data_9H8S
# 
_entry.id   9H8S 
# 
_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   9H8S         pdb_00009h8s 10.2210/pdb9h8s/pdb 
WWPDB D_1292142824 ?            ?                   
# 
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                        9H8S 
_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_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          9H8C 
_pdbx_database_related.content_type   unspecified 
# 
_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 'CHLORIDE ION' 35.453    1   ?                   ? ? ? 
4 non-polymer syn 1,2-ETHANEDIOL 62.068    7   ?                   ? ? ? 
5 non-polymer syn GLYCEROL 92.094    1   ?                   ? ? ? 
6 non-polymer syn 
;4-[(3~{S},5~{R})-3-[2-[(3~{R})-3-fluoranylpyrrolidin-1-yl]pyrimidin-4-yl]-5-methoxy-piperidin-1-yl]carbonyl-1~{H}-pyrrole-2-carbonitrile
;
398.434   1   ?                   ? ? ? 
7 non-polymer syn 'DIMETHYL SULFOXIDE' 78.133    2   ?                   ? ? ? 
8 water       nat water 18.015    468 ?                   ? ? ? 
# 
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 'CHLORIDE ION' CL    
4 1,2-ETHANEDIOL EDO   
5 GLYCEROL GOL   
6 
;4-[(3~{S},5~{R})-3-[2-[(3~{R})-3-fluoranylpyrrolidin-1-yl]pyrimidin-4-yl]-5-methoxy-piperidin-1-yl]carbonyl-1~{H}-pyrrole-2-carbonitrile
;
A1ITF 
7 'DIMETHYL SULFOXIDE' DMS   
8 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 
A1ITF non-polymer         . 
;4-[(3~{S},5~{R})-3-[2-[(3~{R})-3-fluoranylpyrrolidin-1-yl]pyrimidin-4-yl]-5-methoxy-piperidin-1-yl]carbonyl-1~{H}-pyrrole-2-carbonitrile
;
?                               'C20 H23 F N6 O2' 398.434 
ALA   'L-peptide linking' y ALANINE ?                               'C3 H7 N O2'      89.093  
ARG   'L-peptide linking' y ARGININE ?                               'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE ?                               'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ?                               'C4 H7 N O4'      133.103 
CL    non-polymer         . 'CHLORIDE ION' ?                               'Cl -1'           35.453  
CYS   'L-peptide linking' y CYSTEINE ?                               'C3 H7 N O2 S'    121.158 
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 ?   ?   ?   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 ?   ?   ?   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 373 362 362 GLU GLU 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 ?   ?   ?   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        A1ITF 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ITF 
_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 CL    1   501 1   CL    CL  A . 
D 4 EDO   1   502 1   EDO   EDO A . 
E 4 EDO   1   503 2   EDO   EDO A . 
F 4 EDO   1   504 3   EDO   EDO A . 
G 4 EDO   1   505 4   EDO   EDO A . 
H 4 EDO   1   506 5   EDO   EDO A . 
I 4 EDO   1   507 6   EDO   EDO A . 
J 5 GOL   1   508 1   GOL   GOL A . 
K 6 A1ITF 1   509 1   A1ITF LIG A . 
L 7 DMS   1   301 1   DMS   DMS B . 
M 7 DMS   1   302 2   DMS   DMS B . 
N 4 EDO   1   303 7   EDO   EDO B . 
O 8 HOH   1   601 116 HOH   HOH A . 
O 8 HOH   2   602 173 HOH   HOH A . 
O 8 HOH   3   603 237 HOH   HOH A . 
O 8 HOH   4   604 305 HOH   HOH A . 
O 8 HOH   5   605 430 HOH   HOH A . 
O 8 HOH   6   606 230 HOH   HOH A . 
O 8 HOH   7   607 373 HOH   HOH A . 
O 8 HOH   8   608 22  HOH   HOH A . 
O 8 HOH   9   609 43  HOH   HOH A . 
O 8 HOH   10  610 68  HOH   HOH A . 
O 8 HOH   11  611 59  HOH   HOH A . 
O 8 HOH   12  612 455 HOH   HOH A . 
O 8 HOH   13  613 21  HOH   HOH A . 
O 8 HOH   14  614 356 HOH   HOH A . 
O 8 HOH   15  615 188 HOH   HOH A . 
O 8 HOH   16  616 172 HOH   HOH A . 
O 8 HOH   17  617 91  HOH   HOH A . 
O 8 HOH   18  618 97  HOH   HOH A . 
O 8 HOH   19  619 429 HOH   HOH A . 
O 8 HOH   20  620 67  HOH   HOH A . 
O 8 HOH   21  621 143 HOH   HOH A . 
O 8 HOH   22  622 303 HOH   HOH A . 
O 8 HOH   23  623 19  HOH   HOH A . 
O 8 HOH   24  624 364 HOH   HOH A . 
O 8 HOH   25  625 144 HOH   HOH A . 
O 8 HOH   26  626 93  HOH   HOH A . 
O 8 HOH   27  627 7   HOH   HOH A . 
O 8 HOH   28  628 194 HOH   HOH A . 
O 8 HOH   29  629 377 HOH   HOH A . 
O 8 HOH   30  630 105 HOH   HOH A . 
O 8 HOH   31  631 52  HOH   HOH A . 
O 8 HOH   32  632 18  HOH   HOH A . 
O 8 HOH   33  633 137 HOH   HOH A . 
O 8 HOH   34  634 311 HOH   HOH A . 
O 8 HOH   35  635 106 HOH   HOH A . 
O 8 HOH   36  636 368 HOH   HOH A . 
O 8 HOH   37  637 131 HOH   HOH A . 
O 8 HOH   38  638 57  HOH   HOH A . 
O 8 HOH   39  639 85  HOH   HOH A . 
O 8 HOH   40  640 2   HOH   HOH A . 
O 8 HOH   41  641 1   HOH   HOH A . 
O 8 HOH   42  642 159 HOH   HOH A . 
O 8 HOH   43  643 8   HOH   HOH A . 
O 8 HOH   44  644 357 HOH   HOH A . 
O 8 HOH   45  645 164 HOH   HOH A . 
O 8 HOH   46  646 219 HOH   HOH A . 
O 8 HOH   47  647 65  HOH   HOH A . 
O 8 HOH   48  648 5   HOH   HOH A . 
O 8 HOH   49  649 101 HOH   HOH A . 
O 8 HOH   50  650 169 HOH   HOH A . 
O 8 HOH   51  651 61  HOH   HOH A . 
O 8 HOH   52  652 29  HOH   HOH A . 
O 8 HOH   53  653 229 HOH   HOH A . 
O 8 HOH   54  654 109 HOH   HOH A . 
O 8 HOH   55  655 92  HOH   HOH A . 
O 8 HOH   56  656 242 HOH   HOH A . 
O 8 HOH   57  657 321 HOH   HOH A . 
O 8 HOH   58  658 77  HOH   HOH A . 
O 8 HOH   59  659 293 HOH   HOH A . 
O 8 HOH   60  660 220 HOH   HOH A . 
O 8 HOH   61  661 204 HOH   HOH A . 
O 8 HOH   62  662 289 HOH   HOH A . 
O 8 HOH   63  663 75  HOH   HOH A . 
O 8 HOH   64  664 329 HOH   HOH A . 
O 8 HOH   65  665 410 HOH   HOH A . 
O 8 HOH   66  666 341 HOH   HOH A . 
O 8 HOH   67  667 353 HOH   HOH A . 
O 8 HOH   68  668 17  HOH   HOH A . 
O 8 HOH   69  669 330 HOH   HOH A . 
O 8 HOH   70  670 58  HOH   HOH A . 
O 8 HOH   71  671 42  HOH   HOH A . 
O 8 HOH   72  672 369 HOH   HOH A . 
O 8 HOH   73  673 13  HOH   HOH A . 
O 8 HOH   74  674 60  HOH   HOH A . 
O 8 HOH   75  675 211 HOH   HOH A . 
O 8 HOH   76  676 140 HOH   HOH A . 
O 8 HOH   77  677 176 HOH   HOH A . 
O 8 HOH   78  678 31  HOH   HOH A . 
O 8 HOH   79  679 296 HOH   HOH A . 
O 8 HOH   80  680 327 HOH   HOH A . 
O 8 HOH   81  681 334 HOH   HOH A . 
O 8 HOH   82  682 287 HOH   HOH A . 
O 8 HOH   83  683 99  HOH   HOH A . 
O 8 HOH   84  684 66  HOH   HOH A . 
O 8 HOH   85  685 78  HOH   HOH A . 
O 8 HOH   86  686 352 HOH   HOH A . 
O 8 HOH   87  687 104 HOH   HOH A . 
O 8 HOH   88  688 16  HOH   HOH A . 
O 8 HOH   89  689 351 HOH   HOH A . 
O 8 HOH   90  690 309 HOH   HOH A . 
O 8 HOH   91  691 177 HOH   HOH A . 
O 8 HOH   92  692 283 HOH   HOH A . 
O 8 HOH   93  693 158 HOH   HOH A . 
O 8 HOH   94  694 127 HOH   HOH A . 
O 8 HOH   95  695 129 HOH   HOH A . 
O 8 HOH   96  696 119 HOH   HOH A . 
O 8 HOH   97  697 14  HOH   HOH A . 
O 8 HOH   98  698 358 HOH   HOH A . 
O 8 HOH   99  699 265 HOH   HOH A . 
O 8 HOH   100 700 349 HOH   HOH A . 
O 8 HOH   101 701 301 HOH   HOH A . 
O 8 HOH   102 702 312 HOH   HOH A . 
O 8 HOH   103 703 367 HOH   HOH A . 
O 8 HOH   104 704 134 HOH   HOH A . 
O 8 HOH   105 705 62  HOH   HOH A . 
O 8 HOH   106 706 453 HOH   HOH A . 
O 8 HOH   107 707 36  HOH   HOH A . 
O 8 HOH   108 708 380 HOH   HOH A . 
O 8 HOH   109 709 47  HOH   HOH A . 
O 8 HOH   110 710 463 HOH   HOH A . 
O 8 HOH   111 711 107 HOH   HOH A . 
O 8 HOH   112 712 70  HOH   HOH A . 
O 8 HOH   113 713 114 HOH   HOH A . 
O 8 HOH   114 714 365 HOH   HOH A . 
O 8 HOH   115 715 74  HOH   HOH A . 
O 8 HOH   116 716 111 HOH   HOH A . 
O 8 HOH   117 717 56  HOH   HOH A . 
O 8 HOH   118 718 82  HOH   HOH A . 
O 8 HOH   119 719 165 HOH   HOH A . 
O 8 HOH   120 720 288 HOH   HOH A . 
O 8 HOH   121 721 339 HOH   HOH A . 
O 8 HOH   122 722 198 HOH   HOH A . 
O 8 HOH   123 723 185 HOH   HOH A . 
O 8 HOH   124 724 24  HOH   HOH A . 
O 8 HOH   125 725 382 HOH   HOH A . 
O 8 HOH   126 726 196 HOH   HOH A . 
O 8 HOH   127 727 379 HOH   HOH A . 
O 8 HOH   128 728 263 HOH   HOH A . 
O 8 HOH   129 729 268 HOH   HOH A . 
O 8 HOH   130 730 234 HOH   HOH A . 
O 8 HOH   131 731 218 HOH   HOH A . 
O 8 HOH   132 732 290 HOH   HOH A . 
O 8 HOH   133 733 79  HOH   HOH A . 
O 8 HOH   134 734 340 HOH   HOH A . 
O 8 HOH   135 735 49  HOH   HOH A . 
O 8 HOH   136 736 235 HOH   HOH A . 
O 8 HOH   137 737 153 HOH   HOH A . 
O 8 HOH   138 738 39  HOH   HOH A . 
O 8 HOH   139 739 150 HOH   HOH A . 
O 8 HOH   140 740 344 HOH   HOH A . 
O 8 HOH   141 741 155 HOH   HOH A . 
O 8 HOH   142 742 110 HOH   HOH A . 
O 8 HOH   143 743 86  HOH   HOH A . 
O 8 HOH   144 744 413 HOH   HOH A . 
O 8 HOH   145 745 123 HOH   HOH A . 
O 8 HOH   146 746 457 HOH   HOH A . 
O 8 HOH   147 747 335 HOH   HOH A . 
O 8 HOH   148 748 314 HOH   HOH A . 
O 8 HOH   149 749 318 HOH   HOH A . 
O 8 HOH   150 750 316 HOH   HOH A . 
O 8 HOH   151 751 381 HOH   HOH A . 
O 8 HOH   152 752 195 HOH   HOH A . 
O 8 HOH   153 753 27  HOH   HOH A . 
O 8 HOH   154 754 279 HOH   HOH A . 
O 8 HOH   155 755 262 HOH   HOH A . 
O 8 HOH   156 756 96  HOH   HOH A . 
O 8 HOH   157 757 187 HOH   HOH A . 
O 8 HOH   158 758 286 HOH   HOH A . 
O 8 HOH   159 759 161 HOH   HOH A . 
O 8 HOH   160 760 209 HOH   HOH A . 
O 8 HOH   161 761 118 HOH   HOH A . 
O 8 HOH   162 762 11  HOH   HOH A . 
O 8 HOH   163 763 416 HOH   HOH A . 
O 8 HOH   164 764 170 HOH   HOH A . 
O 8 HOH   165 765 253 HOH   HOH A . 
O 8 HOH   166 766 348 HOH   HOH A . 
O 8 HOH   167 767 465 HOH   HOH A . 
O 8 HOH   168 768 46  HOH   HOH A . 
O 8 HOH   169 769 337 HOH   HOH A . 
O 8 HOH   170 770 133 HOH   HOH A . 
O 8 HOH   171 771 378 HOH   HOH A . 
O 8 HOH   172 772 370 HOH   HOH A . 
O 8 HOH   173 773 310 HOH   HOH A . 
O 8 HOH   174 774 285 HOH   HOH A . 
O 8 HOH   175 775 213 HOH   HOH A . 
O 8 HOH   176 776 71  HOH   HOH A . 
O 8 HOH   177 777 225 HOH   HOH A . 
O 8 HOH   178 778 73  HOH   HOH A . 
O 8 HOH   179 779 264 HOH   HOH A . 
O 8 HOH   180 780 298 HOH   HOH A . 
O 8 HOH   181 781 366 HOH   HOH A . 
O 8 HOH   182 782 458 HOH   HOH A . 
O 8 HOH   183 783 81  HOH   HOH A . 
O 8 HOH   184 784 141 HOH   HOH A . 
O 8 HOH   185 785 261 HOH   HOH A . 
O 8 HOH   186 786 384 HOH   HOH A . 
O 8 HOH   187 787 94  HOH   HOH A . 
O 8 HOH   188 788 135 HOH   HOH A . 
O 8 HOH   189 789 30  HOH   HOH A . 
O 8 HOH   190 790 186 HOH   HOH A . 
O 8 HOH   191 791 89  HOH   HOH A . 
O 8 HOH   192 792 274 HOH   HOH A . 
O 8 HOH   193 793 433 HOH   HOH A . 
O 8 HOH   194 794 108 HOH   HOH A . 
O 8 HOH   195 795 226 HOH   HOH A . 
O 8 HOH   196 796 390 HOH   HOH A . 
O 8 HOH   197 797 454 HOH   HOH A . 
O 8 HOH   198 798 431 HOH   HOH A . 
O 8 HOH   199 799 362 HOH   HOH A . 
O 8 HOH   200 800 156 HOH   HOH A . 
O 8 HOH   201 801 284 HOH   HOH A . 
O 8 HOH   202 802 295 HOH   HOH A . 
O 8 HOH   203 803 157 HOH   HOH A . 
O 8 HOH   204 804 175 HOH   HOH A . 
O 8 HOH   205 805 372 HOH   HOH A . 
O 8 HOH   206 806 374 HOH   HOH A . 
O 8 HOH   207 807 217 HOH   HOH A . 
O 8 HOH   208 808 249 HOH   HOH A . 
O 8 HOH   209 809 214 HOH   HOH A . 
O 8 HOH   210 810 180 HOH   HOH A . 
O 8 HOH   211 811 371 HOH   HOH A . 
O 8 HOH   212 812 130 HOH   HOH A . 
O 8 HOH   213 813 375 HOH   HOH A . 
O 8 HOH   214 814 426 HOH   HOH A . 
O 8 HOH   215 815 138 HOH   HOH A . 
O 8 HOH   216 816 308 HOH   HOH A . 
O 8 HOH   217 817 428 HOH   HOH A . 
O 8 HOH   218 818 241 HOH   HOH A . 
O 8 HOH   219 819 425 HOH   HOH A . 
O 8 HOH   220 820 427 HOH   HOH A . 
O 8 HOH   221 821 315 HOH   HOH A . 
O 8 HOH   222 822 333 HOH   HOH A . 
O 8 HOH   223 823 415 HOH   HOH A . 
O 8 HOH   224 824 320 HOH   HOH A . 
O 8 HOH   225 825 168 HOH   HOH A . 
O 8 HOH   226 826 432 HOH   HOH A . 
O 8 HOH   227 827 260 HOH   HOH A . 
O 8 HOH   228 828 418 HOH   HOH A . 
O 8 HOH   229 829 459 HOH   HOH A . 
O 8 HOH   230 830 208 HOH   HOH A . 
O 8 HOH   231 831 376 HOH   HOH A . 
O 8 HOH   232 832 414 HOH   HOH A . 
O 8 HOH   233 833 306 HOH   HOH A . 
O 8 HOH   234 834 451 HOH   HOH A . 
O 8 HOH   235 835 355 HOH   HOH A . 
O 8 HOH   236 836 246 HOH   HOH A . 
O 8 HOH   237 837 383 HOH   HOH A . 
O 8 HOH   238 838 192 HOH   HOH A . 
O 8 HOH   239 839 419 HOH   HOH A . 
O 8 HOH   240 840 460 HOH   HOH A . 
O 8 HOH   241 841 197 HOH   HOH A . 
O 8 HOH   242 842 338 HOH   HOH A . 
O 8 HOH   243 843 420 HOH   HOH A . 
O 8 HOH   244 844 354 HOH   HOH A . 
O 8 HOH   245 845 385 HOH   HOH A . 
O 8 HOH   246 846 191 HOH   HOH A . 
O 8 HOH   247 847 205 HOH   HOH A . 
O 8 HOH   248 848 221 HOH   HOH A . 
O 8 HOH   249 849 332 HOH   HOH A . 
O 8 HOH   250 850 277 HOH   HOH A . 
O 8 HOH   251 851 386 HOH   HOH A . 
O 8 HOH   252 852 387 HOH   HOH A . 
O 8 HOH   253 853 324 HOH   HOH A . 
O 8 HOH   254 854 417 HOH   HOH A . 
O 8 HOH   255 855 276 HOH   HOH A . 
O 8 HOH   256 856 300 HOH   HOH A . 
O 8 HOH   257 857 421 HOH   HOH A . 
O 8 HOH   258 858 468 HOH   HOH A . 
P 8 HOH   1   401 98  HOH   HOH B . 
P 8 HOH   2   402 88  HOH   HOH B . 
P 8 HOH   3   403 304 HOH   HOH B . 
P 8 HOH   4   404 20  HOH   HOH B . 
P 8 HOH   5   405 407 HOH   HOH B . 
P 8 HOH   6   406 325 HOH   HOH B . 
P 8 HOH   7   407 40  HOH   HOH B . 
P 8 HOH   8   408 115 HOH   HOH B . 
P 8 HOH   9   409 441 HOH   HOH B . 
P 8 HOH   10  410 280 HOH   HOH B . 
P 8 HOH   11  411 51  HOH   HOH B . 
P 8 HOH   12  412 231 HOH   HOH B . 
P 8 HOH   13  413 136 HOH   HOH B . 
P 8 HOH   14  414 291 HOH   HOH B . 
P 8 HOH   15  415 69  HOH   HOH B . 
P 8 HOH   16  416 10  HOH   HOH B . 
P 8 HOH   17  417 34  HOH   HOH B . 
P 8 HOH   18  418 28  HOH   HOH B . 
P 8 HOH   19  419 350 HOH   HOH B . 
P 8 HOH   20  420 282 HOH   HOH B . 
P 8 HOH   21  421 113 HOH   HOH B . 
P 8 HOH   22  422 206 HOH   HOH B . 
P 8 HOH   23  423 44  HOH   HOH B . 
P 8 HOH   24  424 272 HOH   HOH B . 
P 8 HOH   25  425 50  HOH   HOH B . 
P 8 HOH   26  426 148 HOH   HOH B . 
P 8 HOH   27  427 278 HOH   HOH B . 
P 8 HOH   28  428 45  HOH   HOH B . 
P 8 HOH   29  429 6   HOH   HOH B . 
P 8 HOH   30  430 174 HOH   HOH B . 
P 8 HOH   31  431 25  HOH   HOH B . 
P 8 HOH   32  432 15  HOH   HOH B . 
P 8 HOH   33  433 64  HOH   HOH B . 
P 8 HOH   34  434 464 HOH   HOH B . 
P 8 HOH   35  435 227 HOH   HOH B . 
P 8 HOH   36  436 23  HOH   HOH B . 
P 8 HOH   37  437 245 HOH   HOH B . 
P 8 HOH   38  438 55  HOH   HOH B . 
P 8 HOH   39  439 132 HOH   HOH B . 
P 8 HOH   40  440 4   HOH   HOH B . 
P 8 HOH   41  441 125 HOH   HOH B . 
P 8 HOH   42  442 322 HOH   HOH B . 
P 8 HOH   43  443 181 HOH   HOH B . 
P 8 HOH   44  444 297 HOH   HOH B . 
P 8 HOH   45  445 33  HOH   HOH B . 
P 8 HOH   46  446 26  HOH   HOH B . 
P 8 HOH   47  447 254 HOH   HOH B . 
P 8 HOH   48  448 102 HOH   HOH B . 
P 8 HOH   49  449 121 HOH   HOH B . 
P 8 HOH   50  450 273 HOH   HOH B . 
P 8 HOH   51  451 100 HOH   HOH B . 
P 8 HOH   52  452 35  HOH   HOH B . 
P 8 HOH   53  453 400 HOH   HOH B . 
P 8 HOH   54  454 437 HOH   HOH B . 
P 8 HOH   55  455 236 HOH   HOH B . 
P 8 HOH   56  456 343 HOH   HOH B . 
P 8 HOH   57  457 41  HOH   HOH B . 
P 8 HOH   58  458 210 HOH   HOH B . 
P 8 HOH   59  459 405 HOH   HOH B . 
P 8 HOH   60  460 393 HOH   HOH B . 
P 8 HOH   61  461 462 HOH   HOH B . 
P 8 HOH   62  462 395 HOH   HOH B . 
P 8 HOH   63  463 149 HOH   HOH B . 
P 8 HOH   64  464 359 HOH   HOH B . 
P 8 HOH   65  465 3   HOH   HOH B . 
P 8 HOH   66  466 83  HOH   HOH B . 
P 8 HOH   67  467 467 HOH   HOH B . 
P 8 HOH   68  468 233 HOH   HOH B . 
P 8 HOH   69  469 160 HOH   HOH B . 
P 8 HOH   70  470 269 HOH   HOH B . 
P 8 HOH   71  471 228 HOH   HOH B . 
P 8 HOH   72  472 142 HOH   HOH B . 
P 8 HOH   73  473 257 HOH   HOH B . 
P 8 HOH   74  474 112 HOH   HOH B . 
P 8 HOH   75  475 399 HOH   HOH B . 
P 8 HOH   76  476 281 HOH   HOH B . 
P 8 HOH   77  477 48  HOH   HOH B . 
P 8 HOH   78  478 184 HOH   HOH B . 
P 8 HOH   79  479 319 HOH   HOH B . 
P 8 HOH   80  480 117 HOH   HOH B . 
P 8 HOH   81  481 342 HOH   HOH B . 
P 8 HOH   82  482 53  HOH   HOH B . 
P 8 HOH   83  483 32  HOH   HOH B . 
P 8 HOH   84  484 224 HOH   HOH B . 
P 8 HOH   85  485 171 HOH   HOH B . 
P 8 HOH   86  486 435 HOH   HOH B . 
P 8 HOH   87  487 271 HOH   HOH B . 
P 8 HOH   88  488 336 HOH   HOH B . 
P 8 HOH   89  489 162 HOH   HOH B . 
P 8 HOH   90  490 267 HOH   HOH B . 
P 8 HOH   91  491 152 HOH   HOH B . 
P 8 HOH   92  492 328 HOH   HOH B . 
P 8 HOH   93  493 232 HOH   HOH B . 
P 8 HOH   94  494 248 HOH   HOH B . 
P 8 HOH   95  495 203 HOH   HOH B . 
P 8 HOH   96  496 256 HOH   HOH B . 
P 8 HOH   97  497 12  HOH   HOH B . 
P 8 HOH   98  498 179 HOH   HOH B . 
P 8 HOH   99  499 215 HOH   HOH B . 
P 8 HOH   100 500 9   HOH   HOH B . 
P 8 HOH   101 501 202 HOH   HOH B . 
P 8 HOH   102 502 394 HOH   HOH B . 
P 8 HOH   103 503 151 HOH   HOH B . 
P 8 HOH   104 504 72  HOH   HOH B . 
P 8 HOH   105 505 275 HOH   HOH B . 
P 8 HOH   106 506 360 HOH   HOH B . 
P 8 HOH   107 507 90  HOH   HOH B . 
P 8 HOH   108 508 120 HOH   HOH B . 
P 8 HOH   109 509 450 HOH   HOH B . 
P 8 HOH   110 510 183 HOH   HOH B . 
P 8 HOH   111 511 189 HOH   HOH B . 
P 8 HOH   112 512 323 HOH   HOH B . 
P 8 HOH   113 513 216 HOH   HOH B . 
P 8 HOH   114 514 424 HOH   HOH B . 
P 8 HOH   115 515 84  HOH   HOH B . 
P 8 HOH   116 516 76  HOH   HOH B . 
P 8 HOH   117 517 466 HOH   HOH B . 
P 8 HOH   118 518 128 HOH   HOH B . 
P 8 HOH   119 519 87  HOH   HOH B . 
P 8 HOH   120 520 147 HOH   HOH B . 
P 8 HOH   121 521 307 HOH   HOH B . 
P 8 HOH   122 522 243 HOH   HOH B . 
P 8 HOH   123 523 397 HOH   HOH B . 
P 8 HOH   124 524 238 HOH   HOH B . 
P 8 HOH   125 525 244 HOH   HOH B . 
P 8 HOH   126 526 404 HOH   HOH B . 
P 8 HOH   127 527 223 HOH   HOH B . 
P 8 HOH   128 528 201 HOH   HOH B . 
P 8 HOH   129 529 95  HOH   HOH B . 
P 8 HOH   130 530 80  HOH   HOH B . 
P 8 HOH   131 531 302 HOH   HOH B . 
P 8 HOH   132 532 200 HOH   HOH B . 
P 8 HOH   133 533 124 HOH   HOH B . 
P 8 HOH   134 534 103 HOH   HOH B . 
P 8 HOH   135 535 37  HOH   HOH B . 
P 8 HOH   136 536 448 HOH   HOH B . 
P 8 HOH   137 537 126 HOH   HOH B . 
P 8 HOH   138 538 412 HOH   HOH B . 
P 8 HOH   139 539 63  HOH   HOH B . 
P 8 HOH   140 540 247 HOH   HOH B . 
P 8 HOH   141 541 401 HOH   HOH B . 
P 8 HOH   142 542 266 HOH   HOH B . 
P 8 HOH   143 543 193 HOH   HOH B . 
P 8 HOH   144 544 239 HOH   HOH B . 
P 8 HOH   145 545 442 HOH   HOH B . 
P 8 HOH   146 546 446 HOH   HOH B . 
P 8 HOH   147 547 139 HOH   HOH B . 
P 8 HOH   148 548 38  HOH   HOH B . 
P 8 HOH   149 549 167 HOH   HOH B . 
P 8 HOH   150 550 326 HOH   HOH B . 
P 8 HOH   151 551 294 HOH   HOH B . 
P 8 HOH   152 552 146 HOH   HOH B . 
P 8 HOH   153 553 388 HOH   HOH B . 
P 8 HOH   154 554 259 HOH   HOH B . 
P 8 HOH   155 555 331 HOH   HOH B . 
P 8 HOH   156 556 363 HOH   HOH B . 
P 8 HOH   157 557 411 HOH   HOH B . 
P 8 HOH   158 558 449 HOH   HOH B . 
P 8 HOH   159 559 252 HOH   HOH B . 
P 8 HOH   160 560 408 HOH   HOH B . 
P 8 HOH   161 561 447 HOH   HOH B . 
P 8 HOH   162 562 391 HOH   HOH B . 
P 8 HOH   163 563 456 HOH   HOH B . 
P 8 HOH   164 564 54  HOH   HOH B . 
P 8 HOH   165 565 345 HOH   HOH B . 
P 8 HOH   166 566 409 HOH   HOH B . 
P 8 HOH   167 567 250 HOH   HOH B . 
P 8 HOH   168 568 212 HOH   HOH B . 
P 8 HOH   169 569 396 HOH   HOH B . 
P 8 HOH   170 570 163 HOH   HOH B . 
P 8 HOH   171 571 222 HOH   HOH B . 
P 8 HOH   172 572 443 HOH   HOH B . 
P 8 HOH   173 573 438 HOH   HOH B . 
P 8 HOH   174 574 154 HOH   HOH B . 
P 8 HOH   175 575 251 HOH   HOH B . 
P 8 HOH   176 576 178 HOH   HOH B . 
P 8 HOH   177 577 199 HOH   HOH B . 
P 8 HOH   178 578 122 HOH   HOH B . 
P 8 HOH   179 579 452 HOH   HOH B . 
P 8 HOH   180 580 190 HOH   HOH B . 
P 8 HOH   181 581 423 HOH   HOH B . 
P 8 HOH   182 582 434 HOH   HOH B . 
P 8 HOH   183 583 422 HOH   HOH B . 
P 8 HOH   184 584 145 HOH   HOH B . 
P 8 HOH   185 585 292 HOH   HOH B . 
P 8 HOH   186 586 258 HOH   HOH B . 
P 8 HOH   187 587 403 HOH   HOH B . 
P 8 HOH   188 588 207 HOH   HOH B . 
P 8 HOH   189 589 444 HOH   HOH B . 
P 8 HOH   190 590 346 HOH   HOH B . 
P 8 HOH   191 591 402 HOH   HOH B . 
P 8 HOH   192 592 406 HOH   HOH B . 
P 8 HOH   193 593 313 HOH   HOH B . 
P 8 HOH   194 594 182 HOH   HOH B . 
P 8 HOH   195 595 461 HOH   HOH B . 
P 8 HOH   196 596 270 HOH   HOH B . 
P 8 HOH   197 597 299 HOH   HOH B . 
P 8 HOH   198 598 361 HOH   HOH B . 
P 8 HOH   199 599 398 HOH   HOH B . 
P 8 HOH   200 600 445 HOH   HOH B . 
P 8 HOH   201 601 240 HOH   HOH B . 
P 8 HOH   202 602 317 HOH   HOH B . 
P 8 HOH   203 603 392 HOH   HOH B . 
P 8 HOH   204 604 439 HOH   HOH B . 
P 8 HOH   205 605 166 HOH   HOH B . 
P 8 HOH   206 606 255 HOH   HOH B . 
P 8 HOH   207 607 440 HOH   HOH B . 
P 8 HOH   208 608 347 HOH   HOH B . 
P 8 HOH   209 609 436 HOH   HOH B . 
P 8 HOH   210 610 389 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 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                      1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS      ? ? ? '(VERSION Jan 10'      2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? '(Version 1.0.5)'      3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? .                      4 
? refinement       ? ? ? ? ? ? ? ? ? ? ? BUSTER   ? ? ? '2.11.8 (26-JUL-2023)' 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                     9H8S 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     71.066 
_cell.length_a_esd                 ? 
_cell.length_b                     69.157 
_cell.length_b_esd                 ? 
_cell.length_c                     166.825 
_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                         9H8S 
_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                   9H8S 
_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             2.43 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.28 
_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   0.9763 
_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        0.9763 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I03 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9H8S 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.157 
_reflns.d_resolution_low                               65.381 
_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                                     38173 
_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                           94.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.0 
_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                                0.171 
_reflns.pdbx_Rpim_I_all                                0.047 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.165 
_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                                    2.157 
_reflns_shell.d_res_low                                     2.271 
_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                             1909 
_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                               14.2 
_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                               2.245 
_reflns_shell.pdbx_Rpim_I_all                               0.593 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.547 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          64.0 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  2.165 
_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]                            1.00450 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.00000 
_refine.aniso_B[2][2]                            1.34840 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            -2.35290 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               40.75 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.941 
_refine.correlation_coeff_Fo_to_Fc_free          0.905 
_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                                 9H8S 
_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                            2.157 
_refine.ls_d_res_low                             65.38 
_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                     38173 
_refine.ls_number_reflns_R_free                  1875 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    84.6 
_refine.ls_percent_reflns_R_free                 4.910 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1970 
_refine.ls_R_factor_R_free                       0.2477 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1944 
_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   0.214 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.220 
_refine.pdbx_overall_SU_R_Blow_DPI               0.285 
_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             0.259 
_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                        9H8S 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.27 
_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                       2.157 
_refine_hist.d_res_low                        65.38 
_refine_hist.number_atoms_solvent             468 
_refine_hist.number_atoms_total               5513 
_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        4973 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         72 
_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' ? 0.008 ? 5179 ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 0.89  ? 6977 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1839 ? 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' ? ?     ? 859  ? t_gen_planes              5.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 5179 ? t_it                      10.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_nbd                     ?     ?            
'X-RAY DIFFRACTION' ? 3.12  ? ?    ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 16.32 ? ?    ? t_other_torsion           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_improper_torsion        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 638  ? t_chiral_improper_torsion 5.00  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? 1    ? 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' ? ?     ? 4851 ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.157 
_refine_ls_shell.d_res_low                        2.23 
_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             723 
_refine_ls_shell.percent_reflns_obs               18.46 
_refine_ls_shell.percent_reflns_R_free            5.37 
_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                  0.2593 
_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                  0.2943 
# 
_struct.entry_id                     9H8S 
_struct.title                        'Human CDK8/Cyclin-C complex with inhibitor 3-7' 
_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        9H8S 
_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 4 ? 
F N N 4 ? 
G N N 4 ? 
H N N 4 ? 
I N N 4 ? 
J N N 5 ? 
K N N 6 ? 
L N N 7 ? 
M N N 7 ? 
N N N 4 ? 
O N N 8 ? 
P N N 8 ? 
# 
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 9H8S A 12 ? 414 ? P49336 1 ? 403 ? 1 403 
2 2 9H8S 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 9H8S GLY A 1  ? UNP P49336 ? ? 'expression tag' -10 1  
1 9H8S PRO A 2  ? UNP P49336 ? ? 'expression tag' -9  2  
1 9H8S MET A 3  ? UNP P49336 ? ? 'expression tag' -8  3  
1 9H8S ASP A 4  ? UNP P49336 ? ? 'expression tag' -7  4  
1 9H8S TYR A 5  ? UNP P49336 ? ? 'expression tag' -6  5  
1 9H8S LYS A 6  ? UNP P49336 ? ? 'expression tag' -5  6  
1 9H8S ASP A 7  ? UNP P49336 ? ? 'expression tag' -4  7  
1 9H8S ASP A 8  ? UNP P49336 ? ? 'expression tag' -3  8  
1 9H8S ASP A 9  ? UNP P49336 ? ? 'expression tag' -2  9  
1 9H8S ASP A 10 ? UNP P49336 ? ? 'expression tag' -1  10 
1 9H8S LYS A 11 ? UNP P49336 ? ? 'expression tag' 0   11 
2 9H8S GLY B 1  ? UNP P24863 ? ? 'expression tag' -29 12 
2 9H8S SER B 2  ? UNP P24863 ? ? 'expression tag' -28 13 
2 9H8S GLY B 3  ? UNP P24863 ? ? 'expression tag' -27 14 
2 9H8S MET B 4  ? UNP P24863 ? ? 'expression tag' -26 15 
2 9H8S LYS B 5  ? UNP P24863 ? ? 'expression tag' -25 16 
2 9H8S GLU B 6  ? UNP P24863 ? ? 'expression tag' -24 17 
2 9H8S THR B 7  ? UNP P24863 ? ? 'expression tag' -23 18 
2 9H8S ALA B 8  ? UNP P24863 ? ? 'expression tag' -22 19 
2 9H8S ALA B 9  ? UNP P24863 ? ? 'expression tag' -21 20 
2 9H8S ALA B 10 ? UNP P24863 ? ? 'expression tag' -20 21 
2 9H8S LYS B 11 ? UNP P24863 ? ? 'expression tag' -19 22 
2 9H8S PHE B 12 ? UNP P24863 ? ? 'expression tag' -18 23 
2 9H8S GLU B 13 ? UNP P24863 ? ? 'expression tag' -17 24 
2 9H8S ARG B 14 ? UNP P24863 ? ? 'expression tag' -16 25 
2 9H8S GLN B 15 ? UNP P24863 ? ? 'expression tag' -15 26 
2 9H8S HIS B 16 ? UNP P24863 ? ? 'expression tag' -14 27 
2 9H8S MET B 17 ? UNP P24863 ? ? 'expression tag' -13 28 
2 9H8S ASP B 18 ? UNP P24863 ? ? 'expression tag' -12 29 
2 9H8S SER B 19 ? UNP P24863 ? ? 'expression tag' -11 30 
2 9H8S PRO B 20 ? UNP P24863 ? ? 'expression tag' -10 31 
2 9H8S ASP B 21 ? UNP P24863 ? ? 'expression tag' -9  32 
2 9H8S LEU B 22 ? UNP P24863 ? ? 'expression tag' -8  33 
2 9H8S GLY B 23 ? UNP P24863 ? ? 'expression tag' -7  34 
2 9H8S THR B 24 ? UNP P24863 ? ? 'expression tag' -6  35 
2 9H8S ASP B 25 ? UNP P24863 ? ? 'expression tag' -5  36 
2 9H8S ASP B 26 ? UNP P24863 ? ? 'expression tag' -4  37 
2 9H8S ASP B 27 ? UNP P24863 ? ? 'expression tag' -3  38 
2 9H8S ASP B 28 ? UNP P24863 ? ? 'expression tag' -2  39 
2 9H8S LYS B 29 ? UNP P24863 ? ? 'expression tag' -1  40 
2 9H8S 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)' 5300  ? 
1 MORE         -5    ? 
1 'SSA (A^2)'  27540 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P 
# 
_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 ALA A 212 ? LEU A 217 ? ALA A 201 LEU A 206 1 ? 6  
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 TRP A 278 ? MET A 284 ? TRP A 267 MET A 273 5 ? 7  
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 ? GLU A 348 ? ASP A 332 GLU A 337 5 ? 6  
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  ? ILE B 45  ? SER B 8   ILE B 15  1 ? 8  
HELX_P HELX_P20 AC2 ASP B 47  ? GLN B 56  ? ASP B 17  GLN B 26  1 ? 10 
HELX_P HELX_P21 AC3 LYS B 57  ? PHE B 61  ? LYS B 27  PHE B 31  5 ? 5  
HELX_P HELX_P22 AC4 SER B 63  ? LEU B 85  ? SER B 33  LEU B 55  1 ? 23 
HELX_P HELX_P23 AC5 ARG B 88  ? TYR B 106 ? ARG B 58  TYR B 76  1 ? 19 
HELX_P HELX_P24 AC6 ASP B 112 ? GLU B 128 ? ASP B 82  GLU B 98  1 ? 17 
HELX_P HELX_P25 AC7 SER B 134 ? PHE B 150 ? SER B 104 PHE B 120 1 ? 17 
HELX_P HELX_P26 AC8 ARG B 161 ? MET B 176 ? ARG B 131 MET B 146 1 ? 16 
HELX_P HELX_P27 AC9 PRO B 185 ? GLY B 197 ? PRO B 155 GLY B 167 1 ? 13 
HELX_P HELX_P28 AD1 GLN B 198 ? TYR B 214 ? GLN B 168 TYR B 184 1 ? 17 
HELX_P HELX_P29 AD2 ARG B 215 ? THR B 216 ? ARG B 185 THR B 186 5 ? 2  
HELX_P HELX_P30 AD3 ASP B 217 ? LEU B 221 ? ASP B 187 LEU B 191 5 ? 5  
HELX_P HELX_P31 AD4 PRO B 223 ? GLN B 239 ? PRO B 193 GLN B 209 1 ? 17 
HELX_P HELX_P32 AD5 ALA B 243 ? GLU B 249 ? ALA B 213 GLU B 219 1 ? 7  
HELX_P HELX_P33 AD6 ASP B 253 ? PHE B 274 ? ASP B 223 PHE B 244 1 ? 22 
HELX_P HELX_P34 AD7 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       3.12 
# 
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 LYS A 94  ? SER A 98  ? LYS A 83  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 VAL A 38  ? N VAL A 27  
AA2 1 2 N GLU A 32  ? N GLU A 21  O LYS A 50  ? O LYS A 39  
AA2 2 3 N TYR A 47  ? N TYR A 36  O LEU A 62  ? O LEU A 51  
AA2 3 4 N ALA A 61  ? N ALA A 50  O PHE A 108 ? O PHE A 97  
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                   9H8S 
_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 TYR A 22  ? ? -142.76 -12.04 
2 1 ARG A 150 ? ? 79.06   -6.52  
3 1 ASP A 151 ? ? -151.07 33.17  
4 1 ASP A 173 ? ? 74.84   82.25  
5 1 LEU A 316 ? ? -93.36  58.40  
# 
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 1.9561  68.8847 56.9994 0.0584  ? 0.0147  ? -0.0277 ? -0.0601 ? 0.0538  ? -0.0375 ? 0.2928 ? 
-0.9721 ? -0.5857 ? 1.9229 ? 0.3868  ? 0.7980 ? 0.1246 ? -0.0377 ? 0.0860  ? -0.1657 ? -0.0709 ? 0.0173  ? -0.1835 ? -0.0927 ? 
-0.0537 ? 
2 'X-RAY DIFFRACTION' ? refined 10.7627 40.1404 55.7265 0.0197  ? -0.0124 ? -0.0144 ? -0.0092 ? -0.0087 ? -0.0865 ? 0.7737 ? 
0.0514  ? 0.0157  ? 1.1482 ? -0.3083 ? 0.2386 ? 0.0354 ? 0.0610  ? -0.0458 ? -0.0879 ? -0.0033 ? 0.0476  ? 0.0123  ? 0.0167  ? 
-0.0321 ? 
3 'X-RAY DIFFRACTION' ? refined -3.5329 68.1058 86.0108 -0.0147 ? -0.0220 ? 0.0247  ? -0.0297 ? 0.0190  ? -0.0192 ? 0.4874 ? 
-0.3089 ? -0.0002 ? 0.1028 ? 0.0616  ? 0.9491 ? 0.0213 ? -0.0439 ? 0.0534  ? -0.0375 ? 0.0673  ? -0.0063 ? -0.0020 ? 0.0277  ? 
-0.0886 ? 
# 
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|-2 - 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 LEU 179 ? A LEU 190 
18  1 Y 1 A PHE 180 ? A PHE 191 
19  1 Y 1 A ASN 181 ? A ASN 192 
20  1 Y 1 A SER 182 ? A SER 193 
21  1 Y 1 A PRO 183 ? A PRO 194 
22  1 Y 1 A LEU 184 ? A LEU 195 
23  1 Y 1 A LYS 185 ? A LYS 196 
24  1 Y 1 A PRO 186 ? A PRO 197 
25  1 Y 1 A LEU 187 ? A LEU 198 
26  1 Y 1 A ALA 188 ? A ALA 199 
27  1 Y 1 A ASP 189 ? A ASP 200 
28  1 Y 1 A LEU 190 ? A LEU 201 
29  1 Y 1 A ASP 191 ? A ASP 202 
30  1 Y 1 A PRO 192 ? A PRO 203 
31  1 Y 1 A VAL 193 ? A VAL 204 
32  1 Y 1 A VAL 194 ? A VAL 205 
33  1 Y 1 A VAL 195 ? A VAL 206 
34  1 Y 1 A GLU 239 ? A GLU 250 
35  1 Y 1 A ASP 240 ? A ASP 251 
36  1 Y 1 A ILE 241 ? A ILE 252 
37  1 Y 1 A LYS 242 ? A LYS 253 
38  1 Y 1 A THR 243 ? A THR 254 
39  1 Y 1 A GLU 363 ? A GLU 374 
40  1 Y 1 A PRO 364 ? A PRO 375 
41  1 Y 1 A ASP 365 ? A ASP 376 
42  1 Y 1 A ASP 366 ? A ASP 377 
43  1 Y 1 A LYS 367 ? A LYS 378 
44  1 Y 1 A GLY 368 ? A GLY 379 
45  1 Y 1 A ASP 369 ? A ASP 380 
46  1 Y 1 A LYS 370 ? A LYS 381 
47  1 Y 1 A LYS 371 ? A LYS 382 
48  1 Y 1 A ASN 372 ? A ASN 383 
49  1 Y 1 A GLN 373 ? A GLN 384 
50  1 Y 1 A GLN 374 ? A GLN 385 
51  1 Y 1 A GLN 375 ? A GLN 386 
52  1 Y 1 A GLN 376 ? A GLN 387 
53  1 Y 1 A GLN 377 ? A GLN 388 
54  1 Y 1 A GLY 378 ? A GLY 389 
55  1 Y 1 A ASN 379 ? A ASN 390 
56  1 Y 1 A ASN 380 ? A ASN 391 
57  1 Y 1 A HIS 381 ? A HIS 392 
58  1 Y 1 A THR 382 ? A THR 393 
59  1 Y 1 A ASN 383 ? A ASN 394 
60  1 Y 1 A GLY 384 ? A GLY 395 
61  1 Y 1 A THR 385 ? A THR 396 
62  1 Y 1 A GLY 386 ? A GLY 397 
63  1 Y 1 A HIS 387 ? A HIS 398 
64  1 Y 1 A PRO 388 ? A PRO 399 
65  1 Y 1 A GLY 389 ? A GLY 400 
66  1 Y 1 A ASN 390 ? A ASN 401 
67  1 Y 1 A GLN 391 ? A GLN 402 
68  1 Y 1 A ASP 392 ? A ASP 403 
69  1 Y 1 A SER 393 ? A SER 404 
70  1 Y 1 A SER 394 ? A SER 405 
71  1 Y 1 A HIS 395 ? A HIS 406 
72  1 Y 1 A THR 396 ? A THR 407 
73  1 Y 1 A GLN 397 ? A GLN 408 
74  1 Y 1 A GLY 398 ? A GLY 409 
75  1 Y 1 A PRO 399 ? A PRO 410 
76  1 Y 1 A PRO 400 ? A PRO 411 
77  1 Y 1 A LEU 401 ? A LEU 412 
78  1 Y 1 A LYS 402 ? A LYS 413 
79  1 Y 1 A LYS 403 ? A LYS 414 
80  1 Y 1 B GLY -29 ? B GLY 1   
81  1 Y 1 B SER -28 ? B SER 2   
82  1 Y 1 B GLY -27 ? B GLY 3   
83  1 Y 1 B MET -26 ? B MET 4   
84  1 Y 1 B LYS -25 ? B LYS 5   
85  1 Y 1 B GLU -24 ? B GLU 6   
86  1 Y 1 B THR -23 ? B THR 7   
87  1 Y 1 B ALA -22 ? B ALA 8   
88  1 Y 1 B ALA -21 ? B ALA 9   
89  1 Y 1 B ALA -20 ? B ALA 10  
90  1 Y 1 B LYS -19 ? B LYS 11  
91  1 Y 1 B PHE -18 ? B PHE 12  
92  1 Y 1 B GLU -17 ? B GLU 13  
93  1 Y 1 B ARG -16 ? B ARG 14  
94  1 Y 1 B GLN -15 ? B GLN 15  
95  1 Y 1 B HIS -14 ? B HIS 16  
96  1 Y 1 B MET -13 ? B MET 17  
97  1 Y 1 B ASP -12 ? B ASP 18  
98  1 Y 1 B SER -11 ? B SER 19  
99  1 Y 1 B PRO -10 ? B PRO 20  
100 1 Y 1 B ASP -9  ? B ASP 21  
101 1 Y 1 B LEU -8  ? B LEU 22  
102 1 Y 1 B GLY -7  ? B GLY 23  
103 1 Y 1 B THR -6  ? B THR 24  
104 1 Y 1 B ASP -5  ? B ASP 25  
105 1 Y 1 B ASP -4  ? B ASP 26  
106 1 Y 1 B ASP -3  ? B ASP 27  
107 1 Y 1 B ASP -2  ? B ASP 28  
108 1 Y 1 B LYS -1  ? B LYS 29  
109 1 Y 1 B ASN 265 ? B ASN 295 
110 1 Y 1 B SER 266 ? B SER 296 
111 1 Y 1 B GLU 267 ? B GLU 297 
112 1 Y 1 B GLY 268 ? B GLY 298 
113 1 Y 1 B GLU 269 ? B GLU 299 
114 1 Y 1 B GLN 270 ? B GLN 300 
115 1 Y 1 B GLY 271 ? B GLY 301 
116 1 Y 1 B PRO 272 ? B PRO 302 
117 1 Y 1 B ASN 273 ? B ASN 303 
118 1 Y 1 B GLY 274 ? B GLY 304 
119 1 Y 1 B SER 275 ? B SER 305 
120 1 Y 1 B GLN 276 ? B GLN 306 
121 1 Y 1 B ASN 277 ? B ASN 307 
122 1 Y 1 B SER 278 ? B SER 308 
123 1 Y 1 B SER 279 ? B SER 309 
124 1 Y 1 B TYR 280 ? B TYR 310 
125 1 Y 1 B SER 281 ? B SER 311 
126 1 Y 1 B GLN 282 ? B GLN 312 
127 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 
A1ITF N1   N  Y N 1   
A1ITF N3   N  Y N 2   
A1ITF C4   C  N N 3   
A1ITF C5   C  N N 4   
A1ITF C6   C  N N 5   
A1ITF C7   C  Y N 6   
A1ITF C8   C  Y N 7   
A1ITF C10  C  Y N 8   
A1ITF C13  C  Y N 9   
A1ITF C15  C  Y N 10  
A1ITF C17  C  N N 11  
A1ITF F    F  N N 12  
A1ITF C18  C  N R 13  
A1ITF C16  C  N N 14  
A1ITF C19  C  N N 15  
A1ITF N5   N  N N 16  
A1ITF C14  C  Y N 17  
A1ITF N4   N  Y N 18  
A1ITF C12  C  Y N 19  
A1ITF C3   C  N S 20  
A1ITF C2   C  N N 21  
A1ITF N    N  N N 22  
A1ITF C1   C  N R 23  
A1ITF O    O  N N 24  
A1ITF C    C  N N 25  
A1ITF O1   O  N N 26  
A1ITF C9   C  Y N 27  
A1ITF C11  C  N N 28  
A1ITF N2   N  N N 29  
A1ITF H1   H  N N 30  
A1ITF H2   H  N N 31  
A1ITF H3   H  N N 32  
A1ITF H4   H  N N 33  
A1ITF H5   H  N N 34  
A1ITF H6   H  N N 35  
A1ITF H7   H  N N 36  
A1ITF H8   H  N N 37  
A1ITF H9   H  N N 38  
A1ITF H10  H  N N 39  
A1ITF H11  H  N N 40  
A1ITF H12  H  N N 41  
A1ITF H13  H  N N 42  
A1ITF H14  H  N N 43  
A1ITF H15  H  N N 44  
A1ITF H16  H  N N 45  
A1ITF H17  H  N N 46  
A1ITF H18  H  N N 47  
A1ITF H19  H  N N 48  
A1ITF H20  H  N N 49  
A1ITF H21  H  N N 50  
A1ITF H22  H  N N 51  
A1ITF H23  H  N N 52  
ALA   N    N  N N 53  
ALA   CA   C  N S 54  
ALA   C    C  N N 55  
ALA   O    O  N N 56  
ALA   CB   C  N N 57  
ALA   OXT  O  N N 58  
ALA   H    H  N N 59  
ALA   H2   H  N N 60  
ALA   HA   H  N N 61  
ALA   HB1  H  N N 62  
ALA   HB2  H  N N 63  
ALA   HB3  H  N N 64  
ALA   HXT  H  N N 65  
ARG   N    N  N N 66  
ARG   CA   C  N S 67  
ARG   C    C  N N 68  
ARG   O    O  N N 69  
ARG   CB   C  N N 70  
ARG   CG   C  N N 71  
ARG   CD   C  N N 72  
ARG   NE   N  N N 73  
ARG   CZ   C  N N 74  
ARG   NH1  N  N N 75  
ARG   NH2  N  N N 76  
ARG   OXT  O  N N 77  
ARG   H    H  N N 78  
ARG   H2   H  N N 79  
ARG   HA   H  N N 80  
ARG   HB2  H  N N 81  
ARG   HB3  H  N N 82  
ARG   HG2  H  N N 83  
ARG   HG3  H  N N 84  
ARG   HD2  H  N N 85  
ARG   HD3  H  N N 86  
ARG   HE   H  N N 87  
ARG   HH11 H  N N 88  
ARG   HH12 H  N N 89  
ARG   HH21 H  N N 90  
ARG   HH22 H  N N 91  
ARG   HXT  H  N N 92  
ASN   N    N  N N 93  
ASN   CA   C  N S 94  
ASN   C    C  N N 95  
ASN   O    O  N N 96  
ASN   CB   C  N N 97  
ASN   CG   C  N N 98  
ASN   OD1  O  N N 99  
ASN   ND2  N  N N 100 
ASN   OXT  O  N N 101 
ASN   H    H  N N 102 
ASN   H2   H  N N 103 
ASN   HA   H  N N 104 
ASN   HB2  H  N N 105 
ASN   HB3  H  N N 106 
ASN   HD21 H  N N 107 
ASN   HD22 H  N N 108 
ASN   HXT  H  N N 109 
ASP   N    N  N N 110 
ASP   CA   C  N S 111 
ASP   C    C  N N 112 
ASP   O    O  N N 113 
ASP   CB   C  N N 114 
ASP   CG   C  N N 115 
ASP   OD1  O  N N 116 
ASP   OD2  O  N N 117 
ASP   OXT  O  N N 118 
ASP   H    H  N N 119 
ASP   H2   H  N N 120 
ASP   HA   H  N N 121 
ASP   HB2  H  N N 122 
ASP   HB3  H  N N 123 
ASP   HD2  H  N N 124 
ASP   HXT  H  N N 125 
CL    CL   CL N N 126 
CYS   N    N  N N 127 
CYS   CA   C  N R 128 
CYS   C    C  N N 129 
CYS   O    O  N N 130 
CYS   CB   C  N N 131 
CYS   SG   S  N N 132 
CYS   OXT  O  N N 133 
CYS   H    H  N N 134 
CYS   H2   H  N N 135 
CYS   HA   H  N N 136 
CYS   HB2  H  N N 137 
CYS   HB3  H  N N 138 
CYS   HG   H  N N 139 
CYS   HXT  H  N N 140 
DMS   S    S  N N 141 
DMS   O    O  N N 142 
DMS   C1   C  N N 143 
DMS   C2   C  N N 144 
DMS   H11  H  N N 145 
DMS   H12  H  N N 146 
DMS   H13  H  N N 147 
DMS   H21  H  N N 148 
DMS   H22  H  N N 149 
DMS   H23  H  N N 150 
EDO   C1   C  N N 151 
EDO   O1   O  N N 152 
EDO   C2   C  N N 153 
EDO   O2   O  N N 154 
EDO   H11  H  N N 155 
EDO   H12  H  N N 156 
EDO   HO1  H  N N 157 
EDO   H21  H  N N 158 
EDO   H22  H  N N 159 
EDO   HO2  H  N N 160 
GLN   N    N  N N 161 
GLN   CA   C  N S 162 
GLN   C    C  N N 163 
GLN   O    O  N N 164 
GLN   CB   C  N N 165 
GLN   CG   C  N N 166 
GLN   CD   C  N N 167 
GLN   OE1  O  N N 168 
GLN   NE2  N  N N 169 
GLN   OXT  O  N N 170 
GLN   H    H  N N 171 
GLN   H2   H  N N 172 
GLN   HA   H  N N 173 
GLN   HB2  H  N N 174 
GLN   HB3  H  N N 175 
GLN   HG2  H  N N 176 
GLN   HG3  H  N N 177 
GLN   HE21 H  N N 178 
GLN   HE22 H  N N 179 
GLN   HXT  H  N N 180 
GLU   N    N  N N 181 
GLU   CA   C  N S 182 
GLU   C    C  N N 183 
GLU   O    O  N N 184 
GLU   CB   C  N N 185 
GLU   CG   C  N N 186 
GLU   CD   C  N N 187 
GLU   OE1  O  N N 188 
GLU   OE2  O  N N 189 
GLU   OXT  O  N N 190 
GLU   H    H  N N 191 
GLU   H2   H  N N 192 
GLU   HA   H  N N 193 
GLU   HB2  H  N N 194 
GLU   HB3  H  N N 195 
GLU   HG2  H  N N 196 
GLU   HG3  H  N N 197 
GLU   HE2  H  N N 198 
GLU   HXT  H  N N 199 
GLY   N    N  N N 200 
GLY   CA   C  N N 201 
GLY   C    C  N N 202 
GLY   O    O  N N 203 
GLY   OXT  O  N N 204 
GLY   H    H  N N 205 
GLY   H2   H  N N 206 
GLY   HA2  H  N N 207 
GLY   HA3  H  N N 208 
GLY   HXT  H  N N 209 
GOL   C1   C  N N 210 
GOL   O1   O  N N 211 
GOL   C2   C  N N 212 
GOL   O2   O  N N 213 
GOL   C3   C  N N 214 
GOL   O3   O  N N 215 
GOL   H11  H  N N 216 
GOL   H12  H  N N 217 
GOL   HO1  H  N N 218 
GOL   H2   H  N N 219 
GOL   HO2  H  N N 220 
GOL   H31  H  N N 221 
GOL   H32  H  N N 222 
GOL   HO3  H  N N 223 
HIS   N    N  N N 224 
HIS   CA   C  N S 225 
HIS   C    C  N N 226 
HIS   O    O  N N 227 
HIS   CB   C  N N 228 
HIS   CG   C  Y N 229 
HIS   ND1  N  Y N 230 
HIS   CD2  C  Y N 231 
HIS   CE1  C  Y N 232 
HIS   NE2  N  Y N 233 
HIS   OXT  O  N N 234 
HIS   H    H  N N 235 
HIS   H2   H  N N 236 
HIS   HA   H  N N 237 
HIS   HB2  H  N N 238 
HIS   HB3  H  N N 239 
HIS   HD1  H  N N 240 
HIS   HD2  H  N N 241 
HIS   HE1  H  N N 242 
HIS   HE2  H  N N 243 
HIS   HXT  H  N N 244 
HOH   O    O  N N 245 
HOH   H1   H  N N 246 
HOH   H2   H  N N 247 
ILE   N    N  N N 248 
ILE   CA   C  N S 249 
ILE   C    C  N N 250 
ILE   O    O  N N 251 
ILE   CB   C  N S 252 
ILE   CG1  C  N N 253 
ILE   CG2  C  N N 254 
ILE   CD1  C  N N 255 
ILE   OXT  O  N N 256 
ILE   H    H  N N 257 
ILE   H2   H  N N 258 
ILE   HA   H  N N 259 
ILE   HB   H  N N 260 
ILE   HG12 H  N N 261 
ILE   HG13 H  N N 262 
ILE   HG21 H  N N 263 
ILE   HG22 H  N N 264 
ILE   HG23 H  N N 265 
ILE   HD11 H  N N 266 
ILE   HD12 H  N N 267 
ILE   HD13 H  N N 268 
ILE   HXT  H  N N 269 
LEU   N    N  N N 270 
LEU   CA   C  N S 271 
LEU   C    C  N N 272 
LEU   O    O  N N 273 
LEU   CB   C  N N 274 
LEU   CG   C  N N 275 
LEU   CD1  C  N N 276 
LEU   CD2  C  N N 277 
LEU   OXT  O  N N 278 
LEU   H    H  N N 279 
LEU   H2   H  N N 280 
LEU   HA   H  N N 281 
LEU   HB2  H  N N 282 
LEU   HB3  H  N N 283 
LEU   HG   H  N N 284 
LEU   HD11 H  N N 285 
LEU   HD12 H  N N 286 
LEU   HD13 H  N N 287 
LEU   HD21 H  N N 288 
LEU   HD22 H  N N 289 
LEU   HD23 H  N N 290 
LEU   HXT  H  N N 291 
LYS   N    N  N N 292 
LYS   CA   C  N S 293 
LYS   C    C  N N 294 
LYS   O    O  N N 295 
LYS   CB   C  N N 296 
LYS   CG   C  N N 297 
LYS   CD   C  N N 298 
LYS   CE   C  N N 299 
LYS   NZ   N  N N 300 
LYS   OXT  O  N N 301 
LYS   H    H  N N 302 
LYS   H2   H  N N 303 
LYS   HA   H  N N 304 
LYS   HB2  H  N N 305 
LYS   HB3  H  N N 306 
LYS   HG2  H  N N 307 
LYS   HG3  H  N N 308 
LYS   HD2  H  N N 309 
LYS   HD3  H  N N 310 
LYS   HE2  H  N N 311 
LYS   HE3  H  N N 312 
LYS   HZ1  H  N N 313 
LYS   HZ2  H  N N 314 
LYS   HZ3  H  N N 315 
LYS   HXT  H  N N 316 
MET   N    N  N N 317 
MET   CA   C  N S 318 
MET   C    C  N N 319 
MET   O    O  N N 320 
MET   CB   C  N N 321 
MET   CG   C  N N 322 
MET   SD   S  N N 323 
MET   CE   C  N N 324 
MET   OXT  O  N N 325 
MET   H    H  N N 326 
MET   H2   H  N N 327 
MET   HA   H  N N 328 
MET   HB2  H  N N 329 
MET   HB3  H  N N 330 
MET   HG2  H  N N 331 
MET   HG3  H  N N 332 
MET   HE1  H  N N 333 
MET   HE2  H  N N 334 
MET   HE3  H  N N 335 
MET   HXT  H  N N 336 
PHE   N    N  N N 337 
PHE   CA   C  N S 338 
PHE   C    C  N N 339 
PHE   O    O  N N 340 
PHE   CB   C  N N 341 
PHE   CG   C  Y N 342 
PHE   CD1  C  Y N 343 
PHE   CD2  C  Y N 344 
PHE   CE1  C  Y N 345 
PHE   CE2  C  Y N 346 
PHE   CZ   C  Y N 347 
PHE   OXT  O  N N 348 
PHE   H    H  N N 349 
PHE   H2   H  N N 350 
PHE   HA   H  N N 351 
PHE   HB2  H  N N 352 
PHE   HB3  H  N N 353 
PHE   HD1  H  N N 354 
PHE   HD2  H  N N 355 
PHE   HE1  H  N N 356 
PHE   HE2  H  N N 357 
PHE   HZ   H  N N 358 
PHE   HXT  H  N N 359 
PRO   N    N  N N 360 
PRO   CA   C  N S 361 
PRO   C    C  N N 362 
PRO   O    O  N N 363 
PRO   CB   C  N N 364 
PRO   CG   C  N N 365 
PRO   CD   C  N N 366 
PRO   OXT  O  N N 367 
PRO   H    H  N N 368 
PRO   HA   H  N N 369 
PRO   HB2  H  N N 370 
PRO   HB3  H  N N 371 
PRO   HG2  H  N N 372 
PRO   HG3  H  N N 373 
PRO   HD2  H  N N 374 
PRO   HD3  H  N N 375 
PRO   HXT  H  N N 376 
SER   N    N  N N 377 
SER   CA   C  N S 378 
SER   C    C  N N 379 
SER   O    O  N N 380 
SER   CB   C  N N 381 
SER   OG   O  N N 382 
SER   OXT  O  N N 383 
SER   H    H  N N 384 
SER   H2   H  N N 385 
SER   HA   H  N N 386 
SER   HB2  H  N N 387 
SER   HB3  H  N N 388 
SER   HG   H  N N 389 
SER   HXT  H  N N 390 
THR   N    N  N N 391 
THR   CA   C  N S 392 
THR   C    C  N N 393 
THR   O    O  N N 394 
THR   CB   C  N R 395 
THR   OG1  O  N N 396 
THR   CG2  C  N N 397 
THR   OXT  O  N N 398 
THR   H    H  N N 399 
THR   H2   H  N N 400 
THR   HA   H  N N 401 
THR   HB   H  N N 402 
THR   HG1  H  N N 403 
THR   HG21 H  N N 404 
THR   HG22 H  N N 405 
THR   HG23 H  N N 406 
THR   HXT  H  N N 407 
TRP   N    N  N N 408 
TRP   CA   C  N S 409 
TRP   C    C  N N 410 
TRP   O    O  N N 411 
TRP   CB   C  N N 412 
TRP   CG   C  Y N 413 
TRP   CD1  C  Y N 414 
TRP   CD2  C  Y N 415 
TRP   NE1  N  Y N 416 
TRP   CE2  C  Y N 417 
TRP   CE3  C  Y N 418 
TRP   CZ2  C  Y N 419 
TRP   CZ3  C  Y N 420 
TRP   CH2  C  Y N 421 
TRP   OXT  O  N N 422 
TRP   H    H  N N 423 
TRP   H2   H  N N 424 
TRP   HA   H  N N 425 
TRP   HB2  H  N N 426 
TRP   HB3  H  N N 427 
TRP   HD1  H  N N 428 
TRP   HE1  H  N N 429 
TRP   HE3  H  N N 430 
TRP   HZ2  H  N N 431 
TRP   HZ3  H  N N 432 
TRP   HH2  H  N N 433 
TRP   HXT  H  N N 434 
TYR   N    N  N N 435 
TYR   CA   C  N S 436 
TYR   C    C  N N 437 
TYR   O    O  N N 438 
TYR   CB   C  N N 439 
TYR   CG   C  Y N 440 
TYR   CD1  C  Y N 441 
TYR   CD2  C  Y N 442 
TYR   CE1  C  Y N 443 
TYR   CE2  C  Y N 444 
TYR   CZ   C  Y N 445 
TYR   OH   O  N N 446 
TYR   OXT  O  N N 447 
TYR   H    H  N N 448 
TYR   H2   H  N N 449 
TYR   HA   H  N N 450 
TYR   HB2  H  N N 451 
TYR   HB3  H  N N 452 
TYR   HD1  H  N N 453 
TYR   HD2  H  N N 454 
TYR   HE1  H  N N 455 
TYR   HE2  H  N N 456 
TYR   HH   H  N N 457 
TYR   HXT  H  N N 458 
VAL   N    N  N N 459 
VAL   CA   C  N S 460 
VAL   C    C  N N 461 
VAL   O    O  N N 462 
VAL   CB   C  N N 463 
VAL   CG1  C  N N 464 
VAL   CG2  C  N N 465 
VAL   OXT  O  N N 466 
VAL   H    H  N N 467 
VAL   H2   H  N N 468 
VAL   HA   H  N N 469 
VAL   HB   H  N N 470 
VAL   HG11 H  N N 471 
VAL   HG12 H  N N 472 
VAL   HG13 H  N N 473 
VAL   HG21 H  N N 474 
VAL   HG22 H  N N 475 
VAL   HG23 H  N N 476 
VAL   HXT  H  N N 477 
# 
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 
A1ITF C   O    sing N N 1   
A1ITF O   C1   sing N N 2   
A1ITF C1  C2   sing N N 3   
A1ITF C1  C5   sing N N 4   
A1ITF C2  C3   sing N N 5   
A1ITF C5  N    sing N N 6   
A1ITF C13 C14  doub Y N 7   
A1ITF C13 C12  sing Y N 8   
A1ITF C3  C12  sing N N 9   
A1ITF C3  C4   sing N N 10  
A1ITF N   C4   sing N N 11  
A1ITF N   C6   sing N N 12  
A1ITF C14 N3   sing Y N 13  
A1ITF C12 N4   doub Y N 14  
A1ITF O1  C6   doub N N 15  
A1ITF C6  C7   sing N N 16  
A1ITF N3  C15  doub Y N 17  
A1ITF N4  C15  sing Y N 18  
A1ITF C15 N5   sing N N 19  
A1ITF C7  C10  sing Y N 20  
A1ITF C7  C8   doub Y N 21  
A1ITF C10 C9   doub Y N 22  
A1ITF C8  N1   sing Y N 23  
A1ITF N5  C16  sing N N 24  
A1ITF N5  C19  sing N N 25  
A1ITF C9  N1   sing Y N 26  
A1ITF C9  C11  sing N N 27  
A1ITF C16 C17  sing N N 28  
A1ITF C19 C18  sing N N 29  
A1ITF C11 N2   trip N N 30  
A1ITF F   C18  sing N N 31  
A1ITF C18 C17  sing N N 32  
A1ITF N1  H1   sing N N 33  
A1ITF C4  H2   sing N N 34  
A1ITF C4  H3   sing N N 35  
A1ITF C5  H4   sing N N 36  
A1ITF C5  H5   sing N N 37  
A1ITF C8  H6   sing N N 38  
A1ITF C10 H7   sing N N 39  
A1ITF C13 H8   sing N N 40  
A1ITF C17 H9   sing N N 41  
A1ITF C17 H10  sing N N 42  
A1ITF C18 H11  sing N N 43  
A1ITF C16 H12  sing N N 44  
A1ITF C16 H13  sing N N 45  
A1ITF C19 H14  sing N N 46  
A1ITF C19 H15  sing N N 47  
A1ITF C14 H16  sing N N 48  
A1ITF C3  H17  sing N N 49  
A1ITF C2  H18  sing N N 50  
A1ITF C2  H19  sing N N 51  
A1ITF C1  H20  sing N N 52  
A1ITF C   H21  sing N N 53  
A1ITF C   H22  sing N N 54  
A1ITF C   H23  sing N N 55  
ALA   N   CA   sing N N 56  
ALA   N   H    sing N N 57  
ALA   N   H2   sing N N 58  
ALA   CA  C    sing N N 59  
ALA   CA  CB   sing N N 60  
ALA   CA  HA   sing N N 61  
ALA   C   O    doub N N 62  
ALA   C   OXT  sing N N 63  
ALA   CB  HB1  sing N N 64  
ALA   CB  HB2  sing N N 65  
ALA   CB  HB3  sing N N 66  
ALA   OXT HXT  sing N N 67  
ARG   N   CA   sing N N 68  
ARG   N   H    sing N N 69  
ARG   N   H2   sing N N 70  
ARG   CA  C    sing N N 71  
ARG   CA  CB   sing N N 72  
ARG   CA  HA   sing N N 73  
ARG   C   O    doub N N 74  
ARG   C   OXT  sing N N 75  
ARG   CB  CG   sing N N 76  
ARG   CB  HB2  sing N N 77  
ARG   CB  HB3  sing N N 78  
ARG   CG  CD   sing N N 79  
ARG   CG  HG2  sing N N 80  
ARG   CG  HG3  sing N N 81  
ARG   CD  NE   sing N N 82  
ARG   CD  HD2  sing N N 83  
ARG   CD  HD3  sing N N 84  
ARG   NE  CZ   sing N N 85  
ARG   NE  HE   sing N N 86  
ARG   CZ  NH1  sing N N 87  
ARG   CZ  NH2  doub N N 88  
ARG   NH1 HH11 sing N N 89  
ARG   NH1 HH12 sing N N 90  
ARG   NH2 HH21 sing N N 91  
ARG   NH2 HH22 sing N N 92  
ARG   OXT HXT  sing N N 93  
ASN   N   CA   sing N N 94  
ASN   N   H    sing N N 95  
ASN   N   H2   sing N N 96  
ASN   CA  C    sing N N 97  
ASN   CA  CB   sing N N 98  
ASN   CA  HA   sing N N 99  
ASN   C   O    doub N N 100 
ASN   C   OXT  sing N N 101 
ASN   CB  CG   sing N N 102 
ASN   CB  HB2  sing N N 103 
ASN   CB  HB3  sing N N 104 
ASN   CG  OD1  doub N N 105 
ASN   CG  ND2  sing N N 106 
ASN   ND2 HD21 sing N N 107 
ASN   ND2 HD22 sing N N 108 
ASN   OXT HXT  sing N N 109 
ASP   N   CA   sing N N 110 
ASP   N   H    sing N N 111 
ASP   N   H2   sing N N 112 
ASP   CA  C    sing N N 113 
ASP   CA  CB   sing N N 114 
ASP   CA  HA   sing N N 115 
ASP   C   O    doub N N 116 
ASP   C   OXT  sing N N 117 
ASP   CB  CG   sing N N 118 
ASP   CB  HB2  sing N N 119 
ASP   CB  HB3  sing N N 120 
ASP   CG  OD1  doub N N 121 
ASP   CG  OD2  sing N N 122 
ASP   OD2 HD2  sing N N 123 
ASP   OXT HXT  sing N N 124 
CYS   N   CA   sing N N 125 
CYS   N   H    sing N N 126 
CYS   N   H2   sing N N 127 
CYS   CA  C    sing N N 128 
CYS   CA  CB   sing N N 129 
CYS   CA  HA   sing N N 130 
CYS   C   O    doub N N 131 
CYS   C   OXT  sing N N 132 
CYS   CB  SG   sing N N 133 
CYS   CB  HB2  sing N N 134 
CYS   CB  HB3  sing N N 135 
CYS   SG  HG   sing N N 136 
CYS   OXT HXT  sing N N 137 
DMS   S   O    doub N N 138 
DMS   S   C1   sing N N 139 
DMS   S   C2   sing N N 140 
DMS   C1  H11  sing N N 141 
DMS   C1  H12  sing N N 142 
DMS   C1  H13  sing N N 143 
DMS   C2  H21  sing N N 144 
DMS   C2  H22  sing N N 145 
DMS   C2  H23  sing N N 146 
EDO   C1  O1   sing N N 147 
EDO   C1  C2   sing N N 148 
EDO   C1  H11  sing N N 149 
EDO   C1  H12  sing N N 150 
EDO   O1  HO1  sing N N 151 
EDO   C2  O2   sing N N 152 
EDO   C2  H21  sing N N 153 
EDO   C2  H22  sing N N 154 
EDO   O2  HO2  sing N N 155 
GLN   N   CA   sing N N 156 
GLN   N   H    sing N N 157 
GLN   N   H2   sing N N 158 
GLN   CA  C    sing N N 159 
GLN   CA  CB   sing N N 160 
GLN   CA  HA   sing N N 161 
GLN   C   O    doub N N 162 
GLN   C   OXT  sing N N 163 
GLN   CB  CG   sing N N 164 
GLN   CB  HB2  sing N N 165 
GLN   CB  HB3  sing N N 166 
GLN   CG  CD   sing N N 167 
GLN   CG  HG2  sing N N 168 
GLN   CG  HG3  sing N N 169 
GLN   CD  OE1  doub N N 170 
GLN   CD  NE2  sing N N 171 
GLN   NE2 HE21 sing N N 172 
GLN   NE2 HE22 sing N N 173 
GLN   OXT HXT  sing N N 174 
GLU   N   CA   sing N N 175 
GLU   N   H    sing N N 176 
GLU   N   H2   sing N N 177 
GLU   CA  C    sing N N 178 
GLU   CA  CB   sing N N 179 
GLU   CA  HA   sing N N 180 
GLU   C   O    doub N N 181 
GLU   C   OXT  sing N N 182 
GLU   CB  CG   sing N N 183 
GLU   CB  HB2  sing N N 184 
GLU   CB  HB3  sing N N 185 
GLU   CG  CD   sing N N 186 
GLU   CG  HG2  sing N N 187 
GLU   CG  HG3  sing N N 188 
GLU   CD  OE1  doub N N 189 
GLU   CD  OE2  sing N N 190 
GLU   OE2 HE2  sing N N 191 
GLU   OXT HXT  sing N N 192 
GLY   N   CA   sing N N 193 
GLY   N   H    sing N N 194 
GLY   N   H2   sing N N 195 
GLY   CA  C    sing N N 196 
GLY   CA  HA2  sing N N 197 
GLY   CA  HA3  sing N N 198 
GLY   C   O    doub N N 199 
GLY   C   OXT  sing N N 200 
GLY   OXT HXT  sing N N 201 
GOL   C1  O1   sing N N 202 
GOL   C1  C2   sing N N 203 
GOL   C1  H11  sing N N 204 
GOL   C1  H12  sing N N 205 
GOL   O1  HO1  sing N N 206 
GOL   C2  O2   sing N N 207 
GOL   C2  C3   sing N N 208 
GOL   C2  H2   sing N N 209 
GOL   O2  HO2  sing N N 210 
GOL   C3  O3   sing N N 211 
GOL   C3  H31  sing N N 212 
GOL   C3  H32  sing N N 213 
GOL   O3  HO3  sing N N 214 
HIS   N   CA   sing N N 215 
HIS   N   H    sing N N 216 
HIS   N   H2   sing N N 217 
HIS   CA  C    sing N N 218 
HIS   CA  CB   sing N N 219 
HIS   CA  HA   sing N N 220 
HIS   C   O    doub N N 221 
HIS   C   OXT  sing N N 222 
HIS   CB  CG   sing N N 223 
HIS   CB  HB2  sing N N 224 
HIS   CB  HB3  sing N N 225 
HIS   CG  ND1  sing Y N 226 
HIS   CG  CD2  doub Y N 227 
HIS   ND1 CE1  doub Y N 228 
HIS   ND1 HD1  sing N N 229 
HIS   CD2 NE2  sing Y N 230 
HIS   CD2 HD2  sing N N 231 
HIS   CE1 NE2  sing Y N 232 
HIS   CE1 HE1  sing N N 233 
HIS   NE2 HE2  sing N N 234 
HIS   OXT HXT  sing N N 235 
HOH   O   H1   sing N N 236 
HOH   O   H2   sing N N 237 
ILE   N   CA   sing N N 238 
ILE   N   H    sing N N 239 
ILE   N   H2   sing N N 240 
ILE   CA  C    sing N N 241 
ILE   CA  CB   sing N N 242 
ILE   CA  HA   sing N N 243 
ILE   C   O    doub N N 244 
ILE   C   OXT  sing N N 245 
ILE   CB  CG1  sing N N 246 
ILE   CB  CG2  sing N N 247 
ILE   CB  HB   sing N N 248 
ILE   CG1 CD1  sing N N 249 
ILE   CG1 HG12 sing N N 250 
ILE   CG1 HG13 sing N N 251 
ILE   CG2 HG21 sing N N 252 
ILE   CG2 HG22 sing N N 253 
ILE   CG2 HG23 sing N N 254 
ILE   CD1 HD11 sing N N 255 
ILE   CD1 HD12 sing N N 256 
ILE   CD1 HD13 sing N N 257 
ILE   OXT HXT  sing N N 258 
LEU   N   CA   sing N N 259 
LEU   N   H    sing N N 260 
LEU   N   H2   sing N N 261 
LEU   CA  C    sing N N 262 
LEU   CA  CB   sing N N 263 
LEU   CA  HA   sing N N 264 
LEU   C   O    doub N N 265 
LEU   C   OXT  sing N N 266 
LEU   CB  CG   sing N N 267 
LEU   CB  HB2  sing N N 268 
LEU   CB  HB3  sing N N 269 
LEU   CG  CD1  sing N N 270 
LEU   CG  CD2  sing N N 271 
LEU   CG  HG   sing N N 272 
LEU   CD1 HD11 sing N N 273 
LEU   CD1 HD12 sing N N 274 
LEU   CD1 HD13 sing N N 275 
LEU   CD2 HD21 sing N N 276 
LEU   CD2 HD22 sing N N 277 
LEU   CD2 HD23 sing N N 278 
LEU   OXT HXT  sing N N 279 
LYS   N   CA   sing N N 280 
LYS   N   H    sing N N 281 
LYS   N   H2   sing N N 282 
LYS   CA  C    sing N N 283 
LYS   CA  CB   sing N N 284 
LYS   CA  HA   sing N N 285 
LYS   C   O    doub N N 286 
LYS   C   OXT  sing N N 287 
LYS   CB  CG   sing N N 288 
LYS   CB  HB2  sing N N 289 
LYS   CB  HB3  sing N N 290 
LYS   CG  CD   sing N N 291 
LYS   CG  HG2  sing N N 292 
LYS   CG  HG3  sing N N 293 
LYS   CD  CE   sing N N 294 
LYS   CD  HD2  sing N N 295 
LYS   CD  HD3  sing N N 296 
LYS   CE  NZ   sing N N 297 
LYS   CE  HE2  sing N N 298 
LYS   CE  HE3  sing N N 299 
LYS   NZ  HZ1  sing N N 300 
LYS   NZ  HZ2  sing N N 301 
LYS   NZ  HZ3  sing N N 302 
LYS   OXT HXT  sing N N 303 
MET   N   CA   sing N N 304 
MET   N   H    sing N N 305 
MET   N   H2   sing N N 306 
MET   CA  C    sing N N 307 
MET   CA  CB   sing N N 308 
MET   CA  HA   sing N N 309 
MET   C   O    doub N N 310 
MET   C   OXT  sing N N 311 
MET   CB  CG   sing N N 312 
MET   CB  HB2  sing N N 313 
MET   CB  HB3  sing N N 314 
MET   CG  SD   sing N N 315 
MET   CG  HG2  sing N N 316 
MET   CG  HG3  sing N N 317 
MET   SD  CE   sing N N 318 
MET   CE  HE1  sing N N 319 
MET   CE  HE2  sing N N 320 
MET   CE  HE3  sing N N 321 
MET   OXT HXT  sing N N 322 
PHE   N   CA   sing N N 323 
PHE   N   H    sing N N 324 
PHE   N   H2   sing N N 325 
PHE   CA  C    sing N N 326 
PHE   CA  CB   sing N N 327 
PHE   CA  HA   sing N N 328 
PHE   C   O    doub N N 329 
PHE   C   OXT  sing N N 330 
PHE   CB  CG   sing N N 331 
PHE   CB  HB2  sing N N 332 
PHE   CB  HB3  sing N N 333 
PHE   CG  CD1  doub Y N 334 
PHE   CG  CD2  sing Y N 335 
PHE   CD1 CE1  sing Y N 336 
PHE   CD1 HD1  sing N N 337 
PHE   CD2 CE2  doub Y N 338 
PHE   CD2 HD2  sing N N 339 
PHE   CE1 CZ   doub Y N 340 
PHE   CE1 HE1  sing N N 341 
PHE   CE2 CZ   sing Y N 342 
PHE   CE2 HE2  sing N N 343 
PHE   CZ  HZ   sing N N 344 
PHE   OXT HXT  sing N N 345 
PRO   N   CA   sing N N 346 
PRO   N   CD   sing N N 347 
PRO   N   H    sing N N 348 
PRO   CA  C    sing N N 349 
PRO   CA  CB   sing N N 350 
PRO   CA  HA   sing N N 351 
PRO   C   O    doub N N 352 
PRO   C   OXT  sing N N 353 
PRO   CB  CG   sing N N 354 
PRO   CB  HB2  sing N N 355 
PRO   CB  HB3  sing N N 356 
PRO   CG  CD   sing N N 357 
PRO   CG  HG2  sing N N 358 
PRO   CG  HG3  sing N N 359 
PRO   CD  HD2  sing N N 360 
PRO   CD  HD3  sing N N 361 
PRO   OXT HXT  sing N N 362 
SER   N   CA   sing N N 363 
SER   N   H    sing N N 364 
SER   N   H2   sing N N 365 
SER   CA  C    sing N N 366 
SER   CA  CB   sing N N 367 
SER   CA  HA   sing N N 368 
SER   C   O    doub N N 369 
SER   C   OXT  sing N N 370 
SER   CB  OG   sing N N 371 
SER   CB  HB2  sing N N 372 
SER   CB  HB3  sing N N 373 
SER   OG  HG   sing N N 374 
SER   OXT HXT  sing N N 375 
THR   N   CA   sing N N 376 
THR   N   H    sing N N 377 
THR   N   H2   sing N N 378 
THR   CA  C    sing N N 379 
THR   CA  CB   sing N N 380 
THR   CA  HA   sing N N 381 
THR   C   O    doub N N 382 
THR   C   OXT  sing N N 383 
THR   CB  OG1  sing N N 384 
THR   CB  CG2  sing N N 385 
THR   CB  HB   sing N N 386 
THR   OG1 HG1  sing N N 387 
THR   CG2 HG21 sing N N 388 
THR   CG2 HG22 sing N N 389 
THR   CG2 HG23 sing N N 390 
THR   OXT HXT  sing N N 391 
TRP   N   CA   sing N N 392 
TRP   N   H    sing N N 393 
TRP   N   H2   sing N N 394 
TRP   CA  C    sing N N 395 
TRP   CA  CB   sing N N 396 
TRP   CA  HA   sing N N 397 
TRP   C   O    doub N N 398 
TRP   C   OXT  sing N N 399 
TRP   CB  CG   sing N N 400 
TRP   CB  HB2  sing N N 401 
TRP   CB  HB3  sing N N 402 
TRP   CG  CD1  doub Y N 403 
TRP   CG  CD2  sing Y N 404 
TRP   CD1 NE1  sing Y N 405 
TRP   CD1 HD1  sing N N 406 
TRP   CD2 CE2  doub Y N 407 
TRP   CD2 CE3  sing Y N 408 
TRP   NE1 CE2  sing Y N 409 
TRP   NE1 HE1  sing N N 410 
TRP   CE2 CZ2  sing Y N 411 
TRP   CE3 CZ3  doub Y N 412 
TRP   CE3 HE3  sing N N 413 
TRP   CZ2 CH2  doub Y N 414 
TRP   CZ2 HZ2  sing N N 415 
TRP   CZ3 CH2  sing Y N 416 
TRP   CZ3 HZ3  sing N N 417 
TRP   CH2 HH2  sing N N 418 
TRP   OXT HXT  sing N N 419 
TYR   N   CA   sing N N 420 
TYR   N   H    sing N N 421 
TYR   N   H2   sing N N 422 
TYR   CA  C    sing N N 423 
TYR   CA  CB   sing N N 424 
TYR   CA  HA   sing N N 425 
TYR   C   O    doub N N 426 
TYR   C   OXT  sing N N 427 
TYR   CB  CG   sing N N 428 
TYR   CB  HB2  sing N N 429 
TYR   CB  HB3  sing N N 430 
TYR   CG  CD1  doub Y N 431 
TYR   CG  CD2  sing Y N 432 
TYR   CD1 CE1  sing Y N 433 
TYR   CD1 HD1  sing N N 434 
TYR   CD2 CE2  doub Y N 435 
TYR   CD2 HD2  sing N N 436 
TYR   CE1 CZ   doub Y N 437 
TYR   CE1 HE1  sing N N 438 
TYR   CE2 CZ   sing Y N 439 
TYR   CE2 HE2  sing N N 440 
TYR   CZ  OH   sing N N 441 
TYR   OH  HH   sing N N 442 
TYR   OXT HXT  sing N N 443 
VAL   N   CA   sing N N 444 
VAL   N   H    sing N N 445 
VAL   N   H2   sing N N 446 
VAL   CA  C    sing N N 447 
VAL   CA  CB   sing N N 448 
VAL   CA  HA   sing N N 449 
VAL   C   O    doub N N 450 
VAL   C   OXT  sing N N 451 
VAL   CB  CG1  sing N N 452 
VAL   CB  CG2  sing N N 453 
VAL   CB  HB   sing N N 454 
VAL   CG1 HG11 sing N N 455 
VAL   CG1 HG12 sing N N 456 
VAL   CG1 HG13 sing N N 457 
VAL   CG2 HG21 sing N N 458 
VAL   CG2 HG22 sing N N 459 
VAL   CG2 HG23 sing N N 460 
VAL   OXT HXT  sing N N 461 
# 
_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                    9H8S 
_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]   0.014071 
_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]   0.014460 
_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]   0.005994 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
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  ? -15.038 80.708 71.666  1.00 49.46 ? 1   MET   A N   1 
ATOM   2    C  CA  . MET   A 1 12  ? -13.646 81.031 71.394  1.00 49.41 ? 1   MET   A CA  1 
ATOM   3    C  C   . MET   A 1 12  ? -13.483 82.543 71.296  1.00 47.23 ? 1   MET   A C   1 
ATOM   4    O  O   . MET   A 1 12  ? -14.252 83.196 70.602  1.00 48.07 ? 1   MET   A O   1 
ATOM   5    C  CB  . MET   A 1 12  ? -13.171 80.312 70.117  1.00 51.57 ? 1   MET   A CB  1 
ATOM   6    C  CG  . MET   A 1 12  ? -12.020 80.996 69.402  1.00 57.26 ? 1   MET   A CG  1 
ATOM   7    S  SD  . MET   A 1 12  ? -11.104 79.891 68.331  1.00 71.85 ? 1   MET   A SD  1 
ATOM   8    C  CE  . MET   A 1 12  ? -10.252 79.009 69.522  1.00 72.29 ? 1   MET   A CE  1 
ATOM   9    N  N   . ASP   A 1 13  ? -12.464 83.092 71.962  1.00 44.48 ? 2   ASP   A N   1 
ATOM   10   C  CA  . ASP   A 1 13  ? -12.168 84.510 71.931  1.00 42.13 ? 2   ASP   A CA  1 
ATOM   11   C  C   . ASP   A 1 13  ? -11.805 84.923 70.514  1.00 40.54 ? 2   ASP   A C   1 
ATOM   12   O  O   . ASP   A 1 13  ? -10.972 84.278 69.873  1.00 40.36 ? 2   ASP   A O   1 
ATOM   13   C  CB  . ASP   A 1 13  ? -11.038 84.845 72.897  1.00 42.10 ? 2   ASP   A CB  1 
ATOM   14   C  CG  . ASP   A 1 13  ? -10.717 86.316 72.915  1.00 43.64 ? 2   ASP   A CG  1 
ATOM   15   O  OD1 . ASP   A 1 13  ? -11.396 87.059 73.650  1.00 43.54 ? 2   ASP   A OD1 1 
ATOM   16   O  OD2 . ASP   A 1 13  ? -9.803  86.729 72.173  1.00 44.66 ? 2   ASP   A OD2 1 
ATOM   17   N  N   . TYR   A 1 14  ? -12.503 85.938 70.015  1.00 39.17 ? 3   TYR   A N   1 
ATOM   18   C  CA  . TYR   A 1 14  ? -12.341 86.461 68.673  1.00 39.11 ? 3   TYR   A CA  1 
ATOM   19   C  C   . TYR   A 1 14  ? -10.912 86.961 68.412  1.00 38.32 ? 3   TYR   A C   1 
ATOM   20   O  O   . TYR   A 1 14  ? -10.341 86.623 67.373  1.00 38.59 ? 3   TYR   A O   1 
ATOM   21   C  CB  . TYR   A 1 14  ? -13.396 87.564 68.394  1.00 39.86 ? 3   TYR   A CB  1 
ATOM   22   C  CG  . TYR   A 1 14  ? -13.198 88.215 67.049  1.00 41.67 ? 3   TYR   A CG  1 
ATOM   23   C  CD1 . TYR   A 1 14  ? -13.495 87.533 65.878  1.00 43.06 ? 3   TYR   A CD1 1 
ATOM   24   C  CD2 . TYR   A 1 14  ? -12.590 89.462 66.940  1.00 42.78 ? 3   TYR   A CD2 1 
ATOM   25   C  CE1 . TYR   A 1 14  ? -13.258 88.102 64.634  1.00 44.38 ? 3   TYR   A CE1 1 
ATOM   26   C  CE2 . TYR   A 1 14  ? -12.326 90.030 65.701  1.00 43.73 ? 3   TYR   A CE2 1 
ATOM   27   C  CZ  . TYR   A 1 14  ? -12.673 89.352 64.550  1.00 45.29 ? 3   TYR   A CZ  1 
ATOM   28   O  OH  . TYR   A 1 14  ? -12.405 89.897 63.318  1.00 47.72 ? 3   TYR   A OH  1 
ATOM   29   N  N   . ASP   A 1 15  ? -10.335 87.742 69.342  1.00 37.50 ? 4   ASP   A N   1 
ATOM   30   C  CA  . ASP   A 1 15  ? -8.970  88.274 69.199  1.00 37.90 ? 4   ASP   A CA  1 
ATOM   31   C  C   . ASP   A 1 15  ? -7.937  87.159 69.126  1.00 37.86 ? 4   ASP   A C   1 
ATOM   32   O  O   . ASP   A 1 15  ? -6.987  87.223 68.343  1.00 38.05 ? 4   ASP   A O   1 
ATOM   33   C  CB  . ASP   A 1 15  ? -8.623  89.226 70.358  1.00 39.68 ? 4   ASP   A CB  1 
ATOM   34   C  CG  . ASP   A 1 15  ? -9.481  90.464 70.390  1.00 45.47 ? 4   ASP   A CG  1 
ATOM   35   O  OD1 . ASP   A 1 15  ? -10.017 90.855 69.310  1.00 45.71 ? 4   ASP   A OD1 1 
ATOM   36   O  OD2 . ASP   A 1 15  ? -9.617  91.052 71.476  1.00 49.27 ? 4   ASP   A OD2 1 
ATOM   37   N  N   . PHE   A 1 16  ? -8.147  86.128 69.928  1.00 37.60 ? 5   PHE   A N   1 
ATOM   38   C  CA  . PHE   A 1 16  ? -7.325  84.938 69.961  1.00 37.85 ? 5   PHE   A CA  1 
ATOM   39   C  C   . PHE   A 1 16  ? -7.441  84.224 68.601  1.00 37.57 ? 5   PHE   A C   1 
ATOM   40   O  O   . PHE   A 1 16  ? -6.432  83.890 67.980  1.00 37.76 ? 5   PHE   A O   1 
ATOM   41   C  CB  . PHE   A 1 16  ? -7.839  84.072 71.104  1.00 38.32 ? 5   PHE   A CB  1 
ATOM   42   C  CG  . PHE   A 1 16  ? -7.208  82.721 71.255  1.00 40.34 ? 5   PHE   A CG  1 
ATOM   43   C  CD1 . PHE   A 1 16  ? -5.920  82.593 71.733  1.00 41.51 ? 5   PHE   A CD1 1 
ATOM   44   C  CD2 . PHE   A 1 16  ? -7.930  81.571 70.989  1.00 42.02 ? 5   PHE   A CD2 1 
ATOM   45   C  CE1 . PHE   A 1 16  ? -5.359  81.349 71.922  1.00 42.58 ? 5   PHE   A CE1 1 
ATOM   46   C  CE2 . PHE   A 1 16  ? -7.358  80.322 71.170  1.00 43.13 ? 5   PHE   A CE2 1 
ATOM   47   C  CZ  . PHE   A 1 16  ? -6.086  80.221 71.659  1.00 42.89 ? 5   PHE   A CZ  1 
ATOM   48   N  N   . LYS   A 1 17  ? -8.665  84.081 68.105  1.00 37.21 ? 6   LYS   A N   1 
ATOM   49   C  CA  . LYS   A 1 17  ? -8.950  83.405 66.848  1.00 37.75 ? 6   LYS   A CA  1 
ATOM   50   C  C   . LYS   A 1 17  ? -8.341  84.106 65.611  1.00 37.78 ? 6   LYS   A C   1 
ATOM   51   O  O   . LYS   A 1 17  ? -7.704  83.425 64.815  1.00 37.60 ? 6   LYS   A O   1 
ATOM   52   C  CB  . LYS   A 1 17  ? -10.465 83.189 66.717  1.00 40.06 ? 6   LYS   A CB  1 
ATOM   53   C  CG  . LYS   A 1 17  ? -10.894 82.478 65.455  1.00 46.03 ? 6   LYS   A CG  1 
ATOM   54   C  CD  . LYS   A 1 17  ? -12.370 82.120 65.502  1.00 51.64 ? 6   LYS   A CD  1 
ATOM   55   C  CE  . LYS   A 1 17  ? -12.994 82.242 64.131  1.00 56.17 ? 6   LYS   A CE  1 
ATOM   56   N  NZ  . LYS   A 1 17  ? -13.175 83.667 63.744  1.00 58.58 ? 6   LYS   A NZ  1 
ATOM   57   N  N   . VAL   A 1 18  ? -8.505  85.442 65.448  1.00 38.10 ? 7   VAL   A N   1 
ATOM   58   C  CA  . VAL   A 1 18  ? -7.919  86.155 64.292  1.00 38.48 ? 7   VAL   A CA  1 
ATOM   59   C  C   . VAL   A 1 18  ? -6.405  86.219 64.351  1.00 37.96 ? 7   VAL   A C   1 
ATOM   60   O  O   . VAL   A 1 18  ? -5.773  86.122 63.309  1.00 38.34 ? 7   VAL   A O   1 
ATOM   61   C  CB  . VAL   A 1 18  ? -8.497  87.561 64.002  1.00 39.87 ? 7   VAL   A CB  1 
ATOM   62   C  CG1 . VAL   A 1 18  ? -9.866  87.466 63.352  1.00 40.92 ? 7   VAL   A CG1 1 
ATOM   63   C  CG2 . VAL   A 1 18  ? -8.518  88.441 65.253  1.00 40.29 ? 7   VAL   A CG2 1 
ATOM   64   N  N   . LYS   A 1 19  ? -5.813  86.362 65.552  1.00 37.26 ? 8   LYS   A N   1 
ATOM   65   C  CA  . LYS   A 1 19  ? -4.362  86.362 65.720  1.00 38.20 ? 8   LYS   A CA  1 
ATOM   66   C  C   . LYS   A 1 19  ? -3.827  85.002 65.260  1.00 38.70 ? 8   LYS   A C   1 
ATOM   67   O  O   . LYS   A 1 19  ? -3.010  84.956 64.336  1.00 39.12 ? 8   LYS   A O   1 
ATOM   68   C  CB  . LYS   A 1 19  ? -3.973  86.647 67.200  1.00 41.03 ? 8   LYS   A CB  1 
ATOM   69   C  CG  . LYS   A 1 19  ? -2.573  86.181 67.597  1.00 46.11 ? 8   LYS   A CG  1 
ATOM   70   C  CD  . LYS   A 1 19  ? -1.722  87.283 68.169  1.00 52.33 ? 8   LYS   A CD  1 
ATOM   71   C  CE  . LYS   A 1 19  ? -0.253  86.971 67.975  1.00 57.86 ? 8   LYS   A CE  1 
ATOM   72   N  NZ  . LYS   A 1 19  ? 0.151   87.026 66.532  1.00 60.91 ? 8   LYS   A NZ  1 
ATOM   73   N  N   . LEU   A 1 20  ? -4.388  83.897 65.807  1.00 38.31 ? 9   LEU   A N   1 
ATOM   74   C  CA  . LEU   A 1 20  ? -3.986  82.554 65.394  1.00 38.59 ? 9   LEU   A CA  1 
ATOM   75   C  C   . LEU   A 1 20  ? -4.144  82.321 63.899  1.00 38.67 ? 9   LEU   A C   1 
ATOM   76   O  O   . LEU   A 1 20  ? -3.251  81.769 63.274  1.00 38.95 ? 9   LEU   A O   1 
ATOM   77   C  CB  . LEU   A 1 20  ? -4.737  81.481 66.171  1.00 38.62 ? 9   LEU   A CB  1 
ATOM   78   C  CG  . LEU   A 1 20  ? -4.323  81.294 67.617  1.00 40.03 ? 9   LEU   A CG  1 
ATOM   79   C  CD1 . LEU   A 1 20  ? -5.131  80.197 68.237  1.00 40.75 ? 9   LEU   A CD1 1 
ATOM   80   C  CD2 . LEU   A 1 20  ? -2.857  80.946 67.735  1.00 40.27 ? 9   LEU   A CD2 1 
ATOM   81   N  N   . SER   A 1 21  ? -5.250  82.765 63.330  1.00 38.40 ? 10  SER   A N   1 
ATOM   82   C  CA  . SER   A 1 21  ? -5.502  82.615 61.914  1.00 39.66 ? 10  SER   A CA  1 
ATOM   83   C  C   . SER   A 1 21  ? -4.467  83.403 61.083  1.00 41.19 ? 10  SER   A C   1 
ATOM   84   O  O   . SER   A 1 21  ? -3.972  82.889 60.085  1.00 41.45 ? 10  SER   A O   1 
ATOM   85   C  CB  . SER   A 1 21  ? -6.927  83.041 61.596  1.00 41.13 ? 10  SER   A CB  1 
ATOM   86   O  OG  . SER   A 1 21  ? -7.263  82.659 60.278  1.00 44.85 ? 10  SER   A OG  1 
ATOM   87   N  N   . SER   A 1 22  ? -4.086  84.613 61.541  1.00 41.75 ? 11  SER   A N   1 
ATOM   88   C  CA  . SER   A 1 22  ? -3.071  85.448 60.894  1.00 42.57 ? 11  SER   A CA  1 
ATOM   89   C  C   . SER   A 1 22  ? -1.677  84.781 60.942  1.00 42.79 ? 11  SER   A C   1 
ATOM   90   O  O   . SER   A 1 22  ? -0.978  84.740 59.931  1.00 42.81 ? 11  SER   A O   1 
ATOM   91   C  CB  . SER   A 1 22  ? -3.018  86.823 61.560  1.00 43.91 ? 11  SER   A CB  1 
ATOM   92   O  OG  . SER   A 1 22  ? -1.972  87.626 61.037  1.00 46.16 ? 11  SER   A OG  1 
ATOM   93   N  N   . GLU   A 1 23  ? -1.287  84.251 62.105  1.00 42.58 ? 12  GLU   A N   1 
ATOM   94   C  CA  . GLU   A 1 23  ? 0.004   83.592 62.255  1.00 43.49 ? 12  GLU   A CA  1 
ATOM   95   C  C   . GLU   A 1 23  ? 0.037   82.162 61.664  1.00 43.23 ? 12  GLU   A C   1 
ATOM   96   O  O   . GLU   A 1 23  ? 1.119   81.590 61.561  1.00 43.62 ? 12  GLU   A O   1 
ATOM   97   C  CB  . GLU   A 1 23  ? 0.376   83.495 63.754  1.00 47.11 ? 12  GLU   A CB  1 
ATOM   98   C  CG  . GLU   A 1 23  ? 0.651   84.823 64.437  1.00 54.65 ? 12  GLU   A CG  1 
ATOM   99   C  CD  . GLU   A 1 23  ? 1.928   85.505 63.979  1.00 65.24 ? 12  GLU   A CD  1 
ATOM   100  O  OE1 . GLU   A 1 23  ? 2.897   84.794 63.626  1.00 66.78 ? 12  GLU   A OE1 1 
ATOM   101  O  OE2 . GLU   A 1 23  ? 1.958   86.758 63.969  1.00 69.36 ? 12  GLU   A OE2 1 
ATOM   102  N  N   . ARG   A 1 24  ? -1.123  81.565 61.332  1.00 42.14 ? 13  ARG   A N   1 
ATOM   103  C  CA  . ARG   A 1 24  ? -1.168  80.174 60.896  1.00 41.95 ? 13  ARG   A CA  1 
ATOM   104  C  C   . ARG   A 1 24  ? -0.573  79.889 59.528  1.00 42.85 ? 13  ARG   A C   1 
ATOM   105  O  O   . ARG   A 1 24  ? -1.072  80.358 58.512  1.00 43.65 ? 13  ARG   A O   1 
ATOM   106  C  CB  . ARG   A 1 24  ? -2.584  79.591 60.970  1.00 41.89 ? 13  ARG   A CB  1 
ATOM   107  C  CG  . ARG   A 1 24  ? -2.611  78.077 60.842  1.00 42.17 ? 13  ARG   A CG  1 
ATOM   108  C  CD  . ARG   A 1 24  ? -3.959  77.460 61.195  1.00 42.48 ? 13  ARG   A CD  1 
ATOM   109  N  NE  . ARG   A 1 24  ? -4.288  77.629 62.611  1.00 42.38 ? 13  ARG   A NE  1 
ATOM   110  C  CZ  . ARG   A 1 24  ? -5.286  78.388 63.059  1.00 43.47 ? 13  ARG   A CZ  1 
ATOM   111  N  NH1 . ARG   A 1 24  ? -6.077  79.038 62.205  1.00 42.16 ? 13  ARG   A NH1 1 
ATOM   112  N  NH2 . ARG   A 1 24  ? -5.508  78.498 64.361  1.00 42.74 ? 13  ARG   A NH2 1 
ATOM   113  N  N   . GLU   A 1 25  ? 0.474   79.059 59.525  1.00 42.90 ? 14  GLU   A N   1 
ATOM   114  C  CA  . GLU   A 1 25  ? 1.170   78.570 58.348  1.00 43.41 ? 14  GLU   A CA  1 
ATOM   115  C  C   . GLU   A 1 25  ? 0.270   77.588 57.621  1.00 42.85 ? 14  GLU   A C   1 
ATOM   116  O  O   . GLU   A 1 25  ? -0.132  76.566 58.173  1.00 42.41 ? 14  GLU   A O   1 
ATOM   117  C  CB  . GLU   A 1 25  ? 2.467   77.863 58.751  1.00 46.82 ? 14  GLU   A CB  1 
ATOM   118  C  CG  . GLU   A 1 25  ? 3.598   78.823 59.062  1.00 55.06 ? 14  GLU   A CG  1 
ATOM   119  C  CD  . GLU   A 1 25  ? 4.909   78.136 59.383  1.00 65.41 ? 14  GLU   A CD  1 
ATOM   120  O  OE1 . GLU   A 1 25  ? 4.877   77.092 60.075  1.00 68.17 ? 14  GLU   A OE1 1 
ATOM   121  O  OE2 . GLU   A 1 25  ? 5.969   78.643 58.948  1.00 68.54 ? 14  GLU   A OE2 1 
ATOM   122  N  N   . ARG   A 1 26  ? -0.067  77.923 56.394  1.00 42.70 ? 15  ARG   A N   1 
ATOM   123  C  CA  . ARG   A 1 26  ? -0.905  77.101 55.567  1.00 43.30 ? 15  ARG   A CA  1 
ATOM   124  C  C   . ARG   A 1 26  ? -0.031  76.354 54.577  1.00 42.93 ? 15  ARG   A C   1 
ATOM   125  O  O   . ARG   A 1 26  ? 0.914   76.911 54.026  1.00 42.93 ? 15  ARG   A O   1 
ATOM   126  C  CB  . ARG   A 1 26  ? -1.964  77.964 54.893  1.00 46.51 ? 15  ARG   A CB  1 
ATOM   127  C  CG  . ARG   A 1 26  ? -2.942  78.521 55.915  1.00 51.46 ? 15  ARG   A CG  1 
ATOM   128  C  CD  . ARG   A 1 26  ? -3.626  79.797 55.474  1.00 56.64 ? 15  ARG   A CD  1 
ATOM   129  N  NE  . ARG   A 1 26  ? -4.872  80.021 56.220  1.00 62.32 ? 15  ARG   A NE  1 
ATOM   130  C  CZ  . ARG   A 1 26  ? -4.943  80.627 57.404  1.00 65.91 ? 15  ARG   A CZ  1 
ATOM   131  N  NH1 . ARG   A 1 26  ? -3.843  81.083 57.993  1.00 65.48 ? 15  ARG   A NH1 1 
ATOM   132  N  NH2 . ARG   A 1 26  ? -6.114  80.773 58.012  1.00 66.37 ? 15  ARG   A NH2 1 
ATOM   133  N  N   . VAL   A 1 27  ? -0.302  75.065 54.412  1.00 42.71 ? 16  VAL   A N   1 
ATOM   134  C  CA  . VAL   A 1 27  ? 0.454   74.183 53.539  1.00 42.68 ? 16  VAL   A CA  1 
ATOM   135  C  C   . VAL   A 1 27  ? 0.390   74.642 52.089  1.00 42.70 ? 16  VAL   A C   1 
ATOM   136  O  O   . VAL   A 1 27  ? 1.408   74.628 51.402  1.00 43.05 ? 16  VAL   A O   1 
ATOM   137  C  CB  . VAL   A 1 27  ? 0.010   72.710 53.736  1.00 43.31 ? 16  VAL   A CB  1 
ATOM   138  C  CG1 . VAL   A 1 27  ? -1.395  72.463 53.199  1.00 43.83 ? 16  VAL   A CG1 1 
ATOM   139  C  CG2 . VAL   A 1 27  ? 1.003   71.746 53.117  1.00 43.85 ? 16  VAL   A CG2 1 
ATOM   140  N  N   . GLU   A 1 28  ? -0.781  75.105 51.637  1.00 42.49 ? 17  GLU   A N   1 
ATOM   141  C  CA  . GLU   A 1 28  ? -0.960  75.575 50.259  1.00 43.20 ? 17  GLU   A CA  1 
ATOM   142  C  C   . GLU   A 1 28  ? -0.194  76.875 49.971  1.00 43.67 ? 17  GLU   A C   1 
ATOM   143  O  O   . GLU   A 1 28  ? 0.120   77.143 48.823  1.00 44.15 ? 17  GLU   A O   1 
ATOM   144  C  CB  . GLU   A 1 28  ? -2.454  75.686 49.878  1.00 43.98 ? 17  GLU   A CB  1 
ATOM   145  C  CG  . GLU   A 1 28  ? -3.201  76.832 50.537  1.00 45.72 ? 17  GLU   A CG  1 
ATOM   146  C  CD  . GLU   A 1 28  ? -3.814  76.525 51.890  1.00 48.99 ? 17  GLU   A CD  1 
ATOM   147  O  OE1 . GLU   A 1 28  ? -3.330  75.598 52.576  1.00 46.93 ? 17  GLU   A OE1 1 
ATOM   148  O  OE2 . GLU   A 1 28  ? -4.784  77.220 52.269  1.00 52.11 ? 17  GLU   A OE2 1 
ATOM   149  N  N   . ASP   A 1 29  ? 0.142   77.651 51.003  1.00 43.57 ? 18  ASP   A N   1 
ATOM   150  C  CA  . ASP   A 1 29  ? 0.924   78.874 50.837  1.00 44.09 ? 18  ASP   A CA  1 
ATOM   151  C  C   . ASP   A 1 29  ? 2.430   78.618 50.971  1.00 43.71 ? 18  ASP   A C   1 
ATOM   152  O  O   . ASP   A 1 29  ? 3.231   79.403 50.461  1.00 43.74 ? 18  ASP   A O   1 
ATOM   153  C  CB  . ASP   A 1 29  ? 0.517   79.916 51.883  1.00 46.12 ? 18  ASP   A CB  1 
ATOM   154  C  CG  . ASP   A 1 29  ? -0.916  80.381 51.773  1.00 51.51 ? 18  ASP   A CG  1 
ATOM   155  O  OD1 . ASP   A 1 29  ? -1.474  80.339 50.645  1.00 51.30 ? 18  ASP   A OD1 1 
ATOM   156  O  OD2 . ASP   A 1 29  ? -1.482  80.797 52.810  1.00 54.99 ? 18  ASP   A OD2 1 
ATOM   157  N  N   . LEU   A 1 30  ? 2.821   77.553 51.693  1.00 43.33 ? 19  LEU   A N   1 
ATOM   158  C  CA  . LEU   A 1 30  ? 4.229   77.272 51.902  1.00 43.12 ? 19  LEU   A CA  1 
ATOM   159  C  C   . LEU   A 1 30  ? 4.821   76.349 50.876  1.00 42.53 ? 19  LEU   A C   1 
ATOM   160  O  O   . LEU   A 1 30  ? 5.992   76.505 50.532  1.00 42.65 ? 19  LEU   A O   1 
ATOM   161  C  CB  . LEU   A 1 30  ? 4.479   76.758 53.313  1.00 43.44 ? 19  LEU   A CB  1 
ATOM   162  C  CG  . LEU   A 1 30  ? 4.462   77.852 54.369  1.00 45.74 ? 19  LEU   A CG  1 
ATOM   163  C  CD1 . LEU   A 1 30  ? 4.223   77.285 55.716  1.00 46.64 ? 19  LEU   A CD1 1 
ATOM   164  C  CD2 . LEU   A 1 30  ? 5.754   78.610 54.372  1.00 46.79 ? 19  LEU   A CD2 1 
ATOM   165  N  N   . PHE   A 1 31  ? 4.034   75.404 50.371  1.00 41.86 ? 20  PHE   A N   1 
ATOM   166  C  CA  . PHE   A 1 31  ? 4.561   74.425 49.439  1.00 41.53 ? 20  PHE   A CA  1 
ATOM   167  C  C   . PHE   A 1 31  ? 3.839   74.340 48.117  1.00 42.45 ? 20  PHE   A C   1 
ATOM   168  O  O   . PHE   A 1 31  ? 2.629   74.554 48.024  1.00 42.83 ? 20  PHE   A O   1 
ATOM   169  C  CB  . PHE   A 1 31  ? 4.619   73.049 50.111  1.00 40.41 ? 20  PHE   A CB  1 
ATOM   170  C  CG  . PHE   A 1 31  ? 5.597   73.016 51.261  1.00 39.17 ? 20  PHE   A CG  1 
ATOM   171  C  CD1 . PHE   A 1 31  ? 6.929   72.722 51.048  1.00 39.05 ? 20  PHE   A CD1 1 
ATOM   172  C  CD2 . PHE   A 1 31  ? 5.186   73.311 52.551  1.00 38.86 ? 20  PHE   A CD2 1 
ATOM   173  C  CE1 . PHE   A 1 31  ? 7.828   72.717 52.102  1.00 39.36 ? 20  PHE   A CE1 1 
ATOM   174  C  CE2 . PHE   A 1 31  ? 6.092   73.336 53.594  1.00 39.01 ? 20  PHE   A CE2 1 
ATOM   175  C  CZ  . PHE   A 1 31  ? 7.408   73.046 53.362  1.00 38.83 ? 20  PHE   A CZ  1 
ATOM   176  N  N   . GLU   A 1 32  ? 4.613   74.029 47.083  1.00 42.68 ? 21  GLU   A N   1 
ATOM   177  C  CA  . GLU   A 1 32  ? 4.134   73.788 45.737  1.00 43.44 ? 21  GLU   A CA  1 
ATOM   178  C  C   . GLU   A 1 32  ? 4.124   72.264 45.589  1.00 43.80 ? 21  GLU   A C   1 
ATOM   179  O  O   . GLU   A 1 32  ? 5.180   71.635 45.632  1.00 44.08 ? 21  GLU   A O   1 
ATOM   180  C  CB  . GLU   A 1 32  ? 5.081   74.431 44.708  1.00 46.18 ? 21  GLU   A CB  1 
ATOM   181  C  CG  . GLU   A 1 32  ? 4.646   74.246 43.262  1.00 51.06 ? 21  GLU   A CG  1 
ATOM   182  C  CD  . GLU   A 1 32  ? 3.199   74.589 42.958  1.00 57.94 ? 21  GLU   A CD  1 
ATOM   183  O  OE1 . GLU   A 1 32  ? 2.727   75.664 43.390  1.00 59.15 ? 21  GLU   A OE1 1 
ATOM   184  O  OE2 . GLU   A 1 32  ? 2.530   73.767 42.294  1.00 61.93 ? 21  GLU   A OE2 1 
ATOM   185  N  N   . TYR   A 1 33  ? 2.936   71.666 45.499  1.00 43.50 ? 22  TYR   A N   1 
ATOM   186  C  CA  . TYR   A 1 33  ? 2.803   70.221 45.437  1.00 43.79 ? 22  TYR   A CA  1 
ATOM   187  C  C   . TYR   A 1 33  ? 1.692   69.747 44.511  1.00 44.95 ? 22  TYR   A C   1 
ATOM   188  O  O   . TYR   A 1 33  ? 1.623   68.557 44.270  1.00 45.09 ? 22  TYR   A O   1 
ATOM   189  C  CB  . TYR   A 1 33  ? 2.567   69.652 46.850  1.00 43.27 ? 22  TYR   A CB  1 
ATOM   190  C  CG  . TYR   A 1 33  ? 1.342   70.232 47.526  1.00 43.23 ? 22  TYR   A CG  1 
ATOM   191  C  CD1 . TYR   A 1 33  ? 0.096   69.643 47.375  1.00 43.74 ? 22  TYR   A CD1 1 
ATOM   192  C  CD2 . TYR   A 1 33  ? 1.428   71.377 48.305  1.00 43.99 ? 22  TYR   A CD2 1 
ATOM   193  C  CE1 . TYR   A 1 33  ? -1.032  70.176 47.984  1.00 44.63 ? 22  TYR   A CE1 1 
ATOM   194  C  CE2 . TYR   A 1 33  ? 0.307   71.919 48.918  1.00 44.88 ? 22  TYR   A CE2 1 
ATOM   195  C  CZ  . TYR   A 1 33  ? -0.923  71.312 48.760  1.00 45.96 ? 22  TYR   A CZ  1 
ATOM   196  O  OH  . TYR   A 1 33  ? -2.045  71.852 49.347  1.00 48.26 ? 22  TYR   A OH  1 
ATOM   197  N  N   . GLU   A 1 34  ? 0.793   70.626 44.036  1.00 46.03 ? 23  GLU   A N   1 
ATOM   198  C  CA  . GLU   A 1 34  ? -0.308  70.187 43.164  1.00 47.49 ? 23  GLU   A CA  1 
ATOM   199  C  C   . GLU   A 1 34  ? 0.201   69.520 41.892  1.00 47.27 ? 23  GLU   A C   1 
ATOM   200  O  O   . GLU   A 1 34  ? 1.039   70.079 41.196  1.00 47.53 ? 23  GLU   A O   1 
ATOM   201  C  CB  . GLU   A 1 34  ? -1.290  71.324 42.866  1.00 51.91 ? 23  GLU   A CB  1 
ATOM   202  C  CG  . GLU   A 1 34  ? -2.306  71.508 43.986  1.00 59.66 ? 23  GLU   A CG  1 
ATOM   203  C  CD  . GLU   A 1 34  ? -3.327  72.601 43.741  1.00 68.64 ? 23  GLU   A CD  1 
ATOM   204  O  OE1 . GLU   A 1 34  ? -3.568  72.940 42.559  1.00 70.89 ? 23  GLU   A OE1 1 
ATOM   205  O  OE2 . GLU   A 1 34  ? -3.888  73.118 44.735  1.00 71.66 ? 23  GLU   A OE2 1 
ATOM   206  N  N   . GLY   A 1 35  ? -0.259  68.298 41.653  1.00 46.45 ? 24  GLY   A N   1 
ATOM   207  C  CA  . GLY   A 1 35  ? 0.199   67.482 40.536  1.00 46.18 ? 24  GLY   A CA  1 
ATOM   208  C  C   . GLY   A 1 35  ? 1.409   66.619 40.879  1.00 45.62 ? 24  GLY   A C   1 
ATOM   209  O  O   . GLY   A 1 35  ? 1.849   65.798 40.065  1.00 45.79 ? 24  GLY   A O   1 
ATOM   210  N  N   . CYS   A 1 36  ? 1.955   66.765 42.103  1.00 44.45 ? 25  CYS   A N   1 
ATOM   211  C  CA  . CYS   A 1 36  ? 3.157   66.055 42.502  1.00 43.40 ? 25  CYS   A CA  1 
ATOM   212  C  C   . CYS   A 1 36  ? 2.906   64.907 43.442  1.00 42.55 ? 25  CYS   A C   1 
ATOM   213  O  O   . CYS   A 1 36  ? 3.810   64.551 44.195  1.00 42.60 ? 25  CYS   A O   1 
ATOM   214  C  CB  . CYS   A 1 36  ? 4.201   67.010 43.069  1.00 43.67 ? 25  CYS   A CB  1 
ATOM   215  S  SG  . CYS   A 1 36  ? 4.511   68.473 42.054  1.00 46.80 ? 25  CYS   A SG  1 
ATOM   216  N  N   . LYS   A 1 37  ? 1.717   64.287 43.385  1.00 41.61 ? 26  LYS   A N   1 
ATOM   217  C  CA  . LYS   A 1 37  ? 1.455   63.121 44.229  1.00 40.95 ? 26  LYS   A CA  1 
ATOM   218  C  C   . LYS   A 1 37  ? 2.301   61.950 43.748  1.00 40.91 ? 26  LYS   A C   1 
ATOM   219  O  O   . LYS   A 1 37  ? 2.324   61.668 42.560  1.00 40.79 ? 26  LYS   A O   1 
ATOM   220  C  CB  . LYS   A 1 37  ? -0.030  62.737 44.222  1.00 41.09 ? 26  LYS   A CB  1 
ATOM   221  C  CG  . LYS   A 1 37  ? -0.361  61.715 45.298  1.00 43.19 ? 26  LYS   A CG  1 
ATOM   222  C  CD  . LYS   A 1 37  ? -1.819  61.306 45.300  1.00 45.70 ? 26  LYS   A CD  1 
ATOM   223  C  CE  . LYS   A 1 37  ? -2.722  62.486 45.521  1.00 48.76 ? 26  LYS   A CE  1 
ATOM   224  N  NZ  . LYS   A 1 37  ? -4.144  62.082 45.655  1.00 50.50 ? 26  LYS   A NZ  1 
ATOM   225  N  N   . VAL   A 1 38  ? 3.024   61.304 44.663  1.00 40.60 ? 27  VAL   A N   1 
ATOM   226  C  CA  . VAL   A 1 38  ? 3.849   60.113 44.416  1.00 40.63 ? 27  VAL   A CA  1 
ATOM   227  C  C   . VAL   A 1 38  ? 3.297   58.866 45.168  1.00 41.68 ? 27  VAL   A C   1 
ATOM   228  O  O   . VAL   A 1 38  ? 3.710   57.743 44.886  1.00 42.01 ? 27  VAL   A O   1 
ATOM   229  C  CB  . VAL   A 1 38  ? 5.340   60.351 44.767  1.00 40.35 ? 27  VAL   A CB  1 
ATOM   230  C  CG1 . VAL   A 1 38  ? 5.941   61.451 43.897  1.00 40.74 ? 27  VAL   A CG1 1 
ATOM   231  C  CG2 . VAL   A 1 38  ? 5.514   60.667 46.251  1.00 40.02 ? 27  VAL   A CG2 1 
ATOM   232  N  N   . GLY   A 1 39  ? 2.385   59.069 46.115  1.00 41.84 ? 28  GLY   A N   1 
ATOM   233  C  CA  . GLY   A 1 39  ? 1.807   57.980 46.877  1.00 42.28 ? 28  GLY   A CA  1 
ATOM   234  C  C   . GLY   A 1 39  ? 0.365   58.217 47.276  1.00 42.62 ? 28  GLY   A C   1 
ATOM   235  O  O   . GLY   A 1 39  ? -0.016  59.320 47.643  1.00 42.04 ? 28  GLY   A O   1 
ATOM   236  N  N   . ARG   A 1 40  ? -0.432  57.158 47.253  1.00 43.44 ? 29  ARG   A N   1 
ATOM   237  C  CA  . ARG   A 1 40  ? -1.831  57.189 47.651  1.00 44.20 ? 29  ARG   A CA  1 
ATOM   238  C  C   . ARG   A 1 40  ? -2.107  55.829 48.250  1.00 44.39 ? 29  ARG   A C   1 
ATOM   239  O  O   . ARG   A 1 40  ? -1.873  54.828 47.586  1.00 45.13 ? 29  ARG   A O   1 
ATOM   240  C  CB  . ARG   A 1 40  ? -2.737  57.410 46.427  1.00 45.83 ? 29  ARG   A CB  1 
ATOM   241  C  CG  . ARG   A 1 40  ? -4.214  57.211 46.725  1.00 49.04 ? 29  ARG   A CG  1 
ATOM   242  C  CD  . ARG   A 1 40  ? -4.738  58.345 47.565  1.00 52.48 ? 29  ARG   A CD  1 
ATOM   243  N  NE  . ARG   A 1 40  ? -6.137  58.172 47.953  1.00 54.78 ? 29  ARG   A NE  1 
ATOM   244  C  CZ  . ARG   A 1 40  ? -6.551  57.976 49.201  1.00 56.50 ? 29  ARG   A CZ  1 
ATOM   245  N  NH1 . ARG   A 1 40  ? -5.674  57.915 50.199  1.00 54.77 ? 29  ARG   A NH1 1 
ATOM   246  N  NH2 . ARG   A 1 40  ? -7.843  57.856 49.465  1.00 56.93 ? 29  ARG   A NH2 1 
ATOM   247  N  N   . GLY   A 1 41  ? -2.584  55.801 49.486  1.00 43.57 ? 30  GLY   A N   1 
ATOM   248  C  CA  . GLY   A 1 41  ? -2.909  54.569 50.193  1.00 43.28 ? 30  GLY   A CA  1 
ATOM   249  C  C   . GLY   A 1 41  ? -3.724  54.832 51.442  1.00 42.89 ? 30  GLY   A C   1 
ATOM   250  O  O   . GLY   A 1 41  ? -4.300  55.909 51.580  1.00 43.26 ? 30  GLY   A O   1 
ATOM   251  N  N   . THR   A 1 42  ? -3.783  53.871 52.371  1.00 42.24 ? 31  THR   A N   1 
ATOM   252  C  CA  . THR   A 1 42  ? -4.545  54.071 53.620  1.00 42.23 ? 31  THR   A CA  1 
ATOM   253  C  C   . THR   A 1 42  ? -3.921  55.140 54.534  1.00 40.96 ? 31  THR   A C   1 
ATOM   254  O  O   . THR   A 1 42  ? -4.585  55.657 55.429  1.00 41.12 ? 31  THR   A O   1 
ATOM   255  C  CB  . THR   A 1 42  ? -4.767  52.747 54.344  1.00 44.42 ? 31  THR   A CB  1 
ATOM   256  O  OG1 . THR   A 1 42  ? -3.490  52.226 54.739  1.00 46.39 ? 31  THR   A OG1 1 
ATOM   257  C  CG2 . THR   A 1 42  ? -5.526  51.734 53.480  1.00 44.71 ? 31  THR   A CG2 1 
ATOM   258  N  N   . TYR   A 1 43  ? -2.644  55.458 54.314  1.00 39.69 ? 32  TYR   A N   1 
ATOM   259  C  CA  . TYR   A 1 43  ? -1.919  56.529 54.991  1.00 38.31 ? 32  TYR   A CA  1 
ATOM   260  C  C   . TYR   A 1 43  ? -2.390  57.917 54.526  1.00 37.70 ? 32  TYR   A C   1 
ATOM   261  O  O   . TYR   A 1 43  ? -2.258  58.887 55.270  1.00 37.69 ? 32  TYR   A O   1 
ATOM   262  C  CB  . TYR   A 1 43  ? -0.414  56.386 54.747  1.00 37.65 ? 32  TYR   A CB  1 
ATOM   263  C  CG  . TYR   A 1 43  ? -0.020  56.221 53.296  1.00 37.26 ? 32  TYR   A CG  1 
ATOM   264  C  CD1 . TYR   A 1 43  ? 0.328   57.317 52.520  1.00 38.05 ? 32  TYR   A CD1 1 
ATOM   265  C  CD2 . TYR   A 1 43  ? 0.099   54.963 52.728  1.00 37.68 ? 32  TYR   A CD2 1 
ATOM   266  C  CE1 . TYR   A 1 43  ? 0.694   57.172 51.192  1.00 38.48 ? 32  TYR   A CE1 1 
ATOM   267  C  CE2 . TYR   A 1 43  ? 0.505   54.804 51.411  1.00 38.26 ? 32  TYR   A CE2 1 
ATOM   268  C  CZ  . TYR   A 1 43  ? 0.806   55.911 50.648  1.00 39.06 ? 32  TYR   A CZ  1 
ATOM   269  O  OH  . TYR   A 1 43  ? 1.182   55.775 49.341  1.00 40.72 ? 32  TYR   A OH  1 
ATOM   270  N  N   . GLY   A 1 44  ? -2.913  58.004 53.305  1.00 36.95 ? 33  GLY   A N   1 
ATOM   271  C  CA  . GLY   A 1 44  ? -3.388  59.249 52.741  1.00 37.59 ? 33  GLY   A CA  1 
ATOM   272  C  C   . GLY   A 1 44  ? -2.760  59.538 51.399  1.00 38.50 ? 33  GLY   A C   1 
ATOM   273  O  O   . GLY   A 1 44  ? -2.756  58.676 50.519  1.00 39.16 ? 33  GLY   A O   1 
ATOM   274  N  N   . HIS   A 1 45  ? -2.219  60.756 51.229  1.00 37.97 ? 34  HIS   A N   1 
ATOM   275  C  CA  . HIS   A 1 45  ? -1.625  61.163 49.959  1.00 37.84 ? 34  HIS   A CA  1 
ATOM   276  C  C   . HIS   A 1 45  ? -0.244  61.748 50.214  1.00 37.33 ? 34  HIS   A C   1 
ATOM   277  O  O   . HIS   A 1 45  ? -0.113  62.632 51.037  1.00 37.35 ? 34  HIS   A O   1 
ATOM   278  C  CB  . HIS   A 1 45  ? -2.503  62.229 49.258  1.00 38.44 ? 34  HIS   A CB  1 
ATOM   279  C  CG  . HIS   A 1 45  ? -3.984  62.013 49.383  1.00 40.54 ? 34  HIS   A CG  1 
ATOM   280  N  ND1 . HIS   A 1 45  ? -4.763  61.717 48.283  1.00 42.36 ? 34  HIS   A ND1 1 
ATOM   281  C  CD2 . HIS   A 1 45  ? -4.778  62.060 50.481  1.00 41.37 ? 34  HIS   A CD2 1 
ATOM   282  C  CE1 . HIS   A 1 45  ? -5.997  61.591 48.742  1.00 42.81 ? 34  HIS   A CE1 1 
ATOM   283  N  NE2 . HIS   A 1 45  ? -6.052  61.777 50.062  1.00 42.45 ? 34  HIS   A NE2 1 
ATOM   284  N  N   . VAL   A 1 46  ? 0.780   61.265 49.518  1.00 36.79 ? 35  VAL   A N   1 
ATOM   285  C  CA  . VAL   A 1 46  ? 2.142   61.771 49.675  1.00 36.53 ? 35  VAL   A CA  1 
ATOM   286  C  C   . VAL   A 1 46  ? 2.533   62.485 48.414  1.00 36.16 ? 35  VAL   A C   1 
ATOM   287  O  O   . VAL   A 1 46  ? 2.373   61.947 47.325  1.00 35.76 ? 35  VAL   A O   1 
ATOM   288  C  CB  . VAL   A 1 46  ? 3.168   60.661 50.018  1.00 36.85 ? 35  VAL   A CB  1 
ATOM   289  C  CG1 . VAL   A 1 46  ? 4.583   61.234 50.080  1.00 36.93 ? 35  VAL   A CG1 1 
ATOM   290  C  CG2 . VAL   A 1 46  ? 2.803   59.975 51.322  1.00 37.47 ? 35  VAL   A CG2 1 
ATOM   291  N  N   . TYR   A 1 47  ? 3.049   63.704 48.562  1.00 36.25 ? 36  TYR   A N   1 
ATOM   292  C  CA  . TYR   A 1 47  ? 3.472   64.560 47.467  1.00 36.27 ? 36  TYR   A CA  1 
ATOM   293  C  C   . TYR   A 1 47  ? 4.939   64.900 47.601  1.00 36.60 ? 36  TYR   A C   1 
ATOM   294  O  O   . TYR   A 1 47  ? 5.461   65.028 48.712  1.00 36.26 ? 36  TYR   A O   1 
ATOM   295  C  CB  . TYR   A 1 47  ? 2.707   65.899 47.534  1.00 36.04 ? 36  TYR   A CB  1 
ATOM   296  C  CG  . TYR   A 1 47  ? 1.206   65.775 47.407  1.00 37.14 ? 36  TYR   A CG  1 
ATOM   297  C  CD1 . TYR   A 1 47  ? 0.413   65.485 48.513  1.00 38.08 ? 36  TYR   A CD1 1 
ATOM   298  C  CD2 . TYR   A 1 47  ? 0.572   66.016 46.197  1.00 38.07 ? 36  TYR   A CD2 1 
ATOM   299  C  CE1 . TYR   A 1 47  ? -0.965  65.360 48.397  1.00 39.32 ? 36  TYR   A CE1 1 
ATOM   300  C  CE2 . TYR   A 1 47  ? -0.803  65.903 46.069  1.00 39.46 ? 36  TYR   A CE2 1 
ATOM   301  C  CZ  . TYR   A 1 47  ? -1.573  65.588 47.174  1.00 41.30 ? 36  TYR   A CZ  1 
ATOM   302  O  OH  . TYR   A 1 47  ? -2.939  65.491 47.029  1.00 44.26 ? 36  TYR   A OH  1 
ATOM   303  N  N   . LYS   A 1 48  ? 5.579   65.137 46.464  1.00 36.96 ? 37  LYS   A N   1 
ATOM   304  C  CA  . LYS   A 1 48  ? 6.931   65.650 46.391  1.00 37.53 ? 37  LYS   A CA  1 
ATOM   305  C  C   . LYS   A 1 48  ? 6.693   67.142 46.295  1.00 38.82 ? 37  LYS   A C   1 
ATOM   306  O  O   . LYS   A 1 48  ? 6.067   67.613 45.339  1.00 38.57 ? 37  LYS   A O   1 
ATOM   307  C  CB  . LYS   A 1 48  ? 7.624   65.138 45.133  1.00 38.76 ? 37  LYS   A CB  1 
ATOM   308  C  CG  . LYS   A 1 48  ? 9.010   65.714 44.954  1.00 41.97 ? 37  LYS   A CG  1 
ATOM   309  C  CD  . LYS   A 1 48  ? 9.639   65.179 43.692  1.00 46.54 ? 37  LYS   A CD  1 
ATOM   310  C  CE  . LYS   A 1 48  ? 11.026  65.718 43.527  1.00 51.52 ? 37  LYS   A CE  1 
ATOM   311  N  NZ  . LYS   A 1 48  ? 11.611  65.332 42.218  1.00 54.83 ? 37  LYS   A NZ  1 
ATOM   312  N  N   . ALA   A 1 49  ? 7.097   67.888 47.323  1.00 39.90 ? 38  ALA   A N   1 
ATOM   313  C  CA  . ALA   A 1 49  ? 6.825   69.315 47.386  1.00 41.50 ? 38  ALA   A CA  1 
ATOM   314  C  C   . ALA   A 1 49  ? 8.079   70.186 47.381  1.00 43.28 ? 38  ALA   A C   1 
ATOM   315  O  O   . ALA   A 1 49  ? 9.153   69.738 47.754  1.00 43.52 ? 38  ALA   A O   1 
ATOM   316  C  CB  . ALA   A 1 49  ? 5.984   69.606 48.628  1.00 41.43 ? 38  ALA   A CB  1 
ATOM   317  N  N   . LYS   A 1 50  ? 7.941   71.435 46.958  1.00 44.65 ? 39  LYS   A N   1 
ATOM   318  C  CA  . LYS   A 1 50  ? 9.019   72.426 46.976  1.00 46.52 ? 39  LYS   A CA  1 
ATOM   319  C  C   . LYS   A 1 50  ? 8.524   73.622 47.791  1.00 47.93 ? 39  LYS   A C   1 
ATOM   320  O  O   . LYS   A 1 50  ? 7.320   73.857 47.841  1.00 48.04 ? 39  LYS   A O   1 
ATOM   321  C  CB  . LYS   A 1 50  ? 9.346   72.899 45.552  1.00 49.22 ? 39  LYS   A CB  1 
ATOM   322  C  CG  . LYS   A 1 50  ? 10.354  72.024 44.834  1.00 55.05 ? 39  LYS   A CG  1 
ATOM   323  C  CD  . LYS   A 1 50  ? 11.777  72.392 45.215  1.00 60.44 ? 39  LYS   A CD  1 
ATOM   324  C  CE  . LYS   A 1 50  ? 12.734  72.234 44.058  1.00 64.74 ? 39  LYS   A CE  1 
ATOM   325  N  NZ  . LYS   A 1 50  ? 12.739  70.843 43.538  1.00 67.64 ? 39  LYS   A NZ  1 
ATOM   326  N  N   . ARG   A 1 51  ? 9.431   74.381 48.415  1.00 48.92 ? 40  ARG   A N   1 
ATOM   327  C  CA  . ARG   A 1 51  ? 9.026   75.577 49.142  1.00 50.75 ? 40  ARG   A CA  1 
ATOM   328  C  C   . ARG   A 1 51  ? 8.719   76.686 48.142  1.00 51.87 ? 40  ARG   A C   1 
ATOM   329  O  O   . ARG   A 1 51  ? 9.443   76.864 47.162  1.00 51.81 ? 40  ARG   A O   1 
ATOM   330  C  CB  . ARG   A 1 51  ? 10.116  76.037 50.098  1.00 53.07 ? 40  ARG   A CB  1 
ATOM   331  C  CG  . ARG   A 1 51  ? 10.487  74.996 51.126  1.00 57.29 ? 40  ARG   A CG  1 
ATOM   332  C  CD  . ARG   A 1 51  ? 11.615  75.493 51.993  1.00 61.77 ? 40  ARG   A CD  1 
ATOM   333  N  NE  . ARG   A 1 51  ? 11.226  76.674 52.758  1.00 66.47 ? 40  ARG   A NE  1 
ATOM   334  C  CZ  . ARG   A 1 51  ? 11.880  77.127 53.821  1.00 70.91 ? 40  ARG   A CZ  1 
ATOM   335  N  NH1 . ARG   A 1 51  ? 11.439  78.196 54.472  1.00 71.86 ? 40  ARG   A NH1 1 
ATOM   336  N  NH2 . ARG   A 1 51  ? 12.970  76.501 54.258  1.00 71.24 ? 40  ARG   A NH2 1 
ATOM   337  N  N   . LYS   A 1 52  ? 7.628   77.407 48.374  1.00 52.60 ? 41  LYS   A N   1 
ATOM   338  C  CA  . LYS   A 1 52  ? 7.224   78.503 47.511  1.00 53.91 ? 41  LYS   A CA  1 
ATOM   339  C  C   . LYS   A 1 52  ? 8.093   79.733 47.764  1.00 56.44 ? 41  LYS   A C   1 
ATOM   340  O  O   . LYS   A 1 52  ? 8.426   80.435 46.816  1.00 56.74 ? 41  LYS   A O   1 
ATOM   341  C  CB  . LYS   A 1 52  ? 5.737   78.820 47.697  1.00 53.95 ? 41  LYS   A CB  1 
ATOM   342  C  CG  . LYS   A 1 52  ? 4.833   77.904 46.893  1.00 54.81 ? 41  LYS   A CG  1 
ATOM   343  C  CD  . LYS   A 1 52  ? 3.406   78.365 46.977  1.00 57.01 ? 41  LYS   A CD  1 
ATOM   344  C  CE  . LYS   A 1 52  ? 2.476   77.439 46.260  1.00 59.73 ? 41  LYS   A CE  1 
ATOM   345  N  NZ  . LYS   A 1 52  ? 1.073   77.900 46.363  1.00 62.27 ? 41  LYS   A NZ  1 
ATOM   346  N  N   . ASP   A 1 53  ? 8.513   79.967 49.029  1.00 57.95 ? 42  ASP   A N   1 
ATOM   347  C  CA  . ASP   A 1 53  ? 9.402   81.087 49.355  1.00 59.65 ? 42  ASP   A CA  1 
ATOM   348  C  C   . ASP   A 1 53  ? 10.830  80.940 48.778  1.00 61.08 ? 42  ASP   A C   1 
ATOM   349  O  O   . ASP   A 1 53  ? 11.615  81.875 48.859  1.00 61.37 ? 42  ASP   A O   1 
ATOM   350  C  CB  . ASP   A 1 53  ? 9.439   81.364 50.866  1.00 61.53 ? 42  ASP   A CB  1 
ATOM   351  C  CG  . ASP   A 1 53  ? 10.010  80.250 51.713  1.00 66.06 ? 42  ASP   A CG  1 
ATOM   352  O  OD1 . ASP   A 1 53  ? 10.631  79.333 51.146  1.00 66.59 ? 42  ASP   A OD1 1 
ATOM   353  O  OD2 . ASP   A 1 53  ? 9.821   80.288 52.945  1.00 68.53 ? 42  ASP   A OD2 1 
ATOM   354  N  N   . GLY   A 1 54  ? 11.145  79.768 48.230  1.00 62.01 ? 43  GLY   A N   1 
ATOM   355  C  CA  . GLY   A 1 54  ? 12.401  79.472 47.558  1.00 63.46 ? 43  GLY   A CA  1 
ATOM   356  C  C   . GLY   A 1 54  ? 13.705  79.636 48.311  1.00 64.49 ? 43  GLY   A C   1 
ATOM   357  O  O   . GLY   A 1 54  ? 14.761  79.651 47.668  1.00 64.85 ? 43  GLY   A O   1 
ATOM   358  N  N   . LYS   A 1 55  ? 13.672  79.730 49.661  1.00 64.65 ? 44  LYS   A N   1 
ATOM   359  C  CA  . LYS   A 1 55  ? 14.930  79.857 50.414  1.00 65.54 ? 44  LYS   A CA  1 
ATOM   360  C  C   . LYS   A 1 55  ? 15.716  78.549 50.506  1.00 65.98 ? 44  LYS   A C   1 
ATOM   361  O  O   . LYS   A 1 55  ? 16.858  78.571 50.952  1.00 66.47 ? 44  LYS   A O   1 
ATOM   362  C  CB  . LYS   A 1 55  ? 14.758  80.502 51.799  1.00 67.82 ? 44  LYS   A CB  1 
ATOM   363  C  CG  . LYS   A 1 55  ? 13.496  80.128 52.545  1.00 71.98 ? 44  LYS   A CG  1 
ATOM   364  C  CD  . LYS   A 1 55  ? 13.125  81.184 53.600  1.00 76.26 ? 44  LYS   A CD  1 
ATOM   365  C  CE  . LYS   A 1 55  ? 12.772  82.523 52.991  1.00 79.55 ? 44  LYS   A CE  1 
ATOM   366  N  NZ  . LYS   A 1 55  ? 12.388  83.523 54.024  1.00 81.28 ? 44  LYS   A NZ  1 
ATOM   367  N  N   . ASP   A 1 56  ? 15.120  77.427 50.048  1.00 65.67 ? 45  ASP   A N   1 
ATOM   368  C  CA  . ASP   A 1 56  ? 15.695  76.090 49.946  1.00 65.68 ? 45  ASP   A CA  1 
ATOM   369  C  C   . ASP   A 1 56  ? 15.409  75.575 48.540  1.00 64.59 ? 45  ASP   A C   1 
ATOM   370  O  O   . ASP   A 1 56  ? 14.340  75.855 47.986  1.00 64.88 ? 45  ASP   A O   1 
ATOM   371  C  CB  . ASP   A 1 56  ? 14.973  75.115 50.903  1.00 68.43 ? 45  ASP   A CB  1 
ATOM   372  C  CG  . ASP   A 1 56  ? 15.660  74.829 52.217  1.00 74.60 ? 45  ASP   A CG  1 
ATOM   373  O  OD1 . ASP   A 1 56  ? 16.902  74.691 52.219  1.00 76.36 ? 45  ASP   A OD1 1 
ATOM   374  O  OD2 . ASP   A 1 56  ? 14.952  74.718 53.243  1.00 76.75 ? 45  ASP   A OD2 1 
ATOM   375  N  N   . ASP   A 1 57  ? 16.319  74.777 47.984  1.00 63.09 ? 46  ASP   A N   1 
ATOM   376  C  CA  . ASP   A 1 57  ? 16.047  74.095 46.711  1.00 62.16 ? 46  ASP   A CA  1 
ATOM   377  C  C   . ASP   A 1 57  ? 15.743  72.575 46.955  1.00 59.86 ? 46  ASP   A C   1 
ATOM   378  O  O   . ASP   A 1 57  ? 15.577  71.813 45.997  1.00 59.96 ? 46  ASP   A O   1 
ATOM   379  C  CB  . ASP   A 1 57  ? 17.203  74.272 45.718  1.00 65.01 ? 46  ASP   A CB  1 
ATOM   380  C  CG  . ASP   A 1 57  ? 16.831  73.906 44.291  1.00 71.87 ? 46  ASP   A CG  1 
ATOM   381  O  OD1 . ASP   A 1 57  ? 15.780  74.395 43.806  1.00 73.03 ? 46  ASP   A OD1 1 
ATOM   382  O  OD2 . ASP   A 1 57  ? 17.583  73.118 43.662  1.00 74.54 ? 46  ASP   A OD2 1 
ATOM   383  N  N   . LYS   A 1 58  ? 15.673  72.152 48.241  1.00 57.31 ? 47  LYS   A N   1 
ATOM   384  C  CA  . LYS   A 1 58  ? 15.436  70.783 48.653  1.00 55.44 ? 47  LYS   A CA  1 
ATOM   385  C  C   . LYS   A 1 58  ? 14.060  70.310 48.248  1.00 52.74 ? 47  LYS   A C   1 
ATOM   386  O  O   . LYS   A 1 58  ? 13.111  71.097 48.184  1.00 52.73 ? 47  LYS   A O   1 
ATOM   387  C  CB  . LYS   A 1 58  ? 15.513  70.675 50.183  1.00 57.41 ? 47  LYS   A CB  1 
ATOM   388  C  CG  . LYS   A 1 58  ? 16.769  71.221 50.821  1.00 61.89 ? 47  LYS   A CG  1 
ATOM   389  C  CD  . LYS   A 1 58  ? 16.621  71.278 52.344  1.00 66.92 ? 47  LYS   A CD  1 
ATOM   390  C  CE  . LYS   A 1 58  ? 16.341  69.923 52.965  1.00 71.80 ? 47  LYS   A CE  1 
ATOM   391  N  NZ  . LYS   A 1 58  ? 16.367  69.967 54.454  1.00 74.54 ? 47  LYS   A NZ  1 
ATOM   392  N  N   . ASP   A 1 59  ? 13.943  69.004 48.024  1.00 50.06 ? 48  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 59  ? 12.656  68.383 47.775  1.00 47.68 ? 48  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 59  ? 12.110  67.950 49.130  1.00 44.22 ? 48  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 59  ? 12.872  67.525 49.999  1.00 43.99 ? 48  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 59  ? 12.813  67.177 46.855  1.00 49.61 ? 48  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 59  ? 13.134  67.590 45.449  1.00 55.14 ? 48  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 59  ? 12.475  68.517 44.942  1.00 57.54 ? 48  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 59  ? 14.040  66.989 44.851  1.00 56.99 ? 48  ASP   A OD2 1 
ATOM   400  N  N   . TYR   A 1 60  ? 10.804  68.071 49.326  1.00 41.71 ? 49  TYR   A N   1 
ATOM   401  C  CA  . TYR   A 1 60  ? 10.167  67.656 50.583  1.00 39.84 ? 49  TYR   A CA  1 
ATOM   402  C  C   . TYR   A 1 60  ? 9.090   66.600 50.319  1.00 37.25 ? 49  TYR   A C   1 
ATOM   403  O  O   . TYR   A 1 60  ? 8.614   66.462 49.196  1.00 36.49 ? 49  TYR   A O   1 
ATOM   404  C  CB  . TYR   A 1 60  ? 9.542   68.871 51.308  1.00 40.05 ? 49  TYR   A CB  1 
ATOM   405  C  CG  . TYR   A 1 60  ? 10.562  69.802 51.923  1.00 41.13 ? 49  TYR   A CG  1 
ATOM   406  C  CD1 . TYR   A 1 60  ? 11.088  70.867 51.200  1.00 42.35 ? 49  TYR   A CD1 1 
ATOM   407  C  CD2 . TYR   A 1 60  ? 11.026  69.599 53.216  1.00 42.23 ? 49  TYR   A CD2 1 
ATOM   408  C  CE1 . TYR   A 1 60  ? 12.045  71.709 51.751  1.00 43.54 ? 49  TYR   A CE1 1 
ATOM   409  C  CE2 . TYR   A 1 60  ? 11.984  70.431 53.778  1.00 43.30 ? 49  TYR   A CE2 1 
ATOM   410  C  CZ  . TYR   A 1 60  ? 12.485  71.493 53.046  1.00 44.75 ? 49  TYR   A CZ  1 
ATOM   411  O  OH  . TYR   A 1 60  ? 13.428  72.322 53.609  1.00 46.60 ? 49  TYR   A OH  1 
ATOM   412  N  N   . ALA   A 1 61  ? 8.729   65.837 51.344  1.00 35.85 ? 50  ALA   A N   1 
ATOM   413  C  CA  . ALA   A 1 61  ? 7.644   64.885 51.250  1.00 35.34 ? 50  ALA   A CA  1 
ATOM   414  C  C   . ALA   A 1 61  ? 6.534   65.462 52.108  1.00 34.78 ? 50  ALA   A C   1 
ATOM   415  O  O   . ALA   A 1 61  ? 6.738   65.779 53.278  1.00 35.08 ? 50  ALA   A O   1 
ATOM   416  C  CB  . ALA   A 1 61  ? 8.063   63.509 51.760  1.00 35.19 ? 50  ALA   A CB  1 
ATOM   417  N  N   . LEU   A 1 62  ? 5.387   65.674 51.504  1.00 34.16 ? 51  LEU   A N   1 
ATOM   418  C  CA  . LEU   A 1 62  ? 4.227   66.229 52.185  1.00 34.04 ? 51  LEU   A CA  1 
ATOM   419  C  C   . LEU   A 1 62  ? 3.166   65.165 52.224  1.00 34.29 ? 51  LEU   A C   1 
ATOM   420  O  O   . LEU   A 1 62  ? 2.768   64.695 51.162  1.00 35.49 ? 51  LEU   A O   1 
ATOM   421  C  CB  . LEU   A 1 62  ? 3.659   67.387 51.365  1.00 33.15 ? 51  LEU   A CB  1 
ATOM   422  C  CG  . LEU   A 1 62  ? 3.788   68.769 51.904  1.00 33.91 ? 51  LEU   A CG  1 
ATOM   423  C  CD1 . LEU   A 1 62  ? 3.023   69.726 51.008  1.00 34.91 ? 51  LEU   A CD1 1 
ATOM   424  C  CD2 . LEU   A 1 62  ? 3.271   68.876 53.360  1.00 33.77 ? 51  LEU   A CD2 1 
ATOM   425  N  N   . LYS   A 1 63  ? 2.643   64.853 53.396  1.00 32.97 ? 52  LYS   A N   1 
ATOM   426  C  CA  . LYS   A 1 63  ? 1.597   63.860 53.495  1.00 32.71 ? 52  LYS   A CA  1 
ATOM   427  C  C   . LYS   A 1 63  ? 0.318   64.461 53.985  1.00 33.64 ? 52  LYS   A C   1 
ATOM   428  O  O   . LYS   A 1 63  ? 0.320   65.057 55.037  1.00 33.94 ? 52  LYS   A O   1 
ATOM   429  C  CB  . LYS   A 1 63  ? 2.014   62.687 54.405  1.00 32.25 ? 52  LYS   A CB  1 
ATOM   430  C  CG  . LYS   A 1 63  ? 0.912   61.643 54.540  1.00 32.89 ? 52  LYS   A CG  1 
ATOM   431  C  CD  . LYS   A 1 63  ? 1.385   60.342 55.080  1.00 34.97 ? 52  LYS   A CD  1 
ATOM   432  C  CE  . LYS   A 1 63  ? 1.854   60.452 56.499  1.00 35.93 ? 52  LYS   A CE  1 
ATOM   433  N  NZ  . LYS   A 1 63  ? 1.938   59.108 57.093  1.00 36.25 ? 52  LYS   A NZ  1 
ATOM   434  N  N   . GLN   A 1 64  ? -0.778  64.287 53.254  1.00 34.48 ? 53  GLN   A N   1 
ATOM   435  C  CA  . GLN   A 1 64  ? -2.086  64.686 53.749  1.00 35.81 ? 53  GLN   A CA  1 
ATOM   436  C  C   . GLN   A 1 64  ? -2.630  63.383 54.334  1.00 36.90 ? 53  GLN   A C   1 
ATOM   437  O  O   . GLN   A 1 64  ? -2.869  62.427 53.594  1.00 36.94 ? 53  GLN   A O   1 
ATOM   438  C  CB  . GLN   A 1 64  ? -3.004  65.175 52.630  1.00 37.54 ? 53  GLN   A CB  1 
ATOM   439  C  CG  . GLN   A 1 64  ? -4.335  65.670 53.156  1.00 41.40 ? 53  GLN   A CG  1 
ATOM   440  C  CD  . GLN   A 1 64  ? -5.285  66.002 52.028  1.00 49.54 ? 53  GLN   A CD  1 
ATOM   441  O  OE1 . GLN   A 1 64  ? -5.476  65.219 51.084  1.00 51.94 ? 53  GLN   A OE1 1 
ATOM   442  N  NE2 . GLN   A 1 64  ? -5.913  67.174 52.098  1.00 51.25 ? 53  GLN   A NE2 1 
ATOM   443  N  N   . ILE   A 1 65  ? -2.754  63.309 55.661  1.00 37.40 ? 54  ILE   A N   1 
ATOM   444  C  CA  . ILE   A 1 65  ? -3.256  62.109 56.317  1.00 38.68 ? 54  ILE   A CA  1 
ATOM   445  C  C   . ILE   A 1 65  ? -4.674  61.775 55.842  1.00 39.73 ? 54  ILE   A C   1 
ATOM   446  O  O   . ILE   A 1 65  ? -5.439  62.669 55.500  1.00 39.82 ? 54  ILE   A O   1 
ATOM   447  C  CB  . ILE   A 1 65  ? -3.161  62.282 57.850  1.00 39.50 ? 54  ILE   A CB  1 
ATOM   448  C  CG1 . ILE   A 1 65  ? -1.691  62.446 58.283  1.00 40.15 ? 54  ILE   A CG1 1 
ATOM   449  C  CG2 . ILE   A 1 65  ? -3.846  61.141 58.590  1.00 40.31 ? 54  ILE   A CG2 1 
ATOM   450  C  CD1 . ILE   A 1 65  ? -1.514  62.864 59.674  1.00 41.01 ? 54  ILE   A CD1 1 
ATOM   451  N  N   . GLU   A 1 66  ? -4.981  60.490 55.747  1.00 40.50 ? 55  GLU   A N   1 
ATOM   452  C  CA  . GLU   A 1 66  ? -6.275  59.987 55.324  1.00 41.34 ? 55  GLU   A CA  1 
ATOM   453  C  C   . GLU   A 1 66  ? -7.394  60.424 56.292  1.00 42.23 ? 55  GLU   A C   1 
ATOM   454  O  O   . GLU   A 1 66  ? -7.224  60.355 57.506  1.00 42.46 ? 55  GLU   A O   1 
ATOM   455  C  CB  . GLU   A 1 66  ? -6.196  58.460 55.237  1.00 42.97 ? 55  GLU   A CB  1 
ATOM   456  C  CG  . GLU   A 1 66  ? -7.497  57.772 54.879  1.00 48.28 ? 55  GLU   A CG  1 
ATOM   457  C  CD  . GLU   A 1 66  ? -7.984  58.018 53.468  1.00 55.75 ? 55  GLU   A CD  1 
ATOM   458  O  OE1 . GLU   A 1 66  ? -7.141  58.249 52.572  1.00 56.66 ? 55  GLU   A OE1 1 
ATOM   459  O  OE2 . GLU   A 1 66  ? -9.218  57.987 53.260  1.00 59.68 ? 55  GLU   A OE2 1 
ATOM   460  N  N   . GLY   A 1 67  ? -8.502  60.903 55.736  1.00 42.49 ? 56  GLY   A N   1 
ATOM   461  C  CA  . GLY   A 1 67  ? -9.673  61.312 56.491  1.00 43.10 ? 56  GLY   A CA  1 
ATOM   462  C  C   . GLY   A 1 67  ? -9.577  62.688 57.106  1.00 43.72 ? 56  GLY   A C   1 
ATOM   463  O  O   . GLY   A 1 67  ? -8.549  63.360 57.001  1.00 44.33 ? 56  GLY   A O   1 
ATOM   464  N  N   . THR   A 1 68  ? -10.664 63.127 57.735  1.00 43.45 ? 57  THR   A N   1 
ATOM   465  C  CA  . THR   A 1 68  ? -10.675 64.425 58.387  1.00 43.67 ? 57  THR   A CA  1 
ATOM   466  C  C   . THR   A 1 68  ? -10.458 64.249 59.896  1.00 42.47 ? 57  THR   A C   1 
ATOM   467  O  O   . THR   A 1 68  ? -10.672 63.174 60.463  1.00 42.44 ? 57  THR   A O   1 
ATOM   468  C  CB  . THR   A 1 68  ? -11.909 65.262 58.000  1.00 46.14 ? 57  THR   A CB  1 
ATOM   469  O  OG1 . THR   A 1 68  ? -13.039 64.856 58.772  1.00 48.36 ? 57  THR   A OG1 1 
ATOM   470  C  CG2 . THR   A 1 68  ? -12.232 65.193 56.496  1.00 46.35 ? 57  THR   A CG2 1 
ATOM   471  N  N   . GLY   A 1 69  ? -9.992  65.310 60.515  1.00 41.00 ? 58  GLY   A N   1 
ATOM   472  C  CA  . GLY   A 1 69  ? -9.716  65.341 61.934  1.00 39.91 ? 58  GLY   A CA  1 
ATOM   473  C  C   . GLY   A 1 69  ? -8.483  64.565 62.294  1.00 38.51 ? 58  GLY   A C   1 
ATOM   474  O  O   . GLY   A 1 69  ? -7.616  64.332 61.458  1.00 38.97 ? 58  GLY   A O   1 
ATOM   475  N  N   . ILE   A 1 70  ? -8.412  64.151 63.537  1.00 37.25 ? 59  ILE   A N   1 
ATOM   476  C  CA  . ILE   A 1 70  ? -7.275  63.399 64.035  1.00 36.64 ? 59  ILE   A CA  1 
ATOM   477  C  C   . ILE   A 1 70  ? -7.769  62.016 64.359  1.00 35.04 ? 59  ILE   A C   1 
ATOM   478  O  O   . ILE   A 1 70  ? -8.407  61.802 65.387  1.00 35.01 ? 59  ILE   A O   1 
ATOM   479  C  CB  . ILE   A 1 70  ? -6.666  64.124 65.257  1.00 37.74 ? 59  ILE   A CB  1 
ATOM   480  C  CG1 . ILE   A 1 70  ? -6.262  65.546 64.868  1.00 39.56 ? 59  ILE   A CG1 1 
ATOM   481  C  CG2 . ILE   A 1 70  ? -5.473  63.365 65.817  1.00 38.45 ? 59  ILE   A CG2 1 
ATOM   482  C  CD1 . ILE   A 1 70  ? -6.710  66.548 65.828  1.00 41.65 ? 59  ILE   A CD1 1 
ATOM   483  N  N   . SER   A 1 71  ? -7.564  61.094 63.429  1.00 33.71 ? 60  SER   A N   1 
ATOM   484  C  CA  . SER   A 1 71  ? -7.955  59.712 63.599  1.00 33.34 ? 60  SER   A CA  1 
ATOM   485  C  C   . SER   A 1 71  ? -6.944  59.032 64.533  1.00 33.70 ? 60  SER   A C   1 
ATOM   486  O  O   . SER   A 1 71  ? -5.909  59.613 64.852  1.00 33.36 ? 60  SER   A O   1 
ATOM   487  C  CB  . SER   A 1 71  ? -7.959  59.011 62.242  1.00 34.19 ? 60  SER   A CB  1 
ATOM   488  O  OG  . SER   A 1 71  ? -6.709  59.141 61.581  1.00 36.26 ? 60  SER   A OG  1 
ATOM   489  N  N   . MET   A 1 72  ? -7.199  57.782 64.936  1.00 34.31 ? 61  MET   A N   1 
ATOM   490  C  CA  . MET   A 1 72  ? -6.240  57.006 65.745  1.00 34.99 ? 61  MET   A CA  1 
ATOM   491  C  C   . MET   A 1 72  ? -4.911  56.882 65.004  1.00 34.24 ? 61  MET   A C   1 
ATOM   492  O  O   . MET   A 1 72  ? -3.856  57.078 65.585  1.00 34.33 ? 61  MET   A O   1 
ATOM   493  C  CB  . MET   A 1 72  ? -6.789  55.597 66.024  1.00 36.36 ? 61  MET   A CB  1 
ATOM   494  C  CG  . MET   A 1 72  ? -8.041  55.613 66.842  1.00 40.64 ? 61  MET   A CG  1 
ATOM   495  S  SD  . MET   A 1 72  ? -7.704  56.195 68.507  1.00 50.67 ? 61  MET   A SD  1 
ATOM   496  C  CE  . MET   A 1 72  ? -6.837  54.782 69.168  1.00 40.80 ? 61  MET   A CE  1 
ATOM   497  N  N   . SER   A 1 73  ? -4.989  56.630 63.706  1.00 33.86 ? 62  SER   A N   1 
ATOM   498  C  CA  . SER   A 1 73  ? -3.840  56.513 62.841  1.00 34.25 ? 62  SER   A CA  1 
ATOM   499  C  C   . SER   A 1 73  ? -3.012  57.816 62.836  1.00 33.36 ? 62  SER   A C   1 
ATOM   500  O  O   . SER   A 1 73  ? -1.821  57.767 63.134  1.00 33.51 ? 62  SER   A O   1 
ATOM   501  C  CB  . SER   A 1 73  ? -4.300  56.136 61.432  1.00 36.48 ? 62  SER   A CB  1 
ATOM   502  O  OG  . SER   A 1 73  ? -3.205  56.063 60.539  1.00 39.79 ? 62  SER   A OG  1 
ATOM   503  N  N   . ALA   A 1 74  ? -3.648  58.974 62.552  1.00 32.41 ? 63  ALA   A N   1 
ATOM   504  C  CA  . ALA   A 1 74  ? -2.978  60.277 62.506  1.00 32.18 ? 63  ALA   A CA  1 
ATOM   505  C  C   . ALA   A 1 74  ? -2.391  60.626 63.879  1.00 31.96 ? 63  ALA   A C   1 
ATOM   506  O  O   . ALA   A 1 74  ? -1.250  61.069 63.992  1.00 31.53 ? 63  ALA   A O   1 
ATOM   507  C  CB  . ALA   A 1 74  ? -3.957  61.362 62.049  1.00 31.99 ? 63  ALA   A CB  1 
ATOM   508  N  N   . CYS   A 1 75  ? -3.152  60.346 64.916  1.00 31.85 ? 64  CYS   A N   1 
ATOM   509  C  CA  . CYS   A 1 75  ? -2.749  60.582 66.276  1.00 33.33 ? 64  CYS   A CA  1 
ATOM   510  C  C   . CYS   A 1 75  ? -1.446  59.836 66.639  1.00 32.60 ? 64  CYS   A C   1 
ATOM   511  O  O   . CYS   A 1 75  ? -0.527  60.465 67.130  1.00 32.75 ? 64  CYS   A O   1 
ATOM   512  C  CB  . CYS   A 1 75  ? -3.894  60.204 67.201  1.00 36.21 ? 64  CYS   A CB  1 
ATOM   513  S  SG  . CYS   A 1 75  ? -3.576  60.562 68.924  1.00 46.62 ? 64  CYS   A SG  1 
ATOM   514  N  N   . ARG   A 1 76  ? -1.344  58.535 66.327  1.00 31.40 ? 65  ARG   A N   1 
ATOM   515  C  CA  . ARG   A 1 76  ? -0.157  57.726 66.603  1.00 31.25 ? 65  ARG   A CA  1 
ATOM   516  C  C   . ARG   A 1 76  ? 1.048   58.210 65.805  1.00 31.27 ? 65  ARG   A C   1 
ATOM   517  O  O   . ARG   A 1 76  ? 2.139   58.330 66.359  1.00 32.04 ? 65  ARG   A O   1 
ATOM   518  C  CB  . ARG   A 1 76  ? -0.428  56.243 66.276  1.00 32.38 ? 65  ARG   A CB  1 
ATOM   519  C  CG  . ARG   A 1 76  ? 0.725   55.332 66.669  1.00 34.26 ? 65  ARG   A CG  1 
ATOM   520  C  CD  . ARG   A 1 76  ? 0.482   53.881 66.314  1.00 35.77 ? 65  ARG   A CD  1 
ATOM   521  N  NE  . ARG   A 1 76  ? 1.386   53.005 67.061  1.00 35.85 ? 65  ARG   A NE  1 
ATOM   522  C  CZ  . ARG   A 1 76  ? 2.378   52.307 66.520  1.00 35.10 ? 65  ARG   A CZ  1 
ATOM   523  N  NH1 . ARG   A 1 76  ? 2.590   52.347 65.210  1.00 33.32 ? 65  ARG   A NH1 1 
ATOM   524  N  NH2 . ARG   A 1 76  ? 3.150   51.545 67.280  1.00 34.22 ? 65  ARG   A NH2 1 
ATOM   525  N  N   . GLU   A 1 77  ? 0.845   58.526 64.519  1.00 30.07 ? 66  GLU   A N   1 
ATOM   526  C  CA  . GLU   A 1 77  ? 1.899   59.010 63.641  1.00 29.99 ? 66  GLU   A CA  1 
ATOM   527  C  C   . GLU   A 1 77  ? 2.492   60.347 64.164  1.00 29.99 ? 66  GLU   A C   1 
ATOM   528  O  O   . GLU   A 1 77  ? 3.712   60.476 64.279  1.00 30.64 ? 66  GLU   A O   1 
ATOM   529  C  CB  . GLU   A 1 77  ? 1.324   59.138 62.221  1.00 32.49 ? 66  GLU   A CB  1 
ATOM   530  C  CG  . GLU   A 1 77  ? 2.191   59.852 61.207  1.00 37.05 ? 66  GLU   A CG  1 
ATOM   531  C  CD  . GLU   A 1 77  ? 3.199   58.994 60.472  1.00 42.55 ? 66  GLU   A CD  1 
ATOM   532  O  OE1 . GLU   A 1 77  ? 3.823   58.133 61.124  1.00 45.83 ? 66  GLU   A OE1 1 
ATOM   533  O  OE2 . GLU   A 1 77  ? 3.414   59.214 59.260  1.00 42.17 ? 66  GLU   A OE2 1 
ATOM   534  N  N   . ILE   A 1 78  ? 1.632   61.311 64.527  1.00 28.68 ? 67  ILE   A N   1 
ATOM   535  C  CA  . ILE   A 1 78  ? 2.059   62.593 65.086  1.00 27.94 ? 67  ILE   A CA  1 
ATOM   536  C  C   . ILE   A 1 78  ? 2.677   62.390 66.475  1.00 28.94 ? 67  ILE   A C   1 
ATOM   537  O  O   . ILE   A 1 78  ? 3.789   62.862 66.695  1.00 29.46 ? 67  ILE   A O   1 
ATOM   538  C  CB  . ILE   A 1 78  ? 0.858   63.570 65.153  1.00 27.38 ? 67  ILE   A CB  1 
ATOM   539  C  CG1 . ILE   A 1 78  ? 0.328   63.912 63.733  1.00 28.17 ? 67  ILE   A CG1 1 
ATOM   540  C  CG2 . ILE   A 1 78  ? 1.203   64.820 65.959  1.00 27.04 ? 67  ILE   A CG2 1 
ATOM   541  C  CD1 . ILE   A 1 78  ? -1.089  64.551 63.700  1.00 29.40 ? 67  ILE   A CD1 1 
ATOM   542  N  N   . ALA   A 1 79  ? 1.987   61.661 67.403  1.00 28.55 ? 68  ALA   A N   1 
ATOM   543  C  CA  . ALA   A 1 79  ? 2.502   61.449 68.759  1.00 29.02 ? 68  ALA   A CA  1 
ATOM   544  C  C   . ALA   A 1 79  ? 3.858   60.812 68.779  1.00 28.62 ? 68  ALA   A C   1 
ATOM   545  O  O   . ALA   A 1 79  ? 4.725   61.276 69.518  1.00 28.73 ? 68  ALA   A O   1 
ATOM   546  C  CB  . ALA   A 1 79  ? 1.527   60.640 69.630  1.00 29.40 ? 68  ALA   A CB  1 
ATOM   547  N  N   . LEU   A 1 80  ? 4.059   59.765 67.968  1.00 28.37 ? 69  LEU   A N   1 
ATOM   548  C  CA  . LEU   A 1 80  ? 5.333   59.049 67.919  1.00 28.28 ? 69  LEU   A CA  1 
ATOM   549  C  C   . LEU   A 1 80  ? 6.432   59.806 67.157  1.00 28.31 ? 69  LEU   A C   1 
ATOM   550  O  O   . LEU   A 1 80  ? 7.501   60.006 67.728  1.00 28.58 ? 69  LEU   A O   1 
ATOM   551  C  CB  . LEU   A 1 80  ? 5.158   57.626 67.382  1.00 28.19 ? 69  LEU   A CB  1 
ATOM   552  C  CG  . LEU   A 1 80  ? 4.304   56.686 68.267  1.00 30.16 ? 69  LEU   A CG  1 
ATOM   553  C  CD1 . LEU   A 1 80  ? 4.266   55.287 67.680  1.00 31.04 ? 69  LEU   A CD1 1 
ATOM   554  C  CD2 . LEU   A 1 80  ? 4.838   56.610 69.719  1.00 29.32 ? 69  LEU   A CD2 1 
ATOM   555  N  N   . LEU   A 1 81  ? 6.169   60.295 65.928  1.00 28.02 ? 70  LEU   A N   1 
ATOM   556  C  CA  . LEU   A 1 81  ? 7.216   61.024 65.178  1.00 29.01 ? 70  LEU   A CA  1 
ATOM   557  C  C   . LEU   A 1 81  ? 7.657   62.353 65.812  1.00 29.46 ? 70  LEU   A C   1 
ATOM   558  O  O   . LEU   A 1 81  ? 8.748   62.855 65.532  1.00 29.21 ? 70  LEU   A O   1 
ATOM   559  C  CB  . LEU   A 1 81  ? 6.835   61.241 63.709  1.00 28.81 ? 70  LEU   A CB  1 
ATOM   560  C  CG  . LEU   A 1 81  ? 6.772   59.971 62.865  1.00 29.62 ? 70  LEU   A CG  1 
ATOM   561  C  CD1 . LEU   A 1 81  ? 6.467   60.306 61.452  1.00 29.56 ? 70  LEU   A CD1 1 
ATOM   562  C  CD2 . LEU   A 1 81  ? 8.074   59.163 62.948  1.00 30.16 ? 70  LEU   A CD2 1 
ATOM   563  N  N   . ARG   A 1 82  ? 6.808   62.910 66.680  1.00 29.36 ? 71  ARG   A N   1 
ATOM   564  C  CA  . ARG   A 1 82  ? 7.104   64.106 67.436  1.00 28.96 ? 71  ARG   A CA  1 
ATOM   565  C  C   . ARG   A 1 82  ? 8.212   63.825 68.502  1.00 28.95 ? 71  ARG   A C   1 
ATOM   566  O  O   . ARG   A 1 82  ? 8.909   64.754 68.914  1.00 29.34 ? 71  ARG   A O   1 
ATOM   567  C  CB  . ARG   A 1 82  ? 5.804   64.563 68.108  1.00 30.54 ? 71  ARG   A CB  1 
ATOM   568  C  CG  . ARG   A 1 82  ? 5.841   65.930 68.729  1.00 33.33 ? 71  ARG   A CG  1 
ATOM   569  C  CD  . ARG   A 1 82  ? 6.235   67.003 67.725  1.00 35.68 ? 71  ARG   A CD  1 
ATOM   570  N  NE  . ARG   A 1 82  ? 6.440   68.283 68.393  1.00 37.05 ? 71  ARG   A NE  1 
ATOM   571  C  CZ  . ARG   A 1 82  ? 7.549   68.631 69.029  1.00 38.33 ? 71  ARG   A CZ  1 
ATOM   572  N  NH1 . ARG   A 1 82  ? 7.623   69.798 69.644  1.00 38.61 ? 71  ARG   A NH1 1 
ATOM   573  N  NH2 . ARG   A 1 82  ? 8.593   67.808 69.062  1.00 37.13 ? 71  ARG   A NH2 1 
ATOM   574  N  N   . GLU   A 1 83  ? 8.404   62.540 68.909  1.00 28.28 ? 72  GLU   A N   1 
ATOM   575  C  CA  . GLU   A 1 83  ? 9.398   62.127 69.902  1.00 28.17 ? 72  GLU   A CA  1 
ATOM   576  C  C   . GLU   A 1 83  ? 10.603  61.388 69.289  1.00 29.00 ? 72  GLU   A C   1 
ATOM   577  O  O   . GLU   A 1 83  ? 11.725  61.544 69.755  1.00 29.81 ? 72  GLU   A O   1 
ATOM   578  C  CB  . GLU   A 1 83  ? 8.747   61.180 70.927  1.00 27.78 ? 72  GLU   A CB  1 
ATOM   579  C  CG  . GLU   A 1 83  ? 7.428   61.672 71.479  1.00 29.30 ? 72  GLU   A CG  1 
ATOM   580  C  CD  . GLU   A 1 83  ? 7.550   62.941 72.303  1.00 31.23 ? 72  GLU   A CD  1 
ATOM   581  O  OE1 . GLU   A 1 83  ? 8.477   63.024 73.137  1.00 31.95 ? 72  GLU   A OE1 1 
