOM   621  C CB  . ASN   A 1 88  ? 17.483  54.109 61.021  1.00 38.53  ? 77  ASN   A CB  1 
ATOM   622  C CG  . ASN   A 1 88  ? 18.850  53.956 60.384  1.00 40.02  ? 77  ASN   A CG  1 
ATOM   623  O OD1 . ASN   A 1 88  ? 19.794  53.447 60.989  1.00 41.39  ? 77  ASN   A OD1 1 
ATOM   624  N ND2 . ASN   A 1 88  ? 18.998  54.409 59.158  1.00 39.01  ? 77  ASN   A ND2 1 
ATOM   625  N N   . VAL   A 1 89  ? 14.789  56.575 61.547  1.00 37.30  ? 78  VAL   A N   1 
ATOM   626  C CA  . VAL   A 1 89  ? 13.335  56.736 61.664  1.00 37.15  ? 78  VAL   A CA  1 
ATOM   627  C C   . VAL   A 1 89  ? 13.018  58.115 61.057  1.00 37.37  ? 78  VAL   A C   1 
ATOM   628  O O   . VAL   A 1 89  ? 13.640  59.108 61.452  1.00 37.50  ? 78  VAL   A O   1 
ATOM   629  C CB  . VAL   A 1 89  ? 12.809  56.633 63.127  1.00 37.31  ? 78  VAL   A CB  1 
ATOM   630  C CG1 . VAL   A 1 89  ? 11.288  56.715 63.164  1.00 37.73  ? 78  VAL   A CG1 1 
ATOM   631  C CG2 . VAL   A 1 89  ? 13.295  55.363 63.822  1.00 37.37  ? 78  VAL   A CG2 1 
ATOM   632  N N   . ILE   A 1 90  ? 12.066  58.193 60.097  1.00 37.22  ? 79  ILE   A N   1 
ATOM   633  C CA  . ILE   A 1 90  ? 11.708  59.464 59.458  1.00 37.64  ? 79  ILE   A CA  1 
ATOM   634  C C   . ILE   A 1 90  ? 11.388  60.567 60.481  1.00 39.73  ? 79  ILE   A C   1 
ATOM   635  O O   . ILE   A 1 90  ? 10.731  60.295 61.479  1.00 40.53  ? 79  ILE   A O   1 
ATOM   636  C CB  . ILE   A 1 90  ? 10.586  59.294 58.415  1.00 36.69  ? 79  ILE   A CB  1 
ATOM   637  C CG1 . ILE   A 1 90  ? 10.569  60.476 57.403  1.00 37.25  ? 79  ILE   A CG1 1 
ATOM   638  C CG2 . ILE   A 1 90  ? 9.234   59.097 59.080  1.00 36.41  ? 79  ILE   A CG2 1 
ATOM   639  C CD1 . ILE   A 1 90  ? 11.840  60.697 56.526  1.00 37.69  ? 79  ILE   A CD1 1 
ATOM   640  N N   . SER   A 1 91  ? 11.953  61.768 60.298  1.00 40.34  ? 80  SER   A N   1 
ATOM   641  C CA  . SER   A 1 91  ? 11.730  62.867 61.237  1.00 41.19  ? 80  SER   A CA  1 
ATOM   642  C C   . SER   A 1 91  ? 10.579  63.765 60.841  1.00 41.75  ? 80  SER   A C   1 
ATOM   643  O O   . SER   A 1 91  ? 10.574  64.309 59.728  1.00 41.89  ? 80  SER   A O   1 
ATOM   644  C CB  . SER   A 1 91  ? 12.983  63.724 61.385  1.00 42.50  ? 80  SER   A CB  1 
ATOM   645  O OG  . SER   A 1 91  ? 13.728  63.364 62.535  1.00 45.40  ? 80  SER   A OG  1 
ATOM   646  N N   . LEU   A 1 92  ? 9.633   63.969 61.778  1.00 41.72  ? 81  LEU   A N   1 
ATOM   647  C CA  . LEU   A 1 92  ? 8.526   64.898 61.583  1.00 41.79  ? 81  LEU   A CA  1 
ATOM   648  C C   . LEU   A 1 92  ? 9.090   66.306 61.801  1.00 42.60  ? 81  LEU   A C   1 
ATOM   649  O O   . LEU   A 1 92  ? 9.809   66.524 62.777  1.00 43.04  ? 81  LEU   A O   1 
ATOM   650  C CB  . LEU   A 1 92  ? 7.396   64.628 62.582  1.00 41.26  ? 81  LEU   A CB  1 
ATOM   651  C CG  . LEU   A 1 92  ? 6.193   65.546 62.442  1.00 41.77  ? 81  LEU   A CG  1 
ATOM   652  C CD1 . LEU   A 1 92  ? 5.466   65.295 61.137  1.00 41.82  ? 81  LEU   A CD1 1 
ATOM   653  C CD2 . LEU   A 1 92  ? 5.258   65.403 63.620  1.00 42.23  ? 81  LEU   A CD2 1 
ATOM   654  N N   . GLN   A 1 93  ? 8.820   67.242 60.883  1.00 42.69  ? 82  GLN   A N   1 
ATOM   655  C CA  . GLN   A 1 93  ? 9.330   68.604 61.012  1.00 43.45  ? 82  GLN   A CA  1 
ATOM   656  C C   . GLN   A 1 93  ? 8.215   69.553 61.421  1.00 44.64  ? 82  GLN   A C   1 
ATOM   657  O O   . GLN   A 1 93  ? 8.424   70.390 62.292  1.00 45.50  ? 82  GLN   A O   1 
ATOM   658  C CB  . GLN   A 1 93  ? 9.985   69.119 59.716  1.00 44.61  ? 82  GLN   A CB  1 
ATOM   659  C CG  . GLN   A 1 93  ? 10.394  68.059 58.724  1.00 49.25  ? 82  GLN   A CG  1 
ATOM   660  C CD  . GLN   A 1 93  ? 11.833  68.224 58.349  1.00 55.62  ? 82  GLN   A CD  1 
ATOM   661  O OE1 . GLN   A 1 93  ? 12.701  67.460 58.793  1.00 58.89  ? 82  GLN   A OE1 1 
ATOM   662  N NE2 . GLN   A 1 93  ? 12.126  69.227 57.531  1.00 55.57  ? 82  GLN   A NE2 1 
ATOM   663  N N   . LYS   A 1 94  ? 7.043   69.451 60.778  1.00 44.50  ? 83  LYS   A N   1 
ATOM   664  C CA  . LYS   A 1 94  ? 5.917   70.338 61.046  1.00 44.77  ? 83  LYS   A CA  1 
ATOM   665  C C   . LYS   A 1 94  ? 4.591   69.599 60.959  1.00 44.52  ? 83  LYS   A C   1 
ATOM   666  O O   . LYS   A 1 94  ? 4.498   68.559 60.321  1.00 44.31  ? 83  LYS   A O   1 
ATOM   667  C CB  . LYS   A 1 94  ? 5.891   71.484 60.021  1.00 47.22  ? 83  LYS   A CB  1 
ATOM   668  C CG  . LYS   A 1 94  ? 6.804   72.653 60.318  1.00 52.81  ? 83  LYS   A CG  1 
ATOM   669  C CD  . LYS   A 1 94  ? 6.527   73.834 59.358  1.00 57.98  ? 83  LYS   A CD  1 
ATOM   670  C CE  . LYS   A 1 94  ? 7.253   75.112 59.741  1.00 61.48  ? 83  LYS   A CE  1 
ATOM   671  N NZ  . LYS   A 1 94  ? 7.131   76.161 58.690  1.00 62.90  ? 83  LYS   A NZ  1 
ATOM   672  N N   . VAL   A 1 95  ? 3.554   70.172 61.576  1.00 44.46  ? 84  VAL   A N   1 
ATOM   673  C CA  . VAL   A 1 95  ? 2.177   69.684 61.554  1.00 44.79  ? 84  VAL   A CA  1 
ATOM   674  C C   . VAL   A 1 95  ? 1.318   70.871 61.133  1.00 45.75  ? 84  VAL   A C   1 
ATOM   675  O O   . VAL   A 1 95  ? 1.471   71.949 61.705  1.00 45.85  ? 84  VAL   A O   1 
ATOM   676  C CB  . VAL   A 1 95  ? 1.732   69.205 62.957  1.00 44.78  ? 84  VAL   A CB  1 
ATOM   677  C CG1 . VAL   A 1 95  ? 0.257   68.813 62.969  1.00 44.74  ? 84  VAL   A CG1 1 
ATOM   678  C CG2 . VAL   A 1 95  ? 2.611   68.072 63.459  1.00 45.17  ? 84  VAL   A CG2 1 
ATOM   679  N N   . PHE   A 1 96  ? 0.441   70.702 60.141  1.00 46.38  ? 85  PHE   A N   1 
ATOM   680  C CA  . PHE   A 1 96  ? -0.449  71.783 59.731  1.00 47.68  ? 85  PHE   A CA  1 
ATOM   681  C C   . PHE   A 1 96  ? -1.868  71.340 59.991  1.00 48.89  ? 85  PHE   A C   1 
ATOM   682  O O   . PHE   A 1 96  ? -2.256  70.235 59.600  1.00 49.19  ? 85  PHE   A O   1 
ATOM   683  C CB  . PHE   A 1 96  ? -0.261  72.174 58.263  1.00 47.73  ? 85  PHE   A CB  1 
ATOM   684  C CG  . PHE   A 1 96  ? 1.152   72.552 57.909  1.00 48.52  ? 85  PHE   A CG  1 
ATOM   685  C CD1 . PHE   A 1 96  ? 1.630   73.818 58.165  1.00 49.54  ? 85  PHE   A CD1 1 
ATOM   686  C CD2 . PHE   A 1 96  ? 1.999   71.643 57.309  1.00 49.48  ? 85  PHE   A CD2 1 
ATOM   687  C CE1 . PHE   A 1 96  ? 2.939   74.163 57.843  1.00 50.31  ? 85  PHE   A CE1 1 
ATOM   688  C CE2 . PHE   A 1 96  ? 3.301   71.996 56.975  1.00 50.27  ? 85  PHE   A CE2 1 
ATOM   689  C CZ  . PHE   A 1 96  ? 3.761   73.253 57.242  1.00 49.95  ? 85  PHE   A CZ  1 
ATOM   690  N N   . LEU   A 1 97  ? -2.627  72.168 60.707  1.00 49.40  ? 86  LEU   A N   1 
ATOM   691  C CA  . LEU   A 1 97  ? -4.005  71.840 61.025  1.00 50.40  ? 86  LEU   A CA  1 
ATOM   692  C C   . LEU   A 1 97  ? -4.950  72.702 60.209  1.00 51.33  ? 86  LEU   A C   1 
ATOM   693  O O   . LEU   A 1 97  ? -5.236  73.838 60.570  1.00 51.23  ? 86  LEU   A O   1 
ATOM   694  C CB  . LEU   A 1 97  ? -4.275  71.968 62.532  1.00 50.51  ? 86  LEU   A CB  1 
ATOM   695  C CG  . LEU   A 1 97  ? -3.437  71.076 63.454  1.00 51.67  ? 86  LEU   A CG  1 
ATOM   696  C CD1 . LEU   A 1 97  ? -3.930  71.161 64.860  1.00 52.14  ? 86  LEU   A CD1 1 
ATOM   697  C CD2 . LEU   A 1 97  ? -3.471  69.628 63.027  1.00 52.27  ? 86  LEU   A CD2 1 
ATOM   698  N N   . SER   A 1 98  ? -5.404  72.160 59.084  1.00 52.02  ? 87  SER   A N   1 
ATOM   699  C CA  . SER   A 1 98  ? -6.307  72.840 58.175  1.00 53.15  ? 87  SER   A CA  1 
ATOM   700  C C   . SER   A 1 98  ? -7.691  72.924 58.822  1.00 54.06  ? 87  SER   A C   1 
ATOM   701  O O   . SER   A 1 98  ? -8.495  72.022 58.647  1.00 53.89  ? 87  SER   A O   1 
ATOM   702  C CB  . SER   A 1 98  ? -6.372  72.059 56.869  1.00 54.81  ? 87  SER   A CB  1 
ATOM   703  O OG  . SER   A 1 98  ? -6.788  72.882 55.796  1.00 57.88  ? 87  SER   A OG  1 
ATOM   704  N N   . HIS   A 1 99  ? -7.945  73.991 59.604  1.00 54.73  ? 88  HIS   A N   1 
ATOM   705  C CA  . HIS   A 1 99  ? -9.181  74.200 60.366  1.00 55.77  ? 88  HIS   A CA  1 
ATOM   706  C C   . HIS   A 1 99  ? -10.459 74.181 59.529  1.00 56.61  ? 88  HIS   A C   1 
ATOM   707  O O   . HIS   A 1 99  ? -11.475 73.602 59.948  1.00 56.95  ? 88  HIS   A O   1 
ATOM   708  C CB  . HIS   A 1 99  ? -9.092  75.508 61.157  1.00 56.78  ? 88  HIS   A CB  1 
ATOM   709  C CG  . HIS   A 1 99  ? -8.348  75.389 62.452  1.00 59.51  ? 88  HIS   A CG  1 
ATOM   710  N ND1 . HIS   A 1 99  ? -8.988  75.553 63.670  1.00 61.39  ? 88  HIS   A ND1 1 
ATOM   711  C CD2 . HIS   A 1 99  ? -7.036  75.137 62.680  1.00 60.72  ? 88  HIS   A CD2 1 
ATOM   712  C CE1 . HIS   A 1 99  ? -8.048  75.415 64.593  1.00 61.90  ? 88  HIS   A CE1 1 
ATOM   713  N NE2 . HIS   A 1 99  ? -6.860  75.148 64.047  1.00 61.81  ? 88  HIS   A NE2 1 
ATOM   714  N N   . ALA   A 1 100 ? -10.400 74.807 58.342  1.00 56.37  ? 89  ALA   A N   1 
ATOM   715  C CA  . ALA   A 1 100 ? -11.518 74.905 57.409  1.00 56.41  ? 89  ALA   A CA  1 
ATOM   716  C C   . ALA   A 1 100 ? -12.099 73.553 56.966  1.00 55.98  ? 89  ALA   A C   1 
ATOM   717  O O   . ALA   A 1 100 ? -13.307 73.440 56.777  1.00 56.40  ? 89  ALA   A O   1 
ATOM   718  C CB  . ALA   A 1 100 ? -11.089 75.700 56.191  1.00 56.81  ? 89  ALA   A CB  1 
ATOM   719  N N   . ASP   A 1 101 ? -11.250 72.540 56.779  1.00 54.93  ? 90  ASP   A N   1 
ATOM   720  C CA  . ASP   A 1 101 ? -11.708 71.221 56.332  1.00 54.37  ? 90  ASP   A CA  1 
ATOM   721  C C   . ASP   A 1 101 ? -11.339 70.053 57.267  1.00 53.42  ? 90  ASP   A C   1 
ATOM   722  O O   . ASP   A 1 101 ? -11.553 68.895 56.895  1.00 53.47  ? 90  ASP   A O   1 
ATOM   723  C CB  . ASP   A 1 101 ? -11.232 70.923 54.896  1.00 55.98  ? 90  ASP   A CB  1 
ATOM   724  C CG  . ASP   A 1 101 ? -9.736  71.013 54.662  1.00 59.62  ? 90  ASP   A CG  1 
ATOM   725  O OD1 . ASP   A 1 101 ? -9.083  71.814 55.335  1.00 59.84  ? 90  ASP   A OD1 1 
ATOM   726  O OD2 . ASP   A 1 101 ? -9.232  70.299 53.778  1.00 62.01  ? 90  ASP   A OD2 1 
ATOM   727  N N   A ARG   A 1 102 ? -10.799 70.373 58.461  0.51 52.84  ? 91  ARG   A N   1 
ATOM   728  N N   B ARG   A 1 102 ? -10.811 70.353 58.470  0.49 52.82  ? 91  ARG   A N   1 
ATOM   729  C CA  A ARG   A 1 102 ? -10.353 69.452 59.503  0.51 52.76  ? 91  ARG   A CA  1 
ATOM   730  C CA  B ARG   A 1 102 ? -10.399 69.369 59.479  0.49 52.74  ? 91  ARG   A CA  1 
ATOM   731  C C   A ARG   A 1 102 ? -9.309  68.446 58.998  0.51 52.62  ? 91  ARG   A C   1 
ATOM   732  C C   B ARG   A 1 102 ? -9.298  68.426 58.995  0.49 52.61  ? 91  ARG   A C   1 
ATOM   733  O O   A ARG   A 1 102 ? -9.207  67.351 59.533  0.51 52.87  ? 91  ARG   A O   1 
ATOM   734  O O   B ARG   A 1 102 ? -9.165  67.334 59.536  0.49 52.85  ? 91  ARG   A O   1 
ATOM   735  C CB  A ARG   A 1 102 ? -11.541 68.763 60.196  0.51 53.82  ? 91  ARG   A CB  1 
ATOM   736  C CB  B ARG   A 1 102 ? -11.593 68.543 59.997  0.49 53.75  ? 91  ARG   A CB  1 
ATOM   737  C CG  A ARG   A 1 102 ? -12.503 69.739 60.884  0.51 55.76  ? 91  ARG   A CG  1 
ATOM   738  C CG  B ARG   A 1 102 ? -12.646 69.338 60.746  0.49 55.57  ? 91  ARG   A CG  1 
ATOM   739  C CD  A ARG   A 1 102 ? -11.996 70.208 62.237  0.51 57.64  ? 91  ARG   A CD  1 
ATOM   740  C CD  B ARG   A 1 102 ? -13.489 68.441 61.649  0.49 57.35  ? 91  ARG   A CD  1 
ATOM   741  N NE  A ARG   A 1 102 ? -11.975 71.669 62.359  0.51 59.22  ? 91  ARG   A NE  1 
ATOM   742  N NE  B ARG   A 1 102 ? -12.697 67.738 62.665  0.49 58.93  ? 91  ARG   A NE  1 
ATOM   743  C CZ  A ARG   A 1 102 ? -12.909 72.388 62.976  0.51 60.24  ? 91  ARG   A CZ  1 
ATOM   744  C CZ  B ARG   A 1 102 ? -12.247 68.299 63.784  0.49 60.68  ? 91  ARG   A CZ  1 
ATOM   745  N NH1 A ARG   A 1 102 ? -13.963 71.793 63.523  0.51 59.40  ? 91  ARG   A NH1 1 
ATOM   746  N NH1 B ARG   A 1 102 ? -12.479 69.582 64.033  0.49 59.78  ? 91  ARG   A NH1 1 
ATOM   747  N NH2 A ARG   A 1 102 ? -12.796 73.709 63.053  0.51 59.73  ? 91  ARG   A NH2 1 
ATOM   748  N NH2 B ARG   A 1 102 ? -11.542 67.586 64.654  0.49 60.62  ? 91  ARG   A NH2 1 
ATOM   749  N N   . LYS   A 1 103 ? -8.521  68.824 57.983  1.00 52.13  ? 92  LYS   A N   1 
ATOM   750  C CA  . LYS   A 1 103 ? -7.468  67.962 57.450  1.00 51.38  ? 92  LYS   A CA  1 
ATOM   751  C C   . LYS   A 1 103 ? -6.127  68.197 58.162  1.00 50.45  ? 92  LYS   A C   1 
ATOM   752  O O   . LYS   A 1 103 ? -5.773  69.338 58.485  1.00 50.20  ? 92  LYS   A O   1 
ATOM   753  C CB  . LYS   A 1 103 ? -7.358  68.081 55.915  1.00 52.83  ? 92  LYS   A CB  1 
ATOM   754  C CG  . LYS   A 1 103 ? -8.469  67.346 55.166  1.00 57.35  ? 92  LYS   A CG  1 
ATOM   755  C CD  . LYS   A 1 103 ? -8.424  65.841 55.460  1.00 63.37  ? 92  LYS   A CD  1 
ATOM   756  C CE  . LYS   A 1 103 ? -9.274  64.945 54.578  1.00 67.55  ? 92  LYS   A CE  1 
ATOM   757  N NZ  . LYS   A 1 103 ? -8.721  63.546 54.519  1.00 69.54  ? 92  LYS   A NZ  1 
ATOM   758  N N   . VAL   A 1 104 ? -5.402  67.104 58.450  1.00 49.37  ? 93  VAL   A N   1 
ATOM   759  C CA  . VAL   A 1 104 ? -4.122  67.209 59.135  1.00 48.86  ? 93  VAL   A CA  1 
ATOM   760  C C   . VAL   A 1 104 ? -2.986  66.865 58.179  1.00 48.19  ? 93  VAL   A C   1 
ATOM   761  O O   . VAL   A 1 104 ? -2.992  65.799 57.562  1.00 48.39  ? 93  VAL   A O   1 
ATOM   762  C CB  . VAL   A 1 104 ? -4.089  66.356 60.422  1.00 49.55  ? 93  VAL   A CB  1 
ATOM   763  C CG1 . VAL   A 1 104 ? -2.717  66.410 61.089  1.00 50.15  ? 93  VAL   A CG1 1 
ATOM   764  C CG2 . VAL   A 1 104 ? -5.177  66.799 61.389  1.00 50.08  ? 93  VAL   A CG2 1 
ATOM   765  N N   . TRP   A 1 105 ? -2.022  67.771 58.046  1.00 47.02  ? 94  TRP   A N   1 
ATOM   766  C CA  . TRP   A 1 105 ? -0.893  67.559 57.164  1.00 46.68  ? 94  TRP   A CA  1 
ATOM   767  C C   . TRP   A 1 105 ? 0.404   67.435 57.957  1.00 46.72  ? 94  TRP   A C   1 
ATOM   768  O O   . TRP   A 1 105 ? 0.588   68.133 58.954  1.00 47.54  ? 94  TRP   A O   1 
ATOM   769  C CB  . TRP   A 1 105 ? -0.776  68.738 56.222  1.00 46.64  ? 94  TRP   A CB  1 
ATOM   770  C CG  . TRP   A 1 105 ? -1.894  68.855 55.244  1.00 46.73  ? 94  TRP   A CG  1 
ATOM   771  C CD1 . TRP   A 1 105 ? -3.126  69.404 55.454  1.00 47.29  ? 94  TRP   A CD1 1 
ATOM   772  C CD2 . TRP   A 1 105 ? -1.838  68.505 53.860  1.00 46.60  ? 94  TRP   A CD2 1 
ATOM   773  N NE1 . TRP   A 1 105 ? -3.855  69.381 54.288  1.00 47.49  ? 94  TRP   A NE1 1 
ATOM   774  C CE2 . TRP   A 1 105 ? -3.080  68.848 53.289  1.00 47.16  ? 94  TRP   A CE2 1 
ATOM   775  C CE3 . TRP   A 1 105 ? -0.854  67.937 53.045  1.00 46.88  ? 94  TRP   A CE3 1 
ATOM   776  C CZ2 . TRP   A 1 105 ? -3.359  68.642 51.942  1.00 47.50  ? 94  TRP   A CZ2 1 
ATOM   777  C CZ3 . TRP   A 1 105 ? -1.135  67.734 51.712  1.00 47.54  ? 94  TRP   A CZ3 1 
ATOM   778  C CH2 . TRP   A 1 105 ? -2.379  68.072 51.176  1.00 47.55  ? 94  TRP   A CH2 1 
ATOM   779  N N   . LEU   A 1 106 ? 1.323   66.576 57.502  1.00 45.41  ? 95  LEU   A N   1 
ATOM   780  C CA  . LEU   A 1 106 ? 2.596   66.372 58.172  1.00 44.54  ? 95  LEU   A CA  1 
ATOM   781  C C   . LEU   A 1 106 ? 3.762   66.629 57.224  1.00 43.96  ? 95  LEU   A C   1 
ATOM   782  O O   . LEU   A 1 106 ? 3.793   66.119 56.109  1.00 43.60  ? 95  LEU   A O   1 
ATOM   783  C CB  . LEU   A 1 106 ? 2.676   64.954 58.746  1.00 44.45  ? 95  LEU   A CB  1 
ATOM   784  C CG  . LEU   A 1 106 ? 1.544   64.522 59.671  1.00 45.64  ? 95  LEU   A CG  1 
ATOM   785  C CD1 . LEU   A 1 106 ? 1.735   63.106 60.108  1.00 46.20  ? 95  LEU   A CD1 1 
ATOM   786  C CD2 . LEU   A 1 106 ? 1.437   65.424 60.890  1.00 46.18  ? 95  LEU   A CD2 1 
ATOM   787  N N   . LEU   A 1 107 ? 4.730   67.415 57.677  1.00 43.81  ? 96  LEU   A N   1 
ATOM   788  C CA  . LEU   A 1 107 ? 5.901   67.761 56.883  1.00 44.14  ? 96  LEU   A CA  1 
ATOM   789  C C   . LEU   A 1 107 ? 7.072   66.863 57.258  1.00 44.43  ? 96  LEU   A C   1 
ATOM   790  O O   . LEU   A 1 107 ? 7.312   66.649 58.439  1.00 44.66  ? 96  LEU   A O   1 
ATOM   791  C CB  . LEU   A 1 107 ? 6.254   69.234 57.140  1.00 44.29  ? 96  LEU   A CB  1 
ATOM   792  C CG  . LEU   A 1 107 ? 7.495   69.783 56.449  1.00 45.34  ? 96  LEU   A CG  1 
ATOM   793  C CD1 . LEU   A 1 107 ? 7.365   69.694 54.940  1.00 45.71  ? 96  LEU   A CD1 1 
ATOM   794  C CD2 . LEU   A 1 107 ? 7.758   71.208 56.880  1.00 45.67  ? 96  LEU   A CD2 1 
ATOM   795  N N   . PHE   A 1 108 ? 7.784   66.324 56.251  1.00 44.29  ? 97  PHE   A N   1 
ATOM   796  C CA  . PHE   A 1 108 ? 8.944   65.443 56.419  1.00 44.67  ? 97  PHE   A CA  1 
ATOM   797  C C   . PHE   A 1 108 ? 10.002  65.724 55.330  1.00 45.78  ? 97  PHE   A C   1 
ATOM   798  O O   . PHE   A 1 108 ? 9.657   66.248 54.273  1.00 46.32  ? 97  PHE   A O   1 
ATOM   799  C CB  . PHE   A 1 108 ? 8.509   63.981 56.215  1.00 44.16  ? 97  PHE   A CB  1 
ATOM   800  C CG  . PHE   A 1 108 ? 7.453   63.414 57.129  1.00 44.20  ? 97  PHE   A CG  1 
ATOM   801  C CD1 . PHE   A 1 108 ? 7.798   62.844 58.339  1.00 44.44  ? 97  PHE   A CD1 1 
ATOM   802  C CD2 . PHE   A 1 108 ? 6.129   63.365 56.736  1.00 44.55  ? 97  PHE   A CD2 1 
ATOM   803  C CE1 . PHE   A 1 108 ? 6.834   62.284 59.153  1.00 44.77  ? 97  PHE   A CE1 1 
ATOM   804  C CE2 . PHE   A 1 108 ? 5.170   62.794 57.552  1.00 44.81  ? 97  PHE   A CE2 1 
ATOM   805  C CZ  . PHE   A 1 108 ? 5.528   62.258 58.755  1.00 44.41  ? 97  PHE   A CZ  1 
ATOM   806  N N   . ASP   A 1 109 ? 11.266  65.299 55.534  1.00 45.79  ? 98  ASP   A N   1 
ATOM   807  C CA  . ASP   A 1 109 ? 12.271  65.383 54.477  1.00 46.26  ? 98  ASP   A CA  1 
ATOM   808  C C   . ASP   A 1 109 ? 11.867  64.344 53.387  1.00 46.51  ? 98  ASP   A C   1 
ATOM   809  O O   . ASP   A 1 109 ? 11.225  63.332 53.689  1.00 46.53  ? 98  ASP   A O   1 
ATOM   810  C CB  . ASP   A 1 109 ? 13.671  65.066 55.016  1.00 48.55  ? 98  ASP   A CB  1 
ATOM   811  C CG  . ASP   A 1 109 ? 14.347  66.206 55.743  1.00 55.60  ? 98  ASP   A CG  1 
ATOM   812  O OD1 . ASP   A 1 109 ? 14.204  67.372 55.290  1.00 57.78  ? 98  ASP   A OD1 1 
ATOM   813  O OD2 . ASP   A 1 109 ? 15.038  65.937 56.757  1.00 58.06  ? 98  ASP   A OD2 1 
ATOM   814  N N   . TYR   A 1 110 ? 12.230  64.598 52.129  1.00 46.43  ? 99  TYR   A N   1 
ATOM   815  C CA  . TYR   A 1 110 ? 11.848  63.719 51.032  1.00 46.26  ? 99  TYR   A CA  1 
ATOM   816  C C   . TYR   A 1 110 ? 12.856  62.615 50.747  1.00 46.43  ? 99  TYR   A C   1 
ATOM   817  O O   . TYR   A 1 110 ? 13.983  62.887 50.340  1.00 46.60  ? 99  TYR   A O   1 
ATOM   818  C CB  . TYR   A 1 110 ? 11.542  64.535 49.764  1.00 46.04  ? 99  TYR   A CB  1 
ATOM   819  C CG  . TYR   A 1 110 ? 10.961  63.720 48.641  1.00 46.54  ? 99  TYR   A CG  1 
ATOM   820  C CD1 . TYR   A 1 110 ? 9.651   63.267 48.691  1.00 47.26  ? 99  TYR   A CD1 1 
ATOM   821  C CD2 . TYR   A 1 110 ? 11.730  63.366 47.544  1.00 47.56  ? 99  TYR   A CD2 1 
ATOM   822  C CE1 . TYR   A 1 110 ? 9.123   62.479 47.678  1.00 48.32  ? 99  TYR   A CE1 1 
ATOM   823  C CE2 . TYR   A 1 110 ? 11.216  62.574 46.528  1.00 48.64  ? 99  TYR   A CE2 1 
ATOM   824  C CZ  . TYR   A 1 110 ? 9.910   62.133 46.596  1.00 49.60  ? 99  TYR   A CZ  1 
ATOM   825  O OH  . TYR   A 1 110 ? 9.401   61.364 45.575  1.00 51.55  ? 99  TYR   A OH  1 
ATOM   826  N N   . ALA   A 1 111 ? 12.420  61.357 50.923  1.00 46.17  ? 100 ALA   A N   1 
ATOM   827  C CA  . ALA   A 1 111 ? 13.188  60.159 50.625  1.00 46.00  ? 100 ALA   A CA  1 
ATOM   828  C C   . ALA   A 1 111 ? 12.858  59.790 49.193  1.00 46.53  ? 100 ALA   A C   1 
ATOM   829  O O   . ALA   A 1 111 ? 11.738  59.370 48.902  1.00 46.18  ? 100 ALA   A O   1 
ATOM   830  C CB  . ALA   A 1 111 ? 12.766  59.038 51.543  1.00 45.71  ? 100 ALA   A CB  1 
ATOM   831  N N   . GLU   A 1 112 ? 13.816  59.998 48.288  1.00 47.04  ? 101 GLU   A N   1 
ATOM   832  C CA  . GLU   A 1 112 ? 13.653  59.721 46.865  1.00 47.69  ? 101 GLU   A CA  1 
ATOM   833  C C   . GLU   A 1 112 ? 13.300  58.266 46.615  1.00 47.66  ? 101 GLU   A C   1 
ATOM   834  O O   . GLU   A 1 112 ? 12.506  57.974 45.720  1.00 48.06  ? 101 GLU   A O   1 
ATOM   835  C CB  . GLU   A 1 112 ? 14.935  60.107 46.096  1.00 50.60  ? 101 GLU   A CB  1 
ATOM   836  C CG  . GLU   A 1 112 ? 14.761  60.232 44.592  1.00 57.26  ? 101 GLU   A CG  1 
ATOM   837  C CD  . GLU   A 1 112 ? 13.622  61.122 44.126  1.00 66.64  ? 101 GLU   A CD  1 
ATOM   838  O OE1 . GLU   A 1 112 ? 13.799  62.364 44.107  1.00 67.56  ? 101 GLU   A OE1 1 
ATOM   839  O OE2 . GLU   A 1 112 ? 12.552  60.572 43.771  1.00 70.14  ? 101 GLU   A OE2 1 
ATOM   840  N N   . HIS   A 1 113 ? 13.861  57.359 47.426  1.00 47.01  ? 102 HIS   A N   1 
ATOM   841  C CA  . HIS   A 1 113 ? 13.656  55.927 47.274  1.00 47.01  ? 102 HIS   A CA  1 
ATOM   842  C C   . HIS   A 1 113 ? 12.967  55.268 48.470  1.00 47.14  ? 102 HIS   A C   1 
ATOM   843  O O   . HIS   A 1 113 ? 12.876  55.857 49.546  1.00 47.42  ? 102 HIS   A O   1 
ATOM   844  C CB  . HIS   A 1 113 ? 15.007  55.248 46.999  1.00 47.41  ? 102 HIS   A CB  1 
ATOM   845  C CG  . HIS   A 1 113 ? 15.732  55.886 45.874  1.00 49.34  ? 102 HIS   A CG  1 
ATOM   846  N ND1 . HIS   A 1 113 ? 15.404  55.606 44.566  1.00 51.24  ? 102 HIS   A ND1 1 
ATOM   847  C CD2 . HIS   A 1 113 ? 16.669  56.859 45.896  1.00 50.77  ? 102 HIS   A CD2 1 
ATOM   848  C CE1 . HIS   A 1 113 ? 16.176  56.387 43.829  1.00 52.07  ? 102 HIS   A CE1 1 
ATOM   849  N NE2 . HIS   A 1 113 ? 16.950  57.164 44.585  1.00 52.16  ? 102 HIS   A NE2 1 
ATOM   850  N N   . ASP   A 1 114 ? 12.437  54.063 48.254  1.00 46.51  ? 103 ASP   A N   1 
ATOM   851  C CA  . ASP   A 1 114 ? 11.841  53.202 49.259  1.00 46.37  ? 103 ASP   A CA  1 
ATOM   852  C C   . ASP   A 1 114 ? 12.157  51.760 48.864  1.00 46.88  ? 103 ASP   A C   1 
ATOM   853  O O   . ASP   A 1 114 ? 12.564  51.519 47.723  1.00 47.12  ? 103 ASP   A O   1 
ATOM   854  C CB  . ASP   A 1 114 ? 10.343  53.473 49.461  1.00 47.31  ? 103 ASP   A CB  1 
ATOM   855  C CG  . ASP   A 1 114 ? 9.463   53.131 48.292  1.00 51.38  ? 103 ASP   A CG  1 
ATOM   856  O OD1 . ASP   A 1 114 ? 9.461   51.971 47.875  1.00 52.51  ? 103 ASP   A OD1 1 
ATOM   857  O OD2 . ASP   A 1 114 ? 8.753   54.019 47.811  1.00 53.76  ? 103 ASP   A OD2 1 
ATOM   858  N N   . LEU   A 1 115 ? 11.990  50.794 49.785  1.00 46.98  ? 104 LEU   A N   1 
ATOM   859  C CA  . LEU   A 1 115 ? 12.354  49.409 49.481  1.00 47.46  ? 104 LEU   A CA  1 
ATOM   860  C C   . LEU   A 1 115 ? 11.417  48.709 48.528  1.00 48.10  ? 104 LEU   A C   1 
ATOM   861  O O   . LEU   A 1 115 ? 11.833  47.746 47.913  1.00 47.64  ? 104 LEU   A O   1 
ATOM   862  C CB  . LEU   A 1 115 ? 12.552  48.585 50.752  1.00 47.48  ? 104 LEU   A CB  1 
ATOM   863  C CG  . LEU   A 1 115 ? 13.960  48.046 51.013  1.00 48.37  ? 104 LEU   A CG  1 
ATOM   864  C CD1 . LEU   A 1 115 ? 15.042  49.102 50.784  1.00 48.48  ? 104 LEU   A CD1 1 
ATOM   865  C CD2 . LEU   A 1 115 ? 14.063  47.538 52.411  1.00 49.14  ? 104 LEU   A CD2 1 
ATOM   866  N N   . TRP   A 1 116 ? 10.191  49.201 48.360  1.00 49.25  ? 105 TRP   A N   1 
ATOM   867  C CA  . TRP   A 1 116 ? 9.232   48.603 47.438  1.00 50.87  ? 105 TRP   A CA  1 
ATOM   868  C C   . TRP   A 1 116 ? 9.696   48.901 46.016  1.00 50.95  ? 105 TRP   A C   1 
ATOM   869  O O   . TRP   A 1 116 ? 9.738   48.000 45.178  1.00 51.26  ? 105 TRP   A O   1 
ATOM   870  C CB  . TRP   A 1 116 ? 7.827   49.189 47.686  1.00 52.01  ? 105 TRP   A CB  1 
ATOM   871  C CG  . TRP   A 1 116 ? 6.729   48.549 46.892  1.00 54.39  ? 105 TRP   A CG  1 
ATOM   872  C CD1 . TRP   A 1 116 ? 5.882   47.570 47.313  1.00 55.85  ? 105 TRP   A CD1 1 
ATOM   873  C CD2 . TRP   A 1 116 ? 6.321   48.883 45.553  1.00 55.41  ? 105 TRP   A CD2 1 
ATOM   874  N NE1 . TRP   A 1 116 ? 4.991   47.250 46.312  1.00 56.45  ? 105 TRP   A NE1 1 
ATOM   875  C CE2 . TRP   A 1 116 ? 5.260   48.022 45.211  1.00 56.28  ? 105 TRP   A CE2 1 
ATOM   876  C CE3 . TRP   A 1 116 ? 6.764   49.812 44.601  1.00 56.39  ? 105 TRP   A CE3 1 
ATOM   877  C CZ2 . TRP   A 1 116 ? 4.647   48.055 43.960  1.00 57.14  ? 105 TRP   A CZ2 1 
ATOM   878  C CZ3 . TRP   A 1 116 ? 6.169   49.826 43.355  1.00 57.30  ? 105 TRP   A CZ3 1 
ATOM   879  C CH2 . TRP   A 1 116 ? 5.114   48.967 43.051  1.00 57.33  ? 105 TRP   A CH2 1 
ATOM   880  N N   . HIS   A 1 117 ? 10.058  50.161 45.749  1.00 50.42  ? 106 HIS   A N   1 
ATOM   881  C CA  . HIS   A 1 117 ? 10.488  50.587 44.436  1.00 50.81  ? 106 HIS   A CA  1 
ATOM   882  C C   . HIS   A 1 117 ? 11.838  49.999 44.029  1.00 50.62  ? 106 HIS   A C   1 
ATOM   883  O O   . HIS   A 1 117 ? 12.003  49.646 42.858  1.00 51.14  ? 106 HIS   A O   1 
ATOM   884  C CB  . HIS   A 1 117 ? 10.467  52.122 44.331  1.00 52.54  ? 106 HIS   A CB  1 
ATOM   885  C CG  . HIS   A 1 117 ? 9.081   52.689 44.194  1.00 56.16  ? 106 HIS   A CG  1 
ATOM   886  N ND1 . HIS   A 1 117 ? 8.469   53.368 45.232  1.00 58.33  ? 106 HIS   A ND1 1 
ATOM   887  C CD2 . HIS   A 1 117 ? 8.225   52.640 43.143  1.00 57.49  ? 106 HIS   A CD2 1 
ATOM   888  C CE1 . HIS   A 1 117 ? 7.271   53.714 44.781  1.00 58.96  ? 106 HIS   A CE1 1 
ATOM   889  N NE2 . HIS   A 1 117 ? 7.077   53.294 43.531  1.00 58.65  ? 106 HIS   A NE2 1 
ATOM   890  N N   . ILE   A 1 118 ? 12.792  49.871 44.981  1.00 49.69  ? 107 ILE   A N   1 
ATOM   891  C CA  . ILE   A 1 118 ? 14.121  49.276 44.740  1.00 49.34  ? 107 ILE   A CA  1 
ATOM   892  C C   . ILE   A 1 118 ? 13.974  47.773 44.430  1.00 50.29  ? 107 ILE   A C   1 
ATOM   893  O O   . ILE   A 1 118 ? 14.566  47.281 43.471  1.00 50.74  ? 107 ILE   A O   1 
ATOM   894  C CB  . ILE   A 1 118 ? 15.041  49.511 45.971  1.00 48.91  ? 107 ILE   A CB  1 
ATOM   895  C CG1 . ILE   A 1 118 ? 15.448  50.985 46.092  1.00 48.91  ? 107 ILE   A CG1 1 
ATOM   896  C CG2 . ILE   A 1 118 ? 16.261  48.561 46.000  1.00 49.10  ? 107 ILE   A CG2 1 
ATOM   897  C CD1 . ILE   A 1 118 ? 16.073  51.339 47.369  1.00 49.50  ? 107 ILE   A CD1 1 
ATOM   898  N N   . ILE   A 1 119 ? 13.177  47.054 45.234  1.00 50.51  ? 108 ILE   A N   1 
ATOM   899  C CA  . ILE   A 1 119 ? 12.933  45.629 45.037  1.00 51.47  ? 108 ILE   A CA  1 
ATOM   900  C C   . ILE   A 1 119 ? 12.215  45.382 43.716  1.00 53.17  ? 108 ILE   A C   1 
ATOM   901  O O   . ILE   A 1 119 ? 12.527  44.410 43.036  1.00 53.04  ? 108 ILE   A O   1 
ATOM   902  C CB  . ILE   A 1 119 ? 12.201  44.991 46.261  1.00 51.27  ? 108 ILE   A CB  1 
ATOM   903  C CG1 . ILE   A 1 119 ? 13.150  44.857 47.470  1.00 51.18  ? 108 ILE   A CG1 1 
ATOM   904  C CG2 . ILE   A 1 119 ? 11.569  43.640 45.918  1.00 51.78  ? 108 ILE   A CG2 1 
ATOM   905  C CD1 . ILE   A 1 119 ? 12.478  44.495 48.728  1.00 51.87  ? 108 ILE   A CD1 1 
ATOM   906  N N   . LYS   A 1 120 ? 11.277  46.263 43.338  1.00 54.93  ? 109 LYS   A N   1 
ATOM   907  C CA  . LYS   A 1 120 ? 10.568  46.111 42.068  1.00 57.02  ? 109 LYS   A CA  1 
ATOM   908  C C   . LYS   A 1 120 ? 11.527  46.283 40.893  1.00 58.51  ? 109 LYS   A C   1 
ATOM   909  O O   . LYS   A 1 120 ? 11.447  45.525 39.933  1.00 58.69  ? 109 LYS   A O   1 
ATOM   910  C CB  . LYS   A 1 120 ? 9.348   47.049 41.954  1.00 59.57  ? 109 LYS   A CB  1 
ATOM   911  C CG  . LYS   A 1 120 ? 8.655   46.925 40.596  1.00 65.39  ? 109 LYS   A CG  1 
ATOM   912  C CD  . LYS   A 1 120 ? 7.186   47.327 40.574  1.00 71.75  ? 109 LYS   A CD  1 
ATOM   913  C CE  . LYS   A 1 120 ? 6.480   46.700 39.376  1.00 76.48  ? 109 LYS   A CE  1 
ATOM   914  N NZ  . LYS   A 1 120 ? 5.112   47.257 39.141  1.00 79.03  ? 109 LYS   A NZ  1 
ATOM   915  N N   . PHE   A 1 121 ? 12.472  47.220 41.001  1.00 59.63  ? 110 PHE   A N   1 
ATOM   916  C CA  . PHE   A 1 121 ? 13.475  47.485 39.976  1.00 61.42  ? 110 PHE   A CA  1 
ATOM   917  C C   . PHE   A 1 121 ? 14.310  46.247 39.712  1.00 63.23  ? 110 PHE   A C   1 
ATOM   918  O O   . PHE   A 1 121 ? 14.535  45.904 38.554  1.00 63.45  ? 110 PHE   A O   1 
ATOM   919  C CB  . PHE   A 1 121 ? 14.367  48.660 40.400  1.00 61.45  ? 110 PHE   A CB  1 
ATOM   920  C CG  . PHE   A 1 121 ? 15.361  49.146 39.377  1.00 62.37  ? 110 PHE   A CG  1 
ATOM   921  C CD1 . PHE   A 1 121 ? 15.002  50.088 38.433  1.00 63.40  ? 110 PHE   A CD1 1 
ATOM   922  C CD2 . PHE   A 1 121 ? 16.670  48.703 39.393  1.00 63.49  ? 110 PHE   A CD2 1 
ATOM   923  C CE1 . PHE   A 1 121 ? 15.931  50.568 37.512  1.00 64.26  ? 110 PHE   A CE1 1 
ATOM   924  C CE2 . PHE   A 1 121 ? 17.599  49.193 38.483  1.00 64.40  ? 110 PHE   A CE2 1 
ATOM   925  C CZ  . PHE   A 1 121 ? 17.226  50.133 37.555  1.00 64.16  ? 110 PHE   A CZ  1 
ATOM   926  N N   . HIS   A 1 122 ? 14.737  45.556 40.776  1.00 64.61  ? 111 HIS   A N   1 
ATOM   927  C CA  . HIS   A 1 122 ? 15.527  44.333 40.646  1.00 66.40  ? 111 HIS   A CA  1 
ATOM   928  C C   . HIS   A 1 122 ? 14.711  43.212 40.032  1.00 68.06  ? 111 HIS   A C   1 
ATOM   929  O O   . HIS   A 1 122 ? 15.203  42.529 39.144  1.00 68.29  ? 111 HIS   A O   1 
ATOM   930  C CB  . HIS   A 1 122 ? 16.108  43.907 41.992  1.00 67.43  ? 111 HIS   A CB  1 
ATOM   931  C CG  . HIS   A 1 122 ? 17.186  44.822 42.474  1.00 70.63  ? 111 HIS   A CG  1 
ATOM   932  N ND1 . HIS   A 1 122 ? 18.293  45.102 41.692  1.00 72.81  ? 111 HIS   A ND1 1 
ATOM   933  C CD2 . HIS   A 1 122 ? 17.302  45.484 43.649  1.00 72.00  ? 111 HIS   A CD2 1 
ATOM   934  C CE1 . HIS   A 1 122 ? 19.038  45.930 42.408  1.00 73.34  ? 111 HIS   A CE1 1 
ATOM   935  N NE2 . HIS   A 1 122 ? 18.481  46.192 43.589  1.00 73.23  ? 111 HIS   A NE2 1 
ATOM   936  N N   . ARG   A 1 123 ? 13.448  43.065 40.448  1.00 69.23  ? 112 ARG   A N   1 
ATOM   937  C CA  . ARG   A 1 123 ? 12.527  42.060 39.914  1.00 70.84  ? 112 ARG   A CA  1 
ATOM   938  C C   . ARG   A 1 123 ? 12.290  42.264 38.417  1.00 72.34  ? 112 ARG   A C   1 
ATOM   939  O O   . ARG   A 1 123 ? 12.190  41.291 37.667  1.00 72.45  ? 112 ARG   A O   1 
ATOM   940  C CB  . ARG   A 1 123 ? 11.186  42.124 40.653  1.00 72.20  ? 112 ARG   A CB  1 
ATOM   941  C CG  . ARG   A 1 123 ? 10.868  40.858 41.403  1.00 75.42  ? 112 ARG   A CG  1 
ATOM   942  C CD  . ARG   A 1 123 ? 9.399   40.745 41.713  1.00 79.83  ? 112 ARG   A CD  1 
ATOM   943  N NE  . ARG   A 1 123 ? 9.020   39.337 41.801  1.00 85.15  ? 112 ARG   A NE  1 
ATOM   944  C CZ  . ARG   A 1 123 ? 7.781   38.897 41.993  1.00 88.93  ? 112 ARG   A CZ  1 
ATOM   945  N NH1 . ARG   A 1 123 ? 7.537   37.595 42.059  1.00 88.53  ? 112 ARG   A NH1 1 
ATOM   946  N NH2 . ARG   A 1 123 ? 6.776   39.756 42.123  1.00 89.75  ? 112 ARG   A NH2 1 
ATOM   947  N N   . ALA   A 1 124 ? 12.197  43.526 37.985  1.00 73.32  ? 113 ALA   A N   1 
ATOM   948  C CA  . ALA   A 1 124 ? 11.988  43.831 36.582  1.00 75.03  ? 113 ALA   A CA  1 
ATOM   949  C C   . ALA   A 1 124 ? 13.228  43.425 35.784  1.00 77.22  ? 113 ALA   A C   1 
ATOM   950  O O   . ALA   A 1 124 ? 13.095  42.754 34.761  1.00 77.54  ? 113 ALA   A O   1 
ATOM   951  C CB  . ALA   A 1 124 ? 11.691  45.313 36.404  1.00 75.02  ? 113 ALA   A CB  1 
ATOM   952  N N   . SER   A 1 125 ? 14.431  43.750 36.304  1.00 78.45  ? 114 SER   A N   1 
ATOM   953  C CA  . SER   A 1 125 ? 15.721  43.441 35.679  1.00 80.07  ? 114 SER   A CA  1 
ATOM   954  C C   . SER   A 1 125 ? 15.955  41.953 35.428  1.00 81.56  ? 114 SER   A C   1 
ATOM   955  O O   . SER   A 1 125 ? 16.589  41.601 34.438  1.00 81.81  ? 114 SER   A O   1 
ATOM   956  C CB  . SER   A 1 125 ? 16.867  44.018 36.501  1.00 81.57  ? 114 SER   A CB  1 
ATOM   957  O OG  . SER   A 1 125 ? 16.849  45.437 36.482  1.00 84.05  ? 114 SER   A OG  1 
ATOM   958  N N   . LYS   A 1 126 ? 15.440  41.085 36.303  1.00 82.49  ? 115 LYS   A N   1 
ATOM   959  C CA  . LYS   A 1 126 ? 15.590  39.640 36.137  1.00 83.92  ? 115 LYS   A CA  1 
ATOM   960  C C   . LYS   A 1 126 ? 14.797  39.181 34.921  1.00 85.16  ? 115 LYS   A C   1 
ATOM   961  O O   . LYS   A 1 126 ? 15.315  38.418 34.105  1.00 85.34  ? 115 LYS   A O   1 
ATOM   962  C CB  . LYS   A 1 126 ? 15.130  38.885 37.403  1.00 85.90  ? 115 LYS   A CB  1 
ATOM   963  C CG  . LYS   A 1 126 ? 15.882  39.322 38.660  1.00 89.70  ? 115 LYS   A CG  1 
ATOM   964  C CD  . LYS   A 1 126 ? 15.754  38.362 39.828  1.00 93.39  ? 115 LYS   A CD  1 
ATOM   965  C CE  . LYS   A 1 126 ? 16.897  38.594 40.785  1.00 97.03  ? 115 LYS   A CE  1 
ATOM   966  N NZ  . LYS   A 1 126 ? 16.832  37.692 41.964  1.00 99.85  ? 115 LYS   A NZ  1 
ATOM   967  N N   . ALA   A 1 127 ? 13.557  39.685 34.776  1.00 85.75  ? 116 ALA   A N   1 
ATOM   968  C CA  . ALA   A 1 127 ? 12.679  39.338 33.655  1.00 86.63  ? 116 ALA   A CA  1 
ATOM   969  C C   . ALA   A 1 127 ? 13.192  39.855 32.313  1.00 87.47  ? 116 ALA   A C   1 
ATOM   970  O O   . ALA   A 1 127 ? 12.849  39.294 31.274  1.00 87.69  ? 116 ALA   A O   1 
ATOM   971  C CB  . ALA   A 1 127 ? 11.275  39.862 33.908  1.00 86.72  ? 116 ALA   A CB  1 
ATOM   972  N N   . ASN   A 1 128 ? 14.002  40.924 32.329  1.00 87.71  ? 117 ASN   A N   1 
ATOM   973  C CA  . ASN   A 1 128 ? 14.565  41.515 31.123  1.00 88.41  ? 117 ASN   A CA  1 
ATOM   974  C C   . ASN   A 1 128 ? 15.995  41.013 30.884  1.00 88.79  ? 117 ASN   A C   1 
ATOM   975  O O   . ASN   A 1 128 ? 16.238  39.805 30.874  1.00 88.95  ? 117 ASN   A O   1 
ATOM   976  C CB  . ASN   A 1 128 ? 14.546  43.037 31.236  1.00 89.71  ? 117 ASN   A CB  1 
ATOM   977  C CG  . ASN   A 1 128 ? 13.175  43.607 31.523  1.00 92.63  ? 117 ASN   A CG  1 
ATOM   978  O OD1 . ASN   A 1 128 ? 12.141  43.042 31.145  1.00 93.42  ? 117 ASN   A OD1 1 
ATOM   979  N ND2 . ASN   A 1 128 ? 13.141  44.745 32.205  1.00 93.24  ? 117 ASN   A ND2 1 
ATOM   980  N N   . LEU   A 1 134 ? 22.719  45.566 43.107  1.00 74.84  ? 123 LEU   A N   1 
ATOM   981  C CA  . LEU   A 1 134 ? 22.983  45.336 44.526  1.00 75.29  ? 123 LEU   A CA  1 
ATOM   982  C C   . LEU   A 1 134 ? 24.505  45.346 44.812  1.00 75.63  ? 123 LEU   A C   1 
ATOM   983  O O   . LEU   A 1 134 ? 25.103  44.270 44.933  1.00 76.04  ? 123 LEU   A O   1 
ATOM   984  C CB  . LEU   A 1 134 ? 22.369  43.993 44.968  1.00 75.54  ? 123 LEU   A CB  1 
ATOM   985  C CG  . LEU   A 1 134 ? 20.934  43.727 44.539  1.00 77.40  ? 123 LEU   A CG  1 
ATOM   986  C CD1 . LEU   A 1 134 ? 20.795  42.355 43.919  1.00 77.97  ? 123 LEU   A CD1 1 
ATOM   987  C CD2 . LEU   A 1 134 ? 19.972  43.894 45.701  1.00 78.42  ? 123 LEU   A CD2 1 
ATOM   988  N N   . PRO   A 1 135 ? 25.149  46.535 44.947  1.00 75.17  ? 124 PRO   A N   1 
ATOM   989  C CA  . PRO   A 1 135 ? 26.599  46.561 45.264  1.00 74.63  ? 124 PRO   A CA  1 
ATOM   990  C C   . PRO   A 1 135 ? 26.936  45.782 46.540  1.00 73.88  ? 124 PRO   A C   1 
ATOM   991  O O   . PRO   A 1 135 ? 26.110  45.756 47.443  1.00 74.48  ? 124 PRO   A O   1 
ATOM   992  C CB  . PRO   A 1 135 ? 26.905  48.051 45.477  1.00 75.53  ? 124 PRO   A CB  1 
ATOM   993  C CG  . PRO   A 1 135 ? 25.770  48.795 44.884  1.00 76.23  ? 124 PRO   A CG  1 
ATOM   994  C CD  . PRO   A 1 135 ? 24.573  47.893 44.871  1.00 74.81  ? 124 PRO   A CD  1 
ATOM   995  N N   . ARG   A 1 136 ? 28.124  45.139 46.603  1.00 72.31  ? 125 ARG   A N   1 
ATOM   996  C CA  . ARG   A 1 136 ? 28.653  44.333 47.719  1.00 71.27  ? 125 ARG   A CA  1 
ATOM   997  C C   . ARG   A 1 136 ? 27.690  44.126 48.951  1.00 69.14  ? 125 ARG   A C   1 
ATOM   998  O O   . ARG   A 1 136 ? 27.083  43.059 49.092  1.00 69.51  ? 125 ARG   A O   1 
ATOM   999  C CB  . ARG   A 1 136 ? 30.005  44.906 48.189  1.00 73.36  ? 125 ARG   A CB  1 
ATOM   1000 C CG  . ARG   A 1 136 ? 31.031  45.071 47.085  1.00 77.44  ? 125 ARG   A CG  1 
ATOM   1001 C CD  . ARG   A 1 136 ? 31.946  43.868 46.956  1.00 80.45  ? 125 ARG   A CD  1 
ATOM   1002 N NE  . ARG   A 1 136 ? 32.827  43.724 48.115  1.00 82.47  ? 125 ARG   A NE  1 
ATOM   1003 C CZ  . ARG   A 1 136 ? 32.710  42.769 49.033  1.00 84.04  ? 125 ARG   A CZ  1 
ATOM   1004 N NH1 . ARG   A 1 136 ? 31.741  41.865 48.942  1.00 83.51  ? 125 ARG   A NH1 1 
ATOM   1005 N NH2 . ARG   A 1 136 ? 33.557  42.714 50.050  1.00 83.57  ? 125 ARG   A NH2 1 
ATOM   1006 N N   . GLY   A 1 137 ? 27.552  45.143 49.807  1.00 66.45  ? 126 GLY   A N   1 
ATOM   1007 C CA  . GLY   A 1 137 ? 26.721  45.044 50.997  1.00 63.84  ? 126 GLY   A CA  1 
ATOM   1008 C C   . GLY   A 1 137 ? 25.583  46.036 51.063  1.00 60.40  ? 126 GLY   A C   1 
ATOM   1009 O O   . GLY   A 1 137 ? 25.354  46.625 52.116  1.00 60.45  ? 126 GLY   A O   1 
ATOM   1010 N N   . MET   A 1 138 ? 24.871  46.240 49.950  1.00 57.29  ? 127 MET   A N   1 
ATOM   1011 C CA  . MET   A 1 138 ? 23.717  47.121 49.948  1.00 54.96  ? 127 MET   A CA  1 
ATOM   1012 C C   . MET   A 1 138 ? 22.582  46.452 50.713  1.00 52.76  ? 127 MET   A C   1 
ATOM   1013 O O   . MET   A 1 138 ? 21.909  47.118 51.490  1.00 53.02  ? 127 MET   A O   1 
ATOM   1014 C CB  . MET   A 1 138 ? 23.264  47.500 48.534  1.00 55.07  ? 127 MET   A CB  1 
ATOM   1015 C CG  . MET   A 1 138 ? 22.118  48.478 48.570  1.00 56.39  ? 127 MET   A CG  1 
ATOM   1016 S SD  . MET   A 1 138 ? 21.354  48.807 46.994  1.00 59.56  ? 127 MET   A SD  1 
ATOM   1017 C CE  . MET   A 1 138 ? 19.740  49.237 47.523  1.00 57.76  ? 127 MET   A CE  1 
ATOM   1018 N N   . VAL   A 1 139 ? 22.389  45.135 50.520  1.00 50.53  ? 128 VAL   A N   1 
ATOM   1019 C CA  . VAL   A 1 139 ? 21.381  44.352 51.230  1.00 48.73  ? 128 VAL   A CA  1 
ATOM   1020 C C   . VAL   A 1 139 ? 21.721  44.329 52.719  1.00 46.82  ? 128 VAL   A C   1 
ATOM   1021 O O   . VAL   A 1 139 ? 20.844  44.583 53.548  1.00 46.74  ? 128 VAL   A O   1 
ATOM   1022 C CB  . VAL   A 1 139 ? 21.295  42.932 50.635  1.00 49.02  ? 128 VAL   A CB  1 
ATOM   1023 C CG1 . VAL   A 1 139 ? 20.486  41.989 51.524  1.00 49.24  ? 128 VAL   A CG1 1 
ATOM   1024 C CG2 . VAL   A 1 139 ? 20.731  42.979 49.220  1.00 49.48  ? 128 VAL   A CG2 1 
ATOM   1025 N N   . LYS   A 1 140 ? 23.004  44.092 53.050  1.00 45.10  ? 129 LYS   A N   1 
ATOM   1026 C CA  . LYS   A 1 140 ? 23.459  44.077 54.439  1.00 44.38  ? 129 LYS   A CA  1 
ATOM   1027 C C   . LYS   A 1 140 ? 23.289  45.444 55.112  1.00 44.09  ? 129 LYS   A C   1 
ATOM   1028 O O   . LYS   A 1 140 ? 22.781  45.512 56.229  1.00 44.59  ? 129 LYS   A O   1 
ATOM   1029 C CB  . LYS   A 1 140 ? 24.921  43.617 54.537  1.00 44.97  ? 129 LYS   A CB  1 
ATOM   1030 C CG  . LYS   A 1 140 ? 25.426  43.521 55.973  1.00 46.08  ? 129 LYS   A CG  1 
ATOM   1031 C CD  . LYS   A 1 140 ? 26.917  43.244 56.059  1.00 47.71  ? 129 LYS   A CD  1 
ATOM   1032 C CE  . LYS   A 1 140 ? 27.331  42.013 55.297  1.00 49.47  ? 129 LYS   A CE  1 
ATOM   1033 N NZ  . LYS   A 1 140 ? 28.578  41.426 55.838  1.00 50.48  ? 129 LYS   A NZ  1 
ATOM   1034 N N   . SER   A 1 141 ? 23.681  46.526 54.434  1.00 43.15  ? 130 SER   A N   1 
ATOM   1035 C CA  . SER   A 1 141 ? 23.535  47.867 54.977  1.00 43.14  ? 130 SER   A CA  1 
ATOM   1036 C C   . SER   A 1 141 ? 22.055  48.209 55.205  1.00 42.43  ? 130 SER   A C   1 
ATOM   1037 O O   . SER   A 1 141 ? 21.723  48.827 56.217  1.00 42.52  ? 130 SER   A O   1 
ATOM   1038 C CB  . SER   A 1 141 ? 24.168  48.893 54.043  1.00 45.11  ? 130 SER   A CB  1 
ATOM   1039 O OG  . SER   A 1 141 ? 25.523  48.582 53.766  1.00 47.96  ? 130 SER   A OG  1 
ATOM   1040 N N   . LEU   A 1 142 ? 21.167  47.794 54.281  1.00 41.28  ? 131 LEU   A N   1 
ATOM   1041 C CA  . LEU   A 1 142 ? 19.728  48.019 54.418  1.00 40.53  ? 131 LEU   A CA  1 
ATOM   1042 C C   . LEU   A 1 142 ? 19.217  47.250 55.631  1.00 40.20  ? 131 LEU   A C   1 
ATOM   1043 O O   . LEU   A 1 142 ? 18.509  47.822 56.452  1.00 40.92  ? 131 LEU   A O   1 
ATOM   1044 C CB  . LEU   A 1 142 ? 18.975  47.568 53.158  1.00 40.27  ? 131 LEU   A CB  1 
ATOM   1045 C CG  . LEU   A 1 142 ? 19.068  48.488 51.951  1.00 40.66  ? 131 LEU   A CG  1 
ATOM   1046 C CD1 . LEU   A 1 142 ? 18.579  47.798 50.712  1.00 40.87  ? 131 LEU   A CD1 1 
ATOM   1047 C CD2 . LEU   A 1 142 ? 18.321  49.757 52.184  1.00 40.92  ? 131 LEU   A CD2 1 
ATOM   1048 N N   . LEU   A 1 143 ? 19.644  45.994 55.798  1.00 39.06  ? 132 LEU   A N   1 
ATOM   1049 C CA  . LEU   A 1 143 ? 19.251  45.205 56.965  1.00 38.45  ? 132 LEU   A CA  1 
ATOM   1050 C C   . LEU   A 1 143 ? 19.708  45.815 58.290  1.00 37.46  ? 132 LEU   A C   1 
ATOM   1051 O O   . LEU   A 1 143 ? 18.868  46.029 59.157  1.00 37.29  ? 132 LEU   A O   1 
ATOM   1052 C CB  . LEU   A 1 143 ? 19.702  43.740 56.861  1.00 38.50  ? 132 LEU   A CB  1 
ATOM   1053 C CG  . LEU   A 1 143 ? 19.189  42.855 57.996  1.00 40.09  ? 132 LEU   A CG  1 
ATOM   1054 C CD1 . LEU   A 1 143 ? 17.657  42.818 58.028  1.00 40.99  ? 132 LEU   A CD1 1 
ATOM   1055 C CD2 . LEU   A 1 143 ? 19.766  41.464 57.926  1.00 40.31  ? 132 LEU   A CD2 1 
ATOM   1056 N N   . TYR   A 1 144 ? 21.015  46.133 58.437  1.00 36.71  ? 133 TYR   A N   1 
ATOM   1057 C CA  . TYR   A 1 144 ? 21.546  46.750 59.660  1.00 36.49  ? 133 TYR   A CA  1 
ATOM   1058 C C   . TYR   A 1 144 ? 20.811  48.034 60.016  1.00 36.24  ? 133 TYR   A C   1 
ATOM   1059 O O   . TYR   A 1 144 ? 20.569  48.274 61.191  1.00 36.55  ? 133 TYR   A O   1 
ATOM   1060 C CB  . TYR   A 1 144 ? 23.058  47.045 59.566  1.00 36.36  ? 133 TYR   A CB  1 
ATOM   1061 C CG  . TYR   A 1 144 ? 23.665  47.365 60.916  1.00 37.76  ? 133 TYR   A CG  1 
ATOM   1062 C CD1 . TYR   A 1 144 ? 23.920  46.363 61.839  1.00 39.59  ? 133 TYR   A CD1 1 
ATOM   1063 C CD2 . TYR   A 1 144 ? 23.959  48.669 61.279  1.00 39.16  ? 133 TYR   A CD2 1 
ATOM   1064 C CE1 . TYR   A 1 144 ? 24.416  46.651 63.106  1.00 40.73  ? 133 TYR   A CE1 1 
ATOM   1065 C CE2 . TYR   A 1 144 ? 24.480  48.970 62.536  1.00 40.64  ? 133 TYR   A CE2 1 
ATOM   1066 C CZ  . TYR   A 1 144 ? 24.711  47.953 63.448  1.00 41.98  ? 133 TYR   A CZ  1 
ATOM   1067 O OH  . TYR   A 1 144 ? 25.252  48.203 64.691  1.00 44.11  ? 133 TYR   A OH  1 
ATOM   1068 N N   . GLN   A 1 145 ? 20.457  48.857 59.014  1.00 35.52  ? 134 GLN   A N   1 
ATOM   1069 C CA  . GLN   A 1 145 ? 19.774  50.111 59.278  1.00 35.44  ? 134 GLN   A CA  1 
ATOM   1070 C C   . GLN   A 1 145 ? 18.313  49.885 59.654  1.00 35.12  ? 134 GLN   A C   1 
ATOM   1071 O O   . GLN   A 1 145 ? 17.833  50.534 60.585  1.00 35.21  ? 134 GLN   A O   1 
ATOM   1072 C CB  . GLN   A 1 145 ? 19.956  51.115 58.128  1.00 37.22  ? 134 GLN   A CB  1 
ATOM   1073 C CG  . GLN   A 1 145 ? 21.419  51.544 57.928  1.00 40.46  ? 134 GLN   A CG  1 
ATOM   1074 C CD  . GLN   A 1 145 ? 21.582  52.752 57.027  1.00 42.99  ? 134 GLN   A CD  1 
ATOM   1075 O OE1 . GLN   A 1 145 ? 20.868  53.741 57.159  1.00 44.41  ? 134 GLN   A OE1 1 
ATOM   1076 N NE2 . GLN   A 1 145 ? 22.550  52.712 56.112  1.00 42.05  ? 134 GLN   A NE2 1 
ATOM   1077 N N   . ILE   A 1 146 ? 17.628  48.918 59.003  1.00 34.44  ? 135 ILE   A N   1 
ATOM   1078 C CA  . ILE   A 1 146 ? 16.242  48.561 59.340  1.00 34.44  ? 135 ILE   A CA  1 
ATOM   1079 C C   . ILE   A 1 146 ? 16.178  48.083 60.785  1.00 35.70  ? 135 ILE   A C   1 
ATOM   1080 O O   . ILE   A 1 146 ? 15.308  48.519 61.536  1.00 36.14  ? 135 ILE   A O   1 
ATOM   1081 C CB  . ILE   A 1 146 ? 15.686  47.483 58.375  1.00 34.02  ? 135 ILE   A CB  1 
ATOM   1082 C CG1 . ILE   A 1 146 ? 15.500  48.064 56.961  1.00 34.55  ? 135 ILE   A CG1 1 
ATOM   1083 C CG2 . ILE   A 1 146 ? 14.384  46.853 58.903  1.00 33.87  ? 135 ILE   A CG2 1 
ATOM   1084 C CD1 . ILE   A 1 146 ? 15.236  47.046 55.877  1.00 35.04  ? 135 ILE   A CD1 1 
ATOM   1085 N N   . LEU   A 1 147 ? 17.145  47.218 61.175  1.00 36.20  ? 136 LEU   A N   1 
ATOM   1086 C CA  . LEU   A 1 147 ? 17.290  46.635 62.514  1.00 36.54  ? 136 LEU   A CA  1 
ATOM   1087 C C   . LEU   A 1 147 ? 17.584  47.705 63.540  1.00 36.85  ? 136 LEU   A C   1 
ATOM   1088 O O   . LEU   A 1 147 ? 16.908  47.764 64.550  1.00 36.82  ? 136 LEU   A O   1 
ATOM   1089 C CB  . LEU   A 1 147 ? 18.401  45.577 62.513  1.00 36.99  ? 136 LEU   A CB  1 
ATOM   1090 C CG  . LEU   A 1 147 ? 18.005  44.201 61.993  1.00 38.35  ? 136 LEU   A CG  1 
ATOM   1091 C CD1 . LEU   A 1 147 ? 19.235  43.371 61.687  1.00 38.53  ? 136 LEU   A CD1 1 
ATOM   1092 C CD2 . LEU   A 1 147 ? 17.063  43.484 62.985  1.00 38.83  ? 136 LEU   A CD2 1 
ATOM   1093 N N   . ASP   A 1 148 ? 18.546  48.581 63.254  1.00 37.32  ? 137 ASP   A N   1 
ATOM   1094 C CA  . ASP   A 1 148 ? 18.933  49.715 64.089  1.00 38.41  ? 137 ASP   A CA  1 
ATOM   1095 C C   . ASP   A 1 148 ? 17.725  50.636 64.462  1.00 39.48  ? 137 ASP   A C   1 
ATOM   1096 O O   . ASP   A 1 148 ? 17.566  50.992 65.628  1.00 39.88  ? 137 ASP   A O   1 
ATOM   1097 C CB  . ASP   A 1 148 ? 20.007  50.520 63.342  1.00 39.61  ? 137 ASP   A CB  1 
ATOM   1098 C CG  . ASP   A 1 148 ? 20.818  51.472 64.177  1.00 44.66  ? 137 ASP   A CG  1 
ATOM   1099 O OD1 . ASP   A 1 148 ? 20.589  51.533 65.409  1.00 45.53  ? 137 ASP   A OD1 1 
ATOM   1100 O OD2 . ASP   A 1 148 ? 21.685  52.155 63.609  1.00 47.41  ? 137 ASP   A OD2 1 
ATOM   1101 N N   . GLY   A 1 149 ? 16.900  50.999 63.481  1.00 39.69  ? 138 GLY   A N   1 
ATOM   1102 C CA  . GLY   A 1 149 ? 15.746  51.865 63.701  1.00 40.34  ? 138 GLY   A CA  1 
ATOM   1103 C C   . GLY   A 1 149 ? 14.657  51.208 64.526  1.00 41.13  ? 138 GLY   A C   1 
ATOM   1104 O O   . GLY   A 1 149 ? 14.097  51.837 65.430  1.00 41.42  ? 138 GLY   A O   1 
ATOM   1105 N N   . ILE   A 1 150 ? 14.357  49.914 64.226  1.00 40.96  ? 139 ILE   A N   1 
ATOM   1106 C CA  . ILE   A 1 150 ? 13.373  49.111 64.957  1.00 40.55  ? 139 ILE   A CA  1 
ATOM   1107 C C   . ILE   A 1 150 ? 13.833  48.867 66.380  1.00 40.48  ? 139 ILE   A C   1 
ATOM   1108 O O   . ILE   A 1 150 ? 13.023  48.912 67.291  1.00 40.90  ? 139 ILE   A O   1 
ATOM   1109 C CB  . ILE   A 1 150 ? 13.072  47.807 64.200  1.00 41.03  ? 139 ILE   A CB  1 
ATOM   1110 C CG1 . ILE   A 1 150 ? 12.201  48.127 62.981  1.00 42.85  ? 139 ILE   A CG1 1 
ATOM   1111 C CG2 . ILE   A 1 150 ? 12.389  46.746 65.090  1.00 41.02  ? 139 ILE   A CG2 1 
ATOM   1112 C CD1 . ILE   A 1 150 ? 10.810  48.749 63.328  1.00 44.37  ? 139 ILE   A CD1 1 
ATOM   1113 N N   . HIS   A 1 151 ? 15.134  48.675 66.583  1.00 39.81  ? 140 HIS   A N   1 
ATOM   1114 C CA  . HIS   A 1 151 ? 15.720  48.485 67.891  1.00 39.65  ? 140 HIS   A CA  1 
ATOM   1115 C C   . HIS   A 1 151 ? 15.471  49.706 68.775  1.00 39.26  ? 140 HIS   A C   1 
ATOM   1116 O O   . HIS   A 1 151 ? 15.184  49.537 69.952  1.00 39.23  ? 140 HIS   A O   1 
ATOM   1117 C CB  . HIS   A 1 151 ? 17.217  48.205 67.740  1.00 40.60  ? 140 HIS   A CB  1 
ATOM   1118 C CG  . HIS   A 1 151 ? 17.980  48.288 69.019  1.00 43.44  ? 140 HIS   A CG  1 
ATOM   1119 N ND1 . HIS   A 1 151 ? 18.746  49.400 69.332  1.00 45.66  ? 140 HIS   A ND1 1 
ATOM   1120 C CD2 . HIS   A 1 151 ? 18.027  47.416 70.050  1.00 44.58  ? 140 HIS   A CD2 1 
ATOM   1121 C CE1 . HIS   A 1 151 ? 19.263  49.147 70.525  1.00 46.22  ? 140 HIS   A CE1 1 
ATOM   1122 N NE2 . HIS   A 1 151 ? 18.855  47.965 70.996  1.00 45.89  ? 140 HIS   A NE2 1 
ATOM   1123 N N   . TYR   A 1 152 ? 15.588  50.921 68.204  1.00 38.85  ? 141 TYR   A N   1 
ATOM   1124 C CA  . TYR   A 1 152 ? 15.349  52.197 68.884  1.00 38.95  ? 141 TYR   A CA  1 
ATOM   1125 C C   . TYR   A 1 152 ? 13.857  52.342 69.246  1.00 39.02  ? 141 TYR   A C   1 
ATOM   1126 O O   . TYR   A 1 152 ? 13.518  52.908 70.286  1.00 39.07  ? 141 TYR   A O   1 
ATOM   1127 C CB  . TYR   A 1 152 ? 15.784  53.355 67.977  1.00 39.21  ? 141 TYR   A CB  1 
ATOM   1128 C CG  . TYR   A 1 152 ? 15.319  54.709 68.465  1.00 40.94  ? 141 TYR   A CG  1 
ATOM   1129 C CD1 . TYR   A 1 152 ? 15.907  55.310 69.568  1.00 42.08  ? 141 TYR   A CD1 1 
ATOM   1130 C CD2 . TYR   A 1 152 ? 14.224  55.339 67.892  1.00 42.04  ? 141 TYR   A CD2 1 
ATOM   1131 C CE1 . TYR   A 1 152 ? 15.466  56.535 70.042  1.00 42.84  ? 141 TYR   A CE1 1 
ATOM   1132 C CE2 . TYR   A 1 152 ? 13.780  56.570 68.352  1.00 42.95  ? 141 TYR   A CE2 1 
ATOM   1133 C CZ  . TYR   A 1 152 ? 14.399  57.163 69.433  1.00 43.78  ? 141 TYR   A CZ  1 
ATOM   1134 O OH  . TYR   A 1 152 ? 13.943  58.365 69.921  1.00 45.20  ? 141 TYR   A OH  1 
ATOM   1135 N N   . LEU   A 1 153 ? 12.970  51.879 68.349  1.00 38.48  ? 142 LEU   A N   1 
ATOM   1136 C CA  . LEU   A 1 153 ? 11.541  51.919 68.574  1.00 38.14  ? 142 LEU   A CA  1 
ATOM   1137 C C   . LEU   A 1 153 ? 11.213  50.940 69.693  1.00 38.55  ? 142 LEU   A C   1 
ATOM   1138 O O   . LEU   A 1 153 ? 10.564  51.307 70.653  1.00 38.17  ? 142 LEU   A O   1 
ATOM   1139 C CB  . LEU   A 1 153 ? 10.790  51.556 67.276  1.00 37.77  ? 142 LEU   A CB  1 
ATOM   1140 C CG  . LEU   A 1 153 ? 10.933  52.534 66.098  1.00 38.17  ? 142 LEU   A CG  1 
ATOM   1141 C CD1 . LEU   A 1 153 ? 10.135  52.058 64.902  1.00 38.40  ? 142 LEU   A CD1 1 
ATOM   1142 C CD2 . LEU   A 1 153 ? 10.481  53.929 66.475  1.00 38.22  ? 142 LEU   A CD2 1 
ATOM   1143 N N   . HIS   A 1 154 ? 11.719  49.713 69.605  1.00 39.47  ? 143 HIS   A N   1 
ATOM   1144 C CA  . HIS   A 1 154 ? 11.500  48.671 70.602  1.00 40.59  ? 143 HIS   A CA  1 
ATOM   1145 C C   . HIS   A 1 154 ? 12.092  49.033 71.969  1.00 41.99  ? 143 HIS   A C   1 
ATOM   1146 O O   . HIS   A 1 154 ? 11.464  48.758 72.992  1.00 42.26  ? 143 HIS   A O   1 
ATOM   1147 C CB  . HIS   A 1 154 ? 11.995  47.306 70.090  1.00 40.64  ? 143 HIS   A CB  1 
ATOM   1148 C CG  . HIS   A 1 154 ? 11.150  46.706 69.003  1.00 41.69  ? 143 HIS   A CG  1 
ATOM   1149 N ND1 . HIS   A 1 154 ? 11.504  45.520 68.399  1.00 42.91  ? 143 HIS   A ND1 1 
ATOM   1150 C CD2 . HIS   A 1 154 ? 9.998   47.152 68.440  1.00 42.86  ? 143 HIS   A CD2 1 
ATOM   1151 C CE1 . HIS   A 1 154 ? 10.568  45.282 67.493  1.00 43.54  ? 143 HIS   A CE1 1 
ATOM   1152 N NE2 . HIS   A 1 154 ? 9.636   46.232 67.486  1.00 43.61  ? 143 HIS   A NE2 1 
ATOM   1153 N N   . ALA   A 1 155 ? 13.231  49.751 71.995  1.00 42.50  ? 144 ALA   A N   1 
ATOM   1154 C CA  . ALA   A 1 155 ? 13.835  50.234 73.237  1.00 43.29  ? 144 ALA   A CA  1 
ATOM   1155 C C   . ALA   A 1 155 ? 12.853  51.176 73.928  1.00 44.83  ? 144 ALA   A C   1 
ATOM   1156 O O   . ALA   A 1 155 ? 12.618  51.035 75.127  1.00 45.10  ? 144 ALA   A O   1 
ATOM   1157 C CB  . ALA   A 1 155 ? 15.143  50.952 72.949  1.00 43.12  ? 144 ALA   A CB  1 
ATOM   1158 N N   . ASN   A 1 156 ? 12.189  52.050 73.140  1.00 45.96  ? 145 ASN   A N   1 
ATOM   1159 C CA  . ASN   A 1 156 ? 11.157  52.977 73.600  1.00 47.45  ? 145 ASN   A CA  1 
ATOM   1160 C C   . ASN   A 1 156 ? 9.758   52.347 73.604  1.00 49.03  ? 145 ASN   A C   1 
ATOM   1161 O O   . ASN   A 1 156 ? 8.787   53.075 73.529  1.00 49.12  ? 145 ASN   A O   1 
ATOM   1162 C CB  . ASN   A 1 156 ? 11.142  54.218 72.728  1.00 48.50  ? 145 ASN   A CB  1 
ATOM   1163 C CG  . ASN   A 1 156 ? 12.349  55.059 72.920  1.00 52.09  ? 145 ASN   A CG  1 
ATOM   1164 O OD1 . ASN   A 1 156 ? 12.647  55.514 74.025  1.00 53.69  ? 145 ASN   A OD1 1 
ATOM   1165 N ND2 . ASN   A 1 156 ? 13.082  55.261 71.850  1.00 52.88  ? 145 ASN   A ND2 1 
ATOM   1166 N N   . TRP   A 1 157 ? 9.651   51.011 73.614  1.00 50.10  ? 146 TRP   A N   1 
ATOM   1167 C CA  . TRP   A 1 157 ? 8.387   50.277 73.664  1.00 51.37  ? 146 TRP   A CA  1 
ATOM   1168 C C   . TRP   A 1 157 ? 7.361   50.671 72.612  1.00 49.31  ? 146 TRP   A C   1 
ATOM   1169 O O   . TRP   A 1 157 ? 6.159   50.685 72.879  1.00 49.34  ? 146 TRP   A O   1 
ATOM   1170 C CB  . TRP   A 1 157 ? 7.800   50.400 75.056  1.00 53.50  ? 146 TRP   A CB  1 
ATOM   1171 C CG  . TRP   A 1 157 ? 8.713   49.842 76.092  1.00 56.97  ? 146 TRP   A CG  1 
ATOM   1172 C CD1 . TRP   A 1 157 ? 9.579   50.536 76.893  1.00 58.88  ? 146 TRP   A CD1 1 
ATOM   1173 C CD2 . TRP   A 1 157 ? 8.924   48.453 76.369  1.00 58.23  ? 146 TRP   A CD2 1 
ATOM   1174 N NE1 . TRP   A 1 157 ? 10.268  49.662 77.705  1.00 59.88  ? 146 TRP   A NE1 1 
ATOM   1175 C CE2 . TRP   A 1 157 ? 9.882   48.374 77.405  1.00 59.60  ? 146 TRP   A CE2 1 
ATOM   1176 C CE3 . TRP   A 1 157 ? 8.360   47.269 75.871  1.00 59.12  ? 146 TRP   A CE3 1 
ATOM   1177 C CZ2 . TRP   A 1 157 ? 10.275  47.157 77.963  1.00 60.46  ? 146 TRP   A CZ2 1 
ATOM   1178 C CZ3 . TRP   A 1 157 ? 8.755   46.067 76.419  1.00 60.55  ? 146 TRP   A CZ3 1 
ATOM   1179 C CH2 . TRP   A 1 157 ? 9.702   46.016 77.453  1.00 60.84  ? 146 TRP   A CH2 1 
ATOM   1180 N N   . VAL   A 1 158 ? 7.840   50.962 71.410  1.00 47.31  ? 147 VAL   A N   1 
ATOM   1181 C CA  . VAL   A 1 158 ? 7.007   51.341 70.281  1.00 45.57  ? 147 VAL   A CA  1 
ATOM   1182 C C   . VAL   A 1 158 ? 7.077   50.230 69.245  1.00 43.89  ? 147 VAL   A C   1 
ATOM   1183 O O   . VAL   A 1 158 ? 8.163   49.870 68.792  1.00 43.46  ? 147 VAL   A O   1 
ATOM   1184 C CB  . VAL   A 1 158 ? 7.467   52.707 69.704  1.00 45.38  ? 147 VAL   A CB  1 
ATOM   1185 C CG1 . VAL   A 1 158 ? 6.875   52.976 68.323  1.00 45.43  ? 147 VAL   A CG1 1 
ATOM   1186 C CG2 . VAL   A 1 158 ? 7.133   53.830 70.667  1.00 45.48  ? 147 VAL   A CG2 1 
ATOM   1187 N N   . LEU   A 1 159 ? 5.929   49.669 68.901  1.00 42.95  ? 148 LEU   A N   1 
ATOM   1188 C CA  . LEU   A 1 159 ? 5.875   48.638 67.877  1.00 43.22  ? 148 LEU   A CA  1 
ATOM   1189 C C   . LEU   A 1 159 ? 5.485   49.287 66.556  1.00 44.21  ? 148 LEU   A C   1 
ATOM   1190 O O   . LEU   A 1 159 ? 4.693   50.232 66.550  1.00 44.93  ? 148 LEU   A O   1 
ATOM   1191 C CB  . LEU   A 1 159 ? 4.878   47.534 68.259  1.00 42.82  ? 148 LEU   A CB  1 
ATOM   1192 C CG  . LEU   A 1 159 ? 5.094   46.926 69.643  1.00 43.11  ? 148 LEU   A CG  1 
ATOM   1193 C CD1 . LEU   A 1 159 ? 3.975   46.032 70.024  1.00 43.35  ? 148 LEU   A CD1 1 
ATOM   1194 C CD2 . LEU   A 1 159 ? 6.419   46.237 69.747  1.00 43.00  ? 148 LEU   A CD2 1 
ATOM   1195 N N   . HIS   A 1 160 ? 6.072   48.835 65.445  1.00 44.07  ? 149 HIS   A N   1 
ATOM   1196 C CA  . HIS   A 1 160 ? 5.712   49.379 64.148  1.00 44.45  ? 149 HIS   A CA  1 
ATOM   1197 C C   . HIS   A 1 160 ? 4.318   48.873 63.798  1.00 44.78  ? 149 HIS   A C   1 
ATOM   1198 O O   . HIS   A 1 160 ? 3.480   49.648 63.375  1.00 44.72  ? 149 HIS   A O   1 
ATOM   1199 C CB  . HIS   A 1 160 ? 6.719   48.994 63.066  1.00 45.40  ? 149 HIS   A CB  1 
ATOM   1200 C CG  . HIS   A 1 160 ? 6.436   49.700 61.783  1.00 48.07  ? 149 HIS   A CG  1 
ATOM   1201 N ND1 . HIS   A 1 160 ? 5.338   49.369 61.006  1.00 49.93  ? 149 HIS   A ND1 1 
ATOM   1202 C CD2 . HIS   A 1 160 ? 7.068   50.753 61.219  1.00 49.49  ? 149 HIS   A CD2 1 
ATOM   1203 C CE1 . HIS   A 1 160 ? 5.352   50.209 59.986  1.00 50.67  ? 149 HIS   A CE1 1 
ATOM   1204 N NE2 . HIS   A 1 160 ? 6.376   51.057 60.067  1.00 50.85  ? 149 HIS   A NE2 1 
ATOM   1205 N N   . ARG   A 1 161 ? 4.070   47.567 63.994  1.00 45.16  ? 150 ARG   A N   1 
ATOM   1206 C CA  . ARG   A 1 161 ? 2.806   46.873 63.742  1.00 45.38  ? 150 ARG   A CA  1 
ATOM   1207 C C   . ARG   A 1 161 ? 2.528   46.589 62.265  1.00 44.85  ? 150 ARG   A C   1 
ATOM   1208 O O   . ARG   A 1 161 ? 1.639   45.791 61.992  1.00 45.39  ? 150 ARG   A O   1 
ATOM   1209 C CB  . ARG   A 1 161 ? 1.605   47.593 64.386  1.00 47.12  ? 150 ARG   A CB  1 
ATOM   1210 C CG  . ARG   A 1 161 ? 1.851   48.034 65.827  1.00 51.51  ? 150 ARG   A CG  1 
ATOM   1211 C CD  . ARG   A 1 161 ? 0.627   47.881 66.692  1.00 55.98  ? 150 ARG   A CD  1 
ATOM   1212 N NE  . ARG   A 1 161 ? -0.041  49.151 66.975  1.00 60.05  ? 150 ARG   A NE  1 
ATOM   1213 C CZ  . ARG   A 1 161 ? -0.120  49.706 68.182  1.00 62.30  ? 150 ARG   A CZ  1 
ATOM   1214 N NH1 . ARG   A 1 161 ? 0.460   49.126 69.229  1.00 61.71  ? 150 ARG   A NH1 1 
ATOM   1215 N NH2 . ARG   A 1 161 ? -0.772  50.847 68.351  1.00 61.91  ? 150 ARG   A NH2 1 
ATOM   1216 N N   . ASP   A 1 162 ? 3.271   47.194 61.320  1.00 43.79  ? 151 ASP   A N   1 
ATOM   1217 C CA  . ASP   A 1 162 ? 2.976   46.991 59.901  1.00 43.57  ? 151 ASP   A CA  1 
ATOM   1218 C C   . ASP   A 1 162 ? 4.179   47.122 58.977  1.00 42.22  ? 151 ASP   A C   1 
ATOM   1219 O O   . ASP   A 1 162 ? 4.036   47.544 57.831  1.00 42.39  ? 151 ASP   A O   1 
ATOM   1220 C CB  . ASP   A 1 162 ? 1.873   47.971 59.461  1.00 46.39  ? 151 ASP   A CB  1 
ATOM   1221 C CG  . ASP   A 1 162 ? 1.004   47.488 58.321  1.00 52.01  ? 151 ASP   A CG  1 
ATOM   1222 O OD1 . ASP   A 1 162 ? 0.916   46.257 58.124  1.00 53.02  ? 151 ASP   A OD1 1 
ATOM   1223 O OD2 . ASP   A 1 162 ? 0.395   48.340 57.641  1.00 54.60  ? 151 ASP   A OD2 1 
ATOM   1224 N N   . LEU   A 1 163 ? 5.361   46.745 59.447  1.00 40.80  ? 152 LEU   A N   1 
ATOM   1225 C CA  . LEU   A 1 163 ? 6.576   46.791 58.637  1.00 40.16  ? 152 LEU   A CA  1 
ATOM   1226 C C   . LEU   A 1 163 ? 6.425   46.071 57.293  1.00 39.67  ? 152 LEU   A C   1 
ATOM   1227 O O   . LEU   A 1 163 ? 5.960   44.923 57.250  1.00 39.93  ? 152 LEU   A O   1 
ATOM   1228 C CB  . LEU   A 1 163 ? 7.703   46.116 59.397  1.00 40.29  ? 152 LEU   A CB  1 
ATOM   1229 C CG  . LEU   A 1 163 ? 8.538   47.002 60.235  1.00 41.47  ? 152 LEU   A CG  1 
ATOM   1230 C CD1 . LEU   A 1 163 ? 9.335   46.183 61.236  1.00 42.12  ? 152 LEU   A CD1 1 
ATOM   1231 C CD2 . LEU   A 1 163 ? 9.427   47.794 59.370  1.00 41.91  ? 152 LEU   A CD2 1 
ATOM   1232 N N   . LYS   A 1 164 ? 6.815   46.757 56.215  1.00 38.58  ? 153 LYS   A N   1 
ATOM   1233 C CA  . LYS   A 1 164 ? 6.775   46.270 54.844  1.00 38.22  ? 153 LYS   A CA  1 
ATOM   1234 C C   . LYS   A 1 164 ? 7.685   47.156 53.964  1.00 38.23  ? 153 LYS   A C   1 
ATOM   1235 O O   . LYS   A 1 164 ? 8.004   48.290 54.337  1.00 37.80  ? 153 LYS   A O   1 
ATOM   1236 C CB  . LYS   A 1 164 ? 5.326   46.240 54.327  1.00 39.85  ? 153 LYS   A CB  1 
ATOM   1237 C CG  . LYS   A 1 164 ? 4.660   47.594 54.309  1.00 43.58  ? 153 LYS   A CG  1 
ATOM   1238 C CD  . LYS   A 1 164 ? 3.331   47.543 53.626  1.00 47.70  ? 153 LYS   A CD  1 
ATOM   1239 C CE  . LYS   A 1 164 ? 2.307   48.269 54.444  1.00 51.87  ? 153 LYS   A CE  1 
ATOM   1240 N NZ  . LYS   A 1 164 ? 2.173   47.625 55.775  1.00 54.48  ? 153 LYS   A NZ  1 
ATOM   1241 N N   . PRO   A 1 165 ? 8.142   46.656 52.798  1.00 38.50  ? 154 PRO   A N   1 
ATOM   1242 C CA  . PRO   A 1 165 ? 9.087   47.441 51.986  1.00 38.74  ? 154 PRO   A CA  1 
ATOM   1243 C C   . PRO   A 1 165 ? 8.669   48.875 51.639  1.00 39.02  ? 154 PRO   A C   1 
ATOM   1244 O O   . PRO   A 1 165 ? 9.536   49.757 51.547  1.00 38.66  ? 154 PRO   A O   1 
ATOM   1245 C CB  . PRO   A 1 165 ? 9.271   46.574 50.734  1.00 39.18  ? 154 PRO   A CB  1 
ATOM   1246 C CG  . PRO   A 1 165 ? 9.051   45.184 51.222  1.00 39.42  ? 154 PRO   A CG  1 
ATOM   1247 C CD  . PRO   A 1 165 ? 7.938   45.311 52.224  1.00 37.75  ? 154 PRO   A CD  1 
ATOM   1248 N N   . ALA   A 1 166 ? 7.371   49.113 51.417  1.00 39.36  ? 155 ALA   A N   1 
ATOM   1249 C CA  . ALA   A 1 166 ? 6.918   50.446 51.034  1.00 40.13  ? 155 ALA   A CA  1 
ATOM   1250 C C   . ALA   A 1 166 ? 7.198   51.485 52.122  1.00 41.04  ? 155 ALA   A C   1 
ATOM   1251 O O   . ALA   A 1 166 ? 7.630   52.584 51.795  1.00 41.56  ? 155 ALA   A O   1 
ATOM   1252 C CB  . ALA   A 1 166 ? 5.453   50.425 50.645  1.00 40.05  ? 155 ALA   A CB  1 
ATOM   1253 N N   . ASN   A 1 167 ? 7.056   51.123 53.413  1.00 40.95  ? 156 ASN   A N   1 
ATOM   1254 C CA  . ASN   A 1 167 ? 7.339   52.069 54.500  1.00 40.84  ? 156 ASN   A CA  1 
ATOM   1255 C C   . ASN   A 1 167 ? 8.805   51.959 55.050  1.00 41.36  ? 156 ASN   A C   1 
ATOM   1256 O O   . ASN   A 1 167 ? 9.069   52.289 56.204  1.00 41.58  ? 156 ASN   A O   1 
ATOM   1257 C CB  . ASN   A 1 167 ? 6.282   51.971 55.606  1.00 40.65  ? 156 ASN   A CB  1 
ATOM   1258 C CG  . ASN   A 1 167 ? 6.131   50.592 56.202  1.00 41.30  ? 156 ASN   A CG  1 
ATOM   1259 O OD1 . ASN   A 1 167 ? 7.084   49.826 56.276  1.00 42.24  ? 156 ASN   A OD1 1 
ATOM   1260 N ND2 . ASN   A 1 167 ? 4.940   50.250 56.654  1.00 40.53  ? 156 ASN   A ND2 1 
ATOM   1261 N N   . ILE   A 1 168 ? 9.743   51.499 54.218  1.00 41.26  ? 157 ILE   A N   1 
ATOM   1262 C CA  . ILE   A 1 168 ? 11.154  51.485 54.567  1.00 41.65  ? 157 ILE   A CA  1 
ATOM   1263 C C   . ILE   A 1 168 ? 11.763  52.384 53.529  1.00 42.04  ? 157 ILE   A C   1 
ATOM   1264 O O   . ILE   A 1 168 ? 12.169  51.920 52.465  1.00 42.68  ? 157 ILE   A O   1 
ATOM   1265 C CB  . ILE   A 1 168 ? 11.829  50.105 54.516  1.00 42.58  ? 157 ILE   A CB  1 
ATOM   1266 C CG1 . ILE   A 1 168 ? 11.076  49.050 55.351  1.00 44.49  ? 157 ILE   A CG1 1 
ATOM   1267 C CG2 . ILE   A 1 168 ? 13.287  50.233 54.936  1.00 42.62  ? 157 ILE   A CG2 1 
ATOM   1268 C CD1 . ILE   A 1 168 ? 10.972  49.377 56.791  1.00 46.15  ? 157 ILE   A CD1 1 
ATOM   1269 N N   . LEU   A 1 169 ? 11.761  53.679 53.788  1.00 41.57  ? 158 LEU   A N   1 
ATOM   1270 C CA  . LEU   A 1 169 ? 12.290  54.664 52.850  1.00 41.58  ? 158 LEU   A CA  1 
ATOM   1271 C C   . LEU   A 1 169 ? 13.828  54.704 52.878  1.00 41.38  ? 158 LEU   A C   1 
ATOM   1272 O O   . LEU   A 1 169 ? 14.445  54.272 53.849  1.00 41.02  ? 158 LEU   A O   1 
ATOM   1273 C CB  . LEU   A 1 169 ? 11.708  56.063 53.146  1.00 41.81  ? 158 LEU   A CB  1 
ATOM   1274 C CG  . LEU   A 1 169 ? 10.218  56.163 53.526  1.00 42.97  ? 158 LEU   A CG  1 
ATOM   1275 C CD1 . LEU   A 1 169 ? 9.857   57.582 53.889  1.00 43.56  ? 158 LEU   A CD1 1 
ATOM   1276 C CD2 . LEU   A 1 169 ? 9.319   55.648 52.411  1.00 43.31  ? 158 LEU   A CD2 1 
ATOM   1277 N N   . VAL   A 1 170 ? 14.442  55.178 51.786  1.00 41.39  ? 159 VAL   A N   1 
ATOM   1278 C CA  . VAL   A 1 170 ? 15.890  55.295 51.629  1.00 41.97  ? 159 VAL   A CA  1 
ATOM   1279 C C   . VAL   A 1 170 ? 16.181  56.615 50.951  1.00 42.95  ? 159 VAL   A C   1 
ATOM   1280 O O   . VAL   A 1 170 ? 15.732  56.817 49.835  1.00 43.22  ? 159 VAL   A O   1 
ATOM   1281 C CB  . VAL   A 1 170 ? 16.525  54.161 50.795  1.00 42.22  ? 159 VAL   A CB  1 
ATOM   1282 C CG1 . VAL   A 1 170 ? 18.033  54.188 50.952  1.00 42.75  ? 159 VAL   A CG1 1 
ATOM   1283 C CG2 . VAL   A 1 170 ? 15.969  52.795 51.164  1.00 42.32  ? 159 VAL   A CG2 1 
ATOM   1284 N N   . MET   A 1 171 ? 16.958  57.492 51.588  1.00 43.52  ? 160 MET   A N   1 
ATOM   1285 C CA  . MET   A 1 171 ? 17.292  58.800 51.038  1.00 44.71  ? 160 MET   A CA  1 
ATOM   1286 C C   . MET   A 1 171 ? 18.156  58.746 49.780  1.00 46.19  ? 160 MET   A C   1 
ATOM   1287 O O   . MET   A 1 171 ? 19.053  57.925 49.684  1.00 46.37  ? 160 MET   A O   1 
ATOM   1288 C CB  . MET   A 1 171 ? 17.984  59.657 52.102  1.00 45.24  ? 160 MET   A CB  1 
ATOM   1289 C CG  . MET   A 1 171 ? 17.226  59.722 53.407  1.00 47.54  ? 160 MET   A CG  1 
ATOM   1290 S SD  . MET   A 1 171 ? 15.590  60.491 53.239  1.00 51.95  ? 160 MET   A SD  1 
ATOM   1291 C CE  . MET   A 1 171 ? 16.030  62.203 53.252  1.00 46.50  ? 160 MET   A CE  1 
ATOM   1292 N N   . GLY   A 1 172 ? 17.880  59.630 48.831  1.00 47.19  ? 161 GLY   A N   1 
ATOM   1293 C CA  . GLY   A 1 172 ? 18.644  59.742 47.593  1.00 48.51  ? 161 GLY   A CA  1 
ATOM   1294 C C   . GLY   A 1 172 ? 19.778  60.745 47.735  1.00 49.64  ? 161 GLY   A C   1 
ATOM   1295 O O   . GLY   A 1 172 ? 20.273  60.958 48.845  1.00 50.06  ? 161 GLY   A O   1 
ATOM   1296 N N   . GLU   A 1 173 ? 20.192  61.406 46.628  1.00 49.63  ? 162 GLU   A N   1 
ATOM   1297 C CA  . GLU   A 1 173 ? 21.288  62.389 46.692  1.00 49.51  ? 162 GLU   A CA  1 
ATOM   1298 C C   . GLU   A 1 173 ? 21.034  63.483 47.711  1.00 48.93  ? 162 GLU   A C   1 
ATOM   1299 O O   . GLU   A 1 173 ? 19.902  63.941 47.844  1.00 49.35  ? 162 GLU   A O   1 
ATOM   1300 C CB  . GLU   A 1 173 ? 21.602  62.986 45.320  1.00 51.84  ? 162 GLU   A CB  1 
ATOM   1301 C CG  . GLU   A 1 173 ? 22.250  62.008 44.355  1.00 57.80  ? 162 GLU   A CG  1 
ATOM   1302 C CD  . GLU   A 1 173 ? 23.532  61.334 44.815  1.00 65.43  ? 162 GLU   A CD  1 
ATOM   1303 O OE1 . GLU   A 1 173 ? 24.247  61.902 45.674  1.00 66.34  ? 162 GLU   A OE1 1 
ATOM   1304 O OE2 . GLU   A 1 173 ? 23.825  60.230 44.298  1.00 68.21  ? 162 GLU   A OE2 1 
ATOM   1305 N N   . GLY   A 1 174 ? 22.060  63.821 48.478  1.00 47.94  ? 163 GLY   A N   1 
ATOM   1306 C CA  . GLY   A 1 174 ? 21.950  64.812 49.537  1.00 47.68  ? 163 GLY   A CA  1 
ATOM   1307 C C   . GLY   A 1 174 ? 22.789  64.473 50.749  1.00 47.40  ? 163 GLY   A C   1 
ATOM   1308 O O   . GLY   A 1 174 ? 23.541  63.494 50.745  1.00 47.69  ? 163 GLY   A O   1 
ATOM   1309 N N   . PRO   A 1 175 ? 22.662  65.260 51.827  1.00 46.68  ? 164 PRO   A N   1 
ATOM   1310 C CA  . PRO   A 1 175 ? 23.485  65.010 53.025  1.00 46.54  ? 164 PRO   A CA  1 
ATOM   1311 C C   . PRO   A 1 175 ? 23.182  63.718 53.774  1.00 46.94  ? 164 PRO   A C   1 
ATOM   1312 O O   . PRO   A 1 175 ? 24.004  63.285 54.580  1.00 47.11  ? 164 PRO   A O   1 
ATOM   1313 C CB  . PRO   A 1 175 ? 23.242  66.242 53.890  1.00 46.87  ? 164 PRO   A CB  1 
ATOM   1314 C CG  . PRO   A 1 175 ? 21.933  66.748 53.453  1.00 47.31  ? 164 PRO   A CG  1 
ATOM   1315 C CD  . PRO   A 1 175 ? 21.826  66.457 51.986  1.00 45.85  ? 164 PRO   A CD  1 
ATOM   1316 N N   . GLU   A 1 176 ? 22.015  63.101 53.522  1.00 46.74  ? 165 GLU   A N   1 
ATOM   1317 C CA  . GLU   A 1 176 ? 21.683  61.829 54.163  1.00 46.85  ? 165 GLU   A CA  1 
ATOM   1318 C C   . GLU   A 1 176 ? 21.644  60.688 53.142  1.00 46.88  ? 165 GLU   A C   1 
ATOM   1319 O O   . GLU   A 1 176 ? 20.913  59.722 53.347  1.00 47.10  ? 165 GLU   A O   1 
ATOM   1320 C CB  . GLU   A 1 176 ? 20.340  61.915 54.900  1.00 48.41  ? 165 GLU   A CB  1 
ATOM   1321 C CG  . GLU   A 1 176 ? 20.365  62.839 56.093  1.00 52.16  ? 165 GLU   A CG  1 
ATOM   1322 C CD  . GLU   A 1 176 ? 19.340  62.480 57.149  1.00 58.13  ? 165 GLU   A CD  1 
ATOM   1323 O OE1 . GLU   A 1 176 ? 19.642  61.606 57.995  1.00 58.92  ? 165 GLU   A OE1 1 
ATOM   1324 O OE2 . GLU   A 1 176 ? 18.239  63.080 57.136  1.00 60.29  ? 165 GLU   A OE2 1 
ATOM   1325 N N   . ARG   A 1 177 ? 22.421  60.793 52.048  1.00 46.44  ? 166 ARG   A N   1 
ATOM   1326 C CA  . ARG   A 1 177 ? 22.442  59.805 50.971  1.00 46.48  ? 166 ARG   A CA  1 
ATOM   1327 C C   . ARG   A 1 177 ? 22.508  58.344 51.441  1.00 46.44  ? 166 ARG   A C   1 
ATOM   1328 O O   . ARG   A 1 177 ? 23.301  58.000 52.327  1.00 46.99  ? 166 ARG   A O   1 
ATOM   1329 C CB  . ARG   A 1 177 ? 23.574  60.114 49.990  1.00 47.58  ? 166 ARG   A CB  1 
ATOM   1330 C CG  . ARG   A 1 177 ? 23.433  59.418 48.650  1.00 50.65  ? 166 ARG   A CG  1 
ATOM   1331 C CD  . ARG   A 1 177 ? 24.787  59.374 47.992  1.00 54.53  ? 166 ARG   A CD  1 
ATOM   1332 N NE  . ARG   A 1 177 ? 24.744  58.794 46.655  1.00 58.37  ? 166 ARG   A NE  1 
ATOM   1333 C CZ  . ARG   A 1 177 ? 25.374  57.679 46.299  1.00 61.71  ? 166 ARG   A CZ  1 
ATOM   1334 N NH1 . ARG   A 1 177 ? 26.092  57.001 47.186  1.00 61.84  ? 166 ARG   A NH1 1 
ATOM   1335 N NH2 . ARG   A 1 177 ? 25.289  57.231 45.054  1.00 62.04  ? 166 ARG   A NH2 1 
ATOM   1336 N N   . GLY   A 1 178 ? 21.630  57.525 50.872  1.00 45.58  ? 167 GLY   A N   1 
ATOM   1337 C CA  . GLY   A 1 178 ? 21.529  56.099 51.148  1.00 45.24  ? 167 GLY   A CA  1 
ATOM   1338 C C   . GLY   A 1 178 ? 21.198  55.724 52.576  1.00 44.91  ? 167 GLY   A C   1 
ATOM   1339 O O   . GLY   A 1 178 ? 21.630  54.670 53.038  1.00 45.14  ? 167 GLY   A O   1 
ATOM   1340 N N   . ARG   A 1 179 ? 20.443  56.567 53.297  1.00 44.23  ? 168 ARG   A N   1 
ATOM   1341 C CA  . ARG   A 1 179 ? 20.090  56.263 54.689  1.00 43.69  ? 168 ARG   A CA  1 
ATOM   1342 C C   . ARG   A 1 179 ? 18.669  55.785 54.810  1.00 42.62  ? 168 ARG   A C   1 
ATOM   1343 O O   . ARG   A 1 179 ? 17.778  56.385 54.235  1.00 42.71  ? 168 ARG   A O   1 
ATOM   1344 C CB  . ARG   A 1 179 ? 20.324  57.473 55.603  1.00 45.25  ? 168 ARG   A CB  1 
ATOM   1345 C CG  . ARG   A 1 179 ? 19.947  57.224 57.044  1.00 48.42  ? 168 ARG   A CG  1 
ATOM   1346 C CD  . ARG   A 1 179 ? 20.412  58.347 57.901  1.00 52.78  ? 168 ARG   A CD  1 
ATOM   1347 N NE  . ARG   A 1 179 ? 21.828  58.209 58.227  1.00 57.16  ? 168 ARG   A NE  1 
ATOM   1348 C CZ  . ARG   A 1 179 ? 22.583  59.194 58.704  1.00 60.73  ? 168 ARG   A CZ  1 
ATOM   1349 N NH1 . ARG   A 1 179 ? 22.068  60.409 58.889  1.00 60.11  ? 168 ARG   A NH1 1 
ATOM   1350 N NH2 . ARG   A 1 179 ? 23.858  58.975 58.997  1.00 61.53  ? 168 ARG   A NH2 1 
ATOM   1351 N N   . VAL   A 1 180 ? 18.451  54.728 55.572  1.00 41.79  ? 169 VAL   A N   1 
ATOM   1352 C CA  . VAL   A 1 180 ? 17.122  54.175 55.769  1.00 41.78  ? 169 VAL   A CA  1 
ATOM   1353 C C   . VAL   A 1 180 ? 16.309  55.027 56.733  1.00 41.82  ? 169 VAL   A C   1 
ATOM   1354 O O   . VAL   A 1 180 ? 16.845  55.565 57.692  1.00 41.98  ? 169 VAL   A O   1 
ATOM   1355 C CB  . VAL   A 1 180 ? 17.215  52.711 56.228  1.00 42.12  ? 169 VAL   A CB  1 
ATOM   1356 C CG1 . VAL   A 1 180 ? 15.850  52.162 56.621  1.00 42.66  ? 169 VAL   A CG1 1 
ATOM   1357 C CG2 . VAL   A 1 180 ? 17.859  51.857 55.150  1.00 42.30  ? 169 VAL   A CG2 1 
ATOM   1358 N N   . LYS   A 1 181 ? 15.024  55.198 56.436  1.00 41.38  ? 170 LYS   A N   1 
ATOM   1359 C CA  . LYS   A 1 181 ? 14.087  55.956 57.242  1.00 41.03  ? 170 LYS   A CA  1 
ATOM   1360 C C   . LYS   A 1 181 ? 12.826  55.119 57.360  1.00 41.55  ? 170 LYS   A C   1 
ATOM   1361 O O   . LYS   A 1 181 ? 12.169  54.864 56.360  1.00 41.68  ? 170 LYS   A O   1 
ATOM   1362 C CB  . LYS   A 1 181 ? 13.753  57.279 56.554  1.00 41.32  ? 170 LYS   A CB  1 
ATOM   1363 C CG  . LYS   A 1 181 ? 14.946  58.180 56.331  1.00 42.38  ? 170 LYS   A CG  1 
ATOM   1364 C CD  . LYS   A 1 181 ? 15.456  58.760 57.623  1.00 43.55  ? 170 LYS   A CD  1 
ATOM   1365 C CE  . LYS   A 1 181 ? 16.563  59.734 57.341  1.00 45.40  ? 170 LYS   A CE  1 
ATOM   1366 N NZ  . LYS   A 1 181 ? 17.190  60.208 58.596  1.00 47.76  ? 170 LYS   A NZ  1 
ATOM   1367 N N   . ILE   A 1 182 ? 12.523  54.637 58.554  1.00 41.87  ? 171 ILE   A N   1 
ATOM   1368 C CA  . ILE   A 1 182 ? 11.318  53.857 58.782  1.00 42.72  ? 171 ILE   A CA  1 
ATOM   1369 C C   . ILE   A 1 182 ? 10.155  54.853 58.811  1.00 44.08  ? 171 ILE   A C   1 
ATOM   1370 O O   . ILE   A 1 182 ? 10.278  55.929 59.392  1.00 44.02  ? 171 ILE   A O   1 
ATOM   1371 C CB  . ILE   A 1 182 ? 11.464  53.042 60.082  1.00 42.95  ? 171 ILE   A CB  1 
ATOM   1372 C CG1 . ILE   A 1 182 ? 12.620  52.046 59.950  1.00 43.19  ? 171 ILE   A CG1 1 
ATOM   1373 C CG2 . ILE   A 1 182 ? 10.162  52.329 60.448  1.00 43.63  ? 171 ILE   A CG2 1 
ATOM   1374 C CD1 . ILE   A 1 182 ? 13.081  51.565 61.198  1.00 44.12  ? 171 ILE   A CD1 1 
ATOM   1375 N N   . ALA   A 1 183 ? 9.062   54.535 58.109  1.00 44.99  ? 172 ALA   A N   1 
ATOM   1376 C CA  . ALA   A 1 183 ? 7.914   55.423 57.990  1.00 46.06  ? 172 ALA   A CA  1 
ATOM   1377 C C   . ALA   A 1 183 ? 6.595   54.753 58.459  1.00 47.92  ? 172 ALA   A C   1 
ATOM   1378 O O   . ALA   A 1 183 ? 6.544   53.538 58.622  1.00 47.67  ? 172 ALA   A O   1 
ATOM   1379 C CB  . ALA   A 1 183 ? 7.799   55.908 56.546  1.00 45.77  ? 172 ALA   A CB  1 
ATOM   1380 N N   . ASP   A 1 184 ? 5.552   55.574 58.716  1.00 49.51  ? 173 ASP   A N   1 
ATOM   1381 C CA  . ASP   A 1 184 ? 4.209   55.212 59.147  1.00 51.07  ? 173 ASP   A CA  1 
ATOM   1382 C C   . ASP   A 1 184 ? 4.139   54.663 60.556  1.00 52.97  ? 173 ASP   A C   1 
ATOM   1383 O O   . ASP   A 1 184 ? 4.116   53.453 60.757  1.00 53.00  ? 173 ASP   A O   1 
ATOM   1384 C CB  . ASP   A 1 184 ? 3.522   54.266 58.159  1.00 52.85  ? 173 ASP   A CB  1 
ATOM   1385 C CG  . ASP   A 1 184 ? 2.019   54.468 58.036  1.00 58.32  ? 173 ASP   A CG  1 
ATOM   1386 O OD1 . ASP   A 1 184 ? 1.453   55.282 58.824  1.00 59.51  ? 173 ASP   A OD1 1 
ATOM   1387 O OD2 . ASP   A 1 184 ? 1.402   53.820 57.151  1.00 60.08  ? 173 ASP   A OD2 1 
ATOM   1388 N N   . MET   A 1 185 ? 4.101   55.554 61.543  1.00 54.76  ? 174 MET   A N   1 
ATOM   1389 C CA  . MET   A 1 185 ? 3.904   55.144 62.943  1.00 57.08  ? 174 MET   A CA  1 
ATOM   1390 C C   . MET   A 1 185 ? 2.413   55.210 63.338  1.00 59.62  ? 174 MET   A C   1 
ATOM   1391 O O   . MET   A 1 185 ? 2.107   55.134 64.521  1.00 59.89  ? 174 MET   A O   1 
ATOM   1392 C CB  . MET   A 1 185 ? 4.698   56.031 63.928  1.00 57.39  ? 174 MET   A CB  1 
ATOM   1393 C CG  . MET   A 1 185 ? 6.183   56.059 63.686  1.00 58.66  ? 174 MET   A CG  1 
ATOM   1394 S SD  . MET   A 1 185 ? 6.929   54.428 63.805  1.00 60.43  ? 174 MET   A SD  1 
ATOM   1395 C CE  . MET   A 1 185 ? 7.927   54.447 62.355  1.00 57.02  ? 174 MET   A CE  1 
ATOM   1396 N N   . GLY   A 1 186 ? 1.513   55.358 62.365  1.00 61.18  ? 175 GLY   A N   1 
ATOM   1397 C CA  . GLY   A 1 186 ? 0.095   55.510 62.614  1.00 63.18  ? 175 GLY   A CA  1 
ATOM   1398 C C   . GLY   A 1 186 ? -0.738  54.258 62.543  1.00 65.49  ? 175 GLY   A C   1 
ATOM   1399 O O   . GLY   A 1 186 ? -1.953  54.369 62.411  1.00 65.59  ? 175 GLY   A O   1 
ATOM   1400 N N   . PHE   A 1 187 ? -0.126  53.065 62.640  1.00 67.49  ? 176 PHE   A N   1 
ATOM   1401 C CA  . PHE   A 1 187 ? -0.920  51.836 62.649  1.00 69.91  ? 176 PHE   A CA  1 
ATOM   1402 C C   . PHE   A 1 187 ? -1.408  51.625 64.077  1.00 72.21  ? 176 PHE   A C   1 
ATOM   1403 O O   . PHE   A 1 187 ? -0.805  50.878 64.846  1.00 72.02  ? 176 PHE   A O   1 
ATOM   1404 C CB  . PHE   A 1 187 ? -0.136  50.631 62.131  1.00 70.16  ? 176 PHE   A CB  1 
ATOM   1405 C CG  . PHE   A 1 187 ? -0.996  49.467 61.699  1.00 71.37  ? 176 PHE   A CG  1 
ATOM   1406 C CD1 . PHE   A 1 187 ? -1.448  48.535 62.620  1.00 72.51  ? 176 PHE   A CD1 1 
ATOM   1407 C CD2 . PHE   A 1 187 ? -1.324  49.286 60.368  1.00 72.42  ? 176 PHE   A CD2 1 
ATOM   1408 C CE1 . PHE   A 1 187 ? -2.220  47.453 62.220  1.00 73.43  ? 176 PHE   A CE1 1 
ATOM   1409 C CE2 . PHE   A 1 187 ? -2.088  48.197 59.967  1.00 73.45  ? 176 PHE   A CE2 1 
ATOM   1410 C CZ  . PHE   A 1 187 ? -2.532  47.287 60.896  1.00 73.38  ? 176 PHE   A CZ  1 
ATOM   1411 N N   . ALA   A 1 188 ? -2.465  52.355 64.454  1.00 74.21  ? 177 ALA   A N   1 
ATOM   1412 C CA  . ALA   A 1 188 ? -3.029  52.256 65.794  1.00 76.64  ? 177 ALA   A CA  1 
ATOM   1413 C C   . ALA   A 1 188 ? -4.003  51.087 65.883  1.00 79.16  ? 177 ALA   A C   1 
ATOM   1414 O O   . ALA   A 1 188 ? -4.623  50.706 64.885  1.00 79.49  ? 177 ALA   A O   1 
ATOM   1415 C CB  . ALA   A 1 188 ? -3.733  53.550 66.173  1.00 76.62  ? 177 ALA   A CB  1 
ATOM   1416 N N   . ARG   A 1 189 ? -4.123  50.506 67.080  1.00 80.59  ? 178 ARG   A N   1 
ATOM   1417 C CA  . ARG   A 1 189 ? -5.042  49.397 67.340  1.00 82.41  ? 178 ARG   A CA  1 
ATOM   1418 C C   . ARG   A 1 189 ? -5.779  49.616 68.684  1.00 83.13  ? 178 ARG   A C   1 
ATOM   1419 O O   . ARG   A 1 189 ? -5.417  50.515 69.449  1.00 83.27  ? 178 ARG   A O   1 
ATOM   1420 C CB  . ARG   A 1 189 ? -4.289  48.046 67.320  1.00 84.85  ? 178 ARG   A CB  1 
ATOM   1421 C CG  . ARG   A 1 189 ? -3.877  47.557 65.924  1.00 89.82  ? 178 ARG   A CG  1 
ATOM   1422 C CD  . ARG   A 1 189 ? -5.079  47.281 65.031  1.00 94.44  ? 178 ARG   A CD  1 
ATOM   1423 N NE  . ARG   A 1 189 ? -4.723  46.520 63.830  1.00 98.39  ? 178 ARG   A NE  1 
ATOM   1424 C CZ  . ARG   A 1 189 ? -4.774  45.191 63.739  1.00 101.12 ? 178 ARG   A CZ  1 
ATOM   1425 N NH1 . ARG   A 1 189 ? -4.434  44.582 62.609  1.00 100.64 ? 178 ARG   A NH1 1 
ATOM   1426 N NH2 . ARG   A 1 189 ? -5.143  44.459 64.784  1.00 101.34 ? 178 ARG   A NH2 1 
ATOM   1427 N N   . LEU   A 1 190 ? -6.818  48.815 68.966  1.00 83.44  ? 179 LEU   A N   1 
ATOM   1428 C CA  . LEU   A 1 190 ? -7.537  48.923 70.237  1.00 84.31  ? 179 LEU   A CA  1 
ATOM   1429 C C   . LEU   A 1 190 ? -7.183  47.753 71.178  1.00 84.71  ? 179 LEU   A C   1 
ATOM   1430 O O   . LEU   A 1 190 ? -6.292  47.865 72.024  1.00 84.78  ? 179 LEU   A O   1 
ATOM   1431 C CB  . LEU   A 1 190 ? -9.050  48.990 70.006  1.00 84.71  ? 179 LEU   A CB  1 
ATOM   1432 C CG  . LEU   A 1 190 ? -9.566  50.301 69.445  1.00 86.40  ? 179 LEU   A CG  1 
ATOM   1433 C CD1 . LEU   A 1 190 ? -11.019 50.177 69.044  1.00 87.12  ? 179 LEU   A CD1 1 
ATOM   1434 C CD2 . LEU   A 1 190 ? -9.384  51.421 70.439  1.00 87.06  ? 179 LEU   A CD2 1 
ATOM   1435 N N   . VAL   A 1 206 ? -5.575  43.793 52.262  1.00 68.96  ? 195 VAL   A N   1 
ATOM   1436 C CA  . VAL   A 1 206 ? -5.824  42.414 51.816  1.00 69.31  ? 195 VAL   A CA  1 
ATOM   1437 C C   . VAL   A 1 206 ? -4.546  41.566 51.638  1.00 68.99  ? 195 VAL   A C   1 
ATOM   1438 O O   . VAL   A 1 206 ? -4.645  40.405 51.234  1.00 69.19  ? 195 VAL   A O   1 
ATOM   1439 C CB  . VAL   A 1 206 ? -6.696  42.354 50.537  1.00 70.26  ? 195 VAL   A CB  1 
ATOM   1440 C CG1 . VAL   A 1 206 ? -8.140  42.754 50.833  1.00 70.77  ? 195 VAL   A CG1 1 
ATOM   1441 C CG2 . VAL   A 1 206 ? -6.100  43.215 49.427  1.00 70.82  ? 195 VAL   A CG2 1 
ATOM   1442 N N   . THR   A 1 207 ? -3.358  42.135 51.918  1.00 68.15  ? 196 THR   A N   1 
ATOM   1443 C CA  . THR   A 1 207 ? -2.097  41.397 51.784  1.00 67.56  ? 196 THR   A CA  1 
ATOM   1444 C C   . THR   A 1 207 ? -1.470  41.139 53.172  1.00 65.72  ? 196 THR   A C   1 
ATOM   1445 O O   . THR   A 1 207 ? -1.363  42.051 53.995  1.00 66.16  ? 196 THR   A O   1 
ATOM   1446 C CB  . THR   A 1 207 ? -1.173  42.094 50.759  1.00 69.36  ? 196 THR   A CB  1 
ATOM   1447 O OG1 . THR   A 1 207 ? -1.473  41.554 49.467  1.00 70.37  ? 196 THR   A OG1 1 
ATOM   1448 C CG2 . THR   A 1 207 ? 0.337   41.921 51.071  1.00 69.79  ? 196 THR   A CG2 1 
ATOM   1449 N N   . PHE   A 1 208 ? -1.082  39.894 53.431  1.00 63.52  ? 197 PHE   A N   1 
ATOM   1450 C CA  . PHE   A 1 208 ? -0.519  39.520 54.725  1.00 61.93  ? 197 PHE   A CA  1 
ATOM   1451 C C   . PHE   A 1 208 ? 0.868   38.871 54.584  1.00 59.47  ? 197 PHE   A C   1 
ATOM   1452 O O   . PHE   A 1 208 ? 1.264   38.102 55.465  1.00 59.64  ? 197 PHE   A O   1 
ATOM   1453 C CB  . PHE   A 1 208 ? -1.486  38.574 55.475  1.00 62.01  ? 197 PHE   A CB  1 
ATOM   1454 C CG  . PHE   A 1 208 ? -2.920  39.050 55.488  1.00 62.81  ? 197 PHE   A CG  1 
ATOM   1455 C CD1 . PHE   A 1 208 ? -3.341  40.013 56.388  1.00 63.70  ? 197 PHE   A CD1 1 
ATOM   1456 C CD2 . PHE   A 1 208 ? -3.836  38.567 54.567  1.00 63.63  ? 197 PHE   A CD2 1 
ATOM   1457 C CE1 . PHE   A 1 208 ? -4.654  40.469 56.380  1.00 64.42  ? 197 PHE   A CE1 1 
ATOM   1458 C CE2 . PHE   A 1 208 ? -5.147  39.029 54.558  1.00 64.32  ? 197 PHE   A CE2 1 
ATOM   1459 C CZ  . PHE   A 1 208 ? -5.547  39.980 55.461  1.00 64.14  ? 197 PHE   A CZ  1 
ATOM   1460 N N   . TRP   A 1 209 ? 1.615   39.191 53.502  1.00 56.77  ? 198 TRP   A N   1 
ATOM   1461 C CA  . TRP   A 1 209 ? 2.931   38.591 53.255  1.00 54.72  ? 198 TRP   A CA  1 
ATOM   1462 C C   . TRP   A 1 209 ? 3.931   38.817 54.380  1.00 53.39  ? 198 TRP   A C   1 
ATOM   1463 O O   . TRP   A 1 209 ? 4.892   38.066 54.505  1.00 53.51  ? 198 TRP   A O   1 
ATOM   1464 C CB  . TRP   A 1 209 ? 3.543   39.074 51.925  1.00 54.15  ? 198 TRP   A CB  1 
ATOM   1465 C CG  . TRP   A 1 209 ? 2.647   38.985 50.722  1.00 54.27  ? 198 TRP   A CG  1 
ATOM   1466 C CD1 . TRP   A 1 209 ? 1.548   38.190 50.566  1.00 55.11  ? 198 TRP   A CD1 1 
ATOM   1467 C CD2 . TRP   A 1 209 ? 2.815   39.684 49.484  1.00 54.07  ? 198 TRP   A CD2 1 
ATOM   1468 N NE1 . TRP   A 1 209 ? 1.005   38.375 49.318  1.00 55.30  ? 198 TRP   A NE1 1 
ATOM   1469 C CE2 . TRP   A 1 209 ? 1.764   39.290 48.633  1.00 54.89  ? 198 TRP   A CE2 1 
ATOM   1470 C CE3 . TRP   A 1 209 ? 3.742   40.616 49.016  1.00 54.23  ? 198 TRP   A CE3 1 
ATOM   1471 C CZ2 . TRP   A 1 209 ? 1.599   39.825 47.360  1.00 55.11  ? 198 TRP   A CZ2 1 
ATOM   1472 C CZ3 . TRP   A 1 209 ? 3.587   41.125 47.745  1.00 54.72  ? 198 TRP   A CZ3 1 
ATOM   1473 C CH2 . TRP   A 1 209 ? 2.538   40.715 46.926  1.00 54.84  ? 198 TRP   A CH2 1 
ATOM   1474 N N   . TYR   A 1 210 ? 3.721   39.855 55.191  1.00 52.13  ? 199 TYR   A N   1 
ATOM   1475 C CA  . TYR   A 1 210 ? 4.630   40.220 56.277  1.00 50.90  ? 199 TYR   A CA  1 
ATOM   1476 C C   . TYR   A 1 210 ? 4.039   39.961 57.661  1.00 51.31  ? 199 TYR   A C   1 
ATOM   1477 O O   . TYR   A 1 210 ? 4.677   40.292 58.660  1.00 51.63  ? 199 TYR   A O   1 
ATOM   1478 C CB  . TYR   A 1 210 ? 5.111   41.686 56.117  1.00 49.49  ? 199 TYR   A CB  1 
ATOM   1479 C CG  . TYR   A 1 210 ? 5.606   41.958 54.714  1.00 48.48  ? 199 TYR   A CG  1 
ATOM   1480 C CD1 . TYR   A 1 210 ? 4.725   42.324 53.706  1.00 48.81  ? 199 TYR   A CD1 1 
ATOM   1481 C CD2 . TYR   A 1 210 ? 6.925   41.711 54.363  1.00 48.66  ? 199 TYR   A CD2 1 
ATOM   1482 C CE1 . TYR   A 1 210 ? 5.148   42.464 52.391  1.00 49.53  ? 199 TYR   A CE1 1 
ATOM   1483 C CE2 . TYR   A 1 210 ? 7.361   41.847 53.051  1.00 49.40  ? 199 TYR   A CE2 1 
ATOM   1484 C CZ  . TYR   A 1 210 ? 6.466   42.212 52.064  1.00 50.28  ? 199 TYR   A CZ  1 
ATOM   1485 O OH  . TYR   A 1 210 ? 6.882   42.386 50.766  1.00 51.23  ? 199 TYR   A OH  1 
ATOM   1486 N N   . ARG   A 1 211 ? 2.844   39.346 57.737  1.00 51.19  ? 200 ARG   A N   1 
ATOM   1487 C CA  . ARG   A 1 211 ? 2.230   39.051 59.021  1.00 51.54  ? 200 ARG   A CA  1 
ATOM   1488 C C   . ARG   A 1 211 ? 2.766   37.735 59.565  1.00 50.79  ? 200 ARG   A C   1 
ATOM   1489 O O   . ARG   A 1 211 ? 2.777   36.712 58.872  1.00 51.06  ? 200 ARG   A O   1 
ATOM   1490 C CB  . ARG   A 1 211 ? 0.684   39.096 58.963  1.00 53.65  ? 200 ARG   A CB  1 
ATOM   1491 C CG  . ARG   A 1 211 ? 0.089   40.380 58.344  1.00 58.89  ? 200 ARG   A CG  1 
ATOM   1492 C CD  . ARG   A 1 211 ? 0.804   41.686 58.724  1.00 64.52  ? 200 ARG   A CD  1 
ATOM   1493 N NE  . ARG   A 1 211 ? -0.109  42.823 58.845  1.00 69.62  ? 200 ARG   A NE  1 
ATOM   1494 C CZ  . ARG   A 1 211 ? -0.227  43.579 59.934  1.00 72.84  ? 200 ARG   A CZ  1 
ATOM   1495 N NH1 . ARG   A 1 211 ? -1.091  44.589 59.959  1.00 72.53  ? 200 ARG   A NH1 1 
ATOM   1496 N NH2 . ARG   A 1 211 ? 0.527   43.339 61.004  1.00 72.93  ? 200 ARG   A NH2 1 
ATOM   1497 N N   . ALA   A 1 212 ? 3.273   37.791 60.797  1.00 49.39  ? 201 ALA   A N   1 
ATOM   1498 C CA  . ALA   A 1 212 ? 3.831   36.657 61.505  1.00 48.43  ? 201 ALA   A CA  1 
ATOM   1499 C C   . ALA   A 1 212 ? 2.800   35.519 61.614  1.00 47.67  ? 201 ALA   A C   1 
ATOM   1500 O O   . ALA   A 1 212 ? 1.589   35.770 61.583  1.00 47.84  ? 201 ALA   A O   1 
ATOM   1501 C CB  . ALA   A 1 212 ? 4.273   37.114 62.879  1.00 48.35  ? 201 ALA   A CB  1 
ATOM   1502 N N   . PRO   A 1 213 ? 3.246   34.253 61.666  1.00 46.71  ? 202 PRO   A N   1 
ATOM   1503 C CA  . PRO   A 1 213 ? 2.283   33.143 61.725  1.00 46.30  ? 202 PRO   A CA  1 
ATOM   1504 C C   . PRO   A 1 213 ? 1.336   33.209 62.921  1.00 46.30  ? 202 PRO   A C   1 
ATOM   1505 O O   . PRO   A 1 213 ? 0.185   32.805 62.802  1.00 46.66  ? 202 PRO   A O   1 
ATOM   1506 C CB  . PRO   A 1 213 ? 3.175   31.898 61.758  1.00 46.70  ? 202 PRO   A CB  1 
ATOM   1507 C CG  . PRO   A 1 213 ? 4.488   32.386 62.247  1.00 47.18  ? 202 PRO   A CG  1 
ATOM   1508 C CD  . PRO   A 1 213 ? 4.633   33.760 61.683  1.00 45.84  ? 202 PRO   A CD  1 
ATOM   1509 N N   . GLU   A 1 214 ? 1.801   33.735 64.060  1.00 45.78  ? 203 GLU   A N   1 
ATOM   1510 C CA  . GLU   A 1 214 ? 0.972   33.830 65.255  1.00 45.47  ? 203 GLU   A CA  1 
ATOM   1511 C C   . GLU   A 1 214 ? -0.200  34.779 65.032  1.00 45.03  ? 203 GLU   A C   1 
ATOM   1512 O O   . GLU   A 1 214 ? -1.302  34.473 65.459  1.00 45.17  ? 203 GLU   A O   1 
ATOM   1513 C CB  . GLU   A 1 214 ? 1.809   34.200 66.496  1.00 47.21  ? 203 GLU   A CB  1 
ATOM   1514 C CG  . GLU   A 1 214 ? 2.391   35.606 66.477  1.00 50.59  ? 203 GLU   A CG  1 
ATOM   1515 C CD  . GLU   A 1 214 ? 3.852   35.705 66.090  1.00 55.46  ? 203 GLU   A CD  1 
ATOM   1516 O OE1 . GLU   A 1 214 ? 4.284   34.949 65.193  1.00 56.67  ? 203 GLU   A OE1 1 
ATOM   1517 O OE2 . GLU   A 1 214 ? 4.567   36.549 66.676  1.00 57.20  ? 203 GLU   A OE2 1 
ATOM   1518 N N   . LEU   A 1 215 ? -0.003  35.868 64.282  1.00 44.46  ? 204 LEU   A N   1 
ATOM   1519 C CA  . LEU   A 1 215 ? -1.090  36.792 63.974  1.00 44.50  ? 204 LEU   A CA  1 
ATOM   1520 C C   . LEU   A 1 215 ? -2.142  36.100 63.121  1.00 45.88  ? 204 LEU   A C   1 
ATOM   1521 O O   . LEU   A 1 215 ? -3.334  36.261 63.373  1.00 46.56  ? 204 LEU   A O   1 
ATOM   1522 C CB  . LEU   A 1 215 ? -0.564  38.022 63.257  1.00 43.81  ? 204 LEU   A CB  1 
ATOM   1523 C CG  . LEU   A 1 215 ? 0.012   39.087 64.154  1.00 44.41  ? 204 LEU   A CG  1 
ATOM   1524 C CD1 . LEU   A 1 215 ? 0.661   40.156 63.337  1.00 45.17  ? 204 LEU   A CD1 1 
ATOM   1525 C CD2 . LEU   A 1 215 ? -1.041  39.658 65.104  1.00 44.30  ? 204 LEU   A CD2 1 
ATOM   1526 N N   . LEU   A 1 216 ? -1.705  35.291 62.141  1.00 46.02  ? 205 LEU   A N   1 
ATOM   1527 C CA  . LEU   A 1 216 ? -2.606  34.514 61.287  1.00 46.61  ? 205 LEU   A CA  1 
ATOM   1528 C C   . LEU   A 1 216 ? -3.383  33.432 62.064  1.00 47.31  ? 205 LEU   A C   1 
ATOM   1529 O O   . LEU   A 1 216 ? -4.313  32.844 61.527  1.00 47.73  ? 205 LEU   A O   1 
ATOM   1530 C CB  . LEU   A 1 216 ? -1.823  33.877 60.135  1.00 46.77  ? 205 LEU   A CB  1 
ATOM   1531 C CG  . LEU   A 1 216 ? -1.025  34.859 59.297  1.00 48.40  ? 205 LEU   A CG  1 
ATOM   1532 C CD1 . LEU   A 1 216 ? -0.003  34.147 58.447  1.00 49.11  ? 205 LEU   A CD1 1 
ATOM   1533 C CD2 . LEU   A 1 216 ? -1.937  35.702 58.446  1.00 49.24  ? 205 LEU   A CD2 1 
ATOM   1534 N N   . LEU   A 1 217 ? -2.997  33.157 63.306  1.00 47.53  ? 206 LEU   A N   1 
ATOM   1535 C CA  . LEU   A 1 217 ? -3.670  32.185 64.153  1.00 48.56  ? 206 LEU   A CA  1 
ATOM   1536 C C   . LEU   A 1 217 ? -4.462  32.842 65.306  1.00 50.34  ? 206 LEU   A C   1 
ATOM   1537 O O   . LEU   A 1 217 ? -4.809  32.183 66.284  1.00 50.14  ? 206 LEU   A O   1 
ATOM   1538 C CB  . LEU   A 1 217 ? -2.672  31.126 64.648  1.00 48.22  ? 206 LEU   A CB  1 
ATOM   1539 C CG  . LEU   A 1 217 ? -2.143  30.259 63.516  1.00 48.93  ? 206 LEU   A CG  1 
ATOM   1540 C CD1 . LEU   A 1 217 ? -0.821  29.638 63.853  1.00 49.46  ? 206 LEU   A CD1 1 
ATOM   1541 C CD2 . LEU   A 1 217 ? -3.172  29.243 63.077  1.00 49.30  ? 206 LEU   A CD2 1 
ATOM   1542 N N   . GLY   A 1 218 ? -4.809  34.117 65.137  1.00 51.85  ? 207 GLY   A N   1 
ATOM   1543 C CA  . GLY   A 1 218 ? -5.626  34.838 66.092  1.00 53.47  ? 207 GLY   A CA  1 
ATOM   1544 C C   . GLY   A 1 218 ? -4.926  35.318 67.339  1.00 55.23  ? 207 GLY   A C   1 
ATOM   1545 O O   . GLY   A 1 218 ? -5.576  35.455 68.373  1.00 55.75  ? 207 GLY   A O   1 
ATOM   1546 N N   . ALA   A 1 219 ? -3.622  35.664 67.264  1.00 56.03  ? 208 ALA   A N   1 
ATOM   1547 C CA  . ALA   A 1 219 ? -2.920  36.247 68.423  1.00 57.25  ? 208 ALA   A CA  1 
ATOM   1548 C C   . ALA   A 1 219 ? -3.578  37.590 68.729  1.00 58.41  ? 208 ALA   A C   1 
ATOM   1549 O O   . ALA   A 1 219 ? -3.867  38.348 67.805  1.00 58.15  ? 208 ALA   A O   1 
ATOM   1550 C CB  . ALA   A 1 219 ? -1.455  36.467 68.102  1.00 57.56  ? 208 ALA   A CB  1 
ATOM   1551 N N   . ARG   A 1 220 ? -3.911  37.831 69.993  1.00 59.50  ? 209 ARG   A N   1 
ATOM   1552 C CA  . ARG   A 1 220 ? -4.670  39.028 70.368  1.00 60.70  ? 209 ARG   A CA  1 
ATOM   1553 C C   . ARG   A 1 220 ? -3.824  40.281 70.643  1.00 60.81  ? 209 ARG   A C   1 
ATOM   1554 O O   . ARG   A 1 220 ? -4.388  41.295 71.040  1.00 61.01  ? 209 ARG   A O   1 
ATOM   1555 C CB  . ARG   A 1 220 ? -5.609  38.745 71.567  1.00 62.86  ? 209 ARG   A CB  1 
ATOM   1556 C CG  . ARG   A 1 220 ? -5.490  37.341 72.173  1.00 67.48  ? 209 ARG   A CG  1 
ATOM   1557 C CD  . ARG   A 1 220 ? -6.829  36.629 72.301  1.00 72.54  ? 209 ARG   A CD  1 
ATOM   1558 N NE  . ARG   A 1 220 ? -7.541  36.497 71.022  1.00 76.46  ? 209 ARG   A NE  1 
ATOM   1559 C CZ  . ARG   A 1 220 ? -8.533  35.634 70.802  1.00 78.33  ? 209 ARG   A CZ  1 
ATOM   1560 N NH1 . ARG   A 1 220 ? -8.917  34.792 71.759  1.00 77.31  ? 209 ARG   A NH1 1 
ATOM   1561 N NH2 . ARG   A 1 220 ? -9.129  35.586 69.616  1.00 77.97  ? 209 ARG   A NH2 1 
ATOM   1562 N N   . HIS   A 1 221 ? -2.493  40.230 70.445  1.00 60.40  ? 210 HIS   A N   1 
ATOM   1563 C CA  . HIS   A 1 221 ? -1.638  41.391 70.723  1.00 60.10  ? 210 HIS   A CA  1 
ATOM   1564 C C   . HIS   A 1 221 ? -0.501  41.542 69.731  1.00 58.79  ? 210 HIS   A C   1 
ATOM   1565 O O   . HIS   A 1 221 ? 0.030   40.552 69.234  1.00 59.30  ? 210 HIS   A O   1 
ATOM   1566 C CB  . HIS   A 1 221 ? -0.984  41.279 72.127  1.00 61.68  ? 210 HIS   A CB  1 
ATOM   1567 C CG  . HIS   A 1 221 ? -1.888  40.811 73.220  1.00 65.26  ? 210 HIS   A CG  1 
ATOM   1568 N ND1 . HIS   A 1 221 ? -2.892  41.625 73.727  1.00 67.32  ? 210 HIS   A ND1 1 
ATOM   1569 C CD2 . HIS   A 1 221 ? -1.909  39.625 73.873  1.00 66.87  ? 210 HIS   A CD2 1 
ATOM   1570 C CE1 . HIS   A 1 221 ? -3.495  40.907 74.662  1.00 68.21  ? 210 HIS   A CE1 1 
ATOM   1571 N NE2 . HIS   A 1 221 ? -2.935  39.696 74.790  1.00 68.27  ? 210 HIS   A NE2 1 
ATOM   1572 N N   . TYR   A 1 222 ? -0.056  42.775 69.526  1.00 57.21  ? 211 TYR   A N   1 
ATOM   1573 C CA  . TYR   A 1 222 ? 1.127   43.031 68.730  1.00 56.29  ? 211 TYR   A CA  1 
ATOM   1574 C C   . TYR   A 1 222 ? 2.321   42.982 69.690  1.00 54.59  ? 211 TYR   A C   1 
ATOM   1575 O O   . TYR   A 1 222 ? 2.224   43.434 70.831  1.00 54.96  ? 211 TYR   A O   1 
ATOM   1576 C CB  . TYR   A 1 222 ? 1.037   44.372 68.004  1.00 56.94  ? 211 TYR   A CB  1 
ATOM   1577 C CG  . TYR   A 1 222 ? 0.305   44.263 66.686  1.00 58.71  ? 211 TYR   A CG  1 
ATOM   1578 C CD1 . TYR   A 1 222 ? 0.893   43.648 65.591  1.00 59.99  ? 211 TYR   A CD1 1 
ATOM   1579 C CD2 . TYR   A 1 222 ? -0.985  44.758 66.540  1.00 60.24  ? 211 TYR   A CD2 1 
ATOM   1580 C CE1 . TYR   A 1 222 ? 0.224   43.541 64.377  1.00 61.17  ? 211 TYR   A CE1 1 
ATOM   1581 C CE2 . TYR   A 1 222 ? -1.665  44.657 65.330  1.00 61.40  ? 211 TYR   A CE2 1 
ATOM   1582 C CZ  . TYR   A 1 222 ? -1.059  44.037 64.252  1.00 62.43  ? 211 TYR   A CZ  1 
ATOM   1583 O OH  . TYR   A 1 222 ? -1.712  43.924 63.048  1.00 64.35  ? 211 TYR   A OH  1 
ATOM   1584 N N   . THR   A 1 223 ? 3.426   42.371 69.258  1.00 52.25  ? 212 THR   A N   1 
ATOM   1585 C CA  . THR   A 1 223 ? 4.643   42.239 70.054  1.00 50.01  ? 212 THR   A CA  1 
ATOM   1586 C C   . THR   A 1 223 ? 5.881   42.659 69.215  1.00 47.95  ? 212 THR   A C   1 
ATOM   1587 O O   . THR   A 1 223 ? 5.756   42.929 68.020  1.00 48.16  ? 212 THR   A O   1 
ATOM   1588 C CB  . THR   A 1 223 ? 4.753   40.797 70.518  1.00 50.75  ? 212 THR   A CB  1 
ATOM   1589 O OG1 . THR   A 1 223 ? 4.839   39.970 69.363  1.00 51.48  ? 212 THR   A OG1 1 
ATOM   1590 C CG2 . THR   A 1 223 ? 3.590   40.376 71.372  1.00 51.31  ? 212 THR   A CG2 1 
ATOM   1591 N N   . LYS   A 1 224 ? 7.068   42.730 69.839  1.00 45.84  ? 213 LYS   A N   1 
ATOM   1592 C CA  . LYS   A 1 224 ? 8.299   43.064 69.144  1.00 44.25  ? 213 LYS   A CA  1 
ATOM   1593 C C   . LYS   A 1 224 ? 8.616   41.984 68.078  1.00 44.00  ? 213 LYS   A C   1 
ATOM   1594 O O   . LYS   A 1 224 ? 9.021   42.310 66.960  1.00 43.89  ? 213 LYS   A O   1 
ATOM   1595 C CB  . LYS   A 1 224 ? 9.441   43.165 70.164  1.00 44.21  ? 213 LYS   A CB  1 
ATOM   1596 C CG  . LYS   A 1 224 ? 9.181   44.124 71.305  1.00 46.19  ? 213 LYS   A CG  1 
ATOM   1597 C CD  . LYS   A 1 224 ? 10.424  44.339 72.152  1.00 50.11  ? 213 LYS   A CD  1 
ATOM   1598 C CE  . LYS   A 1 224 ? 10.275  45.491 73.125  1.00 54.15  ? 213 LYS   A CE  1 
ATOM   1599 N NZ  . LYS   A 1 224 ? 11.543  45.778 73.853  1.00 56.41  ? 213 LYS   A NZ  1 
ATOM   1600 N N   . ALA   A 1 225 ? 8.403   40.689 68.427  1.00 43.37  ? 214 ALA   A N   1 
ATOM   1601 C CA  . ALA   A 1 225 ? 8.651   39.559 67.528  1.00 42.50  ? 214 ALA   A CA  1 
ATOM   1602 C C   . ALA   A 1 225 ? 7.819   39.618 66.262  1.00 41.83  ? 214 ALA   A C   1 
ATOM   1603 O O   . ALA   A 1 225 ? 8.209   39.013 65.271  1.00 42.30  ? 214 ALA   A O   1 
ATOM   1604 C CB  . ALA   A 1 225 ? 8.417   38.239 68.247  1.00 42.48  ? 214 ALA   A CB  1 
ATOM   1605 N N   . ILE   A 1 226 ? 6.682   40.329 66.273  1.00 40.65  ? 215 ILE   A N   1 
ATOM   1606 C CA  . ILE   A 1 226 ? 5.878   40.491 65.073  1.00 39.98  ? 215 ILE   A CA  1 
ATOM   1607 C C   . ILE   A 1 226 ? 6.650   41.387 64.092  1.00 39.07  ? 215 ILE   A C   1 
ATOM   1608 O O   . ILE   A 1 226 ? 6.734   41.065 62.909  1.00 39.22  ? 215 ILE   A O   1 
ATOM   1609 C CB  . ILE   A 1 226 ? 4.475   41.007 65.439  1.00 40.91  ? 215 ILE   A CB  1 
ATOM   1610 C CG1 . ILE   A 1 226 ? 3.624   39.850 65.978  1.00 41.62  ? 215 ILE   A CG1 1 
ATOM   1611 C CG2 . ILE   A 1 226 ? 3.783   41.695 64.246  1.00 41.76  ? 215 ILE   A CG2 1 
ATOM   1612 C CD1 . ILE   A 1 226 ? 2.345   40.270 66.599  1.00 42.62  ? 215 ILE   A CD1 1 
ATOM   1613 N N   . ASP   A 1 227 ? 7.285   42.458 64.592  1.00 38.38  ? 216 ASP   A N   1 
ATOM   1614 C CA  . ASP   A 1 227 ? 8.123   43.331 63.766  1.00 38.11  ? 216 ASP   A CA  1 
ATOM   1615 C C   . ASP   A 1 227 ? 9.376   42.596 63.312  1.00 37.77  ? 216 ASP   A C   1 
ATOM   1616 O O   . ASP   A 1 227 ? 9.849   42.845 62.211  1.00 38.03  ? 216 ASP   A O   1 
ATOM   1617 C CB  . ASP   A 1 227 ? 8.550   44.574 64.541  1.00 39.45  ? 216 ASP   A CB  1 
ATOM   1618 C CG  . ASP   A 1 227 ? 7.434   45.505 64.945  1.00 44.07  ? 216 ASP   A CG  1 
ATOM   1619 O OD1 . ASP   A 1 227 ? 6.270   45.263 64.524  1.00 44.31  ? 216 ASP   A OD1 1 
ATOM   1620 O OD2 . ASP   A 1 227 ? 7.721   46.496 65.673  1.00 46.10  ? 216 ASP   A OD2 1 
ATOM   1621 N N   . ILE   A 1 228 ? 9.934   41.716 64.167  1.00 37.01  ? 217 ILE   A N   1 
ATOM   1622 C CA  . ILE   A 1 228 ? 11.114  40.933 63.832  1.00 36.58  ? 217 ILE   A CA  1 
ATOM   1623 C C   . ILE   A 1 228 ? 10.791  39.949 62.720  1.00 36.44  ? 217 ILE   A C   1 
ATOM   1624 O O   . ILE   A 1 228 ? 11.563  39.883 61.758  1.00 37.19  ? 217 ILE   A O   1 
ATOM   1625 C CB  . ILE   A 1 228 ? 11.755  40.297 65.086  1.00 36.78  ? 217 ILE   A CB  1 
ATOM   1626 C CG1 . ILE   A 1 228 ? 12.522  41.359 65.864  1.00 38.11  ? 217 ILE   A CG1 1 
ATOM   1627 C CG2 . ILE   A 1 228 ? 12.656  39.128 64.756  1.00 36.72  ? 217 ILE   A CG2 1 
ATOM   1628 C CD1 . ILE   A 1 228 ? 13.607  42.049 65.064  1.00 39.47  ? 217 ILE   A CD1 1 
ATOM   1629 N N   . TRP   A 1 229 ? 9.590   39.300 62.748  1.00 35.16  ? 218 TRP   A N   1 
ATOM   1630 C CA  . TRP   A 1 229 ? 9.172   38.386 61.676  1.00 34.56  ? 218 TRP   A CA  1 
ATOM   1631 C C   . TRP   A 1 229 ? 9.159   39.127 60.350  1.00 34.69  ? 218 TRP   A C   1 
ATOM   1632 O O   . TRP   A 1 229 ? 9.714   38.630 59.367  1.00 34.82  ? 218 TRP   A O   1 
ATOM   1633 C CB  . TRP   A 1 229 ? 7.783   37.769 61.942  1.00 34.11  ? 218 TRP   A CB  1 
ATOM   1634 C CG  . TRP   A 1 229 ? 7.272   36.919 60.801  1.00 34.32  ? 218 TRP   A CG  1 
ATOM   1635 C CD1 . TRP   A 1 229 ? 6.503   37.328 59.747  1.00 34.97  ? 218 TRP   A CD1 1 
ATOM   1636 C CD2 . TRP   A 1 229 ? 7.532   35.520 60.587  1.00 34.22  ? 218 TRP   A CD2 1 
ATOM   1637 N NE1 . TRP   A 1 229 ? 6.281   36.276 58.885  1.00 35.09  ? 218 TRP   A NE1 1 
ATOM   1638 C CE2 . TRP   A 1 229 ? 6.900   35.154 59.380  1.00 34.77  ? 218 TRP   A CE2 1 
ATOM   1639 C CE3 . TRP   A 1 229 ? 8.260   34.548 61.283  1.00 34.37  ? 218 TRP   A CE3 1 
ATOM   1640 C CZ2 . TRP   A 1 229 ? 6.962   33.858 58.874  1.00 34.87  ? 218 TRP   A CZ2 1 
ATOM   1641 C CZ3 . TRP   A 1 229 ? 8.345   33.274 60.755  1.00 34.70  ? 218 TRP   A CZ3 1 
ATOM   1642 C CH2 . TRP   A 1 229 ? 7.694   32.940 59.573  1.00 34.62  ? 218 TRP   A CH2 1 
ATOM   1643 N N   . ALA   A 1 230 ? 8.571   40.344 60.358  1.00 34.38  ? 219 ALA   A N   1 
ATOM   1644 C CA  . ALA   A 1 230 ? 8.449   41.242 59.214  1.00 34.45  ? 219 ALA   A CA  1 
ATOM   1645 C C   . ALA   A 1 230 ? 9.808   41.624 58.624  1.00 34.01  ? 219 ALA   A C   1 
ATOM   1646 O O   . ALA   A 1 230 ? 9.953   41.641 57.404  1.00 33.73  ? 219 ALA   A O   1 
ATOM   1647 C CB  . ALA   A 1 230 ? 7.694   42.488 59.631  1.00 34.93  ? 219 ALA   A CB  1 
ATOM   1648 N N   . ILE   A 1 231 ? 10.804  41.894 59.485  1.00 33.90  ? 220 ILE   A N   1 
ATOM   1649 C CA  . ILE   A 1 231 ? 12.169  42.214 59.063  1.00 34.65  ? 220 ILE   A CA  1 
ATOM   1650 C C   . ILE   A 1 231 ? 12.796  41.028 58.315  1.00 36.07  ? 220 ILE   A C   1 
ATOM   1651 O O   . ILE   A 1 231 ? 13.512  41.225 57.338  1.00 36.44  ? 220 ILE   A O   1 
ATOM   1652 C CB  . ILE   A 1 231 ? 13.026  42.662 60.273  1.00 34.78  ? 220 ILE   A CB  1 
ATOM   1653 C CG1 . ILE   A 1 231 ? 12.543  44.026 60.812  1.00 34.91  ? 220 ILE   A CG1 1 
ATOM   1654 C CG2 . ILE   A 1 231 ? 14.522  42.712 59.924  1.00 35.23  ? 220 ILE   A CG2 1 
ATOM   1655 C CD1 . ILE   A 1 231 ? 13.140  44.414 62.101  1.00 35.49  ? 220 ILE   A CD1 1 
ATOM   1656 N N   . GLY   A 1 232 ? 12.484  39.811 58.755  1.00 36.52  ? 221 GLY   A N   1 
ATOM   1657 C CA  . GLY   A 1 232 ? 12.927  38.582 58.118  1.00 36.88  ? 221 GLY   A CA  1 
ATOM   1658 C C   . GLY   A 1 232 ? 12.363  38.449 56.719  1.00 37.02  ? 221 GLY   A C   1 
ATOM   1659 O O   . GLY   A 1 232 ? 13.103  38.101 55.798  1.00 37.55  ? 221 GLY   A O   1 
ATOM   1660 N N   . CYS   A 1 233 ? 11.070  38.773 56.522  1.00 36.61  ? 222 CYS   A N   1 
ATOM   1661 C CA  . CYS   A 1 233 ? 10.461  38.727 55.180  1.00 36.66  ? 222 CYS   A CA  1 
ATOM   1662 C C   . CYS   A 1 233 ? 11.121  39.738 54.257  1.00 36.25  ? 222 CYS   A C   1 
ATOM   1663 O O   . CYS   A 1 233 ? 11.277  39.457 53.075  1.00 36.21  ? 222 CYS   A O   1 
ATOM   1664 C CB  . CYS   A 1 233 ? 8.952   38.943 55.226  1.00 37.33  ? 222 CYS   A CB  1 
ATOM   1665 S SG  . CYS   A 1 233 ? 8.077   37.908 56.423  1.00 40.57  ? 222 CYS   A SG  1 
ATOM   1666 N N   . ILE   A 1 234 ? 11.478  40.921 54.779  1.00 35.84  ? 223 ILE   A N   1 
ATOM   1667 C CA  . ILE   A 1 234 ? 12.155  41.920 53.972  1.00 36.10  ? 223 ILE   A CA  1 
ATOM   1668 C C   . ILE   A 1 234 ? 13.560  41.423 53.642  1.00 37.69  ? 223 ILE   A C   1 
ATOM   1669 O O   . ILE   A 1 234 ? 13.968  41.521 52.493  1.00 38.52  ? 223 ILE   A O   1 
ATOM   1670 C CB  . ILE   A 1 234 ? 12.155  43.310 54.639  1.00 35.71  ? 223 ILE   A CB  1 
ATOM   1671 C CG1 . ILE   A 1 234 ? 10.724  43.749 54.991  1.00 36.19  ? 223 ILE   A CG1 1 
ATOM   1672 C CG2 . ILE   A 1 234 ? 12.846  44.346 53.757  1.00 35.46  ? 223 ILE   A CG2 1 
ATOM   1673 C CD1 . ILE   A 1 234 ? 10.657  44.830 55.971  1.00 36.69  ? 223 ILE   A CD1 1 
ATOM   1674 N N   . PHE   A 1 235 ? 14.264  40.818 54.602  1.00 37.97  ? 224 PHE   A N   1 
ATOM   1675 C CA  . PHE   A 1 235 ? 15.605  40.292 54.377  1.00 38.99  ? 224 PHE   A CA  1 
ATOM   1676 C C   . PHE   A 1 235 ? 15.593  39.210 53.297  1.00 40.46  ? 224 PHE   A C   1 
ATOM   1677 O O   . PHE   A 1 235 ? 16.437  39.241 52.405  1.00 40.71  ? 224 PHE   A O   1 
ATOM   1678 C CB  . PHE   A 1 235 ? 16.219  39.800 55.697  1.00 38.90  ? 224 PHE   A CB  1 
ATOM   1679 C CG  . PHE   A 1 235 ? 17.681  39.403 55.652  1.00 39.44  ? 224 PHE   A CG  1 
ATOM   1680 C CD1 . PHE   A 1 235 ? 18.552  39.992 54.749  1.00 40.18  ? 224 PHE   A CD1 1 
ATOM   1681 C CD2 . PHE   A 1 235 ? 18.191  38.473 56.546  1.00 39.79  ? 224 PHE   A CD2 1 
ATOM   1682 C CE1 . PHE   A 1 235 ? 19.892  39.614 54.703  1.00 40.74  ? 224 PHE   A CE1 1 
ATOM   1683 C CE2 . PHE   A 1 235 ? 19.531  38.112 56.508  1.00 40.31  ? 224 PHE   A CE2 1 
ATOM   1684 C CZ  . PHE   A 1 235 ? 20.374  38.687 55.591  1.00 40.26  ? 224 PHE   A CZ  1 
ATOM   1685 N N   . ALA   A 1 236 ? 14.598  38.311 53.313  1.00 41.47  ? 225 ALA   A N   1 
ATOM   1686 C CA  . ALA   A 1 236 ? 14.488  37.274 52.274  1.00 42.74  ? 225 ALA   A CA  1 
ATOM   1687 C C   . ALA   A 1 236 ? 14.130  37.890 50.918  1.00 44.53  ? 225 ALA   A C   1 
ATOM   1688 O O   . ALA   A 1 236 ? 14.594  37.411 49.894  1.00 45.25  ? 225 ALA   A O   1 
ATOM   1689 C CB  . ALA   A 1 236 ? 13.461  36.231 52.662  1.00 42.33  ? 225 ALA   A CB  1 
ATOM   1690 N N   . GLU   A 1 237 ? 13.343  38.972 50.911  1.00 45.03  ? 226 GLU   A N   1 
ATOM   1691 C CA  . GLU   A 1 237 ? 12.985  39.670 49.685  1.00 45.97  ? 226 GLU   A CA  1 
ATOM   1692 C C   . GLU   A 1 237 ? 14.168  40.469 49.130  1.00 46.84  ? 226 GLU   A C   1 
ATOM   1693 O O   . GLU   A 1 237 ? 14.245  40.682 47.925  1.00 47.13  ? 226 GLU   A O   1 
ATOM   1694 C CB  . GLU   A 1 237 ? 11.809  40.597 49.938  1.00 48.12  ? 226 GLU   A CB  1 
ATOM   1695 C CG  . GLU   A 1 237 ? 11.018  40.933 48.689  1.00 53.38  ? 226 GLU   A CG  1 
ATOM   1696 C CD  . GLU   A 1 237 ? 9.681   41.587 48.974  1.00 60.42  ? 226 GLU   A CD  1 
ATOM   1697 O OE1 . GLU   A 1 237 ? 9.186   41.461 50.119  1.00 60.75  ? 226 GLU   A OE1 1 
ATOM   1698 O OE2 . GLU   A 1 237 ? 9.121   42.218 48.049  1.00 63.52  ? 226 GLU   A OE2 1 
ATOM   1699 N N   . LEU   A 1 238 ? 15.068  40.941 49.995  1.00 47.09  ? 227 LEU   A N   1 
ATOM   1700 C CA  . LEU   A 1 238 ? 16.258  41.658 49.546  1.00 47.75  ? 227 LEU   A CA  1 
ATOM   1701 C C   . LEU   A 1 238 ? 17.278  40.640 48.981  1.00 48.99  ? 227 LEU   A C   1 
ATOM   1702 O O   . LEU   A 1 238 ? 17.986  40.940 48.009  1.00 49.34  ? 227 LEU   A O   1 
ATOM   1703 C CB  . LEU   A 1 238 ? 16.887  42.483 50.687  1.00 47.22  ? 227 LEU   A CB  1 
ATOM   1704 C CG  . LEU   A 1 238 ? 16.135  43.723 51.172  1.00 47.37  ? 227 LEU   A CG  1 
ATOM   1705 C CD1 . LEU   A 1 238 ? 16.808  44.320 52.403  1.00 47.37  ? 227 LEU   A CD1 1 
ATOM   1706 C CD2 . LEU   A 1 238 ? 16.011  44.760 50.081  1.00 47.31  ? 227 LEU   A CD2 1 
ATOM   1707 N N   . LEU   A 1 239 ? 17.345  39.440 49.580  1.00 49.26  ? 228 LEU   A N   1 
ATOM   1708 C CA  . LEU   A 1 239 ? 18.283  38.426 49.134  1.00 50.40  ? 228 LEU   A CA  1 
ATOM   1709 C C   . LEU   A 1 239 ? 17.860  37.732 47.852  1.00 51.36  ? 228 LEU   A C   1 
ATOM   1710 O O   . LEU   A 1 239 ? 18.728  37.260 47.129  1.00 52.19  ? 228 LEU   A O   1 
ATOM   1711 C CB  . LEU   A 1 239 ? 18.499  37.371 50.223  1.00 50.87  ? 228 LEU   A CB  1 
ATOM   1712 C CG  . LEU   A 1 239 ? 19.244  37.827 51.468  1.00 52.68  ? 228 LEU   A CG  1 
ATOM   1713 C CD1 . LEU   A 1 239 ? 19.259  36.741 52.513  1.00 53.06  ? 228 LEU   A CD1 1 
ATOM   1714 C CD2 . LEU   A 1 239 ? 20.648  38.262 51.138  1.00 53.52  ? 228 LEU   A CD2 1 
ATOM   1715 N N   . THR   A 1 240 ? 16.551  37.628 47.568  1.00 51.20  ? 229 THR   A N   1 
ATOM   1716 C CA  . THR   A 1 240 ? 16.091  36.889 46.382  1.00 51.49  ? 229 THR   A CA  1 
ATOM   1717 C C   . THR   A 1 240 ? 15.346  37.701 45.321  1.00 52.42  ? 229 THR   A C   1 
ATOM   1718 O O   . THR   A 1 240 ? 15.202  37.220 44.198  1.00 52.23  ? 229 THR   A O   1 
ATOM   1719 C CB  . THR   A 1 240 ? 15.191  35.717 46.809  1.00 51.58  ? 229 THR   A CB  1 
ATOM   1720 O OG1 . THR   A 1 240 ? 13.931  36.226 47.247  1.00 51.80  ? 229 THR   A OG1 1 
ATOM   1721 C CG2 . THR   A 1 240 ? 15.813  34.859 47.888  1.00 51.52  ? 229 THR   A CG2 1 
ATOM   1722 N N   . SER   A 1 241 ? 14.795  38.870 45.720  1.00 53.37  ? 230 SER   A N   1 
ATOM   1723 C CA  . SER   A 1 241 ? 13.940  39.802 44.951  1.00 54.62  ? 230 SER   A CA  1 
ATOM   1724 C C   . SER   A 1 241 ? 12.438  39.414 44.984  1.00 56.18  ? 230 SER   A C   1 
ATOM   1725 O O   . SER   A 1 241 ? 11.581  40.210 44.617  1.00 56.11  ? 230 SER   A O   1 
ATOM   1726 C CB  . SER   A 1 241 ? 14.439  40.011 43.525  1.00 55.25  ? 230 SER   A CB  1 
ATOM   1727 O OG  . SER   A 1 241 ? 15.729  40.600 43.530  1.00 56.56  ? 230 SER   A OG  1 
ATOM   1728 N N   . GLU   A 1 242 ? 12.124  38.209 45.466  1.00 57.47  ? 231 GLU   A N   1 
ATOM   1729 C CA  . GLU   A 1 242 ? 10.757  37.702 45.548  1.00 58.96  ? 231 GLU   A CA  1 
ATOM   1730 C C   . GLU   A 1 242 ? 10.224  37.833 46.953  1.00 59.79  ? 231 GLU   A C   1 
ATOM   1731 O O   . GLU   A 1 242 ? 10.952  37.530 47.901  1.00 60.05  ? 231 GLU   A O   1 
ATOM   1732 C CB  . GLU   A 1 242 ? 10.745  36.202 45.199  1.00 61.21  ? 231 GLU   A CB  1 
ATOM   1733 C CG  . GLU   A 1 242 ? 10.254  35.902 43.803  1.00 66.76  ? 231 GLU   A CG  1 
ATOM   1734 C CD  . GLU   A 1 242 ? 11.227  36.315 42.721  1.00 74.56  ? 231 GLU   A CD  1 
ATOM   1735 O OE1 . GLU   A 1 242 ? 12.453  36.243 42.970  1.00 76.17  ? 231 GLU   A OE1 1 
ATOM   1736 O OE2 . GLU   A 1 242 ? 10.762  36.700 41.622  1.00 77.03  ? 231 GLU   A OE2 1 
ATOM   1737 N N   . PRO   A 1 243 ? 8.928   38.169 47.127  1.00 59.98  ? 232 PRO   A N   1 
ATOM   1738 C CA  . PRO   A 1 243 ? 8.359   38.163 48.484  1.00 60.01  ? 232 PRO   A CA  1 
ATOM   1739 C C   . PRO   A 1 243 ? 8.305   36.698 48.938  1.00 60.17  ? 232 PRO   A C   1 
ATOM   1740 O O   . PRO   A 1 243 ? 7.708   35.859 48.249  1.00 60.21  ? 232 PRO   A O   1 
ATOM   1741 C CB  . PRO   A 1 243 ? 6.963   38.785 48.300  1.00 60.42  ? 232 PRO   A CB  1 
ATOM   1742 C CG  . PRO   A 1 243 ? 6.983   39.407 46.939  1.00 60.93  ? 232 PRO   A CG  1 
ATOM   1743 C CD  . PRO   A 1 243 ? 7.914   38.544 46.127  1.00 59.54  ? 232 PRO   A CD  1 
ATOM   1744 N N   . ILE   A 1 244 ? 9.042   36.369 50.012  1.00 59.70  ? 233 ILE   A N   1 
ATOM   1745 C CA  . ILE   A 1 244 ? 9.154   34.994 50.477  1.00 59.58  ? 233 ILE   A CA  1 
ATOM   1746 C C   . ILE   A 1 244 ? 7.787   34.347 50.760  1.00 59.95  ? 233 ILE   A C   1 
ATOM   1747 O O   . ILE   A 1 244 ? 7.569   33.197 50.390  1.00 59.93  ? 233 ILE   A O   1 
ATOM   1748 C CB  . ILE   A 1 244 ? 10.128  34.914 51.667  1.00 59.57  ? 233 ILE   A CB  1 
ATOM   1749 C CG1 . ILE   A 1 244 ? 10.301  33.473 52.157  1.00 60.49  ? 233 ILE   A CG1 1 
ATOM   1750 C CG2 . ILE   A 1 244 ? 9.737   35.867 52.776  1.00 59.74  ? 233 ILE   A CG2 1 
ATOM   1751 C CD1 . ILE   A 1 244 ? 11.484  33.235 52.994  1.00 61.56  ? 233 ILE   A CD1 1 
ATOM   1752 N N   . PHE   A 1 245 ? 6.847   35.112 51.316  1.00 60.04  ? 234 PHE   A N   1 
ATOM   1753 C CA  . PHE   A 1 245 ? 5.525   34.593 51.609  1.00 60.50  ? 234 PHE   A CA  1 
ATOM   1754 C C   . PHE   A 1 245 ? 4.480   35.178 50.662  1.00 61.53  ? 234 PHE   A C   1 
ATOM   1755 O O   . PHE   A 1 245 ? 3.359   35.459 51.073  1.00 61.14  ? 234 PHE   A O   1 
ATOM   1756 C CB  . PHE   A 1 245 ? 5.194   34.774 53.098  1.00 60.09  ? 234 PHE   A CB  1 
ATOM   1757 C CG  . PHE   A 1 245 ? 6.243   34.128 53.977  1.00 60.54  ? 234 PHE   A CG  1 
ATOM   1758 C CD1 . PHE   A 1 245 ? 6.535   32.779 53.859  1.00 61.04  ? 234 PHE   A CD1 1 
ATOM   1759 C CD2 . PHE   A 1 245 ? 6.991   34.883 54.864  1.00 61.19  ? 234 PHE   A CD2 1 
ATOM   1760 C CE1 . PHE   A 1 245 ? 7.521   32.192 54.643  1.00 61.42  ? 234 PHE   A CE1 1 
ATOM   1761 C CE2 . PHE   A 1 245 ? 7.997   34.297 55.623  1.00 61.51  ? 234 PHE   A CE2 1 
ATOM   1762 C CZ  . PHE   A 1 245 ? 8.235   32.953 55.529  1.00 61.17  ? 234 PHE   A CZ  1 
ATOM   1763 N N   . HIS   A 1 246 ? 4.844   35.307 49.375  1.00 62.91  ? 235 HIS   A N   1 
ATOM   1764 C CA  . HIS   A 1 246 ? 3.952   35.814 48.340  1.00 65.14  ? 235 HIS   A CA  1 
ATOM   1765 C C   . HIS   A 1 246 ? 2.772   34.882 48.158  1.00 66.28  ? 235 HIS   A C   1 
ATOM   1766 O O   . HIS   A 1 246 ? 2.908   33.764 47.676  1.00 66.46  ? 235 HIS   A O   1 
ATOM   1767 C CB  . HIS   A 1 246 ? 4.684   36.006 47.005  1.00 67.37  ? 235 HIS   A CB  1 
ATOM   1768 C CG  . HIS   A 1 246 ? 3.770   36.345 45.863  1.00 71.57  ? 235 HIS   A CG  1 
ATOM   1769 N ND1 . HIS   A 1 246 ? 3.348   35.377 44.960  1.00 73.89  ? 235 HIS   A ND1 1 
ATOM   1770 C CD2 . HIS   A 1 246 ? 3.196   37.527 45.536  1.00 73.01  ? 235 HIS   A CD2 1 
ATOM   1771 C CE1 . HIS   A 1 246 ? 2.546   36.004 44.112  1.00 74.45  ? 235 HIS   A CE1 1 
ATOM   1772 N NE2 . HIS   A 1 246 ? 2.420   37.297 44.420  1.00 74.31  ? 235 HIS   A NE2 1 
ATOM   1773 N N   . CYS   A 1 247 ? 1.609   35.388 48.474  1.00 67.07  ? 236 CYS   A N   1 
ATOM   1774 C CA  . CYS   A 1 247 ? 0.364   34.658 48.424  1.00 68.34  ? 236 CYS   A CA  1 
ATOM   1775 C C   . CYS   A 1 247 ? -0.684  35.456 47.611  1.00 69.67  ? 236 CYS   A C   1 
ATOM   1776 O O   . CYS   A 1 247 ? -0.652  36.690 47.588  1.00 69.54  ? 236 CYS   A O   1 
ATOM   1777 C CB  . CYS   A 1 247 ? -0.091  34.407 49.860  1.00 69.05  ? 236 CYS   A CB  1 
ATOM   1778 S SG  . CYS   A 1 247 ? -1.740  33.692 50.024  1.00 72.75  ? 236 CYS   A SG  1 
ATOM   1779 N N   . ARG   A 1 248 ? -1.594  34.752 46.928  1.00 70.80  ? 237 ARG   A N   1 
ATOM   1780 C CA  . ARG   A 1 248 ? -2.639  35.406 46.139  1.00 72.54  ? 237 ARG   A CA  1 
ATOM   1781 C C   . ARG   A 1 248 ? -3.683  36.116 47.020  1.00 73.91  ? 237 ARG   A C   1 
ATOM   1782 O O   . ARG   A 1 248 ? -3.808  35.811 48.209  1.00 74.08  ? 237 ARG   A O   1 
ATOM   1783 C CB  . ARG   A 1 248 ? -3.319  34.398 45.219  1.00 74.43  ? 237 ARG   A CB  1 
ATOM   1784 C CG  . ARG   A 1 248 ? -3.978  33.271 45.977  1.00 78.57  ? 237 ARG   A CG  1 
ATOM   1785 C CD  . ARG   A 1 248 ? -4.927  32.535 45.073  1.00 83.17  ? 237 ARG   A CD  1 
ATOM   1786 N NE  . ARG   A 1 248 ? -6.079  33.358 44.706  1.00 87.83  ? 237 ARG   A NE  1 
ATOM   1787 C CZ  . ARG   A 1 248 ? -7.247  33.342 45.344  1.00 91.98  ? 237 ARG   A CZ  1 
ATOM   1788 N NH1 . ARG   A 1 248 ? -7.434  32.537 46.387  1.00 92.48  ? 237 ARG   A NH1 1 
ATOM   1789 N NH2 . ARG   A 1 248 ? -8.239  34.127 44.943  1.00 92.34  ? 237 ARG   A NH2 1 
ATOM   1790 N N   . GLN   A 1 249 ? -4.429  37.070 46.443  1.00 74.60  ? 238 GLN   A N   1 
ATOM   1791 C CA  . GLN   A 1 249 ? -5.403  37.845 47.210  1.00 75.65  ? 238 GLN   A CA  1 
ATOM   1792 C C   . GLN   A 1 249 ? -6.593  37.021 47.705  1.00 76.22  ? 238 GLN   A C   1 
ATOM   1793 O O   . GLN   A 1 249 ? -7.517  36.745 46.945  1.00 76.63  ? 238 GLN   A O   1 
ATOM   1794 C CB  . GLN   A 1 249 ? -5.864  39.072 46.411  1.00 77.69  ? 238 GLN   A CB  1 
ATOM   1795 C CG  . GLN   A 1 249 ? -4.709  39.917 45.866  1.00 81.52  ? 238 GLN   A CG  1 
ATOM   1796 C CD  . GLN   A 1 249 ? -5.148  40.906 44.810  1.00 86.01  ? 238 GLN   A CD  1 
ATOM   1797 O OE1 . GLN   A 1 249 ? -6.231  40.792 44.219  1.00 87.77  ? 238 GLN   A OE1 1 
ATOM   1798 N NE2 . GLN   A 1 249 ? -4.308  41.898 44.540  1.00 86.24  ? 238 GLN   A NE2 1 
ATOM   1799 N N   . SER   A 1 255 ? -10.652 40.197 56.964  1.00 93.05  ? 244 SER   A N   1 
ATOM   1800 C CA  . SER   A 1 255 ? -11.839 40.256 57.819  1.00 93.60  ? 244 SER   A CA  1 
ATOM   1801 C C   . SER   A 1 255 ? -11.713 39.209 58.946  1.00 93.63  ? 244 SER   A C   1 
ATOM   1802 O O   . SER   A 1 255 ? -11.689 39.560 60.133  1.00 94.08  ? 244 SER   A O   1 
ATOM   1803 C CB  . SER   A 1 255 ? -13.104 40.037 56.989  1.00 94.98  ? 244 SER   A CB  1 
ATOM   1804 O OG  . SER   A 1 255 ? -13.055 38.790 56.312  1.00 97.27  ? 244 SER   A OG  1 
ATOM   1805 N N   . ASN   A 1 256 ? -11.586 37.928 58.559  1.00 92.78  ? 245 ASN   A N   1 
ATOM   1806 C CA  . ASN   A 1 256 ? -11.381 36.796 59.456  1.00 92.14  ? 245 ASN   A CA  1 
ATOM   1807 C C   . ASN   A 1 256 ? -9.904  36.873 59.878  1.00 90.70  ? 245 ASN   A C   1 
ATOM   1808 O O   . ASN   A 1 256 ? -9.038  37.033 59.015  1.00 90.89  ? 245 ASN   A O   1 
ATOM   1809 C CB  . ASN   A 1 256 ? -11.675 35.499 58.666  1.00 93.62  ? 245 ASN   A CB  1 
ATOM   1810 C CG  . ASN   A 1 256 ? -11.337 34.177 59.322  1.00 97.03  ? 245 ASN   A CG  1 
ATOM   1811 O OD1 . ASN   A 1 256 ? -11.292 34.039 60.553  1.00 98.25  ? 245 ASN   A OD1 1 
ATOM   1812 N ND2 . ASN   A 1 256 ? -11.093 33.164 58.493  1.00 97.57  ? 245 ASN   A ND2 1 
ATOM   1813 N N   . PRO   A 1 257 ? -9.581  36.828 61.187  1.00 88.95  ? 246 PRO   A N   1 
ATOM   1814 C CA  . PRO   A 1 257 ? -8.157  36.913 61.593  1.00 87.43  ? 246 PRO   A CA  1 
ATOM   1815 C C   . PRO   A 1 257 ? -7.281  35.718 61.179  1.00 85.18  ? 246 PRO   A C   1 
ATOM   1816 O O   . PRO   A 1 257 ? -6.070  35.756 61.354  1.00 85.29  ? 246 PRO   A O   1 
ATOM   1817 C CB  . PRO   A 1 257 ? -8.232  37.066 63.113  1.00 88.50  ? 246 PRO   A CB  1 
ATOM   1818 C CG  . PRO   A 1 257 ? -9.527  36.413 63.485  1.00 89.41  ? 246 PRO   A CG  1 
ATOM   1819 C CD  . PRO   A 1 257 ? -10.477 36.680 62.349  1.00 88.15  ? 246 PRO   A CD  1 
ATOM   1820 N N   . TYR   A 1 258 ? -7.895  34.671 60.612  1.00 83.04  ? 247 TYR   A N   1 
ATOM   1821 C CA  . TYR   A 1 258 ? -7.249  33.453 60.136  1.00 81.38  ? 247 TYR   A CA  1 
ATOM   1822 C C   . TYR   A 1 258 ? -7.234  33.437 58.593  1.00 79.43  ? 247 TYR   A C   1 
ATOM   1823 O O   . TYR   A 1 258 ? -8.282  33.560 57.954  1.00 79.35  ? 247 TYR   A O   1 
ATOM   1824 C CB  . TYR   A 1 258 ? -8.010  32.240 60.705  1.00 81.33  ? 247 TYR   A CB  1 
ATOM   1825 C CG  . TYR   A 1 258 ? -7.579  30.892 60.175  1.00 81.88  ? 247 TYR   A CG  1 
ATOM   1826 C CD1 . TYR   A 1 258 ? -8.240  30.299 59.109  1.00 82.63  ? 247 TYR   A CD1 1 
ATOM   1827 C CD2 . TYR   A 1 258 ? -6.576  30.167 60.800  1.00 82.81  ? 247 TYR   A CD2 1 
ATOM   1828 C CE1 . TYR   A 1 258 ? -7.863  29.052 58.629  1.00 83.50  ? 247 TYR   A CE1 1 
ATOM   1829 C CE2 . TYR   A 1 258 ? -6.203  28.909 60.342  1.00 83.73  ? 247 TYR   A CE2 1 
ATOM   1830 C CZ  . TYR   A 1 258 ? -6.845  28.357 59.249  1.00 84.42  ? 247 TYR   A CZ  1 
ATOM   1831 O OH  . TYR   A 1 258 ? -6.491  27.114 58.783  1.00 85.58  ? 247 TYR   A OH  1 
ATOM   1832 N N   . HIS   A 1 259 ? -6.044  33.287 57.996  1.00 77.59  ? 248 HIS   A N   1 
ATOM   1833 C CA  . HIS   A 1 259 ? -5.903  33.276 56.540  1.00 76.22  ? 248 HIS   A CA  1 
ATOM   1834 C C   . HIS   A 1 259 ? -5.241  32.001 56.063  1.00 73.71  ? 248 HIS   A C   1 
ATOM   1835 O O   . HIS   A 1 259 ? -4.057  31.798 56.321  1.00 73.86  ? 248 HIS   A O   1 
ATOM   1836 C CB  . HIS   A 1 259 ? -5.125  34.507 56.091  1.00 77.87  ? 248 HIS   A CB  1 
ATOM   1837 C CG  . HIS   A 1 259 ? -5.794  35.764 56.533  1.00 81.80  ? 248 HIS   A CG  1 
ATOM   1838 N ND1 . HIS   A 1 259 ? -6.972  36.192 55.944  1.00 84.14  ? 248 HIS   A ND1 1 
ATOM   1839 C CD2 . HIS   A 1 259 ? -5.491  36.589 57.563  1.00 83.37  ? 248 HIS   A CD2 1 
ATOM   1840 C CE1 . HIS   A 1 259 ? -7.323  37.287 56.599  1.00 84.86  ? 248 HIS   A CE1 1 
ATOM   1841 N NE2 . HIS   A 1 259 ? -6.458  37.571 57.580  1.00 84.73  ? 248 HIS   A NE2 1 
ATOM   1842 N N   . HIS   A 1 260 ? -6.012  31.126 55.388  1.00 71.37  ? 249 HIS   A N   1 
ATOM   1843 C CA  . HIS   A 1 260 ? -5.549  29.816 54.928  1.00 69.21  ? 249 HIS   A CA  1 
ATOM   1844 C C   . HIS   A 1 260 ? -4.466  29.869 53.856  1.00 66.91  ? 249 HIS   A C   1 
ATOM   1845 O O   . HIS   A 1 260 ? -3.412  29.267 54.033  1.00 66.51  ? 249 HIS   A O   1 
ATOM   1846 C CB  . HIS   A 1 260 ? -6.730  28.938 54.459  1.00 69.72  ? 249 HIS   A CB  1 
ATOM   1847 C CG  . HIS   A 1 260 ? -6.325  27.547 54.066  1.00 72.06  ? 249 HIS   A CG  1 
ATOM   1848 N ND1 . HIS   A 1 260 ? -5.729  27.279 52.838  1.00 73.97  ? 249 HIS   A ND1 1 
ATOM   1849 C CD2 . HIS   A 1 260 ? -6.451  26.386 54.749  1.00 73.31  ? 249 HIS   A CD2 1 
ATOM   1850 C CE1 . HIS   A 1 260 ? -5.493  25.976 52.826  1.00 74.48  ? 249 HIS   A CE1 1 
ATOM   1851 N NE2 . HIS   A 1 260 ? -5.901  25.396 53.957  1.00 74.51  ? 249 HIS   A NE2 1 
ATOM   1852 N N   . ASP   A 1 261 ? -4.731  30.551 52.737  1.00 65.28  ? 250 ASP   A N   1 
ATOM   1853 C CA  . ASP   A 1 261 ? -3.791  30.609 51.624  1.00 64.21  ? 250 ASP   A CA  1 
ATOM   1854 C C   . ASP   A 1 261 ? -2.440  31.188 52.035  1.00 62.30  ? 250 ASP   A C   1 
ATOM   1855 O O   . ASP   A 1 261 ? -1.413  30.744 51.525  1.00 62.48  ? 250 ASP   A O   1 
ATOM   1856 C CB  . ASP   A 1 261 ? -4.408  31.344 50.423  1.00 66.41  ? 250 ASP   A CB  1 
ATOM   1857 C CG  . ASP   A 1 261 ? -5.687  30.708 49.898  1.00 72.40  ? 250 ASP   A CG  1 
ATOM   1858 O OD1 . ASP   A 1 261 ? -5.813  29.461 49.987  1.00 73.20  ? 250 ASP   A OD1 1 
ATOM   1859 O OD2 . ASP   A 1 261 ? -6.563  31.457 49.387  1.00 75.00  ? 250 ASP   A OD2 1 
ATOM   1860 N N   . GLN   A 1 262 ? -2.430  32.126 53.001  1.00 60.31  ? 251 GLN   A N   1 
ATOM   1861 C CA  . GLN   A 1 262 ? -1.183  32.704 53.498  1.00 58.58  ? 251 GLN   A CA  1 
ATOM   1862 C C   . GLN   A 1 262 ? -0.432  31.728 54.401  1.00 57.08  ? 251 GLN   A C   1 
ATOM   1863 O O   . GLN   A 1 262 ? 0.778   31.538 54.226  1.00 57.08  ? 251 GLN   A O   1 
ATOM   1864 C CB  . GLN   A 1 262 ? -1.418  34.037 54.211  1.00 58.82  ? 251 GLN   A CB  1 
ATOM   1865 C CG  . GLN   A 1 262 ? -0.118  34.706 54.641  1.00 60.02  ? 251 GLN   A CG  1 
ATOM   1866 C CD  . GLN   A 1 262 ? 0.774   35.049 53.471  1.00 61.87  ? 251 GLN   A CD  1 
ATOM   1867 O OE1 . GLN   A 1 262 ? 0.523   35.984 52.712  1.00 63.03  ? 251 GLN   A OE1 1 
ATOM   1868 N NE2 . GLN   A 1 262 ? 1.842   34.305 53.304  1.00 61.67  ? 251 GLN   A NE2 1 
ATOM   1869 N N   . LEU   A 1 263 ? -1.151  31.072 55.339  1.00 55.39  ? 252 LEU   A N   1 
ATOM   1870 C CA  . LEU   A 1 263 ? -0.556  30.075 56.234  1.00 53.95  ? 252 LEU   A CA  1 
ATOM   1871 C C   . LEU   A 1 263 ? 0.017   28.925 55.423  1.00 53.22  ? 252 LEU   A C   1 
ATOM   1872 O O   . LEU   A 1 263 ? 1.137   28.515 55.681  1.00 53.22  ? 252 LEU   A O   1 
ATOM   1873 C CB  . LEU   A 1 263 ? -1.564  29.562 57.260  1.00 53.25  ? 252 LEU   A CB  1 
ATOM   1874 C CG  . LEU   A 1 263 ? -1.647  30.365 58.538  1.00 53.82  ? 252 LEU   A CG  1 
ATOM   1875 C CD1 . LEU   A 1 263 ? -2.834  29.935 59.374  1.00 54.16  ? 252 LEU   A CD1 1 
ATOM   1876 C CD2 . LEU   A 1 263 ? -0.355  30.283 59.321  1.00 53.96  ? 252 LEU   A CD2 1 
ATOM   1877 N N   . ASP   A 1 264 ? -0.693  28.494 54.370  1.00 52.50  ? 253 ASP   A N   1 
ATOM   1878 C CA  . ASP   A 1 264 ? -0.224  27.455 53.464  1.00 52.37  ? 253 ASP   A CA  1 
ATOM   1879 C C   . ASP   A 1 264 ? 1.101   27.881 52.801  1.00 52.42  ? 253 ASP   A C   1 
ATOM   1880 O O   . ASP   A 1 264 ? 2.008   27.063 52.708  1.00 52.79  ? 253 ASP   A O   1 
ATOM   1881 C CB  . ASP   A 1 264 ? -1.310  27.142 52.414  1.00 53.71  ? 253 ASP   A CB  1 
ATOM   1882 C CG  . ASP   A 1 264 ? -0.813  26.375 51.207  1.00 57.73  ? 253 ASP   A CG  1 
ATOM   1883 O OD1 . ASP   A 1 264 ? -0.392  25.220 51.377  1.00 58.28  ? 253 ASP   A OD1 1 
ATOM   1884 O OD2 . ASP   A 1 264 ? -0.807  26.950 50.100  1.00 60.04  ? 253 ASP   A OD2 1 
ATOM   1885 N N   . ARG   A 1 265 ? 1.212   29.153 52.358  1.00 51.97  ? 254 ARG   A N   1 
ATOM   1886 C CA  . ARG   A 1 265 ? 2.416   29.701 51.728  1.00 51.84  ? 254 ARG   A CA  1 
ATOM   1887 C C   . ARG   A 1 265 ? 3.586   29.729 52.712  1.00 51.39  ? 254 ARG   A C   1 
ATOM   1888 O O   . ARG   A 1 265 ? 4.724   29.453 52.318  1.00 51.83  ? 254 ARG   A O   1 
ATOM   1889 C CB  . ARG   A 1 265 ? 2.150   31.102 51.159  1.00 53.46  ? 254 ARG   A CB  1 
ATOM   1890 C CG  . ARG   A 1 265 ? 3.396   31.776 50.581  1.00 57.59  ? 254 ARG   A CG  1 
ATOM   1891 C CD  . ARG   A 1 265 ? 3.998   31.025 49.398  1.00 61.45  ? 254 ARG   A CD  1 
ATOM   1892 N NE  . ARG   A 1 265 ? 5.404   31.376 49.171  1.00 64.59  ? 254 ARG   A NE  1 
ATOM   1893 C CZ  . ARG   A 1 265 ? 6.089   31.061 48.073  1.00 67.57  ? 254 ARG   A CZ  1 
ATOM   1894 N NH1 . ARG   A 1 265 ? 5.502   30.397 47.083  1.00 67.55  ? 254 ARG   A NH1 1 
ATOM   1895 N NH2 . ARG   A 1 265 ? 7.361   31.417 47.952  1.00 67.96  ? 254 ARG   A NH2 1 
ATOM   1896 N N   . ILE   A 1 266 ? 3.309   30.040 53.997  1.00 50.16  ? 255 ILE   A N   1 
ATOM   1897 C CA  . ILE   A 1 266 ? 4.331   30.027 55.044  1.00 48.95  ? 255 ILE   A CA  1 
ATOM   1898 C C   . ILE   A 1 266 ? 4.891   28.611 55.200  1.00 48.16  ? 255 ILE   A C   1 
ATOM   1899 O O   . ILE   A 1 266 ? 6.100   28.441 55.217  1.00 48.03  ? 255 ILE   A O   1 
ATOM   1900 C CB  . ILE   A 1 266 ? 3.786   30.599 56.379  1.00 48.78  ? 255 ILE   A CB  1 
ATOM   1901 C CG1 . ILE   A 1 266 ? 3.573   32.120 56.250  1.00 49.34  ? 255 ILE   A CG1 1 
ATOM   1902 C CG2 . ILE   A 1 266 ? 4.707   30.231 57.565  1.00 49.07  ? 255 ILE   A CG2 1 
ATOM   1903 C CD1 . ILE   A 1 266 ? 3.320   32.908 57.530  1.00 50.46  ? 255 ILE   A CD1 1 
ATOM   1904 N N   . PHE   A 1 267 ? 4.013   27.599 55.252  1.00 47.59  ? 256 PHE   A N   1 
ATOM   1905 C CA  . PHE   A 1 267 ? 4.428   26.206 55.407  1.00 47.45  ? 256 PHE   A CA  1 
ATOM   1906 C C   . PHE   A 1 267 ? 5.122   25.651 54.158  1.00 48.33  ? 256 PHE   A C   1 
ATOM   1907 O O   . PHE   A 1 267 ? 5.945   24.742 54.280  1.00 48.55  ? 256 PHE   A O   1 
ATOM   1908 C CB  . PHE   A 1 267 ? 3.260   25.310 55.826  1.00 46.60  ? 256 PHE   A CB  1 
ATOM   1909 C CG  . PHE   A 1 267 ? 2.509   25.746 57.058  1.00 46.32  ? 256 PHE   A CG  1 
ATOM   1910 C CD1 . PHE   A 1 267 ? 3.184   26.167 58.187  1.00 46.54  ? 256 PHE   A CD1 1 
ATOM   1911 C CD2 . PHE   A 1 267 ? 1.129   25.692 57.100  1.00 46.64  ? 256 PHE   A CD2 1 
ATOM   1912 C CE1 . PHE   A 1 267 ? 2.489   26.576 59.313  1.00 46.93  ? 256 PHE   A CE1 1 
ATOM   1913 C CE2 . PHE   A 1 267 ? 0.440   26.112 58.222  1.00 47.07  ? 256 PHE   A CE2 1 
ATOM   1914 C CZ  . PHE   A 1 267 ? 1.125   26.534 59.327  1.00 46.80  ? 256 PHE   A CZ  1 
ATOM   1915 N N   . ASN   A 1 268 ? 4.812   26.187 52.967  1.00 48.39  ? 257 ASN   A N   1 
ATOM   1916 C CA  . ASN   A 1 268 ? 5.499   25.763 51.742  1.00 49.03  ? 257 ASN   A CA  1 
ATOM   1917 C C   . ASN   A 1 268 ? 6.986   26.175 51.776  1.00 49.18  ? 257 ASN   A C   1 
ATOM   1918 O O   . ASN   A 1 268 ? 7.847   25.501 51.205  1.00 49.16  ? 257 ASN   A O   1 
ATOM   1919 C CB  . ASN   A 1 268 ? 4.832   26.367 50.522  1.00 50.85  ? 257 ASN   A CB  1 
ATOM   1920 C CG  . ASN   A 1 268 ? 3.808   25.456 49.925  1.00 55.78  ? 257 ASN   A CG  1 
ATOM   1921 O OD1 . ASN   A 1 268 ? 4.040   24.257 49.784  1.00 57.70  ? 257 ASN   A OD1 1 
ATOM   1922 N ND2 . ASN   A 1 268 ? 2.648   25.998 49.567  1.00 57.00  ? 257 ASN   A ND2 1 
ATOM   1923 N N   . VAL   A 1 269 ? 7.280   27.286 52.451  1.00 49.05  ? 258 VAL   A N   1 
ATOM   1924 C CA  . VAL   A 1 269 ? 8.633   27.777 52.573  1.00 49.13  ? 258 VAL   A CA  1 
ATOM   1925 C C   . VAL   A 1 269 ? 9.315   27.207 53.829  1.00 49.83  ? 258 VAL   A C   1 
ATOM   1926 O O   . VAL   A 1 269 ? 10.370  26.590 53.717  1.00 49.84  ? 258 VAL   A O   1 
ATOM   1927 C CB  . VAL   A 1 269 ? 8.648   29.319 52.539  1.00 48.72  ? 258 VAL   A CB  1 
ATOM   1928 C CG1 . VAL   A 1 269 ? 10.069  29.843 52.648  1.00 48.87  ? 258 VAL   A CG1 1 
ATOM   1929 C CG2 . VAL   A 1 269 ? 7.961   29.837 51.281  1.00 48.76  ? 258 VAL   A CG2 1 
ATOM   1930 N N   . MET   A 1 270 ? 8.694   27.377 55.012  1.00 49.95  ? 259 MET   A N   1 
ATOM   1931 C CA  . MET   A 1 270 ? 9.263   26.959 56.290  1.00 50.46  ? 259 MET   A CA  1 
ATOM   1932 C C   . MET   A 1 270 ? 9.143   25.497 56.600  1.00 51.61  ? 259 MET   A C   1 
ATOM   1933 O O   . MET   A 1 270 ? 10.071  24.907 57.150  1.00 51.75  ? 259 MET   A O   1 
ATOM   1934 C CB  . MET   A 1 270 ? 8.644   27.760 57.460  1.00 50.17  ? 259 MET   A CB  1 
ATOM   1935 C CG  . MET   A 1 270 ? 8.644   29.273 57.272  1.00 50.54  ? 259 MET   A CG  1 
ATOM   1936 S SD  . MET   A 1 270 ? 10.242  29.971 56.790  1.00 47.56  ? 259 MET   A SD  1 
ATOM   1937 C CE  . MET   A 1 270 ? 11.235  29.465 58.145  1.00 44.25  ? 259 MET   A CE  1 
ATOM   1938 N N   . GLY   A 1 271 ? 7.988   24.944 56.272  1.00 52.30  ? 260 GLY   A N   1 
ATOM   1939 C CA  . GLY   A 1 271 ? 7.573   23.593 56.627  1.00 53.44  ? 260 GLY   A CA  1 
ATOM   1940 C C   . GLY   A 1 271 ? 6.552   23.648 57.758  1.00 54.27  ? 260 GLY   A C   1 
ATOM   1941 O O   . GLY   A 1 271 ? 6.273   24.734 58.293  1.00 54.72  ? 260 GLY   A O   1 
ATOM   1942 N N   . PHE   A 1 272 ? 5.976   22.493 58.143  1.00 54.25  ? 261 PHE   A N   1 
ATOM   1943 C CA  . PHE   A 1 272 ? 5.012   22.497 59.243  1.00 54.96  ? 261 PHE   A CA  1 
ATOM   1944 C C   . PHE   A 1 272 ? 5.751   22.492 60.579  1.00 56.24  ? 261 PHE   A C   1 
ATOM   1945 O O   . PHE   A 1 272 ? 6.621   21.647 60.827  1.00 56.13  ? 261 PHE   A O   1 
ATOM   1946 C CB  . PHE   A 1 272 ? 4.013   21.352 59.143  1.00 54.66  ? 261 PHE   A CB  1 
ATOM   1947 C CG  . PHE   A 1 272 ? 2.687   21.674 59.782  1.00 54.84  ? 261 PHE   A CG  1 
ATOM   1948 C CD1 . PHE   A 1 272 ? 2.493   21.496 61.138  1.00 55.34  ? 261 PHE   A CD1 1 
ATOM   1949 C CD2 . PHE   A 1 272 ? 1.626   22.130 59.018  1.00 55.70  ? 261 PHE   A CD2 1 
ATOM   1950 C CE1 . PHE   A 1 272 ? 1.270   21.792 61.723  1.00 56.22  ? 261 PHE   A CE1 1 
ATOM   1951 C CE2 . PHE   A 1 272 ? 0.398   22.412 59.603  1.00 56.32  ? 261 PHE   A CE2 1 
ATOM   1952 C CZ  . PHE   A 1 272 ? 0.227   22.238 60.950  1.00 56.09  ? 261 PHE   A CZ  1 
ATOM   1953 N N   . PRO   A 1 273 ? 5.433   23.463 61.447  1.00 57.14  ? 262 PRO   A N   1 
ATOM   1954 C CA  . PRO   A 1 273 ? 6.130   23.544 62.730  1.00 58.07  ? 262 PRO   A CA  1 
ATOM   1955 C C   . PRO   A 1 273 ? 5.877   22.348 63.623  1.00 59.38  ? 262 PRO   A C   1 
ATOM   1956 O O   . PRO   A 1 273 ? 4.730   22.037 63.951  1.00 60.13  ? 262 PRO   A O   1 
ATOM   1957 C CB  . PRO   A 1 273 ? 5.575   24.827 63.353  1.00 58.62  ? 262 PRO   A CB  1 
ATOM   1958 C CG  . PRO   A 1 273 ? 4.254   25.031 62.695  1.00 58.74  ? 262 PRO   A CG  1 
ATOM   1959 C CD  . PRO   A 1 273 ? 4.441   24.541 61.301  1.00 56.89  ? 262 PRO   A CD  1 
ATOM   1960 N N   . ALA   A 1 274 ? 6.950   21.672 64.019  1.00 59.57  ? 263 ALA   A N   1 
ATOM   1961 C CA  . ALA   A 1 274 ? 6.851   20.541 64.929  1.00 60.28  ? 263 ALA   A CA  1 
ATOM   1962 C C   . ALA   A 1 274 ? 6.329   21.007 66.297  1.00 61.12  ? 263 ALA   A C   1 
ATOM   1963 O O   . ALA   A 1 274 ? 6.402   22.194 66.619  1.00 61.26  ? 263 ALA   A O   1 
ATOM   1964 C CB  . ALA   A 1 274 ? 8.218   19.891 65.081  1.00 60.38  ? 263 ALA   A CB  1 
ATOM   1965 N N   . ASP   A 1 275 ? 5.813   20.081 67.115  1.00 61.62  ? 264 ASP   A N   1 
ATOM   1966 C CA  . ASP   A 1 275 ? 5.308   20.391 68.464  1.00 62.04  ? 264 ASP   A CA  1 
ATOM   1967 C C   . ASP   A 1 275 ? 6.426   21.037 69.307  1.00 60.69  ? 264 ASP   A C   1 
ATOM   1968 O O   . ASP   A 1 275 ? 6.199   22.033 69.981  1.00 60.76  ? 264 ASP   A O   1 
ATOM   1969 C CB  . ASP   A 1 275 ? 4.798   19.108 69.165  1.00 65.18  ? 264 ASP   A CB  1 
ATOM   1970 C CG  . ASP   A 1 275 ? 4.085   18.111 68.261  1.00 72.50  ? 264 ASP   A CG  1 
ATOM   1971 O OD1 . ASP   A 1 275 ? 4.756   17.521 67.373  1.00 73.40  ? 264 ASP   A OD1 1 
ATOM   1972 O OD2 . ASP   A 1 275 ? 2.864   17.905 68.450  1.00 76.26  ? 264 ASP   A OD2 1 
ATOM   1973 N N   . LYS   A 1 276 ? 7.644   20.493 69.194  1.00 59.32  ? 265 LYS   A N   1 
ATOM   1974 C CA  . LYS   A 1 276 ? 8.842   20.955 69.889  1.00 58.56  ? 265 LYS   A CA  1 
ATOM   1975 C C   . LYS   A 1 276 ? 9.349   22.302 69.391  1.00 57.12  ? 265 LYS   A C   1 
ATOM   1976 O O   . LYS   A 1 276 ? 10.073  22.967 70.120  1.00 57.39  ? 265 LYS   A O   1 
ATOM   1977 C CB  . LYS   A 1 276 ? 9.964   19.917 69.742  1.00 60.81  ? 265 LYS   A CB  1 
ATOM   1978 C CG  . LYS   A 1 276 ? 10.183  19.502 68.290  1.00 65.18  ? 265 LYS   A CG  1 
ATOM   1979 C CD  . LYS   A 1 276 ? 11.517  18.844 68.027  1.00 69.21  ? 265 LYS   A CD  1 
ATOM   1980 C CE  . LYS   A 1 276 ? 11.561  18.362 66.600  1.00 72.70  ? 265 LYS   A CE  1 
ATOM   1981 N NZ  . LYS   A 1 276 ? 10.455  17.403 66.319  1.00 74.48  ? 265 LYS   A NZ  1 
ATOM   1982 N N   . ASP   A 1 277 ? 9.010   22.689 68.154  1.00 55.68  ? 266 ASP   A N   1 
ATOM   1983 C CA  . ASP   A 1 277 ? 9.435   23.946 67.515  1.00 54.71  ? 266 ASP   A CA  1 
ATOM   1984 C C   . ASP   A 1 277 ? 8.607   25.173 67.922  1.00 53.38  ? 266 ASP   A C   1 
ATOM   1985 O O   . ASP   A 1 277 ? 9.047   26.307 67.736  1.00 53.22  ? 266 ASP   A O   1 
ATOM   1986 C CB  . ASP   A 1 277 ? 9.408   23.798 65.980  1.00 56.13  ? 266 ASP   A CB  1 
ATOM   1987 C CG  . ASP   A 1 277 ? 10.458  22.852 65.428  1.00 59.98  ? 266 ASP   A CG  1 
ATOM   1988 O OD1 . ASP   A 1 277 ? 11.512  22.670 66.098  1.00 60.49  ? 266 ASP   A OD1 1 
ATOM   1989 O OD2 . ASP   A 1 277 ? 10.240  22.309 64.319  1.00 61.51  ? 266 ASP   A OD2 1 
ATOM   1990 N N   . TRP   A 1 278 ? 7.396   24.939 68.427  1.00 52.45  ? 267 TRP   A N   1 
ATOM   1991 C CA  . TRP   A 1 278 ? 6.455   25.967 68.844  1.00 51.87  ? 267 TRP   A CA  1 
ATOM   1992 C C   . TRP   A 1 278 ? 5.455   25.255 69.738  1.00 52.48  ? 267 TRP   A C   1 
ATOM   1993 O O   . TRP   A 1 278 ? 4.432   24.794 69.253  1.00 52.37  ? 267 TRP   A O   1 
ATOM   1994 C CB  . TRP   A 1 278 ? 5.753   26.551 67.600  1.00 50.83  ? 267 TRP   A CB  1 
ATOM   1995 C CG  . TRP   A 1 278 ? 4.909   27.774 67.815  1.00 50.11  ? 267 TRP   A CG  1 
ATOM   1996 C CD1 . TRP   A 1 278 ? 4.594   28.373 69.000  1.00 50.71  ? 267 TRP   A CD1 1 
ATOM   1997 C CD2 . TRP   A 1 278 ? 4.249   28.529 66.796  1.00 49.93  ? 267 TRP   A CD2 1 
ATOM   1998 N NE1 . TRP   A 1 278 ? 3.796   29.469 68.778  1.00 50.85  ? 267 TRP   A NE1 1 
ATOM   1999 C CE2 . TRP   A 1 278 ? 3.553   29.576 67.433  1.00 50.67  ? 267 TRP   A CE2 1 
ATOM   2000 C CE3 . TRP   A 1 278 ? 4.176   28.422 65.402  1.00 50.40  ? 267 TRP   A CE3 1 
ATOM   2001 C CZ2 . TRP   A 1 278 ? 2.782   30.496 66.722  1.00 51.32  ? 267 TRP   A CZ2 1 
ATOM   2002 C CZ3 . TRP   A 1 278 ? 3.413   29.335 64.701  1.00 51.11  ? 267 TRP   A CZ3 1 
ATOM   2003 C CH2 . TRP   A 1 278 ? 2.730   30.358 65.357  1.00 51.31  ? 267 TRP   A CH2 1 
ATOM   2004 N N   . GLU   A 1 279 ? 5.792   25.078 71.023  1.00 53.11  ? 268 GLU   A N   1 
ATOM   2005 C CA  . GLU   A 1 279 ? 4.934   24.374 71.978  1.00 54.09  ? 268 GLU   A CA  1 
ATOM   2006 C C   . GLU   A 1 279 ? 3.610   25.112 72.232  1.00 54.47  ? 268 GLU   A C   1 
ATOM   2007 O O   . GLU   A 1 279 ? 2.557   24.469 72.312  1.00 54.91  ? 268 GLU   A O   1 
ATOM   2008 C CB  . GLU   A 1 279 ? 5.680   24.089 73.292  1.00 56.96  ? 268 GLU   A CB  1 
ATOM   2009 C CG  . GLU   A 1 279 ? 6.875   23.168 73.113  1.00 64.26  ? 268 GLU   A CG  1 
ATOM   2010 C CD  . GLU   A 1 279 ? 7.494   22.623 74.388  1.00 74.06  ? 268 GLU   A CD  1 
ATOM   2011 O OE1 . GLU   A 1 279 ? 6.854   22.738 75.460  1.00 76.72  ? 268 GLU   A OE1 1 
ATOM   2012 O OE2 . GLU   A 1 279 ? 8.617   22.072 74.314  1.00 76.26  ? 268 GLU   A OE2 1 
ATOM   2013 N N   . ASP   A 1 280 ? 3.643   26.456 72.292  1.00 53.89  ? 269 ASP   A N   1 
ATOM   2014 C CA  . ASP   A 1 280 ? 2.419   27.226 72.516  1.00 53.81  ? 269 ASP   A CA  1 
ATOM   2015 C C   . ASP   A 1 280 ? 1.561   27.423 71.282  1.00 52.93  ? 269 ASP   A C   1 
ATOM   2016 O O   . ASP   A 1 280 ? 0.651   28.249 71.322  1.00 52.72  ? 269 ASP   A O   1 
ATOM   2017 C CB  . ASP   A 1 280 ? 2.704   28.581 73.174  1.00 56.03  ? 269 ASP   A CB  1 
ATOM   2018 C CG  . ASP   A 1 280 ? 3.430   28.487 74.497  1.00 60.79  ? 269 ASP   A CG  1 
ATOM   2019 O OD1 . ASP   A 1 280 ? 3.459   27.373 75.085  1.00 61.15  ? 269 ASP   A OD1 1 
ATOM   2020 O OD2 . ASP   A 1 280 ? 3.979   29.525 74.947  1.00 62.99  ? 269 ASP   A OD2 1 
ATOM   2021 N N   . ILE   A 1 281 ? 1.804   26.662 70.196  1.00 52.30  ? 270 ILE   A N   1 
ATOM   2022 C CA  . ILE   A 1 281 ? 0.926   26.743 69.023  1.00 52.21  ? 270 ILE   A CA  1 
ATOM   2023 C C   . ILE   A 1 281 ? -0.472  26.221 69.416  1.00 52.81  ? 270 ILE   A C   1 
ATOM   2024 O O   . ILE   A 1 281 ? -1.465  26.784 68.977  1.00 52.79  ? 270 ILE   A O   1 
ATOM   2025 C CB  . ILE   A 1 281 ? 1.513   26.067 67.751  1.00 51.98  ? 270 ILE   A CB  1 
ATOM   2026 C CG1 . ILE   A 1 281 ? 0.783   26.545 66.485  1.00 52.38  ? 270 ILE   A CG1 1 
ATOM   2027 C CG2 . ILE   A 1 281 ? 1.502   24.554 67.861  1.00 52.31  ? 270 ILE   A CG2 1 
ATOM   2028 C CD1 . ILE   A 1 281 ? 1.413   26.119 65.215  1.00 53.25  ? 270 ILE   A CD1 1 
ATOM   2029 N N   . LYS   A 1 282 ? -0.533  25.217 70.334  1.00 53.16  ? 271 LYS   A N   1 
ATOM   2030 C CA  . LYS   A 1 282 ? -1.748  24.648 70.902  1.00 53.95  ? 271 LYS   A CA  1 
ATOM   2031 C C   . LYS   A 1 282 ? -2.587  25.731 71.570  1.00 54.63  ? 271 LYS   A C   1 
ATOM   2032 O O   . LYS   A 1 282 ? -3.813  25.674 71.512  1.00 55.24  ? 271 LYS   A O   1 
ATOM   2033 C CB  . LYS   A 1 282 ? -1.385  23.592 71.954  1.00 56.19  ? 271 LYS   A CB  1 
ATOM   2034 C CG  . LYS   A 1 282 ? -0.536  22.459 71.410  1.00 61.25  ? 271 LYS   A CG  1 
ATOM   2035 C CD  . LYS   A 1 282 ? -0.474  21.294 72.383  1.00 66.64  ? 271 LYS   A CD  1 
ATOM   2036 C CE  . LYS   A 1 282 ? -1.828  20.642 72.601  1.00 71.08  ? 271 LYS   A CE  1 
ATOM   2037 N NZ  . LYS   A 1 282 ? -1.772  19.516 73.587  1.00 73.25  ? 271 LYS   A NZ  1 
ATOM   2038 N N   . LYS   A 1 283 ? -1.929  26.713 72.210  1.00 54.46  ? 272 LYS   A N   1 
ATOM   2039 C CA  . LYS   A 1 283 ? -2.564  27.816 72.920  1.00 54.72  ? 272 LYS   A CA  1 
ATOM   2040 C C   . LYS   A 1 283 ? -3.159  28.892 72.005  1.00 54.33  ? 272 LYS   A C   1 
ATOM   2041 O O   . LYS   A 1 283 ? -3.872  29.750 72.502  1.00 54.32  ? 272 LYS   A O   1 
ATOM   2042 C CB  . LYS   A 1 283 ? -1.584  28.446 73.940  1.00 57.21  ? 272 LYS   A CB  1 
ATOM   2043 C CG  . LYS   A 1 283 ? -1.177  27.513 75.090  1.00 61.87  ? 272 LYS   A CG  1 
ATOM   2044 C CD  . LYS   A 1 283 ? -0.777  28.306 76.344  1.00 66.96  ? 272 LYS   A CD  1 
ATOM   2045 C CE  . LYS   A 1 283 ? 0.632   28.021 76.832  1.00 70.94  ? 272 LYS   A CE  1 
ATOM   2046 N NZ  . LYS   A 1 283 ? 1.294   29.238 77.406  1.00 72.64  ? 272 LYS   A NZ  1 
ATOM   2047 N N   . MET   A 1 284 ? -2.864  28.871 70.691  1.00 54.07  ? 273 MET   A N   1 
ATOM   2048 C CA  . MET   A 1 284 ? -3.411  29.862 69.755  1.00 54.19  ? 273 MET   A CA  1 
ATOM   2049 C C   . MET   A 1 284 ? -4.900  29.654 69.577  1.00 54.65  ? 273 MET   A C   1 
ATOM   2050 O O   . MET   A 1 284 ? -5.349  28.510 69.464  1.00 55.37  ? 273 MET   A O   1 
ATOM   2051 C CB  . MET   A 1 284 ? -2.753  29.769 68.357  1.00 54.41  ? 273 MET   A CB  1 
ATOM   2052 C CG  . MET   A 1 284 ? -1.271  30.037 68.335  1.00 56.85  ? 273 MET   A CG  1 
ATOM   2053 S SD  . MET   A 1 284 ? -0.765  31.599 69.088  1.00 63.59  ? 273 MET   A SD  1 
ATOM   2054 C CE  . MET   A 1 284 ? -1.615  32.719 68.113  1.00 62.23  ? 273 MET   A CE  1 
ATOM   2055 N N   . PRO   A 1 285 ? -5.675  30.746 69.484  1.00 54.28  ? 274 PRO   A N   1 
ATOM   2056 C CA  . PRO   A 1 285 ? -7.126  30.608 69.263  1.00 54.29  ? 274 PRO   A CA  1 
ATOM   2057 C C   . PRO   A 1 285 ? -7.529  29.797 68.026  1.00 54.47  ? 274 PRO   A C   1 
ATOM   2058 O O   . PRO   A 1 285 ? -8.517  29.068 68.077  1.00 54.29  ? 274 PRO   A O   1 
ATOM   2059 C CB  . PRO   A 1 285 ? -7.599  32.061 69.140  1.00 54.81  ? 274 PRO   A CB  1 
ATOM   2060 C CG  . PRO   A 1 285 ? -6.575  32.845 69.868  1.00 55.11  ? 274 PRO   A CG  1 
ATOM   2061 C CD  . PRO   A 1 285 ? -5.280  32.162 69.609  1.00 53.60  ? 274 PRO   A CD  1 
ATOM   2062 N N   . GLU   A 1 286 ? -6.778  29.915 66.919  1.00 54.72  ? 275 GLU   A N   1 
ATOM   2063 C CA  . GLU   A 1 286 ? -7.114  29.189 65.690  1.00 55.37  ? 275 GLU   A CA  1 
ATOM   2064 C C   . GLU   A 1 286 ? -6.311  27.892 65.506  1.00 55.22  ? 275 GLU   A C   1 
ATOM   2065 O O   . GLU   A 1 286 ? -6.172  27.413 64.377  1.00 55.25  ? 275 GLU   A O   1 
ATOM   2066 C CB  . GLU   A 1 286 ? -6.956  30.095 64.456  1.00 58.19  ? 275 GLU   A CB  1 
ATOM   2067 C CG  . GLU   A 1 286 ? -7.498  31.502 64.633  1.00 64.26  ? 275 GLU   A CG  1 
ATOM   2068 C CD  . GLU   A 1 286 ? -8.974  31.722 64.378  1.00 73.03  ? 275 GLU   A CD  1 
ATOM   2069 O OE1 . GLU   A 1 286 ? -9.723  30.723 64.270  1.00 75.20  ? 275 GLU   A OE1 1 
ATOM   2070 O OE2 . GLU   A 1 286 ? -9.381  32.905 64.289  1.00 75.56  ? 275 GLU   A OE2 1 
ATOM   2071 N N   . HIS   A 1 287 ? -5.800  27.315 66.604  1.00 54.85  ? 276 HIS   A N   1 
ATOM   2072 C CA  . HIS   A 1 287 ? -5.023  26.089 66.509  1.00 54.99  ? 276 HIS   A CA  1 
ATOM   2073 C C   . HIS   A 1 287 ? -5.834  24.903 66.001  1.00 55.69  ? 276 HIS   A C   1 
ATOM   2074 O O   . HIS   A 1 287 ? -5.343  24.199 65.118  1.00 56.15  ? 276 HIS   A O   1 
ATOM   2075 C CB  . HIS   A 1 287 ? -4.306  25.748 67.815  1.00 54.94  ? 276 HIS   A CB  1 
ATOM   2076 C CG  . HIS   A 1 287 ? -3.518  24.472 67.731  1.00 56.12  ? 276 HIS   A CG  1 
ATOM   2077 N ND1 . HIS   A 1 287 ? -3.972  23.304 68.318  1.00 57.58  ? 276 HIS   A ND1 1 
ATOM   2078 C CD2 . HIS   A 1 287 ? -2.359  24.210 67.081  1.00 57.07  ? 276 HIS   A CD2 1 
ATOM   2079 C CE1 . HIS   A 1 287 ? -3.054  22.386 68.052  1.00 58.04  ? 276 HIS   A CE1 1 
ATOM   2080 N NE2 . HIS   A 1 287 ? -2.064  22.884 67.315  1.00 58.06  ? 276 HIS   A NE2 1 
ATOM   2081 N N   . SER   A 1 288 ? -7.058  24.674 66.526  1.00 55.38  ? 277 SER   A N   1 
ATOM   2082 C CA  . SER   A 1 288 ? -7.849  23.536 66.049  1.00 55.69  ? 277 SER   A CA  1 
ATOM   2083 C C   . SER   A 1 288 ? -8.389  23.739 64.612  1.00 55.36  ? 277 SER   A C   1 
ATOM   2084 O O   . SER   A 1 288 ? -8.682  22.762 63.926  1.00 55.37  ? 277 SER   A O   1 
ATOM   2085 C CB  . SER   A 1 288 ? -8.939  23.154 67.042  1.00 57.45  ? 277 SER   A CB  1 
ATOM   2086 O OG  . SER   A 1 288 ? -8.421  22.242 68.002  1.00 59.35  ? 277 SER   A OG  1 
ATOM   2087 N N   . THR   A 1 289 ? -8.425  24.985 64.128  1.00 55.03  ? 278 THR   A N   1 
ATOM   2088 C CA  . THR   A 1 289 ? -8.790  25.276 62.737  1.00 54.99  ? 278 THR   A CA  1 
ATOM   2089 C C   . THR   A 1 289 ? -7.608  24.877 61.834  1.00 54.35  ? 278 THR   A C   1 
ATOM   2090 O O   . THR   A 1 289 ? -7.815  24.323 60.763  1.00 54.44  ? 278 THR   A O   1 
ATOM   2091 C CB  . THR   A 1 289 ? -9.110  26.767 62.545  1.00 56.58  ? 278 THR   A CB  1 
ATOM   2092 O OG1 . THR   A 1 289 ? -9.898  27.258 63.635  1.00 58.01  ? 278 THR   A OG1 1 
ATOM   2093 C CG2 . THR   A 1 289 ? -9.817  27.040 61.233  1.00 56.92  ? 278 THR   A CG2 1 
ATOM   2094 N N   . LEU   A 1 290 ? -6.375  25.153 62.282  1.00 53.70  ? 279 LEU   A N   1 
ATOM   2095 C CA  . LEU   A 1 290 ? -5.127  24.823 61.610  1.00 53.74  ? 279 LEU   A CA  1 
ATOM   2096 C C   . LEU   A 1 290 ? -4.989  23.298 61.532  1.00 54.62  ? 279 LEU   A C   1 
ATOM   2097 O O   . LEU   A 1 290 ? -4.606  22.778 60.493  1.00 54.68  ? 279 LEU   A O   1 
ATOM   2098 C CB  . LEU   A 1 290 ? -3.966  25.448 62.415  1.00 53.44  ? 279 LEU   A CB  1 
ATOM   2099 C CG  . LEU   A 1 290 ? -2.539  25.134 61.992  1.00 54.23  ? 279 LEU   A CG  1 
ATOM   2100 C CD1 . LEU   A 1 290 ? -2.170  25.886 60.757  1.00 54.81  ? 279 LEU   A CD1 1 
ATOM   2101 C CD2 . LEU   A 1 290 ? -1.562  25.504 63.083  1.00 54.43  ? 279 LEU   A CD2 1 
ATOM   2102 N N   . MET   A 1 291 ? -5.341  22.574 62.605  1.00 55.30  ? 280 MET   A N   1 
ATOM   2103 C CA  . MET   A 1 291 ? -5.279  21.105 62.605  1.00 56.37  ? 280 MET   A CA  1 
ATOM   2104 C C   . MET   A 1 291 ? -6.296  20.509 61.650  1.00 57.70  ? 280 MET   A C   1 
ATOM   2105 O O   . MET   A 1 291 ? -6.025  19.494 61.015  1.00 58.25  ? 280 MET   A O   1 
ATOM   2106 C CB  . MET   A 1 291 ? -5.530  20.532 64.006  1.00 56.74  ? 280 MET   A CB  1 
ATOM   2107 C CG  . MET   A 1 291 ? -4.674  21.142 65.082  1.00 58.10  ? 280 MET   A CG  1 
ATOM   2108 S SD  . MET   A 1 291 ? -2.949  20.647 65.002  1.00 58.09  ? 280 MET   A SD  1 
ATOM   2109 C CE  . MET   A 1 291 ? -2.227  22.074 64.282  1.00 57.29  ? 280 MET   A CE  1 
ATOM   2110 N N   . LYS   A 1 292 ? -7.472  21.114 61.562  1.00 58.37  ? 281 LYS   A N   1 
ATOM   2111 C CA  . LYS   A 1 292 ? -8.521  20.647 60.670  1.00 59.75  ? 281 LYS   A CA  1 
ATOM   2112 C C   . LYS   A 1 292 ? -8.164  20.916 59.189  1.00 60.69  ? 281 LYS   A C   1 
ATOM   2113 O O   . LYS   A 1 292 ? -8.346  20.043 58.344  1.00 60.58  ? 281 LYS   A O   1 
ATOM   2114 C CB  . LYS   A 1 292 ? -9.838  21.337 61.052  1.00 62.00  ? 281 LYS   A CB  1 
ATOM   2115 C CG  . LYS   A 1 292 ? -11.025 20.957 60.189  1.00 66.77  ? 281 LYS   A CG  1 
ATOM   2116 C CD  . LYS   A 1 292 ? -12.165 21.944 60.357  1.00 71.81  ? 281 LYS   A CD  1 
ATOM   2117 C CE  . LYS   A 1 292 ? -12.054 23.123 59.418  1.00 75.97  ? 281 LYS   A CE  1 
ATOM   2118 N NZ  . LYS   A 1 292 ? -10.893 24.008 59.726  1.00 77.84  ? 281 LYS   A NZ  1 
ATOM   2119 N N   . ASP   A 1 293 ? -7.619  22.108 58.889  1.00 61.31  ? 282 ASP   A N   1 
ATOM   2120 C CA  . ASP   A 1 293 ? -7.289  22.518 57.525  1.00 62.38  ? 282 ASP   A CA  1 
ATOM   2121 C C   . ASP   A 1 293 ? -5.955  22.025 56.972  1.00 63.14  ? 282 ASP   A C   1 
ATOM   2122 O O   . ASP   A 1 293 ? -5.798  21.963 55.746  1.00 63.75  ? 282 ASP   A O   1 
ATOM   2123 C CB  . ASP   A 1 293 ? -7.327  24.051 57.404  1.00 64.25  ? 282 ASP   A CB  1 
ATOM   2124 C CG  . ASP   A 1 293 ? -8.711  24.663 57.435  1.00 69.51  ? 282 ASP   A CG  1 
ATOM   2125 O OD1 . ASP   A 1 293 ? -9.698  23.910 57.284  1.00 70.30  ? 282 ASP   A OD1 1 
ATOM   2126 O OD2 . ASP   A 1 293 ? -8.808  25.899 57.603  1.00 71.96  ? 282 ASP   A OD2 1 
ATOM   2127 N N   . PHE   A 1 294 ? -4.978  21.741 57.839  1.00 62.83  ? 283 PHE   A N   1 
ATOM   2128 C CA  . PHE   A 1 294 ? -3.644  21.384 57.371  1.00 63.21  ? 283 PHE   A CA  1 
ATOM   2129 C C   . PHE   A 1 294 ? -3.141  20.022 57.840  1.00 64.54  ? 283 PHE   A C   1 
ATOM   2130 O O   . PHE   A 1 294 ? -3.613  19.498 58.845  1.00 64.88  ? 283 PHE   A O   1 
ATOM   2131 C CB  . PHE   A 1 294 ? -2.649  22.489 57.773  1.00 62.48  ? 283 PHE   A CB  1 
ATOM   2132 C CG  . PHE   A 1 294 ? -2.915  23.838 57.148  1.00 62.31  ? 283 PHE   A CG  1 
ATOM   2133 C CD1 . PHE   A 1 294 ? -2.365  24.173 55.930  1.00 62.66  ? 283 PHE   A CD1 1 
ATOM   2134 C CD2 . PHE   A 1 294 ? -3.717  24.772 57.782  1.00 62.60  ? 283 PHE   A CD2 1 
ATOM   2135 C CE1 . PHE   A 1 294 ? -2.604  25.416 55.363  1.00 63.01  ? 283 PHE   A CE1 1 
ATOM   2136 C CE2 . PHE   A 1 294 ? -3.963  26.007 57.206  1.00 62.64  ? 283 PHE   A CE2 1 
ATOM   2137 C CZ  . PHE   A 1 294 ? -3.397  26.324 56.007  1.00 62.44  ? 283 PHE   A CZ  1 
ATOM   2138 N N   . ARG   A 1 295 ? -2.163  19.455 57.121  1.00 65.12  ? 284 ARG   A N   1 
ATOM   2139 C CA  . ARG   A 1 295 ? -1.565  18.189 57.513  1.00 66.29  ? 284 ARG   A CA  1 
ATOM   2140 C C   . ARG   A 1 295 ? -0.055  18.293 57.401  1.00 66.32  ? 284 ARG   A C   1 
ATOM   2141 O O   . ARG   A 1 295 ? 0.456   18.769 56.384  1.00 66.19  ? 284 ARG   A O   1 
ATOM   2142 C CB  . ARG   A 1 295 ? -2.112  17.031 56.681  1.00 69.06  ? 284 ARG   A CB  1 
ATOM   2143 C CG  . ARG   A 1 295 ? -3.369  16.398 57.281  1.00 74.43  ? 284 ARG   A CG  1 
ATOM   2144 C CD  . ARG   A 1 295 ? -4.060  15.386 56.363  1.00 79.72  ? 284 ARG   A CD  1 
ATOM   2145 N NE  . ARG   A 1 295 ? -3.112  14.535 55.636  1.00 84.42  ? 284 ARG   A NE  1 
ATOM   2146 C CZ  . ARG   A 1 295 ? -2.540  13.446 56.138  1.00 87.94  ? 284 ARG   A CZ  1 
ATOM   2147 N NH1 . ARG   A 1 295 ? -2.841  13.033 57.364  1.00 88.05  ? 284 ARG   A NH1 1 
ATOM   2148 N NH2 . ARG   A 1 295 ? -1.676  12.751 55.412  1.00 88.23  ? 284 ARG   A NH2 1 
ATOM   2149 N N   . ARG   A 1 296 ? 0.653   17.882 58.467  1.00 66.18  ? 285 ARG   A N   1 
ATOM   2150 C CA  . ARG   A 1 296 ? 2.104   17.956 58.553  1.00 66.77  ? 285 ARG   A CA  1 
ATOM   2151 C C   . ARG   A 1 296 ? 2.840   17.409 57.324  1.00 67.44  ? 285 ARG   A C   1 
ATOM   2152 O O   . ARG   A 1 296 ? 3.809   18.027 56.880  1.00 68.12  ? 285 ARG   A O   1 
ATOM   2153 C CB  . ARG   A 1 296 ? 2.601   17.273 59.841  1.00 68.29  ? 285 ARG   A CB  1 
ATOM   2154 C CG  . ARG   A 1 296 ? 4.133   17.197 59.964  1.00 71.69  ? 285 ARG   A CG  1 
ATOM   2155 C CD  . ARG   A 1 296 ? 4.645   16.748 61.328  1.00 75.09  ? 285 ARG   A CD  1 
ATOM   2156 N NE  . ARG   A 1 296 ? 4.003   17.434 62.454  1.00 78.76  ? 285 ARG   A NE  1 
ATOM   2157 C CZ  . ARG   A 1 296 ? 4.259   18.689 62.815  1.00 81.99  ? 285 ARG   A CZ  1 
ATOM   2158 N NH1 . ARG   A 1 296 ? 5.120   19.424 62.123  1.00 81.74  ? 285 ARG   A NH1 1 
ATOM   2159 N NH2 . ARG   A 1 296 ? 3.627   19.229 63.852  1.00 82.28  ? 285 ARG   A NH2 1 
ATOM   2160 N N   . ASN   A 1 297 ? 2.391   16.263 56.781  1.00 67.11  ? 286 ASN   A N   1 
ATOM   2161 C CA  . ASN   A 1 297 ? 3.032   15.588 55.645  1.00 67.03  ? 286 ASN   A CA  1 
ATOM   2162 C C   . ASN   A 1 297 ? 2.938   16.373 54.314  1.00 65.82  ? 286 ASN   A C   1 
ATOM   2163 O O   . ASN   A 1 297 ? 3.762   16.144 53.422  1.00 66.06  ? 286 ASN   A O   1 
ATOM   2164 C CB  . ASN   A 1 297 ? 2.500   14.141 55.505  1.00 68.90  ? 286 ASN   A CB  1 
ATOM   2165 C CG  . ASN   A 1 297 ? 2.695   13.496 54.143  1.00 73.20  ? 286 ASN   A CG  1 
ATOM   2166 O OD1 . ASN   A 1 297 ? 1.775   13.487 53.299  1.00 74.52  ? 286 ASN   A OD1 1 
ATOM   2167 N ND2 . ASN   A 1 297 ? 3.905   12.991 53.885  1.00 73.91  ? 286 ASN   A ND2 1 
ATOM   2168 N N   . THR   A 1 298 ? 1.971   17.289 54.173  1.00 64.35  ? 287 THR   A N   1 
ATOM   2169 C CA  . THR   A 1 298 ? 1.849   18.091 52.940  1.00 63.66  ? 287 THR   A CA  1 
ATOM   2170 C C   . THR   A 1 298 ? 3.167   18.874 52.642  1.00 62.71  ? 287 THR   A C   1 
ATOM   2171 O O   . THR   A 1 298 ? 3.597   18.999 51.493  1.00 62.57  ? 287 THR   A O   1 
ATOM   2172 C CB  . THR   A 1 298 ? 0.676   19.088 53.080  1.00 64.56  ? 287 THR   A CB  1 
ATOM   2173 O OG1 . THR   A 1 298 ? -0.467  18.441 53.643  1.00 65.33  ? 287 THR   A OG1 1 
ATOM   2174 C CG2 . THR   A 1 298 ? 0.307   19.742 51.765  1.00 64.84  ? 287 THR   A CG2 1 
ATOM   2175 N N   . TYR   A 1 299 ? 3.817   19.327 53.720  1.00 61.65  ? 288 TYR   A N   1 
ATOM   2176 C CA  . TYR   A 1 299 ? 5.022   20.137 53.741  1.00 61.07  ? 288 TYR   A CA  1 
ATOM   2177 C C   . TYR   A 1 299 ? 6.175   19.319 54.315  1.00 60.98  ? 288 TYR   A C   1 
ATOM   2178 O O   . TYR   A 1 299 ? 6.936   19.816 55.158  1.00 61.46  ? 288 TYR   A O   1 
ATOM   2179 C CB  . TYR   A 1 299 ? 4.770   21.384 54.619  1.00 60.72  ? 288 TYR   A CB  1 
ATOM   2180 C CG  . TYR   A 1 299 ? 3.439   22.039 54.348  1.00 60.86  ? 288 TYR   A CG  1 
ATOM   2181 C CD1 . TYR   A 1 299 ? 3.249   22.824 53.222  1.00 61.46  ? 288 TYR   A CD1 1 
ATOM   2182 C CD2 . TYR   A 1 299 ? 2.342   21.785 55.158  1.00 61.43  ? 288 TYR   A CD2 1 
ATOM   2183 C CE1 . TYR   A 1 299 ? 2.019   23.393 52.942  1.00 62.18  ? 288 TYR   A CE1 1 
ATOM   2184 C CE2 . TYR   A 1 299 ? 1.099   22.328 54.874  1.00 62.22  ? 288 TYR   A CE2 1 
ATOM   2185 C CZ  . TYR   A 1 299 ? 0.944   23.137 53.766  1.00 63.00  ? 288 TYR   A CZ  1 
ATOM   2186 O OH  . TYR   A 1 299 ? -0.274  23.682 53.471  1.00 64.43  ? 288 TYR   A OH  1 
ATOM   2187 N N   . THR   A 1 300 ? 6.319   18.065 53.854  1.00 60.13  ? 289 THR   A N   1 
ATOM   2188 C CA  . THR   A 1 300 ? 7.355   17.193 54.392  1.00 59.78  ? 289 THR   A CA  1 
ATOM   2189 C C   . THR   A 1 300 ? 8.753   17.552 53.872  1.00 58.91  ? 289 THR   A C   1 
ATOM   2190 O O   . THR   A 1 300 ? 9.709   17.494 54.648  1.00 59.06  ? 289 THR   A O   1 
ATOM   2191 C CB  . THR   A 1 300 ? 6.998   15.723 54.213  1.00 61.17  ? 289 THR   A CB  1 
ATOM   2192 O OG1 . THR   A 1 300 ? 7.926   14.950 54.971  1.00 62.31  ? 289 THR   A OG1 1 
ATOM   2193 C CG2 . THR   A 1 300 ? 6.994   15.285 52.758  1.00 61.58  ? 289 THR   A CG2 1 
ATOM   2194 N N   . ASN   A 1 301 ? 8.882   17.946 52.601  1.00 57.99  ? 290 ASN   A N   1 
ATOM   2195 C CA  . ASN   A 1 301 ? 10.192  18.351 52.080  1.00 57.98  ? 290 ASN   A CA  1 
ATOM   2196 C C   . ASN   A 1 301 ? 10.337  19.883 52.038  1.00 56.79  ? 290 ASN   A C   1 
ATOM   2197 O O   . ASN   A 1 301 ? 11.097  20.405 51.226  1.00 56.77  ? 290 ASN   A O   1 
ATOM   2198 C CB  . ASN   A 1 301 ? 10.451  17.727 50.713  1.00 60.14  ? 290 ASN   A CB  1 
ATOM   2199 C CG  . ASN   A 1 301 ? 10.572  16.219 50.768  1.00 64.69  ? 290 ASN   A CG  1 
ATOM   2200 O OD1 . ASN   A 1 301 ? 11.510  15.657 51.357  1.00 66.03  ? 290 ASN   A OD1 1 
ATOM   2201 N ND2 . ASN   A 1 301 ? 9.621   15.529 50.150  1.00 65.68  ? 290 ASN   A ND2 1 
ATOM   2202 N N   . CYS   A 1 302 ? 9.608   20.600 52.916  1.00 55.38  ? 291 CYS   A N   1 
ATOM   2203 C CA  . CYS   A 1 302 ? 9.625   22.045 52.956  1.00 54.40  ? 291 CYS   A CA  1 
ATOM   2204 C C   . CYS   A 1 302 ? 10.495  22.536 54.056  1.00 53.66  ? 291 CYS   A C   1 
ATOM   2205 O O   . CYS   A 1 302 ? 10.322  22.147 55.204  1.00 53.83  ? 291 CYS   A O   1 
ATOM   2206 C CB  . CYS   A 1 302 ? 8.213   22.598 53.078  1.00 54.93  ? 291 CYS   A CB  1 
ATOM   2207 S SG  . CYS   A 1 302 ? 7.164   22.245 51.647  1.00 58.61  ? 291 CYS   A SG  1 
ATOM   2208 N N   . SER   A 1 303 ? 11.443  23.396 53.709  1.00 52.85  ? 292 SER   A N   1 
ATOM   2209 C CA  . SER   A 1 303 ? 12.366  24.008 54.662  1.00 52.30  ? 292 SER   A CA  1 
ATOM   2210 C C   . SER   A 1 303 ? 12.821  25.368 54.134  1.00 51.86  ? 292 SER   A C   1 
ATOM   2211 O O   . SER   A 1 303 ? 12.677  25.643 52.931  1.00 52.35  ? 292 SER   A O   1 
ATOM   2212 C CB  . SER   A 1 303 ? 13.578  23.106 54.876  1.00 52.77  ? 292 SER   A CB  1 
ATOM   2213 O OG  . SER   A 1 303 ? 14.322  22.950 53.681  1.00 54.21  ? 292 SER   A OG  1 
ATOM   2214 N N   . LEU   A 1 304 ? 13.327  26.240 55.019  1.00 50.67  ? 293 LEU   A N   1 
ATOM   2215 C CA  . LEU   A 1 304 ? 13.870  27.522 54.568  1.00 50.08  ? 293 LEU   A CA  1 
ATOM   2216 C C   . LEU   A 1 304 ? 15.153  27.259 53.744  1.00 49.75  ? 293 LEU   A C   1 
ATOM   2217 O O   . LEU   A 1 304 ? 15.392  27.948 52.756  1.00 49.97  ? 293 LEU   A O   1 
ATOM   2218 C CB  . LEU   A 1 304 ? 14.171  28.434 55.758  1.00 50.13  ? 293 LEU   A CB  1 
ATOM   2219 C CG  . LEU   A 1 304 ? 14.567  29.867 55.436  1.00 51.09  ? 293 LEU   A CG  1 
ATOM   2220 C CD1 . LEU   A 1 304 ? 13.460  30.586 54.698  1.00 51.69  ? 293 LEU   A CD1 1 
ATOM   2221 C CD2 . LEU   A 1 304 ? 14.923  30.613 56.692  1.00 51.50  ? 293 LEU   A CD2 1 
ATOM   2222 N N   . ILE   A 1 305 ? 15.936  26.218 54.119  1.00 49.12  ? 294 ILE   A N   1 
ATOM   2223 C CA  . ILE   A 1 305 ? 17.143  25.784 53.432  1.00 49.07  ? 294 ILE   A CA  1 
ATOM   2224 C C   . ILE   A 1 305 ? 16.873  25.540 51.950  1.00 49.62  ? 294 ILE   A C   1 
ATOM   2225 O O   . ILE   A 1 305 ? 17.503  26.185 51.117  1.00 49.88  ? 294 ILE   A O   1 
ATOM   2226 C CB  . ILE   A 1 305 ? 17.724  24.524 54.118  1.00 49.04  ? 294 ILE   A CB  1 
ATOM   2227 C CG1 . ILE   A 1 305 ? 18.101  24.823 55.600  1.00 49.94  ? 294 ILE   A CG1 1 
ATOM   2228 C CG2 . ILE   A 1 305 ? 18.858  23.913 53.284  1.00 49.09  ? 294 ILE   A CG2 1 
ATOM   2229 C CD1 . ILE   A 1 305 ? 19.549  25.017 55.938  1.00 51.25  ? 294 ILE   A CD1 1 
ATOM   2230 N N   . LYS   A 1 306 ? 15.901  24.669 51.626  1.00 49.81  ? 295 LYS   A N   1 
ATOM   2231 C CA  . LYS   A 1 306 ? 15.548  24.310 50.260  1.00 50.63  ? 295 LYS   A CA  1 
ATOM   2232 C C   . LYS   A 1 306 ? 15.024  25.491 49.467  1.00 50.87  ? 295 LYS   A C   1 
ATOM   2233 O O   . LYS   A 1 306 ? 15.300  25.587 48.269  1.00 50.65  ? 295 LYS   A O   1 
ATOM   2234 C CB  . LYS   A 1 306 ? 14.566  23.122 50.251  1.00 53.40  ? 295 LYS   A CB  1 
ATOM   2235 C CG  . LYS   A 1 306 ? 15.230  21.815 50.688  1.00 58.65  ? 295 LYS   A CG  1 
ATOM   2236 C CD  . LYS   A 1 306 ? 14.291  20.623 50.675  1.00 64.60  ? 295 LYS   A CD  1 
ATOM   2237 C CE  . LYS   A 1 306 ? 13.902  20.166 49.281  1.00 69.30  ? 295 LYS   A CE  1 
ATOM   2238 N NZ  . LYS   A 1 306 ? 13.239  18.819 49.283  1.00 71.33  ? 295 LYS   A NZ  1 
ATOM   2239 N N   . TYR   A 1 307 ? 14.299  26.415 50.137  1.00 51.10  ? 296 TYR   A N   1 
ATOM   2240 C CA  . TYR   A 1 307 ? 13.777  27.607 49.478  1.00 51.55  ? 296 TYR   A CA  1 
ATOM   2241 C C   . TYR   A 1 307 ? 14.931  28.537 49.068  1.00 52.56  ? 296 TYR   A C   1 
ATOM   2242 O O   . TYR   A 1 307 ? 14.971  29.014 47.929  1.00 52.56  ? 296 TYR   A O   1 
ATOM   2243 C CB  . TYR   A 1 307 ? 12.754  28.349 50.369  1.00 51.01  ? 296 TYR   A CB  1 
ATOM   2244 C CG  . TYR   A 1 307 ? 12.279  29.645 49.739  1.00 51.19  ? 296 TYR   A CG  1 
ATOM   2245 C CD1 . TYR   A 1 307 ? 11.328  29.642 48.729  1.00 51.70  ? 296 TYR   A CD1 1 
ATOM   2246 C CD2 . TYR   A 1 307 ? 12.837  30.865 50.102  1.00 51.52  ? 296 TYR   A CD2 1 
ATOM   2247 C CE1 . TYR   A 1 307 ? 10.921  30.824 48.118  1.00 52.22  ? 296 TYR   A CE1 1 
ATOM   2248 C CE2 . TYR   A 1 307 ? 12.445  32.050 49.491  1.00 51.91  ? 296 TYR   A CE2 1 
ATOM   2249 C CZ  . TYR   A 1 307 ? 11.483  32.026 48.501  1.00 52.66  ? 296 TYR   A CZ  1 
ATOM   2250 O OH  . TYR   A 1 307 ? 11.095  33.187 47.882  1.00 53.70  ? 296 TYR   A OH  1 
ATOM   2251 N N   . MET   A 1 308 ? 15.853  28.810 50.005  1.00 53.08  ? 297 MET   A N   1 
ATOM   2252 C CA  . MET   A 1 308 ? 16.978  29.693 49.720  1.00 53.76  ? 297 MET   A CA  1 
ATOM   2253 C C   . MET   A 1 308 ? 17.993  29.059 48.785  1.00 54.97  ? 297 MET   A C   1 
ATOM   2254 O O   . MET   A 1 308 ? 18.651  29.788 48.059  1.00 55.25  ? 297 MET   A O   1 
ATOM   2255 C CB  . MET   A 1 308 ? 17.636  30.218 50.999  1.00 53.59  ? 297 MET   A CB  1 
ATOM   2256 C CG  . MET   A 1 308 ? 16.657  30.832 51.963  1.00 54.68  ? 297 MET   A CG  1 
ATOM   2257 S SD  . MET   A 1 308 ? 15.676  32.208 51.328  1.00 55.81  ? 297 MET   A SD  1 
ATOM   2258 C CE  . MET   A 1 308 ? 16.932  33.346 50.941  1.00 53.71  ? 297 MET   A CE  1 
ATOM   2259 N N   . GLU   A 1 309 ? 18.091  27.720 48.752  1.00 55.63  ? 298 GLU   A N   1 
ATOM   2260 C CA  . GLU   A 1 309 ? 18.990  27.027 47.827  1.00 56.81  ? 298 GLU   A CA  1 
ATOM   2261 C C   . GLU   A 1 309 ? 18.508  27.260 46.392  1.00 57.41  ? 298 GLU   A C   1 
ATOM   2262 O O   . GLU   A 1 309 ? 19.325  27.571 45.524  1.00 57.60  ? 298 GLU   A O   1 
ATOM   2263 C CB  . GLU   A 1 309 ? 19.075  25.524 48.143  1.00 59.41  ? 298 GLU   A CB  1 
ATOM   2264 C CG  . GLU   A 1 309 ? 20.444  25.109 48.653  1.00 65.44  ? 298 GLU   A CG  1 
ATOM   2265 C CD  . GLU   A 1 309 ? 20.488  23.816 49.447  1.00 74.18  ? 298 GLU   A CD  1 
ATOM   2266 O OE1 . GLU   A 1 309 ? 19.407  23.228 49.689  1.00 76.33  ? 298 GLU   A OE1 1 
ATOM   2267 O OE2 . GLU   A 1 309 ? 21.605  23.391 49.831  1.00 76.49  ? 298 GLU   A OE2 1 
ATOM   2268 N N   . LYS   A 1 310 ? 17.176  27.183 46.166  1.00 57.38  ? 299 LYS   A N   1 
ATOM   2269 C CA  . LYS   A 1 310 ? 16.555  27.465 44.868  1.00 57.74  ? 299 LYS   A CA  1 
ATOM   2270 C C   . LYS   A 1 310 ? 16.799  28.908 44.449  1.00 57.77  ? 299 LYS   A C   1 
ATOM   2271 O O   . LYS   A 1 310 ? 16.988  29.189 43.268  1.00 57.91  ? 299 LYS   A O   1 
ATOM   2272 C CB  . LYS   A 1 310 ? 15.037  27.224 44.917  1.00 59.71  ? 299 LYS   A CB  1 
ATOM   2273 C CG  . LYS   A 1 310 ? 14.664  25.761 45.003  1.00 64.18  ? 299 LYS   A CG  1 
ATOM   2274 C CD  . LYS   A 1 310 ? 13.159  25.536 44.989  1.00 68.11  ? 299 LYS   A CD  1 
ATOM   2275 C CE  . LYS   A 1 310 ? 12.807  24.207 45.613  1.00 71.09  ? 299 LYS   A CE  1 
ATOM   2276 N NZ  . LYS   A 1 310 ? 13.805  23.152 45.277  1.00 72.98  ? 299 LYS   A NZ  1 
ATOM   2277 N N   . HIS   A 1 311 ? 16.775  29.827 45.409  1.00 57.75  ? 300 HIS   A N   1 
ATOM   2278 C CA  . HIS   A 1 311 ? 16.989  31.235 45.130  1.00 58.14  ? 300 HIS   A CA  1 
ATOM   2279 C C   . HIS   A 1 311 ? 18.448  31.662 45.291  1.00 59.13  ? 300 HIS   A C   1 
ATOM   2280 O O   . HIS   A 1 311 ? 18.727  32.822 45.570  1.00 59.71  ? 300 HIS   A O   1 
ATOM   2281 C CB  . HIS   A 1 311 ? 16.032  32.069 45.964  1.00 58.30  ? 300 HIS   A CB  1 
ATOM   2282 C CG  . HIS   A 1 311 ? 14.611  31.910 45.517  1.00 59.71  ? 300 HIS   A CG  1 
ATOM   2283 N ND1 . HIS   A 1 311 ? 13.992  32.864 44.725  1.00 61.21  ? 300 HIS   A ND1 1 
ATOM   2284 C CD2 . HIS   A 1 311 ? 13.749  30.884 45.716  1.00 60.70  ? 300 HIS   A CD2 1 
ATOM   2285 C CE1 . HIS   A 1 311 ? 12.772  32.405 44.493  1.00 61.76  ? 300 HIS   A CE1 1 
ATOM   2286 N NE2 . HIS   A 1 311 ? 12.579  31.213 45.064  1.00 61.71  ? 300 HIS   A NE2 1 
ATOM   2287 N N   . LYS   A 1 312 ? 19.369  30.720 45.051  1.00 59.49  ? 301 LYS   A N   1 
ATOM   2288 C CA  . LYS   A 1 312 ? 20.817  30.857 45.067  1.00 60.30  ? 301 LYS   A CA  1 
ATOM   2289 C C   . LYS   A 1 312 ? 21.373  31.653 46.259  1.00 60.44  ? 301 LYS   A C   1 
ATOM   2290 O O   . LYS   A 1 312 ? 22.085  32.640 46.078  1.00 61.15  ? 301 LYS   A O   1 
ATOM   2291 C CB  . LYS   A 1 312 ? 21.299  31.412 43.731  1.00 62.69  ? 301 LYS   A CB  1 
ATOM   2292 C CG  . LYS   A 1 312 ? 20.949  30.461 42.582  1.00 68.20  ? 301 LYS   A CG  1 
ATOM   2293 C CD  . LYS   A 1 312 ? 21.859  30.686 41.372  1.00 74.93  ? 301 LYS   A CD  1 
ATOM   2294 C CE  . LYS   A 1 312 ? 21.578  29.746 40.217  1.00 80.13  ? 301 LYS   A CE  1 
ATOM   2295 N NZ  . LYS   A 1 312 ? 22.369  30.103 38.999  1.00 82.80  ? 301 LYS   A NZ  1 
ATOM   2296 N N   . VAL   A 1 313 ? 21.053  31.200 47.477  1.00 59.60  ? 302 VAL   A N   1 
ATOM   2297 C CA  . VAL   A 1 313 ? 21.526  31.761 48.743  1.00 59.43  ? 302 VAL   A CA  1 
ATOM   2298 C C   . VAL   A 1 313 ? 22.091  30.580 49.545  1.00 59.89  ? 302 VAL   A C   1 
ATOM   2299 O O   . VAL   A 1 313 ? 21.340  29.674 49.922  1.00 60.03  ? 302 VAL   A O   1 
ATOM   2300 C CB  . VAL   A 1 313 ? 20.399  32.483 49.517  1.00 59.26  ? 302 VAL   A CB  1 
ATOM   2301 C CG1 . VAL   A 1 313 ? 20.843  32.829 50.933  1.00 59.56  ? 302 VAL   A CG1 1 
ATOM   2302 C CG2 . VAL   A 1 313 ? 19.927  33.725 48.773  1.00 59.19  ? 302 VAL   A CG2 1 
ATOM   2303 N N   . LYS   A 1 314 ? 23.414  30.543 49.736  1.00 59.84  ? 303 LYS   A N   1 
ATOM   2304 C CA  . LYS   A 1 314 ? 24.053  29.424 50.424  1.00 60.26  ? 303 LYS   A CA  1 
ATOM   2305 C C   . LYS   A 1 314 ? 23.567  29.228 51.856  1.00 59.98  ? 303 LYS   A C   1 
ATOM   2306 O O   . LYS   A 1 314 ? 23.641  30.138 52.679  1.00 60.19  ? 303 LYS   A O   1 
ATOM   2307 C CB  . LYS   A 1 314 ? 25.584  29.541 50.368  1.00 62.81  ? 303 LYS   A CB  1 
ATOM   2308 C CG  . LYS   A 1 314 ? 26.128  29.591 48.943  1.00 67.95  ? 303 LYS   A CG  1 
ATOM   2309 C CD  . LYS   A 1 314 ? 27.597  29.238 48.909  1.00 73.76  ? 303 LYS   A CD  1 
ATOM   2310 C CE  . LYS   A 1 314 ? 28.121  29.000 47.512  1.00 78.63  ? 303 LYS   A CE  1 
ATOM   2311 N NZ  . LYS   A 1 314 ? 29.448  28.304 47.526  1.00 81.55  ? 303 LYS   A NZ  1 
ATOM   2312 N N   . PRO   A 1 315 ? 23.058  28.027 52.170  1.00 59.26  ? 304 PRO   A N   1 
ATOM   2313 C CA  . PRO   A 1 315 ? 22.566  27.774 53.534  1.00 58.35  ? 304 PRO   A CA  1 
ATOM   2314 C C   . PRO   A 1 315 ? 23.660  27.791 54.601  1.00 56.92  ? 304 PRO   A C   1 
ATOM   2315 O O   . PRO   A 1 315 ? 23.352  27.988 55.774  1.00 57.06  ? 304 PRO   A O   1 
ATOM   2316 C CB  . PRO   A 1 315 ? 21.884  26.401 53.424  1.00 59.32  ? 304 PRO   A CB  1 
ATOM   2317 C CG  . PRO   A 1 315 ? 21.719  26.149 51.954  1.00 59.99  ? 304 PRO   A CG  1 
ATOM   2318 C CD  . PRO   A 1 315 ? 22.876  26.847 51.307  1.00 58.70  ? 304 PRO   A CD  1 
ATOM   2319 N N   . ASP   A 1 316 ? 24.925  27.585 54.212  1.00 55.55  ? 305 ASP   A N   1 
ATOM   2320 C CA  . ASP   A 1 316 ? 26.017  27.659 55.181  1.00 55.18  ? 305 ASP   A CA  1 
ATOM   2321 C C   . ASP   A 1 316 ? 26.559  29.107 55.345  1.00 53.87  ? 305 ASP   A C   1 
ATOM   2322 O O   . ASP   A 1 316 ? 27.504  29.315 56.098  1.00 54.32  ? 305 ASP   A O   1 
ATOM   2323 C CB  . ASP   A 1 316 ? 27.133  26.641 54.885  1.00 57.51  ? 305 ASP   A CB  1 
ATOM   2324 C CG  . ASP   A 1 316 ? 27.655  26.684 53.460  1.00 64.00  ? 305 ASP   A CG  1 
ATOM   2325 O OD1 . ASP   A 1 316 ? 26.974  26.134 52.556  1.00 65.43  ? 305 ASP   A OD1 1 
ATOM   2326 O OD2 . ASP   A 1 316 ? 28.747  27.259 53.246  1.00 66.46  ? 305 ASP   A OD2 1 
ATOM   2327 N N   . SER   A 1 317 ? 25.948  30.101 54.681  1.00 51.87  ? 306 SER   A N   1 
ATOM   2328 C CA  . SER   A 1 317 ? 26.373  31.487 54.800  1.00 50.91  ? 306 SER   A CA  1 
ATOM   2329 C C   . SER   A 1 317 ? 25.922  32.110 56.125  1.00 49.94  ? 306 SER   A C   1 
ATOM   2330 O O   . SER   A 1 317 ? 24.933  31.665 56.712  1.00 50.37  ? 306 SER   A O   1 
ATOM   2331 C CB  . SER   A 1 317 ? 25.807  32.310 53.645  1.00 51.92  ? 306 SER   A CB  1 
ATOM   2332 O OG  . SER   A 1 317 ? 24.389  32.355 53.688  1.00 53.44  ? 306 SER   A OG  1 
ATOM   2333 N N   . LYS   A 1 318 ? 26.612  33.171 56.574  1.00 48.36  ? 307 LYS   A N   1 
ATOM   2334 C CA  . LYS   A 1 318 ? 26.200  33.877 57.780  1.00 47.73  ? 307 LYS   A CA  1 
ATOM   2335 C C   . LYS   A 1 318 ? 24.893  34.671 57.558  1.00 47.27  ? 307 LYS   A C   1 
ATOM   2336 O O   . LYS   A 1 318 ? 24.189  34.979 58.523  1.00 47.25  ? 307 LYS   A O   1 
ATOM   2337 C CB  . LYS   A 1 318 ? 27.320  34.781 58.301  1.00 49.48  ? 307 LYS   A CB  1 
ATOM   2338 C CG  . LYS   A 1 318 ? 28.420  34.018 59.023  1.00 52.31  ? 307 LYS   A CG  1 
ATOM   2339 C CD  . LYS   A 1 318 ? 29.220  34.915 59.942  1.00 55.20  ? 307 LYS   A CD  1 
ATOM   2340 C CE  . LYS   A 1 318 ? 30.533  34.293 60.319  1.00 58.04  ? 307 LYS   A CE  1 
ATOM   2341 N NZ  . LYS   A 1 318 ? 31.581  34.543 59.287  1.00 60.16  ? 307 LYS   A NZ  1 
ATOM   2342 N N   . ALA   A 1 319 ? 24.586  35.013 56.288  1.00 46.62  ? 308 ALA   A N   1 
ATOM   2343 C CA  . ALA   A 1 319 ? 23.352  35.677 55.880  1.00 46.04  ? 308 ALA   A CA  1 
ATOM   2344 C C   . ALA   A 1 319 ? 22.182  34.702 56.063  1.00 45.27  ? 308 ALA   A C   1 
ATOM   2345 O O   . ALA   A 1 319 ? 21.111  35.133 56.492  1.00 45.30  ? 308 ALA   A O   1 
ATOM   2346 C CB  . ALA   A 1 319 ? 23.442  36.090 54.423  1.00 45.90  ? 308 ALA   A CB  1 
ATOM   2347 N N   . PHE   A 1 320 ? 22.379  33.390 55.745  1.00 44.27  ? 309 PHE   A N   1 
ATOM   2348 C CA  . PHE   A 1 320 ? 21.302  32.409 55.920  1.00 43.81  ? 309 PHE   A CA  1 
ATOM   2349 C C   . PHE   A 1 320 ? 20.968  32.192 57.395  1.00 43.59  ? 309 PHE   A C   1 
ATOM   2350 O O   . PHE   A 1 320 ? 19.811  32.299 57.787  1.00 43.56  ? 309 PHE   A O   1 
ATOM   2351 C CB  . PHE   A 1 320 ? 21.571  31.066 55.218  1.00 43.34  ? 309 PHE   A CB  1 
ATOM   2352 C CG  . PHE   A 1 320 ? 20.397  30.123 55.408  1.00 43.77  ? 309 PHE   A CG  1 
ATOM   2353 C CD1 . PHE   A 1 320 ? 19.280  30.207 54.592  1.00 44.22  ? 309 PHE   A CD1 1 
ATOM   2354 C CD2 . PHE   A 1 320 ? 20.366  29.230 56.469  1.00 44.25  ? 309 PHE   A CD2 1 
ATOM   2355 C CE1 . PHE   A 1 320 ? 18.188  29.381 54.801  1.00 44.66  ? 309 PHE   A CE1 1 
ATOM   2356 C CE2 . PHE   A 1 320 ? 19.267  28.414 56.679  1.00 44.68  ? 309 PHE   A CE2 1 
ATOM   2357 C CZ  . PHE   A 1 320 ? 18.194  28.481 55.837  1.00 44.52  ? 309 PHE   A CZ  1 
ATOM   2358 N N   . HIS   A 1 321 ? 21.976  31.901 58.210  1.00 43.25  ? 310 HIS   A N   1 
ATOM   2359 C CA  . HIS   A 1 321 ? 21.798  31.701 59.640  1.00 43.20  ? 310 HIS   A CA  1 
ATOM   2360 C C   . HIS   A 1 321 ? 21.094  32.878 60.330  1.00 43.46  ? 310 HIS   A C   1 
ATOM   2361 O O   . HIS   A 1 321 ? 20.208  32.641 61.146  1.00 44.04  ? 310 HIS   A O   1 
ATOM   2362 C CB  . HIS   A 1 321 ? 23.140  31.361 60.283  1.00 43.20  ? 310 HIS   A CB  1 
ATOM   2363 C CG  . HIS   A 1 321 ? 23.601  30.012 59.855  1.00 44.54  ? 310 HIS   A CG  1 
ATOM   2364 N ND1 . HIS   A 1 321 ? 23.254  28.875 60.570  1.00 45.87  ? 310 HIS   A ND1 1 
ATOM   2365 C CD2 . HIS   A 1 321 ? 24.250  29.638 58.728  1.00 45.46  ? 310 HIS   A CD2 1 
ATOM   2366 C CE1 . HIS   A 1 321 ? 23.762  27.858 59.892  1.00 46.14  ? 310 HIS   A CE1 1 
ATOM   2367 N NE2 . HIS   A 1 321 ? 24.358  28.265 58.770  1.00 46.22  ? 310 HIS   A NE2 1 
ATOM   2368 N N   . LEU   A 1 322 ? 21.416  34.133 59.948  1.00 42.68  ? 311 LEU   A N   1 
ATOM   2369 C CA  . LEU   A 1 322 ? 20.736  35.291 60.524  1.00 42.08  ? 311 LEU   A CA  1 
ATOM   2370 C C   . LEU   A 1 322 ? 19.285  35.320 60.066  1.00 42.17  ? 311 LEU   A C   1 
ATOM   2371 O O   . LEU   A 1 322 ? 18.386  35.505 60.888  1.00 42.47  ? 311 LEU   A O   1 
ATOM   2372 C CB  . LEU   A 1 322 ? 21.428  36.616 60.162  1.00 41.60  ? 311 LEU   A CB  1 
ATOM   2373 C CG  . LEU   A 1 322 ? 20.722  37.883 60.687  1.00 42.43  ? 311 LEU   A CG  1 
ATOM   2374 C CD1 . LEU   A 1 322 ? 20.526  37.824 62.209  1.00 43.54  ? 311 LEU   A CD1 1 
ATOM   2375 C CD2 . LEU   A 1 322 ? 21.445  39.153 60.276  1.00 42.00  ? 311 LEU   A CD2 1 
ATOM   2376 N N   . LEU   A 1 323 ? 19.045  35.089 58.759  1.00 41.67  ? 312 LEU   A N   1 
ATOM   2377 C CA  . LEU   A 1 323 ? 17.702  35.088 58.173  1.00 41.45  ? 312 LEU   A CA  1 
ATOM   2378 C C   . LEU   A 1 323 ? 16.807  34.092 58.904  1.00 41.75  ? 312 LEU   A C   1 
ATOM   2379 O O   . LEU   A 1 323 ? 15.692  34.435 59.288  1.00 42.03  ? 312 LEU   A O   1 
ATOM   2380 C CB  . LEU   A 1 323 ? 17.763  34.782 56.655  1.00 41.09  ? 312 LEU   A CB  1 
ATOM   2381 C CG  . LEU   A 1 323 ? 16.430  34.445 55.973  1.00 42.10  ? 312 LEU   A CG  1 
ATOM   2382 C CD1 . LEU   A 1 323 ? 15.525  35.656 55.889  1.00 42.46  ? 312 LEU   A CD1 1 
ATOM   2383 C CD2 . LEU   A 1 323 ? 16.643  33.812 54.621  1.00 42.35  ? 312 LEU   A CD2 1 
ATOM   2384 N N   . GLN   A 1 324 ? 17.351  32.903 59.172  1.00 41.50  ? 313 GLN   A N   1 
ATOM   2385 C CA  . GLN   A 1 324 ? 16.667  31.812 59.849  1.00 41.77  ? 313 GLN   A CA  1 
ATOM   2386 C C   . GLN   A 1 324 ? 16.293  32.151 61.278  1.00 41.33  ? 313 GLN   A C   1 
ATOM   2387 O O   . GLN   A 1 324 ? 15.252  31.696 61.768  1.00 41.64  ? 313 GLN   A O   1 
ATOM   2388 C CB  . GLN   A 1 324 ? 17.529  30.550 59.803  1.00 43.86  ? 313 GLN   A CB  1 
ATOM   2389 C CG  . GLN   A 1 324 ? 16.802  29.324 60.298  1.00 48.61  ? 313 GLN   A CG  1 
ATOM   2390 C CD  . GLN   A 1 324 ? 17.435  28.057 59.810  1.00 54.66  ? 313 GLN   A CD  1 
ATOM   2391 O OE1 . GLN   A 1 324 ? 16.769  27.198 59.219  1.00 57.50  ? 313 GLN   A OE1 1 
ATOM   2392 N NE2 . GLN   A 1 324 ? 18.732  27.906 60.047  1.00 55.31  ? 313 GLN   A NE2 1 
ATOM   2393 N N   . LYS   A 1 325 ? 17.137  32.940 61.951  1.00 40.45  ? 314 LYS   A N   1 
ATOM   2394 C CA  . LYS   A 1 325 ? 16.879  33.349 63.326  1.00 40.25  ? 314 LYS   A CA  1 
ATOM   2395 C C   . LYS   A 1 325 ? 15.802  34.412 63.413  1.00 40.80  ? 314 LYS   A C   1 
ATOM   2396 O O   . LYS   A 1 325 ? 15.151  34.509 64.447  1.00 41.64  ? 314 LYS   A O   1 
ATOM   2397 C CB  . LYS   A 1 325 ? 18.166  33.789 64.022  1.00 40.90  ? 314 LYS   A CB  1 
ATOM   2398 C CG  . LYS   A 1 325 ? 19.120  32.630 64.220  1.00 43.00  ? 314 LYS   A CG  1 
ATOM   2399 C CD  . LYS   A 1 325 ? 20.524  33.076 64.544  1.00 45.74  ? 314 LYS   A CD  1 
ATOM   2400 C CE  . LYS   A 1 325 ? 21.418  31.872 64.712  1.00 48.26  ? 314 LYS   A CE  1 
ATOM   2401 N NZ  . LYS   A 1 325 ? 22.789  32.255 65.124  1.00 49.35  ? 314 LYS   A NZ  1 
ATOM   2402 N N   . LEU   A 1 326 ? 15.592  35.197 62.330  1.00 40.06  ? 315 LEU   A N   1 
ATOM   2403 C CA  . LEU   A 1 326 ? 14.526  36.193 62.244  1.00 39.55  ? 315 LEU   A CA  1 
ATOM   2404 C C   . LEU   A 1 326 ? 13.243  35.477 61.826  1.00 39.37  ? 315 LEU   A C   1 
ATOM   2405 O O   . LEU   A 1 326 ? 12.193  35.784 62.370  1.00 39.76  ? 315 LEU   A O   1 
ATOM   2406 C CB  . LEU   A 1 326 ? 14.858  37.304 61.217  1.00 39.22  ? 315 LEU   A CB  1 
ATOM   2407 C CG  . LEU   A 1 326 ? 16.142  38.098 61.474  1.00 39.50  ? 315 LEU   A CG  1 
ATOM   2408 C CD1 . LEU   A 1 326 ? 16.731  38.625 60.187  1.00 39.50  ? 315 LEU   A CD1 1 
ATOM   2409 C CD2 . LEU   A 1 326 ? 15.919  39.200 62.488  1.00 39.48  ? 315 LEU   A CD2 1 
ATOM   2410 N N   . LEU   A 1 327 ? 13.316  34.528 60.873  1.00 38.74  ? 316 LEU   A N   1 
ATOM   2411 C CA  . LEU   A 1 327 ? 12.140  33.791 60.411  1.00 39.25  ? 316 LEU   A CA  1 
ATOM   2412 C C   . LEU   A 1 327 ? 11.891  32.508 61.226  1.00 39.52  ? 316 LEU   A C   1 
ATOM   2413 O O   . LEU   A 1 327 ? 11.891  31.406 60.686  1.00 39.78  ? 316 LEU   A O   1 
ATOM   2414 C CB  . LEU   A 1 327 ? 12.226  33.459 58.906  1.00 39.85  ? 316 LEU   A CB  1 
ATOM   2415 C CG  . LEU   A 1 327 ? 12.033  34.597 57.895  1.00 41.88  ? 316 LEU   A CG  1 
ATOM   2416 C CD1 . LEU   A 1 327 ? 12.027  34.063 56.481  1.00 42.15  ? 316 LEU   A CD1 1 
ATOM   2417 C CD2 . LEU   A 1 327 ? 10.745  35.358 58.141  1.00 42.84  ? 316 LEU   A CD2 1 
ATOM   2418 N N   . THR   A 1 328 ? 11.697  32.651 62.526  1.00 39.21  ? 317 THR   A N   1 
ATOM   2419 C CA  . THR   A 1 328 ? 11.394  31.528 63.400  1.00 39.47  ? 317 THR   A CA  1 
ATOM   2420 C C   . THR   A 1 328 ? 9.897   31.538 63.599  1.00 39.97  ? 317 THR   A C   1 
ATOM   2421 O O   . THR   A 1 328 ? 9.345   32.591 63.874  1.00 40.57  ? 317 THR   A O   1 
ATOM   2422 C CB  . THR   A 1 328 ? 12.092  31.717 64.734  1.00 40.63  ? 317 THR   A CB  1 
ATOM   2423 O OG1 . THR   A 1 328 ? 13.509  31.611 64.543  1.00 41.74  ? 317 THR   A OG1 1 
ATOM   2424 C CG2 . THR   A 1 328 ? 11.604  30.747 65.784  1.00 40.74  ? 317 THR   A CG2 1 
ATOM   2425 N N   . MET   A 1 329 ? 9.232   30.390 63.466  1.00 39.60  ? 318 MET   A N   1 
ATOM   2426 C CA  . MET   A 1 329 ? 7.786   30.306 63.618  1.00 39.40  ? 318 MET   A CA  1 
ATOM   2427 C C   . MET   A 1 329 ? 7.323   30.776 64.995  1.00 39.28  ? 318 MET   A C   1 
ATOM   2428 O O   . MET   A 1 329 ? 6.414   31.597 65.076  1.00 38.86  ? 318 MET   A O   1 
ATOM   2429 C CB  . MET   A 1 329 ? 7.338   28.863 63.379  1.00 40.15  ? 318 MET   A CB  1 
ATOM   2430 C CG  . MET   A 1 329 ? 7.667   28.369 62.009  1.00 42.04  ? 318 MET   A CG  1 
ATOM   2431 S SD  . MET   A 1 329 ? 6.554   29.103 60.812  1.00 43.17  ? 318 MET   A SD  1 
ATOM   2432 C CE  . MET   A 1 329 ? 5.893   27.667 60.089  1.00 40.62  ? 318 MET   A CE  1 
ATOM   2433 N N   . ASP   A 1 330 ? 7.973   30.283 66.072  1.00 39.49  ? 319 ASP   A N   1 
ATOM   2434 C CA  . ASP   A 1 330 ? 7.619   30.625 67.445  1.00 40.02  ? 319 ASP   A CA  1 
ATOM   2435 C C   . ASP   A 1 330 ? 8.098   32.022 67.802  1.00 40.92  ? 319 ASP   A C   1 
ATOM   2436 O O   . ASP   A 1 330 ? 9.306   32.282 67.866  1.00 40.98  ? 319 ASP   A O   1 
ATOM   2437 C CB  . ASP   A 1 330 ? 8.187   29.588 68.435  1.00 41.43  ? 319 ASP   A CB  1 
ATOM   2438 C CG  . ASP   A 1 330 ? 7.562   29.639 69.826  1.00 46.15  ? 319 ASP   A CG  1 
ATOM   2439 O OD1 . ASP   A 1 330 ? 6.917   30.652 70.147  1.00 47.04  ? 319 ASP   A OD1 1 
ATOM   2440 O OD2 . ASP   A 1 330 ? 7.708   28.648 70.590  1.00 47.96  ? 319 ASP   A OD2 1 
ATOM   2441 N N   . PRO   A 1 331 ? 7.153   32.926 68.121  1.00 41.11  ? 320 PRO   A N   1 
ATOM   2442 C CA  . PRO   A 1 331 ? 7.545   34.285 68.505  1.00 41.43  ? 320 PRO   A CA  1 
ATOM   2443 C C   . PRO   A 1 331 ? 8.510   34.337 69.680  1.00 42.64  ? 320 PRO   A C   1 
ATOM   2444 O O   . PRO   A 1 331 ? 9.386   35.197 69.679  1.00 43.75  ? 320 PRO   A O   1 
ATOM   2445 C CB  . PRO   A 1 331 ? 6.218   34.944 68.855  1.00 41.62  ? 320 PRO   A CB  1 
ATOM   2446 C CG  . PRO   A 1 331 ? 5.251   33.821 69.037  1.00 41.74  ? 320 PRO   A CG  1 
ATOM   2447 C CD  . PRO   A 1 331 ? 5.687   32.785 68.090  1.00 40.30  ? 320 PRO   A CD  1 
ATOM   2448 N N   . ILE   A 1 332 ? 8.378   33.433 70.669  1.00 42.30  ? 321 ILE   A N   1 
ATOM   2449 C CA  . ILE   A 1 332 ? 9.300   33.443 71.810  1.00 42.40  ? 321 ILE   A CA  1 
ATOM   2450 C C   . ILE   A 1 332 ? 10.683  32.876 71.412  1.00 42.21  ? 321 ILE   A C   1 
ATOM   2451 O O   . ILE   A 1 332 ? 11.675  33.240 72.032  1.00 42.98  ? 321 ILE   A O   1 
ATOM   2452 C CB  . ILE   A 1 332 ? 8.714   32.807 73.103  1.00 42.86  ? 321 ILE   A CB  1 
ATOM   2453 C CG1 . ILE   A 1 332 ? 8.301   31.361 72.889  1.00 43.97  ? 321 ILE   A CG1 1 
ATOM   2454 C CG2 . ILE   A 1 332 ? 7.522   33.604 73.598  1.00 43.34  ? 321 ILE   A CG2 1 
ATOM   2455 C CD1 . ILE   A 1 332 ? 9.308   30.369 73.202  1.00 45.30  ? 321 ILE   A CD1 1 
ATOM   2456 N N   . LYS   A 1 333 ? 10.761  32.029 70.380  1.00 41.30  ? 322 LYS   A N   1 
ATOM   2457 C CA  . LYS   A 1 333 ? 12.051  31.504 69.907  1.00 41.21  ? 322 LYS   A CA  1 
ATOM   2458 C C   . LYS   A 1 333 ? 12.675  32.390 68.796  1.00 41.73  ? 322 LYS   A C   1 
ATOM   2459 O O   . LYS   A 1 333 ? 13.611  31.961 68.123  1.00 42.42  ? 322 LYS   A O   1 
ATOM   2460 C CB  . LYS   A 1 333 ? 11.912  30.048 69.409  1.00 41.51  ? 322 LYS   A CB  1 
ATOM   2461 C CG  . LYS   A 1 333 ? 11.662  29.049 70.523  1.00 43.55  ? 322 LYS   A CG  1 
ATOM   2462 C CD  . LYS   A 1 333 ? 11.439  27.646 70.001  1.00 46.83  ? 322 LYS   A CD  1 
ATOM   2463 C CE  . LYS   A 1 333 ? 11.711  26.611 71.074  1.00 49.90  ? 322 LYS   A CE  1 
ATOM   2464 N NZ  . LYS   A 1 333 ? 10.747  25.475 71.053  1.00 50.65  ? 322 LYS   A NZ  1 
ATOM   2465 N N   . ARG   A 1 334 ? 12.140  33.597 68.583  1.00 41.02  ? 323 ARG   A N   1 
ATOM   2466 C CA  . ARG   A 1 334 ? 12.589  34.513 67.546  1.00 40.78  ? 323 ARG   A CA  1 
ATOM   2467 C C   . ARG   A 1 334 ? 13.601  35.474 68.156  1.00 40.84  ? 323 ARG   A C   1 
ATOM   2468 O O   . ARG   A 1 334 ? 13.390  35.988 69.258  1.00 41.34  ? 323 ARG   A O   1 
ATOM   2469 C CB  . ARG   A 1 334 ? 11.368  35.287 67.028  1.00 41.49  ? 323 ARG   A CB  1 
ATOM   2470 C CG  . ARG   A 1 334 ? 11.425  35.705 65.585  1.00 42.87  ? 323 ARG   A CG  1 
ATOM   2471 C CD  . ARG   A 1 334 ? 10.075  36.240 65.169  1.00 44.09  ? 323 ARG   A CD  1 
ATOM   2472 N NE  . ARG   A 1 334 ? 9.152   35.147 64.891  1.00 46.20  ? 323 ARG   A NE  1 
ATOM   2473 C CZ  . ARG   A 1 334 ? 7.826   35.253 64.888  1.00 48.94  ? 323 ARG   A CZ  1 
ATOM   2474 N NH1 . ARG   A 1 334 ? 7.243   36.407 65.185  1.00 49.05  ? 323 ARG   A NH1 1 
ATOM   2475 N NH2 . ARG   A 1 334 ? 7.072   34.201 64.607  1.00 48.66  ? 323 ARG   A NH2 1 
ATOM   2476 N N   . ILE   A 1 335 ? 14.690  35.726 67.451  1.00 40.10  ? 324 ILE   A N   1 
ATOM   2477 C CA  . ILE   A 1 335 ? 15.746  36.619 67.910  1.00 40.30  ? 324 ILE   A CA  1 
ATOM   2478 C C   . ILE   A 1 335 ? 15.228  38.058 68.142  1.00 40.86  ? 324 ILE   A C   1 
ATOM   2479 O O   . ILE   A 1 335 ? 14.137  38.429 67.676  1.00 41.43  ? 324 ILE   A O   1 
ATOM   2480 C CB  . ILE   A 1 335 ? 16.822  36.568 66.806  1.00 41.04  ? 324 ILE   A CB  1 
ATOM   2481 C CG1 . ILE   A 1 335 ? 18.221  36.783 67.351  1.00 41.99  ? 324 ILE   A CG1 1 
ATOM   2482 C CG2 . ILE   A 1 335 ? 16.510  37.522 65.637  1.00 41.88  ? 324 ILE   A CG2 1 
ATOM   2483 C CD1 . ILE   A 1 335 ? 19.352  36.735 66.215  1.00 43.35  ? 324 ILE   A CD1 1 
ATOM   2484 N N   . THR   A 1 336 ? 16.008  38.874 68.848  1.00 40.34  ? 325 THR   A N   1 
ATOM   2485 C CA  . THR   A 1 336 ? 15.641  40.277 69.050  1.00 40.07  ? 325 THR   A CA  1 
ATOM   2486 C C   . THR   A 1 336 ? 16.443  41.148 68.067  1.00 40.31  ? 325 THR   A C   1 
ATOM   2487 O O   . THR   A 1 336 ? 17.426  40.683 67.490  1.00 40.21  ? 325 THR   A O   1 
ATOM   2488 C CB  . THR   A 1 336 ? 15.844  40.685 70.506  1.00 40.65  ? 325 THR   A CB  1 
ATOM   2489 O OG1 . THR   A 1 336 ? 17.235  40.619 70.836  1.00 41.58  ? 325 THR   A OG1 1 
ATOM   2490 C CG2 . THR   A 1 336 ? 15.023  39.851 71.466  1.00 40.34  ? 325 THR   A CG2 1 
ATOM   2491 N N   . SER   A 1 337 ? 16.024  42.398 67.862  1.00 40.43  ? 326 SER   A N   1 
ATOM   2492 C CA  . SER   A 1 337 ? 16.728  43.315 66.962  1.00 41.21  ? 326 SER   A CA  1 
ATOM   2493 C C   . SER   A 1 337 ? 18.120  43.668 67.495  1.00 42.11  ? 326 SER   A C   1 
ATOM   2494 O O   . SER   A 1 337 ? 19.028  43.912 66.709  1.00 42.64  ? 326 SER   A O   1 
ATOM   2495 C CB  . SER   A 1 337 ? 15.928  44.595 66.789  1.00 42.14  ? 326 SER   A CB  1 
ATOM   2496 O OG  . SER   A 1 337 ? 15.704  45.149 68.073  1.00 44.62  ? 326 SER   A OG  1 
ATOM   2497 N N   . GLU   A 1 338 ? 18.279  43.722 68.821  1.00 42.16  ? 327 GLU   A N   1 
ATOM   2498 C CA  . GLU   A 1 338 ? 19.554  43.979 69.489  1.00 42.88  ? 327 GLU   A CA  1 
ATOM   2499 C C   . GLU   A 1 338 ? 20.484  42.798 69.163  1.00 42.41  ? 327 GLU   A C   1 
ATOM   2500 O O   . GLU   A 1 338 ? 21.623  43.008 68.755  1.00 42.80  ? 327 GLU   A O   1 
ATOM   2501 C CB  . GLU   A 1 338 ? 19.347  44.058 71.026  1.00 47.40  ? 327 GLU   A CB  1 
ATOM   2502 C CG  . GLU   A 1 338 ? 17.977  44.578 71.473  1.00 55.68  ? 327 GLU   A CG  1 
ATOM   2503 C CD  . GLU   A 1 338 ? 17.054  43.649 72.247  1.00 63.79  ? 327 GLU   A CD  1 
ATOM   2504 O OE1 . GLU   A 1 338 ? 17.562  42.769 72.985  1.00 63.94  ? 327 GLU   A OE1 1 
ATOM   2505 O OE2 . GLU   A 1 338 ? 15.816  43.810 72.116  1.00 66.75  ? 327 GLU   A OE2 1 
ATOM   2506 N N   . GLN   A 1 339 ? 19.968  41.554 69.305  1.00 41.53  ? 328 GLN   A N   1 
ATOM   2507 C CA  . GLN   A 1 339 ? 20.677  40.310 69.032  1.00 41.03  ? 328 GLN   A CA  1 
ATOM   2508 C C   . GLN   A 1 339 ? 21.021  40.150 67.561  1.00 40.24  ? 328 GLN   A C   1 
ATOM   2509 O O   . GLN   A 1 339 ? 22.071  39.611 67.234  1.00 40.38  ? 328 GLN   A O   1 
ATOM   2510 C CB  . GLN   A 1 339 ? 19.821  39.134 69.450  1.00 42.62  ? 328 GLN   A CB  1 
ATOM   2511 C CG  . GLN   A 1 339 ? 19.967  38.717 70.885  1.00 46.59  ? 328 GLN   A CG  1 
ATOM   2512 C CD  . GLN   A 1 339 ? 19.002  37.599 71.149  1.00 51.43  ? 328 GLN   A CD  1 
ATOM   2513 O OE1 . GLN   A 1 339 ? 17.818  37.662 70.770  1.00 52.41  ? 328 GLN   A OE1 1 
ATOM   2514 N NE2 . GLN   A 1 339 ? 19.486  36.546 71.790  1.00 52.77  ? 328 GLN   A NE2 1 
ATOM   2515 N N   . ALA   A 1 340 ? 20.134  40.595 66.672  1.00 39.38  ? 329 ALA   A N   1 
ATOM   2516 C CA  . ALA   A 1 340 ? 20.373  40.528 65.243  1.00 38.96  ? 329 ALA   A CA  1 
ATOM   2517 C C   . ALA   A 1 340 ? 21.530  41.458 64.892  1.00 39.15  ? 329 ALA   A C   1 
ATOM   2518 O O   . ALA   A 1 340 ? 22.432  41.030 64.188  1.00 39.28  ? 329 ALA   A O   1 
ATOM   2519 C CB  . ALA   A 1 340 ? 19.123  40.920 64.477  1.00 38.54  ? 329 ALA   A CB  1 
ATOM   2520 N N   . MET   A 1 341 ? 21.568  42.677 65.468  1.00 38.94  ? 330 MET   A N   1 
ATOM   2521 C CA  . MET   A 1 341 ? 22.646  43.642 65.230  1.00 39.76  ? 330 MET   A CA  1 
ATOM   2522 C C   . MET   A 1 341 ? 24.028  43.128 65.673  1.00 40.59  ? 330 MET   A C   1 
ATOM   2523 O O   . MET   A 1 341 ? 25.050  43.482 65.082  1.00 40.21  ? 330 MET   A O   1 
ATOM   2524 C CB  . MET   A 1 341 ? 22.329  44.977 65.905  1.00 40.49  ? 330 MET   A CB  1 
ATOM   2525 C CG  . MET   A 1 341 ? 21.287  45.786 65.175  1.00 41.98  ? 330 MET   A CG  1 
ATOM   2526 S SD  . MET   A 1 341 ? 20.693  47.154 66.202  1.00 45.09  ? 330 MET   A SD  1 
ATOM   2527 C CE  . MET   A 1 341 ? 22.114  48.130 66.282  1.00 42.03  ? 330 MET   A CE  1 
ATOM   2528 N N   . GLN   A 1 342 ? 24.052  42.254 66.687  1.00 41.53  ? 331 GLN   A N   1 
ATOM   2529 C CA  . GLN   A 1 342 ? 25.287  41.627 67.123  1.00 42.40  ? 331 GLN   A CA  1 
ATOM   2530 C C   . GLN   A 1 342 ? 25.658  40.367 66.342  1.00 42.70  ? 331 GLN   A C   1 
ATOM   2531 O O   . GLN   A 1 342 ? 26.663  39.750 66.674  1.00 43.51  ? 331 GLN   A O   1 
ATOM   2532 C CB  . GLN   A 1 342 ? 25.264  41.326 68.608  1.00 44.77  ? 331 GLN   A CB  1 
ATOM   2533 C CG  . GLN   A 1 342 ? 25.957  42.406 69.377  1.00 51.34  ? 331 GLN   A CG  1 
ATOM   2534 C CD  . GLN   A 1 342 ? 24.957  43.081 70.250  1.00 59.91  ? 331 GLN   A CD  1 
ATOM   2535 O OE1 . GLN   A 1 342 ? 24.279  42.426 71.059  1.00 62.82  ? 331 GLN   A OE1 1 
ATOM   2536 N NE2 . GLN   A 1 342 ? 24.827  44.399 70.089  1.00 61.35  ? 331 GLN   A NE2 1 
ATOM   2537 N N   . ASP   A 1 343 ? 24.904  39.993 65.305  1.00 42.09  ? 332 ASP   A N   1 
ATOM   2538 C CA  . ASP   A 1 343 ? 25.222  38.795 64.526  1.00 42.28  ? 332 ASP   A CA  1 
ATOM   2539 C C   . ASP   A 1 343 ? 26.607  38.907 63.852  1.00 42.30  ? 332 ASP   A C   1 
ATOM   2540 O O   . ASP   A 1 343 ? 26.951  39.985 63.372  1.00 42.79  ? 332 ASP   A O   1 
ATOM   2541 C CB  . ASP   A 1 343 ? 24.130  38.517 63.471  1.00 42.76  ? 332 ASP   A CB  1 
ATOM   2542 C CG  . ASP   A 1 343 ? 24.127  37.078 63.040  1.00 44.96  ? 332 ASP   A CG  1 
ATOM   2543 O OD1 . ASP   A 1 343 ? 23.843  36.208 63.888  1.00 45.31  ? 332 ASP   A OD1 1 
ATOM   2544 O OD2 . ASP   A 1 343 ? 24.463  36.811 61.873  1.00 46.47  ? 332 ASP   A OD2 1 
ATOM   2545 N N   . PRO   A 1 344 ? 27.398  37.817 63.784  1.00 41.56  ? 333 PRO   A N   1 
ATOM   2546 C CA  . PRO   A 1 344 ? 28.703  37.900 63.116  1.00 41.77  ? 333 PRO   A CA  1 
ATOM   2547 C C   . PRO   A 1 344 ? 28.638  38.245 61.626  1.00 42.05  ? 333 PRO   A C   1 
ATOM   2548 O O   . PRO   A 1 344 ? 29.662  38.631 61.064  1.00 41.81  ? 333 PRO   A O   1 
ATOM   2549 C CB  . PRO   A 1 344 ? 29.301  36.503 63.335  1.00 42.36  ? 333 PRO   A CB  1 
ATOM   2550 C CG  . PRO   A 1 344 ? 28.150  35.624 63.598  1.00 42.26  ? 333 PRO   A CG  1 
ATOM   2551 C CD  . PRO   A 1 344 ? 27.161  36.465 64.321  1.00 40.75  ? 333 PRO   A CD  1 
ATOM   2552 N N   . TYR   A 1 345 ? 27.449  38.132 60.994  1.00 42.21  ? 334 TYR   A N   1 
ATOM   2553 C CA  . TYR   A 1 345 ? 27.218  38.466 59.590  1.00 42.98  ? 334 TYR   A CA  1 
ATOM   2554 C C   . TYR   A 1 345 ? 27.603  39.923 59.329  1.00 43.74  ? 334 TYR   A C   1 
ATOM   2555 O O   . TYR   A 1 345 ? 28.166  40.231 58.277  1.00 43.90  ? 334 TYR   A O   1 
ATOM   2556 C CB  . TYR   A 1 345 ? 25.744  38.222 59.256  1.00 43.32  ? 334 TYR   A CB  1 
ATOM   2557 C CG  . TYR   A 1 345 ? 25.238  38.851 57.975  1.00 44.63  ? 334 TYR   A CG  1 
ATOM   2558 C CD1 . TYR   A 1 345 ? 25.755  38.476 56.743  1.00 46.13  ? 334 TYR   A CD1 1 
ATOM   2559 C CD2 . TYR   A 1 345 ? 24.167  39.733 57.987  1.00 45.46  ? 334 TYR   A CD2 1 
ATOM   2560 C CE1 . TYR   A 1 345 ? 25.255  39.005 55.560  1.00 47.18  ? 334 TYR   A CE1 1 
ATOM   2561 C CE2 . TYR   A 1 345 ? 23.660  40.272 56.810  1.00 46.65  ? 334 TYR   A CE2 1 
ATOM   2562 C CZ  . TYR   A 1 345 ? 24.203  39.898 55.596  1.00 48.08  ? 334 TYR   A CZ  1 
ATOM   2563 O OH  . TYR   A 1 345 ? 23.730  40.422 54.420  1.00 50.04  ? 334 TYR   A OH  1 
ATOM   2564 N N   . PHE   A 1 346 ? 27.305  40.818 60.295  1.00 43.88  ? 335 PHE   A N   1 
ATOM   2565 C CA  . PHE   A 1 346 ? 27.638  42.237 60.209  1.00 44.09  ? 335 PHE   A CA  1 
ATOM   2566 C C   . PHE   A 1 346 ? 29.144  42.507 60.388  1.00 44.65  ? 335 PHE   A C   1 
ATOM   2567 O O   . PHE   A 1 346 ? 29.617  43.575 60.001  1.00 45.09  ? 335 PHE   A O   1 
ATOM   2568 C CB  . PHE   A 1 346 ? 26.775  43.057 61.175  1.00 43.85  ? 335 PHE   A CB  1 
ATOM   2569 C CG  . PHE   A 1 346 ? 25.308  42.976 60.826  1.00 44.61  ? 335 PHE   A CG  1 
ATOM   2570 C CD1 . PHE   A 1 346 ? 24.846  43.414 59.598  1.00 45.35  ? 335 PHE   A CD1 1 
ATOM   2571 C CD2 . PHE   A 1 346 ? 24.394  42.436 61.716  1.00 45.33  ? 335 PHE   A CD2 1 
ATOM   2572 C CE1 . PHE   A 1 346 ? 23.499  43.316 59.269  1.00 45.87  ? 335 PHE   A CE1 1 
ATOM   2573 C CE2 . PHE   A 1 346 ? 23.048  42.339 61.381  1.00 45.73  ? 335 PHE   A CE2 1 
ATOM   2574 C CZ  . PHE   A 1 346 ? 22.611  42.770 60.160  1.00 45.53  ? 335 PHE   A CZ  1 
ATOM   2575 N N   . LEU   A 1 347 ? 29.897  41.541 60.942  1.00 44.71  ? 336 LEU   A N   1 
ATOM   2576 C CA  . LEU   A 1 347 ? 31.354  41.598 61.097  1.00 45.56  ? 336 LEU   A CA  1 
ATOM   2577 C C   . LEU   A 1 347 ? 32.076  41.029 59.846  1.00 46.57  ? 336 LEU   A C   1 
ATOM   2578 O O   . LEU   A 1 347 ? 33.233  41.357 59.609  1.00 46.80  ? 336 LEU   A O   1 
ATOM   2579 C CB  . LEU   A 1 347 ? 31.801  40.798 62.335  1.00 45.54  ? 336 LEU   A CB  1 
ATOM   2580 C CG  . LEU   A 1 347 ? 31.291  41.257 63.680  1.00 46.22  ? 336 LEU   A CG  1 
ATOM   2581 C CD1 . LEU   A 1 347 ? 31.793  40.352 64.770  1.00 46.43  ? 336 LEU   A CD1 1 
ATOM   2582 C CD2 . LEU   A 1 347 ? 31.720  42.660 63.958  1.00 46.77  ? 336 LEU   A CD2 1 
ATOM   2583 N N   . GLU   A 1 348 ? 31.406  40.142 59.091  1.00 46.98  ? 337 GLU   A N   1 
ATOM   2584 C CA  . GLU   A 1 348 ? 31.897  39.511 57.865  1.00 47.79  ? 337 GLU   A CA  1 
ATOM   2585 C C   . GLU   A 1 348 ? 32.016  40.573 56.760  1.00 48.82  ? 337 GLU   A C   1 
ATOM   2586 O O   . GLU   A 1 348 ? 31.219  41.507 56.711  1.00 48.94  ? 337 GLU   A O   1 
ATOM   2587 C CB  . GLU   A 1 348 ? 30.879  38.442 57.435  1.00 49.47  ? 337 GLU   A CB  1 
ATOM   2588 C CG  . GLU   A 1 348 ? 31.415  37.282 56.624  1.00 53.22  ? 337 GLU   A CG  1 
ATOM   2589 C CD  . GLU   A 1 348 ? 30.323  36.328 56.165  1.00 58.75  ? 337 GLU   A CD  1 
ATOM   2590 O OE1 . GLU   A 1 348 ? 29.398  36.786 55.453  1.00 60.02  ? 337 GLU   A OE1 1 
ATOM   2591 O OE2 . GLU   A 1 348 ? 30.386  35.127 56.517  1.00 59.47  ? 337 GLU   A OE2 1 
ATOM   2592 N N   . ASP   A 1 349 ? 33.005  40.433 55.877  1.00 49.41  ? 338 ASP   A N   1 
ATOM   2593 C CA  . ASP   A 1 349 ? 33.206  41.388 54.788  1.00 50.15  ? 338 ASP   A CA  1 
ATOM   2594 C C   . ASP   A 1 349 ? 32.089  41.237 53.749  1.00 49.96  ? 338 ASP   A C   1 
ATOM   2595 O O   . ASP   A 1 349 ? 31.739  40.112 53.399  1.00 49.62  ? 338 ASP   A O   1 
ATOM   2596 C CB  . ASP   A 1 349 ? 34.590  41.162 54.136  1.00 52.19  ? 338 ASP   A CB  1 
ATOM   2597 C CG  . ASP   A 1 349 ? 34.957  42.154 53.042  1.00 57.73  ? 338 ASP   A CG  1 
ATOM   2598 O OD1 . ASP   A 1 349 ? 34.997  43.378 53.331  1.00 58.06  ? 338 ASP   A OD1 1 
ATOM   2599 O OD2 . ASP   A 1 349 ? 35.209  41.710 51.897  1.00 60.54  ? 338 ASP   A OD2 1 
ATOM   2600 N N   . PRO   A 1 350 ? 31.509  42.345 53.249  1.00 50.00  ? 339 PRO   A N   1 
ATOM   2601 C CA  . PRO   A 1 350 ? 31.787  43.754 53.596  1.00 50.28  ? 339 PRO   A CA  1 
ATOM   2602 C C   . PRO   A 1 350 ? 31.038  44.250 54.843  1.00 50.59  ? 339 PRO   A C   1 
ATOM   2603 O O   . PRO   A 1 350 ? 29.994  43.689 55.181  1.00 50.95  ? 339 PRO   A O   1 
ATOM   2604 C CB  . PRO   A 1 350 ? 31.312  44.506 52.344  1.00 50.76  ? 339 PRO   A CB  1 
ATOM   2605 C CG  . PRO   A 1 350 ? 30.159  43.688 51.838  1.00 51.06  ? 339 PRO   A CG  1 
ATOM   2606 C CD  . PRO   A 1 350 ? 30.458  42.239 52.215  1.00 49.63  ? 339 PRO   A CD  1 
ATOM   2607 N N   . LEU   A 1 351 ? 31.560  45.281 55.529  1.00 50.02  ? 340 LEU   A N   1 
ATOM   2608 C CA  . LEU   A 1 351 ? 30.840  45.819 56.682  1.00 49.81  ? 340 LEU   A CA  1 
ATOM   2609 C C   . LEU   A 1 351 ? 29.654  46.646 56.179  1.00 49.48  ? 340 LEU   A C   1 
ATOM   2610 O O   . LEU   A 1 351 ? 29.712  47.201 55.077  1.00 49.67  ? 340 LEU   A O   1 
ATOM   2611 C CB  . LEU   A 1 351 ? 31.755  46.712 57.543  1.00 50.07  ? 340 LEU   A CB  1 
ATOM   2612 C CG  . LEU   A 1 351 ? 32.950  46.091 58.262  1.00 51.75  ? 340 LEU   A CG  1 
ATOM   2613 C CD1 . LEU   A 1 351 ? 33.423  47.011 59.374  1.00 52.06  ? 340 LEU   A CD1 1 
ATOM   2614 C CD2 . LEU   A 1 351 ? 32.624  44.725 58.861  1.00 52.73  ? 340 LEU   A CD2 1 
ATOM   2615 N N   . PRO   A 1 352 ? 28.582  46.790 56.981  1.00 48.99  ? 341 PRO   A N   1 
ATOM   2616 C CA  . PRO   A 1 352 ? 27.487  47.675 56.567  1.00 48.80  ? 341 PRO   A CA  1 
ATOM   2617 C C   . PRO   A 1 352 ? 27.983  49.120 56.484  1.00 49.69  ? 341 PRO   A C   1 
ATOM   2618 O O   . PRO   A 1 352 ? 28.862  49.541 57.253  1.00 49.84  ? 341 PRO   A O   1 
ATOM   2619 C CB  . PRO   A 1 352 ? 26.457  47.526 57.692  1.00 49.14  ? 341 PRO   A CB  1 
ATOM   2620 C CG  . PRO   A 1 352 ? 26.858  46.316 58.455  1.00 49.72  ? 341 PRO   A CG  1 
ATOM   2621 C CD  . PRO   A 1 352 ? 28.341  46.224 58.323  1.00 48.40  ? 341 PRO   A CD  1 
ATOM   2622 N N   . THR   A 1 353 ? 27.446  49.877 55.533  1.00 50.06  ? 342 THR   A N   1 
ATOM   2623 C CA  . THR   A 1 353 ? 27.813  51.280 55.384  1.00 50.69  ? 342 THR   A CA  1 
ATOM   2624 C C   . THR   A 1 353 ? 26.670  52.195 55.805  1.00 51.20  ? 342 THR   A C   1 
ATOM   2625 O O   . THR   A 1 353 ? 25.511  51.783 55.841  1.00 50.83  ? 342 THR   A O   1 
ATOM   2626 C CB  . THR   A 1 353 ? 28.275  51.552 53.959  1.00 51.65  ? 342 THR   A CB  1 
ATOM   2627 O OG1 . THR   A 1 353 ? 27.237  51.149 53.064  1.00 52.60  ? 342 THR   A OG1 1 
ATOM   2628 C CG2 . THR   A 1 353 ? 29.552  50.814 53.629  1.00 51.76  ? 342 THR   A CG2 1 
ATOM   2629 N N   . SER   A 1 354 ? 27.002  53.435 56.149  1.00 52.18  ? 343 SER   A N   1 
ATOM   2630 C CA  . SER   A 1 354 ? 25.984  54.434 56.495  1.00 53.69  ? 343 SER   A CA  1 
ATOM   2631 C C   . SER   A 1 354 ? 25.189  54.896 55.252  1.00 54.79  ? 343 SER   A C   1 
ATOM   2632 O O   . SER   A 1 354 ? 24.101  55.441 55.380  1.00 55.25  ? 343 SER   A O   1 
ATOM   2633 C CB  . SER   A 1 354 ? 26.616  55.624 57.205  1.00 55.30  ? 343 SER   A CB  1 
ATOM   2634 O OG  . SER   A 1 354 ? 27.745  56.092 56.489  1.00 58.48  ? 343 SER   A OG  1 
ATOM   2635 N N   . ASP   A 1 355 ? 25.730  54.657 54.063  1.00 55.25  ? 344 ASP   A N   1 
ATOM   2636 C CA  . ASP   A 1 355 ? 25.132  54.935 52.777  1.00 56.39  ? 344 ASP   A CA  1 
ATOM   2637 C C   . ASP   A 1 355 ? 24.976  53.550 52.119  1.00 57.07  ? 344 ASP   A C   1 
ATOM   2638 O O   . ASP   A 1 355 ? 25.969  52.955 51.701  1.00 57.21  ? 344 ASP   A O   1 
ATOM   2639 C CB  . ASP   A 1 355 ? 26.108  55.816 51.984  1.00 58.24  ? 344 ASP   A CB  1 
ATOM   2640 C CG  . ASP   A 1 355 ? 25.689  56.185 50.585  1.00 63.45  ? 344 ASP   A CG  1 
ATOM   2641 O OD1 . ASP   A 1 355 ? 24.705  55.598 50.083  1.00 64.23  ? 344 ASP   A OD1 1 
ATOM   2642 O OD2 . ASP   A 1 355 ? 26.365  57.041 49.973  1.00 66.45  ? 344 ASP   A OD2 1 
ATOM   2643 N N   . VAL   A 1 356 ? 23.749  53.026 52.047  1.00 57.31  ? 345 VAL   A N   1 
ATOM   2644 C CA  . VAL   A 1 356 ? 23.502  51.709 51.462  1.00 58.06  ? 345 VAL   A CA  1 
ATOM   2645 C C   . VAL   A 1 356 ? 23.994  51.610 50.023  1.00 59.42  ? 345 VAL   A C   1 
ATOM   2646 O O   . VAL   A 1 356 ? 24.379  50.534 49.595  1.00 59.41  ? 345 VAL   A O   1 
ATOM   2647 C CB  . VAL   A 1 356 ? 22.028  51.255 51.602  1.00 58.33  ? 345 VAL   A CB  1 
ATOM   2648 C CG1 . VAL   A 1 356 ? 21.579  51.298 53.053  1.00 58.85  ? 345 VAL   A CG1 1 
ATOM   2649 C CG2 . VAL   A 1 356 ? 21.103  52.089 50.733  1.00 58.52  ? 345 VAL   A CG2 1 
ATOM   2650 N N   . PHE   A 1 357 ? 24.043  52.729 49.299  1.00 60.68  ? 346 PHE   A N   1 
ATOM   2651 C CA  . PHE   A 1 357 ? 24.519  52.736 47.920  1.00 62.56  ? 346 PHE   A CA  1 
ATOM   2652 C C   . PHE   A 1 357 ? 26.055  52.748 47.800  1.00 65.09  ? 346 PHE   A C   1 
ATOM   2653 O O   . PHE   A 1 357 ? 26.580  52.423 46.737  1.00 65.03  ? 346 PHE   A O   1 
ATOM   2654 C CB  . PHE   A 1 357 ? 23.880  53.890 47.144  1.00 62.19  ? 346 PHE   A CB  1 
ATOM   2655 C CG  . PHE   A 1 357 ? 22.372  53.891 47.246  1.00 62.64  ? 346 PHE   A CG  1 
ATOM   2656 C CD1 . PHE   A 1 357 ? 21.631  52.796 46.832  1.00 63.26  ? 346 PHE   A CD1 1 
ATOM   2657 C CD2 . PHE   A 1 357 ? 21.699  54.972 47.783  1.00 63.27  ? 346 PHE   A CD2 1 
ATOM   2658 C CE1 . PHE   A 1 357 ? 20.245  52.792 46.936  1.00 63.60  ? 346 PHE   A CE1 1 
ATOM   2659 C CE2 . PHE   A 1 357 ? 20.312  54.966 47.881  1.00 63.77  ? 346 PHE   A CE2 1 
ATOM   2660 C CZ  . PHE   A 1 357 ? 19.596  53.874 47.458  1.00 63.35  ? 346 PHE   A CZ  1 
ATOM   2661 N N   . ALA   A 1 358 ? 26.757  53.107 48.899  1.00 66.98  ? 347 ALA   A N   1 
ATOM   2662 C CA  . ALA   A 1 358 ? 28.204  53.190 49.047  1.00 69.17  ? 347 ALA   A CA  1 
ATOM   2663 C C   . ALA   A 1 358 ? 28.930  53.827 47.852  1.00 72.02  ? 347 ALA   A C   1 
ATOM   2664 O O   . ALA   A 1 358 ? 29.663  53.135 47.130  1.00 72.28  ? 347 ALA   A O   1 
ATOM   2665 C CB  . ALA   A 1 358 ? 28.775  51.826 49.364  1.00 69.22  ? 347 ALA   A CB  1 
ATOM   2666 N N   . GLY   A 1 359 ? 28.689  55.130 47.638  1.00 73.67  ? 348 GLY   A N   1 
ATOM   2667 C CA  . GLY   A 1 359 ? 29.308  55.906 46.565  1.00 75.68  ? 348 GLY   A CA  1 
ATOM   2668 C C   . GLY   A 1 359 ? 28.751  55.678 45.168  1.00 77.91  ? 348 GLY   A C   1 
ATOM   2669 O O   . GLY   A 1 359 ? 28.617  56.634 44.392  1.00 78.17  ? 348 GLY   A O   1 
ATOM   2670 N N   . CYS   A 1 360 ? 28.454  54.396 44.832  1.00 79.20  ? 349 CYS   A N   1 
ATOM   2671 C CA  . CYS   A 1 360 ? 27.933  53.892 43.549  1.00 80.70  ? 349 CYS   A CA  1 
ATOM   2672 C C   . CYS   A 1 360 ? 26.760  54.719 43.025  1.00 81.88  ? 349 CYS   A C   1 
ATOM   2673 O O   . CYS   A 1 360 ? 25.845  55.029 43.787  1.00 82.16  ? 349 CYS   A O   1 
ATOM   2674 C CB  . CYS   A 1 360 ? 27.558  52.414 43.656  1.00 81.56  ? 349 CYS   A CB  1 
ATOM   2675 S SG  . CYS   A 1 360 ? 28.618  51.442 44.765  1.00 85.15  ? 349 CYS   A SG  1 
ATOM   2676 N N   . GLN   A 1 361 ? 26.783  55.074 41.731  1.00 82.29  ? 350 GLN   A N   1 
ATOM   2677 C CA  . GLN   A 1 361 ? 25.719  55.871 41.112  1.00 83.07  ? 350 GLN   A CA  1 
ATOM   2678 C C   . GLN   A 1 361 ? 24.390  55.121 41.195  1.00 82.52  ? 350 GLN   A C   1 
ATOM   2679 O O   . GLN   A 1 361 ? 24.246  54.092 40.532  1.00 82.95  ? 350 GLN   A O   1 
ATOM   2680 C CB  . GLN   A 1 361 ? 26.039  56.165 39.629  1.00 85.94  ? 350 GLN   A CB  1 
ATOM   2681 C CG  . GLN   A 1 361 ? 27.472  56.640 39.365  1.00 91.35  ? 350 GLN   A CG  1 
ATOM   2682 C CD  . GLN   A 1 361 ? 27.771  56.785 37.884  1.00 97.37  ? 350 GLN   A CD  1 
ATOM   2683 O OE1 . GLN   A 1 361 ? 26.886  57.076 37.066  1.00 99.21  ? 350 GLN   A OE1 1 
ATOM   2684 N NE2 . GLN   A 1 361 ? 29.034  56.596 37.506  1.00 98.28  ? 350 GLN   A NE2 1 
ATOM   2685 N N   . ILE   A 1 362 ? 23.434  55.622 42.028  1.00 81.16  ? 351 ILE   A N   1 
ATOM   2686 C CA  . ILE   A 1 362 ? 22.086  55.062 42.245  1.00 79.88  ? 351 ILE   A CA  1 
ATOM   2687 C C   . ILE   A 1 362 ? 21.411  54.779 40.905  1.00 78.65  ? 351 ILE   A C   1 
ATOM   2688 O O   . ILE   A 1 362 ? 21.099  55.722 40.175  1.00 79.23  ? 351 ILE   A O   1 
ATOM   2689 C CB  . ILE   A 1 362 ? 21.233  56.064 43.066  1.00 80.06  ? 351 ILE   A CB  1 
ATOM   2690 C CG1 . ILE   A 1 362 ? 21.896  56.405 44.402  1.00 80.89  ? 351 ILE   A CG1 1 
ATOM   2691 C CG2 . ILE   A 1 362 ? 19.811  55.568 43.258  1.00 80.43  ? 351 ILE   A CG2 1 
ATOM   2692 C CD1 . ILE   A 1 362 ? 21.292  57.606 45.086  1.00 82.03  ? 351 ILE   A CD1 1 
ATOM   2693 N N   . PRO   A 1 363 ? 21.259  53.500 40.516  1.00 76.84  ? 352 PRO   A N   1 
ATOM   2694 C CA  . PRO   A 1 363 ? 20.647  53.214 39.206  1.00 75.58  ? 352 PRO   A CA  1 
ATOM   2695 C C   . PRO   A 1 363 ? 19.134  53.425 39.150  1.00 73.97  ? 352 PRO   A C   1 
ATOM   2696 O O   . PRO   A 1 363 ? 18.571  53.631 38.079  1.00 74.13  ? 352 PRO   A O   1 
ATOM   2697 C CB  . PRO   A 1 363 ? 21.040  51.758 38.938  1.00 76.54  ? 352 PRO   A CB  1 
ATOM   2698 C CG  . PRO   A 1 363 ? 21.299  51.160 40.284  1.00 77.20  ? 352 PRO   A CG  1 
ATOM   2699 C CD  . PRO   A 1 363 ? 21.611  52.267 41.255  1.00 76.05  ? 352 PRO   A CD  1 
ATOM   2700 N N   . TYR   A 1 364 ? 18.492  53.389 40.313  1.00 72.58  ? 353 TYR   A N   1 
ATOM   2701 C CA  . TYR   A 1 364 ? 17.053  53.516 40.515  1.00 71.79  ? 353 TYR   A CA  1 
ATOM   2702 C C   . TYR   A 1 364 ? 16.505  54.844 40.040  1.00 71.77  ? 353 TYR   A C   1 
ATOM   2703 O O   . TYR   A 1 364 ? 17.017  55.897 40.417  1.00 71.91  ? 353 TYR   A O   1 
ATOM   2704 C CB  . TYR   A 1 364 ? 16.706  53.301 42.008  1.00 70.98  ? 353 TYR   A CB  1 
ATOM   2705 C CG  . TYR   A 1 364 ? 17.378  52.085 42.603  1.00 70.55  ? 353 TYR   A CG  1 
ATOM   2706 C CD1 . TYR   A 1 364 ? 17.025  50.809 42.201  1.00 70.94  ? 353 TYR   A CD1 1 
ATOM   2707 C CD2 . TYR   A 1 364 ? 18.439  52.217 43.483  1.00 70.96  ? 353 TYR   A CD2 1 
ATOM   2708 C CE1 . TYR   A 1 364 ? 17.673  49.690 42.700  1.00 71.59  ? 353 TYR   A CE1 1 
ATOM   2709 C CE2 . TYR   A 1 364 ? 19.101  51.106 43.983  1.00 71.60  ? 353 TYR   A CE2 1 
ATOM   2710 C CZ  . TYR   A 1 364 ? 18.712  49.842 43.590  1.00 72.37  ? 353 TYR   A CZ  1 
ATOM   2711 O OH  . TYR   A 1 364 ? 19.347  48.732 44.084  1.00 73.88  ? 353 TYR   A OH  1 
ATOM   2712 N N   . PRO   A 1 365 ? 15.447  54.821 39.221  1.00 71.67  ? 354 PRO   A N   1 
ATOM   2713 C CA  . PRO   A 1 365 ? 14.848  56.086 38.781  1.00 72.10  ? 354 PRO   A CA  1 
ATOM   2714 C C   . PRO   A 1 365 ? 14.109  56.786 39.923  1.00 72.90  ? 354 PRO   A C   1 
ATOM   2715 O O   . PRO   A 1 365 ? 13.660  56.137 40.875  1.00 73.07  ? 354 PRO   A O   1 
ATOM   2716 C CB  . PRO   A 1 365 ? 13.883  55.653 37.673  1.00 72.61  ? 354 PRO   A CB  1 
ATOM   2717 C CG  . PRO   A 1 365 ? 13.508  54.260 38.026  1.00 72.79  ? 354 PRO   A CG  1 
ATOM   2718 C CD  . PRO   A 1 365 ? 14.715  53.655 38.695  1.00 71.12  ? 354 PRO   A CD  1 
ATOM   2719 N N   . LYS   A 1 366 ? 13.980  58.108 39.829  1.00 73.07  ? 355 LYS   A N   1 
ATOM   2720 C CA  . LYS   A 1 366 ? 13.264  58.872 40.837  1.00 74.08  ? 355 LYS   A CA  1 
ATOM   2721 C C   . LYS   A 1 366 ? 11.775  58.466 40.860  1.00 75.13  ? 355 LYS   A C   1 
ATOM   2722 O O   . LYS   A 1 366 ? 11.269  57.918 39.873  1.00 75.27  ? 355 LYS   A O   1 
ATOM   2723 C CB  . LYS   A 1 366 ? 13.451  60.366 40.580  1.00 75.87  ? 355 LYS   A CB  1 
ATOM   2724 C CG  . LYS   A 1 366 ? 14.913  60.782 40.628  1.00 80.09  ? 355 LYS   A CG  1 
ATOM   2725 C CD  . LYS   A 1 366 ? 15.110  62.229 40.200  1.00 85.10  ? 355 LYS   A CD  1 
ATOM   2726 C CE  . LYS   A 1 366 ? 16.563  62.643 40.259  1.00 89.46  ? 355 LYS   A CE  1 
ATOM   2727 N NZ  . LYS   A 1 366 ? 16.770  64.024 39.738  1.00 92.19  ? 355 LYS   A NZ  1 
ATOM   2728 N N   . ARG   A 1 367 ? 11.091  58.676 42.001  1.00 75.65  ? 356 ARG   A N   1 
ATOM   2729 C CA  . ARG   A 1 367 ? 9.687   58.272 42.167  1.00 76.39  ? 356 ARG   A CA  1 
ATOM   2730 C C   . ARG   A 1 367 ? 8.688   58.977 41.214  1.00 77.98  ? 356 ARG   A C   1 
ATOM   2731 O O   . ARG   A 1 367 ? 8.650   60.208 41.136  1.00 78.07  ? 356 ARG   A O   1 
ATOM   2732 C CB  . ARG   A 1 367 ? 9.248   58.431 43.625  1.00 76.40  ? 356 ARG   A CB  1 
ATOM   2733 C CG  . ARG   A 1 367 ? 8.135   57.476 44.010  1.00 77.05  ? 356 ARG   A CG  1 
ATOM   2734 C CD  . ARG   A 1 367 ? 7.694   57.647 45.451  1.00 77.47  ? 356 ARG   A CD  1 
ATOM   2735 N NE  . ARG   A 1 367 ? 8.505   56.885 46.406  1.00 76.71  ? 356 ARG   A NE  1 
ATOM   2736 C CZ  . ARG   A 1 367 ? 9.450   57.412 47.178  1.00 76.46  ? 356 ARG   A CZ  1 
ATOM   2737 N NH1 . ARG   A 1 367 ? 9.724   58.709 47.113  1.00 76.38  ? 356 ARG   A NH1 1 
ATOM   2738 N NH2 . ARG   A 1 367 ? 10.117  56.652 48.030  1.00 74.65  ? 356 ARG   A NH2 1 
ATOM   2739 N N   . GLU   A 1 368 ? 7.881   58.179 40.495  1.00 78.97  ? 357 GLU   A N   1 
ATOM   2740 C CA  . GLU   A 1 368 ? 6.897   58.684 39.539  1.00 80.48  ? 357 GLU   A CA  1 
ATOM   2741 C C   . GLU   A 1 368 ? 5.603   59.119 40.238  1.00 81.19  ? 357 GLU   A C   1 
ATOM   2742 O O   . GLU   A 1 368 ? 5.202   58.511 41.228  1.00 81.38  ? 357 GLU   A O   1 
ATOM   2743 C CB  . GLU   A 1 368 ? 6.605   57.626 38.464  1.00 83.89  ? 357 GLU   A CB  1 
ATOM   2744 C CG  . GLU   A 1 368 ? 6.057   58.206 37.170  1.00 90.68  ? 357 GLU   A CG  1 
ATOM   2745 C CD  . GLU   A 1 368 ? 5.555   57.189 36.161  1.00 99.10  ? 357 GLU   A CD  1 
ATOM   2746 O OE1 . GLU   A 1 368 ? 5.755   55.971 36.381  1.00 100.08 ? 357 GLU   A OE1 1 
ATOM   2747 O OE2 . GLU   A 1 368 ? 4.957   57.617 35.146  1.00 102.13 ? 357 GLU   A OE2 1 
ATOM   2748 N N   . PHE   A 1 369 ? 4.948   60.167 39.719  1.00 81.40  ? 358 PHE   A N   1 
ATOM   2749 C CA  . PHE   A 1 369 ? 3.730   60.730 40.305  1.00 82.00  ? 358 PHE   A CA  1 
ATOM   2750 C C   . PHE   A 1 369 ? 2.445   59.897 40.025  1.00 83.39  ? 358 PHE   A C   1 
ATOM   2751 O O   . PHE   A 1 369 ? 2.496   58.913 39.292  1.00 83.76  ? 358 PHE   A O   1 
ATOM   2752 C CB  . PHE   A 1 369 ? 3.575   62.199 39.865  1.00 81.27  ? 358 PHE   A CB  1 
ATOM   2753 C CG  . PHE   A 1 369 ? 4.775   63.032 40.240  1.00 81.31  ? 358 PHE   A CG  1 
ATOM   2754 C CD1 . PHE   A 1 369 ? 5.089   63.266 41.564  1.00 81.91  ? 358 PHE   A CD1 1 
ATOM   2755 C CD2 . PHE   A 1 369 ? 5.626   63.523 39.272  1.00 81.79  ? 358 PHE   A CD2 1 
ATOM   2756 C CE1 . PHE   A 1 369 ? 6.201   64.022 41.910  1.00 82.31  ? 358 PHE   A CE1 1 
ATOM   2757 C CE2 . PHE   A 1 369 ? 6.753   64.254 39.622  1.00 82.27  ? 358 PHE   A CE2 1 
ATOM   2758 C CZ  . PHE   A 1 369 ? 7.024   64.511 40.936  1.00 81.98  ? 358 PHE   A CZ  1 
ATOM   2759 N N   . LEU   A 1 370 ? 1.313   60.274 40.664  1.00 83.95  ? 359 LEU   A N   1 
ATOM   2760 C CA  . LEU   A 1 370 ? -0.010  59.641 40.558  1.00 84.87  ? 359 LEU   A CA  1 
ATOM   2761 C C   . LEU   A 1 370 ? -1.092  60.681 40.135  1.00 86.29  ? 359 LEU   A C   1 
ATOM   2762 O O   . LEU   A 1 370 ? -0.817  61.888 40.115  1.00 86.26  ? 359 LEU   A O   1 
ATOM   2763 C CB  . LEU   A 1 370 ? -0.410  59.040 41.922  1.00 84.62  ? 359 LEU   A CB  1 
ATOM   2764 C CG  . LEU   A 1 370 ? 0.605   58.199 42.660  1.00 85.45  ? 359 LEU   A CG  1 
ATOM   2765 C CD1 . LEU   A 1 370 ? 0.065   57.788 43.996  1.00 85.82  ? 359 LEU   A CD1 1 
ATOM   2766 C CD2 . LEU   A 1 370 ? 0.984   56.986 41.865  1.00 86.03  ? 359 LEU   A CD2 1 
ATOM   2767 N N   . THR   A 1 371 ? -2.327  60.217 39.818  1.00 87.33  ? 360 THR   A N   1 
ATOM   2768 C CA  . THR   A 1 371 ? -3.439  61.109 39.457  1.00 88.82  ? 360 THR   A CA  1 
ATOM   2769 C C   . THR   A 1 371 ? -4.698  60.731 40.273  1.00 89.76  ? 360 THR   A C   1 
ATOM   2770 O O   . THR   A 1 371 ? -5.137  59.577 40.253  1.00 89.75  ? 360 THR   A O   1 
ATOM   2771 C CB  . THR   A 1 371 ? -3.632  61.193 37.915  1.00 90.41  ? 360 THR   A CB  1 
ATOM   2772 O OG1 . THR   A 1 371 ? -3.054  62.419 37.442  1.00 91.53  ? 360 THR   A OG1 1 
ATOM   2773 C CG2 . THR   A 1 371 ? -5.098  61.135 37.469  1.00 90.83  ? 360 THR   A CG2 1 
ATOM   2774 N N   . GLU   A 1 372 ? -5.250  61.707 41.015  1.00 90.34  ? 361 GLU   A N   1 
ATOM   2775 C CA  . GLU   A 1 372 ? -6.425  61.475 41.851  1.00 91.42  ? 361 GLU   A CA  1 
ATOM   2776 C C   . GLU   A 1 372 ? -7.618  62.306 41.387  1.00 91.85  ? 361 GLU   A C   1 
ATOM   2777 O O   . GLU   A 1 372 ? -8.744  61.810 41.371  1.00 92.06  ? 361 GLU   A O   1 
ATOM   2778 C CB  . GLU   A 1 372 ? -6.110  61.760 43.333  1.00 94.10  ? 361 GLU   A CB  1 
ATOM   2779 C CG  . GLU   A 1 372 ? -7.150  61.219 44.306  1.00 99.27  ? 361 GLU   A CG  1 
ATOM   2780 C CD  . GLU   A 1 372 ? -6.963  59.779 44.752  1.00 105.42 ? 361 GLU   A CD  1 
ATOM   2781 O OE1 . GLU   A 1 372 ? -5.933  59.167 44.385  1.00 106.45 ? 361 GLU   A OE1 1 
ATOM   2782 O OE2 . GLU   A 1 372 ? -7.844  59.265 45.479  1.00 107.40 ? 361 GLU   A OE2 1 
ATOM   2783 N N   . ALA   B 2 30  ? 5.139   52.641 75.823  1.00 58.73  ? 0   ALA   B N   1 
ATOM   2784 C CA  . ALA   B 2 30  ? 5.530   53.504 74.701  1.00 59.45  ? 0   ALA   B CA  1 
ATOM   2785 C C   . ALA   B 2 30  ? 6.139   54.807 75.214  1.00 59.85  ? 0   ALA   B C   1 
ATOM   2786 O O   . ALA   B 2 30  ? 5.461   55.581 75.882  1.00 60.03  ? 0   ALA   B O   1 
ATOM   2787 C CB  . ALA   B 2 30  ? 4.338   53.789 73.798  1.00 59.45  ? 0   ALA   B CB  1 
ATOM   2788 N N   . MET   B 2 31  ? 7.428   55.034 74.892  1.00 59.90  ? 1   MET   B N   1 
ATOM   2789 C CA  . MET   B 2 31  ? 8.294   56.135 75.316  1.00 60.47  ? 1   MET   B CA  1 
ATOM   2790 C C   . MET   B 2 31  ? 8.353   56.075 76.823  1.00 60.78  ? 1   MET   B C   1 
ATOM   2791 O O   . MET   B 2 31  ? 7.707   56.877 77.480  1.00 61.41  ? 1   MET   B O   1 
ATOM   2792 C CB  . MET   B 2 31  ? 7.798   57.517 74.815  1.00 61.06  ? 1   MET   B CB  1 
ATOM   2793 C CG  . MET   B 2 31  ? 7.364   57.558 73.358  1.00 62.55  ? 1   MET   B CG  1 
ATOM   2794 S SD  . MET   B 2 31  ? 8.533   56.829 72.189  1.00 65.86  ? 1   MET   B SD  1 
ATOM   2795 C CE  . MET   B 2 31  ? 9.968   57.810 72.481  1.00 64.97  ? 1   MET   B CE  1 
ATOM   2796 N N   . ALA   B 2 32  ? 8.986   55.038 77.364  1.00 60.32  ? 2   ALA   B N   1 
ATOM   2797 C CA  . ALA   B 2 32  ? 8.985   54.836 78.801  1.00 60.65  ? 2   ALA   B CA  1 
ATOM   2798 C C   . ALA   B 2 32  ? 10.177  55.499 79.518  1.00 60.46  ? 2   ALA   B C   1 
ATOM   2799 O O   . ALA   B 2 32  ? 9.953   56.374 80.360  1.00 61.26  ? 2   ALA   B O   1 
ATOM   2800 C CB  . ALA   B 2 32  ? 8.862   53.349 79.132  1.00 61.32  ? 2   ALA   B CB  1 
ATOM   2801 N N   . GLY   B 2 33  ? 11.411  55.135 79.172  1.00 59.23  ? 3   GLY   B N   1 
ATOM   2802 C CA  . GLY   B 2 33  ? 12.578  55.740 79.798  1.00 58.47  ? 3   GLY   B CA  1 
ATOM   2803 C C   . GLY   B 2 33  ? 13.127  56.895 78.991  1.00 57.64  ? 3   GLY   B C   1 
ATOM   2804 O O   . GLY   B 2 33  ? 14.304  57.226 79.123  1.00 57.96  ? 3   GLY   B O   1 
ATOM   2805 N N   . ASN   B 2 34  ? 12.280  57.531 78.154  1.00 56.46  ? 4   ASN   B N   1 
ATOM   2806 C CA  . ASN   B 2 34  ? 12.700  58.628 77.291  1.00 55.66  ? 4   ASN   B CA  1 
ATOM   2807 C C   . ASN   B 2 34  ? 12.493  60.013 77.917  1.00 54.75  ? 4   ASN   B C   1 
ATOM   2808 O O   . ASN   B 2 34  ? 12.568  61.007 77.192  1.00 54.97  ? 4   ASN   B O   1 
ATOM   2809 C CB  . ASN   B 2 34  ? 11.940  58.545 75.969  1.00 56.46  ? 4   ASN   B CB  1 
ATOM   2810 C CG  . ASN   B 2 34  ? 12.637  59.240 74.835  1.00 59.75  ? 4   ASN   B CG  1 
ATOM   2811 O OD1 . ASN   B 2 34  ? 13.849  59.115 74.652  1.00 61.23  ? 4   ASN   B OD1 1 
ATOM   2812 N ND2 . ASN   B 2 34  ? 11.893  60.009 74.061  1.00 60.42  ? 4   ASN   B ND2 1 
ATOM   2813 N N   . PHE   B 2 35  ? 12.262  60.105 79.244  1.00 53.52  ? 5   PHE   B N   1 
ATOM   2814 C CA  . PHE   B 2 35  ? 11.965  61.399 79.853  1.00 53.16  ? 5   PHE   B CA  1 
ATOM   2815 C C   . PHE   B 2 35  ? 12.967  62.509 79.539  1.00 53.26  ? 5   PHE   B C   1 
ATOM   2816 O O   . PHE   B 2 35  ? 12.536  63.563 79.077  1.00 53.99  ? 5   PHE   B O   1 
ATOM   2817 C CB  . PHE   B 2 35  ? 11.725  61.330 81.364  1.00 52.62  ? 5   PHE   B CB  1 
ATOM   2818 C CG  . PHE   B 2 35  ? 11.253  62.667 81.894  1.00 52.59  ? 5   PHE   B CG  1 
ATOM   2819 C CD1 . PHE   B 2 35  ? 10.000  63.154 81.571  1.00 52.88  ? 5   PHE   B CD1 1 
ATOM   2820 C CD2 . PHE   B 2 35  ? 12.094  63.468 82.649  1.00 53.06  ? 5   PHE   B CD2 1 
ATOM   2821 C CE1 . PHE   B 2 35  ? 9.577   64.389 82.038  1.00 53.31  ? 5   PHE   B CE1 1 
ATOM   2822 C CE2 . PHE   B 2 35  ? 11.664  64.699 83.120  1.00 53.46  ? 5   PHE   B CE2 1 
ATOM   2823 C CZ  . PHE   B 2 35  ? 10.411  65.154 82.804  1.00 53.12  ? 5   PHE   B CZ  1 
ATOM   2824 N N   . TRP   B 2 36  ? 14.270  62.289 79.742  1.00 52.32  ? 6   TRP   B N   1 
ATOM   2825 C CA  . TRP   B 2 36  ? 15.260  63.350 79.520  1.00 51.83  ? 6   TRP   B CA  1 
ATOM   2826 C C   . TRP   B 2 36  ? 15.431  63.772 78.034  1.00 50.49  ? 6   TRP   B C   1 
ATOM   2827 O O   . TRP   B 2 36  ? 16.071  64.785 77.749  1.00 50.71  ? 6   TRP   B O   1 
ATOM   2828 C CB  . TRP   B 2 36  ? 16.597  62.992 80.174  1.00 52.04  ? 6   TRP   B CB  1 
ATOM   2829 C CG  . TRP   B 2 36  ? 16.448  62.541 81.601  1.00 52.78  ? 6   TRP   B CG  1 
ATOM   2830 C CD1 . TRP   B 2 36  ? 16.606  61.275 82.080  1.00 53.79  ? 6   TRP   B CD1 1 
ATOM   2831 C CD2 . TRP   B 2 36  ? 16.005  63.337 82.710  1.00 52.86  ? 6   TRP   B CD2 1 
ATOM   2832 N NE1 . TRP   B 2 36  ? 16.337  61.243 83.429  1.00 54.08  ? 6   TRP   B NE1 1 
ATOM   2833 C CE2 . TRP   B 2 36  ? 15.968  62.498 83.839  1.00 53.64  ? 6   TRP   B CE2 1 
ATOM   2834 C CE3 . TRP   B 2 36  ? 15.661  64.683 82.863  1.00 53.42  ? 6   TRP   B CE3 1 
ATOM   2835 C CZ2 . TRP   B 2 36  ? 15.616  62.967 85.099  1.00 54.13  ? 6   TRP   B CZ2 1 
ATOM   2836 C CZ3 . TRP   B 2 36  ? 15.297  65.138 84.110  1.00 54.08  ? 6   TRP   B CZ3 1 
ATOM   2837 C CH2 . TRP   B 2 36  ? 15.286  64.288 85.211  1.00 54.13  ? 6   TRP   B CH2 1 
ATOM   2838 N N   A GLN   B 2 37  ? 14.844  63.015 77.103  0.49 49.65  ? 7   GLN   B N   1 
ATOM   2839 N N   B GLN   B 2 37  ? 14.840  63.015 77.106  0.51 49.55  ? 7   GLN   B N   1 
ATOM   2840 C CA  A GLN   B 2 37  ? 14.890  63.372 75.685  0.49 49.36  ? 7   GLN   B CA  1 
ATOM   2841 C CA  B GLN   B 2 37  ? 14.880  63.351 75.684  0.51 49.14  ? 7   GLN   B CA  1 
ATOM   2842 C C   A GLN   B 2 37  ? 13.472  63.600 75.100  0.49 48.52  ? 7   GLN   B C   1 
ATOM   2843 C C   B GLN   B 2 37  ? 13.469  63.607 75.103  0.51 48.43  ? 7   GLN   B C   1 
ATOM   2844 O O   A GLN   B 2 37  ? 13.322  63.652 73.878  0.49 48.64  ? 7   GLN   B O   1 
ATOM   2845 O O   B GLN   B 2 37  ? 13.320  63.675 73.882  0.51 48.55  ? 7   GLN   B O   1 
ATOM   2846 C CB  A GLN   B 2 37  ? 15.653  62.301 74.880  0.49 51.09  ? 7   GLN   B CB  1 
ATOM   2847 C CB  B GLN   B 2 37  ? 15.569  62.224 74.897  0.51 50.52  ? 7   GLN   B CB  1 
ATOM   2848 C CG  A GLN   B 2 37  ? 16.994  61.887 75.492  0.49 54.40  ? 7   GLN   B CG  1 
ATOM   2849 C CG  B GLN   B 2 37  ? 16.949  61.858 75.424  0.51 53.09  ? 7   GLN   B CG  1 
ATOM   2850 C CD  A GLN   B 2 37  ? 18.179  62.606 74.890  0.49 58.72  ? 7   GLN   B CD  1 
ATOM   2851 C CD  B GLN   B 2 37  ? 17.041  60.395 75.765  0.51 56.41  ? 7   GLN   B CD  1 
ATOM   2852 O OE1 A GLN   B 2 37  ? 18.464  63.772 75.192  0.49 59.31  ? 7   GLN   B OE1 1 
ATOM   2853 O OE1 B GLN   B 2 37  ? 16.452  59.919 76.746  0.51 57.26  ? 7   GLN   B OE1 1 
ATOM   2854 N NE2 A GLN   B 2 37  ? 18.913  61.906 74.034  0.49 60.02  ? 7   GLN   B NE2 1 
ATOM   2855 N NE2 B GLN   B 2 37  ? 17.784  59.647 74.958  0.51 56.96  ? 7   GLN   B NE2 1 
ATOM   2856 N N   . SER   B 2 38  ? 12.439  63.725 75.968  1.00 47.50  ? 8   SER   B N   1 
ATOM   2857 C CA  . SER   B 2 38  ? 11.035  63.898 75.580  1.00 45.90  ? 8   SER   B CA  1 
ATOM   2858 C C   . SER   B 2 38  ? 10.609  65.333 75.386  1.00 45.33  ? 8   SER   B C   1 
ATOM   2859 O O   . SER   B 2 38  ? 11.214  66.224 75.971  1.00 45.76  ? 8   SER   B O   1 
ATOM   2860 C CB  . SER   B 2 38  ? 10.137  63.277 76.645  1.00 45.30  ? 8   SER   B CB  1 
ATOM   2861 O OG  . SER   B 2 38  ? 10.315  63.915 77.897  1.00 45.26  ? 8   SER   B OG  1 
ATOM   2862 N N   . SER   B 2 39  ? 9.523   65.569 74.617  1.00 44.39  ? 9   SER   B N   1 
ATOM   2863 C CA  . SER   B 2 39  ? 8.976   66.922 74.461  1.00 44.14  ? 9   SER   B CA  1 
ATOM   2864 C C   . SER   B 2 39  ? 8.509   67.462 75.822  1.00 44.34  ? 9   SER   B C   1 
ATOM   2865 O O   . SER   B 2 39  ? 8.641   68.649 76.082  1.00 44.82  ? 9   SER   B O   1 
ATOM   2866 C CB  . SER   B 2 39  ? 7.826   66.946 73.459  1.00 44.67  ? 9   SER   B CB  1 
ATOM   2867 O OG  . SER   B 2 39  ? 6.582   66.600 74.043  1.00 46.34  ? 9   SER   B OG  1 
ATOM   2868 N N   . HIS   B 2 40  ? 7.973   66.574 76.689  1.00 43.94  ? 10  HIS   B N   1 
ATOM   2869 C CA  . HIS   B 2 40  ? 7.530   66.855 78.049  1.00 43.78  ? 10  HIS   B CA  1 
ATOM   2870 C C   . HIS   B 2 40  ? 8.652   67.555 78.826  1.00 45.22  ? 10  HIS   B C   1 
ATOM   2871 O O   . HIS   B 2 40  ? 8.426   68.634 79.353  1.00 45.78  ? 10  HIS   B O   1 
ATOM   2872 C CB  . HIS   B 2 40  ? 7.126   65.527 78.738  1.00 42.77  ? 10  HIS   B CB  1 
ATOM   2873 C CG  . HIS   B 2 40  ? 6.536   65.668 80.113  1.00 41.60  ? 10  HIS   B CG  1 
ATOM   2874 N ND1 . HIS   B 2 40  ? 5.550   64.819 80.555  1.00 42.24  ? 10  HIS   B ND1 1 
ATOM   2875 C CD2 . HIS   B 2 40  ? 6.825   66.543 81.103  1.00 41.99  ? 10  HIS   B CD2 1 
ATOM   2876 C CE1 . HIS   B 2 40  ? 5.262   65.210 81.782  1.00 42.35  ? 10  HIS   B CE1 1 
ATOM   2877 N NE2 . HIS   B 2 40  ? 6.007   66.238 82.154  1.00 42.52  ? 10  HIS   B NE2 1 
ATOM   2878 N N   . TYR   B 2 41  ? 9.858   66.988 78.846  1.00 45.72  ? 11  TYR   B N   1 
ATOM   2879 C CA  . TYR   B 2 41  ? 10.972  67.581 79.574  1.00 46.99  ? 11  TYR   B CA  1 
ATOM   2880 C C   . TYR   B 2 41  ? 11.540  68.811 78.879  1.00 47.90  ? 11  TYR   B C   1 
ATOM   2881 O O   . TYR   B 2 41  ? 11.773  69.828 79.527  1.00 48.10  ? 11  TYR   B O   1 
ATOM   2882 C CB  . TYR   B 2 41  ? 12.073  66.533 79.771  1.00 47.62  ? 11  TYR   B CB  1 
ATOM   2883 C CG  . TYR   B 2 41  ? 13.321  67.058 80.437  1.00 49.21  ? 11  TYR   B CG  1 
ATOM   2884 C CD1 . TYR   B 2 41  ? 13.278  67.590 81.718  1.00 50.53  ? 11  TYR   B CD1 1 
ATOM   2885 C CD2 . TYR   B 2 41  ? 14.547  67.017 79.790  1.00 50.37  ? 11  TYR   B CD2 1 
ATOM   2886 C CE1 . TYR   B 2 41  ? 14.421  68.078 82.335  1.00 51.65  ? 11  TYR   B CE1 1 
ATOM   2887 C CE2 . TYR   B 2 41  ? 15.699  67.497 80.399  1.00 51.46  ? 11  TYR   B CE2 1 
ATOM   2888 C CZ  . TYR   B 2 41  ? 15.630  68.029 81.673  1.00 52.77  ? 11  TYR   B CZ  1 
ATOM   2889 O OH  . TYR   B 2 41  ? 16.765  68.492 82.291  1.00 55.01  ? 11  TYR   B OH  1 
ATOM   2890 N N   . LEU   B 2 42  ? 11.787  68.719 77.571  1.00 48.25  ? 12  LEU   B N   1 
ATOM   2891 C CA  . LEU   B 2 42  ? 12.418  69.802 76.830  1.00 48.95  ? 12  LEU   B CA  1 
ATOM   2892 C C   . LEU   B 2 42  ? 11.548  71.043 76.643  1.00 49.35  ? 12  LEU   B C   1 
ATOM   2893 O O   . LEU   B 2 42  ? 12.091  72.140 76.483  1.00 50.18  ? 12  LEU   B O   1 
ATOM   2894 C CB  . LEU   B 2 42  ? 12.936  69.301 75.472  1.00 49.38  ? 12  LEU   B CB  1 
ATOM   2895 C CG  . LEU   B 2 42  ? 13.832  68.055 75.520  1.00 51.07  ? 12  LEU   B CG  1 
ATOM   2896 C CD1 . LEU   B 2 42  ? 14.114  67.524 74.121  1.00 51.74  ? 12  LEU   B CD1 1 
ATOM   2897 C CD2 . LEU   B 2 42  ? 15.103  68.301 76.318  1.00 51.30  ? 12  LEU   B CD2 1 
ATOM   2898 N N   . GLN   B 2 43  ? 10.218  70.896 76.670  1.00 48.63  ? 13  GLN   B N   1 
ATOM   2899 C CA  . GLN   B 2 43  ? 9.329   72.036 76.454  1.00 48.53  ? 13  GLN   B CA  1 
ATOM   2900 C C   . GLN   B 2 43  ? 8.278   72.277 77.531  1.00 48.12  ? 13  GLN   B C   1 
ATOM   2901 O O   . GLN   B 2 43  ? 7.839   73.419 77.688  1.00 48.18  ? 13  GLN   B O   1 
ATOM   2902 C CB  . GLN   B 2 43  ? 8.614   71.906 75.110  1.00 50.08  ? 13  GLN   B CB  1 
ATOM   2903 C CG  . GLN   B 2 43  ? 9.552   71.691 73.944  1.00 54.12  ? 13  GLN   B CG  1 
ATOM   2904 C CD  . GLN   B 2 43  ? 8.818   71.425 72.651  1.00 58.98  ? 13  GLN   B CD  1 
ATOM   2905 O OE1 . GLN   B 2 43  ? 9.277   70.621 71.819  1.00 60.22  ? 13  GLN   B OE1 1 
ATOM   2906 N NE2 . GLN   B 2 43  ? 7.666   72.087 72.446  1.00 58.91  ? 13  GLN   B NE2 1 
ATOM   2907 N N   . TRP   B 2 44  ? 7.843   71.223 78.246  1.00 47.34  ? 14  TRP   B N   1 
ATOM   2908 C CA  . TRP   B 2 44  ? 6.759   71.380 79.201  1.00 46.91  ? 14  TRP   B CA  1 
ATOM   2909 C C   . TRP   B 2 44  ? 7.113   71.223 80.688  1.00 47.55  ? 14  TRP   B C   1 
ATOM   2910 O O   . TRP   B 2 44  ? 6.258   70.836 81.480  1.00 47.71  ? 14  TRP   B O   1 
ATOM   2911 C CB  . TRP   B 2 44  ? 5.619   70.456 78.813  1.00 46.17  ? 14  TRP   B CB  1 
ATOM   2912 C CG  . TRP   B 2 44  ? 4.940   70.924 77.556  1.00 45.48  ? 14  TRP   B CG  1 
ATOM   2913 C CD1 . TRP   B 2 44  ? 5.080   70.406 76.298  1.00 45.90  ? 14  TRP   B CD1 1 
ATOM   2914 C CD2 . TRP   B 2 44  ? 4.084   72.069 77.427  1.00 44.77  ? 14  TRP   B CD2 1 
ATOM   2915 N NE1 . TRP   B 2 44  ? 4.335   71.135 75.401  1.00 45.88  ? 14  TRP   B NE1 1 
ATOM   2916 C CE2 . TRP   B 2 44  ? 3.706   72.160 76.070  1.00 45.49  ? 14  TRP   B CE2 1 
ATOM   2917 C CE3 . TRP   B 2 44  ? 3.622   73.040 78.323  1.00 44.68  ? 14  TRP   B CE3 1 
ATOM   2918 C CZ2 . TRP   B 2 44  ? 2.844   73.153 75.603  1.00 45.76  ? 14  TRP   B CZ2 1 
ATOM   2919 C CZ3 . TRP   B 2 44  ? 2.795   74.037 77.852  1.00 45.43  ? 14  TRP   B CZ3 1 
ATOM   2920 C CH2 . TRP   B 2 44  ? 2.403   74.081 76.511  1.00 45.71  ? 14  TRP   B CH2 1 
ATOM   2921 N N   . ILE   B 2 45  ? 8.349   71.574 81.067  1.00 47.93  ? 15  ILE   B N   1 
ATOM   2922 C CA  . ILE   B 2 45  ? 8.806   71.688 82.453  1.00 48.82  ? 15  ILE   B CA  1 
ATOM   2923 C C   . ILE   B 2 45  ? 9.120   73.184 82.486  1.00 50.08  ? 15  ILE   B C   1 
ATOM   2924 O O   . ILE   B 2 45  ? 10.157  73.634 81.988  1.00 50.43  ? 15  ILE   B O   1 
ATOM   2925 C CB  . ILE   B 2 45  ? 10.034  70.813 82.799  1.00 49.04  ? 15  ILE   B CB  1 
ATOM   2926 C CG1 . ILE   B 2 45  ? 9.710   69.307 82.658  1.00 49.84  ? 15  ILE   B CG1 1 
ATOM   2927 C CG2 . ILE   B 2 45  ? 10.563  71.144 84.202  1.00 49.29  ? 15  ILE   B CG2 1 
ATOM   2928 C CD1 . ILE   B 2 45  ? 8.657   68.803 83.592  1.00 50.93  ? 15  ILE   B CD1 1 
ATOM   2929 N N   . LEU   B 2 46  ? 8.135   73.962 82.914  1.00 50.26  ? 16  LEU   B N   1 
ATOM   2930 C CA  . LEU   B 2 46  ? 8.187   75.409 82.867  1.00 50.67  ? 16  LEU   B CA  1 
ATOM   2931 C C   . LEU   B 2 46  ? 8.873   76.061 84.063  1.00 52.38  ? 16  LEU   B C   1 
ATOM   2932 O O   . LEU   B 2 46  ? 9.027   75.441 85.113  1.00 52.23  ? 16  LEU   B O   1 
ATOM   2933 C CB  . LEU   B 2 46  ? 6.762   75.974 82.687  1.00 49.79  ? 16  LEU   B CB  1 
ATOM   2934 C CG  . LEU   B 2 46  ? 5.823   75.284 81.701  1.00 49.69  ? 16  LEU   B CG  1 
ATOM   2935 C CD1 . LEU   B 2 46  ? 4.500   76.004 81.634  1.00 49.75  ? 16  LEU   B CD1 1 
ATOM   2936 C CD2 . LEU   B 2 46  ? 6.436   75.181 80.331  1.00 49.95  ? 16  LEU   B CD2 1 
ATOM   2937 N N   . ASP   B 2 47  ? 9.289   77.325 83.890  1.00 53.80  ? 17  ASP   B N   1 
ATOM   2938 C CA  . ASP   B 2 47  ? 9.914   78.134 84.938  1.00 55.45  ? 17  ASP   B CA  1 
ATOM   2939 C C   . ASP   B 2 47  ? 8.781   78.760 85.749  1.00 55.96  ? 17  ASP   B C   1 
ATOM   2940 O O   . ASP   B 2 47  ? 7.854   79.331 85.168  1.00 55.72  ? 17  ASP   B O   1 
ATOM   2941 C CB  . ASP   B 2 47  ? 10.787  79.225 84.294  1.00 58.24  ? 17  ASP   B CB  1 
ATOM   2942 C CG  . ASP   B 2 47  ? 11.539  80.116 85.259  1.00 64.48  ? 17  ASP   B CG  1 
ATOM   2943 O OD1 . ASP   B 2 47  ? 10.882  80.809 86.063  1.00 65.28  ? 17  ASP   B OD1 1 
ATOM   2944 O OD2 . ASP   B 2 47  ? 12.786  80.153 85.182  1.00 67.74  ? 17  ASP   B OD2 1 
ATOM   2945 N N   . LYS   B 2 48  ? 8.846   78.655 87.082  1.00 56.60  ? 18  LYS   B N   1 
ATOM   2946 C CA  . LYS   B 2 48  ? 7.785   79.186 87.933  1.00 57.81  ? 18  LYS   B CA  1 
ATOM   2947 C C   . LYS   B 2 48  ? 7.540   80.692 87.716  1.00 59.54  ? 18  LYS   B C   1 
ATOM   2948 O O   . LYS   B 2 48  ? 6.385   81.094 87.594  1.00 60.13  ? 18  LYS   B O   1 
ATOM   2949 C CB  . LYS   B 2 48  ? 8.005   78.849 89.415  1.00 58.74  ? 18  LYS   B CB  1 
ATOM   2950 C CG  . LYS   B 2 48  ? 6.725   78.958 90.233  1.00 62.09  ? 18  LYS   B CG  1 
ATOM   2951 C CD  . LYS   B 2 48  ? 7.028   79.116 91.715  1.00 66.51  ? 18  LYS   B CD  1 
ATOM   2952 C CE  . LYS   B 2 48  ? 5.846   79.622 92.517  1.00 69.85  ? 18  LYS   B CE  1 
ATOM   2953 N NZ  . LYS   B 2 48  ? 5.051   78.523 93.127  1.00 71.72  ? 18  LYS   B NZ  1 
ATOM   2954 N N   . GLN   B 2 49  ? 8.600   81.506 87.582  1.00 59.97  ? 19  GLN   B N   1 
ATOM   2955 C CA  . GLN   B 2 49  ? 8.415   82.937 87.339  1.00 60.73  ? 19  GLN   B CA  1 
ATOM   2956 C C   . GLN   B 2 49  ? 7.790   83.203 85.965  1.00 60.56  ? 19  GLN   B C   1 
ATOM   2957 O O   . GLN   B 2 49  ? 6.933   84.078 85.856  1.00 60.74  ? 19  GLN   B O   1 
ATOM   2958 C CB  . GLN   B 2 49  ? 9.712   83.739 87.584  1.00 62.87  ? 19  GLN   B CB  1 
ATOM   2959 C CG  . GLN   B 2 49  ? 10.146  83.750 89.061  1.00 67.30  ? 19  GLN   B CG  1 
ATOM   2960 C CD  . GLN   B 2 49  ? 9.014   84.099 90.023  1.00 73.38  ? 19  GLN   B CD  1 