ATOM   582  O  OE2 . GLU   A 1 83  ? 6.705   63.845 72.135  1.00 32.92 ? 72  GLU   A OE2 1 
ATOM   583  N  N   . LEU   A 1 84  ? 10.359  60.525 68.327  1.00 29.06 ? 73  LEU   A N   1 
ATOM   584  C  CA  . LEU   A 1 84  ? 11.392  59.686 67.731  1.00 29.74 ? 73  LEU   A CA  1 
ATOM   585  C  C   . LEU   A 1 84  ? 12.465  60.475 66.994  1.00 30.79 ? 73  LEU   A C   1 
ATOM   586  O  O   . LEU   A 1 84  ? 12.154  61.276 66.121  1.00 31.05 ? 73  LEU   A O   1 
ATOM   587  C  CB  . LEU   A 1 84  ? 10.750  58.652 66.785  1.00 29.48 ? 73  LEU   A CB  1 
ATOM   588  C  CG  . LEU   A 1 84  ? 9.774   57.668 67.447  1.00 30.90 ? 73  LEU   A CG  1 
ATOM   589  C  CD1 . LEU   A 1 84  ? 8.879   56.973 66.409  1.00 31.68 ? 73  LEU   A CD1 1 
ATOM   590  C  CD2 . LEU   A 1 84  ? 10.492  56.668 68.350  1.00 30.21 ? 73  LEU   A CD2 1 
ATOM   591  N  N   . LYS   A 1 85  ? 13.733  60.228 67.339  1.00 31.00 ? 74  LYS   A N   1 
ATOM   592  C  CA  . LYS   A 1 85  ? 14.863  60.837 66.663  1.00 31.49 ? 74  LYS   A CA  1 
ATOM   593  C  C   . LYS   A 1 85  ? 15.958  59.788 66.427  1.00 29.91 ? 74  LYS   A C   1 
ATOM   594  O  O   . LYS   A 1 85  ? 16.673  59.403 67.354  1.00 30.00 ? 74  LYS   A O   1 
ATOM   595  C  CB  . LYS   A 1 85  ? 15.396  62.030 67.453  1.00 35.89 ? 74  LYS   A CB  1 
ATOM   596  C  CG  . LYS   A 1 85  ? 16.368  62.871 66.650  1.00 43.79 ? 74  LYS   A CG  1 
ATOM   597  C  CD  . LYS   A 1 85  ? 17.134  63.858 67.526  1.00 51.27 ? 74  LYS   A CD  1 
ATOM   598  C  CE  . LYS   A 1 85  ? 18.032  64.751 66.699  1.00 57.02 ? 74  LYS   A CE  1 
ATOM   599  N  NZ  . LYS   A 1 85  ? 18.581  65.888 67.506  1.00 61.39 ? 74  LYS   A NZ  1 
ATOM   600  N  N   . HIS   A 1 86  ? 16.063  59.299 65.190  1.00 28.17 ? 75  HIS   A N   1 
ATOM   601  C  CA  . HIS   A 1 86  ? 17.062  58.302 64.812  1.00 27.26 ? 75  HIS   A CA  1 
ATOM   602  C  C   . HIS   A 1 86  ? 17.357  58.463 63.308  1.00 27.38 ? 75  HIS   A C   1 
ATOM   603  O  O   . HIS   A 1 86  ? 16.440  58.754 62.543  1.00 26.89 ? 75  HIS   A O   1 
ATOM   604  C  CB  . HIS   A 1 86  ? 16.545  56.868 65.107  1.00 26.56 ? 75  HIS   A CB  1 
ATOM   605  C  CG  . HIS   A 1 86  ? 17.598  55.808 64.947  1.00 27.36 ? 75  HIS   A CG  1 
ATOM   606  N  ND1 . HIS   A 1 86  ? 17.815  55.179 63.728  1.00 29.03 ? 75  HIS   A ND1 1 
ATOM   607  C  CD2 . HIS   A 1 86  ? 18.520  55.363 65.833  1.00 27.39 ? 75  HIS   A CD2 1 
ATOM   608  C  CE1 . HIS   A 1 86  ? 18.849  54.379 63.915  1.00 28.93 ? 75  HIS   A CE1 1 
ATOM   609  N  NE2 . HIS   A 1 86  ? 19.308  54.455 65.167  1.00 28.29 ? 75  HIS   A NE2 1 
ATOM   610  N  N   . PRO   A 1 87  ? 18.624  58.281 62.866  1.00 28.03 ? 76  PRO   A N   1 
ATOM   611  C  CA  . PRO   A 1 87  ? 18.944  58.461 61.435  1.00 27.99 ? 76  PRO   A CA  1 
ATOM   612  C  C   . PRO   A 1 87  ? 18.207  57.525 60.489  1.00 28.66 ? 76  PRO   A C   1 
ATOM   613  O  O   . PRO   A 1 87  ? 18.065  57.836 59.318  1.00 28.96 ? 76  PRO   A O   1 
ATOM   614  C  CB  . PRO   A 1 87  ? 20.453  58.182 61.369  1.00 28.78 ? 76  PRO   A CB  1 
ATOM   615  C  CG  . PRO   A 1 87  ? 20.970  58.432 62.778  1.00 29.24 ? 76  PRO   A CG  1 
ATOM   616  C  CD  . PRO   A 1 87  ? 19.839  57.972 63.659  1.00 27.87 ? 76  PRO   A CD  1 
ATOM   617  N  N   . ASN   A 1 88  ? 17.734  56.381 60.989  1.00 28.43 ? 77  ASN   A N   1 
ATOM   618  C  CA  . ASN   A 1 88  ? 17.031  55.427 60.153  1.00 27.77 ? 77  ASN   A CA  1 
ATOM   619  C  C   . ASN   A 1 88  ? 15.512  55.464 60.318  1.00 28.41 ? 77  ASN   A C   1 
ATOM   620  O  O   . ASN   A 1 88  ? 14.826  54.590 59.812  1.00 28.94 ? 77  ASN   A O   1 
ATOM   621  C  CB  . ASN   A 1 88  ? 17.599  54.033 60.343  1.00 26.70 ? 77  ASN   A CB  1 
ATOM   622  C  CG  . ASN   A 1 88  ? 19.044  53.970 59.885  1.00 25.86 ? 77  ASN   A CG  1 
ATOM   623  O  OD1 . ASN   A 1 88  ? 19.936  53.568 60.639  1.00 27.59 ? 77  ASN   A OD1 1 
ATOM   624  N  ND2 . ASN   A 1 88  ? 19.309  54.392 58.650  1.00 23.38 ? 77  ASN   A ND2 1 
ATOM   625  N  N   . VAL   A 1 89  ? 14.973  56.506 60.940  1.00 28.12 ? 78  VAL   A N   1 
ATOM   626  C  CA  . VAL   A 1 89  ? 13.533  56.681 61.064  1.00 28.08 ? 78  VAL   A CA  1 
ATOM   627  C  C   . VAL   A 1 89  ? 13.249  58.024 60.413  1.00 28.58 ? 78  VAL   A C   1 
ATOM   628  O  O   . VAL   A 1 89  ? 13.927  59.013 60.720  1.00 28.58 ? 78  VAL   A O   1 
ATOM   629  C  CB  . VAL   A 1 89  ? 13.076  56.635 62.555  1.00 28.20 ? 78  VAL   A CB  1 
ATOM   630  C  CG1 . VAL   A 1 89  ? 11.573  56.896 62.700  1.00 28.34 ? 78  VAL   A CG1 1 
ATOM   631  C  CG2 . VAL   A 1 89  ? 13.471  55.310 63.215  1.00 27.57 ? 78  VAL   A CG2 1 
ATOM   632  N  N   . ILE   A 1 90  ? 12.257  58.096 59.492  1.00 28.91 ? 79  ILE   A N   1 
ATOM   633  C  CA  . ILE   A 1 90  ? 11.885  59.358 58.838  1.00 29.36 ? 79  ILE   A CA  1 
ATOM   634  C  C   . ILE   A 1 90  ? 11.594  60.433 59.893  1.00 30.75 ? 79  ILE   A C   1 
ATOM   635  O  O   . ILE   A 1 90  ? 11.015  60.135 60.930  1.00 31.49 ? 79  ILE   A O   1 
ATOM   636  C  CB  . ILE   A 1 90  ? 10.713  59.165 57.837  1.00 29.58 ? 79  ILE   A CB  1 
ATOM   637  C  CG1 . ILE   A 1 90  ? 10.586  60.356 56.857  1.00 30.15 ? 79  ILE   A CG1 1 
ATOM   638  C  CG2 . ILE   A 1 90  ? 9.381   58.891 58.553  1.00 30.01 ? 79  ILE   A CG2 1 
ATOM   639  C  CD1 . ILE   A 1 90  ? 11.756  60.574 55.920  1.00 31.27 ? 79  ILE   A CD1 1 
ATOM   640  N  N   . SER   A 1 91  ? 12.149  61.614 59.711  1.00 31.46 ? 80  SER   A N   1 
ATOM   641  C  CA  . SER   A 1 91  ? 12.026  62.688 60.679  1.00 31.84 ? 80  SER   A CA  1 
ATOM   642  C  C   . SER   A 1 91  ? 10.896  63.646 60.343  1.00 32.13 ? 80  SER   A C   1 
ATOM   643  O  O   . SER   A 1 91  ? 10.837  64.159 59.226  1.00 31.65 ? 80  SER   A O   1 
ATOM   644  C  CB  . SER   A 1 91  ? 13.351  63.425 60.791  1.00 33.37 ? 80  SER   A CB  1 
ATOM   645  O  OG  . SER   A 1 91  ? 13.410  64.070 62.044  1.00 38.33 ? 80  SER   A OG  1 
ATOM   646  N  N   . LEU   A 1 92  ? 9.994   63.877 61.310  1.00 32.60 ? 81  LEU   A N   1 
ATOM   647  C  CA  . LEU   A 1 92  ? 8.869   64.805 61.165  1.00 33.48 ? 81  LEU   A CA  1 
ATOM   648  C  C   . LEU   A 1 92  ? 9.327   66.258 61.348  1.00 35.13 ? 81  LEU   A C   1 
ATOM   649  O  O   . LEU   A 1 92  ? 9.765   66.642 62.431  1.00 35.17 ? 81  LEU   A O   1 
ATOM   650  C  CB  . LEU   A 1 92  ? 7.769   64.467 62.172  1.00 32.78 ? 81  LEU   A CB  1 
ATOM   651  C  CG  . LEU   A 1 92  ? 6.553   65.373 62.182  1.00 33.15 ? 81  LEU   A CG  1 
ATOM   652  C  CD1 . LEU   A 1 92  ? 5.877   65.437 60.802  1.00 33.02 ? 81  LEU   A CD1 1 
ATOM   653  C  CD2 . LEU   A 1 92  ? 5.571   64.944 63.273  1.00 32.93 ? 81  LEU   A CD2 1 
ATOM   654  N  N   . GLN   A 1 93  ? 9.236   67.066 60.285  1.00 36.03 ? 82  GLN   A N   1 
ATOM   655  C  CA  . GLN   A 1 93  ? 9.645   68.461 60.351  1.00 37.09 ? 82  GLN   A CA  1 
ATOM   656  C  C   . GLN   A 1 93  ? 8.525   69.333 60.894  1.00 38.15 ? 82  GLN   A C   1 
ATOM   657  O  O   . GLN   A 1 93  ? 8.756   70.131 61.795  1.00 39.21 ? 82  GLN   A O   1 
ATOM   658  C  CB  . GLN   A 1 93  ? 10.042  69.001 58.966  1.00 38.77 ? 82  GLN   A CB  1 
ATOM   659  C  CG  . GLN   A 1 93  ? 10.664  67.997 58.035  1.00 43.74 ? 82  GLN   A CG  1 
ATOM   660  C  CD  . GLN   A 1 93  ? 12.136  68.163 58.044  1.00 49.69 ? 82  GLN   A CD  1 
ATOM   661  O  OE1 . GLN   A 1 93  ? 12.821  67.704 58.963  1.00 51.81 ? 82  GLN   A OE1 1 
ATOM   662  N  NE2 . GLN   A 1 93  ? 12.645  68.857 57.039  1.00 51.13 ? 82  GLN   A NE2 1 
ATOM   663  N  N   . LYS   A 1 94  ? 7.323   69.222 60.320  1.00 37.70 ? 83  LYS   A N   1 
ATOM   664  C  CA  . LYS   A 1 94  ? 6.230   70.113 60.651  1.00 37.96 ? 83  LYS   A CA  1 
ATOM   665  C  C   . LYS   A 1 94  ? 4.892   69.458 60.484  1.00 36.88 ? 83  LYS   A C   1 
ATOM   666  O  O   . LYS   A 1 94  ? 4.729   68.566 59.652  1.00 36.74 ? 83  LYS   A O   1 
ATOM   667  C  CB  . LYS   A 1 94  ? 6.264   71.335 59.704  1.00 41.73 ? 83  LYS   A CB  1 
ATOM   668  C  CG  . LYS   A 1 94  ? 7.012   72.552 60.234  1.00 49.08 ? 83  LYS   A CG  1 
ATOM   669  C  CD  . LYS   A 1 94  ? 6.933   73.731 59.255  1.00 55.69 ? 83  LYS   A CD  1 
ATOM   670  C  CE  . LYS   A 1 94  ? 7.601   74.968 59.823  1.00 61.22 ? 83  LYS   A CE  1 
ATOM   671  N  NZ  . LYS   A 1 94  ? 7.573   76.118 58.868  1.00 64.13 ? 83  LYS   A NZ  1 
ATOM   672  N  N   . VAL   A 1 95  ? 3.912   69.951 61.243  1.00 36.05 ? 84  VAL   A N   1 
ATOM   673  C  CA  . VAL   A 1 95  ? 2.528   69.532 61.158  1.00 36.31 ? 84  VAL   A CA  1 
ATOM   674  C  C   . VAL   A 1 95  ? 1.716   70.792 60.822  1.00 37.15 ? 84  VAL   A C   1 
ATOM   675  O  O   . VAL   A 1 95  ? 1.869   71.821 61.492  1.00 37.62 ? 84  VAL   A O   1 
ATOM   676  C  CB  . VAL   A 1 95  ? 2.022   68.912 62.477  1.00 36.44 ? 84  VAL   A CB  1 
ATOM   677  C  CG1 . VAL   A 1 95  ? 0.562   68.494 62.359  1.00 36.24 ? 84  VAL   A CG1 1 
ATOM   678  C  CG2 . VAL   A 1 95  ? 2.902   67.744 62.929  1.00 36.78 ? 84  VAL   A CG2 1 
ATOM   679  N  N   . PHE   A 1 96  ? 0.868   70.714 59.798  1.00 37.06 ? 85  PHE   A N   1 
ATOM   680  C  CA  . PHE   A 1 96  ? -0.015  71.803 59.401  1.00 38.32 ? 85  PHE   A CA  1 
ATOM   681  C  C   . PHE   A 1 96  ? -1.428  71.310 59.612  1.00 39.96 ? 85  PHE   A C   1 
ATOM   682  O  O   . PHE   A 1 96  ? -1.775  70.227 59.137  1.00 40.01 ? 85  PHE   A O   1 
ATOM   683  C  CB  . PHE   A 1 96  ? 0.151   72.129 57.917  1.00 38.40 ? 85  PHE   A CB  1 
ATOM   684  C  CG  . PHE   A 1 96  ? 1.543   72.534 57.511  1.00 39.22 ? 85  PHE   A CG  1 
ATOM   685  C  CD1 . PHE   A 1 96  ? 1.965   73.839 57.642  1.00 40.36 ? 85  PHE   A CD1 1 
ATOM   686  C  CD2 . PHE   A 1 96  ? 2.399   71.625 56.922  1.00 40.32 ? 85  PHE   A CD2 1 
ATOM   687  C  CE1 . PHE   A 1 96  ? 3.233   74.221 57.225  1.00 41.36 ? 85  PHE   A CE1 1 
ATOM   688  C  CE2 . PHE   A 1 96  ? 3.670   72.007 56.512  1.00 41.38 ? 85  PHE   A CE2 1 
ATOM   689  C  CZ  . PHE   A 1 96  ? 4.073   73.306 56.648  1.00 41.19 ? 85  PHE   A CZ  1 
ATOM   690  N  N   . LEU   A 1 97  ? -2.242  72.074 60.351  1.00 40.90 ? 86  LEU   A N   1 
ATOM   691  C  CA  . LEU   A 1 97  ? -3.618  71.684 60.608  1.00 41.85 ? 86  LEU   A CA  1 
ATOM   692  C  C   . LEU   A 1 97  ? -4.506  72.619 59.843  1.00 42.49 ? 86  LEU   A C   1 
ATOM   693  O  O   . LEU   A 1 97  ? -4.607  73.790 60.199  1.00 42.99 ? 86  LEU   A O   1 
ATOM   694  C  CB  . LEU   A 1 97  ? -3.948  71.757 62.107  1.00 42.25 ? 86  LEU   A CB  1 
ATOM   695  C  CG  . LEU   A 1 97  ? -3.147  70.856 63.053  1.00 43.77 ? 86  LEU   A CG  1 
ATOM   696  C  CD1 . LEU   A 1 97  ? -3.799  70.814 64.395  1.00 44.70 ? 86  LEU   A CD1 1 
ATOM   697  C  CD2 . LEU   A 1 97  ? -3.049  69.429 62.539  1.00 43.92 ? 86  LEU   A CD2 1 
ATOM   698  N  N   . SER   A 1 98  ? -5.099  72.126 58.758  1.00 42.22 ? 87  SER   A N   1 
ATOM   699  C  CA  . SER   A 1 98  ? -5.964  72.912 57.899  1.00 42.54 ? 87  SER   A CA  1 
ATOM   700  C  C   . SER   A 1 98  ? -7.354  72.955 58.524  1.00 42.86 ? 87  SER   A C   1 
ATOM   701  O  O   . SER   A 1 98  ? -8.085  71.971 58.470  1.00 42.35 ? 87  SER   A O   1 
ATOM   702  C  CB  . SER   A 1 98  ? -6.014  72.276 56.519  1.00 43.90 ? 87  SER   A CB  1 
ATOM   703  O  OG  . SER   A 1 98  ? -6.815  73.078 55.673  1.00 46.78 ? 87  SER   A OG  1 
ATOM   704  N  N   . HIS   A 1 99  ? -7.714  74.086 59.141  1.00 43.62 ? 88  HIS   A N   1 
ATOM   705  C  CA  . HIS   A 1 99  ? -8.967  74.188 59.883  1.00 44.64 ? 88  HIS   A CA  1 
ATOM   706  C  C   . HIS   A 1 99  ? -10.245 74.091 59.030  1.00 46.14 ? 88  HIS   A C   1 
ATOM   707  O  O   . HIS   A 1 99  ? -11.185 73.425 59.472  1.00 47.13 ? 88  HIS   A O   1 
ATOM   708  C  CB  . HIS   A 1 99  ? -8.981  75.450 60.756  1.00 44.97 ? 88  HIS   A CB  1 
ATOM   709  C  CG  . HIS   A 1 99  ? -8.099  75.353 61.974  1.00 45.95 ? 88  HIS   A CG  1 
ATOM   710  N  ND1 . HIS   A 1 99  ? -8.607  75.510 63.246  1.00 47.41 ? 88  HIS   A ND1 1 
ATOM   711  C  CD2 . HIS   A 1 99  ? -6.770  75.107 62.068  1.00 46.45 ? 88  HIS   A CD2 1 
ATOM   712  C  CE1 . HIS   A 1 99  ? -7.578  75.377 64.068  1.00 47.53 ? 88  HIS   A CE1 1 
ATOM   713  N  NE2 . HIS   A 1 99  ? -6.453  75.140 63.405  1.00 47.26 ? 88  HIS   A NE2 1 
ATOM   714  N  N   . ALA   A 1 100 ? -10.294 74.704 57.826  1.00 45.95 ? 89  ALA   A N   1 
ATOM   715  C  CA  . ALA   A 1 100 ? -11.507 74.635 57.007  1.00 46.71 ? 89  ALA   A CA  1 
ATOM   716  C  C   . ALA   A 1 100 ? -11.936 73.209 56.615  1.00 47.26 ? 89  ALA   A C   1 
ATOM   717  O  O   . ALA   A 1 100 ? -13.107 72.854 56.796  1.00 48.30 ? 89  ALA   A O   1 
ATOM   718  C  CB  . ALA   A 1 100 ? -11.376 75.509 55.771  1.00 46.95 ? 89  ALA   A CB  1 
ATOM   719  N  N   . ASP   A 1 101 ? -11.009 72.388 56.102  1.00 46.08 ? 90  ASP   A N   1 
ATOM   720  C  CA  . ASP   A 1 101 ? -11.354 71.022 55.711  1.00 45.46 ? 90  ASP   A CA  1 
ATOM   721  C  C   . ASP   A 1 101 ? -10.983 69.952 56.741  1.00 45.23 ? 90  ASP   A C   1 
ATOM   722  O  O   . ASP   A 1 101 ? -11.193 68.764 56.470  1.00 45.83 ? 90  ASP   A O   1 
ATOM   723  C  CB  . ASP   A 1 101 ? -10.751 70.680 54.336  1.00 46.23 ? 90  ASP   A CB  1 
ATOM   724  C  CG  . ASP   A 1 101 ? -9.263  70.933 54.212  1.00 49.04 ? 90  ASP   A CG  1 
ATOM   725  O  OD1 . ASP   A 1 101 ? -8.640  71.302 55.215  1.00 48.18 ? 90  ASP   A OD1 1 
ATOM   726  O  OD2 . ASP   A 1 101 ? -8.721  70.752 53.104  1.00 52.08 ? 90  ASP   A OD2 1 
ATOM   727  N  N   . ARG   A 1 102 ? -10.424 70.360 57.901  1.00 44.22 ? 91  ARG   A N   1 
ATOM   728  C  CA  . ARG   A 1 102 ? -9.985  69.459 58.966  1.00 43.85 ? 91  ARG   A CA  1 
ATOM   729  C  C   . ARG   A 1 102 ? -8.973  68.429 58.460  1.00 42.68 ? 91  ARG   A C   1 
ATOM   730  O  O   . ARG   A 1 102 ? -9.067  67.256 58.792  1.00 42.32 ? 91  ARG   A O   1 
ATOM   731  C  CB  . ARG   A 1 102 ? -11.166 68.808 59.699  1.00 45.57 ? 91  ARG   A CB  1 
ATOM   732  C  CG  . ARG   A 1 102 ? -11.977 69.799 60.530  1.00 48.97 ? 91  ARG   A CG  1 
ATOM   733  C  CD  . ARG   A 1 102 ? -12.698 69.140 61.705  1.00 51.19 ? 91  ARG   A CD  1 
ATOM   734  N  NE  . ARG   A 1 102 ? -11.833 69.009 62.880  1.00 53.11 ? 91  ARG   A NE  1 
ATOM   735  C  CZ  . ARG   A 1 102 ? -11.644 67.871 63.545  1.00 55.39 ? 91  ARG   A CZ  1 
ATOM   736  N  NH1 . ARG   A 1 102 ? -10.844 67.837 64.610  1.00 53.43 ? 91  ARG   A NH1 1 
ATOM   737  N  NH2 . ARG   A 1 102 ? -12.266 66.762 63.164  1.00 55.86 ? 91  ARG   A NH2 1 
ATOM   738  N  N   . LYS   A 1 103 ? -8.012  68.865 57.632  1.00 41.69 ? 92  LYS   A N   1 
ATOM   739  C  CA  . LYS   A 1 103 ? -7.004  67.952 57.088  1.00 40.83 ? 92  LYS   A CA  1 
ATOM   740  C  C   . LYS   A 1 103 ? -5.677  68.144 57.789  1.00 39.08 ? 92  LYS   A C   1 
ATOM   741  O  O   . LYS   A 1 103 ? -5.346  69.261 58.152  1.00 39.17 ? 92  LYS   A O   1 
ATOM   742  C  CB  . LYS   A 1 103 ? -6.870  68.114 55.564  1.00 42.68 ? 92  LYS   A CB  1 
ATOM   743  C  CG  . LYS   A 1 103 ? -8.068  67.569 54.808  1.00 48.37 ? 92  LYS   A CG  1 
ATOM   744  C  CD  . LYS   A 1 103 ? -8.095  66.051 54.861  1.00 55.01 ? 92  LYS   A CD  1 
ATOM   745  C  CE  . LYS   A 1 103 ? -9.264  65.405 54.150  1.00 60.02 ? 92  LYS   A CE  1 
ATOM   746  N  NZ  . LYS   A 1 103 ? -9.225  63.911 54.287  1.00 62.87 ? 92  LYS   A NZ  1 
ATOM   747  N  N   . VAL   A 1 104 ? -4.935  67.060 58.021  1.00 37.82 ? 93  VAL   A N   1 
ATOM   748  C  CA  . VAL   A 1 104 ? -3.643  67.147 58.686  1.00 36.97 ? 93  VAL   A CA  1 
ATOM   749  C  C   . VAL   A 1 104 ? -2.534  66.863 57.696  1.00 35.84 ? 93  VAL   A C   1 
ATOM   750  O  O   . VAL   A 1 104 ? -2.559  65.845 57.008  1.00 35.72 ? 93  VAL   A O   1 
ATOM   751  C  CB  . VAL   A 1 104 ? -3.540  66.217 59.921  1.00 37.97 ? 93  VAL   A CB  1 
ATOM   752  C  CG1 . VAL   A 1 104 ? -2.196  66.398 60.619  1.00 38.66 ? 93  VAL   A CG1 1 
ATOM   753  C  CG2 . VAL   A 1 104 ? -4.686  66.473 60.894  1.00 38.33 ? 93  VAL   A CG2 1 
ATOM   754  N  N   . TRP   A 1 105 ? -1.561  67.765 57.615  1.00 34.86 ? 94  TRP   A N   1 
ATOM   755  C  CA  . TRP   A 1 105 ? -0.432  67.590 56.721  1.00 34.18 ? 94  TRP   A CA  1 
ATOM   756  C  C   . TRP   A 1 105 ? 0.841   67.410 57.527  1.00 33.71 ? 94  TRP   A C   1 
ATOM   757  O  O   . TRP   A 1 105 ? 1.035   68.103 58.526  1.00 33.92 ? 94  TRP   A O   1 
ATOM   758  C  CB  . TRP   A 1 105 ? -0.285  68.784 55.776  1.00 33.56 ? 94  TRP   A CB  1 
ATOM   759  C  CG  . TRP   A 1 105 ? -1.442  68.952 54.850  1.00 33.58 ? 94  TRP   A CG  1 
ATOM   760  C  CD1 . TRP   A 1 105 ? -2.680  69.441 55.157  1.00 34.26 ? 94  TRP   A CD1 1 
ATOM   761  C  CD2 . TRP   A 1 105 ? -1.466  68.639 53.449  1.00 33.76 ? 94  TRP   A CD2 1 
ATOM   762  N  NE1 . TRP   A 1 105 ? -3.472  69.455 54.032  1.00 34.89 ? 94  TRP   A NE1 1 
ATOM   763  C  CE2 . TRP   A 1 105 ? -2.752  68.966 52.968  1.00 34.41 ? 94  TRP   A CE2 1 
ATOM   764  C  CE3 . TRP   A 1 105 ? -0.529  68.093 52.557  1.00 34.10 ? 94  TRP   A CE3 1 
ATOM   765  C  CZ2 . TRP   A 1 105 ? -3.109  68.807 51.629  1.00 34.72 ? 94  TRP   A CZ2 1 
ATOM   766  C  CZ3 . TRP   A 1 105 ? -0.903  67.898 51.236  1.00 34.70 ? 94  TRP   A CZ3 1 
ATOM   767  C  CH2 . TRP   A 1 105 ? -2.176  68.250 50.786  1.00 34.68 ? 94  TRP   A CH2 1 
ATOM   768  N  N   . LEU   A 1 106 ? 1.708   66.476 57.093  1.00 32.33 ? 95  LEU   A N   1 
ATOM   769  C  CA  . LEU   A 1 106 ? 2.978   66.222 57.745  1.00 31.38 ? 95  LEU   A CA  1 
ATOM   770  C  C   . LEU   A 1 106 ? 4.116   66.464 56.753  1.00 31.54 ? 95  LEU   A C   1 
ATOM   771  O  O   . LEU   A 1 106 ? 4.020   66.099 55.575  1.00 32.11 ? 95  LEU   A O   1 
ATOM   772  C  CB  . LEU   A 1 106 ? 3.042   64.802 58.272  1.00 31.07 ? 95  LEU   A CB  1 
ATOM   773  C  CG  . LEU   A 1 106 ? 1.897   64.306 59.160  1.00 31.12 ? 95  LEU   A CG  1 
ATOM   774  C  CD1 . LEU   A 1 106 ? 2.245   62.968 59.701  1.00 30.53 ? 95  LEU   A CD1 1 
ATOM   775  C  CD2 . LEU   A 1 106 ? 1.627   65.250 60.336  1.00 31.65 ? 95  LEU   A CD2 1 
ATOM   776  N  N   . LEU   A 1 107 ? 5.176   67.112 57.214  1.00 30.47 ? 96  LEU   A N   1 
ATOM   777  C  CA  . LEU   A 1 107 ? 6.301   67.444 56.360  1.00 30.06 ? 96  LEU   A CA  1 
ATOM   778  C  C   . LEU   A 1 107 ? 7.492   66.625 56.794  1.00 30.19 ? 96  LEU   A C   1 
ATOM   779  O  O   . LEU   A 1 107 ? 7.711   66.422 57.988  1.00 30.68 ? 96  LEU   A O   1 
ATOM   780  C  CB  . LEU   A 1 107 ? 6.605   68.950 56.442  1.00 29.52 ? 96  LEU   A CB  1 
ATOM   781  C  CG  . LEU   A 1 107 ? 7.786   69.494 55.622  1.00 29.86 ? 96  LEU   A CG  1 
ATOM   782  C  CD1 . LEU   A 1 107 ? 7.445   69.543 54.154  1.00 29.90 ? 96  LEU   A CD1 1 
ATOM   783  C  CD2 . LEU   A 1 107 ? 8.193   70.884 56.116  1.00 29.55 ? 96  LEU   A CD2 1 
ATOM   784  N  N   . PHE   A 1 108 ? 8.224   66.104 55.803  1.00 29.10 ? 97  PHE   A N   1 
ATOM   785  C  CA  . PHE   A 1 108 ? 9.425   65.301 55.965  1.00 28.54 ? 97  PHE   A CA  1 
ATOM   786  C  C   . PHE   A 1 108 ? 10.396  65.693 54.838  1.00 29.86 ? 97  PHE   A C   1 
ATOM   787  O  O   . PHE   A 1 108 ? 9.997   66.304 53.857  1.00 29.01 ? 97  PHE   A O   1 
ATOM   788  C  CB  . PHE   A 1 108 ? 9.088   63.800 55.743  1.00 27.05 ? 97  PHE   A CB  1 
ATOM   789  C  CG  . PHE   A 1 108 ? 7.922   63.242 56.528  1.00 26.88 ? 97  PHE   A CG  1 
ATOM   790  C  CD1 . PHE   A 1 108 ? 8.101   62.747 57.806  1.00 26.96 ? 97  PHE   A CD1 1 
ATOM   791  C  CD2 . PHE   A 1 108 ? 6.641   63.245 55.997  1.00 26.94 ? 97  PHE   A CD2 1 
ATOM   792  C  CE1 . PHE   A 1 108 ? 7.038   62.219 58.515  1.00 27.09 ? 97  PHE   A CE1 1 
ATOM   793  C  CE2 . PHE   A 1 108 ? 5.573   62.755 56.730  1.00 27.04 ? 97  PHE   A CE2 1 
ATOM   794  C  CZ  . PHE   A 1 108 ? 5.784   62.226 57.973  1.00 26.69 ? 97  PHE   A CZ  1 
ATOM   795  N  N   . ASP   A 1 109 ? 11.633  65.191 54.910  1.00 30.78 ? 98  ASP   A N   1 
ATOM   796  C  CA  . ASP   A 1 109 ? 12.558  65.268 53.803  1.00 31.34 ? 98  ASP   A CA  1 
ATOM   797  C  C   . ASP   A 1 109 ? 12.032  64.269 52.744  1.00 30.87 ? 98  ASP   A C   1 
ATOM   798  O  O   . ASP   A 1 109 ? 11.363  63.289 53.089  1.00 30.94 ? 98  ASP   A O   1 
ATOM   799  C  CB  . ASP   A 1 109 ? 13.961  64.840 54.272  1.00 34.17 ? 98  ASP   A CB  1 
ATOM   800  C  CG  . ASP   A 1 109 ? 14.723  65.947 54.974  1.00 41.23 ? 98  ASP   A CG  1 
ATOM   801  O  OD1 . ASP   A 1 109 ? 14.411  67.135 54.727  1.00 42.38 ? 98  ASP   A OD1 1 
ATOM   802  O  OD2 . ASP   A 1 109 ? 15.634  65.630 55.757  1.00 44.80 ? 98  ASP   A OD2 1 
ATOM   803  N  N   . TYR   A 1 110 ? 12.340  64.504 51.480  1.00 30.79 ? 99  TYR   A N   1 
ATOM   804  C  CA  . TYR   A 1 110 ? 11.894  63.623 50.414  1.00 31.38 ? 99  TYR   A CA  1 
ATOM   805  C  C   . TYR   A 1 110 ? 12.914  62.550 50.166  1.00 31.67 ? 99  TYR   A C   1 
ATOM   806  O  O   . TYR   A 1 110 ? 14.043  62.867 49.810  1.00 33.16 ? 99  TYR   A O   1 
ATOM   807  C  CB  . TYR   A 1 110 ? 11.710  64.415 49.127  1.00 31.87 ? 99  TYR   A CB  1 
ATOM   808  C  CG  . TYR   A 1 110 ? 11.156  63.605 47.986  1.00 32.97 ? 99  TYR   A CG  1 
ATOM   809  C  CD1 . TYR   A 1 110 ? 9.861   63.108 48.026  1.00 33.83 ? 99  TYR   A CD1 1 
ATOM   810  C  CD2 . TYR   A 1 110 ? 11.908  63.371 46.845  1.00 34.31 ? 99  TYR   A CD2 1 
ATOM   811  C  CE1 . TYR   A 1 110 ? 9.332   62.391 46.965  1.00 34.87 ? 99  TYR   A CE1 1 
ATOM   812  C  CE2 . TYR   A 1 110 ? 11.395  62.642 45.782  1.00 35.32 ? 99  TYR   A CE2 1 
ATOM   813  C  CZ  . TYR   A 1 110 ? 10.101  62.161 45.844  1.00 36.54 ? 99  TYR   A CZ  1 
ATOM   814  O  OH  . TYR   A 1 110 ? 9.584   61.443 44.795  1.00 39.83 ? 99  TYR   A OH  1 
ATOM   815  N  N   . ALA   A 1 111 ? 12.508  61.284 50.261  1.00 30.28 ? 100 ALA   A N   1 
ATOM   816  C  CA  . ALA   A 1 111 ? 13.361  60.164 49.962  1.00 30.01 ? 100 ALA   A CA  1 
ATOM   817  C  C   . ALA   A 1 111 ? 12.976  59.756 48.555  1.00 30.49 ? 100 ALA   A C   1 
ATOM   818  O  O   . ALA   A 1 111 ? 11.843  59.351 48.326  1.00 30.71 ? 100 ALA   A O   1 
ATOM   819  C  CB  . ALA   A 1 111 ? 13.089  59.023 50.931  1.00 29.72 ? 100 ALA   A CB  1 
ATOM   820  N  N   . GLU   A 1 112 ? 13.895  59.896 47.607  1.00 30.70 ? 101 GLU   A N   1 
ATOM   821  C  CA  . GLU   A 1 112 ? 13.658  59.557 46.206  1.00 31.73 ? 101 GLU   A CA  1 
ATOM   822  C  C   . GLU   A 1 112 ? 13.353  58.066 46.031  1.00 32.05 ? 101 GLU   A C   1 
ATOM   823  O  O   . GLU   A 1 112 ? 12.603  57.690 45.138  1.00 31.40 ? 101 GLU   A O   1 
ATOM   824  C  CB  . GLU   A 1 112 ? 14.900  59.935 45.386  1.00 35.40 ? 101 GLU   A CB  1 
ATOM   825  C  CG  . GLU   A 1 112 ? 14.687  59.914 43.885  1.00 43.20 ? 101 GLU   A CG  1 
ATOM   826  C  CD  . GLU   A 1 112 ? 13.726  60.994 43.439  1.00 53.01 ? 101 GLU   A CD  1 
ATOM   827  O  OE1 . GLU   A 1 112 ? 14.066  62.191 43.596  1.00 54.03 ? 101 GLU   A OE1 1 
ATOM   828  O  OE2 . GLU   A 1 112 ? 12.618  60.645 42.968  1.00 56.57 ? 101 GLU   A OE2 1 
ATOM   829  N  N   . HIS   A 1 113 ? 13.900  57.216 46.916  1.00 32.34 ? 102 HIS   A N   1 
ATOM   830  C  CA  . HIS   A 1 113 ? 13.748  55.786 46.780  1.00 32.75 ? 102 HIS   A CA  1 
ATOM   831  C  C   . HIS   A 1 113 ? 13.003  55.105 47.906  1.00 32.93 ? 102 HIS   A C   1 
ATOM   832  O  O   . HIS   A 1 113 ? 12.853  55.651 48.981  1.00 33.69 ? 102 HIS   A O   1 
ATOM   833  C  CB  . HIS   A 1 113 ? 15.150  55.162 46.611  1.00 33.66 ? 102 HIS   A CB  1 
ATOM   834  C  CG  . HIS   A 1 113 ? 15.926  55.812 45.523  1.00 36.05 ? 102 HIS   A CG  1 
ATOM   835  N  ND1 . HIS   A 1 113 ? 15.489  55.763 44.218  1.00 38.39 ? 102 HIS   A ND1 1 
ATOM   836  C  CD2 . HIS   A 1 113 ? 17.019  56.599 45.593  1.00 37.68 ? 102 HIS   A CD2 1 
ATOM   837  C  CE1 . HIS   A 1 113 ? 16.344  56.495 43.523  1.00 39.30 ? 102 HIS   A CE1 1 
ATOM   838  N  NE2 . HIS   A 1 113 ? 17.291  57.010 44.304  1.00 39.39 ? 102 HIS   A NE2 1 
ATOM   839  N  N   . ASP   A 1 114 ? 12.545  53.900 47.661  1.00 32.42 ? 103 ASP   A N   1 
ATOM   840  C  CA  . ASP   A 1 114 ? 11.985  53.023 48.677  1.00 32.34 ? 103 ASP   A CA  1 
ATOM   841  C  C   . ASP   A 1 114 ? 12.283  51.610 48.211  1.00 32.51 ? 103 ASP   A C   1 
ATOM   842  O  O   . ASP   A 1 114 ? 12.577  51.392 47.015  1.00 33.14 ? 103 ASP   A O   1 
ATOM   843  C  CB  . ASP   A 1 114 ? 10.494  53.258 48.969  1.00 32.79 ? 103 ASP   A CB  1 
ATOM   844  C  CG  . ASP   A 1 114 ? 9.628   53.191 47.745  1.00 35.38 ? 103 ASP   A CG  1 
ATOM   845  O  OD1 . ASP   A 1 114 ? 9.546   52.114 47.137  1.00 34.93 ? 103 ASP   A OD1 1 
ATOM   846  O  OD2 . ASP   A 1 114 ? 9.037   54.214 47.390  1.00 38.07 ? 103 ASP   A OD2 1 
ATOM   847  N  N   . LEU   A 1 115 ? 12.187  50.641 49.130  1.00 31.31 ? 104 LEU   A N   1 
ATOM   848  C  CA  . LEU   A 1 115 ? 12.498  49.264 48.794  1.00 30.66 ? 104 LEU   A CA  1 
ATOM   849  C  C   . LEU   A 1 115 ? 11.513  48.628 47.827  1.00 30.97 ? 104 LEU   A C   1 
ATOM   850  O  O   . LEU   A 1 115 ? 11.917  47.757 47.070  1.00 30.39 ? 104 LEU   A O   1 
ATOM   851  C  CB  . LEU   A 1 115 ? 12.689  48.414 50.055  1.00 30.25 ? 104 LEU   A CB  1 
ATOM   852  C  CG  . LEU   A 1 115 ? 14.139  48.065 50.440  1.00 31.16 ? 104 LEU   A CG  1 
ATOM   853  C  CD1 . LEU   A 1 115 ? 15.051  49.250 50.382  1.00 31.31 ? 104 LEU   A CD1 1 
ATOM   854  C  CD2 . LEU   A 1 115 ? 14.217  47.432 51.834  1.00 31.42 ? 104 LEU   A CD2 1 
ATOM   855  N  N   . TRP   A 1 116 ? 10.255  49.093 47.779  1.00 31.75 ? 105 TRP   A N   1 
ATOM   856  C  CA  . TRP   A 1 116 ? 9.284   48.550 46.823  1.00 32.90 ? 105 TRP   A CA  1 
ATOM   857  C  C   . TRP   A 1 116 ? 9.761   48.844 45.389  1.00 32.85 ? 105 TRP   A C   1 
ATOM   858  O  O   . TRP   A 1 116 ? 9.750   47.952 44.564  1.00 33.20 ? 105 TRP   A O   1 
ATOM   859  C  CB  . TRP   A 1 116 ? 7.883   49.139 47.049  1.00 33.68 ? 105 TRP   A CB  1 
ATOM   860  C  CG  . TRP   A 1 116 ? 6.812   48.487 46.221  1.00 35.70 ? 105 TRP   A CG  1 
ATOM   861  C  CD1 . TRP   A 1 116 ? 6.007   47.452 46.596  1.00 36.85 ? 105 TRP   A CD1 1 
ATOM   862  C  CD2 . TRP   A 1 116 ? 6.417   48.839 44.879  1.00 36.44 ? 105 TRP   A CD2 1 
ATOM   863  N  NE1 . TRP   A 1 116 ? 5.143   47.130 45.570  1.00 37.30 ? 105 TRP   A NE1 1 
ATOM   864  C  CE2 . TRP   A 1 116 ? 5.383   47.959 44.503  1.00 37.15 ? 105 TRP   A CE2 1 
ATOM   865  C  CE3 . TRP   A 1 116 ? 6.849   49.800 43.958  1.00 37.68 ? 105 TRP   A CE3 1 
ATOM   866  C  CZ2 . TRP   A 1 116 ? 4.760   48.025 43.255  1.00 38.38 ? 105 TRP   A CZ2 1 
ATOM   867  C  CZ3 . TRP   A 1 116 ? 6.262   49.834 42.703  1.00 39.14 ? 105 TRP   A CZ3 1 
ATOM   868  C  CH2 . TRP   A 1 116 ? 5.208   48.975 42.374  1.00 38.94 ? 105 TRP   A CH2 1 
ATOM   869  N  N   . HIS   A 1 117 ? 10.229  50.067 45.119  1.00 32.71 ? 106 HIS   A N   1 
ATOM   870  C  CA  . HIS   A 1 117 ? 10.695  50.454 43.785  1.00 32.94 ? 106 HIS   A CA  1 
ATOM   871  C  C   . HIS   A 1 117 ? 12.034  49.855 43.445  1.00 33.43 ? 106 HIS   A C   1 
ATOM   872  O  O   . HIS   A 1 117 ? 12.231  49.456 42.301  1.00 33.78 ? 106 HIS   A O   1 
ATOM   873  C  CB  . HIS   A 1 117 ? 10.781  51.972 43.639  1.00 32.67 ? 106 HIS   A CB  1 
ATOM   874  C  CG  . HIS   A 1 117 ? 9.448   52.628 43.585  1.00 35.38 ? 106 HIS   A CG  1 
ATOM   875  N  ND1 . HIS   A 1 117 ? 8.814   53.049 44.736  1.00 37.02 ? 106 HIS   A ND1 1 
ATOM   876  C  CD2 . HIS   A 1 117 ? 8.650   52.887 42.520  1.00 36.39 ? 106 HIS   A CD2 1 
ATOM   877  C  CE1 . HIS   A 1 117 ? 7.655   53.533 44.342  1.00 37.71 ? 106 HIS   A CE1 1 
ATOM   878  N  NE2 . HIS   A 1 117 ? 7.508   53.459 43.015  1.00 37.46 ? 106 HIS   A NE2 1 
ATOM   879  N  N   . ILE   A 1 118 ? 12.979  49.837 44.405  1.00 32.95 ? 107 ILE   A N   1 
ATOM   880  C  CA  . ILE   A 1 118 ? 14.313  49.268 44.191  1.00 32.91 ? 107 ILE   A CA  1 
ATOM   881  C  C   . ILE   A 1 118 ? 14.168  47.776 43.874  1.00 33.50 ? 107 ILE   A C   1 
ATOM   882  O  O   . ILE   A 1 118 ? 14.708  47.306 42.880  1.00 33.48 ? 107 ILE   A O   1 
ATOM   883  C  CB  . ILE   A 1 118 ? 15.193  49.517 45.452  1.00 32.94 ? 107 ILE   A CB  1 
ATOM   884  C  CG1 . ILE   A 1 118 ? 15.623  51.004 45.538  1.00 33.54 ? 107 ILE   A CG1 1 
ATOM   885  C  CG2 . ILE   A 1 118 ? 16.387  48.532 45.556  1.00 32.54 ? 107 ILE   A CG2 1 
ATOM   886  C  CD1 . ILE   A 1 118 ? 16.331  51.401 46.872  1.00 33.94 ? 107 ILE   A CD1 1 
ATOM   887  N  N   . ILE   A 1 119 ? 13.364  47.056 44.669  1.00 34.18 ? 108 ILE   A N   1 
ATOM   888  C  CA  . ILE   A 1 119 ? 13.144  45.635 44.441  1.00 35.26 ? 108 ILE   A CA  1 
ATOM   889  C  C   . ILE   A 1 119 ? 12.438  45.415 43.103  1.00 36.97 ? 108 ILE   A C   1 
ATOM   890  O  O   . ILE   A 1 119 ? 12.843  44.535 42.351  1.00 37.31 ? 108 ILE   A O   1 
ATOM   891  C  CB  . ILE   A 1 119 ? 12.418  44.956 45.624  1.00 34.80 ? 108 ILE   A CB  1 
ATOM   892  C  CG1 . ILE   A 1 119 ? 13.333  44.875 46.859  1.00 34.65 ? 108 ILE   A CG1 1 
ATOM   893  C  CG2 . ILE   A 1 119 ? 11.881  43.567 45.232  1.00 35.06 ? 108 ILE   A CG2 1 
ATOM   894  C  CD1 . ILE   A 1 119 ? 12.587  44.564 48.182  1.00 34.75 ? 108 ILE   A CD1 1 
ATOM   895  N  N   . LYS   A 1 120 ? 11.411  46.224 42.791  1.00 37.72 ? 109 LYS   A N   1 
ATOM   896  C  CA  . LYS   A 1 120 ? 10.703  46.120 41.519  1.00 39.58 ? 109 LYS   A CA  1 
ATOM   897  C  C   . LYS   A 1 120 ? 11.648  46.328 40.337  1.00 39.90 ? 109 LYS   A C   1 
ATOM   898  O  O   . LYS   A 1 120 ? 11.507  45.644 39.341  1.00 40.03 ? 109 LYS   A O   1 
ATOM   899  C  CB  . LYS   A 1 120 ? 9.540   47.114 41.443  1.00 43.51 ? 109 LYS   A CB  1 
ATOM   900  C  CG  . LYS   A 1 120 ? 8.217   46.451 41.106  1.00 50.91 ? 109 LYS   A CG  1 
ATOM   901  C  CD  . LYS   A 1 120 ? 7.427   47.266 40.083  1.00 58.91 ? 109 LYS   A CD  1 
ATOM   902  C  CE  . LYS   A 1 120 ? 6.368   46.421 39.399  1.00 64.68 ? 109 LYS   A CE  1 
ATOM   903  N  NZ  . LYS   A 1 120 ? 5.383   47.249 38.650  1.00 67.97 ? 109 LYS   A NZ  1 
ATOM   904  N  N   . PHE   A 1 121 ? 12.651  47.201 40.482  1.00 40.11 ? 110 PHE   A N   1 
ATOM   905  C  CA  . PHE   A 1 121 ? 13.640  47.440 39.441  1.00 41.56 ? 110 PHE   A CA  1 
ATOM   906  C  C   . PHE   A 1 121 ? 14.494  46.198 39.184  1.00 42.94 ? 110 PHE   A C   1 
ATOM   907  O  O   . PHE   A 1 121 ? 14.693  45.828 38.024  1.00 43.40 ? 110 PHE   A O   1 
ATOM   908  C  CB  . PHE   A 1 121 ? 14.512  48.653 39.783  1.00 41.60 ? 110 PHE   A CB  1 
ATOM   909  C  CG  . PHE   A 1 121 ? 15.398  49.124 38.657  1.00 42.39 ? 110 PHE   A CG  1 
ATOM   910  C  CD1 . PHE   A 1 121 ? 14.889  49.903 37.633  1.00 43.42 ? 110 PHE   A CD1 1 
ATOM   911  C  CD2 . PHE   A 1 121 ? 16.748  48.821 38.643  1.00 43.31 ? 110 PHE   A CD2 1 
ATOM   912  C  CE1 . PHE   A 1 121 ? 15.717  50.379 36.618  1.00 44.02 ? 110 PHE   A CE1 1 
ATOM   913  C  CE2 . PHE   A 1 121 ? 17.574  49.301 37.632  1.00 44.23 ? 110 PHE   A CE2 1 
ATOM   914  C  CZ  . PHE   A 1 121 ? 17.052  50.071 36.621  1.00 43.94 ? 110 PHE   A CZ  1 
ATOM   915  N  N   . HIS   A 1 122 ? 14.960  45.529 40.248  1.00 43.25 ? 111 HIS   A N   1 
ATOM   916  C  CA  . HIS   A 1 122 ? 15.745  44.313 40.092  1.00 44.87 ? 111 HIS   A CA  1 
ATOM   917  C  C   . HIS   A 1 122 ? 14.894  43.156 39.555  1.00 46.89 ? 111 HIS   A C   1 
ATOM   918  O  O   . HIS   A 1 122 ? 15.361  42.405 38.707  1.00 46.30 ? 111 HIS   A O   1 
ATOM   919  C  CB  . HIS   A 1 122 ? 16.442  43.931 41.402  1.00 45.34 ? 111 HIS   A CB  1 
ATOM   920  C  CG  . HIS   A 1 122 ? 17.494  44.919 41.786  1.00 48.01 ? 111 HIS   A CG  1 
ATOM   921  N  ND1 . HIS   A 1 122 ? 18.691  45.002 41.091  1.00 50.34 ? 111 HIS   A ND1 1 
ATOM   922  C  CD2 . HIS   A 1 122 ? 17.480  45.869 42.751  1.00 48.85 ? 111 HIS   A CD2 1 
ATOM   923  C  CE1 . HIS   A 1 122 ? 19.366  45.986 41.664  1.00 50.82 ? 111 HIS   A CE1 1 
ATOM   924  N  NE2 . HIS   A 1 122 ? 18.670  46.542 42.661  1.00 50.22 ? 111 HIS   A NE2 1 
ATOM   925  N  N   . ARG   A 1 123 ? 13.639  43.038 40.022  1.00 48.73 ? 112 ARG   A N   1 
ATOM   926  C  CA  . ARG   A 1 123 ? 12.713  42.001 39.581  1.00 51.10 ? 112 ARG   A CA  1 
ATOM   927  C  C   . ARG   A 1 123 ? 12.442  42.154 38.076  1.00 53.70 ? 112 ARG   A C   1 
ATOM   928  O  O   . ARG   A 1 123 ? 12.543  41.174 37.339  1.00 54.06 ? 112 ARG   A O   1 
ATOM   929  C  CB  . ARG   A 1 123 ? 11.411  42.088 40.386  1.00 52.49 ? 112 ARG   A CB  1 
ATOM   930  C  CG  . ARG   A 1 123 ? 10.531  40.855 40.318  1.00 56.57 ? 112 ARG   A CG  1 
ATOM   931  C  CD  . ARG   A 1 123 ? 9.381   40.988 41.300  1.00 61.15 ? 112 ARG   A CD  1 
ATOM   932  N  NE  . ARG   A 1 123 ? 8.434   39.874 41.218  1.00 65.71 ? 112 ARG   A NE  1 
ATOM   933  C  CZ  . ARG   A 1 123 ? 7.331   39.771 41.960  1.00 69.17 ? 112 ARG   A CZ  1 
ATOM   934  N  NH1 . ARG   A 1 123 ? 6.524   38.727 41.817  1.00 68.87 ? 112 ARG   A NH1 1 
ATOM   935  N  NH2 . ARG   A 1 123 ? 7.031   40.709 42.855  1.00 69.32 ? 112 ARG   A NH2 1 
ATOM   936  N  N   . ALA   A 1 124 ? 12.168  43.388 37.610  1.00 55.18 ? 113 ALA   A N   1 
ATOM   937  C  CA  . ALA   A 1 124 ? 11.925  43.647 36.185  1.00 57.23 ? 113 ALA   A CA  1 
ATOM   938  C  C   . ALA   A 1 124 ? 13.160  43.395 35.317  1.00 59.97 ? 113 ALA   A C   1 
ATOM   939  O  O   . ALA   A 1 124 ? 13.017  43.141 34.126  1.00 60.64 ? 113 ALA   A O   1 
ATOM   940  C  CB  . ALA   A 1 124 ? 11.430  45.070 35.976  1.00 56.93 ? 113 ALA   A CB  1 
ATOM   941  N  N   . SER   A 1 125 ? 14.364  43.478 35.898  1.00 61.45 ? 114 SER   A N   1 
ATOM   942  C  CA  . SER   A 1 125 ? 15.607  43.237 35.178  1.00 63.22 ? 114 SER   A CA  1 
ATOM   943  C  C   . SER   A 1 125 ? 15.765  41.745 34.896  1.00 65.27 ? 114 SER   A C   1 
ATOM   944  O  O   . SER   A 1 125 ? 15.958  41.375 33.742  1.00 65.24 ? 114 SER   A O   1 
ATOM   945  C  CB  . SER   A 1 125 ? 16.797  43.785 35.957  1.00 64.24 ? 114 SER   A CB  1 
ATOM   946  O  OG  . SER   A 1 125 ? 16.615  45.167 36.226  1.00 66.23 ? 114 SER   A OG  1 
ATOM   947  N  N   . LYS   A 1 126 ? 15.587  40.882 35.918  1.00 66.95 ? 115 LYS   A N   1 
ATOM   948  C  CA  . LYS   A 1 126 ? 15.652  39.419 35.752  1.00 68.93 ? 115 LYS   A CA  1 
ATOM   949  C  C   . LYS   A 1 126 ? 14.694  38.925 34.656  1.00 70.85 ? 115 LYS   A C   1 
ATOM   950  O  O   . LYS   A 1 126 ? 14.967  37.919 33.996  1.00 71.12 ? 115 LYS   A O   1 
ATOM   951  C  CB  . LYS   A 1 126 ? 15.306  38.702 37.069  1.00 70.70 ? 115 LYS   A CB  1 
ATOM   952  C  CG  . LYS   A 1 126 ? 16.187  39.084 38.253  1.00 74.70 ? 115 LYS   A CG  1 
ATOM   953  C  CD  . LYS   A 1 126 ? 16.002  38.127 39.435  1.00 78.84 ? 115 LYS   A CD  1 
ATOM   954  C  CE  . LYS   A 1 126 ? 14.584  38.117 39.956  1.00 82.57 ? 115 LYS   A CE  1 
ATOM   955  N  NZ  . LYS   A 1 126 ? 13.932  36.796 39.778  1.00 84.80 ? 115 LYS   A NZ  1 
ATOM   956  N  N   . ALA   A 1 127 ? 13.562  39.629 34.481  1.00 71.99 ? 116 ALA   A N   1 
ATOM   957  C  CA  . ALA   A 1 127 ? 12.558  39.307 33.476  1.00 73.47 ? 116 ALA   A CA  1 
ATOM   958  C  C   . ALA   A 1 127 ? 13.065  39.663 32.078  1.00 74.76 ? 116 ALA   A C   1 
ATOM   959  O  O   . ALA   A 1 127 ? 12.889  38.880 31.150  1.00 75.29 ? 116 ALA   A O   1 
ATOM   960  C  CB  . ALA   A 1 127 ? 11.267  40.056 33.777  1.00 73.58 ? 116 ALA   A CB  1 
ATOM   961  N  N   . ASN   A 1 128 ? 13.726  40.821 31.938  1.00 75.24 ? 117 ASN   A N   1 
ATOM   962  C  CA  . ASN   A 1 128 ? 14.254  41.294 30.662  1.00 76.29 ? 117 ASN   A CA  1 
ATOM   963  C  C   . ASN   A 1 128 ? 15.725  40.910 30.452  1.00 76.93 ? 117 ASN   A C   1 
ATOM   964  O  O   . ASN   A 1 128 ? 16.137  39.799 30.788  1.00 77.28 ? 117 ASN   A O   1 
ATOM   965  C  CB  . ASN   A 1 128 ? 14.084  42.809 30.555  1.00 77.74 ? 117 ASN   A CB  1 
ATOM   966  C  CG  . ASN   A 1 128 ? 12.671  43.280 30.807  1.00 81.34 ? 117 ASN   A CG  1 
ATOM   967  O  OD1 . ASN   A 1 128 ? 11.697  42.609 30.468  1.00 82.39 ? 117 ASN   A OD1 1 
ATOM   968  N  ND2 . ASN   A 1 128 ? 12.527  44.443 31.427  1.00 82.30 ? 117 ASN   A ND2 1 
ATOM   969  N  N   . LEU   A 1 134 ? 23.234  45.322 41.891  1.00 61.11 ? 123 LEU   A N   1 
ATOM   970  C  CA  . LEU   A 1 134 ? 23.424  45.922 43.214  1.00 61.16 ? 123 LEU   A CA  1 
ATOM   971  C  C   . LEU   A 1 134 ? 24.904  45.988 43.561  1.00 60.57 ? 123 LEU   A C   1 
ATOM   972  O  O   . LEU   A 1 134 ? 25.607  44.997 43.349  1.00 61.21 ? 123 LEU   A O   1 
ATOM   973  C  CB  . LEU   A 1 134 ? 22.776  45.059 44.322  1.00 61.66 ? 123 LEU   A CB  1 
ATOM   974  C  CG  . LEU   A 1 134 ? 21.553  44.201 44.015  1.00 63.92 ? 123 LEU   A CG  1 
ATOM   975  C  CD1 . LEU   A 1 134 ? 21.701  42.830 44.653  1.00 64.49 ? 123 LEU   A CD1 1 
ATOM   976  C  CD2 . LEU   A 1 134 ? 20.290  44.849 44.551  1.00 65.03 ? 123 LEU   A CD2 1 
ATOM   977  N  N   . PRO   A 1 135 ? 25.384  47.054 44.241  1.00 59.18 ? 124 PRO   A N   1 
ATOM   978  C  CA  . PRO   A 1 135 ? 26.757  47.004 44.786  1.00 58.01 ? 124 PRO   A CA  1 
ATOM   979  C  C   . PRO   A 1 135 ? 26.871  45.841 45.810  1.00 56.46 ? 124 PRO   A C   1 
ATOM   980  O  O   . PRO   A 1 135 ? 25.851  45.307 46.270  1.00 56.75 ? 124 PRO   A O   1 
ATOM   981  C  CB  . PRO   A 1 135 ? 26.939  48.374 45.461  1.00 58.92 ? 124 PRO   A CB  1 
ATOM   982  C  CG  . PRO   A 1 135 ? 25.790  49.225 44.991  1.00 59.67 ? 124 PRO   A CG  1 
ATOM   983  C  CD  . PRO   A 1 135 ? 24.676  48.282 44.652  1.00 58.50 ? 124 PRO   A CD  1 
ATOM   984  N  N   . ARG   A 1 136 ? 28.099  45.397 46.103  1.00 54.36 ? 125 ARG   A N   1 
ATOM   985  C  CA  . ARG   A 1 136 ? 28.380  44.249 46.967  1.00 52.59 ? 125 ARG   A CA  1 
ATOM   986  C  C   . ARG   A 1 136 ? 27.605  44.196 48.329  1.00 49.33 ? 125 ARG   A C   1 
ATOM   987  O  O   . ARG   A 1 136 ? 26.907  43.212 48.618  1.00 49.50 ? 125 ARG   A O   1 
ATOM   988  C  CB  . ARG   A 1 136 ? 29.888  44.164 47.210  1.00 55.09 ? 125 ARG   A CB  1 
ATOM   989  C  CG  . ARG   A 1 136 ? 30.468  42.772 47.028  1.00 59.67 ? 125 ARG   A CG  1 
ATOM   990  C  CD  . ARG   A 1 136 ? 31.912  42.856 46.560  1.00 64.05 ? 125 ARG   A CD  1 
ATOM   991  N  NE  . ARG   A 1 136 ? 32.754  43.604 47.498  1.00 67.85 ? 125 ARG   A NE  1 
ATOM   992  C  CZ  . ARG   A 1 136 ? 33.374  43.062 48.543  1.00 70.99 ? 125 ARG   A CZ  1 
ATOM   993  N  NH1 . ARG   A 1 136 ? 33.252  41.763 48.797  1.00 70.52 ? 125 ARG   A NH1 1 
ATOM   994  N  NH2 . ARG   A 1 136 ? 34.127  43.812 49.338  1.00 71.25 ? 125 ARG   A NH2 1 
ATOM   995  N  N   . GLY   A 1 137 ? 27.716  45.246 49.124  1.00 46.11 ? 126 GLY   A N   1 
ATOM   996  C  CA  . GLY   A 1 137 ? 27.071  45.286 50.429  1.00 43.42 ? 126 GLY   A CA  1 
ATOM   997  C  C   . GLY   A 1 137 ? 25.791  46.090 50.491  1.00 39.70 ? 126 GLY   A C   1 
ATOM   998  O  O   . GLY   A 1 137 ? 25.396  46.477 51.586  1.00 38.88 ? 126 GLY   A O   1 
ATOM   999  N  N   . MET   A 1 138 ? 25.115  46.332 49.335  1.00 36.86 ? 127 MET   A N   1 
ATOM   1000 C  CA  . MET   A 1 138 ? 23.877  47.109 49.354  1.00 35.35 ? 127 MET   A CA  1 
ATOM   1001 C  C   . MET   A 1 138 ? 22.768  46.463 50.178  1.00 33.85 ? 127 MET   A C   1 
ATOM   1002 O  O   . MET   A 1 138 ? 22.183  47.141 51.019  1.00 34.23 ? 127 MET   A O   1 
ATOM   1003 C  CB  . MET   A 1 138 ? 23.381  47.462 47.956  1.00 36.13 ? 127 MET   A CB  1 
ATOM   1004 C  CG  . MET   A 1 138 ? 22.130  48.316 47.971  1.00 38.46 ? 127 MET   A CG  1 
ATOM   1005 S  SD  . MET   A 1 138 ? 21.442  48.616 46.325  1.00 41.96 ? 127 MET   A SD  1 
ATOM   1006 C  CE  . MET   A 1 138 ? 19.897  49.319 46.783  1.00 42.71 ? 127 MET   A CE  1 
ATOM   1007 N  N   . VAL   A 1 139 ? 22.514  45.168 49.971  1.00 32.13 ? 128 VAL   A N   1 
ATOM   1008 C  CA  . VAL   A 1 139 ? 21.512  44.387 50.673  1.00 31.76 ? 128 VAL   A CA  1 
ATOM   1009 C  C   . VAL   A 1 139 ? 21.856  44.319 52.164  1.00 31.67 ? 128 VAL   A C   1 
ATOM   1010 O  O   . VAL   A 1 139 ? 20.998  44.585 53.017  1.00 31.68 ? 128 VAL   A O   1 
ATOM   1011 C  CB  . VAL   A 1 139 ? 21.415  42.980 50.042  1.00 32.66 ? 128 VAL   A CB  1 
ATOM   1012 C  CG1 . VAL   A 1 139 ? 20.627  42.015 50.925  1.00 33.32 ? 128 VAL   A CG1 1 
ATOM   1013 C  CG2 . VAL   A 1 139 ? 20.812  43.047 48.639  1.00 33.32 ? 128 VAL   A CG2 1 
ATOM   1014 N  N   . LYS   A 1 140 ? 23.132  44.020 52.475  1.00 30.77 ? 129 LYS   A N   1 
ATOM   1015 C  CA  . LYS   A 1 140 ? 23.602  43.945 53.847  1.00 30.17 ? 129 LYS   A CA  1 
ATOM   1016 C  C   . LYS   A 1 140 ? 23.414  45.278 54.560  1.00 30.36 ? 129 LYS   A C   1 
ATOM   1017 O  O   . LYS   A 1 140 ? 22.949  45.294 55.698  1.00 31.29 ? 129 LYS   A O   1 
ATOM   1018 C  CB  . LYS   A 1 140 ? 25.076  43.521 53.896  1.00 30.63 ? 129 LYS   A CB  1 
ATOM   1019 C  CG  . LYS   A 1 140 ? 25.608  43.451 55.331  1.00 32.28 ? 129 LYS   A CG  1 
ATOM   1020 C  CD  . LYS   A 1 140 ? 27.080  43.099 55.419  1.00 33.93 ? 129 LYS   A CD  1 
ATOM   1021 C  CE  . LYS   A 1 140 ? 27.399  41.831 54.666  1.00 34.65 ? 129 LYS   A CE  1 
ATOM   1022 N  NZ  . LYS   A 1 140 ? 28.708  41.275 55.076  1.00 35.78 ? 129 LYS   A NZ  1 
ATOM   1023 N  N   . SER   A 1 141 ? 23.739  46.387 53.882  1.00 29.31 ? 130 SER   A N   1 
ATOM   1024 C  CA  . SER   A 1 141 ? 23.637  47.732 54.433  1.00 28.74 ? 130 SER   A CA  1 
ATOM   1025 C  C   . SER   A 1 141 ? 22.199  48.139 54.642  1.00 28.96 ? 130 SER   A C   1 
ATOM   1026 O  O   . SER   A 1 141 ? 21.889  48.776 55.647  1.00 29.40 ? 130 SER   A O   1 
ATOM   1027 C  CB  . SER   A 1 141 ? 24.320  48.731 53.517  1.00 29.03 ? 130 SER   A CB  1 
ATOM   1028 O  OG  . SER   A 1 141 ? 25.666  48.349 53.323  1.00 29.98 ? 130 SER   A OG  1 
ATOM   1029 N  N   . LEU   A 1 142 ? 21.308  47.769 53.701  1.00 28.23 ? 131 LEU   A N   1 
ATOM   1030 C  CA  . LEU   A 1 142 ? 19.878  48.027 53.823  1.00 27.95 ? 131 LEU   A CA  1 
ATOM   1031 C  C   . LEU   A 1 142 ? 19.344  47.282 55.052  1.00 28.40 ? 131 LEU   A C   1 
ATOM   1032 O  O   . LEU   A 1 142 ? 18.669  47.886 55.866  1.00 29.04 ? 131 LEU   A O   1 
ATOM   1033 C  CB  . LEU   A 1 142 ? 19.145  47.548 52.555  1.00 27.50 ? 131 LEU   A CB  1 
ATOM   1034 C  CG  . LEU   A 1 142 ? 19.294  48.439 51.326  1.00 27.76 ? 131 LEU   A CG  1 
ATOM   1035 C  CD1 . LEU   A 1 142 ? 18.817  47.724 50.076  1.00 27.78 ? 131 LEU   A CD1 1 
ATOM   1036 C  CD2 . LEU   A 1 142 ? 18.535  49.734 51.503  1.00 28.35 ? 131 LEU   A CD2 1 
ATOM   1037 N  N   . LEU   A 1 143 ? 19.709  45.998 55.214  1.00 28.28 ? 132 LEU   A N   1 
ATOM   1038 C  CA  . LEU   A 1 143 ? 19.281  45.183 56.342  1.00 29.15 ? 132 LEU   A CA  1 
ATOM   1039 C  C   . LEU   A 1 143 ? 19.817  45.746 57.660  1.00 28.58 ? 132 LEU   A C   1 
ATOM   1040 O  O   . LEU   A 1 143 ? 19.052  45.873 58.609  1.00 28.32 ? 132 LEU   A O   1 
ATOM   1041 C  CB  . LEU   A 1 143 ? 19.726  43.709 56.176  1.00 29.60 ? 132 LEU   A CB  1 
ATOM   1042 C  CG  . LEU   A 1 143 ? 19.404  42.802 57.373  1.00 30.93 ? 132 LEU   A CG  1 
ATOM   1043 C  CD1 . LEU   A 1 143 ? 17.914  42.707 57.607  1.00 31.20 ? 132 LEU   A CD1 1 
ATOM   1044 C  CD2 . LEU   A 1 143 ? 20.001  41.435 57.212  1.00 31.45 ? 132 LEU   A CD2 1 
ATOM   1045 N  N   . TYR   A 1 144 ? 21.112  46.121 57.706  1.00 28.03 ? 133 TYR   A N   1 
ATOM   1046 C  CA  . TYR   A 1 144 ? 21.702  46.700 58.915  1.00 28.46 ? 133 TYR   A CA  1 
ATOM   1047 C  C   . TYR   A 1 144 ? 20.975  47.972 59.324  1.00 27.81 ? 133 TYR   A C   1 
ATOM   1048 O  O   . TYR   A 1 144 ? 20.696  48.173 60.507  1.00 28.11 ? 133 TYR   A O   1 
ATOM   1049 C  CB  . TYR   A 1 144 ? 23.205  47.014 58.751  1.00 28.81 ? 133 TYR   A CB  1 
ATOM   1050 C  CG  . TYR   A 1 144 ? 23.835  47.328 60.092  1.00 29.78 ? 133 TYR   A CG  1 
ATOM   1051 C  CD1 . TYR   A 1 144 ? 24.251  46.309 60.939  1.00 30.60 ? 133 TYR   A CD1 1 
ATOM   1052 C  CD2 . TYR   A 1 144 ? 23.883  48.632 60.574  1.00 30.61 ? 133 TYR   A CD2 1 
ATOM   1053 C  CE1 . TYR   A 1 144 ? 24.743  46.581 62.213  1.00 31.52 ? 133 TYR   A CE1 1 
ATOM   1054 C  CE2 . TYR   A 1 144 ? 24.364  48.915 61.848  1.00 31.69 ? 133 TYR   A CE2 1 
ATOM   1055 C  CZ  . TYR   A 1 144 ? 24.795  47.884 62.665  1.00 32.72 ? 133 TYR   A CZ  1 
ATOM   1056 O  OH  . TYR   A 1 144 ? 25.308  48.150 63.905  1.00 35.06 ? 133 TYR   A OH  1 
ATOM   1057 N  N   . GLN   A 1 145 ? 20.661  48.824 58.345  1.00 26.96 ? 134 GLN   A N   1 
ATOM   1058 C  CA  . GLN   A 1 145 ? 19.985  50.079 58.629  1.00 26.75 ? 134 GLN   A CA  1 
ATOM   1059 C  C   . GLN   A 1 145 ? 18.525  49.868 59.051  1.00 26.57 ? 134 GLN   A C   1 
ATOM   1060 O  O   . GLN   A 1 145 ? 18.080  50.517 59.998  1.00 27.09 ? 134 GLN   A O   1 
ATOM   1061 C  CB  . GLN   A 1 145 ? 20.147  51.058 57.473  1.00 27.92 ? 134 GLN   A CB  1 
ATOM   1062 C  CG  . GLN   A 1 145 ? 21.586  51.555 57.405  1.00 29.44 ? 134 GLN   A CG  1 
ATOM   1063 C  CD  . GLN   A 1 145 ? 21.749  52.696 56.454  1.00 30.35 ? 134 GLN   A CD  1 
ATOM   1064 O  OE1 . GLN   A 1 145 ? 20.902  53.577 56.373  1.00 29.41 ? 134 GLN   A OE1 1 
ATOM   1065 N  NE2 . GLN   A 1 145 ? 22.858  52.706 55.731  1.00 31.01 ? 134 GLN   A NE2 1 
ATOM   1066 N  N   . ILE   A 1 146 ? 17.813  48.896 58.439  1.00 25.50 ? 135 ILE   A N   1 
ATOM   1067 C  CA  . ILE   A 1 146 ? 16.449  48.572 58.855  1.00 25.10 ? 135 ILE   A CA  1 
ATOM   1068 C  C   . ILE   A 1 146 ? 16.466  48.070 60.309  1.00 26.49 ? 135 ILE   A C   1 
ATOM   1069 O  O   . ILE   A 1 146 ? 15.638  48.486 61.119  1.00 27.43 ? 135 ILE   A O   1 
ATOM   1070 C  CB  . ILE   A 1 146 ? 15.833  47.509 57.921  1.00 24.10 ? 135 ILE   A CB  1 
ATOM   1071 C  CG1 . ILE   A 1 146 ? 15.636  48.076 56.491  1.00 24.61 ? 135 ILE   A CG1 1 
ATOM   1072 C  CG2 . ILE   A 1 146 ? 14.516  46.984 58.480  1.00 23.49 ? 135 ILE   A CG2 1 
ATOM   1073 C  CD1 . ILE   A 1 146 ? 15.360  46.992 55.466  1.00 24.75 ? 135 ILE   A CD1 1 
ATOM   1074 N  N   . LEU   A 1 147 ? 17.443  47.201 60.633  1.00 25.92 ? 136 LEU   A N   1 
ATOM   1075 C  CA  . LEU   A 1 147 ? 17.625  46.638 61.961  1.00 25.71 ? 136 LEU   A CA  1 
ATOM   1076 C  C   . LEU   A 1 147 ? 17.931  47.705 62.975  1.00 25.59 ? 136 LEU   A C   1 
ATOM   1077 O  O   . LEU   A 1 147 ? 17.347  47.692 64.043  1.00 26.06 ? 136 LEU   A O   1 
ATOM   1078 C  CB  . LEU   A 1 147 ? 18.749  45.602 61.933  1.00 25.80 ? 136 LEU   A CB  1 
ATOM   1079 C  CG  . LEU   A 1 147 ? 18.402  44.257 61.299  1.00 25.25 ? 136 LEU   A CG  1 
ATOM   1080 C  CD1 . LEU   A 1 147 ? 19.654  43.420 61.125  1.00 24.31 ? 136 LEU   A CD1 1 
ATOM   1081 C  CD2 . LEU   A 1 147 ? 17.326  43.529 62.125  1.00 25.59 ? 136 LEU   A CD2 1 
ATOM   1082 N  N   . ASP   A 1 148 ? 18.792  48.670 62.625  1.00 25.51 ? 137 ASP   A N   1 
ATOM   1083 C  CA  . ASP   A 1 148 ? 19.149  49.817 63.466  1.00 25.36 ? 137 ASP   A CA  1 
ATOM   1084 C  C   . ASP   A 1 148 ? 17.930  50.711 63.784  1.00 25.66 ? 137 ASP   A C   1 
ATOM   1085 O  O   . ASP   A 1 148 ? 17.757  51.095 64.934  1.00 25.55 ? 137 ASP   A O   1 
ATOM   1086 C  CB  . ASP   A 1 148 ? 20.250  50.635 62.782  1.00 25.99 ? 137 ASP   A CB  1 
ATOM   1087 C  CG  . ASP   A 1 148 ? 21.128  51.444 63.724  1.00 29.75 ? 137 ASP   A CG  1 
ATOM   1088 O  OD1 . ASP   A 1 148 ? 20.777  51.555 64.923  1.00 29.79 ? 137 ASP   A OD1 1 
ATOM   1089 O  OD2 . ASP   A 1 148 ? 22.165  51.989 63.254  1.00 30.86 ? 137 ASP   A OD2 1 
ATOM   1090 N  N   . GLY   A 1 149 ? 17.106  51.030 62.779  1.00 25.25 ? 138 GLY   A N   1 
ATOM   1091 C  CA  . GLY   A 1 149 ? 15.917  51.847 62.988  1.00 25.47 ? 138 GLY   A CA  1 
ATOM   1092 C  C   . GLY   A 1 149 ? 14.850  51.123 63.781  1.00 26.86 ? 138 GLY   A C   1 
ATOM   1093 O  O   . GLY   A 1 149 ? 14.214  51.719 64.654  1.00 27.69 ? 138 GLY   A O   1 
ATOM   1094 N  N   . ILE   A 1 150 ? 14.655  49.813 63.510  1.00 26.90 ? 139 ILE   A N   1 
ATOM   1095 C  CA  . ILE   A 1 150 ? 13.675  48.992 64.226  1.00 27.68 ? 139 ILE   A CA  1 
ATOM   1096 C  C   . ILE   A 1 150 ? 14.112  48.773 65.679  1.00 27.93 ? 139 ILE   A C   1 
ATOM   1097 O  O   . ILE   A 1 150 ? 13.290  48.838 66.589  1.00 27.22 ? 139 ILE   A O   1 
ATOM   1098 C  CB  . ILE   A 1 150 ? 13.411  47.659 63.482  1.00 28.52 ? 139 ILE   A CB  1 
ATOM   1099 C  CG1 . ILE   A 1 150 ? 12.678  47.914 62.136  1.00 30.66 ? 139 ILE   A CG1 1 
ATOM   1100 C  CG2 . ILE   A 1 150 ? 12.626  46.670 64.349  1.00 28.76 ? 139 ILE   A CG2 1 
ATOM   1101 C  CD1 . ILE   A 1 150 ? 11.331  48.660 62.256  1.00 32.47 ? 139 ILE   A CD1 1 
ATOM   1102 N  N   . HIS   A 1 151 ? 15.414  48.581 65.899  1.00 28.27 ? 140 HIS   A N   1 
ATOM   1103 C  CA  . HIS   A 1 151 ? 15.947  48.419 67.245  1.00 29.30 ? 140 HIS   A CA  1 
ATOM   1104 C  C   . HIS   A 1 151 ? 15.723  49.684 68.059  1.00 29.81 ? 140 HIS   A C   1 
ATOM   1105 O  O   . HIS   A 1 151 ? 15.399  49.590 69.233  1.00 30.20 ? 140 HIS   A O   1 
ATOM   1106 C  CB  . HIS   A 1 151 ? 17.436  48.025 67.216  1.00 30.94 ? 140 HIS   A CB  1 
ATOM   1107 C  CG  . HIS   A 1 151 ? 18.094  48.095 68.549  1.00 34.95 ? 140 HIS   A CG  1 
ATOM   1108 N  ND1 . HIS   A 1 151 ? 18.973  49.114 68.855  1.00 37.41 ? 140 HIS   A ND1 1 
ATOM   1109 C  CD2 . HIS   A 1 151 ? 17.892  47.340 69.654  1.00 36.49 ? 140 HIS   A CD2 1 
ATOM   1110 C  CE1 . HIS   A 1 151 ? 19.318  48.924 70.123  1.00 38.00 ? 140 HIS   A CE1 1 
ATOM   1111 N  NE2 . HIS   A 1 151 ? 18.686  47.878 70.650  1.00 37.74 ? 140 HIS   A NE2 1 
ATOM   1112 N  N   . TYR   A 1 152 ? 15.855  50.865 67.431  1.00 29.48 ? 141 TYR   A N   1 
ATOM   1113 C  CA  . TYR   A 1 152 ? 15.615  52.118 68.124  1.00 28.70 ? 141 TYR   A CA  1 
ATOM   1114 C  C   . TYR   A 1 152 ? 14.131  52.216 68.513  1.00 28.19 ? 141 TYR   A C   1 
ATOM   1115 O  O   . TYR   A 1 152 ? 13.810  52.593 69.645  1.00 27.93 ? 141 TYR   A O   1 
ATOM   1116 C  CB  . TYR   A 1 152 ? 16.031  53.285 67.236  1.00 28.11 ? 141 TYR   A CB  1 
ATOM   1117 C  CG  . TYR   A 1 152 ? 15.569  54.615 67.780  1.00 28.15 ? 141 TYR   A CG  1 
ATOM   1118 C  CD1 . TYR   A 1 152 ? 16.226  55.221 68.845  1.00 28.06 ? 141 TYR   A CD1 1 
ATOM   1119 C  CD2 . TYR   A 1 152 ? 14.435  55.239 67.274  1.00 28.48 ? 141 TYR   A CD2 1 
ATOM   1120 C  CE1 . TYR   A 1 152 ? 15.794  56.438 69.355  1.00 28.17 ? 141 TYR   A CE1 1 
ATOM   1121 C  CE2 . TYR   A 1 152 ? 14.007  56.460 67.764  1.00 28.75 ? 141 TYR   A CE2 1 
ATOM   1122 C  CZ  . TYR   A 1 152 ? 14.667  57.041 68.826  1.00 29.08 ? 141 TYR   A CZ  1 
ATOM   1123 O  OH  . TYR   A 1 152 ? 14.191  58.222 69.320  1.00 30.30 ? 141 TYR   A OH  1 
ATOM   1124 N  N   . LEU   A 1 153 ? 13.220  51.889 67.562  1.00 27.30 ? 142 LEU   A N   1 
ATOM   1125 C  CA  . LEU   A 1 153 ? 11.785  51.894 67.824  1.00 27.20 ? 142 LEU   A CA  1 
ATOM   1126 C  C   . LEU   A 1 153 ? 11.459  50.931 68.986  1.00 26.94 ? 142 LEU   A C   1 
ATOM   1127 O  O   . LEU   A 1 153 ? 10.843  51.346 69.956  1.00 26.64 ? 142 LEU   A O   1 
ATOM   1128 C  CB  . LEU   A 1 153 ? 10.984  51.492 66.564  1.00 27.61 ? 142 LEU   A CB  1 
ATOM   1129 C  CG  . LEU   A 1 153 ? 11.057  52.437 65.343  1.00 28.86 ? 142 LEU   A CG  1 
ATOM   1130 C  CD1 . LEU   A 1 153 ? 10.191  51.920 64.210  1.00 29.45 ? 142 LEU   A CD1 1 
ATOM   1131 C  CD2 . LEU   A 1 153 ? 10.621  53.823 65.699  1.00 28.66 ? 142 LEU   A CD2 1 
ATOM   1132 N  N   . HIS   A 1 154 ? 11.936  49.672 68.908  1.00 26.62 ? 143 HIS   A N   1 
ATOM   1133 C  CA  . HIS   A 1 154 ? 11.702  48.630 69.907  1.00 26.74 ? 143 HIS   A CA  1 
ATOM   1134 C  C   . HIS   A 1 154 ? 12.308  48.979 71.261  1.00 27.56 ? 143 HIS   A C   1 
ATOM   1135 O  O   . HIS   A 1 154 ? 11.678  48.714 72.271  1.00 27.31 ? 143 HIS   A O   1 
ATOM   1136 C  CB  . HIS   A 1 154 ? 12.193  47.255 69.418  1.00 26.00 ? 143 HIS   A CB  1 
ATOM   1137 C  CG  . HIS   A 1 154 ? 11.388  46.665 68.291  1.00 26.12 ? 143 HIS   A CG  1 
ATOM   1138 N  ND1 . HIS   A 1 154 ? 11.705  45.433 67.758  1.00 27.40 ? 143 HIS   A ND1 1 
ATOM   1139 C  CD2 . HIS   A 1 154 ? 10.301  47.150 67.646  1.00 26.32 ? 143 HIS   A CD2 1 
ATOM   1140 C  CE1 . HIS   A 1 154 ? 10.815  45.217 66.806  1.00 27.93 ? 143 HIS   A CE1 1 
ATOM   1141 N  NE2 . HIS   A 1 154 ? 9.949   46.224 66.706  1.00 27.17 ? 143 HIS   A NE2 1 
ATOM   1142 N  N   . ALA   A 1 155 ? 13.490  49.604 71.291  1.00 27.82 ? 144 ALA   A N   1 
ATOM   1143 C  CA  . ALA   A 1 155 ? 14.088  50.044 72.555  1.00 28.86 ? 144 ALA   A CA  1 
ATOM   1144 C  C   . ALA   A 1 155 ? 13.192  51.105 73.240  1.00 30.90 ? 144 ALA   A C   1 
ATOM   1145 O  O   . ALA   A 1 155 ? 13.212  51.247 74.464  1.00 31.36 ? 144 ALA   A O   1 
ATOM   1146 C  CB  . ALA   A 1 155 ? 15.487  50.604 72.325  1.00 28.19 ? 144 ALA   A CB  1 
ATOM   1147 N  N   . ASN   A 1 156 ? 12.397  51.832 72.444  1.00 31.54 ? 145 ASN   A N   1 
ATOM   1148 C  CA  . ASN   A 1 156 ? 11.453  52.823 72.916  1.00 32.41 ? 145 ASN   A CA  1 
ATOM   1149 C  C   . ASN   A 1 156 ? 10.027  52.278 73.029  1.00 34.00 ? 145 ASN   A C   1 
ATOM   1150 O  O   . ASN   A 1 156 ? 9.106   53.077 73.107  1.00 34.54 ? 145 ASN   A O   1 
ATOM   1151 C  CB  . ASN   A 1 156 ? 11.482  54.022 71.986  1.00 32.19 ? 145 ASN   A CB  1 
ATOM   1152 C  CG  . ASN   A 1 156 ? 12.687  54.866 72.243  1.00 33.08 ? 145 ASN   A CG  1 
ATOM   1153 O  OD1 . ASN   A 1 156 ? 12.866  55.370 73.337  1.00 34.36 ? 145 ASN   A OD1 1 
ATOM   1154 N  ND2 . ASN   A 1 156 ? 13.556  55.007 71.261  1.00 32.69 ? 145 ASN   A ND2 1 
ATOM   1155 N  N   . TRP   A 1 157 ? 9.842   50.945 72.979  1.00 34.44 ? 146 TRP   A N   1 
ATOM   1156 C  CA  . TRP   A 1 157 ? 8.566   50.243 73.045  1.00 35.73 ? 146 TRP   A CA  1 
ATOM   1157 C  C   . TRP   A 1 157 ? 7.598   50.625 71.931  1.00 34.01 ? 146 TRP   A C   1 
ATOM   1158 O  O   . TRP   A 1 157 ? 6.383   50.630 72.128  1.00 34.19 ? 146 TRP   A O   1 
ATOM   1159 C  CB  . TRP   A 1 157 ? 7.932   50.398 74.412  1.00 37.84 ? 146 TRP   A CB  1 
ATOM   1160 C  CG  . TRP   A 1 157 ? 8.825   49.882 75.490  1.00 41.72 ? 146 TRP   A CG  1 
ATOM   1161 C  CD1 . TRP   A 1 157 ? 9.604   50.619 76.337  1.00 43.80 ? 146 TRP   A CD1 1 
ATOM   1162 C  CD2 . TRP   A 1 157 ? 9.107   48.504 75.774  1.00 42.98 ? 146 TRP   A CD2 1 
ATOM   1163 N  NE1 . TRP   A 1 157 ? 10.327  49.782 77.158  1.00 44.91 ? 146 TRP   A NE1 1 
ATOM   1164 C  CE2 . TRP   A 1 157 ? 10.038  48.477 76.832  1.00 44.46 ? 146 TRP   A CE2 1 
ATOM   1165 C  CE3 . TRP   A 1 157 ? 8.645   47.289 75.246  1.00 43.66 ? 146 TRP   A CE3 1 
ATOM   1166 C  CZ2 . TRP   A 1 157 ? 10.487  47.282 77.396  1.00 45.23 ? 146 TRP   A CZ2 1 
ATOM   1167 C  CZ3 . TRP   A 1 157 ? 9.120   46.109 75.782  1.00 44.73 ? 146 TRP   A CZ3 1 
ATOM   1168 C  CH2 . TRP   A 1 157 ? 10.032  46.112 76.842  1.00 45.11 ? 146 TRP   A CH2 1 
ATOM   1169 N  N   . VAL   A 1 158 ? 8.142   50.919 70.762  1.00 31.92 ? 147 VAL   A N   1 
ATOM   1170 C  CA  . VAL   A 1 158 ? 7.336   51.253 69.611  1.00 30.80 ? 147 VAL   A CA  1 
ATOM   1171 C  C   . VAL   A 1 158 ? 7.390   50.112 68.617  1.00 29.70 ? 147 VAL   A C   1 
ATOM   1172 O  O   . VAL   A 1 158 ? 8.466   49.748 68.131  1.00 29.49 ? 147 VAL   A O   1 
ATOM   1173 C  CB  . VAL   A 1 158 ? 7.749   52.608 68.960  1.00 30.53 ? 147 VAL   A CB  1 
ATOM   1174 C  CG1 . VAL   A 1 158 ? 7.045   52.818 67.618  1.00 30.95 ? 147 VAL   A CG1 1 
ATOM   1175 C  CG2 . VAL   A 1 158 ? 7.464   53.763 69.897  1.00 30.03 ? 147 VAL   A CG2 1 
ATOM   1176 N  N   . LEU   A 1 159 ? 6.235   49.534 68.330  1.00 28.93 ? 148 LEU   A N   1 
ATOM   1177 C  CA  . LEU   A 1 159 ? 6.174   48.519 67.289  1.00 28.97 ? 148 LEU   A CA  1 
ATOM   1178 C  C   . LEU   A 1 159 ? 5.759   49.236 66.005  1.00 28.71 ? 148 LEU   A C   1 
ATOM   1179 O  O   . LEU   A 1 159 ? 4.984   50.191 66.057  1.00 29.02 ? 148 LEU   A O   1 
ATOM   1180 C  CB  . LEU   A 1 159 ? 5.195   47.403 67.632  1.00 29.36 ? 148 LEU   A CB  1 
ATOM   1181 C  CG  . LEU   A 1 159 ? 5.287   46.848 69.058  1.00 30.99 ? 148 LEU   A CG  1 
ATOM   1182 C  CD1 . LEU   A 1 159 ? 4.200   45.892 69.305  1.00 31.35 ? 148 LEU   A CD1 1 
ATOM   1183 C  CD2 . LEU   A 1 159 ? 6.649   46.247 69.344  1.00 31.05 ? 148 LEU   A CD2 1 
ATOM   1184 N  N   . HIS   A 1 160 ? 6.319   48.837 64.880  1.00 28.04 ? 149 HIS   A N   1 
ATOM   1185 C  CA  . HIS   A 1 160 ? 5.939   49.418 63.605  1.00 27.73 ? 149 HIS   A CA  1 
ATOM   1186 C  C   . HIS   A 1 160 ? 4.578   48.825 63.252  1.00 28.53 ? 149 HIS   A C   1 
ATOM   1187 O  O   . HIS   A 1 160 ? 3.662   49.579 62.960  1.00 28.57 ? 149 HIS   A O   1 
ATOM   1188 C  CB  . HIS   A 1 160 ? 6.975   49.136 62.514  1.00 26.82 ? 149 HIS   A CB  1 
ATOM   1189 C  CG  . HIS   A 1 160 ? 6.643   49.825 61.229  1.00 27.52 ? 149 HIS   A CG  1 
ATOM   1190 N  ND1 . HIS   A 1 160 ? 5.520   49.481 60.492  1.00 28.74 ? 149 HIS   A ND1 1 
ATOM   1191 C  CD2 . HIS   A 1 160 ? 7.278   50.840 60.606  1.00 28.14 ? 149 HIS   A CD2 1 
ATOM   1192 C  CE1 . HIS   A 1 160 ? 5.524   50.273 59.438  1.00 29.04 ? 149 HIS   A CE1 1 
ATOM   1193 N  NE2 . HIS   A 1 160 ? 6.560   51.106 59.464  1.00 29.69 ? 149 HIS   A NE2 1 
ATOM   1194 N  N   . ARG   A 1 161 ? 4.451   47.475 63.291  1.00 29.02 ? 150 ARG   A N   1 
ATOM   1195 C  CA  . ARG   A 1 161 ? 3.222   46.711 63.010  1.00 29.82 ? 150 ARG   A CA  1 
ATOM   1196 C  C   . ARG   A 1 161 ? 2.901   46.532 61.522  1.00 30.33 ? 150 ARG   A C   1 
ATOM   1197 O  O   . ARG   A 1 161 ? 1.948   45.813 61.205  1.00 31.04 ? 150 ARG   A O   1 
ATOM   1198 C  CB  . ARG   A 1 161 ? 1.990   47.309 63.708  1.00 31.79 ? 150 ARG   A CB  1 
ATOM   1199 C  CG  . ARG   A 1 161 ? 2.055   47.403 65.242  1.00 35.35 ? 150 ARG   A CG  1 
ATOM   1200 C  CD  . ARG   A 1 161 ? 0.831   48.152 65.758  1.00 38.70 ? 150 ARG   A CD  1 
ATOM   1201 N  NE  . ARG   A 1 161 ? 0.905   48.449 67.189  1.00 42.12 ? 150 ARG   A NE  1 
ATOM   1202 C  CZ  . ARG   A 1 161 ? 0.280   49.466 67.778  1.00 44.72 ? 150 ARG   A CZ  1 
ATOM   1203 N  NH1 . ARG   A 1 161 ? 0.397   49.656 69.085  1.00 44.01 ? 150 ARG   A NH1 1 
ATOM   1204 N  NH2 . ARG   A 1 161 ? -0.455  50.310 67.061  1.00 45.15 ? 150 ARG   A NH2 1 
ATOM   1205 N  N   . ASP   A 1 162 ? 3.651   47.171 60.610  1.00 29.72 ? 151 ASP   A N   1 
ATOM   1206 C  CA  . ASP   A 1 162 ? 3.328   47.051 59.192  1.00 29.99 ? 151 ASP   A CA  1 
ATOM   1207 C  C   . ASP   A 1 162 ? 4.525   47.187 58.276  1.00 29.48 ? 151 ASP   A C   1 
ATOM   1208 O  O   . ASP   A 1 162 ? 4.376   47.688 57.161  1.00 29.89 ? 151 ASP   A O   1 
ATOM   1209 C  CB  . ASP   A 1 162 ? 2.222   48.046 58.813  1.00 32.43 ? 151 ASP   A CB  1 
ATOM   1210 C  CG  . ASP   A 1 162 ? 1.564   47.749 57.475  1.00 39.21 ? 151 ASP   A CG  1 
ATOM   1211 O  OD1 . ASP   A 1 162 ? 1.415   46.553 57.139  1.00 39.13 ? 151 ASP   A OD1 1 
ATOM   1212 O  OD2 . ASP   A 1 162 ? 1.183   48.714 56.777  1.00 43.27 ? 151 ASP   A OD2 1 
ATOM   1213 N  N   . LEU   A 1 163 ? 5.708   46.731 58.718  1.00 28.21 ? 152 LEU   A N   1 
ATOM   1214 C  CA  . LEU   A 1 163 ? 6.899   46.818 57.893  1.00 28.52 ? 152 LEU   A CA  1 
ATOM   1215 C  C   . LEU   A 1 163 ? 6.751   46.119 56.561  1.00 28.41 ? 152 LEU   A C   1 
ATOM   1216 O  O   . LEU   A 1 163 ? 6.408   44.944 56.497  1.00 29.02 ? 152 LEU   A O   1 
ATOM   1217 C  CB  . LEU   A 1 163 ? 8.121   46.241 58.590  1.00 29.28 ? 152 LEU   A CB  1 
ATOM   1218 C  CG  . LEU   A 1 163 ? 8.687   47.039 59.711  1.00 32.08 ? 152 LEU   A CG  1 
ATOM   1219 C  CD1 . LEU   A 1 163 ? 9.717   46.215 60.440  1.00 33.02 ? 152 LEU   A CD1 1 
ATOM   1220 C  CD2 . LEU   A 1 163 ? 9.299   48.356 59.192  1.00 32.98 ? 152 LEU   A CD2 1 
ATOM   1221 N  N   . LYS   A 1 164 ? 7.073   46.826 55.511  1.00 27.57 ? 153 LYS   A N   1 
ATOM   1222 C  CA  . LYS   A 1 164 ? 7.048   46.282 54.165  1.00 27.64 ? 153 LYS   A CA  1 
ATOM   1223 C  C   . LYS   A 1 164 ? 8.004   47.104 53.314  1.00 27.21 ? 153 LYS   A C   1 
ATOM   1224 O  O   . LYS   A 1 164 ? 8.356   48.218 53.678  1.00 26.97 ? 153 LYS   A O   1 
ATOM   1225 C  CB  . LYS   A 1 164 ? 5.614   46.279 53.596  1.00 29.70 ? 153 LYS   A CB  1 
ATOM   1226 C  CG  . LYS   A 1 164 ? 4.972   47.642 53.598  1.00 34.63 ? 153 LYS   A CG  1 
ATOM   1227 C  CD  . LYS   A 1 164 ? 3.695   47.621 52.848  1.00 40.42 ? 153 LYS   A CD  1 
ATOM   1228 C  CE  . LYS   A 1 164 ? 2.612   48.300 53.616  1.00 44.62 ? 153 LYS   A CE  1 
ATOM   1229 N  NZ  . LYS   A 1 164 ? 2.293   47.483 54.789  1.00 47.42 ? 153 LYS   A NZ  1 
ATOM   1230 N  N   . PRO   A 1 165 ? 8.482   46.563 52.180  1.00 27.08 ? 154 PRO   A N   1 
ATOM   1231 C  CA  . PRO   A 1 165 ? 9.410   47.340 51.326  1.00 26.71 ? 154 PRO   A CA  1 
ATOM   1232 C  C   . PRO   A 1 165 ? 8.938   48.768 51.022  1.00 27.39 ? 154 PRO   A C   1 
ATOM   1233 O  O   . PRO   A 1 165 ? 9.748   49.682 51.025  1.00 28.11 ? 154 PRO   A O   1 
ATOM   1234 C  CB  . PRO   A 1 165 ? 9.502   46.485 50.049  1.00 26.66 ? 154 PRO   A CB  1 
ATOM   1235 C  CG  . PRO   A 1 165 ? 9.221   45.084 50.509  1.00 26.79 ? 154 PRO   A CG  1 
ATOM   1236 C  CD  . PRO   A 1 165 ? 8.200   45.225 51.616  1.00 25.24 ? 154 PRO   A CD  1 
ATOM   1237 N  N   . ALA   A 1 166 ? 7.638   48.973 50.785  1.00 27.21 ? 155 ALA   A N   1 
ATOM   1238 C  CA  . ALA   A 1 166 ? 7.107   50.303 50.461  1.00 27.33 ? 155 ALA   A CA  1 
ATOM   1239 C  C   . ALA   A 1 166 ? 7.323   51.374 51.543  1.00 28.14 ? 155 ALA   A C   1 
ATOM   1240 O  O   . ALA   A 1 166 ? 7.506   52.543 51.193  1.00 27.89 ? 155 ALA   A O   1 
ATOM   1241 C  CB  . ALA   A 1 166 ? 5.639   50.215 50.101  1.00 27.02 ? 155 ALA   A CB  1 
ATOM   1242 N  N   . ASN   A 1 167 ? 7.298   51.000 52.847  1.00 28.08 ? 156 ASN   A N   1 
ATOM   1243 C  CA  . ASN   A 1 167 ? 7.539   52.006 53.892  1.00 28.20 ? 156 ASN   A CA  1 
ATOM   1244 C  C   . ASN   A 1 167 ? 9.008   52.009 54.391  1.00 29.34 ? 156 ASN   A C   1 
ATOM   1245 O  O   . ASN   A 1 167 ? 9.300   52.583 55.436  1.00 30.28 ? 156 ASN   A O   1 
ATOM   1246 C  CB  . ASN   A 1 167 ? 6.534   51.919 55.031  1.00 28.12 ? 156 ASN   A CB  1 
ATOM   1247 C  CG  . ASN   A 1 167 ? 6.401   50.545 55.607  1.00 29.41 ? 156 ASN   A CG  1 
ATOM   1248 O  OD1 . ASN   A 1 167 ? 7.388   49.824 55.770  1.00 30.28 ? 156 ASN   A OD1 1 
ATOM   1249 N  ND2 . ASN   A 1 167 ? 5.181   50.158 55.936  1.00 28.38 ? 156 ASN   A ND2 1 
ATOM   1250 N  N   . ILE   A 1 168 ? 9.933   51.388 53.634  1.00 28.87 ? 157 ILE   A N   1 
ATOM   1251 C  CA  . ILE   A 1 168 ? 11.347  51.447 53.946  1.00 28.60 ? 157 ILE   A CA  1 
ATOM   1252 C  C   . ILE   A 1 168 ? 11.928  52.346 52.851  1.00 28.12 ? 157 ILE   A C   1 
ATOM   1253 O  O   . ILE   A 1 168 ? 12.271  51.891 51.753  1.00 28.03 ? 157 ILE   A O   1 
ATOM   1254 C  CB  . ILE   A 1 168 ? 12.041  50.066 53.960  1.00 29.49 ? 157 ILE   A CB  1 
ATOM   1255 C  CG1 . ILE   A 1 168 ? 11.407  49.094 54.981  1.00 30.83 ? 157 ILE   A CG1 1 
ATOM   1256 C  CG2 . ILE   A 1 168 ? 13.549  50.239 54.190  1.00 29.87 ? 157 ILE   A CG2 1 
ATOM   1257 C  CD1 . ILE   A 1 168 ? 11.485  49.566 56.398  1.00 32.72 ? 157 ILE   A CD1 1 
ATOM   1258 N  N   . LEU   A 1 169 ? 11.972  53.633 53.129  1.00 27.80 ? 158 LEU   A N   1 
ATOM   1259 C  CA  . LEU   A 1 169 ? 12.488  54.634 52.206  1.00 27.56 ? 158 LEU   A CA  1 
ATOM   1260 C  C   . LEU   A 1 169 ? 14.007  54.662 52.231  1.00 28.12 ? 158 LEU   A C   1 
ATOM   1261 O  O   . LEU   A 1 169 ? 14.613  54.271 53.224  1.00 27.60 ? 158 LEU   A O   1 
ATOM   1262 C  CB  . LEU   A 1 169 ? 11.966  56.015 52.593  1.00 27.18 ? 158 LEU   A CB  1 
ATOM   1263 C  CG  . LEU   A 1 169 ? 10.470  56.147 52.865  1.00 27.36 ? 158 LEU   A CG  1 
ATOM   1264 C  CD1 . LEU   A 1 169 ? 10.150  57.532 53.348  1.00 27.01 ? 158 LEU   A CD1 1 
ATOM   1265 C  CD2 . LEU   A 1 169 ? 9.668   55.804 51.648  1.00 27.56 ? 158 LEU   A CD2 1 
ATOM   1266 N  N   . VAL   A 1 170 ? 14.634  55.136 51.136  1.00 28.26 ? 159 VAL   A N   1 
ATOM   1267 C  CA  . VAL   A 1 170 ? 16.077  55.247 51.045  1.00 28.95 ? 159 VAL   A CA  1 
ATOM   1268 C  C   . VAL   A 1 170 ? 16.350  56.615 50.395  1.00 29.56 ? 159 VAL   A C   1 
ATOM   1269 O  O   . VAL   A 1 170 ? 15.811  56.906 49.321  1.00 29.11 ? 159 VAL   A O   1 
ATOM   1270 C  CB  . VAL   A 1 170 ? 16.731  54.088 50.232  1.00 29.71 ? 159 VAL   A CB  1 
ATOM   1271 C  CG1 . VAL   A 1 170 ? 18.237  54.249 50.191  1.00 30.77 ? 159 VAL   A CG1 1 
ATOM   1272 C  CG2 . VAL   A 1 170 ? 16.376  52.717 50.790  1.00 29.74 ? 159 VAL   A CG2 1 
ATOM   1273 N  N   . MET   A 1 171 ? 17.149  57.464 51.057  1.00 29.45 ? 160 MET   A N   1 
ATOM   1274 C  CA  . MET   A 1 171 ? 17.432  58.787 50.523  1.00 30.34 ? 160 MET   A CA  1 
ATOM   1275 C  C   . MET   A 1 171 ? 18.218  58.731 49.215  1.00 31.75 ? 160 MET   A C   1 
ATOM   1276 O  O   . MET   A 1 171 ? 19.089  57.873 49.040  1.00 31.82 ? 160 MET   A O   1 
ATOM   1277 C  CB  . MET   A 1 171 ? 18.186  59.638 51.550  1.00 30.36 ? 160 MET   A CB  1 
ATOM   1278 C  CG  . MET   A 1 171 ? 17.440  59.823 52.866  1.00 31.33 ? 160 MET   A CG  1 
ATOM   1279 S  SD  . MET   A 1 171 ? 15.893  60.725 52.649  1.00 35.87 ? 160 MET   A SD  1 
ATOM   1280 C  CE  . MET   A 1 171 ? 16.501  62.317 52.251  1.00 31.51 ? 160 MET   A CE  1 
ATOM   1281 N  N   . GLY   A 1 172 ? 17.899  59.644 48.306  1.00 32.33 ? 161 GLY   A N   1 
ATOM   1282 C  CA  . GLY   A 1 172 ? 18.623  59.760 47.047  1.00 33.49 ? 161 GLY   A CA  1 
ATOM   1283 C  C   . GLY   A 1 172 ? 19.781  60.737 47.190  1.00 34.95 ? 161 GLY   A C   1 
ATOM   1284 O  O   . GLY   A 1 172 ? 20.252  60.992 48.307  1.00 35.00 ? 161 GLY   A O   1 
ATOM   1285 N  N   . GLU   A 1 173 ? 20.240  61.330 46.072  1.00 35.60 ? 162 GLU   A N   1 
ATOM   1286 C  CA  . GLU   A 1 173 ? 21.355  62.287 46.109  1.00 36.66 ? 162 GLU   A CA  1 
ATOM   1287 C  C   . GLU   A 1 173 ? 21.171  63.403 47.125  1.00 37.35 ? 162 GLU   A C   1 
ATOM   1288 O  O   . GLU   A 1 173 ? 20.070  63.925 47.274  1.00 38.00 ? 162 GLU   A O   1 
ATOM   1289 C  CB  . GLU   A 1 173 ? 21.644  62.883 44.720  1.00 38.89 ? 162 GLU   A CB  1 
ATOM   1290 C  CG  . GLU   A 1 173 ? 22.017  61.851 43.667  1.00 43.89 ? 162 GLU   A CG  1 
ATOM   1291 C  CD  . GLU   A 1 173 ? 23.351  61.164 43.873  1.00 50.37 ? 162 GLU   A CD  1 
ATOM   1292 O  OE1 . GLU   A 1 173 ? 24.207  61.721 44.600  1.00 50.82 ? 162 GLU   A OE1 1 
ATOM   1293 O  OE2 . GLU   A 1 173 ? 23.544  60.068 43.297  1.00 53.44 ? 162 GLU   A OE2 1 
ATOM   1294 N  N   . GLY   A 1 174 ? 22.237  63.710 47.851  1.00 36.95 ? 163 GLY   A N   1 
ATOM   1295 C  CA  . GLY   A 1 174 ? 22.222  64.744 48.871  1.00 37.02 ? 163 GLY   A CA  1 
ATOM   1296 C  C   . GLY   A 1 174 ? 23.102  64.388 50.046  1.00 37.55 ? 163 GLY   A C   1 
ATOM   1297 O  O   . GLY   A 1 174 ? 23.900  63.447 49.984  1.00 37.38 ? 163 GLY   A O   1 
ATOM   1298 N  N   . PRO   A 1 175 ? 22.941  65.124 51.158  1.00 37.89 ? 164 PRO   A N   1 
ATOM   1299 C  CA  . PRO   A 1 175 ? 23.768  64.858 52.354  1.00 38.23 ? 164 PRO   A CA  1 
ATOM   1300 C  C   . PRO   A 1 175 ? 23.515  63.530 53.071  1.00 39.15 ? 164 PRO   A C   1 
ATOM   1301 O  O   . PRO   A 1 175 ? 24.338  63.130 53.904  1.00 39.76 ? 164 PRO   A O   1 
ATOM   1302 C  CB  . PRO   A 1 175 ? 23.451  66.032 53.279  1.00 39.05 ? 164 PRO   A CB  1 
ATOM   1303 C  CG  . PRO   A 1 175 ? 22.136  66.543 52.824  1.00 39.66 ? 164 PRO   A CG  1 
ATOM   1304 C  CD  . PRO   A 1 175 ? 22.057  66.289 51.343  1.00 37.46 ? 164 PRO   A CD  1 
ATOM   1305 N  N   . GLU   A 1 176 ? 22.382  62.848 52.768  1.00 38.34 ? 165 GLU   A N   1 
ATOM   1306 C  CA  . GLU   A 1 176 ? 22.034  61.561 53.393  1.00 37.47 ? 165 GLU   A CA  1 
ATOM   1307 C  C   . GLU   A 1 176 ? 21.875  60.448 52.350  1.00 36.91 ? 165 GLU   A C   1 
ATOM   1308 O  O   . GLU   A 1 176 ? 21.100  59.511 52.541  1.00 36.69 ? 165 GLU   A O   1 
ATOM   1309 C  CB  . GLU   A 1 176 ? 20.741  61.676 54.201  1.00 38.18 ? 165 GLU   A CB  1 
ATOM   1310 C  CG  . GLU   A 1 176 ? 20.833  62.619 55.377  1.00 40.78 ? 165 GLU   A CG  1 
ATOM   1311 C  CD  . GLU   A 1 176 ? 19.695  62.407 56.353  1.00 44.70 ? 165 GLU   A CD  1 
ATOM   1312 O  OE1 . GLU   A 1 176 ? 19.845  61.567 57.269  1.00 43.88 ? 165 GLU   A OE1 1 
ATOM   1313 O  OE2 . GLU   A 1 176 ? 18.643  63.063 56.186  1.00 47.72 ? 165 GLU   A OE2 1 
ATOM   1314 N  N   . ARG   A 1 177 ? 22.624  60.539 51.257  1.00 36.04 ? 166 ARG   A N   1 
ATOM   1315 C  CA  . ARG   A 1 177 ? 22.611  59.583 50.166  1.00 35.62 ? 166 ARG   A CA  1 
ATOM   1316 C  C   . ARG   A 1 177 ? 22.674  58.114 50.653  1.00 34.87 ? 166 ARG   A C   1 
ATOM   1317 O  O   . ARG   A 1 177 ? 23.552  57.753 51.453  1.00 35.37 ? 166 ARG   A O   1 
ATOM   1318 C  CB  . ARG   A 1 177 ? 23.795  59.899 49.254  1.00 36.73 ? 166 ARG   A CB  1 
ATOM   1319 C  CG  . ARG   A 1 177 ? 23.708  59.279 47.888  1.00 40.67 ? 166 ARG   A CG  1 
ATOM   1320 C  CD  . ARG   A 1 177 ? 25.021  59.519 47.181  1.00 45.10 ? 166 ARG   A CD  1 
ATOM   1321 N  NE  . ARG   A 1 177 ? 24.980  59.033 45.809  1.00 49.69 ? 166 ARG   A NE  1 
ATOM   1322 C  CZ  . ARG   A 1 177 ? 25.401  57.836 45.418  1.00 53.11 ? 166 ARG   A CZ  1 
ATOM   1323 N  NH1 . ARG   A 1 177 ? 25.929  56.989 46.295  1.00 51.74 ? 166 ARG   A NH1 1 
ATOM   1324 N  NH2 . ARG   A 1 177 ? 25.326  57.486 44.143  1.00 54.54 ? 166 ARG   A NH2 1 
ATOM   1325 N  N   . GLY   A 1 178 ? 21.699  57.323 50.221  1.00 33.24 ? 167 GLY   A N   1 
ATOM   1326 C  CA  . GLY   A 1 178 ? 21.604  55.910 50.558  1.00 32.46 ? 167 GLY   A CA  1 
ATOM   1327 C  C   . GLY   A 1 178 ? 21.340  55.592 52.014  1.00 31.32 ? 167 GLY   A C   1 
ATOM   1328 O  O   . GLY   A 1 178 ? 21.782  54.556 52.499  1.00 31.29 ? 167 GLY   A O   1 
ATOM   1329 N  N   . ARG   A 1 179 ? 20.669  56.484 52.737  1.00 30.36 ? 168 ARG   A N   1 
ATOM   1330 C  CA  . ARG   A 1 179 ? 20.350  56.220 54.133  1.00 29.68 ? 168 ARG   A CA  1 
ATOM   1331 C  C   . ARG   A 1 179 ? 18.925  55.733 54.199  1.00 28.73 ? 168 ARG   A C   1 
ATOM   1332 O  O   . ARG   A 1 179 ? 18.041  56.372 53.636  1.00 29.29 ? 168 ARG   A O   1 
ATOM   1333 C  CB  . ARG   A 1 179 ? 20.554  57.459 55.014  1.00 31.01 ? 168 ARG   A CB  1 
ATOM   1334 C  CG  . ARG   A 1 179 ? 20.166  57.204 56.454  1.00 33.98 ? 168 ARG   A CG  1 
ATOM   1335 C  CD  . ARG   A 1 179 ? 20.629  58.304 57.330  1.00 38.18 ? 168 ARG   A CD  1 
ATOM   1336 N  NE  . ARG   A 1 179 ? 22.077  58.276 57.524  1.00 41.84 ? 168 ARG   A NE  1 
ATOM   1337 C  CZ  . ARG   A 1 179 ? 22.785  59.299 57.992  1.00 45.11 ? 168 ARG   A CZ  1 
ATOM   1338 N  NH1 . ARG   A 1 179 ? 22.188  60.447 58.298  1.00 44.57 ? 168 ARG   A NH1 1 
ATOM   1339 N  NH2 . ARG   A 1 179 ? 24.097  59.186 58.156  1.00 46.13 ? 168 ARG   A NH2 1 
ATOM   1340 N  N   . VAL   A 1 180 ? 18.700  54.596 54.851  1.00 27.68 ? 169 VAL   A N   1 
ATOM   1341 C  CA  . VAL   A 1 180 ? 17.357  54.048 55.020  1.00 27.15 ? 169 VAL   A CA  1 
ATOM   1342 C  C   . VAL   A 1 180 ? 16.589  54.932 56.001  1.00 26.71 ? 169 VAL   A C   1 
ATOM   1343 O  O   . VAL   A 1 180 ? 17.142  55.370 56.999  1.00 26.80 ? 169 VAL   A O   1 
ATOM   1344 C  CB  . VAL   A 1 180 ? 17.425  52.584 55.529  1.00 27.57 ? 169 VAL   A CB  1 
ATOM   1345 C  CG1 . VAL   A 1 180 ? 16.077  52.107 56.085  1.00 27.79 ? 169 VAL   A CG1 1 
ATOM   1346 C  CG2 . VAL   A 1 180 ? 17.931  51.647 54.438  1.00 27.30 ? 169 VAL   A CG2 1 
ATOM   1347 N  N   . LYS   A 1 181 ? 15.327  55.197 55.701  1.00 26.21 ? 170 LYS   A N   1 
ATOM   1348 C  CA  . LYS   A 1 181 ? 14.405  55.939 56.543  1.00 26.24 ? 170 LYS   A CA  1 
ATOM   1349 C  C   . LYS   A 1 181 ? 13.152  55.081 56.665  1.00 26.75 ? 170 LYS   A C   1 
ATOM   1350 O  O   . LYS   A 1 181 ? 12.468  54.860 55.680  1.00 27.58 ? 170 LYS   A O   1 
ATOM   1351 C  CB  . LYS   A 1 181 ? 14.033  57.284 55.912  1.00 26.29 ? 170 LYS   A CB  1 
ATOM   1352 C  CG  . LYS   A 1 181 ? 15.193  58.237 55.735  1.00 27.46 ? 170 LYS   A CG  1 
ATOM   1353 C  CD  . LYS   A 1 181 ? 15.749  58.724 57.058  1.00 27.60 ? 170 LYS   A CD  1 
ATOM   1354 C  CE  . LYS   A 1 181 ? 16.925  59.626 56.778  1.00 28.29 ? 170 LYS   A CE  1 
ATOM   1355 N  NZ  . LYS   A 1 181 ? 17.511  60.199 58.025  1.00 27.78 ? 170 LYS   A NZ  1 
ATOM   1356 N  N   . ILE   A 1 182 ? 12.892  54.546 57.840  1.00 26.10 ? 171 ILE   A N   1 
ATOM   1357 C  CA  . ILE   A 1 182 ? 11.705  53.766 58.106  1.00 25.82 ? 171 ILE   A CA  1 
ATOM   1358 C  C   . ILE   A 1 182 ? 10.557  54.770 58.222  1.00 25.57 ? 171 ILE   A C   1 
ATOM   1359 O  O   . ILE   A 1 182 ? 10.647  55.771 58.930  1.00 25.00 ? 171 ILE   A O   1 
ATOM   1360 C  CB  . ILE   A 1 182 ? 11.901  52.901 59.386  1.00 26.29 ? 171 ILE   A CB  1 
ATOM   1361 C  CG1 . ILE   A 1 182 ? 12.910  51.760 59.103  1.00 27.25 ? 171 ILE   A CG1 1 
ATOM   1362 C  CG2 . ILE   A 1 182 ? 10.554  52.338 59.906  1.00 26.09 ? 171 ILE   A CG2 1 
ATOM   1363 C  CD1 . ILE   A 1 182 ? 13.341  51.050 60.344  1.00 29.10 ? 171 ILE   A CD1 1 
ATOM   1364 N  N   . ALA   A 1 183 ? 9.494   54.522 57.475  1.00 26.01 ? 172 ALA   A N   1 
ATOM   1365 C  CA  . ALA   A 1 183 ? 8.350   55.413 57.422  1.00 26.44 ? 172 ALA   A CA  1 
ATOM   1366 C  C   . ALA   A 1 183 ? 7.060   54.725 57.896  1.00 27.36 ? 172 ALA   A C   1 
ATOM   1367 O  O   . ALA   A 1 183 ? 7.008   53.494 57.990  1.00 27.50 ? 172 ALA   A O   1 
ATOM   1368 C  CB  . ALA   A 1 183 ? 8.192   55.945 55.987  1.00 25.88 ? 172 ALA   A CB  1 
ATOM   1369 N  N   . ASP   A 1 184 ? 6.036   55.537 58.211  1.00 28.22 ? 173 ASP   A N   1 
ATOM   1370 C  CA  . ASP   A 1 184 ? 4.687   55.135 58.569  1.00 29.94 ? 173 ASP   A CA  1 
ATOM   1371 C  C   . ASP   A 1 184 ? 4.531   54.556 59.980  1.00 32.29 ? 173 ASP   A C   1 
ATOM   1372 O  O   . ASP   A 1 184 ? 4.449   53.340 60.134  1.00 32.82 ? 173 ASP   A O   1 
ATOM   1373 C  CB  . ASP   A 1 184 ? 4.107   54.175 57.517  1.00 30.38 ? 173 ASP   A CB  1 
ATOM   1374 C  CG  . ASP   A 1 184 ? 2.607   54.242 57.356  1.00 34.88 ? 173 ASP   A CG  1 
ATOM   1375 O  OD1 . ASP   A 1 184 ? 1.938   54.815 58.247  1.00 36.19 ? 173 ASP   A OD1 1 
ATOM   1376 O  OD2 . ASP   A 1 184 ? 2.091   53.705 56.342  1.00 36.88 ? 173 ASP   A OD2 1 
ATOM   1377 N  N   . MET   A 1 185 ? 4.415   55.421 60.991  1.00 33.47 ? 174 MET   A N   1 
ATOM   1378 C  CA  . MET   A 1 185 ? 4.090   54.986 62.356  1.00 35.79 ? 174 MET   A CA  1 
ATOM   1379 C  C   . MET   A 1 185 ? 2.564   55.034 62.598  1.00 37.52 ? 174 MET   A C   1 
ATOM   1380 O  O   . MET   A 1 185 ? 2.143   54.939 63.748  1.00 37.65 ? 174 MET   A O   1 
ATOM   1381 C  CB  . MET   A 1 185 ? 4.732   55.893 63.431  1.00 37.06 ? 174 MET   A CB  1 
ATOM   1382 C  CG  . MET   A 1 185 ? 6.238   55.946 63.415  1.00 40.13 ? 174 MET   A CG  1 
ATOM   1383 S  SD  . MET   A 1 185 ? 7.087   54.362 63.329  1.00 43.63 ? 174 MET   A SD  1 
ATOM   1384 C  CE  . MET   A 1 185 ? 7.865   54.562 61.750  1.00 44.79 ? 174 MET   A CE  1 
ATOM   1385 N  N   . GLY   A 1 186 ? 1.758   55.202 61.550  1.00 38.44 ? 175 GLY   A N   1 
ATOM   1386 C  CA  . GLY   A 1 186 ? 0.327   55.373 61.707  1.00 40.33 ? 175 GLY   A CA  1 
ATOM   1387 C  C   . GLY   A 1 186 ? -0.520  54.132 61.759  1.00 42.56 ? 175 GLY   A C   1 
ATOM   1388 O  O   . GLY   A 1 186 ? -1.746  54.244 61.701  1.00 42.96 ? 175 GLY   A O   1 
ATOM   1389 N  N   . PHE   A 1 187 ? 0.098   52.950 61.880  1.00 44.01 ? 176 PHE   A N   1 
ATOM   1390 C  CA  . PHE   A 1 187 ? -0.675  51.725 61.990  1.00 46.23 ? 176 PHE   A CA  1 
ATOM   1391 C  C   . PHE   A 1 187 ? -1.159  51.595 63.440  1.00 48.67 ? 176 PHE   A C   1 
ATOM   1392 O  O   . PHE   A 1 187 ? -0.573  50.859 64.229  1.00 48.31 ? 176 PHE   A O   1 
ATOM   1393 C  CB  . PHE   A 1 187 ? 0.140   50.507 61.550  1.00 46.23 ? 176 PHE   A CB  1 
ATOM   1394 C  CG  . PHE   A 1 187 ? -0.722  49.397 61.010  1.00 47.28 ? 176 PHE   A CG  1 
ATOM   1395 C  CD1 . PHE   A 1 187 ? -1.113  49.386 59.682  1.00 48.51 ? 176 PHE   A CD1 1 
ATOM   1396 C  CD2 . PHE   A 1 187 ? -1.144  48.365 61.829  1.00 48.35 ? 176 PHE   A CD2 1 
ATOM   1397 C  CE1 . PHE   A 1 187 ? -1.910  48.360 59.184  1.00 49.48 ? 176 PHE   A CE1 1 
ATOM   1398 C  CE2 . PHE   A 1 187 ? -1.929  47.331 61.324  1.00 49.26 ? 176 PHE   A CE2 1 
ATOM   1399 C  CZ  . PHE   A 1 187 ? -2.322  47.345 60.012  1.00 49.19 ? 176 PHE   A CZ  1 
ATOM   1400 N  N   . ALA   A 1 188 ? -2.195  52.364 63.804  1.00 50.91 ? 177 ALA   A N   1 
ATOM   1401 C  CA  . ALA   A 1 188 ? -2.730  52.328 65.158  1.00 53.58 ? 177 ALA   A CA  1 
ATOM   1402 C  C   . ALA   A 1 188 ? -3.726  51.192 65.283  1.00 56.19 ? 177 ALA   A C   1 
ATOM   1403 O  O   . ALA   A 1 188 ? -4.496  50.934 64.349  1.00 56.39 ? 177 ALA   A O   1 
ATOM   1404 C  CB  . ALA   A 1 188 ? -3.390  53.640 65.508  1.00 53.76 ? 177 ALA   A CB  1 
ATOM   1405 N  N   . ARG   A 1 189 ? -3.663  50.467 66.417  1.00 57.47 ? 178 ARG   A N   1 
ATOM   1406 C  CA  . ARG   A 1 189 ? -4.533  49.326 66.681  1.00 59.22 ? 178 ARG   A CA  1 
ATOM   1407 C  C   . ARG   A 1 189 ? -5.205  49.406 68.056  1.00 60.15 ? 178 ARG   A C   1 
ATOM   1408 O  O   . ARG   A 1 189 ? -5.068  50.401 68.769  1.00 60.63 ? 178 ARG   A O   1 
ATOM   1409 C  CB  . ARG   A 1 189 ? -3.747  48.016 66.551  1.00 61.50 ? 178 ARG   A CB  1 
ATOM   1410 C  CG  . ARG   A 1 189 ? -3.017  47.870 65.214  1.00 66.32 ? 178 ARG   A CG  1 
ATOM   1411 C  CD  . ARG   A 1 189 ? -3.964  47.813 64.027  1.00 70.76 ? 178 ARG   A CD  1 
ATOM   1412 N  NE  . ARG   A 1 189 ? -4.905  46.693 64.098  1.00 74.60 ? 178 ARG   A NE  1 
ATOM   1413 C  CZ  . ARG   A 1 189 ? -5.931  46.526 63.268  1.00 77.15 ? 178 ARG   A CZ  1 
ATOM   1414 N  NH1 . ARG   A 1 189 ? -6.741  45.483 63.405  1.00 76.40 ? 178 ARG   A NH1 1 
ATOM   1415 N  NH2 . ARG   A 1 189 ? -6.153  47.399 62.290  1.00 77.43 ? 178 ARG   A NH2 1 
ATOM   1416 N  N   . THR   A 1 207 ? -2.170  42.802 50.984  1.00 44.38 ? 196 THR   A N   1 
ATOM   1417 C  CA  . THR   A 1 207 ? -1.590  41.457 51.048  1.00 44.52 ? 196 THR   A CA  1 
ATOM   1418 C  C   . THR   A 1 207 ? -1.012  41.152 52.441  1.00 43.52 ? 196 THR   A C   1 
ATOM   1419 O  O   . THR   A 1 207 ? -0.686  42.071 53.186  1.00 43.64 ? 196 THR   A O   1 
ATOM   1420 C  CB  . THR   A 1 207 ? -0.538  41.270 49.943  1.00 46.27 ? 196 THR   A CB  1 
ATOM   1421 O  OG1 . THR   A 1 207 ? 0.670   41.954 50.297  1.00 47.72 ? 196 THR   A OG1 1 
ATOM   1422 C  CG2 . THR   A 1 207 ? -1.030  41.730 48.581  1.00 46.78 ? 196 THR   A CG2 1 
ATOM   1423 N  N   . PHE   A 1 208 ? -0.831  39.864 52.764  1.00 42.07 ? 197 PHE   A N   1 
ATOM   1424 C  CA  . PHE   A 1 208 ? -0.296  39.451 54.060  1.00 40.96 ? 197 PHE   A CA  1 
ATOM   1425 C  C   . PHE   A 1 208 ? 1.112   38.819 53.960  1.00 37.26 ? 197 PHE   A C   1 
ATOM   1426 O  O   . PHE   A 1 208 ? 1.546   38.169 54.909  1.00 36.65 ? 197 PHE   A O   1 
ATOM   1427 C  CB  . PHE   A 1 208 ? -1.281  38.490 54.774  1.00 42.38 ? 197 PHE   A CB  1 
ATOM   1428 C  CG  . PHE   A 1 208 ? -2.710  38.988 54.788  1.00 44.64 ? 197 PHE   A CG  1 
ATOM   1429 C  CD1 . PHE   A 1 208 ? -3.140  39.885 55.748  1.00 45.97 ? 197 PHE   A CD1 1 
ATOM   1430 C  CD2 . PHE   A 1 208 ? -3.616  38.577 53.822  1.00 46.08 ? 197 PHE   A CD2 1 
ATOM   1431 C  CE1 . PHE   A 1 208 ? -4.447  40.364 55.741  1.00 46.91 ? 197 PHE   A CE1 1 
ATOM   1432 C  CE2 . PHE   A 1 208 ? -4.926  39.051 53.826  1.00 46.80 ? 197 PHE   A CE2 1 
ATOM   1433 C  CZ  . PHE   A 1 208 ? -5.330  39.943 54.782  1.00 46.53 ? 197 PHE   A CZ  1 
ATOM   1434 N  N   . TRP   A 1 209 ? 1.844   39.066 52.853  1.00 34.58 ? 198 TRP   A N   1 
ATOM   1435 C  CA  . TRP   A 1 209 ? 3.180   38.513 52.596  1.00 32.71 ? 198 TRP   A CA  1 
ATOM   1436 C  C   . TRP   A 1 209 ? 4.200   38.760 53.679  1.00 31.18 ? 198 TRP   A C   1 
ATOM   1437 O  O   . TRP   A 1 209 ? 5.188   38.024 53.771  1.00 31.16 ? 198 TRP   A O   1 
ATOM   1438 C  CB  . TRP   A 1 209 ? 3.758   39.015 51.268  1.00 32.43 ? 198 TRP   A CB  1 
ATOM   1439 C  CG  . TRP   A 1 209 ? 2.834   38.940 50.087  1.00 33.49 ? 198 TRP   A CG  1 
ATOM   1440 C  CD1 . TRP   A 1 209 ? 1.720   38.156 49.948  1.00 34.49 ? 198 TRP   A CD1 1 
ATOM   1441 C  CD2 . TRP   A 1 209 ? 3.020   39.597 48.830  1.00 33.46 ? 198 TRP   A CD2 1 
ATOM   1442 N  NE1 . TRP   A 1 209 ? 1.163   38.348 48.707  1.00 35.13 ? 198 TRP   A NE1 1 
ATOM   1443 C  CE2 . TRP   A 1 209 ? 1.955   39.211 47.991  1.00 34.66 ? 198 TRP   A CE2 1 
ATOM   1444 C  CE3 . TRP   A 1 209 ? 3.969   40.500 48.340  1.00 34.07 ? 198 TRP   A CE3 1 
ATOM   1445 C  CZ2 . TRP   A 1 209 ? 1.795   39.730 46.704  1.00 35.17 ? 198 TRP   A CZ2 1 
ATOM   1446 C  CZ3 . TRP   A 1 209 ? 3.836   40.975 47.044  1.00 34.98 ? 198 TRP   A CZ3 1 
ATOM   1447 C  CH2 . TRP   A 1 209 ? 2.773   40.573 46.234  1.00 34.93 ? 198 TRP   A CH2 1 
ATOM   1448 N  N   . TYR   A 1 210 ? 3.996   39.803 54.476  1.00 29.78 ? 199 TYR   A N   1 
ATOM   1449 C  CA  . TYR   A 1 210 ? 4.943   40.176 55.534  1.00 29.08 ? 199 TYR   A CA  1 
ATOM   1450 C  C   . TYR   A 1 210 ? 4.402   39.898 56.938  1.00 29.85 ? 199 TYR   A C   1 
ATOM   1451 O  O   . TYR   A 1 210 ? 5.072   40.218 57.910  1.00 30.04 ? 199 TYR   A O   1 
ATOM   1452 C  CB  . TYR   A 1 210 ? 5.393   41.656 55.364  1.00 28.01 ? 199 TYR   A CB  1 
ATOM   1453 C  CG  . TYR   A 1 210 ? 5.865   41.928 53.953  1.00 27.58 ? 199 TYR   A CG  1 
ATOM   1454 C  CD1 . TYR   A 1 210 ? 7.169   41.651 53.574  1.00 28.31 ? 199 TYR   A CD1 1 
ATOM   1455 C  CD2 . TYR   A 1 210 ? 4.967   42.299 52.958  1.00 27.74 ? 199 TYR   A CD2 1 
ATOM   1456 C  CE1 . TYR   A 1 210 ? 7.577   41.764 52.252  1.00 29.24 ? 199 TYR   A CE1 1 
ATOM   1457 C  CE2 . TYR   A 1 210 ? 5.363   42.419 51.633  1.00 28.63 ? 199 TYR   A CE2 1 
ATOM   1458 C  CZ  . TYR   A 1 210 ? 6.666   42.133 51.280  1.00 30.11 ? 199 TYR   A CZ  1 
ATOM   1459 O  OH  . TYR   A 1 210 ? 7.071   42.284 49.981  1.00 32.19 ? 199 TYR   A OH  1 
ATOM   1460 N  N   . ARG   A 1 211 ? 3.214   39.280 57.045  1.00 30.35 ? 200 ARG   A N   1 
ATOM   1461 C  CA  . ARG   A 1 211 ? 2.580   38.966 58.313  1.00 31.48 ? 200 ARG   A CA  1 
ATOM   1462 C  C   . ARG   A 1 211 ? 3.079   37.668 58.903  1.00 30.31 ? 200 ARG   A C   1 
ATOM   1463 O  O   . ARG   A 1 211 ? 3.003   36.617 58.266  1.00 30.26 ? 200 ARG   A O   1 
ATOM   1464 C  CB  . ARG   A 1 211 ? 1.046   38.998 58.183  1.00 34.76 ? 200 ARG   A CB  1 
ATOM   1465 C  CG  . ARG   A 1 211 ? 0.513   40.362 57.702  1.00 42.58 ? 200 ARG   A CG  1 
ATOM   1466 C  CD  . ARG   A 1 211 ? 1.104   41.543 58.494  1.00 49.32 ? 200 ARG   A CD  1 
ATOM   1467 N  NE  . ARG   A 1 211 ? 0.387   42.801 58.301  1.00 55.27 ? 200 ARG   A NE  1 
ATOM   1468 C  CZ  . ARG   A 1 211 ? 0.092   43.650 59.283  1.00 59.96 ? 200 ARG   A CZ  1 
ATOM   1469 N  NH1 . ARG   A 1 211 ? 0.436   43.372 60.540  1.00 60.63 ? 200 ARG   A NH1 1 
ATOM   1470 N  NH2 . ARG   A 1 211 ? -0.549  44.784 59.020  1.00 60.23 ? 200 ARG   A NH2 1 
ATOM   1471 N  N   . ALA   A 1 212 ? 3.623   37.753 60.127  1.00 29.05 ? 201 ALA   A N   1 
ATOM   1472 C  CA  . ALA   A 1 212 ? 4.134   36.612 60.888  1.00 28.25 ? 201 ALA   A CA  1 
ATOM   1473 C  C   . ALA   A 1 212 ? 3.047   35.536 61.023  1.00 28.15 ? 201 ALA   A C   1 
ATOM   1474 O  O   . ALA   A 1 212 ? 1.870   35.887 61.042  1.00 28.62 ? 201 ALA   A O   1 
ATOM   1475 C  CB  . ALA   A 1 212 ? 4.569   37.087 62.267  1.00 27.34 ? 201 ALA   A CB  1 
ATOM   1476 N  N   . PRO   A 1 213 ? 3.399   34.241 61.070  1.00 27.63 ? 202 PRO   A N   1 
ATOM   1477 C  CA  . PRO   A 1 213 ? 2.361   33.203 61.158  1.00 28.30 ? 202 PRO   A CA  1 
ATOM   1478 C  C   . PRO   A 1 213 ? 1.493   33.246 62.420  1.00 29.32 ? 202 PRO   A C   1 
ATOM   1479 O  O   . PRO   A 1 213 ? 0.330   32.861 62.335  1.00 30.34 ? 202 PRO   A O   1 
ATOM   1480 C  CB  . PRO   A 1 213 ? 3.155   31.896 61.042  1.00 28.51 ? 202 PRO   A CB  1 
ATOM   1481 C  CG  . PRO   A 1 213 ? 4.523   32.253 61.538  1.00 28.58 ? 202 PRO   A CG  1 
ATOM   1482 C  CD  . PRO   A 1 213 ? 4.749   33.645 61.033  1.00 26.88 ? 202 PRO   A CD  1 
ATOM   1483 N  N   . GLU   A 1 214 ? 2.007   33.730 63.562  1.00 28.85 ? 203 GLU   A N   1 
ATOM   1484 C  CA  . GLU   A 1 214 ? 1.174   33.862 64.765  1.00 29.31 ? 203 GLU   A CA  1 
ATOM   1485 C  C   . GLU   A 1 214 ? -0.005  34.830 64.498  1.00 30.91 ? 203 GLU   A C   1 
ATOM   1486 O  O   . GLU   A 1 214 ? -1.116  34.535 64.909  1.00 31.71 ? 203 GLU   A O   1 
ATOM   1487 C  CB  . GLU   A 1 214 ? 1.984   34.243 66.024  1.00 29.09 ? 203 GLU   A CB  1 
ATOM   1488 C  CG  . GLU   A 1 214 ? 2.664   35.599 65.993  1.00 30.38 ? 203 GLU   A CG  1 
ATOM   1489 C  CD  . GLU   A 1 214 ? 4.074   35.623 65.420  1.00 31.86 ? 203 GLU   A CD  1 
ATOM   1490 O  OE1 . GLU   A 1 214 ? 4.398   34.751 64.581  1.00 31.28 ? 203 GLU   A OE1 1 
ATOM   1491 O  OE2 . GLU   A 1 214 ? 4.855   36.528 65.803  1.00 30.65 ? 203 GLU   A OE2 1 
ATOM   1492 N  N   . LEU   A 1 215 ? 0.198   35.886 63.696  1.00 31.06 ? 204 LEU   A N   1 
ATOM   1493 C  CA  . LEU   A 1 215 ? -0.889  36.796 63.331  1.00 32.48 ? 204 LEU   A CA  1 
ATOM   1494 C  C   . LEU   A 1 215 ? -1.934  36.038 62.504  1.00 34.32 ? 204 LEU   A C   1 
ATOM   1495 O  O   . LEU   A 1 215 ? -3.131  36.226 62.713  1.00 35.32 ? 204 LEU   A O   1 
ATOM   1496 C  CB  . LEU   A 1 215 ? -0.372  37.983 62.488  1.00 32.56 ? 204 LEU   A CB  1 
ATOM   1497 C  CG  . LEU   A 1 215 ? 0.391   39.074 63.214  1.00 33.33 ? 204 LEU   A CG  1 
ATOM   1498 C  CD1 . LEU   A 1 215 ? 1.001   40.041 62.214  1.00 33.29 ? 204 LEU   A CD1 1 
ATOM   1499 C  CD2 . LEU   A 1 215 ? -0.496  39.791 64.225  1.00 33.82 ? 204 LEU   A CD2 1 
ATOM   1500 N  N   . LEU   A 1 216 ? -1.486  35.167 61.581  1.00 34.04 ? 205 LEU   A N   1 
ATOM   1501 C  CA  . LEU   A 1 216 ? -2.404  34.380 60.757  1.00 34.62 ? 205 LEU   A CA  1 
ATOM   1502 C  C   . LEU   A 1 216 ? -3.161  33.295 61.537  1.00 35.32 ? 205 LEU   A C   1 
ATOM   1503 O  O   . LEU   A 1 216 ? -4.140  32.755 61.033  1.00 35.75 ? 205 LEU   A O   1 
ATOM   1504 C  CB  . LEU   A 1 216 ? -1.674  33.766 59.568  1.00 34.63 ? 205 LEU   A CB  1 
ATOM   1505 C  CG  . LEU   A 1 216 ? -0.891  34.760 58.729  1.00 35.39 ? 205 LEU   A CG  1 
ATOM   1506 C  CD1 . LEU   A 1 216 ? 0.054   34.048 57.797  1.00 35.38 ? 205 LEU   A CD1 1 
ATOM   1507 C  CD2 . LEU   A 1 216 ? -1.819  35.693 58.000  1.00 36.10 ? 205 LEU   A CD2 1 
ATOM   1508 N  N   . LEU   A 1 217 ? -2.696  32.960 62.745  1.00 35.07 ? 206 LEU   A N   1 
ATOM   1509 C  CA  . LEU   A 1 217 ? -3.330  31.985 63.613  1.00 35.39 ? 206 LEU   A CA  1 
ATOM   1510 C  C   . LEU   A 1 217 ? -4.115  32.615 64.782  1.00 36.47 ? 206 LEU   A C   1 
ATOM   1511 O  O   . LEU   A 1 217 ? -4.458  31.915 65.729  1.00 37.01 ? 206 LEU   A O   1 
ATOM   1512 C  CB  . LEU   A 1 217 ? -2.292  30.993 64.143  1.00 35.17 ? 206 LEU   A CB  1 
ATOM   1513 C  CG  . LEU   A 1 217 ? -1.628  30.112 63.098  1.00 35.97 ? 206 LEU   A CG  1 
ATOM   1514 C  CD1 . LEU   A 1 217 ? -0.507  29.314 63.715  1.00 36.37 ? 206 LEU   A CD1 1 
ATOM   1515 C  CD2 . LEU   A 1 217 ? -2.646  29.204 62.412  1.00 36.09 ? 206 LEU   A CD2 1 
ATOM   1516 N  N   . GLY   A 1 218 ? -4.397  33.908 64.715  1.00 37.01 ? 207 GLY   A N   1 
ATOM   1517 C  CA  . GLY   A 1 218 ? -5.211  34.576 65.719  1.00 37.73 ? 207 GLY   A CA  1 
ATOM   1518 C  C   . GLY   A 1 218 ? -4.529  35.240 66.891  1.00 38.99 ? 207 GLY   A C   1 
ATOM   1519 O  O   . GLY   A 1 218 ? -5.206  35.548 67.875  1.00 39.34 ? 207 GLY   A O   1 
ATOM   1520 N  N   . ALA   A 1 219 ? -3.212  35.541 66.816  1.00 39.61 ? 208 ALA   A N   1 
ATOM   1521 C  CA  . ALA   A 1 219 ? -2.527  36.255 67.906  1.00 41.15 ? 208 ALA   A CA  1 
ATOM   1522 C  C   . ALA   A 1 219 ? -3.237  37.589 68.176  1.00 42.59 ? 208 ALA   A C   1 
ATOM   1523 O  O   . ALA   A 1 219 ? -3.625  38.269 67.227  1.00 42.04 ? 208 ALA   A O   1 
ATOM   1524 C  CB  . ALA   A 1 219 ? -1.070  36.507 67.560  1.00 41.35 ? 208 ALA   A CB  1 
ATOM   1525 N  N   . ARG   A 1 220 ? -3.539  37.856 69.452  1.00 44.37 ? 209 ARG   A N   1 
ATOM   1526 C  CA  . ARG   A 1 220 ? -4.328  39.010 69.884  1.00 46.51 ? 209 ARG   A CA  1 
ATOM   1527 C  C   . ARG   A 1 220 ? -3.540  40.298 70.040  1.00 47.44 ? 209 ARG   A C   1 
ATOM   1528 O  O   . ARG   A 1 220 ? -4.150  41.335 70.291  1.00 48.24 ? 209 ARG   A O   1 
ATOM   1529 C  CB  . ARG   A 1 220 ? -5.044  38.717 71.214  1.00 49.24 ? 209 ARG   A CB  1 
ATOM   1530 C  CG  . ARG   A 1 220 ? -5.566  37.285 71.384  1.00 54.82 ? 209 ARG   A CG  1 
ATOM   1531 C  CD  . ARG   A 1 220 ? -6.911  37.072 70.703  1.00 59.92 ? 209 ARG   A CD  1 
ATOM   1532 N  NE  . ARG   A 1 220 ? -7.623  35.919 71.266  1.00 63.56 ? 209 ARG   A NE  1 
ATOM   1533 C  CZ  . ARG   A 1 220 ? -8.658  35.320 70.687  1.00 66.18 ? 209 ARG   A CZ  1 
ATOM   1534 N  NH1 . ARG   A 1 220 ? -9.109  35.744 69.512  1.00 65.93 ? 209 ARG   A NH1 1 
ATOM   1535 N  NH2 . ARG   A 1 220 ? -9.242  34.281 71.270  1.00 66.56 ? 209 ARG   A NH2 1 
ATOM   1536 N  N   . HIS   A 1 221 ? -2.202  40.245 69.973  1.00 46.91 ? 210 HIS   A N   1 
ATOM   1537 C  CA  . HIS   A 1 221 ? -1.404  41.452 70.151  1.00 46.76 ? 210 HIS   A CA  1 
ATOM   1538 C  C   . HIS   A 1 221 ? -0.225  41.519 69.205  1.00 44.92 ? 210 HIS   A C   1 
ATOM   1539 O  O   . HIS   A 1 221 ? 0.319   40.492 68.790  1.00 44.98 ? 210 HIS   A O   1 
ATOM   1540 C  CB  . HIS   A 1 221 ? -0.902  41.582 71.609  1.00 48.53 ? 210 HIS   A CB  1 
ATOM   1541 C  CG  . HIS   A 1 221 ? -1.958  41.357 72.645  1.00 52.24 ? 210 HIS   A CG  1 
ATOM   1542 N  ND1 . HIS   A 1 221 ? -3.061  42.187 72.743  1.00 54.49 ? 210 HIS   A ND1 1 
ATOM   1543 C  CD2 . HIS   A 1 221 ? -2.054  40.391 73.585  1.00 53.78 ? 210 HIS   A CD2 1 
ATOM   1544 C  CE1 . HIS   A 1 221 ? -3.788  41.706 73.737  1.00 55.04 ? 210 HIS   A CE1 1 
ATOM   1545 N  NE2 . HIS   A 1 221 ? -3.221  40.629 74.278  1.00 55.11 ? 210 HIS   A NE2 1 
ATOM   1546 N  N   . TYR   A 1 222 ? 0.185   42.743 68.882  1.00 43.00 ? 211 TYR   A N   1 
ATOM   1547 C  CA  . TYR   A 1 222 ? 1.384   42.949 68.098  1.00 41.49 ? 211 TYR   A CA  1 
ATOM   1548 C  C   . TYR   A 1 222 ? 2.554   42.878 69.067  1.00 38.76 ? 211 TYR   A C   1 
ATOM   1549 O  O   . TYR   A 1 222 ? 2.449   43.302 70.221  1.00 38.27 ? 211 TYR   A O   1 
ATOM   1550 C  CB  . TYR   A 1 222 ? 1.352   44.296 67.376  1.00 42.21 ? 211 TYR   A CB  1 
ATOM   1551 C  CG  . TYR   A 1 222 ? 0.418   44.278 66.195  1.00 44.24 ? 211 TYR   A CG  1 
ATOM   1552 C  CD1 . TYR   A 1 222 ? 0.841   43.820 64.954  1.00 45.68 ? 211 TYR   A CD1 1 
ATOM   1553 C  CD2 . TYR   A 1 222 ? -0.906  44.669 66.326  1.00 45.98 ? 211 TYR   A CD2 1 
ATOM   1554 C  CE1 . TYR   A 1 222 ? -0.020  43.792 63.863  1.00 47.30 ? 211 TYR   A CE1 1 
ATOM   1555 C  CE2 . TYR   A 1 222 ? -1.776  44.645 65.244  1.00 47.57 ? 211 TYR   A CE2 1 
ATOM   1556 C  CZ  . TYR   A 1 222 ? -1.333  44.197 64.016  1.00 49.08 ? 211 TYR   A CZ  1 
ATOM   1557 O  OH  . TYR   A 1 222 ? -2.205  44.174 62.952  1.00 52.23 ? 211 TYR   A OH  1 
ATOM   1558 N  N   . THR   A 1 223 ? 3.661   42.304 68.609  1.00 36.71 ? 212 THR   A N   1 
ATOM   1559 C  CA  . THR   A 1 223 ? 4.872   42.146 69.406  1.00 35.08 ? 212 THR   A CA  1 
ATOM   1560 C  C   . THR   A 1 223 ? 6.093   42.622 68.587  1.00 33.25 ? 212 THR   A C   1 
ATOM   1561 O  O   . THR   A 1 223 ? 5.979   42.870 67.381  1.00 34.17 ? 212 THR   A O   1 
ATOM   1562 C  CB  . THR   A 1 223 ? 5.029   40.651 69.766  1.00 36.10 ? 212 THR   A CB  1 
ATOM   1563 O  OG1 . THR   A 1 223 ? 5.229   39.921 68.540  1.00 37.38 ? 212 THR   A OG1 1 
ATOM   1564 C  CG2 . THR   A 1 223 ? 3.849   40.102 70.558  1.00 35.50 ? 212 THR   A CG2 1 
ATOM   1565 N  N   . LYS   A 1 224 ? 7.267   42.702 69.222  1.00 30.48 ? 213 LYS   A N   1 
ATOM   1566 C  CA  . LYS   A 1 224 ? 8.502   43.013 68.534  1.00 29.00 ? 213 LYS   A CA  1 
ATOM   1567 C  C   . LYS   A 1 224 ? 8.826   41.910 67.507  1.00 28.01 ? 213 LYS   A C   1 
ATOM   1568 O  O   . LYS   A 1 224 ? 9.328   42.199 66.426  1.00 28.06 ? 213 LYS   A O   1 
ATOM   1569 C  CB  . LYS   A 1 224 ? 9.633   43.107 69.560  1.00 30.34 ? 213 LYS   A CB  1 
ATOM   1570 C  CG  . LYS   A 1 224 ? 9.516   44.324 70.445  1.00 34.46 ? 213 LYS   A CG  1 
ATOM   1571 C  CD  . LYS   A 1 224 ? 10.615  44.416 71.489  1.00 38.77 ? 213 LYS   A CD  1 
ATOM   1572 C  CE  . LYS   A 1 224 ? 10.372  45.639 72.343  1.00 42.92 ? 213 LYS   A CE  1 
ATOM   1573 N  NZ  . LYS   A 1 224 ? 11.306  45.722 73.491  1.00 46.13 ? 213 LYS   A NZ  1 
ATOM   1574 N  N   . ALA   A 1 225 ? 8.519   40.646 67.847  1.00 27.08 ? 214 ALA   A N   1 
ATOM   1575 C  CA  . ALA   A 1 225 ? 8.762   39.482 67.003  1.00 26.34 ? 214 ALA   A CA  1 
ATOM   1576 C  C   . ALA   A 1 225 ? 8.044   39.564 65.660  1.00 25.51 ? 214 ALA   A C   1 
ATOM   1577 O  O   . ALA   A 1 225 ? 8.588   39.108 64.657  1.00 25.35 ? 214 ALA   A O   1 
ATOM   1578 C  CB  . ALA   A 1 225 ? 8.389   38.209 67.741  1.00 25.85 ? 214 ALA   A CB  1 
ATOM   1579 N  N   . ILE   A 1 226 ? 6.874   40.201 65.627  1.00 24.76 ? 215 ILE   A N   1 
ATOM   1580 C  CA  . ILE   A 1 226 ? 6.096   40.378 64.408  1.00 25.06 ? 215 ILE   A CA  1 
ATOM   1581 C  C   . ILE   A 1 226 ? 6.851   41.295 63.431  1.00 24.94 ? 215 ILE   A C   1 
ATOM   1582 O  O   . ILE   A 1 226 ? 6.904   40.995 62.230  1.00 24.72 ? 215 ILE   A O   1 
ATOM   1583 C  CB  . ILE   A 1 226 ? 4.679   40.857 64.784  1.00 26.08 ? 215 ILE   A CB  1 
ATOM   1584 C  CG1 . ILE   A 1 226 ? 3.845   39.667 65.244  1.00 26.73 ? 215 ILE   A CG1 1 
ATOM   1585 C  CG2 . ILE   A 1 226 ? 3.971   41.602 63.644  1.00 27.33 ? 215 ILE   A CG2 1 
ATOM   1586 C  CD1 . ILE   A 1 226 ? 2.720   40.031 66.040  1.00 28.01 ? 215 ILE   A CD1 1 
ATOM   1587 N  N   . ASP   A 1 227 ? 7.508   42.354 63.965  1.00 23.93 ? 216 ASP   A N   1 
ATOM   1588 C  CA  . ASP   A 1 227 ? 8.322   43.259 63.158  1.00 24.40 ? 216 ASP   A CA  1 
ATOM   1589 C  C   . ASP   A 1 227 ? 9.544   42.518 62.633  1.00 24.59 ? 216 ASP   A C   1 
ATOM   1590 O  O   . ASP   A 1 227 ? 9.897   42.704 61.471  1.00 25.04 ? 216 ASP   A O   1 
ATOM   1591 C  CB  . ASP   A 1 227 ? 8.796   44.481 63.962  1.00 24.77 ? 216 ASP   A CB  1 
ATOM   1592 C  CG  . ASP   A 1 227 ? 7.758   45.539 64.288  1.00 26.11 ? 216 ASP   A CG  1 
ATOM   1593 O  OD1 . ASP   A 1 227 ? 6.681   45.538 63.647  1.00 26.33 ? 216 ASP   A OD1 1 
ATOM   1594 O  OD2 . ASP   A 1 227 ? 8.031   46.385 65.181  1.00 25.05 ? 216 ASP   A OD2 1 
ATOM   1595 N  N   . ILE   A 1 228 ? 10.191  41.694 63.488  1.00 24.07 ? 217 ILE   A N   1 
ATOM   1596 C  CA  . ILE   A 1 228 ? 11.363  40.892 63.130  1.00 24.01 ? 217 ILE   A CA  1 
ATOM   1597 C  C   . ILE   A 1 228 ? 11.071  39.933 61.978  1.00 24.43 ? 217 ILE   A C   1 
ATOM   1598 O  O   . ILE   A 1 228 ? 11.866  39.876 61.034  1.00 25.50 ? 217 ILE   A O   1 
ATOM   1599 C  CB  . ILE   A 1 228 ? 11.987  40.179 64.347  1.00 23.98 ? 217 ILE   A CB  1 
ATOM   1600 C  CG1 . ILE   A 1 228 ? 12.487  41.203 65.403  1.00 25.04 ? 217 ILE   A CG1 1 
ATOM   1601 C  CG2 . ILE   A 1 228 ? 13.088  39.222 63.913  1.00 23.69 ? 217 ILE   A CG2 1 
ATOM   1602 C  CD1 . ILE   A 1 228 ? 13.432  42.248 64.853  1.00 26.59 ? 217 ILE   A CD1 1 
ATOM   1603 N  N   . TRP   A 1 229 ? 9.912   39.247 61.996  1.00 23.76 ? 218 TRP   A N   1 
ATOM   1604 C  CA  . TRP   A 1 229 ? 9.484   38.385 60.887  1.00 23.96 ? 218 TRP   A CA  1 
ATOM   1605 C  C   . TRP   A 1 229 ? 9.387   39.188 59.594  1.00 24.26 ? 218 TRP   A C   1 
ATOM   1606 O  O   . TRP   A 1 229 ? 9.831   38.715 58.556  1.00 24.63 ? 218 TRP   A O   1 
ATOM   1607 C  CB  . TRP   A 1 229 ? 8.111   37.751 61.171  1.00 24.15 ? 218 TRP   A CB  1 
ATOM   1608 C  CG  . TRP   A 1 229 ? 7.612   36.872 60.064  1.00 25.09 ? 218 TRP   A CG  1 
ATOM   1609 C  CD1 . TRP   A 1 229 ? 6.892   37.252 58.965  1.00 26.02 ? 218 TRP   A CD1 1 
ATOM   1610 C  CD2 . TRP   A 1 229 ? 7.848   35.464 59.922  1.00 25.64 ? 218 TRP   A CD2 1 
ATOM   1611 N  NE1 . TRP   A 1 229 ? 6.667   36.168 58.147  1.00 26.19 ? 218 TRP   A NE1 1 
ATOM   1612 C  CE2 . TRP   A 1 229 ? 7.214   35.050 58.732  1.00 26.23 ? 218 TRP   A CE2 1 
ATOM   1613 C  CE3 . TRP   A 1 229 ? 8.529   34.512 60.687  1.00 26.10 ? 218 TRP   A CE3 1 
ATOM   1614 C  CZ2 . TRP   A 1 229 ? 7.221   33.726 58.314  1.00 26.89 ? 218 TRP   A CZ2 1 
ATOM   1615 C  CZ3 . TRP   A 1 229 ? 8.577   33.211 60.235  1.00 26.79 ? 218 TRP   A CZ3 1 
ATOM   1616 C  CH2 . TRP   A 1 229 ? 7.931   32.832 59.062  1.00 26.90 ? 218 TRP   A CH2 1 
ATOM   1617 N  N   . ALA   A 1 230 ? 8.808   40.402 59.650  1.00 24.62 ? 219 ALA   A N   1 
ATOM   1618 C  CA  . ALA   A 1 230 ? 8.662   41.264 58.473  1.00 24.67 ? 219 ALA   A CA  1 
ATOM   1619 C  C   . ALA   A 1 230 ? 10.023  41.653 57.909  1.00 24.70 ? 219 ALA   A C   1 
ATOM   1620 O  O   . ALA   A 1 230 ? 10.194  41.648 56.687  1.00 25.23 ? 219 ALA   A O   1 
ATOM   1621 C  CB  . ALA   A 1 230 ? 7.848   42.497 58.818  1.00 24.37 ? 219 ALA   A CB  1 
ATOM   1622 N  N   . ILE   A 1 231 ? 11.006  41.919 58.787  1.00 24.36 ? 220 ILE   A N   1 
ATOM   1623 C  CA  . ILE   A 1 231 ? 12.382  42.231 58.380  1.00 24.98 ? 220 ILE   A CA  1 
ATOM   1624 C  C   . ILE   A 1 231 ? 13.018  41.017 57.685  1.00 26.40 ? 220 ILE   A C   1 
ATOM   1625 O  O   . ILE   A 1 231 ? 13.741  41.179 56.702  1.00 26.76 ? 220 ILE   A O   1 
ATOM   1626 C  CB  . ILE   A 1 231 ? 13.232  42.736 59.576  1.00 24.77 ? 220 ILE   A CB  1 
ATOM   1627 C  CG1 . ILE   A 1 231 ? 12.723  44.097 60.068  1.00 24.54 ? 220 ILE   A CG1 1 
ATOM   1628 C  CG2 . ILE   A 1 231 ? 14.710  42.821 59.212  1.00 25.19 ? 220 ILE   A CG2 1 
ATOM   1629 C  CD1 . ILE   A 1 231 ? 13.246  44.493 61.334  1.00 24.60 ? 220 ILE   A CD1 1 
ATOM   1630 N  N   . GLY   A 1 232 ? 12.715  39.813 58.179  1.00 26.57 ? 221 GLY   A N   1 
ATOM   1631 C  CA  . GLY   A 1 232 ? 13.164  38.578 57.560  1.00 27.05 ? 221 GLY   A CA  1 
ATOM   1632 C  C   . GLY   A 1 232 ? 12.575  38.427 56.170  1.00 27.37 ? 221 GLY   A C   1 
ATOM   1633 O  O   . GLY   A 1 232 ? 13.293  38.053 55.237  1.00 27.98 ? 221 GLY   A O   1 
ATOM   1634 N  N   . CYS   A 1 233 ? 11.275  38.768 55.987  1.00 26.75 ? 222 CYS   A N   1 
ATOM   1635 C  CA  . CYS   A 1 233 ? 10.666  38.696 54.640  1.00 26.71 ? 222 CYS   A CA  1 
ATOM   1636 C  C   . CYS   A 1 233 ? 11.362  39.663 53.698  1.00 26.89 ? 222 CYS   A C   1 
ATOM   1637 O  O   . CYS   A 1 233 ? 11.559  39.341 52.530  1.00 27.08 ? 222 CYS   A O   1 
ATOM   1638 C  CB  . CYS   A 1 233 ? 9.166   38.981 54.677  1.00 26.31 ? 222 CYS   A CB  1 
ATOM   1639 S  SG  . CYS   A 1 233 ? 8.202   37.877 55.735  1.00 27.09 ? 222 CYS   A SG  1 
ATOM   1640 N  N   . ILE   A 1 234 ? 11.660  40.882 54.189  1.00 26.63 ? 223 ILE   A N   1 
ATOM   1641 C  CA  . ILE   A 1 234 ? 12.300  41.907 53.378  1.00 26.29 ? 223 ILE   A CA  1 
ATOM   1642 C  C   . ILE   A 1 234 ? 13.707  41.472 52.986  1.00 26.42 ? 223 ILE   A C   1 
ATOM   1643 O  O   . ILE   A 1 234 ? 14.064  41.587 51.815  1.00 26.46 ? 223 ILE   A O   1 
ATOM   1644 C  CB  . ILE   A 1 234 ? 12.290  43.259 54.116  1.00 26.15 ? 223 ILE   A CB  1 
ATOM   1645 C  CG1 . ILE   A 1 234 ? 10.848  43.807 54.292  1.00 26.54 ? 223 ILE   A CG1 1 
ATOM   1646 C  CG2 . ILE   A 1 234 ? 13.183  44.282 53.441  1.00 26.06 ? 223 ILE   A CG2 1 
ATOM   1647 C  CD1 . ILE   A 1 234 ? 10.759  44.952 55.424  1.00 25.93 ? 223 ILE   A CD1 1 
ATOM   1648 N  N   . PHE   A 1 235 ? 14.496  40.954 53.950  1.00 25.87 ? 224 PHE   A N   1 
ATOM   1649 C  CA  . PHE   A 1 235 ? 15.858  40.471 53.726  1.00 26.04 ? 224 PHE   A CA  1 
ATOM   1650 C  C   . PHE   A 1 235 ? 15.881  39.411 52.628  1.00 27.14 ? 224 PHE   A C   1 
ATOM   1651 O  O   . PHE   A 1 235 ? 16.590  39.594 51.646  1.00 28.13 ? 224 PHE   A O   1 
ATOM   1652 C  CB  . PHE   A 1 235 ? 16.488  39.962 55.031  1.00 25.28 ? 224 PHE   A CB  1 
ATOM   1653 C  CG  . PHE   A 1 235 ? 17.924  39.507 54.912  1.00 25.12 ? 224 PHE   A CG  1 
ATOM   1654 C  CD1 . PHE   A 1 235 ? 18.788  40.099 53.995  1.00 25.71 ? 224 PHE   A CD1 1 
ATOM   1655 C  CD2 . PHE   A 1 235 ? 18.433  38.535 55.761  1.00 24.86 ? 224 PHE   A CD2 1 
ATOM   1656 C  CE1 . PHE   A 1 235 ? 20.116  39.687 53.900  1.00 25.89 ? 224 PHE   A CE1 1 
ATOM   1657 C  CE2 . PHE   A 1 235 ? 19.759  38.125 55.658  1.00 25.20 ? 224 PHE   A CE2 1 
ATOM   1658 C  CZ  . PHE   A 1 235 ? 20.595  38.713 54.739  1.00 25.03 ? 224 PHE   A CZ  1 
ATOM   1659 N  N   . ALA   A 1 236 ? 15.037  38.376 52.727  1.00 27.31 ? 225 ALA   A N   1 
ATOM   1660 C  CA  . ALA   A 1 236 ? 14.905  37.330 51.703  1.00 27.50 ? 225 ALA   A CA  1 
ATOM   1661 C  C   . ALA   A 1 236 ? 14.554  37.945 50.335  1.00 28.45 ? 225 ALA   A C   1 
ATOM   1662 O  O   . ALA   A 1 236 ? 15.140  37.569 49.315  1.00 29.71 ? 225 ALA   A O   1 
ATOM   1663 C  CB  . ALA   A 1 236 ? 13.826  36.340 52.118  1.00 27.32 ? 225 ALA   A CB  1 
ATOM   1664 N  N   . GLU   A 1 237 ? 13.635  38.920 50.311  1.00 27.49 ? 226 GLU   A N   1 
ATOM   1665 C  CA  . GLU   A 1 237 ? 13.234  39.573 49.077  1.00 27.84 ? 226 GLU   A CA  1 
ATOM   1666 C  C   . GLU   A 1 237 ? 14.381  40.415 48.492  1.00 28.25 ? 226 GLU   A C   1 
ATOM   1667 O  O   . GLU   A 1 237 ? 14.506  40.485 47.278  1.00 29.18 ? 226 GLU   A O   1 
ATOM   1668 C  CB  . GLU   A 1 237 ? 12.005  40.443 49.330  1.00 30.21 ? 226 GLU   A CB  1 
ATOM   1669 C  CG  . GLU   A 1 237 ? 11.340  41.010 48.086  1.00 33.16 ? 226 GLU   A CG  1 
ATOM   1670 C  CD  . GLU   A 1 237 ? 9.927   41.504 48.337  1.00 39.01 ? 226 GLU   A CD  1 
ATOM   1671 O  OE1 . GLU   A 1 237 ? 9.386   41.274 49.445  1.00 42.01 ? 226 GLU   A OE1 1 
ATOM   1672 O  OE2 . GLU   A 1 237 ? 9.352   42.123 47.419  1.00 40.24 ? 226 GLU   A OE2 1 
ATOM   1673 N  N   . LEU   A 1 238 ? 15.239  41.010 49.333  1.00 27.20 ? 227 LEU   A N   1 
ATOM   1674 C  CA  . LEU   A 1 238 ? 16.386  41.767 48.850  1.00 27.45 ? 227 LEU   A CA  1 
ATOM   1675 C  C   . LEU   A 1 238 ? 17.411  40.821 48.192  1.00 28.37 ? 227 LEU   A C   1 
ATOM   1676 O  O   . LEU   A 1 238 ? 18.029  41.177 47.181  1.00 28.04 ? 227 LEU   A O   1 
ATOM   1677 C  CB  . LEU   A 1 238 ? 17.031  42.555 50.002  1.00 27.09 ? 227 LEU   A CB  1 
ATOM   1678 C  CG  . LEU   A 1 238 ? 16.214  43.749 50.495  1.00 27.62 ? 227 LEU   A CG  1 
ATOM   1679 C  CD1 . LEU   A 1 238 ? 16.776  44.303 51.787  1.00 28.05 ? 227 LEU   A CD1 1 
ATOM   1680 C  CD2 . LEU   A 1 238 ? 16.091  44.812 49.414  1.00 27.74 ? 227 LEU   A CD2 1 
ATOM   1681 N  N   . LEU   A 1 239 ? 17.585  39.616 48.766  1.00 28.83 ? 228 LEU   A N   1 
ATOM   1682 C  CA  . LEU   A 1 239 ? 18.505  38.619 48.235  1.00 29.77 ? 228 LEU   A CA  1 
ATOM   1683 C  C   . LEU   A 1 239 ? 17.998  37.959 46.926  1.00 31.42 ? 228 LEU   A C   1 
ATOM   1684 O  O   . LEU   A 1 239 ? 18.812  37.641 46.070  1.00 32.64 ? 228 LEU   A O   1 
ATOM   1685 C  CB  . LEU   A 1 239 ? 18.725  37.527 49.277  1.00 29.67 ? 228 LEU   A CB  1 
ATOM   1686 C  CG  . LEU   A 1 239 ? 19.444  37.941 50.569  1.00 30.18 ? 228 LEU   A CG  1 
ATOM   1687 C  CD1 . LEU   A 1 239 ? 19.236  36.900 51.654  1.00 29.93 ? 228 LEU   A CD1 1 
ATOM   1688 C  CD2 . LEU   A 1 239 ? 20.942  38.223 50.318  1.00 30.04 ? 228 LEU   A CD2 1 
ATOM   1689 N  N   . THR   A 1 240 ? 16.681  37.773 46.752  1.00 31.25 ? 229 THR   A N   1 
ATOM   1690 C  CA  . THR   A 1 240 ? 16.151  37.037 45.586  1.00 31.61 ? 229 THR   A CA  1 
ATOM   1691 C  C   . THR   A 1 240 ? 15.353  37.862 44.568  1.00 32.76 ? 229 THR   A C   1 
ATOM   1692 O  O   . THR   A 1 240 ? 15.057  37.354 43.484  1.00 33.81 ? 229 THR   A O   1 
ATOM   1693 C  CB  . THR   A 1 240 ? 15.229  35.891 46.092  1.00 31.85 ? 229 THR   A CB  1 
ATOM   1694 O  OG1 . THR   A 1 240 ? 14.008  36.467 46.570  1.00 32.91 ? 229 THR   A OG1 1 
ATOM   1695 C  CG2 . THR   A 1 240 ? 15.859  35.059 47.233  1.00 31.46 ? 229 THR   A CG2 1 
ATOM   1696 N  N   . SER   A 1 241 ? 14.900  39.059 44.972  1.00 32.75 ? 230 SER   A N   1 
ATOM   1697 C  CA  . SER   A 1 241 ? 14.028  39.994 44.237  1.00 33.63 ? 230 SER   A CA  1 
ATOM   1698 C  C   . SER   A 1 241 ? 12.572  39.563 44.176  1.00 34.32 ? 230 SER   A C   1 
ATOM   1699 O  O   . SER   A 1 241 ? 11.795  40.160 43.431  1.00 34.91 ? 230 SER   A O   1 
ATOM   1700 C  CB  . SER   A 1 241 ? 14.542  40.275 42.830  1.00 34.93 ? 230 SER   A CB  1 
ATOM   1701 O  OG  . SER   A 1 241 ? 15.905  40.658 42.880  1.00 37.77 ? 230 SER   A OG  1 
ATOM   1702 N  N   . GLU   A 1 242 ? 12.203  38.529 44.938  1.00 33.93 ? 231 GLU   A N   1 
ATOM   1703 C  CA  . GLU   A 1 242 ? 10.880  37.934 44.938  1.00 34.49 ? 231 GLU   A CA  1 
ATOM   1704 C  C   . GLU   A 1 242 ? 10.361  37.957 46.371  1.00 33.46 ? 231 GLU   A C   1 
ATOM   1705 O  O   . GLU   A 1 242 ? 11.114  37.631 47.300  1.00 32.75 ? 231 GLU   A O   1 
ATOM   1706 C  CB  . GLU   A 1 242 ? 11.023  36.452 44.527  1.00 38.63 ? 231 GLU   A CB  1 
ATOM   1707 C  CG  . GLU   A 1 242 ? 10.315  36.050 43.245  1.00 48.08 ? 231 GLU   A CG  1 
ATOM   1708 C  CD  . GLU   A 1 242 ? 11.015  36.497 41.981  1.00 58.57 ? 231 GLU   A CD  1 
ATOM   1709 O  OE1 . GLU   A 1 242 ? 12.266  36.580 41.992  1.00 61.60 ? 231 GLU   A OE1 1 
ATOM   1710 O  OE2 . GLU   A 1 242 ? 10.315  36.760 40.977  1.00 62.16 ? 231 GLU   A OE2 1 
ATOM   1711 N  N   . PRO   A 1 243 ? 9.057   38.231 46.571  1.00 32.79 ? 232 PRO   A N   1 
ATOM   1712 C  CA  . PRO   A 1 243 ? 8.506   38.164 47.928  1.00 32.15 ? 232 PRO   A CA  1 
ATOM   1713 C  C   . PRO   A 1 243 ? 8.492   36.706 48.350  1.00 31.17 ? 232 PRO   A C   1 
ATOM   1714 O  O   . PRO   A 1 243 ? 7.907   35.872 47.652  1.00 31.41 ? 232 PRO   A O   1 
ATOM   1715 C  CB  . PRO   A 1 243 ? 7.091   38.743 47.771  1.00 32.99 ? 232 PRO   A CB  1 
ATOM   1716 C  CG  . PRO   A 1 243 ? 7.092   39.434 46.425  1.00 33.64 ? 232 PRO   A CG  1 
ATOM   1717 C  CD  . PRO   A 1 243 ? 8.013   38.589 45.592  1.00 32.29 ? 232 PRO   A CD  1 
ATOM   1718 N  N   . ILE   A 1 244 ? 9.222   36.375 49.419  1.00 29.95 ? 233 ILE   A N   1 
ATOM   1719 C  CA  . ILE   A 1 244 ? 9.355   34.986 49.848  1.00 29.30 ? 233 ILE   A CA  1 
ATOM   1720 C  C   . ILE   A 1 244 ? 8.002   34.316 50.109  1.00 29.68 ? 233 ILE   A C   1 
ATOM   1721 O  O   . ILE   A 1 244 ? 7.794   33.182 49.674  1.00 30.04 ? 233 ILE   A O   1 
ATOM   1722 C  CB  . ILE   A 1 244 ? 10.333  34.835 51.042  1.00 28.79 ? 233 ILE   A CB  1 
ATOM   1723 C  CG1 . ILE   A 1 244 ? 10.599  33.355 51.342  1.00 29.41 ? 233 ILE   A CG1 1 
ATOM   1724 C  CG2 . ILE   A 1 244 ? 9.855   35.603 52.278  1.00 28.70 ? 233 ILE   A CG2 1 
ATOM   1725 C  CD1 . ILE   A 1 244 ? 11.631  33.095 52.411  1.00 30.40 ? 233 ILE   A CD1 1 
ATOM   1726 N  N   . PHE   A 1 245 ? 7.065   35.040 50.725  1.00 29.44 ? 234 PHE   A N   1 
ATOM   1727 C  CA  . PHE   A 1 245 ? 5.762   34.467 51.015  1.00 29.89 ? 234 PHE   A CA  1 
ATOM   1728 C  C   . PHE   A 1 245 ? 4.685   35.041 50.096  1.00 31.86 ? 234 PHE   A C   1 
ATOM   1729 O  O   . PHE   A 1 245 ? 3.540   35.238 50.512  1.00 31.59 ? 234 PHE   A O   1 
ATOM   1730 C  CB  . PHE   A 1 245 ? 5.435   34.593 52.504  1.00 28.59 ? 234 PHE   A CB  1 
ATOM   1731 C  CG  . PHE   A 1 245 ? 6.508   33.968 53.376  1.00 27.74 ? 234 PHE   A CG  1 
ATOM   1732 C  CD1 . PHE   A 1 245 ? 6.861   32.634 53.223  1.00 27.73 ? 234 PHE   A CD1 1 
ATOM   1733 C  CD2 . PHE   A 1 245 ? 7.183   34.721 54.323  1.00 27.76 ? 234 PHE   A CD2 1 
ATOM   1734 C  CE1 . PHE   A 1 245 ? 7.851   32.061 54.020  1.00 28.21 ? 234 PHE   A CE1 1 
ATOM   1735 C  CE2 . PHE   A 1 245 ? 8.184   34.149 55.110  1.00 28.33 ? 234 PHE   A CE2 1 
ATOM   1736 C  CZ  . PHE   A 1 245 ? 8.507   32.821 54.961  1.00 27.89 ? 234 PHE   A CZ  1 
ATOM   1737 N  N   . HIS   A 1 246 ? 5.038   35.230 48.804  1.00 33.32 ? 235 HIS   A N   1 
ATOM   1738 C  CA  . HIS   A 1 246 ? 4.114   35.715 47.786  1.00 36.41 ? 235 HIS   A CA  1 
ATOM   1739 C  C   . HIS   A 1 246 ? 2.898   34.795 47.719  1.00 37.77 ? 235 HIS   A C   1 
ATOM   1740 O  O   . HIS   A 1 246 ? 3.049   33.592 47.735  1.00 37.68 ? 235 HIS   A O   1 
ATOM   1741 C  CB  . HIS   A 1 246 ? 4.771   35.807 46.395  1.00 38.65 ? 235 HIS   A CB  1 
ATOM   1742 C  CG  . HIS   A 1 246 ? 3.773   36.132 45.336  1.00 43.54 ? 235 HIS   A CG  1 
ATOM   1743 N  ND1 . HIS   A 1 246 ? 3.061   35.133 44.686  1.00 46.77 ? 235 HIS   A ND1 1 
ATOM   1744 C  CD2 . HIS   A 1 246 ? 3.289   37.335 44.950  1.00 45.46 ? 235 HIS   A CD2 1 
ATOM   1745 C  CE1 . HIS   A 1 246 ? 2.217   35.763 43.880  1.00 47.77 ? 235 HIS   A CE1 1 
ATOM   1746 N  NE2 . HIS   A 1 246 ? 2.316   37.090 44.010  1.00 47.51 ? 235 HIS   A NE2 1 
ATOM   1747 N  N   . CYS   A 1 247 ? 1.723   35.373 47.602  1.00 38.99 ? 236 CYS   A N   1 
ATOM   1748 C  CA  . CYS   A 1 247 ? 0.486   34.644 47.689  1.00 40.99 ? 236 CYS   A CA  1 
ATOM   1749 C  C   . CYS   A 1 247 ? -0.623  35.390 46.920  1.00 42.75 ? 236 CYS   A C   1 
ATOM   1750 O  O   . CYS   A 1 247 ? -0.585  36.620 46.828  1.00 42.87 ? 236 CYS   A O   1 
ATOM   1751 C  CB  . CYS   A 1 247 ? 0.154   34.541 49.178  1.00 42.16 ? 236 CYS   A CB  1 
ATOM   1752 S  SG  . CYS   A 1 247 ? -1.370  33.666 49.546  1.00 49.37 ? 236 CYS   A SG  1 
ATOM   1753 N  N   . ARG   A 1 248 ? -1.637  34.669 46.428  1.00 44.10 ? 237 ARG   A N   1 
ATOM   1754 C  CA  . ARG   A 1 248 ? -2.760  35.307 45.738  1.00 46.47 ? 237 ARG   A CA  1 
ATOM   1755 C  C   . ARG   A 1 248 ? -3.636  36.114 46.704  1.00 48.51 ? 237 ARG   A C   1 
ATOM   1756 O  O   . ARG   A 1 248 ? -3.673  35.831 47.906  1.00 48.25 ? 237 ARG   A O   1 
ATOM   1757 C  CB  . ARG   A 1 248 ? -3.623  34.274 45.011  1.00 48.63 ? 237 ARG   A CB  1 
ATOM   1758 C  CG  . ARG   A 1 248 ? -4.269  33.264 45.948  1.00 53.01 ? 237 ARG   A CG  1 
ATOM   1759 C  CD  . ARG   A 1 248 ? -5.071  32.228 45.187  1.00 57.50 ? 237 ARG   A CD  1 
ATOM   1760 N  NE  . ARG   A 1 248 ? -6.270  32.781 44.555  1.00 61.83 ? 237 ARG   A NE  1 
ATOM   1761 C  CZ  . ARG   A 1 248 ? -7.439  32.948 45.173  1.00 65.74 ? 237 ARG   A CZ  1 
ATOM   1762 N  NH1 . ARG   A 1 248 ? -7.578  32.612 46.452  1.00 65.52 ? 237 ARG   A NH1 1 
ATOM   1763 N  NH2 . ARG   A 1 248 ? -8.478  33.449 44.515  1.00 66.38 ? 237 ARG   A NH2 1 
ATOM   1764 N  N   . GLN   A 1 249 ? -4.341  37.123 46.162  1.00 50.29 ? 238 GLN   A N   1 
ATOM   1765 C  CA  . GLN   A 1 249 ? -5.248  38.003 46.901  1.00 52.36 ? 238 GLN   A CA  1 
ATOM   1766 C  C   . GLN   A 1 249 ? -6.392  37.223 47.578  1.00 53.17 ? 238 GLN   A C   1 
ATOM   1767 O  O   . GLN   A 1 249 ? -6.925  36.273 46.999  1.00 53.58 ? 238 GLN   A O   1 
ATOM   1768 C  CB  . GLN   A 1 249 ? -5.821  39.072 45.956  1.00 55.43 ? 238 GLN   A CB  1 
ATOM   1769 C  CG  . GLN   A 1 249 ? -4.740  39.836 45.173  1.00 61.37 ? 238 GLN   A CG  1 
ATOM   1770 C  CD  . GLN   A 1 249 ? -5.311  40.726 44.085  1.00 68.01 ? 238 GLN   A CD  1 
ATOM   1771 O  OE1 . GLN   A 1 249 ? -6.497  40.645 43.723  1.00 70.20 ? 238 GLN   A OE1 1 
ATOM   1772 N  NE2 . GLN   A 1 249 ? -4.474  41.601 43.538  1.00 68.88 ? 238 GLN   A NE2 1 
ATOM   1773 N  N   . SER   A 1 255 ? -11.483 40.141 57.346  1.00 67.95 ? 244 SER   A N   1 
ATOM   1774 C  CA  . SER   A 1 255 ? -12.034 40.271 58.696  1.00 68.51 ? 244 SER   A CA  1 
ATOM   1775 C  C   . SER   A 1 255 ? -11.481 39.166 59.605  1.00 68.27 ? 244 SER   A C   1 
ATOM   1776 O  O   . SER   A 1 255 ? -11.046 39.436 60.727  1.00 68.81 ? 244 SER   A O   1 
ATOM   1777 C  CB  . SER   A 1 255 ? -13.561 40.214 58.658  1.00 70.36 ? 244 SER   A CB  1 
ATOM   1778 O  OG  . SER   A 1 255 ? -14.031 38.921 58.307  1.00 72.81 ? 244 SER   A OG  1 
ATOM   1779 N  N   . ASN   A 1 256 ? -11.491 37.925 59.100  1.00 67.16 ? 245 ASN   A N   1 
ATOM   1780 C  CA  . ASN   A 1 256 ? -11.012 36.723 59.775  1.00 66.29 ? 245 ASN   A CA  1 
ATOM   1781 C  C   . ASN   A 1 256 ? -9.486  36.787 59.830  1.00 64.17 ? 245 ASN   A C   1 
ATOM   1782 O  O   . ASN   A 1 256 ? -8.865  37.026 58.800  1.00 64.39 ? 245 ASN   A O   1 
ATOM   1783 C  CB  . ASN   A 1 256 ? -11.478 35.507 58.946  1.00 68.28 ? 245 ASN   A CB  1 
ATOM   1784 C  CG  . ASN   A 1 256 ? -11.007 34.141 59.388  1.00 72.93 ? 245 ASN   A CG  1 
ATOM   1785 O  OD1 . ASN   A 1 256 ? -10.695 33.889 60.563  1.00 74.69 ? 245 ASN   A OD1 1 
ATOM   1786 N  ND2 . ASN   A 1 256 ? -10.958 33.213 58.438  1.00 73.79 ? 245 ASN   A ND2 1 
ATOM   1787 N  N   . PRO   A 1 257 ? -8.855  36.629 61.010  1.00 62.04 ? 246 PRO   A N   1 
ATOM   1788 C  CA  . PRO   A 1 257 ? -7.373  36.667 61.060  1.00 60.29 ? 246 PRO   A CA  1 
ATOM   1789 C  C   . PRO   A 1 257 ? -6.727  35.490 60.321  1.00 57.97 ? 246 PRO   A C   1 
ATOM   1790 O  O   . PRO   A 1 257 ? -5.650  35.630 59.742  1.00 58.22 ? 246 PRO   A O   1 
ATOM   1791 C  CB  . PRO   A 1 257 ? -7.057  36.613 62.560  1.00 61.29 ? 246 PRO   A CB  1 
ATOM   1792 C  CG  . PRO   A 1 257 ? -8.249  35.971 63.182  1.00 62.31 ? 246 PRO   A CG  1 
ATOM   1793 C  CD  . PRO   A 1 257 ? -9.446  36.347 62.333  1.00 61.23 ? 246 PRO   A CD  1 
ATOM   1794 N  N   . TYR   A 1 258 ? -7.406  34.337 60.321  1.00 55.23 ? 247 TYR   A N   1 
ATOM   1795 C  CA  . TYR   A 1 258 ? -6.963  33.126 59.665  1.00 53.23 ? 247 TYR   A CA  1 
ATOM   1796 C  C   . TYR   A 1 258 ? -7.045  33.223 58.138  1.00 51.70 ? 247 TYR   A C   1 
ATOM   1797 O  O   . TYR   A 1 258 ? -8.123  33.428 57.579  1.00 51.66 ? 247 TYR   A O   1 
ATOM   1798 C  CB  . TYR   A 1 258 ? -7.767  31.930 60.196  1.00 52.73 ? 247 TYR   A CB  1 
ATOM   1799 C  CG  . TYR   A 1 258 ? -7.320  30.603 59.635  1.00 52.52 ? 247 TYR   A CG  1 
ATOM   1800 C  CD1 . TYR   A 1 258 ? -6.273  29.898 60.216  1.00 53.04 ? 247 TYR   A CD1 1 
ATOM   1801 C  CD2 . TYR   A 1 258 ? -7.942  30.050 58.524  1.00 52.62 ? 247 TYR   A CD2 1 
ATOM   1802 C  CE1 . TYR   A 1 258 ? -5.859  28.677 59.706  1.00 53.57 ? 247 TYR   A CE1 1 
ATOM   1803 C  CE2 . TYR   A 1 258 ? -7.516  28.846 57.987  1.00 53.37 ? 247 TYR   A CE2 1 
ATOM   1804 C  CZ  . TYR   A 1 258 ? -6.482  28.155 58.589  1.00 54.24 ? 247 TYR   A CZ  1 
ATOM   1805 O  OH  . TYR   A 1 258 ? -6.092  26.942 58.093  1.00 55.33 ? 247 TYR   A OH  1 
ATOM   1806 N  N   . HIS   A 1 259 ? -5.901  33.021 57.471  1.00 50.26 ? 248 HIS   A N   1 
ATOM   1807 C  CA  . HIS   A 1 259 ? -5.769  33.063 56.016  1.00 49.10 ? 248 HIS   A CA  1 
ATOM   1808 C  C   . HIS   A 1 259 ? -5.060  31.812 55.518  1.00 46.92 ? 248 HIS   A C   1 
ATOM   1809 O  O   . HIS   A 1 259 ? -3.845  31.694 55.669  1.00 47.13 ? 248 HIS   A O   1 
ATOM   1810 C  CB  . HIS   A 1 259 ? -5.000  34.316 55.594  1.00 50.61 ? 248 HIS   A CB  1 
ATOM   1811 C  CG  . HIS   A 1 259 ? -5.659  35.575 56.059  1.00 54.38 ? 248 HIS   A CG  1 
ATOM   1812 N  ND1 . HIS   A 1 259 ? -6.925  35.929 55.621  1.00 56.61 ? 248 HIS   A ND1 1 
ATOM   1813 C  CD2 . HIS   A 1 259 ? -5.215  36.516 56.922  1.00 55.80 ? 248 HIS   A CD2 1 
ATOM   1814 C  CE1 . HIS   A 1 259 ? -7.205  37.072 56.224  1.00 57.22 ? 248 HIS   A CE1 1 
ATOM   1815 N  NE2 . HIS   A 1 259 ? -6.216  37.454 57.034  1.00 57.15 ? 248 HIS   A NE2 1 
ATOM   1816 N  N   . HIS   A 1 260 ? -5.827  30.885 54.922  1.00 44.67 ? 249 HIS   A N   1 
ATOM   1817 C  CA  . HIS   A 1 260 ? -5.358  29.596 54.437  1.00 43.02 ? 249 HIS   A CA  1 
ATOM   1818 C  C   . HIS   A 1 260 ? -4.193  29.649 53.438  1.00 41.87 ? 249 HIS   A C   1 
ATOM   1819 O  O   . HIS   A 1 260 ? -3.187  28.987 53.666  1.00 42.17 ? 249 HIS   A O   1 
ATOM   1820 C  CB  . HIS   A 1 260 ? -6.525  28.778 53.844  1.00 42.85 ? 249 HIS   A CB  1 
ATOM   1821 C  CG  . HIS   A 1 260 ? -6.113  27.414 53.392  1.00 42.95 ? 249 HIS   A CG  1 
ATOM   1822 N  ND1 . HIS   A 1 260 ? -5.622  27.192 52.116  1.00 44.19 ? 249 HIS   A ND1 1 
ATOM   1823 C  CD2 . HIS   A 1 260 ? -6.099  26.251 54.075  1.00 43.60 ? 249 HIS   A CD2 1 