ATOM   2961 O OE1 . GLN   B 2 49  ? 8.617   83.287 90.872  1.00 75.50  ? 19  GLN   B OE1 1 
ATOM   2962 N NE2 . GLN   B 2 49  ? 8.438   85.292 89.880  1.00 73.90  ? 19  GLN   B NE2 1 
ATOM   2963 N N   . ASP   B 2 50  ? 8.147   82.399 84.948  1.00 60.00  ? 20  ASP   B N   1 
ATOM   2964 C CA  . ASP   B 2 50  ? 7.553   82.511 83.615  1.00 59.95  ? 20  ASP   B CA  1 
ATOM   2965 C C   . ASP   B 2 50  ? 6.054   82.199 83.696  1.00 58.79  ? 20  ASP   B C   1 
ATOM   2966 O O   . ASP   B 2 50  ? 5.240   82.902 83.097  1.00 58.77  ? 20  ASP   B O   1 
ATOM   2967 C CB  . ASP   B 2 50  ? 8.230   81.539 82.629  1.00 62.78  ? 20  ASP   B CB  1 
ATOM   2968 C CG  . ASP   B 2 50  ? 9.595   81.972 82.125  1.00 69.78  ? 20  ASP   B CG  1 
ATOM   2969 O OD1 . ASP   B 2 50  ? 10.028  83.105 82.463  1.00 71.49  ? 20  ASP   B OD1 1 
ATOM   2970 O OD2 . ASP   B 2 50  ? 10.233  81.184 81.385  1.00 72.35  ? 20  ASP   B OD2 1 
ATOM   2971 N N   . LEU   B 2 51  ? 5.700   81.160 84.464  1.00 57.74  ? 21  LEU   B N   1 
ATOM   2972 C CA  . LEU   B 2 51  ? 4.327   80.705 84.686  1.00 57.28  ? 21  LEU   B CA  1 
ATOM   2973 C C   . LEU   B 2 51  ? 3.465   81.771 85.387  1.00 57.05  ? 21  LEU   B C   1 
ATOM   2974 O O   . LEU   B 2 51  ? 2.351   82.047 84.938  1.00 57.06  ? 21  LEU   B O   1 
ATOM   2975 C CB  . LEU   B 2 51  ? 4.356   79.400 85.500  1.00 56.90  ? 21  LEU   B CB  1 
ATOM   2976 C CG  . LEU   B 2 51  ? 3.048   78.678 85.665  1.00 57.82  ? 21  LEU   B CG  1 
ATOM   2977 C CD1 . LEU   B 2 51  ? 2.531   78.212 84.343  1.00 58.35  ? 21  LEU   B CD1 1 
ATOM   2978 C CD2 . LEU   B 2 51  ? 3.216   77.484 86.571  1.00 58.38  ? 21  LEU   B CD2 1 
ATOM   2979 N N   . LEU   B 2 52  ? 3.998   82.386 86.466  1.00 56.69  ? 22  LEU   B N   1 
ATOM   2980 C CA  . LEU   B 2 52  ? 3.303   83.430 87.236  1.00 56.62  ? 22  LEU   B CA  1 
ATOM   2981 C C   . LEU   B 2 52  ? 3.117   84.688 86.421  1.00 56.05  ? 22  LEU   B C   1 
ATOM   2982 O O   . LEU   B 2 52  ? 2.094   85.352 86.551  1.00 56.18  ? 22  LEU   B O   1 
ATOM   2983 C CB  . LEU   B 2 52  ? 4.050   83.790 88.538  1.00 56.88  ? 22  LEU   B CB  1 
ATOM   2984 C CG  . LEU   B 2 52  ? 4.443   82.649 89.475  1.00 58.40  ? 22  LEU   B CG  1 
ATOM   2985 C CD1 . LEU   B 2 52  ? 5.130   83.175 90.691  1.00 58.89  ? 22  LEU   B CD1 1 
ATOM   2986 C CD2 . LEU   B 2 52  ? 3.257   81.770 89.849  1.00 59.16  ? 22  LEU   B CD2 1 
ATOM   2987 N N   . LYS   B 2 53  ? 4.114   85.028 85.603  1.00 55.38  ? 23  LYS   B N   1 
ATOM   2988 C CA  . LYS   B 2 53  ? 4.102   86.187 84.731  1.00 55.55  ? 23  LYS   B CA  1 
ATOM   2989 C C   . LYS   B 2 53  ? 2.960   86.058 83.731  1.00 55.65  ? 23  LYS   B C   1 
ATOM   2990 O O   . LYS   B 2 53  ? 2.169   86.981 83.600  1.00 55.54  ? 23  LYS   B O   1 
ATOM   2991 C CB  . LYS   B 2 53  ? 5.473   86.305 84.038  1.00 57.74  ? 23  LYS   B CB  1 
ATOM   2992 C CG  . LYS   B 2 53  ? 5.536   87.184 82.796  1.00 62.12  ? 23  LYS   B CG  1 
ATOM   2993 C CD  . LYS   B 2 53  ? 6.980   87.321 82.317  1.00 66.52  ? 23  LYS   B CD  1 
ATOM   2994 C CE  . LYS   B 2 53  ? 7.829   88.178 83.239  1.00 69.77  ? 23  LYS   B CE  1 
ATOM   2995 N NZ  . LYS   B 2 53  ? 8.129   89.508 82.625  1.00 71.35  ? 23  LYS   B NZ  1 
ATOM   2996 N N   . GLU   B 2 54  ? 2.823   84.892 83.080  1.00 56.06  ? 24  GLU   B N   1 
ATOM   2997 C CA  . GLU   B 2 54  ? 1.723   84.661 82.132  1.00 56.76  ? 24  GLU   B CA  1 
ATOM   2998 C C   . GLU   B 2 54  ? 0.351   84.687 82.805  1.00 56.73  ? 24  GLU   B C   1 
ATOM   2999 O O   . GLU   B 2 54  ? -0.635  85.071 82.190  1.00 56.70  ? 24  GLU   B O   1 
ATOM   3000 C CB  . GLU   B 2 54  ? 1.906   83.335 81.368  1.00 59.41  ? 24  GLU   B CB  1 
ATOM   3001 C CG  . GLU   B 2 54  ? 2.631   83.483 80.041  1.00 65.01  ? 24  GLU   B CG  1 
ATOM   3002 C CD  . GLU   B 2 54  ? 2.032   84.516 79.104  1.00 71.81  ? 24  GLU   B CD  1 
ATOM   3003 O OE1 . GLU   B 2 54  ? 0.842   84.369 78.741  1.00 73.39  ? 24  GLU   B OE1 1 
ATOM   3004 O OE2 . GLU   B 2 54  ? 2.747   85.481 78.745  1.00 73.43  ? 24  GLU   B OE2 1 
ATOM   3005 N N   . ARG   B 2 55  ? 0.298   84.281 84.071  1.00 56.67  ? 25  ARG   B N   1 
ATOM   3006 C CA  . ARG   B 2 55  ? -0.912  84.227 84.884  1.00 56.97  ? 25  ARG   B CA  1 
ATOM   3007 C C   . ARG   B 2 55  ? -1.465  85.602 85.222  1.00 56.64  ? 25  ARG   B C   1 
ATOM   3008 O O   . ARG   B 2 55  ? -2.671  85.730 85.432  1.00 56.86  ? 25  ARG   B O   1 
ATOM   3009 C CB  . ARG   B 2 55  ? -0.605  83.449 86.170  1.00 58.64  ? 25  ARG   B CB  1 
ATOM   3010 C CG  . ARG   B 2 55  ? -1.798  83.141 87.056  1.00 61.94  ? 25  ARG   B CG  1 
ATOM   3011 C CD  . ARG   B 2 55  ? -1.426  82.053 88.035  1.00 65.78  ? 25  ARG   B CD  1 
ATOM   3012 N NE  . ARG   B 2 55  ? -1.124  80.802 87.339  1.00 69.42  ? 25  ARG   B NE  1 
ATOM   3013 C CZ  . ARG   B 2 55  ? -0.549  79.748 87.906  1.00 72.27  ? 25  ARG   B CZ  1 
ATOM   3014 N NH1 . ARG   B 2 55  ? -0.191  79.785 89.185  1.00 72.68  ? 25  ARG   B NH1 1 
ATOM   3015 N NH2 . ARG   B 2 55  ? -0.320  78.650 87.197  1.00 71.94  ? 25  ARG   B NH2 1 
ATOM   3016 N N   . GLN   B 2 56  ? -0.600  86.629 85.265  1.00 56.06  ? 26  GLN   B N   1 
ATOM   3017 C CA  . GLN   B 2 56  ? -0.995  87.986 85.605  1.00 56.20  ? 26  GLN   B CA  1 
ATOM   3018 C C   . GLN   B 2 56  ? -2.164  88.528 84.783  1.00 56.43  ? 26  GLN   B C   1 
ATOM   3019 O O   . GLN   B 2 56  ? -2.960  89.283 85.331  1.00 56.66  ? 26  GLN   B O   1 
ATOM   3020 C CB  . GLN   B 2 56  ? 0.201   88.940 85.555  1.00 57.81  ? 26  GLN   B CB  1 
ATOM   3021 C CG  . GLN   B 2 56  ? 1.255   88.691 86.638  1.00 61.63  ? 26  GLN   B CG  1 
ATOM   3022 C CD  . GLN   B 2 56  ? 0.678   88.614 88.038  1.00 66.99  ? 26  GLN   B CD  1 
ATOM   3023 O OE1 . GLN   B 2 56  ? -0.070  89.492 88.492  1.00 68.09  ? 26  GLN   B OE1 1 
ATOM   3024 N NE2 . GLN   B 2 56  ? 1.010   87.545 88.753  1.00 68.56  ? 26  GLN   B NE2 1 
ATOM   3025 N N   . LYS   B 2 57  ? -2.337  88.088 83.519  1.00 56.36  ? 27  LYS   B N   1 
ATOM   3026 C CA  . LYS   B 2 57  ? -3.475  88.509 82.680  1.00 56.46  ? 27  LYS   B CA  1 
ATOM   3027 C C   . LYS   B 2 57  ? -4.806  88.151 83.373  1.00 56.18  ? 27  LYS   B C   1 
ATOM   3028 O O   . LYS   B 2 57  ? -5.758  88.941 83.372  1.00 55.78  ? 27  LYS   B O   1 
ATOM   3029 C CB  . LYS   B 2 57  ? -3.431  87.827 81.290  1.00 58.15  ? 27  LYS   B CB  1 
ATOM   3030 C CG  . LYS   B 2 57  ? -2.062  87.773 80.630  1.00 62.18  ? 27  LYS   B CG  1 
ATOM   3031 C CD  . LYS   B 2 57  ? -2.049  86.833 79.411  1.00 66.93  ? 27  LYS   B CD  1 
ATOM   3032 C CE  . LYS   B 2 57  ? -2.496  85.413 79.719  1.00 70.65  ? 27  LYS   B CE  1 
ATOM   3033 N NZ  . LYS   B 2 57  ? -1.884  84.408 78.801  1.00 72.49  ? 27  LYS   B NZ  1 
ATOM   3034 N N   . ASP   B 2 58  ? -4.851  86.954 83.979  1.00 55.80  ? 28  ASP   B N   1 
ATOM   3035 C CA  . ASP   B 2 58  ? -6.036  86.479 84.679  1.00 55.91  ? 28  ASP   B CA  1 
ATOM   3036 C C   . ASP   B 2 58  ? -6.098  86.871 86.151  1.00 56.55  ? 28  ASP   B C   1 
ATOM   3037 O O   . ASP   B 2 58  ? -7.184  86.852 86.743  1.00 56.31  ? 28  ASP   B O   1 
ATOM   3038 C CB  . ASP   B 2 58  ? -6.192  84.975 84.500  1.00 56.10  ? 28  ASP   B CB  1 
ATOM   3039 C CG  . ASP   B 2 58  ? -6.769  84.573 83.159  1.00 58.16  ? 28  ASP   B CG  1 
ATOM   3040 O OD1 . ASP   B 2 58  ? -7.098  85.471 82.354  1.00 57.56  ? 28  ASP   B OD1 1 
ATOM   3041 O OD2 . ASP   B 2 58  ? -6.905  83.365 82.917  1.00 60.42  ? 28  ASP   B OD2 1 
ATOM   3042 N N   . LEU   B 2 59  ? -4.955  87.258 86.737  1.00 57.13  ? 29  LEU   B N   1 
ATOM   3043 C CA  . LEU   B 2 59  ? -4.954  87.722 88.115  1.00 57.92  ? 29  LEU   B CA  1 
ATOM   3044 C C   . LEU   B 2 59  ? -5.486  89.161 88.251  1.00 58.91  ? 29  LEU   B C   1 
ATOM   3045 O O   . LEU   B 2 59  ? -5.492  89.706 89.353  1.00 59.47  ? 29  LEU   B O   1 
ATOM   3046 C CB  . LEU   B 2 59  ? -3.602  87.520 88.809  1.00 58.06  ? 29  LEU   B CB  1 
ATOM   3047 C CG  . LEU   B 2 59  ? -3.095  86.061 88.862  1.00 59.54  ? 29  LEU   B CG  1 
ATOM   3048 C CD1 . LEU   B 2 59  ? -1.877  85.942 89.748  1.00 60.05  ? 29  LEU   B CD1 1 
ATOM   3049 C CD2 . LEU   B 2 59  ? -4.176  85.084 89.362  1.00 60.27  ? 29  LEU   B CD2 1 
ATOM   3050 N N   . LYS   B 2 60  ? -6.003  89.744 87.164  1.00 59.08  ? 30  LYS   B N   1 
ATOM   3051 C CA  . LYS   B 2 60  ? -6.674  91.026 87.225  1.00 60.24  ? 30  LYS   B CA  1 
ATOM   3052 C C   . LYS   B 2 60  ? -8.125  90.756 87.657  1.00 60.60  ? 30  LYS   B C   1 
ATOM   3053 O O   . LYS   B 2 60  ? -8.641  91.442 88.533  1.00 61.20  ? 30  LYS   B O   1 
ATOM   3054 C CB  . LYS   B 2 60  ? -6.617  91.746 85.867  1.00 62.86  ? 30  LYS   B CB  1 
ATOM   3055 C CG  . LYS   B 2 60  ? -5.197  92.192 85.498  1.00 67.94  ? 30  LYS   B CG  1 
ATOM   3056 C CD  . LYS   B 2 60  ? -5.105  92.827 84.120  1.00 73.10  ? 30  LYS   B CD  1 
ATOM   3057 C CE  . LYS   B 2 60  ? -5.296  94.327 84.159  1.00 77.62  ? 30  LYS   B CE  1 
ATOM   3058 N NZ  . LYS   B 2 60  ? -5.087  94.951 82.817  1.00 80.34  ? 30  LYS   B NZ  1 
ATOM   3059 N N   . PHE   B 2 61  ? -8.754  89.723 87.089  1.00 60.35  ? 31  PHE   B N   1 
ATOM   3060 C CA  . PHE   B 2 61  ? -10.125 89.324 87.383  1.00 60.87  ? 31  PHE   B CA  1 
ATOM   3061 C C   . PHE   B 2 61  ? -10.258 88.441 88.640  1.00 59.72  ? 31  PHE   B C   1 
ATOM   3062 O O   . PHE   B 2 61  ? -11.245 88.555 89.364  1.00 59.73  ? 31  PHE   B O   1 
ATOM   3063 C CB  . PHE   B 2 61  ? -10.718 88.602 86.160  1.00 61.88  ? 31  PHE   B CB  1 
ATOM   3064 C CG  . PHE   B 2 61  ? -10.817 89.483 84.932  1.00 63.80  ? 31  PHE   B CG  1 
ATOM   3065 C CD1 . PHE   B 2 61  ? -11.973 90.197 84.662  1.00 64.94  ? 31  PHE   B CD1 1 
ATOM   3066 C CD2 . PHE   B 2 61  ? -9.753  89.599 84.052  1.00 65.14  ? 31  PHE   B CD2 1 
ATOM   3067 C CE1 . PHE   B 2 61  ? -12.065 90.995 83.531  1.00 65.75  ? 31  PHE   B CE1 1 
ATOM   3068 C CE2 . PHE   B 2 61  ? -9.846  90.409 82.927  1.00 65.94  ? 31  PHE   B CE2 1 
ATOM   3069 C CZ  . PHE   B 2 61  ? -11.003 91.094 82.671  1.00 65.69  ? 31  PHE   B CZ  1 
ATOM   3070 N N   . LEU   B 2 62  ? -9.279  87.550 88.884  1.00 58.42  ? 32  LEU   B N   1 
ATOM   3071 C CA  . LEU   B 2 62  ? -9.287  86.621 90.021  1.00 56.98  ? 32  LEU   B CA  1 
ATOM   3072 C C   . LEU   B 2 62  ? -8.058  86.775 90.933  1.00 55.66  ? 32  LEU   B C   1 
ATOM   3073 O O   . LEU   B 2 62  ? -6.960  87.024 90.440  1.00 55.51  ? 32  LEU   B O   1 
ATOM   3074 C CB  . LEU   B 2 62  ? -9.305  85.194 89.476  1.00 56.67  ? 32  LEU   B CB  1 
ATOM   3075 C CG  . LEU   B 2 62  ? -10.538 84.812 88.694  1.00 57.65  ? 32  LEU   B CG  1 
ATOM   3076 C CD1 . LEU   B 2 62  ? -10.194 83.883 87.548  1.00 57.59  ? 32  LEU   B CD1 1 
ATOM   3077 C CD2 . LEU   B 2 62  ? -11.599 84.244 89.612  1.00 58.32  ? 32  LEU   B CD2 1 
ATOM   3078 N N   . SER   B 2 63  ? -8.226  86.560 92.251  1.00 54.38  ? 33  SER   B N   1 
ATOM   3079 C CA  . SER   B 2 63  ? -7.082  86.601 93.162  1.00 53.84  ? 33  SER   B CA  1 
ATOM   3080 C C   . SER   B 2 63  ? -6.212  85.346 92.939  1.00 54.08  ? 33  SER   B C   1 
ATOM   3081 O O   . SER   B 2 63  ? -6.582  84.478 92.146  1.00 54.27  ? 33  SER   B O   1 
ATOM   3082 C CB  . SER   B 2 63  ? -7.546  86.712 94.614  1.00 54.30  ? 33  SER   B CB  1 
ATOM   3083 O OG  . SER   B 2 63  ? -7.975  85.487 95.181  1.00 55.68  ? 33  SER   B OG  1 
ATOM   3084 N N   . GLU   B 2 64  ? -5.042  85.256 93.588  1.00 53.96  ? 34  GLU   B N   1 
ATOM   3085 C CA  . GLU   B 2 64  ? -4.192  84.067 93.452  1.00 54.16  ? 34  GLU   B CA  1 
ATOM   3086 C C   . GLU   B 2 64  ? -4.920  82.838 94.014  1.00 53.25  ? 34  GLU   B C   1 
ATOM   3087 O O   . GLU   B 2 64  ? -4.822  81.751 93.452  1.00 52.79  ? 34  GLU   B O   1 
ATOM   3088 C CB  . GLU   B 2 64  ? -2.867  84.262 94.199  1.00 57.58  ? 34  GLU   B CB  1 
ATOM   3089 C CG  . GLU   B 2 64  ? -1.973  85.322 93.602  1.00 64.81  ? 34  GLU   B CG  1 
ATOM   3090 C CD  . GLU   B 2 64  ? -0.512  84.924 93.600  1.00 73.92  ? 34  GLU   B CD  1 
ATOM   3091 O OE1 . GLU   B 2 64  ? 0.257   85.502 94.403  1.00 76.41  ? 34  GLU   B OE1 1 
ATOM   3092 O OE2 . GLU   B 2 64  ? -0.137  84.031 92.802  1.00 75.70  ? 34  GLU   B OE2 1 
ATOM   3093 N N   . GLU   B 2 65  ? -5.650  83.039 95.131  1.00 52.88  ? 35  GLU   B N   1 
ATOM   3094 C CA  . GLU   B 2 65  ? -6.436  82.045 95.855  1.00 52.80  ? 35  GLU   B CA  1 
ATOM   3095 C C   . GLU   B 2 65  ? -7.591  81.563 94.996  1.00 51.73  ? 35  GLU   B C   1 
ATOM   3096 O O   . GLU   B 2 65  ? -7.818  80.369 94.913  1.00 52.18  ? 35  GLU   B O   1 
ATOM   3097 C CB  . GLU   B 2 65  ? -6.966  82.653 97.159  1.00 55.63  ? 35  GLU   B CB  1 
ATOM   3098 C CG  . GLU   B 2 65  ? -6.783  81.765 98.371  1.00 62.49  ? 35  GLU   B CG  1 
ATOM   3099 C CD  . GLU   B 2 65  ? -7.254  82.373 99.680  1.00 72.41  ? 35  GLU   B CD  1 
ATOM   3100 O OE1 . GLU   B 2 65  ? -7.806  83.498 99.656  1.00 73.89  ? 35  GLU   B OE1 1 
ATOM   3101 O OE2 . GLU   B 2 65  ? -7.073  81.720 100.734 1.00 76.35  ? 35  GLU   B OE2 1 
ATOM   3102 N N   . GLU   B 2 66  ? -8.292  82.474 94.331  1.00 50.27  ? 36  GLU   B N   1 
ATOM   3103 C CA  . GLU   B 2 66  ? -9.397  82.111 93.457  1.00 49.65  ? 36  GLU   B CA  1 
ATOM   3104 C C   . GLU   B 2 66  ? -8.918  81.356 92.241  1.00 48.57  ? 36  GLU   B C   1 
ATOM   3105 O O   . GLU   B 2 66  ? -9.602  80.440 91.807  1.00 48.77  ? 36  GLU   B O   1 
ATOM   3106 C CB  . GLU   B 2 66  ? -10.183 83.352 93.039  1.00 52.29  ? 36  GLU   B CB  1 
ATOM   3107 C CG  . GLU   B 2 66  ? -10.654 84.142 94.242  1.00 56.78  ? 36  GLU   B CG  1 
ATOM   3108 C CD  . GLU   B 2 66  ? -11.517 85.339 93.931  1.00 61.45  ? 36  GLU   B CD  1 
ATOM   3109 O OE1 . GLU   B 2 66  ? -11.066 86.233 93.177  1.00 61.82  ? 36  GLU   B OE1 1 
ATOM   3110 O OE2 . GLU   B 2 66  ? -12.649 85.381 94.459  1.00 63.68  ? 36  GLU   B OE2 1 
ATOM   3111 N N   . TYR   B 2 67  ? -7.744  81.713 91.703  1.00 47.80  ? 37  TYR   B N   1 
ATOM   3112 C CA  . TYR   B 2 67  ? -7.158  81.032 90.552  1.00 47.80  ? 37  TYR   B CA  1 
ATOM   3113 C C   . TYR   B 2 67  ? -6.815  79.577 90.917  1.00 48.27  ? 37  TYR   B C   1 
ATOM   3114 O O   . TYR   B 2 67  ? -7.082  78.670 90.125  1.00 48.45  ? 37  TYR   B O   1 
ATOM   3115 C CB  . TYR   B 2 67  ? -5.916  81.786 90.035  1.00 47.64  ? 37  TYR   B CB  1 
ATOM   3116 C CG  . TYR   B 2 67  ? -5.462  81.303 88.675  1.00 48.33  ? 37  TYR   B CG  1 
ATOM   3117 C CD1 . TYR   B 2 67  ? -4.611  80.213 88.550  1.00 49.08  ? 37  TYR   B CD1 1 
ATOM   3118 C CD2 . TYR   B 2 67  ? -5.913  81.911 87.512  1.00 49.05  ? 37  TYR   B CD2 1 
ATOM   3119 C CE1 . TYR   B 2 67  ? -4.235  79.728 87.306  1.00 49.78  ? 37  TYR   B CE1 1 
ATOM   3120 C CE2 . TYR   B 2 67  ? -5.539  81.437 86.259  1.00 49.83  ? 37  TYR   B CE2 1 
ATOM   3121 C CZ  . TYR   B 2 67  ? -4.696  80.344 86.161  1.00 50.41  ? 37  TYR   B CZ  1 
ATOM   3122 O OH  . TYR   B 2 67  ? -4.294  79.864 84.939  1.00 51.04  ? 37  TYR   B OH  1 
ATOM   3123 N N   . TRP   B 2 68  ? -6.251  79.354 92.128  1.00 48.28  ? 38  TRP   B N   1 
ATOM   3124 C CA  . TRP   B 2 68  ? -5.910  78.018 92.619  1.00 48.62  ? 38  TRP   B CA  1 
ATOM   3125 C C   . TRP   B 2 68  ? -7.186  77.226 92.793  1.00 47.45  ? 38  TRP   B C   1 
ATOM   3126 O O   . TRP   B 2 68  ? -7.307  76.146 92.235  1.00 47.85  ? 38  TRP   B O   1 
ATOM   3127 C CB  . TRP   B 2 68  ? -5.121  78.065 93.952  1.00 49.58  ? 38  TRP   B CB  1 
ATOM   3128 C CG  . TRP   B 2 68  ? -4.576  76.732 94.428  1.00 51.70  ? 38  TRP   B CG  1 
ATOM   3129 C CD1 . TRP   B 2 68  ? -4.514  75.557 93.725  1.00 52.83  ? 38  TRP   B CD1 1 
ATOM   3130 C CD2 . TRP   B 2 68  ? -3.909  76.482 95.679  1.00 52.50  ? 38  TRP   B CD2 1 
ATOM   3131 N NE1 . TRP   B 2 68  ? -3.882  74.591 94.471  1.00 53.34  ? 38  TRP   B NE1 1 
ATOM   3132 C CE2 . TRP   B 2 68  ? -3.501  75.131 95.675  1.00 53.37  ? 38  TRP   B CE2 1 
ATOM   3133 C CE3 . TRP   B 2 68  ? -3.608  77.272 96.797  1.00 53.22  ? 38  TRP   B CE3 1 
ATOM   3134 C CZ2 . TRP   B 2 68  ? -2.855  74.544 96.768  1.00 54.28  ? 38  TRP   B CZ2 1 
ATOM   3135 C CZ3 . TRP   B 2 68  ? -2.950  76.692 97.867  1.00 54.16  ? 38  TRP   B CZ3 1 
ATOM   3136 C CH2 . TRP   B 2 68  ? -2.585  75.345 97.849  1.00 54.34  ? 38  TRP   B CH2 1 
ATOM   3137 N N   . LYS   B 2 69  ? -8.168  77.795 93.486  1.00 46.06  ? 39  LYS   B N   1 
ATOM   3138 C CA  . LYS   B 2 69  ? -9.467  77.189 93.719  1.00 45.03  ? 39  LYS   B CA  1 
ATOM   3139 C C   . LYS   B 2 69  ? -10.158 76.813 92.411  1.00 44.77  ? 39  LYS   B C   1 
ATOM   3140 O O   . LYS   B 2 69  ? -10.842 75.796 92.365  1.00 45.27  ? 39  LYS   B O   1 
ATOM   3141 C CB  . LYS   B 2 69  ? -10.330 78.144 94.538  1.00 45.54  ? 39  LYS   B CB  1 
ATOM   3142 C CG  . LYS   B 2 69  ? -9.824  78.314 95.953  1.00 47.64  ? 39  LYS   B CG  1 
ATOM   3143 C CD  . LYS   B 2 69  ? -10.572 79.395 96.706  1.00 50.72  ? 39  LYS   B CD  1 
ATOM   3144 C CE  . LYS   B 2 69  ? -10.180 79.387 98.162  1.00 53.91  ? 39  LYS   B CE  1 
ATOM   3145 N NZ  . LYS   B 2 69  ? -10.924 80.395 98.961  1.00 55.86  ? 39  LYS   B NZ  1 
ATOM   3146 N N   . LEU   B 2 70  ? -9.973  77.603 91.350  1.00 44.03  ? 40  LEU   B N   1 
ATOM   3147 C CA  . LEU   B 2 70  ? -10.557 77.289 90.050  1.00 44.44  ? 40  LEU   B CA  1 
ATOM   3148 C C   . LEU   B 2 70  ? -9.828  76.104 89.414  1.00 45.02  ? 40  LEU   B C   1 
ATOM   3149 O O   . LEU   B 2 70  ? -10.457 75.226 88.817  1.00 45.19  ? 40  LEU   B O   1 
ATOM   3150 C CB  . LEU   B 2 70  ? -10.444 78.501 89.131  1.00 44.81  ? 40  LEU   B CB  1 
ATOM   3151 C CG  . LEU   B 2 70  ? -11.760 79.125 88.736  1.00 46.51  ? 40  LEU   B CG  1 
ATOM   3152 C CD1 . LEU   B 2 70  ? -11.545 80.473 88.121  1.00 47.57  ? 40  LEU   B CD1 1 
ATOM   3153 C CD2 . LEU   B 2 70  ? -12.472 78.271 87.772  1.00 46.84  ? 40  LEU   B CD2 1 
ATOM   3154 N N   . GLN   B 2 71  ? -8.487  76.080 89.553  1.00 44.97  ? 41  GLN   B N   1 
ATOM   3155 C CA  . GLN   B 2 71  ? -7.633  75.020 89.035  1.00 44.83  ? 41  GLN   B CA  1 
ATOM   3156 C C   . GLN   B 2 71  ? -7.866  73.693 89.768  1.00 43.95  ? 41  GLN   B C   1 
ATOM   3157 O O   . GLN   B 2 71  ? -7.686  72.636 89.180  1.00 44.28  ? 41  GLN   B O   1 
ATOM   3158 C CB  . GLN   B 2 71  ? -6.157  75.464 89.025  1.00 47.12  ? 41  GLN   B CB  1 
ATOM   3159 C CG  . GLN   B 2 71  ? -5.845  76.518 87.934  1.00 51.92  ? 41  GLN   B CG  1 
ATOM   3160 C CD  . GLN   B 2 71  ? -5.876  75.983 86.492  1.00 57.81  ? 41  GLN   B CD  1 
ATOM   3161 O OE1 . GLN   B 2 71  ? -5.344  74.908 86.185  1.00 61.06  ? 41  GLN   B OE1 1 
ATOM   3162 N NE2 . GLN   B 2 71  ? -6.480  76.720 85.559  1.00 56.85  ? 41  GLN   B NE2 1 
ATOM   3163 N N   . ILE   B 2 72  ? -8.305  73.745 91.031  1.00 42.98  ? 42  ILE   B N   1 
ATOM   3164 C CA  . ILE   B 2 72  ? -8.670  72.564 91.816  1.00 42.61  ? 42  ILE   B CA  1 
ATOM   3165 C C   . ILE   B 2 72  ? -10.017 72.063 91.291  1.00 42.54  ? 42  ILE   B C   1 
ATOM   3166 O O   . ILE   B 2 72  ? -10.189 70.863 91.088  1.00 43.04  ? 42  ILE   B O   1 
ATOM   3167 C CB  . ILE   B 2 72  ? -8.771  72.938 93.313  1.00 42.68  ? 42  ILE   B CB  1 
ATOM   3168 C CG1 . ILE   B 2 72  ? -7.392  73.204 93.919  1.00 43.30  ? 42  ILE   B CG1 1 
ATOM   3169 C CG2 . ILE   B 2 72  ? -9.527  71.889 94.100  1.00 43.14  ? 42  ILE   B CG2 1 
ATOM   3170 C CD1 . ILE   B 2 72  ? -7.438  74.056 95.164  1.00 44.23  ? 42  ILE   B CD1 1 
ATOM   3171 N N   . PHE   B 2 73  ? -10.961 72.991 91.069  1.00 41.75  ? 43  PHE   B N   1 
ATOM   3172 C CA  . PHE   B 2 73  ? -12.298 72.724 90.579  1.00 41.44  ? 43  PHE   B CA  1 
ATOM   3173 C C   . PHE   B 2 73  ? -12.280 71.975 89.266  1.00 40.76  ? 43  PHE   B C   1 
ATOM   3174 O O   . PHE   B 2 73  ? -12.817 70.871 89.216  1.00 40.51  ? 43  PHE   B O   1 
ATOM   3175 C CB  . PHE   B 2 73  ? -13.104 74.029 90.469  1.00 41.48  ? 43  PHE   B CB  1 
ATOM   3176 C CG  . PHE   B 2 73  ? -14.498 73.800 89.956  1.00 42.14  ? 43  PHE   B CG  1 
ATOM   3177 C CD1 . PHE   B 2 73  ? -15.408 73.062 90.687  1.00 42.64  ? 43  PHE   B CD1 1 
ATOM   3178 C CD2 . PHE   B 2 73  ? -14.891 74.297 88.724  1.00 43.10  ? 43  PHE   B CD2 1 
ATOM   3179 C CE1 . PHE   B 2 73  ? -16.694 72.850 90.209  1.00 43.32  ? 43  PHE   B CE1 1 
ATOM   3180 C CE2 . PHE   B 2 73  ? -16.177 74.068 88.244  1.00 43.63  ? 43  PHE   B CE2 1 
ATOM   3181 C CZ  . PHE   B 2 73  ? -17.063 73.328 88.982  1.00 43.08  ? 43  PHE   B CZ  1 
ATOM   3182 N N   . PHE   B 2 74  ? -11.613 72.523 88.222  1.00 40.12  ? 44  PHE   B N   1 
ATOM   3183 C CA  . PHE   B 2 74  ? -11.562 71.859 86.912  1.00 39.63  ? 44  PHE   B CA  1 
ATOM   3184 C C   . PHE   B 2 74  ? -10.774 70.541 86.936  1.00 38.89  ? 44  PHE   B C   1 
ATOM   3185 O O   . PHE   B 2 74  ? -11.077 69.631 86.162  1.00 38.91  ? 44  PHE   B O   1 
ATOM   3186 C CB  . PHE   B 2 74  ? -11.088 72.809 85.817  1.00 39.70  ? 44  PHE   B CB  1 
ATOM   3187 C CG  . PHE   B 2 74  ? -12.205 73.746 85.407  1.00 40.57  ? 44  PHE   B CG  1 
ATOM   3188 C CD1 . PHE   B 2 74  ? -13.349 73.261 84.790  1.00 41.40  ? 44  PHE   B CD1 1 
ATOM   3189 C CD2 . PHE   B 2 74  ? -12.144 75.098 85.703  1.00 41.13  ? 44  PHE   B CD2 1 
ATOM   3190 C CE1 . PHE   B 2 74  ? -14.394 74.114 84.451  1.00 41.91  ? 44  PHE   B CE1 1 
ATOM   3191 C CE2 . PHE   B 2 74  ? -13.186 75.946 85.352  1.00 41.72  ? 44  PHE   B CE2 1 
ATOM   3192 C CZ  . PHE   B 2 74  ? -14.309 75.447 84.746  1.00 41.61  ? 44  PHE   B CZ  1 
ATOM   3193 N N   . THR   B 2 75  ? -9.866  70.377 87.907  1.00 37.95  ? 45  THR   B N   1 
ATOM   3194 C CA  . THR   B 2 75  ? -9.184  69.105 88.117  1.00 37.50  ? 45  THR   B CA  1 
ATOM   3195 C C   . THR   B 2 75  ? -10.228 68.068 88.564  1.00 37.15  ? 45  THR   B C   1 
ATOM   3196 O O   . THR   B 2 75  ? -10.271 66.975 88.015  1.00 37.32  ? 45  THR   B O   1 
ATOM   3197 C CB  . THR   B 2 75  ? -8.029  69.284 89.108  1.00 38.04  ? 45  THR   B CB  1 
ATOM   3198 O OG1 . THR   B 2 75  ? -7.039  70.101 88.472  1.00 39.39  ? 45  THR   B OG1 1 
ATOM   3199 C CG2 . THR   B 2 75  ? -7.408  67.972 89.516  1.00 37.52  ? 45  THR   B CG2 1 
ATOM   3200 N N   . ASN   B 2 76  ? -11.128 68.459 89.478  1.00 36.66  ? 46  ASN   B N   1 
ATOM   3201 C CA  . ASN   B 2 76  ? -12.206 67.611 89.968  1.00 36.91  ? 46  ASN   B CA  1 
ATOM   3202 C C   . ASN   B 2 76  ? -13.269 67.314 88.895  1.00 37.36  ? 46  ASN   B C   1 
ATOM   3203 O O   . ASN   B 2 76  ? -13.875 66.245 88.942  1.00 37.78  ? 46  ASN   B O   1 
ATOM   3204 C CB  . ASN   B 2 76  ? -12.865 68.239 91.192  1.00 37.95  ? 46  ASN   B CB  1 
ATOM   3205 C CG  . ASN   B 2 76  ? -11.948 68.394 92.383  1.00 40.77  ? 46  ASN   B CG  1 
ATOM   3206 O OD1 . ASN   B 2 76  ? -10.807 67.906 92.394  1.00 41.43  ? 46  ASN   B OD1 1 
ATOM   3207 N ND2 . ASN   B 2 76  ? -12.434 69.088 93.418  1.00 41.10  ? 46  ASN   B ND2 1 
ATOM   3208 N N   . VAL   B 2 77  ? -13.512 68.253 87.944  1.00 36.97  ? 47  VAL   B N   1 
ATOM   3209 C CA  . VAL   B 2 77  ? -14.467 68.070 86.846  1.00 36.66  ? 47  VAL   B CA  1 
ATOM   3210 C C   . VAL   B 2 77  ? -13.929 67.006 85.893  1.00 36.98  ? 47  VAL   B C   1 
ATOM   3211 O O   . VAL   B 2 77  ? -14.640 66.050 85.571  1.00 36.78  ? 47  VAL   B O   1 
ATOM   3212 C CB  . VAL   B 2 77  ? -14.751 69.392 86.104  1.00 37.18  ? 47  VAL   B CB  1 
ATOM   3213 C CG1 . VAL   B 2 77  ? -15.663 69.164 84.903  1.00 37.39  ? 47  VAL   B CG1 1 
ATOM   3214 C CG2 . VAL   B 2 77  ? -15.340 70.442 87.040  1.00 37.77  ? 47  VAL   B CG2 1 
ATOM   3215 N N   . ILE   B 2 78  ? -12.641 67.134 85.503  1.00 37.15  ? 48  ILE   B N   1 
ATOM   3216 C CA  . ILE   B 2 78  ? -11.951 66.190 84.622  1.00 37.86  ? 48  ILE   B CA  1 
ATOM   3217 C C   . ILE   B 2 78  ? -11.978 64.796 85.241  1.00 38.71  ? 48  ILE   B C   1 
ATOM   3218 O O   . ILE   B 2 78  ? -12.344 63.844 84.567  1.00 39.40  ? 48  ILE   B O   1 
ATOM   3219 C CB  . ILE   B 2 78  ? -10.506 66.682 84.335  1.00 38.68  ? 48  ILE   B CB  1 
ATOM   3220 C CG1 . ILE   B 2 78  ? -10.513 67.925 83.434  1.00 39.40  ? 48  ILE   B CG1 1 
ATOM   3221 C CG2 . ILE   B 2 78  ? -9.643  65.576 83.722  1.00 39.61  ? 48  ILE   B CG2 1 
ATOM   3222 C CD1 . ILE   B 2 78  ? -9.179  68.580 83.255  1.00 40.50  ? 48  ILE   B CD1 1 
ATOM   3223 N N   . GLN   B 2 79  ? -11.668 64.685 86.541  1.00 38.65  ? 49  GLN   B N   1 
ATOM   3224 C CA  . GLN   B 2 79  ? -11.707 63.415 87.264  1.00 38.76  ? 49  GLN   B CA  1 
ATOM   3225 C C   . GLN   B 2 79  ? -13.109 62.799 87.243  1.00 38.89  ? 49  GLN   B C   1 
ATOM   3226 O O   . GLN   B 2 79  ? -13.238 61.618 86.942  1.00 39.43  ? 49  GLN   B O   1 
ATOM   3227 C CB  . GLN   B 2 79  ? -11.163 63.578 88.694  1.00 40.18  ? 49  GLN   B CB  1 
ATOM   3228 C CG  . GLN   B 2 79  ? -11.253 62.333 89.564  1.00 44.22  ? 49  GLN   B CG  1 
ATOM   3229 C CD  . GLN   B 2 79  ? -10.399 61.178 89.083  1.00 51.58  ? 49  GLN   B CD  1 
ATOM   3230 O OE1 . GLN   B 2 79  ? -9.204  61.314 88.823  1.00 54.53  ? 49  GLN   B OE1 1 
ATOM   3231 N NE2 . GLN   B 2 79  ? -10.987 59.988 88.981  1.00 53.02  ? 49  GLN   B NE2 1 
ATOM   3232 N N   . ALA   B 2 80  ? -14.153 63.593 87.478  1.00 38.54  ? 50  ALA   B N   1 
ATOM   3233 C CA  . ALA   B 2 80  ? -15.521 63.084 87.450  1.00 39.00  ? 50  ALA   B CA  1 
ATOM   3234 C C   . ALA   B 2 80  ? -15.924 62.639 86.041  1.00 40.12  ? 50  ALA   B C   1 
ATOM   3235 O O   . ALA   B 2 80  ? -16.595 61.612 85.895  1.00 40.14  ? 50  ALA   B O   1 
ATOM   3236 C CB  . ALA   B 2 80  ? -16.474 64.140 87.957  1.00 38.92  ? 50  ALA   B CB  1 
ATOM   3237 N N   . LEU   B 2 81  ? -15.484 63.397 85.000  1.00 40.71  ? 51  LEU   B N   1 
ATOM   3238 C CA  . LEU   B 2 81  ? -15.745 63.087 83.590  1.00 41.33  ? 51  LEU   B CA  1 
ATOM   3239 C C   . LEU   B 2 81  ? -15.112 61.750 83.255  1.00 41.75  ? 51  LEU   B C   1 
ATOM   3240 O O   . LEU   B 2 81  ? -15.761 60.902 82.652  1.00 42.08  ? 51  LEU   B O   1 
ATOM   3241 C CB  . LEU   B 2 81  ? -15.136 64.153 82.655  1.00 41.86  ? 51  LEU   B CB  1 
ATOM   3242 C CG  . LEU   B 2 81  ? -15.828 65.488 82.531  1.00 43.66  ? 51  LEU   B CG  1 
ATOM   3243 C CD1 . LEU   B 2 81  ? -15.060 66.392 81.577  1.00 43.76  ? 51  LEU   B CD1 1 
ATOM   3244 C CD2 . LEU   B 2 81  ? -17.264 65.314 82.079  1.00 44.63  ? 51  LEU   B CD2 1 
ATOM   3245 N N   . GLY   B 2 82  ? -13.846 61.583 83.643  1.00 41.59  ? 52  GLY   B N   1 
ATOM   3246 C CA  . GLY   B 2 82  ? -13.082 60.369 83.412  1.00 41.95  ? 52  GLY   B CA  1 
ATOM   3247 C C   . GLY   B 2 82  ? -13.709 59.178 84.092  1.00 42.28  ? 52  GLY   B C   1 
ATOM   3248 O O   . GLY   B 2 82  ? -13.771 58.104 83.499  1.00 42.92  ? 52  GLY   B O   1 
ATOM   3249 N N   . GLU   B 2 83  ? -14.215 59.354 85.326  1.00 42.11  ? 53  GLU   B N   1 
ATOM   3250 C CA  . GLU   B 2 83  ? -14.881 58.265 86.043  1.00 42.84  ? 53  GLU   B CA  1 
ATOM   3251 C C   . GLU   B 2 83  ? -16.118 57.816 85.280  1.00 43.52  ? 53  GLU   B C   1 
ATOM   3252 O O   . GLU   B 2 83  ? -16.255 56.637 84.991  1.00 43.63  ? 53  GLU   B O   1 
ATOM   3253 C CB  . GLU   B 2 83  ? -15.248 58.667 87.479  1.00 44.70  ? 53  GLU   B CB  1 
ATOM   3254 C CG  . GLU   B 2 83  ? -14.065 58.680 88.425  1.00 50.00  ? 53  GLU   B CG  1 
ATOM   3255 C CD  . GLU   B 2 83  ? -14.319 59.427 89.721  1.00 57.84  ? 53  GLU   B CD  1 
ATOM   3256 O OE1 . GLU   B 2 83  ? -15.505 59.623 90.078  1.00 59.75  ? 53  GLU   B OE1 1 
ATOM   3257 O OE2 . GLU   B 2 83  ? -13.329 59.819 90.381  1.00 58.86  ? 53  GLU   B OE2 1 
ATOM   3258 N N   . HIS   B 2 84  ? -16.948 58.768 84.852  1.00 43.99  ? 54  HIS   B N   1 
ATOM   3259 C CA  . HIS   B 2 84  ? -18.157 58.509 84.080  1.00 45.03  ? 54  HIS   B CA  1 
ATOM   3260 C C   . HIS   B 2 84  ? -17.870 57.671 82.828  1.00 45.97  ? 54  HIS   B C   1 
ATOM   3261 O O   . HIS   B 2 84  ? -18.617 56.743 82.516  1.00 46.45  ? 54  HIS   B O   1 
ATOM   3262 C CB  . HIS   B 2 84  ? -18.802 59.845 83.677  1.00 45.92  ? 54  HIS   B CB  1 
ATOM   3263 C CG  . HIS   B 2 84  ? -20.220 59.713 83.241  1.00 48.86  ? 54  HIS   B CG  1 
ATOM   3264 N ND1 . HIS   B 2 84  ? -21.265 59.924 84.121  1.00 50.93  ? 54  HIS   B ND1 1 
ATOM   3265 C CD2 . HIS   B 2 84  ? -20.726 59.351 82.039  1.00 50.47  ? 54  HIS   B CD2 1 
ATOM   3266 C CE1 . HIS   B 2 84  ? -22.371 59.708 83.426  1.00 51.60  ? 54  HIS   B CE1 1 
ATOM   3267 N NE2 . HIS   B 2 84  ? -22.099 59.360 82.166  1.00 51.60  ? 54  HIS   B NE2 1 
ATOM   3268 N N   . LEU   B 2 85  ? -16.769 57.970 82.139  1.00 46.18  ? 55  LEU   B N   1 
ATOM   3269 C CA  . LEU   B 2 85  ? -16.396 57.256 80.923  1.00 47.15  ? 55  LEU   B CA  1 
ATOM   3270 C C   . LEU   B 2 85  ? -15.591 55.966 81.156  1.00 48.48  ? 55  LEU   B C   1 
ATOM   3271 O O   . LEU   B 2 85  ? -15.060 55.384 80.206  1.00 48.47  ? 55  LEU   B O   1 
ATOM   3272 C CB  . LEU   B 2 85  ? -15.654 58.209 79.998  1.00 47.21  ? 55  LEU   B CB  1 
ATOM   3273 C CG  . LEU   B 2 85  ? -16.512 59.350 79.513  1.00 48.58  ? 55  LEU   B CG  1 
ATOM   3274 C CD1 . LEU   B 2 85  ? -15.674 60.539 79.127  1.00 49.05  ? 55  LEU   B CD1 1 
ATOM   3275 C CD2 . LEU   B 2 85  ? -17.433 58.892 78.411  1.00 49.00  ? 55  LEU   B CD2 1 
ATOM   3276 N N   . LYS   B 2 86  ? -15.523 55.517 82.419  1.00 49.28  ? 56  LYS   B N   1 
ATOM   3277 C CA  . LYS   B 2 86  ? -14.809 54.329 82.865  1.00 50.35  ? 56  LYS   B CA  1 
ATOM   3278 C C   . LYS   B 2 86  ? -13.366 54.295 82.348  1.00 50.45  ? 56  LYS   B C   1 
ATOM   3279 O O   . LYS   B 2 86  ? -12.831 53.231 82.029  1.00 51.00  ? 56  LYS   B O   1 
ATOM   3280 C CB  . LYS   B 2 86  ? -15.601 53.052 82.526  1.00 53.05  ? 56  LYS   B CB  1 
ATOM   3281 C CG  . LYS   B 2 86  ? -16.955 52.962 83.240  1.00 57.89  ? 56  LYS   B CG  1 
ATOM   3282 C CD  . LYS   B 2 86  ? -17.620 51.611 82.998  1.00 63.39  ? 56  LYS   B CD  1 
ATOM   3283 C CE  . LYS   B 2 86  ? -18.826 51.364 83.880  1.00 68.25  ? 56  LYS   B CE  1 
ATOM   3284 N NZ  . LYS   B 2 86  ? -19.274 49.934 83.832  1.00 71.07  ? 56  LYS   B NZ  1 
ATOM   3285 N N   . LEU   B 2 87  ? -12.743 55.469 82.277  1.00 49.82  ? 57  LEU   B N   1 
ATOM   3286 C CA  . LEU   B 2 87  ? -11.385 55.612 81.789  1.00 50.10  ? 57  LEU   B CA  1 
ATOM   3287 C C   . LEU   B 2 87  ? -10.372 55.410 82.894  1.00 51.24  ? 57  LEU   B C   1 
ATOM   3288 O O   . LEU   B 2 87  ? -10.624 55.762 84.048  1.00 51.83  ? 57  LEU   B O   1 
ATOM   3289 C CB  . LEU   B 2 87  ? -11.194 57.002 81.184  1.00 49.49  ? 57  LEU   B CB  1 
ATOM   3290 C CG  . LEU   B 2 87  ? -12.142 57.369 80.072  1.00 49.68  ? 57  LEU   B CG  1 
ATOM   3291 C CD1 . LEU   B 2 87  ? -11.982 58.808 79.705  1.00 49.93  ? 57  LEU   B CD1 1 
ATOM   3292 C CD2 . LEU   B 2 87  ? -11.920 56.499 78.878  1.00 49.95  ? 57  LEU   B CD2 1 
ATOM   3293 N N   . ARG   B 2 88  ? -9.213  54.871 82.536  1.00 51.34  ? 58  ARG   B N   1 
ATOM   3294 C CA  . ARG   B 2 88  ? -8.120  54.636 83.470  1.00 51.82  ? 58  ARG   B CA  1 
ATOM   3295 C C   . ARG   B 2 88  ? -7.589  55.958 84.036  1.00 50.57  ? 58  ARG   B C   1 
ATOM   3296 O O   . ARG   B 2 88  ? -7.738  57.007 83.403  1.00 50.74  ? 58  ARG   B O   1 
ATOM   3297 C CB  . ARG   B 2 88  ? -6.983  53.931 82.730  1.00 54.68  ? 58  ARG   B CB  1 
ATOM   3298 C CG  . ARG   B 2 88  ? -6.691  52.539 83.203  1.00 60.25  ? 58  ARG   B CG  1 
ATOM   3299 C CD  . ARG   B 2 88  ? -5.637  51.935 82.296  1.00 66.32  ? 58  ARG   B CD  1 
ATOM   3300 N NE  . ARG   B 2 88  ? -4.830  50.918 82.976  1.00 71.54  ? 58  ARG   B NE  1 
ATOM   3301 C CZ  . ARG   B 2 88  ? -4.997  49.608 82.835  1.00 74.80  ? 58  ARG   B CZ  1 
ATOM   3302 N NH1 . ARG   B 2 88  ? -4.213  48.760 83.489  1.00 75.19  ? 58  ARG   B NH1 1 
ATOM   3303 N NH2 . ARG   B 2 88  ? -5.965  49.134 82.056  1.00 74.71  ? 58  ARG   B NH2 1 
ATOM   3304 N N   . GLN   B 2 89  ? -6.932  55.891 85.201  1.00 49.17  ? 59  GLN   B N   1 
ATOM   3305 C CA  . GLN   B 2 89  ? -6.338  57.050 85.851  1.00 48.60  ? 59  GLN   B CA  1 
ATOM   3306 C C   . GLN   B 2 89  ? -5.325  57.747 84.955  1.00 48.79  ? 59  GLN   B C   1 
ATOM   3307 O O   . GLN   B 2 89  ? -5.331  58.971 84.919  1.00 49.37  ? 59  GLN   B O   1 
ATOM   3308 C CB  . GLN   B 2 89  ? -5.686  56.663 87.187  1.00 49.27  ? 59  GLN   B CB  1 
ATOM   3309 C CG  . GLN   B 2 89  ? -5.360  57.835 88.081  1.00 51.79  ? 59  GLN   B CG  1 
ATOM   3310 C CD  . GLN   B 2 89  ? -6.582  58.662 88.420  1.00 56.95  ? 59  GLN   B CD  1 
ATOM   3311 O OE1 . GLN   B 2 89  ? -7.600  58.145 88.889  1.00 59.28  ? 59  GLN   B OE1 1 
ATOM   3312 N NE2 . GLN   B 2 89  ? -6.511  59.969 88.192  1.00 57.12  ? 59  GLN   B NE2 1 
ATOM   3313 N N   . GLN   B 2 90  ? -4.485  57.000 84.201  1.00 48.08  ? 60  GLN   B N   1 
ATOM   3314 C CA  . GLN   B 2 90  ? -3.489  57.614 83.309  1.00 47.82  ? 60  GLN   B CA  1 
ATOM   3315 C C   . GLN   B 2 90  ? -4.139  58.475 82.246  1.00 46.41  ? 60  GLN   B C   1 
ATOM   3316 O O   . GLN   B 2 90  ? -3.570  59.499 81.878  1.00 46.51  ? 60  GLN   B O   1 
ATOM   3317 C CB  . GLN   B 2 90  ? -2.559  56.569 82.669  1.00 50.62  ? 60  GLN   B CB  1 
ATOM   3318 C CG  . GLN   B 2 90  ? -1.416  57.154 81.827  1.00 55.87  ? 60  GLN   B CG  1 
ATOM   3319 C CD  . GLN   B 2 90  ? -0.266  56.174 81.641  1.00 63.05  ? 60  GLN   B CD  1 
ATOM   3320 O OE1 . GLN   B 2 90  ? 0.828   56.345 82.200  1.00 65.65  ? 60  GLN   B OE1 1 
ATOM   3321 N NE2 . GLN   B 2 90  ? -0.475  55.129 80.844  1.00 63.94  ? 60  GLN   B NE2 1 
ATOM   3322 N N   . VAL   B 2 91  ? -5.339  58.095 81.776  1.00 45.11  ? 61  VAL   B N   1 
ATOM   3323 C CA  . VAL   B 2 91  ? -6.046  58.911 80.797  1.00 44.72  ? 61  VAL   B CA  1 
ATOM   3324 C C   . VAL   B 2 91  ? -6.484  60.223 81.444  1.00 44.16  ? 61  VAL   B C   1 
ATOM   3325 O O   . VAL   B 2 91  ? -6.230  61.290 80.885  1.00 44.04  ? 61  VAL   B O   1 
ATOM   3326 C CB  . VAL   B 2 91  ? -7.220  58.170 80.142  1.00 45.49  ? 61  VAL   B CB  1 
ATOM   3327 C CG1 . VAL   B 2 91  ? -8.027  59.111 79.248  1.00 45.95  ? 61  VAL   B CG1 1 
ATOM   3328 C CG2 . VAL   B 2 91  ? -6.721  56.970 79.352  1.00 45.98  ? 61  VAL   B CG2 1 
ATOM   3329 N N   . ILE   B 2 92  ? -7.069  60.145 82.656  1.00 43.59  ? 62  ILE   B N   1 
ATOM   3330 C CA  . ILE   B 2 92  ? -7.513  61.313 83.419  1.00 43.43  ? 62  ILE   B CA  1 
ATOM   3331 C C   . ILE   B 2 92  ? -6.342  62.251 83.735  1.00 43.80  ? 62  ILE   B C   1 
ATOM   3332 O O   . ILE   B 2 92  ? -6.447  63.462 83.532  1.00 44.34  ? 62  ILE   B O   1 
ATOM   3333 C CB  . ILE   B 2 92  ? -8.272  60.894 84.699  1.00 43.35  ? 62  ILE   B CB  1 
ATOM   3334 C CG1 . ILE   B 2 92  ? -9.455  59.977 84.369  1.00 44.11  ? 62  ILE   B CG1 1 
ATOM   3335 C CG2 . ILE   B 2 92  ? -8.733  62.106 85.468  1.00 43.51  ? 62  ILE   B CG2 1 
ATOM   3336 C CD1 . ILE   B 2 92  ? -10.090 59.327 85.593  1.00 45.00  ? 62  ILE   B CD1 1 
ATOM   3337 N N   . ALA   B 2 93  ? -5.218  61.687 84.194  1.00 43.25  ? 63  ALA   B N   1 
ATOM   3338 C CA  . ALA   B 2 93  ? -4.013  62.430 84.526  1.00 43.03  ? 63  ALA   B CA  1 
ATOM   3339 C C   . ALA   B 2 93  ? -3.469  63.133 83.300  1.00 42.80  ? 63  ALA   B C   1 
ATOM   3340 O O   . ALA   B 2 93  ? -3.112  64.296 83.406  1.00 44.24  ? 63  ALA   B O   1 
ATOM   3341 C CB  . ALA   B 2 93  ? -2.969  61.496 85.097  1.00 43.59  ? 63  ALA   B CB  1 
ATOM   3342 N N   . THR   B 2 94  ? -3.469  62.479 82.129  1.00 41.26  ? 64  THR   B N   1 
ATOM   3343 C CA  . THR   B 2 94  ? -3.011  63.083 80.870  1.00 40.21  ? 64  THR   B CA  1 
ATOM   3344 C C   . THR   B 2 94  ? -3.953  64.228 80.474  1.00 39.35  ? 64  THR   B C   1 
ATOM   3345 O O   . THR   B 2 94  ? -3.499  65.303 80.097  1.00 39.07  ? 64  THR   B O   1 
ATOM   3346 C CB  . THR   B 2 94  ? -2.909  61.990 79.795  1.00 40.83  ? 64  THR   B CB  1 
ATOM   3347 O OG1 . THR   B 2 94  ? -1.731  61.245 80.039  1.00 42.06  ? 64  THR   B OG1 1 
ATOM   3348 C CG2 . THR   B 2 94  ? -2.834  62.530 78.400  1.00 40.71  ? 64  THR   B CG2 1 
ATOM   3349 N N   . ALA   B 2 95  ? -5.267  64.008 80.618  1.00 38.92  ? 65  ALA   B N   1 
ATOM   3350 C CA  . ALA   B 2 95  ? -6.292  65.010 80.327  1.00 38.86  ? 65  ALA   B CA  1 
ATOM   3351 C C   . ALA   B 2 95  ? -6.068  66.270 81.183  1.00 38.47  ? 65  ALA   B C   1 
ATOM   3352 O O   . ALA   B 2 95  ? -6.145  67.397 80.671  1.00 38.18  ? 65  ALA   B O   1 
ATOM   3353 C CB  . ALA   B 2 95  ? -7.690  64.433 80.584  1.00 38.62  ? 65  ALA   B CB  1 
ATOM   3354 N N   . THR   B 2 96  ? -5.762  66.064 82.480  1.00 37.86  ? 66  THR   B N   1 
ATOM   3355 C CA  . THR   B 2 96  ? -5.528  67.149 83.418  1.00 37.55  ? 66  THR   B CA  1 
ATOM   3356 C C   . THR   B 2 96  ? -4.293  67.938 83.009  1.00 37.63  ? 66  THR   B C   1 
ATOM   3357 O O   . THR   B 2 96  ? -4.307  69.173 83.025  1.00 37.99  ? 66  THR   B O   1 
ATOM   3358 C CB  . THR   B 2 96  ? -5.400  66.610 84.836  1.00 37.93  ? 66  THR   B CB  1 
ATOM   3359 O OG1 . THR   B 2 96  ? -6.534  65.797 85.141  1.00 37.57  ? 66  THR   B OG1 1 
ATOM   3360 C CG2 . THR   B 2 96  ? -5.250  67.733 85.862  1.00 38.57  ? 66  THR   B CG2 1 
ATOM   3361 N N   . VAL   B 2 97  ? -3.224  67.228 82.614  1.00 36.78  ? 67  VAL   B N   1 
ATOM   3362 C CA  . VAL   B 2 97  ? -1.993  67.890 82.188  1.00 35.67  ? 67  VAL   B CA  1 
ATOM   3363 C C   . VAL   B 2 97  ? -2.238  68.734 80.934  1.00 35.09  ? 67  VAL   B C   1 
ATOM   3364 O O   . VAL   B 2 97  ? -1.784  69.867 80.904  1.00 35.53  ? 67  VAL   B O   1 
ATOM   3365 C CB  . VAL   B 2 97  ? -0.822  66.892 82.037  1.00 35.73  ? 67  VAL   B CB  1 
ATOM   3366 C CG1 . VAL   B 2 97  ? 0.441   67.606 81.596  1.00 36.47  ? 67  VAL   B CG1 1 
ATOM   3367 C CG2 . VAL   B 2 97  ? -0.577  66.145 83.339  1.00 35.69  ? 67  VAL   B CG2 1 
ATOM   3368 N N   . TYR   B 2 98  ? -3.018  68.240 79.935  1.00 34.07  ? 68  TYR   B N   1 
ATOM   3369 C CA  . TYR   B 2 98  ? -3.309  69.028 78.727  1.00 33.71  ? 68  TYR   B CA  1 
ATOM   3370 C C   . TYR   B 2 98  ? -4.038  70.316 79.101  1.00 33.44  ? 68  TYR   B C   1 
ATOM   3371 O O   . TYR   B 2 98  ? -3.722  71.377 78.564  1.00 33.86  ? 68  TYR   B O   1 
ATOM   3372 C CB  . TYR   B 2 98  ? -4.216  68.274 77.741  1.00 33.86  ? 68  TYR   B CB  1 
ATOM   3373 C CG  . TYR   B 2 98  ? -3.635  67.058 77.067  1.00 34.25  ? 68  TYR   B CG  1 
ATOM   3374 C CD1 . TYR   B 2 98  ? -2.262  66.861 77.003  1.00 35.30  ? 68  TYR   B CD1 1 
ATOM   3375 C CD2 . TYR   B 2 98  ? -4.455  66.139 76.430  1.00 34.54  ? 68  TYR   B CD2 1 
ATOM   3376 C CE1 . TYR   B 2 98  ? -1.721  65.740 76.380  1.00 35.84  ? 68  TYR   B CE1 1 
ATOM   3377 C CE2 . TYR   B 2 98  ? -3.926  65.026 75.786  1.00 35.38  ? 68  TYR   B CE2 1 
ATOM   3378 C CZ  . TYR   B 2 98  ? -2.559  64.831 75.764  1.00 36.21  ? 68  TYR   B CZ  1 
ATOM   3379 O OH  . TYR   B 2 98  ? -2.039  63.719 75.166  1.00 37.12  ? 68  TYR   B OH  1 
ATOM   3380 N N   . PHE   B 2 99  ? -5.009  70.210 80.014  1.00 32.85  ? 69  PHE   B N   1 
ATOM   3381 C CA  . PHE   B 2 99  ? -5.819  71.314 80.490  1.00 33.50  ? 69  PHE   B CA  1 
ATOM   3382 C C   . PHE   B 2 99  ? -4.935  72.352 81.172  1.00 34.21  ? 69  PHE   B C   1 
ATOM   3383 O O   . PHE   B 2 99  ? -4.949  73.523 80.778  1.00 33.65  ? 69  PHE   B O   1 
ATOM   3384 C CB  . PHE   B 2 99  ? -6.896  70.777 81.443  1.00 33.78  ? 69  PHE   B CB  1 
ATOM   3385 C CG  . PHE   B 2 99  ? -7.937  71.787 81.847  1.00 34.81  ? 69  PHE   B CG  1 
ATOM   3386 C CD1 . PHE   B 2 99  ? -9.085  71.962 81.092  1.00 35.57  ? 69  PHE   B CD1 1 
ATOM   3387 C CD2 . PHE   B 2 99  ? -7.756  72.581 82.969  1.00 35.66  ? 69  PHE   B CD2 1 
ATOM   3388 C CE1 . PHE   B 2 99  ? -10.034 72.901 81.454  1.00 36.18  ? 69  PHE   B CE1 1 
ATOM   3389 C CE2 . PHE   B 2 99  ? -8.698  73.534 83.316  1.00 36.31  ? 69  PHE   B CE2 1 
ATOM   3390 C CZ  . PHE   B 2 99  ? -9.836  73.679 82.566  1.00 36.08  ? 69  PHE   B CZ  1 
ATOM   3391 N N   . LYS   B 2 100 ? -4.109  71.903 82.146  1.00 35.14  ? 70  LYS   B N   1 
ATOM   3392 C CA  . LYS   B 2 100 ? -3.147  72.745 82.867  1.00 35.98  ? 70  LYS   B CA  1 
ATOM   3393 C C   . LYS   B 2 100 ? -2.207  73.440 81.905  1.00 36.88  ? 70  LYS   B C   1 
ATOM   3394 O O   . LYS   B 2 100 ? -1.973  74.627 82.055  1.00 37.19  ? 70  LYS   B O   1 
ATOM   3395 C CB  . LYS   B 2 100 ? -2.309  71.920 83.851  1.00 37.08  ? 70  LYS   B CB  1 
ATOM   3396 C CG  . LYS   B 2 100 ? -3.083  71.413 85.027  1.00 41.02  ? 70  LYS   B CG  1 
ATOM   3397 C CD  . LYS   B 2 100 ? -2.132  71.061 86.124  1.00 45.87  ? 70  LYS   B CD  1 
ATOM   3398 C CE  . LYS   B 2 100 ? -2.848  70.481 87.300  1.00 49.96  ? 70  LYS   B CE  1 
ATOM   3399 N NZ  . LYS   B 2 100 ? -3.789  71.460 87.914  1.00 52.56  ? 70  LYS   B NZ  1 
ATOM   3400 N N   . ARG   B 2 101 ? -1.668  72.696 80.927  1.00 37.30  ? 71  ARG   B N   1 
ATOM   3401 C CA  . ARG   B 2 101 ? -0.753  73.194 79.908  1.00 37.96  ? 71  ARG   B CA  1 
ATOM   3402 C C   . ARG   B 2 101 ? -1.418  74.296 79.089  1.00 39.08  ? 71  ARG   B C   1 
ATOM   3403 O O   . ARG   B 2 101 ? -0.808  75.330 78.847  1.00 39.10  ? 71  ARG   B O   1 
ATOM   3404 C CB  . ARG   B 2 101 ? -0.316  72.041 78.986  1.00 38.09  ? 71  ARG   B CB  1 
ATOM   3405 C CG  . ARG   B 2 101 ? 0.741   71.158 79.590  1.00 39.48  ? 71  ARG   B CG  1 
ATOM   3406 C CD  . ARG   B 2 101 ? 1.237   70.166 78.569  1.00 41.90  ? 71  ARG   B CD  1 
ATOM   3407 N NE  . ARG   B 2 101 ? 2.191   69.202 79.130  1.00 43.04  ? 71  ARG   B NE  1 
ATOM   3408 C CZ  . ARG   B 2 101 ? 2.787   68.243 78.424  1.00 42.34  ? 71  ARG   B CZ  1 
ATOM   3409 N NH1 . ARG   B 2 101 ? 2.546   68.117 77.120  1.00 40.05  ? 71  ARG   B NH1 1 
ATOM   3410 N NH2 . ARG   B 2 101 ? 3.636   67.411 79.011  1.00 41.33  ? 71  ARG   B NH2 1 
ATOM   3411 N N   . PHE   B 2 102 ? -2.678  74.083 78.673  1.00 39.86  ? 72  PHE   B N   1 
ATOM   3412 C CA  . PHE   B 2 102 ? -3.395  75.060 77.867  1.00 40.60  ? 72  PHE   B CA  1 
ATOM   3413 C C   . PHE   B 2 102 ? -3.568  76.365 78.623  1.00 40.99  ? 72  PHE   B C   1 
ATOM   3414 O O   . PHE   B 2 102 ? -3.280  77.417 78.067  1.00 41.24  ? 72  PHE   B O   1 
ATOM   3415 C CB  . PHE   B 2 102 ? -4.746  74.508 77.362  1.00 40.69  ? 72  PHE   B CB  1 
ATOM   3416 C CG  . PHE   B 2 102 ? -5.461  75.451 76.420  1.00 42.03  ? 72  PHE   B CG  1 
ATOM   3417 C CD1 . PHE   B 2 102 ? -5.165  75.463 75.068  1.00 43.31  ? 72  PHE   B CD1 1 
ATOM   3418 C CD2 . PHE   B 2 102 ? -6.403  76.351 76.892  1.00 43.30  ? 72  PHE   B CD2 1 
ATOM   3419 C CE1 . PHE   B 2 102 ? -5.805  76.352 74.204  1.00 44.26  ? 72  PHE   B CE1 1 
ATOM   3420 C CE2 . PHE   B 2 102 ? -7.040  77.240 76.030  1.00 44.29  ? 72  PHE   B CE2 1 
ATOM   3421 C CZ  . PHE   B 2 102 ? -6.745  77.227 74.689  1.00 44.22  ? 72  PHE   B CZ  1 
ATOM   3422 N N   . TYR   B 2 103 ? -3.995  76.305 79.889  1.00 40.89  ? 73  TYR   B N   1 
ATOM   3423 C CA  . TYR   B 2 103 ? -4.205  77.522 80.660  1.00 41.31  ? 73  TYR   B CA  1 
ATOM   3424 C C   . TYR   B 2 103 ? -2.936  78.063 81.337  1.00 42.36  ? 73  TYR   B C   1 
ATOM   3425 O O   . TYR   B 2 103 ? -2.983  79.152 81.907  1.00 42.63  ? 73  TYR   B O   1 
ATOM   3426 C CB  . TYR   B 2 103 ? -5.353  77.357 81.624  1.00 41.25  ? 73  TYR   B CB  1 
ATOM   3427 C CG  . TYR   B 2 103 ? -6.640  77.171 80.861  1.00 42.15  ? 73  TYR   B CG  1 
ATOM   3428 C CD1 . TYR   B 2 103 ? -7.204  78.217 80.147  1.00 43.18  ? 73  TYR   B CD1 1 
ATOM   3429 C CD2 . TYR   B 2 103 ? -7.255  75.932 80.791  1.00 43.16  ? 73  TYR   B CD2 1 
ATOM   3430 C CE1 . TYR   B 2 103 ? -8.367  78.041 79.410  1.00 44.41  ? 73  TYR   B CE1 1 
ATOM   3431 C CE2 . TYR   B 2 103 ? -8.428  75.747 80.075  1.00 44.22  ? 73  TYR   B CE2 1 
ATOM   3432 C CZ  . TYR   B 2 103 ? -8.981  76.801 79.380  1.00 45.47  ? 73  TYR   B CZ  1 
ATOM   3433 O OH  . TYR   B 2 103 ? -10.134 76.603 78.657  1.00 47.26  ? 73  TYR   B OH  1 
ATOM   3434 N N   . ALA   B 2 104 ? -1.788  77.376 81.188  1.00 42.95  ? 74  ALA   B N   1 
ATOM   3435 C CA  . ALA   B 2 104 ? -0.493  77.901 81.617  1.00 43.70  ? 74  ALA   B CA  1 
ATOM   3436 C C   . ALA   B 2 104 ? -0.060  78.963 80.591  1.00 45.03  ? 74  ALA   B C   1 
ATOM   3437 O O   . ALA   B 2 104 ? 0.538   79.965 80.972  1.00 45.06  ? 74  ALA   B O   1 
ATOM   3438 C CB  . ALA   B 2 104 ? 0.544   76.801 81.668  1.00 43.60  ? 74  ALA   B CB  1 
ATOM   3439 N N   . ARG   B 2 105 ? -0.368  78.760 79.298  1.00 46.29  ? 75  ARG   B N   1 
ATOM   3440 C CA  . ARG   B 2 105 ? -0.024  79.736 78.276  1.00 48.49  ? 75  ARG   B CA  1 
ATOM   3441 C C   . ARG   B 2 105 ? -1.180  80.652 77.910  1.00 49.10  ? 75  ARG   B C   1 
ATOM   3442 O O   . ARG   B 2 105 ? -0.940  81.797 77.521  1.00 49.81  ? 75  ARG   B O   1 
ATOM   3443 C CB  . ARG   B 2 105 ? 0.574   79.056 77.030  1.00 51.77  ? 75  ARG   B CB  1 
ATOM   3444 C CG  . ARG   B 2 105 ? 2.065   78.729 77.209  1.00 58.23  ? 75  ARG   B CG  1 
ATOM   3445 C CD  . ARG   B 2 105 ? 2.595   77.750 76.182  1.00 64.54  ? 75  ARG   B CD  1 
ATOM   3446 N NE  . ARG   B 2 105 ? 2.585   78.323 74.835  1.00 70.72  ? 75  ARG   B NE  1 
ATOM   3447 C CZ  . ARG   B 2 105 ? 3.011   77.691 73.745  1.00 75.06  ? 75  ARG   B CZ  1 
ATOM   3448 N NH1 . ARG   B 2 105 ? 2.963   78.292 72.562  1.00 75.83  ? 75  ARG   B NH1 1 
ATOM   3449 N NH2 . ARG   B 2 105 ? 3.486   76.453 73.828  1.00 75.26  ? 75  ARG   B NH2 1 
ATOM   3450 N N   . TYR   B 2 106 ? -2.425  80.183 78.049  1.00 48.82  ? 76  TYR   B N   1 
ATOM   3451 C CA  . TYR   B 2 106 ? -3.574  80.982 77.641  1.00 49.33  ? 76  TYR   B CA  1 
ATOM   3452 C C   . TYR   B 2 106 ? -4.479  81.361 78.788  1.00 49.17  ? 76  TYR   B C   1 
ATOM   3453 O O   . TYR   B 2 106 ? -4.426  80.775 79.866  1.00 49.39  ? 76  TYR   B O   1 
ATOM   3454 C CB  . TYR   B 2 106 ? -4.346  80.299 76.497  1.00 49.97  ? 76  TYR   B CB  1 
ATOM   3455 C CG  . TYR   B 2 106 ? -3.440  80.091 75.309  1.00 51.82  ? 76  TYR   B CG  1 
ATOM   3456 C CD1 . TYR   B 2 106 ? -3.224  81.107 74.394  1.00 53.29  ? 76  TYR   B CD1 1 
ATOM   3457 C CD2 . TYR   B 2 106 ? -2.672  78.941 75.193  1.00 53.40  ? 76  TYR   B CD2 1 
ATOM   3458 C CE1 . TYR   B 2 106 ? -2.320  80.958 73.352  1.00 54.85  ? 76  TYR   B CE1 1 
ATOM   3459 C CE2 . TYR   B 2 106 ? -1.756  78.784 74.167  1.00 54.85  ? 76  TYR   B CE2 1 
ATOM   3460 C CZ  . TYR   B 2 106 ? -1.590  79.791 73.239  1.00 56.45  ? 76  TYR   B CZ  1 
ATOM   3461 O OH  . TYR   B 2 106 ? -0.659  79.637 72.239  1.00 59.35  ? 76  TYR   B OH  1 
ATOM   3462 N N   . SER   B 2 107 ? -5.260  82.413 78.571  1.00 48.50  ? 77  SER   B N   1 
ATOM   3463 C CA  . SER   B 2 107 ? -6.174  82.935 79.557  1.00 48.16  ? 77  SER   B CA  1 
ATOM   3464 C C   . SER   B 2 107 ? -7.467  82.122 79.584  1.00 47.65  ? 77  SER   B C   1 
ATOM   3465 O O   . SER   B 2 107 ? -7.883  81.583 78.559  1.00 47.74  ? 77  SER   B O   1 
ATOM   3466 C CB  . SER   B 2 107 ? -6.473  84.394 79.237  1.00 49.47  ? 77  SER   B CB  1 
ATOM   3467 O OG  . SER   B 2 107 ? -7.640  84.886 79.875  1.00 51.99  ? 77  SER   B OG  1 
ATOM   3468 N N   . LEU   B 2 108 ? -8.140  82.108 80.751  1.00 46.78  ? 78  LEU   B N   1 
ATOM   3469 C CA  . LEU   B 2 108 ? -9.426  81.448 80.962  1.00 46.13  ? 78  LEU   B CA  1 
ATOM   3470 C C   . LEU   B 2 108 ? -10.526 81.978 80.027  1.00 45.51  ? 78  LEU   B C   1 
ATOM   3471 O O   . LEU   B 2 108 ? -11.576 81.340 79.905  1.00 46.03  ? 78  LEU   B O   1 
ATOM   3472 C CB  . LEU   B 2 108 ? -9.860  81.548 82.442  1.00 46.20  ? 78  LEU   B CB  1 
ATOM   3473 C CG  . LEU   B 2 108 ? -9.013  80.716 83.430  1.00 47.90  ? 78  LEU   B CG  1 
ATOM   3474 C CD1 . LEU   B 2 108 ? -9.011  81.324 84.809  1.00 48.47  ? 78  LEU   B CD1 1 
ATOM   3475 C CD2 . LEU   B 2 108 ? -9.458  79.242 83.481  1.00 48.35  ? 78  LEU   B CD2 1 
ATOM   3476 N N   . LYS   B 2 109 ? -10.296 83.123 79.358  1.00 44.36  ? 79  LYS   B N   1 
ATOM   3477 C CA  . LYS   B 2 109 ? -11.285 83.661 78.437  1.00 44.11  ? 79  LYS   B CA  1 
ATOM   3478 C C   . LYS   B 2 109 ? -11.097 83.158 77.018  1.00 43.34  ? 79  LYS   B C   1 
ATOM   3479 O O   . LYS   B 2 109 ? -12.068 83.129 76.274  1.00 43.77  ? 79  LYS   B O   1 
ATOM   3480 C CB  . LYS   B 2 109 ? -11.348 85.197 78.476  1.00 46.29  ? 79  LYS   B CB  1 
ATOM   3481 C CG  . LYS   B 2 109 ? -10.148 85.883 77.857  1.00 50.80  ? 79  LYS   B CG  1 
ATOM   3482 C CD  . LYS   B 2 109 ? -10.418 87.319 77.524  1.00 55.73  ? 79  LYS   B CD  1 
ATOM   3483 C CE  . LYS   B 2 109 ? -9.112  87.995 77.206  1.00 61.28  ? 79  LYS   B CE  1 
ATOM   3484 N NZ  . LYS   B 2 109 ? -9.167  88.774 75.935  1.00 64.90  ? 79  LYS   B NZ  1 
ATOM   3485 N N   . SER   B 2 110 ? -9.873  82.740 76.634  1.00 42.24  ? 80  SER   B N   1 
ATOM   3486 C CA  . SER   B 2 110 ? -9.587  82.274 75.275  1.00 41.68  ? 80  SER   B CA  1 
ATOM   3487 C C   . SER   B 2 110 ? -10.559 81.165 74.823  1.00 40.73  ? 80  SER   B C   1 
ATOM   3488 O O   . SER   B 2 110 ? -11.319 81.362 73.881  1.00 40.61  ? 80  SER   B O   1 
ATOM   3489 C CB  . SER   B 2 110 ? -8.121  81.876 75.140  1.00 43.05  ? 80  SER   B CB  1 
ATOM   3490 O OG  . SER   B 2 110 ? -7.738  80.895 76.088  1.00 45.66  ? 80  SER   B OG  1 
ATOM   3491 N N   . ILE   B 2 111 ? -10.607 80.055 75.560  1.00 40.03  ? 81  ILE   B N   1 
ATOM   3492 C CA  . ILE   B 2 111 ? -11.564 78.972 75.344  1.00 39.51  ? 81  ILE   B CA  1 
ATOM   3493 C C   . ILE   B 2 111 ? -12.248 78.699 76.689  1.00 39.27  ? 81  ILE   B C   1 
ATOM   3494 O O   . ILE   B 2 111 ? -11.596 78.760 77.738  1.00 39.27  ? 81  ILE   B O   1 
ATOM   3495 C CB  . ILE   B 2 111 ? -10.913 77.695 74.734  1.00 39.53  ? 81  ILE   B CB  1 
ATOM   3496 C CG1 . ILE   B 2 111 ? -10.451 77.976 73.291  1.00 40.48  ? 81  ILE   B CG1 1 
ATOM   3497 C CG2 . ILE   B 2 111 ? -11.883 76.515 74.768  1.00 39.81  ? 81  ILE   B CG2 1 
ATOM   3498 C CD1 . ILE   B 2 111 ? -9.762  76.887 72.603  1.00 41.63  ? 81  ILE   B CD1 1 
ATOM   3499 N N   . ASP   B 2 112 ? -13.566 78.437 76.669  1.00 38.81  ? 82  ASP   B N   1 
ATOM   3500 C CA  . ASP   B 2 112 ? -14.318 78.118 77.877  1.00 38.78  ? 82  ASP   B CA  1 
ATOM   3501 C C   . ASP   B 2 112 ? -13.782 76.831 78.478  1.00 39.43  ? 82  ASP   B C   1 
ATOM   3502 O O   . ASP   B 2 112 ? -13.850 75.799 77.826  1.00 39.38  ? 82  ASP   B O   1 
ATOM   3503 C CB  . ASP   B 2 112 ? -15.805 77.930 77.537  1.00 39.47  ? 82  ASP   B CB  1 
ATOM   3504 C CG  . ASP   B 2 112 ? -16.700 77.612 78.728  1.00 43.12  ? 82  ASP   B CG  1 
ATOM   3505 O OD1 . ASP   B 2 112 ? -16.226 77.717 79.880  1.00 43.93  ? 82  ASP   B OD1 1 
ATOM   3506 O OD2 . ASP   B 2 112 ? -17.871 77.253 78.511  1.00 44.20  ? 82  ASP   B OD2 1 
ATOM   3507 N N   . PRO   B 2 113 ? -13.265 76.872 79.724  1.00 40.05  ? 83  PRO   B N   1 
ATOM   3508 C CA  . PRO   B 2 113 ? -12.785 75.631 80.368  1.00 40.17  ? 83  PRO   B CA  1 
ATOM   3509 C C   . PRO   B 2 113 ? -13.847 74.534 80.461  1.00 40.47  ? 83  PRO   B C   1 
ATOM   3510 O O   . PRO   B 2 113 ? -13.505 73.366 80.448  1.00 41.03  ? 83  PRO   B O   1 
ATOM   3511 C CB  . PRO   B 2 113 ? -12.340 76.098 81.759  1.00 40.83  ? 83  PRO   B CB  1 
ATOM   3512 C CG  . PRO   B 2 113 ? -12.997 77.437 81.966  1.00 41.26  ? 83  PRO   B CG  1 
ATOM   3513 C CD  . PRO   B 2 113 ? -13.106 78.045 80.610  1.00 39.68  ? 83  PRO   B CD  1 
ATOM   3514 N N   . VAL   B 2 114 ? -15.127 74.898 80.491  1.00 40.13  ? 84  VAL   B N   1 
ATOM   3515 C CA  . VAL   B 2 114 ? -16.248 73.961 80.504  1.00 40.32  ? 84  VAL   B CA  1 
ATOM   3516 C C   . VAL   B 2 114 ? -16.334 73.160 79.186  1.00 40.29  ? 84  VAL   B C   1 
ATOM   3517 O O   . VAL   B 2 114 ? -16.775 72.010 79.203  1.00 41.21  ? 84  VAL   B O   1 
ATOM   3518 C CB  . VAL   B 2 114 ? -17.553 74.702 80.873  1.00 41.27  ? 84  VAL   B CB  1 
ATOM   3519 C CG1 . VAL   B 2 114 ? -18.769 73.784 80.846  1.00 41.78  ? 84  VAL   B CG1 1 
ATOM   3520 C CG2 . VAL   B 2 114 ? -17.407 75.361 82.237  1.00 41.95  ? 84  VAL   B CG2 1 
ATOM   3521 N N   . LEU   B 2 115 ? -15.853 73.727 78.065  1.00 39.20  ? 85  LEU   B N   1 
ATOM   3522 C CA  . LEU   B 2 115 ? -15.754 73.030 76.773  1.00 38.88  ? 85  LEU   B CA  1 
ATOM   3523 C C   . LEU   B 2 115 ? -14.382 72.330 76.685  1.00 38.95  ? 85  LEU   B C   1 
ATOM   3524 O O   . LEU   B 2 115 ? -14.275 71.229 76.158  1.00 39.14  ? 85  LEU   B O   1 
ATOM   3525 C CB  . LEU   B 2 115 ? -15.912 74.024 75.608  1.00 38.95  ? 85  LEU   B CB  1 
ATOM   3526 C CG  . LEU   B 2 115 ? -15.578 73.522 74.195  1.00 40.32  ? 85  LEU   B CG  1 
ATOM   3527 C CD1 . LEU   B 2 115 ? -16.508 72.439 73.763  1.00 40.80  ? 85  LEU   B CD1 1 
ATOM   3528 C CD2 . LEU   B 2 115 ? -15.674 74.637 73.187  1.00 40.95  ? 85  LEU   B CD2 1 
ATOM   3529 N N   . MET   B 2 116 ? -13.334 72.982 77.208  1.00 38.71  ? 86  MET   B N   1 
ATOM   3530 C CA  . MET   B 2 116 ? -11.964 72.512 77.206  1.00 38.43  ? 86  MET   B CA  1 
ATOM   3531 C C   . MET   B 2 116 ? -11.776 71.209 77.982  1.00 38.70  ? 86  MET   B C   1 
ATOM   3532 O O   . MET   B 2 116 ? -11.171 70.286 77.445  1.00 39.20  ? 86  MET   B O   1 
ATOM   3533 C CB  . MET   B 2 116 ? -11.033 73.624 77.704  1.00 38.44  ? 86  MET   B CB  1 
ATOM   3534 C CG  . MET   B 2 116 ? -9.556  73.276 77.638  1.00 40.39  ? 86  MET   B CG  1 
ATOM   3535 S SD  . MET   B 2 116 ? -8.943  72.713 76.025  1.00 42.06  ? 86  MET   B SD  1 
ATOM   3536 C CE  . MET   B 2 116 ? -8.756  74.200 75.200  1.00 41.19  ? 86  MET   B CE  1 
ATOM   3537 N N   . ALA   B 2 117 ? -12.311 71.105 79.208  1.00 38.21  ? 87  ALA   B N   1 
ATOM   3538 C CA  . ALA   B 2 117 ? -12.176 69.894 80.032  1.00 38.16  ? 87  ALA   B CA  1 
ATOM   3539 C C   . ALA   B 2 117 ? -12.619 68.584 79.333  1.00 38.39  ? 87  ALA   B C   1 
ATOM   3540 O O   . ALA   B 2 117 ? -11.799 67.672 79.261  1.00 38.34  ? 87  ALA   B O   1 
ATOM   3541 C CB  . ALA   B 2 117 ? -12.882 70.068 81.369  1.00 38.08  ? 87  ALA   B CB  1 
ATOM   3542 N N   . PRO   B 2 118 ? -13.853 68.455 78.769  1.00 38.54  ? 88  PRO   B N   1 
ATOM   3543 C CA  . PRO   B 2 118 ? -14.203 67.204 78.061  1.00 38.28  ? 88  PRO   B CA  1 
ATOM   3544 C C   . PRO   B 2 118 ? -13.428 67.019 76.755  1.00 38.32  ? 88  PRO   B C   1 
ATOM   3545 O O   . PRO   B 2 118 ? -13.209 65.876 76.328  1.00 38.37  ? 88  PRO   B O   1 
ATOM   3546 C CB  . PRO   B 2 118 ? -15.703 67.341 77.810  1.00 39.05  ? 88  PRO   B CB  1 
ATOM   3547 C CG  . PRO   B 2 118 ? -15.950 68.813 77.792  1.00 39.66  ? 88  PRO   B CG  1 
ATOM   3548 C CD  . PRO   B 2 118 ? -14.977 69.419 78.750  1.00 38.08  ? 88  PRO   B CD  1 
ATOM   3549 N N   . THR   B 2 119 ? -12.970 68.138 76.127  1.00 37.82  ? 89  THR   B N   1 
ATOM   3550 C CA  . THR   B 2 119 ? -12.130 68.064 74.931  1.00 37.62  ? 89  THR   B CA  1 
ATOM   3551 C C   . THR   B 2 119 ? -10.821 67.373 75.303  1.00 37.86  ? 89  THR   B C   1 
ATOM   3552 O O   . THR   B 2 119 ? -10.420 66.425 74.622  1.00 38.57  ? 89  THR   B O   1 
ATOM   3553 C CB  . THR   B 2 119 ? -11.853 69.444 74.347  1.00 38.15  ? 89  THR   B CB  1 
ATOM   3554 O OG1 . THR   B 2 119 ? -13.083 70.054 73.968  1.00 39.51  ? 89  THR   B OG1 1 
ATOM   3555 C CG2 . THR   B 2 119 ? -10.944 69.373 73.151  1.00 37.85  ? 89  THR   B CG2 1 
ATOM   3556 N N   . CYS   B 2 120 ? -10.220 67.774 76.443  1.00 37.17  ? 90  CYS   B N   1 
ATOM   3557 C CA  . CYS   B 2 120 ? -9.000  67.167 76.951  1.00 37.57  ? 90  CYS   B CA  1 
ATOM   3558 C C   . CYS   B 2 120 ? -9.179  65.685 77.203  1.00 38.03  ? 90  CYS   B C   1 
ATOM   3559 O O   . CYS   B 2 120 ? -8.311  64.908 76.813  1.00 38.65  ? 90  CYS   B O   1 
ATOM   3560 C CB  . CYS   B 2 120 ? -8.506  67.885 78.197  1.00 38.50  ? 90  CYS   B CB  1 
ATOM   3561 S SG  . CYS   B 2 120 ? -7.779  69.508 77.868  1.00 42.86  ? 90  CYS   B SG  1 
ATOM   3562 N N   . VAL   B 2 121 ? -10.312 65.277 77.804  1.00 37.56  ? 91  VAL   B N   1 
ATOM   3563 C CA  . VAL   B 2 121 ? -10.604 63.863 78.068  1.00 37.42  ? 91  VAL   B CA  1 
ATOM   3564 C C   . VAL   B 2 121 ? -10.639 63.067 76.752  1.00 37.55  ? 91  VAL   B C   1 
ATOM   3565 O O   . VAL   B 2 121 ? -9.942  62.069 76.608  1.00 37.35  ? 91  VAL   B O   1 
ATOM   3566 C CB  . VAL   B 2 121 ? -11.905 63.705 78.907  1.00 37.74  ? 91  VAL   B CB  1 
ATOM   3567 C CG1 . VAL   B 2 121 ? -12.428 62.279 78.872  1.00 38.06  ? 91  VAL   B CG1 1 
ATOM   3568 C CG2 . VAL   B 2 121 ? -11.697 64.161 80.349  1.00 37.88  ? 91  VAL   B CG2 1 
ATOM   3569 N N   . PHE   B 2 122 ? -11.402 63.553 75.785  1.00 38.14  ? 92  PHE   B N   1 
ATOM   3570 C CA  . PHE   B 2 122 ? -11.566 62.967 74.456  1.00 39.26  ? 92  PHE   B CA  1 
ATOM   3571 C C   . PHE   B 2 122 ? -10.215 62.750 73.745  1.00 39.30  ? 92  PHE   B C   1 
ATOM   3572 O O   . PHE   B 2 122 ? -9.932  61.632 73.317  1.00 39.93  ? 92  PHE   B O   1 
ATOM   3573 C CB  . PHE   B 2 122 ? -12.513 63.871 73.647  1.00 40.01  ? 92  PHE   B CB  1 
ATOM   3574 C CG  . PHE   B 2 122 ? -12.651 63.648 72.161  1.00 41.07  ? 92  PHE   B CG  1 
ATOM   3575 C CD1 . PHE   B 2 122 ? -13.346 62.560 71.672  1.00 41.88  ? 92  PHE   B CD1 1 
ATOM   3576 C CD2 . PHE   B 2 122 ? -12.214 64.604 71.260  1.00 42.20  ? 92  PHE   B CD2 1 
ATOM   3577 C CE1 . PHE   B 2 122 ? -13.509 62.373 70.306  1.00 42.77  ? 92  PHE   B CE1 1 
ATOM   3578 C CE2 . PHE   B 2 122 ? -12.410 64.435 69.897  1.00 43.17  ? 92  PHE   B CE2 1 
ATOM   3579 C CZ  . PHE   B 2 122 ? -13.042 63.309 69.426  1.00 42.95  ? 92  PHE   B CZ  1 
ATOM   3580 N N   . LEU   B 2 123 ? -9.354  63.774 73.689  1.00 38.45  ? 93  LEU   B N   1 
ATOM   3581 C CA  . LEU   B 2 123 ? -8.033  63.636 73.077  1.00 37.98  ? 93  LEU   B CA  1 
ATOM   3582 C C   . LEU   B 2 123 ? -7.137  62.696 73.876  1.00 39.32  ? 93  LEU   B C   1 
ATOM   3583 O O   . LEU   B 2 123 ? -6.491  61.834 73.285  1.00 39.66  ? 93  LEU   B O   1 
ATOM   3584 C CB  . LEU   B 2 123 ? -7.362  65.003 72.947  1.00 36.85  ? 93  LEU   B CB  1 
ATOM   3585 C CG  . LEU   B 2 123 ? -6.013  65.036 72.263  1.00 36.17  ? 93  LEU   B CG  1 
ATOM   3586 C CD1 . LEU   B 2 123 ? -6.102  64.536 70.851  1.00 35.40  ? 93  LEU   B CD1 1 
ATOM   3587 C CD2 . LEU   B 2 123 ? -5.452  66.441 72.284  1.00 36.79  ? 93  LEU   B CD2 1 
ATOM   3588 N N   . ALA   B 2 124 ? -7.122  62.816 75.211  1.00 39.98  ? 94  ALA   B N   1 
ATOM   3589 C CA  . ALA   B 2 124 ? -6.283  61.956 76.041  1.00 41.36  ? 94  ALA   B CA  1 
ATOM   3590 C C   . ALA   B 2 124 ? -6.597  60.474 75.851  1.00 42.61  ? 94  ALA   B C   1 
ATOM   3591 O O   . ALA   B 2 124 ? -5.680  59.657 75.904  1.00 42.67  ? 94  ALA   B O   1 
ATOM   3592 C CB  . ALA   B 2 124 ? -6.404  62.341 77.506  1.00 41.75  ? 94  ALA   B CB  1 
ATOM   3593 N N   . SER   B 2 125 ? -7.880  60.124 75.589  1.00 43.10  ? 95  SER   B N   1 
ATOM   3594 C CA  . SER   B 2 125 ? -8.247  58.718 75.346  1.00 43.74  ? 95  SER   B CA  1 
ATOM   3595 C C   . SER   B 2 125 ? -7.734  58.224 74.010  1.00 43.29  ? 95  SER   B C   1 
ATOM   3596 O O   . SER   B 2 125 ? -7.525  57.032 73.864  1.00 43.60  ? 95  SER   B O   1 
ATOM   3597 C CB  . SER   B 2 125 ? -9.758  58.505 75.407  1.00 45.91  ? 95  SER   B CB  1 
ATOM   3598 O OG  . SER   B 2 125 ? -10.296 59.127 76.561  1.00 49.33  ? 95  SER   B OG  1 
ATOM   3599 N N   . LYS   B 2 126 ? -7.581  59.110 73.028  1.00 42.73  ? 96  LYS   B N   1 
ATOM   3600 C CA  . LYS   B 2 126 ? -7.089  58.724 71.721  1.00 43.13  ? 96  LYS   B CA  1 
ATOM   3601 C C   . LYS   B 2 126 ? -5.599  58.515 71.771  1.00 44.34  ? 96  LYS   B C   1 
ATOM   3602 O O   . LYS   B 2 126 ? -5.109  57.493 71.284  1.00 44.50  ? 96  LYS   B O   1 
ATOM   3603 C CB  . LYS   B 2 126 ? -7.494  59.745 70.663  1.00 43.91  ? 96  LYS   B CB  1 
ATOM   3604 C CG  . LYS   B 2 126 ? -9.001  59.827 70.526  1.00 46.71  ? 96  LYS   B CG  1 
ATOM   3605 C CD  . LYS   B 2 126 ? -9.415  60.406 69.205  1.00 49.14  ? 96  LYS   B CD  1 
ATOM   3606 C CE  . LYS   B 2 126 ? -9.579  61.883 69.283  1.00 51.26  ? 96  LYS   B CE  1 
ATOM   3607 N NZ  . LYS   B 2 126 ? -10.406 62.354 68.154  1.00 53.44  ? 96  LYS   B NZ  1 
ATOM   3608 N N   . VAL   B 2 127 ? -4.885  59.444 72.436  1.00 45.03  ? 97  VAL   B N   1 
ATOM   3609 C CA  . VAL   B 2 127 ? -3.436  59.399 72.633  1.00 45.82  ? 97  VAL   B CA  1 
ATOM   3610 C C   . VAL   B 2 127 ? -3.079  58.132 73.394  1.00 47.05  ? 97  VAL   B C   1 
ATOM   3611 O O   . VAL   B 2 127 ? -2.255  57.343 72.930  1.00 47.27  ? 97  VAL   B O   1 
ATOM   3612 C CB  . VAL   B 2 127 ? -2.935  60.670 73.376  1.00 45.98  ? 97  VAL   B CB  1 
ATOM   3613 C CG1 . VAL   B 2 127 ? -1.441  60.599 73.635  1.00 46.48  ? 97  VAL   B CG1 1 
ATOM   3614 C CG2 . VAL   B 2 127 ? -3.299  61.940 72.621  1.00 46.00  ? 97  VAL   B CG2 1 
ATOM   3615 N N   . GLU   B 2 128 ? -3.789  57.882 74.506  1.00 47.79  ? 98  GLU   B N   1 
ATOM   3616 C CA  . GLU   B 2 128 ? -3.554  56.732 75.373  1.00 48.65  ? 98  GLU   B CA  1 
ATOM   3617 C C   . GLU   B 2 128 ? -4.107  55.402 74.844  1.00 50.16  ? 98  GLU   B C   1 
ATOM   3618 O O   . GLU   B 2 128 ? -4.149  54.432 75.601  1.00 50.31  ? 98  GLU   B O   1 
ATOM   3619 C CB  . GLU   B 2 128 ? -4.079  57.020 76.785  1.00 49.42  ? 98  GLU   B CB  1 
ATOM   3620 C CG  . GLU   B 2 128 ? -3.450  58.245 77.436  1.00 49.60  ? 98  GLU   B CG  1 
ATOM   3621 C CD  . GLU   B 2 128 ? -2.078  58.020 78.035  1.00 51.86  ? 98  GLU   B CD  1 
ATOM   3622 O OE1 . GLU   B 2 128 ? -1.739  56.847 78.312  1.00 54.57  ? 98  GLU   B OE1 1 
ATOM   3623 O OE2 . GLU   B 2 128 ? -1.342  59.012 78.236  1.00 50.70  ? 98  GLU   B OE2 1 
ATOM   3624 N N   . GLU   B 2 129 ? -4.491  55.349 73.546  1.00 51.27  ? 99  GLU   B N   1 
ATOM   3625 C CA  . GLU   B 2 129 ? -4.969  54.153 72.832  1.00 52.88  ? 99  GLU   B CA  1 
ATOM   3626 C C   . GLU   B 2 129 ? -6.193  53.482 73.436  1.00 54.00  ? 99  GLU   B C   1 
ATOM   3627 O O   . GLU   B 2 129 ? -6.441  52.303 73.173  1.00 53.98  ? 99  GLU   B O   1 
ATOM   3628 C CB  . GLU   B 2 129 ? -3.845  53.121 72.668  1.00 55.84  ? 99  GLU   B CB  1 
ATOM   3629 C CG  . GLU   B 2 129 ? -2.679  53.617 71.832  1.00 62.54  ? 99  GLU   B CG  1 
ATOM   3630 C CD  . GLU   B 2 129 ? -2.398  52.752 70.621  1.00 71.46  ? 99  GLU   B CD  1 
ATOM   3631 O OE1 . GLU   B 2 129 ? -2.528  53.258 69.481  1.00 72.03  ? 99  GLU   B OE1 1 
ATOM   3632 O OE2 . GLU   B 2 129 ? -2.073  51.555 70.812  1.00 75.41  ? 99  GLU   B OE2 1 
ATOM   3633 N N   . PHE   B 2 130 ? -6.958  54.231 74.234  1.00 54.54  ? 100 PHE   B N   1 
ATOM   3634 C CA  . PHE   B 2 130 ? -8.170  53.747 74.861  1.00 55.30  ? 100 PHE   B CA  1 
ATOM   3635 C C   . PHE   B 2 130 ? -9.262  53.640 73.799  1.00 54.27  ? 100 PHE   B C   1 
ATOM   3636 O O   . PHE   B 2 130 ? -9.883  52.596 73.662  1.00 54.82  ? 100 PHE   B O   1 
ATOM   3637 C CB  . PHE   B 2 130 ? -8.590  54.698 75.992  1.00 56.71  ? 100 PHE   B CB  1 
ATOM   3638 C CG  . PHE   B 2 130 ? -8.715  54.020 77.331  1.00 59.28  ? 100 PHE   B CG  1 
ATOM   3639 C CD1 . PHE   B 2 130 ? -9.949  53.580 77.792  1.00 60.93  ? 100 PHE   B CD1 1 
ATOM   3640 C CD2 . PHE   B 2 130 ? -7.593  53.777 78.109  1.00 60.81  ? 100 PHE   B CD2 1 
ATOM   3641 C CE1 . PHE   B 2 130 ? -10.060 52.936 79.021  1.00 62.07  ? 100 PHE   B CE1 1 
ATOM   3642 C CE2 . PHE   B 2 130 ? -7.706  53.138 79.338  1.00 61.94  ? 100 PHE   B CE2 1 
ATOM   3643 C CZ  . PHE   B 2 130 ? -8.939  52.724 79.788  1.00 61.97  ? 100 PHE   B CZ  1 
ATOM   3644 N N   . GLY   B 2 131 ? -9.447  54.692 73.027  1.00 53.02  ? 101 GLY   B N   1 
ATOM   3645 C CA  . GLY   B 2 131 ? -10.447 54.710 71.977  1.00 52.58  ? 101 GLY   B CA  1 
ATOM   3646 C C   . GLY   B 2 131 ? -10.968 56.096 71.674  1.00 52.13  ? 101 GLY   B C   1 
ATOM   3647 O O   . GLY   B 2 131 ? -10.520 57.096 72.246  1.00 52.28  ? 101 GLY   B O   1 
ATOM   3648 N N   . VAL   B 2 132 ? -11.915 56.159 70.749  1.00 51.38  ? 102 VAL   B N   1 
ATOM   3649 C CA  . VAL   B 2 132 ? -12.560 57.404 70.392  1.00 51.04  ? 102 VAL   B CA  1 
ATOM   3650 C C   . VAL   B 2 132 ? -13.922 57.362 71.062  1.00 51.09  ? 102 VAL   B C   1 
ATOM   3651 O O   . VAL   B 2 132 ? -14.744 56.520 70.704  1.00 51.01  ? 102 VAL   B O   1 
ATOM   3652 C CB  . VAL   B 2 132 ? -12.714 57.551 68.868  1.00 51.14  ? 102 VAL   B CB  1 
ATOM   3653 C CG1 . VAL   B 2 132 ? -13.548 58.777 68.528  1.00 51.54  ? 102 VAL   B CG1 1 
ATOM   3654 C CG2 . VAL   B 2 132 ? -11.362 57.592 68.173  1.00 51.26  ? 102 VAL   B CG2 1 
ATOM   3655 N N   . VAL   B 2 133 ? -14.151 58.227 72.069  1.00 51.05  ? 103 VAL   B N   1 
ATOM   3656 C CA  . VAL   B 2 133 ? -15.438 58.283 72.754  1.00 51.02  ? 103 VAL   B CA  1 
ATOM   3657 C C   . VAL   B 2 133 ? -16.470 58.822 71.754  1.00 51.50  ? 103 VAL   B C   1 
ATOM   3658 O O   . VAL   B 2 133 ? -16.198 59.811 71.048  1.00 51.76  ? 103 VAL   B O   1 
ATOM   3659 C CB  . VAL   B 2 133 ? -15.376 59.157 74.017  1.00 51.28  ? 103 VAL   B CB  1 
ATOM   3660 C CG1 . VAL   B 2 133 ? -16.695 59.097 74.779  1.00 51.61  ? 103 VAL   B CG1 1 
ATOM   3661 C CG2 . VAL   B 2 133 ? -14.204 58.759 74.908  1.00 51.52  ? 103 VAL   B CG2 1 
ATOM   3662 N N   . SER   B 2 134 ? -17.613 58.124 71.627  1.00 51.11  ? 104 SER   B N   1 
ATOM   3663 C CA  . SER   B 2 134 ? -18.642 58.512 70.666  1.00 51.12  ? 104 SER   B CA  1 
ATOM   3664 C C   . SER   B 2 134 ? -19.217 59.884 70.937  1.00 51.00  ? 104 SER   B C   1 
ATOM   3665 O O   . SER   B 2 134 ? -19.221 60.336 72.075  1.00 50.94  ? 104 SER   B O   1 
ATOM   3666 C CB  . SER   B 2 134 ? -19.758 57.471 70.596  1.00 51.95  ? 104 SER   B CB  1 
ATOM   3667 O OG  . SER   B 2 134 ? -20.648 57.509 71.699  1.00 52.68  ? 104 SER   B OG  1 
ATOM   3668 N N   . ASN   B 2 135 ? -19.725 60.549 69.888  1.00 50.93  ? 105 ASN   B N   1 
ATOM   3669 C CA  . ASN   B 2 135 ? -20.333 61.880 69.982  1.00 51.22  ? 105 ASN   B CA  1 
ATOM   3670 C C   . ASN   B 2 135 ? -21.390 61.937 71.088  1.00 50.54  ? 105 ASN   B C   1 
ATOM   3671 O O   . ASN   B 2 135 ? -21.291 62.762 71.996  1.00 50.76  ? 105 ASN   B O   1 
ATOM   3672 C CB  . ASN   B 2 135 ? -20.970 62.277 68.636  1.00 53.13  ? 105 ASN   B CB  1 
ATOM   3673 C CG  . ASN   B 2 135 ? -20.035 62.252 67.458  1.00 56.93  ? 105 ASN   B CG  1 
ATOM   3674 O OD1 . ASN   B 2 135 ? -18.840 61.962 67.601  1.00 58.58  ? 105 ASN   B OD1 1 
ATOM   3675 N ND2 . ASN   B 2 135 ? -20.565 62.566 66.271  1.00 57.23  ? 105 ASN   B ND2 1 
ATOM   3676 N N   . THR   B 2 136 ? -22.323 60.974 71.061  1.00 49.51  ? 106 THR   B N   1 
ATOM   3677 C CA  . THR   B 2 136 ? -23.423 60.878 72.009  1.00 48.76  ? 106 THR   B CA  1 
ATOM   3678 C C   . THR   B 2 136 ? -22.926 60.644 73.417  1.00 47.68  ? 106 THR   B C   1 
ATOM   3679 O O   . THR   B 2 136 ? -23.339 61.349 74.328  1.00 47.75  ? 106 THR   B O   1 
ATOM   3680 C CB  . THR   B 2 136 ? -24.445 59.812 71.584  1.00 49.83  ? 106 THR   B CB  1 
ATOM   3681 O OG1 . THR   B 2 136 ? -24.557 59.746 70.162  1.00 50.72  ? 106 THR   B OG1 1 
ATOM   3682 C CG2 . THR   B 2 136 ? -25.817 60.052 72.198  1.00 50.37  ? 106 THR   B CG2 1 
ATOM   3683 N N   . ARG   B 2 137 ? -22.010 59.691 73.583  1.00 46.65  ? 107 ARG   B N   1 
ATOM   3684 C CA  . ARG   B 2 137 ? -21.442 59.306 74.868  1.00 46.16  ? 107 ARG   B CA  1 
ATOM   3685 C C   . ARG   B 2 137 ? -20.592 60.376 75.520  1.00 45.96  ? 107 ARG   B C   1 
ATOM   3686 O O   . ARG   B 2 137 ? -20.621 60.495 76.736  1.00 46.05  ? 107 ARG   B O   1 
ATOM   3687 C CB  . ARG   B 2 137 ? -20.621 58.034 74.706  1.00 46.97  ? 107 ARG   B CB  1 
ATOM   3688 C CG  . ARG   B 2 137 ? -20.514 57.218 75.966  1.00 48.75  ? 107 ARG   B CG  1 
ATOM   3689 C CD  . ARG   B 2 137 ? -19.660 56.007 75.719  1.00 50.09  ? 107 ARG   B CD  1 
ATOM   3690 N NE  . ARG   B 2 137 ? -18.857 55.699 76.893  1.00 51.62  ? 107 ARG   B NE  1 
ATOM   3691 C CZ  . ARG   B 2 137 ? -17.575 55.360 76.861  1.00 52.72  ? 107 ARG   B CZ  1 
ATOM   3692 N NH1 . ARG   B 2 137 ? -16.933 55.267 75.702  1.00 50.80  ? 107 ARG   B NH1 1 
ATOM   3693 N NH2 . ARG   B 2 137 ? -16.925 55.100 77.988  1.00 53.14  ? 107 ARG   B NH2 1 
ATOM   3694 N N   . LEU   B 2 138 ? -19.835 61.152 74.733  1.00 45.67  ? 108 LEU   B N   1 
ATOM   3695 C CA  . LEU   B 2 138 ? -18.978 62.209 75.273  1.00 45.58  ? 108 LEU   B CA  1 
ATOM   3696 C C   . LEU   B 2 138 ? -19.805 63.384 75.747  1.00 45.17  ? 108 LEU   B C   1 
ATOM   3697 O O   . LEU   B 2 138 ? -19.574 63.915 76.830  1.00 45.07  ? 108 LEU   B O   1 
ATOM   3698 C CB  . LEU   B 2 138 ? -17.937 62.678 74.239  1.00 45.87  ? 108 LEU   B CB  1 
ATOM   3699 C CG  . LEU   B 2 138 ? -17.011 63.793 74.727  1.00 48.00  ? 108 LEU   B CG  1 
ATOM   3700 C CD1 . LEU   B 2 138 ? -16.198 63.346 75.954  1.00 49.01  ? 108 LEU   B CD1 1 
ATOM   3701 C CD2 . LEU   B 2 138 ? -16.106 64.288 73.615  1.00 48.59  ? 108 LEU   B CD2 1 
ATOM   3702 N N   . ILE   B 2 139 ? -20.762 63.793 74.925  1.00 44.76  ? 109 ILE   B N   1 
ATOM   3703 C CA  . ILE   B 2 139 ? -21.632 64.901 75.244  1.00 44.65  ? 109 ILE   B CA  1 
ATOM   3704 C C   . ILE   B 2 139 ? -22.563 64.540 76.408  1.00 44.99  ? 109 ILE   B C   1 
ATOM   3705 O O   . ILE   B 2 139 ? -22.784 65.369 77.291  1.00 45.11  ? 109 ILE   B O   1 
ATOM   3706 C CB  . ILE   B 2 139 ? -22.370 65.321 73.956  1.00 44.68  ? 109 ILE   B CB  1 
ATOM   3707 C CG1 . ILE   B 2 139 ? -21.388 65.967 72.961  1.00 45.30  ? 109 ILE   B CG1 1 
ATOM   3708 C CG2 . ILE   B 2 139 ? -23.542 66.245 74.248  1.00 45.13  ? 109 ILE   B CG2 1 
ATOM   3709 C CD1 . ILE   B 2 139 ? -20.675 67.189 73.488  1.00 46.20  ? 109 ILE   B CD1 1 
ATOM   3710 N N   . ALA   B 2 140 ? -23.048 63.292 76.451  1.00 44.95  ? 110 ALA   B N   1 
ATOM   3711 C CA  . ALA   B 2 140 ? -23.923 62.856 77.528  1.00 45.62  ? 110 ALA   B CA  1 
ATOM   3712 C C   . ALA   B 2 140 ? -23.170 62.719 78.839  1.00 46.40  ? 110 ALA   B C   1 
ATOM   3713 O O   . ALA   B 2 140 ? -23.742 63.003 79.890  1.00 47.07  ? 110 ALA   B O   1 
ATOM   3714 C CB  . ALA   B 2 140 ? -24.605 61.554 77.169  1.00 45.82  ? 110 ALA   B CB  1 
ATOM   3715 N N   . ALA   B 2 141 ? -21.889 62.312 78.797  1.00 46.26  ? 111 ALA   B N   1 
ATOM   3716 C CA  . ALA   B 2 141 ? -21.087 62.225 80.024  1.00 46.34  ? 111 ALA   B CA  1 
ATOM   3717 C C   . ALA   B 2 141 ? -20.855 63.650 80.553  1.00 46.11  ? 111 ALA   B C   1 
ATOM   3718 O O   . ALA   B 2 141 ? -21.102 63.903 81.718  1.00 46.03  ? 111 ALA   B O   1 
ATOM   3719 C CB  . ALA   B 2 141 ? -19.758 61.515 79.766  1.00 46.32  ? 111 ALA   B CB  1 
ATOM   3720 N N   . ALA   B 2 142 ? -20.500 64.592 79.672  1.00 46.05  ? 112 ALA   B N   1 
ATOM   3721 C CA  . ALA   B 2 142 ? -20.310 65.996 80.033  1.00 46.56  ? 112 ALA   B CA  1 
ATOM   3722 C C   . ALA   B 2 142 ? -21.595 66.616 80.610  1.00 47.14  ? 112 ALA   B C   1 
ATOM   3723 O O   . ALA   B 2 142 ? -21.541 67.385 81.569  1.00 46.79  ? 112 ALA   B O   1 
ATOM   3724 C CB  . ALA   B 2 142 ? -19.857 66.783 78.814  1.00 46.39  ? 112 ALA   B CB  1 
ATOM   3725 N N   . THR   B 2 143 ? -22.747 66.273 80.026  1.00 47.68  ? 113 THR   B N   1 
ATOM   3726 C CA  . THR   B 2 143 ? -24.024 66.796 80.484  1.00 48.53  ? 113 THR   B CA  1 
ATOM   3727 C C   . THR   B 2 143 ? -24.372 66.225 81.861  1.00 49.62  ? 113 THR   B C   1 
ATOM   3728 O O   . THR   B 2 143 ? -24.603 66.998 82.794  1.00 49.82  ? 113 THR   B O   1 
ATOM   3729 C CB  . THR   B 2 143 ? -25.128 66.557 79.439  1.00 49.06  ? 113 THR   B CB  1 
ATOM   3730 O OG1 . THR   B 2 143 ? -24.784 67.212 78.216  1.00 49.69  ? 113 THR   B OG1 1 
ATOM   3731 C CG2 . THR   B 2 143 ? -26.466 67.067 79.903  1.00 49.22  ? 113 THR   B CG2 1 
ATOM   3732 N N   . SER   B 2 144 ? -24.358 64.887 82.001  1.00 49.89  ? 114 SER   B N   1 
ATOM   3733 C CA  . SER   B 2 144 ? -24.677 64.214 83.255  1.00 50.73  ? 114 SER   B CA  1 
ATOM   3734 C C   . SER   B 2 144 ? -23.734 64.564 84.402  1.00 51.17  ? 114 SER   B C   1 
ATOM   3735 O O   . SER   B 2 144 ? -24.195 64.728 85.529  1.00 51.37  ? 114 SER   B O   1 
ATOM   3736 C CB  . SER   B 2 144 ? -24.723 62.702 83.060  1.00 52.48  ? 114 SER   B CB  1 
ATOM   3737 O OG  . SER   B 2 144 ? -24.887 62.009 84.291  1.00 55.17  ? 114 SER   B OG  1 
ATOM   3738 N N   . VAL   B 2 145 ? -22.426 64.639 84.140  1.00 51.18  ? 115 VAL   B N   1 
ATOM   3739 C CA  . VAL   B 2 145 ? -21.462 64.957 85.181  1.00 51.80  ? 115 VAL   B CA  1 
ATOM   3740 C C   . VAL   B 2 145 ? -21.710 66.354 85.751  1.00 52.57  ? 115 VAL   B C   1 
ATOM   3741 O O   . VAL   B 2 145 ? -21.827 66.493 86.969  1.00 52.88  ? 115 VAL   B O   1 
ATOM   3742 C CB  . VAL   B 2 145 ? -20.002 64.726 84.721  1.00 52.47  ? 115 VAL   B CB  1 
ATOM   3743 C CG1 . VAL   B 2 145 ? -19.009 65.343 85.689  1.00 53.16  ? 115 VAL   B CG1 1 
ATOM   3744 C CG2 . VAL   B 2 145 ? -19.718 63.244 84.569  1.00 52.82  ? 115 VAL   B CG2 1 
ATOM   3745 N N   . LEU   B 2 146 ? -21.878 67.361 84.889  1.00 52.99  ? 116 LEU   B N   1 
ATOM   3746 C CA  . LEU   B 2 146 ? -22.128 68.716 85.377  1.00 54.15  ? 116 LEU   B CA  1 
ATOM   3747 C C   . LEU   B 2 146 ? -23.478 68.861 86.050  1.00 54.78  ? 116 LEU   B C   1 
ATOM   3748 O O   . LEU   B 2 146 ? -23.587 69.586 87.029  1.00 55.17  ? 116 LEU   B O   1 
ATOM   3749 C CB  . LEU   B 2 146 ? -21.928 69.770 84.285  1.00 54.73  ? 116 LEU   B CB  1 
ATOM   3750 C CG  . LEU   B 2 146 ? -20.559 69.734 83.597  1.00 56.74  ? 116 LEU   B CG  1 
ATOM   3751 C CD1 . LEU   B 2 146 ? -20.475 70.788 82.525  1.00 57.75  ? 116 LEU   B CD1 1 
ATOM   3752 C CD2 . LEU   B 2 146 ? -19.419 69.904 84.589  1.00 57.34  ? 116 LEU   B CD2 1 
ATOM   3753 N N   . LYS   B 2 147 ? -24.499 68.152 85.559  1.00 54.68  ? 117 LYS   B N   1 
ATOM   3754 C CA  . LYS   B 2 147 ? -25.844 68.207 86.137  1.00 54.53  ? 117 LYS   B CA  1 
ATOM   3755 C C   . LYS   B 2 147 ? -25.908 67.547 87.512  1.00 53.73  ? 117 LYS   B C   1 
ATOM   3756 O O   . LYS   B 2 147 ? -26.316 68.190 88.466  1.00 54.09  ? 117 LYS   B O   1 
ATOM   3757 C CB  . LYS   B 2 147 ? -26.867 67.579 85.170  1.00 56.74  ? 117 LYS   B CB  1 
ATOM   3758 C CG  . LYS   B 2 147 ? -28.285 67.474 85.699  1.00 61.57  ? 117 LYS   B CG  1 
ATOM   3759 C CD  . LYS   B 2 147 ? -29.230 67.034 84.582  1.00 66.87  ? 117 LYS   B CD  1 
ATOM   3760 C CE  . LYS   B 2 147 ? -30.682 66.968 85.009  1.00 71.07  ? 117 LYS   B CE  1 
ATOM   3761 N NZ  . LYS   B 2 147 ? -31.587 66.692 83.853  1.00 73.41  ? 117 LYS   B NZ  1 
ATOM   3762 N N   . THR   B 2 148 ? -25.469 66.299 87.629  1.00 52.88  ? 118 THR   B N   1 
ATOM   3763 C CA  . THR   B 2 148 ? -25.539 65.573 88.890  1.00 52.99  ? 118 THR   B CA  1 
ATOM   3764 C C   . THR   B 2 148 ? -24.504 65.972 89.935  1.00 52.56  ? 118 THR   B C   1 
ATOM   3765 O O   . THR   B 2 148 ? -24.856 66.165 91.097  1.00 53.10  ? 118 THR   B O   1 
ATOM   3766 C CB  . THR   B 2 148 ? -25.462 64.056 88.644  1.00 54.62  ? 118 THR   B CB  1 
ATOM   3767 O OG1 . THR   B 2 148 ? -24.163 63.742 88.129  1.00 55.91  ? 118 THR   B OG1 1 
ATOM   3768 C CG2 . THR   B 2 148 ? -26.552 63.554 87.703  1.00 54.82  ? 118 THR   B CG2 1 
ATOM   3769 N N   . ARG   B 2 149 ? -23.232 66.068 89.544  1.00 51.36  ? 119 ARG   B N   1 
ATOM   3770 C CA  . ARG   B 2 149 ? -22.161 66.298 90.499  1.00 50.30  ? 119 ARG   B CA  1 
ATOM   3771 C C   . ARG   B 2 149 ? -21.723 67.738 90.654  1.00 48.50  ? 119 ARG   B C   1 
ATOM   3772 O O   . ARG   B 2 149 ? -21.180 68.073 91.700  1.00 48.02  ? 119 ARG   B O   1 
ATOM   3773 C CB  . ARG   B 2 149 ? -20.967 65.397 90.150  1.00 51.90  ? 119 ARG   B CB  1 
ATOM   3774 C CG  . ARG   B 2 149 ? -21.367 63.925 90.218  1.00 56.15  ? 119 ARG   B CG  1 
ATOM   3775 C CD  . ARG   B 2 149 ? -20.429 62.984 89.484  1.00 60.05  ? 119 ARG   B CD  1 
ATOM   3776 N NE  . ARG   B 2 149 ? -19.230 62.714 90.275  1.00 63.38  ? 119 ARG   B NE  1 
ATOM   3777 C CZ  . ARG   B 2 149 ? -18.288 61.838 89.942  1.00 65.56  ? 119 ARG   B CZ  1 
ATOM   3778 N NH1 . ARG   B 2 149 ? -18.396 61.127 88.823  1.00 65.27  ? 119 ARG   B NH1 1 
ATOM   3779 N NH2 . ARG   B 2 149 ? -17.222 61.675 90.718  1.00 65.32  ? 119 ARG   B NH2 1 
ATOM   3780 N N   . PHE   B 2 150 ? -21.959 68.590 89.658  1.00 47.79  ? 120 PHE   B N   1 
ATOM   3781 C CA  . PHE   B 2 150 ? -21.488 69.974 89.728  1.00 47.70  ? 120 PHE   B CA  1 
ATOM   3782 C C   . PHE   B 2 150 ? -22.592 71.022 89.617  1.00 47.92  ? 120 PHE   B C   1 
ATOM   3783 O O   . PHE   B 2 150 ? -22.330 72.112 89.120  1.00 47.90  ? 120 PHE   B O   1 
ATOM   3784 C CB  . PHE   B 2 150 ? -20.395 70.208 88.667  1.00 47.17  ? 120 PHE   B CB  1 
ATOM   3785 C CG  . PHE   B 2 150 ? -19.168 69.351 88.871  1.00 47.25  ? 120 PHE   B CG  1 
ATOM   3786 C CD1 . PHE   B 2 150 ? -19.068 68.104 88.289  1.00 47.70  ? 120 PHE   B CD1 1 
ATOM   3787 C CD2 . PHE   B 2 150 ? -18.132 69.777 89.680  1.00 47.83  ? 120 PHE   B CD2 1 
ATOM   3788 C CE1 . PHE   B 2 150 ? -17.965 67.296 88.530  1.00 48.12  ? 120 PHE   B CE1 1 
ATOM   3789 C CE2 . PHE   B 2 150 ? -17.014 68.981 89.888  1.00 48.18  ? 120 PHE   B CE2 1 
ATOM   3790 C CZ  . PHE   B 2 150 ? -16.948 67.740 89.326  1.00 47.84  ? 120 PHE   B CZ  1 
ATOM   3791 N N   . SER   B 2 151 ? -23.820 70.705 90.068  1.00 47.99  ? 121 SER   B N   1 
ATOM   3792 C CA  . SER   B 2 151 ? -24.960 71.635 89.962  1.00 48.35  ? 121 SER   B CA  1 
ATOM   3793 C C   . SER   B 2 151 ? -24.828 72.882 90.826  1.00 48.31  ? 121 SER   B C   1 
ATOM   3794 O O   . SER   B 2 151 ? -25.441 73.910 90.513  1.00 48.84  ? 121 SER   B O   1 
ATOM   3795 C CB  . SER   B 2 151 ? -26.286 70.931 90.236  1.00 49.77  ? 121 SER   B CB  1 
ATOM   3796 O OG  . SER   B 2 151 ? -26.184 70.059 91.348  1.00 52.02  ? 121 SER   B OG  1 
ATOM   3797 N N   . TYR   B 2 152 ? -24.005 72.809 91.888  1.00 47.45  ? 122 TYR   B N   1 
ATOM   3798 C CA  . TYR   B 2 152 ? -23.733 73.952 92.745  1.00 47.04  ? 122 TYR   B CA  1 
ATOM   3799 C C   . TYR   B 2 152 ? -22.977 75.066 91.985  1.00 48.59  ? 122 TYR   B C   1 
ATOM   3800 O O   . TYR   B 2 152 ? -23.108 76.249 92.326  1.00 48.98  ? 122 TYR   B O   1 
ATOM   3801 C CB  . TYR   B 2 152 ? -22.953 73.507 93.986  1.00 45.77  ? 122 TYR   B CB  1 
ATOM   3802 C CG  . TYR   B 2 152 ? -21.623 72.863 93.674  1.00 45.17  ? 122 TYR   B CG  1 
ATOM   3803 C CD1 . TYR   B 2 152 ? -20.507 73.635 93.370  1.00 45.44  ? 122 TYR   B CD1 1 
ATOM   3804 C CD2 . TYR   B 2 152 ? -21.461 71.489 93.746  1.00 45.48  ? 122 TYR   B CD2 1 
ATOM   3805 C CE1 . TYR   B 2 152 ? -19.280 73.053 93.086  1.00 45.82  ? 122 TYR   B CE1 1 
ATOM   3806 C CE2 . TYR   B 2 152 ? -20.235 70.893 93.466  1.00 46.02  ? 122 TYR   B CE2 1 
ATOM   3807 C CZ  . TYR   B 2 152 ? -19.148 71.681 93.134  1.00 46.38  ? 122 TYR   B CZ  1 
ATOM   3808 O OH  . TYR   B 2 152 ? -17.935 71.112 92.863  1.00 47.06  ? 122 TYR   B OH  1 
ATOM   3809 N N   . ALA   B 2 153 ? -22.175 74.688 90.965  1.00 49.18  ? 123 ALA   B N   1 
ATOM   3810 C CA  . ALA   B 2 153 ? -21.397 75.639 90.177  1.00 50.22  ? 123 ALA   B CA  1 
ATOM   3811 C C   . ALA   B 2 153 ? -22.000 75.906 88.797  1.00 51.22  ? 123 ALA   B C   1 
ATOM   3812 O O   . ALA   B 2 153 ? -21.730 76.951 88.213  1.00 51.35  ? 123 ALA   B O   1 
ATOM   3813 C CB  . ALA   B 2 153 ? -19.956 75.177 90.056  1.00 50.17  ? 123 ALA   B CB  1 
ATOM   3814 N N   . PHE   B 2 154 ? -22.848 75.001 88.295  1.00 51.88  ? 124 PHE   B N   1 
ATOM   3815 C CA  . PHE   B 2 154 ? -23.479 75.181 86.992  1.00 53.06  ? 124 PHE   B CA  1 
ATOM   3816 C C   . PHE   B 2 154 ? -24.977 75.001 87.072  1.00 54.34  ? 124 PHE   B C   1 
ATOM   3817 O O   . PHE   B 2 154 ? -25.471 73.873 87.085  1.00 54.48  ? 124 PHE   B O   1 
ATOM   3818 C CB  . PHE   B 2 154 ? -22.905 74.217 85.939  1.00 52.93  ? 124 PHE   B CB  1 
ATOM   3819 C CG  . PHE   B 2 154 ? -21.408 74.283 85.795  1.00 53.50  ? 124 PHE   B CG  1 
ATOM   3820 C CD1 . PHE   B 2 154 ? -20.802 75.386 85.233  1.00 54.22  ? 124 PHE   B CD1 1 
ATOM   3821 C CD2 . PHE   B 2 154 ? -20.608 73.242 86.229  1.00 54.34  ? 124 PHE   B CD2 1 
ATOM   3822 C CE1 . PHE   B 2 154 ? -19.423 75.456 85.123  1.00 55.03  ? 124 PHE   B CE1 1 
ATOM   3823 C CE2 . PHE   B 2 154 ? -19.229 73.307 86.102  1.00 55.02  ? 124 PHE   B CE2 1 
ATOM   3824 C CZ  . PHE   B 2 154 ? -18.644 74.408 85.542  1.00 54.79  ? 124 PHE   B CZ  1 
ATOM   3825 N N   . PRO   B 2 155 ? -25.728 76.105 87.064  1.00 55.24  ? 125 PRO   B N   1 
ATOM   3826 C CA  . PRO   B 2 155 ? -27.196 75.985 87.091  1.00 55.89  ? 125 PRO   B CA  1 
ATOM   3827 C C   . PRO   B 2 155 ? -27.791 75.488 85.762  1.00 56.14  ? 125 PRO   B C   1 
ATOM   3828 O O   . PRO   B 2 155 ? -28.790 74.767 85.763  1.00 55.95  ? 125 PRO   B O   1 
ATOM   3829 C CB  . PRO   B 2 155 ? -27.654 77.409 87.416  1.00 56.73  ? 125 PRO   B CB  1 
ATOM   3830 C CG  . PRO   B 2 155 ? -26.548 78.291 86.902  1.00 56.98  ? 125 PRO   B CG  1 
ATOM   3831 C CD  . PRO   B 2 155 ? -25.283 77.514 87.054  1.00 55.05  ? 125 PRO   B CD  1 
ATOM   3832 N N   . LYS   B 2 156 ? -27.163 75.867 84.628  1.00 56.22  ? 126 LYS   B N   1 
ATOM   3833 C CA  . LYS   B 2 156 ? -27.623 75.486 83.292  1.00 56.65  ? 126 LYS   B CA  1 
ATOM   3834 C C   . LYS   B 2 156 ? -27.077 74.119 82.849  1.00 56.67  ? 126 LYS   B C   1 
ATOM   3835 O O   . LYS   B 2 156 ? -26.042 73.663 83.339  1.00 56.84  ? 126 LYS   B O   1 
ATOM   3836 C CB  . LYS   B 2 156 ? -27.207 76.551 82.258  1.00 58.71  ? 126 LYS   B CB  1 
ATOM   3837 C CG  . LYS   B 2 156 ? -27.543 77.987 82.645  1.00 63.75  ? 126 LYS   B CG  1 
ATOM   3838 C CD  . LYS   B 2 156 ? -26.884 79.002 81.685  1.00 69.31  ? 126 LYS   B CD  1 
ATOM   3839 C CE  . LYS   B 2 156 ? -26.590 80.342 82.351  1.00 73.90  ? 126 LYS   B CE  1 
ATOM   3840 N NZ  . LYS   B 2 156 ? -25.937 81.329 81.436  1.00 76.10  ? 126 LYS   B NZ  1 
ATOM   3841 N N   . GLU   B 2 157 ? -27.761 73.487 81.887  1.00 56.21  ? 127 GLU   B N   1 
ATOM   3842 C CA  . GLU   B 2 157 ? -27.342 72.221 81.279  1.00 56.08  ? 127 GLU   B CA  1 
ATOM   3843 C C   . GLU   B 2 157 ? -26.058 72.459 80.417  1.00 54.48  ? 127 GLU   B C   1 
ATOM   3844 O O   . GLU   B 2 157 ? -25.814 73.581 79.967  1.00 54.60  ? 127 GLU   B O   1 
ATOM   3845 C CB  . GLU   B 2 157 ? -28.494 71.705 80.382  1.00 59.51  ? 127 GLU   B CB  1 
ATOM   3846 C CG  . GLU   B 2 157 ? -28.490 70.208 80.112  1.00 66.30  ? 127 GLU   B CG  1 
ATOM   3847 C CD  . GLU   B 2 157 ? -29.265 69.779 78.875  1.00 75.35  ? 127 GLU   B CD  1 
ATOM   3848 O OE1 . GLU   B 2 157 ? -29.205 70.502 77.851  1.00 76.96  ? 127 GLU   B OE1 1 
ATOM   3849 O OE2 . GLU   B 2 157 ? -29.926 68.714 78.924  1.00 78.27  ? 127 GLU   B OE2 1 
ATOM   3850 N N   . PHE   B 2 158 ? -25.253 71.410 80.168  1.00 52.70  ? 128 PHE   B N   1 
ATOM   3851 C CA  . PHE   B 2 158 ? -24.043 71.526 79.338  1.00 51.47  ? 128 PHE   B CA  1 
ATOM   3852 C C   . PHE   B 2 158 ? -24.436 71.984 77.935  1.00 51.25  ? 128 PHE   B C   1 
ATOM   3853 O O   . PHE   B 2 158 ? -25.252 71.338 77.275  1.00 51.87  ? 128 PHE   B O   1 
ATOM   3854 C CB  . PHE   B 2 158 ? -23.293 70.190 79.286  1.00 50.36  ? 128 PHE   B CB  1 
ATOM   3855 C CG  . PHE   B 2 158 ? -22.027 70.200 78.464  1.00 49.71  ? 128 PHE   B CG  1 
ATOM   3856 C CD1 . PHE   B 2 158 ? -20.882 70.813 78.936  1.00 49.63  ? 128 PHE   B CD1 1 
ATOM   3857 C CD2 . PHE   B 2 158 ? -21.967 69.546 77.246  1.00 50.02  ? 128 PHE   B CD2 1 
ATOM   3858 C CE1 . PHE   B 2 158 ? -19.709 70.783 78.202  1.00 49.97  ? 128 PHE   B CE1 1 
ATOM   3859 C CE2 . PHE   B 2 158 ? -20.790 69.522 76.513  1.00 50.36  ? 128 PHE   B CE2 1 
ATOM   3860 C CZ  . PHE   B 2 158 ? -19.668 70.136 76.999  1.00 49.91  ? 128 PHE   B CZ  1 
ATOM   3861 N N   . PRO   B 2 159 ? -23.944 73.154 77.507  1.00 50.37  ? 129 PRO   B N   1 
ATOM   3862 C CA  . PRO   B 2 159 ? -24.429 73.731 76.248  1.00 50.06  ? 129 PRO   B CA  1 
ATOM   3863 C C   . PRO   B 2 159 ? -23.744 73.337 74.953  1.00 50.23  ? 129 PRO   B C   1 
ATOM   3864 O O   . PRO   B 2 159 ? -24.240 73.703 73.883  1.00 50.80  ? 129 PRO   B O   1 
ATOM   3865 C CB  . PRO   B 2 159 ? -24.238 75.221 76.481  1.00 50.54  ? 129 PRO   B CB  1 
ATOM   3866 C CG  . PRO   B 2 159 ? -23.002 75.286 77.308  1.00 51.02  ? 129 PRO   B CG  1 
ATOM   3867 C CD  . PRO   B 2 159 ? -23.044 74.084 78.217  1.00 49.62  ? 129 PRO   B CD  1 
ATOM   3868 N N   . TYR   B 2 160 ? -22.592 72.672 75.028  1.00 49.62  ? 130 TYR   B N   1 
ATOM   3869 C CA  . TYR   B 2 160 ? -21.824 72.363 73.828  1.00 49.46  ? 130 TYR   B CA  1 
ATOM   3870 C C   . TYR   B 2 160 ? -22.230 71.072 73.139  1.00 49.63  ? 130 TYR   B C   1 
ATOM   3871 O O   . TYR   B 2 160 ? -22.745 70.152 73.770  1.00 49.42  ? 130 TYR   B O   1 
ATOM   3872 C CB  . TYR   B 2 160 ? -20.324 72.384 74.126  1.00 49.01  ? 130 TYR   B CB  1 
ATOM   3873 C CG  . TYR   B 2 160 ? -19.906 73.722 74.673  1.00 49.56  ? 130 TYR   B CG  1 
ATOM   3874 C CD1 . TYR   B 2 160 ? -19.868 74.843 73.858  1.00 50.39  ? 130 TYR   B CD1 1 
ATOM   3875 C CD2 . TYR   B 2 160 ? -19.663 73.896 76.029  1.00 50.23  ? 130 TYR   B CD2 1 
ATOM   3876 C CE1 . TYR   B 2 160 ? -19.522 76.088 74.361  1.00 51.06  ? 130 TYR   B CE1 1 
ATOM   3877 C CE2 . TYR   B 2 160 ? -19.329 75.140 76.548  1.00 50.91  ? 130 TYR   B CE2 1 
ATOM   3878 C CZ  . TYR   B 2 160 ? -19.261 76.235 75.709  1.00 51.78  ? 130 TYR   B CZ  1 
ATOM   3879 O OH  . TYR   B 2 160 ? -18.957 77.482 76.190  1.00 53.05  ? 130 TYR   B OH  1 
ATOM   3880 N N   . ARG   B 2 161 ? -22.017 71.046 71.824  1.00 49.90  ? 131 ARG   B N   1 
ATOM   3881 C CA  . ARG   B 2 161 ? -22.267 69.920 70.942  1.00 51.06  ? 131 ARG   B CA  1 
ATOM   3882 C C   . ARG   B 2 161 ? -20.931 69.373 70.421  1.00 51.25  ? 131 ARG   B C   1 
ATOM   3883 O O   . ARG   B 2 161 ? -19.895 70.030 70.545  1.00 51.26  ? 131 ARG   B O   1 
ATOM   3884 C CB  . ARG   B 2 161 ? -23.155 70.349 69.770  1.00 53.73  ? 131 ARG   B CB  1 
ATOM   3885 C CG  . ARG   B 2 161 ? -24.634 70.257 70.070  1.00 59.25  ? 131 ARG   B CG  1 
ATOM   3886 C CD  . ARG   B 2 161 ? -25.406 71.216 69.190  1.00 65.24  ? 131 ARG   B CD  1 
ATOM   3887 N NE  . ARG   B 2 161 ? -25.089 72.613 69.499  1.00 70.68  ? 131 ARG   B NE  1 
ATOM   3888 C CZ  . ARG   B 2 161 ? -25.688 73.326 70.453  1.00 75.28  ? 131 ARG   B CZ  1 
ATOM   3889 N NH1 . ARG   B 2 161 ? -26.638 72.779 71.206  1.00 75.63  ? 131 ARG   B NH1 1 
ATOM   3890 N NH2 . ARG   B 2 161 ? -25.337 74.586 70.667  1.00 76.26  ? 131 ARG   B NH2 1 
ATOM   3891 N N   . MET   B 2 162 ? -20.953 68.180 69.814  1.00 51.09  ? 132 MET   B N   1 
ATOM   3892 C CA  . MET   B 2 162 ? -19.737 67.560 69.309  1.00 51.14  ? 132 MET   B CA  1 
ATOM   3893 C C   . MET   B 2 162 ? -18.959 68.431 68.337  1.00 51.80  ? 132 MET   B C   1 
ATOM   3894 O O   . MET   B 2 162 ? -17.737 68.295 68.275  1.00 52.46  ? 132 MET   B O   1 
ATOM   3895 C CB  . MET   B 2 162 ? -20.004 66.175 68.706  1.00 50.64  ? 132 MET   B CB  1 
ATOM   3896 C CG  . MET   B 2 162 ? -18.777 65.316 68.663  1.00 50.15  ? 132 MET   B CG  1 
ATOM   3897 S SD  . MET   B 2 162 ? -18.184 64.948 70.324  1.00 46.68  ? 132 MET   B SD  1 
ATOM   3898 C CE  . MET   B 2 162 ? -16.589 64.339 69.937  1.00 43.72  ? 132 MET   B CE  1 
ATOM   3899 N N   . ASN   B 2 163 ? -19.630 69.337 67.614  1.00 51.64  ? 133 ASN   B N   1 
ATOM   3900 C CA  . ASN   B 2 163 ? -18.903 70.223 66.699  1.00 52.41  ? 133 ASN   B CA  1 
ATOM   3901 C C   . ASN   B 2 163 ? -17.987 71.187 67.453  1.00 51.58  ? 133 ASN   B C   1 
ATOM   3902 O O   . ASN   B 2 163 ? -16.913 71.521 66.958  1.00 51.76  ? 133 ASN   B O   1 
ATOM   3903 C CB  . ASN   B 2 163 ? -19.826 70.951 65.702  1.00 55.20  ? 133 ASN   B CB  1 
ATOM   3904 C CG  . ASN   B 2 163 ? -21.108 71.505 66.279  1.00 60.88  ? 133 ASN   B CG  1 
ATOM   3905 O OD1 . ASN   B 2 163 ? -22.085 70.764 66.517  1.00 62.91  ? 133 ASN   B OD1 1 
ATOM   3906 N ND2 . ASN   B 2 163 ? -21.144 72.832 66.485  1.00 62.02  ? 133 ASN   B ND2 1 
ATOM   3907 N N   . HIS   B 2 164 ? -18.391 71.589 68.668  1.00 50.50  ? 134 HIS   B N   1 
ATOM   3908 C CA  . HIS   B 2 164 ? -17.629 72.485 69.522  1.00 49.98  ? 134 HIS   B CA  1 
ATOM   3909 C C   . HIS   B 2 164 ? -16.415 71.778 70.121  1.00 49.08  ? 134 HIS   B C   1 
ATOM   3910 O O   . HIS   B 2 164 ? -15.345 72.369 70.208  1.00 49.19  ? 134 HIS   B O   1 
ATOM   3911 C CB  . HIS   B 2 164 ? -18.533 73.052 70.625  1.00 50.85  ? 134 HIS   B CB  1 
ATOM   3912 C CG  . HIS   B 2 164 ? -19.727 73.781 70.083  1.00 53.24  ? 134 HIS   B CG  1 
ATOM   3913 N ND1 . HIS   B 2 164 ? -20.995 73.586 70.607  1.00 55.18  ? 134 HIS   B ND1 1 
ATOM   3914 C CD2 . HIS   B 2 164 ? -19.811 74.656 69.053  1.00 53.98  ? 134 HIS   B CD2 1 
ATOM   3915 C CE1 . HIS   B 2 164 ? -21.799 74.358 69.893  1.00 55.33  ? 134 HIS   B CE1 1 
ATOM   3916 N NE2 . HIS   B 2 164 ? -21.134 75.016 68.945  1.00 54.92  ? 134 HIS   B NE2 1 
ATOM   3917 N N   . ILE   B 2 165 ? -16.578 70.513 70.511  1.00 48.14  ? 135 ILE   B N   1 
ATOM   3918 C CA  . ILE   B 2 165 ? -15.521 69.695 71.095  1.00 47.71  ? 135 ILE   B CA  1 
ATOM   3919 C C   . ILE   B 2 165 ? -14.450 69.390 70.043  1.00 47.80  ? 135 ILE   B C   1 
ATOM   3920 O O   . ILE   B 2 165 ? -13.256 69.473 70.329  1.00 47.73  ? 135 ILE   B O   1 
ATOM   3921 C CB  . ILE   B 2 165 ? -16.143 68.394 71.629  1.00 47.72  ? 135 ILE   B CB  1 
ATOM   3922 C CG1 . ILE   B 2 165 ? -17.249 68.675 72.677  1.00 48.29  ? 135 ILE   B CG1 1 
ATOM   3923 C CG2 . ILE   B 2 165 ? -15.071 67.440 72.123  1.00 48.31  ? 135 ILE   B CG2 1 
ATOM   3924 C CD1 . ILE   B 2 165 ? -16.830 68.838 74.143  1.00 49.53  ? 135 ILE   B CD1 1 
ATOM   3925 N N   . LEU   B 2 166 ? -14.881 69.037 68.821  1.00 47.74  ? 136 LEU   B N   1 
ATOM   3926 C CA  . LEU   B 2 166 ? -13.969 68.749 67.710  1.00 47.85  ? 136 LEU   B CA  1 
ATOM   3927 C C   . LEU   B 2 166 ? -13.207 70.007 67.294  1.00 48.35  ? 136 LEU   B C   1 
ATOM   3928 O O   . LEU   B 2 166 ? -12.065 69.903 66.850  1.00 48.99  ? 136 LEU   B O   1 
ATOM   3929 C CB  . LEU   B 2 166 ? -14.732 68.187 66.495  1.00 47.60  ? 136 LEU   B CB  1 
ATOM   3930 C CG  . LEU   B 2 166 ? -15.360 66.796 66.636  1.00 48.33  ? 136 LEU   B CG  1 
ATOM   3931 C CD1 . LEU   B 2 166 ? -16.118 66.409 65.372  1.00 48.20  ? 136 LEU   B CD1 1 
ATOM   3932 C CD2 . LEU   B 2 166 ? -14.318 65.745 66.994  1.00 48.66  ? 136 LEU   B CD2 1 
ATOM   3933 N N   . GLU   B 2 167 ? -13.846 71.184 67.403  1.00 48.00  ? 137 GLU   B N   1 
ATOM   3934 C CA  . GLU   B 2 167 ? -13.247 72.467 67.050  1.00 48.16  ? 137 GLU   B CA  1 
ATOM   3935 C C   . GLU   B 2 167 ? -12.167 72.789 68.071  1.00 46.30  ? 137 GLU   B C   1 
ATOM   3936 O O   . GLU   B 2 167 ? -11.015 72.941 67.698  1.00 46.29  ? 137 GLU   B O   1 
ATOM   3937 C CB  . GLU   B 2 167 ? -14.328 73.570 66.989  1.00 52.68  ? 137 GLU   B CB  1 
ATOM   3938 C CG  . GLU   B 2 167 ? -13.780 74.966 66.729  1.00 61.80  ? 137 GLU   B CG  1 
ATOM   3939 C CD  . GLU   B 2 167 ? -14.565 76.091 67.387  1.00 71.48  ? 137 GLU   B CD  1 
ATOM   3940 O OE1 . GLU   B 2 167 ? -15.367 75.796 68.306  1.00 73.75  ? 137 GLU   B OE1 1 
ATOM   3941 O OE2 . GLU   B 2 167 ? -14.369 77.267 66.990  1.00 73.25  ? 137 GLU   B OE2 1 
ATOM   3942 N N   . CYS   B 2 168 ? -12.529 72.793 69.362  1.00 44.72  ? 138 CYS   B N   1 
ATOM   3943 C CA  . CYS   B 2 168 ? -11.641 73.004 70.500  1.00 43.66  ? 138 CYS   B CA  1 
ATOM   3944 C C   . CYS   B 2 168 ? -10.429 72.044 70.457  1.00 44.10  ? 138 CYS   B C   1 
ATOM   3945 O O   . CYS   B 2 168 ? -9.339  72.403 70.889  1.00 44.48  ? 138 CYS   B O   1 
ATOM   3946 C CB  . CYS   B 2 168 ? -12.435 72.849 71.794  1.00 42.70  ? 138 CYS   B CB  1 
ATOM   3947 S SG  . CYS   B 2 168 ? -11.464 73.067 73.303  1.00 43.40  ? 138 CYS   B SG  1 
ATOM   3948 N N   . GLU   B 2 169 ? -10.613 70.848 69.908  1.00 43.94  ? 139 GLU   B N   1 
ATOM   3949 C CA  . GLU   B 2 169 ? -9.561  69.861 69.808  1.00 44.54  ? 139 GLU   B CA  1 
ATOM   3950 C C   . GLU   B 2 169 ? -8.485  70.300 68.838  1.00 46.05  ? 139 GLU   B C   1 
ATOM   3951 O O   . GLU   B 2 169 ? -7.303  70.091 69.110  1.00 46.64  ? 139 GLU   B O   1 
ATOM   3952 C CB  . GLU   B 2 169 ? -10.151 68.523 69.381  1.00 45.22  ? 139 GLU   B CB  1 
ATOM   3953 C CG  . GLU   B 2 169 ? -9.176  67.370 69.481  1.00 46.94  ? 139 GLU   B CG  1 
ATOM   3954 C CD  . GLU   B 2 169 ? -9.615  66.139 68.722  1.00 51.33  ? 139 GLU   B CD  1 
ATOM   3955 O OE1 . GLU   B 2 169 ? -10.493 66.257 67.837  1.00 53.67  ? 139 GLU   B OE1 1 
ATOM   3956 O OE2 . GLU   B 2 169 ? -9.061  65.053 68.998  1.00 52.41  ? 139 GLU   B OE2 1 
ATOM   3957 N N   . PHE   B 2 170 ? -8.865  70.939 67.720  1.00 46.59  ? 140 PHE   B N   1 
ATOM   3958 C CA  . PHE   B 2 170 ? -7.868  71.432 66.766  1.00 48.02  ? 140 PHE   B CA  1 
ATOM   3959 C C   . PHE   B 2 170 ? -6.975  72.486 67.438  1.00 48.64  ? 140 PHE   B C   1 
ATOM   3960 O O   . PHE   B 2 170 ? -5.751  72.386 67.368  1.00 48.59  ? 140 PHE   B O   1 
ATOM   3961 C CB  . PHE   B 2 170 ? -8.527  71.952 65.481  1.00 48.57  ? 140 PHE   B CB  1 
ATOM   3962 C CG  . PHE   B 2 170 ? -8.298  71.003 64.331  1.00 50.56  ? 140 PHE   B CG  1 
ATOM   3963 C CD1 . PHE   B 2 170 ? -8.530  69.638 64.476  1.00 51.99  ? 140 PHE   B CD1 1 
ATOM   3964 C CD2 . PHE   B 2 170 ? -7.800  71.458 63.123  1.00 51.77  ? 140 PHE   B CD2 1 
ATOM   3965 C CE1 . PHE   B 2 170 ? -8.280  68.754 63.423  1.00 52.76  ? 140 PHE   B CE1 1 
ATOM   3966 C CE2 . PHE   B 2 170 ? -7.561  70.571 62.072  1.00 52.78  ? 140 PHE   B CE2 1 
ATOM   3967 C CZ  . PHE   B 2 170 ? -7.795  69.226 62.232  1.00 52.58  ? 140 PHE   B CZ  1 
ATOM   3968 N N   . TYR   B 2 171 ? -7.613  73.397 68.208  1.00 48.79  ? 141 TYR   B N   1 
ATOM   3969 C CA  . TYR   B 2 171 ? -6.979  74.450 68.989  1.00 49.21  ? 141 TYR   B CA  1 
ATOM   3970 C C   . TYR   B 2 171 ? -6.068  73.867 70.067  1.00 49.38  ? 141 TYR   B C   1 
ATOM   3971 O O   . TYR   B 2 171 ? -4.901  74.235 70.120  1.00 49.72  ? 141 TYR   B O   1 
ATOM   3972 C CB  . TYR   B 2 171 ? -8.041  75.353 69.637  1.00 49.47  ? 141 TYR   B CB  1 
ATOM   3973 C CG  . TYR   B 2 171 ? -8.657  76.355 68.691  1.00 50.66  ? 141 TYR   B CG  1 
ATOM   3974 C CD1 . TYR   B 2 171 ? -8.190  77.659 68.628  1.00 52.18  ? 141 TYR   B CD1 1 
ATOM   3975 C CD2 . TYR   B 2 171 ? -9.720  76.006 67.874  1.00 51.63  ? 141 TYR   B CD2 1 
ATOM   3976 C CE1 . TYR   B 2 171 ? -8.742  78.582 67.744  1.00 53.49  ? 141 TYR   B CE1 1 
ATOM   3977 C CE2 . TYR   B 2 171 ? -10.294 76.922 67.002  1.00 52.80  ? 141 TYR   B CE2 1 
ATOM   3978 C CZ  . TYR   B 2 171 ? -9.798  78.209 66.931  1.00 54.09  ? 141 TYR   B CZ  1 
ATOM   3979 O OH  . TYR   B 2 171 ? -10.362 79.117 66.062  1.00 55.20  ? 141 TYR   B OH  1 
ATOM   3980 N N   . LEU   B 2 172 ? -6.570  72.945 70.911  1.00 48.90  ? 142 LEU   B N   1 
ATOM   3981 C CA  . LEU   B 2 172 ? -5.775  72.337 71.975  1.00 49.07  ? 142 LEU   B CA  1 
ATOM   3982 C C   . LEU   B 2 172 ? -4.563  71.619 71.392  1.00 49.73  ? 142 LEU   B C   1 
ATOM   3983 O O   . LEU   B 2 172 ? -3.456  71.797 71.897  1.00 50.24  ? 142 LEU   B O   1 
ATOM   3984 C CB  . LEU   B 2 172 ? -6.633  71.365 72.800  1.00 49.16  ? 142 LEU   B CB  1 
ATOM   3985 C CG  . LEU   B 2 172 ? -5.888  70.488 73.818  1.00 50.14  ? 142 LEU   B CG  1 
ATOM   3986 C CD1 . LEU   B 2 172 ? -5.309  71.317 74.938  1.00 50.29  ? 142 LEU   B CD1 1 
ATOM   3987 C CD2 . LEU   B 2 172 ? -6.769  69.366 74.340  1.00 50.56  ? 142 LEU   B CD2 1 
ATOM   3988 N N   . LEU   B 2 173 ? -4.754  70.857 70.302  1.00 49.60  ? 143 LEU   B N   1 
ATOM   3989 C CA  . LEU   B 2 173 ? -3.644  70.150 69.666  1.00 49.98  ? 143 LEU   B CA  1 
ATOM   3990 C C   . LEU   B 2 173 ? -2.502  71.075 69.246  1.00 50.71  ? 143 LEU   B C   1 
ATOM   3991 O O   . LEU   B 2 173 ? -1.362  70.832 69.641  1.00 51.37  ? 143 LEU   B O   1 
ATOM   3992 C CB  . LEU   B 2 173 ? -4.119  69.311 68.478  1.00 49.95  ? 143 LEU   B CB  1 
ATOM   3993 C CG  . LEU   B 2 173 ? -3.037  68.531 67.757  1.00 50.87  ? 143 LEU   B CG  1 
ATOM   3994 C CD1 . LEU   B 2 173 ? -2.437  67.484 68.656  1.00 51.33  ? 143 LEU   B CD1 1 
ATOM   3995 C CD2 . LEU   B 2 173 ? -3.588  67.880 66.533  1.00 51.37  ? 143 LEU   B CD2 1 
ATOM   3996 N N   . GLU   B 2 174 ? -2.800  72.148 68.496  1.00 50.43  ? 144 GLU   B N   1 
ATOM   3997 C CA  . GLU   B 2 174 ? -1.765  73.056 68.033  1.00 50.97  ? 144 GLU   B CA  1 
ATOM   3998 C C   . GLU   B 2 174 ? -1.175  73.940 69.118  1.00 51.72  ? 144 GLU   B C   1 
ATOM   3999 O O   . GLU   B 2 174 ? 0.025   74.217 69.093  1.00 51.97  ? 144 GLU   B O   1 
ATOM   4000 C CB  . GLU   B 2 174 ? -2.267  73.902 66.865  1.00 53.20  ? 144 GLU   B CB  1 
ATOM   4001 C CG  . GLU   B 2 174 ? -3.428  74.805 67.213  1.00 58.53  ? 144 GLU   B CG  1 
ATOM   4002 C CD  . GLU   B 2 174 ? -3.802  75.769 66.109  1.00 65.72  ? 144 GLU   B CD  1 
ATOM   4003 O OE1 . GLU   B 2 174 ? -4.490  75.328 65.159  1.00 68.29  ? 144 GLU   B OE1 1 
ATOM   4004 O OE2 . GLU   B 2 174 ? -3.413  76.959 66.189  1.00 66.29  ? 144 GLU   B OE2 1 
ATOM   4005 N N   . LEU   B 2 175 ? -1.993  74.370 70.086  1.00 51.87  ? 145 LEU   B N   1 
ATOM   4006 C CA  . LEU   B 2 175 ? -1.505  75.248 71.153  1.00 52.36  ? 145 LEU   B CA  1 
ATOM   4007 C C   . LEU   B 2 175 ? -0.826  74.500 72.318  1.00 52.45  ? 145 LEU   B C   1 
ATOM   4008 O O   . LEU   B 2 175 ? -0.722  75.004 73.435  1.00 52.87  ? 145 LEU   B O   1 
ATOM   4009 C CB  . LEU   B 2 175 ? -2.617  76.174 71.636  1.00 52.91  ? 145 LEU   B CB  1 
ATOM   4010 C CG  . LEU   B 2 175 ? -3.238  77.031 70.522  1.00 54.70  ? 145 LEU   B CG  1 
ATOM   4011 C CD1 . LEU   B 2 175 ? -4.463  77.735 71.004  1.00 55.68  ? 145 LEU   B CD1 1 
ATOM   4012 C CD2 . LEU   B 2 175 ? -2.235  78.001 69.937  1.00 54.98  ? 145 LEU   B CD2 1 
ATOM   4013 N N   . MET   B 2 176 ? -0.365  73.300 72.024  1.00 52.04  ? 146 MET   B N   1 
ATOM   4014 C CA  . MET   B 2 176 ? 0.448   72.414 72.841  1.00 52.28  ? 146 MET   B CA  1 
ATOM   4015 C C   . MET   B 2 176 ? 1.664   71.934 72.037  1.00 51.87  ? 146 MET   B C   1 
ATOM   4016 O O   . MET   B 2 176 ? 2.395   71.089 72.529  1.00 51.96  ? 146 MET   B O   1 
ATOM   4017 C CB  . MET   B 2 176 ? -0.348  71.175 73.233  1.00 53.21  ? 146 MET   B CB  1 
ATOM   4018 C CG  . MET   B 2 176 ? -1.231  71.367 74.428  1.00 55.05  ? 146 MET   B CG  1 
ATOM   4019 S SD  . MET   B 2 176 ? -1.574  69.783 75.211  1.00 57.27  ? 146 MET   B SD  1 
ATOM   4020 C CE  . MET   B 2 176 ? -2.250  68.851 73.828  1.00 54.66  ? 146 MET   B CE  1 
ATOM   4021 N N   . ASP   B 2 177 ? 1.871   72.457 70.809  1.00 51.54  ? 147 ASP   B N   1 
ATOM   4022 C CA  . ASP   B 2 177 ? 2.905   72.080 69.867  1.00 51.73  ? 147 ASP   B CA  1 
ATOM   4023 C C   . ASP   B 2 177 ? 2.860   70.595 69.563  1.00 50.65  ? 147 ASP   B C   1 
ATOM   4024 O O   . ASP   B 2 177 ? 3.909   69.999 69.329  1.00 51.01  ? 147 ASP   B O   1 
ATOM   4025 C CB  . ASP   B 2 177 ? 4.302   72.535 70.309  1.00 54.70  ? 147 ASP   B CB  1 
ATOM   4026 C CG  . ASP   B 2 177 ? 5.299   72.573 69.164  1.00 63.22  ? 147 ASP   B CG  1 
ATOM   4027 O OD1 . ASP   B 2 177 ? 4.857   72.661 67.986  1.00 64.65  ? 147 ASP   B OD1 1 
ATOM   4028 O OD2 . ASP   B 2 177 ? 6.519   72.497 69.437  1.00 67.21  ? 147 ASP   B OD2 1 
ATOM   4029 N N   . CYS   B 2 178 ? 1.635   69.995 69.576  1.00 48.93  ? 148 CYS   B N   1 
ATOM   4030 C CA  . CYS   B 2 178 ? 1.397   68.577 69.338  1.00 47.69  ? 148 CYS   B CA  1 
ATOM   4031 C C   . CYS   B 2 178 ? 2.093   67.668 70.358  1.00 46.21  ? 148 CYS   B C   1 
ATOM   4032 O O   . CYS   B 2 178 ? 2.318   66.501 70.072  1.00 46.40  ? 148 CYS   B O   1 
ATOM   4033 C CB  . CYS   B 2 178 ? 1.746   68.193 67.902  1.00 48.33  ? 148 CYS   B CB  1 
ATOM   4034 S SG  . CYS   B 2 178 ? 0.787   69.079 66.644  1.00 51.46  ? 148 CYS   B SG  1 
ATOM   4035 N N   . CYS   B 2 179 ? 2.429   68.189 71.544  1.00 44.79  ? 149 CYS   B N   1 
ATOM   4036 C CA  . CYS   B 2 179 ? 3.075   67.400 72.586  1.00 43.85  ? 149 CYS   B CA  1 
ATOM   4037 C C   . CYS   B 2 179 ? 1.991   66.645 73.306  1.00 43.11  ? 149 CYS   B C   1 
ATOM   4038 O O   . CYS   B 2 179 ? 1.283   67.226 74.139  1.00 43.36  ? 149 CYS   B O   1 
ATOM   4039 C CB  . CYS   B 2 179 ? 3.849   68.301 73.536  1.00 43.77  ? 149 CYS   B CB  1 
ATOM   4040 S SG  . CYS   B 2 179 ? 5.089   69.326 72.714  1.00 44.05  ? 149 CYS   B SG  1 
ATOM   4041 N N   . LEU   B 2 180 ? 1.833   65.357 72.946  1.00 41.76  ? 150 LEU   B N   1 
ATOM   4042 C CA  . LEU   B 2 180 ? 0.786   64.491 73.452  1.00 40.81  ? 150 LEU   B CA  1 
ATOM   4043 C C   . LEU   B 2 180 ? 1.265   63.474 74.480  1.00 40.26  ? 150 LEU   B C   1 
ATOM   4044 O O   . LEU   B 2 180 ? 0.501   63.132 75.384  1.00 39.97  ? 150 LEU   B O   1 
ATOM   4045 C CB  . LEU   B 2 180 ? 0.062   63.811 72.279  1.00 40.89  ? 150 LEU   B CB  1 
ATOM   4046 C CG  . LEU   B 2 180 ? -0.508  64.770 71.218  1.00 42.41  ? 150 LEU   B CG  1 
ATOM   4047 C CD1 . LEU   B 2 180 ? -1.146  64.023 70.071  1.00 42.51  ? 150 LEU   B CD1 1 
ATOM   4048 C CD2 . LEU   B 2 180 ? -1.502  65.762 71.832  1.00 43.37  ? 150 LEU   B CD2 1 
ATOM   4049 N N   . ILE   B 2 181 ? 2.520   62.999 74.368  1.00 39.93  ? 151 ILE   B N   1 
ATOM   4050 C CA  . ILE   B 2 181 ? 3.062   62.021 75.324  1.00 39.84  ? 151 ILE   B CA  1 
ATOM   4051 C C   . ILE   B 2 181 ? 3.397   62.672 76.658  1.00 38.69  ? 151 ILE   B C   1 
ATOM   4052 O O   . ILE   B 2 181 ? 4.298   63.516 76.736  1.00 38.68  ? 151 ILE   B O   1 
ATOM   4053 C CB  . ILE   B 2 181 ? 4.248   61.200 74.753  1.00 40.67  ? 151 ILE   B CB  1 
ATOM   4054 C CG1 . ILE   B 2 181 ? 3.798   60.298 73.584  1.00 41.95  ? 151 ILE   B CG1 1 
ATOM   4055 C CG2 . ILE   B 2 181 ? 4.917   60.367 75.838  1.00 41.14  ? 151 ILE   B CG2 1 
ATOM   4056 C CD1 . ILE   B 2 181 ? 2.633   59.336 73.922  1.00 43.35  ? 151 ILE   B CD1 1 
ATOM   4057 N N   . VAL   B 2 182 ? 2.638   62.292 77.700  1.00 37.62  ? 152 VAL   B N   1 
ATOM   4058 C CA  . VAL   B 2 182 ? 2.787   62.845 79.040  1.00 37.00  ? 152 VAL   B CA  1 
ATOM   4059 C C   . VAL   B 2 182 ? 3.227   61.797 80.051  1.00 36.57  ? 152 VAL   B C   1 
ATOM   4060 O O   . VAL   B 2 182 ? 2.647   60.716 80.145  1.00 36.67  ? 152 VAL   B O   1 
ATOM   4061 C CB  . VAL   B 2 182 ? 1.511   63.590 79.498  1.00 37.48  ? 152 VAL   B CB  1 
ATOM   4062 C CG1 . VAL   B 2 182 ? 1.613   64.027 80.959  1.00 37.91  ? 152 VAL   B CG1 1 
ATOM   4063 C CG2 . VAL   B 2 182 ? 1.223   64.789 78.594  1.00 37.86  ? 152 VAL   B CG2 1 
ATOM   4064 N N   . TYR   B 2 183 ? 4.262   62.132 80.807  1.00 35.72  ? 153 TYR   B N   1 
ATOM   4065 C CA  . TYR   B 2 183 ? 4.812   61.309 81.855  1.00 35.42  ? 153 TYR   B CA  1 
ATOM   4066 C C   . TYR   B 2 183 ? 4.171   61.707 83.183  1.00 34.83  ? 153 TYR   B C   1 
ATOM   4067 O O   . TYR   B 2 183 ? 3.986   62.886 83.472  1.00 34.88  ? 153 TYR   B O   1 
ATOM   4068 C CB  . TYR   B 2 183 ? 6.315   61.503 81.902  1.00 36.12  ? 153 TYR   B CB  1 
ATOM   4069 C CG  . TYR   B 2 183 ? 7.017   60.996 80.664  1.00 38.50  ? 153 TYR   B CG  1 
ATOM   4070 C CD1 . TYR   B 2 183 ? 7.060   61.754 79.503  1.00 39.87  ? 153 TYR   B CD1 1 
ATOM   4071 C CD2 . TYR   B 2 183 ? 7.655   59.763 80.660  1.00 40.36  ? 153 TYR   B CD2 1 
ATOM   4072 C CE1 . TYR   B 2 183 ? 7.721   61.297 78.371  1.00 41.17  ? 153 TYR   B CE1 1 
ATOM   4073 C CE2 . TYR   B 2 183 ? 8.334   59.305 79.544  1.00 41.45  ? 153 TYR   B CE2 1 
ATOM   4074 C CZ  . TYR   B 2 183 ? 8.358   60.070 78.396  1.00 42.63  ? 153 TYR   B CZ  1 
ATOM   4075 O OH  . TYR   B 2 183 ? 9.017   59.580 77.290  1.00 44.99  ? 153 TYR   B OH  1 
ATOM   4076 N N   . HIS   B 2 184 ? 3.769   60.719 83.956  1.00 34.42  ? 154 HIS   B N   1 
ATOM   4077 C CA  . HIS   B 2 184 ? 3.104   60.917 85.233  1.00 34.59  ? 154 HIS   B CA  1 
ATOM   4078 C C   . HIS   B 2 184 ? 3.924   60.264 86.366  1.00 35.08  ? 154 HIS   B C   1 
ATOM   4079 O O   . HIS   B 2 184 ? 4.841   59.483 86.086  1.00 35.41  ? 154 HIS   B O   1 
ATOM   4080 C CB  . HIS   B 2 184 ? 1.691   60.326 85.141  1.00 35.41  ? 154 HIS   B CB  1 
ATOM   4081 C CG  . HIS   B 2 184 ? 0.868   60.933 84.052  1.00 37.66  ? 154 HIS   B CG  1 
ATOM   4082 N ND1 . HIS   B 2 184 ? 0.559   62.286 84.050  1.00 39.61  ? 154 HIS   B ND1 1 
ATOM   4083 C CD2 . HIS   B 2 184 ? 0.307   60.355 82.965  1.00 38.33  ? 154 HIS   B CD2 1 
ATOM   4084 C CE1 . HIS   B 2 184 ? -0.177  62.482 82.970  1.00 39.86  ? 154 HIS   B CE1 1 
ATOM   4085 N NE2 . HIS   B 2 184 ? -0.358  61.350 82.288  1.00 39.50  ? 154 HIS   B NE2 1 
ATOM   4086 N N   . PRO   B 2 185 ? 3.644   60.573 87.649  1.00 35.13  ? 155 PRO   B N   1 
ATOM   4087 C CA  . PRO   B 2 185 ? 4.457   59.998 88.729  1.00 35.49  ? 155 PRO   B CA  1 
ATOM   4088 C C   . PRO   B 2 185 ? 4.046   58.608 89.190  1.00 36.23  ? 155 PRO   B C   1 
ATOM   4089 O O   . PRO   B 2 185 ? 4.720   58.069 90.051  1.00 36.18  ? 155 PRO   B O   1 
ATOM   4090 C CB  . PRO   B 2 185 ? 4.306   61.020 89.872  1.00 36.18  ? 155 PRO   B CB  1 
ATOM   4091 C CG  . PRO   B 2 185 ? 3.439   62.140 89.331  1.00 36.37  ? 155 PRO   B CG  1 
ATOM   4092 C CD  . PRO   B 2 185 ? 2.673   61.538 88.189  1.00 34.73  ? 155 PRO   B CD  1 
ATOM   4093 N N   . TYR   B 2 186 ? 2.949   58.036 88.655  1.00 36.93  ? 156 TYR   B N   1 
ATOM   4094 C CA  . TYR   B 2 186 ? 2.454   56.719 89.070  1.00 37.77  ? 156 TYR   B CA  1 
ATOM   4095 C C   . TYR   B 2 186 ? 3.454   55.618 88.731  1.00 39.38  ? 156 TYR   B C   1 
ATOM   4096 O O   . TYR   B 2 186 ? 3.706   54.747 89.560  1.00 39.09  ? 156 TYR   B O   1 
ATOM   4097 C CB  . TYR   B 2 186 ? 1.086   56.422 88.435  1.00 37.67  ? 156 TYR   B CB  1 
ATOM   4098 C CG  . TYR   B 2 186 ? 0.029   57.491 88.643  1.00 38.33  ? 156 TYR   B CG  1 
ATOM   4099 C CD1 . TYR   B 2 186 ? -0.787  57.484 89.768  1.00 38.74  ? 156 TYR   B CD1 1 
ATOM   4100 C CD2 . TYR   B 2 186 ? -0.195  58.472 87.685  1.00 39.26  ? 156 TYR   B CD2 1 
ATOM   4101 C CE1 . TYR   B 2 186 ? -1.791  58.429 89.939  1.00 39.26  ? 156 TYR   B CE1 1 
ATOM   4102 C CE2 . TYR   B 2 186 ? -1.187  59.432 87.852  1.00 39.93  ? 156 TYR   B CE2 1 
ATOM   4103 C CZ  . TYR   B 2 186 ? -1.987  59.405 88.979  1.00 40.53  ? 156 TYR   B CZ  1 
ATOM   4104 O OH  . TYR   B 2 186 ? -2.951  60.373 89.144  1.00 42.32  ? 156 TYR   B OH  1 
ATOM   4105 N N   . ARG   B 2 187 ? 4.037   55.670 87.507  1.00 40.81  ? 157 ARG   B N   1 
ATOM   4106 C CA  . ARG   B 2 187 ? 5.052   54.718 87.036  1.00 42.18  ? 157 ARG   B CA  1 
ATOM   4107 C C   . ARG   B 2 187 ? 6.321   54.741 87.926  1.00 41.98  ? 157 ARG   B C   1 
ATOM   4108 O O   . ARG   B 2 187 ? 6.650   53.689 88.471  1.00 42.26  ? 157 ARG   B O   1 
ATOM   4109 C CB  . ARG   B 2 187 ? 5.378   54.958 85.558  1.00 45.49  ? 157 ARG   B CB  1 
ATOM   4110 C CG  . ARG   B 2 187 ? 6.175   53.837 84.891  1.00 52.03  ? 157 ARG   B CG  1 
ATOM   4111 C CD  . ARG   B 2 187 ? 5.312   52.908 84.033  1.00 57.98  ? 157 ARG   B CD  1 
ATOM   4112 N NE  . ARG   B 2 187 ? 4.430   53.627 83.100  1.00 62.58  ? 157 ARG   B NE  1 
ATOM   4113 C CZ  . ARG   B 2 187 ? 3.686   53.037 82.167  1.00 65.50  ? 157 ARG   B CZ  1 
ATOM   4114 N NH1 . ARG   B 2 187 ? 3.726   51.717 82.011  1.00 65.33  ? 157 ARG   B NH1 1 
ATOM   4115 N NH2 . ARG   B 2 187 ? 2.906   53.762 81.375  1.00 65.65  ? 157 ARG   B NH2 1 
ATOM   4116 N N   . PRO   B 2 188 ? 6.990   55.893 88.186  1.00 41.45  ? 158 PRO   B N   1 
ATOM   4117 C CA  . PRO   B 2 188 ? 8.128   55.869 89.115  1.00 41.47  ? 158 PRO   B CA  1 
ATOM   4118 C C   . PRO   B 2 188 ? 7.709   55.485 90.521  1.00 42.10  ? 158 PRO   B C   1 
ATOM   4119 O O   . PRO   B 2 188 ? 8.418   54.704 91.136  1.00 42.75  ? 158 PRO   B O   1 
ATOM   4120 C CB  . PRO   B 2 188 ? 8.685   57.295 89.079  1.00 41.92  ? 158 PRO   B CB  1 
ATOM   4121 C CG  . PRO   B 2 188 ? 7.622   58.121 88.542  1.00 42.51  ? 158 PRO   B CG  1 
ATOM   4122 C CD  . PRO   B 2 188 ? 6.784   57.246 87.642  1.00 41.02  ? 158 PRO   B CD  1 
ATOM   4123 N N   . LEU   B 2 189 ? 6.550   55.949 91.014  1.00 42.01  ? 159 LEU   B N   1 
ATOM   4124 C CA  . LEU   B 2 189 ? 6.106   55.613 92.373  1.00 42.97  ? 159 LEU   B CA  1 
ATOM   4125 C C   . LEU   B 2 189 ? 6.044   54.106 92.622  1.00 44.61  ? 159 LEU   B C   1 
ATOM   4126 O O   . LEU   B 2 189 ? 6.489   53.620 93.670  1.00 44.85  ? 159 LEU   B O   1 
ATOM   4127 C CB  . LEU   B 2 189 ? 4.740   56.240 92.674  1.00 42.79  ? 159 LEU   B CB  1 
ATOM   4128 C CG  . LEU   B 2 189 ? 4.132   55.913 94.033  1.00 43.25  ? 159 LEU   B CG  1 
ATOM   4129 C CD1 . LEU   B 2 189 ? 4.871   56.620 95.145  1.00 43.56  ? 159 LEU   B CD1 1 
ATOM   4130 C CD2 . LEU   B 2 189 ? 2.687   56.230 94.044  1.00 43.65  ? 159 LEU   B CD2 1 
ATOM   4131 N N   . LEU   B 2 190 ? 5.519   53.373 91.640  1.00 45.30  ? 160 LEU   B N   1 
ATOM   4132 C CA  . LEU   B 2 190 ? 5.408   51.930 91.717  1.00 46.12  ? 160 LEU   B CA  1 
ATOM   4133 C C   . LEU   B 2 190 ? 6.769   51.277 91.809  1.00 46.65  ? 160 LEU   B C   1 
ATOM   4134 O O   . LEU   B 2 190 ? 6.935   50.337 92.582  1.00 46.77  ? 160 LEU   B O   1 
ATOM   4135 C CB  . LEU   B 2 190 ? 4.650   51.426 90.510  1.00 46.50  ? 160 LEU   B CB  1 
ATOM   4136 C CG  . LEU   B 2 190 ? 3.312   50.872 90.865  1.00 48.36  ? 160 LEU   B CG  1 
ATOM   4137 C CD1 . LEU   B 2 190 ? 2.340   51.020 89.702  1.00 48.94  ? 160 LEU   B CD1 1 
ATOM   4138 C CD2 . LEU   B 2 190 ? 3.452   49.453 91.393  1.00 49.26  ? 160 LEU   B CD2 1 
ATOM   4139 N N   . GLN   B 2 191 ? 7.742   51.785 91.053  1.00 46.88  ? 161 GLN   B N   1 
ATOM   4140 C CA  . GLN   B 2 191 ? 9.092   51.272 91.114  1.00 48.40  ? 161 GLN   B CA  1 
ATOM   4141 C C   . GLN   B 2 191 ? 9.720   51.574 92.477  1.00 49.46  ? 161 GLN   B C   1 
ATOM   4142 O O   . GLN   B 2 191 ? 10.354  50.706 93.077  1.00 50.05  ? 161 GLN   B O   1 
ATOM   4143 C CB  . GLN   B 2 191 ? 9.929   51.834 89.968  1.00 50.79  ? 161 GLN   B CB  1 
ATOM   4144 C CG  . GLN   B 2 191 ? 9.586   51.167 88.643  1.00 55.77  ? 161 GLN   B CG  1 
ATOM   4145 C CD  . GLN   B 2 191 ? 10.136  51.913 87.453  1.00 61.62  ? 161 GLN   B CD  1 
ATOM   4146 O OE1 . GLN   B 2 191 ? 10.234  53.152 87.449  1.00 63.44  ? 161 GLN   B OE1 1 
ATOM   4147 N NE2 . GLN   B 2 191 ? 10.489  51.171 86.408  1.00 62.36  ? 161 GLN   B NE2 1 
ATOM   4148 N N   . TYR   B 2 192 ? 9.499   52.778 92.990  1.00 49.52  ? 162 TYR   B N   1 
ATOM   4149 C CA  . TYR   B 2 192 ? 10.006  53.175 94.293  1.00 49.87  ? 162 TYR   B CA  1 
ATOM   4150 C C   . TYR   B 2 192 ? 9.487   52.295 95.422  1.00 49.98  ? 162 TYR   B C   1 
ATOM   4151 O O   . TYR   B 2 192 ? 10.306  51.780 96.168  1.00 49.78  ? 162 TYR   B O   1 
ATOM   4152 C CB  . TYR   B 2 192 ? 9.711   54.666 94.563  1.00 50.15  ? 162 TYR   B CB  1 
ATOM   4153 C CG  . TYR   B 2 192 ? 10.523  55.588 93.685  1.00 50.92  ? 162 TYR   B CG  1 
ATOM   4154 C CD1 . TYR   B 2 192 ? 11.835  55.287 93.358  1.00 51.93  ? 162 TYR   B CD1 1 
ATOM   4155 C CD2 . TYR   B 2 192 ? 9.980   56.759 93.181  1.00 51.58  ? 162 TYR   B CD2 1 
ATOM   4156 C CE1 . TYR   B 2 192 ? 12.574  56.106 92.522  1.00 52.81  ? 162 TYR   B CE1 1 
ATOM   4157 C CE2 . TYR   B 2 192 ? 10.702  57.573 92.320  1.00 52.36  ? 162 TYR   B CE2 1 
ATOM   4158 C CZ  . TYR   B 2 192 ? 12.008  57.253 92.011  1.00 53.44  ? 162 TYR   B CZ  1 
ATOM   4159 O OH  . TYR   B 2 192 ? 12.765  58.043 91.184  1.00 55.20  ? 162 TYR   B OH  1 
ATOM   4160 N N   . VAL   B 2 193 ? 8.147   52.098 95.551  1.00 50.45  ? 163 VAL   B N   1 
ATOM   4161 C CA  . VAL   B 2 193 ? 7.593   51.268 96.637  1.00 51.64  ? 163 VAL   B CA  1 
ATOM   4162 C C   . VAL   B 2 193 ? 7.923   49.786 96.470  1.00 53.06  ? 163 VAL   B C   1 
ATOM   4163 O O   . VAL   B 2 193 ? 7.946   49.061 97.463  1.00 53.11  ? 163 VAL   B O   1 
ATOM   4164 C CB  . VAL   B 2 193 ? 6.085   51.469 96.917  1.00 52.21  ? 163 VAL   B CB  1 
ATOM   4165 C CG1 . VAL   B 2 193 ? 5.732   52.939 96.988  1.00 52.62  ? 163 VAL   B CG1 1 
ATOM   4166 C CG2 . VAL   B 2 193 ? 5.227   50.753 95.886  1.00 52.71  ? 163 VAL   B CG2 1 
ATOM   4167 N N   . GLN   B 2 194 ? 8.197   49.328 95.222  1.00 54.04  ? 164 GLN   B N   1 
ATOM   4168 C CA  . GLN   B 2 194 ? 8.622   47.958 94.963  1.00 55.04  ? 164 GLN   B CA  1 
ATOM   4169 C C   . GLN   B 2 194 ? 10.031  47.847 95.548  1.00 55.96  ? 164 GLN   B C   1 
ATOM   4170 O O   . GLN   B 2 194 ? 10.235  47.002 96.404  1.00 56.56  ? 164 GLN   B O   1 
ATOM   4171 C CB  . GLN   B 2 194 ? 8.624   47.631 93.457  1.00 56.79  ? 164 GLN   B CB  1 
ATOM   4172 C CG  . GLN   B 2 194 ? 9.278   46.276 93.119  1.00 60.45  ? 164 GLN   B CG  1 
ATOM   4173 C CD  . GLN   B 2 194 ? 9.978   46.295 91.768  1.00 64.90  ? 164 GLN   B CD  1 
ATOM   4174 O OE1 . GLN   B 2 194 ? 10.935  47.060 91.539  1.00 66.79  ? 164 GLN   B OE1 1 
ATOM   4175 N NE2 . GLN   B 2 194 ? 9.520   45.453 90.840  1.00 64.40  ? 164 GLN   B NE2 1 
ATOM   4176 N N   . ASP   B 2 195 ? 10.939  48.796 95.239  1.00 55.98  ? 165 ASP   B N   1 
ATOM   4177 C CA  . ASP   B 2 195 ? 12.288  48.788 95.805  1.00 56.88  ? 165 ASP   B CA  1 
ATOM   4178 C C   . ASP   B 2 195 ? 12.283  48.772 97.336  1.00 57.38  ? 165 ASP   B C   1 
ATOM   4179 O O   . ASP   B 2 195 ? 13.009  47.997 97.948  1.00 57.77  ? 165 ASP   B O   1 
ATOM   4180 C CB  . ASP   B 2 195 ? 13.109  49.968 95.291  1.00 59.23  ? 165 ASP   B CB  1 
ATOM   4181 C CG  . ASP   B 2 195 ? 14.545  49.883 95.737  1.00 65.29  ? 165 ASP   B CG  1 
ATOM   4182 O OD1 . ASP   B 2 195 ? 15.128  48.793 95.626  1.00 66.52  ? 165 ASP   B OD1 1 
ATOM   4183 O OD2 . ASP   B 2 195 ? 15.073  50.898 96.233  1.00 68.47  ? 165 ASP   B OD2 1 
ATOM   4184 N N   . MET   B 2 196 ? 11.442  49.599 97.940  1.00 57.50  ? 166 MET   B N   1 
ATOM   4185 C CA  . MET   B 2 196 ? 11.261  49.685 99.391  1.00 57.98  ? 166 MET   B CA  1 
ATOM   4186 C C   . MET   B 2 196 ? 10.722  48.395 100.005 1.00 58.60  ? 166 MET   B C   1 
ATOM   4187 O O   . MET   B 2 196 ? 10.949  48.141 101.186 1.00 58.36  ? 166 MET   B O   1 
ATOM   4188 C CB  . MET   B 2 196 ? 10.225  50.774 99.705  1.00 57.96  ? 166 MET   B CB  1 
ATOM   4189 C CG  . MET   B 2 196 ? 10.777  52.140 99.767  1.00 58.98  ? 166 MET   B CG  1 
ATOM   4190 S SD  . MET   B 2 196 ? 9.635   53.148 100.712 1.00 60.25  ? 166 MET   B SD  1 
ATOM   4191 C CE  . MET   B 2 196 ? 10.603  54.568 100.938 1.00 57.56  ? 166 MET   B CE  1 
ATOM   4192 N N   . GLY   B 2 197 ? 9.925   47.664 99.228  1.00 59.30  ? 167 GLY   B N   1 
ATOM   4193 C CA  . GLY   B 2 197 ? 9.228   46.463 99.663  1.00 60.63  ? 167 GLY   B CA  1 
ATOM   4194 C C   . GLY   B 2 197 ? 8.017   46.765 100.533 1.00 61.76  ? 167 GLY   B C   1 
ATOM   4195 O O   . GLY   B 2 197 ? 7.548   45.893 101.271 1.00 62.17  ? 167 GLY   B O   1 
ATOM   4196 N N   . GLN   B 2 198 ? 7.507   48.006 100.471 1.00 61.96  ? 168 GLN   B N   1 
ATOM   4197 C CA  . GLN   B 2 198 ? 6.378   48.431 101.284 1.00 63.05  ? 168 GLN   B CA  1 
ATOM   4198 C C   . GLN   B 2 198 ? 5.190   48.783 100.401 1.00 63.90  ? 168 GLN   B C   1 
ATOM   4199 O O   . GLN   B 2 198 ? 4.525   49.796 100.626 1.00 64.23  ? 168 GLN   B O   1 
ATOM   4200 C CB  . GLN   B 2 198 ? 6.789   49.637 102.145 1.00 64.99  ? 168 GLN   B CB  1 
ATOM   4201 C CG  . GLN   B 2 198 ? 7.805   49.306 103.221 1.00 68.85  ? 168 GLN   B CG  1 
ATOM   4202 C CD  . GLN   B 2 198 ? 7.235   48.366 104.242 1.00 73.98  ? 168 GLN   B CD  1 
ATOM   4203 O OE1 . GLN   B 2 198 ? 6.037   48.391 104.552 1.00 76.41  ? 168 GLN   B OE1 1 
ATOM   4204 N NE2 . GLN   B 2 198 ? 8.082   47.514 104.789 1.00 74.66  ? 168 GLN   B NE2 1 
ATOM   4205 N N   . GLU   B 2 199 ? 4.934   47.957 99.376  1.00 64.06  ? 169 GLU   B N   1 
ATOM   4206 C CA  . GLU   B 2 199 ? 3.852   48.188 98.422  1.00 64.60  ? 169 GLU   B CA  1 
ATOM   4207 C C   . GLU   B 2 199 ? 2.494   48.094 99.101  1.00 64.58  ? 169 GLU   B C   1 
ATOM   4208 O O   . GLU   B 2 199 ? 1.613   48.919 98.853  1.00 64.63  ? 169 GLU   B O   1 
ATOM   4209 C CB  . GLU   B 2 199 ? 3.921   47.180 97.264  1.00 67.42  ? 169 GLU   B CB  1 
ATOM   4210 C CG  . GLU   B 2 199 ? 5.316   46.963 96.713  1.00 74.69  ? 169 GLU   B CG  1 
ATOM   4211 C CD  . GLU   B 2 199 ? 5.356   45.963 95.577  1.00 84.99  ? 169 GLU   B CD  1 
ATOM   4212 O OE1 . GLU   B 2 199 ? 6.294   45.133 95.552  1.00 87.21  ? 169 GLU   B OE1 1 
ATOM   4213 O OE2 . GLU   B 2 199 ? 4.442   45.999 94.720  1.00 88.47  ? 169 GLU   B OE2 1 
ATOM   4214 N N   . ASP   B 2 200 ? 2.325   47.087 99.958  1.00 64.24  ? 170 ASP   B N   1 
ATOM   4215 C CA  . ASP   B 2 200 ? 1.063   46.881 100.644 1.00 64.37  ? 170 ASP   B CA  1 
ATOM   4216 C C   . ASP   B 2 200 ? 0.794   47.992 101.627 1.00 63.94  ? 170 ASP   B C   1 
ATOM   4217 O O   . ASP   B 2 200 ? -0.319  48.510 101.679 1.00 64.48  ? 170 ASP   B O   1 
ATOM   4218 C CB  . ASP   B 2 200 ? 1.048   45.519 101.356 1.00 66.39  ? 170 ASP   B CB  1 
ATOM   4219 C CG  . ASP   B 2 200 ? 0.532   44.376 100.505 1.00 71.35  ? 170 ASP   B CG  1 
ATOM   4220 O OD1 . ASP   B 2 200 ? 0.476   44.536 99.260  1.00 71.54  ? 170 ASP   B OD1 1 
ATOM   4221 O OD2 . ASP   B 2 200 ? 0.184   43.318 101.081 1.00 74.30  ? 170 ASP   B OD2 1 
ATOM   4222 N N   . MET   B 2 201 ? 1.813   48.380 102.385 1.00 62.90  ? 171 MET   B N   1 
ATOM   4223 C CA  . MET   B 2 201 ? 1.650   49.391 103.408 1.00 62.34  ? 171 MET   B CA  1 
ATOM   4224 C C   . MET   B 2 201 ? 1.526   50.809 102.871 1.00 60.28  ? 171 MET   B C   1 
ATOM   4225 O O   . MET   B 2 201 ? 0.652   51.535 103.321 1.00 60.43  ? 171 MET   B O   1 
ATOM   4226 C CB  . MET   B 2 201 ? 2.782   49.288 104.439 1.00 64.38  ? 171 MET   B CB  1 
ATOM   4227 C CG  . MET   B 2 201 ? 2.306   49.459 105.858 1.00 69.51  ? 171 MET   B CG  1 
ATOM   4228 S SD  . MET   B 2 201 ? 3.159   50.824 106.695 1.00 82.99  ? 171 MET   B SD  1 
ATOM   4229 C CE  . MET   B 2 201 ? 2.084   51.044 108.163 1.00 80.44  ? 171 MET   B CE  1 
ATOM   4230 N N   . LEU   B 2 202 ? 2.371   51.208 101.912 1.00 58.38  ? 172 LEU   B N   1 
ATOM   4231 C CA  . LEU   B 2 202 ? 2.388   52.591 101.438 1.00 57.02  ? 172 LEU   B CA  1 
ATOM   4232 C C   . LEU   B 2 202 ? 1.732   52.915 100.099 1.00 55.00  ? 172 LEU   B C   1 
ATOM   4233 O O   . LEU   B 2 202 ? 1.304   54.057 99.942  1.00 54.69  ? 172 LEU   B O   1 
ATOM   4234 C CB  . LEU   B 2 202 ? 3.830   53.096 101.365 1.00 57.27  ? 172 LEU   B CB  1 
ATOM   4235 C CG  . LEU   B 2 202 ? 4.591   53.123 102.651 1.00 58.82  ? 172 LEU   B CG  1 
ATOM   4236 C CD1 . LEU   B 2 202 ? 6.074   53.239 102.381 1.00 59.51  ? 172 LEU   B CD1 1 
ATOM   4237 C CD2 . LEU   B 2 202 ? 4.084   54.240 103.557 1.00 59.37  ? 172 LEU   B CD2 1 
ATOM   4238 N N   . LEU   B 2 203 ? 1.737   51.996 99.110  1.00 53.40  ? 173 LEU   B N   1 
ATOM   4239 C CA  . LEU   B 2 203 ? 1.210   52.336 97.779  1.00 52.48  ? 173 LEU   B CA  1 
ATOM   4240 C C   . LEU   B 2 203 ? -0.210  52.929 97.780  1.00 50.78  ? 173 LEU   B C   1 
ATOM   4241 O O   . LEU   B 2 203 ? -0.383  53.964 97.138  1.00 50.70  ? 173 LEU   B O   1 
ATOM   4242 C CB  . LEU   B 2 203 ? 1.314   51.194 96.760  1.00 52.99  ? 173 LEU   B CB  1 
ATOM   4243 C CG  . LEU   B 2 203 ? 1.264   51.611 95.283  1.00 54.74  ? 173 LEU   B CG  1 
ATOM   4244 C CD1 . LEU   B 2 203 ? 2.337   52.644 94.944  1.00 55.24  ? 173 LEU   B CD1 1 
ATOM   4245 C CD2 . LEU   B 2 203 ? 1.455   50.423 94.382  1.00 55.51  ? 173 LEU   B CD2 1 
ATOM   4246 N N   . PRO   B 2 204 ? -1.210  52.395 98.522  1.00 49.25  ? 174 PRO   B N   1 
ATOM   4247 C CA  . PRO   B 2 204 ? -2.544  53.025 98.496  1.00 48.11  ? 174 PRO   B CA  1 
ATOM   4248 C C   . PRO   B 2 204 ? -2.567  54.516 98.868  1.00 46.55  ? 174 PRO   B C   1 
ATOM   4249 O O   . PRO   B 2 204 ? -3.278  55.291 98.234  1.00 46.54  ? 174 PRO   B O   1 
ATOM   4250 C CB  . PRO   B 2 204 ? -3.358  52.161 99.465  1.00 48.74  ? 174 PRO   B CB  1 
ATOM   4251 C CG  . PRO   B 2 204 ? -2.678  50.862 99.469  1.00 49.34  ? 174 PRO   B CG  1 
ATOM   4252 C CD  . PRO   B 2 204 ? -1.225  51.167 99.343  1.00 48.31  ? 174 PRO   B CD  1 
ATOM   4253 N N   . LEU   B 2 205 ? -1.771  54.919 99.869  1.00 45.05  ? 175 LEU   B N   1 
ATOM   4254 C CA  . LEU   B 2 205 ? -1.701  56.307 100.319 1.00 43.77  ? 175 LEU   B CA  1 
ATOM   4255 C C   . LEU   B 2 205 ? -0.843  57.140 99.404  1.00 42.68  ? 175 LEU   B C   1 
ATOM   4256 O O   . LEU   B 2 205 ? -1.259  58.228 99.029  1.00 42.92  ? 175 LEU   B O   1 
ATOM   4257 C CB  . LEU   B 2 205 ? -1.167  56.375 101.751 1.00 43.79  ? 175 LEU   B CB  1 
ATOM   4258 C CG  . LEU   B 2 205 ? -0.896  57.756 102.328 1.00 45.14  ? 175 LEU   B CG  1 
ATOM   4259 C CD1 . LEU   B 2 205 ? -2.160  58.598 102.374 1.00 45.53  ? 175 LEU   B CD1 1 
ATOM   4260 C CD2 . LEU   B 2 205 ? -0.330  57.635 103.697 1.00 45.88  ? 175 LEU   B CD2 1 
ATOM   4261 N N   . ALA   B 2 206 ? 0.344   56.648 99.023  1.00 41.66  ? 176 ALA   B N   1 
ATOM   4262 C CA  . ALA   B 2 206 ? 1.245   57.390 98.140  1.00 41.04  ? 176 ALA   B CA  1 
ATOM   4263 C C   . ALA   B 2 206 ? 0.585   57.654 96.804  1.00 40.73  ? 176 ALA   B C   1 
ATOM   4264 O O   . ALA   B 2 206 ? 0.664   58.766 96.308  1.00 40.69  ? 176 ALA   B O   1 
ATOM   4265 C CB  . ALA   B 2 206 ? 2.545   56.634 97.946  1.00 40.90  ? 176 ALA   B CB  1 
ATOM   4266 N N   . TRP   B 2 207 ? -0.144  56.668 96.273  1.00 40.65  ? 177 TRP   B N   1 
ATOM   4267 C CA  . TRP   B 2 207 ? -0.882  56.789 95.016  1.00 40.99  ? 177 TRP   B CA  1 
ATOM   4268 C C   . TRP   B 2 207 ? -1.940  57.881 95.154  1.00 39.95  ? 177 TRP   B C   1 
ATOM   4269 O O   . TRP   B 2 207 ? -2.076  58.716 94.257  1.00 40.46  ? 177 TRP   B O   1 
ATOM   4270 C CB  . TRP   B 2 207 ? -1.522  55.438 94.639  1.00 41.73  ? 177 TRP   B CB  1 
ATOM   4271 C CG  . TRP   B 2 207 ? -2.252  55.432 93.333  1.00 43.53  ? 177 TRP   B CG  1 
ATOM   4272 C CD1 . TRP   B 2 207 ? -3.517  55.887 93.092  1.00 44.76  ? 177 TRP   B CD1 1 
ATOM   4273 C CD2 . TRP   B 2 207 ? -1.798  54.842 92.108  1.00 44.50  ? 177 TRP   B CD2 1 
ATOM   4274 N NE1 . TRP   B 2 207 ? -3.855  55.677 91.773  1.00 45.36  ? 177 TRP   B NE1 1 
ATOM   4275 C CE2 . TRP   B 2 207 ? -2.827  55.011 91.153  1.00 45.26  ? 177 TRP   B CE2 1 
ATOM   4276 C CE3 . TRP   B 2 207 ? -0.619  54.181 91.723  1.00 45.16  ? 177 TRP   B CE3 1 
ATOM   4277 C CZ2 . TRP   B 2 207 ? -2.711  54.545 89.844  1.00 45.65  ? 177 TRP   B CZ2 1 
ATOM   4278 C CZ3 . TRP   B 2 207 ? -0.505  53.729 90.422  1.00 45.74  ? 177 TRP   B CZ3 1 
ATOM   4279 C CH2 . TRP   B 2 207 ? -1.538  53.922 89.498  1.00 45.84  ? 177 TRP   B CH2 1 
ATOM   4280 N N   . ARG   B 2 208 ? -2.645  57.910 96.293  1.00 38.37  ? 178 ARG   B N   1 
ATOM   4281 C CA  . ARG   B 2 208 ? -3.664  58.911 96.570  1.00 37.86  ? 178 ARG   B CA  1 
ATOM   4282 C C   . ARG   B 2 208 ? -3.062  60.305 96.576  1.00 37.73  ? 178 ARG   B C   1 
ATOM   4283 O O   . ARG   B 2 208 ? -3.629  61.217 95.979  1.00 38.19  ? 178 ARG   B O   1 
ATOM   4284 C CB  . ARG   B 2 208 ? -4.359  58.605 97.903  1.00 38.60  ? 178 ARG   B CB  1 
ATOM   4285 C CG  . ARG   B 2 208 ? -5.305  59.699 98.369  1.00 39.71  ? 178 ARG   B CG  1 
ATOM   4286 C CD  . ARG   B 2 208 ? -4.727  60.445 99.539  1.00 40.47  ? 178 ARG   B CD  1 
ATOM   4287 N NE  . ARG   B 2 208 ? -5.365  61.743 99.661  1.00 40.77  ? 178 ARG   B NE  1 
ATOM   4288 C CZ  . ARG   B 2 208 ? -6.332  62.034 100.520 1.00 40.49  ? 178 ARG   B CZ  1 
ATOM   4289 N NH1 . ARG   B 2 208 ? -6.862  63.248 100.541 1.00 40.25  ? 178 ARG   B NH1 1 
ATOM   4290 N NH2 . ARG   B 2 208 ? -6.777  61.112 101.368 1.00 37.77  ? 178 ARG   B NH2 1 
ATOM   4291 N N   . ILE   B 2 209 ? -1.909  60.471 97.234  1.00 36.97  ? 179 ILE   B N   1 
ATOM   4292 C CA  . ILE   B 2 209 ? -1.214  61.750 97.276  1.00 36.44  ? 179 ILE   B CA  1 
ATOM   4293 C C   . ILE   B 2 209 ? -0.772  62.167 95.875  1.00 36.71  ? 179 ILE   B C   1 
ATOM   4294 O O   . ILE   B 2 209 ? -0.917  63.335 95.541  1.00 37.32  ? 179 ILE   B O   1 
ATOM   4295 C CB  . ILE   B 2 209 ? -0.080  61.732 98.319  1.00 36.02  ? 179 ILE   B CB  1 
ATOM   4296 C CG1 . ILE   B 2 209 ? -0.659  61.415 99.727  1.00 36.10  ? 179 ILE   B CG1 1 
ATOM   4297 C CG2 . ILE   B 2 209 ? 0.686   63.045 98.308  1.00 36.08  ? 179 ILE   B CG2 1 
ATOM   4298 C CD1 . ILE   B 2 209 ? 0.369   61.225 100.832 1.00 36.70  ? 179 ILE   B CD1 1 
ATOM   4299 N N   . VAL   B 2 210 ? -0.387  61.213 95.008  1.00 36.58  ? 180 VAL   B N   1 
ATOM   4300 C CA  . VAL   B 2 210 ? -0.048  61.510 93.612  1.00 37.28  ? 180 VAL   B CA  1 
ATOM   4301 C C   . VAL   B 2 210 ? -1.260  62.120 92.883  1.00 38.39  ? 180 VAL   B C   1 
ATOM   4302 O O   . VAL   B 2 210 ? -1.095  63.097 92.147  1.00 38.94  ? 180 VAL   B O   1 
ATOM   4303 C CB  . VAL   B 2 210 ? 0.553   60.304 92.852  1.00 37.45  ? 180 VAL   B CB  1 
ATOM   4304 C CG1 . VAL   B 2 210 ? 0.711   60.614 91.370  1.00 37.90  ? 180 VAL   B CG1 1 
ATOM   4305 C CG2 . VAL   B 2 210 ? 1.892   59.905 93.443  1.00 37.61  ? 180 VAL   B CG2 1 
ATOM   4306 N N   . ASN   B 2 211 ? -2.480  61.603 93.151  1.00 38.25  ? 181 ASN   B N   1 
ATOM   4307 C CA  . ASN   B 2 211 ? -3.717  62.135 92.572  1.00 38.43  ? 181 ASN   B CA  1 
ATOM   4308 C C   . ASN   B 2 211 ? -3.915  63.570 93.008  1.00 39.97  ? 181 ASN   B C   1 
ATOM   4309 O O   . ASN   B 2 211 ? -4.330  64.397 92.200  1.00 40.66  ? 181 ASN   B O   1 
ATOM   4310 C CB  . ASN   B 2 211 ? -4.942  61.331 93.019  1.00 38.31  ? 181 ASN   B CB  1 
ATOM   4311 C CG  . ASN   B 2 211 ? -4.950  59.895 92.583  1.00 39.89  ? 181 ASN   B CG  1 
ATOM   4312 O OD1 . ASN   B 2 211 ? -4.367  59.531 91.568  1.00 40.92  ? 181 ASN   B OD1 1 
ATOM   4313 N ND2 . ASN   B 2 211 ? -5.618  59.048 93.341  1.00 39.40  ? 181 ASN   B ND2 1 
ATOM   4314 N N   . ASP   B 2 212 ? -3.642  63.865 94.290  1.00 40.35  ? 182 ASP   B N   1 
ATOM   4315 C CA  . ASP   B 2 212 ? -3.823  65.186 94.868  1.00 41.19  ? 182 ASP   B CA  1 
ATOM   4316 C C   . ASP   B 2 212 ? -2.868  66.208 94.279  1.00 41.99  ? 182 ASP   B C   1 
ATOM   4317 O O   . ASP   B 2 212 ? -3.261  67.370 94.120  1.00 42.17  ? 182 ASP   B O   1 
ATOM   4318 C CB  . ASP   B 2 212 ? -3.670  65.132 96.391  1.00 43.00  ? 182 ASP   B CB  1 
ATOM   4319 C CG  . ASP   B 2 212 ? -4.728  64.324 97.110  1.00 47.88  ? 182 ASP   B CG  1 
ATOM   4320 O OD1 . ASP   B 2 212 ? -5.774  64.040 96.500  1.00 49.27  ? 182 ASP   B OD1 1 
ATOM   4321 O OD2 . ASP   B 2 212 ? -4.511  63.979 98.279  1.00 49.45  ? 182 ASP   B OD2 1 
ATOM   4322 N N   . THR   B 2 213 ? -1.632  65.799 93.918  1.00 41.98  ? 183 THR   B N   1 
ATOM   4323 C CA  . THR   B 2 213 ? -0.696  66.762 93.324  1.00 42.77  ? 183 THR   B CA  1 
ATOM   4324 C C   . THR   B 2 213 ? -1.233  67.401 92.037  1.00 43.53  ? 183 THR   B C   1 
ATOM   4325 O O   . THR   B 2 213 ? -0.707  68.428 91.608  1.00 43.99  ? 183 THR   B O   1 
ATOM   4326 C CB  . THR   B 2 213 ? 0.692   66.172 93.130  1.00 44.31  ? 183 THR   B CB  1 
ATOM   4327 O OG1 . THR   B 2 213 ? 0.638   65.043 92.249  1.00 45.46  ? 183 THR   B OG1 1 
ATOM   4328 C CG2 . THR   B 2 213 ? 1.349   65.811 94.441  1.00 44.58  ? 183 THR   B CG2 1 
ATOM   4329 N N   . TYR   B 2 214 ? -2.285  66.813 91.425  1.00 43.40  ? 184 TYR   B N   1 
ATOM   4330 C CA  . TYR   B 2 214 ? -2.881  67.386 90.228  1.00 43.64  ? 184 TYR   B CA  1 
ATOM   4331 C C   . TYR   B 2 214 ? -3.765  68.574 90.529  1.00 44.36  ? 184 TYR   B C   1 
ATOM   4332 O O   . TYR   B 2 214 ? -4.110  69.299 89.614  1.00 45.14  ? 184 TYR   B O   1 
ATOM   4333 C CB  . TYR   B 2 214 ? -3.605  66.344 89.378  1.00 43.63  ? 184 TYR   B CB  1 
ATOM   4334 C CG  . TYR   B 2 214 ? -2.665  65.405 88.653  1.00 44.00  ? 184 TYR   B CG  1 
ATOM   4335 C CD1 . TYR   B 2 214 ? -2.161  64.279 89.280  1.00 44.99  ? 184 TYR   B CD1 1 
ATOM   4336 C CD2 . TYR   B 2 214 ? -2.291  65.641 87.336  1.00 44.57  ? 184 TYR   B CD2 1 
ATOM   4337 C CE1 . TYR   B 2 214 ? -1.286  63.418 88.627  1.00 46.12  ? 184 TYR   B CE1 1 
ATOM   4338 C CE2 . TYR   B 2 214 ? -1.423  64.786 86.669  1.00 45.51  ? 184 TYR   B CE2 1 
ATOM   4339 C CZ  . TYR   B 2 214 ? -0.911  63.677 87.323  1.00 46.76  ? 184 TYR   B CZ  1 
ATOM   4340 O OH  . TYR   B 2 214 ? -0.053  62.798 86.693  1.00 47.92  ? 184 TYR   B OH  1 
ATOM   4341 N N   . ARG   B 2 215 ? -4.108  68.823 91.793  1.00 44.16  ? 185 ARG   B N   1 
ATOM   4342 C CA  . ARG   B 2 215 ? -4.848  70.027 92.178  1.00 44.17  ? 185 ARG   B CA  1 
ATOM   4343 C C   . ARG   B 2 215 ? -3.899  71.278 92.137  1.00 43.58  ? 185 ARG   B C   1 
ATOM   4344 O O   . ARG   B 2 215 ? -4.385  72.405 92.199  1.00 44.08  ? 185 ARG   B O   1 
ATOM   4345 C CB  . ARG   B 2 215 ? -5.420  69.852 93.603  1.00 46.00  ? 185 ARG   B CB  1 
ATOM   4346 C CG  . ARG   B 2 215 ? -6.759  69.116 93.698  1.00 50.17  ? 185 ARG   B CG  1 
ATOM   4347 C CD  . ARG   B 2 215 ? -6.709  67.637 93.342  1.00 54.64  ? 185 ARG   B CD  1 
ATOM   4348 N NE  . ARG   B 2 215 ? -8.031  67.085 93.005  1.00 58.02  ? 185 ARG   B NE  1 
ATOM   4349 C CZ  . ARG   B 2 215 ? -8.222  65.914 92.394  1.00 59.87  ? 185 ARG   B CZ  1 
ATOM   4350 N NH1 . ARG   B 2 215 ? -7.184  65.144 92.076  1.00 58.80  ? 185 ARG   B NH1 1 
ATOM   4351 N NH2 . ARG   B 2 215 ? -9.453  65.492 92.125  1.00 59.51  ? 185 ARG   B NH2 1 
ATOM   4352 N N   . THR   B 2 216 ? -2.553  71.068 92.021  1.00 42.54  ? 186 THR   B N   1 
ATOM   4353 C CA  . THR   B 2 216 ? -1.472  72.070 92.039  1.00 41.81  ? 186 THR   B CA  1 
ATOM   4354 C C   . THR   B 2 216 ? -0.692  72.140 90.693  1.00 41.69  ? 186 THR   B C   1 
ATOM   4355 O O   . THR   B 2 216 ? -0.873  71.283 89.842  1.00 42.32  ? 186 THR   B O   1 
ATOM   4356 C CB  . THR   B 2 216 ? -0.500  71.705 93.193  1.00 42.18  ? 186 THR   B CB  1 
ATOM   4357 O OG1 . THR   B 2 216 ? 0.275   70.582 92.793  1.00 42.17  ? 186 THR   B OG1 1 
ATOM   4358 C CG2 . THR   B 2 216 ? -1.210  71.410 94.526  1.00 42.69  ? 186 THR   B CG2 1 
ATOM   4359 N N   . ASP   B 2 217 ? 0.232   73.099 90.538  1.00 41.14  ? 187 ASP   B N   1 
ATOM   4360 C CA  . ASP   B 2 217 ? 1.038   73.232 89.325  1.00 41.29  ? 187 ASP   B CA  1 
ATOM   4361 C C   . ASP   B 2 217 ? 2.256   72.313 89.277  1.00 40.76  ? 187 ASP   B C   1 
ATOM   4362 O O   . ASP   B 2 217 ? 3.079   72.474 88.376  1.00 41.13  ? 187 ASP   B O   1 
ATOM   4363 C CB  . ASP   B 2 217 ? 1.541   74.675 89.197  1.00 43.92  ? 187 ASP   B CB  1 
ATOM   4364 C CG  . ASP   B 2 217 ? 0.447   75.708 89.022  1.00 51.59  ? 187 ASP   B CG  1 
ATOM   4365 O OD1 . ASP   B 2 217 ? -0.614  75.362 88.437  1.00 53.72  ? 187 ASP   B OD1 1 
ATOM   4366 O OD2 . ASP   B 2 217 ? 0.652   76.872 89.453  1.00 53.92  ? 187 ASP   B OD2 1 
ATOM   4367 N N   . LEU   B 2 218 ? 2.405   71.380 90.228  1.00 39.89  ? 188 LEU   B N   1 
ATOM   4368 C CA  . LEU   B 2 218 ? 3.598   70.533 90.314  1.00 39.52  ? 188 LEU   B CA  1 
ATOM   4369 C C   . LEU   B 2 218 ? 3.960   69.802 89.037  1.00 39.30  ? 188 LEU   B C   1 
ATOM   4370 O O   . LEU   B 2 218 ? 5.143   69.704 88.726  1.00 39.71  ? 188 LEU   B O   1 
ATOM   4371 C CB  . LEU   B 2 218 ? 3.516   69.548 91.476  1.00 39.48  ? 188 LEU   B CB  1 
ATOM   4372 C CG  . LEU   B 2 218 ? 3.611   70.182 92.853  1.00 40.83  ? 188 LEU   B CG  1 
ATOM   4373 C CD1 . LEU   B 2 218 ? 3.250   69.185 93.937  1.00 41.56  ? 188 LEU   B CD1 1 
ATOM   4374 C CD2 . LEU   B 2 218 ? 4.961   70.844 93.085  1.00 40.91  ? 188 LEU   B CD2 1 
ATOM   4375 N N   . CYS   B 2 219 ? 2.970   69.333 88.278  1.00 38.65  ? 189 CYS   B N   1 
ATOM   4376 C CA  . CYS   B 2 219 ? 3.237   68.635 87.026  1.00 38.74  ? 189 CYS   B CA  1 
ATOM   4377 C C   . CYS   B 2 219 ? 3.925   69.518 85.983  1.00 38.34  ? 189 CYS   B C   1 
ATOM   4378 O O   . CYS   B 2 219 ? 4.627   68.997 85.112  1.00 38.79  ? 189 CYS   B O   1 
ATOM   4379 C CB  . CYS   B 2 219 ? 1.974   67.976 86.472  1.00 39.89  ? 189 CYS   B CB  1 
ATOM   4380 S SG  . CYS   B 2 219 ? 0.746   69.132 85.814  1.00 43.80  ? 189 CYS   B SG  1 
ATOM   4381 N N   . LEU   B 2 220 ? 3.733   70.845 86.068  1.00 37.41  ? 190 LEU   B N   1 
ATOM   4382 C CA  . LEU   B 2 220 ? 4.347   71.785 85.138  1.00 37.11  ? 190 LEU   B CA  1 
ATOM   4383 C C   . LEU   B 2 220 ? 5.723   72.258 85.597  1.00 38.78  ? 190 LEU   B C   1 
ATOM   4384 O O   . LEU   B 2 220 ? 6.380   72.984 84.858  1.00 39.32  ? 190 LEU   B O   1 
ATOM   4385 C CB  . LEU   B 2 220 ? 3.458   73.021 84.967  1.00 35.92  ? 190 LEU   B CB  1 
ATOM   4386 C CG  . LEU   B 2 220 ? 2.047   72.834 84.419  1.00 35.72  ? 190 LEU   B CG  1 
ATOM   4387 C CD1 . LEU   B 2 220 ? 1.374   74.172 84.224  1.00 35.60  ? 190 LEU   B CD1 1 
ATOM   4388 C CD2 . LEU   B 2 220 ? 2.046   72.095 83.106  1.00 35.64  ? 190 LEU   B CD2 1 
ATOM   4389 N N   . LEU   B 2 221 ? 6.160   71.893 86.810  1.00 39.17  ? 191 LEU   B N   1 
ATOM   4390 C CA  . LEU   B 2 221 ? 7.403   72.413 87.355  1.00 39.58  ? 191 LEU   B CA  1 
ATOM   4391 C C   . LEU   B 2 221 ? 8.440   71.369 87.627  1.00 40.24  ? 191 LEU   B C   1 
ATOM   4392 O O   . LEU   B 2 221 ? 9.632   71.653 87.512  1.00 40.23  ? 191 LEU   B O   1 
ATOM   4393 C CB  . LEU   B 2 221 ? 7.084   73.164 88.656  1.00 39.35  ? 191 LEU   B CB  1 
ATOM   4394 C CG  . LEU   B 2 221 ? 6.070   74.273 88.524  1.00 39.62  ? 191 LEU   B CG  1 
ATOM   4395 C CD1 . LEU   B 2 221 ? 5.495   74.640 89.858  1.00 39.96  ? 191 LEU   B CD1 1 
ATOM   4396 C CD2 . LEU   B 2 221 ? 6.666   75.441 87.806  1.00 40.00  ? 191 LEU   B CD2 1 
ATOM   4397 N N   . TYR   B 2 222 ? 8.006   70.172 88.021  1.00 40.71  ? 192 TYR   B N   1 
ATOM   4398 C CA  . TYR   B 2 222 ? 8.943   69.123 88.401  1.00 41.69  ? 192 TYR   B CA  1 
ATOM   4399 C C   . TYR   B 2 222 ? 8.819   67.841 87.602  1.00 42.33  ? 192 TYR   B C   1 
ATOM   4400 O O   . TYR   B 2 222 ? 7.707   67.444 87.238  1.00 42.87  ? 192 TYR   B O   1 
ATOM   4401 C CB  . TYR   B 2 222 ? 8.769   68.811 89.894  1.00 41.87  ? 192 TYR   B CB  1 
ATOM   4402 C CG  . TYR   B 2 222 ? 9.036   70.002 90.786  1.00 43.08  ? 192 TYR   B CG  1 
ATOM   4403 C CD1 . TYR   B 2 222 ? 10.319  70.284 91.238  1.00 44.31  ? 192 TYR   B CD1 1 
ATOM   4404 C CD2 . TYR   B 2 222 ? 8.001   70.829 91.209  1.00 44.03  ? 192 TYR   B CD2 1 
ATOM   4405 C CE1 . TYR   B 2 222 ? 10.569  71.365 92.077  1.00 45.27  ? 192 TYR   B CE1 1 
ATOM   4406 C CE2 . TYR   B 2 222 ? 8.239   71.915 92.044  1.00 44.93  ? 192 TYR   B CE2 1 
ATOM   4407 C CZ  . TYR   B 2 222 ? 9.524   72.173 92.482  1.00 45.96  ? 192 TYR   B CZ  1 
ATOM   4408 O OH  . TYR   B 2 222 ? 9.773   73.241 93.295  1.00 47.29  ? 192 TYR   B OH  1 
ATOM   4409 N N   . PRO   B 2 223 ? 9.951   67.123 87.392  1.00 42.09  ? 193 PRO   B N   1 
ATOM   4410 C CA  . PRO   B 2 223 ? 9.871   65.809 86.722  1.00 42.20  ? 193 PRO   B CA  1 
ATOM   4411 C C   . PRO   B 2 223 ? 8.974   64.844 87.512  1.00 42.58  ? 193 PRO   B C   1 
ATOM   4412 O O   . PRO   B 2 223 ? 8.888   64.916 88.742  1.00 42.66  ? 193 PRO   B O   1 
ATOM   4413 C CB  . PRO   B 2 223 ? 11.333  65.322 86.700  1.00 42.65  ? 193 PRO   B CB  1 
ATOM   4414 C CG  . PRO   B 2 223 ? 12.149  66.547 86.926  1.00 42.76  ? 193 PRO   B CG  1 
ATOM   4415 C CD  . PRO   B 2 223 ? 11.335  67.448 87.787  1.00 41.13  ? 193 PRO   B CD  1 
ATOM   4416 N N   . PRO   B 2 224 ? 8.260   63.956 86.811  1.00 42.58  ? 194 PRO   B N   1 
ATOM   4417 C CA  . PRO   B 2 224 ? 7.342   63.038 87.503  1.00 42.31  ? 194 PRO   B CA  1 
ATOM   4418 C C   . PRO   B 2 224 ? 7.967   62.203 88.611  1.00 42.10  ? 194 PRO   B C   1 
ATOM   4419 O O   . PRO   B 2 224 ? 7.346   62.069 89.652  1.00 42.61  ? 194 PRO   B O   1 
ATOM   4420 C CB  . PRO   B 2 224 ? 6.809   62.163 86.375  1.00 43.14  ? 194 PRO   B CB  1 
ATOM   4421 C CG  . PRO   B 2 224 ? 6.954   62.999 85.165  1.00 43.82  ? 194 PRO   B CG  1 
ATOM   4422 C CD  . PRO   B 2 224 ? 8.223   63.755 85.352  1.00 42.17  ? 194 PRO   B CD  1 
ATOM   4423 N N   . PHE   B 2 225 ? 9.184   61.665 88.420  1.00 41.41  ? 195 PHE   B N   1 
ATOM   4424 C CA  . PHE   B 2 225 ? 9.837   60.864 89.461  1.00 41.15  ? 195 PHE   B CA  1 
ATOM   4425 C C   . PHE   B 2 225 ? 10.079  61.657 90.756  1.00 41.01  ? 195 PHE   B C   1 
ATOM   4426 O O   . PHE   B 2 225 ? 10.122  61.066 91.840  1.00 40.99  ? 195 PHE   B O   1 
ATOM   4427 C CB  . PHE   B 2 225 ? 11.139  60.234 88.950  1.00 40.85  ? 195 PHE   B CB  1 
ATOM   4428 C CG  . PHE   B 2 225 ? 12.334  61.148 88.978  1.00 41.50  ? 195 PHE   B CG  1 
ATOM   4429 C CD1 . PHE   B 2 225 ? 12.584  62.019 87.931  1.00 42.36  ? 195 PHE   B CD1 1 
ATOM   4430 C CD2 . PHE   B 2 225 ? 13.200  61.151 90.062  1.00 42.24  ? 195 PHE   B CD2 1 
ATOM   4431 C CE1 . PHE   B 2 225 ? 13.672  62.878 87.970  1.00 42.94  ? 195 PHE   B CE1 1 
ATOM   4432 C CE2 . PHE   B 2 225 ? 14.284  62.016 90.101  1.00 42.87  ? 195 PHE   B CE2 1 
ATOM   4433 C CZ  . PHE   B 2 225 ? 14.525  62.858 89.043  1.00 42.68  ? 195 PHE   B CZ  1 
ATOM   4434 N N   . MET   B 2 226 ? 10.237  62.989 90.640  1.00 40.40  ? 196 MET   B N   1 
ATOM   4435 C CA  . MET   B 2 226 ? 10.446  63.820 91.804  1.00 40.50  ? 196 MET   B CA  1 
ATOM   4436 C C   . MET   B 2 226 ? 9.159   63.995 92.574  1.00 40.43  ? 196 MET   B C   1 
ATOM   4437 O O   . MET   B 2 226 ? 9.172   63.897 93.796  1.00 41.11  ? 196 MET   B O   1 
ATOM   4438 C CB  . MET   B 2 226 ? 11.078  65.148 91.423  1.00 41.74  ? 196 MET   B CB  1 
ATOM   4439 C CG  . MET   B 2 226 ? 12.562  65.033 91.217  1.00 45.60  ? 196 MET   B CG  1 
ATOM   4440 S SD  . MET   B 2 226 ? 13.326  66.623 90.856  1.00 56.95  ? 196 MET   B SD  1 
ATOM   4441 C CE  . MET   B 2 226 ? 15.021  66.102 90.532  1.00 56.38  ? 196 MET   B CE  1 
ATOM   4442 N N   . ILE   B 2 227 ? 8.033   64.189 91.881  1.00 39.70  ? 197 ILE   B N   1 
ATOM   4443 C CA  . ILE   B 2 227 ? 6.728   64.287 92.544  1.00 39.51  ? 197 ILE   B CA  1 
ATOM   4444 C C   . ILE   B 2 227 ? 6.396   62.929 93.209  1.00 40.61  ? 197 ILE   B C   1 
ATOM   4445 O O   . ILE   B 2 227 ? 5.842   62.898 94.302  1.00 41.28  ? 197 ILE   B O   1 
ATOM   4446 C CB  . ILE   B 2 227 ? 5.640   64.719 91.528  1.00 38.96  ? 197 ILE   B CB  1 
ATOM   4447 C CG1 . ILE   B 2 227 ? 6.060   66.007 90.786  1.00 39.19  ? 197 ILE   B CG1 1 
ATOM   4448 C CG2 . ILE   B 2 227 ? 4.273   64.864 92.196  1.00 38.93  ? 197 ILE   B CG2 1 
ATOM   4449 C CD1 . ILE   B 2 227 ? 5.210   66.369 89.661  1.00 39.82  ? 197 ILE   B CD1 1 
ATOM   4450 N N   . ALA   B 2 228 ? 6.783   61.815 92.570  1.00 40.44  ? 198 ALA   B N   1 
ATOM   4451 C CA  . ALA   B 2 228 ? 6.593   60.482 93.098  1.00 40.82  ? 198 ALA   B CA  1 
ATOM   4452 C C   . ALA   B 2 228 ? 7.353   60.316 94.428  1.00 41.09  ? 198 ALA   B C   1 
ATOM   4453 O O   . ALA   B 2 228 ? 6.787   59.786 95.382  1.00 41.56  ? 198 ALA   B O   1 
ATOM   4454 C CB  . ALA   B 2 228 ? 7.075   59.462 92.082  1.00 41.15  ? 198 ALA   B CB  1 
ATOM   4455 N N   . LEU   B 2 229 ? 8.620   60.779 94.498  1.00 40.41  ? 199 LEU   B N   1 
ATOM   4456 C CA  . LEU   B 2 229 ? 9.440   60.715 95.711  1.00 40.12  ? 199 LEU   B CA  1 
ATOM   4457 C C   . LEU   B 2 229 ? 8.858   61.583 96.805  1.00 39.83  ? 199 LEU   B C   1 
ATOM   4458 O O   . LEU   B 2 229 ? 8.931   61.219 97.971  1.00 39.87  ? 199 LEU   B O   1 
ATOM   4459 C CB  . LEU   B 2 229 ? 10.881  61.174 95.426  1.00 40.45  ? 199 LEU   B CB  1 
ATOM   4460 C CG  . LEU   B 2 229 ? 11.718  60.217 94.606  1.00 41.99  ? 199 LEU   B CG  1 
ATOM   4461 C CD1 . LEU   B 2 229 ? 12.956  60.884 94.060  1.00 42.47  ? 199 LEU   B CD1 1 
ATOM   4462 C CD2 . LEU   B 2 229 ? 12.035  58.975 95.384  1.00 42.66  ? 199 LEU   B CD2 1 
ATOM   4463 N N   . ALA   B 2 230 ? 8.319   62.748 96.442  1.00 39.63  ? 200 ALA   B N   1 
ATOM   4464 C CA  . ALA   B 2 230 ? 7.718   63.645 97.407  1.00 40.32  ? 200 ALA   B CA  1 
ATOM   4465 C C   . ALA   B 2 230 ? 6.453   63.013 97.978  1.00 41.61  ? 200 ALA   B C   1 
ATOM   4466 O O   . ALA   B 2 230 ? 6.298   62.980 99.196  1.00 42.17  ? 200 ALA   B O   1 
ATOM   4467 C CB  . ALA   B 2 230 ? 7.407   64.972 96.755  1.00 40.13  ? 200 ALA   B CB  1 
ATOM   4468 N N   . CYS   B 2 231 ? 5.605   62.416 97.117  1.00 41.97  ? 201 CYS   B N   1 
ATOM   4469 C CA  . CYS   B 2 231 ? 4.373   61.737 97.517  1.00 42.79  ? 201 CYS   B CA  1 
ATOM   4470 C C   . CYS   B 2 231 ? 4.627   60.529 98.375  1.00 43.22  ? 201 CYS   B C   1 
ATOM   4471 O O   . CYS   B 2 231 ? 3.862   60.268 99.298  1.00 43.50  ? 201 CYS   B O   1 
ATOM   4472 C CB  . CYS   B 2 231 ? 3.545   61.375 96.298  1.00 43.57  ? 201 CYS   B CB  1 
ATOM   4473 S SG  . CYS   B 2 231 ? 2.829   62.801 95.471  1.00 46.82  ? 201 CYS   B SG  1 
ATOM   4474 N N   . LEU   B 2 232 ? 5.686   59.791 98.068  1.00 43.28  ? 202 LEU   B N   1 
ATOM   4475 C CA  . LEU   B 2 232 ? 6.105   58.641 98.857  1.00 44.07  ? 202 LEU   B CA  1 
ATOM   4476 C C   . LEU   B 2 232 ? 6.633   59.097 100.230 1.00 44.58  ? 202 LEU   B C   1 
ATOM   4477 O O   . LEU   B 2 232 ? 6.412   58.405 101.231 1.00 44.80  ? 202 LEU   B O   1 
ATOM   4478 C CB  . LEU   B 2 232 ? 7.199   57.865 98.108  1.00 44.10  ? 202 LEU   B CB  1 
ATOM   4479 C CG  . LEU   B 2 232 ? 7.699   56.598 98.766  1.00 45.34  ? 202 LEU   B CG  1 
ATOM   4480 C CD1 . LEU   B 2 232 ? 6.557   55.648 99.067  1.00 45.98  ? 202 LEU   B CD1 1 
ATOM   4481 C CD2 . LEU   B 2 232 ? 8.737   55.907 97.895  1.00 45.78  ? 202 LEU   B CD2 1 
ATOM   4482 N N   . HIS   B 2 233 ? 7.309   60.265 100.274 1.00 44.32  ? 203 HIS   B N   1 
ATOM   4483 C CA  . HIS   B 2 233 ? 7.836   60.801 101.511 1.00 45.14  ? 203 HIS   B CA  1 
ATOM   4484 C C   . HIS   B 2 233 ? 6.719   61.177 102.442 1.00 45.39  ? 203 HIS   B C   1 
ATOM   4485 O O   . HIS   B 2 233 ? 6.763   60.757 103.593 1.00 45.99  ? 203 HIS   B O   1 
ATOM   4486 C CB  . HIS   B 2 233 ? 8.760   62.009 101.286 1.00 46.73  ? 203 HIS   B CB  1 
ATOM   4487 C CG  . HIS   B 2 233 ? 9.409   62.495 102.553 1.00 50.10  ? 203 HIS   B CG  1 
ATOM   4488 N ND1 . HIS   B 2 233 ? 10.691  62.092 102.912 1.00 52.16  ? 203 HIS   B ND1 1 
ATOM   4489 C CD2 . HIS   B 2 233 ? 8.921   63.310 103.521 1.00 51.44  ? 203 HIS   B CD2 1 
ATOM   4490 C CE1 . HIS   B 2 233 ? 10.941  62.685 104.068 1.00 52.77  ? 203 HIS   B CE1 1 
ATOM   4491 N NE2 . HIS   B 2 233 ? 9.902   63.420 104.479 1.00 52.62  ? 203 HIS   B NE2 1 
ATOM   4492 N N   . VAL   B 2 234 ? 5.718   61.964 101.976 1.00 44.67  ? 204 VAL   B N   1 
ATOM   4493 C CA  . VAL   B 2 234 ? 4.591   62.377 102.818 1.00 44.28  ? 204 VAL   B CA  1 
ATOM   4494 C C   . VAL   B 2 234 ? 3.830   61.141 103.313 1.00 44.84  ? 204 VAL   B C   1 
ATOM   4495 O O   . VAL   B 2 234 ? 3.468   61.086 104.477 1.00 44.90  ? 204 VAL   B O   1 
ATOM   4496 C CB  . VAL   B 2 234 ? 3.667   63.384 102.093 1.00 44.25  ? 204 VAL   B CB  1 
ATOM   4497 C CG1 . VAL   B 2 234 ? 2.538   63.853 102.999 1.00 44.42  ? 204 VAL   B CG1 1 
ATOM   4498 C CG2 . VAL   B 2 234 ? 4.455   64.575 101.572 1.00 44.43  ? 204 VAL   B CG2 1 
ATOM   4499 N N   . ALA   B 2 235 ? 3.683   60.111 102.461 1.00 45.10  ? 205 ALA   B N   1 
ATOM   4500 C CA  . ALA   B 2 235 ? 3.023   58.862 102.832 1.00 45.84  ? 205 ALA   B CA  1 
ATOM   4501 C C   . ALA   B 2 235 ? 3.757   58.154 103.977 1.00 46.81  ? 205 ALA   B C   1 
ATOM   4502 O O   . ALA   B 2 235 ? 3.104   57.581 104.848 1.00 47.13  ? 205 ALA   B O   1 
ATOM   4503 C CB  . ALA   B 2 235 ? 2.931   57.941 101.627 1.00 45.77  ? 205 ALA   B CB  1 
ATOM   4504 N N   . CYS   B 2 236 ? 5.113   58.196 103.962 1.00 46.97  ? 206 CYS   B N   1 
ATOM   4505 C CA  . CYS   B 2 236 ? 6.021   57.623 104.969 1.00 47.25  ? 206 CYS   B CA  1 
ATOM   4506 C C   . CYS   B 2 236 ? 5.872   58.348 106.298 1.00 47.55  ? 206 CYS   B C   1 
ATOM   4507 O O   . CYS   B 2 236 ? 5.961   57.716 107.341 1.00 47.78  ? 206 CYS   B O   1 
ATOM   4508 C CB  . CYS   B 2 236 ? 7.468   57.682 104.485 1.00 47.92  ? 206 CYS   B CB  1 
ATOM   4509 S SG  . CYS   B 2 236 ? 8.002   56.240 103.535 1.00 51.73  ? 206 CYS   B SG  1 
ATOM   4510 N N   . VAL   B 2 237 ? 5.714   59.685 106.256 1.00 47.41  ? 207 VAL   B N   1 
ATOM   4511 C CA  . VAL   B 2 237 ? 5.545   60.528 107.430 1.00 47.73  ? 207 VAL   B CA  1 
ATOM   4512 C C   . VAL   B 2 237 ? 4.198   60.162 108.077 1.00 49.10  ? 207 VAL   B C   1 
ATOM   4513 O O   . VAL   B 2 237 ? 4.165   59.783 109.253 1.00 49.35  ? 207 VAL   B O   1 
ATOM   4514 C CB  . VAL   B 2 237 ? 5.595   62.032 107.039 1.00 47.72  ? 207 VAL   B CB  1 
ATOM   4515 C CG1 . VAL   B 2 237 ? 5.086   62.915 108.165 1.00 48.18  ? 207 VAL   B CG1 1 
ATOM   4516 C CG2 . VAL   B 2 237 ? 6.979   62.462 106.594 1.00 48.16  ? 207 VAL   B CG2 1 
ATOM   4517 N N   . VAL   B 2 238 ? 3.104   60.210 107.271 1.00 49.76  ? 208 VAL   B N   1 
ATOM   4518 C CA  . VAL   B 2 238 ? 1.720   59.954 107.646 1.00 50.25  ? 208 VAL   B CA  1 
ATOM   4519 C C   . VAL   B 2 238 ? 1.561   58.600 108.312 1.00 52.37  ? 208 VAL   B C   1 
ATOM   4520 O O   . VAL   B 2 238 ? 0.920   58.518 109.364 1.00 52.81  ? 208 VAL   B O   1 
ATOM   4521 C CB  . VAL   B 2 238 ? 0.778   60.158 106.432 1.00 49.64  ? 208 VAL   B CB  1 
ATOM   4522 C CG1 . VAL   B 2 238 ? -0.599  59.553 106.672 1.00 49.86  ? 208 VAL   B CG1 1 
ATOM   4523 C CG2 . VAL   B 2 238 ? 0.660   61.636 106.081 1.00 49.43  ? 208 VAL   B CG2 1 
ATOM   4524 N N   . GLN   B 2 239 ? 2.185   57.555 107.752 1.00 53.44  ? 209 GLN   B N   1 
ATOM   4525 C CA  . GLN   B 2 239 ? 2.067   56.225 108.337 1.00 55.44  ? 209 GLN   B CA  1 
ATOM   4526 C C   . GLN   B 2 239 ? 3.146   55.876 109.373 1.00 57.26  ? 209 GLN   B C   1 
ATOM   4527 O O   . GLN   B 2 239 ? 3.106   54.776 109.937 1.00 57.88  ? 209 GLN   B O   1 
ATOM   4528 C CB  . GLN   B 2 239 ? 2.010   55.163 107.248 1.00 57.60  ? 209 GLN   B CB  1 
ATOM   4529 C CG  . GLN   B 2 239 ? 0.914   55.418 106.242 1.00 62.20  ? 209 GLN   B CG  1 
ATOM   4530 C CD  . GLN   B 2 239 ? 0.615   54.171 105.465 1.00 68.28  ? 209 GLN   B CD  1 
ATOM   4531 O OE1 . GLN   B 2 239 ? 0.428   53.097 106.038 1.00 70.72  ? 209 GLN   B OE1 1 
ATOM   4532 N NE2 . GLN   B 2 239 ? 0.563   54.278 104.144 1.00 68.79  ? 209 GLN   B NE2 1 
ATOM   4533 N N   . GLN   B 2 240 ? 4.097   56.791 109.619 1.00 57.96  ? 210 GLN   B N   1 
ATOM   4534 C CA  . GLN   B 2 240 ? 5.185   56.624 110.579 1.00 59.29  ? 210 GLN   B CA  1 
ATOM   4535 C C   . GLN   B 2 240 ? 6.125   55.462 110.236 1.00 60.56  ? 210 GLN   B C   1 
ATOM   4536 O O   . GLN   B 2 240 ? 6.503   54.661 111.094 1.00 61.21  ? 210 GLN   B O   1 
ATOM   4537 C CB  . GLN   B 2 240 ? 4.651   56.535 111.998 1.00 61.01  ? 210 GLN   B CB  1 
ATOM   4538 C CG  . GLN   B 2 240 ? 3.989   57.833 112.398 1.00 65.39  ? 210 GLN   B CG  1 
ATOM   4539 C CD  . GLN   B 2 240 ? 3.344   57.727 113.745 1.00 71.12  ? 210 GLN   B CD  1 
ATOM   4540 O OE1 . GLN   B 2 240 ? 3.842   57.040 114.647 1.00 73.09  ? 210 GLN   B OE1 1 
ATOM   4541 N NE2 . GLN   B 2 240 ? 2.217   58.412 113.909 1.00 72.06  ? 210 GLN   B NE2 1 
ATOM   4542 N N   . LYS   B 2 241 ? 6.494   55.387 108.961 1.00 60.63  ? 211 LYS   B N   1 
ATOM   4543 C CA  . LYS   B 2 241 ? 7.420   54.411 108.418 1.00 61.02  ? 211 LYS   B CA  1 
ATOM   4544 C C   . LYS   B 2 241 ? 8.758   55.160 108.259 1.00 61.76  ? 211 LYS   B C   1 
ATOM   4545 O O   . LYS   B 2 241 ? 8.797   56.249 107.685 1.00 62.06  ? 211 LYS   B O   1 
ATOM   4546 C CB  . LYS   B 2 241 ? 6.877   53.894 107.075 1.00 62.42  ? 211 LYS   B CB  1 
ATOM   4547 C CG  . LYS   B 2 241 ? 7.890   53.185 106.200 1.00 66.19  ? 211 LYS   B CG  1 
ATOM   4548 C CD  . LYS   B 2 241 ? 8.375   51.890 106.812 1.00 70.02  ? 211 LYS   B CD  1 
ATOM   4549 C CE  . LYS   B 2 241 ? 9.619   51.388 106.135 1.00 72.93  ? 211 LYS   B CE  1 
ATOM   4550 N NZ  . LYS   B 2 241 ? 9.973   50.044 106.634 1.00 75.23  ? 211 LYS   B NZ  1 
ATOM   4551 N N   . ASP   B 2 242 ? 9.832   54.626 108.846 1.00 61.87  ? 212 ASP   B N   1 
ATOM   4552 C CA  . ASP   B 2 242 ? 11.142  55.274 108.809 1.00 62.06  ? 212 ASP   B CA  1 
ATOM   4553 C C   . ASP   B 2 242 ? 11.858  54.923 107.529 1.00 60.70  ? 212 ASP   B C   1 
ATOM   4554 O O   . ASP   B 2 242 ? 12.390  53.830 107.415 1.00 60.74  ? 212 ASP   B O   1 
ATOM   4555 C CB  . ASP   B 2 242 ? 11.983  54.834 110.025 1.00 65.37  ? 212 ASP   B CB  1 
ATOM   4556 C CG  . ASP   B 2 242 ? 13.290  55.586 110.238 1.00 72.39  ? 212 ASP   B CG  1 
ATOM   4557 O OD1 . ASP   B 2 242 ? 13.556  56.549 109.482 1.00 73.77  ? 212 ASP   B OD1 1 
ATOM   4558 O OD2 . ASP   B 2 242 ? 14.048  55.210 111.165 1.00 75.05  ? 212 ASP   B OD2 1 
ATOM   4559 N N   . ALA   B 2 243 ? 11.893  55.846 106.578 1.00 59.69  ? 213 ALA   B N   1 
ATOM   4560 C CA  . ALA   B 2 243 ? 12.579  55.620 105.310 1.00 59.20  ? 213 ALA   B CA  1 
ATOM   4561 C C   . ALA   B 2 243 ? 13.747  56.574 105.097 1.00 58.80  ? 213 ALA   B C   1 
ATOM   4562 O O   . ALA   B 2 243 ? 14.133  56.791 103.955 1.00 58.79  ? 213 ALA   B O   1 
ATOM   4563 C CB  . ALA   B 2 243 ? 11.601  55.744 104.158 1.00 59.09  ? 213 ALA   B CB  1 
ATOM   4564 N N   . ARG   B 2 244 ? 14.322  57.127 106.178 1.00 58.62  ? 214 ARG   B N   1 
ATOM   4565 C CA  . ARG   B 2 244 ? 15.430  58.073 106.088 1.00 59.22  ? 214 ARG   B CA  1 
ATOM   4566 C C   . ARG   B 2 244 ? 16.616  57.515 105.335 1.00 59.19  ? 214 ARG   B C   1 
ATOM   4567 O O   . ARG   B 2 244 ? 17.172  58.212 104.492 1.00 59.11  ? 214 ARG   B O   1 
ATOM   4568 C CB  . ARG   B 2 244 ? 15.875  58.547 107.474 1.00 61.17  ? 214 ARG   B CB  1 
ATOM   4569 C CG  . ARG   B 2 244 ? 14.870  59.428 108.175 1.00 65.75  ? 214 ARG   B CG  1 
ATOM   4570 C CD  . ARG   B 2 244 ? 15.304  59.758 109.592 1.00 71.32  ? 214 ARG   B CD  1 
ATOM   4571 N NE  . ARG   B 2 244 ? 15.628  58.563 110.377 1.00 76.41  ? 214 ARG   B NE  1 
ATOM   4572 C CZ  . ARG   B 2 244 ? 15.364  58.419 111.672 1.00 80.31  ? 214 ARG   B CZ  1 
ATOM   4573 N NH1 . ARG   B 2 244 ? 15.698  57.300 112.303 1.00 80.57  ? 214 ARG   B NH1 1 
ATOM   4574 N NH2 . ARG   B 2 244 ? 14.751  59.389 112.344 1.00 80.83  ? 214 ARG   B NH2 1 
ATOM   4575 N N   . GLN   B 2 245 ? 17.013  56.270 105.640 1.00 59.09  ? 215 GLN   B N   1 
ATOM   4576 C CA  . GLN   B 2 245 ? 18.141  55.633 104.982 1.00 59.45  ? 215 GLN   B CA  1 
ATOM   4577 C C   . GLN   B 2 245 ? 17.870  55.418 103.505 1.00 59.09  ? 215 GLN   B C   1 
ATOM   4578 O O   . GLN   B 2 245 ? 18.700  55.806 102.686 1.00 58.95  ? 215 GLN   B O   1 
ATOM   4579 C CB  . GLN   B 2 245 ? 18.498  54.306 105.656 1.00 62.06  ? 215 GLN   B CB  1 
ATOM   4580 C CG  . GLN   B 2 245 ? 19.809  53.735 105.131 1.00 67.27  ? 215 GLN   B CG  1 
ATOM   4581 C CD  . GLN   B 2 245 ? 20.202  52.437 105.789 1.00 73.22  ? 215 GLN   B CD  1 
ATOM   4582 O OE1 . GLN   B 2 245 ? 20.082  52.269 107.013 1.00 75.31  ? 215 GLN   B OE1 1 
ATOM   4583 N NE2 . GLN   B 2 245 ? 20.703  51.497 104.983 1.00 73.79  ? 215 GLN   B NE2 1 
ATOM   4584 N N   . TRP   B 2 246 ? 16.684  54.866 103.146 1.00 58.72  ? 216 TRP   B N   1 
ATOM   4585 C CA  . TRP   B 2 246 ? 16.310  54.616 101.745 1.00 58.61  ? 216 TRP   B CA  1 
ATOM   4586 C C   . TRP   B 2 246 ? 16.398  55.899 100.924 1.00 58.37  ? 216 TRP   B C   1 
ATOM   4587 O O   . TRP   B 2 246 ? 16.984  55.887 99.837  1.00 58.23  ? 216 TRP   B O   1 
ATOM   4588 C CB  . TRP   B 2 246 ? 14.899  54.002 101.657 1.00 58.44  ? 216 TRP   B CB  1 
ATOM   4589 C CG  . TRP   B 2 246 ? 14.461  53.591 100.277 1.00 58.78  ? 216 TRP   B CG  1 
ATOM   4590 C CD1 . TRP   B 2 246 ? 14.556  52.348 99.727  1.00 59.52  ? 216 TRP   B CD1 1 
ATOM   4591 C CD2 . TRP   B 2 246 ? 13.763  54.402 99.314  1.00 59.01  ? 216 TRP   B CD2 1 
ATOM   4592 N NE1 . TRP   B 2 246 ? 14.012  52.345 98.464  1.00 59.81  ? 216 TRP   B NE1 1 
ATOM   4593 C CE2 . TRP   B 2 246 ? 13.532  53.597 98.180  1.00 59.69  ? 216 TRP   B CE2 1 
ATOM   4594 C CE3 . TRP   B 2 246 ? 13.370  55.749 99.275  1.00 59.49  ? 216 TRP   B CE3 1 
ATOM   4595 C CZ2 . TRP   B 2 246 ? 12.873  54.078 97.048  1.00 60.31  ? 216 TRP   B CZ2 1 
ATOM   4596 C CZ3 . TRP   B 2 246 ? 12.727  56.224 98.148  1.00 60.20  ? 216 TRP   B CZ3 1 
ATOM   4597 C CH2 . TRP   B 2 246 ? 12.493  55.396 97.049  1.00 60.34  ? 216 TRP   B CH2 1 
ATOM   4598 N N   . PHE   B 2 247 ? 15.865  57.009 101.484 1.00 58.19  ? 217 PHE   B N   1 
ATOM   4599 C CA  . PHE   B 2 247 ? 15.868  58.339 100.872 1.00 58.81  ? 217 PHE   B CA  1 
ATOM   4600 C C   . PHE   B 2 247 ? 17.287  58.929 100.780 1.00 59.80  ? 217 PHE   B C   1 
ATOM   4601 O O   . PHE   B 2 247 ? 17.626  59.575 99.786  1.00 59.93  ? 217 PHE   B O   1 
ATOM   4602 C CB  . PHE   B 2 247 ? 14.910  59.290 101.609 1.00 58.40  ? 217 PHE   B CB  1 
ATOM   4603 C CG  . PHE   B 2 247 ? 13.490  59.268 101.096 1.00 58.98  ? 217 PHE   B CG  1 
ATOM   4604 C CD1 . PHE   B 2 247 ? 13.121  60.018 99.994  1.00 59.74  ? 217 PHE   B CD1 1 
ATOM   4605 C CD2 . PHE   B 2 247 ? 12.515  58.525 101.736 1.00 59.73  ? 217 PHE   B CD2 1 
ATOM   4606 C CE1 . PHE   B 2 247 ? 11.810  60.006 99.530  1.00 60.24  ? 217 PHE   B CE1 1 
ATOM   4607 C CE2 . PHE   B 2 247 ? 11.204  58.518 101.271 1.00 60.29  ? 217 PHE   B CE2 1 
ATOM   4608 C CZ  . PHE   B 2 247 ? 10.865  59.248 100.166 1.00 59.99  ? 217 PHE   B CZ  1 
ATOM   4609 N N   . ALA   B 2 248 ? 18.122  58.685 101.801 1.00 60.24  ? 218 ALA   B N   1 
ATOM   4610 C CA  . ALA   B 2 248 ? 19.514  59.135 101.781 1.00 60.95  ? 218 ALA   B CA  1 
ATOM   4611 C C   . ALA   B 2 248 ? 20.299  58.380 100.705 1.00 61.50  ? 218 ALA   B C   1 
ATOM   4612 O O   . ALA   B 2 248 ? 21.166  58.969 100.071 1.00 61.69  ? 218 ALA   B O   1 
ATOM   4613 C CB  . ALA   B 2 248 ? 20.163  58.933 103.138 1.00 61.07  ? 218 ALA   B CB  1 
ATOM   4614 N N   . GLU   B 2 249 ? 19.959  57.098 100.454 1.00 61.66  ? 219 GLU   B N   1 
ATOM   4615 C CA  . GLU   B 2 249 ? 20.596  56.278 99.417  1.00 62.23  ? 219 GLU   B CA  1 
ATOM   4616 C C   . GLU   B 2 249 ? 20.180  56.652 97.980  1.00 62.35  ? 219 GLU   B C   1 
ATOM   4617 O O   . GLU   B 2 249 ? 20.646  56.015 97.035  1.00 62.41  ? 219 GLU   B O   1 
ATOM   4618 C CB  . GLU   B 2 249 ? 20.366  54.779 99.676  1.00 64.51  ? 219 GLU   B CB  1 
ATOM   4619 C CG  . GLU   B 2 249 ? 21.123  54.248 100.881 1.00 68.84  ? 219 GLU   B CG  1 
ATOM   4620 C CD  . GLU   B 2 249 ? 20.565  52.976 101.496 1.00 74.26  ? 219 GLU   B CD  1 
ATOM   4621 O OE1 . GLU   B 2 249 ? 19.528  52.467 101.005 1.00 74.61  ? 219 GLU   B OE1 1 
ATOM   4622 O OE2 . GLU   B 2 249 ? 21.174  52.486 102.474 1.00 76.21  ? 219 GLU   B OE2 1 
ATOM   4623 N N   . LEU   B 2 250 ? 19.314  57.670 97.807  1.00 62.28  ? 220 LEU   B N   1 
ATOM   4624 C CA  . LEU   B 2 250 ? 18.909  58.109 96.475  1.00 62.81  ? 220 LEU   B CA  1 
ATOM   4625 C C   . LEU   B 2 250 ? 19.822  59.238 96.022  1.00 63.65  ? 220 LEU   B C   1 
ATOM   4626 O O   . LEU   B 2 250 ? 20.129  60.143 96.803  1.00 63.65  ? 220 LEU   B O   1 
ATOM   4627 C CB  . LEU   B 2 250 ? 17.478  58.656 96.467  1.00 62.70  ? 220 LEU   B CB  1 
ATOM   4628 C CG  . LEU   B 2 250 ? 16.362  57.843 97.075  1.00 63.57  ? 220 LEU   B CG  1 
ATOM   4629 C CD1 . LEU   B 2 250 ? 15.150  58.709 97.261  1.00 63.74  ? 220 LEU   B CD1 1 
ATOM   4630 C CD2 . LEU   B 2 250 ? 16.006  56.668 96.201  1.00 64.17  ? 220 LEU   B CD2 1 
ATOM   4631 N N   . SER   B 2 251 ? 20.214  59.221 94.748  1.00 64.20  ? 221 SER   B N   1 
ATOM   4632 C CA  . SER   B 2 251 ? 21.036  60.289 94.186  1.00 65.10  ? 221 SER   B CA  1 
ATOM   4633 C C   . SER   B 2 251 ? 20.075  61.315 93.593  1.00 65.70  ? 221 SER   B C   1 
ATOM   4634 O O   . SER   B 2 251 ? 19.840  61.311 92.384  1.00 65.90  ? 221 SER   B O   1 
ATOM   4635 C CB  . SER   B 2 251 ? 21.976  59.744 93.113  1.00 66.37  ? 221 SER   B CB  1 
ATOM   4636 O OG  . SER   B 2 251 ? 21.306  58.894 92.195  1.00 68.39  ? 221 SER   B OG  1 
ATOM   4637 N N   . VAL   B 2 252 ? 19.455  62.139 94.468  1.00 65.70  ? 222 VAL   B N   1 
ATOM   4638 C CA  . VAL   B 2 252 ? 18.463  63.151 94.095  1.00 66.05  ? 222 VAL   B CA  1 
ATOM   4639 C C   . VAL   B 2 252 ? 18.696  64.463 94.822  1.00 66.22  ? 222 VAL   B C   1 
ATOM   4640 O O   . VAL   B 2 252 ? 19.215  64.471 95.939  1.00 66.25  ? 222 VAL   B O   1 
ATOM   4641 C CB  . VAL   B 2 252 ? 17.015  62.675 94.379  1.00 66.71  ? 222 VAL   B CB  1 
ATOM   4642 C CG1 . VAL   B 2 252 ? 16.567  61.603 93.392  1.00 67.44  ? 222 VAL   B CG1 1 
ATOM   4643 C CG2 . VAL   B 2 252 ? 16.860  62.208 95.825  1.00 66.90  ? 222 VAL   B CG2 1 
ATOM   4644 N N   . ASP   B 2 253 ? 18.250  65.571 94.218  1.00 66.13  ? 223 ASP   B N   1 
ATOM   4645 C CA  . ASP   B 2 253 ? 18.358  66.881 94.842  1.00 66.74  ? 223 ASP   B CA  1 
ATOM   4646 C C   . ASP   B 2 253 ? 17.288  66.902 95.920  1.00 67.19  ? 223 ASP   B C   1 
ATOM   4647 O O   . ASP   B 2 253 ? 16.108  67.098 95.617  1.00 67.92  ? 223 ASP   B O   1 
ATOM   4648 C CB  . ASP   B 2 253 ? 18.106  67.991 93.801  1.00 68.58  ? 223 ASP   B CB  1 
ATOM   4649 C CG  . ASP   B 2 253 ? 18.471  69.398 94.240  1.00 73.09  ? 223 ASP   B CG  1 
ATOM   4650 O OD1 . ASP   B 2 253 ? 18.413  69.675 95.458  1.00 74.02  ? 223 ASP   B OD1 1 
ATOM   4651 O OD2 . ASP   B 2 253 ? 18.796  70.231 93.358  1.00 74.92  ? 223 ASP   B OD2 1 
ATOM   4652 N N   . MET   B 2 254 ? 17.686  66.648 97.173  1.00 66.48  ? 224 MET   B N   1 
ATOM   4653 C CA  . MET   B 2 254 ? 16.722  66.617 98.266  1.00 66.00  ? 224 MET   B CA  1 
ATOM   4654 C C   . MET   B 2 254 ? 16.103  67.971 98.566  1.00 65.26  ? 224 MET   B C   1 
ATOM   4655 O O   . MET   B 2 254 ? 15.122  68.005 99.293  1.00 65.44  ? 224 MET   B O   1 
ATOM   4656 C CB  . MET   B 2 254 ? 17.299  65.974 99.530  1.00 66.68  ? 224 MET   B CB  1 
ATOM   4657 C CG  . MET   B 2 254 ? 17.382  64.459 99.447  1.00 69.16  ? 224 MET   B CG  1 
ATOM   4658 S SD  . MET   B 2 254 ? 15.788  63.621 99.166  1.00 74.10  ? 224 MET   B SD  1 
ATOM   4659 C CE  . MET   B 2 254 ? 14.843  64.189 100.623 1.00 71.76  ? 224 MET   B CE  1 
ATOM   4660 N N   . GLU   B 2 255 ? 16.637  69.078 98.011  1.00 64.44  ? 225 GLU   B N   1 
ATOM   4661 C CA  . GLU   B 2 255 ? 16.027  70.393 98.223  1.00 64.16  ? 225 GLU   B CA  1 
ATOM   4662 C C   . GLU   B 2 255 ? 14.782  70.486 97.352  1.00 62.88  ? 225 GLU   B C   1 
ATOM   4663 O O   . GLU   B 2 255 ? 13.718  70.856 97.849  1.00 62.90  ? 225 GLU   B O   1 
ATOM   4664 C CB  . GLU   B 2 255 ? 17.012  71.543 97.935  1.00 67.22  ? 225 GLU   B CB  1 
ATOM   4665 C CG  . GLU   B 2 255 ? 16.378  72.930 97.897  1.00 74.38  ? 225 GLU   B CG  1 
ATOM   4666 C CD  . GLU   B 2 255 ? 15.469  73.336 99.050  1.00 82.91  ? 225 GLU   B CD  1 
ATOM   4667 O OE1 . GLU   B 2 255 ? 15.764  72.968 100.210 1.00 84.88  ? 225 GLU   B OE1 1 
ATOM   4668 O OE2 . GLU   B 2 255 ? 14.460  74.033 98.791  1.00 85.12  ? 225 GLU   B OE2 1 
ATOM   4669 N N   . LYS   B 2 256 ? 14.900  70.067 96.076  1.00 61.45  ? 226 LYS   B N   1 
ATOM   4670 C CA  . LYS   B 2 256 ? 13.800  70.036 95.119  1.00 60.26  ? 226 LYS   B CA  1 
ATOM   4671 C C   . LYS   B 2 256 ? 12.646  69.174 95.640  1.00 58.63  ? 226 LYS   B C   1 
ATOM   4672 O O   . LYS   B 2 256 ? 11.500  69.560 95.473  1.00 58.59  ? 226 LYS   B O   1 
ATOM   4673 C CB  . LYS   B 2 256 ? 14.293  69.511 93.769  1.00 62.06  ? 226 LYS   B CB  1 
ATOM   4674 C CG  . LYS   B 2 256 ? 15.241  70.467 93.068  1.00 66.52  ? 226 LYS   B CG  1 
ATOM   4675 C CD  . LYS   B 2 256 ? 14.496  71.670 92.518  1.00 71.21  ? 226 LYS   B CD  1 
ATOM   4676 C CE  . LYS   B 2 256 ? 15.194  72.296 91.337  1.00 74.89  ? 226 LYS   B CE  1 
ATOM   4677 N NZ  . LYS   B 2 256 ? 14.219  72.942 90.414  1.00 77.42  ? 226 LYS   B NZ  1 
ATOM   4678 N N   . ILE   B 2 257 ? 12.948  68.034 96.298  1.00 57.16  ? 227 ILE   B N   1 
ATOM   4679 C CA  . ILE   B 2 257 ? 11.942  67.138 96.883  1.00 56.28  ? 227 ILE   B CA  1 
ATOM   4680 C C   . ILE   B 2 257 ? 11.209  67.866 98.021  1.00 55.58  ? 227 ILE   B C   1 
ATOM   4681 O O   . ILE   B 2 257 ? 9.984   67.792 98.115  1.00 55.87  ? 227 ILE   B O   1 
ATOM   4682 C CB  . ILE   B 2 257 ? 12.608  65.828 97.385  1.00 56.53  ? 227 ILE   B CB  1 
ATOM   4683 C CG1 . ILE   B 2 257 ? 13.349  65.091 96.253  1.00 57.43  ? 227 ILE   B CG1 1 
ATOM   4684 C CG2 . ILE   B 2 257 ? 11.624  64.916 98.121  1.00 56.64  ? 227 ILE   B CG2 1 
ATOM   4685 C CD1 . ILE   B 2 257 ? 12.488  64.621 95.160  1.00 58.71  ? 227 ILE   B CD1 1 
ATOM   4686 N N   . LEU   B 2 258 ? 11.957  68.608 98.853  1.00 54.36  ? 228 LEU   B N   1 
ATOM   4687 C CA  . LEU   B 2 258 ? 11.391  69.379 99.953  1.00 53.64  ? 228 LEU   B CA  1 
ATOM   4688 C C   . LEU   B 2 258 ? 10.509  70.518 99.465  1.00 52.01  ? 228 LEU   B C   1 
ATOM   4689 O O   . LEU   B 2 258 ? 9.544   70.863 100.132 1.00 51.97  ? 228 LEU   B O   1 
ATOM   4690 C CB  . LEU   B 2 258 ? 12.497  69.908 100.866 1.00 54.51  ? 228 LEU   B CB  1 
ATOM   4691 C CG  . LEU   B 2 258 ? 13.209  68.833 101.678 1.00 56.85  ? 228 LEU   B CG  1 
ATOM   4692 C CD1 . LEU   B 2 258 ? 14.436  69.393 102.378 1.00 57.61  ? 228 LEU   B CD1 1 
ATOM   4693 C CD2 . LEU   B 2 258 ? 12.256  68.153 102.656 1.00 57.70  ? 228 LEU   B CD2 1 
ATOM   4694 N N   . GLU   B 2 259 ? 10.806  71.082 98.289  1.00 50.56  ? 229 GLU   B N   1 
ATOM   4695 C CA  . GLU   B 2 259 ? 9.978   72.124 97.701  1.00 49.75  ? 229 GLU   B CA  1 
ATOM   4696 C C   . GLU   B 2 259 ? 8.612   71.521 97.357  1.00 48.43  ? 229 GLU   B C   1 
ATOM   4697 O O   . GLU   B 2 259 ? 7.587   72.065 97.750  1.00 48.76  ? 229 GLU   B O   1 
ATOM   4698 C CB  . GLU   B 2 259 ? 10.629  72.674 96.418  1.00 52.48  ? 229 GLU   B CB  1 
ATOM   4699 C CG  . GLU   B 2 259 ? 11.947  73.393 96.621  1.00 58.84  ? 229 GLU   B CG  1 
ATOM   4700 C CD  . GLU   B 2 259 ? 12.598  73.896 95.345  1.00 67.69  ? 229 GLU   B CD  1 
ATOM   4701 O OE1 . GLU   B 2 259 ? 12.207  73.437 94.247  1.00 69.46  ? 229 GLU   B OE1 1 
ATOM   4702 O OE2 . GLU   B 2 259 ? 13.506  74.753 95.444  1.00 71.06  ? 229 GLU   B OE2 1 
ATOM   4703 N N   . ILE   B 2 260 ? 8.615   70.351 96.695  1.00 46.94  ? 230 ILE   B N   1 
ATOM   4704 C CA  . ILE   B 2 260 ? 7.411   69.642 96.279  1.00 45.76  ? 230 ILE   B CA  1 
ATOM   4705 C C   . ILE   B 2 260 ? 6.580   69.230 97.478  1.00 45.20  ? 230 ILE   B C   1 
ATOM   4706 O O   . ILE   B 2 260 ? 5.359   69.382 97.466  1.00 45.43  ? 230 ILE   B O   1 
ATOM   4707 C CB  . ILE   B 2 260 ? 7.759   68.435 95.387  1.00 45.62  ? 230 ILE   B CB  1 
ATOM   4708 C CG1 . ILE   B 2 260 ? 8.711   68.810 94.250  1.00 45.80  ? 230 ILE   B CG1 1 
ATOM   4709 C CG2 . ILE   B 2 260 ? 6.491   67.806 94.836  1.00 46.31  ? 230 ILE   B CG2 1 
ATOM   4710 C CD1 . ILE   B 2 260 ? 9.304   67.613 93.567  1.00 46.69  ? 230 ILE   B CD1 1 
ATOM   4711 N N   . ILE   B 2 261 ? 7.248   68.747 98.539  1.00 44.35  ? 231 ILE   B N   1 
ATOM   4712 C CA  . ILE   B 2 261 ? 6.593   68.338 99.786  1.00 43.45  ? 231 ILE   B CA  1 
ATOM   4713 C C   . ILE   B 2 261 ? 5.837   69.514 100.397 1.00 42.77  ? 231 ILE   B C   1 
ATOM   4714 O O   . ILE   B 2 261 ? 4.677   69.363 100.755 1.00 42.09  ? 231 ILE   B O   1 
ATOM   4715 C CB  . ILE   B 2 261 ? 7.628   67.718 100.759 1.00 43.31  ? 231 ILE   B CB  1 
ATOM   4716 C CG1 . ILE   B 2 261 ? 8.097   66.361 100.231 1.00 44.01  ? 231 ILE   B CG1 1 
ATOM   4717 C CG2 . ILE   B 2 261 ? 7.060   67.591 102.177 1.00 43.45  ? 231 ILE   B CG2 1 
ATOM   4718 C CD1 . ILE   B 2 261 ? 9.256   65.817 100.919 1.00 45.54  ? 231 ILE   B CD1 1 
ATOM   4719 N N   . ARG   B 2 262 ? 6.463   70.702 100.422 1.00 42.82  ? 232 ARG   B N   1 
ATOM   4720 C CA  . ARG   B 2 262 ? 5.835   71.906 100.943 1.00 43.90  ? 232 ARG   B CA  1 
ATOM   4721 C C   . ARG   B 2 262 ? 4.549   72.236 100.194 1.00 44.42  ? 232 ARG   B C   1 
ATOM   4722 O O   . ARG   B 2 262 ? 3.535   72.517 100.824 1.00 44.49  ? 232 ARG   B O   1 
ATOM   4723 C CB  . ARG   B 2 262 ? 6.809   73.086 100.933 1.00 45.86  ? 232 ARG   B CB  1 
ATOM   4724 C CG  . ARG   B 2 262 ? 7.891   72.945 101.994 1.00 50.15  ? 232 ARG   B CG  1 
ATOM   4725 C CD  . ARG   B 2 262 ? 8.948   74.026 101.891 1.00 54.81  ? 232 ARG   B CD  1 
ATOM   4726 N NE  . ARG   B 2 262 ? 10.278  73.507 102.223 1.00 59.43  ? 232 ARG   B NE  1 
ATOM   4727 C CZ  . ARG   B 2 262 ? 11.405  73.882 101.620 1.00 62.21  ? 232 ARG   B CZ  1 
ATOM   4728 N NH1 . ARG   B 2 262 ? 11.379  74.798 100.655 1.00 61.55  ? 232 ARG   B NH1 1 
ATOM   4729 N NH2 . ARG   B 2 262 ? 12.567  73.338 101.973 1.00 62.04  ? 232 ARG   B NH2 1 
ATOM   4730 N N   . VAL   B 2 263 ? 4.567   72.114 98.865  1.00 44.48  ? 233 VAL   B N   1 
ATOM   4731 C CA  . VAL   B 2 263 ? 3.380   72.334 98.036  1.00 44.78  ? 233 VAL   B CA  1 
ATOM   4732 C C   . VAL   B 2 263 ? 2.264   71.345 98.419  1.00 45.25  ? 233 VAL   B C   1 
ATOM   4733 O O   . VAL   B 2 263 ? 1.111   71.758 98.572  1.00 45.72  ? 233 VAL   B O   1 
ATOM   4734 C CB  . VAL   B 2 263 ? 3.729   72.226 96.542  1.00 44.97  ? 233 VAL   B CB  1 
ATOM   4735 C CG1 . VAL   B 2 263 ? 2.483   72.382 95.682  1.00 45.51  ? 233 VAL   B CG1 1 
ATOM   4736 C CG2 . VAL   B 2 263 ? 4.780   73.252 96.166  1.00 44.91  ? 233 VAL   B CG2 1 
ATOM   4737 N N   . ILE   B 2 264 ? 2.621   70.053 98.613  1.00 44.69  ? 234 ILE   B N   1 
ATOM   4738 C CA  . ILE   B 2 264 ? 1.681   69.001 99.033  1.00 44.63  ? 234 ILE   B CA  1 
ATOM   4739 C C   . ILE   B 2 264 ? 1.070   69.295 100.426 1.00 44.67  ? 234 ILE   B C   1 
ATOM   4740 O O   . ILE   B 2 264 ? -0.139  69.180 100.603 1.00 44.59  ? 234 ILE   B O   1 
ATOM   4741 C CB  . ILE   B 2 264 ? 2.353   67.601 98.971  1.00 44.57  ? 234 ILE   B CB  1 
ATOM   4742 C CG1 . ILE   B 2 264 ? 2.733   67.233 97.522  1.00 45.06  ? 234 ILE   B CG1 1 
ATOM   4743 C CG2 . ILE   B 2 264 ? 1.469   66.534 99.594  1.00 44.62  ? 234 ILE   B CG2 1 
ATOM   4744 C CD1 . ILE   B 2 264 ? 3.637   66.081 97.407  1.00 45.81  ? 234 ILE   B CD1 1 
ATOM   4745 N N   . LEU   B 2 265 ? 1.896   69.732 101.388 1.00 44.42  ? 235 LEU   B N   1 
ATOM   4746 C CA  . LEU   B 2 265 ? 1.408   70.079 102.718 1.00 44.28  ? 235 LEU   B CA  1 
ATOM   4747 C C   . LEU   B 2 265 ? 0.517   71.310 102.646 1.00 45.53  ? 235 LEU   B C   1 
ATOM   4748 O O   . LEU   B 2 265 ? -0.512  71.358 103.315 1.00 45.80  ? 235 LEU   B O   1 
ATOM   4749 C CB  . LEU   B 2 265 ? 2.579   70.343 103.669 1.00 43.40  ? 235 LEU   B CB  1 
ATOM   4750 C CG  . LEU   B 2 265 ? 3.538   69.195 103.914 1.00 43.28  ? 235 LEU   B CG  1 
ATOM   4751 C CD1 . LEU   B 2 265 ? 4.600   69.604 104.867 1.00 43.36  ? 235 LEU   B CD1 1 
ATOM   4752 C CD2 . LEU   B 2 265 ? 2.832   68.006 104.472 1.00 43.33  ? 235 LEU   B CD2 1 
ATOM   4753 N N   . LYS   B 2 266 ? 0.905   72.301 101.822 1.00 46.20  ? 236 LYS   B N   1 
ATOM   4754 C CA  . LYS   B 2 266 ? 0.157   73.540 101.631 1.00 47.30  ? 236 LYS   B CA  1 
ATOM   4755 C C   . LYS   B 2 266 ? -1.216  73.233 101.058 1.00 48.04  ? 236 LYS   B C   1 
ATOM   4756 O O   . LYS   B 2 266 ? -2.208  73.813 101.500 1.00 48.85  ? 236 LYS   B O   1 
ATOM   4757 C CB  . LYS   B 2 266 ? 0.924   74.514 100.706 1.00 49.77  ? 236 LYS   B CB  1 
ATOM   4758 C CG  . LYS   B 2 266 ? 0.152   75.786 100.393 1.00 55.45  ? 236 LYS   B CG  1 
ATOM   4759 C CD  . LYS   B 2 266 ? 1.005   76.951 99.904  1.00 61.73  ? 236 LYS   B CD  1 
ATOM   4760 C CE  . LYS   B 2 266 ? 0.123   78.166 99.622  1.00 66.47  ? 236 LYS   B CE  1 
ATOM   4761 N NZ  . LYS   B 2 266 ? 0.906   79.386 99.267  1.00 68.82  ? 236 LYS   B NZ  1 
ATOM   4762 N N   . LEU   B 2 267 ? -1.274  72.302 100.087 1.00 47.52  ? 237 LEU   B N   1 
ATOM   4763 C CA  . LEU   B 2 267 ? -2.493  71.858 99.432  1.00 47.27  ? 237 LEU   B CA  1 
ATOM   4764 C C   . LEU   B 2 267 ? -3.500  71.349 100.460 1.00 47.08  ? 237 LEU   B C   1 
ATOM   4765 O O   . LEU   B 2 267 ? -4.692  71.577 100.279 1.00 47.76  ? 237 LEU   B O   1 
ATOM   4766 C CB  . LEU   B 2 267 ? -2.146  70.762 98.397  1.00 47.41  ? 237 LEU   B CB  1 
ATOM   4767 C CG  . LEU   B 2 267 ? -3.202  69.689 98.097  1.00 48.69  ? 237 LEU   B CG  1 
ATOM   4768 C CD1 . LEU   B 2 267 ? -4.194  70.160 97.059  1.00 49.43  ? 237 LEU   B CD1 1 
ATOM   4769 C CD2 . LEU   B 2 267 ? -2.570  68.383 97.773  1.00 49.16  ? 237 LEU   B CD2 1 
ATOM   4770 N N   . TYR   B 2 268 ? -3.040  70.637 101.501 1.00 46.18  ? 238 TYR   B N   1 
ATOM   4771 C CA  . TYR   B 2 268 ? -3.961  70.091 102.491 1.00 46.20  ? 238 TYR   B CA  1 
ATOM   4772 C C   . TYR   B 2 268 ? -4.549  71.145 103.391 1.00 46.37  ? 238 TYR   B C   1 
ATOM   4773 O O   . TYR   B 2 268 ? -5.703  71.012 103.786 1.00 46.36  ? 238 TYR   B O   1 
ATOM   4774 C CB  . TYR   B 2 268 ? -3.331  68.956 103.279 1.00 46.24  ? 238 TYR   B CB  1 
ATOM   4775 C CG  . TYR   B 2 268 ? -3.131  67.747 102.401 1.00 46.63  ? 238 TYR   B CG  1 
ATOM   4776 C CD1 . TYR   B 2 268 ? -4.181  67.222 101.660 1.00 47.29  ? 238 TYR   B CD1 1 
ATOM   4777 C CD2 . TYR   B 2 268 ? -1.886  67.149 102.281 1.00 47.31  ? 238 TYR   B CD2 1 
ATOM   4778 C CE1 . TYR   B 2 268 ? -3.995  66.141 100.815 1.00 48.27  ? 238 TYR   B CE1 1 
ATOM   4779 C CE2 . TYR   B 2 268 ? -1.685  66.070 101.432 1.00 48.27  ? 238 TYR   B CE2 1 
ATOM   4780 C CZ  . TYR   B 2 268 ? -2.742  65.572 100.694 1.00 49.14  ? 238 TYR   B CZ  1 
ATOM   4781 O OH  . TYR   B 2 268 ? -2.560  64.492 99.870  1.00 50.24  ? 238 TYR   B OH  1 
ATOM   4782 N N   . GLU   B 2 269 ? -3.798  72.213 103.674 1.00 46.45  ? 239 GLU   B N   1 
ATOM   4783 C CA  . GLU   B 2 269 ? -4.339  73.325 104.441 1.00 46.96  ? 239 GLU   B CA  1 
ATOM   4784 C C   . GLU   B 2 269 ? -5.345  74.098 103.586 1.00 47.02  ? 239 GLU   B C   1 
ATOM   4785 O O   . GLU   B 2 269 ? -6.366  74.531 104.112 1.00 47.15  ? 239 GLU   B O   1 
ATOM   4786 C CB  . GLU   B 2 269 ? -3.227  74.239 104.972 1.00 49.35  ? 239 GLU   B CB  1 
ATOM   4787 C CG  . GLU   B 2 269 ? -2.322  73.550 105.975 1.00 54.29  ? 239 GLU   B CG  1 
ATOM   4788 C CD  . GLU   B 2 269 ? -3.021  72.855 107.133 1.00 60.41  ? 239 GLU   B CD  1 
ATOM   4789 O OE1 . GLU   B 2 269 ? -3.900  73.482 107.772 1.00 61.31  ? 239 GLU   B OE1 1 
ATOM   4790 O OE2 . GLU   B 2 269 ? -2.682  71.677 107.399 1.00 61.04  ? 239 GLU   B OE2 1 
ATOM   4791 N N   . GLN   B 2 270 ? -5.084  74.242 102.268 1.00 46.78  ? 240 GLN   B N   1 
ATOM   4792 C CA  . GLN   B 2 270 ? -6.023  74.900 101.363 1.00 47.14  ? 240 GLN   B CA  1 
ATOM   4793 C C   . GLN   B 2 270 ? -7.292  74.052 101.231 1.00 46.75  ? 240 GLN   B C   1 
ATOM   4794 O O   . GLN   B 2 270 ? -8.389  74.595 101.263 1.00 46.92  ? 240 GLN   B O   1 
ATOM   4795 C CB  . GLN   B 2 270 ? -5.386  75.194 99.995  1.00 49.21  ? 240 GLN   B CB  1 
ATOM   4796 C CG  . GLN   B 2 270 ? -6.374  75.572 98.873  1.00 54.00  ? 240 GLN   B CG  1 
ATOM   4797 C CD  . GLN   B 2 270 ? -6.953  76.985 98.917  1.00 60.09  ? 240 GLN   B CD  1 
ATOM   4798 O OE1 . GLN   B 2 270 ? -6.654  77.817 98.046  1.00 62.75  ? 240 GLN   B OE1 1 
ATOM   4799 N NE2 . GLN   B 2 270 ? -7.830  77.290 99.892  1.00 59.97  ? 240 GLN   B NE2 1 
ATOM   4800 N N   . TRP   B 2 271 ? -7.143  72.723 101.171 1.00 46.11  ? 241 TRP   B N   1 
ATOM   4801 C CA  . TRP   B 2 271 ? -8.232  71.749 101.117 1.00 45.61  ? 241 TRP   B CA  1 
ATOM   4802 C C   . TRP   B 2 271 ? -9.165  71.950 102.323 1.00 45.87  ? 241 TRP   B C   1 
ATOM   4803 O O   . TRP   B 2 271 ? -10.372 72.062 102.146 1.00 46.24  ? 241 TRP   B O   1 
ATOM   4804 C CB  . TRP   B 2 271 ? -7.635  70.336 101.132 1.00 44.84  ? 241 TRP   B CB  1 
ATOM   4805 C CG  . TRP   B 2 271 ? -8.578  69.225 100.767 1.00 44.52  ? 241 TRP   B CG  1 
ATOM   4806 C CD1 . TRP   B 2 271 ? -9.836  69.003 101.254 1.00 44.76  ? 241 TRP   B CD1 1 
ATOM   4807 C CD2 . TRP   B 2 271 ? -8.265  68.101 99.937  1.00 44.12  ? 241 TRP   B CD2 1 
ATOM   4808 N NE1 . TRP   B 2 271 ? -10.329 67.818 100.762 1.00 44.81  ? 241 TRP   B NE1 1 
ATOM   4809 C CE2 . TRP   B 2 271 ? -9.387  67.248 99.945  1.00 44.60  ? 241 TRP   B CE2 1 
ATOM   4810 C CE3 . TRP   B 2 271 ? -7.143  67.736 99.185  1.00 44.16  ? 241 TRP   B CE3 1 
ATOM   4811 C CZ2 . TRP   B 2 271 ? -9.434  66.085 99.189  1.00 45.06  ? 241 TRP   B CZ2 1 
ATOM   4812 C CZ3 . TRP   B 2 271 ? -7.183  66.567 98.462  1.00 44.83  ? 241 TRP   B CZ3 1 
ATOM   4813 C CH2 . TRP   B 2 271 ? -8.306  65.742 98.490  1.00 45.09  ? 241 TRP   B CH2 1 
ATOM   4814 N N   . LYS   B 2 272 ? -8.595  72.049 103.528 1.00 45.72  ? 242 LYS   B N   1 
ATOM   4815 C CA  . LYS   B 2 272 ? -9.317  72.263 104.770 1.00 46.13  ? 242 LYS   B CA  1 
ATOM   4816 C C   . LYS   B 2 272 ? -10.033 73.591 104.747 1.00 46.93  ? 242 LYS   B C   1 
ATOM   4817 O O   . LYS   B 2 272 ? -11.203 73.643 105.113 1.00 48.01  ? 242 LYS   B O   1 
ATOM   4818 C CB  . LYS   B 2 272 ? -8.334  72.178 105.957 1.00 47.83  ? 242 LYS   B CB  1 
ATOM   4819 C CG  . LYS   B 2 272 ? -8.590  73.078 107.168 1.00 51.12  ? 242 LYS   B CG  1 
ATOM   4820 C CD  . LYS   B 2 272 ? -7.337  73.118 107.988 1.00 56.07  ? 242 LYS   B CD  1 
ATOM   4821 C CE  . LYS   B 2 272 ? -7.426  73.977 109.210 1.00 60.66  ? 242 LYS   B CE  1 
ATOM   4822 N NZ  . LYS   B 2 272 ? -6.267  73.715 110.117 1.00 63.37  ? 242 LYS   B NZ  1 
ATOM   4823 N N   . ASN   B 2 273 ? -9.361  74.658 104.307 1.00 46.46  ? 243 ASN   B N   1 
ATOM   4824 C CA  . ASN   B 2 273 ? -9.962  75.984 104.312 1.00 46.82  ? 243 ASN   B CA  1 
ATOM   4825 C C   . ASN   B 2 273 ? -10.782 76.345 103.079 1.00 47.04  ? 243 ASN   B C   1 
ATOM   4826 O O   . ASN   B 2 273 ? -11.181 77.505 102.943 1.00 47.84  ? 243 ASN   B O   1 
ATOM   4827 C CB  . ASN   B 2 273 ? -8.891  77.024 104.536 1.00 48.39  ? 243 ASN   B CB  1 
ATOM   4828 C CG  . ASN   B 2 273 ? -8.128  76.833 105.816 1.00 52.75  ? 243 ASN   B CG  1 
ATOM   4829 O OD1 . ASN   B 2 273 ? -6.893  76.856 105.824 1.00 54.44  ? 243 ASN   B OD1 1 
ATOM   4830 N ND2 . ASN   B 2 273 ? -8.840  76.631 106.927 1.00 53.58  ? 243 ASN   B ND2 1 
ATOM   4831 N N   . PHE   B 2 274 ? -11.044 75.389 102.187 1.00 46.30  ? 244 PHE   B N   1 
ATOM   4832 C CA  . PHE   B 2 274 ? -11.780 75.685 100.963 1.00 46.40  ? 244 PHE   B CA  1 
ATOM   4833 C C   . PHE   B 2 274 ? -13.028 74.855 100.870 1.00 47.00  ? 244 PHE   B C   1 
ATOM   4834 O O   . PHE   B 2 274 ? -12.959 73.646 101.052 1.00 47.85  ? 244 PHE   B O   1 
ATOM   4835 C CB  . PHE   B 2 274 ? -10.858 75.448 99.750  1.00 46.20  ? 244 PHE   B CB  1 
ATOM   4836 C CG  . PHE   B 2 274 ? -11.436 75.444 98.353  1.00 46.78  ? 244 PHE   B CG  1 
ATOM   4837 C CD1 . PHE   B 2 274 ? -12.275 76.464 97.926  1.00 47.77  ? 244 PHE   B CD1 1 
ATOM   4838 C CD2 . PHE   B 2 274 ? -11.053 74.484 97.432  1.00 47.22  ? 244 PHE   B CD2 1 
ATOM   4839 C CE1 . PHE   B 2 274 ? -12.772 76.480 96.629  1.00 48.40  ? 244 PHE   B CE1 1 
ATOM   4840 C CE2 . PHE   B 2 274 ? -11.554 74.501 96.140  1.00 48.03  ? 244 PHE   B CE2 1 
ATOM   4841 C CZ  . PHE   B 2 274 ? -12.378 75.521 95.735  1.00 48.05  ? 244 PHE   B CZ  1 
ATOM   4842 N N   . ASP   B 2 275 ? -14.173 75.488 100.600 1.00 46.72  ? 245 ASP   B N   1 
ATOM   4843 C CA  . ASP   B 2 275 ? -15.426 74.777 100.392 1.00 47.15  ? 245 ASP   B CA  1 
ATOM   4844 C C   . ASP   B 2 275 ? -15.847 75.105 98.973  1.00 46.77  ? 245 ASP   B C   1 
ATOM   4845 O O   . ASP   B 2 275 ? -16.554 76.093 98.758  1.00 47.02  ? 245 ASP   B O   1 
ATOM   4846 C CB  . ASP   B 2 275 ? -16.507 75.243 101.377 1.00 49.72  ? 245 ASP   B CB  1 
ATOM   4847 C CG  . ASP   B 2 275 ? -17.671 74.264 101.529 1.00 55.41  ? 245 ASP   B CG  1 
ATOM   4848 O OD1 . ASP   B 2 275 ? -17.956 73.508 100.555 1.00 55.44  ? 245 ASP   B OD1 1 
ATOM   4849 O OD2 . ASP   B 2 275 ? -18.291 74.245 102.621 1.00 58.08  ? 245 ASP   B OD2 1 
ATOM   4850 N N   . GLU   B 2 276 ? -15.411 74.298 98.000  1.00 45.94  ? 246 GLU   B N   1 
ATOM   4851 C CA  . GLU   B 2 276 ? -15.736 74.568 96.601  1.00 45.72  ? 246 GLU   B CA  1 
ATOM   4852 C C   . GLU   B 2 276 ? -17.226 74.637 96.322  1.00 44.75  ? 246 GLU   B C   1 
ATOM   4853 O O   . GLU   B 2 276 ? -17.647 75.417 95.467  1.00 44.84  ? 246 GLU   B O   1 
ATOM   4854 C CB  . GLU   B 2 276 ? -15.042 73.594 95.629  1.00 48.24  ? 246 GLU   B CB  1 
ATOM   4855 C CG  . GLU   B 2 276 ? -15.333 72.123 95.836  1.00 54.28  ? 246 GLU   B CG  1 
ATOM   4856 C CD  . GLU   B 2 276 ? -15.016 71.248 94.640  1.00 62.27  ? 246 GLU   B CD  1 
ATOM   4857 O OE1 . GLU   B 2 276 ? -15.434 70.067 94.650  1.00 64.79  ? 246 GLU   B OE1 1 
ATOM   4858 O OE2 . GLU   B 2 276 ? -14.373 71.742 93.684  1.00 63.70  ? 246 GLU   B OE2 1 
ATOM   4859 N N   A ARG   B 2 277 ? -18.028 73.837 97.039  0.51 43.98  ? 247 ARG   B N   1 
ATOM   4860 N N   B ARG   B 2 277 ? -18.027 73.838 97.039  0.49 44.00  ? 247 ARG   B N   1 
ATOM   4861 C CA  A ARG   B 2 277 ? -19.467 73.833 96.819  0.51 43.52  ? 247 ARG   B CA  1 
ATOM   4862 C CA  B ARG   B 2 277 ? -19.468 73.839 96.832  0.49 43.59  ? 247 ARG   B CA  1 
ATOM   4863 C C   A ARG   B 2 277 ? -20.098 75.185 97.172  0.51 43.75  ? 247 ARG   B C   1 
ATOM   4864 C C   B ARG   B 2 277 ? -20.084 75.197 97.162  0.49 43.77  ? 247 ARG   B C   1 
ATOM   4865 O O   A ARG   B 2 277 ? -21.002 75.634 96.471  0.51 43.79  ? 247 ARG   B O   1 
ATOM   4866 O O   B ARG   B 2 277 ? -20.975 75.652 96.448  0.49 43.81  ? 247 ARG   B O   1 
ATOM   4867 C CB  A ARG   B 2 277 ? -20.142 72.646 97.525  0.51 43.40  ? 247 ARG   B CB  1 
ATOM   4868 C CB  B ARG   B 2 277 ? -20.130 72.701 97.616  0.49 43.57  ? 247 ARG   B CB  1 
ATOM   4869 C CG  A ARG   B 2 277 ? -19.483 71.307 97.207  0.51 43.59  ? 247 ARG   B CG  1 
ATOM   4870 C CG  B ARG   B 2 277 ? -19.861 71.333 97.019  0.49 43.86  ? 247 ARG   B CG  1 
ATOM   4871 C CD  A ARG   B 2 277 ? -20.476 70.165 97.159  0.51 44.29  ? 247 ARG   B CD  1 
ATOM   4872 C CD  B ARG   B 2 277 ? -19.572 70.288 98.068  0.49 44.70  ? 247 ARG   B CD  1 
ATOM   4873 N NE  A ARG   B 2 277 ? -19.945 69.012 96.431  0.51 44.87  ? 247 ARG   B NE  1 
ATOM   4874 N NE  B ARG   B 2 277 ? -18.200 69.792 97.960  0.49 45.67  ? 247 ARG   B NE  1 
ATOM   4875 C CZ  A ARG   B 2 277 ? -20.694 68.086 95.836  0.51 45.76  ? 247 ARG   B CZ  1 
ATOM   4876 C CZ  B ARG   B 2 277 ? -17.235 70.053 98.836  0.49 46.63  ? 247 ARG   B CZ  1 
ATOM   4877 N NH1 A ARG   B 2 277 ? -22.019 68.174 95.865  0.51 44.85  ? 247 ARG   B NH1 1 
ATOM   4878 N NH1 B ARG   B 2 277 ? -17.481 70.801 99.902  0.49 46.28  ? 247 ARG   B NH1 1 
ATOM   4879 N NH2 A ARG   B 2 277 ? -20.124 67.077 95.191  0.51 45.14  ? 247 ARG   B NH2 1 
ATOM   4880 N NH2 B ARG   B 2 277 ? -16.016 69.569 98.652  0.49 45.89  ? 247 ARG   B NH2 1 
ATOM   4881 N N   . LYS   B 2 278 ? -19.563 75.878 98.187  1.00 43.77  ? 248 LYS   B N   1 
ATOM   4882 C CA  . LYS   B 2 278 ? -20.089 77.186 98.580  1.00 44.47  ? 248 LYS   B CA  1 
ATOM   4883 C C   . LYS   B 2 278 ? -19.414 78.366 97.876  1.00 44.94  ? 248 LYS   B C   1 
ATOM   4884 O O   . LYS   B 2 278 ? -20.011 79.443 97.789  1.00 45.21  ? 248 LYS   B O   1 
ATOM   4885 C CB  . LYS   B 2 278 ? -19.994 77.371 100.105 1.00 46.59  ? 248 LYS   B CB  1 
ATOM   4886 C CG  . LYS   B 2 278 ? -20.559 76.204 100.913 1.00 51.38  ? 248 LYS   B CG  1 
ATOM   4887 C CD  . LYS   B 2 278 ? -20.632 76.535 102.405 1.00 55.87  ? 248 LYS   B CD  1 
ATOM   4888 C CE  . LYS   B 2 278 ? -21.205 75.414 103.235 1.00 58.76  ? 248 LYS   B CE  1 
ATOM   4889 N NZ  . LYS   B 2 278 ? -21.306 75.789 104.669 1.00 60.79  ? 248 LYS   B NZ  1 
ATOM   4890 N N   . GLU   B 2 279 ? -18.166 78.189 97.390  1.00 44.66  ? 249 GLU   B N   1 
ATOM   4891 C CA  . GLU   B 2 279 ? -17.442 79.299 96.765  1.00 44.46  ? 249 GLU   B CA  1 
ATOM   4892 C C   . GLU   B 2 279 ? -17.318 79.277 95.243  1.00 44.29  ? 249 GLU   B C   1 
ATOM   4893 O O   . GLU   B 2 279 ? -17.016 80.317 94.665  1.00 44.28  ? 249 GLU   B O   1 
ATOM   4894 C CB  . GLU   B 2 279 ? -16.028 79.398 97.337  1.00 46.25  ? 249 GLU   B CB  1 
ATOM   4895 C CG  . GLU   B 2 279 ? -15.926 79.372 98.848  1.00 51.07  ? 249 GLU   B CG  1 
ATOM   4896 C CD  . GLU   B 2 279 ? -14.489 79.281 99.326  1.00 57.97  ? 249 GLU   B CD  1 
ATOM   4897 O OE1 . GLU   B 2 279 ? -13.597 79.805 98.618  1.00 58.19  ? 249 GLU   B OE1 1 
ATOM   4898 O OE2 . GLU   B 2 279 ? -14.253 78.677 100.401 1.00 60.84  ? 249 GLU   B OE2 1 
ATOM   4899 N N   . MET   B 2 280 ? -17.493 78.119 94.598  1.00 44.09  ? 250 MET   B N   1 
ATOM   4900 C CA  . MET   B 2 280 ? -17.234 78.004 93.169  1.00 44.71  ? 250 MET   B CA  1 
ATOM   4901 C C   . MET   B 2 280 ? -18.169 78.715 92.215  1.00 45.62  ? 250 MET   B C   1 
ATOM   4902 O O   . MET   B 2 280 ? -17.708 79.043 91.117  1.00 46.16  ? 250 MET   B O   1 
ATOM   4903 C CB  . MET   B 2 280 ? -17.107 76.553 92.705  1.00 45.09  ? 250 MET   B CB  1 
ATOM   4904 C CG  . MET   B 2 280 ? -15.705 75.955 92.874  1.00 45.37  ? 250 MET   B CG  1 
ATOM   4905 S SD  . MET   B 2 280 ? -14.290 77.043 92.604  1.00 41.35  ? 250 MET   B SD  1 
ATOM   4906 C CE  . MET   B 2 280 ? -14.572 77.568 90.944  1.00 37.60  ? 250 MET   B CE  1 
ATOM   4907 N N   . ALA   B 2 281 ? -19.450 78.916 92.560  1.00 45.41  ? 251 ALA   B N   1 
ATOM   4908 C CA  . ALA   B 2 281 ? -20.338 79.621 91.629  1.00 45.66  ? 251 ALA   B CA  1 
ATOM   4909 C C   . ALA   B 2 281 ? -19.907 81.088 91.502  1.00 45.78  ? 251 ALA   B C   1 
ATOM   4910 O O   . ALA   B 2 281 ? -19.980 81.646 90.413  1.00 46.45  ? 251 ALA   B O   1 
ATOM   4911 C CB  . ALA   B 2 281 ? -21.785 79.514 92.077  1.00 46.05  ? 251 ALA   B CB  1 
ATOM   4912 N N   . THR   B 2 282 ? -19.404 81.689 92.601  1.00 45.12  ? 252 THR   B N   1 
ATOM   4913 C CA  . THR   B 2 282 ? -18.922 83.068 92.659  1.00 44.55  ? 252 THR   B CA  1 
ATOM   4914 C C   . THR   B 2 282 ? -17.562 83.154 91.986  1.00 43.94  ? 252 THR   B C   1 
ATOM   4915 O O   . THR   B 2 282 ? -17.332 84.086 91.207  1.00 44.30  ? 252 THR   B O   1 
ATOM   4916 C CB  . THR   B 2 282 ? -18.787 83.587 94.101  1.00 45.87  ? 252 THR   B CB  1 
ATOM   4917 O OG1 . THR   B 2 282 ? -19.663 82.907 95.004  1.00 47.43  ? 252 THR   B OG1 1 
ATOM   4918 C CG2 . THR   B 2 282 ? -18.997 85.079 94.191  1.00 46.32  ? 252 THR   B CG2 1 
ATOM   4919 N N   . ILE   B 2 283 ? -16.660 82.186 92.254  1.00 42.75  ? 253 ILE   B N   1 
ATOM   4920 C CA  . ILE   B 2 283 ? -15.351 82.209 91.616  1.00 42.67  ? 253 ILE   B CA  1 
ATOM   4921 C C   . ILE   B 2 283 ? -15.477 82.056 90.105  1.00 44.28  ? 253 ILE   B C   1 
ATOM   4922 O O   . ILE   B 2 283 ? -14.716 82.682 89.382  1.00 44.71  ? 253 ILE   B O   1 
ATOM   4923 C CB  . ILE   B 2 283 ? -14.341 81.227 92.231  1.00 42.22  ? 253 ILE   B CB  1 
ATOM   4924 C CG1 . ILE   B 2 283 ? -14.178 81.466 93.737  1.00 42.05  ? 253 ILE   B CG1 1 
ATOM   4925 C CG2 . ILE   B 2 283 ? -13.003 81.334 91.516  1.00 42.81  ? 253 ILE   B CG2 1 
ATOM   4926 C CD1 . ILE   B 2 283 ? -13.270 80.493 94.459  1.00 42.38  ? 253 ILE   B CD1 1 
ATOM   4927 N N   . LEU   B 2 284 ? -16.478 81.296 89.617  1.00 45.26  ? 254 LEU   B N   1 
ATOM   4928 C CA  . LEU   B 2 284 ? -16.710 81.142 88.178  1.00 46.68  ? 254 LEU   B CA  1 
ATOM   4929 C C   . LEU   B 2 284 ? -17.298 82.412 87.560  1.00 48.51  ? 254 LEU   B C   1 
ATOM   4930 O O   . LEU   B 2 284 ? -17.086 82.653 86.373  1.00 49.16  ? 254 LEU   B O   1 
ATOM   4931 C CB  . LEU   B 2 284 ? -17.625 79.955 87.877  1.00 46.79  ? 254 LEU   B CB  1 
ATOM   4932 C CG  . LEU   B 2 284 ? -16.979 78.577 87.932  1.00 48.25  ? 254 LEU   B CG  1 
ATOM   4933 C CD1 . LEU   B 2 284 ? -18.024 77.483 87.844  1.00 48.63  ? 254 LEU   B CD1 1 
ATOM   4934 C CD2 . LEU   B 2 284 ? -15.958 78.412 86.833  1.00 48.88  ? 254 LEU   B CD2 1 
ATOM   4935 N N   . SER   B 2 285 ? -18.034 83.221 88.341  1.00 49.21  ? 255 SER   B N   1 
ATOM   4936 C CA  . SER   B 2 285 ? -18.605 84.458 87.812  1.00 50.80  ? 255 SER   B CA  1 
ATOM   4937 C C   . SER   B 2 285 ? -17.540 85.556 87.683  1.00 52.59  ? 255 SER   B C   1 
ATOM   4938 O O   . SER   B 2 285 ? -17.623 86.375 86.769  1.00 53.26  ? 255 SER   B O   1 
ATOM   4939 C CB  . SER   B 2 285 ? -19.791 84.928 88.652  1.00 51.64  ? 255 SER   B CB  1 
ATOM   4940 O OG  . SER   B 2 285 ? -19.405 85.651 89.809  1.00 53.42  ? 255 SER   B OG  1 
ATOM   4941 N N   . LYS   B 2 286 ? -16.554 85.575 88.601  1.00 52.91  ? 256 LYS   B N   1 
ATOM   4942 C CA  . LYS   B 2 286 ? -15.462 86.545 88.605  1.00 53.74  ? 256 LYS   B CA  1 
ATOM   4943 C C   . LYS   B 2 286 ? -14.489 86.343 87.437  1.00 55.77  ? 256 LYS   B C   1 
ATOM   4944 O O   . LYS   B 2 286 ? -13.825 87.290 87.007  1.00 56.32  ? 256 LYS   B O   1 
ATOM   4945 C CB  . LYS   B 2 286 ? -14.673 86.430 89.906  1.00 54.74  ? 256 LYS   B CB  1 
ATOM   4946 C CG  . LYS   B 2 286 ? -15.377 86.941 91.148  1.00 57.51  ? 256 LYS   B CG  1 
ATOM   4947 C CD  . LYS   B 2 286 ? -14.322 87.214 92.214  1.00 60.89  ? 256 LYS   B CD  1 
ATOM   4948 C CE  . LYS   B 2 286 ? -14.868 87.663 93.547  1.00 63.76  ? 256 LYS   B CE  1 
ATOM   4949 N NZ  . LYS   B 2 286 ? -13.760 88.051 94.467  1.00 64.91  ? 256 LYS   B NZ  1 
ATOM   4950 N N   . MET   B 2 287 ? -14.371 85.106 86.969  1.00 56.75  ? 257 MET   B N   1 
ATOM   4951 C CA  . MET   B 2 287 ? -13.514 84.658 85.882  1.00 58.38  ? 257 MET   B CA  1 
ATOM   4952 C C   . MET   B 2 287 ? -13.728 85.455 84.599  1.00 60.51  ? 257 MET   B C   1 
ATOM   4953 O O   . MET   B 2 287 ? -14.867 85.791 84.300  1.00 60.72  ? 257 MET   B O   1 
ATOM   4954 C CB  . MET   B 2 287 ? -13.871 83.190 85.633  1.00 58.74  ? 257 MET   B CB  1 
ATOM   4955 C CG  . MET   B 2 287 ? -12.966 82.484 84.693  1.00 60.02  ? 257 MET   B CG  1 
ATOM   4956 S SD  . MET   B 2 287 ? -13.371 80.749 84.676  1.00 59.97  ? 257 MET   B SD  1 
ATOM   4957 C CE  . MET   B 2 287 ? -15.023 80.797 83.959  1.00 56.37  ? 257 MET   B CE  1 
ATOM   4958 N N   . PRO   B 2 288 ? -12.669 85.756 83.813  1.00 62.21  ? 258 PRO   B N   1 
ATOM   4959 C CA  . PRO   B 2 288 ? -12.872 86.491 82.550  1.00 63.79  ? 258 PRO   B CA  1 
ATOM   4960 C C   . PRO   B 2 288 ? -13.600 85.672 81.484  1.00 66.31  ? 258 PRO   B C   1 
ATOM   4961 O O   . PRO   B 2 288 ? -13.433 84.453 81.401  1.00 66.37  ? 258 PRO   B O   1 
ATOM   4962 C CB  . PRO   B 2 288 ? -11.450 86.844 82.109  1.00 64.01  ? 258 PRO   B CB  1 
ATOM   4963 C CG  . PRO   B 2 288 ? -10.609 85.814 82.715  1.00 63.98  ? 258 PRO   B CG  1 
ATOM   4964 C CD  . PRO   B 2 288 ? -11.243 85.459 84.032  1.00 62.06  ? 258 PRO   B CD  1 
ATOM   4965 N N   . LYS   B 2 289 ? -14.443 86.338 80.687  1.00 68.21  ? 259 LYS   B N   1 
ATOM   4966 C CA  . LYS   B 2 289 ? -15.234 85.649 79.670  1.00 70.48  ? 259 LYS   B CA  1 
ATOM   4967 C C   . LYS   B 2 289 ? -14.848 86.063 78.235  1.00 72.92  ? 259 LYS   B C   1 
ATOM   4968 O O   . LYS   B 2 289 ? -14.262 87.131 78.018  1.00 72.98  ? 259 LYS   B O   1 
ATOM   4969 C CB  . LYS   B 2 289 ? -16.741 85.821 79.954  1.00 72.27  ? 259 LYS   B CB  1 
ATOM   4970 C CG  . LYS   B 2 289 ? -17.170 85.413 81.373  1.00 75.69  ? 259 LYS   B CG  1 
ATOM   4971 C CD  . LYS   B 2 289 ? -16.829 83.962 81.718  1.00 78.61  ? 259 LYS   B CD  1 
ATOM   4972 C CE  . LYS   B 2 289 ? -17.510 83.506 82.984  1.00 81.07  ? 259 LYS   B CE  1 
ATOM   4973 N NZ  . LYS   B 2 289 ? -17.252 84.428 84.117  1.00 82.74  ? 259 LYS   B NZ  1 
ATOM   4974 N N   . PRO   B 2 290 ? -15.119 85.193 77.248  1.00 74.71  ? 260 PRO   B N   1 
ATOM   4975 C CA  . PRO   B 2 290 ? -14.701 85.492 75.876  1.00 76.41  ? 260 PRO   B CA  1 
ATOM   4976 C C   . PRO   B 2 290 ? -15.382 86.691 75.235  1.00 79.07  ? 260 PRO   B C   1 
ATOM   4977 O O   . PRO   B 2 290 ? -16.606 86.795 75.281  1.00 79.58  ? 260 PRO   B O   1 
ATOM   4978 C CB  . PRO   B 2 290 ? -15.057 84.214 75.111  1.00 76.82  ? 260 PRO   B CB  1 
ATOM   4979 C CG  . PRO   B 2 290 ? -15.252 83.154 76.141  1.00 76.82  ? 260 PRO   B CG  1 
ATOM   4980 C CD  . PRO   B 2 290 ? -15.761 83.869 77.342  1.00 74.74  ? 260 PRO   B CD  1 
ATOM   4981 N N   . LYS   B 2 291 ? -14.587 87.577 74.608  1.00 80.53  ? 261 LYS   B N   1 
ATOM   4982 C CA  . LYS   B 2 291 ? -15.103 88.731 73.878  1.00 82.44  ? 261 LYS   B CA  1 
ATOM   4983 C C   . LYS   B 2 291 ? -15.798 88.197 72.619  1.00 84.59  ? 261 LYS   B C   1 
ATOM   4984 O O   . LYS   B 2 291 ? -15.218 87.396 71.896  1.00 84.85  ? 261 LYS   B O   1 
ATOM   4985 C CB  . LYS   B 2 291 ? -13.948 89.681 73.505  1.00 84.04  ? 261 LYS   B CB  1 
ATOM   4986 C CG  . LYS   B 2 291 ? -14.341 90.816 72.571  1.00 87.92  ? 261 LYS   B CG  1 
ATOM   4987 C CD  . LYS   B 2 291 ? -13.224 91.840 72.407  1.00 92.14  ? 261 LYS   B CD  1 
ATOM   4988 C CE  . LYS   B 2 291 ? -13.079 92.742 73.613  1.00 96.04  ? 261 LYS   B CE  1 
ATOM   4989 N NZ  . LYS   B 2 291 ? -12.011 93.767 73.429  1.00 98.36  ? 261 LYS   B NZ  1 
ATOM   4990 N N   . PRO   B 2 292 ? -17.066 88.565 72.377  1.00 86.03  ? 262 PRO   B N   1 
ATOM   4991 C CA  . PRO   B 2 292 ? -17.772 88.038 71.192  1.00 86.87  ? 262 PRO   B CA  1 
ATOM   4992 C C   . PRO   B 2 292 ? -17.347 88.721 69.883  1.00 87.80  ? 262 PRO   B C   1 
ATOM   4993 O O   . PRO   B 2 292 ? -16.735 89.793 69.908  1.00 87.65  ? 262 PRO   B O   1 
ATOM   4994 C CB  . PRO   B 2 292 ? -19.238 88.322 71.525  1.00 87.63  ? 262 PRO   B CB  1 
ATOM   4995 C CG  . PRO   B 2 292 ? -19.174 89.610 72.305  1.00 88.02  ? 262 PRO   B CG  1 
ATOM   4996 C CD  . PRO   B 2 292 ? -17.911 89.504 73.145  1.00 86.06  ? 262 PRO   B CD  1 
ATOM   4997 N N   . PRO   B 2 293 ? -17.669 88.123 68.724  1.00 88.53  ? 263 PRO   B N   1 
ATOM   4998 C CA  . PRO   B 2 293 ? -17.291 88.754 67.448  1.00 89.43  ? 263 PRO   B CA  1 
ATOM   4999 C C   . PRO   B 2 293 ? -18.048 90.052 67.180  1.00 91.15  ? 263 PRO   B C   1 
ATOM   5000 O O   . PRO   B 2 293 ? -19.161 90.217 67.671  1.00 91.44  ? 263 PRO   B O   1 
ATOM   5001 C CB  . PRO   B 2 293 ? -17.636 87.683 66.410  1.00 89.74  ? 263 PRO   B CB  1 
ATOM   5002 C CG  . PRO   B 2 293 ? -18.691 86.869 67.049  1.00 89.88  ? 263 PRO   B CG  1 
ATOM   5003 C CD  . PRO   B 2 293 ? -18.387 86.852 68.513  1.00 88.08  ? 263 PRO   B CD  1 
ATOM   5004 N N   . PRO   B 2 294 ? -17.464 90.988 66.407  1.00 92.27  ? 264 PRO   B N   1 
ATOM   5005 C CA  . PRO   B 2 294 ? -18.153 92.259 66.136  1.00 93.32  ? 264 PRO   B CA  1 
ATOM   5006 C C   . PRO   B 2 294 ? -19.589 92.131 65.631  1.00 94.80  ? 264 PRO   B C   1 
ATOM   5007 O O   . PRO   B 2 294 ? -19.866 91.414 64.664  1.00 94.90  ? 264 PRO   B O   1 
ATOM   5008 C CB  . PRO   B 2 294 ? -17.239 92.942 65.115  1.00 93.68  ? 264 PRO   B CB  1 
ATOM   5009 C CG  . PRO   B 2 294 ? -15.893 92.407 65.418  1.00 93.80  ? 264 PRO   B CG  1 
ATOM   5010 C CD  . PRO   B 2 294 ? -16.133 90.964 65.775  1.00 92.03  ? 264 PRO   B CD  1 
ATOM   5011 N N   . ASN   B 2 295 ? -20.506 92.814 66.334  1.00 95.58  ? 265 ASN   B N   1 
ATOM   5012 C CA  . ASN   B 2 295 ? -21.935 92.819 66.036  1.00 96.71  ? 265 ASN   B CA  1 
ATOM   5013 C C   . ASN   B 2 295 ? -22.553 94.216 66.232  1.00 97.13  ? 265 ASN   B C   1 
ATOM   5014 O O   . ASN   B 2 295 ? -21.840 95.221 66.297  1.00 97.23  ? 265 ASN   B O   1 
ATOM   5015 C CB  . ASN   B 2 295 ? -22.670 91.762 66.882  1.00 98.44  ? 265 ASN   B CB  1 
ATOM   5016 C CG  . ASN   B 2 295 ? -22.302 91.748 68.355  1.00 102.58 ? 265 ASN   B CG  1 
ATOM   5017 O OD1 . ASN   B 2 295 ? -22.164 92.790 69.004  1.00 103.99 ? 265 ASN   B OD1 1 
ATOM   5018 N ND2 . ASN   B 2 295 ? -22.143 90.556 68.926  1.00 103.52 ? 265 ASN   B ND2 1 
HETATM 5019 C C1  . EDO   C 3 .   ? 27.983  47.723 61.753  1.00 74.05  ? 501 EDO   A C1  1 
HETATM 5020 O O1  . EDO   C 3 .   ? 28.351  49.084 61.913  1.00 74.05  ? 501 EDO   A O1  1 
HETATM 5021 C C2  . EDO   C 3 .   ? 29.183  46.827 61.943  1.00 74.08  ? 501 EDO   A C2  1 
HETATM 5022 O O2  . EDO   C 3 .   ? 28.996  45.993 63.078  1.00 74.05  ? 501 EDO   A O2  1 
HETATM 5023 C C1  . GOL   D 4 .   ? 18.660  62.310 61.703  1.00 65.06  ? 502 GOL   A C1  1 
HETATM 5024 O O1  . GOL   D 4 .   ? 20.013  61.946 61.435  1.00 65.29  ? 502 GOL   A O1  1 
HETATM 5025 C C2  . GOL   D 4 .   ? 18.218  61.868 63.085  1.00 64.64  ? 502 GOL   A C2  1 
HETATM 5026 O O2  . GOL   D 4 .   ? 16.854  62.252 63.309  1.00 64.58  ? 502 GOL   A O2  1 
HETATM 5027 C C3  . GOL   D 4 .   ? 19.102  62.417 64.186  1.00 64.07  ? 502 GOL   A C3  1 
HETATM 5028 O O3  . GOL   D 4 .   ? 18.910  61.717 65.408  1.00 63.54  ? 502 GOL   A O3  1 
HETATM 5029 N N1  . A1IS8 E 5 .   ? 7.816   59.751 51.732  1.00 46.82  ? 503 A1IS8 A N1  1 
HETATM 5030 N N3  . A1IS8 E 5 .   ? 5.050   54.362 50.195  1.00 45.31  ? 503 A1IS8 A N3  1 
HETATM 5031 C C4  . A1IS8 E 5 .   ? 6.817   59.059 52.309  1.00 46.79  ? 503 A1IS8 A C4  1 
HETATM 5032 C C5  . A1IS8 E 5 .   ? 8.046   59.454 50.446  1.00 46.66  ? 503 A1IS8 A C5  1 
HETATM 5033 C C6  . A1IS8 E 5 .   ? 7.337   58.504 49.745  1.00 46.53  ? 503 A1IS8 A C6  1 
HETATM 5034 C C7  . A1IS8 E 5 .   ? 6.330   57.853 50.434  1.00 46.30  ? 503 A1IS8 A C7  1 
HETATM 5035 C C8  . A1IS8 E 5 .   ? 5.543   56.710 49.838  1.00 45.68  ? 503 A1IS8 A C8  1 
HETATM 5036 C C10 . A1IS8 E 5 .   ? 4.976   55.213 47.875  1.00 45.42  ? 503 A1IS8 A C10 1 
HETATM 5037 C C13 . A1IS8 E 5 .   ? 4.106   53.797 50.971  1.00 45.34  ? 503 A1IS8 A C13 1 
HETATM 5038 C C15 . A1IS8 E 5 .   ? 3.345   53.433 53.329  1.00 45.42  ? 503 A1IS8 A C15 1 
HETATM 5039 C C17 . A1IS8 E 5 .   ? 3.921   55.576 52.976  1.00 45.24  ? 503 A1IS8 A C17 1 
HETATM 5040 N N5  . A1IS8 E 5 .   ? 2.957   57.302 56.001  1.00 45.00  ? 503 A1IS8 A N5  1 
HETATM 5041 C C18 . A1IS8 E 5 .   ? 3.161   56.501 55.210  1.00 45.09  ? 503 A1IS8 A C18 1 
HETATM 5042 C C16 . A1IS8 E 5 .   ? 3.394   55.474 54.240  1.00 45.28  ? 503 A1IS8 A C16 1 
HETATM 5043 N N4  . A1IS8 E 5 .   ? 3.052   54.162 54.443  1.00 45.36  ? 503 A1IS8 A N4  1 
HETATM 5044 C C14 . A1IS8 E 5 .   ? 3.877   54.287 52.376  1.00 45.27  ? 503 A1IS8 A C14 1 
HETATM 5045 O O   . A1IS8 E 5 .   ? 3.355   52.922 50.563  1.00 45.56  ? 503 A1IS8 A O   1 
HETATM 5046 C C11 . A1IS8 E 5 .   ? 5.245   54.008 48.780  1.00 45.26  ? 503 A1IS8 A C11 1 
HETATM 5047 C C9  . A1IS8 E 5 .   ? 5.739   56.462 48.339  1.00 45.41  ? 503 A1IS8 A C9  1 
HETATM 5048 C C12 . A1IS8 E 5 .   ? 5.929   55.450 50.618  1.00 45.44  ? 503 A1IS8 A C12 1 
HETATM 5049 N N2  . A1IS8 E 5 .   ? 6.030   58.139 51.711  1.00 46.59  ? 503 A1IS8 A N2  1 
HETATM 5050 N N   . A1IS8 E 5 .   ? 6.615   59.248 53.645  1.00 46.75  ? 503 A1IS8 A N   1 
HETATM 5051 C C2  . A1IS8 E 5 .   ? 7.324   60.243 54.456  1.00 46.73  ? 503 A1IS8 A C2  1 
HETATM 5052 C C1  . A1IS8 E 5 .   ? 6.820   59.962 55.864  1.00 46.90  ? 503 A1IS8 A C1  1 
HETATM 5053 C C3  . A1IS8 E 5 .   ? 5.658   58.476 54.436  1.00 46.83  ? 503 A1IS8 A C3  1 
HETATM 5054 C C   . A1IS8 E 5 .   ? 5.472   59.316 55.642  1.00 47.08  ? 503 A1IS8 A C   1 
HETATM 5055 F F   . A1IS8 E 5 .   ? 4.530   60.315 55.326  1.00 47.33  ? 503 A1IS8 A F   1 
HETATM 5056 S S   . DMS   F 6 .   ? -3.367  52.009 94.006  1.00 94.52  ? 301 DMS   B S   1 
HETATM 5057 O O   . DMS   F 6 .   ? -4.472  52.031 92.986  1.00 94.52  ? 301 DMS   B O   1 
HETATM 5058 C C1  . DMS   F 6 .   ? -2.123  50.820 93.438  1.00 94.46  ? 301 DMS   B C1  1 
HETATM 5059 C C2  . DMS   F 6 .   ? -3.943  51.083 95.467  1.00 94.31  ? 301 DMS   B C2  1 
HETATM 5060 S S   . DMS   G 6 .   ? 10.980  59.087 106.326 1.00 95.04  ? 302 DMS   B S   1 
HETATM 5061 O O   . DMS   G 6 .   ? 11.947  60.063 105.707 1.00 95.02  ? 302 DMS   B O   1 
HETATM 5062 C C1  . DMS   G 6 .   ? 9.402   59.945 106.449 1.00 94.97  ? 302 DMS   B C1  1 
HETATM 5063 C C2  . DMS   G 6 .   ? 11.248  59.045 108.123 1.00 95.04  ? 302 DMS   B C2  1 
HETATM 5064 C C1  . GOL   H 4 .   ? 6.170   55.625 81.360  1.00 69.77  ? 303 GOL   B C1  1 
HETATM 5065 O O1  . GOL   H 4 .   ? 7.194   55.806 82.337  1.00 69.58  ? 303 GOL   B O1  1 
HETATM 5066 C C2  . GOL   H 4 .   ? 5.320   56.870 81.192  1.00 69.88  ? 303 GOL   B C2  1 
HETATM 5067 O O2  . GOL   H 4 .   ? 4.619   57.169 82.411  1.00 69.70  ? 303 GOL   B O2  1 
HETATM 5068 C C3  . GOL   H 4 .   ? 4.338   56.760 80.038  1.00 69.77  ? 303 GOL   B C3  1 
HETATM 5069 O O3  . GOL   H 4 .   ? 4.962   56.933 78.770  1.00 69.32  ? 303 GOL   B O3  1 
HETATM 5070 O O   . HOH   I 7 .   ? -6.923  64.211 58.216  1.00 55.51  ? 601 HOH   A O   1 
HETATM 5071 O O   . HOH   I 7 .   ? 4.895   40.592 60.937  1.00 43.24  ? 602 HOH   A O   1 
HETATM 5072 O O   . HOH   I 7 .   ? 11.920  38.923 68.475  1.00 46.14  ? 603 HOH   A O   1 
HETATM 5073 O O   . HOH   I 7 .   ? 10.301  62.809 64.543  1.00 39.78  ? 604 HOH   A O   1 
HETATM 5074 O O   . HOH   I 7 .   ? 12.385  64.446 58.058  1.00 49.28  ? 605 HOH   A O   1 
HETATM 5075 O O   . HOH   I 7 .   ? 14.836  70.295 56.478  1.00 45.04  ? 606 HOH   A O   1 
HETATM 5076 O O   . HOH   I 7 .   ? 9.254   39.197 51.613  1.00 26.47  ? 607 HOH   A O   1 
HETATM 5077 O O   . HOH   I 7 .   ? 29.540  32.986 55.502  1.00 28.92  ? 608 HOH   A O   1 
HETATM 5078 O O   . HOH   I 7 .   ? 10.815  25.290 51.273  1.00 44.09  ? 609 HOH   A O   1 
HETATM 5079 O O   . HOH   I 7 .   ? 2.757   51.957 62.270  1.00 40.85  ? 610 HOH   A O   1 
HETATM 5080 O O   . HOH   I 7 .   ? 12.082  35.454 48.871  1.00 43.39  ? 611 HOH   A O   1 
HETATM 5081 O O   . HOH   I 7 .   ? 29.190  39.173 54.566  1.00 60.73  ? 612 HOH   A O   1 
HETATM 5082 O O   . HOH   I 7 .   ? 4.299   44.446 66.546  1.00 50.66  ? 613 HOH   A O   1 
HETATM 5083 O O   . HOH   I 7 .   ? -2.735  75.426 58.831  1.00 54.83  ? 614 HOH   A O   1 
HETATM 5084 O O   . HOH   I 7 .   ? 4.655   30.881 71.407  1.00 51.22  ? 615 HOH   A O   1 
HETATM 5085 O O   . HOH   I 7 .   ? -4.436  37.995 65.285  1.00 43.28  ? 616 HOH   A O   1 
HETATM 5086 O O   . HOH   I 7 .   ? 22.637  52.096 61.182  1.00 44.43  ? 617 HOH   A O   1 
HETATM 5087 O O   . HOH   I 7 .   ? 3.938   63.740 71.789  1.00 26.12  ? 618 HOH   A O   1 
HETATM 5088 O O   . HOH   I 7 .   ? 22.845  36.442 66.295  1.00 44.06  ? 619 HOH   A O   1 
HETATM 5089 O O   . HOH   I 7 .   ? 8.456   26.174 72.205  1.00 44.45  ? 620 HOH   A O   1 
HETATM 5090 O O   . HOH   I 7 .   ? 11.176  36.967 70.551  1.00 31.13  ? 621 HOH   A O   1 
HETATM 5091 O O   . HOH   I 7 .   ? -2.971  19.197 54.176  1.00 35.56  ? 622 HOH   A O   1 
HETATM 5092 O O   . HOH   I 7 .   ? 24.870  42.441 50.484  1.00 49.50  ? 623 HOH   A O   1 
HETATM 5093 O O   . HOH   I 7 .   ? 23.369  33.770 62.858  1.00 25.63  ? 624 HOH   A O   1 
HETATM 5094 O O   . HOH   I 7 .   ? 4.252   36.280 56.656  1.00 41.58  ? 625 HOH   A O   1 
HETATM 5095 O O   . HOH   I 7 .   ? 5.729   45.128 61.866  1.00 35.67  ? 626 HOH   A O   1 
HETATM 5096 O O   . HOH   I 7 .   ? 27.497  42.393 64.512  1.00 30.61  ? 627 HOH   A O   1 
HETATM 5097 O O   . HOH   I 7 .   ? 24.034  58.869 41.950  1.00 44.01  ? 628 HOH   A O   1 
HETATM 5098 O O   . HOH   I 7 .   ? 25.342  34.365 61.044  1.00 24.06  ? 629 HOH   A O   1 
HETATM 5099 O O   . HOH   I 7 .   ? 11.429  60.271 64.403  1.00 22.87  ? 630 HOH   A O   1 
HETATM 5100 O O   . HOH   I 7 .   ? 15.431  66.848 59.309  1.00 54.08  ? 631 HOH   A O   1 
HETATM 5101 O O   . HOH   I 7 .   ? 9.191   60.710 74.796  1.00 30.71  ? 632 HOH   A O   1 
HETATM 5102 O O   . HOH   I 7 .   ? 13.810  43.667 69.411  1.00 27.54  ? 633 HOH   A O   1 
HETATM 5103 O O   . HOH   I 7 .   ? -5.187  75.261 55.103  1.00 46.60  ? 634 HOH   A O   1 
HETATM 5104 O O   . HOH   I 7 .   ? 2.292   51.312 56.396  1.00 45.58  ? 635 HOH   A O   1 
HETATM 5105 O O   . HOH   I 7 .   ? 16.704  63.992 59.251  1.00 46.62  ? 636 HOH   A O   1 
HETATM 5106 O O   . HOH   I 7 .   ? -8.204  39.676 58.956  1.00 47.70  ? 637 HOH   A O   1 
HETATM 5107 O O   . HOH   I 7 .   ? 13.960  60.395 63.891  1.00 41.91  ? 638 HOH   A O   1 
HETATM 5108 O O   . HOH   I 7 .   ? -8.962  61.006 52.356  1.00 43.34  ? 639 HOH   A O   1 
HETATM 5109 O O   . HOH   I 7 .   ? 10.886  22.993 73.004  1.00 44.44  ? 640 HOH   A O   1 
HETATM 5110 O O   . HOH   I 7 .   ? 16.001  61.729 48.823  1.00 31.52  ? 641 HOH   A O   1 
HETATM 5111 O O   . HOH   I 7 .   ? 10.173  60.960 52.696  1.00 42.86  ? 642 HOH   A O   1 
HETATM 5112 O O   . HOH   I 7 .   ? 23.436  46.649 69.226  1.00 50.97  ? 643 HOH   A O   1 
HETATM 5113 O O   . HOH   I 7 .   ? 0.700   11.308 55.603  1.00 47.86  ? 644 HOH   A O   1 
HETATM 5114 O O   . HOH   I 7 .   ? 15.579  61.073 60.742  1.00 43.46  ? 645 HOH   A O   1 
HETATM 5115 O O   . HOH   I 7 .   ? 7.586   17.436 67.349  1.00 55.29  ? 646 HOH   A O   1 
HETATM 5116 O O   . HOH   I 7 .   ? 8.204   44.465 46.583  1.00 45.94  ? 647 HOH   A O   1 
HETATM 5117 O O   . HOH   I 7 .   ? -1.322  53.731 57.954  1.00 45.95  ? 648 HOH   A O   1 
HETATM 5118 O O   . HOH   I 7 .   ? 18.938  72.987 48.491  1.00 61.40  ? 649 HOH   A O   1 
HETATM 5119 O O   . HOH   I 7 .   ? 16.047  34.997 42.468  1.00 38.38  ? 650 HOH   A O   1 
HETATM 5120 O O   . HOH   I 7 .   ? 8.727   75.731 56.363  1.00 48.03  ? 651 HOH   A O   1 
HETATM 5121 O O   . HOH   I 7 .   ? 8.533   78.547 57.952  1.00 45.21  ? 652 HOH   A O   1 
HETATM 5122 O O   . HOH   I 7 .   ? -0.642  75.514 61.102  1.00 38.06  ? 653 HOH   A O   1 
HETATM 5123 O O   . HOH   I 7 .   ? 8.588   20.159 57.489  1.00 51.66  ? 654 HOH   A O   1 
HETATM 5124 O O   . HOH   I 7 .   ? 5.557   46.983 50.718  1.00 28.16  ? 655 HOH   A O   1 
HETATM 5125 O O   . HOH   I 7 .   ? 6.965   18.755 50.593  1.00 57.16  ? 656 HOH   A O   1 
HETATM 5126 O O   . HOH   I 7 .   ? 24.253  43.491 47.586  1.00 40.61  ? 657 HOH   A O   1 
HETATM 5127 O O   . HOH   I 7 .   ? -11.568 93.548 69.468  1.00 56.25  ? 658 HOH   A O   1 
HETATM 5128 O O   . HOH   I 7 .   ? -18.256 82.426 72.373  1.00 47.66  ? 659 HOH   A O   1 
HETATM 5129 O O   . HOH   I 7 .   ? -13.350 61.531 59.070  1.00 55.80  ? 660 HOH   A O   1 
HETATM 5130 O O   . HOH   I 7 .   ? 0.232   73.092 45.251  1.00 33.49  ? 661 HOH   A O   1 
HETATM 5131 O O   . HOH   I 7 .   ? -7.232  28.140 47.817  1.00 53.78  ? 662 HOH   A O   1 
HETATM 5132 O O   . HOH   I 7 .   ? 35.078  38.401 56.166  1.00 39.04  ? 663 HOH   A O   1 
HETATM 5133 O O   . HOH   I 7 .   ? 19.931  62.736 51.137  1.00 40.61  ? 664 HOH   A O   1 
HETATM 5134 O O   . HOH   I 7 .   ? 6.738   37.945 52.050  1.00 25.05  ? 665 HOH   A O   1 
HETATM 5135 O O   . HOH   I 7 .   ? -9.500  26.565 66.904  1.00 57.60  ? 666 HOH   A O   1 
HETATM 5136 O O   . HOH   I 7 .   ? -2.944  73.997 56.480  1.00 46.89  ? 667 HOH   A O   1 
HETATM 5137 O O   . HOH   I 7 .   ? 23.275  55.728 58.848  1.00 44.73  ? 668 HOH   A O   1 
HETATM 5138 O O   . HOH   I 7 .   ? 18.629  35.099 43.712  1.00 51.80  ? 669 HOH   A O   1 
HETATM 5139 O O   . HOH   I 7 .   ? 0.993   77.884 62.508  1.00 38.21  ? 670 HOH   A O   1 
HETATM 5140 O O   . HOH   I 7 .   ? 1.245   42.510 55.324  1.00 43.76  ? 671 HOH   A O   1 
HETATM 5141 O O   . HOH   I 7 .   ? 8.037   34.129 45.852  1.00 38.41  ? 672 HOH   A O   1 
HETATM 5142 O O   . HOH   I 7 .   ? 0.765   38.250 70.969  1.00 44.00  ? 673 HOH   A O   1 
HETATM 5143 O O   . HOH   I 7 .   ? -0.468  76.403 45.673  1.00 58.76  ? 674 HOH   A O   1 
HETATM 5144 O O   . HOH   I 7 .   ? 18.685  59.469 43.844  1.00 48.53  ? 675 HOH   A O   1 
HETATM 5145 O O   . HOH   I 7 .   ? 14.333  62.214 58.506  1.00 50.49  ? 676 HOH   A O   1 
HETATM 5146 O O   . HOH   I 7 .   ? 14.785  46.638 72.406  1.00 53.79  ? 677 HOH   A O   1 
HETATM 5147 O O   . HOH   I 7 .   ? 26.981  36.061 53.740  1.00 50.74  ? 678 HOH   A O   1 
HETATM 5148 O O   . HOH   I 7 .   ? 9.761   20.391 48.484  1.00 52.19  ? 679 HOH   A O   1 
HETATM 5149 O O   . HOH   I 7 .   ? -5.260  67.295 49.058  1.00 51.14  ? 680 HOH   A O   1 
HETATM 5150 O O   . HOH   I 7 .   ? 32.279  37.044 61.102  1.00 29.20  ? 681 HOH   A O   1 
HETATM 5151 O O   . HOH   I 7 .   ? 6.095   44.439 48.632  1.00 47.77  ? 682 HOH   A O   1 
HETATM 5152 O O   . HOH   I 7 .   ? -7.798  76.183 57.465  1.00 48.33  ? 683 HOH   A O   1 
HETATM 5153 O O   . HOH   I 7 .   ? 3.582   43.026 60.897  1.00 49.96  ? 684 HOH   A O   1 
HETATM 5154 O O   . HOH   I 7 .   ? -1.163  58.233 59.023  1.00 59.74  ? 685 HOH   A O   1 
HETATM 5155 O O   . HOH   I 7 .   ? -9.037  31.838 55.436  1.00 48.42  ? 686 HOH   A O   1 
HETATM 5156 O O   . HOH   I 7 .   ? 0.649   83.228 58.599  1.00 48.60  ? 687 HOH   A O   1 
HETATM 5157 O O   . HOH   I 7 .   ? -15.616 65.803 60.817  1.00 58.38  ? 688 HOH   A O   1 
HETATM 5158 O O   . HOH   I 7 .   ? -4.865  34.076 52.657  1.00 45.66  ? 689 HOH   A O   1 
HETATM 5159 O O   . HOH   I 7 .   ? 10.860  57.255 36.829  1.00 57.16  ? 690 HOH   A O   1 
HETATM 5160 O O   . HOH   I 7 .   ? 28.499  46.031 66.193  1.00 42.42  ? 691 HOH   A O   1 
HETATM 5161 O O   . HOH   I 7 .   ? 16.272  78.170 45.515  1.00 41.58  ? 692 HOH   A O   1 
HETATM 5162 O O   . HOH   I 7 .   ? -5.666  57.282 58.895  1.00 40.26  ? 693 HOH   A O   1 
HETATM 5163 O O   . HOH   I 7 .   ? 24.995  58.880 54.849  1.00 39.26  ? 694 HOH   A O   1 
HETATM 5164 O O   . HOH   I 7 .   ? 14.435  15.203 50.219  1.00 58.82  ? 695 HOH   A O   1 
HETATM 5165 O O   . HOH   I 7 .   ? 17.828  78.797 47.667  1.00 66.98  ? 696 HOH   A O   1 
HETATM 5166 O O   . HOH   I 7 .   ? -7.516  32.077 52.562  1.00 38.00  ? 697 HOH   A O   1 
HETATM 5167 O O   . HOH   I 7 .   ? 7.852   19.429 75.927  1.00 43.26  ? 698 HOH   A O   1 
HETATM 5168 O O   . HOH   I 7 .   ? 30.293  54.180 56.200  1.00 48.20  ? 699 HOH   A O   1 
HETATM 5169 O O   . HOH   I 7 .   ? 24.576  62.929 57.712  1.00 56.51  ? 700 HOH   A O   1 
HETATM 5170 O O   . HOH   I 7 .   ? 17.825  47.060 73.915  1.00 52.08  ? 701 HOH   A O   1 
HETATM 5171 O O   . HOH   I 7 .   ? 13.090  26.345 58.235  1.00 44.40  ? 702 HOH   A O   1 
HETATM 5172 O O   . HOH   I 7 .   ? 19.870  29.568 62.578  1.00 43.18  ? 703 HOH   A O   1 
HETATM 5173 O O   . HOH   I 7 .   ? 26.082  46.378 67.831  1.00 23.47  ? 704 HOH   A O   1 
HETATM 5174 O O   . HOH   I 7 .   ? 2.892   50.618 70.837  1.00 33.51  ? 705 HOH   A O   1 
HETATM 5175 O O   . HOH   I 7 .   ? 6.514   43.097 73.042  1.00 32.70  ? 706 HOH   A O   1 
HETATM 5176 O O   . HOH   I 7 .   ? 8.293   68.972 65.240  1.00 56.37  ? 707 HOH   A O   1 
HETATM 5177 O O   . HOH   I 7 .   ? 24.858  33.480 49.646  1.00 51.60  ? 708 HOH   A O   1 
HETATM 5178 O O   . HOH   I 7 .   ? -7.151  54.158 50.412  1.00 62.03  ? 709 HOH   A O   1 
HETATM 5179 O O   . HOH   I 7 .   ? 12.862  24.461 68.506  1.00 50.19  ? 710 HOH   A O   1 
HETATM 5180 O O   . HOH   I 7 .   ? 2.725   44.865 46.584  1.00 51.26  ? 711 HOH   A O   1 
HETATM 5181 O O   . HOH   I 7 .   ? 27.213  49.009 50.548  1.00 39.56  ? 712 HOH   A O   1 
HETATM 5182 O O   . HOH   I 7 .   ? -13.840 64.627 62.853  1.00 32.73  ? 713 HOH   A O   1 
HETATM 5183 O O   . HOH   I 7 .   ? -6.169  70.813 52.363  1.00 53.46  ? 714 HOH   A O   1 
HETATM 5184 O O   . HOH   I 7 .   ? 4.583   47.898 73.871  1.00 41.97  ? 715 HOH   A O   1 
HETATM 5185 O O   . HOH   I 7 .   ? 29.174  55.019 53.639  1.00 52.88  ? 716 HOH   A O   1 
HETATM 5186 O O   . HOH   I 7 .   ? 4.363   71.603 64.526  1.00 50.37  ? 717 HOH   A O   1 
HETATM 5187 O O   . HOH   I 7 .   ? 22.169  53.922 67.250  1.00 53.03  ? 718 HOH   A O   1 
HETATM 5188 O O   . HOH   I 7 .   ? 0.210   44.960 54.845  1.00 51.04  ? 719 HOH   A O   1 
HETATM 5189 O O   . HOH   I 7 .   ? 11.863  65.278 70.936  1.00 51.24  ? 720 HOH   A O   1 
HETATM 5190 O O   . HOH   I 7 .   ? 18.981  76.872 44.543  1.00 65.15  ? 721 HOH   A O   1 
HETATM 5191 O O   . HOH   I 7 .   ? -3.455  22.515 52.639  1.00 43.90  ? 722 HOH   A O   1 
HETATM 5192 O O   . HOH   I 7 .   ? 32.076  50.617 56.424  1.00 48.94  ? 723 HOH   A O   1 
HETATM 5193 O O   . HOH   I 7 .   ? -9.568  64.778 51.093  1.00 47.11  ? 724 HOH   A O   1 
HETATM 5194 O O   . HOH   I 7 .   ? -11.726 30.376 61.417  1.00 34.82  ? 725 HOH   A O   1 
HETATM 5195 O O   . HOH   I 7 .   ? 2.345   49.163 47.626  1.00 59.87  ? 726 HOH   A O   1 
HETATM 5196 O O   . HOH   I 7 .   ? 20.068  54.166 69.192  1.00 47.07  ? 727 HOH   A O   1 
HETATM 5197 O O   . HOH   I 7 .   ? -8.908  54.280 53.396  1.00 60.31  ? 728 HOH   A O   1 
HETATM 5198 O O   . HOH   I 7 .   ? 13.380  19.250 53.754  1.00 49.04  ? 729 HOH   A O   1 
HETATM 5199 O O   . HOH   I 7 .   ? 8.956   25.135 60.663  1.00 45.07  ? 730 HOH   A O   1 
HETATM 5200 O O   . HOH   I 7 .   ? -2.813  35.006 72.016  1.00 64.81  ? 731 HOH   A O   1 
HETATM 5201 O O   . HOH   I 7 .   ? 12.886  68.408 63.560  1.00 41.71  ? 732 HOH   A O   1 
HETATM 5202 O O   . HOH   I 7 .   ? 3.961   53.629 41.569  1.00 49.84  ? 733 HOH   A O   1 
HETATM 5203 O O   . HOH   I 7 .   ? 16.883  68.680 45.891  1.00 57.87  ? 734 HOH   A O   1 
HETATM 5204 O O   . HOH   I 7 .   ? 10.583  26.115 48.721  1.00 56.19  ? 735 HOH   A O   1 
HETATM 5205 O O   . HOH   I 7 .   ? 5.901   19.748 72.947  1.00 50.37  ? 736 HOH   A O   1 
HETATM 5206 O O   . HOH   I 7 .   ? 25.305  51.835 59.647  1.00 48.79  ? 737 HOH   A O   1 
HETATM 5207 O O   . HOH   I 7 .   ? 3.679   50.841 46.007  1.00 45.07  ? 738 HOH   A O   1 
HETATM 5208 O O   . HOH   I 7 .   ? 12.063  41.232 69.762  1.00 40.43  ? 739 HOH   A O   1 
HETATM 5209 O O   . HOH   I 7 .   ? 22.257  39.017 47.292  1.00 47.43  ? 740 HOH   A O   1 
HETATM 5210 O O   . HOH   I 7 .   ? -5.413  18.123 54.645  1.00 44.59  ? 741 HOH   A O   1 
HETATM 5211 O O   . HOH   I 7 .   ? 24.425  40.052 48.210  1.00 50.59  ? 742 HOH   A O   1 
HETATM 5212 O O   . HOH   I 7 .   ? 2.712   53.634 45.236  1.00 58.23  ? 743 HOH   A O   1 
HETATM 5213 O O   . HOH   I 7 .   ? 8.720   60.511 36.957  1.00 54.40  ? 744 HOH   A O   1 
HETATM 5214 O O   . HOH   I 7 .   ? 24.293  35.749 50.778  1.00 46.86  ? 745 HOH   A O   1 
HETATM 5215 O O   . HOH   I 7 .   ? 34.461  37.468 62.411  1.00 36.81  ? 746 HOH   A O   1 
HETATM 5216 O O   . HOH   I 7 .   ? 1.707   48.400 74.002  1.00 46.32  ? 747 HOH   A O   1 
HETATM 5217 O O   . HOH   J 7 .   ? 10.746  74.467 86.316  1.00 50.62  ? 401 HOH   B O   1 
HETATM 5218 O O   . HOH   J 7 .   ? -20.766 81.593 88.175  1.00 53.88  ? 402 HOH   B O   1 
HETATM 5219 O O   . HOH   J 7 .   ? 1.401   58.621 79.989  1.00 46.79  ? 403 HOH   B O   1 
HETATM 5220 O O   . HOH   J 7 .   ? 11.021  68.918 71.627  1.00 50.60  ? 404 HOH   B O   1 
HETATM 5221 O O   . HOH   J 7 .   ? -25.262 69.365 82.714  1.00 45.40  ? 405 HOH   B O   1 
HETATM 5222 O O   . HOH   J 7 .   ? 0.311   60.532 77.218  1.00 31.99  ? 406 HOH   B O   1 
HETATM 5223 O O   . HOH   J 7 .   ? -14.188 79.389 65.700  1.00 55.61  ? 407 HOH   B O   1 
HETATM 5224 O O   . HOH   J 7 .   ? 4.633   65.941 76.196  1.00 21.76  ? 408 HOH   B O   1 
HETATM 5225 O O   . HOH   J 7 .   ? -21.085 76.950 94.298  1.00 41.53  ? 409 HOH   B O   1 
HETATM 5226 O O   . HOH   J 7 .   ? -7.710  64.888 95.126  1.00 27.20  ? 410 HOH   B O   1 
HETATM 5227 O O   . HOH   J 7 .   ? -5.864  51.715 90.907  1.00 54.25  ? 411 HOH   B O   1 
HETATM 5228 O O   . HOH   J 7 .   ? 0.263   69.004 89.289  1.00 44.39  ? 412 HOH   B O   1 
HETATM 5229 O O   . HOH   J 7 .   ? -24.572 68.264 92.598  1.00 41.59  ? 413 HOH   B O   1 
HETATM 5230 O O   . HOH   J 7 .   ? -22.584 79.407 88.140  1.00 59.12  ? 414 HOH   B O   1 
HETATM 5231 O O   . HOH   J 7 .   ? 2.538   78.079 90.780  1.00 35.10  ? 415 HOH   B O   1 
HETATM 5232 O O   . HOH   J 7 .   ? -25.234 71.431 84.444  1.00 35.04  ? 416 HOH   B O   1 
HETATM 5233 O O   . HOH   J 7 .   ? -1.288  52.920 102.203 1.00 34.00  ? 417 HOH   B O   1 
HETATM 5234 O O   . HOH   J 7 .   ? -0.894  70.357 105.986 1.00 33.57  ? 418 HOH   B O   1 
HETATM 5235 O O   . HOH   J 7 .   ? -10.760 90.396 74.571  1.00 38.31  ? 419 HOH   B O   1 
HETATM 5236 O O   . HOH   J 7 .   ? 10.840  72.429 79.702  1.00 31.71  ? 420 HOH   B O   1 
HETATM 5237 O O   . HOH   J 7 .   ? -19.695 77.989 80.332  1.00 52.10  ? 421 HOH   B O   1 
HETATM 5238 O O   . HOH   J 7 .   ? -28.416 72.646 76.444  1.00 50.70  ? 422 HOH   B O   1 
HETATM 5239 O O   . HOH   J 7 .   ? -5.074  81.371 82.859  1.00 34.64  ? 423 HOH   B O   1 
HETATM 5240 O O   . HOH   J 7 .   ? -7.958  62.465 96.406  1.00 31.79  ? 424 HOH   B O   1 
HETATM 5241 O O   . HOH   J 7 .   ? 15.746  59.748 79.341  1.00 49.96  ? 425 HOH   B O   1 
HETATM 5242 O O   . HOH   J 7 .   ? 17.133  60.904 104.315 1.00 42.27  ? 426 HOH   B O   1 
HETATM 5243 O O   . HOH   J 7 .   ? -22.515 58.864 68.609  1.00 38.84  ? 427 HOH   B O   1 
HETATM 5244 O O   . HOH   J 7 .   ? -17.643 55.618 73.104  1.00 42.35  ? 428 HOH   B O   1 
HETATM 5245 O O   . HOH   J 7 .   ? -20.698 55.674 83.910  1.00 60.06  ? 429 HOH   B O   1 
HETATM 5246 O O   . HOH   J 7 .   ? -10.051 79.672 101.639 1.00 37.87  ? 430 HOH   B O   1 
HETATM 5247 O O   . HOH   J 7 .   ? 1.270   65.967 89.710  1.00 42.22  ? 431 HOH   B O   1 
HETATM 5248 O O   . HOH   J 7 .   ? -8.316  65.125 87.183  1.00 37.45  ? 432 HOH   B O   1 
HETATM 5249 O O   . HOH   J 7 .   ? -19.729 71.233 101.508 1.00 41.46  ? 433 HOH   B O   1 
HETATM 5250 O O   . HOH   J 7 .   ? -24.322 77.169 71.050  1.00 43.75  ? 434 HOH   B O   1 
HETATM 5251 O O   . HOH   J 7 .   ? 20.725  69.871 97.047  1.00 39.87  ? 435 HOH   B O   1 
HETATM 5252 O O   . HOH   J 7 .   ? -13.968 67.810 99.547  1.00 47.25  ? 436 HOH   B O   1 
HETATM 5253 O O   . HOH   J 7 .   ? -14.229 54.920 77.099  1.00 35.24  ? 437 HOH   B O   1 
HETATM 5254 O O   . HOH   J 7 .   ? 7.169   86.375 87.553  1.00 56.30  ? 438 HOH   B O   1 
HETATM 5255 O O   . HOH   J 7 .   ? -3.778  72.361 110.630 1.00 50.98  ? 439 HOH   B O   1 
HETATM 5256 O O   . HOH   J 7 .   ? 3.161   51.373 77.508  1.00 37.07  ? 440 HOH   B O   1 
HETATM 5257 O O   . HOH   J 7 .   ? -23.166 68.083 66.363  1.00 46.71  ? 441 HOH   B O   1 
HETATM 5258 O O   . HOH   J 7 .   ? -11.870 61.422 65.833  1.00 30.77  ? 442 HOH   B O   1 
HETATM 5259 O O   . HOH   J 7 .   ? 15.831  74.847 93.707  1.00 59.19  ? 443 HOH   B O   1 
HETATM 5260 O O   . HOH   J 7 .   ? -5.450  54.700 96.387  1.00 51.09  ? 444 HOH   B O   1 
HETATM 5261 O O   . HOH   J 7 .   ? 5.704   75.618 75.589  1.00 35.36  ? 445 HOH   B O   1 
HETATM 5262 O O   . HOH   J 7 .   ? 12.716  74.918 82.799  1.00 43.11  ? 446 HOH   B O   1 
HETATM 5263 O O   . HOH   J 7 .   ? -6.279  72.046 86.322  1.00 36.26  ? 447 HOH   B O   1 
HETATM 5264 O O   . HOH   J 7 .   ? 1.214   82.396 75.520  1.00 49.59  ? 448 HOH   B O   1 
HETATM 5265 O O   . HOH   J 7 .   ? -7.059  90.630 91.772  1.00 51.82  ? 449 HOH   B O   1 
HETATM 5266 O O   . HOH   J 7 .   ? 14.878  48.700 100.248 1.00 54.36  ? 450 HOH   B O   1 
HETATM 5267 O O   . HOH   J 7 .   ? 0.367   88.788 91.467  1.00 35.27  ? 451 HOH   B O   1 
HETATM 5268 O O   . HOH   J 7 .   ? -20.658 55.900 80.384  1.00 42.69  ? 452 HOH   B O   1 
HETATM 5269 O O   . HOH   J 7 .   ? -23.035 61.063 86.559  1.00 30.91  ? 453 HOH   B O   1 
HETATM 5270 O O   . HOH   J 7 .   ? -11.481 64.146 65.768  1.00 40.86  ? 454 HOH   B O   1 
HETATM 5271 O O   . HOH   J 7 .   ? 5.550   60.932 111.809 1.00 52.23  ? 455 HOH   B O   1 
HETATM 5272 O O   . HOH   J 7 .   ? 6.950   82.870 93.484  1.00 56.24  ? 456 HOH   B O   1 
HETATM 5273 O O   . HOH   J 7 .   ? 17.860  51.350 103.404 1.00 51.00  ? 457 HOH   B O   1 
HETATM 5274 O O   . HOH   J 7 .   ? 8.368   58.262 110.060 1.00 59.47  ? 458 HOH   B O   1 
HETATM 5275 O O   . HOH   J 7 .   ? 19.361  66.981 81.258  1.00 55.09  ? 459 HOH   B O   1 
HETATM 5276 O O   . HOH   J 7 .   ? -5.689  63.038 88.302  1.00 34.35  ? 460 HOH   B O   1 
HETATM 5277 O O   . HOH   J 7 .   ? -24.178 76.791 84.038  1.00 53.86  ? 461 HOH   B O   1 
HETATM 5278 O O   . HOH   J 7 .   ? -30.620 74.616 81.065  1.00 48.49  ? 462 HOH   B O   1 
HETATM 5279 O O   . HOH   J 7 .   ? -28.321 71.702 86.519  1.00 48.00  ? 463 HOH   B O   1 
HETATM 5280 O O   . HOH   J 7 .   ? -5.363  79.654 105.508 1.00 56.96  ? 464 HOH   B O   1 
HETATM 5281 O O   . HOH   J 7 .   ? -19.384 58.829 67.147  1.00 45.97  ? 465 HOH   B O   1 
HETATM 5282 O O   . HOH   J 7 .   ? 2.516   56.963 84.986  1.00 54.11  ? 466 HOH   B O   1 
HETATM 5283 O O   . HOH   J 7 .   ? 12.740  70.874 87.865  1.00 49.20  ? 467 HOH   B O   1 
HETATM 5284 O O   . HOH   J 7 .   ? -24.463 76.463 105.088 1.00 57.62  ? 468 HOH   B O   1 
HETATM 5285 O O   . HOH   J 7 .   ? 2.442   76.441 69.143  1.00 42.14  ? 469 HOH   B O   1 
HETATM 5286 O O   . HOH   J 7 .   ? 8.246   44.193 88.081  1.00 41.57  ? 470 HOH   B O   1 
HETATM 5287 O O   . HOH   J 7 .   ? 12.140  48.484 85.424  1.00 55.24  ? 471 HOH   B O   1 
HETATM 5288 O O   . HOH   J 7 .   ? -6.539  52.987 86.742  1.00 44.09  ? 472 HOH   B O   1 
HETATM 5289 O O   . HOH   J 7 .   ? 12.879  55.515 89.004  1.00 28.66  ? 473 HOH   B O   1 
HETATM 5290 O O   . HOH   J 7 .   ? 4.256   46.065 102.938 1.00 64.65  ? 474 HOH   B O   1 
HETATM 5291 O O   . HOH   J 7 .   ? -1.920  81.486 91.495  1.00 48.96  ? 475 HOH   B O   1 
HETATM 5292 O O   . HOH   J 7 .   ? -24.119 75.301 67.445  1.00 57.39  ? 476 HOH   B O   1 
HETATM 5293 O O   . HOH   J 7 .   ? -0.415  84.718 75.635  1.00 52.58  ? 477 HOH   B O   1 
HETATM 5294 O O   . HOH   J 7 .   ? 17.609  53.287 97.776  1.00 57.98  ? 478 HOH   B O   1 
HETATM 5295 O O   . HOH   J 7 .   ? 13.871  59.533 84.979  1.00 57.40  ? 479 HOH   B O   1 
HETATM 5296 O O   . HOH   J 7 .   ? 10.513  60.745 85.447  1.00 44.86  ? 480 HOH   B O   1 
HETATM 5297 O O   . HOH   J 7 .   ? -23.159 77.613 68.038  1.00 47.09  ? 481 HOH   B O   1 
HETATM 5298 O O   . HOH   J 7 .   ? -7.518  88.273 80.307  1.00 50.69  ? 482 HOH   B O   1 
HETATM 5299 O O   . HOH   J 7 .   ? 18.811  56.539 92.261  1.00 50.51  ? 483 HOH   B O   1 
HETATM 5300 O O   . HOH   J 7 .   ? -5.114  55.972 101.075 1.00 49.11  ? 484 HOH   B O   1 