ATOM   1824 C  CE1 . HIS   A 1 260 ? -5.304  25.913 52.070  1.00 44.57 ? 249 HIS   A CE1 1 
ATOM   1825 N  NE2 . HIS   A 1 260 ? -5.583  25.301 53.221  1.00 44.90 ? 249 HIS   A NE2 1 
ATOM   1826 N  N   . ASP   A 1 261 ? -4.359  30.342 52.311  1.00 40.35 ? 250 ASP   A N   1 
ATOM   1827 C  CA  . ASP   A 1 261 ? -3.346  30.402 51.262  1.00 39.63 ? 250 ASP   A CA  1 
ATOM   1828 C  C   . ASP   A 1 261 ? -2.053  31.037 51.720  1.00 37.61 ? 250 ASP   A C   1 
ATOM   1829 O  O   . ASP   A 1 261 ? -0.981  30.584 51.317  1.00 37.62 ? 250 ASP   A O   1 
ATOM   1830 C  CB  . ASP   A 1 261 ? -3.890  31.145 50.029  1.00 41.99 ? 250 ASP   A CB  1 
ATOM   1831 C  CG  . ASP   A 1 261 ? -4.958  30.388 49.271  1.00 49.28 ? 250 ASP   A CG  1 
ATOM   1832 O  OD1 . ASP   A 1 261 ? -5.343  29.273 49.723  1.00 50.53 ? 250 ASP   A OD1 1 
ATOM   1833 O  OD2 . ASP   A 1 261 ? -5.417  30.903 48.226  1.00 52.76 ? 250 ASP   A OD2 1 
ATOM   1834 N  N   . GLN   A 1 262 ? -2.145  32.085 52.548  1.00 35.42 ? 251 GLN   A N   1 
ATOM   1835 C  CA  . GLN   A 1 262 ? -0.946  32.715 53.064  1.00 34.43 ? 251 GLN   A CA  1 
ATOM   1836 C  C   . GLN   A 1 262 ? -0.146  31.718 53.954  1.00 33.54 ? 251 GLN   A C   1 
ATOM   1837 O  O   . GLN   A 1 262 ? 1.054   31.547 53.741  1.00 33.65 ? 251 GLN   A O   1 
ATOM   1838 C  CB  . GLN   A 1 262 ? -1.262  34.040 53.779  1.00 34.49 ? 251 GLN   A CB  1 
ATOM   1839 C  CG  . GLN   A 1 262 ? -0.009  34.768 54.219  1.00 34.48 ? 251 GLN   A CG  1 
ATOM   1840 C  CD  . GLN   A 1 262 ? 0.842   35.185 53.042  1.00 34.49 ? 251 GLN   A CD  1 
ATOM   1841 O  OE1 . GLN   A 1 262 ? 0.499   36.102 52.318  1.00 33.95 ? 251 GLN   A OE1 1 
ATOM   1842 N  NE2 . GLN   A 1 262 ? 1.972   34.525 52.832  1.00 34.45 ? 251 GLN   A NE2 1 
ATOM   1843 N  N   . LEU   A 1 263 ? -0.834  30.982 54.845  1.00 32.34 ? 252 LEU   A N   1 
ATOM   1844 C  CA  . LEU   A 1 263 ? -0.171  29.982 55.692  1.00 31.45 ? 252 LEU   A CA  1 
ATOM   1845 C  C   . LEU   A 1 263 ? 0.396   28.855 54.842  1.00 31.75 ? 252 LEU   A C   1 
ATOM   1846 O  O   . LEU   A 1 263 ? 1.533   28.446 55.047  1.00 32.30 ? 252 LEU   A O   1 
ATOM   1847 C  CB  . LEU   A 1 263 ? -1.114  29.433 56.748  1.00 30.31 ? 252 LEU   A CB  1 
ATOM   1848 C  CG  . LEU   A 1 263 ? -1.290  30.297 57.967  1.00 30.47 ? 252 LEU   A CG  1 
ATOM   1849 C  CD1 . LEU   A 1 263 ? -2.555  29.913 58.728  1.00 30.51 ? 252 LEU   A CD1 1 
ATOM   1850 C  CD2 . LEU   A 1 263 ? -0.061  30.239 58.849  1.00 30.17 ? 252 LEU   A CD2 1 
ATOM   1851 N  N   . ASP   A 1 264 ? -0.353  28.417 53.830  1.00 31.23 ? 253 ASP   A N   1 
ATOM   1852 C  CA  . ASP   A 1 264 ? 0.077   27.401 52.888  1.00 31.14 ? 253 ASP   A CA  1 
ATOM   1853 C  C   . ASP   A 1 264 ? 1.387   27.817 52.189  1.00 30.72 ? 253 ASP   A C   1 
ATOM   1854 O  O   . ASP   A 1 264 ? 2.276   26.988 52.038  1.00 31.31 ? 253 ASP   A O   1 
ATOM   1855 C  CB  . ASP   A 1 264 ? -1.053  27.144 51.869  1.00 33.39 ? 253 ASP   A CB  1 
ATOM   1856 C  CG  . ASP   A 1 264 ? -0.685  26.246 50.709  1.00 39.17 ? 253 ASP   A CG  1 
ATOM   1857 O  OD1 . ASP   A 1 264 ? -0.190  25.120 50.958  1.00 40.17 ? 253 ASP   A OD1 1 
ATOM   1858 O  OD2 . ASP   A 1 264 ? -0.883  26.663 49.564  1.00 42.84 ? 253 ASP   A OD2 1 
ATOM   1859 N  N   . ARG   A 1 265 ? 1.511   29.079 51.776  1.00 30.52 ? 254 ARG   A N   1 
ATOM   1860 C  CA  . ARG   A 1 265 ? 2.732   29.596 51.135  1.00 30.98 ? 254 ARG   A CA  1 
ATOM   1861 C  C   . ARG   A 1 265 ? 3.919   29.566 52.127  1.00 31.60 ? 254 ARG   A C   1 
ATOM   1862 O  O   . ARG   A 1 265 ? 5.034   29.184 51.758  1.00 32.66 ? 254 ARG   A O   1 
ATOM   1863 C  CB  . ARG   A 1 265 ? 2.510   31.022 50.603  1.00 31.38 ? 254 ARG   A CB  1 
ATOM   1864 C  CG  . ARG   A 1 265 ? 3.784   31.691 50.085  1.00 33.07 ? 254 ARG   A CG  1 
ATOM   1865 C  CD  . ARG   A 1 265 ? 4.444   30.955 48.927  1.00 34.79 ? 254 ARG   A CD  1 
ATOM   1866 N  NE  . ARG   A 1 265 ? 5.773   31.483 48.615  1.00 36.41 ? 254 ARG   A NE  1 
ATOM   1867 C  CZ  . ARG   A 1 265 ? 6.451   31.213 47.502  1.00 37.15 ? 254 ARG   A CZ  1 
ATOM   1868 N  NH1 . ARG   A 1 265 ? 5.927   30.433 46.572  1.00 37.17 ? 254 ARG   A NH1 1 
ATOM   1869 N  NH2 . ARG   A 1 265 ? 7.658   31.727 47.314  1.00 36.48 ? 254 ARG   A NH2 1 
ATOM   1870 N  N   . ILE   A 1 266 ? 3.670   29.934 53.380  1.00 30.60 ? 255 ILE   A N   1 
ATOM   1871 C  CA  . ILE   A 1 266 ? 4.692   29.877 54.419  1.00 30.26 ? 255 ILE   A CA  1 
ATOM   1872 C  C   . ILE   A 1 266 ? 5.157   28.429 54.639  1.00 30.97 ? 255 ILE   A C   1 
ATOM   1873 O  O   . ILE   A 1 266 ? 6.361   28.194 54.694  1.00 31.53 ? 255 ILE   A O   1 
ATOM   1874 C  CB  . ILE   A 1 266 ? 4.171   30.522 55.709  1.00 30.00 ? 255 ILE   A CB  1 
ATOM   1875 C  CG1 . ILE   A 1 266 ? 3.912   32.021 55.479  1.00 29.95 ? 255 ILE   A CG1 1 
ATOM   1876 C  CG2 . ILE   A 1 266 ? 5.134   30.268 56.885  1.00 30.57 ? 255 ILE   A CG2 1 
ATOM   1877 C  CD1 . ILE   A 1 266 ? 3.308   32.755 56.655  1.00 30.92 ? 255 ILE   A CD1 1 
ATOM   1878 N  N   . PHE   A 1 267 ? 4.225   27.453 54.687  1.00 30.38 ? 256 PHE   A N   1 
ATOM   1879 C  CA  . PHE   A 1 267 ? 4.613   26.055 54.862  1.00 30.06 ? 256 PHE   A CA  1 
ATOM   1880 C  C   . PHE   A 1 267 ? 5.310   25.525 53.617  1.00 30.57 ? 256 PHE   A C   1 
ATOM   1881 O  O   . PHE   A 1 267 ? 6.280   24.794 53.737  1.00 29.94 ? 256 PHE   A O   1 
ATOM   1882 C  CB  . PHE   A 1 267 ? 3.444   25.174 55.301  1.00 29.58 ? 256 PHE   A CB  1 
ATOM   1883 C  CG  . PHE   A 1 267 ? 2.708   25.650 56.532  1.00 29.99 ? 256 PHE   A CG  1 
ATOM   1884 C  CD1 . PHE   A 1 267 ? 3.395   26.182 57.611  1.00 30.85 ? 256 PHE   A CD1 1 
ATOM   1885 C  CD2 . PHE   A 1 267 ? 1.327   25.583 56.600  1.00 30.46 ? 256 PHE   A CD2 1 
ATOM   1886 C  CE1 . PHE   A 1 267 ? 2.710   26.632 58.738  1.00 31.65 ? 256 PHE   A CE1 1 
ATOM   1887 C  CE2 . PHE   A 1 267 ? 0.647   26.052 57.710  1.00 31.25 ? 256 PHE   A CE2 1 
ATOM   1888 C  CZ  . PHE   A 1 267 ? 1.343   26.556 58.783  1.00 31.47 ? 256 PHE   A CZ  1 
ATOM   1889 N  N   . ASN   A 1 268 ? 4.897   25.957 52.425  1.00 31.84 ? 257 ASN   A N   1 
ATOM   1890 C  CA  . ASN   A 1 268 ? 5.576   25.565 51.191  1.00 33.21 ? 257 ASN   A CA  1 
ATOM   1891 C  C   . ASN   A 1 268 ? 7.033   26.049 51.190  1.00 33.04 ? 257 ASN   A C   1 
ATOM   1892 O  O   . ASN   A 1 268 ? 7.902   25.349 50.691  1.00 33.87 ? 257 ASN   A O   1 
ATOM   1893 C  CB  . ASN   A 1 268 ? 4.821   26.065 49.972  1.00 36.58 ? 257 ASN   A CB  1 
ATOM   1894 C  CG  . ASN   A 1 268 ? 4.086   24.939 49.318  1.00 44.14 ? 257 ASN   A CG  1 
ATOM   1895 O  OD1 . ASN   A 1 268 ? 4.700   24.028 48.750  1.00 47.20 ? 257 ASN   A OD1 1 
ATOM   1896 N  ND2 . ASN   A 1 268 ? 2.760   24.934 49.426  1.00 45.69 ? 257 ASN   A ND2 1 
ATOM   1897 N  N   . VAL   A 1 269 ? 7.315   27.202 51.812  1.00 32.27 ? 258 VAL   A N   1 
ATOM   1898 C  CA  . VAL   A 1 269 ? 8.683   27.708 51.892  1.00 32.14 ? 258 VAL   A CA  1 
ATOM   1899 C  C   . VAL   A 1 269 ? 9.470   27.137 53.096  1.00 32.05 ? 258 VAL   A C   1 
ATOM   1900 O  O   . VAL   A 1 269 ? 10.541  26.567 52.922  1.00 31.98 ? 258 VAL   A O   1 
ATOM   1901 C  CB  . VAL   A 1 269 ? 8.714   29.259 51.855  1.00 31.90 ? 258 VAL   A CB  1 
ATOM   1902 C  CG1 . VAL   A 1 269 ? 10.098  29.803 52.206  1.00 31.35 ? 258 VAL   A CG1 1 
ATOM   1903 C  CG2 . VAL   A 1 269 ? 8.235   29.781 50.497  1.00 32.00 ? 258 VAL   A CG2 1 
ATOM   1904 N  N   . MET   A 1 270 ? 8.932   27.291 54.295  1.00 31.82 ? 259 MET   A N   1 
ATOM   1905 C  CA  . MET   A 1 270 ? 9.585   26.933 55.543  1.00 32.65 ? 259 MET   A CA  1 
ATOM   1906 C  C   . MET   A 1 270 ? 9.469   25.481 55.962  1.00 33.37 ? 259 MET   A C   1 
ATOM   1907 O  O   . MET   A 1 270 ? 10.292  24.978 56.731  1.00 33.78 ? 259 MET   A O   1 
ATOM   1908 C  CB  . MET   A 1 270 ? 8.963   27.772 56.676  1.00 32.88 ? 259 MET   A CB  1 
ATOM   1909 C  CG  . MET   A 1 270 ? 8.967   29.268 56.412  1.00 33.83 ? 259 MET   A CG  1 
ATOM   1910 S  SD  . MET   A 1 270 ? 10.625  29.966 56.248  1.00 33.69 ? 259 MET   A SD  1 
ATOM   1911 C  CE  . MET   A 1 270 ? 11.302  29.540 57.787  1.00 29.05 ? 259 MET   A CE  1 
ATOM   1912 N  N   . GLY   A 1 271 ? 8.393   24.857 55.546  1.00 33.06 ? 260 GLY   A N   1 
ATOM   1913 C  CA  . GLY   A 1 271 ? 8.019   23.543 56.026  1.00 33.69 ? 260 GLY   A CA  1 
ATOM   1914 C  C   . GLY   A 1 271 ? 6.963   23.707 57.111  1.00 34.30 ? 260 GLY   A C   1 
ATOM   1915 O  O   . GLY   A 1 271 ? 6.643   24.830 57.532  1.00 33.69 ? 260 GLY   A O   1 
ATOM   1916 N  N   . PHE   A 1 272 ? 6.374   22.590 57.543  1.00 34.88 ? 261 PHE   A N   1 
ATOM   1917 C  CA  . PHE   A 1 272 ? 5.345   22.628 58.564  1.00 35.50 ? 261 PHE   A CA  1 
ATOM   1918 C  C   . PHE   A 1 272 ? 6.043   22.541 59.905  1.00 36.24 ? 261 PHE   A C   1 
ATOM   1919 O  O   . PHE   A 1 272 ? 6.958   21.732 60.083  1.00 36.13 ? 261 PHE   A O   1 
ATOM   1920 C  CB  . PHE   A 1 272 ? 4.302   21.511 58.356  1.00 35.40 ? 261 PHE   A CB  1 
ATOM   1921 C  CG  . PHE   A 1 272 ? 3.030   21.749 59.139  1.00 35.80 ? 261 PHE   A CG  1 
ATOM   1922 C  CD1 . PHE   A 1 272 ? 2.898   21.284 60.438  1.00 36.49 ? 261 PHE   A CD1 1 
ATOM   1923 C  CD2 . PHE   A 1 272 ? 1.974   22.442 58.582  1.00 36.14 ? 261 PHE   A CD2 1 
ATOM   1924 C  CE1 . PHE   A 1 272 ? 1.745   21.540 61.168  1.00 37.12 ? 261 PHE   A CE1 1 
ATOM   1925 C  CE2 . PHE   A 1 272 ? 0.808   22.665 59.305  1.00 36.76 ? 261 PHE   A CE2 1 
ATOM   1926 C  CZ  . PHE   A 1 272 ? 0.711   22.239 60.600  1.00 36.58 ? 261 PHE   A CZ  1 
ATOM   1927 N  N   . PRO   A 1 273 ? 5.712   23.447 60.830  1.00 37.08 ? 262 PRO   A N   1 
ATOM   1928 C  CA  . PRO   A 1 273 ? 6.396   23.425 62.128  1.00 38.29 ? 262 PRO   A CA  1 
ATOM   1929 C  C   . PRO   A 1 273 ? 6.068   22.159 62.906  1.00 40.04 ? 262 PRO   A C   1 
ATOM   1930 O  O   . PRO   A 1 273 ? 4.912   21.752 62.991  1.00 40.80 ? 262 PRO   A O   1 
ATOM   1931 C  CB  . PRO   A 1 273 ? 5.878   24.682 62.831  1.00 38.30 ? 262 PRO   A CB  1 
ATOM   1932 C  CG  . PRO   A 1 273 ? 4.565   24.957 62.195  1.00 38.41 ? 262 PRO   A CG  1 
ATOM   1933 C  CD  . PRO   A 1 273 ? 4.699   24.513 60.763  1.00 36.64 ? 262 PRO   A CD  1 
ATOM   1934 N  N   . ALA   A 1 274 ? 7.090   21.516 63.431  1.00 40.79 ? 263 ALA   A N   1 
ATOM   1935 C  CA  . ALA   A 1 274 ? 6.904   20.360 64.303  1.00 42.05 ? 263 ALA   A CA  1 
ATOM   1936 C  C   . ALA   A 1 274 ? 6.510   20.874 65.698  1.00 43.23 ? 263 ALA   A C   1 
ATOM   1937 O  O   . ALA   A 1 274 ? 6.743   22.042 66.016  1.00 43.30 ? 263 ALA   A O   1 
ATOM   1938 C  CB  . ALA   A 1 274 ? 8.190   19.547 64.377  1.00 42.28 ? 263 ALA   A CB  1 
ATOM   1939 N  N   . ASP   A 1 275 ? 5.955   20.011 66.560  1.00 44.09 ? 264 ASP   A N   1 
ATOM   1940 C  CA  . ASP   A 1 275 ? 5.590   20.395 67.934  1.00 44.96 ? 264 ASP   A CA  1 
ATOM   1941 C  C   . ASP   A 1 275 ? 6.778   21.062 68.675  1.00 43.79 ? 264 ASP   A C   1 
ATOM   1942 O  O   . ASP   A 1 275 ? 6.600   22.078 69.330  1.00 43.85 ? 264 ASP   A O   1 
ATOM   1943 C  CB  . ASP   A 1 275 ? 5.136   19.150 68.736  1.00 48.44 ? 264 ASP   A CB  1 
ATOM   1944 C  CG  . ASP   A 1 275 ? 3.834   18.498 68.287  1.00 55.91 ? 264 ASP   A CG  1 
ATOM   1945 O  OD1 . ASP   A 1 275 ? 3.090   19.129 67.499  1.00 57.25 ? 264 ASP   A OD1 1 
ATOM   1946 O  OD2 . ASP   A 1 275 ? 3.546   17.359 68.748  1.00 58.82 ? 264 ASP   A OD2 1 
ATOM   1947 N  N   . LYS   A 1 276 ? 7.983   20.513 68.510  1.00 42.79 ? 265 LYS   A N   1 
ATOM   1948 C  CA  . LYS   A 1 276 ? 9.179   21.008 69.173  1.00 43.05 ? 265 LYS   A CA  1 
ATOM   1949 C  C   . LYS   A 1 276 ? 9.645   22.366 68.671  1.00 42.07 ? 265 LYS   A C   1 
ATOM   1950 O  O   . LYS   A 1 276 ? 10.249  23.114 69.437  1.00 42.38 ? 265 LYS   A O   1 
ATOM   1951 C  CB  . LYS   A 1 276 ? 10.315  19.973 69.088  1.00 46.52 ? 265 LYS   A CB  1 
ATOM   1952 C  CG  . LYS   A 1 276 ? 10.798  19.688 67.666  1.00 52.16 ? 265 LYS   A CG  1 
ATOM   1953 C  CD  . LYS   A 1 276 ? 11.780  18.523 67.634  1.00 58.00 ? 265 LYS   A CD  1 
ATOM   1954 C  CE  . LYS   A 1 276 ? 11.898  17.940 66.252  1.00 62.89 ? 265 LYS   A CE  1 
ATOM   1955 N  NZ  . LYS   A 1 276 ? 10.616  17.323 65.810  1.00 65.71 ? 265 LYS   A NZ  1 
ATOM   1956 N  N   . ASP   A 1 277 ? 9.347   22.690 67.399  1.00 40.73 ? 266 ASP   A N   1 
ATOM   1957 C  CA  . ASP   A 1 277 ? 9.697   23.949 66.749  1.00 40.04 ? 266 ASP   A CA  1 
ATOM   1958 C  C   . ASP   A 1 277 ? 8.855   25.115 67.293  1.00 38.88 ? 266 ASP   A C   1 
ATOM   1959 O  O   . ASP   A 1 277 ? 9.346   26.234 67.400  1.00 38.70 ? 266 ASP   A O   1 
ATOM   1960 C  CB  . ASP   A 1 277 ? 9.464   23.843 65.233  1.00 41.62 ? 266 ASP   A CB  1 
ATOM   1961 C  CG  . ASP   A 1 277 ? 10.357  22.860 64.509  1.00 46.80 ? 266 ASP   A CG  1 
ATOM   1962 O  OD1 . ASP   A 1 277 ? 11.471  22.583 65.015  1.00 47.75 ? 266 ASP   A OD1 1 
ATOM   1963 O  OD2 . ASP   A 1 277 ? 9.950   22.377 63.421  1.00 49.11 ? 266 ASP   A OD2 1 
ATOM   1964 N  N   . TRP   A 1 278 ? 7.589   24.859 67.587  1.00 37.98 ? 267 TRP   A N   1 
ATOM   1965 C  CA  . TRP   A 1 278 ? 6.683   25.884 68.071  1.00 38.09 ? 267 TRP   A CA  1 
ATOM   1966 C  C   . TRP   A 1 278 ? 5.708   25.259 69.074  1.00 39.32 ? 267 TRP   A C   1 
ATOM   1967 O  O   . TRP   A 1 278 ? 4.573   24.954 68.736  1.00 39.19 ? 267 TRP   A O   1 
ATOM   1968 C  CB  . TRP   A 1 278 ? 5.946   26.519 66.883  1.00 37.09 ? 267 TRP   A CB  1 
ATOM   1969 C  CG  . TRP   A 1 278 ? 5.144   27.753 67.178  1.00 36.46 ? 267 TRP   A CG  1 
ATOM   1970 C  CD1 . TRP   A 1 278 ? 4.938   28.351 68.390  1.00 37.06 ? 267 TRP   A CD1 1 
ATOM   1971 C  CD2 . TRP   A 1 278 ? 4.457   28.554 66.214  1.00 36.11 ? 267 TRP   A CD2 1 
ATOM   1972 N  NE1 . TRP   A 1 278 ? 4.114   29.441 68.241  1.00 37.27 ? 267 TRP   A NE1 1 
ATOM   1973 C  CE2 . TRP   A 1 278 ? 3.803   29.586 66.914  1.00 36.86 ? 267 TRP   A CE2 1 
ATOM   1974 C  CE3 . TRP   A 1 278 ? 4.309   28.481 64.823  1.00 36.06 ? 267 TRP   A CE3 1 
ATOM   1975 C  CZ2 . TRP   A 1 278 ? 3.026   30.542 66.269  1.00 37.21 ? 267 TRP   A CZ2 1 
ATOM   1976 C  CZ3 . TRP   A 1 278 ? 3.525   29.414 64.194  1.00 36.70 ? 267 TRP   A CZ3 1 
ATOM   1977 C  CH2 . TRP   A 1 278 ? 2.908   30.440 64.910  1.00 37.02 ? 267 TRP   A CH2 1 
ATOM   1978 N  N   . GLU   A 1 279 ? 6.165   25.070 70.304  1.00 40.36 ? 268 GLU   A N   1 
ATOM   1979 C  CA  . GLU   A 1 279 ? 5.378   24.462 71.363  1.00 42.32 ? 268 GLU   A CA  1 
ATOM   1980 C  C   . GLU   A 1 279 ? 4.060   25.170 71.629  1.00 43.60 ? 268 GLU   A C   1 
ATOM   1981 O  O   . GLU   A 1 279 ? 3.027   24.514 71.659  1.00 44.66 ? 268 GLU   A O   1 
ATOM   1982 C  CB  . GLU   A 1 279 ? 6.211   24.332 72.643  1.00 45.26 ? 268 GLU   A CB  1 
ATOM   1983 C  CG  . GLU   A 1 279 ? 7.375   23.375 72.462  1.00 52.25 ? 268 GLU   A CG  1 
ATOM   1984 C  CD  . GLU   A 1 279 ? 7.960   22.798 73.736  1.00 60.14 ? 268 GLU   A CD  1 
ATOM   1985 O  OE1 . GLU   A 1 279 ? 7.208   22.643 74.728  1.00 60.85 ? 268 GLU   A OE1 1 
ATOM   1986 O  OE2 . GLU   A 1 279 ? 9.176   22.494 73.738  1.00 62.69 ? 268 GLU   A OE2 1 
ATOM   1987 N  N   . ASP   A 1 280 ? 4.074   26.490 71.752  1.00 43.61 ? 269 ASP   A N   1 
ATOM   1988 C  CA  . ASP   A 1 280 ? 2.862   27.245 72.031  1.00 44.46 ? 269 ASP   A CA  1 
ATOM   1989 C  C   . ASP   A 1 280 ? 1.947   27.438 70.830  1.00 44.78 ? 269 ASP   A C   1 
ATOM   1990 O  O   . ASP   A 1 280 ? 1.047   28.272 70.906  1.00 44.85 ? 269 ASP   A O   1 
ATOM   1991 C  CB  . ASP   A 1 280 ? 3.189   28.591 72.683  1.00 46.76 ? 269 ASP   A CB  1 
ATOM   1992 C  CG  . ASP   A 1 280 ? 3.756   28.473 74.083  1.00 51.89 ? 269 ASP   A CG  1 
ATOM   1993 O  OD1 . ASP   A 1 280 ? 3.540   27.417 74.728  1.00 52.40 ? 269 ASP   A OD1 1 
ATOM   1994 O  OD2 . ASP   A 1 280 ? 4.422   29.428 74.533  1.00 54.66 ? 269 ASP   A OD2 1 
ATOM   1995 N  N   . ILE   A 1 281 ? 2.148   26.680 69.732  1.00 44.55 ? 270 ILE   A N   1 
ATOM   1996 C  CA  . ILE   A 1 281 ? 1.242   26.778 68.585  1.00 44.70 ? 270 ILE   A CA  1 
ATOM   1997 C  C   . ILE   A 1 281 ? -0.158  26.272 68.995  1.00 46.04 ? 270 ILE   A C   1 
ATOM   1998 O  O   . ILE   A 1 281 ? -1.155  26.810 68.523  1.00 46.26 ? 270 ILE   A O   1 
ATOM   1999 C  CB  . ILE   A 1 281 ? 1.777   26.071 67.312  1.00 44.03 ? 270 ILE   A CB  1 
ATOM   2000 C  CG1 . ILE   A 1 281 ? 1.156   26.694 66.040  1.00 44.09 ? 270 ILE   A CG1 1 
ATOM   2001 C  CG2 . ILE   A 1 281 ? 1.556   24.543 67.372  1.00 43.90 ? 270 ILE   A CG2 1 
ATOM   2002 C  CD1 . ILE   A 1 281 ? 1.640   26.081 64.716  1.00 44.86 ? 270 ILE   A CD1 1 
ATOM   2003 N  N   . LYS   A 1 282 ? -0.228  25.280 69.916  1.00 46.62 ? 271 LYS   A N   1 
ATOM   2004 C  CA  . LYS   A 1 282 ? -1.471  24.736 70.460  1.00 47.70 ? 271 LYS   A CA  1 
ATOM   2005 C  C   . LYS   A 1 282 ? -2.329  25.842 71.076  1.00 48.03 ? 271 LYS   A C   1 
ATOM   2006 O  O   . LYS   A 1 282 ? -3.544  25.762 71.011  1.00 48.83 ? 271 LYS   A O   1 
ATOM   2007 C  CB  . LYS   A 1 282 ? -1.153  23.687 71.541  1.00 50.78 ? 271 LYS   A CB  1 
ATOM   2008 C  CG  . LYS   A 1 282 ? -0.668  22.344 71.001  1.00 56.40 ? 271 LYS   A CG  1 
ATOM   2009 C  CD  . LYS   A 1 282 ? -0.443  21.314 72.119  1.00 62.19 ? 271 LYS   A CD  1 
ATOM   2010 C  CE  . LYS   A 1 282 ? -1.708  21.017 72.913  1.00 66.84 ? 271 LYS   A CE  1 
ATOM   2011 N  NZ  . LYS   A 1 282 ? -1.656  19.695 73.617  1.00 68.72 ? 271 LYS   A NZ  1 
ATOM   2012 N  N   . LYS   A 1 283 ? -1.697  26.880 71.652  1.00 47.62 ? 272 LYS   A N   1 
ATOM   2013 C  CA  . LYS   A 1 283 ? -2.338  28.019 72.307  1.00 47.48 ? 272 LYS   A CA  1 
ATOM   2014 C  C   . LYS   A 1 283 ? -2.940  29.049 71.355  1.00 46.44 ? 272 LYS   A C   1 
ATOM   2015 O  O   . LYS   A 1 283 ? -3.627  29.951 71.825  1.00 46.76 ? 272 LYS   A O   1 
ATOM   2016 C  CB  . LYS   A 1 283 ? -1.326  28.746 73.209  1.00 50.20 ? 272 LYS   A CB  1 
ATOM   2017 C  CG  . LYS   A 1 283 ? -0.855  27.959 74.427  1.00 54.92 ? 272 LYS   A CG  1 
ATOM   2018 C  CD  . LYS   A 1 283 ? -0.206  28.931 75.400  1.00 60.17 ? 272 LYS   A CD  1 
ATOM   2019 C  CE  . LYS   A 1 283 ? 0.516   28.276 76.545  1.00 64.53 ? 272 LYS   A CE  1 
ATOM   2020 N  NZ  . LYS   A 1 283 ? 1.329   29.281 77.287  1.00 67.43 ? 272 LYS   A NZ  1 
ATOM   2021 N  N   . MET   A 1 284 ? -2.634  28.978 70.051  1.00 45.04 ? 273 MET   A N   1 
ATOM   2022 C  CA  . MET   A 1 284 ? -3.177  29.933 69.094  1.00 44.07 ? 273 MET   A CA  1 
ATOM   2023 C  C   . MET   A 1 284 ? -4.655  29.710 68.895  1.00 43.57 ? 273 MET   A C   1 
ATOM   2024 O  O   . MET   A 1 284 ? -5.087  28.568 68.748  1.00 43.77 ? 273 MET   A O   1 
ATOM   2025 C  CB  . MET   A 1 284 ? -2.464  29.826 67.733  1.00 44.41 ? 273 MET   A CB  1 
ATOM   2026 C  CG  . MET   A 1 284 ? -0.951  30.026 67.801  1.00 45.49 ? 273 MET   A CG  1 
ATOM   2027 S  SD  . MET   A 1 284 ? -0.396  31.557 68.589  1.00 44.18 ? 273 MET   A SD  1 
ATOM   2028 C  CE  . MET   A 1 284 ? -1.084  32.692 67.551  1.00 39.40 ? 273 MET   A CE  1 
ATOM   2029 N  N   . PRO   A 1 285 ? -5.452  30.792 68.840  1.00 43.14 ? 274 PRO   A N   1 
ATOM   2030 C  CA  . PRO   A 1 285 ? -6.904  30.636 68.626  1.00 42.75 ? 274 PRO   A CA  1 
ATOM   2031 C  C   . PRO   A 1 285 ? -7.308  29.836 67.385  1.00 42.85 ? 274 PRO   A C   1 
ATOM   2032 O  O   . PRO   A 1 285 ? -8.326  29.145 67.421  1.00 43.55 ? 274 PRO   A O   1 
ATOM   2033 C  CB  . PRO   A 1 285 ? -7.396  32.081 68.554  1.00 43.13 ? 274 PRO   A CB  1 
ATOM   2034 C  CG  . PRO   A 1 285 ? -6.404  32.848 69.351  1.00 43.46 ? 274 PRO   A CG  1 
ATOM   2035 C  CD  . PRO   A 1 285 ? -5.091  32.212 69.016  1.00 42.26 ? 274 PRO   A CD  1 
ATOM   2036 N  N   . GLU   A 1 286 ? -6.512  29.889 66.305  1.00 41.94 ? 275 GLU   A N   1 
ATOM   2037 C  CA  . GLU   A 1 286 ? -6.831  29.136 65.089  1.00 41.54 ? 275 GLU   A CA  1 
ATOM   2038 C  C   . GLU   A 1 286 ? -6.040  27.836 64.952  1.00 40.63 ? 275 GLU   A C   1 
ATOM   2039 O  O   . GLU   A 1 286 ? -5.969  27.311 63.846  1.00 41.03 ? 275 GLU   A O   1 
ATOM   2040 C  CB  . GLU   A 1 286 ? -6.595  29.987 63.830  1.00 43.27 ? 275 GLU   A CB  1 
ATOM   2041 C  CG  . GLU   A 1 286 ? -7.218  31.366 63.879  1.00 48.69 ? 275 GLU   A CG  1 
ATOM   2042 C  CD  . GLU   A 1 286 ? -8.728  31.412 63.880  1.00 55.61 ? 275 GLU   A CD  1 
ATOM   2043 O  OE1 . GLU   A 1 286 ? -9.356  30.520 63.267  1.00 56.45 ? 275 GLU   A OE1 1 
ATOM   2044 O  OE2 . GLU   A 1 286 ? -9.284  32.358 64.480  1.00 59.69 ? 275 GLU   A OE2 1 
ATOM   2045 N  N   . HIS   A 1 287 ? -5.435  27.326 66.032  1.00 39.57 ? 276 HIS   A N   1 
ATOM   2046 C  CA  . HIS   A 1 287 ? -4.671  26.085 65.944  1.00 39.57 ? 276 HIS   A CA  1 
ATOM   2047 C  C   . HIS   A 1 287 ? -5.505  24.896 65.452  1.00 40.25 ? 276 HIS   A C   1 
ATOM   2048 O  O   . HIS   A 1 287 ? -5.002  24.134 64.629  1.00 40.84 ? 276 HIS   A O   1 
ATOM   2049 C  CB  . HIS   A 1 287 ? -3.960  25.730 67.252  1.00 39.32 ? 276 HIS   A CB  1 
ATOM   2050 C  CG  . HIS   A 1 287 ? -3.171  24.458 67.149  1.00 40.18 ? 276 HIS   A CG  1 
ATOM   2051 N  ND1 . HIS   A 1 287 ? -3.558  23.311 67.819  1.00 41.64 ? 276 HIS   A ND1 1 
ATOM   2052 C  CD2 . HIS   A 1 287 ? -2.084  24.174 66.392  1.00 40.87 ? 276 HIS   A CD2 1 
ATOM   2053 C  CE1 . HIS   A 1 287 ? -2.665  22.389 67.497  1.00 42.03 ? 276 HIS   A CE1 1 
ATOM   2054 N  NE2 . HIS   A 1 287 ? -1.760  22.861 66.639  1.00 41.91 ? 276 HIS   A NE2 1 
ATOM   2055 N  N   . SER   A 1 288 ? -6.752  24.729 65.932  1.00 39.71 ? 277 SER   A N   1 
ATOM   2056 C  CA  . SER   A 1 288 ? -7.570  23.603 65.483  1.00 40.33 ? 277 SER   A CA  1 
ATOM   2057 C  C   . SER   A 1 288 ? -8.017  23.738 64.025  1.00 40.76 ? 277 SER   A C   1 
ATOM   2058 O  O   . SER   A 1 288 ? -8.152  22.736 63.342  1.00 40.95 ? 277 SER   A O   1 
ATOM   2059 C  CB  . SER   A 1 288 ? -8.737  23.365 66.428  1.00 42.13 ? 277 SER   A CB  1 
ATOM   2060 O  OG  . SER   A 1 288 ? -8.280  22.539 67.491  1.00 44.25 ? 277 SER   A OG  1 
ATOM   2061 N  N   . THR   A 1 289 ? -8.146  24.974 63.527  1.00 40.71 ? 278 THR   A N   1 
ATOM   2062 C  CA  . THR   A 1 289 ? -8.438  25.253 62.126  1.00 40.93 ? 278 THR   A CA  1 
ATOM   2063 C  C   . THR   A 1 289 ? -7.190  24.892 61.276  1.00 40.89 ? 278 THR   A C   1 
ATOM   2064 O  O   . THR   A 1 289 ? -7.319  24.389 60.154  1.00 41.80 ? 278 THR   A O   1 
ATOM   2065 C  CB  . THR   A 1 289 ? -8.818  26.732 61.954  1.00 42.23 ? 278 THR   A CB  1 
ATOM   2066 O  OG1 . THR   A 1 289 ? -9.812  27.084 62.914  1.00 43.37 ? 278 THR   A OG1 1 
ATOM   2067 C  CG2 . THR   A 1 289 ? -9.337  27.042 60.557  1.00 42.80 ? 278 THR   A CG2 1 
ATOM   2068 N  N   . LEU   A 1 290 ? -5.987  25.139 61.815  1.00 39.37 ? 279 LEU   A N   1 
ATOM   2069 C  CA  . LEU   A 1 290 ? -4.742  24.802 61.152  1.00 38.42 ? 279 LEU   A CA  1 
ATOM   2070 C  C   . LEU   A 1 290 ? -4.629  23.269 61.044  1.00 38.62 ? 279 LEU   A C   1 
ATOM   2071 O  O   . LEU   A 1 290 ? -4.270  22.755 59.991  1.00 38.70 ? 279 LEU   A O   1 
ATOM   2072 C  CB  . LEU   A 1 290 ? -3.568  25.389 61.947  1.00 37.49 ? 279 LEU   A CB  1 
ATOM   2073 C  CG  . LEU   A 1 290 ? -2.196  25.031 61.434  1.00 37.27 ? 279 LEU   A CG  1 
ATOM   2074 C  CD1 . LEU   A 1 290 ? -1.950  25.674 60.109  1.00 37.35 ? 279 LEU   A CD1 1 
ATOM   2075 C  CD2 . LEU   A 1 290 ? -1.121  25.361 62.444  1.00 36.86 ? 279 LEU   A CD2 1 
ATOM   2076 N  N   . MET   A 1 291 ? -4.994  22.538 62.113  1.00 38.70 ? 280 MET   A N   1 
ATOM   2077 C  CA  . MET   A 1 291 ? -4.965  21.077 62.125  1.00 38.85 ? 280 MET   A CA  1 
ATOM   2078 C  C   . MET   A 1 291 ? -5.995  20.502 61.176  1.00 40.33 ? 280 MET   A C   1 
ATOM   2079 O  O   . MET   A 1 291 ? -5.725  19.502 60.529  1.00 40.78 ? 280 MET   A O   1 
ATOM   2080 C  CB  . MET   A 1 291 ? -5.211  20.528 63.532  1.00 38.37 ? 280 MET   A CB  1 
ATOM   2081 C  CG  . MET   A 1 291 ? -4.270  21.054 64.556  1.00 40.13 ? 280 MET   A CG  1 
ATOM   2082 S  SD  . MET   A 1 291 ? -2.610  20.403 64.387  1.00 43.58 ? 280 MET   A SD  1 
ATOM   2083 C  CE  . MET   A 1 291 ? -1.775  21.805 63.646  1.00 43.01 ? 280 MET   A CE  1 
ATOM   2084 N  N   . LYS   A 1 292 ? -7.176  21.098 61.114  1.00 41.18 ? 281 LYS   A N   1 
ATOM   2085 C  CA  . LYS   A 1 292 ? -8.243  20.625 60.245  1.00 42.82 ? 281 LYS   A CA  1 
ATOM   2086 C  C   . LYS   A 1 292 ? -7.919  20.852 58.769  1.00 43.98 ? 281 LYS   A C   1 
ATOM   2087 O  O   . LYS   A 1 292 ? -8.180  19.985 57.952  1.00 44.36 ? 281 LYS   A O   1 
ATOM   2088 C  CB  . LYS   A 1 292 ? -9.549  21.349 60.602  1.00 45.37 ? 281 LYS   A CB  1 
ATOM   2089 C  CG  . LYS   A 1 292 ? -10.754 20.835 59.858  1.00 50.25 ? 281 LYS   A CG  1 
ATOM   2090 C  CD  . LYS   A 1 292 ? -11.938 21.764 60.019  1.00 56.31 ? 281 LYS   A CD  1 
ATOM   2091 C  CE  . LYS   A 1 292 ? -12.091 22.724 58.865  1.00 61.22 ? 281 LYS   A CE  1 
ATOM   2092 N  NZ  . LYS   A 1 292 ? -11.306 23.967 59.067  1.00 64.46 ? 281 LYS   A NZ  1 
ATOM   2093 N  N   . ASP   A 1 293 ? -7.330  22.006 58.425  1.00 44.39 ? 282 ASP   A N   1 
ATOM   2094 C  CA  . ASP   A 1 293 ? -7.033  22.331 57.027  1.00 44.78 ? 282 ASP   A CA  1 
ATOM   2095 C  C   . ASP   A 1 293 ? -5.685  21.870 56.524  1.00 45.37 ? 282 ASP   A C   1 
ATOM   2096 O  O   . ASP   A 1 293 ? -5.437  21.983 55.323  1.00 45.94 ? 282 ASP   A O   1 
ATOM   2097 C  CB  . ASP   A 1 293 ? -7.084  23.845 56.818  1.00 46.01 ? 282 ASP   A CB  1 
ATOM   2098 C  CG  . ASP   A 1 293 ? -8.434  24.476 57.022  1.00 50.05 ? 282 ASP   A CG  1 
ATOM   2099 O  OD1 . ASP   A 1 293 ? -9.450  23.763 56.880  1.00 50.35 ? 282 ASP   A OD1 1 
ATOM   2100 O  OD2 . ASP   A 1 293 ? -8.478  25.687 57.301  1.00 52.67 ? 282 ASP   A OD2 1 
ATOM   2101 N  N   . PHE   A 1 294 ? -4.777  21.467 57.418  1.00 45.27 ? 283 PHE   A N   1 
ATOM   2102 C  CA  . PHE   A 1 294 ? -3.419  21.142 57.000  1.00 45.71 ? 283 PHE   A CA  1 
ATOM   2103 C  C   . PHE   A 1 294 ? -2.880  19.836 57.534  1.00 47.22 ? 283 PHE   A C   1 
ATOM   2104 O  O   . PHE   A 1 294 ? -3.170  19.452 58.666  1.00 47.69 ? 283 PHE   A O   1 
ATOM   2105 C  CB  . PHE   A 1 294 ? -2.451  22.277 57.411  1.00 44.54 ? 283 PHE   A CB  1 
ATOM   2106 C  CG  . PHE   A 1 294 ? -2.654  23.584 56.685  1.00 43.79 ? 283 PHE   A CG  1 
ATOM   2107 C  CD1 . PHE   A 1 294 ? -3.522  24.541 57.175  1.00 43.91 ? 283 PHE   A CD1 1 
ATOM   2108 C  CD2 . PHE   A 1 294 ? -1.963  23.863 55.527  1.00 43.77 ? 283 PHE   A CD2 1 
ATOM   2109 C  CE1 . PHE   A 1 294 ? -3.700  25.740 56.509  1.00 44.28 ? 283 PHE   A CE1 1 
ATOM   2110 C  CE2 . PHE   A 1 294 ? -2.156  25.059 54.860  1.00 44.29 ? 283 PHE   A CE2 1 
ATOM   2111 C  CZ  . PHE   A 1 294 ? -3.021  25.989 55.355  1.00 44.07 ? 283 PHE   A CZ  1 
ATOM   2112 N  N   . ARG   A 1 295 ? -2.013  19.201 56.744  1.00 47.79 ? 284 ARG   A N   1 
ATOM   2113 C  CA  . ARG   A 1 295 ? -1.319  17.991 57.136  1.00 49.05 ? 284 ARG   A CA  1 
ATOM   2114 C  C   . ARG   A 1 295 ? 0.173   18.208 56.960  1.00 48.73 ? 284 ARG   A C   1 
ATOM   2115 O  O   . ARG   A 1 295 ? 0.621   18.596 55.885  1.00 48.62 ? 284 ARG   A O   1 
ATOM   2116 C  CB  . ARG   A 1 295 ? -1.781  16.781 56.314  1.00 52.20 ? 284 ARG   A CB  1 
ATOM   2117 C  CG  . ARG   A 1 295 ? -3.033  16.139 56.861  1.00 58.96 ? 284 ARG   A CG  1 
ATOM   2118 C  CD  . ARG   A 1 295 ? -3.282  14.791 56.236  1.00 66.31 ? 284 ARG   A CD  1 
ATOM   2119 N  NE  . ARG   A 1 295 ? -3.809  14.907 54.877  1.00 73.72 ? 284 ARG   A NE  1 
ATOM   2120 C  CZ  . ARG   A 1 295 ? -5.097  14.789 54.561  1.00 79.12 ? 284 ARG   A CZ  1 
ATOM   2121 N  NH1 . ARG   A 1 295 ? -6.001  14.538 55.503  1.00 79.55 ? 284 ARG   A NH1 1 
ATOM   2122 N  NH2 . ARG   A 1 295 ? -5.491  14.919 53.300  1.00 80.45 ? 284 ARG   A NH2 1 
ATOM   2123 N  N   . ARG   A 1 296 ? 0.935   17.951 58.018  1.00 48.54 ? 285 ARG   A N   1 
ATOM   2124 C  CA  . ARG   A 1 296 ? 2.388   18.059 58.053  1.00 49.30 ? 285 ARG   A CA  1 
ATOM   2125 C  C   . ARG   A 1 296 ? 3.101   17.478 56.812  1.00 49.67 ? 285 ARG   A C   1 
ATOM   2126 O  O   . ARG   A 1 296 ? 3.931   18.160 56.210  1.00 49.53 ? 285 ARG   A O   1 
ATOM   2127 C  CB  . ARG   A 1 296 ? 2.904   17.378 59.340  1.00 50.56 ? 285 ARG   A CB  1 
ATOM   2128 C  CG  . ARG   A 1 296 ? 4.364   16.876 59.296  1.00 53.79 ? 285 ARG   A CG  1 
ATOM   2129 C  CD  . ARG   A 1 296 ? 4.882   16.353 60.634  1.00 56.95 ? 285 ARG   A CD  1 
ATOM   2130 N  NE  . ARG   A 1 296 ? 4.359   17.117 61.768  1.00 59.25 ? 285 ARG   A NE  1 
ATOM   2131 C  CZ  . ARG   A 1 296 ? 4.752   18.341 62.097  1.00 60.15 ? 285 ARG   A CZ  1 
ATOM   2132 N  NH1 . ARG   A 1 296 ? 5.688   18.961 61.382  1.00 58.94 ? 285 ARG   A NH1 1 
ATOM   2133 N  NH2 . ARG   A 1 296 ? 4.179   18.976 63.112  1.00 59.39 ? 285 ARG   A NH2 1 
ATOM   2134 N  N   . ASN   A 1 297 ? 2.793   16.209 56.467  1.00 49.59 ? 286 ASN   A N   1 
ATOM   2135 C  CA  . ASN   A 1 297 ? 3.423   15.469 55.377  1.00 49.92 ? 286 ASN   A CA  1 
ATOM   2136 C  C   . ASN   A 1 297 ? 3.342   16.160 54.008  1.00 48.82 ? 286 ASN   A C   1 
ATOM   2137 O  O   . ASN   A 1 297 ? 4.183   15.873 53.159  1.00 49.60 ? 286 ASN   A O   1 
ATOM   2138 C  CB  . ASN   A 1 297 ? 2.885   14.034 55.307  1.00 52.39 ? 286 ASN   A CB  1 
ATOM   2139 C  CG  . ASN   A 1 297 ? 3.418   13.259 54.129  1.00 57.00 ? 286 ASN   A CG  1 
ATOM   2140 O  OD1 . ASN   A 1 297 ? 2.767   13.175 53.074  1.00 58.31 ? 286 ASN   A OD1 1 
ATOM   2141 N  ND2 . ASN   A 1 297 ? 4.651   12.775 54.255  1.00 58.01 ? 286 ASN   A ND2 1 
ATOM   2142 N  N   . THR   A 1 298 ? 2.370   17.056 53.784  1.00 46.85 ? 287 THR   A N   1 
ATOM   2143 C  CA  . THR   A 1 298 ? 2.272   17.800 52.521  1.00 45.63 ? 287 THR   A CA  1 
ATOM   2144 C  C   . THR   A 1 298 ? 3.573   18.611 52.250  1.00 44.56 ? 287 THR   A C   1 
ATOM   2145 O  O   . THR   A 1 298 ? 4.005   18.772 51.112  1.00 44.92 ? 287 THR   A O   1 
ATOM   2146 C  CB  . THR   A 1 298 ? 1.126   18.806 52.645  1.00 46.75 ? 287 THR   A CB  1 
ATOM   2147 O  OG1 . THR   A 1 298 ? -0.059  18.155 53.118  1.00 47.45 ? 287 THR   A OG1 1 
ATOM   2148 C  CG2 . THR   A 1 298 ? 0.868   19.593 51.352  1.00 46.96 ? 287 THR   A CG2 1 
ATOM   2149 N  N   . TYR   A 1 299 ? 4.199   19.100 53.320  1.00 42.89 ? 288 TYR   A N   1 
ATOM   2150 C  CA  . TYR   A 1 299 ? 5.381   19.956 53.279  1.00 41.02 ? 288 TYR   A CA  1 
ATOM   2151 C  C   . TYR   A 1 299 ? 6.639   19.229 53.747  1.00 41.58 ? 288 TYR   A C   1 
ATOM   2152 O  O   . TYR   A 1 299 ? 7.559   19.856 54.264  1.00 41.81 ? 288 TYR   A O   1 
ATOM   2153 C  CB  . TYR   A 1 299 ? 5.120   21.164 54.188  1.00 39.28 ? 288 TYR   A CB  1 
ATOM   2154 C  CG  . TYR   A 1 299 ? 3.792   21.829 53.913  1.00 37.86 ? 288 TYR   A CG  1 
ATOM   2155 C  CD1 . TYR   A 1 299 ? 3.602   22.593 52.776  1.00 37.58 ? 288 TYR   A CD1 1 
ATOM   2156 C  CD2 . TYR   A 1 299 ? 2.694   21.612 54.744  1.00 37.92 ? 288 TYR   A CD2 1 
ATOM   2157 C  CE1 . TYR   A 1 299 ? 2.373   23.166 52.492  1.00 38.17 ? 288 TYR   A CE1 1 
ATOM   2158 C  CE2 . TYR   A 1 299 ? 1.459   22.184 54.471  1.00 37.80 ? 288 TYR   A CE2 1 
ATOM   2159 C  CZ  . TYR   A 1 299 ? 1.314   22.983 53.357  1.00 38.58 ? 288 TYR   A CZ  1 
ATOM   2160 O  OH  . TYR   A 1 299 ? 0.114   23.551 53.042  1.00 40.22 ? 288 TYR   A OH  1 
ATOM   2161 N  N   . THR   A 1 300 ? 6.696   17.922 53.548  1.00 41.91 ? 289 THR   A N   1 
ATOM   2162 C  CA  . THR   A 1 300 ? 7.802   17.103 54.012  1.00 42.37 ? 289 THR   A CA  1 
ATOM   2163 C  C   . THR   A 1 300 ? 9.148   17.483 53.343  1.00 41.94 ? 289 THR   A C   1 
ATOM   2164 O  O   . THR   A 1 300 ? 10.162  17.536 54.038  1.00 42.35 ? 289 THR   A O   1 
ATOM   2165 C  CB  . THR   A 1 300 ? 7.429   15.619 53.887  1.00 43.85 ? 289 THR   A CB  1 
ATOM   2166 O  OG1 . THR   A 1 300 ? 8.351   14.861 54.654  1.00 45.36 ? 289 THR   A OG1 1 
ATOM   2167 C  CG2 . THR   A 1 300 ? 7.414   15.133 52.453  1.00 44.35 ? 289 THR   A CG2 1 
ATOM   2168 N  N   . ASN   A 1 301 ? 9.157   17.804 52.045  1.00 41.09 ? 290 ASN   A N   1 
ATOM   2169 C  CA  . ASN   A 1 301 ? 10.405  18.209 51.376  1.00 41.18 ? 290 ASN   A CA  1 
ATOM   2170 C  C   . ASN   A 1 301 ? 10.542  19.750 51.306  1.00 39.75 ? 290 ASN   A C   1 
ATOM   2171 O  O   . ASN   A 1 301 ? 11.196  20.266 50.404  1.00 39.97 ? 290 ASN   A O   1 
ATOM   2172 C  CB  . ASN   A 1 301 ? 10.462  17.617 49.956  1.00 43.31 ? 290 ASN   A CB  1 
ATOM   2173 C  CG  . ASN   A 1 301 ? 10.567  16.117 49.933  1.00 48.38 ? 290 ASN   A CG  1 
ATOM   2174 O  OD1 . ASN   A 1 301 ? 11.306  15.505 50.715  1.00 49.32 ? 290 ASN   A OD1 1 
ATOM   2175 N  ND2 . ASN   A 1 301 ? 9.821   15.491 49.032  1.00 50.21 ? 290 ASN   A ND2 1 
ATOM   2176 N  N   . CYS   A 1 302 ? 9.892   20.477 52.219  1.00 37.92 ? 291 CYS   A N   1 
ATOM   2177 C  CA  . CYS   A 1 302 ? 9.903   21.931 52.207  1.00 36.33 ? 291 CYS   A CA  1 
ATOM   2178 C  C   . CYS   A 1 302 ? 10.763  22.462 53.306  1.00 35.22 ? 291 CYS   A C   1 
ATOM   2179 O  O   . CYS   A 1 302 ? 10.607  22.040 54.447  1.00 34.74 ? 291 CYS   A O   1 
ATOM   2180 C  CB  . CYS   A 1 302 ? 8.481   22.475 52.311  1.00 36.02 ? 291 CYS   A CB  1 
ATOM   2181 S  SG  . CYS   A 1 302 ? 7.441   22.086 50.883  1.00 37.03 ? 291 CYS   A SG  1 
ATOM   2182 N  N   . SER   A 1 303 ? 11.679  23.383 52.971  1.00 34.82 ? 292 SER   A N   1 
ATOM   2183 C  CA  . SER   A 1 303 ? 12.542  24.051 53.955  1.00 35.03 ? 292 SER   A CA  1 
ATOM   2184 C  C   . SER   A 1 303 ? 13.099  25.366 53.413  1.00 34.75 ? 292 SER   A C   1 
ATOM   2185 O  O   . SER   A 1 303 ? 13.146  25.567 52.194  1.00 35.62 ? 292 SER   A O   1 
ATOM   2186 C  CB  . SER   A 1 303 ? 13.670  23.146 54.443  1.00 36.00 ? 292 SER   A CB  1 
ATOM   2187 O  OG  . SER   A 1 303 ? 14.658  22.978 53.443  1.00 38.99 ? 292 SER   A OG  1 
ATOM   2188 N  N   . LEU   A 1 304 ? 13.490  26.286 54.310  1.00 33.42 ? 293 LEU   A N   1 
ATOM   2189 C  CA  . LEU   A 1 304 ? 14.083  27.559 53.908  1.00 32.71 ? 293 LEU   A CA  1 
ATOM   2190 C  C   . LEU   A 1 304 ? 15.372  27.314 53.107  1.00 33.15 ? 293 LEU   A C   1 
ATOM   2191 O  O   . LEU   A 1 304 ? 15.583  27.960 52.086  1.00 32.69 ? 293 LEU   A O   1 
ATOM   2192 C  CB  . LEU   A 1 304 ? 14.362  28.418 55.142  1.00 32.34 ? 293 LEU   A CB  1 
ATOM   2193 C  CG  . LEU   A 1 304 ? 14.813  29.849 54.864  1.00 33.09 ? 293 LEU   A CG  1 
ATOM   2194 C  CD1 . LEU   A 1 304 ? 13.740  30.630 54.109  1.00 32.99 ? 293 LEU   A CD1 1 
ATOM   2195 C  CD2 . LEU   A 1 304 ? 15.175  30.563 56.154  1.00 33.17 ? 293 LEU   A CD2 1 
ATOM   2196 N  N   . ILE   A 1 305 ? 16.169  26.301 53.508  1.00 34.09 ? 294 ILE   A N   1 
ATOM   2197 C  CA  . ILE   A 1 305 ? 17.390  25.880 52.811  1.00 35.68 ? 294 ILE   A CA  1 
ATOM   2198 C  C   . ILE   A 1 305 ? 17.097  25.592 51.334  1.00 36.78 ? 294 ILE   A C   1 
ATOM   2199 O  O   . ILE   A 1 305 ? 17.747  26.159 50.454  1.00 36.82 ? 294 ILE   A O   1 
ATOM   2200 C  CB  . ILE   A 1 305 ? 18.020  24.646 53.534  1.00 36.73 ? 294 ILE   A CB  1 
ATOM   2201 C  CG1 . ILE   A 1 305 ? 18.720  25.062 54.836  1.00 37.85 ? 294 ILE   A CG1 1 
ATOM   2202 C  CG2 . ILE   A 1 305 ? 18.977  23.850 52.629  1.00 37.69 ? 294 ILE   A CG2 1 
ATOM   2203 C  CD1 . ILE   A 1 305 ? 18.982  23.972 55.741  1.00 38.72 ? 294 ILE   A CD1 1 
ATOM   2204 N  N   . LYS   A 1 306 ? 16.096  24.736 51.068  1.00 37.24 ? 295 LYS   A N   1 
ATOM   2205 C  CA  . LYS   A 1 306 ? 15.769  24.367 49.704  1.00 38.00 ? 295 LYS   A CA  1 
ATOM   2206 C  C   . LYS   A 1 306 ? 15.250  25.548 48.936  1.00 37.20 ? 295 LYS   A C   1 
ATOM   2207 O  O   . LYS   A 1 306 ? 15.672  25.764 47.813  1.00 37.25 ? 295 LYS   A O   1 
ATOM   2208 C  CB  . LYS   A 1 306 ? 14.811  23.175 49.679  1.00 41.57 ? 295 LYS   A CB  1 
ATOM   2209 C  CG  . LYS   A 1 306 ? 15.492  21.902 50.181  1.00 48.59 ? 295 LYS   A CG  1 
ATOM   2210 C  CD  . LYS   A 1 306 ? 14.583  20.677 50.126  1.00 55.05 ? 295 LYS   A CD  1 
ATOM   2211 C  CE  . LYS   A 1 306 ? 14.148  20.334 48.722  1.00 59.70 ? 295 LYS   A CE  1 
ATOM   2212 N  NZ  . LYS   A 1 306 ? 13.641  18.933 48.625  1.00 62.72 ? 295 LYS   A NZ  1 
ATOM   2213 N  N   . TYR   A 1 307 ? 14.400  26.372 49.564  1.00 36.43 ? 296 TYR   A N   1 
ATOM   2214 C  CA  . TYR   A 1 307 ? 13.892  27.578 48.916  1.00 35.79 ? 296 TYR   A CA  1 
ATOM   2215 C  C   . TYR   A 1 307 ? 15.033  28.520 48.481  1.00 36.05 ? 296 TYR   A C   1 
ATOM   2216 O  O   . TYR   A 1 307 ? 15.091  28.892 47.311  1.00 36.09 ? 296 TYR   A O   1 
ATOM   2217 C  CB  . TYR   A 1 307 ? 12.864  28.320 49.808  1.00 34.65 ? 296 TYR   A CB  1 
ATOM   2218 C  CG  . TYR   A 1 307 ? 12.410  29.619 49.182  1.00 34.09 ? 296 TYR   A CG  1 
ATOM   2219 C  CD1 . TYR   A 1 307 ? 11.435  29.633 48.190  1.00 33.79 ? 296 TYR   A CD1 1 
ATOM   2220 C  CD2 . TYR   A 1 307 ? 13.052  30.819 49.478  1.00 34.33 ? 296 TYR   A CD2 1 
ATOM   2221 C  CE1 . TYR   A 1 307 ? 11.078  30.815 47.549  1.00 34.12 ? 296 TYR   A CE1 1 
ATOM   2222 C  CE2 . TYR   A 1 307 ? 12.717  31.997 48.830  1.00 34.51 ? 296 TYR   A CE2 1 
ATOM   2223 C  CZ  . TYR   A 1 307 ? 11.714  31.997 47.883  1.00 34.99 ? 296 TYR   A CZ  1 
ATOM   2224 O  OH  . TYR   A 1 307 ? 11.351  33.188 47.303  1.00 36.00 ? 296 TYR   A OH  1 
ATOM   2225 N  N   . MET   A 1 308 ? 15.914  28.904 49.423  1.00 36.26 ? 297 MET   A N   1 
ATOM   2226 C  CA  . MET   A 1 308 ? 17.020  29.808 49.149  1.00 37.72 ? 297 MET   A CA  1 
ATOM   2227 C  C   . MET   A 1 308 ? 18.012  29.211 48.159  1.00 39.19 ? 297 MET   A C   1 
ATOM   2228 O  O   . MET   A 1 308 ? 18.597  29.964 47.392  1.00 39.00 ? 297 MET   A O   1 
ATOM   2229 C  CB  . MET   A 1 308 ? 17.711  30.293 50.442  1.00 38.08 ? 297 MET   A CB  1 
ATOM   2230 C  CG  . MET   A 1 308 ? 16.817  31.150 51.347  1.00 39.67 ? 297 MET   A CG  1 
ATOM   2231 S  SD  . MET   A 1 308 ? 16.001  32.587 50.575  1.00 43.80 ? 297 MET   A SD  1 
ATOM   2232 C  CE  . MET   A 1 308 ? 17.335  33.639 50.351  1.00 43.15 ? 297 MET   A CE  1 
ATOM   2233 N  N   . GLU   A 1 309 ? 18.158  27.862 48.132  1.00 40.27 ? 298 GLU   A N   1 
ATOM   2234 C  CA  . GLU   A 1 309 ? 19.014  27.159 47.178  1.00 41.40 ? 298 GLU   A CA  1 
ATOM   2235 C  C   . GLU   A 1 309 ? 18.499  27.385 45.766  1.00 41.96 ? 298 GLU   A C   1 
ATOM   2236 O  O   . GLU   A 1 309 ? 19.299  27.681 44.883  1.00 42.45 ? 298 GLU   A O   1 
ATOM   2237 C  CB  . GLU   A 1 309 ? 19.062  25.647 47.475  1.00 44.09 ? 298 GLU   A CB  1 
ATOM   2238 C  CG  . GLU   A 1 309 ? 20.271  25.239 48.292  1.00 48.61 ? 298 GLU   A CG  1 
ATOM   2239 C  CD  . GLU   A 1 309 ? 20.326  23.787 48.713  1.00 55.56 ? 298 GLU   A CD  1 
ATOM   2240 O  OE1 . GLU   A 1 309 ? 19.355  23.043 48.438  1.00 56.94 ? 298 GLU   A OE1 1 
ATOM   2241 O  OE2 . GLU   A 1 309 ? 21.349  23.389 49.317  1.00 57.88 ? 298 GLU   A OE2 1 
ATOM   2242 N  N   . LYS   A 1 310 ? 17.169  27.291 45.554  1.00 41.81 ? 299 LYS   A N   1 
ATOM   2243 C  CA  . LYS   A 1 310 ? 16.559  27.544 44.241  1.00 42.32 ? 299 LYS   A CA  1 
ATOM   2244 C  C   . LYS   A 1 310 ? 16.849  28.974 43.757  1.00 42.83 ? 299 LYS   A C   1 
ATOM   2245 O  O   . LYS   A 1 310 ? 17.065  29.203 42.564  1.00 42.92 ? 299 LYS   A O   1 
ATOM   2246 C  CB  . LYS   A 1 310 ? 15.042  27.314 44.275  1.00 44.02 ? 299 LYS   A CB  1 
ATOM   2247 C  CG  . LYS   A 1 310 ? 14.649  25.910 44.704  1.00 49.14 ? 299 LYS   A CG  1 
ATOM   2248 C  CD  . LYS   A 1 310 ? 13.146  25.659 44.526  1.00 54.32 ? 299 LYS   A CD  1 
ATOM   2249 C  CE  . LYS   A 1 310 ? 12.719  24.329 45.097  1.00 58.28 ? 299 LYS   A CE  1 
ATOM   2250 N  NZ  . LYS   A 1 310 ? 13.583  23.215 44.614  1.00 61.42 ? 299 LYS   A NZ  1 
ATOM   2251 N  N   . HIS   A 1 311 ? 16.884  29.925 44.690  1.00 42.67 ? 300 HIS   A N   1 
ATOM   2252 C  CA  . HIS   A 1 311 ? 17.165  31.311 44.373  1.00 43.30 ? 300 HIS   A CA  1 
ATOM   2253 C  C   . HIS   A 1 311 ? 18.651  31.693 44.463  1.00 45.14 ? 300 HIS   A C   1 
ATOM   2254 O  O   . HIS   A 1 311 ? 18.975  32.872 44.555  1.00 46.21 ? 300 HIS   A O   1 
ATOM   2255 C  CB  . HIS   A 1 311 ? 16.296  32.216 45.224  1.00 42.80 ? 300 HIS   A CB  1 
ATOM   2256 C  CG  . HIS   A 1 311 ? 14.854  32.038 44.898  1.00 43.37 ? 300 HIS   A CG  1 
ATOM   2257 N  ND1 . HIS   A 1 311 ? 14.289  32.652 43.803  1.00 44.47 ? 300 HIS   A ND1 1 
ATOM   2258 C  CD2 . HIS   A 1 311 ? 13.931  31.231 45.472  1.00 44.62 ? 300 HIS   A CD2 1 
ATOM   2259 C  CE1 . HIS   A 1 311 ? 13.032  32.243 43.768  1.00 45.09 ? 300 HIS   A CE1 1 
ATOM   2260 N  NE2 . HIS   A 1 311 ? 12.769  31.391 44.756  1.00 45.44 ? 300 HIS   A NE2 1 
ATOM   2261 N  N   . LYS   A 1 312 ? 19.535  30.698 44.393  1.00 45.48 ? 301 LYS   A N   1 
ATOM   2262 C  CA  . LYS   A 1 312 ? 20.984  30.812 44.360  1.00 46.34 ? 301 LYS   A CA  1 
ATOM   2263 C  C   . LYS   A 1 312 ? 21.609  31.498 45.569  1.00 46.29 ? 301 LYS   A C   1 
ATOM   2264 O  O   . LYS   A 1 312 ? 22.655  32.120 45.437  1.00 46.98 ? 301 LYS   A O   1 
ATOM   2265 C  CB  . LYS   A 1 312 ? 21.447  31.458 43.046  1.00 48.88 ? 301 LYS   A CB  1 
ATOM   2266 C  CG  . LYS   A 1 312 ? 21.449  30.433 41.910  1.00 54.53 ? 301 LYS   A CG  1 
ATOM   2267 C  CD  . LYS   A 1 312 ? 21.306  31.069 40.527  1.00 61.19 ? 301 LYS   A CD  1 
ATOM   2268 C  CE  . LYS   A 1 312 ? 21.439  30.047 39.421  1.00 66.51 ? 301 LYS   A CE  1 
ATOM   2269 N  NZ  . LYS   A 1 312 ? 21.062  30.610 38.088  1.00 70.10 ? 301 LYS   A NZ  1 
ATOM   2270 N  N   . VAL   A 1 313 ? 21.034  31.308 46.758  1.00 45.38 ? 302 VAL   A N   1 
ATOM   2271 C  CA  . VAL   A 1 313 ? 21.596  31.860 47.985  1.00 44.94 ? 302 VAL   A CA  1 
ATOM   2272 C  C   . VAL   A 1 313 ? 22.157  30.678 48.754  1.00 45.25 ? 302 VAL   A C   1 
ATOM   2273 O  O   . VAL   A 1 313 ? 21.421  29.728 49.021  1.00 45.55 ? 302 VAL   A O   1 
ATOM   2274 C  CB  . VAL   A 1 313 ? 20.535  32.649 48.789  1.00 44.92 ? 302 VAL   A CB  1 
ATOM   2275 C  CG1 . VAL   A 1 313 ? 20.993  32.912 50.223  1.00 44.91 ? 302 VAL   A CG1 1 
ATOM   2276 C  CG2 . VAL   A 1 313 ? 20.176  33.949 48.077  1.00 44.82 ? 302 VAL   A CG2 1 
ATOM   2277 N  N   . LYS   A 1 314 ? 23.466  30.690 49.053  1.00 45.20 ? 303 LYS   A N   1 
ATOM   2278 C  CA  . LYS   A 1 314 ? 24.106  29.547 49.708  1.00 45.64 ? 303 LYS   A CA  1 
ATOM   2279 C  C   . LYS   A 1 314 ? 23.704  29.334 51.177  1.00 45.28 ? 303 LYS   A C   1 
ATOM   2280 O  O   . LYS   A 1 314 ? 23.853  30.214 52.025  1.00 44.98 ? 303 LYS   A O   1 
ATOM   2281 C  CB  . LYS   A 1 314 ? 25.632  29.603 49.564  1.00 48.39 ? 303 LYS   A CB  1 
ATOM   2282 C  CG  . LYS   A 1 314 ? 26.075  29.467 48.111  1.00 53.66 ? 303 LYS   A CG  1 
ATOM   2283 C  CD  . LYS   A 1 314 ? 27.586  29.312 47.960  1.00 59.17 ? 303 LYS   A CD  1 
ATOM   2284 C  CE  . LYS   A 1 314 ? 27.966  29.104 46.504  1.00 63.86 ? 303 LYS   A CE  1 
ATOM   2285 N  NZ  . LYS   A 1 314 ? 29.290  28.430 46.347  1.00 66.49 ? 303 LYS   A NZ  1 
ATOM   2286 N  N   . PRO   A 1 315 ? 23.212  28.124 51.492  1.00 44.79 ? 304 PRO   A N   1 
ATOM   2287 C  CA  . PRO   A 1 315 ? 22.804  27.837 52.880  1.00 44.02 ? 304 PRO   A CA  1 
ATOM   2288 C  C   . PRO   A 1 315 ? 23.942  27.867 53.897  1.00 42.77 ? 304 PRO   A C   1 
ATOM   2289 O  O   . PRO   A 1 315 ? 23.687  28.004 55.091  1.00 43.14 ? 304 PRO   A O   1 
ATOM   2290 C  CB  . PRO   A 1 315 ? 22.175  26.445 52.794  1.00 45.05 ? 304 PRO   A CB  1 
ATOM   2291 C  CG  . PRO   A 1 315 ? 21.889  26.233 51.338  1.00 45.74 ? 304 PRO   A CG  1 
ATOM   2292 C  CD  . PRO   A 1 315 ? 22.939  26.986 50.596  1.00 44.23 ? 304 PRO   A CD  1 
ATOM   2293 N  N   . ASP   A 1 316 ? 25.186  27.745 53.442  1.00 41.45 ? 305 ASP   A N   1 
ATOM   2294 C  CA  . ASP   A 1 316 ? 26.325  27.789 54.363  1.00 40.74 ? 305 ASP   A CA  1 
ATOM   2295 C  C   . ASP   A 1 316 ? 26.812  29.234 54.621  1.00 37.70 ? 305 ASP   A C   1 
ATOM   2296 O  O   . ASP   A 1 316 ? 27.700  29.431 55.432  1.00 37.68 ? 305 ASP   A O   1 
ATOM   2297 C  CB  . ASP   A 1 316 ? 27.461  26.844 53.926  1.00 44.47 ? 305 ASP   A CB  1 
ATOM   2298 C  CG  . ASP   A 1 316 ? 27.720  26.819 52.430  1.00 55.33 ? 305 ASP   A CG  1 
ATOM   2299 O  OD1 . ASP   A 1 316 ? 26.840  26.309 51.676  1.00 57.43 ? 305 ASP   A OD1 1 
ATOM   2300 O  OD2 . ASP   A 1 316 ? 28.811  27.289 52.004  1.00 59.58 ? 305 ASP   A OD2 1 
ATOM   2301 N  N   . SER   A 1 317 ? 26.213  30.232 53.970  1.00 34.97 ? 306 SER   A N   1 
ATOM   2302 C  CA  . SER   A 1 317 ? 26.581  31.610 54.152  1.00 33.29 ? 306 SER   A CA  1 
ATOM   2303 C  C   . SER   A 1 317 ? 26.046  32.181 55.467  1.00 31.99 ? 306 SER   A C   1 
ATOM   2304 O  O   . SER   A 1 317 ? 25.009  31.751 55.964  1.00 31.90 ? 306 SER   A O   1 
ATOM   2305 C  CB  . SER   A 1 317 ? 26.055  32.443 52.992  1.00 33.73 ? 306 SER   A CB  1 
ATOM   2306 O  OG  . SER   A 1 317 ? 24.639  32.438 53.005  1.00 35.43 ? 306 SER   A OG  1 
ATOM   2307 N  N   . LYS   A 1 318 ? 26.733  33.198 55.984  1.00 30.56 ? 307 LYS   A N   1 
ATOM   2308 C  CA  . LYS   A 1 318 ? 26.316  33.947 57.151  1.00 29.69 ? 307 LYS   A CA  1 
ATOM   2309 C  C   . LYS   A 1 318 ? 24.978  34.678 56.879  1.00 29.14 ? 307 LYS   A C   1 
ATOM   2310 O  O   . LYS   A 1 318 ? 24.133  34.800 57.786  1.00 29.21 ? 307 LYS   A O   1 
ATOM   2311 C  CB  . LYS   A 1 318 ? 27.420  34.925 57.573  1.00 30.54 ? 307 LYS   A CB  1 
ATOM   2312 C  CG  . LYS   A 1 318 ? 28.718  34.204 57.937  1.00 34.41 ? 307 LYS   A CG  1 
ATOM   2313 C  CD  . LYS   A 1 318 ? 29.513  34.998 58.952  1.00 39.41 ? 307 LYS   A CD  1 
ATOM   2314 C  CE  . LYS   A 1 318 ? 30.598  34.195 59.598  1.00 42.69 ? 307 LYS   A CE  1 
ATOM   2315 N  NZ  . LYS   A 1 318 ? 31.915  34.464 58.961  1.00 45.70 ? 307 LYS   A NZ  1 
ATOM   2316 N  N   . ALA   A 1 319 ? 24.770  35.134 55.627  1.00 28.17 ? 308 ALA   A N   1 
ATOM   2317 C  CA  . ALA   A 1 319 ? 23.521  35.774 55.204  1.00 27.34 ? 308 ALA   A CA  1 
ATOM   2318 C  C   . ALA   A 1 319 ? 22.344  34.803 55.434  1.00 27.71 ? 308 ALA   A C   1 
ATOM   2319 O  O   . ALA   A 1 319 ? 21.384  35.194 56.084  1.00 28.47 ? 308 ALA   A O   1 
ATOM   2320 C  CB  . ALA   A 1 319 ? 23.593  36.170 53.730  1.00 26.09 ? 308 ALA   A CB  1 
ATOM   2321 N  N   . PHE   A 1 320 ? 22.469  33.525 54.994  1.00 26.94 ? 309 PHE   A N   1 
ATOM   2322 C  CA  . PHE   A 1 320 ? 21.413  32.531 55.152  1.00 26.94 ? 309 PHE   A CA  1 
ATOM   2323 C  C   . PHE   A 1 320 ? 21.118  32.265 56.624  1.00 27.62 ? 309 PHE   A C   1 
ATOM   2324 O  O   . PHE   A 1 320 ? 19.955  32.327 57.017  1.00 27.92 ? 309 PHE   A O   1 
ATOM   2325 C  CB  . PHE   A 1 320 ? 21.729  31.222 54.419  1.00 26.38 ? 309 PHE   A CB  1 
ATOM   2326 C  CG  . PHE   A 1 320 ? 20.601  30.229 54.584  1.00 26.90 ? 309 PHE   A CG  1 
ATOM   2327 C  CD1 . PHE   A 1 320 ? 19.508  30.243 53.725  1.00 27.57 ? 309 PHE   A CD1 1 
ATOM   2328 C  CD2 . PHE   A 1 320 ? 20.593  29.336 55.640  1.00 27.00 ? 309 PHE   A CD2 1 
ATOM   2329 C  CE1 . PHE   A 1 320 ? 18.454  29.375 53.915  1.00 27.78 ? 309 PHE   A CE1 1 
ATOM   2330 C  CE2 . PHE   A 1 320 ? 19.513  28.503 55.850  1.00 27.55 ? 309 PHE   A CE2 1 
ATOM   2331 C  CZ  . PHE   A 1 320 ? 18.458  28.529 54.987  1.00 27.75 ? 309 PHE   A CZ  1 
ATOM   2332 N  N   . HIS   A 1 321 ? 22.164  31.993 57.435  1.00 27.34 ? 310 HIS   A N   1 
ATOM   2333 C  CA  . HIS   A 1 321 ? 22.001  31.727 58.859  1.00 28.00 ? 310 HIS   A CA  1 
ATOM   2334 C  C   . HIS   A 1 321 ? 21.298  32.874 59.580  1.00 28.36 ? 310 HIS   A C   1 
ATOM   2335 O  O   . HIS   A 1 321 ? 20.434  32.602 60.398  1.00 29.23 ? 310 HIS   A O   1 
ATOM   2336 C  CB  . HIS   A 1 321 ? 23.330  31.329 59.516  1.00 28.43 ? 310 HIS   A CB  1 
ATOM   2337 C  CG  . HIS   A 1 321 ? 23.755  29.955 59.127  1.00 30.49 ? 310 HIS   A CG  1 
ATOM   2338 N  ND1 . HIS   A 1 321 ? 23.521  28.868 59.953  1.00 32.20 ? 310 HIS   A ND1 1 
ATOM   2339 C  CD2 . HIS   A 1 321 ? 24.321  29.517 57.973  1.00 31.62 ? 310 HIS   A CD2 1 
ATOM   2340 C  CE1 . HIS   A 1 321 ? 23.986  27.815 59.294  1.00 32.71 ? 310 HIS   A CE1 1 
ATOM   2341 N  NE2 . HIS   A 1 321 ? 24.476  28.157 58.099  1.00 32.35 ? 310 HIS   A NE2 1 
ATOM   2342 N  N   . LEU   A 1 322 ? 21.566  34.130 59.194  1.00 27.66 ? 311 LEU   A N   1 
ATOM   2343 C  CA  . LEU   A 1 322 ? 20.863  35.274 59.757  1.00 27.63 ? 311 LEU   A CA  1 
ATOM   2344 C  C   . LEU   A 1 322 ? 19.405  35.323 59.287  1.00 27.76 ? 311 LEU   A C   1 
ATOM   2345 O  O   . LEU   A 1 322 ? 18.499  35.477 60.116  1.00 28.21 ? 311 LEU   A O   1 
ATOM   2346 C  CB  . LEU   A 1 322 ? 21.577  36.605 59.475  1.00 27.32 ? 311 LEU   A CB  1 
ATOM   2347 C  CG  . LEU   A 1 322 ? 20.904  37.837 60.081  1.00 27.79 ? 311 LEU   A CG  1 
ATOM   2348 C  CD1 . LEU   A 1 322 ? 20.739  37.689 61.606  1.00 28.26 ? 311 LEU   A CD1 1 
ATOM   2349 C  CD2 . LEU   A 1 322 ? 21.650  39.119 59.711  1.00 27.71 ? 311 LEU   A CD2 1 
ATOM   2350 N  N   . LEU   A 1 323 ? 19.155  35.093 57.987  1.00 26.83 ? 312 LEU   A N   1 
ATOM   2351 C  CA  . LEU   A 1 323 ? 17.786  35.031 57.465  1.00 26.67 ? 312 LEU   A CA  1 
ATOM   2352 C  C   . LEU   A 1 323 ? 16.931  33.994 58.223  1.00 28.18 ? 312 LEU   A C   1 
ATOM   2353 O  O   . LEU   A 1 323 ? 15.809  34.297 58.622  1.00 29.19 ? 312 LEU   A O   1 
ATOM   2354 C  CB  . LEU   A 1 323 ? 17.789  34.699 55.972  1.00 25.81 ? 312 LEU   A CB  1 
ATOM   2355 C  CG  . LEU   A 1 323 ? 16.419  34.552 55.318  1.00 26.38 ? 312 LEU   A CG  1 
ATOM   2356 C  CD1 . LEU   A 1 323 ? 15.631  35.858 55.393  1.00 26.13 ? 312 LEU   A CD1 1 
ATOM   2357 C  CD2 . LEU   A 1 323 ? 16.554  34.064 53.876  1.00 26.68 ? 312 LEU   A CD2 1 
ATOM   2358 N  N   . GLN   A 1 324 ? 17.493  32.809 58.477  1.00 28.02 ? 313 GLN   A N   1 
ATOM   2359 C  CA  . GLN   A 1 324 ? 16.818  31.736 59.184  1.00 28.11 ? 313 GLN   A CA  1 
ATOM   2360 C  C   . GLN   A 1 324 ? 16.521  32.091 60.645  1.00 27.37 ? 313 GLN   A C   1 
ATOM   2361 O  O   . GLN   A 1 324 ? 15.503  31.671 61.172  1.00 28.09 ? 313 GLN   A O   1 
ATOM   2362 C  CB  . GLN   A 1 324 ? 17.641  30.449 59.061  1.00 30.70 ? 313 GLN   A CB  1 
ATOM   2363 C  CG  . GLN   A 1 324 ? 16.949  29.226 59.627  1.00 37.10 ? 313 GLN   A CG  1 
ATOM   2364 C  CD  . GLN   A 1 324 ? 17.569  27.979 59.075  1.00 45.37 ? 313 GLN   A CD  1 
ATOM   2365 O  OE1 . GLN   A 1 324 ? 16.966  27.275 58.242  1.00 48.26 ? 313 GLN   A OE1 1 
ATOM   2366 N  NE2 . GLN   A 1 324 ? 18.800  27.702 59.504  1.00 45.69 ? 313 GLN   A NE2 1 
ATOM   2367 N  N   . LYS   A 1 325 ? 17.389  32.853 61.292  1.00 26.57 ? 314 LYS   A N   1 
ATOM   2368 C  CA  . LYS   A 1 325 ? 17.150  33.310 62.650  1.00 27.06 ? 314 LYS   A CA  1 
ATOM   2369 C  C   . LYS   A 1 325 ? 16.018  34.378 62.690  1.00 28.68 ? 314 LYS   A C   1 
ATOM   2370 O  O   . LYS   A 1 325 ? 15.282  34.454 63.671  1.00 30.38 ? 314 LYS   A O   1 
ATOM   2371 C  CB  . LYS   A 1 325 ? 18.445  33.827 63.276  1.00 26.90 ? 314 LYS   A CB  1 
ATOM   2372 C  CG  . LYS   A 1 325 ? 19.448  32.706 63.452  1.00 26.33 ? 314 LYS   A CG  1 
ATOM   2373 C  CD  . LYS   A 1 325 ? 20.736  33.151 64.081  1.00 27.08 ? 314 LYS   A CD  1 
ATOM   2374 C  CE  . LYS   A 1 325 ? 21.639  31.951 64.156  1.00 28.42 ? 314 LYS   A CE  1 
ATOM   2375 N  NZ  . LYS   A 1 325 ? 23.019  32.299 64.557  1.00 29.33 ? 314 LYS   A NZ  1 
ATOM   2376 N  N   . LEU   A 1 326 ? 15.846  35.159 61.613  1.00 27.66 ? 315 LEU   A N   1 
ATOM   2377 C  CA  . LEU   A 1 326 ? 14.777  36.165 61.545  1.00 27.20 ? 315 LEU   A CA  1 
ATOM   2378 C  C   . LEU   A 1 326 ? 13.442  35.506 61.189  1.00 27.21 ? 315 LEU   A C   1 
ATOM   2379 O  O   . LEU   A 1 326 ? 12.392  35.904 61.708  1.00 26.95 ? 315 LEU   A O   1 
ATOM   2380 C  CB  . LEU   A 1 326 ? 15.109  37.237 60.502  1.00 26.45 ? 315 LEU   A CB  1 
ATOM   2381 C  CG  . LEU   A 1 326 ? 16.371  38.061 60.722  1.00 26.86 ? 315 LEU   A CG  1 
ATOM   2382 C  CD1 . LEU   A 1 326 ? 16.789  38.767 59.426  1.00 27.12 ? 315 LEU   A CD1 1 
ATOM   2383 C  CD2 . LEU   A 1 326 ? 16.168  39.096 61.787  1.00 27.19 ? 315 LEU   A CD2 1 
ATOM   2384 N  N   . LEU   A 1 327 ? 13.490  34.510 60.278  1.00 26.30 ? 316 LEU   A N   1 
ATOM   2385 C  CA  . LEU   A 1 327 ? 12.336  33.769 59.827  1.00 26.11 ? 316 LEU   A CA  1 
ATOM   2386 C  C   . LEU   A 1 327 ? 12.136  32.489 60.647  1.00 27.62 ? 316 LEU   A C   1 
ATOM   2387 O  O   . LEU   A 1 327 ? 12.149  31.391 60.104  1.00 28.98 ? 316 LEU   A O   1 
ATOM   2388 C  CB  . LEU   A 1 327 ? 12.436  33.459 58.316  1.00 25.41 ? 316 LEU   A CB  1 
ATOM   2389 C  CG  . LEU   A 1 327 ? 12.262  34.656 57.351  1.00 25.97 ? 316 LEU   A CG  1 
ATOM   2390 C  CD1 . LEU   A 1 327 ? 12.242  34.203 55.894  1.00 25.47 ? 316 LEU   A CD1 1 
ATOM   2391 C  CD2 . LEU   A 1 327 ? 10.996  35.459 57.671  1.00 26.17 ? 316 LEU   A CD2 1 
ATOM   2392 N  N   . THR   A 1 328 ? 11.979  32.623 61.948  1.00 27.32 ? 317 THR   A N   1 
ATOM   2393 C  CA  . THR   A 1 328 ? 11.708  31.492 62.815  1.00 27.97 ? 317 THR   A CA  1 
ATOM   2394 C  C   . THR   A 1 328 ? 10.206  31.486 63.027  1.00 28.53 ? 317 THR   A C   1 
ATOM   2395 O  O   . THR   A 1 328 ? 9.664   32.518 63.357  1.00 29.48 ? 317 THR   A O   1 
ATOM   2396 C  CB  . THR   A 1 328 ? 12.487  31.661 64.109  1.00 29.83 ? 317 THR   A CB  1 
ATOM   2397 O  OG1 . THR   A 1 328 ? 13.884  31.618 63.791  1.00 31.22 ? 317 THR   A OG1 1 
ATOM   2398 C  CG2 . THR   A 1 328 ? 12.168  30.603 65.100  1.00 30.14 ? 317 THR   A CG2 1 
ATOM   2399 N  N   . MET   A 1 329 ? 9.519   30.369 62.804  1.00 28.50 ? 318 MET   A N   1 
ATOM   2400 C  CA  . MET   A 1 329 ? 8.057   30.306 62.965  1.00 28.88 ? 318 MET   A CA  1 
ATOM   2401 C  C   . MET   A 1 329 ? 7.593   30.709 64.373  1.00 28.30 ? 318 MET   A C   1 
ATOM   2402 O  O   . MET   A 1 329 ? 6.722   31.563 64.505  1.00 27.87 ? 318 MET   A O   1 
ATOM   2403 C  CB  . MET   A 1 329 ? 7.528   28.915 62.612  1.00 29.80 ? 318 MET   A CB  1 
ATOM   2404 C  CG  . MET   A 1 329 ? 8.008   28.444 61.291  1.00 34.69 ? 318 MET   A CG  1 
ATOM   2405 S  SD  . MET   A 1 329 ? 6.947   29.036 59.989  1.00 43.58 ? 318 MET   A SD  1 
ATOM   2406 C  CE  . MET   A 1 329 ? 5.594   28.017 60.239  1.00 36.30 ? 318 MET   A CE  1 
ATOM   2407 N  N   . ASP   A 1 330 ? 8.184   30.110 65.409  1.00 28.27 ? 319 ASP   A N   1 
ATOM   2408 C  CA  . ASP   A 1 330 ? 7.814   30.439 66.782  1.00 28.65 ? 319 ASP   A CA  1 
ATOM   2409 C  C   . ASP   A 1 330 ? 8.372   31.810 67.093  1.00 29.49 ? 319 ASP   A C   1 
ATOM   2410 O  O   . ASP   A 1 330 ? 9.588   31.995 67.034  1.00 29.74 ? 319 ASP   A O   1 
ATOM   2411 C  CB  . ASP   A 1 330 ? 8.369   29.393 67.747  1.00 29.08 ? 319 ASP   A CB  1 
ATOM   2412 C  CG  . ASP   A 1 330 ? 7.879   29.509 69.174  1.00 32.79 ? 319 ASP   A CG  1 
ATOM   2413 O  OD1 . ASP   A 1 330 ? 7.247   30.530 69.507  1.00 33.35 ? 319 ASP   A OD1 1 
ATOM   2414 O  OD2 . ASP   A 1 330 ? 8.130   28.583 69.959  1.00 34.18 ? 319 ASP   A OD2 1 
ATOM   2415 N  N   . PRO   A 1 331 ? 7.489   32.795 67.376  1.00 29.39 ? 320 PRO   A N   1 
ATOM   2416 C  CA  . PRO   A 1 331 ? 7.973   34.147 67.685  1.00 29.23 ? 320 PRO   A CA  1 
ATOM   2417 C  C   . PRO   A 1 331 ? 8.906   34.226 68.894  1.00 29.62 ? 320 PRO   A C   1 
ATOM   2418 O  O   . PRO   A 1 331 ? 9.847   35.039 68.877  1.00 29.86 ? 320 PRO   A O   1 
ATOM   2419 C  CB  . PRO   A 1 331 ? 6.683   34.927 67.958  1.00 30.08 ? 320 PRO   A CB  1 
ATOM   2420 C  CG  . PRO   A 1 331 ? 5.648   33.879 68.338  1.00 30.25 ? 320 PRO   A CG  1 
ATOM   2421 C  CD  . PRO   A 1 331 ? 6.013   32.716 67.445  1.00 28.71 ? 320 PRO   A CD  1 
ATOM   2422 N  N   . ILE   A 1 332 ? 8.656   33.421 69.952  1.00 29.12 ? 321 ILE   A N   1 
ATOM   2423 C  CA  . ILE   A 1 332 ? 9.545   33.444 71.124  1.00 29.49 ? 321 ILE   A CA  1 
ATOM   2424 C  C   . ILE   A 1 332 ? 10.961  32.936 70.763  1.00 28.27 ? 321 ILE   A C   1 
ATOM   2425 O  O   . ILE   A 1 332 ? 11.900  33.194 71.515  1.00 28.61 ? 321 ILE   A O   1 
ATOM   2426 C  CB  . ILE   A 1 332 ? 8.972   32.710 72.381  1.00 30.95 ? 321 ILE   A CB  1 
ATOM   2427 C  CG1 . ILE   A 1 332 ? 8.874   31.210 72.138  1.00 32.32 ? 321 ILE   A CG1 1 
ATOM   2428 C  CG2 . ILE   A 1 332 ? 7.643   33.302 72.865  1.00 31.25 ? 321 ILE   A CG2 1 
ATOM   2429 C  CD1 . ILE   A 1 332 ? 8.726   30.419 73.328  1.00 34.58 ? 321 ILE   A CD1 1 
ATOM   2430 N  N   . LYS   A 1 333 ? 11.117  32.234 69.618  1.00 26.37 ? 322 LYS   A N   1 
ATOM   2431 C  CA  . LYS   A 1 333 ? 12.412  31.749 69.125  1.00 25.72 ? 322 LYS   A CA  1 
ATOM   2432 C  C   . LYS   A 1 333 ? 13.023  32.620 68.032  1.00 25.48 ? 322 LYS   A C   1 
ATOM   2433 O  O   . LYS   A 1 333 ? 14.082  32.287 67.513  1.00 25.74 ? 322 LYS   A O   1 
ATOM   2434 C  CB  . LYS   A 1 333 ? 12.325  30.292 68.640  1.00 26.84 ? 322 LYS   A CB  1 
ATOM   2435 C  CG  . LYS   A 1 333 ? 12.149  29.313 69.776  1.00 29.36 ? 322 LYS   A CG  1 
ATOM   2436 C  CD  . LYS   A 1 333 ? 12.082  27.876 69.299  1.00 31.66 ? 322 LYS   A CD  1 
ATOM   2437 C  CE  . LYS   A 1 333 ? 11.871  26.972 70.501  1.00 35.11 ? 322 LYS   A CE  1 
ATOM   2438 N  NZ  . LYS   A 1 333 ? 11.392  25.611 70.112  1.00 37.25 ? 322 LYS   A NZ  1 
ATOM   2439 N  N   . ARG   A 1 334 ? 12.372  33.723 67.672  1.00 25.12 ? 323 ARG   A N   1 
ATOM   2440 C  CA  . ARG   A 1 334 ? 12.879  34.659 66.677  1.00 25.29 ? 323 ARG   A CA  1 
ATOM   2441 C  C   . ARG   A 1 334 ? 13.971  35.524 67.346  1.00 25.56 ? 323 ARG   A C   1 
ATOM   2442 O  O   . ARG   A 1 334 ? 13.856  35.895 68.523  1.00 25.46 ? 323 ARG   A O   1 
ATOM   2443 C  CB  . ARG   A 1 334 ? 11.720  35.539 66.182  1.00 25.44 ? 323 ARG   A CB  1 
ATOM   2444 C  CG  . ARG   A 1 334 ? 11.585  35.616 64.683  1.00 26.38 ? 323 ARG   A CG  1 
ATOM   2445 C  CD  . ARG   A 1 334 ? 10.234  36.200 64.275  1.00 27.09 ? 323 ARG   A CD  1 
ATOM   2446 N  NE  . ARG   A 1 334 ? 9.245   35.148 64.060  1.00 27.49 ? 323 ARG   A NE  1 
ATOM   2447 C  CZ  . ARG   A 1 334 ? 7.936   35.282 64.243  1.00 28.80 ? 323 ARG   A CZ  1 
ATOM   2448 N  NH1 . ARG   A 1 334 ? 7.435   36.422 64.686  1.00 28.27 ? 323 ARG   A NH1 1 
ATOM   2449 N  NH2 . ARG   A 1 334 ? 7.123   34.260 64.022  1.00 29.14 ? 323 ARG   A NH2 1 
ATOM   2450 N  N   . ILE   A 1 335 ? 15.026  35.825 66.606  1.00 25.46 ? 324 ILE   A N   1 
ATOM   2451 C  CA  . ILE   A 1 335 ? 16.132  36.666 67.091  1.00 26.00 ? 324 ILE   A CA  1 
ATOM   2452 C  C   . ILE   A 1 335 ? 15.619  38.103 67.361  1.00 26.40 ? 324 ILE   A C   1 
ATOM   2453 O  O   . ILE   A 1 335 ? 14.653  38.550 66.716  1.00 26.11 ? 324 ILE   A O   1 
ATOM   2454 C  CB  . ILE   A 1 335 ? 17.154  36.665 65.926  1.00 27.24 ? 324 ILE   A CB  1 
ATOM   2455 C  CG1 . ILE   A 1 335 ? 18.549  37.113 66.334  1.00 28.26 ? 324 ILE   A CG1 1 
ATOM   2456 C  CG2 . ILE   A 1 335 ? 16.645  37.489 64.727  1.00 28.14 ? 324 ILE   A CG2 1 
ATOM   2457 C  CD1 . ILE   A 1 335 ? 19.589  37.048 65.093  1.00 29.11 ? 324 ILE   A CD1 1 
ATOM   2458 N  N   . THR   A 1 336 ? 16.260  38.840 68.291  1.00 26.72 ? 325 THR   A N   1 
ATOM   2459 C  CA  . THR   A 1 336 ? 15.879  40.242 68.498  1.00 27.45 ? 325 THR   A CA  1 
ATOM   2460 C  C   . THR   A 1 336 ? 16.614  41.099 67.453  1.00 27.86 ? 325 THR   A C   1 
ATOM   2461 O  O   . THR   A 1 336 ? 17.610  40.638 66.865  1.00 27.90 ? 325 THR   A O   1 
ATOM   2462 C  CB  . THR   A 1 336 ? 16.219  40.701 69.917  1.00 29.61 ? 325 THR   A CB  1 
ATOM   2463 O  OG1 . THR   A 1 336 ? 17.642  40.736 70.080  1.00 31.78 ? 325 THR   A OG1 1 
ATOM   2464 C  CG2 . THR   A 1 336 ? 15.563  39.849 70.991  1.00 28.67 ? 325 THR   A CG2 1 
ATOM   2465 N  N   . SER   A 1 337 ? 16.161  42.350 67.235  1.00 27.68 ? 326 SER   A N   1 
ATOM   2466 C  CA  . SER   A 1 337 ? 16.833  43.259 66.292  1.00 28.87 ? 326 SER   A CA  1 
ATOM   2467 C  C   . SER   A 1 337 ? 18.272  43.563 66.767  1.00 29.43 ? 326 SER   A C   1 
ATOM   2468 O  O   . SER   A 1 337 ? 19.181  43.644 65.945  1.00 30.20 ? 326 SER   A O   1 
ATOM   2469 C  CB  . SER   A 1 337 ? 16.055  44.567 66.150  1.00 29.96 ? 326 SER   A CB  1 
ATOM   2470 O  OG  . SER   A 1 337 ? 15.832  45.105 67.447  1.00 32.33 ? 326 SER   A OG  1 
ATOM   2471 N  N   . GLU   A 1 338 ? 18.481  43.696 68.070  1.00 29.12 ? 327 GLU   A N   1 
ATOM   2472 C  CA  . GLU   A 1 338 ? 19.815  43.951 68.607  1.00 30.25 ? 327 GLU   A CA  1 
ATOM   2473 C  C   . GLU   A 1 338 ? 20.733  42.730 68.406  1.00 30.65 ? 327 GLU   A C   1 
ATOM   2474 O  O   . GLU   A 1 338 ? 21.882  42.897 67.990  1.00 31.44 ? 327 GLU   A O   1 
ATOM   2475 C  CB  . GLU   A 1 338 ? 19.769  44.456 70.065  1.00 33.47 ? 327 GLU   A CB  1 
ATOM   2476 C  CG  . GLU   A 1 338 ? 18.888  43.650 71.006  1.00 41.80 ? 327 GLU   A CG  1 
ATOM   2477 C  CD  . GLU   A 1 338 ? 17.394  43.923 71.164  1.00 51.56 ? 327 GLU   A CD  1 
ATOM   2478 O  OE1 . GLU   A 1 338 ? 16.728  44.360 70.195  1.00 51.41 ? 327 GLU   A OE1 1 
ATOM   2479 O  OE2 . GLU   A 1 338 ? 16.876  43.623 72.267  1.00 55.97 ? 327 GLU   A OE2 1 
ATOM   2480 N  N   . GLN   A 1 339 ? 20.206  41.506 68.587  1.00 29.93 ? 328 GLN   A N   1 
ATOM   2481 C  CA  . GLN   A 1 339 ? 20.997  40.308 68.322  1.00 29.74 ? 328 GLN   A CA  1 
ATOM   2482 C  C   . GLN   A 1 339 ? 21.310  40.210 66.819  1.00 29.38 ? 328 GLN   A C   1 
ATOM   2483 O  O   . GLN   A 1 339 ? 22.417  39.827 66.453  1.00 29.45 ? 328 GLN   A O   1 
ATOM   2484 C  CB  . GLN   A 1 339 ? 20.252  39.070 68.751  1.00 31.82 ? 328 GLN   A CB  1 
ATOM   2485 C  CG  . GLN   A 1 339 ? 20.122  38.888 70.245  1.00 36.01 ? 328 GLN   A CG  1 
ATOM   2486 C  CD  . GLN   A 1 339 ? 19.384  37.600 70.466  1.00 41.22 ? 328 GLN   A CD  1 
ATOM   2487 O  OE1 . GLN   A 1 339 ? 18.161  37.504 70.290  1.00 42.20 ? 328 GLN   A OE1 1 
ATOM   2488 N  NE2 . GLN   A 1 339 ? 20.128  36.562 70.778  1.00 43.08 ? 328 GLN   A NE2 1 
ATOM   2489 N  N   . ALA   A 1 340 ? 20.352  40.586 65.946  1.00 28.29 ? 329 ALA   A N   1 
ATOM   2490 C  CA  . ALA   A 1 340 ? 20.582  40.551 64.508  1.00 27.51 ? 329 ALA   A CA  1 
ATOM   2491 C  C   . ALA   A 1 340 ? 21.732  41.508 64.127  1.00 27.59 ? 329 ALA   A C   1 
ATOM   2492 O  O   . ALA   A 1 340 ? 22.633  41.095 63.413  1.00 27.53 ? 329 ALA   A O   1 
ATOM   2493 C  CB  . ALA   A 1 340 ? 19.311  40.902 63.765  1.00 26.92 ? 329 ALA   A CB  1 
ATOM   2494 N  N   . MET   A 1 341 ? 21.771  42.716 64.706  1.00 27.35 ? 330 MET   A N   1 
ATOM   2495 C  CA  . MET   A 1 341 ? 22.838  43.704 64.456  1.00 28.28 ? 330 MET   A CA  1 
ATOM   2496 C  C   . MET   A 1 341 ? 24.234  43.211 64.878  1.00 29.03 ? 330 MET   A C   1 
ATOM   2497 O  O   . MET   A 1 341 ? 25.254  43.610 64.289  1.00 29.43 ? 330 MET   A O   1 
ATOM   2498 C  CB  . MET   A 1 341 ? 22.511  45.037 65.141  1.00 28.67 ? 330 MET   A CB  1 
ATOM   2499 C  CG  . MET   A 1 341 ? 21.336  45.781 64.492  1.00 30.94 ? 330 MET   A CG  1 
ATOM   2500 S  SD  . MET   A 1 341 ? 20.795  47.223 65.479  1.00 36.14 ? 330 MET   A SD  1 
ATOM   2501 C  CE  . MET   A 1 341 ? 22.181  48.275 65.251  1.00 33.03 ? 330 MET   A CE  1 
ATOM   2502 N  N   . GLN   A 1 342 ? 24.270  42.319 65.882  1.00 28.60 ? 331 GLN   A N   1 
ATOM   2503 C  CA  . GLN   A 1 342 ? 25.499  41.714 66.364  1.00 29.06 ? 331 GLN   A CA  1 
ATOM   2504 C  C   . GLN   A 1 342 ? 25.917  40.463 65.565  1.00 28.22 ? 331 GLN   A C   1 
ATOM   2505 O  O   . GLN   A 1 342 ? 26.979  39.901 65.830  1.00 27.93 ? 331 GLN   A O   1 
ATOM   2506 C  CB  . GLN   A 1 342 ? 25.377  41.389 67.864  1.00 31.31 ? 331 GLN   A CB  1 
ATOM   2507 C  CG  . GLN   A 1 342 ? 25.223  42.645 68.704  1.00 36.78 ? 331 GLN   A CG  1 
ATOM   2508 C  CD  . GLN   A 1 342 ? 24.641  42.383 70.075  1.00 45.76 ? 331 GLN   A CD  1 
ATOM   2509 O  OE1 . GLN   A 1 342 ? 24.199  41.271 70.409  1.00 49.09 ? 331 GLN   A OE1 1 
ATOM   2510 N  NE2 . GLN   A 1 342 ? 24.618  43.414 70.915  1.00 47.78 ? 331 GLN   A NE2 1 
ATOM   2511 N  N   . ASP   A 1 343 ? 25.100  40.017 64.599  1.00 27.57 ? 332 ASP   A N   1 
ATOM   2512 C  CA  . ASP   A 1 343 ? 25.403  38.830 63.826  1.00 28.12 ? 332 ASP   A CA  1 
ATOM   2513 C  C   . ASP   A 1 343 ? 26.747  38.935 63.114  1.00 28.87 ? 332 ASP   A C   1 
ATOM   2514 O  O   . ASP   A 1 343 ? 27.038  39.988 62.544  1.00 28.57 ? 332 ASP   A O   1 
ATOM   2515 C  CB  . ASP   A 1 343 ? 24.313  38.590 62.773  1.00 29.46 ? 332 ASP   A CB  1 
ATOM   2516 C  CG  . ASP   A 1 343 ? 24.300  37.162 62.323  1.00 32.75 ? 332 ASP   A CG  1 
ATOM   2517 O  OD1 . ASP   A 1 343 ? 25.026  36.842 61.356  1.00 33.80 ? 332 ASP   A OD1 1 
ATOM   2518 O  OD2 . ASP   A 1 343 ? 23.625  36.334 62.991  1.00 33.37 ? 332 ASP   A OD2 1 
ATOM   2519 N  N   . PRO   A 1 344 ? 27.531  37.828 63.073  1.00 29.06 ? 333 PRO   A N   1 
ATOM   2520 C  CA  . PRO   A 1 344 ? 28.821  37.867 62.361  1.00 29.17 ? 333 PRO   A CA  1 
ATOM   2521 C  C   . PRO   A 1 344 ? 28.724  38.216 60.874  1.00 29.20 ? 333 PRO   A C   1 
ATOM   2522 O  O   . PRO   A 1 344 ? 29.731  38.605 60.279  1.00 29.81 ? 333 PRO   A O   1 
ATOM   2523 C  CB  . PRO   A 1 344 ? 29.399  36.460 62.563  1.00 29.71 ? 333 PRO   A CB  1 
ATOM   2524 C  CG  . PRO   A 1 344 ? 28.268  35.619 63.078  1.00 30.14 ? 333 PRO   A CG  1 
ATOM   2525 C  CD  . PRO   A 1 344 ? 27.316  36.535 63.753  1.00 28.41 ? 333 PRO   A CD  1 
ATOM   2526 N  N   . TYR   A 1 345 ? 27.523  38.141 60.275  1.00 28.26 ? 334 TYR   A N   1 
ATOM   2527 C  CA  . TYR   A 1 345 ? 27.285  38.527 58.877  1.00 28.07 ? 334 TYR   A CA  1 
ATOM   2528 C  C   . TYR   A 1 345 ? 27.708  39.984 58.675  1.00 29.24 ? 334 TYR   A C   1 
ATOM   2529 O  O   . TYR   A 1 345 ? 28.307  40.307 57.658  1.00 30.13 ? 334 TYR   A O   1 
ATOM   2530 C  CB  . TYR   A 1 345 ? 25.786  38.384 58.571  1.00 27.22 ? 334 TYR   A CB  1 
ATOM   2531 C  CG  . TYR   A 1 345 ? 25.286  38.950 57.258  1.00 27.37 ? 334 TYR   A CG  1 
ATOM   2532 C  CD1 . TYR   A 1 345 ? 25.827  38.537 56.048  1.00 27.81 ? 334 TYR   A CD1 1 
ATOM   2533 C  CD2 . TYR   A 1 345 ? 24.202  39.817 57.221  1.00 27.83 ? 334 TYR   A CD2 1 
ATOM   2534 C  CE1 . TYR   A 1 345 ? 25.328  39.001 54.837  1.00 28.29 ? 334 TYR   A CE1 1 
ATOM   2535 C  CE2 . TYR   A 1 345 ? 23.679  40.270 56.013  1.00 28.41 ? 334 TYR   A CE2 1 
ATOM   2536 C  CZ  . TYR   A 1 345 ? 24.233  39.842 54.823  1.00 28.95 ? 334 TYR   A CZ  1 
ATOM   2537 O  OH  . TYR   A 1 345 ? 23.729  40.270 53.625  1.00 29.70 ? 334 TYR   A OH  1 
ATOM   2538 N  N   . PHE   A 1 346 ? 27.450  40.855 59.681  1.00 28.94 ? 335 PHE   A N   1 
ATOM   2539 C  CA  . PHE   A 1 346 ? 27.800  42.267 59.599  1.00 28.91 ? 335 PHE   A CA  1 
ATOM   2540 C  C   . PHE   A 1 346 ? 29.300  42.539 59.805  1.00 29.33 ? 335 PHE   A C   1 
ATOM   2541 O  O   . PHE   A 1 346 ? 29.753  43.627 59.489  1.00 28.49 ? 335 PHE   A O   1 
ATOM   2542 C  CB  . PHE   A 1 346 ? 26.921  43.100 60.530  1.00 28.04 ? 335 PHE   A CB  1 
ATOM   2543 C  CG  . PHE   A 1 346 ? 25.477  43.000 60.101  1.00 27.97 ? 335 PHE   A CG  1 
ATOM   2544 C  CD1 . PHE   A 1 346 ? 25.072  43.464 58.864  1.00 28.07 ? 335 PHE   A CD1 1 
ATOM   2545 C  CD2 . PHE   A 1 346 ? 24.526  42.419 60.927  1.00 28.18 ? 335 PHE   A CD2 1 
ATOM   2546 C  CE1 . PHE   A 1 346 ? 23.742  43.363 58.464  1.00 28.42 ? 335 PHE   A CE1 1 
ATOM   2547 C  CE2 . PHE   A 1 346 ? 23.203  42.329 60.527  1.00 28.34 ? 335 PHE   A CE2 1 
ATOM   2548 C  CZ  . PHE   A 1 346 ? 22.819  42.789 59.292  1.00 27.76 ? 335 PHE   A CZ  1 
ATOM   2549 N  N   . LEU   A 1 347 ? 30.069  41.545 60.290  1.00 29.99 ? 336 LEU   A N   1 
ATOM   2550 C  CA  . LEU   A 1 347 ? 31.529  41.635 60.422  1.00 30.85 ? 336 LEU   A CA  1 
ATOM   2551 C  C   . LEU   A 1 347 ? 32.263  41.016 59.206  1.00 31.42 ? 336 LEU   A C   1 
ATOM   2552 O  O   . LEU   A 1 347 ? 33.466  41.188 59.053  1.00 31.87 ? 336 LEU   A O   1 
ATOM   2553 C  CB  . LEU   A 1 347 ? 32.010  40.940 61.706  1.00 30.74 ? 336 LEU   A CB  1 
ATOM   2554 C  CG  . LEU   A 1 347 ? 31.368  41.404 62.992  1.00 32.40 ? 336 LEU   A CG  1 
ATOM   2555 C  CD1 . LEU   A 1 347 ? 31.895  40.598 64.187  1.00 32.81 ? 336 LEU   A CD1 1 
ATOM   2556 C  CD2 . LEU   A 1 347 ? 31.587  42.898 63.200  1.00 32.92 ? 336 LEU   A CD2 1 
ATOM   2557 N  N   . GLU   A 1 348 ? 31.553  40.260 58.380  1.00 31.50 ? 337 GLU   A N   1 
ATOM   2558 C  CA  . GLU   A 1 348 ? 32.097  39.606 57.207  1.00 31.65 ? 337 GLU   A CA  1 
ATOM   2559 C  C   . GLU   A 1 348 ? 32.189  40.624 56.062  1.00 32.21 ? 337 GLU   A C   1 
ATOM   2560 O  O   . GLU   A 1 348 ? 31.344  41.506 55.943  1.00 31.37 ? 337 GLU   A O   1 
ATOM   2561 C  CB  . GLU   A 1 348 ? 31.151  38.465 56.829  1.00 33.21 ? 337 GLU   A CB  1 
ATOM   2562 C  CG  . GLU   A 1 348 ? 31.578  37.620 55.644  1.00 37.60 ? 337 GLU   A CG  1 
ATOM   2563 C  CD  . GLU   A 1 348 ? 30.500  36.640 55.231  1.00 42.05 ? 337 GLU   A CD  1 
ATOM   2564 O  OE1 . GLU   A 1 348 ? 29.407  37.104 54.834  1.00 43.59 ? 337 GLU   A OE1 1 
ATOM   2565 O  OE2 . GLU   A 1 348 ? 30.742  35.414 55.306  1.00 42.46 ? 337 GLU   A OE2 1 
ATOM   2566 N  N   . ASP   A 1 349 ? 33.209  40.491 55.218  1.00 33.36 ? 338 ASP   A N   1 
ATOM   2567 C  CA  . ASP   A 1 349 ? 33.364  41.347 54.049  1.00 34.93 ? 338 ASP   A CA  1 
ATOM   2568 C  C   . ASP   A 1 349 ? 32.217  41.056 53.043  1.00 35.49 ? 338 ASP   A C   1 
ATOM   2569 O  O   . ASP   A 1 349 ? 31.926  39.892 52.758  1.00 35.43 ? 338 ASP   A O   1 
ATOM   2570 C  CB  . ASP   A 1 349 ? 34.740  41.094 53.399  1.00 37.46 ? 338 ASP   A CB  1 
ATOM   2571 C  CG  . ASP   A 1 349 ? 34.919  41.816 52.084  1.00 44.13 ? 338 ASP   A CG  1 
ATOM   2572 O  OD1 . ASP   A 1 349 ? 35.105  43.050 52.106  1.00 45.02 ? 338 ASP   A OD1 1 
ATOM   2573 O  OD2 . ASP   A 1 349 ? 34.824  41.154 51.029  1.00 48.01 ? 338 ASP   A OD2 1 
ATOM   2574 N  N   . PRO   A 1 350 ? 31.533  42.091 52.521  1.00 35.81 ? 339 PRO   A N   1 
ATOM   2575 C  CA  . PRO   A 1 350 ? 31.775  43.529 52.738  1.00 35.70 ? 339 PRO   A CA  1 
ATOM   2576 C  C   . PRO   A 1 350 ? 31.054  44.103 53.959  1.00 35.76 ? 339 PRO   A C   1 
ATOM   2577 O  O   . PRO   A 1 350 ? 29.989  43.614 54.297  1.00 36.14 ? 339 PRO   A O   1 
ATOM   2578 C  CB  . PRO   A 1 350 ? 31.258  44.146 51.436  1.00 36.26 ? 339 PRO   A CB  1 
ATOM   2579 C  CG  . PRO   A 1 350 ? 30.118  43.251 51.020  1.00 36.59 ? 339 PRO   A CG  1 
ATOM   2580 C  CD  . PRO   A 1 350 ? 30.442  41.862 51.545  1.00 35.38 ? 339 PRO   A CD  1 
ATOM   2581 N  N   . LEU   A 1 351 ? 31.622  45.107 54.621  1.00 35.20 ? 340 LEU   A N   1 
ATOM   2582 C  CA  . LEU   A 1 351 ? 30.970  45.730 55.773  1.00 35.87 ? 340 LEU   A CA  1 
ATOM   2583 C  C   . LEU   A 1 351 ? 29.794  46.613 55.357  1.00 34.97 ? 340 LEU   A C   1 
ATOM   2584 O  O   . LEU   A 1 351 ? 29.845  47.225 54.303  1.00 35.09 ? 340 LEU   A O   1 
ATOM   2585 C  CB  . LEU   A 1 351 ? 31.979  46.587 56.563  1.00 37.12 ? 340 LEU   A CB  1 
ATOM   2586 C  CG  . LEU   A 1 351 ? 33.135  45.865 57.284  1.00 40.35 ? 340 LEU   A CG  1 
ATOM   2587 C  CD1 . LEU   A 1 351 ? 33.717  46.767 58.372  1.00 41.38 ? 340 LEU   A CD1 1 
ATOM   2588 C  CD2 . LEU   A 1 351 ? 32.685  44.517 57.931  1.00 40.94 ? 340 LEU   A CD2 1 
ATOM   2589 N  N   . PRO   A 1 352 ? 28.727  46.715 56.170  1.00 34.35 ? 341 PRO   A N   1 
ATOM   2590 C  CA  . PRO   A 1 352 ? 27.636  47.639 55.820  1.00 34.14 ? 341 PRO   A CA  1 
ATOM   2591 C  C   . PRO   A 1 352 ? 28.139  49.090 55.767  1.00 34.07 ? 341 PRO   A C   1 
ATOM   2592 O  O   . PRO   A 1 352 ? 29.042  49.470 56.527  1.00 34.77 ? 341 PRO   A O   1 
ATOM   2593 C  CB  . PRO   A 1 352 ? 26.614  47.439 56.948  1.00 34.22 ? 341 PRO   A CB  1 
ATOM   2594 C  CG  . PRO   A 1 352 ? 27.369  46.881 58.060  1.00 34.22 ? 341 PRO   A CG  1 
ATOM   2595 C  CD  . PRO   A 1 352 ? 28.490  46.070 57.477  1.00 33.10 ? 341 PRO   A CD  1 
ATOM   2596 N  N   . THR   A 1 353 ? 27.618  49.881 54.825  1.00 32.88 ? 342 THR   A N   1 
ATOM   2597 C  CA  . THR   A 1 353 ? 28.025  51.282 54.699  1.00 32.47 ? 342 THR   A CA  1 
ATOM   2598 C  C   . THR   A 1 353 ? 26.859  52.217 55.003  1.00 32.57 ? 342 THR   A C   1 
ATOM   2599 O  O   . THR   A 1 353 ? 25.698  51.831 54.830  1.00 32.05 ? 342 THR   A O   1 
ATOM   2600 C  CB  . THR   A 1 353 ? 28.592  51.563 53.294  1.00 32.19 ? 342 THR   A CB  1 
ATOM   2601 O  OG1 . THR   A 1 353 ? 27.545  51.425 52.339  1.00 32.85 ? 342 THR   A OG1 1 
ATOM   2602 C  CG2 . THR   A 1 353 ? 29.732  50.636 52.929  1.00 31.79 ? 342 THR   A CG2 1 
ATOM   2603 N  N   . SER   A 1 354 ? 27.174  53.455 55.432  1.00 33.34 ? 343 SER   A N   1 
ATOM   2604 C  CA  . SER   A 1 354 ? 26.191  54.511 55.703  1.00 34.21 ? 343 SER   A CA  1 
ATOM   2605 C  C   . SER   A 1 354 ? 25.365  54.828 54.454  1.00 34.05 ? 343 SER   A C   1 
ATOM   2606 O  O   . SER   A 1 354 ? 24.170  55.092 54.535  1.00 33.65 ? 343 SER   A O   1 
ATOM   2607 C  CB  . SER   A 1 354 ? 26.889  55.775 56.191  1.00 36.67 ? 343 SER   A CB  1 
ATOM   2608 O  OG  . SER   A 1 354 ? 27.343  55.599 57.520  1.00 41.16 ? 343 SER   A OG  1 
ATOM   2609 N  N   . ASP   A 1 355 ? 26.006  54.793 53.302  1.00 34.57 ? 344 ASP   A N   1 
ATOM   2610 C  CA  . ASP   A 1 355 ? 25.345  54.988 52.026  1.00 35.81 ? 344 ASP   A CA  1 
ATOM   2611 C  C   . ASP   A 1 355 ? 25.193  53.572 51.454  1.00 36.39 ? 344 ASP   A C   1 
ATOM   2612 O  O   . ASP   A 1 355 ? 26.196  52.962 51.098  1.00 36.35 ? 344 ASP   A O   1 
ATOM   2613 C  CB  . ASP   A 1 355 ? 26.255  55.860 51.122  1.00 37.29 ? 344 ASP   A CB  1 
ATOM   2614 C  CG  . ASP   A 1 355 ? 25.777  56.110 49.705  1.00 40.68 ? 344 ASP   A CG  1 
ATOM   2615 O  OD1 . ASP   A 1 355 ? 24.715  55.561 49.324  1.00 40.16 ? 344 ASP   A OD1 1 
ATOM   2616 O  OD2 . ASP   A 1 355 ? 26.476  56.837 48.968  1.00 44.05 ? 344 ASP   A OD2 1 
ATOM   2617 N  N   . VAL   A 1 356 ? 23.964  53.042 51.382  1.00 36.76 ? 345 VAL   A N   1 
ATOM   2618 C  CA  . VAL   A 1 356 ? 23.723  51.710 50.830  1.00 37.96 ? 345 VAL   A CA  1 
ATOM   2619 C  C   . VAL   A 1 356 ? 24.185  51.600 49.388  1.00 40.24 ? 345 VAL   A C   1 
ATOM   2620 O  O   . VAL   A 1 356 ? 24.614  50.529 48.972  1.00 40.52 ? 345 VAL   A O   1 
ATOM   2621 C  CB  . VAL   A 1 356 ? 22.270  51.213 51.007  1.00 37.66 ? 345 VAL   A CB  1 
ATOM   2622 C  CG1 . VAL   A 1 356 ? 21.872  51.206 52.476  1.00 37.88 ? 345 VAL   A CG1 1 
ATOM   2623 C  CG2 . VAL   A 1 356 ? 21.291  52.035 50.174  1.00 37.63 ? 345 VAL   A CG2 1 
ATOM   2624 N  N   . PHE   A 1 357 ? 24.150  52.707 48.630  1.00 42.02 ? 346 PHE   A N   1 
ATOM   2625 C  CA  . PHE   A 1 357 ? 24.631  52.703 47.252  1.00 43.87 ? 346 PHE   A CA  1 
ATOM   2626 C  C   . PHE   A 1 357 ? 26.175  52.707 47.155  1.00 46.94 ? 346 PHE   A C   1 
ATOM   2627 O  O   . PHE   A 1 357 ? 26.700  52.550 46.060  1.00 47.55 ? 346 PHE   A O   1 
ATOM   2628 C  CB  . PHE   A 1 357 ? 24.013  53.856 46.450  1.00 42.97 ? 346 PHE   A CB  1 
ATOM   2629 C  CG  . PHE   A 1 357 ? 22.509  53.934 46.559  1.00 42.89 ? 346 PHE   A CG  1 
ATOM   2630 C  CD1 . PHE   A 1 357 ? 21.711  52.891 46.125  1.00 43.22 ? 346 PHE   A CD1 1 
ATOM   2631 C  CD2 . PHE   A 1 357 ? 21.895  55.042 47.111  1.00 43.45 ? 346 PHE   A CD2 1 
ATOM   2632 C  CE1 . PHE   A 1 357 ? 20.331  52.961 46.232  1.00 43.50 ? 346 PHE   A CE1 1 
ATOM   2633 C  CE2 . PHE   A 1 357 ? 20.510  55.109 47.212  1.00 43.92 ? 346 PHE   A CE2 1 
ATOM   2634 C  CZ  . PHE   A 1 357 ? 19.737  54.074 46.759  1.00 43.28 ? 346 PHE   A CZ  1 
ATOM   2635 N  N   . ALA   A 1 358 ? 26.884  52.867 48.290  1.00 49.12 ? 347 ALA   A N   1 
ATOM   2636 C  CA  . ALA   A 1 358 ? 28.340  52.875 48.427  1.00 52.18 ? 347 ALA   A CA  1 
ATOM   2637 C  C   . ALA   A 1 358 ? 29.058  53.670 47.332  1.00 55.41 ? 347 ALA   A C   1 
ATOM   2638 O  O   . ALA   A 1 358 ? 29.870  53.114 46.578  1.00 56.07 ? 347 ALA   A O   1 
ATOM   2639 C  CB  . ALA   A 1 358 ? 28.864  51.452 48.501  1.00 52.51 ? 347 ALA   A CB  1 
ATOM   2640 N  N   . GLY   A 1 359 ? 28.704  54.953 47.218  1.00 56.87 ? 348 GLY   A N   1 
ATOM   2641 C  CA  . GLY   A 1 359 ? 29.293  55.853 46.232  1.00 58.35 ? 348 GLY   A CA  1 
ATOM   2642 C  C   . GLY   A 1 359 ? 28.939  55.568 44.783  1.00 59.81 ? 348 GLY   A C   1 
ATOM   2643 O  O   . GLY   A 1 359 ? 29.183  56.418 43.924  1.00 60.53 ? 348 GLY   A O   1 
ATOM   2644 N  N   . CYS   A 1 360 ? 28.378  54.373 44.484  1.00 60.23 ? 349 CYS   A N   1 
ATOM   2645 C  CA  . CYS   A 1 360 ? 28.016  53.964 43.118  1.00 60.98 ? 349 CYS   A CA  1 
ATOM   2646 C  C   . CYS   A 1 360 ? 26.924  54.820 42.544  1.00 61.71 ? 349 CYS   A C   1 
ATOM   2647 O  O   . CYS   A 1 360 ? 26.051  55.265 43.283  1.00 61.72 ? 349 CYS   A O   1 
ATOM   2648 C  CB  . CYS   A 1 360 ? 27.624  52.488 43.061  1.00 61.16 ? 349 CYS   A CB  1 
ATOM   2649 S  SG  . CYS   A 1 360 ? 28.927  51.347 43.587  1.00 63.54 ? 349 CYS   A SG  1 
ATOM   2650 N  N   . GLN   A 1 361 ? 26.916  54.989 41.206  1.00 62.13 ? 350 GLN   A N   1 
ATOM   2651 C  CA  . GLN   A 1 361 ? 25.869  55.725 40.483  1.00 62.87 ? 350 GLN   A CA  1 
ATOM   2652 C  C   . GLN   A 1 361 ? 24.520  55.039 40.774  1.00 62.23 ? 350 GLN   A C   1 
ATOM   2653 O  O   . GLN   A 1 361 ? 24.446  53.814 40.676  1.00 62.93 ? 350 GLN   A O   1 
ATOM   2654 C  CB  . GLN   A 1 361 ? 26.133  55.670 38.957  1.00 65.51 ? 350 GLN   A CB  1 
ATOM   2655 C  CG  . GLN   A 1 361 ? 27.492  56.229 38.515  1.00 71.00 ? 350 GLN   A CG  1 
ATOM   2656 C  CD  . GLN   A 1 361 ? 27.816  55.913 37.061  1.00 77.84 ? 350 GLN   A CD  1 
ATOM   2657 O  OE1 . GLN   A 1 361 ? 27.597  54.793 36.573  1.00 80.34 ? 350 GLN   A OE1 1 
ATOM   2658 N  NE2 . GLN   A 1 361 ? 28.365  56.887 36.337  1.00 78.38 ? 350 GLN   A NE2 1 
ATOM   2659 N  N   . ILE   A 1 362 ? 23.517  55.789 41.238  1.00 60.58 ? 351 ILE   A N   1 
ATOM   2660 C  CA  . ILE   A 1 362 ? 22.211  55.199 41.536  1.00 59.29 ? 351 ILE   A CA  1 
ATOM   2661 C  C   . ILE   A 1 362 ? 21.530  54.911 40.197  1.00 58.56 ? 351 ILE   A C   1 
ATOM   2662 O  O   . ILE   A 1 362 ? 21.201  55.850 39.460  1.00 59.14 ? 351 ILE   A O   1 
ATOM   2663 C  CB  . ILE   A 1 362 ? 21.350  56.146 42.406  1.00 58.66 ? 351 ILE   A CB  1 
ATOM   2664 C  CG1 . ILE   A 1 362 ? 21.994  56.398 43.767  1.00 58.87 ? 351 ILE   A CG1 1 
ATOM   2665 C  CG2 . ILE   A 1 362 ? 19.932  55.634 42.546  1.00 58.96 ? 351 ILE   A CG2 1 
ATOM   2666 C  CD1 . ILE   A 1 362 ? 21.353  57.557 44.527  1.00 59.88 ? 351 ILE   A CD1 1 
ATOM   2667 N  N   . PRO   A 1 363 ? 21.351  53.626 39.836  1.00 56.84 ? 352 PRO   A N   1 
ATOM   2668 C  CA  . PRO   A 1 363 ? 20.698  53.327 38.548  1.00 55.85 ? 352 PRO   A CA  1 
ATOM   2669 C  C   . PRO   A 1 363 ? 19.169  53.430 38.579  1.00 54.47 ? 352 PRO   A C   1 
ATOM   2670 O  O   . PRO   A 1 363 ? 18.528  53.448 37.527  1.00 54.60 ? 352 PRO   A O   1 
ATOM   2671 C  CB  . PRO   A 1 363 ? 21.164  51.902 38.244  1.00 56.76 ? 352 PRO   A CB  1 
ATOM   2672 C  CG  . PRO   A 1 363 ? 21.412  51.283 39.605  1.00 57.43 ? 352 PRO   A CG  1 
ATOM   2673 C  CD  . PRO   A 1 363 ? 21.693  52.399 40.589  1.00 56.03 ? 352 PRO   A CD  1 
ATOM   2674 N  N   . TYR   A 1 364 ? 18.594  53.459 39.792  1.00 53.00 ? 353 TYR   A N   1 
ATOM   2675 C  CA  . TYR   A 1 364 ? 17.164  53.496 40.044  1.00 52.18 ? 353 TYR   A CA  1 
ATOM   2676 C  C   . TYR   A 1 364 ? 16.547  54.772 39.533  1.00 52.43 ? 353 TYR   A C   1 
ATOM   2677 O  O   . TYR   A 1 364 ? 17.069  55.860 39.773  1.00 52.70 ? 353 TYR   A O   1 
ATOM   2678 C  CB  . TYR   A 1 364 ? 16.870  53.301 41.545  1.00 51.29 ? 353 TYR   A CB  1 
ATOM   2679 C  CG  . TYR   A 1 364 ? 17.569  52.082 42.101  1.00 50.84 ? 353 TYR   A CG  1 
ATOM   2680 C  CD1 . TYR   A 1 364 ? 17.193  50.804 41.712  1.00 51.03 ? 353 TYR   A CD1 1 
ATOM   2681 C  CD2 . TYR   A 1 364 ? 18.672  52.208 42.930  1.00 51.06 ? 353 TYR   A CD2 1 
ATOM   2682 C  CE1 . TYR   A 1 364 ? 17.880  49.684 42.152  1.00 51.25 ? 353 TYR   A CE1 1 
ATOM   2683 C  CE2 . TYR   A 1 364 ? 19.365  51.094 43.379  1.00 51.63 ? 353 TYR   A CE2 1 
ATOM   2684 C  CZ  . TYR   A 1 364 ? 18.963  49.833 42.990  1.00 51.94 ? 353 TYR   A CZ  1 
ATOM   2685 O  OH  . TYR   A 1 364 ? 19.653  48.732 43.425  1.00 52.69 ? 353 TYR   A OH  1 
ATOM   2686 N  N   . PRO   A 1 365 ? 15.439  54.659 38.792  1.00 52.39 ? 354 PRO   A N   1 
ATOM   2687 C  CA  . PRO   A 1 365 ? 14.790  55.867 38.284  1.00 52.72 ? 354 PRO   A CA  1 
ATOM   2688 C  C   . PRO   A 1 365 ? 14.065  56.652 39.381  1.00 53.79 ? 354 PRO   A C   1 
ATOM   2689 O  O   . PRO   A 1 365 ? 13.744  56.113 40.448  1.00 54.25 ? 354 PRO   A O   1 
ATOM   2690 C  CB  . PRO   A 1 365 ? 13.807  55.317 37.252  1.00 53.06 ? 354 PRO   A CB  1 
ATOM   2691 C  CG  . PRO   A 1 365 ? 13.455  53.976 37.757  1.00 53.27 ? 354 PRO   A CG  1 
ATOM   2692 C  CD  . PRO   A 1 365 ? 14.703  53.440 38.403  1.00 51.80 ? 354 PRO   A CD  1 
ATOM   2693 N  N   . LYS   A 1 366 ? 13.807  57.930 39.115  1.00 54.05 ? 355 LYS   A N   1 
ATOM   2694 C  CA  . LYS   A 1 366 ? 13.064  58.755 40.046  1.00 54.71 ? 355 LYS   A CA  1 
ATOM   2695 C  C   . LYS   A 1 366 ? 11.592  58.303 40.072  1.00 54.81 ? 355 LYS   A C   1 
ATOM   2696 O  O   . LYS   A 1 366 ? 11.107  57.648 39.136  1.00 54.75 ? 355 LYS   A O   1 
ATOM   2697 C  CB  . LYS   A 1 366 ? 13.207  60.235 39.691  1.00 57.22 ? 355 LYS   A CB  1 
ATOM   2698 C  CG  . LYS   A 1 366 ? 14.625  60.747 39.899  1.00 62.07 ? 355 LYS   A CG  1 
ATOM   2699 C  CD  . LYS   A 1 366 ? 14.665  62.260 39.906  1.00 67.75 ? 355 LYS   A CD  1 
ATOM   2700 C  CE  . LYS   A 1 366 ? 16.074  62.794 40.006  1.00 72.61 ? 355 LYS   A CE  1 
ATOM   2701 N  NZ  . LYS   A 1 366 ? 16.083  64.266 40.229  1.00 76.01 ? 355 LYS   A NZ  1 
ATOM   2702 N  N   . ARG   A 1 367 ? 10.907  58.592 41.177  1.00 54.51 ? 356 ARG   A N   1 
ATOM   2703 C  CA  . ARG   A 1 367 ? 9.520   58.191 41.342  1.00 54.54 ? 356 ARG   A CA  1 
ATOM   2704 C  C   . ARG   A 1 367 ? 8.589   58.928 40.381  1.00 56.08 ? 356 ARG   A C   1 
ATOM   2705 O  O   . ARG   A 1 367 ? 8.811   60.099 40.065  1.00 56.35 ? 356 ARG   A O   1 
ATOM   2706 C  CB  . ARG   A 1 367 ? 9.080   58.360 42.806  1.00 53.60 ? 356 ARG   A CB  1 
ATOM   2707 C  CG  . ARG   A 1 367 ? 8.549   57.072 43.407  1.00 52.03 ? 356 ARG   A CG  1 
ATOM   2708 C  CD  . ARG   A 1 367 ? 7.911   57.290 44.763  1.00 50.21 ? 356 ARG   A CD  1 
ATOM   2709 N  NE  . ARG   A 1 367 ? 8.728   56.763 45.858  1.00 47.06 ? 356 ARG   A NE  1 
ATOM   2710 C  CZ  . ARG   A 1 367 ? 9.561   57.495 46.588  1.00 45.42 ? 356 ARG   A CZ  1 
ATOM   2711 N  NH1 . ARG   A 1 367 ? 9.694   58.797 46.353  1.00 45.15 ? 356 ARG   A NH1 1 
ATOM   2712 N  NH2 . ARG   A 1 367 ? 10.262  56.936 47.563  1.00 42.39 ? 356 ARG   A NH2 1 
ATOM   2713 N  N   . GLU   A 1 368 ? 7.573   58.229 39.884  1.00 57.11 ? 357 GLU   A N   1 
ATOM   2714 C  CA  . GLU   A 1 368 ? 6.624   58.815 38.953  1.00 58.84 ? 357 GLU   A CA  1 
ATOM   2715 C  C   . GLU   A 1 368 ? 5.452   59.472 39.662  1.00 60.51 ? 357 GLU   A C   1 
ATOM   2716 O  O   . GLU   A 1 368 ? 4.990   59.001 40.696  1.00 60.71 ? 357 GLU   A O   1 
ATOM   2717 C  CB  . GLU   A 1 368 ? 6.124   57.771 37.951  1.00 61.51 ? 357 GLU   A CB  1 
ATOM   2718 C  CG  . GLU   A 1 368 ? 6.680   57.979 36.557  1.00 67.08 ? 357 GLU   A CG  1 
ATOM   2719 C  CD  . GLU   A 1 368 ? 6.032   57.111 35.497  1.00 74.37 ? 357 GLU   A CD  1 
ATOM   2720 O  OE1 . GLU   A 1 368 ? 5.603   55.980 35.830  1.00 74.79 ? 357 GLU   A OE1 1 
ATOM   2721 O  OE2 . GLU   A 1 368 ? 5.952   57.565 34.331  1.00 77.20 ? 357 GLU   A OE2 1 
ATOM   2722 N  N   . PHE   A 1 369 ? 4.960   60.558 39.086  1.00 61.73 ? 358 PHE   A N   1 
ATOM   2723 C  CA  . PHE   A 1 369 ? 3.843   61.294 39.639  1.00 63.22 ? 358 PHE   A CA  1 
ATOM   2724 C  C   . PHE   A 1 369 ? 2.513   60.712 39.212  1.00 66.12 ? 358 PHE   A C   1 
ATOM   2725 O  O   . PHE   A 1 369 ? 2.225   60.632 38.017  1.00 66.98 ? 358 PHE   A O   1 
ATOM   2726 C  CB  . PHE   A 1 369 ? 3.934   62.761 39.244  1.00 62.22 ? 358 PHE   A CB  1 
ATOM   2727 C  CG  . PHE   A 1 369 ? 5.189   63.402 39.763  1.00 62.08 ? 358 PHE   A CG  1 
ATOM   2728 C  CD1 . PHE   A 1 369 ? 5.324   63.707 41.103  1.00 62.37 ? 358 PHE   A CD1 1 
ATOM   2729 C  CD2 . PHE   A 1 369 ? 6.254   63.654 38.922  1.00 62.57 ? 358 PHE   A CD2 1 
ATOM   2730 C  CE1 . PHE   A 1 369 ? 6.476   64.304 41.583  1.00 62.79 ? 358 PHE   A CE1 1 
ATOM   2731 C  CE2 . PHE   A 1 369 ? 7.409   64.247 39.405  1.00 63.18 ? 358 PHE   A CE2 1 
ATOM   2732 C  CZ  . PHE   A 1 369 ? 7.516   64.561 40.735  1.00 62.77 ? 358 PHE   A CZ  1 
ATOM   2733 N  N   . LEU   A 1 370 ? 1.704   60.308 40.199  1.00 67.42 ? 359 LEU   A N   1 
ATOM   2734 C  CA  . LEU   A 1 370 ? 0.365   59.763 40.031  1.00 68.87 ? 359 LEU   A CA  1 
ATOM   2735 C  C   . LEU   A 1 370 ? -0.576  60.888 39.600  1.00 70.88 ? 359 LEU   A C   1 
ATOM   2736 O  O   . LEU   A 1 370 ? -0.532  61.976 40.174  1.00 71.14 ? 359 LEU   A O   1 
ATOM   2737 C  CB  . LEU   A 1 370 ? -0.137  59.205 41.374  1.00 68.77 ? 359 LEU   A CB  1 
ATOM   2738 C  CG  . LEU   A 1 370 ? 0.782   58.244 42.103  1.00 70.23 ? 359 LEU   A CG  1 
ATOM   2739 C  CD1 . LEU   A 1 370 ? 0.223   57.886 43.457  1.00 70.65 ? 359 LEU   A CD1 1 
ATOM   2740 C  CD2 . LEU   A 1 370 ? 1.005   56.994 41.292  1.00 71.08 ? 359 LEU   A CD2 1 
ATOM   2741 N  N   . THR   A 1 371 ? -1.434  60.633 38.603  1.00 72.15 ? 360 THR   A N   1 
ATOM   2742 C  CA  . THR   A 1 371 ? -2.421  61.626 38.183  1.00 73.63 ? 360 THR   A CA  1 
ATOM   2743 C  C   . THR   A 1 371 ? -3.716  61.254 38.904  1.00 74.27 ? 360 THR   A C   1 
ATOM   2744 O  O   . THR   A 1 371 ? -4.613  60.639 38.322  1.00 74.28 ? 360 THR   A O   1 
ATOM   2745 C  CB  . THR   A 1 371 ? -2.581  61.661 36.662  1.00 75.77 ? 360 THR   A CB  1 
ATOM   2746 O  OG1 . THR   A 1 371 ? -1.304  61.777 36.021  1.00 77.19 ? 360 THR   A OG1 1 
ATOM   2747 C  CG2 . THR   A 1 371 ? -3.470  62.786 36.210  1.00 76.08 ? 360 THR   A CG2 1 
ATOM   2748 N  N   . GLU   A 1 372 ? -3.763  61.566 40.206  1.00 74.54 ? 361 GLU   A N   1 
ATOM   2749 C  CA  . GLU   A 1 372 ? -4.876  61.225 41.082  1.00 75.17 ? 361 GLU   A CA  1 
ATOM   2750 C  C   . GLU   A 1 372 ? -6.133  62.063 40.843  1.00 75.28 ? 361 GLU   A C   1 
ATOM   2751 O  O   . GLU   A 1 372 ? -6.117  63.279 41.022  1.00 75.33 ? 361 GLU   A O   1 
ATOM   2752 C  CB  . GLU   A 1 372 ? -4.433  61.304 42.550  1.00 77.53 ? 361 GLU   A CB  1 
ATOM   2753 C  CG  . GLU   A 1 372 ? -5.518  60.926 43.546  1.00 82.12 ? 361 GLU   A CG  1 
ATOM   2754 C  CD  . GLU   A 1 372 ? -5.500  59.486 44.018  1.00 87.24 ? 361 GLU   A CD  1 
ATOM   2755 O  OE1 . GLU   A 1 372 ? -4.532  58.762 43.689  1.00 88.25 ? 361 GLU   A OE1 1 
ATOM   2756 O  OE2 . GLU   A 1 372 ? -6.457  59.083 44.719  1.00 88.66 ? 361 GLU   A OE2 1 
ATOM   2757 N  N   . GLU   A 1 373 ? -7.235  61.398 40.480  1.00 75.11 ? 362 GLU   A N   1 
ATOM   2758 C  CA  . GLU   A 1 373 ? -8.502  62.077 40.240  1.00 75.07 ? 362 GLU   A CA  1 
ATOM   2759 C  C   . GLU   A 1 373 ? -9.674  61.346 40.895  1.00 75.51 ? 362 GLU   A C   1 
ATOM   2760 O  O   . GLU   A 1 373 ? -9.700  60.115 40.925  1.00 75.71 ? 362 GLU   A O   1 
ATOM   2761 C  CB  . GLU   A 1 373 ? -8.748  62.246 38.736  1.00 75.81 ? 362 GLU   A CB  1 
ATOM   2762 C  CG  . GLU   A 1 373 ? -9.924  63.153 38.445  1.00 77.48 ? 362 GLU   A CG  1 
ATOM   2763 C  CD  . GLU   A 1 373 ? -9.746  64.567 38.957  1.00 80.30 ? 362 GLU   A CD  1 
ATOM   2764 O  OE1 . GLU   A 1 373 ? -8.659  65.148 38.734  1.00 80.69 ? 362 GLU   A OE1 1 
ATOM   2765 O  OE2 . GLU   A 1 373 ? -10.699 65.102 39.568  1.00 81.26 ? 362 GLU   A OE2 1 
ATOM   2766 N  N   . ALA   B 2 30  ? 5.242   52.716 75.149  1.00 45.16 ? 0   ALA   B N   1 
ATOM   2767 C  CA  . ALA   B 2 30  ? 5.528   53.638 74.045  1.00 45.50 ? 0   ALA   B CA  1 
ATOM   2768 C  C   . ALA   B 2 30  ? 6.255   54.872 74.555  1.00 45.12 ? 0   ALA   B C   1 
ATOM   2769 O  O   . ALA   B 2 30  ? 5.694   55.703 75.273  1.00 46.03 ? 0   ALA   B O   1 
ATOM   2770 C  CB  . ALA   B 2 30  ? 4.257   54.032 73.319  1.00 45.60 ? 0   ALA   B CB  1 
ATOM   2771 N  N   . MET   B 2 31  ? 7.524   54.963 74.192  1.00 43.58 ? 1   MET   B N   1 
ATOM   2772 C  CA  . MET   B 2 31  ? 8.471   56.006 74.558  1.00 42.41 ? 1   MET   B CA  1 
ATOM   2773 C  C   . MET   B 2 31  ? 8.928   55.944 76.011  1.00 42.29 ? 1   MET   B C   1 
ATOM   2774 O  O   . MET   B 2 31  ? 9.644   56.841 76.455  1.00 42.43 ? 1   MET   B O   1 
ATOM   2775 C  CB  . MET   B 2 31  ? 7.969   57.403 74.183  1.00 41.31 ? 1   MET   B CB  1 
ATOM   2776 C  CG  . MET   B 2 31  ? 7.596   57.550 72.715  1.00 40.46 ? 1   MET   B CG  1 
ATOM   2777 S  SD  . MET   B 2 31  ? 8.800   56.871 71.544  1.00 38.88 ? 1   MET   B SD  1 
ATOM   2778 C  CE  . MET   B 2 31  ? 10.278  57.771 71.973  1.00 34.75 ? 1   MET   B CE  1 
ATOM   2779 N  N   . ALA   B 2 32  ? 8.631   54.841 76.726  1.00 41.77 ? 2   ALA   B N   1 
ATOM   2780 C  CA  . ALA   B 2 32  ? 9.110   54.653 78.100  1.00 41.89 ? 2   ALA   B CA  1 
ATOM   2781 C  C   . ALA   B 2 32  ? 10.644  54.605 78.065  1.00 41.48 ? 2   ALA   B C   1 
ATOM   2782 O  O   . ALA   B 2 32  ? 11.222  54.062 77.107  1.00 41.94 ? 2   ALA   B O   1 
ATOM   2783 C  CB  . ALA   B 2 32  ? 8.557   53.354 78.673  1.00 42.06 ? 2   ALA   B CB  1 
ATOM   2784 N  N   . GLY   B 2 33  ? 11.278  55.303 78.998  1.00 40.13 ? 3   GLY   B N   1 
ATOM   2785 C  CA  . GLY   B 2 33  ? 12.731  55.368 79.016  1.00 39.75 ? 3   GLY   B CA  1 
ATOM   2786 C  C   . GLY   B 2 33  ? 13.297  56.559 78.271  1.00 39.68 ? 3   GLY   B C   1 
ATOM   2787 O  O   . GLY   B 2 33  ? 14.436  56.958 78.532  1.00 40.72 ? 3   GLY   B O   1 
ATOM   2788 N  N   . ASN   B 2 34  ? 12.506  57.175 77.359  1.00 37.97 ? 4   ASN   B N   1 
ATOM   2789 C  CA  . ASN   B 2 34  ? 12.968  58.306 76.553  1.00 36.65 ? 4   ASN   B CA  1 
ATOM   2790 C  C   . ASN   B 2 34  ? 12.759  59.712 77.180  1.00 35.86 ? 4   ASN   B C   1 
ATOM   2791 O  O   . ASN   B 2 34  ? 12.927  60.709 76.481  1.00 36.08 ? 4   ASN   B O   1 
ATOM   2792 C  CB  . ASN   B 2 34  ? 12.302  58.241 75.174  1.00 36.69 ? 4   ASN   B CB  1 
ATOM   2793 C  CG  . ASN   B 2 34  ? 12.975  59.073 74.131  1.00 39.00 ? 4   ASN   B CG  1 
ATOM   2794 O  OD1 . ASN   B 2 34  ? 14.157  58.914 73.863  1.00 41.12 ? 4   ASN   B OD1 1 
ATOM   2795 N  ND2 . ASN   B 2 34  ? 12.252  60.006 73.539  1.00 39.37 ? 4   ASN   B ND2 1 
ATOM   2796 N  N   . PHE   B 2 35  ? 12.435  59.813 78.478  1.00 34.89 ? 5   PHE   B N   1 
ATOM   2797 C  CA  . PHE   B 2 35  ? 12.181  61.116 79.108  1.00 34.33 ? 5   PHE   B CA  1 
ATOM   2798 C  C   . PHE   B 2 35  ? 13.203  62.205 78.809  1.00 35.29 ? 5   PHE   B C   1 
ATOM   2799 O  O   . PHE   B 2 35  ? 12.799  63.317 78.470  1.00 35.19 ? 5   PHE   B O   1 
ATOM   2800 C  CB  . PHE   B 2 35  ? 11.982  61.032 80.628  1.00 32.79 ? 5   PHE   B CB  1 
ATOM   2801 C  CG  . PHE   B 2 35  ? 11.539  62.371 81.182  1.00 32.33 ? 5   PHE   B CG  1 
ATOM   2802 C  CD1 . PHE   B 2 35  ? 10.276  62.873 80.900  1.00 32.48 ? 5   PHE   B CD1 1 
ATOM   2803 C  CD2 . PHE   B 2 35  ? 12.416  63.169 81.899  1.00 32.41 ? 5   PHE   B CD2 1 
ATOM   2804 C  CE1 . PHE   B 2 35  ? 9.879   64.119 81.381  1.00 32.72 ? 5   PHE   B CE1 1 
ATOM   2805 C  CE2 . PHE   B 2 35  ? 12.009  64.405 82.393  1.00 32.88 ? 5   PHE   B CE2 1 
ATOM   2806 C  CZ  . PHE   B 2 35  ? 10.743  64.868 82.135  1.00 32.57 ? 5   PHE   B CZ  1 
ATOM   2807 N  N   . TRP   B 2 36  ? 14.506  61.910 78.950  1.00 35.47 ? 6   TRP   B N   1 
ATOM   2808 C  CA  . TRP   B 2 36  ? 15.524  62.947 78.765  1.00 35.47 ? 6   TRP   B CA  1 
ATOM   2809 C  C   . TRP   B 2 36  ? 15.692  63.423 77.314  1.00 35.33 ? 6   TRP   B C   1 
ATOM   2810 O  O   . TRP   B 2 36  ? 16.344  64.435 77.076  1.00 35.37 ? 6   TRP   B O   1 
ATOM   2811 C  CB  . TRP   B 2 36  ? 16.858  62.507 79.380  1.00 35.25 ? 6   TRP   B CB  1 
ATOM   2812 C  CG  . TRP   B 2 36  ? 16.742  62.158 80.839  1.00 35.23 ? 6   TRP   B CG  1 
ATOM   2813 C  CD1 . TRP   B 2 36  ? 16.880  60.920 81.392  1.00 36.21 ? 6   TRP   B CD1 1 
ATOM   2814 C  CD2 . TRP   B 2 36  ? 16.379  63.041 81.915  1.00 34.98 ? 6   TRP   B CD2 1 
ATOM   2815 N  NE1 . TRP   B 2 36  ? 16.657  60.981 82.750  1.00 36.70 ? 6   TRP   B NE1 1 
ATOM   2816 C  CE2 . TRP   B 2 36  ? 16.371  62.277 83.100  1.00 36.16 ? 6   TRP   B CE2 1 
ATOM   2817 C  CE3 . TRP   B 2 36  ? 16.049  64.400 81.992  1.00 35.23 ? 6   TRP   B CE3 1 
ATOM   2818 C  CZ2 . TRP   B 2 36  ? 16.078  62.835 84.348  1.00 36.55 ? 6   TRP   B CZ2 1 
ATOM   2819 C  CZ3 . TRP   B 2 36  ? 15.758  64.951 83.227  1.00 36.04 ? 6   TRP   B CZ3 1 
ATOM   2820 C  CH2 . TRP   B 2 36  ? 15.786  64.177 84.388  1.00 36.40 ? 6   TRP   B CH2 1 
ATOM   2821 N  N   . GLN   B 2 37  ? 15.051  62.753 76.360  1.00 34.94 ? 7   GLN   B N   1 
ATOM   2822 C  CA  . GLN   B 2 37  ? 15.091  63.163 74.954  1.00 35.23 ? 7   GLN   B CA  1 
ATOM   2823 C  C   . GLN   B 2 37  ? 13.680  63.478 74.422  1.00 34.28 ? 7   GLN   B C   1 
ATOM   2824 O  O   . GLN   B 2 37  ? 13.509  63.622 73.213  1.00 34.82 ? 7   GLN   B O   1 
ATOM   2825 C  CB  . GLN   B 2 37  ? 15.719  62.047 74.100  1.00 38.35 ? 7   GLN   B CB  1 
ATOM   2826 C  CG  . GLN   B 2 37  ? 17.162  61.686 74.490  1.00 45.91 ? 7   GLN   B CG  1 
ATOM   2827 C  CD  . GLN   B 2 37  ? 17.273  60.614 75.565  1.00 55.23 ? 7   GLN   B CD  1 
ATOM   2828 O  OE1 . GLN   B 2 37  ? 18.155  60.666 76.434  1.00 59.31 ? 7   GLN   B OE1 1 
ATOM   2829 N  NE2 . GLN   B 2 37  ? 16.387  59.619 75.548  1.00 56.10 ? 7   GLN   B NE2 1 
ATOM   2830 N  N   . SER   B 2 38  ? 12.674  63.582 75.312  1.00 32.49 ? 8   SER   B N   1 
ATOM   2831 C  CA  . SER   B 2 38  ? 11.282  63.785 74.951  1.00 31.25 ? 8   SER   B CA  1 
ATOM   2832 C  C   . SER   B 2 38  ? 10.893  65.251 74.814  1.00 30.34 ? 8   SER   B C   1 
ATOM   2833 O  O   . SER   B 2 38  ? 11.526  66.109 75.423  1.00 30.80 ? 8   SER   B O   1 
ATOM   2834 C  CB  . SER   B 2 38  ? 10.401  63.140 76.019  1.00 31.33 ? 8   SER   B CB  1 
ATOM   2835 O  OG  . SER   B 2 38  ? 10.529  63.832 77.247  1.00 32.74 ? 8   SER   B OG  1 
ATOM   2836 N  N   . SER   B 2 39  ? 9.793   65.530 74.116  1.00 29.05 ? 9   SER   B N   1 
ATOM   2837 C  CA  . SER   B 2 39  ? 9.264   66.894 74.028  1.00 29.02 ? 9   SER   B CA  1 
ATOM   2838 C  C   . SER   B 2 39  ? 8.706   67.355 75.391  1.00 29.15 ? 9   SER   B C   1 
ATOM   2839 O  O   . SER   B 2 39  ? 8.645   68.546 75.651  1.00 29.78 ? 9   SER   B O   1 
ATOM   2840 C  CB  . SER   B 2 39  ? 8.152   66.963 72.991  1.00 29.61 ? 9   SER   B CB  1 
ATOM   2841 O  OG  . SER   B 2 39  ? 6.996   66.271 73.446  1.00 31.18 ? 9   SER   B OG  1 
ATOM   2842 N  N   . HIS   B 2 40  ? 8.274   66.420 76.256  1.00 28.52 ? 10  HIS   B N   1 
ATOM   2843 C  CA  . HIS   B 2 40  ? 7.771   66.717 77.591  1.00 28.99 ? 10  HIS   B CA  1 
ATOM   2844 C  C   . HIS   B 2 40  ? 8.904   67.404 78.367  1.00 30.11 ? 10  HIS   B C   1 
ATOM   2845 O  O   . HIS   B 2 40  ? 8.710   68.494 78.872  1.00 30.12 ? 10  HIS   B O   1 
ATOM   2846 C  CB  . HIS   B 2 40  ? 7.312   65.403 78.290  1.00 28.88 ? 10  HIS   B CB  1 
ATOM   2847 C  CG  . HIS   B 2 40  ? 6.815   65.543 79.696  1.00 30.62 ? 10  HIS   B CG  1 
ATOM   2848 N  ND1 . HIS   B 2 40  ? 5.817   64.725 80.180  1.00 31.95 ? 10  HIS   B ND1 1 
ATOM   2849 C  CD2 . HIS   B 2 40  ? 7.221   66.369 80.696  1.00 32.26 ? 10  HIS   B CD2 1 
ATOM   2850 C  CE1 . HIS   B 2 40  ? 5.621   65.093 81.437  1.00 32.56 ? 10  HIS   B CE1 1 
ATOM   2851 N  NE2 . HIS   B 2 40  ? 6.441   66.075 81.795  1.00 33.22 ? 10  HIS   B NE2 1 
ATOM   2852 N  N   . TYR   B 2 41  ? 10.094  66.824 78.341  1.00 30.96 ? 11  TYR   B N   1 
ATOM   2853 C  CA  . TYR   B 2 41  ? 11.241  67.388 79.022  1.00 33.12 ? 11  TYR   B CA  1 
ATOM   2854 C  C   . TYR   B 2 41  ? 11.844  68.618 78.318  1.00 33.95 ? 11  TYR   B C   1 
ATOM   2855 O  O   . TYR   B 2 41  ? 12.088  69.637 78.956  1.00 34.58 ? 11  TYR   B O   1 
ATOM   2856 C  CB  . TYR   B 2 41  ? 12.295  66.289 79.247  1.00 34.03 ? 11  TYR   B CB  1 
ATOM   2857 C  CG  . TYR   B 2 41  ? 13.600  66.803 79.795  1.00 35.96 ? 11  TYR   B CG  1 
ATOM   2858 C  CD1 . TYR   B 2 41  ? 13.674  67.363 81.063  1.00 37.45 ? 11  TYR   B CD1 1 
ATOM   2859 C  CD2 . TYR   B 2 41  ? 14.758  66.757 79.035  1.00 37.44 ? 11  TYR   B CD2 1 
ATOM   2860 C  CE1 . TYR   B 2 41  ? 14.870  67.866 81.560  1.00 38.68 ? 11  TYR   B CE1 1 
ATOM   2861 C  CE2 . TYR   B 2 41  ? 15.963  67.240 79.527  1.00 38.66 ? 11  TYR   B CE2 1 
ATOM   2862 C  CZ  . TYR   B 2 41  ? 16.015  67.795 80.789  1.00 39.96 ? 11  TYR   B CZ  1 
ATOM   2863 O  OH  . TYR   B 2 41  ? 17.212  68.257 81.265  1.00 42.61 ? 11  TYR   B OH  1 
ATOM   2864 N  N   . LEU   B 2 42  ? 12.066  68.527 77.018  1.00 33.66 ? 12  LEU   B N   1 
ATOM   2865 C  CA  . LEU   B 2 42  ? 12.695  69.585 76.260  1.00 33.76 ? 12  LEU   B CA  1 
ATOM   2866 C  C   . LEU   B 2 42  ? 11.828  70.816 76.012  1.00 34.37 ? 12  LEU   B C   1 
ATOM   2867 O  O   . LEU   B 2 42  ? 12.387  71.899 75.844  1.00 34.78 ? 12  LEU   B O   1 
ATOM   2868 C  CB  . LEU   B 2 42  ? 13.238  69.027 74.944  1.00 33.87 ? 12  LEU   B CB  1 
ATOM   2869 C  CG  . LEU   B 2 42  ? 14.272  67.911 75.132  1.00 35.47 ? 12  LEU   B CG  1 
ATOM   2870 C  CD1 . LEU   B 2 42  ? 14.662  67.282 73.801  1.00 35.57 ? 12  LEU   B CD1 1 
ATOM   2871 C  CD2 . LEU   B 2 42  ? 15.489  68.406 75.928  1.00 36.05 ? 12  LEU   B CD2 1 
ATOM   2872 N  N   . GLN   B 2 43  ? 10.493  70.694 76.040  1.00 34.13 ? 13  GLN   B N   1 
ATOM   2873 C  CA  . GLN   B 2 43  ? 9.630   71.853 75.792  1.00 34.25 ? 13  GLN   B CA  1 
ATOM   2874 C  C   . GLN   B 2 43  ? 8.606   72.118 76.879  1.00 34.14 ? 13  GLN   B C   1 
ATOM   2875 O  O   . GLN   B 2 43  ? 8.159   73.266 77.023  1.00 34.94 ? 13  GLN   B O   1 
ATOM   2876 C  CB  . GLN   B 2 43  ? 8.857   71.670 74.488  1.00 35.82 ? 13  GLN   B CB  1 
ATOM   2877 C  CG  . GLN   B 2 43  ? 9.713   71.800 73.278  1.00 41.50 ? 13  GLN   B CG  1 
ATOM   2878 C  CD  . GLN   B 2 43  ? 8.913   71.554 72.040  1.00 46.76 ? 13  GLN   B CD  1 
ATOM   2879 O  OE1 . GLN   B 2 43  ? 9.230   70.651 71.265  1.00 47.85 ? 13  GLN   B OE1 1 
ATOM   2880 N  NE2 . GLN   B 2 43  ? 7.861   72.347 71.825  1.00 46.76 ? 13  GLN   B NE2 1 
ATOM   2881 N  N   . TRP   B 2 44  ? 8.155   71.067 77.565  1.00 32.69 ? 14  TRP   B N   1 
ATOM   2882 C  CA  . TRP   B 2 44  ? 7.064   71.234 78.513  1.00 32.16 ? 14  TRP   B CA  1 
ATOM   2883 C  C   . TRP   B 2 44  ? 7.430   71.074 79.979  1.00 32.13 ? 14  TRP   B C   1 
ATOM   2884 O  O   . TRP   B 2 44  ? 6.567   70.797 80.798  1.00 32.54 ? 14  TRP   B O   1 
ATOM   2885 C  CB  . TRP   B 2 44  ? 5.921   70.333 78.123  1.00 31.30 ? 14  TRP   B CB  1 
ATOM   2886 C  CG  . TRP   B 2 44  ? 5.265   70.796 76.857  1.00 30.87 ? 14  TRP   B CG  1 
ATOM   2887 C  CD1 . TRP   B 2 44  ? 5.450   70.297 75.603  1.00 31.22 ? 14  TRP   B CD1 1 
ATOM   2888 C  CD2 . TRP   B 2 44  ? 4.381   71.919 76.716  1.00 30.66 ? 14  TRP   B CD2 1 
ATOM   2889 N  NE1 . TRP   B 2 44  ? 4.674   70.990 74.700  1.00 31.35 ? 14  TRP   B NE1 1 
ATOM   2890 C  CE2 . TRP   B 2 44  ? 4.010   71.992 75.359  1.00 31.39 ? 14  TRP   B CE2 1 
ATOM   2891 C  CE3 . TRP   B 2 44  ? 3.857   72.860 77.611  1.00 31.14 ? 14  TRP   B CE3 1 
ATOM   2892 C  CZ2 . TRP   B 2 44  ? 3.161   72.989 74.872  1.00 32.28 ? 14  TRP   B CZ2 1 
ATOM   2893 C  CZ3 . TRP   B 2 44  ? 3.016   73.849 77.126  1.00 32.03 ? 14  TRP   B CZ3 1 
ATOM   2894 C  CH2 . TRP   B 2 44  ? 2.660   73.894 75.780  1.00 32.25 ? 14  TRP   B CH2 1 
ATOM   2895 N  N   . ILE   B 2 45  ? 8.692   71.305 80.312  1.00 32.14 ? 15  ILE   B N   1 
ATOM   2896 C  CA  . ILE   B 2 45  ? 9.165   71.426 81.683  1.00 32.88 ? 15  ILE   B CA  1 
ATOM   2897 C  C   . ILE   B 2 45  ? 9.521   72.914 81.749  1.00 33.60 ? 15  ILE   B C   1 
ATOM   2898 O  O   . ILE   B 2 45  ? 10.543  73.347 81.217  1.00 33.64 ? 15  ILE   B O   1 
ATOM   2899 C  CB  . ILE   B 2 45  ? 10.349  70.513 82.049  1.00 32.79 ? 15  ILE   B CB  1 
ATOM   2900 C  CG1 . ILE   B 2 45  ? 9.902   69.035 82.077  1.00 33.29 ? 15  ILE   B CG1 1 
ATOM   2901 C  CG2 . ILE   B 2 45  ? 10.935  70.946 83.404  1.00 32.75 ? 15  ILE   B CG2 1 
ATOM   2902 C  CD1 . ILE   B 2 45  ? 8.915   68.657 83.195  1.00 34.29 ? 15  ILE   B CD1 1 
ATOM   2903 N  N   . LEU   B 2 46  ? 8.596   73.698 82.279  1.00 33.98 ? 16  LEU   B N   1 
ATOM   2904 C  CA  . LEU   B 2 46  ? 8.643   75.150 82.303  1.00 34.94 ? 16  LEU   B CA  1 
ATOM   2905 C  C   . LEU   B 2 46  ? 9.394   75.774 83.466  1.00 35.61 ? 16  LEU   B C   1 
ATOM   2906 O  O   . LEU   B 2 46  ? 9.630   75.139 84.485  1.00 34.54 ? 16  LEU   B O   1 
ATOM   2907 C  CB  . LEU   B 2 46  ? 7.203   75.690 82.260  1.00 35.46 ? 16  LEU   B CB  1 
ATOM   2908 C  CG  . LEU   B 2 46  ? 6.298   75.120 81.151  1.00 37.04 ? 16  LEU   B CG  1 
ATOM   2909 C  CD1 . LEU   B 2 46  ? 4.865   75.635 81.291  1.00 37.11 ? 16  LEU   B CD1 1 
ATOM   2910 C  CD2 . LEU   B 2 46  ? 6.900   75.383 79.745  1.00 37.26 ? 16  LEU   B CD2 1 
ATOM   2911 N  N   . ASP   B 2 47  ? 9.784   77.048 83.278  1.00 37.44 ? 17  ASP   B N   1 
ATOM   2912 C  CA  . ASP   B 2 47  ? 10.449  77.907 84.256  1.00 39.15 ? 17  ASP   B CA  1 
ATOM   2913 C  C   . ASP   B 2 47  ? 9.317   78.545 85.068  1.00 39.61 ? 17  ASP   B C   1 
ATOM   2914 O  O   . ASP   B 2 47  ? 8.420   79.142 84.479  1.00 39.65 ? 17  ASP   B O   1 
ATOM   2915 C  CB  . ASP   B 2 47  ? 11.214  79.001 83.501  1.00 42.62 ? 17  ASP   B CB  1 
ATOM   2916 C  CG  . ASP   B 2 47  ? 12.161  79.834 84.341  1.00 50.78 ? 17  ASP   B CG  1 
ATOM   2917 O  OD1 . ASP   B 2 47  ? 11.787  80.201 85.483  1.00 51.31 ? 17  ASP   B OD1 1 
ATOM   2918 O  OD2 . ASP   B 2 47  ? 13.270  80.151 83.843  1.00 55.53 ? 17  ASP   B OD2 1 
ATOM   2919 N  N   . LYS   B 2 48  ? 9.339   78.418 86.395  1.00 40.12 ? 18  LYS   B N   1 
ATOM   2920 C  CA  . LYS   B 2 48  ? 8.263   78.955 87.240  1.00 41.63 ? 18  LYS   B CA  1 
ATOM   2921 C  C   . LYS   B 2 48  ? 7.959   80.443 86.986  1.00 43.47 ? 18  LYS   B C   1 
ATOM   2922 O  O   . LYS   B 2 48  ? 6.789   80.819 86.908  1.00 43.68 ? 18  LYS   B O   1 
ATOM   2923 C  CB  . LYS   B 2 48  ? 8.555   78.697 88.722  1.00 42.94 ? 18  LYS   B CB  1 
ATOM   2924 C  CG  . LYS   B 2 48  ? 7.327   78.768 89.586  1.00 47.48 ? 18  LYS   B CG  1 
ATOM   2925 C  CD  . LYS   B 2 48  ? 7.671   78.651 91.061  1.00 53.28 ? 18  LYS   B CD  1 
ATOM   2926 C  CE  . LYS   B 2 48  ? 6.418   78.728 91.903  1.00 58.38 ? 18  LYS   B CE  1 
ATOM   2927 N  NZ  . LYS   B 2 48  ? 6.721   78.896 93.352  1.00 61.68 ? 18  LYS   B NZ  1 
ATOM   2928 N  N   . GLN   B 2 49  ? 9.011   81.271 86.781  1.00 44.01 ? 19  GLN   B N   1 
ATOM   2929 C  CA  . GLN   B 2 49  ? 8.848   82.688 86.497  1.00 44.57 ? 19  GLN   B CA  1 
ATOM   2930 C  C   . GLN   B 2 49  ? 8.178   82.971 85.158  1.00 44.59 ? 19  GLN   B C   1 
ATOM   2931 O  O   . GLN   B 2 49  ? 7.360   83.885 85.081  1.00 45.37 ? 19  GLN   B O   1 
ATOM   2932 C  CB  . GLN   B 2 49  ? 10.178  83.441 86.632  1.00 47.05 ? 19  GLN   B CB  1 
ATOM   2933 C  CG  . GLN   B 2 49  ? 10.660  83.521 88.081  1.00 52.68 ? 19  GLN   B CG  1 
ATOM   2934 C  CD  . GLN   B 2 49  ? 9.598   84.072 89.011  1.00 60.67 ? 19  GLN   B CD  1 
ATOM   2935 O  OE1 . GLN   B 2 49  ? 9.108   83.381 89.916  1.00 63.17 ? 19  GLN   B OE1 1 
ATOM   2936 N  NE2 . GLN   B 2 49  ? 9.182   85.310 88.770  1.00 62.36 ? 19  GLN   B NE2 1 
ATOM   2937 N  N   . ASP   B 2 50  ? 8.472   82.184 84.127  1.00 43.72 ? 20  ASP   B N   1 
ATOM   2938 C  CA  . ASP   B 2 50  ? 7.820   82.338 82.830  1.00 43.46 ? 20  ASP   B CA  1 
ATOM   2939 C  C   . ASP   B 2 50  ? 6.324   82.045 82.955  1.00 43.19 ? 20  ASP   B C   1 
ATOM   2940 O  O   . ASP   B 2 50  ? 5.496   82.755 82.380  1.00 43.17 ? 20  ASP   B O   1 
ATOM   2941 C  CB  . ASP   B 2 50  ? 8.438   81.375 81.809  1.00 45.50 ? 20  ASP   B CB  1 
ATOM   2942 C  CG  . ASP   B 2 50  ? 9.838   81.735 81.344  1.00 52.14 ? 20  ASP   B CG  1 
ATOM   2943 O  OD1 . ASP   B 2 50  ? 10.361  82.796 81.783  1.00 53.35 ? 20  ASP   B OD1 1 
ATOM   2944 O  OD2 . ASP   B 2 50  ? 10.409  80.967 80.522  1.00 54.66 ? 20  ASP   B OD2 1 
ATOM   2945 N  N   . LEU   B 2 51  ? 5.987   81.009 83.734  1.00 42.78 ? 21  LEU   B N   1 
ATOM   2946 C  CA  . LEU   B 2 51  ? 4.628   80.564 83.978  1.00 42.86 ? 21  LEU   B CA  1 
ATOM   2947 C  C   . LEU   B 2 51  ? 3.852   81.657 84.733  1.00 43.02 ? 21  LEU   B C   1 
ATOM   2948 O  O   . LEU   B 2 51  ? 2.763   82.047 84.301  1.00 42.39 ? 21  LEU   B O   1 
ATOM   2949 C  CB  . LEU   B 2 51  ? 4.688   79.248 84.776  1.00 42.68 ? 21  LEU   B CB  1 
ATOM   2950 C  CG  . LEU   B 2 51  ? 3.405   78.480 84.899  1.00 43.76 ? 21  LEU   B CG  1 
ATOM   2951 C  CD1 . LEU   B 2 51  ? 2.978   77.971 83.566  1.00 43.98 ? 21  LEU   B CD1 1 
ATOM   2952 C  CD2 . LEU   B 2 51  ? 3.558   77.321 85.880  1.00 44.32 ? 21  LEU   B CD2 1 
ATOM   2953 N  N   . LEU   B 2 52  ? 4.443   82.182 85.826  1.00 43.58 ? 22  LEU   B N   1 
ATOM   2954 C  CA  . LEU   B 2 52  ? 3.840   83.254 86.614  1.00 44.86 ? 22  LEU   B CA  1 
ATOM   2955 C  C   . LEU   B 2 52  ? 3.656   84.509 85.770  1.00 45.15 ? 22  LEU   B C   1 
ATOM   2956 O  O   . LEU   B 2 52  ? 2.664   85.215 85.943  1.00 45.33 ? 22  LEU   B O   1 
ATOM   2957 C  CB  . LEU   B 2 52  ? 4.693   83.596 87.852  1.00 45.96 ? 22  LEU   B CB  1 
ATOM   2958 C  CG  . LEU   B 2 52  ? 5.013   82.472 88.845  1.00 48.91 ? 22  LEU   B CG  1 
ATOM   2959 C  CD1 . LEU   B 2 52  ? 5.695   83.020 90.080  1.00 50.01 ? 22  LEU   B CD1 1 
ATOM   2960 C  CD2 . LEU   B 2 52  ? 3.773   81.661 89.237  1.00 49.93 ? 22  LEU   B CD2 1 
ATOM   2961 N  N   . LYS   B 2 53  ? 4.608   84.787 84.858  1.00 44.78 ? 23  LYS   B N   1 
ATOM   2962 C  CA  . LYS   B 2 53  ? 4.533   85.936 83.979  1.00 45.50 ? 23  LYS   B CA  1 
ATOM   2963 C  C   . LYS   B 2 53  ? 3.350   85.796 83.032  1.00 45.32 ? 23  LYS   B C   1 
ATOM   2964 O  O   . LYS   B 2 53  ? 2.583   86.740 82.882  1.00 46.15 ? 23  LYS   B O   1 
ATOM   2965 C  CB  . LYS   B 2 53  ? 5.841   86.111 83.193  1.00 48.87 ? 23  LYS   B CB  1 
ATOM   2966 C  CG  . LYS   B 2 53  ? 5.921   87.439 82.448  1.00 55.71 ? 23  LYS   B CG  1 
ATOM   2967 C  CD  . LYS   B 2 53  ? 6.667   87.298 81.135  1.00 61.90 ? 23  LYS   B CD  1 
ATOM   2968 C  CE  . LYS   B 2 53  ? 6.863   88.635 80.464  1.00 66.93 ? 23  LYS   B CE  1 
ATOM   2969 N  NZ  . LYS   B 2 53  ? 7.809   88.544 79.315  1.00 69.79 ? 23  LYS   B NZ  1 
ATOM   2970 N  N   . GLU   B 2 54  ? 3.187   84.629 82.394  1.00 44.40 ? 24  GLU   B N   1 
ATOM   2971 C  CA  . GLU   B 2 54  ? 2.058   84.407 81.493  1.00 43.89 ? 24  GLU   B CA  1 
ATOM   2972 C  C   . GLU   B 2 54  ? 0.717   84.429 82.221  1.00 43.13 ? 24  GLU   B C   1 
ATOM   2973 O  O   . GLU   B 2 54  ? -0.286  84.808 81.631  1.00 43.16 ? 24  GLU   B O   1 
ATOM   2974 C  CB  . GLU   B 2 54  ? 2.227   83.108 80.689  1.00 46.70 ? 24  GLU   B CB  1 
ATOM   2975 C  CG  . GLU   B 2 54  ? 3.086   83.247 79.442  1.00 53.40 ? 24  GLU   B CG  1 
ATOM   2976 C  CD  . GLU   B 2 54  ? 2.772   84.471 78.601  1.00 62.74 ? 24  GLU   B CD  1 
ATOM   2977 O  OE1 . GLU   B 2 54  ? 1.637   84.559 78.077  1.00 64.48 ? 24  GLU   B OE1 1 
ATOM   2978 O  OE2 . GLU   B 2 54  ? 3.643   85.368 78.518  1.00 65.95 ? 24  GLU   B OE2 1 
ATOM   2979 N  N   . ARG   B 2 55  ? 0.700   84.042 83.502  1.00 42.33 ? 25  ARG   B N   1 
ATOM   2980 C  CA  . ARG   B 2 55  ? -0.511  84.025 84.309  1.00 42.57 ? 25  ARG   B CA  1 
ATOM   2981 C  C   . ARG   B 2 55  ? -1.024  85.422 84.659  1.00 42.49 ? 25  ARG   B C   1 
ATOM   2982 O  O   . ARG   B 2 55  ? -2.211  85.568 84.936  1.00 42.63 ? 25  ARG   B O   1 
ATOM   2983 C  CB  . ARG   B 2 55  ? -0.275  83.211 85.589  1.00 44.00 ? 25  ARG   B CB  1 
ATOM   2984 C  CG  . ARG   B 2 55  ? -1.513  83.075 86.466  1.00 47.30 ? 25  ARG   B CG  1 
ATOM   2985 C  CD  . ARG   B 2 55  ? -1.270  82.155 87.631  1.00 50.22 ? 25  ARG   B CD  1 
ATOM   2986 N  NE  . ARG   B 2 55  ? -1.058  80.788 87.165  1.00 54.10 ? 25  ARG   B NE  1 
ATOM   2987 C  CZ  . ARG   B 2 55  ? -0.172  79.946 87.685  1.00 56.54 ? 25  ARG   B CZ  1 
ATOM   2988 N  NH1 . ARG   B 2 55  ? 0.608   80.328 88.690  1.00 56.81 ? 25  ARG   B NH1 1 
ATOM   2989 N  NH2 . ARG   B 2 55  ? -0.036  78.726 87.183  1.00 55.35 ? 25  ARG   B NH2 1 
ATOM   2990 N  N   . GLN   B 2 56  ? -0.144  86.447 84.655  1.00 42.16 ? 26  GLN   B N   1 
ATOM   2991 C  CA  . GLN   B 2 56  ? -0.502  87.820 85.021  1.00 42.16 ? 26  GLN   B CA  1 
ATOM   2992 C  C   . GLN   B 2 56  ? -1.697  88.368 84.267  1.00 42.40 ? 26  GLN   B C   1 
ATOM   2993 O  O   . GLN   B 2 56  ? -2.479  89.116 84.848  1.00 42.33 ? 26  GLN   B O   1 
ATOM   2994 C  CB  . GLN   B 2 56  ? 0.695   88.768 84.873  1.00 44.06 ? 26  GLN   B CB  1 
ATOM   2995 C  CG  . GLN   B 2 56  ? 1.857   88.498 85.830  1.00 48.96 ? 26  GLN   B CG  1 
ATOM   2996 C  CD  . GLN   B 2 56  ? 1.451   88.474 87.285  1.00 55.57 ? 26  GLN   B CD  1 
ATOM   2997 O  OE1 . GLN   B 2 56  ? 0.704   89.336 87.778  1.00 57.71 ? 26  GLN   B OE1 1 
ATOM   2998 N  NE2 . GLN   B 2 56  ? 1.941   87.478 88.007  1.00 56.93 ? 26  GLN   B NE2 1 
ATOM   2999 N  N   . LYS   B 2 57  ? -1.875  87.978 82.996  1.00 42.58 ? 27  LYS   B N   1 
ATOM   3000 C  CA  . LYS   B 2 57  ? -3.020  88.437 82.216  1.00 43.47 ? 27  LYS   B CA  1 
ATOM   3001 C  C   . LYS   B 2 57  ? -4.344  87.934 82.799  1.00 43.78 ? 27  LYS   B C   1 
ATOM   3002 O  O   . LYS   B 2 57  ? -5.340  88.664 82.778  1.00 44.41 ? 27  LYS   B O   1 
ATOM   3003 C  CB  . LYS   B 2 57  ? -2.867  88.111 80.710  1.00 45.80 ? 27  LYS   B CB  1 
ATOM   3004 C  CG  . LYS   B 2 57  ? -2.740  86.623 80.374  1.00 49.31 ? 27  LYS   B CG  1 
ATOM   3005 C  CD  . LYS   B 2 57  ? -2.256  86.410 78.938  1.00 52.80 ? 27  LYS   B CD  1 
ATOM   3006 C  CE  . LYS   B 2 57  ? -2.233  84.950 78.516  1.00 56.07 ? 27  LYS   B CE  1 
ATOM   3007 N  NZ  . LYS   B 2 57  ? -1.027  84.213 79.002  1.00 57.55 ? 27  LYS   B NZ  1 
ATOM   3008 N  N   . ASP   B 2 58  ? -4.351  86.723 83.375  1.00 43.25 ? 28  ASP   B N   1 
ATOM   3009 C  CA  . ASP   B 2 58  ? -5.547  86.211 84.040  1.00 43.37 ? 28  ASP   B CA  1 
ATOM   3010 C  C   . ASP   B 2 58  ? -5.688  86.733 85.467  1.00 43.62 ? 28  ASP   B C   1 
ATOM   3011 O  O   . ASP   B 2 58  ? -6.809  86.847 85.960  1.00 43.58 ? 28  ASP   B O   1 
ATOM   3012 C  CB  . ASP   B 2 58  ? -5.622  84.680 83.989  1.00 44.49 ? 28  ASP   B CB  1 
ATOM   3013 C  CG  . ASP   B 2 58  ? -6.093  84.133 82.652  1.00 49.07 ? 28  ASP   B CG  1 
ATOM   3014 O  OD1 . ASP   B 2 58  ? -6.587  84.919 81.826  1.00 49.89 ? 28  ASP   B OD1 1 
ATOM   3015 O  OD2 . ASP   B 2 58  ? -5.973  82.920 82.436  1.00 51.95 ? 28  ASP   B OD2 1 
ATOM   3016 N  N   . LEU   B 2 59  ? -4.559  87.077 86.118  1.00 43.72 ? 29  LEU   B N   1 
ATOM   3017 C  CA  . LEU   B 2 59  ? -4.538  87.626 87.470  1.00 44.43 ? 29  LEU   B CA  1 
ATOM   3018 C  C   . LEU   B 2 59  ? -5.049  89.068 87.570  1.00 45.80 ? 29  LEU   B C   1 
ATOM   3019 O  O   . LEU   B 2 59  ? -5.109  89.617 88.670  1.00 46.30 ? 29  LEU   B O   1 
ATOM   3020 C  CB  . LEU   B 2 59  ? -3.167  87.475 88.130  1.00 44.33 ? 29  LEU   B CB  1 
ATOM   3021 C  CG  . LEU   B 2 59  ? -2.639  86.027 88.213  1.00 45.66 ? 29  LEU   B CG  1 
ATOM   3022 C  CD1 . LEU   B 2 59  ? -1.322  85.970 88.967  1.00 46.32 ? 29  LEU   B CD1 1 
ATOM   3023 C  CD2 . LEU   B 2 59  ? -3.656  85.082 88.862  1.00 45.74 ? 29  LEU   B CD2 1 
ATOM   3024 N  N   . LYS   B 2 60  ? -5.460  89.664 86.450  1.00 46.10 ? 30  LYS   B N   1 
ATOM   3025 C  CA  . LYS   B 2 60  ? -6.116  90.954 86.464  1.00 47.31 ? 30  LYS   B CA  1 
ATOM   3026 C  C   . LYS   B 2 60  ? -7.584  90.762 86.906  1.00 47.92 ? 30  LYS   B C   1 
ATOM   3027 O  O   . LYS   B 2 60  ? -8.162  91.673 87.491  1.00 48.73 ? 30  LYS   B O   1 
ATOM   3028 C  CB  . LYS   B 2 60  ? -6.047  91.611 85.074  1.00 50.27 ? 30  LYS   B CB  1 
ATOM   3029 C  CG  . LYS   B 2 60  ? -4.689  92.253 84.782  1.00 55.75 ? 30  LYS   B CG  1 
ATOM   3030 C  CD  . LYS   B 2 60  ? -4.110  91.815 83.438  1.00 61.67 ? 30  LYS   B CD  1 
ATOM   3031 C  CE  . LYS   B 2 60  ? -2.659  92.222 83.284  1.00 66.13 ? 30  LYS   B CE  1 
ATOM   3032 N  NZ  . LYS   B 2 60  ? -2.061  91.726 82.011  1.00 68.49 ? 30  LYS   B NZ  1 
ATOM   3033 N  N   . PHE   B 2 61  ? -8.180  89.575 86.652  1.00 47.27 ? 31  PHE   B N   1 
ATOM   3034 C  CA  . PHE   B 2 61  ? -9.561  89.251 86.986  1.00 47.22 ? 31  PHE   B CA  1 
ATOM   3035 C  C   . PHE   B 2 61  ? -9.667  88.363 88.234  1.00 45.46 ? 31  PHE   B C   1 
ATOM   3036 O  O   . PHE   B 2 61  ? -10.653 88.437 88.967  1.00 45.02 ? 31  PHE   B O   1 
ATOM   3037 C  CB  . PHE   B 2 61  ? -10.207 88.520 85.803  1.00 48.12 ? 31  PHE   B CB  1 
ATOM   3038 C  CG  . PHE   B 2 61  ? -10.214 89.313 84.518  1.00 50.15 ? 31  PHE   B CG  1 
ATOM   3039 C  CD1 . PHE   B 2 61  ? -9.154  89.233 83.627  1.00 51.50 ? 31  PHE   B CD1 1 
ATOM   3040 C  CD2 . PHE   B 2 61  ? -11.294 90.105 84.180  1.00 51.12 ? 31  PHE   B CD2 1 
ATOM   3041 C  CE1 . PHE   B 2 61  ? -9.165  89.957 82.446  1.00 52.30 ? 31  PHE   B CE1 1 
ATOM   3042 C  CE2 . PHE   B 2 61  ? -11.308 90.812 82.987  1.00 52.08 ? 31  PHE   B CE2 1 
ATOM   3043 C  CZ  . PHE   B 2 61  ? -10.244 90.734 82.129  1.00 51.97 ? 31  PHE   B CZ  1 
ATOM   3044 N  N   . LEU   B 2 62  ? -8.676  87.485 88.443  1.00 43.78 ? 32  LEU   B N   1 
ATOM   3045 C  CA  . LEU   B 2 62  ? -8.708  86.549 89.559  1.00 42.54 ? 32  LEU   B CA  1 
ATOM   3046 C  C   . LEU   B 2 62  ? -7.501  86.702 90.452  1.00 41.85 ? 32  LEU   B C   1 
ATOM   3047 O  O   . LEU   B 2 62  ? -6.418  86.976 89.957  1.00 42.36 ? 32  LEU   B O   1 
ATOM   3048 C  CB  . LEU   B 2 62  ? -8.715  85.112 89.010  1.00 42.06 ? 32  LEU   B CB  1 
ATOM   3049 C  CG  . LEU   B 2 62  ? -9.846  84.764 88.056  1.00 42.69 ? 32  LEU   B CG  1 
ATOM   3050 C  CD1 . LEU   B 2 62  ? -9.374  83.828 86.989  1.00 43.00 ? 32  LEU   B CD1 1 
ATOM   3051 C  CD2 . LEU   B 2 62  ? -11.036 84.191 88.799  1.00 42.89 ? 32  LEU   B CD2 1 
ATOM   3052 N  N   . SER   B 2 63  ? -7.657  86.453 91.753  1.00 40.83 ? 33  SER   B N   1 
ATOM   3053 C  CA  . SER   B 2 63  ? -6.506  86.453 92.651  1.00 40.54 ? 33  SER   B CA  1 
ATOM   3054 C  C   . SER   B 2 63  ? -5.702  85.174 92.389  1.00 41.13 ? 33  SER   B C   1 
ATOM   3055 O  O   . SER   B 2 63  ? -6.213  84.228 91.770  1.00 41.77 ? 33  SER   B O   1 
ATOM   3056 C  CB  . SER   B 2 63  ? -6.949  86.532 94.109  1.00 40.72 ? 33  SER   B CB  1 
ATOM   3057 O  OG  . SER   B 2 63  ? -7.552  85.327 94.537  1.00 42.56 ? 33  SER   B OG  1 
ATOM   3058 N  N   . GLU   B 2 64  ? -4.456  85.105 92.879  1.00 40.79 ? 34  GLU   B N   1 
ATOM   3059 C  CA  . GLU   B 2 64  ? -3.640  83.893 92.714  1.00 40.85 ? 34  GLU   B CA  1 
ATOM   3060 C  C   . GLU   B 2 64  ? -4.341  82.664 93.325  1.00 39.11 ? 34  GLU   B C   1 
ATOM   3061 O  O   . GLU   B 2 64  ? -4.294  81.577 92.763  1.00 39.06 ? 34  GLU   B O   1 
ATOM   3062 C  CB  . GLU   B 2 64  ? -2.279  84.085 93.383  1.00 45.12 ? 34  GLU   B CB  1 
ATOM   3063 C  CG  . GLU   B 2 64  ? -1.348  85.000 92.620  1.00 52.45 ? 34  GLU   B CG  1 
ATOM   3064 C  CD  . GLU   B 2 64  ? 0.094   84.703 92.969  1.00 60.93 ? 34  GLU   B CD  1 
ATOM   3065 O  OE1 . GLU   B 2 64  ? 0.442   84.829 94.165  1.00 62.54 ? 34  GLU   B OE1 1 
ATOM   3066 O  OE2 . GLU   B 2 64  ? 0.865   84.316 92.059  1.00 63.11 ? 34  GLU   B OE2 1 
ATOM   3067 N  N   . GLU   B 2 65  ? -5.018  82.876 94.457  1.00 37.60 ? 35  GLU   B N   1 
ATOM   3068 C  CA  . GLU   B 2 65  ? -5.783  81.883 95.198  1.00 36.32 ? 35  GLU   B CA  1 
ATOM   3069 C  C   . GLU   B 2 65  ? -6.974  81.383 94.377  1.00 34.73 ? 35  GLU   B C   1 
ATOM   3070 O  O   . GLU   B 2 65  ? -7.203  80.189 94.299  1.00 35.36 ? 35  GLU   B O   1 
ATOM   3071 C  CB  . GLU   B 2 65  ? -6.262  82.510 96.513  1.00 38.57 ? 35  GLU   B CB  1 
ATOM   3072 C  CG  . GLU   B 2 65  ? -6.624  81.511 97.584  1.00 45.78 ? 35  GLU   B CG  1 
ATOM   3073 C  CD  . GLU   B 2 65  ? -6.919  82.155 98.924  1.00 54.85 ? 35  GLU   B CD  1 
ATOM   3074 O  OE1 . GLU   B 2 65  ? -7.483  83.273 98.935  1.00 57.34 ? 35  GLU   B OE1 1 
ATOM   3075 O  OE2 . GLU   B 2 65  ? -6.591  81.540 99.963  1.00 57.65 ? 35  GLU   B OE2 1 
ATOM   3076 N  N   . GLU   B 2 66  ? -7.719  82.281 93.761  1.00 33.26 ? 36  GLU   B N   1 
ATOM   3077 C  CA  . GLU   B 2 66  ? -8.869  81.952 92.929  1.00 32.55 ? 36  GLU   B CA  1 
ATOM   3078 C  C   . GLU   B 2 66  ? -8.452  81.263 91.643  1.00 31.75 ? 36  GLU   B C   1 
ATOM   3079 O  O   . GLU   B 2 66  ? -9.196  80.441 91.134  1.00 31.57 ? 36  GLU   B O   1 
ATOM   3080 C  CB  . GLU   B 2 66  ? -9.629  83.237 92.578  1.00 34.95 ? 36  GLU   B CB  1 
ATOM   3081 C  CG  . GLU   B 2 66  ? -10.251 83.927 93.776  1.00 36.92 ? 36  GLU   B CG  1 
ATOM   3082 C  CD  . GLU   B 2 66  ? -10.917 85.223 93.370  1.00 41.84 ? 36  GLU   B CD  1 
ATOM   3083 O  OE1 . GLU   B 2 66  ? -10.342 85.934 92.514  1.00 41.27 ? 36  GLU   B OE1 1 
ATOM   3084 O  OE2 . GLU   B 2 66  ? -12.023 85.516 93.880  1.00 44.68 ? 36  GLU   B OE2 1 
ATOM   3085 N  N   . TYR   B 2 67  ? -7.292  81.629 91.088  1.00 31.74 ? 37  TYR   B N   1 
ATOM   3086 C  CA  . TYR   B 2 67  ? -6.767  80.987 89.892  1.00 32.06 ? 37  TYR   B CA  1 
ATOM   3087 C  C   . TYR   B 2 67  ? -6.376  79.537 90.274  1.00 33.77 ? 37  TYR   B C   1 
ATOM   3088 O  O   . TYR   B 2 67  ? -6.656  78.610 89.514  1.00 34.38 ? 37  TYR   B O   1 
ATOM   3089 C  CB  . TYR   B 2 67  ? -5.558  81.772 89.333  1.00 30.97 ? 37  TYR   B CB  1 
ATOM   3090 C  CG  . TYR   B 2 67  ? -5.058  81.226 88.016  1.00 30.38 ? 37  TYR   B CG  1 
ATOM   3091 C  CD1 . TYR   B 2 67  ? -4.191  80.141 87.973  1.00 30.84 ? 37  TYR   B CD1 1 
ATOM   3092 C  CD2 . TYR   B 2 67  ? -5.525  81.729 86.811  1.00 30.70 ? 37  TYR   B CD2 1 
ATOM   3093 C  CE1 . TYR   B 2 67  ? -3.782  79.586 86.764  1.00 31.03 ? 37  TYR   B CE1 1 
ATOM   3094 C  CE2 . TYR   B 2 67  ? -5.109  81.197 85.597  1.00 31.11 ? 37  TYR   B CE2 1 
ATOM   3095 C  CZ  . TYR   B 2 67  ? -4.234  80.128 85.578  1.00 31.78 ? 37  TYR   B CZ  1 
ATOM   3096 O  OH  . TYR   B 2 67  ? -3.815  79.608 84.377  1.00 33.66 ? 37  TYR   B OH  1 
ATOM   3097 N  N   . TRP   B 2 68  ? -5.761  79.337 91.467  1.00 33.86 ? 38  TRP   B N   1 
ATOM   3098 C  CA  . TRP   B 2 68  ? -5.401  77.995 91.908  1.00 34.34 ? 38  TRP   B CA  1 
ATOM   3099 C  C   . TRP   B 2 68  ? -6.667  77.145 92.093  1.00 33.49 ? 38  TRP   B C   1 
ATOM   3100 O  O   . TRP   B 2 68  ? -6.750  76.057 91.516  1.00 34.94 ? 38  TRP   B O   1 
ATOM   3101 C  CB  . TRP   B 2 68  ? -4.520  78.012 93.186  1.00 34.90 ? 38  TRP   B CB  1 
ATOM   3102 C  CG  . TRP   B 2 68  ? -4.019  76.652 93.635  1.00 36.52 ? 38  TRP   B CG  1 
ATOM   3103 C  CD1 . TRP   B 2 68  ? -4.000  75.489 92.907  1.00 37.46 ? 38  TRP   B CD1 1 
ATOM   3104 C  CD2 . TRP   B 2 68  ? -3.381  76.348 94.892  1.00 37.07 ? 38  TRP   B CD2 1 
ATOM   3105 N  NE1 . TRP   B 2 68  ? -3.438  74.476 93.650  1.00 37.94 ? 38  TRP   B NE1 1 
ATOM   3106 C  CE2 . TRP   B 2 68  ? -3.056  74.974 94.875  1.00 37.92 ? 38  TRP   B CE2 1 
ATOM   3107 C  CE3 . TRP   B 2 68  ? -3.086  77.098 96.045  1.00 37.62 ? 38  TRP   B CE3 1 
ATOM   3108 C  CZ2 . TRP   B 2 68  ? -2.419  74.346 95.952  1.00 38.47 ? 38  TRP   B CZ2 1 
ATOM   3109 C  CZ3 . TRP   B 2 68  ? -2.462  76.473 97.112  1.00 38.20 ? 38  TRP   B CZ3 1 
ATOM   3110 C  CH2 . TRP   B 2 68  ? -2.134  75.117 97.061  1.00 38.48 ? 38  TRP   B CH2 1 
ATOM   3111 N  N   . LYS   B 2 69  ? -7.680  77.680 92.779  1.00 31.09 ? 39  LYS   B N   1 
ATOM   3112 C  CA  . LYS   B 2 69  ? -8.954  76.999 92.994  1.00 29.84 ? 39  LYS   B CA  1 
ATOM   3113 C  C   . LYS   B 2 69  ? -9.647  76.583 91.696  1.00 29.87 ? 39  LYS   B C   1 
ATOM   3114 O  O   . LYS   B 2 69  ? -10.264 75.526 91.659  1.00 28.72 ? 39  LYS   B O   1 
ATOM   3115 C  CB  . LYS   B 2 69  ? -9.870  77.881 93.832  1.00 30.28 ? 39  LYS   B CB  1 
ATOM   3116 C  CG  . LYS   B 2 69  ? -9.337  78.076 95.237  1.00 32.79 ? 39  LYS   B CG  1 
ATOM   3117 C  CD  . LYS   B 2 69  ? -10.037 79.209 96.000  1.00 33.77 ? 39  LYS   B CD  1 
ATOM   3118 C  CE  . LYS   B 2 69  ? -9.643  79.164 97.455  1.00 34.12 ? 39  LYS   B CE  1 
ATOM   3119 N  NZ  . LYS   B 2 69  ? -10.486 80.047 98.311  1.00 34.35 ? 39  LYS   B NZ  1 
ATOM   3120 N  N   . LEU   B 2 70  ? -9.543  77.408 90.632  1.00 31.16 ? 40  LEU   B N   1 
ATOM   3121 C  CA  . LEU   B 2 70  ? -10.114 77.095 89.320  1.00 33.14 ? 40  LEU   B CA  1 
ATOM   3122 C  C   . LEU   B 2 70  ? -9.365  75.902 88.695  1.00 34.36 ? 40  LEU   B C   1 
ATOM   3123 O  O   . LEU   B 2 70  ? -9.984  75.054 88.046  1.00 34.69 ? 40  LEU   B O   1 
ATOM   3124 C  CB  . LEU   B 2 70  ? -10.006 78.306 88.376  1.00 34.25 ? 40  LEU   B CB  1 
ATOM   3125 C  CG  . LEU   B 2 70  ? -11.318 78.988 88.004  1.00 37.41 ? 40  LEU   B CG  1 
ATOM   3126 C  CD1 . LEU   B 2 70  ? -11.079 80.155 87.079  1.00 38.80 ? 40  LEU   B CD1 1 
ATOM   3127 C  CD2 . LEU   B 2 70  ? -12.245 78.041 87.311  1.00 38.28 ? 40  LEU   B CD2 1 
ATOM   3128 N  N   . GLN   B 2 71  ? -8.033  75.821 88.915  1.00 34.44 ? 41  GLN   B N   1 
ATOM   3129 C  CA  . GLN   B 2 71  ? -7.250  74.715 88.371  1.00 34.68 ? 41  GLN   B CA  1 
ATOM   3130 C  C   . GLN   B 2 71  ? -7.552  73.416 89.105  1.00 33.20 ? 41  GLN   B C   1 
ATOM   3131 O  O   . GLN   B 2 71  ? -7.575  72.362 88.473  1.00 32.93 ? 41  GLN   B O   1 
ATOM   3132 C  CB  . GLN   B 2 71  ? -5.750  75.057 88.310  1.00 37.47 ? 41  GLN   B CB  1 
ATOM   3133 C  CG  . GLN   B 2 71  ? -5.447  76.178 87.287  1.00 42.65 ? 41  GLN   B CG  1 
ATOM   3134 C  CD  . GLN   B 2 71  ? -5.643  75.781 85.817  1.00 50.62 ? 41  GLN   B CD  1 
ATOM   3135 O  OE1 . GLN   B 2 71  ? -4.953  74.903 85.269  1.00 52.22 ? 41  GLN   B OE1 1 
ATOM   3136 N  NE2 . GLN   B 2 71  ? -6.572  76.444 85.128  1.00 52.37 ? 41  GLN   B NE2 1 
ATOM   3137 N  N   . ILE   B 2 72  ? -7.837  73.495 90.429  1.00 32.03 ? 42  ILE   B N   1 
ATOM   3138 C  CA  . ILE   B 2 72  ? -8.246  72.356 91.251  1.00 30.97 ? 42  ILE   B CA  1 
ATOM   3139 C  C   . ILE   B 2 72  ? -9.591  71.858 90.708  1.00 30.41 ? 42  ILE   B C   1 
ATOM   3140 O  O   . ILE   B 2 72  ? -9.731  70.677 90.416  1.00 30.93 ? 42  ILE   B O   1 
ATOM   3141 C  CB  . ILE   B 2 72  ? -8.359  72.757 92.753  1.00 30.89 ? 42  ILE   B CB  1 
ATOM   3142 C  CG1 . ILE   B 2 72  ? -6.978  72.945 93.401  1.00 31.13 ? 42  ILE   B CG1 1 
ATOM   3143 C  CG2 . ILE   B 2 72  ? -9.206  71.750 93.537  1.00 31.10 ? 42  ILE   B CG2 1 
ATOM   3144 C  CD1 . ILE   B 2 72  ? -7.034  73.642 94.654  1.00 31.87 ? 42  ILE   B CD1 1 
ATOM   3145 N  N   . PHE   B 2 73  ? -10.543 72.785 90.525  1.00 29.80 ? 43  PHE   B N   1 
ATOM   3146 C  CA  . PHE   B 2 73  ? -11.883 72.546 90.022  1.00 29.40 ? 43  PHE   B CA  1 
ATOM   3147 C  C   . PHE   B 2 73  ? -11.865 71.814 88.697  1.00 29.20 ? 43  PHE   B C   1 
ATOM   3148 O  O   . PHE   B 2 73  ? -12.474 70.754 88.612  1.00 30.51 ? 43  PHE   B O   1 
ATOM   3149 C  CB  . PHE   B 2 73  ? -12.675 73.875 89.907  1.00 28.87 ? 43  PHE   B CB  1 
ATOM   3150 C  CG  . PHE   B 2 73  ? -14.075 73.685 89.359  1.00 28.84 ? 43  PHE   B CG  1 
ATOM   3151 C  CD1 . PHE   B 2 73  ? -15.016 72.960 90.062  1.00 29.34 ? 43  PHE   B CD1 1 
ATOM   3152 C  CD2 . PHE   B 2 73  ? -14.421 74.174 88.117  1.00 29.53 ? 43  PHE   B CD2 1 
ATOM   3153 C  CE1 . PHE   B 2 73  ? -16.289 72.769 89.554  1.00 30.21 ? 43  PHE   B CE1 1 
ATOM   3154 C  CE2 . PHE   B 2 73  ? -15.694 73.977 87.604  1.00 30.24 ? 43  PHE   B CE2 1 
ATOM   3155 C  CZ  . PHE   B 2 73  ? -16.616 73.261 88.319  1.00 30.12 ? 43  PHE   B CZ  1 
ATOM   3156 N  N   . PHE   B 2 74  ? -11.136 72.320 87.693  1.00 28.29 ? 44  PHE   B N   1 
ATOM   3157 C  CA  . PHE   B 2 74  ? -11.076 71.714 86.362  1.00 28.69 ? 44  PHE   B CA  1 
ATOM   3158 C  C   . PHE   B 2 74  ? -10.307 70.404 86.331  1.00 28.15 ? 44  PHE   B C   1 
ATOM   3159 O  O   . PHE   B 2 74  ? -10.672 69.527 85.547  1.00 28.12 ? 44  PHE   B O   1 
ATOM   3160 C  CB  . PHE   B 2 74  ? -10.575 72.696 85.296  1.00 29.41 ? 44  PHE   B CB  1 
ATOM   3161 C  CG  . PHE   B 2 74  ? -11.709 73.572 84.823  1.00 30.36 ? 44  PHE   B CG  1 
ATOM   3162 C  CD1 . PHE   B 2 74  ? -12.759 73.037 84.090  1.00 31.02 ? 44  PHE   B CD1 1 
ATOM   3163 C  CD2 . PHE   B 2 74  ? -11.760 74.916 85.166  1.00 30.92 ? 44  PHE   B CD2 1 
ATOM   3164 C  CE1 . PHE   B 2 74  ? -13.834 73.829 83.700  1.00 31.65 ? 44  PHE   B CE1 1 
ATOM   3165 C  CE2 . PHE   B 2 74  ? -12.826 75.712 84.757  1.00 31.72 ? 44  PHE   B CE2 1 
ATOM   3166 C  CZ  . PHE   B 2 74  ? -13.866 75.157 84.041  1.00 31.69 ? 44  PHE   B CZ  1 
ATOM   3167 N  N   . THR   B 2 75  ? -9.359  70.192 87.258  1.00 27.49 ? 45  THR   B N   1 
ATOM   3168 C  CA  . THR   B 2 75  ? -8.735  68.873 87.408  1.00 28.09 ? 45  THR   B CA  1 
ATOM   3169 C  C   . THR   B 2 75  ? -9.819  67.868 87.878  1.00 28.07 ? 45  THR   B C   1 
ATOM   3170 O  O   . THR   B 2 75  ? -9.891  66.742 87.380  1.00 28.30 ? 45  THR   B O   1 
ATOM   3171 C  CB  . THR   B 2 75  ? -7.615  68.937 88.444  1.00 30.20 ? 45  THR   B CB  1 
ATOM   3172 O  OG1 . THR   B 2 75  ? -6.588  69.767 87.923  1.00 32.64 ? 45  THR   B OG1 1 
ATOM   3173 C  CG2 . THR   B 2 75  ? -7.043  67.575 88.772  1.00 30.28 ? 45  THR   B CG2 1 
ATOM   3174 N  N   . ASN   B 2 76  ? -10.687 68.294 88.817  1.00 27.60 ? 46  ASN   B N   1 
ATOM   3175 C  CA  . ASN   B 2 76  ? -11.769 67.437 89.308  1.00 27.42 ? 46  ASN   B CA  1 
ATOM   3176 C  C   . ASN   B 2 76  ? -12.822 67.191 88.236  1.00 28.37 ? 46  ASN   B C   1 
ATOM   3177 O  O   . ASN   B 2 76  ? -13.444 66.142 88.246  1.00 28.73 ? 46  ASN   B O   1 
ATOM   3178 C  CB  . ASN   B 2 76  ? -12.411 68.042 90.549  1.00 27.04 ? 46  ASN   B CB  1 
ATOM   3179 C  CG  . ASN   B 2 76  ? -11.453 68.129 91.707  1.00 28.78 ? 46  ASN   B CG  1 
ATOM   3180 O  OD1 . ASN   B 2 76  ? -10.425 67.441 91.754  1.00 30.26 ? 46  ASN   B OD1 1 
ATOM   3181 N  ND2 . ASN   B 2 76  ? -11.759 68.982 92.667  1.00 28.03 ? 46  ASN   B ND2 1 
ATOM   3182 N  N   . VAL   B 2 77  ? -13.040 68.156 87.325  1.00 28.66 ? 47  VAL   B N   1 
ATOM   3183 C  CA  . VAL   B 2 77  ? -14.009 67.990 86.244  1.00 29.07 ? 47  VAL   B CA  1 
ATOM   3184 C  C   . VAL   B 2 77  ? -13.476 66.923 85.289  1.00 29.10 ? 47  VAL   B C   1 
ATOM   3185 O  O   . VAL   B 2 77  ? -14.208 65.996 84.950  1.00 29.54 ? 47  VAL   B O   1 
ATOM   3186 C  CB  . VAL   B 2 77  ? -14.270 69.339 85.512  1.00 29.79 ? 47  VAL   B CB  1 
ATOM   3187 C  CG1 . VAL   B 2 77  ? -15.073 69.132 84.229  1.00 30.15 ? 47  VAL   B CG1 1 
ATOM   3188 C  CG2 . VAL   B 2 77  ? -14.955 70.349 86.429  1.00 29.92 ? 47  VAL   B CG2 1 
ATOM   3189 N  N   . ILE   B 2 78  ? -12.192 67.023 84.894  1.00 28.40 ? 48  ILE   B N   1 
ATOM   3190 C  CA  . ILE   B 2 78  ? -11.563 66.058 83.983  1.00 28.69 ? 48  ILE   B CA  1 
ATOM   3191 C  C   . ILE   B 2 78  ? -11.566 64.642 84.571  1.00 29.37 ? 48  ILE   B C   1 
ATOM   3192 O  O   . ILE   B 2 78  ? -11.921 63.685 83.885  1.00 29.55 ? 48  ILE   B O   1 
ATOM   3193 C  CB  . ILE   B 2 78  ? -10.141 66.536 83.571  1.00 28.86 ? 48  ILE   B CB  1 
ATOM   3194 C  CG1 . ILE   B 2 78  ? -10.217 67.809 82.724  1.00 28.78 ? 48  ILE   B CG1 1 
ATOM   3195 C  CG2 . ILE   B 2 78  ? -9.369  65.446 82.815  1.00 29.49 ? 48  ILE   B CG2 1 
ATOM   3196 C  CD1 . ILE   B 2 78  ? -8.946  68.523 82.666  1.00 29.40 ? 48  ILE   B CD1 1 
ATOM   3197 N  N   . GLN   B 2 79  ? -11.250 64.523 85.868  1.00 29.67 ? 49  GLN   B N   1 
ATOM   3198 C  CA  . GLN   B 2 79  ? -11.287 63.268 86.609  1.00 30.24 ? 49  GLN   B CA  1 
ATOM   3199 C  C   . GLN   B 2 79  ? -12.690 62.628 86.530  1.00 30.39 ? 49  GLN   B C   1 
ATOM   3200 O  O   . GLN   B 2 79  ? -12.810 61.439 86.251  1.00 31.20 ? 49  GLN   B O   1 
ATOM   3201 C  CB  . GLN   B 2 79  ? -10.899 63.521 88.082  1.00 32.39 ? 49  GLN   B CB  1 
ATOM   3202 C  CG  . GLN   B 2 79  ? -10.975 62.291 88.958  1.00 36.86 ? 49  GLN   B CG  1 
ATOM   3203 C  CD  . GLN   B 2 79  ? -9.907  61.304 88.570  1.00 44.05 ? 49  GLN   B CD  1 
ATOM   3204 O  OE1 . GLN   B 2 79  ? -8.768  61.675 88.225  1.00 45.92 ? 49  GLN   B OE1 1 
ATOM   3205 N  NE2 . GLN   B 2 79  ? -10.239 60.020 88.643  1.00 45.41 ? 49  GLN   B NE2 1 
ATOM   3206 N  N   . ALA   B 2 80  ? -13.733 63.419 86.752  1.00 29.72 ? 50  ALA   B N   1 
ATOM   3207 C  CA  . ALA   B 2 80  ? -15.114 62.975 86.727  1.00 29.97 ? 50  ALA   B CA  1 
ATOM   3208 C  C   . ALA   B 2 80  ? -15.523 62.592 85.317  1.00 30.82 ? 50  ALA   B C   1 
ATOM   3209 O  O   . ALA   B 2 80  ? -16.253 61.621 85.140  1.00 30.38 ? 50  ALA   B O   1 
ATOM   3210 C  CB  . ALA   B 2 80  ? -16.018 64.088 87.241  1.00 29.90 ? 50  ALA   B CB  1 
ATOM   3211 N  N   . LEU   B 2 81  ? -15.070 63.349 84.300  1.00 31.90 ? 51  LEU   B N   1 
ATOM   3212 C  CA  . LEU   B 2 81  ? -15.391 63.021 82.907  1.00 33.58 ? 51  LEU   B CA  1 
ATOM   3213 C  C   . LEU   B 2 81  ? -14.780 61.668 82.549  1.00 34.08 ? 51  LEU   B C   1 
ATOM   3214 O  O   . LEU   B 2 81  ? -15.445 60.861 81.919  1.00 33.77 ? 51  LEU   B O   1 
ATOM   3215 C  CB  . LEU   B 2 81  ? -14.853 64.073 81.920  1.00 34.73 ? 51  LEU   B CB  1 
ATOM   3216 C  CG  . LEU   B 2 81  ? -15.414 65.470 81.984  1.00 37.88 ? 51  LEU   B CG  1 
ATOM   3217 C  CD1 . LEU   B 2 81  ? -14.527 66.436 81.195  1.00 38.75 ? 51  LEU   B CD1 1 
ATOM   3218 C  CD2 . LEU   B 2 81  ? -16.826 65.509 81.461  1.00 39.09 ? 51  LEU   B CD2 1 
ATOM   3219 N  N   . GLY   B 2 82  ? -13.525 61.451 82.958  1.00 34.99 ? 52  GLY   B N   1 
ATOM   3220 C  CA  . GLY   B 2 82  ? -12.792 60.225 82.699  1.00 36.29 ? 52  GLY   B CA  1 
ATOM   3221 C  C   . GLY   B 2 82  ? -13.424 59.036 83.384  1.00 37.48 ? 52  GLY   B C   1 
ATOM   3222 O  O   . GLY   B 2 82  ? -13.568 57.979 82.773  1.00 38.53 ? 52  GLY   B O   1 
ATOM   3223 N  N   . GLU   B 2 83  ? -13.852 59.207 84.640  1.00 37.07 ? 53  GLU   B N   1 
ATOM   3224 C  CA  . GLU   B 2 83  ? -14.517 58.138 85.378  1.00 37.04 ? 53  GLU   B CA  1 
ATOM   3225 C  C   . GLU   B 2 83  ? -15.821 57.749 84.710  1.00 38.12 ? 53  GLU   B C   1 
ATOM   3226 O  O   . GLU   B 2 83  ? -16.110 56.553 84.553  1.00 39.41 ? 53  GLU   B O   1 
ATOM   3227 C  CB  . GLU   B 2 83  ? -14.788 58.572 86.815  1.00 38.00 ? 53  GLU   B CB  1 
ATOM   3228 C  CG  . GLU   B 2 83  ? -13.549 58.572 87.688  1.00 41.79 ? 53  GLU   B CG  1 
ATOM   3229 C  CD  . GLU   B 2 83  ? -13.728 59.235 89.038  1.00 47.64 ? 53  GLU   B CD  1 
ATOM   3230 O  OE1 . GLU   B 2 83  ? -14.872 59.612 89.378  1.00 49.03 ? 53  GLU   B OE1 1 
ATOM   3231 O  OE2 . GLU   B 2 83  ? -12.715 59.384 89.757  1.00 50.04 ? 53  GLU   B OE2 1 
ATOM   3232 N  N   . HIS   B 2 84  ? -16.586 58.739 84.261  1.00 37.45 ? 54  HIS   B N   1 
ATOM   3233 C  CA  . HIS   B 2 84  ? -17.855 58.501 83.601  1.00 37.65 ? 54  HIS   B CA  1 
ATOM   3234 C  C   . HIS   B 2 84  ? -17.663 57.717 82.309  1.00 37.74 ? 54  HIS   B C   1 
ATOM   3235 O  O   . HIS   B 2 84  ? -18.453 56.827 82.004  1.00 38.28 ? 54  HIS   B O   1 
ATOM   3236 C  CB  . HIS   B 2 84  ? -18.540 59.840 83.319  1.00 38.82 ? 54  HIS   B CB  1 
ATOM   3237 C  CG  . HIS   B 2 84  ? -19.942 59.711 82.812  1.00 41.31 ? 54  HIS   B CG  1 
ATOM   3238 N  ND1 . HIS   B 2 84  ? -21.025 59.858 83.654  1.00 43.38 ? 54  HIS   B ND1 1 
ATOM   3239 C  CD2 . HIS   B 2 84  ? -20.389 59.432 81.565  1.00 42.02 ? 54  HIS   B CD2 1 
ATOM   3240 C  CE1 . HIS   B 2 84  ? -22.092 59.672 82.896  1.00 43.84 ? 54  HIS   B CE1 1 
ATOM   3241 N  NE2 . HIS   B 2 84  ? -21.756 59.408 81.634  1.00 43.34 ? 54  HIS   B NE2 1 
ATOM   3242 N  N   . LEU   B 2 85  ? -16.598 58.024 81.569  1.00 37.32 ? 55  LEU   B N   1 
ATOM   3243 C  CA  . LEU   B 2 85  ? -16.275 57.350 80.318  1.00 37.39 ? 55  LEU   B CA  1 
ATOM   3244 C  C   . LEU   B 2 85  ? -15.469 56.043 80.507  1.00 39.08 ? 55  LEU   B C   1 
ATOM   3245 O  O   . LEU   B 2 85  ? -15.062 55.434 79.522  1.00 39.20 ? 55  LEU   B O   1 
ATOM   3246 C  CB  . LEU   B 2 85  ? -15.537 58.325 79.391  1.00 36.35 ? 55  LEU   B CB  1 
ATOM   3247 C  CG  . LEU   B 2 85  ? -16.374 59.470 78.836  1.00 36.09 ? 55  LEU   B CG  1 
ATOM   3248 C  CD1 . LEU   B 2 85  ? -15.502 60.629 78.413  1.00 36.04 ? 55  LEU   B CD1 1 
ATOM   3249 C  CD2 . LEU   B 2 85  ? -17.229 59.013 77.684  1.00 36.05 ? 55  LEU   B CD2 1 
ATOM   3250 N  N   . LYS   B 2 86  ? -15.253 55.613 81.763  1.00 40.13 ? 56  LYS   B N   1 
ATOM   3251 C  CA  . LYS   B 2 86  ? -14.533 54.392 82.131  1.00 41.91 ? 56  LYS   B CA  1 
ATOM   3252 C  C   . LYS   B 2 86  ? -13.088 54.386 81.639  1.00 42.78 ? 56  LYS   B C   1 
ATOM   3253 O  O   . LYS   B 2 86  ? -12.539 53.334 81.318  1.00 43.37 ? 56  LYS   B O   1 
ATOM   3254 C  CB  . LYS   B 2 86  ? -15.298 53.127 81.697  1.00 44.82 ? 56  LYS   B CB  1 
ATOM   3255 C  CG  . LYS   B 2 86  ? -16.549 52.866 82.526  1.00 50.66 ? 56  LYS   B CG  1 
ATOM   3256 C  CD  . LYS   B 2 86  ? -17.568 51.995 81.784  1.00 56.97 ? 56  LYS   B CD  1 
ATOM   3257 C  CE  . LYS   B 2 86  ? -18.902 51.971 82.509  1.00 62.18 ? 56  LYS   B CE  1 
ATOM   3258 N  NZ  . LYS   B 2 86  ? -20.016 51.439 81.659  1.00 65.05 ? 56  LYS   B NZ  1 
ATOM   3259 N  N   . LEU   B 2 87  ? -12.470 55.564 81.600  1.00 42.63 ? 57  LEU   B N   1 
ATOM   3260 C  CA  . LEU   B 2 87  ? -11.101 55.687 81.161  1.00 42.85 ? 57  LEU   B CA  1 
ATOM   3261 C  C   . LEU   B 2 87  ? -10.146 55.362 82.279  1.00 43.56 ? 57  LEU   B C   1 
ATOM   3262 O  O   . LEU   B 2 87  ? -10.423 55.630 83.445  1.00 44.17 ? 57  LEU   B O   1 
ATOM   3263 C  CB  . LEU   B 2 87  ? -10.830 57.097 80.600  1.00 42.50 ? 57  LEU   B CB  1 
ATOM   3264 C  CG  . LEU   B 2 87  ? -11.730 57.525 79.456  1.00 43.20 ? 57  LEU   B CG  1 
ATOM   3265 C  CD1 . LEU   B 2 87  ? -11.418 58.914 79.039  1.00 43.77 ? 57  LEU   B CD1 1 
ATOM   3266 C  CD2 . LEU   B 2 87  ? -11.559 56.628 78.266  1.00 43.55 ? 57  LEU   B CD2 1 
ATOM   3267 N  N   . ARG   B 2 88  ? -9.008  54.789 81.914  1.00 43.61 ? 58  ARG   B N   1 
ATOM   3268 C  CA  . ARG   B 2 88  ? -7.930  54.438 82.835  1.00 43.78 ? 58  ARG   B CA  1 
ATOM   3269 C  C   . ARG   B 2 88  ? -7.312  55.745 83.379  1.00 42.26 ? 58  ARG   B C   1 
ATOM   3270 O  O   . ARG   B 2 88  ? -7.375  56.764 82.707  1.00 41.94 ? 58  ARG   B O   1 
ATOM   3271 C  CB  . ARG   B 2 88  ? -6.916  53.573 82.057  1.00 46.79 ? 58  ARG   B CB  1 
ATOM   3272 C  CG  . ARG   B 2 88  ? -5.575  53.297 82.715  1.00 53.26 ? 58  ARG   B CG  1 
ATOM   3273 C  CD  . ARG   B 2 88  ? -4.793  52.278 81.887  1.00 59.78 ? 58  ARG   B CD  1 
ATOM   3274 N  NE  . ARG   B 2 88  ? -3.865  52.900 80.936  1.00 64.41 ? 58  ARG   B NE  1 
ATOM   3275 C  CZ  . ARG   B 2 88  ? -4.127  53.102 79.648  1.00 67.86 ? 58  ARG   B CZ  1 
ATOM   3276 N  NH1 . ARG   B 2 88  ? -3.220  53.671 78.862  1.00 69.18 ? 58  ARG   B NH1 1 
ATOM   3277 N  NH2 . ARG   B 2 88  ? -5.297  52.740 79.135  1.00 67.44 ? 58  ARG   B NH2 1 
ATOM   3278 N  N   . GLN   B 2 89  ? -6.757  55.733 84.604  1.00 41.32 ? 59  GLN   B N   1 
ATOM   3279 C  CA  . GLN   B 2 89  ? -6.171  56.923 85.221  1.00 40.84 ? 59  GLN   B CA  1 
ATOM   3280 C  C   . GLN   B 2 89  ? -5.122  57.588 84.335  1.00 40.76 ? 59  GLN   B C   1 
ATOM   3281 O  O   . GLN   B 2 89  ? -5.048  58.807 84.310  1.00 41.06 ? 59  GLN   B O   1 
ATOM   3282 C  CB  . GLN   B 2 89  ? -5.578  56.602 86.599  1.00 41.65 ? 59  GLN   B CB  1 
ATOM   3283 C  CG  . GLN   B 2 89  ? -5.155  57.817 87.416  1.00 45.20 ? 59  GLN   B CG  1 
ATOM   3284 C  CD  . GLN   B 2 89  ? -6.317  58.712 87.806  1.00 50.66 ? 59  GLN   B CD  1 
ATOM   3285 O  OE1 . GLN   B 2 89  ? -7.284  58.279 88.457  1.00 52.64 ? 59  GLN   B OE1 1 
ATOM   3286 N  NE2 . GLN   B 2 89  ? -6.243  59.991 87.432  1.00 50.15 ? 59  GLN   B NE2 1 
ATOM   3287 N  N   . GLN   B 2 90  ? -4.364  56.799 83.560  1.00 40.00 ? 60  GLN   B N   1 
ATOM   3288 C  CA  . GLN   B 2 90  ? -3.329  57.332 82.688  1.00 39.51 ? 60  GLN   B CA  1 
ATOM   3289 C  C   . GLN   B 2 90  ? -3.911  58.251 81.613  1.00 37.29 ? 60  GLN   B C   1 
ATOM   3290 O  O   . GLN   B 2 90  ? -3.283  59.244 81.266  1.00 37.07 ? 60  GLN   B O   1 
ATOM   3291 C  CB  . GLN   B 2 90  ? -2.518  56.204 82.046  1.00 42.48 ? 60  GLN   B CB  1 
ATOM   3292 C  CG  . GLN   B 2 90  ? -1.192  56.712 81.481  1.00 49.15 ? 60  GLN   B CG  1 
ATOM   3293 C  CD  . GLN   B 2 90  ? -0.322  55.621 80.921  1.00 56.59 ? 60  GLN   B CD  1 
ATOM   3294 O  OE1 . GLN   B 2 90  ? -0.068  54.594 81.565  1.00 59.16 ? 60  GLN   B OE1 1 
ATOM   3295 N  NE2 . GLN   B 2 90  ? 0.161   55.829 79.705  1.00 57.51 ? 60  GLN   B NE2 1 
ATOM   3296 N  N   . VAL   B 2 91  ? -5.092  57.903 81.076  1.00 35.20 ? 61  VAL   B N   1 
ATOM   3297 C  CA  . VAL   B 2 91  ? -5.774  58.714 80.079  1.00 33.67 ? 61  VAL   B CA  1 
ATOM   3298 C  C   . VAL   B 2 91  ? -6.193  60.039 80.728  1.00 31.50 ? 61  VAL   B C   1 
ATOM   3299 O  O   . VAL   B 2 91  ? -5.890  61.110 80.204  1.00 31.16 ? 61  VAL   B O   1 
ATOM   3300 C  CB  . VAL   B 2 91  ? -6.986  57.981 79.475  1.00 34.44 ? 61  VAL   B CB  1 
ATOM   3301 C  CG1 . VAL   B 2 91  ? -7.758  58.909 78.546  1.00 35.32 ? 61  VAL   B CG1 1 
ATOM   3302 C  CG2 . VAL   B 2 91  ? -6.559  56.710 78.748  1.00 34.93 ? 61  VAL   B CG2 1 
ATOM   3303 N  N   . ILE   B 2 92  ? -6.812  59.959 81.910  1.00 29.92 ? 62  ILE   B N   1 
ATOM   3304 C  CA  . ILE   B 2 92  ? -7.229  61.125 82.686  1.00 28.95 ? 62  ILE   B CA  1 
ATOM   3305 C  C   . ILE   B 2 92  ? -6.036  62.051 83.004  1.00 28.03 ? 62  ILE   B C   1 
ATOM   3306 O  O   . ILE   B 2 92  ? -6.145  63.256 82.848  1.00 28.56 ? 62  ILE   B O   1 
ATOM   3307 C  CB  . ILE   B 2 92  ? -7.952  60.670 83.968  1.00 29.09 ? 62  ILE   B CB  1 
ATOM   3308 C  CG1 . ILE   B 2 92  ? -9.154  59.770 83.627  1.00 30.18 ? 62  ILE   B CG1 1 
ATOM   3309 C  CG2 . ILE   B 2 92  ? -8.358  61.872 84.797  1.00 29.33 ? 62  ILE   B CG2 1 
ATOM   3310 C  CD1 . ILE   B 2 92  ? -9.904  59.186 84.826  1.00 31.85 ? 62  ILE   B CD1 1 
ATOM   3311 N  N   . ALA   B 2 93  ? -4.898  61.486 83.376  1.00 27.43 ? 63  ALA   B N   1 
ATOM   3312 C  CA  . ALA   B 2 93  ? -3.702  62.241 83.714  1.00 27.94 ? 63  ALA   B CA  1 
ATOM   3313 C  C   . ALA   B 2 93  ? -3.147  62.955 82.507  1.00 28.16 ? 63  ALA   B C   1 
ATOM   3314 O  O   . ALA   B 2 93  ? -2.807  64.130 82.610  1.00 29.15 ? 63  ALA   B O   1 
ATOM   3315 C  CB  . ALA   B 2 93  ? -2.649  61.324 84.315  1.00 27.92 ? 63  ALA   B CB  1 
ATOM   3316 N  N   . THR   B 2 94  ? -3.110  62.281 81.348  1.00 27.34 ? 64  THR   B N   1 
ATOM   3317 C  CA  . THR   B 2 94  ? -2.624  62.872 80.114  1.00 26.98 ? 64  THR   B CA  1 
ATOM   3318 C  C   . THR   B 2 94  ? -3.531  64.049 79.720  1.00 26.81 ? 64  THR   B C   1 
ATOM   3319 O  O   . THR   B 2 94  ? -3.033  65.118 79.386  1.00 26.90 ? 64  THR   B O   1 
ATOM   3320 C  CB  . THR   B 2 94  ? -2.484  61.759 79.079  1.00 27.40 ? 64  THR   B CB  1 
ATOM   3321 O  OG1 . THR   B 2 94  ? -1.342  60.978 79.442  1.00 28.41 ? 64  THR   B OG1 1 
ATOM   3322 C  CG2 . THR   B 2 94  ? -2.321  62.270 77.656  1.00 26.73 ? 64  THR   B CG2 1 
ATOM   3323 N  N   . ALA   B 2 95  ? -4.862  63.863 79.847  1.00 26.48 ? 65  ALA   B N   1 
ATOM   3324 C  CA  . ALA   B 2 95  ? -5.852  64.894 79.543  1.00 26.60 ? 65  ALA   B CA  1 
ATOM   3325 C  C   . ALA   B 2 95  ? -5.688  66.100 80.480  1.00 26.21 ? 65  ALA   B C   1 
ATOM   3326 O  O   . ALA   B 2 95  ? -5.897  67.233 80.071  1.00 25.68 ? 65  ALA   B O   1 
ATOM   3327 C  CB  . ALA   B 2 95  ? -7.250  64.318 79.698  1.00 26.33 ? 65  ALA   B CB  1 
ATOM   3328 N  N   . THR   B 2 96  ? -5.351  65.842 81.748  1.00 25.87 ? 66  THR   B N   1 
ATOM   3329 C  CA  . THR   B 2 96  ? -5.166  66.901 82.724  1.00 26.12 ? 66  THR   B CA  1 
ATOM   3330 C  C   . THR   B 2 96  ? -3.953  67.736 82.354  1.00 26.73 ? 66  THR   B C   1 
ATOM   3331 O  O   . THR   B 2 96  ? -4.008  68.956 82.435  1.00 27.29 ? 66  THR   B O   1 
ATOM   3332 C  CB  . THR   B 2 96  ? -5.015  66.285 84.110  1.00 26.23 ? 66  THR   B CB  1 
ATOM   3333 O  OG1 . THR   B 2 96  ? -6.203  65.539 84.414  1.00 26.28 ? 66  THR   B OG1 1 
ATOM   3334 C  CG2 . THR   B 2 96  ? -4.700  67.324 85.170  1.00 26.03 ? 66  THR   B CG2 1 
ATOM   3335 N  N   . VAL   B 2 97  ? -2.866  67.076 81.927  1.00 26.85 ? 67  VAL   B N   1 
ATOM   3336 C  CA  . VAL   B 2 97  ? -1.637  67.742 81.529  1.00 27.16 ? 67  VAL   B CA  1 
ATOM   3337 C  C   . VAL   B 2 97  ? -1.873  68.584 80.296  1.00 27.28 ? 67  VAL   B C   1 
ATOM   3338 O  O   . VAL   B 2 97  ? -1.413  69.714 80.272  1.00 28.31 ? 67  VAL   B O   1 
ATOM   3339 C  CB  . VAL   B 2 97  ? -0.466  66.738 81.355  1.00 27.84 ? 67  VAL   B CB  1 
ATOM   3340 C  CG1 . VAL   B 2 97  ? 0.757   67.409 80.710  1.00 28.25 ? 67  VAL   B CG1 1 
ATOM   3341 C  CG2 . VAL   B 2 97  ? -0.094  66.117 82.696  1.00 27.72 ? 67  VAL   B CG2 1 
ATOM   3342 N  N   . TYR   B 2 98  ? -2.651  68.092 79.308  1.00 26.64 ? 68  TYR   B N   1 
ATOM   3343 C  CA  . TYR   B 2 98  ? -2.953  68.867 78.087  1.00 26.46 ? 68  TYR   B CA  1 
ATOM   3344 C  C   . TYR   B 2 98  ? -3.679  70.164 78.468  1.00 26.43 ? 68  TYR   B C   1 
ATOM   3345 O  O   . TYR   B 2 98  ? -3.374  71.217 77.939  1.00 26.57 ? 68  TYR   B O   1 
ATOM   3346 C  CB  . TYR   B 2 98  ? -3.879  68.084 77.128  1.00 26.34 ? 68  TYR   B CB  1 
ATOM   3347 C  CG  . TYR   B 2 98  ? -3.299  66.871 76.431  1.00 26.84 ? 68  TYR   B CG  1 
ATOM   3348 C  CD1 . TYR   B 2 98  ? -1.926  66.661 76.372  1.00 27.32 ? 68  TYR   B CD1 1 
ATOM   3349 C  CD2 . TYR   B 2 98  ? -4.125  65.953 75.797  1.00 27.44 ? 68  TYR   B CD2 1 
ATOM   3350 C  CE1 . TYR   B 2 98  ? -1.394  65.561 75.706  1.00 27.82 ? 68  TYR   B CE1 1 
ATOM   3351 C  CE2 . TYR   B 2 98  ? -3.606  64.844 75.144  1.00 28.23 ? 68  TYR   B CE2 1 
ATOM   3352 C  CZ  . TYR   B 2 98  ? -2.242  64.652 75.097  1.00 28.78 ? 68  TYR   B CZ  1 
ATOM   3353 O  OH  . TYR   B 2 98  ? -1.767  63.538 74.460  1.00 29.28 ? 68  TYR   B OH  1 
ATOM   3354 N  N   . PHE   B 2 99  ? -4.641  70.066 79.390  1.00 26.06 ? 69  PHE   B N   1 
ATOM   3355 C  CA  . PHE   B 2 99  ? -5.427  71.188 79.878  1.00 26.32 ? 69  PHE   B CA  1 
ATOM   3356 C  C   . PHE   B 2 99  ? -4.514  72.201 80.575  1.00 26.70 ? 69  PHE   B C   1 
ATOM   3357 O  O   . PHE   B 2 99  ? -4.634  73.403 80.339  1.00 26.52 ? 69  PHE   B O   1 
ATOM   3358 C  CB  . PHE   B 2 99  ? -6.483  70.643 80.858  1.00 26.50 ? 69  PHE   B CB  1 
ATOM   3359 C  CG  . PHE   B 2 99  ? -7.486  71.670 81.314  1.00 27.47 ? 69  PHE   B CG  1 
ATOM   3360 C  CD1 . PHE   B 2 99  ? -7.237  72.461 82.424  1.00 27.53 ? 69  PHE   B CD1 1 
ATOM   3361 C  CD2 . PHE   B 2 99  ? -8.667  71.868 80.609  1.00 27.94 ? 69  PHE   B CD2 1 
ATOM   3362 C  CE1 . PHE   B 2 99  ? -8.136  73.432 82.808  1.00 28.27 ? 69  PHE   B CE1 1 
ATOM   3363 C  CE2 . PHE   B 2 99  ? -9.580  72.820 81.018  1.00 28.21 ? 69  PHE   B CE2 1 
ATOM   3364 C  CZ  . PHE   B 2 99  ? -9.312  73.590 82.116  1.00 28.28 ? 69  PHE   B CZ  1 
ATOM   3365 N  N   . LYS   B 2 100 ? -3.592  71.720 81.440  1.00 26.81 ? 70  LYS   B N   1 
ATOM   3366 C  CA  . LYS   B 2 100 ? -2.663  72.614 82.147  1.00 26.60 ? 70  LYS   B CA  1 
ATOM   3367 C  C   . LYS   B 2 100 ? -1.709  73.282 81.179  1.00 27.63 ? 70  LYS   B C   1 
ATOM   3368 O  O   . LYS   B 2 100 ? -1.410  74.449 81.343  1.00 28.30 ? 70  LYS   B O   1 
ATOM   3369 C  CB  . LYS   B 2 100 ? -1.832  71.835 83.174  1.00 26.01 ? 70  LYS   B CB  1 
ATOM   3370 C  CG  . LYS   B 2 100 ? -2.607  71.395 84.380  1.00 26.76 ? 70  LYS   B CG  1 
ATOM   3371 C  CD  . LYS   B 2 100 ? -1.650  70.785 85.383  1.00 28.58 ? 70  LYS   B CD  1 
ATOM   3372 C  CE  . LYS   B 2 100 ? -2.358  70.204 86.567  1.00 30.24 ? 70  LYS   B CE  1 
ATOM   3373 N  NZ  . LYS   B 2 100 ? -3.219  71.225 87.233  1.00 30.53 ? 70  LYS   B NZ  1 
ATOM   3374 N  N   . ARG   B 2 101 ? -1.196  72.530 80.189  1.00 28.11 ? 71  ARG   B N   1 
ATOM   3375 C  CA  . ARG   B 2 101 ? -0.277  73.057 79.192  1.00 28.33 ? 71  ARG   B CA  1 
ATOM   3376 C  C   . ARG   B 2 101 ? -0.973  74.132 78.366  1.00 28.85 ? 71  ARG   B C   1 
ATOM   3377 O  O   . ARG   B 2 101 ? -0.380  75.171 78.100  1.00 28.71 ? 71  ARG   B O   1 
ATOM   3378 C  CB  . ARG   B 2 101 ? 0.257   71.916 78.309  1.00 29.28 ? 71  ARG   B CB  1 
ATOM   3379 C  CG  . ARG   B 2 101 ? 1.206   70.975 79.055  1.00 30.00 ? 71  ARG   B CG  1 
ATOM   3380 C  CD  . ARG   B 2 101 ? 1.757   69.893 78.145  1.00 31.78 ? 71  ARG   B CD  1 
ATOM   3381 N  NE  . ARG   B 2 101 ? 2.838   69.123 78.782  1.00 33.18 ? 71  ARG   B NE  1 
ATOM   3382 C  CZ  . ARG   B 2 101 ? 3.454   68.083 78.217  1.00 31.55 ? 71  ARG   B CZ  1 
ATOM   3383 N  NH1 . ARG   B 2 101 ? 3.105   67.675 77.005  1.00 26.61 ? 71  ARG   B NH1 1 
ATOM   3384 N  NH2 . ARG   B 2 101 ? 4.435   67.457 78.856  1.00 31.87 ? 71  ARG   B NH2 1 
ATOM   3385 N  N   . PHE   B 2 102 ? -2.252  73.928 78.029  1.00 29.44 ? 72  PHE   B N   1 
ATOM   3386 C  CA  . PHE   B 2 102 ? -2.993  74.928 77.269  1.00 30.37 ? 72  PHE   B CA  1 
ATOM   3387 C  C   . PHE   B 2 102 ? -3.128  76.251 78.043  1.00 30.11 ? 72  PHE   B C   1 
ATOM   3388 O  O   . PHE   B 2 102 ? -2.828  77.313 77.498  1.00 30.39 ? 72  PHE   B O   1 
ATOM   3389 C  CB  . PHE   B 2 102 ? -4.368  74.396 76.835  1.00 30.58 ? 72  PHE   B CB  1 
ATOM   3390 C  CG  . PHE   B 2 102 ? -5.049  75.355 75.893  1.00 31.67 ? 72  PHE   B CG  1 
ATOM   3391 C  CD1 . PHE   B 2 102 ? -4.808  75.302 74.537  1.00 32.71 ? 72  PHE   B CD1 1 
ATOM   3392 C  CD2 . PHE   B 2 102 ? -5.909  76.330 76.371  1.00 33.02 ? 72  PHE   B CD2 1 
ATOM   3393 C  CE1 . PHE   B 2 102 ? -5.430  76.196 73.671  1.00 34.15 ? 72  PHE   B CE1 1 
ATOM   3394 C  CE2 . PHE   B 2 102 ? -6.529  77.225 75.504  1.00 34.15 ? 72  PHE   B CE2 1 
ATOM   3395 C  CZ  . PHE   B 2 102 ? -6.279  77.161 74.161  1.00 34.05 ? 72  PHE   B CZ  1 
ATOM   3396 N  N   . TYR   B 2 103 ? -3.582  76.189 79.295  1.00 29.29 ? 73  TYR   B N   1 
ATOM   3397 C  CA  . TYR   B 2 103 ? -3.765  77.388 80.093  1.00 29.45 ? 73  TYR   B CA  1 
ATOM   3398 C  C   . TYR   B 2 103 ? -2.466  77.913 80.743  1.00 31.50 ? 73  TYR   B C   1 
ATOM   3399 O  O   . TYR   B 2 103 ? -2.482  78.993 81.325  1.00 31.69 ? 73  TYR   B O   1 
ATOM   3400 C  CB  . TYR   B 2 103 ? -4.892  77.193 81.100  1.00 28.16 ? 73  TYR   B CB  1 
ATOM   3401 C  CG  . TYR   B 2 103 ? -6.201  77.038 80.367  1.00 27.05 ? 73  TYR   B CG  1 
ATOM   3402 C  CD1 . TYR   B 2 103 ? -6.714  78.072 79.602  1.00 26.81 ? 73  TYR   B CD1 1 
ATOM   3403 C  CD2 . TYR   B 2 103 ? -6.856  75.814 80.323  1.00 26.96 ? 73  TYR   B CD2 1 
ATOM   3404 C  CE1 . TYR   B 2 103 ? -7.896  77.929 78.897  1.00 27.55 ? 73  TYR   B CE1 1 
ATOM   3405 C  CE2 . TYR   B 2 103 ? -8.036  75.655 79.615  1.00 27.42 ? 73  TYR   B CE2 1 
ATOM   3406 C  CZ  . TYR   B 2 103 ? -8.550  76.712 78.894  1.00 28.48 ? 73  TYR   B CZ  1 
ATOM   3407 O  OH  . TYR   B 2 103 ? -9.705  76.562 78.171  1.00 29.79 ? 73  TYR   B OH  1 
ATOM   3408 N  N   . ALA   B 2 104 ? -1.349  77.201 80.602  1.00 32.77 ? 74  ALA   B N   1 
ATOM   3409 C  CA  . ALA   B 2 104 ? -0.050  77.705 81.043  1.00 34.52 ? 74  ALA   B CA  1 
ATOM   3410 C  C   . ALA   B 2 104 ? 0.389   78.782 80.021  1.00 36.60 ? 74  ALA   B C   1 
ATOM   3411 O  O   . ALA   B 2 104 ? 0.981   79.789 80.405  1.00 37.08 ? 74  ALA   B O   1 
ATOM   3412 C  CB  . ALA   B 2 104 ? 0.969   76.579 81.065  1.00 34.45 ? 74  ALA   B CB  1 
ATOM   3413 N  N   . ARG   B 2 105 ? 0.077   78.587 78.728  1.00 37.60 ? 75  ARG   B N   1 
ATOM   3414 C  CA  . ARG   B 2 105 ? 0.430   79.543 77.687  1.00 39.37 ? 75  ARG   B CA  1 
ATOM   3415 C  C   . ARG   B 2 105 ? -0.697  80.480 77.310  1.00 39.73 ? 75  ARG   B C   1 
ATOM   3416 O  O   . ARG   B 2 105 ? -0.415  81.583 76.856  1.00 40.66 ? 75  ARG   B O   1 
ATOM   3417 C  CB  . ARG   B 2 105 ? 0.919   78.808 76.430  1.00 42.58 ? 75  ARG   B CB  1 
ATOM   3418 C  CG  . ARG   B 2 105 ? 2.347   78.309 76.553  1.00 49.29 ? 75  ARG   B CG  1 
ATOM   3419 C  CD  . ARG   B 2 105 ? 2.754   77.388 75.418  1.00 55.64 ? 75  ARG   B CD  1 
ATOM   3420 N  NE  . ARG   B 2 105 ? 2.563   77.983 74.096  1.00 61.43 ? 75  ARG   B NE  1 
ATOM   3421 C  CZ  . ARG   B 2 105 ? 3.097   77.509 72.974  1.00 66.08 ? 75  ARG   B CZ  1 
ATOM   3422 N  NH1 . ARG   B 2 105 ? 2.861   78.111 71.814  1.00 67.02 ? 75  ARG   B NH1 1 
ATOM   3423 N  NH2 . ARG   B 2 105 ? 3.883   76.439 73.004  1.00 66.27 ? 75  ARG   B NH2 1 
ATOM   3424 N  N   . TYR   B 2 106 ? -1.962  80.067 77.475  1.00 39.31 ? 76  TYR   B N   1 
ATOM   3425 C  CA  . TYR   B 2 106 ? -3.089  80.898 77.055  1.00 39.49 ? 76  TYR   B CA  1 
ATOM   3426 C  C   . TYR   B 2 106 ? -4.030  81.267 78.179  1.00 38.29 ? 76  TYR   B C   1 
ATOM   3427 O  O   . TYR   B 2 106 ? -4.102  80.593 79.209  1.00 38.24 ? 76  TYR   B O   1 
ATOM   3428 C  CB  . TYR   B 2 106 ? -3.850  80.243 75.877  1.00 40.62 ? 76  TYR   B CB  1 
ATOM   3429 C  CG  . TYR   B 2 106 ? -2.923  79.988 74.709  1.00 42.99 ? 76  TYR   B CG  1 
ATOM   3430 C  CD1 . TYR   B 2 106 ? -2.576  81.011 73.841  1.00 44.37 ? 76  TYR   B CD1 1 
ATOM   3431 C  CD2 . TYR   B 2 106 ? -2.269  78.771 74.568  1.00 45.00 ? 76  TYR   B CD2 1 
ATOM   3432 C  CE1 . TYR   B 2 106 ? -1.667  80.809 72.815  1.00 45.89 ? 76  TYR   B CE1 1 
ATOM   3433 C  CE2 . TYR   B 2 106 ? -1.330  78.568 73.569  1.00 46.51 ? 76  TYR   B CE2 1 
ATOM   3434 C  CZ  . TYR   B 2 106 ? -1.032  79.592 72.693  1.00 47.76 ? 76  TYR   B CZ  1 
ATOM   3435 O  OH  . TYR   B 2 106 ? -0.118  79.399 71.688  1.00 50.92 ? 76  TYR   B OH  1 
ATOM   3436 N  N   . SER   B 2 107 ? -4.763  82.354 77.971  1.00 36.90 ? 77  SER   B N   1 
ATOM   3437 C  CA  . SER   B 2 107 ? -5.721  82.863 78.927  1.00 36.29 ? 77  SER   B CA  1 
ATOM   3438 C  C   . SER   B 2 107 ? -6.969  81.988 79.007  1.00 35.44 ? 77  SER   B C   1 
ATOM   3439 O  O   . SER   B 2 107 ? -7.390  81.418 78.005  1.00 35.04 ? 77  SER   B O   1 
ATOM   3440 C  CB  . SER   B 2 107 ? -6.123  84.282 78.543  1.00 37.38 ? 77  SER   B CB  1 
ATOM   3441 O  OG  . SER   B 2 107 ? -7.214  84.750 79.322  1.00 40.19 ? 77  SER   B OG  1 
ATOM   3442 N  N   . LEU   B 2 108 ? -7.599  81.955 80.193  1.00 34.75 ? 78  LEU   B N   1 
ATOM   3443 C  CA  . LEU   B 2 108 ? -8.865  81.271 80.434  1.00 34.31 ? 78  LEU   B CA  1 
ATOM   3444 C  C   . LEU   B 2 108 ? -9.974  81.781 79.461  1.00 34.74 ? 78  LEU   B C   1 
ATOM   3445 O  O   . LEU   B 2 108 ? -10.930 81.064 79.195  1.00 34.95 ? 78  LEU   B O   1 
ATOM   3446 C  CB  . LEU   B 2 108 ? -9.289  81.469 81.903  1.00 33.82 ? 78  LEU   B CB  1 
ATOM   3447 C  CG  . LEU   B 2 108 ? -8.499  80.636 82.949  1.00 35.14 ? 78  LEU   B CG  1 
ATOM   3448 C  CD1 . LEU   B 2 108 ? -8.695  81.179 84.368  1.00 35.60 ? 78  LEU   B CD1 1 
ATOM   3449 C  CD2 . LEU   B 2 108 ? -8.892  79.143 82.898  1.00 34.91 ? 78  LEU   B CD2 1 
ATOM   3450 N  N   . LYS   B 2 109 ? -9.831  82.992 78.912  1.00 34.86 ? 79  LYS   B N   1 
ATOM   3451 C  CA  . LYS   B 2 109 ? -10.813 83.534 77.981  1.00 35.65 ? 79  LYS   B CA  1 
ATOM   3452 C  C   . LYS   B 2 109 ? -10.595 83.073 76.532  1.00 35.34 ? 79  LYS   B C   1 
ATOM   3453 O  O   . LYS   B 2 109 ? -11.489 83.240 75.714  1.00 35.60 ? 79  LYS   B O   1 
ATOM   3454 C  CB  . LYS   B 2 109 ? -10.857 85.072 78.051  1.00 38.18 ? 79  LYS   B CB  1 
ATOM   3455 C  CG  . LYS   B 2 109 ? -9.728  85.774 77.339  1.00 43.60 ? 79  LYS   B CG  1 
ATOM   3456 C  CD  . LYS   B 2 109 ? -9.999  87.257 77.169  1.00 49.65 ? 79  LYS   B CD  1 
ATOM   3457 C  CE  . LYS   B 2 109 ? -8.840  87.883 76.427  1.00 56.47 ? 79  LYS   B CE  1 
ATOM   3458 N  NZ  . LYS   B 2 109 ? -9.040  89.343 76.156  1.00 60.49 ? 79  LYS   B NZ  1 
ATOM   3459 N  N   . SER   B 2 110 ? -9.411  82.539 76.191  1.00 34.23 ? 80  SER   B N   1 
ATOM   3460 C  CA  . SER   B 2 110 ? -9.110  82.151 74.820  1.00 34.00 ? 80  SER   B CA  1 
ATOM   3461 C  C   . SER   B 2 110 ? -10.116 81.096 74.335  1.00 33.17 ? 80  SER   B C   1 
ATOM   3462 O  O   . SER   B 2 110 ? -10.801 81.300 73.333  1.00 32.72 ? 80  SER   B O   1 
ATOM   3463 C  CB  . SER   B 2 110 ? -7.672  81.668 74.716  1.00 36.05 ? 80  SER   B CB  1 
ATOM   3464 O  OG  . SER   B 2 110 ? -7.537  80.469 75.463  1.00 40.81 ? 80  SER   B OG  1 
ATOM   3465 N  N   . ILE   B 2 111 ? -10.296 80.038 75.129  1.00 32.30 ? 81  ILE   B N   1 
ATOM   3466 C  CA  . ILE   B 2 111 ? -11.266 78.985 74.867  1.00 31.63 ? 81  ILE   B CA  1 
ATOM   3467 C  C   . ILE   B 2 111 ? -11.915 78.655 76.196  1.00 31.13 ? 81  ILE   B C   1 
ATOM   3468 O  O   . ILE   B 2 111 ? -11.220 78.553 77.200  1.00 31.62 ? 81  ILE   B O   1 
ATOM   3469 C  CB  . ILE   B 2 111 ? -10.599 77.735 74.239  1.00 32.25 ? 81  ILE   B CB  1 
ATOM   3470 C  CG1 . ILE   B 2 111 ? -10.062 78.025 72.811  1.00 33.07 ? 81  ILE   B CG1 1 
ATOM   3471 C  CG2 . ILE   B 2 111 ? -11.557 76.515 74.239  1.00 32.84 ? 81  ILE   B CG2 1 
ATOM   3472 C  CD1 . ILE   B 2 111 ? -9.296  76.836 72.160  1.00 33.97 ? 81  ILE   B CD1 1 
ATOM   3473 N  N   . ASP   B 2 112 ? -13.236 78.457 76.219  1.00 30.45 ? 82  ASP   B N   1 
ATOM   3474 C  CA  . ASP   B 2 112 ? -13.956 78.069 77.430  1.00 30.70 ? 82  ASP   B CA  1 
ATOM   3475 C  C   . ASP   B 2 112 ? -13.384 76.760 78.004  1.00 30.98 ? 82  ASP   B C   1 
ATOM   3476 O  O   . ASP   B 2 112 ? -13.431 75.726 77.344  1.00 31.41 ? 82  ASP   B O   1 
ATOM   3477 C  CB  . ASP   B 2 112 ? -15.457 77.863 77.107  1.00 31.46 ? 82  ASP   B CB  1 
ATOM   3478 C  CG  . ASP   B 2 112 ? -16.364 77.595 78.297  1.00 34.99 ? 82  ASP   B CG  1 
ATOM   3479 O  OD1 . ASP   B 2 112 ? -15.838 77.423 79.430  1.00 34.83 ? 82  ASP   B OD1 1 
ATOM   3480 O  OD2 . ASP   B 2 112 ? -17.602 77.560 78.105  1.00 36.49 ? 82  ASP   B OD2 1 
ATOM   3481 N  N   . PRO   B 2 113 ? -12.872 76.795 79.246  1.00 30.36 ? 83  PRO   B N   1 
ATOM   3482 C  CA  . PRO   B 2 113 ? -12.371 75.563 79.869  1.00 29.90 ? 83  PRO   B CA  1 
ATOM   3483 C  C   . PRO   B 2 113 ? -13.418 74.442 79.983  1.00 30.17 ? 83  PRO   B C   1 
ATOM   3484 O  O   . PRO   B 2 113 ? -13.038 73.278 80.039  1.00 30.24 ? 83  PRO   B O   1 
ATOM   3485 C  CB  . PRO   B 2 113 ? -11.872 76.032 81.241  1.00 30.26 ? 83  PRO   B CB  1 
ATOM   3486 C  CG  . PRO   B 2 113 ? -12.582 77.332 81.490  1.00 30.45 ? 83  PRO   B CG  1 
ATOM   3487 C  CD  . PRO   B 2 113 ? -12.721 77.961 80.141  1.00 29.38 ? 83  PRO   B CD  1 
ATOM   3488 N  N   . VAL   B 2 114 ? -14.728 74.776 79.946  1.00 29.78 ? 84  VAL   B N   1 
ATOM   3489 C  CA  . VAL   B 2 114 ? -15.832 73.797 79.947  1.00 29.01 ? 84  VAL   B CA  1 
ATOM   3490 C  C   . VAL   B 2 114 ? -15.813 72.979 78.640  1.00 27.88 ? 84  VAL   B C   1 
ATOM   3491 O  O   . VAL   B 2 114 ? -16.148 71.806 78.651  1.00 27.93 ? 84  VAL   B O   1 
ATOM   3492 C  CB  . VAL   B 2 114 ? -17.209 74.494 80.193  1.00 29.56 ? 84  VAL   B CB  1 
ATOM   3493 C  CG1 . VAL   B 2 114 ? -18.397 73.566 79.925  1.00 29.56 ? 84  VAL   B CG1 1 
ATOM   3494 C  CG2 . VAL   B 2 114 ? -17.271 75.065 81.597  1.00 29.79 ? 84  VAL   B CG2 1 
ATOM   3495 N  N   . LEU   B 2 115 ? -15.386 73.590 77.531  1.00 26.87 ? 85  LEU   B N   1 
ATOM   3496 C  CA  . LEU   B 2 115 ? -15.227 72.935 76.241  1.00 26.46 ? 85  LEU   B CA  1 
ATOM   3497 C  C   . LEU   B 2 115 ? -13.834 72.276 76.165  1.00 27.50 ? 85  LEU   B C   1 
ATOM   3498 O  O   . LEU   B 2 115 ? -13.683 71.184 75.611  1.00 27.99 ? 85  LEU   B O   1 
ATOM   3499 C  CB  . LEU   B 2 115 ? -15.394 73.985 75.126  1.00 25.93 ? 85  LEU   B CB  1 
ATOM   3500 C  CG  . LEU   B 2 115 ? -15.107 73.535 73.689  1.00 26.56 ? 85  LEU   B CG  1 
ATOM   3501 C  CD1 . LEU   B 2 115 ? -15.988 72.383 73.270  1.00 26.22 ? 85  LEU   B CD1 1 
ATOM   3502 C  CD2 . LEU   B 2 115 ? -15.235 74.702 72.718  1.00 26.81 ? 85  LEU   B CD2 1 
ATOM   3503 N  N   . MET   B 2 116 ? -12.810 72.940 76.718  1.00 27.86 ? 86  MET   B N   1 
ATOM   3504 C  CA  . MET   B 2 116 ? -11.450 72.408 76.707  1.00 28.09 ? 86  MET   B CA  1 
ATOM   3505 C  C   . MET   B 2 116 ? -11.322 71.093 77.468  1.00 28.10 ? 86  MET   B C   1 
ATOM   3506 O  O   . MET   B 2 116 ? -10.683 70.180 76.948  1.00 29.54 ? 86  MET   B O   1 
ATOM   3507 C  CB  . MET   B 2 116 ? -10.417 73.440 77.236  1.00 27.85 ? 86  MET   B CB  1 
ATOM   3508 C  CG  . MET   B 2 116 ? -8.955  72.956 77.110  1.00 28.27 ? 86  MET   B CG  1 
ATOM   3509 S  SD  . MET   B 2 116 ? -8.479  72.548 75.379  1.00 28.61 ? 86  MET   B SD  1 
ATOM   3510 C  CE  . MET   B 2 116 ? -8.306  74.128 74.730  1.00 28.13 ? 86  MET   B CE  1 
ATOM   3511 N  N   . ALA   B 2 117 ? -11.945 70.968 78.658  1.00 27.07 ? 87  ALA   B N   1 
ATOM   3512 C  CA  . ALA   B 2 117 ? -11.850 69.757 79.495  1.00 26.97 ? 87  ALA   B CA  1 
ATOM   3513 C  C   . ALA   B 2 117 ? -12.311 68.460 78.779  1.00 28.21 ? 87  ALA   B C   1 
ATOM   3514 O  O   . ALA   B 2 117 ? -11.481 67.551 78.667  1.00 28.99 ? 87  ALA   B O   1 
ATOM   3515 C  CB  . ALA   B 2 117 ? -12.560 69.950 80.832  1.00 26.11 ? 87  ALA   B CB  1 
ATOM   3516 N  N   . PRO   B 2 118 ? -13.530 68.359 78.179  1.00 28.06 ? 88  PRO   B N   1 
ATOM   3517 C  CA  . PRO   B 2 118 ? -13.862 67.135 77.421  1.00 28.14 ? 88  PRO   B CA  1 
ATOM   3518 C  C   . PRO   B 2 118 ? -13.017 66.982 76.155  1.00 28.28 ? 88  PRO   B C   1 
ATOM   3519 O  O   . PRO   B 2 118 ? -12.745 65.859 75.761  1.00 28.30 ? 88  PRO   B O   1 
ATOM   3520 C  CB  . PRO   B 2 118 ? -15.348 67.302 77.078  1.00 28.41 ? 88  PRO   B CB  1 
ATOM   3521 C  CG  . PRO   B 2 118 ? -15.615 68.725 77.193  1.00 28.69 ? 88  PRO   B CG  1 
ATOM   3522 C  CD  . PRO   B 2 118 ? -14.669 69.295 78.203  1.00 27.25 ? 88  PRO   B CD  1 
ATOM   3523 N  N   . THR   B 2 119 ? -12.556 68.091 75.551  1.00 27.95 ? 89  THR   B N   1 
ATOM   3524 C  CA  . THR   B 2 119 ? -11.711 68.009 74.356  1.00 27.90 ? 89  THR   B CA  1 
ATOM   3525 C  C   . THR   B 2 119 ? -10.372 67.362 74.700  1.00 27.90 ? 89  THR   B C   1 
ATOM   3526 O  O   . THR   B 2 119 ? -9.848  66.595 73.905  1.00 27.78 ? 89  THR   B O   1 
ATOM   3527 C  CB  . THR   B 2 119 ? -11.458 69.403 73.755  1.00 28.41 ? 89  THR   B CB  1 
ATOM   3528 O  OG1 . THR   B 2 119 ? -12.697 70.064 73.489  1.00 29.76 ? 89  THR   B OG1 1 
ATOM   3529 C  CG2 . THR   B 2 119 ? -10.620 69.339 72.505  1.00 27.54 ? 89  THR   B CG2 1 
ATOM   3530 N  N   . CYS   B 2 120 ? -9.811  67.694 75.876  1.00 27.79 ? 90  CYS   B N   1 
ATOM   3531 C  CA  . CYS   B 2 120 ? -8.552  67.122 76.349  1.00 27.82 ? 90  CYS   B CA  1 
ATOM   3532 C  C   . CYS   B 2 120 ? -8.720  65.634 76.586  1.00 28.47 ? 90  CYS   B C   1 
ATOM   3533 O  O   . CYS   B 2 120 ? -7.856  64.845 76.200  1.00 28.79 ? 90  CYS   B O   1 
ATOM   3534 C  CB  . CYS   B 2 120 ? -8.083  67.834 77.615  1.00 27.53 ? 90  CYS   B CB  1 
ATOM   3535 S  SG  . CYS   B 2 120 ? -7.392  69.478 77.327  1.00 27.42 ? 90  CYS   B SG  1 
ATOM   3536 N  N   . VAL   B 2 121 ? -9.845  65.241 77.220  1.00 28.43 ? 91  VAL   B N   1 
ATOM   3537 C  CA  . VAL   B 2 121 ? -10.168 63.843 77.473  1.00 27.99 ? 91  VAL   B CA  1 
ATOM   3538 C  C   . VAL   B 2 121 ? -10.288 63.064 76.141  1.00 28.26 ? 91  VAL   B C   1 
ATOM   3539 O  O   . VAL   B 2 121 ? -9.762  61.960 76.013  1.00 28.29 ? 91  VAL   B O   1 
ATOM   3540 C  CB  . VAL   B 2 121 ? -11.462 63.738 78.324  1.00 27.83 ? 91  VAL   B CB  1 
ATOM   3541 C  CG1 . VAL   B 2 121 ? -12.015 62.315 78.323  1.00 27.34 ? 91  VAL   B CG1 1 
ATOM   3542 C  CG2 . VAL   B 2 121 ? -11.226 64.233 79.754  1.00 28.04 ? 91  VAL   B CG2 1 
ATOM   3543 N  N   . PHE   B 2 122 ? -11.014 63.627 75.178  1.00 27.80 ? 92  PHE   B N   1 
ATOM   3544 C  CA  . PHE   B 2 122 ? -11.247 63.020 73.867  1.00 27.55 ? 92  PHE   B CA  1 
ATOM   3545 C  C   . PHE   B 2 122 ? -9.926  62.771 73.128  1.00 27.33 ? 92  PHE   B C   1 
ATOM   3546 O  O   . PHE   B 2 122 ? -9.730  61.685 72.595  1.00 28.15 ? 92  PHE   B O   1 
ATOM   3547 C  CB  . PHE   B 2 122 ? -12.183 63.935 73.044  1.00 27.26 ? 92  PHE   B CB  1 
ATOM   3548 C  CG  . PHE   B 2 122 ? -12.434 63.549 71.609  1.00 28.06 ? 92  PHE   B CG  1 
ATOM   3549 C  CD1 . PHE   B 2 122 ? -13.204 62.444 71.297  1.00 29.01 ? 92  PHE   B CD1 1 
ATOM   3550 C  CD2 . PHE   B 2 122 ? -11.982 64.345 70.573  1.00 28.93 ? 92  PHE   B CD2 1 
ATOM   3551 C  CE1 . PHE   B 2 122 ? -13.446 62.095 69.972  1.00 30.01 ? 92  PHE   B CE1 1 
ATOM   3552 C  CE2 . PHE   B 2 122 ? -12.245 64.011 69.249  1.00 29.85 ? 92  PHE   B CE2 1 
ATOM   3553 C  CZ  . PHE   B 2 122 ? -12.991 62.897 68.955  1.00 29.76 ? 92  PHE   B CZ  1 
ATOM   3554 N  N   . LEU   B 2 123 ? -9.005  63.741 73.134  1.00 26.30 ? 93  LEU   B N   1 
ATOM   3555 C  CA  . LEU   B 2 123 ? -7.707  63.572 72.460  1.00 25.73 ? 93  LEU   B CA  1 
ATOM   3556 C  C   . LEU   B 2 123 ? -6.791  62.601 73.217  1.00 26.61 ? 93  LEU   B C   1 
ATOM   3557 O  O   . LEU   B 2 123 ? -6.157  61.762 72.585  1.00 26.96 ? 93  LEU   B O   1 
ATOM   3558 C  CB  . LEU   B 2 123 ? -7.013  64.942 72.268  1.00 24.68 ? 93  LEU   B CB  1 
ATOM   3559 C  CG  . LEU   B 2 123 ? -5.642  64.960 71.565  1.00 24.84 ? 93  LEU   B CG  1 
ATOM   3560 C  CD1 . LEU   B 2 123 ? -5.705  64.405 70.156  1.00 24.48 ? 93  LEU   B CD1 1 
ATOM   3561 C  CD2 . LEU   B 2 123 ? -5.030  66.376 71.560  1.00 25.34 ? 93  LEU   B CD2 1 
ATOM   3562 N  N   . ALA   B 2 124 ? -6.737  62.682 74.563  1.00 26.63 ? 94  ALA   B N   1 
ATOM   3563 C  CA  . ALA   B 2 124 ? -5.869  61.802 75.348  1.00 27.60 ? 94  ALA   B CA  1 
ATOM   3564 C  C   . ALA   B 2 124 ? -6.253  60.343 75.160  1.00 29.44 ? 94  ALA   B C   1 
ATOM   3565 O  O   . ALA   B 2 124 ? -5.388  59.484 75.081  1.00 29.54 ? 94  ALA   B O   1 
ATOM   3566 C  CB  . ALA   B 2 124 ? -5.927  62.168 76.832  1.00 27.04 ? 94  ALA   B CB  1 
ATOM   3567 N  N   . SER   B 2 125 ? -7.556  60.066 75.081  1.00 30.24 ? 95  SER   B N   1 
ATOM   3568 C  CA  . SER   B 2 125 ? -8.076  58.725 74.858  1.00 30.98 ? 95  SER   B CA  1 
ATOM   3569 C  C   . SER   B 2 125 ? -7.551  58.162 73.510  1.00 30.83 ? 95  SER   B C   1 
ATOM   3570 O  O   . SER   B 2 125 ? -7.309  56.973 73.417  1.00 30.75 ? 95  SER   B O   1 
ATOM   3571 C  CB  . SER   B 2 125 ? -9.600  58.748 74.910  1.00 33.46 ? 95  SER   B CB  1 
ATOM   3572 O  OG  . SER   B 2 125 ? -10.131 57.496 74.505  1.00 39.38 ? 95  SER   B OG  1 
ATOM   3573 N  N   . LYS   B 2 126 ? -7.314  59.017 72.503  1.00 30.41 ? 96  LYS   B N   1 
ATOM   3574 C  CA  . LYS   B 2 126 ? -6.770  58.568 71.219  1.00 30.83 ? 96  LYS   B CA  1 
ATOM   3575 C  C   . LYS   B 2 126 ? -5.274  58.293 71.306  1.00 31.98 ? 96  LYS   B C   1 
ATOM   3576 O  O   . LYS   B 2 126 ? -4.811  57.268 70.804  1.00 32.14 ? 96  LYS   B O   1 
ATOM   3577 C  CB  . LYS   B 2 126 ? -7.068  59.588 70.117  1.00 30.85 ? 96  LYS   B CB  1 
ATOM   3578 C  CG  . LYS   B 2 126 ? -8.560  59.799 69.982  1.00 31.90 ? 96  LYS   B CG  1 
ATOM   3579 C  CD  . LYS   B 2 126 ? -8.936  60.351 68.659  1.00 32.92 ? 96  LYS   B CD  1 
ATOM   3580 C  CE  . LYS   B 2 126 ? -8.963  61.831 68.715  1.00 33.51 ? 96  LYS   B CE  1 
ATOM   3581 N  NZ  . LYS   B 2 126 ? -9.881  62.389 67.693  1.00 34.32 ? 96  LYS   B NZ  1 
ATOM   3582 N  N   . VAL   B 2 127 ? -4.522  59.199 71.982  1.00 32.02 ? 97  VAL   B N   1 
ATOM   3583 C  CA  . VAL   B 2 127 ? -3.080  59.085 72.165  1.00 31.76 ? 97  VAL   B CA  1 
ATOM   3584 C  C   . VAL   B 2 127 ? -2.756  57.849 72.983  1.00 32.67 ? 97  VAL   B C   1 
ATOM   3585 O  O   . VAL   B 2 127 ? -1.866  57.086 72.626  1.00 32.16 ? 97  VAL   B O   1 
ATOM   3586 C  CB  . VAL   B 2 127 ? -2.507  60.385 72.796  1.00 31.39 ? 97  VAL   B CB  1 
ATOM   3587 C  CG1 . VAL   B 2 127 ? -1.017  60.262 73.120  1.00 31.15 ? 97  VAL   B CG1 1 
ATOM   3588 C  CG2 . VAL   B 2 127 ? -2.779  61.587 71.904  1.00 31.08 ? 97  VAL   B CG2 1 
ATOM   3589 N  N   . GLU   B 2 128 ? -3.506  57.629 74.062  1.00 34.12 ? 98  GLU   B N   1 
ATOM   3590 C  CA  . GLU   B 2 128 ? -3.295  56.483 74.942  1.00 36.24 ? 98  GLU   B CA  1 
ATOM   3591 C  C   . GLU   B 2 128 ? -3.845  55.140 74.381  1.00 38.67 ? 98  GLU   B C   1 
ATOM   3592 O  O   . GLU   B 2 128 ? -3.826  54.131 75.092  1.00 39.09 ? 98  GLU   B O   1 
ATOM   3593 C  CB  . GLU   B 2 128 ? -3.848  56.780 76.338  1.00 37.83 ? 98  GLU   B CB  1 
ATOM   3594 C  CG  . GLU   B 2 128 ? -3.273  58.056 76.938  1.00 40.88 ? 98  GLU   B CG  1 
ATOM   3595 C  CD  . GLU   B 2 128 ? -1.855  57.927 77.455  1.00 46.87 ? 98  GLU   B CD  1 
ATOM   3596 O  OE1 . GLU   B 2 128 ? -1.455  56.789 77.791  1.00 50.76 ? 98  GLU   B OE1 1 
ATOM   3597 O  OE2 . GLU   B 2 128 ? -1.150  58.957 77.548  1.00 46.26 ? 98  GLU   B OE2 1 
ATOM   3598 N  N   . GLU   B 2 129 ? -4.290  55.145 73.104  1.00 39.59 ? 99  GLU   B N   1 
ATOM   3599 C  CA  . GLU   B 2 129 ? -4.817  54.028 72.339  1.00 41.64 ? 99  GLU   B CA  1 
ATOM   3600 C  C   . GLU   B 2 129 ? -6.007  53.361 73.012  1.00 43.07 ? 99  GLU   B C   1 
ATOM   3601 O  O   . GLU   B 2 129 ? -6.158  52.144 72.966  1.00 43.52 ? 99  GLU   B O   1 
ATOM   3602 C  CB  . GLU   B 2 129 ? -3.710  53.025 71.967  1.00 44.95 ? 99  GLU   B CB  1 
ATOM   3603 C  CG  . GLU   B 2 129 ? -2.640  53.667 71.094  1.00 50.42 ? 99  GLU   B CG  1 
ATOM   3604 C  CD  . GLU   B 2 129 ? -1.905  52.748 70.137  1.00 57.94 ? 99  GLU   B CD  1 
ATOM   3605 O  OE1 . GLU   B 2 129 ? -2.331  52.647 68.963  1.00 60.50 ? 99  GLU   B OE1 1 
ATOM   3606 O  OE2 . GLU   B 2 129 ? -0.888  52.147 70.552  1.00 59.06 ? 99  GLU   B OE2 1 
ATOM   3607 N  N   . PHE   B 2 130 ? -6.840  54.167 73.650  1.00 43.53 ? 100 PHE   B N   1 
ATOM   3608 C  CA  . PHE   B 2 130 ? -8.076  53.714 74.259  1.00 44.80 ? 100 PHE   B CA  1 
ATOM   3609 C  C   . PHE   B 2 130 ? -9.172  53.690 73.167  1.00 43.22 ? 100 PHE   B C   1 
ATOM   3610 O  O   . PHE   B 2 130 ? -10.014 52.800 73.170  1.00 43.58 ? 100 PHE   B O   1 
ATOM   3611 C  CB  . PHE   B 2 130 ? -8.483  54.655 75.407  1.00 46.95 ? 100 PHE   B CB  1 
ATOM   3612 C  CG  . PHE   B 2 130 ? -9.185  53.979 76.557  1.00 50.30 ? 100 PHE   B CG  1 
ATOM   3613 C  CD1 . PHE   B 2 130 ? -10.500 53.561 76.439  1.00 52.21 ? 100 PHE   B CD1 1 
ATOM   3614 C  CD2 . PHE   B 2 130 ? -8.535  53.778 77.765  1.00 52.58 ? 100 PHE   B CD2 1 
ATOM   3615 C  CE1 . PHE   B 2 130 ? -11.142 52.922 77.496  1.00 53.58 ? 100 PHE   B CE1 1 
ATOM   3616 C  CE2 . PHE   B 2 130 ? -9.188  53.170 78.830  1.00 53.98 ? 100 PHE   B CE2 1 
ATOM   3617 C  CZ  . PHE   B 2 130 ? -10.483 52.727 78.682  1.00 53.82 ? 100 PHE   B CZ  1 
ATOM   3618 N  N   . GLY   B 2 131 ? -9.135  54.647 72.242  1.00 41.29 ? 101 GLY   B N   1 
ATOM   3619 C  CA  . GLY   B 2 131 ? -10.080 54.727 71.145  1.00 40.29 ? 101 GLY   B CA  1 
ATOM   3620 C  C   . GLY   B 2 131 ? -10.698 56.096 70.941  1.00 39.41 ? 101 GLY   B C   1 
ATOM   3621 O  O   . GLY   B 2 131 ? -10.467 57.041 71.702  1.00 38.56 ? 101 GLY   B O   1 
ATOM   3622 N  N   . VAL   B 2 132 ? -11.515 56.196 69.907  1.00 39.20 ? 102 VAL   B N   1 
ATOM   3623 C  CA  . VAL   B 2 132 ? -12.239 57.413 69.601  1.00 38.94 ? 102 VAL   B CA  1 
ATOM   3624 C  C   . VAL   B 2 132 ? -13.566 57.322 70.338  1.00 38.81 ? 102 VAL   B C   1 
ATOM   3625 O  O   . VAL   B 2 132 ? -14.400 56.504 69.953  1.00 39.00 ? 102 VAL   B O   1 
ATOM   3626 C  CB  . VAL   B 2 132 ? -12.507 57.520 68.088  1.00 39.48 ? 102 VAL   B CB  1 
ATOM   3627 C  CG1 . VAL   B 2 132 ? -13.232 58.816 67.760  1.00 39.77 ? 102 VAL   B CG1 1 
ATOM   3628 C  CG2 . VAL   B 2 132 ? -11.220 57.377 67.281  1.00 39.83 ? 102 VAL   B CG2 1 
ATOM   3629 N  N   . VAL   B 2 133 ? -13.783 58.147 71.392  1.00 38.15 ? 103 VAL   B N   1 
ATOM   3630 C  CA  . VAL   B 2 133 ? -15.057 58.182 72.118  1.00 38.01 ? 103 VAL   B CA  1 
ATOM   3631 C  C   . VAL   B 2 133 ? -16.094 58.724 71.130  1.00 38.59 ? 103 VAL   B C   1 
ATOM   3632 O  O   . VAL   B 2 133 ? -15.847 59.764 70.515  1.00 39.03 ? 103 VAL   B O   1 
ATOM   3633 C  CB  . VAL   B 2 133 ? -14.967 59.119 73.355  1.00 38.53 ? 103 VAL   B CB  1 
ATOM   3634 C  CG1 . VAL   B 2 133 ? -16.315 59.247 74.045  1.00 38.57 ? 103 VAL   B CG1 1 
ATOM   3635 C  CG2 . VAL   B 2 133 ? -13.898 58.652 74.339  1.00 39.13 ? 103 VAL   B CG2 1 
ATOM   3636 N  N   . SER   B 2 134 ? -17.202 58.004 70.903  1.00 38.51 ? 104 SER   B N   1 
ATOM   3637 C  CA  . SER   B 2 134 ? -18.215 58.450 69.946  1.00 38.74 ? 104 SER   B CA  1 
ATOM   3638 C  C   . SER   B 2 134 ? -18.753 59.851 70.252  1.00 38.63 ? 104 SER   B C   1 
ATOM   3639 O  O   . SER   B 2 134 ? -18.609 60.342 71.372  1.00 39.22 ? 104 SER   B O   1 
ATOM   3640 C  CB  . SER   B 2 134 ? -19.346 57.435 69.823  1.00 39.99 ? 104 SER   B CB  1 
ATOM   3641 O  OG  . SER   B 2 134 ? -20.281 57.498 70.886  1.00 41.77 ? 104 SER   B OG  1 
ATOM   3642 N  N   . ASN   B 2 135 ? -19.310 60.516 69.244  1.00 37.81 ? 105 ASN   B N   1 
ATOM   3643 C  CA  . ASN   B 2 135 ? -19.858 61.866 69.364  1.00 37.34 ? 105 ASN   B CA  1 
ATOM   3644 C  C   . ASN   B 2 135 ? -20.941 61.909 70.449  1.00 37.20 ? 105 ASN   B C   1 
ATOM   3645 O  O   . ASN   B 2 135 ? -20.870 62.732 71.369  1.00 37.04 ? 105 ASN   B O   1 
ATOM   3646 C  CB  . ASN   B 2 135 ? -20.435 62.302 68.008  1.00 37.37 ? 105 ASN   B CB  1 
ATOM   3647 C  CG  . ASN   B 2 135 ? -19.406 62.336 66.903  1.00 39.43 ? 105 ASN   B CG  1 
ATOM   3648 O  OD1 . ASN   B 2 135 ? -18.200 62.105 67.122  1.00 39.76 ? 105 ASN   B OD1 1 
ATOM   3649 N  ND2 . ASN   B 2 135 ? -19.854 62.643 65.691  1.00 40.18 ? 105 ASN   B ND2 1 
ATOM   3650 N  N   . THR   B 2 136 ? -21.892 60.966 70.382  1.00 36.67 ? 106 THR   B N   1 
ATOM   3651 C  CA  . THR   B 2 136 ? -22.966 60.917 71.359  1.00 37.07 ? 106 THR   B CA  1 
ATOM   3652 C  C   . THR   B 2 136 ? -22.448 60.599 72.754  1.00 35.99 ? 106 THR   B C   1 
ATOM   3653 O  O   . THR   B 2 136 ? -22.846 61.267 73.703  1.00 35.79 ? 106 THR   B O   1 
ATOM   3654 C  CB  . THR   B 2 136 ? -24.082 59.978 70.920  1.00 39.47 ? 106 THR   B CB  1 
ATOM   3655 O  OG1 . THR   B 2 136 ? -24.456 60.300 69.581  1.00 41.41 ? 106 THR   B OG1 1 
ATOM   3656 C  CG2 . THR   B 2 136 ? -25.307 60.099 71.812  1.00 40.14 ? 106 THR   B CG2 1 
ATOM   3657 N  N   . ARG   B 2 137 ? -21.523 59.636 72.874  1.00 34.75 ? 107 ARG   B N   1 
ATOM   3658 C  CA  . ARG   B 2 137 ? -20.993 59.265 74.171  1.00 34.55 ? 107 ARG   B CA  1 
ATOM   3659 C  C   . ARG   B 2 137 ? -20.229 60.401 74.843  1.00 34.50 ? 107 ARG   B C   1 
ATOM   3660 O  O   . ARG   B 2 137 ? -20.442 60.652 76.025  1.00 34.76 ? 107 ARG   B O   1 
ATOM   3661 C  CB  . ARG   B 2 137 ? -20.136 58.007 74.072  1.00 35.54 ? 107 ARG   B CB  1 
ATOM   3662 C  CG  . ARG   B 2 137 ? -20.269 57.086 75.273  1.00 37.91 ? 107 ARG   B CG  1 
ATOM   3663 C  CD  . ARG   B 2 137 ? -19.447 55.820 75.097  1.00 39.94 ? 107 ARG   B CD  1 
ATOM   3664 N  NE  . ARG   B 2 137 ? -18.541 55.607 76.222  1.00 42.52 ? 107 ARG   B NE  1 
ATOM   3665 C  CZ  . ARG   B 2 137 ? -17.234 55.390 76.106  1.00 43.85 ? 107 ARG   B CZ  1 
ATOM   3666 N  NH1 . ARG   B 2 137 ? -16.667 55.331 74.908  1.00 41.00 ? 107 ARG   B NH1 1 
ATOM   3667 N  NH2 . ARG   B 2 137 ? -16.489 55.201 77.189  1.00 44.52 ? 107 ARG   B NH2 1 
ATOM   3668 N  N   . LEU   B 2 138 ? -19.366 61.113 74.095  1.00 33.88 ? 108 LEU   B N   1 
ATOM   3669 C  CA  . LEU   B 2 138 ? -18.594 62.229 74.656  1.00 33.16 ? 108 LEU   B CA  1 
ATOM   3670 C  C   . LEU   B 2 138 ? -19.505 63.389 75.061  1.00 32.27 ? 108 LEU   B C   1 
ATOM   3671 O  O   . LEU   B 2 138 ? -19.329 63.955 76.140  1.00 32.88 ? 108 LEU   B O   1 
ATOM   3672 C  CB  . LEU   B 2 138 ? -17.529 62.713 73.653  1.00 33.44 ? 108 LEU   B CB  1 
ATOM   3673 C  CG  . LEU   B 2 138 ? -16.604 63.813 74.176  1.00 34.69 ? 108 LEU   B CG  1 
ATOM   3674 C  CD1 . LEU   B 2 138 ? -15.655 63.269 75.253  1.00 34.54 ? 108 LEU   B CD1 1 
ATOM   3675 C  CD2 . LEU   B 2 138 ? -15.872 64.478 73.047  1.00 35.16 ? 108 LEU   B CD2 1 
ATOM   3676 N  N   . ILE   B 2 139 ? -20.486 63.730 74.217  1.00 31.10 ? 109 ILE   B N   1 
ATOM   3677 C  CA  . ILE   B 2 139 ? -21.407 64.823 74.526  1.00 31.45 ? 109 ILE   B CA  1 
ATOM   3678 C  C   . ILE   B 2 139 ? -22.348 64.463 75.684  1.00 31.88 ? 109 ILE   B C   1 
ATOM   3679 O  O   . ILE   B 2 139 ? -22.576 65.298 76.557  1.00 32.35 ? 109 ILE   B O   1 
ATOM   3680 C  CB  . ILE   B 2 139 ? -22.166 65.327 73.264  1.00 31.72 ? 109 ILE   B CB  1 
ATOM   3681 C  CG1 . ILE   B 2 139 ? -21.192 65.937 72.220  1.00 32.79 ? 109 ILE   B CG1 1 
ATOM   3682 C  CG2 . ILE   B 2 139 ? -23.261 66.311 73.634  1.00 31.96 ? 109 ILE   B CG2 1 
ATOM   3683 C  CD1 . ILE   B 2 139 ? -20.282 67.047 72.775  1.00 34.45 ? 109 ILE   B CD1 1 
ATOM   3684 N  N   . ALA   B 2 140 ? -22.855 63.219 75.724  1.00 31.70 ? 110 ALA   B N   1 
ATOM   3685 C  CA  . ALA   B 2 140 ? -23.728 62.804 76.820  1.00 31.86 ? 110 ALA   B CA  1 
ATOM   3686 C  C   . ALA   B 2 140 ? -22.953 62.726 78.125  1.00 32.06 ? 110 ALA   B C   1 
ATOM   3687 O  O   . ALA   B 2 140 ? -23.497 63.098 79.148  1.00 32.29 ? 110 ALA   B O   1 
ATOM   3688 C  CB  . ALA   B 2 140 ? -24.397 61.476 76.520  1.00 31.65 ? 110 ALA   B CB  1 
ATOM   3689 N  N   . ALA   B 2 141 ? -21.696 62.270 78.095  1.00 31.94 ? 111 ALA   B N   1 
ATOM   3690 C  CA  . ALA   B 2 141 ? -20.897 62.189 79.316  1.00 32.15 ? 111 ALA   B CA  1 
ATOM   3691 C  C   . ALA   B 2 141 ? -20.621 63.579 79.884  1.00 31.50 ? 111 ALA   B C   1 
ATOM   3692 O  O   . ALA   B 2 141 ? -20.749 63.760 81.080  1.00 31.28 ? 111 ALA   B O   1 
ATOM   3693 C  CB  . ALA   B 2 141 ? -19.590 61.452 79.062  1.00 32.41 ? 111 ALA   B CB  1 
ATOM   3694 N  N   . ALA   B 2 142 ? -20.256 64.558 79.038  1.00 30.52 ? 112 ALA   B N   1 
ATOM   3695 C  CA  . ALA   B 2 142 ? -19.999 65.928 79.496  1.00 29.83 ? 112 ALA   B CA  1 
ATOM   3696 C  C   . ALA   B 2 142 ? -21.290 66.583 80.025  1.00 29.74 ? 112 ALA   B C   1 
ATOM   3697 O  O   . ALA   B 2 142 ? -21.265 67.225 81.075  1.00 29.24 ? 112 ALA   B O   1 
ATOM   3698 C  CB  . ALA   B 2 142 ? -19.399 66.767 78.370  1.00 29.36 ? 112 ALA   B CB  1 
ATOM   3699 N  N   . THR   B 2 143 ? -22.415 66.401 79.312  1.00 29.79 ? 113 THR   B N   1 
ATOM   3700 C  CA  . THR   B 2 143 ? -23.707 66.924 79.736  1.00 30.99 ? 113 THR   B CA  1 
ATOM   3701 C  C   . THR   B 2 143 ? -24.093 66.292 81.103  1.00 32.68 ? 113 THR   B C   1 
ATOM   3702 O  O   . THR   B 2 143 ? -24.451 66.998 82.046  1.00 32.97 ? 113 THR   B O   1 
ATOM   3703 C  CB  . THR   B 2 143 ? -24.784 66.606 78.671  1.00 32.07 ? 113 THR   B CB  1 
ATOM   3704 O  OG1 . THR   B 2 143 ? -24.439 67.185 77.401  1.00 33.07 ? 113 THR   B OG1 1 
ATOM   3705 C  CG2 . THR   B 2 143 ? -26.150 67.072 79.087  1.00 32.08 ? 113 THR   B CG2 1 
ATOM   3706 N  N   . SER   B 2 144 ? -23.931 64.979 81.221  1.00 33.16 ? 114 SER   B N   1 
ATOM   3707 C  CA  . SER   B 2 144 ? -24.278 64.244 82.415  1.00 34.57 ? 114 SER   B CA  1 
ATOM   3708 C  C   . SER   B 2 144 ? -23.379 64.526 83.617  1.00 35.35 ? 114 SER   B C   1 
ATOM   3709 O  O   . SER   B 2 144 ? -23.884 64.695 84.719  1.00 35.82 ? 114 SER   B O   1 
ATOM   3710 C  CB  . SER   B 2 144 ? -24.343 62.753 82.118  1.00 36.35 ? 114 SER   B CB  1 
ATOM   3711 O  OG  . SER   B 2 144 ? -24.878 62.084 83.244  1.00 40.69 ? 114 SER   B OG  1 
ATOM   3712 N  N   . VAL   B 2 145 ? -22.068 64.555 83.421  1.00 35.61 ? 115 VAL   B N   1 
ATOM   3713 C  CA  . VAL   B 2 145 ? -21.112 64.823 84.492  1.00 36.52 ? 115 VAL   B CA  1 
ATOM   3714 C  C   . VAL   B 2 145 ? -21.323 66.223 85.065  1.00 37.83 ? 115 VAL   B C   1 
ATOM   3715 O  O   . VAL   B 2 145 ? -21.436 66.360 86.281  1.00 38.15 ? 115 VAL   B O   1 
ATOM   3716 C  CB  . VAL   B 2 145 ? -19.647 64.559 84.038  1.00 36.46 ? 115 VAL   B CB  1 
ATOM   3717 C  CG1 . VAL   B 2 145 ? -18.628 65.272 84.914  1.00 36.85 ? 115 VAL   B CG1 1 
ATOM   3718 C  CG2 . VAL   B 2 145 ? -19.362 63.074 84.004  1.00 36.43 ? 115 VAL   B CG2 1 
ATOM   3719 N  N   . LEU   B 2 146 ? -21.401 67.247 84.208  1.00 38.44 ? 116 LEU   B N   1 
ATOM   3720 C  CA  . LEU   B 2 146 ? -21.595 68.611 84.694  1.00 40.02 ? 116 LEU   B CA  1 
ATOM   3721 C  C   . LEU   B 2 146 ? -22.941 68.808 85.419  1.00 41.60 ? 116 LEU   B C   1 
ATOM   3722 O  O   . LEU   B 2 146 ? -23.003 69.520 86.425  1.00 41.67 ? 116 LEU   B O   1 
ATOM   3723 C  CB  . LEU   B 2 146 ? -21.402 69.624 83.575  1.00 40.28 ? 116 LEU   B CB  1 
ATOM   3724 C  CG  . LEU   B 2 146 ? -20.015 69.604 82.916  1.00 42.47 ? 116 LEU   B CG  1 
ATOM   3725 C  CD1 . LEU   B 2 146 ? -19.950 70.564 81.774  1.00 43.19 ? 116 LEU   B CD1 1 
ATOM   3726 C  CD2 . LEU   B 2 146 ? -18.905 69.909 83.908  1.00 43.16 ? 116 LEU   B CD2 1 
ATOM   3727 N  N   . LYS   B 2 147 ? -23.995 68.135 84.939  1.00 41.94 ? 117 LYS   B N   1 
ATOM   3728 C  CA  . LYS   B 2 147 ? -25.329 68.210 85.512  1.00 42.97 ? 117 LYS   B CA  1 
ATOM   3729 C  C   . LYS   B 2 147 ? -25.434 67.510 86.867  1.00 43.44 ? 117 LYS   B C   1 
ATOM   3730 O  O   . LYS   B 2 147 ? -25.927 68.106 87.813  1.00 43.92 ? 117 LYS   B O   1 
ATOM   3731 C  CB  . LYS   B 2 147 ? -26.348 67.626 84.519  1.00 46.01 ? 117 LYS   B CB  1 
ATOM   3732 C  CG  . LYS   B 2 147 ? -27.780 67.530 85.015  1.00 52.73 ? 117 LYS   B CG  1 
ATOM   3733 C  CD  . LYS   B 2 147 ? -28.742 67.402 83.818  1.00 59.97 ? 117 LYS   B CD  1 
ATOM   3734 C  CE  . LYS   B 2 147 ? -30.156 67.023 84.219  1.00 65.69 ? 117 LYS   B CE  1 
ATOM   3735 N  NZ  . LYS   B 2 147 ? -31.037 66.803 83.028  1.00 68.47 ? 117 LYS   B NZ  1 
ATOM   3736 N  N   . THR   B 2 148 ? -24.990 66.254 86.963  1.00 43.15 ? 118 THR   B N   1 
ATOM   3737 C  CA  . THR   B 2 148 ? -25.136 65.481 88.187  1.00 43.49 ? 118 THR   B CA  1 
ATOM   3738 C  C   . THR   B 2 148 ? -24.046 65.699 89.222  1.00 42.78 ? 118 THR   B C   1 
ATOM   3739 O  O   . THR   B 2 148 ? -24.303 65.492 90.406  1.00 43.38 ? 118 THR   B O   1 
ATOM   3740 C  CB  . THR   B 2 148 ? -25.267 63.991 87.860  1.00 45.31 ? 118 THR   B CB  1 
ATOM   3741 O  OG1 . THR   B 2 148 ? -24.023 63.530 87.340  1.00 46.86 ? 118 THR   B OG1 1 
ATOM   3742 C  CG2 . THR   B 2 148 ? -26.379 63.713 86.860  1.00 45.73 ? 118 THR   B CG2 1 
ATOM   3743 N  N   . ARG   B 2 149 ? -22.842 66.087 88.803  1.00 41.32 ? 119 ARG   B N   1 
ATOM   3744 C  CA  . ARG   B 2 149 ? -21.744 66.249 89.749  1.00 40.18 ? 119 ARG   B CA  1 
ATOM   3745 C  C   . ARG   B 2 149 ? -21.298 67.688 89.953  1.00 38.23 ? 119 ARG   B C   1 
ATOM   3746 O  O   . ARG   B 2 149 ? -20.717 67.973 90.991  1.00 38.43 ? 119 ARG   B O   1 
ATOM   3747 C  CB  . ARG   B 2 149 ? -20.561 65.350 89.353  1.00 42.03 ? 119 ARG   B CB  1 
ATOM   3748 C  CG  . ARG   B 2 149 ? -20.919 63.866 89.474  1.00 46.90 ? 119 ARG   B CG  1 
ATOM   3749 C  CD  . ARG   B 2 149 ? -19.901 62.926 88.853  1.00 51.27 ? 119 ARG   B CD  1 
ATOM   3750 N  NE  . ARG   B 2 149 ? -18.705 62.755 89.686  1.00 55.63 ? 119 ARG   B NE  1 
ATOM   3751 C  CZ  . ARG   B 2 149 ? -17.711 61.916 89.405  1.00 59.42 ? 119 ARG   B CZ  1 
ATOM   3752 N  NH1 . ARG   B 2 149 ? -17.754 61.165 88.307  1.00 60.12 ? 119 ARG   B NH1 1 
ATOM   3753 N  NH2 . ARG   B 2 149 ? -16.657 61.836 90.207  1.00 59.48 ? 119 ARG   B NH2 1 
ATOM   3754 N  N   . PHE   B 2 150 ? -21.559 68.595 88.996  1.00 36.42 ? 120 PHE   B N   1 
ATOM   3755 C  CA  . PHE   B 2 150 ? -21.071 69.968 89.112  1.00 35.46 ? 120 PHE   B CA  1 
ATOM   3756 C  C   . PHE   B 2 150 ? -22.140 71.053 88.968  1.00 35.67 ? 120 PHE   B C   1 
ATOM   3757 O  O   . PHE   B 2 150 ? -21.805 72.151 88.521  1.00 35.68 ? 120 PHE   B O   1 
ATOM   3758 C  CB  . PHE   B 2 150 ? -19.929 70.206 88.102  1.00 34.56 ? 120 PHE   B CB  1 
ATOM   3759 C  CG  . PHE   B 2 150 ? -18.734 69.292 88.281  1.00 34.21 ? 120 PHE   B CG  1 
ATOM   3760 C  CD1 . PHE   B 2 150 ? -17.759 69.576 89.216  1.00 34.36 ? 120 PHE   B CD1 1 
ATOM   3761 C  CD2 . PHE   B 2 150 ? -18.601 68.144 87.528  1.00 34.21 ? 120 PHE   B CD2 1 
ATOM   3762 C  CE1 . PHE   B 2 150 ? -16.685 68.728 89.408  1.00 34.52 ? 120 PHE   B CE1 1 
ATOM   3763 C  CE2 . PHE   B 2 150 ? -17.535 67.292 87.732  1.00 34.87 ? 120 PHE   B CE2 1 
ATOM   3764 C  CZ  . PHE   B 2 150 ? -16.588 67.582 88.684  1.00 34.43 ? 120 PHE   B CZ  1 
ATOM   3765 N  N   . SER   B 2 151 ? -23.413 70.783 89.355  1.00 35.73 ? 121 SER   B N   1 
ATOM   3766 C  CA  . SER   B 2 151 ? -24.458 71.810 89.197  1.00 36.76 ? 121 SER   B CA  1 
ATOM   3767 C  C   . SER   B 2 151 ? -24.329 72.967 90.189  1.00 38.38 ? 121 SER   B C   1 
ATOM   3768 O  O   . SER   B 2 151 ? -24.895 74.029 89.952  1.00 38.92 ? 121 SER   B O   1 
ATOM   3769 C  CB  . SER   B 2 151 ? -25.856 71.214 89.212  1.00 37.69 ? 121 SER   B CB  1 
ATOM   3770 O  OG  . SER   B 2 151 ? -26.010 70.352 90.319  1.00 40.90 ? 121 SER   B OG  1 
ATOM   3771 N  N   . TYR   B 2 152 ? -23.530 72.796 91.258  1.00 38.67 ? 122 TYR   B N   1 
ATOM   3772 C  CA  . TYR   B 2 152 ? -23.241 73.888 92.171  1.00 39.62 ? 122 TYR   B CA  1 
ATOM   3773 C  C   . TYR   B 2 152 ? -22.474 75.020 91.434  1.00 42.03 ? 122 TYR   B C   1 
ATOM   3774 O  O   . TYR   B 2 152 ? -22.541 76.180 91.842  1.00 42.82 ? 122 TYR   B O   1 
ATOM   3775 C  CB  . TYR   B 2 152 ? -22.399 73.373 93.343  1.00 38.62 ? 122 TYR   B CB  1 
ATOM   3776 C  CG  . TYR   B 2 152 ? -21.094 72.704 92.972  1.00 38.30 ? 122 TYR   B CG  1 
ATOM   3777 C  CD1 . TYR   B 2 152 ? -19.947 73.450 92.744  1.00 38.93 ? 122 TYR   B CD1 1 
ATOM   3778 C  CD2 . TYR   B 2 152 ? -20.973 71.324 92.974  1.00 39.21 ? 122 TYR   B CD2 1 
ATOM   3779 C  CE1 . TYR   B 2 152 ? -18.729 72.843 92.467  1.00 39.54 ? 122 TYR   B CE1 1 
ATOM   3780 C  CE2 . TYR   B 2 152 ? -19.758 70.703 92.695  1.00 39.99 ? 122 TYR   B CE2 1 
ATOM   3781 C  CZ  . TYR   B 2 152 ? -18.635 71.469 92.452  1.00 40.50 ? 122 TYR   B CZ  1 
ATOM   3782 O  OH  . TYR   B 2 152 ? -17.426 70.875 92.195  1.00 41.67 ? 122 TYR   B OH  1 
ATOM   3783 N  N   . ALA   B 2 153 ? -21.710 74.670 90.372  1.00 42.50 ? 123 ALA   B N   1 
ATOM   3784 C  CA  . ALA   B 2 153 ? -20.924 75.623 89.607  1.00 43.00 ? 123 ALA   B CA  1 
ATOM   3785 C  C   . ALA   B 2 153 ? -21.587 75.953 88.265  1.00 43.54 ? 123 ALA   B C   1 
ATOM   3786 O  O   . ALA   B 2 153 ? -21.393 77.043 87.755  1.00 43.76 ? 123 ALA   B O   1 
ATOM   3787 C  CB  . ALA   B 2 153 ? -19.528 75.068 89.384  1.00 42.73 ? 123 ALA   B CB  1 
ATOM   3788 N  N   . PHE   B 2 154 ? -22.354 75.022 87.692  1.00 43.97 ? 124 PHE   B N   1 
ATOM   3789 C  CA  . PHE   B 2 154 ? -22.999 75.230 86.409  1.00 45.02 ? 124 PHE   B CA  1 
ATOM   3790 C  C   . PHE   B 2 154 ? -24.515 75.172 86.491  1.00 46.86 ? 124 PHE   B C   1 
ATOM   3791 O  O   . PHE   B 2 154 ? -25.081 74.086 86.572  1.00 47.31 ? 124 PHE   B O   1 
ATOM   3792 C  CB  . PHE   B 2 154 ? -22.493 74.203 85.386  1.00 44.27 ? 124 PHE   B CB  1 
ATOM   3793 C  CG  . PHE   B 2 154 ? -20.998 74.254 85.204  1.00 44.00 ? 124 PHE   B CG  1 
ATOM   3794 C  CD1 . PHE   B 2 154 ? -20.381 75.396 84.728  1.00 44.13 ? 124 PHE   B CD1 1 
ATOM   3795 C  CD2 . PHE   B 2 154 ? -20.207 73.161 85.517  1.00 44.22 ? 124 PHE   B CD2 1 
ATOM   3796 C  CE1 . PHE   B 2 154 ? -19.001 75.450 84.591  1.00 44.34 ? 124 PHE   B CE1 1 
ATOM   3797 C  CE2 . PHE   B 2 154 ? -18.826 73.216 85.359  1.00 44.37 ? 124 PHE   B CE2 1 
ATOM   3798 C  CZ  . PHE   B 2 154 ? -18.236 74.352 84.890  1.00 43.78 ? 124 PHE   B CZ  1 
ATOM   3799 N  N   . PRO   B 2 155 ? -25.202 76.322 86.406  1.00 47.78 ? 125 PRO   B N   1 
ATOM   3800 C  CA  . PRO   B 2 155 ? -26.679 76.290 86.436  1.00 48.18 ? 125 PRO   B CA  1 
ATOM   3801 C  C   . PRO   B 2 155 ? -27.297 75.794 85.114  1.00 48.30 ? 125 PRO   B C   1 
ATOM   3802 O  O   . PRO   B 2 155 ? -28.356 75.154 85.130  1.00 48.51 ? 125 PRO   B O   1 
ATOM   3803 C  CB  . PRO   B 2 155 ? -27.061 77.740 86.753  1.00 48.65 ? 125 PRO   B CB  1 
ATOM   3804 C  CG  . PRO   B 2 155 ? -25.925 78.556 86.240  1.00 49.09 ? 125 PRO   B CG  1 
ATOM   3805 C  CD  . PRO   B 2 155 ? -24.676 77.697 86.281  1.00 47.53 ? 125 PRO   B CD  1 
ATOM   3806 N  N   . LYS   B 2 156 ? -26.622 76.055 83.976  1.00 47.47 ? 126 LYS   B N   1 
ATOM   3807 C  CA  . LYS   B 2 156 ? -27.132 75.635 82.675  1.00 47.47 ? 126 LYS   B CA  1 
ATOM   3808 C  C   . LYS   B 2 156 ? -26.523 74.312 82.197  1.00 46.77 ? 126 LYS   B C   1 
ATOM   3809 O  O   . LYS   B 2 156 ? -25.437 73.916 82.625  1.00 47.07 ? 126 LYS   B O   1 
ATOM   3810 C  CB  . LYS   B 2 156 ? -26.902 76.725 81.618  1.00 50.03 ? 126 LYS   B CB  1 
ATOM   3811 C  CG  . LYS   B 2 156 ? -27.534 78.063 81.942  1.00 55.37 ? 126 LYS   B CG  1 
ATOM   3812 C  CD  . LYS   B 2 156 ? -26.963 79.147 81.035  1.00 61.77 ? 126 LYS   B CD  1 
ATOM   3813 C  CE  . LYS   B 2 156 ? -27.389 80.536 81.450  1.00 67.49 ? 126 LYS   B CE  1 
ATOM   3814 N  NZ  . LYS   B 2 156 ? -26.638 81.594 80.710  1.00 71.14 ? 126 LYS   B NZ  1 
ATOM   3815 N  N   . GLU   B 2 157 ? -27.226 73.638 81.292  1.00 45.52 ? 127 GLU   B N   1 
ATOM   3816 C  CA  . GLU   B 2 157 ? -26.771 72.384 80.707  1.00 44.60 ? 127 GLU   B CA  1 
ATOM   3817 C  C   . GLU   B 2 157 ? -25.567 72.640 79.752  1.00 42.15 ? 127 GLU   B C   1 
ATOM   3818 O  O   . GLU   B 2 157 ? -25.486 73.708 79.143  1.00 42.00 ? 127 GLU   B O   1 
ATOM   3819 C  CB  . GLU   B 2 157 ? -27.947 71.761 79.942  1.00 48.11 ? 127 GLU   B CB  1 
ATOM   3820 C  CG  . GLU   B 2 157 ? -27.659 70.450 79.240  1.00 56.28 ? 127 GLU   B CG  1 
ATOM   3821 C  CD  . GLU   B 2 157 ? -28.897 69.798 78.655  1.00 66.24 ? 127 GLU   B CD  1 
ATOM   3822 O  OE1 . GLU   B 2 157 ? -28.889 69.469 77.444  1.00 67.59 ? 127 GLU   B OE1 1 
ATOM   3823 O  OE2 . GLU   B 2 157 ? -29.881 69.620 79.411  1.00 69.66 ? 127 GLU   B OE2 1 
ATOM   3824 N  N   . PHE   B 2 158 ? -24.642 71.655 79.617  1.00 39.57 ? 128 PHE   B N   1 
ATOM   3825 C  CA  . PHE   B 2 158 ? -23.485 71.704 78.716  1.00 37.65 ? 128 PHE   B CA  1 
ATOM   3826 C  C   . PHE   B 2 158 ? -23.945 72.105 77.298  1.00 37.68 ? 128 PHE   B C   1 
ATOM   3827 O  O   . PHE   B 2 158 ? -24.772 71.417 76.701  1.00 38.23 ? 128 PHE   B O   1 
ATOM   3828 C  CB  . PHE   B 2 158 ? -22.798 70.331 78.691  1.00 35.83 ? 128 PHE   B CB  1 
ATOM   3829 C  CG  . PHE   B 2 158 ? -21.555 70.244 77.842  1.00 34.68 ? 128 PHE   B CG  1 
ATOM   3830 C  CD1 . PHE   B 2 158 ? -20.357 70.782 78.282  1.00 34.63 ? 128 PHE   B CD1 1 
ATOM   3831 C  CD2 . PHE   B 2 158 ? -21.571 69.585 76.626  1.00 34.40 ? 128 PHE   B CD2 1 
ATOM   3832 C  CE1 . PHE   B 2 158 ? -19.206 70.683 77.512  1.00 34.77 ? 128 PHE   B CE1 1 
ATOM   3833 C  CE2 . PHE   B 2 158 ? -20.418 69.489 75.856  1.00 34.58 ? 128 PHE   B CE2 1 
ATOM   3834 C  CZ  . PHE   B 2 158 ? -19.245 70.040 76.302  1.00 34.49 ? 128 PHE   B CZ  1 
ATOM   3835 N  N   . PRO   B 2 159 ? -23.523 73.281 76.820  1.00 36.90 ? 129 PRO   B N   1 
ATOM   3836 C  CA  . PRO   B 2 159 ? -24.054 73.782 75.542  1.00 37.15 ? 129 PRO   B CA  1 
ATOM   3837 C  C   . PRO   B 2 159 ? -23.318 73.378 74.276  1.00 37.36 ? 129 PRO   B C   1 
ATOM   3838 O  O   . PRO   B 2 159 ? -23.763 73.745 73.187  1.00 38.14 ? 129 PRO   B O   1 
ATOM   3839 C  CB  . PRO   B 2 159 ? -23.928 75.292 75.707  1.00 37.90 ? 129 PRO   B CB  1 
ATOM   3840 C  CG  . PRO   B 2 159 ? -22.677 75.453 76.532  1.00 38.08 ? 129 PRO   B CG  1 
ATOM   3841 C  CD  . PRO   B 2 159 ? -22.633 74.267 77.470  1.00 36.21 ? 129 PRO   B CD  1 
ATOM   3842 N  N   . TYR   B 2 160 ? -22.183 72.696 74.405  1.00 36.51 ? 130 TYR   B N   1 
ATOM   3843 C  CA  . TYR   B 2 160 ? -21.370 72.371 73.243  1.00 36.34 ? 130 TYR   B CA  1 
ATOM   3844 C  C   . TYR   B 2 160 ? -21.739 71.067 72.554  1.00 36.85 ? 130 TYR   B C   1 
ATOM   3845 O  O   . TYR   B 2 160 ? -22.264 70.129 73.148  1.00 37.29 ? 130 TYR   B O   1 
ATOM   3846 C  CB  . TYR   B 2 160 ? -19.878 72.405 73.606  1.00 35.73 ? 130 TYR   B CB  1 
ATOM   3847 C  CG  . TYR   B 2 160 ? -19.469 73.751 74.156  1.00 35.13 ? 130 TYR   B CG  1 
ATOM   3848 C  CD1 . TYR   B 2 160 ? -19.409 74.870 73.333  1.00 35.54 ? 130 TYR   B CD1 1 
ATOM   3849 C  CD2 . TYR   B 2 160 ? -19.238 73.928 75.513  1.00 35.16 ? 130 TYR   B CD2 1 
ATOM   3850 C  CE1 . TYR   B 2 160 ? -19.070 76.116 73.836  1.00 36.00 ? 130 TYR   B CE1 1 
ATOM   3851 C  CE2 . TYR   B 2 160 ? -18.892 75.168 76.028  1.00 35.86 ? 130 TYR   B CE2 1 
ATOM   3852 C  CZ  . TYR   B 2 160 ? -18.812 76.263 75.185  1.00 36.92 ? 130 TYR   B CZ  1 
ATOM   3853 O  OH  . TYR   B 2 160 ? -18.490 77.502 75.676  1.00 38.15 ? 130 TYR   B OH  1 
ATOM   3854 N  N   . ARG   B 2 161 ? -21.478 71.037 71.276  1.00 36.95 ? 131 ARG   B N   1 
ATOM   3855 C  CA  . ARG   B 2 161 ? -21.739 69.897 70.428  1.00 37.60 ? 131 ARG   B CA  1 
ATOM   3856 C  C   . ARG   B 2 161 ? -20.426 69.367 69.876  1.00 37.42 ? 131 ARG   B C   1 
ATOM   3857 O  O   . ARG   B 2 161 ? -19.380 70.009 70.018  1.00 37.68 ? 131 ARG   B O   1 
ATOM   3858 C  CB  . ARG   B 2 161 ? -22.732 70.288 69.326  1.00 39.91 ? 131 ARG   B CB  1 
ATOM   3859 C  CG  . ARG   B 2 161 ? -24.103 70.558 69.916  1.00 46.53 ? 131 ARG   B CG  1 
ATOM   3860 C  CD  . ARG   B 2 161 ? -25.104 71.112 68.915  1.00 53.59 ? 131 ARG   B CD  1 
ATOM   3861 N  NE  . ARG   B 2 161 ? -24.766 72.458 68.443  1.00 59.67 ? 131 ARG   B NE  1 
ATOM   3862 C  CZ  . ARG   B 2 161 ? -25.012 73.579 69.120  1.00 63.47 ? 131 ARG   B CZ  1 
ATOM   3863 N  NH1 . ARG   B 2 161 ? -25.554 73.528 70.332  1.00 62.89 ? 131 ARG   B NH1 1 
ATOM   3864 N  NH2 . ARG   B 2 161 ? -24.690 74.758 68.601  1.00 64.42 ? 131 ARG   B NH2 1 
ATOM   3865 N  N   . MET   B 2 162 ? -20.466 68.191 69.244  1.00 36.69 ? 132 MET   B N   1 
ATOM   3866 C  CA  . MET   B 2 162 ? -19.271 67.582 68.707  1.00 36.05 ? 132 MET   B CA  1 
ATOM   3867 C  C   . MET   B 2 162 ? -18.474 68.471 67.766  1.00 36.20 ? 132 MET   B C   1 
ATOM   3868 O  O   . MET   B 2 162 ? -17.240 68.433 67.843  1.00 36.78 ? 132 MET   B O   1 
ATOM   3869 C  CB  . MET   B 2 162 ? -19.552 66.225 68.054  1.00 35.57 ? 132 MET   B CB  1 
ATOM   3870 C  CG  . MET   B 2 162 ? -18.332 65.338 68.062  1.00 35.42 ? 132 MET   B CG  1 
ATOM   3871 S  SD  . MET   B 2 162 ? -17.714 65.024 69.744  1.00 35.08 ? 132 MET   B SD  1 
ATOM   3872 C  CE  . MET   B 2 162 ? -16.255 64.238 69.360  1.00 32.96 ? 132 MET   B CE  1 
ATOM   3873 N  N   . ASN   B 2 163 ? -19.138 69.307 66.930  1.00 35.39 ? 133 ASN   B N   1 
ATOM   3874 C  CA  . ASN   B 2 163 ? -18.376 70.185 66.036  1.00 36.04 ? 133 ASN   B CA  1 
ATOM   3875 C  C   . ASN   B 2 163 ? -17.445 71.137 66.810  1.00 34.47 ? 133 ASN   B C   1 
ATOM   3876 O  O   . ASN   B 2 163 ? -16.332 71.386 66.358  1.00 34.10 ? 133 ASN   B O   1 
ATOM   3877 C  CB  . ASN   B 2 163 ? -19.271 70.941 65.029  1.00 39.05 ? 133 ASN   B CB  1 
ATOM   3878 C  CG  . ASN   B 2 163 ? -20.352 71.781 65.663  1.00 46.25 ? 133 ASN   B CG  1 
ATOM   3879 O  OD1 . ASN   B 2 163 ? -21.268 71.273 66.333  1.00 48.82 ? 133 ASN   B OD1 1 
ATOM   3880 N  ND2 . ASN   B 2 163 ? -20.282 73.085 65.453  1.00 48.20 ? 133 ASN   B ND2 1 
ATOM   3881 N  N   . HIS   B 2 164 ? -17.863 71.563 68.021  1.00 33.35 ? 134 HIS   B N   1 
ATOM   3882 C  CA  . HIS   B 2 164 ? -17.092 72.453 68.890  1.00 33.03 ? 134 HIS   B CA  1 
ATOM   3883 C  C   . HIS   B 2 164 ? -15.901 71.740 69.461  1.00 32.47 ? 134 HIS   B C   1 
ATOM   3884 O  O   . HIS   B 2 164 ? -14.823 72.318 69.506  1.00 32.73 ? 134 HIS   B O   1 
ATOM   3885 C  CB  . HIS   B 2 164 ? -17.959 73.001 70.040  1.00 34.15 ? 134 HIS   B CB  1 
ATOM   3886 C  CG  . HIS   B 2 164 ? -19.139 73.774 69.567  1.00 36.28 ? 134 HIS   B CG  1 
ATOM   3887 N  ND1 . HIS   B 2 164 ? -20.411 73.426 69.934  1.00 38.20 ? 134 HIS   B ND1 1 
ATOM   3888 C  CD2 . HIS   B 2 164 ? -19.199 74.818 68.710  1.00 37.17 ? 134 HIS   B CD2 1 
ATOM   3889 C  CE1 . HIS   B 2 164 ? -21.206 74.293 69.336  1.00 38.52 ? 134 HIS   B CE1 1 
ATOM   3890 N  NE2 . HIS   B 2 164 ? -20.517 75.141 68.580  1.00 38.18 ? 134 HIS   B NE2 1 
ATOM   3891 N  N   . ILE   B 2 165 ? -16.090 70.488 69.901  1.00 31.95 ? 135 ILE   B N   1 
ATOM   3892 C  CA  . ILE   B 2 165 ? -15.021 69.631 70.420  1.00 31.72 ? 135 ILE   B CA  1 
ATOM   3893 C  C   . ILE   B 2 165 ? -13.996 69.393 69.301  1.00 32.12 ? 135 ILE   B C   1 
ATOM   3894 O  O   . ILE   B 2 165 ? -12.799 69.467 69.554  1.00 32.51 ? 135 ILE   B O   1 
ATOM   3895 C  CB  . ILE   B 2 165 ? -15.613 68.290 70.899  1.00 30.90 ? 135 ILE   B CB  1 
ATOM   3896 C  CG1 . ILE   B 2 165 ? -16.532 68.496 72.137  1.00 31.18 ? 135 ILE   B CG1 1 
ATOM   3897 C  CG2 . ILE   B 2 165 ? -14.517 67.233 71.108  1.00 30.81 ? 135 ILE   B CG2 1 
ATOM   3898 C  CD1 . ILE   B 2 165 ? -15.896 68.399 73.506  1.00 31.55 ? 135 ILE   B CD1 1 
ATOM   3899 N  N   . LEU   B 2 166 ? -14.466 69.105 68.079  1.00 31.87 ? 136 LEU   B N   1 
ATOM   3900 C  CA  . LEU   B 2 166 ? -13.584 68.858 66.941  1.00 32.02 ? 136 LEU   B CA  1 
ATOM   3901 C  C   . LEU   B 2 166 ? -12.801 70.102 66.585  1.00 32.66 ? 136 LEU   B C   1 
ATOM   3902 O  O   . LEU   B 2 166 ? -11.619 69.993 66.298  1.00 33.19 ? 136 LEU   B O   1 
ATOM   3903 C  CB  . LEU   B 2 166 ? -14.358 68.327 65.722  1.00 31.87 ? 136 LEU   B CB  1 
ATOM   3904 C  CG  . LEU   B 2 166 ? -14.954 66.926 65.873  1.00 33.42 ? 136 LEU   B CG  1 
ATOM   3905 C  CD1 . LEU   B 2 166 ? -15.722 66.512 64.619  1.00 33.76 ? 136 LEU   B CD1 1 
ATOM   3906 C  CD2 . LEU   B 2 166 ? -13.888 65.890 66.192  1.00 33.31 ? 136 LEU   B CD2 1 
ATOM   3907 N  N   . GLU   B 2 167 ? -13.433 71.288 66.668  1.00 32.67 ? 137 GLU   B N   1 
ATOM   3908 C  CA  . GLU   B 2 167 ? -12.785 72.573 66.405  1.00 33.01 ? 137 GLU   B CA  1 
ATOM   3909 C  C   . GLU   B 2 167 ? -11.708 72.779 67.457  1.00 31.16 ? 137 GLU   B C   1 
ATOM   3910 O  O   . GLU   B 2 167 ? -10.568 73.060 67.121  1.00 31.24 ? 137 GLU   B O   1 
ATOM   3911 C  CB  . GLU   B 2 167 ? -13.809 73.756 66.463  1.00 37.43 ? 137 GLU   B CB  1 
ATOM   3912 C  CG  . GLU   B 2 167 ? -14.719 73.901 65.249  1.00 47.34 ? 137 GLU   B CG  1 
ATOM   3913 C  CD  . GLU   B 2 167 ? -16.005 74.699 65.437  1.00 57.35 ? 137 GLU   B CD  1 
ATOM   3914 O  OE1 . GLU   B 2 167 ? -16.913 74.567 64.581  1.00 58.22 ? 137 GLU   B OE1 1 
ATOM   3915 O  OE2 . GLU   B 2 167 ? -16.113 75.446 66.440  1.00 60.60 ? 137 GLU   B OE2 1 
ATOM   3916 N  N   . CYS   B 2 168 ? -12.074 72.604 68.728  1.00 29.76 ? 138 CYS   B N   1 
ATOM   3917 C  CA  . CYS   B 2 168 ? -11.187 72.777 69.874  1.00 29.12 ? 138 CYS   B CA  1 
ATOM   3918 C  C   . CYS   B 2 168 ? -9.994  71.842 69.823  1.00 29.31 ? 138 CYS   B C   1 
ATOM   3919 O  O   . CYS   B 2 168 ? -8.898  72.244 70.190  1.00 29.80 ? 138 CYS   B O   1 
ATOM   3920 C  CB  . CYS   B 2 168 ? -11.956 72.605 71.178  1.00 28.28 ? 138 CYS   B CB  1 
ATOM   3921 S  SG  . CYS   B 2 168 ? -11.020 73.103 72.635  1.00 29.89 ? 138 CYS   B SG  1 
ATOM   3922 N  N   . GLU   B 2 169 ? -10.198 70.610 69.344  1.00 28.63 ? 139 GLU   B N   1 
ATOM   3923 C  CA  . GLU   B 2 169 ? -9.150  69.601 69.226  1.00 28.85 ? 139 GLU   B CA  1 
ATOM   3924 C  C   . GLU   B 2 169 ? -8.047  70.078 68.316  1.00 30.12 ? 139 GLU   B C   1 
ATOM   3925 O  O   . GLU   B 2 169 ? -6.876  69.960 68.666  1.00 30.31 ? 139 GLU   B O   1 
ATOM   3926 C  CB  . GLU   B 2 169 ? -9.740  68.281 68.708  1.00 29.15 ? 139 GLU   B CB  1 
ATOM   3927 C  CG  . GLU   B 2 169 ? -8.773  67.125 68.830  1.00 30.35 ? 139 GLU   B CG  1 
ATOM   3928 C  CD  . GLU   B 2 169 ? -9.267  65.865 68.160  1.00 33.56 ? 139 GLU   B CD  1 
ATOM   3929 O  OE1 . GLU   B 2 169 ? -10.069 65.972 67.202  1.00 34.10 ? 139 GLU   B OE1 1 
ATOM   3930 O  OE2 . GLU   B 2 169 ? -8.843  64.767 68.586  1.00 33.64 ? 139 GLU   B OE2 1 
ATOM   3931 N  N   . PHE   B 2 170 ? -8.415  70.712 67.186  1.00 30.81 ? 140 PHE   B N   1 
ATOM   3932 C  CA  . PHE   B 2 170 ? -7.434  71.273 66.276  1.00 32.38 ? 140 PHE   B CA  1 
ATOM   3933 C  C   . PHE   B 2 170 ? -6.608  72.357 66.965  1.00 33.06 ? 140 PHE   B C   1 
ATOM   3934 O  O   . PHE   B 2 170 ? -5.388  72.314 66.895  1.00 33.64 ? 140 PHE   B O   1 
ATOM   3935 C  CB  . PHE   B 2 170 ? -8.105  71.786 64.990  1.00 33.11 ? 140 PHE   B CB  1 
ATOM   3936 C  CG  . PHE   B 2 170 ? -7.931  70.837 63.829  1.00 35.08 ? 140 PHE   B CG  1 
ATOM   3937 C  CD1 . PHE   B 2 170 ? -7.933  69.462 64.025  1.00 36.54 ? 140 PHE   B CD1 1 
ATOM   3938 C  CD2 . PHE   B 2 170 ? -7.720  71.315 62.550  1.00 36.31 ? 140 PHE   B CD2 1 
ATOM   3939 C  CE1 . PHE   B 2 170 ? -7.740  68.588 62.962  1.00 37.35 ? 140 PHE   B CE1 1 
ATOM   3940 C  CE2 . PHE   B 2 170 ? -7.528  70.439 61.490  1.00 37.42 ? 140 PHE   B CE2 1 
ATOM   3941 C  CZ  . PHE   B 2 170 ? -7.545  69.084 61.701  1.00 37.37 ? 140 PHE   B CZ  1 
ATOM   3942 N  N   . TYR   B 2 171 ? -7.264  73.254 67.710  1.00 32.74 ? 141 TYR   B N   1 
ATOM   3943 C  CA  . TYR   B 2 171 ? -6.597  74.318 68.450  1.00 33.21 ? 141 TYR   B CA  1 
ATOM   3944 C  C   . TYR   B 2 171 ? -5.678  73.773 69.550  1.00 33.06 ? 141 TYR   B C   1 
ATOM   3945 O  O   . TYR   B 2 171 ? -4.562  74.238 69.699  1.00 34.05 ? 141 TYR   B O   1 
ATOM   3946 C  CB  . TYR   B 2 171 ? -7.632  75.281 69.056  1.00 33.75 ? 141 TYR   B CB  1 
ATOM   3947 C  CG  . TYR   B 2 171 ? -8.167  76.278 68.051  1.00 35.59 ? 141 TYR   B CG  1 
ATOM   3948 C  CD1 . TYR   B 2 171 ? -7.394  77.348 67.623  1.00 36.92 ? 141 TYR   B CD1 1 
ATOM   3949 C  CD2 . TYR   B 2 171 ? -9.450  76.158 67.540  1.00 36.84 ? 141 TYR   B CD2 1 
ATOM   3950 C  CE1 . TYR   B 2 171 ? -7.875  78.260 66.691  1.00 38.19 ? 141 TYR   B CE1 1 
ATOM   3951 C  CE2 . TYR   B 2 171 ? -9.941  77.061 66.604  1.00 38.04 ? 141 TYR   B CE2 1 
ATOM   3952 C  CZ  . TYR   B 2 171 ? -9.158  78.124 66.197  1.00 39.34 ? 141 TYR   B CZ  1 
ATOM   3953 O  OH  . TYR   B 2 171 ? -9.657  79.038 65.298  1.00 41.25 ? 141 TYR   B OH  1 
ATOM   3954 N  N   . LEU   B 2 172 ? -6.146  72.806 70.316  1.00 31.34 ? 142 LEU   B N   1 
ATOM   3955 C  CA  . LEU   B 2 172 ? -5.378  72.215 71.393  1.00 30.71 ? 142 LEU   B CA  1 
ATOM   3956 C  C   . LEU   B 2 172 ? -4.136  71.512 70.843  1.00 30.97 ? 142 LEU   B C   1 
ATOM   3957 O  O   . LEU   B 2 172 ? -3.048  71.642 71.409  1.00 30.33 ? 142 LEU   B O   1 
ATOM   3958 C  CB  . LEU   B 2 172 ? -6.273  71.223 72.158  1.00 29.81 ? 142 LEU   B CB  1 
ATOM   3959 C  CG  . LEU   B 2 172 ? -5.605  70.442 73.260  1.00 29.88 ? 142 LEU   B CG  1 
ATOM   3960 C  CD1 . LEU   B 2 172 ? -5.089  71.373 74.342  1.00 29.28 ? 142 LEU   B CD1 1 
ATOM   3961 C  CD2 . LEU   B 2 172 ? -6.565  69.381 73.827  1.00 29.91 ? 142 LEU   B CD2 1 
ATOM   3962 N  N   . LEU   B 2 173 ? -4.291  70.800 69.723  1.00 31.87 ? 143 LEU   B N   1 
ATOM   3963 C  CA  . LEU   B 2 173 ? -3.171  70.082 69.126  1.00 33.21 ? 143 LEU   B CA  1 
ATOM   3964 C  C   . LEU   B 2 173 ? -2.074  71.011 68.659  1.00 33.55 ? 143 LEU   B C   1 
ATOM   3965 O  O   . LEU   B 2 173 ? -0.920  70.788 69.000  1.00 34.06 ? 143 LEU   B O   1 
ATOM   3966 C  CB  . LEU   B 2 173 ? -3.647  69.174 67.990  1.00 34.07 ? 143 LEU   B CB  1 
ATOM   3967 C  CG  . LEU   B 2 173 ? -2.600  68.296 67.323  1.00 36.06 ? 143 LEU   B CG  1 
ATOM   3968 C  CD1 . LEU   B 2 173 ? -1.915  67.378 68.331  1.00 36.25 ? 143 LEU   B CD1 1 
ATOM   3969 C  CD2 . LEU   B 2 173 ? -3.253  67.432 66.252  1.00 37.42 ? 143 LEU   B CD2 1 
ATOM   3970 N  N   . GLU   B 2 174 ? -2.421  72.080 67.948  1.00 33.82 ? 144 GLU   B N   1 
ATOM   3971 C  CA  . GLU   B 2 174 ? -1.421  73.022 67.455  1.00 34.44 ? 144 GLU   B CA  1 
ATOM   3972 C  C   . GLU   B 2 174 ? -0.816  73.871 68.541  1.00 34.29 ? 144 GLU   B C   1 
ATOM   3973 O  O   . GLU   B 2 174 ? 0.385   74.150 68.505  1.00 34.36 ? 144 GLU   B O   1 
ATOM   3974 C  CB  . GLU   B 2 174 ? -1.963  73.893 66.310  1.00 36.91 ? 144 GLU   B CB  1 
ATOM   3975 C  CG  . GLU   B 2 174 ? -3.189  74.680 66.688  1.00 44.20 ? 144 GLU   B CG  1 
ATOM   3976 C  CD  . GLU   B 2 174 ? -3.744  75.547 65.578  1.00 52.61 ? 144 GLU   B CD  1 
ATOM   3977 O  OE1 . GLU   B 2 174 ? -4.530  75.021 64.753  1.00 51.60 ? 144 GLU   B OE1 1 
ATOM   3978 O  OE2 . GLU   B 2 174 ? -3.397  76.754 65.542  1.00 55.99 ? 144 GLU   B OE2 1 
ATOM   3979 N  N   . LEU   B 2 175 ? -1.620  74.254 69.527  1.00 34.29 ? 145 LEU   B N   1 
ATOM   3980 C  CA  . LEU   B 2 175 ? -1.125  75.091 70.601  1.00 34.90 ? 145 LEU   B CA  1 
ATOM   3981 C  C   . LEU   B 2 175 ? -0.276  74.303 71.621  1.00 34.96 ? 145 LEU   B C   1 
ATOM   3982 O  O   . LEU   B 2 175 ? 0.441   74.918 72.396  1.00 36.38 ? 145 LEU   B O   1 
ATOM   3983 C  CB  . LEU   B 2 175 ? -2.250  75.908 71.208  1.00 36.09 ? 145 LEU   B CB  1 
ATOM   3984 C  CG  . LEU   B 2 175 ? -2.894  76.887 70.143  1.00 38.67 ? 145 LEU   B CG  1 
ATOM   3985 C  CD1 . LEU   B 2 175 ? -4.054  77.663 70.718  1.00 39.77 ? 145 LEU   B CD1 1 
ATOM   3986 C  CD2 . LEU   B 2 175 ? -1.884  77.860 69.570  1.00 38.72 ? 145 LEU   B CD2 1 
ATOM   3987 N  N   . MET   B 2 176 ? -0.241  72.961 71.540  1.00 33.13 ? 146 MET   B N   1 
ATOM   3988 C  CA  . MET   B 2 176 ? 0.707   72.157 72.318  1.00 31.57 ? 146 MET   B CA  1 
ATOM   3989 C  C   . MET   B 2 176 ? 1.931   71.771 71.461  1.00 29.85 ? 146 MET   B C   1 
ATOM   3990 O  O   . MET   B 2 176 ? 2.742   70.961 71.897  1.00 29.18 ? 146 MET   B O   1 
ATOM   3991 C  CB  . MET   B 2 176 ? 0.058   70.879 72.859  1.00 31.63 ? 146 MET   B CB  1 
ATOM   3992 C  CG  . MET   B 2 176 ? -1.001  71.146 73.865  1.00 33.62 ? 146 MET   B CG  1 
ATOM   3993 S  SD  . MET   B 2 176 ? -1.476  69.642 74.727  1.00 36.54 ? 146 MET   B SD  1 
ATOM   3994 C  CE  . MET   B 2 176 ? -2.196  68.683 73.419  1.00 33.09 ? 146 MET   B CE  1 
ATOM   3995 N  N   . ASP   B 2 177 ? 2.068   72.346 70.260  1.00 29.49 ? 147 ASP   B N   1 
ATOM   3996 C  CA  . ASP   B 2 177 ? 3.145   72.068 69.330  1.00 29.54 ? 147 ASP   B CA  1 
ATOM   3997 C  C   . ASP   B 2 177 ? 3.151   70.565 68.962  1.00 29.40 ? 147 ASP   B C   1 
ATOM   3998 O  O   . ASP   B 2 177 ? 4.215   69.988 68.740  1.00 29.55 ? 147 ASP   B O   1 
ATOM   3999 C  CB  . ASP   B 2 177 ? 4.486   72.564 69.899  1.00 30.95 ? 147 ASP   B CB  1 
ATOM   4000 C  CG  . ASP   B 2 177 ? 5.613   72.575 68.891  1.00 38.63 ? 147 ASP   B CG  1 
ATOM   4001 O  OD1 . ASP   B 2 177 ? 5.319   72.631 67.668  1.00 39.83 ? 147 ASP   B OD1 1 
ATOM   4002 O  OD2 . ASP   B 2 177 ? 6.796   72.497 69.318  1.00 42.15 ? 147 ASP   B OD2 1 
ATOM   4003 N  N   . CYS   B 2 178 ? 1.949   69.935 68.932  1.00 28.81 ? 148 CYS   B N   1 
ATOM   4004 C  CA  . CYS   B 2 178 ? 1.758   68.525 68.606  1.00 28.95 ? 148 CYS   B CA  1 
ATOM   4005 C  C   . CYS   B 2 178 ? 2.469   67.575 69.551  1.00 28.74 ? 148 CYS   B C   1 
ATOM   4006 O  O   . CYS   B 2 178 ? 2.731   66.450 69.160  1.00 29.76 ? 148 CYS   B O   1 
ATOM   4007 C  CB  . CYS   B 2 178 ? 2.133   68.246 67.154  1.00 29.64 ? 148 CYS   B CB  1 
ATOM   4008 S  SG  . CYS   B 2 178 ? 1.029   69.023 65.956  1.00 33.21 ? 148 CYS   B SG  1 
ATOM   4009 N  N   . CYS   B 2 179 ? 2.762   68.005 70.779  1.00 27.52 ? 149 CYS   B N   1 
ATOM   4010 C  CA  . CYS   B 2 179 ? 3.420   67.196 71.800  1.00 26.92 ? 149 CYS   B CA  1 
ATOM   4011 C  C   . CYS   B 2 179 ? 2.334   66.399 72.483  1.00 27.37 ? 149 CYS   B C   1 
ATOM   4012 O  O   . CYS   B 2 179 ? 1.535   66.975 73.235  1.00 27.59 ? 149 CYS   B O   1 
ATOM   4013 C  CB  . CYS   B 2 179 ? 4.157   68.094 72.791  1.00 26.75 ? 149 CYS   B CB  1 
ATOM   4014 S  SG  . CYS   B 2 179 ? 5.530   69.033 72.061  1.00 29.97 ? 149 CYS   B SG  1 
ATOM   4015 N  N   . LEU   B 2 180 ? 2.270   65.074 72.215  1.00 26.82 ? 150 LEU   B N   1 
ATOM   4016 C  CA  . LEU   B 2 180 ? 1.207   64.242 72.773  1.00 26.51 ? 150 LEU   B CA  1 
ATOM   4017 C  C   . LEU   B 2 180 ? 1.673   63.239 73.806  1.00 26.25 ? 150 LEU   B C   1 
ATOM   4018 O  O   . LEU   B 2 180 ? 0.891   62.870 74.685  1.00 26.23 ? 150 LEU   B O   1 
ATOM   4019 C  CB  . LEU   B 2 180 ? 0.433   63.548 71.654  1.00 26.61 ? 150 LEU   B CB  1 
ATOM   4020 C  CG  . LEU   B 2 180 ? -0.251  64.518 70.677  1.00 27.93 ? 150 LEU   B CG  1 
ATOM   4021 C  CD1 . LEU   B 2 180 ? -0.703  63.812 69.427  1.00 27.49 ? 150 LEU   B CD1 1 
ATOM   4022 C  CD2 . LEU   B 2 180 ? -1.408  65.235 71.363  1.00 28.72 ? 150 LEU   B CD2 1 
ATOM   4023 N  N   . ILE   B 2 181 ? 2.930   62.806 73.720  1.00 25.95 ? 151 ILE   B N   1 
ATOM   4024 C  CA  . ILE   B 2 181 ? 3.455   61.843 74.685  1.00 26.47 ? 151 ILE   B CA  1 
ATOM   4025 C  C   . ILE   B 2 181 ? 3.783   62.547 76.001  1.00 26.70 ? 151 ILE   B C   1 
ATOM   4026 O  O   . ILE   B 2 181 ? 4.646   63.429 76.044  1.00 27.10 ? 151 ILE   B O   1 
ATOM   4027 C  CB  . ILE   B 2 181 ? 4.645   61.033 74.123  1.00 27.17 ? 151 ILE   B CB  1 
ATOM   4028 C  CG1 . ILE   B 2 181 ? 4.249   60.275 72.844  1.00 28.40 ? 151 ILE   B CG1 1 
ATOM   4029 C  CG2 . ILE   B 2 181 ? 5.224   60.075 75.194  1.00 26.97 ? 151 ILE   B CG2 1 
ATOM   4030 C  CD1 . ILE   B 2 181 ? 3.120   59.276 73.072  1.00 30.40 ? 151 ILE   B CD1 1 
ATOM   4031 N  N   . VAL   B 2 182 ? 3.028   62.211 77.048  1.00 25.92 ? 152 VAL   B N   1 
ATOM   4032 C  CA  . VAL   B 2 182 ? 3.201   62.770 78.377  1.00 25.67 ? 152 VAL   B CA  1 
ATOM   4033 C  C   . VAL   B 2 182 ? 3.693   61.650 79.334  1.00 25.13 ? 152 VAL   B C   1 
ATOM   4034 O  O   . VAL   B 2 182 ? 3.228   60.519 79.253  1.00 25.37 ? 152 VAL   B O   1 
ATOM   4035 C  CB  . VAL   B 2 182 ? 1.858   63.389 78.880  1.00 26.01 ? 152 VAL   B CB  1 
ATOM   4036 C  CG1 . VAL   B 2 182 ? 2.000   63.968 80.290  1.00 25.76 ? 152 VAL   B CG1 1 
ATOM   4037 C  CG2 . VAL   B 2 182 ? 1.330   64.438 77.897  1.00 26.18 ? 152 VAL   B CG2 1 
ATOM   4038 N  N   . TYR   B 2 183 ? 4.633   61.981 80.210  1.00 24.51 ? 153 TYR   B N   1 
ATOM   4039 C  CA  . TYR   B 2 183 ? 5.201   61.116 81.235  1.00 24.99 ? 153 TYR   B CA  1 
ATOM   4040 C  C   . TYR   B 2 183 ? 4.554   61.459 82.574  1.00 25.18 ? 153 TYR   B C   1 
ATOM   4041 O  O   . TYR   B 2 183 ? 4.377   62.627 82.877  1.00 25.39 ? 153 TYR   B O   1 
ATOM   4042 C  CB  . TYR   B 2 183 ? 6.716   61.329 81.313  1.00 25.04 ? 153 TYR   B CB  1 
ATOM   4043 C  CG  . TYR   B 2 183 ? 7.400   60.835 80.062  1.00 26.43 ? 153 TYR   B CG  1 
ATOM   4044 C  CD1 . TYR   B 2 183 ? 7.435   61.614 78.914  1.00 27.05 ? 153 TYR   B CD1 1 
ATOM   4045 C  CD2 . TYR   B 2 183 ? 7.975   59.568 80.011  1.00 27.32 ? 153 TYR   B CD2 1 
ATOM   4046 C  CE1 . TYR   B 2 183 ? 8.014   61.149 77.748  1.00 28.14 ? 153 TYR   B CE1 1 
ATOM   4047 C  CE2 . TYR   B 2 183 ? 8.598   59.110 78.855  1.00 28.50 ? 153 TYR   B CE2 1 
ATOM   4048 C  CZ  . TYR   B 2 183 ? 8.595   59.899 77.717  1.00 29.32 ? 153 TYR   B CZ  1 
ATOM   4049 O  OH  . TYR   B 2 183 ? 9.164   59.475 76.540  1.00 30.77 ? 153 TYR   B OH  1 
ATOM   4050 N  N   . HIS   B 2 184 ? 4.159   60.458 83.351  1.00 24.81 ? 154 HIS   B N   1 
ATOM   4051 C  CA  . HIS   B 2 184 ? 3.489   60.690 84.639  1.00 24.67 ? 154 HIS   B CA  1 
ATOM   4052 C  C   . HIS   B 2 184 ? 4.281   60.039 85.785  1.00 24.91 ? 154 HIS   B C   1 
ATOM   4053 O  O   . HIS   B 2 184 ? 5.117   59.168 85.532  1.00 25.44 ? 154 HIS   B O   1 
ATOM   4054 C  CB  . HIS   B 2 184 ? 2.030   60.159 84.589  1.00 24.57 ? 154 HIS   B CB  1 
ATOM   4055 C  CG  . HIS   B 2 184 ? 1.204   60.751 83.484  1.00 25.78 ? 154 HIS   B CG  1 
ATOM   4056 N  ND1 . HIS   B 2 184 ? 0.719   62.047 83.557  1.00 27.22 ? 154 HIS   B ND1 1 
ATOM   4057 C  CD2 . HIS   B 2 184 ? 0.810   60.205 82.311  1.00 26.45 ? 154 HIS   B CD2 1 
ATOM   4058 C  CE1 . HIS   B 2 184 ? 0.026   62.237 82.450  1.00 27.42 ? 154 HIS   B CE1 1 
ATOM   4059 N  NE2 . HIS   B 2 184 ? 0.047   61.155 81.670  1.00 27.66 ? 154 HIS   B NE2 1 
ATOM   4060 N  N   . PRO   B 2 185 ? 4.047   60.437 87.052  1.00 24.29 ? 155 PRO   B N   1 
ATOM   4061 C  CA  . PRO   B 2 185 ? 4.824   59.854 88.156  1.00 24.91 ? 155 PRO   B CA  1 
ATOM   4062 C  C   . PRO   B 2 185 ? 4.442   58.433 88.538  1.00 26.18 ? 155 PRO   B C   1 
ATOM   4063 O  O   . PRO   B 2 185 ? 5.155   57.830 89.327  1.00 26.51 ? 155 PRO   B O   1 
ATOM   4064 C  CB  . PRO   B 2 185 ? 4.561   60.825 89.340  1.00 24.58 ? 155 PRO   B CB  1 
ATOM   4065 C  CG  . PRO   B 2 185 ? 3.907   62.030 88.744  1.00 24.17 ? 155 PRO   B CG  1 
ATOM   4066 C  CD  . PRO   B 2 185 ? 3.153   61.499 87.546  1.00 23.03 ? 155 PRO   B CD  1 
ATOM   4067 N  N   . TYR   B 2 186 ? 3.359   57.884 87.985  1.00 26.69 ? 156 TYR   B N   1 
ATOM   4068 C  CA  . TYR   B 2 186 ? 2.881   56.557 88.361  1.00 27.75 ? 156 TYR   B CA  1 
ATOM   4069 C  C   . TYR   B 2 186 ? 3.848   55.410 88.091  1.00 29.27 ? 156 TYR   B C   1 
ATOM   4070 O  O   . TYR   B 2 186 ? 3.993   54.550 88.956  1.00 29.48 ? 156 TYR   B O   1 
ATOM   4071 C  CB  . TYR   B 2 186 ? 1.540   56.263 87.695  1.00 27.86 ? 156 TYR   B CB  1 
ATOM   4072 C  CG  . TYR   B 2 186 ? 0.480   57.286 88.015  1.00 28.19 ? 156 TYR   B CG  1 
ATOM   4073 C  CD1 . TYR   B 2 186 ? -0.189  57.267 89.231  1.00 28.95 ? 156 TYR   B CD1 1 
ATOM   4074 C  CD2 . TYR   B 2 186 ? 0.123   58.257 87.090  1.00 28.42 ? 156 TYR   B CD2 1 
ATOM   4075 C  CE1 . TYR   B 2 186 ? -1.197  58.185 89.513  1.00 29.97 ? 156 TYR   B CE1 1 
ATOM   4076 C  CE2 . TYR   B 2 186 ? -0.847  59.206 87.376  1.00 29.06 ? 156 TYR   B CE2 1 
ATOM   4077 C  CZ  . TYR   B 2 186 ? -1.515  59.163 88.582  1.00 30.24 ? 156 TYR   B CZ  1 
ATOM   4078 O  OH  . TYR   B 2 186 ? -2.469  60.116 88.854  1.00 31.39 ? 156 TYR   B OH  1 
ATOM   4079 N  N   . ARG   B 2 187 ? 4.450   55.352 86.884  1.00 29.79 ? 157 ARG   B N   1 
ATOM   4080 C  CA  . ARG   B 2 187 ? 5.412   54.322 86.516  1.00 30.65 ? 157 ARG   B CA  1 
ATOM   4081 C  C   . ARG   B 2 187 ? 6.661   54.414 87.406  1.00 30.42 ? 157 ARG   B C   1 
ATOM   4082 O  O   . ARG   B 2 187 ? 6.965   53.427 88.092  1.00 30.77 ? 157 ARG   B O   1 
ATOM   4083 C  CB  . ARG   B 2 187 ? 5.731   54.380 85.010  1.00 33.99 ? 157 ARG   B CB  1 
ATOM   4084 C  CG  . ARG   B 2 187 ? 6.980   53.622 84.573  1.00 40.87 ? 157 ARG   B CG  1 
ATOM   4085 C  CD  . ARG   B 2 187 ? 7.075   53.395 83.046  1.00 48.66 ? 157 ARG   B CD  1 
ATOM   4086 N  NE  . ARG   B 2 187 ? 6.657   54.549 82.237  1.00 55.37 ? 157 ARG   B NE  1 
ATOM   4087 C  CZ  . ARG   B 2 187 ? 7.450   55.562 81.897  1.00 58.32 ? 157 ARG   B CZ  1 
ATOM   4088 N  NH1 . ARG   B 2 187 ? 8.719   55.580 82.285  1.00 58.94 ? 157 ARG   B NH1 1 
ATOM   4089 N  NH2 . ARG   B 2 187 ? 6.979   56.565 81.177  1.00 58.06 ? 157 ARG   B NH2 1 
ATOM   4090 N  N   . PRO   B 2 188 ? 7.361   55.576 87.512  1.00 29.98 ? 158 PRO   B N   1 
ATOM   4091 C  CA  . PRO   B 2 188 ? 8.516   55.635 88.436  1.00 29.75 ? 158 PRO   B CA  1 
ATOM   4092 C  C   . PRO   B 2 188 ? 8.104   55.319 89.866  1.00 30.39 ? 158 PRO   B C   1 
ATOM   4093 O  O   . PRO   B 2 188 ? 8.840   54.613 90.547  1.00 30.57 ? 158 PRO   B O   1 
ATOM   4094 C  CB  . PRO   B 2 188 ? 9.044   57.066 88.304  1.00 30.01 ? 158 PRO   B CB  1 
ATOM   4095 C  CG  . PRO   B 2 188 ? 8.034   57.807 87.535  1.00 30.46 ? 158 PRO   B CG  1 
ATOM   4096 C  CD  . PRO   B 2 188 ? 7.196   56.841 86.770  1.00 28.90 ? 158 PRO   B CD  1 
ATOM   4097 N  N   . LEU   B 2 189 ? 6.893   55.730 90.292  1.00 30.77 ? 159 LEU   B N   1 
ATOM   4098 C  CA  . LEU   B 2 189 ? 6.425   55.403 91.646  1.00 31.99 ? 159 LEU   B CA  1 
ATOM   4099 C  C   . LEU   B 2 189 ? 6.351   53.894 91.876  1.00 33.27 ? 159 LEU   B C   1 
ATOM   4100 O  O   . LEU   B 2 189 ? 6.816   53.420 92.914  1.00 33.39 ? 159 LEU   B O   1 
ATOM   4101 C  CB  . LEU   B 2 189 ? 5.087   56.088 91.995  1.00 31.87 ? 159 LEU   B CB  1 
ATOM   4102 C  CG  . LEU   B 2 189 ? 4.447   55.661 93.313  1.00 33.09 ? 159 LEU   B CG  1 
ATOM   4103 C  CD1 . LEU   B 2 189 ? 5.272   56.138 94.508  1.00 33.34 ? 159 LEU   B CD1 1 
ATOM   4104 C  CD2 . LEU   B 2 189 ? 3.026   56.116 93.387  1.00 33.94 ? 159 LEU   B CD2 1 
ATOM   4105 N  N   . LEU   B 2 190 ? 5.808   53.129 90.906  1.00 34.10 ? 160 LEU   B N   1 
ATOM   4106 C  CA  . LEU   B 2 190 ? 5.727   51.667 91.034  1.00 35.34 ? 160 LEU   B CA  1 
ATOM   4107 C  C   . LEU   B 2 190 ? 7.112   51.059 91.158  1.00 35.99 ? 160 LEU   B C   1 
ATOM   4108 O  O   . LEU   B 2 190 ? 7.301   50.159 91.958  1.00 36.56 ? 160 LEU   B O   1 
ATOM   4109 C  CB  . LEU   B 2 190 ? 5.017   51.049 89.829  1.00 36.46 ? 160 LEU   B CB  1 
ATOM   4110 C  CG  . LEU   B 2 190 ? 3.535   51.380 89.712  1.00 39.32 ? 160 LEU   B CG  1 
ATOM   4111 C  CD1 . LEU   B 2 190 ? 3.048   51.224 88.285  1.00 39.71 ? 160 LEU   B CD1 1 
ATOM   4112 C  CD2 . LEU   B 2 190 ? 2.722   50.547 90.684  1.00 40.46 ? 160 LEU   B CD2 1 
ATOM   4113 N  N   . GLN   B 2 191 ? 8.082   51.570 90.399  1.00 35.85 ? 161 GLN   B N   1 
ATOM   4114 C  CA  . GLN   B 2 191 ? 9.457   51.095 90.449  1.00 36.07 ? 161 GLN   B CA  1 
ATOM   4115 C  C   . GLN   B 2 191 ? 10.091  51.413 91.804  1.00 35.52 ? 161 GLN   B C   1 
ATOM   4116 O  O   . GLN   B 2 191 ? 10.792  50.574 92.356  1.00 35.45 ? 161 GLN   B O   1 
ATOM   4117 C  CB  . GLN   B 2 191 ? 10.277  51.707 89.302  1.00 38.47 ? 161 GLN   B CB  1 
ATOM   4118 C  CG  . GLN   B 2 191 ? 9.772   51.275 87.920  1.00 43.52 ? 161 GLN   B CG  1 
ATOM   4119 C  CD  . GLN   B 2 191 ? 10.308  52.125 86.781  1.00 49.72 ? 161 GLN   B CD  1 
ATOM   4120 O  OE1 . GLN   B 2 191 ? 10.845  53.225 86.975  1.00 51.85 ? 161 GLN   B OE1 1 
ATOM   4121 N  NE2 . GLN   B 2 191 ? 10.153  51.642 85.555  1.00 50.48 ? 161 GLN   B NE2 1 
ATOM   4122 N  N   . TYR   B 2 192 ? 9.814   52.594 92.360  1.00 35.01 ? 162 TYR   B N   1 
ATOM   4123 C  CA  . TYR   B 2 192 ? 10.349  52.969 93.670  1.00 35.21 ? 162 TYR   B CA  1 
ATOM   4124 C  C   . TYR   B 2 192 ? 9.784   52.119 94.801  1.00 35.48 ? 162 TYR   B C   1 
ATOM   4125 O  O   . TYR   B 2 192 ? 10.562  51.615 95.596  1.00 35.47 ? 162 TYR   B O   1 
ATOM   4126 C  CB  . TYR   B 2 192 ? 10.134  54.456 93.966  1.00 35.08 ? 162 TYR   B CB  1 
ATOM   4127 C  CG  . TYR   B 2 192 ? 10.942  55.367 93.074  1.00 35.80 ? 162 TYR   B CG  1 
ATOM   4128 C  CD1 . TYR   B 2 192 ? 12.284  55.122 92.830  1.00 36.34 ? 162 TYR   B CD1 1 
ATOM   4129 C  CD2 . TYR   B 2 192 ? 10.369  56.492 92.493  1.00 36.67 ? 162 TYR   B CD2 1 
ATOM   4130 C  CE1 . TYR   B 2 192 ? 13.040  55.973 92.034  1.00 37.24 ? 162 TYR   B CE1 1 
ATOM   4131 C  CE2 . TYR   B 2 192 ? 11.096  57.310 91.641  1.00 37.42 ? 162 TYR   B CE2 1 
ATOM   4132 C  CZ  . TYR   B 2 192 ? 12.442  57.068 91.441  1.00 38.27 ? 162 TYR   B CZ  1 
ATOM   4133 O  OH  . TYR   B 2 192 ? 13.178  57.904 90.645  1.00 40.06 ? 162 TYR   B OH  1 
ATOM   4134 N  N   . VAL   B 2 193 ? 8.451   51.938 94.878  1.00 35.97 ? 163 VAL   B N   1 
ATOM   4135 C  CA  . VAL   B 2 193 ? 7.861   51.128 95.956  1.00 36.92 ? 163 VAL   B CA  1 
ATOM   4136 C  C   . VAL   B 2 193 ? 8.227   49.646 95.823  1.00 38.10 ? 163 VAL   B C   1 
ATOM   4137 O  O   . VAL   B 2 193 ? 8.338   48.949 96.842  1.00 38.82 ? 163 VAL   B O   1 
ATOM   4138 C  CB  . VAL   B 2 193 ? 6.341   51.337 96.140  1.00 37.66 ? 163 VAL   B CB  1 
ATOM   4139 C  CG1 . VAL   B 2 193 ? 6.006   52.812 96.228  1.00 37.95 ? 163 VAL   B CG1 1 
ATOM   4140 C  CG2 . VAL   B 2 193 ? 5.552   50.678 95.015  1.00 38.55 ? 163 VAL   B CG2 1 
ATOM   4141 N  N   . GLN   B 2 194 ? 8.475   49.172 94.587  1.00 38.15 ? 164 GLN   B N   1 
ATOM   4142 C  CA  . GLN   B 2 194 ? 8.922   47.811 94.340  1.00 38.78 ? 164 GLN   B CA  1 
ATOM   4143 C  C   . GLN   B 2 194 ? 10.338  47.709 94.905  1.00 39.08 ? 164 GLN   B C   1 
ATOM   4144 O  O   . GLN   B 2 194 ? 10.580  46.847 95.737  1.00 39.58 ? 164 GLN   B O   1 
ATOM   4145 C  CB  . GLN   B 2 194 ? 8.903   47.472 92.840  1.00 40.67 ? 164 GLN   B CB  1 
ATOM   4146 C  CG  . GLN   B 2 194 ? 9.590   46.143 92.520  1.00 45.78 ? 164 GLN   B CG  1 
ATOM   4147 C  CD  . GLN   B 2 194 ? 9.944   45.992 91.063  1.00 51.85 ? 164 GLN   B CD  1 
ATOM   4148 O  OE1 . GLN   B 2 194 ? 10.943  46.550 90.570  1.00 53.33 ? 164 GLN   B OE1 1 
ATOM   4149 N  NE2 . GLN   B 2 194 ? 9.134   45.215 90.349  1.00 52.59 ? 164 GLN   B NE2 1 
ATOM   4150 N  N   . ASP   B 2 195 ? 11.226  48.662 94.580  1.00 38.54 ? 165 ASP   B N   1 
ATOM   4151 C  CA  . ASP   B 2 195 ? 12.575  48.683 95.134  1.00 39.17 ? 165 ASP   B CA  1 
ATOM   4152 C  C   . ASP   B 2 195 ? 12.561  48.711 96.666  1.00 40.01 ? 165 ASP   B C   1 
ATOM   4153 O  O   . ASP   B 2 195 ? 13.327  48.002 97.289  1.00 40.28 ? 165 ASP   B O   1 
ATOM   4154 C  CB  . ASP   B 2 195 ? 13.364  49.879 94.595  1.00 40.75 ? 165 ASP   B CB  1 
ATOM   4155 C  CG  . ASP   B 2 195 ? 14.793  49.895 95.080  1.00 46.65 ? 165 ASP   B CG  1 
ATOM   4156 O  OD1 . ASP   B 2 195 ? 15.614  49.186 94.501  1.00 48.92 ? 165 ASP   B OD1 1 
ATOM   4157 O  OD2 . ASP   B 2 195 ? 15.079  50.600 96.060  1.00 49.14 ? 165 ASP   B OD2 1 
ATOM   4158 N  N   . MET   B 2 196 ? 11.693  49.526 97.260  1.00 40.85 ? 166 MET   B N   1 
ATOM   4159 C  CA  . MET   B 2 196 ? 11.532  49.631 98.711  1.00 42.27 ? 166 MET   B CA  1 
ATOM   4160 C  C   . MET   B 2 196 ? 11.035  48.335 99.357  1.00 43.66 ? 166 MET   B C   1 
ATOM   4161 O  O   . MET   B 2 196 ? 11.206  48.162 100.558 1.00 43.86 ? 166 MET   B O   1 
ATOM   4162 C  CB  . MET   B 2 196 ? 10.489  50.702 99.043  1.00 42.65 ? 166 MET   B CB  1 
ATOM   4163 C  CG  . MET   B 2 196 ? 11.047  52.053 99.263  1.00 44.88 ? 166 MET   B CG  1 
ATOM   4164 S  SD  . MET   B 2 196 ? 9.869   53.036 100.216 1.00 48.90 ? 166 MET   B SD  1 
ATOM   4165 C  CE  . MET   B 2 196 ? 10.788  54.514 100.392 1.00 44.18 ? 166 MET   B CE  1 
ATOM   4166 N  N   . GLY   B 2 197 ? 10.357  47.491 98.584  1.00 44.40 ? 167 GLY   B N   1 
ATOM   4167 C  CA  . GLY   B 2 197 ? 9.738   46.276 99.089  1.00 46.02 ? 167 GLY   B CA  1 
ATOM   4168 C  C   . GLY   B 2 197 ? 8.564   46.612 99.995  1.00 47.65 ? 167 GLY   B C   1 
ATOM   4169 O  O   . GLY   B 2 197 ? 8.244   45.846 100.906 1.00 48.33 ? 167 GLY   B O   1 
ATOM   4170 N  N   . GLN   B 2 198 ? 7.910   47.771 99.747  1.00 47.77 ? 168 GLN   B N   1 
ATOM   4171 C  CA  . GLN   B 2 198 ? 6.832   48.286 100.566 1.00 48.62 ? 168 GLN   B CA  1 
ATOM   4172 C  C   . GLN   B 2 198 ? 5.547   48.569 99.794  1.00 49.18 ? 168 GLN   B C   1 
ATOM   4173 O  O   . GLN   B 2 198 ? 4.782   49.438 100.203 1.00 49.00 ? 168 GLN   B O   1 
ATOM   4174 C  CB  . GLN   B 2 198 ? 7.309   49.570 101.257 1.00 50.33 ? 168 GLN   B CB  1 
ATOM   4175 C  CG  . GLN   B 2 198 ? 8.262   49.325 102.398 1.00 54.63 ? 168 GLN   B CG  1 
ATOM   4176 C  CD  . GLN   B 2 198 ? 7.566   48.620 103.522 1.00 60.35 ? 168 GLN   B CD  1 
ATOM   4177 O  OE1 . GLN   B 2 198 ? 6.405   48.909 103.842 1.00 62.84 ? 168 GLN   B OE1 1 
ATOM   4178 N  NE2 . GLN   B 2 198 ? 8.258   47.680 104.140 1.00 60.87 ? 168 GLN   B NE2 1 
ATOM   4179 N  N   . GLU   B 2 199 ? 5.284   47.813 98.721  1.00 49.61 ? 169 GLU   B N   1 
ATOM   4180 C  CA  . GLU   B 2 199 ? 4.096   47.994 97.890  1.00 50.31 ? 169 GLU   B CA  1 
ATOM   4181 C  C   . GLU   B 2 199 ? 2.766   47.926 98.637  1.00 50.89 ? 169 GLU   B C   1 
ATOM   4182 O  O   . GLU   B 2 199 ? 1.941   48.820 98.472  1.00 51.27 ? 169 GLU   B O   1 
ATOM   4183 C  CB  . GLU   B 2 199 ? 4.099   47.001 96.727  1.00 52.64 ? 169 GLU   B CB  1 
ATOM   4184 C  CG  . GLU   B 2 199 ? 5.339   47.120 95.869  1.00 58.18 ? 169 GLU   B CG  1 
ATOM   4185 C  CD  . GLU   B 2 199 ? 5.427   46.096 94.760  1.00 65.50 ? 169 GLU   B CD  1 
ATOM   4186 O  OE1 . GLU   B 2 199 ? 5.864   44.956 95.040  1.00 66.38 ? 169 GLU   B OE1 1 
ATOM   4187 O  OE2 . GLU   B 2 199 ? 5.062   46.433 93.611  1.00 69.00 ? 169 GLU   B OE2 1 
ATOM   4188 N  N   . ASP   B 2 200 ? 2.545   46.887 99.449  1.00 50.90 ? 170 ASP   B N   1 
ATOM   4189 C  CA  . ASP   B 2 200 ? 1.273   46.734 100.154 1.00 51.27 ? 170 ASP   B CA  1 
ATOM   4190 C  C   . ASP   B 2 200 ? 0.957   47.892 101.086 1.00 50.23 ? 170 ASP   B C   1 
ATOM   4191 O  O   . ASP   B 2 200 ? -0.193  48.305 101.185 1.00 50.22 ? 170 ASP   B O   1 
ATOM   4192 C  CB  . ASP   B 2 200 ? 1.219   45.396 100.915 1.00 54.05 ? 170 ASP   B CB  1 
ATOM   4193 C  CG  . ASP   B 2 200 ? 1.143   44.168 100.020 1.00 61.31 ? 170 ASP   B CG  1 
ATOM   4194 O  OD1 . ASP   B 2 200 ? 0.858   44.328 98.805  1.00 62.40 ? 170 ASP   B OD1 1 
ATOM   4195 O  OD2 . ASP   B 2 200 ? 1.362   43.045 100.533 1.00 64.88 ? 170 ASP   B OD2 1 
ATOM   4196 N  N   . MET   B 2 201 ? 1.971   48.412 101.766 1.00 49.32 ? 171 MET   B N   1 
ATOM   4197 C  CA  . MET   B 2 201 ? 1.782   49.474 102.741 1.00 48.77 ? 171 MET   B CA  1 
ATOM   4198 C  C   . MET   B 2 201 ? 1.778   50.876 102.139 1.00 46.69 ? 171 MET   B C   1 
ATOM   4199 O  O   . MET   B 2 201 ? 0.919   51.677 102.482 1.00 47.00 ? 171 MET   B O   1 
ATOM   4200 C  CB  . MET   B 2 201 ? 2.862   49.371 103.836 1.00 50.42 ? 171 MET   B CB  1 
ATOM   4201 C  CG  . MET   B 2 201 ? 2.672   50.334 104.986 1.00 55.19 ? 171 MET   B CG  1 
ATOM   4202 S  SD  . MET   B 2 201 ? 4.229   50.643 105.878 1.00 67.89 ? 171 MET   B SD  1 
ATOM   4203 C  CE  . MET   B 2 201 ? 3.631   51.582 107.259 1.00 67.26 ? 171 MET   B CE  1 
ATOM   4204 N  N   . LEU   B 2 202 ? 2.739   51.181 101.258 1.00 44.21 ? 172 LEU   B N   1 
ATOM   4205 C  CA  . LEU   B 2 202 ? 2.906   52.527 100.750 1.00 42.40 ? 172 LEU   B CA  1 
ATOM   4206 C  C   . LEU   B 2 202 ? 2.288   52.838 99.405  1.00 40.05 ? 172 LEU   B C   1 
ATOM   4207 O  O   . LEU   B 2 202 ? 1.973   54.002 99.187  1.00 39.68 ? 172 LEU   B O   1 
ATOM   4208 C  CB  . LEU   B 2 202 ? 4.396   52.869 100.704 1.00 42.87 ? 172 LEU   B CB  1 
ATOM   4209 C  CG  . LEU   B 2 202 ? 5.095   52.896 102.059 1.00 44.25 ? 172 LEU   B CG  1 
ATOM   4210 C  CD1 . LEU   B 2 202 ? 6.586   53.011 101.889 1.00 44.60 ? 172 LEU   B CD1 1 
ATOM   4211 C  CD2 . LEU   B 2 202 ? 4.562   54.034 102.919 1.00 44.56 ? 172 LEU   B CD2 1 
ATOM   4212 N  N   . LEU   B 2 203 ? 2.162   51.859 98.490  1.00 38.17 ? 173 LEU   B N   1 
ATOM   4213 C  CA  . LEU   B 2 203 ? 1.641   52.150 97.151  1.00 36.98 ? 173 LEU   B CA  1 
ATOM   4214 C  C   . LEU   B 2 203 ? 0.231   52.787 97.138  1.00 35.27 ? 173 LEU   B C   1 
ATOM   4215 O  O   . LEU   B 2 203 ? 0.096   53.822 96.502  1.00 34.91 ? 173 LEU   B O   1 
ATOM   4216 C  CB  . LEU   B 2 203 ? 1.708   50.944 96.206  1.00 37.19 ? 173 LEU   B CB  1 
ATOM   4217 C  CG  . LEU   B 2 203 ? 1.325   51.220 94.749  1.00 39.04 ? 173 LEU   B CG  1 
ATOM   4218 C  CD1 . LEU   B 2 203 ? 2.245   52.258 94.112  1.00 38.96 ? 173 LEU   B CD1 1 
ATOM   4219 C  CD2 . LEU   B 2 203 ? 1.272   49.924 93.934  1.00 39.80 ? 173 LEU   B CD2 1 
ATOM   4220 N  N   . PRO   B 2 204 ? -0.814  52.256 97.814  1.00 34.20 ? 174 PRO   B N   1 
ATOM   4221 C  CA  . PRO   B 2 204 ? -2.129  52.937 97.773  1.00 32.92 ? 174 PRO   B CA  1 
ATOM   4222 C  C   . PRO   B 2 204 ? -2.098  54.434 98.122  1.00 31.70 ? 174 PRO   B C   1 
ATOM   4223 O  O   . PRO   B 2 204 ? -2.637  55.243 97.363  1.00 31.91 ? 174 PRO   B O   1 
ATOM   4224 C  CB  . PRO   B 2 204 ? -2.983  52.114 98.738  1.00 33.34 ? 174 PRO   B CB  1 
ATOM   4225 C  CG  . PRO   B 2 204 ? -2.356  50.729 98.663  1.00 34.33 ? 174 PRO   B CG  1 
ATOM   4226 C  CD  . PRO   B 2 204 ? -0.885  51.004 98.607  1.00 33.24 ? 174 PRO   B CD  1 
ATOM   4227 N  N   . LEU   B 2 205 ? -1.449  54.807 99.235  1.00 30.35 ? 175 LEU   B N   1 
ATOM   4228 C  CA  . LEU   B 2 205 ? -1.343  56.192 99.651  1.00 30.05 ? 175 LEU   B CA  1 
ATOM   4229 C  C   . LEU   B 2 205 ? -0.475  57.033 98.716  1.00 29.35 ? 175 LEU   B C   1 
ATOM   4230 O  O   . LEU   B 2 205 ? -0.912  58.093 98.300  1.00 29.02 ? 175 LEU   B O   1 
ATOM   4231 C  CB  . LEU   B 2 205 ? -0.821  56.282 101.083 1.00 30.84 ? 175 LEU   B CB  1 
ATOM   4232 C  CG  . LEU   B 2 205 ? -0.670  57.676 101.658 1.00 33.19 ? 175 LEU   B CG  1 
ATOM   4233 C  CD1 . LEU   B 2 205 ? -1.982  58.456 101.612 1.00 33.98 ? 175 LEU   B CD1 1 
ATOM   4234 C  CD2 . LEU   B 2 205 ? -0.194  57.600 103.060 1.00 34.14 ? 175 LEU   B CD2 1 
ATOM   4235 N  N   . ALA   B 2 206 ? 0.728   56.550 98.337  1.00 28.82 ? 176 ALA   B N   1 
ATOM   4236 C  CA  . ALA   B 2 206 ? 1.604   57.309 97.441  1.00 27.96 ? 176 ALA   B CA  1 
ATOM   4237 C  C   . ALA   B 2 206 ? 0.933   57.542 96.097  1.00 27.55 ? 176 ALA   B C   1 
ATOM   4238 O  O   . ALA   B 2 206 ? 1.053   58.620 95.546  1.00 27.38 ? 176 ALA   B O   1 
ATOM   4239 C  CB  . ALA   B 2 206 ? 2.928   56.586 97.255  1.00 27.44 ? 176 ALA   B CB  1 
ATOM   4240 N  N   . TRP   B 2 207 ? 0.186   56.555 95.598  1.00 27.43 ? 177 TRP   B N   1 
ATOM   4241 C  CA  . TRP   B 2 207 ? -0.542  56.661 94.337  1.00 27.82 ? 177 TRP   B CA  1 
ATOM   4242 C  C   . TRP   B 2 207 ? -1.606  57.749 94.437  1.00 26.40 ? 177 TRP   B C   1 
ATOM   4243 O  O   . TRP   B 2 207 ? -1.745  58.542 93.520  1.00 26.57 ? 177 TRP   B O   1 
ATOM   4244 C  CB  . TRP   B 2 207 ? -1.192  55.311 93.986  1.00 28.37 ? 177 TRP   B CB  1 
ATOM   4245 C  CG  . TRP   B 2 207 ? -1.872  55.281 92.659  1.00 29.74 ? 177 TRP   B CG  1 
ATOM   4246 C  CD1 . TRP   B 2 207 ? -3.112  55.768 92.350  1.00 30.46 ? 177 TRP   B CD1 1 
ATOM   4247 C  CD2 . TRP   B 2 207 ? -1.376  54.655 91.466  1.00 30.20 ? 177 TRP   B CD2 1 
ATOM   4248 N  NE1 . TRP   B 2 207 ? -3.413  55.487 91.035  1.00 30.74 ? 177 TRP   B NE1 1 
ATOM   4249 C  CE2 . TRP   B 2 207 ? -2.368  54.795 90.474  1.00 30.73 ? 177 TRP   B CE2 1 
ATOM   4250 C  CE3 . TRP   B 2 207 ? -0.197  53.965 91.150  1.00 30.75 ? 177 TRP   B CE3 1 
ATOM   4251 C  CZ2 . TRP   B 2 207 ? -2.192  54.318 89.178  1.00 31.77 ? 177 TRP   B CZ2 1 
ATOM   4252 C  CZ3 . TRP   B 2 207 ? -0.038  53.469 89.873  1.00 31.72 ? 177 TRP   B CZ3 1 
ATOM   4253 C  CH2 . TRP   B 2 207 ? -1.018  53.660 88.898  1.00 31.88 ? 177 TRP   B CH2 1 
ATOM   4254 N  N   . ARG   B 2 208 ? -2.336  57.803 95.557  1.00 25.62 ? 178 ARG   B N   1 
ATOM   4255 C  CA  . ARG   B 2 208 ? -3.374  58.806 95.795  1.00 25.21 ? 178 ARG   B CA  1 
ATOM   4256 C  C   . ARG   B 2 208 ? -2.742  60.184 95.897  1.00 26.29 ? 178 ARG   B C   1 
ATOM   4257 O  O   . ARG   B 2 208 ? -3.298  61.139 95.374  1.00 26.86 ? 178 ARG   B O   1 
ATOM   4258 C  CB  . ARG   B 2 208 ? -4.180  58.447 97.061  1.00 25.33 ? 178 ARG   B CB  1 
ATOM   4259 C  CG  . ARG   B 2 208 ? -5.032  59.577 97.628  1.00 26.39 ? 178 ARG   B CG  1 
ATOM   4260 C  CD  . ARG   B 2 208 ? -4.328  60.261 98.797  1.00 27.71 ? 178 ARG   B CD  1 
ATOM   4261 N  NE  . ARG   B 2 208 ? -4.861  61.600 98.971  1.00 28.39 ? 178 ARG   B NE  1 
ATOM   4262 C  CZ  . ARG   B 2 208 ? -5.770  61.943 99.880  1.00 28.35 ? 178 ARG   B CZ  1 
ATOM   4263 N  NH1 . ARG   B 2 208 ? -6.221  63.187 99.934  1.00 27.42 ? 178 ARG   B NH1 1 
ATOM   4264 N  NH2 . ARG   B 2 208 ? -6.238  61.041 100.735 1.00 25.78 ? 178 ARG   B NH2 1 
ATOM   4265 N  N   . ILE   B 2 209 ? -1.552  60.292 96.521  1.00 26.13 ? 179 ILE   B N   1 
ATOM   4266 C  CA  . ILE   B 2 209 ? -0.859  61.559 96.614  1.00 26.28 ? 179 ILE   B CA  1 
ATOM   4267 C  C   . ILE   B 2 209 ? -0.432  62.017 95.233  1.00 26.42 ? 179 ILE   B C   1 
ATOM   4268 O  O   . ILE   B 2 209 ? -0.622  63.188 94.914  1.00 26.99 ? 179 ILE   B O   1 
ATOM   4269 C  CB  . ILE   B 2 209 ? 0.282   61.538 97.659  1.00 26.48 ? 179 ILE   B CB  1 
ATOM   4270 C  CG1 . ILE   B 2 209 ? -0.303  61.268 99.088  1.00 27.27 ? 179 ILE   B CG1 1 
ATOM   4271 C  CG2 . ILE   B 2 209 ? 1.031   62.864 97.616  1.00 26.37 ? 179 ILE   B CG2 1 
ATOM   4272 C  CD1 . ILE   B 2 209 ? 0.708   61.103 100.186 1.00 28.01 ? 179 ILE   B CD1 1 
ATOM   4273 N  N   . VAL   B 2 210 ? 0.024   61.102 94.361  1.00 25.88 ? 180 VAL   B N   1 
ATOM   4274 C  CA  . VAL   B 2 210 ? 0.346   61.446 92.965  1.00 26.67 ? 180 VAL   B CA  1 
ATOM   4275 C  C   . VAL   B 2 210 ? -0.926  61.995 92.274  1.00 27.62 ? 180 VAL   B C   1 
ATOM   4276 O  O   . VAL   B 2 210 ? -0.845  62.992 91.579  1.00 27.85 ? 180 VAL   B O   1 
ATOM   4277 C  CB  . VAL   B 2 210 ? 0.935   60.257 92.147  1.00 26.94 ? 180 VAL   B CB  1 
ATOM   4278 C  CG1 . VAL   B 2 210 ? 1.022   60.613 90.656  1.00 26.73 ? 180 VAL   B CG1 1 
ATOM   4279 C  CG2 . VAL   B 2 210 ? 2.299   59.830 92.679  1.00 26.65 ? 180 VAL   B CG2 1 
ATOM   4280 N  N   . ASN   B 2 211 ? -2.112  61.406 92.540  1.00 27.80 ? 181 ASN   B N   1 
ATOM   4281 C  CA  . ASN   B 2 211 ? -3.378  61.934 91.985  1.00 28.26 ? 181 ASN   B CA  1 
ATOM   4282 C  C   . ASN   B 2 211 ? -3.593  63.374 92.393  1.00 28.31 ? 181 ASN   B C   1 
ATOM   4283 O  O   . ASN   B 2 211 ? -3.933  64.203 91.555  1.00 29.64 ? 181 ASN   B O   1 
ATOM   4284 C  CB  . ASN   B 2 211 ? -4.588  61.112 92.453  1.00 28.43 ? 181 ASN   B CB  1 
ATOM   4285 C  CG  . ASN   B 2 211 ? -4.640  59.738 91.878  1.00 29.65 ? 181 ASN   B CG  1 
ATOM   4286 O  OD1 . ASN   B 2 211 ? -3.976  59.433 90.894  1.00 30.24 ? 181 ASN   B OD1 1 
ATOM   4287 N  ND2 . ASN   B 2 211 ? -5.440  58.884 92.485  1.00 29.47 ? 181 ASN   B ND2 1 
ATOM   4288 N  N   . ASP   B 2 212 ? -3.312  63.675 93.662  1.00 26.98 ? 182 ASP   B N   1 
ATOM   4289 C  CA  . ASP   B 2 212 ? -3.413  65.004 94.253  1.00 25.78 ? 182 ASP   B CA  1 
ATOM   4290 C  C   . ASP   B 2 212 ? -2.464  66.030 93.636  1.00 25.38 ? 182 ASP   B C   1 
ATOM   4291 O  O   . ASP   B 2 212 ? -2.838  67.197 93.522  1.00 25.53 ? 182 ASP   B O   1 
ATOM   4292 C  CB  . ASP   B 2 212 ? -3.167  64.915 95.756  1.00 25.29 ? 182 ASP   B CB  1 
ATOM   4293 C  CG  . ASP   B 2 212 ? -4.210  64.140 96.520  1.00 27.61 ? 182 ASP   B CG  1 
ATOM   4294 O  OD1 . ASP   B 2 212 ? -5.300  63.915 95.978  1.00 27.90 ? 182 ASP   B OD1 1 
ATOM   4295 O  OD2 . ASP   B 2 212 ? -3.943  63.778 97.659  1.00 29.28 ? 182 ASP   B OD2 1 
ATOM   4296 N  N   . THR   B 2 213 ? -1.252  65.624 93.234  1.00 25.00 ? 183 THR   B N   1 
ATOM   4297 C  CA  . THR   B 2 213 ? -0.307  66.570 92.610  1.00 25.83 ? 183 THR   B CA  1 
ATOM   4298 C  C   . THR   B 2 213 ? -0.852  67.206 91.322  1.00 26.82 ? 183 THR   B C   1 
ATOM   4299 O  O   . THR   B 2 213 ? -0.366  68.261 90.921  1.00 27.43 ? 183 THR   B O   1 
ATOM   4300 C  CB  . THR   B 2 213 ? 1.063   65.939 92.389  1.00 26.67 ? 183 THR   B CB  1 
ATOM   4301 O  OG1 . THR   B 2 213 ? 0.962   64.864 91.438  1.00 26.27 ? 183 THR   B OG1 1 
ATOM   4302 C  CG2 . THR   B 2 213 ? 1.695   65.480 93.698  1.00 27.11 ? 183 THR   B CG2 1 
ATOM   4303 N  N   . TYR   B 2 214 ? -1.869  66.600 90.699  1.00 27.58 ? 184 TYR   B N   1 
ATOM   4304 C  CA  . TYR   B 2 214 ? -2.497  67.190 89.504  1.00 29.07 ? 184 TYR   B CA  1 
ATOM   4305 C  C   . TYR   B 2 214 ? -3.381  68.371 89.837  1.00 31.36 ? 184 TYR   B C   1 
ATOM   4306 O  O   . TYR   B 2 214 ? -3.743  69.108 88.943  1.00 32.35 ? 184 TYR   B O   1 
ATOM   4307 C  CB  . TYR   B 2 214 ? -3.240  66.152 88.651  1.00 28.63 ? 184 TYR   B CB  1 
ATOM   4308 C  CG  . TYR   B 2 214 ? -2.282  65.197 87.972  1.00 28.60 ? 184 TYR   B CG  1 