HETATM 5301 O O   . HOH   J 7 .   ? -4.680  77.858 103.368 1.00 34.95  ? 485 HOH   B O   1 
HETATM 5302 O O   . HOH   J 7 .   ? -2.346  46.833 99.436  1.00 46.62  ? 486 HOH   B O   1 
HETATM 5303 O O   . HOH   J 7 .   ? -7.787  60.108 95.819  1.00 40.42  ? 487 HOH   B O   1 
HETATM 5304 O O   . HOH   J 7 .   ? -13.409 53.017 70.670  1.00 45.51  ? 488 HOH   B O   1 
HETATM 5305 O O   . HOH   J 7 .   ? 10.447  75.604 78.455  1.00 50.01  ? 489 HOH   B O   1 
HETATM 5306 O O   . HOH   J 7 .   ? 17.216  65.218 72.254  1.00 61.84  ? 490 HOH   B O   1 
HETATM 5307 O O   . HOH   J 7 .   ? 1.352   72.809 66.150  1.00 42.51  ? 491 HOH   B O   1 
HETATM 5308 O O   . HOH   J 7 .   ? -24.075 62.434 66.761  1.00 47.02  ? 492 HOH   B O   1 
HETATM 5309 O O   . HOH   J 7 .   ? -12.522 54.196 75.416  1.00 56.00  ? 493 HOH   B O   1 
HETATM 5310 O O   . HOH   J 7 .   ? -19.087 82.782 98.570  1.00 48.70  ? 494 HOH   B O   1 
HETATM 5311 O O   . HOH   J 7 .   ? -17.961 75.367 65.884  1.00 42.11  ? 495 HOH   B O   1 
HETATM 5312 O O   . HOH   J 7 .   ? 14.223  57.828 82.658  1.00 50.61  ? 496 HOH   B O   1 
HETATM 5313 O O   . HOH   J 7 .   ? -4.914  85.726 97.391  1.00 41.01  ? 497 HOH   B O   1 
HETATM 5314 O O   . HOH   J 7 .   ? -0.499  75.329 93.484  1.00 49.96  ? 498 HOH   B O   1 
HETATM 5315 O O   . HOH   J 7 .   ? -18.360 78.810 82.619  1.00 36.38  ? 499 HOH   B O   1 
HETATM 5316 O O   . HOH   J 7 .   ? -16.165 89.149 84.880  1.00 47.03  ? 500 HOH   B O   1 
HETATM 5317 O O   . HOH   J 7 .   ? -10.480 56.240 87.700  1.00 51.95  ? 501 HOH   B O   1 
HETATM 5318 O O   . HOH   J 7 .   ? -4.244  89.316 92.765  1.00 58.14  ? 502 HOH   B O   1 
HETATM 5319 O O   . HOH   J 7 .   ? 14.668  71.448 81.179  1.00 55.27  ? 503 HOH   B O   1 
HETATM 5320 O O   . HOH   J 7 .   ? 14.769  51.927 92.680  1.00 49.07  ? 504 HOH   B O   1 
HETATM 5321 O O   . HOH   J 7 .   ? 4.125   79.484 80.063  1.00 31.59  ? 505 HOH   B O   1 
HETATM 5322 O O   . HOH   J 7 .   ? 10.199  76.384 91.295  1.00 59.59  ? 506 HOH   B O   1 
HETATM 5323 O O   . HOH   J 7 .   ? -2.251  77.546 102.158 1.00 60.93  ? 507 HOH   B O   1 
HETATM 5324 O O   . HOH   J 7 .   ? 3.053   75.290 93.057  1.00 39.27  ? 508 HOH   B O   1 
HETATM 5325 O O   . HOH   J 7 .   ? 2.027   43.331 104.406 1.00 52.40  ? 509 HOH   B O   1 
HETATM 5326 O O   . HOH   J 7 .   ? -18.764 80.969 78.014  1.00 44.73  ? 510 HOH   B O   1 
HETATM 5327 O O   . HOH   J 7 .   ? -1.386  80.924 96.501  1.00 46.09  ? 511 HOH   B O   1 
HETATM 5328 O O   . HOH   J 7 .   ? 1.496   56.217 76.173  1.00 51.36  ? 512 HOH   B O   1 
HETATM 5329 O O   . HOH   J 7 .   ? -18.286 96.159 67.689  1.00 52.95  ? 513 HOH   B O   1 
HETATM 5330 O O   . HOH   J 7 .   ? 16.679  58.689 91.212  1.00 29.59  ? 514 HOH   B O   1 
HETATM 5331 O O   . HOH   J 7 .   ? -2.501  83.531 97.521  1.00 59.39  ? 515 HOH   B O   1 
HETATM 5332 O O   . HOH   J 7 .   ? 14.706  70.202 85.245  1.00 40.09  ? 516 HOH   B O   1 
HETATM 5333 O O   . HOH   J 7 .   ? -22.529 75.242 82.183  1.00 49.94  ? 517 HOH   B O   1 
HETATM 5334 O O   . HOH   J 7 .   ? 7.992   50.973 110.086 1.00 45.36  ? 518 HOH   B O   1 
HETATM 5335 O O   . HOH   J 7 .   ? -23.561 64.361 68.974  1.00 39.37  ? 519 HOH   B O   1 
HETATM 5336 O O   . HOH   J 7 .   ? 5.063   50.835 111.477 1.00 52.95  ? 520 HOH   B O   1 
HETATM 5337 O O   . HOH   J 7 .   ? -6.138  84.706 75.201  1.00 53.82  ? 521 HOH   B O   1 
HETATM 5338 O O   . HOH   J 7 .   ? 16.051  55.404 90.980  1.00 57.54  ? 522 HOH   B O   1 
HETATM 5339 O O   . HOH   J 7 .   ? -21.311 86.218 83.607  1.00 63.54  ? 523 HOH   B O   1 
HETATM 5340 O O   . HOH   J 7 .   ? 24.541  49.468 102.527 1.00 54.02  ? 524 HOH   B O   1 
HETATM 5341 O O   . HOH   J 7 .   ? 13.967  52.526 90.130  1.00 55.18  ? 525 HOH   B O   1 
HETATM 5342 O O   . HOH   J 7 .   ? 3.453   90.224 92.072  1.00 65.07  ? 526 HOH   B O   1 
HETATM 5343 O O   . HOH   J 7 .   ? 20.326  64.461 83.398  1.00 49.66  ? 527 HOH   B O   1 
HETATM 5344 O O   . HOH   J 7 .   ? 0.970   49.472 76.946  1.00 64.72  ? 528 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 
1    N N   . MET A 12  ? 0.7950 0.6121 0.8852 -0.0229 -0.0315 0.0228  1   MET A N   
2    C CA  . MET A 12  ? 0.8068 0.6206 0.8795 -0.0255 -0.0320 0.0241  1   MET A CA  
3    C C   . MET A 12  ? 0.8021 0.6080 0.8552 -0.0250 -0.0256 0.0306  1   MET A C   
4    O O   . MET A 12  ? 0.8064 0.6142 0.8564 -0.0197 -0.0233 0.0332  1   MET A O   
5    C CB  . MET A 12  ? 0.8241 0.6519 0.8999 -0.0230 -0.0401 0.0171  1   MET A CB  
6    C CG  . MET A 12  ? 0.8862 0.7124 0.9586 -0.0276 -0.0420 0.0150  1   MET A CG  
7    S SD  . MET A 12  ? 1.0473 0.8874 1.1337 -0.0260 -0.0505 0.0068  1   MET A SD  
8    C CE  . MET A 12  ? 1.0215 0.8582 1.1268 -0.0280 -0.0471 0.0042  1   MET A CE  
9    N N   . ASP A 13  ? 0.7900 0.5872 0.8301 -0.0299 -0.0221 0.0325  2   ASP A N   
10   C CA  . ASP A 13  ? 0.7843 0.5729 0.8069 -0.0308 -0.0138 0.0372  2   ASP A CA  
11   C C   . ASP A 13  ? 0.7745 0.5704 0.7905 -0.0253 -0.0135 0.0345  2   ASP A C   
12   O O   . ASP A 13  ? 0.7733 0.5770 0.7936 -0.0249 -0.0190 0.0287  2   ASP A O   
13   C CB  . ASP A 13  ? 0.8019 0.5819 0.8164 -0.0376 -0.0111 0.0366  2   ASP A CB  
14   C CG  . ASP A 13  ? 0.8534 0.6241 0.8521 -0.0401 -0.0007 0.0397  2   ASP A CG  
15   O OD1 . ASP A 13  ? 0.8717 0.6306 0.8618 -0.0408 0.0063  0.0468  2   ASP A OD1 
16   O OD2 . ASP A 13  ? 0.8675 0.6413 0.8626 -0.0417 0.0020  0.0350  2   ASP A OD2 
17   N N   . TYR A 14  ? 0.7667 0.5585 0.7708 -0.0193 -0.0064 0.0390  3   TYR A N   
18   C CA  . TYR A 14  ? 0.7613 0.5551 0.7539 -0.0104 -0.0040 0.0369  3   TYR A CA  
19   C C   . TYR A 14  ? 0.7573 0.5441 0.7402 -0.0146 0.0034  0.0346  3   TYR A C   
20   O O   . TYR A 14  ? 0.7536 0.5440 0.7359 -0.0103 0.0008  0.0299  3   TYR A O   
21   C CB  . TYR A 14  ? 0.7668 0.5550 0.7445 -0.0013 0.0042  0.0427  3   TYR A CB  
22   C CG  . TYR A 14  ? 0.7840 0.5692 0.7437 0.0110  0.0092  0.0409  3   TYR A CG  
23   C CD1 . TYR A 14  ? 0.7915 0.5879 0.7550 0.0227  -0.0015 0.0352  3   TYR A CD1 
24   C CD2 . TYR A 14  ? 0.8089 0.5781 0.7470 0.0115  0.0256  0.0440  3   TYR A CD2 
25   C CE1 . TYR A 14  ? 0.8153 0.6050 0.7582 0.0368  0.0034  0.0337  3   TYR A CE1 
26   C CE2 . TYR A 14  ? 0.8311 0.5926 0.7499 0.0246  0.0331  0.0424  3   TYR A CE2 
27   C CZ  . TYR A 14  ? 0.8439 0.6146 0.7634 0.0383  0.0217  0.0378  3   TYR A CZ  
28   O OH  . TYR A 14  ? 0.8826 0.6416 0.7785 0.0541  0.0296  0.0366  3   TYR A OH  
29   N N   . ASP A 15  ? 0.7546 0.5309 0.7311 -0.0231 0.0127  0.0371  4   ASP A N   
30   C CA  . ASP A 15  ? 0.7557 0.5262 0.7272 -0.0284 0.0213  0.0328  4   ASP A CA  
31   C C   . ASP A 15  ? 0.7304 0.5111 0.7169 -0.0327 0.0112  0.0252  4   ASP A C   
32   O O   . ASP A 15  ? 0.7254 0.5052 0.7109 -0.0319 0.0155  0.0206  4   ASP A O   
33   C CB  . ASP A 15  ? 0.7880 0.5472 0.7527 -0.0372 0.0319  0.0350  4   ASP A CB  
34   C CG  . ASP A 15  ? 0.8652 0.6119 0.8116 -0.0328 0.0450  0.0434  4   ASP A CG  
35   O OD1 . ASP A 15  ? 0.8741 0.6217 0.8126 -0.0216 0.0456  0.0470  4   ASP A OD1 
36   O OD2 . ASP A 15  ? 0.9085 0.6446 0.8476 -0.0399 0.0546  0.0459  4   ASP A OD2 
37   N N   . PHE A 16  ? 0.7136 0.5023 0.7130 -0.0360 -0.0007 0.0244  5   PHE A N   
38   C CA  . PHE A 16  ? 0.7019 0.5003 0.7138 -0.0389 -0.0106 0.0183  5   PHE A CA  
39   C C   . PHE A 16  ? 0.6850 0.4911 0.7002 -0.0317 -0.0165 0.0165  5   PHE A C   
40   O O   . PHE A 16  ? 0.6870 0.4966 0.7056 -0.0325 -0.0183 0.0120  5   PHE A O   
41   C CB  . PHE A 16  ? 0.7035 0.5036 0.7232 -0.0417 -0.0185 0.0191  5   PHE A CB  
42   C CG  . PHE A 16  ? 0.7130 0.5223 0.7436 -0.0417 -0.0287 0.0146  5   PHE A CG  
43   C CD1 . PHE A 16  ? 0.7231 0.5359 0.7564 -0.0455 -0.0317 0.0089  5   PHE A CD1 
44   C CD2 . PHE A 16  ? 0.7219 0.5361 0.7607 -0.0379 -0.0345 0.0154  5   PHE A CD2 
45   C CE1 . PHE A 16  ? 0.7281 0.5478 0.7683 -0.0444 -0.0398 0.0057  5   PHE A CE1 
46   C CE2 . PHE A 16  ? 0.7279 0.5482 0.7747 -0.0380 -0.0413 0.0116  5   PHE A CE2 
47   C CZ  . PHE A 16  ? 0.7235 0.5456 0.7691 -0.0408 -0.0436 0.0076  5   PHE A CZ  
48   N N   . LYS A 17  ? 0.6678 0.4761 0.6818 -0.0241 -0.0193 0.0195  6   LYS A N   
49   C CA  . LYS A 17  ? 0.6601 0.4755 0.6760 -0.0156 -0.0261 0.0167  6   LYS A CA  
50   C C   . LYS A 17  ? 0.6627 0.4702 0.6640 -0.0086 -0.0187 0.0159  6   LYS A C   
51   O O   . LYS A 17  ? 0.6672 0.4772 0.6708 -0.0066 -0.0230 0.0124  6   LYS A O   
52   C CB  . LYS A 17  ? 0.6812 0.5026 0.7015 -0.0084 -0.0313 0.0178  6   LYS A CB  
53   C CG  . LYS A 17  ? 0.7318 0.5635 0.7579 0.0000  -0.0416 0.0124  6   LYS A CG  
54   C CD  . LYS A 17  ? 0.7930 0.6319 0.8226 0.0098  -0.0463 0.0110  6   LYS A CD  
55   C CE  . LYS A 17  ? 0.8432 0.6886 0.8688 0.0229  -0.0546 0.0051  6   LYS A CE  
56   N NZ  . LYS A 17  ? 0.8787 0.7102 0.8781 0.0331  -0.0466 0.0075  6   LYS A NZ  
57   N N   . VAL A 18  ? 0.6640 0.4593 0.6488 -0.0043 -0.0058 0.0194  7   VAL A N   
58   C CA  . VAL A 18  ? 0.6723 0.4546 0.6401 0.0040  0.0054  0.0187  7   VAL A CA  
59   C C   . VAL A 18  ? 0.6634 0.4408 0.6361 -0.0045 0.0122  0.0148  7   VAL A C   
60   O O   . VAL A 18  ? 0.6631 0.4333 0.6299 0.0017  0.0159  0.0126  7   VAL A O   
61   C CB  . VAL A 18  ? 0.6973 0.4647 0.6430 0.0122  0.0210  0.0234  7   VAL A CB  
62   C CG1 . VAL A 18  ? 0.7056 0.4774 0.6429 0.0268  0.0142  0.0255  7   VAL A CG1 
63   C CG2 . VAL A 18  ? 0.7060 0.4687 0.6523 0.0007  0.0305  0.0266  7   VAL A CG2 
64   N N   . LYS A 19  ? 0.6566 0.4374 0.6404 -0.0177 0.0136  0.0131  8   LYS A N   
65   C CA  . LYS A 19  ? 0.6617 0.4415 0.6546 -0.0263 0.0187  0.0071  8   LYS A CA  
66   C C   . LYS A 19  ? 0.6687 0.4592 0.6736 -0.0266 0.0060  0.0039  8   LYS A C   
67   O O   . LYS A 19  ? 0.6787 0.4637 0.6841 -0.0254 0.0117  0.0007  8   LYS A O   
68   C CB  . LYS A 19  ? 0.6718 0.4547 0.6733 -0.0385 0.0204  0.0045  8   LYS A CB  
69   C CG  . LYS A 19  ? 0.6970 0.4907 0.7161 -0.0475 0.0131  -0.0032 8   LYS A CG  
70   C CD  . LYS A 19  ? 0.7475 0.5370 0.7723 -0.0557 0.0253  -0.0108 8   LYS A CD  
71   C CE  . LYS A 19  ? 0.7953 0.5847 0.8297 -0.0564 0.0306  -0.0176 8   LYS A CE  
72   N NZ  . LYS A 19  ? 0.8177 0.6200 0.8616 -0.0548 0.0147  -0.0182 8   LYS A NZ  
73   N N   . LEU A 20  ? 0.6622 0.4654 0.6758 -0.0275 -0.0091 0.0050  9   LEU A N   
74   C CA  . LEU A 20  ? 0.6651 0.4774 0.6881 -0.0275 -0.0198 0.0025  9   LEU A CA  
75   C C   . LEU A 20  ? 0.6890 0.4960 0.7031 -0.0169 -0.0200 0.0036  9   LEU A C   
76   O O   . LEU A 20  ? 0.6929 0.4992 0.7097 -0.0168 -0.0210 0.0016  9   LEU A O   
77   C CB  . LEU A 20  ? 0.6499 0.4737 0.6822 -0.0297 -0.0324 0.0032  9   LEU A CB  
78   C CG  . LEU A 20  ? 0.6506 0.4780 0.6897 -0.0377 -0.0343 0.0016  9   LEU A CG  
79   C CD1 . LEU A 20  ? 0.6550 0.4880 0.6999 -0.0371 -0.0428 0.0029  9   LEU A CD1 
80   C CD2 . LEU A 20  ? 0.6457 0.4773 0.6915 -0.0428 -0.0347 -0.0040 9   LEU A CD2 
81   N N   . SER A 21  ? 0.7024 0.5050 0.7049 -0.0069 -0.0194 0.0065  10  SER A N   
82   C CA  . SER A 21  ? 0.7237 0.5195 0.7138 0.0066  -0.0205 0.0068  10  SER A CA  
83   C C   . SER A 21  ? 0.7489 0.5259 0.7262 0.0109  -0.0056 0.0066  10  SER A C   
84   O O   . SER A 21  ? 0.7578 0.5284 0.7300 0.0177  -0.0071 0.0060  10  SER A O   
85   C CB  . SER A 21  ? 0.7432 0.5379 0.7221 0.0179  -0.0216 0.0087  10  SER A CB  
86   O OG  . SER A 21  ? 0.7750 0.5716 0.7481 0.0309  -0.0312 0.0065  10  SER A OG  
87   N N   . SER A 22  ? 0.7570 0.5235 0.7297 0.0068  0.0101  0.0068  11  SER A N   
88   C CA  . SER A 22  ? 0.7791 0.5257 0.7423 0.0099  0.0282  0.0054  11  SER A CA  
89   C C   . SER A 22  ? 0.7905 0.5412 0.7714 -0.0003 0.0278  0.0009  11  SER A C   
90   O O   . SER A 22  ? 0.8075 0.5427 0.7824 0.0052  0.0376  0.0001  11  SER A O   
91   C CB  . SER A 22  ? 0.7991 0.5343 0.7552 0.0066  0.0466  0.0054  11  SER A CB  
92   O OG  . SER A 22  ? 0.8364 0.5498 0.7842 0.0100  0.0675  0.0030  11  SER A OG  
93   N N   . GLU A 23  ? 0.7809 0.5505 0.7820 -0.0137 0.0175  -0.0020 12  GLU A N   
94   C CA  . GLU A 23  ? 0.7871 0.5635 0.8054 -0.0223 0.0155  -0.0070 12  GLU A CA  
95   C C   . GLU A 23  ? 0.7929 0.5739 0.8115 -0.0174 0.0031  -0.0046 12  GLU A C   
96   O O   . GLU A 23  ? 0.7991 0.5761 0.8234 -0.0186 0.0065  -0.0065 12  GLU A O   
97   C CB  . GLU A 23  ? 0.8183 0.6125 0.8538 -0.0349 0.0076  -0.0114 12  GLU A CB  
98   C CG  . GLU A 23  ? 0.9152 0.7053 0.9517 -0.0410 0.0192  -0.0147 12  GLU A CG  
99   C CD  . GLU A 23  ? 1.0589 0.8411 1.1050 -0.0468 0.0357  -0.0228 12  GLU A CD  
100  O OE1 . GLU A 23  ? 1.0867 0.8712 1.1446 -0.0485 0.0356  -0.0271 12  GLU A OE1 
101  O OE2 . GLU A 23  ? 1.1077 0.8812 1.1508 -0.0501 0.0499  -0.0253 12  GLU A OE2 
102  N N   . ARG A 24  ? 0.7861 0.5756 0.8002 -0.0125 -0.0106 -0.0011 13  ARG A N   
103  C CA  . ARG A 24  ? 0.7814 0.5772 0.7964 -0.0088 -0.0233 0.0004  13  ARG A CA  
104  C C   . ARG A 24  ? 0.8047 0.5845 0.8086 0.0003  -0.0183 0.0020  13  ARG A C   
105  O O   . ARG A 24  ? 0.8192 0.5842 0.8051 0.0133  -0.0137 0.0041  13  ARG A O   
106  C CB  . ARG A 24  ? 0.7756 0.5799 0.7875 -0.0034 -0.0347 0.0020  13  ARG A CB  
107  C CG  . ARG A 24  ? 0.7681 0.5849 0.7884 -0.0049 -0.0484 0.0014  13  ARG A CG  
108  C CD  . ARG A 24  ? 0.7564 0.5878 0.7881 -0.0104 -0.0564 0.0002  13  ARG A CD  
109  N NE  . ARG A 24  ? 0.7681 0.5993 0.7957 -0.0047 -0.0565 0.0005  13  ARG A NE  
110  C CZ  . ARG A 24  ? 0.7765 0.6130 0.8108 -0.0096 -0.0563 0.0008  13  ARG A CZ  
111  N NH1 . ARG A 24  ? 0.7594 0.6007 0.8029 -0.0192 -0.0564 0.0006  13  ARG A NH1 
112  N NH2 . ARG A 24  ? 0.7730 0.6090 0.8034 -0.0036 -0.0559 0.0015  13  ARG A NH2 
113  N N   . GLU A 25  ? 0.8071 0.5890 0.8203 -0.0050 -0.0192 0.0013  14  GLU A N   
114  C CA  . GLU A 25  ? 0.8232 0.5887 0.8270 0.0027  -0.0146 0.0037  14  GLU A CA  
115  C C   . GLU A 25  ? 0.8223 0.5892 0.8155 0.0119  -0.0278 0.0067  14  GLU A C   
116  O O   . GLU A 25  ? 0.8132 0.5981 0.8164 0.0061  -0.0407 0.0061  14  GLU A O   
117  C CB  . GLU A 25  ? 0.8533 0.6251 0.8726 -0.0067 -0.0147 0.0023  14  GLU A CB  
118  C CG  . GLU A 25  ? 0.9247 0.6994 0.9602 -0.0167 -0.0038 -0.0035 14  GLU A CG  
119  C CD  . GLU A 25  ? 1.0249 0.8111 1.0778 -0.0249 -0.0071 -0.0064 14  GLU A CD  
120  O OE1 . GLU A 25  ? 1.0422 0.8362 1.0936 -0.0242 -0.0185 -0.0027 14  GLU A OE1 
121  O OE2 . GLU A 25  ? 1.0578 0.8459 1.1265 -0.0320 0.0021  -0.0131 14  GLU A OE2 
122  N N   . ARG A 26  ? 0.8295 0.5761 0.8022 0.0269  -0.0237 0.0089  15  ARG A N   
123  C CA  . ARG A 26  ? 0.8365 0.5837 0.7986 0.0372  -0.0367 0.0098  15  ARG A CA  
124  C C   . ARG A 26  ? 0.8379 0.5725 0.7939 0.0404  -0.0367 0.0131  15  ARG A C   
125  O O   . ARG A 26  ? 0.8464 0.5592 0.7944 0.0442  -0.0224 0.0157  15  ARG A O   
126  C CB  . ARG A 26  ? 0.8767 0.6102 0.8170 0.0548  -0.0349 0.0092  15  ARG A CB  
127  C CG  . ARG A 26  ? 0.9301 0.6835 0.8786 0.0526  -0.0436 0.0058  15  ARG A CG  
128  C CD  . ARG A 26  ? 1.0067 0.7471 0.9358 0.0669  -0.0358 0.0056  15  ARG A CD  
129  N NE  . ARG A 26  ? 1.0804 0.8016 0.9833 0.0887  -0.0372 0.0055  15  ARG A NE  
130  C CZ  . ARG A 26  ? 1.1360 0.8390 1.0138 0.1068  -0.0285 0.0058  15  ARG A CZ  
131  N NH1 . ARG A 26  ? 1.1519 0.8359 1.0033 0.1290  -0.0310 0.0051  15  ARG A NH1 
132  N NH2 . ARG A 26  ? 1.1348 0.8366 1.0113 0.1040  -0.0166 0.0068  15  ARG A NH2 
133  N N   . VAL A 27  ? 0.8276 0.5747 0.7881 0.0383  -0.0509 0.0131  16  VAL A N   
134  C CA  . VAL A 27  ? 0.8335 0.5695 0.7876 0.0405  -0.0518 0.0172  16  VAL A CA  
135  C C   . VAL A 27  ? 0.8568 0.5619 0.7838 0.0596  -0.0458 0.0200  16  VAL A C   
136  O O   . VAL A 27  ? 0.8701 0.5536 0.7895 0.0621  -0.0346 0.0248  16  VAL A O   
137  C CB  . VAL A 27  ? 0.8297 0.5843 0.7924 0.0347  -0.0666 0.0160  16  VAL A CB  
138  C CG1 . VAL A 27  ? 0.8374 0.5966 0.7928 0.0453  -0.0793 0.0111  16  VAL A CG1 
139  C CG2 . VAL A 27  ? 0.8355 0.5798 0.7936 0.0332  -0.0650 0.0217  16  VAL A CG2 
140  N N   . GLU A 28  ? 0.8610 0.5624 0.7727 0.0743  -0.0519 0.0167  17  GLU A N   
141  C CA  . GLU A 28  ? 0.8860 0.5568 0.7670 0.0967  -0.0477 0.0184  17  GLU A CA  
142  C C   . GLU A 28  ? 0.9085 0.5502 0.7738 0.1053  -0.0257 0.0214  17  GLU A C   
143  O O   . GLU A 28  ? 0.9374 0.5465 0.7744 0.1247  -0.0174 0.0242  17  GLU A O   
144  C CB  . GLU A 28  ? 0.9056 0.5844 0.7757 0.1114  -0.0634 0.0120  17  GLU A CB  
145  C CG  . GLU A 28  ? 0.9409 0.6280 0.8111 0.1153  -0.0612 0.0079  17  GLU A CG  
146  C CD  . GLU A 28  ? 0.9577 0.6784 0.8584 0.0957  -0.0678 0.0044  17  GLU A CD  
147  O OE1 . GLU A 28  ? 0.9413 0.6816 0.8625 0.0815  -0.0772 0.0032  17  GLU A OE1 
148  O OE2 . GLU A 28  ? 0.9814 0.7065 0.8836 0.0957  -0.0623 0.0031  17  GLU A OE2 
149  N N   . ASP A 29  ? 0.8946 0.5458 0.7769 0.0919  -0.0151 0.0203  18  ASP A N   
150  C CA  . ASP A 29  ? 0.9057 0.5306 0.7780 0.0968  0.0087  0.0217  18  ASP A CA  
151  C C   . ASP A 29  ? 0.9004 0.5157 0.7870 0.0851  0.0221  0.0243  18  ASP A C   
152  O O   . ASP A 29  ? 0.9155 0.4990 0.7897 0.0933  0.0432  0.0263  18  ASP A O   
153  C CB  . ASP A 29  ? 0.9167 0.5569 0.8008 0.0880  0.0139  0.0180  18  ASP A CB  
154  C CG  . ASP A 29  ? 0.9807 0.6229 0.8472 0.1025  0.0074  0.0159  18  ASP A CG  
155  O OD1 . ASP A 29  ? 1.0029 0.6265 0.8420 0.1241  0.0042  0.0165  18  ASP A OD1 
156  O OD2 . ASP A 29  ? 1.0017 0.6631 0.8806 0.0936  0.0057  0.0134  18  ASP A OD2 
157  N N   . LEU A 30  ? 0.8797 0.5218 0.7926 0.0668  0.0112  0.0238  19  LEU A N   
158  C CA  . LEU A 30  ? 0.8793 0.5189 0.8099 0.0549  0.0210  0.0249  19  LEU A CA  
159  C C   . LEU A 30  ? 0.8911 0.5114 0.8102 0.0618  0.0207  0.0313  19  LEU A C   
160  O O   . LEU A 30  ? 0.8981 0.5009 0.8228 0.0594  0.0363  0.0332  19  LEU A O   
161  C CB  . LEU A 30  ? 0.8603 0.5370 0.8213 0.0344  0.0098  0.0210  19  LEU A CB  
162  C CG  . LEU A 30  ? 0.8690 0.5561 0.8501 0.0226  0.0203  0.0145  19  LEU A CG  
163  C CD1 . LEU A 30  ? 0.8677 0.5718 0.8492 0.0208  0.0126  0.0114  19  LEU A CD1 
164  C CD2 . LEU A 30  ? 0.8637 0.5729 0.8721 0.0065  0.0164  0.0112  19  LEU A CD2 
165  N N   . PHE A 31  ? 0.8897 0.5123 0.7938 0.0703  0.0041  0.0341  20  PHE A N   
166  C CA  . PHE A 31  ? 0.9012 0.5059 0.7935 0.0760  0.0028  0.0407  20  PHE A CA  
167  C C   . PHE A 31  ? 0.9227 0.5012 0.7808 0.0985  -0.0022 0.0436  20  PHE A C   
168  O O   . PHE A 31  ? 0.9236 0.5097 0.7708 0.1083  -0.0135 0.0391  20  PHE A O   
169  C CB  . PHE A 31  ? 0.8841 0.5191 0.7953 0.0606  -0.0131 0.0414  20  PHE A CB  
170  C CG  . PHE A 31  ? 0.8733 0.5315 0.8144 0.0414  -0.0095 0.0389  20  PHE A CG  
171  C CD1 . PHE A 31  ? 0.8812 0.5300 0.8321 0.0358  0.0019  0.0421  20  PHE A CD1 
172  C CD2 . PHE A 31  ? 0.8670 0.5557 0.8264 0.0303  -0.0174 0.0325  20  PHE A CD2 
173  C CE1 . PHE A 31  ? 0.8733 0.5456 0.8520 0.0201  0.0035  0.0377  20  PHE A CE1 
174  C CE2 . PHE A 31  ? 0.8595 0.5682 0.8435 0.0154  -0.0150 0.0290  20  PHE A CE2 
175  C CZ  . PHE A 31  ? 0.8548 0.5565 0.8487 0.0107  -0.0054 0.0309  20  PHE A CZ  
176  N N   . GLU A 32  ? 0.9389 0.4871 0.7809 0.1072  0.0053  0.0508  21  GLU A N   
177  C CA  . GLU A 32  ? 0.9706 0.4908 0.7785 0.1290  -0.0003 0.0543  21  GLU A CA  
178  C C   . GLU A 32  ? 0.9704 0.5063 0.7841 0.1208  -0.0168 0.0573  21  GLU A C   
179  O O   . GLU A 32  ? 0.9682 0.4998 0.7915 0.1105  -0.0102 0.0638  21  GLU A O   
180  C CB  . GLU A 32  ? 1.0279 0.4979 0.8115 0.1448  0.0223  0.0614  21  GLU A CB  
181  C CG  . GLU A 32  ? 1.1072 0.5435 0.8486 0.1731  0.0175  0.0635  21  GLU A CG  
182  C CD  . GLU A 32  ? 1.1681 0.6035 0.8915 0.1901  0.0145  0.0562  21  GLU A CD  
183  O OE1 . GLU A 32  ? 1.1926 0.6130 0.9136 0.1935  0.0347  0.0551  21  GLU A OE1 
184  O OE2 . GLU A 32  ? 1.1741 0.6252 0.8876 0.1995  -0.0074 0.0507  21  GLU A OE2 
185  N N   . TYR A 33  ? 0.9681 0.5229 0.7776 0.1248  -0.0374 0.0519  22  TYR A N   
186  C CA  . TYR A 33  ? 0.9673 0.5390 0.7836 0.1158  -0.0522 0.0531  22  TYR A CA  
187  C C   . TYR A 33  ? 0.9880 0.5566 0.7840 0.1319  -0.0696 0.0480  22  TYR A C   
188  O O   . TYR A 33  ? 0.9867 0.5635 0.7846 0.1264  -0.0800 0.0489  22  TYR A O   
189  C CB  . TYR A 33  ? 0.9396 0.5554 0.7901 0.0929  -0.0603 0.0480  22  TYR A CB  
190  C CG  . TYR A 33  ? 0.9355 0.5754 0.7963 0.0931  -0.0693 0.0378  22  TYR A CG  
191  C CD1 . TYR A 33  ? 0.9389 0.5966 0.8004 0.0969  -0.0869 0.0297  22  TYR A CD1 
192  C CD2 . TYR A 33  ? 0.9373 0.5831 0.8091 0.0885  -0.0595 0.0356  22  TYR A CD2 
193  C CE1 . TYR A 33  ? 0.9378 0.6170 0.8103 0.0974  -0.0944 0.0205  22  TYR A CE1 
194  C CE2 . TYR A 33  ? 0.9380 0.6044 0.8182 0.0885  -0.0669 0.0276  22  TYR A CE2 
195  C CZ  . TYR A 33  ? 0.9450 0.6281 0.8259 0.0930  -0.0843 0.0203  22  TYR A CZ  
196  O OH  . TYR A 33  ? 0.9556 0.6591 0.8469 0.0932  -0.0910 0.0124  22  TYR A OH  
197  N N   . GLU A 34  ? 1.0050 0.5643 0.7828 0.1514  -0.0735 0.0415  23  GLU A N   
198  C CA  . GLU A 34  ? 1.0223 0.5825 0.7831 0.1682  -0.0925 0.0336  23  GLU A CA  
199  C C   . GLU A 34  ? 1.0402 0.5653 0.7705 0.1837  -0.0933 0.0400  23  GLU A C   
200  O O   . GLU A 34  ? 1.0676 0.5511 0.7712 0.1986  -0.0776 0.0486  23  GLU A O   
201  C CB  . GLU A 34  ? 1.0703 0.6281 0.8166 0.1880  -0.0964 0.0249  23  GLU A CB  
202  C CG  . GLU A 34  ? 1.1271 0.7290 0.9003 0.1788  -0.1135 0.0121  23  GLU A CG  
203  C CD  . GLU A 34  ? 1.2363 0.8363 0.9937 0.2003  -0.1184 0.0035  23  GLU A CD  
204  O OE1 . GLU A 34  ? 1.2609 0.8482 0.9932 0.2242  -0.1308 -0.0029 23  GLU A OE1 
205  O OE2 . GLU A 34  ? 1.2695 0.8800 1.0381 0.1944  -0.1098 0.0031  23  GLU A OE2 
206  N N   . GLY A 35  ? 1.0224 0.5631 0.7574 0.1795  -0.1100 0.0357  24  GLY A N   
207  C CA  . GLY A 35  ? 1.0392 0.5493 0.7468 0.1915  -0.1124 0.0419  24  GLY A CA  
208  C C   . GLY A 35  ? 1.0275 0.5355 0.7466 0.1715  -0.1025 0.0542  24  GLY A C   
209  O O   . GLY A 35  ? 1.0351 0.5329 0.7425 0.1726  -0.1084 0.0577  24  GLY A O   
210  N N   . CYS A 36  ? 1.0044 0.5233 0.7467 0.1532  -0.0877 0.0600  25  CYS A N   
211  C CA  . CYS A 36  ? 0.9911 0.5104 0.7457 0.1351  -0.0777 0.0709  25  CYS A CA  
212  C C   . CYS A 36  ? 0.9637 0.5257 0.7484 0.1120  -0.0872 0.0664  25  CYS A C   
213  O O   . CYS A 36  ? 0.9630 0.5417 0.7700 0.0944  -0.0785 0.0702  25  CYS A O   
214  C CB  . CYS A 36  ? 0.9934 0.4994 0.7563 0.1296  -0.0565 0.0784  25  CYS A CB  
215  S SG  . CYS A 36  ? 1.0362 0.5040 0.7742 0.1538  -0.0424 0.0777  25  CYS A SG  
216  N N   . LYS A 37  ? 0.9397 0.5181 0.7248 0.1125  -0.1038 0.0578  26  LYS A N   
217  C CA  . LYS A 37  ? 0.9062 0.5204 0.7179 0.0916  -0.1091 0.0535  26  LYS A CA  
218  C C   . LYS A 37  ? 0.9059 0.5090 0.7092 0.0841  -0.1044 0.0642  26  LYS A C   
219  O O   . LYS A 37  ? 0.9248 0.5065 0.7053 0.0952  -0.1098 0.0662  26  LYS A O   
220  C CB  . LYS A 37  ? 0.9069 0.5465 0.7295 0.0933  -0.1263 0.0371  26  LYS A CB  
221  C CG  . LYS A 37  ? 0.9230 0.5980 0.7752 0.0720  -0.1277 0.0313  26  LYS A CG  
222  C CD  . LYS A 37  ? 0.9545 0.6518 0.8195 0.0729  -0.1430 0.0143  26  LYS A CD  
223  C CE  . LYS A 37  ? 0.9852 0.6935 0.8568 0.0841  -0.1526 0.0019  26  LYS A CE  
224  N NZ  . LYS A 37  ? 0.9886 0.7263 0.8837 0.0799  -0.1652 -0.0161 26  LYS A NZ  
225  N N   . VAL A 38  ? 0.8847 0.5013 0.7043 0.0666  -0.0945 0.0711  27  VAL A N   
226  C CA  . VAL A 38  ? 0.8834 0.4904 0.6945 0.0594  -0.0884 0.0823  27  VAL A CA  
227  C C   . VAL A 38  ? 0.8691 0.5038 0.6942 0.0448  -0.0928 0.0767  27  VAL A C   
228  O O   . VAL A 38  ? 0.8771 0.5037 0.6920 0.0399  -0.0885 0.0849  27  VAL A O   
229  C CB  . VAL A 38  ? 0.8884 0.4870 0.7040 0.0527  -0.0728 0.0946  27  VAL A CB  
230  C CG1 . VAL A 38  ? 0.9147 0.4794 0.7149 0.0675  -0.0645 0.1004  27  VAL A CG1 
231  C CG2 . VAL A 38  ? 0.8687 0.5006 0.7134 0.0385  -0.0700 0.0890  27  VAL A CG2 
232  N N   . GLY A 39  ? 0.8459 0.5107 0.6935 0.0380  -0.0990 0.0636  28  GLY A N   
233  C CA  . GLY A 39  ? 0.8324 0.5212 0.6948 0.0248  -0.0998 0.0569  28  GLY A CA  
234  C C   . GLY A 39  ? 0.8184 0.5317 0.7011 0.0239  -0.1100 0.0394  28  GLY A C   
235  O O   . GLY A 39  ? 0.8105 0.5308 0.7022 0.0288  -0.1141 0.0336  28  GLY A O   
236  N N   . ARG A 40  ? 0.8142 0.5403 0.7052 0.0171  -0.1127 0.0305  29  ARG A N   
237  C CA  . ARG A 40  ? 0.8079 0.5581 0.7224 0.0147  -0.1210 0.0123  29  ARG A CA  
238  C C   . ARG A 40  ? 0.8024 0.5678 0.7315 0.0002  -0.1131 0.0066  29  ARG A C   
239  O O   . ARG A 40  ? 0.8155 0.5703 0.7318 -0.0024 -0.1092 0.0106  29  ARG A O   
240  C CB  . ARG A 40  ? 0.8313 0.5755 0.7382 0.0297  -0.1373 0.0012  29  ARG A CB  
241  C CG  . ARG A 40  ? 0.8593 0.6299 0.7930 0.0275  -0.1472 -0.0200 29  ARG A CG  
242  C CD  . ARG A 40  ? 0.8944 0.6851 0.8509 0.0245  -0.1471 -0.0265 29  ARG A CD  
243  N NE  . ARG A 40  ? 0.9206 0.7372 0.9077 0.0171  -0.1508 -0.0454 29  ARG A NE  
244  C CZ  . ARG A 40  ? 0.9344 0.7706 0.9465 0.0105  -0.1478 -0.0525 29  ARG A CZ  
245  N NH1 . ARG A 40  ? 0.9336 0.7675 0.9428 0.0101  -0.1420 -0.0424 29  ARG A NH1 
246  N NH2 . ARG A 40  ? 0.9205 0.7778 0.9618 0.0038  -0.1496 -0.0702 29  ARG A NH2 
247  N N   . GLY A 41  ? 0.7829 0.5698 0.7363 -0.0086 -0.1084 -0.0017 30  GLY A N   
248  C CA  . GLY A 41  ? 0.7796 0.5780 0.7468 -0.0213 -0.0972 -0.0079 30  GLY A CA  
249  C C   . GLY A 41  ? 0.7691 0.5881 0.7638 -0.0276 -0.0935 -0.0190 30  GLY A C   
250  O O   . GLY A 41  ? 0.7669 0.5944 0.7728 -0.0221 -0.1033 -0.0253 30  GLY A O   
251  N N   . THR A 42  ? 0.7625 0.5868 0.7656 -0.0382 -0.0778 -0.0207 31  THR A N   
252  C CA  . THR A 42  ? 0.7528 0.5917 0.7799 -0.0441 -0.0703 -0.0303 31  THR A CA  
253  C C   . THR A 42  ? 0.7487 0.5893 0.7741 -0.0411 -0.0710 -0.0221 31  THR A C   
254  O O   . THR A 42  ? 0.7438 0.5956 0.7884 -0.0423 -0.0713 -0.0303 31  THR A O   
255  C CB  . THR A 42  ? 0.7765 0.6128 0.8038 -0.0531 -0.0495 -0.0299 31  THR A CB  
256  O OG1 . THR A 42  ? 0.8128 0.6361 0.8136 -0.0520 -0.0412 -0.0120 31  THR A OG1 
257  C CG2 . THR A 42  ? 0.7767 0.6130 0.8112 -0.0585 -0.0452 -0.0413 31  THR A CG2 
258  N N   . TYR A 43  ? 0.7512 0.5805 0.7549 -0.0378 -0.0699 -0.0064 32  TYR A N   
259  C CA  . TYR A 43  ? 0.7459 0.5758 0.7467 -0.0350 -0.0708 0.0014  32  TYR A CA  
260  C C   . TYR A 43  ? 0.7543 0.5862 0.7601 -0.0275 -0.0849 -0.0020 32  TYR A C   
261  O O   . TYR A 43  ? 0.7606 0.5957 0.7697 -0.0262 -0.0853 0.0005  32  TYR A O   
262  C CB  . TYR A 43  ? 0.7443 0.5619 0.7233 -0.0335 -0.0659 0.0169  32  TYR A CB  
263  C CG  . TYR A 43  ? 0.7436 0.5463 0.7059 -0.0285 -0.0719 0.0234  32  TYR A CG  
264  C CD1 . TYR A 43  ? 0.7492 0.5440 0.7009 -0.0311 -0.0671 0.0254  32  TYR A CD1 
265  C CD2 . TYR A 43  ? 0.7516 0.5451 0.7068 -0.0205 -0.0805 0.0281  32  TYR A CD2 
266  C CE1 . TYR A 43  ? 0.7661 0.5444 0.7003 -0.0256 -0.0726 0.0319  32  TYR A CE1 
267  C CE2 . TYR A 43  ? 0.7720 0.5471 0.7091 -0.0139 -0.0846 0.0346  32  TYR A CE2 
268  C CZ  . TYR A 43  ? 0.7856 0.5531 0.7119 -0.0163 -0.0815 0.0366  32  TYR A CZ  
269  O OH  . TYR A 43  ? 0.8148 0.5612 0.7208 -0.0090 -0.0853 0.0439  32  TYR A OH  
270  N N   . GLY A 44  ? 0.7555 0.5840 0.7589 -0.0213 -0.0958 -0.0075 33  GLY A N   
271  C CA  . GLY A 44  ? 0.7629 0.5903 0.7659 -0.0111 -0.1081 -0.0108 33  GLY A CA  
272  C C   . GLY A 44  ? 0.7802 0.5875 0.7591 -0.0006 -0.1138 -0.0025 33  GLY A C   
273  O O   . GLY A 44  ? 0.7936 0.5916 0.7613 0.0005  -0.1149 -0.0013 33  GLY A O   
274  N N   . HIS A 45  ? 0.7786 0.5764 0.7483 0.0074  -0.1156 0.0034  34  HIS A N   
275  C CA  . HIS A 45  ? 0.7922 0.5659 0.7377 0.0196  -0.1184 0.0113  34  HIS A CA  
276  C C   . HIS A 45  ? 0.7906 0.5515 0.7272 0.0182  -0.1079 0.0247  34  HIS A C   
277  O O   . HIS A 45  ? 0.7820 0.5507 0.7287 0.0154  -0.1043 0.0244  34  HIS A O   
278  C CB  . HIS A 45  ? 0.8094 0.5789 0.7497 0.0349  -0.1293 0.0036  34  HIS A CB  
279  C CG  . HIS A 45  ? 0.8366 0.6271 0.7952 0.0358  -0.1404 -0.0132 34  HIS A CG  
280  N ND1 . HIS A 45  ? 0.8686 0.6567 0.8209 0.0462  -0.1528 -0.0227 34  HIS A ND1 
281  C CD2 . HIS A 45  ? 0.8367 0.6501 0.8204 0.0281  -0.1405 -0.0223 34  HIS A CD2 
282  C CE1 . HIS A 45  ? 0.8596 0.6716 0.8362 0.0438  -0.1602 -0.0384 34  HIS A CE1 
283  N NE2 . HIS A 45  ? 0.8438 0.6705 0.8398 0.0328  -0.1524 -0.0380 34  HIS A NE2 
284  N N   . VAL A 46  ? 0.7984 0.5392 0.7170 0.0202  -0.1027 0.0359  35  VAL A N   
285  C CA  . VAL A 46  ? 0.8011 0.5292 0.7141 0.0195  -0.0923 0.0472  35  VAL A CA  
286  C C   . VAL A 46  ? 0.8179 0.5160 0.7097 0.0347  -0.0918 0.0525  35  VAL A C   
287  O O   . VAL A 46  ? 0.8292 0.5109 0.7031 0.0446  -0.0976 0.0529  35  VAL A O   
288  C CB  . VAL A 46  ? 0.8019 0.5301 0.7131 0.0098  -0.0836 0.0567  35  VAL A CB  
289  C CG1 . VAL A 46  ? 0.8086 0.5250 0.7176 0.0098  -0.0738 0.0664  35  VAL A CG1 
290  C CG2 . VAL A 46  ? 0.7925 0.5464 0.7208 -0.0021 -0.0817 0.0513  35  VAL A CG2 
291  N N   . TYR A 47  ? 0.8151 0.5047 0.7083 0.0377  -0.0841 0.0555  36  TYR A N   
292  C CA  . TYR A 47  ? 0.8301 0.4878 0.7030 0.0530  -0.0791 0.0602  36  TYR A CA  
293  C C   . TYR A 47  ? 0.8324 0.4746 0.7062 0.0495  -0.0638 0.0701  36  TYR A C   
294  O O   . TYR A 47  ? 0.8163 0.4778 0.7105 0.0367  -0.0589 0.0697  36  TYR A O   
295  C CB  . TYR A 47  ? 0.8317 0.4911 0.7061 0.0618  -0.0811 0.0521  36  TYR A CB  
296  C CG  . TYR A 47  ? 0.8409 0.5182 0.7186 0.0661  -0.0962 0.0404  36  TYR A CG  
297  C CD1 . TYR A 47  ? 0.8366 0.5467 0.7392 0.0531  -0.1015 0.0324  36  TYR A CD1 
298  C CD2 . TYR A 47  ? 0.8645 0.5250 0.7209 0.0848  -0.1047 0.0363  36  TYR A CD2 
299  C CE1 . TYR A 47  ? 0.8423 0.5692 0.7520 0.0564  -0.1141 0.0205  36  TYR A CE1 
300  C CE2 . TYR A 47  ? 0.8689 0.5486 0.7318 0.0893  -0.1195 0.0234  36  TYR A CE2 
301  C CZ  . TYR A 47  ? 0.8655 0.5792 0.7572 0.0741  -0.1237 0.0154  36  TYR A CZ  
302  O OH  . TYR A 47  ? 0.8821 0.6156 0.7846 0.0778  -0.1372 0.0016  36  TYR A OH  
303  N N   . LYS A 48  ? 0.8539 0.4603 0.7060 0.0622  -0.0559 0.0779  37  LYS A N   
304  C CA  . LYS A 48  ? 0.8703 0.4574 0.7248 0.0610  -0.0391 0.0858  37  LYS A CA  
305  C C   . LYS A 48  ? 0.8969 0.4725 0.7501 0.0704  -0.0318 0.0804  37  LYS A C   
306  O O   . LYS A 48  ? 0.9191 0.4704 0.7483 0.0882  -0.0330 0.0795  37  LYS A O   
307  C CB  . LYS A 48  ? 0.9018 0.4509 0.7311 0.0715  -0.0323 0.0975  37  LYS A CB  
308  C CG  . LYS A 48  ? 0.9357 0.4642 0.7706 0.0692  -0.0134 0.1058  37  LYS A CG  
309  C CD  . LYS A 48  ? 1.0054 0.4845 0.8093 0.0866  -0.0038 0.1161  37  LYS A CD  
310  C CE  . LYS A 48  ? 1.0536 0.5114 0.8633 0.0829  0.0145  0.1262  37  LYS A CE  
311  N NZ  . LYS A 48  ? 1.1035 0.5135 0.8801 0.0987  0.0217  0.1384  37  LYS A NZ  
312  N N   . ALA A 49  ? 0.8923 0.4868 0.7699 0.0594  -0.0253 0.0755  38  ALA A N   
313  C CA  . ALA A 49  ? 0.9106 0.4980 0.7893 0.0656  -0.0172 0.0696  38  ALA A CA  
314  C C   . ALA A 49  ? 0.9353 0.5006 0.8210 0.0653  0.0045  0.0722  38  ALA A C   
315  O O   . ALA A 49  ? 0.9348 0.5009 0.8340 0.0561  0.0115  0.0766  38  ALA A O   
316  C CB  . ALA A 49  ? 0.8899 0.5150 0.7905 0.0542  -0.0265 0.0601  38  ALA A CB  
317  N N   . LYS A 50  ? 0.9556 0.4999 0.8318 0.0763  0.0164  0.0690  39  LYS A N   
318  C CA  . LYS A 50  ? 0.9755 0.4963 0.8591 0.0768  0.0403  0.0691  39  LYS A CA  
319  C C   . LYS A 50  ? 0.9735 0.5050 0.8672 0.0749  0.0461  0.0597  39  LYS A C   
320  O O   . LYS A 50  ? 0.9741 0.5074 0.8514 0.0847  0.0377  0.0568  39  LYS A O   
321  C CB  . LYS A 50  ? 1.0330 0.5009 0.8836 0.0980  0.0555  0.0769  39  LYS A CB  
322  C CG  . LYS A 50  ? 1.0907 0.5380 0.9402 0.0967  0.0632  0.0867  39  LYS A CG  
323  C CD  . LYS A 50  ? 1.1333 0.5706 1.0083 0.0877  0.0869  0.0852  39  LYS A CD  
324  C CE  . LYS A 50  ? 1.1925 0.5879 1.0549 0.0959  0.1032  0.0959  39  LYS A CE  
325  N NZ  . LYS A 50  ? 1.2231 0.6195 1.0682 0.0978  0.0864  0.1058  39  LYS A NZ  
326  N N   . ARG A 51  ? 0.9718 0.5112 0.8928 0.0625  0.0602  0.0543  40  ARG A N   
327  C CA  . ARG A 51  ? 0.9851 0.5345 0.9166 0.0590  0.0671  0.0453  40  ARG A CA  
328  C C   . ARG A 51  ? 1.0167 0.5256 0.9209 0.0780  0.0863  0.0458  40  ARG A C   
329  O O   . ARG A 51  ? 1.0371 0.5071 0.9304 0.0877  0.1073  0.0497  40  ARG A O   
330  C CB  . ARG A 51  ? 0.9959 0.5643 0.9649 0.0409  0.0770  0.0376  40  ARG A CB  
331  C CG  . ARG A 51  ? 1.0380 0.6445 1.0306 0.0251  0.0593  0.0366  40  ARG A CG  
332  C CD  . ARG A 51  ? 1.0817 0.7239 1.1001 0.0110  0.0528  0.0261  40  ARG A CD  
333  N NE  . ARG A 51  ? 1.1291 0.7701 1.1742 0.0026  0.0707  0.0173  40  ARG A NE  
334  C CZ  . ARG A 51  ? 1.1649 0.8188 1.2260 -0.0045 0.0759  0.0070  40  ARG A CZ  
335  N NH1 . ARG A 51  ? 1.1663 0.8193 1.2545 -0.0126 0.0927  -0.0027 40  ARG A NH1 
336  N NH2 . ARG A 51  ? 1.1622 0.8292 1.2132 -0.0036 0.0652  0.0059  40  ARG A NH2 
337  N N   . LYS A 52  ? 1.0187 0.5354 0.9114 0.0841  0.0807  0.0418  41  LYS A N   
338  C CA  . LYS A 52  ? 1.0474 0.5278 0.9107 0.1040  0.0983  0.0418  41  LYS A CA  
339  C C   . LYS A 52  ? 1.0696 0.5307 0.9460 0.0996  0.1284  0.0370  41  LYS A C   
340  O O   . LYS A 52  ? 1.0947 0.5126 0.9451 0.1176  0.1514  0.0389  41  LYS A O   
341  C CB  . LYS A 52  ? 1.0499 0.5494 0.9021 0.1095  0.0838  0.0381  41  LYS A CB  
342  C CG  . LYS A 52  ? 1.0806 0.5949 0.9189 0.1168  0.0568  0.0405  41  LYS A CG  
343  C CD  . LYS A 52  ? 1.1440 0.6208 0.9399 0.1452  0.0590  0.0444  41  LYS A CD  
344  C CE  . LYS A 52  ? 1.1773 0.6705 0.9591 0.1563  0.0413  0.0397  41  LYS A CE  
345  N NZ  . LYS A 52  ? 1.1729 0.7116 0.9796 0.1399  0.0148  0.0363  41  LYS A NZ  
346  N N   . ASP A 53  ? 1.0596 0.5514 0.9756 0.0768  0.1292  0.0297  42  ASP A N   
347  C CA  . ASP A 53  ? 1.0752 0.5540 1.0103 0.0698  0.1571  0.0220  42  ASP A CA  
348  C C   . ASP A 53  ? 1.0947 0.5451 1.0411 0.0692  0.1790  0.0230  42  ASP A C   
349  O O   . ASP A 53  ? 1.0978 0.5284 1.0571 0.0667  0.2070  0.0163  42  ASP A O   
350  C CB  . ASP A 53  ? 1.0692 0.5920 1.0415 0.0473  0.1487  0.0117  42  ASP A CB  
351  C CG  . ASP A 53  ? 1.0954 0.6585 1.0941 0.0311  0.1244  0.0109  42  ASP A CG  
352  O OD1 . ASP A 53  ? 1.1074 0.6638 1.1114 0.0305  0.1241  0.0152  42  ASP A OD1 
353  O OD2 . ASP A 53  ? 1.0984 0.6979 1.1112 0.0199  0.1070  0.0062  42  ASP A OD2 
354  N N   . GLY A 54  ? 1.1073 0.5554 1.0503 0.0709  0.1678  0.0310  43  GLY A N   
355  C CA  . GLY A 54  ? 1.1312 0.5496 1.0819 0.0722  0.1876  0.0340  43  GLY A CA  
356  C C   . GLY A 54  ? 1.1202 0.5598 1.1195 0.0510  0.1971  0.0240  43  GLY A C   
357  O O   . GLY A 54  ? 1.1276 0.5449 1.1375 0.0510  0.2133  0.0261  43  GLY A O   
358  N N   . LYS A 55  ? 1.0983 0.5807 1.1277 0.0337  0.1867  0.0127  44  LYS A N   
359  C CA  . LYS A 55  ? 1.0843 0.5925 1.1617 0.0143  0.1919  0.0006  44  LYS A CA  
360  C C   . LYS A 55  ? 1.0739 0.6166 1.1665 0.0047  0.1662  0.0040  44  LYS A C   
361  O O   . LYS A 55  ? 1.0548 0.6408 1.1762 -0.0102 0.1505  -0.0053 44  LYS A O   
362  C CB  . LYS A 55  ? 1.0948 0.6320 1.1961 0.0013  0.1920  -0.0140 44  LYS A CB  
363  C CG  . LYS A 55  ? 1.1468 0.6995 1.2236 0.0054  0.1736  -0.0108 44  LYS A CG  
364  C CD  . LYS A 55  ? 1.1720 0.7698 1.2773 -0.0115 0.1591  -0.0226 44  LYS A CD  
365  C CE  . LYS A 55  ? 1.2175 0.8127 1.3069 -0.0084 0.1630  -0.0249 44  LYS A CE  
366  N NZ  . LYS A 55  ? 1.2484 0.8134 1.3423 -0.0068 0.1969  -0.0327 44  LYS A NZ  
367  N N   . ASP A 56  ? 1.0848 0.6066 1.1553 0.0147  0.1624  0.0175  45  ASP A N   
368  C CA  . ASP A 56  ? 1.0726 0.6223 1.1508 0.0077  0.1401  0.0228  45  ASP A CA  
369  C C   . ASP A 56  ? 1.0828 0.5999 1.1423 0.0176  0.1460  0.0366  45  ASP A C   
370  O O   . ASP A 56  ? 1.0754 0.5985 1.1591 0.0099  0.1503  0.0359  45  ASP A O   
371  C CB  . ASP A 56  ? 1.0944 0.6741 1.1556 0.0073  0.1113  0.0261  45  ASP A CB  
372  C CG  . ASP A 56  ? 1.1340 0.7599 1.2183 -0.0065 0.0898  0.0221  45  ASP A CG  
373  O OD1 . ASP A 56  ? 1.1226 0.7739 1.2408 -0.0187 0.0916  0.0093  45  ASP A OD1 
374  O OD2 . ASP A 56  ? 1.1654 0.8017 1.2330 -0.0044 0.0716  0.0307  45  ASP A OD2 
375  N N   . ASP A 57  ? 1.0966 0.5805 1.1129 0.0353  0.1449  0.0486  46  ASP A N   
376  C CA  . ASP A 57  ? 1.1101 0.5603 1.1001 0.0473  0.1473  0.0632  46  ASP A CA  
377  C C   . ASP A 57  ? 1.0749 0.5557 1.0650 0.0399  0.1217  0.0703  46  ASP A C   
378  O O   . ASP A 57  ? 1.0918 0.5489 1.0601 0.0481  0.1210  0.0827  46  ASP A O   
379  C CB  . ASP A 57  ? 1.1559 0.5676 1.1574 0.0500  0.1772  0.0647  46  ASP A CB  
380  C CG  . ASP A 57  ? 1.2590 0.6348 1.2349 0.0614  0.1806  0.0805  46  ASP A CG  
381  O OD1 . ASP A 57  ? 1.2930 0.6488 1.2274 0.0769  0.1700  0.0906  46  ASP A OD1 
382  O OD2 . ASP A 57  ? 1.2910 0.6600 1.2892 0.0549  0.1929  0.0823  46  ASP A OD2 
383  N N   . LYS A 58  ? 1.0260 0.5560 1.0371 0.0258  0.1020  0.0628  47  LYS A N   
384  C CA  . LYS A 58  ? 0.9976 0.5555 1.0080 0.0193  0.0809  0.0685  47  LYS A CA  
385  C C   . LYS A 58  ? 0.9835 0.5396 0.9602 0.0283  0.0633  0.0755  47  LYS A C   
386  O O   . LYS A 58  ? 0.9925 0.5385 0.9524 0.0372  0.0625  0.0729  47  LYS A O   
387  C CB  . LYS A 58  ? 0.9942 0.6015 1.0379 0.0032  0.0688  0.0570  47  LYS A CB  
388  C CG  . LYS A 58  ? 1.0366 0.6510 1.1181 -0.0060 0.0840  0.0462  47  LYS A CG  
389  C CD  . LYS A 58  ? 1.0748 0.7373 1.1856 -0.0190 0.0701  0.0330  47  LYS A CD  
390  C CE  . LYS A 58  ? 1.1191 0.8084 1.2355 -0.0239 0.0553  0.0365  47  LYS A CE  
391  N NZ  . LYS A 58  ? 1.1345 0.8622 1.2532 -0.0291 0.0351  0.0303  47  LYS A NZ  
392  N N   . ASP A 59  ? 0.9601 0.5264 0.9276 0.0262  0.0499  0.0835  48  ASP A N   
393  C CA  . ASP A 59  ? 0.9502 0.5194 0.8914 0.0323  0.0327  0.0881  48  ASP A CA  
394  C C   . ASP A 59  ? 0.9034 0.5184 0.8603 0.0201  0.0151  0.0811  48  ASP A C   
395  O O   . ASP A 59  ? 0.8892 0.5290 0.8674 0.0089  0.0134  0.0789  48  ASP A O   
396  C CB  . ASP A 59  ? 0.9881 0.5353 0.9069 0.0383  0.0316  0.1013  48  ASP A CB  
397  C CG  . ASP A 59  ? 1.0774 0.5737 0.9669 0.0561  0.0441  0.1093  48  ASP A CG  
398  O OD1 . ASP A 59  ? 1.1032 0.5830 0.9801 0.0673  0.0480  0.1047  48  ASP A OD1 
399  O OD2 . ASP A 59  ? 1.1157 0.5870 0.9924 0.0601  0.0504  0.1205  48  ASP A OD2 
400  N N   . TYR A 60  ? 0.8775 0.5029 0.8237 0.0234  0.0026  0.0771  49  TYR A N   
401  C CA  . TYR A 60  ? 0.8379 0.5017 0.7972 0.0132  -0.0118 0.0706  49  TYR A CA  
402  C C   . TYR A 60  ? 0.8183 0.4867 0.7600 0.0163  -0.0256 0.0733  49  TYR A C   
403  O O   . TYR A 60  ? 0.8354 0.4812 0.7554 0.0278  -0.0273 0.0764  49  TYR A O   
404  C CB  . TYR A 60  ? 0.8279 0.5051 0.7989 0.0115  -0.0125 0.0602  49  TYR A CB  
405  C CG  . TYR A 60  ? 0.8256 0.5081 0.8206 0.0046  -0.0007 0.0538  49  TYR A CG  
406  C CD1 . TYR A 60  ? 0.8440 0.4993 0.8377 0.0109  0.0159  0.0529  49  TYR A CD1 
407  C CD2 . TYR A 60  ? 0.8194 0.5333 0.8380 -0.0072 -0.0056 0.0474  49  TYR A CD2 
408  C CE1 . TYR A 60  ? 0.8480 0.5088 0.8672 0.0035  0.0281  0.0449  49  TYR A CE1 
409  C CE2 . TYR A 60  ? 0.8213 0.5425 0.8644 -0.0134 0.0038  0.0390  49  TYR A CE2 
410  C CZ  . TYR A 60  ? 0.8427 0.5383 0.8881 -0.0092 0.0209  0.0373  49  TYR A CZ  
411  O OH  . TYR A 60  ? 0.8493 0.5528 0.9224 -0.0166 0.0316  0.0269  49  TYR A OH  
412  N N   . ALA A 61  ? 0.7834 0.4801 0.7342 0.0070  -0.0348 0.0709  50  ALA A N   
413  C CA  . ALA A 61  ? 0.7709 0.4755 0.7106 0.0078  -0.0462 0.0705  50  ALA A CA  
414  C C   . ALA A 61  ? 0.7527 0.4774 0.7034 0.0057  -0.0532 0.0602  50  ALA A C   
415  O O   . ALA A 61  ? 0.7411 0.4856 0.7093 -0.0020 -0.0524 0.0550  50  ALA A O   
416  C CB  . ALA A 61  ? 0.7632 0.4835 0.7054 -0.0004 -0.0481 0.0741  50  ALA A CB  
417  N N   . LEU A 62  ? 0.7507 0.4690 0.6910 0.0138  -0.0599 0.0567  51  LEU A N   
418  C CA  . LEU A 62  ? 0.7410 0.4758 0.6908 0.0132  -0.0661 0.0473  51  LEU A CA  
419  C C   . LEU A 62  ? 0.7316 0.4799 0.6810 0.0120  -0.0770 0.0428  51  LEU A C   
420  O O   . LEU A 62  ? 0.7460 0.4816 0.6809 0.0203  -0.0822 0.0434  51  LEU A O   
421  C CB  . LEU A 62  ? 0.7533 0.4681 0.6913 0.0262  -0.0637 0.0457  51  LEU A CB  
422  C CG  . LEU A 62  ? 0.7625 0.4875 0.7105 0.0259  -0.0628 0.0386  51  LEU A CG  
423  C CD1 . LEU A 62  ? 0.7646 0.5018 0.7315 0.0144  -0.0549 0.0376  51  LEU A CD1 
424  C CD2 . LEU A 62  ? 0.7791 0.4783 0.7098 0.0407  -0.0565 0.0390  51  LEU A CD2 
425  N N   . LYS A 63  ? 0.7071 0.4791 0.6721 0.0024  -0.0796 0.0376  52  LYS A N   
426  C CA  . LYS A 63  ? 0.7041 0.4879 0.6721 0.0002  -0.0867 0.0321  52  LYS A CA  
427  C C   . LYS A 63  ? 0.7020 0.5005 0.6827 0.0003  -0.0927 0.0219  52  LYS A C   
428  O O   . LYS A 63  ? 0.6959 0.5067 0.6890 -0.0056 -0.0899 0.0195  52  LYS A O   
429  C CB  . LYS A 63  ? 0.7136 0.5083 0.6861 -0.0096 -0.0823 0.0345  52  LYS A CB  
430  C CG  . LYS A 63  ? 0.7398 0.5439 0.7163 -0.0128 -0.0856 0.0282  52  LYS A CG  
431  C CD  . LYS A 63  ? 0.7788 0.5865 0.7525 -0.0197 -0.0781 0.0323  52  LYS A CD  
432  C CE  . LYS A 63  ? 0.8014 0.6210 0.7832 -0.0248 -0.0720 0.0320  52  LYS A CE  
433  N NZ  . LYS A 63  ? 0.8197 0.6414 0.7955 -0.0288 -0.0637 0.0347  52  LYS A NZ  
434  N N   . GLN A 64  ? 0.7089 0.5070 0.6873 0.0073  -0.1013 0.0153  53  GLN A N   
435  C CA  . GLN A 64  ? 0.7129 0.5272 0.7064 0.0068  -0.1071 0.0047  53  GLN A CA  
436  C C   . GLN A 64  ? 0.7190 0.5470 0.7252 -0.0024 -0.1067 -0.0005 53  GLN A C   
437  O O   . GLN A 64  ? 0.7207 0.5449 0.7215 -0.0015 -0.1094 -0.0017 53  GLN A O   
438  C CB  . GLN A 64  ? 0.7372 0.5468 0.7240 0.0202  -0.1173 -0.0022 53  GLN A CB  
439  C CG  . GLN A 64  ? 0.7747 0.6027 0.7796 0.0200  -0.1230 -0.0133 53  GLN A CG  
440  C CD  . GLN A 64  ? 0.8564 0.6866 0.8593 0.0326  -0.1357 -0.0238 53  GLN A CD  
441  O OE1 . GLN A 64  ? 0.8763 0.7114 0.8833 0.0325  -0.1423 -0.0307 53  GLN A OE1 
442  N NE2 . GLN A 64  ? 0.8841 0.7112 0.8803 0.0445  -0.1395 -0.0264 53  GLN A NE2 
443  N N   . ILE A 65  ? 0.7186 0.5600 0.7402 -0.0108 -0.1017 -0.0035 54  ILE A N   
444  C CA  . ILE A 65  ? 0.7248 0.5755 0.7576 -0.0189 -0.0969 -0.0085 54  ILE A CA  
445  C C   . ILE A 65  ? 0.7270 0.5872 0.7745 -0.0175 -0.1039 -0.0216 54  ILE A C   
446  O O   . ILE A 65  ? 0.7301 0.5956 0.7846 -0.0116 -0.1118 -0.0280 54  ILE A O   
447  C CB  . ILE A 65  ? 0.7289 0.5863 0.7701 -0.0255 -0.0882 -0.0075 54  ILE A CB  
448  C CG1 . ILE A 65  ? 0.7483 0.5992 0.7771 -0.0260 -0.0833 0.0030  54  ILE A CG1 
449  C CG2 . ILE A 65  ? 0.7325 0.5944 0.7821 -0.0320 -0.0794 -0.0123 54  ILE A CG2 
450  C CD1 . ILE A 65  ? 0.7613 0.6179 0.7956 -0.0294 -0.0775 0.0031  54  ILE A CD1 
451  N N   . GLU A 66  ? 0.7233 0.5857 0.7755 -0.0225 -0.1004 -0.0264 55  GLU A N   
452  C CA  . GLU A 66  ? 0.7203 0.5936 0.7908 -0.0227 -0.1060 -0.0415 55  GLU A CA  
453  C C   . GLU A 66  ? 0.7100 0.5970 0.8054 -0.0261 -0.1040 -0.0515 55  GLU A C   
454  O O   . GLU A 66  ? 0.7096 0.5963 0.8096 -0.0326 -0.0922 -0.0482 55  GLU A O   
455  C CB  . GLU A 66  ? 0.7519 0.6233 0.8235 -0.0300 -0.0975 -0.0442 55  GLU A CB  
456  C CG  . GLU A 66  ? 0.8136 0.6975 0.9086 -0.0323 -0.1012 -0.0623 55  GLU A CG  
457  C CD  . GLU A 66  ? 0.9065 0.7910 0.9966 -0.0224 -0.1184 -0.0693 55  GLU A CD  
458  O OE1 . GLU A 66  ? 0.9442 0.8148 1.0116 -0.0190 -0.1204 -0.0610 55  GLU A OE1 
459  O OE2 . GLU A 66  ? 0.9166 0.8144 1.0243 -0.0169 -0.1299 -0.0830 55  GLU A OE2 
460  N N   . GLY A 67  ? 0.7013 0.5990 0.8109 -0.0203 -0.1157 -0.0637 56  GLY A N   
461  C CA  . GLY A 67  ? 0.6943 0.6058 0.8300 -0.0226 -0.1151 -0.0745 56  GLY A CA  
462  C C   . GLY A 67  ? 0.6998 0.6098 0.8309 -0.0193 -0.1153 -0.0671 56  GLY A C   
463  O O   . GLY A 67  ? 0.7147 0.6134 0.8240 -0.0164 -0.1145 -0.0541 56  GLY A O   
464  N N   . THR A 68  ? 0.6869 0.6080 0.8401 -0.0203 -0.1153 -0.0758 57  THR A N   
465  C CA  . THR A 68  ? 0.6965 0.6155 0.8455 -0.0178 -0.1144 -0.0690 57  THR A CA  
466  C C   . THR A 68  ? 0.6890 0.6038 0.8449 -0.0269 -0.0995 -0.0645 57  THR A C   
467  O O   . THR A 68  ? 0.6875 0.6045 0.8605 -0.0337 -0.0901 -0.0715 57  THR A O   
468  C CB  . THR A 68  ? 0.7144 0.6456 0.8763 -0.0094 -0.1256 -0.0790 57  THR A CB  
469  O OG1 . THR A 68  ? 0.7178 0.6628 0.9118 -0.0149 -0.1232 -0.0935 57  THR A OG1 
470  C CG2 . THR A 68  ? 0.7247 0.6565 0.8734 0.0034  -0.1405 -0.0830 57  THR A CG2 
471  N N   . GLY A 69  ? 0.6854 0.5922 0.8266 -0.0261 -0.0966 -0.0534 58  GLY A N   
472  C CA  . GLY A 69  ? 0.6833 0.5837 0.8256 -0.0317 -0.0843 -0.0484 58  GLY A CA  
473  C C   . GLY A 69  ? 0.6816 0.5722 0.8082 -0.0352 -0.0757 -0.0406 58  GLY A C   
474  O O   . GLY A 69  ? 0.6867 0.5753 0.8013 -0.0342 -0.0789 -0.0374 58  GLY A O   
475  N N   . ILE A 70  ? 0.6743 0.5575 0.7991 -0.0378 -0.0646 -0.0373 59  ILE A N   
476  C CA  . ILE A 70  ? 0.6803 0.5546 0.7886 -0.0387 -0.0563 -0.0308 59  ILE A CA  
477  C C   . ILE A 70  ? 0.6795 0.5498 0.7951 -0.0418 -0.0441 -0.0367 59  ILE A C   
478  O O   . ILE A 70  ? 0.6818 0.5453 0.8052 -0.0426 -0.0320 -0.0402 59  ILE A O   
479  C CB  . ILE A 70  ? 0.6921 0.5589 0.7882 -0.0367 -0.0523 -0.0239 59  ILE A CB  
480  C CG1 . ILE A 70  ? 0.7107 0.5810 0.7986 -0.0348 -0.0626 -0.0184 59  ILE A CG1 
481  C CG2 . ILE A 70  ? 0.7042 0.5624 0.7838 -0.0352 -0.0432 -0.0194 59  ILE A CG2 
482  C CD1 . ILE A 70  ? 0.7291 0.6009 0.8241 -0.0341 -0.0655 -0.0193 59  ILE A CD1 
483  N N   . SER A 71  ? 0.6724 0.5452 0.7855 -0.0432 -0.0458 -0.0383 60  SER A N   
484  C CA  . SER A 71  ? 0.6713 0.5397 0.7900 -0.0468 -0.0327 -0.0442 60  SER A CA  
485  C C   . SER A 71  ? 0.6793 0.5340 0.7765 -0.0447 -0.0189 -0.0362 60  SER A C   
486  O O   . SER A 71  ? 0.6894 0.5418 0.7691 -0.0407 -0.0235 -0.0270 60  SER A O   
487  C CB  . SER A 71  ? 0.6911 0.5651 0.8093 -0.0483 -0.0398 -0.0470 60  SER A CB  
488  O OG  . SER A 71  ? 0.7261 0.5972 0.8218 -0.0451 -0.0475 -0.0358 60  SER A OG  
489  N N   . MET A 72  ? 0.6740 0.5193 0.7713 -0.0463 -0.0015 -0.0403 61  MET A N   
490  C CA  . MET A 72  ? 0.6875 0.5183 0.7597 -0.0414 0.0124  -0.0327 61  MET A CA  
491  C C   . MET A 72  ? 0.6910 0.5249 0.7419 -0.0395 0.0036  -0.0228 61  MET A C   
492  O O   . MET A 72  ? 0.6987 0.5287 0.7302 -0.0337 0.0030  -0.0148 61  MET A O   
493  C CB  . MET A 72  ? 0.7032 0.5218 0.7781 -0.0433 0.0344  -0.0393 61  MET A CB  
494  C CG  . MET A 72  ? 0.7332 0.5439 0.8270 -0.0439 0.0477  -0.0482 61  MET A CG  
495  S SD  . MET A 72  ? 0.7983 0.5895 0.8682 -0.0326 0.0580  -0.0402 61  MET A SD  
496  C CE  . MET A 72  ? 0.7824 0.5501 0.8270 -0.0264 0.0861  -0.0388 61  MET A CE  
497  N N   . SER A 73  ? 0.6824 0.5236 0.7387 -0.0440 -0.0044 -0.0244 62  SER A N   
498  C CA  . SER A 73  ? 0.6878 0.5302 0.7271 -0.0429 -0.0124 -0.0154 62  SER A CA  
499  C C   . SER A 73  ? 0.6735 0.5213 0.7076 -0.0394 -0.0267 -0.0085 62  SER A C   
500  O O   . SER A 73  ? 0.6837 0.5289 0.7007 -0.0359 -0.0264 -0.0003 62  SER A O   
501  C CB  . SER A 73  ? 0.7166 0.5637 0.7647 -0.0473 -0.0190 -0.0202 62  SER A CB  
502  O OG  . SER A 73  ? 0.7704 0.6179 0.8053 -0.0453 -0.0307 -0.0118 62  SER A OG  
503  N N   . ALA A 74  ? 0.6492 0.5047 0.6984 -0.0401 -0.0382 -0.0127 63  ALA A N   
504  C CA  . ALA A 74  ? 0.6389 0.4978 0.6844 -0.0373 -0.0491 -0.0075 63  ALA A CA  
505  C C   . ALA A 74  ? 0.6337 0.4902 0.6720 -0.0343 -0.0444 -0.0044 63  ALA A C   
506  O O   . ALA A 74  ? 0.6381 0.4959 0.6676 -0.0321 -0.0491 0.0010  63  ALA A O   
507  C CB  . ALA A 74  ? 0.6306 0.4961 0.6916 -0.0373 -0.0591 -0.0131 63  ALA A CB  
508  N N   . CYS A 75  ? 0.6250 0.4768 0.6673 -0.0337 -0.0344 -0.0088 64  CYS A N   
509  C CA  . CYS A 75  ? 0.6255 0.4716 0.6589 -0.0288 -0.0289 -0.0073 64  CYS A CA  
510  C C   . CYS A 75  ? 0.6139 0.4563 0.6262 -0.0236 -0.0246 -0.0016 64  CYS A C   
511  O O   . CYS A 75  ? 0.6087 0.4541 0.6133 -0.0196 -0.0301 0.0011  64  CYS A O   
512  C CB  . CYS A 75  ? 0.6449 0.4816 0.6852 -0.0282 -0.0156 -0.0132 64  CYS A CB  
513  S SG  . CYS A 75  ? 0.7209 0.5481 0.7541 -0.0213 -0.0117 -0.0126 64  CYS A SG  
514  N N   . ARG A 76  ? 0.6102 0.4472 0.6141 -0.0238 -0.0151 -0.0004 65  ARG A N   
515  C CA  . ARG A 76  ? 0.6147 0.4472 0.5966 -0.0180 -0.0089 0.0053  65  ARG A CA  
516  C C   . ARG A 76  ? 0.6067 0.4484 0.5851 -0.0186 -0.0210 0.0112  65  ARG A C   
517  O O   . ARG A 76  ? 0.6137 0.4569 0.5791 -0.0121 -0.0217 0.0142  65  ARG A O   
518  C CB  . ARG A 76  ? 0.6368 0.4607 0.6116 -0.0196 0.0052  0.0054  65  ARG A CB  
519  C CG  . ARG A 76  ? 0.6725 0.4897 0.6209 -0.0117 0.0144  0.0119  65  ARG A CG  
520  C CD  . ARG A 76  ? 0.7090 0.5153 0.6471 -0.0129 0.0313  0.0125  65  ARG A CD  
521  N NE  . ARG A 76  ? 0.7420 0.5389 0.6509 -0.0019 0.0432  0.0181  65  ARG A NE  
522  C CZ  . ARG A 76  ? 0.7435 0.5410 0.6360 -0.0003 0.0441  0.0259  65  ARG A CZ  
523  N NH1 . ARG A 76  ? 0.7117 0.5162 0.6134 -0.0095 0.0349  0.0295  65  ARG A NH1 
524  N NH2 . ARG A 76  ? 0.7383 0.5280 0.6032 0.0118  0.0549  0.0303  65  ARG A NH2 
525  N N   . GLU A 77  ? 0.5913 0.4380 0.5808 -0.0250 -0.0299 0.0122  66  GLU A N   
526  C CA  . GLU A 77  ? 0.5852 0.4363 0.5714 -0.0252 -0.0387 0.0181  66  GLU A CA  
527  C C   . GLU A 77  ? 0.5710 0.4291 0.5637 -0.0236 -0.0469 0.0167  66  GLU A C   
528  O O   . GLU A 77  ? 0.5746 0.4367 0.5621 -0.0208 -0.0492 0.0195  66  GLU A O   
529  C CB  . GLU A 77  ? 0.6086 0.4583 0.6004 -0.0297 -0.0447 0.0199  66  GLU A CB  
530  C CG  . GLU A 77  ? 0.6834 0.5307 0.6643 -0.0285 -0.0460 0.0281  66  GLU A CG  
531  C CD  . GLU A 77  ? 0.7962 0.6372 0.7770 -0.0304 -0.0512 0.0317  66  GLU A CD  
532  O OE1 . GLU A 77  ? 0.8323 0.6724 0.8208 -0.0321 -0.0548 0.0266  66  GLU A OE1 
533  O OE2 . GLU A 77  ? 0.8306 0.6667 0.8030 -0.0292 -0.0515 0.0391  66  GLU A OE2 
534  N N   . ILE A 78  ? 0.5535 0.4135 0.5585 -0.0254 -0.0505 0.0116  67  ILE A N   
535  C CA  . ILE A 78  ? 0.5434 0.4090 0.5547 -0.0246 -0.0569 0.0096  67  ILE A CA  
536  C C   . ILE A 78  ? 0.5526 0.4197 0.5546 -0.0183 -0.0542 0.0078  67  ILE A C   
537  O O   . ILE A 78  ? 0.5617 0.4356 0.5641 -0.0165 -0.0592 0.0072  67  ILE A O   
538  C CB  . ILE A 78  ? 0.5332 0.3991 0.5575 -0.0275 -0.0602 0.0054  67  ILE A CB  
539  C CG1 . ILE A 78  ? 0.5345 0.3999 0.5652 -0.0304 -0.0656 0.0064  67  ILE A CG1 
540  C CG2 . ILE A 78  ? 0.5328 0.4023 0.5610 -0.0264 -0.0637 0.0027  67  ILE A CG2 
541  C CD1 . ILE A 78  ? 0.5422 0.4084 0.5837 -0.0315 -0.0682 0.0021  67  ILE A CD1 
542  N N   . ALA A 79  ? 0.5471 0.4068 0.5405 -0.0139 -0.0457 0.0061  68  ALA A N   
543  C CA  . ALA A 79  ? 0.5522 0.4097 0.5322 -0.0044 -0.0429 0.0040  68  ALA A CA  
544  C C   . ALA A 79  ? 0.5582 0.4204 0.5248 0.0015  -0.0433 0.0066  68  ALA A C   
545  O O   . ALA A 79  ? 0.5619 0.4314 0.5258 0.0074  -0.0494 0.0033  68  ALA A O   
546  C CB  . ALA A 79  ? 0.5569 0.4001 0.5273 0.0009  -0.0303 0.0023  68  ALA A CB  
547  N N   . LEU A 80  ? 0.5577 0.4166 0.5170 0.0000  -0.0374 0.0118  69  LEU A N   
548  C CA  . LEU A 80  ? 0.5615 0.4241 0.5068 0.0062  -0.0364 0.0154  69  LEU A CA  
549  C C   . LEU A 80  ? 0.5632 0.4385 0.5210 0.0019  -0.0472 0.0165  69  LEU A C   
550  O O   . LEU A 80  ? 0.5635 0.4481 0.5188 0.0084  -0.0519 0.0137  69  LEU A O   
551  C CB  . LEU A 80  ? 0.5637 0.4164 0.4948 0.0062  -0.0244 0.0213  69  LEU A CB  
552  C CG  . LEU A 80  ? 0.5822 0.4201 0.4960 0.0138  -0.0090 0.0197  69  LEU A CG  
553  C CD1 . LEU A 80  ? 0.5879 0.4160 0.4903 0.0117  0.0044  0.0248  69  LEU A CD1 
554  C CD2 . LEU A 80  ? 0.5922 0.4284 0.4857 0.0294  -0.0068 0.0175  69  LEU A CD2 
555  N N   . LEU A 81  ? 0.5582 0.4329 0.5298 -0.0077 -0.0507 0.0193  70  LEU A N   
556  C CA  . LEU A 81  ? 0.5563 0.4377 0.5397 -0.0115 -0.0573 0.0205  70  LEU A CA  
557  C C   . LEU A 81  ? 0.5533 0.4456 0.5505 -0.0110 -0.0646 0.0127  70  LEU A C   
558  O O   . LEU A 81  ? 0.5528 0.4528 0.5594 -0.0117 -0.0681 0.0112  70  LEU A O   
559  C CB  . LEU A 81  ? 0.5541 0.4281 0.5458 -0.0191 -0.0584 0.0244  70  LEU A CB  
560  C CG  . LEU A 81  ? 0.5672 0.4317 0.5479 -0.0204 -0.0534 0.0322  70  LEU A CG  
561  C CD1 . LEU A 81  ? 0.5686 0.4252 0.5559 -0.0251 -0.0564 0.0339  70  LEU A CD1 
562  C CD2 . LEU A 81  ? 0.5740 0.4398 0.5478 -0.0180 -0.0516 0.0380  70  LEU A CD2 
563  N N   . ARG A 82  ? 0.5471 0.4391 0.5467 -0.0101 -0.0661 0.0072  71  ARG A N   
564  C CA  . ARG A 82  ? 0.5389 0.4396 0.5497 -0.0096 -0.0724 -0.0009 71  ARG A CA  
565  C C   . ARG A 82  ? 0.5369 0.4481 0.5414 -0.0001 -0.0761 -0.0067 71  ARG A C   
566  O O   . ARG A 82  ? 0.5283 0.4511 0.5464 -0.0003 -0.0826 -0.0147 71  ARG A O   
567  C CB  . ARG A 82  ? 0.5582 0.4521 0.5680 -0.0098 -0.0714 -0.0032 71  ARG A CB  
568  C CG  . ARG A 82  ? 0.6001 0.4995 0.6215 -0.0115 -0.0769 -0.0103 71  ARG A CG  
569  C CD  . ARG A 82  ? 0.6391 0.5419 0.6780 -0.0200 -0.0788 -0.0110 71  ARG A CD  
570  N NE  . ARG A 82  ? 0.6810 0.5888 0.7304 -0.0218 -0.0822 -0.0186 71  ARG A NE  
571  C CZ  . ARG A 82  ? 0.7084 0.6279 0.7653 -0.0197 -0.0869 -0.0272 71  ARG A CZ  
572  N NH1 . ARG A 82  ? 0.6985 0.6214 0.7650 -0.0222 -0.0892 -0.0347 71  ARG A NH1 
573  N NH2 . ARG A 82  ? 0.7104 0.6388 0.7655 -0.0147 -0.0893 -0.0292 71  ARG A NH2 
574  N N   . GLU A 83  ? 0.5439 0.4510 0.5280 0.0091  -0.0713 -0.0038 72  GLU A N   
575  C CA  . GLU A 83  ? 0.5495 0.4652 0.5224 0.0218  -0.0747 -0.0094 72  GLU A CA  
576  C C   . GLU A 83  ? 0.5562 0.4795 0.5261 0.0245  -0.0743 -0.0060 72  GLU A C   
577  O O   . GLU A 83  ? 0.5552 0.4921 0.5253 0.0332  -0.0806 -0.0130 72  GLU A O   
578  C CB  . GLU A 83  ? 0.5811 0.4833 0.5275 0.0341  -0.0671 -0.0085 72  GLU A CB  
579  C CG  . GLU A 83  ? 0.6219 0.5118 0.5691 0.0315  -0.0639 -0.0095 72  GLU A CG  
580  C CD  . GLU A 83  ? 0.6626 0.5586 0.6190 0.0333  -0.0732 -0.0185 72  GLU A CD  
581  O OE1 . GLU A 83  ? 0.6877 0.5898 0.6341 0.0459  -0.0789 -0.0257 72  GLU A OE1 
582  O OE2 . GLU A 83  ? 0.6536 0.5478 0.6255 0.0230  -0.0747 -0.0187 72  GLU A OE2 
583  N N   . LEU A 84  ? 0.5626 0.4771 0.5285 0.0183  -0.0670 0.0044  73  LEU A N   
584  C CA  . LEU A 84  ? 0.5693 0.4879 0.5291 0.0212  -0.0648 0.0097  73  LEU A CA  
585  C C   . LEU A 84  ? 0.5605 0.4911 0.5448 0.0144  -0.0710 0.0072  73  LEU A C   
586  O O   . LEU A 84  ? 0.5565 0.4824 0.5576 0.0035  -0.0712 0.0087  73  LEU A O   
587  C CB  . LEU A 84  ? 0.5824 0.4852 0.5268 0.0176  -0.0539 0.0216  73  LEU A CB  
588  C CG  . LEU A 84  ? 0.6147 0.5044 0.5351 0.0249  -0.0436 0.0235  73  LEU A CG  
589  C CD1 . LEU A 84  ? 0.6294 0.5045 0.5463 0.0161  -0.0345 0.0312  73  LEU A CD1 
590  C CD2 . LEU A 84  ? 0.6300 0.5200 0.5250 0.0397  -0.0379 0.0247  73  LEU A CD2 
591  N N   . LYS A 85  ? 0.5538 0.4987 0.5396 0.0220  -0.0748 0.0029  74  LYS A N   
592  C CA  . LYS A 85  ? 0.5423 0.4991 0.5531 0.0168  -0.0786 -0.0008 74  LYS A CA  
593  C C   . LYS A 85  ? 0.5359 0.4970 0.5363 0.0237  -0.0756 0.0051  74  LYS A C   
594  O O   . LYS A 85  ? 0.5330 0.5090 0.5273 0.0361  -0.0806 -0.0021 74  LYS A O   
595  C CB  . LYS A 85  ? 0.5548 0.5312 0.5894 0.0182  -0.0889 -0.0177 74  LYS A CB  
596  C CG  . LYS A 85  ? 0.6025 0.5903 0.6694 0.0107  -0.0902 -0.0238 74  LYS A CG  
597  C CD  . LYS A 85  ? 0.6656 0.6738 0.7595 0.0107  -0.0996 -0.0430 74  LYS A CD  
598  C CE  . LYS A 85  ? 0.7213 0.7243 0.8433 -0.0036 -0.0954 -0.0471 74  LYS A CE  
599  N NZ  . LYS A 85  ? 0.7254 0.7465 0.8725 -0.0048 -0.1030 -0.0664 74  LYS A NZ  
600  N N   . HIS A 86  ? 0.5327 0.4800 0.5298 0.0168  -0.0675 0.0180  75  HIS A N   
601  C CA  . HIS A 86  ? 0.5350 0.4830 0.5220 0.0216  -0.0629 0.0260  75  HIS A CA  
602  C C   . HIS A 86  ? 0.5311 0.4659 0.5306 0.0106  -0.0571 0.0356  75  HIS A C   
603  O O   . HIS A 86  ? 0.5354 0.4529 0.5334 0.0024  -0.0534 0.0417  75  HIS A O   
604  C CB  . HIS A 86  ? 0.5619 0.4980 0.5121 0.0297  -0.0546 0.0363  75  HIS A CB  
605  C CG  . HIS A 86  ? 0.5941 0.5335 0.5300 0.0379  -0.0501 0.0431  75  HIS A CG  
606  N ND1 . HIS A 86  ? 0.6247 0.5502 0.5559 0.0314  -0.0418 0.0572  75  HIS A ND1 
607  C CD2 . HIS A 86  ? 0.6052 0.5606 0.5314 0.0528  -0.0535 0.0372  75  HIS A CD2 
608  C CE1 . HIS A 86  ? 0.6321 0.5656 0.5515 0.0413  -0.0395 0.0602  75  HIS A CE1 
609  N NE2 . HIS A 86  ? 0.6232 0.5755 0.5389 0.0550  -0.0466 0.0481  75  HIS A NE2 
610  N N   . PRO A 87  ? 0.5252 0.4665 0.5364 0.0115  -0.0558 0.0369  76  PRO A N   
611  C CA  . PRO A 87  ? 0.5266 0.4503 0.5479 0.0024  -0.0482 0.0468  76  PRO A CA  
612  C C   . PRO A 87  ? 0.5392 0.4373 0.5323 0.0002  -0.0395 0.0645  76  PRO A C   
613  O O   . PRO A 87  ? 0.5425 0.4205 0.5392 -0.0066 -0.0342 0.0723  76  PRO A O   
614  C CB  . PRO A 87  ? 0.5233 0.4608 0.5604 0.0061  -0.0479 0.0443  76  PRO A CB  
615  C CG  . PRO A 87  ? 0.5274 0.4852 0.5487 0.0193  -0.0539 0.0387  76  PRO A CG  
616  C CD  . PRO A 87  ? 0.5083 0.4728 0.5255 0.0218  -0.0611 0.0284  76  PRO A CD  
617  N N   . ASN A 88  ? 0.5375 0.4345 0.5016 0.0068  -0.0370 0.0700  77  ASN A N   
618  C CA  . ASN A 88  ? 0.5459 0.4204 0.4842 0.0043  -0.0283 0.0846  77  ASN A CA  
619  C C   . ASN A 88  ? 0.5478 0.4137 0.4763 0.0011  -0.0285 0.0829  77  ASN A C   
620  O O   . ASN A 88  ? 0.5620 0.4129 0.4693 -0.0002 -0.0215 0.0917  77  ASN A O   
621  C CB  . ASN A 88  ? 0.5593 0.4334 0.4715 0.0123  -0.0209 0.0939  77  ASN A CB  
622  C CG  . ASN A 88  ? 0.5753 0.4499 0.4954 0.0130  -0.0181 0.1005  77  ASN A CG  
623  O OD1 . ASN A 88  ? 0.5893 0.4785 0.5050 0.0220  -0.0181 0.0993  77  ASN A OD1 
624  N ND2 . ASN A 88  ? 0.5644 0.4219 0.4960 0.0049  -0.0153 0.1073  77  ASN A ND2 
625  N N   . VAL A 89  ? 0.5323 0.4073 0.4777 -0.0009 -0.0359 0.0711  78  VAL A N   
626  C CA  . VAL A 89  ? 0.5343 0.4022 0.4751 -0.0043 -0.0365 0.0685  78  VAL A CA  
627  C C   . VAL A 89  ? 0.5307 0.3953 0.4940 -0.0114 -0.0419 0.0638  78  VAL A C   
628  O O   . VAL A 89  ? 0.5214 0.3981 0.5052 -0.0117 -0.0468 0.0552  78  VAL A O   
629  C CB  . VAL A 89  ? 0.5346 0.4140 0.4692 0.0024  -0.0384 0.0592  78  VAL A CB  
630  C CG1 . VAL A 89  ? 0.5438 0.4141 0.4757 -0.0019 -0.0370 0.0572  78  VAL A CG1 
631  C CG2 . VAL A 89  ? 0.5428 0.4242 0.4527 0.0129  -0.0315 0.0628  78  VAL A CG2 
632  N N   . ILE A 90  ? 0.5356 0.3839 0.4948 -0.0162 -0.0406 0.0683  79  ILE A N   
633  C CA  . ILE A 90  ? 0.5378 0.3797 0.5128 -0.0204 -0.0442 0.0647  79  ILE A CA  
634  C C   . ILE A 90  ? 0.5536 0.4104 0.5454 -0.0209 -0.0500 0.0523  79  ILE A C   
635  O O   . ILE A 90  ? 0.5625 0.4282 0.5491 -0.0189 -0.0520 0.0475  79  ILE A O   
636  C CB  . ILE A 90  ? 0.5351 0.3594 0.4997 -0.0223 -0.0437 0.0695  79  ILE A CB  
637  C CG1 . ILE A 90  ? 0.5434 0.3541 0.5176 -0.0231 -0.0447 0.0693  79  ILE A CG1 
638  C CG2 . ILE A 90  ? 0.5306 0.3609 0.4921 -0.0230 -0.0462 0.0634  79  ILE A CG2 
639  C CD1 . ILE A 90  ? 0.5522 0.3500 0.5300 -0.0222 -0.0389 0.0758  79  ILE A CD1 
640  N N   . SER A 91  ? 0.5543 0.4129 0.5655 -0.0232 -0.0511 0.0471  80  SER A N   
641  C CA  . SER A 91  ? 0.5553 0.4272 0.5825 -0.0244 -0.0559 0.0353  80  SER A CA  
642  C C   . SER A 91  ? 0.5649 0.4271 0.5943 -0.0271 -0.0567 0.0336  80  SER A C   
643  O O   . SER A 91  ? 0.5714 0.4178 0.6023 -0.0282 -0.0528 0.0373  80  SER A O   
644  C CB  . SER A 91  ? 0.5614 0.4423 0.6111 -0.0259 -0.0552 0.0280  80  SER A CB  
645  O OG  . SER A 91  ? 0.5898 0.4914 0.6440 -0.0218 -0.0598 0.0210  80  SER A OG  
646  N N   . LEU A 92  ? 0.5620 0.4324 0.5907 -0.0270 -0.0610 0.0277  81  LEU A N   
647  C CA  . LEU A 92  ? 0.5638 0.4281 0.5960 -0.0290 -0.0623 0.0250  81  LEU A CA  
648  C C   . LEU A 92  ? 0.5665 0.4351 0.6169 -0.0314 -0.0615 0.0173  81  LEU A C   
649  O O   . LEU A 92  ? 0.5637 0.4472 0.6244 -0.0316 -0.0638 0.0099  81  LEU A O   
650  C CB  . LEU A 92  ? 0.5566 0.4274 0.5835 -0.0281 -0.0656 0.0214  81  LEU A CB  
651  C CG  . LEU A 92  ? 0.5631 0.4296 0.5944 -0.0298 -0.0673 0.0185  81  LEU A CG  
652  C CD1 . LEU A 92  ? 0.5708 0.4238 0.5943 -0.0290 -0.0669 0.0239  81  LEU A CD1 
653  C CD2 . LEU A 92  ? 0.5671 0.4404 0.5971 -0.0291 -0.0693 0.0140  81  LEU A CD2 
654  N N   . GLN A 93  ? 0.5712 0.4260 0.6247 -0.0323 -0.0573 0.0183  82  GLN A N   
655  C CA  . GLN A 93  ? 0.5751 0.4306 0.6452 -0.0351 -0.0530 0.0108  82  GLN A CA  
656  C C   . GLN A 93  ? 0.5901 0.4458 0.6604 -0.0358 -0.0546 0.0065  82  GLN A C   
657  O O   . GLN A 93  ? 0.5934 0.4592 0.6762 -0.0388 -0.0548 -0.0019 82  GLN A O   
658  C CB  . GLN A 93  ? 0.5955 0.4313 0.6681 -0.0342 -0.0428 0.0144  82  GLN A CB  
659  C CG  . GLN A 93  ? 0.6628 0.4855 0.7229 -0.0309 -0.0407 0.0247  82  GLN A CG  
660  C CD  . GLN A 93  ? 0.7401 0.5591 0.8142 -0.0324 -0.0323 0.0240  82  GLN A CD  
661  O OE1 . GLN A 93  ? 0.7748 0.6076 0.8550 -0.0337 -0.0349 0.0235  82  GLN A OE1 
662  N NE2 . GLN A 93  ? 0.7443 0.5435 0.8236 -0.0314 -0.0208 0.0235  82  GLN A NE2 
663  N N   . LYS A 94  ? 0.5963 0.4410 0.6534 -0.0327 -0.0558 0.0117  83  LYS A N   
664  C CA  . LYS A 94  ? 0.6003 0.4440 0.6566 -0.0323 -0.0569 0.0086  83  LYS A CA  
665  C C   . LYS A 94  ? 0.6008 0.4445 0.6462 -0.0297 -0.0632 0.0117  83  LYS A C   
666  O O   . LYS A 94  ? 0.6026 0.4419 0.6391 -0.0275 -0.0650 0.0167  83  LYS A O   
667  C CB  . LYS A 94  ? 0.6380 0.4637 0.6922 -0.0292 -0.0485 0.0093  83  LYS A CB  
668  C CG  . LYS A 94  ? 0.7041 0.5294 0.7729 -0.0330 -0.0395 0.0027  83  LYS A CG  
669  C CD  . LYS A 94  ? 0.7792 0.5827 0.8410 -0.0281 -0.0283 0.0037  83  LYS A CD  
670  C CE  . LYS A 94  ? 0.8189 0.6210 0.8960 -0.0328 -0.0166 -0.0043 83  LYS A CE  
671  N NZ  . LYS A 94  ? 0.8491 0.6249 0.9159 -0.0261 -0.0018 -0.0025 83  LYS A NZ  
672  N N   . VAL A 95  ? 0.5980 0.4461 0.6451 -0.0301 -0.0656 0.0082  84  VAL A N   
673  C CA  . VAL A 95  ? 0.6034 0.4527 0.6457 -0.0281 -0.0705 0.0087  84  VAL A CA  
674  C C   . VAL A 95  ? 0.6183 0.4609 0.6593 -0.0247 -0.0695 0.0072  84  VAL A C   
675  O O   . VAL A 95  ? 0.6175 0.4610 0.6636 -0.0268 -0.0657 0.0044  84  VAL A O   
676  C CB  . VAL A 95  ? 0.5980 0.4590 0.6444 -0.0310 -0.0729 0.0055  84  VAL A CB  
677  C CG1 . VAL A 95  ? 0.5973 0.4590 0.6435 -0.0299 -0.0756 0.0043  84  VAL A CG1 
678  C CG2 . VAL A 95  ? 0.6021 0.4683 0.6457 -0.0317 -0.0726 0.0068  84  VAL A CG2 
679  N N   . PHE A 96  ? 0.6309 0.4668 0.6644 -0.0188 -0.0726 0.0084  85  PHE A N   
680  C CA  . PHE A 96  ? 0.6507 0.4807 0.6803 -0.0130 -0.0722 0.0067  85  PHE A CA  
681  C C   . PHE A 96  ? 0.6614 0.5009 0.6954 -0.0121 -0.0794 0.0032  85  PHE A C   
682  O O   . PHE A 96  ? 0.6641 0.5067 0.6982 -0.0113 -0.0846 0.0024  85  PHE A O   
683  C CB  . PHE A 96  ? 0.6621 0.4740 0.6775 -0.0030 -0.0696 0.0095  85  PHE A CB  
684  C CG  . PHE A 96  ? 0.6771 0.4763 0.6900 -0.0037 -0.0598 0.0126  85  PHE A CG  
685  C CD1 . PHE A 96  ? 0.6913 0.4842 0.7068 -0.0047 -0.0497 0.0110  85  PHE A CD1 
686  C CD2 . PHE A 96  ? 0.6927 0.4856 0.7018 -0.0035 -0.0594 0.0168  85  PHE A CD2 
687  C CE1 . PHE A 96  ? 0.7041 0.4855 0.7219 -0.0060 -0.0390 0.0120  85  PHE A CE1 
688  C CE2 . PHE A 96  ? 0.7065 0.4873 0.7163 -0.0041 -0.0493 0.0192  85  PHE A CE2 
689  C CZ  . PHE A 96  ? 0.7022 0.4777 0.7179 -0.0056 -0.0390 0.0161  85  PHE A CZ  
690  N N   . LEU A 97  ? 0.6646 0.5087 0.7037 -0.0130 -0.0788 0.0006  86  LEU A N   
691  C CA  . LEU A 97  ? 0.6717 0.5249 0.7186 -0.0126 -0.0842 -0.0035 86  LEU A CA  
692  C C   . LEU A 97  ? 0.6865 0.5359 0.7278 -0.0031 -0.0868 -0.0055 86  LEU A C   
693  O O   . LEU A 97  ? 0.6865 0.5338 0.7262 -0.0019 -0.0829 -0.0051 86  LEU A O   
694  C CB  . LEU A 97  ? 0.6673 0.5277 0.7241 -0.0197 -0.0815 -0.0046 86  LEU A CB  
695  C CG  . LEU A 97  ? 0.6801 0.5437 0.7393 -0.0259 -0.0792 -0.0035 86  LEU A CG  
696  C CD1 . LEU A 97  ? 0.6831 0.5498 0.7482 -0.0294 -0.0767 -0.0050 86  LEU A CD1 
697  C CD2 . LEU A 97  ? 0.6869 0.5527 0.7464 -0.0261 -0.0814 -0.0040 86  LEU A CD2 
698  N N   . SER A 98  ? 0.6974 0.5453 0.7339 0.0047  -0.0935 -0.0081 87  SER A N   
699  C CA  . SER A 98  ? 0.7154 0.5601 0.7438 0.0174  -0.0981 -0.0114 87  SER A CA  
700  C C   . SER A 98  ? 0.7168 0.5762 0.7608 0.0161  -0.1027 -0.0176 87  SER A C   
701  O O   . SER A 98  ? 0.7069 0.5774 0.7632 0.0161  -0.1104 -0.0246 87  SER A O   
702  C CB  . SER A 98  ? 0.7408 0.5810 0.7607 0.0262  -0.1059 -0.0139 87  SER A CB  
703  O OG  . SER A 98  ? 0.7891 0.6186 0.7917 0.0426  -0.1086 -0.0155 87  SER A OG  
704  N N   . HIS A 99  ? 0.7252 0.5843 0.7701 0.0143  -0.0970 -0.0155 88  HIS A N   
705  C CA  . HIS A 99  ? 0.7298 0.6001 0.7893 0.0123  -0.0988 -0.0196 88  HIS A CA  
706  C C   . HIS A 99  ? 0.7361 0.6151 0.7997 0.0235  -0.1086 -0.0278 88  HIS A C   
707  O O   . HIS A 99  ? 0.7288 0.6217 0.8134 0.0200  -0.1130 -0.0350 88  HIS A O   
708  C CB  . HIS A 99  ? 0.7465 0.6107 0.8003 0.0103  -0.0900 -0.0142 88  HIS A CB  
709  C CG  . HIS A 99  ? 0.7795 0.6426 0.8391 -0.0022 -0.0832 -0.0102 88  HIS A CG  
710  N ND1 . HIS A 99  ? 0.7984 0.6654 0.8687 -0.0082 -0.0805 -0.0101 88  HIS A ND1 
711  C CD2 . HIS A 99  ? 0.7980 0.6559 0.8531 -0.0080 -0.0791 -0.0069 88  HIS A CD2 
712  C CE1 . HIS A 99  ? 0.8064 0.6697 0.8758 -0.0161 -0.0756 -0.0069 88  HIS A CE1 
713  N NE2 . HIS A 99  ? 0.8090 0.6687 0.8709 -0.0165 -0.0752 -0.0056 88  HIS A NE2 
714  N N   . ALA A 100 ? 0.7427 0.6126 0.7865 0.0382  -0.1113 -0.0278 89  ALA A N   
715  C CA  . ALA A 100 ? 0.7413 0.6183 0.7838 0.0532  -0.1222 -0.0365 89  ALA A CA  
716  C C   . ALA A 100 ? 0.7248 0.6166 0.7853 0.0525  -0.1343 -0.0474 89  ALA A C   
717  O O   . ALA A 100 ? 0.7203 0.6274 0.7952 0.0586  -0.1437 -0.0581 89  ALA A O   
718  C CB  . ALA A 100 ? 0.7628 0.6214 0.7744 0.0710  -0.1210 -0.0335 89  ALA A CB  
719  N N   . ASP A 101 ? 0.7130 0.6008 0.7734 0.0454  -0.1338 -0.0454 90  ASP A N   
720  C CA  . ASP A 101 ? 0.6967 0.5964 0.7726 0.0437  -0.1432 -0.0555 90  ASP A CA  
721  C C   . ASP A 101 ? 0.6771 0.5818 0.7709 0.0260  -0.1366 -0.0545 90  ASP A C   
722  O O   . ASP A 101 ? 0.6718 0.5833 0.7764 0.0233  -0.1413 -0.0618 90  ASP A O   
723  C CB  . ASP A 101 ? 0.7280 0.6163 0.7824 0.0567  -0.1506 -0.0563 90  ASP A CB  
724  C CG  . ASP A 101 ? 0.7889 0.6557 0.8208 0.0549  -0.1415 -0.0433 90  ASP A CG  
725  O OD1 . ASP A 101 ? 0.7961 0.6549 0.8227 0.0492  -0.1305 -0.0343 90  ASP A OD1 
726  O OD2 . ASP A 101 ? 0.8259 0.6838 0.8463 0.0595  -0.1454 -0.0430 90  ASP A OD2 
727  N N   A ARG A 102 ? 0.6707 0.5709 0.7659 0.0155  -0.1254 -0.0459 91  ARG A N   
728  N N   B ARG A 102 ? 0.6703 0.5707 0.7659 0.0153  -0.1254 -0.0461 91  ARG A N   
729  C CA  A ARG A 102 ? 0.6660 0.5669 0.7719 0.0016  -0.1170 -0.0433 91  ARG A CA  
730  C CA  B ARG A 102 ? 0.6650 0.5667 0.7720 0.0015  -0.1174 -0.0440 91  ARG A CA  
731  C C   A ARG A 102 ? 0.6699 0.5640 0.7655 -0.0010 -0.1162 -0.0397 91  ARG A C   
732  C C   B ARG A 102 ? 0.6698 0.5639 0.7654 -0.0011 -0.1162 -0.0397 91  ARG A C   
733  O O   A ARG A 102 ? 0.6688 0.5657 0.7741 -0.0095 -0.1113 -0.0412 91  ARG A O   
734  O O   B ARG A 102 ? 0.6689 0.5655 0.7737 -0.0097 -0.1112 -0.0410 91  ARG A O   
735  C CB  A ARG A 102 ? 0.6658 0.5798 0.7994 -0.0047 -0.1158 -0.0533 91  ARG A CB  
736  C CB  B ARG A 102 ? 0.6640 0.5793 0.7989 -0.0043 -0.1173 -0.0551 91  ARG A CB  
737  C CG  A ARG A 102 ? 0.6851 0.6040 0.8296 -0.0036 -0.1143 -0.0550 91  ARG A CG  
738  C CG  B ARG A 102 ? 0.6800 0.6018 0.8295 -0.0043 -0.1155 -0.0583 91  ARG A CG  
739  C CD  A ARG A 102 ? 0.7136 0.6230 0.8533 -0.0111 -0.1029 -0.0453 91  ARG A CD  
740  C CD  B ARG A 102 ? 0.6911 0.6198 0.8680 -0.0134 -0.1084 -0.0662 91  ARG A CD  
741  N NE  A ARG A 102 ? 0.7395 0.6439 0.8667 -0.0061 -0.1025 -0.0391 91  ARG A NE  
742  N NE  B ARG A 102 ? 0.7162 0.6340 0.8886 -0.0226 -0.0959 -0.0593 91  ARG A NE  
743  C CZ  A ARG A 102 ? 0.7484 0.6557 0.8849 -0.0056 -0.1003 -0.0401 91  ARG A CZ  
744  C CZ  B ARG A 102 ? 0.7449 0.6525 0.9084 -0.0257 -0.0874 -0.0501 91  ARG A CZ  
745  N NH1 A ARG A 102 ? 0.7270 0.6421 0.8878 -0.0097 -0.0984 -0.0476 91  ARG A NH1 
746  N NH1 B ARG A 102 ? 0.7356 0.6418 0.8940 -0.0222 -0.0890 -0.0458 91  ARG A NH1 
747  N NH2 A ARG A 102 ? 0.7488 0.6498 0.8708 -0.0011 -0.0983 -0.0336 91  ARG A NH2 
748  N NH2 B ARG A 102 ? 0.7493 0.6472 0.9067 -0.0312 -0.0773 -0.0454 91  ARG A NH2 
749  N N   . LYS A 103 ? 0.6744 0.5572 0.7490 0.0071  -0.1192 -0.0344 92  LYS A N   
750  C CA  . LYS A 103 ? 0.6717 0.5457 0.7349 0.0053  -0.1178 -0.0293 92  LYS A CA  
751  C C   . LYS A 103 ? 0.6658 0.5310 0.7201 -0.0013 -0.1080 -0.0187 92  LYS A C   
752  O O   . LYS A 103 ? 0.6663 0.5263 0.7148 0.0000  -0.1040 -0.0144 92  LYS A O   
753  C CB  . LYS A 103 ? 0.6993 0.5632 0.7448 0.0187  -0.1258 -0.0300 92  LYS A CB  
754  C CG  . LYS A 103 ? 0.7495 0.6243 0.8053 0.0241  -0.1372 -0.0426 92  LYS A CG  
755  C CD  . LYS A 103 ? 0.8186 0.7008 0.8883 0.0125  -0.1346 -0.0462 92  LYS A CD  
756  C CE  . LYS A 103 ? 0.8661 0.7563 0.9442 0.0167  -0.1449 -0.0588 92  LYS A CE  
757  N NZ  . LYS A 103 ? 0.8924 0.7794 0.9704 0.0075  -0.1394 -0.0570 92  LYS A NZ  
758  N N   . VAL A 104 ? 0.6525 0.5169 0.7066 -0.0085 -0.1038 -0.0156 93  VAL A N   
759  C CA  . VAL A 104 ? 0.6499 0.5090 0.6976 -0.0137 -0.0961 -0.0075 93  VAL A CA  
760  C C   . VAL A 104 ? 0.6503 0.4976 0.6830 -0.0109 -0.0954 -0.0010 93  VAL A C   
761  O O   . VAL A 104 ? 0.6546 0.5003 0.6839 -0.0107 -0.0974 -0.0012 93  VAL A O   
762  C CB  . VAL A 104 ? 0.6534 0.5193 0.7099 -0.0222 -0.0900 -0.0083 93  VAL A CB  
763  C CG1 . VAL A 104 ? 0.6647 0.5271 0.7137 -0.0253 -0.0843 -0.0016 93  VAL A CG1 
764  C CG2 . VAL A 104 ? 0.6532 0.5263 0.7235 -0.0242 -0.0889 -0.0137 93  VAL A CG2 
765  N N   . TRP A 105 ? 0.6413 0.4793 0.6659 -0.0088 -0.0913 0.0045  94  TRP A N   
766  C CA  . TRP A 105 ? 0.6459 0.4702 0.6577 -0.0059 -0.0885 0.0110  94  TRP A CA  
767  C C   . TRP A 105 ? 0.6447 0.4709 0.6595 -0.0130 -0.0816 0.0155  94  TRP A C   
768  O O   . TRP A 105 ? 0.6500 0.4833 0.6731 -0.0170 -0.0788 0.0136  94  TRP A O   
769  C CB  . TRP A 105 ? 0.6544 0.4629 0.6548 0.0040  -0.0869 0.0126  94  TRP A CB  
770  C CG  . TRP A 105 ? 0.6596 0.4639 0.6521 0.0151  -0.0947 0.0082  94  TRP A CG  
771  C CD1 . TRP A 105 ? 0.6615 0.4752 0.6602 0.0188  -0.1000 0.0013  94  TRP A CD1 
772  C CD2 . TRP A 105 ? 0.6690 0.4572 0.6444 0.0261  -0.0984 0.0099  94  TRP A CD2 
773  N NE1 . TRP A 105 ? 0.6699 0.4770 0.6575 0.0318  -0.1081 -0.0027 94  TRP A NE1 
774  C CE2 . TRP A 105 ? 0.6766 0.4669 0.6485 0.0370  -0.1073 0.0025  94  TRP A CE2 
775  C CE3 . TRP A 105 ? 0.6827 0.4539 0.6447 0.0286  -0.0950 0.0170  94  TRP A CE3 
776  C CZ2 . TRP A 105 ? 0.6916 0.4676 0.6455 0.0516  -0.1141 0.0010  94  TRP A CZ2 
777  C CZ3 . TRP A 105 ? 0.7028 0.4574 0.6462 0.0421  -0.1004 0.0170  94  TRP A CZ3 
778  C CH2 . TRP A 105 ? 0.7034 0.4608 0.6424 0.0539  -0.1104 0.0086  94  TRP A CH2 
779  N N   . LEU A 106 ? 0.6325 0.4525 0.6403 -0.0137 -0.0794 0.0210  95  LEU A N   
780  C CA  . LEU A 106 ? 0.6193 0.4427 0.6302 -0.0189 -0.0739 0.0243  95  LEU A CA  
781  C C   . LEU A 106 ? 0.6195 0.4272 0.6235 -0.0157 -0.0687 0.0303  95  LEU A C   
782  O O   . LEU A 106 ? 0.6237 0.4175 0.6155 -0.0108 -0.0692 0.0351  95  LEU A O   
783  C CB  . LEU A 106 ? 0.6158 0.4476 0.6256 -0.0230 -0.0738 0.0256  95  LEU A CB  
784  C CG  . LEU A 106 ? 0.6249 0.4680 0.6411 -0.0257 -0.0755 0.0197  95  LEU A CG  
785  C CD1 . LEU A 106 ? 0.6328 0.4787 0.6439 -0.0281 -0.0714 0.0216  95  LEU A CD1 
786  C CD2 . LEU A 106 ? 0.6258 0.4775 0.6514 -0.0277 -0.0749 0.0154  95  LEU A CD2 
787  N N   . LEU A 107 ? 0.6143 0.4233 0.6269 -0.0183 -0.0631 0.0295  96  LEU A N   
788  C CA  . LEU A 107 ? 0.6243 0.4178 0.6349 -0.0161 -0.0553 0.0338  96  LEU A CA  
789  C C   . LEU A 107 ? 0.6243 0.4249 0.6390 -0.0205 -0.0534 0.0370  96  LEU A C   
790  O O   . LEU A 107 ? 0.6178 0.4370 0.6420 -0.0252 -0.0559 0.0327  96  LEU A O   
791  C CB  . LEU A 107 ? 0.6236 0.4146 0.6448 -0.0169 -0.0483 0.0287  96  LEU A CB  
792  C CG  . LEU A 107 ? 0.6413 0.4156 0.6658 -0.0154 -0.0365 0.0308  96  LEU A CG  
793  C CD1 . LEU A 107 ? 0.6621 0.4079 0.6668 -0.0054 -0.0321 0.0381  96  LEU A CD1 
794  C CD2 . LEU A 107 ? 0.6410 0.4154 0.6789 -0.0179 -0.0282 0.0234  96  LEU A CD2 
795  N N   . PHE A 108 ? 0.6308 0.4154 0.6364 -0.0176 -0.0489 0.0447  97  PHE A N   
796  C CA  . PHE A 108 ? 0.6337 0.4225 0.6412 -0.0204 -0.0462 0.0492  97  PHE A CA  
797  C C   . PHE A 108 ? 0.6557 0.4223 0.6616 -0.0173 -0.0364 0.0553  97  PHE A C   
798  O O   . PHE A 108 ? 0.6736 0.4173 0.6689 -0.0108 -0.0325 0.0582  97  PHE A O   
799  C CB  . PHE A 108 ? 0.6324 0.4213 0.6243 -0.0198 -0.0503 0.0554  97  PHE A CB  
800  C CG  . PHE A 108 ? 0.6276 0.4331 0.6189 -0.0223 -0.0566 0.0506  97  PHE A CG  
801  C CD1 . PHE A 108 ? 0.6233 0.4463 0.6189 -0.0252 -0.0569 0.0481  97  PHE A CD1 
802  C CD2 . PHE A 108 ? 0.6352 0.4371 0.6206 -0.0203 -0.0614 0.0484  97  PHE A CD2 
803  C CE1 . PHE A 108 ? 0.6250 0.4580 0.6181 -0.0262 -0.0595 0.0441  97  PHE A CE1 
804  C CE2 . PHE A 108 ? 0.6333 0.4485 0.6207 -0.0229 -0.0648 0.0435  97  PHE A CE2 
805  C CZ  . PHE A 108 ? 0.6226 0.4515 0.6132 -0.0259 -0.0626 0.0419  97  PHE A CZ  
806  N N   . ASP A 109 ? 0.6513 0.4227 0.6658 -0.0202 -0.0320 0.0575  98  ASP A N   
807  C CA  . ASP A 109 ? 0.6655 0.4137 0.6784 -0.0173 -0.0214 0.0645  98  ASP A CA  
808  C C   . ASP A 109 ? 0.6843 0.4118 0.6708 -0.0118 -0.0226 0.0765  98  ASP A C   
809  O O   . ASP A 109 ? 0.6847 0.4229 0.6604 -0.0131 -0.0305 0.0785  98  ASP A O   
810  C CB  . ASP A 109 ? 0.6841 0.4460 0.7146 -0.0218 -0.0176 0.0631  98  ASP A CB  
811  C CG  . ASP A 109 ? 0.7593 0.5351 0.8183 -0.0263 -0.0137 0.0505  98  ASP A CG  
812  O OD1 . ASP A 109 ? 0.7900 0.5503 0.8548 -0.0252 -0.0055 0.0467  98  ASP A OD1 
813  O OD2 . ASP A 109 ? 0.7765 0.5780 0.8515 -0.0300 -0.0181 0.0436  98  ASP A OD2 
814  N N   . TYR A 110 ? 0.6975 0.3935 0.6730 -0.0052 -0.0137 0.0838  99  TYR A N   
815  C CA  . TYR A 110 ? 0.7119 0.3851 0.6607 0.0015  -0.0152 0.0944  99  TYR A CA  
816  C C   . TYR A 110 ? 0.7181 0.3851 0.6610 -0.0004 -0.0105 0.1052  99  TYR A C   
817  O O   . TYR A 110 ? 0.7227 0.3751 0.6727 0.0004  0.0008  0.1094  99  TYR A O   
818  C CB  . TYR A 110 ? 0.7262 0.3640 0.6590 0.0132  -0.0088 0.0972  99  TYR A CB  
819  C CG  . TYR A 110 ? 0.7501 0.3649 0.6534 0.0221  -0.0134 0.1058  99  TYR A CG  
820  C CD1 . TYR A 110 ? 0.7584 0.3851 0.6520 0.0235  -0.0270 0.1015  99  TYR A CD1 
821  C CD2 . TYR A 110 ? 0.7797 0.3611 0.6662 0.0290  -0.0040 0.1175  99  TYR A CD2 
822  C CE1 . TYR A 110 ? 0.7864 0.3944 0.6551 0.0313  -0.0323 0.1071  99  TYR A CE1 
823  C CE2 . TYR A 110 ? 0.8099 0.3699 0.6682 0.0375  -0.0092 0.1250  99  TYR A CE2 
824  C CZ  . TYR A 110 ? 0.8201 0.3945 0.6699 0.0386  -0.0239 0.1190  99  TYR A CZ  
825  O OH  . TYR A 110 ? 0.8603 0.4145 0.6838 0.0472  -0.0298 0.1243  99  TYR A OH  
826  N N   . ALA A 111 ? 0.7160 0.3926 0.6456 -0.0026 -0.0177 0.1095  100 ALA A N   
827  C CA  . ALA A 111 ? 0.7200 0.3899 0.6381 -0.0037 -0.0135 0.1210  100 ALA A CA  
828  C C   . ALA A 111 ? 0.7471 0.3823 0.6385 0.0045  -0.0118 0.1310  100 ALA A C   
829  O O   . ALA A 111 ? 0.7479 0.3819 0.6248 0.0070  -0.0202 0.1292  100 ALA A O   
830  C CB  . ALA A 111 ? 0.7090 0.4040 0.6236 -0.0092 -0.0199 0.1196  100 ALA A CB  
831  N N   . GLU A 112 ? 0.6586 0.5267 0.6020 -0.0242 -0.0019 0.0631  101 GLU A N   
832  C CA  . GLU A 112 ? 0.6696 0.5411 0.6013 -0.0261 -0.0034 0.0695  101 GLU A CA  
833  C C   . GLU A 112 ? 0.6722 0.5472 0.5914 -0.0262 -0.0054 0.0647  101 GLU A C   
834  O O   . GLU A 112 ? 0.6797 0.5562 0.5903 -0.0272 -0.0097 0.0692  101 GLU A O   
835  C CB  . GLU A 112 ? 0.7076 0.5794 0.6354 -0.0289 0.0015  0.0730  101 GLU A CB  
836  C CG  . GLU A 112 ? 0.7958 0.6688 0.7110 -0.0314 0.0007  0.0817  101 GLU A CG  
837  C CD  . GLU A 112 ? 0.9138 0.7853 0.8330 -0.0311 -0.0052 0.0912  101 GLU A CD  
838  O OE1 . GLU A 112 ? 0.9228 0.7914 0.8528 -0.0313 -0.0042 0.0978  101 GLU A OE1 
839  O OE2 . GLU A 112 ? 0.9596 0.8328 0.8724 -0.0309 -0.0111 0.0925  101 GLU A OE2 
840  N N   . HIS A 113 ? 0.6638 0.5397 0.5825 -0.0254 -0.0029 0.0559  102 HIS A N   
841  C CA  . HIS A 113 ? 0.6665 0.5450 0.5748 -0.0254 -0.0041 0.0506  102 HIS A CA  
842  C C   . HIS A 113 ? 0.6661 0.5447 0.5804 -0.0230 -0.0064 0.0445  102 HIS A C   
843  O O   . HIS A 113 ? 0.6668 0.5431 0.5917 -0.0213 -0.0057 0.0428  102 HIS A O   
844  C CB  . HIS A 113 ? 0.6732 0.5530 0.5752 -0.0267 0.0015  0.0463  102 HIS A CB  
845  C CG  . HIS A 113 ? 0.6996 0.5793 0.5959 -0.0290 0.0054  0.0523  102 HIS A CG  
846  N ND1 . HIS A 113 ? 0.7290 0.6084 0.6095 -0.0310 0.0046  0.0562  102 HIS A ND1 
847  C CD2 . HIS A 113 ? 0.7152 0.5944 0.6195 -0.0299 0.0097  0.0557  102 HIS A CD2 
848  C CE1 . HIS A 113 ? 0.7403 0.6193 0.6188 -0.0328 0.0093  0.0619  102 HIS A CE1 
849  N NE2 . HIS A 113 ? 0.7362 0.6154 0.6301 -0.0322 0.0125  0.0621  102 HIS A NE2 
850  N N   . ASP A 114 ? 0.6600 0.5406 0.5665 -0.0231 -0.0090 0.0413  103 ASP A N   
851  C CA  . ASP A 114 ? 0.6568 0.5380 0.5672 -0.0213 -0.0106 0.0358  103 ASP A CA  
852  C C   . ASP A 114 ? 0.6663 0.5488 0.5661 -0.0224 -0.0105 0.0307  103 ASP A C   
853  O O   . ASP A 114 ? 0.6731 0.5556 0.5618 -0.0245 -0.0096 0.0318  103 ASP A O   
854  C CB  . ASP A 114 ? 0.6662 0.5478 0.5837 -0.0199 -0.0153 0.0397  103 ASP A CB  
855  C CG  . ASP A 114 ? 0.7193 0.6030 0.6299 -0.0218 -0.0211 0.0446  103 ASP A CG  
856  O OD1 . ASP A 114 ? 0.7367 0.6213 0.6373 -0.0234 -0.0229 0.0410  103 ASP A OD1 
857  O OD2 . ASP A 114 ? 0.7476 0.6317 0.6635 -0.0218 -0.0245 0.0522  103 ASP A OD2 
858  N N   . LEU A 115 ? 0.6664 0.5495 0.5691 -0.0210 -0.0108 0.0250  104 LEU A N   
859  C CA  . LEU A 115 ? 0.6750 0.5585 0.5696 -0.0218 -0.0103 0.0198  104 LEU A CA  
860  C C   . LEU A 115 ? 0.6863 0.5697 0.5717 -0.0236 -0.0151 0.0207  104 LEU A C   
861  O O   . LEU A 115 ? 0.6842 0.5662 0.5596 -0.0249 -0.0140 0.0168  104 LEU A O   
862  C CB  . LEU A 115 ? 0.6731 0.5568 0.5740 -0.0201 -0.0094 0.0143  104 LEU A CB  
863  C CG  . LEU A 115 ? 0.6842 0.5681 0.5855 -0.0199 -0.0049 0.0099  104 LEU A CG  
864  C CD1 . LEU A 115 ? 0.6847 0.5687 0.5888 -0.0205 -0.0010 0.0124  104 LEU A CD1 
865  C CD2 . LEU A 115 ? 0.6916 0.5754 0.6002 -0.0185 -0.0054 0.0065  104 LEU A CD2 
866  N N   . TRP A 116 ? 0.6993 0.5837 0.5881 -0.0239 -0.0206 0.0261  105 TRP A N   
867  C CA  . TRP A 116 ? 0.7226 0.6069 0.6034 -0.0265 -0.0271 0.0279  105 TRP A CA  
868  C C   . TRP A 116 ? 0.7296 0.6116 0.5948 -0.0295 -0.0271 0.0307  105 TRP A C   
869  O O   . TRP A 116 ? 0.7391 0.6185 0.5899 -0.0321 -0.0286 0.0275  105 TRP A O   
870  C CB  . TRP A 116 ? 0.7322 0.6192 0.6248 -0.0258 -0.0330 0.0344  105 TRP A CB  
871  C CG  . TRP A 116 ? 0.7636 0.6514 0.6515 -0.0288 -0.0415 0.0370  105 TRP A CG  
872  C CD1 . TRP A 116 ? 0.7798 0.6691 0.6731 -0.0291 -0.0454 0.0348  105 TRP A CD1 
873  C CD2 . TRP A 116 ? 0.7803 0.6673 0.6577 -0.0325 -0.0480 0.0431  105 TRP A CD2 
874  N NE1 . TRP A 116 ? 0.7894 0.6788 0.6768 -0.0330 -0.0545 0.0386  105 TRP A NE1 
875  C CE2 . TRP A 116 ? 0.7914 0.6792 0.6677 -0.0352 -0.0565 0.0435  105 TRP A CE2 
876  C CE3 . TRP A 116 ? 0.7963 0.6817 0.6646 -0.0341 -0.0478 0.0485  105 TRP A CE3 
877  C CZ2 . TRP A 116 ? 0.8064 0.6930 0.6715 -0.0399 -0.0655 0.0489  105 TRP A CZ2 
878  C CZ3 . TRP A 116 ? 0.8123 0.6965 0.6683 -0.0385 -0.0560 0.0541  105 TRP A CZ3 
879  C CH2 . TRP A 116 ? 0.8131 0.6978 0.6673 -0.0414 -0.0653 0.0542  105 TRP A CH2 
880  N N   . HIS A 117 ? 0.7221 0.6043 0.5894 -0.0293 -0.0250 0.0365  106 HIS A N   
881  C CA  . HIS A 117 ? 0.7327 0.6127 0.5853 -0.0322 -0.0244 0.0406  106 HIS A CA  
882  C C   . HIS A 117 ? 0.7348 0.6125 0.5760 -0.0328 -0.0163 0.0347  106 HIS A C   
883  O O   . HIS A 117 ? 0.7486 0.6229 0.5715 -0.0357 -0.0159 0.0348  106 HIS A O   
884  C CB  . HIS A 117 ? 0.7516 0.6326 0.6121 -0.0317 -0.0243 0.0493  106 HIS A CB  
885  C CG  . HIS A 117 ? 0.7943 0.6770 0.6625 -0.0320 -0.0328 0.0570  106 HIS A CG  
886  N ND1 . HIS A 117 ? 0.8145 0.6991 0.7025 -0.0287 -0.0332 0.0592  106 HIS A ND1 
887  C CD2 . HIS A 117 ? 0.8143 0.6968 0.6733 -0.0353 -0.0410 0.0631  106 HIS A CD2 
888  C CE1 . HIS A 117 ? 0.8203 0.7067 0.7131 -0.0296 -0.0410 0.0668  106 HIS A CE1 
889  N NE2 . HIS A 117 ? 0.8223 0.7078 0.6983 -0.0338 -0.0468 0.0698  106 HIS A NE2 
890  N N   . ILE A 118 ? 0.7192 0.5981 0.5707 -0.0301 -0.0098 0.0298  107 ILE A N   
891  C CA  . ILE A 118 ? 0.7171 0.5947 0.5628 -0.0299 -0.0015 0.0245  107 ILE A CA  
892  C C   . ILE A 118 ? 0.7338 0.6085 0.5687 -0.0307 -0.0019 0.0173  107 ILE A C   
893  O O   . ILE A 118 ? 0.7455 0.6166 0.5657 -0.0322 0.0029  0.0147  107 ILE A O   
894  C CB  . ILE A 118 ? 0.7052 0.5855 0.5678 -0.0272 0.0031  0.0221  107 ILE A CB  
895  C CG1 . ILE A 118 ? 0.7018 0.5834 0.5730 -0.0272 0.0049  0.0284  107 ILE A CG1 
896  C CG2 . ILE A 118 ? 0.7077 0.5879 0.5698 -0.0263 0.0104  0.0158  107 ILE A CG2 
897  C CD1 . ILE A 118 ? 0.7036 0.5867 0.5906 -0.0254 0.0066  0.0264  107 ILE A CD1 
898  N N   . ILE A 119 ? 0.7339 0.6095 0.5758 -0.0296 -0.0071 0.0141  108 ILE A N   
899  C CA  . ILE A 119 ? 0.7498 0.6222 0.5838 -0.0305 -0.0084 0.0075  108 ILE A CA  
900  C C   . ILE A 119 ? 0.7793 0.6471 0.5939 -0.0345 -0.0134 0.0086  108 ILE A C   
901  O O   . ILE A 119 ? 0.7842 0.6465 0.5847 -0.0360 -0.0109 0.0027  108 ILE A O   
902  C CB  . ILE A 119 ? 0.7420 0.6167 0.5895 -0.0287 -0.0129 0.0051  108 ILE A CB  
903  C CG1 . ILE A 119 ? 0.7355 0.6126 0.5967 -0.0254 -0.0074 0.0020  108 ILE A CG1 
904  C CG2 . ILE A 119 ? 0.7523 0.6232 0.5918 -0.0305 -0.0171 0.0001  108 ILE A CG2 
905  C CD1 . ILE A 119 ? 0.7395 0.6187 0.6127 -0.0237 -0.0111 0.0012  108 ILE A CD1 
906  N N   . LYS A 120 ? 0.8014 0.6708 0.6151 -0.0364 -0.0206 0.0163  109 LYS A N   
907  C CA  . LYS A 120 ? 0.8356 0.7007 0.6303 -0.0410 -0.0273 0.0186  109 LYS A CA  
908  C C   . LYS A 120 ? 0.8629 0.7228 0.6372 -0.0431 -0.0204 0.0182  109 LYS A C   
909  O O   . LYS A 120 ? 0.8744 0.7276 0.6278 -0.0466 -0.0215 0.0142  109 LYS A O   
910  C CB  . LYS A 120 ? 0.8645 0.7332 0.6656 -0.0425 -0.0372 0.0283  109 LYS A CB  
911  C CG  . LYS A 120 ? 0.9466 0.8107 0.7272 -0.0481 -0.0458 0.0316  109 LYS A CG  
912  C CD  . LYS A 120 ? 1.0228 0.8908 0.8127 -0.0499 -0.0583 0.0405  109 LYS A CD  
913  C CE  . LYS A 120 ? 1.0914 0.9540 0.8606 -0.0563 -0.0687 0.0411  109 LYS A CE  
914  N NZ  . LYS A 120 ? 1.1191 0.9861 0.8976 -0.0587 -0.0820 0.0517  109 LYS A NZ  
915  N N   . PHE A 121 ? 0.8744 0.7369 0.6545 -0.0411 -0.0125 0.0216  110 PHE A N   
916  C CA  . PHE A 121 ? 0.9038 0.7624 0.6675 -0.0426 -0.0040 0.0221  110 PHE A CA  
917  C C   . PHE A 121 ? 0.9319 0.7853 0.6854 -0.0420 0.0046  0.0121  110 PHE A C   
918  O O   . PHE A 121 ? 0.9447 0.7911 0.6749 -0.0450 0.0082  0.0100  110 PHE A O   
919  C CB  . PHE A 121 ? 0.8978 0.7613 0.6760 -0.0401 0.0029  0.0275  110 PHE A CB  
920  C CG  . PHE A 121 ? 0.9147 0.7756 0.6793 -0.0417 0.0121  0.0304  110 PHE A CG  
921  C CD1 . PHE A 121 ? 0.9325 0.7917 0.6847 -0.0450 0.0089  0.0394  110 PHE A CD1 
922  C CD2 . PHE A 121 ? 0.9286 0.7890 0.6948 -0.0397 0.0243  0.0251  110 PHE A CD2 
923  C CE1 . PHE A 121 ? 0.9484 0.8052 0.6880 -0.0465 0.0183  0.0429  110 PHE A CE1 
924  C CE2 . PHE A 121 ? 0.9442 0.8027 0.6999 -0.0409 0.0342  0.0285  110 PHE A CE2 
925  C CZ  . PHE A 121 ? 0.9464 0.8030 0.6883 -0.0444 0.0314  0.0373  110 PHE A CZ  
926  N N   . HIS A 122 ? 0.9429 0.7990 0.7131 -0.0384 0.0079  0.0060  111 HIS A N   
927  C CA  . HIS A 122 ? 0.9689 0.8202 0.7338 -0.0371 0.0161  -0.0033 111 HIS A CA  
928  C C   . HIS A 122 ? 0.9985 0.8420 0.7456 -0.0403 0.0103  -0.0093 111 HIS A C   
929  O O   . HIS A 122 ? 1.0102 0.8457 0.7390 -0.0416 0.0170  -0.0154 111 HIS A O   
930  C CB  . HIS A 122 ? 0.9723 0.8288 0.7610 -0.0327 0.0192  -0.0069 111 HIS A CB  
931  C CG  . HIS A 122 ? 1.0057 0.8682 0.8097 -0.0302 0.0262  -0.0028 111 HIS A CG  
932  N ND1 . HIS A 122 ? 1.0358 0.8970 0.8337 -0.0302 0.0370  -0.0021 111 HIS A ND1 
933  C CD2 . HIS A 122 ? 1.0140 0.8831 0.8387 -0.0281 0.0238  0.0008  111 HIS A CD2 
934  C CE1 . HIS A 122 ? 1.0341 0.9018 0.8508 -0.0283 0.0400  0.0022  111 HIS A CE1 
935  N NE2 . HIS A 122 ? 1.0261 0.8982 0.8583 -0.0271 0.0319  0.0037  111 HIS A NE2 
936  N N   . ARG A 123 ? 1.0111 0.8563 0.7629 -0.0418 -0.0018 -0.0074 112 ARG A N   
937  C CA  . ARG A 123 ? 1.0387 0.8769 0.7759 -0.0457 -0.0098 -0.0121 112 ARG A CA  
938  C C   . ARG A 123 ? 1.0702 0.9004 0.7780 -0.0511 -0.0121 -0.0106 112 ARG A C   
939  O O   . ARG A 123 ? 1.0816 0.9020 0.7694 -0.0543 -0.0125 -0.0179 112 ARG A O   
940  C CB  . ARG A 123 ? 1.0493 0.8928 0.8012 -0.0463 -0.0224 -0.0079 112 ARG A CB  
941  C CG  . ARG A 123 ? 1.0872 0.9295 0.8489 -0.0452 -0.0244 -0.0148 112 ARG A CG  
942  C CD  . ARG A 123 ? 1.1393 0.9846 0.9092 -0.0475 -0.0373 -0.0109 112 ARG A CD  
943  N NE  . ARG A 123 ? 1.2091 1.0488 0.9773 -0.0491 -0.0405 -0.0184 112 ARG A NE  
944  C CZ  . ARG A 123 ? 1.2546 1.0953 1.0292 -0.0519 -0.0514 -0.0167 112 ARG A CZ  
945  N NH1 . ARG A 123 ? 1.2519 1.0868 1.0252 -0.0535 -0.0537 -0.0238 112 ARG A NH1 
946  N NH2 . ARG A 123 ? 1.2594 1.1071 1.0436 -0.0529 -0.0600 -0.0075 112 ARG A NH2 
947  N N   . ALA A 124 ? 1.0825 0.9162 0.7870 -0.0523 -0.0138 -0.0012 113 ALA A N   
948  C CA  . ALA A 124 ? 1.1162 0.9426 0.7920 -0.0578 -0.0165 0.0019  113 ALA A CA  
949  C C   . ALA A 124 ? 1.1532 0.9715 0.8092 -0.0576 -0.0019 -0.0048 113 ALA A C   
950  O O   . ALA A 124 ? 1.1703 0.9775 0.7983 -0.0620 -0.0023 -0.0101 113 ALA A O   
951  C CB  . ALA A 124 ? 1.1125 0.9450 0.7927 -0.0586 -0.0210 0.0146  113 ALA A CB  
952  N N   . SER A 125 ? 1.1620 0.9853 0.8335 -0.0526 0.0111  -0.0052 114 SER A N   
953  C CA  . SER A 125 ? 1.1885 1.0060 0.8478 -0.0513 0.0271  -0.0105 114 SER A CA  
954  C C   . SER A 125 ? 1.2149 1.0223 0.8618 -0.0513 0.0323  -0.0232 114 SER A C   
955  O O   . SER A 125 ? 1.2293 1.0269 0.8523 -0.0529 0.0422  -0.0280 114 SER A O   
956  C CB  . SER A 125 ? 1.1956 1.0224 0.8813 -0.0458 0.0376  -0.0081 114 SER A CB  
957  O OG  . SER A 125 ? 1.2225 1.0559 0.9150 -0.0463 0.0357  0.0030  114 SER A OG  
958  N N   . LYS A 126 ? 1.2211 1.0298 0.8833 -0.0497 0.0261  -0.0285 115 LYS A N   
959  C CA  . LYS A 126 ? 1.2456 1.0441 0.8988 -0.0496 0.0300  -0.0404 115 LYS A CA  
960  C C   . LYS A 126 ? 1.2769 1.0624 0.8962 -0.0565 0.0228  -0.0443 115 LYS A C   
961  O O   . LYS A 126 ? 1.2906 1.0636 0.8882 -0.0577 0.0316  -0.0535 115 LYS A O   
962  C CB  . LYS A 126 ? 1.2605 1.0641 0.9394 -0.0467 0.0236  -0.0435 115 LYS A CB  
963  C CG  . LYS A 126 ? 1.2941 1.1097 1.0046 -0.0406 0.0294  -0.0398 115 LYS A CG  
964  C CD  . LYS A 126 ? 1.3325 1.1509 1.0650 -0.0375 0.0264  -0.0440 115 LYS A CD  
965  C CE  . LYS A 126 ? 1.3675 1.1943 1.1249 -0.0319 0.0352  -0.0424 115 LYS A CE  
966  N NZ  . LYS A 126 ? 1.3953 1.2248 1.1736 -0.0289 0.0324  -0.0455 115 LYS A NZ  
967  N N   . ALA A 127 ? 1.2850 1.0731 0.8998 -0.0611 0.0069  -0.0371 116 ALA A N   
968  C CA  . ALA A 127 ? 1.3105 1.0871 0.8939 -0.0687 -0.0034 -0.0391 116 ALA A CA  
969  C C   . ALA A 127 ? 1.3352 1.1030 0.8852 -0.0724 0.0036  -0.0376 116 ALA A C   
970  O O   . ALA A 127 ? 1.3535 1.1074 0.8711 -0.0784 0.0002  -0.0433 116 ALA A O   
971  C CB  . ALA A 127 ? 1.3063 1.0900 0.8987 -0.0722 -0.0223 -0.0298 116 ALA A CB  
972  N N   . ASN A 128 ? 1.3335 1.1087 0.8905 -0.0693 0.0130  -0.0299 117 ASN A N   
973  C CA  . ASN A 128 ? 1.3546 1.1227 0.8821 -0.0724 0.0211  -0.0269 117 ASN A CA  
974  C C   . ASN A 128 ? 1.3631 1.1253 0.8854 -0.0683 0.0428  -0.0354 117 ASN A C   
975  O O   . ASN A 128 ? 1.3698 1.1230 0.8869 -0.0672 0.0487  -0.0476 117 ASN A O   
976  C CB  . ASN A 128 ? 1.3633 1.1428 0.9024 -0.0720 0.0181  -0.0123 117 ASN A CB  
977  C CG  . ASN A 128 ? 1.3949 1.1811 0.9437 -0.0751 -0.0018 -0.0030 117 ASN A CG  
978  O OD1 . ASN A 128 ? 1.4119 1.1919 0.9459 -0.0804 -0.0153 -0.0050 117 ASN A OD1 
979  N ND2 . ASN A 128 ? 1.3896 1.1886 0.9646 -0.0719 -0.0040 0.0075  117 ASN A ND2 
980  N N   . LEU A 134 ? 1.0368 0.9137 0.8932 -0.0218 0.0661  -0.0004 123 LEU A N   
981  C CA  . LEU A 134 ? 1.0330 0.9153 0.9123 -0.0196 0.0611  -0.0013 123 LEU A CA  
982  C C   . LEU A 134 ? 1.0287 0.9164 0.9287 -0.0176 0.0700  0.0001  123 LEU A C   
983  O O   . LEU A 134 ? 1.0316 0.9189 0.9388 -0.0151 0.0755  -0.0046 123 LEU A O   
984  C CB  . LEU A 134 ? 1.0381 0.9169 0.9150 -0.0182 0.0568  -0.0083 123 LEU A CB  
985  C CG  . LEU A 134 ? 1.0702 0.9433 0.9274 -0.0204 0.0491  -0.0104 123 LEU A CG  
986  C CD1 . LEU A 134 ? 1.0839 0.9499 0.9288 -0.0200 0.0526  -0.0182 123 LEU A CD1 
987  C CD2 . LEU A 134 ? 1.0794 0.9553 0.9450 -0.0204 0.0376  -0.0089 123 LEU A CD2 
988  N N   . PRO A 135 ? 1.0171 0.9098 0.9290 -0.0188 0.0712  0.0068  124 PRO A N   
989  C CA  . PRO A 135 ? 1.0005 0.8995 0.9356 -0.0173 0.0785  0.0090  124 PRO A CA  
990  C C   . PRO A 135 ? 0.9835 0.8859 0.9377 -0.0152 0.0732  0.0062  124 PRO A C   
991  O O   . PRO A 135 ? 0.9920 0.8934 0.9446 -0.0156 0.0624  0.0047  124 PRO A O   
992  C CB  . PRO A 135 ? 1.0073 0.9103 0.9520 -0.0198 0.0761  0.0167  124 PRO A CB  
993  C CG  . PRO A 135 ? 1.0246 0.9229 0.9487 -0.0222 0.0715  0.0190  124 PRO A CG  
994  C CD  . PRO A 135 ? 1.0139 0.9070 0.9214 -0.0215 0.0654  0.0130  124 PRO A CD  
995  N N   . ARG A 136 ? 0.9562 0.8626 0.9287 -0.0128 0.0810  0.0058  125 ARG A N   
996  C CA  . ARG A 136 ? 0.9348 0.8451 0.9281 -0.0107 0.0769  0.0045  125 ARG A CA  
997  C C   . ARG A 136 ? 0.9090 0.8180 0.9001 -0.0115 0.0627  0.0026  125 ARG A C   
998  O O   . ARG A 136 ? 0.9173 0.8223 0.9013 -0.0099 0.0606  -0.0025 125 ARG A O   
999  C CB  . ARG A 136 ? 0.9492 0.8680 0.9702 -0.0111 0.0790  0.0107  125 ARG A CB  
1000 C CG  . ARG A 136 ? 0.9979 0.9192 1.0253 -0.0101 0.0942  0.0133  125 ARG A CG  
1001 C CD  . ARG A 136 ? 1.0297 0.9532 1.0739 -0.0059 0.1038  0.0109  125 ARG A CD  
1002 N NE  . ARG A 136 ? 1.0423 0.9739 1.1172 -0.0055 0.0974  0.0150  125 ARG A NE  
1003 C CZ  . ARG A 136 ? 1.0594 0.9911 1.1427 -0.0038 0.0898  0.0125  125 ARG A CZ  
1004 N NH1 . ARG A 136 ? 1.0615 0.9857 1.1260 -0.0022 0.0881  0.0057  125 ARG A NH1 
1005 N NH2 . ARG A 136 ? 1.0417 0.9809 1.1526 -0.0041 0.0833  0.0174  125 ARG A NH2 
1006 N N   . GLY A 137 ? 0.8723 0.7837 0.8687 -0.0141 0.0537  0.0066  126 GLY A N   
1007 C CA  . GLY A 137 ? 0.8406 0.7503 0.8346 -0.0149 0.0419  0.0052  126 GLY A CA  
1008 C C   . GLY A 137 ? 0.8033 0.7093 0.7822 -0.0171 0.0358  0.0061  126 GLY A C   
1009 O O   . GLY A 137 ? 0.8026 0.7087 0.7856 -0.0188 0.0276  0.0075  126 GLY A O   
1010 N N   . MET A 138 ? 0.7709 0.6733 0.7325 -0.0174 0.0397  0.0054  127 MET A N   
1011 C CA  . MET A 138 ? 0.7467 0.6458 0.6957 -0.0191 0.0339  0.0069  127 MET A CA  
1012 C C   . MET A 138 ? 0.7219 0.6182 0.6646 -0.0184 0.0264  0.0033  127 MET A C   
1013 O O   . MET A 138 ? 0.7256 0.6208 0.6680 -0.0193 0.0198  0.0045  127 MET A O   
1014 C CB  . MET A 138 ? 0.7545 0.6507 0.6871 -0.0200 0.0390  0.0083  127 MET A CB  
1015 C CG  . MET A 138 ? 0.7751 0.6688 0.6987 -0.0216 0.0324  0.0112  127 MET A CG  
1016 S SD  . MET A 138 ? 0.8234 0.7134 0.7262 -0.0231 0.0353  0.0137  127 MET A SD  
1017 C CE  . MET A 138 ? 0.8033 0.6909 0.7004 -0.0236 0.0249  0.0148  127 MET A CE  
1018 N N   . VAL A 139 ? 0.6956 0.5903 0.6339 -0.0167 0.0279  -0.0012 128 VAL A N   
1019 C CA  . VAL A 139 ? 0.6750 0.5673 0.6091 -0.0160 0.0215  -0.0043 128 VAL A CA  
1020 C C   . VAL A 139 ? 0.6457 0.5403 0.5928 -0.0159 0.0159  -0.0035 128 VAL A C   
1021 O O   . VAL A 139 ? 0.6463 0.5393 0.5901 -0.0165 0.0097  -0.0033 128 VAL A O   
1022 C CB  . VAL A 139 ? 0.6813 0.5709 0.6101 -0.0145 0.0251  -0.0092 128 VAL A CB  
1023 C CG1 . VAL A 139 ? 0.6846 0.5726 0.6138 -0.0138 0.0188  -0.0118 128 VAL A CG1 
1024 C CG2 . VAL A 139 ? 0.6945 0.5800 0.6056 -0.0156 0.0288  -0.0105 128 VAL A CG2 
1025 N N   . LYS A 140 ? 0.6179 0.5161 0.5797 -0.0153 0.0181  -0.0025 129 LYS A N   
1026 C CA  . LYS A 140 ? 0.6042 0.5043 0.5778 -0.0159 0.0118  -0.0010 129 LYS A CA  
1027 C C   . LYS A 140 ? 0.6011 0.5004 0.5739 -0.0185 0.0067  0.0016  129 LYS A C   
1028 O O   . LYS A 140 ? 0.6090 0.5059 0.5795 -0.0194 0.0002  0.0012  129 LYS A O   
1029 C CB  . LYS A 140 ? 0.6039 0.5089 0.5958 -0.0151 0.0148  0.0007  129 LYS A CB  
1030 C CG  . LYS A 140 ? 0.6134 0.5203 0.6171 -0.0164 0.0065  0.0029  129 LYS A CG  
1031 C CD  . LYS A 140 ? 0.6249 0.5377 0.6502 -0.0160 0.0084  0.0061  129 LYS A CD  
1032 C CE  . LYS A 140 ? 0.6444 0.5586 0.6765 -0.0124 0.0164  0.0042  129 LYS A CE  
1033 N NZ  . LYS A 140 ? 0.6474 0.5672 0.7032 -0.0115 0.0154  0.0078  129 LYS A NZ  
1034 N N   . SER A 141 ? 0.5885 0.4887 0.5625 -0.0198 0.0102  0.0043  130 SER A N   
1035 C CA  . SER A 141 ? 0.5891 0.4872 0.5629 -0.0223 0.0060  0.0065  130 SER A CA  
1036 C C   . SER A 141 ? 0.5864 0.4795 0.5464 -0.0220 0.0028  0.0050  130 SER A C   
1037 O O   . SER A 141 ? 0.5890 0.4786 0.5479 -0.0233 -0.0022 0.0048  130 SER A O   
1038 C CB  . SER A 141 ? 0.6119 0.5119 0.5900 -0.0236 0.0111  0.0102  130 SER A CB  
1039 O OG  . SER A 141 ? 0.6414 0.5467 0.6344 -0.0236 0.0153  0.0122  130 SER A OG  
1040 N N   . LEU A 142 ? 0.5755 0.4678 0.5252 -0.0205 0.0057  0.0040  131 LEU A N   
1041 C CA  . LEU A 142 ? 0.5706 0.4593 0.5102 -0.0201 0.0027  0.0034  131 LEU A CA  
1042 C C   . LEU A 142 ? 0.5670 0.4542 0.5061 -0.0193 -0.0017 0.0007  131 LEU A C   
1043 O O   . LEU A 142 ? 0.5781 0.4621 0.5146 -0.0196 -0.0048 0.0007  131 LEU A O   
1044 C CB  . LEU A 142 ? 0.5707 0.4592 0.5002 -0.0193 0.0054  0.0032  131 LEU A CB  
1045 C CG  . LEU A 142 ? 0.5771 0.4657 0.5023 -0.0204 0.0089  0.0069  131 LEU A CG  
1046 C CD1 . LEU A 142 ? 0.5838 0.4718 0.4974 -0.0202 0.0113  0.0060  131 LEU A CD1 
1047 C CD2 . LEU A 142 ? 0.5812 0.4676 0.5060 -0.0210 0.0059  0.0102  131 LEU A CD2 
1048 N N   . LEU A 143 ? 0.5509 0.4400 0.4934 -0.0184 -0.0016 -0.0012 132 LEU A N   
1049 C CA  . LEU A 143 ? 0.5435 0.4313 0.4860 -0.0179 -0.0058 -0.0028 132 LEU A CA  
1050 C C   . LEU A 143 ? 0.5306 0.4165 0.4763 -0.0197 -0.0102 -0.0020 132 LEU A C   
1051 O O   . LEU A 143 ? 0.5317 0.4139 0.4713 -0.0199 -0.0128 -0.0027 132 LEU A O   
1052 C CB  . LEU A 143 ? 0.5420 0.4318 0.4891 -0.0166 -0.0049 -0.0044 132 LEU A CB  
1053 C CG  . LEU A 143 ? 0.5628 0.4510 0.5092 -0.0162 -0.0092 -0.0052 132 LEU A CG  
1054 C CD1 . LEU A 143 ? 0.5783 0.4639 0.5154 -0.0158 -0.0100 -0.0059 132 LEU A CD1 
1055 C CD2 . LEU A 143 ? 0.5627 0.4525 0.5163 -0.0148 -0.0084 -0.0061 132 LEU A CD2 
1056 N N   . TYR A 144 ? 0.5171 0.4053 0.4724 -0.0212 -0.0110 -0.0005 133 TYR A N   
1057 C CA  . TYR A 144 ? 0.5144 0.4001 0.4721 -0.0238 -0.0165 0.0002  133 TYR A CA  
1058 C C   . TYR A 144 ? 0.5159 0.3957 0.4653 -0.0251 -0.0173 -0.0005 133 TYR A C   
1059 O O   . TYR A 144 ? 0.5235 0.3981 0.4672 -0.0265 -0.0214 -0.0018 133 TYR A O   
1060 C CB  . TYR A 144 ? 0.5067 0.3964 0.4785 -0.0257 -0.0175 0.0028  133 TYR A CB  
1061 C CG  . TYR A 144 ? 0.5245 0.4116 0.4987 -0.0291 -0.0254 0.0035  133 TYR A CG  
1062 C CD1 . TYR A 144 ? 0.5469 0.4346 0.5228 -0.0294 -0.0306 0.0040  133 TYR A CD1 
1063 C CD2 . TYR A 144 ? 0.5436 0.4268 0.5176 -0.0324 -0.0283 0.0038  133 TYR A CD2 
1064 C CE1 . TYR A 144 ? 0.5628 0.4470 0.5379 -0.0332 -0.0390 0.0049  133 TYR A CE1 
1065 C CE2 . TYR A 144 ? 0.5637 0.4430 0.5373 -0.0363 -0.0365 0.0039  133 TYR A CE2 
1066 C CZ  . TYR A 144 ? 0.5806 0.4604 0.5539 -0.0368 -0.0421 0.0046  133 TYR A CZ  
1067 O OH  . TYR A 144 ? 0.6099 0.4853 0.5809 -0.0413 -0.0514 0.0051  133 TYR A OH  
1068 N N   . GLN A 145 ? 0.5072 0.3870 0.4555 -0.0245 -0.0132 0.0005  134 GLN A N   
1069 C CA  . GLN A 145 ? 0.5099 0.3838 0.4530 -0.0252 -0.0133 0.0002  134 GLN A CA  
1070 C C   . GLN A 145 ? 0.5101 0.3805 0.4439 -0.0232 -0.0126 -0.0014 134 GLN A C   
1071 O O   . GLN A 145 ? 0.5151 0.3791 0.4438 -0.0238 -0.0137 -0.0031 134 GLN A O   
1072 C CB  . GLN A 145 ? 0.5307 0.4059 0.4775 -0.0255 -0.0096 0.0031  134 GLN A CB  
1073 C CG  . GLN A 145 ? 0.5672 0.4453 0.5250 -0.0280 -0.0098 0.0053  134 GLN A CG  
1074 C CD  . GLN A 145 ? 0.5982 0.4758 0.5594 -0.0290 -0.0066 0.0086  134 GLN A CD  
1075 O OE1 . GLN A 145 ? 0.6194 0.4914 0.5767 -0.0292 -0.0069 0.0088  134 GLN A OE1 
1076 N NE2 . GLN A 145 ? 0.5817 0.4648 0.5512 -0.0297 -0.0030 0.0118  134 GLN A NE2 
1077 N N   . ILE A 146 ? 0.5009 0.3751 0.4327 -0.0209 -0.0108 -0.0013 135 ILE A N   
1078 C CA  . ILE A 146 ? 0.5035 0.3757 0.4294 -0.0191 -0.0103 -0.0021 135 ILE A CA  
1079 C C   . ILE A 146 ? 0.5219 0.3905 0.4439 -0.0197 -0.0128 -0.0041 135 ILE A C   
1080 O O   . ILE A 146 ? 0.5309 0.3945 0.4477 -0.0191 -0.0118 -0.0050 135 ILE A O   
1081 C CB  . ILE A 146 ? 0.4968 0.3735 0.4222 -0.0176 -0.0092 -0.0016 135 ILE A CB  
1082 C CG1 . ILE A 146 ? 0.5030 0.3816 0.4282 -0.0174 -0.0071 0.0008  135 ILE A CG1 
1083 C CG2 . ILE A 146 ? 0.4963 0.3721 0.4186 -0.0162 -0.0097 -0.0021 135 ILE A CG2 
1084 C CD1 . ILE A 146 ? 0.5090 0.3909 0.4316 -0.0169 -0.0064 0.0006  135 ILE A CD1 
1085 N N   . LEU A 147 ? 0.5265 0.3975 0.4514 -0.0207 -0.0157 -0.0043 136 LEU A N   
1086 C CA  . LEU A 147 ? 0.5331 0.4012 0.4540 -0.0218 -0.0192 -0.0051 136 LEU A CA  
1087 C C   . LEU A 147 ? 0.5413 0.4024 0.4566 -0.0244 -0.0216 -0.0064 136 LEU A C   
1088 O O   . LEU A 147 ? 0.5460 0.4013 0.4519 -0.0247 -0.0216 -0.0079 136 LEU A O   
1089 C CB  . LEU A 147 ? 0.5347 0.4075 0.4631 -0.0224 -0.0223 -0.0040 136 LEU A CB  
1090 C CG  . LEU A 147 ? 0.5496 0.4264 0.4809 -0.0201 -0.0207 -0.0037 136 LEU A CG  
1091 C CD1 . LEU A 147 ? 0.5468 0.4282 0.4888 -0.0201 -0.0220 -0.0026 136 LEU A CD1 
1092 C CD2 . LEU A 147 ? 0.5590 0.4328 0.4834 -0.0197 -0.0218 -0.0037 136 LEU A CD2 
1093 N N   . ASP A 148 ? 0.5455 0.4065 0.4660 -0.0264 -0.0230 -0.0061 137 ASP A N   
1094 C CA  . ASP A 148 ? 0.5634 0.4168 0.4793 -0.0296 -0.0258 -0.0078 137 ASP A CA  
1095 C C   . ASP A 148 ? 0.5828 0.4280 0.4892 -0.0284 -0.0216 -0.0103 137 ASP A C   
1096 O O   . ASP A 148 ? 0.5943 0.4307 0.4901 -0.0302 -0.0231 -0.0132 137 ASP A O   
1097 C CB  . ASP A 148 ? 0.5741 0.4303 0.5008 -0.0315 -0.0267 -0.0061 137 ASP A CB  
1098 C CG  . ASP A 148 ? 0.6405 0.4902 0.5662 -0.0360 -0.0320 -0.0073 137 ASP A CG  
1099 O OD1 . ASP A 148 ? 0.6581 0.4998 0.5721 -0.0380 -0.0355 -0.0101 137 ASP A OD1 
1100 O OD2 . ASP A 148 ? 0.6711 0.5231 0.6071 -0.0378 -0.0328 -0.0055 137 ASP A OD2 
1101 N N   . GLY A 149 ? 0.5835 0.4310 0.4936 -0.0255 -0.0165 -0.0092 138 GLY A N   
1102 C CA  . GLY A 149 ? 0.5955 0.4364 0.5009 -0.0237 -0.0119 -0.0106 138 GLY A CA  
1103 C C   . GLY A 149 ? 0.6090 0.4472 0.5064 -0.0218 -0.0093 -0.0119 138 GLY A C   
1104 O O   . GLY A 149 ? 0.6184 0.4477 0.5078 -0.0217 -0.0064 -0.0148 138 GLY A O   
1105 N N   . ILE A 150 ? 0.6037 0.4492 0.5034 -0.0203 -0.0097 -0.0099 139 ILE A N   
1106 C CA  . ILE A 150 ? 0.6008 0.4452 0.4950 -0.0187 -0.0073 -0.0101 139 ILE A CA  
1107 C C   . ILE A 150 ? 0.6059 0.4437 0.4886 -0.0213 -0.0099 -0.0123 139 ILE A C   
1108 O O   . ILE A 150 ? 0.6162 0.4478 0.4899 -0.0206 -0.0061 -0.0137 139 ILE A O   
1109 C CB  . ILE A 150 ? 0.6016 0.4549 0.5023 -0.0172 -0.0081 -0.0074 139 ILE A CB  
1110 C CG1 . ILE A 150 ? 0.6207 0.4783 0.5289 -0.0149 -0.0053 -0.0053 139 ILE A CG1 
1111 C CG2 . ILE A 150 ? 0.6033 0.4560 0.4993 -0.0166 -0.0073 -0.0070 139 ILE A CG2 
1112 C CD1 . ILE A 150 ? 0.6411 0.4952 0.5495 -0.0125 -0.0001 -0.0047 139 ILE A CD1 
1113 N N   . HIS A 151 ? 0.5971 0.4356 0.4799 -0.0245 -0.0163 -0.0123 140 HIS A N   
1114 C CA  . HIS A 151 ? 0.6010 0.4331 0.4726 -0.0279 -0.0209 -0.0136 140 HIS A CA  
1115 C C   . HIS A 151 ? 0.6044 0.4242 0.4631 -0.0296 -0.0188 -0.0179 140 HIS A C   
1116 O O   . HIS A 151 ? 0.6115 0.4235 0.4556 -0.0310 -0.0185 -0.0196 140 HIS A O   
1117 C CB  . HIS A 151 ? 0.6090 0.4456 0.4878 -0.0310 -0.0287 -0.0119 140 HIS A CB  
1118 C CG  . HIS A 151 ? 0.6509 0.4805 0.5191 -0.0356 -0.0357 -0.0127 140 HIS A CG  
1119 N ND1 . HIS A 151 ? 0.6821 0.5052 0.5474 -0.0395 -0.0398 -0.0150 140 HIS A ND1 
1120 C CD2 . HIS A 151 ? 0.6692 0.4965 0.5281 -0.0373 -0.0396 -0.0113 140 HIS A CD2 
1121 C CE1 . HIS A 151 ? 0.6951 0.5123 0.5490 -0.0437 -0.0469 -0.0152 140 HIS A CE1 
1122 N NE2 . HIS A 151 ? 0.6916 0.5112 0.5408 -0.0425 -0.0469 -0.0127 140 HIS A NE2 
1123 N N   . TYR A 152 ? 0.5985 0.4156 0.4620 -0.0296 -0.0171 -0.0195 141 TYR A N   
1124 C CA  . TYR A 152 ? 0.6074 0.4117 0.4608 -0.0309 -0.0144 -0.0242 141 TYR A CA  
1125 C C   . TYR A 152 ? 0.6119 0.4112 0.4593 -0.0270 -0.0048 -0.0258 141 TYR A C   
1126 O O   . TYR A 152 ? 0.6215 0.4084 0.4544 -0.0280 -0.0014 -0.0302 141 TYR A O   
1127 C CB  . TYR A 152 ? 0.6069 0.4114 0.4713 -0.0312 -0.0145 -0.0242 141 TYR A CB  
1128 C CG  . TYR A 152 ? 0.6357 0.4270 0.4929 -0.0314 -0.0099 -0.0289 141 TYR A CG  
1129 C CD1 . TYR A 152 ? 0.6591 0.4375 0.5022 -0.0361 -0.0136 -0.0340 141 TYR A CD1 
1130 C CD2 . TYR A 152 ? 0.6476 0.4382 0.5115 -0.0269 -0.0018 -0.0284 141 TYR A CD2 
1131 C CE1 . TYR A 152 ? 0.6759 0.4403 0.5115 -0.0362 -0.0086 -0.0393 141 TYR A CE1 
1132 C CE2 . TYR A 152 ? 0.6651 0.4428 0.5241 -0.0266 0.0034  -0.0328 141 TYR A CE2 
1133 C CZ  . TYR A 152 ? 0.6851 0.4491 0.5294 -0.0311 0.0005  -0.0388 141 TYR A CZ  
1134 O OH  . TYR A 152 ? 0.7100 0.4593 0.5482 -0.0307 0.0063  -0.0441 141 TYR A OH  
1135 N N   . LEU A 153 ? 0.5982 0.4067 0.4573 -0.0226 -0.0003 -0.0221 142 LEU A N   
1136 C CA  . LEU A 153 ? 0.5947 0.4010 0.4533 -0.0187 0.0085  -0.0221 142 LEU A CA  
1137 C C   . LEU A 153 ? 0.6050 0.4086 0.4509 -0.0193 0.0097  -0.0224 142 LEU A C   
1138 O O   . LEU A 153 ? 0.6073 0.4011 0.4417 -0.0187 0.0162  -0.0254 142 LEU A O   
1139 C CB  . LEU A 153 ? 0.5806 0.3985 0.4560 -0.0149 0.0104  -0.0171 142 LEU A CB  
1140 C CG  . LEU A 153 ? 0.5809 0.4013 0.4680 -0.0140 0.0100  -0.0156 142 LEU A CG  
1141 C CD1 . LEU A 153 ? 0.5758 0.4069 0.4761 -0.0112 0.0106  -0.0104 142 LEU A CD1 
1142 C CD2 . LEU A 153 ? 0.5855 0.3953 0.4713 -0.0128 0.0159  -0.0184 142 LEU A CD2 
1143 N N   . HIS A 154 ? 0.6135 0.4250 0.4611 -0.0206 0.0038  -0.0193 143 HIS A N   
1144 C CA  . HIS A 154 ? 0.6318 0.4417 0.4688 -0.0216 0.0040  -0.0182 143 HIS A CA  
1145 C C   . HIS A 154 ? 0.6606 0.4580 0.4768 -0.0258 0.0016  -0.0220 143 HIS A C   
1146 O O   . HIS A 154 ? 0.6710 0.4615 0.4732 -0.0258 0.0065  -0.0227 143 HIS A O   
1147 C CB  . HIS A 154 ? 0.6257 0.4466 0.4717 -0.0220 -0.0023 -0.0137 143 HIS A CB  
1148 C CG  . HIS A 154 ? 0.6306 0.4615 0.4920 -0.0183 0.0007  -0.0104 143 HIS A CG  
1149 N ND1 . HIS A 154 ? 0.6401 0.4799 0.5105 -0.0183 -0.0039 -0.0073 143 HIS A ND1 
1150 C CD2 . HIS A 154 ? 0.6422 0.4749 0.5115 -0.0149 0.0073  -0.0097 143 HIS A CD2 
1151 C CE1 . HIS A 154 ? 0.6424 0.4883 0.5237 -0.0155 -0.0006 -0.0054 143 HIS A CE1 
1152 N NE2 . HIS A 154 ? 0.6442 0.4868 0.5260 -0.0135 0.0057  -0.0062 143 HIS A NE2 
1153 N N   . ALA A 155 ? 0.6694 0.4626 0.4827 -0.0295 -0.0054 -0.0246 144 ALA A N   
1154 C CA  . ALA A 155 ? 0.6907 0.4706 0.4834 -0.0345 -0.0092 -0.0287 144 ALA A CA  
1155 C C   . ALA A 155 ? 0.7194 0.4857 0.4981 -0.0330 0.0012  -0.0341 144 ALA A C   
1156 O O   . ALA A 155 ? 0.7332 0.4892 0.4912 -0.0350 0.0035  -0.0364 144 ALA A O   
1157 C CB  . ALA A 155 ? 0.6876 0.4664 0.4843 -0.0386 -0.0183 -0.0301 144 ALA A CB  
1158 N N   . ASN A 156 ? 0.7294 0.4963 0.5205 -0.0290 0.0084  -0.0355 145 ASN A N   
1159 C CA  . ASN A 156 ? 0.7545 0.5100 0.5385 -0.0262 0.0199  -0.0401 145 ASN A CA  
1160 C C   . ASN A 156 ? 0.7710 0.5315 0.5606 -0.0209 0.0305  -0.0368 145 ASN A C   
1161 O O   . ASN A 156 ? 0.7717 0.5281 0.5665 -0.0169 0.0407  -0.0384 145 ASN A O   
1162 C CB  . ASN A 156 ? 0.7636 0.5179 0.5613 -0.0243 0.0219  -0.0418 145 ASN A CB  
1163 C CG  . ASN A 156 ? 0.8142 0.5601 0.6050 -0.0296 0.0139  -0.0460 145 ASN A CG  
1164 O OD1 . ASN A 156 ? 0.8463 0.5771 0.6165 -0.0335 0.0135  -0.0520 145 ASN A OD1 
1165 N ND2 . ASN A 156 ? 0.8156 0.5707 0.6231 -0.0304 0.0073  -0.0428 145 ASN A ND2 
1166 N N   . TRP A 157 ? 0.7805 0.5506 0.5723 -0.0208 0.0278  -0.0316 146 TRP A N   
1167 C CA  . TRP A 157 ? 0.7926 0.5683 0.5908 -0.0167 0.0365  -0.0277 146 TRP A CA  
1168 C C   . TRP A 157 ? 0.7566 0.5400 0.5771 -0.0114 0.0430  -0.0251 146 TRP A C   
1169 O O   . TRP A 157 ? 0.7559 0.5385 0.5804 -0.0076 0.0535  -0.0239 146 TRP A O   
1170 C CB  . TRP A 157 ? 0.8312 0.5935 0.6080 -0.0170 0.0458  -0.0311 146 TRP A CB  
1171 C CG  . TRP A 157 ? 0.8849 0.6406 0.6390 -0.0227 0.0382  -0.0320 146 TRP A CG  
1172 C CD1 . TRP A 157 ? 0.9208 0.6627 0.6537 -0.0277 0.0334  -0.0378 146 TRP A CD1 
1173 C CD2 . TRP A 157 ? 0.8992 0.6621 0.6513 -0.0245 0.0327  -0.0263 146 TRP A CD2 
1174 N NE1 . TRP A 157 ? 0.9393 0.6796 0.6561 -0.0325 0.0252  -0.0356 146 TRP A NE1 
1175 C CE2 . TRP A 157 ? 0.9275 0.6807 0.6563 -0.0304 0.0250  -0.0283 146 TRP A CE2 
1176 C CE3 . TRP A 157 ? 0.9008 0.6769 0.6688 -0.0219 0.0334  -0.0195 146 TRP A CE3 
1177 C CZ2 . TRP A 157 ? 0.9398 0.6962 0.6611 -0.0334 0.0184  -0.0230 146 TRP A CZ2 
1178 C CZ3 . TRP A 157 ? 0.9203 0.6990 0.6811 -0.0247 0.0275  -0.0149 146 TRP A CZ3 
1179 C CH2 . TRP A 157 ? 0.9347 0.7040 0.6729 -0.0302 0.0201  -0.0164 146 TRP A CH2 
1180 N N   . VAL A 158 ? 0.7236 0.5150 0.5592 -0.0112 0.0365  -0.0234 147 VAL A N   
1181 C CA  . VAL A 158 ? 0.6918 0.4912 0.5484 -0.0070 0.0399  -0.0200 147 VAL A CA  
1182 C C   . VAL A 158 ? 0.6612 0.4752 0.5313 -0.0069 0.0330  -0.0144 147 VAL A C   
1183 O O   . VAL A 158 ? 0.6546 0.4726 0.5240 -0.0098 0.0243  -0.0142 147 VAL A O   
1184 C CB  . VAL A 158 ? 0.6894 0.4842 0.5507 -0.0071 0.0386  -0.0226 147 VAL A CB  
1185 C CG1 . VAL A 158 ? 0.6794 0.4845 0.5624 -0.0038 0.0384  -0.0174 147 VAL A CG1 
1186 C CG2 . VAL A 158 ? 0.6994 0.4787 0.5498 -0.0063 0.0472  -0.0285 147 VAL A CG2 
1187 N N   . LEU A 159 ? 0.6427 0.4641 0.5253 -0.0039 0.0373  -0.0099 148 LEU A N   
1188 C CA  . LEU A 159 ? 0.6378 0.4716 0.5326 -0.0040 0.0310  -0.0052 148 LEU A CA  
1189 C C   . LEU A 159 ? 0.6430 0.4828 0.5539 -0.0021 0.0297  -0.0024 148 LEU A C   
1190 O O   . LEU A 159 ? 0.6509 0.4876 0.5685 0.0008  0.0360  -0.0019 148 LEU A O   
1191 C CB  . LEU A 159 ? 0.6298 0.4682 0.5291 -0.0028 0.0347  -0.0014 148 LEU A CB  
1192 C CG  . LEU A 159 ? 0.6412 0.4729 0.5239 -0.0046 0.0373  -0.0030 148 LEU A CG  
1193 C CD1 . LEU A 159 ? 0.6409 0.4765 0.5296 -0.0031 0.0429  0.0013  148 LEU A CD1 
1194 C CD2 . LEU A 159 ? 0.6429 0.4749 0.5160 -0.0084 0.0279  -0.0042 148 LEU A CD2 
1195 N N   . HIS A 160 ? 0.6370 0.4844 0.5531 -0.0036 0.0219  -0.0006 149 HIS A N   
1196 C CA  . HIS A 160 ? 0.6357 0.4887 0.5645 -0.0024 0.0198  0.0028  149 HIS A CA  
1197 C C   . HIS A 160 ? 0.6331 0.4928 0.5755 -0.0002 0.0218  0.0079  149 HIS A C   
1198 O O   . HIS A 160 ? 0.6282 0.4890 0.5821 0.0021  0.0245  0.0110  149 HIS A O   
1199 C CB  . HIS A 160 ? 0.6461 0.5044 0.5745 -0.0048 0.0118  0.0031  149 HIS A CB  
1200 C CG  . HIS A 160 ? 0.6754 0.5377 0.6132 -0.0041 0.0098  0.0066  149 HIS A CG  
1201 N ND1 . HIS A 160 ? 0.6932 0.5620 0.6420 -0.0030 0.0085  0.0115  149 HIS A ND1 
1202 C CD2 . HIS A 160 ? 0.6942 0.5544 0.6319 -0.0047 0.0085  0.0065  149 HIS A CD2 
1203 C CE1 . HIS A 160 ? 0.7004 0.5708 0.6542 -0.0029 0.0062  0.0144  149 HIS A CE1 
1204 N NE2 . HIS A 160 ? 0.7064 0.5717 0.6539 -0.0038 0.0066  0.0117  149 HIS A NE2 
1205 N N   . ARG A 161 ? 0.6365 0.5006 0.5790 -0.0012 0.0201  0.0091  150 ARG A N   
1206 C CA  . ARG A 161 ? 0.6326 0.5034 0.5883 -0.0001 0.0209  0.0140  150 ARG A CA  
1207 C C   . ARG A 161 ? 0.6197 0.4986 0.5857 -0.0012 0.0133  0.0178  150 ARG A C   
1208 O O   . ARG A 161 ? 0.6213 0.5059 0.5972 -0.0015 0.0115  0.0216  150 ARG A O   
1209 C CB  . ARG A 161 ? 0.6522 0.5208 0.6173 0.0035  0.0303  0.0164  150 ARG A CB  
1210 C CG  . ARG A 161 ? 0.7157 0.5741 0.6675 0.0044  0.0389  0.0118  150 ARG A CG  
1211 C CD  . ARG A 161 ? 0.7701 0.6279 0.7289 0.0072  0.0488  0.0144  150 ARG A CD  
1212 N NE  . ARG A 161 ? 0.8212 0.6737 0.7868 0.0110  0.0581  0.0143  150 ARG A NE  
1213 C CZ  . ARG A 161 ? 0.8569 0.6987 0.8115 0.0126  0.0686  0.0101  150 ARG A CZ  
1214 N NH1 . ARG A 161 ? 0.8582 0.6936 0.7929 0.0103  0.0702  0.0063  150 ARG A NH1 
1215 N NH2 . ARG A 161 ? 0.8509 0.6876 0.8139 0.0165  0.0776  0.0099  150 ARG A NH2 
1216 N N   . ASP A 162 ? 0.6074 0.4863 0.5702 -0.0022 0.0086  0.0170  151 ASP A N   
1217 C CA  . ASP A 162 ? 0.6003 0.4855 0.5697 -0.0037 0.0015  0.0207  151 ASP A CA  
1218 C C   . ASP A 162 ? 0.5866 0.4712 0.5463 -0.0059 -0.0036 0.0183  151 ASP A C   
1219 O O   . ASP A 162 ? 0.5869 0.4742 0.5494 -0.0068 -0.0077 0.0214  151 ASP A O   