ATOM   4309 C  CD1 . TYR   B 2 214 ? -1.735  65.496 86.730  1.00 29.17 ? 184 TYR   B CD1 1 
ATOM   4310 C  CD2 . TYR   B 2 214 ? -1.859  64.041 88.609  1.00 28.73 ? 184 TYR   B CD2 1 
ATOM   4311 C  CE1 . TYR   B 2 214 ? -0.835  64.635 86.113  1.00 29.99 ? 184 TYR   B CE1 1 
ATOM   4312 C  CE2 . TYR   B 2 214 ? -0.956  63.177 88.010  1.00 29.71 ? 184 TYR   B CE2 1 
ATOM   4313 C  CZ  . TYR   B 2 214 ? -0.444  63.475 86.759  1.00 30.78 ? 184 TYR   B CZ  1 
ATOM   4314 O  OH  . TYR   B 2 214 ? 0.457   62.618 86.181  1.00 31.52 ? 184 TYR   B OH  1 
ATOM   4315 N  N   . ARG   B 2 215 ? -3.683  68.607 91.118  1.00 32.10 ? 185 ARG   B N   1 
ATOM   4316 C  CA  . ARG   B 2 215 ? -4.415  69.794 91.533  1.00 32.85 ? 185 ARG   B CA  1 
ATOM   4317 C  C   . ARG   B 2 215 ? -3.458  71.033 91.633  1.00 33.50 ? 185 ARG   B C   1 
ATOM   4318 O  O   . ARG   B 2 215 ? -3.918  72.124 91.958  1.00 35.15 ? 185 ARG   B O   1 
ATOM   4319 C  CB  . ARG   B 2 215 ? -5.151  69.529 92.859  1.00 34.10 ? 185 ARG   B CB  1 
ATOM   4320 C  CG  . ARG   B 2 215 ? -6.504  68.810 92.688  1.00 37.89 ? 185 ARG   B CG  1 
ATOM   4321 C  CD  . ARG   B 2 215 ? -6.418  67.304 92.426  1.00 42.19 ? 185 ARG   B CD  1 
ATOM   4322 N  NE  . ARG   B 2 215 ? -7.690  66.723 91.968  1.00 45.80 ? 185 ARG   B NE  1 
ATOM   4323 C  CZ  . ARG   B 2 215 ? -7.814  65.504 91.434  1.00 48.14 ? 185 ARG   B CZ  1 
ATOM   4324 N  NH1 . ARG   B 2 215 ? -6.749  64.727 91.281  1.00 47.12 ? 185 ARG   B NH1 1 
ATOM   4325 N  NH2 . ARG   B 2 215 ? -9.002  65.059 91.046  1.00 47.71 ? 185 ARG   B NH2 1 
ATOM   4326 N  N   . THR   B 2 216 ? -2.147  70.873 91.313  1.00 31.70 ? 186 THR   B N   1 
ATOM   4327 C  CA  . THR   B 2 216 ? -1.101  71.901 91.398  1.00 30.72 ? 186 THR   B CA  1 
ATOM   4328 C  C   . THR   B 2 216 ? -0.368  72.010 90.023  1.00 29.72 ? 186 THR   B C   1 
ATOM   4329 O  O   . THR   B 2 216 ? -0.651  71.221 89.119  1.00 29.72 ? 186 THR   B O   1 
ATOM   4330 C  CB  . THR   B 2 216 ? -0.084  71.500 92.538  1.00 31.96 ? 186 THR   B CB  1 
ATOM   4331 O  OG1 . THR   B 2 216 ? 0.733   70.427 92.068  1.00 33.14 ? 186 THR   B OG1 1 
ATOM   4332 C  CG2 . THR   B 2 216 ? -0.766  71.098 93.849  1.00 32.29 ? 186 THR   B CG2 1 
ATOM   4333 N  N   . ASP   B 2 217 ? 0.617   72.923 89.896  1.00 28.75 ? 187 ASP   B N   1 
ATOM   4334 C  CA  . ASP   B 2 217 ? 1.406   73.106 88.680  1.00 28.66 ? 187 ASP   B CA  1 
ATOM   4335 C  C   . ASP   B 2 217 ? 2.616   72.161 88.571  1.00 28.33 ? 187 ASP   B C   1 
ATOM   4336 O  O   . ASP   B 2 217 ? 3.380   72.299 87.614  1.00 28.52 ? 187 ASP   B O   1 
ATOM   4337 C  CB  . ASP   B 2 217 ? 1.945   74.541 88.635  1.00 30.81 ? 187 ASP   B CB  1 
ATOM   4338 C  CG  . ASP   B 2 217 ? 0.893   75.604 88.420  1.00 37.58 ? 187 ASP   B CG  1 
ATOM   4339 O  OD1 . ASP   B 2 217 ? -0.138  75.297 87.773  1.00 39.05 ? 187 ASP   B OD1 1 
ATOM   4340 O  OD2 . ASP   B 2 217 ? 1.105   76.755 88.889  1.00 40.57 ? 187 ASP   B OD2 1 
ATOM   4341 N  N   . LEU   B 2 218 ? 2.826   71.247 89.541  1.00 27.56 ? 188 LEU   B N   1 
ATOM   4342 C  CA  . LEU   B 2 218 ? 3.994   70.354 89.572  1.00 27.59 ? 188 LEU   B CA  1 
ATOM   4343 C  C   . LEU   B 2 218 ? 4.349   69.644 88.264  1.00 28.49 ? 188 LEU   B C   1 
ATOM   4344 O  O   . LEU   B 2 218 ? 5.529   69.625 87.907  1.00 29.07 ? 188 LEU   B O   1 
ATOM   4345 C  CB  . LEU   B 2 218 ? 3.883   69.329 90.682  1.00 27.41 ? 188 LEU   B CB  1 
ATOM   4346 C  CG  . LEU   B 2 218 ? 4.032   69.923 92.096  1.00 28.51 ? 188 LEU   B CG  1 
ATOM   4347 C  CD1 . LEU   B 2 218 ? 3.660   68.907 93.150  1.00 29.12 ? 188 LEU   B CD1 1 
ATOM   4348 C  CD2 . LEU   B 2 218 ? 5.418   70.484 92.316  1.00 27.76 ? 188 LEU   B CD2 1 
ATOM   4349 N  N   . CYS   B 2 219 ? 3.377   69.062 87.551  1.00 28.17 ? 189 CYS   B N   1 
ATOM   4350 C  CA  . CYS   B 2 219 ? 3.667   68.380 86.284  1.00 28.76 ? 189 CYS   B CA  1 
ATOM   4351 C  C   . CYS   B 2 219 ? 4.268   69.315 85.219  1.00 30.46 ? 189 CYS   B C   1 
ATOM   4352 O  O   . CYS   B 2 219 ? 4.844   68.831 84.244  1.00 31.97 ? 189 CYS   B O   1 
ATOM   4353 C  CB  . CYS   B 2 219 ? 2.430   67.671 85.754  1.00 28.28 ? 189 CYS   B CB  1 
ATOM   4354 S  SG  . CYS   B 2 219 ? 1.161   68.795 85.139  1.00 30.07 ? 189 CYS   B SG  1 
ATOM   4355 N  N   . LEU   B 2 220 ? 4.101   70.636 85.365  1.00 30.23 ? 190 LEU   B N   1 
ATOM   4356 C  CA  . LEU   B 2 220 ? 4.697   71.592 84.425  1.00 30.33 ? 190 LEU   B CA  1 
ATOM   4357 C  C   . LEU   B 2 220 ? 6.085   72.047 84.885  1.00 31.02 ? 190 LEU   B C   1 
ATOM   4358 O  O   . LEU   B 2 220 ? 6.749   72.740 84.140  1.00 32.06 ? 190 LEU   B O   1 
ATOM   4359 C  CB  . LEU   B 2 220 ? 3.813   72.848 84.287  1.00 30.11 ? 190 LEU   B CB  1 
ATOM   4360 C  CG  . LEU   B 2 220 ? 2.333   72.629 83.917  1.00 31.30 ? 190 LEU   B CG  1 
ATOM   4361 C  CD1 . LEU   B 2 220 ? 1.567   73.937 83.978  1.00 31.86 ? 190 LEU   B CD1 1 
ATOM   4362 C  CD2 . LEU   B 2 220 ? 2.188   72.032 82.521  1.00 31.50 ? 190 LEU   B CD2 1 
ATOM   4363 N  N   . LEU   B 2 221 ? 6.520   71.709 86.105  1.00 30.75 ? 191 LEU   B N   1 
ATOM   4364 C  CA  . LEU   B 2 221 ? 7.760   72.219 86.663  1.00 30.69 ? 191 LEU   B CA  1 
ATOM   4365 C  C   . LEU   B 2 221 ? 8.820   71.192 86.972  1.00 31.01 ? 191 LEU   B C   1 
ATOM   4366 O  O   . LEU   B 2 221 ? 9.995   71.546 87.063  1.00 31.72 ? 191 LEU   B O   1 
ATOM   4367 C  CB  . LEU   B 2 221 ? 7.430   72.983 87.950  1.00 30.70 ? 191 LEU   B CB  1 
ATOM   4368 C  CG  . LEU   B 2 221 ? 6.456   74.158 87.815  1.00 31.45 ? 191 LEU   B CG  1 
ATOM   4369 C  CD1 . LEU   B 2 221 ? 6.116   74.728 89.200  1.00 31.33 ? 191 LEU   B CD1 1 
ATOM   4370 C  CD2 . LEU   B 2 221 ? 7.027   75.261 86.890  1.00 31.20 ? 191 LEU   B CD2 1 
ATOM   4371 N  N   . TYR   B 2 222 ? 8.432   69.945 87.192  1.00 30.93 ? 192 TYR   B N   1 
ATOM   4372 C  CA  . TYR   B 2 222 ? 9.390   68.916 87.585  1.00 30.86 ? 192 TYR   B CA  1 
ATOM   4373 C  C   . TYR   B 2 222 ? 9.248   67.636 86.798  1.00 31.58 ? 192 TYR   B C   1 
ATOM   4374 O  O   . TYR   B 2 222 ? 8.124   67.212 86.528  1.00 32.06 ? 192 TYR   B O   1 
ATOM   4375 C  CB  . TYR   B 2 222 ? 9.185   68.586 89.077  1.00 30.09 ? 192 TYR   B CB  1 
ATOM   4376 C  CG  . TYR   B 2 222 ? 9.464   69.750 90.003  1.00 30.40 ? 192 TYR   B CG  1 
ATOM   4377 C  CD1 . TYR   B 2 222 ? 10.754  70.026 90.437  1.00 31.19 ? 192 TYR   B CD1 1 
ATOM   4378 C  CD2 . TYR   B 2 222 ? 8.435   70.561 90.466  1.00 30.71 ? 192 TYR   B CD2 1 
ATOM   4379 C  CE1 . TYR   B 2 222 ? 11.015  71.087 91.297  1.00 32.08 ? 192 TYR   B CE1 1 
ATOM   4380 C  CE2 . TYR   B 2 222 ? 8.682   71.614 91.339  1.00 31.36 ? 192 TYR   B CE2 1 
ATOM   4381 C  CZ  . TYR   B 2 222 ? 9.974   71.878 91.746  1.00 32.83 ? 192 TYR   B CZ  1 
ATOM   4382 O  OH  . TYR   B 2 222 ? 10.224  72.924 92.596  1.00 35.05 ? 192 TYR   B OH  1 
ATOM   4383 N  N   . PRO   B 2 223 ? 10.367  66.914 86.590  1.00 31.39 ? 193 PRO   B N   1 
ATOM   4384 C  CA  . PRO   B 2 223 ? 10.281  65.573 85.971  1.00 31.59 ? 193 PRO   B CA  1 
ATOM   4385 C  C   . PRO   B 2 223 ? 9.423   64.637 86.825  1.00 32.10 ? 193 PRO   B C   1 
ATOM   4386 O  O   . PRO   B 2 223 ? 9.439   64.730 88.059  1.00 32.51 ? 193 PRO   B O   1 
ATOM   4387 C  CB  . PRO   B 2 223 ? 11.741  65.096 85.939  1.00 31.90 ? 193 PRO   B CB  1 
ATOM   4388 C  CG  . PRO   B 2 223 ? 12.551  66.374 85.985  1.00 32.44 ? 193 PRO   B CG  1 
ATOM   4389 C  CD  . PRO   B 2 223 ? 11.764  67.285 86.888  1.00 30.71 ? 193 PRO   B CD  1 
ATOM   4390 N  N   . PRO   B 2 224 ? 8.647   63.752 86.178  1.00 31.52 ? 194 PRO   B N   1 
ATOM   4391 C  CA  . PRO   B 2 224 ? 7.732   62.869 86.932  1.00 30.97 ? 194 PRO   B CA  1 
ATOM   4392 C  C   . PRO   B 2 224 ? 8.344   62.017 88.034  1.00 30.52 ? 194 PRO   B C   1 
ATOM   4393 O  O   . PRO   B 2 224 ? 7.686   61.789 89.051  1.00 30.61 ? 194 PRO   B O   1 
ATOM   4394 C  CB  . PRO   B 2 224 ? 7.122   61.977 85.853  1.00 31.52 ? 194 PRO   B CB  1 
ATOM   4395 C  CG  . PRO   B 2 224 ? 7.267   62.748 84.601  1.00 32.70 ? 194 PRO   B CG  1 
ATOM   4396 C  CD  . PRO   B 2 224 ? 8.517   63.557 84.720  1.00 31.20 ? 194 PRO   B CD  1 
ATOM   4397 N  N   . PHE   B 2 225 ? 9.570   61.531 87.840  1.00 30.06 ? 195 PHE   B N   1 
ATOM   4398 C  CA  . PHE   B 2 225 ? 10.217  60.710 88.856  1.00 30.72 ? 195 PHE   B CA  1 
ATOM   4399 C  C   . PHE   B 2 225 ? 10.444  61.509 90.146  1.00 30.71 ? 195 PHE   B C   1 
ATOM   4400 O  O   . PHE   B 2 225 ? 10.377  60.928 91.215  1.00 31.23 ? 195 PHE   B O   1 
ATOM   4401 C  CB  . PHE   B 2 225 ? 11.513  60.050 88.331  1.00 31.06 ? 195 PHE   B CB  1 
ATOM   4402 C  CG  . PHE   B 2 225 ? 12.704  60.968 88.284  1.00 32.18 ? 195 PHE   B CG  1 
ATOM   4403 C  CD1 . PHE   B 2 225 ? 12.960  61.737 87.167  1.00 33.08 ? 195 PHE   B CD1 1 
ATOM   4404 C  CD2 . PHE   B 2 225 ? 13.573  61.063 89.362  1.00 33.24 ? 195 PHE   B CD2 1 
ATOM   4405 C  CE1 . PHE   B 2 225 ? 14.050  62.599 87.134  1.00 33.77 ? 195 PHE   B CE1 1 
ATOM   4406 C  CE2 . PHE   B 2 225 ? 14.650  61.942 89.331  1.00 33.80 ? 195 PHE   B CE2 1 
ATOM   4407 C  CZ  . PHE   B 2 225 ? 14.890  62.692 88.210  1.00 33.33 ? 195 PHE   B CZ  1 
ATOM   4408 N  N   . MET   B 2 226 ? 10.631  62.841 90.047  1.00 30.38 ? 196 MET   B N   1 
ATOM   4409 C  CA  . MET   B 2 226 ? 10.819  63.703 91.201  1.00 30.84 ? 196 MET   B CA  1 
ATOM   4410 C  C   . MET   B 2 226 ? 9.510   63.902 91.940  1.00 30.07 ? 196 MET   B C   1 
ATOM   4411 O  O   . MET   B 2 226 ? 9.512   63.912 93.173  1.00 29.90 ? 196 MET   B O   1 
ATOM   4412 C  CB  . MET   B 2 226 ? 11.433  65.040 90.792  1.00 32.45 ? 196 MET   B CB  1 
ATOM   4413 C  CG  . MET   B 2 226 ? 12.887  64.944 90.390  1.00 36.40 ? 196 MET   B CG  1 
ATOM   4414 S  SD  . MET   B 2 226 ? 13.475  66.610 90.013  1.00 48.37 ? 196 MET   B SD  1 
ATOM   4415 C  CE  . MET   B 2 226 ? 14.953  66.251 89.127  1.00 46.67 ? 196 MET   B CE  1 
ATOM   4416 N  N   . ILE   B 2 227 ? 8.384   64.024 91.201  1.00 29.26 ? 197 ILE   B N   1 
ATOM   4417 C  CA  . ILE   B 2 227 ? 7.061   64.124 91.825  1.00 29.31 ? 197 ILE   B CA  1 
ATOM   4418 C  C   . ILE   B 2 227 ? 6.715   62.787 92.510  1.00 29.45 ? 197 ILE   B C   1 
ATOM   4419 O  O   . ILE   B 2 227 ? 6.164   62.783 93.613  1.00 30.12 ? 197 ILE   B O   1 
ATOM   4420 C  CB  . ILE   B 2 227 ? 5.971   64.555 90.805  1.00 29.50 ? 197 ILE   B CB  1 
ATOM   4421 C  CG1 . ILE   B 2 227 ? 6.393   65.818 90.039  1.00 29.59 ? 197 ILE   B CG1 1 
ATOM   4422 C  CG2 . ILE   B 2 227 ? 4.600   64.740 91.483  1.00 29.37 ? 197 ILE   B CG2 1 
ATOM   4423 C  CD1 . ILE   B 2 227 ? 5.496   66.126 88.879  1.00 30.11 ? 197 ILE   B CD1 1 
ATOM   4424 N  N   . ALA   B 2 228 ? 7.096   61.662 91.900  1.00 28.90 ? 198 ALA   B N   1 
ATOM   4425 C  CA  . ALA   B 2 228 ? 6.860   60.336 92.482  1.00 28.81 ? 198 ALA   B CA  1 
ATOM   4426 C  C   . ALA   B 2 228 ? 7.638   60.194 93.795  1.00 29.26 ? 198 ALA   B C   1 
ATOM   4427 O  O   . ALA   B 2 228 ? 7.093   59.694 94.777  1.00 29.23 ? 198 ALA   B O   1 
ATOM   4428 C  CB  . ALA   B 2 228 ? 7.289   59.256 91.504  1.00 28.41 ? 198 ALA   B CB  1 
ATOM   4429 N  N   . LEU   B 2 229 ? 8.900   60.663 93.827  1.00 29.11 ? 199 LEU   B N   1 
ATOM   4430 C  CA  . LEU   B 2 229 ? 9.696   60.604 95.052  1.00 29.36 ? 199 LEU   B CA  1 
ATOM   4431 C  C   . LEU   B 2 229 ? 9.114   61.463 96.158  1.00 29.11 ? 199 LEU   B C   1 
ATOM   4432 O  O   . LEU   B 2 229 ? 9.141   61.056 97.312  1.00 29.25 ? 199 LEU   B O   1 
ATOM   4433 C  CB  . LEU   B 2 229 ? 11.158  60.991 94.764  1.00 29.53 ? 199 LEU   B CB  1 
ATOM   4434 C  CG  . LEU   B 2 229 ? 11.891  59.927 93.944  1.00 30.60 ? 199 LEU   B CG  1 
ATOM   4435 C  CD1 . LEU   B 2 229 ? 13.167  60.428 93.406  1.00 30.94 ? 199 LEU   B CD1 1 
ATOM   4436 C  CD2 . LEU   B 2 229 ? 12.102  58.689 94.753  1.00 31.81 ? 199 LEU   B CD2 1 
ATOM   4437 N  N   . ALA   B 2 230 ? 8.585   62.650 95.818  1.00 28.83 ? 200 ALA   B N   1 
ATOM   4438 C  CA  . ALA   B 2 230 ? 7.999   63.525 96.828  1.00 29.15 ? 200 ALA   B CA  1 
ATOM   4439 C  C   . ALA   B 2 230 ? 6.757   62.895 97.427  1.00 29.33 ? 200 ALA   B C   1 
ATOM   4440 O  O   . ALA   B 2 230 ? 6.591   62.927 98.647  1.00 29.88 ? 200 ALA   B O   1 
ATOM   4441 C  CB  . ALA   B 2 230 ? 7.670   64.876 96.235  1.00 29.01 ? 200 ALA   B CB  1 
ATOM   4442 N  N   . CYS   B 2 231 ? 5.921   62.267 96.582  1.00 28.70 ? 201 CYS   B N   1 
ATOM   4443 C  CA  . CYS   B 2 231 ? 4.707   61.584 97.014  1.00 28.83 ? 201 CYS   B CA  1 
ATOM   4444 C  C   . CYS   B 2 231 ? 4.999   60.404 97.867  1.00 29.70 ? 201 CYS   B C   1 
ATOM   4445 O  O   . CYS   B 2 231 ? 4.289   60.181 98.837  1.00 29.68 ? 201 CYS   B O   1 
ATOM   4446 C  CB  . CYS   B 2 231 ? 3.862   61.199 95.814  1.00 28.49 ? 201 CYS   B CB  1 
ATOM   4447 S  SG  . CYS   B 2 231 ? 3.348   62.618 94.846  1.00 28.08 ? 201 CYS   B SG  1 
ATOM   4448 N  N   . LEU   B 2 232 ? 6.026   59.623 97.486  1.00 30.55 ? 202 LEU   B N   1 
ATOM   4449 C  CA  . LEU   B 2 232 ? 6.471   58.473 98.248  1.00 31.78 ? 202 LEU   B CA  1 
ATOM   4450 C  C   . LEU   B 2 232 ? 7.014   58.924 99.611  1.00 33.57 ? 202 LEU   B C   1 
ATOM   4451 O  O   . LEU   B 2 232 ? 6.758   58.261 100.621 1.00 33.91 ? 202 LEU   B O   1 
ATOM   4452 C  CB  . LEU   B 2 232 ? 7.534   57.686 97.472  1.00 31.40 ? 202 LEU   B CB  1 
ATOM   4453 C  CG  . LEU   B 2 232 ? 8.013   56.395 98.113  1.00 32.74 ? 202 LEU   B CG  1 
ATOM   4454 C  CD1 . LEU   B 2 232 ? 6.835   55.482 98.515  1.00 33.13 ? 202 LEU   B CD1 1 
ATOM   4455 C  CD2 . LEU   B 2 232 ? 8.978   55.656 97.191  1.00 32.95 ? 202 LEU   B CD2 1 
ATOM   4456 N  N   . HIS   B 2 233 ? 7.736   60.057 99.645  1.00 34.10 ? 203 HIS   B N   1 
ATOM   4457 C  CA  . HIS   B 2 233 ? 8.264   60.595 100.888 1.00 35.06 ? 203 HIS   B CA  1 
ATOM   4458 C  C   . HIS   B 2 233 ? 7.123   60.996 101.810 1.00 34.79 ? 203 HIS   B C   1 
ATOM   4459 O  O   . HIS   B 2 233 ? 7.157   60.618 102.978 1.00 34.65 ? 203 HIS   B O   1 
ATOM   4460 C  CB  . HIS   B 2 233 ? 9.200   61.791 100.623 1.00 37.14 ? 203 HIS   B CB  1 
ATOM   4461 C  CG  . HIS   B 2 233 ? 9.782   62.386 101.872 1.00 41.24 ? 203 HIS   B CG  1 
ATOM   4462 N  ND1 . HIS   B 2 233 ? 11.014  61.970 102.367 1.00 43.28 ? 203 HIS   B ND1 1 
ATOM   4463 C  CD2 . HIS   B 2 233 ? 9.279   63.339 102.696 1.00 42.76 ? 203 HIS   B CD2 1 
ATOM   4464 C  CE1 . HIS   B 2 233 ? 11.207  62.669 103.476 1.00 43.99 ? 203 HIS   B CE1 1 
ATOM   4465 N  NE2 . HIS   B 2 233 ? 10.196  63.506 103.715 1.00 43.93 ? 203 HIS   B NE2 1 
ATOM   4466 N  N   . VAL   B 2 234 ? 6.099   61.732 101.291 1.00 34.35 ? 204 VAL   B N   1 
ATOM   4467 C  CA  . VAL   B 2 234 ? 4.945   62.153 102.107 1.00 34.26 ? 204 VAL   B CA  1 
ATOM   4468 C  C   . VAL   B 2 234 ? 4.180   60.942 102.609 1.00 34.55 ? 204 VAL   B C   1 
ATOM   4469 O  O   . VAL   B 2 234 ? 3.752   60.940 103.754 1.00 34.55 ? 204 VAL   B O   1 
ATOM   4470 C  CB  . VAL   B 2 234 ? 3.997   63.164 101.401 1.00 34.62 ? 204 VAL   B CB  1 
ATOM   4471 C  CG1 . VAL   B 2 234 ? 2.748   63.443 102.245 1.00 34.83 ? 204 VAL   B CG1 1 
ATOM   4472 C  CG2 . VAL   B 2 234 ? 4.715   64.459 101.068 1.00 34.50 ? 204 VAL   B CG2 1 
ATOM   4473 N  N   . ALA   B 2 235 ? 4.064   59.882 101.784 1.00 34.48 ? 205 ALA   B N   1 
ATOM   4474 C  CA  . ALA   B 2 235 ? 3.373   58.668 102.195 1.00 34.81 ? 205 ALA   B CA  1 
ATOM   4475 C  C   . ALA   B 2 235 ? 4.109   58.020 103.374 1.00 35.28 ? 205 ALA   B C   1 
ATOM   4476 O  O   . ALA   B 2 235 ? 3.465   57.633 104.343 1.00 34.85 ? 205 ALA   B O   1 
ATOM   4477 C  CB  . ALA   B 2 235 ? 3.238   57.695 101.029 1.00 34.29 ? 205 ALA   B CB  1 
ATOM   4478 N  N   . CYS   B 2 236 ? 5.451   57.986 103.326 1.00 35.66 ? 206 CYS   B N   1 
ATOM   4479 C  CA  . CYS   B 2 236 ? 6.286   57.458 104.417 1.00 36.66 ? 206 CYS   B CA  1 
ATOM   4480 C  C   . CYS   B 2 236 ? 6.071   58.249 105.705 1.00 37.72 ? 206 CYS   B C   1 
ATOM   4481 O  O   . CYS   B 2 236 ? 6.034   57.660 106.765 1.00 37.98 ? 206 CYS   B O   1 
ATOM   4482 C  CB  . CYS   B 2 236 ? 7.763   57.465 104.031 1.00 36.81 ? 206 CYS   B CB  1 
ATOM   4483 S  SG  . CYS   B 2 236 ? 8.190   56.344 102.687 1.00 38.38 ? 206 CYS   B SG  1 
ATOM   4484 N  N   . VAL   B 2 237 ? 5.994   59.588 105.620 1.00 38.23 ? 207 VAL   B N   1 
ATOM   4485 C  CA  . VAL   B 2 237 ? 5.797   60.434 106.785 1.00 38.78 ? 207 VAL   B CA  1 
ATOM   4486 C  C   . VAL   B 2 237 ? 4.425   60.173 107.392 1.00 41.21 ? 207 VAL   B C   1 
ATOM   4487 O  O   . VAL   B 2 237 ? 4.302   60.001 108.608 1.00 42.16 ? 207 VAL   B O   1 
ATOM   4488 C  CB  . VAL   B 2 237 ? 5.998   61.923 106.431 1.00 38.20 ? 207 VAL   B CB  1 
ATOM   4489 C  CG1 . VAL   B 2 237 ? 5.696   62.827 107.627 1.00 38.00 ? 207 VAL   B CG1 1 
ATOM   4490 C  CG2 . VAL   B 2 237 ? 7.406   62.172 105.919 1.00 38.13 ? 207 VAL   B CG2 1 
ATOM   4491 N  N   . VAL   B 2 238 ? 3.398   60.106 106.543 1.00 41.86 ? 208 VAL   B N   1 
ATOM   4492 C  CA  . VAL   B 2 238 ? 2.026   59.848 106.962 1.00 42.52 ? 208 VAL   B CA  1 
ATOM   4493 C  C   . VAL   B 2 238 ? 1.916   58.491 107.645 1.00 44.42 ? 208 VAL   B C   1 
ATOM   4494 O  O   . VAL   B 2 238 ? 1.357   58.383 108.739 1.00 44.89 ? 208 VAL   B O   1 
ATOM   4495 C  CB  . VAL   B 2 238 ? 1.050   59.996 105.771 1.00 41.99 ? 208 VAL   B CB  1 
ATOM   4496 C  CG1 . VAL   B 2 238 ? -0.327  59.437 106.107 1.00 42.43 ? 208 VAL   B CG1 1 
ATOM   4497 C  CG2 . VAL   B 2 238 ? 0.944   61.453 105.356 1.00 41.92 ? 208 VAL   B CG2 1 
ATOM   4498 N  N   . GLN   B 2 239 ? 2.494   57.469 107.031 1.00 45.44 ? 209 GLN   B N   1 
ATOM   4499 C  CA  . GLN   B 2 239 ? 2.453   56.122 107.572 1.00 46.87 ? 209 GLN   B CA  1 
ATOM   4500 C  C   . GLN   B 2 239 ? 3.600   55.775 108.519 1.00 48.31 ? 209 GLN   B C   1 
ATOM   4501 O  O   . GLN   B 2 239 ? 3.778   54.606 108.858 1.00 48.58 ? 209 GLN   B O   1 
ATOM   4502 C  CB  . GLN   B 2 239 ? 2.348   55.113 106.441 1.00 49.15 ? 209 GLN   B CB  1 
ATOM   4503 C  CG  . GLN   B 2 239 ? 0.898   54.785 106.176 1.00 54.15 ? 209 GLN   B CG  1 
ATOM   4504 C  CD  . GLN   B 2 239 ? 0.727   54.140 104.845 1.00 60.89 ? 209 GLN   B CD  1 
ATOM   4505 O  OE1 . GLN   B 2 239 ? 1.280   54.587 103.841 1.00 62.82 ? 209 GLN   B OE1 1 
ATOM   4506 N  NE2 . GLN   B 2 239 ? -0.057  53.077 104.808 1.00 62.63 ? 209 GLN   B NE2 1 
ATOM   4507 N  N   . GLN   B 2 240 ? 4.352   56.789 108.974 1.00 49.18 ? 210 GLN   B N   1 
ATOM   4508 C  CA  . GLN   B 2 240 ? 5.457   56.680 109.922 1.00 50.44 ? 210 GLN   B CA  1 
ATOM   4509 C  C   . GLN   B 2 240 ? 6.405   55.539 109.607 1.00 51.32 ? 210 GLN   B C   1 
ATOM   4510 O  O   . GLN   B 2 240 ? 6.752   54.741 110.475 1.00 51.89 ? 210 GLN   B O   1 
ATOM   4511 C  CB  . GLN   B 2 240 ? 4.918   56.615 111.349 1.00 52.27 ? 210 GLN   B CB  1 
ATOM   4512 C  CG  . GLN   B 2 240 ? 4.072   57.854 111.654 1.00 56.33 ? 210 GLN   B CG  1 
ATOM   4513 C  CD  . GLN   B 2 240 ? 3.429   57.850 113.015 1.00 61.54 ? 210 GLN   B CD  1 
ATOM   4514 O  OE1 . GLN   B 2 240 ? 3.529   56.885 113.782 1.00 62.30 ? 210 GLN   B OE1 1 
ATOM   4515 N  NE2 . GLN   B 2 240 ? 2.743   58.945 113.335 1.00 62.82 ? 210 GLN   B NE2 1 
ATOM   4516 N  N   . LYS   B 2 241 ? 6.806   55.466 108.339 1.00 51.12 ? 211 LYS   B N   1 
ATOM   4517 C  CA  . LYS   B 2 241 ? 7.718   54.473 107.813 1.00 51.46 ? 211 LYS   B CA  1 
ATOM   4518 C  C   . LYS   B 2 241 ? 9.072   55.134 107.665 1.00 52.15 ? 211 LYS   B C   1 
ATOM   4519 O  O   . LYS   B 2 241 ? 9.196   56.150 106.976 1.00 53.06 ? 211 LYS   B O   1 
ATOM   4520 C  CB  . LYS   B 2 241 ? 7.215   53.964 106.449 1.00 53.17 ? 211 LYS   B CB  1 
ATOM   4521 C  CG  . LYS   B 2 241 ? 8.153   52.977 105.775 1.00 58.46 ? 211 LYS   B CG  1 
ATOM   4522 C  CD  . LYS   B 2 241 ? 8.258   51.669 106.572 1.00 64.68 ? 211 LYS   B CD  1 
ATOM   4523 C  CE  . LYS   B 2 241 ? 9.247   50.688 105.978 1.00 69.08 ? 211 LYS   B CE  1 
ATOM   4524 N  NZ  . LYS   B 2 241 ? 9.070   49.322 106.550 1.00 71.32 ? 211 LYS   B NZ  1 
ATOM   4525 N  N   . ASP   B 2 242 ? 10.084  54.585 108.326 1.00 51.84 ? 212 ASP   B N   1 
ATOM   4526 C  CA  . ASP   B 2 242 ? 11.428  55.125 108.247 1.00 51.59 ? 212 ASP   B CA  1 
ATOM   4527 C  C   . ASP   B 2 242 ? 12.021  54.727 106.909 1.00 50.64 ? 212 ASP   B C   1 
ATOM   4528 O  O   . ASP   B 2 242 ? 12.187  53.546 106.641 1.00 51.11 ? 212 ASP   B O   1 
ATOM   4529 C  CB  . ASP   B 2 242 ? 12.283  54.580 109.396 1.00 53.86 ? 212 ASP   B CB  1 
ATOM   4530 C  CG  . ASP   B 2 242 ? 13.627  55.269 109.580 1.00 60.00 ? 212 ASP   B CG  1 
ATOM   4531 O  OD1 . ASP   B 2 242 ? 13.972  56.141 108.746 1.00 60.51 ? 212 ASP   B OD1 1 
ATOM   4532 O  OD2 . ASP   B 2 242 ? 14.337  54.933 110.555 1.00 63.30 ? 212 ASP   B OD2 1 
ATOM   4533 N  N   . ALA   B 2 243 ? 12.317  55.702 106.068 1.00 49.56 ? 213 ALA   B N   1 
ATOM   4534 C  CA  . ALA   B 2 243 ? 12.922  55.448 104.767 1.00 49.25 ? 213 ALA   B CA  1 
ATOM   4535 C  C   . ALA   B 2 243 ? 14.028  56.454 104.446 1.00 48.95 ? 213 ALA   B C   1 
ATOM   4536 O  O   . ALA   B 2 243 ? 14.301  56.696 103.272 1.00 48.52 ? 213 ALA   B O   1 
ATOM   4537 C  CB  . ALA   B 2 243 ? 11.863  55.467 103.684 1.00 49.27 ? 213 ALA   B CB  1 
ATOM   4538 N  N   . ARG   B 2 244 ? 14.685  57.016 105.487 1.00 48.84 ? 214 ARG   B N   1 
ATOM   4539 C  CA  . ARG   B 2 244 ? 15.760  57.991 105.327 1.00 48.99 ? 214 ARG   B CA  1 
ATOM   4540 C  C   . ARG   B 2 244 ? 16.948  57.419 104.591 1.00 48.18 ? 214 ARG   B C   1 
ATOM   4541 O  O   . ARG   B 2 244 ? 17.503  58.094 103.734 1.00 48.25 ? 214 ARG   B O   1 
ATOM   4542 C  CB  . ARG   B 2 244 ? 16.194  58.565 106.678 1.00 50.87 ? 214 ARG   B CB  1 
ATOM   4543 C  CG  . ARG   B 2 244 ? 15.106  59.405 107.343 1.00 55.84 ? 214 ARG   B CG  1 
ATOM   4544 C  CD  . ARG   B 2 244 ? 15.322  59.585 108.839 1.00 60.74 ? 214 ARG   B CD  1 
ATOM   4545 N  NE  . ARG   B 2 244 ? 15.581  58.306 109.504 1.00 65.15 ? 214 ARG   B NE  1 
ATOM   4546 C  CZ  . ARG   B 2 244 ? 16.136  58.180 110.704 1.00 67.92 ? 214 ARG   B CZ  1 
ATOM   4547 N  NH1 . ARG   B 2 244 ? 16.359  56.975 111.214 1.00 67.40 ? 214 ARG   B NH1 1 
ATOM   4548 N  NH2 . ARG   B 2 244 ? 16.480  59.257 111.401 1.00 68.16 ? 214 ARG   B NH2 1 
ATOM   4549 N  N   . GLN   B 2 245 ? 17.330  56.178 104.908 1.00 47.32 ? 215 GLN   B N   1 
ATOM   4550 C  CA  . GLN   B 2 245 ? 18.460  55.523 104.266 1.00 46.97 ? 215 GLN   B CA  1 
ATOM   4551 C  C   . GLN   B 2 245 ? 18.158  55.232 102.809 1.00 45.40 ? 215 GLN   B C   1 
ATOM   4552 O  O   . GLN   B 2 245 ? 19.016  55.460 101.956 1.00 45.78 ? 215 GLN   B O   1 
ATOM   4553 C  CB  . GLN   B 2 245 ? 18.843  54.235 105.014 1.00 50.12 ? 215 GLN   B CB  1 
ATOM   4554 C  CG  . GLN   B 2 245 ? 20.144  53.616 104.513 1.00 56.20 ? 215 GLN   B CG  1 
ATOM   4555 C  CD  . GLN   B 2 245 ? 20.266  52.162 104.895 1.00 63.53 ? 215 GLN   B CD  1 
ATOM   4556 O  OE1 . GLN   B 2 245 ? 20.265  51.795 106.084 1.00 65.11 ? 215 GLN   B OE1 1 
ATOM   4557 N  NE2 . GLN   B 2 245 ? 20.379  51.302 103.883 1.00 65.19 ? 215 GLN   B NE2 1 
ATOM   4558 N  N   . TRP   B 2 246 ? 16.932  54.774 102.498 1.00 43.65 ? 216 TRP   B N   1 
ATOM   4559 C  CA  . TRP   B 2 246 ? 16.556  54.517 101.101 1.00 42.56 ? 216 TRP   B CA  1 
ATOM   4560 C  C   . TRP   B 2 246 ? 16.598  55.834 100.310 1.00 42.38 ? 216 TRP   B C   1 
ATOM   4561 O  O   . TRP   B 2 246 ? 17.184  55.874 99.231  1.00 42.24 ? 216 TRP   B O   1 
ATOM   4562 C  CB  . TRP   B 2 246 ? 15.172  53.830 100.986 1.00 41.61 ? 216 TRP   B CB  1 
ATOM   4563 C  CG  . TRP   B 2 246 ? 14.787  53.451 99.577  1.00 41.36 ? 216 TRP   B CG  1 
ATOM   4564 C  CD1 . TRP   B 2 246 ? 15.021  52.262 98.957  1.00 41.88 ? 216 TRP   B CD1 1 
ATOM   4565 C  CD2 . TRP   B 2 246 ? 14.099  54.275 98.618  1.00 41.19 ? 216 TRP   B CD2 1 
ATOM   4566 N  NE1 . TRP   B 2 246 ? 14.541  52.297 97.665  1.00 42.03 ? 216 TRP   B NE1 1 
ATOM   4567 C  CE2 . TRP   B 2 246 ? 13.985  53.526 97.427  1.00 41.90 ? 216 TRP   B CE2 1 
ATOM   4568 C  CE3 . TRP   B 2 246 ? 13.616  55.590 98.633  1.00 41.48 ? 216 TRP   B CE3 1 
ATOM   4569 C  CZ2 . TRP   B 2 246 ? 13.372  54.036 96.277  1.00 42.25 ? 216 TRP   B CZ2 1 
ATOM   4570 C  CZ3 . TRP   B 2 246 ? 13.006  56.087 97.497  1.00 42.53 ? 216 TRP   B CZ3 1 
ATOM   4571 C  CH2 . TRP   B 2 246 ? 12.894  55.315 96.334  1.00 42.38 ? 216 TRP   B CH2 1 
ATOM   4572 N  N   . PHE   B 2 247 ? 16.051  56.924 100.887 1.00 42.29 ? 217 PHE   B N   1 
ATOM   4573 C  CA  . PHE   B 2 247 ? 16.063  58.243 100.244 1.00 42.90 ? 217 PHE   B CA  1 
ATOM   4574 C  C   . PHE   B 2 247 ? 17.481  58.850 100.096 1.00 44.64 ? 217 PHE   B C   1 
ATOM   4575 O  O   . PHE   B 2 247 ? 17.761  59.515 99.106  1.00 44.60 ? 217 PHE   B O   1 
ATOM   4576 C  CB  . PHE   B 2 247 ? 15.106  59.217 100.956 1.00 41.81 ? 217 PHE   B CB  1 
ATOM   4577 C  CG  . PHE   B 2 247 ? 13.692  59.160 100.417 1.00 41.01 ? 217 PHE   B CG  1 
ATOM   4578 C  CD1 . PHE   B 2 247 ? 13.365  59.773 99.221  1.00 40.99 ? 217 PHE   B CD1 1 
ATOM   4579 C  CD2 . PHE   B 2 247 ? 12.697  58.491 101.104 1.00 40.83 ? 217 PHE   B CD2 1 
ATOM   4580 C  CE1 . PHE   B 2 247 ? 12.077  59.703 98.721  1.00 41.06 ? 217 PHE   B CE1 1 
ATOM   4581 C  CE2 . PHE   B 2 247 ? 11.417  58.405 100.589 1.00 41.01 ? 217 PHE   B CE2 1 
ATOM   4582 C  CZ  . PHE   B 2 247 ? 11.115  59.013 99.402  1.00 40.71 ? 217 PHE   B CZ  1 
ATOM   4583 N  N   . ALA   B 2 248 ? 18.369  58.615 101.074 1.00 45.74 ? 218 ALA   B N   1 
ATOM   4584 C  CA  . ALA   B 2 248 ? 19.747  59.105 101.042 1.00 46.78 ? 218 ALA   B CA  1 
ATOM   4585 C  C   . ALA   B 2 248 ? 20.567  58.359 99.993  1.00 47.96 ? 218 ALA   B C   1 
ATOM   4586 O  O   . ALA   B 2 248 ? 21.414  58.969 99.340  1.00 48.49 ? 218 ALA   B O   1 
ATOM   4587 C  CB  . ALA   B 2 248 ? 20.393  58.959 102.413 1.00 46.80 ? 218 ALA   B CB  1 
ATOM   4588 N  N   . GLU   B 2 249 ? 20.297  57.061 99.786  1.00 48.17 ? 219 GLU   B N   1 
ATOM   4589 C  CA  . GLU   B 2 249 ? 21.013  56.291 98.768  1.00 49.31 ? 219 GLU   B CA  1 
ATOM   4590 C  C   . GLU   B 2 249 ? 20.656  56.683 97.319  1.00 49.65 ? 219 GLU   B C   1 
ATOM   4591 O  O   . GLU   B 2 249 ? 21.279  56.180 96.389  1.00 49.65 ? 219 GLU   B O   1 
ATOM   4592 C  CB  . GLU   B 2 249 ? 20.825  54.779 98.980  1.00 52.71 ? 219 GLU   B CB  1 
ATOM   4593 C  CG  . GLU   B 2 249 ? 21.635  54.231 100.145 1.00 58.42 ? 219 GLU   B CG  1 
ATOM   4594 C  CD  . GLU   B 2 249 ? 21.211  52.865 100.648 1.00 65.39 ? 219 GLU   B CD  1 
ATOM   4595 O  OE1 . GLU   B 2 249 ? 20.325  52.244 100.016 1.00 66.73 ? 219 GLU   B OE1 1 
ATOM   4596 O  OE2 . GLU   B 2 249 ? 21.761  52.420 101.682 1.00 67.66 ? 219 GLU   B OE2 1 
ATOM   4597 N  N   . LEU   B 2 250 ? 19.676  57.577 97.131  1.00 49.74 ? 220 LEU   B N   1 
ATOM   4598 C  CA  . LEU   B 2 250 ? 19.246  58.049 95.818  1.00 50.49 ? 220 LEU   B CA  1 
ATOM   4599 C  C   . LEU   B 2 250 ? 20.212  59.098 95.283  1.00 51.19 ? 220 LEU   B C   1 
ATOM   4600 O  O   . LEU   B 2 250 ? 20.620  59.988 96.029  1.00 51.39 ? 220 LEU   B O   1 
ATOM   4601 C  CB  . LEU   B 2 250 ? 17.865  58.716 95.941  1.00 50.45 ? 220 LEU   B CB  1 
ATOM   4602 C  CG  . LEU   B 2 250 ? 16.665  57.814 96.054  1.00 51.23 ? 220 LEU   B CG  1 
ATOM   4603 C  CD1 . LEU   B 2 250 ? 15.435  58.622 96.362  1.00 51.60 ? 220 LEU   B CD1 1 
ATOM   4604 C  CD2 . LEU   B 2 250 ? 16.468  57.026 94.784  1.00 51.56 ? 220 LEU   B CD2 1 
ATOM   4605 N  N   . SER   B 2 251 ? 20.523  59.044 93.989  1.00 51.53 ? 221 SER   B N   1 
ATOM   4606 C  CA  . SER   B 2 251 ? 21.364  60.062 93.367  1.00 52.84 ? 221 SER   B CA  1 
ATOM   4607 C  C   . SER   B 2 251 ? 20.416  61.114 92.793  1.00 53.44 ? 221 SER   B C   1 
ATOM   4608 O  O   . SER   B 2 251 ? 20.231  61.210 91.579  1.00 53.40 ? 221 SER   B O   1 
ATOM   4609 C  CB  . SER   B 2 251 ? 22.235  59.456 92.270  1.00 54.76 ? 221 SER   B CB  1 
ATOM   4610 O  OG  . SER   B 2 251 ? 21.438  58.785 91.309  1.00 57.83 ? 221 SER   B OG  1 
ATOM   4611 N  N   . VAL   B 2 252 ? 19.742  61.846 93.689  1.00 53.60 ? 222 VAL   B N   1 
ATOM   4612 C  CA  . VAL   B 2 252 ? 18.768  62.870 93.319  1.00 53.90 ? 222 VAL   B CA  1 
ATOM   4613 C  C   . VAL   B 2 252 ? 19.030  64.163 94.091  1.00 53.90 ? 222 VAL   B C   1 
ATOM   4614 O  O   . VAL   B 2 252 ? 19.611  64.144 95.176  1.00 53.89 ? 222 VAL   B O   1 
ATOM   4615 C  CB  . VAL   B 2 252 ? 17.298  62.404 93.532  1.00 54.56 ? 222 VAL   B CB  1 
ATOM   4616 C  CG1 . VAL   B 2 252 ? 16.999  61.112 92.777  1.00 55.27 ? 222 VAL   B CG1 1 
ATOM   4617 C  CG2 . VAL   B 2 252 ? 16.970  62.260 95.016  1.00 54.88 ? 222 VAL   B CG2 1 
ATOM   4618 N  N   . ASP   B 2 253 ? 18.569  65.288 93.535  1.00 53.64 ? 223 ASP   B N   1 
ATOM   4619 C  CA  . ASP   B 2 253 ? 18.688  66.586 94.183  1.00 53.45 ? 223 ASP   B CA  1 
ATOM   4620 C  C   . ASP   B 2 253 ? 17.564  66.636 95.199  1.00 53.03 ? 223 ASP   B C   1 
ATOM   4621 O  O   . ASP   B 2 253 ? 16.423  66.896 94.823  1.00 53.35 ? 223 ASP   B O   1 
ATOM   4622 C  CB  . ASP   B 2 253 ? 18.510  67.706 93.139  1.00 55.07 ? 223 ASP   B CB  1 
ATOM   4623 C  CG  . ASP   B 2 253 ? 18.834  69.107 93.631  1.00 59.34 ? 223 ASP   B CG  1 
ATOM   4624 O  OD1 . ASP   B 2 253 ? 19.057  69.273 94.855  1.00 59.66 ? 223 ASP   B OD1 1 
ATOM   4625 O  OD2 . ASP   B 2 253 ? 18.864  70.040 92.790  1.00 61.56 ? 223 ASP   B OD2 1 
ATOM   4626 N  N   . MET   B 2 254 ? 17.868  66.362 96.476  1.00 52.21 ? 224 MET   B N   1 
ATOM   4627 C  CA  . MET   B 2 254 ? 16.857  66.374 97.538  1.00 51.78 ? 224 MET   B CA  1 
ATOM   4628 C  C   . MET   B 2 254 ? 16.287  67.756 97.835  1.00 51.07 ? 224 MET   B C   1 
ATOM   4629 O  O   . MET   B 2 254 ? 15.275  67.839 98.526  1.00 51.15 ? 224 MET   B O   1 
ATOM   4630 C  CB  . MET   B 2 254 ? 17.369  65.715 98.827  1.00 52.48 ? 224 MET   B CB  1 
ATOM   4631 C  CG  . MET   B 2 254 ? 17.469  64.206 98.735  1.00 55.40 ? 224 MET   B CG  1 
ATOM   4632 S  SD  . MET   B 2 254 ? 15.877  63.347 98.563  1.00 60.92 ? 224 MET   B SD  1 
ATOM   4633 C  CE  . MET   B 2 254 ? 15.015  63.969 99.993  1.00 59.97 ? 224 MET   B CE  1 
ATOM   4634 N  N   . GLU   B 2 255 ? 16.919  68.837 97.336  1.00 50.26 ? 225 GLU   B N   1 
ATOM   4635 C  CA  . GLU   B 2 255 ? 16.365  70.178 97.535  1.00 49.90 ? 225 GLU   B CA  1 
ATOM   4636 C  C   . GLU   B 2 255 ? 15.136  70.336 96.656  1.00 47.97 ? 225 GLU   B C   1 
ATOM   4637 O  O   . GLU   B 2 255 ? 14.112  70.817 97.134  1.00 48.21 ? 225 GLU   B O   1 
ATOM   4638 C  CB  . GLU   B 2 255 ? 17.396  71.300 97.299  1.00 53.26 ? 225 GLU   B CB  1 
ATOM   4639 C  CG  . GLU   B 2 255 ? 16.859  72.705 97.555  1.00 60.27 ? 225 GLU   B CG  1 
ATOM   4640 C  CD  . GLU   B 2 255 ? 16.006  72.947 98.794  1.00 69.44 ? 225 GLU   B CD  1 
ATOM   4641 O  OE1 . GLU   B 2 255 ? 16.396  72.495 99.897  1.00 72.36 ? 225 GLU   B OE1 1 
ATOM   4642 O  OE2 . GLU   B 2 255 ? 14.946  73.604 98.660  1.00 70.98 ? 225 GLU   B OE2 1 
ATOM   4643 N  N   . LYS   B 2 256 ? 15.191  69.836 95.417  1.00 46.16 ? 226 LYS   B N   1 
ATOM   4644 C  CA  . LYS   B 2 256 ? 14.032  69.865 94.533  1.00 44.90 ? 226 LYS   B CA  1 
ATOM   4645 C  C   . LYS   B 2 256 ? 12.914  68.958 95.033  1.00 42.80 ? 226 LYS   B C   1 
ATOM   4646 O  O   . LYS   B 2 256 ? 11.753  69.301 94.874  1.00 43.06 ? 226 LYS   B O   1 
ATOM   4647 C  CB  . LYS   B 2 256 ? 14.428  69.554 93.091  1.00 46.80 ? 226 LYS   B CB  1 
ATOM   4648 C  CG  . LYS   B 2 256 ? 15.235  70.689 92.510  1.00 51.77 ? 226 LYS   B CG  1 
ATOM   4649 C  CD  . LYS   B 2 256 ? 15.630  70.454 91.083  1.00 57.77 ? 226 LYS   B CD  1 
ATOM   4650 C  CE  . LYS   B 2 256 ? 16.438  71.635 90.599  1.00 62.77 ? 226 LYS   B CE  1 
ATOM   4651 N  NZ  . LYS   B 2 256 ? 15.798  72.925 90.982  1.00 65.44 ? 226 LYS   B NZ  1 
ATOM   4652 N  N   . ILE   B 2 257 ? 13.256  67.843 95.685  1.00 40.86 ? 227 ILE   B N   1 
ATOM   4653 C  CA  . ILE   B 2 257 ? 12.286  66.929 96.273  1.00 39.90 ? 227 ILE   B CA  1 
ATOM   4654 C  C   . ILE   B 2 257 ? 11.557  67.624 97.416  1.00 39.73 ? 227 ILE   B C   1 
ATOM   4655 O  O   . ILE   B 2 257 ? 10.337  67.506 97.516  1.00 40.13 ? 227 ILE   B O   1 
ATOM   4656 C  CB  . ILE   B 2 257 ? 12.983  65.608 96.710  1.00 39.86 ? 227 ILE   B CB  1 
ATOM   4657 C  CG1 . ILE   B 2 257 ? 13.670  64.924 95.510  1.00 40.27 ? 227 ILE   B CG1 1 
ATOM   4658 C  CG2 . ILE   B 2 257 ? 12.036  64.644 97.447  1.00 39.74 ? 227 ILE   B CG2 1 
ATOM   4659 C  CD1 . ILE   B 2 257 ? 12.742  64.592 94.395  1.00 41.25 ? 227 ILE   B CD1 1 
ATOM   4660 N  N   . LEU   B 2 258 ? 12.288  68.401 98.240  1.00 39.08 ? 228 LEU   B N   1 
ATOM   4661 C  CA  . LEU   B 2 258 ? 11.697  69.154 99.338  1.00 39.09 ? 228 LEU   B CA  1 
ATOM   4662 C  C   . LEU   B 2 258 ? 10.830  70.297 98.817  1.00 38.07 ? 228 LEU   B C   1 
ATOM   4663 O  O   . LEU   B 2 258 ? 9.810   70.598 99.427  1.00 38.66 ? 228 LEU   B O   1 
ATOM   4664 C  CB  . LEU   B 2 258 ? 12.777  69.690 100.278 1.00 40.02 ? 228 LEU   B CB  1 
ATOM   4665 C  CG  . LEU   B 2 258 ? 13.481  68.653 101.135 1.00 41.72 ? 228 LEU   B CG  1 
ATOM   4666 C  CD1 . LEU   B 2 258 ? 14.663  69.270 101.835 1.00 42.63 ? 228 LEU   B CD1 1 
ATOM   4667 C  CD2 . LEU   B 2 258 ? 12.530  68.055 102.144 1.00 42.47 ? 228 LEU   B CD2 1 
ATOM   4668 N  N   . GLU   B 2 259 ? 11.183  70.892 97.661  1.00 36.36 ? 229 GLU   B N   1 
ATOM   4669 C  CA  . GLU   B 2 259 ? 10.362  71.922 97.034  1.00 35.49 ? 229 GLU   B CA  1 
ATOM   4670 C  C   . GLU   B 2 259 ? 9.010   71.304 96.634  1.00 34.23 ? 229 GLU   B C   1 
ATOM   4671 O  O   . GLU   B 2 259 ? 7.978   71.918 96.854  1.00 34.37 ? 229 GLU   B O   1 
ATOM   4672 C  CB  . GLU   B 2 259 ? 11.037  72.485 95.764  1.00 37.40 ? 229 GLU   B CB  1 
ATOM   4673 C  CG  . GLU   B 2 259 ? 12.285  73.303 96.007  1.00 41.72 ? 229 GLU   B CG  1 
ATOM   4674 C  CD  . GLU   B 2 259 ? 13.038  73.751 94.765  1.00 48.88 ? 229 GLU   B CD  1 
ATOM   4675 O  OE1 . GLU   B 2 259 ? 12.604  73.415 93.638  1.00 48.65 ? 229 GLU   B OE1 1 
ATOM   4676 O  OE2 . GLU   B 2 259 ? 14.074  74.439 94.926  1.00 51.59 ? 229 GLU   B OE2 1 
ATOM   4677 N  N   . ILE   B 2 260 ? 9.021   70.077 96.093  1.00 32.82 ? 230 ILE   B N   1 
ATOM   4678 C  CA  . ILE   B 2 260 ? 7.796   69.406 95.694  1.00 32.16 ? 230 ILE   B CA  1 
ATOM   4679 C  C   . ILE   B 2 260 ? 6.989   69.008 96.916  1.00 32.09 ? 230 ILE   B C   1 
ATOM   4680 O  O   . ILE   B 2 260 ? 5.789   69.236 96.943  1.00 32.31 ? 230 ILE   B O   1 
ATOM   4681 C  CB  . ILE   B 2 260 ? 8.093   68.214 94.775  1.00 32.13 ? 230 ILE   B CB  1 
ATOM   4682 C  CG1 . ILE   B 2 260 ? 8.946   68.643 93.568  1.00 32.40 ? 230 ILE   B CG1 1 
ATOM   4683 C  CG2 . ILE   B 2 260 ? 6.800   67.559 94.328  1.00 32.55 ? 230 ILE   B CG2 1 
ATOM   4684 C  CD1 . ILE   B 2 260 ? 9.514   67.492 92.814  1.00 33.05 ? 230 ILE   B CD1 1 
ATOM   4685 N  N   . ILE   B 2 261 ? 7.646   68.516 97.974  1.00 31.89 ? 231 ILE   B N   1 
ATOM   4686 C  CA  . ILE   B 2 261 ? 6.966   68.138 99.209  1.00 32.68 ? 231 ILE   B CA  1 
ATOM   4687 C  C   . ILE   B 2 261 ? 6.226   69.328 99.802  1.00 33.79 ? 231 ILE   B C   1 
ATOM   4688 O  O   . ILE   B 2 261 ? 5.058   69.181 100.160 1.00 34.60 ? 231 ILE   B O   1 
ATOM   4689 C  CB  . ILE   B 2 261 ? 7.947   67.478 100.213 1.00 32.99 ? 231 ILE   B CB  1 
ATOM   4690 C  CG1 . ILE   B 2 261 ? 8.343   66.073 99.743  1.00 34.36 ? 231 ILE   B CG1 1 
ATOM   4691 C  CG2 . ILE   B 2 261 ? 7.388   67.448 101.644 1.00 32.93 ? 231 ILE   B CG2 1 
ATOM   4692 C  CD1 . ILE   B 2 261 ? 9.678   65.571 100.341 1.00 35.92 ? 231 ILE   B CD1 1 
ATOM   4693 N  N   . ARG   B 2 262 ? 6.865   70.526 99.806  1.00 33.56 ? 232 ARG   B N   1 
ATOM   4694 C  CA  . ARG   B 2 262 ? 6.248   71.743 100.327 1.00 33.61 ? 232 ARG   B CA  1 
ATOM   4695 C  C   . ARG   B 2 262 ? 5.018   72.124 99.510  1.00 32.38 ? 232 ARG   B C   1 
ATOM   4696 O  O   . ARG   B 2 262 ? 4.032   72.573 100.084 1.00 32.46 ? 232 ARG   B O   1 
ATOM   4697 C  CB  . ARG   B 2 262 ? 7.273   72.898 100.465 1.00 35.96 ? 232 ARG   B CB  1 
ATOM   4698 C  CG  . ARG   B 2 262 ? 8.387   72.567 101.473 1.00 40.47 ? 232 ARG   B CG  1 
ATOM   4699 C  CD  . ARG   B 2 262 ? 9.346   73.711 101.773 1.00 45.07 ? 232 ARG   B CD  1 
ATOM   4700 N  NE  . ARG   B 2 262 ? 10.307  73.954 100.693 1.00 49.78 ? 232 ARG   B NE  1 
ATOM   4701 C  CZ  . ARG   B 2 262 ? 11.594  73.606 100.733 1.00 52.62 ? 232 ARG   B CZ  1 
ATOM   4702 N  NH1 . ARG   B 2 262 ? 12.092  72.995 101.802 1.00 52.47 ? 232 ARG   B NH1 1 
ATOM   4703 N  NH2 . ARG   B 2 262 ? 12.391  73.871 99.704  1.00 52.16 ? 232 ARG   B NH2 1 
ATOM   4704 N  N   . VAL   B 2 263 ? 5.046   71.901 98.186  1.00 31.22 ? 233 VAL   B N   1 
ATOM   4705 C  CA  . VAL   B 2 263 ? 3.873   72.152 97.348  1.00 30.85 ? 233 VAL   B CA  1 
ATOM   4706 C  C   . VAL   B 2 263 ? 2.725   71.180 97.731  1.00 30.53 ? 233 VAL   B C   1 
ATOM   4707 O  O   . VAL   B 2 263 ? 1.590   71.622 97.903  1.00 30.51 ? 233 VAL   B O   1 
ATOM   4708 C  CB  . VAL   B 2 263 ? 4.178   72.136 95.834  1.00 30.88 ? 233 VAL   B CB  1 
ATOM   4709 C  CG1 . VAL   B 2 263 ? 2.900   72.329 95.032  1.00 31.49 ? 233 VAL   B CG1 1 
ATOM   4710 C  CG2 . VAL   B 2 263 ? 5.189   73.217 95.474  1.00 30.79 ? 233 VAL   B CG2 1 
ATOM   4711 N  N   . ILE   B 2 264 ? 3.036   69.887 97.943  1.00 30.18 ? 234 ILE   B N   1 
ATOM   4712 C  CA  . ILE   B 2 264 ? 2.021   68.919 98.360  1.00 31.00 ? 234 ILE   B CA  1 
ATOM   4713 C  C   . ILE   B 2 264 ? 1.417   69.265 99.742  1.00 32.49 ? 234 ILE   B C   1 
ATOM   4714 O  O   . ILE   B 2 264 ? 0.194   69.302 99.879  1.00 32.54 ? 234 ILE   B O   1 
ATOM   4715 C  CB  . ILE   B 2 264 ? 2.535   67.459 98.292  1.00 30.71 ? 234 ILE   B CB  1 
ATOM   4716 C  CG1 . ILE   B 2 264 ? 3.023   67.105 96.867  1.00 30.68 ? 234 ILE   B CG1 1 
ATOM   4717 C  CG2 . ILE   B 2 264 ? 1.446   66.470 98.772  1.00 30.65 ? 234 ILE   B CG2 1 
ATOM   4718 C  CD1 . ILE   B 2 264 ? 3.774   65.816 96.813  1.00 30.93 ? 234 ILE   B CD1 1 
ATOM   4719 N  N   . LEU   B 2 265 ? 2.258   69.595 100.732 1.00 33.56 ? 235 LEU   B N   1 
ATOM   4720 C  CA  . LEU   B 2 265 ? 1.768   69.977 102.060 1.00 35.08 ? 235 LEU   B CA  1 
ATOM   4721 C  C   . LEU   B 2 265 ? 0.889   71.235 101.986 1.00 36.06 ? 235 LEU   B C   1 
ATOM   4722 O  O   . LEU   B 2 265 ? -0.141  71.304 102.652 1.00 36.62 ? 235 LEU   B O   1 
ATOM   4723 C  CB  . LEU   B 2 265 ? 2.943   70.195 103.027 1.00 35.46 ? 235 LEU   B CB  1 
ATOM   4724 C  CG  . LEU   B 2 265 ? 3.838   68.981 103.258 1.00 37.12 ? 235 LEU   B CG  1 
ATOM   4725 C  CD1 . LEU   B 2 265 ? 4.984   69.324 104.203 1.00 37.72 ? 235 LEU   B CD1 1 
ATOM   4726 C  CD2 . LEU   B 2 265 ? 3.050   67.838 103.860 1.00 37.71 ? 235 LEU   B CD2 1 
ATOM   4727 N  N   . LYS   B 2 266 ? 1.263   72.193 101.130 1.00 35.99 ? 236 LYS   B N   1 
ATOM   4728 C  CA  . LYS   B 2 266 ? 0.507   73.428 100.924 1.00 36.21 ? 236 LYS   B CA  1 
ATOM   4729 C  C   . LYS   B 2 266 ? -0.852  73.135 100.280 1.00 35.45 ? 236 LYS   B C   1 
ATOM   4730 O  O   . LYS   B 2 266 ? -1.853  73.768 100.628 1.00 36.78 ? 236 LYS   B O   1 
ATOM   4731 C  CB  . LYS   B 2 266 ? 1.308   74.424 100.060 1.00 38.77 ? 236 LYS   B CB  1 
ATOM   4732 C  CG  . LYS   B 2 266 ? 0.613   75.765 99.888  1.00 44.89 ? 236 LYS   B CG  1 
ATOM   4733 C  CD  . LYS   B 2 266 ? 1.395   76.740 99.018  1.00 51.92 ? 236 LYS   B CD  1 
ATOM   4734 C  CE  . LYS   B 2 266 ? 0.773   78.123 99.060  1.00 57.72 ? 236 LYS   B CE  1 
ATOM   4735 N  NZ  . LYS   B 2 266 ? 1.775   79.198 98.802  1.00 61.29 ? 236 LYS   B NZ  1 
ATOM   4736 N  N   . LEU   B 2 267 ? -0.902  72.178 99.355  1.00 33.54 ? 237 LEU   B N   1 
ATOM   4737 C  CA  . LEU   B 2 267 ? -2.162  71.783 98.721  1.00 32.43 ? 237 LEU   B CA  1 
ATOM   4738 C  C   . LEU   B 2 267 ? -3.136  71.240 99.771  1.00 30.74 ? 237 LEU   B C   1 
ATOM   4739 O  O   . LEU   B 2 267 ? -4.314  71.520 99.678  1.00 30.54 ? 237 LEU   B O   1 
ATOM   4740 C  CB  . LEU   B 2 267 ? -1.930  70.742 97.589  1.00 32.88 ? 237 LEU   B CB  1 
ATOM   4741 C  CG  . LEU   B 2 267 ? -3.149  69.855 97.202  1.00 34.53 ? 237 LEU   B CG  1 
ATOM   4742 C  CD1 . LEU   B 2 267 ? -4.204  70.641 96.403  1.00 34.60 ? 237 LEU   B CD1 1 
ATOM   4743 C  CD2 . LEU   B 2 267 ? -2.717  68.589 96.567  1.00 35.57 ? 237 LEU   B CD2 1 
ATOM   4744 N  N   . TYR   B 2 268 ? -2.653  70.486 100.757 1.00 30.24 ? 238 TYR   B N   1 
ATOM   4745 C  CA  . TYR   B 2 268 ? -3.532  69.928 101.792 1.00 30.30 ? 238 TYR   B CA  1 
ATOM   4746 C  C   . TYR   B 2 268 ? -4.142  70.992 102.677 1.00 30.85 ? 238 TYR   B C   1 
ATOM   4747 O  O   . TYR   B 2 268 ? -5.297  70.855 103.073 1.00 31.45 ? 238 TYR   B O   1 
ATOM   4748 C  CB  . TYR   B 2 268 ? -2.837  68.827 102.604 1.00 29.44 ? 238 TYR   B CB  1 
ATOM   4749 C  CG  . TYR   B 2 268 ? -2.637  67.603 101.750 1.00 29.42 ? 238 TYR   B CG  1 
ATOM   4750 C  CD1 . TYR   B 2 268 ? -3.642  67.157 100.893 1.00 30.45 ? 238 TYR   B CD1 1 
ATOM   4751 C  CD2 . TYR   B 2 268 ? -1.430  66.921 101.749 1.00 29.24 ? 238 TYR   B CD2 1 
ATOM   4752 C  CE1 . TYR   B 2 268 ? -3.441  66.078 100.050 1.00 31.06 ? 238 TYR   B CE1 1 
ATOM   4753 C  CE2 . TYR   B 2 268 ? -1.239  65.804 100.952 1.00 30.18 ? 238 TYR   B CE2 1 
ATOM   4754 C  CZ  . TYR   B 2 268 ? -2.238  65.401 100.081 1.00 31.76 ? 238 TYR   B CZ  1 
ATOM   4755 O  OH  . TYR   B 2 268 ? -2.034  64.344 99.229  1.00 33.25 ? 238 TYR   B OH  1 
ATOM   4756 N  N   . GLU   B 2 269 ? -3.388  72.056 102.954 1.00 30.60 ? 239 GLU   B N   1 
ATOM   4757 C  CA  . GLU   B 2 269 ? -3.871  73.189 103.720 1.00 31.32 ? 239 GLU   B CA  1 
ATOM   4758 C  C   . GLU   B 2 269 ? -4.876  73.984 102.894 1.00 31.89 ? 239 GLU   B C   1 
ATOM   4759 O  O   . GLU   B 2 269 ? -5.918  74.377 103.425 1.00 32.04 ? 239 GLU   B O   1 
ATOM   4760 C  CB  . GLU   B 2 269 ? -2.695  74.074 104.170 1.00 33.54 ? 239 GLU   B CB  1 
ATOM   4761 C  CG  . GLU   B 2 269 ? -1.758  73.348 105.114 1.00 38.07 ? 239 GLU   B CG  1 
ATOM   4762 C  CD  . GLU   B 2 269 ? -2.464  72.801 106.341 1.00 45.39 ? 239 GLU   B CD  1 
ATOM   4763 O  OE1 . GLU   B 2 269 ? -3.232  73.567 106.972 1.00 46.48 ? 239 GLU   B OE1 1 
ATOM   4764 O  OE2 . GLU   B 2 269 ? -2.284  71.597 106.643 1.00 46.38 ? 239 GLU   B OE2 1 
ATOM   4765 N  N   . GLN   B 2 270 ? -4.593  74.182 101.592 1.00 31.66 ? 240 GLN   B N   1 
ATOM   4766 C  CA  . GLN   B 2 270 ? -5.533  74.865 100.705 1.00 32.68 ? 240 GLN   B CA  1 
ATOM   4767 C  C   . GLN   B 2 270 ? -6.820  74.056 100.568 1.00 32.34 ? 240 GLN   B C   1 
ATOM   4768 O  O   . GLN   B 2 270 ? -7.882  74.624 100.651 1.00 33.00 ? 240 GLN   B O   1 
ATOM   4769 C  CB  . GLN   B 2 270 ? -4.928  75.107 99.306  1.00 35.93 ? 240 GLN   B CB  1 
ATOM   4770 C  CG  . GLN   B 2 270 ? -5.913  75.738 98.285  1.00 42.09 ? 240 GLN   B CG  1 
ATOM   4771 C  CD  . GLN   B 2 270 ? -6.279  77.191 98.583  1.00 48.91 ? 240 GLN   B CD  1 
ATOM   4772 O  OE1 . GLN   B 2 270 ? -5.717  78.137 98.000  1.00 51.09 ? 240 GLN   B OE1 1 
ATOM   4773 N  NE2 . GLN   B 2 270 ? -7.244  77.412 99.486  1.00 49.36 ? 240 GLN   B NE2 1 
ATOM   4774 N  N   . TRP   B 2 271 ? -6.722  72.742 100.372 1.00 31.79 ? 241 TRP   B N   1 
ATOM   4775 C  CA  . TRP   B 2 271 ? -7.823  71.777 100.223 1.00 31.03 ? 241 TRP   B CA  1 
ATOM   4776 C  C   . TRP   B 2 271 ? -8.758  71.906 101.432 1.00 31.60 ? 241 TRP   B C   1 
ATOM   4777 O  O   . TRP   B 2 271 ? -9.961  72.105 101.267 1.00 32.24 ? 241 TRP   B O   1 
ATOM   4778 C  CB  . TRP   B 2 271 ? -7.196  70.374 100.173 1.00 29.66 ? 241 TRP   B CB  1 
ATOM   4779 C  CG  . TRP   B 2 271 ? -8.111  69.235 99.887  1.00 28.43 ? 241 TRP   B CG  1 
ATOM   4780 C  CD1 . TRP   B 2 271 ? -9.343  69.000 100.428 1.00 28.63 ? 241 TRP   B CD1 1 
ATOM   4781 C  CD2 . TRP   B 2 271 ? -7.777  68.075 99.130  1.00 28.07 ? 241 TRP   B CD2 1 
ATOM   4782 N  NE1 . TRP   B 2 271 ? -9.820  67.792 99.999  1.00 28.72 ? 241 TRP   B NE1 1 
ATOM   4783 C  CE2 . TRP   B 2 271 ? -8.874  67.197 99.203  1.00 28.65 ? 241 TRP   B CE2 1 
ATOM   4784 C  CE3 . TRP   B 2 271 ? -6.658  67.701 98.378  1.00 28.50 ? 241 TRP   B CE3 1 
ATOM   4785 C  CZ2 . TRP   B 2 271 ? -8.897  65.977 98.526  1.00 29.39 ? 241 TRP   B CZ2 1 
ATOM   4786 C  CZ3 . TRP   B 2 271 ? -6.667  66.478 97.742  1.00 29.64 ? 241 TRP   B CZ3 1 
ATOM   4787 C  CH2 . TRP   B 2 271 ? -7.787  65.640 97.799  1.00 29.67 ? 241 TRP   B CH2 1 
ATOM   4788 N  N   . LYS   B 2 272 ? -8.177  71.891 102.634 1.00 31.45 ? 242 LYS   B N   1 
ATOM   4789 C  CA  . LYS   B 2 272 ? -8.873  72.056 103.889 1.00 32.44 ? 242 LYS   B CA  1 
ATOM   4790 C  C   . LYS   B 2 272 ? -9.654  73.369 103.921 1.00 34.18 ? 242 LYS   B C   1 
ATOM   4791 O  O   . LYS   B 2 272 ? -10.835 73.364 104.273 1.00 35.61 ? 242 LYS   B O   1 
ATOM   4792 C  CB  . LYS   B 2 272 ? -7.846  72.009 105.034 1.00 33.32 ? 242 LYS   B CB  1 
ATOM   4793 C  CG  . LYS   B 2 272 ? -8.310  72.575 106.371 1.00 35.68 ? 242 LYS   B CG  1 
ATOM   4794 C  CD  . LYS   B 2 272 ? -7.122  72.886 107.211 1.00 38.32 ? 242 LYS   B CD  1 
ATOM   4795 C  CE  . LYS   B 2 272 ? -7.521  73.600 108.455 1.00 41.69 ? 242 LYS   B CE  1 
ATOM   4796 N  NZ  . LYS   B 2 272 ? -6.335  74.226 109.108 1.00 43.97 ? 242 LYS   B NZ  1 
ATOM   4797 N  N   . ASN   B 2 273 ? -9.008  74.485 103.565 1.00 33.80 ? 243 ASN   B N   1 
ATOM   4798 C  CA  . ASN   B 2 273 ? -9.642  75.796 103.640 1.00 33.80 ? 243 ASN   B CA  1 
ATOM   4799 C  C   . ASN   B 2 273 ? -10.533 76.159 102.468 1.00 34.94 ? 243 ASN   B C   1 
ATOM   4800 O  O   . ASN   B 2 273 ? -11.263 77.134 102.545 1.00 36.09 ? 243 ASN   B O   1 
ATOM   4801 C  CB  . ASN   B 2 273 ? -8.590  76.871 103.839 1.00 34.02 ? 243 ASN   B CB  1 
ATOM   4802 C  CG  . ASN   B 2 273 ? -7.838  76.705 105.131 1.00 37.28 ? 243 ASN   B CG  1 
ATOM   4803 O  OD1 . ASN   B 2 273 ? -6.610  76.805 105.168 1.00 38.89 ? 243 ASN   B OD1 1 
ATOM   4804 N  ND2 . ASN   B 2 273 ? -8.550  76.422 106.220 1.00 37.25 ? 243 ASN   B ND2 1 
ATOM   4805 N  N   . PHE   B 2 274 ? -10.487 75.396 101.401 1.00 34.26 ? 244 PHE   B N   1 
ATOM   4806 C  CA  . PHE   B 2 274 ? -11.244 75.657 100.204 1.00 34.05 ? 244 PHE   B CA  1 
ATOM   4807 C  C   . PHE   B 2 274 ? -12.538 74.860 100.204 1.00 35.11 ? 244 PHE   B C   1 
ATOM   4808 O  O   . PHE   B 2 274 ? -12.483 73.652 100.404 1.00 35.63 ? 244 PHE   B O   1 
ATOM   4809 C  CB  . PHE   B 2 274 ? -10.364 75.209 99.017  1.00 33.00 ? 244 PHE   B CB  1 
ATOM   4810 C  CG  . PHE   B 2 274 ? -10.955 75.251 97.634  1.00 32.93 ? 244 PHE   B CG  1 
ATOM   4811 C  CD1 . PHE   B 2 274 ? -11.809 76.270 97.259  1.00 33.31 ? 244 PHE   B CD1 1 
ATOM   4812 C  CD2 . PHE   B 2 274 ? -10.594 74.316 96.684  1.00 33.55 ? 244 PHE   B CD2 1 
ATOM   4813 C  CE1 . PHE   B 2 274 ? -12.336 76.319 95.982  1.00 34.03 ? 244 PHE   B CE1 1 
ATOM   4814 C  CE2 . PHE   B 2 274 ? -11.112 74.373 95.404  1.00 34.37 ? 244 PHE   B CE2 1 
ATOM   4815 C  CZ  . PHE   B 2 274 ? -11.971 75.383 95.053  1.00 33.92 ? 244 PHE   B CZ  1 
ATOM   4816 N  N   . ASP   B 2 275 ? -13.688 75.508 99.952  1.00 35.14 ? 245 ASP   B N   1 
ATOM   4817 C  CA  . ASP   B 2 275 ? -14.910 74.766 99.719  1.00 36.02 ? 245 ASP   B CA  1 
ATOM   4818 C  C   . ASP   B 2 275 ? -15.322 75.075 98.308  1.00 35.83 ? 245 ASP   B C   1 
ATOM   4819 O  O   . ASP   B 2 275 ? -16.014 76.053 98.038  1.00 36.37 ? 245 ASP   B O   1 
ATOM   4820 C  CB  . ASP   B 2 275 ? -16.062 75.041 100.691 1.00 39.08 ? 245 ASP   B CB  1 
ATOM   4821 C  CG  . ASP   B 2 275 ? -17.180 74.003 100.554 1.00 45.29 ? 245 ASP   B CG  1 
ATOM   4822 O  OD1 . ASP   B 2 275 ? -17.326 73.416 99.455  1.00 45.08 ? 245 ASP   B OD1 1 
ATOM   4823 O  OD2 . ASP   B 2 275 ? -17.892 73.753 101.557 1.00 50.01 ? 245 ASP   B OD2 1 
ATOM   4824 N  N   . GLU   B 2 276 ? -14.935 74.193 97.425  1.00 34.91 ? 246 GLU   B N   1 
ATOM   4825 C  CA  . GLU   B 2 276 ? -15.177 74.242 95.999  1.00 34.58 ? 246 GLU   B CA  1 
ATOM   4826 C  C   . GLU   B 2 276 ? -16.634 74.375 95.638  1.00 33.06 ? 246 GLU   B C   1 
ATOM   4827 O  O   . GLU   B 2 276 ? -16.973 75.103 94.710  1.00 33.00 ? 246 GLU   B O   1 
ATOM   4828 C  CB  . GLU   B 2 276 ? -14.547 72.971 95.418  1.00 37.96 ? 246 GLU   B CB  1 
ATOM   4829 C  CG  . GLU   B 2 276 ? -14.901 72.562 94.009  1.00 44.03 ? 246 GLU   B CG  1 
ATOM   4830 C  CD  . GLU   B 2 276 ? -14.263 71.222 93.698  1.00 50.95 ? 246 GLU   B CD  1 
ATOM   4831 O  OE1 . GLU   B 2 276 ? -14.237 70.354 94.600  1.00 53.42 ? 246 GLU   B OE1 1 
ATOM   4832 O  OE2 . GLU   B 2 276 ? -13.768 71.043 92.564  1.00 52.67 ? 246 GLU   B OE2 1 
ATOM   4833 N  N   A ARG   B 2 277 ? -17.511 73.697 96.377  0.50 32.43 ? 247 ARG   B N   1 
ATOM   4834 N  N   B ARG   B 2 277 ? -17.504 73.690 96.375  0.50 32.51 ? 247 ARG   B N   1 
ATOM   4835 C  CA  A ARG   B 2 277 ? -18.941 73.747 96.089  0.50 32.20 ? 247 ARG   B CA  1 
ATOM   4836 C  CA  B ARG   B 2 277 ? -18.937 73.736 96.112  0.50 32.37 ? 247 ARG   B CA  1 
ATOM   4837 C  C   A ARG   B 2 277 ? -19.567 75.086 96.474  0.50 32.39 ? 247 ARG   B C   1 
ATOM   4838 C  C   B ARG   B 2 277 ? -19.549 75.090 96.465  0.50 32.47 ? 247 ARG   B C   1 
ATOM   4839 O  O   A ARG   B 2 277 ? -20.456 75.565 95.774  0.50 32.24 ? 247 ARG   B O   1 
ATOM   4840 O  O   B ARG   B 2 277 ? -20.426 75.572 95.752  0.50 32.31 ? 247 ARG   B O   1 
ATOM   4841 C  CB  A ARG   B 2 277 ? -19.665 72.555 96.707  0.50 32.47 ? 247 ARG   B CB  1 
ATOM   4842 C  CB  B ARG   B 2 277 ? -19.651 72.587 96.828  0.50 32.83 ? 247 ARG   B CB  1 
ATOM   4843 C  CG  A ARG   B 2 277 ? -19.103 71.257 96.175  0.50 33.55 ? 247 ARG   B CG  1 
ATOM   4844 C  CG  B ARG   B 2 277 ? -19.354 71.241 96.199  0.50 34.21 ? 247 ARG   B CG  1 
ATOM   4845 C  CD  A ARG   B 2 277 ? -19.837 70.037 96.654  0.50 34.78 ? 247 ARG   B CD  1 
ATOM   4846 C  CD  B ARG   B 2 277 ? -19.400 70.081 97.176  0.50 35.97 ? 247 ARG   B CD  1 
ATOM   4847 N  NE  A ARG   B 2 277 ? -19.429 68.854 95.896  0.50 35.26 ? 247 ARG   B NE  1 
ATOM   4848 N  NE  B ARG   B 2 277 ? -18.495 70.254 98.310  0.50 37.57 ? 247 ARG   B NE  1 
ATOM   4849 C  CZ  A ARG   B 2 277 ? -20.256 68.081 95.204  0.50 34.80 ? 247 ARG   B CZ  1 
ATOM   4850 C  CZ  B ARG   B 2 277 ? -17.193 69.983 98.285  0.50 39.96 ? 247 ARG   B CZ  1 
ATOM   4851 N  NH1 A ARG   B 2 277 ? -21.558 68.343 95.181  0.50 33.53 ? 247 ARG   B NH1 1 
ATOM   4852 N  NH1 B ARG   B 2 277 ? -16.620 69.545 97.169  0.50 38.95 ? 247 ARG   B NH1 1 
ATOM   4853 N  NH2 A ARG   B 2 277 ? -19.792 67.037 94.534  0.50 33.95 ? 247 ARG   B NH2 1 
ATOM   4854 N  NH2 B ARG   B 2 277 ? -16.449 70.172 99.367  0.50 40.19 ? 247 ARG   B NH2 1 
ATOM   4855 N  N   . LYS   B 2 278 ? -19.058 75.724 97.536  1.00 32.44 ? 248 LYS   B N   1 
ATOM   4856 C  CA  . LYS   B 2 278 ? -19.562 77.026 97.938  1.00 32.71 ? 248 LYS   B CA  1 
ATOM   4857 C  C   . LYS   B 2 278 ? -18.928 78.155 97.119  1.00 32.90 ? 248 LYS   B C   1 
ATOM   4858 O  O   . LYS   B 2 278 ? -19.595 79.149 96.852  1.00 32.91 ? 248 LYS   B O   1 
ATOM   4859 C  CB  . LYS   B 2 278 ? -19.354 77.250 99.435  1.00 34.30 ? 248 LYS   B CB  1 
ATOM   4860 C  CG  . LYS   B 2 278 ? -20.190 76.286 100.290 1.00 38.76 ? 248 LYS   B CG  1 
ATOM   4861 C  CD  . LYS   B 2 278 ? -19.782 76.330 101.749 1.00 43.50 ? 248 LYS   B CD  1 
ATOM   4862 C  CE  . LYS   B 2 278 ? -20.809 75.665 102.632 1.00 48.44 ? 248 LYS   B CE  1 
ATOM   4863 N  NZ  . LYS   B 2 278 ? -20.189 75.021 103.818 1.00 51.41 ? 248 LYS   B NZ  1 
ATOM   4864 N  N   . GLU   B 2 279 ? -17.663 77.991 96.676  1.00 32.40 ? 249 GLU   B N   1 
ATOM   4865 C  CA  . GLU   B 2 279 ? -16.963 79.079 96.006  1.00 32.10 ? 249 GLU   B CA  1 
ATOM   4866 C  C   . GLU   B 2 279 ? -16.907 79.101 94.481  1.00 32.33 ? 249 GLU   B C   1 
ATOM   4867 O  O   . GLU   B 2 279 ? -16.645 80.180 93.944  1.00 32.73 ? 249 GLU   B O   1 
ATOM   4868 C  CB  . GLU   B 2 279 ? -15.521 79.138 96.505  1.00 33.00 ? 249 GLU   B CB  1 
ATOM   4869 C  CG  . GLU   B 2 279 ? -15.390 79.259 98.009  1.00 38.01 ? 249 GLU   B CG  1 
ATOM   4870 C  CD  . GLU   B 2 279 ? -13.947 79.227 98.474  1.00 42.91 ? 249 GLU   B CD  1 
ATOM   4871 O  OE1 . GLU   B 2 279 ? -13.088 79.786 97.755  1.00 42.81 ? 249 GLU   B OE1 1 
ATOM   4872 O  OE2 . GLU   B 2 279 ? -13.670 78.630 99.540  1.00 45.11 ? 249 GLU   B OE2 1 
ATOM   4873 N  N   . MET   B 2 280 ? -17.044 77.960 93.786  1.00 32.03 ? 250 MET   B N   1 
ATOM   4874 C  CA  . MET   B 2 280 ? -16.790 77.940 92.348  1.00 32.30 ? 250 MET   B CA  1 
ATOM   4875 C  C   . MET   B 2 280 ? -17.732 78.735 91.465  1.00 32.87 ? 250 MET   B C   1 
ATOM   4876 O  O   . MET   B 2 280 ? -17.260 79.218 90.439  1.00 32.65 ? 250 MET   B O   1 
ATOM   4877 C  CB  . MET   B 2 280 ? -16.650 76.529 91.782  1.00 32.80 ? 250 MET   B CB  1 
ATOM   4878 C  CG  . MET   B 2 280 ? -15.371 75.812 92.209  1.00 33.61 ? 250 MET   B CG  1 
ATOM   4879 S  SD  . MET   B 2 280 ? -13.842 76.755 92.102  1.00 36.31 ? 250 MET   B SD  1 
ATOM   4880 C  CE  . MET   B 2 280 ? -13.926 77.281 90.382  1.00 27.38 ? 250 MET   B CE  1 
ATOM   4881 N  N   . ALA   B 2 281 ? -19.015 78.898 91.818  1.00 33.62 ? 251 ALA   B N   1 
ATOM   4882 C  CA  . ALA   B 2 281 ? -19.916 79.693 90.958  1.00 34.30 ? 251 ALA   B CA  1 
ATOM   4883 C  C   . ALA   B 2 281 ? -19.475 81.160 90.924  1.00 35.28 ? 251 ALA   B C   1 
ATOM   4884 O  O   . ALA   B 2 281 ? -19.556 81.789 89.872  1.00 36.00 ? 251 ALA   B O   1 
ATOM   4885 C  CB  . ALA   B 2 281 ? -21.353 79.571 91.417  1.00 34.11 ? 251 ALA   B CB  1 
ATOM   4886 N  N   . THR   B 2 282 ? -18.916 81.675 92.039  1.00 35.30 ? 252 THR   B N   1 
ATOM   4887 C  CA  . THR   B 2 282 ? -18.411 83.043 92.122  1.00 35.87 ? 252 THR   B CA  1 
ATOM   4888 C  C   . THR   B 2 282 ? -17.089 83.177 91.388  1.00 35.95 ? 252 THR   B C   1 
ATOM   4889 O  O   . THR   B 2 282 ? -16.903 84.149 90.659  1.00 37.25 ? 252 THR   B O   1 
ATOM   4890 C  CB  . THR   B 2 282 ? -18.227 83.468 93.576  1.00 37.72 ? 252 THR   B CB  1 
ATOM   4891 O  OG1 . THR   B 2 282 ? -19.420 83.182 94.301  1.00 39.44 ? 252 THR   B OG1 1 
ATOM   4892 C  CG2 . THR   B 2 282 ? -17.858 84.932 93.705  1.00 37.79 ? 252 THR   B CG2 1 
ATOM   4893 N  N   . ILE   B 2 283 ? -16.173 82.213 91.559  1.00 34.69 ? 253 ILE   B N   1 
ATOM   4894 C  CA  . ILE   B 2 283 ? -14.875 82.233 90.883  1.00 33.75 ? 253 ILE   B CA  1 
ATOM   4895 C  C   . ILE   B 2 283 ? -15.031 82.119 89.366  1.00 33.76 ? 253 ILE   B C   1 
ATOM   4896 O  O   . ILE   B 2 283 ? -14.363 82.846 88.624  1.00 33.98 ? 253 ILE   B O   1 
ATOM   4897 C  CB  . ILE   B 2 283 ? -13.941 81.151 91.465  1.00 33.32 ? 253 ILE   B CB  1 
ATOM   4898 C  CG1 . ILE   B 2 283 ? -13.697 81.403 92.974  1.00 33.61 ? 253 ILE   B CG1 1 
ATOM   4899 C  CG2 . ILE   B 2 283 ? -12.634 81.065 90.669  1.00 33.13 ? 253 ILE   B CG2 1 
ATOM   4900 C  CD1 . ILE   B 2 283 ? -12.781 80.426 93.674  1.00 34.06 ? 253 ILE   B CD1 1 
ATOM   4901 N  N   . LEU   B 2 284 ? -15.950 81.263 88.902  1.00 33.43 ? 254 LEU   B N   1 
ATOM   4902 C  CA  . LEU   B 2 284 ? -16.188 81.116 87.473  1.00 34.28 ? 254 LEU   B CA  1 
ATOM   4903 C  C   . LEU   B 2 284 ? -16.768 82.407 86.879  1.00 35.90 ? 254 LEU   B C   1 
ATOM   4904 O  O   . LEU   B 2 284 ? -16.471 82.706 85.732  1.00 36.24 ? 254 LEU   B O   1 
ATOM   4905 C  CB  . LEU   B 2 284 ? -17.088 79.906 87.159  1.00 34.17 ? 254 LEU   B CB  1 
ATOM   4906 C  CG  . LEU   B 2 284 ? -16.458 78.518 87.292  1.00 35.20 ? 254 LEU   B CG  1 
ATOM   4907 C  CD1 . LEU   B 2 284 ? -17.518 77.452 87.430  1.00 35.60 ? 254 LEU   B CD1 1 
ATOM   4908 C  CD2 . LEU   B 2 284 ? -15.568 78.196 86.113  1.00 35.45 ? 254 LEU   B CD2 1 
ATOM   4909 N  N   . SER   B 2 285 ? -17.563 83.190 87.657  1.00 36.97 ? 255 SER   B N   1 
ATOM   4910 C  CA  . SER   B 2 285 ? -18.113 84.466 87.181  1.00 38.25 ? 255 SER   B CA  1 
ATOM   4911 C  C   . SER   B 2 285 ? -17.032 85.538 87.051  1.00 39.50 ? 255 SER   B C   1 
ATOM   4912 O  O   . SER   B 2 285 ? -17.134 86.391 86.172  1.00 40.71 ? 255 SER   B O   1 
ATOM   4913 C  CB  . SER   B 2 285 ? -19.245 84.960 88.075  1.00 40.21 ? 255 SER   B CB  1 
ATOM   4914 O  OG  . SER   B 2 285 ? -18.751 85.404 89.328  1.00 44.13 ? 255 SER   B OG  1 
ATOM   4915 N  N   . LYS   B 2 286 ? -16.002 85.502 87.897  1.00 39.31 ? 256 LYS   B N   1 
ATOM   4916 C  CA  . LYS   B 2 286 ? -14.902 86.466 87.804  1.00 40.27 ? 256 LYS   B CA  1 
ATOM   4917 C  C   . LYS   B 2 286 ? -13.940 86.167 86.646  1.00 41.68 ? 256 LYS   B C   1 
ATOM   4918 O  O   . LYS   B 2 286 ? -13.202 87.046 86.228  1.00 42.38 ? 256 LYS   B O   1 
ATOM   4919 C  CB  . LYS   B 2 286 ? -14.094 86.504 89.107  1.00 41.84 ? 256 LYS   B CB  1 
ATOM   4920 C  CG  . LYS   B 2 286 ? -14.884 86.956 90.324  1.00 45.50 ? 256 LYS   B CG  1 
ATOM   4921 C  CD  . LYS   B 2 286 ? -13.972 87.078 91.533  1.00 49.34 ? 256 LYS   B CD  1 
ATOM   4922 C  CE  . LYS   B 2 286 ? -14.721 87.617 92.721  1.00 53.07 ? 256 LYS   B CE  1 
ATOM   4923 N  NZ  . LYS   B 2 286 ? -13.831 87.802 93.895  1.00 55.34 ? 256 LYS   B NZ  1 
ATOM   4924 N  N   . MET   B 2 287 ? -13.906 84.926 86.178  1.00 42.18 ? 257 MET   B N   1 
ATOM   4925 C  CA  . MET   B 2 287 ? -13.014 84.426 85.138  1.00 43.18 ? 257 MET   B CA  1 
ATOM   4926 C  C   . MET   B 2 287 ? -13.254 85.140 83.808  1.00 44.68 ? 257 MET   B C   1 
ATOM   4927 O  O   . MET   B 2 287 ? -14.407 85.307 83.406  1.00 45.20 ? 257 MET   B O   1 
ATOM   4928 C  CB  . MET   B 2 287 ? -13.235 82.899 85.020  1.00 43.32 ? 257 MET   B CB  1 
ATOM   4929 C  CG  . MET   B 2 287 ? -12.512 82.224 83.889  1.00 44.88 ? 257 MET   B CG  1 
ATOM   4930 S  SD  . MET   B 2 287 ? -12.917 80.449 83.805  1.00 43.89 ? 257 MET   B SD  1 
ATOM   4931 C  CE  . MET   B 2 287 ? -14.614 80.538 83.352  1.00 44.27 ? 257 MET   B CE  1 
ATOM   4932 N  N   . PRO   B 2 288 ? -12.179 85.595 83.123  1.00 45.07 ? 258 PRO   B N   1 
ATOM   4933 C  CA  . PRO   B 2 288 ? -12.361 86.253 81.820  1.00 46.09 ? 258 PRO   B CA  1 
ATOM   4934 C  C   . PRO   B 2 288 ? -13.079 85.364 80.812  1.00 47.98 ? 258 PRO   B C   1 
ATOM   4935 O  O   . PRO   B 2 288 ? -12.733 84.195 80.673  1.00 48.02 ? 258 PRO   B O   1 
ATOM   4936 C  CB  . PRO   B 2 288 ? -10.925 86.554 81.370  1.00 46.12 ? 258 PRO   B CB  1 
ATOM   4937 C  CG  . PRO   B 2 288 ? -10.070 85.669 82.159  1.00 46.04 ? 258 PRO   B CG  1 
ATOM   4938 C  CD  . PRO   B 2 288 ? -10.753 85.485 83.472  1.00 44.42 ? 258 PRO   B CD  1 
ATOM   4939 N  N   . LYS   B 2 289 ? -14.110 85.897 80.147  1.00 49.34 ? 259 LYS   B N   1 
ATOM   4940 C  CA  . LYS   B 2 289 ? -14.884 85.115 79.175  1.00 51.23 ? 259 LYS   B CA  1 
ATOM   4941 C  C   . LYS   B 2 289 ? -14.505 85.437 77.725  1.00 53.30 ? 259 LYS   B C   1 
ATOM   4942 O  O   . LYS   B 2 289 ? -14.081 86.553 77.431  1.00 53.46 ? 259 LYS   B O   1 
ATOM   4943 C  CB  . LYS   B 2 289 ? -16.398 85.318 79.394  1.00 52.29 ? 259 LYS   B CB  1 
ATOM   4944 C  CG  . LYS   B 2 289 ? -16.860 85.046 80.818  1.00 54.95 ? 259 LYS   B CG  1 
ATOM   4945 C  CD  . LYS   B 2 289 ? -16.572 83.618 81.296  1.00 57.63 ? 259 LYS   B CD  1 
ATOM   4946 C  CE  . LYS   B 2 289 ? -17.296 83.311 82.583  1.00 59.21 ? 259 LYS   B CE  1 
ATOM   4947 N  NZ  . LYS   B 2 289 ? -17.097 84.386 83.598  1.00 60.31 ? 259 LYS   B NZ  1 
ATOM   4948 N  N   . PRO   B 2 290 ? -14.631 84.460 76.805  1.00 54.89 ? 260 PRO   B N   1 
ATOM   4949 C  CA  . PRO   B 2 290 ? -14.277 84.723 75.400  1.00 56.12 ? 260 PRO   B CA  1 
ATOM   4950 C  C   . PRO   B 2 290 ? -15.068 85.868 74.797  1.00 57.89 ? 260 PRO   B C   1 
ATOM   4951 O  O   . PRO   B 2 290 ? -16.283 85.923 74.974  1.00 58.49 ? 260 PRO   B O   1 
ATOM   4952 C  CB  . PRO   B 2 290 ? -14.628 83.403 74.693  1.00 56.46 ? 260 PRO   B CB  1 
ATOM   4953 C  CG  . PRO   B 2 290 ? -14.629 82.361 75.758  1.00 56.40 ? 260 PRO   B CG  1 
ATOM   4954 C  CD  . PRO   B 2 290 ? -15.095 83.069 76.995  1.00 54.73 ? 260 PRO   B CD  1 
ATOM   4955 N  N   . LYS   B 2 291 ? -14.379 86.788 74.115  1.00 58.58 ? 261 LYS   B N   1 
ATOM   4956 C  CA  . LYS   B 2 291 ? -14.998 87.938 73.463  1.00 59.81 ? 261 LYS   B CA  1 
ATOM   4957 C  C   . LYS   B 2 291 ? -15.650 87.490 72.155  1.00 61.02 ? 261 LYS   B C   1 
ATOM   4958 O  O   . LYS   B 2 291 ? -15.008 86.848 71.325  1.00 60.88 ? 261 LYS   B O   1 
ATOM   4959 C  CB  . LYS   B 2 291 ? -13.939 89.029 73.192  1.00 61.54 ? 261 LYS   B CB  1 
ATOM   4960 C  CG  . LYS   B 2 291 ? -14.415 90.196 72.334  1.00 65.57 ? 261 LYS   B CG  1 
ATOM   4961 C  CD  . LYS   B 2 291 ? -13.249 91.044 71.815  1.00 69.83 ? 261 LYS   B CD  1 
ATOM   4962 C  CE  . LYS   B 2 291 ? -12.720 92.000 72.860  1.00 73.63 ? 261 LYS   B CE  1 
ATOM   4963 N  NZ  . LYS   B 2 291 ? -11.688 92.925 72.305  1.00 75.74 ? 261 LYS   B NZ  1 
ATOM   4964 N  N   . PRO   B 2 292 ? -16.935 87.824 71.957  1.00 62.17 ? 262 PRO   B N   1 
ATOM   4965 C  CA  . PRO   B 2 292 ? -17.618 87.435 70.713  1.00 62.70 ? 262 PRO   B CA  1 
ATOM   4966 C  C   . PRO   B 2 292 ? -17.150 88.238 69.495  1.00 62.98 ? 262 PRO   B C   1 
ATOM   4967 O  O   . PRO   B 2 292 ? -16.597 89.329 69.635  1.00 62.91 ? 262 PRO   B O   1 
ATOM   4968 C  CB  . PRO   B 2 292 ? -19.090 87.723 71.030  1.00 63.55 ? 262 PRO   B CB  1 
ATOM   4969 C  CG  . PRO   B 2 292 ? -19.034 88.869 71.973  1.00 64.06 ? 262 PRO   B CG  1 
ATOM   4970 C  CD  . PRO   B 2 292 ? -17.831 88.588 72.848  1.00 62.26 ? 262 PRO   B CD  1 
ATOM   4971 N  N   . PRO   B 2 293 ? -17.349 87.699 68.282  1.00 63.20 ? 263 PRO   B N   1 
ATOM   4972 C  CA  . PRO   B 2 293 ? -16.922 88.436 67.075  1.00 63.78 ? 263 PRO   B CA  1 
ATOM   4973 C  C   . PRO   B 2 293 ? -17.738 89.713 66.834  1.00 64.84 ? 263 PRO   B C   1 
ATOM   4974 O  O   . PRO   B 2 293 ? -18.870 89.802 67.301  1.00 65.19 ? 263 PRO   B O   1 
ATOM   4975 C  CB  . PRO   B 2 293 ? -17.117 87.412 65.950  1.00 64.27 ? 263 PRO   B CB  1 
ATOM   4976 C  CG  . PRO   B 2 293 ? -18.127 86.462 66.465  1.00 64.39 ? 263 PRO   B CG  1 
ATOM   4977 C  CD  . PRO   B 2 293 ? -17.969 86.402 67.949  1.00 62.52 ? 263 PRO   B CD  1 
ATOM   4978 N  N   . PRO   B 2 294 ? -17.198 90.719 66.114  1.00 65.35 ? 264 PRO   B N   1 
ATOM   4979 C  CA  . PRO   B 2 294 ? -17.966 91.962 65.894  1.00 65.97 ? 264 PRO   B CA  1 
ATOM   4980 C  C   . PRO   B 2 294 ? -19.278 91.819 65.111  1.00 66.66 ? 264 PRO   B C   1 
ATOM   4981 O  O   . PRO   B 2 294 ? -19.489 90.846 64.387  1.00 67.12 ? 264 PRO   B O   1 
ATOM   4982 C  CB  . PRO   B 2 294 ? -16.973 92.874 65.163  1.00 66.51 ? 264 PRO   B CB  1 
ATOM   4983 C  CG  . PRO   B 2 294 ? -15.966 91.961 64.565  1.00 66.71 ? 264 PRO   B CG  1 
ATOM   4984 C  CD  . PRO   B 2 294 ? -15.858 90.796 65.503  1.00 64.98 ? 264 PRO   B CD  1 
HETATM 4985 CL CL  . CL    C 3 .   ? 11.402  27.437 62.346  1.00 67.72 ? 501 CL    A CL  1 
HETATM 4986 C  C1  . EDO   D 4 .   ? 18.732  62.175 63.995  1.00 56.36 ? 502 EDO   A C1  1 
HETATM 4987 O  O1  . EDO   D 4 .   ? 19.942  61.496 64.279  1.00 56.56 ? 502 EDO   A O1  1 
HETATM 4988 C  C2  . EDO   D 4 .   ? 18.313  61.951 62.564  1.00 56.19 ? 502 EDO   A C2  1 
HETATM 4989 O  O2  . EDO   D 4 .   ? 16.906  62.132 62.456  1.00 56.05 ? 502 EDO   A O2  1 
HETATM 4990 C  C1  . EDO   E 4 .   ? -11.955 72.926 62.688  1.00 73.71 ? 503 EDO   A C1  1 
HETATM 4991 O  O1  . EDO   E 4 .   ? -13.198 72.654 62.066  1.00 73.84 ? 503 EDO   A O1  1 
HETATM 4992 C  C2  . EDO   E 4 .   ? -11.883 74.388 63.027  1.00 73.75 ? 503 EDO   A C2  1 
HETATM 4993 O  O2  . EDO   E 4 .   ? -11.040 74.586 64.152  1.00 73.75 ? 503 EDO   A O2  1 
HETATM 4994 C  C1  . EDO   F 4 .   ? -7.541  16.929 59.600  1.00 61.90 ? 504 EDO   A C1  1 
HETATM 4995 O  O1  . EDO   F 4 .   ? -6.584  17.078 60.642  1.00 61.88 ? 504 EDO   A O1  1 
HETATM 4996 C  C2  . EDO   F 4 .   ? -6.837  16.717 58.280  1.00 61.75 ? 504 EDO   A C2  1 
HETATM 4997 O  O2  . EDO   F 4 .   ? -5.797  17.668 58.117  1.00 61.50 ? 504 EDO   A O2  1 
HETATM 4998 C  C1  . EDO   G 4 .   ? -1.437  58.380 58.494  1.00 53.36 ? 505 EDO   A C1  1 
HETATM 4999 O  O1  . EDO   G 4 .   ? -0.824  59.079 57.428  1.00 53.29 ? 505 EDO   A O1  1 
HETATM 5000 C  C2  . EDO   G 4 .   ? -0.377  57.841 59.394  1.00 53.49 ? 505 EDO   A C2  1 
HETATM 5001 O  O2  . EDO   G 4 .   ? 0.501   56.971 58.698  1.00 53.43 ? 505 EDO   A O2  1 
HETATM 5002 C  C1  . EDO   H 4 .   ? 28.411  46.731 61.387  1.00 60.91 ? 506 EDO   A C1  1 
HETATM 5003 O  O1  . EDO   H 4 .   ? 28.537  48.135 61.200  1.00 61.14 ? 506 EDO   A O1  1 
HETATM 5004 C  C2  . EDO   H 4 .   ? 29.521  46.200 62.251  1.00 60.70 ? 506 EDO   A C2  1 
HETATM 5005 O  O2  . EDO   H 4 .   ? 28.936  45.494 63.336  1.00 60.55 ? 506 EDO   A O2  1 
HETATM 5006 C  C1  . EDO   I 4 .   ? 12.406  64.932 69.499  1.00 57.56 ? 507 EDO   A C1  1 
HETATM 5007 O  O1  . EDO   I 4 .   ? 13.814  64.872 69.657  1.00 57.84 ? 507 EDO   A O1  1 
HETATM 5008 C  C2  . EDO   I 4 .   ? 11.751  65.019 70.853  1.00 57.26 ? 507 EDO   A C2  1 
HETATM 5009 O  O2  . EDO   I 4 .   ? 10.670  65.931 70.799  1.00 57.13 ? 507 EDO   A O2  1 
HETATM 5010 C  C1  . GOL   J 5 .   ? 1.274   49.694 45.843  1.00 73.12 ? 508 GOL   A C1  1 
HETATM 5011 O  O1  . GOL   J 5 .   ? 0.457   48.529 45.839  1.00 73.29 ? 508 GOL   A O1  1 
HETATM 5012 C  C2  . GOL   J 5 .   ? 2.488   49.508 46.727  1.00 72.79 ? 508 GOL   A C2  1 
HETATM 5013 O  O2  . GOL   J 5 .   ? 2.079   49.288 48.079  1.00 72.67 ? 508 GOL   A O2  1 
HETATM 5014 C  C3  . GOL   J 5 .   ? 3.440   50.682 46.658  1.00 72.61 ? 508 GOL   A C3  1 
HETATM 5015 O  O3  . GOL   J 5 .   ? 3.862   50.920 45.321  1.00 72.61 ? 508 GOL   A O3  1 
HETATM 5016 N  N1  . A1ITF K 6 .   ? 3.161   53.984 53.899  1.00 28.78 ? 509 A1ITF A N1  1 
HETATM 5017 N  N3  . A1ITF K 6 .   ? 7.975   59.537 51.045  1.00 29.59 ? 509 A1ITF A N3  1 
HETATM 5018 C  C4  . A1ITF K 6 .   ? 5.968   55.210 50.062  1.00 30.50 ? 509 A1ITF A C4  1 
HETATM 5019 C  C5  . A1ITF K 6 .   ? 5.274   53.757 48.228  1.00 30.76 ? 509 A1ITF A C5  1 
HETATM 5020 C  C6  . A1ITF K 6 .   ? 4.139   53.564 50.403  1.00 29.61 ? 509 A1ITF A C6  1 
HETATM 5021 C  C7  . A1ITF K 6 .   ? 3.906   54.067 51.801  1.00 29.31 ? 509 A1ITF A C7  1 
HETATM 5022 C  C8  . A1ITF K 6 .   ? 3.454   53.226 52.808  1.00 29.12 ? 509 A1ITF A C8  1 
HETATM 5023 C  C10 . A1ITF K 6 .   ? 3.910   55.377 52.348  1.00 29.11 ? 509 A1ITF A C10 1 
HETATM 5024 C  C13 . A1ITF K 6 .   ? 7.451   58.246 49.092  1.00 30.04 ? 509 A1ITF A C13 1 
HETATM 5025 C  C15 . A1ITF K 6 .   ? 6.981   58.865 51.653  1.00 29.43 ? 509 A1ITF A C15 1 
HETATM 5026 C  C17 . A1ITF K 6 .   ? 7.107   59.791 55.192  1.00 29.05 ? 509 A1ITF A C17 1 
HETATM 5027 F  F   . A1ITF K 6 .   ? 4.794   60.245 54.885  1.00 30.38 ? 509 A1ITF A F   1 
HETATM 5028 C  C18 . A1ITF K 6 .   ? 5.720   59.204 55.054  1.00 29.49 ? 509 A1ITF A C18 1 
HETATM 5029 C  C16 . A1ITF K 6 .   ? 7.498   60.127 53.759  1.00 28.97 ? 509 A1ITF A C16 1 
HETATM 5030 C  C19 . A1ITF K 6 .   ? 5.754   58.436 53.780  1.00 29.10 ? 509 A1ITF A C19 1 
HETATM 5031 N  N5  . A1ITF K 6 .   ? 6.750   59.140 52.972  1.00 29.05 ? 509 A1ITF A N5  1 
HETATM 5032 C  C14 . A1ITF K 6 .   ? 8.185   59.201 49.762  1.00 29.85 ? 509 A1ITF A C14 1 
HETATM 5033 N  N4  . A1ITF K 6 .   ? 6.196   57.918 51.095  1.00 29.84 ? 509 A1ITF A N4  1 
HETATM 5034 C  C12 . A1ITF K 6 .   ? 6.454   57.617 49.814  1.00 30.12 ? 509 A1ITF A C12 1 
HETATM 5035 C  C3  . A1ITF K 6 .   ? 5.631   56.478 49.264  1.00 30.53 ? 509 A1ITF A C3  1 
HETATM 5036 C  C2  . A1ITF K 6 .   ? 5.736   56.192 47.756  1.00 30.53 ? 509 A1ITF A C2  1 
HETATM 5037 N  N   . A1ITF K 6 .   ? 5.087   54.124 49.633  1.00 30.38 ? 509 A1ITF A N   1 
HETATM 5038 C  C1  . A1ITF K 6 .   ? 4.904   54.966 47.390  1.00 31.08 ? 509 A1ITF A C1  1 
HETATM 5039 O  O   . A1ITF K 6 .   ? 4.434   54.606 46.085  1.00 31.79 ? 509 A1ITF A O   1 
HETATM 5040 C  C   . A1ITF K 6 .   ? 5.366   54.808 45.057  1.00 31.66 ? 509 A1ITF A C   1 
HETATM 5041 O  O1  . A1ITF K 6 .   ? 3.427   52.654 50.004  1.00 29.05 ? 509 A1ITF A O1  1 
HETATM 5042 C  C9  . A1ITF K 6 .   ? 3.429   55.302 53.631  1.00 28.82 ? 509 A1ITF A C9  1 
HETATM 5043 C  C11 . A1ITF K 6 .   ? 3.157   56.356 54.556  1.00 27.81 ? 509 A1ITF A C11 1 
HETATM 5044 N  N2  . A1ITF K 6 .   ? 2.915   57.157 55.330  1.00 27.56 ? 509 A1ITF A N2  1 
HETATM 5045 S  S   . DMS   L 7 .   ? -3.114  51.654 92.701  1.00 89.46 ? 301 DMS   B S   1 
HETATM 5046 O  O   . DMS   L 7 .   ? -2.862  50.360 91.976  1.00 89.60 ? 301 DMS   B O   1 
HETATM 5047 C  C1  . DMS   L 7 .   ? -2.459  51.480 94.374  1.00 89.28 ? 301 DMS   B C1  1 
HETATM 5048 C  C2  . DMS   L 7 .   ? -4.857  51.686 93.195  1.00 89.41 ? 301 DMS   B C2  1 
HETATM 5049 S  S   . DMS   M 7 .   ? 11.338  59.200 105.462 1.00 82.25 ? 302 DMS   B S   1 
HETATM 5050 O  O   . DMS   M 7 .   ? 12.617  59.946 105.191 1.00 82.29 ? 302 DMS   B O   1 
HETATM 5051 C  C1  . DMS   M 7 .   ? 10.086  60.114 104.553 1.00 82.25 ? 302 DMS   B C1  1 
HETATM 5052 C  C2  . DMS   M 7 .   ? 10.741  59.662 107.112 1.00 82.11 ? 302 DMS   B C2  1 
HETATM 5053 C  C1  . EDO   N 4 .   ? 4.858   57.536 78.627  1.00 66.68 ? 303 EDO   B C1  1 
HETATM 5054 O  O1  . EDO   N 4 .   ? 5.829   56.510 78.499  1.00 66.77 ? 303 EDO   B O1  1 
HETATM 5055 C  C2  . EDO   N 4 .   ? 3.922   57.505 77.451  1.00 66.80 ? 303 EDO   B C2  1 
HETATM 5056 O  O2  . EDO   N 4 .   ? 3.247   56.259 77.384  1.00 66.97 ? 303 EDO   B O2  1 
HETATM 5057 O  O   . HOH   O 8 .   ? -6.369  58.615 58.959  1.00 42.64 ? 601 HOH   A O   1 
HETATM 5058 O  O   . HOH   O 8 .   ? 12.500  64.243 57.463  1.00 28.82 ? 602 HOH   A O   1 
HETATM 5059 O  O   . HOH   O 8 .   ? 29.407  39.139 53.491  1.00 35.04 ? 603 HOH   A O   1 
HETATM 5060 O  O   . HOH   O 8 .   ? 22.579  52.225 60.858  1.00 29.95 ? 604 HOH   A O   1 
HETATM 5061 O  O   . HOH   O 8 .   ? 25.083  42.790 50.195  1.00 31.20 ? 605 HOH   A O   1 
HETATM 5062 O  O   . HOH   O 8 .   ? 7.616   78.136 51.394  1.00 47.30 ? 606 HOH   A O   1 
HETATM 5063 O  O   . HOH   O 8 .   ? 11.550  62.972 41.496  1.00 67.48 ? 607 HOH   A O   1 
HETATM 5064 O  O   . HOH   O 8 .   ? 10.609  62.746 63.900  1.00 28.89 ? 608 HOH   A O   1 
HETATM 5065 O  O   . HOH   O 8 .   ? 4.481   37.542 68.192  1.00 35.18 ? 609 HOH   A O   1 
HETATM 5066 O  O   . HOH   O 8 .   ? 5.148   30.957 70.885  1.00 34.70 ? 610 HOH   A O   1 
HETATM 5067 O  O   . HOH   O 8 .   ? 29.428  33.317 54.696  1.00 32.12 ? 611 HOH   A O   1 
HETATM 5068 O  O   . HOH   O 8 .   ? 30.072  50.164 58.758  1.00 68.93 ? 612 HOH   A O   1 
HETATM 5069 O  O   . HOH   O 8 .   ? 15.901  61.747 48.446  1.00 33.37 ? 613 HOH   A O   1 
HETATM 5070 O  O   . HOH   O 8 .   ? 3.030   51.885 61.702  1.00 31.23 ? 614 HOH   A O   1 
HETATM 5071 O  O   . HOH   O 8 .   ? 13.741  61.433 71.345  1.00 39.02 ? 615 HOH   A O   1 
HETATM 5072 O  O   . HOH   O 8 .   ? 9.458   39.026 51.074  1.00 23.56 ? 616 HOH   A O   1 
HETATM 5073 O  O   . HOH   O 8 .   ? -6.242  64.485 57.305  1.00 47.93 ? 617 HOH   A O   1 
HETATM 5074 O  O   . HOH   O 8 .   ? 2.310   51.252 55.547  1.00 34.49 ? 618 HOH   A O   1 
HETATM 5075 O  O   . HOH   O 8 .   ? 23.988  43.921 47.430  1.00 32.89 ? 619 HOH   A O   1 
HETATM 5076 O  O   . HOH   O 8 .   ? 19.148  51.216 67.131  1.00 40.28 ? 620 HOH   A O   1 
HETATM 5077 O  O   . HOH   O 8 .   ? 0.073   88.132 62.806  1.00 49.33 ? 621 HOH   A O   1 
HETATM 5078 O  O   . HOH   O 8 .   ? 5.824   58.464 58.597  1.00 22.55 ? 622 HOH   A O   1 
HETATM 5079 O  O   . HOH   O 8 .   ? 12.517  35.547 48.507  1.00 32.86 ? 623 HOH   A O   1 
HETATM 5080 O  O   . HOH   O 8 .   ? -2.063  19.627 53.918  1.00 48.77 ? 624 HOH   A O   1 
HETATM 5081 O  O   . HOH   O 8 .   ? 6.345   44.380 48.589  1.00 36.28 ? 625 HOH   A O   1 
HETATM 5082 O  O   . HOH   O 8 .   ? 6.583   28.018 71.999  1.00 36.62 ? 626 HOH   A O   1 
HETATM 5083 O  O   . HOH   O 8 .   ? 4.316   63.405 71.146  1.00 22.98 ? 627 HOH   A O   1 
HETATM 5084 O  O   . HOH   O 8 .   ? 4.602   57.056 42.419  1.00 38.40 ? 628 HOH   A O   1 
HETATM 5085 O  O   . HOH   O 8 .   ? 28.504  50.171 62.868  1.00 51.30 ? 629 HOH   A O   1 
HETATM 5086 O  O   . HOH   O 8 .   ? 13.589  29.225 60.545  1.00 42.52 ? 630 HOH   A O   1 
HETATM 5087 O  O   . HOH   O 8 .   ? 8.759   26.155 70.796  1.00 37.03 ? 631 HOH   A O   1 
HETATM 5088 O  O   . HOH   O 8 .   ? 12.783  25.800 57.088  1.00 25.76 ? 632 HOH   A O   1 
HETATM 5089 O  O   . HOH   O 8 .   ? 11.613  36.846 69.677  1.00 39.47 ? 633 HOH   A O   1 
HETATM 5090 O  O   . HOH   O 8 .   ? -4.620  74.832 54.766  1.00 65.47 ? 634 HOH   A O   1 
HETATM 5091 O  O   . HOH   O 8 .   ? 14.845  67.061 51.716  1.00 59.79 ? 635 HOH   A O   1 
HETATM 5092 O  O   . HOH   O 8 .   ? -0.340  64.137 35.264  1.00 53.15 ? 636 HOH   A O   1 
HETATM 5093 O  O   . HOH   O 8 .   ? -6.445  22.955 69.374  1.00 53.70 ? 637 HOH   A O   1 
HETATM 5094 O  O   . HOH   O 8 .   ? 23.044  36.689 65.566  1.00 42.12 ? 638 HOH   A O   1 
HETATM 5095 O  O   . HOH   O 8 .   ? 29.519  45.737 65.924  1.00 42.04 ? 639 HOH   A O   1 
HETATM 5096 O  O   . HOH   O 8 .   ? 25.371  34.438 60.122  1.00 21.53 ? 640 HOH   A O   1 
HETATM 5097 O  O   . HOH   O 8 .   ? 27.617  42.466 63.775  1.00 25.93 ? 641 HOH   A O   1 
HETATM 5098 O  O   . HOH   O 8 .   ? 8.559   44.601 46.780  1.00 40.42 ? 642 HOH   A O   1 
HETATM 5099 O  O   . HOH   O 8 .   ? 4.868   40.370 60.604  1.00 23.04 ? 643 HOH   A O   1 
HETATM 5100 O  O   . HOH   O 8 .   ? 16.280  32.428 65.969  1.00 26.92 ? 644 HOH   A O   1 
HETATM 5101 O  O   . HOH   O 8 .   ? 15.631  59.225 71.361  1.00 41.14 ? 645 HOH   A O   1 
HETATM 5102 O  O   . HOH   O 8 .   ? 24.829  39.680 51.236  1.00 50.30 ? 646 HOH   A O   1 
HETATM 5103 O  O   . HOH   O 8 .   ? 11.537  60.253 63.702  1.00 29.89 ? 647 HOH   A O   1 
HETATM 5104 O  O   . HOH   O 8 .   ? 15.895  60.862 60.298  1.00 25.20 ? 648 HOH   A O   1 
HETATM 5105 O  O   . HOH   O 8 .   ? 11.728  55.526 43.775  1.00 43.09 ? 649 HOH   A O   1 
HETATM 5106 O  O   . HOH   O 8 .   ? 12.242  73.655 48.336  1.00 53.10 ? 650 HOH   A O   1 
HETATM 5107 O  O   . HOH   O 8 .   ? 11.337  68.533 71.142  1.00 40.94 ? 651 HOH   A O   1 
HETATM 5108 O  O   . HOH   O 8 .   ? 23.638  33.774 62.099  1.00 31.61 ? 652 HOH   A O   1 
HETATM 5109 O  O   . HOH   O 8 .   ? -0.698  80.676 48.061  1.00 63.27 ? 653 HOH   A O   1 
HETATM 5110 O  O   . HOH   O 8 .   ? 9.414   33.334 45.396  1.00 58.68 ? 654 HOH   A O   1 
HETATM 5111 O  O   . HOH   O 8 .   ? 15.778  25.514 56.535  1.00 51.89 ? 655 HOH   A O   1 
HETATM 5112 O  O   . HOH   O 8 .   ? 1.484   50.917 50.808  1.00 45.09 ? 656 HOH   A O   1 
HETATM 5113 O  O   . HOH   O 8 .   ? 14.768  71.104 56.351  1.00 75.90 ? 657 HOH   A O   1 
HETATM 5114 O  O   . HOH   O 8 .   ? -1.203  80.376 64.427  1.00 43.78 ? 658 HOH   A O   1 
HETATM 5115 O  O   . HOH   O 8 .   ? 11.539  23.258 72.598  1.00 54.14 ? 659 HOH   A O   1 
HETATM 5116 O  O   . HOH   O 8 .   ? 28.047  58.793 50.057  1.00 49.62 ? 660 HOH   A O   1 
HETATM 5117 O  O   . HOH   O 8 .   ? -4.450  56.708 57.959  1.00 46.83 ? 661 HOH   A O   1 
HETATM 5118 O  O   . HOH   O 8 .   ? 15.389  65.257 49.736  1.00 52.14 ? 662 HOH   A O   1 
HETATM 5119 O  O   . HOH   O 8 .   ? 10.304  27.757 65.327  1.00 37.43 ? 663 HOH   A O   1 
HETATM 5120 O  O   . HOH   O 8 .   ? 7.729   20.076 56.997  1.00 58.30 ? 664 HOH   A O   1 
HETATM 5121 O  O   . HOH   O 8 .   ? 18.571  46.652 73.106  1.00 58.63 ? 665 HOH   A O   1 
HETATM 5122 O  O   . HOH   O 8 .   ? -10.363 89.674 73.735  1.00 44.33 ? 666 HOH   A O   1 
HETATM 5123 O  O   . HOH   O 8 .   ? 23.414  55.873 57.414  1.00 57.82 ? 667 HOH   A O   1 
HETATM 5124 O  O   . HOH   O 8 .   ? 4.586   36.225 56.048  1.00 25.67 ? 668 HOH   A O   1 
HETATM 5125 O  O   . HOH   O 8 .   ? -9.094  34.466 66.253  1.00 72.73 ? 669 HOH   A O   1 
HETATM 5126 O  O   . HOH   O 8 .   ? 12.104  38.795 67.756  1.00 35.44 ? 670 HOH   A O   1 
HETATM 5127 O  O   . HOH   O 8 .   ? 10.243  60.849 51.936  1.00 27.53 ? 671 HOH   A O   1 
HETATM 5128 O  O   . HOH   O 8 .   ? -5.637  65.895 48.405  1.00 59.93 ? 672 HOH   A O   1 
HETATM 5129 O  O   . HOH   O 8 .   ? 13.695  43.680 68.552  1.00 23.14 ? 673 HOH   A O   1 
HETATM 5130 O  O   . HOH   O 8 .   ? 0.671   83.680 57.971  1.00 38.26 ? 674 HOH   A O   1 
HETATM 5131 O  O   . HOH   O 8 .   ? -5.794  89.610 67.563  1.00 47.52 ? 675 HOH   A O   1 
HETATM 5132 O  O   . HOH   O 8 .   ? 13.300  24.436 68.462  1.00 46.55 ? 676 HOH   A O   1 
HETATM 5133 O  O   . HOH   O 8 .   ? -4.374  37.994 64.554  1.00 39.03 ? 677 HOH   A O   1 
HETATM 5134 O  O   . HOH   O 8 .   ? 10.674  25.143 50.438  1.00 36.49 ? 678 HOH   A O   1 
HETATM 5135 O  O   . HOH   O 8 .   ? 15.838  34.890 42.426  1.00 56.16 ? 679 HOH   A O   1 
HETATM 5136 O  O   . HOH   O 8 .   ? 2.425   81.585 48.914  1.00 57.78 ? 680 HOH   A O   1 
HETATM 5137 O  O   . HOH   O 8 .   ? 23.048  54.374 64.412  1.00 52.88 ? 681 HOH   A O   1 
HETATM 5138 O  O   . HOH   O 8 .   ? -4.486  65.355 44.700  1.00 46.23 ? 682 HOH   A O   1 
HETATM 5139 O  O   . HOH   O 8 .   ? 20.792  25.795 58.988  1.00 41.20 ? 683 HOH   A O   1 
HETATM 5140 O  O   . HOH   O 8 .   ? 4.664   44.563 65.564  1.00 31.35 ? 684 HOH   A O   1 
HETATM 5141 O  O   . HOH   O 8 .   ? 13.538  53.761 43.902  1.00 41.74 ? 685 HOH   A O   1 
HETATM 5142 O  O   . HOH   O 8 .   ? -13.576 64.529 62.048  1.00 57.79 ? 686 HOH   A O   1 
HETATM 5143 O  O   . HOH   O 8 .   ? -7.071  62.036 59.915  1.00 54.60 ? 687 HOH   A O   1 
HETATM 5144 O  O   . HOH   O 8 .   ? 14.116  60.256 63.249  1.00 29.97 ? 688 HOH   A O   1 
HETATM 5145 O  O   . HOH   O 8 .   ? 3.654   71.780 40.626  1.00 52.03 ? 689 HOH   A O   1 
HETATM 5146 O  O   . HOH   O 8 .   ? 5.893   44.913 61.001  1.00 26.20 ? 690 HOH   A O   1 
HETATM 5147 O  O   . HOH   O 8 .   ? 13.044  63.765 64.835  1.00 52.40 ? 691 HOH   A O   1 
HETATM 5148 O  O   . HOH   O 8 .   ? 16.453  42.594 45.303  1.00 62.63 ? 692 HOH   A O   1 
HETATM 5149 O  O   . HOH   O 8 .   ? -8.054  39.737 58.540  1.00 60.13 ? 693 HOH   A O   1 
HETATM 5150 O  O   . HOH   O 8 .   ? 18.384  41.086 72.801  1.00 54.04 ? 694 HOH   A O   1 
HETATM 5151 O  O   . HOH   O 8 .   ? -1.448  37.691 50.990  1.00 47.11 ? 695 HOH   A O   1 
HETATM 5152 O  O   . HOH   O 8 .   ? -7.982  26.419 68.164  1.00 49.70 ? 696 HOH   A O   1 
HETATM 5153 O  O   . HOH   O 8 .   ? 7.037   37.845 51.606  1.00 27.01 ? 697 HOH   A O   1 
HETATM 5154 O  O   . HOH   O 8 .   ? -15.050 79.023 73.983  1.00 35.93 ? 698 HOH   A O   1 
HETATM 5155 O  O   . HOH   O 8 .   ? 9.356   41.414 44.640  1.00 49.67 ? 699 HOH   A O   1 
HETATM 5156 O  O   . HOH   O 8 .   ? 13.094  47.276 75.120  1.00 77.94 ? 700 HOH   A O   1 
HETATM 5157 O  O   . HOH   O 8 .   ? 1.292   53.208 48.051  1.00 45.88 ? 701 HOH   A O   1 
HETATM 5158 O  O   . HOH   O 8 .   ? 1.320   14.482 50.957  1.00 56.98 ? 702 HOH   A O   1 
HETATM 5159 O  O   . HOH   O 8 .   ? 5.616   12.208 51.600  1.00 54.88 ? 703 HOH   A O   1 
HETATM 5160 O  O   . HOH   O 8 .   ? 4.639   71.741 63.381  1.00 48.75 ? 704 HOH   A O   1 
HETATM 5161 O  O   . HOH   O 8 .   ? 6.982   18.400 50.250  1.00 46.82 ? 705 HOH   A O   1 
HETATM 5162 O  O   . HOH   O 8 .   ? -7.612  22.491 53.501  1.00 60.58 ? 706 HOH   A O   1 
HETATM 5163 O  O   . HOH   O 8 .   ? 3.804   50.334 69.814  1.00 38.36 ? 707 HOH   A O   1 
HETATM 5164 O  O   . HOH   O 8 .   ? 28.402  57.938 58.838  1.00 68.24 ? 708 HOH   A O   1 
HETATM 5165 O  O   . HOH   O 8 .   ? -2.424  74.009 56.059  1.00 35.59 ? 709 HOH   A O   1 
HETATM 5166 O  O   . HOH   O 8 .   ? 12.103  34.913 73.826  1.00 49.35 ? 710 HOH   A O   1 
HETATM 5167 O  O   . HOH   O 8 .   ? 0.475   72.718 63.856  1.00 40.49 ? 711 HOH   A O   1 
HETATM 5168 O  O   . HOH   O 8 .   ? 0.624   73.351 45.069  1.00 54.15 ? 712 HOH   A O   1 
HETATM 5169 O  O   . HOH   O 8 .   ? 22.197  28.805 62.526  1.00 45.48 ? 713 HOH   A O   1 
HETATM 5170 O  O   . HOH   O 8 .   ? 0.751   80.442 55.220  1.00 42.18 ? 714 HOH   A O   1 
HETATM 5171 O  O   . HOH   O 8 .   ? 20.247  29.903 61.441  1.00 36.46 ? 715 HOH   A O   1 
HETATM 5172 O  O   . HOH   O 8 .   ? 18.540  59.392 43.193  1.00 45.30 ? 716 HOH   A O   1 
HETATM 5173 O  O   . HOH   O 8 .   ? 14.331  62.032 57.831  1.00 32.99 ? 717 HOH   A O   1 
HETATM 5174 O  O   . HOH   O 8 .   ? 1.374   77.864 62.026  1.00 51.24 ? 718 HOH   A O   1 
HETATM 5175 O  O   . HOH   O 8 .   ? 7.972   69.071 64.394  1.00 79.64 ? 719 HOH   A O   1 
HETATM 5176 O  O   . HOH   O 8 .   ? 19.903  35.734 44.153  1.00 71.74 ? 720 HOH   A O   1 
HETATM 5177 O  O   . HOH   O 8 .   ? 25.007  63.259 47.057  1.00 51.91 ? 721 HOH   A O   1 
HETATM 5178 O  O   . HOH   O 8 .   ? -2.306  51.449 51.689  1.00 51.02 ? 722 HOH   A O   1 
HETATM 5179 O  O   . HOH   O 8 .   ? -2.790  75.351 58.523  1.00 60.09 ? 723 HOH   A O   1 
HETATM 5180 O  O   . HOH   O 8 .   ? 27.038  35.777 53.749  1.00 27.97 ? 724 HOH   A O   1 
HETATM 5181 O  O   . HOH   O 8 .   ? 2.879   31.516 69.901  1.00 52.20 ? 725 HOH   A O   1 
HETATM 5182 O  O   . HOH   O 8 .   ? 14.131  27.037 58.956  1.00 41.09 ? 726 HOH   A O   1 
HETATM 5183 O  O   . HOH   O 8 .   ? 12.796  50.889 78.292  1.00 67.84 ? 727 HOH   A O   1 
HETATM 5184 O  O   . HOH   O 8 .   ? -8.029  75.830 56.329  1.00 60.21 ? 728 HOH   A O   1 
HETATM 5185 O  O   . HOH   O 8 .   ? -5.823  71.312 53.087  1.00 46.55 ? 729 HOH   A O   1 
HETATM 5186 O  O   . HOH   O 8 .   ? 14.162  45.830 72.750  1.00 49.36 ? 730 HOH   A O   1 
HETATM 5187 O  O   . HOH   O 8 .   ? -6.531  76.734 58.551  1.00 52.43 ? 731 HOH   A O   1 
HETATM 5188 O  O   . HOH   O 8 .   ? -4.351  80.307 52.273  1.00 58.79 ? 732 HOH   A O   1 
HETATM 5189 O  O   . HOH   O 8 .   ? 25.024  33.206 49.155  1.00 41.64 ? 733 HOH   A O   1 
HETATM 5190 O  O   . HOH   O 8 .   ? -11.601 93.340 69.019  1.00 57.40 ? 734 HOH   A O   1 
HETATM 5191 O  O   . HOH   O 8 .   ? 19.953  62.934 50.539  1.00 39.42 ? 735 HOH   A O   1 
HETATM 5192 O  O   . HOH   O 8 .   ? -7.818  29.228 47.668  1.00 52.22 ? 736 HOH   A O   1 
HETATM 5193 O  O   . HOH   O 8 .   ? 7.792   68.957 43.302  1.00 54.70 ? 737 HOH   A O   1 
HETATM 5194 O  O   . HOH   O 8 .   ? 1.933   41.945 54.793  1.00 32.73 ? 738 HOH   A O   1 
HETATM 5195 O  O   . HOH   O 8 .   ? 14.573  58.933 36.402  1.00 51.52 ? 739 HOH   A O   1 
HETATM 5196 O  O   . HOH   O 8 .   ? 11.078  69.459 68.688  1.00 62.87 ? 740 HOH   A O   1 
HETATM 5197 O  O   . HOH   O 8 .   ? -9.706  26.870 65.916  1.00 55.81 ? 741 HOH   A O   1 
HETATM 5198 O  O   . HOH   O 8 .   ? -9.726  56.456 63.956  1.00 37.71 ? 742 HOH   A O   1 
HETATM 5199 O  O   . HOH   O 8 .   ? 0.041   58.975 36.557  1.00 61.88 ? 743 HOH   A O   1 
HETATM 5200 O  O   . HOH   O 8 .   ? 3.609   32.251 43.941  1.00 53.73 ? 744 HOH   A O   1 
HETATM 5201 O  O   . HOH   O 8 .   ? 19.449  58.379 68.003  1.00 55.53 ? 745 HOH   A O   1 
HETATM 5202 O  O   . HOH   O 8 .   ? 18.755  74.346 49.736  1.00 69.15 ? 746 HOH   A O   1 
HETATM 5203 O  O   . HOH   O 8 .   ? 35.303  38.438 56.014  1.00 40.35 ? 747 HOH   A O   1 
HETATM 5204 O  O   . HOH   O 8 .   ? 16.152  68.416 57.060  1.00 68.90 ? 748 HOH   A O   1 
HETATM 5205 O  O   . HOH   O 8 .   ? 3.235   74.540 61.376  1.00 58.66 ? 749 HOH   A O   1 
HETATM 5206 O  O   . HOH   O 8 .   ? -8.759  31.416 54.268  1.00 51.08 ? 750 HOH   A O   1 
HETATM 5207 O  O   . HOH   O 8 .   ? -4.560  33.904 52.114  1.00 46.08 ? 751 HOH   A O   1 
HETATM 5208 O  O   . HOH   O 8 .   ? 22.477  25.618 56.581  1.00 52.26 ? 752 HOH   A O   1 
HETATM 5209 O  O   . HOH   O 8 .   ? -7.553  55.519 62.448  1.00 37.74 ? 753 HOH   A O   1 
HETATM 5210 O  O   . HOH   O 8 .   ? 8.071   17.578 67.501  1.00 54.31 ? 754 HOH   A O   1 
HETATM 5211 O  O   . HOH   O 8 .   ? 0.808   38.357 70.937  1.00 59.68 ? 755 HOH   A O   1 
HETATM 5212 O  O   . HOH   O 8 .   ? 29.040  55.118 52.973  1.00 43.46 ? 756 HOH   A O   1 
HETATM 5213 O  O   . HOH   O 8 .   ? 11.116  50.881 39.813  1.00 52.60 ? 757 HOH   A O   1 
HETATM 5214 O  O   . HOH   O 8 .   ? 16.920  21.062 54.275  1.00 58.82 ? 758 HOH   A O   1 
HETATM 5215 O  O   . HOH   O 8 .   ? 24.743  50.989 64.955  1.00 48.17 ? 759 HOH   A O   1 
HETATM 5216 O  O   . HOH   O 8 .   ? 10.277  21.452 47.706  1.00 45.30 ? 760 HOH   A O   1 
HETATM 5217 O  O   . HOH   O 8 .   ? 27.087  49.056 50.413  1.00 47.39 ? 761 HOH   A O   1 
HETATM 5218 O  O   . HOH   O 8 .   ? 5.508   46.802 50.165  1.00 25.62 ? 762 HOH   A O   1 
HETATM 5219 O  O   . HOH   O 8 .   ? -0.511  45.489 70.164  1.00 59.11 ? 763 HOH   A O   1 
HETATM 5220 O  O   . HOH   O 8 .   ? 3.389   44.135 56.932  1.00 58.73 ? 764 HOH   A O   1 
HETATM 5221 O  O   . HOH   O 8 .   ? 17.043  63.958 58.730  1.00 57.72 ? 765 HOH   A O   1 
HETATM 5222 O  O   . HOH   O 8 .   ? -0.271  75.069 46.487  1.00 53.93 ? 766 HOH   A O   1 
HETATM 5223 O  O   . HOH   O 8 .   ? -0.744  81.949 55.825  1.00 80.73 ? 767 HOH   A O   1 
HETATM 5224 O  O   . HOH   O 8 .   ? 32.576  37.205 60.367  1.00 35.83 ? 768 HOH   A O   1 
HETATM 5225 O  O   . HOH   O 8 .   ? -11.199 30.215 60.729  1.00 44.09 ? 769 HOH   A O   1 
HETATM 5226 O  O   . HOH   O 8 .   ? 25.552  25.459 56.875  1.00 49.35 ? 770 HOH   A O   1 
HETATM 5227 O  O   . HOH   O 8 .   ? 31.961  50.538 55.994  1.00 60.93 ? 771 HOH   A O   1 
HETATM 5228 O  O   . HOH   O 8 .   ? -8.543  64.873 50.392  1.00 55.87 ? 772 HOH   A O   1 
HETATM 5229 O  O   . HOH   O 8 .   ? 12.025  57.910 36.119  1.00 56.60 ? 773 HOH   A O   1 
HETATM 5230 O  O   . HOH   O 8 .   ? 8.315   39.804 70.902  1.00 43.03 ? 774 HOH   A O   1 
HETATM 5231 O  O   . HOH   O 8 .   ? 17.124  63.223 46.303  1.00 46.44 ? 775 HOH   A O   1 
HETATM 5232 O  O   . HOH   O 8 .   ? 7.007   42.302 72.380  1.00 39.08 ? 776 HOH   A O   1 
HETATM 5233 O  O   . HOH   O 8 .   ? 8.997   75.335 56.115  1.00 53.14 ? 777 HOH   A O   1 
HETATM 5234 O  O   . HOH   O 8 .   ? -0.320  75.116 61.017  1.00 69.46 ? 778 HOH   A O   1 
HETATM 5235 O  O   . HOH   O 8 .   ? -0.664  45.800 54.819  1.00 50.78 ? 779 HOH   A O   1 
HETATM 5236 O  O   . HOH   O 8 .   ? -9.479  61.238 52.523  1.00 57.96 ? 780 HOH   A O   1 
HETATM 5237 O  O   . HOH   O 8 .   ? 8.606   78.935 57.094  1.00 61.74 ? 781 HOH   A O   1 
HETATM 5238 O  O   . HOH   O 8 .   ? -6.037  18.241 54.924  1.00 67.69 ? 782 HOH   A O   1 
HETATM 5239 O  O   . HOH   O 8 .   ? 2.392   21.321 65.003  1.00 52.57 ? 783 HOH   A O   1 
HETATM 5240 O  O   . HOH   O 8 .   ? 8.801   25.289 59.925  1.00 60.17 ? 784 HOH   A O   1 
HETATM 5241 O  O   . HOH   O 8 .   ? -4.661  72.563 51.152  1.00 55.37 ? 785 HOH   A O   1 
HETATM 5242 O  O   . HOH   O 8 .   ? 13.590  83.867 47.181  1.00 55.46 ? 786 HOH   A O   1 
HETATM 5243 O  O   . HOH   O 8 .   ? -7.252  31.841 51.883  1.00 56.59 ? 787 HOH   A O   1 
HETATM 5244 O  O   . HOH   O 8 .   ? -6.832  69.552 50.015  1.00 54.49 ? 788 HOH   A O   1 
HETATM 5245 O  O   . HOH   O 8 .   ? 25.074  58.988 54.099  1.00 43.36 ? 789 HOH   A O   1 
HETATM 5246 O  O   . HOH   O 8 .   ? -6.762  26.399 70.589  1.00 61.80 ? 790 HOH   A O   1 
HETATM 5247 O  O   . HOH   O 8 .   ? -2.729  22.011 52.373  1.00 44.54 ? 791 HOH   A O   1 
HETATM 5248 O  O   . HOH   O 8 .   ? -1.411  64.686 41.881  1.00 58.31 ? 792 HOH   A O   1 
HETATM 5249 O  O   . HOH   O 8 .   ? 8.400   17.772 47.079  1.00 60.39 ? 793 HOH   A O   1 
HETATM 5250 O  O   . HOH   O 8 .   ? 30.468  53.793 55.747  1.00 48.96 ? 794 HOH   A O   1 
HETATM 5251 O  O   . HOH   O 8 .   ? 29.861  53.841 58.802  1.00 51.36 ? 795 HOH   A O   1 
HETATM 5252 O  O   . HOH   O 8 .   ? 16.690  65.407 71.267  1.00 56.55 ? 796 HOH   A O   1 
HETATM 5253 O  O   . HOH   O 8 .   ? -8.522  24.924 51.671  1.00 60.05 ? 797 HOH   A O   1 
HETATM 5254 O  O   . HOH   O 8 .   ? 10.861  42.989 75.373  1.00 72.33 ? 798 HOH   A O   1 
HETATM 5255 O  O   . HOH   O 8 .   ? -17.576 83.237 71.020  1.00 60.49 ? 799 HOH   A O   1 
HETATM 5256 O  O   . HOH   O 8 .   ? 6.956   54.585 39.902  1.00 59.75 ? 800 HOH   A O   1 
HETATM 5257 O  O   . HOH   O 8 .   ? 22.050  54.189 67.097  1.00 53.96 ? 801 HOH   A O   1 
HETATM 5258 O  O   . HOH   O 8 .   ? -4.631  68.303 47.828  1.00 67.91 ? 802 HOH   A O   1 
HETATM 5259 O  O   . HOH   O 8 .   ? 27.402  60.586 44.031  1.00 57.33 ? 803 HOH   A O   1 
HETATM 5260 O  O   . HOH   O 8 .   ? 3.799   43.000 60.330  1.00 45.79 ? 804 HOH   A O   1 
HETATM 5261 O  O   . HOH   O 8 .   ? -8.137  54.688 50.641  1.00 65.26 ? 805 HOH   A O   1 
HETATM 5262 O  O   . HOH   O 8 .   ? 13.349  67.296 63.101  1.00 65.63 ? 806 HOH   A O   1 
HETATM 5263 O  O   . HOH   O 8 .   ? 2.678   21.499 70.105  1.00 69.42 ? 807 HOH   A O   1 
HETATM 5264 O  O   . HOH   O 8 .   ? 18.471  65.396 53.689  1.00 62.07 ? 808 HOH   A O   1 
HETATM 5265 O  O   . HOH   O 8 .   ? 11.722  21.795 57.679  1.00 55.66 ? 809 HOH   A O   1 
HETATM 5266 O  O   . HOH   O 8 .   ? 26.857  46.136 66.223  1.00 49.66 ? 810 HOH   A O   1 
HETATM 5267 O  O   . HOH   O 8 .   ? -6.689  64.402 45.763  1.00 63.05 ? 811 HOH   A O   1 
HETATM 5268 O  O   . HOH   O 8 .   ? 4.545   54.483 41.560  1.00 64.06 ? 812 HOH   A O   1 
HETATM 5269 O  O   . HOH   O 8 .   ? 2.893   44.554 46.259  1.00 49.73 ? 813 HOH   A O   1 
HETATM 5270 O  O   . HOH   O 8 .   ? 22.691  62.234 61.260  1.00 66.16 ? 814 HOH   A O   1 
HETATM 5271 O  O   . HOH   O 8 .   ? -1.252  53.488 57.392  1.00 58.61 ? 815 HOH   A O   1 
HETATM 5272 O  O   . HOH   O 8 .   ? 6.801   61.467 36.233  1.00 69.59 ? 816 HOH   A O   1 
HETATM 5273 O  O   . HOH   O 8 .   ? 11.616  35.944 32.617  1.00 66.14 ? 817 HOH   A O   1 
HETATM 5274 O  O   . HOH   O 8 .   ? -2.829  34.943 71.308  1.00 46.24 ? 818 HOH   A O   1 
HETATM 5275 O  O   . HOH   O 8 .   ? 0.908   49.109 42.382  1.00 76.22 ? 819 HOH   A O   1 
HETATM 5276 O  O   . HOH   O 8 .   ? 11.665  69.877 63.803  1.00 72.35 ? 820 HOH   A O   1 
HETATM 5277 O  O   . HOH   O 8 .   ? 10.850  23.367 59.873  1.00 60.96 ? 821 HOH   A O   1 
HETATM 5278 O  O   . HOH   O 8 .   ? 16.987  67.380 49.078  1.00 60.60 ? 822 HOH   A O   1 
HETATM 5279 O  O   . HOH   O 8 .   ? -3.521  44.693 69.124  1.00 58.17 ? 823 HOH   A O   1 
HETATM 5280 O  O   . HOH   O 8 .   ? -1.091  51.691 49.205  1.00 49.49 ? 824 HOH   A O   1 
HETATM 5281 O  O   . HOH   O 8 .   ? 24.800  62.905 57.818  1.00 69.15 ? 825 HOH   A O   1 
HETATM 5282 O  O   . HOH   O 8 .   ? 3.563   42.633 73.610  1.00 68.20 ? 826 HOH   A O   1 
HETATM 5283 O  O   . HOH   O 8 .   ? 5.896   82.493 49.030  1.00 67.55 ? 827 HOH   A O   1 
HETATM 5284 O  O   . HOH   O 8 .   ? -4.971  87.085 71.429  1.00 46.61 ? 828 HOH   A O   1 
HETATM 5285 O  O   . HOH   O 8 .   ? 9.450   70.313 66.462  1.00 78.92 ? 829 HOH   A O   1 
HETATM 5286 O  O   . HOH   O 8 .   ? 20.071  53.787 68.744  1.00 39.02 ? 830 HOH   A O   1 
HETATM 5287 O  O   . HOH   O 8 .   ? 23.340  46.452 69.031  1.00 67.57 ? 831 HOH   A O   1 
HETATM 5288 O  O   . HOH   O 8 .   ? -8.971  28.672 50.672  1.00 66.31 ? 832 HOH   A O   1 
HETATM 5289 O  O   . HOH   O 8 .   ? 9.052   26.804 73.222  1.00 45.26 ? 833 HOH   A O   1 
HETATM 5290 O  O   . HOH   O 8 .   ? 26.275  44.104 74.301  1.00 52.60 ? 834 HOH   A O   1 
HETATM 5291 O  O   . HOH   O 8 .   ? 5.664   74.938 63.177  1.00 72.55 ? 835 HOH   A O   1 
HETATM 5292 O  O   . HOH   O 8 .   ? 10.999  25.641 47.846  1.00 47.45 ? 836 HOH   A O   1 
HETATM 5293 O  O   . HOH   O 8 .   ? 14.955  83.823 49.496  1.00 58.89 ? 837 HOH   A O   1 
HETATM 5294 O  O   . HOH   O 8 .   ? 12.260  40.999 69.115  1.00 40.00 ? 838 HOH   A O   1 
HETATM 5295 O  O   . HOH   O 8 .   ? -3.955  42.029 66.004  1.00 57.29 ? 839 HOH   A O   1 
HETATM 5296 O  O   . HOH   O 8 .   ? 27.561  46.081 70.935  1.00 53.43 ? 840 HOH   A O   1 
HETATM 5297 O  O   . HOH   O 8 .   ? 29.071  33.984 51.938  1.00 49.47 ? 841 HOH   A O   1 
HETATM 5298 O  O   . HOH   O 8 .   ? 25.358  51.869 58.840  1.00 52.23 ? 842 HOH   A O   1 
HETATM 5299 O  O   . HOH   O 8 .   ? -6.512  41.942 65.315  1.00 55.15 ? 843 HOH   A O   1 
HETATM 5300 O  O   . HOH   O 8 .   ? 23.610  55.601 62.188  1.00 59.70 ? 844 HOH   A O   1 
HETATM 5301 O  O   . HOH   O 8 .   ? 13.874  19.016 53.459  1.00 64.47 ? 845 HOH   A O   1 
HETATM 5302 O  O   . HOH   O 8 .   ? 0.377   51.005 53.499  1.00 30.87 ? 846 HOH   A O   1 
HETATM 5303 O  O   . HOH   O 8 .   ? -6.711  85.247 74.433  1.00 63.00 ? 847 HOH   A O   1 
HETATM 5304 O  O   . HOH   O 8 .   ? 29.336  59.866 46.191  1.00 57.17 ? 848 HOH   A O   1 
HETATM 5305 O  O   . HOH   O 8 .   ? 7.859   37.377 71.736  1.00 46.13 ? 849 HOH   A O   1 
HETATM 5306 O  O   . HOH   O 8 .   ? 10.805  39.256 71.315  1.00 55.80 ? 850 HOH   A O   1 
HETATM 5307 O  O   . HOH   O 8 .   ? 34.676  36.700 61.533  1.00 48.25 ? 851 HOH   A O   1 
HETATM 5308 O  O   . HOH   O 8 .   ? 29.175  57.941 53.162  1.00 52.37 ? 852 HOH   A O   1 
HETATM 5309 O  O   . HOH   O 8 .   ? 24.347  35.405 49.640  1.00 48.92 ? 853 HOH   A O   1 
HETATM 5310 O  O   . HOH   O 8 .   ? 0.737   80.835 66.120  1.00 67.34 ? 854 HOH   A O   1 
HETATM 5311 O  O   . HOH   O 8 .   ? 2.234   36.319 69.795  1.00 55.44 ? 855 HOH   A O   1 
HETATM 5312 O  O   . HOH   O 8 .   ? 18.376  20.331 52.176  1.00 60.83 ? 856 HOH   A O   1 
HETATM 5313 O  O   . HOH   O 8 .   ? -9.637  42.113 65.297  1.00 69.67 ? 857 HOH   A O   1 
HETATM 5314 O  O   . HOH   O 8 .   ? 5.482   48.435 77.998  1.00 54.84 ? 858 HOH   A O   1 
HETATM 5315 O  O   . HOH   P 8 .   ? 15.761  58.929 78.815  1.00 32.00 ? 401 HOH   B O   1 
HETATM 5316 O  O   . HOH   P 8 .   ? 10.780  74.143 86.340  1.00 42.41 ? 402 HOH   B O   1 
HETATM 5317 O  O   . HOH   P 8 .   ? 1.339   68.422 75.184  1.00 43.09 ? 403 HOH   B O   1 
HETATM 5318 O  O   . HOH   P 8 .   ? -16.229 60.844 67.902  1.00 32.81 ? 404 HOH   B O   1 
HETATM 5319 O  O   . HOH   P 8 .   ? 12.216  48.610 91.053  1.00 62.24 ? 405 HOH   B O   1 
HETATM 5320 O  O   . HOH   P 8 .   ? 19.790  61.278 97.980  1.00 54.38 ? 406 HOH   B O   1 
HETATM 5321 O  O   . HOH   P 8 .   ? -1.013  52.942 101.483 1.00 32.94 ? 407 HOH   B O   1 
HETATM 5322 O  O   . HOH   P 8 .   ? -20.491 77.022 93.696  1.00 43.80 ? 408 HOH   B O   1 
HETATM 5323 O  O   . HOH   P 8 .   ? -1.612  50.110 89.796  1.00 61.71 ? 409 HOH   B O   1 
HETATM 5324 O  O   . HOH   P 8 .   ? -24.560 68.401 91.033  1.00 39.16 ? 410 HOH   B O   1 
HETATM 5325 O  O   . HOH   P 8 .   ? 4.629   69.172 81.115  1.00 27.47 ? 411 HOH   B O   1 
HETATM 5326 O  O   . HOH   P 8 .   ? -7.101  64.213 94.188  1.00 49.68 ? 412 HOH   B O   1 
HETATM 5327 O  O   . HOH   P 8 .   ? -17.341 74.507 103.937 1.00 46.24 ? 413 HOH   B O   1 
HETATM 5328 O  O   . HOH   P 8 .   ? -26.712 75.698 78.021  1.00 51.42 ? 414 HOH   B O   1 
HETATM 5329 O  O   . HOH   P 8 .   ? -13.457 81.438 79.651  1.00 47.16 ? 415 HOH   B O   1 
HETATM 5330 O  O   . HOH   P 8 .   ? 7.188   63.452 75.493  1.00 22.60 ? 416 HOH   B O   1 
HETATM 5331 O  O   . HOH   P 8 .   ? -4.453  80.824 82.167  1.00 36.09 ? 417 HOH   B O   1 
HETATM 5332 O  O   . HOH   P 8 .   ? 0.798   60.381 76.548  1.00 29.36 ? 418 HOH   B O   1 
HETATM 5333 O  O   . HOH   P 8 .   ? -18.664 73.773 62.804  1.00 56.63 ? 419 HOH   B O   1 
HETATM 5334 O  O   . HOH   P 8 .   ? -16.011 55.940 67.967  1.00 48.02 ? 420 HOH   B O   1 
HETATM 5335 O  O   . HOH   P 8 .   ? -4.688  89.311 91.250  1.00 55.09 ? 421 HOH   B O   1 
HETATM 5336 O  O   . HOH   P 8 .   ? -20.838 81.100 87.677  1.00 48.80 ? 422 HOH   B O   1 
HETATM 5337 O  O   . HOH   P 8 .   ? -24.881 69.587 81.710  1.00 30.68 ? 423 HOH   B O   1 
HETATM 5338 O  O   . HOH   P 8 .   ? 9.005   72.674 67.869  1.00 54.16 ? 424 HOH   B O   1 
HETATM 5339 O  O   . HOH   P 8 .   ? 11.400  72.194 78.970  1.00 37.75 ? 425 HOH   B O   1 
HETATM 5340 O  O   . HOH   P 8 .   ? 0.321   80.922 82.707  1.00 38.49 ? 426 HOH   B O   1 
HETATM 5341 O  O   . HOH   P 8 .   ? -11.139 55.939 85.980  1.00 45.15 ? 427 HOH   B O   1 
HETATM 5342 O  O   . HOH   P 8 .   ? 6.316   66.555 84.696  1.00 25.66 ? 428 HOH   B O   1 
HETATM 5343 O  O   . HOH   P 8 .   ? -11.386 59.667 72.033  1.00 27.64 ? 429 HOH   B O   1 
HETATM 5344 O  O   . HOH   P 8 .   ? 18.116  48.256 94.608  1.00 36.13 ? 430 HOH   B O   1 
HETATM 5345 O  O   . HOH   P 8 .   ? -20.201 80.593 94.677  1.00 37.51 ? 431 HOH   B O   1 
HETATM 5346 O  O   . HOH   P 8 .   ? -10.804 64.469 65.107  1.00 31.30 ? 432 HOH   B O   1 
HETATM 5347 O  O   . HOH   P 8 .   ? -7.826  80.652 64.179  1.00 40.53 ? 433 HOH   B O   1 
HETATM 5348 O  O   . HOH   P 8 .   ? 1.509   56.222 75.326  1.00 48.63 ? 434 HOH   B O   1 
HETATM 5349 O  O   . HOH   P 8 .   ? 3.309   77.476 90.263  1.00 53.59 ? 435 HOH   B O   1 
HETATM 5350 O  O   . HOH   P 8 .   ? 9.477   60.548 74.087  1.00 23.28 ? 436 HOH   B O   1 
HETATM 5351 O  O   . HOH   P 8 .   ? 6.203   60.260 110.509 1.00 53.13 ? 437 HOH   B O   1 
HETATM 5352 O  O   . HOH   P 8 .   ? -7.369  62.161 96.076  1.00 33.75 ? 438 HOH   B O   1 
HETATM 5353 O  O   . HOH   P 8 .   ? -19.394 77.807 80.138  1.00 53.47 ? 439 HOH   B O   1 
HETATM 5354 O  O   . HOH   P 8 .   ? 5.094   66.111 75.403  1.00 24.16 ? 440 HOH   B O   1 
HETATM 5355 O  O   . HOH   P 8 .   ? -8.757  85.245 97.001  1.00 48.81 ? 441 HOH   B O   1 
HETATM 5356 O  O   . HOH   P 8 .   ? -26.039 69.045 76.151  1.00 54.68 ? 442 HOH   B O   1 
HETATM 5357 O  O   . HOH   P 8 .   ? -7.974  77.194 108.794 1.00 55.63 ? 443 HOH   B O   1 
HETATM 5358 O  O   . HOH   P 8 .   ? 8.044   74.659 97.083  1.00 53.04 ? 444 HOH   B O   1 
HETATM 5359 O  O   . HOH   P 8 .   ? -0.486  70.035 105.071 1.00 41.53 ? 445 HOH   B O   1 
HETATM 5360 O  O   . HOH   P 8 .   ? 0.681   68.757 88.422  1.00 30.40 ? 446 HOH   B O   1 
HETATM 5361 O  O   . HOH   P 8 .   ? 0.659   60.407 110.475 1.00 53.50 ? 447 HOH   B O   1 
HETATM 5362 O  O   . HOH   P 8 .   ? -24.912 69.928 73.905  1.00 55.04 ? 448 HOH   B O   1 
HETATM 5363 O  O   . HOH   P 8 .   ? 7.277   58.772 83.855  1.00 32.36 ? 449 HOH   B O   1 
HETATM 5364 O  O   . HOH   P 8 .   ? 17.334  49.818 97.454  1.00 51.74 ? 450 HOH   B O   1 
HETATM 5365 O  O   . HOH   P 8 .   ? -9.625  79.444 100.869 1.00 55.66 ? 451 HOH   B O   1 
HETATM 5366 O  O   . HOH   P 8 .   ? -7.913  64.972 86.598  1.00 26.25 ? 452 HOH   B O   1 
HETATM 5367 O  O   . HOH   P 8 .   ? -27.647 62.365 83.407  1.00 51.13 ? 453 HOH   B O   1 
HETATM 5368 O  O   . HOH   P 8 .   ? 18.773  65.811 76.916  1.00 58.66 ? 454 HOH   B O   1 
HETATM 5369 O  O   . HOH   P 8 .   ? 12.622  75.062 81.978  1.00 54.15 ? 455 HOH   B O   1 
HETATM 5370 O  O   . HOH   P 8 .   ? -0.183  81.664 91.021  1.00 75.58 ? 456 HOH   B O   1 
HETATM 5371 O  O   . HOH   P 8 .   ? 1.494   65.984 88.924  1.00 39.42 ? 457 HOH   B O   1 
HETATM 5372 O  O   . HOH   P 8 .   ? -13.791 54.970 76.461  1.00 57.34 ? 458 HOH   B O   1 
HETATM 5373 O  O   . HOH   P 8 .   ? -24.298 76.883 70.392  1.00 50.39 ? 459 HOH   B O   1 
HETATM 5374 O  O   . HOH   P 8 .   ? 16.158  75.148 92.659  1.00 77.05 ? 460 HOH   B O   1 
HETATM 5375 O  O   . HOH   P 8 .   ? -15.092 54.066 71.162  1.00 70.03 ? 461 HOH   B O   1 
HETATM 5376 O  O   . HOH   P 8 .   ? 8.196   83.705 92.553  1.00 70.93 ? 462 HOH   B O   1 
HETATM 5377 O  O   . HOH   P 8 .   ? -4.741  54.750 95.558  1.00 47.24 ? 463 HOH   B O   1 
HETATM 5378 O  O   . HOH   P 8 .   ? -15.176 75.697 69.091  1.00 41.21 ? 464 HOH   B O   1 
HETATM 5379 O  O   . HOH   P 8 .   ? -0.035  56.831 70.488  1.00 48.24 ? 465 HOH   B O   1 
HETATM 5380 O  O   . HOH   P 8 .   ? -17.162 78.800 81.517  1.00 51.56 ? 466 HOH   B O   1 
HETATM 5381 O  O   . HOH   P 8 .   ? 4.718   51.030 77.362  1.00 64.85 ? 467 HOH   B O   1 
HETATM 5382 O  O   . HOH   P 8 .   ? -22.685 58.909 79.001  1.00 55.63 ? 468 HOH   B O   1 
HETATM 5383 O  O   . HOH   P 8 .   ? -22.247 68.702 65.638  1.00 52.89 ? 469 HOH   B O   1 
HETATM 5384 O  O   . HOH   P 8 .   ? 7.479   86.355 86.742  1.00 55.67 ? 470 HOH   B O   1 
HETATM 5385 O  O   . HOH   P 8 .   ? 1.255   58.449 79.491  1.00 45.29 ? 471 HOH   B O   1 
HETATM 5386 O  O   . HOH   P 8 .   ? -6.967  88.215 80.484  1.00 61.75 ? 472 HOH   B O   1 
HETATM 5387 O  O   . HOH   P 8 .   ? 15.239  48.762 99.264  1.00 47.19 ? 473 HOH   B O   1 
HETATM 5388 O  O   . HOH   P 8 .   ? -24.581 71.298 83.394  1.00 42.37 ? 474 HOH   B O   1 
HETATM 5389 O  O   . HOH   P 8 .   ? -20.466 60.527 86.386  1.00 60.14 ? 475 HOH   B O   1 
HETATM 5390 O  O   . HOH   P 8 .   ? 1.960   52.335 70.267  1.00 55.55 ? 476 HOH   B O   1 
HETATM 5391 O  O   . HOH   P 8 .   ? -4.521  62.269 87.120  1.00 37.18 ? 477 HOH   B O   1 
HETATM 5392 O  O   . HOH   P 8 .   ? 9.338   78.300 80.507  1.00 44.08 ? 478 HOH   B O   1 
HETATM 5393 O  O   . HOH   P 8 .   ? 10.487  75.656 98.374  1.00 64.99 ? 479 HOH   B O   1 
HETATM 5394 O  O   . HOH   P 8 .   ? -7.129  59.760 94.651  1.00 36.16 ? 480 HOH   B O   1 
HETATM 5395 O  O   . HOH   P 8 .   ? 19.355  66.790 80.011  1.00 70.28 ? 481 HOH   B O   1 
HETATM 5396 O  O   . HOH   P 8 .   ? 4.659   57.716 82.446  1.00 26.47 ? 482 HOH   B O   1 
HETATM 5397 O  O   . HOH   P 8 .   ? -2.683  56.589 68.975  1.00 41.06 ? 483 HOH   B O   1 
HETATM 5398 O  O   . HOH   P 8 .   ? -4.157  72.400 109.653 1.00 50.25 ? 484 HOH   B O   1 
HETATM 5399 O  O   . HOH   P 8 .   ? -22.993 66.794 68.936  1.00 45.48 ? 485 HOH   B O   1 
HETATM 5400 O  O   . HOH   P 8 .   ? 11.204  57.458 80.943  1.00 52.19 ? 486 HOH   B O   1 
HETATM 5401 O  O   . HOH   P 8 .   ? 18.232  65.142 90.653  1.00 56.43 ? 487 HOH   B O   1 
HETATM 5402 O  O   . HOH   P 8 .   ? -13.760 64.223 90.409  1.00 48.14 ? 488 HOH   B O   1 
HETATM 5403 O  O   . HOH   P 8 .   ? 18.106  51.038 102.078 1.00 47.73 ? 489 HOH   B O   1 
HETATM 5404 O  O   . HOH   P 8 .   ? 6.305   74.886 73.475  1.00 60.36 ? 490 HOH   B O   1 
HETATM 5405 O  O   . HOH   P 8 .   ? -10.347 82.774 97.283  1.00 42.38 ? 491 HOH   B O   1 
HETATM 5406 O  O   . HOH   P 8 .   ? 9.562   52.243 109.997 1.00 52.17 ? 492 HOH   B O   1 
HETATM 5407 O  O   . HOH   P 8 .   ? -6.225  56.147 90.569  1.00 45.70 ? 493 HOH   B O   1 
HETATM 5408 O  O   . HOH   P 8 .   ? -12.274 53.688 68.595  1.00 55.46 ? 494 HOH   B O   1 
HETATM 5409 O  O   . HOH   P 8 .   ? -18.746 86.702 82.886  1.00 50.07 ? 495 HOH   B O   1 
HETATM 5410 O  O   . HOH   P 8 .   ? -9.526  94.417 73.654  1.00 64.31 ? 496 HOH   B O   1 
HETATM 5411 O  O   . HOH   P 8 .   ? -5.810  71.811 85.922  1.00 39.39 ? 497 HOH   B O   1 
HETATM 5412 O  O   . HOH   P 8 .   ? -1.671  81.791 80.735  1.00 35.72 ? 498 HOH   B O   1 
HETATM 5413 O  O   . HOH   P 8 .   ? -3.329  87.399 94.414  1.00 56.57 ? 499 HOH   B O   1 
HETATM 5414 O  O   . HOH   P 8 .   ? 3.087   56.840 84.687  1.00 21.46 ? 500 HOH   B O   1 
HETATM 5415 O  O   . HOH   P 8 .   ? -12.636 84.068 96.423  1.00 53.02 ? 501 HOH   B O   1 
HETATM 5416 O  O   . HOH   P 8 .   ? 13.652  76.086 97.389  1.00 57.61 ? 502 HOH   B O   1 
HETATM 5417 O  O   . HOH   P 8 .   ? -2.586  76.442 89.067  1.00 52.62 ? 503 HOH   B O   1 
HETATM 5418 O  O   . HOH   P 8 .   ? -12.022 61.825 65.655  1.00 40.92 ? 504 HOH   B O   1 
HETATM 5419 O  O   . HOH   P 8 .   ? 18.850  57.352 91.866  1.00 73.28 ? 505 HOH   B O   1 
HETATM 5420 O  O   . HOH   P 8 .   ? -15.661 71.101 63.430  1.00 52.03 ? 506 HOH   B O   1 
HETATM 5421 O  O   . HOH   P 8 .   ? 6.732   75.653 75.814  1.00 47.53 ? 507 HOH   B O   1 
HETATM 5422 O  O   . HOH   P 8 .   ? -2.045  75.904 83.950  1.00 40.39 ? 508 HOH   B O   1 
HETATM 5423 O  O   . HOH   P 8 .   ? -7.697  61.480 91.077  1.00 60.19 ? 509 HOH   B O   1 
HETATM 5424 O  O   . HOH   P 8 .   ? -19.835 55.361 79.695  1.00 56.21 ? 510 HOH   B O   1 
HETATM 5425 O  O   . HOH   P 8 .   ? 17.281  61.151 103.721 1.00 55.38 ? 511 HOH   B O   1 
HETATM 5426 O  O   . HOH   P 8 .   ? -6.152  63.282 88.248  1.00 36.19 ? 512 HOH   B O   1 
HETATM 5427 O  O   . HOH   P 8 .   ? -13.145 71.501 98.308  1.00 38.81 ? 513 HOH   B O   1 
HETATM 5428 O  O   . HOH   P 8 .   ? -0.712  77.533 64.255  1.00 70.04 ? 514 HOH   B O   1 
HETATM 5429 O  O   . HOH   P 8 .   ? -19.349 58.920 66.608  1.00 47.61 ? 515 HOH   B O   1 
HETATM 5430 O  O   . HOH   P 8 .   ? 4.297   46.515 102.534 1.00 66.73 ? 516 HOH   B O   1 
HETATM 5431 O  O   . HOH   P 8 .   ? -16.697 58.256 91.492  1.00 66.31 ? 517 HOH   B O   1 
HETATM 5432 O  O   . HOH   P 8 .   ? 1.863   72.872 66.092  1.00 50.97 ? 518 HOH   B O   1 
HETATM 5433 O  O   . HOH   P 8 .   ? 4.312   64.568 85.316  1.00 44.45 ? 519 HOH   B O   1 
HETATM 5434 O  O   . HOH   P 8 .   ? -20.185 55.400 84.170  1.00 55.04 ? 520 HOH   B O   1 
HETATM 5435 O  O   . HOH   P 8 .   ? 16.273  58.139 90.952  1.00 51.11 ? 521 HOH   B O   1 
HETATM 5436 O  O   . HOH   P 8 .   ? -13.487 69.254 99.711  1.00 56.88 ? 522 HOH   B O   1 
HETATM 5437 O  O   . HOH   P 8 .   ? 0.816   88.416 90.764  1.00 67.90 ? 523 HOH   B O   1 
HETATM 5438 O  O   . HOH   P 8 .   ? -23.649 76.530 83.124  1.00 74.72 ? 524 HOH   B O   1 
HETATM 5439 O  O   . HOH   P 8 .   ? 12.979  74.242 90.627  1.00 64.42 ? 525 HOH   B O   1 
HETATM 5440 O  O   . HOH   P 8 .   ? -28.022 72.117 75.956  1.00 64.18 ? 526 HOH   B O   1 
HETATM 5441 O  O   . HOH   P 8 .   ? -28.251 72.018 84.599  1.00 61.45 ? 527 HOH   B O   1 
HETATM 5442 O  O   . HOH   P 8 .   ? 17.776  53.482 97.211  1.00 59.06 ? 528 HOH   B O   1 
HETATM 5443 O  O   . HOH   P 8 .   ? -4.343  84.317 75.488  1.00 42.85 ? 529 HOH   B O   1 
HETATM 5444 O  O   . HOH   P 8 .   ? -22.220 58.654 67.996  1.00 46.96 ? 530 HOH   B O   1 
HETATM 5445 O  O   . HOH   P 8 .   ? 3.012   61.760 110.950 1.00 65.55 ? 531 HOH   B O   1 
HETATM 5446 O  O   . HOH   P 8 .   ? 2.413   76.586 69.009  1.00 53.84 ? 532 HOH   B O   1 
HETATM 5447 O  O   . HOH   P 8 .   ? 12.940  55.159 88.517  1.00 54.73 ? 533 HOH   B O   1 
HETATM 5448 O  O   . HOH   P 8 .   ? 13.029  70.639 87.818  1.00 40.68 ? 534 HOH   B O   1 
HETATM 5449 O  O   . HOH   P 8 .   ? 3.758   53.136 81.767  1.00 61.41 ? 535 HOH   B O   1 
HETATM 5450 O  O   . HOH   P 8 .   ? 10.882  65.361 106.307 1.00 59.15 ? 536 HOH   B O   1 
HETATM 5451 O  O   . HOH   P 8 .   ? -30.140 74.865 80.479  1.00 52.60 ? 537 HOH   B O   1 
HETATM 5452 O  O   . HOH   P 8 .   ? 15.179  52.790 104.431 1.00 59.85 ? 538 HOH   B O   1 
HETATM 5453 O  O   . HOH   P 8 .   ? 1.101   74.781 92.563  1.00 46.13 ? 539 HOH   B O   1 
HETATM 5454 O  O   . HOH   P 8 .   ? 0.818   83.002 74.159  1.00 67.73 ? 540 HOH   B O   1 
HETATM 5455 O  O   . HOH   P 8 .   ? -2.892  54.182 84.912  1.00 59.02 ? 541 HOH   B O   1 
HETATM 5456 O  O   . HOH   P 8 .   ? 5.447   70.313 65.303  1.00 66.23 ? 542 HOH   B O   1 
HETATM 5457 O  O   . HOH   P 8 .   ? 11.106  76.298 88.253  1.00 59.85 ? 543 HOH   B O   1 
HETATM 5458 O  O   . HOH   P 8 .   ? -11.444 70.517 96.417  1.00 44.88 ? 544 HOH   B O   1 
HETATM 5459 O  O   . HOH   P 8 .   ? -28.214 74.367 89.844  1.00 77.80 ? 545 HOH   B O   1 
HETATM 5460 O  O   . HOH   P 8 .   ? 5.233   44.633 99.788  1.00 65.42 ? 546 HOH   B O   1 
HETATM 5461 O  O   . HOH   P 8 .   ? 14.483  71.562 80.340  1.00 57.88 ? 547 HOH   B O   1 
HETATM 5462 O  O   . HOH   P 8 .   ? 10.627  60.781 84.719  1.00 47.62 ? 548 HOH   B O   1 
HETATM 5463 O  O   . HOH   P 8 .   ? -4.669  77.939 102.624 1.00 51.94 ? 549 HOH   B O   1 
HETATM 5464 O  O   . HOH   P 8 .   ? -6.114  52.979 86.490  1.00 64.61 ? 550 HOH   B O   1 
HETATM 5465 O  O   . HOH   P 8 .   ? -15.590 88.831 84.344  1.00 58.45 ? 551 HOH   B O   1 
HETATM 5466 O  O   . HOH   P 8 .   ? -4.531  85.558 96.522  1.00 51.46 ? 552 HOH   B O   1 
HETATM 5467 O  O   . HOH   P 8 .   ? 14.342  56.969 81.953  1.00 67.69 ? 553 HOH   B O   1 
HETATM 5468 O  O   . HOH   P 8 .   ? -13.466 54.492 73.886  1.00 61.73 ? 554 HOH   B O   1 
HETATM 5469 O  O   . HOH   P 8 .   ? 3.300   75.320 66.694  1.00 64.38 ? 555 HOH   B O   1 
HETATM 5470 O  O   . HOH   P 8 .   ? -20.929 91.066 69.842  1.00 61.89 ? 556 HOH   B O   1 
HETATM 5471 O  O   . HOH   P 8 .   ? -16.117 80.929 79.213  1.00 42.16 ? 557 HOH   B O   1 
HETATM 5472 O  O   . HOH   P 8 .   ? -18.734 55.177 86.473  1.00 65.37 ? 558 HOH   B O   1 
HETATM 5473 O  O   . HOH   P 8 .   ? -22.718 76.052 65.952  1.00 58.75 ? 559 HOH   B O   1 
HETATM 5474 O  O   . HOH   P 8 .   ? 12.429  51.626 103.667 1.00 66.99 ? 560 HOH   B O   1 
HETATM 5475 O  O   . HOH   P 8 .   ? 8.299   66.065 105.281 1.00 67.63 ? 561 HOH   B O   1 
HETATM 5476 O  O   . HOH   P 8 .   ? 7.684   75.313 93.262  1.00 55.68 ? 562 HOH   B O   1 
HETATM 5477 O  O   . HOH   P 8 .   ? -17.740 65.599 92.017  1.00 64.46 ? 563 HOH   B O   1 
HETATM 5478 O  O   . HOH   P 8 .   ? -9.536  68.876 95.447  1.00 38.24 ? 564 HOH   B O   1 
HETATM 5479 O  O   . HOH   P 8 .   ? 7.912   75.882 69.594  1.00 69.92 ? 565 HOH   B O   1 
HETATM 5480 O  O   . HOH   P 8 .   ? 24.546  50.561 100.428 1.00 66.80 ? 566 HOH   B O   1 
HETATM 5481 O  O   . HOH   P 8 .   ? -27.035 63.275 78.646  1.00 56.83 ? 567 HOH   B O   1 
HETATM 5482 O  O   . HOH   P 8 .   ? -2.912  46.898 99.315  1.00 60.58 ? 568 HOH   B O   1 
HETATM 5483 O  O   . HOH   P 8 .   ? 3.514   90.092 81.938  1.00 76.38 ? 569 HOH   B O   1 
HETATM 5484 O  O   . HOH   P 8 .   ? 17.572  73.721 94.370  1.00 61.11 ? 570 HOH   B O   1 
HETATM 5485 O  O   . HOH   P 8 .   ? -2.306  77.107 101.969 1.00 52.95 ? 571 HOH   B O   1 
HETATM 5486 O  O   . HOH   P 8 .   ? -26.972 75.607 72.944  1.00 63.31 ? 572 HOH   B O   1 
HETATM 5487 O  O   . HOH   P 8 .   ? -5.830  87.913 78.154  1.00 53.65 ? 573 HOH   B O   1 
HETATM 5488 O  O   . HOH   P 8 .   ? -24.987 59.644 79.932  1.00 58.65 ? 574 HOH   B O   1 
HETATM 5489 O  O   . HOH   P 8 .   ? -14.708 62.031 65.964  1.00 46.68 ? 575 HOH   B O   1 
HETATM 5490 O  O   . HOH   P 8 .   ? -5.206  55.496 100.012 1.00 46.07 ? 576 HOH   B O   1 
HETATM 5491 O  O   . HOH   P 8 .   ? -23.653 64.305 69.489  1.00 54.77 ? 577 HOH   B O   1 
HETATM 5492 O  O   . HOH   P 8 .   ? -23.370 63.522 66.508  1.00 64.74 ? 578 HOH   B O   1 
HETATM 5493 O  O   . HOH   P 8 .   ? -18.707 57.725 87.201  1.00 59.76 ? 579 HOH   B O   1 
HETATM 5494 O  O   . HOH   P 8 .   ? -7.435  90.778 91.356  1.00 58.37 ? 580 HOH   B O   1 
HETATM 5495 O  O   . HOH   P 8 .   ? -4.861  77.752 108.362 1.00 69.61 ? 581 HOH   B O   1 
HETATM 5496 O  O   . HOH   P 8 .   ? 0.334   53.284 85.083  1.00 50.23 ? 582 HOH   B O   1 
HETATM 5497 O  O   . HOH   P 8 .   ? -11.300 79.011 105.944 1.00 51.62 ? 583 HOH   B O   1 
HETATM 5498 O  O   . HOH   P 8 .   ? -0.977  84.940 75.148  1.00 66.57 ? 584 HOH   B O   1 
HETATM 5499 O  O   . HOH   P 8 .   ? -22.032 55.535 82.231  1.00 58.52 ? 585 HOH   B O   1 
HETATM 5500 O  O   . HOH   P 8 .   ? 13.294  74.033 84.412  1.00 63.39 ? 586 HOH   B O   1 
HETATM 5501 O  O   . HOH   P 8 .   ? -21.886 78.980 74.666  1.00 60.89 ? 587 HOH   B O   1 
HETATM 5502 O  O   . HOH   P 8 .   ? 1.714   51.864 73.363  1.00 66.99 ? 588 HOH   B O   1 
HETATM 5503 O  O   . HOH   P 8 .   ? 15.997  53.629 93.845  1.00 63.56 ? 589 HOH   B O   1 
HETATM 5504 O  O   . HOH   P 8 .   ? -18.084 81.346 77.505  1.00 41.94 ? 590 HOH   B O   1 
HETATM 5505 O  O   . HOH   P 8 .   ? -21.168 79.271 77.922  1.00 80.94 ? 591 HOH   B O   1 
HETATM 5506 O  O   . HOH   P 8 .   ? -22.717 77.516 72.492  1.00 57.30 ? 592 HOH   B O   1 
HETATM 5507 O  O   . HOH   P 8 .   ? 10.636  76.370 78.612  1.00 54.70 ? 593 HOH   B O   1 
HETATM 5508 O  O   . HOH   P 8 .   ? -22.035 75.538 81.290  1.00 55.33 ? 594 HOH   B O   1 
HETATM 5509 O  O   . HOH   P 8 .   ? 0.020   48.044 90.419  1.00 72.45 ? 595 HOH   B O   1 
HETATM 5510 O  O   . HOH   P 8 .   ? -16.735 58.498 66.145  1.00 64.22 ? 596 HOH   B O   1 
HETATM 5511 O  O   . HOH   P 8 .   ? -2.881  83.743 97.751  1.00 65.43 ? 597 HOH   B O   1 
HETATM 5512 O  O   . HOH   P 8 .   ? -12.796 76.465 69.680  1.00 44.21 ? 598 HOH   B O   1 
HETATM 5513 O  O   . HOH   P 8 .   ? -1.970  80.855 96.222  1.00 55.82 ? 599 HOH   B O   1 
HETATM 5514 O  O   . HOH   P 8 .   ? 15.047  52.272 91.874  1.00 77.28 ? 600 HOH   B O   1 
HETATM 5515 O  O   . HOH   P 8 .   ? 5.662   79.602 79.732  1.00 45.75 ? 601 HOH   B O   1 
HETATM 5516 O  O   . HOH   P 8 .   ? -19.656 66.404 63.934  1.00 63.26 ? 602 HOH   B O   1 
HETATM 5517 O  O   . HOH   P 8 .   ? 10.611  77.185 93.541  1.00 67.31 ? 603 HOH   B O   1 
HETATM 5518 O  O   . HOH   P 8 .   ? 4.711   90.118 84.593  1.00 68.07 ? 604 HOH   B O   1 
HETATM 5519 O  O   . HOH   P 8 .   ? 5.866   77.941 77.010  1.00 66.06 ? 605 HOH   B O   1 
HETATM 5520 O  O   . HOH   P 8 .   ? 3.902   75.464 92.314  1.00 46.18 ? 606 HOH   B O   1 
HETATM 5521 O  O   . HOH   P 8 .   ? -0.281  79.837 94.406  1.00 56.89 ? 607 HOH   B O   1 
HETATM 5522 O  O   . HOH   P 8 .   ? 20.098  64.568 81.532  1.00 64.47 ? 608 HOH   B O   1 
HETATM 5523 O  O   . HOH   P 8 .   ? 18.403  63.708 87.873  1.00 72.12 ? 609 HOH   B O   1 
HETATM 5524 O  O   . HOH   P 8 .   ? 19.954  64.988 84.164  1.00 59.30 ? 610 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  ? 0.7102 0.5564 0.6127 0.0905  0.0603  0.0791  1   MET A N   
2    C CA  . MET A 12  ? 0.7188 0.5567 0.6018 0.0850  0.0531  0.0756  1   MET A CA  
3    C C   . MET A 12  ? 0.7029 0.5267 0.5648 0.0884  0.0544  0.0762  1   MET A C   
4    O O   . MET A 12  ? 0.7106 0.5389 0.5770 0.0938  0.0548  0.0775  1   MET A O   
5    C CB  . MET A 12  ? 0.7366 0.5900 0.6330 0.0798  0.0428  0.0713  1   MET A CB  
6    C CG  . MET A 12  ? 0.8165 0.6627 0.6964 0.0762  0.0366  0.0682  1   MET A CG  
7    S SD  . MET A 12  ? 0.9936 0.8522 0.8840 0.0689  0.0266  0.0639  1   MET A SD  
8    C CE  . MET A 12  ? 1.0023 0.8561 0.8881 0.0633  0.0280  0.0632  1   MET A CE  
9    N N   . ASP A 13  ? 0.6813 0.4881 0.5207 0.0856  0.0546  0.0747  2   ASP A N   
10   C CA  . ASP A 13  ? 0.6635 0.4548 0.4823 0.0875  0.0566  0.0744  2   ASP A CA  
11   C C   . ASP A 13  ? 0.6409 0.4377 0.4616 0.0858  0.0511  0.0717  2   ASP A C   
12   O O   . ASP A 13  ? 0.6340 0.4382 0.4612 0.0796  0.0443  0.0679  2   ASP A O   
13   C CB  . ASP A 13  ? 0.6758 0.4497 0.4741 0.0836  0.0561  0.0712  2   ASP A CB  
14   C CG  . ASP A 13  ? 0.7079 0.4645 0.4859 0.0846  0.0589  0.0701  2   ASP A CG  
15   O OD1 . ASP A 13  ? 0.7150 0.4589 0.4805 0.0910  0.0662  0.0740  2   ASP A OD1 
16   O OD2 . ASP A 13  ? 0.7224 0.4773 0.4973 0.0793  0.0548  0.0656  2   ASP A OD2 
17   N N   . TYR A 14  ? 0.6270 0.4196 0.4418 0.0925  0.0548  0.0740  3   TYR A N   
18   C CA  . TYR A 14  ? 0.6267 0.4204 0.4390 0.0943  0.0517  0.0723  3   TYR A CA  
19   C C   . TYR A 14  ? 0.6259 0.4066 0.4236 0.0872  0.0506  0.0680  3   TYR A C   
20   O O   . TYR A 14  ? 0.6259 0.4119 0.4283 0.0844  0.0457  0.0654  3   TYR A O   
21   C CB  . TYR A 14  ? 0.6407 0.4288 0.4450 0.1048  0.0574  0.0760  3   TYR A CB  
22   C CG  . TYR A 14  ? 0.6677 0.4521 0.4635 0.1087  0.0555  0.0745  3   TYR A CG  
23   C CD1 . TYR A 14  ? 0.6756 0.4751 0.4855 0.1118  0.0477  0.0727  3   TYR A CD1 
24   C CD2 . TYR A 14  ? 0.6967 0.4601 0.4689 0.1092  0.0617  0.0740  3   TYR A CD2 
25   C CE1 . TYR A 14  ? 0.6986 0.4911 0.4967 0.1170  0.0464  0.0714  3   TYR A CE1 
26   C CE2 . TYR A 14  ? 0.7144 0.4707 0.4763 0.1133  0.0619  0.0728  3   TYR A CE2 
27   C CZ  . TYR A 14  ? 0.7257 0.4959 0.4992 0.1180  0.0544  0.0718  3   TYR A CZ  
28   O OH  . TYR A 14  ? 0.7644 0.5245 0.5243 0.1239  0.0551  0.0708  3   TYR A OH  
29   N N   . ASP A 15  ? 0.6268 0.3903 0.4077 0.0845  0.0552  0.0669  4   ASP A N   
30   C CA  . ASP A 15  ? 0.6394 0.3906 0.4099 0.0771  0.0549  0.0616  4   ASP A CA  
31   C C   . ASP A 15  ? 0.6313 0.3929 0.4144 0.0684  0.0471  0.0571  4   ASP A C   
32   O O   . ASP A 15  ? 0.6338 0.3939 0.4182 0.0632  0.0454  0.0534  4   ASP A O   
33   C CB  . ASP A 15  ? 0.6745 0.4064 0.4270 0.0759  0.0598  0.0600  4   ASP A CB  
34   C CG  . ASP A 15  ? 0.7575 0.4758 0.4943 0.0840  0.0685  0.0643  4   ASP A CG  
35   O OD1 . ASP A 15  ? 0.7600 0.4803 0.4966 0.0898  0.0711  0.0669  4   ASP A OD1 
36   O OD2 . ASP A 15  ? 0.8148 0.5194 0.5379 0.0857  0.0727  0.0650  4   ASP A OD2 
37   N N   . PHE A 16  ? 0.6220 0.3930 0.4138 0.0675  0.0436  0.0579  5   PHE A N   
38   C CA  . PHE A 16  ? 0.6178 0.3995 0.4210 0.0608  0.0366  0.0545  5   PHE A CA  
39   C C   . PHE A 16  ? 0.6044 0.4009 0.4223 0.0603  0.0325  0.0552  5   PHE A C   
40   O O   . PHE A 16  ? 0.6047 0.4036 0.4265 0.0544  0.0285  0.0517  5   PHE A O   
41   C CB  . PHE A 16  ? 0.6213 0.4070 0.4278 0.0631  0.0366  0.0568  5   PHE A CB  
42   C CG  . PHE A 16  ? 0.6397 0.4363 0.4568 0.0582  0.0305  0.0544  5   PHE A CG  
43   C CD1 . PHE A 16  ? 0.6580 0.4496 0.4694 0.0527  0.0256  0.0486  5   PHE A CD1 
44   C CD2 . PHE A 16  ? 0.6506 0.4621 0.4838 0.0596  0.0298  0.0575  5   PHE A CD2 
45   C CE1 . PHE A 16  ? 0.6659 0.4667 0.4852 0.0494  0.0203  0.0467  5   PHE A CE1 
46   C CE2 . PHE A 16  ? 0.6593 0.4790 0.5003 0.0556  0.0253  0.0556  5   PHE A CE2 
47   C CZ  . PHE A 16  ? 0.6610 0.4749 0.4936 0.0510  0.0208  0.0507  5   PHE A CZ  
48   N N   . LYS A 17  ? 0.5943 0.3995 0.4199 0.0672  0.0335  0.0594  6   LYS A N   
49   C CA  . LYS A 17  ? 0.5923 0.4109 0.4309 0.0686  0.0284  0.0595  6   LYS A CA  
50   C C   . LYS A 17  ? 0.5986 0.4089 0.4280 0.0692  0.0285  0.0578  6   LYS A C   
51   O O   . LYS A 17  ? 0.5923 0.4082 0.4279 0.0656  0.0237  0.0559  6   LYS A O   
52   C CB  . LYS A 17  ? 0.6141 0.4437 0.4643 0.0766  0.0289  0.0630  6   LYS A CB  
53   C CG  . LYS A 17  ? 0.6800 0.5241 0.5446 0.0793  0.0220  0.0620  6   LYS A CG  
54   C CD  . LYS A 17  ? 0.7406 0.5986 0.6227 0.0861  0.0216  0.0637  6   LYS A CD  
55   C CE  . LYS A 17  ? 0.7941 0.6592 0.6809 0.0939  0.0153  0.0622  6   LYS A CE  
56   N NZ  . LYS A 17  ? 0.8361 0.6868 0.7029 0.1021  0.0195  0.0637  6   LYS A NZ  
57   N N   . VAL A 18  ? 0.6130 0.4083 0.4265 0.0740  0.0350  0.0588  7   VAL A N   
58   C CA  . VAL A 18  ? 0.6255 0.4089 0.4277 0.0757  0.0377  0.0576  7   VAL A CA  
59   C C   . VAL A 18  ? 0.6225 0.3974 0.4224 0.0657  0.0391  0.0533  7   VAL A C   
60   O O   . VAL A 18  ? 0.6286 0.4003 0.4279 0.0648  0.0391  0.0522  7   VAL A O   
61   C CB  . VAL A 18  ? 0.6543 0.4219 0.4385 0.0845  0.0457  0.0599  7   VAL A CB  
62   C CG1 . VAL A 18  ? 0.6634 0.4403 0.4510 0.0964  0.0426  0.0630  7   VAL A CG1 
63   C CG2 . VAL A 18  ? 0.6670 0.4228 0.4409 0.0827  0.0523  0.0603  7   VAL A CG2 
64   N N   . LYS A 19  ? 0.6152 0.3862 0.4143 0.0589  0.0399  0.0506  8   LYS A N   
65   C CA  . LYS A 19  ? 0.6281 0.3940 0.4294 0.0491  0.0397  0.0451  8   LYS A CA  
66   C C   . LYS A 19  ? 0.6243 0.4054 0.4407 0.0446  0.0321  0.0441  8   LYS A C   
67   O O   . LYS A 19  ? 0.6300 0.4080 0.4485 0.0416  0.0333  0.0424  8   LYS A O   
68   C CB  . LYS A 19  ? 0.6669 0.4275 0.4646 0.0446  0.0391  0.0415  8   LYS A CB  
69   C CG  . LYS A 19  ? 0.7276 0.4907 0.5339 0.0350  0.0342  0.0346  8   LYS A CG  
70   C CD  . LYS A 19  ? 0.8137 0.5614 0.6132 0.0300  0.0379  0.0282  8   LYS A CD  
71   C CE  . LYS A 19  ? 0.8785 0.6292 0.6909 0.0207  0.0346  0.0208  8   LYS A CE  
72   N NZ  . LYS A 19  ? 0.9157 0.6649 0.7337 0.0193  0.0401  0.0222  8   LYS A NZ  
73   N N   . LEU A 20  ? 0.6112 0.4073 0.4372 0.0452  0.0259  0.0458  9   LEU A N   
74   C CA  . LEU A 20  ? 0.6056 0.4158 0.4449 0.0415  0.0192  0.0453  9   LEU A CA  
75   C C   . LEU A 20  ? 0.6051 0.4176 0.4465 0.0450  0.0183  0.0472  9   LEU A C   
76   O O   . LEU A 20  ? 0.6063 0.4208 0.4526 0.0405  0.0161  0.0456  9   LEU A O   
77   C CB  . LEU A 20  ? 0.5986 0.4220 0.4467 0.0428  0.0150  0.0474  9   LEU A CB  
78   C CG  . LEU A 20  ? 0.6181 0.4393 0.4635 0.0396  0.0143  0.0451  9   LEU A CG  
79   C CD1 . LEU A 20  ? 0.6212 0.4529 0.4743 0.0422  0.0128  0.0480  9   LEU A CD1 
80   C CD2 . LEU A 20  ? 0.6204 0.4415 0.4683 0.0321  0.0102  0.0397  9   LEU A CD2 
81   N N   . SER A 21  ? 0.6037 0.4149 0.4403 0.0538  0.0199  0.0504  10  SER A N   
82   C CA  . SER A 21  ? 0.6203 0.4314 0.4553 0.0597  0.0180  0.0517  10  SER A CA  
83   C C   . SER A 21  ? 0.6496 0.4430 0.4725 0.0588  0.0246  0.0505  10  SER A C   
84   O O   . SER A 21  ? 0.6528 0.4455 0.4766 0.0590  0.0228  0.0505  10  SER A O   
85   C CB  . SER A 21  ? 0.6394 0.4524 0.4712 0.0708  0.0176  0.0544  10  SER A CB  
86   O OG  . SER A 21  ? 0.6857 0.5012 0.5172 0.0778  0.0127  0.0547  10  SER A OG  
87   N N   . SER A 22  ? 0.6654 0.4435 0.4777 0.0573  0.0330  0.0493  11  SER A N   
88   C CA  . SER A 22  ? 0.6850 0.4444 0.4879 0.0552  0.0420  0.0475  11  SER A CA  
89   C C   . SER A 22  ? 0.6824 0.4456 0.4977 0.0444  0.0405  0.0438  11  SER A C   
90   O O   . SER A 22  ? 0.6860 0.4409 0.4997 0.0443  0.0447  0.0438  11  SER A O   
91   C CB  . SER A 22  ? 0.7110 0.4547 0.5027 0.0547  0.0511  0.0461  11  SER A CB  
92   O OG  . SER A 22  ? 0.7476 0.4729 0.5334 0.0512  0.0613  0.0435  11  SER A OG  
93   N N   . GLU A 23  ? 0.6722 0.4468 0.4990 0.0364  0.0350  0.0407  12  GLU A N   
94   C CA  . GLU A 23  ? 0.6776 0.4577 0.5172 0.0270  0.0323  0.0365  12  GLU A CA  
95   C C   . GLU A 23  ? 0.6664 0.4608 0.5153 0.0269  0.0248  0.0388  12  GLU A C   
96   O O   . GLU A 23  ? 0.6669 0.4650 0.5254 0.0203  0.0234  0.0362  12  GLU A O   
97   C CB  . GLU A 23  ? 0.7192 0.5057 0.5651 0.0206  0.0276  0.0318  12  GLU A CB  
98   C CG  . GLU A 23  ? 0.8219 0.5940 0.6607 0.0184  0.0338  0.0276  12  GLU A CG  
99   C CD  . GLU A 23  ? 0.9580 0.7187 0.8020 0.0117  0.0410  0.0222  12  GLU A CD  
100  O OE1 . GLU A 23  ? 0.9709 0.7384 0.8282 0.0061  0.0386  0.0197  12  GLU A OE1 
101  O OE2 . GLU A 23  ? 1.0186 0.7627 0.8540 0.0120  0.0501  0.0205  12  GLU A OE2 
102  N N   . ARG A 24  ? 0.6502 0.4533 0.4977 0.0340  0.0198  0.0430  13  ARG A N   
103  C CA  . ARG A 24  ? 0.6400 0.4569 0.4969 0.0335  0.0123  0.0444  13  ARG A CA  
104  C C   . ARG A 24  ? 0.6545 0.4649 0.5088 0.0349  0.0138  0.0457  13  ARG A C   
105  O O   . ARG A 24  ? 0.6719 0.4720 0.5148 0.0433  0.0166  0.0480  13  ARG A O   
106  C CB  . ARG A 24  ? 0.6343 0.4630 0.4941 0.0398  0.0064  0.0473  13  ARG A CB  
107  C CG  . ARG A 24  ? 0.6289 0.4728 0.5007 0.0373  -0.0012 0.0477  13  ARG A CG  
108  C CD  . ARG A 24  ? 0.6256 0.4827 0.5057 0.0414  -0.0058 0.0492  13  ARG A CD  
109  N NE  . ARG A 24  ? 0.6226 0.4825 0.5051 0.0394  -0.0037 0.0489  13  ARG A NE  
110  C CZ  . ARG A 24  ? 0.6383 0.4959 0.5176 0.0448  -0.0006 0.0503  13  ARG A CZ  
111  N NH1 . ARG A 24  ? 0.6243 0.4784 0.4990 0.0526  -0.0002 0.0515  13  ARG A NH1 
112  N NH2 . ARG A 24  ? 0.6290 0.4866 0.5083 0.0434  0.0021  0.0504  13  ARG A NH2 
113  N N   . GLU A 25  ? 0.6501 0.4661 0.5139 0.0278  0.0117  0.0442  14  GLU A N   
114  C CA  . GLU A 25  ? 0.6586 0.4693 0.5215 0.0282  0.0132  0.0456  14  GLU A CA  
115  C C   . GLU A 25  ? 0.6493 0.4680 0.5108 0.0347  0.0055  0.0488  14  GLU A C   
116  O O   . GLU A 25  ? 0.6352 0.4699 0.5065 0.0322  -0.0021 0.0487  14  GLU A O   
117  C CB  . GLU A 25  ? 0.6951 0.5129 0.5709 0.0187  0.0120  0.0429  14  GLU A CB  
118  C CG  . GLU A 25  ? 0.8015 0.6092 0.6811 0.0125  0.0201  0.0386  14  GLU A CG  
119  C CD  . GLU A 25  ? 0.9250 0.7408 0.8196 0.0040  0.0182  0.0351  14  GLU A CD  
120  O OE1 . GLU A 25  ? 0.9525 0.7840 0.8539 0.0017  0.0093  0.0345  14  GLU A OE1 
121  O OE2 . GLU A 25  ? 0.9661 0.7721 0.8660 0.0001  0.0262  0.0328  14  GLU A OE2 
122  N N   . ARG A 26  ? 0.6560 0.4619 0.5045 0.0436  0.0077  0.0511  15  ARG A N   
123  C CA  . ARG A 26  ? 0.6627 0.4739 0.5088 0.0509  -0.0005 0.0528  15  ARG A CA  
124  C C   . ARG A 26  ? 0.6611 0.4659 0.5042 0.0506  -0.0002 0.0543  15  ARG A C   
125  O O   . ARG A 26  ? 0.6693 0.4574 0.5046 0.0504  0.0091  0.0553  15  ARG A O   
126  C CB  . ARG A 26  ? 0.7116 0.5126 0.5431 0.0635  -0.0001 0.0537  15  ARG A CB  
127  C CG  . ARG A 26  ? 0.7696 0.5796 0.6062 0.0640  -0.0012 0.0526  15  ARG A CG  
128  C CD  . ARG A 26  ? 0.8455 0.6409 0.6656 0.0749  0.0037  0.0534  15  ARG A CD  
129  N NE  . ARG A 26  ? 0.9113 0.7188 0.7379 0.0781  -0.0004 0.0529  15  ARG A NE  
130  C CZ  . ARG A 26  ? 0.9547 0.7643 0.7851 0.0730  0.0043  0.0527  15  ARG A CZ  
131  N NH1 . ARG A 26  ? 0.9524 0.7540 0.7815 0.0643  0.0118  0.0519  15  ARG A NH1 
132  N NH2 . ARG A 26  ? 0.9553 0.7749 0.7915 0.0768  0.0014  0.0529  15  ARG A NH2 
133  N N   . VAL A 27  ? 0.6515 0.4693 0.5021 0.0497  -0.0093 0.0546  16  VAL A N   
134  C CA  . VAL A 27  ? 0.6535 0.4667 0.5014 0.0493  -0.0102 0.0564  16  VAL A CA  
135  C C   . VAL A 27  ? 0.6679 0.4594 0.4952 0.0611  -0.0071 0.0585  16  VAL A C   
136  O O   . VAL A 27  ? 0.6797 0.4565 0.4996 0.0610  0.0001  0.0608  16  VAL A O   
137  C CB  . VAL A 27  ? 0.6514 0.4830 0.5112 0.0462  -0.0207 0.0558  16  VAL A CB  
138  C CG1 . VAL A 27  ? 0.6571 0.4933 0.5149 0.0553  -0.0300 0.0545  16  VAL A CG1 
139  C CG2 . VAL A 27  ? 0.6597 0.4879 0.5185 0.0432  -0.0205 0.0578  16  VAL A CG2 
140  N N   . GLU A 28  ? 0.6697 0.4577 0.4870 0.0722  -0.0117 0.0578  17  GLU A N   
141  C CA  . GLU A 28  ? 0.6942 0.4595 0.4876 0.0864  -0.0098 0.0594  17  GLU A CA  
142  C C   . GLU A 28  ? 0.7135 0.4541 0.4916 0.0891  0.0060  0.0616  17  GLU A C   
143  O O   . GLU A 28  ? 0.7344 0.4514 0.4917 0.0991  0.0118  0.0640  17  GLU A O   
144  C CB  . GLU A 28  ? 0.7044 0.4742 0.4923 0.0988  -0.0208 0.0568  17  GLU A CB  
145  C CG  . GLU A 28  ? 0.7259 0.4975 0.5137 0.1016  -0.0177 0.0557  17  GLU A CG  
146  C CD  . GLU A 28  ? 0.7507 0.5480 0.5627 0.0919  -0.0227 0.0535  17  GLU A CD  
147  O OE1 . GLU A 28  ? 0.7142 0.5259 0.5430 0.0801  -0.0245 0.0532  17  GLU A OE1 
148  O OE2 . GLU A 28  ? 0.7885 0.5900 0.6013 0.0970  -0.0239 0.0522  17  GLU A OE2 
149  N N   . ASP A 29  ? 0.7077 0.4521 0.4957 0.0803  0.0136  0.0605  18  ASP A N   
150  C CA  . ASP A 29  ? 0.7252 0.4473 0.5027 0.0807  0.0296  0.0615  18  ASP A CA  
151  C C   . ASP A 29  ? 0.7176 0.4366 0.5066 0.0693  0.0386  0.0619  18  ASP A C   
152  O O   . ASP A 29  ? 0.7283 0.4250 0.5087 0.0706  0.0533  0.0631  18  ASP A O   
153  C CB  . ASP A 29  ? 0.7479 0.4743 0.5302 0.0772  0.0332  0.0593  18  ASP A CB  
154  C CG  . ASP A 29  ? 0.8195 0.5471 0.5908 0.0889  0.0269  0.0591  18  ASP A CG  
155  O OD1 . ASP A 29  ? 0.8268 0.5425 0.5799 0.1030  0.0237  0.0605  18  ASP A OD1 
156  O OD2 . ASP A 29  ? 0.8565 0.5961 0.6367 0.0850  0.0250  0.0574  18  ASP A OD2 
157  N N   . LEU A 30  ? 0.6987 0.4397 0.5081 0.0583  0.0308  0.0604  19  LEU A N   
158  C CA  . LEU A 30  ? 0.6914 0.4327 0.5143 0.0477  0.0377  0.0599  19  LEU A CA  
159  C C   . LEU A 30  ? 0.6882 0.4220 0.5059 0.0505  0.0382  0.0635  19  LEU A C   
160  O O   . LEU A 30  ? 0.6925 0.4144 0.5135 0.0468  0.0496  0.0645  19  LEU A O   
161  C CB  . LEU A 30  ? 0.6795 0.4459 0.5252 0.0352  0.0304  0.0560  19  LEU A CB  
162  C CG  . LEU A 30  ? 0.7061 0.4740 0.5580 0.0302  0.0345  0.0520  19  LEU A CG  
163  C CD1 . LEU A 30  ? 0.7048 0.4957 0.5714 0.0229  0.0243  0.0488  19  LEU A CD1 
164  C CD2 . LEU A 30  ? 0.7209 0.4767 0.5801 0.0237  0.0474  0.0495  19  LEU A CD2 
165  N N   . PHE A 31  ? 0.6800 0.4198 0.4905 0.0570  0.0266  0.0651  20  PHE A N   
166  C CA  . PHE A 31  ? 0.6802 0.4130 0.4846 0.0597  0.0259  0.0685  20  PHE A CA  
167  C C   . PHE A 31  ? 0.7064 0.4209 0.4854 0.0753  0.0227  0.0712  20  PHE A C   
168  O O   . PHE A 31  ? 0.7130 0.4305 0.4839 0.0836  0.0140  0.0694  20  PHE A O   
169  C CB  . PHE A 31  ? 0.6518 0.4098 0.4738 0.0507  0.0145  0.0674  20  PHE A CB  
170  C CG  . PHE A 31  ? 0.6240 0.3963 0.4679 0.0372  0.0180  0.0649  20  PHE A CG  
171  C CD1 . PHE A 31  ? 0.6217 0.3892 0.4727 0.0317  0.0258  0.0662  20  PHE A CD1 
172  C CD2 . PHE A 31  ? 0.6101 0.3994 0.4668 0.0309  0.0135  0.0608  20  PHE A CD2 
173  C CE1 . PHE A 31  ? 0.6139 0.3954 0.4860 0.0204  0.0274  0.0626  20  PHE A CE1 
174  C CE2 . PHE A 31  ? 0.6025 0.4029 0.4768 0.0203  0.0155  0.0575  20  PHE A CE2 
175  C CZ  . PHE A 31  ? 0.5985 0.3958 0.4811 0.0151  0.0218  0.0579  20  PHE A CZ  
176  N N   . GLU A 32  ? 0.7202 0.4148 0.4864 0.0801  0.0299  0.0752  21  GLU A N   
177  C CA  . GLU A 32  ? 0.7459 0.4196 0.4850 0.0960  0.0267  0.0779  21  GLU A CA  
178  C C   . GLU A 32  ? 0.7437 0.4314 0.4890 0.0929  0.0144  0.0783  21  GLU A C   
179  O O   . GLU A 32  ? 0.7439 0.4328 0.4981 0.0850  0.0199  0.0809  21  GLU A O   
180  C CB  . GLU A 32  ? 0.7990 0.4377 0.5180 0.1038  0.0451  0.0828  21  GLU A CB  
181  C CG  . GLU A 32  ? 0.8811 0.4926 0.5664 0.1228  0.0429  0.0858  21  GLU A CG  
182  C CD  . GLU A 32  ? 0.9740 0.5848 0.6425 0.1368  0.0300  0.0824  21  GLU A CD  
183  O OE1 . GLU A 32  ? 0.9896 0.6001 0.6576 0.1384  0.0338  0.0804  21  GLU A OE1 
184  O OE2 . GLU A 32  ? 1.0284 0.6394 0.6851 0.1461  0.0155  0.0813  21  GLU A OE2 
185  N N   . TYR A 33  ? 0.7364 0.4364 0.4799 0.0982  -0.0019 0.0752  22  TYR A N   
186  C CA  . TYR A 33  ? 0.7328 0.4472 0.4838 0.0945  -0.0138 0.0746  22  TYR A CA  
187  C C   . TYR A 33  ? 0.7546 0.4639 0.4896 0.1081  -0.0282 0.0720  22  TYR A C   
188  O O   . TYR A 33  ? 0.7529 0.4693 0.4909 0.1064  -0.0372 0.0714  22  TYR A O   
189  C CB  . TYR A 33  ? 0.7053 0.4527 0.4860 0.0797  -0.0205 0.0712  22  TYR A CB  
190  C CG  . TYR A 33  ? 0.6973 0.4591 0.4863 0.0809  -0.0275 0.0665  22  TYR A CG  
191  C CD1 . TYR A 33  ? 0.6987 0.4725 0.4909 0.0859  -0.0420 0.0624  22  TYR A CD1 
192  C CD2 . TYR A 33  ? 0.7045 0.4676 0.4992 0.0772  -0.0194 0.0659  22  TYR A CD2 
193  C CE1 . TYR A 33  ? 0.7023 0.4895 0.5040 0.0874  -0.0475 0.0583  22  TYR A CE1 
194  C CE2 . TYR A 33  ? 0.7097 0.4847 0.5109 0.0790  -0.0250 0.0623  22  TYR A CE2 
195  C CZ  . TYR A 33  ? 0.7179 0.5053 0.5232 0.0841  -0.0387 0.0588  22  TYR A CZ  
196  O OH  . TYR A 33  ? 0.7403 0.5397 0.5538 0.0863  -0.0434 0.0554  22  TYR A OH  
197  N N   . GLU A 34  ? 0.7772 0.4755 0.4965 0.1215  -0.0314 0.0696  23  GLU A N   
198  C CA  . GLU A 34  ? 0.8012 0.4962 0.5069 0.1356  -0.0474 0.0653  23  GLU A CA  
199  C C   . GLU A 34  ? 0.8150 0.4854 0.4958 0.1456  -0.0481 0.0684  23  GLU A C   
200  O O   . GLU A 34  ? 0.8355 0.4767 0.4936 0.1528  -0.0342 0.0740  23  GLU A O   
201  C CB  . GLU A 34  ? 0.8648 0.5511 0.5563 0.1499  -0.0503 0.0622  23  GLU A CB  
202  C CG  . GLU A 34  ? 0.9440 0.6606 0.6622 0.1425  -0.0583 0.0569  23  GLU A CG  
203  C CD  . GLU A 34  ? 1.0640 0.7742 0.7700 0.1568  -0.0617 0.0536  23  GLU A CD  
204  O OE1 . GLU A 34  ? 1.1106 0.7961 0.7869 0.1753  -0.0645 0.0532  23  GLU A OE1 
205  O OE2 . GLU A 34  ? 1.0898 0.8187 0.8144 0.1504  -0.0615 0.0515  23  GLU A OE2 
206  N N   . GLY A 35  ? 0.7988 0.4807 0.4853 0.1450  -0.0629 0.0649  24  GLY A N   
207  C CA  . GLY A 35  ? 0.8098 0.4707 0.4743 0.1532  -0.0653 0.0675  24  GLY A CA  
208  C C   . GLY A 35  ? 0.7976 0.4626 0.4731 0.1390  -0.0561 0.0733  24  GLY A C   
209  O O   . GLY A 35  ? 0.8100 0.4598 0.4699 0.1436  -0.0575 0.0760  24  GLY A O   
210  N N   . CYS A 36  ? 0.7671 0.4526 0.4691 0.1222  -0.0474 0.0748  25  CYS A N   
211  C CA  . CYS A 36  ? 0.7484 0.4388 0.4617 0.1094  -0.0383 0.0798  25  CYS A CA  
212  C C   . CYS A 36  ? 0.7187 0.4397 0.4583 0.0957  -0.0475 0.0767  25  CYS A C   
213  O O   . CYS A 36  ? 0.7105 0.4424 0.4656 0.0833  -0.0398 0.0796  25  CYS A O   
214  C CB  . CYS A 36  ? 0.7506 0.4370 0.4716 0.1022  -0.0205 0.0838  25  CYS A CB  
215  S SG  . CYS A 36  ? 0.8128 0.4611 0.5042 0.1177  -0.0057 0.0875  25  CYS A SG  
216  N N   . LYS A 37  ? 0.7007 0.4346 0.4455 0.0983  -0.0634 0.0705  26  LYS A N   
217  C CA  . LYS A 37  ? 0.6757 0.4358 0.4444 0.0858  -0.0702 0.0677  26  LYS A CA  
218  C C   . LYS A 37  ? 0.6805 0.4325 0.4414 0.0832  -0.0685 0.0720  26  LYS A C   
219  O O   . LYS A 37  ? 0.6939 0.4244 0.4317 0.0943  -0.0722 0.0731  26  LYS A O   
220  C CB  . LYS A 37  ? 0.6691 0.4440 0.4480 0.0891  -0.0864 0.0593  26  LYS A CB  
221  C CG  . LYS A 37  ? 0.6773 0.4794 0.4842 0.0752  -0.0898 0.0563  26  LYS A CG  
222  C CD  . LYS A 37  ? 0.6991 0.5165 0.5208 0.0774  -0.1042 0.0475  26  LYS A CD  
223  C CE  . LYS A 37  ? 0.7344 0.5571 0.5612 0.0835  -0.1070 0.0435  26  LYS A CE  
224  N NZ  . LYS A 37  ? 0.7434 0.5845 0.5908 0.0844  -0.1202 0.0344  26  LYS A NZ  
225  N N   . VAL A 38  ? 0.6659 0.4331 0.4438 0.0699  -0.0626 0.0745  27  VAL A N   
226  C CA  . VAL A 38  ? 0.6689 0.4323 0.4427 0.0658  -0.0603 0.0788  27  VAL A CA  
227  C C   . VAL A 38  ? 0.6683 0.4545 0.4609 0.0563  -0.0681 0.0749  27  VAL A C   
228  O O   . VAL A 38  ? 0.6750 0.4583 0.4630 0.0540  -0.0686 0.0773  27  VAL A O   
229  C CB  . VAL A 38  ? 0.6661 0.4252 0.4418 0.0596  -0.0452 0.0856  27  VAL A CB  
230  C CG1 . VAL A 38  ? 0.6860 0.4188 0.4429 0.0691  -0.0352 0.0898  27  VAL A CG1 
231  C CG2 . VAL A 38  ? 0.6457 0.4286 0.4464 0.0477  -0.0414 0.0836  27  VAL A CG2 
232  N N   . GLY A 39  ? 0.6566 0.4637 0.4695 0.0511  -0.0725 0.0694  28  GLY A N   
233  C CA  . GLY A 39  ? 0.6494 0.4762 0.4808 0.0425  -0.0773 0.0656  28  GLY A CA  
234  C C   . GLY A 39  ? 0.6430 0.4850 0.4913 0.0429  -0.0859 0.0578  28  GLY A C   
235  O O   . GLY A 39  ? 0.6329 0.4786 0.4859 0.0450  -0.0847 0.0563  28  GLY A O   
236  N N   . ARG A 40  ? 0.6467 0.4980 0.5059 0.0403  -0.0937 0.0527  29  ARG A N   
237  C CA  . ARG A 40  ? 0.6438 0.5114 0.5241 0.0396  -0.1014 0.0446  29  ARG A CA  
238  C C   . ARG A 40  ? 0.6362 0.5166 0.5336 0.0300  -0.1007 0.0422  29  ARG A C   
239  O O   . ARG A 40  ? 0.6509 0.5236 0.5401 0.0302  -0.1041 0.0422  29  ARG A O   
240  C CB  . ARG A 40  ? 0.6698 0.5291 0.5423 0.0515  -0.1153 0.0381  29  ARG A CB  
241  C CG  . ARG A 40  ? 0.6955 0.5735 0.5941 0.0505  -0.1248 0.0283  29  ARG A CG  
242  C CD  . ARG A 40  ? 0.7310 0.6204 0.6427 0.0502  -0.1210 0.0275  29  ARG A CD  
243  N NE  . ARG A 40  ? 0.7443 0.6528 0.6844 0.0487  -0.1281 0.0185  29  ARG A NE  
244  C CZ  . ARG A 40  ? 0.7520 0.6778 0.7168 0.0390  -0.1205 0.0179  29  ARG A CZ  
245  N NH1 . ARG A 40  ? 0.7307 0.6570 0.6931 0.0308  -0.1071 0.0252  29  ARG A NH1 
246  N NH2 . ARG A 40  ? 0.7431 0.6850 0.7349 0.0384  -0.1260 0.0096  29  ARG A NH2 
247  N N   . GLY A 41  ? 0.6131 0.5105 0.5320 0.0225  -0.0954 0.0405  30  GLY A N   
248  C CA  . GLY A 41  ? 0.6000 0.5084 0.5359 0.0137  -0.0919 0.0383  30  GLY A CA  
249  C C   . GLY A 41  ? 0.5819 0.5065 0.5412 0.0087  -0.0865 0.0354  30  GLY A C   
250  O O   . GLY A 41  ? 0.5831 0.5122 0.5483 0.0127  -0.0889 0.0332  30  GLY A O   
251  N N   . THR A 42  ? 0.5672 0.4990 0.5386 0.0007  -0.0782 0.0356  31  THR A N   
252  C CA  . THR A 42  ? 0.5561 0.5005 0.5481 -0.0033 -0.0708 0.0336  31  THR A CA  
253  C C   . THR A 42  ? 0.5430 0.4867 0.5266 -0.0025 -0.0635 0.0390  31  THR A C   
254  O O   . THR A 42  ? 0.5380 0.4895 0.5348 -0.0032 -0.0590 0.0376  31  THR A O   
255  C CB  . THR A 42  ? 0.5783 0.5268 0.5827 -0.0106 -0.0620 0.0326  31  THR A CB  
256  O OG1 . THR A 42  ? 0.6123 0.5526 0.5976 -0.0129 -0.0541 0.0399  31  THR A OG1 
257  C CG2 . THR A 42  ? 0.5772 0.5274 0.5943 -0.0123 -0.0695 0.0255  31  THR A CG2 
258  N N   . TYR A 43  ? 0.5372 0.4712 0.4997 -0.0010 -0.0621 0.0449  32  TYR A N   
259  C CA  . TYR A 43  ? 0.5232 0.4553 0.4772 0.0000  -0.0570 0.0490  32  TYR A CA  
260  C C   . TYR A 43  ? 0.5161 0.4470 0.4695 0.0060  -0.0624 0.0471  32  TYR A C   
261  O O   . TYR A 43  ? 0.5156 0.4478 0.4686 0.0064  -0.0581 0.0484  32  TYR A O   
262  C CB  . TYR A 43  ? 0.5241 0.4468 0.4596 -0.0003 -0.0542 0.0547  32  TYR A CB  
263  C CG  . TYR A 43  ? 0.5272 0.4388 0.4496 0.0037  -0.0606 0.0559  32  TYR A CG  
264  C CD1 . TYR A 43  ? 0.5442 0.4463 0.4554 0.0095  -0.0633 0.0572  32  TYR A CD1 
265  C CD2 . TYR A 43  ? 0.5350 0.4430 0.4538 0.0022  -0.0623 0.0562  32  TYR A CD2 
266  C CE1 . TYR A 43  ? 0.5592 0.4476 0.4553 0.0147  -0.0678 0.0588  32  TYR A CE1 
267  C CE2 . TYR A 43  ? 0.5516 0.4466 0.4553 0.0068  -0.0677 0.0577  32  TYR A CE2 
268  C CZ  . TYR A 43  ? 0.5692 0.4539 0.4610 0.0136  -0.0702 0.0592  32  TYR A CZ  
269  O OH  . TYR A 43  ? 0.6014 0.4701 0.4755 0.0198  -0.0744 0.0611  32  TYR A OH  
270  N N   . GLY A 44  ? 0.5086 0.4355 0.4598 0.0114  -0.0718 0.0439  33  GLY A N   
271  C CA  . GLY A 44  ? 0.5191 0.4426 0.4666 0.0190  -0.0773 0.0420  33  GLY A CA  
272  C C   . GLY A 44  ? 0.5431 0.4504 0.4692 0.0261  -0.0823 0.0440  33  GLY A C   
273  O O   . GLY A 44  ? 0.5552 0.4571 0.4758 0.0279  -0.0883 0.0427  33  GLY A O   
274  N N   . HIS A 45  ? 0.5441 0.4416 0.4568 0.0307  -0.0790 0.0472  34  HIS A N   
275  C CA  . HIS A 45  ? 0.5563 0.4348 0.4467 0.0389  -0.0812 0.0497  34  HIS A CA  
276  C C   . HIS A 45  ? 0.5567 0.4256 0.4359 0.0363  -0.0705 0.0560  34  HIS A C   
277  O O   . HIS A 45  ? 0.5539 0.4270 0.4382 0.0338  -0.0647 0.0565  34  HIS A O   
278  C CB  . HIS A 45  ? 0.5680 0.4404 0.4521 0.0500  -0.0877 0.0460  34  HIS A CB  
279  C CG  . HIS A 45  ? 0.5832 0.4707 0.4862 0.0519  -0.0973 0.0385  34  HIS A CG  
280  N ND1 . HIS A 45  ? 0.6088 0.4925 0.5082 0.0609  -0.1100 0.0328  34  HIS A ND1 
281  C CD2 . HIS A 45  ? 0.5801 0.4857 0.5061 0.0461  -0.0955 0.0356  34  HIS A CD2 
282  C CE1 . HIS A 45  ? 0.6005 0.5021 0.5240 0.0596  -0.1159 0.0260  34  HIS A CE1 
283  N NE2 . HIS A 45  ? 0.5861 0.5007 0.5260 0.0507  -0.1065 0.0280  34  HIS A NE2 
284  N N   . VAL A 46  ? 0.5588 0.4149 0.4242 0.0369  -0.0677 0.0603  35  VAL A N   
285  C CA  . VAL A 46  ? 0.5608 0.4081 0.4189 0.0344  -0.0573 0.0656  35  VAL A CA  
286  C C   . VAL A 46  ? 0.5707 0.3951 0.4081 0.0441  -0.0550 0.0683  35  VAL A C   
287  O O   . VAL A 46  ? 0.5743 0.3866 0.3979 0.0511  -0.0603 0.0688  35  VAL A O   
288  C CB  . VAL A 46  ? 0.5628 0.4138 0.4234 0.0270  -0.0530 0.0691  35  VAL A CB  
289  C CG1 . VAL A 46  ? 0.5682 0.4108 0.4243 0.0250  -0.0430 0.0735  35  VAL A CG1 
290  C CG2 . VAL A 46  ? 0.5583 0.4290 0.4362 0.0187  -0.0536 0.0667  35  VAL A CG2 
291  N N   . TYR A 47  ? 0.5754 0.3922 0.4096 0.0452  -0.0466 0.0700  36  TYR A N   
292  C CA  . TYR A 47  ? 0.5907 0.3828 0.4046 0.0548  -0.0408 0.0730  36  TYR A CA  
293  C C   . TYR A 47  ? 0.5975 0.3815 0.4119 0.0498  -0.0275 0.0775  36  TYR A C   
294  O O   . TYR A 47  ? 0.5826 0.3811 0.4140 0.0400  -0.0234 0.0766  36  TYR A O   
295  C CB  . TYR A 47  ? 0.5900 0.3786 0.4009 0.0610  -0.0406 0.0702  36  TYR A CB  
296  C CG  . TYR A 47  ? 0.6002 0.3977 0.4132 0.0670  -0.0535 0.0648  36  TYR A CG  
297  C CD1 . TYR A 47  ? 0.5968 0.4184 0.4317 0.0596  -0.0588 0.0607  36  TYR A CD1 
298  C CD2 . TYR A 47  ? 0.6241 0.4050 0.4175 0.0812  -0.0599 0.0634  36  TYR A CD2 
299  C CE1 . TYR A 47  ? 0.6073 0.4382 0.4484 0.0647  -0.0700 0.0552  36  TYR A CE1 
300  C CE2 . TYR A 47  ? 0.6367 0.4275 0.4351 0.0871  -0.0730 0.0572  36  TYR A CE2 
301  C CZ  . TYR A 47  ? 0.6427 0.4595 0.4670 0.0783  -0.0777 0.0530  36  TYR A CZ  
302  O OH  . TYR A 47  ? 0.6738 0.5012 0.5066 0.0840  -0.0900 0.0463  36  TYR A OH  
303  N N   . LYS A 48  ? 0.6164 0.3758 0.4120 0.0576  -0.0205 0.0819  37  LYS A N   
304  C CA  . LYS A 48  ? 0.6273 0.3750 0.4236 0.0546  -0.0059 0.0859  37  LYS A CA  
305  C C   . LYS A 48  ? 0.6497 0.3852 0.4401 0.0599  0.0011  0.0847  37  LYS A C   
306  O O   . LYS A 48  ? 0.6600 0.3763 0.4290 0.0725  0.0001  0.0852  37  LYS A O   
307  C CB  . LYS A 48  ? 0.6573 0.3813 0.4342 0.0620  -0.0003 0.0918  37  LYS A CB  
308  C CG  . LYS A 48  ? 0.7018 0.4116 0.4812 0.0597  0.0168  0.0960  37  LYS A CG  
309  C CD  . LYS A 48  ? 0.7752 0.4594 0.5338 0.0680  0.0233  0.1026  37  LYS A CD  
310  C CE  . LYS A 48  ? 0.8406 0.5114 0.6055 0.0652  0.0420  0.1067  37  LYS A CE  
311  N NZ  . LYS A 48  ? 0.9003 0.5410 0.6420 0.0753  0.0510  0.1140  37  LYS A NZ  
312  N N   . ALA A 49  ? 0.6537 0.4005 0.4619 0.0510  0.0070  0.0822  38  ALA A N   
313  C CA  . ALA A 49  ? 0.6785 0.4155 0.4827 0.0547  0.0137  0.0805  38  ALA A CA  
314  C C   . ALA A 49  ? 0.7036 0.4276 0.5133 0.0508  0.0306  0.0820  38  ALA A C   
315  O O   . ALA A 49  ? 0.6989 0.4304 0.5243 0.0420  0.0351  0.0825  38  ALA A O   
316  C CB  . ALA A 49  ? 0.6649 0.4249 0.4844 0.0487  0.0056  0.0752  38  ALA A CB  
317  N N   . LYS A 50  ? 0.7315 0.4356 0.5292 0.0576  0.0403  0.0822  39  LYS A N   
318  C CA  . LYS A 50  ? 0.7575 0.4479 0.5623 0.0537  0.0579  0.0825  39  LYS A CA  
319  C C   . LYS A 50  ? 0.7714 0.4670 0.5825 0.0510  0.0593  0.0777  39  LYS A C   
320  O O   . LYS A 50  ? 0.7756 0.4740 0.5756 0.0575  0.0503  0.0764  39  LYS A O   
321  C CB  . LYS A 50  ? 0.8123 0.4662 0.5916 0.0664  0.0722  0.0880  39  LYS A CB  
322  C CG  . LYS A 50  ? 0.8901 0.5338 0.6678 0.0666  0.0787  0.0932  39  LYS A CG  
323  C CD  . LYS A 50  ? 0.9501 0.5943 0.7522 0.0556  0.0943  0.0926  39  LYS A CD  
324  C CE  . LYS A 50  ? 1.0178 0.6335 0.8086 0.0619  0.1108  0.0994  39  LYS A CE  
325  N NZ  . LYS A 50  ? 1.0571 0.6751 0.8380 0.0654  0.1015  0.1039  39  LYS A NZ  
326  N N   . ARG A 51  ? 0.7774 0.4743 0.6068 0.0416  0.0702  0.0747  40  ARG A N   
327  C CA  . ARG A 51  ? 0.7987 0.4971 0.6322 0.0393  0.0729  0.0702  40  ARG A CA  
328  C C   . ARG A 51  ? 0.8319 0.4984 0.6406 0.0516  0.0861  0.0731  40  ARG A C   
329  O O   . ARG A 51  ? 0.8427 0.4844 0.6415 0.0567  0.1006  0.0772  40  ARG A O   
330  C CB  . ARG A 51  ? 0.8155 0.5242 0.6766 0.0258  0.0797  0.0648  40  ARG A CB  
331  C CG  . ARG A 51  ? 0.8518 0.5900 0.7351 0.0154  0.0670  0.0614  40  ARG A CG  
332  C CD  . ARG A 51  ? 0.8966 0.6436 0.8067 0.0036  0.0727  0.0548  40  ARG A CD  
333  N NE  . ARG A 51  ? 0.9552 0.7022 0.8682 0.0011  0.0742  0.0495  40  ARG A NE  
334  C CZ  . ARG A 51  ? 0.9999 0.7590 0.9352 -0.0088 0.0737  0.0417  40  ARG A CZ  
335  N NH1 . ARG A 51  ? 1.0131 0.7699 0.9475 -0.0102 0.0748  0.0372  40  ARG A NH1 
336  N NH2 . ARG A 51  ? 0.9917 0.7653 0.9499 -0.0169 0.0711  0.0378  40  ARG A NH2 
337  N N   . LYS A 52  ? 0.8452 0.5110 0.6424 0.0574  0.0817  0.0715  41  LYS A N   
338  C CA  . LYS A 52  ? 0.8805 0.5162 0.6516 0.0705  0.0934  0.0740  41  LYS A CA  
339  C C   . LYS A 52  ? 0.9145 0.5355 0.6944 0.0644  0.1127  0.0718  41  LYS A C   
340  O O   . LYS A 52  ? 0.9349 0.5242 0.6967 0.0732  0.1299  0.0752  41  LYS A O   
341  C CB  . LYS A 52  ? 0.8837 0.5255 0.6409 0.0793  0.0813  0.0727  41  LYS A CB  
342  C CG  . LYS A 52  ? 0.9002 0.5425 0.6398 0.0914  0.0672  0.0751  41  LYS A CG  
343  C CD  . LYS A 52  ? 0.9308 0.5770 0.6582 0.1012  0.0573  0.0732  41  LYS A CD  
344  C CE  . LYS A 52  ? 0.9681 0.6183 0.6830 0.1123  0.0412  0.0735  41  LYS A CE  
345  N NZ  . LYS A 52  ? 1.0010 0.6571 0.7078 0.1221  0.0311  0.0707  41  LYS A NZ  
346  N N   . ASP A 53  ? 0.9173 0.5597 0.7250 0.0496  0.1106  0.0658  42  ASP A N   
347  C CA  . ASP A 53  ? 0.9381 0.5691 0.7592 0.0418  0.1277  0.0620  42  ASP A CA  
348  C C   . ASP A 53  ? 0.9561 0.5742 0.7905 0.0369  0.1436  0.0630  42  ASP A C   
349  O O   . ASP A 53  ? 0.9602 0.5653 0.8065 0.0313  0.1604  0.0598  42  ASP A O   
350  C CB  . ASP A 53  ? 0.9452 0.6017 0.7910 0.0285  0.1192  0.0543  42  ASP A CB  
351  C CG  . ASP A 53  ? 0.9839 0.6702 0.8558 0.0171  0.1059  0.0507  42  ASP A CG  
352  O OD1 . ASP A 53  ? 0.9890 0.6762 0.8650 0.0168  0.1061  0.0538  42  ASP A OD1 
353  O OD2 . ASP A 53  ? 1.0035 0.7108 0.8895 0.0094  0.0954  0.0451  42  ASP A OD2 
354  N N   . GLY A 54  ? 0.9667 0.5888 0.8005 0.0388  0.1385  0.0672  43  GLY A N   
355  C CA  . GLY A 54  ? 0.9861 0.5953 0.8297 0.0363  0.1530  0.0697  43  GLY A CA  
356  C C   . GLY A 54  ? 0.9820 0.6045 0.8639 0.0204  0.1601  0.0631  43  GLY A C   
357  O O   . GLY A 54  ? 0.9886 0.5956 0.8796 0.0191  0.1767  0.0651  43  GLY A O   
358  N N   . LYS A 55  ? 0.9670 0.6176 0.8719 0.0089  0.1476  0.0550  44  LYS A N   
359  C CA  . LYS A 55  ? 0.9607 0.6259 0.9036 -0.0056 0.1517  0.0469  44  LYS A CA  
360  C C   . LYS A 55  ? 0.9537 0.6384 0.9149 -0.0107 0.1434  0.0474  44  LYS A C   
361  O O   . LYS A 55  ? 0.9457 0.6411 0.9388 -0.0212 0.1475  0.0410  44  LYS A O   
362  C CB  . LYS A 55  ? 0.9775 0.6619 0.9376 -0.0150 0.1424  0.0371  44  LYS A CB  
363  C CG  . LYS A 55  ? 1.0292 0.7314 0.9743 -0.0117 0.1221  0.0375  44  LYS A CG  
364  C CD  . LYS A 55  ? 1.0801 0.7869 1.0304 -0.0165 0.1196  0.0300  44  LYS A CD  
365  C CE  . LYS A 55  ? 1.1373 0.8149 1.0703 -0.0107 0.1370  0.0318  44  LYS A CE  
366  N NZ  . LYS A 55  ? 1.1568 0.8383 1.0934 -0.0153 0.1344  0.0248  44  LYS A NZ  
367  N N   . ASP A 56  ? 0.9550 0.6436 0.8965 -0.0031 0.1323  0.0545  45  ASP A N   
368  C CA  . ASP A 56  ? 0.9473 0.6502 0.8980 -0.0053 0.1251  0.0572  45  ASP A CA  
369  C C   . ASP A 56  ? 0.9513 0.6301 0.8729 0.0073  0.1315  0.0676  45  ASP A C   
370  O O   . ASP A 56  ? 0.9700 0.6334 0.8619 0.0182  0.1299  0.0717  45  ASP A O   
371  C CB  . ASP A 56  ? 0.9725 0.7048 0.9229 -0.0074 0.1017  0.0553  45  ASP A CB  
372  C CG  . ASP A 56  ? 1.0310 0.7918 1.0117 -0.0189 0.0917  0.0465  45  ASP A CG  
373  O OD1 . ASP A 56  ? 1.0439 0.8087 1.0487 -0.0253 0.0984  0.0435  45  ASP A OD1 
374  O OD2 . ASP A 56  ? 1.0526 0.8312 1.0325 -0.0208 0.0770  0.0426  45  ASP A OD2 
375  N N   . ASP A 57  ? 0.9308 0.6068 0.8596 0.0067  0.1372  0.0715  46  ASP A N   
376  C CA  . ASP A 57  ? 0.9361 0.5904 0.8355 0.0191  0.1404  0.0813  46  ASP A CA  
377  C C   . ASP A 57  ? 0.9003 0.5769 0.7970 0.0186  0.1211  0.0835  46  ASP A C   
378  O O   . ASP A 57  ? 0.9136 0.5761 0.7884 0.0276  0.1210  0.0908  46  ASP A O   
379  C CB  . ASP A 57  ? 0.9797 0.6079 0.8825 0.0214  0.1633  0.0861  46  ASP A CB  
380  C CG  . ASP A 57  ? 1.0899 0.6860 0.9548 0.0373  0.1700  0.0964  46  ASP A CG  
381  O OD1 . ASP A 57  ? 1.1208 0.6991 0.9549 0.0489  0.1682  0.0986  46  ASP A OD1 
382  O OD2 . ASP A 57  ? 1.1263 0.7145 0.9914 0.0391  0.1764  0.1020  46  ASP A OD2 
383  N N   . LYS A 58  ? 0.8502 0.5597 0.7677 0.0087  0.1055  0.0769  47  LYS A N   
384  C CA  . LYS A 58  ? 0.8191 0.5505 0.7369 0.0071  0.0889  0.0779  47  LYS A CA  
385  C C   . LYS A 58  ? 0.7957 0.5232 0.6850 0.0163  0.0772  0.0818  47  LYS A C   
386  O O   . LYS A 58  ? 0.8028 0.5223 0.6784 0.0215  0.0759  0.0808  47  LYS A O   
387  C CB  . LYS A 58  ? 0.8255 0.5883 0.7674 -0.0034 0.0762  0.0695  47  LYS A CB  
388  C CG  . LYS A 58  ? 0.8686 0.6404 0.8426 -0.0132 0.0835  0.0624  47  LYS A CG  
389  C CD  . LYS A 58  ? 0.9177 0.7166 0.9085 -0.0207 0.0692  0.0533  47  LYS A CD  
390  C CE  . LYS A 58  ? 0.9734 0.7933 0.9613 -0.0208 0.0531  0.0541  47  LYS A CE  
391  N NZ  . LYS A 58  ? 0.9952 0.8384 0.9985 -0.0267 0.0409  0.0451  47  LYS A NZ  
392  N N   . ASP A 59  ? 0.7618 0.4964 0.6439 0.0181  0.0681  0.0856  48  ASP A N   
393  C CA  . ASP A 59  ? 0.7381 0.4742 0.5993 0.0251  0.0547  0.0875  48  ASP A CA  
394  C C   . ASP A 59  ? 0.6794 0.4456 0.5552 0.0174  0.0400  0.0819  48  ASP A C   
395  O O   . ASP A 59  ? 0.6637 0.4481 0.5596 0.0088  0.0380  0.0789  48  ASP A O   
396  C CB  . ASP A 59  ? 0.7706 0.4975 0.6167 0.0307  0.0530  0.0940  48  ASP A CB  
397  C CG  . ASP A 59  ? 0.8591 0.5520 0.6838 0.0414  0.0669  0.1002  48  ASP A CG  
398  O OD1 . ASP A 59  ? 0.9013 0.5761 0.7090 0.0498  0.0705  0.1002  48  ASP A OD1 
399  O OD2 . ASP A 59  ? 0.8864 0.5691 0.7098 0.0423  0.0748  0.1053  48  ASP A OD2 
400  N N   . TYR A 60  ? 0.6495 0.4200 0.5152 0.0213  0.0302  0.0802  49  TYR A N   
401  C CA  . TYR A 60  ? 0.6135 0.4095 0.4908 0.0153  0.0179  0.0755  49  TYR A CA  
402  C C   . TYR A 60  ? 0.5828 0.3840 0.4486 0.0198  0.0062  0.0772  49  TYR A C   
403  O O   . TYR A 60  ? 0.5846 0.3698 0.4322 0.0285  0.0056  0.0805  49  TYR A O   
404  C CB  . TYR A 60  ? 0.6137 0.4129 0.4951 0.0143  0.0177  0.0707  49  TYR A CB  
405  C CG  . TYR A 60  ? 0.6215 0.4216 0.5197 0.0073  0.0266  0.0667  49  TYR A CG  
406  C CD1 . TYR A 60  ? 0.6450 0.4242 0.5399 0.0098  0.0404  0.0677  49  TYR A CD1 
407  C CD2 . TYR A 60  ? 0.6222 0.4429 0.5395 -0.0012 0.0214  0.0613  49  TYR A CD2 
408  C CE1 . TYR A 60  ? 0.6535 0.4337 0.5672 0.0025  0.0489  0.0628  49  TYR A CE1 
409  C CE2 . TYR A 60  ? 0.6294 0.4517 0.5640 -0.0075 0.0278  0.0561  49  TYR A CE2 
410  C CZ  . TYR A 60  ? 0.6542 0.4572 0.5888 -0.0064 0.0415  0.0565  49  TYR A CZ  
411  O OH  . TYR A 60  ? 0.6702 0.4753 0.6252 -0.0136 0.0481  0.0501  49  TYR A OH  
412  N N   . ALA A 61  ? 0.5545 0.3769 0.4308 0.0143  -0.0027 0.0745  50  ALA A N   
413  C CA  . ALA A 61  ? 0.5478 0.3770 0.4179 0.0170  -0.0129 0.0747  50  ALA A CA  
414  C C   . ALA A 61  ? 0.5351 0.3754 0.4110 0.0165  -0.0182 0.0703  50  ALA A C   
415  O O   . ALA A 61  ? 0.5308 0.3831 0.4189 0.0106  -0.0177 0.0671  50  ALA A O   
416  C CB  . ALA A 61  ? 0.5392 0.3819 0.4162 0.0116  -0.0167 0.0755  50  ALA A CB  
417  N N   . LEU A 62  ? 0.5322 0.3670 0.3986 0.0235  -0.0231 0.0698  51  LEU A N   
418  C CA  . LEU A 62  ? 0.5259 0.3701 0.3976 0.0243  -0.0277 0.0661  51  LEU A CA  
419  C C   . LEU A 62  ? 0.5241 0.3794 0.3994 0.0251  -0.0372 0.0646  51  LEU A C   
420  O O   . LEU A 62  ? 0.5451 0.3925 0.4107 0.0312  -0.0419 0.0654  51  LEU A O   
421  C CB  . LEU A 62  ? 0.5240 0.3526 0.3829 0.0334  -0.0259 0.0660  51  LEU A CB  
422  C CG  . LEU A 62  ? 0.5343 0.3592 0.3950 0.0326  -0.0190 0.0645  51  LEU A CG  
423  C CD1 . LEU A 62  ? 0.5575 0.3665 0.4024 0.0437  -0.0183 0.0647  51  LEU A CD1 
424  C CD2 . LEU A 62  ? 0.5213 0.3650 0.3969 0.0262  -0.0222 0.0609  51  LEU A CD2 
425  N N   . LYS A 63  ? 0.4974 0.3692 0.3860 0.0199  -0.0396 0.0620  52  LYS A N   
426  C CA  . LYS A 63  ? 0.4884 0.3708 0.3838 0.0199  -0.0467 0.0600  52  LYS A CA  
427  C C   . LYS A 63  ? 0.4948 0.3849 0.3982 0.0222  -0.0496 0.0565  52  LYS A C   
428  O O   . LYS A 63  ? 0.4949 0.3904 0.4042 0.0191  -0.0457 0.0558  52  LYS A O   
429  C CB  . LYS A 63  ? 0.4760 0.3697 0.3799 0.0125  -0.0455 0.0605  52  LYS A CB  
430  C CG  . LYS A 63  ? 0.4778 0.3813 0.3907 0.0118  -0.0505 0.0582  52  LYS A CG  
431  C CD  . LYS A 63  ? 0.5012 0.4105 0.4172 0.0064  -0.0484 0.0595  52  LYS A CD  
432  C CE  . LYS A 63  ? 0.5096 0.4255 0.4300 0.0022  -0.0429 0.0596  52  LYS A CE  
433  N NZ  . LYS A 63  ? 0.5109 0.4324 0.4341 -0.0013 -0.0408 0.0602  52  LYS A NZ  
434  N N   . GLN A 64  ? 0.5051 0.3958 0.4093 0.0280  -0.0569 0.0540  53  GLN A N   
435  C CA  . GLN A 64  ? 0.5146 0.4153 0.4305 0.0301  -0.0600 0.0502  53  GLN A CA  
436  C C   . GLN A 64  ? 0.5184 0.4332 0.4505 0.0244  -0.0620 0.0482  53  GLN A C   
437  O O   . GLN A 64  ? 0.5183 0.4335 0.4517 0.0252  -0.0678 0.0466  53  GLN A O   
438  C CB  . GLN A 64  ? 0.5404 0.4354 0.4507 0.0404  -0.0678 0.0473  53  GLN A CB  
439  C CG  . GLN A 64  ? 0.5807 0.4872 0.5052 0.0429  -0.0706 0.0433  53  GLN A CG  
440  C CD  . GLN A 64  ? 0.6865 0.5893 0.6067 0.0541  -0.0805 0.0392  53  GLN A CD  
441  O OE1 . GLN A 64  ? 0.7183 0.6189 0.6362 0.0578  -0.0889 0.0366  53  GLN A OE1 
442  N NE2 . GLN A 64  ? 0.7092 0.6106 0.6273 0.0608  -0.0802 0.0381  53  GLN A NE2 
443  N N   . ILE A 65  ? 0.5182 0.4421 0.4608 0.0189  -0.0563 0.0483  54  ILE A N   
444  C CA  . ILE A 65  ? 0.5260 0.4606 0.4830 0.0139  -0.0552 0.0468  54  ILE A CA  
445  C C   . ILE A 65  ? 0.5314 0.4742 0.5041 0.0168  -0.0617 0.0417  54  ILE A C   
446  O O   . ILE A 65  ? 0.5314 0.4750 0.5066 0.0226  -0.0658 0.0392  54  ILE A O   
447  C CB  . ILE A 65  ? 0.5335 0.4724 0.4950 0.0100  -0.0468 0.0480  54  ILE A CB  
448  C CG1 . ILE A 65  ? 0.5483 0.4807 0.4964 0.0073  -0.0425 0.0514  54  ILE A CG1 
449  C CG2 . ILE A 65  ? 0.5362 0.4835 0.5121 0.0063  -0.0431 0.0467  54  ILE A CG2 
450  C CD1 . ILE A 65  ? 0.5588 0.4926 0.5068 0.0058  -0.0365 0.0518  54  ILE A CD1 
451  N N   . GLU A 66  ? 0.5359 0.4842 0.5189 0.0131  -0.0630 0.0396  55  GLU A N   
452  C CA  . GLU A 66  ? 0.5369 0.4945 0.5394 0.0144  -0.0694 0.0333  55  GLU A CA  
453  C C   . GLU A 66  ? 0.5378 0.5062 0.5605 0.0140  -0.0648 0.0307  55  GLU A C   
454  O O   . GLU A 66  ? 0.5396 0.5091 0.5646 0.0098  -0.0544 0.0338  55  GLU A O   
455  C CB  . GLU A 66  ? 0.5544 0.5143 0.5638 0.0086  -0.0687 0.0320  55  GLU A CB  
456  C CG  . GLU A 66  ? 0.6101 0.5805 0.6439 0.0082  -0.0746 0.0242  55  GLU A CG  
457  C CD  . GLU A 66  ? 0.7057 0.6747 0.7378 0.0157  -0.0895 0.0186  55  GLU A CD  
458  O OE1 . GLU A 66  ? 0.7295 0.6855 0.7377 0.0204  -0.0944 0.0216  55  GLU A OE1 
459  O OE2 . GLU A 66  ? 0.7443 0.7243 0.7990 0.0178  -0.0961 0.0108  55  GLU A OE2 
460  N N   . GLY A 67  ? 0.5346 0.5096 0.5701 0.0195  -0.0727 0.0252  56  GLY A N   
461  C CA  . GLY A 67  ? 0.5315 0.5174 0.5887 0.0201  -0.0690 0.0224  56  GLY A CA  
462  C C   . GLY A 67  ? 0.5442 0.5259 0.5912 0.0239  -0.0641 0.0263  56  GLY A C   
463  O O   . GLY A 67  ? 0.5634 0.5338 0.5870 0.0253  -0.0630 0.0310  56  GLY A O   
464  N N   . THR A 68  ? 0.5316 0.5221 0.5971 0.0255  -0.0607 0.0241  57  THR A N   
465  C CA  . THR A 68  ? 0.5391 0.5252 0.5952 0.0291  -0.0554 0.0278  57  THR A CA  
466  C C   . THR A 68  ? 0.5242 0.5082 0.5813 0.0237  -0.0415 0.0322  57  THR A C   
467  O O   . THR A 68  ? 0.5179 0.5060 0.5885 0.0185  -0.0352 0.0317  57  THR A O   
468  C CB  . THR A 68  ? 0.5633 0.5572 0.6328 0.0370  -0.0613 0.0234  57  THR A CB  
469  O OG1 . THR A 68  ? 0.5775 0.5840 0.6761 0.0346  -0.0554 0.0206  57  THR A OG1 
470  C CG2 . THR A 68  ? 0.5652 0.5612 0.6347 0.0438  -0.0765 0.0174  57  THR A CG2 
471  N N   . GLY A 69  ? 0.5139 0.4895 0.5545 0.0258  -0.0367 0.0364  58  GLY A N   
472  C CA  . GLY A 69  ? 0.5034 0.4738 0.5392 0.0230  -0.0250 0.0404  58  GLY A CA  
473  C C   . GLY A 69  ? 0.4926 0.4561 0.5142 0.0180  -0.0219 0.0431  58  GLY A C   
474  O O   . GLY A 69  ? 0.5030 0.4637 0.5141 0.0167  -0.0284 0.0431  58  GLY A O   
475  N N   . ILE A 70  ? 0.4783 0.4381 0.4989 0.0162  -0.0118 0.0454  59  ILE A N   
476  C CA  . ILE A 70  ? 0.4776 0.4307 0.4838 0.0130  -0.0085 0.0477  59  ILE A CA  
477  C C   . ILE A 70  ? 0.4517 0.4081 0.4717 0.0100  -0.0018 0.0470  59  ILE A C   
478  O O   . ILE A 70  ? 0.4500 0.4039 0.4764 0.0112  0.0089  0.0481  59  ILE A O   
479  C CB  . ILE A 70  ? 0.5009 0.4435 0.4894 0.0153  -0.0027 0.0505  59  ILE A CB  
480  C CG1 . ILE A 70  ? 0.5289 0.4679 0.5064 0.0175  -0.0086 0.0504  59  ILE A CG1 
481  C CG2 . ILE A 70  ? 0.5172 0.4533 0.4905 0.0135  -0.0007 0.0519  59  ILE A CG2 
482  C CD1 . ILE A 70  ? 0.5587 0.4920 0.5317 0.0214  -0.0031 0.0515  59  ILE A CD1 
483  N N   . SER A 71  ? 0.4316 0.3926 0.4568 0.0066  -0.0073 0.0451  60  SER A N   
484  C CA  . SER A 71  ? 0.4217 0.3851 0.4599 0.0030  -0.0010 0.0440  60  SER A CA  
485  C C   . SER A 71  ? 0.4361 0.3891 0.4554 0.0024  0.0071  0.0478  60  SER A C   
486  O O   . SER A 71  ? 0.4407 0.3872 0.4395 0.0043  0.0047  0.0503  60  SER A O   
487  C CB  . SER A 71  ? 0.4277 0.3976 0.4740 0.0001  -0.0108 0.0404  60  SER A CB  
488  O OG  . SER A 71  ? 0.4625 0.4271 0.4880 0.0000  -0.0183 0.0426  60  SER A OG  
489  N N   . MET A 72  ? 0.4422 0.3933 0.4682 0.0001  0.0163  0.0478  61  MET A N   
490  C CA  . MET A 72  ? 0.4611 0.4013 0.4672 0.0010  0.0237  0.0513  61  MET A CA  
491  C C   . MET A 72  ? 0.4571 0.3970 0.4467 -0.0004 0.0136  0.0522  61  MET A C   
492  O O   . MET A 72  ? 0.4673 0.4003 0.4367 0.0023  0.0135  0.0546  61  MET A O   
493  C CB  . MET A 72  ? 0.4755 0.4133 0.4928 -0.0016 0.0353  0.0507  61  MET A CB  
494  C CG  . MET A 72  ? 0.5244 0.4606 0.5591 -0.0002 0.0484  0.0501  61  MET A CG  
495  S SD  . MET A 72  ? 0.6652 0.5847 0.6754 0.0082  0.0599  0.0551  61  MET A SD  
496  C CE  . MET A 72  ? 0.5522 0.4572 0.5409 0.0102  0.0702  0.0580  61  MET A CE  
497  N N   . SER A 73  ? 0.4470 0.3940 0.4456 -0.0040 0.0045  0.0500  62  SER A N   
498  C CA  . SER A 73  ? 0.4568 0.4027 0.4419 -0.0051 -0.0042 0.0512  62  SER A CA  
499  C C   . SER A 73  ? 0.4508 0.3945 0.4223 -0.0024 -0.0103 0.0525  62  SER A C   
500  O O   . SER A 73  ? 0.4594 0.3984 0.4153 -0.0017 -0.0106 0.0546  62  SER A O   
501  C CB  . SER A 73  ? 0.4790 0.4310 0.4762 -0.0078 -0.0128 0.0481  62  SER A CB  
502  O OG  . SER A 73  ? 0.5268 0.4754 0.5096 -0.0080 -0.0202 0.0499  62  SER A OG  
503  N N   . ALA A 74  ? 0.4354 0.3823 0.4139 -0.0005 -0.0145 0.0508  63  ALA A N   
504  C CA  . ALA A 74  ? 0.4372 0.3809 0.4045 0.0017  -0.0189 0.0516  63  ALA A CA  
505  C C   . ALA A 74  ? 0.4404 0.3782 0.3958 0.0037  -0.0132 0.0529  63  ALA A C   
506  O O   . ALA A 74  ? 0.4403 0.3744 0.3833 0.0040  -0.0160 0.0533  63  ALA A O   
507  C CB  . ALA A 74  ? 0.4305 0.3777 0.4072 0.0042  -0.0226 0.0496  63  ALA A CB  
508  N N   . CYS A 75  ? 0.4383 0.3744 0.3976 0.0055  -0.0048 0.0532  64  CYS A N   
509  C CA  . CYS A 75  ? 0.4641 0.3921 0.4100 0.0093  0.0009  0.0542  64  CYS A CA  
510  C C   . CYS A 75  ? 0.4617 0.3852 0.3919 0.0098  0.0005  0.0549  64  CYS A C   
511  O O   . CYS A 75  ? 0.4690 0.3887 0.3868 0.0120  -0.0029 0.0540  64  CYS A O   
512  C CB  . CYS A 75  ? 0.4995 0.4241 0.4524 0.0118  0.0121  0.0549  64  CYS A CB  
513  S SG  . CYS A 75  ? 0.6427 0.5532 0.5753 0.0191  0.0198  0.0563  64  CYS A SG  
514  N N   . ARG A 76  ? 0.4456 0.3700 0.3773 0.0078  0.0031  0.0560  65  ARG A N   
515  C CA  . ARG A 76  ? 0.4499 0.3705 0.3669 0.0090  0.0030  0.0570  65  ARG A CA  
516  C C   . ARG A 76  ? 0.4503 0.3747 0.3633 0.0067  -0.0069 0.0563  65  ARG A C   
517  O O   . ARG A 76  ? 0.4648 0.3865 0.3660 0.0093  -0.0093 0.0554  65  ARG A O   
518  C CB  . ARG A 76  ? 0.4630 0.3834 0.3838 0.0067  0.0086  0.0585  65  ARG A CB  
519  C CG  . ARG A 76  ? 0.4943 0.4094 0.3980 0.0093  0.0100  0.0599  65  ARG A CG  
520  C CD  . ARG A 76  ? 0.5132 0.4267 0.4192 0.0070  0.0164  0.0616  65  ARG A CD  
521  N NE  . ARG A 76  ? 0.5234 0.4287 0.4099 0.0121  0.0210  0.0633  65  ARG A NE  
522  C CZ  . ARG A 76  ? 0.5162 0.4226 0.3949 0.0112  0.0174  0.0647  65  ARG A CZ  
523  N NH1 . ARG A 76  ? 0.4881 0.4018 0.3760 0.0053  0.0099  0.0650  65  ARG A NH1 
524  N NH2 . ARG A 76  ? 0.5137 0.4126 0.3740 0.0173  0.0217  0.0660  65  ARG A NH2 
525  N N   . GLU A 77  ? 0.4299 0.3596 0.3530 0.0027  -0.0124 0.0562  66  GLU A N   
526  C CA  . GLU A 77  ? 0.4294 0.3603 0.3496 0.0008  -0.0195 0.0562  66  GLU A CA  
527  C C   . GLU A 77  ? 0.4315 0.3607 0.3475 0.0024  -0.0222 0.0540  66  GLU A C   
528  O O   . GLU A 77  ? 0.4416 0.3704 0.3521 0.0023  -0.0251 0.0529  66  GLU A O   
529  C CB  . GLU A 77  ? 0.4573 0.3907 0.3865 -0.0016 -0.0236 0.0566  66  GLU A CB  
530  C CG  . GLU A 77  ? 0.5168 0.4481 0.4428 -0.0024 -0.0289 0.0570  66  GLU A CG  
531  C CD  . GLU A 77  ? 0.5889 0.5185 0.5094 -0.0039 -0.0302 0.0593  66  GLU A CD  
532  O OE1 . GLU A 77  ? 0.6319 0.5622 0.5473 -0.0040 -0.0276 0.0601  66  GLU A OE1 
533  O OE2 . GLU A 77  ? 0.5856 0.5117 0.5052 -0.0041 -0.0333 0.0605  66  GLU A OE2 
534  N N   . ILE A 78  ? 0.4139 0.3421 0.3336 0.0039  -0.0211 0.0528  67  ILE A N   
535  C CA  . ILE A 78  ? 0.4070 0.3321 0.3224 0.0053  -0.0230 0.0503  67  ILE A CA  
536  C C   . ILE A 78  ? 0.4246 0.3459 0.3291 0.0091  -0.0218 0.0483  67  ILE A C   
537  O O   . ILE A 78  ? 0.4326 0.3535 0.3332 0.0090  -0.0262 0.0453  67  ILE A O   
538  C CB  . ILE A 78  ? 0.3985 0.3226 0.3192 0.0067  -0.0211 0.0501  67  ILE A CB  
539  C CG1 . ILE A 78  ? 0.4048 0.3316 0.3339 0.0050  -0.0242 0.0510  67  ILE A CG1 
540  C CG2 . ILE A 78  ? 0.3981 0.3170 0.3124 0.0087  -0.0218 0.0475  67  ILE A CG2 
541  C CD1 . ILE A 78  ? 0.4175 0.3455 0.3542 0.0074  -0.0225 0.0509  67  ILE A CD1 
542  N N   . ALA A 79  ? 0.4225 0.3401 0.3221 0.0130  -0.0156 0.0496  68  ALA A N   
543  C CA  . ALA A 79  ? 0.4358 0.3464 0.3206 0.0191  -0.0142 0.0478  68  ALA A CA  
544  C C   . ALA A 79  ? 0.4323 0.3448 0.3102 0.0198  -0.0189 0.0462  68  ALA A C   
545  O O   . ALA A 79  ? 0.4373 0.3474 0.3070 0.0234  -0.0238 0.0420  68  ALA A O   
546  C CB  . ALA A 79  ? 0.4449 0.3482 0.3242 0.0240  -0.0042 0.0504  68  ALA A CB  
547  N N   . LEU A 80  ? 0.4265 0.3433 0.3082 0.0166  -0.0180 0.0490  69  LEU A N   
548  C CA  . LEU A 80  ? 0.4266 0.3456 0.3023 0.0176  -0.0217 0.0482  69  LEU A CA  
549  C C   . LEU A 80  ? 0.4221 0.3475 0.3060 0.0133  -0.0294 0.0456  69  LEU A C   
550  O O   . LEU A 80  ? 0.4265 0.3531 0.3064 0.0160  -0.0344 0.0413  69  LEU A O   
551  C CB  . LEU A 80  ? 0.4255 0.3450 0.3005 0.0163  -0.0168 0.0524  69  LEU A CB  
552  C CG  . LEU A 80  ? 0.4562 0.3674 0.3222 0.0212  -0.0071 0.0545  69  LEU A CG  
553  C CD1 . LEU A 80  ? 0.4674 0.3787 0.3332 0.0191  -0.0023 0.0581  69  LEU A CD1 
554  C CD2 . LEU A 80  ? 0.4549 0.3574 0.3018 0.0309  -0.0063 0.0521  69  LEU A CD2 
555  N N   . LEU A 81  ? 0.4136 0.3420 0.3089 0.0074  -0.0300 0.0474  70  LEU A N   
556  C CA  . LEU A 81  ? 0.4226 0.3543 0.3255 0.0036  -0.0345 0.0454  70  LEU A CA  
557  C C   . LEU A 81  ? 0.4277 0.3585 0.3330 0.0040  -0.0380 0.0397  70  LEU A C   
558  O O   . LEU A 81  ? 0.4213 0.3549 0.3336 0.0016  -0.0413 0.0363  70  LEU A O   
559  C CB  . LEU A 81  ? 0.4176 0.3488 0.3280 -0.0008 -0.0333 0.0490  70  LEU A CB  
560  C CG  . LEU A 81  ? 0.4283 0.3600 0.3372 -0.0019 -0.0317 0.0536  70  LEU A CG  
561  C CD1 . LEU A 81  ? 0.4270 0.3559 0.3404 -0.0044 -0.0319 0.0561  70  LEU A CD1 
562  C CD2 . LEU A 81  ? 0.4353 0.3695 0.3410 -0.0014 -0.0328 0.0537  70  LEU A CD2 
563  N N   . ARG A 82  ? 0.4297 0.3562 0.3298 0.0071  -0.0368 0.0383  71  ARG A N   
564  C CA  . ARG A 82  ? 0.4257 0.3495 0.3253 0.0083  -0.0401 0.0327  71  ARG A CA  
565  C C   . ARG A 82  ? 0.4273 0.3522 0.3204 0.0130  -0.0460 0.0267  71  ARG A C   
566  O O   . ARG A 82  ? 0.4310 0.3561 0.3278 0.0126  -0.0511 0.0200  71  ARG A O   
567  C CB  . ARG A 82  ? 0.4499 0.3673 0.3431 0.0117  -0.0361 0.0340  71  ARG A CB  
568  C CG  . ARG A 82  ? 0.4874 0.3999 0.3790 0.0125  -0.0384 0.0292  71  ARG A CG  
569  C CD  . ARG A 82  ? 0.5129 0.4268 0.4161 0.0064  -0.0392 0.0278  71  ARG A CD  
570  N NE  . ARG A 82  ? 0.5324 0.4411 0.4342 0.0068  -0.0413 0.0221  71  ARG A NE  
571  C CZ  . ARG A 82  ? 0.5479 0.4574 0.4511 0.0070  -0.0474 0.0145  71  ARG A CZ  
572  N NH1 . ARG A 82  ? 0.5539 0.4575 0.4555 0.0074  -0.0493 0.0090  71  ARG A NH1 
573  N NH2 . ARG A 82  ? 0.5293 0.4456 0.4359 0.0071  -0.0519 0.0120  71  ARG A NH2 
574  N N   . GLU A 83  ? 0.4218 0.3472 0.3056 0.0176  -0.0455 0.0285  72  GLU A N   
575  C CA  . GLU A 83  ? 0.4232 0.3490 0.2980 0.0243  -0.0515 0.0229  72  GLU A CA  
576  C C   . GLU A 83  ? 0.4284 0.3630 0.3105 0.0224  -0.0549 0.0224  72  GLU A C   
577  O O   . GLU A 83  ? 0.4362 0.3754 0.3209 0.0250  -0.0625 0.0155  72  GLU A O   
578  C CB  . GLU A 83  ? 0.4280 0.3447 0.2828 0.0334  -0.0470 0.0255  72  GLU A CB  
579  C CG  . GLU A 83  ? 0.4528 0.3598 0.3006 0.0358  -0.0408 0.0279  72  GLU A CG  
580  C CD  . GLU A 83  ? 0.4802 0.3822 0.3243 0.0387  -0.0462 0.0215  72  GLU A CD  
581  O OE1 . GLU A 83  ? 0.4926 0.3931 0.3283 0.0449  -0.0542 0.0145  72  GLU A OE1 
582  O OE2 . GLU A 83  ? 0.5009 0.4000 0.3498 0.0354  -0.0429 0.0230  72  GLU A OE2 
583  N N   . LEU A 84  ? 0.4277 0.3641 0.3122 0.0188  -0.0495 0.0293  73  LEU A N   
584  C CA  . LEU A 84  ? 0.4327 0.3756 0.3216 0.0177  -0.0510 0.0304  73  LEU A CA  
585  C C   . LEU A 84  ? 0.4375 0.3876 0.3449 0.0118  -0.0549 0.0267  73  LEU A C   
586  O O   . LEU A 84  ? 0.4377 0.3865 0.3553 0.0054  -0.0519 0.0285  73  LEU A O   
587  C CB  . LEU A 84  ? 0.4309 0.3719 0.3173 0.0148  -0.0438 0.0389  73  LEU A CB  
588  C CG  . LEU A 84  ? 0.4563 0.3902 0.3273 0.0200  -0.0379 0.0426  73  LEU A CG  
589  C CD1 . LEU A 84  ? 0.4658 0.3981 0.3398 0.0151  -0.0313 0.0494  73  LEU A CD1 
590  C CD2 . LEU A 84  ? 0.4532 0.3853 0.3092 0.0285  -0.0390 0.0411  73  LEU A CD2 
591  N N   . LYS A 85  ? 0.4363 0.3934 0.3482 0.0144  -0.0609 0.0213  74  LYS A N   
592  C CA  . LYS A 85  ? 0.4331 0.3976 0.3658 0.0088  -0.0632 0.0174  74  LYS A CA  
593  C C   . LYS A 85  ? 0.4098 0.3815 0.3453 0.0111  -0.0649 0.0181  74  LYS A C   
594  O O   . LYS A 85  ? 0.4103 0.3873 0.3421 0.0180  -0.0721 0.0120  74  LYS A O   
595  C CB  . LYS A 85  ? 0.4843 0.4520 0.4273 0.0090  -0.0706 0.0066  74  LYS A CB  
596  C CG  . LYS A 85  ? 0.5741 0.5474 0.5423 0.0013  -0.0699 0.0026  74  LYS A CG  
597  C CD  . LYS A 85  ? 0.6626 0.6413 0.6440 0.0016  -0.0787 -0.0102 74  LYS A CD  
598  C CE  . LYS A 85  ? 0.7247 0.7077 0.7341 -0.0070 -0.0754 -0.0144 74  LYS A CE  
599  N NZ  . LYS A 85  ? 0.7740 0.7606 0.7980 -0.0083 -0.0830 -0.0276 74  LYS A NZ  
600  N N   . HIS A 86  ? 0.3864 0.3574 0.3266 0.0064  -0.0582 0.0255  75  HIS A N   
601  C CA  . HIS A 86  ? 0.3722 0.3487 0.3150 0.0081  -0.0581 0.0277  75  HIS A CA  
602  C C   . HIS A 86  ? 0.3704 0.3444 0.3256 0.0010  -0.0507 0.0336  75  HIS A C   
603  O O   . HIS A 86  ? 0.3686 0.3337 0.3194 -0.0027 -0.0451 0.0392  75  HIS A O   
604  C CB  . HIS A 86  ? 0.3722 0.3443 0.2925 0.0143  -0.0558 0.0338  75  HIS A CB  
605  C CG  . HIS A 86  ? 0.3809 0.3584 0.3004 0.0179  -0.0564 0.0353  75  HIS A CG  
606  N ND1 . HIS A 86  ? 0.4021 0.3772 0.3237 0.0140  -0.0498 0.0433  75  HIS A ND1 
607  C CD2 . HIS A 86  ? 0.3794 0.3643 0.2968 0.0257  -0.0633 0.0294  75  HIS A CD2 
608  C CE1 . HIS A 86  ? 0.3988 0.3802 0.3201 0.0189  -0.0520 0.0425  75  HIS A CE1 
609  N NE2 . HIS A 86  ? 0.3892 0.3773 0.3084 0.0262  -0.0604 0.0340  75  HIS A NE2 
610  N N   . PRO A 87  ? 0.3714 0.3520 0.3415 -0.0001 -0.0504 0.0324  76  PRO A N   
611  C CA  . PRO A 87  ? 0.3696 0.3444 0.3496 -0.0057 -0.0416 0.0386  76  PRO A CA  
612  C C   . PRO A 87  ? 0.3875 0.3517 0.3497 -0.0054 -0.0352 0.0495  76  PRO A C   
613  O O   . PRO A 87  ? 0.3938 0.3485 0.3579 -0.0089 -0.0283 0.0549  76  PRO A O   
614  C CB  . PRO A 87  ? 0.3702 0.3551 0.3682 -0.0051 -0.0426 0.0351  76  PRO A CB  
615  C CG  . PRO A 87  ? 0.3694 0.3671 0.3745 -0.0009 -0.0539 0.0235  76  PRO A CG  
616  C CD  . PRO A 87  ? 0.3622 0.3553 0.3415 0.0046  -0.0579 0.0248  76  PRO A CD  
617  N N   . ASN A 88  ? 0.3907 0.3549 0.3348 -0.0007 -0.0372 0.0525  77  ASN A N   
618  C CA  . ASN A 88  ? 0.3907 0.3454 0.3191 -0.0007 -0.0319 0.0616  77  ASN A CA  
619  C C   . ASN A 88  ? 0.4051 0.3533 0.3212 -0.0010 -0.0317 0.0632  77  ASN A C   
620  O O   . ASN A 88  ? 0.4181 0.3597 0.3219 -0.0007 -0.0286 0.0691  77  ASN A O   
621  C CB  . ASN A 88  ? 0.3798 0.3369 0.2979 0.0040  -0.0316 0.0649  77  ASN A CB  
622  C CG  . ASN A 88  ? 0.3626 0.3252 0.2948 0.0039  -0.0303 0.0648  77  ASN A CG  
623  O OD1 . ASN A 88  ? 0.3800 0.3525 0.3157 0.0084  -0.0347 0.0605  77  ASN A OD1 
624  N ND2 . ASN A 88  ? 0.3309 0.2862 0.2713 -0.0004 -0.0240 0.0692  77  ASN A ND2 
625  N N   . VAL A 89  ? 0.3993 0.3491 0.3202 -0.0020 -0.0346 0.0579  78  VAL A N   
626  C CA  . VAL A 89  ? 0.4032 0.3476 0.3160 -0.0024 -0.0339 0.0591  78  VAL A CA  
627  C C   . VAL A 89  ? 0.4078 0.3482 0.3302 -0.0063 -0.0328 0.0580  78  VAL A C   
628  O O   . VAL A 89  ? 0.4026 0.3466 0.3368 -0.0077 -0.0344 0.0526  78  VAL A O   
629  C CB  . VAL A 89  ? 0.4060 0.3538 0.3118 0.0020  -0.0373 0.0544  78  VAL A CB  
630  C CG1 . VAL A 89  ? 0.4111 0.3537 0.3119 0.0013  -0.0353 0.0556  78  VAL A CG1 
631  C CG2 . VAL A 89  ? 0.4016 0.3509 0.2952 0.0076  -0.0373 0.0555  78  VAL A CG2 
632  N N   . ILE A 90  ? 0.4163 0.3485 0.3338 -0.0076 -0.0301 0.0624  79  ILE A N   
633  C CA  . ILE A 90  ? 0.4222 0.3483 0.3450 -0.0095 -0.0285 0.0618  79  ILE A CA  
634  C C   . ILE A 90  ? 0.4365 0.3668 0.3648 -0.0098 -0.0312 0.0555  79  ILE A C   
635  O O   . ILE A 90  ? 0.4462 0.3806 0.3695 -0.0077 -0.0339 0.0534  79  ILE A O   
636  C CB  . ILE A 90  ? 0.4306 0.3481 0.3451 -0.0087 -0.0274 0.0663  79  ILE A CB  
637  C CG1 . ILE A 90  ? 0.4406 0.3481 0.3569 -0.0087 -0.0247 0.0669  79  ILE A CG1 
638  C CG2 . ILE A 90  ? 0.4363 0.3573 0.3468 -0.0077 -0.0299 0.0650  79  ILE A CG2 
639  C CD1 . ILE A 90  ? 0.4565 0.3562 0.3756 -0.0092 -0.0193 0.0694  79  ILE A CD1 
640  N N   . SER A 91  ? 0.4430 0.3713 0.3812 -0.0120 -0.0297 0.0522  80  SER A N   
641  C CA  . SER A 91  ? 0.4449 0.3762 0.3886 -0.0125 -0.0322 0.0457  80  SER A CA  
642  C C   . SER A 91  ? 0.4524 0.3760 0.3925 -0.0125 -0.0301 0.0466  80  SER A C   
643  O O   . SER A 91  ? 0.4491 0.3639 0.3894 -0.0131 -0.0255 0.0496  80  SER A O   
644  C CB  . SER A 91  ? 0.4582 0.3925 0.4173 -0.0154 -0.0318 0.0400  80  SER A CB  
645  O OG  . SER A 91  ? 0.5180 0.4576 0.4807 -0.0149 -0.0371 0.0323  80  SER A OG  
646  N N   . LEU A 92  ? 0.4591 0.3850 0.3945 -0.0106 -0.0329 0.0443  81  LEU A N   
647  C CA  . LEU A 92  ? 0.4732 0.3933 0.4057 -0.0098 -0.0313 0.0447  81  LEU A CA  
648  C C   . LEU A 92  ? 0.4931 0.4094 0.4324 -0.0119 -0.0297 0.0398  81  LEU A C   
649  O O   . LEU A 92  ? 0.4910 0.4115 0.4339 -0.0123 -0.0329 0.0340  81  LEU A O   
650  C CB  . LEU A 92  ? 0.4653 0.3886 0.3914 -0.0069 -0.0335 0.0445  81  LEU A CB  
651  C CG  . LEU A 92  ? 0.4721 0.3911 0.3963 -0.0055 -0.0320 0.0447  81  LEU A CG  
652  C CD1 . LEU A 92  ? 0.4726 0.3864 0.3957 -0.0047 -0.0303 0.0489  81  LEU A CD1 
653  C CD2 . LEU A 92  ? 0.4699 0.3917 0.3895 -0.0025 -0.0325 0.0446  81  LEU A CD2 
654  N N   . GLN A 93  ? 0.5074 0.4142 0.4473 -0.0125 -0.0245 0.0419  82  GLN A N   
655  C CA  . GLN A 93  ? 0.5208 0.4216 0.4669 -0.0146 -0.0208 0.0375  82  GLN A CA  
656  C C   . GLN A 93  ? 0.5374 0.4349 0.4771 -0.0124 -0.0213 0.0363  82  GLN A C   
657  O O   . GLN A 93  ? 0.5494 0.4475 0.4928 -0.0139 -0.0223 0.0307  82  GLN A O   
658  C CB  . GLN A 93  ? 0.5460 0.4343 0.4929 -0.0150 -0.0126 0.0407  82  GLN A CB  
659  C CG  . GLN A 93  ? 0.6093 0.4964 0.5561 -0.0147 -0.0108 0.0454  82  GLN A CG  
660  C CD  . GLN A 93  ? 0.6791 0.5679 0.6411 -0.0191 -0.0070 0.0418  82  GLN A CD  
661  O OE1 . GLN A 93  ? 0.6986 0.6000 0.6701 -0.0215 -0.0124 0.0372  82  GLN A OE1 
662  N NE2 . GLN A 93  ? 0.7009 0.5762 0.6657 -0.0196 0.0029  0.0435  82  GLN A NE2 
663  N N   . LYS A 94  ? 0.5360 0.4297 0.4667 -0.0085 -0.0207 0.0412  83  LYS A N   
664  C CA  . LYS A 94  ? 0.5424 0.4323 0.4678 -0.0058 -0.0200 0.0407  83  LYS A CA  
665  C C   . LYS A 94  ? 0.5294 0.4226 0.4493 -0.0016 -0.0227 0.0446  83  LYS A C   
666  O O   . LYS A 94  ? 0.5278 0.4220 0.4463 -0.0004 -0.0240 0.0481  83  LYS A O   
667  C CB  . LYS A 94  ? 0.5957 0.4719 0.5180 -0.0046 -0.0133 0.0414  83  LYS A CB  
668  C CG  . LYS A 94  ? 0.6886 0.5596 0.6165 -0.0082 -0.0092 0.0359  83  LYS A CG  
669  C CD  . LYS A 94  ? 0.7796 0.6344 0.7021 -0.0061 -0.0003 0.0372  83  LYS A CD  
670  C CE  . LYS A 94  ? 0.8494 0.6983 0.7784 -0.0103 0.0046  0.0312  83  LYS A CE  
671  N NZ  . LYS A 94  ? 0.8946 0.7250 0.8171 -0.0080 0.0156  0.0327  83  LYS A NZ  
672  N N   . VAL A 95  ? 0.5192 0.4135 0.4369 0.0007  -0.0232 0.0437  84  VAL A N   
673  C CA  . VAL A 95  ? 0.5217 0.4196 0.4382 0.0046  -0.0249 0.0463  84  VAL A CA  
674  C C   . VAL A 95  ? 0.5363 0.4268 0.4485 0.0085  -0.0223 0.0465  84  VAL A C   
675  O O   . VAL A 95  ? 0.5445 0.4303 0.4545 0.0080  -0.0196 0.0441  84  VAL A O   
676  C CB  . VAL A 95  ? 0.5203 0.4256 0.4385 0.0047  -0.0260 0.0455  84  VAL A CB  
677  C CG1 . VAL A 95  ? 0.5153 0.4249 0.4367 0.0081  -0.0262 0.0477  84  VAL A CG1 
678  C CG2 . VAL A 95  ? 0.5225 0.4332 0.4417 0.0021  -0.0279 0.0450  84  VAL A CG2 
679  N N   . PHE A 96  ? 0.5362 0.4251 0.4466 0.0131  -0.0237 0.0488  85  PHE A N   
680  C CA  . PHE A 96  ? 0.5562 0.4384 0.4613 0.0188  -0.0221 0.0491  85  PHE A CA  
681  C C   . PHE A 96  ? 0.5717 0.4635 0.4832 0.0224  -0.0258 0.0495  85  PHE A C   
682  O O   . PHE A 96  ? 0.5682 0.4668 0.4852 0.0227  -0.0301 0.0500  85  PHE A O   
683  C CB  . PHE A 96  ? 0.5638 0.4348 0.4603 0.0236  -0.0213 0.0507  85  PHE A CB  
684  C CG  . PHE A 96  ? 0.5792 0.4394 0.4716 0.0203  -0.0156 0.0507  85  PHE A CG  
685  C CD1 . PHE A 96  ? 0.5990 0.4479 0.4867 0.0200  -0.0086 0.0493  85  PHE A CD1 
686  C CD2 . PHE A 96  ? 0.5927 0.4529 0.4864 0.0177  -0.0164 0.0521  85  PHE A CD2 
687  C CE1 . PHE A 96  ? 0.6152 0.4538 0.5026 0.0167  -0.0020 0.0488  85  PHE A CE1 
688  C CE2 . PHE A 96  ? 0.6098 0.4599 0.5024 0.0149  -0.0099 0.0521  85  PHE A CE2 
689  C CZ  . PHE A 96  ? 0.6117 0.4512 0.5022 0.0142  -0.0025 0.0503  85  PHE A CZ  
690  N N   . LEU A 97  ? 0.5832 0.4754 0.4952 0.0249  -0.0236 0.0490  86  LEU A N   
691  C CA  . LEU A 97  ? 0.5890 0.4906 0.5103 0.0283  -0.0257 0.0491  86  LEU A CA  
692  C C   . LEU A 97  ? 0.5999 0.4973 0.5174 0.0359  -0.0266 0.0491  86  LEU A C   
693  O O   . LEU A 97  ? 0.6112 0.5010 0.5212 0.0383  -0.0223 0.0493  86  LEU A O   
694  C CB  . LEU A 97  ? 0.5920 0.4967 0.5167 0.0265  -0.0215 0.0490  86  LEU A CB  
695  C CG  . LEU A 97  ? 0.6100 0.5174 0.5356 0.0211  -0.0204 0.0487  86  LEU A CG  
696  C CD1 . LEU A 97  ? 0.6209 0.5294 0.5483 0.0224  -0.0161 0.0491  86  LEU A CD1 
697  C CD2 . LEU A 97  ? 0.6068 0.5220 0.5399 0.0187  -0.0237 0.0491  86  LEU A CD2 
698  N N   . SER A 98  ? 0.5940 0.4951 0.5151 0.0406  -0.0327 0.0483  87  SER A N   
699  C CA  . SER A 98  ? 0.6011 0.4981 0.5172 0.0500  -0.0356 0.0475  87  SER A CA  
700  C C   . SER A 98  ? 0.5964 0.5051 0.5270 0.0530  -0.0365 0.0463  87  SER A C   
701  O O   . SER A 98  ? 0.5800 0.5017 0.5273 0.0525  -0.0413 0.0442  87  SER A O   
702  C CB  . SER A 98  ? 0.6196 0.5153 0.5331 0.0547  -0.0432 0.0463  87  SER A CB  
703  O OG  . SER A 98  ? 0.6605 0.5505 0.5662 0.0659  -0.0468 0.0450  87  SER A OG  
704  N N   . HIS A 99  ? 0.6093 0.5132 0.5347 0.0560  -0.0311 0.0474  88  HIS A N   
705  C CA  . HIS A 99  ? 0.6143 0.5281 0.5536 0.0585  -0.0298 0.0470  88  HIS A CA  
706  C C   . HIS A 99  ? 0.6263 0.5496 0.5773 0.0671  -0.0374 0.0439  88  HIS A C   
707  O O   . HIS A 99  ? 0.6269 0.5644 0.5995 0.0662  -0.0385 0.0421  88  HIS A O   
708  C CB  . HIS A 99  ? 0.6253 0.5296 0.5539 0.0599  -0.0218 0.0493  88  HIS A CB  
709  C CG  . HIS A 99  ? 0.6405 0.5404 0.5649 0.0519  -0.0156 0.0507  88  HIS A CG  
710  N ND1 . HIS A 99  ? 0.6575 0.5584 0.5856 0.0514  -0.0098 0.0521  88  HIS A ND1 
711  C CD2 . HIS A 99  ? 0.6515 0.5454 0.5679 0.0454  -0.0150 0.0505  88  HIS A CD2 
712  C CE1 . HIS A 99  ? 0.6637 0.5584 0.5840 0.0453  -0.0068 0.0523  88  HIS A CE1 
713  N NE2 . HIS A 99  ? 0.6631 0.5548 0.5777 0.0414  -0.0102 0.0510  88  HIS A NE2 
714  N N   . ALA A 100 ? 0.6310 0.5462 0.5687 0.0760  -0.0426 0.0427  89  ALA A N   
715  C CA  . ALA A 100 ? 0.6342 0.5585 0.5822 0.0859  -0.0519 0.0385  89  ALA A CA  
716  C C   . ALA A 100 ? 0.6288 0.5686 0.5984 0.0831  -0.0609 0.0339  89  ALA A C   
717  O O   . ALA A 100 ? 0.6287 0.5843 0.6221 0.0851  -0.0648 0.0301  89  ALA A O   
718  C CB  . ALA A 100 ? 0.6499 0.5592 0.5747 0.0976  -0.0558 0.0380  89  ALA A CB  
719  N N   . ASP A 101 ? 0.6173 0.5528 0.5806 0.0782  -0.0636 0.0341  90  ASP A N   
720  C CA  . ASP A 101 ? 0.5990 0.5473 0.5810 0.0751  -0.0717 0.0297  90  ASP A CA  
721  C C   . ASP A 101 ? 0.5886 0.5449 0.5851 0.0626  -0.0652 0.0314  90  ASP A C   
722  O O   . ASP A 101 ? 0.5882 0.5537 0.5997 0.0589  -0.0702 0.0280  90  ASP A O   
723  C CB  . ASP A 101 ? 0.6176 0.5557 0.5832 0.0799  -0.0802 0.0283  90  ASP A CB  
724  C CG  . ASP A 101 ? 0.6672 0.5876 0.6085 0.0761  -0.0732 0.0338  90  ASP A CG  
725  O OD1 . ASP A 101 ? 0.6580 0.5757 0.5968 0.0688  -0.0631 0.0379  90  ASP A OD1 
726  O OD2 . ASP A 101 ? 0.7148 0.6238 0.6404 0.0808  -0.0779 0.0337  90  ASP A OD2 
727  N N   . ARG A 102 ? 0.5795 0.5307 0.5698 0.0568  -0.0543 0.0362  91  ARG A N   
728  C CA  . ARG A 102 ? 0.5710 0.5260 0.5691 0.0470  -0.0472 0.0382  91  ARG A CA  
729  C C   . ARG A 102 ? 0.5591 0.5113 0.5513 0.0416  -0.0501 0.0385  91  ARG A C   
730  O O   . ARG A 102 ? 0.5475 0.5074 0.5530 0.0360  -0.0491 0.0375  91  ARG A O   
731  C CB  . ARG A 102 ? 0.5791 0.5483 0.6042 0.0452  -0.0441 0.0359  91  ARG A CB  
732  C CG  . ARG A 102 ? 0.6205 0.5903 0.6498 0.0492  -0.0376 0.0374  91  ARG A CG  
733  C CD  . ARG A 102 ? 0.6391 0.6167 0.6893 0.0451  -0.0283 0.0379  91  ARG A CD  
734  N NE  . ARG A 102 ? 0.6714 0.6388 0.7077 0.0400  -0.0183 0.0426  91  ARG A NE  
735  C CZ  . ARG A 102 ? 0.6975 0.6661 0.7408 0.0343  -0.0123 0.0433  91  ARG A CZ  
736  N NH1 . ARG A 102 ? 0.6816 0.6395 0.7090 0.0319  -0.0045 0.0471  91  ARG A NH1 
737  N NH2 . ARG A 102 ? 0.6922 0.6720 0.7582 0.0317  -0.0140 0.0396  91  ARG A NH2 
738  N N   . LYS A 103 ? 0.5574 0.4975 0.5293 0.0438  -0.0527 0.0400  92  LYS A N   
739  C CA  . LYS A 103 ? 0.5501 0.4862 0.5151 0.0395  -0.0549 0.0409  92  LYS A CA  
740  C C   . LYS A 103 ? 0.5347 0.4628 0.4874 0.0335  -0.0474 0.0448  92  LYS A C   
741  O O   . LYS A 103 ? 0.5417 0.4620 0.4845 0.0348  -0.0428 0.0463  92  LYS A O   
742  C CB  . LYS A 103 ? 0.5806 0.5080 0.5330 0.0469  -0.0629 0.0396  92  LYS A CB  
743  C CG  . LYS A 103 ? 0.6449 0.5819 0.6112 0.0525  -0.0733 0.0340  92  LYS A CG  
744  C CD  . LYS A 103 ? 0.7209 0.6674 0.7019 0.0455  -0.0758 0.0320  92  LYS A CD  
745  C CE  . LYS A 103 ? 0.7747 0.7320 0.7736 0.0496  -0.0867 0.0249  92  LYS A CE  
746  N NZ  . LYS A 103 ? 0.8034 0.7685 0.8168 0.0416  -0.0871 0.0230  92  LYS A NZ  
747  N N   . VAL A 104 ? 0.5176 0.4476 0.4717 0.0271  -0.0463 0.0458  93  VAL A N   
748  C CA  . VAL A 104 ? 0.5120 0.4362 0.4565 0.0220  -0.0407 0.0484  93  VAL A CA  
749  C C   . VAL A 104 ? 0.5040 0.4202 0.4377 0.0213  -0.0427 0.0498  93  VAL A C   
750  O O   . VAL A 104 ? 0.5010 0.4194 0.4369 0.0209  -0.0469 0.0496  93  VAL A O   
751  C CB  . VAL A 104 ? 0.5199 0.4509 0.4718 0.0165  -0.0363 0.0488  93  VAL A CB  
752  C CG1 . VAL A 104 ? 0.5340 0.4593 0.4755 0.0128  -0.0326 0.0502  93  VAL A CG1 
753  C CG2 . VAL A 104 ? 0.5192 0.4557 0.4814 0.0180  -0.0324 0.0480  93  VAL A CG2 
754  N N   . TRP A 105 ? 0.4987 0.4047 0.4213 0.0211  -0.0390 0.0511  94  TRP A N   
755  C CA  . TRP A 105 ? 0.4962 0.3930 0.4095 0.0205  -0.0386 0.0529  94  TRP A CA  
756  C C   . TRP A 105 ? 0.4898 0.3874 0.4037 0.0138  -0.0342 0.0535  94  TRP A C   
757  O O   . TRP A 105 ? 0.4916 0.3901 0.4070 0.0117  -0.0310 0.0521  94  TRP A O   
758  C CB  . TRP A 105 ? 0.4973 0.3795 0.3982 0.0266  -0.0365 0.0536  94  TRP A CB  
759  C CG  . TRP A 105 ? 0.4995 0.3795 0.3970 0.0353  -0.0422 0.0525  94  TRP A CG  
760  C CD1 . TRP A 105 ? 0.5041 0.3903 0.4073 0.0396  -0.0449 0.0503  94  TRP A CD1 
761  C CD2 . TRP A 105 ? 0.5087 0.3788 0.3953 0.0422  -0.0467 0.0531  94  TRP A CD2 
762  N NE1 . TRP A 105 ? 0.5151 0.3975 0.4132 0.0487  -0.0518 0.0488  94  TRP A NE1 
763  C CE2 . TRP A 105 ? 0.5164 0.3881 0.4030 0.0509  -0.0533 0.0503  94  TRP A CE2 
764  C CE3 . TRP A 105 ? 0.5199 0.3793 0.3965 0.0426  -0.0459 0.0556  94  TRP A CE3 
765  C CZ2 . TRP A 105 ? 0.5275 0.3895 0.4024 0.0607  -0.0602 0.0493  94  TRP A CZ2 
766  C CZ3 . TRP A 105 ? 0.5352 0.3839 0.3993 0.0520  -0.0516 0.0554  94  TRP A CZ3 
767  C CH2 . TRP A 105 ? 0.5351 0.3849 0.3977 0.0612  -0.0593 0.0519  94  TRP A CH2 
768  N N   . LEU A 106 ? 0.4730 0.3700 0.3854 0.0112  -0.0347 0.0551  95  LEU A N   
769  C CA  . LEU A 106 ? 0.4598 0.3585 0.3739 0.0058  -0.0317 0.0551  95  LEU A CA  
770  C C   . LEU A 106 ? 0.4674 0.3553 0.3758 0.0058  -0.0285 0.0569  95  LEU A C   
771  O O   . LEU A 106 ? 0.4793 0.3599 0.3810 0.0094  -0.0296 0.0595  95  LEU A O   
772  C CB  . LEU A 106 ? 0.4515 0.3595 0.3696 0.0029  -0.0337 0.0556  95  LEU A CB  
773  C CG  . LEU A 106 ? 0.4473 0.3639 0.3714 0.0032  -0.0347 0.0545  95  LEU A CG  
774  C CD1 . LEU A 106 ? 0.4375 0.3596 0.3628 0.0005  -0.0341 0.0553  95  LEU A CD1 
775  C CD2 . LEU A 106 ? 0.4531 0.3708 0.3785 0.0035  -0.0322 0.0523  95  LEU A CD2 
776  N N   . LEU A 107 ? 0.4534 0.3393 0.3650 0.0023  -0.0243 0.0553  96  LEU A N   
777  C CA  . LEU A 107 ? 0.4524 0.3276 0.3621 0.0018  -0.0188 0.0567  96  LEU A CA  
778  C C   . LEU A 107 ? 0.4492 0.3317 0.3663 -0.0031 -0.0188 0.0562  96  LEU A C   
779  O O   . LEU A 107 ? 0.4496 0.3428 0.3732 -0.0063 -0.0216 0.0529  96  LEU A O   
780  C CB  . LEU A 107 ? 0.4482 0.3145 0.3588 0.0015  -0.0127 0.0542  96  LEU A CB  
781  C CG  . LEU A 107 ? 0.4566 0.3098 0.3679 0.0006  -0.0039 0.0551  96  LEU A CG  
782  C CD1 . LEU A 107 ? 0.4676 0.3041 0.3642 0.0079  -0.0004 0.0599  96  LEU A CD1 
783  C CD2 . LEU A 107 ? 0.4525 0.3006 0.3697 -0.0022 0.0022  0.0507  96  LEU A CD2 
784  N N   . PHE A 108 ? 0.4386 0.3142 0.3529 -0.0026 -0.0159 0.0598  97  PHE A N   
785  C CA  . PHE A 108 ? 0.4275 0.3085 0.3484 -0.0062 -0.0150 0.0602  97  PHE A CA  
786  C C   . PHE A 108 ? 0.4490 0.3160 0.3695 -0.0056 -0.0066 0.0629  97  PHE A C   
787  O O   . PHE A 108 ? 0.4466 0.2984 0.3572 -0.0010 -0.0023 0.0655  97  PHE A O   
788  C CB  . PHE A 108 ? 0.4091 0.2948 0.3239 -0.0050 -0.0196 0.0638  97  PHE A CB  
789  C CG  . PHE A 108 ? 0.4041 0.2996 0.3176 -0.0045 -0.0256 0.0625  97  PHE A CG  
790  C CD1 . PHE A 108 ? 0.3996 0.3066 0.3180 -0.0068 -0.0279 0.0598  97  PHE A CD1 
791  C CD2 . PHE A 108 ? 0.4079 0.3001 0.3157 -0.0008 -0.0284 0.0635  97  PHE A CD2 
792  C CE1 . PHE A 108 ? 0.3996 0.3129 0.3167 -0.0059 -0.0309 0.0591  97  PHE A CE1 
793  C CE2 . PHE A 108 ? 0.4053 0.3065 0.3156 -0.0009 -0.0322 0.0619  97  PHE A CE2 
794  C CZ  . PHE A 108 ? 0.3962 0.3071 0.3109 -0.0036 -0.0324 0.0602  97  PHE A CZ  
795  N N   . ASP A 109 ? 0.4564 0.3273 0.3860 -0.0089 -0.0041 0.0630  98  ASP A N   
796  C CA  . ASP A 109 ? 0.4680 0.3254 0.3974 -0.0079 0.0050  0.0668  98  ASP A CA  
797  C C   . ASP A 109 ? 0.4710 0.3192 0.3828 -0.0024 0.0034  0.0736  98  ASP A C   
798  O O   . ASP A 109 ? 0.4704 0.3279 0.3773 -0.0020 -0.0046 0.0741  98  ASP A O   
799  C CB  . ASP A 109 ? 0.4948 0.3623 0.4410 -0.0128 0.0067  0.0646  98  ASP A CB  
800  C CG  . ASP A 109 ? 0.5762 0.4486 0.5419 -0.0178 0.0100  0.0573  98  ASP A CG  
801  O OD1 . ASP A 109 ? 0.5946 0.4562 0.5594 -0.0175 0.0156  0.0558  98  ASP A OD1 
802  O OD2 . ASP A 109 ? 0.6115 0.4978 0.5929 -0.0216 0.0067  0.0525  98  ASP A OD2 
803  N N   . TYR A 110 ? 0.4798 0.3083 0.3818 0.0022  0.0115  0.0784  99  TYR A N   
804  C CA  . TYR A 110 ? 0.4973 0.3142 0.3806 0.0085  0.0095  0.0842  99  TYR A CA  
805  C C   . TYR A 110 ? 0.5000 0.3179 0.3855 0.0068  0.0122  0.0881  99  TYR A C   
806  O O   . TYR A 110 ? 0.5191 0.3293 0.4117 0.0058  0.0223  0.0899  99  TYR A O   
807  C CB  . TYR A 110 ? 0.5176 0.3088 0.3844 0.0167  0.0172  0.0877  99  TYR A CB  
808  C CG  . TYR A 110 ? 0.5438 0.3205 0.3884 0.0251  0.0135  0.0926  99  TYR A CG  
809  C CD1 . TYR A 110 ? 0.5552 0.3385 0.3918 0.0280  0.0012  0.0907  99  TYR A CD1 
810  C CD2 . TYR A 110 ? 0.5722 0.3275 0.4041 0.0305  0.0224  0.0988  99  TYR A CD2 
811  C CE1 . TYR A 110 ? 0.5792 0.3492 0.3964 0.0359  -0.0037 0.0936  99  TYR A CE1 
812  C CE2 . TYR A 110 ? 0.5977 0.3375 0.4066 0.0393  0.0181  0.1028  99  TYR A CE2 
813  C CZ  . TYR A 110 ? 0.6129 0.3606 0.4147 0.0419  0.0042  0.0996  99  TYR A CZ  
814  O OH  . TYR A 110 ? 0.6667 0.3995 0.4470 0.0506  -0.0016 0.1021  99  TYR A OH  
815  N N   . ALA A 111 ? 0.4821 0.3075 0.3611 0.0070  0.0045  0.0898  100 ALA A N   
816  C CA  . ALA A 111 ? 0.4793 0.3043 0.3566 0.0065  0.0067  0.0943  100 ALA A CA  
817  C C   . ALA A 111 ? 0.5002 0.3034 0.3550 0.0143  0.0079  0.1002  100 ALA A C   
818  O O   . ALA A 111 ? 0.5071 0.3094 0.3504 0.0175  -0.0005 0.0994  100 ALA A O   
819  C CB  . ALA A 111 ? 0.4681 0.3119 0.3491 0.0028  -0.0018 0.0924  100 ALA A CB  
820  N N   . GLU A 112 ? 0.4282 0.3972 0.3410 -0.0159 0.0056  0.0428  101 GLU A N   
821  C CA  . GLU A 112 ? 0.4442 0.4143 0.3470 -0.0148 0.0046  0.0471  101 GLU A CA  
822  C C   . GLU A 112 ? 0.4518 0.4223 0.3437 -0.0138 0.0028  0.0427  101 GLU A C   
823  O O   . GLU A 112 ? 0.4464 0.4164 0.3302 -0.0131 -0.0003 0.0445  101 GLU A O   
824  C CB  . GLU A 112 ? 0.4910 0.4627 0.3913 -0.0149 0.0089  0.0516  101 GLU A CB  
825  C CG  . GLU A 112 ? 0.5933 0.5652 0.4827 -0.0139 0.0085  0.0571  101 GLU A CG  
826  C CD  . GLU A 112 ? 0.7165 0.6870 0.6106 -0.0142 0.0053  0.0631  101 GLU A CD  
827  O OE1 . GLU A 112 ? 0.7259 0.6963 0.6308 -0.0150 0.0072  0.0672  101 GLU A OE1 
828  O OE2 . GLU A 112 ? 0.7638 0.7333 0.6522 -0.0137 0.0006  0.0637  101 GLU A OE2 
829  N N   . HIS A 113 ? 0.4552 0.4264 0.3472 -0.0140 0.0041  0.0370  102 HIS A N   
830  C CA  . HIS A 113 ? 0.4633 0.4347 0.3462 -0.0131 0.0027  0.0329  102 HIS A CA  
831  C C   . HIS A 113 ? 0.4647 0.4354 0.3511 -0.0133 0.0002  0.0278  102 HIS A C   
832  O O   . HIS A 113 ? 0.4717 0.4417 0.3666 -0.0142 0.0005  0.0263  102 HIS A O   
833  C CB  . HIS A 113 ? 0.4756 0.4487 0.3547 -0.0127 0.0070  0.0315  102 HIS A CB  
834  C CG  . HIS A 113 ? 0.5066 0.4806 0.3826 -0.0123 0.0106  0.0369  102 HIS A CG  
835  N ND1 . HIS A 113 ? 0.5403 0.5131 0.4054 -0.0114 0.0098  0.0403  102 HIS A ND1 
836  C CD2 . HIS A 113 ? 0.5243 0.5000 0.4074 -0.0130 0.0147  0.0400  102 HIS A CD2 
837  C CE1 . HIS A 113 ? 0.5515 0.5254 0.4165 -0.0113 0.0141  0.0454  102 HIS A CE1 
838  N NE2 . HIS A 113 ? 0.5481 0.5239 0.4247 -0.0122 0.0173  0.0456  102 HIS A NE2 
839  N N   . ASP A 114 ? 0.4607 0.4312 0.3400 -0.0126 -0.0021 0.0249  103 ASP A N   
840  C CA  . ASP A 114 ? 0.4589 0.4291 0.3407 -0.0127 -0.0039 0.0202  103 ASP A CA  
841  C C   . ASP A 114 ? 0.4640 0.4343 0.3369 -0.0118 -0.0045 0.0171  103 ASP A C   
842  O O   . ASP A 114 ? 0.4751 0.4449 0.3391 -0.0111 -0.0042 0.0186  103 ASP A O   
843  C CB  . ASP A 114 ? 0.4632 0.4324 0.3503 -0.0128 -0.0075 0.0209  103 ASP A CB  
844  C CG  . ASP A 114 ? 0.4979 0.4664 0.3798 -0.0123 -0.0117 0.0241  103 ASP A CG  
845  O OD1 . ASP A 114 ? 0.4953 0.4633 0.3687 -0.0119 -0.0139 0.0222  103 ASP A OD1 
846  O OD2 . ASP A 114 ? 0.5307 0.4988 0.4171 -0.0125 -0.0130 0.0285  103 ASP A OD2 
847  N N   . LEU A 115 ? 0.4481 0.4186 0.3231 -0.0119 -0.0051 0.0129  104 LEU A N   
848  C CA  . LEU A 115 ? 0.4422 0.4124 0.3104 -0.0111 -0.0055 0.0096  104 LEU A CA  
849  C C   . LEU A 115 ? 0.4493 0.4174 0.3102 -0.0106 -0.0098 0.0094  104 LEU A C   
850  O O   . LEU A 115 ? 0.4453 0.4120 0.2976 -0.0097 -0.0095 0.0074  104 LEU A O   
851  C CB  . LEU A 115 ? 0.4351 0.4062 0.3082 -0.0114 -0.0052 0.0059  104 LEU A CB  
852  C CG  . LEU A 115 ? 0.4457 0.4184 0.3199 -0.0113 -0.0015 0.0046  104 LEU A CG  
853  C CD1 . LEU A 115 ? 0.4460 0.4200 0.3236 -0.0119 0.0016  0.0076  104 LEU A CD1 
854  C CD2 . LEU A 115 ? 0.4470 0.4203 0.3267 -0.0121 -0.0021 0.0019  104 LEU A CD2 
855  N N   . TRP A 116 ? 0.4582 0.4257 0.3226 -0.0111 -0.0137 0.0115  105 TRP A N   
856  C CA  . TRP A 116 ? 0.4755 0.4409 0.3336 -0.0111 -0.0191 0.0118  105 TRP A CA  
857  C C   . TRP A 116 ? 0.4794 0.4431 0.3255 -0.0106 -0.0189 0.0142  105 TRP A C   
858  O O   . TRP A 116 ? 0.4883 0.4494 0.3238 -0.0102 -0.0209 0.0119  105 TRP A O   
859  C CB  . TRP A 116 ? 0.4824 0.4481 0.3491 -0.0118 -0.0234 0.0148  105 TRP A CB  
860  C CG  . TRP A 116 ? 0.5100 0.4738 0.3726 -0.0122 -0.0302 0.0151  105 TRP A CG  
861  C CD1 . TRP A 116 ? 0.5235 0.4868 0.3897 -0.0126 -0.0339 0.0125  105 TRP A CD1 
862  C CD2 . TRP A 116 ? 0.5227 0.4846 0.3770 -0.0125 -0.0346 0.0186  105 TRP A CD2 
863  N NE1 . TRP A 116 ? 0.5316 0.4927 0.3929 -0.0132 -0.0409 0.0138  105 TRP A NE1 
864  C CE2 . TRP A 116 ? 0.5328 0.4928 0.3858 -0.0133 -0.0416 0.0175  105 TRP A CE2 
865  C CE3 . TRP A 116 ? 0.5409 0.5023 0.3885 -0.0124 -0.0336 0.0229  105 TRP A CE3 
866  C CZ2 . TRP A 116 ? 0.5520 0.5095 0.3967 -0.0141 -0.0483 0.0202  105 TRP A CZ2 
867  C CZ3 . TRP A 116 ? 0.5634 0.5222 0.4015 -0.0130 -0.0396 0.0258  105 TRP A CZ3 
868  C CH2 . TRP A 116 ? 0.5621 0.5189 0.3986 -0.0139 -0.0472 0.0244  105 TRP A CH2 
869  N N   . HIS A 117 ? 0.4769 0.4417 0.3242 -0.0107 -0.0160 0.0185  106 HIS A N   
870  C CA  . HIS A 117 ? 0.4841 0.4475 0.3200 -0.0102 -0.0150 0.0218  106 HIS A CA  
871  C C   . HIS A 117 ? 0.4930 0.4561 0.3209 -0.0090 -0.0093 0.0192  106 HIS A C   
872  O O   . HIS A 117 ? 0.5030 0.4633 0.3172 -0.0083 -0.0091 0.0191  106 HIS A O   
873  C CB  . HIS A 117 ? 0.4784 0.4432 0.3198 -0.0107 -0.0134 0.0279  106 HIS A CB  
874  C CG  . HIS A 117 ? 0.5107 0.4753 0.3583 -0.0115 -0.0190 0.0316  106 HIS A CG  
875  N ND1 . HIS A 117 ? 0.5262 0.4922 0.3881 -0.0119 -0.0195 0.0312  106 HIS A ND1 
876  C CD2 . HIS A 117 ? 0.5261 0.4890 0.3675 -0.0118 -0.0243 0.0357  106 HIS A CD2 
877  C CE1 . HIS A 117 ? 0.5339 0.4994 0.3995 -0.0123 -0.0246 0.0352  106 HIS A CE1 
878  N NE2 . HIS A 117 ? 0.5352 0.4990 0.3891 -0.0125 -0.0282 0.0382  106 HIS A NE2 
879  N N   . ILE A 118 ? 0.4834 0.4491 0.3196 -0.0088 -0.0044 0.0175  107 ILE A N   
880  C CA  . ILE A 118 ? 0.4841 0.4503 0.3162 -0.0076 0.0014  0.0155  107 ILE A CA  
881  C C   . ILE A 118 ? 0.4954 0.4586 0.3189 -0.0066 -0.0001 0.0101  107 ILE A C   
882  O O   . ILE A 118 ? 0.4998 0.4605 0.3117 -0.0053 0.0028  0.0091  107 ILE A O   
883  C CB  . ILE A 118 ? 0.4790 0.4486 0.3241 -0.0081 0.0050  0.0148  107 ILE A CB  
884  C CG1 . ILE A 118 ? 0.4836 0.4552 0.3357 -0.0090 0.0074  0.0200  107 ILE A CG1 
885  C CG2 . ILE A 118 ? 0.4739 0.4443 0.3182 -0.0069 0.0095  0.0116  107 ILE A CG2 
886  C CD1 . ILE A 118 ? 0.4834 0.4576 0.3485 -0.0101 0.0092  0.0193  107 ILE A CD1 
887  N N   . ILE A 119 ? 0.5024 0.4653 0.3311 -0.0073 -0.0045 0.0068  108 ILE A N   
888  C CA  . ILE A 119 ? 0.5191 0.4790 0.3416 -0.0066 -0.0066 0.0017  108 ILE A CA  
889  C C   . ILE A 119 ? 0.5471 0.5023 0.3552 -0.0065 -0.0107 0.0016  108 ILE A C   
890  O O   . ILE A 119 ? 0.5564 0.5078 0.3534 -0.0053 -0.0093 -0.0019 108 ILE A O   
891  C CB  . ILE A 119 ? 0.5096 0.4705 0.3420 -0.0075 -0.0104 -0.0010 108 ILE A CB  
892  C CG1 . ILE A 119 ? 0.5031 0.4674 0.3459 -0.0074 -0.0062 -0.0019 108 ILE A CG1 
893  C CG2 . ILE A 119 ? 0.5163 0.4733 0.3426 -0.0072 -0.0143 -0.0056 108 ILE A CG2 
894  C CD1 . ILE A 119 ? 0.5005 0.4662 0.3535 -0.0086 -0.0093 -0.0030 108 ILE A CD1 
895  N N   . LYS A 120 ? 0.5566 0.5117 0.3649 -0.0078 -0.0159 0.0055  109 LYS A N   
896  C CA  . LYS A 120 ? 0.5862 0.5368 0.3807 -0.0082 -0.0210 0.0063  109 LYS A CA  
897  C C   . LYS A 120 ? 0.5962 0.5443 0.3755 -0.0069 -0.0160 0.0074  109 LYS A C   
898  O O   . LYS A 120 ? 0.6048 0.5476 0.3687 -0.0066 -0.0181 0.0048  109 LYS A O   
899  C CB  . LYS A 120 ? 0.6337 0.5856 0.4337 -0.0097 -0.0271 0.0117  109 LYS A CB  
900  C CG  . LYS A 120 ? 0.7293 0.6781 0.5269 -0.0110 -0.0362 0.0104  109 LYS A CG  
901  C CD  . LYS A 120 ? 0.8333 0.7805 0.6246 -0.0122 -0.0422 0.0160  109 LYS A CD  
902  C CE  . LYS A 120 ? 0.9104 0.8530 0.6941 -0.0135 -0.0517 0.0141  109 LYS A CE  
903  N NZ  . LYS A 120 ? 0.9526 0.8947 0.7352 -0.0151 -0.0592 0.0205  109 LYS A NZ  
904  N N   . PHE A 121 ? 0.5962 0.5478 0.3798 -0.0062 -0.0090 0.0110  110 PHE A N   
905  C CA  . PHE A 121 ? 0.6194 0.5693 0.3905 -0.0048 -0.0026 0.0127  110 PHE A CA  
906  C C   . PHE A 121 ? 0.6405 0.5874 0.4035 -0.0028 0.0024  0.0067  110 PHE A C   
907  O O   . PHE A 121 ? 0.6539 0.5957 0.3995 -0.0017 0.0041  0.0054  110 PHE A O   
908  C CB  . PHE A 121 ? 0.6149 0.5697 0.3959 -0.0046 0.0035  0.0182  110 PHE A CB  
909  C CG  . PHE A 121 ? 0.6292 0.5828 0.3987 -0.0034 0.0101  0.0220  110 PHE A CG  
910  C CD1 . PHE A 121 ? 0.6465 0.5980 0.4054 -0.0040 0.0075  0.0274  110 PHE A CD1 
911  C CD2 . PHE A 121 ? 0.6401 0.5950 0.4104 -0.0016 0.0190  0.0208  110 PHE A CD2 
912  C CE1 . PHE A 121 ? 0.6580 0.6086 0.4061 -0.0029 0.0141  0.0316  110 PHE A CE1 
913  C CE2 . PHE A 121 ? 0.6551 0.6094 0.4160 -0.0003 0.0260  0.0249  110 PHE A CE2 
914  C CZ  . PHE A 121 ? 0.6561 0.6081 0.4052 -0.0009 0.0238  0.0302  110 PHE A CZ  
915  N N   . HIS A 122 ? 0.6395 0.5890 0.4146 -0.0023 0.0047  0.0029  111 HIS A N   
916  C CA  . HIS A 122 ? 0.6626 0.6094 0.4329 -0.0003 0.0093  -0.0027 111 HIS A CA  
917  C C   . HIS A 122 ? 0.6942 0.6344 0.4528 -0.0004 0.0034  -0.0084 111 HIS A C   
918  O O   . HIS A 122 ? 0.6931 0.6280 0.4382 0.0013  0.0069  -0.0124 111 HIS A O   
919  C CB  . HIS A 122 ? 0.6613 0.6128 0.4488 0.0000  0.0124  -0.0044 111 HIS A CB  
920  C CG  . HIS A 122 ? 0.6899 0.6468 0.4873 0.0002  0.0186  0.0005  111 HIS A CG  
921  N ND1 . HIS A 122 ? 0.7209 0.6779 0.5141 0.0022  0.0270  0.0018  111 HIS A ND1 
922  C CD2 . HIS A 122 ? 0.6944 0.6562 0.5056 -0.0015 0.0174  0.0042  111 HIS A CD2 
923  C CE1 . HIS A 122 ? 0.7209 0.6833 0.5267 0.0014  0.0301  0.0066  111 HIS A CE1 
924  N NE2 . HIS A 122 ? 0.7091 0.6741 0.5252 -0.0008 0.0243  0.0079  111 HIS A NE2 
925  N N   . ARG A 123 ? 0.7159 0.6561 0.4797 -0.0025 -0.0054 -0.0088 112 ARG A N   
926  C CA  . ARG A 123 ? 0.7508 0.6849 0.5059 -0.0032 -0.0125 -0.0137 112 ARG A CA  
927  C C   . ARG A 123 ? 0.7929 0.7207 0.5267 -0.0032 -0.0147 -0.0134 112 ARG A C   
928  O O   . ARG A 123 ? 0.8044 0.7252 0.5242 -0.0023 -0.0148 -0.0190 112 ARG A O   
929  C CB  . ARG A 123 ? 0.7635 0.7000 0.5309 -0.0055 -0.0210 -0.0123 112 ARG A CB  
930  C CG  . ARG A 123 ? 0.8175 0.7493 0.5828 -0.0063 -0.0282 -0.0175 112 ARG A CG  
931  C CD  . ARG A 123 ? 0.8688 0.8044 0.6500 -0.0083 -0.0346 -0.0153 112 ARG A CD  
932  N NE  . ARG A 123 ? 0.9281 0.8594 0.7091 -0.0095 -0.0422 -0.0193 112 ARG A NE  
933  C CZ  . ARG A 123 ? 0.9666 0.9004 0.7612 -0.0112 -0.0481 -0.0178 112 ARG A CZ  
934  N NH1 . ARG A 123 ? 0.9640 0.8938 0.7589 -0.0124 -0.0550 -0.0212 112 ARG A NH1 
935  N NH2 . ARG A 123 ? 0.9618 0.9019 0.7701 -0.0117 -0.0469 -0.0128 112 ARG A NH2 
936  N N   . ALA A 124 ? 0.8121 0.7417 0.5428 -0.0042 -0.0160 -0.0068 113 ALA A N   
937  C CA  . ALA A 124 ? 0.8471 0.7707 0.5566 -0.0044 -0.0183 -0.0053 113 ALA A CA  
938  C C   . ALA A 124 ? 0.8884 0.8082 0.5821 -0.0019 -0.0086 -0.0073 113 ALA A C   
939  O O   . ALA A 124 ? 0.9064 0.8189 0.5787 -0.0017 -0.0100 -0.0089 113 ALA A O   
940  C CB  . ALA A 124 ? 0.8411 0.7684 0.5534 -0.0059 -0.0213 0.0032  113 ALA A CB  
941  N N   . SER A 125 ? 0.9021 0.8265 0.6061 0.0001  0.0013  -0.0071 114 SER A N   
942  C CA  . SER A 125 ? 0.9293 0.8510 0.6219 0.0030  0.0119  -0.0086 114 SER A CA  
943  C C   . SER A 125 ? 0.9607 0.8753 0.6439 0.0045  0.0130  -0.0176 114 SER A C   
944  O O   . SER A 125 ? 0.9700 0.8769 0.6318 0.0058  0.0156  -0.0204 114 SER A O   
945  C CB  . SER A 125 ? 0.9338 0.8632 0.6437 0.0043  0.0212  -0.0051 114 SER A CB  
946  O OG  . SER A 125 ? 0.9541 0.8893 0.6731 0.0027  0.0198  0.0027  114 SER A OG  
947  N N   . LYS A 126 ? 0.9766 0.8928 0.6744 0.0043  0.0103  -0.0221 115 LYS A N   
948  C CA  . LYS A 126 ? 1.0060 0.9153 0.6976 0.0056  0.0103  -0.0306 115 LYS A CA  
949  C C   . LYS A 126 ? 1.0409 0.9403 0.7107 0.0043  0.0025  -0.0348 115 LYS A C   
950  O O   . LYS A 126 ? 1.0517 0.9428 0.7076 0.0059  0.0049  -0.0418 115 LYS A O   
951  C CB  . LYS A 126 ? 1.0205 0.9335 0.7322 0.0047  0.0060  -0.0332 115 LYS A CB  
952  C CG  . LYS A 126 ? 1.0611 0.9832 0.7940 0.0055  0.0121  -0.0297 115 LYS A CG  
953  C CD  . LYS A 126 ? 1.1074 1.0315 0.8566 0.0051  0.0090  -0.0331 115 LYS A CD  
954  C CE  . LYS A 126 ? 1.1527 1.0774 0.9072 0.0021  -0.0018 -0.0326 115 LYS A CE  
955  N NZ  . LYS A 126 ? 1.1846 1.1025 0.9349 0.0018  -0.0073 -0.0391 115 LYS A NZ  
956  N N   . ALA A 127 ? 1.0559 0.9560 0.7234 0.0014  -0.0073 -0.0304 116 ALA A N   
957  C CA  . ALA A 127 ? 1.0839 0.9755 0.7321 -0.0006 -0.0167 -0.0330 116 ALA A CA  
958  C C   . ALA A 127 ? 1.1111 0.9961 0.7333 0.0007  -0.0118 -0.0323 116 ALA A C   
959  O O   . ALA A 127 ? 1.1282 1.0030 0.7294 0.0008  -0.0141 -0.0385 116 ALA A O   
960  C CB  . ALA A 127 ? 1.0811 0.9767 0.7381 -0.0039 -0.0281 -0.0272 116 ALA A CB  
961  N N   . ASN A 128 ? 1.1149 1.0055 0.7382 0.0016  -0.0046 -0.0250 117 ASN A N   
962  C CA  . ASN A 128 ? 1.1378 1.0233 0.7376 0.0029  0.0012  -0.0227 117 ASN A CA  
963  C C   . ASN A 128 ? 1.1476 1.0319 0.7436 0.0069  0.0163  -0.0257 117 ASN A C   
964  O O   . ASN A 128 ? 1.1516 1.0331 0.7515 0.0087  0.0199  -0.0332 117 ASN A O   
965  C CB  . ASN A 128 ? 1.1527 1.0447 0.7564 0.0015  0.0002  -0.0121 117 ASN A CB  
966  C CG  . ASN A 128 ? 1.1952 1.0893 0.8059 -0.0021 -0.0137 -0.0082 117 ASN A CG  
967  O OD1 . ASN A 128 ? 1.2137 1.1015 0.8154 -0.0041 -0.0240 -0.0124 117 ASN A OD1 
968  N ND2 . ASN A 128 ? 1.1986 1.1014 0.8269 -0.0031 -0.0143 -0.0002 117 ASN A ND2 
969  N N   . LEU A 134 ? 0.8413 0.8116 0.6692 0.0063  0.0523  0.0085  123 LEU A N   
970  C CA  . LEU A 134 ? 0.8341 0.8098 0.6799 0.0038  0.0487  0.0110  123 LEU A CA  
971  C C   . LEU A 134 ? 0.8200 0.8006 0.6807 0.0046  0.0552  0.0139  123 LEU A C   
972  O O   . LEU A 134 ? 0.8279 0.8080 0.6898 0.0070  0.0602  0.0114  123 LEU A O   
973  C CB  . LEU A 134 ? 0.8389 0.8142 0.6897 0.0027  0.0417  0.0062  123 LEU A CB  
974  C CG  . LEU A 134 ? 0.8735 0.8434 0.7117 0.0029  0.0364  0.0012  123 LEU A CG  
975  C CD1 . LEU A 134 ? 0.8793 0.8484 0.7226 0.0038  0.0354  -0.0038 123 LEU A CD1 
976  C CD2 . LEU A 134 ? 0.8875 0.8574 0.7260 0.0003  0.0285  0.0020  123 LEU A CD2 
977  N N   . PRO A 135 ? 0.7962 0.7816 0.6706 0.0024  0.0544  0.0187  124 PRO A N   
978  C CA  . PRO A 135 ? 0.7740 0.7644 0.6657 0.0026  0.0586  0.0213  124 PRO A CA  
979  C C   . PRO A 135 ? 0.7516 0.7426 0.6510 0.0026  0.0550  0.0169  124 PRO A C   
980  O O   . PRO A 135 ? 0.7583 0.7465 0.6514 0.0018  0.0486  0.0126  124 PRO A O   
981  C CB  . PRO A 135 ? 0.7805 0.7745 0.6837 -0.0006 0.0555  0.0262  124 PRO A CB  
982  C CG  . PRO A 135 ? 0.7950 0.7858 0.6865 -0.0016 0.0521  0.0271  124 PRO A CG  
983  C CD  . PRO A 135 ? 0.7869 0.7729 0.6631 -0.0004 0.0488  0.0216  124 PRO A CD  
984  N N   . ARG A 136 ? 0.7191 0.7139 0.6323 0.0036  0.0592  0.0184  125 ARG A N   
985  C CA  . ARG A 136 ? 0.6935 0.6892 0.6154 0.0039  0.0567  0.0153  125 ARG A CA  
986  C C   . ARG A 136 ? 0.6513 0.6470 0.5760 0.0007  0.0467  0.0133  125 ARG A C   
987  O O   . ARG A 136 ? 0.6563 0.6491 0.5755 0.0012  0.0431  0.0088  125 ARG A O   
988  C CB  . ARG A 136 ? 0.7172 0.7183 0.6577 0.0047  0.0617  0.0194  125 ARG A CB  
989  C CG  . ARG A 136 ? 0.7741 0.7747 0.7186 0.0079  0.0664  0.0166  125 ARG A CG  
990  C CD  . ARG A 136 ? 0.8233 0.8283 0.7819 0.0101  0.0756  0.0213  125 ARG A CD  
991  N NE  . ARG A 136 ? 0.8627 0.8740 0.8411 0.0071  0.0722  0.0270  125 ARG A NE  
992  C CZ  . ARG A 136 ? 0.8959 0.9108 0.8907 0.0060  0.0680  0.0280  125 ARG A CZ  
993  N NH1 . ARG A 136 ? 0.8905 0.9036 0.8854 0.0078  0.0671  0.0240  125 ARG A NH1 
994  N NH2 . ARG A 136 ? 0.8918 0.9120 0.9035 0.0029  0.0642  0.0332  125 ARG A NH2 
995  N N   . GLY A 137 ? 0.6070 0.6054 0.5396 -0.0024 0.0425  0.0165  126 GLY A N   
996  C CA  . GLY A 137 ? 0.5724 0.5705 0.5069 -0.0054 0.0340  0.0147  126 GLY A CA  
997  C C   . GLY A 137 ? 0.5298 0.5247 0.4539 -0.0071 0.0298  0.0136  126 GLY A C   
998  O O   . GLY A 137 ? 0.5186 0.5133 0.4455 -0.0098 0.0239  0.0131  126 GLY A O   
999  N N   . MET A 138 ? 0.4989 0.4909 0.4107 -0.0055 0.0325  0.0132  127 MET A N   
1000 C CA  . MET A 138 ? 0.4834 0.4727 0.3871 -0.0070 0.0283  0.0127  127 MET A CA  
1001 C C   . MET A 138 ? 0.4664 0.4534 0.3663 -0.0078 0.0223  0.0086  127 MET A C   
1002 O O   . MET A 138 ? 0.4708 0.4573 0.3726 -0.0101 0.0180  0.0088  127 MET A O   
1003 C CB  . MET A 138 ? 0.4982 0.4849 0.3898 -0.0053 0.0316  0.0138  127 MET A CB  
1004 C CG  . MET A 138 ? 0.5304 0.5148 0.4161 -0.0068 0.0270  0.0142  127 MET A CG  
1005 S SD  . MET A 138 ? 0.5810 0.5620 0.4511 -0.0052 0.0292  0.0157  127 MET A SD  
1006 C CE  . MET A 138 ? 0.5919 0.5709 0.4601 -0.0072 0.0220  0.0156  127 MET A CE  
1007 N N   . VAL A 139 ? 0.4468 0.4320 0.3420 -0.0061 0.0223  0.0051  128 VAL A N   
1008 C CA  . VAL A 139 ? 0.4436 0.4268 0.3362 -0.0067 0.0172  0.0016  128 VAL A CA  
1009 C C   . VAL A 139 ? 0.4385 0.4240 0.3409 -0.0088 0.0137  0.0019  128 VAL A C   
1010 O O   . VAL A 139 ? 0.4393 0.4236 0.3408 -0.0106 0.0094  0.0011  128 VAL A O   
1011 C CB  . VAL A 139 ? 0.4576 0.4384 0.3448 -0.0042 0.0186  -0.0020 128 VAL A CB  
1012 C CG1 . VAL A 139 ? 0.4660 0.4456 0.3543 -0.0049 0.0136  -0.0049 128 VAL A CG1 
1013 C CG2 . VAL A 139 ? 0.4716 0.4487 0.3457 -0.0026 0.0203  -0.0030 128 VAL A CG2 
1014 N N   . LYS A 140 ? 0.4229 0.4114 0.3348 -0.0086 0.0157  0.0035  129 LYS A N   
1015 C CA  . LYS A 140 ? 0.4116 0.4022 0.3326 -0.0109 0.0119  0.0044  129 LYS A CA  
1016 C C   . LYS A 140 ? 0.4137 0.4041 0.3358 -0.0138 0.0089  0.0059  129 LYS A C   
1017 O O   . LYS A 140 ? 0.4259 0.4152 0.3478 -0.0158 0.0044  0.0049  129 LYS A O   
1018 C CB  . LYS A 140 ? 0.4123 0.4066 0.3448 -0.0102 0.0145  0.0067  129 LYS A CB  
1019 C CG  . LYS A 140 ? 0.4295 0.4259 0.3712 -0.0130 0.0093  0.0081  129 LYS A CG  
1020 C CD  . LYS A 140 ? 0.4444 0.4449 0.3999 -0.0126 0.0110  0.0113  129 LYS A CD  
1021 C CE  . LYS A 140 ? 0.4528 0.4536 0.4101 -0.0090 0.0157  0.0101  129 LYS A CE  
1022 N NZ  . LYS A 140 ? 0.4605 0.4655 0.4335 -0.0089 0.0160  0.0132  129 LYS A NZ  
1023 N N   . SER A 141 ? 0.3999 0.3910 0.3229 -0.0140 0.0117  0.0084  130 SER A N   
1024 C CA  . SER A 141 ? 0.3922 0.3825 0.3173 -0.0166 0.0094  0.0099  130 SER A CA  
1025 C C   . SER A 141 ? 0.3990 0.3857 0.3157 -0.0171 0.0069  0.0077  130 SER A C   
1026 O O   . SER A 141 ? 0.4048 0.3898 0.3224 -0.0194 0.0037  0.0070  130 SER A O   
1027 C CB  . SER A 141 ? 0.3941 0.3860 0.3231 -0.0163 0.0135  0.0136  130 SER A CB  
1028 O OG  . SER A 141 ? 0.4015 0.3972 0.3402 -0.0157 0.0165  0.0161  130 SER A OG  
1029 N N   . LEU A 142 ? 0.3929 0.3781 0.3015 -0.0150 0.0084  0.0066  131 LEU A N   
1030 C CA  . LEU A 142 ? 0.3925 0.3747 0.2947 -0.0152 0.0060  0.0050  131 LEU A CA  
1031 C C   . LEU A 142 ? 0.3986 0.3797 0.3007 -0.0161 0.0025  0.0023  131 LEU A C   
1032 O O   . LEU A 142 ? 0.4076 0.3868 0.3092 -0.0176 0.0005  0.0016  131 LEU A O   
1033 C CB  . LEU A 142 ? 0.3901 0.3709 0.2841 -0.0129 0.0074  0.0044  131 LEU A CB  
1034 C CG  . LEU A 142 ? 0.3943 0.3751 0.2853 -0.0121 0.0104  0.0075  131 LEU A CG  
1035 C CD1 . LEU A 142 ? 0.3983 0.3775 0.2796 -0.0100 0.0114  0.0065  131 LEU A CD1 
1036 C CD2 . LEU A 142 ? 0.4020 0.3814 0.2939 -0.0135 0.0087  0.0092  131 LEU A CD2 
1037 N N   . LEU A 143 ? 0.3964 0.3787 0.2994 -0.0153 0.0022  0.0010  132 LEU A N   
1038 C CA  . LEU A 143 ? 0.4075 0.3891 0.3107 -0.0161 -0.0009 -0.0008 132 LEU A CA  
1039 C C   . LEU A 143 ? 0.3991 0.3808 0.3062 -0.0188 -0.0032 -0.0001 132 LEU A C   
1040 O O   . LEU A 143 ? 0.3975 0.3769 0.3016 -0.0200 -0.0053 -0.0013 132 LEU A O   
1041 C CB  . LEU A 143 ? 0.4122 0.3951 0.3172 -0.0145 -0.0006 -0.0017 132 LEU A CB  
1042 C CG  . LEU A 143 ? 0.4288 0.4113 0.3350 -0.0155 -0.0038 -0.0026 132 LEU A CG  
1043 C CD1 . LEU A 143 ? 0.4349 0.4148 0.3359 -0.0155 -0.0053 -0.0041 132 LEU A CD1 
1044 C CD2 . LEU A 143 ? 0.4337 0.4175 0.3439 -0.0140 -0.0034 -0.0030 132 LEU A CD2 
1045 N N   . TYR A 144 ? 0.3892 0.3731 0.3027 -0.0197 -0.0028 0.0019  133 TYR A N   
1046 C CA  . TYR A 144 ? 0.3937 0.3772 0.3106 -0.0227 -0.0061 0.0025  133 TYR A CA  
1047 C C   . TYR A 144 ? 0.3879 0.3678 0.3009 -0.0243 -0.0068 0.0014  133 TYR A C   
1048 O O   . TYR A 144 ? 0.3937 0.3708 0.3037 -0.0263 -0.0096 0.0000  133 TYR A O   
1049 C CB  . TYR A 144 ? 0.3939 0.3806 0.3204 -0.0236 -0.0058 0.0054  133 TYR A CB  
1050 C CG  . TYR A 144 ? 0.4053 0.3913 0.3351 -0.0270 -0.0108 0.0058  133 TYR A CG  
1051 C CD1 . TYR A 144 ? 0.4146 0.4018 0.3465 -0.0278 -0.0142 0.0062  133 TYR A CD1 
1052 C CD2 . TYR A 144 ? 0.4168 0.4000 0.3463 -0.0296 -0.0127 0.0056  133 TYR A CD2 
1053 C CE1 . TYR A 144 ? 0.4264 0.4122 0.3591 -0.0312 -0.0197 0.0066  133 TYR A CE1 
1054 C CE2 . TYR A 144 ? 0.4309 0.4122 0.3610 -0.0330 -0.0180 0.0052  133 TYR A CE2 
1055 C CZ  . TYR A 144 ? 0.4432 0.4258 0.3743 -0.0339 -0.0217 0.0059  133 TYR A CZ  
1056 O OH  . TYR A 144 ? 0.4738 0.4542 0.4043 -0.0375 -0.0277 0.0059  133 TYR A OH  
1057 N N   . GLN A 145 ? 0.3774 0.3569 0.2899 -0.0233 -0.0040 0.0023  134 GLN A N   
1058 C CA  . GLN A 145 ? 0.3766 0.3525 0.2871 -0.0245 -0.0042 0.0016  134 GLN A CA  
1059 C C   . GLN A 145 ? 0.3775 0.3504 0.2815 -0.0238 -0.0044 -0.0008 134 GLN A C   
1060 O O   . GLN A 145 ? 0.3861 0.3553 0.2879 -0.0253 -0.0053 -0.0025 134 GLN A O   
1061 C CB  . GLN A 145 ? 0.3903 0.3669 0.3035 -0.0237 -0.0013 0.0041  134 GLN A CB  
1062 C CG  . GLN A 145 ? 0.4061 0.3850 0.3276 -0.0252 -0.0013 0.0067  134 GLN A CG  
1063 C CD  . GLN A 145 ? 0.4164 0.3954 0.3412 -0.0250 0.0015  0.0096  134 GLN A CD  
1064 O OE1 . GLN A 145 ? 0.4062 0.3823 0.3289 -0.0251 0.0017  0.0093  134 GLN A OE1 
1065 N NE2 . GLN A 145 ? 0.4215 0.4042 0.3527 -0.0245 0.0039  0.0130  134 GLN A NE2 
1066 N N   . ILE A 146 ? 0.3645 0.3386 0.2656 -0.0216 -0.0035 -0.0011 135 ILE A N   
1067 C CA  . ILE A 146 ? 0.3615 0.3335 0.2587 -0.0209 -0.0038 -0.0028 135 ILE A CA  
1068 C C   . ILE A 146 ? 0.3803 0.3508 0.2755 -0.0225 -0.0057 -0.0044 135 ILE A C   
1069 O O   . ILE A 146 ? 0.3942 0.3615 0.2865 -0.0231 -0.0053 -0.0058 135 ILE A O   
1070 C CB  . ILE A 146 ? 0.3489 0.3225 0.2444 -0.0187 -0.0036 -0.0027 135 ILE A CB  
1071 C CG1 . ILE A 146 ? 0.3554 0.3294 0.2502 -0.0173 -0.0021 -0.0011 135 ILE A CG1 
1072 C CG2 . ILE A 146 ? 0.3423 0.3143 0.2359 -0.0183 -0.0043 -0.0040 135 ILE A CG2 
1073 C CD1 . ILE A 146 ? 0.3579 0.3329 0.2497 -0.0154 -0.0023 -0.0014 135 ILE A CD1 
1074 N N   . LEU A 147 ? 0.3718 0.3445 0.2687 -0.0231 -0.0074 -0.0039 136 LEU A N   
1075 C CA  . LEU A 147 ? 0.3701 0.3418 0.2649 -0.0247 -0.0098 -0.0045 136 LEU A CA  
1076 C C   . LEU A 147 ? 0.3707 0.3388 0.2629 -0.0274 -0.0112 -0.0055 136 LEU A C   
1077 O O   . LEU A 147 ? 0.3796 0.3444 0.2662 -0.0284 -0.0116 -0.0070 136 LEU A O   
1078 C CB  . LEU A 147 ? 0.3686 0.3438 0.2678 -0.0248 -0.0116 -0.0030 136 LEU A CB  
1079 C CG  . LEU A 147 ? 0.3605 0.3379 0.2610 -0.0224 -0.0108 -0.0029 136 LEU A CG  
1080 C CD1 . LEU A 147 ? 0.3454 0.3260 0.2522 -0.0221 -0.0118 -0.0013 136 LEU A CD1 
1081 C CD2 . LEU A 147 ? 0.3668 0.3424 0.2633 -0.0224 -0.0116 -0.0036 136 LEU A CD2 
1082 N N   . ASP A 148 ? 0.3682 0.3365 0.2645 -0.0285 -0.0116 -0.0048 137 ASP A N   
1083 C CA  . ASP A 148 ? 0.3683 0.3325 0.2629 -0.0312 -0.0133 -0.0061 137 ASP A CA  
1084 C C   . ASP A 148 ? 0.3755 0.3345 0.2649 -0.0309 -0.0108 -0.0086 137 ASP A C   
1085 O O   . ASP A 148 ? 0.3777 0.3319 0.2611 -0.0328 -0.0119 -0.0110 137 ASP A O   
1086 C CB  . ASP A 148 ? 0.3730 0.3391 0.2755 -0.0322 -0.0138 -0.0042 137 ASP A CB  
1087 C CG  . ASP A 148 ? 0.4214 0.3843 0.3247 -0.0358 -0.0178 -0.0049 137 ASP A CG  
1088 O OD1 . ASP A 148 ? 0.4261 0.3841 0.3216 -0.0376 -0.0199 -0.0076 137 ASP A OD1 
1089 O OD2 . ASP A 148 ? 0.4319 0.3971 0.3436 -0.0369 -0.0187 -0.0027 137 ASP A OD2 
1090 N N   . GLY A 149 ? 0.3693 0.3292 0.2609 -0.0286 -0.0075 -0.0080 138 GLY A N   
1091 C CA  . GLY A 149 ? 0.3743 0.3299 0.2635 -0.0279 -0.0048 -0.0097 138 GLY A CA  
1092 C C   . GLY A 149 ? 0.3943 0.3482 0.2780 -0.0271 -0.0035 -0.0112 138 GLY A C   
1093 O O   . GLY A 149 ? 0.4079 0.3567 0.2874 -0.0276 -0.0016 -0.0136 138 GLY A O   
1094 N N   . ILE A 150 ? 0.3935 0.3513 0.2775 -0.0258 -0.0040 -0.0098 139 ILE A N   
1095 C CA  . ILE A 150 ? 0.4049 0.3618 0.2852 -0.0251 -0.0028 -0.0104 139 ILE A CA  
1096 C C   . ILE A 150 ? 0.4115 0.3652 0.2846 -0.0273 -0.0043 -0.0118 139 ILE A C   
1097 O O   . ILE A 150 ? 0.4056 0.3556 0.2732 -0.0273 -0.0018 -0.0132 139 ILE A O   
1098 C CB  . ILE A 150 ? 0.4128 0.3744 0.2963 -0.0233 -0.0035 -0.0085 139 ILE A CB  
1099 C CG1 . ILE A 150 ? 0.4379 0.4012 0.3261 -0.0212 -0.0022 -0.0074 139 ILE A CG1 
1100 C CG2 . ILE A 150 ? 0.4169 0.3780 0.2977 -0.0230 -0.0028 -0.0085 139 ILE A CG2 
1101 C CD1 . ILE A 150 ? 0.4612 0.4219 0.3507 -0.0203 0.0007  -0.0077 139 ILE A CD1 
1102 N N   . HIS A 151 ? 0.4153 0.3703 0.2884 -0.0293 -0.0081 -0.0112 140 HIS A N   
1103 C CA  . HIS A 151 ? 0.4319 0.3838 0.2977 -0.0318 -0.0109 -0.0121 140 HIS A CA  
1104 C C   . HIS A 151 ? 0.4429 0.3877 0.3019 -0.0335 -0.0098 -0.0155 140 HIS A C   
1105 O O   . HIS A 151 ? 0.4525 0.3928 0.3020 -0.0346 -0.0094 -0.0171 140 HIS A O   
1106 C CB  . HIS A 151 ? 0.4503 0.4054 0.3200 -0.0337 -0.0160 -0.0102 140 HIS A CB  
1107 C CG  . HIS A 151 ? 0.5048 0.4561 0.3671 -0.0370 -0.0202 -0.0109 140 HIS A CG  
1108 N ND1 . HIS A 151 ? 0.5370 0.4853 0.3990 -0.0398 -0.0235 -0.0122 140 HIS A ND1 
1109 C CD2 . HIS A 151 ? 0.5276 0.4771 0.3819 -0.0380 -0.0217 -0.0106 140 HIS A CD2 
1110 C CE1 . HIS A 151 ? 0.5487 0.4933 0.4019 -0.0425 -0.0275 -0.0128 140 HIS A CE1 
1111 N NE2 . HIS A 151 ? 0.5470 0.4921 0.3947 -0.0416 -0.0264 -0.0117 140 HIS A NE2 
1112 N N   . TYR A 152 ? 0.4377 0.3812 0.3011 -0.0335 -0.0088 -0.0165 141 TYR A N   
1113 C CA  . TYR A 152 ? 0.4321 0.3682 0.2901 -0.0348 -0.0074 -0.0201 141 TYR A CA  
1114 C C   . TYR A 152 ? 0.4283 0.3608 0.2820 -0.0327 -0.0016 -0.0218 141 TYR A C   
1115 O O   . TYR A 152 ? 0.4305 0.3562 0.2745 -0.0337 0.0000  -0.0250 141 TYR A O   
1116 C CB  . TYR A 152 ? 0.4220 0.3580 0.2880 -0.0350 -0.0075 -0.0200 141 TYR A CB  
1117 C CG  . TYR A 152 ? 0.4263 0.3544 0.2887 -0.0357 -0.0051 -0.0238 141 TYR A CG  
1118 C CD1 . TYR A 152 ? 0.4299 0.3512 0.2849 -0.0390 -0.0082 -0.0273 141 TYR A CD1 
1119 C CD2 . TYR A 152 ? 0.4298 0.3564 0.2961 -0.0331 0.0002  -0.0242 141 TYR A CD2 
1120 C CE1 . TYR A 152 ? 0.4355 0.3483 0.2866 -0.0395 -0.0057 -0.0315 141 TYR A CE1 
1121 C CE2 . TYR A 152 ? 0.4365 0.3554 0.3006 -0.0335 0.0029  -0.0278 141 TYR A CE2 
1122 C CZ  . TYR A 152 ? 0.4457 0.3574 0.3017 -0.0366 0.0004  -0.0319 141 TYR A CZ  
1123 O OH  . TYR A 152 ? 0.4650 0.3680 0.3183 -0.0367 0.0036  -0.0361 141 TYR A OH  
1124 N N   . LEU A 153 ? 0.4131 0.3499 0.2741 -0.0297 0.0016  -0.0196 142 LEU A N   
1125 C CA  . LEU A 153 ? 0.4129 0.3476 0.2731 -0.0274 0.0071  -0.0202 142 LEU A CA  
1126 C C   . LEU A 153 ? 0.4130 0.3462 0.2643 -0.0279 0.0081  -0.0205 142 LEU A C   
1127 O O   . LEU A 153 ? 0.4137 0.3408 0.2576 -0.0279 0.0121  -0.0230 142 LEU A O   
1128 C CB  . LEU A 153 ? 0.4128 0.3533 0.2831 -0.0247 0.0085  -0.0170 142 LEU A CB  
1129 C CG  . LEU A 153 ? 0.4254 0.3673 0.3039 -0.0238 0.0083  -0.0159 142 LEU A CG  
1130 C CD1 . LEU A 153 ? 0.4287 0.3755 0.3147 -0.0214 0.0088  -0.0128 142 LEU A CD1 
1131 C CD2 . LEU A 153 ? 0.4248 0.3605 0.3037 -0.0238 0.0117  -0.0183 142 LEU A CD2 
1132 N N   . HIS A 154 ? 0.4072 0.3454 0.2590 -0.0282 0.0046  -0.0178 143 HIS A N   
1133 C CA  . HIS A 154 ? 0.4112 0.3490 0.2559 -0.0287 0.0049  -0.0169 143 HIS A CA  
1134 C C   . HIS A 154 ? 0.4281 0.3594 0.2596 -0.0315 0.0033  -0.0194 143 HIS A C   
1135 O O   . HIS A 154 ? 0.4291 0.3567 0.2518 -0.0315 0.0066  -0.0199 143 HIS A O   
1136 C CB  . HIS A 154 ? 0.3979 0.3424 0.2478 -0.0285 0.0010  -0.0134 143 HIS A CB  
1137 C CG  . HIS A 154 ? 0.3942 0.3438 0.2543 -0.0258 0.0026  -0.0112 143 HIS A CG  
1138 N ND1 . HIS A 154 ? 0.4071 0.3618 0.2723 -0.0253 -0.0003 -0.0087 143 HIS A ND1 
1139 C CD2 . HIS A 154 ? 0.3948 0.3445 0.2606 -0.0237 0.0063  -0.0113 143 HIS A CD2 
1140 C CE1 . HIS A 154 ? 0.4105 0.3678 0.2830 -0.0231 0.0013  -0.0078 143 HIS A CE1 
1141 N NE2 . HIS A 154 ? 0.4013 0.3561 0.2748 -0.0221 0.0050  -0.0089 143 HIS A NE2 
1142 N N   . ALA A 155 ? 0.4324 0.3621 0.2624 -0.0341 -0.0016 -0.0208 144 ALA A N   
1143 C CA  . ALA A 155 ? 0.4524 0.3751 0.2692 -0.0372 -0.0042 -0.0236 144 ALA A CA  
1144 C C   . ALA A 155 ? 0.4840 0.3980 0.2922 -0.0367 0.0018  -0.0282 144 ALA A C   
1145 O O   . ALA A 155 ? 0.4970 0.4039 0.2908 -0.0386 0.0020  -0.0308 144 ALA A O   
1146 C CB  . ALA A 155 ? 0.4428 0.3656 0.2626 -0.0401 -0.0110 -0.0241 144 ALA A CB  
1147 N N   . ASN A 156 ? 0.4890 0.4033 0.3060 -0.0342 0.0068  -0.0290 145 ASN A N   
1148 C CA  . ASN A 156 ? 0.5042 0.4109 0.3166 -0.0329 0.0135  -0.0330 145 ASN A CA  
1149 C C   . ASN A 156 ? 0.5231 0.4311 0.3374 -0.0296 0.0210  -0.0313 145 ASN A C   
1150 O O   . ASN A 156 ? 0.5309 0.4346 0.3467 -0.0277 0.0275  -0.0335 145 ASN A O   
1151 C CB  . ASN A 156 ? 0.4980 0.4042 0.3208 -0.0322 0.0141  -0.0342 145 ASN A CB  
1152 C CG  . ASN A 156 ? 0.5122 0.4137 0.3310 -0.0356 0.0086  -0.0372 145 ASN A CG  
1153 O OD1 . ASN A 156 ? 0.5355 0.4283 0.3416 -0.0377 0.0085  -0.0416 145 ASN A OD1 
1154 N ND2 . ASN A 156 ? 0.5020 0.4090 0.3312 -0.0364 0.0038  -0.0347 145 ASN A ND2 
1155 N N   . TRP A 157 ? 0.5260 0.4402 0.3422 -0.0290 0.0200  -0.0271 146 TRP A N   
1156 C CA  . TRP A 157 ? 0.5403 0.4570 0.3604 -0.0262 0.0261  -0.0245 146 TRP A CA  
1157 C C   . TRP A 157 ? 0.5122 0.4326 0.3475 -0.0232 0.0297  -0.0231 146 TRP A C   
1158 O O   . TRP A 157 ? 0.5135 0.4331 0.3523 -0.0208 0.0364  -0.0223 146 TRP A O   
1159 C CB  . TRP A 157 ? 0.5740 0.4831 0.3807 -0.0261 0.0325  -0.0268 146 TRP A CB  
1160 C CG  . TRP A 157 ? 0.6294 0.5352 0.4204 -0.0293 0.0282  -0.0273 146 TRP A CG  
1161 C CD1 . TRP A 157 ? 0.6633 0.5610 0.4397 -0.0321 0.0256  -0.0317 146 TRP A CD1 
1162 C CD2 . TRP A 157 ? 0.6445 0.5552 0.4335 -0.0301 0.0247  -0.0228 146 TRP A CD2 
1163 N NE1 . TRP A 157 ? 0.6814 0.5787 0.4464 -0.0348 0.0205  -0.0300 146 TRP A NE1 
1164 C CE2 . TRP A 157 ? 0.6703 0.5757 0.4433 -0.0335 0.0201  -0.0243 146 TRP A CE2 
1165 C CE3 . TRP A 157 ? 0.6468 0.5655 0.4466 -0.0285 0.0248  -0.0176 146 TRP A CE3 
1166 C CZ2 . TRP A 157 ? 0.6809 0.5890 0.4485 -0.0351 0.0160  -0.0202 146 TRP A CZ2 
1167 C CZ3 . TRP A 157 ? 0.6612 0.5823 0.4562 -0.0300 0.0209  -0.0141 146 TRP A CZ3 
1168 C CH2 . TRP A 157 ? 0.6729 0.5890 0.4523 -0.0332 0.0166  -0.0151 146 TRP A CH2 
1169 N N   . VAL A 158 ? 0.4813 0.4059 0.3258 -0.0233 0.0251  -0.0222 147 VAL A N   
1170 C CA  . VAL A 158 ? 0.4612 0.3895 0.3194 -0.0208 0.0270  -0.0203 147 VAL A CA  
1171 C C   . VAL A 158 ? 0.4419 0.3783 0.3082 -0.0202 0.0227  -0.0162 147 VAL A C   
1172 O O   . VAL A 158 ? 0.4384 0.3780 0.3043 -0.0216 0.0171  -0.0156 147 VAL A O   
1173 C CB  . VAL A 158 ? 0.4572 0.3831 0.3195 -0.0211 0.0259  -0.0222 147 VAL A CB  
1174 C CG1 . VAL A 158 ? 0.4563 0.3871 0.3327 -0.0189 0.0261  -0.0190 147 VAL A CG1 
1175 C CG2 . VAL A 158 ? 0.4561 0.3731 0.3120 -0.0212 0.0310  -0.0267 147 VAL A CG2 
1176 N N   . LEU A 159 ? 0.4284 0.3681 0.3026 -0.0181 0.0255  -0.0135 148 LEU A N   
1177 C CA  . LEU A 159 ? 0.4240 0.3704 0.3062 -0.0175 0.0213  -0.0101 148 LEU A CA  
1178 C C   . LEU A 159 ? 0.4167 0.3651 0.3089 -0.0161 0.0205  -0.0090 148 LEU A C   
1179 O O   . LEU A 159 ? 0.4201 0.3659 0.3166 -0.0149 0.0246  -0.0094 148 LEU A O   
1180 C CB  . LEU A 159 ? 0.4270 0.3758 0.3130 -0.0164 0.0235  -0.0074 148 LEU A CB  
1181 C CG  . LEU A 159 ? 0.4519 0.3978 0.3279 -0.0174 0.0263  -0.0078 148 LEU A CG  
1182 C CD1 . LEU A 159 ? 0.4536 0.4020 0.3357 -0.0161 0.0293  -0.0044 148 LEU A CD1 
1183 C CD2 . LEU A 159 ? 0.4552 0.4017 0.3229 -0.0197 0.0208  -0.0083 148 LEU A CD2 
1184 N N   . HIS A 160 ? 0.4057 0.3584 0.3011 -0.0164 0.0153  -0.0077 149 HIS A N   
1185 C CA  . HIS A 160 ? 0.3985 0.3532 0.3018 -0.0153 0.0139  -0.0060 149 HIS A CA  
1186 C C   . HIS A 160 ? 0.4047 0.3621 0.3171 -0.0137 0.0145  -0.0032 149 HIS A C   
1187 O O   . HIS A 160 ? 0.4030 0.3597 0.3229 -0.0124 0.0167  -0.0018 149 HIS A O   
1188 C CB  . HIS A 160 ? 0.3863 0.3442 0.2885 -0.0160 0.0087  -0.0054 149 HIS A CB  
1189 C CG  . HIS A 160 ? 0.3928 0.3520 0.3009 -0.0150 0.0073  -0.0035 149 HIS A CG  
1190 N ND1 . HIS A 160 ? 0.4050 0.3666 0.3204 -0.0137 0.0061  -0.0009 149 HIS A ND1 
1191 C CD2 . HIS A 160 ? 0.4009 0.3594 0.3090 -0.0154 0.0066  -0.0033 149 HIS A CD2 
1192 C CE1 . HIS A 160 ? 0.4078 0.3697 0.3259 -0.0133 0.0044  0.0008  149 HIS A CE1 
1193 N NE2 . HIS A 160 ? 0.4178 0.3781 0.3319 -0.0142 0.0050  -0.0004 149 HIS A NE2 
1194 N N   . ARG A 161 ? 0.4099 0.3701 0.3226 -0.0138 0.0124  -0.0020 150 ARG A N   
1195 C CA  . ARG A 161 ? 0.4161 0.3790 0.3381 -0.0127 0.0122  0.0008  150 ARG A CA  
1196 C C   . ARG A 161 ? 0.4193 0.3852 0.3477 -0.0123 0.0069  0.0028  150 ARG A C   
1197 O O   . ARG A 161 ? 0.4250 0.3930 0.3613 -0.0118 0.0052  0.0051  150 ARG A O   
1198 C CB  . ARG A 161 ? 0.4393 0.4004 0.3681 -0.0113 0.0182  0.0020  150 ARG A CB  
1199 C CG  . ARG A 161 ? 0.4881 0.4454 0.4096 -0.0115 0.0244  0.0002  150 ARG A CG  
1200 C CD  . ARG A 161 ? 0.5287 0.4838 0.4577 -0.0097 0.0313  0.0012  150 ARG A CD  
1201 N NE  . ARG A 161 ? 0.5769 0.5269 0.4966 -0.0097 0.0381  -0.0013 150 ARG A NE  
1202 C CZ  . ARG A 161 ? 0.6108 0.5563 0.5319 -0.0083 0.0452  -0.0025 150 ARG A CZ  
1203 N NH1 . ARG A 161 ? 0.6074 0.5474 0.5174 -0.0084 0.0512  -0.0052 150 ARG A NH1 
1204 N NH2 . ARG A 161 ? 0.6121 0.5582 0.5453 -0.0067 0.0462  -0.0011 150 ARG A NH2 
1205 N N   . ASP A 162 ? 0.4128 0.3786 0.3377 -0.0126 0.0041  0.0021  151 ASP A N   
1206 C CA  . ASP A 162 ? 0.4142 0.3821 0.3430 -0.0123 -0.0009 0.0040  151 ASP A CA  
1207 C C   . ASP A 162 ? 0.4102 0.3784 0.3315 -0.0128 -0.0039 0.0029  151 ASP A C   
1208 O O   . ASP A 162 ? 0.4149 0.3836 0.3373 -0.0126 -0.0065 0.0046  151 ASP A O   
1209 C CB  . ASP A 162 ? 0.4421 0.4099 0.3803 -0.0113 0.0000  0.0068  151 ASP A CB  
1210 C CG  . ASP A 162 ? 0.5256 0.4955 0.4688 -0.0112 -0.0060 0.0096  151 ASP A CG  
1211 O OD1 . ASP A 162 ? 0.5242 0.4955 0.4672 -0.0116 -0.0099 0.0095  151 ASP A OD1 
1212 O OD2 . ASP A 162 ? 0.5755 0.5453 0.5230 -0.0107 -0.0071 0.0120  151 ASP A OD2 
1213 N N   . LEU A 163 ? 0.3966 0.3646 0.3106 -0.0136 -0.0034 0.0006  152 LEU A N   
1214 C CA  . LEU A 163 ? 0.4024 0.3709 0.3105 -0.0140 -0.0053 -0.0002 152 LEU A CA  
1215 C C   . LEU A 163 ? 0.4009 0.3707 0.3080 -0.0135 -0.0095 0.0005  152 LEU A C   
1216 O O   . LEU A 163 ? 0.4081 0.3785 0.3161 -0.0134 -0.0117 -0.0001 152 LEU A O   
1217 C CB  . LEU A 163 ? 0.4137 0.3822 0.3164 -0.0149 -0.0047 -0.0023 152 LEU A CB  
1218 C CG  . LEU A 163 ? 0.4506 0.4172 0.3511 -0.0159 -0.0018 -0.0034 152 LEU A CG  
1219 C CD1 . LEU A 163 ? 0.4637 0.4308 0.3601 -0.0169 -0.0024 -0.0047 152 LEU A CD1 
1220 C CD2 . LEU A 163 ? 0.4625 0.4281 0.3624 -0.0162 -0.0011 -0.0031 152 LEU A CD2 
1221 N N   . LYS A 164 ? 0.3911 0.3607 0.2956 -0.0133 -0.0106 0.0016  153 LYS A N   
1222 C CA  . LYS A 164 ? 0.3932 0.3630 0.2938 -0.0129 -0.0144 0.0020  153 LYS A CA  
1223 C C   . LYS A 164 ? 0.3897 0.3594 0.2849 -0.0128 -0.0135 0.0028  153 LYS A C   
1224 O O   . LYS A 164 ? 0.3860 0.3555 0.2830 -0.0131 -0.0108 0.0039  153 LYS A O   
1225 C CB  . LYS A 164 ? 0.4176 0.3874 0.3236 -0.0127 -0.0181 0.0043  153 LYS A CB  
1226 C CG  . LYS A 164 ? 0.4781 0.4478 0.3899 -0.0125 -0.0170 0.0074  153 LYS A CG  
1227 C CD  . LYS A 164 ? 0.5495 0.5195 0.4669 -0.0125 -0.0216 0.0103  153 LYS A CD  
1228 C CE  . LYS A 164 ? 0.5986 0.5690 0.5278 -0.0120 -0.0194 0.0126  153 LYS A CE  
1229 N NZ  . LYS A 164 ? 0.6325 0.6034 0.5658 -0.0120 -0.0169 0.0108  153 LYS A NZ  
1230 N N   . PRO A 165 ? 0.3905 0.3598 0.2786 -0.0124 -0.0153 0.0023  154 PRO A N   
1231 C CA  . PRO A 165 ? 0.3875 0.3569 0.2703 -0.0121 -0.0136 0.0038  154 PRO A CA  
1232 C C   . PRO A 165 ? 0.3952 0.3644 0.2812 -0.0123 -0.0135 0.0075  154 PRO A C   
1233 O O   . PRO A 165 ? 0.4042 0.3737 0.2903 -0.0125 -0.0106 0.0089  154 PRO A O   
1234 C CB  . PRO A 165 ? 0.3904 0.3584 0.2643 -0.0115 -0.0161 0.0028  154 PRO A CB  
1235 C CG  . PRO A 165 ? 0.3918 0.3593 0.2668 -0.0114 -0.0179 -0.0005 154 PRO A CG  
1236 C CD  . PRO A 165 ? 0.3686 0.3371 0.2531 -0.0121 -0.0187 0.0003  154 PRO A CD  
1237 N N   . ALA A 166 ? 0.3916 0.3604 0.2818 -0.0123 -0.0168 0.0096  155 ALA A N   
1238 C CA  . ALA A 166 ? 0.3917 0.3603 0.2866 -0.0124 -0.0170 0.0137  155 ALA A CA  
1239 C C   . ALA A 166 ? 0.3996 0.3679 0.3017 -0.0126 -0.0127 0.0138  155 ALA A C   
1240 O O   . ALA A 166 ? 0.3958 0.3638 0.3001 -0.0127 -0.0116 0.0168  155 ALA A O   
1241 C CB  . ALA A 166 ? 0.3860 0.3545 0.2862 -0.0124 -0.0217 0.0161  155 ALA A CB  
1242 N N   . ASN A 167 ? 0.3976 0.3658 0.3033 -0.0129 -0.0104 0.0107  156 ASN A N   
1243 C CA  . ASN A 167 ? 0.3981 0.3649 0.3084 -0.0132 -0.0064 0.0101  156 ASN A CA  
1244 C C   . ASN A 167 ? 0.4141 0.3807 0.3199 -0.0142 -0.0040 0.0077  156 ASN A C   
1245 O O   . ASN A 167 ? 0.4259 0.3908 0.3339 -0.0149 -0.0015 0.0060  156 ASN A O   
1246 C CB  . ASN A 167 ? 0.3954 0.3611 0.3121 -0.0130 -0.0048 0.0088  156 ASN A CB  
1247 C CG  . ASN A 167 ? 0.4120 0.3787 0.3265 -0.0130 -0.0054 0.0063  156 ASN A CG  
1248 O OD1 . ASN A 167 ? 0.4249 0.3922 0.3334 -0.0136 -0.0055 0.0041  156 ASN A OD1 
1249 N ND2 . ASN A 167 ? 0.3969 0.3638 0.3175 -0.0125 -0.0058 0.0070  156 ASN A ND2 
1250 N N   . ILE A 168 ? 0.4097 0.3780 0.3094 -0.0141 -0.0049 0.0076  157 ILE A N   
1251 C CA  . ILE A 168 ? 0.4067 0.3755 0.3043 -0.0149 -0.0029 0.0064  157 ILE A CA  
1252 C C   . ILE A 168 ? 0.4007 0.3700 0.2976 -0.0148 -0.0021 0.0098  157 ILE A C   
1253 O O   . ILE A 168 ? 0.4010 0.3715 0.2924 -0.0140 -0.0025 0.0110  157 ILE A O   
1254 C CB  . ILE A 168 ? 0.4190 0.3894 0.3121 -0.0147 -0.0034 0.0041  157 ILE A CB  
1255 C CG1 . ILE A 168 ? 0.4358 0.4058 0.3299 -0.0148 -0.0044 0.0015  157 ILE A CG1 
1256 C CG2 . ILE A 168 ? 0.4234 0.3949 0.3167 -0.0155 -0.0014 0.0038  157 ILE A CG2 
1257 C CD1 . ILE A 168 ? 0.4592 0.4278 0.3560 -0.0160 -0.0028 0.0001  157 ILE A CD1 
1258 N N   . LEU A 169 ? 0.3955 0.3634 0.2975 -0.0155 -0.0007 0.0114  158 LEU A N   
1259 C CA  . LEU A 169 ? 0.3920 0.3602 0.2950 -0.0156 0.0003  0.0153  158 LEU A CA  
1260 C C   . LEU A 169 ? 0.3987 0.3684 0.3013 -0.0164 0.0025  0.0153  158 LEU A C   
1261 O O   . LEU A 169 ? 0.3918 0.3615 0.2955 -0.0173 0.0028  0.0122  158 LEU A O   
1262 C CB  . LEU A 169 ? 0.3855 0.3512 0.2960 -0.0161 0.0011  0.0169  158 LEU A CB  
1263 C CG  . LEU A 169 ? 0.3870 0.3512 0.3015 -0.0153 -0.0002 0.0169  158 LEU A CG  
1264 C CD1 . LEU A 169 ? 0.3808 0.3419 0.3036 -0.0157 0.0015  0.0179  158 LEU A CD1 
1265 C CD2 . LEU A 169 ? 0.3899 0.3556 0.3018 -0.0142 -0.0032 0.0204  158 LEU A CD2 
1266 N N   . VAL A 170 ? 0.4004 0.3714 0.3018 -0.0161 0.0040  0.0192  159 VAL A N   
1267 C CA  . VAL A 170 ? 0.4080 0.3808 0.3111 -0.0167 0.0066  0.0202  159 VAL A CA  
1268 C C   . VAL A 170 ? 0.4143 0.3868 0.3220 -0.0172 0.0082  0.0253  159 VAL A C   
1269 O O   . VAL A 170 ? 0.4098 0.3823 0.3139 -0.0162 0.0081  0.0290  159 VAL A O   
1270 C CB  . VAL A 170 ? 0.4192 0.3943 0.3153 -0.0153 0.0081  0.0200  159 VAL A CB  
1271 C CG1 . VAL A 170 ? 0.4304 0.4079 0.3309 -0.0158 0.0115  0.0216  159 VAL A CG1 
1272 C CG2 . VAL A 170 ? 0.4208 0.3959 0.3132 -0.0147 0.0062  0.0154  159 VAL A CG2 
1273 N N   . MET A 171 ? 0.4103 0.3824 0.3263 -0.0189 0.0092  0.0257  160 MET A N   
1274 C CA  . MET A 171 ? 0.4197 0.3912 0.3417 -0.0196 0.0107  0.0307  160 MET A CA  
1275 C C   . MET A 171 ? 0.4375 0.4121 0.3566 -0.0186 0.0139  0.0357  160 MET A C   
1276 O O   . MET A 171 ? 0.4385 0.4157 0.3548 -0.0180 0.0159  0.0349  160 MET A O   
1277 C CB  . MET A 171 ? 0.4173 0.3872 0.3491 -0.0220 0.0106  0.0295  160 MET A CB  
1278 C CG  . MET A 171 ? 0.4305 0.3962 0.3638 -0.0229 0.0082  0.0244  160 MET A CG  
1279 S SD  . MET A 171 ? 0.4885 0.4506 0.4239 -0.0219 0.0077  0.0258  160 MET A SD  
1280 C CE  . MET A 171 ? 0.4303 0.3910 0.3760 -0.0232 0.0091  0.0308  160 MET A CE  
1281 N N   . GLY A 172 ? 0.4448 0.4189 0.3646 -0.0183 0.0147  0.0412  161 GLY A N   
1282 C CA  . GLY A 172 ? 0.4598 0.4363 0.3762 -0.0174 0.0184  0.0469  161 GLY A CA  
1283 C C   . GLY A 172 ? 0.4741 0.4518 0.4019 -0.0190 0.0213  0.0506  161 GLY A C   
1284 O O   . GLY A 172 ? 0.4720 0.4490 0.4089 -0.0208 0.0201  0.0475  161 GLY A O   
1285 N N   . GLU A 173 ? 0.4819 0.4611 0.4097 -0.0185 0.0249  0.0575  162 GLU A N   
1286 C CA  . GLU A 173 ? 0.4907 0.4713 0.4310 -0.0201 0.0279  0.0621  162 GLU A CA  
1287 C C   . GLU A 173 ? 0.4961 0.4737 0.4493 -0.0225 0.0247  0.0610  162 GLU A C   
1288 O O   . GLU A 173 ? 0.5055 0.4798 0.4584 -0.0224 0.0217  0.0605  162 GLU A O   
1289 C CB  . GLU A 173 ? 0.5191 0.5013 0.4571 -0.0191 0.0322  0.0706  162 GLU A CB  
1290 C CG  . GLU A 173 ? 0.5863 0.5707 0.5108 -0.0167 0.0366  0.0717  162 GLU A CG  
1291 C CD  . GLU A 173 ? 0.6657 0.6536 0.5945 -0.0165 0.0411  0.0704  162 GLU A CD  
1292 O OE1 . GLU A 173 ? 0.6658 0.6553 0.6098 -0.0184 0.0415  0.0712  162 GLU A OE1 
1293 O OE2 . GLU A 173 ? 0.7080 0.6969 0.6256 -0.0143 0.0442  0.0686  162 GLU A OE2 
1294 N N   . GLY A 174 ? 0.4871 0.4654 0.4514 -0.0245 0.0251  0.0603  163 GLY A N   
1295 C CA  . GLY A 174 ? 0.4854 0.4599 0.4614 -0.0272 0.0219  0.0584  163 GLY A CA  
1296 C C   . GLY A 174 ? 0.4901 0.4647 0.4720 -0.0293 0.0198  0.0534  163 GLY A C   
1297 O O   . GLY A 174 ? 0.4872 0.4657 0.4673 -0.0288 0.0214  0.0529  163 GLY A O   
1298 N N   . PRO A 175 ? 0.4938 0.4635 0.4824 -0.0318 0.0160  0.0495  164 PRO A N   
1299 C CA  . PRO A 175 ? 0.4968 0.4656 0.4901 -0.0344 0.0128  0.0447  164 PRO A CA  
1300 C C   . PRO A 175 ? 0.5117 0.4811 0.4948 -0.0336 0.0107  0.0384  164 PRO A C   
1301 O O   . PRO A 175 ? 0.5182 0.4881 0.5045 -0.0356 0.0081  0.0357  164 PRO A O   
1302 C CB  . PRO A 175 ? 0.5072 0.4690 0.5073 -0.0370 0.0093  0.0416  164 PRO A CB  
1303 C CG  . PRO A 175 ? 0.5173 0.4762 0.5134 -0.0349 0.0105  0.0425  164 PRO A CG  
1304 C CD  . PRO A 175 ? 0.4888 0.4530 0.4814 -0.0323 0.0146  0.0495  164 PRO A CD  
1305 N N   . GLU A 176 ? 0.5053 0.4745 0.4768 -0.0310 0.0114  0.0365  165 GLU A N   
1306 C CA  . GLU A 176 ? 0.4974 0.4670 0.4594 -0.0301 0.0097  0.0310  165 GLU A CA  
1307 C C   . GLU A 176 ? 0.4916 0.4657 0.4451 -0.0271 0.0126  0.0328  165 GLU A C   
1308 O O   . GLU A 176 ? 0.4920 0.4657 0.4365 -0.0256 0.0116  0.0292  165 GLU A O   
1309 C CB  . GLU A 176 ? 0.5100 0.4743 0.4664 -0.0299 0.0074  0.0258  165 GLU A CB  
1310 C CG  . GLU A 176 ? 0.5431 0.5015 0.5050 -0.0327 0.0047  0.0222  165 GLU A CG  
1311 C CD  . GLU A 176 ? 0.5968 0.5503 0.5513 -0.0323 0.0032  0.0162  165 GLU A CD  
1312 O OE1 . GLU A 176 ? 0.5884 0.5414 0.5373 -0.0331 0.0012  0.0118  165 GLU A OE1 
1313 O OE2 . GLU A 176 ? 0.6360 0.5862 0.5909 -0.0311 0.0045  0.0163  165 GLU A OE2 
1314 N N   . ARG A 177 ? 0.4784 0.4563 0.4346 -0.0262 0.0165  0.0385  166 ARG A N   
1315 C CA  . ARG A 177 ? 0.4749 0.4562 0.4222 -0.0233 0.0200  0.0403  166 ARG A CA  
1316 C C   . ARG A 177 ? 0.4670 0.4496 0.4082 -0.0224 0.0189  0.0352  166 ARG A C   
1317 O O   . ARG A 177 ? 0.4708 0.4548 0.4181 -0.0238 0.0177  0.0335  166 ARG A O   
1318 C CB  . ARG A 177 ? 0.4856 0.4707 0.4392 -0.0231 0.0249  0.0466  166 ARG A CB  
1319 C CG  . ARG A 177 ? 0.5383 0.5255 0.4814 -0.0201 0.0296  0.0495  166 ARG A CG  
1320 C CD  . ARG A 177 ? 0.5906 0.5817 0.5411 -0.0198 0.0355  0.0554  166 ARG A CD  
1321 N NE  . ARG A 177 ? 0.6523 0.6445 0.5912 -0.0169 0.0409  0.0585  166 ARG A NE  
1322 C CZ  . ARG A 177 ? 0.6973 0.6912 0.6294 -0.0147 0.0444  0.0565  166 ARG A CZ  
1323 N NH1 . ARG A 177 ? 0.6776 0.6731 0.6151 -0.0150 0.0431  0.0521  166 ARG A NH1 
1324 N NH2 . ARG A 177 ? 0.7195 0.7132 0.6394 -0.0121 0.0494  0.0590  166 ARG A NH2 
1325 N N   . GLY A 178 ? 0.4504 0.4322 0.3803 -0.0203 0.0185  0.0331  167 GLY A N   
1326 C CA  . GLY A 178 ? 0.4423 0.4249 0.3661 -0.0192 0.0176  0.0286  167 GLY A CA  
1327 C C   . GLY A 178 ? 0.4278 0.4086 0.3535 -0.0208 0.0133  0.0236  167 GLY A C   
1328 O O   . GLY A 178 ? 0.4271 0.4094 0.3523 -0.0207 0.0126  0.0211  167 GLY A O   
1329 N N   . ARG A 179 ? 0.4161 0.3933 0.3440 -0.0224 0.0107  0.0223  168 ARG A N   
1330 C CA  . ARG A 179 ? 0.4085 0.3832 0.3361 -0.0239 0.0071  0.0174  168 ARG A CA  
1331 C C   . ARG A 179 ? 0.3997 0.3723 0.3196 -0.0224 0.0061  0.0148  168 ARG A C   
1332 O O   . ARG A 179 ? 0.4076 0.3787 0.3266 -0.0216 0.0066  0.0165  168 ARG A O   
1333 C CB  . ARG A 179 ? 0.4243 0.3954 0.3587 -0.0266 0.0053  0.0168  168 ARG A CB  
1334 C CG  . ARG A 179 ? 0.4642 0.4316 0.3955 -0.0281 0.0020  0.0115  168 ARG A CG  
1335 C CD  . ARG A 179 ? 0.5168 0.4801 0.4537 -0.0311 0.0000  0.0103  168 ARG A CD  
1336 N NE  . ARG A 179 ? 0.5600 0.5259 0.5040 -0.0332 -0.0017 0.0119  168 ARG A NE  
1337 C CZ  . ARG A 179 ? 0.5997 0.5630 0.5513 -0.0361 -0.0038 0.0123  168 ARG A CZ  
1338 N NH1 . ARG A 179 ? 0.5944 0.5520 0.5469 -0.0371 -0.0041 0.0107  168 ARG A NH1 
1339 N NH2 . ARG A 179 ? 0.6090 0.5752 0.5685 -0.0381 -0.0057 0.0143  168 ARG A NH2 
1340 N N   . VAL A 180 ? 0.3878 0.3606 0.3034 -0.0221 0.0045  0.0113  169 VAL A N   
1341 C CA  . VAL A 180 ? 0.3835 0.3547 0.2935 -0.0209 0.0034  0.0089  169 VAL A CA  
1342 C C   . VAL A 180 ? 0.3788 0.3457 0.2905 -0.0221 0.0025  0.0070  169 VAL A C   
1343 O O   . VAL A 180 ? 0.3798 0.3446 0.2939 -0.0241 0.0016  0.0051  169 VAL A O   
1344 C CB  . VAL A 180 ? 0.3895 0.3621 0.2958 -0.0204 0.0022  0.0061  169 VAL A CB  
1345 C CG1 . VAL A 180 ? 0.3943 0.3648 0.2968 -0.0198 0.0009  0.0036  169 VAL A CG1 
1346 C CG2 . VAL A 180 ? 0.3859 0.3617 0.2896 -0.0186 0.0037  0.0074  169 VAL A CG2 
1347 N N   . LYS A 181 ? 0.3732 0.3385 0.2839 -0.0208 0.0028  0.0073  170 LYS A N   
1348 C CA  . LYS A 181 ? 0.3744 0.3355 0.2871 -0.0212 0.0030  0.0054  170 LYS A CA  
1349 C C   . LYS A 181 ? 0.3819 0.3431 0.2915 -0.0196 0.0026  0.0042  170 LYS A C   
1350 O O   . LYS A 181 ? 0.3919 0.3548 0.3012 -0.0181 0.0021  0.0066  170 LYS A O   
1351 C CB  . LYS A 181 ? 0.3737 0.3331 0.2919 -0.0210 0.0041  0.0085  170 LYS A CB  
1352 C CG  . LYS A 181 ? 0.3871 0.3462 0.3101 -0.0226 0.0046  0.0105  170 LYS A CG  
1353 C CD  . LYS A 181 ? 0.3896 0.3446 0.3143 -0.0249 0.0039  0.0066  170 LYS A CD  
1354 C CE  . LYS A 181 ? 0.3962 0.3514 0.3274 -0.0267 0.0038  0.0092  170 LYS A CE  
1355 N NZ  . LYS A 181 ? 0.3907 0.3412 0.3237 -0.0295 0.0021  0.0054  170 LYS A NZ  
1356 N N   . ILE A 182 ? 0.3751 0.3346 0.2822 -0.0202 0.0026  0.0007  171 ILE A N   
1357 C CA  . ILE A 182 ? 0.3720 0.3315 0.2777 -0.0189 0.0027  -0.0003 171 ILE A CA  
1358 C C   . ILE A 182 ? 0.3682 0.3247 0.2788 -0.0181 0.0046  0.0003  171 ILE A C   
1359 O O   . ILE A 182 ? 0.3616 0.3141 0.2741 -0.0189 0.0064  -0.0013 171 ILE A O   
1360 C CB  . ILE A 182 ? 0.3796 0.3382 0.2809 -0.0198 0.0025  -0.0036 171 ILE A CB  
1361 C CG1 . ILE A 182 ? 0.3915 0.3539 0.2901 -0.0201 0.0004  -0.0033 171 ILE A CG1 
1362 C CG2 . ILE A 182 ? 0.3774 0.3352 0.2788 -0.0186 0.0037  -0.0043 171 ILE A CG2 
1363 C CD1 . ILE A 182 ? 0.4164 0.3779 0.3113 -0.0214 -0.0004 -0.0057 171 ILE A CD1 
1364 N N   . ALA A 183 ? 0.3722 0.3304 0.2857 -0.0164 0.0039  0.0027  172 ALA A N   
1365 C CA  . ALA A 183 ? 0.3760 0.3322 0.2965 -0.0154 0.0054  0.0043  172 ALA A CA  
1366 C C   . ALA A 183 ? 0.3867 0.3431 0.3099 -0.0142 0.0062  0.0038  172 ALA A C   
1367 O O   . ALA A 183 ? 0.3889 0.3475 0.3083 -0.0141 0.0047  0.0030  172 ALA A O   
1368 C CB  . ALA A 183 ? 0.3670 0.3252 0.2909 -0.0147 0.0034  0.0090  172 ALA A CB  
1369 N N   . ASP A 184 ? 0.3959 0.3498 0.3266 -0.0131 0.0089  0.0046  173 ASP A N   
1370 C CA  . ASP A 184 ? 0.4156 0.3698 0.3523 -0.0117 0.0104  0.0053  173 ASP A CA  
1371 C C   . ASP A 184 ? 0.4474 0.3995 0.3802 -0.0118 0.0142  0.0015  173 ASP A C   
1372 O O   . ASP A 184 ? 0.4542 0.4089 0.3839 -0.0119 0.0127  0.0012  173 ASP A O   
1373 C CB  . ASP A 184 ? 0.4190 0.3779 0.3576 -0.0112 0.0058  0.0086  173 ASP A CB  
1374 C CG  . ASP A 184 ? 0.4718 0.4316 0.4217 -0.0097 0.0059  0.0117  173 ASP A CG  