1220 C CB  . ASP A 162 ? 0.6304 0.5181 0.6143 -0.0016 0.0026  0.0264  151 ASP A CB  
1221 C CG  . ASP A 162 ? 0.6956 0.5907 0.6898 -0.0032 -0.0048 0.0321  151 ASP A CG  
1222 O OD1 . ASP A 162 ? 0.7081 0.6060 0.7005 -0.0056 -0.0090 0.0314  151 ASP A OD1 
1223 O OD2 . ASP A 162 ? 0.7242 0.6216 0.7287 -0.0023 -0.0067 0.0375  151 ASP A OD2 
1224 N N   . LEU A 163 ? 0.5733 0.4547 0.5222 -0.0071 -0.0032 0.0135  152 LEU A N   
1225 C CA  . LEU A 163 ? 0.5678 0.4490 0.5092 -0.0090 -0.0066 0.0113  152 LEU A CA  
1226 C C   . LEU A 163 ? 0.5601 0.4457 0.5015 -0.0109 -0.0122 0.0128  152 LEU A C   
1227 O O   . LEU A 163 ? 0.5621 0.4499 0.5050 -0.0118 -0.0145 0.0126  152 LEU A O   
1228 C CB  . LEU A 163 ? 0.5729 0.4515 0.5065 -0.0099 -0.0062 0.0068  152 LEU A CB  
1229 C CG  . LEU A 163 ? 0.5912 0.4645 0.5198 -0.0098 -0.0035 0.0043  152 LEU A CG  
1230 C CD1 . LEU A 163 ? 0.6022 0.4734 0.5246 -0.0109 -0.0040 0.0013  152 LEU A CD1 
1231 C CD2 . LEU A 163 ? 0.5971 0.4704 0.5247 -0.0107 -0.0049 0.0044  152 LEU A CD2 
1232 N N   . LYS A 164 ? 0.5471 0.4331 0.4858 -0.0118 -0.0142 0.0143  153 LYS A N   
1233 C CA  . LYS A 164 ? 0.5430 0.4314 0.4776 -0.0142 -0.0191 0.0154  153 LYS A CA  
1234 C C   . LYS A 164 ? 0.5457 0.4329 0.4740 -0.0151 -0.0188 0.0161  153 LYS A C   
1235 O O   . LYS A 164 ? 0.5400 0.4252 0.4709 -0.0138 -0.0158 0.0172  153 LYS A O   
1236 C CB  . LYS A 164 ? 0.5600 0.4518 0.5025 -0.0146 -0.0235 0.0207  153 LYS A CB  
1237 C CG  . LYS A 164 ? 0.6040 0.4965 0.5555 -0.0128 -0.0224 0.0262  153 LYS A CG  
1238 C CD  . LYS A 164 ? 0.6516 0.5485 0.6124 -0.0138 -0.0282 0.0325  153 LYS A CD  
1239 C CE  . LYS A 164 ? 0.6986 0.5968 0.6754 -0.0105 -0.0244 0.0368  153 LYS A CE  
1240 N NZ  . LYS A 164 ? 0.7312 0.6282 0.7107 -0.0086 -0.0186 0.0329  153 LYS A NZ  
1241 N N   . PRO A 165 ? 0.5520 0.4395 0.4714 -0.0174 -0.0212 0.0152  154 PRO A N   
1242 C CA  . PRO A 165 ? 0.5576 0.4439 0.4706 -0.0183 -0.0196 0.0161  154 PRO A CA  
1243 C C   . PRO A 165 ? 0.5596 0.4460 0.4770 -0.0179 -0.0201 0.0223  154 PRO A C   
1244 O O   . PRO A 165 ? 0.5559 0.4407 0.4725 -0.0177 -0.0169 0.0229  154 PRO A O   
1245 C CB  . PRO A 165 ? 0.5670 0.4529 0.4687 -0.0209 -0.0221 0.0146  154 PRO A CB  
1246 C CG  . PRO A 165 ? 0.5699 0.4556 0.4722 -0.0209 -0.0231 0.0101  154 PRO A CG  
1247 C CD  . PRO A 165 ? 0.5442 0.4319 0.4581 -0.0193 -0.0246 0.0126  154 PRO A CD  
1248 N N   . ALA A 166 ? 0.5612 0.4495 0.4849 -0.0177 -0.0242 0.0273  155 ALA A N   
1249 C CA  . ALA A 166 ? 0.5688 0.4572 0.4986 -0.0171 -0.0252 0.0341  155 ALA A CA  
1250 C C   . ALA A 166 ? 0.5785 0.4640 0.5169 -0.0143 -0.0195 0.0334  155 ALA A C   
1251 O O   . ALA A 166 ? 0.5854 0.4690 0.5247 -0.0143 -0.0181 0.0364  155 ALA A O   
1252 C CB  . ALA A 166 ? 0.5640 0.4558 0.5020 -0.0174 -0.0311 0.0401  155 ALA A CB  
1253 N N   . ASN A 167 ? 0.5762 0.4605 0.5192 -0.0123 -0.0161 0.0291  156 ASN A N   
1254 C CA  . ASN A 167 ? 0.5747 0.4543 0.5226 -0.0101 -0.0108 0.0272  156 ASN A CA  
1255 C C   . ASN A 167 ? 0.5850 0.4614 0.5252 -0.0112 -0.0081 0.0214  156 ASN A C   
1256 O O   . ASN A 167 ? 0.5890 0.4609 0.5300 -0.0102 -0.0048 0.0178  156 ASN A O   
1257 C CB  . ASN A 167 ? 0.5697 0.4485 0.5262 -0.0074 -0.0079 0.0267  156 ASN A CB  
1258 C CG  . ASN A 167 ? 0.5786 0.4592 0.5316 -0.0077 -0.0082 0.0229  156 ASN A CG  
1259 O OD1 . ASN A 167 ? 0.5935 0.4739 0.5377 -0.0094 -0.0089 0.0186  156 ASN A OD1 
1260 N ND2 . ASN A 167 ? 0.5652 0.4479 0.5269 -0.0061 -0.0073 0.0248  156 ASN A ND2 
1261 N N   . ILE A 168 ? 0.5855 0.4638 0.5182 -0.0134 -0.0096 0.0206  157 ILE A N   
1262 C CA  . ILE A 168 ? 0.5923 0.4689 0.5213 -0.0145 -0.0075 0.0166  157 ILE A CA  
1263 C C   . ILE A 168 ? 0.5975 0.4741 0.5256 -0.0159 -0.0070 0.0205  157 ILE A C   
1264 O O   . ILE A 168 ? 0.6068 0.4861 0.5287 -0.0175 -0.0076 0.0215  157 ILE A O   
1265 C CB  . ILE A 168 ? 0.6052 0.4842 0.5286 -0.0155 -0.0080 0.0125  157 ILE A CB  
1266 C CG1 . ILE A 168 ? 0.6289 0.5083 0.5531 -0.0144 -0.0090 0.0100  157 ILE A CG1 
1267 C CG2 . ILE A 168 ? 0.6061 0.4839 0.5295 -0.0165 -0.0061 0.0098  157 ILE A CG2 
1268 C CD1 . ILE A 168 ? 0.6504 0.5260 0.5772 -0.0132 -0.0070 0.0079  157 ILE A CD1 
1269 N N   . LEU A 169 ? 0.5909 0.4639 0.5247 -0.0155 -0.0056 0.0228  158 LEU A N   
1270 C CA  . LEU A 169 ? 0.5909 0.4635 0.5254 -0.0169 -0.0050 0.0276  158 LEU A CA  
1271 C C   . LEU A 169 ? 0.5888 0.4613 0.5219 -0.0189 -0.0027 0.0253  158 LEU A C   
1272 O O   . LEU A 169 ? 0.5844 0.4559 0.5182 -0.0190 -0.0022 0.0201  158 LEU A O   
1273 C CB  . LEU A 169 ? 0.5925 0.4605 0.5358 -0.0155 -0.0042 0.0312  158 LEU A CB  
1274 C CG  . LEU A 169 ? 0.6052 0.4726 0.5548 -0.0128 -0.0050 0.0331  158 LEU A CG  
1275 C CD1 . LEU A 169 ? 0.6113 0.4728 0.5709 -0.0111 -0.0027 0.0356  158 LEU A CD1 
1276 C CD2 . LEU A 169 ? 0.6081 0.4811 0.5563 -0.0131 -0.0093 0.0386  158 LEU A CD2 
1277 N N   . VAL A 170 ? 0.5891 0.4630 0.5206 -0.0206 -0.0014 0.0297  159 VAL A N   
1278 C CA  . VAL A 170 ? 0.5957 0.4705 0.5285 -0.0225 0.0016  0.0290  159 VAL A CA  
1279 C C   . VAL A 170 ? 0.6073 0.4804 0.5441 -0.0239 0.0030  0.0354  159 VAL A C   
1280 O O   . VAL A 170 ? 0.6120 0.4864 0.5438 -0.0243 0.0028  0.0409  159 VAL A O   
1281 C CB  . VAL A 170 ? 0.5999 0.4792 0.5252 -0.0233 0.0037  0.0276  159 VAL A CB  
1282 C CG1 . VAL A 170 ? 0.6041 0.4849 0.5353 -0.0246 0.0073  0.0263  159 VAL A CG1 
1283 C CG2 . VAL A 170 ? 0.6023 0.4830 0.5227 -0.0219 0.0017  0.0226  159 VAL A CG2 
1284 N N   . MET A 171 ? 0.6127 0.4826 0.5582 -0.0251 0.0040  0.0350  160 MET A N   
1285 C CA  . MET A 171 ? 0.6266 0.4941 0.5780 -0.0267 0.0055  0.0412  160 MET A CA  
1286 C C   . MET A 171 ? 0.6449 0.5168 0.5931 -0.0287 0.0093  0.0463  160 MET A C   
1287 O O   . MET A 171 ? 0.6464 0.5223 0.5930 -0.0294 0.0119  0.0435  160 MET A O   
1288 C CB  . MET A 171 ? 0.6318 0.4939 0.5932 -0.0281 0.0051  0.0386  160 MET A CB  
1289 C CG  . MET A 171 ? 0.6627 0.5189 0.6247 -0.0263 0.0027  0.0329  160 MET A CG  
1290 S SD  . MET A 171 ? 0.7194 0.5713 0.6832 -0.0232 0.0023  0.0367  160 MET A SD  
1291 C CE  . MET A 171 ? 0.6494 0.4935 0.6240 -0.0250 0.0034  0.0406  160 MET A CE  
1292 N N   . GLY A 172 ? 0.6581 0.5290 0.6059 -0.0295 0.0099  0.0541  161 GLY A N   
1293 C CA  . GLY A 172 ? 0.6753 0.5493 0.6186 -0.0317 0.0143  0.0600  161 GLY A CA  
1294 C C   . GLY A 172 ? 0.6858 0.5586 0.6416 -0.0340 0.0175  0.0631  161 GLY A C   
1295 O O   . GLY A 172 ? 0.6884 0.5591 0.6546 -0.0344 0.0161  0.0583  161 GLY A O   
1296 N N   . GLU A 173 ? 0.6858 0.5594 0.6407 -0.0360 0.0213  0.0714  162 GLU A N   
1297 C CA  . GLU A 173 ? 0.6799 0.5527 0.6486 -0.0387 0.0245  0.0755  162 GLU A CA  
1298 C C   . GLU A 173 ? 0.6704 0.5364 0.6523 -0.0389 0.0200  0.0746  162 GLU A C   
1299 O O   . GLU A 173 ? 0.6776 0.5392 0.6583 -0.0371 0.0164  0.0759  162 GLU A O   
1300 C CB  . GLU A 173 ? 0.7104 0.5845 0.6749 -0.0408 0.0294  0.0858  162 GLU A CB  
1301 C CG  . GLU A 173 ? 0.7881 0.6676 0.7406 -0.0413 0.0364  0.0860  162 GLU A CG  
1302 C CD  . GLU A 173 ? 0.8801 0.7642 0.8417 -0.0416 0.0413  0.0806  162 GLU A CD  
1303 O OE1 . GLU A 173 ? 0.8857 0.7696 0.8652 -0.0430 0.0401  0.0798  162 GLU A OE1 
1304 O OE2 . GLU A 173 ? 0.9176 0.8053 0.8689 -0.0406 0.0461  0.0772  162 GLU A OE2 
1305 N N   . GLY A 174 ? 0.6539 0.5189 0.6487 -0.0411 0.0202  0.0717  163 GLY A N   
1306 C CA  . GLY A 174 ? 0.6497 0.5065 0.6554 -0.0420 0.0160  0.0691  163 GLY A CA  
1307 C C   . GLY A 174 ? 0.6440 0.5001 0.6567 -0.0437 0.0134  0.0612  163 GLY A C   
1308 O O   . GLY A 174 ? 0.6458 0.5087 0.6575 -0.0440 0.0148  0.0587  163 GLY A O   
1309 N N   . PRO A 175 ? 0.6358 0.4827 0.6550 -0.0449 0.0091  0.0572  164 PRO A N   
1310 C CA  . PRO A 175 ? 0.6329 0.4780 0.6572 -0.0475 0.0051  0.0500  164 PRO A CA  
1311 C C   . PRO A 175 ? 0.6406 0.4883 0.6547 -0.0452 0.0027  0.0423  164 PRO A C   
1312 O O   . PRO A 175 ? 0.6412 0.4899 0.6590 -0.0475 -0.0008 0.0380  164 PRO A O   
1313 C CB  . PRO A 175 ? 0.6396 0.4720 0.6694 -0.0494 0.0014  0.0473  164 PRO A CB  
1314 C CG  . PRO A 175 ? 0.6482 0.4762 0.6733 -0.0456 0.0035  0.0501  164 PRO A CG  
1315 C CD  . PRO A 175 ? 0.6273 0.4645 0.6501 -0.0443 0.0079  0.0591  164 PRO A CD  
1316 N N   . GLU A 176 ? 0.6416 0.4905 0.6439 -0.0410 0.0039  0.0412  165 GLU A N   
1317 C CA  . GLU A 176 ? 0.6452 0.4968 0.6382 -0.0389 0.0020  0.0347  165 GLU A CA  
1318 C C   . GLU A 176 ? 0.6444 0.5057 0.6309 -0.0368 0.0056  0.0370  165 GLU A C   
1319 O O   . GLU A 176 ? 0.6498 0.5126 0.6271 -0.0341 0.0048  0.0332  165 GLU A O   
1320 C CB  . GLU A 176 ? 0.6699 0.5143 0.6551 -0.0359 0.0004  0.0302  165 GLU A CB  
1321 C CG  . GLU A 176 ? 0.7203 0.5533 0.7083 -0.0378 -0.0026 0.0253  165 GLU A CG  
1322 C CD  . GLU A 176 ? 0.8011 0.6281 0.7795 -0.0352 -0.0035 0.0185  165 GLU A CD  
1323 O OE1 . GLU A 176 ? 0.8128 0.6406 0.7852 -0.0359 -0.0063 0.0131  165 GLU A OE1 
1324 O OE2 . GLU A 176 ? 0.8305 0.6521 0.8082 -0.0323 -0.0012 0.0191  165 GLU A OE2 
1325 N N   . ARG A 177 ? 0.6356 0.5025 0.6263 -0.0381 0.0100  0.0431  166 ARG A N   
1326 C CA  . ARG A 177 ? 0.6364 0.5106 0.6191 -0.0365 0.0146  0.0451  166 ARG A CA  
1327 C C   . ARG A 177 ? 0.6362 0.5144 0.6138 -0.0347 0.0137  0.0386  166 ARG A C   
1328 O O   . ARG A 177 ? 0.6403 0.5195 0.6255 -0.0359 0.0114  0.0350  166 ARG A O   
1329 C CB  . ARG A 177 ? 0.6463 0.5254 0.6360 -0.0388 0.0205  0.0514  166 ARG A CB  
1330 C CG  . ARG A 177 ? 0.6876 0.5714 0.6654 -0.0374 0.0266  0.0545  166 ARG A CG  
1331 C CD  . ARG A 177 ? 0.7323 0.6214 0.7183 -0.0393 0.0339  0.0585  166 ARG A CD  
1332 N NE  . ARG A 177 ? 0.7845 0.6765 0.7570 -0.0384 0.0411  0.0613  166 ARG A NE  
1333 C CZ  . ARG A 177 ? 0.8261 0.7227 0.7960 -0.0372 0.0471  0.0583  166 ARG A CZ  
1334 N NH1 . ARG A 177 ? 0.8227 0.7225 0.8046 -0.0365 0.0461  0.0533  166 ARG A NH1 
1335 N NH2 . ARG A 177 ? 0.8352 0.7322 0.7899 -0.0367 0.0541  0.0604  166 ARG A NH2 
1336 N N   . GLY A 178 ? 0.6289 0.5087 0.5940 -0.0322 0.0146  0.0377  167 GLY A N   
1337 C CA  . GLY A 178 ? 0.6256 0.5085 0.5850 -0.0304 0.0142  0.0322  167 GLY A CA  
1338 C C   . GLY A 178 ? 0.6218 0.5018 0.5826 -0.0297 0.0087  0.0263  167 GLY A C   
1339 O O   . GLY A 178 ? 0.6235 0.5064 0.5853 -0.0291 0.0081  0.0224  167 GLY A O   
1340 N N   . ARG A 179 ? 0.6153 0.4891 0.5761 -0.0296 0.0052  0.0256  168 ARG A N   
1341 C CA  . ARG A 179 ? 0.6103 0.4801 0.5698 -0.0291 0.0009  0.0198  168 ARG A CA  
1342 C C   . ARG A 179 ? 0.6001 0.4684 0.5508 -0.0262 0.0001  0.0181  168 ARG A C   
1343 O O   . ARG A 179 ? 0.6024 0.4690 0.5514 -0.0251 0.0008  0.0214  168 ARG A O   
1344 C CB  . ARG A 179 ? 0.6306 0.4929 0.5957 -0.0314 -0.0018 0.0188  168 ARG A CB  
1345 C CG  . ARG A 179 ? 0.6743 0.5308 0.6346 -0.0313 -0.0056 0.0127  168 ARG A CG  
1346 C CD  . ARG A 179 ? 0.7310 0.5791 0.6953 -0.0344 -0.0084 0.0109  168 ARG A CD  
1347 N NE  . ARG A 179 ? 0.7830 0.6337 0.7550 -0.0382 -0.0118 0.0109  168 ARG A NE  
1348 C CZ  . ARG A 179 ? 0.8278 0.6730 0.8065 -0.0422 -0.0150 0.0107  168 ARG A CZ  
1349 N NH1 . ARG A 179 ? 0.8234 0.6591 0.8012 -0.0427 -0.0145 0.0099  168 ARG A NH1 
1350 N NH2 . ARG A 179 ? 0.8338 0.6827 0.8215 -0.0458 -0.0189 0.0114  168 ARG A NH2 
1351 N N   . VAL A 180 ? 0.5907 0.4599 0.5374 -0.0251 -0.0018 0.0136  169 VAL A N   
1352 C CA  . VAL A 180 ? 0.5929 0.4613 0.5331 -0.0226 -0.0024 0.0121  169 VAL A CA  
1353 C C   . VAL A 180 ? 0.5959 0.4569 0.5361 -0.0218 -0.0031 0.0106  169 VAL A C   
1354 O O   . VAL A 180 ? 0.5993 0.4549 0.5409 -0.0235 -0.0044 0.0078  169 VAL A O   
1355 C CB  . VAL A 180 ? 0.5974 0.4689 0.5343 -0.0219 -0.0037 0.0084  169 VAL A CB  
1356 C CG1 . VAL A 180 ? 0.6063 0.4766 0.5382 -0.0196 -0.0045 0.0069  169 VAL A CG1 
1357 C CG2 . VAL A 180 ? 0.5977 0.4753 0.5343 -0.0219 -0.0016 0.0095  169 VAL A CG2 
1358 N N   . LYS A 181 ? 0.5909 0.4513 0.5300 -0.0195 -0.0022 0.0125  170 LYS A N   
1359 C CA  . LYS A 181 ? 0.5883 0.4419 0.5288 -0.0178 -0.0011 0.0114  170 LYS A CA  
1360 C C   . LYS A 181 ? 0.5948 0.4509 0.5331 -0.0152 -0.0008 0.0113  170 LYS A C   
1361 O O   . LYS A 181 ? 0.5943 0.4554 0.5341 -0.0142 -0.0015 0.0155  170 LYS A O   
1362 C CB  . LYS A 181 ? 0.5908 0.4416 0.5377 -0.0174 0.0003  0.0164  170 LYS A CB  
1363 C CG  . LYS A 181 ? 0.6037 0.4521 0.5545 -0.0203 0.0001  0.0176  170 LYS A CG  
1364 C CD  . LYS A 181 ? 0.6214 0.4611 0.5722 -0.0220 -0.0002 0.0122  170 LYS A CD  
1365 C CE  . LYS A 181 ? 0.6436 0.4808 0.6007 -0.0252 -0.0009 0.0141  170 LYS A CE  
1366 N NZ  . LYS A 181 ? 0.6769 0.5051 0.6327 -0.0279 -0.0029 0.0083  170 LYS A NZ  
1367 N N   . ILE A 182 ? 0.6011 0.4540 0.5357 -0.0144 -0.0001 0.0068  171 ILE A N   
1368 C CA  . ILE A 182 ? 0.6113 0.4664 0.5455 -0.0120 0.0008  0.0070  171 ILE A CA  
1369 C C   . ILE A 182 ? 0.6274 0.4789 0.5686 -0.0094 0.0040  0.0097  171 ILE A C   
1370 O O   . ILE A 182 ? 0.6289 0.4725 0.5711 -0.0091 0.0067  0.0078  171 ILE A O   
1371 C CB  . ILE A 182 ? 0.6174 0.4698 0.5448 -0.0124 0.0011  0.0020  171 ILE A CB  
1372 C CG1 . ILE A 182 ? 0.6201 0.4770 0.5440 -0.0147 -0.0025 0.0006  171 ILE A CG1 
1373 C CG2 . ILE A 182 ? 0.6251 0.4793 0.5535 -0.0099 0.0031  0.0027  171 ILE A CG2 
1374 C CD1 . ILE A 182 ? 0.6351 0.4884 0.5530 -0.0159 -0.0036 -0.0032 171 ILE A CD1 
1375 N N   . ALA A 183 ? 0.6351 0.4921 0.5820 -0.0076 0.0034  0.0143  172 ALA A N   
1376 C CA  . ALA A 183 ? 0.6459 0.5011 0.6031 -0.0048 0.0059  0.0185  172 ALA A CA  
1377 C C   . ALA A 183 ? 0.6668 0.5247 0.6292 -0.0022 0.0080  0.0194  172 ALA A C   
1378 O O   . ALA A 183 ? 0.6638 0.5259 0.6216 -0.0030 0.0062  0.0177  172 ALA A O   
1379 C CB  . ALA A 183 ? 0.6388 0.4987 0.6014 -0.0054 0.0022  0.0256  172 ALA A CB  
1380 N N   . ASP A 184 ? 0.6842 0.5393 0.6578 0.0011  0.0123  0.0222  173 ASP A N   
1381 C CA  . ASP A 184 ? 0.6999 0.5574 0.6831 0.0041  0.0157  0.0244  173 ASP A CA  
1382 C C   . ASP A 184 ? 0.7280 0.5807 0.7038 0.0049  0.0216  0.0182  173 ASP A C   
1383 O O   . ASP A 184 ? 0.7286 0.5858 0.6993 0.0036  0.0196  0.0171  173 ASP A O   
1384 C CB  . ASP A 184 ? 0.7170 0.5851 0.7061 0.0032  0.0094  0.0302  173 ASP A CB  
1385 C CG  . ASP A 184 ? 0.7788 0.6510 0.7863 0.0062  0.0109  0.0368  173 ASP A CG  
1386 O OD1 . ASP A 184 ? 0.7927 0.6594 0.8091 0.0099  0.0187  0.0366  173 ASP A OD1 
1387 O OD2 . ASP A 184 ? 0.7964 0.6767 0.8098 0.0049  0.0043  0.0422  173 ASP A OD2 
1388 N N   . MET A 185 ? 0.7545 0.5972 0.7289 0.0069  0.0290  0.0142  174 MET A N   
1389 C CA  . MET A 185 ? 0.7889 0.6255 0.7545 0.0077  0.0358  0.0087  174 MET A CA  
1390 C C   . MET A 185 ? 0.8162 0.6536 0.7956 0.0121  0.0438  0.0120  174 MET A C   
1391 O O   . MET A 185 ? 0.8240 0.6544 0.7970 0.0136  0.0520  0.0078  174 MET A O   
1392 C CB  . MET A 185 ? 0.8017 0.6246 0.7541 0.0067  0.0399  0.0013  174 MET A CB  
1393 C CG  . MET A 185 ? 0.8218 0.6435 0.7636 0.0024  0.0326  -0.0016 174 MET A CG  
1394 S SD  . MET A 185 ? 0.8453 0.6746 0.7761 -0.0011 0.0258  -0.0027 174 MET A SD  
1395 C CE  . MET A 185 ? 0.7984 0.6350 0.7332 -0.0038 0.0175  0.0007  174 MET A CE  
1396 N N   . GLY A 186 ? 0.8269 0.6726 0.8250 0.0141  0.0415  0.0198  175 GLY A N   
1397 C CA  . GLY A 186 ? 0.8454 0.6934 0.8616 0.0184  0.0486  0.0245  175 GLY A CA  
1398 C C   . GLY A 186 ? 0.8687 0.7268 0.8926 0.0183  0.0469  0.0287  175 GLY A C   
1399 O O   . GLY A 186 ? 0.8617 0.7248 0.9056 0.0214  0.0504  0.0349  175 GLY A O   
1400 N N   . PHE A 187 ? 0.8977 0.7589 0.9078 0.0146  0.0416  0.0259  176 PHE A N   
1401 C CA  . PHE A 187 ? 0.9230 0.7928 0.9405 0.0142  0.0401  0.0297  176 PHE A CA  
1402 C C   . PHE A 187 ? 0.9551 0.8192 0.9695 0.0165  0.0517  0.0266  176 PHE A C   
1403 O O   . PHE A 187 ? 0.9595 0.8199 0.9569 0.0144  0.0526  0.0217  176 PHE A O   
1404 C CB  . PHE A 187 ? 0.9284 0.8031 0.9343 0.0096  0.0304  0.0282  176 PHE A CB  
1405 C CG  . PHE A 187 ? 0.9367 0.8210 0.9538 0.0085  0.0259  0.0334  176 PHE A CG  
1406 C CD1 . PHE A 187 ? 0.9510 0.8359 0.9681 0.0087  0.0307  0.0329  176 PHE A CD1 
1407 C CD2 . PHE A 187 ? 0.9444 0.8365 0.9709 0.0066  0.0163  0.0388  176 PHE A CD2 
1408 C CE1 . PHE A 187 ? 0.9560 0.8494 0.9845 0.0071  0.0261  0.0377  176 PHE A CE1 
1409 C CE2 . PHE A 187 ? 0.9516 0.8515 0.9877 0.0047  0.0110  0.0431  176 PHE A CE2 
1410 C CZ  . PHE A 187 ? 0.9497 0.8504 0.9879 0.0050  0.0159  0.0425  176 PHE A CZ  
1411 N N   . ALA A 188 ? 0.9755 0.8383 1.0059 0.0210  0.0614  0.0297  177 ALA A N   
1412 C CA  . ALA A 188 ? 1.0092 0.8658 1.0370 0.0237  0.0746  0.0271  177 ALA A CA  
1413 C C   . ALA A 188 ? 1.0336 0.9000 1.0743 0.0237  0.0754  0.0329  177 ALA A C   
1414 O O   . ALA A 188 ? 1.0276 0.9054 1.0873 0.0231  0.0678  0.0403  177 ALA A O   
1415 C CB  . ALA A 188 ? 1.0072 0.8568 1.0470 0.0290  0.0863  0.0273  177 ALA A CB  
1416 N N   . ARG A 189 ? 1.0569 0.9185 1.0866 0.0239  0.0843  0.0299  178 ARG A N   
1417 C CA  . ARG A 189 ? 1.0732 0.9430 1.1149 0.0239  0.0869  0.0355  178 ARG A CA  
1418 C C   . ARG A 189 ? 1.0848 0.9476 1.1262 0.0278  0.1045  0.0345  178 ARG A C   
1419 O O   . ARG A 189 ? 1.0957 0.9457 1.1223 0.0297  0.1135  0.0279  178 ARG A O   
1420 C CB  . ARG A 189 ? 1.1082 0.9809 1.1348 0.0188  0.0775  0.0340  178 ARG A CB  
1421 C CG  . ARG A 189 ? 1.1666 1.0480 1.1981 0.0153  0.0617  0.0364  178 ARG A CG  
1422 C CD  . ARG A 189 ? 1.2119 1.1053 1.2712 0.0158  0.0575  0.0452  178 ARG A CD  
1423 N NE  . ARG A 189 ? 1.2594 1.1597 1.3191 0.0114  0.0426  0.0469  178 ARG A NE  
1424 C CZ  . ARG A 189 ? 1.2926 1.1975 1.3519 0.0080  0.0370  0.0480  178 ARG A CZ  
1425 N NH1 . ARG A 189 ? 1.2854 1.1948 1.3435 0.0041  0.0242  0.0485  178 ARG A NH1 
1426 N NH2 . ARG A 189 ? 1.2958 1.1999 1.3548 0.0084  0.0445  0.0486  178 ARG A NH2 
1427 N N   . LEU A 190 ? 1.0808 0.9512 1.1384 0.0287  0.1098  0.0409  179 LEU A N   
1428 C CA  . LEU A 190 ? 1.0941 0.9582 1.1511 0.0323  0.1278  0.0406  179 LEU A CA  
1429 C C   . LEU A 190 ? 1.1071 0.9682 1.1434 0.0289  0.1298  0.0388  179 LEU A C   
1430 O O   . LEU A 190 ? 1.1219 0.9708 1.1284 0.0272  0.1321  0.0312  179 LEU A O   
1431 C CB  . LEU A 190 ? 1.0838 0.9582 1.1767 0.0364  0.1353  0.0501  179 LEU A CB  
1432 C CG  . LEU A 190 ? 1.0980 0.9727 1.2122 0.0412  0.1385  0.0524  179 LEU A CG  
1433 C CD1 . LEU A 190 ? 1.0895 0.9776 1.2431 0.0442  0.1418  0.0637  179 LEU A CD1 
1434 C CD2 . LEU A 190 ? 1.1166 0.9751 1.2163 0.0454  0.1545  0.0445  179 LEU A CD2 
1435 N N   . VAL A 206 ? 0.8738 0.8083 0.9380 -0.0257 -0.0701 0.0708  195 VAL A N   
1436 C CA  . VAL A 206 ? 0.8796 0.8139 0.9401 -0.0313 -0.0789 0.0686  195 VAL A CA  
1437 C C   . VAL A 206 ? 0.8871 0.8131 0.9211 -0.0333 -0.0780 0.0579  195 VAL A C   
1438 O O   . VAL A 206 ? 0.8920 0.8159 0.9210 -0.0379 -0.0847 0.0548  195 VAL A O   
1439 C CB  . VAL A 206 ? 0.8884 0.8263 0.9547 -0.0371 -0.0944 0.0758  195 VAL A CB  
1440 C CG1 . VAL A 206 ? 0.8807 0.8284 0.9797 -0.0357 -0.0963 0.0871  195 VAL A CG1 
1441 C CG2 . VAL A 206 ? 0.9025 0.8370 0.9513 -0.0386 -0.0997 0.0765  195 VAL A CG2 
1442 N N   . THR A 207 ? 0.8833 0.8043 0.9018 -0.0301 -0.0699 0.0523  196 THR A N   
1443 C CA  . THR A 207 ? 0.8854 0.7993 0.8820 -0.0313 -0.0679 0.0429  196 THR A CA  
1444 C C   . THR A 207 ? 0.8627 0.7748 0.8597 -0.0271 -0.0567 0.0381  196 THR A C   
1445 O O   . THR A 207 ? 0.8661 0.7791 0.8685 -0.0227 -0.0487 0.0396  196 THR A O   
1446 C CB  . THR A 207 ? 0.9161 0.8258 0.8936 -0.0324 -0.0698 0.0408  196 THR A CB  
1447 O OG1 . THR A 207 ? 0.9328 0.8405 0.9004 -0.0382 -0.0809 0.0410  196 THR A OG1 
1448 C CG2 . THR A 207 ? 0.9290 0.8329 0.8898 -0.0304 -0.0617 0.0323  196 THR A CG2 
1449 N N   . PHE A 208 ? 0.8379 0.7467 0.8290 -0.0286 -0.0565 0.0326  197 PHE A N   
1450 C CA  . PHE A 208 ? 0.8184 0.7254 0.8094 -0.0254 -0.0475 0.0290  197 PHE A CA  
1451 C C   . PHE A 208 ? 0.7951 0.6958 0.7688 -0.0260 -0.0460 0.0210  197 PHE A C   
1452 O O   . PHE A 208 ? 0.7977 0.6966 0.7716 -0.0249 -0.0419 0.0182  197 PHE A O   
1453 C CB  . PHE A 208 ? 0.8133 0.7233 0.8196 -0.0260 -0.0472 0.0320  197 PHE A CB  
1454 C CG  . PHE A 208 ? 0.8142 0.7312 0.8409 -0.0259 -0.0492 0.0405  197 PHE A CG  
1455 C CD1 . PHE A 208 ? 0.8210 0.7410 0.8584 -0.0214 -0.0408 0.0446  197 PHE A CD1 
1456 C CD2 . PHE A 208 ? 0.8207 0.7409 0.8561 -0.0305 -0.0598 0.0443  197 PHE A CD2 
1457 C CE1 . PHE A 208 ? 0.8207 0.7475 0.8796 -0.0208 -0.0417 0.0529  197 PHE A CE1 
1458 C CE2 . PHE A 208 ? 0.8196 0.7473 0.8768 -0.0304 -0.0622 0.0532  197 PHE A CE2 
1459 C CZ  . PHE A 208 ? 0.8120 0.7433 0.8819 -0.0252 -0.0527 0.0576  197 PHE A CZ  
1460 N N   . TRP A 209 ? 0.7666 0.6642 0.7263 -0.0274 -0.0487 0.0180  198 TRP A N   
1461 C CA  . TRP A 209 ? 0.7473 0.6392 0.6924 -0.0277 -0.0466 0.0107  198 TRP A CA  
1462 C C   . TRP A 209 ? 0.7312 0.6221 0.6751 -0.0240 -0.0384 0.0083  198 TRP A C   
1463 O O   . TRP A 209 ? 0.7361 0.6234 0.6738 -0.0238 -0.0364 0.0033  198 TRP A O   
1464 C CB  . TRP A 209 ? 0.7460 0.6350 0.6764 -0.0296 -0.0492 0.0087  198 TRP A CB  
1465 C CG  . TRP A 209 ? 0.7486 0.6375 0.6761 -0.0340 -0.0584 0.0114  198 TRP A CG  
1466 C CD1 . TRP A 209 ? 0.7561 0.6461 0.6917 -0.0373 -0.0656 0.0134  198 TRP A CD1 
1467 C CD2 . TRP A 209 ? 0.7507 0.6379 0.6657 -0.0363 -0.0622 0.0126  198 TRP A CD2 
1468 N NE1 . TRP A 209 ? 0.7611 0.6502 0.6899 -0.0417 -0.0746 0.0157  198 TRP A NE1 
1469 C CE2 . TRP A 209 ? 0.7611 0.6482 0.6761 -0.0412 -0.0725 0.0154  198 TRP A CE2 
1470 C CE3 . TRP A 209 ? 0.7570 0.6427 0.6609 -0.0351 -0.0581 0.0121  198 TRP A CE3 
1471 C CZ2 . TRP A 209 ? 0.7685 0.6539 0.6713 -0.0448 -0.0792 0.0181  198 TRP A CZ2 
1472 C CZ3 . TRP A 209 ? 0.7676 0.6516 0.6598 -0.0384 -0.0637 0.0148  198 TRP A CZ3 
1473 C CH2 . TRP A 209 ? 0.7698 0.6534 0.6603 -0.0433 -0.0743 0.0176  198 TRP A CH2 
1474 N N   . TYR A 210 ? 0.7124 0.6059 0.6625 -0.0211 -0.0340 0.0118  199 TYR A N   
1475 C CA  . TYR A 210 ? 0.6982 0.5901 0.6457 -0.0183 -0.0274 0.0098  199 TYR A CA  
1476 C C   . TYR A 210 ? 0.7004 0.5932 0.6562 -0.0166 -0.0234 0.0119  199 TYR A C   
1477 O O   . TYR A 210 ? 0.7063 0.5969 0.6586 -0.0147 -0.0186 0.0106  199 TYR A O   
1478 C CB  . TYR A 210 ? 0.6816 0.5732 0.6255 -0.0167 -0.0247 0.0107  199 TYR A CB  
1479 C CG  . TYR A 210 ? 0.6719 0.5627 0.6072 -0.0186 -0.0281 0.0098  199 TYR A CG  
1480 C CD1 . TYR A 210 ? 0.6749 0.5677 0.6118 -0.0204 -0.0333 0.0138  199 TYR A CD1 
1481 C CD2 . TYR A 210 ? 0.6784 0.5664 0.6041 -0.0190 -0.0264 0.0052  199 TYR A CD2 
1482 C CE1 . TYR A 210 ? 0.6883 0.5795 0.6143 -0.0228 -0.0366 0.0131  199 TYR A CE1 
1483 C CE2 . TYR A 210 ? 0.6913 0.5779 0.6076 -0.0209 -0.0283 0.0041  199 TYR A CE2 
1484 C CZ  . TYR A 210 ? 0.7026 0.5903 0.6174 -0.0230 -0.0334 0.0079  199 TYR A CZ  
1485 O OH  . TYR A 210 ? 0.7194 0.6049 0.6222 -0.0252 -0.0352 0.0073  199 TYR A OH  
1486 N N   . ARG A 211 ? 0.6944 0.5901 0.6606 -0.0176 -0.0256 0.0154  200 ARG A N   
1487 C CA  . ARG A 211 ? 0.6958 0.5924 0.6700 -0.0161 -0.0208 0.0181  200 ARG A CA  
1488 C C   . ARG A 211 ? 0.6882 0.5822 0.6594 -0.0170 -0.0209 0.0156  200 ARG A C   
1489 O O   . ARG A 211 ? 0.6916 0.5849 0.6634 -0.0195 -0.0260 0.0139  200 ARG A O   
1490 C CB  . ARG A 211 ? 0.7156 0.6173 0.7055 -0.0164 -0.0218 0.0242  200 ARG A CB  
1491 C CG  . ARG A 211 ? 0.7790 0.6837 0.7747 -0.0153 -0.0226 0.0280  200 ARG A CG  
1492 C CD  . ARG A 211 ? 0.8539 0.7554 0.8421 -0.0123 -0.0168 0.0262  200 ARG A CD  
1493 N NE  . ARG A 211 ? 0.9137 0.8178 0.9137 -0.0098 -0.0134 0.0313  200 ARG A NE  
1494 C CZ  . ARG A 211 ? 0.9549 0.8563 0.9565 -0.0064 -0.0045 0.0314  200 ARG A CZ  
1495 N NH1 . ARG A 211 ? 0.9462 0.8495 0.9603 -0.0038 -0.0009 0.0359  200 ARG A NH1 
1496 N NH2 . ARG A 211 ? 0.9615 0.8578 0.9518 -0.0057 0.0008  0.0270  200 ARG A NH2 
1497 N N   . ALA A 212 ? 0.6727 0.5643 0.6396 -0.0153 -0.0155 0.0151  201 ALA A N   
1498 C CA  . ALA A 212 ? 0.6622 0.5513 0.6268 -0.0159 -0.0153 0.0140  201 ALA A CA  
1499 C C   . ALA A 212 ? 0.6481 0.5392 0.6238 -0.0175 -0.0169 0.0174  201 ALA A C   
1500 O O   . ALA A 212 ? 0.6457 0.5405 0.6317 -0.0176 -0.0161 0.0216  201 ALA A O   
1501 C CB  . ALA A 212 ? 0.6644 0.5506 0.6223 -0.0141 -0.0096 0.0146  201 ALA A CB  
1502 N N   . PRO A 213 ? 0.6367 0.5254 0.6126 -0.0190 -0.0196 0.0160  202 PRO A N   
1503 C CA  . PRO A 213 ? 0.6273 0.5173 0.6148 -0.0210 -0.0216 0.0193  202 PRO A CA  
1504 C C   . PRO A 213 ? 0.6240 0.5164 0.6189 -0.0201 -0.0157 0.0255  202 PRO A C   
1505 O O   . PRO A 213 ? 0.6230 0.5188 0.6310 -0.0216 -0.0167 0.0297  202 PRO A O   
1506 C CB  . PRO A 213 ? 0.6346 0.5202 0.6197 -0.0221 -0.0242 0.0164  202 PRO A CB  
1507 C CG  . PRO A 213 ? 0.6451 0.5282 0.6192 -0.0200 -0.0217 0.0139  202 PRO A CG  
1508 C CD  . PRO A 213 ? 0.6296 0.5144 0.5975 -0.0188 -0.0207 0.0119  202 PRO A CD  
1509 N N   . GLU A 214 ? 0.6209 0.5112 0.6072 -0.0179 -0.0096 0.0263  203 GLU A N   
1510 C CA  . GLU A 214 ? 0.6154 0.5067 0.6054 -0.0169 -0.0023 0.0317  203 GLU A CA  
1511 C C   . GLU A 214 ? 0.6051 0.5008 0.6049 -0.0156 0.0014  0.0346  203 GLU A C   
1512 O O   . GLU A 214 ? 0.6017 0.5007 0.6139 -0.0157 0.0053  0.0401  203 GLU A O   
1513 C CB  . GLU A 214 ? 0.6443 0.5305 0.6191 -0.0155 0.0028  0.0311  203 GLU A CB  
1514 C CG  . GLU A 214 ? 0.6916 0.5755 0.6553 -0.0136 0.0049  0.0271  203 GLU A CG  
1515 C CD  . GLU A 214 ? 0.7574 0.6386 0.7113 -0.0141 -0.0005 0.0220  203 GLU A CD  
1516 O OE1 . GLU A 214 ? 0.7708 0.6532 0.7291 -0.0154 -0.0064 0.0202  203 GLU A OE1 
1517 O OE2 . GLU A 214 ? 0.7846 0.6621 0.7267 -0.0133 0.0015  0.0198  203 GLU A OE2 
1518 N N   . LEU A 215 ? 0.5987 0.4951 0.5956 -0.0144 -0.0001 0.0318  204 LEU A N   
1519 C CA  . LEU A 215 ? 0.5938 0.4946 0.6023 -0.0130 0.0026  0.0352  204 LEU A CA  
1520 C C   . LEU A 215 ? 0.6034 0.5102 0.6296 -0.0155 -0.0035 0.0392  204 LEU A C   
1521 O O   . LEU A 215 ? 0.6052 0.5167 0.6472 -0.0148 0.0002  0.0451  204 LEU A O   
1522 C CB  . LEU A 215 ? 0.5876 0.4875 0.5893 -0.0116 0.0010  0.0317  204 LEU A CB  
1523 C CG  . LEU A 215 ? 0.6010 0.4958 0.5907 -0.0089 0.0085  0.0293  204 LEU A CG  
1524 C CD1 . LEU A 215 ? 0.6131 0.5066 0.5966 -0.0083 0.0056  0.0258  204 LEU A CD1 
1525 C CD2 . LEU A 215 ? 0.5969 0.4920 0.5943 -0.0062 0.0185  0.0334  204 LEU A CD2 
1526 N N   . LEU A 216 ? 0.6063 0.5122 0.6301 -0.0187 -0.0127 0.0361  205 LEU A N   
1527 C CA  . LEU A 216 ? 0.6077 0.5174 0.6457 -0.0223 -0.0203 0.0389  205 LEU A CA  
1528 C C   . LEU A 216 ? 0.6116 0.5232 0.6629 -0.0236 -0.0179 0.0439  205 LEU A C   
1529 O O   . LEU A 216 ? 0.6105 0.5260 0.6772 -0.0267 -0.0235 0.0476  205 LEU A O   
1530 C CB  . LEU A 216 ? 0.6143 0.5201 0.6428 -0.0254 -0.0295 0.0329  205 LEU A CB  
1531 C CG  . LEU A 216 ? 0.6400 0.5439 0.6551 -0.0245 -0.0316 0.0283  205 LEU A CG  
1532 C CD1 . LEU A 216 ? 0.6549 0.5534 0.6577 -0.0267 -0.0371 0.0216  205 LEU A CD1 
1533 C CD2 . LEU A 216 ? 0.6463 0.5551 0.6698 -0.0252 -0.0357 0.0322  205 LEU A CD2 
1534 N N   . LEU A 217 ? 0.6174 0.5260 0.6625 -0.0218 -0.0103 0.0446  206 LEU A N   
1535 C CA  . LEU A 217 ? 0.6264 0.5363 0.6825 -0.0229 -0.0066 0.0501  206 LEU A CA  
1536 C C   . LEU A 217 ? 0.6461 0.5586 0.7081 -0.0198 0.0053  0.0560  206 LEU A C   
1537 O O   . LEU A 217 ? 0.6423 0.5545 0.7081 -0.0200 0.0112  0.0605  206 LEU A O   
1538 C CB  . LEU A 217 ? 0.6278 0.5316 0.6729 -0.0239 -0.0076 0.0475  206 LEU A CB  
1539 C CG  . LEU A 217 ? 0.6381 0.5389 0.6820 -0.0270 -0.0179 0.0424  206 LEU A CG  
1540 C CD1 . LEU A 217 ? 0.6512 0.5457 0.6821 -0.0266 -0.0183 0.0384  206 LEU A CD1 
1541 C CD2 . LEU A 217 ? 0.6359 0.5392 0.6979 -0.0310 -0.0233 0.0462  206 LEU A CD2 
1542 N N   . GLY A 218 ? 0.6637 0.5787 0.7277 -0.0170 0.0090  0.0562  207 GLY A N   
1543 C CA  . GLY A 218 ? 0.6812 0.5981 0.7521 -0.0136 0.0212  0.0610  207 GLY A CA  
1544 C C   . GLY A 218 ? 0.7126 0.6223 0.7634 -0.0108 0.0312  0.0583  207 GLY A C   
1545 O O   . GLY A 218 ? 0.7183 0.6277 0.7722 -0.0089 0.0425  0.0625  207 GLY A O   
1546 N N   . ALA A 219 ? 0.7318 0.6353 0.7618 -0.0107 0.0277  0.0513  208 ALA A N   
1547 C CA  . ALA A 219 ? 0.7566 0.6524 0.7662 -0.0087 0.0357  0.0484  208 ALA A CA  
1548 C C   . ALA A 219 ? 0.7706 0.6659 0.7830 -0.0050 0.0454  0.0487  208 ALA A C   
1549 O O   . ALA A 219 ? 0.7627 0.6618 0.7849 -0.0038 0.0423  0.0482  208 ALA A O   
1550 C CB  . ALA A 219 ? 0.7683 0.6590 0.7598 -0.0095 0.0287  0.0415  208 ALA A CB  
1551 N N   . ARG A 220 ? 0.7883 0.6790 0.7936 -0.0031 0.0575  0.0504  209 ARG A N   
1552 C CA  . ARG A 220 ? 0.8023 0.6916 0.8122 0.0009  0.0691  0.0509  209 ARG A CA  
1553 C C   . ARG A 220 ? 0.8134 0.6937 0.8034 0.0027  0.0717  0.0436  209 ARG A C   
1554 O O   . ARG A 220 ? 0.8163 0.6935 0.8085 0.0061  0.0822  0.0431  209 ARG A O   
1555 C CB  . ARG A 220 ? 0.8289 0.7172 0.8424 0.0023  0.0832  0.0562  209 ARG A CB  
1556 C CG  . ARG A 220 ? 0.8888 0.7771 0.8979 -0.0010 0.0817  0.0602  209 ARG A CG  
1557 C CD  . ARG A 220 ? 0.9420 0.8383 0.9759 -0.0010 0.0877  0.0692  209 ARG A CD  
1558 N NE  . ARG A 220 ? 0.9788 0.8858 1.0405 -0.0016 0.0792  0.0725  209 ARG A NE  
1559 C CZ  . ARG A 220 ? 0.9916 0.9070 1.0777 -0.0034 0.0783  0.0802  209 ARG A CZ  
1560 N NH1 . ARG A 220 ? 0.9785 0.8933 1.0655 -0.0044 0.0860  0.0857  209 ARG A NH1 
1561 N NH2 . ARG A 220 ? 0.9763 0.9005 1.0857 -0.0046 0.0689  0.0829  209 ARG A NH2 
1562 N N   . HIS A 221 ? 0.8156 0.6915 0.7878 0.0004  0.0627  0.0380  210 HIS A N   
1563 C CA  . HIS A 221 ? 0.8209 0.6880 0.7748 0.0014  0.0642  0.0313  210 HIS A CA  
1564 C C   . HIS A 221 ? 0.8054 0.6734 0.7548 -0.0005 0.0520  0.0271  210 HIS A C   
1565 O O   . HIS A 221 ? 0.8103 0.6822 0.7607 -0.0031 0.0429  0.0276  210 HIS A O   
1566 C CB  . HIS A 221 ? 0.8529 0.7094 0.7813 0.0000  0.0692  0.0286  210 HIS A CB  
1567 C CG  . HIS A 221 ? 0.8991 0.7537 0.8267 0.0008  0.0809  0.0331  210 HIS A CG  
1568 N ND1 . HIS A 221 ? 0.9247 0.7763 0.8570 0.0045  0.0949  0.0338  210 HIS A ND1 
1569 C CD2 . HIS A 221 ? 0.9208 0.7759 0.8442 -0.0015 0.0811  0.0376  210 HIS A CD2 
1570 C CE1 . HIS A 221 ? 0.9369 0.7875 0.8671 0.0043  0.1037  0.0385  210 HIS A CE1 
1571 N NE2 . HIS A 221 ? 0.9390 0.7916 0.8634 0.0005  0.0955  0.0412  210 HIS A NE2 
1572 N N   . TYR A 222 ? 0.7890 0.6525 0.7323 0.0008  0.0526  0.0226  211 TYR A N   
1573 C CA  . TYR A 222 ? 0.7795 0.6428 0.7166 -0.0009 0.0427  0.0185  211 TYR A CA  
1574 C C   . TYR A 222 ? 0.7683 0.6230 0.6830 -0.0032 0.0414  0.0142  211 TYR A C   
1575 O O   . TYR A 222 ? 0.7802 0.6264 0.6817 -0.0027 0.0492  0.0124  211 TYR A O   
1576 C CB  . TYR A 222 ? 0.7859 0.6487 0.7290 0.0012  0.0434  0.0168  211 TYR A CB  
1577 C CG  . TYR A 222 ? 0.7982 0.6708 0.7618 0.0017  0.0384  0.0212  211 TYR A CG  
1578 C CD1 . TYR A 222 ? 0.8120 0.6898 0.7773 -0.0008 0.0277  0.0210  211 TYR A CD1 
1579 C CD2 . TYR A 222 ? 0.8104 0.6868 0.7916 0.0046  0.0443  0.0258  211 TYR A CD2 
1580 C CE1 . TYR A 222 ? 0.8192 0.7047 0.8001 -0.0011 0.0223  0.0249  211 TYR A CE1 
1581 C CE2 . TYR A 222 ? 0.8159 0.7013 0.8157 0.0045  0.0381  0.0306  211 TYR A CE2 
1582 C CZ  . TYR A 222 ? 0.8281 0.7176 0.8262 0.0013  0.0267  0.0300  211 TYR A CZ  
1583 O OH  . TYR A 222 ? 0.8449 0.7420 0.8581 0.0003  0.0196  0.0345  211 TYR A OH  
1584 N N   . THR A 223 ? 0.7394 0.5959 0.6499 -0.0058 0.0317  0.0128  212 THR A N   
1585 C CA  . THR A 223 ? 0.7193 0.5692 0.6117 -0.0084 0.0282  0.0098  212 THR A CA  
1586 C C   . THR A 223 ? 0.6933 0.5441 0.5846 -0.0097 0.0199  0.0063  212 THR A C   
1587 O O   . THR A 223 ? 0.6902 0.5465 0.5931 -0.0087 0.0173  0.0063  212 THR A O   
1588 C CB  . THR A 223 ? 0.7283 0.5803 0.6197 -0.0102 0.0252  0.0135  212 THR A CB  
1589 O OG1 . THR A 223 ? 0.7300 0.5902 0.6358 -0.0106 0.0185  0.0151  212 THR A OG1 
1590 C CG2 . THR A 223 ? 0.7355 0.5865 0.6274 -0.0093 0.0340  0.0176  212 THR A CG2 
1591 N N   . LYS A 224 ? 0.6730 0.5182 0.5506 -0.0122 0.0156  0.0038  213 LYS A N   
1592 C CA  . LYS A 224 ? 0.6522 0.4987 0.5303 -0.0136 0.0083  0.0012  213 LYS A CA  
1593 C C   . LYS A 224 ? 0.6420 0.4972 0.5326 -0.0137 0.0024  0.0032  213 LYS A C   
1594 O O   . LYS A 224 ? 0.6371 0.4961 0.5345 -0.0134 -0.0006 0.0019  213 LYS A O   
1595 C CB  . LYS A 224 ? 0.6592 0.4987 0.5219 -0.0168 0.0041  -0.0006 213 LYS A CB  
1596 C CG  . LYS A 224 ? 0.6933 0.5220 0.5398 -0.0174 0.0097  -0.0035 213 LYS A CG  
1597 C CD  . LYS A 224 ? 0.7503 0.5718 0.5816 -0.0215 0.0031  -0.0057 213 LYS A CD  
1598 C CE  . LYS A 224 ? 0.8118 0.6205 0.6251 -0.0227 0.0080  -0.0103 213 LYS A CE  
1599 N NZ  . LYS A 224 ? 0.8477 0.6491 0.6464 -0.0276 -0.0003 -0.0125 213 LYS A NZ  
1600 N N   . ALA A 225 ? 0.6326 0.4900 0.5253 -0.0143 0.0012  0.0064  214 ALA A N   
1601 C CA  . ALA A 225 ? 0.6159 0.4795 0.5196 -0.0145 -0.0037 0.0077  214 ALA A CA  
1602 C C   . ALA A 225 ? 0.6016 0.4707 0.5171 -0.0130 -0.0029 0.0078  214 ALA A C   
1603 O O   . ALA A 225 ? 0.6042 0.4769 0.5261 -0.0134 -0.0070 0.0070  214 ALA A O   
1604 C CB  . ALA A 225 ? 0.6154 0.4791 0.5197 -0.0153 -0.0042 0.0115  214 ALA A CB  
1605 N N   . ILE A 226 ? 0.5856 0.4548 0.5039 -0.0115 0.0024  0.0089  215 ILE A N   
1606 C CA  . ILE A 226 ? 0.5717 0.4461 0.5014 -0.0105 0.0018  0.0099  215 ILE A CA  
1607 C C   . ILE A 226 ? 0.5604 0.4352 0.4887 -0.0106 -0.0011 0.0070  215 ILE A C   
1608 O O   . ILE A 226 ? 0.5594 0.4380 0.4928 -0.0111 -0.0050 0.0067  215 ILE A O   
1609 C CB  . ILE A 226 ? 0.5811 0.4561 0.5171 -0.0087 0.0083  0.0129  215 ILE A CB  
1610 C CG1 . ILE A 226 ? 0.5874 0.4646 0.5296 -0.0091 0.0101  0.0168  215 ILE A CG1 
1611 C CG2 . ILE A 226 ? 0.5869 0.4663 0.5336 -0.0077 0.0072  0.0142  215 ILE A CG2 
1612 C CD1 . ILE A 226 ? 0.5979 0.4753 0.5463 -0.0072 0.0182  0.0203  215 ILE A CD1 
1613 N N   . ASP A 227 ? 0.5560 0.4261 0.4762 -0.0104 0.0008  0.0047  216 ASP A N   
1614 C CA  . ASP A 227 ? 0.5528 0.4230 0.4720 -0.0107 -0.0016 0.0026  216 ASP A CA  
1615 C C   . ASP A 227 ? 0.5483 0.4203 0.4664 -0.0123 -0.0066 0.0010  216 ASP A C   
1616 O O   . ASP A 227 ? 0.5500 0.4244 0.4706 -0.0125 -0.0086 0.0002  216 ASP A O   
1617 C CB  . ASP A 227 ? 0.5747 0.4383 0.4860 -0.0107 0.0012  0.0004  216 ASP A CB  
1618 C CG  . ASP A 227 ? 0.6339 0.4942 0.5465 -0.0086 0.0077  0.0011  216 ASP A CG  
1619 O OD1 . ASP A 227 ? 0.6323 0.4969 0.5546 -0.0069 0.0097  0.0043  216 ASP A OD1 
1620 O OD2 . ASP A 227 ? 0.6646 0.5176 0.5693 -0.0086 0.0107  -0.0015 216 ASP A OD2 
1621 N N   . ILE A 228 ? 0.5403 0.4108 0.4550 -0.0133 -0.0083 0.0009  217 ILE A N   
1622 C CA  . ILE A 228 ? 0.5337 0.4059 0.4502 -0.0143 -0.0125 0.0000  217 ILE A CA  
1623 C C   . ILE A 228 ? 0.5282 0.4045 0.4519 -0.0140 -0.0138 0.0001  217 ILE A C   
1624 O O   . ILE A 228 ? 0.5364 0.4144 0.4622 -0.0141 -0.0152 -0.0017 217 ILE A O   
1625 C CB  . ILE A 228 ? 0.5386 0.4081 0.4507 -0.0156 -0.0146 0.0011  217 ILE A CB  
1626 C CG1 . ILE A 228 ? 0.5599 0.4247 0.4636 -0.0170 -0.0155 -0.0002 217 ILE A CG1 
1627 C CG2 . ILE A 228 ? 0.5348 0.4070 0.4533 -0.0159 -0.0184 0.0015  217 ILE A CG2 
1628 C CD1 . ILE A 228 ? 0.5753 0.4418 0.4827 -0.0175 -0.0176 -0.0019 217 ILE A CD1 
1629 N N   . TRP A 229 ? 0.5104 0.3879 0.4378 -0.0137 -0.0129 0.0019  218 TRP A N   
1630 C CA  . TRP A 229 ? 0.5000 0.3801 0.4332 -0.0140 -0.0150 0.0015  218 TRP A CA  
1631 C C   . TRP A 229 ? 0.5012 0.3828 0.4339 -0.0141 -0.0156 0.0001  218 TRP A C   
1632 O O   . TRP A 229 ? 0.5029 0.3849 0.4353 -0.0148 -0.0173 -0.0023 218 TRP A O   
1633 C CB  . TRP A 229 ? 0.4919 0.3732 0.4308 -0.0142 -0.0145 0.0045  218 TRP A CB  
1634 C CG  . TRP A 229 ? 0.4922 0.3752 0.4365 -0.0154 -0.0179 0.0038  218 TRP A CG  
1635 C CD1 . TRP A 229 ? 0.4990 0.3841 0.4456 -0.0162 -0.0197 0.0042  218 TRP A CD1 
1636 C CD2 . TRP A 229 ? 0.4903 0.3720 0.4378 -0.0165 -0.0204 0.0024  218 TRP A CD2 
1637 N NE1 . TRP A 229 ? 0.4999 0.3846 0.4489 -0.0181 -0.0236 0.0026  218 TRP A NE1 
1638 C CE2 . TRP A 229 ? 0.4963 0.3786 0.4463 -0.0181 -0.0237 0.0011  218 TRP A CE2 
1639 C CE3 . TRP A 229 ? 0.4925 0.3721 0.4413 -0.0164 -0.0207 0.0023  218 TRP A CE3 
1640 C CZ2 . TRP A 229 ? 0.4976 0.3773 0.4502 -0.0196 -0.0265 -0.0013 218 TRP A CZ2 
1641 C CZ3 . TRP A 229 ? 0.4957 0.3735 0.4492 -0.0173 -0.0231 0.0005  218 TRP A CZ3 
1642 C CH2 . TRP A 229 ? 0.4944 0.3717 0.4493 -0.0189 -0.0257 -0.0017 218 TRP A CH2 
1643 N N   . ALA A 230 ? 0.4974 0.3794 0.4294 -0.0134 -0.0137 0.0016  219 ALA A N   
1644 C CA  . ALA A 230 ? 0.4980 0.3814 0.4295 -0.0136 -0.0144 0.0018  219 ALA A CA  
1645 C C   . ALA A 230 ? 0.4943 0.3769 0.4211 -0.0140 -0.0145 -0.0008 219 ALA A C   
1646 O O   . ALA A 230 ? 0.4910 0.3746 0.4159 -0.0148 -0.0157 -0.0015 219 ALA A O   
1647 C CB  . ALA A 230 ? 0.5036 0.3866 0.4370 -0.0123 -0.0116 0.0043  219 ALA A CB  
1648 N N   . ILE A 231 ? 0.4942 0.3749 0.4190 -0.0137 -0.0133 -0.0019 220 ILE A N   
1649 C CA  . ILE A 231 ? 0.5041 0.3848 0.4277 -0.0142 -0.0131 -0.0036 220 ILE A CA  
1650 C C   . ILE A 231 ? 0.5212 0.4031 0.4463 -0.0145 -0.0138 -0.0056 220 ILE A C   
1651 O O   . ILE A 231 ? 0.5259 0.4085 0.4500 -0.0147 -0.0125 -0.0068 220 ILE A O   
1652 C CB  . ILE A 231 ? 0.5069 0.3853 0.4294 -0.0146 -0.0132 -0.0038 220 ILE A CB  
1653 C CG1 . ILE A 231 ? 0.5106 0.3859 0.4301 -0.0144 -0.0115 -0.0030 220 ILE A CG1 
1654 C CG2 . ILE A 231 ? 0.5113 0.3909 0.4364 -0.0153 -0.0137 -0.0048 220 ILE A CG2 
1655 C CD1 . ILE A 231 ? 0.5206 0.3917 0.4360 -0.0154 -0.0121 -0.0038 220 ILE A CD1 
1656 N N   . GLY A 232 ? 0.5262 0.4077 0.4538 -0.0143 -0.0151 -0.0060 221 GLY A N   
1657 C CA  . GLY A 232 ? 0.5301 0.4112 0.4599 -0.0144 -0.0153 -0.0084 221 GLY A CA  
1658 C C   . GLY A 232 ? 0.5334 0.4141 0.4591 -0.0152 -0.0154 -0.0102 221 GLY A C   
1659 O O   . GLY A 232 ? 0.5412 0.4208 0.4649 -0.0153 -0.0136 -0.0131 221 GLY A O   
1660 N N   . CYS A 233 ? 0.5285 0.4098 0.4528 -0.0160 -0.0175 -0.0082 222 CYS A N   
1661 C CA  . CYS A 233 ? 0.5310 0.4117 0.4502 -0.0177 -0.0194 -0.0090 222 CYS A CA  
1662 C C   . CYS A 233 ? 0.5279 0.4087 0.4407 -0.0179 -0.0174 -0.0091 222 CYS A C   
1663 O O   . CYS A 233 ? 0.5305 0.4092 0.4360 -0.0192 -0.0174 -0.0114 222 CYS A O   
1664 C CB  . CYS A 233 ? 0.5380 0.4204 0.4601 -0.0186 -0.0228 -0.0054 222 CYS A CB  
1665 S SG  . CYS A 233 ? 0.5757 0.4587 0.5070 -0.0184 -0.0240 -0.0038 222 CYS A SG  
1666 N N   . ILE A 234 ? 0.5216 0.4041 0.4362 -0.0169 -0.0155 -0.0067 223 ILE A N   
1667 C CA  . ILE A 234 ? 0.5263 0.4090 0.4365 -0.0172 -0.0133 -0.0060 223 ILE A CA  
1668 C C   . ILE A 234 ? 0.5469 0.4288 0.4564 -0.0168 -0.0095 -0.0093 223 ILE A C   
1669 O O   . ILE A 234 ? 0.5599 0.4408 0.4629 -0.0176 -0.0073 -0.0103 223 ILE A O   
1670 C CB  . ILE A 234 ? 0.5199 0.4036 0.4334 -0.0164 -0.0125 -0.0028 223 ILE A CB  
1671 C CG1 . ILE A 234 ? 0.5247 0.4090 0.4412 -0.0161 -0.0149 0.0005  223 ILE A CG1 
1672 C CG2 . ILE A 234 ? 0.5178 0.4017 0.4279 -0.0170 -0.0103 -0.0012 223 ILE A CG2 
1673 C CD1 . ILE A 234 ? 0.5301 0.4136 0.4504 -0.0149 -0.0131 0.0023  223 ILE A CD1 
1674 N N   . PHE A 235 ? 0.5480 0.4303 0.4644 -0.0156 -0.0088 -0.0106 224 PHE A N   
1675 C CA  . PHE A 235 ? 0.5597 0.4420 0.4796 -0.0148 -0.0051 -0.0129 224 PHE A CA  
1676 C C   . PHE A 235 ? 0.5811 0.4603 0.4959 -0.0150 -0.0030 -0.0169 224 PHE A C   
1677 O O   . PHE A 235 ? 0.5855 0.4638 0.4974 -0.0148 0.0019  -0.0187 224 PHE A O   
1678 C CB  . PHE A 235 ? 0.5551 0.4385 0.4845 -0.0138 -0.0064 -0.0124 224 PHE A CB  
1679 C CG  . PHE A 235 ? 0.5588 0.4434 0.4964 -0.0128 -0.0032 -0.0132 224 PHE A CG  
1680 C CD1 . PHE A 235 ? 0.5676 0.4536 0.5054 -0.0128 0.0016  -0.0134 224 PHE A CD1 
1681 C CD2 . PHE A 235 ? 0.5600 0.4451 0.5067 -0.0119 -0.0049 -0.0129 224 PHE A CD2 
1682 C CE1 . PHE A 235 ? 0.5706 0.4585 0.5189 -0.0116 0.0053  -0.0135 224 PHE A CE1 
1683 C CE2 . PHE A 235 ? 0.5624 0.4494 0.5198 -0.0107 -0.0022 -0.0127 224 PHE A CE2 
1684 C CZ  . PHE A 235 ? 0.5607 0.4494 0.5197 -0.0104 0.0032  -0.0131 224 PHE A CZ  
1685 N N   . ALA A 236 ? 0.5954 0.4722 0.5080 -0.0157 -0.0064 -0.0184 225 ALA A N   
1686 C CA  . ALA A 236 ? 0.6153 0.4873 0.5212 -0.0166 -0.0052 -0.0231 225 ALA A CA  
1687 C C   . ALA A 236 ? 0.6433 0.5132 0.5355 -0.0187 -0.0049 -0.0236 225 ALA A C   
1688 O O   . ALA A 236 ? 0.6567 0.5221 0.5404 -0.0193 -0.0010 -0.0277 225 ALA A O   
1689 C CB  . ALA A 236 ? 0.6101 0.4799 0.5182 -0.0175 -0.0100 -0.0241 225 ALA A CB  
1690 N N   . GLU A 237 ? 0.6494 0.5222 0.5392 -0.0199 -0.0086 -0.0190 226 GLU A N   
1691 C CA  . GLU A 237 ? 0.6659 0.5372 0.5433 -0.0221 -0.0094 -0.0176 226 GLU A CA  
1692 C C   . GLU A 237 ? 0.6780 0.5499 0.5519 -0.0214 -0.0029 -0.0170 226 GLU A C   
1693 O O   . GLU A 237 ? 0.6870 0.5559 0.5479 -0.0233 -0.0012 -0.0174 226 GLU A O   
1694 C CB  . GLU A 237 ? 0.6914 0.5660 0.5711 -0.0230 -0.0153 -0.0119 226 GLU A CB  
1695 C CG  . GLU A 237 ? 0.7627 0.6353 0.6302 -0.0262 -0.0195 -0.0099 226 GLU A CG  
1696 C CD  . GLU A 237 ? 0.8486 0.7248 0.7223 -0.0270 -0.0262 -0.0040 226 GLU A CD  
1697 O OE1 . GLU A 237 ? 0.8477 0.7268 0.7338 -0.0252 -0.0272 -0.0028 226 GLU A OE1 
1698 O OE2 . GLU A 237 ? 0.8903 0.7663 0.7567 -0.0293 -0.0302 -0.0001 226 GLU A OE2 
1699 N N   . LEU A 238 ? 0.6761 0.5517 0.5613 -0.0192 0.0005  -0.0155 227 LEU A N   
1700 C CA  . LEU A 238 ? 0.6840 0.5609 0.5694 -0.0187 0.0068  -0.0144 227 LEU A CA  
1701 C C   . LEU A 238 ? 0.7011 0.5751 0.5854 -0.0176 0.0139  -0.0195 227 LEU A C   
1702 O O   . LEU A 238 ? 0.7081 0.5808 0.5858 -0.0180 0.0204  -0.0198 227 LEU A O   
1703 C CB  . LEU A 238 ? 0.6712 0.5526 0.5701 -0.0174 0.0068  -0.0110 227 LEU A CB  
1704 C CG  . LEU A 238 ? 0.6721 0.5552 0.5723 -0.0181 0.0025  -0.0064 227 LEU A CG  
1705 C CD1 . LEU A 238 ? 0.6675 0.5530 0.5793 -0.0172 0.0023  -0.0048 227 LEU A CD1 
1706 C CD2 . LEU A 238 ? 0.6744 0.5570 0.5663 -0.0196 0.0038  -0.0028 227 LEU A CD2 
1707 N N   . LEU A 239 ? 0.7026 0.5752 0.5938 -0.0162 0.0133  -0.0231 228 LEU A N   
1708 C CA  . LEU A 239 ? 0.7175 0.5869 0.6105 -0.0146 0.0204  -0.0280 228 LEU A CA  
1709 C C   . LEU A 239 ? 0.7382 0.5996 0.6137 -0.0163 0.0226  -0.0334 228 LEU A C   
1710 O O   . LEU A 239 ? 0.7510 0.6086 0.6234 -0.0152 0.0312  -0.0374 228 LEU A O   
1711 C CB  . LEU A 239 ? 0.7184 0.5885 0.6258 -0.0125 0.0186  -0.0294 228 LEU A CB  
1712 C CG  . LEU A 239 ? 0.7337 0.6103 0.6578 -0.0110 0.0172  -0.0250 228 LEU A CG  
1713 C CD1 . LEU A 239 ? 0.7346 0.6112 0.6700 -0.0096 0.0138  -0.0255 228 LEU A CD1 
1714 C CD2 . LEU A 239 ? 0.7405 0.6201 0.6728 -0.0096 0.0245  -0.0238 228 LEU A CD2 
1715 N N   . THR A 240 ? 0.7407 0.5993 0.6052 -0.0191 0.0152  -0.0336 229 THR A N   
1716 C CA  . THR A 240 ? 0.7535 0.6032 0.5999 -0.0216 0.0154  -0.0392 229 THR A CA  
1717 C C   . THR A 240 ? 0.7722 0.6198 0.5998 -0.0255 0.0117  -0.0367 229 THR A C   
1718 O O   . THR A 240 ? 0.7786 0.6180 0.5877 -0.0280 0.0132  -0.0414 229 THR A O   
1719 C CB  . THR A 240 ? 0.7549 0.6009 0.6039 -0.0226 0.0089  -0.0426 229 THR A CB  
1720 O OG1 . THR A 240 ? 0.7558 0.6059 0.6065 -0.0246 -0.0008 -0.0375 229 THR A OG1 
1721 C CG2 . THR A 240 ? 0.7475 0.5952 0.6149 -0.0191 0.0113  -0.0440 229 THR A CG2 
1722 N N   . SER A 241 ? 0.7804 0.6347 0.6126 -0.0261 0.0062  -0.0294 230 SER A N   
1723 C CA  . SER A 241 ? 0.8005 0.6547 0.6200 -0.0295 0.0004  -0.0245 230 SER A CA  
1724 C C   . SER A 241 ? 0.8213 0.6745 0.6387 -0.0324 -0.0107 -0.0235 230 SER A C   
1725 O O   . SER A 241 ? 0.8214 0.6764 0.6343 -0.0348 -0.0172 -0.0179 230 SER A O   
1726 C CB  . SER A 241 ? 0.8174 0.6657 0.6162 -0.0317 0.0060  -0.0260 230 SER A CB  
1727 O OG  . SER A 241 ? 0.8314 0.6824 0.6354 -0.0291 0.0161  -0.0248 230 SER A OG  
1728 N N   . GLU A 242 ? 0.8368 0.6873 0.6597 -0.0322 -0.0129 -0.0283 231 GLU A N   
1729 C CA  . GLU A 242 ? 0.8556 0.7053 0.6792 -0.0351 -0.0229 -0.0276 231 GLU A CA  
1730 C C   . GLU A 242 ? 0.8568 0.7140 0.7011 -0.0327 -0.0260 -0.0233 231 GLU A C   
1731 O O   . GLU A 242 ? 0.8555 0.7147 0.7113 -0.0292 -0.0209 -0.0248 231 GLU A O   
1732 C CB  . GLU A 242 ? 0.8893 0.7302 0.7063 -0.0367 -0.0229 -0.0359 231 GLU A CB  
1733 C CG  . GLU A 242 ? 0.9701 0.8021 0.7643 -0.0420 -0.0273 -0.0393 231 GLU A CG  
1734 C CD  . GLU A 242 ? 1.0771 0.9038 0.8522 -0.0423 -0.0191 -0.0418 231 GLU A CD  
1735 O OE1 . GLU A 242 ? 1.0956 0.9227 0.8758 -0.0382 -0.0081 -0.0446 231 GLU A OE1 
1736 O OE2 . GLU A 242 ? 1.1164 0.9387 0.8718 -0.0468 -0.0238 -0.0404 231 GLU A OE2 
1737 N N   . PRO A 243 ? 0.8562 0.7169 0.7056 -0.0345 -0.0344 -0.0180 232 PRO A N   
1738 C CA  . PRO A 243 ? 0.8485 0.7152 0.7165 -0.0322 -0.0360 -0.0145 232 PRO A CA  
1739 C C   . PRO A 243 ? 0.8501 0.7132 0.7230 -0.0323 -0.0363 -0.0196 232 PRO A C   
1740 O O   . PRO A 243 ? 0.8544 0.7125 0.7209 -0.0359 -0.0415 -0.0226 232 PRO A O   
1741 C CB  . PRO A 243 ? 0.8511 0.7216 0.7231 -0.0345 -0.0442 -0.0078 232 PRO A CB  
1742 C CG  . PRO A 243 ? 0.8638 0.7315 0.7196 -0.0376 -0.0469 -0.0064 232 PRO A CG  
1743 C CD  . PRO A 243 ? 0.8544 0.7139 0.6939 -0.0389 -0.0428 -0.0145 232 PRO A CD  
1744 N N   . ILE A 244 ? 0.8401 0.7049 0.7232 -0.0288 -0.0309 -0.0209 233 ILE A N   
1745 C CA  . ILE A 244 ? 0.8380 0.6992 0.7267 -0.0285 -0.0305 -0.0251 233 ILE A CA  
1746 C C   . ILE A 244 ? 0.8401 0.7018 0.7360 -0.0310 -0.0377 -0.0229 233 ILE A C   
1747 O O   . ILE A 244 ? 0.8425 0.6982 0.7363 -0.0332 -0.0402 -0.0273 233 ILE A O   
1748 C CB  . ILE A 244 ? 0.8333 0.6973 0.7327 -0.0245 -0.0248 -0.0247 233 ILE A CB  
1749 C CG1 . ILE A 244 ? 0.8439 0.7041 0.7504 -0.0240 -0.0244 -0.0280 233 ILE A CG1 
1750 C CG2 . ILE A 244 ? 0.8303 0.7010 0.7386 -0.0228 -0.0253 -0.0185 233 ILE A CG2 
1751 C CD1 . ILE A 244 ? 0.8544 0.7157 0.7691 -0.0206 -0.0192 -0.0284 233 ILE A CD1 
1752 N N   . PHE A 245 ? 0.8363 0.7044 0.7406 -0.0309 -0.0409 -0.0163 234 PHE A N   
1753 C CA  . PHE A 245 ? 0.8383 0.7082 0.7523 -0.0332 -0.0471 -0.0131 234 PHE A CA  
1754 C C   . PHE A 245 ? 0.8519 0.7233 0.7624 -0.0368 -0.0546 -0.0094 234 PHE A C   
1755 O O   . PHE A 245 ? 0.8411 0.7180 0.7639 -0.0373 -0.0585 -0.0033 234 PHE A O   
1756 C CB  . PHE A 245 ? 0.8262 0.7018 0.7551 -0.0302 -0.0441 -0.0082 234 PHE A CB  
1757 C CG  . PHE A 245 ? 0.8318 0.7054 0.7629 -0.0274 -0.0385 -0.0111 234 PHE A CG  
1758 C CD1 . PHE A 245 ? 0.8399 0.7080 0.7714 -0.0285 -0.0391 -0.0156 234 PHE A CD1 
1759 C CD2 . PHE A 245 ? 0.8387 0.7151 0.7712 -0.0241 -0.0332 -0.0095 234 PHE A CD2 
1760 C CE1 . PHE A 245 ? 0.8440 0.7105 0.7792 -0.0259 -0.0346 -0.0174 234 PHE A CE1 
1761 C CE2 . PHE A 245 ? 0.8426 0.7173 0.7773 -0.0220 -0.0295 -0.0115 234 PHE A CE2 
1762 C CZ  . PHE A 245 ? 0.8389 0.7092 0.7759 -0.0228 -0.0302 -0.0148 234 PHE A CZ  
1763 N N   . HIS A 246 ? 0.8766 0.7429 0.7706 -0.0393 -0.0565 -0.0128 235 HIS A N   
1764 C CA  . HIS A 246 ? 0.9069 0.7736 0.7945 -0.0435 -0.0649 -0.0092 235 HIS A CA  
1765 C C   . HIS A 246 ? 0.9197 0.7851 0.8136 -0.0480 -0.0742 -0.0085 235 HIS A C   
1766 O O   . HIS A 246 ? 0.9272 0.7847 0.8132 -0.0510 -0.0764 -0.0150 235 HIS A O   
1767 C CB  . HIS A 246 ? 0.9451 0.8047 0.8101 -0.0458 -0.0645 -0.0137 235 HIS A CB  
1768 C CG  . HIS A 246 ? 1.0018 0.8602 0.8572 -0.0513 -0.0748 -0.0101 235 HIS A CG  
1769 N ND1 . HIS A 246 ? 1.0381 0.8883 0.8812 -0.0570 -0.0824 -0.0148 235 HIS A ND1 
1770 C CD2 . HIS A 246 ? 1.0177 0.8816 0.8747 -0.0519 -0.0793 -0.0021 235 HIS A CD2 
1771 C CE1 . HIS A 246 ? 1.0470 0.8983 0.8837 -0.0613 -0.0919 -0.0091 235 HIS A CE1 
1772 N NE2 . HIS A 246 ? 1.0393 0.8991 0.8850 -0.0583 -0.0903 -0.0009 235 HIS A NE2 
1773 N N   . CYS A 247 ? 0.9223 0.7951 0.8309 -0.0487 -0.0796 -0.0005 236 CYS A N   
1774 C CA  . CYS A 247 ? 0.9343 0.8082 0.8542 -0.0530 -0.0888 0.0024  236 CYS A CA  
1775 C C   . CYS A 247 ? 0.9489 0.8272 0.8711 -0.0567 -0.0990 0.0100  236 CYS A C   
1776 O O   . CYS A 247 ? 0.9451 0.8285 0.8687 -0.0541 -0.0970 0.0154  236 CYS A O   
1777 C CB  . CYS A 247 ? 0.9337 0.8141 0.8758 -0.0495 -0.0841 0.0063  236 CYS A CB  
1778 S SG  . CYS A 247 ? 0.9720 0.8568 0.9351 -0.0540 -0.0938 0.0124  236 CYS A SG  
1779 N N   . ARG A 248 ? 0.9638 0.8397 0.8865 -0.0630 -0.1107 0.0107  237 ARG A N   
1780 C CA  . ARG A 248 ? 0.9833 0.8634 0.9096 -0.0674 -0.1224 0.0189  237 ARG A CA  
1781 C C   . ARG A 248 ? 0.9866 0.8794 0.9424 -0.0642 -0.1222 0.0299  237 ARG A C   
1782 O O   . ARG A 248 ? 0.9817 0.8786 0.9545 -0.0604 -0.1149 0.0305  237 ARG A O   
1783 C CB  . ARG A 248 ? 1.0116 0.8853 0.9311 -0.0757 -0.1359 0.0165  237 ARG A CB  
1784 C CG  . ARG A 248 ? 1.0572 0.9321 0.9960 -0.0770 -0.1376 0.0161  237 ARG A CG  
1785 C CD  . ARG A 248 ? 1.1175 0.9880 1.0547 -0.0859 -0.1536 0.0166  237 ARG A CD  
1786 N NE  . ARG A 248 ? 1.1686 1.0484 1.1202 -0.0888 -0.1647 0.0283  237 ARG A NE  
1787 C CZ  . ARG A 248 ? 1.2073 1.0977 1.1899 -0.0890 -0.1688 0.0377  237 ARG A CZ  
1788 N NH1 . ARG A 248 ? 1.2067 1.0994 1.2075 -0.0868 -0.1626 0.0367  237 ARG A NH1 
1789 N NH2 . ARG A 248 ? 1.2042 1.1032 1.2010 -0.0914 -0.1789 0.0487  237 ARG A NH2 
1790 N N   . GLN A 249 ? 0.9915 0.8898 0.9531 -0.0658 -0.1298 0.0388  238 GLN A N   
1791 C CA  . GLN A 249 ? 0.9913 0.9012 0.9819 -0.0623 -0.1285 0.0494  238 GLN A CA  
1792 C C   . GLN A 249 ? 0.9885 0.9038 1.0037 -0.0648 -0.1340 0.0539  238 GLN A C   
1793 O O   . GLN A 249 ? 0.9914 0.9080 1.0121 -0.0713 -0.1479 0.0585  238 GLN A O   
1794 C CB  . GLN A 249 ? 1.0151 0.9294 1.0074 -0.0633 -0.1357 0.0584  238 GLN A CB  
1795 C CG  . GLN A 249 ? 1.0731 0.9823 1.0420 -0.0611 -0.1303 0.0550  238 GLN A CG  
1796 C CD  . GLN A 249 ? 1.1306 1.0416 1.0957 -0.0643 -0.1405 0.0636  238 GLN A CD  
1797 O OE1 . GLN A 249 ? 1.1486 1.0631 1.1232 -0.0695 -0.1542 0.0709  238 GLN A OE1 
1798 N NE2 . GLN A 249 ? 1.1387 1.0476 1.0904 -0.0614 -0.1346 0.0636  238 GLN A NE2 
1799 N N   . SER A 255 ? 1.1315 1.0941 1.3100 -0.0216 -0.0461 0.0919  244 SER A N   
1800 C CA  . SER A 255 ? 1.1261 1.0962 1.3340 -0.0184 -0.0370 0.1001  244 SER A CA  
1801 C C   . SER A 255 ? 1.1285 1.0960 1.3330 -0.0182 -0.0278 0.0969  244 SER A C   
1802 O O   . SER A 255 ? 1.1348 1.1003 1.3395 -0.0130 -0.0124 0.0963  244 SER A O   
1803 C CB  . SER A 255 ? 1.1306 1.1107 1.3675 -0.0226 -0.0492 0.1106  244 SER A CB  
1804 O OG  . SER A 255 ? 1.1617 1.1409 1.3930 -0.0300 -0.0626 0.1087  244 SER A OG  
1805 N N   . ASN A 256 ? 1.1199 1.0861 1.3192 -0.0241 -0.0375 0.0946  245 ASN A N   
1806 C CA  . ASN A 256 ? 1.1143 1.0774 1.3092 -0.0249 -0.0315 0.0919  245 ASN A CA  
1807 C C   . ASN A 256 ? 1.1102 1.0630 1.2729 -0.0227 -0.0259 0.0815  245 ASN A C   
1808 O O   . ASN A 256 ? 1.1206 1.0686 1.2642 -0.0245 -0.0339 0.0754  245 ASN A O   
1809 C CB  . ASN A 256 ? 1.1310 1.0951 1.3309 -0.0324 -0.0460 0.0924  245 ASN A CB  
1810 C CG  . ASN A 256 ? 1.1779 1.1374 1.3716 -0.0346 -0.0435 0.0890  245 ASN A CG  
1811 O OD1 . ASN A 256 ? 1.1934 1.1521 1.3877 -0.0309 -0.0303 0.0898  245 ASN A OD1 
1812 N ND2 . ASN A 256 ? 1.1883 1.1439 1.3752 -0.0408 -0.0563 0.0851  245 ASN A ND2 
1813 N N   . PRO A 257 ? 1.0915 1.0407 1.2473 -0.0188 -0.0122 0.0797  246 PRO A N   
1814 C CA  . PRO A 257 ? 1.0852 1.0251 1.2117 -0.0172 -0.0084 0.0705  246 PRO A CA  
1815 C C   . PRO A 257 ? 1.0635 0.9981 1.1747 -0.0216 -0.0169 0.0645  246 PRO A C   
1816 O O   . PRO A 257 ? 1.0746 1.0023 1.1639 -0.0206 -0.0154 0.0575  246 PRO A O   
1817 C CB  . PRO A 257 ? 1.1000 1.0376 1.2250 -0.0129 0.0073  0.0716  246 PRO A CB  
1818 C CG  . PRO A 257 ? 1.1005 1.0454 1.2515 -0.0139 0.0105  0.0802  246 PRO A CG  
1819 C CD  . PRO A 257 ? 1.0741 1.0273 1.2478 -0.0161 0.0003  0.0861  246 PRO A CD  
1820 N N   . TYR A 258 ? 1.0312 0.9688 1.1550 -0.0264 -0.0259 0.0673  247 TYR A N   
1821 C CA  . TYR A 258 ? 1.0156 0.9478 1.1287 -0.0308 -0.0342 0.0620  247 TYR A CA  
1822 C C   . TYR A 258 ? 0.9923 0.9238 1.1018 -0.0353 -0.0483 0.0594  247 TYR A C   
1823 O O   . TYR A 258 ? 0.9834 0.9211 1.1103 -0.0381 -0.0555 0.0653  247 TYR A O   
1824 C CB  . TYR A 258 ? 1.0086 0.9431 1.1385 -0.0335 -0.0337 0.0670  247 TYR A CB  
1825 C CG  . TYR A 258 ? 1.0194 0.9482 1.1434 -0.0386 -0.0428 0.0624  247 TYR A CG  
1826 C CD1 . TYR A 258 ? 1.0249 0.9550 1.1595 -0.0444 -0.0555 0.0635  247 TYR A CD1 
1827 C CD2 . TYR A 258 ? 1.0384 0.9601 1.1479 -0.0377 -0.0389 0.0576  247 TYR A CD2 
1828 C CE1 . TYR A 258 ? 1.0402 0.9634 1.1690 -0.0490 -0.0633 0.0584  247 TYR A CE1 
1829 C CE2 . TYR A 258 ? 1.0532 0.9689 1.1594 -0.0419 -0.0464 0.0534  247 TYR A CE2 
1830 C CZ  . TYR A 258 ? 1.0588 0.9747 1.1741 -0.0475 -0.0582 0.0533  247 TYR A CZ  
1831 O OH  . TYR A 258 ? 1.0773 0.9857 1.1888 -0.0517 -0.0652 0.0483  247 TYR A OH  
1832 N N   . HIS A 259 ? 0.9791 0.9031 1.0659 -0.0362 -0.0521 0.0509  248 HIS A N   
1833 C CA  . HIS A 259 ? 0.9654 0.8869 1.0437 -0.0404 -0.0641 0.0475  248 HIS A CA  
1834 C C   . HIS A 259 ? 0.9404 0.8537 1.0066 -0.0444 -0.0699 0.0402  248 HIS A C   
1835 O O   . HIS A 259 ? 0.9498 0.8569 0.9997 -0.0423 -0.0651 0.0337  248 HIS A O   
1836 C CB  . HIS A 259 ? 0.9921 0.9120 1.0545 -0.0375 -0.0623 0.0444  248 HIS A CB  
1837 C CG  . HIS A 259 ? 1.0353 0.9621 1.1107 -0.0335 -0.0565 0.0512  248 HIS A CG  
1838 N ND1 . HIS A 259 ? 1.0566 0.9903 1.1500 -0.0354 -0.0632 0.0589  248 HIS A ND1 
1839 C CD2 . HIS A 259 ? 1.0554 0.9825 1.1296 -0.0280 -0.0447 0.0517  248 HIS A CD2 
1840 C CE1 . HIS A 259 ? 1.0609 0.9991 1.1644 -0.0303 -0.0544 0.0636  248 HIS A CE1 
1841 N NE2 . HIS A 259 ? 1.0648 0.9985 1.1560 -0.0259 -0.0429 0.0590  248 HIS A NE2 
1842 N N   . HIS A 260 ? 0.9077 0.8208 0.9833 -0.0503 -0.0802 0.0416  249 HIS A N   
1843 C CA  . HIS A 260 ? 0.8863 0.7904 0.9529 -0.0546 -0.0859 0.0346  249 HIS A CA  
1844 C C   . HIS A 260 ? 0.8686 0.7638 0.9098 -0.0557 -0.0895 0.0251  249 HIS A C   
1845 O O   . HIS A 260 ? 0.8702 0.7579 0.8990 -0.0543 -0.0852 0.0181  249 HIS A O   
1846 C CB  . HIS A 260 ? 0.8867 0.7921 0.9704 -0.0613 -0.0968 0.0385  249 HIS A CB  
1847 C CG  . HIS A 260 ? 0.9223 0.8173 0.9984 -0.0657 -0.1021 0.0311  249 HIS A CG  
1848 N ND1 . HIS A 260 ? 0.9568 0.8418 1.0118 -0.0695 -0.1096 0.0221  249 HIS A ND1 
1849 C CD2 . HIS A 260 ? 0.9355 0.8278 1.0223 -0.0669 -0.1002 0.0316  249 HIS A CD2 
1850 C CE1 . HIS A 260 ? 0.9665 0.8428 1.0205 -0.0724 -0.1116 0.0168  249 HIS A CE1 
1851 N NE2 . HIS A 260 ? 0.9591 0.8396 1.0325 -0.0710 -0.1064 0.0225  249 HIS A NE2 
1852 N N   . ASP A 261 ? 0.8502 0.7458 0.8842 -0.0584 -0.0974 0.0254  250 ASP A N   
1853 C CA  . ASP A 261 ? 0.8479 0.7348 0.8569 -0.0601 -0.1007 0.0170  250 ASP A CA  
1854 C C   . ASP A 261 ? 0.8294 0.7140 0.8238 -0.0541 -0.0897 0.0123  250 ASP A C   
1855 O O   . ASP A 261 ? 0.8404 0.7163 0.8171 -0.0545 -0.0884 0.0039  250 ASP A O   
1856 C CB  . ASP A 261 ? 0.8768 0.7653 0.8810 -0.0643 -0.1113 0.0201  250 ASP A CB  
1857 C CG  . ASP A 261 ? 0.9476 0.8376 0.9656 -0.0714 -0.1245 0.0245  250 ASP A CG  
1858 O OD1 . ASP A 261 ? 0.9582 0.8428 0.9802 -0.0748 -0.1273 0.0209  250 ASP A OD1 
1859 O OD2 . ASP A 261 ? 0.9758 0.8722 1.0017 -0.0738 -0.1325 0.0319  250 ASP A OD2 
1860 N N   . GLN A 262 ? 0.7991 0.6910 0.8016 -0.0487 -0.0813 0.0175  251 GLN A N   
1861 C CA  . GLN A 262 ? 0.7817 0.6719 0.7724 -0.0435 -0.0717 0.0138  251 GLN A CA  
1862 C C   . GLN A 262 ? 0.7640 0.6501 0.7546 -0.0415 -0.0654 0.0099  251 GLN A C   
1863 O O   . GLN A 262 ? 0.7705 0.6509 0.7475 -0.0400 -0.0620 0.0035  251 GLN A O   
1864 C CB  . GLN A 262 ? 0.7798 0.6774 0.7777 -0.0390 -0.0655 0.0198  251 GLN A CB  
1865 C CG  . GLN A 262 ? 0.8001 0.6953 0.7852 -0.0346 -0.0570 0.0159  251 GLN A CG  
1866 C CD  . GLN A 262 ? 0.8311 0.7215 0.7981 -0.0357 -0.0595 0.0106  251 GLN A CD  
1867 O OE1 . GLN A 262 ? 0.8464 0.7387 0.8099 -0.0365 -0.0628 0.0131  251 GLN A OE1 
1868 N NE2 . GLN A 262 ? 0.8345 0.7185 0.7903 -0.0357 -0.0574 0.0036  251 GLN A NE2 
1869 N N   . LEU A 263 ? 0.7363 0.6254 0.7430 -0.0416 -0.0641 0.0145  252 LEU A N   
1870 C CA  . LEU A 263 ? 0.7188 0.6041 0.7268 -0.0402 -0.0592 0.0124  252 LEU A CA  
1871 C C   . LEU A 263 ? 0.7154 0.5916 0.7151 -0.0433 -0.0638 0.0048  252 LEU A C   
1872 O O   . LEU A 263 ? 0.7196 0.5908 0.7117 -0.0410 -0.0593 0.0001  252 LEU A O   
1873 C CB  . LEU A 263 ? 0.7022 0.5922 0.7290 -0.0405 -0.0574 0.0196  252 LEU A CB  
1874 C CG  . LEU A 263 ? 0.7060 0.6016 0.7374 -0.0360 -0.0482 0.0251  252 LEU A CG  
1875 C CD1 . LEU A 263 ? 0.7023 0.6028 0.7527 -0.0368 -0.0460 0.0329  252 LEU A CD1 
1876 C CD2 . LEU A 263 ? 0.7131 0.6046 0.7325 -0.0325 -0.0416 0.0216  252 LEU A CD2 
1877 N N   . ASP A 264 ? 0.7072 0.5805 0.7072 -0.0486 -0.0730 0.0033  253 ASP A N   
1878 C CA  . ASP A 264 ? 0.7125 0.5751 0.7022 -0.0521 -0.0775 -0.0050 253 ASP A CA  
1879 C C   . ASP A 264 ? 0.7217 0.5788 0.6911 -0.0497 -0.0733 -0.0126 253 ASP A C   
1880 O O   . ASP A 264 ? 0.7309 0.5802 0.6945 -0.0487 -0.0700 -0.0190 253 ASP A O   
1881 C CB  . ASP A 264 ? 0.7296 0.5902 0.7209 -0.0589 -0.0892 -0.0049 253 ASP A CB  
1882 C CG  . ASP A 264 ? 0.7905 0.6383 0.7645 -0.0631 -0.0943 -0.0149 253 ASP A CG  
1883 O OD1 . ASP A 264 ? 0.7998 0.6396 0.7748 -0.0635 -0.0926 -0.0201 253 ASP A OD1 
1884 O OD2 . ASP A 264 ? 0.8257 0.6710 0.7844 -0.0658 -0.0993 -0.0176 253 ASP A OD2 
1885 N N   . ARG A 265 ? 0.7176 0.5788 0.6782 -0.0485 -0.0728 -0.0111 254 ARG A N   
1886 C CA  . ARG A 265 ? 0.7233 0.5806 0.6660 -0.0463 -0.0683 -0.0168 254 ARG A CA  
1887 C C   . ARG A 265 ? 0.7166 0.5749 0.6610 -0.0407 -0.0586 -0.0177 254 ARG A C   
1888 O O   . ARG A 265 ? 0.7275 0.5798 0.6618 -0.0392 -0.0544 -0.0241 254 ARG A O   
1889 C CB  . ARG A 265 ? 0.7441 0.6068 0.6805 -0.0463 -0.0701 -0.0129 254 ARG A CB  
1890 C CG  . ARG A 265 ? 0.8030 0.6626 0.7224 -0.0439 -0.0646 -0.0174 254 ARG A CG  
1891 C CD  . ARG A 265 ? 0.8615 0.7101 0.7633 -0.0469 -0.0658 -0.0263 254 ARG A CD  
1892 N NE  . ARG A 265 ? 0.9060 0.7517 0.7963 -0.0434 -0.0571 -0.0309 254 ARG A NE  
1893 C CZ  . ARG A 265 ? 0.9528 0.7894 0.8254 -0.0450 -0.0553 -0.0383 254 ARG A CZ  
1894 N NH1 . ARG A 265 ? 0.9590 0.7873 0.8204 -0.0505 -0.0623 -0.0426 254 ARG A NH1 
1895 N NH2 . ARG A 265 ? 0.9604 0.7958 0.8261 -0.0414 -0.0463 -0.0414 254 ARG A NH2 
1896 N N   . ILE A 266 ? 0.6944 0.5598 0.6517 -0.0378 -0.0551 -0.0112 255 ILE A N   
1897 C CA  . ILE A 266 ? 0.6782 0.5443 0.6373 -0.0334 -0.0477 -0.0111 255 ILE A CA  
1898 C C   . ILE A 266 ? 0.6695 0.5287 0.6315 -0.0336 -0.0470 -0.0153 255 ILE A C   
1899 O O   . ILE A 266 ? 0.6707 0.5266 0.6278 -0.0310 -0.0426 -0.0192 255 ILE A O   
1900 C CB  . ILE A 266 ? 0.6701 0.5436 0.6397 -0.0311 -0.0445 -0.0035 255 ILE A CB  
1901 C CG1 . ILE A 266 ? 0.6767 0.5555 0.6424 -0.0296 -0.0431 -0.0006 255 ILE A CG1 
1902 C CG2 . ILE A 266 ? 0.6733 0.5461 0.6451 -0.0279 -0.0390 -0.0029 255 ILE A CG2 
1903 C CD1 . ILE A 266 ? 0.6871 0.5711 0.6589 -0.0266 -0.0378 0.0050  255 ILE A CD1 
1904 N N   . PHE A 267 ? 0.6600 0.5169 0.6311 -0.0368 -0.0516 -0.0143 256 PHE A N   
1905 C CA  . PHE A 267 ? 0.6592 0.5087 0.6350 -0.0372 -0.0513 -0.0178 256 PHE A CA  
1906 C C   . PHE A 267 ? 0.6776 0.5170 0.6416 -0.0386 -0.0520 -0.0274 256 PHE A C   
1907 O O   . PHE A 267 ? 0.6818 0.5148 0.6479 -0.0370 -0.0487 -0.0314 256 PHE A O   
1908 C CB  . PHE A 267 ? 0.6435 0.4933 0.6337 -0.0406 -0.0560 -0.0135 256 PHE A CB  
1909 C CG  . PHE A 267 ? 0.6330 0.4918 0.6350 -0.0393 -0.0538 -0.0040 256 PHE A CG  
1910 C CD1 . PHE A 267 ? 0.6347 0.4972 0.6365 -0.0349 -0.0473 -0.0005 256 PHE A CD1 
1911 C CD2 . PHE A 267 ? 0.6319 0.4950 0.6453 -0.0426 -0.0582 0.0015  256 PHE A CD2 
1912 C CE1 . PHE A 267 ? 0.6347 0.5040 0.6444 -0.0339 -0.0443 0.0075  256 PHE A CE1 
1913 C CE2 . PHE A 267 ? 0.6312 0.5022 0.6553 -0.0410 -0.0544 0.0100  256 PHE A CE2 
1914 C CZ  . PHE A 267 ? 0.6280 0.5014 0.6489 -0.0366 -0.0471 0.0126  256 PHE A CZ  
1915 N N   . ASN A 268 ? 0.6832 0.5207 0.6345 -0.0415 -0.0558 -0.0309 257 ASN A N   
1916 C CA  . ASN A 268 ? 0.7000 0.5268 0.6361 -0.0429 -0.0551 -0.0405 257 ASN A CA  
1917 C C   . ASN A 268 ? 0.7041 0.5306 0.6339 -0.0378 -0.0459 -0.0436 257 ASN A C   
1918 O O   . ASN A 268 ? 0.7089 0.5264 0.6326 -0.0370 -0.0417 -0.0511 257 ASN A O   
1919 C CB  . ASN A 268 ? 0.7283 0.5535 0.6502 -0.0475 -0.0615 -0.0422 257 ASN A CB  
1920 C CG  . ASN A 268 ? 0.7928 0.6111 0.7153 -0.0537 -0.0706 -0.0447 257 ASN A CG  
1921 O OD1 . ASN A 268 ? 0.8202 0.6286 0.7437 -0.0549 -0.0703 -0.0508 257 ASN A OD1 
1922 N ND2 . ASN A 268 ? 0.8065 0.6295 0.7299 -0.0580 -0.0794 -0.0397 257 ASN A ND2 
1923 N N   . VAL A 269 ? 0.6984 0.5344 0.6307 -0.0345 -0.0427 -0.0378 258 VAL A N   
1924 C CA  . VAL A 269 ? 0.7001 0.5373 0.6292 -0.0302 -0.0351 -0.0393 258 VAL A CA  
1925 C C   . VAL A 269 ? 0.7035 0.5428 0.6469 -0.0265 -0.0314 -0.0363 258 VAL A C   
1926 O O   . VAL A 269 ? 0.7046 0.5390 0.6500 -0.0242 -0.0267 -0.0405 258 VAL A O   
1927 C CB  . VAL A 269 ? 0.6944 0.5394 0.6174 -0.0292 -0.0342 -0.0352 258 VAL A CB  
1928 C CG1 . VAL A 269 ? 0.6964 0.5429 0.6177 -0.0252 -0.0268 -0.0364 258 VAL A CG1 
1929 C CG2 . VAL A 269 ? 0.7002 0.5429 0.6094 -0.0331 -0.0387 -0.0370 258 VAL A CG2 
1930 N N   . MET A 270 ? 0.6995 0.5454 0.6529 -0.0262 -0.0335 -0.0289 259 MET A N   
1931 C CA  . MET A 270 ? 0.7014 0.5497 0.6662 -0.0233 -0.0311 -0.0246 259 MET A CA  
1932 C C   . MET A 270 ? 0.7145 0.5570 0.6895 -0.0240 -0.0325 -0.0251 259 MET A C   
1933 O O   . MET A 270 ? 0.7144 0.5552 0.6969 -0.0213 -0.0297 -0.0245 259 MET A O   
1934 C CB  . MET A 270 ? 0.6938 0.5502 0.6623 -0.0229 -0.0319 -0.0166 259 MET A CB  
1935 C CG  . MET A 270 ? 0.6996 0.5613 0.6595 -0.0222 -0.0306 -0.0154 259 MET A CG  
1936 S SD  . MET A 270 ? 0.6642 0.5257 0.6170 -0.0194 -0.0259 -0.0193 259 MET A SD  
1937 C CE  . MET A 270 ? 0.6187 0.4812 0.5813 -0.0167 -0.0240 -0.0158 259 MET A CE  
1938 N N   . GLY A 271 ? 0.7235 0.5632 0.7004 -0.0277 -0.0373 -0.0254 260 GLY A N   
1939 C CA  . GLY A 271 ? 0.7359 0.5704 0.7242 -0.0293 -0.0396 -0.0247 260 GLY A CA  
1940 C C   . GLY A 271 ? 0.7409 0.5821 0.7391 -0.0304 -0.0419 -0.0155 260 GLY A C   
1941 O O   . GLY A 271 ? 0.7448 0.5939 0.7402 -0.0294 -0.0407 -0.0106 260 GLY A O   
1942 N N   . PHE A 272 ? 0.7379 0.5756 0.7479 -0.0324 -0.0444 -0.0131 261 PHE A N   
1943 C CA  . PHE A 272 ? 0.7415 0.5855 0.7613 -0.0334 -0.0452 -0.0039 261 PHE A CA  
1944 C C   . PHE A 272 ? 0.7556 0.6026 0.7787 -0.0299 -0.0410 0.0023  261 PHE A C   
1945 O O   . PHE A 272 ? 0.7542 0.5963 0.7821 -0.0283 -0.0400 0.0016  261 PHE A O   
1946 C CB  . PHE A 272 ? 0.7351 0.5749 0.7669 -0.0376 -0.0497 -0.0025 261 PHE A CB  
1947 C CG  . PHE A 272 ? 0.7320 0.5794 0.7722 -0.0397 -0.0509 0.0059  261 PHE A CG  
1948 C CD1 . PHE A 272 ? 0.7341 0.5858 0.7827 -0.0384 -0.0473 0.0148  261 PHE A CD1 
1949 C CD2 . PHE A 272 ? 0.7419 0.5923 0.7822 -0.0431 -0.0554 0.0054  261 PHE A CD2 
1950 C CE1 . PHE A 272 ? 0.7402 0.5988 0.7970 -0.0400 -0.0466 0.0225  261 PHE A CE1 
1951 C CE2 . PHE A 272 ? 0.7435 0.6016 0.7948 -0.0447 -0.0557 0.0137  261 PHE A CE2 
1952 C CZ  . PHE A 272 ? 0.7365 0.5986 0.7962 -0.0430 -0.0505 0.0220  261 PHE A CZ  
1953 N N   . PRO A 273 ? 0.7655 0.6200 0.7855 -0.0289 -0.0386 0.0085  262 PRO A N   
1954 C CA  . PRO A 273 ? 0.7766 0.6333 0.7963 -0.0263 -0.0355 0.0143  262 PRO A CA  
1955 C C   . PRO A 273 ? 0.7903 0.6445 0.8213 -0.0273 -0.0361 0.0208  262 PRO A C   
1956 O O   . PRO A 273 ? 0.7969 0.6527 0.8352 -0.0298 -0.0364 0.0256  262 PRO A O   
1957 C CB  . PRO A 273 ? 0.7837 0.6472 0.7964 -0.0257 -0.0326 0.0185  262 PRO A CB  
1958 C CG  . PRO A 273 ? 0.7831 0.6490 0.7999 -0.0283 -0.0343 0.0183  262 PRO A CG  
1959 C CD  . PRO A 273 ? 0.7613 0.6221 0.7780 -0.0300 -0.0386 0.0105  262 PRO A CD  
1960 N N   . ALA A 274 ? 0.7929 0.6434 0.8272 -0.0255 -0.0362 0.0216  263 ALA A N   
1961 C CA  . ALA A 274 ? 0.7992 0.6471 0.8442 -0.0262 -0.0370 0.0289  263 ALA A CA  
1962 C C   . ALA A 274 ? 0.8095 0.6626 0.8503 -0.0266 -0.0345 0.0384  263 ALA A C   
1963 O O   . ALA A 274 ? 0.8138 0.6712 0.8426 -0.0255 -0.0321 0.0385  263 ALA A O   
1964 C CB  . ALA A 274 ? 0.8003 0.6440 0.8500 -0.0237 -0.0378 0.0284  263 ALA A CB  
1965 N N   . ASP A 275 ? 0.8133 0.6649 0.8630 -0.0283 -0.0345 0.0463  264 ASP A N   
1966 C CA  . ASP A 275 ? 0.8193 0.6744 0.8637 -0.0289 -0.0311 0.0559  264 ASP A CA  
1967 C C   . ASP A 275 ? 0.8063 0.6621 0.8375 -0.0268 -0.0308 0.0580  264 ASP A C   
1968 O O   . ASP A 275 ? 0.8106 0.6693 0.8287 -0.0266 -0.0274 0.0602  264 ASP A O   
1969 C CB  . ASP A 275 ? 0.8558 0.7081 0.9129 -0.0310 -0.0315 0.0646  264 ASP A CB  
1970 C CG  . ASP A 275 ? 0.9440 0.7930 1.0177 -0.0334 -0.0342 0.0617  264 ASP A CG  
1971 O OD1 . ASP A 275 ? 0.9554 0.7989 1.0347 -0.0328 -0.0379 0.0549  264 ASP A OD1 
1972 O OD2 . ASP A 275 ? 0.9883 0.8398 1.0695 -0.0361 -0.0325 0.0664  264 ASP A OD2 
1973 N N   . LYS A 276 ? 0.7888 0.6412 0.8240 -0.0252 -0.0346 0.0568  265 LYS A N   
1974 C CA  . LYS A 276 ? 0.7819 0.6348 0.8082 -0.0237 -0.0365 0.0591  265 LYS A CA  
1975 C C   . LYS A 276 ? 0.7666 0.6226 0.7812 -0.0222 -0.0355 0.0519  265 LYS A C   
1976 O O   . LYS A 276 ? 0.7730 0.6302 0.7774 -0.0218 -0.0367 0.0543  265 LYS A O   
1977 C CB  . LYS A 276 ? 0.8074 0.6565 0.8467 -0.0222 -0.0407 0.0600  265 LYS A CB  
1978 C CG  . LYS A 276 ? 0.8601 0.7065 0.9098 -0.0208 -0.0407 0.0501  265 LYS A CG  
1979 C CD  . LYS A 276 ? 0.9083 0.7515 0.9698 -0.0182 -0.0431 0.0493  265 LYS A CD  
1980 C CE  . LYS A 276 ? 0.9513 0.7897 1.0212 -0.0171 -0.0414 0.0390  265 LYS A CE  
1981 N NZ  . LYS A 276 ? 0.9728 0.8064 1.0507 -0.0196 -0.0415 0.0388  265 LYS A NZ  
1982 N N   . ASP A 277 ? 0.7476 0.6046 0.7635 -0.0217 -0.0341 0.0435  266 ASP A N   
1983 C CA  . ASP A 277 ? 0.7376 0.5974 0.7438 -0.0203 -0.0330 0.0367  266 ASP A CA  
1984 C C   . ASP A 277 ? 0.7237 0.5870 0.7174 -0.0210 -0.0294 0.0375  266 ASP A C   
1985 O O   . ASP A 277 ? 0.7243 0.5894 0.7085 -0.0200 -0.0286 0.0337  266 ASP A O   
1986 C CB  . ASP A 277 ? 0.7542 0.6126 0.7658 -0.0198 -0.0331 0.0278  266 ASP A CB  
1987 C CG  . ASP A 277 ? 0.8010 0.6552 0.8229 -0.0182 -0.0348 0.0247  266 ASP A CG  
1988 O OD1 . ASP A 277 ? 0.8065 0.6607 0.8311 -0.0168 -0.0364 0.0286  266 ASP A OD1 
1989 O OD2 . ASP A 277 ? 0.8199 0.6703 0.8470 -0.0185 -0.0347 0.0183  266 ASP A OD2 
1990 N N   . TRP A 278 ? 0.7112 0.5751 0.7065 -0.0226 -0.0267 0.0422  267 TRP A N   
1991 C CA  . TRP A 278 ? 0.7058 0.5726 0.6925 -0.0229 -0.0218 0.0436  267 TRP A CA  
1992 C C   . TRP A 278 ? 0.7119 0.5785 0.7034 -0.0246 -0.0188 0.0516  267 TRP A C   
1993 O O   . TRP A 278 ? 0.7062 0.5743 0.7092 -0.0257 -0.0180 0.0523  267 TRP A O   
1994 C CB  . TRP A 278 ? 0.6904 0.5601 0.6808 -0.0227 -0.0212 0.0375  267 TRP A CB  
1995 C CG  . TRP A 278 ? 0.6823 0.5553 0.6662 -0.0222 -0.0162 0.0378  267 TRP A CG  
1996 C CD1 . TRP A 278 ? 0.6932 0.5659 0.6678 -0.0219 -0.0109 0.0423  267 TRP A CD1 
1997 C CD2 . TRP A 278 ? 0.6781 0.5543 0.6647 -0.0220 -0.0158 0.0337  267 TRP A CD2 
1998 N NE1 . TRP A 278 ? 0.6946 0.5702 0.6675 -0.0210 -0.0064 0.0408  267 TRP A NE1 
1999 C CE2 . TRP A 278 ? 0.6886 0.5669 0.6699 -0.0210 -0.0098 0.0362  267 TRP A CE2 
2000 C CE3 . TRP A 278 ? 0.6819 0.5588 0.6743 -0.0226 -0.0200 0.0284  267 TRP A CE3 
2001 C CZ2 . TRP A 278 ? 0.6944 0.5764 0.6790 -0.0204 -0.0083 0.0343  267 TRP A CZ2 
2002 C CZ3 . TRP A 278 ? 0.6894 0.5699 0.6827 -0.0226 -0.0194 0.0268  267 TRP A CZ3 
2003 C CH2 . TRP A 278 ? 0.6917 0.5751 0.6826 -0.0214 -0.0138 0.0301  267 TRP A CH2 
2004 N N   . GLU A 279 ? 0.7235 0.5878 0.7067 -0.0251 -0.0178 0.0583  268 GLU A N   
2005 C CA  . GLU A 279 ? 0.7352 0.5986 0.7212 -0.0268 -0.0142 0.0671  268 GLU A CA  
2006 C C   . GLU A 279 ? 0.7397 0.6062 0.7235 -0.0269 -0.0062 0.0686  268 GLU A C   
2007 O O   . GLU A 279 ? 0.7408 0.6090 0.7365 -0.0282 -0.0031 0.0737  268 GLU A O   
2008 C CB  . GLU A 279 ? 0.7767 0.6363 0.7512 -0.0277 -0.0155 0.0741  268 GLU A CB  
2009 C CG  . GLU A 279 ? 0.8674 0.7245 0.8495 -0.0275 -0.0234 0.0748  268 GLU A CG  
2010 C CD  . GLU A 279 ? 0.9952 0.8488 0.9701 -0.0290 -0.0263 0.0840  268 GLU A CD  
2011 O OE1 . GLU A 279 ? 1.0330 0.8851 0.9967 -0.0307 -0.0217 0.0908  268 GLU A OE1 
2012 O OE2 . GLU A 279 ? 1.0214 0.8736 1.0023 -0.0284 -0.0331 0.0848  268 GLU A OE2 
2013 N N   . ASP A 280 ? 0.7365 0.6037 0.7074 -0.0254 -0.0026 0.0643  269 ASP A N   
2014 C CA  . ASP A 280 ? 0.7348 0.6047 0.7052 -0.0248 0.0059  0.0655  269 ASP A CA  
2015 C C   . ASP A 280 ? 0.7164 0.5917 0.7029 -0.0244 0.0054  0.0619  269 ASP A C   
2016 O O   . ASP A 280 ? 0.7124 0.5906 0.7001 -0.0233 0.0118  0.0622  269 ASP A O   
2017 C CB  . ASP A 280 ? 0.7705 0.6376 0.7209 -0.0234 0.0109  0.0628  269 ASP A CB  
2018 C CG  . ASP A 280 ? 0.8392 0.7001 0.7706 -0.0247 0.0115  0.0670  269 ASP A CG  
2019 O OD1 . ASP A 280 ? 0.8431 0.7025 0.7777 -0.0265 0.0097  0.0740  269 ASP A OD1 
2020 O OD2 . ASP A 280 ? 0.8744 0.7314 0.7876 -0.0243 0.0132  0.0636  269 ASP A OD2 
2021 N N   . ILE A 281 ? 0.7041 0.5802 0.7029 -0.0253 -0.0021 0.0587  270 ILE A N   
2022 C CA  . ILE A 281 ? 0.6967 0.5772 0.7098 -0.0259 -0.0040 0.0560  270 ILE A CA  
2023 C C   . ILE A 281 ? 0.6982 0.5822 0.7262 -0.0276 0.0005  0.0636  270 ILE A C   
2024 O O   . ILE A 281 ? 0.6933 0.5822 0.7304 -0.0274 0.0027  0.0640  270 ILE A O   
2025 C CB  . ILE A 281 ? 0.6922 0.5710 0.7119 -0.0271 -0.0128 0.0498  270 ILE A CB  
2026 C CG1 . ILE A 281 ? 0.6935 0.5760 0.7207 -0.0278 -0.0156 0.0456  270 ILE A CG1 
2027 C CG2 . ILE A 281 ? 0.6937 0.5694 0.7246 -0.0293 -0.0162 0.0533  270 ILE A CG2 
2028 C CD1 . ILE A 281 ? 0.7054 0.5848 0.7331 -0.0288 -0.0229 0.0383  270 ILE A CD1 
2029 N N   . LYS A 282 ? 0.7026 0.5842 0.7332 -0.0290 0.0024  0.0705  271 LYS A N   
2030 C CA  . LYS A 282 ? 0.7070 0.5915 0.7513 -0.0306 0.0078  0.0791  271 LYS A CA  
2031 C C   . LYS A 282 ? 0.7158 0.6037 0.7562 -0.0287 0.0185  0.0822  271 LYS A C   
2032 O O   . LYS A 282 ? 0.7162 0.6095 0.7733 -0.0294 0.0229  0.0871  271 LYS A O   
2033 C CB  . LYS A 282 ? 0.7377 0.6178 0.7794 -0.0320 0.0087  0.0863  271 LYS A CB  
2034 C CG  . LYS A 282 ? 0.8013 0.6771 0.8488 -0.0335 -0.0008 0.0839  271 LYS A CG  
2035 C CD  . LYS A 282 ? 0.8695 0.7419 0.9207 -0.0353 0.0000  0.0931  271 LYS A CD  
2036 C CE  . LYS A 282 ? 0.9183 0.7940 0.9883 -0.0379 0.0040  0.1009  271 LYS A CE  
2037 N NZ  . LYS A 282 ? 0.9460 0.8181 1.0191 -0.0398 0.0054  0.1110  271 LYS A NZ  
2038 N N   . LYS A 283 ? 0.7218 0.6063 0.7411 -0.0263 0.0230  0.0795  272 LYS A N   
2039 C CA  . LYS A 283 ? 0.7274 0.6127 0.7392 -0.0240 0.0342  0.0810  272 LYS A CA  
2040 C C   . LYS A 283 ? 0.7178 0.6082 0.7382 -0.0220 0.0350  0.0764  272 LYS A C   
2041 O O   . LYS A 283 ? 0.7177 0.6091 0.7370 -0.0198 0.0451  0.0781  272 LYS A O   
2042 C CB  . LYS A 283 ? 0.7705 0.6484 0.7547 -0.0229 0.0375  0.0789  272 LYS A CB  
2043 C CG  . LYS A 283 ? 0.8347 0.7075 0.8087 -0.0250 0.0385  0.0858  272 LYS A CG  
2044 C CD  . LYS A 283 ? 0.9108 0.7763 0.8572 -0.0244 0.0455  0.0857  272 LYS A CD  
2045 C CE  . LYS A 283 ? 0.9693 0.8285 0.8977 -0.0261 0.0371  0.0850  272 LYS A CE  
2046 N NZ  . LYS A 283 ? 1.0013 0.8542 0.9047 -0.0253 0.0387  0.0794  272 LYS A NZ  
2047 N N   . MET A 284 ? 0.7112 0.6040 0.7394 -0.0227 0.0250  0.0709  273 MET A N   
2048 C CA  . MET A 284 ? 0.7083 0.6059 0.7447 -0.0213 0.0243  0.0675  273 MET A CA  
2049 C C   . MET A 284 ? 0.7037 0.6085 0.7641 -0.0221 0.0276  0.0742  273 MET A C   
2050 O O   . MET A 284 ? 0.7074 0.6142 0.7823 -0.0251 0.0241  0.0787  273 MET A O   
2051 C CB  . MET A 284 ? 0.7108 0.6085 0.7480 -0.0225 0.0125  0.0606  273 MET A CB  
2052 C CG  . MET A 284 ? 0.7501 0.6421 0.7676 -0.0216 0.0089  0.0540  273 MET A CG  
2053 S SD  . MET A 284 ? 0.8432 0.7319 0.8412 -0.0182 0.0165  0.0510  273 MET A SD  
2054 C CE  . MET A 284 ? 0.8203 0.7147 0.8295 -0.0166 0.0170  0.0494  273 MET A CE  
2055 N N   . PRO A 285 ? 0.6954 0.6044 0.7627 -0.0195 0.0338  0.0751  274 PRO A N   
2056 C CA  . PRO A 285 ? 0.6838 0.6012 0.7779 -0.0202 0.0366  0.0823  274 PRO A CA  
2057 C C   . PRO A 285 ? 0.6782 0.6002 0.7912 -0.0243 0.0237  0.0829  274 PRO A C   
2058 O O   . PRO A 285 ? 0.6674 0.5942 0.8013 -0.0268 0.0239  0.0900  274 PRO A O   
2059 C CB  . PRO A 285 ? 0.6885 0.6087 0.7853 -0.0163 0.0429  0.0814  274 PRO A CB  
2060 C CG  . PRO A 285 ? 0.7042 0.6161 0.7737 -0.0135 0.0487  0.0755  274 PRO A CG  
2061 C CD  . PRO A 285 ? 0.6924 0.5988 0.7454 -0.0159 0.0388  0.0701  274 PRO A CD  
2062 N N   . GLU A 286 ? 0.6848 0.6047 0.7898 -0.0255 0.0126  0.0756  275 GLU A N   
2063 C CA  . GLU A 286 ? 0.6876 0.6100 0.8063 -0.0299 -0.0001 0.0749  275 GLU A CA  
2064 C C   . GLU A 286 ? 0.6902 0.6061 0.8020 -0.0331 -0.0074 0.0713  275 GLU A C   
2065 O O   . GLU A 286 ? 0.6903 0.6046 0.8045 -0.0365 -0.0184 0.0670  275 GLU A O   
2066 C CB  . GLU A 286 ? 0.7240 0.6477 0.8393 -0.0297 -0.0077 0.0696  275 GLU A CB  
2067 C CG  . GLU A 286 ? 0.7980 0.7264 0.9173 -0.0257 -0.0004 0.0721  275 GLU A CG  
2068 C CD  . GLU A 286 ? 0.8967 0.8344 1.0438 -0.0264 0.0000  0.0803  275 GLU A CD  
2069 O OE1 . GLU A 286 ? 0.9168 0.8582 1.0822 -0.0304 -0.0046 0.0854  275 GLU A OE1 
2070 O OE2 . GLU A 286 ? 0.9257 0.8672 1.0779 -0.0230 0.0047  0.0821  275 GLU A OE2 
2071 N N   . HIS A 287 ? 0.6898 0.6013 0.7930 -0.0322 -0.0014 0.0731  276 HIS A N   
2072 C CA  . HIS A 287 ? 0.6952 0.6004 0.7939 -0.0347 -0.0077 0.0706  276 HIS A CA  
2073 C C   . HIS A 287 ? 0.6967 0.6032 0.8163 -0.0396 -0.0145 0.0740  276 HIS A C   
2074 O O   . HIS A 287 ? 0.7046 0.6061 0.8226 -0.0422 -0.0239 0.0683  276 HIS A O   
2075 C CB  . HIS A 287 ? 0.7003 0.6008 0.7862 -0.0330 -0.0008 0.0732  276 HIS A CB  
2076 C CG  . HIS A 287 ? 0.7179 0.6121 0.8023 -0.0352 -0.0072 0.0715  276 HIS A CG  
2077 N ND1 . HIS A 287 ? 0.7326 0.6259 0.8292 -0.0377 -0.0062 0.0786  276 HIS A ND1 
2078 C CD2 . HIS A 287 ? 0.7351 0.6238 0.8094 -0.0351 -0.0141 0.0639  276 HIS A CD2 
2079 C CE1 . HIS A 287 ? 0.7418 0.6286 0.8350 -0.0388 -0.0127 0.0750  276 HIS A CE1 
2080 N NE2 . HIS A 287 ? 0.7474 0.6312 0.8275 -0.0372 -0.0172 0.0660  276 HIS A NE2 
2081 N N   . SER A 288 ? 0.6841 0.5967 0.8235 -0.0408 -0.0096 0.0831  277 SER A N   
2082 C CA  . SER A 288 ? 0.6804 0.5941 0.8414 -0.0461 -0.0169 0.0868  277 SER A CA  
2083 C C   . SER A 288 ? 0.6720 0.5886 0.8430 -0.0495 -0.0283 0.0832  277 SER A C   
2084 O O   . SER A 288 ? 0.6691 0.5832 0.8514 -0.0546 -0.0379 0.0824  277 SER A O   
2085 C CB  . SER A 288 ? 0.6943 0.6137 0.8747 -0.0468 -0.0082 0.0984  277 SER A CB  
2086 O OG  . SER A 288 ? 0.7224 0.6361 0.8967 -0.0470 -0.0041 0.1015  277 SER A OG  
2087 N N   . THR A 289 ? 0.6686 0.5889 0.8334 -0.0469 -0.0282 0.0803  278 THR A N   
2088 C CA  . THR A 289 ? 0.6659 0.5880 0.8355 -0.0502 -0.0399 0.0767  278 THR A CA  
2089 C C   . THR A 289 ? 0.6678 0.5800 0.8171 -0.0517 -0.0484 0.0657  278 THR A C   
2090 O O   . THR A 289 ? 0.6689 0.5780 0.8216 -0.0567 -0.0598 0.0622  278 THR A O   
2091 C CB  . THR A 289 ? 0.6840 0.6127 0.8529 -0.0466 -0.0365 0.0779  278 THR A CB  
2092 O OG1 . THR A 289 ? 0.6955 0.6312 0.8775 -0.0432 -0.0240 0.0865  278 THR A OG1 
2093 C CG2 . THR A 289 ? 0.6832 0.6160 0.8634 -0.0506 -0.0486 0.0780  278 THR A CG2 
2094 N N   . LEU A 290 ? 0.6684 0.5753 0.7965 -0.0475 -0.0428 0.0605  279 LEU A N   
2095 C CA  . LEU A 290 ? 0.6781 0.5760 0.7876 -0.0477 -0.0478 0.0507  279 LEU A CA  
2096 C C   . LEU A 290 ? 0.6897 0.5805 0.8053 -0.0514 -0.0527 0.0493  279 LEU A C   
2097 O O   . LEU A 290 ? 0.6947 0.5785 0.8043 -0.0544 -0.0608 0.0418  279 LEU A O   
2098 C CB  . LEU A 290 ? 0.6812 0.5770 0.7723 -0.0422 -0.0393 0.0483  279 LEU A CB  
2099 C CG  . LEU A 290 ? 0.6997 0.5873 0.7737 -0.0413 -0.0419 0.0396  279 LEU A CG  
2100 C CD1 . LEU A 290 ? 0.7111 0.5975 0.7739 -0.0415 -0.0469 0.0324  279 LEU A CD1 
2101 C CD2 . LEU A 290 ? 0.7067 0.5932 0.7684 -0.0368 -0.0340 0.0402  279 LEU A CD2 
2102 N N   . MET A 291 ? 0.6939 0.5859 0.8214 -0.0516 -0.0475 0.0567  280 MET A N   
2103 C CA  . MET A 291 ? 0.7069 0.5920 0.8429 -0.0552 -0.0519 0.0565  280 MET A CA  
2104 C C   . MET A 291 ? 0.7185 0.6034 0.8706 -0.0616 -0.0621 0.0565  280 MET A C   
2105 O O   . MET A 291 ? 0.7284 0.6043 0.8804 -0.0653 -0.0694 0.0508  280 MET A O   
2106 C CB  . MET A 291 ? 0.7078 0.5947 0.8535 -0.0542 -0.0438 0.0661  280 MET A CB  
2107 C CG  . MET A 291 ? 0.7302 0.6174 0.8598 -0.0488 -0.0342 0.0676  280 MET A CG  
2108 S SD  . MET A 291 ? 0.7395 0.6166 0.8509 -0.0465 -0.0364 0.0595  280 MET A SD  
2109 C CE  . MET A 291 ? 0.7353 0.6139 0.8276 -0.0432 -0.0366 0.0510  280 MET A CE  
2110 N N   . LYS A 292 ? 0.7190 0.6133 0.8856 -0.0631 -0.0629 0.0629  281 LYS A N   
2111 C CA  . LYS A 292 ? 0.7303 0.6258 0.9141 -0.0697 -0.0739 0.0642  281 LYS A CA  
2112 C C   . LYS A 292 ? 0.7492 0.6388 0.9179 -0.0725 -0.0849 0.0540  281 LYS A C   
2113 O O   . LYS A 292 ? 0.7493 0.6317 0.9208 -0.0786 -0.0955 0.0495  281 LYS A O   
2114 C CB  . LYS A 292 ? 0.7474 0.6559 0.9526 -0.0698 -0.0706 0.0751  281 LYS A CB  
2115 C CG  . LYS A 292 ? 0.7995 0.7115 1.0261 -0.0769 -0.0828 0.0784  281 LYS A CG  
2116 C CD  . LYS A 292 ? 0.8521 0.7779 1.0982 -0.0757 -0.0797 0.0882  281 LYS A CD  
2117 C CE  . LYS A 292 ? 0.9078 0.8362 1.1425 -0.0745 -0.0850 0.0841  281 LYS A CE  
2118 N NZ  . LYS A 292 ? 0.9414 0.8665 1.1495 -0.0676 -0.0760 0.0778  281 LYS A NZ  
2119 N N   . ASP A 293 ? 0.7621 0.6539 0.9136 -0.0683 -0.0821 0.0501  282 ASP A N   
2120 C CA  . ASP A 293 ? 0.7826 0.6696 0.9181 -0.0706 -0.0912 0.0417  282 ASP A CA  
2121 C C   . ASP A 293 ? 0.8040 0.6783 0.9167 -0.0700 -0.0920 0.0300  282 ASP A C   
2122 O O   . ASP A 293 ? 0.8180 0.6857 0.9184 -0.0736 -0.1006 0.0224  282 ASP A O   
2123 C CB  . ASP A 293 ? 0.8057 0.7008 0.9346 -0.0666 -0.0879 0.0437  282 ASP A CB  
2124 C CG  . ASP A 293 ? 0.8611 0.7679 1.0121 -0.0682 -0.0903 0.0536  282 ASP A CG  
2125 O OD1 . ASP A 293 ? 0.8636 0.7725 1.0349 -0.0736 -0.0972 0.0586  282 ASP A OD1 
2126 O OD2 . ASP A 293 ? 0.8903 0.8041 1.0397 -0.0640 -0.0854 0.0567  282 ASP A OD2 
2127 N N   . PHE A 294 ? 0.8032 0.6743 0.9096 -0.0652 -0.0830 0.0287  283 PHE A N   
2128 C CA  . PHE A 294 ? 0.8180 0.6784 0.9053 -0.0635 -0.0822 0.0184  283 PHE A CA  
2129 C C   . PHE A 294 ? 0.8360 0.6878 0.9285 -0.0639 -0.0807 0.0168  283 PHE A C   
2130 O O   . PHE A 294 ? 0.8338 0.6890 0.9422 -0.0640 -0.0776 0.0248  283 PHE A O   
2131 C CB  . PHE A 294 ? 0.8126 0.6765 0.8846 -0.0570 -0.0737 0.0172  283 PHE A CB  
2132 C CG  . PHE A 294 ? 0.8111 0.6810 0.8753 -0.0564 -0.0754 0.0171  283 PHE A CG  
2133 C CD1 . PHE A 294 ? 0.8232 0.6875 0.8700 -0.0575 -0.0799 0.0088  283 PHE A CD1 
2134 C CD2 . PHE A 294 ? 0.8077 0.6885 0.8821 -0.0545 -0.0718 0.0257  283 PHE A CD2 
2135 C CE1 . PHE A 294 ? 0.8281 0.6978 0.8681 -0.0571 -0.0816 0.0098  283 PHE A CE1 
2136 C CE2 . PHE A 294 ? 0.8084 0.6943 0.8774 -0.0538 -0.0735 0.0262  283 PHE A CE2 
2137 C CZ  . PHE A 294 ? 0.8133 0.6939 0.8653 -0.0552 -0.0787 0.0186  283 PHE A CZ  
2138 N N   . ARG A 295 ? 0.8516 0.6919 0.9309 -0.0639 -0.0822 0.0066  284 ARG A N   
2139 C CA  . ARG A 295 ? 0.8676 0.6988 0.9521 -0.0636 -0.0803 0.0045  284 ARG A CA  
2140 C C   . ARG A 295 ? 0.8753 0.7006 0.9440 -0.0585 -0.0745 -0.0028 284 ARG A C   
2141 O O   . ARG A 295 ? 0.8804 0.7016 0.9329 -0.0584 -0.0758 -0.0113 284 ARG A O   
2142 C CB  . ARG A 295 ? 0.9042 0.7248 0.9951 -0.0703 -0.0892 -0.0005 284 ARG A CB  
2143 C CG  . ARG A 295 ? 0.9628 0.7878 1.0774 -0.0747 -0.0929 0.0090  284 ARG A CG  
2144 C CD  . ARG A 295 ? 1.0309 0.8458 1.1521 -0.0827 -0.1039 0.0040  284 ARG A CD  
2145 N NE  . ARG A 295 ? 1.1001 0.8985 1.2089 -0.0832 -0.1049 -0.0082 284 ARG A NE  
2146 C CZ  . ARG A 295 ? 1.1449 0.9349 1.2614 -0.0817 -0.1012 -0.0091 284 ARG A CZ  
2147 N NH1 . ARG A 295 ? 1.1379 0.9341 1.2734 -0.0803 -0.0972 0.0019  284 ARG A NH1 
2148 N NH2 . ARG A 295 ? 1.1574 0.9321 1.2629 -0.0816 -0.1012 -0.0208 284 ARG A NH2 
2149 N N   . ARG A 296 ? 0.8717 0.6972 0.9458 -0.0544 -0.0682 0.0012  285 ARG A N   
2150 C CA  . ARG A 296 ? 0.8839 0.7054 0.9477 -0.0492 -0.0626 -0.0035 285 ARG A CA  
2151 C C   . ARG A 296 ? 0.8997 0.7086 0.9540 -0.0500 -0.0642 -0.0158 285 ARG A C   
2152 O O   . ARG A 296 ? 0.9131 0.7211 0.9539 -0.0466 -0.0603 -0.0215 285 ARG A O   
2153 C CB  . ARG A 296 ? 0.8993 0.7212 0.9741 -0.0462 -0.0581 0.0037  285 ARG A CB  
2154 C CG  . ARG A 296 ? 0.9457 0.7637 1.0144 -0.0411 -0.0534 0.0000  285 ARG A CG  
2155 C CD  . ARG A 296 ? 0.9850 0.8052 1.0632 -0.0382 -0.0501 0.0090  285 ARG A CD  
2156 N NE  . ARG A 296 ? 1.0278 0.8583 1.1066 -0.0380 -0.0481 0.0194  285 ARG A NE  
2157 C CZ  . ARG A 296 ? 1.0700 0.9081 1.1373 -0.0355 -0.0449 0.0210  285 ARG A CZ  
2158 N NH1 . ARG A 296 ? 1.0708 0.9087 1.1262 -0.0331 -0.0439 0.0137  285 ARG A NH1 
2159 N NH2 . ARG A 296 ? 1.0711 0.9167 1.1385 -0.0355 -0.0422 0.0298  285 ARG A NH2 
2160 N N   . ASN A 297 ? 0.8968 0.6953 0.9579 -0.0545 -0.0693 -0.0200 286 ASN A N   
2161 C CA  . ASN A 297 ? 0.9038 0.6877 0.9555 -0.0556 -0.0700 -0.0324 286 ASN A CA  
2162 C C   . ASN A 297 ? 0.8960 0.6775 0.9272 -0.0580 -0.0730 -0.0410 286 ASN A C   
2163 O O   . ASN A 297 ? 0.9070 0.6778 0.9250 -0.0571 -0.0702 -0.0515 286 ASN A O   
2164 C CB  . ASN A 297 ? 0.9269 0.6993 0.9917 -0.0604 -0.0751 -0.0345 286 ASN A CB  
2165 C CG  . ASN A 297 ? 0.9910 0.7467 1.0437 -0.0639 -0.0781 -0.0484 286 ASN A CG  
2166 O OD1 . ASN A 297 ? 1.0112 0.7627 1.0575 -0.0705 -0.0864 -0.0524 286 ASN A OD1 
2167 N ND2 . ASN A 297 ? 1.0047 0.7502 1.0533 -0.0596 -0.0712 -0.0560 286 ASN A ND2 
2168 N N   . THR A 298 ? 0.8751 0.6661 0.9037 -0.0609 -0.0780 -0.0363 287 THR A N   
2169 C CA  . THR A 298 ? 0.8735 0.6628 0.8825 -0.0635 -0.0818 -0.0427 287 THR A CA  
2170 C C   . THR A 298 ? 0.8668 0.6563 0.8595 -0.0577 -0.0734 -0.0476 287 THR A C   
2171 O O   . THR A 298 ? 0.8739 0.6551 0.8483 -0.0590 -0.0734 -0.0568 287 THR A O   
2172 C CB  . THR A 298 ? 0.8791 0.6814 0.8924 -0.0661 -0.0874 -0.0340 287 THR A CB  
2173 O OG1 . THR A 298 ? 0.8813 0.6864 0.9147 -0.0702 -0.0930 -0.0270 287 THR A OG1 
2174 C CG2 . THR A 298 ? 0.8893 0.6892 0.8850 -0.0703 -0.0941 -0.0392 287 THR A CG2 
2175 N N   . TYR A 299 ? 0.8480 0.6466 0.8478 -0.0518 -0.0662 -0.0412 288 TYR A N   
2176 C CA  . TYR A 299 ? 0.8430 0.6447 0.8328 -0.0462 -0.0585 -0.0430 288 TYR A CA  
2177 C C   . TYR A 299 ? 0.8407 0.6375 0.8387 -0.0416 -0.0519 -0.0444 288 TYR A C   
2178 O O   . TYR A 299 ? 0.8430 0.6472 0.8451 -0.0368 -0.0467 -0.0391 288 TYR A O   
2179 C CB  . TYR A 299 ? 0.8327 0.6490 0.8251 -0.0437 -0.0570 -0.0335 288 TYR A CB  
2180 C CG  . TYR A 299 ? 0.8325 0.6551 0.8249 -0.0479 -0.0637 -0.0292 288 TYR A CG  
2181 C CD1 . TYR A 299 ? 0.8453 0.6674 0.8227 -0.0502 -0.0671 -0.0332 288 TYR A CD1 
2182 C CD2 . TYR A 299 ? 0.8324 0.6609 0.8409 -0.0500 -0.0670 -0.0209 288 TYR A CD2 
2183 C CE1 . TYR A 299 ? 0.8517 0.6797 0.8313 -0.0542 -0.0742 -0.0284 288 TYR A CE1 
2184 C CE2 . TYR A 299 ? 0.8391 0.6737 0.8511 -0.0538 -0.0732 -0.0165 288 TYR A CE2 
2185 C CZ  . TYR A 299 ? 0.8536 0.6882 0.8518 -0.0558 -0.0773 -0.0201 288 TYR A CZ  
2186 O OH  . TYR A 299 ? 0.8679 0.7089 0.8715 -0.0596 -0.0842 -0.0148 288 TYR A OH  
2187 N N   . THR A 300 ? 0.8334 0.6171 0.8343 -0.0432 -0.0523 -0.0513 289 THR A N   
2188 C CA  . THR A 300 ? 0.8269 0.6055 0.8390 -0.0388 -0.0464 -0.0519 289 THR A CA  
2189 C C   . THR A 300 ? 0.8198 0.5957 0.8228 -0.0338 -0.0381 -0.0583 289 THR A C   
2190 O O   . THR A 300 ? 0.8169 0.5967 0.8303 -0.0287 -0.0330 -0.0541 289 THR A O   
2191 C CB  . THR A 300 ? 0.8455 0.6112 0.8676 -0.0418 -0.0493 -0.0559 289 THR A CB  
2192 O OG1 . THR A 300 ? 0.8557 0.6190 0.8930 -0.0371 -0.0440 -0.0532 289 THR A OG1 
2193 C CG2 . THR A 300 ? 0.8607 0.6113 0.8676 -0.0453 -0.0502 -0.0693 289 THR A CG2 
2194 N N   . ASN A 301 ? 0.8165 0.5862 0.8007 -0.0354 -0.0369 -0.0675 290 ASN A N   
2195 C CA  . ASN A 301 ? 0.8198 0.5876 0.7957 -0.0308 -0.0278 -0.0730 290 ASN A CA  
2196 C C   . ASN A 301 ? 0.8045 0.5841 0.7693 -0.0297 -0.0268 -0.0691 290 ASN A C   
2197 O O   . ASN A 301 ? 0.8093 0.5866 0.7612 -0.0280 -0.0209 -0.0748 290 ASN A O   
2198 C CB  . ASN A 301 ? 0.8575 0.6088 0.8187 -0.0327 -0.0246 -0.0863 290 ASN A CB  
2199 C CG  . ASN A 301 ? 0.9156 0.6535 0.8889 -0.0327 -0.0236 -0.0911 290 ASN A CG  
2200 O OD1 . ASN A 301 ? 0.9274 0.6645 0.9170 -0.0274 -0.0172 -0.0895 290 ASN A OD1 
2201 N ND2 . ASN A 301 ? 0.9340 0.6610 0.9007 -0.0389 -0.0304 -0.0969 290 ASN A ND2 
2202 N N   . CYS A 302 ? 0.7806 0.5726 0.7509 -0.0305 -0.0319 -0.0594 291 CYS A N   
2203 C CA  . CYS A 302 ? 0.7676 0.5702 0.7292 -0.0296 -0.0315 -0.0553 291 CYS A CA  
2204 C C   . CYS A 302 ? 0.7519 0.5637 0.7234 -0.0247 -0.0271 -0.0485 291 CYS A C   
2205 O O   . CYS A 302 ? 0.7481 0.5640 0.7333 -0.0238 -0.0289 -0.0415 291 CYS A O   
2206 C CB  . CYS A 302 ? 0.7728 0.5816 0.7325 -0.0340 -0.0394 -0.0500 291 CYS A CB  
2207 S SG  . CYS A 302 ? 0.8273 0.6262 0.7732 -0.0410 -0.0469 -0.0573 291 CYS A SG  
2208 N N   . SER A 303 ? 0.7430 0.5578 0.7074 -0.0219 -0.0217 -0.0501 292 SER A N   
2209 C CA  . SER A 303 ? 0.7303 0.5539 0.7029 -0.0177 -0.0184 -0.0440 292 SER A CA  
2210 C C   . SER A 303 ? 0.7271 0.5558 0.6877 -0.0170 -0.0153 -0.0447 292 SER A C   
2211 O O   . SER A 303 ? 0.7395 0.5636 0.6860 -0.0188 -0.0142 -0.0506 292 SER A O   
2212 C CB  . SER A 303 ? 0.7336 0.5529 0.7187 -0.0138 -0.0130 -0.0456 292 SER A CB  
2213 O OG  . SER A 303 ? 0.7566 0.5686 0.7345 -0.0125 -0.0063 -0.0543 292 SER A OG  
2214 N N   . LEU A 304 ? 0.7074 0.5451 0.6727 -0.0147 -0.0146 -0.0383 293 LEU A N   
2215 C CA  . LEU A 304 ? 0.7014 0.5438 0.6578 -0.0139 -0.0115 -0.0385 293 LEU A CA  
2216 C C   . LEU A 304 ? 0.6987 0.5366 0.6550 -0.0113 -0.0037 -0.0443 293 LEU A C   
2217 O O   . LEU A 304 ? 0.7058 0.5427 0.6501 -0.0118 -0.0001 -0.0479 293 LEU A O   
2218 C CB  . LEU A 304 ? 0.6971 0.5486 0.6591 -0.0125 -0.0128 -0.0310 293 LEU A CB  
2219 C CG  . LEU A 304 ? 0.7102 0.5667 0.6643 -0.0122 -0.0106 -0.0302 293 LEU A CG  
2220 C CD1 . LEU A 304 ? 0.7221 0.5786 0.6633 -0.0151 -0.0133 -0.0311 293 LEU A CD1 
2221 C CD2 . LEU A 304 ? 0.7112 0.5745 0.6710 -0.0112 -0.0123 -0.0237 293 LEU A CD2 
2222 N N   . ILE A 305 ? 0.6870 0.5218 0.6575 -0.0085 -0.0007 -0.0449 294 ILE A N   
2223 C CA  . ILE A 305 ? 0.6865 0.5166 0.6612 -0.0053 0.0078  -0.0501 294 ILE A CA  
2224 C C   . ILE A 305 ? 0.7025 0.5225 0.6604 -0.0071 0.0120  -0.0596 294 ILE A C   
2225 O O   . ILE A 305 ? 0.7088 0.5286 0.6579 -0.0063 0.0185  -0.0627 294 ILE A O   
2226 C CB  . ILE A 305 ? 0.6806 0.5077 0.6750 -0.0024 0.0088  -0.0487 294 ILE A CB  
2227 C CG1 . ILE A 305 ? 0.6838 0.5207 0.6928 -0.0010 0.0041  -0.0386 294 ILE A CG1 
2228 C CG2 . ILE A 305 ? 0.6816 0.5019 0.6817 0.0012  0.0189  -0.0553 294 ILE A CG2 
2229 C CD1 . ILE A 305 ? 0.6937 0.5359 0.7175 0.0027  0.0083  -0.0353 294 ILE A CD1 
2230 N N   . LYS A 306 ? 0.7096 0.5212 0.6619 -0.0102 0.0078  -0.0638 295 LYS A N   
2231 C CA  . LYS A 306 ? 0.7298 0.5298 0.6641 -0.0129 0.0100  -0.0733 295 LYS A CA  
2232 C C   . LYS A 306 ? 0.7388 0.5413 0.6528 -0.0162 0.0079  -0.0735 295 LYS A C   
2233 O O   . LYS A 306 ? 0.7440 0.5391 0.6415 -0.0172 0.0133  -0.0804 295 LYS A O   
2234 C CB  . LYS A 306 ? 0.7675 0.5584 0.7028 -0.0161 0.0041  -0.0767 295 LYS A CB  
2235 C CG  . LYS A 306 ? 0.8305 0.6146 0.7834 -0.0127 0.0085  -0.0790 295 LYS A CG  
2236 C CD  . LYS A 306 ? 0.9084 0.6826 0.8635 -0.0161 0.0028  -0.0824 295 LYS A CD  
2237 C CE  . LYS A 306 ? 0.9796 0.7390 0.9144 -0.0200 0.0037  -0.0939 295 LYS A CE  
2238 N NZ  . LYS A 306 ? 1.0074 0.7551 0.9479 -0.0229 -0.0008 -0.0982 295 LYS A NZ  
2239 N N   . TYR A 307 ? 0.7379 0.5507 0.6531 -0.0178 0.0007  -0.0656 296 TYR A N   
2240 C CA  . TYR A 307 ? 0.7478 0.5640 0.6469 -0.0207 -0.0020 -0.0642 296 TYR A CA  
2241 C C   . TYR A 307 ? 0.7608 0.5806 0.6557 -0.0179 0.0064  -0.0641 296 TYR A C   
2242 O O   . TYR A 307 ? 0.7681 0.5837 0.6453 -0.0197 0.0092  -0.0677 296 TYR A O   
2243 C CB  . TYR A 307 ? 0.7359 0.5619 0.6404 -0.0222 -0.0104 -0.0558 296 TYR A CB  
2244 C CG  . TYR A 307 ? 0.7414 0.5714 0.6323 -0.0246 -0.0129 -0.0533 296 TYR A CG  
2245 C CD1 . TYR A 307 ? 0.7546 0.5792 0.6305 -0.0293 -0.0184 -0.0560 296 TYR A CD1 
2246 C CD2 . TYR A 307 ? 0.7421 0.5805 0.6351 -0.0223 -0.0100 -0.0483 296 TYR A CD2 
2247 C CE1 . TYR A 307 ? 0.7639 0.5921 0.6280 -0.0314 -0.0211 -0.0528 296 TYR A CE1 
2248 C CE2 . TYR A 307 ? 0.7498 0.5911 0.6313 -0.0243 -0.0120 -0.0457 296 TYR A CE2 
2249 C CZ  . TYR A 307 ? 0.7657 0.6022 0.6331 -0.0287 -0.0175 -0.0476 296 TYR A CZ  
2250 O OH  . TYR A 307 ? 0.7813 0.6208 0.6382 -0.0306 -0.0201 -0.0440 296 TYR A OH  
2251 N N   . MET A 308 ? 0.7593 0.5868 0.6706 -0.0139 0.0098  -0.0592 297 MET A N   
2252 C CA  . MET A 308 ? 0.7664 0.5983 0.6777 -0.0114 0.0173  -0.0580 297 MET A CA  
2253 C C   . MET A 308 ? 0.7853 0.6093 0.6940 -0.0092 0.0281  -0.0652 297 MET A C   
2254 O O   . MET A 308 ? 0.7911 0.6159 0.6921 -0.0086 0.0350  -0.0659 297 MET A O   
2255 C CB  . MET A 308 ? 0.7547 0.5970 0.6842 -0.0086 0.0164  -0.0504 297 MET A CB  
2256 C CG  . MET A 308 ? 0.7660 0.6147 0.6968 -0.0105 0.0073  -0.0440 297 MET A CG  
2257 S SD  . MET A 308 ? 0.7852 0.6366 0.6989 -0.0140 0.0034  -0.0420 297 MET A SD  
2258 C CE  . MET A 308 ? 0.7571 0.6130 0.6706 -0.0122 0.0106  -0.0404 297 MET A CE  
2259 N N   . GLU A 309 ? 0.7945 0.6100 0.7091 -0.0080 0.0303  -0.0706 298 GLU A N   
2260 C CA  . GLU A 309 ? 0.8137 0.6196 0.7254 -0.0056 0.0419  -0.0786 298 GLU A CA  
2261 C C   . GLU A 309 ? 0.8340 0.6303 0.7172 -0.0095 0.0441  -0.0857 298 GLU A C   
2262 O O   . GLU A 309 ? 0.8403 0.6334 0.7147 -0.0081 0.0546  -0.0892 298 GLU A O   
2263 C CB  . GLU A 309 ? 0.8450 0.6426 0.7696 -0.0037 0.0430  -0.0829 298 GLU A CB  
2264 C CG  . GLU A 309 ? 0.9123 0.7132 0.8611 0.0022  0.0515  -0.0809 298 GLU A CG  
2265 C CD  . GLU A 309 ? 1.0174 0.8148 0.9862 0.0044  0.0492  -0.0805 298 GLU A CD  
2266 O OE1 . GLU A 309 ? 1.0476 0.8404 1.0120 0.0012  0.0408  -0.0815 298 GLU A OE1 
2267 O OE2 . GLU A 309 ? 1.0387 0.8383 1.0291 0.0093  0.0557  -0.0785 298 GLU A OE2 
2268 N N   . LYS A 310 ? 0.8396 0.6320 0.7085 -0.0147 0.0337  -0.0867 299 LYS A N   
2269 C CA  . LYS A 310 ? 0.8564 0.6403 0.6971 -0.0195 0.0326  -0.0920 299 LYS A CA  
2270 C C   . LYS A 310 ? 0.8577 0.6491 0.6881 -0.0201 0.0345  -0.0868 299 LYS A C   
2271 O O   . LYS A 310 ? 0.8691 0.6534 0.6778 -0.0220 0.0400  -0.0912 299 LYS A O   
2272 C CB  . LYS A 310 ? 0.8848 0.6663 0.7178 -0.0252 0.0187  -0.0913 299 LYS A CB  
2273 C CG  . LYS A 310 ? 0.9434 0.7141 0.7810 -0.0262 0.0164  -0.0979 299 LYS A CG  
2274 C CD  . LYS A 310 ? 0.9959 0.7647 0.8273 -0.0323 0.0025  -0.0968 299 LYS A CD  
2275 C CE  . LYS A 310 ? 1.0305 0.7937 0.8769 -0.0325 -0.0009 -0.0993 299 LYS A CE  
2276 N NZ  . LYS A 310 ? 1.0580 0.8089 0.9061 -0.0292 0.0099  -0.1084 299 LYS A NZ  
2277 N N   . HIS A 311 ? 0.8481 0.6531 0.6931 -0.0186 0.0301  -0.0775 300 HIS A N   
2278 C CA  . HIS A 311 ? 0.8527 0.6652 0.6911 -0.0191 0.0313  -0.0718 300 HIS A CA  
2279 C C   . HIS A 311 ? 0.8593 0.6773 0.7102 -0.0145 0.0426  -0.0698 300 HIS A C   
2280 O O   . HIS A 311 ? 0.8621 0.6892 0.7173 -0.0140 0.0424  -0.0630 300 HIS A O   
2281 C CB  . HIS A 311 ? 0.8493 0.6717 0.6941 -0.0208 0.0201  -0.0634 300 HIS A CB  
2282 C CG  . HIS A 311 ? 0.8732 0.6911 0.7043 -0.0260 0.0097  -0.0643 300 HIS A CG  
2283 N ND1 . HIS A 311 ? 0.8976 0.7160 0.7120 -0.0297 0.0053  -0.0614 300 HIS A ND1 
2284 C CD2 . HIS A 311 ? 0.8868 0.6996 0.7198 -0.0281 0.0030  -0.0673 300 HIS A CD2 
2285 C CE1 . HIS A 311 ? 0.9084 0.7226 0.7159 -0.0340 -0.0046 -0.0624 300 HIS A CE1 
2286 N NE2 . HIS A 311 ? 0.9053 0.7159 0.7236 -0.0333 -0.0062 -0.0662 300 HIS A NE2 
2287 N N   . LYS A 312 ? 0.8638 0.6756 0.7208 -0.0112 0.0527  -0.0757 301 LYS A N   
2288 C CA  . LYS A 312 ? 0.8682 0.6836 0.7392 -0.0065 0.0649  -0.0749 301 LYS A CA  
2289 C C   . LYS A 312 ? 0.8575 0.6872 0.7518 -0.0042 0.0618  -0.0654 301 LYS A C   
2290 O O   . LYS A 312 ? 0.8635 0.6995 0.7604 -0.0034 0.0669  -0.0612 301 LYS A O   
2291 C CB  . LYS A 312 ? 0.9069 0.7173 0.7578 -0.0075 0.0754  -0.0779 301 LYS A CB  
2292 C CG  . LYS A 312 ? 0.9901 0.7841 0.8171 -0.0096 0.0798  -0.0886 301 LYS A CG  
2293 C CD  . LYS A 312 ? 1.0826 0.8698 0.8947 -0.0086 0.0955  -0.0931 301 LYS A CD  
2294 C CE  . LYS A 312 ? 1.1633 0.9322 0.9492 -0.0109 0.1008  -0.1048 301 LYS A CE  
2295 N NZ  . LYS A 312 ? 1.2060 0.9677 0.9725 -0.0105 0.1164  -0.1087 301 LYS A NZ  
2296 N N   . VAL A 313 ? 0.8400 0.6740 0.7506 -0.0034 0.0534  -0.0621 302 VAL A N   
2297 C CA  . VAL A 313 ? 0.8269 0.6725 0.7585 -0.0017 0.0490  -0.0539 302 VAL A CA  
2298 C C   . VAL A 313 ? 0.8259 0.6710 0.7788 0.0017  0.0498  -0.0541 302 VAL A C   
2299 O O   . VAL A 313 ? 0.8291 0.6697 0.7822 0.0009  0.0441  -0.0561 302 VAL A O   
2300 C CB  . VAL A 313 ? 0.8246 0.6754 0.7517 -0.0049 0.0368  -0.0486 302 VAL A CB  
2301 C CG1 . VAL A 313 ? 0.8188 0.6788 0.7655 -0.0034 0.0319  -0.0414 302 VAL A CG1 
2302 C CG2 . VAL A 313 ? 0.8290 0.6811 0.7388 -0.0078 0.0360  -0.0469 302 VAL A CG2 
2303 N N   . LYS A 314 ? 0.8174 0.6670 0.7894 0.0054  0.0571  -0.0518 303 LYS A N   
2304 C CA  . LYS A 314 ? 0.8153 0.6646 0.8099 0.0090  0.0583  -0.0512 303 LYS A CA  
2305 C C   . LYS A 314 ? 0.8063 0.6608 0.8118 0.0081  0.0460  -0.0449 303 LYS A C   
2306 O O   . LYS A 314 ? 0.8046 0.6679 0.8146 0.0067  0.0395  -0.0380 303 LYS A O   
2307 C CB  . LYS A 314 ? 0.8386 0.6935 0.8545 0.0130  0.0679  -0.0484 303 LYS A CB  
2308 C CG  . LYS A 314 ? 0.9091 0.7579 0.9149 0.0145  0.0825  -0.0548 303 LYS A CG  
2309 C CD  . LYS A 314 ? 0.9727 0.8252 1.0046 0.0195  0.0935  -0.0530 303 LYS A CD  
2310 C CE  . LYS A 314 ? 1.0404 0.8844 1.0627 0.0217  0.1104  -0.0606 303 LYS A CE  
2311 N NZ  . LYS A 314 ? 1.0672 0.9128 1.1186 0.0276  0.1222  -0.0599 303 LYS A NZ  
2312 N N   . PRO A 315 ? 0.7980 0.6462 0.8072 0.0085  0.0430  -0.0473 304 PRO A N   
2313 C CA  . PRO A 315 ? 0.7821 0.6345 0.8004 0.0075  0.0320  -0.0408 304 PRO A CA  
2314 C C   . PRO A 315 ? 0.7531 0.6140 0.7955 0.0099  0.0298  -0.0328 304 PRO A C   
2315 O O   . PRO A 315 ? 0.7520 0.6178 0.7980 0.0082  0.0203  -0.0262 304 PRO A O   
2316 C CB  . PRO A 315 ? 0.7978 0.6404 0.8155 0.0076  0.0311  -0.0456 304 PRO A CB  
2317 C CG  . PRO A 315 ? 0.8151 0.6477 0.8165 0.0072  0.0395  -0.0555 304 PRO A CG  
2318 C CD  . PRO A 315 ? 0.7967 0.6328 0.8008 0.0097  0.0494  -0.0560 304 PRO A CD  
2319 N N   . ASP A 316 ? 0.7298 0.5921 0.7886 0.0136  0.0384  -0.0330 305 ASP A N   
2320 C CA  . ASP A 316 ? 0.7140 0.5851 0.7974 0.0154  0.0353  -0.0244 305 ASP A CA  
2321 C C   . ASP A 316 ? 0.6944 0.5749 0.7775 0.0136  0.0336  -0.0196 305 ASP A C   
2322 O O   . ASP A 316 ? 0.6910 0.5792 0.7939 0.0142  0.0300  -0.0123 305 ASP A O   
2323 C CB  . ASP A 316 ? 0.7360 0.6054 0.8438 0.0205  0.0440  -0.0251 305 ASP A CB  
2324 C CG  . ASP A 316 ? 0.8210 0.6857 0.9251 0.0231  0.0590  -0.0327 305 ASP A CG  
2325 O OD1 . ASP A 316 ? 0.8485 0.7022 0.9351 0.0230  0.0647  -0.0418 305 ASP A OD1 
2326 O OD2 . ASP A 316 ? 0.8450 0.7166 0.9634 0.0250  0.0652  -0.0294 305 ASP A OD2 
2327 N N   . SER A 317 ? 0.6765 0.5562 0.7382 0.0109  0.0350  -0.0229 306 SER A N   
2328 C CA  . SER A 317 ? 0.6622 0.5494 0.7228 0.0089  0.0334  -0.0187 306 SER A CA  
2329 C C   . SER A 317 ? 0.6492 0.5410 0.7075 0.0056  0.0206  -0.0125 306 SER A C   
2330 O O   . SER A 317 ? 0.6586 0.5469 0.7081 0.0042  0.0141  -0.0127 306 SER A O   
2331 C CB  . SER A 317 ? 0.6835 0.5675 0.7218 0.0072  0.0390  -0.0238 306 SER A CB  
2332 O OG  . SER A 317 ? 0.7112 0.5903 0.7289 0.0045  0.0330  -0.0266 306 SER A OG  
2333 N N   . LYS A 318 ? 0.6245 0.5234 0.6897 0.0040  0.0174  -0.0072 307 LYS A N   
2334 C CA  . LYS A 318 ? 0.6175 0.5189 0.6771 0.0004  0.0061  -0.0024 307 LYS A CA  
2335 C C   . LYS A 318 ? 0.6211 0.5188 0.6562 -0.0022 0.0045  -0.0058 307 LYS A C   
2336 O O   . LYS A 318 ? 0.6238 0.5210 0.6506 -0.0046 -0.0035 -0.0035 307 LYS A O   
2337 C CB  . LYS A 318 ? 0.6326 0.5413 0.7062 -0.0012 0.0026  0.0036  307 LYS A CB  
2338 C CG  . LYS A 318 ? 0.6585 0.5718 0.7574 0.0003  -0.0011 0.0096  307 LYS A CG  
2339 C CD  . LYS A 318 ? 0.6897 0.6092 0.7986 -0.0031 -0.0100 0.0164  307 LYS A CD  
2340 C CE  . LYS A 318 ? 0.7137 0.6395 0.8522 -0.0015 -0.0118 0.0229  307 LYS A CE  
2341 N NZ  . LYS A 318 ? 0.7329 0.6637 0.8891 0.0011  -0.0010 0.0228  307 LYS A NZ  
2342 N N   . ALA A 319 ? 0.6174 0.5126 0.6412 -0.0018 0.0122  -0.0107 308 ALA A N   
2343 C CA  . ALA A 319 ? 0.6182 0.5100 0.6210 -0.0039 0.0111  -0.0135 308 ALA A CA  
2344 C C   . ALA A 319 ? 0.6131 0.4996 0.6074 -0.0039 0.0079  -0.0162 308 ALA A C   
2345 O O   . ALA A 319 ? 0.6176 0.5030 0.6006 -0.0060 0.0027  -0.0155 308 ALA A O   
2346 C CB  . ALA A 319 ? 0.6201 0.5100 0.6139 -0.0035 0.0199  -0.0173 308 ALA A CB  
2347 N N   . PHE A 320 ? 0.5993 0.4821 0.6005 -0.0016 0.0114  -0.0192 309 PHE A N   
2348 C CA  . PHE A 320 ? 0.5974 0.4748 0.5925 -0.0020 0.0082  -0.0215 309 PHE A CA  
2349 C C   . PHE A 320 ? 0.5921 0.4716 0.5925 -0.0030 -0.0003 -0.0160 309 PHE A C   
2350 O O   . PHE A 320 ? 0.5957 0.4736 0.5858 -0.0049 -0.0048 -0.0156 309 PHE A O   
2351 C CB  . PHE A 320 ? 0.5916 0.4629 0.5923 0.0004  0.0141  -0.0266 309 PHE A CB  
2352 C CG  . PHE A 320 ? 0.6009 0.4664 0.5957 -0.0008 0.0098  -0.0287 309 PHE A CG  
2353 C CD1 . PHE A 320 ? 0.6140 0.4746 0.5916 -0.0031 0.0095  -0.0333 309 PHE A CD1 
2354 C CD2 . PHE A 320 ? 0.6031 0.4685 0.6099 -0.0001 0.0050  -0.0249 309 PHE A CD2 
2355 C CE1 . PHE A 320 ? 0.6222 0.4782 0.5965 -0.0046 0.0049  -0.0346 309 PHE A CE1 
2356 C CE2 . PHE A 320 ? 0.6115 0.4721 0.6141 -0.0015 0.0011  -0.0260 309 PHE A CE2 
2357 C CZ  . PHE A 320 ? 0.6162 0.4721 0.6033 -0.0038 0.0013  -0.0310 309 PHE A CZ  
2358 N N   . HIS A 321 ? 0.5813 0.4643 0.5977 -0.0019 -0.0026 -0.0114 310 HIS A N   
2359 C CA  . HIS A 321 ? 0.5790 0.4635 0.5989 -0.0032 -0.0109 -0.0055 310 HIS A CA  
2360 C C   . HIS A 321 ? 0.5865 0.4724 0.5925 -0.0062 -0.0158 -0.0033 310 HIS A C   
2361 O O   . HIS A 321 ? 0.5967 0.4807 0.5961 -0.0076 -0.0203 -0.0013 310 HIS A O   
2362 C CB  . HIS A 321 ? 0.5710 0.4597 0.6107 -0.0019 -0.0132 -0.0001 310 HIS A CB  
2363 C CG  . HIS A 321 ? 0.5839 0.4700 0.6385 0.0015  -0.0087 -0.0016 310 HIS A CG  
2364 N ND1 . HIS A 321 ? 0.5998 0.4828 0.6604 0.0019  -0.0128 0.0012  310 HIS A ND1 
2365 C CD2 . HIS A 321 ? 0.5934 0.4780 0.6560 0.0045  0.0005  -0.0062 310 HIS A CD2 
2366 C CE1 . HIS A 321 ? 0.5997 0.4797 0.6737 0.0053  -0.0066 -0.0017 310 HIS A CE1 
2367 N NE2 . HIS A 321 ? 0.6002 0.4807 0.6751 0.0070  0.0020  -0.0066 310 HIS A NE2 
2368 N N   . LEU A 322 ? 0.5772 0.4658 0.5787 -0.0072 -0.0141 -0.0040 311 LEU A N   
2369 C CA  . LEU A 322 ? 0.5738 0.4625 0.5625 -0.0098 -0.0177 -0.0028 311 LEU A CA  
2370 C C   . LEU A 322 ? 0.5806 0.4658 0.5557 -0.0101 -0.0162 -0.0059 311 LEU A C   
2371 O O   . LEU A 322 ? 0.5874 0.4712 0.5550 -0.0115 -0.0196 -0.0042 311 LEU A O   
2372 C CB  . LEU A 322 ? 0.5668 0.4584 0.5553 -0.0107 -0.0162 -0.0026 311 LEU A CB  
2373 C CG  . LEU A 322 ? 0.5820 0.4723 0.5578 -0.0132 -0.0192 -0.0020 311 LEU A CG  
2374 C CD1 . LEU A 322 ? 0.5977 0.4862 0.5703 -0.0150 -0.0261 0.0014  311 LEU A CD1 
2375 C CD2 . LEU A 322 ? 0.5753 0.4679 0.5527 -0.0143 -0.0177 -0.0017 311 LEU A CD2 
2376 N N   . LEU A 323 ? 0.5758 0.4595 0.5481 -0.0091 -0.0111 -0.0104 312 LEU A N   
2377 C CA  . LEU A 323 ? 0.5778 0.4585 0.5386 -0.0100 -0.0106 -0.0130 312 LEU A CA  
2378 C C   . LEU A 323 ? 0.5821 0.4606 0.5438 -0.0103 -0.0142 -0.0118 312 LEU A C   
2379 O O   . LEU A 323 ? 0.5879 0.4661 0.5429 -0.0116 -0.0163 -0.0104 312 LEU A O   
2380 C CB  . LEU A 323 ? 0.5754 0.4536 0.5324 -0.0094 -0.0054 -0.0180 312 LEU A CB  
2381 C CG  . LEU A 323 ? 0.5927 0.4672 0.5395 -0.0108 -0.0065 -0.0208 312 LEU A CG  
2382 C CD1 . LEU A 323 ? 0.5998 0.4761 0.5374 -0.0124 -0.0086 -0.0188 312 LEU A CD1 
2383 C CD2 . LEU A 323 ? 0.5991 0.4688 0.5412 -0.0105 -0.0019 -0.0264 312 LEU A CD2 
2384 N N   . GLN A 324 ? 0.5759 0.4531 0.5477 -0.0091 -0.0144 -0.0114 313 GLN A N   
2385 C CA  . GLN A 324 ? 0.5792 0.4539 0.5541 -0.0093 -0.0174 -0.0096 313 GLN A CA  
2386 C C   . GLN A 324 ? 0.5739 0.4502 0.5465 -0.0106 -0.0218 -0.0040 313 GLN A C   
2387 O O   . GLN A 324 ? 0.5792 0.4539 0.5492 -0.0116 -0.0235 -0.0023 313 GLN A O   
2388 C CB  . GLN A 324 ? 0.6019 0.4746 0.5901 -0.0074 -0.0163 -0.0100 313 GLN A CB  
2389 C CG  . GLN A 324 ? 0.6620 0.5310 0.6540 -0.0078 -0.0188 -0.0086 313 GLN A CG  
2390 C CD  . GLN A 324 ? 0.7359 0.6009 0.7400 -0.0057 -0.0163 -0.0111 313 GLN A CD  
2391 O OE1 . GLN A 324 ? 0.7739 0.6334 0.7775 -0.0061 -0.0153 -0.0149 313 GLN A OE1 
2392 N NE2 . GLN A 324 ? 0.7392 0.6065 0.7557 -0.0035 -0.0153 -0.0089 313 GLN A NE2 
2393 N N   . LYS A 325 ? 0.5616 0.4406 0.5348 -0.0110 -0.0236 -0.0012 314 LYS A N   
2394 C CA  . LYS A 325 ? 0.5610 0.4398 0.5285 -0.0127 -0.0277 0.0034  314 LYS A CA  
2395 C C   . LYS A 325 ? 0.5723 0.4505 0.5274 -0.0138 -0.0263 0.0024  314 LYS A C   
2396 O O   . LYS A 325 ? 0.5856 0.4621 0.5343 -0.0149 -0.0277 0.0054  314 LYS A O   
2397 C CB  . LYS A 325 ? 0.5671 0.4480 0.5390 -0.0134 -0.0313 0.0065  314 LYS A CB  
2398 C CG  . LYS A 325 ? 0.5885 0.4703 0.5752 -0.0122 -0.0336 0.0095  314 LYS A CG  
2399 C CD  . LYS A 325 ? 0.6191 0.5043 0.6145 -0.0127 -0.0372 0.0125  314 LYS A CD  
2400 C CE  . LYS A 325 ? 0.6448 0.5312 0.6578 -0.0111 -0.0394 0.0163  314 LYS A CE  
2401 N NZ  . LYS A 325 ? 0.6531 0.5439 0.6782 -0.0118 -0.0437 0.0204  314 LYS A NZ  
2402 N N   . LEU A 326 ? 0.5637 0.4428 0.5155 -0.0134 -0.0231 -0.0013 315 LEU A N   
2403 C CA  . LEU A 326 ? 0.5604 0.4391 0.5033 -0.0140 -0.0216 -0.0018 315 LEU A CA  
2404 C C   . LEU A 326 ? 0.5582 0.4363 0.5014 -0.0140 -0.0208 -0.0023 315 LEU A C   
2405 O O   . LEU A 326 ? 0.5645 0.4422 0.5040 -0.0144 -0.0203 -0.0004 315 LEU A O   
2406 C CB  . LEU A 326 ? 0.5566 0.4367 0.4970 -0.0139 -0.0193 -0.0044 315 LEU A CB  
2407 C CG  . LEU A 326 ? 0.5591 0.4403 0.5014 -0.0143 -0.0200 -0.0039 315 LEU A CG  
2408 C CD1 . LEU A 326 ? 0.5579 0.4410 0.5018 -0.0138 -0.0169 -0.0062 315 LEU A CD1 
2409 C CD2 . LEU A 326 ? 0.5619 0.4411 0.4970 -0.0157 -0.0215 -0.0024 315 LEU A CD2 
2410 N N   . LEU A 327 ? 0.5488 0.4263 0.4967 -0.0136 -0.0205 -0.0049 316 LEU A N   
2411 C CA  . LEU A 327 ? 0.5555 0.4317 0.5043 -0.0143 -0.0210 -0.0056 316 LEU A CA  
2412 C C   . LEU A 327 ? 0.5573 0.4318 0.5125 -0.0145 -0.0227 -0.0029 316 LEU A C   
2413 O O   . LEU A 327 ? 0.5596 0.4317 0.5201 -0.0147 -0.0233 -0.0050 316 LEU A O   
2414 C CB  . LEU A 327 ? 0.5640 0.4385 0.5117 -0.0146 -0.0201 -0.0105 316 LEU A CB  
2415 C CG  . LEU A 327 ? 0.5919 0.4676 0.5319 -0.0151 -0.0191 -0.0122 316 LEU A CG  
2416 C CD1 . LEU A 327 ? 0.5976 0.4700 0.5337 -0.0160 -0.0186 -0.0169 316 LEU A CD1 
2417 C CD2 . LEU A 327 ? 0.6040 0.4818 0.5419 -0.0160 -0.0205 -0.0091 316 LEU A CD2 
2418 N N   . THR A 328 ? 0.5536 0.4285 0.5077 -0.0148 -0.0233 0.0016  317 THR A N   
2419 C CA  . THR A 328 ? 0.5557 0.4290 0.5149 -0.0152 -0.0247 0.0055  317 THR A CA  
2420 C C   . THR A 328 ? 0.5620 0.4360 0.5207 -0.0163 -0.0236 0.0077  317 THR A C   
2421 O O   . THR A 328 ? 0.5711 0.4465 0.5238 -0.0163 -0.0215 0.0086  317 THR A O   
2422 C CB  . THR A 328 ? 0.5716 0.4446 0.5276 -0.0154 -0.0261 0.0098  317 THR A CB  
2423 O OG1 . THR A 328 ? 0.5840 0.4574 0.5445 -0.0145 -0.0279 0.0087  317 THR A OG1 
2424 C CG2 . THR A 328 ? 0.5726 0.4439 0.5312 -0.0162 -0.0272 0.0152  317 THR A CG2 
2425 N N   . MET A 329 ? 0.5553 0.4279 0.5214 -0.0172 -0.0247 0.0088  318 MET A N   
2426 C CA  . MET A 329 ? 0.5513 0.4254 0.5204 -0.0185 -0.0238 0.0118  318 MET A CA  
2427 C C   . MET A 329 ? 0.5509 0.4258 0.5157 -0.0183 -0.0206 0.0173  318 MET A C   
2428 O O   . MET A 329 ? 0.5455 0.4225 0.5086 -0.0182 -0.0176 0.0184  318 MET A O   
2429 C CB  . MET A 329 ? 0.5582 0.4300 0.5375 -0.0199 -0.0262 0.0125  318 MET A CB  
2430 C CG  . MET A 329 ? 0.5823 0.4514 0.5636 -0.0204 -0.0286 0.0061  318 MET A CG  
2431 S SD  . MET A 329 ? 0.5967 0.4680 0.5757 -0.0223 -0.0301 0.0036  318 MET A SD  
2432 C CE  . MET A 329 ? 0.5630 0.4298 0.5506 -0.0253 -0.0344 0.0016  318 MET A CE  
2433 N N   . ASP A 330 ? 0.5550 0.4278 0.5176 -0.0183 -0.0211 0.0208  319 ASP A N   
2434 C CA  . ASP A 330 ? 0.5646 0.4364 0.5197 -0.0186 -0.0179 0.0259  319 ASP A CA  
2435 C C   . ASP A 330 ? 0.5804 0.4514 0.5229 -0.0179 -0.0161 0.0238  319 ASP A C   
2436 O O   . ASP A 330 ? 0.5830 0.4529 0.5212 -0.0179 -0.0192 0.0220  319 ASP A O   
2437 C CB  . ASP A 330 ? 0.5832 0.4522 0.5388 -0.0195 -0.0202 0.0310  319 ASP A CB  
2438 C CG  . ASP A 330 ? 0.6462 0.5134 0.5938 -0.0205 -0.0165 0.0373  319 ASP A CG  
2439 O OD1 . ASP A 330 ? 0.6602 0.5275 0.5997 -0.0201 -0.0113 0.0368  319 ASP A OD1 
2440 O OD2 . ASP A 330 ? 0.6693 0.5344 0.6186 -0.0216 -0.0182 0.0430  319 ASP A OD2 
2441 N N   . PRO A 331 ? 0.5843 0.4556 0.5220 -0.0175 -0.0109 0.0244  320 PRO A N   
2442 C CA  . PRO A 331 ? 0.5931 0.4622 0.5187 -0.0170 -0.0088 0.0219  320 PRO A CA  
2443 C C   . PRO A 331 ? 0.6142 0.4786 0.5274 -0.0183 -0.0108 0.0234  320 PRO A C   
2444 O O   . PRO A 331 ? 0.6312 0.4939 0.5372 -0.0185 -0.0128 0.0203  320 PRO A O   
2445 C CB  . PRO A 331 ? 0.5959 0.4651 0.5205 -0.0161 -0.0016 0.0234  320 PRO A CB  
2446 C CG  . PRO A 331 ? 0.5934 0.4647 0.5279 -0.0166 0.0000  0.0284  320 PRO A CG  
2447 C CD  . PRO A 331 ? 0.5708 0.4445 0.5159 -0.0174 -0.0065 0.0273  320 PRO A CD  
2448 N N   . ILE A 332 ? 0.6115 0.4737 0.5221 -0.0195 -0.0109 0.0287  321 ILE A N   
2449 C CA  . ILE A 332 ? 0.6187 0.4761 0.5163 -0.0215 -0.0143 0.0311  321 ILE A CA  
2450 C C   . ILE A 332 ? 0.6133 0.4725 0.5181 -0.0219 -0.0225 0.0309  321 ILE A C   
2451 O O   . ILE A 332 ? 0.6268 0.4832 0.5229 -0.0235 -0.0270 0.0313  321 ILE A O   
2452 C CB  . ILE A 332 ? 0.6285 0.4822 0.5180 -0.0230 -0.0115 0.0377  321 ILE A CB  
2453 C CG1 . ILE A 332 ? 0.6364 0.4933 0.5408 -0.0229 -0.0126 0.0425  321 ILE A CG1 
2454 C CG2 . ILE A 332 ? 0.6383 0.4894 0.5189 -0.0223 -0.0019 0.0374  321 ILE A CG2 
2455 C CD1 . ILE A 332 ? 0.6524 0.5085 0.5603 -0.0242 -0.0200 0.0466  321 ILE A CD1 
2456 N N   . LYS A 333 ? 0.5952 0.4583 0.5158 -0.0206 -0.0244 0.0300  322 LYS A N   
2457 C CA  . LYS A 333 ? 0.5905 0.4552 0.5202 -0.0203 -0.0303 0.0293  322 LYS A CA  
2458 C C   . LYS A 333 ? 0.5952 0.4625 0.5277 -0.0191 -0.0303 0.0230  322 LYS A C   
2459 O O   . LYS A 333 ? 0.5999 0.4692 0.5425 -0.0182 -0.0331 0.0215  322 LYS A O   
2460 C CB  . LYS A 333 ? 0.5888 0.4547 0.5337 -0.0195 -0.0316 0.0312  322 LYS A CB  
2461 C CG  . LYS A 333 ? 0.6155 0.4790 0.5602 -0.0210 -0.0330 0.0388  322 LYS A CG  
2462 C CD  . LYS A 333 ? 0.6516 0.5153 0.6123 -0.0203 -0.0338 0.0403  322 LYS A CD  
2463 C CE  . LYS A 333 ? 0.6906 0.5519 0.6536 -0.0216 -0.0372 0.0488  322 LYS A CE  
2464 N NZ  . LYS A 333 ? 0.6971 0.5574 0.6700 -0.0220 -0.0352 0.0523  322 LYS A NZ  
2465 N N   . ARG A 334 ? 0.5890 0.4561 0.5136 -0.0189 -0.0266 0.0196  323 ARG A N   
2466 C CA  . ARG A 334 ? 0.5847 0.4539 0.5109 -0.0179 -0.0260 0.0144  323 ARG A CA  
2467 C C   . ARG A 334 ? 0.5888 0.4560 0.5070 -0.0193 -0.0289 0.0140  323 ARG A C   
2468 O O   . ARG A 334 ? 0.6006 0.4636 0.5064 -0.0209 -0.0287 0.0156  323 ARG A O   
2469 C CB  . ARG A 334 ? 0.5944 0.4642 0.5180 -0.0170 -0.0209 0.0121  323 ARG A CB  
2470 C CG  . ARG A 334 ? 0.6088 0.4818 0.5381 -0.0159 -0.0202 0.0079  323 ARG A CG  
2471 C CD  . ARG A 334 ? 0.6240 0.4980 0.5532 -0.0153 -0.0165 0.0076  323 ARG A CD  
2472 N NE  . ARG A 334 ? 0.6476 0.5231 0.5846 -0.0154 -0.0165 0.0094  323 ARG A NE  
2473 C CZ  . ARG A 334 ? 0.6809 0.5577 0.6208 -0.0153 -0.0137 0.0113  323 ARG A CZ  
2474 N NH1 . ARG A 334 ? 0.6838 0.5604 0.6196 -0.0145 -0.0098 0.0117  323 ARG A NH1 
2475 N NH2 . ARG A 334 ? 0.6740 0.5522 0.6225 -0.0160 -0.0148 0.0131  323 ARG A NH2 
2476 N N   . ILE A 335 ? 0.5764 0.4462 0.5012 -0.0190 -0.0313 0.0119  324 ILE A N   
2477 C CA  . ILE A 335 ? 0.5807 0.4493 0.5011 -0.0207 -0.0349 0.0117  324 ILE A CA  
2478 C C   . ILE A 335 ? 0.5932 0.4582 0.5012 -0.0215 -0.0319 0.0088  324 ILE A C   
2479 O O   . ILE A 335 ? 0.6010 0.4659 0.5072 -0.0200 -0.0265 0.0068  324 ILE A O   
2480 C CB  . ILE A 335 ? 0.5842 0.4575 0.5177 -0.0196 -0.0359 0.0098  324 ILE A CB  
2481 C CG1 . ILE A 335 ? 0.5948 0.4686 0.5320 -0.0215 -0.0420 0.0123  324 ILE A CG1 
2482 C CG2 . ILE A 335 ? 0.5944 0.4692 0.5275 -0.0184 -0.0312 0.0053  324 ILE A CG2 
2483 C CD1 . ILE A 335 ? 0.6050 0.4842 0.5580 -0.0200 -0.0414 0.0109  324 ILE A CD1 
2484 N N   . THR A 336 ? 0.5902 0.4517 0.4907 -0.0240 -0.0357 0.0086  325 THR A N   
2485 C CA  . THR A 336 ? 0.5921 0.4488 0.4817 -0.0248 -0.0328 0.0052  325 THR A CA  