1375 O OD1 . ASP A 184 ? 0.4871 0.4443 0.4434 -0.0087 0.0109  0.0110  173 ASP A OD1 
1376 O OD2 . ASP A 184 ? 0.4953 0.4583 0.4478 -0.0095 0.0009  0.0150  173 ASP A OD2 
1377 N N   . MET A 185 ? 0.4639 0.4108 0.3969 -0.0116 0.0191  -0.0012 174 MET A N   
1378 C CA  . MET A 185 ? 0.4957 0.4397 0.4243 -0.0115 0.0236  -0.0045 174 MET A CA  
1379 C C   . MET A 185 ? 0.5142 0.4581 0.4531 -0.0092 0.0279  -0.0025 174 MET A C   
1380 O O   . MET A 185 ? 0.5178 0.4583 0.4542 -0.0087 0.0334  -0.0049 174 MET A O   
1381 C CB  . MET A 185 ? 0.5165 0.4536 0.4381 -0.0126 0.0271  -0.0091 174 MET A CB  
1382 C CG  . MET A 185 ? 0.5583 0.4949 0.4714 -0.0151 0.0232  -0.0111 174 MET A CG  
1383 S SD  . MET A 185 ? 0.6035 0.5453 0.5089 -0.0164 0.0184  -0.0106 174 MET A SD  
1384 C CE  . MET A 185 ? 0.6154 0.5619 0.5248 -0.0168 0.0135  -0.0073 174 MET A CE  
1385 N N   . GLY A 186 ? 0.5209 0.4683 0.4712 -0.0080 0.0257  0.0020  175 GLY A N   
1386 C CA  . GLY A 186 ? 0.5406 0.4883 0.5036 -0.0058 0.0295  0.0045  175 GLY A CA  
1387 C C   . GLY A 186 ? 0.5659 0.5178 0.5334 -0.0053 0.0288  0.0069  175 GLY A C   
1388 O O   . GLY A 186 ? 0.5660 0.5193 0.5468 -0.0035 0.0310  0.0102  175 GLY A O   
1389 N N   . PHE A 187 ? 0.5867 0.5407 0.5449 -0.0067 0.0256  0.0056  176 PHE A N   
1390 C CA  . PHE A 187 ? 0.6120 0.5697 0.5750 -0.0064 0.0248  0.0078  176 PHE A CA  
1391 C C   . PHE A 187 ? 0.6442 0.5989 0.6061 -0.0055 0.0329  0.0060  176 PHE A C   
1392 O O   . PHE A 187 ? 0.6436 0.5972 0.5949 -0.0065 0.0338  0.0037  176 PHE A O   
1393 C CB  . PHE A 187 ? 0.6138 0.5744 0.5682 -0.0081 0.0187  0.0072  176 PHE A CB  
1394 C CG  . PHE A 187 ? 0.6229 0.5879 0.5857 -0.0079 0.0148  0.0105  176 PHE A CG  
1395 C CD1 . PHE A 187 ? 0.6353 0.6031 0.6046 -0.0080 0.0084  0.0136  176 PHE A CD1 
1396 C CD2 . PHE A 187 ? 0.6358 0.6017 0.5998 -0.0079 0.0171  0.0108  176 PHE A CD2 
1397 C CE1 . PHE A 187 ? 0.6441 0.6151 0.6209 -0.0082 0.0039  0.0163  176 PHE A CE1 
1398 C CE2 . PHE A 187 ? 0.6431 0.6126 0.6159 -0.0080 0.0130  0.0139  176 PHE A CE2 
1399 C CZ  . PHE A 187 ? 0.6393 0.6112 0.6186 -0.0082 0.0062  0.0164  176 PHE A CZ  
1400 N N   . ALA A 188 ? 0.6697 0.6225 0.6423 -0.0034 0.0391  0.0073  177 ALA A N   
1401 C CA  . ALA A 188 ? 0.7051 0.6544 0.6764 -0.0022 0.0481  0.0058  177 ALA A CA  
1402 C C   . ALA A 188 ? 0.7335 0.6873 0.7143 -0.0015 0.0488  0.0098  177 ALA A C   
1403 O O   . ALA A 188 ? 0.7296 0.6883 0.7247 -0.0010 0.0444  0.0144  177 ALA A O   
1404 C CB  . ALA A 188 ? 0.7062 0.6510 0.6853 0.0000  0.0554  0.0052  177 ALA A CB  
1405 N N   . ARG A 189 ? 0.7529 0.7052 0.7256 -0.0017 0.0536  0.0084  178 ARG A N   
1406 C CA  . ARG A 189 ? 0.7708 0.7271 0.7520 -0.0012 0.0550  0.0124  178 ARG A CA  
1407 C C   . ARG A 189 ? 0.7840 0.7368 0.7646 0.0006  0.0663  0.0122  178 ARG A C   
1408 O O   . ARG A 189 ? 0.7945 0.7411 0.7679 0.0016  0.0732  0.0085  178 ARG A O   
1409 C CB  . ARG A 189 ? 0.8018 0.7609 0.7741 -0.0035 0.0483  0.0123  178 ARG A CB  
1410 C CG  . ARG A 189 ? 0.8622 0.8242 0.8333 -0.0051 0.0380  0.0120  178 ARG A CG  
1411 C CD  . ARG A 189 ? 0.9115 0.8779 0.8992 -0.0045 0.0330  0.0164  178 ARG A CD  
1412 N NE  . ARG A 189 ? 0.9550 0.9254 0.9542 -0.0044 0.0324  0.0204  178 ARG A NE  
1413 C CZ  . ARG A 189 ? 0.9804 0.9546 0.9962 -0.0040 0.0283  0.0248  178 ARG A CZ  
1414 N NH1 . ARG A 189 ? 0.9662 0.9437 0.9928 -0.0042 0.0277  0.0284  178 ARG A NH1 
1415 N NH2 . ARG A 189 ? 0.9817 0.9564 1.0038 -0.0037 0.0245  0.0261  178 ARG A NH2 
1416 N N   . THR A 207 ? 0.5874 0.5586 0.5403 -0.0164 -0.0535 0.0163  196 THR A N   
1417 C CA  . THR A 207 ? 0.5921 0.5612 0.5382 -0.0169 -0.0545 0.0117  196 THR A CA  
1418 C C   . THR A 207 ? 0.5783 0.5489 0.5263 -0.0160 -0.0465 0.0100  196 THR A C   
1419 O O   . THR A 207 ? 0.5791 0.5512 0.5277 -0.0150 -0.0400 0.0108  196 THR A O   
1420 C CB  . THR A 207 ? 0.6213 0.5869 0.5497 -0.0170 -0.0570 0.0080  196 THR A CB  
1421 O OG1 . THR A 207 ? 0.6424 0.6084 0.5625 -0.0158 -0.0499 0.0066  196 THR A OG1 
1422 C CG2 . THR A 207 ? 0.6301 0.5937 0.5536 -0.0180 -0.0645 0.0101  196 THR A CG2 
1423 N N   . PHE A 208 ? 0.5602 0.5300 0.5083 -0.0164 -0.0473 0.0074  197 PHE A N   
1424 C CA  . PHE A 208 ? 0.5453 0.5163 0.4947 -0.0158 -0.0408 0.0063  197 PHE A CA  
1425 C C   . PHE A 208 ? 0.5033 0.4723 0.4403 -0.0155 -0.0394 0.0018  197 PHE A C   
1426 O O   . PHE A 208 ? 0.4950 0.4646 0.4331 -0.0153 -0.0359 0.0009  197 PHE A O   
1427 C CB  . PHE A 208 ? 0.5583 0.5307 0.5211 -0.0164 -0.0415 0.0083  197 PHE A CB  
1428 C CG  . PHE A 208 ? 0.5814 0.5559 0.5588 -0.0166 -0.0431 0.0131  197 PHE A CG  
1429 C CD1 . PHE A 208 ? 0.5949 0.5719 0.5797 -0.0156 -0.0363 0.0162  197 PHE A CD1 
1430 C CD2 . PHE A 208 ? 0.5977 0.5716 0.5816 -0.0180 -0.0516 0.0145  197 PHE A CD2 
1431 C CE1 . PHE A 208 ? 0.6011 0.5803 0.6010 -0.0155 -0.0371 0.0209  197 PHE A CE1 
1432 C CE2 . PHE A 208 ? 0.6008 0.5773 0.6003 -0.0183 -0.0534 0.0196  197 PHE A CE2 
1433 C CZ  . PHE A 208 ? 0.5935 0.5729 0.6016 -0.0168 -0.0458 0.0229  197 PHE A CZ  
1434 N N   . TRP A 209 ? 0.4739 0.4406 0.3992 -0.0153 -0.0416 -0.0005 198 TRP A N   
1435 C CA  . TRP A 209 ? 0.4545 0.4192 0.3690 -0.0147 -0.0400 -0.0045 198 TRP A CA  
1436 C C   . TRP A 209 ? 0.4350 0.4017 0.3482 -0.0140 -0.0334 -0.0049 198 TRP A C   
1437 O O   . TRP A 209 ? 0.4364 0.4022 0.3452 -0.0136 -0.0320 -0.0076 198 TRP A O   
1438 C CB  . TRP A 209 ? 0.4559 0.4182 0.3582 -0.0144 -0.0418 -0.0060 198 TRP A CB  
1439 C CG  . TRP A 209 ? 0.4707 0.4305 0.3714 -0.0153 -0.0491 -0.0055 198 TRP A CG  
1440 C CD1 . TRP A 209 ? 0.4811 0.4399 0.3894 -0.0165 -0.0553 -0.0051 198 TRP A CD1 
1441 C CD2 . TRP A 209 ? 0.4747 0.4323 0.3644 -0.0153 -0.0517 -0.0053 198 TRP A CD2 
1442 N NE1 . TRP A 209 ? 0.4919 0.4480 0.3949 -0.0175 -0.0621 -0.0046 198 TRP A NE1 
1443 C CE2 . TRP A 209 ? 0.4905 0.4456 0.3811 -0.0167 -0.0600 -0.0048 198 TRP A CE2 
1444 C CE3 . TRP A 209 ? 0.4858 0.4433 0.3655 -0.0144 -0.0479 -0.0051 198 TRP A CE3 
1445 C CZ2 . TRP A 209 ? 0.5012 0.4535 0.3816 -0.0172 -0.0648 -0.0039 198 TRP A CZ2 
1446 C CZ3 . TRP A 209 ? 0.5015 0.4564 0.3713 -0.0147 -0.0519 -0.0042 198 TRP A CZ3 
1447 C CH2 . TRP A 209 ? 0.5020 0.4541 0.3712 -0.0161 -0.0603 -0.0037 198 TRP A CH2 
1448 N N   . TYR A 210 ? 0.4152 0.3841 0.3322 -0.0139 -0.0294 -0.0024 199 TYR A N   
1449 C CA  . TYR A 210 ? 0.4067 0.3767 0.3215 -0.0136 -0.0239 -0.0027 199 TYR A CA  
1450 C C   . TYR A 210 ? 0.4136 0.3850 0.3357 -0.0139 -0.0209 -0.0011 199 TYR A C   
1451 O O   . TYR A 210 ? 0.4166 0.3884 0.3362 -0.0140 -0.0169 -0.0013 199 TYR A O   
1452 C CB  . TYR A 210 ? 0.3945 0.3648 0.3051 -0.0134 -0.0211 -0.0019 199 TYR A CB  
1453 C CG  . TYR A 210 ? 0.3919 0.3610 0.2951 -0.0130 -0.0236 -0.0027 199 TYR A CG  
1454 C CD1 . TYR A 210 ? 0.4039 0.3724 0.2994 -0.0126 -0.0222 -0.0050 199 TYR A CD1 
1455 C CD2 . TYR A 210 ? 0.3940 0.3622 0.2978 -0.0132 -0.0276 -0.0010 199 TYR A CD2 
1456 C CE1 . TYR A 210 ? 0.4188 0.3857 0.3064 -0.0121 -0.0238 -0.0058 199 TYR A CE1 
1457 C CE2 . TYR A 210 ? 0.4088 0.3753 0.3037 -0.0130 -0.0302 -0.0017 199 TYR A CE2 
1458 C CZ  . TYR A 210 ? 0.4308 0.3964 0.3170 -0.0123 -0.0278 -0.0042 199 TYR A CZ  
1459 O OH  . TYR A 210 ? 0.4611 0.4246 0.3375 -0.0119 -0.0292 -0.0047 199 TYR A OH  
1460 N N   . ARG A 211 ? 0.4169 0.3887 0.3478 -0.0142 -0.0231 0.0007  200 ARG A N   
1461 C CA  . ARG A 211 ? 0.4282 0.4013 0.3666 -0.0144 -0.0198 0.0029  200 ARG A CA  
1462 C C   . ARG A 211 ? 0.4134 0.3864 0.3517 -0.0148 -0.0199 0.0021  200 ARG A C   
1463 O O   . ARG A 211 ? 0.4125 0.3846 0.3528 -0.0150 -0.0243 0.0010  200 ARG A O   
1464 C CB  . ARG A 211 ? 0.4655 0.4396 0.4156 -0.0145 -0.0214 0.0061  200 ARG A CB  
1465 C CG  . ARG A 211 ? 0.5637 0.5382 0.5158 -0.0140 -0.0210 0.0077  200 ARG A CG  
1466 C CD  . ARG A 211 ? 0.6511 0.6251 0.5978 -0.0134 -0.0146 0.0072  200 ARG A CD  
1467 N NE  . ARG A 211 ? 0.7246 0.6988 0.6765 -0.0127 -0.0131 0.0093  200 ARG A NE  
1468 C CZ  . ARG A 211 ? 0.7833 0.7570 0.7379 -0.0120 -0.0068 0.0102  200 ARG A CZ  
1469 N NH1 . ARG A 211 ? 0.7932 0.7661 0.7442 -0.0120 -0.0018 0.0091  200 ARG A NH1 
1470 N NH2 . ARG A 211 ? 0.7848 0.7584 0.7454 -0.0112 -0.0055 0.0121  200 ARG A NH2 
1471 N N   . ALA A 212 ? 0.3983 0.3717 0.3337 -0.0149 -0.0154 0.0027  201 ALA A N   
1472 C CA  . ALA A 212 ? 0.3880 0.3616 0.3236 -0.0153 -0.0151 0.0030  201 ALA A CA  
1473 C C   . ALA A 212 ? 0.3831 0.3573 0.3293 -0.0156 -0.0168 0.0053  201 ALA A C   
1474 O O   . ALA A 212 ? 0.3862 0.3612 0.3399 -0.0155 -0.0162 0.0076  201 ALA A O   
1475 C CB  . ALA A 212 ? 0.3780 0.3518 0.3090 -0.0156 -0.0101 0.0041  201 ALA A CB  
1476 N N   . PRO A 213 ? 0.3758 0.3496 0.3244 -0.0159 -0.0192 0.0051  202 PRO A N   
1477 C CA  . PRO A 213 ? 0.3804 0.3546 0.3405 -0.0165 -0.0213 0.0075  202 PRO A CA  
1478 C C   . PRO A 213 ? 0.3904 0.3664 0.3571 -0.0166 -0.0165 0.0122  202 PRO A C   
1479 O O   . PRO A 213 ? 0.3993 0.3762 0.3774 -0.0169 -0.0176 0.0149  202 PRO A O   
1480 C CB  . PRO A 213 ? 0.3835 0.3563 0.3436 -0.0166 -0.0242 0.0060  202 PRO A CB  
1481 C CG  . PRO A 213 ? 0.3875 0.3606 0.3379 -0.0163 -0.0214 0.0048  202 PRO A CG  
1482 C CD  . PRO A 213 ? 0.3686 0.3415 0.3112 -0.0158 -0.0202 0.0028  202 PRO A CD  
1483 N N   . GLU A 214 ? 0.3867 0.3630 0.3463 -0.0165 -0.0112 0.0133  203 GLU A N   
1484 C CA  . GLU A 214 ? 0.3909 0.3683 0.3546 -0.0165 -0.0055 0.0176  203 GLU A CA  
1485 C C   . GLU A 214 ? 0.4087 0.3868 0.3788 -0.0158 -0.0031 0.0187  203 GLU A C   
1486 O O   . GLU A 214 ? 0.4149 0.3944 0.3958 -0.0157 -0.0007 0.0226  203 GLU A O   
1487 C CB  . GLU A 214 ? 0.3922 0.3686 0.3445 -0.0168 -0.0007 0.0180  203 GLU A CB  
1488 C CG  . GLU A 214 ? 0.4127 0.3877 0.3539 -0.0165 0.0011  0.0147  203 GLU A CG  
1489 C CD  . GLU A 214 ? 0.4343 0.4086 0.3677 -0.0169 -0.0029 0.0112  203 GLU A CD  
1490 O OE1 . GLU A 214 ? 0.4255 0.4003 0.3628 -0.0168 -0.0076 0.0101  203 GLU A OE1 
1491 O OE2 . GLU A 214 ? 0.4226 0.3956 0.3464 -0.0172 -0.0012 0.0095  203 GLU A OE2 
1492 N N   . LEU A 215 ? 0.4124 0.3898 0.3780 -0.0153 -0.0044 0.0158  204 LEU A N   
1493 C CA  . LEU A 215 ? 0.4277 0.4058 0.4008 -0.0146 -0.0031 0.0172  204 LEU A CA  
1494 C C   . LEU A 215 ? 0.4457 0.4253 0.4329 -0.0151 -0.0084 0.0193  204 LEU A C   
1495 O O   . LEU A 215 ? 0.4538 0.4351 0.4531 -0.0147 -0.0062 0.0230  204 LEU A O   
1496 C CB  . LEU A 215 ? 0.4314 0.4084 0.3972 -0.0142 -0.0046 0.0140  204 LEU A CB  
1497 C CG  . LEU A 215 ? 0.4456 0.4208 0.4002 -0.0138 0.0006  0.0121  204 LEU A CG  
1498 C CD1 . LEU A 215 ? 0.4472 0.4216 0.3960 -0.0136 -0.0021 0.0094  204 LEU A CD1 
1499 C CD2 . LEU A 215 ? 0.4506 0.4254 0.4091 -0.0129 0.0080  0.0145  204 LEU A CD2 
1500 N N   . LEU A 216 ? 0.4429 0.4216 0.4289 -0.0159 -0.0155 0.0169  205 LEU A N   
1501 C CA  . LEU A 216 ? 0.4461 0.4252 0.4443 -0.0168 -0.0218 0.0182  205 LEU A CA  
1502 C C   . LEU A 216 ? 0.4501 0.4307 0.4610 -0.0174 -0.0206 0.0224  205 LEU A C   
1503 O O   . LEU A 216 ? 0.4509 0.4322 0.4751 -0.0182 -0.0252 0.0245  205 LEU A O   
1504 C CB  . LEU A 216 ? 0.4493 0.4257 0.4407 -0.0174 -0.0292 0.0137  205 LEU A CB  
1505 C CG  . LEU A 216 ? 0.4636 0.4386 0.4425 -0.0169 -0.0302 0.0101  205 LEU A CG  
1506 C CD1 . LEU A 216 ? 0.4674 0.4394 0.4376 -0.0171 -0.0351 0.0055  205 LEU A CD1 
1507 C CD2 . LEU A 216 ? 0.4707 0.4464 0.4545 -0.0169 -0.0326 0.0117  205 LEU A CD2 
1508 N N   . LEU A 217 ? 0.4482 0.4291 0.4553 -0.0171 -0.0148 0.0239  206 LEU A N   
1509 C CA  . LEU A 217 ? 0.4481 0.4306 0.4661 -0.0176 -0.0124 0.0286  206 LEU A CA  
1510 C C   . LEU A 217 ? 0.4597 0.4441 0.4821 -0.0166 -0.0034 0.0332  206 LEU A C   
1511 O O   . LEU A 217 ? 0.4641 0.4497 0.4922 -0.0168 0.0007  0.0375  206 LEU A O   
1512 C CB  . LEU A 217 ? 0.4480 0.4292 0.4592 -0.0181 -0.0127 0.0278  206 LEU A CB  
1513 C CG  . LEU A 217 ? 0.4593 0.4383 0.4692 -0.0188 -0.0205 0.0237  206 LEU A CG  
1514 C CD1 . LEU A 217 ? 0.4669 0.4448 0.4703 -0.0189 -0.0198 0.0233  206 LEU A CD1 
1515 C CD2 . LEU A 217 ? 0.4557 0.4345 0.4811 -0.0199 -0.0265 0.0251  206 LEU A CD2 
1516 N N   . GLY A 218 ? 0.4672 0.4518 0.4872 -0.0155 0.0001  0.0325  207 GLY A N   
1517 C CA  . GLY A 218 ? 0.4745 0.4602 0.4990 -0.0143 0.0092  0.0363  207 GLY A CA  
1518 C C   . GLY A 218 ? 0.4962 0.4798 0.5055 -0.0134 0.0173  0.0352  207 GLY A C   
1519 O O   . GLY A 218 ? 0.4996 0.4834 0.5118 -0.0124 0.0257  0.0385  207 GLY A O   
1520 N N   . ALA A 219 ? 0.5104 0.4915 0.5032 -0.0138 0.0152  0.0305  208 ALA A N   
1521 C CA  . ALA A 219 ? 0.5359 0.5143 0.5133 -0.0135 0.0216  0.0290  208 ALA A CA  
1522 C C   . ALA A 219 ? 0.5541 0.5314 0.5326 -0.0119 0.0285  0.0289  208 ALA A C   
1523 O O   . ALA A 219 ? 0.5446 0.5227 0.5298 -0.0113 0.0258  0.0277  208 ALA A O   
1524 C CB  . ALA A 219 ? 0.5439 0.5203 0.5068 -0.0143 0.0171  0.0241  208 ALA A CB  
1525 N N   . ARG A 220 ? 0.5789 0.5544 0.5527 -0.0111 0.0374  0.0307  209 ARG A N   
1526 C CA  . ARG A 220 ? 0.6058 0.5796 0.5817 -0.0093 0.0457  0.0308  209 ARG A CA  
1527 C C   . ARG A 220 ? 0.6241 0.5934 0.5850 -0.0090 0.0475  0.0255  209 ARG A C   
1528 O O   . ARG A 220 ? 0.6341 0.6014 0.5972 -0.0073 0.0541  0.0250  209 ARG A O   
1529 C CB  . ARG A 220 ? 0.6405 0.6135 0.6170 -0.0084 0.0556  0.0350  209 ARG A CB  
1530 C CG  . ARG A 220 ? 0.7060 0.6828 0.6941 -0.0091 0.0544  0.0407  209 ARG A CG  
1531 C CD  . ARG A 220 ? 0.7612 0.7424 0.7732 -0.0082 0.0540  0.0451  209 ARG A CD  
1532 N NE  . ARG A 220 ? 0.8025 0.7865 0.8261 -0.0085 0.0568  0.0515  209 ARG A NE  
1533 C CZ  . ARG A 220 ? 0.8268 0.8152 0.8725 -0.0086 0.0541  0.0562  209 ARG A CZ  
1534 N NH1 . ARG A 220 ? 0.8189 0.8092 0.8767 -0.0086 0.0479  0.0551  209 ARG A NH1 
1535 N NH2 . ARG A 220 ? 0.8274 0.8181 0.8835 -0.0090 0.0570  0.0622  209 ARG A NH2 
1536 N N   . HIS A 221 ? 0.6228 0.5904 0.5693 -0.0106 0.0424  0.0218  210 HIS A N   
1537 C CA  . HIS A 221 ? 0.6268 0.5900 0.5598 -0.0107 0.0436  0.0169  210 HIS A CA  
1538 C C   . HIS A 221 ? 0.6051 0.5689 0.5329 -0.0120 0.0350  0.0136  210 HIS A C   
1539 O O   . HIS A 221 ? 0.6047 0.5710 0.5333 -0.0131 0.0289  0.0143  210 HIS A O   
1540 C CB  . HIS A 221 ? 0.6564 0.6147 0.5726 -0.0113 0.0493  0.0158  210 HIS A CB  
1541 C CG  . HIS A 221 ? 0.7029 0.6602 0.6217 -0.0100 0.0586  0.0194  210 HIS A CG  
1542 N ND1 . HIS A 221 ? 0.7290 0.6852 0.6562 -0.0077 0.0663  0.0199  210 HIS A ND1 
1543 C CD2 . HIS A 221 ? 0.7238 0.6812 0.6386 -0.0105 0.0614  0.0230  210 HIS A CD2 
1544 C CE1 . HIS A 221 ? 0.7359 0.6915 0.6637 -0.0068 0.0743  0.0237  210 HIS A CE1 
1545 N NE2 . HIS A 221 ? 0.7392 0.6956 0.6592 -0.0086 0.0716  0.0258  210 HIS A NE2 
1546 N N   . TYR A 222 ? 0.5832 0.5444 0.5061 -0.0118 0.0351  0.0100  211 TYR A N   
1547 C CA  . TYR A 222 ? 0.5660 0.5275 0.4830 -0.0130 0.0283  0.0070  211 TYR A CA  
1548 C C   . TYR A 222 ? 0.5375 0.4958 0.4392 -0.0147 0.0282  0.0049  211 TYR A C   
1549 O O   . TYR A 222 ? 0.5356 0.4897 0.4286 -0.0148 0.0338  0.0041  211 TYR A O   
1550 C CB  . TYR A 222 ? 0.5750 0.5351 0.4939 -0.0123 0.0284  0.0047  211 TYR A CB  
1551 C CG  . TYR A 222 ? 0.5946 0.5583 0.5280 -0.0111 0.0257  0.0072  211 TYR A CG  
1552 C CD1 . TYR A 222 ? 0.6110 0.5776 0.5470 -0.0118 0.0182  0.0072  211 TYR A CD1 
1553 C CD2 . TYR A 222 ? 0.6127 0.5767 0.5575 -0.0095 0.0307  0.0097  211 TYR A CD2 
1554 C CE1 . TYR A 222 ? 0.6267 0.5960 0.5745 -0.0111 0.0148  0.0094  211 TYR A CE1 
1555 C CE2 . TYR A 222 ? 0.6271 0.5945 0.5860 -0.0087 0.0271  0.0125  211 TYR A CE2 
1556 C CZ  . TYR A 222 ? 0.6452 0.6150 0.6048 -0.0097 0.0188  0.0123  211 TYR A CZ  
1557 O OH  . TYR A 222 ? 0.6799 0.6525 0.6521 -0.0093 0.0145  0.0151  211 TYR A OH  
1558 N N   . THR A 223 ? 0.5121 0.4722 0.4104 -0.0160 0.0218  0.0041  212 THR A N   
1559 C CA  . THR A 223 ? 0.4963 0.4542 0.3822 -0.0179 0.0199  0.0028  212 THR A CA  
1560 C C   . THR A 223 ? 0.4738 0.4322 0.3572 -0.0188 0.0146  0.0001  212 THR A C   
1561 O O   . THR A 223 ? 0.4824 0.4430 0.3729 -0.0179 0.0123  -0.0004 212 THR A O   
1562 C CB  . THR A 223 ? 0.5080 0.4685 0.3952 -0.0186 0.0176  0.0060  212 THR A CB  
1563 O OG1 . THR A 223 ? 0.5198 0.4844 0.4162 -0.0182 0.0121  0.0065  212 THR A OG1 
1564 C CG2 . THR A 223 ? 0.4992 0.4597 0.3899 -0.0177 0.0230  0.0096  212 THR A CG2 
1565 N N   . LYS A 224 ? 0.4427 0.3992 0.3162 -0.0206 0.0123  -0.0012 213 LYS A N   
1566 C CA  . LYS A 224 ? 0.4239 0.3814 0.2965 -0.0216 0.0074  -0.0030 213 LYS A CA  
1567 C C   . LYS A 224 ? 0.4070 0.3694 0.2877 -0.0210 0.0031  -0.0014 213 LYS A C   
1568 O O   . LYS A 224 ? 0.4060 0.3701 0.2900 -0.0206 0.0006  -0.0025 213 LYS A O   
1569 C CB  . LYS A 224 ? 0.4452 0.4001 0.3073 -0.0240 0.0052  -0.0038 213 LYS A CB  
1570 C CG  . LYS A 224 ? 0.5027 0.4514 0.3551 -0.0248 0.0086  -0.0066 213 LYS A CG  
1571 C CD  . LYS A 224 ? 0.5623 0.5077 0.4032 -0.0276 0.0053  -0.0074 213 LYS A CD  
1572 C CE  . LYS A 224 ? 0.6207 0.5588 0.4511 -0.0284 0.0090  -0.0110 213 LYS A CE  
1573 N NZ  . LYS A 224 ? 0.6674 0.6010 0.4844 -0.0315 0.0055  -0.0120 213 LYS A NZ  
1574 N N   . ALA A 225 ? 0.3937 0.3578 0.2772 -0.0209 0.0025  0.0012  214 ALA A N   
1575 C CA  . ALA A 225 ? 0.3808 0.3484 0.2717 -0.0203 -0.0013 0.0024  214 ALA A CA  
1576 C C   . ALA A 225 ? 0.3671 0.3363 0.2658 -0.0187 -0.0018 0.0016  214 ALA A C   
1577 O O   . ALA A 225 ? 0.3635 0.3344 0.2652 -0.0182 -0.0052 0.0007  214 ALA A O   
1578 C CB  . ALA A 225 ? 0.3735 0.3420 0.2668 -0.0205 -0.0012 0.0056  214 ALA A CB  
1579 N N   . ILE A 226 ? 0.3569 0.3253 0.2584 -0.0179 0.0014  0.0019  215 ILE A N   
1580 C CA  . ILE A 226 ? 0.3578 0.3275 0.2667 -0.0166 0.0002  0.0017  215 ILE A CA  
1581 C C   . ILE A 226 ? 0.3574 0.3269 0.2633 -0.0165 -0.0016 -0.0005 215 ILE A C   
1582 O O   . ILE A 226 ? 0.3532 0.3240 0.2620 -0.0159 -0.0048 -0.0010 215 ILE A O   
1583 C CB  . ILE A 226 ? 0.3693 0.3383 0.2834 -0.0158 0.0044  0.0034  215 ILE A CB  
1584 C CG1 . ILE A 226 ? 0.3748 0.3452 0.2957 -0.0157 0.0049  0.0064  215 ILE A CG1 
1585 C CG2 . ILE A 226 ? 0.3827 0.3524 0.3032 -0.0148 0.0033  0.0033  215 ILE A CG2 
1586 C CD1 . ILE A 226 ? 0.3900 0.3597 0.3146 -0.0150 0.0106  0.0085  215 ILE A CD1 
1587 N N   . ASP A 227 ? 0.3474 0.3148 0.2469 -0.0173 0.0003  -0.0019 216 ASP A N   
1588 C CA  . ASP A 227 ? 0.3541 0.3214 0.2514 -0.0174 -0.0010 -0.0035 216 ASP A CA  
1589 C C   . ASP A 227 ? 0.3563 0.3255 0.2524 -0.0177 -0.0043 -0.0040 216 ASP A C   
1590 O O   . ASP A 227 ? 0.3614 0.3316 0.2584 -0.0170 -0.0058 -0.0045 216 ASP A O   
1591 C CB  . ASP A 227 ? 0.3618 0.3260 0.2534 -0.0184 0.0014  -0.0049 216 ASP A CB  
1592 C CG  . ASP A 227 ? 0.3792 0.3407 0.2721 -0.0177 0.0055  -0.0052 216 ASP A CG  
1593 O OD1 . ASP A 227 ? 0.3792 0.3420 0.2792 -0.0163 0.0061  -0.0037 216 ASP A OD1 
1594 O OD2 . ASP A 227 ? 0.3689 0.3267 0.2562 -0.0187 0.0079  -0.0069 216 ASP A OD2 
1595 N N   . ILE A 228 ? 0.3504 0.3199 0.2444 -0.0186 -0.0052 -0.0035 217 ILE A N   
1596 C CA  . ILE A 228 ? 0.3487 0.3201 0.2434 -0.0188 -0.0080 -0.0035 217 ILE A CA  
1597 C C   . ILE A 228 ? 0.3520 0.3248 0.2513 -0.0173 -0.0097 -0.0038 217 ILE A C   
1598 O O   . ILE A 228 ? 0.3653 0.3390 0.2648 -0.0167 -0.0107 -0.0048 217 ILE A O   
1599 C CB  . ILE A 228 ? 0.3490 0.3204 0.2417 -0.0201 -0.0091 -0.0022 217 ILE A CB  
1600 C CG1 . ILE A 228 ? 0.3654 0.3345 0.2514 -0.0220 -0.0084 -0.0026 217 ILE A CG1 
1601 C CG2 . ILE A 228 ? 0.3434 0.3171 0.2397 -0.0199 -0.0117 -0.0018 217 ILE A CG2 
1602 C CD1 . ILE A 228 ? 0.3853 0.3543 0.2706 -0.0225 -0.0091 -0.0040 217 ILE A CD1 
1603 N N   . TRP A 229 ? 0.3423 0.3151 0.2455 -0.0168 -0.0099 -0.0029 218 TRP A N   
1604 C CA  . TRP A 229 ? 0.3433 0.3165 0.2506 -0.0157 -0.0123 -0.0036 218 TRP A CA  
1605 C C   . TRP A 229 ? 0.3479 0.3206 0.2532 -0.0149 -0.0128 -0.0050 218 TRP A C   
1606 O O   . TRP A 229 ? 0.3530 0.3254 0.2573 -0.0141 -0.0145 -0.0065 218 TRP A O   
1607 C CB  . TRP A 229 ? 0.3438 0.3168 0.2568 -0.0156 -0.0126 -0.0021 218 TRP A CB  
1608 C CG  . TRP A 229 ? 0.3545 0.3271 0.2717 -0.0149 -0.0160 -0.0031 218 TRP A CG  
1609 C CD1 . TRP A 229 ? 0.3663 0.3382 0.2843 -0.0144 -0.0180 -0.0038 218 TRP A CD1 
1610 C CD2 . TRP A 229 ? 0.3604 0.3326 0.2811 -0.0147 -0.0184 -0.0036 218 TRP A CD2 
1611 N NE1 . TRP A 229 ? 0.3680 0.3387 0.2885 -0.0142 -0.0217 -0.0052 218 TRP A NE1 
1612 C CE2 . TRP A 229 ? 0.3677 0.3384 0.2904 -0.0142 -0.0217 -0.0053 218 TRP A CE2 
1613 C CE3 . TRP A 229 ? 0.3654 0.3381 0.2880 -0.0150 -0.0183 -0.0027 218 TRP A CE3 
1614 C CZ2 . TRP A 229 ? 0.3754 0.3445 0.3017 -0.0140 -0.0247 -0.0067 218 TRP A CZ2 
1615 C CZ3 . TRP A 229 ? 0.3731 0.3447 0.3003 -0.0145 -0.0209 -0.0037 218 TRP A CZ3 
1616 C CH2 . TRP A 229 ? 0.3745 0.3441 0.3034 -0.0140 -0.0239 -0.0060 218 TRP A CH2 
1617 N N   . ALA A 230 ? 0.3529 0.3251 0.2575 -0.0150 -0.0111 -0.0044 219 ALA A N   
1618 C CA  . ALA A 230 ? 0.3542 0.3260 0.2573 -0.0144 -0.0118 -0.0047 219 ALA A CA  
1619 C C   . ALA A 230 ? 0.3560 0.3281 0.2543 -0.0143 -0.0113 -0.0058 219 ALA A C   
1620 O O   . ALA A 230 ? 0.3637 0.3355 0.2596 -0.0135 -0.0125 -0.0064 219 ALA A O   
1621 C CB  . ALA A 230 ? 0.3500 0.3212 0.2548 -0.0146 -0.0097 -0.0034 219 ALA A CB  
1622 N N   . ILE A 231 ? 0.3520 0.3246 0.2490 -0.0152 -0.0097 -0.0058 220 ILE A N   
1623 C CA  . ILE A 231 ? 0.3603 0.3338 0.2552 -0.0152 -0.0090 -0.0062 220 ILE A CA  
1624 C C   . ILE A 231 ? 0.3778 0.3520 0.2731 -0.0141 -0.0100 -0.0072 220 ILE A C   
1625 O O   . ILE A 231 ? 0.3830 0.3574 0.2763 -0.0132 -0.0091 -0.0077 220 ILE A O   
1626 C CB  . ILE A 231 ? 0.3576 0.3312 0.2522 -0.0168 -0.0082 -0.0057 220 ILE A CB  
1627 C CG1 . ILE A 231 ? 0.3558 0.3276 0.2490 -0.0177 -0.0067 -0.0056 220 ILE A CG1 
1628 C CG2 . ILE A 231 ? 0.3623 0.3375 0.2575 -0.0169 -0.0080 -0.0056 220 ILE A CG2 
1629 C CD1 . ILE A 231 ? 0.3577 0.3282 0.2489 -0.0194 -0.0064 -0.0058 220 ILE A CD1 
1630 N N   . GLY A 232 ? 0.3792 0.3533 0.2772 -0.0141 -0.0114 -0.0075 221 GLY A N   
1631 C CA  . GLY A 232 ? 0.3848 0.3588 0.2841 -0.0129 -0.0123 -0.0089 221 GLY A CA  
1632 C C   . GLY A 232 ? 0.3906 0.3627 0.2867 -0.0117 -0.0133 -0.0106 221 GLY A C   
1633 O O   . GLY A 232 ? 0.3995 0.3708 0.2930 -0.0104 -0.0125 -0.0123 221 GLY A O   
1634 N N   . CYS A 233 ? 0.3831 0.3542 0.2790 -0.0120 -0.0151 -0.0101 222 CYS A N   
1635 C CA  . CYS A 233 ? 0.3847 0.3536 0.2767 -0.0113 -0.0172 -0.0115 222 CYS A CA  
1636 C C   . CYS A 233 ? 0.3891 0.3578 0.2748 -0.0107 -0.0153 -0.0114 222 CYS A C   
1637 O O   . CYS A 233 ? 0.3941 0.3607 0.2740 -0.0097 -0.0158 -0.0131 222 CYS A O   
1638 C CB  . CYS A 233 ? 0.3787 0.3472 0.2738 -0.0120 -0.0199 -0.0100 222 CYS A CB  
1639 S SG  . CYS A 233 ? 0.3856 0.3544 0.2893 -0.0127 -0.0216 -0.0092 222 CYS A SG  
1640 N N   . ILE A 234 ? 0.3849 0.3555 0.2715 -0.0114 -0.0131 -0.0093 223 ILE A N   
1641 C CA  . ILE A 234 ? 0.3820 0.3527 0.2641 -0.0110 -0.0110 -0.0084 223 ILE A CA  
1642 C C   . ILE A 234 ? 0.3841 0.3554 0.2644 -0.0100 -0.0082 -0.0094 223 ILE A C   
1643 O O   . ILE A 234 ? 0.3870 0.3571 0.2614 -0.0089 -0.0070 -0.0098 223 ILE A O   
1644 C CB  . ILE A 234 ? 0.3789 0.3509 0.2639 -0.0121 -0.0095 -0.0061 223 ILE A CB  
1645 C CG1 . ILE A 234 ? 0.3833 0.3545 0.2707 -0.0126 -0.0113 -0.0048 223 ILE A CG1 
1646 C CG2 . ILE A 234 ? 0.3784 0.3510 0.2609 -0.0119 -0.0070 -0.0046 223 ILE A CG2 
1647 C CD1 . ILE A 234 ? 0.3741 0.3456 0.2654 -0.0136 -0.0092 -0.0035 223 ILE A CD1 
1648 N N   . PHE A 235 ? 0.3749 0.3479 0.2602 -0.0103 -0.0072 -0.0096 224 PHE A N   
1649 C CA  . PHE A 235 ? 0.3762 0.3502 0.2629 -0.0093 -0.0045 -0.0101 224 PHE A CA  
1650 C C   . PHE A 235 ? 0.3925 0.3639 0.2748 -0.0074 -0.0041 -0.0129 224 PHE A C   
1651 O O   . PHE A 235 ? 0.4067 0.3775 0.2848 -0.0060 -0.0009 -0.0132 224 PHE A O   
1652 C CB  . PHE A 235 ? 0.3636 0.3397 0.2573 -0.0102 -0.0050 -0.0094 224 PHE A CB  
1653 C CG  . PHE A 235 ? 0.3596 0.3374 0.2576 -0.0093 -0.0024 -0.0091 224 PHE A CG  
1654 C CD1 . PHE A 235 ? 0.3672 0.3458 0.2639 -0.0082 0.0013  -0.0084 224 PHE A CD1 
1655 C CD2 . PHE A 235 ? 0.3537 0.3328 0.2582 -0.0095 -0.0035 -0.0088 224 PHE A CD2 
1656 C CE1 . PHE A 235 ? 0.3667 0.3474 0.2694 -0.0072 0.0042  -0.0077 224 PHE A CE1 
1657 C CE2 . PHE A 235 ? 0.3554 0.3364 0.2659 -0.0085 -0.0012 -0.0080 224 PHE A CE2 
1658 C CZ  . PHE A 235 ? 0.3529 0.3348 0.2631 -0.0073 0.0029  -0.0075 224 PHE A CZ  
1659 N N   . ALA A 236 ? 0.3953 0.3646 0.2779 -0.0073 -0.0072 -0.0149 225 ALA A N   
1660 C CA  . ALA A 236 ? 0.4005 0.3659 0.2783 -0.0058 -0.0077 -0.0184 225 ALA A CA  
1661 C C   . ALA A 236 ? 0.4170 0.3797 0.2843 -0.0052 -0.0076 -0.0191 225 ALA A C   
1662 O O   . ALA A 236 ? 0.4360 0.3960 0.2966 -0.0035 -0.0050 -0.0214 225 ALA A O   
1663 C CB  . ALA A 236 ? 0.3979 0.3614 0.2789 -0.0065 -0.0121 -0.0198 225 ALA A CB  
1664 N N   . GLU A 237 ? 0.4052 0.3685 0.2709 -0.0065 -0.0101 -0.0169 226 GLU A N   
1665 C CA  . GLU A 237 ? 0.4136 0.3745 0.2697 -0.0063 -0.0109 -0.0165 226 GLU A CA  
1666 C C   . GLU A 237 ? 0.4197 0.3819 0.2717 -0.0053 -0.0055 -0.0148 226 GLU A C   
1667 O O   . GLU A 237 ? 0.4359 0.3952 0.2777 -0.0043 -0.0044 -0.0155 226 GLU A O   
1668 C CB  . GLU A 237 ? 0.4425 0.4043 0.3009 -0.0078 -0.0148 -0.0137 226 GLU A CB  
1669 C CG  . GLU A 237 ? 0.4837 0.4430 0.3332 -0.0079 -0.0175 -0.0127 226 GLU A CG  
1670 C CD  . GLU A 237 ? 0.5560 0.5158 0.4104 -0.0094 -0.0225 -0.0102 226 GLU A CD  
1671 O OE1 . GLU A 237 ? 0.5901 0.5518 0.4541 -0.0101 -0.0234 -0.0099 226 GLU A OE1 
1672 O OE2 . GLU A 237 ? 0.5740 0.5323 0.4228 -0.0097 -0.0253 -0.0083 226 GLU A OE2 
1673 N N   . LEU A 238 ? 0.4026 0.3688 0.2621 -0.0056 -0.0023 -0.0124 227 LEU A N   
1674 C CA  . LEU A 238 ? 0.4056 0.3734 0.2638 -0.0049 0.0029  -0.0103 227 LEU A CA  
1675 C C   . LEU A 238 ? 0.4187 0.3850 0.2741 -0.0026 0.0073  -0.0128 227 LEU A C   
1676 O O   . LEU A 238 ? 0.4171 0.3825 0.2659 -0.0013 0.0117  -0.0120 227 LEU A O   
1677 C CB  . LEU A 238 ? 0.3963 0.3684 0.2647 -0.0062 0.0042  -0.0074 227 LEU A CB  
1678 C CG  . LEU A 238 ? 0.4021 0.3749 0.2725 -0.0080 0.0016  -0.0049 227 LEU A CG  
1679 C CD1 . LEU A 238 ? 0.4036 0.3793 0.2829 -0.0096 0.0020  -0.0035 227 LEU A CD1 
1680 C CD2 . LEU A 238 ? 0.4058 0.3779 0.2703 -0.0078 0.0029  -0.0023 227 LEU A CD2 
1681 N N   . LEU A 239 ? 0.4229 0.3889 0.2835 -0.0021 0.0066  -0.0155 228 LEU A N   
1682 C CA  . LEU A 239 ? 0.4358 0.4000 0.2955 0.0002  0.0110  -0.0183 228 LEU A CA  
1683 C C   . LEU A 239 ? 0.4632 0.4210 0.3095 0.0017  0.0108  -0.0224 228 LEU A C   
1684 O O   . LEU A 239 ? 0.4813 0.4368 0.3222 0.0040  0.0164  -0.0241 228 LEU A O   
1685 C CB  . LEU A 239 ? 0.4306 0.3959 0.3008 0.0002  0.0095  -0.0196 228 LEU A CB  
1686 C CG  . LEU A 239 ? 0.4311 0.4019 0.3136 -0.0012 0.0096  -0.0160 228 LEU A CG  
1687 C CD1 . LEU A 239 ? 0.4251 0.3964 0.3156 -0.0019 0.0062  -0.0167 228 LEU A CD1 
1688 C CD2 . LEU A 239 ? 0.4265 0.4002 0.3144 0.0002  0.0157  -0.0139 228 LEU A CD2 
1689 N N   . THR A 240 ? 0.4640 0.4186 0.3047 0.0005  0.0046  -0.0240 229 THR A N   
1690 C CA  . THR A 240 ? 0.4752 0.4229 0.3030 0.0014  0.0029  -0.0285 229 THR A CA  
1691 C C   . THR A 240 ? 0.4949 0.4399 0.3098 0.0005  -0.0001 -0.0273 229 THR A C   
1692 O O   . THR A 240 ? 0.5147 0.4535 0.3164 0.0012  -0.0013 -0.0308 229 THR A O   
1693 C CB  . THR A 240 ? 0.4776 0.4228 0.3099 0.0005  -0.0032 -0.0318 229 THR A CB  
1694 O OG1 . THR A 240 ? 0.4894 0.4364 0.3247 -0.0020 -0.0094 -0.0291 229 THR A OG1 
1695 C CG2 . THR A 240 ? 0.4671 0.4151 0.3131 0.0009  -0.0015 -0.0320 229 THR A CG2 
1696 N N   . SER A 241 ? 0.4921 0.4413 0.3110 -0.0012 -0.0021 -0.0224 230 SER A N   
1697 C CA  . SER A 241 ? 0.5064 0.4544 0.3171 -0.0024 -0.0060 -0.0197 230 SER A CA  
1698 C C   . SER A 241 ? 0.5166 0.4616 0.3260 -0.0041 -0.0144 -0.0211 230 SER A C   
1699 O O   . SER A 241 ? 0.5271 0.4703 0.3290 -0.0051 -0.0186 -0.0191 230 SER A O   
1700 C CB  . SER A 241 ? 0.5294 0.4735 0.3244 -0.0010 -0.0022 -0.0198 230 SER A CB  
1701 O OG  . SER A 241 ? 0.5632 0.5105 0.3612 0.0006  0.0061  -0.0180 230 SER A OG  
1702 N N   . GLU A 242 ? 0.5090 0.4538 0.3265 -0.0045 -0.0172 -0.0240 231 GLU A N   
1703 C CA  . GLU A 242 ? 0.5166 0.4586 0.3353 -0.0060 -0.0250 -0.0254 231 GLU A CA  
1704 C C   . GLU A 242 ? 0.4965 0.4435 0.3312 -0.0072 -0.0265 -0.0231 231 GLU A C   
1705 O O   . GLU A 242 ? 0.4840 0.4338 0.3266 -0.0066 -0.0224 -0.0234 231 GLU A O   
1706 C CB  . GLU A 242 ? 0.5726 0.5087 0.3866 -0.0051 -0.0260 -0.0315 231 GLU A CB  
1707 C CG  . GLU A 242 ? 0.6994 0.6282 0.4992 -0.0057 -0.0317 -0.0348 231 GLU A CG  
1708 C CD  . GLU A 242 ? 0.8394 0.7643 0.6216 -0.0043 -0.0277 -0.0356 231 GLU A CD  
1709 O OE1 . GLU A 242 ? 0.8777 0.8040 0.6589 -0.0022 -0.0193 -0.0359 231 GLU A OE1 
1710 O OE2 . GLU A 242 ? 0.8905 0.8110 0.6602 -0.0055 -0.0331 -0.0355 231 GLU A OE2 
1711 N N   . PRO A 243 ? 0.4861 0.4338 0.3259 -0.0090 -0.0324 -0.0208 232 PRO A N   
1712 C CA  . PRO A 243 ? 0.4719 0.4236 0.3260 -0.0099 -0.0331 -0.0188 232 PRO A CA  
1713 C C   . PRO A 243 ? 0.4586 0.4085 0.3173 -0.0098 -0.0343 -0.0223 232 PRO A C   
1714 O O   . PRO A 243 ? 0.4644 0.4096 0.3194 -0.0102 -0.0393 -0.0253 232 PRO A O   
1715 C CB  . PRO A 243 ? 0.4812 0.4334 0.3390 -0.0115 -0.0389 -0.0156 232 PRO A CB  
1716 C CG  . PRO A 243 ? 0.4944 0.4439 0.3398 -0.0114 -0.0407 -0.0148 232 PRO A CG  
1717 C CD  . PRO A 243 ? 0.4830 0.4278 0.3161 -0.0102 -0.0388 -0.0197 232 PRO A CD  
1718 N N   . ILE A 244 ? 0.4397 0.3924 0.3057 -0.0092 -0.0301 -0.0222 233 ILE A N   
1719 C CA  . ILE A 244 ? 0.4304 0.3815 0.3016 -0.0089 -0.0308 -0.0250 233 ILE A CA  
1720 C C   . ILE A 244 ? 0.4330 0.3830 0.3116 -0.0105 -0.0368 -0.0247 233 ILE A C   
1721 O O   . ILE A 244 ? 0.4393 0.3849 0.3173 -0.0105 -0.0400 -0.0282 233 ILE A O   
1722 C CB  . ILE A 244 ? 0.4201 0.3751 0.2988 -0.0084 -0.0259 -0.0237 233 ILE A CB  
1723 C CG1 . ILE A 244 ? 0.4270 0.3799 0.3108 -0.0078 -0.0264 -0.0264 233 ILE A CG1 
1724 C CG2 . ILE A 244 ? 0.4147 0.3744 0.3012 -0.0097 -0.0254 -0.0194 233 ILE A CG2 
1725 C CD1 . ILE A 244 ? 0.4360 0.3923 0.3268 -0.0073 -0.0225 -0.0248 233 ILE A CD1 
1726 N N   . PHE A 245 ? 0.4265 0.3799 0.3120 -0.0117 -0.0382 -0.0207 234 PHE A N   
1727 C CA  . PHE A 245 ? 0.4293 0.3824 0.3240 -0.0131 -0.0434 -0.0195 234 PHE A CA  
1728 C C   . PHE A 245 ? 0.4555 0.4071 0.3479 -0.0142 -0.0490 -0.0182 234 PHE A C   
1729 O O   . PHE A 245 ? 0.4480 0.4017 0.3503 -0.0154 -0.0518 -0.0149 234 PHE A O   
1730 C CB  . PHE A 245 ? 0.4073 0.3651 0.3137 -0.0136 -0.0405 -0.0157 234 PHE A CB  
1731 C CG  . PHE A 245 ? 0.3957 0.3546 0.3037 -0.0128 -0.0361 -0.0165 234 PHE A CG  
1732 C CD1 . PHE A 245 ? 0.3961 0.3521 0.3055 -0.0124 -0.0375 -0.0195 234 PHE A CD1 
1733 C CD2 . PHE A 245 ? 0.3946 0.3571 0.3030 -0.0125 -0.0311 -0.0143 234 PHE A CD2 
1734 C CE1 . PHE A 245 ? 0.4008 0.3581 0.3130 -0.0117 -0.0339 -0.0195 234 PHE A CE1 
1735 C CE2 . PHE A 245 ? 0.4009 0.3645 0.3110 -0.0121 -0.0281 -0.0145 234 PHE A CE2 
1736 C CZ  . PHE A 245 ? 0.3953 0.3566 0.3078 -0.0116 -0.0295 -0.0168 234 PHE A CZ  
1737 N N   . HIS A 246 ? 0.4797 0.4273 0.3589 -0.0139 -0.0508 -0.0208 235 HIS A N   
1738 C CA  . HIS A 246 ? 0.5211 0.4665 0.3958 -0.0151 -0.0572 -0.0196 235 HIS A CA  
1739 C C   . HIS A 246 ? 0.5362 0.4794 0.4193 -0.0169 -0.0649 -0.0200 235 HIS A C   
1740 O O   . HIS A 246 ? 0.5360 0.4758 0.4198 -0.0170 -0.0663 -0.0238 235 HIS A O   
1741 C CB  . HIS A 246 ? 0.5571 0.4973 0.4141 -0.0144 -0.0579 -0.0230 235 HIS A CB  
1742 C CG  . HIS A 246 ? 0.6219 0.5591 0.4734 -0.0161 -0.0660 -0.0218 235 HIS A CG  
1743 N ND1 . HIS A 246 ? 0.6654 0.5969 0.5146 -0.0176 -0.0739 -0.0250 235 HIS A ND1 
1744 C CD2 . HIS A 246 ? 0.6459 0.5851 0.4962 -0.0167 -0.0679 -0.0171 235 HIS A CD2 
1745 C CE1 . HIS A 246 ? 0.6797 0.6101 0.5252 -0.0191 -0.0807 -0.0222 235 HIS A CE1 
1746 N NE2 . HIS A 246 ? 0.6746 0.6097 0.5210 -0.0186 -0.0772 -0.0172 235 HIS A NE2 
1747 N N   . CYS A 247 ? 0.5487 0.4937 0.4388 -0.0183 -0.0699 -0.0159 236 CYS A N   
1748 C CA  . CYS A 247 ? 0.5704 0.5147 0.4723 -0.0202 -0.0770 -0.0148 236 CYS A CA  
1749 C C   . CYS A 247 ? 0.5920 0.5364 0.4957 -0.0219 -0.0844 -0.0110 236 CYS A C   
1750 O O   . CYS A 247 ? 0.5933 0.5405 0.4951 -0.0213 -0.0820 -0.0074 236 CYS A O   
1751 C CB  . CYS A 247 ? 0.5777 0.5276 0.4964 -0.0200 -0.0722 -0.0113 236 CYS A CB  
1752 S SG  . CYS A 247 ? 0.6625 0.6131 0.6001 -0.0221 -0.0790 -0.0085 236 CYS A SG  
1753 N N   . ARG A 248 ? 0.6085 0.5498 0.5175 -0.0241 -0.0937 -0.0112 237 ARG A N   
1754 C CA  . ARG A 248 ? 0.6370 0.5787 0.5501 -0.0259 -0.1019 -0.0069 237 ARG A CA  
1755 C C   . ARG A 248 ? 0.6538 0.6029 0.5866 -0.0257 -0.0992 0.0002  237 ARG A C   
1756 O O   . ARG A 248 ? 0.6450 0.5980 0.5901 -0.0249 -0.0931 0.0014  237 ARG A O   
1757 C CB  . ARG A 248 ? 0.6654 0.6017 0.5805 -0.0286 -0.1134 -0.0089 237 ARG A CB  
1758 C CG  . ARG A 248 ? 0.7138 0.6521 0.6481 -0.0295 -0.1140 -0.0082 237 ARG A CG  
1759 C CD  . ARG A 248 ? 0.7719 0.7043 0.7085 -0.0325 -0.1259 -0.0105 237 ARG A CD  
1760 N NE  . ARG A 248 ? 0.8240 0.7573 0.7678 -0.0349 -0.1358 -0.0055 237 ARG A NE  
1761 C CZ  . ARG A 248 ? 0.8639 0.8030 0.8310 -0.0360 -0.1382 0.0012  237 ARG A CZ  
1762 N NH1 . ARG A 248 ? 0.8537 0.7980 0.8378 -0.0349 -0.1308 0.0035  237 ARG A NH1 
1763 N NH2 . ARG A 248 ? 0.8695 0.8092 0.8434 -0.0382 -0.1477 0.0059  237 ARG A NH2 
1764 N N   . GLN A 249 ? 0.6748 0.6256 0.6104 -0.0265 -0.1035 0.0051  238 GLN A N   
1765 C CA  . GLN A 249 ? 0.6926 0.6498 0.6471 -0.0261 -0.1012 0.0120  238 GLN A CA  
1766 C C   . GLN A 249 ? 0.6949 0.6545 0.6707 -0.0274 -0.1042 0.0147  238 GLN A C   
1767 O O   . GLN A 249 ? 0.7007 0.6568 0.6784 -0.0297 -0.1133 0.0132  238 GLN A O   
1768 C CB  . GLN A 249 ? 0.7318 0.6892 0.6849 -0.0270 -0.1074 0.0166  238 GLN A CB  
1769 C CG  . GLN A 249 ? 0.8150 0.7697 0.7470 -0.0259 -0.1050 0.0147  238 GLN A CG  
1770 C CD  . GLN A 249 ? 0.9006 0.8544 0.8293 -0.0272 -0.1128 0.0194  238 GLN A CD  
1771 O OE1 . GLN A 249 ? 0.9242 0.8785 0.8645 -0.0292 -0.1221 0.0235  238 GLN A OE1 
1772 N NE2 . GLN A 249 ? 0.9169 0.8697 0.8305 -0.0261 -0.1094 0.0195  238 GLN A NE2 
1773 N N   . SER A 255 ? 0.8261 0.8218 0.9340 -0.0149 -0.0346 0.0496  244 SER A N   
1774 C CA  . SER A 255 ? 0.8285 0.8266 0.9479 -0.0129 -0.0229 0.0529  244 SER A CA  
1775 C C   . SER A 255 ? 0.8283 0.8254 0.9402 -0.0132 -0.0184 0.0506  244 SER A C   
1776 O O   . SER A 255 ? 0.8380 0.8342 0.9421 -0.0115 -0.0080 0.0493  244 SER A O   
1777 C CB  . SER A 255 ? 0.8412 0.8437 0.9883 -0.0129 -0.0241 0.0603  244 SER A CB  
1778 O OG  . SER A 255 ? 0.8686 0.8722 1.0255 -0.0154 -0.0323 0.0621  244 SER A OG  
1779 N N   . ASN A 256 ? 0.8137 0.8106 0.9274 -0.0156 -0.0269 0.0501  245 ASN A N   
1780 C CA  . ASN A 256 ? 0.8047 0.8007 0.9134 -0.0163 -0.0250 0.0486  245 ASN A CA  
1781 C C   . ASN A 256 ? 0.7874 0.7796 0.8712 -0.0160 -0.0237 0.0419  245 ASN A C   
1782 O O   . ASN A 256 ? 0.7948 0.7846 0.8672 -0.0168 -0.0305 0.0380  245 ASN A O   
1783 C CB  . ASN A 256 ? 0.8266 0.8225 0.9452 -0.0190 -0.0363 0.0494  245 ASN A CB  
1784 C CG  . ASN A 256 ? 0.8870 0.8815 1.0023 -0.0201 -0.0368 0.0478  245 ASN A CG  
1785 O OD1 . ASN A 256 ? 0.9101 0.9053 1.0225 -0.0190 -0.0277 0.0486  245 ASN A OD1 
1786 N ND2 . ASN A 256 ? 0.8987 0.8908 1.0142 -0.0225 -0.0477 0.0455  245 ASN A ND2 
1787 N N   . PRO A 257 ? 0.7636 0.7551 0.8385 -0.0150 -0.0149 0.0408  246 PRO A N   
1788 C CA  . PRO A 257 ? 0.7498 0.7381 0.8028 -0.0149 -0.0144 0.0350  246 PRO A CA  
1789 C C   . PRO A 257 ? 0.7230 0.7093 0.7701 -0.0167 -0.0229 0.0317  246 PRO A C   
1790 O O   . PRO A 257 ? 0.7323 0.7160 0.7640 -0.0169 -0.0259 0.0268  246 PRO A O   
1791 C CB  . PRO A 257 ? 0.7642 0.7524 0.8121 -0.0138 -0.0040 0.0358  246 PRO A CB  
1792 C CG  . PRO A 257 ? 0.7700 0.7611 0.8363 -0.0138 -0.0008 0.0418  246 PRO A CG  
1793 C CD  . PRO A 257 ? 0.7494 0.7430 0.8338 -0.0139 -0.0054 0.0452  246 PRO A CD  
1794 N N   . TYR A 258 ? 0.6837 0.6710 0.7439 -0.0180 -0.0266 0.0344  247 TYR A N   
1795 C CA  . TYR A 258 ? 0.6601 0.6450 0.7175 -0.0197 -0.0346 0.0314  247 TYR A CA  
1796 C C   . TYR A 258 ? 0.6423 0.6248 0.6972 -0.0209 -0.0450 0.0284  247 TYR A C   
1797 O O   . TYR A 258 ? 0.6369 0.6208 0.7049 -0.0218 -0.0499 0.0316  247 TYR A O   
1798 C CB  . TYR A 258 ? 0.6476 0.6341 0.7218 -0.0208 -0.0351 0.0357  247 TYR A CB  
1799 C CG  . TYR A 258 ? 0.6466 0.6299 0.7191 -0.0225 -0.0427 0.0325  247 TYR A CG  
1800 C CD1 . TYR A 258 ? 0.6570 0.6386 0.7197 -0.0221 -0.0398 0.0302  247 TYR A CD1 
1801 C CD2 . TYR A 258 ? 0.6456 0.6271 0.7265 -0.0244 -0.0531 0.0317  247 TYR A CD2 
1802 C CE1 . TYR A 258 ? 0.6650 0.6433 0.7273 -0.0234 -0.0463 0.0272  247 TYR A CE1 
1803 C CE2 . TYR A 258 ? 0.6573 0.6347 0.7359 -0.0259 -0.0599 0.0280  247 TYR A CE2 
1804 C CZ  . TYR A 258 ? 0.6718 0.6476 0.7416 -0.0252 -0.0560 0.0257  247 TYR A CZ  
1805 O OH  . TYR A 258 ? 0.6872 0.6587 0.7565 -0.0264 -0.0622 0.0220  247 TYR A OH  
1806 N N   . HIS A 259 ? 0.6309 0.6097 0.6691 -0.0211 -0.0484 0.0226  248 HIS A N   
1807 C CA  . HIS A 259 ? 0.6197 0.5951 0.6507 -0.0221 -0.0575 0.0189  248 HIS A CA  
1808 C C   . HIS A 259 ? 0.5961 0.5670 0.6197 -0.0231 -0.0626 0.0140  248 HIS A C   
1809 O O   . HIS A 259 ? 0.6038 0.5729 0.6139 -0.0221 -0.0591 0.0101  248 HIS A O   
1810 C CB  . HIS A 259 ? 0.6441 0.6189 0.6600 -0.0209 -0.0551 0.0165  248 HIS A CB  
1811 C CG  . HIS A 259 ? 0.6882 0.6666 0.7113 -0.0198 -0.0500 0.0209  248 HIS A CG  
1812 N ND1 . HIS A 259 ? 0.7110 0.6913 0.7487 -0.0205 -0.0544 0.0252  248 HIS A ND1 
1813 C CD2 . HIS A 259 ? 0.7074 0.6872 0.7256 -0.0180 -0.0411 0.0214  248 HIS A CD2 
1814 C CE1 . HIS A 259 ? 0.7165 0.6995 0.7582 -0.0189 -0.0473 0.0282  248 HIS A CE1 
1815 N NE2 . HIS A 259 ? 0.7197 0.7022 0.7496 -0.0174 -0.0392 0.0257  248 HIS A NE2 
1816 N N   . HIS A 260 ? 0.5649 0.5338 0.5985 -0.0251 -0.0709 0.0141  249 HIS A N   
1817 C CA  . HIS A 260 ? 0.5470 0.5109 0.5766 -0.0262 -0.0762 0.0094  249 HIS A CA  
1818 C C   . HIS A 260 ? 0.5411 0.4998 0.5500 -0.0256 -0.0785 0.0024  249 HIS A C   
1819 O O   . HIS A 260 ? 0.5482 0.5045 0.5496 -0.0247 -0.0756 -0.0012 249 HIS A O   
1820 C CB  . HIS A 260 ? 0.5406 0.5026 0.5848 -0.0288 -0.0860 0.0108  249 HIS A CB  
1821 C CG  . HIS A 260 ? 0.5449 0.5009 0.5863 -0.0300 -0.0915 0.0057  249 HIS A CG  
1822 N ND1 . HIS A 260 ? 0.5679 0.5170 0.5943 -0.0307 -0.0985 -0.0010 249 HIS A ND1 
1823 C CD2 . HIS A 260 ? 0.5499 0.5055 0.6013 -0.0304 -0.0904 0.0065  249 HIS A CD2 
1824 C CE1 . HIS A 260 ? 0.5737 0.5182 0.6014 -0.0313 -0.1011 -0.0047 249 HIS A CE1 
1825 N NE2 . HIS A 260 ? 0.5714 0.5197 0.6147 -0.0313 -0.0967 -0.0002 249 HIS A NE2 
1826 N N   . ASP A 261 ? 0.5253 0.4818 0.5259 -0.0261 -0.0839 0.0008  250 ASP A N   
1827 C CA  . ASP A 261 ? 0.5247 0.4758 0.5054 -0.0256 -0.0860 -0.0055 250 ASP A CA  
1828 C C   . ASP A 261 ? 0.5026 0.4554 0.4709 -0.0232 -0.0769 -0.0070 250 ASP A C   
1829 O O   . ASP A 261 ? 0.5082 0.4571 0.4642 -0.0223 -0.0758 -0.0122 250 ASP A O   
1830 C CB  . ASP A 261 ? 0.5574 0.5064 0.5318 -0.0268 -0.0934 -0.0055 250 ASP A CB  
1831 C CG  . ASP A 261 ? 0.6483 0.5935 0.6306 -0.0296 -0.1048 -0.0057 250 ASP A CG  
1832 O OD1 . ASP A 261 ? 0.6603 0.6048 0.6549 -0.0307 -0.1068 -0.0057 250 ASP A OD1 
1833 O OD2 . ASP A 261 ? 0.6950 0.6379 0.6716 -0.0309 -0.1122 -0.0056 250 ASP A OD2 
1834 N N   . GLN A 262 ? 0.4717 0.4300 0.4440 -0.0221 -0.0704 -0.0026 251 GLN A N   
1835 C CA  . GLN A 262 ? 0.4622 0.4220 0.4240 -0.0202 -0.0624 -0.0038 251 GLN A CA  
1836 C C   . GLN A 262 ? 0.4506 0.4103 0.4134 -0.0196 -0.0581 -0.0053 251 GLN A C   
1837 O O   . GLN A 262 ? 0.4565 0.4140 0.4082 -0.0185 -0.0558 -0.0091 251 GLN A O   
1838 C CB  . GLN A 262 ? 0.4601 0.4247 0.4258 -0.0194 -0.0568 0.0007  251 GLN A CB  
1839 C CG  . GLN A 262 ? 0.4633 0.4289 0.4179 -0.0179 -0.0497 -0.0007 251 GLN A CG  
1840 C CD  . GLN A 262 ? 0.4694 0.4319 0.4092 -0.0174 -0.0516 -0.0044 251 GLN A CD  
1841 O OE1 . GLN A 262 ? 0.4636 0.4261 0.4003 -0.0175 -0.0538 -0.0032 251 GLN A OE1 
1842 N NE2 . GLN A 262 ? 0.4727 0.4326 0.4035 -0.0167 -0.0504 -0.0086 251 GLN A NE2 
1843 N N   . LEU A 263 ? 0.4301 0.3917 0.4069 -0.0203 -0.0576 -0.0020 252 LEU A N   
1844 C CA  . LEU A 263 ? 0.4181 0.3797 0.3970 -0.0199 -0.0543 -0.0024 252 LEU A CA  
1845 C C   . LEU A 263 ? 0.4254 0.3814 0.3995 -0.0201 -0.0590 -0.0078 252 LEU A C   
1846 O O   . LEU A 263 ? 0.4349 0.3897 0.4027 -0.0189 -0.0558 -0.0104 252 LEU A O   
1847 C CB  . LEU A 263 ? 0.3974 0.3620 0.3924 -0.0207 -0.0529 0.0029  252 LEU A CB  
1848 C CG  . LEU A 263 ? 0.3970 0.3663 0.3945 -0.0199 -0.0452 0.0076  252 LEU A CG  
1849 C CD1 . LEU A 263 ? 0.3908 0.3630 0.4054 -0.0207 -0.0442 0.0134  252 LEU A CD1 
1850 C CD2 . LEU A 263 ? 0.3958 0.3658 0.3848 -0.0189 -0.0393 0.0069  252 LEU A CD2 
1851 N N   . ASP A 264 ? 0.4194 0.3715 0.3957 -0.0215 -0.0668 -0.0098 253 ASP A N   
1852 C CA  . ASP A 264 ? 0.4225 0.3678 0.3928 -0.0218 -0.0718 -0.0159 253 ASP A CA  
1853 C C   . ASP A 264 ? 0.4241 0.3667 0.3765 -0.0199 -0.0688 -0.0209 253 ASP A C   
1854 O O   . ASP A 264 ? 0.4342 0.3730 0.3823 -0.0189 -0.0675 -0.0251 253 ASP A O   
1855 C CB  . ASP A 264 ? 0.4512 0.3926 0.4249 -0.0240 -0.0815 -0.0170 253 ASP A CB  
1856 C CG  . ASP A 264 ? 0.5304 0.4632 0.4946 -0.0244 -0.0874 -0.0243 253 ASP A CG  
1857 O OD1 . ASP A 264 ? 0.5432 0.4728 0.5104 -0.0240 -0.0866 -0.0271 253 ASP A OD1 
1858 O OD2 . ASP A 264 ? 0.5818 0.5107 0.5352 -0.0252 -0.0927 -0.0271 253 ASP A OD2 
1859 N N   . ARG A 265 ? 0.4241 0.3684 0.3672 -0.0194 -0.0673 -0.0202 254 ARG A N   
1860 C CA  . ARG A 265 ? 0.4359 0.3783 0.3629 -0.0177 -0.0636 -0.0240 254 ARG A CA  
1861 C C   . ARG A 265 ? 0.4426 0.3882 0.3698 -0.0160 -0.0558 -0.0233 254 ARG A C   
1862 O O   . ARG A 265 ? 0.4595 0.4024 0.3790 -0.0145 -0.0532 -0.0272 254 ARG A O   
1863 C CB  . ARG A 265 ? 0.4427 0.3871 0.3623 -0.0177 -0.0636 -0.0220 254 ARG A CB  
1864 C CG  . ARG A 265 ? 0.4694 0.4130 0.3742 -0.0159 -0.0587 -0.0245 254 ARG A CG  
1865 C CD  . ARG A 265 ? 0.4977 0.4342 0.3899 -0.0152 -0.0605 -0.0308 254 ARG A CD  
1866 N NE  . ARG A 265 ? 0.5220 0.4586 0.4028 -0.0131 -0.0541 -0.0326 254 ARG A NE  
1867 C CZ  . ARG A 265 ? 0.5378 0.4686 0.4049 -0.0120 -0.0537 -0.0375 254 ARG A CZ  
1868 N NH1 . ARG A 265 ? 0.5424 0.4662 0.4036 -0.0129 -0.0599 -0.0418 254 ARG A NH1 
1869 N NH2 . ARG A 265 ? 0.5317 0.4635 0.3908 -0.0101 -0.0469 -0.0381 254 ARG A NH2 
1870 N N   . ILE A 266 ? 0.4250 0.3763 0.3613 -0.0162 -0.0520 -0.0182 255 ILE A N   
1871 C CA  . ILE A 266 ? 0.4195 0.3737 0.3565 -0.0151 -0.0459 -0.0170 255 ILE A CA  
1872 C C   . ILE A 266 ? 0.4277 0.3793 0.3697 -0.0148 -0.0465 -0.0189 255 ILE A C   
1873 O O   . ILE A 266 ? 0.4365 0.3875 0.3742 -0.0134 -0.0432 -0.0208 255 ILE A O   
1874 C CB  . ILE A 266 ? 0.4121 0.3716 0.3563 -0.0156 -0.0423 -0.0113 255 ILE A CB  
1875 C CG1 . ILE A 266 ? 0.4124 0.3741 0.3514 -0.0155 -0.0408 -0.0099 255 ILE A CG1 
1876 C CG2 . ILE A 266 ? 0.4181 0.3801 0.3634 -0.0150 -0.0373 -0.0097 255 ILE A CG2 
1877 C CD1 . ILE A 266 ? 0.4212 0.3870 0.3665 -0.0159 -0.0369 -0.0051 255 ILE A CD1 
1878 N N   . PHE A 267 ? 0.4174 0.3671 0.3696 -0.0160 -0.0510 -0.0184 256 PHE A N   
1879 C CA  . PHE A 267 ? 0.4125 0.3591 0.3707 -0.0158 -0.0520 -0.0202 256 PHE A CA  
1880 C C   . PHE A 267 ? 0.4242 0.3642 0.3732 -0.0147 -0.0538 -0.0272 256 PHE A C   
1881 O O   . PHE A 267 ? 0.4167 0.3549 0.3660 -0.0133 -0.0513 -0.0293 256 PHE A O   
1882 C CB  . PHE A 267 ? 0.4016 0.3480 0.3744 -0.0176 -0.0560 -0.0172 256 PHE A CB  
1883 C CG  . PHE A 267 ? 0.4017 0.3543 0.3836 -0.0184 -0.0531 -0.0102 256 PHE A CG  
1884 C CD1 . PHE A 267 ? 0.4118 0.3689 0.3913 -0.0175 -0.0468 -0.0068 256 PHE A CD1 
1885 C CD2 . PHE A 267 ? 0.4036 0.3573 0.3963 -0.0201 -0.0566 -0.0069 256 PHE A CD2 
1886 C CE1 . PHE A 267 ? 0.4183 0.3801 0.4041 -0.0182 -0.0435 -0.0009 256 PHE A CE1 
1887 C CE2 . PHE A 267 ? 0.4091 0.3682 0.4099 -0.0205 -0.0527 -0.0005 256 PHE A CE2 
1888 C CZ  . PHE A 267 ? 0.4122 0.3750 0.4086 -0.0195 -0.0459 0.0022  256 PHE A CZ  
1889 N N   . ASN A 268 ? 0.4447 0.3809 0.3844 -0.0151 -0.0577 -0.0306 257 ASN A N   
1890 C CA  . ASN A 268 ? 0.4683 0.3974 0.3960 -0.0139 -0.0587 -0.0376 257 ASN A CA  
1891 C C   . ASN A 268 ? 0.4686 0.3993 0.3876 -0.0115 -0.0513 -0.0387 257 ASN A C   
1892 O O   . ASN A 268 ? 0.4820 0.4081 0.3968 -0.0098 -0.0493 -0.0434 257 ASN A O   
1893 C CB  . ASN A 268 ? 0.5156 0.4407 0.4334 -0.0151 -0.0644 -0.0402 257 ASN A CB  
1894 C CG  . ASN A 268 ? 0.6129 0.5307 0.5335 -0.0167 -0.0720 -0.0443 257 ASN A CG  
1895 O OD1 . ASN A 268 ? 0.6558 0.5667 0.5711 -0.0156 -0.0720 -0.0503 257 ASN A OD1 
1896 N ND2 . ASN A 268 ? 0.6290 0.5479 0.5590 -0.0192 -0.0785 -0.0411 257 ASN A ND2 
1897 N N   . VAL A 269 ? 0.4570 0.3943 0.3749 -0.0112 -0.0471 -0.0343 258 VAL A N   
1898 C CA  . VAL A 269 ? 0.4567 0.3960 0.3686 -0.0093 -0.0407 -0.0346 258 VAL A CA  
1899 C C   . VAL A 269 ? 0.4509 0.3939 0.3729 -0.0086 -0.0370 -0.0318 258 VAL A C   
1900 O O   . VAL A 269 ? 0.4508 0.3919 0.3724 -0.0068 -0.0339 -0.0343 258 VAL A O   
1901 C CB  . VAL A 269 ? 0.4545 0.3981 0.3595 -0.0095 -0.0384 -0.0317 258 VAL A CB  
1902 C CG1 . VAL A 269 ? 0.4473 0.3943 0.3497 -0.0079 -0.0320 -0.0307 258 VAL A CG1 
1903 C CG2 . VAL A 269 ? 0.4610 0.4006 0.3544 -0.0097 -0.0416 -0.0345 258 VAL A CG2 
1904 N N   . MET A 270 ? 0.4435 0.3912 0.3742 -0.0100 -0.0372 -0.0265 259 MET A N   
1905 C CA  . MET A 270 ? 0.4500 0.4016 0.3887 -0.0098 -0.0343 -0.0227 259 MET A CA  
1906 C C   . MET A 270 ? 0.4562 0.4057 0.4058 -0.0099 -0.0363 -0.0225 259 MET A C   
1907 O O   . MET A 270 ? 0.4589 0.4103 0.4142 -0.0093 -0.0340 -0.0202 259 MET A O   
1908 C CB  . MET A 270 ? 0.4503 0.4073 0.3919 -0.0114 -0.0334 -0.0171 259 MET A CB  
1909 C CG  . MET A 270 ? 0.4645 0.4236 0.3972 -0.0114 -0.0315 -0.0167 259 MET A CG  
1910 S SD  . MET A 270 ? 0.4647 0.4253 0.3900 -0.0100 -0.0269 -0.0178 259 MET A SD  
1911 C CE  . MET A 270 ? 0.4022 0.3665 0.3351 -0.0105 -0.0251 -0.0135 259 MET A CE  
1912 N N   . GLY A 271 ? 0.4523 0.3982 0.4058 -0.0110 -0.0409 -0.0239 260 GLY A N   
1913 C CA  . GLY A 271 ? 0.4567 0.4009 0.4225 -0.0116 -0.0433 -0.0227 260 GLY A CA  
1914 C C   . GLY A 271 ? 0.4601 0.4088 0.4345 -0.0136 -0.0442 -0.0163 260 GLY A C   
1915 O O   . GLY A 271 ? 0.4523 0.4052 0.4227 -0.0141 -0.0422 -0.0132 260 GLY A O   
1916 N N   . PHE A 272 ? 0.4637 0.4111 0.4503 -0.0145 -0.0468 -0.0142 261 PHE A N   
1917 C CA  . PHE A 272 ? 0.4671 0.4186 0.4630 -0.0162 -0.0468 -0.0077 261 PHE A CA  
1918 C C   . PHE A 272 ? 0.4741 0.4300 0.4727 -0.0159 -0.0425 -0.0023 261 PHE A C   
1919 O O   . PHE A 272 ? 0.4722 0.4268 0.4739 -0.0150 -0.0420 -0.0026 261 PHE A O   
1920 C CB  . PHE A 272 ? 0.4627 0.4110 0.4714 -0.0176 -0.0519 -0.0075 261 PHE A CB  
1921 C CG  . PHE A 272 ? 0.4632 0.4156 0.4812 -0.0194 -0.0519 -0.0010 261 PHE A CG  
1922 C CD1 . PHE A 272 ? 0.4677 0.4238 0.4950 -0.0199 -0.0489 0.0058  261 PHE A CD1 
1923 C CD2 . PHE A 272 ? 0.4676 0.4204 0.4854 -0.0204 -0.0545 -0.0014 261 PHE A CD2 
1924 C CE1 . PHE A 272 ? 0.4717 0.4316 0.5073 -0.0211 -0.0475 0.0119  261 PHE A CE1 
1925 C CE2 . PHE A 272 ? 0.4706 0.4275 0.4987 -0.0217 -0.0537 0.0048  261 PHE A CE2 
1926 C CZ  . PHE A 272 ? 0.4643 0.4247 0.5008 -0.0219 -0.0496 0.0113  261 PHE A CZ  
1927 N N   . PRO A 273 ? 0.4840 0.4448 0.4801 -0.0166 -0.0392 0.0026  262 PRO A N   
1928 C CA  . PRO A 273 ? 0.4982 0.4624 0.4942 -0.0166 -0.0356 0.0077  262 PRO A CA  
1929 C C   . PRO A 273 ? 0.5161 0.4804 0.5249 -0.0174 -0.0366 0.0126  262 PRO A C   
1930 O O   . PRO A 273 ? 0.5227 0.4868 0.5405 -0.0185 -0.0380 0.0150  262 PRO A O   
1931 C CB  . PRO A 273 ? 0.4991 0.4670 0.4889 -0.0173 -0.0321 0.0109  262 PRO A CB  
1932 C CG  . PRO A 273 ? 0.4995 0.4667 0.4932 -0.0179 -0.0339 0.0099  262 PRO A CG  
1933 C CD  . PRO A 273 ? 0.4787 0.4415 0.4720 -0.0174 -0.0386 0.0037  262 PRO A CD  
1934 N N   . ALA A 274 ? 0.5248 0.4893 0.5356 -0.0169 -0.0361 0.0144  263 ALA A N   
1935 C CA  . ALA A 274 ? 0.5368 0.5017 0.5593 -0.0177 -0.0367 0.0202  263 ALA A CA  
1936 C C   . ALA A 274 ? 0.5511 0.5204 0.5708 -0.0189 -0.0330 0.0276  263 ALA A C   
1937 O O   . ALA A 274 ? 0.5553 0.5267 0.5634 -0.0189 -0.0303 0.0273  263 ALA A O   
1938 C CB  . ALA A 274 ? 0.5390 0.5027 0.5648 -0.0166 -0.0375 0.0200  263 ALA A CB  
1939 N N   . ASP A 275 ? 0.5584 0.5286 0.5881 -0.0199 -0.0328 0.0341  264 ASP A N   
1940 C CA  . ASP A 275 ? 0.5695 0.5432 0.5954 -0.0210 -0.0287 0.0414  264 ASP A CA  
1941 C C   . ASP A 275 ? 0.5586 0.5339 0.5714 -0.0209 -0.0270 0.0426  264 ASP A C   
1942 O O   . ASP A 275 ? 0.5624 0.5393 0.5644 -0.0214 -0.0235 0.0440  264 ASP A O   
1943 C CB  . ASP A 275 ? 0.6091 0.5832 0.6481 -0.0220 -0.0289 0.0489  264 ASP A CB  
1944 C CG  . ASP A 275 ? 0.6993 0.6722 0.7528 -0.0226 -0.0303 0.0497  264 ASP A CG  
1945 O OD1 . ASP A 275 ? 0.7167 0.6892 0.7695 -0.0225 -0.0307 0.0453  264 ASP A OD1 
1946 O OD2 . ASP A 275 ? 0.7318 0.7046 0.7984 -0.0233 -0.0313 0.0552  264 ASP A OD2 
1947 N N   . LYS A 276 ? 0.5457 0.5202 0.5601 -0.0203 -0.0297 0.0415  265 LYS A N   
1948 C CA  . LYS A 276 ? 0.5516 0.5277 0.5564 -0.0205 -0.0294 0.0431  265 LYS A CA  
1949 C C   . LYS A 276 ? 0.5433 0.5197 0.5354 -0.0200 -0.0283 0.0375  265 LYS A C   
1950 O O   . LYS A 276 ? 0.5501 0.5280 0.5320 -0.0209 -0.0273 0.0393  265 LYS A O   
1951 C CB  . LYS A 276 ? 0.5928 0.5683 0.6063 -0.0198 -0.0327 0.0442  265 LYS A CB  
1952 C CG  . LYS A 276 ? 0.6635 0.6363 0.6821 -0.0179 -0.0345 0.0366  265 LYS A CG  
1953 C CD  . LYS A 276 ? 0.7339 0.7058 0.7640 -0.0169 -0.0369 0.0381  265 LYS A CD  
1954 C CE  . LYS A 276 ? 0.7950 0.7626 0.8320 -0.0150 -0.0380 0.0307  265 LYS A CE  
1955 N NZ  . LYS A 276 ? 0.8294 0.7939 0.8736 -0.0154 -0.0391 0.0293  265 LYS A NZ  
1956 N N   . ASP A 277 ? 0.5267 0.5014 0.5193 -0.0189 -0.0287 0.0308  266 ASP A N   
1957 C CA  . ASP A 277 ? 0.5216 0.4963 0.5036 -0.0183 -0.0276 0.0254  266 ASP A CA  
1958 C C   . ASP A 277 ? 0.5094 0.4853 0.4826 -0.0192 -0.0243 0.0266  266 ASP A C   
1959 O O   . ASP A 277 ? 0.5104 0.4869 0.4732 -0.0193 -0.0229 0.0248  266 ASP A O   
1960 C CB  . ASP A 277 ? 0.5414 0.5135 0.5264 -0.0169 -0.0291 0.0187  266 ASP A CB  
1961 C CG  . ASP A 277 ? 0.6055 0.5753 0.5973 -0.0155 -0.0314 0.0158  266 ASP A CG  
1962 O OD1 . ASP A 277 ? 0.6167 0.5878 0.6097 -0.0153 -0.0315 0.0182  266 ASP A OD1 
1963 O OD2 . ASP A 277 ? 0.6346 0.6010 0.6304 -0.0146 -0.0331 0.0111  266 ASP A OD2 
1964 N N   . TRP A 278 ? 0.4963 0.4723 0.4746 -0.0197 -0.0228 0.0294  267 TRP A N   
1965 C CA  . TRP A 278 ? 0.4994 0.4762 0.4715 -0.0202 -0.0188 0.0305  267 TRP A CA  
1966 C C   . TRP A 278 ? 0.5126 0.4904 0.4909 -0.0210 -0.0163 0.0371  267 TRP A C   
1967 O O   . TRP A 278 ? 0.5078 0.4856 0.4956 -0.0210 -0.0159 0.0380  267 TRP A O   
1968 C CB  . TRP A 278 ? 0.4866 0.4626 0.4600 -0.0194 -0.0193 0.0256  267 TRP A CB  
1969 C CG  . TRP A 278 ? 0.4803 0.4571 0.4478 -0.0195 -0.0151 0.0258  267 TRP A CG  
1970 C CD1 . TRP A 278 ? 0.4901 0.4675 0.4506 -0.0201 -0.0104 0.0293  267 TRP A CD1 
1971 C CD2 . TRP A 278 ? 0.4759 0.4523 0.4438 -0.0189 -0.0153 0.0222  267 TRP A CD2 
1972 N NE1 . TRP A 278 ? 0.4935 0.4709 0.4516 -0.0196 -0.0071 0.0280  267 TRP A NE1 
1973 C CE2 . TRP A 278 ? 0.4867 0.4638 0.4500 -0.0189 -0.0103 0.0240  267 TRP A CE2 
1974 C CE3 . TRP A 278 ? 0.4745 0.4497 0.4460 -0.0183 -0.0194 0.0177  267 TRP A CE3 
1975 C CZ2 . TRP A 278 ? 0.4909 0.4680 0.4549 -0.0184 -0.0093 0.0219  267 TRP A CZ2 
1976 C CZ3 . TRP A 278 ? 0.4828 0.4580 0.4538 -0.0180 -0.0190 0.0160  267 TRP A CZ3 
1977 C CH2 . TRP A 278 ? 0.4873 0.4638 0.4555 -0.0180 -0.0141 0.0182  267 TRP A CH2 
1978 N N   . GLU A 279 ? 0.5273 0.5057 0.5004 -0.0220 -0.0147 0.0422  268 GLU A N   
1979 C CA  . GLU A 279 ? 0.5505 0.5297 0.5278 -0.0228 -0.0117 0.0494  268 GLU A CA  
1980 C C   . GLU A 279 ? 0.5667 0.5463 0.5434 -0.0226 -0.0061 0.0505  268 GLU A C   
1981 O O   . GLU A 279 ? 0.5758 0.5563 0.5646 -0.0227 -0.0048 0.0542  268 GLU A O   
1982 C CB  . GLU A 279 ? 0.5909 0.5702 0.5586 -0.0240 -0.0112 0.0544  268 GLU A CB  
1983 C CG  . GLU A 279 ? 0.6776 0.6570 0.6508 -0.0241 -0.0167 0.0551  268 GLU A CG  
1984 C CD  . GLU A 279 ? 0.7786 0.7585 0.7482 -0.0255 -0.0175 0.0624  268 GLU A CD  
1985 O OE1 . GLU A 279 ? 0.7882 0.7682 0.7554 -0.0263 -0.0136 0.0684  268 GLU A OE1 
1986 O OE2 . GLU A 279 ? 0.8109 0.7910 0.7803 -0.0257 -0.0218 0.0625  268 GLU A OE2 
1987 N N   . ASP A 280 ? 0.5711 0.5501 0.5357 -0.0223 -0.0029 0.0474  269 ASP A N   
1988 C CA  . ASP A 280 ? 0.5819 0.5611 0.5463 -0.0218 0.0032  0.0484  269 ASP A CA  
1989 C C   . ASP A 280 ? 0.5819 0.5618 0.5578 -0.0209 0.0019  0.0452  269 ASP A C   
1990 O O   . ASP A 280 ? 0.5826 0.5629 0.5587 -0.0203 0.0065  0.0452  269 ASP A O   
1991 C CB  . ASP A 280 ? 0.6174 0.5948 0.5647 -0.0219 0.0074  0.0463  269 ASP A CB  
1992 C CG  . ASP A 280 ? 0.6870 0.6630 0.6216 -0.0231 0.0096  0.0505  269 ASP A CG  
1993 O OD1 . ASP A 280 ? 0.6914 0.6683 0.6314 -0.0237 0.0101  0.0567  269 ASP A OD1 
1994 O OD2 . ASP A 280 ? 0.7278 0.7016 0.6473 -0.0236 0.0104  0.0478  269 ASP A OD2 
1995 N N   . ILE A 281 ? 0.5757 0.5556 0.5613 -0.0209 -0.0044 0.0425  270 ILE A N   
1996 C CA  . ILE A 281 ? 0.5741 0.5543 0.5702 -0.0204 -0.0068 0.0398  270 ILE A CA  
1997 C C   . ILE A 281 ? 0.5857 0.5676 0.5960 -0.0207 -0.0039 0.0456  270 ILE A C   
1998 O O   . ILE A 281 ? 0.5859 0.5687 0.6029 -0.0203 -0.0029 0.0452  270 ILE A O   
1999 C CB  . ILE A 281 ? 0.5644 0.5430 0.5654 -0.0204 -0.0142 0.0350  270 ILE A CB  
2000 C CG1 . ILE A 281 ? 0.5645 0.5424 0.5683 -0.0199 -0.0170 0.0304  270 ILE A CG1 
2001 C CG2 . ILE A 281 ? 0.5584 0.5366 0.5730 -0.0211 -0.0173 0.0384  270 ILE A CG2 
2002 C CD1 . ILE A 281 ? 0.5744 0.5497 0.5803 -0.0198 -0.0238 0.0250  270 ILE A CD1 
2003 N N   . LYS A 282 ? 0.5912 0.5737 0.6065 -0.0214 -0.0022 0.0517  271 LYS A N   
2004 C CA  . LYS A 282 ? 0.5995 0.5840 0.6288 -0.0218 0.0015  0.0584  271 LYS A CA  
2005 C C   . LYS A 282 ? 0.6046 0.5902 0.6303 -0.0209 0.0096  0.0605  271 LYS A C   
2006 O O   . LYS A 282 ? 0.6094 0.5969 0.6491 -0.0207 0.0121  0.0639  271 LYS A O   
2007 C CB  . LYS A 282 ? 0.6380 0.6228 0.6685 -0.0226 0.0031  0.0650  271 LYS A CB  
2008 C CG  . LYS A 282 ? 0.7061 0.6899 0.7471 -0.0233 -0.0041 0.0648  271 LYS A CG  
2009 C CD  . LYS A 282 ? 0.7782 0.7626 0.8221 -0.0242 -0.0023 0.0726  271 LYS A CD  
2010 C CE  . LYS A 282 ? 0.8328 0.8195 0.8875 -0.0245 0.0038  0.0807  271 LYS A CE  
2011 N NZ  . LYS A 282 ? 0.8533 0.8404 0.9175 -0.0256 0.0034  0.0885  271 LYS A NZ  
2012 N N   . LYS A 283 ? 0.6058 0.5901 0.6135 -0.0203 0.0138  0.0582  272 LYS A N   
2013 C CA  . LYS A 283 ? 0.6062 0.5903 0.6075 -0.0193 0.0221  0.0590  272 LYS A CA  
2014 C C   . LYS A 283 ? 0.5914 0.5759 0.5970 -0.0183 0.0218  0.0547  272 LYS A C   
2015 O O   . LYS A 283 ? 0.5960 0.5805 0.6000 -0.0171 0.0290  0.0557  272 LYS A O   
2016 C CB  . LYS A 283 ? 0.6488 0.6302 0.6282 -0.0194 0.0253  0.0572  272 LYS A CB  
2017 C CG  . LYS A 283 ? 0.7113 0.6920 0.6835 -0.0204 0.0273  0.0627  272 LYS A CG  
2018 C CD  . LYS A 283 ? 0.7862 0.7635 0.7365 -0.0206 0.0317  0.0610  272 LYS A CD  
2019 C CE  . LYS A 283 ? 0.8455 0.8216 0.7849 -0.0220 0.0318  0.0657  272 LYS A CE  
2020 N NZ  . LYS A 283 ? 0.8910 0.8631 0.8080 -0.0226 0.0335  0.0625  272 LYS A NZ  
2021 N N   . MET A 284 ? 0.5723 0.5568 0.5821 -0.0185 0.0137  0.0498  273 MET A N   
2022 C CA  . MET A 284 ? 0.5587 0.5435 0.5723 -0.0177 0.0124  0.0462  273 MET A CA  
2023 C C   . MET A 284 ? 0.5450 0.5324 0.5781 -0.0176 0.0138  0.0507  273 MET A C   
2024 O O   . MET A 284 ? 0.5426 0.5313 0.5893 -0.0186 0.0104  0.0541  273 MET A O   
2025 C CB  . MET A 284 ? 0.5639 0.5476 0.5758 -0.0182 0.0034  0.0403  273 MET A CB  
2026 C CG  . MET A 284 ? 0.5839 0.5654 0.5790 -0.0183 0.0016  0.0361  273 MET A CG  
2027 S SD  . MET A 284 ? 0.5738 0.5538 0.5512 -0.0176 0.0081  0.0339  273 MET A SD  
2028 C CE  . MET A 284 ? 0.5117 0.4919 0.4932 -0.0166 0.0075  0.0309  273 MET A CE  
2029 N N   . PRO A 285 ? 0.5381 0.5264 0.5745 -0.0163 0.0183  0.0509  274 PRO A N   
2030 C CA  . PRO A 285 ? 0.5252 0.5165 0.5826 -0.0161 0.0195  0.0558  274 PRO A CA  
2031 C C   . PRO A 285 ? 0.5211 0.5134 0.5936 -0.0176 0.0092  0.0553  274 PRO A C   
2032 O O   . PRO A 285 ? 0.5229 0.5176 0.6141 -0.0182 0.0088  0.0605  274 PRO A O   
2033 C CB  . PRO A 285 ? 0.5305 0.5218 0.5865 -0.0145 0.0246  0.0544  274 PRO A CB  
2034 C CG  . PRO A 285 ? 0.5430 0.5311 0.5772 -0.0137 0.0302  0.0510  274 PRO A CG  
2035 C CD  . PRO A 285 ? 0.5323 0.5186 0.5548 -0.0151 0.0228  0.0471  274 PRO A CD  
2036 N N   . GLU A 286 ? 0.5131 0.5031 0.5773 -0.0183 0.0008  0.0490  275 GLU A N   
2037 C CA  . GLU A 286 ? 0.5045 0.4941 0.5798 -0.0198 -0.0094 0.0476  275 GLU A CA  
2038 C C   . GLU A 286 ? 0.4945 0.4819 0.5675 -0.0210 -0.0148 0.0458  275 GLU A C   
2039 O O   . GLU A 286 ? 0.4992 0.4844 0.5753 -0.0221 -0.0236 0.0422  275 GLU A O   
2040 C CB  . GLU A 286 ? 0.5291 0.5171 0.5977 -0.0197 -0.0155 0.0420  275 GLU A CB  
2041 C CG  . GLU A 286 ? 0.5967 0.5865 0.6667 -0.0183 -0.0106 0.0431  275 GLU A CG  
2042 C CD  . GLU A 286 ? 0.6760 0.6691 0.7676 -0.0184 -0.0097 0.0490  275 GLU A CD  
2043 O OE1 . GLU A 286 ? 0.6817 0.6753 0.7877 -0.0201 -0.0171 0.0508  275 GLU A OE1 
2044 O OE2 . GLU A 286 ? 0.7261 0.7210 0.8208 -0.0167 -0.0017 0.0518  275 GLU A OE2 
2045 N N   . HIS A 287 ? 0.4831 0.4704 0.5502 -0.0208 -0.0098 0.0481  276 HIS A N   
2046 C CA  . HIS A 287 ? 0.4839 0.4691 0.5504 -0.0218 -0.0146 0.0470  276 HIS A CA  
2047 C C   . HIS A 287 ? 0.4860 0.4712 0.5720 -0.0234 -0.0207 0.0495  276 HIS A C   
2048 O O   . HIS A 287 ? 0.4946 0.4766 0.5805 -0.0242 -0.0282 0.0452  276 HIS A O   
2049 C CB  . HIS A 287 ? 0.4834 0.4690 0.5417 -0.0215 -0.0086 0.0504  276 HIS A CB  
2050 C CG  . HIS A 287 ? 0.4945 0.4780 0.5541 -0.0224 -0.0137 0.0497  276 HIS A CG  
2051 N ND1 . HIS A 287 ? 0.5086 0.4931 0.5805 -0.0233 -0.0128 0.0559  276 HIS A ND1 
2052 C CD2 . HIS A 287 ? 0.5069 0.4875 0.5586 -0.0224 -0.0193 0.0437  276 HIS A CD2 
2053 C CE1 . HIS A 287 ? 0.5148 0.4967 0.5856 -0.0237 -0.0181 0.0534  276 HIS A CE1 
2054 N NE2 . HIS A 287 ? 0.5180 0.4976 0.5769 -0.0231 -0.0219 0.0459  276 HIS A NE2 
2055 N N   . SER A 288 ? 0.4725 0.4608 0.5754 -0.0238 -0.0174 0.0562  277 SER A N   
2056 C CA  . SER A 288 ? 0.4736 0.4619 0.5969 -0.0256 -0.0237 0.0589  277 SER A CA  
2057 C C   . SER A 288 ? 0.4779 0.4641 0.6067 -0.0267 -0.0335 0.0541  277 SER A C   
2058 O O   . SER A 288 ? 0.4782 0.4617 0.6161 -0.0285 -0.0417 0.0525  277 SER A O   
2059 C CB  . SER A 288 ? 0.4890 0.4815 0.6300 -0.0258 -0.0171 0.0681  277 SER A CB  
2060 O OG  . SER A 288 ? 0.5164 0.5091 0.6560 -0.0258 -0.0125 0.0724  277 SER A OG  
2061 N N   . THR A 289 ? 0.4794 0.4663 0.6009 -0.0258 -0.0332 0.0514  278 THR A N   
2062 C CA  . THR A 289 ? 0.4827 0.4674 0.6052 -0.0268 -0.0426 0.0467  278 THR A CA  
2063 C C   . THR A 289 ? 0.4896 0.4688 0.5953 -0.0270 -0.0486 0.0384  278 THR A C   
2064 O O   . THR A 289 ? 0.5016 0.4770 0.6097 -0.0285 -0.0581 0.0344  278 THR A O   
2065 C CB  . THR A 289 ? 0.4997 0.4868 0.6182 -0.0255 -0.0393 0.0468  278 THR A CB  
2066 O OG1 . THR A 289 ? 0.5079 0.4997 0.6402 -0.0248 -0.0312 0.0543  278 THR A OG1 
2067 C CG2 . THR A 289 ? 0.5063 0.4917 0.6284 -0.0268 -0.0493 0.0439  278 THR A CG2 
2068 N N   . LEU A 290 ? 0.4761 0.4547 0.5652 -0.0254 -0.0432 0.0360  279 LEU A N   
2069 C CA  . LEU A 290 ? 0.4704 0.4445 0.5449 -0.0252 -0.0471 0.0291  279 LEU A CA  
2070 C C   . LEU A 290 ? 0.4709 0.4418 0.5545 -0.0264 -0.0521 0.0286  279 LEU A C   
2071 O O   . LEU A 290 ? 0.4748 0.4407 0.5548 -0.0271 -0.0592 0.0226  279 LEU A O   
2072 C CB  . LEU A 290 ? 0.4636 0.4387 0.5220 -0.0234 -0.0398 0.0283  279 LEU A CB  
2073 C CG  . LEU A 290 ? 0.4666 0.4379 0.5118 -0.0228 -0.0424 0.0221  279 LEU A CG  
2074 C CD1 . LEU A 290 ? 0.4718 0.4402 0.5072 -0.0226 -0.0471 0.0159  279 LEU A CD1 
2075 C CD2 . LEU A 290 ? 0.4646 0.4374 0.4985 -0.0216 -0.0357 0.0231  279 LEU A CD2 
2076 N N   . MET A 291 ? 0.4671 0.4405 0.5628 -0.0269 -0.0482 0.0351  280 MET A N   
2077 C CA  . MET A 291 ? 0.4662 0.4368 0.5731 -0.0281 -0.0523 0.0358  280 MET A CA  
2078 C C   . MET A 291 ? 0.4808 0.4489 0.6027 -0.0303 -0.0613 0.0349  280 MET A C   
2079 O O   . MET A 291 ? 0.4873 0.4501 0.6119 -0.0313 -0.0679 0.0307  280 MET A O   
2080 C CB  . MET A 291 ? 0.4555 0.4299 0.5724 -0.0281 -0.0456 0.0442  280 MET A CB  
2081 C CG  . MET A 291 ? 0.4820 0.4585 0.5841 -0.0264 -0.0376 0.0458  280 MET A CG  
2082 S SD  . MET A 291 ? 0.5313 0.5037 0.6207 -0.0257 -0.0398 0.0404  280 MET A SD  
2083 C CE  . MET A 291 ? 0.5314 0.5029 0.5998 -0.0242 -0.0395 0.0329  280 MET A CE  
2084 N N   . LYS A 292 ? 0.4868 0.4583 0.6194 -0.0310 -0.0615 0.0388  281 LYS A N   
2085 C CA  . LYS A 292 ? 0.5030 0.4725 0.6513 -0.0335 -0.0708 0.0388  281 LYS A CA  
2086 C C   . LYS A 292 ? 0.5237 0.4874 0.6598 -0.0341 -0.0800 0.0300  281 LYS A C   
2087 O O   . LYS A 292 ? 0.5282 0.4866 0.6704 -0.0362 -0.0892 0.0265  281 LYS A O   
2088 C CB  . LYS A 292 ? 0.5283 0.5039 0.6917 -0.0338 -0.0680 0.0460  281 LYS A CB  
2089 C CG  . LYS A 292 ? 0.5837 0.5583 0.7672 -0.0367 -0.0777 0.0477  281 LYS A CG  
2090 C CD  . LYS A 292 ? 0.6541 0.6347 0.8509 -0.0367 -0.0753 0.0540  281 LYS A CD  
2091 C CE  . LYS A 292 ? 0.7196 0.6987 0.9079 -0.0370 -0.0820 0.0494  281 LYS A CE  
2092 N NZ  . LYS A 292 ? 0.7670 0.7474 0.9347 -0.0341 -0.0744 0.0468  281 LYS A NZ  
2093 N N   . ASP A 293 ? 0.5349 0.4990 0.6528 -0.0324 -0.0774 0.0263  282 ASP A N   
2094 C CA  . ASP A 293 ? 0.5461 0.5048 0.6506 -0.0329 -0.0852 0.0186  282 ASP A CA  
2095 C C   . ASP A 293 ? 0.5613 0.5140 0.6485 -0.0318 -0.0860 0.0108  282 ASP A C   
2096 O O   . ASP A 293 ? 0.5742 0.5214 0.6499 -0.0323 -0.0924 0.0042  282 ASP A O   
2097 C CB  . ASP A 293 ? 0.5639 0.5259 0.6583 -0.0316 -0.0822 0.0189  282 ASP A CB  
2098 C CG  . ASP A 293 ? 0.6079 0.5752 0.7187 -0.0325 -0.0823 0.0257  282 ASP A CG  
2099 O OD1 . ASP A 293 ? 0.6054 0.5727 0.7349 -0.0347 -0.0883 0.0289  282 ASP A OD1 
2100 O OD2 . ASP A 293 ? 0.6413 0.6126 0.7471 -0.0309 -0.0766 0.0278  282 ASP A OD2 
2101 N N   . PHE A 294 ? 0.5608 0.5146 0.6447 -0.0303 -0.0791 0.0116  283 PHE A N   
2102 C CA  . PHE A 294 ? 0.5732 0.5221 0.6415 -0.0288 -0.0786 0.0048  283 PHE A CA  
2103 C C   . PHE A 294 ? 0.5908 0.5373 0.6660 -0.0287 -0.0777 0.0050  283 PHE A C   
2104 O O   . PHE A 294 ? 0.5914 0.5421 0.6787 -0.0289 -0.0735 0.0119  283 PHE A O   
2105 C CB  . PHE A 294 ? 0.5625 0.5149 0.6148 -0.0264 -0.0708 0.0045  283 PHE A CB  
2106 C CG  . PHE A 294 ? 0.5562 0.5095 0.5981 -0.0261 -0.0717 0.0026  283 PHE A CG  
2107 C CD1 . PHE A 294 ? 0.5539 0.5128 0.6018 -0.0263 -0.0688 0.0082  283 PHE A CD1 
2108 C CD2 . PHE A 294 ? 0.5628 0.5112 0.5889 -0.0255 -0.0749 -0.0044 283 PHE A CD2 
2109 C CE1 . PHE A 294 ? 0.5611 0.5207 0.6006 -0.0260 -0.0697 0.0069  283 PHE A CE1 
2110 C CE2 . PHE A 294 ? 0.5721 0.5214 0.5891 -0.0254 -0.0759 -0.0053 283 PHE A CE2 
2111 C CZ  . PHE A 294 ? 0.5651 0.5200 0.5893 -0.0256 -0.0736 0.0004  283 PHE A CZ  
2112 N N   . ARG A 295 ? 0.6032 0.5429 0.6697 -0.0281 -0.0809 -0.0024 284 ARG A N   
2113 C CA  . ARG A 295 ? 0.6183 0.5550 0.6904 -0.0275 -0.0799 -0.0030 284 ARG A CA  
2114 C C   . ARG A 295 ? 0.6203 0.5552 0.6761 -0.0249 -0.0755 -0.0080 284 ARG A C   
2115 O O   . ARG A 295 ? 0.6250 0.5555 0.6668 -0.0242 -0.0775 -0.0150 284 ARG A O   
2116 C CB  . ARG A 295 ? 0.6578 0.5866 0.7390 -0.0294 -0.0885 -0.0075 284 ARG A CB  
2117 C CG  . ARG A 295 ? 0.7353 0.6663 0.8385 -0.0319 -0.0917 -0.0008 284 ARG A CG  
2118 C CD  . ARG A 295 ? 0.8278 0.7505 0.9412 -0.0336 -0.0997 -0.0051 284 ARG A CD  
2119 N NE  . ARG A 295 ? 0.9260 0.8419 1.0332 -0.0354 -0.1088 -0.0121 284 ARG A NE  
2120 C CZ  . ARG A 295 ? 0.9901 0.9057 1.1105 -0.0385 -0.1165 -0.0098 284 ARG A CZ  
2121 N NH1 . ARG A 295 ? 0.9863 0.9082 1.1279 -0.0399 -0.1152 -0.0006 284 ARG A NH1 
2122 N NH2 . ARG A 295 ? 1.0117 0.9207 1.1243 -0.0402 -0.1255 -0.0164 284 ARG A NH2 
2123 N N   . ARG A 296 ? 0.6159 0.5544 0.6741 -0.0237 -0.0695 -0.0039 285 ARG A N   
2124 C CA  . ARG A 296 ? 0.6296 0.5674 0.6763 -0.0213 -0.0651 -0.0069 285 ARG A CA  
2125 C C   . ARG A 296 ? 0.6394 0.5690 0.6789 -0.0202 -0.0682 -0.0161 285 ARG A C   
2126 O O   . ARG A 296 ? 0.6430 0.5714 0.6677 -0.0185 -0.0658 -0.0208 285 ARG A O   
2127 C CB  . ARG A 296 ? 0.6413 0.5826 0.6973 -0.0208 -0.0610 -0.0005 285 ARG A CB  
2128 C CG  . ARG A 296 ? 0.6844 0.6232 0.7361 -0.0187 -0.0586 -0.0037 285 ARG A CG  
2129 C CD  . ARG A 296 ? 0.7203 0.6633 0.7803 -0.0184 -0.0550 0.0038  285 ARG A CD  
2130 N NE  . ARG A 296 ? 0.7473 0.6973 0.8068 -0.0195 -0.0514 0.0115  285 ARG A NE  
2131 C CZ  . ARG A 296 ? 0.7614 0.7156 0.8082 -0.0189 -0.0474 0.0123  285 ARG A CZ  
2132 N NH1 . ARG A 296 ? 0.7507 0.7035 0.7852 -0.0173 -0.0466 0.0065  285 ARG A NH1 
2133 N NH2 . ARG A 296 ? 0.7502 0.7096 0.7966 -0.0198 -0.0440 0.0187  285 ARG A NH2 
2134 N N   . ASN A 297 ? 0.6369 0.5602 0.6871 -0.0210 -0.0731 -0.0187 286 ASN A N   
2135 C CA  . ASN A 297 ? 0.6460 0.5600 0.6907 -0.0199 -0.0757 -0.0277 286 ASN A CA  
2136 C C   . ASN A 297 ? 0.6395 0.5484 0.6671 -0.0198 -0.0788 -0.0354 286 ASN A C   
2137 O O   . ASN A 297 ? 0.6550 0.5573 0.6725 -0.0180 -0.0780 -0.0429 286 ASN A O   
2138 C CB  . ASN A 297 ? 0.6741 0.5819 0.7345 -0.0214 -0.0812 -0.0286 286 ASN A CB  
2139 C CG  . ASN A 297 ? 0.7382 0.6350 0.7924 -0.0204 -0.0841 -0.0389 286 ASN A CG  
2140 O OD1 . ASN A 297 ? 0.7590 0.6488 0.8078 -0.0219 -0.0907 -0.0450 286 ASN A OD1 
2141 N ND2 . ASN A 297 ? 0.7520 0.6469 0.8052 -0.0176 -0.0791 -0.0410 286 ASN A ND2 
2142 N N   . THR A 298 ? 0.6145 0.5265 0.6391 -0.0216 -0.0819 -0.0334 287 THR A N   
2143 C CA  . THR A 298 ? 0.6060 0.5137 0.6139 -0.0217 -0.0851 -0.0396 287 THR A CA  
2144 C C   . THR A 298 ? 0.5978 0.5067 0.5886 -0.0188 -0.0781 -0.0425 287 THR A C   
2145 O O   . THR A 298 ? 0.6095 0.5121 0.5853 -0.0178 -0.0789 -0.0496 287 THR A O   
2146 C CB  . THR A 298 ? 0.6176 0.5310 0.6275 -0.0237 -0.0878 -0.0344 287 THR A CB  
2147 O OG1 . THR A 298 ? 0.6199 0.5344 0.6486 -0.0263 -0.0927 -0.0297 287 THR A OG1 
2148 C CG2 . THR A 298 ? 0.6269 0.5363 0.6209 -0.0243 -0.0923 -0.0395 287 THR A CG2 
2149 N N   . TYR A 299 ? 0.5731 0.4898 0.5665 -0.0174 -0.0711 -0.0367 288 TYR A N   
2150 C CA  . TYR A 299 ? 0.5528 0.4723 0.5335 -0.0150 -0.0645 -0.0377 288 TYR A CA  
2151 C C   . TYR A 299 ? 0.5587 0.4778 0.5432 -0.0128 -0.0595 -0.0381 288 TYR A C   
2152 O O   . TYR A 299 ? 0.5612 0.4854 0.5420 -0.0113 -0.0537 -0.0356 288 TYR A O   
2153 C CB  . TYR A 299 ? 0.5276 0.4562 0.5085 -0.0155 -0.0611 -0.0306 288 TYR A CB  
2154 C CG  . TYR A 299 ? 0.5090 0.4390 0.4906 -0.0177 -0.0657 -0.0286 288 TYR A CG  
2155 C CD1 . TYR A 299 ? 0.5107 0.4378 0.4794 -0.0178 -0.0684 -0.0326 288 TYR A CD1 
2156 C CD2 . TYR A 299 ? 0.5036 0.4374 0.4999 -0.0196 -0.0676 -0.0225 288 TYR A CD2 
2157 C CE1 . TYR A 299 ? 0.5170 0.4453 0.4879 -0.0199 -0.0734 -0.0304 288 TYR A CE1 
2158 C CE2 . TYR A 299 ? 0.5006 0.4358 0.4999 -0.0215 -0.0719 -0.0204 288 TYR A CE2 
2159 C CZ  . TYR A 299 ? 0.5154 0.4480 0.5023 -0.0216 -0.0750 -0.0242 288 TYR A CZ  
2160 O OH  . TYR A 299 ? 0.5344 0.4685 0.5253 -0.0235 -0.0798 -0.0218 288 TYR A OH  
2161 N N   . THR A 300 ? 0.5623 0.4751 0.5550 -0.0126 -0.0619 -0.0414 289 THR A N   
2162 C CA  . THR A 300 ? 0.5661 0.4783 0.5656 -0.0105 -0.0577 -0.0412 289 THR A CA  
2163 C C   . THR A 300 ? 0.5654 0.4757 0.5524 -0.0074 -0.0520 -0.0462 289 THR A C   
2164 O O   . THR A 300 ? 0.5677 0.4826 0.5587 -0.0058 -0.0469 -0.0427 289 THR A O   
2165 C CB  . THR A 300 ? 0.5829 0.4880 0.5950 -0.0111 -0.0620 -0.0438 289 THR A CB  
2166 O OG1 . THR A 300 ? 0.5980 0.5046 0.6210 -0.0094 -0.0581 -0.0408 289 THR A OG1 
2167 C CG2 . THR A 300 ? 0.5961 0.4902 0.5989 -0.0105 -0.0652 -0.0540 289 THR A CG2 
2168 N N   . ASN A 301 ? 0.5616 0.4657 0.5339 -0.0067 -0.0528 -0.0535 290 ASN A N   
2169 C CA  . ASN A 301 ? 0.5672 0.4697 0.5277 -0.0037 -0.0465 -0.0578 290 ASN A CA  
2170 C C   . ASN A 301 ? 0.5510 0.4598 0.4994 -0.0038 -0.0438 -0.0551 290 ASN A C   
2171 O O   . ASN A 301 ? 0.5591 0.4653 0.4942 -0.0020 -0.0402 -0.0594 290 ASN A O   
2172 C CB  . ASN A 301 ? 0.6017 0.4926 0.5512 -0.0026 -0.0479 -0.0678 290 ASN A CB  
2173 C CG  . ASN A 301 ? 0.6647 0.5481 0.6253 -0.0018 -0.0493 -0.0716 290 ASN A CG  
2174 O OD1 . ASN A 301 ? 0.6713 0.5574 0.6453 -0.0003 -0.0456 -0.0684 290 ASN A OD1 
2175 N ND2 . ASN A 301 ? 0.6928 0.5663 0.6485 -0.0031 -0.0552 -0.0785 290 ASN A ND2 
2176 N N   . CYS A 302 ? 0.5237 0.4402 0.4768 -0.0059 -0.0453 -0.0481 291 CYS A N   
2177 C CA  . CYS A 302 ? 0.5051 0.4271 0.4483 -0.0062 -0.0433 -0.0454 291 CYS A CA  
2178 C C   . CYS A 302 ? 0.4868 0.4167 0.4348 -0.0055 -0.0381 -0.0396 291 CYS A C   
2179 O O   . CYS A 302 ? 0.4754 0.4092 0.4352 -0.0064 -0.0386 -0.0344 291 CYS A O   
2180 C CB  . CYS A 302 ? 0.5002 0.4242 0.4441 -0.0090 -0.0487 -0.0426 291 CYS A CB  
2181 S SG  . CYS A 302 ? 0.5187 0.4335 0.4549 -0.0104 -0.0563 -0.0492 291 CYS A SG  
2182 N N   . SER A 303 ? 0.4840 0.4161 0.4228 -0.0040 -0.0334 -0.0402 292 SER A N   
2183 C CA  . SER A 303 ? 0.4832 0.4226 0.4253 -0.0037 -0.0291 -0.0348 292 SER A CA  
2184 C C   . SER A 303 ? 0.4828 0.4243 0.4132 -0.0029 -0.0256 -0.0353 292 SER A C   
2185 O O   . SER A 303 ? 0.4989 0.4358 0.4187 -0.0019 -0.0249 -0.0402 292 SER A O   
2186 C CB  . SER A 303 ? 0.4921 0.4318 0.4440 -0.0019 -0.0262 -0.0340 292 SER A CB  
2187 O OG  . SER A 303 ? 0.5330 0.4687 0.4797 0.0008  -0.0220 -0.0391 292 SER A OG  
2188 N N   . LEU A 304 ? 0.4632 0.4114 0.3951 -0.0037 -0.0235 -0.0302 293 LEU A N   
2189 C CA  . LEU A 304 ? 0.4564 0.4070 0.3794 -0.0031 -0.0200 -0.0299 293 LEU A CA  
2190 C C   . LEU A 304 ? 0.4635 0.4120 0.3841 -0.0004 -0.0151 -0.0332 293 LEU A C   
2191 O O   . LEU A 304 ? 0.4617 0.4083 0.3719 0.0006  -0.0128 -0.0359 293 LEU A O   
2192 C CB  . LEU A 304 ? 0.4483 0.4056 0.3750 -0.0045 -0.0191 -0.0241 293 LEU A CB  
2193 C CG  . LEU A 304 ? 0.4594 0.4195 0.3784 -0.0046 -0.0163 -0.0232 293 LEU A CG  
2194 C CD1 . LEU A 304 ? 0.4617 0.4200 0.3718 -0.0054 -0.0183 -0.0247 293 LEU A CD1 
2195 C CD2 . LEU A 304 ? 0.4573 0.4228 0.3801 -0.0061 -0.0158 -0.0182 293 LEU A CD2 
2196 N N   . ILE A 305 ? 0.4722 0.4205 0.4028 0.0009  -0.0135 -0.0330 294 ILE A N   
2197 C CA  . ILE A 305 ? 0.4928 0.4388 0.4241 0.0039  -0.0082 -0.0360 294 ILE A CA  
2198 C C   . ILE A 305 ? 0.5133 0.4514 0.4329 0.0055  -0.0071 -0.0431 294 ILE A C   
2199 O O   . ILE A 305 ? 0.5170 0.4540 0.4279 0.0072  -0.0023 -0.0452 294 ILE A O   
2200 C CB  . ILE A 305 ? 0.5010 0.4472 0.4472 0.0049  -0.0079 -0.0345 294 ILE A CB  
2201 C CG1 . ILE A 305 ? 0.5094 0.4634 0.4651 0.0037  -0.0079 -0.0274 294 ILE A CG1 
2202 C CG2 . ILE A 305 ? 0.5143 0.4556 0.4623 0.0084  -0.0026 -0.0393 294 ILE A CG2 
2203 C CD1 . ILE A 305 ? 0.5156 0.4706 0.4852 0.0037  -0.0097 -0.0243 294 ILE A CD1 
2204 N N   . LYS A 306 ? 0.5212 0.4536 0.4401 0.0047  -0.0119 -0.0466 295 LYS A N   
2205 C CA  . LYS A 306 ? 0.5377 0.4614 0.4445 0.0058  -0.0121 -0.0538 295 LYS A CA  
2206 C C   . LYS A 306 ? 0.5328 0.4563 0.4245 0.0048  -0.0131 -0.0542 295 LYS A C   
2207 O O   . LYS A 306 ? 0.5390 0.4580 0.4183 0.0065  -0.0094 -0.0583 295 LYS A O   
2208 C CB  . LYS A 306 ? 0.5836 0.5012 0.4948 0.0047  -0.0180 -0.0570 295 LYS A CB  
2209 C CG  . LYS A 306 ? 0.6682 0.5843 0.5936 0.0064  -0.0160 -0.0575 295 LYS A CG  
2210 C CD  . LYS A 306 ? 0.7504 0.6598 0.6813 0.0053  -0.0218 -0.0609 295 LYS A CD  
2211 C CE  . LYS A 306 ? 0.8176 0.7165 0.7343 0.0058  -0.0235 -0.0694 295 LYS A CE  
2212 N NZ  . LYS A 306 ? 0.8559 0.7471 0.7803 0.0055  -0.0278 -0.0738 295 LYS A NZ  
2213 N N   . TYR A 307 ? 0.5208 0.4495 0.4137 0.0021  -0.0172 -0.0495 296 TYR A N   
2214 C CA  . TYR A 307 ? 0.5167 0.4460 0.3973 0.0011  -0.0184 -0.0489 296 TYR A CA  
2215 C C   . TYR A 307 ? 0.5213 0.4531 0.3952 0.0029  -0.0114 -0.0479 296 TYR A C   
2216 O O   . TYR A 307 ? 0.5278 0.4554 0.3880 0.0038  -0.0099 -0.0510 296 TYR A O   
2217 C CB  . TYR A 307 ? 0.4986 0.4335 0.3844 -0.0018 -0.0230 -0.0435 296 TYR A CB  
2218 C CG  . TYR A 307 ? 0.4947 0.4306 0.3697 -0.0026 -0.0238 -0.0422 296 TYR A CG  
2219 C CD1 . TYR A 307 ? 0.4958 0.4265 0.3614 -0.0036 -0.0289 -0.0450 296 TYR A CD1 
2220 C CD2 . TYR A 307 ? 0.4964 0.4378 0.3703 -0.0024 -0.0196 -0.0384 296 TYR A CD2 
2221 C CE1 . TYR A 307 ? 0.5030 0.4344 0.3588 -0.0043 -0.0298 -0.0434 296 TYR A CE1 
2222 C CE2 . TYR A 307 ? 0.5017 0.4436 0.3661 -0.0030 -0.0200 -0.0371 296 TYR A CE2 
2223 C CZ  . TYR A 307 ? 0.5123 0.4494 0.3679 -0.0039 -0.0251 -0.0393 296 TYR A CZ  
2224 O OH  . TYR A 307 ? 0.5274 0.4655 0.3749 -0.0046 -0.0259 -0.0370 296 TYR A OH  
2225 N N   . MET A 308 ? 0.5185 0.4572 0.4021 0.0032  -0.0077 -0.0433 297 MET A N   
2226 C CA  . MET A 308 ? 0.5368 0.4788 0.4174 0.0046  -0.0015 -0.0414 297 MET A CA  
2227 C C   . MET A 308 ? 0.5586 0.4958 0.4347 0.0078  0.0049  -0.0459 297 MET A C   
2228 O O   . MET A 308 ? 0.5589 0.4961 0.4267 0.0091  0.0098  -0.0458 297 MET A O   
2229 C CB  . MET A 308 ? 0.5346 0.4845 0.4276 0.0037  -0.0002 -0.0356 297 MET A CB  
2230 C CG  . MET A 308 ? 0.5529 0.5071 0.4474 0.0008  -0.0048 -0.0314 297 MET A CG  
2231 S SD  . MET A 308 ? 0.6095 0.5634 0.4912 -0.0004 -0.0061 -0.0307 297 MET A SD  
2232 C CE  . MET A 308 ? 0.6004 0.5581 0.4812 0.0007  0.0002  -0.0282 297 MET A CE  
2233 N N   . GLU A 309 ? 0.5720 0.5045 0.4535 0.0093  0.0050  -0.0498 298 GLU A N   
2234 C CA  . GLU A 309 ? 0.5897 0.5162 0.4671 0.0127  0.0115  -0.0549 298 GLU A CA  
2235 C C   . GLU A 309 ? 0.6059 0.5249 0.4633 0.0132  0.0116  -0.0602 298 GLU A C   
2236 O O   . GLU A 309 ? 0.6159 0.5326 0.4645 0.0156  0.0187  -0.0619 298 GLU A O   
2237 C CB  . GLU A 309 ? 0.6218 0.5440 0.5093 0.0138  0.0105  -0.0583 298 GLU A CB  
2238 C CG  . GLU A 309 ? 0.6716 0.5990 0.5765 0.0156  0.0151  -0.0547 298 GLU A CG  
2239 C CD  . GLU A 309 ? 0.7566 0.6804 0.6740 0.0166  0.0138  -0.0568 298 GLU A CD  
2240 O OE1 . GLU A 309 ? 0.7776 0.6948 0.6909 0.0157  0.0088  -0.0612 298 GLU A OE1 
2241 O OE2 . GLU A 309 ? 0.7798 0.7075 0.7120 0.0182  0.0175  -0.0537 298 GLU A OE2 
2242 N N   . LYS A 310 ? 0.6078 0.5229 0.4580 0.0107  0.0036  -0.0621 299 LYS A N   
2243 C CA  . LYS A 310 ? 0.6234 0.5310 0.4537 0.0104  0.0017  -0.0666 299 LYS A CA  
2244 C C   . LYS A 310 ? 0.6319 0.5434 0.4522 0.0104  0.0052  -0.0628 299 LYS A C   
2245 O O   . LYS A 310 ? 0.6403 0.5463 0.4441 0.0118  0.0086  -0.0659 299 LYS A O   
2246 C CB  . LYS A 310 ? 0.6465 0.5512 0.4747 0.0072  -0.0087 -0.0676 299 LYS A CB  
2247 C CG  . LYS A 310 ? 0.7094 0.6098 0.5477 0.0069  -0.0127 -0.0711 299 LYS A CG  
2248 C CD  . LYS A 310 ? 0.7774 0.6738 0.6128 0.0037  -0.0230 -0.0726 299 LYS A CD  
2249 C CE  . LYS A 310 ? 0.8241 0.7175 0.6726 0.0030  -0.0273 -0.0748 299 LYS A CE  
2250 N NZ  . LYS A 310 ? 0.8669 0.7526 0.7143 0.0060  -0.0223 -0.0814 299 LYS A NZ  
2251 N N   . HIS A 311 ? 0.6235 0.5442 0.4536 0.0089  0.0045  -0.0559 300 HIS A N   
2252 C CA  . HIS A 311 ? 0.6322 0.5571 0.4559 0.0086  0.0075  -0.0516 300 HIS A CA  
2253 C C   . HIS A 311 ? 0.6521 0.5815 0.4814 0.0110  0.0168  -0.0490 300 HIS A C   
2254 O O   . HIS A 311 ? 0.6638 0.5986 0.4935 0.0104  0.0190  -0.0441 300 HIS A O   
2255 C CB  . HIS A 311 ? 0.6218 0.5529 0.4516 0.0055  0.0014  -0.0462 300 HIS A CB  
2256 C CG  . HIS A 311 ? 0.6325 0.5593 0.4559 0.0033  -0.0070 -0.0481 300 HIS A CG  
2257 N ND1 . HIS A 311 ? 0.6528 0.5759 0.4609 0.0026  -0.0094 -0.0487 300 HIS A ND1 
2258 C CD2 . HIS A 311 ? 0.6462 0.5719 0.4772 0.0017  -0.0135 -0.0493 300 HIS A CD2 
2259 C CE1 . HIS A 311 ? 0.6619 0.5818 0.4693 0.0005  -0.0178 -0.0501 300 HIS A CE1 
2260 N NE2 . HIS A 311 ? 0.6612 0.5827 0.4827 -0.0001 -0.0203 -0.0505 300 HIS A NE2 
2261 N N   . LYS A 312 ? 0.6555 0.5824 0.4901 0.0137  0.0223  -0.0522 301 LYS A N   
2262 C CA  . LYS A 312 ? 0.6630 0.5932 0.5046 0.0165  0.0316  -0.0504 301 LYS A CA  
2263 C C   . LYS A 312 ? 0.6534 0.5936 0.5119 0.0153  0.0319  -0.0433 301 LYS A C   
2264 O O   . LYS A 312 ? 0.6595 0.6037 0.5219 0.0166  0.0386  -0.0400 301 LYS A O   
2265 C CB  . LYS A 312 ? 0.7016 0.6285 0.5272 0.0184  0.0387  -0.0513 301 LYS A CB  
2266 C CG  . LYS A 312 ? 0.7813 0.6975 0.5930 0.0211  0.0421  -0.0592 301 LYS A CG  
2267 C CD  . LYS A 312 ? 0.8752 0.7857 0.6641 0.0218  0.0452  -0.0609 301 LYS A CD  
2268 C CE  . LYS A 312 ? 0.9514 0.8505 0.7253 0.0246  0.0496  -0.0692 301 LYS A CE  
2269 N NZ  . LYS A 312 ? 1.0075 0.8998 0.7559 0.0246  0.0504  -0.0711 301 LYS A NZ  
2270 N N   . VAL A 313 ? 0.6371 0.5808 0.5062 0.0128  0.0251  -0.0411 302 VAL A N   
2271 C CA  . VAL A 313 ? 0.6239 0.5760 0.5077 0.0113  0.0244  -0.0350 302 VAL A CA  
2272 C C   . VAL A 313 ? 0.6226 0.5755 0.5212 0.0123  0.0246  -0.0352 302 VAL A C   
2273 O O   . VAL A 313 ? 0.6271 0.5765 0.5270 0.0118  0.0201  -0.0380 302 VAL A O   
2274 C CB  . VAL A 313 ? 0.6227 0.5781 0.5061 0.0077  0.0171  -0.0319 302 VAL A CB  
2275 C CG1 . VAL A 313 ? 0.6155 0.5777 0.5133 0.0060  0.0152  -0.0268 302 VAL A CG1 
2276 C CG2 . VAL A 313 ? 0.6252 0.5808 0.4969 0.0069  0.0176  -0.0304 302 VAL A CG2 
2277 N N   . LYS A 314 ? 0.6165 0.5738 0.5272 0.0139  0.0299  -0.0321 303 LYS A N   
2278 C CA  . LYS A 314 ? 0.6167 0.5749 0.5427 0.0152  0.0304  -0.0318 303 LYS A CA  
2279 C C   . LYS A 314 ? 0.6071 0.5695 0.5437 0.0122  0.0228  -0.0278 303 LYS A C   
2280 O O   . LYS A 314 ? 0.5999 0.5683 0.5407 0.0097  0.0201  -0.0228 303 LYS A O   
2281 C CB  . LYS A 314 ? 0.6464 0.6082 0.5839 0.0177  0.0381  -0.0291 303 LYS A CB  
2282 C CG  . LYS A 314 ? 0.7183 0.6746 0.6460 0.0214  0.0470  -0.0336 303 LYS A CG  
2283 C CD  . LYS A 314 ? 0.7823 0.7419 0.7240 0.0246  0.0557  -0.0311 303 LYS A CD  
2284 C CE  . LYS A 314 ? 0.8477 0.8008 0.7781 0.0286  0.0656  -0.0361 303 LYS A CE  
2285 N NZ  . LYS A 314 ? 0.8755 0.8296 0.8214 0.0325  0.0746  -0.0354 303 LYS A NZ  
2286 N N   . PRO A 315 ? 0.6006 0.5596 0.5415 0.0124  0.0196  -0.0302 304 PRO A N   
2287 C CA  . PRO A 315 ? 0.5867 0.5492 0.5368 0.0097  0.0129  -0.0261 304 PRO A CA  
2288 C C   . PRO A 315 ? 0.5634 0.5325 0.5291 0.0093  0.0130  -0.0200 304 PRO A C   
2289 O O   . PRO A 315 ? 0.5653 0.5382 0.5357 0.0065  0.0076  -0.0157 304 PRO A O   
2290 C CB  . PRO A 315 ? 0.6009 0.5577 0.5533 0.0106  0.0106  -0.0299 304 PRO A CB  
2291 C CG  . PRO A 315 ? 0.6164 0.5657 0.5561 0.0128  0.0142  -0.0369 304 PRO A CG  
2292 C CD  . PRO A 315 ? 0.5977 0.5486 0.5342 0.0149  0.0216  -0.0367 304 PRO A CD  
2293 N N   . ASP A 316 ? 0.5436 0.5141 0.5173 0.0120  0.0192  -0.0195 305 ASP A N   
2294 C CA  . ASP A 316 ? 0.5269 0.5039 0.5170 0.0115  0.0188  -0.0133 305 ASP A CA  
2295 C C   . ASP A 316 ? 0.4869 0.4696 0.4758 0.0094  0.0187  -0.0091 305 ASP A C   
2296 O O   . ASP A 316 ? 0.4807 0.4689 0.4822 0.0082  0.0170  -0.0036 305 ASP A O   
2297 C CB  . ASP A 316 ? 0.5698 0.5461 0.5737 0.0153  0.0249  -0.0137 305 ASP A CB  
2298 C CG  . ASP A 316 ? 0.7117 0.6830 0.7075 0.0190  0.0337  -0.0194 305 ASP A CG  
2299 O OD1 . ASP A 316 ? 0.7450 0.7089 0.7283 0.0201  0.0342  -0.0258 305 ASP A OD1 
2300 O OD2 . ASP A 316 ? 0.7625 0.7370 0.7643 0.0209  0.0403  -0.0173 305 ASP A OD2 
2301 N N   . SER A 317 ? 0.4578 0.4389 0.4322 0.0087  0.0198  -0.0113 306 SER A N   
2302 C CA  . SER A 317 ? 0.4354 0.4210 0.4084 0.0067  0.0197  -0.0077 306 SER A CA  
2303 C C   . SER A 317 ? 0.4183 0.4067 0.3907 0.0026  0.0120  -0.0043 306 SER A C   
2304 O O   . SER A 317 ? 0.4195 0.4056 0.3868 0.0013  0.0074  -0.0056 306 SER A O   
2305 C CB  . SER A 317 ? 0.4472 0.4297 0.4048 0.0074  0.0234  -0.0110 306 SER A CB  
2306 O OG  . SER A 317 ? 0.4741 0.4527 0.4194 0.0059  0.0188  -0.0141 306 SER A OG  
2307 N N   . LYS A 318 ? 0.3970 0.3901 0.3742 0.0005  0.0108  -0.0001 307 LYS A N   
2308 C CA  . LYS A 318 ? 0.3862 0.3811 0.3607 -0.0034 0.0043  0.0027  307 LYS A CA  
2309 C C   . LYS A 318 ? 0.3856 0.3771 0.3445 -0.0045 0.0032  -0.0004 307 LYS A C   
2310 O O   . LYS A 318 ? 0.3882 0.3790 0.3424 -0.0069 -0.0017 0.0000  307 LYS A O   
2311 C CB  . LYS A 318 ? 0.3927 0.3923 0.3755 -0.0052 0.0036  0.0072  307 LYS A CB  
2312 C CG  . LYS A 318 ? 0.4345 0.4380 0.4349 -0.0045 0.0037  0.0112  307 LYS A CG  
2313 C CD  . LYS A 318 ? 0.4937 0.5016 0.5021 -0.0080 -0.0016 0.0163  307 LYS A CD  
2314 C CE  . LYS A 318 ? 0.5281 0.5398 0.5540 -0.0080 -0.0041 0.0211  307 LYS A CE  
2315 N NZ  . LYS A 318 ? 0.5600 0.5759 0.6006 -0.0064 0.0009  0.0240  307 LYS A NZ  
2316 N N   . ALA A 319 ? 0.3766 0.3661 0.3276 -0.0027 0.0080  -0.0032 308 ALA A N   
2317 C CA  . ALA A 319 ? 0.3716 0.3579 0.3091 -0.0034 0.0071  -0.0058 308 ALA A CA  
2318 C C   . ALA A 319 ? 0.3790 0.3617 0.3121 -0.0034 0.0037  -0.0086 308 ALA A C   
2319 O O   . ALA A 319 ? 0.3903 0.3726 0.3188 -0.0055 -0.0002 -0.0082 308 ALA A O   
2320 C CB  . ALA A 319 ? 0.3591 0.3432 0.2890 -0.0011 0.0127  -0.0081 308 ALA A CB  
2321 N N   . PHE A 320 ? 0.3689 0.3493 0.3053 -0.0010 0.0053  -0.0110 309 PHE A N   
2322 C CA  . PHE A 320 ? 0.3709 0.3477 0.3050 -0.0010 0.0020  -0.0135 309 PHE A CA  
2323 C C   . PHE A 320 ? 0.3768 0.3559 0.3167 -0.0035 -0.0031 -0.0101 309 PHE A C   
2324 O O   . PHE A 320 ? 0.3828 0.3605 0.3176 -0.0050 -0.0063 -0.0105 309 PHE A O   
2325 C CB  . PHE A 320 ? 0.3639 0.3372 0.3013 0.0019  0.0048  -0.0169 309 PHE A CB  
2326 C CG  . PHE A 320 ? 0.3723 0.3416 0.3083 0.0015  0.0008  -0.0194 309 PHE A CG  
2327 C CD1 . PHE A 320 ? 0.3859 0.3505 0.3111 0.0017  -0.0003 -0.0235 309 PHE A CD1 
2328 C CD2 . PHE A 320 ? 0.3698 0.3403 0.3157 0.0007  -0.0024 -0.0169 309 PHE A CD2 
2329 C CE1 . PHE A 320 ? 0.3896 0.3509 0.3151 0.0010  -0.0044 -0.0252 309 PHE A CE1 
2330 C CE2 . PHE A 320 ? 0.3779 0.3453 0.3236 0.0001  -0.0061 -0.0184 309 PHE A CE2 
2331 C CZ  . PHE A 320 ? 0.3851 0.3480 0.3213 0.0002  -0.0071 -0.0225 309 PHE A CZ  
2332 N N   . HIS A 321 ? 0.3686 0.3512 0.3191 -0.0039 -0.0038 -0.0064 310 HIS A N   
2333 C CA  . HIS A 321 ? 0.3749 0.3594 0.3297 -0.0064 -0.0087 -0.0027 310 HIS A CA  
2334 C C   . HIS A 321 ? 0.3819 0.3671 0.3285 -0.0093 -0.0113 -0.0014 310 HIS A C   
2335 O O   . HIS A 321 ? 0.3941 0.3784 0.3383 -0.0107 -0.0144 -0.0005 310 HIS A O   
2336 C CB  . HIS A 321 ? 0.3747 0.3630 0.3423 -0.0065 -0.0096 0.0015  310 HIS A CB  
2337 C CG  . HIS A 321 ? 0.3981 0.3851 0.3753 -0.0038 -0.0078 0.0007  310 HIS A CG  
2338 N ND1 . HIS A 321 ? 0.4177 0.4044 0.4014 -0.0044 -0.0114 0.0029  310 HIS A ND1 
2339 C CD2 . HIS A 321 ? 0.4117 0.3971 0.3924 -0.0005 -0.0023 -0.0024 310 HIS A CD2 
2340 C CE1 . HIS A 321 ? 0.4219 0.4069 0.4140 -0.0014 -0.0083 0.0011  310 HIS A CE1 
2341 N NE2 . HIS A 321 ? 0.4184 0.4022 0.4085 0.0011  -0.0026 -0.0024 310 HIS A NE2 
2342 N N   . LEU A 322 ? 0.3742 0.3604 0.3163 -0.0098 -0.0096 -0.0017 311 LEU A N   
2343 C CA  . LEU A 322 ? 0.3765 0.3624 0.3108 -0.0122 -0.0114 -0.0012 311 LEU A CA  
2344 C C   . LEU A 322 ? 0.3820 0.3647 0.3081 -0.0117 -0.0111 -0.0040 311 LEU A C   
2345 O O   . LEU A 322 ? 0.3891 0.3710 0.3118 -0.0133 -0.0133 -0.0033 311 LEU A O   
2346 C CB  . LEU A 322 ? 0.3724 0.3600 0.3057 -0.0129 -0.0098 -0.0004 311 LEU A CB  
2347 C CG  . LEU A 322 ? 0.3812 0.3677 0.3071 -0.0153 -0.0114 -0.0002 311 LEU A CG  
2348 C CD1 . LEU A 322 ? 0.3873 0.3738 0.3127 -0.0179 -0.0156 0.0019  311 LEU A CD1 
2349 C CD2 . LEU A 322 ? 0.3795 0.3673 0.3059 -0.0160 -0.0098 0.0006  311 LEU A CD2 
2350 N N   . LEU A 323 ? 0.3719 0.3525 0.2951 -0.0095 -0.0086 -0.0071 312 LEU A N   
2351 C CA  . LEU A 323 ? 0.3729 0.3505 0.2897 -0.0092 -0.0094 -0.0096 312 LEU A CA  
2352 C C   . LEU A 323 ? 0.3914 0.3679 0.3113 -0.0099 -0.0124 -0.0091 312 LEU A C   
2353 O O   . LEU A 323 ? 0.4055 0.3813 0.3224 -0.0110 -0.0140 -0.0087 312 LEU A O   
2354 C CB  . LEU A 323 ? 0.3643 0.3391 0.2772 -0.0069 -0.0070 -0.0131 312 LEU A CB  
2355 C CG  . LEU A 323 ? 0.3748 0.3461 0.2814 -0.0068 -0.0090 -0.0156 312 LEU A CG  
2356 C CD1 . LEU A 323 ? 0.3731 0.3451 0.2745 -0.0082 -0.0098 -0.0143 312 LEU A CD1 
2357 C CD2 . LEU A 323 ? 0.3817 0.3492 0.2829 -0.0046 -0.0072 -0.0194 312 LEU A CD2 
2358 N N   . GLN A 324 ? 0.3870 0.3637 0.3140 -0.0091 -0.0129 -0.0087 313 GLN A N   
2359 C CA  . GLN A 324 ? 0.3870 0.3627 0.3185 -0.0096 -0.0155 -0.0076 313 GLN A CA  
2360 C C   . GLN A 324 ? 0.3769 0.3547 0.3084 -0.0120 -0.0175 -0.0036 313 GLN A C   
2361 O O   . GLN A 324 ? 0.3862 0.3631 0.3180 -0.0128 -0.0190 -0.0026 313 GLN A O   
2362 C CB  . GLN A 324 ? 0.4170 0.3923 0.3572 -0.0080 -0.0153 -0.0078 313 GLN A CB  
2363 C CG  . GLN A 324 ? 0.4966 0.4705 0.4426 -0.0083 -0.0179 -0.0067 313 GLN A CG  
2364 C CD  . GLN A 324 ? 0.5994 0.5712 0.5531 -0.0062 -0.0171 -0.0085 313 GLN A CD  
2365 O OE1 . GLN A 324 ? 0.6377 0.6053 0.5908 -0.0050 -0.0173 -0.0124 313 GLN A OE1 
2366 N NE2 . GLN A 324 ? 0.6001 0.5745 0.5616 -0.0056 -0.0163 -0.0059 313 GLN A NE2 
2367 N N   . LYS A 325 ? 0.3662 0.3464 0.2970 -0.0133 -0.0175 -0.0014 314 LYS A N   
2368 C CA  . LYS A 325 ? 0.3731 0.3541 0.3009 -0.0157 -0.0193 0.0018  314 LYS A CA  
2369 C C   . LYS A 325 ? 0.3967 0.3762 0.3166 -0.0165 -0.0181 0.0005  314 LYS A C   
2370 O O   . LYS A 325 ? 0.4194 0.3983 0.3365 -0.0179 -0.0186 0.0023  314 LYS A O   
2371 C CB  . LYS A 325 ? 0.3698 0.3531 0.2992 -0.0171 -0.0205 0.0042  314 LYS A CB  
2372 C CG  . LYS A 325 ? 0.3587 0.3438 0.2979 -0.0164 -0.0220 0.0065  314 LYS A CG  
2373 C CD  . LYS A 325 ? 0.3662 0.3539 0.3089 -0.0180 -0.0242 0.0096  314 LYS A CD  
2374 C CE  . LYS A 325 ? 0.3786 0.3682 0.3331 -0.0170 -0.0255 0.0122  314 LYS A CE  
2375 N NZ  . LYS A 325 ? 0.3868 0.3796 0.3479 -0.0182 -0.0278 0.0155  314 LYS A NZ  
2376 N N   . LEU A 326 ? 0.3852 0.3641 0.3018 -0.0155 -0.0163 -0.0022 315 LEU A N   
2377 C CA  . LEU A 326 ? 0.3816 0.3591 0.2925 -0.0160 -0.0153 -0.0031 315 LEU A CA  
2378 C C   . LEU A 326 ? 0.3818 0.3578 0.2941 -0.0152 -0.0157 -0.0038 315 LEU A C   
2379 O O   . LEU A 326 ? 0.3792 0.3546 0.2900 -0.0160 -0.0152 -0.0029 315 LEU A O   
2380 C CB  . LEU A 326 ? 0.3733 0.3508 0.2810 -0.0153 -0.0136 -0.0049 315 LEU A CB  
2381 C CG  . LEU A 326 ? 0.3780 0.3570 0.2856 -0.0162 -0.0130 -0.0040 315 LEU A CG  
2382 C CD1 . LEU A 326 ? 0.3816 0.3608 0.2879 -0.0150 -0.0109 -0.0054 315 LEU A CD1 
2383 C CD2 . LEU A 326 ? 0.3838 0.3621 0.2874 -0.0183 -0.0134 -0.0030 315 LEU A CD2 
2384 N N   . LEU A 327 ? 0.3695 0.3446 0.2852 -0.0138 -0.0166 -0.0056 316 LEU A N   
2385 C CA  . LEU A 327 ? 0.3668 0.3402 0.2849 -0.0133 -0.0181 -0.0066 316 LEU A CA  
2386 C C   . LEU A 327 ? 0.3838 0.3572 0.3085 -0.0136 -0.0195 -0.0045 316 LEU A C   
2387 O O   . LEU A 327 ? 0.4000 0.3718 0.3293 -0.0127 -0.0209 -0.0060 316 LEU A O   
2388 C CB  . LEU A 327 ? 0.3593 0.3304 0.2757 -0.0116 -0.0186 -0.0103 316 LEU A CB  
2389 C CG  . LEU A 327 ? 0.3690 0.3395 0.2784 -0.0113 -0.0176 -0.0117 316 LEU A CG  
2390 C CD1 . LEU A 327 ? 0.3648 0.3322 0.2706 -0.0099 -0.0185 -0.0153 316 LEU A CD1 
2391 C CD2 . LEU A 327 ? 0.3716 0.3424 0.2805 -0.0124 -0.0183 -0.0101 316 LEU A CD2 
2392 N N   . THR A 328 ? 0.3795 0.3542 0.3045 -0.0150 -0.0191 -0.0012 317 THR A N   
2393 C CA  . THR A 328 ? 0.3856 0.3606 0.3165 -0.0156 -0.0202 0.0018  317 THR A CA  
2394 C C   . THR A 328 ? 0.3924 0.3667 0.3251 -0.0160 -0.0198 0.0030  317 THR A C   
2395 O O   . THR A 328 ? 0.4058 0.3804 0.3340 -0.0166 -0.0178 0.0035  317 THR A O   
2396 C CB  . THR A 328 ? 0.4094 0.3860 0.3380 -0.0170 -0.0200 0.0053  317 THR A CB  
2397 O OG1 . THR A 328 ? 0.4264 0.4040 0.3560 -0.0165 -0.0207 0.0044  317 THR A OG1 
2398 C CG2 . THR A 328 ? 0.4116 0.3884 0.3450 -0.0177 -0.0209 0.0093  317 THR A CG2 
2399 N N   . MET A 329 ? 0.3897 0.3632 0.3300 -0.0158 -0.0216 0.0035  318 MET A N   
2400 C CA  . MET A 329 ? 0.3932 0.3664 0.3378 -0.0163 -0.0214 0.0052  318 MET A CA  
2401 C C   . MET A 329 ? 0.3859 0.3606 0.3289 -0.0173 -0.0182 0.0096  318 MET A C   
2402 O O   . MET A 329 ? 0.3809 0.3558 0.3223 -0.0175 -0.0158 0.0101  318 MET A O   
2403 C CB  . MET A 329 ? 0.4020 0.3738 0.3565 -0.0161 -0.0244 0.0055  318 MET A CB  
2404 C CG  . MET A 329 ? 0.4648 0.4340 0.4193 -0.0151 -0.0272 0.0006  318 MET A CG  
2405 S SD  . MET A 329 ? 0.5786 0.5459 0.5313 -0.0149 -0.0295 -0.0028 318 MET A SD  
2406 C CE  . MET A 329 ? 0.4826 0.4492 0.4476 -0.0160 -0.0322 -0.0001 318 MET A CE  
2407 N N   . ASP A 330 ? 0.3853 0.3607 0.3283 -0.0180 -0.0179 0.0129  319 ASP A N   
2408 C CA  . ASP A 330 ? 0.3912 0.3671 0.3301 -0.0191 -0.0146 0.0170  319 ASP A CA  
2409 C C   . ASP A 330 ? 0.4058 0.3813 0.3335 -0.0195 -0.0127 0.0152  319 ASP A C   
2410 O O   . ASP A 330 ? 0.4102 0.3859 0.3338 -0.0198 -0.0145 0.0139  319 ASP A O   
2411 C CB  . ASP A 330 ? 0.3958 0.3723 0.3368 -0.0200 -0.0157 0.0213  319 ASP A CB  
2412 C CG  . ASP A 330 ? 0.4443 0.4208 0.3807 -0.0211 -0.0123 0.0262  319 ASP A CG  
2413 O OD1 . ASP A 330 ? 0.4537 0.4295 0.3838 -0.0212 -0.0085 0.0256  319 ASP A OD1 
2414 O OD2 . ASP A 330 ? 0.4609 0.4379 0.3997 -0.0219 -0.0133 0.0306  319 ASP A OD2 
2415 N N   . PRO A 331 ? 0.4059 0.3807 0.3299 -0.0195 -0.0090 0.0151  320 PRO A N   
2416 C CA  . PRO A 331 ? 0.4077 0.3814 0.3215 -0.0200 -0.0071 0.0130  320 PRO A CA  
2417 C C   . PRO A 331 ? 0.4159 0.3886 0.3207 -0.0216 -0.0072 0.0148  320 PRO A C   
2418 O O   . PRO A 331 ? 0.4215 0.3935 0.3197 -0.0222 -0.0084 0.0125  320 PRO A O   
2419 C CB  . PRO A 331 ? 0.4189 0.3916 0.3325 -0.0195 -0.0024 0.0134  320 PRO A CB  
2420 C CG  . PRO A 331 ? 0.4178 0.3915 0.3399 -0.0193 -0.0011 0.0175  320 PRO A CG  
2421 C CD  . PRO A 331 ? 0.3951 0.3702 0.3256 -0.0191 -0.0062 0.0170  320 PRO A CD  
2422 N N   . ILE A 332 ? 0.4098 0.3824 0.3143 -0.0224 -0.0063 0.0191  321 ILE A N   
2423 C CA  . ILE A 332 ? 0.4181 0.3895 0.3131 -0.0242 -0.0075 0.0212  321 ILE A CA  
2424 C C   . ILE A 332 ? 0.4011 0.3741 0.2990 -0.0247 -0.0130 0.0211  321 ILE A C   
2425 O O   . ILE A 332 ? 0.4081 0.3804 0.2986 -0.0264 -0.0153 0.0221  321 ILE A O   
2426 C CB  . ILE A 332 ? 0.4375 0.4082 0.3301 -0.0250 -0.0051 0.0266  321 ILE A CB  
2427 C CG1 . ILE A 332 ? 0.4499 0.4231 0.3548 -0.0245 -0.0077 0.0303  321 ILE A CG1 
2428 C CG2 . ILE A 332 ? 0.4431 0.4119 0.3324 -0.0244 0.0016  0.0270  321 ILE A CG2 
2429 C CD1 . ILE A 332 ? 0.4794 0.4523 0.3821 -0.0256 -0.0069 0.0363  321 ILE A CD1 
2430 N N   . LYS A 333 ? 0.3728 0.3478 0.2814 -0.0232 -0.0152 0.0197  322 LYS A N   
2431 C CA  . LYS A 333 ? 0.3625 0.3391 0.2758 -0.0231 -0.0192 0.0192  322 LYS A CA  
2432 C C   . LYS A 333 ? 0.3595 0.3364 0.2722 -0.0222 -0.0195 0.0146  322 LYS A C   
2433 O O   . LYS A 333 ? 0.3609 0.3392 0.2781 -0.0218 -0.0218 0.0140  322 LYS A O   
2434 C CB  . LYS A 333 ? 0.3723 0.3501 0.2975 -0.0219 -0.0210 0.0208  322 LYS A CB  
2435 C CG  . LYS A 333 ? 0.4035 0.3815 0.3306 -0.0230 -0.0218 0.0265  322 LYS A CG  
2436 C CD  . LYS A 333 ? 0.4280 0.4067 0.3681 -0.0219 -0.0237 0.0280  322 LYS A CD  
2437 C CE  . LYS A 333 ? 0.4709 0.4499 0.4131 -0.0231 -0.0242 0.0346  322 LYS A CE  
2438 N NZ  . LYS A 333 ? 0.4936 0.4726 0.4493 -0.0222 -0.0253 0.0364  322 LYS A NZ  
2439 N N   . ARG A 334 ? 0.3569 0.3326 0.2647 -0.0219 -0.0168 0.0117  323 ARG A N   
2440 C CA  . ARG A 334 ? 0.3595 0.3353 0.2660 -0.0213 -0.0167 0.0080  323 ARG A CA  
2441 C C   . ARG A 334 ? 0.3652 0.3407 0.2652 -0.0230 -0.0179 0.0081  323 ARG A C   
2442 O O   . ARG A 334 ? 0.3670 0.3407 0.2596 -0.0247 -0.0176 0.0097  323 ARG A O   
2443 C CB  . ARG A 334 ? 0.3625 0.3371 0.2670 -0.0205 -0.0137 0.0058  323 ARG A CB  
2444 C CG  . ARG A 334 ? 0.3729 0.3479 0.2814 -0.0188 -0.0140 0.0029  323 ARG A CG  
2445 C CD  . ARG A 334 ? 0.3821 0.3562 0.2910 -0.0182 -0.0120 0.0021  323 ARG A CD  
2446 N NE  . ARG A 334 ? 0.3848 0.3591 0.3007 -0.0176 -0.0128 0.0032  323 ARG A NE  
2447 C CZ  . ARG A 334 ? 0.4004 0.3744 0.3194 -0.0174 -0.0111 0.0045  323 ARG A CZ  
2448 N NH1 . ARG A 334 ? 0.3953 0.3685 0.3105 -0.0176 -0.0078 0.0046  323 ARG A NH1 
2449 N NH2 . ARG A 334 ? 0.4019 0.3763 0.3289 -0.0171 -0.0125 0.0058  323 ARG A NH2 
2450 N N   . ILE A 335 ? 0.3627 0.3395 0.2653 -0.0227 -0.0193 0.0066  324 ILE A N   
2451 C CA  . ILE A 335 ? 0.3707 0.3475 0.2695 -0.0245 -0.0211 0.0068  324 ILE A CA  
2452 C C   . ILE A 335 ? 0.3796 0.3535 0.2698 -0.0255 -0.0190 0.0046  324 ILE A C   
2453 O O   . ILE A 335 ? 0.3763 0.3494 0.2663 -0.0241 -0.0159 0.0026  324 ILE A O   
2454 C CB  . ILE A 335 ? 0.3833 0.3625 0.2891 -0.0232 -0.0216 0.0056  324 ILE A CB  
2455 C CG1 . ILE A 335 ? 0.3953 0.3758 0.3025 -0.0250 -0.0245 0.0070  324 ILE A CG1 
2456 C CG2 . ILE A 335 ? 0.3952 0.3739 0.2999 -0.0217 -0.0185 0.0023  324 ILE A CG2 
2457 C CD1 . ILE A 335 ? 0.4022 0.3855 0.3182 -0.0232 -0.0236 0.0063  324 ILE A CD1 
2458 N N   . THR A 336 ? 0.3865 0.3586 0.2702 -0.0279 -0.0209 0.0049  325 THR A N   
2459 C CA  . THR A 336 ? 0.3993 0.3679 0.2756 -0.0287 -0.0188 0.0022  325 THR A CA  
2460 C C   . THR A 336 ? 0.4026 0.3726 0.2834 -0.0283 -0.0190 0.0004  325 THR A C   
2461 O O   . THR A 336 ? 0.3996 0.3728 0.2876 -0.0279 -0.0210 0.0016  325 THR A O   
2462 C CB  . THR A 336 ? 0.4314 0.3962 0.2976 -0.0316 -0.0209 0.0026  325 THR A CB  
2463 O OG1 . THR A 336 ? 0.4576 0.4238 0.3262 -0.0336 -0.0261 0.0039  325 THR A OG1 
2464 C CG2 . THR A 336 ? 0.4218 0.3852 0.2823 -0.0321 -0.0203 0.0051  325 THR A CG2 
2465 N N   . SER A 337 ? 0.4024 0.3698 0.2796 -0.0283 -0.0165 -0.0021 326 SER A N   
2466 C CA  . SER A 337 ? 0.4158 0.3842 0.2970 -0.0282 -0.0164 -0.0032 326 SER A CA  
2467 C C   . SER A 337 ? 0.4223 0.3911 0.3047 -0.0306 -0.0206 -0.0022 326 SER A C   
2468 O O   . SER A 337 ? 0.4285 0.4005 0.3183 -0.0302 -0.0213 -0.0014 326 SER A O   
2469 C CB  . SER A 337 ? 0.4320 0.3969 0.3095 -0.0280 -0.0133 -0.0056 326 SER A CB  
2470 O OG  . SER A 337 ? 0.4664 0.4266 0.3353 -0.0300 -0.0134 -0.0069 326 SER A OG  
2471 N N   . GLU A 338 ? 0.4218 0.3874 0.2971 -0.0333 -0.0234 -0.0021 327 GLU A N   
2472 C CA  . GLU A 338 ? 0.4356 0.4014 0.3122 -0.0361 -0.0287 -0.0008 327 GLU A CA  
2473 C C   . GLU A 338 ? 0.4359 0.4069 0.3217 -0.0357 -0.0317 0.0028  327 GLU A C   
2474 O O   . GLU A 338 ? 0.4420 0.4160 0.3364 -0.0364 -0.0340 0.0043  327 GLU A O   
2475 C CB  . GLU A 338 ? 0.4824 0.4423 0.3469 -0.0393 -0.0316 -0.0020 327 GLU A CB  
2476 C CG  . GLU A 338 ? 0.5916 0.5494 0.4472 -0.0392 -0.0305 -0.0012 327 GLU A CG  
2477 C CD  . GLU A 338 ? 0.7188 0.6730 0.5672 -0.0374 -0.0243 -0.0036 327 GLU A CD  
2478 O OE1 . GLU A 338 ? 0.7149 0.6701 0.5682 -0.0351 -0.0200 -0.0053 327 GLU A OE1 
2479 O OE2 . GLU A 338 ? 0.7792 0.7298 0.6175 -0.0384 -0.0238 -0.0033 327 GLU A OE2 
2480 N N   . GLN A 339 ? 0.4263 0.3986 0.3123 -0.0343 -0.0311 0.0044  328 GLN A N   
2481 C CA  . GLN A 339 ? 0.4190 0.3959 0.3151 -0.0335 -0.0333 0.0077  328 GLN A CA  
2482 C C   . GLN A 339 ? 0.4099 0.3904 0.3159 -0.0306 -0.0299 0.0070  328 GLN A C   
2483 O O   . GLN A 339 ? 0.4064 0.3905 0.3222 -0.0304 -0.0315 0.0091  328 GLN A O   
2484 C CB  . GLN A 339 ? 0.4458 0.4228 0.3404 -0.0325 -0.0328 0.0094  328 GLN A CB  
2485 C CG  . GLN A 339 ? 0.5030 0.4770 0.3883 -0.0352 -0.0362 0.0114  328 GLN A CG  
2486 C CD  . GLN A 339 ? 0.5682 0.5431 0.4547 -0.0337 -0.0350 0.0137  328 GLN A CD  
2487 O OE1 . GLN A 339 ? 0.5822 0.5556 0.4655 -0.0321 -0.0306 0.0122  328 GLN A OE1 
2488 N NE2 . GLN A 339 ? 0.5886 0.5662 0.4820 -0.0341 -0.0389 0.0178  328 GLN A NE2 
2489 N N   . ALA A 340 ? 0.3974 0.3769 0.3008 -0.0285 -0.0253 0.0042  329 ALA A N   
2490 C CA  . ALA A 340 ? 0.3845 0.3665 0.2945 -0.0259 -0.0221 0.0034  329 ALA A CA  
2491 C C   . ALA A 340 ? 0.3833 0.3668 0.2982 -0.0269 -0.0225 0.0040  329 ALA A C   
2492 O O   . ALA A 340 ? 0.3785 0.3654 0.3022 -0.0256 -0.0216 0.0054  329 ALA A O   
2493 C CB  . ALA A 340 ? 0.3792 0.3593 0.2844 -0.0241 -0.0183 0.0007  329 ALA A CB  
2494 N N   . MET A 341 ? 0.3826 0.3636 0.2928 -0.0294 -0.0240 0.0033  330 MET A N   
2495 C CA  . MET A 341 ? 0.3923 0.3744 0.3080 -0.0308 -0.0250 0.0042  330 MET A CA  
2496 C C   . MET A 341 ? 0.3975 0.3829 0.3226 -0.0324 -0.0292 0.0076  330 MET A C   
2497 O O   . MET A 341 ? 0.3984 0.3868 0.3330 -0.0324 -0.0287 0.0094  330 MET A O   
2498 C CB  . MET A 341 ? 0.4013 0.3787 0.3095 -0.0334 -0.0263 0.0022  330 MET A CB  
2499 C CG  . MET A 341 ? 0.4326 0.4074 0.3354 -0.0317 -0.0217 -0.0005 330 MET A CG  
2500 S SD  . MET A 341 ? 0.5038 0.4719 0.3975 -0.0344 -0.0227 -0.0034 330 MET A SD  
2501 C CE  . MET A 341 ? 0.4614 0.4303 0.3632 -0.0368 -0.0253 -0.0021 330 MET A CE  
2502 N N   . GLN A 342 ? 0.3927 0.3779 0.3162 -0.0335 -0.0331 0.0091  331 GLN A N   
2503 C CA  . GLN A 342 ? 0.3942 0.3827 0.3274 -0.0350 -0.0379 0.0130  331 GLN A CA  
2504 C C   . GLN A 342 ? 0.3783 0.3713 0.3226 -0.0318 -0.0352 0.0150  331 GLN A C   
2505 O O   . GLN A 342 ? 0.3699 0.3662 0.3250 -0.0324 -0.0384 0.0187  331 GLN A O   
2506 C CB  . GLN A 342 ? 0.4262 0.4119 0.3516 -0.0381 -0.0440 0.0143  331 GLN A CB  
2507 C CG  . GLN A 342 ? 0.5008 0.4812 0.4155 -0.0416 -0.0471 0.0121  331 GLN A CG  
2508 C CD  . GLN A 342 ? 0.6205 0.5964 0.5219 -0.0438 -0.0507 0.0119  331 GLN A CD  
2509 O OE1 . GLN A 342 ? 0.6630 0.6397 0.5626 -0.0427 -0.0505 0.0136  331 GLN A OE1 
2510 N NE2 . GLN A 342 ? 0.6513 0.6217 0.5424 -0.0471 -0.0539 0.0097  331 GLN A NE2 
2511 N N   . ASP A 343 ? 0.3709 0.3637 0.3130 -0.0284 -0.0296 0.0126  332 ASP A N   
2512 C CA  . ASP A 343 ? 0.3740 0.3696 0.3249 -0.0252 -0.0266 0.0134  332 ASP A CA  
2513 C C   . ASP A 343 ? 0.3776 0.3773 0.3418 -0.0242 -0.0248 0.0157  332 ASP A C   
2514 O O   . ASP A 343 ? 0.3736 0.3736 0.3382 -0.0245 -0.0226 0.0152  332 ASP A O   
2515 C CB  . ASP A 343 ? 0.3936 0.3873 0.3384 -0.0221 -0.0212 0.0096  332 ASP A CB  
2516 C CG  . ASP A 343 ? 0.4331 0.4277 0.3836 -0.0193 -0.0195 0.0096  332 ASP A CG  
2517 O OD1 . ASP A 343 ? 0.4432 0.4397 0.4014 -0.0169 -0.0158 0.0096  332 ASP A OD1 
2518 O OD2 . ASP A 343 ? 0.4423 0.4354 0.3901 -0.0196 -0.0217 0.0098  332 ASP A OD2 
2519 N N   . PRO A 344 ? 0.3751 0.3779 0.3512 -0.0228 -0.0251 0.0184  333 PRO A N   
2520 C CA  . PRO A 344 ? 0.3703 0.3773 0.3609 -0.0214 -0.0222 0.0209  333 PRO A CA  
2521 C C   . PRO A 344 ? 0.3712 0.3780 0.3604 -0.0181 -0.0141 0.0182  333 PRO A C   
2522 O O   . PRO A 344 ? 0.3745 0.3844 0.3738 -0.0173 -0.0110 0.0204  333 PRO A O   
2523 C CB  . PRO A 344 ? 0.3723 0.3816 0.3747 -0.0198 -0.0231 0.0236  333 PRO A CB  
2524 C CG  . PRO A 344 ? 0.3821 0.3881 0.3751 -0.0197 -0.0250 0.0218  333 PRO A CG  
2525 C CD  . PRO A 344 ? 0.3663 0.3689 0.3443 -0.0225 -0.0280 0.0199  333 PRO A CD  
2526 N N   . TYR A 345 ? 0.3646 0.3677 0.3413 -0.0164 -0.0110 0.0139  334 TYR A N   
2527 C CA  . TYR A 345 ? 0.3641 0.3662 0.3364 -0.0137 -0.0042 0.0113  334 TYR A CA  
2528 C C   . TYR A 345 ? 0.3784 0.3817 0.3510 -0.0154 -0.0034 0.0128  334 TYR A C   
2529 O O   . TYR A 345 ? 0.3878 0.3926 0.3645 -0.0135 0.0022  0.0135  334 TYR A O   
2530 C CB  . TYR A 345 ? 0.3596 0.3572 0.3176 -0.0129 -0.0037 0.0070  334 TYR A CB  
2531 C CG  . TYR A 345 ? 0.3648 0.3605 0.3148 -0.0109 0.0015  0.0044  334 TYR A CG  
2532 C CD1 . TYR A 345 ? 0.3694 0.3653 0.3218 -0.0076 0.0076  0.0036  334 TYR A CD1 
2533 C CD2 . TYR A 345 ? 0.3750 0.3680 0.3142 -0.0121 0.0004  0.0027  334 TYR A CD2 
2534 C CE1 . TYR A 345 ? 0.3796 0.3731 0.3224 -0.0059 0.0119  0.0014  334 TYR A CE1 
2535 C CE2 . TYR A 345 ? 0.3857 0.3768 0.3171 -0.0104 0.0043  0.0009  334 TYR A CE2 
2536 C CZ  . TYR A 345 ? 0.3921 0.3833 0.3244 -0.0074 0.0098  0.0002  334 TYR A CZ  
2537 O OH  . TYR A 345 ? 0.4056 0.3944 0.3286 -0.0059 0.0132  -0.0014 334 TYR A OH  
2538 N N   . PHE A 346 ? 0.3763 0.3785 0.3449 -0.0190 -0.0089 0.0134  335 PHE A N   
2539 C CA  . PHE A 346 ? 0.3756 0.3781 0.3449 -0.0210 -0.0090 0.0146  335 PHE A CA  
2540 C C   . PHE A 346 ? 0.3742 0.3811 0.3591 -0.0224 -0.0103 0.0191  335 PHE A C   
2541 O O   . PHE A 346 ? 0.3621 0.3700 0.3506 -0.0236 -0.0091 0.0206  335 PHE A O   
2542 C CB  . PHE A 346 ? 0.3693 0.3680 0.3281 -0.0241 -0.0136 0.0127  335 PHE A CB  
2543 C CG  . PHE A 346 ? 0.3738 0.3688 0.3200 -0.0224 -0.0112 0.0090  335 PHE A CG  
2544 C CD1 . PHE A 346 ? 0.3766 0.3710 0.3189 -0.0202 -0.0060 0.0078  335 PHE A CD1 
2545 C CD2 . PHE A 346 ? 0.3799 0.3723 0.3186 -0.0230 -0.0141 0.0072  335 PHE A CD2 
2546 C CE1 . PHE A 346 ? 0.3855 0.3768 0.3174 -0.0189 -0.0047 0.0048  335 PHE A CE1 
2547 C CE2 . PHE A 346 ? 0.3859 0.3755 0.3153 -0.0215 -0.0121 0.0043  335 PHE A CE2 
2548 C CZ  . PHE A 346 ? 0.3798 0.3688 0.3062 -0.0195 -0.0078 0.0031  335 PHE A CZ  
2549 N N   . LEU A 347 ? 0.3781 0.3879 0.3736 -0.0223 -0.0126 0.0217  336 LEU A N   
2550 C CA  . LEU A 347 ? 0.3815 0.3962 0.3947 -0.0233 -0.0138 0.0267  336 LEU A CA  
2551 C C   . LEU A 347 ? 0.3838 0.4020 0.4080 -0.0190 -0.0054 0.0281  336 LEU A C   
2552 O O   . LEU A 347 ? 0.3826 0.4053 0.4230 -0.0191 -0.0042 0.0325  336 LEU A O   
2553 C CB  . LEU A 347 ? 0.3773 0.3934 0.3974 -0.0258 -0.0219 0.0295  336 LEU A CB  
2554 C CG  . LEU A 347 ? 0.4036 0.4157 0.4118 -0.0300 -0.0300 0.0282  336 LEU A CG  
2555 C CD1 . LEU A 347 ? 0.4062 0.4197 0.4206 -0.0323 -0.0378 0.0318  336 LEU A CD1 
2556 C CD2 . LEU A 347 ? 0.4111 0.4218 0.4178 -0.0334 -0.0326 0.0283  336 LEU A CD2 
2557 N N   . GLU A 348 ? 0.3884 0.4042 0.4043 -0.0153 0.0003  0.0244  337 GLU A N   
2558 C CA  . GLU A 348 ? 0.3875 0.4049 0.4101 -0.0109 0.0089  0.0245  337 GLU A CA  
2559 C C   . GLU A 348 ? 0.3958 0.4132 0.4148 -0.0096 0.0158  0.0245  337 GLU A C   
2560 O O   . GLU A 348 ? 0.3903 0.4048 0.3966 -0.0110 0.0147  0.0224  337 GLU A O   
2561 C CB  . GLU A 348 ? 0.4121 0.4255 0.4243 -0.0080 0.0111  0.0198  337 GLU A CB  
2562 C CG  . GLU A 348 ? 0.4664 0.4795 0.4826 -0.0032 0.0200  0.0184  337 GLU A CG  
2563 C CD  . GLU A 348 ? 0.5287 0.5366 0.5324 -0.0009 0.0212  0.0129  337 GLU A CD  
2564 O OE1 . GLU A 348 ? 0.5547 0.5588 0.5425 -0.0013 0.0210  0.0094  337 GLU A OE1 
2565 O OE2 . GLU A 348 ? 0.5317 0.5392 0.5424 0.0012  0.0220  0.0123  337 GLU A OE2 
2566 N N   . ASP A 349 ? 0.4055 0.4261 0.4360 -0.0069 0.0233  0.0271  338 ASP A N   
2567 C CA  . ASP A 349 ? 0.4265 0.4472 0.4537 -0.0053 0.0309  0.0278  338 ASP A CA  
2568 C C   . ASP A 349 ? 0.4420 0.4571 0.4494 -0.0024 0.0356  0.0223  338 ASP A C   
2569 O O   . ASP A 349 ? 0.4434 0.4560 0.4469 0.0003  0.0377  0.0188  338 ASP A O   
2570 C CB  . ASP A 349 ? 0.4511 0.4765 0.4959 -0.0025 0.0389  0.0321  338 ASP A CB  
2571 C CG  . ASP A 349 ? 0.5370 0.5622 0.5774 -0.0002 0.0485  0.0330  338 ASP A CG  
2572 O OD1 . ASP A 349 ? 0.5470 0.5739 0.5897 -0.0027 0.0473  0.0363  338 ASP A OD1 
2573 O OD2 . ASP A 349 ? 0.5894 0.6121 0.6228 0.0041  0.0569  0.0303  338 ASP A OD2 
2574 N N   . PRO A 350 ? 0.4509 0.4637 0.4460 -0.0033 0.0364  0.0215  339 PRO A N   
2575 C CA  . PRO A 350 ? 0.4476 0.4624 0.4463 -0.0064 0.0344  0.0251  339 PRO A CA  
2576 C C   . PRO A 350 ? 0.4504 0.4635 0.4448 -0.0106 0.0247  0.0240  339 PRO A C   
2577 O O   . PRO A 350 ? 0.4602 0.4697 0.4431 -0.0107 0.0212  0.0199  339 PRO A O   
2578 C CB  . PRO A 350 ? 0.4599 0.4721 0.4457 -0.0044 0.0409  0.0243  339 PRO A CB  
2579 C CG  . PRO A 350 ? 0.4713 0.4783 0.4407 -0.0022 0.0409  0.0186  339 PRO A CG  
2580 C CD  . PRO A 350 ? 0.4534 0.4609 0.4299 -0.0009 0.0398  0.0168  339 PRO A CD  
2581 N N   . LEU A 351 ? 0.4394 0.4548 0.4430 -0.0141 0.0206  0.0275  340 LEU A N   
2582 C CA  . LEU A 351 ? 0.4507 0.4634 0.4489 -0.0180 0.0121  0.0259  340 LEU A CA  
2583 C C   . LEU A 351 ? 0.4456 0.4540 0.4292 -0.0183 0.0127  0.0233  340 LEU A C   
2584 O O   . LEU A 351 ? 0.4475 0.4562 0.4295 -0.0168 0.0184  0.0249  340 LEU A O   
2585 C CB  . LEU A 351 ? 0.4608 0.4763 0.4732 -0.0219 0.0072  0.0300  340 LEU A CB  
2586 C CG  . LEU A 351 ? 0.4949 0.5147 0.5236 -0.0229 0.0037  0.0334  340 LEU A CG  
2587 C CD1 . LEU A 351 ? 0.5050 0.5252 0.5420 -0.0280 -0.0047 0.0359  340 LEU A CD1 
2588 C CD2 . LEU A 351 ? 0.5044 0.5229 0.5282 -0.0220 0.0003  0.0307  340 LEU A CD2 
2589 N N   . PRO A 352 ? 0.4424 0.4469 0.4157 -0.0201 0.0072  0.0199  341 PRO A N   
2590 C CA  . PRO A 352 ? 0.4448 0.4455 0.4068 -0.0204 0.0077  0.0180  341 PRO A CA  
2591 C C   . PRO A 352 ? 0.4417 0.4429 0.4101 -0.0227 0.0076  0.0211  341 PRO A C   
2592 O O   . PRO A 352 ? 0.4464 0.4493 0.4255 -0.0255 0.0038  0.0233  341 PRO A O   
2593 C CB  . PRO A 352 ? 0.4499 0.4469 0.4033 -0.0222 0.0017  0.0144  341 PRO A CB  
2594 C CG  . PRO A 352 ? 0.4468 0.4455 0.4078 -0.0242 -0.0031 0.0153  341 PRO A CG  
2595 C CD  . PRO A 352 ? 0.4274 0.4308 0.3996 -0.0221 0.0005  0.0181  341 PRO A CD  
2596 N N   . THR A 353 ? 0.4289 0.4286 0.3916 -0.0216 0.0115  0.0217  342 THR A N   
2597 C CA  . THR A 353 ? 0.4216 0.4214 0.3908 -0.0237 0.0117  0.0249  342 THR A CA  
2598 C C   . THR A 353 ? 0.4274 0.4223 0.3879 -0.0251 0.0089  0.0226  342 THR A C   
2599 O O   . THR A 353 ? 0.4255 0.4178 0.3746 -0.0235 0.0090  0.0195  342 THR A O   
2600 C CB  . THR A 353 ? 0.4158 0.4186 0.3885 -0.0212 0.0193  0.0292  342 THR A CB  
2601 O OG1 . THR A 353 ? 0.4296 0.4298 0.3885 -0.0186 0.0227  0.0276  342 THR A OG1 
2602 C CG2 . THR A 353 ? 0.4062 0.4136 0.3881 -0.0193 0.0236  0.0315  342 THR A CG2 
2603 N N   . SER A 354 ? 0.4353 0.4289 0.4024 -0.0280 0.0065  0.0241  343 SER A N   
2604 C CA  . SER A 354 ? 0.4500 0.4386 0.4114 -0.0294 0.0045  0.0223  343 SER A CA  
2605 C C   . SER A 354 ? 0.4503 0.4384 0.4048 -0.0267 0.0093  0.0237  343 SER A C   
2606 O O   . SER A 354 ? 0.4493 0.4337 0.3956 -0.0263 0.0082  0.0213  343 SER A O   
2607 C CB  . SER A 354 ? 0.4781 0.4654 0.4497 -0.0328 0.0018  0.0242  343 SER A CB  
2608 O OG  . SER A 354 ? 0.5345 0.5204 0.5090 -0.0359 -0.0045 0.0218  343 SER A OG  
2609 N N   . ASP A 355 ? 0.4546 0.4463 0.4125 -0.0248 0.0146  0.0279  344 ASP A N   
2610 C CA  . ASP A 355 ? 0.4731 0.4644 0.4231 -0.0223 0.0190  0.0299  344 ASP A CA  
2611 C C   . ASP A 355 ? 0.4829 0.4755 0.4245 -0.0192 0.0216  0.0279  344 ASP A C   
2612 O O   . ASP A 355 ? 0.4795 0.4755 0.4261 -0.0180 0.0252  0.0296  344 ASP A O   
2613 C CB  . ASP A 355 ? 0.4882 0.4821 0.4465 -0.0222 0.0238  0.0362  344 ASP A CB  
2614 C CG  . ASP A 355 ? 0.5339 0.5276 0.4839 -0.0198 0.0288  0.0395  344 ASP A CG  
2615 O OD1 . ASP A 355 ? 0.5324 0.5239 0.4697 -0.0180 0.0282  0.0367  344 ASP A OD1 
2616 O OD2 . ASP A 355 ? 0.5739 0.5697 0.5302 -0.0197 0.0332  0.0451  344 ASP A OD2 
2617 N N   . VAL A 356 ? 0.4922 0.4820 0.4224 -0.0180 0.0198  0.0244  345 VAL A N   
2618 C CA  . VAL A 356 ? 0.5102 0.5002 0.4321 -0.0153 0.0216  0.0220  345 VAL A CA  
2619 C C   . VAL A 356 ? 0.5399 0.5312 0.4578 -0.0128 0.0279  0.0251  345 VAL A C   
2620 O O   . VAL A 356 ? 0.5440 0.5362 0.4593 -0.0106 0.0311  0.0237  345 VAL A O   
2621 C CB  . VAL A 356 ? 0.5109 0.4975 0.4225 -0.0147 0.0180  0.0180  345 VAL A CB  
2622 C CG1 . VAL A 356 ? 0.5131 0.4983 0.4279 -0.0169 0.0129  0.0149  345 VAL A CG1 
2623 C CG2 . VAL A 356 ? 0.5134 0.4978 0.4184 -0.0143 0.0181  0.0198  345 VAL A CG2 
2624 N N   . PHE A 357 ? 0.5627 0.5538 0.4802 -0.0129 0.0303  0.0294  346 PHE A N   
2625 C CA  . PHE A 357 ? 0.5874 0.5794 0.4999 -0.0106 0.0369  0.0330  346 PHE A CA  
2626 C C   . PHE A 357 ? 0.6208 0.6172 0.5454 -0.0103 0.0425  0.0366  346 PHE A C   
2627 O O   . PHE A 357 ? 0.6295 0.6268 0.5503 -0.0080 0.0493  0.0394  346 PHE A O   
2628 C CB  . PHE A 357 ? 0.5783 0.5687 0.4858 -0.0109 0.0374  0.0372  346 PHE A CB  
2629 C CG  . PHE A 357 ? 0.5814 0.5681 0.4801 -0.0113 0.0318  0.0346  346 PHE A CG  
2630 C CD1 . PHE A 357 ? 0.5906 0.5749 0.4767 -0.0096 0.0304  0.0308  346 PHE A CD1 
2631 C CD2 . PHE A 357 ? 0.5872 0.5726 0.4912 -0.0134 0.0279  0.0358  346 PHE A CD2 
2632 C CE1 . PHE A 357 ? 0.5971 0.5786 0.4772 -0.0101 0.0250  0.0290  346 PHE A CE1 
2633 C CE2 . PHE A 357 ? 0.5962 0.5785 0.4939 -0.0135 0.0234  0.0338  346 PHE A CE2 
2634 C CZ  . PHE A 357 ? 0.5925 0.5732 0.4788 -0.0119 0.0218  0.0308  346 PHE A CZ  
2635 N N   . ALA A 358 ? 0.6430 0.6417 0.5816 -0.0126 0.0395  0.0366  347 ALA A N   
2636 C CA  . ALA A 358 ? 0.6752 0.6785 0.6289 -0.0129 0.0431  0.0401  347 ALA A CA  
2637 C C   . ALA A 358 ? 0.7141 0.7196 0.6718 -0.0120 0.0504  0.0467  347 ALA A C   
2638 O O   . ALA A 358 ? 0.7210 0.7290 0.6803 -0.0094 0.0578  0.0488  347 ALA A O   
2639 C CB  . ALA A 358 ? 0.6786 0.6835 0.6331 -0.0108 0.0453  0.0374  347 ALA A CB  
2640 N N   . GLY A 359 ? 0.7325 0.7367 0.6915 -0.0139 0.0489  0.0500  348 GLY A N   
2641 C CA  . GLY A 359 ? 0.7493 0.7554 0.7125 -0.0134 0.0553  0.0571  348 GLY A CA  
2642 C C   . GLY A 359 ? 0.7735 0.7782 0.7209 -0.0100 0.0620  0.0588  348 GLY A C   
2643 O O   . GLY A 359 ? 0.7821 0.7876 0.7300 -0.0097 0.0668  0.0651  348 GLY A O   
2644 N N   . CYS A 360 ? 0.7844 0.7867 0.7173 -0.0076 0.0623  0.0535  349 CYS A N   
2645 C CA  . CYS A 360 ? 0.8007 0.8004 0.7159 -0.0045 0.0679  0.0540  349 CYS A CA  
2646 C C   . CYS A 360 ? 0.8148 0.8112 0.7188 -0.0052 0.0649  0.0561  349 CYS A C   
2647 O O   . CYS A 360 ? 0.8149 0.8096 0.7205 -0.0074 0.0573  0.0541  349 CYS A O   
2648 C CB  . CYS A 360 ? 0.8077 0.8047 0.7112 -0.0022 0.0674  0.0470  349 CYS A CB  
2649 S SG  . CYS A 360 ? 0.8322 0.8330 0.7491 -0.0006 0.0719  0.0449  349 CYS A SG  
2650 N N   . GLN A 361 ? 0.8247 0.8196 0.7163 -0.0032 0.0709  0.0601  350 GLN A N   
2651 C CA  . GLN A 361 ? 0.8394 0.8309 0.7185 -0.0037 0.0680  0.0630  350 GLN A CA  
2652 C C   . GLN A 361 ? 0.8367 0.8241 0.7039 -0.0039 0.0600  0.0563  350 GLN A C   
2653 O O   . GLN A 361 ? 0.8490 0.8346 0.7074 -0.0021 0.0605  0.0507  350 GLN A O   
2654 C CB  . GLN A 361 ? 0.8784 0.8683 0.7421 -0.0011 0.0760  0.0673  350 GLN A CB  
2655 C CG  . GLN A 361 ? 0.9431 0.9372 0.8175 -0.0004 0.0858  0.0745  350 GLN A CG  
2656 C CD  . GLN A 361 ? 1.0362 1.0282 0.8933 0.0027  0.0951  0.0775  350 GLN A CD  
2657 O OE1 . GLN A 361 ? 1.0746 1.0627 0.9153 0.0051  0.0970  0.0720  350 GLN A OE1 
2658 N NE2 . GLN A 361 ? 1.0415 1.0353 0.9013 0.0028  0.1015  0.0864  350 GLN A NE2 
2659 N N   . ILE A 362 ? 0.8153 0.8014 0.6849 -0.0060 0.0527  0.0567  351 ILE A N   
2660 C CA  . ILE A 362 ? 0.8032 0.7858 0.6639 -0.0062 0.0453  0.0511  351 ILE A CA  
2661 C C   . ILE A 362 ? 0.8018 0.7806 0.6426 -0.0046 0.0455  0.0522  351 ILE A C   
2662 O O   . ILE A 362 ? 0.8107 0.7887 0.6475 -0.0051 0.0454  0.0583  351 ILE A O   
2663 C CB  . ILE A 362 ? 0.7921 0.7744 0.6624 -0.0087 0.0385  0.0517  351 ILE A CB  
2664 C CG1 . ILE A 362 ? 0.7882 0.7731 0.6757 -0.0105 0.0376  0.0498  351 ILE A CG1 
2665 C CG2 . ILE A 362 ? 0.7999 0.7789 0.6616 -0.0087 0.0315  0.0474  351 ILE A CG2 
2666 C CD1 . ILE A 362 ? 0.7981 0.7819 0.6952 -0.0128 0.0327  0.0510  351 ILE A CD1 
2667 N N   . PRO A 363 ? 0.7852 0.7613 0.6132 -0.0029 0.0457  0.0467  352 PRO A N   
2668 C CA  . PRO A 363 ? 0.7811 0.7526 0.5884 -0.0017 0.0451  0.0472  352 PRO A CA  
2669 C C   . PRO A 363 ? 0.7665 0.7351 0.5682 -0.0032 0.0354  0.0461  352 PRO A C   
2670 O O   . PRO A 363 ? 0.7747 0.7395 0.5605 -0.0029 0.0331  0.0480  352 PRO A O   
2671 C CB  . PRO A 363 ? 0.7967 0.7658 0.5941 0.0006  0.0491  0.0409  352 PRO A CB  
2672 C CG  . PRO A 363 ? 0.7991 0.7710 0.6118 0.0001  0.0471  0.0357  352 PRO A CG  
2673 C CD  . PRO A 363 ? 0.7735 0.7501 0.6052 -0.0021 0.0459  0.0397  352 PRO A CD  
2674 N N   . TYR A 364 ? 0.7431 0.7132 0.5576 -0.0047 0.0297  0.0431  353 TYR A N   
2675 C CA  . TYR A 364 ? 0.7337 0.7018 0.5472 -0.0060 0.0211  0.0418  353 TYR A CA  
2676 C C   . TYR A 364 ? 0.7367 0.7046 0.5508 -0.0071 0.0183  0.0489  353 TYR A C   
2677 O O   . TYR A 364 ? 0.7356 0.7061 0.5608 -0.0078 0.0213  0.0538  353 TYR A O   
2678 C CB  . TYR A 364 ? 0.7168 0.6869 0.5451 -0.0071 0.0177  0.0374  353 TYR A CB  
2679 C CG  . TYR A 364 ? 0.7106 0.6813 0.5399 -0.0061 0.0203  0.0313  353 TYR A CG  
2680 C CD1 . TYR A 364 ? 0.7178 0.6854 0.5357 -0.0050 0.0186  0.0262  353 TYR A CD1 
2681 C CD2 . TYR A 364 ? 0.7081 0.6822 0.5498 -0.0063 0.0246  0.0310  353 TYR A CD2 
2682 C CE1 . TYR A 364 ? 0.7200 0.6879 0.5395 -0.0039 0.0214  0.0211  353 TYR A CE1 
2683 C CE2 . TYR A 364 ? 0.7145 0.6894 0.5579 -0.0053 0.0270  0.0263  353 TYR A CE2 
2684 C CZ  . TYR A 364 ? 0.7231 0.6949 0.5557 -0.0040 0.0257  0.0214  353 TYR A CZ  
2685 O OH  . TYR A 364 ? 0.7314 0.7038 0.5669 -0.0029 0.0282  0.0171  353 TYR A OH  
2686 N N   . PRO A 365 ? 0.7410 0.7057 0.5439 -0.0074 0.0123  0.0499  354 PRO A N   
2687 C CA  . PRO A 365 ? 0.7448 0.7093 0.5491 -0.0084 0.0089  0.0574  354 PRO A CA  
2688 C C   . PRO A 365 ? 0.7516 0.7181 0.5742 -0.0098 0.0048  0.0582  354 PRO A C   
2689 O O   . PRO A 365 ? 0.7545 0.7216 0.5852 -0.0101 0.0027  0.0524  354 PRO A O   
2690 C CB  . PRO A 365 ? 0.7563 0.7166 0.5433 -0.0085 0.0026  0.0574  354 PRO A CB  
2691 C CG  . PRO A 365 ? 0.7604 0.7191 0.5447 -0.0081 -0.0003 0.0490  354 PRO A CG  
2692 C CD  . PRO A 365 ? 0.7393 0.7001 0.5288 -0.0069 0.0074  0.0445  354 PRO A CD  
2693 N N   . LYS A 366 ? 0.7524 0.7195 0.5815 -0.0106 0.0039  0.0654  355 LYS A N   
2694 C CA  . LYS A 366 ? 0.7549 0.7229 0.6008 -0.0117 0.0004  0.0663  355 LYS A CA  
2695 C C   . LYS A 366 ? 0.7573 0.7236 0.6017 -0.0120 -0.0077 0.0646  355 LYS A C   
2696 O O   . LYS A 366 ? 0.7621 0.7263 0.5921 -0.0118 -0.0116 0.0649  355 LYS A O   
2697 C CB  . LYS A 366 ? 0.7838 0.7526 0.6378 -0.0124 0.0018  0.0747  355 LYS A CB  
2698 C CG  . LYS A 366 ? 0.8425 0.8133 0.7028 -0.0124 0.0094  0.0763  355 LYS A CG  
2699 C CD  . LYS A 366 ? 0.9098 0.8811 0.7833 -0.0134 0.0102  0.0835  355 LYS A CD  
2700 C CE  . LYS A 366 ? 0.9684 0.9417 0.8488 -0.0137 0.0172  0.0860  355 LYS A CE  
2701 N NZ  . LYS A 366 ? 1.0061 0.9795 0.9023 -0.0150 0.0174  0.0920  355 LYS A NZ  
2702 N N   . ARG A 367 ? 0.7484 0.7154 0.6075 -0.0125 -0.0099 0.0625  356 ARG A N   
2703 C CA  . ARG A 367 ? 0.7482 0.7143 0.6096 -0.0127 -0.0168 0.0611  356 ARG A CA  
2704 C C   . ARG A 367 ? 0.7683 0.7334 0.6289 -0.0132 -0.0224 0.0688  356 ARG A C   
2705 O O   . ARG A 367 ? 0.7699 0.7354 0.6359 -0.0134 -0.0207 0.0753  356 ARG A O   
2706 C CB  . ARG A 367 ? 0.7307 0.6975 0.6082 -0.0129 -0.0163 0.0571  356 ARG A CB  
2707 C CG  . ARG A 367 ? 0.7115 0.6781 0.5871 -0.0127 -0.0188 0.0504  356 ARG A CG  
2708 C CD  . ARG A 367 ? 0.6835 0.6505 0.5739 -0.0128 -0.0184 0.0475  356 ARG A CD  
2709 N NE  . ARG A 367 ? 0.6429 0.6105 0.5347 -0.0128 -0.0139 0.0413  356 ARG A NE  
2710 C CZ  . ARG A 367 ? 0.6200 0.5876 0.5183 -0.0131 -0.0092 0.0406  356 ARG A CZ  
2711 N NH1 . ARG A 367 ? 0.6144 0.5816 0.5193 -0.0134 -0.0079 0.0456  356 ARG A NH1 
2712 N NH2 . ARG A 367 ? 0.5813 0.5493 0.4800 -0.0134 -0.0063 0.0352  356 ARG A NH2 
2713 N N   . GLU A 368 ? 0.7840 0.7478 0.6381 -0.0135 -0.0295 0.0685  357 GLU A N   
2714 C CA  . GLU A 368 ? 0.8066 0.7695 0.6596 -0.0142 -0.0363 0.0760  357 GLU A CA  
2715 C C   . GLU A 368 ? 0.8207 0.7848 0.6934 -0.0144 -0.0400 0.0784  357 GLU A C   
2716 O O   . GLU A 368 ? 0.8197 0.7847 0.7022 -0.0141 -0.0398 0.0730  357 GLU A O   
2717 C CB  . GLU A 368 ? 0.8472 0.8074 0.6826 -0.0148 -0.0431 0.0749  357 GLU A CB  
2718 C CG  . GLU A 368 ? 0.9248 0.8828 0.7413 -0.0150 -0.0430 0.0800  357 GLU A CG  
2719 C CD  . GLU A 368 ? 1.0244 0.9786 0.8228 -0.0159 -0.0512 0.0797  357 GLU A CD  