2486 C C   . THR A 336 ? 0.5913 0.4512 0.4890 -0.0247 -0.0334 0.0026  325 THR A C   
2487 O O   . THR A 336 ? 0.5844 0.4494 0.4941 -0.0245 -0.0364 0.0038  325 THR A O   
2488 C CB  . THR A 336 ? 0.6074 0.4562 0.4808 -0.0283 -0.0362 0.0060  325 THR A CB  
2489 O OG1 . THR A 336 ? 0.6179 0.4675 0.4946 -0.0312 -0.0448 0.0079  325 THR A OG1 
2490 C CG2 . THR A 336 ? 0.6078 0.4532 0.4718 -0.0285 -0.0344 0.0091  325 THR A CG2 
2491 N N   . SER A 337 ? 0.5959 0.4525 0.4879 -0.0246 -0.0299 -0.0005 326 SER A N   
2492 C CA  . SER A 337 ? 0.6026 0.4615 0.5016 -0.0248 -0.0300 -0.0023 326 SER A CA  
2493 C C   . SER A 337 ? 0.6140 0.4717 0.5142 -0.0283 -0.0370 -0.0015 326 SER A C   
2494 O O   . SER A 337 ? 0.6153 0.4777 0.5269 -0.0284 -0.0382 -0.0011 326 SER A O   
2495 C CB  . SER A 337 ? 0.6179 0.4724 0.5108 -0.0241 -0.0250 -0.0051 326 SER A CB  
2496 O OG  . SER A 337 ? 0.6570 0.5026 0.5356 -0.0261 -0.0252 -0.0066 326 SER A OG  
2497 N N   . GLU A 338 ? 0.6208 0.4720 0.5091 -0.0314 -0.0416 -0.0010 327 GLU A N   
2498 C CA  . GLU A 338 ? 0.6304 0.4799 0.5189 -0.0356 -0.0502 0.0005  327 GLU A CA  
2499 C C   . GLU A 338 ? 0.6162 0.4741 0.5211 -0.0350 -0.0547 0.0051  327 GLU A C   
2500 O O   . GLU A 338 ? 0.6151 0.4776 0.5332 -0.0362 -0.0584 0.0065  327 GLU A O   
2501 C CB  . GLU A 338 ? 0.6976 0.5373 0.5663 -0.0393 -0.0543 0.0005  327 GLU A CB  
2502 C CG  . GLU A 338 ? 0.8107 0.6423 0.6627 -0.0379 -0.0464 -0.0032 327 GLU A CG  
2503 C CD  . GLU A 338 ? 0.9177 0.7468 0.7593 -0.0369 -0.0434 -0.0012 327 GLU A CD  
2504 O OE1 . GLU A 338 ? 0.9205 0.7497 0.7593 -0.0392 -0.0499 0.0030  327 GLU A OE1 
2505 O OE2 . GLU A 338 ? 0.9572 0.7845 0.7947 -0.0339 -0.0345 -0.0030 327 GLU A OE2 
2506 N N   . GLN A 339 ? 0.6040 0.4640 0.5099 -0.0329 -0.0535 0.0075  328 GLN A N   
2507 C CA  . GLN A 339 ? 0.5902 0.4570 0.5119 -0.0317 -0.0565 0.0117  328 GLN A CA  
2508 C C   . GLN A 339 ? 0.5722 0.4462 0.5106 -0.0283 -0.0514 0.0103  328 GLN A C   
2509 O O   . GLN A 339 ? 0.5668 0.4462 0.5212 -0.0279 -0.0540 0.0130  328 GLN A O   
2510 C CB  . GLN A 339 ? 0.6119 0.4778 0.5297 -0.0301 -0.0550 0.0139  328 GLN A CB  
2511 C CG  . GLN A 339 ? 0.6674 0.5284 0.5744 -0.0334 -0.0619 0.0183  328 GLN A CG  
2512 C CD  . GLN A 339 ? 0.7298 0.5902 0.6341 -0.0315 -0.0587 0.0206  328 GLN A CD  
2513 O OE1 . GLN A 339 ? 0.7441 0.6035 0.6437 -0.0292 -0.0510 0.0177  328 GLN A OE1 
2514 N NE2 . GLN A 339 ? 0.7449 0.6061 0.6539 -0.0325 -0.0647 0.0266  328 GLN A NE2 
2515 N N   . ALA A 340 ? 0.5624 0.4363 0.4974 -0.0259 -0.0440 0.0064  329 ALA A N   
2516 C CA  . ALA A 340 ? 0.5516 0.4309 0.4980 -0.0233 -0.0388 0.0047  329 ALA A CA  
2517 C C   . ALA A 340 ? 0.5505 0.4321 0.5048 -0.0249 -0.0403 0.0050  329 ALA A C   
2518 O O   . ALA A 340 ? 0.5454 0.4326 0.5144 -0.0237 -0.0391 0.0062  329 ALA A O   
2519 C CB  . ALA A 340 ? 0.5492 0.4272 0.4881 -0.0213 -0.0323 0.0014  329 ALA A CB  
2520 N N   . MET A 341 ? 0.5523 0.4294 0.4980 -0.0279 -0.0429 0.0041  330 MET A N   
2521 C CA  . MET A 341 ? 0.5593 0.4381 0.5131 -0.0302 -0.0451 0.0047  330 MET A CA  
2522 C C   . MET A 341 ? 0.5635 0.4467 0.5318 -0.0322 -0.0522 0.0091  330 MET A C   
2523 O O   . MET A 341 ? 0.5521 0.4404 0.5352 -0.0327 -0.0520 0.0108  330 MET A O   
2524 C CB  . MET A 341 ? 0.5757 0.4467 0.5161 -0.0334 -0.0472 0.0024  330 MET A CB  
2525 C CG  . MET A 341 ? 0.5978 0.4663 0.5312 -0.0313 -0.0399 -0.0009 330 MET A CG  
2526 S SD  . MET A 341 ? 0.6466 0.5037 0.5631 -0.0342 -0.0412 -0.0043 330 MET A SD  
2527 C CE  . MET A 341 ? 0.6050 0.4618 0.5301 -0.0387 -0.0471 -0.0034 330 MET A CE  
2528 N N   . GLN A 342 ? 0.5769 0.4586 0.5424 -0.0333 -0.0582 0.0118  331 GLN A N   
2529 C CA  . GLN A 342 ? 0.5812 0.4676 0.5623 -0.0349 -0.0657 0.0172  331 GLN A CA  
2530 C C   . GLN A 342 ? 0.5765 0.4701 0.5758 -0.0306 -0.0614 0.0193  331 GLN A C   
2531 O O   . GLN A 342 ? 0.5799 0.4780 0.5953 -0.0312 -0.0670 0.0245  331 GLN A O   
2532 C CB  . GLN A 342 ? 0.6166 0.4977 0.5865 -0.0387 -0.0754 0.0202  331 GLN A CB  
2533 C CG  . GLN A 342 ? 0.7030 0.5800 0.6679 -0.0445 -0.0840 0.0207  331 GLN A CG  
2534 C CD  . GLN A 342 ? 0.8242 0.6901 0.7622 -0.0470 -0.0845 0.0167  331 GLN A CD  
2535 O OE1 . GLN A 342 ? 0.8671 0.7285 0.7914 -0.0471 -0.0858 0.0176  331 GLN A OE1 
2536 N NE2 . GLN A 342 ? 0.8466 0.7074 0.7769 -0.0488 -0.0825 0.0121  331 GLN A NE2 
2537 N N   . ASP A 343 ? 0.5691 0.4635 0.5669 -0.0264 -0.0519 0.0156  332 ASP A N   
2538 C CA  . ASP A 343 ? 0.5648 0.4639 0.5779 -0.0224 -0.0470 0.0163  332 ASP A CA  
2539 C C   . ASP A 343 ? 0.5553 0.4614 0.5905 -0.0217 -0.0451 0.0187  332 ASP A C   
2540 O O   . ASP A 343 ? 0.5608 0.4682 0.5968 -0.0230 -0.0430 0.0177  332 ASP A O   
2541 C CB  . ASP A 343 ? 0.5743 0.4716 0.5788 -0.0190 -0.0378 0.0111  332 ASP A CB  
2542 C CG  . ASP A 343 ? 0.5986 0.4971 0.6126 -0.0156 -0.0343 0.0110  332 ASP A CG  
2543 O OD1 . ASP A 343 ? 0.6037 0.5004 0.6173 -0.0158 -0.0390 0.0136  332 ASP A OD1 
2544 O OD2 . ASP A 343 ? 0.6144 0.5150 0.6364 -0.0129 -0.0269 0.0085  332 ASP A OD2 
2545 N N   . PRO A 344 ? 0.5381 0.4486 0.5926 -0.0194 -0.0452 0.0222  333 PRO A N   
2546 C CA  . PRO A 344 ? 0.5306 0.4482 0.6084 -0.0181 -0.0417 0.0248  333 PRO A CA  
2547 C C   . PRO A 344 ? 0.5337 0.4524 0.6115 -0.0152 -0.0292 0.0200  333 PRO A C   
2548 O O   . PRO A 344 ? 0.5234 0.4476 0.6178 -0.0148 -0.0253 0.0221  333 PRO A O   
2549 C CB  . PRO A 344 ? 0.5305 0.4512 0.6278 -0.0153 -0.0430 0.0290  333 PRO A CB  
2550 C CG  . PRO A 344 ? 0.5361 0.4509 0.6188 -0.0139 -0.0427 0.0264  333 PRO A CG  
2551 C CD  . PRO A 344 ? 0.5270 0.4363 0.5849 -0.0176 -0.0478 0.0246  333 PRO A CD  
2552 N N   . TYR A 345 ? 0.5436 0.4572 0.6030 -0.0135 -0.0232 0.0142  334 TYR A N   
2553 C CA  . TYR A 345 ? 0.5553 0.4684 0.6093 -0.0115 -0.0124 0.0096  334 TYR A CA  
2554 C C   . TYR A 345 ? 0.5647 0.4798 0.6176 -0.0142 -0.0120 0.0107  334 TYR A C   
2555 O O   . TYR A 345 ? 0.5634 0.4814 0.6231 -0.0129 -0.0036 0.0102  334 TYR A O   
2556 C CB  . TYR A 345 ? 0.5687 0.4756 0.6016 -0.0107 -0.0103 0.0044  334 TYR A CB  
2557 C CG  . TYR A 345 ? 0.5899 0.4950 0.6108 -0.0102 -0.0023 0.0003  334 TYR A CG  
2558 C CD1 . TYR A 345 ? 0.6067 0.5127 0.6331 -0.0076 0.0074  -0.0020 334 TYR A CD1 
2559 C CD2 . TYR A 345 ? 0.6074 0.5091 0.6109 -0.0121 -0.0042 -0.0013 334 TYR A CD2 
2560 C CE1 . TYR A 345 ? 0.6255 0.5290 0.6382 -0.0076 0.0140  -0.0053 334 TYR A CE1 
2561 C CE2 . TYR A 345 ? 0.6265 0.5266 0.6192 -0.0118 0.0019  -0.0040 334 TYR A CE2 
2562 C CZ  . TYR A 345 ? 0.6433 0.5442 0.6395 -0.0098 0.0105  -0.0059 334 TYR A CZ  
2563 O OH  . TYR A 345 ? 0.6730 0.5718 0.6565 -0.0101 0.0161  -0.0080 334 TYR A OH  
2564 N N   . PHE A 346 ? 0.5701 0.4830 0.6141 -0.0180 -0.0205 0.0121  335 PHE A N   
2565 C CA  . PHE A 346 ? 0.5728 0.4862 0.6160 -0.0212 -0.0215 0.0131  335 PHE A CA  
2566 C C   . PHE A 346 ? 0.5700 0.4900 0.6364 -0.0230 -0.0242 0.0185  335 PHE A C   
2567 O O   . PHE A 346 ? 0.5737 0.4954 0.6443 -0.0251 -0.0228 0.0198  335 PHE A O   
2568 C CB  . PHE A 346 ? 0.5779 0.4850 0.6032 -0.0245 -0.0288 0.0118  335 PHE A CB  
2569 C CG  . PHE A 346 ? 0.5956 0.4975 0.6017 -0.0226 -0.0248 0.0074  335 PHE A CG  
2570 C CD1 . PHE A 346 ? 0.6070 0.5087 0.6074 -0.0210 -0.0169 0.0050  335 PHE A CD1 
2571 C CD2 . PHE A 346 ? 0.6102 0.5076 0.6046 -0.0227 -0.0290 0.0062  335 PHE A CD2 
2572 C CE1 . PHE A 346 ? 0.6201 0.5177 0.6050 -0.0197 -0.0144 0.0018  335 PHE A CE1 
2573 C CE2 . PHE A 346 ? 0.6213 0.5150 0.6013 -0.0211 -0.0253 0.0029  335 PHE A CE2 
2574 C CZ  . PHE A 346 ? 0.6200 0.5140 0.5961 -0.0196 -0.0186 0.0008  335 PHE A CZ  
2575 N N   . LEU A 347 ? 0.5638 0.4879 0.6470 -0.0222 -0.0283 0.0223  336 LEU A N   
2576 C CA  . LEU A 347 ? 0.5632 0.4949 0.6730 -0.0234 -0.0310 0.0284  336 LEU A CA  
2577 C C   . LEU A 347 ? 0.5678 0.5054 0.6962 -0.0187 -0.0182 0.0288  336 LEU A C   
2578 O O   . LEU A 347 ? 0.5609 0.5055 0.7118 -0.0193 -0.0165 0.0335  336 LEU A O   
2579 C CB  . LEU A 347 ? 0.5590 0.4922 0.6790 -0.0249 -0.0426 0.0334  336 LEU A CB  
2580 C CG  . LEU A 347 ? 0.5756 0.5026 0.6780 -0.0300 -0.0555 0.0337  336 LEU A CG  
2581 C CD1 . LEU A 347 ? 0.5746 0.5030 0.6866 -0.0312 -0.0662 0.0394  336 LEU A CD1 
2582 C CD2 . LEU A 347 ? 0.5828 0.5092 0.6849 -0.0353 -0.0610 0.0348  336 LEU A CD2 
2583 N N   . GLU A 348 ? 0.5770 0.5114 0.6966 -0.0142 -0.0092 0.0239  337 GLU A N   
2584 C CA  . GLU A 348 ? 0.5826 0.5196 0.7136 -0.0095 0.0045  0.0223  337 GLU A CA  
2585 C C   . GLU A 348 ? 0.5972 0.5349 0.7227 -0.0101 0.0138  0.0209  337 GLU A C   
2586 O O   . GLU A 348 ? 0.6068 0.5403 0.7124 -0.0127 0.0114  0.0187  337 GLU A O   
2587 C CB  . GLU A 348 ? 0.6114 0.5417 0.7267 -0.0060 0.0095  0.0160  337 GLU A CB  
2588 C CG  . GLU A 348 ? 0.6540 0.5849 0.7833 -0.0008 0.0206  0.0142  337 GLU A CG  
2589 C CD  . GLU A 348 ? 0.7329 0.6556 0.8438 0.0016  0.0246  0.0072  337 GLU A CD  
2590 O OE1 . GLU A 348 ? 0.7584 0.6760 0.8462 0.0007  0.0280  0.0022  337 GLU A OE1 
2591 O OE2 . GLU A 348 ? 0.7393 0.6605 0.8599 0.0042  0.0237  0.0072  337 GLU A OE2 
2592 N N   . ASP A 349 ? 0.5970 0.5397 0.7405 -0.0075 0.0248  0.0226  338 ASP A N   
2593 C CA  . ASP A 349 ? 0.6075 0.5511 0.7468 -0.0081 0.0347  0.0224  338 ASP A CA  
2594 C C   . ASP A 349 ? 0.6171 0.5528 0.7285 -0.0063 0.0429  0.0152  338 ASP A C   
2595 O O   . ASP A 349 ? 0.6159 0.5475 0.7221 -0.0028 0.0478  0.0106  338 ASP A O   
2596 C CB  . ASP A 349 ? 0.6215 0.5727 0.7888 -0.0054 0.0458  0.0265  338 ASP A CB  
2597 C CG  . ASP A 349 ? 0.6915 0.6445 0.8574 -0.0063 0.0567  0.0278  338 ASP A CG  
2598 O OD1 . ASP A 349 ? 0.6953 0.6501 0.8604 -0.0108 0.0502  0.0314  338 ASP A OD1 
2599 O OD2 . ASP A 349 ? 0.7278 0.6797 0.8926 -0.0026 0.0719  0.0252  338 ASP A OD2 
2600 N N   . PRO A 350 ? 0.6243 0.5573 0.7180 -0.0089 0.0438  0.0145  339 PRO A N   
2601 C CA  . PRO A 350 ? 0.6258 0.5615 0.7231 -0.0132 0.0383  0.0192  339 PRO A CA  
2602 C C   . PRO A 350 ? 0.6342 0.5666 0.7216 -0.0167 0.0237  0.0191  339 PRO A C   
2603 O O   . PRO A 350 ? 0.6460 0.5730 0.7170 -0.0158 0.0198  0.0149  339 PRO A O   
2604 C CB  . PRO A 350 ? 0.6389 0.5712 0.7184 -0.0134 0.0474  0.0177  339 PRO A CB  
2605 C CG  . PRO A 350 ? 0.6528 0.5780 0.7092 -0.0111 0.0498  0.0111  339 PRO A CG  
2606 C CD  . PRO A 350 ? 0.6308 0.5565 0.6982 -0.0077 0.0504  0.0087  339 PRO A CD  
2607 N N   . LEU A 351 ? 0.6228 0.5577 0.7199 -0.0208 0.0162  0.0235  340 LEU A N   
2608 C CA  . LEU A 351 ? 0.6259 0.5558 0.7110 -0.0243 0.0038  0.0225  340 LEU A CA  
2609 C C   . LEU A 351 ? 0.6317 0.5550 0.6934 -0.0249 0.0059  0.0192  340 LEU A C   
2610 O O   . LEU A 351 ? 0.6347 0.5586 0.6940 -0.0244 0.0144  0.0200  340 LEU A O   
2611 C CB  . LEU A 351 ? 0.6230 0.5557 0.7238 -0.0292 -0.0053 0.0275  340 LEU A CB  
2612 C CG  . LEU A 351 ? 0.6336 0.5732 0.7596 -0.0300 -0.0112 0.0324  340 LEU A CG  
2613 C CD1 . LEU A 351 ? 0.6357 0.5746 0.7679 -0.0362 -0.0244 0.0357  340 LEU A CD1 
2614 C CD2 . LEU A 351 ? 0.6471 0.5857 0.7706 -0.0272 -0.0148 0.0307  340 LEU A CD2 
2615 N N   . PRO A 352 ? 0.6331 0.5500 0.6781 -0.0260 -0.0016 0.0162  341 PRO A N   
2616 C CA  . PRO A 352 ? 0.6387 0.5500 0.6654 -0.0265 -0.0001 0.0141  341 PRO A CA  
2617 C C   . PRO A 352 ? 0.6481 0.5592 0.6806 -0.0300 -0.0009 0.0174  341 PRO A C   
2618 O O   . PRO A 352 ? 0.6451 0.5578 0.6909 -0.0333 -0.0071 0.0200  341 PRO A O   
2619 C CB  . PRO A 352 ? 0.6495 0.5548 0.6626 -0.0271 -0.0082 0.0110  341 PRO A CB  
2620 C CG  . PRO A 352 ? 0.6537 0.5613 0.6742 -0.0262 -0.0123 0.0110  341 PRO A CG  
2621 C CD  . PRO A 352 ? 0.6272 0.5418 0.6700 -0.0270 -0.0115 0.0152  341 PRO A CD  
2622 N N   . THR A 353 ? 0.6566 0.5656 0.6798 -0.0297 0.0047  0.0177  342 THR A N   
2623 C CA  . THR A 353 ? 0.6633 0.5712 0.6916 -0.0329 0.0045  0.0212  342 THR A CA  
2624 C C   . THR A 353 ? 0.6773 0.5771 0.6909 -0.0340 0.0001  0.0191  342 THR A C   
2625 O O   . THR A 353 ? 0.6787 0.5750 0.6776 -0.0318 -0.0001 0.0159  342 THR A O   
2626 C CB  . THR A 353 ? 0.6729 0.5848 0.7049 -0.0319 0.0150  0.0248  342 THR A CB  
2627 O OG1 . THR A 353 ? 0.6919 0.6010 0.7057 -0.0291 0.0201  0.0224  342 THR A OG1 
2628 C CG2 . THR A 353 ? 0.6657 0.5853 0.7157 -0.0308 0.0207  0.0271  342 THR A CG2 
2629 N N   . SER A 354 ? 0.6890 0.5857 0.7081 -0.0376 -0.0034 0.0212  343 SER A N   
2630 C CA  . SER A 354 ? 0.7148 0.6030 0.7222 -0.0385 -0.0062 0.0194  343 SER A CA  
2631 C C   . SER A 354 ? 0.7317 0.6192 0.7308 -0.0364 0.0006  0.0216  343 SER A C   
2632 O O   . SER A 354 ? 0.7429 0.6244 0.7319 -0.0356 -0.0006 0.0203  343 SER A O   
2633 C CB  . SER A 354 ? 0.7338 0.6175 0.7498 -0.0432 -0.0118 0.0205  343 SER A CB  
2634 O OG  . SER A 354 ? 0.7667 0.6562 0.7991 -0.0452 -0.0084 0.0259  343 SER A OG  
2635 N N   . ASP A 355 ? 0.7341 0.6276 0.7374 -0.0355 0.0079  0.0253  344 ASP A N   
2636 C CA  . ASP A 355 ? 0.7516 0.6451 0.7459 -0.0340 0.0142  0.0282  344 ASP A CA  
2637 C C   . ASP A 355 ? 0.7615 0.6589 0.7482 -0.0309 0.0189  0.0259  344 ASP A C   
2638 O O   . ASP A 355 ? 0.7586 0.6613 0.7538 -0.0305 0.0240  0.0268  344 ASP A O   
2639 C CB  . ASP A 355 ? 0.7704 0.6667 0.7757 -0.0363 0.0194  0.0345  344 ASP A CB  
2640 C CG  . ASP A 355 ? 0.8396 0.7360 0.8353 -0.0355 0.0262  0.0389  344 ASP A CG  
2641 O OD1 . ASP A 355 ? 0.8551 0.7502 0.8354 -0.0332 0.0272  0.0370  344 ASP A OD1 
2642 O OD2 . ASP A 355 ? 0.8745 0.7722 0.8782 -0.0377 0.0304  0.0448  344 ASP A OD2 
2643 N N   . VAL A 356 ? 0.7702 0.6647 0.7425 -0.0288 0.0172  0.0228  345 VAL A N   
2644 C CA  . VAL A 356 ? 0.7818 0.6784 0.7460 -0.0263 0.0207  0.0198  345 VAL A CA  
2645 C C   . VAL A 356 ? 0.7994 0.6983 0.7598 -0.0261 0.0296  0.0226  345 VAL A C   
2646 O O   . VAL A 356 ? 0.7990 0.7000 0.7581 -0.0245 0.0345  0.0200  345 VAL A O   
2647 C CB  . VAL A 356 ? 0.7911 0.6839 0.7414 -0.0247 0.0166  0.0167  345 VAL A CB  
2648 C CG1 . VAL A 356 ? 0.7976 0.6877 0.7506 -0.0247 0.0096  0.0139  345 VAL A CG1 
2649 C CG2 . VAL A 356 ? 0.7977 0.6878 0.7380 -0.0252 0.0170  0.0203  345 VAL A CG2 
2650 N N   . PHE A 357 ? 0.8161 0.7142 0.7751 -0.0279 0.0323  0.0280  346 PHE A N   
2651 C CA  . PHE A 357 ? 0.8413 0.7409 0.7947 -0.0281 0.0413  0.0314  346 PHE A CA  
2652 C C   . PHE A 357 ? 0.8660 0.7709 0.8362 -0.0287 0.0485  0.0338  346 PHE A C   
2653 O O   . PHE A 357 ? 0.8661 0.7724 0.8321 -0.0282 0.0582  0.0354  346 PHE A O   
2654 C CB  . PHE A 357 ? 0.8408 0.7373 0.7850 -0.0299 0.0411  0.0373  346 PHE A CB  
2655 C CG  . PHE A 357 ? 0.8522 0.7444 0.7835 -0.0292 0.0340  0.0359  346 PHE A CG  
2656 C CD1 . PHE A 357 ? 0.8653 0.7562 0.7822 -0.0278 0.0334  0.0318  346 PHE A CD1 
2657 C CD2 . PHE A 357 ? 0.8599 0.7492 0.7950 -0.0299 0.0280  0.0387  346 PHE A CD2 
2658 C CE1 . PHE A 357 ? 0.8736 0.7616 0.7815 -0.0274 0.0264  0.0313  346 PHE A CE1 
2659 C CE2 . PHE A 357 ? 0.8701 0.7564 0.7964 -0.0289 0.0221  0.0381  346 PHE A CE2 
2660 C CZ  . PHE A 357 ? 0.8691 0.7554 0.7826 -0.0278 0.0212  0.0348  346 PHE A CZ  
2661 N N   . ALA A 358 ? 0.8829 0.7902 0.8717 -0.0299 0.0438  0.0343  347 ALA A N   
2662 C CA  . ALA A 358 ? 0.9016 0.8149 0.9116 -0.0310 0.0479  0.0373  347 ALA A CA  
2663 C C   . ALA A 358 ? 0.9358 0.8516 0.9491 -0.0321 0.0584  0.0437  347 ALA A C   
2664 O O   . ALA A 358 ? 0.9367 0.8563 0.9532 -0.0305 0.0685  0.0440  347 ALA A O   
2665 C CB  . ALA A 358 ? 0.8983 0.8155 0.9160 -0.0284 0.0500  0.0332  347 ALA A CB  
2666 N N   . GLY A 359 ? 0.9579 0.8711 0.9700 -0.0348 0.0566  0.0489  348 GLY A N   
2667 C CA  . GLY A 359 ? 0.9817 0.8968 0.9969 -0.0366 0.0657  0.0564  348 GLY A CA  
2668 C C   . GLY A 359 ? 1.0185 0.9308 1.0110 -0.0354 0.0739  0.0578  348 GLY A C   
2669 O O   . GLY A 359 ? 1.0243 0.9348 1.0112 -0.0375 0.0771  0.0645  348 GLY A O   
2670 N N   . CYS A 360 ? 1.0396 0.9511 1.0186 -0.0325 0.0771  0.0516  349 CYS A N   
2671 C CA  . CYS A 360 ? 1.0681 0.9757 1.0225 -0.0317 0.0843  0.0509  349 CYS A CA  
2672 C C   . CYS A 360 ? 1.0910 0.9932 1.0269 -0.0336 0.0787  0.0548  349 CYS A C   
2673 O O   . CYS A 360 ? 1.0954 0.9952 1.0310 -0.0337 0.0678  0.0534  349 CYS A O   
2674 C CB  . CYS A 360 ? 1.0830 0.9887 1.0273 -0.0287 0.0844  0.0421  349 CYS A CB  
2675 S SG  . CYS A 360 ? 1.1178 1.0296 1.0878 -0.0261 0.0847  0.0373  349 CYS A SG  
2676 N N   . GLN A 361 ? 1.1020 1.0019 1.0226 -0.0351 0.0864  0.0602  350 GLN A N   
2677 C CA  . GLN A 361 ? 1.1193 1.0144 1.0227 -0.0372 0.0811  0.0655  350 GLN A CA  
2678 C C   . GLN A 361 ? 1.1196 1.0104 1.0054 -0.0361 0.0723  0.0596  350 GLN A C   
2679 O O   . GLN A 361 ? 1.1316 1.0198 1.0002 -0.0354 0.0765  0.0546  350 GLN A O   
2680 C CB  . GLN A 361 ? 1.1620 1.0549 1.0484 -0.0392 0.0916  0.0720  350 GLN A CB  
2681 C CG  . GLN A 361 ? 1.2233 1.1211 1.1265 -0.0401 0.1034  0.0778  350 GLN A CG  
2682 C CD  . GLN A 361 ? 1.3072 1.2021 1.1905 -0.0419 0.1153  0.0836  350 GLN A CD  
2683 O OE1 . GLN A 361 ? 1.3404 1.2296 1.1995 -0.0439 0.1121  0.0872  350 GLN A OE1 
2684 N NE2 . GLN A 361 ? 1.3141 1.2128 1.2072 -0.0414 0.1296  0.0851  350 GLN A NE2 
2685 N N   . ILE A 362 ? 1.1010 0.9906 0.9920 -0.0360 0.0608  0.0599  351 ILE A N   
2686 C CA  . ILE A 362 ? 1.0898 0.9763 0.9689 -0.0351 0.0515  0.0556  351 ILE A CA  
2687 C C   . ILE A 362 ? 1.0843 0.9666 0.9374 -0.0368 0.0522  0.0578  351 ILE A C   
2688 O O   . ILE A 362 ? 1.0947 0.9752 0.9407 -0.0391 0.0511  0.0663  351 ILE A O   
2689 C CB  . ILE A 362 ? 1.0889 0.9746 0.9786 -0.0351 0.0417  0.0589  351 ILE A CB  
2690 C CG1 . ILE A 362 ? 1.0911 0.9791 1.0032 -0.0342 0.0404  0.0562  351 ILE A CG1 
2691 C CG2 . ILE A 362 ? 1.0975 0.9808 0.9776 -0.0341 0.0328  0.0558  351 ILE A CG2 
2692 C CD1 . ILE A 362 ? 1.1029 0.9884 1.0253 -0.0346 0.0335  0.0599  351 ILE A CD1 
2693 N N   . PRO A 363 ? 1.0672 0.9471 0.9052 -0.0362 0.0542  0.0507  352 PRO A N   
2694 C CA  . PRO A 363 ? 1.0623 0.9367 0.8727 -0.0387 0.0542  0.0523  352 PRO A CA  
2695 C C   . PRO A 363 ? 1.0456 0.9177 0.8473 -0.0401 0.0411  0.0550  352 PRO A C   
2696 O O   . PRO A 363 ? 1.0558 0.9238 0.8371 -0.0432 0.0386  0.0598  352 PRO A O   
2697 C CB  . PRO A 363 ? 1.0790 0.9506 0.8785 -0.0375 0.0608  0.0426  352 PRO A CB  
2698 C CG  . PRO A 363 ? 1.0787 0.9546 0.8999 -0.0341 0.0588  0.0360  352 PRO A CG  
2699 C CD  . PRO A 363 ? 1.0544 0.9357 0.8994 -0.0334 0.0559  0.0411  352 PRO A CD  
2700 N N   . TYR A 364 ? 1.0218 0.8964 0.8394 -0.0380 0.0330  0.0524  353 TYR A N   
2701 C CA  . TYR A 364 ? 1.0126 0.8864 0.8287 -0.0384 0.0211  0.0545  353 TYR A CA  
2702 C C   . TYR A 364 ? 1.0123 0.8858 0.8288 -0.0403 0.0164  0.0655  353 TYR A C   
2703 O O   . TYR A 364 ? 1.0085 0.8838 0.8400 -0.0396 0.0191  0.0704  353 TYR A O   
2704 C CB  . TYR A 364 ? 0.9947 0.8716 0.8306 -0.0353 0.0165  0.0494  353 TYR A CB  
2705 C CG  . TYR A 364 ? 0.9879 0.8656 0.8270 -0.0333 0.0212  0.0397  353 TYR A CG  
2706 C CD1 . TYR A 364 ? 0.9985 0.8734 0.8235 -0.0337 0.0203  0.0334  353 TYR A CD1 
2707 C CD2 . TYR A 364 ? 0.9864 0.8672 0.8425 -0.0314 0.0264  0.0374  353 TYR A CD2 
2708 C CE1 . TYR A 364 ? 1.0053 0.8805 0.8344 -0.0317 0.0250  0.0252  353 TYR A CE1 
2709 C CE2 . TYR A 364 ? 0.9927 0.8746 0.8531 -0.0295 0.0304  0.0298  353 TYR A CE2 
2710 C CZ  . TYR A 364 ? 1.0078 0.8869 0.8552 -0.0294 0.0301  0.0238  353 TYR A CZ  
2711 O OH  . TYR A 364 ? 1.0248 0.9045 0.8779 -0.0274 0.0340  0.0167  353 TYR A OH  
2712 N N   . PRO A 365 ? 1.0170 0.8879 0.8182 -0.0428 0.0085  0.0700  354 PRO A N   
2713 C CA  . PRO A 365 ? 1.0218 0.8925 0.8254 -0.0444 0.0029  0.0818  354 PRO A CA  
2714 C C   . PRO A 365 ? 1.0228 0.8963 0.8506 -0.0415 -0.0034 0.0838  354 PRO A C   
2715 O O   . PRO A 365 ? 1.0214 0.8965 0.8583 -0.0390 -0.0063 0.0767  354 PRO A O   
2716 C CB  . PRO A 365 ? 1.0370 0.9043 0.8176 -0.0482 -0.0052 0.0851  354 PRO A CB  
2717 C CG  . PRO A 365 ? 1.0412 0.9078 0.8166 -0.0475 -0.0077 0.0745  354 PRO A CG  
2718 C CD  . PRO A 365 ? 1.0173 0.8850 0.7998 -0.0446 0.0033  0.0650  354 PRO A CD  
2719 N N   . LYS A 366 ? 1.0216 0.8951 0.8596 -0.0417 -0.0049 0.0934  355 LYS A N   
2720 C CA  . LYS A 366 ? 1.0267 0.9012 0.8870 -0.0388 -0.0097 0.0956  355 LYS A CA  
2721 C C   . LYS A 366 ? 1.0396 0.9152 0.8998 -0.0384 -0.0201 0.0969  355 LYS A C   
2722 O O   . LYS A 366 ? 1.0476 0.9225 0.8900 -0.0416 -0.0254 0.0997  355 LYS A O   
2723 C CB  . LYS A 366 ? 1.0464 0.9196 0.9167 -0.0394 -0.0089 0.1062  355 LYS A CB  
2724 C CG  . LYS A 366 ? 1.0988 0.9715 0.9725 -0.0400 0.0011  0.1053  355 LYS A CG  
2725 C CD  . LYS A 366 ? 1.1601 1.0309 1.0424 -0.0413 0.0018  0.1168  355 LYS A CD  
2726 C CE  . LYS A 366 ? 1.2134 1.0842 1.1013 -0.0424 0.0114  0.1166  355 LYS A CE  
2727 N NZ  . LYS A 366 ? 1.2461 1.1146 1.1421 -0.0441 0.0122  0.1286  355 LYS A NZ  
2728 N N   . ARG A 367 ? 1.0393 0.9161 0.9188 -0.0349 -0.0227 0.0944  356 ARG A N   
2729 C CA  . ARG A 367 ? 1.0465 0.9253 0.9306 -0.0341 -0.0314 0.0956  356 ARG A CA  
2730 C C   . ARG A 367 ? 1.0667 0.9459 0.9505 -0.0361 -0.0403 0.1084  356 ARG A C   
2731 O O   . ARG A 367 ? 1.0643 0.9424 0.9596 -0.0354 -0.0402 0.1169  356 ARG A O   
2732 C CB  . ARG A 367 ? 1.0393 0.9188 0.9445 -0.0296 -0.0302 0.0907  356 ARG A CB  
2733 C CG  . ARG A 367 ? 1.0457 0.9280 0.9537 -0.0286 -0.0359 0.0875  356 ARG A CG  
2734 C CD  . ARG A 367 ? 1.0446 0.9270 0.9720 -0.0242 -0.0332 0.0830  356 ARG A CD  
2735 N NE  . ARG A 367 ? 1.0360 0.9176 0.9609 -0.0230 -0.0271 0.0719  356 ARG A NE  
2736 C CZ  . ARG A 367 ? 1.0321 0.9107 0.9621 -0.0216 -0.0205 0.0678  356 ARG A CZ  
2737 N NH1 . ARG A 367 ? 1.0294 0.9052 0.9674 -0.0213 -0.0185 0.0732  356 ARG A NH1 
2738 N NH2 . ARG A 367 ? 1.0101 0.8884 0.9380 -0.0209 -0.0165 0.0587  356 ARG A NH2 
2739 N N   . GLU A 368 ? 1.0831 0.9634 0.9542 -0.0390 -0.0487 0.1100  357 GLU A N   
2740 C CA  . GLU A 368 ? 1.1025 0.9836 0.9718 -0.0418 -0.0592 0.1225  357 GLU A CA  
2741 C C   . GLU A 368 ? 1.1016 0.9863 0.9971 -0.0384 -0.0654 0.1274  357 GLU A C   
2742 O O   . GLU A 368 ? 1.0994 0.9863 1.0063 -0.0353 -0.0640 0.1198  357 GLU A O   
2743 C CB  . GLU A 368 ? 1.1546 1.0346 0.9983 -0.0471 -0.0665 0.1217  357 GLU A CB  
2744 C CG  . GLU A 368 ? 1.2450 1.1237 1.0768 -0.0519 -0.0762 0.1352  357 GLU A CG  
2745 C CD  . GLU A 368 ? 1.3606 1.2373 1.1676 -0.0577 -0.0860 0.1347  357 GLU A CD  
2746 O OE1 . GLU A 368 ? 1.3769 1.2522 1.1733 -0.0583 -0.0837 0.1230  357 GLU A OE1 
2747 O OE2 . GLU A 368 ? 1.4023 1.2782 1.2001 -0.0621 -0.0964 0.1464  357 GLU A OE2 
2748 N N   . PHE A 369 ? 1.1006 0.9860 1.0062 -0.0388 -0.0718 0.1407  358 PHE A N   
2749 C CA  . PHE A 369 ? 1.0977 0.9866 1.0312 -0.0351 -0.0767 0.1470  358 PHE A CA  
2750 C C   . PHE A 369 ? 1.1132 1.0068 1.0485 -0.0371 -0.0885 0.1498  358 PHE A C   
2751 O O   . PHE A 369 ? 1.1255 1.0187 1.0382 -0.0419 -0.0937 0.1466  358 PHE A O   
2752 C CB  . PHE A 369 ? 1.0847 0.9722 1.0310 -0.0345 -0.0787 0.1607  358 PHE A CB  
2753 C CG  . PHE A 369 ? 1.0863 0.9690 1.0342 -0.0327 -0.0675 0.1579  358 PHE A CG  
2754 C CD1 . PHE A 369 ? 1.0891 0.9699 1.0533 -0.0278 -0.0582 0.1489  358 PHE A CD1 
2755 C CD2 . PHE A 369 ? 1.0987 0.9784 1.0304 -0.0364 -0.0662 0.1639  358 PHE A CD2 
2756 C CE1 . PHE A 369 ? 1.0952 0.9712 1.0611 -0.0269 -0.0492 0.1462  358 PHE A CE1 
2757 C CE2 . PHE A 369 ? 1.1051 0.9808 1.0400 -0.0352 -0.0561 0.1615  358 PHE A CE2 
2758 C CZ  . PHE A 369 ? 1.0960 0.9699 1.0487 -0.0306 -0.0483 0.1527  358 PHE A CZ  
2759 N N   . LEU A 370 ? 1.1095 1.0073 1.0731 -0.0333 -0.0919 0.1550  359 LEU A N   
2760 C CA  . LEU A 370 ? 1.1158 1.0194 1.0896 -0.0344 -0.1028 0.1592  359 LEU A CA  
2761 C C   . LEU A 370 ? 1.1248 1.0321 1.1219 -0.0336 -0.1119 0.1758  359 LEU A C   
2762 O O   . LEU A 370 ? 1.1218 1.0265 1.1291 -0.0311 -0.1080 0.1825  359 LEU A O   
2763 C CB  . LEU A 370 ? 1.1060 1.0122 1.0971 -0.0296 -0.0962 0.1494  359 LEU A CB  
2764 C CG  . LEU A 370 ? 1.1224 1.0253 1.0989 -0.0287 -0.0859 0.1339  359 LEU A CG  
2765 C CD1 . LEU A 370 ? 1.1200 1.0253 1.1155 -0.0239 -0.0802 0.1272  359 LEU A CD1 
2766 C CD2 . LEU A 370 ? 1.1395 1.0412 1.0881 -0.0344 -0.0909 0.1285  359 LEU A CD2 
2767 N N   . THR A 371 ? 1.1324 1.0458 1.1401 -0.0357 -0.1243 0.1828  360 THR A N   
2768 C CA  . THR A 371 ? 1.1411 1.0592 1.1746 -0.0348 -0.1339 0.1994  360 THR A CA  
2769 C C   . THR A 371 ? 1.1402 1.0657 1.2048 -0.0311 -0.1361 0.2004  360 THR A C   
2770 O O   . THR A 371 ? 1.1408 1.0698 1.1994 -0.0344 -0.1421 0.1959  360 THR A O   
2771 C CB  . THR A 371 ? 1.1676 1.0857 1.1817 -0.0426 -0.1496 0.2119  360 THR A CB  
2772 O OG1 . THR A 371 ? 1.1847 1.0982 1.1949 -0.0422 -0.1465 0.2197  360 THR A OG1 
2773 C CG2 . THR A 371 ? 1.1632 1.0890 1.1989 -0.0447 -0.1660 0.2262  360 THR A CG2 
2774 N N   . GLU A 372 ? 1.1356 1.0629 1.2339 -0.0242 -0.1300 0.2060  361 GLU A N   
2775 C CA  . GLU A 372 ? 1.1362 1.0704 1.2669 -0.0198 -0.1293 0.2075  361 GLU A CA  
2776 C C   . GLU A 372 ? 1.1289 1.0695 1.2915 -0.0186 -0.1396 0.2259  361 GLU A C   
2777 O O   . GLU A 372 ? 1.1221 1.0710 1.3046 -0.0193 -0.1483 0.2321  361 GLU A O   
2778 C CB  . GLU A 372 ? 1.1668 1.0973 1.3114 -0.0119 -0.1108 0.1961  361 GLU A CB  
2779 C CG  . GLU A 372 ? 1.2215 1.1581 1.3921 -0.0078 -0.1072 0.1940  361 GLU A CG  
2780 C CD  . GLU A 372 ? 1.3047 1.2423 1.4583 -0.0101 -0.1051 0.1810  361 GLU A CD  
2781 O OE1 . GLU A 372 ? 1.3302 1.2632 1.4511 -0.0146 -0.1057 0.1724  361 GLU A OE1 
2782 O OE2 . GLU A 372 ? 1.3213 1.2642 1.4954 -0.0073 -0.1023 0.1799  361 GLU A OE2 
2783 N N   . ALA B 30  ? 0.8385 0.6527 0.7404 0.0308  0.0112  -0.0294 0   ALA B N   
2784 C CA  . ALA B 30  ? 0.8417 0.6692 0.7479 0.0288  0.0154  -0.0304 0   ALA B CA  
2785 C C   . ALA B 30  ? 0.8319 0.6856 0.7566 0.0242  0.0235  -0.0308 0   ALA B C   
2786 O O   . ALA B 30  ? 0.8288 0.6852 0.7667 0.0148  0.0255  -0.0268 0   ALA B O   
2787 C CB  . ALA B 30  ? 0.8461 0.6606 0.7521 0.0198  0.0126  -0.0257 0   ALA B CB  
2788 N N   . MET B 31  ? 0.8260 0.6990 0.7509 0.0308  0.0279  -0.0358 1   MET B N   
2789 C CA  . MET B 31  ? 0.8192 0.7188 0.7597 0.0276  0.0355  -0.0378 1   MET B CA  
2790 C C   . MET B 31  ? 0.8192 0.7231 0.7671 0.0279  0.0353  -0.0387 1   MET B C   
2791 O O   . MET B 31  ? 0.8223 0.7282 0.7831 0.0185  0.0374  -0.0353 1   MET B O   
2792 C CB  . MET B 31  ? 0.8205 0.7257 0.7736 0.0150  0.0405  -0.0333 1   MET B CB  
2793 C CG  . MET B 31  ? 0.8453 0.7412 0.7900 0.0139  0.0397  -0.0308 1   MET B CG  
2794 S SD  . MET B 31  ? 0.8895 0.7933 0.8197 0.0264  0.0401  -0.0362 1   MET B SD  
2795 C CE  . MET B 31  ? 0.8622 0.7995 0.8068 0.0248  0.0494  -0.0397 1   MET B CE  
2796 N N   . ALA B 32  ? 0.8173 0.7195 0.7551 0.0395  0.0321  -0.0427 2   ALA B N   
2797 C CA  . ALA B 32  ? 0.8194 0.7234 0.7616 0.0413  0.0313  -0.0432 2   ALA B CA  
2798 C C   . ALA B 32  ? 0.8032 0.7366 0.7574 0.0439  0.0366  -0.0488 2   ALA B C   
2799 O O   . ALA B 32  ? 0.8054 0.7480 0.7741 0.0361  0.0395  -0.0476 2   ALA B O   
2800 C CB  . ALA B 32  ? 0.8409 0.7240 0.7649 0.0519  0.0247  -0.0437 2   ALA B CB  
2801 N N   . GLY B 33  ? 0.7844 0.7333 0.7327 0.0544  0.0378  -0.0548 3   GLY B N   
2802 C CA  . GLY B 33  ? 0.7607 0.7402 0.7208 0.0565  0.0425  -0.0606 3   GLY B CA  
2803 C C   . GLY B 33  ? 0.7388 0.7396 0.7116 0.0477  0.0491  -0.0615 3   GLY B C   
2804 O O   . GLY B 33  ? 0.7313 0.7596 0.7112 0.0505  0.0531  -0.0671 3   GLY B O   
2805 N N   . ASN B 34  ? 0.7269 0.7158 0.7025 0.0367  0.0506  -0.0559 4   ASN B N   
2806 C CA  . ASN B 34  ? 0.7081 0.7131 0.6935 0.0279  0.0571  -0.0555 4   ASN B CA  
2807 C C   . ASN B 34  ? 0.6876 0.7015 0.6911 0.0140  0.0617  -0.0539 4   ASN B C   
2808 O O   . ASN B 34  ? 0.6861 0.7060 0.6965 0.0045  0.0669  -0.0517 4   ASN B O   
2809 C CB  . ASN B 34  ? 0.7275 0.7142 0.7036 0.0252  0.0561  -0.0504 4   ASN B CB  
2810 C CG  . ASN B 34  ? 0.7626 0.7659 0.7416 0.0220  0.0622  -0.0507 4   ASN B CG  
2811 O OD1 . ASN B 34  ? 0.7738 0.7997 0.7530 0.0283  0.0653  -0.0558 4   ASN B OD1 
2812 N ND2 . ASN B 34  ? 0.7738 0.7671 0.7548 0.0123  0.0645  -0.0451 4   ASN B ND2 
2813 N N   . PHE B 35  ? 0.6697 0.6839 0.6800 0.0132  0.0601  -0.0550 5   PHE B N   
2814 C CA  . PHE B 35  ? 0.6583 0.6777 0.6840 0.0008  0.0637  -0.0537 5   PHE B CA  
2815 C C   . PHE B 35  ? 0.6474 0.6910 0.6852 -0.0072 0.0706  -0.0570 5   PHE B C   
2816 O O   . PHE B 35  ? 0.6564 0.6950 0.7002 -0.0188 0.0744  -0.0530 5   PHE B O   
2817 C CB  . PHE B 35  ? 0.6497 0.6692 0.6806 0.0025  0.0610  -0.0554 5   PHE B CB  
2818 C CG  . PHE B 35  ? 0.6446 0.6648 0.6889 -0.0100 0.0641  -0.0535 5   PHE B CG  
2819 C CD1 . PHE B 35  ? 0.6552 0.6551 0.6991 -0.0175 0.0636  -0.0465 5   PHE B CD1 
2820 C CD2 . PHE B 35  ? 0.6392 0.6807 0.6962 -0.0141 0.0674  -0.0592 5   PHE B CD2 
2821 C CE1 . PHE B 35  ? 0.6573 0.6566 0.7117 -0.0275 0.0663  -0.0450 5   PHE B CE1 
2822 C CE2 . PHE B 35  ? 0.6414 0.6810 0.7089 -0.0252 0.0698  -0.0579 5   PHE B CE2 
2823 C CZ  . PHE B 35  ? 0.6450 0.6629 0.7106 -0.0314 0.0693  -0.0507 5   PHE B CZ  
2824 N N   . TRP B 36  ? 0.6260 0.6951 0.6667 -0.0015 0.0725  -0.0639 6   TRP B N   
2825 C CA  . TRP B 36  ? 0.6071 0.7015 0.6607 -0.0106 0.0792  -0.0672 6   TRP B CA  
2826 C C   . TRP B 36  ? 0.5905 0.6862 0.6416 -0.0161 0.0842  -0.0636 6   TRP B C   
2827 O O   . TRP B 36  ? 0.5841 0.6971 0.6457 -0.0263 0.0905  -0.0646 6   TRP B O   
2828 C CB  . TRP B 36  ? 0.5980 0.7227 0.6566 -0.0030 0.0796  -0.0759 6   TRP B CB  
2829 C CG  . TRP B 36  ? 0.6075 0.7308 0.6669 0.0038  0.0747  -0.0793 6   TRP B CG  
2830 C CD1 . TRP B 36  ? 0.6247 0.7459 0.6729 0.0194  0.0695  -0.0819 6   TRP B CD1 
2831 C CD2 . TRP B 36  ? 0.6060 0.7265 0.6760 -0.0043 0.0743  -0.0796 6   TRP B CD2 
2832 N NE1 . TRP B 36  ? 0.6280 0.7471 0.6798 0.0214  0.0664  -0.0837 6   TRP B NE1 
2833 C CE2 . TRP B 36  ? 0.6178 0.7371 0.6832 0.0072  0.0692  -0.0826 6   TRP B CE2 
2834 C CE3 . TRP B 36  ? 0.6099 0.7281 0.6917 -0.0195 0.0778  -0.0779 6   TRP B CE3 
2835 C CZ2 . TRP B 36  ? 0.6217 0.7401 0.6948 0.0041  0.0676  -0.0840 6   TRP B CZ2 
2836 C CZ3 . TRP B 36  ? 0.6168 0.7326 0.7056 -0.0222 0.0759  -0.0797 6   TRP B CZ3 
2837 C CH2 . TRP B 36  ? 0.6182 0.7353 0.7031 -0.0105 0.0709  -0.0827 6   TRP B CH2 
2838 N N   A GLN B 37  ? 0.5908 0.6679 0.6278 -0.0097 0.0815  -0.0592 7   GLN B N   
2839 N N   B GLN B 37  ? 0.5895 0.6666 0.6265 -0.0097 0.0814  -0.0592 7   GLN B N   
2840 C CA  A GLN B 37  ? 0.5888 0.6649 0.6216 -0.0137 0.0858  -0.0553 7   GLN B CA  
2841 C CA  B GLN B 37  ? 0.5863 0.6620 0.6187 -0.0134 0.0856  -0.0553 7   GLN B CA  
2842 C C   A GLN B 37  ? 0.5904 0.6365 0.6167 -0.0188 0.0838  -0.0474 7   GLN B C   
2843 C C   B GLN B 37  ? 0.5893 0.6352 0.6155 -0.0188 0.0838  -0.0474 7   GLN B C   
2844 O O   A GLN B 37  ? 0.5963 0.6367 0.6152 -0.0191 0.0857  -0.0436 7   GLN B O   
2845 O O   B GLN B 37  ? 0.5952 0.6354 0.6141 -0.0192 0.0857  -0.0436 7   GLN B O   
2846 C CB  A GLN B 37  ? 0.6116 0.6974 0.6321 0.0000  0.0847  -0.0583 7   GLN B CB  
2847 C CB  B GLN B 37  ? 0.6054 0.6890 0.6249 0.0007  0.0840  -0.0581 7   GLN B CB  
2848 C CG  A GLN B 37  ? 0.6422 0.7579 0.6670 0.0083  0.0854  -0.0664 7   GLN B CG  
2849 C CG  B GLN B 37  ? 0.6263 0.7406 0.6502 0.0085  0.0853  -0.0661 7   GLN B CG  
2850 C CD  A GLN B 37  ? 0.6834 0.8302 0.7174 0.0028  0.0933  -0.0687 7   GLN B CD  
2851 C CD  B GLN B 37  ? 0.6751 0.7833 0.6848 0.0261  0.0783  -0.0697 7   GLN B CD  
2852 O OE1 A GLN B 37  ? 0.6816 0.8413 0.7307 -0.0111 0.0986  -0.0688 7   GLN B OE1 
2853 O OE1 B GLN B 37  ? 0.6916 0.7851 0.6989 0.0298  0.0730  -0.0701 7   GLN B OE1 
2854 N NE2 A GLN B 37  ? 0.6986 0.8585 0.7232 0.0138  0.0941  -0.0708 7   GLN B NE2 
2855 N NE2 B GLN B 37  ? 0.6823 0.8008 0.6811 0.0378  0.0785  -0.0724 7   GLN B NE2 
2856 N N   . SER B 38  ? 0.5825 0.6110 0.6113 -0.0220 0.0799  -0.0449 8   SER B N   
2857 C CA  . SER B 38  ? 0.5728 0.5750 0.5964 -0.0261 0.0773  -0.0379 8   SER B CA  
2858 C C   . SER B 38  ? 0.5641 0.5622 0.5959 -0.0392 0.0824  -0.0335 8   SER B C   
2859 O O   . SER B 38  ? 0.5612 0.5730 0.6045 -0.0466 0.0868  -0.0361 8   SER B O   
2860 C CB  . SER B 38  ? 0.5706 0.5579 0.5927 -0.0224 0.0708  -0.0373 8   SER B CB  
2861 O OG  . SER B 38  ? 0.5631 0.5594 0.5972 -0.0270 0.0721  -0.0399 8   SER B OG  
2862 N N   . SER B 39  ? 0.5609 0.5392 0.5864 -0.0420 0.0813  -0.0270 9   SER B N   
2863 C CA  . SER B 39  ? 0.5586 0.5292 0.5895 -0.0531 0.0856  -0.0222 9   SER B CA  
2864 C C   . SER B 39  ? 0.5591 0.5263 0.5993 -0.0575 0.0841  -0.0230 9   SER B C   
2865 O O   . SER B 39  ? 0.5620 0.5311 0.6098 -0.0666 0.0887  -0.0226 9   SER B O   
2866 C CB  . SER B 39  ? 0.5752 0.5257 0.5963 -0.0530 0.0837  -0.0154 9   SER B CB  
2867 O OG  . SER B 39  ? 0.6023 0.5366 0.6218 -0.0513 0.0776  -0.0127 9   SER B OG  
2868 N N   . HIS B 40  ? 0.5564 0.5181 0.5952 -0.0509 0.0778  -0.0242 10  HIS B N   
2869 C CA  . HIS B 40  ? 0.5525 0.5123 0.5987 -0.0525 0.0758  -0.0253 10  HIS B CA  
2870 C C   . HIS B 40  ? 0.5606 0.5397 0.6179 -0.0569 0.0799  -0.0314 10  HIS B C   
2871 O O   . HIS B 40  ? 0.5659 0.5429 0.6304 -0.0645 0.0822  -0.0310 10  HIS B O   
2872 C CB  . HIS B 40  ? 0.5430 0.4978 0.5842 -0.0431 0.0690  -0.0262 10  HIS B CB  
2873 C CG  . HIS B 40  ? 0.5272 0.4791 0.5743 -0.0434 0.0665  -0.0262 10  HIS B CG  
2874 N ND1 . HIS B 40  ? 0.5412 0.4805 0.5832 -0.0386 0.0608  -0.0230 10  HIS B ND1 
2875 C CD2 . HIS B 40  ? 0.5260 0.4863 0.5832 -0.0479 0.0688  -0.0291 10  HIS B CD2 
2876 C CE1 . HIS B 40  ? 0.5396 0.4809 0.5886 -0.0397 0.0604  -0.0236 10  HIS B CE1 
2877 N NE2 . HIS B 40  ? 0.5347 0.4882 0.5927 -0.0448 0.0648  -0.0276 10  HIS B NE2 
2878 N N   . TYR B 41  ? 0.5603 0.5582 0.6186 -0.0522 0.0809  -0.0372 11  TYR B N   
2879 C CA  . TYR B 41  ? 0.5655 0.5849 0.6350 -0.0563 0.0843  -0.0438 11  TYR B CA  
2880 C C   . TYR B 41  ? 0.5727 0.5991 0.6480 -0.0681 0.0915  -0.0432 11  TYR B C   
2881 O O   . TYR B 41  ? 0.5706 0.6016 0.6553 -0.0768 0.0941  -0.0456 11  TYR B O   
2882 C CB  . TYR B 41  ? 0.5673 0.6065 0.6354 -0.0464 0.0829  -0.0502 11  TYR B CB  
2883 C CG  . TYR B 41  ? 0.5747 0.6405 0.6548 -0.0501 0.0862  -0.0577 11  TYR B CG  
2884 C CD1 . TYR B 41  ? 0.5872 0.6566 0.6762 -0.0534 0.0850  -0.0613 11  TYR B CD1 
2885 C CD2 . TYR B 41  ? 0.5810 0.6695 0.6633 -0.0501 0.0904  -0.0615 11  TYR B CD2 
2886 C CE1 . TYR B 41  ? 0.5892 0.6836 0.6895 -0.0573 0.0876  -0.0689 11  TYR B CE1 
2887 C CE2 . TYR B 41  ? 0.5818 0.6972 0.6761 -0.0544 0.0933  -0.0688 11  TYR B CE2 
2888 C CZ  . TYR B 41  ? 0.5945 0.7125 0.6979 -0.0583 0.0916  -0.0727 11  TYR B CZ  
2889 O OH  . TYR B 41  ? 0.6099 0.7550 0.7252 -0.0627 0.0939  -0.0805 11  TYR B OH  
2890 N N   . LEU B 42  ? 0.5792 0.6060 0.6483 -0.0684 0.0947  -0.0401 12  LEU B N   
2891 C CA  . LEU B 42  ? 0.5839 0.6183 0.6575 -0.0795 0.1022  -0.0389 12  LEU B CA  
2892 C C   . LEU B 42  ? 0.5959 0.6098 0.6693 -0.0898 0.1048  -0.0330 12  LEU B C   
2893 O O   . LEU B 42  ? 0.6028 0.6217 0.6820 -0.1011 0.1109  -0.0331 12  LEU B O   
2894 C CB  . LEU B 42  ? 0.5895 0.6313 0.6554 -0.0757 0.1052  -0.0370 12  LEU B CB  
2895 C CG  . LEU B 42  ? 0.6051 0.6666 0.6686 -0.0638 0.1027  -0.0428 12  LEU B CG  
2896 C CD1 . LEU B 42  ? 0.6165 0.6802 0.6694 -0.0582 0.1047  -0.0402 12  LEU B CD1 
2897 C CD2 . LEU B 42  ? 0.5943 0.6846 0.6703 -0.0669 0.1055  -0.0506 12  LEU B CD2 
2898 N N   . GLN B 43  ? 0.5966 0.5878 0.6633 -0.0862 0.1004  -0.0279 13  GLN B N   
2899 C CA  . GLN B 43  ? 0.6025 0.5740 0.6674 -0.0939 0.1026  -0.0221 13  GLN B CA  
2900 C C   . GLN B 43  ? 0.6013 0.5591 0.6680 -0.0928 0.0980  -0.0214 13  GLN B C   
2901 O O   . GLN B 43  ? 0.6057 0.5516 0.6734 -0.0999 0.1003  -0.0190 13  GLN B O   
2902 C CB  . GLN B 43  ? 0.6310 0.5876 0.6842 -0.0915 0.1030  -0.0148 13  GLN B CB  
2903 C CG  . GLN B 43  ? 0.6793 0.6481 0.7288 -0.0914 0.1077  -0.0145 13  GLN B CG  
2904 C CD  . GLN B 43  ? 0.7499 0.7043 0.7869 -0.0871 0.1071  -0.0079 13  GLN B CD  
2905 O OE1 . GLN B 43  ? 0.7651 0.7273 0.7959 -0.0808 0.1069  -0.0083 13  GLN B OE1 
2906 N NE2 . GLN B 43  ? 0.7575 0.6911 0.7898 -0.0896 0.1064  -0.0020 13  GLN B NE2 
2907 N N   . TRP B 44  ? 0.5914 0.5498 0.6574 -0.0837 0.0917  -0.0230 14  TRP B N   
2908 C CA  . TRP B 44  ? 0.5897 0.5359 0.6568 -0.0820 0.0875  -0.0214 14  TRP B CA  
2909 C C   . TRP B 44  ? 0.5915 0.5486 0.6667 -0.0798 0.0850  -0.0276 14  TRP B C   
2910 O O   . TRP B 44  ? 0.5960 0.5463 0.6706 -0.0746 0.0804  -0.0263 14  TRP B O   
2911 C CB  . TRP B 44  ? 0.5874 0.5208 0.6461 -0.0746 0.0823  -0.0161 14  TRP B CB  
2912 C CG  . TRP B 44  ? 0.5859 0.5053 0.6368 -0.0771 0.0841  -0.0095 14  TRP B CG  
2913 C CD1 . TRP B 44  ? 0.5941 0.5125 0.6373 -0.0748 0.0847  -0.0072 14  TRP B CD1 
2914 C CD2 . TRP B 44  ? 0.5823 0.4872 0.6317 -0.0819 0.0860  -0.0047 14  TRP B CD2 
2915 N NE1 . TRP B 44  ? 0.6005 0.5050 0.6376 -0.0778 0.0866  -0.0010 14  TRP B NE1 
2916 C CE2 . TRP B 44  ? 0.5974 0.4931 0.6379 -0.0820 0.0875  0.0008  14  TRP B CE2 
2917 C CE3 . TRP B 44  ? 0.5819 0.4804 0.6355 -0.0854 0.0864  -0.0046 14  TRP B CE3 
2918 C CZ2 . TRP B 44  ? 0.6076 0.4880 0.6431 -0.0848 0.0892  0.0065  14  TRP B CZ2 
2919 C CZ3 . TRP B 44  ? 0.5984 0.4811 0.6467 -0.0882 0.0882  0.0008  14  TRP B CZ3 
2920 C CH2 . TRP B 44  ? 0.6078 0.4817 0.6471 -0.0877 0.0896  0.0064  14  TRP B CH2 
2921 N N   . ILE B 45  ? 0.5878 0.5624 0.6709 -0.0841 0.0882  -0.0342 15  ILE B N   
2922 C CA  . ILE B 45  ? 0.5923 0.5787 0.6838 -0.0835 0.0865  -0.0410 15  ILE B CA  
2923 C C   . ILE B 45  ? 0.6072 0.5916 0.7041 -0.0956 0.0913  -0.0424 15  ILE B C   
2924 O O   . ILE B 45  ? 0.6063 0.6026 0.7072 -0.1031 0.0961  -0.0452 15  ILE B O   
2925 C CB  . ILE B 45  ? 0.5859 0.5960 0.6814 -0.0780 0.0857  -0.0482 15  ILE B CB  
2926 C CG1 . ILE B 45  ? 0.5996 0.6072 0.6868 -0.0658 0.0809  -0.0462 15  ILE B CG1 
2927 C CG2 . ILE B 45  ? 0.5815 0.6051 0.6862 -0.0786 0.0845  -0.0557 15  ILE B CG2 
2928 C CD1 . ILE B 45  ? 0.6183 0.6139 0.7029 -0.0594 0.0756  -0.0438 15  ILE B CD1 
2929 N N   . LEU B 46  ? 0.6157 0.5828 0.7110 -0.0976 0.0902  -0.0394 16  LEU B N   
2930 C CA  . LEU B 46  ? 0.6237 0.5812 0.7204 -0.1083 0.0942  -0.0394 16  LEU B CA  
2931 C C   . LEU B 46  ? 0.6389 0.6068 0.7447 -0.1131 0.0940  -0.0477 16  LEU B C   
2932 O O   . LEU B 46  ? 0.6314 0.6113 0.7418 -0.1063 0.0899  -0.0528 16  LEU B O   
2933 C CB  . LEU B 46  ? 0.6234 0.5562 0.7122 -0.1069 0.0930  -0.0321 16  LEU B CB  
2934 C CG  . LEU B 46  ? 0.6287 0.5508 0.7086 -0.1008 0.0915  -0.0241 16  LEU B CG  
2935 C CD1 . LEU B 46  ? 0.6387 0.5395 0.7119 -0.0998 0.0905  -0.0179 16  LEU B CD1 
2936 C CD2 . LEU B 46  ? 0.6323 0.5572 0.7086 -0.1047 0.0959  -0.0217 16  LEU B CD2 
2937 N N   . ASP B 47  ? 0.6581 0.6204 0.7657 -0.1250 0.0983  -0.0492 17  ASP B N   
2938 C CA  . ASP B 47  ? 0.6742 0.6432 0.7895 -0.1318 0.0981  -0.0573 17  ASP B CA  
2939 C C   . ASP B 47  ? 0.6891 0.6376 0.7997 -0.1285 0.0948  -0.0559 17  ASP B C   
2940 O O   . ASP B 47  ? 0.6965 0.6225 0.7983 -0.1294 0.0961  -0.0489 17  ASP B O   
2941 C CB  . ASP B 47  ? 0.7087 0.6778 0.8265 -0.1472 0.1044  -0.0587 17  ASP B CB  
2942 C CG  . ASP B 47  ? 0.7826 0.7587 0.9087 -0.1566 0.1044  -0.0677 17  ASP B CG  
2943 O OD1 . ASP B 47  ? 0.7994 0.7588 0.9224 -0.1564 0.1017  -0.0690 17  ASP B OD1 
2944 O OD2 . ASP B 47  ? 0.8133 0.8118 0.9485 -0.1645 0.1071  -0.0736 17  ASP B OD2 
2945 N N   . LYS B 48  ? 0.6927 0.6495 0.8084 -0.1238 0.0904  -0.0625 18  LYS B N   
2946 C CA  . LYS B 48  ? 0.7151 0.6551 0.8262 -0.1190 0.0871  -0.0614 18  LYS B CA  
2947 C C   . LYS B 48  ? 0.7463 0.6640 0.8520 -0.1287 0.0899  -0.0606 18  LYS B C   
2948 O O   . LYS B 48  ? 0.7637 0.6606 0.8605 -0.1244 0.0891  -0.0544 18  LYS B O   
2949 C CB  . LYS B 48  ? 0.7201 0.6744 0.8374 -0.1124 0.0823  -0.0692 18  LYS B CB  
2950 C CG  . LYS B 48  ? 0.7691 0.7094 0.8807 -0.1029 0.0783  -0.0662 18  LYS B CG  
2951 C CD  . LYS B 48  ? 0.8200 0.7704 0.9366 -0.0995 0.0745  -0.0750 18  LYS B CD  
2952 C CE  . LYS B 48  ? 0.8695 0.8045 0.9798 -0.0921 0.0715  -0.0727 18  LYS B CE  
2953 N NZ  . LYS B 48  ? 0.8915 0.8328 1.0006 -0.0788 0.0680  -0.0684 18  LYS B NZ  
2954 N N   . GLN B 49  ? 0.7490 0.6705 0.8593 -0.1418 0.0934  -0.0661 19  GLN B N   
2955 C CA  . GLN B 49  ? 0.7689 0.6664 0.8724 -0.1518 0.0963  -0.0651 19  GLN B CA  
2956 C C   . GLN B 49  ? 0.7768 0.6545 0.8697 -0.1536 0.1006  -0.0546 19  GLN B C   
2957 O O   . GLN B 49  ? 0.7912 0.6432 0.8736 -0.1532 0.1009  -0.0503 19  GLN B O   
2958 C CB  . GLN B 49  ? 0.7905 0.6966 0.9017 -0.1669 0.0988  -0.0738 19  GLN B CB  
2959 C CG  . GLN B 49  ? 0.8392 0.7595 0.9584 -0.1648 0.0937  -0.0848 19  GLN B CG  
2960 C CD  . GLN B 49  ? 0.9246 0.8270 1.0363 -0.1547 0.0887  -0.0848 19  GLN B CD  
2961 O OE1 . GLN B 49  ? 0.9469 0.8606 1.0610 -0.1420 0.0840  -0.0863 19  GLN B OE1 
2962 N NE2 . GLN B 49  ? 0.9444 0.8178 1.0456 -0.1594 0.0899  -0.0824 19  GLN B NE2 
2963 N N   . ASP B 50  ? 0.7651 0.6548 0.8598 -0.1535 0.1035  -0.0503 20  ASP B N   
2964 C CA  . ASP B 50  ? 0.7733 0.6468 0.8577 -0.1535 0.1072  -0.0404 20  ASP B CA  
2965 C C   . ASP B 50  ? 0.7663 0.6250 0.8422 -0.1404 0.1030  -0.0340 20  ASP B C   
2966 O O   . ASP B 50  ? 0.7774 0.6135 0.8423 -0.1401 0.1046  -0.0273 20  ASP B O   
2967 C CB  . ASP B 50  ? 0.8016 0.6940 0.8898 -0.1536 0.1099  -0.0382 20  ASP B CB  
2968 C CG  . ASP B 50  ? 0.8842 0.7889 0.9783 -0.1674 0.1160  -0.0414 20  ASP B CG  
2969 O OD1 . ASP B 50  ? 0.9081 0.8049 1.0033 -0.1790 0.1183  -0.0451 20  ASP B OD1 
2970 O OD2 . ASP B 50  ? 0.9097 0.8322 1.0070 -0.1668 0.1183  -0.0403 20  ASP B OD2 
2971 N N   . LEU B 51  ? 0.7469 0.6192 0.8277 -0.1298 0.0977  -0.0360 21  LEU B N   
2972 C CA  . LEU B 51  ? 0.7459 0.6096 0.8210 -0.1177 0.0933  -0.0304 21  LEU B CA  
2973 C C   . LEU B 51  ? 0.7515 0.5959 0.8202 -0.1155 0.0916  -0.0302 21  LEU B C   
2974 O O   . LEU B 51  ? 0.7601 0.5883 0.8195 -0.1102 0.0912  -0.0232 21  LEU B O   
2975 C CB  . LEU B 51  ? 0.7319 0.6156 0.8145 -0.1087 0.0886  -0.0335 21  LEU B CB  
2976 C CG  . LEU B 51  ? 0.7465 0.6257 0.8248 -0.0975 0.0843  -0.0275 21  LEU B CG  
2977 C CD1 . LEU B 51  ? 0.7573 0.6304 0.8294 -0.0961 0.0855  -0.0196 21  LEU B CD1 
2978 C CD2 . LEU B 51  ? 0.7453 0.6425 0.8303 -0.0900 0.0802  -0.0309 21  LEU B CD2 
2979 N N   . LEU B 52  ? 0.7448 0.5913 0.8179 -0.1191 0.0905  -0.0383 22  LEU B N   
2980 C CA  . LEU B 52  ? 0.7523 0.5805 0.8186 -0.1165 0.0886  -0.0396 22  LEU B CA  
2981 C C   . LEU B 52  ? 0.7576 0.5596 0.8125 -0.1236 0.0927  -0.0357 22  LEU B C   
2982 O O   . LEU B 52  ? 0.7692 0.5517 0.8137 -0.1174 0.0914  -0.0321 22  LEU B O   
2983 C CB  . LEU B 52  ? 0.7503 0.5873 0.8237 -0.1194 0.0862  -0.0503 22  LEU B CB  
2984 C CG  . LEU B 52  ? 0.7571 0.6205 0.8415 -0.1129 0.0824  -0.0555 22  LEU B CG  
2985 C CD1 . LEU B 52  ? 0.7591 0.6294 0.8490 -0.1159 0.0801  -0.0661 22  LEU B CD1 
2986 C CD2 . LEU B 52  ? 0.7665 0.6325 0.8487 -0.0988 0.0785  -0.0499 22  LEU B CD2 
2987 N N   . LYS B 53  ? 0.7487 0.5505 0.8049 -0.1362 0.0979  -0.0362 23  LYS B N   
2988 C CA  . LYS B 53  ? 0.7629 0.5398 0.8079 -0.1446 0.1028  -0.0319 23  LYS B CA  
2989 C C   . LYS B 53  ? 0.7727 0.5356 0.8063 -0.1362 0.1036  -0.0213 23  LYS B C   
2990 O O   . LYS B 53  ? 0.7839 0.5220 0.8045 -0.1334 0.1039  -0.0175 23  LYS B O   
2991 C CB  . LYS B 53  ? 0.7854 0.5719 0.8366 -0.1595 0.1085  -0.0340 23  LYS B CB  
2992 C CG  . LYS B 53  ? 0.8520 0.6167 0.8918 -0.1683 0.1150  -0.0270 23  LYS B CG  
2993 C CD  . LYS B 53  ? 0.9006 0.6783 0.9484 -0.1842 0.1207  -0.0302 23  LYS B CD  
2994 C CE  . LYS B 53  ? 0.9401 0.7172 0.9935 -0.1960 0.1203  -0.0398 23  LYS B CE  
2995 N NZ  . LYS B 53  ? 0.9723 0.7233 1.0155 -0.2103 0.1262  -0.0372 23  LYS B NZ  
2996 N N   . GLU B 54  ? 0.7712 0.5499 0.8089 -0.1312 0.1032  -0.0170 24  GLU B N   
2997 C CA  . GLU B 54  ? 0.7868 0.5552 0.8147 -0.1229 0.1031  -0.0076 24  GLU B CA  
2998 C C   . GLU B 54  ? 0.7905 0.5517 0.8134 -0.1101 0.0979  -0.0053 24  GLU B C   
2999 O O   . GLU B 54  ? 0.7991 0.5445 0.8106 -0.1043 0.0981  0.0016  24  GLU B O   
3000 C CB  . GLU B 54  ? 0.8119 0.5996 0.8456 -0.1204 0.1030  -0.0047 24  GLU B CB  
3001 C CG  . GLU B 54  ? 0.8848 0.6703 0.9150 -0.1289 0.1091  -0.0011 24  GLU B CG  
3002 C CD  . GLU B 54  ? 0.9847 0.7440 0.9997 -0.1299 0.1129  0.0062  24  GLU B CD  
3003 O OE1 . GLU B 54  ? 1.0103 0.7609 1.0171 -0.1199 0.1103  0.0123  24  GLU B OE1 
3004 O OE2 . GLU B 54  ? 1.0106 0.7579 1.0214 -0.1408 0.1184  0.0060  24  GLU B OE2 
3005 N N   . ARG B 55  ? 0.7827 0.5566 0.8138 -0.1054 0.0935  -0.0110 25  ARG B N   
3006 C CA  . ARG B 55  ? 0.7881 0.5599 0.8164 -0.0933 0.0886  -0.0095 25  ARG B CA  
3007 C C   . ARG B 55  ? 0.7960 0.5436 0.8123 -0.0912 0.0888  -0.0096 25  ARG B C   
3008 O O   . ARG B 55  ? 0.8032 0.5446 0.8128 -0.0803 0.0860  -0.0054 25  ARG B O   
3009 C CB  . ARG B 55  ? 0.7984 0.5911 0.8387 -0.0900 0.0846  -0.0161 25  ARG B CB  
3010 C CG  . ARG B 55  ? 0.8391 0.6355 0.8787 -0.0774 0.0798  -0.0142 25  ARG B CG  
3011 C CD  . ARG B 55  ? 0.8762 0.6955 0.9275 -0.0744 0.0766  -0.0188 25  ARG B CD  
3012 N NE  . ARG B 55  ? 0.9156 0.7492 0.9727 -0.0758 0.0769  -0.0162 25  ARG B NE  
3013 C CZ  . ARG B 55  ? 0.9423 0.7950 1.0086 -0.0745 0.0750  -0.0199 25  ARG B CZ  
3014 N NH1 . ARG B 55  ? 0.9429 0.8043 1.0143 -0.0720 0.0728  -0.0264 25  ARG B NH1 
3015 N NH2 . ARG B 55  ? 0.9340 0.7964 1.0031 -0.0751 0.0751  -0.0173 25  ARG B NH2 
3016 N N   . GLN B 56  ? 0.7944 0.5283 0.8074 -0.1016 0.0920  -0.0143 26  GLN B N   
3017 C CA  . GLN B 56  ? 0.8093 0.5167 0.8092 -0.1006 0.0921  -0.0153 26  GLN B CA  
3018 C C   . GLN B 56  ? 0.8246 0.5110 0.8086 -0.0925 0.0930  -0.0064 26  GLN B C   
3019 O O   . GLN B 56  ? 0.8362 0.5069 0.8099 -0.0841 0.0906  -0.0064 26  GLN B O   
3020 C CB  . GLN B 56  ? 0.8343 0.5292 0.8329 -0.1158 0.0960  -0.0209 26  GLN B CB  
3021 C CG  . GLN B 56  ? 0.8720 0.5853 0.8844 -0.1224 0.0940  -0.0315 26  GLN B CG  
3022 C CD  . GLN B 56  ? 0.9373 0.6563 0.9517 -0.1113 0.0880  -0.0367 26  GLN B CD  
3023 O OE1 . GLN B 56  ? 0.9620 0.6607 0.9646 -0.1047 0.0860  -0.0369 26  GLN B OE1 
3024 N NE2 . GLN B 56  ? 0.9433 0.6900 0.9717 -0.1082 0.0851  -0.0408 26  GLN B NE2 
3025 N N   . LYS B 57  ? 0.8240 0.5118 0.8058 -0.0931 0.0957  0.0011  27  LYS B N   
3026 C CA  . LYS B 57  ? 0.8359 0.5066 0.8028 -0.0843 0.0962  0.0097  27  LYS B CA  
3027 C C   . LYS B 57  ? 0.8298 0.5084 0.7963 -0.0688 0.0905  0.0115  27  LYS B C   
3028 O O   . LYS B 57  ? 0.8352 0.4963 0.7880 -0.0595 0.0896  0.0148  27  LYS B O   
3029 C CB  . LYS B 57  ? 0.8550 0.5324 0.8221 -0.0863 0.0990  0.0165  27  LYS B CB  
3030 C CG  . LYS B 57  ? 0.9033 0.5838 0.8755 -0.1010 0.1044  0.0148  27  LYS B CG  
3031 C CD  . LYS B 57  ? 0.9586 0.6516 0.9330 -0.1006 0.1059  0.0206  27  LYS B CD  
3032 C CE  . LYS B 57  ? 0.9933 0.7117 0.9795 -0.0931 0.1007  0.0202  27  LYS B CE  
3033 N NZ  . LYS B 57  ? 1.0093 0.7434 1.0016 -0.0971 0.1023  0.0217  27  LYS B NZ  
3034 N N   . ASP B 58  ? 0.8113 0.5165 0.7924 -0.0659 0.0870  0.0095  28  ASP B N   
3035 C CA  . ASP B 58  ? 0.8081 0.5249 0.7913 -0.0529 0.0820  0.0114  28  ASP B CA  
3036 C C   . ASP B 58  ? 0.8152 0.5332 0.8002 -0.0483 0.0790  0.0049  28  ASP B C   
3037 O O   . ASP B 58  ? 0.8114 0.5339 0.7942 -0.0364 0.0756  0.0069  28  ASP B O   
3038 C CB  . ASP B 58  ? 0.7978 0.5402 0.7936 -0.0517 0.0797  0.0138  28  ASP B CB  
3039 C CG  . ASP B 58  ? 0.8256 0.5673 0.8168 -0.0500 0.0805  0.0216  28  ASP B CG  
3040 O OD1 . ASP B 58  ? 0.8289 0.5512 0.8068 -0.0488 0.0830  0.0257  28  ASP B OD1 
3041 O OD2 . ASP B 58  ? 0.8453 0.6052 0.8452 -0.0495 0.0784  0.0235  28  ASP B OD2 
3042 N N   . LEU B 59  ? 0.8223 0.5371 0.8112 -0.0575 0.0803  -0.0030 29  LEU B N   
3043 C CA  . LEU B 59  ? 0.8325 0.5465 0.8217 -0.0533 0.0773  -0.0100 29  LEU B CA  
3044 C C   . LEU B 59  ? 0.8606 0.5457 0.8321 -0.0481 0.0773  -0.0102 29  LEU B C   
3045 O O   . LEU B 59  ? 0.8701 0.5504 0.8391 -0.0442 0.0748  -0.0165 29  LEU B O   
3046 C CB  . LEU B 59  ? 0.8269 0.5516 0.8276 -0.0637 0.0775  -0.0193 29  LEU B CB  
3047 C CG  . LEU B 59  ? 0.8305 0.5841 0.8474 -0.0662 0.0767  -0.0199 29  LEU B CG  
3048 C CD1 . LEU B 59  ? 0.8297 0.5952 0.8567 -0.0731 0.0760  -0.0298 29  LEU B CD1 
3049 C CD2 . LEU B 59  ? 0.8327 0.6035 0.8540 -0.0537 0.0729  -0.0155 29  LEU B CD2 
3050 N N   . LYS B 60  ? 0.8735 0.5395 0.8317 -0.0464 0.0799  -0.0033 30  LYS B N   
3051 C CA  . LYS B 60  ? 0.9040 0.5419 0.8431 -0.0387 0.0797  -0.0022 30  LYS B CA  
3052 C C   . LYS B 60  ? 0.9061 0.5543 0.8423 -0.0209 0.0756  0.0021  30  LYS B C   
3053 O O   . LYS B 60  ? 0.9200 0.5583 0.8471 -0.0111 0.0730  -0.0008 30  LYS B O   
3054 C CB  . LYS B 60  ? 0.9502 0.5632 0.8751 -0.0436 0.0843  0.0038  30  LYS B CB  
3055 C CG  . LYS B 60  ? 1.0182 0.6189 0.9442 -0.0617 0.0889  -0.0003 30  LYS B CG  
3056 C CD  . LYS B 60  ? 1.0960 0.6733 1.0081 -0.0669 0.0943  0.0067  30  LYS B CD  
3057 C CE  . LYS B 60  ? 1.1731 0.7121 1.0639 -0.0666 0.0957  0.0059  30  LYS B CE  
3058 N NZ  . LYS B 60  ? 1.2201 0.7355 1.0970 -0.0732 0.1017  0.0130  30  LYS B NZ  
3059 N N   . PHE B 61  ? 0.8932 0.5624 0.8375 -0.0170 0.0749  0.0087  31  PHE B N   
3060 C CA  . PHE B 61  ? 0.8950 0.5787 0.8391 -0.0020 0.0713  0.0136  31  PHE B CA  
3061 C C   . PHE B 61  ? 0.8666 0.5772 0.8253 0.0019  0.0677  0.0102  31  PHE B C   
3062 O O   . PHE B 61  ? 0.8652 0.5829 0.8212 0.0148  0.0648  0.0114  31  PHE B O   
3063 C CB  . PHE B 61  ? 0.9039 0.5974 0.8498 -0.0011 0.0720  0.0221  31  PHE B CB  
3064 C CG  . PHE B 61  ? 0.9422 0.6102 0.8715 -0.0016 0.0752  0.0268  31  PHE B CG  
3065 C CD1 . PHE B 61  ? 0.9656 0.6222 0.8797 0.0121  0.0741  0.0317  31  PHE B CD1 
3066 C CD2 . PHE B 61  ? 0.9634 0.6197 0.8920 -0.0150 0.0796  0.0265  31  PHE B CD2 
3067 C CE1 . PHE B 61  ? 0.9894 0.6219 0.8870 0.0126  0.0772  0.0364  31  PHE B CE1 
3068 C CE2 . PHE B 61  ? 0.9869 0.6193 0.8994 -0.0152 0.0831  0.0315  31  PHE B CE2 
3069 C CZ  . PHE B 61  ? 0.9931 0.6131 0.8898 -0.0013 0.0818  0.0365  31  PHE B CZ  
3070 N N   . LEU B 62  ? 0.8400 0.5661 0.8136 -0.0085 0.0682  0.0063  32  LEU B N   
3071 C CA  . LEU B 62  ? 0.8089 0.5599 0.7961 -0.0056 0.0652  0.0034  32  LEU B CA  
3072 C C   . LEU B 62  ? 0.7904 0.5413 0.7832 -0.0129 0.0652  -0.0064 32  LEU B C   
3073 O O   . LEU B 62  ? 0.7915 0.5327 0.7850 -0.0250 0.0679  -0.0101 32  LEU B O   
3074 C CB  . LEU B 62  ? 0.7935 0.5662 0.7935 -0.0098 0.0651  0.0080  32  LEU B CB  
3075 C CG  . LEU B 62  ? 0.8048 0.5835 0.8021 -0.0029 0.0641  0.0170  32  LEU B CG  
3076 C CD1 . LEU B 62  ? 0.7999 0.5851 0.8033 -0.0115 0.0654  0.0207  32  LEU B CD1 
3077 C CD2 . LEU B 62  ? 0.8047 0.6037 0.8074 0.0077  0.0607  0.0197  32  LEU B CD2 
3078 N N   . SER B 63  ? 0.7681 0.5322 0.7658 -0.0059 0.0622  -0.0105 33  SER B N   
3079 C CA  . SER B 63  ? 0.7579 0.5256 0.7621 -0.0120 0.0616  -0.0201 33  SER B CA  
3080 C C   . SER B 63  ? 0.7493 0.5370 0.7684 -0.0211 0.0625  -0.0208 33  SER B C   
3081 O O   . SER B 63  ? 0.7472 0.5442 0.7706 -0.0220 0.0632  -0.0138 33  SER B O   
3082 C CB  . SER B 63  ? 0.7610 0.5373 0.7648 -0.0004 0.0580  -0.0240 33  SER B CB  
3083 O OG  . SER B 63  ? 0.7659 0.5688 0.7808 0.0050  0.0564  -0.0208 33  SER B OG  
3084 N N   . GLU B 64  ? 0.7433 0.5372 0.7696 -0.0278 0.0622  -0.0294 34  GLU B N   
3085 C CA  . GLU B 64  ? 0.7351 0.5486 0.7744 -0.0346 0.0627  -0.0306 34  GLU B CA  
3086 C C   . GLU B 64  ? 0.7141 0.5489 0.7602 -0.0255 0.0603  -0.0260 34  GLU B C   
3087 O O   . GLU B 64  ? 0.7022 0.5487 0.7550 -0.0284 0.0609  -0.0219 34  GLU B O   
3088 C CB  . GLU B 64  ? 0.7748 0.5931 0.8200 -0.0416 0.0623  -0.0414 34  GLU B CB  
3089 C CG  . GLU B 64  ? 0.8738 0.6739 0.9146 -0.0538 0.0651  -0.0461 34  GLU B CG  
3090 C CD  . GLU B 64  ? 0.9811 0.7947 1.0328 -0.0652 0.0663  -0.0531 34  GLU B CD  
3091 O OE1 . GLU B 64  ? 1.0122 0.8256 1.0656 -0.0693 0.0650  -0.0626 34  GLU B OE1 
3092 O OE2 . GLU B 64  ? 0.9977 0.8227 1.0559 -0.0695 0.0684  -0.0494 34  GLU B OE2 
3093 N N   . GLU B 65  ? 0.7089 0.5477 0.7525 -0.0145 0.0577  -0.0266 35  GLU B N   
3094 C CA  . GLU B 65  ? 0.6997 0.5578 0.7485 -0.0053 0.0556  -0.0220 35  GLU B CA  
3095 C C   . GLU B 65  ? 0.6861 0.5461 0.7335 -0.0023 0.0561  -0.0115 35  GLU B C   
3096 O O   . GLU B 65  ? 0.6844 0.5594 0.7388 -0.0022 0.0555  -0.0067 35  GLU B O   
3097 C CB  . GLU B 65  ? 0.7366 0.5961 0.7809 0.0059  0.0533  -0.0254 35  GLU B CB  
3098 C CG  . GLU B 65  ? 0.8139 0.6945 0.8658 0.0116  0.0514  -0.0271 35  GLU B CG  
3099 C CD  . GLU B 65  ? 0.9405 0.8232 0.9874 0.0232  0.0491  -0.0310 35  GLU B CD  
3100 O OE1 . GLU B 65  ? 0.9676 0.8355 1.0044 0.0283  0.0487  -0.0315 35  GLU B OE1 
3101 O OE2 . GLU B 65  ? 0.9834 0.8822 1.0355 0.0280  0.0478  -0.0336 35  GLU B OE2 
3102 N N   . GLU B 66  ? 0.6760 0.5204 0.7137 0.0000  0.0568  -0.0080 36  GLU B N   
3103 C CA  . GLU B 66  ? 0.6679 0.5147 0.7039 0.0029  0.0569  0.0016  36  GLU B CA  
3104 C C   . GLU B 66  ? 0.6526 0.4999 0.6931 -0.0070 0.0585  0.0045  36  GLU B C   
3105 O O   . GLU B 66  ? 0.6501 0.5085 0.6946 -0.0061 0.0576  0.0112  36  GLU B O   
3106 C CB  . GLU B 66  ? 0.7115 0.5407 0.7346 0.0090  0.0573  0.0039  36  GLU B CB  
3107 C CG  . GLU B 66  ? 0.7711 0.5985 0.7879 0.0202  0.0555  0.0005  36  GLU B CG  
3108 C CD  . GLU B 66  ? 0.8407 0.6509 0.8431 0.0288  0.0555  0.0029  36  GLU B CD  
3109 O OE1 . GLU B 66  ? 0.8564 0.6433 0.8492 0.0237  0.0573  0.0009  36  GLU B OE1 
3110 O OE2 . GLU B 66  ? 0.8664 0.6868 0.8663 0.0410  0.0538  0.0070  36  GLU B OE2 
3111 N N   . TYR B 67  ? 0.6468 0.4830 0.6866 -0.0167 0.0608  -0.0005 37  TYR B N   
3112 C CA  . TYR B 67  ? 0.6452 0.4823 0.6886 -0.0258 0.0625  0.0015  37  TYR B CA  
3113 C C   . TYR B 67  ? 0.6411 0.4978 0.6952 -0.0270 0.0610  0.0015  37  TYR B C   
3114 O O   . TYR B 67  ? 0.6408 0.5028 0.6971 -0.0289 0.0606  0.0068  37  TYR B O   
3115 C CB  . TYR B 67  ? 0.6486 0.4721 0.6895 -0.0359 0.0657  -0.0042 37  TYR B CB  
3116 C CG  . TYR B 67  ? 0.6575 0.4795 0.6993 -0.0438 0.0681  -0.0010 37  TYR B CG  
3117 C CD1 . TYR B 67  ? 0.6594 0.4954 0.7101 -0.0490 0.0682  -0.0031 37  TYR B CD1 
3118 C CD2 . TYR B 67  ? 0.6748 0.4815 0.7073 -0.0449 0.0701  0.0043  37  TYR B CD2 
3119 C CE1 . TYR B 67  ? 0.6684 0.5038 0.7191 -0.0549 0.0701  -0.0002 37  TYR B CE1 
3120 C CE2 . TYR B 67  ? 0.6848 0.4911 0.7175 -0.0511 0.0722  0.0074  37  TYR B CE2 
3121 C CZ  . TYR B 67  ? 0.6842 0.5051 0.7261 -0.0561 0.0722  0.0050  37  TYR B CZ  
3122 O OH  . TYR B 67  ? 0.6923 0.5132 0.7336 -0.0613 0.0741  0.0077  37  TYR B OH  
3123 N N   . TRP B 68  ? 0.6361 0.5027 0.6956 -0.0252 0.0599  -0.0044 38  TRP B N   
3124 C CA  . TRP B 68  ? 0.6320 0.5157 0.6998 -0.0249 0.0584  -0.0047 38  TRP B CA  
3125 C C   . TRP B 68  ? 0.6137 0.5066 0.6825 -0.0183 0.0563  0.0034  38  TRP B C   
3126 O O   . TRP B 68  ? 0.6158 0.5147 0.6877 -0.0208 0.0557  0.0077  38  TRP B O   
3127 C CB  . TRP B 68  ? 0.6400 0.5320 0.7118 -0.0226 0.0575  -0.0128 38  TRP B CB  
3128 C CG  . TRP B 68  ? 0.6593 0.5671 0.7381 -0.0221 0.0563  -0.0139 38  TRP B CG  
3129 C CD1 . TRP B 68  ? 0.6712 0.5838 0.7523 -0.0249 0.0562  -0.0095 38  TRP B CD1 
3130 C CD2 . TRP B 68  ? 0.6644 0.5834 0.7470 -0.0183 0.0550  -0.0204 38  TRP B CD2 
3131 N NE1 . TRP B 68  ? 0.6720 0.5971 0.7575 -0.0226 0.0550  -0.0125 38  TRP B NE1 
3132 C CE2 . TRP B 68  ? 0.6704 0.6004 0.7571 -0.0184 0.0544  -0.0190 38  TRP B CE2 
3133 C CE3 . TRP B 68  ? 0.6733 0.5935 0.7553 -0.0143 0.0541  -0.0276 38  TRP B CE3 
3134 C CZ2 . TRP B 68  ? 0.6766 0.6191 0.7665 -0.0138 0.0531  -0.0239 38  TRP B CZ2 
3135 C CZ3 . TRP B 68  ? 0.6791 0.6132 0.7653 -0.0103 0.0526  -0.0328 38  TRP B CZ3 
3136 C CH2 . TRP B 68  ? 0.6764 0.6217 0.7665 -0.0098 0.0522  -0.0308 38  TRP B CH2 
3137 N N   . LYS B 69  ? 0.5969 0.4906 0.6626 -0.0102 0.0554  0.0057  39  LYS B N   
3138 C CA  . LYS B 69  ? 0.5798 0.4843 0.6468 -0.0040 0.0537  0.0136  39  LYS B CA  
3139 C C   . LYS B 69  ? 0.5778 0.4797 0.6435 -0.0075 0.0535  0.0208  39  LYS B C   
3140 O O   . LYS B 69  ? 0.5791 0.4921 0.6488 -0.0070 0.0520  0.0268  39  LYS B O   
3141 C CB  . LYS B 69  ? 0.5878 0.4923 0.6500 0.0059  0.0531  0.0140  39  LYS B CB  
3142 C CG  . LYS B 69  ? 0.6119 0.5224 0.6756 0.0109  0.0526  0.0076  39  LYS B CG  
3143 C CD  . LYS B 69  ? 0.6540 0.5619 0.7110 0.0213  0.0519  0.0068  39  LYS B CD  
3144 C CE  . LYS B 69  ? 0.6911 0.6076 0.7498 0.0272  0.0509  0.0009  39  LYS B CE  
3145 N NZ  . LYS B 69  ? 0.7190 0.6333 0.7702 0.0386  0.0500  -0.0002 39  LYS B NZ  
3146 N N   . LEU B 70  ? 0.5753 0.4626 0.6352 -0.0112 0.0550  0.0202  40  LEU B N   
3147 C CA  . LEU B 70  ? 0.5821 0.4666 0.6400 -0.0142 0.0547  0.0264  40  LEU B CA  
3148 C C   . LEU B 70  ? 0.5868 0.4745 0.6494 -0.0219 0.0545  0.0262  40  LEU B C   
3149 O O   . LEU B 70  ? 0.5866 0.4798 0.6507 -0.0233 0.0526  0.0316  40  LEU B O   
3150 C CB  . LEU B 70  ? 0.5958 0.4623 0.6445 -0.0153 0.0569  0.0257  40  LEU B CB  
3151 C CG  . LEU B 70  ? 0.6205 0.4843 0.6624 -0.0080 0.0560  0.0316  40  LEU B CG  
3152 C CD1 . LEU B 70  ? 0.6446 0.4876 0.6754 -0.0078 0.0584  0.0300  40  LEU B CD1 
3153 C CD2 . LEU B 70  ? 0.6214 0.4929 0.6655 -0.0097 0.0542  0.0381  40  LEU B CD2 
3154 N N   . GLN B 71  ? 0.5865 0.4713 0.6509 -0.0268 0.0561  0.0195  41  GLN B N   
3155 C CA  . GLN B 71  ? 0.5825 0.4706 0.6503 -0.0328 0.0561  0.0181  41  GLN B CA  
3156 C C   . GLN B 71  ? 0.5653 0.4663 0.6384 -0.0306 0.0535  0.0201  41  GLN B C   
3157 O O   . GLN B 71  ? 0.5686 0.4714 0.6426 -0.0339 0.0523  0.0218  41  GLN B O   
3158 C CB  . GLN B 71  ? 0.6128 0.4965 0.6812 -0.0380 0.0587  0.0102  41  GLN B CB  
3159 C CG  . GLN B 71  ? 0.6804 0.5495 0.7427 -0.0429 0.0618  0.0097  41  GLN B CG  
3160 C CD  . GLN B 71  ? 0.7571 0.6226 0.8167 -0.0471 0.0623  0.0138  41  GLN B CD  
3161 O OE1 . GLN B 71  ? 0.7949 0.6673 0.8576 -0.0495 0.0614  0.0131  41  GLN B OE1 
3162 N NE2 . GLN B 71  ? 0.7512 0.6051 0.8036 -0.0473 0.0636  0.0178  41  GLN B NE2 
3163 N N   . ILE B 72  ? 0.5494 0.4586 0.6251 -0.0246 0.0526  0.0201  42  ILE B N   
3164 C CA  . ILE B 72  ? 0.5396 0.4604 0.6192 -0.0220 0.0506  0.0233  42  ILE B CA  
3165 C C   . ILE B 72  ? 0.5376 0.4617 0.6171 -0.0220 0.0487  0.0320  42  ILE B C   
3166 O O   . ILE B 72  ? 0.5422 0.4698 0.6233 -0.0249 0.0469  0.0356  42  ILE B O   
3167 C CB  . ILE B 72  ? 0.5372 0.4659 0.6185 -0.0149 0.0508  0.0210  42  ILE B CB  
3168 C CG1 . ILE B 72  ? 0.5447 0.4732 0.6272 -0.0152 0.0518  0.0119  42  ILE B CG1 
3169 C CG2 . ILE B 72  ? 0.5380 0.4786 0.6223 -0.0114 0.0492  0.0269  42  ILE B CG2 
3170 C CD1 . ILE B 72  ? 0.5555 0.4873 0.6376 -0.0085 0.0520  0.0078  42  ILE B CD1 
3171 N N   . PHE B 73  ? 0.5288 0.4515 0.6059 -0.0188 0.0489  0.0352  43  PHE B N   
3172 C CA  . PHE B 73  ? 0.5229 0.4513 0.6004 -0.0181 0.0470  0.0429  43  PHE B CA  
3173 C C   . PHE B 73  ? 0.5162 0.4397 0.5927 -0.0250 0.0455  0.0452  43  PHE B C   
3174 O O   . PHE B 73  ? 0.5098 0.4402 0.5893 -0.0277 0.0431  0.0497  43  PHE B O   
3175 C CB  . PHE B 73  ? 0.5255 0.4516 0.5988 -0.0121 0.0477  0.0444  43  PHE B CB  
3176 C CG  . PHE B 73  ? 0.5308 0.4655 0.6048 -0.0108 0.0456  0.0520  43  PHE B CG  
3177 C CD1 . PHE B 73  ? 0.5297 0.4809 0.6094 -0.0090 0.0441  0.0574  43  PHE B CD1 
3178 C CD2 . PHE B 73  ? 0.5471 0.4745 0.6161 -0.0116 0.0452  0.0539  43  PHE B CD2 
3179 C CE1 . PHE B 73  ? 0.5343 0.4960 0.6157 -0.0086 0.0420  0.0642  43  PHE B CE1 
3180 C CE2 . PHE B 73  ? 0.5500 0.4876 0.6201 -0.0101 0.0429  0.0604  43  PHE B CE2 
3181 C CZ  . PHE B 73  ? 0.5348 0.4903 0.6118 -0.0092 0.0411  0.0653  43  PHE B CZ  
3182 N N   . PHE B 74  ? 0.5138 0.4250 0.5856 -0.0281 0.0468  0.0421  44  PHE B N   
3183 C CA  . PHE B 74  ? 0.5100 0.4162 0.5796 -0.0337 0.0454  0.0438  44  PHE B CA  
3184 C C   . PHE B 74  ? 0.4998 0.4066 0.5713 -0.0381 0.0441  0.0419  44  PHE B C   
3185 O O   . PHE B 74  ? 0.5008 0.4066 0.5712 -0.0419 0.0414  0.0447  44  PHE B O   
3186 C CB  . PHE B 74  ? 0.5172 0.4107 0.5805 -0.0352 0.0477  0.0416  44  PHE B CB  
3187 C CG  . PHE B 74  ? 0.5301 0.4222 0.5893 -0.0308 0.0475  0.0459  44  PHE B CG  
3188 C CD1 . PHE B 74  ? 0.5383 0.4369 0.5977 -0.0305 0.0442  0.0517  44  PHE B CD1 
3189 C CD2 . PHE B 74  ? 0.5412 0.4259 0.5958 -0.0263 0.0501  0.0439  44  PHE B CD2 
3190 C CE1 . PHE B 74  ? 0.5458 0.4453 0.6012 -0.0251 0.0438  0.0555  44  PHE B CE1 
3191 C CE2 . PHE B 74  ? 0.5511 0.4339 0.6003 -0.0206 0.0498  0.0479  44  PHE B CE2 
3192 C CZ  . PHE B 74  ? 0.5466 0.4379 0.5965 -0.0195 0.0467  0.0537  44  PHE B CZ  
3193 N N   . THR B 75  ? 0.4863 0.3954 0.5602 -0.0369 0.0454  0.0372  45  THR B N   
3194 C CA  . THR B 75  ? 0.4800 0.3903 0.5546 -0.0390 0.0441  0.0357  45  THR B CA  
3195 C C   . THR B 75  ? 0.4726 0.3897 0.5494 -0.0391 0.0410  0.0422  45  THR B C   
3196 O O   . THR B 75  ? 0.4764 0.3902 0.5512 -0.0429 0.0384  0.0441  45  THR B O   
3197 C CB  . THR B 75  ? 0.4854 0.3982 0.5618 -0.0364 0.0462  0.0290  45  THR B CB  
3198 O OG1 . THR B 75  ? 0.5052 0.4118 0.5798 -0.0387 0.0489  0.0234  45  THR B OG1 
3199 C CG2 . THR B 75  ? 0.4781 0.3932 0.5542 -0.0362 0.0447  0.0277  45  THR B CG2 
3200 N N   . ASN B 76  ? 0.4621 0.3883 0.5424 -0.0352 0.0413  0.0457  46  ASN B N   
3201 C CA  . ASN B 76  ? 0.4613 0.3963 0.5446 -0.0358 0.0391  0.0527  46  ASN B CA  
3202 C C   . ASN B 76  ? 0.4670 0.4024 0.5500 -0.0405 0.0362  0.0582  46  ASN B C   
3203 O O   . ASN B 76  ? 0.4708 0.4095 0.5552 -0.0447 0.0336  0.0629  46  ASN B O   
3204 C CB  . ASN B 76  ? 0.4694 0.4161 0.5564 -0.0296 0.0406  0.0549  46  ASN B CB  
3205 C CG  . ASN B 76  ? 0.5045 0.4527 0.5918 -0.0246 0.0427  0.0498  46  ASN B CG  
3206 O OD1 . ASN B 76  ? 0.5155 0.4578 0.6009 -0.0259 0.0430  0.0448  46  ASN B OD1 
3207 N ND2 . ASN B 76  ? 0.5050 0.4624 0.5943 -0.0180 0.0441  0.0506  46  ASN B ND2 
3208 N N   . VAL B 77  ? 0.4640 0.3959 0.5449 -0.0400 0.0366  0.0576  47  VAL B N   
3209 C CA  . VAL B 77  ? 0.4599 0.3928 0.5400 -0.0435 0.0336  0.0619  47  VAL B CA  
3210 C C   . VAL B 77  ? 0.4685 0.3916 0.5448 -0.0498 0.0310  0.0605  47  VAL B C   
3211 O O   . VAL B 77  ? 0.4648 0.3906 0.5421 -0.0547 0.0273  0.0645  47  VAL B O   
3212 C CB  . VAL B 77  ? 0.4687 0.3986 0.5454 -0.0397 0.0350  0.0613  47  VAL B CB  
3213 C CG1 . VAL B 77  ? 0.4713 0.4029 0.5465 -0.0426 0.0316  0.0652  47  VAL B CG1 
3214 C CG2 . VAL B 77  ? 0.4729 0.4109 0.5514 -0.0323 0.0371  0.0625  47  VAL B CG2 
3215 N N   . ILE B 78  ? 0.4758 0.3881 0.5478 -0.0497 0.0328  0.0545  48  ILE B N   
3216 C CA  . ILE B 78  ? 0.4896 0.3922 0.5566 -0.0539 0.0308  0.0521  48  ILE B CA  
3217 C C   . ILE B 78  ? 0.5002 0.4029 0.5676 -0.0565 0.0281  0.0537  48  ILE B C   
3218 O O   . ILE B 78  ? 0.5116 0.4096 0.5759 -0.0611 0.0242  0.0556  48  ILE B O   
3219 C CB  . ILE B 78  ? 0.5038 0.3987 0.5673 -0.0523 0.0342  0.0453  48  ILE B CB  
3220 C CG1 . ILE B 78  ? 0.5151 0.4061 0.5759 -0.0514 0.0366  0.0446  48  ILE B CG1 
3221 C CG2 . ILE B 78  ? 0.5199 0.4068 0.5781 -0.0547 0.0324  0.0422  48  ILE B CG2 
3222 C CD1 . ILE B 78  ? 0.5316 0.4171 0.5903 -0.0509 0.0408  0.0386  48  ILE B CD1 
3223 N N   . GLN B 79  ? 0.4969 0.4045 0.5673 -0.0535 0.0301  0.0533  49  GLN B N   
3224 C CA  . GLN B 79  ? 0.4988 0.4056 0.5684 -0.0552 0.0281  0.0556  49  GLN B CA  
3225 C C   . GLN B 79  ? 0.4976 0.4098 0.5700 -0.0604 0.0248  0.0631  49  GLN B C   
3226 O O   . GLN B 79  ? 0.5083 0.4131 0.5768 -0.0655 0.0214  0.0649  49  GLN B O   
3227 C CB  . GLN B 79  ? 0.5140 0.4265 0.5861 -0.0496 0.0312  0.0539  49  GLN B CB  
3228 C CG  . GLN B 79  ? 0.5661 0.4777 0.6363 -0.0504 0.0299  0.0572  49  GLN B CG  
3229 C CD  . GLN B 79  ? 0.6666 0.5645 0.7285 -0.0518 0.0276  0.0542  49  GLN B CD  
3230 O OE1 . GLN B 79  ? 0.7067 0.6000 0.7652 -0.0484 0.0288  0.0476  49  GLN B OE1 
3231 N NE2 . GLN B 79  ? 0.6883 0.5796 0.7464 -0.0567 0.0243  0.0590  49  GLN B NE2 
3232 N N   . ALA B 80  ? 0.4870 0.4119 0.5656 -0.0593 0.0256  0.0672  50  ALA B N   
3233 C CA  . ALA B 80  ? 0.4884 0.4224 0.5711 -0.0646 0.0227  0.0743  50  ALA B CA  
3234 C C   . ALA B 80  ? 0.5057 0.4335 0.5853 -0.0710 0.0182  0.0746  50  ALA B C   
3235 O O   . ALA B 80  ? 0.5058 0.4335 0.5857 -0.0782 0.0144  0.0786  50  ALA B O   
3236 C CB  . ALA B 80  ? 0.4796 0.4301 0.5690 -0.0603 0.0247  0.0778  50  ALA B CB  
3237 N N   . LEU B 81  ? 0.5165 0.4382 0.5923 -0.0685 0.0186  0.0703  51  LEU B N   
3238 C CA  . LEU B 81  ? 0.5278 0.4432 0.5994 -0.0729 0.0145  0.0697  51  LEU B CA  
3239 C C   . LEU B 81  ? 0.5401 0.4412 0.6050 -0.0775 0.0113  0.0675  51  LEU B C   
3240 O O   . LEU B 81  ? 0.5458 0.4442 0.6089 -0.0841 0.0063  0.0695  51  LEU B O   
3241 C CB  . LEU B 81  ? 0.5379 0.4475 0.6052 -0.0682 0.0167  0.0653  51  LEU B CB  
3242 C CG  . LEU B 81  ? 0.5566 0.4755 0.6267 -0.0635 0.0188  0.0672  51  LEU B CG  
3243 C CD1 . LEU B 81  ? 0.5633 0.4723 0.6270 -0.0599 0.0213  0.0629  51  LEU B CD1 
3244 C CD2 . LEU B 81  ? 0.5641 0.4943 0.6375 -0.0666 0.0145  0.0723  51  LEU B CD2 
3245 N N   . GLY B 82  ? 0.5426 0.4346 0.6032 -0.0738 0.0139  0.0628  52  GLY B N   
3246 C CA  . GLY B 82  ? 0.5547 0.4323 0.6071 -0.0758 0.0114  0.0600  52  GLY B CA  
3247 C C   . GLY B 82  ? 0.5595 0.4352 0.6118 -0.0813 0.0083  0.0648  52  GLY B C   
3248 O O   . GLY B 82  ? 0.5739 0.4376 0.6193 -0.0863 0.0037  0.0647  52  GLY B O   
3249 N N   . GLU B 83  ? 0.5511 0.4383 0.6105 -0.0807 0.0109  0.0694  53  GLU B N   
3250 C CA  . GLU B 83  ? 0.5606 0.4471 0.6202 -0.0867 0.0088  0.0752  53  GLU B CA  
3251 C C   . GLU B 83  ? 0.5675 0.4568 0.6293 -0.0962 0.0037  0.0795  53  GLU B C   
3252 O O   . GLU B 83  ? 0.5751 0.4519 0.6308 -0.1031 -0.0006 0.0806  53  GLU B O   
3253 C CB  . GLU B 83  ? 0.5767 0.4777 0.6439 -0.0836 0.0130  0.0797  53  GLU B CB  
3254 C CG  . GLU B 83  ? 0.6466 0.5431 0.7102 -0.0755 0.0168  0.0758  53  GLU B CG  
3255 C CD  . GLU B 83  ? 0.7382 0.6504 0.8091 -0.0701 0.0212  0.0785  53  GLU B CD  
3256 O OE1 . GLU B 83  ? 0.7553 0.6814 0.8334 -0.0731 0.0214  0.0849  53  GLU B OE1 
3257 O OE2 . GLU B 83  ? 0.7519 0.6634 0.8212 -0.0625 0.0244  0.0739  53  GLU B OE2 
3258 N N   . HIS B 84  ? 0.5660 0.4703 0.6353 -0.0961 0.0039  0.0811  54  HIS B N   
3259 C CA  . HIS B 84  ? 0.5756 0.4870 0.6484 -0.1042 -0.0010 0.0846  54  HIS B CA  
3260 C C   . HIS B 84  ? 0.5965 0.4903 0.6599 -0.1092 -0.0067 0.0807  54  HIS B C   
3261 O O   . HIS B 84  ? 0.6036 0.4949 0.6663 -0.1188 -0.0119 0.0834  54  HIS B O   
3262 C CB  . HIS B 84  ? 0.5789 0.5072 0.6585 -0.0995 0.0005  0.0851  54  HIS B CB  
3263 C CG  . HIS B 84  ? 0.6091 0.5523 0.6952 -0.1065 -0.0037 0.0899  54  HIS B CG  
3264 N ND1 . HIS B 84  ? 0.6248 0.5891 0.7210 -0.1079 -0.0021 0.0963  54  HIS B ND1 
3265 C CD2 . HIS B 84  ? 0.6309 0.5720 0.7148 -0.1123 -0.0094 0.0887  54  HIS B CD2 
3266 C CE1 . HIS B 84  ? 0.6281 0.6037 0.7286 -0.1147 -0.0069 0.0989  54  HIS B CE1 
3267 N NE2 . HIS B 84  ? 0.6350 0.5970 0.7284 -0.1177 -0.0116 0.0943  54  HIS B NE2 
3268 N N   . LEU B 85  ? 0.6057 0.4875 0.6614 -0.1029 -0.0058 0.0741  55  LEU B N   
3269 C CA  . LEU B 85  ? 0.6269 0.4922 0.6723 -0.1055 -0.0108 0.0697  55  LEU B CA  
3270 C C   . LEU B 85  ? 0.6542 0.4990 0.6889 -0.1069 -0.0129 0.0675  55  LEU B C   
3271 O O   . LEU B 85  ? 0.6628 0.4920 0.6869 -0.1068 -0.0166 0.0628  55  LEU B O   
3272 C CB  . LEU B 85  ? 0.6296 0.4930 0.6714 -0.0979 -0.0086 0.0643  55  LEU B CB  
3273 C CG  . LEU B 85  ? 0.6393 0.5183 0.6880 -0.0965 -0.0079 0.0663  55  LEU B CG  
3274 C CD1 . LEU B 85  ? 0.6462 0.5245 0.6928 -0.0879 -0.0029 0.0625  55  LEU B CD1 
3275 C CD2 . LEU B 85  ? 0.6453 0.5245 0.6920 -0.1027 -0.0147 0.0668  55  LEU B CD2 
3276 N N   . LYS B 86  ? 0.6637 0.5085 0.7001 -0.1074 -0.0104 0.0710  56  LYS B N   
3277 C CA  . LYS B 86  ? 0.6873 0.5130 0.7129 -0.1075 -0.0116 0.0699  56  LYS B CA  
3278 C C   . LYS B 86  ? 0.6965 0.5088 0.7115 -0.0986 -0.0107 0.0621  56  LYS B C   
3279 O O   . LYS B 86  ? 0.7142 0.5070 0.7165 -0.0986 -0.0143 0.0593  56  LYS B O   
3280 C CB  . LYS B 86  ? 0.7275 0.5406 0.7475 -0.1187 -0.0183 0.0729  56  LYS B CB  
3281 C CG  . LYS B 86  ? 0.7800 0.6083 0.8111 -0.1283 -0.0185 0.0812  56  LYS B CG  
3282 C CD  . LYS B 86  ? 0.8567 0.6705 0.8815 -0.1409 -0.0250 0.0841  56  LYS B CD  
3283 C CE  . LYS B 86  ? 0.9100 0.7380 0.9450 -0.1510 -0.0243 0.0931  56  LYS B CE  
3284 N NZ  . LYS B 86  ? 0.9548 0.7639 0.9815 -0.1637 -0.0297 0.0961  56  LYS B NZ  
3285 N N   . LEU B 87  ? 0.6834 0.5063 0.7032 -0.0910 -0.0059 0.0588  57  LEU B N   
3286 C CA  . LEU B 87  ? 0.6920 0.5073 0.7042 -0.0829 -0.0041 0.0517  57  LEU B CA  
3287 C C   . LEU B 87  ? 0.7079 0.5211 0.7177 -0.0761 -0.0003 0.0499  57  LEU B C   
3288 O O   . LEU B 87  ? 0.7094 0.5329 0.7268 -0.0754 0.0031  0.0534  57  LEU B O   
3289 C CB  . LEU B 87  ? 0.6782 0.5055 0.6967 -0.0791 -0.0004 0.0493  57  LEU B CB  
3290 C CG  . LEU B 87  ? 0.6788 0.5097 0.6991 -0.0837 -0.0037 0.0508  57  LEU B CG  
3291 C CD1 . LEU B 87  ? 0.6765 0.5183 0.7023 -0.0793 0.0009  0.0494  57  LEU B CD1 
3292 C CD2 . LEU B 87  ? 0.6912 0.5067 0.6998 -0.0851 -0.0091 0.0471  57  LEU B CD2 
3293 N N   . ARG B 88  ? 0.7169 0.5181 0.7157 -0.0702 -0.0009 0.0441  58  ARG B N   
3294 C CA  . ARG B 88  ? 0.7247 0.5245 0.7197 -0.0623 0.0022  0.0412  58  ARG B CA  
3295 C C   . ARG B 88  ? 0.6993 0.5171 0.7051 -0.0573 0.0085  0.0391  58  ARG B C   
3296 O O   . ARG B 88  ? 0.6962 0.5231 0.7087 -0.0585 0.0104  0.0382  58  ARG B O   
3297 C CB  . ARG B 88  ? 0.7701 0.5561 0.7512 -0.0561 0.0002  0.0347  58  ARG B CB  
3298 C CG  . ARG B 88  ? 0.8512 0.6193 0.8188 -0.0536 -0.0031 0.0349  58  ARG B CG  
3299 C CD  . ARG B 88  ? 0.9370 0.6924 0.8903 -0.0466 -0.0055 0.0281  58  ARG B CD  
3300 N NE  . ARG B 88  ? 1.0117 0.7545 0.9521 -0.0387 -0.0063 0.0261  58  ARG B NE  
3301 C CZ  . ARG B 88  ? 1.0660 0.7854 0.9907 -0.0392 -0.0117 0.0269  58  ARG B CZ  
3302 N NH1 . ARG B 88  ? 1.0791 0.7869 0.9909 -0.0304 -0.0120 0.0251  58  ARG B NH1 
3303 N NH2 . ARG B 88  ? 1.0703 0.7770 0.9912 -0.0484 -0.0171 0.0294  58  ARG B NH2 
3304 N N   . GLN B 89  ? 0.6801 0.5017 0.6863 -0.0514 0.0115  0.0379  59  GLN B N   
3305 C CA  . GLN B 89  ? 0.6645 0.5019 0.6799 -0.0467 0.0169  0.0350  59  GLN B CA  
3306 C C   . GLN B 89  ? 0.6659 0.5069 0.6810 -0.0435 0.0191  0.0283  59  GLN B C   
3307 O O   . GLN B 89  ? 0.6665 0.5188 0.6905 -0.0441 0.0227  0.0273  59  GLN B O   
3308 C CB  . GLN B 89  ? 0.6729 0.5126 0.6866 -0.0400 0.0189  0.0339  59  GLN B CB  
3309 C CG  . GLN B 89  ? 0.6956 0.5523 0.7199 -0.0365 0.0237  0.0319  59  GLN B CG  
3310 C CD  . GLN B 89  ? 0.7544 0.6203 0.7890 -0.0415 0.0249  0.0376  59  GLN B CD  
3311 O OE1 . GLN B 89  ? 0.7843 0.6486 0.8194 -0.0453 0.0233  0.0443  59  GLN B OE1 
3312 N NE2 . GLN B 89  ? 0.7507 0.6265 0.7931 -0.0416 0.0279  0.0351  59  GLN B NE2 
3313 N N   . GLN B 90  ? 0.6638 0.4949 0.6682 -0.0400 0.0170  0.0239  60  GLN B N   
3314 C CA  . GLN B 90  ? 0.6591 0.4951 0.6629 -0.0371 0.0194  0.0179  60  GLN B CA  
3315 C C   . GLN B 90  ? 0.6389 0.4771 0.6472 -0.0428 0.0199  0.0197  60  GLN B C   
3316 O O   . GLN B 90  ? 0.6357 0.4827 0.6487 -0.0421 0.0240  0.0167  60  GLN B O   
3317 C CB  . GLN B 90  ? 0.7025 0.5280 0.6928 -0.0313 0.0168  0.0132  60  GLN B CB  
3318 C CG  . GLN B 90  ? 0.7665 0.6000 0.7563 -0.0275 0.0200  0.0070  60  GLN B CG  
3319 C CD  . GLN B 90  ? 0.8629 0.6919 0.8407 -0.0186 0.0186  0.0015  60  GLN B CD  
3320 O OE1 . GLN B 90  ? 0.8911 0.7321 0.8712 -0.0126 0.0220  -0.0034 60  GLN B OE1 
3321 N NE2 . GLN B 90  ? 0.8843 0.6965 0.8487 -0.0172 0.0134  0.0016  60  GLN B NE2 
3322 N N   . VAL B 91  ? 0.6254 0.4561 0.6323 -0.0485 0.0157  0.0248  61  VAL B N   
3323 C CA  . VAL B 91  ? 0.6184 0.4519 0.6290 -0.0530 0.0158  0.0268  61  VAL B CA  
3324 C C   . VAL B 91  ? 0.6030 0.4494 0.6254 -0.0544 0.0202  0.0293  61  VAL B C   
3325 O O   . VAL B 91  ? 0.5988 0.4503 0.6242 -0.0542 0.0236  0.0278  61  VAL B O   
3326 C CB  . VAL B 91  ? 0.6326 0.4569 0.6389 -0.0587 0.0098  0.0309  61  VAL B CB  
3327 C CG1 . VAL B 91  ? 0.6352 0.4649 0.6460 -0.0622 0.0100  0.0332  61  VAL B CG1 
3328 C CG2 . VAL B 91  ? 0.6484 0.4575 0.6410 -0.0568 0.0052  0.0275  61  VAL B CG2 
3329 N N   . ILE B 92  ? 0.5923 0.4435 0.6205 -0.0551 0.0203  0.0329  62  ILE B N   
3330 C CA  . ILE B 92  ? 0.5830 0.4460 0.6213 -0.0551 0.0240  0.0350  62  ILE B CA  
3331 C C   . ILE B 92  ? 0.5845 0.4539 0.6258 -0.0509 0.0291  0.0294  62  ILE B C   
3332 O O   . ILE B 92  ? 0.5882 0.4625 0.6341 -0.0516 0.0322  0.0292  62  ILE B O   
3333 C CB  . ILE B 92  ? 0.5792 0.4464 0.6216 -0.0557 0.0232  0.0397  62  ILE B CB  
3334 C CG1 . ILE B 92  ? 0.5913 0.4531 0.6315 -0.0617 0.0181  0.0455  62  ILE B CG1 
3335 C CG2 . ILE B 92  ? 0.5741 0.4535 0.6257 -0.0544 0.0267  0.0415  62  ILE B CG2 
3336 C CD1 . ILE B 92  ? 0.6009 0.4654 0.6436 -0.0630 0.0175  0.0507  62  ILE B CD1 
3337 N N   . ALA B 93  ? 0.5788 0.4478 0.6168 -0.0467 0.0299  0.0247  63  ALA B N   
3338 C CA  . ALA B 93  ? 0.5723 0.4492 0.6136 -0.0434 0.0343  0.0186  63  ALA B CA  
3339 C C   . ALA B 93  ? 0.5700 0.4463 0.6098 -0.0451 0.0366  0.0157  63  ALA B C   
3340 O O   . ALA B 93  ? 0.5843 0.4669 0.6295 -0.0460 0.0407  0.0135  63  ALA B O   
3341 C CB  . ALA B 93  ? 0.5808 0.4579 0.6174 -0.0379 0.0337  0.0143  63  ALA B CB  
3342 N N   . THR B 94  ? 0.5559 0.4239 0.5879 -0.0459 0.0340  0.0161  64  THR B N   
3343 C CA  . THR B 94  ? 0.5436 0.4109 0.5731 -0.0473 0.0363  0.0142  64  THR B CA  
3344 C C   . THR B 94  ? 0.5314 0.3986 0.5650 -0.0513 0.0378  0.0185  64  THR B C   
3345 O O   . THR B 94  ? 0.5263 0.3963 0.5620 -0.0525 0.0422  0.0169  64  THR B O   
3346 C CB  . THR B 94  ? 0.5582 0.4161 0.5772 -0.0459 0.0323  0.0136  64  THR B CB  
3347 O OG1 . THR B 94  ? 0.5748 0.4342 0.5891 -0.0407 0.0324  0.0084  64  THR B OG1 
3348 C CG2 . THR B 94  ? 0.5586 0.4143 0.5738 -0.0475 0.0337  0.0136  64  THR B CG2 
3349 N N   . ALA B 95  ? 0.5265 0.3910 0.5612 -0.0532 0.0343  0.0239  65  ALA B N   
3350 C CA  . ALA B 95  ? 0.5244 0.3899 0.5623 -0.0555 0.0350  0.0282  65  ALA B CA  
3351 C C   . ALA B 95  ? 0.5150 0.3868 0.5598 -0.0547 0.0399  0.0271  65  ALA B C   
3352 O O   . ALA B 95  ? 0.5119 0.3823 0.5565 -0.0555 0.0429  0.0277  65  ALA B O   
3353 C CB  . ALA B 95  ? 0.5209 0.3863 0.5603 -0.0573 0.0303  0.0338  65  ALA B CB  
3354 N N   . THR B 96  ? 0.5039 0.3813 0.5533 -0.0527 0.0404  0.0253  66  THR B N   
3355 C CA  . THR B 96  ? 0.4961 0.3792 0.5514 -0.0515 0.0441  0.0233  66  THR B CA  
3356 C C   . THR B 96  ? 0.4972 0.3805 0.5522 -0.0527 0.0486  0.0179  66  THR B C   
3357 O O   . THR B 96  ? 0.5015 0.3838 0.5582 -0.0540 0.0519  0.0176  66  THR B O   
3358 C CB  . THR B 96  ? 0.4975 0.3870 0.5567 -0.0485 0.0433  0.0222  66  THR B CB  
3359 O OG1 . THR B 96  ? 0.4930 0.3823 0.5522 -0.0485 0.0395  0.0279  66  THR B OG1 
3360 C CG2 . THR B 96  ? 0.5017 0.3972 0.5666 -0.0467 0.0465  0.0197  66  THR B CG2 
3361 N N   . VAL B 97  ? 0.4870 0.3713 0.5391 -0.0523 0.0488  0.0138  67  VAL B N   
3362 C CA  . VAL B 97  ? 0.4718 0.3591 0.5243 -0.0542 0.0533  0.0088  67  VAL B CA  
3363 C C   . VAL B 97  ? 0.4681 0.3484 0.5167 -0.0576 0.0557  0.0115  67  VAL B C   
3364 O O   . VAL B 97  ? 0.4730 0.3534 0.5236 -0.0606 0.0602  0.0098  67  VAL B O   
3365 C CB  . VAL B 97  ? 0.4718 0.3640 0.5216 -0.0517 0.0528  0.0039  67  VAL B CB  
3366 C CG1 . VAL B 97  ? 0.4786 0.3770 0.5299 -0.0542 0.0578  -0.0010 67  VAL B CG1 
3367 C CG2 . VAL B 97  ? 0.4682 0.3668 0.5209 -0.0473 0.0508  0.0013  67  VAL B CG2 
3368 N N   . TYR B 98  ? 0.4595 0.3329 0.5021 -0.0574 0.0528  0.0159  68  TYR B N   
3369 C CA  . TYR B 98  ? 0.4589 0.3255 0.4966 -0.0595 0.0550  0.0189  68  TYR B CA  
3370 C C   . TYR B 98  ? 0.4557 0.3190 0.4957 -0.0605 0.0571  0.0218  68  TYR B C   
3371 O O   . TYR B 98  ? 0.4635 0.3220 0.5009 -0.0628 0.0615  0.0220  68  TYR B O   
3372 C CB  . TYR B 98  ? 0.4648 0.3257 0.4960 -0.0584 0.0504  0.0230  68  TYR B CB  
3373 C CG  . TYR B 98  ? 0.4719 0.3321 0.4974 -0.0568 0.0477  0.0206  68  TYR B CG  
3374 C CD1 . TYR B 98  ? 0.4837 0.3488 0.5086 -0.0561 0.0507  0.0154  68  TYR B CD1 
3375 C CD2 . TYR B 98  ? 0.4793 0.3340 0.4992 -0.0559 0.0420  0.0233  68  TYR B CD2 
3376 C CE1 . TYR B 98  ? 0.4932 0.3573 0.5114 -0.0531 0.0481  0.0130  68  TYR B CE1 
3377 C CE2 . TYR B 98  ? 0.4932 0.3450 0.5061 -0.0538 0.0392  0.0206  68  TYR B CE2 
3378 C CZ  . TYR B 98  ? 0.5027 0.3588 0.5142 -0.0517 0.0423  0.0155  68  TYR B CZ  
3379 O OH  . TYR B 98  ? 0.5181 0.3710 0.5213 -0.0482 0.0392  0.0127  68  TYR B OH  
3380 N N   . PHE B 99  ? 0.4463 0.3117 0.4901 -0.0583 0.0541  0.0242  69  PHE B N   
3381 C CA  . PHE B 99  ? 0.4548 0.3179 0.5000 -0.0573 0.0552  0.0269  69  PHE B CA  
3382 C C   . PHE B 99  ? 0.4629 0.3259 0.5111 -0.0589 0.0599  0.0224  69  PHE B C   
3383 O O   . PHE B 99  ? 0.4596 0.3146 0.5041 -0.0604 0.0633  0.0232  69  PHE B O   
3384 C CB  . PHE B 99  ? 0.4551 0.3240 0.5045 -0.0542 0.0511  0.0300  69  PHE B CB  
3385 C CG  . PHE B 99  ? 0.4683 0.3363 0.5181 -0.0514 0.0514  0.0335  69  PHE B CG  
3386 C CD1 . PHE B 99  ? 0.4798 0.3457 0.5259 -0.0498 0.0493  0.0389  69  PHE B CD1 
3387 C CD2 . PHE B 99  ? 0.4772 0.3470 0.5305 -0.0495 0.0536  0.0310  69  PHE B CD2 
3388 C CE1 . PHE B 99  ? 0.4877 0.3537 0.5332 -0.0457 0.0496  0.0420  69  PHE B CE1 
3389 C CE2 . PHE B 99  ? 0.4865 0.3547 0.5386 -0.0456 0.0538  0.0339  69  PHE B CE2 
3390 C CZ  . PHE B 99  ? 0.4854 0.3521 0.5335 -0.0434 0.0519  0.0396  69  PHE B CZ  
3391 N N   . LYS B 100 ? 0.4700 0.3411 0.5239 -0.0589 0.0599  0.0173  70  LYS B N   
3392 C CA  . LYS B 100 ? 0.4787 0.3521 0.5363 -0.0611 0.0636  0.0117  70  LYS B CA  
3393 C C   . LYS B 100 ? 0.4926 0.3615 0.5473 -0.0665 0.0683  0.0097  70  LYS B C   
3394 O O   . LYS B 100 ? 0.4986 0.3617 0.5528 -0.0696 0.0717  0.0083  70  LYS B O   
3395 C CB  . LYS B 100 ? 0.4869 0.3718 0.5503 -0.0595 0.0624  0.0063  70  LYS B CB  
3396 C CG  . LYS B 100 ? 0.5340 0.4238 0.6006 -0.0545 0.0589  0.0079  70  LYS B CG  
3397 C CD  . LYS B 100 ? 0.5904 0.4904 0.6621 -0.0528 0.0589  0.0016  70  LYS B CD  
3398 C CE  . LYS B 100 ? 0.6398 0.5447 0.7137 -0.0474 0.0558  0.0036  70  LYS B CE  
3399 N NZ  . LYS B 100 ? 0.6733 0.5755 0.7481 -0.0456 0.0559  0.0063  70  LYS B NZ  
3400 N N   . ARG B 101 ? 0.4982 0.3691 0.5501 -0.0676 0.0685  0.0097  71  ARG B N   
3401 C CA  . ARG B 101 ? 0.5083 0.3771 0.5571 -0.0726 0.0733  0.0085  71  ARG B CA  
3402 C C   . ARG B 101 ? 0.5294 0.3844 0.5712 -0.0744 0.0758  0.0137  71  ARG B C   
3403 O O   . ARG B 101 ? 0.5317 0.3817 0.5721 -0.0796 0.0808  0.0126  71  ARG B O   
3404 C CB  . ARG B 101 ? 0.5094 0.3828 0.5548 -0.0710 0.0720  0.0084  71  ARG B CB  
3405 C CG  . ARG B 101 ? 0.5211 0.4077 0.5714 -0.0696 0.0712  0.0024  71  ARG B CG  
3406 C CD  . ARG B 101 ? 0.5526 0.4420 0.5975 -0.0674 0.0704  0.0021  71  ARG B CD  
3407 N NE  . ARG B 101 ? 0.5621 0.4635 0.6098 -0.0640 0.0691  -0.0035 71  ARG B NE  
3408 C CZ  . ARG B 101 ? 0.5537 0.4590 0.5962 -0.0605 0.0681  -0.0052 71  ARG B CZ  
3409 N NH1 . ARG B 101 ? 0.5294 0.4280 0.5643 -0.0604 0.0683  -0.0018 71  ARG B NH1 
3410 N NH2 . ARG B 101 ? 0.5367 0.4527 0.5809 -0.0561 0.0667  -0.0104 71  ARG B NH2 
3411 N N   . PHE B 102 ? 0.5429 0.3918 0.5799 -0.0701 0.0724  0.0193  72  PHE B N   
3412 C CA  . PHE B 102 ? 0.5592 0.3953 0.5883 -0.0699 0.0743  0.0245  72  PHE B CA  
3413 C C   . PHE B 102 ? 0.5667 0.3949 0.5957 -0.0708 0.0767  0.0240  72  PHE B C   
3414 O O   . PHE B 102 ? 0.5757 0.3927 0.5986 -0.0742 0.0812  0.0252  72  PHE B O   
3415 C CB  . PHE B 102 ? 0.5622 0.3965 0.5871 -0.0646 0.0693  0.0300  72  PHE B CB  
3416 C CG  . PHE B 102 ? 0.5864 0.4086 0.6018 -0.0630 0.0711  0.0353  72  PHE B CG  
3417 C CD1 . PHE B 102 ? 0.6069 0.4239 0.6146 -0.0641 0.0733  0.0375  72  PHE B CD1 
3418 C CD2 . PHE B 102 ? 0.6055 0.4213 0.6186 -0.0594 0.0707  0.0381  72  PHE B CD2 
3419 C CE1 . PHE B 102 ? 0.6263 0.4315 0.6239 -0.0618 0.0751  0.0426  72  PHE B CE1 
3420 C CE2 . PHE B 102 ? 0.6254 0.4292 0.6282 -0.0566 0.0723  0.0429  72  PHE B CE2 
3421 C CZ  . PHE B 102 ? 0.6290 0.4273 0.6240 -0.0579 0.0745  0.0453  72  PHE B CZ  
3422 N N   . TYR B 103 ? 0.5618 0.3950 0.5967 -0.0678 0.0739  0.0221  73  TYR B N   
3423 C CA  . TYR B 103 ? 0.5703 0.3954 0.6040 -0.0674 0.0755  0.0211  73  TYR B CA  
3424 C C   . TYR B 103 ? 0.5816 0.4081 0.6200 -0.0736 0.0790  0.0141  73  TYR B C   
3425 O O   . TYR B 103 ? 0.5887 0.4061 0.6249 -0.0743 0.0805  0.0125  73  TYR B O   
3426 C CB  . TYR B 103 ? 0.5674 0.3965 0.6035 -0.0603 0.0712  0.0229  73  TYR B CB  
3427 C CG  . TYR B 103 ? 0.5816 0.4079 0.6120 -0.0552 0.0685  0.0298  73  TYR B CG  
3428 C CD1 . TYR B 103 ? 0.6024 0.4151 0.6230 -0.0532 0.0704  0.0337  73  TYR B CD1 
3429 C CD2 . TYR B 103 ? 0.5895 0.4267 0.6238 -0.0528 0.0640  0.0323  73  TYR B CD2 
3430 C CE1 . TYR B 103 ? 0.6200 0.4322 0.6354 -0.0480 0.0677  0.0397  73  TYR B CE1 
3431 C CE2 . TYR B 103 ? 0.6046 0.4411 0.6345 -0.0490 0.0611  0.0381  73  TYR B CE2 
3432 C CZ  . TYR B 103 ? 0.6272 0.4525 0.6481 -0.0462 0.0629  0.0416  73  TYR B CZ  
3433 O OH  . TYR B 103 ? 0.6506 0.4775 0.6674 -0.0418 0.0597  0.0470  73  TYR B OH  
3434 N N   . ALA B 104 ? 0.5835 0.4209 0.6274 -0.0781 0.0803  0.0100  74  ALA B N   
3435 C CA  . ALA B 104 ? 0.5902 0.4313 0.6388 -0.0852 0.0839  0.0034  74  ALA B CA  
3436 C C   . ALA B 104 ? 0.6139 0.4417 0.6555 -0.0924 0.0896  0.0054  74  ALA B C   
3437 O O   . ALA B 104 ? 0.6161 0.4379 0.6580 -0.0987 0.0928  0.0018  74  ALA B O   
3438 C CB  . ALA B 104 ? 0.5808 0.4393 0.6365 -0.0865 0.0835  -0.0011 74  ALA B CB  
3439 N N   . ARG B 105 ? 0.6339 0.4563 0.6684 -0.0917 0.0909  0.0112  75  ARG B N   
3440 C CA  . ARG B 105 ? 0.6690 0.4780 0.6953 -0.0978 0.0967  0.0143  75  ARG B CA  
3441 C C   . ARG B 105 ? 0.6873 0.4763 0.7021 -0.0936 0.0967  0.0205  75  ARG B C   
3442 O O   . ARG B 105 ? 0.7040 0.4772 0.7112 -0.0987 0.1014  0.0220  75  ARG B O   
3443 C CB  . ARG B 105 ? 0.7088 0.5248 0.7333 -0.0997 0.0991  0.0163  75  ARG B CB  
3444 C CG  . ARG B 105 ? 0.7823 0.6148 0.8156 -0.1067 0.1021  0.0100  75  ARG B CG  
3445 C CD  . ARG B 105 ? 0.8587 0.7023 0.8912 -0.1055 0.1029  0.0111  75  ARG B CD  
3446 N NE  . ARG B 105 ? 0.9439 0.7766 0.9664 -0.1082 0.1078  0.0170  75  ARG B NE  
3447 C CZ  . ARG B 105 ? 0.9978 0.8374 1.0168 -0.1072 0.1096  0.0189  75  ARG B CZ  
3448 N NH1 . ARG B 105 ? 1.0145 0.8433 1.0234 -0.1093 0.1143  0.0247  75  ARG B NH1 
3449 N NH2 . ARG B 105 ? 0.9928 0.8494 1.0171 -0.1033 0.1065  0.0150  75  ARG B NH2 
3450 N N   . TYR B 106 ? 0.6842 0.4737 0.6972 -0.0844 0.0916  0.0240  76  TYR B N   
3451 C CA  . TYR B 106 ? 0.6999 0.4730 0.7016 -0.0788 0.0912  0.0300  76  TYR B CA  
3452 C C   . TYR B 106 ? 0.6983 0.4692 0.7009 -0.0724 0.0876  0.0292  76  TYR B C   
3453 O O   . TYR B 106 ? 0.6935 0.4773 0.7058 -0.0709 0.0843  0.0250  76  TYR B O   
3454 C CB  . TYR B 106 ? 0.7092 0.4841 0.7055 -0.0733 0.0890  0.0359  76  TYR B CB  
3455 C CG  . TYR B 106 ? 0.7335 0.5088 0.7267 -0.0789 0.0933  0.0369  76  TYR B CG  
3456 C CD1 . TYR B 106 ? 0.7612 0.5203 0.7432 -0.0820 0.0989  0.0408  76  TYR B CD1 
3457 C CD2 . TYR B 106 ? 0.7454 0.5369 0.7465 -0.0813 0.0923  0.0335  76  TYR B CD2 
3458 C CE1 . TYR B 106 ? 0.7812 0.5421 0.7606 -0.0874 0.1036  0.0418  76  TYR B CE1 
3459 C CE2 . TYR B 106 ? 0.7640 0.5576 0.7624 -0.0859 0.0966  0.0339  76  TYR B CE2 
3460 C CZ  . TYR B 106 ? 0.7926 0.5717 0.7805 -0.0892 0.1024  0.0382  76  TYR B CZ  
3461 O OH  . TYR B 106 ? 0.8289 0.6117 0.8143 -0.0938 0.1072  0.0390  76  TYR B OH  
3462 N N   . SER B 107 ? 0.6994 0.4528 0.6905 -0.0680 0.0884  0.0332  77  SER B N   
3463 C CA  . SER B 107 ? 0.6970 0.4465 0.6863 -0.0605 0.0854  0.0329  77  SER B CA  
3464 C C   . SER B 107 ? 0.6858 0.4475 0.6773 -0.0510 0.0800  0.0371  77  SER B C   
3465 O O   . SER B 107 ? 0.6869 0.4515 0.6755 -0.0493 0.0790  0.0417  77  SER B O   
3466 C CB  . SER B 107 ? 0.7269 0.4516 0.7013 -0.0588 0.0886  0.0355  77  SER B CB  
3467 O OG  . SER B 107 ? 0.7623 0.4822 0.7309 -0.0481 0.0852  0.0373  77  SER B OG  
3468 N N   . LEU B 108 ? 0.6710 0.4395 0.6667 -0.0447 0.0764  0.0357  78  LEU B N   
3469 C CA  . LEU B 108 ? 0.6576 0.4391 0.6560 -0.0362 0.0715  0.0397  78  LEU B CA  
3470 C C   . LEU B 108 ? 0.6565 0.4293 0.6433 -0.0289 0.0709  0.0462  78  LEU B C   
3471 O O   . LEU B 108 ? 0.6579 0.4436 0.6473 -0.0231 0.0668  0.0500  78  LEU B O   
3472 C CB  . LEU B 108 ? 0.6542 0.4433 0.6580 -0.0307 0.0689  0.0370  78  LEU B CB  
3473 C CG  . LEU B 108 ? 0.6669 0.4699 0.6833 -0.0355 0.0681  0.0313  78  LEU B CG  
3474 C CD1 . LEU B 108 ? 0.6738 0.4766 0.6915 -0.0316 0.0675  0.0270  78  LEU B CD1 
3475 C CD2 . LEU B 108 ? 0.6631 0.4852 0.6887 -0.0349 0.0643  0.0337  78  LEU B CD2 
3476 N N   . LYS B 109 ? 0.6534 0.4051 0.6270 -0.0291 0.0749  0.0476  79  LYS B N   
3477 C CA  . LYS B 109 ? 0.6574 0.4001 0.6184 -0.0211 0.0746  0.0538  79  LYS B CA  
3478 C C   . LYS B 109 ? 0.6487 0.3916 0.6066 -0.0245 0.0756  0.0573  79  LYS B C   
3479 O O   . LYS B 109 ? 0.6557 0.4002 0.6071 -0.0172 0.0733  0.0622  79  LYS B O   
3480 C CB  . LYS B 109 ? 0.6987 0.4163 0.6440 -0.0171 0.0779  0.0544  79  LYS B CB  
3481 C CG  . LYS B 109 ? 0.7648 0.4624 0.7029 -0.0269 0.0839  0.0532  79  LYS B CG  
3482 C CD  . LYS B 109 ? 0.8429 0.5128 0.7617 -0.0220 0.0870  0.0562  79  LYS B CD  
3483 C CE  . LYS B 109 ? 0.9210 0.5721 0.8351 -0.0342 0.0932  0.0541  79  LYS B CE  
3484 N NZ  . LYS B 109 ? 0.9807 0.6087 0.8765 -0.0331 0.0977  0.0602  79  LYS B NZ  
3485 N N   . SER B 110 ? 0.6332 0.3762 0.5956 -0.0347 0.0788  0.0546  80  SER B N   
3486 C CA  . SER B 110 ? 0.6273 0.3703 0.5860 -0.0376 0.0801  0.0575  80  SER B CA  
3487 C C   . SER B 110 ? 0.6084 0.3680 0.5712 -0.0324 0.0742  0.0603  80  SER B C   
3488 O O   . SER B 110 ? 0.6112 0.3671 0.5646 -0.0266 0.0732  0.0650  80  SER B O   
3489 C CB  . SER B 110 ? 0.6417 0.3871 0.6067 -0.0486 0.0839  0.0534  80  SER B CB  
3490 O OG  . SER B 110 ? 0.6641 0.4270 0.6436 -0.0516 0.0809  0.0484  80  SER B OG  
3491 N N   . ILE B 111 ? 0.5891 0.3667 0.5653 -0.0342 0.0701  0.0574  81  ILE B N   
3492 C CA  . ILE B 111 ? 0.5754 0.3689 0.5568 -0.0307 0.0640  0.0595  81  ILE B CA  
3493 C C   . ILE B 111 ? 0.5651 0.3711 0.5560 -0.0276 0.0604  0.0585  81  ILE B C   
3494 O O   . ILE B 111 ? 0.5626 0.3696 0.5599 -0.0308 0.0620  0.0543  81  ILE B O   
3495 C CB  . ILE B 111 ? 0.5711 0.3729 0.5578 -0.0367 0.0625  0.0577  81  ILE B CB  
3496 C CG1 . ILE B 111 ? 0.5902 0.3818 0.5661 -0.0376 0.0655  0.0598  81  ILE B CG1 
3497 C CG2 . ILE B 111 ? 0.5671 0.3848 0.5607 -0.0348 0.0556  0.0589  81  ILE B CG2 
3498 C CD1 . ILE B 111 ? 0.6018 0.3994 0.5804 -0.0424 0.0647  0.0577  81  ILE B CD1 
3499 N N   . ASP B 112 ? 0.5554 0.3720 0.5471 -0.0211 0.0558  0.0622  82  ASP B N   
3500 C CA  . ASP B 112 ? 0.5472 0.3783 0.5479 -0.0179 0.0525  0.0623  82  ASP B CA  
3501 C C   . ASP B 112 ? 0.5475 0.3904 0.5603 -0.0249 0.0505  0.0593  82  ASP B C   
3502 O O   . ASP B 112 ? 0.5439 0.3932 0.5593 -0.0284 0.0474  0.0600  82  ASP B O   
3503 C CB  . ASP B 112 ? 0.5520 0.3955 0.5521 -0.0111 0.0478  0.0672  82  ASP B CB  
3504 C CG  . ASP B 112 ? 0.5893 0.4505 0.5988 -0.0076 0.0446  0.0683  82  ASP B CG  
3505 O OD1 . ASP B 112 ? 0.5977 0.4592 0.6122 -0.0085 0.0463  0.0654  82  ASP B OD1 
3506 O OD2 . ASP B 112 ? 0.5972 0.4730 0.6091 -0.0040 0.0404  0.0720  82  ASP B OD2 
3507 N N   . PRO B 113 ? 0.5524 0.3976 0.5716 -0.0263 0.0518  0.0557  83  PRO B N   
3508 C CA  . PRO B 113 ? 0.5469 0.4030 0.5765 -0.0316 0.0499  0.0532  83  PRO B CA  
3509 C C   . PRO B 113 ? 0.5434 0.4150 0.5793 -0.0312 0.0446  0.0569  83  PRO B C   
3510 O O   . PRO B 113 ? 0.5472 0.4238 0.5881 -0.0363 0.0424  0.0558  83  PRO B O   
3511 C CB  . PRO B 113 ? 0.5537 0.4104 0.5875 -0.0304 0.0520  0.0495  83  PRO B CB  
3512 C CG  . PRO B 113 ? 0.5638 0.4133 0.5905 -0.0232 0.0536  0.0510  83  PRO B CG  
3513 C CD  . PRO B 113 ? 0.5514 0.3886 0.5676 -0.0224 0.0550  0.0537  83  PRO B CD  
3514 N N   . VAL B 114 ? 0.5369 0.4160 0.5719 -0.0253 0.0424  0.0613  84  VAL B N   
3515 C CA  . VAL B 114 ? 0.5318 0.4273 0.5730 -0.0257 0.0373  0.0653  84  VAL B CA  
3516 C C   . VAL B 114 ? 0.5326 0.4269 0.5714 -0.0303 0.0341  0.0662  84  VAL B C   
3517 O O   . VAL B 114 ? 0.5389 0.4431 0.5836 -0.0349 0.0299  0.0675  84  VAL B O   
3518 C CB  . VAL B 114 ? 0.5405 0.4463 0.5812 -0.0173 0.0362  0.0694  84  VAL B CB  
3519 C CG1 . VAL B 114 ? 0.5380 0.4634 0.5860 -0.0188 0.0311  0.0738  84  VAL B CG1 
3520 C CG2 . VAL B 114 ? 0.5480 0.4552 0.5909 -0.0126 0.0389  0.0679  84  VAL B CG2 
3521 N N   . LEU B 115 ? 0.5264 0.4075 0.5557 -0.0295 0.0361  0.0653  85  LEU B N   
3522 C CA  . LEU B 115 ? 0.5246 0.4027 0.5499 -0.0330 0.0335  0.0654  85  LEU B CA  
3523 C C   . LEU B 115 ? 0.5280 0.3981 0.5538 -0.0394 0.0352  0.0609  85  LEU B C   
3524 O O   . LEU B 115 ? 0.5296 0.4013 0.5560 -0.0436 0.0316  0.0600  85  LEU B O   
3525 C CB  . LEU B 115 ? 0.5327 0.4009 0.5464 -0.0279 0.0354  0.0671  85  LEU B CB  
3526 C CG  . LEU B 115 ? 0.5543 0.4163 0.5612 -0.0304 0.0340  0.0665  85  LEU B CG  
3527 C CD1 . LEU B 115 ? 0.5551 0.4295 0.5658 -0.0324 0.0269  0.0679  85  LEU B CD1 
3528 C CD2 . LEU B 115 ? 0.5699 0.4213 0.5645 -0.0244 0.0368  0.0688  85  LEU B CD2 
3529 N N   . MET B 116 ? 0.5279 0.3898 0.5530 -0.0398 0.0405  0.0577  86  MET B N   
3530 C CA  . MET B 116 ? 0.5260 0.3824 0.5517 -0.0447 0.0429  0.0530  86  MET B CA  
3531 C C   . MET B 116 ? 0.5241 0.3887 0.5577 -0.0482 0.0397  0.0512  86  MET B C   
3532 O O   . MET B 116 ? 0.5316 0.3941 0.5637 -0.0514 0.0381  0.0490  86  MET B O   
3533 C CB  . MET B 116 ? 0.5293 0.3776 0.5537 -0.0446 0.0489  0.0501  86  MET B CB  
3534 C CG  . MET B 116 ? 0.5549 0.3997 0.5801 -0.0495 0.0520  0.0451  86  MET B CG  
3535 S SD  . MET B 116 ? 0.5803 0.4198 0.5980 -0.0520 0.0522  0.0448  86  MET B SD  
3536 C CE  . MET B 116 ? 0.5767 0.4035 0.5848 -0.0509 0.0578  0.0470  86  MET B CE  
3537 N N   . ALA B 117 ? 0.5126 0.3860 0.5533 -0.0469 0.0386  0.0523  87  ALA B N   
3538 C CA  . ALA B 117 ? 0.5076 0.3876 0.5547 -0.0499 0.0360  0.0514  87  ALA B CA  
3539 C C   . ALA B 117 ? 0.5104 0.3918 0.5565 -0.0537 0.0305  0.0529  87  ALA B C   
3540 O O   . ALA B 117 ? 0.5116 0.3887 0.5565 -0.0565 0.0297  0.0498  87  ALA B O   
3541 C CB  . ALA B 117 ? 0.5009 0.3911 0.5549 -0.0473 0.0358  0.0536  87  ALA B CB  
3542 N N   . PRO B 118 ? 0.5105 0.3973 0.5564 -0.0538 0.0264  0.0572  88  PRO B N   
3543 C CA  . PRO B 118 ? 0.5079 0.3944 0.5523 -0.0585 0.0208  0.0578  88  PRO B CA  
3544 C C   . PRO B 118 ? 0.5150 0.3904 0.5505 -0.0590 0.0206  0.0545  88  PRO B C   
3545 O O   . PRO B 118 ? 0.5180 0.3892 0.5506 -0.0624 0.0166  0.0529  88  PRO B O   
3546 C CB  . PRO B 118 ? 0.5129 0.4105 0.5601 -0.0582 0.0169  0.0627  88  PRO B CB  
3547 C CG  . PRO B 118 ? 0.5208 0.4199 0.5663 -0.0516 0.0209  0.0641  88  PRO B CG  
3548 C CD  . PRO B 118 ? 0.5020 0.3960 0.5487 -0.0494 0.0265  0.0612  88  PRO B CD  
3549 N N   . THR B 119 ? 0.5123 0.3820 0.5425 -0.0553 0.0250  0.0537  89  THR B N   
3550 C CA  . THR B 119 ? 0.5158 0.3760 0.5375 -0.0553 0.0260  0.0509  89  THR B CA  
3551 C C   . THR B 119 ? 0.5202 0.3762 0.5420 -0.0573 0.0277  0.0462  89  THR B C   
3552 O O   . THR B 119 ? 0.5325 0.3839 0.5491 -0.0585 0.0248  0.0439  89  THR B O   
3553 C CB  . THR B 119 ? 0.5263 0.3809 0.5424 -0.0517 0.0314  0.0516  89  THR B CB  
3554 O OG1 . THR B 119 ? 0.5429 0.4012 0.5572 -0.0483 0.0294  0.0559  89  THR B OG1 
3555 C CG2 . THR B 119 ? 0.5281 0.3744 0.5356 -0.0517 0.0333  0.0493  89  THR B CG2 
3556 N N   . CYS B 120 ? 0.5089 0.3672 0.5363 -0.0570 0.0318  0.0445  90  CYS B N   
3557 C CA  . CYS B 120 ? 0.5140 0.3710 0.5423 -0.0578 0.0334  0.0398  90  CYS B CA  
3558 C C   . CYS B 120 ? 0.5200 0.3769 0.5482 -0.0596 0.0279  0.0394  90  CYS B C   
3559 O O   . CYS B 120 ? 0.5311 0.3831 0.5542 -0.0593 0.0272  0.0357  90  CYS B O   
3560 C CB  . CYS B 120 ? 0.5223 0.3835 0.5571 -0.0570 0.0379  0.0381  90  CYS B CB  
3561 S SG  . CYS B 120 ? 0.5797 0.4366 0.6124 -0.0564 0.0449  0.0366  90  CYS B SG  
3562 N N   . VAL B 121 ? 0.5108 0.3726 0.5437 -0.0613 0.0241  0.0433  91  VAL B N   
3563 C CA  . VAL B 121 ? 0.5100 0.3697 0.5421 -0.0642 0.0188  0.0437  91  VAL B CA  
3564 C C   . VAL B 121 ? 0.5173 0.3687 0.5406 -0.0658 0.0141  0.0425  91  VAL B C   
3565 O O   . VAL B 121 ? 0.5193 0.3629 0.5368 -0.0658 0.0120  0.0392  91  VAL B O   
3566 C CB  . VAL B 121 ? 0.5087 0.3771 0.5481 -0.0668 0.0162  0.0490  91  VAL B CB  
3567 C CG1 . VAL B 121 ? 0.5146 0.3793 0.5521 -0.0718 0.0102  0.0505  91  VAL B CG1 
3568 C CG2 . VAL B 121 ? 0.5057 0.3812 0.5523 -0.0645 0.0203  0.0494  91  VAL B CG2 
3569 N N   . PHE B 122 ? 0.5250 0.3778 0.5465 -0.0660 0.0125  0.0446  92  PHE B N   
3570 C CA  . PHE B 122 ? 0.5442 0.3903 0.5571 -0.0667 0.0078  0.0434  92  PHE B CA  
3571 C C   . PHE B 122 ? 0.5506 0.3880 0.5547 -0.0635 0.0099  0.0384  92  PHE B C   
3572 O O   . PHE B 122 ? 0.5636 0.3930 0.5606 -0.0640 0.0055  0.0356  92  PHE B O   
3573 C CB  . PHE B 122 ? 0.5520 0.4034 0.5648 -0.0656 0.0073  0.0467  92  PHE B CB  
3574 C CG  . PHE B 122 ? 0.5704 0.4165 0.5738 -0.0645 0.0037  0.0454  92  PHE B CG  
3575 C CD1 . PHE B 122 ? 0.5823 0.4262 0.5827 -0.0684 -0.0041 0.0450  92  PHE B CD1 
3576 C CD2 . PHE B 122 ? 0.5874 0.4311 0.5849 -0.0599 0.0079  0.0450  92  PHE B CD2 
3577 C CE1 . PHE B 122 ? 0.5981 0.4377 0.5894 -0.0669 -0.0080 0.0434  92  PHE B CE1 
3578 C CE2 . PHE B 122 ? 0.6041 0.4439 0.5924 -0.0581 0.0045  0.0442  92  PHE B CE2 
3579 C CZ  . PHE B 122 ? 0.6029 0.4409 0.5882 -0.0612 -0.0036 0.0430  92  PHE B CZ  
3580 N N   . LEU B 123 ? 0.5392 0.3781 0.5435 -0.0603 0.0167  0.0370  93  LEU B N   
3581 C CA  . LEU B 123 ? 0.5372 0.3713 0.5345 -0.0574 0.0196  0.0325  93  LEU B CA  
3582 C C   . LEU B 123 ? 0.5547 0.3872 0.5521 -0.0566 0.0193  0.0287  93  LEU B C   
3583 O O   . LEU B 123 ? 0.5639 0.3903 0.5528 -0.0542 0.0171  0.0251  93  LEU B O   
3584 C CB  . LEU B 123 ? 0.5213 0.3587 0.5203 -0.0558 0.0273  0.0326  93  LEU B CB  
3585 C CG  . LEU B 123 ? 0.5152 0.3510 0.5082 -0.0534 0.0314  0.0286  93  LEU B CG  
3586 C CD1 . LEU B 123 ? 0.5109 0.3410 0.4931 -0.0512 0.0281  0.0282  93  LEU B CD1 
3587 C CD2 . LEU B 123 ? 0.5211 0.3599 0.5170 -0.0540 0.0392  0.0293  93  LEU B CD2 
3588 N N   . ALA B 124 ? 0.5585 0.3962 0.5642 -0.0576 0.0211  0.0293  94  ALA B N   
3589 C CA  . ALA B 124 ? 0.5765 0.4131 0.5817 -0.0558 0.0209  0.0259  94  ALA B CA  
3590 C C   . ALA B 124 ? 0.5982 0.4249 0.5958 -0.0563 0.0140  0.0254  94  ALA B C   
3591 O O   . ALA B 124 ? 0.6029 0.4245 0.5938 -0.0527 0.0132  0.0214  94  ALA B O   
3592 C CB  . ALA B 124 ? 0.5758 0.4198 0.5908 -0.0565 0.0234  0.0273  94  ALA B CB  
3593 N N   . SER B 125 ? 0.6054 0.4291 0.6030 -0.0608 0.0087  0.0294  95  SER B N   
3594 C CA  . SER B 125 ? 0.6200 0.4322 0.6096 -0.0629 0.0015  0.0289  95  SER B CA  
3595 C C   . SER B 125 ? 0.6216 0.4244 0.5988 -0.0598 -0.0014 0.0248  95  SER B C   
3596 O O   . SER B 125 ? 0.6327 0.4235 0.6004 -0.0590 -0.0062 0.0223  95  SER B O   
3597 C CB  . SER B 125 ? 0.6455 0.4593 0.6396 -0.0697 -0.0034 0.0341  95  SER B CB  
3598 O OG  . SER B 125 ? 0.6812 0.5062 0.6870 -0.0716 -0.0001 0.0382  95  SER B OG  
3599 N N   . LYS B 126 ? 0.6134 0.4205 0.5895 -0.0577 0.0014  0.0243  96  LYS B N   
3600 C CA  . LYS B 126 ? 0.6250 0.4248 0.5890 -0.0539 -0.0008 0.0207  96  LYS B CA  
3601 C C   . LYS B 126 ? 0.6422 0.4415 0.6010 -0.0475 0.0031  0.0157  96  LYS B C   
3602 O O   . LYS B 126 ? 0.6514 0.4408 0.5985 -0.0436 -0.0009 0.0118  96  LYS B O   
3603 C CB  . LYS B 126 ? 0.6332 0.4380 0.5972 -0.0536 0.0010  0.0226  96  LYS B CB  
3604 C CG  . LYS B 126 ? 0.6666 0.4733 0.6348 -0.0588 -0.0039 0.0269  96  LYS B CG  
3605 C CD  . LYS B 126 ? 0.6986 0.5067 0.6618 -0.0569 -0.0046 0.0277  96  LYS B CD  
3606 C CE  . LYS B 126 ? 0.7201 0.5375 0.6902 -0.0559 0.0021  0.0314  96  LYS B CE  
3607 N NZ  . LYS B 126 ? 0.7487 0.5676 0.7143 -0.0546 0.0000  0.0335  96  LYS B NZ  
3608 N N   . VAL B 127 ? 0.6445 0.4546 0.6117 -0.0463 0.0105  0.0157  97  VAL B N   
3609 C CA  . VAL B 127 ? 0.6537 0.4682 0.6189 -0.0409 0.0151  0.0110  97  VAL B CA  
3610 C C   . VAL B 127 ? 0.6734 0.4808 0.6335 -0.0379 0.0112  0.0083  97  VAL B C   
3611 O O   . VAL B 127 ? 0.6815 0.4836 0.6308 -0.0318 0.0096  0.0038  97  VAL B O   
3612 C CB  . VAL B 127 ? 0.6474 0.4752 0.6245 -0.0424 0.0230  0.0117  97  VAL B CB  
3613 C CG1 . VAL B 127 ? 0.6515 0.4866 0.6279 -0.0375 0.0273  0.0065  97  VAL B CG1 
3614 C CG2 . VAL B 127 ? 0.6454 0.4772 0.6253 -0.0450 0.0270  0.0148  97  VAL B CG2 
3615 N N   . GLU B 128 ? 0.6811 0.4871 0.6475 -0.0419 0.0093  0.0113  98  GLU B N   
3616 C CA  . GLU B 128 ? 0.6964 0.4943 0.6578 -0.0395 0.0060  0.0099  98  GLU B CA  
3617 C C   . GLU B 128 ? 0.7258 0.5056 0.6744 -0.0402 -0.0021 0.0097  98  GLU B C   
3618 O O   . GLU B 128 ? 0.7325 0.5026 0.6765 -0.0398 -0.0053 0.0099  98  GLU B O   
3619 C CB  . GLU B 128 ? 0.7004 0.5044 0.6731 -0.0433 0.0078  0.0137  98  GLU B CB  
3620 C CG  . GLU B 128 ? 0.6935 0.5136 0.6776 -0.0421 0.0151  0.0129  98  GLU B CG  
3621 C CD  . GLU B 128 ? 0.7209 0.5463 0.7033 -0.0353 0.0182  0.0076  98  GLU B CD  
3622 O OE1 . GLU B 128 ? 0.7614 0.5776 0.7343 -0.0308 0.0146  0.0056  98  GLU B OE1 
3623 O OE2 . GLU B 128 ? 0.6992 0.5379 0.6894 -0.0345 0.0240  0.0054  98  GLU B OE2 
3624 N N   . GLU B 129 ? 0.7440 0.5183 0.6859 -0.0411 -0.0055 0.0091  99  GLU B N   
3625 C CA  . GLU B 129 ? 0.7748 0.5311 0.7032 -0.0418 -0.0138 0.0077  99  GLU B CA  
3626 C C   . GLU B 129 ? 0.7914 0.5387 0.7218 -0.0502 -0.0194 0.0120  99  GLU B C   
3627 O O   . GLU B 129 ? 0.8010 0.5306 0.7193 -0.0512 -0.0263 0.0105  99  GLU B O   
3628 C CB  . GLU B 129 ? 0.8212 0.5661 0.7343 -0.0326 -0.0157 0.0019  99  GLU B CB  
3629 C CG  . GLU B 129 ? 0.9044 0.6583 0.8134 -0.0243 -0.0112 -0.0026 99  GLU B CG  
3630 C CD  . GLU B 129 ? 1.0279 0.7681 0.9190 -0.0182 -0.0167 -0.0073 99  GLU B CD  
3631 O OE1 . GLU B 129 ? 1.0345 0.7784 0.9237 -0.0178 -0.0165 -0.0077 99  GLU B OE1 
3632 O OE2 . GLU B 129 ? 1.0877 0.8121 0.9655 -0.0132 -0.0216 -0.0105 99  GLU B OE2 
3633 N N   . PHE B 130 ? 0.7892 0.5486 0.7343 -0.0564 -0.0165 0.0173  100 PHE B N   
3634 C CA  . PHE B 130 ? 0.7987 0.5543 0.7482 -0.0652 -0.0207 0.0224  100 PHE B CA  
3635 C C   . PHE B 130 ? 0.7870 0.5399 0.7350 -0.0715 -0.0267 0.0235  100 PHE B C   
3636 O O   . PHE B 130 ? 0.8007 0.5402 0.7419 -0.0771 -0.0337 0.0239  100 PHE B O   
3637 C CB  . PHE B 130 ? 0.8056 0.5779 0.7713 -0.0681 -0.0151 0.0273  100 PHE B CB  
3638 C CG  . PHE B 130 ? 0.8389 0.6073 0.8061 -0.0702 -0.0152 0.0303  100 PHE B CG  
3639 C CD1 . PHE B 130 ? 0.8587 0.6260 0.8304 -0.0792 -0.0188 0.0359  100 PHE B CD1 
3640 C CD2 . PHE B 130 ? 0.8603 0.6265 0.8238 -0.0630 -0.0118 0.0275  100 PHE B CD2 
3641 C CE1 . PHE B 130 ? 0.8743 0.6376 0.8466 -0.0811 -0.0184 0.0393  100 PHE B CE1 
3642 C CE2 . PHE B 130 ? 0.8760 0.6379 0.8395 -0.0640 -0.0118 0.0305  100 PHE B CE2 
3643 C CZ  . PHE B 130 ? 0.8758 0.6355 0.8434 -0.0731 -0.0149 0.0367  100 PHE B CZ  
3644 N N   . GLY B 131 ? 0.7656 0.5302 0.7187 -0.0704 -0.0242 0.0238  101 GLY B N   
3645 C CA  . GLY B 131 ? 0.7606 0.5251 0.7122 -0.0749 -0.0297 0.0245  101 GLY B CA  
3646 C C   . GLY B 131 ? 0.7456 0.5274 0.7078 -0.0751 -0.0255 0.0277  101 GLY B C   
3647 O O   . GLY B 131 ? 0.7413 0.5337 0.7115 -0.0719 -0.0181 0.0292  101 GLY B O   
3648 N N   . VAL B 132 ? 0.7358 0.5195 0.6970 -0.0784 -0.0305 0.0285  102 VAL B N   
3649 C CA  . VAL B 132 ? 0.7238 0.5224 0.6930 -0.0779 -0.0276 0.0318  102 VAL B CA  
3650 C C   . VAL B 132 ? 0.7176 0.5259 0.6976 -0.0861 -0.0308 0.0368  102 VAL B C   
3651 O O   . VAL B 132 ? 0.7187 0.5231 0.6963 -0.0925 -0.0385 0.0367  102 VAL B O   
3652 C CB  . VAL B 132 ? 0.7289 0.5252 0.6889 -0.0747 -0.0311 0.0292  102 VAL B CB  
3653 C CG1 . VAL B 132 ? 0.7268 0.5377 0.6939 -0.0740 -0.0289 0.0331  102 VAL B CG1 
3654 C CG2 . VAL B 132 ? 0.7367 0.5251 0.6857 -0.0665 -0.0275 0.0245  102 VAL B CG2 
3655 N N   . VAL B 133 ? 0.7088 0.5299 0.7008 -0.0861 -0.0251 0.0412  103 VAL B N   
3656 C CA  . VAL B 133 ? 0.7006 0.5344 0.7037 -0.0927 -0.0271 0.0465  103 VAL B CA  
3657 C C   . VAL B 133 ? 0.7028 0.5469 0.7072 -0.0931 -0.0306 0.0477  103 VAL B C   
3658 O O   . VAL B 133 ? 0.7060 0.5530 0.7077 -0.0862 -0.0271 0.0470  103 VAL B O   
3659 C CB  . VAL B 133 ? 0.6965 0.5416 0.7103 -0.0905 -0.0199 0.0502  103 VAL B CB  
3660 C CG1 . VAL B 133 ? 0.6922 0.5516 0.7171 -0.0969 -0.0220 0.0559  103 VAL B CG1 
3661 C CG2 . VAL B 133 ? 0.7034 0.5394 0.7149 -0.0881 -0.0160 0.0481  103 VAL B CG2 
3662 N N   . SER B 134 ? 0.6952 0.5440 0.7027 -0.1013 -0.0378 0.0494  104 SER B N   
3663 C CA  . SER B 134 ? 0.6913 0.5514 0.6998 -0.1017 -0.0422 0.0500  104 SER B CA  
3664 C C   . SER B 134 ? 0.6806 0.5591 0.6980 -0.0965 -0.0371 0.0544  104 SER B C   
3665 O O   . SER B 134 ? 0.6747 0.5604 0.7004 -0.0959 -0.0318 0.0579  104 SER B O   
3666 C CB  . SER B 134 ? 0.6995 0.5632 0.7112 -0.1128 -0.0510 0.0508  104 SER B CB  
3667 O OG  . SER B 134 ? 0.6991 0.5786 0.7241 -0.1190 -0.0501 0.0565  104 SER B OG  
3668 N N   . ASN B 135 ? 0.6783 0.5641 0.6928 -0.0921 -0.0390 0.0541  105 ASN B N   
3669 C CA  . ASN B 135 ? 0.6749 0.5765 0.6949 -0.0856 -0.0349 0.0580  105 ASN B CA  
3670 C C   . ASN B 135 ? 0.6555 0.5757 0.6892 -0.0904 -0.0351 0.0631  105 ASN B C   
3671 O O   . ASN B 135 ? 0.6544 0.5806 0.6937 -0.0860 -0.0287 0.0662  105 ASN B O   
3672 C CB  . ASN B 135 ? 0.6992 0.6065 0.7132 -0.0814 -0.0391 0.0570  105 ASN B CB  
3673 C CG  . ASN B 135 ? 0.7573 0.6485 0.7573 -0.0760 -0.0390 0.0524  105 ASN B CG  
3674 O OD1 . ASN B 135 ? 0.7851 0.6610 0.7797 -0.0752 -0.0353 0.0498  105 ASN B OD1 
3675 N ND2 . ASN B 135 ? 0.7618 0.6574 0.7554 -0.0717 -0.0428 0.0515  105 ASN B ND2 
3676 N N   . THR B 136 ? 0.6381 0.5663 0.6768 -0.0999 -0.0425 0.0637  106 THR B N   
3677 C CA  . THR B 136 ? 0.6174 0.5658 0.6695 -0.1059 -0.0435 0.0689  106 THR B CA  
3678 C C   . THR B 136 ? 0.6032 0.5478 0.6607 -0.1084 -0.0382 0.0714  106 THR B C   
3679 O O   . THR B 136 ? 0.5964 0.5556 0.6623 -0.1051 -0.0336 0.0757  106 THR B O   
3680 C CB  . THR B 136 ? 0.6271 0.5835 0.6828 -0.1175 -0.0527 0.0686  106 THR B CB  
3681 O OG1 . THR B 136 ? 0.6426 0.5952 0.6895 -0.1155 -0.0585 0.0641  106 THR B OG1 
3682 C CG2 . THR B 136 ? 0.6197 0.6047 0.6895 -0.1215 -0.0539 0.0741  106 THR B CG2 
3683 N N   . ARG B 137 ? 0.5989 0.5234 0.6502 -0.1127 -0.0387 0.0685  107 ARG B N   
3684 C CA  . ARG B 137 ? 0.5937 0.5121 0.6480 -0.1149 -0.0344 0.0704  107 ARG B CA  
3685 C C   . ARG B 137 ? 0.5916 0.5086 0.6461 -0.1048 -0.0258 0.0705  107 ARG B C   
3686 O O   . ARG B 137 ? 0.5883 0.5116 0.6497 -0.1049 -0.0217 0.0738  107 ARG B O   
3687 C CB  . ARG B 137 ? 0.6148 0.5103 0.6596 -0.1201 -0.0377 0.0665  107 ARG B CB  
3688 C CG  . ARG B 137 ? 0.6376 0.5288 0.6858 -0.1263 -0.0364 0.0696  107 ARG B CG  
3689 C CD  . ARG B 137 ? 0.6671 0.5331 0.7031 -0.1292 -0.0396 0.0653  107 ARG B CD  
3690 N NE  . ARG B 137 ? 0.6896 0.5471 0.7247 -0.1272 -0.0346 0.0664  107 ARG B NE  
3691 C CZ  . ARG B 137 ? 0.7133 0.5521 0.7377 -0.1217 -0.0329 0.0618  107 ARG B CZ  
3692 N NH1 . ARG B 137 ? 0.6967 0.5232 0.7104 -0.1176 -0.0355 0.0559  107 ARG B NH1 
3693 N NH2 . ARG B 137 ? 0.7204 0.5540 0.7446 -0.1195 -0.0286 0.0630  107 ARG B NH2 
3694 N N   . LEU B 138 ? 0.5931 0.5021 0.6400 -0.0965 -0.0230 0.0669  108 LEU B N   
3695 C CA  . LEU B 138 ? 0.5929 0.4995 0.6395 -0.0881 -0.0150 0.0664  108 LEU B CA  
3696 C C   . LEU B 138 ? 0.5793 0.5034 0.6335 -0.0831 -0.0118 0.0707  108 LEU B C   
3697 O O   . LEU B 138 ? 0.5752 0.5031 0.6341 -0.0799 -0.0066 0.0723  108 LEU B O   
3698 C CB  . LEU B 138 ? 0.6047 0.4975 0.6406 -0.0820 -0.0127 0.0618  108 LEU B CB  
3699 C CG  . LEU B 138 ? 0.6329 0.5226 0.6684 -0.0748 -0.0046 0.0610  108 LEU B CG  
3700 C CD1 . LEU B 138 ? 0.6460 0.5314 0.6848 -0.0762 -0.0014 0.0601  108 LEU B CD1 
3701 C CD2 . LEU B 138 ? 0.6475 0.5258 0.6728 -0.0698 -0.0022 0.0574  108 LEU B CD2 
3702 N N   . ILE B 139 ? 0.5705 0.5053 0.6248 -0.0815 -0.0151 0.0721  109 ILE B N   
3703 C CA  . ILE B 139 ? 0.5617 0.5134 0.6213 -0.0753 -0.0128 0.0760  109 ILE B CA  
3704 C C   . ILE B 139 ? 0.5560 0.5259 0.6276 -0.0800 -0.0136 0.0807  109 ILE B C   
3705 O O   . ILE B 139 ? 0.5527 0.5322 0.6290 -0.0742 -0.0091 0.0835  109 ILE B O   
3706 C CB  . ILE B 139 ? 0.5615 0.5197 0.6166 -0.0718 -0.0168 0.0759  109 ILE B CB  
3707 C CG1 . ILE B 139 ? 0.5793 0.5200 0.6220 -0.0650 -0.0138 0.0723  109 ILE B CG1 
3708 C CG2 . ILE B 139 ? 0.5581 0.5374 0.6191 -0.0657 -0.0162 0.0802  109 ILE B CG2 
3709 C CD1 . ILE B 139 ? 0.5938 0.5278 0.6339 -0.0569 -0.0058 0.0727  109 ILE B CD1 
3710 N N   . ALA B 140 ? 0.5529 0.5263 0.6287 -0.0907 -0.0191 0.0817  110 ALA B N   
3711 C CA  . ALA B 140 ? 0.5519 0.5426 0.6389 -0.0967 -0.0197 0.0868  110 ALA B CA  
3712 C C   . ALA B 140 ? 0.5634 0.5473 0.6524 -0.0962 -0.0142 0.0878  110 ALA B C   
3713 O O   . ALA B 140 ? 0.5637 0.5637 0.6610 -0.0951 -0.0115 0.0923  110 ALA B O   
3714 C CB  . ALA B 140 ? 0.5524 0.5462 0.6424 -0.1096 -0.0270 0.0875  110 ALA B CB  
3715 N N   . ALA B 141 ? 0.5716 0.5334 0.6527 -0.0962 -0.0125 0.0835  111 ALA B N   
3716 C CA  . ALA B 141 ? 0.5743 0.5299 0.6565 -0.0944 -0.0074 0.0837  111 ALA B CA  
3717 C C   . ALA B 141 ? 0.5689 0.5304 0.6525 -0.0835 -0.0012 0.0837  111 ALA B C   
3718 O O   . ALA B 141 ? 0.5625 0.5343 0.6522 -0.0813 0.0021  0.0868  111 ALA B O   
3719 C CB  . ALA B 141 ? 0.5849 0.5173 0.6578 -0.0956 -0.0074 0.0785  111 ALA B CB  
3720 N N   . ALA B 142 ? 0.5722 0.5277 0.6496 -0.0769 0.0002  0.0806  112 ALA B N   
3721 C CA  . ALA B 142 ? 0.5781 0.5360 0.6548 -0.0670 0.0056  0.0803  112 ALA B CA  
3722 C C   . ALA B 142 ? 0.5757 0.5555 0.6598 -0.0631 0.0058  0.0854  112 ALA B C   
3723 O O   . ALA B 142 ? 0.5690 0.5535 0.6553 -0.0566 0.0101  0.0863  112 ALA B O   
3724 C CB  . ALA B 142 ? 0.5827 0.5296 0.6503 -0.0620 0.0064  0.0770  112 ALA B CB  
3725 N N   . THR B 143 ? 0.5766 0.5707 0.6645 -0.0668 0.0007  0.0885  113 THR B N   
3726 C CA  . THR B 143 ? 0.5768 0.5950 0.6720 -0.0629 0.0004  0.0934  113 THR B CA  
3727 C C   . THR B 143 ? 0.5832 0.6143 0.6879 -0.0670 0.0018  0.0975  113 THR B C   
3728 O O   . THR B 143 ? 0.5814 0.6225 0.6888 -0.0592 0.0058  0.0996  113 THR B O   
3729 C CB  . THR B 143 ? 0.5783 0.6103 0.6753 -0.0660 -0.0056 0.0950  113 THR B CB  
3730 O OG1 . THR B 143 ? 0.5937 0.6136 0.6806 -0.0602 -0.0062 0.0915  113 THR B OG1 
3731 C CG2 . THR B 143 ? 0.5684 0.6285 0.6734 -0.0615 -0.0061 0.1000  113 THR B CG2 
3732 N N   . SER B 144 ? 0.5863 0.6151 0.6943 -0.0786 -0.0012 0.0987  114 SER B N   
3733 C CA  . SER B 144 ? 0.5907 0.6301 0.7067 -0.0836 0.0002  0.1033  114 SER B CA  
3734 C C   . SER B 144 ? 0.6000 0.6304 0.7140 -0.0775 0.0061  0.1021  114 SER B C   
3735 O O   . SER B 144 ? 0.5954 0.6408 0.7156 -0.0748 0.0090  0.1062  114 SER B O   
3736 C CB  . SER B 144 ? 0.6146 0.6477 0.7316 -0.0976 -0.0044 0.1044  114 SER B CB  
3737 O OG  . SER B 144 ? 0.6447 0.6839 0.7674 -0.1027 -0.0023 0.1092  114 SER B OG  
3738 N N   . VAL B 145 ? 0.6104 0.6180 0.7161 -0.0753 0.0078  0.0963  115 VAL B N   
3739 C CA  . VAL B 145 ? 0.6216 0.6211 0.7255 -0.0697 0.0129  0.0941  115 VAL B CA  
3740 C C   . VAL B 145 ? 0.6276 0.6372 0.7326 -0.0583 0.0170  0.0944  115 VAL B C   
3741 O O   . VAL B 145 ? 0.6270 0.6459 0.7362 -0.0548 0.0199  0.0967  115 VAL B O   
3742 C CB  . VAL B 145 ? 0.6408 0.6165 0.7362 -0.0700 0.0137  0.0876  115 VAL B CB  
3743 C CG1 . VAL B 145 ? 0.6520 0.6219 0.7457 -0.0627 0.0189  0.0842  115 VAL B CG1 
3744 C CG2 . VAL B 145 ? 0.6493 0.6148 0.7427 -0.0795 0.0102  0.0877  115 VAL B CG2 
3745 N N   . LEU B 146 ? 0.6348 0.6428 0.7356 -0.0523 0.0169  0.0924  116 LEU B N   
3746 C CA  . LEU B 146 ? 0.6478 0.6621 0.7475 -0.0409 0.0204  0.0924  116 LEU B CA  
3747 C C   . LEU B 146 ? 0.6446 0.6848 0.7519 -0.0377 0.0199  0.0985  116 LEU B C   
3748 O O   . LEU B 146 ? 0.6470 0.6941 0.7550 -0.0293 0.0232  0.0991  116 LEU B O   
3749 C CB  . LEU B 146 ? 0.6616 0.6650 0.7528 -0.0349 0.0207  0.0892  116 LEU B CB  
3750 C CG  . LEU B 146 ? 0.6976 0.6772 0.7812 -0.0377 0.0219  0.0834  116 LEU B CG  
3751 C CD1 . LEU B 146 ? 0.7165 0.6864 0.7914 -0.0322 0.0226  0.0815  116 LEU B CD1 
3752 C CD2 . LEU B 146 ? 0.7087 0.6783 0.7915 -0.0358 0.0262  0.0795  116 LEU B CD2 
3753 N N   . LYS B 147 ? 0.6363 0.6918 0.7495 -0.0445 0.0157  0.1028  117 LYS B N   
3754 C CA  . LYS B 147 ? 0.6221 0.7060 0.7438 -0.0426 0.0152  0.1091  117 LYS B CA  
3755 C C   . LYS B 147 ? 0.6064 0.7003 0.7350 -0.0459 0.0176  0.1130  117 LYS B C   
3756 O O   . LYS B 147 ? 0.6053 0.7136 0.7364 -0.0372 0.0207  0.1154  117 LYS B O   
3757 C CB  . LYS B 147 ? 0.6436 0.7419 0.7702 -0.0505 0.0096  0.1121  117 LYS B CB  
3758 C CG  . LYS B 147 ? 0.6903 0.8216 0.8275 -0.0506 0.0087  0.1187  117 LYS B CG  
3759 C CD  . LYS B 147 ? 0.7515 0.8966 0.8928 -0.0577 0.0027  0.1202  117 LYS B CD  
3760 C CE  . LYS B 147 ? 0.7887 0.9701 0.9415 -0.0585 0.0015  0.1267  117 LYS B CE  
3761 N NZ  . LYS B 147 ? 0.8123 1.0082 0.9688 -0.0644 -0.0048 0.1272  117 LYS B NZ  
3762 N N   . THR B 148 ? 0.5980 0.6829 0.7284 -0.0574 0.0163  0.1136  118 THR B N   
3763 C CA  . THR B 148 ? 0.5949 0.6879 0.7307 -0.0611 0.0186  0.1181  118 THR B CA  
3764 C C   . THR B 148 ? 0.5949 0.6761 0.7261 -0.0532 0.0234  0.1149  118 THR B C   
3765 O O   . THR B 148 ? 0.5956 0.6913 0.7306 -0.0479 0.0266  0.1184  118 THR B O   
3766 C CB  . THR B 148 ? 0.6176 0.7028 0.7550 -0.0761 0.0154  0.1202  118 THR B CB  
3767 O OG1 . THR B 148 ? 0.6463 0.7032 0.7747 -0.0777 0.0148  0.1138  118 THR B OG1 
3768 C CG2 . THR B 148 ? 0.6138 0.7124 0.7566 -0.0856 0.0101  0.1234  118 THR B CG2 
3769 N N   . ARG B 149 ? 0.5905 0.6472 0.7139 -0.0523 0.0239  0.1081  119 ARG B N   
3770 C CA  . ARG B 149 ? 0.5820 0.6276 0.7015 -0.0465 0.0277  0.1043  119 ARG B CA  
3771 C C   . ARG B 149 ? 0.5622 0.6034 0.6770 -0.0345 0.0306  0.0992  119 ARG B C   
3772 O O   . ARG B 149 ? 0.5571 0.5967 0.6706 -0.0283 0.0337  0.0971  119 ARG B O   
3773 C CB  . ARG B 149 ? 0.6115 0.6348 0.7257 -0.0532 0.0267  0.1000  119 ARG B CB  
3774 C CG  . ARG B 149 ? 0.6640 0.6887 0.7809 -0.0646 0.0241  0.1052  119 ARG B CG  
3775 C CD  . ARG B 149 ? 0.7230 0.7253 0.8332 -0.0715 0.0215  0.1012  119 ARG B CD  
3776 N NE  . ARG B 149 ? 0.7711 0.7607 0.8764 -0.0679 0.0242  0.0976  119 ARG B NE  
3777 C CZ  . ARG B 149 ? 0.8072 0.7781 0.9057 -0.0718 0.0227  0.0941  119 ARG B CZ  
3778 N NH1 . ARG B 149 ? 0.8079 0.7689 0.9031 -0.0796 0.0183  0.0936  119 ARG B NH1 
3779 N NH2 . ARG B 149 ? 0.8084 0.7707 0.9027 -0.0670 0.0253  0.0907  119 ARG B NH2 
3780 N N   . PHE B 150 ? 0.5554 0.5938 0.6668 -0.0311 0.0294  0.0972  120 PHE B N   
3781 C CA  . PHE B 150 ? 0.5592 0.5890 0.6642 -0.0205 0.0320  0.0922  120 PHE B CA  
3782 C C   . PHE B 150 ? 0.5576 0.6012 0.6619 -0.0113 0.0319  0.0949  120 PHE B C   
3783 O O   . PHE B 150 ? 0.5637 0.5959 0.6604 -0.0046 0.0328  0.0912  120 PHE B O   
3784 C CB  . PHE B 150 ? 0.5627 0.5692 0.6603 -0.0232 0.0318  0.0860  120 PHE B CB  
3785 C CG  . PHE B 150 ? 0.5686 0.5615 0.6653 -0.0295 0.0324  0.0822  120 PHE B CG  
3786 C CD1 . PHE B 150 ? 0.5752 0.5642 0.6731 -0.0391 0.0294  0.0835  120 PHE B CD1 
3787 C CD2 . PHE B 150 ? 0.5795 0.5641 0.6738 -0.0251 0.0355  0.0771  120 PHE B CD2 
3788 C CE1 . PHE B 150 ? 0.5852 0.5621 0.6812 -0.0432 0.0299  0.0801  120 PHE B CE1 
3789 C CE2 . PHE B 150 ? 0.5876 0.5620 0.6810 -0.0297 0.0359  0.0735  120 PHE B CE2 
3790 C CZ  . PHE B 150 ? 0.5844 0.5550 0.6783 -0.0381 0.0332  0.0752  120 PHE B CZ  
3791 N N   . SER B 151 ? 0.5478 0.6161 0.6596 -0.0107 0.0310  0.1015  121 SER B N   
3792 C CA  . SER B 151 ? 0.5468 0.6321 0.6582 -0.0009 0.0306  0.1044  121 SER B CA  
3793 C C   . SER B 151 ? 0.5489 0.6324 0.6542 0.0132  0.0339  0.1018  121 SER B C   
3794 O O   . SER B 151 ? 0.5560 0.6436 0.6561 0.0235  0.0337  0.1019  121 SER B O   
3795 C CB  . SER B 151 ? 0.5515 0.6663 0.6734 -0.0047 0.0289  0.1122  121 SER B CB  
3796 O OG  . SER B 151 ? 0.5752 0.6976 0.7035 -0.0100 0.0307  0.1154  121 SER B OG  
3797 N N   . TYR B 152 ? 0.5405 0.6169 0.6454 0.0145  0.0366  0.0990  122 TYR B N   
3798 C CA  . TYR B 152 ? 0.5391 0.6108 0.6373 0.0272  0.0393  0.0952  122 TYR B CA  
3799 C C   . TYR B 152 ? 0.5710 0.6174 0.6579 0.0313  0.0397  0.0885  122 TYR B C   
3800 O O   . TYR B 152 ? 0.5799 0.6221 0.6590 0.0431  0.0408  0.0861  122 TYR B O   
3801 C CB  . TYR B 152 ? 0.5230 0.5926 0.6234 0.0264  0.0416  0.0931  122 TYR B CB  
3802 C CG  . TYR B 152 ? 0.5225 0.5716 0.6221 0.0166  0.0416  0.0883  122 TYR B CG  
3803 C CD1 . TYR B 152 ? 0.5361 0.5625 0.6279 0.0182  0.0425  0.0805  122 TYR B CD1 
3804 C CD2 . TYR B 152 ? 0.5232 0.5757 0.6291 0.0060  0.0408  0.0914  122 TYR B CD2 
3805 C CE1 . TYR B 152 ? 0.5464 0.5569 0.6378 0.0098  0.0427  0.0759  122 TYR B CE1 
3806 C CE2 . TYR B 152 ? 0.5367 0.5711 0.6408 -0.0015 0.0407  0.0867  122 TYR B CE2 
3807 C CZ  . TYR B 152 ? 0.5500 0.5648 0.6473 0.0008  0.0417  0.0789  122 TYR B CZ  
3808 O OH  . TYR B 152 ? 0.5642 0.5640 0.6600 -0.0058 0.0417  0.0742  122 TYR B OH  
3809 N N   . ALA B 153 ? 0.5849 0.6135 0.6701 0.0217  0.0388  0.0856  123 ALA B N   
3810 C CA  . ALA B 153 ? 0.6096 0.6141 0.6846 0.0235  0.0396  0.0799  123 ALA B CA  
3811 C C   . ALA B 153 ? 0.6243 0.6268 0.6951 0.0235  0.0376  0.0823  123 ALA B C   
3812 O O   . ALA B 153 ? 0.6350 0.6207 0.6954 0.0287  0.0386  0.0794  123 ALA B O   
3813 C CB  . ALA B 153 ? 0.6149 0.6014 0.6898 0.0144  0.0407  0.0746  123 ALA B CB  
3814 N N   . PHE B 154 ? 0.6246 0.6440 0.7027 0.0179  0.0347  0.0876  124 PHE B N   
3815 C CA  . PHE B 154 ? 0.6404 0.6605 0.7150 0.0180  0.0321  0.0896  124 PHE B CA  
3816 C C   . PHE B 154 ? 0.6451 0.6936 0.7260 0.0220  0.0296  0.0959  124 PHE B C   
3817 O O   . PHE B 154 ? 0.6380 0.7030 0.7291 0.0130  0.0272  0.0997  124 PHE B O   
3818 C CB  . PHE B 154 ? 0.6414 0.6519 0.7178 0.0055  0.0301  0.0886  124 PHE B CB  
3819 C CG  . PHE B 154 ? 0.6584 0.6444 0.7298 0.0009  0.0326  0.0827  124 PHE B CG  
3820 C CD1 . PHE B 154 ? 0.6779 0.6439 0.7384 0.0056  0.0349  0.0789  124 PHE B CD1 
3821 C CD2 . PHE B 154 ? 0.6682 0.6513 0.7453 -0.0080 0.0327  0.0810  124 PHE B CD2 
3822 C CE1 . PHE B 154 ? 0.6959 0.6421 0.7529 0.0007  0.0374  0.0736  124 PHE B CE1 
3823 C CE2 . PHE B 154 ? 0.6846 0.6482 0.7576 -0.0115 0.0350  0.0753  124 PHE B CE2 
3824 C CZ  . PHE B 154 ? 0.6906 0.6370 0.7543 -0.0077 0.0373  0.0716  124 PHE B CZ  
3825 N N   . PRO B 155 ? 0.6568 0.7110 0.7310 0.0352  0.0299  0.0970  125 PRO B N   
3826 C CA  . PRO B 155 ? 0.6529 0.7375 0.7332 0.0399  0.0274  0.1028  125 PRO B CA  
3827 C C   . PRO B 155 ? 0.6529 0.7448 0.7354 0.0339  0.0232  0.1051  125 PRO B C   
3828 O O   . PRO B 155 ? 0.6381 0.7568 0.7310 0.0297  0.0204  0.1098  125 PRO B O   
3829 C CB  . PRO B 155 ? 0.6674 0.7513 0.7368 0.0576  0.0290  0.1022  125 PRO B CB  
3830 C CG  . PRO B 155 ? 0.6868 0.7358 0.7422 0.0599  0.0310  0.0964  125 PRO B CG  
3831 C CD  . PRO B 155 ? 0.6661 0.6994 0.7262 0.0466  0.0324  0.0929  125 PRO B CD  
3832 N N   . LYS B 156 ? 0.6650 0.7335 0.7376 0.0331  0.0229  0.1016  126 LYS B N   
3833 C CA  . LYS B 156 ? 0.6691 0.7417 0.7415 0.0286  0.0188  0.1028  126 LYS B CA  
3834 C C   . LYS B 156 ? 0.6682 0.7367 0.7482 0.0120  0.0164  0.1020  126 LYS B C   
3835 O O   . LYS B 156 ? 0.6747 0.7288 0.7563 0.0050  0.0186  0.0994  126 LYS B O   
3836 C CB  . LYS B 156 ? 0.7085 0.7574 0.7650 0.0365  0.0198  0.1000  126 LYS B CB  
3837 C CG  . LYS B 156 ? 0.7773 0.8225 0.8225 0.0534  0.0223  0.1000  126 LYS B CG  
3838 C CD  . LYS B 156 ? 0.8634 0.8786 0.8914 0.0591  0.0242  0.0972  126 LYS B CD  
3839 C CE  . LYS B 156 ? 0.9317 0.9288 0.9472 0.0711  0.0282  0.0950  126 LYS B CE  
3840 N NZ  . LYS B 156 ? 0.9757 0.9422 0.9736 0.0757  0.0304  0.0930  126 LYS B NZ  
3841 N N   . GLU B 157 ? 0.6573 0.7377 0.7409 0.0065  0.0116  0.1038  127 GLU B N   
3842 C CA  . GLU B 157 ? 0.6559 0.7307 0.7443 -0.0083 0.0084  0.1027  127 GLU B CA  
3843 C C   . GLU B 157 ? 0.6498 0.6933 0.7269 -0.0096 0.0101  0.0976  127 GLU B C   
3844 O O   . GLU B 157 ? 0.6595 0.6898 0.7254 0.0002  0.0124  0.0960  127 GLU B O   
3845 C CB  . GLU B 157 ? 0.6906 0.7867 0.7840 -0.0119 0.0023  0.1053  127 GLU B CB  
3846 C CG  . GLU B 157 ? 0.7727 0.8720 0.8746 -0.0281 -0.0020 0.1055  127 GLU B CG  
3847 C CD  . GLU B 157 ? 0.8832 0.9937 0.9860 -0.0323 -0.0085 0.1056  127 GLU B CD  
3848 O OE1 . GLU B 157 ? 0.9099 1.0117 1.0025 -0.0245 -0.0093 0.1034  127 GLU B OE1 
3849 O OE2 . GLU B 157 ? 0.9111 1.0386 1.0244 -0.0438 -0.0129 0.1078  127 GLU B OE2 
3850 N N   . PHE B 158 ? 0.6306 0.6621 0.7098 -0.0213 0.0089  0.0952  128 PHE B N   
3851 C CA  . PHE B 158 ? 0.6270 0.6322 0.6964 -0.0230 0.0104  0.0906  128 PHE B CA  
3852 C C   . PHE B 158 ? 0.6280 0.6306 0.6888 -0.0185 0.0079  0.0905  128 PHE B C   
3853 O O   . PHE B 158 ? 0.6299 0.6464 0.6945 -0.0226 0.0024  0.0920  128 PHE B O   
3854 C CB  . PHE B 158 ? 0.6145 0.6112 0.6877 -0.0354 0.0086  0.0885  128 PHE B CB  
3855 C CG  . PHE B 158 ? 0.6174 0.5900 0.6814 -0.0372 0.0102  0.0838  128 PHE B CG  
3856 C CD1 . PHE B 158 ? 0.6233 0.5799 0.6827 -0.0342 0.0158  0.0806  128 PHE B CD1 
3857 C CD2 . PHE B 158 ? 0.6245 0.5915 0.6845 -0.0423 0.0061  0.0822  128 PHE B CD2 
3858 C CE1 . PHE B 158 ? 0.6364 0.5737 0.6884 -0.0364 0.0176  0.0766  128 PHE B CE1 
3859 C CE2 . PHE B 158 ? 0.6385 0.5852 0.6900 -0.0434 0.0079  0.0781  128 PHE B CE2 
3860 C CZ  . PHE B 158 ? 0.6385 0.5713 0.6865 -0.0407 0.0139  0.0755  128 PHE B CZ  
3861 N N   . PRO B 159 ? 0.6261 0.6124 0.6753 -0.0097 0.0117  0.0890  129 PRO B N   
3862 C CA  . PRO B 159 ? 0.6258 0.6107 0.6654 -0.0030 0.0097  0.0898  129 PRO B CA  
3863 C C   . PRO B 159 ? 0.6358 0.6049 0.6679 -0.0077 0.0084  0.0871  129 PRO B C   
3864 O O   . PRO B 159 ? 0.6452 0.6153 0.6695 -0.0022 0.0062  0.0880  129 PRO B O   
3865 C CB  . PRO B 159 ? 0.6396 0.6123 0.6685 0.0091  0.0149  0.0900  129 PRO B CB  
3866 C CG  . PRO B 159 ? 0.6509 0.6070 0.6805 0.0049  0.0198  0.0869  129 PRO B CG  
3867 C CD  . PRO B 159 ? 0.6240 0.5936 0.6677 -0.0046 0.0178  0.0869  129 PRO B CD  
3868 N N   . TYR B 160 ? 0.6325 0.5873 0.6656 -0.0163 0.0100  0.0838  130 TYR B N   
3869 C CA  . TYR B 160 ? 0.6384 0.5777 0.6633 -0.0196 0.0094  0.0811  130 TYR B CA  
3870 C C   . TYR B 160 ? 0.6363 0.5841 0.6653 -0.0275 0.0025  0.0803  130 TYR B C   
3871 O O   . TYR B 160 ? 0.6256 0.5870 0.6653 -0.0344 -0.0012 0.0811  130 TYR B O   
3872 C CB  . TYR B 160 ? 0.6401 0.5597 0.6623 -0.0234 0.0148  0.0776  130 TYR B CB  
3873 C CG  . TYR B 160 ? 0.6523 0.5615 0.6691 -0.0164 0.0212  0.0778  130 TYR B CG  
3874 C CD1 . TYR B 160 ? 0.6712 0.5681 0.6753 -0.0089 0.0241  0.0788  130 TYR B CD1 
3875 C CD2 . TYR B 160 ? 0.6578 0.5694 0.6813 -0.0166 0.0240  0.0773  130 TYR B CD2 
3876 C CE1 . TYR B 160 ? 0.6858 0.5706 0.6837 -0.0030 0.0297  0.0789  130 TYR B CE1 
3877 C CE2 . TYR B 160 ? 0.6718 0.5730 0.6896 -0.0102 0.0292  0.0769  130 TYR B CE2 
3878 C CZ  . TYR B 160 ? 0.6919 0.5789 0.6967 -0.0038 0.0320  0.0777  130 TYR B CZ  
3879 O OH  . TYR B 160 ? 0.7146 0.5886 0.7123 0.0022  0.0368  0.0773  130 TYR B OH  
3880 N N   . ARG B 161 ? 0.6459 0.5848 0.6653 -0.0263 0.0008  0.0787  131 ARG B N   
3881 C CA  . ARG B 161 ? 0.6592 0.6017 0.6790 -0.0328 -0.0060 0.0768  131 ARG B CA  
3882 C C   . ARG B 161 ? 0.6704 0.5931 0.6837 -0.0373 -0.0043 0.0727  131 ARG B C   
3883 O O   . ARG B 161 ? 0.6773 0.5853 0.6851 -0.0346 0.0022  0.0718  131 ARG B O   
3884 C CB  . ARG B 161 ? 0.6929 0.6430 0.7056 -0.0259 -0.0098 0.0781  131 ARG B CB  
3885 C CG  . ARG B 161 ? 0.7512 0.7272 0.7729 -0.0251 -0.0151 0.0810  131 ARG B CG  
3886 C CD  . ARG B 161 ? 0.8277 0.8104 0.8406 -0.0135 -0.0162 0.0829  131 ARG B CD  
3887 N NE  . ARG B 161 ? 0.9031 0.8749 0.9076 -0.0024 -0.0089 0.0851  131 ARG B NE  
3888 C CZ  . ARG B 161 ? 0.9565 0.9388 0.9652 0.0037  -0.0065 0.0880  131 ARG B CZ  
3889 N NH1 . ARG B 161 ? 0.9483 0.9547 0.9706 -0.0001 -0.0103 0.0897  131 ARG B NH1 
3890 N NH2 . ARG B 161 ? 0.9768 0.9453 0.9756 0.0136  -0.0003 0.0895  131 ARG B NH2 
3891 N N   . MET B 162 ? 0.6684 0.5910 0.6818 -0.0442 -0.0105 0.0701  132 MET B N   
3892 C CA  . MET B 162 ? 0.6769 0.5824 0.6836 -0.0475 -0.0096 0.0659  132 MET B CA  
3893 C C   . MET B 162 ? 0.6941 0.5861 0.6881 -0.0404 -0.0047 0.0652  132 MET B C   
3894 O O   . MET B 162 ? 0.7084 0.5869 0.6981 -0.0417 -0.0008 0.0625  132 MET B O   
3895 C CB  . MET B 162 ? 0.6705 0.5768 0.6769 -0.0548 -0.0179 0.0630  132 MET B CB  
3896 C CG  . MET B 162 ? 0.6710 0.5613 0.6731 -0.0590 -0.0172 0.0588  132 MET B CG  
3897 S SD  . MET B 162 ? 0.6242 0.5132 0.6363 -0.0641 -0.0131 0.0593  132 MET B SD  
3898 C CE  . MET B 162 ? 0.5960 0.4660 0.5990 -0.0643 -0.0108 0.0540  132 MET B CE  
3899 N N   . ASN B 163 ? 0.6929 0.5887 0.6805 -0.0326 -0.0047 0.0678  133 ASN B N   
3900 C CA  . ASN B 163 ? 0.7118 0.5936 0.6861 -0.0259 0.0007  0.0680  133 ASN B CA  
3901 C C   . ASN B 163 ? 0.7050 0.5759 0.6789 -0.0243 0.0097  0.0690  133 ASN B C   
3902 O O   . ASN B 163 ? 0.7144 0.5716 0.6805 -0.0238 0.0149  0.0678  133 ASN B O   
3903 C CB  . ASN B 163 ? 0.7483 0.6352 0.7140 -0.0170 -0.0014 0.0708  133 ASN B CB  
3904 C CG  . ASN B 163 ? 0.8128 0.7157 0.7845 -0.0125 -0.0032 0.0743  133 ASN B CG  
3905 O OD1 . ASN B 163 ? 0.8296 0.7500 0.8108 -0.0165 -0.0101 0.0741  133 ASN B OD1 
3906 N ND2 . ASN B 163 ? 0.8312 0.7285 0.7968 -0.0041 0.0027  0.0777  133 ASN B ND2 
3907 N N   . HIS B 164 ? 0.6861 0.5640 0.6687 -0.0242 0.0114  0.0709  134 HIS B N   
3908 C CA  . HIS B 164 ? 0.6825 0.5510 0.6655 -0.0232 0.0189  0.0712  134 HIS B CA  
3909 C C   . HIS B 164 ? 0.6712 0.5339 0.6596 -0.0307 0.0212  0.0674  134 HIS B C   
3910 O O   . HIS B 164 ? 0.6778 0.5289 0.6626 -0.0310 0.0275  0.0661  134 HIS B O   
3911 C CB  . HIS B 164 ? 0.6876 0.5668 0.6776 -0.0197 0.0190  0.0740  134 HIS B CB  
3912 C CG  . HIS B 164 ? 0.7174 0.6039 0.7016 -0.0107 0.0168  0.0777  134 HIS B CG  
3913 N ND1 . HIS B 164 ? 0.7325 0.6390 0.7250 -0.0089 0.0119  0.0798  134 HIS B ND1 
3914 C CD2 . HIS B 164 ? 0.7342 0.6116 0.7050 -0.0030 0.0188  0.0796  134 HIS B CD2 
3915 C CE1 . HIS B 164 ? 0.7362 0.6458 0.7201 0.0005  0.0109  0.0825  134 HIS B CE1 
3916 N NE2 . HIS B 164 ? 0.7418 0.6332 0.7119 0.0046  0.0149  0.0826  134 HIS B NE2 
3917 N N   . ILE B 165 ? 0.6540 0.5246 0.6505 -0.0369 0.0159  0.0655  135 ILE B N   
3918 C CA  . ILE B 165 ? 0.6487 0.5145 0.6495 -0.0430 0.0171  0.0618  135 ILE B CA  
3919 C C   . ILE B 165 ? 0.6567 0.5111 0.6484 -0.0435 0.0185  0.0587  135 ILE B C   
3920 O O   . ILE B 165 ? 0.6582 0.5056 0.6495 -0.0451 0.0235  0.0561  135 ILE B O   
3921 C CB  . ILE B 165 ? 0.6429 0.5183 0.6521 -0.0489 0.0104  0.0614  135 ILE B CB  
3922 C CG1 . ILE B 165 ? 0.6421 0.5318 0.6610 -0.0484 0.0093  0.0651  135 ILE B CG1 
3923 C CG2 . ILE B 165 ? 0.6518 0.5206 0.6630 -0.0540 0.0109  0.0575  135 ILE B CG2 
3924 C CD1 . ILE B 165 ? 0.6549 0.5458 0.6813 -0.0492 0.0136  0.0650  135 ILE B CD1 
3925 N N   . LEU B 166 ? 0.6585 0.5125 0.6428 -0.0418 0.0142  0.0587  136 LEU B N   
3926 C CA  . LEU B 166 ? 0.6665 0.5110 0.6407 -0.0409 0.0152  0.0561  136 LEU B CA  
3927 C C   . LEU B 166 ? 0.6783 0.5139 0.6450 -0.0368 0.0236  0.0576  136 LEU B C   
3928 O O   . LEU B 166 ? 0.6903 0.5189 0.6521 -0.0376 0.0274  0.0553  136 LEU B O   
3929 C CB  . LEU B 166 ? 0.6649 0.5116 0.6321 -0.0390 0.0082  0.0558  136 LEU B CB  
3930 C CG  . LEU B 166 ? 0.6707 0.5230 0.6427 -0.0445 -0.0007 0.0534  136 LEU B CG  
3931 C CD1 . LEU B 166 ? 0.6708 0.5254 0.6352 -0.0423 -0.0076 0.0527  136 LEU B CD1 
3932 C CD2 . LEU B 166 ? 0.6772 0.5219 0.6495 -0.0489 -0.0009 0.0491  136 LEU B CD2 
3933 N N   . GLU B 167 ? 0.6742 0.5100 0.6394 -0.0324 0.0263  0.0617  137 GLU B N   
3934 C CA  . GLU B 167 ? 0.6827 0.5077 0.6396 -0.0290 0.0342  0.0639  137 GLU B CA  
3935 C C   . GLU B 167 ? 0.6585 0.4793 0.6215 -0.0336 0.0404  0.0618  137 GLU B C   
3936 O O   . GLU B 167 ? 0.6620 0.4758 0.6209 -0.0356 0.0456  0.0603  137 GLU B O   
3937 C CB  . GLU B 167 ? 0.7413 0.5665 0.6938 -0.0222 0.0346  0.0686  137 GLU B CB  
3938 C CG  . GLU B 167 ? 0.8649 0.6757 0.8077 -0.0189 0.0428  0.0714  137 GLU B CG  
3939 C CD  . GLU B 167 ? 0.9883 0.7973 0.9301 -0.0136 0.0445  0.0748  137 GLU B CD  
3940 O OE1 . GLU B 167 ? 1.0099 0.8307 0.9614 -0.0132 0.0402  0.0745  137 GLU B OE1 
3941 O OE2 . GLU B 167 ? 1.0191 0.8141 0.9497 -0.0095 0.0502  0.0778  137 GLU B OE2 
3942 N N   . CYS B 168 ? 0.6330 0.4600 0.6063 -0.0353 0.0394  0.0615  138 CYS B N   
3943 C CA  . CYS B 168 ? 0.6176 0.4431 0.5981 -0.0393 0.0439  0.0589  138 CYS B CA  
3944 C C   . CYS B 168 ? 0.6224 0.4481 0.6052 -0.0442 0.0445  0.0542  138 CYS B C   
3945 O O   . CYS B 168 ? 0.6277 0.4501 0.6123 -0.0471 0.0499  0.0518  138 CYS B O   
3946 C CB  . CYS B 168 ? 0.5989 0.4338 0.5897 -0.0394 0.0408  0.0593  138 CYS B CB  
3947 S SG  . CYS B 168 ? 0.6048 0.4396 0.6045 -0.0432 0.0453  0.0557  138 CYS B SG  
3948 N N   . GLU B 169 ? 0.6193 0.4488 0.6013 -0.0449 0.0387  0.0528  139 GLU B N   
3949 C CA  . GLU B 169 ? 0.6269 0.4562 0.6091 -0.0477 0.0384  0.0483  139 GLU B CA  
3950 C C   . GLU B 169 ? 0.6510 0.4740 0.6247 -0.0470 0.0441  0.0475  139 GLU B C   
3951 O O   . GLU B 169 ? 0.6575 0.4812 0.6333 -0.0493 0.0477  0.0440  139 GLU B O   
3952 C CB  . GLU B 169 ? 0.6351 0.4672 0.6160 -0.0481 0.0302  0.0471  139 GLU B CB  
3953 C CG  . GLU B 169 ? 0.6573 0.4881 0.6380 -0.0500 0.0289  0.0423  139 GLU B CG  
3954 C CD  . GLU B 169 ? 0.7155 0.5444 0.6905 -0.0498 0.0211  0.0406  139 GLU B CD  
3955 O OE1 . GLU B 169 ? 0.7468 0.5757 0.7167 -0.0480 0.0175  0.0427  139 GLU B OE1 
3956 O OE2 . GLU B 169 ? 0.7300 0.5569 0.7046 -0.0511 0.0185  0.0368  139 GLU B OE2 
3957 N N   . PHE B 170 ? 0.6627 0.4806 0.6268 -0.0434 0.0453  0.0509  140 PHE B N   
3958 C CA  . PHE B 170 ? 0.6856 0.4978 0.6410 -0.0428 0.0515  0.0511  140 PHE B CA  
3959 C C   . PHE B 170 ? 0.6935 0.5024 0.6524 -0.0465 0.0599  0.0512  140 PHE B C   
3960 O O   . PHE B 170 ? 0.6922 0.5025 0.6515 -0.0495 0.0645  0.0485  140 PHE B O   
3961 C CB  . PHE B 170 ? 0.6985 0.5053 0.6418 -0.0375 0.0513  0.0554  140 PHE B CB  
3962 C CG  . PHE B 170 ? 0.7260 0.5338 0.6614 -0.0349 0.0477  0.0534  140 PHE B CG  
3963 C CD1 . PHE B 170 ? 0.7412 0.5540 0.6800 -0.0356 0.0399  0.0493  140 PHE B CD1 
3964 C CD2 . PHE B 170 ? 0.7469 0.5495 0.6705 -0.0317 0.0522  0.0554  140 PHE B CD2 
3965 C CE1 . PHE B 170 ? 0.7542 0.5662 0.6842 -0.0327 0.0362  0.0468  140 PHE B CE1 
3966 C CE2 . PHE B 170 ? 0.7620 0.5659 0.6775 -0.0284 0.0488  0.0531  140 PHE B CE2 
3967 C CZ  . PHE B 170 ? 0.7570 0.5652 0.6755 -0.0287 0.0405  0.0485  140 PHE B CZ  
3968 N N   . TYR B 171 ? 0.6951 0.5012 0.6575 -0.0465 0.0610  0.0536  141 TYR B N   
3969 C CA  . TYR B 171 ? 0.7008 0.5023 0.6666 -0.0502 0.0676  0.0533  141 TYR B CA  
3970 C C   . TYR B 171 ? 0.6965 0.5062 0.6734 -0.0550 0.0681  0.0478  141 TYR B C   
3971 O O   . TYR B 171 ? 0.7007 0.5099 0.6786 -0.0594 0.0739  0.0456  141 TYR B O   
3972 C CB  . TYR B 171 ? 0.7055 0.5025 0.6716 -0.0472 0.0669  0.0565  141 TYR B CB  
3973 C CG  . TYR B 171 ? 0.7286 0.5145 0.6819 -0.0423 0.0691  0.0620  141 TYR B CG  
3974 C CD1 . TYR B 171 ? 0.7545 0.5270 0.7011 -0.0437 0.0763  0.0642  141 TYR B CD1 
3975 C CD2 . TYR B 171 ? 0.7419 0.5303 0.6894 -0.0362 0.0639  0.0649  141 TYR B CD2 
3976 C CE1 . TYR B 171 ? 0.7798 0.5400 0.7126 -0.0384 0.0786  0.0696  141 TYR B CE1 
3977 C CE2 . TYR B 171 ? 0.7643 0.5428 0.6990 -0.0303 0.0658  0.0699  141 TYR B CE2 
3978 C CZ  . TYR B 171 ? 0.7883 0.5520 0.7150 -0.0310 0.0733  0.0725  141 TYR B CZ  
3979 O OH  . TYR B 171 ? 0.8110 0.5630 0.7232 -0.0244 0.0754  0.0779  141 TYR B OH  
3980 N N   . LEU B 172 ? 0.6852 0.5028 0.6701 -0.0544 0.0620  0.0457  142 LEU B N   
3981 C CA  . LEU B 172 ? 0.6816 0.5068 0.6760 -0.0576 0.0620  0.0407  142 LEU B CA  
3982 C C   . LEU B 172 ? 0.6894 0.5183 0.6818 -0.0590 0.0637  0.0370  142 LEU B C   
3983 O O   . LEU B 172 ? 0.6929 0.5260 0.6900 -0.0623 0.0680  0.0334  142 LEU B O   
3984 C CB  . LEU B 172 ? 0.6784 0.5101 0.6793 -0.0561 0.0550  0.0403  142 LEU B CB  
3985 C CG  . LEU B 172 ? 0.6858 0.5248 0.6945 -0.0579 0.0539  0.0355  142 LEU B CG  
3986 C CD1 . LEU B 172 ? 0.6847 0.5257 0.7002 -0.0601 0.0584  0.0332  142 LEU B CD1 
3987 C CD2 . LEU B 172 ? 0.6886 0.5317 0.7009 -0.0568 0.0469  0.0362  142 LEU B CD2 
3988 N N   . LEU B 173 ? 0.6905 0.5185 0.6756 -0.0561 0.0603  0.0377  143 LEU B N   
3989 C CA  . LEU B 173 ? 0.6953 0.5270 0.6768 -0.0558 0.0616  0.0342  143 LEU B CA  
3990 C C   . LEU B 173 ? 0.7050 0.5371 0.6847 -0.0589 0.0702  0.0341  143 LEU B C   
3991 O O   . LEU B 173 ? 0.7092 0.5493 0.6935 -0.0610 0.0732  0.0298  143 LEU B O   
3992 C CB  . LEU B 173 ? 0.6989 0.5278 0.6710 -0.0515 0.0565  0.0350  143 LEU B CB  
3993 C CG  . LEU B 173 ? 0.7115 0.5437 0.6778 -0.0494 0.0574  0.0313  143 LEU B CG  
3994 C CD1 . LEU B 173 ? 0.7133 0.5517 0.6852 -0.0493 0.0548  0.0260  143 LEU B CD1 
3995 C CD2 . LEU B 173 ? 0.7228 0.5505 0.6783 -0.0447 0.0522  0.0322  143 LEU B CD2 
3996 N N   . GLU B 174 ? 0.7065 0.5304 0.6793 -0.0592 0.0744  0.0389  144 GLU B N   
3997 C CA  . GLU B 174 ? 0.7146 0.5373 0.6846 -0.0633 0.0830  0.0397  144 GLU B CA  
3998 C C   . GLU B 174 ? 0.7209 0.5445 0.6995 -0.0697 0.0879  0.0379  144 GLU B C   
3999 O O   . GLU B 174 ? 0.7212 0.5509 0.7026 -0.0747 0.0937  0.0355  144 GLU B O   
4000 C CB  . GLU B 174 ? 0.7506 0.5623 0.7086 -0.0613 0.0860  0.0459  144 GLU B CB  
4001 C CG  . GLU B 174 ? 0.8222 0.6231 0.7784 -0.0600 0.0850  0.0502  144 GLU B CG  
4002 C CD  . GLU B 174 ? 0.9217 0.7105 0.8648 -0.0576 0.0890  0.0564  144 GLU B CD  
4003 O OE1 . GLU B 174 ? 0.9573 0.7451 0.8922 -0.0514 0.0850  0.0587  144 GLU B OE1 
4004 O OE2 . GLU B 174 ? 0.9330 0.7124 0.8732 -0.0618 0.0959  0.0590  144 GLU B OE2 
4005 N N   . LEU B 175 ? 0.7229 0.5418 0.7060 -0.0697 0.0854  0.0386  145 LEU B N   
4006 C CA  . LEU B 175 ? 0.7269 0.5452 0.7173 -0.0753 0.0894  0.0364  145 LEU B CA  
4007 C C   . LEU B 175 ? 0.7197 0.5514 0.7217 -0.0769 0.0873  0.0298  145 LEU B C   
4008 O O   . LEU B 175 ? 0.7225 0.5548 0.7315 -0.0796 0.0879  0.0273  145 LEU B O   
4009 C CB  . LEU B 175 ? 0.7386 0.5452 0.7268 -0.0736 0.0883  0.0399  145 LEU B CB  
4010 C CG  . LEU B 175 ? 0.7703 0.5626 0.7455 -0.0711 0.0909  0.0464  145 LEU B CG  
4011 C CD1 . LEU B 175 ? 0.7866 0.5698 0.7591 -0.0666 0.0882  0.0496  145 LEU B CD1 
4012 C CD2 . LEU B 175 ? 0.7781 0.5629 0.7480 -0.0775 0.0994  0.0478  145 LEU B CD2 
4013 N N   . MET B 176 ? 0.7111 0.5526 0.7138 -0.0743 0.0846  0.0270  146 MET B N   
4014 C CA  . MET B 176 ? 0.7070 0.5616 0.7177 -0.0742 0.0829  0.0208  146 MET B CA  
4015 C C   . MET B 176 ? 0.6994 0.5636 0.7077 -0.0744 0.0861  0.0182  146 MET B C   
4016 O O   . MET B 176 ? 0.6952 0.5709 0.7081 -0.0725 0.0844  0.0131  146 MET B O   
4017 C CB  . MET B 176 ? 0.7182 0.5740 0.7295 -0.0684 0.0749  0.0203  146 MET B CB  
4018 C CG  . MET B 176 ? 0.7403 0.5938 0.7576 -0.0679 0.0716  0.0211  146 MET B CG  
4019 S SD  . MET B 176 ? 0.7655 0.6245 0.7859 -0.0633 0.0640  0.0188  146 MET B SD  
4020 C CE  . MET B 176 ? 0.7381 0.5909 0.7480 -0.0597 0.0592  0.0219  146 MET B CE  
4021 N N   . ASP B 177 ? 0.6993 0.5592 0.6997 -0.0759 0.0908  0.0218  147 ASP B N   
4022 C CA  . ASP B 177 ? 0.7000 0.5690 0.6965 -0.0753 0.0944  0.0205  147 ASP B CA  
4023 C C   . ASP B 177 ? 0.6861 0.5599 0.6786 -0.0673 0.0880  0.0179  147 ASP B C   
4024 O O   . ASP B 177 ? 0.6866 0.5726 0.6791 -0.0654 0.0895  0.0139  147 ASP B O   
4025 C CB  . ASP B 177 ? 0.7303 0.6131 0.7351 -0.0819 0.1007  0.0162  147 ASP B CB  
4026 C CG  . ASP B 177 ? 0.8368 0.7286 0.8369 -0.0830 0.1068  0.0169  147 ASP B CG  
4027 O OD1 . ASP B 177 ? 0.8612 0.7446 0.8505 -0.0802 0.1077  0.0219  147 ASP B OD1 
4028 O OD2 . ASP B 177 ? 0.8793 0.7880 0.8864 -0.0863 0.1105  0.0122  147 ASP B OD2 
4029 N N   . CYS B 178 ? 0.6687 0.5329 0.6574 -0.0627 0.0808  0.0198  148 CYS B N   
4030 C CA  . CYS B 178 ? 0.6547 0.5191 0.6384 -0.0559 0.0736  0.0175  148 CYS B CA  
4031 C C   . CYS B 178 ? 0.6307 0.5047 0.6206 -0.0539 0.0712  0.0115  148 CYS B C   
4032 O O   . CYS B 178 ? 0.6346 0.5098 0.6187 -0.0480 0.0669  0.0086  148 CYS B O   
4033 C CB  . CYS B 178 ? 0.6666 0.5309 0.6390 -0.0515 0.0743  0.0182  148 CYS B CB  
4034 S SG  . CYS B 178 ? 0.7136 0.5654 0.6762 -0.0516 0.0758  0.0255  148 CYS B SG  
4035 N N   . CYS B 179 ? 0.6071 0.4871 0.6075 -0.0581 0.0736  0.0094  149 CYS B N   
4036 C CA  . CYS B 179 ? 0.5901 0.4797 0.5962 -0.0555 0.0714  0.0038  149 CYS B CA  
4037 C C   . CYS B 179 ? 0.5835 0.4647 0.5897 -0.0527 0.0641  0.0049  149 CYS B C   
4038 O O   . CYS B 179 ? 0.5857 0.4637 0.5982 -0.0559 0.0636  0.0069  149 CYS B O   
4039 C CB  . CYS B 179 ? 0.5820 0.4818 0.5990 -0.0612 0.0767  0.0009  149 CYS B CB  
4040 S SG  . CYS B 179 ? 0.5818 0.4920 0.5998 -0.0672 0.0860  0.0004  149 CYS B SG  
4041 N N   . LEU B 180 ? 0.5705 0.4475 0.5688 -0.0468 0.0583  0.0037  150 LEU B N   
4042 C CA  . LEU B 180 ? 0.5621 0.4299 0.5587 -0.0449 0.0511  0.0052  150 LEU B CA  
4043 C C   . LEU B 180 ? 0.5536 0.4248 0.5514 -0.0408 0.0480  0.0010  150 LEU B C   
4044 O O   . LEU B 180 ? 0.5502 0.4170 0.5513 -0.0416 0.0443  0.0026  150 LEU B O   
4045 C CB  . LEU B 180 ? 0.5704 0.4274 0.5559 -0.0423 0.0460  0.0074  150 LEU B CB  
4046 C CG  . LEU B 180 ? 0.5919 0.4449 0.5746 -0.0451 0.0485  0.0120  150 LEU B CG  
4047 C CD1 . LEU B 180 ? 0.6000 0.4439 0.5714 -0.0417 0.0429  0.0131  150 LEU B CD1 
4048 C CD2 . LEU B 180 ? 0.6023 0.4529 0.5927 -0.0498 0.0493  0.0165  150 LEU B CD2 
4049 N N   . ILE B 181 ? 0.5474 0.4273 0.5424 -0.0361 0.0497  -0.0042 151 ILE B N   
4050 C CA  . ILE B 181 ? 0.5453 0.4285 0.5397 -0.0306 0.0469  -0.0084 151 ILE B CA  
4051 C C   . ILE B 181 ? 0.5233 0.4172 0.5297 -0.0332 0.0501  -0.0102 151 ILE B C   
4052 O O   . ILE B 181 ? 0.5164 0.4238 0.5295 -0.0356 0.0558  -0.0130 151 ILE B O   
4053 C CB  . ILE B 181 ? 0.5567 0.4460 0.5424 -0.0226 0.0469  -0.0137 151 ILE B CB  
4054 C CG1 . ILE B 181 ? 0.5824 0.4578 0.5538 -0.0184 0.0419  -0.0127 151 ILE B CG1 
4055 C CG2 . ILE B 181 ? 0.5611 0.4554 0.5464 -0.0161 0.0449  -0.0183 151 ILE B CG2 
4056 C CD1 . ILE B 181 ? 0.6080 0.4656 0.5735 -0.0180 0.0341  -0.0102 151 ILE B CD1 
4057 N N   . VAL B 182 ? 0.5107 0.3988 0.5197 -0.0332 0.0464  -0.0084 152 VAL B N   
4058 C CA  . VAL B 182 ? 0.4966 0.3935 0.5159 -0.0348 0.0485  -0.0098 152 VAL B CA  
4059 C C   . VAL B 182 ? 0.4912 0.3904 0.5081 -0.0278 0.0455  -0.0131 152 VAL B C   
4060 O O   . VAL B 182 ? 0.4990 0.3863 0.5080 -0.0244 0.0403  -0.0110 152 VAL B O   
4061 C CB  . VAL B 182 ? 0.5027 0.3933 0.5281 -0.0404 0.0481  -0.0043 152 VAL B CB  
4062 C CG1 . VAL B 182 ? 0.5023 0.4011 0.5369 -0.0406 0.0495  -0.0061 152 VAL B CG1 
4063 C CG2 . VAL B 182 ? 0.5075 0.3963 0.5347 -0.0463 0.0518  -0.0014 152 VAL B CG2 
4064 N N   . TYR B 183 ? 0.4731 0.3875 0.4964 -0.0259 0.0487  -0.0184 153 TYR B N   
4065 C CA  . TYR B 183 ? 0.4682 0.3876 0.4898 -0.0184 0.0466  -0.0221 153 TYR B CA  
4066 C C   . TYR B 183 ? 0.4581 0.3780 0.4875 -0.0205 0.0462  -0.0202 153 TYR B C   
4067 O O   . TYR B 183 ? 0.4536 0.3792 0.4926 -0.0266 0.0495  -0.0198 153 TYR B O   
4068 C CB  . TYR B 183 ? 0.4697 0.4084 0.4944 -0.0148 0.0502  -0.0294 153 TYR B CB  
4069 C CG  . TYR B 183 ? 0.5022 0.4425 0.5183 -0.0109 0.0506  -0.0315 153 TYR B CG  
4070 C CD1 . TYR B 183 ? 0.5186 0.4601 0.5361 -0.0170 0.0542  -0.0298 153 TYR B CD1 
4071 C CD2 . TYR B 183 ? 0.5292 0.4697 0.5346 -0.0001 0.0475  -0.0351 153 TYR B CD2 
4072 C CE1 . TYR B 183 ? 0.5370 0.4813 0.5462 -0.0127 0.0548  -0.0316 153 TYR B CE1 
4073 C CE2 . TYR B 183 ? 0.5451 0.4881 0.5419 0.0048  0.0478  -0.0374 153 TYR B CE2 
4074 C CZ  . TYR B 183 ? 0.5584 0.5040 0.5574 -0.0016 0.0516  -0.0356 153 TYR B CZ  
4075 O OH  . TYR B 183 ? 0.5904 0.5390 0.5799 0.0042  0.0519  -0.0378 153 TYR B OH  
4076 N N   . HIS B 184 ? 0.4570 0.3695 0.4811 -0.0153 0.0422  -0.0186 154 HIS B N   
4077 C CA  . HIS B 184 ? 0.4573 0.3700 0.4870 -0.0159 0.0416  -0.0161 154 HIS B CA  
4078 C C   . HIS B 184 ? 0.4615 0.3823 0.4892 -0.0071 0.0408  -0.0207 154 HIS B C   
4079 O O   . HIS B 184 ? 0.4674 0.3904 0.4874 -0.0001 0.0398  -0.0248 154 HIS B O   
4080 C CB  . HIS B 184 ? 0.4749 0.3708 0.4997 -0.0186 0.0377  -0.0084 154 HIS B CB  
4081 C CG  . HIS B 184 ? 0.5052 0.3944 0.5314 -0.0259 0.0379  -0.0043 154 HIS B CG  
4082 N ND1 . HIS B 184 ? 0.5248 0.4200 0.5603 -0.0317 0.0415  -0.0033 154 HIS B ND1 
4083 C CD2 . HIS B 184 ? 0.5204 0.3972 0.5386 -0.0277 0.0348  -0.0012 154 HIS B CD2 
4084 C CE1 . HIS B 184 ? 0.5315 0.4184 0.5645 -0.0361 0.0406  0.0007  154 HIS B CE1 
4085 N NE2 . HIS B 184 ? 0.5338 0.4102 0.5569 -0.0341 0.0365  0.0019  154 HIS B NE2 
4086 N N   . PRO B 185 ? 0.4583 0.3843 0.4920 -0.0062 0.0412  -0.0202 155 PRO B N   
4087 C CA  . PRO B 185 ? 0.4608 0.3956 0.4921 0.0030  0.0405  -0.0248 155 PRO B CA  
4088 C C   . PRO B 185 ? 0.4790 0.3996 0.4981 0.0098  0.0365  -0.0208 155 PRO B C   
4089 O O   . PRO B 185 ? 0.4776 0.4041 0.4929 0.0187  0.0358  -0.0242 155 PRO B O   
4090 C CB  . PRO B 185 ? 0.4621 0.4082 0.5045 0.0010  0.0426  -0.0261 155 PRO B CB  
4091 C CG  . PRO B 185 ? 0.4633 0.4053 0.5132 -0.0091 0.0445  -0.0222 155 PRO B CG  
4092 C CD  . PRO B 185 ? 0.4503 0.3763 0.4928 -0.0124 0.0424  -0.0162 155 PRO B CD  
4093 N N   . TYR B 186 ? 0.4960 0.3983 0.5088 0.0057  0.0337  -0.0138 156 TYR B N   
4094 C CA  . TYR B 186 ? 0.5161 0.4022 0.5168 0.0102  0.0299  -0.0092 156 TYR B CA  
4095 C C   . TYR B 186 ? 0.5429 0.4237 0.5297 0.0199  0.0277  -0.0137 156 TYR B C   
4096 O O   . TYR B 186 ? 0.5439 0.4196 0.5216 0.0282  0.0261  -0.0136 156 TYR B O   
4097 C CB  . TYR B 186 ? 0.5214 0.3904 0.5195 0.0017  0.0273  -0.0013 156 TYR B CB  
4098 C CG  . TYR B 186 ? 0.5237 0.3983 0.5344 -0.0069 0.0292  0.0034  156 TYR B CG  
4099 C CD1 . TYR B 186 ? 0.5276 0.4027 0.5417 -0.0076 0.0293  0.0086  156 TYR B CD1 
4100 C CD2 . TYR B 186 ? 0.5318 0.4102 0.5496 -0.0137 0.0309  0.0031  156 TYR B CD2 
4101 C CE1 . TYR B 186 ? 0.5288 0.4094 0.5533 -0.0143 0.0308  0.0130  156 TYR B CE1 
4102 C CE2 . TYR B 186 ? 0.5358 0.4180 0.5632 -0.0203 0.0324  0.0074  156 TYR B CE2 
4103 C CZ  . TYR B 186 ? 0.5419 0.4256 0.5727 -0.0203 0.0322  0.0122  156 TYR B CZ  
4104 O OH  . TYR B 186 ? 0.5598 0.4485 0.5995 -0.0254 0.0336  0.0161  156 TYR B OH  
4105 N N   . ARG B 187 ? 0.5615 0.4434 0.5457 0.0197  0.0279  -0.0175 157 ARG B N   
4106 C CA  . ARG B 187 ? 0.5843 0.4632 0.5550 0.0299  0.0260  -0.0225 157 ARG B CA  
4107 C C   . ARG B 187 ? 0.5750 0.4728 0.5471 0.0405  0.0279  -0.0296 157 ARG B C   
4108 O O   . ARG B 187 ? 0.5855 0.4755 0.5447 0.0509  0.0253  -0.0303 157 ARG B O   
4109 C CB  . ARG B 187 ? 0.6265 0.5062 0.5960 0.0272  0.0265  -0.0249 157 ARG B CB  
4110 C CG  . ARG B 187 ? 0.7175 0.5893 0.6702 0.0378  0.0235  -0.0289 157 ARG B CG  
4111 C CD  . ARG B 187 ? 0.8063 0.6513 0.7452 0.0355  0.0185  -0.0244 157 ARG B CD  
4112 N NE  . ARG B 187 ? 0.8631 0.7052 0.8096 0.0237  0.0190  -0.0205 157 ARG B NE  
4113 C CZ  . ARG B 187 ? 0.9096 0.7323 0.8466 0.0202  0.0148  -0.0174 157 ARG B CZ  
4114 N NH1 . ARG B 187 ? 0.9202 0.7229 0.8392 0.0270  0.0097  -0.0178 157 ARG B NH1 
4115 N NH2 . ARG B 187 ? 0.9091 0.7317 0.8535 0.0103  0.0155  -0.0141 157 ARG B NH2 
4116 N N   . PRO B 188 ? 0.5555 0.4773 0.5422 0.0380  0.0320  -0.0347 158 PRO B N   
4117 C CA  . PRO B 188 ? 0.5488 0.4896 0.5370 0.0479  0.0331  -0.0416 158 PRO B CA  
4118 C C   . PRO B 188 ? 0.5591 0.4955 0.5448 0.0528  0.0317  -0.0388 158 PRO B C   
4119 O O   . PRO B 188 ? 0.5697 0.5086 0.5459 0.0650  0.0302  -0.0421 158 PRO B O   
4120 C CB  . PRO B 188 ? 0.5408 0.5055 0.5465 0.0406  0.0376  -0.0466 158 PRO B CB  
4121 C CG  . PRO B 188 ? 0.5486 0.5044 0.5620 0.0277  0.0389  -0.0409 158 PRO B CG  
4122 C CD  . PRO B 188 ? 0.5418 0.4738 0.5432 0.0265  0.0357  -0.0346 158 PRO B CD  
4123 N N   . LEU B 189 ? 0.5582 0.4875 0.5507 0.0445  0.0321  -0.0325 159 LEU B N   
4124 C CA  . LEU B 189 ? 0.5721 0.4982 0.5624 0.0490  0.0312  -0.0291 159 LEU B CA  
4125 C C   . LEU B 189 ? 0.6056 0.5124 0.5769 0.0587  0.0277  -0.0258 159 LEU B C   
4126 O O   . LEU B 189 ? 0.6095 0.5200 0.5747 0.0691  0.0272  -0.0275 159 LEU B O   
4127 C CB  . LEU B 189 ? 0.5692 0.4887 0.5679 0.0385  0.0320  -0.0215 159 LEU B CB  
4128 C CG  . LEU B 189 ? 0.5770 0.4929 0.5734 0.0423  0.0316  -0.0167 159 LEU B CG  
4129 C CD1 . LEU B 189 ? 0.5711 0.5085 0.5754 0.0484  0.0335  -0.0230 159 LEU B CD1 
4130 C CD2 . LEU B 189 ? 0.5833 0.4901 0.5851 0.0322  0.0318  -0.0081 159 LEU B CD2 
4131 N N   . LEU B 190 ? 0.6249 0.5106 0.5859 0.0554  0.0251  -0.0216 160 LEU B N   
4132 C CA  . LEU B 190 ? 0.6495 0.5123 0.5907 0.0631  0.0214  -0.0183 160 LEU B CA  
4133 C C   . LEU B 190 ? 0.6580 0.5269 0.5876 0.0784  0.0205  -0.0258 160 LEU B C   
4134 O O   . LEU B 190 ? 0.6676 0.5261 0.5832 0.0888  0.0186  -0.0246 160 LEU B O   
4135 C CB  . LEU B 190 ? 0.6640 0.5048 0.5978 0.0554  0.0185  -0.0138 160 LEU B CB  
4136 C CG  . LEU B 190 ? 0.6959 0.5159 0.6255 0.0480  0.0165  -0.0042 160 LEU B CG  
4137 C CD1 . LEU B 190 ? 0.7060 0.5150 0.6386 0.0353  0.0148  -0.0001 160 LEU B CD1 
4138 C CD2 . LEU B 190 ? 0.7215 0.5199 0.6304 0.0574  0.0133  -0.0017 160 LEU B CD2 
4139 N N   . GLN B 191 ? 0.6530 0.5398 0.5884 0.0801  0.0219  -0.0334 161 GLN B N   
4140 C CA  . GLN B 191 ? 0.6715 0.5696 0.5979 0.0950  0.0214  -0.0412 161 GLN B CA  
4141 C C   . GLN B 191 ? 0.6763 0.5948 0.6083 0.1031  0.0230  -0.0453 161 GLN B C   
4142 O O   . GLN B 191 ? 0.6890 0.6056 0.6070 0.1178  0.0212  -0.0478 161 GLN B O   
4143 C CB  . GLN B 191 ? 0.6937 0.6091 0.6268 0.0933  0.0232  -0.0478 161 GLN B CB  
4144 C CG  . GLN B 191 ? 0.7681 0.6621 0.6888 0.0917  0.0205  -0.0453 161 GLN B CG  
4145 C CD  . GLN B 191 ? 0.8339 0.7439 0.7634 0.0867  0.0231  -0.0497 161 GLN B CD  
4146 O OE1 . GLN B 191 ? 0.8441 0.7742 0.7921 0.0773  0.0272  -0.0512 161 GLN B OE1 
4147 N NE2 . GLN B 191 ? 0.8514 0.7513 0.7667 0.0930  0.0207  -0.0515 161 GLN B NE2 
4148 N N   . TYR B 192 ? 0.6648 0.6010 0.6157 0.0942  0.0261  -0.0459 162 TYR B N   
4149 C CA  . TYR B 192 ? 0.6605 0.6165 0.6179 0.1006  0.0274  -0.0500 162 TYR B CA  
4150 C C   . TYR B 192 ? 0.6715 0.6114 0.6161 0.1087  0.0255  -0.0444 162 TYR B C   
4151 O O   . TYR B 192 ? 0.6691 0.6170 0.6053 0.1230  0.0245  -0.0487 162 TYR B O   
4152 C CB  . TYR B 192 ? 0.6510 0.6247 0.6300 0.0882  0.0306  -0.0513 162 TYR B CB  
4153 C CG  . TYR B 192 ? 0.6498 0.6439 0.6412 0.0821  0.0331  -0.0583 162 TYR B CG  
4154 C CD1 . TYR B 192 ? 0.6580 0.6690 0.6460 0.0914  0.0330  -0.0664 162 TYR B CD1 
4155 C CD2 . TYR B 192 ? 0.6523 0.6491 0.6582 0.0673  0.0357  -0.0566 162 TYR B CD2 
4156 C CE1 . TYR B 192 ? 0.6588 0.6893 0.6583 0.0850  0.0358  -0.0721 162 TYR B CE1 
4157 C CE2 . TYR B 192 ? 0.6535 0.6667 0.6694 0.0610  0.0384  -0.0621 162 TYR B CE2 
4158 C CZ  . TYR B 192 ? 0.6621 0.6929 0.6754 0.0693  0.0386  -0.0698 162 TYR B CZ  
4159 O OH  . TYR B 192 ? 0.6749 0.7239 0.6984 0.0627  0.0417  -0.0749 162 TYR B OH  
4160 N N   . VAL B 193 ? 0.6853 0.6035 0.6280 0.1001  0.0250  -0.0345 163 VAL B N   
4161 C CA  . VAL B 193 ? 0.7097 0.6123 0.6402 0.1066  0.0239  -0.0279 163 VAL B CA  
4162 C C   . VAL B 193 ? 0.7431 0.6231 0.6496 0.1184  0.0206  -0.0264 163 VAL B C   
4163 O O   . VAL B 193 ? 0.7508 0.6224 0.6447 0.1286  0.0199  -0.0236 163 VAL B O   
4164 C CB  . VAL B 193 ? 0.7196 0.6086 0.6555 0.0942  0.0247  -0.0176 163 VAL B CB  
4165 C CG1 . VAL B 193 ? 0.7111 0.6196 0.6687 0.0832  0.0276  -0.0191 163 VAL B CG1 
4166 C CG2 . VAL B 193 ? 0.7381 0.5997 0.6647 0.0859  0.0224  -0.0105 163 VAL B CG2 
4167 N N   . GLN B 194 ? 0.7617 0.6310 0.6604 0.1180  0.0186  -0.0284 164 GLN B N   
4168 C CA  . GLN B 194 ? 0.7898 0.6374 0.6642 0.1305  0.0151  -0.0285 164 GLN B CA  
4169 C C   . GLN B 194 ? 0.7957 0.6648 0.6657 0.1481  0.0153  -0.0376 164 GLN B C   
4170 O O   . GLN B 194 ? 0.8121 0.6711 0.6661 0.1610  0.0140  -0.0361 164 GLN B O   
4171 C CB  . GLN B 194 ? 0.8185 0.6527 0.6867 0.1263  0.0128  -0.0296 164 GLN B CB  
4172 C CG  . GLN B 194 ? 0.8804 0.6943 0.7223 0.1417  0.0089  -0.0318 164 GLN B CG  
4173 C CD  . GLN B 194 ? 0.9356 0.7551 0.7752 0.1443  0.0078  -0.0386 164 GLN B CD  
4174 O OE1 . GLN B 194 ? 0.9452 0.7955 0.7969 0.1478  0.0103  -0.0466 164 GLN B OE1 
4175 N NE2 . GLN B 194 ? 0.9443 0.7346 0.7681 0.1424  0.0041  -0.0355 164 GLN B NE2 
4176 N N   . ASP B 195 ? 0.7801 0.6810 0.6660 0.1480  0.0174  -0.0465 165 ASP B N   
4177 C CA  . ASP B 195 ? 0.7834 0.7100 0.6679 0.1636  0.0176  -0.0559 165 ASP B CA  
4178 C C   . ASP B 195 ? 0.7877 0.7212 0.6715 0.1716  0.0181  -0.0550 165 ASP B C   
4179 O O   . ASP B 195 ? 0.7973 0.7317 0.6659 0.1890  0.0165  -0.0581 165 ASP B O   
4180 C CB  . ASP B 195 ? 0.7947 0.7558 0.7001 0.1579  0.0204  -0.0647 165 ASP B CB  
4181 C CG  . ASP B 195 ? 0.8625 0.8520 0.7664 0.1738  0.0202  -0.0749 165 ASP B CG  
4182 O OD1 . ASP B 195 ? 0.8878 0.8683 0.7715 0.1899  0.0175  -0.0766 165 ASP B OD1 
4183 O OD2 . ASP B 195 ? 0.8861 0.9068 0.8085 0.1704  0.0225  -0.0812 165 ASP B OD2 
4184 N N   . MET B 196 ? 0.7829 0.7202 0.6816 0.1597  0.0203  -0.0507 166 MET B N   
4185 C CA  . MET B 196 ? 0.7868 0.7300 0.6861 0.1655  0.0211  -0.0489 166 MET B CA  
4186 C C   . MET B 196 ? 0.8124 0.7254 0.6886 0.1745  0.0193  -0.0402 166 MET B C   
4187 O O   . MET B 196 ? 0.8099 0.7277 0.6797 0.1860  0.0194  -0.0402 166 MET B O   
4188 C CB  . MET B 196 ? 0.7787 0.7265 0.6971 0.1492  0.0236  -0.0442 166 MET B CB  
4189 C CG  . MET B 196 ? 0.7736 0.7536 0.7137 0.1437  0.0256  -0.0528 166 MET B CG  
4190 S SD  . MET B 196 ? 0.7838 0.7668 0.7388 0.1326  0.0279  -0.0473 166 MET B SD  
4191 C CE  . MET B 196 ? 0.7306 0.7502 0.7064 0.1299  0.0293  -0.0595 166 MET B CE  
4192 N N   . GLY B 197 ? 0.8356 0.7173 0.7003 0.1678  0.0178  -0.0326 167 GLY B N   
4193 C CA  . GLY B 197 ? 0.8708 0.7191 0.7139 0.1721  0.0163  -0.0229 167 GLY B CA  
4194 C C   . GLY B 197 ? 0.8847 0.7270 0.7349 0.1621  0.0185  -0.0133 167 GLY B C   
4195 O O   . GLY B 197 ? 0.9024 0.7233 0.7364 0.1671  0.0183  -0.0054 167 GLY B O   
4196 N N   . GLN B 198 ? 0.8732 0.7342 0.7470 0.1483  0.0210  -0.0136 168 GLN B N   
4197 C CA  . GLN B 198 ? 0.8844 0.7445 0.7669 0.1393  0.0234  -0.0053 168 GLN B CA  
4198 C C   . GLN B 198 ? 0.8955 0.7444 0.7880 0.1203  0.0237  0.0013  168 GLN B C   
4199 O O   . GLN B 198 ? 0.8891 0.7518 0.7995 0.1101  0.0260  0.0030  168 GLN B O   
4200 C CB  . GLN B 198 ? 0.8920 0.7850 0.7924 0.1415  0.0257  -0.0118 168 GLN B CB  
4201 C CG  . GLN B 198 ? 0.9396 0.8455 0.8308 0.1602  0.0253  -0.0176 168 GLN B CG  
4202 C CD  . GLN B 198 ? 1.0166 0.9035 0.8909 0.1677  0.0258  -0.0081 168 GLN B CD  
4203 O OE1 . GLN B 198 ? 1.0501 0.9261 0.9272 0.1579  0.0276  0.0019  168 GLN B OE1 
4204 N NE2 . GLN B 198 ? 1.0327 0.9157 0.8884 0.1856  0.0243  -0.0107 168 GLN B NE2 
4205 N N   . GLU B 199 ? 0.9099 0.7339 0.7904 0.1162  0.0210  0.0044  169 GLU B N   
4206 C CA  . GLU B 199 ? 0.9177 0.7307 0.8062 0.0990  0.0206  0.0100  169 GLU B CA  
4207 C C   . GLU B 199 ? 0.9202 0.7230 0.8107 0.0895  0.0221  0.0215  169 GLU B C   
4208 O O   . GLU B 199 ? 0.9129 0.7233 0.8195 0.0763  0.0234  0.0248  169 GLU B O   
4209 C CB  . GLU B 199 ? 0.9674 0.7545 0.8397 0.0984  0.0167  0.0103  169 GLU B CB  
4210 C CG  . GLU B 199 ? 1.0598 0.8538 0.9241 0.1115  0.0151  -0.0001 169 GLU B CG  
4211 C CD  . GLU B 199 ? 1.2045 0.9724 1.0521 0.1115  0.0111  0.0000  169 GLU B CD  
4212 O OE1 . GLU B 199 ? 1.2413 1.0016 1.0709 0.1264  0.0089  -0.0048 169 GLU B OE1 
4213 O OE2 . GLU B 199 ? 1.2516 1.0068 1.1032 0.0973  0.0098  0.0047  169 GLU B OE2 
4214 N N   . ASP B 200 ? 0.9270 0.7129 0.8009 0.0967  0.0219  0.0278  170 ASP B N   
4215 C CA  . ASP B 200 ? 0.9316 0.7081 0.8062 0.0880  0.0238  0.0395  170 ASP B CA  
4216 C C   . ASP B 200 ? 0.9112 0.7147 0.8033 0.0876  0.0276  0.0397  170 ASP B C   
4217 O O   . ASP B 200 ? 0.9124 0.7204 0.8169 0.0753  0.0293  0.0462  170 ASP B O   
4218 C CB  . ASP B 200 ? 0.9739 0.7244 0.8243 0.0964  0.0231  0.0464  170 ASP B CB  
4219 C CG  . ASP B 200 ? 1.0537 0.7696 0.8877 0.0891  0.0196  0.0520  170 ASP B CG  
4220 O OD1 . ASP B 200 ? 1.0555 0.7681 0.8945 0.0808  0.0169  0.0483  170 ASP B OD1 
4221 O OD2 . ASP B 200 ? 1.1054 0.7968 0.9207 0.0916  0.0194  0.0601  170 ASP B OD2 
4222 N N   . MET B 201 ? 0.8914 0.7140 0.7846 0.1013  0.0286  0.0320  171 MET B N   
4223 C CA  . MET B 201 ? 0.8712 0.7186 0.7788 0.1028  0.0318  0.0311  171 MET B CA  
4224 C C   . MET B 201 ? 0.8305 0.6995 0.7605 0.0932  0.0326  0.0254  171 MET B C   
4225 O O   . MET B 201 ? 0.8252 0.7037 0.7671 0.0864  0.0349  0.0299  171 MET B O   
4226 C CB  . MET B 201 ? 0.8951 0.7555 0.7954 0.1210  0.0320  0.0244  171 MET B CB  
4227 C CG  . MET B 201 ? 0.9563 0.8265 0.8582 0.1258  0.0349  0.0294  171 MET B CG  
4228 S SD  . MET B 201 ? 1.1104 1.0168 1.0259 0.1366  0.0356  0.0166  171 MET B SD  
4229 C CE  . MET B 201 ? 1.0742 0.9885 0.9935 0.1373  0.0392  0.0256  171 MET B CE  
4230 N N   . LEU B 202 ? 0.8023 0.6785 0.7373 0.0929  0.0311  0.0160  172 LEU B N   
4231 C CA  . LEU B 202 ? 0.7718 0.6678 0.7268 0.0846  0.0322  0.0101  172 LEU B CA  
4232 C C   . LEU B 202 ? 0.7466 0.6346 0.7088 0.0702  0.0315  0.0124  172 LEU B C   
4233 O O   . LEU B 202 ? 0.7332 0.6340 0.7109 0.0620  0.0331  0.0114  172 LEU B O   
4234 C CB  . LEU B 202 ? 0.7670 0.6828 0.7262 0.0930  0.0318  -0.0026 172 LEU B CB  
4235 C CG  . LEU B 202 ? 0.7825 0.7136 0.7388 0.1070  0.0323  -0.0076 172 LEU B CG  
4236 C CD1 . LEU B 202 ? 0.7860 0.7330 0.7423 0.1159  0.0310  -0.0197 172 LEU B CD1 
4237 C CD2 . LEU B 202 ? 0.7791 0.7273 0.7494 0.1042  0.0345  -0.0075 172 LEU B CD2 
4238 N N   . LEU B 203 ? 0.7367 0.6046 0.6876 0.0678  0.0290  0.0143  173 LEU B N   
4239 C CA  . LEU B 203 ? 0.7248 0.5867 0.6823 0.0552  0.0280  0.0152  173 LEU B CA  
4240 C C   . LEU B 203 ? 0.6993 0.5617 0.6683 0.0424  0.0293  0.0233  173 LEU B C   
4241 O O   . LEU B 203 ? 0.6904 0.5633 0.6725 0.0349  0.0302  0.0206  173 LEU B O   
4242 C CB  . LEU B 203 ? 0.7444 0.5827 0.6865 0.0548  0.0245  0.0165  173 LEU B CB  
4243 C CG  . LEU B 203 ? 0.7650 0.6018 0.7129 0.0458  0.0232  0.0136  173 LEU B CG  
4244 C CD1 . LEU B 203 ? 0.7601 0.6196 0.7191 0.0488  0.0251  0.0034  173 LEU B CD1 
4245 C CD2 . LEU B 203 ? 0.7884 0.6017 0.7190 0.0476  0.0194  0.0139  173 LEU B CD2 
4246 N N   . PRO B 204 ? 0.6843 0.5378 0.6492 0.0399  0.0298  0.0330  174 PRO B N   
4247 C CA  . PRO B 204 ? 0.6643 0.5224 0.6412 0.0283  0.0311  0.0402  174 PRO B CA  
4248 C C   . PRO B 204 ? 0.6312 0.5128 0.6248 0.0279  0.0339  0.0360  174 PRO B C   
4249 O O   . PRO B 204 ? 0.6259 0.5121 0.6302 0.0187  0.0342  0.0373  174 PRO B O   
4250 C CB  . PRO B 204 ? 0.6782 0.5266 0.6470 0.0285  0.0320  0.0505  174 PRO B CB  
4251 C CG  . PRO B 204 ? 0.6987 0.5275 0.6485 0.0361  0.0298  0.0502  174 PRO B CG  
4252 C CD  . PRO B 204 ? 0.6829 0.5212 0.6314 0.0471  0.0293  0.0386  174 PRO B CD  
4253 N N   . LEU B 205 ? 0.6069 0.5029 0.6020 0.0382  0.0355  0.0304  175 LEU B N   
4254 C CA  . LEU B 205 ? 0.5791 0.4956 0.5882 0.0388  0.0377  0.0254  175 LEU B CA  
4255 C C   . LEU B 205 ? 0.5603 0.4845 0.5767 0.0365  0.0373  0.0157  175 LEU B C   
4256 O O   . LEU B 205 ? 0.5572 0.4887 0.5848 0.0297  0.0384  0.0147  175 LEU B O   
4257 C CB  . LEU B 205 ? 0.5761 0.5047 0.5831 0.0507  0.0390  0.0226  175 LEU B CB  
4258 C CG  . LEU B 205 ? 0.5822 0.5313 0.6016 0.0529  0.0406  0.0156  175 LEU B CG  
4259 C CD1 . LEU B 205 ? 0.5825 0.5356 0.6117 0.0451  0.0421  0.0215  175 LEU B CD1 
4260 C CD2 . LEU B 205 ? 0.5895 0.5490 0.6047 0.0654  0.0412  0.0126  175 LEU B CD2 
4261 N N   . ALA B 206 ? 0.5502 0.4728 0.5598 0.0424  0.0360  0.0088  176 ALA B N   
4262 C CA  . ALA B 206 ? 0.5372 0.4686 0.5535 0.0401  0.0361  -0.0002 176 ALA B CA  
4263 C C   . ALA B 206 ? 0.5351 0.4574 0.5552 0.0286  0.0357  0.0030  176 ALA B C   
4264 O O   . ALA B 206 ? 0.5282 0.4592 0.5586 0.0230  0.0372  -0.0008 176 ALA B O   
4265 C CB  . ALA B 206 ? 0.5386 0.4702 0.5454 0.0491  0.0347  -0.0070 176 ALA B CB  
4266 N N   . TRP B 207 ? 0.5431 0.4471 0.5544 0.0248  0.0337  0.0104  177 TRP B N   
4267 C CA  . TRP B 207 ? 0.5497 0.4443 0.5633 0.0143  0.0327  0.0140  177 TRP B CA  
4268 C C   . TRP B 207 ? 0.5299 0.4323 0.5558 0.0069  0.0345  0.0181  177 TRP B C   
4269 O O   . TRP B 207 ? 0.5332 0.4382 0.5660 0.0005  0.0350  0.0164  177 TRP B O   
4270 C CB  . TRP B 207 ? 0.5703 0.4438 0.5715 0.0119  0.0296  0.0212  177 TRP B CB  
4271 C CG  . TRP B 207 ? 0.5961 0.4595 0.5982 0.0017  0.0277  0.0243  177 TRP B CG  
4272 C CD1 . TRP B 207 ? 0.6090 0.4729 0.6189 -0.0078 0.0277  0.0308  177 TRP B CD1 
4273 C CD2 . TRP B 207 ? 0.6153 0.4665 0.6088 0.0010  0.0250  0.0214  177 TRP B CD2 
4274 N NE1 . TRP B 207 ? 0.6209 0.4744 0.6283 -0.0147 0.0252  0.0316  177 TRP B NE1 
4275 C CE2 . TRP B 207 ? 0.6261 0.4707 0.6230 -0.0095 0.0234  0.0259  177 TRP B CE2 
4276 C CE3 . TRP B 207 ? 0.6290 0.4751 0.6117 0.0090  0.0236  0.0150  177 TRP B CE3 
4277 C CZ2 . TRP B 207 ? 0.6374 0.4699 0.6272 -0.0123 0.0204  0.0243  177 TRP B CZ2 
4278 C CZ3 . TRP B 207 ? 0.6429 0.4769 0.6183 0.0065  0.0209  0.0136  177 TRP B CZ3 
4279 C CH2 . TRP B 207 ? 0.6453 0.4723 0.6243 -0.0042 0.0193  0.0180  177 TRP B CH2 
4280 N N   . ARG B 208 ? 0.5077 0.4145 0.5356 0.0087  0.0356  0.0233  178 ARG B N   
4281 C CA  . ARG B 208 ? 0.4949 0.4104 0.5333 0.0038  0.0373  0.0272  178 ARG B CA  
4282 C C   . ARG B 208 ? 0.4856 0.4145 0.5334 0.0048  0.0392  0.0193  178 ARG B C   
4283 O O   . ARG B 208 ? 0.4886 0.4193 0.5433 -0.0014 0.0400  0.0202  178 ARG B O   
4284 C CB  . ARG B 208 ? 0.5032 0.4228 0.5407 0.0078  0.0384  0.0337  178 ARG B CB  
4285 C CG  . ARG B 208 ? 0.5098 0.4414 0.5575 0.0056  0.0403  0.0368  178 ARG B CG  
4286 C CD  . ARG B 208 ? 0.5137 0.4593 0.5649 0.0143  0.0422  0.0310  178 ARG B CD  
4287 N NE  . ARG B 208 ? 0.5111 0.4664 0.5716 0.0124  0.0436  0.0308  178 ARG B NE  
4288 C CZ  . ARG B 208 ? 0.5040 0.4672 0.5674 0.0145  0.0450  0.0366  178 ARG B CZ  
4289 N NH1 . ARG B 208 ? 0.4960 0.4668 0.5664 0.0137  0.0460  0.0356  178 ARG B NH1 
4290 N NH2 . ARG B 208 ? 0.4712 0.4343 0.5295 0.0177  0.0455  0.0437  178 ARG B NH2 
4291 N N   . ILE B 209 ? 0.4731 0.4110 0.5206 0.0124  0.0400  0.0114  179 ILE B N   
4292 C CA  . ILE B 209 ? 0.4595 0.4095 0.5154 0.0125  0.0416  0.0030  179 ILE B CA  
4293 C C   . ILE B 209 ? 0.4634 0.4098 0.5216 0.0056  0.0418  -0.0007 179 ILE B C   
4294 O O   . ILE B 209 ? 0.4674 0.4176 0.5328 0.0007  0.0433  -0.0029 179 ILE B O   
4295 C CB  . ILE B 209 ? 0.4505 0.4125 0.5056 0.0219  0.0419  -0.0048 179 ILE B CB  
4296 C CG1 . ILE B 209 ? 0.4512 0.4168 0.5037 0.0290  0.0420  -0.0002 179 ILE B CG1 
4297 C CG2 . ILE B 209 ? 0.4442 0.4184 0.5083 0.0202  0.0432  -0.0141 179 ILE B CG2 
4298 C CD1 . ILE B 209 ? 0.4559 0.4328 0.5057 0.0399  0.0418  -0.0071 179 ILE B CD1 
4299 N N   . VAL B 210 ? 0.4673 0.4046 0.5182 0.0051  0.0402  -0.0004 180 VAL B N   
4300 C CA  . VAL B 210 ? 0.4771 0.4106 0.5289 -0.0010 0.0405  -0.0030 180 VAL B CA  
4301 C C   . VAL B 210 ? 0.4920 0.4189 0.5478 -0.0095 0.0407  0.0032  180 VAL B C   
4302 O O   . VAL B 210 ? 0.4967 0.4256 0.5574 -0.0144 0.0424  0.0005  180 VAL B O   
4303 C CB  . VAL B 210 ? 0.4856 0.4101 0.5271 0.0016  0.0384  -0.0038 180 VAL B CB  
4304 C CG1 . VAL B 210 ? 0.4927 0.4127 0.5345 -0.0047 0.0386  -0.0051 180 VAL B CG1 
4305 C CG2 . VAL B 210 ? 0.4857 0.4196 0.5237 0.0109  0.0384  -0.0113 180 VAL B CG2 
4306 N N   . ASN B 211 ? 0.4931 0.4134 0.5469 -0.0110 0.0392  0.0116  181 ASN B N   
4307 C CA  . ASN B 211 ? 0.4952 0.4120 0.5530 -0.0180 0.0390  0.0178  181 ASN B CA  
4308 C C   . ASN B 211 ? 0.5087 0.4349 0.5749 -0.0183 0.0416  0.0158  181 ASN B C   
4309 O O   . ASN B 211 ? 0.5172 0.4414 0.5864 -0.0232 0.0424  0.0165  181 ASN B O   
4310 C CB  . ASN B 211 ? 0.4959 0.4082 0.5514 -0.0193 0.0373  0.0268  181 ASN B CB  
4311 C CG  . ASN B 211 ? 0.5236 0.4228 0.5694 -0.0204 0.0342  0.0299  181 ASN B CG  
4312 O OD1 . ASN B 211 ? 0.5409 0.4323 0.5817 -0.0217 0.0328  0.0267  181 ASN B OD1 
4313 N ND2 . ASN B 211 ? 0.5197 0.4155 0.5619 -0.0197 0.0332  0.0362  181 ASN B ND2 
4314 N N   . ASP B 212 ? 0.5096 0.4451 0.5783 -0.0124 0.0428  0.0131  182 ASP B N   
4315 C CA  . ASP B 212 ? 0.5155 0.4588 0.5906 -0.0114 0.0447  0.0106  182 ASP B CA  
4316 C C   . ASP B 212 ? 0.5241 0.4688 0.6024 -0.0143 0.0464  0.0027  182 ASP B C   
4317 O O   . ASP B 212 ? 0.5254 0.4697 0.6072 -0.0169 0.0478  0.0023  182 ASP B O   
4318 C CB  . ASP B 212 ? 0.5350 0.4878 0.6108 -0.0035 0.0450  0.0090  182 ASP B CB  
4319 C CG  . ASP B 212 ? 0.5977 0.5505 0.6709 -0.0010 0.0443  0.0178  182 ASP B CG  
4320 O OD1 . ASP B 212 ? 0.6173 0.5645 0.6903 -0.0062 0.0435  0.0253  182 ASP B OD1 
4321 O OD2 . ASP B 212 ? 0.6161 0.5752 0.6877 0.0060  0.0445  0.0172  182 ASP B OD2 
4322 N N   . THR B 213 ? 0.5241 0.4703 0.6005 -0.0139 0.0465  -0.0034 183 THR B N   
4323 C CA  . THR B 213 ? 0.5320 0.4810 0.6121 -0.0180 0.0486  -0.0106 183 THR B CA  
4324 C C   . THR B 213 ? 0.5447 0.4844 0.6248 -0.0253 0.0497  -0.0072 183 THR B C   
4325 O O   . THR B 213 ? 0.5494 0.4895 0.6324 -0.0296 0.0520  -0.0116 183 THR B O   
4326 C CB  . THR B 213 ? 0.5501 0.5051 0.6286 -0.0160 0.0487  -0.0173 183 THR B CB  
4327 O OG1 . THR B 213 ? 0.5695 0.5165 0.6414 -0.0162 0.0471  -0.0135 183 THR B OG1 
4328 C CG2 . THR B 213 ? 0.5497 0.5158 0.6285 -0.0080 0.0478  -0.0221 183 THR B CG2 
4329 N N   . TYR B 214 ? 0.5471 0.4784 0.6236 -0.0270 0.0480  0.0006  184 TYR B N   
4330 C CA  . TYR B 214 ? 0.5530 0.4762 0.6288 -0.0328 0.0487  0.0042  184 TYR B CA  
4331 C C   . TYR B 214 ? 0.5614 0.4839 0.6402 -0.0333 0.0498  0.0066  184 TYR B C   
4332 O O   . TYR B 214 ? 0.5738 0.4898 0.6515 -0.0372 0.0509  0.0084  184 TYR B O   
4333 C CB  . TYR B 214 ? 0.5571 0.4725 0.6279 -0.0346 0.0459  0.0105  184 TYR B CB  
4334 C CG  . TYR B 214 ? 0.5646 0.4770 0.6303 -0.0346 0.0450  0.0075  184 TYR B CG  
4335 C CD1 . TYR B 214 ? 0.5778 0.4919 0.6399 -0.0297 0.0433  0.0060  184 TYR B CD1 
4336 C CD2 . TYR B 214 ? 0.5742 0.4820 0.6374 -0.0385 0.0461  0.0062  184 TYR B CD2 
4337 C CE1 . TYR B 214 ? 0.5951 0.5062 0.6511 -0.0281 0.0423  0.0028  184 TYR B CE1 
4338 C CE2 . TYR B 214 ? 0.5885 0.4946 0.6463 -0.0373 0.0452  0.0031  184 TYR B CE2 
4339 C CZ  . TYR B 214 ? 0.6049 0.5127 0.6589 -0.0318 0.0432  0.0012  184 TYR B CZ  
4340 O OH  . TYR B 214 ? 0.6226 0.5283 0.6698 -0.0290 0.0421  -0.0020 184 TYR B OH  
4341 N N   . ARG B 215 ? 0.5559 0.4846 0.6373 -0.0286 0.0496  0.0065  185 ARG B N   
4342 C CA  . ARG B 215 ? 0.5557 0.4839 0.6388 -0.0275 0.0506  0.0077  185 ARG B CA  
4343 C C   . ARG B 215 ? 0.5484 0.4748 0.6328 -0.0298 0.0532  -0.0001 185 ARG B C   
4344 O O   . ARG B 215 ? 0.5564 0.4781 0.6401 -0.0297 0.0542  0.0001  185 ARG B O   
4345 C CB  . ARG B 215 ? 0.5755 0.5121 0.6604 -0.0208 0.0497  0.0096  185 ARG B CB  
4346 C CG  . ARG B 215 ? 0.6279 0.5661 0.7122 -0.0196 0.0479  0.0189  185 ARG B CG  
4347 C CD  . ARG B 215 ? 0.6859 0.6222 0.7679 -0.0218 0.0460  0.0224  185 ARG B CD  
4348 N NE  . ARG B 215 ? 0.7290 0.6648 0.8107 -0.0241 0.0443  0.0313  185 ARG B NE  
4349 C CZ  . ARG B 215 ? 0.7551 0.6858 0.8338 -0.0279 0.0420  0.0352  185 ARG B CZ  
4350 N NH1 . ARG B 215 ? 0.7447 0.6699 0.8194 -0.0285 0.0414  0.0311  185 ARG B NH1 
4351 N NH2 . ARG B 215 ? 0.7500 0.6816 0.8294 -0.0310 0.0403  0.0429  185 ARG B NH2 
4352 N N   . THR B 216 ? 0.5335 0.4635 0.6193 -0.0321 0.0541  -0.0070 186 THR B N   
4353 C CA  . THR B 216 ? 0.5232 0.4541 0.6113 -0.0358 0.0564  -0.0151 186 THR B CA  
4354 C C   . THR B 216 ? 0.5233 0.4502 0.6104 -0.0430 0.0587  -0.0165 186 THR B C   
4355 O O   . THR B 216 ? 0.5331 0.4575 0.6173 -0.0436 0.0579  -0.0123 186 THR B O   
4356 C CB  . THR B 216 ? 0.5223 0.4662 0.6141 -0.0317 0.0556  -0.0224 186 THR B CB  
4357 O OG1 . THR B 216 ? 0.5206 0.4700 0.6119 -0.0314 0.0551  -0.0236 186 THR B OG1 
4358 C CG2 . THR B 216 ? 0.5269 0.4762 0.6188 -0.0235 0.0535  -0.0203 186 THR B CG2 
4359 N N   . ASP B 217 ? 0.5156 0.4426 0.6049 -0.0485 0.0614  -0.0228 187 ASP B N   
4360 C CA  . ASP B 217 ? 0.5184 0.4435 0.6071 -0.0555 0.0642  -0.0241 187 ASP B CA  
4361 C C   . ASP B 217 ? 0.5061 0.4448 0.5976 -0.0550 0.0642  -0.0292 187 ASP B C   
4362 O O   . ASP B 217 ? 0.5101 0.4505 0.6019 -0.0606 0.0670  -0.0312 187 ASP B O   
4363 C CB  . ASP B 217 ? 0.5531 0.4727 0.6428 -0.0628 0.0675  -0.0284 187 ASP B CB  
4364 C CG  . ASP B 217 ? 0.6573 0.5609 0.7418 -0.0631 0.0680  -0.0236 187 ASP B CG  
4365 O OD1 . ASP B 217 ? 0.6880 0.5848 0.7681 -0.0600 0.0668  -0.0159 187 ASP B OD1 
4366 O OD2 . ASP B 217 ? 0.6888 0.5866 0.7732 -0.0664 0.0694  -0.0277 187 ASP B OD2 
4367 N N   . LEU B 218 ? 0.4914 0.4399 0.5843 -0.0479 0.0614  -0.0312 188 LEU B N   
4368 C CA  . LEU B 218 ? 0.4816 0.4437 0.5762 -0.0455 0.0611  -0.0367 188 LEU B CA  
4369 C C   . LEU B 218 ? 0.4807 0.4413 0.5712 -0.0469 0.0619  -0.0345 188 LEU B C   
4370 O O   . LEU B 218 ? 0.4815 0.4533 0.5742 -0.0485 0.0636  -0.0401 188 LEU B O   
4371 C CB  . LEU B 218 ? 0.4789 0.4483 0.5728 -0.0361 0.0578  -0.0375 188 LEU B CB  
4372 C CG  . LEU B 218 ? 0.4921 0.4687 0.5905 -0.0333 0.0570  -0.0425 188 LEU B CG  
4373 C CD1 . LEU B 218 ? 0.5007 0.4817 0.5965 -0.0234 0.0540  -0.0408 188 LEU B CD1 
4374 C CD2 . LEU B 218 ? 0.4867 0.4765 0.5913 -0.0372 0.0587  -0.0525 188 LEU B CD2 
4375 N N   . CYS B 219 ? 0.4786 0.4268 0.5632 -0.0465 0.0607  -0.0268 189 CYS B N   
4376 C CA  . CYS B 219 ? 0.4823 0.4276 0.5618 -0.0472 0.0609  -0.0248 189 CYS B CA  
4377 C C   . CYS B 219 ? 0.4767 0.4228 0.5575 -0.0549 0.0653  -0.0267 189 CYS B C   
4378 O O   . CYS B 219 ? 0.4819 0.4321 0.5599 -0.0548 0.0664  -0.0279 189 CYS B O   
4379 C CB  . CYS B 219 ? 0.5036 0.4354 0.5766 -0.0457 0.0580  -0.0167 189 CYS B CB  
4380 S SG  . CYS B 219 ? 0.5578 0.4765 0.6301 -0.0514 0.0594  -0.0102 189 CYS B SG  
4381 N N   . LEU B 220 ? 0.4653 0.4069 0.5494 -0.0611 0.0681  -0.0269 190 LEU B N   
4382 C CA  . LEU B 220 ? 0.4616 0.4020 0.5465 -0.0694 0.0728  -0.0280 190 LEU B CA  
4383 C C   . LEU B 220 ? 0.4751 0.4311 0.5673 -0.0738 0.0755  -0.0365 190 LEU B C   
4384 O O   . LEU B 220 ? 0.4811 0.4383 0.5747 -0.0817 0.0799  -0.0377 190 LEU B O   
4385 C CB  . LEU B 220 ? 0.4524 0.3774 0.5352 -0.0741 0.0744  -0.0238 190 LEU B CB  
4386 C CG  . LEU B 220 ? 0.4569 0.3675 0.5330 -0.0710 0.0722  -0.0154 190 LEU B CG  
4387 C CD1 . LEU B 220 ? 0.4609 0.3576 0.5342 -0.0749 0.0744  -0.0123 190 LEU B CD1 
4388 C CD2 . LEU B 220 ? 0.4586 0.3666 0.5289 -0.0705 0.0722  -0.0116 190 LEU B CD2 
4389 N N   . LEU B 221 ? 0.4742 0.4426 0.5714 -0.0691 0.0731  -0.0423 191 LEU B N   
4390 C CA  . LEU B 221 ? 0.4713 0.4561 0.5764 -0.0734 0.0750  -0.0511 191 LEU B CA  
4391 C C   . LEU B 221 ? 0.4722 0.4769 0.5797 -0.0672 0.0737  -0.0566 191 LEU B C   
4392 O O   . LEU B 221 ? 0.4647 0.4859 0.5781 -0.0718 0.0763  -0.0630 191 LEU B O   
4393 C CB  . LEU B 221 ? 0.4676 0.4509 0.5766 -0.0733 0.0733  -0.0546 191 LEU B CB  
4394 C CG  . LEU B 221 ? 0.4788 0.4422 0.5844 -0.0778 0.0742  -0.0498 191 LEU B CG  
4395 C CD1 . LEU B 221 ? 0.4833 0.4446 0.5902 -0.0733 0.0712  -0.0520 191 LEU B CD1 
4396 C CD2 . LEU B 221 ? 0.4847 0.4436 0.5916 -0.0896 0.0790  -0.0513 191 LEU B CD2 
4397 N N   . TYR B 222 ? 0.4801 0.4838 0.5827 -0.0568 0.0697  -0.0544 192 TYR B N   
4398 C CA  . TYR B 222 ? 0.4869 0.5076 0.5895 -0.0486 0.0679  -0.0596 192 TYR B CA  
4399 C C   . TYR B 222 ? 0.4997 0.5155 0.5931 -0.0416 0.0662  -0.0554 192 TYR B C   
4400 O O   . TYR B 222 ? 0.5147 0.5129 0.6014 -0.0400 0.0643  -0.0481 192 TYR B O   
4401 C CB  . TYR B 222 ? 0.4871 0.5127 0.5912 -0.0409 0.0642  -0.0626 192 TYR B CB  
4402 C CG  . TYR B 222 ? 0.4974 0.5296 0.6099 -0.0464 0.0651  -0.0685 192 TYR B CG  
4403 C CD1 . TYR B 222 ? 0.5032 0.5571 0.6234 -0.0481 0.0659  -0.0780 192 TYR B CD1 
4404 C CD2 . TYR B 222 ? 0.5143 0.5318 0.6267 -0.0494 0.0646  -0.0650 192 TYR B CD2 
4405 C CE1 . TYR B 222 ? 0.5111 0.5703 0.6385 -0.0535 0.0660  -0.0842 192 TYR B CE1 
4406 C CE2 . TYR B 222 ? 0.5223 0.5440 0.6408 -0.0538 0.0649  -0.0710 192 TYR B CE2 
4407 C CZ  . TYR B 222 ? 0.5261 0.5680 0.6521 -0.0562 0.0654  -0.0807 192 TYR B CZ  
4408 O OH  . TYR B 222 ? 0.5399 0.5853 0.6717 -0.0611 0.0651  -0.0873 192 TYR B OH  
4409 N N   . PRO B 223 ? 0.4915 0.5235 0.5841 -0.0366 0.0664  -0.0605 193 PRO B N   
4410 C CA  . PRO B 223 ? 0.4985 0.5245 0.5803 -0.0281 0.0641  -0.0574 193 PRO B CA  
4411 C C   . PRO B 223 ? 0.5101 0.5231 0.5847 -0.0194 0.0592  -0.0535 193 PRO B C   
4412 O O   . PRO B 223 ? 0.5085 0.5260 0.5865 -0.0162 0.0576  -0.0557 193 PRO B O   
4413 C CB  . PRO B 223 ? 0.4960 0.5452 0.5791 -0.0225 0.0650  -0.0651 193 PRO B CB  
4414 C CG  . PRO B 223 ? 0.4873 0.5542 0.5831 -0.0321 0.0690  -0.0710 193 PRO B CG  
4415 C CD  . PRO B 223 ? 0.4683 0.5252 0.5693 -0.0377 0.0684  -0.0697 193 PRO B CD  
4416 N N   . PRO B 224 ? 0.5191 0.5155 0.5834 -0.0162 0.0568  -0.0474 194 PRO B N   
4417 C CA  . PRO B 224 ? 0.5225 0.5053 0.5797 -0.0099 0.0524  -0.0428 194 PRO B CA  
4418 C C   . PRO B 224 ? 0.5179 0.5097 0.5719 0.0009  0.0500  -0.0472 194 PRO B C   
4419 O O   . PRO B 224 ? 0.5257 0.5132 0.5800 0.0035  0.0482  -0.0450 194 PRO B O   
4420 C CB  . PRO B 224 ? 0.5422 0.5085 0.5884 -0.0087 0.0502  -0.0375 194 PRO B CB  
4421 C CG  . PRO B 224 ? 0.5493 0.5167 0.5988 -0.0168 0.0538  -0.0370 194 PRO B CG  
4422 C CD  . PRO B 224 ? 0.5184 0.5074 0.5767 -0.0187 0.0578  -0.0444 194 PRO B CD  
4423 N N   . PHE B 225 ? 0.5057 0.5111 0.5566 0.0079  0.0502  -0.0534 195 PHE B N   
4424 C CA  . PHE B 225 ? 0.5007 0.5155 0.5474 0.0197  0.0479  -0.0580 195 PHE B CA  
4425 C C   . PHE B 225 ? 0.4903 0.5202 0.5477 0.0190  0.0487  -0.0626 195 PHE B C   
4426 O O   . PHE B 225 ? 0.4907 0.5226 0.5441 0.0281  0.0463  -0.0637 195 PHE B O   
4427 C CB  . PHE B 225 ? 0.4936 0.5230 0.5353 0.0279  0.0481  -0.0643 195 PHE B CB  
4428 C CG  . PHE B 225 ? 0.4885 0.5458 0.5427 0.0243  0.0517  -0.0725 195 PHE B CG  
4429 C CD1 . PHE B 225 ? 0.4951 0.5581 0.5565 0.0136  0.0558  -0.0728 195 PHE B CD1 
4430 C CD2 . PHE B 225 ? 0.4894 0.5674 0.5480 0.0311  0.0511  -0.0799 195 PHE B CD2 
4431 C CE1 . PHE B 225 ? 0.4898 0.5785 0.5631 0.0085  0.0594  -0.0800 195 PHE B CE1 
4432 C CE2 . PHE B 225 ? 0.4842 0.5891 0.5554 0.0263  0.0542  -0.0878 195 PHE B CE2 
4433 C CZ  . PHE B 225 ? 0.4777 0.5877 0.5562 0.0145  0.0584  -0.0877 195 PHE B CZ  
4434 N N   . MET B 226 ? 0.4752 0.5147 0.5452 0.0083  0.0521  -0.0652 196 MET B N   
4435 C CA  . MET B 226 ? 0.4690 0.5212 0.5486 0.0067  0.0525  -0.0702 196 MET B CA  
4436 C C   . MET B 226 ? 0.4736 0.5102 0.5523 0.0060  0.0509  -0.0640 196 MET B C   
4437 O O   . MET B 226 ? 0.4799 0.5225 0.5594 0.0123  0.0492  -0.0663 196 MET B O   
4438 C CB  . MET B 226 ? 0.4762 0.5417 0.5680 -0.0048 0.0563  -0.0753 196 MET B CB  
4439 C CG  . MET B 226 ? 0.5155 0.6059 0.6112 -0.0025 0.0577  -0.0838 196 MET B CG  
4440 S SD  . MET B 226 ? 0.6489 0.7555 0.7596 -0.0180 0.0624  -0.0899 196 MET B SD  
4441 C CE  . MET B 226 ? 0.6305 0.7678 0.7438 -0.0132 0.0639  -0.0982 196 MET B CE  
4442 N N   . ILE B 227 ? 0.4715 0.4891 0.5480 -0.0005 0.0513  -0.0560 197 ILE B N   
4443 C CA  . ILE B 227 ? 0.4739 0.4781 0.5494 -0.0009 0.0498  -0.0493 197 ILE B CA  
4444 C C   . ILE B 227 ? 0.4934 0.4909 0.5588 0.0097  0.0465  -0.0457 197 ILE B C   
4445 O O   . ILE B 227 ? 0.5022 0.4987 0.5676 0.0135  0.0454  -0.0436 197 ILE B O   
4446 C CB  . ILE B 227 ? 0.4727 0.4601 0.5476 -0.0096 0.0508  -0.0417 197 ILE B CB  
4447 C CG1 . ILE B 227 ? 0.4715 0.4636 0.5540 -0.0196 0.0545  -0.0449 197 ILE B CG1 
4448 C CG2 . ILE B 227 ? 0.4759 0.4525 0.5506 -0.0099 0.0495  -0.0349 197 ILE B CG2 
4449 C CD1 . ILE B 227 ? 0.4852 0.4624 0.5656 -0.0267 0.0556  -0.0383 197 ILE B CD1 
4450 N N   . ALA B 228 ? 0.4961 0.4887 0.5519 0.0149  0.0450  -0.0450 198 ALA B N   
4451 C CA  . ALA B 228 ? 0.5077 0.4914 0.5518 0.0249  0.0420  -0.0419 198 ALA B CA  
4452 C C   . ALA B 228 ? 0.5060 0.5050 0.5504 0.0349  0.0413  -0.0478 198 ALA B C   
4453 O O   . ALA B 228 ? 0.5157 0.5083 0.5550 0.0406  0.0398  -0.0437 198 ALA B O   
4454 C CB  . ALA B 228 ? 0.5179 0.4945 0.5511 0.0290  0.0405  -0.0420 198 ALA B CB  
4455 N N   . LEU B 229 ? 0.4882 0.5084 0.5389 0.0369  0.0426  -0.0573 199 LEU B N   
4456 C CA  . LEU B 229 ? 0.4781 0.5162 0.5302 0.0464  0.0417  -0.0643 199 LEU B CA  
4457 C C   . LEU B 229 ? 0.4707 0.5120 0.5306 0.0438  0.0420  -0.0640 199 LEU B C   
4458 O O   . LEU B 229 ? 0.4708 0.5168 0.5271 0.0532  0.0404  -0.0651 199 LEU B O   
4459 C CB  . LEU B 229 ? 0.4716 0.5341 0.5311 0.0464  0.0431  -0.0747 199 LEU B CB  
4460 C CG  . LEU B 229 ? 0.4931 0.5586 0.5437 0.0536  0.0425  -0.0769 199 LEU B CG  
4461 C CD1 . LEU B 229 ? 0.4876 0.5779 0.5481 0.0499  0.0449  -0.0858 199 LEU B CD1 
4462 C CD2 . LEU B 229 ? 0.5065 0.5705 0.5438 0.0697  0.0394  -0.0774 199 LEU B CD2 
4463 N N   . ALA B 230 ? 0.4658 0.5047 0.5353 0.0319  0.0440  -0.0629 200 ALA B N   
4464 C CA  . ALA B 230 ? 0.4719 0.5124 0.5478 0.0297  0.0442  -0.0628 200 ALA B CA  
4465 C C   . ALA B 230 ? 0.4959 0.5205 0.5644 0.0337  0.0429  -0.0531 200 ALA B C   
4466 O O   . ALA B 230 ? 0.5017 0.5313 0.5694 0.0407  0.0420  -0.0535 200 ALA B O   
4467 C CB  . ALA B 230 ? 0.4672 0.5053 0.5525 0.0168  0.0466  -0.0631 200 ALA B CB  
4468 N N   . CYS B 231 ? 0.5085 0.5151 0.5710 0.0300  0.0428  -0.0444 201 CYS B N   
4469 C CA  . CYS B 231 ? 0.5262 0.5178 0.5819 0.0319  0.0416  -0.0345 201 CYS B CA  
4470 C C   . CYS B 231 ? 0.5355 0.5260 0.5806 0.0437  0.0398  -0.0334 201 CYS B C   
4471 O O   . CYS B 231 ? 0.5416 0.5277 0.5836 0.0473  0.0395  -0.0276 201 CYS B O   
4472 C CB  . CYS B 231 ? 0.5430 0.5173 0.5951 0.0244  0.0414  -0.0270 201 CYS B CB  
4473 S SG  . CYS B 231 ? 0.5815 0.5535 0.6440 0.0117  0.0436  -0.0253 201 CYS B SG  
4474 N N   . LEU B 232 ? 0.5372 0.5315 0.5759 0.0503  0.0388  -0.0385 202 LEU B N   
4475 C CA  . LEU B 232 ? 0.5514 0.5448 0.5783 0.0633  0.0370  -0.0384 202 LEU B CA  
4476 C C   . LEU B 232 ? 0.5503 0.5622 0.5814 0.0712  0.0371  -0.0446 202 LEU B C   
4477 O O   . LEU B 232 ? 0.5571 0.5656 0.5796 0.0806  0.0362  -0.0412 202 LEU B O   
4478 C CB  . LEU B 232 ? 0.5541 0.5487 0.5729 0.0692  0.0358  -0.0435 202 LEU B CB  
4479 C CG  . LEU B 232 ? 0.5763 0.5668 0.5798 0.0839  0.0337  -0.0434 202 LEU B CG  
4480 C CD1 . LEU B 232 ? 0.5963 0.5628 0.5880 0.0846  0.0327  -0.0322 202 LEU B CD1 
4481 C CD2 . LEU B 232 ? 0.5843 0.5756 0.5795 0.0898  0.0325  -0.0484 202 LEU B CD2 
4482 N N   . HIS B 233 ? 0.5366 0.5671 0.5803 0.0672  0.0381  -0.0535 203 HIS B N   
4483 C CA  . HIS B 233 ? 0.5391 0.5880 0.5878 0.0737  0.0376  -0.0607 203 HIS B CA  
4484 C C   . HIS B 233 ? 0.5438 0.5873 0.5936 0.0736  0.0380  -0.0547 203 HIS B C   
4485 O O   . HIS B 233 ? 0.5516 0.6001 0.5959 0.0843  0.0371  -0.0549 203 HIS B O   
4486 C CB  . HIS B 233 ? 0.5483 0.6168 0.6104 0.0672  0.0384  -0.0715 203 HIS B CB  
4487 C CG  . HIS B 233 ? 0.5827 0.6713 0.6494 0.0743  0.0371  -0.0803 203 HIS B CG  
4488 N ND1 . HIS B 233 ? 0.6031 0.7108 0.6681 0.0839  0.0356  -0.0893 203 HIS B ND1 
4489 C CD2 . HIS B 233 ? 0.5968 0.6890 0.6685 0.0738  0.0369  -0.0814 203 HIS B CD2 
4490 C CE1 . HIS B 233 ? 0.6041 0.7267 0.6740 0.0883  0.0343  -0.0957 203 HIS B CE1 
4491 N NE2 . HIS B 233 ? 0.6042 0.7174 0.6777 0.0827  0.0350  -0.0914 203 HIS B NE2 
4492 N N   . VAL B 234 ? 0.5355 0.5698 0.5919 0.0625  0.0395  -0.0496 204 VAL B N   
4493 C CA  . VAL B 234 ? 0.5315 0.5620 0.5891 0.0626  0.0400  -0.0437 204 VAL B CA  
4494 C C   . VAL B 234 ? 0.5465 0.5648 0.5924 0.0694  0.0397  -0.0335 204 VAL B C   
4495 O O   . VAL B 234 ? 0.5468 0.5692 0.5901 0.0767  0.0397  -0.0314 204 VAL B O   
4496 C CB  . VAL B 234 ? 0.5311 0.5536 0.5965 0.0502  0.0415  -0.0398 204 VAL B CB  
4497 C CG1 . VAL B 234 ? 0.5334 0.5544 0.6000 0.0517  0.0420  -0.0342 204 VAL B CG1 
4498 C CG2 . VAL B 234 ? 0.5270 0.5587 0.6024 0.0428  0.0421  -0.0492 204 VAL B CG2 
4499 N N   . ALA B 235 ? 0.5575 0.5609 0.5953 0.0675  0.0392  -0.0277 205 ALA B N   
4500 C CA  . ALA B 235 ? 0.5758 0.5647 0.6012 0.0725  0.0388  -0.0180 205 ALA B CA  
4501 C C   . ALA B 235 ? 0.5890 0.5847 0.6050 0.0872  0.0380  -0.0209 205 ALA B C   
4502 O O   . ALA B 235 ? 0.5974 0.5872 0.6060 0.0926  0.0385  -0.0135 205 ALA B O   
4503 C CB  . ALA B 235 ? 0.5834 0.5547 0.6011 0.0678  0.0378  -0.0136 205 ALA B CB  
4504 N N   . CYS B 236 ? 0.5866 0.5954 0.6026 0.0938  0.0368  -0.0316 206 CYS B N   
4505 C CA  . CYS B 236 ? 0.5896 0.6086 0.5971 0.1090  0.0355  -0.0367 206 CYS B CA  
4506 C C   . CYS B 236 ? 0.5867 0.6205 0.5995 0.1143  0.0360  -0.0393 206 CYS B C   
4507 O O   . CYS B 236 ? 0.5925 0.6276 0.5955 0.1265  0.0356  -0.0375 206 CYS B O   
4508 C CB  . CYS B 236 ? 0.5924 0.6263 0.6021 0.1129  0.0342  -0.0483 206 CYS B CB  
4509 S SG  . CYS B 236 ? 0.6511 0.6694 0.6448 0.1185  0.0327  -0.0463 206 CYS B SG  
4510 N N   . VAL B 237 ? 0.5765 0.6211 0.6036 0.1060  0.0366  -0.0440 207 VAL B N   
4511 C CA  . VAL B 237 ? 0.5744 0.6322 0.6070 0.1101  0.0366  -0.0475 207 VAL B CA  
4512 C C   . VAL B 237 ? 0.5976 0.6436 0.6243 0.1116  0.0382  -0.0351 207 VAL B C   
4513 O O   . VAL B 237 ? 0.6016 0.6525 0.6211 0.1231  0.0382  -0.0335 207 VAL B O   
4514 C CB  . VAL B 237 ? 0.5663 0.6330 0.6139 0.0991  0.0368  -0.0546 207 VAL B CB  
4515 C CG1 . VAL B 237 ? 0.5680 0.6428 0.6198 0.1021  0.0368  -0.0560 207 VAL B CG1 
4516 C CG2 . VAL B 237 ? 0.5644 0.6466 0.6188 0.0975  0.0355  -0.0673 207 VAL B CG2 
4517 N N   . VAL B 238 ? 0.6101 0.6413 0.6393 0.1002  0.0398  -0.0260 208 VAL B N   
4518 C CA  . VAL B 238 ? 0.6206 0.6420 0.6468 0.0983  0.0416  -0.0137 208 VAL B CA  
4519 C C   . VAL B 238 ? 0.6552 0.6677 0.6668 0.1075  0.0420  -0.0057 208 VAL B C   
4520 O O   . VAL B 238 ? 0.6611 0.6763 0.6693 0.1133  0.0435  0.0002  208 VAL B O   
4521 C CB  . VAL B 238 ? 0.6152 0.6238 0.6469 0.0840  0.0425  -0.0069 208 VAL B CB  
4522 C CG1 . VAL B 238 ? 0.6231 0.6210 0.6502 0.0815  0.0442  0.0069  208 VAL B CG1 
4523 C CG2 . VAL B 238 ? 0.6055 0.6224 0.6502 0.0766  0.0427  -0.0128 208 VAL B CG2 
4524 N N   . GLN B 239 ? 0.6755 0.6774 0.6774 0.1099  0.0408  -0.0057 209 GLN B N   
4525 C CA  . GLN B 239 ? 0.7104 0.7001 0.6960 0.1188  0.0412  0.0020  209 GLN B CA  
4526 C C   . GLN B 239 ? 0.7327 0.7336 0.7096 0.1355  0.0401  -0.0048 209 GLN B C   
4527 O O   . GLN B 239 ? 0.7492 0.7392 0.7107 0.1445  0.0405  0.0016  209 GLN B O   
4528 C CB  . GLN B 239 ? 0.7481 0.7161 0.7244 0.1135  0.0402  0.0072  209 GLN B CB  
4529 C CG  . GLN B 239 ? 0.8074 0.7647 0.7912 0.0976  0.0409  0.0142  209 GLN B CG  
4530 C CD  . GLN B 239 ? 0.8966 0.8298 0.8681 0.0935  0.0398  0.0217  209 GLN B CD  
4531 O OE1 . GLN B 239 ? 0.9366 0.8568 0.8937 0.0995  0.0402  0.0288  209 GLN B OE1 
4532 N NE2 . GLN B 239 ? 0.9041 0.8297 0.8798 0.0833  0.0385  0.0203  209 GLN B NE2 
4533 N N   . GLN B 240 ? 0.7313 0.7534 0.7174 0.1395  0.0386  -0.0177 210 GLN B N   
4534 C CA  . GLN B 240 ? 0.7451 0.7825 0.7252 0.1552  0.0370  -0.0261 210 GLN B CA  
4535 C C   . GLN B 240 ? 0.7682 0.7983 0.7345 0.1641  0.0354  -0.0282 210 GLN B C   
4536 O O   . GLN B 240 ? 0.7812 0.8108 0.7335 0.1788  0.0349  -0.0272 210 GLN B O   
4537 C CB  . GLN B 240 ? 0.7676 0.8088 0.7415 0.1653  0.0384  -0.0208 210 GLN B CB  
4538 C CG  . GLN B 240 ? 0.8144 0.8680 0.8020 0.1596  0.0393  -0.0226 210 GLN B CG  
4539 C CD  . GLN B 240 ? 0.8883 0.9448 0.8693 0.1690  0.0412  -0.0157 210 GLN B CD  
4540 O OE1 . GLN B 240 ? 0.9168 0.9754 0.8850 0.1833  0.0410  -0.0153 210 GLN B OE1 
4541 N NE2 . GLN B 240 ? 0.8974 0.9546 0.8861 0.1619  0.0431  -0.0101 210 GLN B NE2 
4542 N N   . LYS B 241 ? 0.7700 0.7942 0.7394 0.1559  0.0345  -0.0309 211 LYS B N   
4543 C CA  . LYS B 241 ? 0.7809 0.7991 0.7385 0.1635  0.0327  -0.0340 211 LYS B CA  
4544 C C   . LYS B 241 ? 0.7778 0.8227 0.7460 0.1665  0.0309  -0.0491 211 LYS B C   
4545 O O   . LYS B 241 ? 0.7727 0.8282 0.7572 0.1546  0.0312  -0.0545 211 LYS B O   
4546 C CB  . LYS B 241 ? 0.8072 0.8026 0.7619 0.1518  0.0328  -0.0272 211 LYS B CB  
4547 C CG  . LYS B 241 ? 0.8591 0.8508 0.8051 0.1570  0.0308  -0.0327 211 LYS B CG  
4548 C CD  . LYS B 241 ? 0.9182 0.8996 0.8426 0.1742  0.0295  -0.0307 211 LYS B CD  
4549 C CE  . LYS B 241 ? 0.9558 0.9422 0.8729 0.1830  0.0271  -0.0392 211 LYS B CE  
4550 N NZ  . LYS B 241 ? 0.9985 0.9687 0.8913 0.1997  0.0258  -0.0358 211 LYS B NZ  
4551 N N   . ASP B 242 ? 0.7783 0.8351 0.7373 0.1826  0.0290  -0.0559 212 ASP B N   
4552 C CA  . ASP B 242 ? 0.7678 0.8534 0.7369 0.1863  0.0271  -0.0705 212 ASP B CA  
4553 C C   . ASP B 242 ? 0.7512 0.8355 0.7195 0.1834  0.0264  -0.0744 212 ASP B C   
4554 O O   . ASP B 242 ? 0.7594 0.8366 0.7119 0.1955  0.0251  -0.0738 212 ASP B O   
4555 C CB  . ASP B 242 ? 0.8078 0.9091 0.7668 0.2061  0.0251  -0.0764 212 ASP B CB  
4556 C CG  . ASP B 242 ? 0.8812 1.0169 0.8522 0.2103  0.0228  -0.0921 212 ASP B CG  
4557 O OD1 . ASP B 242 ? 0.8890 1.0368 0.8772 0.1965  0.0231  -0.0986 212 ASP B OD1 
4558 O OD2 . ASP B 242 ? 0.9128 1.0634 0.8754 0.2273  0.0208  -0.0979 212 ASP B OD2 
4559 N N   . ALA B 243 ? 0.7308 0.8219 0.7152 0.1682  0.0273  -0.0782 213 ALA B N   
4560 C CA  . ALA B 243 ? 0.7241 0.8162 0.7091 0.1647  0.0270  -0.0820 213 ALA B CA  
4561 C C   . ALA B 243 ? 0.7031 0.8270 0.7040 0.1616  0.0266  -0.0954 213 ALA B C   
4562 O O   . ALA B 243 ? 0.7000 0.8269 0.7070 0.1532  0.0274  -0.0981 213 ALA B O   
4563 C CB  . ALA B 243 ? 0.7292 0.7990 0.7172 0.1489  0.0288  -0.0735 213 ALA B CB  
4564 N N   . ARG B 244 ? 0.6907 0.8386 0.6979 0.1680  0.0253  -0.1040 214 ARG B N   
4565 C CA  . ARG B 244 ? 0.6824 0.8621 0.7056 0.1640  0.0246  -0.1173 214 ARG B CA  
4566 C C   . ARG B 244 ? 0.6781 0.8724 0.6983 0.1703  0.0239  -0.1238 214 ARG B C   
4567 O O   . ARG B 244 ? 0.6677 0.8768 0.7013 0.1592  0.0251  -0.1298 214 ARG B O   
4568 C CB  . ARG B 244 ? 0.6983 0.9005 0.7256 0.1727  0.0224  -0.1256 214 ARG B CB  
4569 C CG  . ARG B 244 ? 0.7565 0.9511 0.7906 0.1649  0.0231  -0.1221 214 ARG B CG  
4570 C CD  . ARG B 244 ? 0.8196 1.0352 0.8550 0.1758  0.0205  -0.1303 214 ARG B CD  
4571 N NE  . ARG B 244 ? 0.8896 1.1059 0.9075 0.1965  0.0188  -0.1288 214 ARG B NE  
4572 C CZ  . ARG B 244 ? 0.9409 1.1592 0.9515 0.2085  0.0175  -0.1279 214 ARG B CZ  
4573 N NH1 . ARG B 244 ? 0.9503 1.1677 0.9435 0.2276  0.0163  -0.1261 214 ARG B NH1 
4574 N NH2 . ARG B 244 ? 0.9440 1.1641 0.9633 0.2023  0.0176  -0.1285 214 ARG B NH2 
4575 N N   . GLN B 245 ? 0.6843 0.8744 0.6863 0.1885  0.0222  -0.1225 215 GLN B N   
4576 C CA  . GLN B 245 ? 0.6862 0.8900 0.6825 0.1978  0.0212  -0.1285 215 GLN B CA  
4577 C C   . GLN B 245 ? 0.6879 0.8742 0.6830 0.1876  0.0231  -0.1231 215 GLN B C   
4578 O O   . GLN B 245 ? 0.6764 0.8825 0.6810 0.1827  0.0239  -0.1301 215 GLN B O   
4579 C CB  . GLN B 245 ? 0.7287 0.9267 0.7026 0.2208  0.0187  -0.1272 215 GLN B CB  
4580 C CG  . GLN B 245 ? 0.7901 1.0078 0.7582 0.2332  0.0173  -0.1353 215 GLN B CG  
4581 C CD  . GLN B 245 ? 0.8756 1.0867 0.8197 0.2574  0.0147  -0.1343 215 GLN B CD  
4582 O OE1 . GLN B 245 ? 0.9038 1.1161 0.8413 0.2682  0.0134  -0.1340 215 GLN B OE1 
4583 N NE2 . GLN B 245 ? 0.8902 1.0939 0.8196 0.2674  0.0140  -0.1340 215 GLN B NE2 
4584 N N   . TRP B 246 ? 0.6987 0.8492 0.6831 0.1833  0.0239  -0.1108 216 TRP B N   
4585 C CA  . TRP B 246 ? 0.7046 0.8358 0.6864 0.1738  0.0253  -0.1051 216 TRP B CA  
4586 C C   . TRP B 246 ? 0.6898 0.8353 0.6928 0.1552  0.0278  -0.1091 216 TRP B C   
4587 O O   . TRP B 246 ? 0.6850 0.8375 0.6901 0.1521  0.0288  -0.1121 216 TRP B O   
4588 C CB  . TRP B 246 ? 0.7194 0.8120 0.6892 0.1698  0.0255  -0.0916 216 TRP B CB  
4589 C CG  . TRP B 246 ? 0.7329 0.8034 0.6972 0.1618  0.0260  -0.0858 216 TRP B CG  
4590 C CD1 . TRP B 246 ? 0.7555 0.8058 0.7001 0.1714  0.0242  -0.0822 216 TRP B CD1 
4591 C CD2 . TRP B 246 ? 0.7338 0.7974 0.7110 0.1431  0.0282  -0.0822 216 TRP B CD2 
4592 N NE1 . TRP B 246 ? 0.7648 0.7981 0.7099 0.1598  0.0249  -0.0775 216 TRP B NE1 
4593 C CE2 . TRP B 246 ? 0.7536 0.7956 0.7188 0.1425  0.0274  -0.0774 216 TRP B CE2 
4594 C CE3 . TRP B 246 ? 0.7299 0.8038 0.7266 0.1276  0.0305  -0.0834 216 TRP B CE3 
4595 C CZ2 . TRP B 246 ? 0.7627 0.7937 0.7352 0.1271  0.0290  -0.0732 216 TRP B CZ2 
4596 C CZ3 . TRP B 246 ? 0.7407 0.8028 0.7439 0.1127  0.0323  -0.0789 216 TRP B CZ3 
4597 C CH2 . TRP B 246 ? 0.7531 0.7950 0.7446 0.1126  0.0315  -0.0740 216 TRP B CH2 
4598 N N   . PHE B 247 ? 0.6810 0.8313 0.6985 0.1438  0.0290  -0.1094 217 PHE B N   
4599 C CA  . PHE B 247 ? 0.6788 0.8400 0.7156 0.1258  0.0315  -0.1128 217 PHE B CA  
4600 C C   . PHE B 247 ? 0.6752 0.8726 0.7243 0.1255  0.0316  -0.1256 217 PHE B C   
4601 O O   . PHE B 247 ? 0.6706 0.8762 0.7303 0.1134  0.0341  -0.1280 217 PHE B O   
4602 C CB  . PHE B 247 ? 0.6728 0.8275 0.7187 0.1162  0.0321  -0.1098 217 PHE B CB  
4603 C CG  . PHE B 247 ? 0.6915 0.8154 0.7340 0.1067  0.0335  -0.0978 217 PHE B CG  
4604 C CD1 . PHE B 247 ? 0.7005 0.8175 0.7518 0.0911  0.0359  -0.0954 217 PHE B CD1 
4605 C CD2 . PHE B 247 ? 0.7120 0.8150 0.7425 0.1131  0.0325  -0.0887 217 PHE B CD2 
4606 C CE1 . PHE B 247 ? 0.7165 0.8074 0.7649 0.0830  0.0368  -0.0847 217 PHE B CE1 
4607 C CE2 . PHE B 247 ? 0.7281 0.8058 0.7567 0.1037  0.0337  -0.0779 217 PHE B CE2 
4608 C CZ  . PHE B 247 ? 0.7231 0.7955 0.7607 0.0891  0.0356  -0.0763 217 PHE B CZ  
4609 N N   . ALA B 248 ? 0.6738 0.8938 0.7214 0.1391  0.0292  -0.1336 218 ALA B N   
4610 C CA  . ALA B 248 ? 0.6664 0.9239 0.7254 0.1401  0.0289  -0.1463 218 ALA B CA  
4611 C C   . ALA B 248 ? 0.6734 0.9375 0.7257 0.1460  0.0296  -0.1475 218 ALA B C   
4612 O O   . ALA B 248 ? 0.6634 0.9520 0.7285 0.1382  0.0314  -0.1544 218 ALA B O   
4613 C CB  . ALA B 248 ? 0.6615 0.9407 0.7182 0.1553  0.0256  -0.1542 218 ALA B CB  
4614 N N   . GLU B 249 ? 0.6899 0.9309 0.7220 0.1590  0.0284  -0.1404 219 GLU B N   
4615 C CA  . GLU B 249 ? 0.6999 0.9426 0.7222 0.1666  0.0286  -0.1410 219 GLU B CA  
4616 C C   . GLU B 249 ? 0.7039 0.9335 0.7315 0.1507  0.0319  -0.1359 219 GLU B C   
4617 O O   . GLU B 249 ? 0.7071 0.9375 0.7268 0.1562  0.0322  -0.1361 219 GLU B O   
4618 C CB  . GLU B 249 ? 0.7452 0.9641 0.7419 0.1861  0.0258  -0.1353 219 GLU B CB  
4619 C CG  . GLU B 249 ? 0.7966 1.0339 0.7853 0.2059  0.0227  -0.1418 219 GLU B CG  
4620 C CD  . GLU B 249 ? 0.8835 1.0909 0.8472 0.2225  0.0202  -0.1342 219 GLU B CD  
4621 O OE1 . GLU B 249 ? 0.9037 1.0745 0.8566 0.2176  0.0207  -0.1235 219 GLU B OE1 
4622 O OE2 . GLU B 249 ? 0.9066 1.1274 0.8614 0.2403  0.0178  -0.1391 219 GLU B OE2 
4623 N N   . LEU B 250 ? 0.7030 0.9207 0.7429 0.1323  0.0341  -0.1314 220 LEU B N   
4624 C CA  . LEU B 250 ? 0.7119 0.9179 0.7569 0.1173  0.0372  -0.1266 220 LEU B CA  
4625 C C   . LEU B 250 ? 0.7057 0.9429 0.7699 0.1052  0.0403  -0.1348 220 LEU B C   
4626 O O   . LEU B 250 ? 0.6946 0.9512 0.7725 0.0994  0.0404  -0.1412 220 LEU B O   
4627 C CB  . LEU B 250 ? 0.7190 0.8965 0.7669 0.1038  0.0382  -0.1174 220 LEU B CB  
4628 C CG  . LEU B 250 ? 0.7449 0.8923 0.7783 0.1106  0.0358  -0.1085 220 LEU B CG  
4629 C CD1 . LEU B 250 ? 0.7496 0.8808 0.7914 0.0965  0.0371  -0.1021 220 LEU B CD1 
4630 C CD2 . LEU B 250 ? 0.7665 0.8891 0.7825 0.1166  0.0347  -0.1016 220 LEU B CD2 
4631 N N   . SER B 251 ? 0.7111 0.9520 0.7760 0.1005  0.0430  -0.1343 221 SER B N   
4632 C CA  . SER B 251 ? 0.7074 0.9761 0.7901 0.0871  0.0468  -0.1406 221 SER B CA  
4633 C C   . SER B 251 ? 0.7189 0.9673 0.8100 0.0674  0.0499  -0.1339 221 SER B C   
4634 O O   . SER B 251 ? 0.7261 0.9632 0.8147 0.0610  0.0525  -0.1288 221 SER B O   
4635 C CB  . SER B 251 ? 0.7194 1.0044 0.7979 0.0932  0.0484  -0.1432 221 SER B CB  
4636 O OG  . SER B 251 ? 0.7602 1.0156 0.8228 0.0974  0.0481  -0.1347 221 SER B OG  
4637 N N   . VAL B 252 ? 0.7185 0.9602 0.8175 0.0593  0.0493  -0.1337 222 VAL B N   
4638 C CA  . VAL B 252 ? 0.7276 0.9488 0.8334 0.0423  0.0517  -0.1276 222 VAL B CA  
4639 C C   . VAL B 252 ? 0.7195 0.9555 0.8411 0.0307  0.0525  -0.1340 222 VAL B C   
4640 O O   . VAL B 252 ? 0.7127 0.9668 0.8378 0.0375  0.0498  -0.1415 222 VAL B O   
4641 C CB  . VAL B 252 ? 0.7513 0.9377 0.8456 0.0456  0.0495  -0.1176 222 VAL B CB  
4642 C CG1 . VAL B 252 ? 0.7725 0.9377 0.8521 0.0514  0.0492  -0.1098 222 VAL B CG1 
4643 C CG2 . VAL B 252 ? 0.7550 0.9425 0.8443 0.0580  0.0456  -0.1195 222 VAL B CG2 
4644 N N   . ASP B 253 ? 0.7189 0.9448 0.8488 0.0136  0.0559  -0.1311 223 ASP B N   
4645 C CA  . ASP B 253 ? 0.7196 0.9536 0.8626 0.0013  0.0565  -0.1366 223 ASP B CA  
4646 C C   . ASP B 253 ? 0.7335 0.9479 0.8717 0.0061  0.0532  -0.1332 223 ASP B C   
4647 O O   . ASP B 253 ? 0.7534 0.9403 0.8869 0.0013  0.0539  -0.1244 223 ASP B O   
4648 C CB  . ASP B 253 ? 0.7440 0.9679 0.8939 -0.0173 0.0613  -0.1330 223 ASP B CB  
4649 C CG  . ASP B 253 ? 0.7932 1.0273 0.9567 -0.0320 0.0625  -0.1399 223 ASP B CG  
4650 O OD1 . ASP B 253 ? 0.8026 1.0409 0.9689 -0.0288 0.0590  -0.1453 223 ASP B OD1 
4651 O OD2 . ASP B 253 ? 0.8132 1.0497 0.9836 -0.0468 0.0669  -0.1398 223 ASP B OD2 
4652 N N   . MET B 254 ? 0.7193 0.9487 0.8578 0.0165  0.0495  -0.1399 224 MET B N   
4653 C CA  . MET B 254 ? 0.7204 0.9338 0.8537 0.0225  0.0465  -0.1368 224 MET B CA  
4654 C C   . MET B 254 ? 0.7118 0.9149 0.8529 0.0093  0.0473  -0.1371 224 MET B C   
4655 O O   . MET B 254 ? 0.7211 0.9081 0.8573 0.0135  0.0454  -0.1328 224 MET B O   
4656 C CB  . MET B 254 ? 0.7238 0.9558 0.8540 0.0382  0.0425  -0.1436 224 MET B CB  
4657 C CG  . MET B 254 ? 0.7611 0.9897 0.8770 0.0549  0.0410  -0.1395 224 MET B CG  
4658 S SD  . MET B 254 ? 0.8422 1.0308 0.9425 0.0590  0.0409  -0.1244 224 MET B SD  
4659 C CE  . MET B 254 ? 0.8150 0.9950 0.9168 0.0599  0.0389  -0.1232 224 MET B CE  
4660 N N   . GLU B 255 ? 0.6950 0.9063 0.8473 -0.0062 0.0500  -0.1418 225 GLU B N   
4661 C CA  . GLU B 255 ? 0.6943 0.8917 0.8519 -0.0187 0.0507  -0.1418 225 GLU B CA  
4662 C C   . GLU B 255 ? 0.6906 0.8571 0.8413 -0.0237 0.0532  -0.1297 225 GLU B C   
4663 O O   . GLU B 255 ? 0.6985 0.8459 0.8455 -0.0232 0.0520  -0.1252 225 GLU B O   
4664 C CB  . GLU B 255 ? 0.7230 0.9374 0.8936 -0.0343 0.0528  -0.1507 225 GLU B CB  
4665 C CG  . GLU B 255 ? 0.8191 1.0140 0.9929 -0.0488 0.0542  -0.1496 225 GLU B CG  
4666 C CD  . GLU B 255 ? 0.9331 1.1137 1.1032 -0.0440 0.0506  -0.1499 225 GLU B CD  
4667 O OE1 . GLU B 255 ? 0.9530 1.1486 1.1234 -0.0333 0.0465  -0.1565 225 GLU B OE1 
4668 O OE2 . GLU B 255 ? 0.9710 1.1259 1.1373 -0.0501 0.0519  -0.1437 225 GLU B OE2 
4669 N N   . LYS B 256 ? 0.6746 0.8374 0.8229 -0.0270 0.0564  -0.1245 226 LYS B N   
4670 C CA  . LYS B 256 ? 0.6707 0.8066 0.8121 -0.0309 0.0585  -0.1133 226 LYS B CA  
4671 C C   . LYS B 256 ? 0.6596 0.7777 0.7905 -0.0192 0.0555  -0.1056 226 LYS B C   
4672 O O   . LYS B 256 ? 0.6673 0.7639 0.7950 -0.0229 0.0559  -0.0983 226 LYS B O   
4673 C CB  . LYS B 256 ? 0.6931 0.8326 0.8325 -0.0329 0.0615  -0.1104 226 LYS B CB  
4674 C CG  . LYS B 256 ? 0.7414 0.8951 0.8908 -0.0469 0.0657  -0.1156 226 LYS B CG  
4675 C CD  . LYS B 256 ? 0.8076 0.9399 0.9582 -0.0609 0.0687  -0.1108 226 LYS B CD  
4676 C CE  . LYS B 256 ? 0.8503 0.9891 1.0061 -0.0740 0.0740  -0.1111 226 LYS B CE  
4677 N NZ  . LYS B 256 ? 0.8930 1.0047 1.0438 -0.0828 0.0770  -0.1022 226 LYS B NZ  
4678 N N   . ILE B 257 ? 0.6396 0.7672 0.7650 -0.0052 0.0526  -0.1071 227 ILE B N   
4679 C CA  . ILE B 257 ? 0.6371 0.7492 0.7523 0.0057  0.0500  -0.0998 227 ILE B CA  
4680 C C   . ILE B 257 ? 0.6293 0.7358 0.7467 0.0058  0.0484  -0.1001 227 ILE B C   
4681 O O   . ILE B 257 ? 0.6411 0.7285 0.7533 0.0066  0.0481  -0.0916 227 ILE B O   
4682 C CB  . ILE B 257 ? 0.6385 0.7629 0.7466 0.0208  0.0474  -0.1025 227 ILE B CB  
4683 C CG1 . ILE B 257 ? 0.6493 0.7790 0.7537 0.0225  0.0487  -0.1025 227 ILE B CG1 
4684 C CG2 . ILE B 257 ? 0.6487 0.7574 0.7459 0.0317  0.0449  -0.0951 227 ILE B CG2 
4685 C CD1 . ILE B 257 ? 0.6760 0.7823 0.7726 0.0194  0.0497  -0.0926 227 ILE B CD1 
4686 N N   . LEU B 258 ? 0.6053 0.7295 0.7306 0.0047  0.0473  -0.1101 228 LEU B N   
4687 C CA  . LEU B 258 ? 0.5967 0.7174 0.7239 0.0053  0.0456  -0.1121 228 LEU B CA  
4688 C C   . LEU B 258 ? 0.5817 0.6833 0.7110 -0.0065 0.0476  -0.1077 228 LEU B C   
4689 O O   . LEU B 258 ? 0.5860 0.6761 0.7124 -0.0038 0.0464  -0.1042 228 LEU B O   
4690 C CB  . LEU B 258 ? 0.5971 0.7419 0.7321 0.0062  0.0435  -0.1250 228 LEU B CB  
4691 C CG  . LEU B 258 ? 0.6218 0.7852 0.7530 0.0213  0.0406  -0.1295 228 LEU B CG  
4692 C CD1 . LEU B 258 ? 0.6192 0.8101 0.7597 0.0207  0.0386  -0.1432 228 LEU B CD1 
4693 C CD2 . LEU B 258 ? 0.6395 0.7918 0.7609 0.0342  0.0385  -0.1231 228 LEU B CD2 
4694 N N   . GLU B 259 ? 0.5633 0.6613 0.6965 -0.0188 0.0508  -0.1073 229 GLU B N   
4695 C CA  . GLU B 259 ? 0.5597 0.6377 0.6930 -0.0292 0.0530  -0.1024 229 GLU B CA  
4696 C C   . GLU B 259 ? 0.5525 0.6103 0.6772 -0.0244 0.0530  -0.0903 229 GLU B C   
4697 O O   . GLU B 259 ? 0.5621 0.6064 0.6843 -0.0241 0.0524  -0.0863 229 GLU B O   
4698 C CB  . GLU B 259 ? 0.5924 0.6711 0.7303 -0.0424 0.0569  -0.1035 229 GLU B CB  
4699 C CG  . GLU B 259 ? 0.6631 0.7618 0.8107 -0.0503 0.0574  -0.1149 229 GLU B CG  
4700 C CD  . GLU B 259 ? 0.7731 0.8736 0.9251 -0.0637 0.0620  -0.1151 229 GLU B CD  
4701 O OE1 . GLU B 259 ? 0.8007 0.8907 0.9477 -0.0644 0.0645  -0.1069 229 GLU B OE1 
4702 O OE2 . GLU B 259 ? 0.8089 0.9217 0.9692 -0.0738 0.0630  -0.1235 229 GLU B OE2 
4703 N N   . ILE B 260 ? 0.5355 0.5926 0.6553 -0.0200 0.0533  -0.0851 230 ILE B N   
4704 C CA  . ILE B 260 ? 0.5290 0.5686 0.6410 -0.0164 0.0530  -0.0740 230 ILE B CA  
4705 C C   . ILE B 260 ? 0.5243 0.5609 0.6322 -0.0067 0.0503  -0.0708 230 ILE B C   
4706 O O   . ILE B 260 ? 0.5330 0.5554 0.6378 -0.0070 0.0503  -0.0631 230 ILE B O   
4707 C CB  . ILE B 260 ? 0.5288 0.5689 0.6356 -0.0133 0.0532  -0.0709 230 ILE B CB  
4708 C CG1 . ILE B 260 ? 0.5275 0.5743 0.6385 -0.0219 0.0561  -0.0747 230 ILE B CG1 
4709 C CG2 . ILE B 260 ? 0.5466 0.5673 0.6457 -0.0121 0.0526  -0.0598 230 ILE B CG2 
4710 C CD1 . ILE B 260 ? 0.5386 0.5909 0.6444 -0.0164 0.0559  -0.0742 230 ILE B CD1 
4711 N N   . ILE B 261 ? 0.5085 0.5600 0.6164 0.0024  0.0482  -0.0767 231 ILE B N   
4712 C CA  . ILE B 261 ? 0.4987 0.5499 0.6024 0.0127  0.0460  -0.0741 231 ILE B CA  
4713 C C   . ILE B 261 ? 0.4910 0.5365 0.5975 0.0099  0.0459  -0.0742 231 ILE B C   
4714 O O   . ILE B 261 ? 0.4871 0.5228 0.5893 0.0137  0.0456  -0.0664 231 ILE B O   
4715 C CB  . ILE B 261 ? 0.4908 0.5608 0.5939 0.0231  0.0438  -0.0818 231 ILE B CB  
4716 C CG1 . ILE B 261 ? 0.5016 0.5728 0.5979 0.0290  0.0435  -0.0795 231 ILE B CG1 
4717 C CG2 . ILE B 261 ? 0.4932 0.5649 0.5927 0.0333  0.0418  -0.0807 231 ILE B CG2 
4718 C CD1 . ILE B 261 ? 0.5147 0.6052 0.6104 0.0386  0.0417  -0.0877 231 ILE B CD1 
4719 N N   . ARG B 262 ? 0.4876 0.5385 0.6008 0.0027  0.0463  -0.0827 232 ARG B N   
4720 C CA  . ARG B 262 ? 0.5033 0.5469 0.6178 0.0001  0.0460  -0.0841 232 ARG B CA  
4721 C C   . ARG B 262 ? 0.5176 0.5416 0.6286 -0.0043 0.0478  -0.0739 232 ARG B C   
4722 O O   . ARG B 262 ? 0.5217 0.5391 0.6295 0.0005  0.0469  -0.0697 232 ARG B O   
4723 C CB  . ARG B 262 ? 0.5236 0.5739 0.6450 -0.0089 0.0462  -0.0950 232 ARG B CB  
4724 C CG  . ARG B 262 ? 0.5695 0.6412 0.6948 -0.0031 0.0435  -0.1060 232 ARG B CG  
4725 C CD  . ARG B 262 ? 0.6230 0.7031 0.7562 -0.0138 0.0436  -0.1172 232 ARG B CD  
4726 N NE  . ARG B 262 ? 0.6716 0.7764 0.8101 -0.0110 0.0421  -0.1264 232 ARG B NE  
4727 C CZ  . ARG B 262 ? 0.7001 0.8173 0.8464 -0.0212 0.0435  -0.1335 232 ARG B CZ  
4728 N NH1 . ARG B 262 ? 0.6948 0.8001 0.8439 -0.0355 0.0466  -0.1323 232 ARG B NH1 
4729 N NH2 . ARG B 262 ? 0.6880 0.8302 0.8390 -0.0169 0.0419  -0.1417 232 ARG B NH2 
4730 N N   . VAL B 263 ? 0.5210 0.5370 0.6319 -0.0122 0.0500  -0.0697 233 VAL B N   
4731 C CA  . VAL B 263 ? 0.5319 0.5306 0.6391 -0.0159 0.0515  -0.0601 233 VAL B CA  
4732 C C   . VAL B 263 ? 0.5407 0.5359 0.6428 -0.0075 0.0501  -0.0507 233 VAL B C   
4733 O O   . VAL B 263 ? 0.5502 0.5368 0.6500 -0.0062 0.0501  -0.0449 233 VAL B O   
4734 C CB  . VAL B 263 ? 0.5361 0.5289 0.6435 -0.0247 0.0539  -0.0577 233 VAL B CB  
4735 C CG1 . VAL B 263 ? 0.5500 0.5261 0.6531 -0.0275 0.0549  -0.0479 233 VAL B CG1 
4736 C CG2 . VAL B 263 ? 0.5325 0.5289 0.6451 -0.0342 0.0559  -0.0660 233 VAL B CG2 
4737 N N   . ILE B 264 ? 0.5320 0.5342 0.6318 -0.0016 0.0490  -0.0494 234 ILE B N   
4738 C CA  . ILE B 264 ? 0.5341 0.5330 0.6285 0.0055  0.0479  -0.0407 234 ILE B CA  
4739 C C   . ILE B 264 ? 0.5333 0.5369 0.6272 0.0134  0.0468  -0.0403 234 ILE B C   
4740 O O   . ILE B 264 ? 0.5350 0.5328 0.6263 0.0155  0.0469  -0.0319 234 ILE B O   
4741 C CB  . ILE B 264 ? 0.5332 0.5367 0.6235 0.0105  0.0469  -0.0405 234 ILE B CB  
4742 C CG1 . ILE B 264 ? 0.5418 0.5393 0.6311 0.0038  0.0478  -0.0395 234 ILE B CG1 
4743 C CG2 . ILE B 264 ? 0.5373 0.5366 0.6213 0.0176  0.0458  -0.0319 234 ILE B CG2 
4744 C CD1 . ILE B 264 ? 0.5509 0.5537 0.6358 0.0091  0.0468  -0.0419 234 ILE B CD1 
4745 N N   . LEU B 265 ? 0.5254 0.5406 0.6217 0.0177  0.0458  -0.0496 235 LEU B N   
4746 C CA  . LEU B 265 ? 0.5222 0.5427 0.6173 0.0260  0.0446  -0.0504 235 LEU B CA  
4747 C C   . LEU B 265 ? 0.5407 0.5525 0.6367 0.0227  0.0452  -0.0489 235 LEU B C   
4748 O O   . LEU B 265 ? 0.5453 0.5563 0.6385 0.0288  0.0450  -0.0434 235 LEU B O   
4749 C CB  . LEU B 265 ? 0.5055 0.5407 0.6029 0.0310  0.0429  -0.0621 235 LEU B CB  
4750 C CG  . LEU B 265 ? 0.5010 0.5471 0.5964 0.0372  0.0419  -0.0647 235 LEU B CG  
4751 C CD1 . LEU B 265 ? 0.4955 0.5580 0.5940 0.0419  0.0399  -0.0767 235 LEU B CD1 
4752 C CD2 . LEU B 265 ? 0.5047 0.5487 0.5928 0.0464  0.0418  -0.0555 235 LEU B CD2 
4753 N N   . LYS B 266 ? 0.5504 0.5555 0.6494 0.0133  0.0461  -0.0534 236 LYS B N   
4754 C CA  . LYS B 266 ? 0.5684 0.5622 0.6665 0.0099  0.0467  -0.0525 236 LYS B CA  
4755 C C   . LYS B 266 ? 0.5819 0.5666 0.6768 0.0102  0.0478  -0.0405 236 LYS B C   
4756 O O   . LYS B 266 ? 0.5941 0.5755 0.6864 0.0147  0.0476  -0.0370 236 LYS B O   
4757 C CB  . LYS B 266 ? 0.6012 0.5878 0.7021 -0.0014 0.0480  -0.0587 236 LYS B CB  
4758 C CG  . LYS B 266 ? 0.6793 0.6504 0.7770 -0.0049 0.0489  -0.0568 236 LYS B CG  
4759 C CD  . LYS B 266 ? 0.7606 0.7248 0.8599 -0.0146 0.0497  -0.0653 236 LYS B CD  
4760 C CE  . LYS B 266 ? 0.8288 0.7745 0.9221 -0.0164 0.0504  -0.0626 236 LYS B CE  
4761 N NZ  . LYS B 266 ? 0.8620 0.7978 0.9549 -0.0259 0.0511  -0.0708 236 LYS B NZ  
4762 N N   . LEU B 267 ? 0.5764 0.5580 0.6712 0.0060  0.0487  -0.0345 237 LEU B N   
4763 C CA  . LEU B 267 ? 0.5764 0.5508 0.6688 0.0049  0.0492  -0.0235 237 LEU B CA  
4764 C C   . LEU B 267 ? 0.5726 0.5531 0.6631 0.0136  0.0485  -0.0169 237 LEU B C   
4765 O O   . LEU B 267 ? 0.5829 0.5597 0.6722 0.0141  0.0488  -0.0096 237 LEU B O   
4766 C CB  . LEU B 267 ? 0.5792 0.5510 0.6712 0.0000  0.0495  -0.0201 237 LEU B CB  
4767 C CG  . LEU B 267 ? 0.5974 0.5660 0.6866 0.0008  0.0489  -0.0094 237 LEU B CG  
4768 C CD1 . LEU B 267 ? 0.6101 0.5692 0.6989 -0.0047 0.0496  -0.0031 237 LEU B CD1 
4769 C CD2 . LEU B 267 ? 0.6039 0.5730 0.6909 0.0004  0.0482  -0.0088 237 LEU B CD2 
4770 N N   . TYR B 268 ? 0.5581 0.5487 0.6480 0.0206  0.0476  -0.0191 238 TYR B N   
4771 C CA  . TYR B 268 ? 0.5570 0.5539 0.6445 0.0287  0.0474  -0.0121 238 TYR B CA  
4772 C C   . TYR B 268 ? 0.5581 0.5587 0.6451 0.0351  0.0473  -0.0137 238 TYR B C   
4773 O O   . TYR B 268 ? 0.5575 0.5611 0.6431 0.0394  0.0479  -0.0056 238 TYR B O   
4774 C CB  . TYR B 268 ? 0.5558 0.5605 0.6408 0.0349  0.0468  -0.0130 238 TYR B CB  
4775 C CG  . TYR B 268 ? 0.5634 0.5621 0.6464 0.0301  0.0468  -0.0083 238 TYR B CG  
4776 C CD1 . TYR B 268 ? 0.5745 0.5656 0.6565 0.0251  0.0472  0.0017  238 TYR B CD1 
4777 C CD2 . TYR B 268 ? 0.5716 0.5725 0.6534 0.0308  0.0460  -0.0146 238 TYR B CD2 
4778 C CE1 . TYR B 268 ? 0.5904 0.5740 0.6695 0.0206  0.0467  0.0052  238 TYR B CE1 
4779 C CE2 . TYR B 268 ? 0.5873 0.5811 0.6657 0.0272  0.0457  -0.0110 238 TYR B CE2 
4780 C CZ  . TYR B 268 ? 0.6020 0.5861 0.6788 0.0219  0.0459  -0.0012 238 TYR B CZ  
4781 O OH  . TYR B 268 ? 0.6204 0.5959 0.6927 0.0187  0.0451  0.0020  238 TYR B OH  
4782 N N   . GLU B 269 ? 0.5589 0.5591 0.6468 0.0353  0.0465  -0.0240 239 GLU B N   
4783 C CA  . GLU B 269 ? 0.5660 0.5666 0.6518 0.0414  0.0460  -0.0265 239 GLU B CA  
4784 C C   . GLU B 269 ? 0.5707 0.5604 0.6553 0.0373  0.0469  -0.0212 239 GLU B C   
4785 O O   . GLU B 269 ? 0.5727 0.5643 0.6545 0.0441  0.0470  -0.0171 239 GLU B O   
4786 C CB  . GLU B 269 ? 0.5956 0.5973 0.6820 0.0419  0.0443  -0.0397 239 GLU B CB  
4787 C CG  . GLU B 269 ? 0.6535 0.6687 0.7406 0.0482  0.0429  -0.0454 239 GLU B CG  
4788 C CD  . GLU B 269 ? 0.7287 0.7544 0.8123 0.0600  0.0429  -0.0396 239 GLU B CD  
4789 O OE1 . GLU B 269 ? 0.7408 0.7672 0.8214 0.0667  0.0428  -0.0374 239 GLU B OE1 
4790 O OE2 . GLU B 269 ? 0.7344 0.7672 0.8174 0.0631  0.0431  -0.0371 239 GLU B OE2 
4791 N N   . GLN B 270 ? 0.5708 0.5499 0.6567 0.0272  0.0478  -0.0208 240 GLN B N   
4792 C CA  . GLN B 270 ? 0.5796 0.5481 0.6634 0.0238  0.0487  -0.0153 240 GLN B CA  
4793 C C   . GLN B 270 ? 0.5728 0.5468 0.6569 0.0262  0.0491  -0.0034 240 GLN B C   
4794 O O   . GLN B 270 ? 0.5758 0.5493 0.6577 0.0301  0.0493  0.0015  240 GLN B O   
4795 C CB  . GLN B 270 ? 0.6095 0.5662 0.6942 0.0129  0.0497  -0.0176 240 GLN B CB  
4796 C CG  . GLN B 270 ? 0.6745 0.6208 0.7566 0.0093  0.0507  -0.0103 240 GLN B CG  
4797 C CD  . GLN B 270 ? 0.7568 0.6930 0.8333 0.0126  0.0508  -0.0117 240 GLN B CD  
4798 O OE1 . GLN B 270 ? 0.7961 0.7184 0.8696 0.0065  0.0518  -0.0142 240 GLN B OE1 
4799 N NE2 . GLN B 270 ? 0.7542 0.6964 0.8281 0.0227  0.0498  -0.0097 240 GLN B NE2 
4800 N N   . TRP B 271 ? 0.5619 0.5418 0.6483 0.0244  0.0491  0.0008  241 TRP B N   
4801 C CA  . TRP B 271 ? 0.5536 0.5390 0.6405 0.0251  0.0494  0.0118  241 TRP B CA  
4802 C C   . TRP B 271 ? 0.5534 0.5501 0.6393 0.0350  0.0497  0.0158  241 TRP B C   
4803 O O   . TRP B 271 ? 0.5570 0.5569 0.6431 0.0361  0.0502  0.0234  241 TRP B O   
4804 C CB  . TRP B 271 ? 0.5428 0.5306 0.6302 0.0228  0.0491  0.0133  241 TRP B CB  
4805 C CG  . TRP B 271 ? 0.5383 0.5273 0.6259 0.0197  0.0491  0.0241  241 TRP B CG  
4806 C CD1 . TRP B 271 ? 0.5385 0.5357 0.6267 0.0228  0.0497  0.0329  241 TRP B CD1 
4807 C CD2 . TRP B 271 ? 0.5357 0.5181 0.6224 0.0129  0.0484  0.0268  241 TRP B CD2 
4808 N NE1 . TRP B 271 ? 0.5394 0.5352 0.6278 0.0170  0.0493  0.0410  241 TRP B NE1 
4809 C CE2 . TRP B 271 ? 0.5408 0.5262 0.6276 0.0112  0.0483  0.0372  241 TRP B CE2 
4810 C CE3 . TRP B 271 ? 0.5392 0.5139 0.6248 0.0083  0.0478  0.0212  241 TRP B CE3 
4811 C CZ2 . TRP B 271 ? 0.5495 0.5279 0.6346 0.0044  0.0471  0.0418  241 TRP B CZ2 
4812 C CZ3 . TRP B 271 ? 0.5505 0.5190 0.6338 0.0032  0.0468  0.0259  241 TRP B CZ3 
4813 C CH2 . TRP B 271 ? 0.5538 0.5230 0.6364 0.0013  0.0463  0.0358  241 TRP B CH2 
4814 N N   . LYS B 272 ? 0.5496 0.5531 0.6342 0.0425  0.0494  0.0102  242 LYS B N   
4815 C CA  . LYS B 272 ? 0.5517 0.5667 0.6344 0.0532  0.0498  0.0126  242 LYS B CA  
4816 C C   . LYS B 272 ? 0.5635 0.5757 0.6438 0.0575  0.0496  0.0114  242 LYS B C   
4817 O O   . LYS B 272 ? 0.5745 0.5956 0.6541 0.0633  0.0504  0.0187  242 LYS B O   
4818 C CB  . LYS B 272 ? 0.5717 0.5927 0.6527 0.0603  0.0489  0.0046  242 LYS B CB  
4819 C CG  . LYS B 272 ? 0.6122 0.6405 0.6897 0.0719  0.0484  0.0004  242 LYS B CG  
4820 C CD  . LYS B 272 ? 0.6742 0.7057 0.7506 0.0760  0.0468  -0.0102 242 LYS B CD  
4821 C CE  . LYS B 272 ? 0.7316 0.7696 0.8038 0.0877  0.0455  -0.0160 242 LYS B CE  
4822 N NZ  . LYS B 272 ? 0.7640 0.8086 0.8353 0.0925  0.0438  -0.0251 242 LYS B NZ  
4823 N N   . ASN B 273 ? 0.5623 0.5623 0.6407 0.0546  0.0486  0.0025  243 ASN B N   
4824 C CA  . ASN B 273 ? 0.5706 0.5643 0.6442 0.0595  0.0482  0.0005  243 ASN B CA  
4825 C C   . ASN B 273 ? 0.5763 0.5617 0.6491 0.0546  0.0489  0.0066  243 ASN B C   
4826 O O   . ASN B 273 ? 0.5911 0.5683 0.6583 0.0587  0.0485  0.0046  243 ASN B O   
4827 C CB  . ASN B 273 ? 0.5950 0.5780 0.6655 0.0590  0.0467  -0.0120 243 ASN B CB  
4828 C CG  . ASN B 273 ? 0.6471 0.6394 0.7176 0.0654  0.0454  -0.0192 243 ASN B CG  
4829 O OD1 . ASN B 273 ? 0.6689 0.6583 0.7413 0.0605  0.0445  -0.0280 243 ASN B OD1 
4830 N ND2 . ASN B 273 ? 0.6541 0.6594 0.7224 0.0769  0.0455  -0.0155 243 ASN B ND2 
4831 N N   . PHE B 274 ? 0.5651 0.5517 0.6423 0.0466  0.0496  0.0138  244 PHE B N   
4832 C CA  . PHE B 274 ? 0.5690 0.5485 0.6454 0.0419  0.0499  0.0191  244 PHE B CA  
4833 C C   . PHE B 274 ? 0.5711 0.5639 0.6510 0.0427  0.0503  0.0304  244 PHE B C   
4834 O O   . PHE B 274 ? 0.5779 0.5782 0.6621 0.0390  0.0505  0.0346  244 PHE B O   
4835 C CB  . PHE B 274 ? 0.5703 0.5370 0.6482 0.0304  0.0500  0.0161  244 PHE B CB  
4836 C CG  . PHE B 274 ? 0.5801 0.5398 0.6576 0.0240  0.0503  0.0217  244 PHE B CG  
4837 C CD1 . PHE B 274 ? 0.5961 0.5501 0.6687 0.0279  0.0503  0.0238  244 PHE B CD1 
4838 C CD2 . PHE B 274 ? 0.5853 0.5427 0.6662 0.0150  0.0502  0.0241  244 PHE B CD2 
4839 C CE1 . PHE B 274 ? 0.6066 0.5544 0.6781 0.0228  0.0503  0.0286  244 PHE B CE1 
4840 C CE2 . PHE B 274 ? 0.5980 0.5490 0.6779 0.0097  0.0501  0.0286  244 PHE B CE2 
4841 C CZ  . PHE B 274 ? 0.6013 0.5476 0.6767 0.0134  0.0502  0.0307  244 PHE B CZ  
4842 N N   . ASP B 275 ? 0.5672 0.5630 0.6449 0.0474  0.0503  0.0352  245 ASP B N   
4843 C CA  . ASP B 275 ? 0.5664 0.5767 0.6483 0.0470  0.0505  0.0459  245 ASP B CA  
4844 C C   . ASP B 275 ? 0.5650 0.5665 0.6457 0.0414  0.0498  0.0483  245 ASP B C   
4845 O O   . ASP B 275 ? 0.5702 0.5703 0.6462 0.0478  0.0497  0.0490  245 ASP B O   
4846 C CB  . ASP B 275 ? 0.5943 0.6204 0.6746 0.0591  0.0511  0.0498  245 ASP B CB  
4847 C CG  . ASP B 275 ? 0.6573 0.7039 0.7440 0.0581  0.0518  0.0610  245 ASP B CG  
4848 O OD1 . ASP B 275 ? 0.6563 0.7027 0.7474 0.0482  0.0512  0.0662  245 ASP B OD1 
4849 O OD2 . ASP B 275 ? 0.6855 0.7488 0.7726 0.0670  0.0530  0.0646  245 ASP B OD2 
4850 N N   . GLU B 276 ? 0.5556 0.5505 0.6394 0.0305  0.0493  0.0495  246 GLU B N   
4851 C CA  . GLU B 276 ? 0.5562 0.5424 0.6384 0.0252  0.0486  0.0514  246 GLU B CA  
4852 C C   . GLU B 276 ? 0.5392 0.5387 0.6226 0.0288  0.0479  0.0596  246 GLU B C   
4853 O O   . GLU B 276 ? 0.5440 0.5369 0.6229 0.0305  0.0474  0.0599  246 GLU B O   
4854 C CB  . GLU B 276 ? 0.5899 0.5683 0.6748 0.0137  0.0479  0.0514  246 GLU B CB  
4855 C CG  . GLU B 276 ? 0.6608 0.6500 0.7515 0.0086  0.0471  0.0574  246 GLU B CG  
4856 C CD  . GLU B 276 ? 0.7644 0.7457 0.8560 -0.0017 0.0456  0.0587  246 GLU B CD  
4857 O OE1 . GLU B 276 ? 0.7928 0.7810 0.8880 -0.0066 0.0444  0.0644  246 GLU B OE1 
4858 O OE2 . GLU B 276 ? 0.7882 0.7557 0.8763 -0.0050 0.0457  0.0541  246 GLU B OE2 
4859 N N   A ARG B 277 ? 0.5210 0.5398 0.6102 0.0302  0.0479  0.0664  247 ARG B N   
4860 N N   B ARG B 277 ? 0.5212 0.5400 0.6105 0.0302  0.0479  0.0663  247 ARG B N   
4861 C CA  A ARG B 277 ? 0.5086 0.5443 0.6006 0.0330  0.0473  0.0744  247 ARG B CA  
4862 C CA  B ARG B 277 ? 0.5094 0.5452 0.6014 0.0331  0.0473  0.0743  247 ARG B CA  
4863 C C   A ARG B 277 ? 0.5126 0.5514 0.5984 0.0462  0.0477  0.0731  247 ARG B C   
4864 C C   B ARG B 277 ? 0.5130 0.5515 0.5987 0.0461  0.0477  0.0730  247 ARG B C   
4865 O O   A ARG B 277 ? 0.5120 0.5557 0.5963 0.0490  0.0468  0.0767  247 ARG B O   
4866 O O   B ARG B 277 ? 0.5125 0.5556 0.5966 0.0489  0.0468  0.0765  247 ARG B O   
4867 C CB  A ARG B 277 ? 0.4977 0.5538 0.5976 0.0302  0.0476  0.0822  247 ARG B CB  
4868 C CB  B ARG B 277 ? 0.4997 0.5561 0.5994 0.0310  0.0478  0.0820  247 ARG B CB  
4869 C CG  A ARG B 277 ? 0.5010 0.5505 0.6046 0.0180  0.0469  0.0831  247 ARG B CG  
4870 C CG  B ARG B 277 ? 0.5028 0.5562 0.6074 0.0178  0.0466  0.0851  247 ARG B CG  
4871 C CD  A ARG B 277 ? 0.5021 0.5679 0.6128 0.0109  0.0462  0.0926  247 ARG B CD  
4872 C CD  B ARG B 277 ? 0.5103 0.5699 0.6180 0.0157  0.0479  0.0877  247 ARG B CD  
4873 N NE  A ARG B 277 ? 0.5129 0.5673 0.6248 -0.0013 0.0445  0.0930  247 ARG B NE  
4874 N NE  B ARG B 277 ? 0.5296 0.5713 0.6344 0.0107  0.0477  0.0815  247 ARG B NE  
4875 C CZ  A ARG B 277 ? 0.5203 0.5815 0.6368 -0.0107 0.0425  0.0996  247 ARG B CZ  
4876 C CZ  B ARG B 277 ? 0.5446 0.5810 0.6462 0.0164  0.0490  0.0753  247 ARG B CZ  
4877 N NH1 A ARG B 277 ? 0.5001 0.5819 0.6220 -0.0100 0.0422  0.1065  247 ARG B NH1 
4878 N NH1 B ARG B 277 ? 0.5375 0.5832 0.6376 0.0271  0.0505  0.0742  247 ARG B NH1 
4879 N NH2 A ARG B 277 ? 0.5172 0.5650 0.6328 -0.0208 0.0406  0.0989  247 ARG B NH2 
4880 N NH2 B ARG B 277 ? 0.5406 0.5630 0.6400 0.0118  0.0486  0.0698  247 ARG B NH2 
4881 N N   . LYS B 278 ? 0.5160 0.5501 0.5969 0.0546  0.0488  0.0672  248 LYS B N   
4882 C CA  . LYS B 278 ? 0.5276 0.5615 0.6004 0.0681  0.0490  0.0651  248 LYS B CA  
4883 C C   . LYS B 278 ? 0.5455 0.5537 0.6082 0.0692  0.0485  0.0576  248 LYS B C   
4884 O O   . LYS B 278 ? 0.5531 0.5575 0.6073 0.0792  0.0482  0.0571  248 LYS B O   
4885 C CB  . LYS B 278 ? 0.5518 0.5949 0.6234 0.0780  0.0500  0.0628  248 LYS B CB  
4886 C CG  . LYS B 278 ? 0.6013 0.6688 0.6819 0.0769  0.0512  0.0705  248 LYS B CG  
4887 C CD  . LYS B 278 ? 0.6557 0.7337 0.7334 0.0893  0.0524  0.0687  248 LYS B CD  
4888 C CE  . LYS B 278 ? 0.6816 0.7838 0.7673 0.0887  0.0542  0.0772  248 LYS B CE  
4889 N NZ  . LYS B 278 ? 0.7049 0.8181 0.7867 0.1021  0.0555  0.0756  248 LYS B NZ  
4890 N N   . GLU B 279 ? 0.5481 0.5381 0.6107 0.0592  0.0487  0.0519  249 GLU B N   
4891 C CA  . GLU B 279 ? 0.5569 0.5221 0.6101 0.0587  0.0489  0.0450  249 GLU B CA  
4892 C C   . GLU B 279 ? 0.5595 0.5122 0.6112 0.0501  0.0488  0.0466  249 GLU B C   
4893 O O   . GLU B 279 ? 0.5690 0.5024 0.6112 0.0515  0.0492  0.0430  249 GLU B O   
4894 C CB  . GLU B 279 ? 0.5837 0.5369 0.6367 0.0546  0.0494  0.0361  249 GLU B CB  
4895 C CG  . GLU B 279 ? 0.6409 0.6048 0.6948 0.0626  0.0494  0.0331  249 GLU B CG  
4896 C CD  . GLU B 279 ? 0.7308 0.6858 0.7860 0.0573  0.0495  0.0243  249 GLU B CD  
4897 O OE1 . GLU B 279 ? 0.7408 0.6774 0.7928 0.0501  0.0498  0.0186  249 GLU B OE1 
4898 O OE2 . GLU B 279 ? 0.7616 0.7292 0.8210 0.0603  0.0494  0.0233  249 GLU B OE2 
4899 N N   . MET B 280 ? 0.5512 0.5130 0.6111 0.0412  0.0482  0.0517  250 MET B N   
4900 C CA  . MET B 280 ? 0.5635 0.5134 0.6219 0.0327  0.0479  0.0524  250 MET B CA  
4901 C C   . MET B 280 ? 0.5783 0.5250 0.6299 0.0375  0.0472  0.0563  250 MET B C   
4902 O O   . MET B 280 ? 0.5926 0.5226 0.6388 0.0327  0.0478  0.0546  250 MET B O   
4903 C CB  . MET B 280 ? 0.5624 0.5209 0.6299 0.0222  0.0469  0.0561  250 MET B CB  
4904 C CG  . MET B 280 ? 0.5678 0.5179 0.6382 0.0141  0.0478  0.0505  250 MET B CG  
4905 S SD  . MET B 280 ? 0.5272 0.4539 0.5902 0.0119  0.0498  0.0410  250 MET B SD  
4906 C CE  . MET B 280 ? 0.4864 0.3996 0.5427 0.0087  0.0500  0.0436  250 MET B CE  
4907 N N   . ALA B 281 ? 0.5702 0.5334 0.6217 0.0469  0.0462  0.0615  251 ALA B N   
4908 C CA  . ALA B 281 ? 0.5766 0.5375 0.6208 0.0528  0.0453  0.0650  251 ALA B CA  
4909 C C   . ALA B 281 ? 0.5911 0.5276 0.6206 0.0600  0.0467  0.0597  251 ALA B C   
4910 O O   . ALA B 281 ? 0.6069 0.5298 0.6281 0.0604  0.0467  0.0605  251 ALA B O   
4911 C CB  . ALA B 281 ? 0.5716 0.5585 0.6195 0.0617  0.0439  0.0715  251 ALA B CB  
4912 N N   . THR B 282 ? 0.5863 0.5158 0.6121 0.0652  0.0477  0.0541  252 THR B N   
4913 C CA  . THR B 282 ? 0.5923 0.4966 0.6038 0.0711  0.0487  0.0482  252 THR B CA  
4914 C C   . THR B 282 ? 0.5926 0.4743 0.6024 0.0587  0.0504  0.0431  252 THR B C   
4915 O O   . THR B 282 ? 0.6086 0.4679 0.6067 0.0590  0.0515  0.0416  252 THR B O   
4916 C CB  . THR B 282 ? 0.6096 0.5150 0.6183 0.0798  0.0486  0.0432  252 THR B CB  
4917 O OG1 . THR B 282 ? 0.6169 0.5506 0.6344 0.0860  0.0477  0.0477  252 THR B OG1 
4918 C CG2 . THR B 282 ? 0.6278 0.5131 0.6193 0.0917  0.0485  0.0399  252 THR B CG2 
4919 N N   . ILE B 283 ? 0.5720 0.4596 0.5929 0.0480  0.0508  0.0406  253 ILE B N   
4920 C CA  . ILE B 283 ? 0.5769 0.4469 0.5973 0.0363  0.0526  0.0357  253 ILE B CA  
4921 C C   . ILE B 283 ? 0.6004 0.4635 0.6184 0.0306  0.0531  0.0400  253 ILE B C   
4922 O O   . ILE B 283 ? 0.6150 0.4578 0.6260 0.0253  0.0551  0.0371  253 ILE B O   
4923 C CB  . ILE B 283 ? 0.5645 0.4433 0.5962 0.0279  0.0527  0.0318  253 ILE B CB  
4924 C CG1 . ILE B 283 ? 0.5600 0.4450 0.5928 0.0346  0.0522  0.0271  253 ILE B CG1 
4925 C CG2 . ILE B 283 ? 0.5777 0.4402 0.6087 0.0166  0.0547  0.0267  253 ILE B CG2 
4926 C CD1 . ILE B 283 ? 0.5573 0.4528 0.6003 0.0286  0.0521  0.0235  253 ILE B CD1 
4927 N N   . LEU B 284 ? 0.6056 0.4855 0.6286 0.0319  0.0512  0.0470  254 LEU B N   
4928 C CA  . LEU B 284 ? 0.6262 0.5011 0.6462 0.0279  0.0511  0.0511  254 LEU B CA  
4929 C C   . LEU B 284 ? 0.6594 0.5193 0.6647 0.0368  0.0517  0.0527  254 LEU B C   
4930 O O   . LEU B 284 ? 0.6743 0.5206 0.6730 0.0332  0.0528  0.0540  254 LEU B O   
4931 C CB  . LEU B 284 ? 0.6168 0.5145 0.6465 0.0262  0.0483  0.0574  254 LEU B CB  
4932 C CG  . LEU B 284 ? 0.6286 0.5351 0.6698 0.0153  0.0477  0.0568  254 LEU B CG  
4933 C CD1 . LEU B 284 ? 0.6231 0.5515 0.6731 0.0141  0.0446  0.0631  254 LEU B CD1 
4934 C CD2 . LEU B 284 ? 0.6424 0.5335 0.6812 0.0059  0.0490  0.0542  254 LEU B CD2 
4935 N N   . SER B 285 ? 0.6696 0.5314 0.6686 0.0493  0.0510  0.0529  255 SER B N   
4936 C CA  . SER B 285 ? 0.7005 0.5463 0.6834 0.0595  0.0514  0.0543  255 SER B CA  
4937 C C   . SER B 285 ? 0.7380 0.5519 0.7084 0.0565  0.0543  0.0486  255 SER B C   
4938 O O   . SER B 285 ? 0.7575 0.5518 0.7144 0.0591  0.0556  0.0502  255 SER B O   
4939 C CB  . SER B 285 ? 0.7079 0.5669 0.6871 0.0750  0.0496  0.0565  255 SER B CB  
4940 O OG  . SER B 285 ? 0.7352 0.5851 0.7095 0.0804  0.0502  0.0508  255 SER B OG  
4941 N N   . LYS B 286 ? 0.7421 0.5512 0.7169 0.0509  0.0553  0.0420  256 LYS B N   
4942 C CA  . LYS B 286 ? 0.7652 0.5463 0.7304 0.0459  0.0578  0.0358  256 LYS B CA  
4943 C C   . LYS B 286 ? 0.7948 0.5635 0.7607 0.0323  0.0606  0.0357  256 LYS B C   
4944 O O   . LYS B 286 ? 0.8140 0.5571 0.7686 0.0285  0.0633  0.0332  256 LYS B O   
4945 C CB  . LYS B 286 ? 0.7742 0.5592 0.7466 0.0428  0.0575  0.0285  256 LYS B CB  
4946 C CG  . LYS B 286 ? 0.8091 0.5992 0.7770 0.0564  0.0553  0.0266  256 LYS B CG  
4947 C CD  . LYS B 286 ? 0.8532 0.6368 0.8233 0.0521  0.0554  0.0177  256 LYS B CD  
4948 C CE  . LYS B 286 ? 0.8894 0.6780 0.8551 0.0653  0.0532  0.0146  256 LYS B CE  
4949 N NZ  . LYS B 286 ? 0.9073 0.6859 0.8732 0.0605  0.0529  0.0048  256 LYS B NZ  
4950 N N   . MET B 287 ? 0.7970 0.5836 0.7757 0.0248  0.0601  0.0384  257 MET B N   
4951 C CA  . MET B 287 ? 0.8186 0.5995 0.7999 0.0128  0.0623  0.0387  257 MET B CA  
4952 C C   . MET B 287 ? 0.8571 0.6180 0.8240 0.0142  0.0644  0.0426  257 MET B C   
4953 O O   . MET B 287 ? 0.8619 0.6239 0.8211 0.0248  0.0628  0.0475  257 MET B O   
4954 C CB  . MET B 287 ? 0.8106 0.6158 0.8053 0.0096  0.0599  0.0424  257 MET B CB  
4955 C CG  . MET B 287 ? 0.8257 0.6295 0.8251 -0.0019 0.0615  0.0420  257 MET B CG  
4956 S SD  . MET B 287 ? 0.8116 0.6416 0.8255 -0.0050 0.0580  0.0451  257 MET B SD  
4957 C CE  . MET B 287 ? 0.7650 0.6029 0.7740 0.0041  0.0550  0.0530  257 MET B CE  
4958 N N   . PRO B 288 ? 0.8856 0.6296 0.8485 0.0040  0.0681  0.0409  258 PRO B N   
4959 C CA  . PRO B 288 ? 0.9170 0.6415 0.8652 0.0055  0.0706  0.0454  258 PRO B CA  
4960 C C   . PRO B 288 ? 0.9437 0.6817 0.8940 0.0076  0.0688  0.0518  258 PRO B C   
4961 O O   . PRO B 288 ? 0.9336 0.6910 0.8973 0.0019  0.0671  0.0518  258 PRO B O   
4962 C CB  . PRO B 288 ? 0.9259 0.6337 0.8724 -0.0078 0.0753  0.0418  258 PRO B CB  
4963 C CG  . PRO B 288 ? 0.9136 0.6401 0.8772 -0.0165 0.0745  0.0370  258 PRO B CG  
4964 C CD  . PRO B 288 ? 0.8813 0.6242 0.8525 -0.0088 0.0705  0.0350  258 PRO B CD  
4965 N N   . LYS B 289 ? 0.9759 0.7034 0.9122 0.0165  0.0688  0.0569  259 LYS B N   
4966 C CA  . LYS B 289 ? 0.9999 0.7407 0.9372 0.0198  0.0665  0.0626  259 LYS B CA  
4967 C C   . LYS B 289 ? 1.0409 0.7636 0.9660 0.0166  0.0699  0.0658  259 LYS B C   
4968 O O   . LYS B 289 ? 1.0546 0.7515 0.9667 0.0149  0.0743  0.0652  259 LYS B O   
4969 C CB  . LYS B 289 ? 1.0199 0.7726 0.9536 0.0344  0.0625  0.0664  259 LYS B CB  
4970 C CG  . LYS B 289 ? 1.0527 0.8251 0.9981 0.0381  0.0595  0.0640  259 LYS B CG  
4971 C CD  . LYS B 289 ? 1.0755 0.8711 1.0402 0.0283  0.0575  0.0626  259 LYS B CD  
4972 C CE  . LYS B 289 ? 1.0960 0.9133 1.0711 0.0335  0.0544  0.0622  259 LYS B CE  
4973 N NZ  . LYS B 289 ? 1.1224 0.9289 1.0924 0.0386  0.0559  0.0579  259 LYS B NZ  
4974 N N   . PRO B 290 ? 1.0580 0.7935 0.9871 0.0151  0.0681  0.0692  260 PRO B N   
4975 C CA  . PRO B 290 ? 1.0884 0.8085 1.0062 0.0122  0.0715  0.0723  260 PRO B CA  
4976 C C   . PRO B 290 ? 1.1355 0.8358 1.0330 0.0233  0.0731  0.0769  260 PRO B C   
4977 O O   . PRO B 290 ? 1.1402 0.8495 1.0339 0.0354  0.0692  0.0798  260 PRO B O   
4978 C CB  . PRO B 290 ? 1.0835 0.8247 1.0104 0.0104  0.0677  0.0743  260 PRO B CB  
4979 C CG  . PRO B 290 ? 1.0698 0.8346 1.0145 0.0077  0.0635  0.0713  260 PRO B CG  
4980 C CD  . PRO B 290 ? 1.0442 0.8078 0.9877 0.0150  0.0630  0.0701  260 PRO B CD  
4981 N N   . LYS B 291 ? 1.1674 0.8411 1.0511 0.0191  0.0788  0.0779  261 LYS B N   
4982 C CA  . LYS B 291 ? 1.2067 0.8572 1.0683 0.0291  0.0810  0.0828  261 LYS B CA  
4983 C C   . LYS B 291 ? 1.2315 0.8930 1.0895 0.0349  0.0787  0.0880  261 LYS B C   
4984 O O   . LYS B 291 ? 1.2297 0.8995 1.0948 0.0263  0.0794  0.0881  261 LYS B O   
4985 C CB  . LYS B 291 ? 1.2415 0.8611 1.0905 0.0203  0.0882  0.0829  261 LYS B CB  
4986 C CG  . LYS B 291 ? 1.3080 0.9005 1.1322 0.0293  0.0914  0.0889  261 LYS B CG  
4987 C CD  . LYS B 291 ? 1.3765 0.9365 1.1880 0.0197  0.0987  0.0889  261 LYS B CD  
4988 C CE  . LYS B 291 ? 1.4330 0.9758 1.2403 0.0198  0.0989  0.0844  261 LYS B CE  
4989 N NZ  . LYS B 291 ? 1.4776 0.9874 1.2721 0.0091  0.1058  0.0843  261 LYS B NZ  
4990 N N   . PRO B 292 ? 1.2523 0.9165 1.1001 0.0500  0.0753  0.0918  262 PRO B N   
4991 C CA  . PRO B 292 ? 1.2597 0.9365 1.1046 0.0559  0.0724  0.0961  262 PRO B CA  
4992 C C   . PRO B 292 ? 1.2861 0.9383 1.1115 0.0566  0.0776  0.1007  262 PRO B C   
4993 O O   . PRO B 292 ? 1.2987 0.9217 1.1098 0.0551  0.0833  0.1017  262 PRO B O   
4994 C CB  . PRO B 292 ? 1.2669 0.9554 1.1072 0.0723  0.0673  0.0982  262 PRO B CB  
4995 C CG  . PRO B 292 ? 1.2845 0.9484 1.1113 0.0784  0.0704  0.0974  262 PRO B CG  
4996 C CD  . PRO B 292 ? 1.2587 0.9148 1.0962 0.0632  0.0739  0.0922  262 PRO B CD  
4997 N N   . PRO B 293 ? 1.2923 0.9554 1.1162 0.0589  0.0756  0.1037  263 PRO B N   
4998 C CA  . PRO B 293 ? 1.3175 0.9582 1.1221 0.0605  0.0807  0.1087  263 PRO B CA  
4999 C C   . PRO B 293 ? 1.3547 0.9734 1.1353 0.0760  0.0821  0.1135  263 PRO B C   
5000 O O   . PRO B 293 ? 1.3552 0.9843 1.1348 0.0886  0.0772  0.1136  263 PRO B O   
5001 C CB  . PRO B 293 ? 1.3122 0.9747 1.1227 0.0611  0.0765  0.1097  263 PRO B CB  
5002 C CG  . PRO B 293 ? 1.2989 0.9914 1.1248 0.0658  0.0684  0.1072  263 PRO B CG  
5003 C CD  . PRO B 293 ? 1.2707 0.9661 1.1097 0.0597  0.0685  0.1027  263 PRO B CD  
5004 N N   . PRO B 294 ? 1.3859 0.9738 1.1462 0.0757  0.0889  0.1179  264 PRO B N   
5005 C CA  . PRO B 294 ? 1.4161 0.9790 1.1506 0.0912  0.0905  0.1228  264 PRO B CA  
5006 C C   . PRO B 294 ? 1.4313 1.0114 1.1592 0.1096  0.0842  0.1258  264 PRO B C   
5007 O O   . PRO B 294 ? 1.4262 1.0230 1.1565 0.1113  0.0816  0.1275  264 PRO B O   
5008 C CB  . PRO B 294 ? 1.4370 0.9693 1.1531 0.0856  0.0988  0.1278  264 PRO B CB  
5009 C CG  . PRO B 294 ? 1.4318 0.9673 1.1649 0.0654  0.1027  0.1239  264 PRO B CG  
5010 C CD  . PRO B 294 ? 1.3880 0.9620 1.1469 0.0615  0.0959  0.1188  264 PRO B CD  
5011 N N   . ASN B 295 ? 1.4448 1.0221 1.1646 0.1236  0.0813  0.1257  265 ASN B N   
5012 C CA  . ASN B 295 ? 1.4555 1.0504 1.1688 0.1426  0.0752  0.1281  265 ASN B CA  
5013 C C   . ASN B 295 ? 1.4785 1.0466 1.1653 0.1605  0.0766  0.1314  265 ASN B C   
5014 O O   . ASN B 295 ? 1.4975 1.0288 1.1680 0.1576  0.0829  0.1326  265 ASN B O   
5015 C CB  . ASN B 295 ? 1.4553 1.0911 1.1940 0.1422  0.0675  0.1235  265 ASN B CB  
5016 C CG  . ASN B 295 ? 1.5027 1.1400 1.2550 0.1350  0.0677  0.1184  265 ASN B CG  
5017 O OD1 . ASN B 295 ? 1.5331 1.1462 1.2720 0.1406  0.0705  0.1182  265 ASN B OD1 
5018 N ND2 . ASN B 295 ? 1.4966 1.1619 1.2749 0.1229  0.0644  0.1141  265 ASN B ND2 
# 