2720 O OE1 . GLU A 368 ? 1.0308 0.9837 0.8271 -0.0161 -0.0546 0.0728  357 GLU A OE1 
2721 O OE2 . GLU A 368 ? 1.0651 1.0172 0.8510 -0.0166 -0.0545 0.0864  357 GLU A OE2 
2722 N N   . PHE A 369 ? 0.8341 0.7984 0.7130 -0.0148 -0.0431 0.0868  358 PHE A N   
2723 C CA  . PHE A 369 ? 0.8459 0.8113 0.7448 -0.0147 -0.0461 0.0901  358 PHE A CA  
2724 C C   . PHE A 369 ? 0.8826 0.8478 0.7819 -0.0154 -0.0556 0.0919  358 PHE A C   
2725 O O   . PHE A 369 ? 0.8977 0.8617 0.7853 -0.0164 -0.0622 0.0971  358 PHE A O   
2726 C CB  . PHE A 369 ? 0.8303 0.7958 0.7380 -0.0147 -0.0451 0.0989  358 PHE A CB  
2727 C CG  . PHE A 369 ? 0.8275 0.7931 0.7381 -0.0143 -0.0362 0.0973  358 PHE A CG  
2728 C CD1 . PHE A 369 ? 0.8263 0.7919 0.7515 -0.0137 -0.0310 0.0920  358 PHE A CD1 
2729 C CD2 . PHE A 369 ? 0.8379 0.8033 0.7361 -0.0146 -0.0330 0.1008  358 PHE A CD2 
2730 C CE1 . PHE A 369 ? 0.8307 0.7961 0.7590 -0.0137 -0.0239 0.0906  358 PHE A CE1 
2731 C CE2 . PHE A 369 ? 0.8439 0.8096 0.7469 -0.0144 -0.0252 0.0998  358 PHE A CE2 
2732 C CZ  . PHE A 369 ? 0.8337 0.7994 0.7518 -0.0142 -0.0212 0.0946  358 PHE A CZ  
2733 N N   . LEU A 370 ? 0.8941 0.8604 0.8070 -0.0149 -0.0563 0.0877  359 LEU A N   
2734 C CA  . LEU A 370 ? 0.9105 0.8773 0.8291 -0.0156 -0.0649 0.0892  359 LEU A CA  
2735 C C   . LEU A 370 ? 0.9307 0.8984 0.8639 -0.0157 -0.0699 0.0988  359 LEU A C   
2736 O O   . LEU A 370 ? 0.9286 0.8970 0.8772 -0.0147 -0.0648 0.1013  359 LEU A O   
2737 C CB  . LEU A 370 ? 0.9042 0.8723 0.8364 -0.0147 -0.0618 0.0827  359 LEU A CB  
2738 C CG  . LEU A 370 ? 0.9260 0.8936 0.8488 -0.0143 -0.0557 0.0734  359 LEU A CG  
2739 C CD1 . LEU A 370 ? 0.9261 0.8948 0.8633 -0.0135 -0.0525 0.0685  359 LEU A CD1 
2740 C CD2 . LEU A 370 ? 0.9437 0.9096 0.8473 -0.0153 -0.0605 0.0703  359 LEU A CD2 
2741 N N   . THR A 371 ? 0.9482 0.9156 0.8774 -0.0171 -0.0803 0.1043  360 THR A N   
2742 C CA  . THR A 371 ? 0.9614 0.9301 0.9062 -0.0174 -0.0863 0.1142  360 THR A CA  
2743 C C   . THR A 371 ? 0.9621 0.9330 0.9270 -0.0171 -0.0899 0.1133  360 THR A C   
2744 O O   . THR A 371 ? 0.9623 0.9335 0.9264 -0.0186 -0.0999 0.1159  360 THR A O   
2745 C CB  . THR A 371 ? 0.9942 0.9613 0.9232 -0.0193 -0.0960 0.1217  360 THR A CB  
2746 O OG1 . THR A 371 ? 1.0201 0.9850 0.9278 -0.0194 -0.0914 0.1213  360 THR A OG1 
2747 C CG2 . THR A 371 ? 0.9922 0.9608 0.9376 -0.0196 -0.1021 0.1329  360 THR A CG2 
2748 N N   . GLU A 372 ? 0.9594 0.9314 0.9412 -0.0152 -0.0814 0.1092  361 GLU A N   
2749 C CA  . GLU A 372 ? 0.9602 0.9343 0.9617 -0.0144 -0.0819 0.1076  361 GLU A CA  
2750 C C   . GLU A 372 ? 0.9534 0.9295 0.9775 -0.0141 -0.0875 0.1171  361 GLU A C   
2751 O O   . GLU A 372 ? 0.9496 0.9257 0.9867 -0.0127 -0.0833 0.1216  361 GLU A O   
2752 C CB  . GLU A 372 ? 0.9876 0.9614 0.9969 -0.0124 -0.0701 0.0999  361 GLU A CB  
2753 C CG  . GLU A 372 ? 1.0386 1.0143 1.0671 -0.0113 -0.0687 0.0979  361 GLU A CG  
2754 C CD  . GLU A 372 ? 1.1062 1.0822 1.1264 -0.0118 -0.0687 0.0904  361 GLU A CD  
2755 O OE1 . GLU A 372 ? 1.1265 1.1010 1.1257 -0.0129 -0.0688 0.0855  361 GLU A OE1 
2756 O OE2 . GLU A 372 ? 1.1184 1.0962 1.1540 -0.0112 -0.0683 0.0897  361 GLU A OE2 
2757 N N   . GLU A 373 ? 0.9485 0.9263 0.9790 -0.0153 -0.0969 0.1200  362 GLU A N   
2758 C CA  . GLU A 373 ? 0.9393 0.9196 0.9933 -0.0151 -0.1033 0.1295  362 GLU A CA  
2759 C C   . GLU A 373 ? 0.9378 0.9209 1.0104 -0.0148 -0.1055 0.1283  362 GLU A C   
2760 O O   . GLU A 373 ? 0.9438 0.9268 1.0061 -0.0162 -0.1087 0.1228  362 GLU A O   
2761 C CB  . GLU A 373 ? 0.9521 0.9320 0.9962 -0.0176 -0.1161 0.1384  362 GLU A CB  
2762 C CG  . GLU A 373 ? 0.9640 0.9465 1.0334 -0.0174 -0.1225 0.1496  362 GLU A CG  
2763 C CD  . GLU A 373 ? 0.9940 0.9767 1.0805 -0.0148 -0.1136 0.1532  362 GLU A CD  
2764 O OE1 . GLU A 373 ? 1.0043 0.9845 1.0769 -0.0146 -0.1084 0.1525  362 GLU A OE1 
2765 O OE2 . GLU A 373 ? 0.9960 0.9809 1.1105 -0.0130 -0.1117 0.1569  362 GLU A OE2 
2766 N N   . ALA B 30  ? 0.6255 0.5631 0.5273 0.0248  -0.0131 -0.0002 0   ALA B N   
2767 C CA  . ALA B 30  ? 0.6251 0.5723 0.5314 0.0244  -0.0111 -0.0004 0   ALA B CA  
2768 C C   . ALA B 30  ? 0.6130 0.5739 0.5275 0.0226  -0.0062 -0.0005 0   ALA B C   
2769 O O   . ALA B 30  ? 0.6213 0.5842 0.5434 0.0172  -0.0034 0.0014  0   ALA B O   
2770 C CB  . ALA B 30  ? 0.6264 0.5696 0.5367 0.0194  -0.0115 0.0021  0   ALA B CB  
2771 N N   . MET B 31  ? 0.5909 0.5615 0.5034 0.0272  -0.0052 -0.0030 1   MET B N   
2772 C CA  . MET B 31  ? 0.5692 0.5539 0.4883 0.0260  -0.0008 -0.0040 1   MET B CA  
2773 C C   . MET B 31  ? 0.5663 0.5541 0.4865 0.0263  0.0003  -0.0054 1   MET B C   
2774 O O   . MET B 31  ? 0.5620 0.5616 0.4885 0.0245  0.0038  -0.0066 1   MET B O   
2775 C CB  . MET B 31  ? 0.5506 0.5401 0.4791 0.0195  0.0031  -0.0015 1   MET B CB  
2776 C CG  . MET B 31  ? 0.5406 0.5288 0.4680 0.0199  0.0024  0.0000  1   MET B CG  
2777 S SD  . MET B 31  ? 0.5211 0.5157 0.4406 0.0278  0.0005  -0.0026 1   MET B SD  
2778 C CE  . MET B 31  ? 0.4612 0.4731 0.3861 0.0274  0.0052  -0.0044 1   MET B CE  
2779 N N   . ALA B 32  ? 0.5652 0.5430 0.4788 0.0292  -0.0028 -0.0056 2   ALA B N   
2780 C CA  . ALA B 32  ? 0.5658 0.5466 0.4791 0.0309  -0.0020 -0.0070 2   ALA B CA  
2781 C C   . ALA B 32  ? 0.5572 0.5510 0.4678 0.0368  -0.0012 -0.0109 2   ALA B C   
2782 O O   . ALA B 32  ? 0.5648 0.5596 0.4690 0.0421  -0.0031 -0.0123 2   ALA B O   
2783 C CB  . ALA B 32  ? 0.5756 0.5422 0.4805 0.0338  -0.0056 -0.0061 2   ALA B CB  
2784 N N   . GLY B 33  ? 0.5343 0.5397 0.4509 0.0356  0.0019  -0.0126 3   GLY B N   
2785 C CA  . GLY B 33  ? 0.5249 0.5453 0.4403 0.0404  0.0030  -0.0164 3   GLY B CA  
2786 C C   . GLY B 33  ? 0.5169 0.5506 0.4402 0.0362  0.0065  -0.0170 3   GLY B C   
2787 O O   . GLY B 33  ? 0.5241 0.5731 0.4501 0.0374  0.0085  -0.0201 3   GLY B O   
2788 N N   . ASN B 34  ? 0.4955 0.5243 0.4230 0.0309  0.0074  -0.0139 4   ASN B N   
2789 C CA  . ASN B 34  ? 0.4728 0.5125 0.4072 0.0268  0.0109  -0.0137 4   ASN B CA  
2790 C C   . ASN B 34  ? 0.4575 0.5020 0.4029 0.0186  0.0152  -0.0130 4   ASN B C   
2791 O O   . ASN B 34  ? 0.4566 0.5067 0.4076 0.0142  0.0183  -0.0120 4   ASN B O   
2792 C CB  . ASN B 34  ? 0.4766 0.5088 0.4087 0.0265  0.0097  -0.0108 4   ASN B CB  
2793 C CG  . ASN B 34  ? 0.5008 0.5444 0.4368 0.0250  0.0127  -0.0104 4   ASN B CG  
2794 O OD1 . ASN B 34  ? 0.5243 0.5799 0.4581 0.0290  0.0132  -0.0129 4   ASN B OD1 
2795 N ND2 . ASN B 34  ? 0.5046 0.5450 0.4461 0.0193  0.0151  -0.0072 4   ASN B ND2 
2796 N N   . PHE B 35  ? 0.4450 0.4874 0.3932 0.0168  0.0155  -0.0137 5   PHE B N   
2797 C CA  . PHE B 35  ? 0.4337 0.4794 0.3915 0.0095  0.0191  -0.0135 5   PHE B CA  
2798 C C   . PHE B 35  ? 0.4389 0.4985 0.4033 0.0057  0.0231  -0.0155 5   PHE B C   
2799 O O   . PHE B 35  ? 0.4361 0.4943 0.4067 -0.0006 0.0260  -0.0135 5   PHE B O   
2800 C CB  . PHE B 35  ? 0.4137 0.4588 0.3732 0.0095  0.0189  -0.0150 5   PHE B CB  
2801 C CG  . PHE B 35  ? 0.4045 0.4507 0.3733 0.0022  0.0222  -0.0146 5   PHE B CG  
2802 C CD1 . PHE B 35  ? 0.4092 0.4447 0.3804 -0.0020 0.0226  -0.0107 5   PHE B CD1 
2803 C CD2 . PHE B 35  ? 0.3995 0.4578 0.3742 -0.0003 0.0248  -0.0183 5   PHE B CD2 
2804 C CE1 . PHE B 35  ? 0.4097 0.4454 0.3883 -0.0079 0.0255  -0.0103 5   PHE B CE1 
2805 C CE2 . PHE B 35  ? 0.4030 0.4609 0.3854 -0.0068 0.0276  -0.0183 5   PHE B CE2 
2806 C CZ  . PHE B 35  ? 0.4024 0.4485 0.3864 -0.0103 0.0279  -0.0142 5   PHE B CZ  
2807 N N   . TRP B 36  ? 0.4372 0.5104 0.4001 0.0093  0.0232  -0.0193 6   TRP B N   
2808 C CA  . TRP B 36  ? 0.4300 0.5180 0.3998 0.0048  0.0270  -0.0214 6   TRP B CA  
2809 C C   . TRP B 36  ? 0.4272 0.5172 0.3978 0.0026  0.0290  -0.0188 6   TRP B C   
2810 O O   . TRP B 36  ? 0.4223 0.5223 0.3994 -0.0028 0.0328  -0.0194 6   TRP B O   
2811 C CB  . TRP B 36  ? 0.4224 0.5263 0.3908 0.0093  0.0266  -0.0265 6   TRP B CB  
2812 C CG  . TRP B 36  ? 0.4225 0.5257 0.3905 0.0115  0.0253  -0.0291 6   TRP B CG  
2813 C CD1 . TRP B 36  ? 0.4382 0.5396 0.3980 0.0197  0.0219  -0.0305 6   TRP B CD1 
2814 C CD2 . TRP B 36  ? 0.4169 0.5198 0.3924 0.0057  0.0272  -0.0303 6   TRP B CD2 
2815 N NE1 . TRP B 36  ? 0.4439 0.5449 0.4058 0.0195  0.0218  -0.0323 6   TRP B NE1 
2816 C CE2 . TRP B 36  ? 0.4332 0.5359 0.4050 0.0111  0.0249  -0.0324 6   TRP B CE2 
2817 C CE3 . TRP B 36  ? 0.4174 0.5195 0.4017 -0.0031 0.0306  -0.0296 6   TRP B CE3 
2818 C CZ2 . TRP B 36  ? 0.4361 0.5395 0.4132 0.0081  0.0259  -0.0342 6   TRP B CZ2 
2819 C CZ3 . TRP B 36  ? 0.4260 0.5279 0.4153 -0.0060 0.0313  -0.0316 6   TRP B CZ3 
2820 C CH2 . TRP B 36  ? 0.4312 0.5345 0.4171 -0.0004 0.0289  -0.0340 6   TRP B CH2 
2821 N N   . GLN B 37  ? 0.4276 0.5079 0.3920 0.0064  0.0266  -0.0157 7   GLN B N   
2822 C CA  . GLN B 37  ? 0.4308 0.5123 0.3954 0.0051  0.0282  -0.0128 7   GLN B CA  
2823 C C   . GLN B 37  ? 0.4238 0.4900 0.3887 0.0023  0.0281  -0.0082 7   GLN B C   
2824 O O   . GLN B 37  ? 0.4316 0.4964 0.3949 0.0027  0.0287  -0.0054 7   GLN B O   
2825 C CB  . GLN B 37  ? 0.4718 0.5578 0.4278 0.0135  0.0252  -0.0137 7   GLN B CB  
2826 C CG  . GLN B 37  ? 0.5623 0.6652 0.5170 0.0176  0.0252  -0.0182 7   GLN B CG  
2827 C CD  . GLN B 37  ? 0.6830 0.7836 0.6318 0.0238  0.0216  -0.0213 7   GLN B CD  
2828 O OE1 . GLN B 37  ? 0.7301 0.8427 0.6808 0.0246  0.0225  -0.0252 7   GLN B OE1 
2829 N NE2 . GLN B 37  ? 0.7017 0.7868 0.6430 0.0283  0.0176  -0.0199 7   GLN B NE2 
2830 N N   . SER B 38  ? 0.4040 0.4598 0.3707 -0.0002 0.0273  -0.0074 8   SER B N   
2831 C CA  . SER B 38  ? 0.3928 0.4351 0.3595 -0.0023 0.0268  -0.0034 8   SER B CA  
2832 C C   . SER B 38  ? 0.3794 0.4204 0.3532 -0.0094 0.0312  -0.0010 8   SER B C   
2833 O O   . SER B 38  ? 0.3810 0.4289 0.3605 -0.0138 0.0343  -0.0029 8   SER B O   
2834 C CB  . SER B 38  ? 0.3975 0.4305 0.3624 -0.0013 0.0238  -0.0036 8   SER B CB  
2835 O OG  . SER B 38  ? 0.4124 0.4486 0.3831 -0.0051 0.0259  -0.0054 8   SER B OG  
2836 N N   . SER B 39  ? 0.3665 0.3978 0.3395 -0.0105 0.0312  0.0029  9   SER B N   
2837 C CA  . SER B 39  ? 0.3654 0.3931 0.3439 -0.0163 0.0352  0.0055  9   SER B CA  
2838 C C   . SER B 39  ? 0.3672 0.3905 0.3498 -0.0197 0.0356  0.0045  9   SER B C   
2839 O O   . SER B 39  ? 0.3739 0.3964 0.3614 -0.0247 0.0391  0.0050  9   SER B O   
2840 C CB  . SER B 39  ? 0.3768 0.3956 0.3526 -0.0153 0.0347  0.0098  9   SER B CB  
2841 O OG  . SER B 39  ? 0.4005 0.4105 0.3738 -0.0136 0.0311  0.0105  9   SER B OG  
2842 N N   . HIS B 40  ? 0.3612 0.3812 0.3413 -0.0168 0.0320  0.0031  10  HIS B N   
2843 C CA  . HIS B 40  ? 0.3669 0.3841 0.3504 -0.0190 0.0320  0.0020  10  HIS B CA  
2844 C C   . HIS B 40  ? 0.3762 0.4032 0.3647 -0.0220 0.0346  -0.0019 10  HIS B C   
2845 O O   . HIS B 40  ? 0.3751 0.4008 0.3685 -0.0265 0.0373  -0.0021 10  HIS B O   
2846 C CB  . HIS B 40  ? 0.3683 0.3817 0.3473 -0.0147 0.0276  0.0014  10  HIS B CB  
2847 C CG  . HIS B 40  ? 0.3901 0.4016 0.3718 -0.0160 0.0273  0.0005  10  HIS B CG  
2848 N ND1 . HIS B 40  ? 0.4103 0.4147 0.3890 -0.0140 0.0242  0.0022  10  HIS B ND1 
2849 C CD2 . HIS B 40  ? 0.4074 0.4240 0.3943 -0.0188 0.0296  -0.0021 10  HIS B CD2 
2850 C CE1 . HIS B 40  ? 0.4165 0.4221 0.3986 -0.0153 0.0249  0.0010  10  HIS B CE1 
2851 N NE2 . HIS B 40  ? 0.4209 0.4336 0.4079 -0.0180 0.0279  -0.0018 10  HIS B NE2 
2852 N N   . TYR B 41  ? 0.3841 0.4210 0.3711 -0.0194 0.0340  -0.0050 11  TYR B N   
2853 C CA  . TYR B 41  ? 0.4061 0.4544 0.3978 -0.0220 0.0363  -0.0092 11  TYR B CA  
2854 C C   . TYR B 41  ? 0.4135 0.4665 0.4101 -0.0279 0.0408  -0.0087 11  TYR B C   
2855 O O   . TYR B 41  ? 0.4189 0.4741 0.4211 -0.0332 0.0436  -0.0107 11  TYR B O   
2856 C CB  . TYR B 41  ? 0.4156 0.4740 0.4034 -0.0165 0.0340  -0.0128 11  TYR B CB  
2857 C CG  . TYR B 41  ? 0.4335 0.5067 0.4261 -0.0188 0.0363  -0.0175 11  TYR B CG  
2858 C CD1 . TYR B 41  ? 0.4498 0.5258 0.4474 -0.0218 0.0372  -0.0207 11  TYR B CD1 
2859 C CD2 . TYR B 41  ? 0.4484 0.5335 0.4407 -0.0182 0.0375  -0.0188 11  TYR B CD2 
2860 C CE1 . TYR B 41  ? 0.4589 0.5493 0.4613 -0.0245 0.0392  -0.0255 11  TYR B CE1 
2861 C CE2 . TYR B 41  ? 0.4571 0.5574 0.4544 -0.0210 0.0396  -0.0234 11  TYR B CE2 
2862 C CZ  . TYR B 41  ? 0.4711 0.5739 0.4735 -0.0243 0.0404  -0.0268 11  TYR B CZ  
2863 O OH  . TYR B 41  ? 0.4976 0.6162 0.5051 -0.0272 0.0423  -0.0318 11  TYR B OH  
2864 N N   . LEU B 42  ? 0.4103 0.4644 0.4044 -0.0269 0.0416  -0.0061 12  LEU B N   
2865 C CA  . LEU B 42  ? 0.4086 0.4676 0.4065 -0.0320 0.0460  -0.0051 12  LEU B CA  
2866 C C   . LEU B 42  ? 0.4191 0.4671 0.4198 -0.0373 0.0492  -0.0015 12  LEU B C   
2867 O O   . LEU B 42  ? 0.4218 0.4728 0.4269 -0.0433 0.0533  -0.0015 12  LEU B O   
2868 C CB  . LEU B 42  ? 0.4096 0.4742 0.4033 -0.0283 0.0457  -0.0033 12  LEU B CB  
2869 C CG  . LEU B 42  ? 0.4268 0.5036 0.4172 -0.0227 0.0430  -0.0071 12  LEU B CG  
2870 C CD1 . LEU B 42  ? 0.4284 0.5097 0.4136 -0.0178 0.0421  -0.0052 12  LEU B CD1 
2871 C CD2 . LEU B 42  ? 0.4275 0.5185 0.4236 -0.0266 0.0452  -0.0118 12  LEU B CD2 
2872 N N   . GLN B 43  ? 0.4210 0.4566 0.4191 -0.0355 0.0474  0.0015  13  GLN B N   
2873 C CA  . GLN B 43  ? 0.4255 0.4507 0.4253 -0.0394 0.0504  0.0050  13  GLN B CA  
2874 C C   . GLN B 43  ? 0.4265 0.4433 0.4274 -0.0400 0.0492  0.0046  13  GLN B C   
2875 O O   . GLN B 43  ? 0.4382 0.4481 0.4413 -0.0439 0.0520  0.0059  13  GLN B O   
2876 C CB  . GLN B 43  ? 0.4491 0.4678 0.4442 -0.0363 0.0501  0.0100  13  GLN B CB  
2877 C CG  . GLN B 43  ? 0.5191 0.5444 0.5133 -0.0365 0.0525  0.0116  13  GLN B CG  
2878 C CD  . GLN B 43  ? 0.5892 0.6086 0.5786 -0.0326 0.0518  0.0162  13  GLN B CD  
2879 O OE1 . GLN B 43  ? 0.6027 0.6272 0.5883 -0.0279 0.0496  0.0163  13  GLN B OE1 
2880 N NE2 . GLN B 43  ? 0.5929 0.6019 0.5820 -0.0339 0.0535  0.0197  13  GLN B NE2 
2881 N N   . TRP B 44  ? 0.4089 0.4254 0.4076 -0.0357 0.0451  0.0033  14  TRP B N   
2882 C CA  . TRP B 44  ? 0.4045 0.4135 0.4038 -0.0356 0.0438  0.0036  14  TRP B CA  
2883 C C   . TRP B 44  ? 0.4016 0.4156 0.4037 -0.0358 0.0426  -0.0008 14  TRP B C   
2884 O O   . TRP B 44  ? 0.4083 0.4181 0.4099 -0.0341 0.0405  -0.0005 14  TRP B O   
2885 C CB  . TRP B 44  ? 0.3974 0.3999 0.3920 -0.0313 0.0404  0.0069  14  TRP B CB  
2886 C CG  . TRP B 44  ? 0.3947 0.3911 0.3872 -0.0314 0.0419  0.0114  14  TRP B CG  
2887 C CD1 . TRP B 44  ? 0.3999 0.3975 0.3889 -0.0289 0.0414  0.0133  14  TRP B CD1 
2888 C CD2 . TRP B 44  ? 0.3943 0.3829 0.3877 -0.0335 0.0444  0.0143  14  TRP B CD2 
2889 N NE1 . TRP B 44  ? 0.4039 0.3953 0.3917 -0.0293 0.0433  0.0174  14  TRP B NE1 
2890 C CE2 . TRP B 44  ? 0.4057 0.3912 0.3959 -0.0320 0.0452  0.0181  14  TRP B CE2 
2891 C CE3 . TRP B 44  ? 0.4010 0.3850 0.3971 -0.0359 0.0459  0.0139  14  TRP B CE3 
2892 C CZ2 . TRP B 44  ? 0.4197 0.3976 0.4090 -0.0327 0.0477  0.0217  14  TRP B CZ2 
2893 C CZ3 . TRP B 44  ? 0.4154 0.3912 0.4104 -0.0366 0.0483  0.0173  14  TRP B CZ3 
2894 C CH2 . TRP B 44  ? 0.4203 0.3932 0.4119 -0.0349 0.0492  0.0213  14  TRP B CH2 
2895 N N   . ILE B 45  ? 0.3974 0.4211 0.4027 -0.0381 0.0441  -0.0049 15  ILE B N   
2896 C CA  . ILE B 45  ? 0.4035 0.4333 0.4123 -0.0389 0.0437  -0.0097 15  ILE B CA  
2897 C C   . ILE B 45  ? 0.4112 0.4403 0.4252 -0.0456 0.0478  -0.0111 15  ILE B C   
2898 O O   . ILE B 45  ? 0.4088 0.4444 0.4250 -0.0493 0.0504  -0.0124 15  ILE B O   
2899 C CB  . ILE B 45  ? 0.3983 0.4408 0.4067 -0.0360 0.0421  -0.0139 15  ILE B CB  
2900 C CG1 . ILE B 45  ? 0.4075 0.4478 0.4097 -0.0292 0.0379  -0.0124 15  ILE B CG1 
2901 C CG2 . ILE B 45  ? 0.3938 0.4438 0.4068 -0.0379 0.0426  -0.0193 15  ILE B CG2 
2902 C CD1 . ILE B 45  ? 0.4224 0.4569 0.4237 -0.0268 0.0356  -0.0120 15  ILE B CD1 
2903 N N   . LEU B 46  ? 0.4187 0.4387 0.4337 -0.0472 0.0484  -0.0102 16  LEU B N   
2904 C CA  . LEU B 46  ? 0.4314 0.4463 0.4497 -0.0531 0.0521  -0.0107 16  LEU B CA  
2905 C C   . LEU B 46  ? 0.4362 0.4573 0.4597 -0.0568 0.0529  -0.0168 16  LEU B C   
2906 O O   . LEU B 46  ? 0.4198 0.4484 0.4442 -0.0540 0.0503  -0.0205 16  LEU B O   
2907 C CB  . LEU B 46  ? 0.4434 0.4448 0.4592 -0.0520 0.0522  -0.0066 16  LEU B CB  
2908 C CG  . LEU B 46  ? 0.4670 0.4624 0.4779 -0.0482 0.0511  -0.0008 16  LEU B CG  
2909 C CD1 . LEU B 46  ? 0.4723 0.4567 0.4810 -0.0466 0.0509  0.0025  16  LEU B CD1 
2910 C CD2 . LEU B 46  ? 0.4701 0.4658 0.4800 -0.0504 0.0539  0.0018  16  LEU B CD2 
2911 N N   . ASP B 47  ? 0.4595 0.4770 0.4859 -0.0634 0.0565  -0.0178 17  ASP B N   
2912 C CA  . ASP B 47  ? 0.4783 0.4996 0.5098 -0.0684 0.0578  -0.0237 17  ASP B CA  
2913 C C   . ASP B 47  ? 0.4882 0.4982 0.5187 -0.0671 0.0571  -0.0235 17  ASP B C   
2914 O O   . ASP B 47  ? 0.4940 0.4911 0.5213 -0.0672 0.0585  -0.0190 17  ASP B O   
2915 C CB  . ASP B 47  ? 0.5219 0.5414 0.5559 -0.0763 0.0623  -0.0236 17  ASP B CB  
2916 C CG  . ASP B 47  ? 0.6213 0.6469 0.6612 -0.0830 0.0638  -0.0303 17  ASP B CG  
2917 O OD1 . ASP B 47  ? 0.6286 0.6513 0.6698 -0.0825 0.0623  -0.0341 17  ASP B OD1 
2918 O OD2 . ASP B 47  ? 0.6777 0.7112 0.7210 -0.0889 0.0664  -0.0319 17  ASP B OD2 
2919 N N   . LYS B 48  ? 0.4922 0.5073 0.5248 -0.0654 0.0548  -0.0284 18  LYS B N   
2920 C CA  . LYS B 48  ? 0.5147 0.5207 0.5462 -0.0632 0.0538  -0.0285 18  LYS B CA  
2921 C C   . LYS B 48  ? 0.5426 0.5353 0.5738 -0.0682 0.0570  -0.0279 18  LYS B C   
2922 O O   . LYS B 48  ? 0.5503 0.5316 0.5777 -0.0654 0.0568  -0.0242 18  LYS B O   
2923 C CB  . LYS B 48  ? 0.5272 0.5426 0.5616 -0.0610 0.0513  -0.0346 18  LYS B CB  
2924 C CG  . LYS B 48  ? 0.5876 0.5967 0.6198 -0.0562 0.0492  -0.0335 18  LYS B CG  
2925 C CD  . LYS B 48  ? 0.6569 0.6754 0.6920 -0.0541 0.0471  -0.0398 18  LYS B CD  
2926 C CE  . LYS B 48  ? 0.7241 0.7372 0.7570 -0.0489 0.0452  -0.0383 18  LYS B CE  
2927 N NZ  . LYS B 48  ? 0.7622 0.7833 0.7979 -0.0472 0.0436  -0.0448 18  LYS B NZ  
2928 N N   . GLN B 49  ? 0.5477 0.5419 0.5825 -0.0757 0.0599  -0.0313 19  GLN B N   
2929 C CA  . GLN B 49  ? 0.5596 0.5401 0.5938 -0.0811 0.0633  -0.0308 19  GLN B CA  
2930 C C   . GLN B 49  ? 0.5656 0.5338 0.5947 -0.0807 0.0657  -0.0232 19  GLN B C   
2931 O O   . GLN B 49  ? 0.5816 0.5353 0.6071 -0.0805 0.0671  -0.0209 19  GLN B O   
2932 C CB  . GLN B 49  ? 0.5875 0.5731 0.6270 -0.0900 0.0658  -0.0364 19  GLN B CB  
2933 C CG  . GLN B 49  ? 0.6542 0.6490 0.6983 -0.0906 0.0635  -0.0446 19  GLN B CG  
2934 C CD  . GLN B 49  ? 0.7599 0.7439 0.8013 -0.0868 0.0618  -0.0458 19  GLN B CD  
2935 O OE1 . GLN B 49  ? 0.7897 0.7797 0.8307 -0.0801 0.0583  -0.0472 19  GLN B OE1 
2936 N NE2 . GLN B 49  ? 0.7876 0.7554 0.8265 -0.0904 0.0643  -0.0447 19  GLN B NE2 
2937 N N   . ASP B 50  ? 0.5530 0.5270 0.5812 -0.0797 0.0661  -0.0193 20  ASP B N   
2938 C CA  . ASP B 50  ? 0.5546 0.5187 0.5779 -0.0782 0.0682  -0.0121 20  ASP B CA  
2939 C C   . ASP B 50  ? 0.5555 0.5117 0.5738 -0.0709 0.0658  -0.0083 20  ASP B C   
2940 O O   . ASP B 50  ? 0.5610 0.5044 0.5748 -0.0699 0.0676  -0.0039 20  ASP B O   
2941 C CB  . ASP B 50  ? 0.5770 0.5512 0.6004 -0.0774 0.0683  -0.0095 20  ASP B CB  
2942 C CG  . ASP B 50  ? 0.6573 0.6391 0.6847 -0.0846 0.0715  -0.0115 20  ASP B CG  
2943 O OD1 . ASP B 50  ? 0.6727 0.6512 0.7032 -0.0914 0.0740  -0.0150 20  ASP B OD1 
2944 O OD2 . ASP B 50  ? 0.6861 0.6773 0.7135 -0.0835 0.0715  -0.0096 20  ASP B OD2 
2945 N N   . LEU B 51  ? 0.5473 0.5117 0.5663 -0.0658 0.0617  -0.0099 21  LEU B N   
2946 C CA  . LEU B 51  ? 0.5510 0.5111 0.5662 -0.0592 0.0590  -0.0068 21  LEU B CA  
2947 C C   . LEU B 51  ? 0.5570 0.5068 0.5707 -0.0588 0.0595  -0.0078 21  LEU B C   
2948 O O   . LEU B 51  ? 0.5538 0.4938 0.5629 -0.0556 0.0600  -0.0034 21  LEU B O   
2949 C CB  . LEU B 51  ? 0.5443 0.5162 0.5612 -0.0552 0.0549  -0.0090 21  LEU B CB  
2950 C CG  . LEU B 51  ? 0.5596 0.5299 0.5732 -0.0489 0.0519  -0.0052 21  LEU B CG  
2951 C CD1 . LEU B 51  ? 0.5645 0.5321 0.5746 -0.0472 0.0521  0.0003  21  LEU B CD1 
2952 C CD2 . LEU B 51  ? 0.5627 0.5434 0.5779 -0.0457 0.0484  -0.0079 21  LEU B CD2 
2953 N N   . LEU B 52  ? 0.5621 0.5143 0.5794 -0.0617 0.0593  -0.0140 22  LEU B N   
2954 C CA  . LEU B 52  ? 0.5821 0.5246 0.5979 -0.0612 0.0596  -0.0160 22  LEU B CA  
2955 C C   . LEU B 52  ? 0.5921 0.5192 0.6041 -0.0645 0.0635  -0.0131 22  LEU B C   
2956 O O   . LEU B 52  ? 0.5996 0.5156 0.6070 -0.0612 0.0637  -0.0114 22  LEU B O   
2957 C CB  . LEU B 52  ? 0.5922 0.5409 0.6130 -0.0645 0.0588  -0.0239 22  LEU B CB  
2958 C CG  . LEU B 52  ? 0.6233 0.5875 0.6477 -0.0612 0.0553  -0.0276 22  LEU B CG  
2959 C CD1 . LEU B 52  ? 0.6341 0.6031 0.6628 -0.0638 0.0546  -0.0355 22  LEU B CD1 
2960 C CD2 . LEU B 52  ? 0.6368 0.6022 0.6582 -0.0534 0.0521  -0.0240 22  LEU B CD2 
2961 N N   . LYS B 53  ? 0.5872 0.5137 0.6006 -0.0705 0.0668  -0.0123 23  LYS B N   
2962 C CA  . LYS B 53  ? 0.6025 0.5143 0.6119 -0.0740 0.0710  -0.0090 23  LYS B CA  
2963 C C   . LYS B 53  ? 0.6049 0.5091 0.6079 -0.0679 0.0714  -0.0016 23  LYS B C   
2964 O O   . LYS B 53  ? 0.6220 0.5121 0.6194 -0.0661 0.0730  0.0008  23  LYS B O   
2965 C CB  . LYS B 53  ? 0.6428 0.5582 0.6557 -0.0818 0.0745  -0.0093 23  LYS B CB  
2966 C CG  . LYS B 53  ? 0.7361 0.6354 0.7453 -0.0868 0.0793  -0.0065 23  LYS B CG  
2967 C CD  . LYS B 53  ? 0.8133 0.7157 0.8231 -0.0908 0.0828  -0.0023 23  LYS B CD  
2968 C CE  . LYS B 53  ? 0.8834 0.7699 0.8897 -0.0966 0.0880  0.0005  23  LYS B CE  
2969 N NZ  . LYS B 53  ? 0.9172 0.8092 0.9254 -0.1018 0.0917  0.0038  23  LYS B NZ  
2970 N N   . GLU B 54  ? 0.5901 0.5036 0.5932 -0.0644 0.0697  0.0018  24  GLU B N   
2971 C CA  . GLU B 54  ? 0.5873 0.4956 0.5847 -0.0586 0.0696  0.0083  24  GLU B CA  
2972 C C   . GLU B 54  ? 0.5800 0.4848 0.5741 -0.0520 0.0668  0.0088  24  GLU B C   
2973 O O   . GLU B 54  ? 0.5851 0.4815 0.5734 -0.0478 0.0677  0.0135  24  GLU B O   
2974 C CB  . GLU B 54  ? 0.6189 0.5381 0.6173 -0.0566 0.0679  0.0109  24  GLU B CB  
2975 C CG  . GLU B 54  ? 0.7038 0.6231 0.7022 -0.0605 0.0714  0.0136  24  GLU B CG  
2976 C CD  . GLU B 54  ? 0.8286 0.7334 0.8219 -0.0616 0.0758  0.0179  24  GLU B CD  
2977 O OE1 . GLU B 54  ? 0.8547 0.7529 0.8423 -0.0559 0.0757  0.0225  24  GLU B OE1 
2978 O OE2 . GLU B 54  ? 0.8704 0.7703 0.8650 -0.0681 0.0795  0.0165  24  GLU B OE2 
2979 N N   . ARG B 55  ? 0.5663 0.4781 0.5638 -0.0509 0.0637  0.0042  25  ARG B N   
2980 C CA  . ARG B 55  ? 0.5706 0.4813 0.5657 -0.0449 0.0610  0.0045  25  ARG B CA  
2981 C C   . ARG B 55  ? 0.5756 0.4724 0.5662 -0.0440 0.0628  0.0039  25  ARG B C   
2982 O O   . ARG B 55  ? 0.5799 0.4737 0.5663 -0.0379 0.0614  0.0059  25  ARG B O   
2983 C CB  . ARG B 55  ? 0.5831 0.5058 0.5830 -0.0440 0.0574  -0.0002 25  ARG B CB  
2984 C CG  . ARG B 55  ? 0.6251 0.5489 0.6230 -0.0376 0.0546  0.0005  25  ARG B CG  
2985 C CD  . ARG B 55  ? 0.6565 0.5928 0.6589 -0.0364 0.0513  -0.0032 25  ARG B CD  
2986 N NE  . ARG B 55  ? 0.7019 0.6476 0.7061 -0.0362 0.0496  -0.0011 25  ARG B NE  
2987 C CZ  . ARG B 55  ? 0.7279 0.6839 0.7363 -0.0376 0.0481  -0.0044 25  ARG B CZ  
2988 N NH1 . ARG B 55  ? 0.7290 0.6886 0.7409 -0.0396 0.0481  -0.0103 25  ARG B NH1 
2989 N NH2 . ARG B 55  ? 0.7106 0.6731 0.7194 -0.0368 0.0466  -0.0022 25  ARG B NH2 
2990 N N   . GLN B 56  ? 0.5741 0.4626 0.5652 -0.0499 0.0659  0.0009  26  GLN B N   
2991 C CA  . GLN B 56  ? 0.5808 0.4542 0.5671 -0.0496 0.0677  -0.0004 26  GLN B CA  
2992 C C   . GLN B 56  ? 0.5905 0.4522 0.5683 -0.0437 0.0691  0.0056  26  GLN B C   
2993 O O   . GLN B 56  ? 0.5940 0.4472 0.5670 -0.0394 0.0686  0.0048  26  GLN B O   
2994 C CB  . GLN B 56  ? 0.6069 0.4723 0.5949 -0.0582 0.0712  -0.0037 26  GLN B CB  
2995 C CG  . GLN B 56  ? 0.6627 0.5390 0.6587 -0.0639 0.0698  -0.0110 26  GLN B CG  
2996 C CD  . GLN B 56  ? 0.7446 0.6250 0.7418 -0.0600 0.0662  -0.0163 26  GLN B CD  
2997 O OE1 . GLN B 56  ? 0.7771 0.6464 0.7693 -0.0565 0.0659  -0.0170 26  GLN B OE1 
2998 N NE2 . GLN B 56  ? 0.7543 0.6509 0.7577 -0.0600 0.0632  -0.0199 26  GLN B NE2 
2999 N N   . LYS B 57  ? 0.5933 0.4554 0.5690 -0.0428 0.0707  0.0114  27  LYS B N   
3000 C CA  . LYS B 57  ? 0.6105 0.4631 0.5781 -0.0365 0.0720  0.0172  27  LYS B CA  
3001 C C   . LYS B 57  ? 0.6129 0.4720 0.5786 -0.0284 0.0682  0.0182  27  LYS B C   
3002 O O   . LYS B 57  ? 0.6262 0.4763 0.5847 -0.0226 0.0687  0.0204  27  LYS B O   
3003 C CB  . LYS B 57  ? 0.6405 0.4934 0.6064 -0.0372 0.0744  0.0229  27  LYS B CB  
3004 C CG  . LYS B 57  ? 0.6778 0.5470 0.6489 -0.0368 0.0716  0.0238  27  LYS B CG  
3005 C CD  . LYS B 57  ? 0.7222 0.5916 0.6924 -0.0387 0.0743  0.0281  27  LYS B CD  
3006 C CE  . LYS B 57  ? 0.7575 0.6416 0.7314 -0.0374 0.0713  0.0292  27  LYS B CE  
3007 N NZ  . LYS B 57  ? 0.7703 0.6650 0.7515 -0.0428 0.0699  0.0247  27  LYS B NZ  
3008 N N   . ASP B 58  ? 0.5991 0.4735 0.5707 -0.0279 0.0644  0.0165  28  ASP B N   
3009 C CA  . ASP B 58  ? 0.5985 0.4802 0.5691 -0.0212 0.0609  0.0173  28  ASP B CA  
3010 C C   . ASP B 58  ? 0.6019 0.4826 0.5730 -0.0197 0.0592  0.0124  28  ASP B C   
3011 O O   . ASP B 58  ? 0.6021 0.4839 0.5697 -0.0132 0.0574  0.0135  28  ASP B O   
3012 C CB  . ASP B 58  ? 0.6058 0.5029 0.5815 -0.0210 0.0577  0.0184  28  ASP B CB  
3013 C CG  . ASP B 58  ? 0.6641 0.5629 0.6373 -0.0192 0.0582  0.0239  28  ASP B CG  
3014 O OD1 . ASP B 58  ? 0.6798 0.5691 0.6469 -0.0166 0.0607  0.0274  28  ASP B OD1 
3015 O OD2 . ASP B 58  ? 0.6959 0.6051 0.6729 -0.0201 0.0559  0.0246  28  ASP B OD2 
3016 N N   . LEU B 59  ? 0.6023 0.4815 0.5775 -0.0254 0.0599  0.0069  29  LEU B N   
3017 C CA  . LEU B 59  ? 0.6114 0.4896 0.5873 -0.0243 0.0583  0.0013  29  LEU B CA  
3018 C C   . LEU B 59  ? 0.6368 0.4984 0.6050 -0.0214 0.0602  0.0009  29  LEU B C   
3019 O O   . LEU B 59  ? 0.6441 0.5035 0.6117 -0.0198 0.0588  -0.0038 29  LEU B O   
3020 C CB  . LEU B 59  ? 0.6059 0.4896 0.5890 -0.0313 0.0581  -0.0050 29  LEU B CB  
3021 C CG  . LEU B 59  ? 0.6149 0.5152 0.6048 -0.0330 0.0559  -0.0053 29  LEU B CG  
3022 C CD1 . LEU B 59  ? 0.6191 0.5255 0.6154 -0.0388 0.0557  -0.0120 29  LEU B CD1 
3023 C CD2 . LEU B 59  ? 0.6122 0.5234 0.6025 -0.0265 0.0523  -0.0035 29  LEU B CD2 
3024 N N   . LYS B 60  ? 0.6467 0.4966 0.6082 -0.0199 0.0631  0.0059  30  LYS B N   
3025 C CA  . LYS B 60  ? 0.6704 0.5040 0.6230 -0.0155 0.0648  0.0066  30  LYS B CA  
3026 C C   . LYS B 60  ? 0.6778 0.5170 0.6259 -0.0055 0.0619  0.0089  30  LYS B C   
3027 O O   . LYS B 60  ? 0.6931 0.5233 0.6350 -0.0004 0.0616  0.0072  30  LYS B O   
3028 C CB  . LYS B 60  ? 0.7147 0.5343 0.6610 -0.0168 0.0691  0.0116  30  LYS B CB  
3029 C CG  . LYS B 60  ? 0.7867 0.5963 0.7352 -0.0263 0.0726  0.0090  30  LYS B CG  
3030 C CD  . LYS B 60  ? 0.8604 0.6720 0.8108 -0.0308 0.0755  0.0137  30  LYS B CD  
3031 C CE  . LYS B 60  ? 0.9170 0.7238 0.8718 -0.0413 0.0785  0.0107  30  LYS B CE  
3032 N NZ  . LYS B 60  ? 0.9447 0.7558 0.9017 -0.0453 0.0812  0.0152  30  LYS B NZ  
3033 N N   . PHE B 61  ? 0.6634 0.5178 0.6148 -0.0028 0.0597  0.0124  31  PHE B N   
3034 C CA  . PHE B 61  ? 0.6610 0.5236 0.6094 0.0056  0.0571  0.0151  31  PHE B CA  
3035 C C   . PHE B 61  ? 0.6313 0.5097 0.5862 0.0064  0.0532  0.0120  31  PHE B C   
3036 O O   . PHE B 61  ? 0.6249 0.5084 0.5773 0.0131  0.0510  0.0122  31  PHE B O   
3037 C CB  . PHE B 61  ? 0.6708 0.5395 0.6181 0.0077  0.0573  0.0214  31  PHE B CB  
3038 C CG  . PHE B 61  ? 0.7035 0.5582 0.6438 0.0082  0.0612  0.0253  31  PHE B CG  
3039 C CD1 . PHE B 61  ? 0.7212 0.5714 0.6640 0.0012  0.0639  0.0260  31  PHE B CD1 
3040 C CD2 . PHE B 61  ? 0.7215 0.5685 0.6523 0.0162  0.0622  0.0285  31  PHE B CD2 
3041 C CE1 . PHE B 61  ? 0.7378 0.5754 0.6739 0.0020  0.0677  0.0300  31  PHE B CE1 
3042 C CE2 . PHE B 61  ? 0.7403 0.5745 0.6641 0.0173  0.0659  0.0324  31  PHE B CE2 
3043 C CZ  . PHE B 61  ? 0.7395 0.5689 0.6661 0.0100  0.0687  0.0333  31  PHE B CZ  
3044 N N   . LEU B 62  ? 0.6045 0.4916 0.5676 -0.0001 0.0523  0.0096  32  LEU B N   
3045 C CA  . LEU B 62  ? 0.5817 0.4838 0.5508 0.0006  0.0489  0.0072  32  LEU B CA  
3046 C C   . LEU B 62  ? 0.5712 0.4736 0.5454 -0.0044 0.0487  0.0005  32  LEU B C   
3047 O O   . LEU B 62  ? 0.5790 0.4752 0.5551 -0.0108 0.0509  -0.0014 32  LEU B O   
3048 C CB  . LEU B 62  ? 0.5699 0.4843 0.5438 -0.0016 0.0476  0.0107  32  LEU B CB  
3049 C CG  . LEU B 62  ? 0.5785 0.4951 0.5487 0.0024  0.0475  0.0169  32  LEU B CG  
3050 C CD1 . LEU B 62  ? 0.5801 0.5002 0.5533 -0.0020 0.0479  0.0196  32  LEU B CD1 
3051 C CD2 . LEU B 62  ? 0.5769 0.5055 0.5473 0.0080  0.0445  0.0188  32  LEU B CD2 
3052 N N   . SER B 63  ? 0.5544 0.4658 0.5312 -0.0015 0.0460  -0.0029 33  SER B N   
3053 C CA  . SER B 63  ? 0.5478 0.4625 0.5301 -0.0059 0.0453  -0.0095 33  SER B CA  
3054 C C   . SER B 63  ? 0.5494 0.4752 0.5383 -0.0108 0.0448  -0.0091 33  SER B C   
3055 O O   . SER B 63  ? 0.5552 0.4872 0.5445 -0.0097 0.0442  -0.0039 33  SER B O   
3056 C CB  . SER B 63  ? 0.5475 0.4694 0.5301 -0.0004 0.0426  -0.0131 33  SER B CB  
3057 O OG  . SER B 63  ? 0.5649 0.5019 0.5505 0.0029  0.0401  -0.0101 33  SER B OG  
3058 N N   . GLU B 64  ? 0.5422 0.4713 0.5363 -0.0158 0.0449  -0.0146 34  GLU B N   
3059 C CA  . GLU B 64  ? 0.5375 0.4775 0.5372 -0.0195 0.0442  -0.0147 34  GLU B CA  
3060 C C   . GLU B 64  ? 0.5105 0.4637 0.5118 -0.0148 0.0412  -0.0120 34  GLU B C   
3061 O O   . GLU B 64  ? 0.5074 0.4664 0.5103 -0.0159 0.0407  -0.0086 34  GLU B O   
3062 C CB  . GLU B 64  ? 0.5887 0.5322 0.5934 -0.0243 0.0444  -0.0219 34  GLU B CB  
3063 C CG  . GLU B 64  ? 0.6851 0.6179 0.6897 -0.0312 0.0475  -0.0241 34  GLU B CG  
3064 C CD  . GLU B 64  ? 0.7876 0.7288 0.7985 -0.0369 0.0476  -0.0298 34  GLU B CD  
3065 O OE1 . GLU B 64  ? 0.8051 0.7525 0.8188 -0.0360 0.0459  -0.0358 34  GLU B OE1 
3066 O OE2 . GLU B 64  ? 0.8140 0.7569 0.8270 -0.0418 0.0493  -0.0284 34  GLU B OE2 
3067 N N   . GLU B 65  ? 0.4903 0.4475 0.4907 -0.0095 0.0394  -0.0135 35  GLU B N   
3068 C CA  . GLU B 65  ? 0.4698 0.4390 0.4712 -0.0047 0.0368  -0.0109 35  GLU B CA  
3069 C C   . GLU B 65  ? 0.4506 0.4200 0.4491 -0.0023 0.0366  -0.0036 35  GLU B C   
3070 O O   . GLU B 65  ? 0.4552 0.4328 0.4555 -0.0023 0.0353  -0.0002 35  GLU B O   
3071 C CB  . GLU B 65  ? 0.4977 0.4697 0.4980 0.0008  0.0353  -0.0143 35  GLU B CB  
3072 C CG  . GLU B 65  ? 0.5835 0.5698 0.5863 0.0048  0.0329  -0.0135 35  GLU B CG  
3073 C CD  . GLU B 65  ? 0.6973 0.6874 0.6994 0.0103  0.0314  -0.0176 35  GLU B CD  
3074 O OE1 . GLU B 65  ? 0.7331 0.7149 0.7308 0.0133  0.0318  -0.0185 35  GLU B OE1 
3075 O OE2 . GLU B 65  ? 0.7280 0.7291 0.7333 0.0122  0.0299  -0.0199 35  GLU B OE2 
3076 N N   . GLU B 66  ? 0.4367 0.3968 0.4302 -0.0003 0.0379  -0.0013 36  GLU B N   
3077 C CA  . GLU B 66  ? 0.4287 0.3892 0.4190 0.0022  0.0378  0.0052  36  GLU B CA  
3078 C C   . GLU B 66  ? 0.4188 0.3775 0.4101 -0.0025 0.0388  0.0082  36  GLU B C   
3079 O O   . GLU B 66  ? 0.4149 0.3788 0.4059 -0.0015 0.0377  0.0129  36  GLU B O   
3080 C CB  . GLU B 66  ? 0.4647 0.4147 0.4485 0.0062  0.0392  0.0062  36  GLU B CB  
3081 C CG  . GLU B 66  ? 0.4899 0.4417 0.4713 0.0123  0.0379  0.0038  36  GLU B CG  
3082 C CD  . GLU B 66  ? 0.5588 0.4984 0.5327 0.0165  0.0394  0.0045  36  GLU B CD  
3083 O OE1 . GLU B 66  ? 0.5567 0.4831 0.5281 0.0131  0.0419  0.0039  36  GLU B OE1 
3084 O OE2 . GLU B 66  ? 0.5946 0.5382 0.5648 0.0235  0.0381  0.0060  36  GLU B OE2 
3085 N N   . TYR B 67  ? 0.4206 0.3722 0.4131 -0.0075 0.0408  0.0055  37  TYR B N   
3086 C CA  . TYR B 67  ? 0.4246 0.3753 0.4181 -0.0117 0.0418  0.0079  37  TYR B CA  
3087 C C   . TYR B 67  ? 0.4411 0.4031 0.4390 -0.0131 0.0395  0.0078  37  TYR B C   
3088 O O   . TYR B 67  ? 0.4478 0.4127 0.4456 -0.0137 0.0387  0.0116  37  TYR B O   
3089 C CB  . TYR B 67  ? 0.4137 0.3554 0.4076 -0.0169 0.0446  0.0048  37  TYR B CB  
3090 C CG  . TYR B 67  ? 0.4065 0.3471 0.4007 -0.0205 0.0459  0.0076  37  TYR B CG  
3091 C CD1 . TYR B 67  ? 0.4082 0.3569 0.4066 -0.0236 0.0448  0.0064  37  TYR B CD1 
3092 C CD2 . TYR B 67  ? 0.4147 0.3471 0.4045 -0.0200 0.0479  0.0117  37  TYR B CD2 
3093 C CE1 . TYR B 67  ? 0.4108 0.3592 0.4090 -0.0260 0.0456  0.0089  37  TYR B CE1 
3094 C CE2 . TYR B 67  ? 0.4199 0.3523 0.4099 -0.0226 0.0489  0.0144  37  TYR B CE2 
3095 C CZ  . TYR B 67  ? 0.4243 0.3647 0.4184 -0.0256 0.0477  0.0129  37  TYR B CZ  
3096 O OH  . TYR B 67  ? 0.4482 0.3888 0.4421 -0.0276 0.0484  0.0152  37  TYR B OH  
3097 N N   . TRP B 68  ? 0.4390 0.4073 0.4403 -0.0131 0.0383  0.0033  38  TRP B N   
3098 C CA  . TRP B 68  ? 0.4407 0.4189 0.4452 -0.0135 0.0363  0.0033  38  TRP B CA  
3099 C C   . TRP B 68  ? 0.4283 0.4125 0.4317 -0.0100 0.0342  0.0084  38  TRP B C   
3100 O O   . TRP B 68  ? 0.4457 0.4326 0.4493 -0.0114 0.0332  0.0115  38  TRP B O   
3101 C CB  . TRP B 68  ? 0.4446 0.4290 0.4525 -0.0134 0.0356  -0.0025 38  TRP B CB  
3102 C CG  . TRP B 68  ? 0.4612 0.4550 0.4715 -0.0134 0.0338  -0.0026 38  TRP B CG  
3103 C CD1 . TRP B 68  ? 0.4727 0.4681 0.4824 -0.0146 0.0330  0.0009  38  TRP B CD1 
3104 C CD2 . TRP B 68  ? 0.4645 0.4667 0.4774 -0.0118 0.0327  -0.0070 38  TRP B CD2 
3105 N NE1 . TRP B 68  ? 0.4756 0.4789 0.4869 -0.0136 0.0315  -0.0005 38  TRP B NE1 
3106 C CE2 . TRP B 68  ? 0.4732 0.4813 0.4865 -0.0117 0.0314  -0.0052 38  TRP B CE2 
3107 C CE3 . TRP B 68  ? 0.4700 0.4752 0.4844 -0.0099 0.0326  -0.0123 38  TRP B CE3 
3108 C CZ2 . TRP B 68  ? 0.4766 0.4935 0.4916 -0.0096 0.0302  -0.0083 38  TRP B CZ2 
3109 C CZ3 . TRP B 68  ? 0.4732 0.4882 0.4899 -0.0079 0.0313  -0.0156 38  TRP B CZ3 
3110 C CH2 . TRP B 68  ? 0.4748 0.4956 0.4917 -0.0076 0.0302  -0.0134 38  TRP B CH2 
3111 N N   . LYS B 69  ? 0.3979 0.3837 0.3996 -0.0058 0.0336  0.0094  39  LYS B N   
3112 C CA  . LYS B 69  ? 0.3800 0.3727 0.3809 -0.0027 0.0319  0.0142  39  LYS B CA  
3113 C C   . LYS B 69  ? 0.3820 0.3723 0.3809 -0.0039 0.0319  0.0193  39  LYS B C   
3114 O O   . LYS B 69  ? 0.3651 0.3616 0.3646 -0.0041 0.0302  0.0229  39  LYS B O   
3115 C CB  . LYS B 69  ? 0.3858 0.3802 0.3847 0.0025  0.0316  0.0140  39  LYS B CB  
3116 C CG  . LYS B 69  ? 0.4152 0.4145 0.4163 0.0046  0.0309  0.0093  39  LYS B CG  
3117 C CD  . LYS B 69  ? 0.4287 0.4274 0.4271 0.0100  0.0309  0.0077  39  LYS B CD  
3118 C CE  . LYS B 69  ? 0.4297 0.4361 0.4306 0.0126  0.0297  0.0036  39  LYS B CE  
3119 N NZ  . LYS B 69  ? 0.4329 0.4413 0.4309 0.0190  0.0290  0.0026  39  LYS B NZ  
3120 N N   . LEU B 70  ? 0.4022 0.3834 0.3984 -0.0049 0.0339  0.0195  40  LEU B N   
3121 C CA  . LEU B 70  ? 0.4286 0.4076 0.4227 -0.0057 0.0340  0.0238  40  LEU B CA  
3122 C C   . LEU B 70  ? 0.4430 0.4233 0.4392 -0.0098 0.0332  0.0241  40  LEU B C   
3123 O O   . LEU B 70  ? 0.4464 0.4295 0.4420 -0.0104 0.0318  0.0277  40  LEU B O   
3124 C CB  . LEU B 70  ? 0.4476 0.4159 0.4380 -0.0054 0.0367  0.0237  40  LEU B CB  
3125 C CG  . LEU B 70  ? 0.4895 0.4564 0.4754 -0.0008 0.0371  0.0271  40  LEU B CG  
3126 C CD1 . LEU B 70  ? 0.5126 0.4676 0.4941 -0.0004 0.0401  0.0271  40  LEU B CD1 
3127 C CD2 . LEU B 70  ? 0.4983 0.4720 0.4840 -0.0004 0.0354  0.0316  40  LEU B CD2 
3128 N N   . GLN B 71  ? 0.4438 0.4226 0.4422 -0.0126 0.0339  0.0202  41  GLN B N   
3129 C CA  . GLN B 71  ? 0.4459 0.4261 0.4455 -0.0157 0.0330  0.0201  41  GLN B CA  
3130 C C   . GLN B 71  ? 0.4243 0.4121 0.4253 -0.0151 0.0303  0.0214  41  GLN B C   
3131 O O   . GLN B 71  ? 0.4209 0.4092 0.4212 -0.0165 0.0289  0.0235  41  GLN B O   
3132 C CB  . GLN B 71  ? 0.4816 0.4592 0.4830 -0.0185 0.0347  0.0156  41  GLN B CB  
3133 C CG  . GLN B 71  ? 0.5507 0.5197 0.5502 -0.0202 0.0376  0.0155  41  GLN B CG  
3134 C CD  . GLN B 71  ? 0.6533 0.6193 0.6505 -0.0211 0.0379  0.0192  41  GLN B CD  
3135 O OE1 . GLN B 71  ? 0.6726 0.6408 0.6706 -0.0229 0.0371  0.0190  41  GLN B OE1 
3136 N NE2 . GLN B 71  ? 0.6782 0.6396 0.6722 -0.0191 0.0389  0.0224  41  GLN B NE2 
3137 N N   . ILE B 72  ? 0.4071 0.4003 0.4095 -0.0127 0.0296  0.0204  42  ILE B N   
3138 C CA  . ILE B 72  ? 0.3910 0.3913 0.3943 -0.0117 0.0275  0.0223  42  ILE B CA  
3139 C C   . ILE B 72  ? 0.3838 0.3858 0.3857 -0.0117 0.0262  0.0276  42  ILE B C   
3140 O O   . ILE B 72  ? 0.3901 0.3933 0.3917 -0.0135 0.0246  0.0300  42  ILE B O   
3141 C CB  . ILE B 72  ? 0.3875 0.3937 0.3923 -0.0085 0.0274  0.0203  42  ILE B CB  
3142 C CG1 . ILE B 72  ? 0.3898 0.3965 0.3964 -0.0088 0.0280  0.0147  42  ILE B CG1 
3143 C CG2 . ILE B 72  ? 0.3875 0.4013 0.3927 -0.0070 0.0255  0.0240  42  ILE B CG2 
3144 C CD1 . ILE B 72  ? 0.3974 0.4084 0.4052 -0.0055 0.0281  0.0118  42  ILE B CD1 
3145 N N   . PHE B 73  ? 0.3766 0.3784 0.3773 -0.0096 0.0270  0.0292  43  PHE B N   
3146 C CA  . PHE B 73  ? 0.3709 0.3759 0.3703 -0.0090 0.0260  0.0338  43  PHE B CA  
3147 C C   . PHE B 73  ? 0.3699 0.3715 0.3682 -0.0121 0.0252  0.0357  43  PHE B C   
3148 O O   . PHE B 73  ? 0.3849 0.3906 0.3837 -0.0138 0.0233  0.0386  43  PHE B O   
3149 C CB  . PHE B 73  ? 0.3652 0.3692 0.3625 -0.0053 0.0273  0.0343  43  PHE B CB  
3150 C CG  . PHE B 73  ? 0.3637 0.3727 0.3596 -0.0042 0.0264  0.0388  43  PHE B CG  
3151 C CD1 . PHE B 73  ? 0.3660 0.3851 0.3635 -0.0039 0.0246  0.0417  43  PHE B CD1 
3152 C CD2 . PHE B 73  ? 0.3748 0.3794 0.3679 -0.0037 0.0272  0.0401  43  PHE B CD2 
3153 C CE1 . PHE B 73  ? 0.3753 0.4005 0.3720 -0.0034 0.0236  0.0456  43  PHE B CE1 
3154 C CE2 . PHE B 73  ? 0.3821 0.3929 0.3741 -0.0026 0.0262  0.0438  43  PHE B CE2 
3155 C CZ  . PHE B 73  ? 0.3763 0.3977 0.3704 -0.0027 0.0243  0.0464  43  PHE B CZ  
3156 N N   . PHE B 74  ? 0.3612 0.3555 0.3582 -0.0131 0.0267  0.0340  44  PHE B N   
3157 C CA  . PHE B 74  ? 0.3678 0.3590 0.3634 -0.0153 0.0261  0.0354  44  PHE B CA  
3158 C C   . PHE B 74  ? 0.3608 0.3517 0.3571 -0.0181 0.0243  0.0346  44  PHE B C   
3159 O O   . PHE B 74  ? 0.3608 0.3516 0.3560 -0.0198 0.0226  0.0366  44  PHE B O   
3160 C CB  . PHE B 74  ? 0.3799 0.3639 0.3735 -0.0150 0.0285  0.0344  44  PHE B CB  
3161 C CG  . PHE B 74  ? 0.3928 0.3767 0.3839 -0.0120 0.0294  0.0370  44  PHE B CG  
3162 C CD1 . PHE B 74  ? 0.4003 0.3882 0.3902 -0.0117 0.0278  0.0403  44  PHE B CD1 
3163 C CD2 . PHE B 74  ? 0.4017 0.3819 0.3913 -0.0092 0.0317  0.0359  44  PHE B CD2 
3164 C CE1 . PHE B 74  ? 0.4085 0.3979 0.3959 -0.0082 0.0286  0.0425  44  PHE B CE1 
3165 C CE2 . PHE B 74  ? 0.4129 0.3929 0.3992 -0.0055 0.0325  0.0383  44  PHE B CE2 
3166 C CZ  . PHE B 74  ? 0.4112 0.3965 0.3964 -0.0048 0.0310  0.0417  44  PHE B CZ  
3167 N N   . THR B 75  ? 0.3517 0.3433 0.3494 -0.0182 0.0245  0.0318  45  THR B N   
3168 C CA  . THR B 75  ? 0.3594 0.3512 0.3569 -0.0198 0.0227  0.0313  45  THR B CA  
3169 C C   . THR B 75  ? 0.3577 0.3537 0.3552 -0.0205 0.0203  0.0350  45  THR B C   
3170 O O   . THR B 75  ? 0.3617 0.3558 0.3576 -0.0225 0.0184  0.0364  45  THR B O   
3171 C CB  . THR B 75  ? 0.3850 0.3783 0.3840 -0.0189 0.0234  0.0275  45  THR B CB  
3172 O OG1 . THR B 75  ? 0.4171 0.4069 0.4163 -0.0194 0.0255  0.0242  45  THR B OG1 
3173 C CG2 . THR B 75  ? 0.3864 0.3802 0.3841 -0.0194 0.0215  0.0273  45  THR B CG2 
3174 N N   . ASN B 76  ? 0.3493 0.3511 0.3483 -0.0188 0.0206  0.0366  46  ASN B N   
3175 C CA  . ASN B 76  ? 0.3450 0.3522 0.3445 -0.0198 0.0188  0.0405  46  ASN B CA  
3176 C C   . ASN B 76  ? 0.3572 0.3648 0.3559 -0.0218 0.0176  0.0435  46  ASN B C   
3177 O O   . ASN B 76  ? 0.3612 0.3708 0.3597 -0.0244 0.0157  0.0463  46  ASN B O   
3178 C CB  . ASN B 76  ? 0.3373 0.3518 0.3385 -0.0170 0.0196  0.0413  46  ASN B CB  
3179 C CG  . ASN B 76  ? 0.3586 0.3741 0.3607 -0.0149 0.0203  0.0383  46  ASN B CG  
3180 O OD1 . ASN B 76  ? 0.3788 0.3909 0.3802 -0.0158 0.0200  0.0363  46  ASN B OD1 
3181 N ND2 . ASN B 76  ? 0.3470 0.3676 0.3504 -0.0115 0.0213  0.0375  46  ASN B ND2 
3182 N N   . VAL B 77  ? 0.3617 0.3676 0.3596 -0.0205 0.0188  0.0431  47  VAL B N   
3183 C CA  . VAL B 77  ? 0.3668 0.3741 0.3637 -0.0217 0.0177  0.0456  47  VAL B CA  
3184 C C   . VAL B 77  ? 0.3695 0.3712 0.3648 -0.0248 0.0159  0.0450  47  VAL B C   
3185 O O   . VAL B 77  ? 0.3746 0.3782 0.3697 -0.0276 0.0136  0.0471  47  VAL B O   
3186 C CB  . VAL B 77  ? 0.3768 0.3828 0.3723 -0.0186 0.0197  0.0452  47  VAL B CB  
3187 C CG1 . VAL B 77  ? 0.3814 0.3886 0.3755 -0.0194 0.0186  0.0471  47  VAL B CG1 
3188 C CG2 . VAL B 77  ? 0.3765 0.3878 0.3726 -0.0150 0.0210  0.0458  47  VAL B CG2 
3189 N N   . ILE B 78  ? 0.3633 0.3583 0.3574 -0.0244 0.0168  0.0419  48  ILE B N   
3190 C CA  . ILE B 78  ? 0.3695 0.3592 0.3614 -0.0264 0.0151  0.0410  48  ILE B CA  
3191 C C   . ILE B 78  ? 0.3785 0.3675 0.3698 -0.0288 0.0126  0.0418  48  ILE B C   
3192 O O   . ILE B 78  ? 0.3821 0.3688 0.3716 -0.0312 0.0102  0.0428  48  ILE B O   
3193 C CB  . ILE B 78  ? 0.3737 0.3582 0.3646 -0.0251 0.0170  0.0376  48  ILE B CB  
3194 C CG1 . ILE B 78  ? 0.3732 0.3566 0.3638 -0.0234 0.0194  0.0374  48  ILE B CG1 
3195 C CG2 . ILE B 78  ? 0.3842 0.3640 0.3724 -0.0262 0.0150  0.0363  48  ILE B CG2 
3196 C CD1 . ILE B 78  ? 0.3822 0.3621 0.3729 -0.0226 0.0218  0.0345  48  ILE B CD1 
3197 N N   . GLN B 79  ? 0.3814 0.3723 0.3738 -0.0280 0.0132  0.0416  49  GLN B N   
3198 C CA  . GLN B 79  ? 0.3891 0.3792 0.3805 -0.0298 0.0114  0.0430  49  GLN B CA  
3199 C C   . GLN B 79  ? 0.3897 0.3832 0.3817 -0.0331 0.0095  0.0469  49  GLN B C   
3200 O O   . GLN B 79  ? 0.4022 0.3913 0.3919 -0.0361 0.0072  0.0480  49  GLN B O   
3201 C CB  . GLN B 79  ? 0.4147 0.4085 0.4076 -0.0275 0.0129  0.0425  49  GLN B CB  
3202 C CG  . GLN B 79  ? 0.4719 0.4651 0.4634 -0.0286 0.0115  0.0445  49  GLN B CG  
3203 C CD  . GLN B 79  ? 0.5672 0.5522 0.5544 -0.0286 0.0102  0.0425  49  GLN B CD  
3204 O OE1 . GLN B 79  ? 0.5920 0.5746 0.5783 -0.0264 0.0110  0.0388  49  GLN B OE1 
3205 N NE2 . GLN B 79  ? 0.5868 0.5675 0.5712 -0.0311 0.0081  0.0450  49  GLN B NE2 
3206 N N   . ALA B 80  ? 0.3778 0.3790 0.3726 -0.0327 0.0104  0.0489  50  ALA B N   
3207 C CA  . ALA B 80  ? 0.3784 0.3857 0.3746 -0.0358 0.0089  0.0526  50  ALA B CA  
3208 C C   . ALA B 80  ? 0.3905 0.3953 0.3853 -0.0383 0.0070  0.0525  50  ALA B C   
3209 O O   . ALA B 80  ? 0.3847 0.3903 0.3794 -0.0427 0.0047  0.0545  50  ALA B O   
3210 C CB  . ALA B 80  ? 0.3733 0.3904 0.3722 -0.0332 0.0106  0.0542  50  ALA B CB  
3211 N N   . LEU B 81  ? 0.4055 0.4074 0.3992 -0.0358 0.0079  0.0501  51  LEU B N   
3212 C CA  . LEU B 81  ? 0.4280 0.4280 0.4200 -0.0374 0.0060  0.0496  51  LEU B CA  
3213 C C   . LEU B 81  ? 0.4381 0.4297 0.4272 -0.0403 0.0034  0.0484  51  LEU B C   
3214 O O   . LEU B 81  ? 0.4344 0.4257 0.4228 -0.0438 0.0008  0.0491  51  LEU B O   
3215 C CB  . LEU B 81  ? 0.4437 0.4413 0.4345 -0.0337 0.0079  0.0475  51  LEU B CB  
3216 C CG  . LEU B 81  ? 0.4812 0.4846 0.4733 -0.0301 0.0104  0.0484  51  LEU B CG  
3217 C CD1 . LEU B 81  ? 0.4947 0.4926 0.4848 -0.0268 0.0127  0.0463  51  LEU B CD1 
3218 C CD2 . LEU B 81  ? 0.4937 0.5051 0.4865 -0.0308 0.0091  0.0506  51  LEU B CD2 
3219 N N   . GLY B 82  ? 0.4523 0.4374 0.4395 -0.0386 0.0041  0.0464  52  GLY B N   
3220 C CA  . GLY B 82  ? 0.4731 0.4494 0.4563 -0.0400 0.0018  0.0450  52  GLY B CA  
3221 C C   . GLY B 82  ? 0.4888 0.4636 0.4714 -0.0441 -0.0003 0.0475  52  GLY B C   
3222 O O   . GLY B 82  ? 0.5052 0.4740 0.4848 -0.0471 -0.0031 0.0473  52  GLY B O   
3223 N N   . GLU B 83  ? 0.4810 0.4613 0.4663 -0.0445 0.0012  0.0500  53  GLU B N   
3224 C CA  . GLU B 83  ? 0.4809 0.4606 0.4658 -0.0488 -0.0003 0.0533  53  GLU B CA  
3225 C C   . GLU B 83  ? 0.4928 0.4763 0.4793 -0.0539 -0.0024 0.0553  53  GLU B C   
3226 O O   . GLU B 83  ? 0.5120 0.4895 0.4961 -0.0586 -0.0050 0.0562  53  GLU B O   
3227 C CB  . GLU B 83  ? 0.4895 0.4768 0.4775 -0.0474 0.0020  0.0558  53  GLU B CB  
3228 C CG  . GLU B 83  ? 0.5395 0.5227 0.5255 -0.0433 0.0035  0.0541  53  GLU B CG  
3229 C CD  . GLU B 83  ? 0.6097 0.6015 0.5989 -0.0408 0.0059  0.0557  53  GLU B CD  
3230 O OE1 . GLU B 83  ? 0.6232 0.6239 0.6159 -0.0423 0.0063  0.0587  53  GLU B OE1 
3231 O OE2 . GLU B 83  ? 0.6410 0.6312 0.6290 -0.0369 0.0072  0.0537  53  GLU B OE2 
3232 N N   . HIS B 84  ? 0.4800 0.4729 0.4700 -0.0530 -0.0016 0.0556  54  HIS B N   
3233 C CA  . HIS B 84  ? 0.4798 0.4790 0.4718 -0.0573 -0.0035 0.0570  54  HIS B CA  
3234 C C   . HIS B 84  ? 0.4848 0.4759 0.4734 -0.0596 -0.0066 0.0545  54  HIS B C   
3235 O O   . HIS B 84  ? 0.4916 0.4827 0.4802 -0.0652 -0.0092 0.0555  54  HIS B O   
3236 C CB  . HIS B 84  ? 0.4897 0.5002 0.4849 -0.0540 -0.0017 0.0574  54  HIS B CB  
3237 C CG  . HIS B 84  ? 0.5172 0.5376 0.5149 -0.0578 -0.0034 0.0591  54  HIS B CG  
3238 N ND1 . HIS B 84  ? 0.5382 0.5703 0.5396 -0.0597 -0.0027 0.0626  54  HIS B ND1 
3239 C CD2 . HIS B 84  ? 0.5262 0.5471 0.5232 -0.0598 -0.0057 0.0576  54  HIS B CD2 
3240 C CE1 . HIS B 84  ? 0.5409 0.5809 0.5440 -0.0630 -0.0046 0.0631  54  HIS B CE1 
3241 N NE2 . HIS B 84  ? 0.5376 0.5710 0.5382 -0.0632 -0.0065 0.0599  54  HIS B NE2 
3242 N N   . LEU B 85  ? 0.4827 0.4671 0.4683 -0.0553 -0.0063 0.0511  55  LEU B N   
3243 C CA  . LEU B 85  ? 0.4873 0.4642 0.4691 -0.0561 -0.0091 0.0483  55  LEU B CA  
3244 C C   . LEU B 85  ? 0.5148 0.4787 0.4915 -0.0577 -0.0112 0.0471  55  LEU B C   
3245 O O   . LEU B 85  ? 0.5202 0.4765 0.4927 -0.0575 -0.0138 0.0444  55  LEU B O   
3246 C CB  . LEU B 85  ? 0.4745 0.4513 0.4553 -0.0505 -0.0076 0.0455  55  LEU B CB  
3247 C CG  . LEU B 85  ? 0.4666 0.4539 0.4506 -0.0486 -0.0061 0.0463  55  LEU B CG  
3248 C CD1 . LEU B 85  ? 0.4665 0.4530 0.4498 -0.0428 -0.0032 0.0447  55  LEU B CD1 
3249 C CD2 . LEU B 85  ? 0.4654 0.4554 0.4490 -0.0511 -0.0092 0.0455  55  LEU B CD2 
3250 N N   . LYS B 86  ? 0.5292 0.4903 0.5054 -0.0586 -0.0103 0.0493  56  LYS B N   
3251 C CA  . LYS B 86  ? 0.5577 0.5064 0.5283 -0.0595 -0.0119 0.0489  56  LYS B CA  
3252 C C   . LYS B 86  ? 0.5730 0.5138 0.5387 -0.0538 -0.0119 0.0451  56  LYS B C   
3253 O O   . LYS B 86  ? 0.5862 0.5157 0.5458 -0.0539 -0.0144 0.0434  56  LYS B O   
3254 C CB  . LYS B 86  ? 0.5976 0.5398 0.5657 -0.0660 -0.0156 0.0496  56  LYS B CB  
3255 C CG  . LYS B 86  ? 0.6680 0.6168 0.6402 -0.0723 -0.0154 0.0540  56  LYS B CG  
3256 C CD  . LYS B 86  ? 0.7485 0.6956 0.7206 -0.0797 -0.0189 0.0541  56  LYS B CD  
3257 C CE  . LYS B 86  ? 0.8089 0.7668 0.7866 -0.0860 -0.0183 0.0586  56  LYS B CE  
3258 N NZ  . LYS B 86  ? 0.8437 0.8047 0.8231 -0.0931 -0.0215 0.0581  56  LYS B NZ  
3259 N N   . LEU B 87  ? 0.5683 0.5150 0.5364 -0.0490 -0.0091 0.0436  57  LEU B N   
3260 C CA  . LEU B 87  ? 0.5740 0.5157 0.5384 -0.0439 -0.0086 0.0402  57  LEU B CA  
3261 C C   . LEU B 87  ? 0.5851 0.5231 0.5470 -0.0412 -0.0073 0.0401  57  LEU B C   
3262 O O   . LEU B 87  ? 0.5903 0.5329 0.5553 -0.0417 -0.0054 0.0424  57  LEU B O   
3263 C CB  . LEU B 87  ? 0.5657 0.5151 0.5338 -0.0405 -0.0059 0.0388  57  LEU B CB  
3264 C CG  . LEU B 87  ? 0.5725 0.5264 0.5425 -0.0418 -0.0068 0.0389  57  LEU B CG  
3265 C CD1 . LEU B 87  ? 0.5768 0.5367 0.5495 -0.0382 -0.0037 0.0382  57  LEU B CD1 
3266 C CD2 . LEU B 87  ? 0.5808 0.5277 0.5461 -0.0422 -0.0103 0.0366  57  LEU B CD2 
3267 N N   . ARG B 88  ? 0.5901 0.5205 0.5463 -0.0377 -0.0084 0.0372  58  ARG B N   
3268 C CA  . ARG B 88  ? 0.5946 0.5216 0.5473 -0.0339 -0.0074 0.0363  58  ARG B CA  
3269 C C   . ARG B 88  ? 0.5704 0.5071 0.5282 -0.0306 -0.0037 0.0352  58  ARG B C   
3270 O O   . ARG B 88  ? 0.5632 0.5056 0.5247 -0.0303 -0.0023 0.0342  58  ARG B O   
3271 C CB  . ARG B 88  ? 0.6383 0.5560 0.5833 -0.0305 -0.0098 0.0331  58  ARG B CB  
3272 C CG  . ARG B 88  ? 0.7225 0.6381 0.6631 -0.0250 -0.0089 0.0311  58  ARG B CG  
3273 C CD  . ARG B 88  ? 0.8113 0.7169 0.7432 -0.0217 -0.0119 0.0282  58  ARG B CD  
3274 N NE  . ARG B 88  ? 0.8682 0.7786 0.8002 -0.0177 -0.0113 0.0247  58  ARG B NE  
3275 C CZ  . ARG B 88  ? 0.9118 0.8225 0.8442 -0.0185 -0.0127 0.0235  58  ARG B CZ  
3276 N NH1 . ARG B 88  ? 0.9268 0.8425 0.8592 -0.0147 -0.0117 0.0208  58  ARG B NH1 
3277 N NH2 . ARG B 88  ? 0.9075 0.8144 0.8404 -0.0232 -0.0150 0.0251  58  ARG B NH2 
3278 N N   . GLN B 89  ? 0.5580 0.4963 0.5156 -0.0283 -0.0020 0.0354  59  GLN B N   
3279 C CA  . GLN B 89  ? 0.5474 0.4946 0.5096 -0.0255 0.0013  0.0339  59  GLN B CA  
3280 C C   . GLN B 89  ? 0.5457 0.4949 0.5080 -0.0227 0.0022  0.0301  59  GLN B C   
3281 O O   . GLN B 89  ? 0.5456 0.5016 0.5129 -0.0225 0.0048  0.0292  59  GLN B O   
3282 C CB  . GLN B 89  ? 0.5579 0.5061 0.5187 -0.0227 0.0024  0.0339  59  GLN B CB  
3283 C CG  . GLN B 89  ? 0.5978 0.5558 0.5640 -0.0205 0.0055  0.0323  59  GLN B CG  
3284 C CD  . GLN B 89  ? 0.6626 0.6271 0.6350 -0.0232 0.0069  0.0350  59  GLN B CD  
3285 O OE1 . GLN B 89  ? 0.6874 0.6524 0.6603 -0.0254 0.0064  0.0386  59  GLN B OE1 
3286 N NE2 . GLN B 89  ? 0.6529 0.6228 0.6297 -0.0230 0.0088  0.0332  59  GLN B NE2 
3287 N N   . GLN B 90  ? 0.5401 0.4831 0.4965 -0.0206 0.0003  0.0279  60  GLN B N   
3288 C CA  . GLN B 90  ? 0.5331 0.4787 0.4892 -0.0178 0.0012  0.0246  60  GLN B CA  
3289 C C   . GLN B 90  ? 0.5027 0.4514 0.4627 -0.0199 0.0020  0.0251  60  GLN B C   
3290 O O   . GLN B 90  ? 0.4973 0.4512 0.4601 -0.0188 0.0044  0.0234  60  GLN B O   
3291 C CB  . GLN B 90  ? 0.5758 0.5143 0.5240 -0.0145 -0.0016 0.0224  60  GLN B CB  
3292 C CG  . GLN B 90  ? 0.6587 0.6022 0.6065 -0.0107 -0.0001 0.0189  60  GLN B CG  
3293 C CD  . GLN B 90  ? 0.7576 0.6954 0.6971 -0.0064 -0.0028 0.0165  60  GLN B CD  
3294 O OE1 . GLN B 90  ? 0.7941 0.7260 0.7277 -0.0040 -0.0045 0.0164  60  GLN B OE1 
3295 N NE2 . GLN B 90  ? 0.7692 0.7086 0.7075 -0.0048 -0.0031 0.0147  60  GLN B NE2 
3296 N N   . VAL B 91  ? 0.4773 0.4229 0.4373 -0.0231 0.0000  0.0274  61  VAL B N   
3297 C CA  . VAL B 91  ? 0.4558 0.4046 0.4189 -0.0246 0.0006  0.0282  61  VAL B CA  
3298 C C   . VAL B 91  ? 0.4239 0.3800 0.3932 -0.0255 0.0040  0.0296  61  VAL B C   
3299 O O   . VAL B 91  ? 0.4176 0.3772 0.3892 -0.0245 0.0064  0.0288  61  VAL B O   
3300 C CB  . VAL B 91  ? 0.4672 0.4123 0.4289 -0.0279 -0.0025 0.0301  61  VAL B CB  
3301 C CG1 . VAL B 91  ? 0.4756 0.4258 0.4407 -0.0288 -0.0016 0.0310  61  VAL B CG1 
3302 C CG2 . VAL B 91  ? 0.4786 0.4152 0.4334 -0.0268 -0.0062 0.0282  61  VAL B CG2 
3303 N N   . ILE B 92  ? 0.4024 0.3603 0.3739 -0.0271 0.0043  0.0316  62  ILE B N   
3304 C CA  . ILE B 92  ? 0.3862 0.3507 0.3629 -0.0273 0.0072  0.0327  62  ILE B CA  
3305 C C   . ILE B 92  ? 0.3731 0.3405 0.3515 -0.0248 0.0101  0.0298  62  ILE B C   
3306 O O   . ILE B 92  ? 0.3776 0.3484 0.3592 -0.0246 0.0126  0.0296  62  ILE B O   
3307 C CB  . ILE B 92  ? 0.3871 0.3532 0.3650 -0.0288 0.0067  0.0352  62  ILE B CB  
3308 C CG1 . ILE B 92  ? 0.4021 0.3659 0.3788 -0.0324 0.0039  0.0381  62  ILE B CG1 
3309 C CG2 . ILE B 92  ? 0.3862 0.3594 0.3689 -0.0282 0.0094  0.0359  62  ILE B CG2 
3310 C CD1 . ILE B 92  ? 0.4223 0.3877 0.4000 -0.0345 0.0034  0.0413  62  ILE B CD1 
3311 N N   . ALA B 93  ? 0.3668 0.3328 0.3426 -0.0227 0.0098  0.0273  63  ALA B N   
3312 C CA  . ALA B 93  ? 0.3714 0.3413 0.3490 -0.0208 0.0123  0.0241  63  ALA B CA  
3313 C C   . ALA B 93  ? 0.3739 0.3441 0.3518 -0.0206 0.0138  0.0226  63  ALA B C   
3314 O O   . ALA B 93  ? 0.3842 0.3579 0.3656 -0.0209 0.0167  0.0215  63  ALA B O   
3315 C CB  . ALA B 93  ? 0.3725 0.3417 0.3465 -0.0181 0.0113  0.0218  63  ALA B CB  
3316 N N   . THR B 94  ? 0.3662 0.3325 0.3403 -0.0202 0.0118  0.0228  64  THR B N   
3317 C CA  . THR B 94  ? 0.3614 0.3284 0.3353 -0.0197 0.0131  0.0220  64  THR B CA  
3318 C C   . THR B 94  ? 0.3577 0.3259 0.3350 -0.0213 0.0152  0.0242  64  THR B C   
3319 O O   . THR B 94  ? 0.3575 0.3277 0.3368 -0.0214 0.0182  0.0235  64  THR B O   
3320 C CB  . THR B 94  ? 0.3699 0.3326 0.3384 -0.0182 0.0099  0.0216  64  THR B CB  
3321 O OG1 . THR B 94  ? 0.3840 0.3465 0.3491 -0.0156 0.0089  0.0190  64  THR B OG1 
3322 C CG2 . THR B 94  ? 0.3615 0.3249 0.3294 -0.0175 0.0108  0.0217  64  THR B CG2 
3323 N N   . ALA B 95  ? 0.3537 0.3209 0.3315 -0.0227 0.0138  0.0270  65  ALA B N   
3324 C CA  . ALA B 95  ? 0.3539 0.3227 0.3342 -0.0235 0.0154  0.0292  65  ALA B CA  
3325 C C   . ALA B 95  ? 0.3468 0.3183 0.3308 -0.0235 0.0187  0.0287  65  ALA B C   
3326 O O   . ALA B 95  ? 0.3396 0.3112 0.3248 -0.0232 0.0212  0.0295  65  ALA B O   
3327 C CB  . ALA B 95  ? 0.3503 0.3195 0.3306 -0.0249 0.0130  0.0319  65  ALA B CB  
3328 N N   . THR B 96  ? 0.3415 0.3147 0.3269 -0.0236 0.0186  0.0275  66  THR B N   
3329 C CA  . THR B 96  ? 0.3426 0.3185 0.3313 -0.0234 0.0212  0.0263  66  THR B CA  
3330 C C   . THR B 96  ? 0.3501 0.3260 0.3397 -0.0235 0.0239  0.0235  66  THR B C   
3331 O O   . THR B 96  ? 0.3566 0.3322 0.3481 -0.0239 0.0266  0.0233  66  THR B O   
3332 C CB  . THR B 96  ? 0.3429 0.3214 0.3324 -0.0229 0.0201  0.0254  66  THR B CB  
3333 O OG1 . THR B 96  ? 0.3437 0.3223 0.3325 -0.0236 0.0178  0.0286  66  THR B OG1 
3334 C CG2 . THR B 96  ? 0.3381 0.3200 0.3310 -0.0224 0.0224  0.0234  66  THR B CG2 
3335 N N   . VAL B 97  ? 0.3522 0.3282 0.3399 -0.0230 0.0233  0.0214  67  VAL B N   
3336 C CA  . VAL B 97  ? 0.3552 0.3328 0.3440 -0.0235 0.0258  0.0188  67  VAL B CA  
3337 C C   . VAL B 97  ? 0.3578 0.3326 0.3461 -0.0242 0.0279  0.0207  67  VAL B C   
3338 O O   . VAL B 97  ? 0.3702 0.3448 0.3605 -0.0255 0.0311  0.0198  67  VAL B O   
3339 C CB  . VAL B 97  ? 0.3639 0.3436 0.3502 -0.0222 0.0244  0.0163  67  VAL B CB  
3340 C CG1 . VAL B 97  ? 0.3678 0.3505 0.3552 -0.0229 0.0271  0.0141  67  VAL B CG1 
3341 C CG2 . VAL B 97  ? 0.3612 0.3440 0.3479 -0.0210 0.0231  0.0142  67  VAL B CG2 
3342 N N   . TYR B 98  ? 0.3514 0.3237 0.3369 -0.0232 0.0262  0.0234  68  TYR B N   
3343 C CA  . TYR B 98  ? 0.3503 0.3203 0.3347 -0.0230 0.0281  0.0256  68  TYR B CA  
3344 C C   . TYR B 98  ? 0.3500 0.3181 0.3362 -0.0235 0.0308  0.0271  68  TYR B C   
3345 O O   . TYR B 98  ? 0.3525 0.3184 0.3388 -0.0240 0.0341  0.0276  68  TYR B O   
3346 C CB  . TYR B 98  ? 0.3503 0.3190 0.3315 -0.0216 0.0253  0.0279  68  TYR B CB  
3347 C CG  . TYR B 98  ? 0.3576 0.3264 0.3356 -0.0204 0.0225  0.0267  68  TYR B CG  
3348 C CD1 . TYR B 98  ? 0.3633 0.3341 0.3408 -0.0199 0.0232  0.0241  68  TYR B CD1 
3349 C CD2 . TYR B 98  ? 0.3667 0.3340 0.3419 -0.0195 0.0191  0.0280  68  TYR B CD2 
3350 C CE1 . TYR B 98  ? 0.3708 0.3416 0.3445 -0.0179 0.0205  0.0229  68  TYR B CE1 
3351 C CE2 . TYR B 98  ? 0.3783 0.3446 0.3498 -0.0180 0.0162  0.0265  68  TYR B CE2 
3352 C CZ  . TYR B 98  ? 0.3850 0.3529 0.3555 -0.0169 0.0169  0.0240  68  TYR B CZ  
3353 O OH  . TYR B 98  ? 0.3933 0.3599 0.3592 -0.0146 0.0139  0.0225  68  TYR B OH  
3354 N N   . PHE B 99  ? 0.3447 0.3136 0.3320 -0.0233 0.0294  0.0279  69  PHE B N   
3355 C CA  . PHE B 99  ? 0.3481 0.3156 0.3365 -0.0229 0.0313  0.0292  69  PHE B CA  
3356 C C   . PHE B 99  ? 0.3525 0.3188 0.3431 -0.0242 0.0344  0.0264  69  PHE B C   
3357 O O   . PHE B 99  ? 0.3517 0.3140 0.3419 -0.0242 0.0373  0.0271  69  PHE B O   
3358 C CB  . PHE B 99  ? 0.3491 0.3196 0.3383 -0.0223 0.0288  0.0303  69  PHE B CB  
3359 C CG  . PHE B 99  ? 0.3613 0.3317 0.3509 -0.0208 0.0302  0.0319  69  PHE B CG  
3360 C CD1 . PHE B 99  ? 0.3614 0.3317 0.3529 -0.0207 0.0318  0.0299  69  PHE B CD1 
3361 C CD2 . PHE B 99  ? 0.3679 0.3385 0.3554 -0.0191 0.0298  0.0351  69  PHE B CD2 
3362 C CE1 . PHE B 99  ? 0.3712 0.3407 0.3621 -0.0186 0.0329  0.0312  69  PHE B CE1 
3363 C CE2 . PHE B 99  ? 0.3713 0.3421 0.3584 -0.0169 0.0311  0.0365  69  PHE B CE2 
3364 C CZ  . PHE B 99  ? 0.3721 0.3420 0.3606 -0.0165 0.0326  0.0346  69  PHE B CZ  
3365 N N   . LYS B 100 ? 0.3521 0.3218 0.3449 -0.0253 0.0336  0.0231  70  LYS B N   
3366 C CA  . LYS B 100 ? 0.3484 0.3183 0.3438 -0.0271 0.0362  0.0197  70  LYS B CA  
3367 C C   . LYS B 100 ? 0.3623 0.3300 0.3576 -0.0291 0.0392  0.0191  70  LYS B C   
3368 O O   . LYS B 100 ? 0.3715 0.3360 0.3679 -0.0309 0.0421  0.0180  70  LYS B O   
3369 C CB  . LYS B 100 ? 0.3383 0.3140 0.3358 -0.0273 0.0345  0.0162  70  LYS B CB  
3370 C CG  . LYS B 100 ? 0.3468 0.3250 0.3450 -0.0256 0.0324  0.0164  70  LYS B CG  
3371 C CD  . LYS B 100 ? 0.3675 0.3513 0.3673 -0.0253 0.0314  0.0127  70  LYS B CD  
3372 C CE  . LYS B 100 ? 0.3874 0.3742 0.3876 -0.0232 0.0293  0.0134  70  LYS B CE  
3373 N NZ  . LYS B 100 ? 0.3907 0.3768 0.3923 -0.0226 0.0304  0.0140  70  LYS B NZ  
3374 N N   . ARG B 101 ? 0.3683 0.3376 0.3619 -0.0289 0.0384  0.0197  71  ARG B N   
3375 C CA  . ARG B 101 ? 0.3716 0.3401 0.3649 -0.0306 0.0412  0.0196  71  ARG B CA  
3376 C C   . ARG B 101 ? 0.3811 0.3429 0.3723 -0.0304 0.0440  0.0231  71  ARG B C   
3377 O O   . ARG B 101 ? 0.3801 0.3388 0.3720 -0.0328 0.0476  0.0229  71  ARG B O   
3378 C CB  . ARG B 101 ? 0.3830 0.3553 0.3742 -0.0293 0.0393  0.0198  71  ARG B CB  
3379 C CG  . ARG B 101 ? 0.3896 0.3682 0.3820 -0.0291 0.0372  0.0161  71  ARG B CG  
3380 C CD  . ARG B 101 ? 0.4123 0.3938 0.4015 -0.0270 0.0353  0.0161  71  ARG B CD  
3381 N NE  . ARG B 101 ? 0.4277 0.4155 0.4173 -0.0263 0.0339  0.0123  71  ARG B NE  
3382 C CZ  . ARG B 101 ? 0.4072 0.3980 0.3936 -0.0237 0.0318  0.0115  71  ARG B CZ  
3383 N NH1 . ARG B 101 ? 0.3468 0.3349 0.3295 -0.0219 0.0307  0.0139  71  ARG B NH1 
3384 N NH2 . ARG B 101 ? 0.4093 0.4061 0.3955 -0.0224 0.0307  0.0080  71  ARG B NH2 
3385 N N   . PHE B 102 ? 0.3902 0.3497 0.3788 -0.0276 0.0424  0.0263  72  PHE B N   
3386 C CA  . PHE B 102 ? 0.4048 0.3583 0.3907 -0.0262 0.0449  0.0298  72  PHE B CA  
3387 C C   . PHE B 102 ? 0.4032 0.3512 0.3898 -0.0273 0.0477  0.0290  72  PHE B C   
3388 O O   . PHE B 102 ? 0.4092 0.3512 0.3943 -0.0284 0.0514  0.0302  72  PHE B O   
3389 C CB  . PHE B 102 ? 0.4082 0.3623 0.3914 -0.0227 0.0423  0.0329  72  PHE B CB  
3390 C CG  . PHE B 102 ? 0.4249 0.3739 0.4045 -0.0204 0.0449  0.0364  72  PHE B CG  
3391 C CD1 . PHE B 102 ? 0.4392 0.3877 0.4161 -0.0193 0.0461  0.0385  72  PHE B CD1 
3392 C CD2 . PHE B 102 ? 0.4439 0.3886 0.4221 -0.0188 0.0464  0.0377  72  PHE B CD2 
3393 C CE1 . PHE B 102 ? 0.4603 0.4040 0.4332 -0.0165 0.0487  0.0420  72  PHE B CE1 
3394 C CE2 . PHE B 102 ? 0.4615 0.4009 0.4352 -0.0158 0.0489  0.0411  72  PHE B CE2 
3395 C CZ  . PHE B 102 ? 0.4612 0.4001 0.4324 -0.0147 0.0502  0.0433  72  PHE B CZ  
3396 N N   . TYR B 103 ? 0.3916 0.3412 0.3800 -0.0269 0.0460  0.0272  73  TYR B N   
3397 C CA  . TYR B 103 ? 0.3952 0.3397 0.3839 -0.0272 0.0481  0.0261  73  TYR B CA  
3398 C C   . TYR B 103 ? 0.4203 0.3644 0.4123 -0.0315 0.0500  0.0217  73  TYR B C   
3399 O O   . TYR B 103 ? 0.4245 0.3632 0.4165 -0.0324 0.0520  0.0202  73  TYR B O   
3400 C CB  . TYR B 103 ? 0.3782 0.3251 0.3669 -0.0243 0.0455  0.0263  73  TYR B CB  
3401 C CG  . TYR B 103 ? 0.3653 0.3119 0.3505 -0.0205 0.0445  0.0306  73  TYR B CG  
3402 C CD1 . TYR B 103 ? 0.3661 0.3057 0.3470 -0.0184 0.0472  0.0334  73  TYR B CD1 
3403 C CD2 . TYR B 103 ? 0.3618 0.3151 0.3475 -0.0193 0.0410  0.0320  73  TYR B CD2 
3404 C CE1 . TYR B 103 ? 0.3762 0.3170 0.3538 -0.0145 0.0463  0.0371  73  TYR B CE1 
3405 C CE2 . TYR B 103 ? 0.3683 0.3226 0.3511 -0.0164 0.0399  0.0355  73  TYR B CE2 
3406 C CZ  . TYR B 103 ? 0.3849 0.3337 0.3637 -0.0137 0.0425  0.0380  73  TYR B CZ  
3407 O OH  . TYR B 103 ? 0.4016 0.3528 0.3775 -0.0103 0.0415  0.0412  73  TYR B OH  
3408 N N   . ALA B 104 ? 0.4335 0.3836 0.4281 -0.0340 0.0495  0.0195  74  ALA B N   
3409 C CA  . ALA B 104 ? 0.4540 0.4055 0.4521 -0.0384 0.0516  0.0153  74  ALA B CA  
3410 C C   . ALA B 104 ? 0.4833 0.4276 0.4797 -0.0412 0.0559  0.0172  74  ALA B C   
3411 O O   . ALA B 104 ? 0.4902 0.4305 0.4882 -0.0450 0.0586  0.0147  74  ALA B O   
3412 C CB  . ALA B 104 ? 0.4491 0.4102 0.4497 -0.0393 0.0498  0.0128  74  ALA B CB  
3413 N N   . ARG B 105 ? 0.4977 0.4401 0.4908 -0.0394 0.0567  0.0215  75  ARG B N   
3414 C CA  . ARG B 105 ? 0.5231 0.4587 0.5140 -0.0415 0.0610  0.0242  75  ARG B CA  
3415 C C   . ARG B 105 ? 0.5329 0.4579 0.5187 -0.0385 0.0628  0.0281  75  ARG B C   
3416 O O   . ARG B 105 ? 0.5482 0.4647 0.5319 -0.0407 0.0669  0.0296  75  ARG B O   
3417 C CB  . ARG B 105 ? 0.5624 0.5032 0.5522 -0.0409 0.0611  0.0265  75  ARG B CB  
3418 C CG  . ARG B 105 ? 0.6430 0.5928 0.6370 -0.0447 0.0611  0.0229  75  ARG B CG  
3419 C CD  . ARG B 105 ? 0.7218 0.6781 0.7143 -0.0427 0.0602  0.0248  75  ARG B CD  
3420 N NE  . ARG B 105 ? 0.7981 0.7491 0.7869 -0.0419 0.0634  0.0296  75  ARG B NE  
3421 C CZ  . ARG B 105 ? 0.8557 0.8118 0.8432 -0.0408 0.0639  0.0314  75  ARG B CZ  
3422 N NH1 . ARG B 105 ? 0.8705 0.8217 0.8543 -0.0396 0.0670  0.0361  75  ARG B NH1 
3423 N NH2 . ARG B 105 ? 0.8542 0.8203 0.8434 -0.0404 0.0613  0.0287  75  ARG B NH2 
3424 N N   . TYR B 106 ? 0.5282 0.4536 0.5117 -0.0335 0.0600  0.0299  76  TYR B N   
3425 C CA  . TYR B 106 ? 0.5352 0.4521 0.5132 -0.0295 0.0615  0.0337  76  TYR B CA  
3426 C C   . TYR B 106 ? 0.5210 0.4356 0.4983 -0.0268 0.0599  0.0325  76  TYR B C   
3427 O O   . TYR B 106 ? 0.5169 0.4383 0.4978 -0.0269 0.0568  0.0296  76  TYR B O   
3428 C CB  . TYR B 106 ? 0.5496 0.4695 0.5242 -0.0251 0.0603  0.0380  76  TYR B CB  
3429 C CG  . TYR B 106 ? 0.5790 0.5008 0.5536 -0.0270 0.0621  0.0394  76  TYR B CG  
3430 C CD1 . TYR B 106 ? 0.6002 0.5142 0.5715 -0.0278 0.0668  0.0423  76  TYR B CD1 
3431 C CD2 . TYR B 106 ? 0.6003 0.5315 0.5781 -0.0282 0.0594  0.0375  76  TYR B CD2 
3432 C CE1 . TYR B 106 ? 0.6185 0.5353 0.5900 -0.0297 0.0687  0.0436  76  TYR B CE1 
3433 C CE2 . TYR B 106 ? 0.6185 0.5525 0.5963 -0.0297 0.0611  0.0384  76  TYR B CE2 
3434 C CZ  . TYR B 106 ? 0.6375 0.5649 0.6124 -0.0305 0.0658  0.0416  76  TYR B CZ  
3435 O OH  . TYR B 106 ? 0.6762 0.6074 0.6511 -0.0318 0.0676  0.0428  76  TYR B OH  
3436 N N   . SER B 107 ? 0.5083 0.4133 0.4804 -0.0239 0.0623  0.0350  77  SER B N   
3437 C CA  . SER B 107 ? 0.5023 0.4043 0.4724 -0.0203 0.0611  0.0342  77  SER B CA  
3438 C C   . SER B 107 ? 0.4888 0.3993 0.4583 -0.0153 0.0573  0.0362  77  SER B C   
3439 O O   . SER B 107 ? 0.4831 0.3973 0.4510 -0.0132 0.0567  0.0394  77  SER B O   
3440 C CB  . SER B 107 ? 0.5229 0.4113 0.4862 -0.0179 0.0648  0.0366  77  SER B CB  
3441 O OG  . SER B 107 ? 0.5603 0.4464 0.5204 -0.0129 0.0635  0.0365  77  SER B OG  
3442 N N   . LEU B 108 ? 0.4786 0.3924 0.4492 -0.0133 0.0550  0.0343  78  LEU B N   
3443 C CA  . LEU B 108 ? 0.4705 0.3926 0.4407 -0.0088 0.0517  0.0362  78  LEU B CA  
3444 C C   . LEU B 108 ? 0.4791 0.3979 0.4428 -0.0033 0.0529  0.0407  78  LEU B C   
3445 O O   . LEU B 108 ? 0.4791 0.4061 0.4426 -0.0004 0.0504  0.0429  78  LEU B O   
3446 C CB  . LEU B 108 ? 0.4628 0.3875 0.4345 -0.0072 0.0500  0.0336  78  LEU B CB  
3447 C CG  . LEU B 108 ? 0.4750 0.4070 0.4531 -0.0111 0.0478  0.0296  78  LEU B CG  
3448 C CD1 . LEU B 108 ? 0.4805 0.4127 0.4593 -0.0095 0.0471  0.0265  78  LEU B CD1 
3449 C CD2 . LEU B 108 ? 0.4674 0.4105 0.4484 -0.0113 0.0443  0.0310  78  LEU B CD2 
3450 N N   . LYS B 109 ? 0.4864 0.3934 0.4448 -0.0019 0.0567  0.0421  79  LYS B N   
3451 C CA  . LYS B 109 ? 0.4999 0.4033 0.4512 0.0040  0.0581  0.0464  79  LYS B CA  
3452 C C   . LYS B 109 ? 0.4958 0.4008 0.4462 0.0037  0.0591  0.0494  79  LYS B C   
3453 O O   . LYS B 109 ? 0.5006 0.4062 0.4459 0.0091  0.0595  0.0529  79  LYS B O   
3454 C CB  . LYS B 109 ? 0.5391 0.4278 0.4837 0.0067  0.0619  0.0469  79  LYS B CB  
3455 C CG  . LYS B 109 ? 0.6122 0.4892 0.5552 0.0025  0.0662  0.0474  79  LYS B CG  
3456 C CD  . LYS B 109 ? 0.6970 0.5581 0.6314 0.0062  0.0700  0.0491  79  LYS B CD  
3457 C CE  . LYS B 109 ? 0.7874 0.6373 0.7207 0.0009  0.0745  0.0501  79  LYS B CE  
3458 N NZ  . LYS B 109 ? 0.8475 0.6795 0.7715 0.0041  0.0787  0.0523  79  LYS B NZ  
3459 N N   . SER B 110 ? 0.4799 0.3860 0.4346 -0.0019 0.0596  0.0481  80  SER B N   
3460 C CA  . SER B 110 ? 0.4770 0.3845 0.4304 -0.0019 0.0606  0.0507  80  SER B CA  
3461 C C   . SER B 110 ? 0.4627 0.3813 0.4163 0.0016  0.0568  0.0523  80  SER B C   
3462 O O   . SER B 110 ? 0.4586 0.3771 0.4074 0.0063  0.0577  0.0557  80  SER B O   
3463 C CB  . SER B 110 ? 0.5008 0.4097 0.4593 -0.0083 0.0611  0.0484  80  SER B CB  
3464 O OG  . SER B 110 ? 0.5558 0.4746 0.5200 -0.0107 0.0570  0.0454  80  SER B OG  
3465 N N   . ILE B 111 ? 0.4469 0.3747 0.4057 -0.0004 0.0528  0.0499  81  ILE B N   
3466 C CA  . ILE B 111 ? 0.4346 0.3728 0.3942 0.0017  0.0489  0.0509  81  ILE B CA  
3467 C C   . ILE B 111 ? 0.4254 0.3692 0.3881 0.0015  0.0460  0.0492  81  ILE B C   
3468 O O   . ILE B 111 ? 0.4307 0.3736 0.3971 -0.0020 0.0457  0.0463  81  ILE B O   
3469 C CB  . ILE B 111 ? 0.4396 0.3832 0.4025 -0.0015 0.0466  0.0499  81  ILE B CB  
3470 C CG1 . ILE B 111 ? 0.4525 0.3923 0.4119 -0.0004 0.0493  0.0520  81  ILE B CG1 
3471 C CG2 . ILE B 111 ? 0.4431 0.3969 0.4077 -0.0009 0.0420  0.0500  81  ILE B CG2 
3472 C CD1 . ILE B 111 ? 0.4613 0.4062 0.4233 -0.0030 0.0471  0.0507  81  ILE B CD1 
3473 N N   . ASP B 112 ? 0.4149 0.3657 0.3762 0.0054  0.0439  0.0510  82  ASP B N   
3474 C CA  . ASP B 112 ? 0.4147 0.3727 0.3789 0.0054  0.0412  0.0500  82  ASP B CA  
3475 C C   . ASP B 112 ? 0.4145 0.3780 0.3847 0.0000  0.0382  0.0477  82  ASP B C   
3476 O O   . ASP B 112 ? 0.4179 0.3860 0.3894 -0.0018 0.0359  0.0481  82  ASP B O   
3477 C CB  . ASP B 112 ? 0.4220 0.3891 0.3841 0.0097  0.0393  0.0525  82  ASP B CB  
3478 C CG  . ASP B 112 ? 0.4631 0.4389 0.4276 0.0104  0.0368  0.0523  82  ASP B CG  
3479 O OD1 . ASP B 112 ? 0.4600 0.4352 0.4281 0.0074  0.0363  0.0501  82  ASP B OD1 
3480 O OD2 . ASP B 112 ? 0.4799 0.4640 0.4426 0.0141  0.0355  0.0543  82  ASP B OD2 
3481 N N   . PRO B 113 ? 0.4058 0.3685 0.3792 -0.0023 0.0380  0.0452  83  PRO B N   
3482 C CA  . PRO B 113 ? 0.3968 0.3644 0.3749 -0.0066 0.0353  0.0433  83  PRO B CA  
3483 C C   . PRO B 113 ? 0.3964 0.3737 0.3762 -0.0069 0.0316  0.0449  83  PRO B C   
3484 O O   . PRO B 113 ? 0.3955 0.3754 0.3779 -0.0103 0.0293  0.0440  83  PRO B O   
3485 C CB  . PRO B 113 ? 0.4011 0.3671 0.3815 -0.0073 0.0360  0.0406  83  PRO B CB  
3486 C CG  . PRO B 113 ? 0.4058 0.3684 0.3826 -0.0029 0.0380  0.0416  83  PRO B CG  
3487 C CD  . PRO B 113 ? 0.3958 0.3527 0.3679 -0.0007 0.0403  0.0439  83  PRO B CD  
3488 N N   . VAL B 114 ? 0.3903 0.3730 0.3683 -0.0033 0.0311  0.0473  84  VAL B N   
3489 C CA  . VAL B 114 ? 0.3767 0.3695 0.3562 -0.0040 0.0278  0.0490  84  VAL B CA  
3490 C C   . VAL B 114 ? 0.3623 0.3559 0.3412 -0.0057 0.0262  0.0495  84  VAL B C   
3491 O O   . VAL B 114 ? 0.3604 0.3594 0.3416 -0.0089 0.0231  0.0497  84  VAL B O   
3492 C CB  . VAL B 114 ? 0.3820 0.3816 0.3595 0.0007  0.0280  0.0513  84  VAL B CB  
3493 C CG1 . VAL B 114 ? 0.3776 0.3889 0.3566 -0.0003 0.0249  0.0532  84  VAL B CG1 
3494 C CG2 . VAL B 114 ? 0.3843 0.3847 0.3628 0.0022  0.0287  0.0505  84  VAL B CG2 
3495 N N   . LEU B 115 ? 0.3525 0.3402 0.3281 -0.0035 0.0284  0.0498  85  LEU B N   
3496 C CA  . LEU B 115 ? 0.3478 0.3356 0.3221 -0.0043 0.0272  0.0499  85  LEU B CA  
3497 C C   . LEU B 115 ? 0.3622 0.3444 0.3382 -0.0081 0.0269  0.0476  85  LEU B C   
3498 O O   . LEU B 115 ? 0.3677 0.3516 0.3442 -0.0102 0.0242  0.0469  85  LEU B O   
3499 C CB  . LEU B 115 ? 0.3438 0.3281 0.3132 0.0006  0.0301  0.0516  85  LEU B CB  
3500 C CG  . LEU B 115 ? 0.3527 0.3365 0.3201 0.0011  0.0295  0.0518  85  LEU B CG  
3501 C CD1 . LEU B 115 ? 0.3449 0.3378 0.3137 -0.0001 0.0253  0.0517  85  LEU B CD1 
3502 C CD2 . LEU B 115 ? 0.3589 0.3388 0.3210 0.0065  0.0331  0.0540  85  LEU B CD2 
3503 N N   . MET B 116 ? 0.3688 0.3446 0.3452 -0.0087 0.0296  0.0462  86  MET B N   
3504 C CA  . MET B 116 ? 0.3724 0.3444 0.3504 -0.0118 0.0296  0.0438  86  MET B CA  
3505 C C   . MET B 116 ? 0.3704 0.3459 0.3513 -0.0151 0.0261  0.0423  86  MET B C   
3506 O O   . MET B 116 ? 0.3890 0.3636 0.3696 -0.0168 0.0244  0.0411  86  MET B O   
3507 C CB  . MET B 116 ? 0.3714 0.3371 0.3498 -0.0123 0.0332  0.0422  86  MET B CB  
3508 C CG  . MET B 116 ? 0.3770 0.3404 0.3568 -0.0153 0.0335  0.0397  86  MET B CG  
3509 S SD  . MET B 116 ? 0.3825 0.3450 0.3595 -0.0145 0.0335  0.0406  86  MET B SD  
3510 C CE  . MET B 116 ? 0.3795 0.3358 0.3536 -0.0124 0.0385  0.0425  86  MET B CE  
3511 N N   . ALA B 117 ? 0.3554 0.3348 0.3385 -0.0157 0.0251  0.0425  87  ALA B N   
3512 C CA  . ALA B 117 ? 0.3524 0.3345 0.3379 -0.0187 0.0222  0.0417  87  ALA B CA  
3513 C C   . ALA B 117 ? 0.3677 0.3519 0.3524 -0.0206 0.0186  0.0423  87  ALA B C   
3514 O O   . ALA B 117 ? 0.3787 0.3598 0.3630 -0.0224 0.0171  0.0406  87  ALA B O   
3515 C CB  . ALA B 117 ? 0.3392 0.3260 0.3270 -0.0185 0.0220  0.0425  87  ALA B CB  
3516 N N   . PRO B 118 ? 0.3643 0.3534 0.3484 -0.0200 0.0172  0.0444  88  PRO B N   
3517 C CA  . PRO B 118 ? 0.3653 0.3555 0.3486 -0.0223 0.0136  0.0443  88  PRO B CA  
3518 C C   . PRO B 118 ? 0.3695 0.3549 0.3500 -0.0212 0.0136  0.0427  88  PRO B C   
3519 O O   . PRO B 118 ? 0.3709 0.3542 0.3502 -0.0231 0.0107  0.0415  88  PRO B O   
3520 C CB  . PRO B 118 ? 0.3659 0.3640 0.3495 -0.0216 0.0126  0.0465  88  PRO B CB  
3521 C CG  . PRO B 118 ? 0.3694 0.3686 0.3522 -0.0174 0.0160  0.0477  88  PRO B CG  
3522 C CD  . PRO B 118 ? 0.3525 0.3467 0.3363 -0.0172 0.0184  0.0466  88  PRO B CD  
3523 N N   . THR B 119 ? 0.3667 0.3496 0.3456 -0.0180 0.0169  0.0429  89  THR B N   
3524 C CA  . THR B 119 ? 0.3681 0.3474 0.3444 -0.0166 0.0174  0.0418  89  THR B CA  
3525 C C   . THR B 119 ? 0.3696 0.3445 0.3460 -0.0184 0.0169  0.0393  89  THR B C   
3526 O O   . THR B 119 ? 0.3693 0.3426 0.3436 -0.0183 0.0151  0.0380  89  THR B O   
3527 C CB  . THR B 119 ? 0.3760 0.3531 0.3505 -0.0132 0.0216  0.0431  89  THR B CB  
3528 O OG1 . THR B 119 ? 0.3921 0.3731 0.3655 -0.0105 0.0222  0.0454  89  THR B OG1 
3529 C CG2 . THR B 119 ? 0.3667 0.3412 0.3385 -0.0117 0.0223  0.0425  89  THR B CG2 
3530 N N   . CYS B 120 ? 0.3678 0.3415 0.3465 -0.0196 0.0186  0.0385  90  CYS B N   
3531 C CA  . CYS B 120 ? 0.3691 0.3401 0.3480 -0.0208 0.0183  0.0360  90  CYS B CA  
3532 C C   . CYS B 120 ? 0.3777 0.3483 0.3557 -0.0226 0.0141  0.0353  90  CYS B C   
3533 O O   . CYS B 120 ? 0.3834 0.3513 0.3591 -0.0223 0.0126  0.0333  90  CYS B O   
3534 C CB  . CYS B 120 ? 0.3644 0.3355 0.3462 -0.0214 0.0207  0.0351  90  CYS B CB  
3535 S SG  . CYS B 120 ? 0.3637 0.3323 0.3457 -0.0202 0.0257  0.0349  90  CYS B SG  
3536 N N   . VAL B 121 ? 0.3758 0.3490 0.3552 -0.0243 0.0123  0.0369  91  VAL B N   
3537 C CA  . VAL B 121 ? 0.3710 0.3430 0.3494 -0.0268 0.0085  0.0367  91  VAL B CA  
3538 C C   . VAL B 121 ? 0.3762 0.3461 0.3513 -0.0266 0.0056  0.0359  91  VAL B C   
3539 O O   . VAL B 121 ? 0.3791 0.3444 0.3513 -0.0273 0.0029  0.0343  91  VAL B O   
3540 C CB  . VAL B 121 ? 0.3665 0.3432 0.3475 -0.0290 0.0076  0.0392  91  VAL B CB  
3541 C CG1 . VAL B 121 ? 0.3613 0.3363 0.3410 -0.0324 0.0036  0.0396  91  VAL B CG1 
3542 C CG2 . VAL B 121 ? 0.3679 0.3462 0.3515 -0.0289 0.0097  0.0395  91  VAL B CG2 
3543 N N   . PHE B 122 ? 0.3693 0.3425 0.3443 -0.0254 0.0059  0.0370  92  PHE B N   
3544 C CA  . PHE B 122 ? 0.3674 0.3401 0.3394 -0.0247 0.0032  0.0361  92  PHE B CA  
3545 C C   . PHE B 122 ? 0.3672 0.3354 0.3359 -0.0222 0.0033  0.0338  92  PHE B C   
3546 O O   . PHE B 122 ? 0.3797 0.3445 0.3452 -0.0224 -0.0002 0.0320  92  PHE B O   
3547 C CB  . PHE B 122 ? 0.3616 0.3400 0.3342 -0.0226 0.0045  0.0378  92  PHE B CB  
3548 C CG  . PHE B 122 ? 0.3723 0.3518 0.3419 -0.0208 0.0023  0.0369  92  PHE B CG  
3549 C CD1 . PHE B 122 ? 0.3842 0.3647 0.3532 -0.0235 -0.0021 0.0359  92  PHE B CD1 
3550 C CD2 . PHE B 122 ? 0.3839 0.3638 0.3515 -0.0165 0.0047  0.0370  92  PHE B CD2 
3551 C CE1 . PHE B 122 ? 0.3974 0.3794 0.3636 -0.0216 -0.0045 0.0344  92  PHE B CE1 
3552 C CE2 . PHE B 122 ? 0.3959 0.3777 0.3607 -0.0143 0.0026  0.0361  92  PHE B CE2 
3553 C CZ  . PHE B 122 ? 0.3944 0.3776 0.3586 -0.0166 -0.0021 0.0346  92  PHE B CZ  
3554 N N   . LEU B 123 ? 0.3540 0.3221 0.3233 -0.0200 0.0071  0.0337  93  LEU B N   
3555 C CA  . LEU B 123 ? 0.3485 0.3141 0.3149 -0.0176 0.0076  0.0317  93  LEU B CA  
3556 C C   . LEU B 123 ? 0.3613 0.3233 0.3264 -0.0185 0.0058  0.0295  93  LEU B C   
3557 O O   . LEU B 123 ? 0.3679 0.3273 0.3291 -0.0168 0.0035  0.0275  93  LEU B O   
3558 C CB  . LEU B 123 ? 0.3343 0.3014 0.3021 -0.0159 0.0125  0.0325  93  LEU B CB  
3559 C CG  . LEU B 123 ? 0.3371 0.3038 0.3027 -0.0137 0.0138  0.0309  93  LEU B CG  
3560 C CD1 . LEU B 123 ? 0.3338 0.3009 0.2954 -0.0108 0.0115  0.0305  93  LEU B CD1 
3561 C CD2 . LEU B 123 ? 0.3424 0.3102 0.3101 -0.0134 0.0190  0.0321  93  LEU B CD2 
3562 N N   . ALA B 124 ? 0.3607 0.3226 0.3284 -0.0204 0.0068  0.0297  94  ALA B N   
3563 C CA  . ALA B 124 ? 0.3747 0.3335 0.3407 -0.0205 0.0054  0.0277  94  ALA B CA  
3564 C C   . ALA B 124 ? 0.4009 0.3546 0.3628 -0.0213 0.0008  0.0271  94  ALA B C   
3565 O O   . ALA B 124 ? 0.4050 0.3548 0.3627 -0.0195 -0.0010 0.0249  94  ALA B O   
3566 C CB  . ALA B 124 ? 0.3658 0.3262 0.3354 -0.0221 0.0072  0.0284  94  ALA B CB  
3567 N N   . SER B 125 ? 0.4107 0.3646 0.3736 -0.0240 -0.0012 0.0288  95  SER B N   
3568 C CA  . SER B 125 ? 0.4231 0.3717 0.3824 -0.0259 -0.0057 0.0283  95  SER B CA  
3569 C C   . SER B 125 ? 0.4240 0.3693 0.3782 -0.0230 -0.0081 0.0257  95  SER B C   
3570 O O   . SER B 125 ? 0.4268 0.3653 0.3762 -0.0229 -0.0116 0.0240  95  SER B O   
3571 C CB  . SER B 125 ? 0.4524 0.4042 0.4147 -0.0297 -0.0068 0.0306  95  SER B CB  
3572 O OG  . SER B 125 ? 0.5301 0.4769 0.4892 -0.0322 -0.0113 0.0297  95  SER B OG  
3573 N N   . LYS B 126 ? 0.4170 0.3668 0.3718 -0.0201 -0.0062 0.0256  96  LYS B N   
3574 C CA  . LYS B 126 ? 0.4244 0.3726 0.3745 -0.0166 -0.0083 0.0233  96  LYS B CA  
3575 C C   . LYS B 126 ? 0.4409 0.3868 0.3875 -0.0131 -0.0077 0.0211  96  LYS B C   
3576 O O   . LYS B 126 ? 0.4464 0.3875 0.3873 -0.0108 -0.0111 0.0187  96  LYS B O   
3577 C CB  . LYS B 126 ? 0.4221 0.3764 0.3737 -0.0144 -0.0061 0.0244  96  LYS B CB  
3578 C CG  . LYS B 126 ? 0.4334 0.3910 0.3877 -0.0170 -0.0070 0.0262  96  LYS B CG  
3579 C CD  . LYS B 126 ? 0.4450 0.4073 0.3986 -0.0140 -0.0066 0.0265  96  LYS B CD  
3580 C CE  . LYS B 126 ? 0.4497 0.4169 0.4065 -0.0126 -0.0015 0.0292  96  LYS B CE  
3581 N NZ  . LYS B 126 ? 0.4582 0.4308 0.4149 -0.0104 -0.0012 0.0305  96  LYS B NZ  
3582 N N   . VAL B 127 ? 0.4390 0.3888 0.3889 -0.0126 -0.0035 0.0217  97  VAL B N   
3583 C CA  . VAL B 127 ? 0.4362 0.3865 0.3839 -0.0096 -0.0024 0.0197  97  VAL B CA  
3584 C C   . VAL B 127 ? 0.4512 0.3953 0.3948 -0.0094 -0.0054 0.0180  97  VAL B C   
3585 O O   . VAL B 127 ? 0.4475 0.3890 0.3855 -0.0057 -0.0074 0.0156  97  VAL B O   
3586 C CB  . VAL B 127 ? 0.4277 0.3840 0.3808 -0.0104 0.0027  0.0206  97  VAL B CB  
3587 C CG1 . VAL B 127 ? 0.4245 0.3831 0.3760 -0.0079 0.0039  0.0181  97  VAL B CG1 
3588 C CG2 . VAL B 127 ? 0.4214 0.3821 0.3772 -0.0102 0.0058  0.0225  97  VAL B CG2 
3589 N N   . GLU B 128 ? 0.4697 0.4112 0.4155 -0.0130 -0.0058 0.0196  98  GLU B N   
3590 C CA  . GLU B 128 ? 0.5002 0.4349 0.4419 -0.0130 -0.0083 0.0188  98  GLU B CA  
3591 C C   . GLU B 128 ? 0.5361 0.4616 0.4716 -0.0134 -0.0133 0.0179  98  GLU B C   
3592 O O   . GLU B 128 ? 0.5453 0.4632 0.4767 -0.0139 -0.0155 0.0178  98  GLU B O   
3593 C CB  . GLU B 128 ? 0.5184 0.4544 0.4646 -0.0164 -0.0065 0.0210  98  GLU B CB  
3594 C CG  . GLU B 128 ? 0.5525 0.4965 0.5043 -0.0159 -0.0020 0.0212  98  GLU B CG  
3595 C CD  . GLU B 128 ? 0.6286 0.5743 0.5782 -0.0124 -0.0008 0.0186  98  GLU B CD  
3596 O OE1 . GLU B 128 ? 0.6815 0.6215 0.6254 -0.0103 -0.0034 0.0174  98  GLU B OE1 
3597 O OE2 . GLU B 128 ? 0.6172 0.5698 0.5707 -0.0118 0.0026  0.0177  98  GLU B OE2 
3598 N N   . GLU B 129 ? 0.5480 0.4738 0.4824 -0.0130 -0.0151 0.0173  99  GLU B N   
3599 C CA  . GLU B 129 ? 0.5784 0.4965 0.5073 -0.0134 -0.0199 0.0158  99  GLU B CA  
3600 C C   . GLU B 129 ? 0.5981 0.5107 0.5279 -0.0192 -0.0221 0.0176  99  GLU B C   
3601 O O   . GLU B 129 ? 0.6090 0.5116 0.5329 -0.0201 -0.0261 0.0163  99  GLU B O   
3602 C CB  . GLU B 129 ? 0.6254 0.5367 0.5457 -0.0081 -0.0227 0.0125  99  GLU B CB  
3603 C CG  . GLU B 129 ? 0.6926 0.6111 0.6122 -0.0026 -0.0208 0.0108  99  GLU B CG  
3604 C CD  . GLU B 129 ? 0.7922 0.7060 0.7032 0.0031  -0.0245 0.0074  99  GLU B CD  
3605 O OE1 . GLU B 129 ? 0.8251 0.7391 0.7345 0.0041  -0.0268 0.0063  99  GLU B OE1 
3606 O OE2 . GLU B 129 ? 0.8094 0.7197 0.7148 0.0072  -0.0252 0.0056  99  GLU B OE2 
3607 N N   . PHE B 130 ? 0.5994 0.5184 0.5363 -0.0232 -0.0195 0.0206  100 PHE B N   
3608 C CA  . PHE B 130 ? 0.6155 0.5323 0.5546 -0.0292 -0.0209 0.0229  100 PHE B CA  
3609 C C   . PHE B 130 ? 0.5942 0.5136 0.5345 -0.0317 -0.0234 0.0225  100 PHE B C   
3610 O O   . PHE B 130 ? 0.6008 0.5152 0.5398 -0.0363 -0.0267 0.0226  100 PHE B O   
3611 C CB  . PHE B 130 ? 0.6378 0.5622 0.5839 -0.0315 -0.0170 0.0261  100 PHE B CB  
3612 C CG  . PHE B 130 ? 0.6812 0.6019 0.6279 -0.0362 -0.0178 0.0286  100 PHE B CG  
3613 C CD1 . PHE B 130 ? 0.7047 0.6256 0.6532 -0.0418 -0.0200 0.0302  100 PHE B CD1 
3614 C CD2 . PHE B 130 ? 0.7115 0.6295 0.6570 -0.0350 -0.0162 0.0294  100 PHE B CD2 
3615 C CE1 . PHE B 130 ? 0.7229 0.6408 0.6720 -0.0466 -0.0205 0.0329  100 PHE B CE1 
3616 C CE2 . PHE B 130 ? 0.7300 0.6450 0.6759 -0.0391 -0.0166 0.0322  100 PHE B CE2 
3617 C CZ  . PHE B 130 ? 0.7275 0.6422 0.6752 -0.0451 -0.0187 0.0341  100 PHE B CZ  
3618 N N   . GLY B 131 ? 0.5663 0.4935 0.5090 -0.0288 -0.0217 0.0221  101 GLY B N   
3619 C CA  . GLY B 131 ? 0.5519 0.4832 0.4956 -0.0299 -0.0237 0.0215  101 GLY B CA  
3620 C C   . GLY B 131 ? 0.5350 0.4776 0.4848 -0.0295 -0.0202 0.0238  101 GLY B C   
3621 O O   . GLY B 131 ? 0.5216 0.4684 0.4752 -0.0289 -0.0160 0.0260  101 GLY B O   
3622 N N   . VAL B 132 ? 0.5307 0.4780 0.4809 -0.0295 -0.0219 0.0231  102 VAL B N   
3623 C CA  . VAL B 132 ? 0.5224 0.4801 0.4772 -0.0286 -0.0189 0.0253  102 VAL B CA  
3624 C C   . VAL B 132 ? 0.5178 0.4799 0.4770 -0.0342 -0.0196 0.0274  102 VAL B C   
3625 O O   . VAL B 132 ? 0.5204 0.4825 0.4790 -0.0378 -0.0235 0.0261  102 VAL B O   
3626 C CB  . VAL B 132 ? 0.5286 0.4903 0.4813 -0.0251 -0.0206 0.0234  102 VAL B CB  
3627 C CG1 . VAL B 132 ? 0.5275 0.4995 0.4839 -0.0232 -0.0173 0.0259  102 VAL B CG1 
3628 C CG2 . VAL B 132 ? 0.5360 0.4936 0.4838 -0.0197 -0.0207 0.0211  102 VAL B CG2 
3629 N N   . VAL B 133 ? 0.5065 0.4730 0.4700 -0.0351 -0.0160 0.0305  103 VAL B N   
3630 C CA  . VAL B 133 ? 0.5011 0.4739 0.4690 -0.0398 -0.0162 0.0329  103 VAL B CA  
3631 C C   . VAL B 133 ? 0.5047 0.4873 0.4741 -0.0387 -0.0167 0.0330  103 VAL B C   
3632 O O   . VAL B 133 ? 0.5092 0.4955 0.4783 -0.0335 -0.0139 0.0334  103 VAL B O   
3633 C CB  . VAL B 133 ? 0.5055 0.4816 0.4771 -0.0393 -0.0119 0.0359  103 VAL B CB  
3634 C CG1 . VAL B 133 ? 0.5016 0.4862 0.4776 -0.0432 -0.0120 0.0385  103 VAL B CG1 
3635 C CG2 . VAL B 133 ? 0.5164 0.4842 0.4864 -0.0396 -0.0113 0.0356  103 VAL B CG2 
3636 N N   . SER B 134 ? 0.5020 0.4885 0.4726 -0.0433 -0.0202 0.0324  104 SER B N   
3637 C CA  . SER B 134 ? 0.5009 0.4981 0.4728 -0.0420 -0.0210 0.0321  104 SER B CA  
3638 C C   . SER B 134 ? 0.4951 0.5025 0.4702 -0.0385 -0.0168 0.0352  104 SER B C   
3639 O O   . SER B 134 ? 0.5020 0.5091 0.4793 -0.0390 -0.0139 0.0377  104 SER B O   
3640 C CB  . SER B 134 ? 0.5150 0.5160 0.4885 -0.0486 -0.0254 0.0309  104 SER B CB  
3641 O OG  . SER B 134 ? 0.5337 0.5417 0.5119 -0.0535 -0.0246 0.0339  104 SER B OG  
3642 N N   . ASN B 135 ? 0.4822 0.4978 0.4568 -0.0344 -0.0163 0.0349  105 ASN B N   
3643 C CA  . ASN B 135 ? 0.4728 0.4973 0.4489 -0.0300 -0.0125 0.0377  105 ASN B CA  
3644 C C   . ASN B 135 ? 0.4667 0.4996 0.4472 -0.0342 -0.0124 0.0401  105 ASN B C   
3645 O O   . ASN B 135 ? 0.4639 0.4976 0.4459 -0.0325 -0.0090 0.0427  105 ASN B O   
3646 C CB  . ASN B 135 ? 0.4711 0.5037 0.4452 -0.0252 -0.0130 0.0367  105 ASN B CB  
3647 C CG  . ASN B 135 ? 0.5009 0.5268 0.4706 -0.0204 -0.0128 0.0348  105 ASN B CG  
3648 O OD1 . ASN B 135 ? 0.5091 0.5245 0.4772 -0.0204 -0.0120 0.0342  105 ASN B OD1 
3649 N ND2 . ASN B 135 ? 0.5088 0.5416 0.4764 -0.0158 -0.0134 0.0339  105 ASN B ND2 
3650 N N   . THR B 136 ? 0.4573 0.4962 0.4400 -0.0399 -0.0163 0.0391  106 THR B N   
3651 C CA  . THR B 136 ? 0.4576 0.5060 0.4447 -0.0444 -0.0164 0.0415  106 THR B CA  
3652 C C   . THR B 136 ? 0.4459 0.4870 0.4346 -0.0481 -0.0152 0.0435  106 THR B C   
3653 O O   . THR B 136 ? 0.4406 0.4876 0.4317 -0.0473 -0.0126 0.0464  106 THR B O   
3654 C CB  . THR B 136 ? 0.4844 0.5415 0.4738 -0.0505 -0.0208 0.0399  106 THR B CB  
3655 O OG1 . THR B 136 ? 0.5073 0.5713 0.4948 -0.0460 -0.0219 0.0376  106 THR B OG1 
3656 C CG2 . THR B 136 ? 0.4867 0.5573 0.4810 -0.0544 -0.0205 0.0427  106 THR B CG2 
3657 N N   . ARG B 137 ? 0.4352 0.4633 0.4217 -0.0512 -0.0169 0.0419  107 ARG B N   
3658 C CA  . ARG B 137 ? 0.4348 0.4558 0.4222 -0.0541 -0.0158 0.0436  107 ARG B CA  
3659 C C   . ARG B 137 ? 0.4348 0.4538 0.4221 -0.0486 -0.0113 0.0452  107 ARG B C   
3660 O O   . ARG B 137 ? 0.4363 0.4582 0.4261 -0.0497 -0.0095 0.0477  107 ARG B O   
3661 C CB  . ARG B 137 ? 0.4531 0.4603 0.4370 -0.0574 -0.0186 0.0413  107 ARG B CB  
3662 C CG  . ARG B 137 ? 0.4841 0.4870 0.4693 -0.0638 -0.0195 0.0433  107 ARG B CG  
3663 C CD  . ARG B 137 ? 0.5164 0.5044 0.4968 -0.0663 -0.0225 0.0409  107 ARG B CD  
3664 N NE  . ARG B 137 ? 0.5524 0.5318 0.5313 -0.0657 -0.0206 0.0423  107 ARG B NE  
3665 C CZ  . ARG B 137 ? 0.5746 0.5428 0.5488 -0.0619 -0.0204 0.0403  107 ARG B CZ  
3666 N NH1 . ARG B 137 ? 0.5410 0.5051 0.5116 -0.0584 -0.0219 0.0369  107 ARG B NH1 
3667 N NH2 . ARG B 137 ? 0.5855 0.5475 0.5585 -0.0612 -0.0187 0.0416  107 ARG B NH2 
3668 N N   . LEU B 138 ? 0.4295 0.4440 0.4138 -0.0427 -0.0094 0.0437  108 LEU B N   
3669 C CA  . LEU B 138 ? 0.4214 0.4332 0.4055 -0.0380 -0.0052 0.0448  108 LEU B CA  
3670 C C   . LEU B 138 ? 0.4059 0.4280 0.3922 -0.0351 -0.0025 0.0474  108 LEU B C   
3671 O O   . LEU B 138 ? 0.4132 0.4352 0.4010 -0.0342 0.0000  0.0489  108 LEU B O   
3672 C CB  . LEU B 138 ? 0.4282 0.4335 0.4087 -0.0330 -0.0037 0.0429  108 LEU B CB  
3673 C CG  . LEU B 138 ? 0.4454 0.4468 0.4256 -0.0291 0.0006  0.0436  108 LEU B CG  
3674 C CD1 . LEU B 138 ? 0.4458 0.4401 0.4265 -0.0314 0.0008  0.0430  108 LEU B CD1 
3675 C CD2 . LEU B 138 ? 0.4536 0.4518 0.4307 -0.0243 0.0025  0.0426  108 LEU B CD2 
3676 N N   . ILE B 139 ? 0.3881 0.4193 0.3744 -0.0333 -0.0032 0.0476  109 ILE B N   
3677 C CA  . ILE B 139 ? 0.3887 0.4301 0.3761 -0.0297 -0.0009 0.0500  109 ILE B CA  
3678 C C   . ILE B 139 ? 0.3899 0.4400 0.3813 -0.0340 -0.0018 0.0521  109 ILE B C   
3679 O O   . ILE B 139 ? 0.3944 0.4483 0.3867 -0.0312 0.0007  0.0541  109 ILE B O   
3680 C CB  . ILE B 139 ? 0.3901 0.4395 0.3755 -0.0254 -0.0012 0.0496  109 ILE B CB  
3681 C CG1 . ILE B 139 ? 0.4078 0.4489 0.3889 -0.0200 0.0008  0.0484  109 ILE B CG1 
3682 C CG2 . ILE B 139 ? 0.3890 0.4503 0.3751 -0.0216 0.0006  0.0520  109 ILE B CG2 
3683 C CD1 . ILE B 139 ? 0.4321 0.4652 0.4116 -0.0160 0.0052  0.0495  109 ILE B CD1 
3684 N N   . ALA B 140 ? 0.3860 0.4388 0.3796 -0.0408 -0.0054 0.0517  110 ALA B N   
3685 C CA  . ALA B 140 ? 0.3839 0.4452 0.3815 -0.0456 -0.0061 0.0542  110 ALA B CA  
3686 C C   . ALA B 140 ? 0.3888 0.4425 0.3870 -0.0465 -0.0043 0.0555  110 ALA B C   
3687 O O   . ALA B 140 ? 0.3882 0.4496 0.3889 -0.0462 -0.0029 0.0581  110 ALA B O   
3688 C CB  . ALA B 140 ? 0.3795 0.4439 0.3790 -0.0534 -0.0102 0.0536  110 ALA B CB  
3689 N N   . ALA B 141 ? 0.3926 0.4325 0.3884 -0.0469 -0.0044 0.0537  111 ALA B N   
3690 C CA  . ALA B 141 ? 0.3973 0.4307 0.3935 -0.0472 -0.0027 0.0545  111 ALA B CA  
3691 C C   . ALA B 141 ? 0.3884 0.4237 0.3846 -0.0410 0.0011  0.0552  111 ALA B C   
3692 O O   . ALA B 141 ? 0.3840 0.4225 0.3821 -0.0410 0.0024  0.0570  111 ALA B O   
3693 C CB  . ALA B 141 ? 0.4063 0.4256 0.3994 -0.0480 -0.0037 0.0521  111 ALA B CB  
3694 N N   . ALA B 142 ? 0.3776 0.4107 0.3714 -0.0356 0.0028  0.0538  112 ALA B N   
3695 C CA  . ALA B 142 ? 0.3690 0.4023 0.3622 -0.0299 0.0064  0.0543  112 ALA B CA  
3696 C C   . ALA B 142 ? 0.3631 0.4090 0.3579 -0.0279 0.0071  0.0568  112 ALA B C   
3697 O O   . ALA B 142 ? 0.3559 0.4035 0.3515 -0.0255 0.0091  0.0577  112 ALA B O   
3698 C CB  . ALA B 142 ? 0.3661 0.3936 0.3558 -0.0253 0.0082  0.0527  112 ALA B CB  
3699 N N   . THR B 143 ? 0.3603 0.4160 0.3555 -0.0286 0.0054  0.0576  113 THR B N   
3700 C CA  . THR B 143 ? 0.3703 0.4402 0.3671 -0.0265 0.0057  0.0600  113 THR B CA  
3701 C C   . THR B 143 ? 0.3885 0.4642 0.3891 -0.0309 0.0050  0.0622  113 THR B C   
3702 O O   . THR B 143 ? 0.3899 0.4717 0.3911 -0.0275 0.0067  0.0638  113 THR B O   
3703 C CB  . THR B 143 ? 0.3804 0.4608 0.3774 -0.0276 0.0034  0.0600  113 THR B CB  
3704 O OG1 . THR B 143 ? 0.3959 0.4714 0.3890 -0.0229 0.0042  0.0583  113 THR B OG1 
3705 C CG2 . THR B 143 ? 0.3744 0.4714 0.3730 -0.0255 0.0035  0.0624  113 THR B CG2 
3706 N N   . SER B 144 ? 0.3949 0.4675 0.3975 -0.0380 0.0026  0.0621  114 SER B N   
3707 C CA  . SER B 144 ? 0.4102 0.4874 0.4160 -0.0428 0.0020  0.0646  114 SER B CA  
3708 C C   . SER B 144 ? 0.4224 0.4928 0.4279 -0.0406 0.0041  0.0648  114 SER B C   
3709 O O   . SER B 144 ? 0.4248 0.5035 0.4325 -0.0400 0.0050  0.0673  114 SER B O   
3710 C CB  . SER B 144 ? 0.4335 0.5071 0.4404 -0.0510 -0.0012 0.0645  114 SER B CB  
3711 O OG  . SER B 144 ? 0.4854 0.5651 0.4954 -0.0559 -0.0015 0.0677  114 SER B OG  
3712 N N   . VAL B 145 ? 0.4310 0.4878 0.4341 -0.0392 0.0049  0.0622  115 VAL B N   
3713 C CA  . VAL B 145 ? 0.4447 0.4954 0.4476 -0.0369 0.0068  0.0617  115 VAL B CA  
3714 C C   . VAL B 145 ? 0.4596 0.5155 0.4623 -0.0305 0.0095  0.0619  115 VAL B C   
3715 O O   . VAL B 145 ? 0.4616 0.5220 0.4658 -0.0294 0.0104  0.0633  115 VAL B O   
3716 C CB  . VAL B 145 ? 0.4497 0.4859 0.4499 -0.0368 0.0070  0.0585  115 VAL B CB  
3717 C CG1 . VAL B 145 ? 0.4564 0.4877 0.4562 -0.0329 0.0095  0.0570  115 VAL B CG1 
3718 C CG2 . VAL B 145 ? 0.4514 0.4817 0.4512 -0.0426 0.0044  0.0586  115 VAL B CG2 
3719 N N   . LEU B 146 ? 0.4684 0.5236 0.4687 -0.0259 0.0107  0.0607  116 LEU B N   
3720 C CA  . LEU B 146 ? 0.4878 0.5460 0.4869 -0.0194 0.0131  0.0607  116 LEU B CA  
3721 C C   . LEU B 146 ? 0.5022 0.5754 0.5029 -0.0179 0.0128  0.0637  116 LEU B C   
3722 O O   . LEU B 146 ? 0.5021 0.5785 0.5028 -0.0138 0.0143  0.0641  116 LEU B O   
3723 C CB  . LEU B 146 ? 0.4941 0.5470 0.4894 -0.0148 0.0146  0.0592  116 LEU B CB  
3724 C CG  . LEU B 146 ? 0.5270 0.5660 0.5205 -0.0156 0.0155  0.0564  116 LEU B CG  
3725 C CD1 . LEU B 146 ? 0.5388 0.5736 0.5286 -0.0113 0.0172  0.0557  116 LEU B CD1 
3726 C CD2 . LEU B 146 ? 0.5380 0.5698 0.5320 -0.0149 0.0171  0.0545  116 LEU B CD2 
3727 N N   . LYS B 147 ? 0.5026 0.5859 0.5051 -0.0214 0.0108  0.0657  117 LYS B N   
3728 C CA  . LYS B 147 ? 0.5094 0.6092 0.5140 -0.0208 0.0103  0.0688  117 LYS B CA  
3729 C C   . LYS B 147 ? 0.5125 0.6174 0.5206 -0.0243 0.0100  0.0711  117 LYS B C   
3730 O O   . LYS B 147 ? 0.5154 0.6293 0.5239 -0.0202 0.0111  0.0726  117 LYS B O   
3731 C CB  . LYS B 147 ? 0.5443 0.6538 0.5502 -0.0244 0.0081  0.0698  117 LYS B CB  
3732 C CG  . LYS B 147 ? 0.6219 0.7507 0.6307 -0.0251 0.0073  0.0730  117 LYS B CG  
3733 C CD  . LYS B 147 ? 0.7104 0.8490 0.7192 -0.0261 0.0055  0.0728  117 LYS B CD  
3734 C CE  . LYS B 147 ? 0.7746 0.9339 0.7873 -0.0291 0.0042  0.0759  117 LYS B CE  
3735 N NZ  . LYS B 147 ? 0.8062 0.9757 0.8194 -0.0307 0.0022  0.0751  117 LYS B NZ  
3736 N N   . THR B 148 ? 0.5101 0.6094 0.5201 -0.0313 0.0085  0.0715  118 THR B N   
3737 C CA  . THR B 148 ? 0.5119 0.6157 0.5247 -0.0350 0.0083  0.0743  118 THR B CA  
3738 C C   . THR B 148 ? 0.5061 0.6014 0.5179 -0.0320 0.0100  0.0731  118 THR B C   
3739 O O   . THR B 148 ? 0.5108 0.6129 0.5244 -0.0320 0.0105  0.0756  118 THR B O   
3740 C CB  . THR B 148 ? 0.5352 0.6365 0.5498 -0.0440 0.0060  0.0756  118 THR B CB  
3741 O OG1 . THR B 148 ? 0.5613 0.6459 0.5733 -0.0454 0.0055  0.0726  118 THR B OG1 
3742 C CG2 . THR B 148 ? 0.5369 0.6478 0.5529 -0.0477 0.0041  0.0763  118 THR B CG2 
3743 N N   . ARG B 149 ? 0.4929 0.5747 0.5022 -0.0296 0.0108  0.0694  119 ARG B N   
3744 C CA  . ARG B 149 ? 0.4813 0.5557 0.4898 -0.0272 0.0122  0.0677  119 ARG B CA  
3745 C C   . ARG B 149 ? 0.4579 0.5300 0.4646 -0.0200 0.0143  0.0649  119 ARG B C   
3746 O O   . ARG B 149 ? 0.4609 0.5317 0.4677 -0.0172 0.0154  0.0638  119 ARG B O   
3747 C CB  . ARG B 149 ? 0.5097 0.5705 0.5169 -0.0309 0.0114  0.0656  119 ARG B CB  
3748 C CG  . ARG B 149 ? 0.5707 0.6321 0.5791 -0.0378 0.0094  0.0685  119 ARG B CG  
3749 C CD  . ARG B 149 ? 0.6314 0.6791 0.6374 -0.0412 0.0082  0.0664  119 ARG B CD  
3750 N NE  . ARG B 149 ? 0.6896 0.7299 0.6942 -0.0391 0.0092  0.0648  119 ARG B NE  
3751 C CZ  . ARG B 149 ? 0.7422 0.7712 0.7442 -0.0409 0.0083  0.0630  119 ARG B CZ  
3752 N NH1 . ARG B 149 ? 0.7538 0.7766 0.7540 -0.0449 0.0062  0.0625  119 ARG B NH1 
3753 N NH2 . ARG B 149 ? 0.7450 0.7692 0.7456 -0.0383 0.0094  0.0615  119 ARG B NH2 
3754 N N   . PHE B 150 ? 0.4361 0.5071 0.4406 -0.0168 0.0149  0.0636  120 PHE B N   
3755 C CA  . PHE B 150 ? 0.4264 0.4924 0.4283 -0.0104 0.0170  0.0609  120 PHE B CA  
3756 C C   . PHE B 150 ? 0.4271 0.5012 0.4269 -0.0047 0.0177  0.0620  120 PHE B C   
3757 O O   . PHE B 150 ? 0.4308 0.4979 0.4271 -0.0002 0.0193  0.0598  120 PHE B O   
3758 C CB  . PHE B 150 ? 0.4204 0.4725 0.4201 -0.0110 0.0178  0.0576  120 PHE B CB  
3759 C CG  . PHE B 150 ? 0.4184 0.4622 0.4192 -0.0151 0.0172  0.0559  120 PHE B CG  
3760 C CD1 . PHE B 150 ? 0.4216 0.4612 0.4228 -0.0134 0.0184  0.0534  120 PHE B CD1 
3761 C CD2 . PHE B 150 ? 0.4194 0.4600 0.4205 -0.0203 0.0154  0.0564  120 PHE B CD2 
3762 C CE1 . PHE B 150 ? 0.4256 0.4588 0.4272 -0.0165 0.0179  0.0518  120 PHE B CE1 
3763 C CE2 . PHE B 150 ? 0.4302 0.4634 0.4314 -0.0232 0.0149  0.0549  120 PHE B CE2 
3764 C CZ  . PHE B 150 ? 0.4256 0.4556 0.4270 -0.0211 0.0162  0.0527  120 PHE B CZ  
3765 N N   . SER B 151 ? 0.4224 0.5113 0.4240 -0.0047 0.0167  0.0654  121 SER B N   
3766 C CA  . SER B 151 ? 0.4333 0.5311 0.4323 0.0017  0.0173  0.0664  121 SER B CA  
3767 C C   . SER B 151 ? 0.4548 0.5523 0.4513 0.0090  0.0188  0.0650  121 SER B C   
3768 O O   . SER B 151 ? 0.4623 0.5619 0.4548 0.0156  0.0197  0.0648  121 SER B O   
3769 C CB  . SER B 151 ? 0.4384 0.5536 0.4399 -0.0004 0.0157  0.0703  121 SER B CB  
3770 O OG  . SER B 151 ? 0.4753 0.5978 0.4809 -0.0043 0.0150  0.0726  121 SER B OG  
3771 N N   . TYR B 152 ? 0.4592 0.5529 0.4574 0.0084  0.0192  0.0636  122 TYR B N   
3772 C CA  . TYR B 152 ? 0.4727 0.5641 0.4684 0.0151  0.0205  0.0613  122 TYR B CA  
3773 C C   . TYR B 152 ? 0.5098 0.5862 0.5010 0.0184  0.0222  0.0576  122 TYR B C   
3774 O O   . TYR B 152 ? 0.5218 0.5958 0.5092 0.0250  0.0232  0.0558  122 TYR B O   
3775 C CB  . TYR B 152 ? 0.4596 0.5494 0.4582 0.0132  0.0205  0.0601  122 TYR B CB  
3776 C CG  . TYR B 152 ? 0.4593 0.5367 0.4594 0.0076  0.0205  0.0577  122 TYR B CG  
3777 C CD1 . TYR B 152 ? 0.4723 0.5365 0.4704 0.0090  0.0219  0.0533  122 TYR B CD1 
3778 C CD2 . TYR B 152 ? 0.4691 0.5483 0.4724 0.0012  0.0193  0.0599  122 TYR B CD2 
3779 C CE1 . TYR B 152 ? 0.4828 0.5374 0.4822 0.0044  0.0220  0.0511  122 TYR B CE1 
3780 C CE2 . TYR B 152 ? 0.4824 0.5506 0.4863 -0.0029 0.0193  0.0576  122 TYR B CE2 
3781 C CZ  . TYR B 152 ? 0.4933 0.5502 0.4954 -0.0011 0.0206  0.0532  122 TYR B CZ  
3782 O OH  . TYR B 152 ? 0.5110 0.5586 0.5136 -0.0047 0.0206  0.0508  122 TYR B OH  
3783 N N   . ALA B 153 ? 0.5193 0.5850 0.5106 0.0138  0.0224  0.0564  123 ALA B N   
3784 C CA  . ALA B 153 ? 0.5316 0.5831 0.5189 0.0157  0.0243  0.0534  123 ALA B CA  
3785 C C   . ALA B 153 ? 0.5398 0.5908 0.5236 0.0174  0.0246  0.0551  123 ALA B C   
3786 O O   . ALA B 153 ? 0.5472 0.5893 0.5262 0.0216  0.0265  0.0538  123 ALA B O   
3787 C CB  . ALA B 153 ? 0.5311 0.5719 0.5207 0.0102  0.0246  0.0508  123 ALA B CB  
3788 N N   . PHE B 154 ? 0.5413 0.6018 0.5274 0.0140  0.0229  0.0580  124 PHE B N   
3789 C CA  . PHE B 154 ? 0.5551 0.6170 0.5383 0.0156  0.0229  0.0593  124 PHE B CA  
3790 C C   . PHE B 154 ? 0.5730 0.6516 0.5561 0.0184  0.0217  0.0624  124 PHE B C   
3791 O O   . PHE B 154 ? 0.5735 0.6629 0.5610 0.0134  0.0196  0.0645  124 PHE B O   
3792 C CB  . PHE B 154 ? 0.5464 0.6039 0.5319 0.0089  0.0219  0.0592  124 PHE B CB  
3793 C CG  . PHE B 154 ? 0.5479 0.5904 0.5333 0.0064  0.0231  0.0563  124 PHE B CG  
3794 C CD1 . PHE B 154 ? 0.5548 0.5859 0.5358 0.0102  0.0257  0.0545  124 PHE B CD1 
3795 C CD2 . PHE B 154 ? 0.5502 0.5903 0.5396 0.0003  0.0219  0.0553  124 PHE B CD2 
3796 C CE1 . PHE B 154 ? 0.5614 0.5803 0.5429 0.0073  0.0270  0.0518  124 PHE B CE1 
3797 C CE2 . PHE B 154 ? 0.5562 0.5842 0.5454 -0.0016 0.0231  0.0525  124 PHE B CE2 
3798 C CZ  . PHE B 154 ? 0.5532 0.5714 0.5388 0.0016  0.0256  0.0507  124 PHE B CZ  
3799 N N   . PRO B 155 ? 0.5855 0.6665 0.5633 0.0265  0.0228  0.0628  125 PRO B N   
3800 C CA  . PRO B 155 ? 0.5848 0.6837 0.5622 0.0298  0.0216  0.0657  125 PRO B CA  
3801 C C   . PRO B 155 ? 0.5842 0.6892 0.5617 0.0277  0.0205  0.0670  125 PRO B C   
3802 O O   . PRO B 155 ? 0.5803 0.7020 0.5609 0.0259  0.0187  0.0693  125 PRO B O   
3803 C CB  . PRO B 155 ? 0.5936 0.6909 0.5640 0.0401  0.0233  0.0651  125 PRO B CB  
3804 C CG  . PRO B 155 ? 0.6075 0.6842 0.5734 0.0415  0.0256  0.0624  125 PRO B CG  
3805 C CD  . PRO B 155 ? 0.5890 0.6564 0.5604 0.0329  0.0253  0.0607  125 PRO B CD  
3806 N N   . LYS B 156 ? 0.5790 0.6711 0.5535 0.0277  0.0216  0.0656  126 LYS B N   
3807 C CA  . LYS B 156 ? 0.5775 0.6747 0.5516 0.0265  0.0206  0.0664  126 LYS B CA  
3808 C C   . LYS B 156 ? 0.5679 0.6619 0.5473 0.0171  0.0188  0.0657  126 LYS B C   
3809 O O   . LYS B 156 ? 0.5744 0.6578 0.5563 0.0126  0.0190  0.0642  126 LYS B O   
3810 C CB  . LYS B 156 ? 0.6159 0.7024 0.5826 0.0332  0.0230  0.0658  126 LYS B CB  
3811 C CG  . LYS B 156 ? 0.6854 0.7732 0.6452 0.0433  0.0248  0.0665  126 LYS B CG  
3812 C CD  . LYS B 156 ? 0.7743 0.8461 0.7264 0.0489  0.0277  0.0658  126 LYS B CD  
3813 C CE  . LYS B 156 ? 0.8507 0.9189 0.7947 0.0590  0.0298  0.0661  126 LYS B CE  
3814 N NZ  . LYS B 156 ? 0.9058 0.9548 0.8423 0.0631  0.0331  0.0656  126 LYS B NZ  
3815 N N   . GLU B 157 ? 0.5484 0.6518 0.5293 0.0145  0.0168  0.0664  127 GLU B N   
3816 C CA  . GLU B 157 ? 0.5364 0.6368 0.5213 0.0062  0.0147  0.0655  127 GLU B CA  
3817 C C   . GLU B 157 ? 0.5120 0.5956 0.4938 0.0068  0.0161  0.0634  127 GLU B C   
3818 O O   . GLU B 157 ? 0.5138 0.5920 0.4901 0.0134  0.0184  0.0633  127 GLU B O   
3819 C CB  . GLU B 157 ? 0.5752 0.6910 0.5618 0.0043  0.0122  0.0665  127 GLU B CB  
3820 C CG  . GLU B 157 ? 0.6781 0.7919 0.6684 -0.0039 0.0095  0.0652  127 GLU B CG  
3821 C CD  . GLU B 157 ? 0.7978 0.9283 0.7906 -0.0068 0.0067  0.0658  127 GLU B CD  
3822 O OE1 . GLU B 157 ? 0.8156 0.9451 0.8073 -0.0076 0.0053  0.0642  127 GLU B OE1 
3823 O OE2 . GLU B 157 ? 0.8351 0.9806 0.8310 -0.0082 0.0058  0.0678  127 GLU B OE2 
3824 N N   . PHE B 158 ? 0.4812 0.5565 0.4659 0.0000  0.0149  0.0620  128 PHE B N   
3825 C CA  . PHE B 158 ? 0.4623 0.5236 0.4447 -0.0004 0.0159  0.0601  128 PHE B CA  
3826 C C   . PHE B 158 ? 0.4632 0.5269 0.4417 0.0039  0.0161  0.0602  128 PHE B C   
3827 O O   . PHE B 158 ? 0.4662 0.5402 0.4462 0.0019  0.0135  0.0604  128 PHE B O   
3828 C CB  . PHE B 158 ? 0.4394 0.4964 0.4256 -0.0081 0.0135  0.0587  128 PHE B CB  
3829 C CG  . PHE B 158 ? 0.4298 0.4738 0.4140 -0.0087 0.0142  0.0567  128 PHE B CG  
3830 C CD1 . PHE B 158 ? 0.4333 0.4659 0.4165 -0.0078 0.0167  0.0555  128 PHE B CD1 
3831 C CD2 . PHE B 158 ? 0.4266 0.4706 0.4100 -0.0104 0.0123  0.0557  128 PHE B CD2 
3832 C CE1 . PHE B 158 ? 0.4391 0.4613 0.4207 -0.0085 0.0174  0.0537  128 PHE B CE1 
3833 C CE2 . PHE B 158 ? 0.4332 0.4663 0.4146 -0.0105 0.0129  0.0540  128 PHE B CE2 
3834 C CZ  . PHE B 158 ? 0.4357 0.4584 0.4163 -0.0096 0.0156  0.0531  128 PHE B CZ  
3835 N N   . PRO B 159 ? 0.4580 0.5131 0.4311 0.0102  0.0193  0.0603  129 PRO B N   
3836 C CA  . PRO B 159 ? 0.4616 0.5197 0.4301 0.0156  0.0200  0.0610  129 PRO B CA  
3837 C C   . PRO B 159 ? 0.4670 0.5182 0.4343 0.0143  0.0197  0.0597  129 PRO B C   
3838 O O   . PRO B 159 ? 0.4772 0.5315 0.4405 0.0191  0.0202  0.0603  129 PRO B O   
3839 C CB  . PRO B 159 ? 0.4757 0.5262 0.4382 0.0233  0.0239  0.0620  129 PRO B CB  
3840 C CG  . PRO B 159 ? 0.4818 0.5192 0.4458 0.0201  0.0255  0.0607  129 PRO B CG  
3841 C CD  . PRO B 159 ? 0.4541 0.4970 0.4249 0.0128  0.0226  0.0598  129 PRO B CD  
3842 N N   . TYR B 160 ? 0.4584 0.5004 0.4284 0.0087  0.0192  0.0581  130 TYR B N   
3843 C CA  . TYR B 160 ? 0.4591 0.4941 0.4275 0.0080  0.0192  0.0569  130 TYR B CA  
3844 C C   . TYR B 160 ? 0.4624 0.5044 0.4333 0.0037  0.0150  0.0555  130 TYR B C   
3845 O O   . TYR B 160 ? 0.4643 0.5132 0.4395 -0.0015 0.0119  0.0550  130 TYR B O   
3846 C CB  . TYR B 160 ? 0.4556 0.4772 0.4247 0.0052  0.0210  0.0556  130 TYR B CB  
3847 C CG  . TYR B 160 ? 0.4516 0.4653 0.4178 0.0091  0.0251  0.0565  130 TYR B CG  
3848 C CD1 . TYR B 160 ? 0.4605 0.4689 0.4210 0.0151  0.0284  0.0579  130 TYR B CD1 
3849 C CD2 . TYR B 160 ? 0.4519 0.4636 0.4206 0.0073  0.0256  0.0560  130 TYR B CD2 
3850 C CE1 . TYR B 160 ? 0.4703 0.4700 0.4275 0.0184  0.0321  0.0586  130 TYR B CE1 
3851 C CE2 . TYR B 160 ? 0.4642 0.4683 0.4301 0.0108  0.0291  0.0563  130 TYR B CE2 
3852 C CZ  . TYR B 160 ? 0.4817 0.4793 0.4418 0.0161  0.0323  0.0576  130 TYR B CZ  
3853 O OH  . TYR B 160 ? 0.5015 0.4900 0.4581 0.0193  0.0357  0.0578  130 TYR B OH  
3854 N N   . ARG B 161 ? 0.4653 0.5053 0.4333 0.0060  0.0150  0.0548  131 ARG B N   
3855 C CA  . ARG B 161 ? 0.4713 0.5166 0.4407 0.0029  0.0111  0.0529  131 ARG B CA  
3856 C C   . ARG B 161 ? 0.4729 0.5074 0.4415 0.0009  0.0108  0.0511  131 ARG B C   
3857 O O   . ARG B 161 ? 0.4801 0.5046 0.4470 0.0024  0.0141  0.0515  131 ARG B O   
3858 C CB  . ARG B 161 ? 0.4982 0.5536 0.4644 0.0086  0.0108  0.0535  131 ARG B CB  
3859 C CG  . ARG B 161 ? 0.5772 0.6459 0.5448 0.0098  0.0101  0.0549  131 ARG B CG  
3860 C CD  . ARG B 161 ? 0.6643 0.7439 0.6280 0.0168  0.0103  0.0555  131 ARG B CD  
3861 N NE  . ARG B 161 ? 0.7459 0.8183 0.7030 0.0254  0.0149  0.0576  131 ARG B NE  
3862 C CZ  . ARG B 161 ? 0.7957 0.8662 0.7498 0.0303  0.0181  0.0599  131 ARG B CZ  
3863 N NH1 . ARG B 161 ? 0.7853 0.8614 0.7428 0.0278  0.0173  0.0604  131 ARG B NH1 
3864 N NH2 . ARG B 161 ? 0.8127 0.8751 0.7600 0.0377  0.0222  0.0618  131 ARG B NH2 
3865 N N   . MET B 162 ? 0.4625 0.4993 0.4323 -0.0027 0.0068  0.0488  132 MET B N   
3866 C CA  . MET B 162 ? 0.4579 0.4855 0.4265 -0.0041 0.0061  0.0467  132 MET B CA  
3867 C C   . MET B 162 ? 0.4632 0.4851 0.4273 0.0018  0.0096  0.0475  132 MET B C   
3868 O O   . MET B 162 ? 0.4736 0.4864 0.4373 0.0008  0.0110  0.0469  132 MET B O   
3869 C CB  . MET B 162 ? 0.4504 0.4812 0.4198 -0.0079 0.0010  0.0439  132 MET B CB  
3870 C CG  . MET B 162 ? 0.4521 0.4727 0.4210 -0.0110 -0.0005 0.0417  132 MET B CG  
3871 S SD  . MET B 162 ? 0.4491 0.4626 0.4213 -0.0164 0.0002  0.0422  132 MET B SD  
3872 C CE  . MET B 162 ? 0.4264 0.4295 0.3963 -0.0172 -0.0010 0.0396  132 MET B CE  
3873 N N   . ASN B 163 ? 0.4521 0.4795 0.4130 0.0080  0.0114  0.0491  133 ASN B N   
3874 C CA  . ASN B 163 ? 0.4639 0.4853 0.4201 0.0136  0.0152  0.0506  133 ASN B CA  
3875 C C   . ASN B 163 ? 0.4476 0.4587 0.4034 0.0136  0.0198  0.0523  133 ASN B C   
3876 O O   . ASN B 163 ? 0.4460 0.4496 0.4000 0.0143  0.0222  0.0525  133 ASN B O   
3877 C CB  . ASN B 163 ? 0.5012 0.5298 0.4530 0.0209  0.0166  0.0523  133 ASN B CB  
3878 C CG  . ASN B 163 ? 0.5905 0.6248 0.5418 0.0238  0.0181  0.0545  133 ASN B CG  
3879 O OD1 . ASN B 163 ? 0.6191 0.6619 0.5739 0.0206  0.0152  0.0537  133 ASN B OD1 
3880 N ND2 . ASN B 163 ? 0.6184 0.6481 0.5647 0.0301  0.0228  0.0575  133 ASN B ND2 
3881 N N   . HIS B 164 ? 0.4327 0.4439 0.3905 0.0121  0.0208  0.0532  134 HIS B N   
3882 C CA  . HIS B 164 ? 0.4316 0.4338 0.3895 0.0117  0.0247  0.0543  134 HIS B CA  
3883 C C   . HIS B 164 ? 0.4255 0.4215 0.3868 0.0061  0.0238  0.0521  134 HIS B C   
3884 O O   . HIS B 164 ? 0.4317 0.4196 0.3921 0.0060  0.0270  0.0523  134 HIS B O   
3885 C CB  . HIS B 164 ? 0.4443 0.4499 0.4034 0.0121  0.0252  0.0554  134 HIS B CB  
3886 C CG  . HIS B 164 ? 0.4704 0.4825 0.4255 0.0185  0.0262  0.0576  134 HIS B CG  
3887 N ND1 . HIS B 164 ? 0.4902 0.5140 0.4471 0.0185  0.0235  0.0577  134 HIS B ND1 
3888 C CD2 . HIS B 164 ? 0.4847 0.4936 0.4339 0.0251  0.0297  0.0598  134 HIS B CD2 
3889 C CE1 . HIS B 164 ? 0.4945 0.5225 0.4465 0.0256  0.0253  0.0596  134 HIS B CE1 
3890 N NE2 . HIS B 164 ? 0.4950 0.5137 0.4420 0.0300  0.0290  0.0610  134 HIS B NE2 
3891 N N   . ILE B 165 ? 0.4165 0.4163 0.3813 0.0013  0.0195  0.0501  135 ILE B N   
3892 C CA  . ILE B 165 ? 0.4145 0.4090 0.3817 -0.0035 0.0181  0.0478  135 ILE B CA  
3893 C C   . ILE B 165 ? 0.4217 0.4121 0.3864 -0.0022 0.0185  0.0468  135 ILE B C   
3894 O O   . ILE B 165 ? 0.4286 0.4130 0.3937 -0.0035 0.0201  0.0459  135 ILE B O   
3895 C CB  . ILE B 165 ? 0.4015 0.4007 0.3717 -0.0082 0.0133  0.0463  135 ILE B CB  
3896 C CG1 . ILE B 165 ? 0.4025 0.4066 0.3757 -0.0099 0.0132  0.0477  135 ILE B CG1 
3897 C CG2 . ILE B 165 ? 0.4022 0.3954 0.3731 -0.0119 0.0113  0.0439  135 ILE B CG2 
3898 C CD1 . ILE B 165 ? 0.4077 0.4075 0.3836 -0.0130 0.0140  0.0472  135 ILE B CD1 
3899 N N   . LEU B 166 ? 0.4180 0.4127 0.3802 0.0007  0.0168  0.0467  136 LEU B N   
3900 C CA  . LEU B 166 ? 0.4217 0.4139 0.3811 0.0027  0.0169  0.0458  136 LEU B CA  
3901 C C   . LEU B 166 ? 0.4323 0.4194 0.3892 0.0061  0.0223  0.0480  136 LEU B C   
3902 O O   . LEU B 166 ? 0.4406 0.4236 0.3969 0.0056  0.0234  0.0472  136 LEU B O   
3903 C CB  . LEU B 166 ? 0.4184 0.4171 0.3754 0.0056  0.0138  0.0450  136 LEU B CB  
3904 C CG  . LEU B 166 ? 0.4361 0.4386 0.3952 0.0014  0.0080  0.0421  136 LEU B CG  
3905 C CD1 . LEU B 166 ? 0.4388 0.4484 0.3956 0.0044  0.0050  0.0410  136 LEU B CD1 
3906 C CD2 . LEU B 166 ? 0.4367 0.4328 0.3963 -0.0023 0.0057  0.0395  136 LEU B CD2 
3907 N N   . GLU B 167 ? 0.4329 0.4201 0.3882 0.0092  0.0257  0.0508  137 GLU B N   
3908 C CA  . GLU B 167 ? 0.4403 0.4211 0.3929 0.0120  0.0312  0.0534  137 GLU B CA  
3909 C C   . GLU B 167 ? 0.4181 0.3922 0.3736 0.0075  0.0330  0.0523  137 GLU B C   
3910 O O   . GLU B 167 ? 0.4208 0.3904 0.3757 0.0069  0.0357  0.0524  137 GLU B O   
3911 C CB  . GLU B 167 ? 0.4972 0.4782 0.4467 0.0165  0.0340  0.0564  137 GLU B CB  
3912 C CG  . GLU B 167 ? 0.6221 0.6093 0.5672 0.0226  0.0336  0.0580  137 GLU B CG  
3913 C CD  . GLU B 167 ? 0.7485 0.7394 0.6911 0.0272  0.0346  0.0601  137 GLU B CD  
3914 O OE1 . GLU B 167 ? 0.7577 0.7567 0.6976 0.0318  0.0331  0.0607  137 GLU B OE1 
3915 O OE2 . GLU B 167 ? 0.7912 0.7775 0.7340 0.0266  0.0368  0.0611  137 GLU B OE2 
3916 N N   . CYS B 168 ? 0.3991 0.3737 0.3580 0.0043  0.0316  0.0512  138 CYS B N   
3917 C CA  . CYS B 168 ? 0.3915 0.3612 0.3536 0.0003  0.0330  0.0498  138 CYS B CA  
3918 C C   . CYS B 168 ? 0.3936 0.3626 0.3575 -0.0029 0.0314  0.0472  138 CYS B C   
3919 O O   . CYS B 168 ? 0.4009 0.3656 0.3659 -0.0049 0.0339  0.0464  138 CYS B O   
3920 C CB  . CYS B 168 ? 0.3790 0.3513 0.3441 -0.0017 0.0311  0.0491  138 CYS B CB  
3921 S SG  . CYS B 168 ? 0.4001 0.3669 0.3685 -0.0053 0.0333  0.0475  138 CYS B SG  
3922 N N   . GLU B 169 ? 0.3836 0.3566 0.3474 -0.0033 0.0271  0.0457  139 GLU B N   
3923 C CA  . GLU B 169 ? 0.3866 0.3589 0.3508 -0.0052 0.0250  0.0431  139 GLU B CA  
3924 C C   . GLU B 169 ? 0.4040 0.3743 0.3661 -0.0034 0.0281  0.0436  139 GLU B C   
3925 O O   . GLU B 169 ? 0.4066 0.3752 0.3700 -0.0055 0.0291  0.0420  139 GLU B O   
3926 C CB  . GLU B 169 ? 0.3895 0.3654 0.3527 -0.0052 0.0198  0.0415  139 GLU B CB  
3927 C CG  . GLU B 169 ? 0.4053 0.3794 0.3685 -0.0071 0.0170  0.0386  139 GLU B CG  
3928 C CD  . GLU B 169 ? 0.4461 0.4218 0.4072 -0.0068 0.0119  0.0368  139 GLU B CD  
3929 O OE1 . GLU B 169 ? 0.4524 0.4317 0.4117 -0.0042 0.0110  0.0376  139 GLU B OE1 
3930 O OE2 . GLU B 169 ? 0.4480 0.4212 0.4088 -0.0090 0.0087  0.0344  139 GLU B OE2 
3931 N N   . PHE B 170 ? 0.4136 0.3847 0.3724 0.0006  0.0301  0.0460  140 PHE B N   
3932 C CA  . PHE B 170 ? 0.4347 0.4043 0.3913 0.0025  0.0336  0.0474  140 PHE B CA  
3933 C C   . PHE B 170 ? 0.4444 0.4090 0.4028 -0.0002 0.0385  0.0482  140 PHE B C   
3934 O O   . PHE B 170 ? 0.4516 0.4158 0.4109 -0.0019 0.0400  0.0472  140 PHE B O   
3935 C CB  . PHE B 170 ? 0.4447 0.4162 0.3970 0.0078  0.0350  0.0503  140 PHE B CB  
3936 C CG  . PHE B 170 ? 0.4689 0.4452 0.4189 0.0107  0.0319  0.0490  140 PHE B CG  
3937 C CD1 . PHE B 170 ? 0.4862 0.4649 0.4373 0.0089  0.0265  0.0454  140 PHE B CD1 
3938 C CD2 . PHE B 170 ? 0.4852 0.4630 0.4313 0.0153  0.0345  0.0514  140 PHE B CD2 
3939 C CE1 . PHE B 170 ? 0.4962 0.4784 0.4445 0.0119  0.0234  0.0438  140 PHE B CE1 
3940 C CE2 . PHE B 170 ? 0.4985 0.4811 0.4422 0.0185  0.0314  0.0499  140 PHE B CE2 
3941 C CZ  . PHE B 170 ? 0.4968 0.4815 0.4415 0.0168  0.0257  0.0459  140 PHE B CZ  
3942 N N   . TYR B 171 ? 0.4414 0.4024 0.4003 -0.0006 0.0405  0.0496  141 TYR B N   
3943 C CA  . TYR B 171 ? 0.4487 0.4039 0.4091 -0.0034 0.0448  0.0499  141 TYR B CA  
3944 C C   . TYR B 171 ? 0.4451 0.4011 0.4100 -0.0081 0.0434  0.0463  141 TYR B C   
3945 O O   . TYR B 171 ? 0.4578 0.4118 0.4241 -0.0108 0.0463  0.0456  141 TYR B O   
3946 C CB  . TYR B 171 ? 0.4572 0.4086 0.4166 -0.0020 0.0464  0.0517  141 TYR B CB  
3947 C CG  . TYR B 171 ? 0.4834 0.4314 0.4375 0.0027  0.0498  0.0557  141 TYR B CG  
3948 C CD1 . TYR B 171 ? 0.5033 0.4445 0.4552 0.0024  0.0550  0.0579  141 TYR B CD1 
3949 C CD2 . TYR B 171 ? 0.4989 0.4509 0.4501 0.0075  0.0480  0.0573  141 TYR B CD2 
3950 C CE1 . TYR B 171 ? 0.5226 0.4598 0.4688 0.0072  0.0585  0.0619  141 TYR B CE1 
3951 C CE2 . TYR B 171 ? 0.5169 0.4661 0.4624 0.0127  0.0512  0.0610  141 TYR B CE2 
3952 C CZ  . TYR B 171 ? 0.5370 0.4782 0.4797 0.0128  0.0565  0.0635  141 TYR B CZ  
3953 O OH  . TYR B 171 ? 0.5644 0.5019 0.5009 0.0185  0.0600  0.0676  141 TYR B OH  
3954 N N   . LEU B 172 ? 0.4215 0.3807 0.3886 -0.0092 0.0392  0.0441  142 LEU B N   
3955 C CA  . LEU B 172 ? 0.4120 0.3722 0.3826 -0.0128 0.0376  0.0408  142 LEU B CA  
3956 C C   . LEU B 172 ? 0.4145 0.3773 0.3850 -0.0133 0.0370  0.0390  142 LEU B C   
3957 O O   . LEU B 172 ? 0.4055 0.3687 0.3783 -0.0160 0.0385  0.0369  142 LEU B O   
3958 C CB  . LEU B 172 ? 0.3993 0.3622 0.3712 -0.0132 0.0331  0.0397  142 LEU B CB  
3959 C CG  . LEU B 172 ? 0.3988 0.3630 0.3736 -0.0160 0.0311  0.0366  142 LEU B CG  
3960 C CD1 . LEU B 172 ? 0.3909 0.3531 0.3685 -0.0182 0.0341  0.0355  142 LEU B CD1 
3961 C CD2 . LEU B 172 ? 0.3983 0.3646 0.3735 -0.0165 0.0267  0.0363  142 LEU B CD2 
3962 N N   . LEU B 173 ? 0.4261 0.3913 0.3935 -0.0105 0.0349  0.0395  143 LEU B N   
3963 C CA  . LEU B 173 ? 0.4424 0.4106 0.4088 -0.0100 0.0339  0.0378  143 LEU B CA  
3964 C C   . LEU B 173 ? 0.4465 0.4149 0.4132 -0.0107 0.0387  0.0388  143 LEU B C   
3965 O O   . LEU B 173 ? 0.4516 0.4227 0.4199 -0.0126 0.0392  0.0365  143 LEU B O   
3966 C CB  . LEU B 173 ? 0.4538 0.4243 0.4165 -0.0063 0.0304  0.0380  143 LEU B CB  
3967 C CG  . LEU B 173 ? 0.4786 0.4524 0.4392 -0.0046 0.0286  0.0359  143 LEU B CG  
3968 C CD1 . LEU B 173 ? 0.4805 0.4546 0.4424 -0.0066 0.0260  0.0324  143 LEU B CD1 
3969 C CD2 . LEU B 173 ? 0.4967 0.4719 0.4533 -0.0008 0.0247  0.0357  143 LEU B CD2 
3970 N N   . GLU B 174 ? 0.4514 0.4172 0.4163 -0.0094 0.0425  0.0423  144 GLU B N   
3971 C CA  . GLU B 174 ? 0.4595 0.4246 0.4244 -0.0106 0.0476  0.0440  144 GLU B CA  
3972 C C   . GLU B 174 ? 0.4574 0.4194 0.4261 -0.0156 0.0507  0.0428  144 GLU B C   
3973 O O   . GLU B 174 ? 0.4568 0.4212 0.4273 -0.0184 0.0533  0.0419  144 GLU B O   
3974 C CB  . GLU B 174 ? 0.4931 0.4554 0.4541 -0.0073 0.0509  0.0485  144 GLU B CB  
3975 C CG  . GLU B 174 ? 0.5877 0.5441 0.5476 -0.0063 0.0519  0.0505  144 GLU B CG  
3976 C CD  . GLU B 174 ? 0.6969 0.6502 0.6520 -0.0021 0.0552  0.0551  144 GLU B CD  
3977 O OE1 . GLU B 174 ? 0.6839 0.6408 0.6360 0.0026  0.0527  0.0561  144 GLU B OE1 
3978 O OE2 . GLU B 174 ? 0.7420 0.6891 0.6961 -0.0035 0.0604  0.0576  144 GLU B OE2 
3979 N N   . LEU B 175 ? 0.4584 0.4161 0.4285 -0.0166 0.0503  0.0424  145 LEU B N   
3980 C CA  . LEU B 175 ? 0.4661 0.4204 0.4394 -0.0210 0.0530  0.0408  145 LEU B CA  
3981 C C   . LEU B 175 ? 0.4638 0.4234 0.4411 -0.0238 0.0505  0.0363  145 LEU B C   
3982 O O   . LEU B 175 ? 0.4810 0.4400 0.4615 -0.0277 0.0528  0.0342  145 LEU B O   
3983 C CB  . LEU B 175 ? 0.4837 0.4315 0.4562 -0.0203 0.0538  0.0423  145 LEU B CB  
3984 C CG  . LEU B 175 ? 0.5198 0.4618 0.4875 -0.0171 0.0572  0.0470  145 LEU B CG  
3985 C CD1 . LEU B 175 ? 0.5365 0.4724 0.5023 -0.0152 0.0578  0.0483  145 LEU B CD1 
3986 C CD2 . LEU B 175 ? 0.5220 0.4600 0.4890 -0.0196 0.0625  0.0487  145 LEU B CD2 
3987 N N   . MET B 176 ? 0.4390 0.4039 0.4158 -0.0218 0.0462  0.0345  146 MET B N   
3988 C CA  . MET B 176 ? 0.4168 0.3869 0.3960 -0.0235 0.0441  0.0305  146 MET B CA  
3989 C C   . MET B 176 ? 0.3931 0.3693 0.3715 -0.0230 0.0448  0.0298  146 MET B C   
3990 O O   . MET B 176 ? 0.3827 0.3642 0.3619 -0.0230 0.0427  0.0265  146 MET B O   
3991 C CB  . MET B 176 ? 0.4174 0.3886 0.3958 -0.0215 0.0389  0.0290  146 MET B CB  
3992 C CG  . MET B 176 ? 0.4432 0.4110 0.4231 -0.0222 0.0381  0.0294  146 MET B CG  
3993 S SD  . MET B 176 ? 0.4797 0.4493 0.4594 -0.0212 0.0326  0.0274  146 MET B SD  
3994 C CE  . MET B 176 ? 0.4376 0.4068 0.4128 -0.0180 0.0293  0.0293  146 MET B CE  
3995 N N   . ASP B 177 ? 0.3895 0.3652 0.3658 -0.0220 0.0477  0.0329  147 ASP B N   
3996 C CA  . ASP B 177 ? 0.3884 0.3706 0.3635 -0.0210 0.0487  0.0328  147 ASP B CA  
3997 C C   . ASP B 177 ? 0.3863 0.3727 0.3583 -0.0166 0.0435  0.0310  147 ASP B C   
3998 O O   . ASP B 177 ? 0.3860 0.3793 0.3575 -0.0157 0.0428  0.0289  147 ASP B O   
3999 C CB  . ASP B 177 ? 0.4032 0.3903 0.3824 -0.0257 0.0517  0.0304  147 ASP B CB  
4000 C CG  . ASP B 177 ? 0.4982 0.4929 0.4767 -0.0254 0.0540  0.0312  147 ASP B CG  
4001 O OD1 . ASP B 177 ? 0.5147 0.5088 0.4897 -0.0221 0.0548  0.0347  147 ASP B OD1 
4002 O OD2 . ASP B 177 ? 0.5392 0.5415 0.5206 -0.0280 0.0549  0.0282  147 ASP B OD2 
4003 N N   . CYS B 178 ? 0.3809 0.3632 0.3505 -0.0139 0.0397  0.0315  148 CYS B N   
4004 C CA  . CYS B 178 ? 0.3834 0.3672 0.3494 -0.0102 0.0345  0.0298  148 CYS B CA  
4005 C C   . CYS B 178 ? 0.3796 0.3660 0.3462 -0.0106 0.0316  0.0258  148 CYS B C   
4006 O O   . CYS B 178 ? 0.3932 0.3813 0.3561 -0.0072 0.0280  0.0240  148 CYS B O   
4007 C CB  . CYS B 178 ? 0.3921 0.3798 0.3543 -0.0061 0.0344  0.0309  148 CYS B CB  
4008 S SG  . CYS B 178 ? 0.4392 0.4237 0.3991 -0.0037 0.0363  0.0356  148 CYS B SG  
4009 N N   . CYS B 179 ? 0.3629 0.3493 0.3335 -0.0141 0.0331  0.0242  149 CYS B N   
4010 C CA  . CYS B 179 ? 0.3542 0.3434 0.3253 -0.0142 0.0308  0.0205  149 CYS B CA  
4011 C C   . CYS B 179 ? 0.3621 0.3458 0.3320 -0.0136 0.0269  0.0204  149 CYS B C   
4012 O O   . CYS B 179 ? 0.3651 0.3454 0.3379 -0.0160 0.0278  0.0215  149 CYS B O   
4013 C CB  . CYS B 179 ? 0.3492 0.3416 0.3254 -0.0183 0.0343  0.0189  149 CYS B CB  
4014 S SG  . CYS B 179 ? 0.3869 0.3867 0.3652 -0.0204 0.0393  0.0189  149 CYS B SG  
4015 N N   . LEU B 180 ? 0.3570 0.3395 0.3223 -0.0103 0.0224  0.0191  150 LEU B N   
4016 C CA  . LEU B 180 ? 0.3556 0.3324 0.3194 -0.0103 0.0187  0.0193  150 LEU B CA  
4017 C C   . LEU B 180 ? 0.3530 0.3293 0.3152 -0.0094 0.0160  0.0166  150 LEU B C   
4018 O O   . LEU B 180 ? 0.3538 0.3262 0.3167 -0.0109 0.0144  0.0171  150 LEU B O   
4019 C CB  . LEU B 180 ? 0.3593 0.3328 0.3189 -0.0079 0.0154  0.0205  150 LEU B CB  
4020 C CG  . LEU B 180 ? 0.3756 0.3494 0.3362 -0.0081 0.0178  0.0235  150 LEU B CG  
4021 C CD1 . LEU B 180 ? 0.3719 0.3446 0.3279 -0.0048 0.0147  0.0238  150 LEU B CD1 
4022 C CD2 . LEU B 180 ? 0.3853 0.3565 0.3496 -0.0110 0.0191  0.0257  150 LEU B CD2 
4023 N N   . ILE B 181 ? 0.3484 0.3292 0.3083 -0.0069 0.0158  0.0140  151 ILE B N   
4024 C CA  . ILE B 181 ? 0.3560 0.3364 0.3133 -0.0050 0.0135  0.0114  151 ILE B CA  
4025 C C   . ILE B 181 ? 0.3558 0.3402 0.3185 -0.0078 0.0162  0.0104  151 ILE B C   
4026 O O   . ILE B 181 ? 0.3573 0.3486 0.3236 -0.0091 0.0196  0.0092  151 ILE B O   
4027 C CB  . ILE B 181 ? 0.3654 0.3495 0.3173 -0.0002 0.0118  0.0087  151 ILE B CB  
4028 C CG1 . ILE B 181 ? 0.3844 0.3640 0.3306 0.0030  0.0086  0.0093  151 ILE B CG1 
4029 C CG2 . ILE B 181 ? 0.3641 0.3478 0.3126 0.0025  0.0097  0.0060  151 ILE B CG2 
4030 C CD1 . ILE B 181 ? 0.4144 0.3838 0.3570 0.0028  0.0044  0.0101  151 ILE B CD1 
4031 N N   . VAL B 182 ? 0.3471 0.3272 0.3104 -0.0089 0.0148  0.0109  152 VAL B N   
4032 C CA  . VAL B 182 ? 0.3414 0.3248 0.3092 -0.0108 0.0168  0.0099  152 VAL B CA  
4033 C C   . VAL B 182 ? 0.3358 0.3191 0.2998 -0.0077 0.0144  0.0077  152 VAL B C   
4034 O O   . VAL B 182 ? 0.3429 0.3196 0.3016 -0.0057 0.0110  0.0086  152 VAL B O   
4035 C CB  . VAL B 182 ? 0.3458 0.3253 0.3173 -0.0142 0.0175  0.0127  152 VAL B CB  
4036 C CG1 . VAL B 182 ? 0.3400 0.3230 0.3159 -0.0156 0.0193  0.0114  152 VAL B CG1 
4037 C CG2 . VAL B 182 ? 0.3474 0.3261 0.3213 -0.0163 0.0198  0.0150  152 VAL B CG2 
4038 N N   . TYR B 183 ? 0.3247 0.3153 0.2911 -0.0072 0.0161  0.0049  153 TYR B N   
4039 C CA  . TYR B 183 ? 0.3314 0.3236 0.2946 -0.0037 0.0146  0.0026  153 TYR B CA  
4040 C C   . TYR B 183 ? 0.3326 0.3245 0.2997 -0.0057 0.0153  0.0033  153 TYR B C   
4041 O O   . TYR B 183 ? 0.3321 0.3274 0.3053 -0.0091 0.0181  0.0033  153 TYR B O   
4042 C CB  . TYR B 183 ? 0.3283 0.3312 0.2920 -0.0016 0.0161  -0.0014 153 TYR B CB  
4043 C CG  . TYR B 183 ? 0.3470 0.3512 0.3060 0.0015  0.0150  -0.0021 153 TYR B CG  
4044 C CD1 . TYR B 183 ? 0.3534 0.3595 0.3150 -0.0010 0.0170  -0.0010 153 TYR B CD1 
4045 C CD2 . TYR B 183 ? 0.3614 0.3644 0.3124 0.0074  0.0120  -0.0037 153 TYR B CD2 
4046 C CE1 . TYR B 183 ? 0.3681 0.3759 0.3251 0.0022  0.0159  -0.0014 153 TYR B CE1 
4047 C CE2 . TYR B 183 ? 0.3774 0.3819 0.3235 0.0110  0.0108  -0.0045 153 TYR B CE2 
4048 C CZ  . TYR B 183 ? 0.3858 0.3932 0.3352 0.0083  0.0127  -0.0033 153 TYR B CZ  
4049 O OH  . TYR B 183 ? 0.4050 0.4146 0.3496 0.0120  0.0115  -0.0039 153 TYR B OH  
4050 N N   . HIS B 184 ? 0.3308 0.3180 0.2939 -0.0034 0.0130  0.0043  154 HIS B N   
4051 C CA  . HIS B 184 ? 0.3279 0.3152 0.2941 -0.0047 0.0136  0.0054  154 HIS B CA  
4052 C C   . HIS B 184 ? 0.3306 0.3220 0.2940 -0.0003 0.0131  0.0029  154 HIS B C   
4053 O O   . HIS B 184 ? 0.3393 0.3307 0.2968 0.0040  0.0116  0.0012  154 HIS B O   
4054 C CB  . HIS B 184 ? 0.3302 0.3084 0.2949 -0.0066 0.0116  0.0098  154 HIS B CB  
4055 C CG  . HIS B 184 ? 0.3457 0.3209 0.3128 -0.0102 0.0119  0.0121  154 HIS B CG  
4056 N ND1 . HIS B 184 ? 0.3608 0.3392 0.3340 -0.0133 0.0146  0.0128  154 HIS B ND1 
4057 C CD2 . HIS B 184 ? 0.3574 0.3267 0.3208 -0.0104 0.0099  0.0135  154 HIS B CD2 
4058 C CE1 . HIS B 184 ? 0.3646 0.3393 0.3377 -0.0151 0.0142  0.0150  154 HIS B CE1 
4059 N NE2 . HIS B 184 ? 0.3712 0.3409 0.3388 -0.0135 0.0114  0.0154  154 HIS B NE2 
4060 N N   . PRO B 185 ? 0.3203 0.3155 0.2873 -0.0006 0.0143  0.0027  155 PRO B N   
4061 C CA  . PRO B 185 ? 0.3274 0.3275 0.2916 0.0042  0.0139  0.0003  155 PRO B CA  
4062 C C   . PRO B 185 ? 0.3488 0.3406 0.3052 0.0077  0.0113  0.0029  155 PRO B C   
4063 O O   . PRO B 185 ? 0.3533 0.3482 0.3057 0.0127  0.0110  0.0011  155 PRO B O   
4064 C CB  . PRO B 185 ? 0.3188 0.3256 0.2896 0.0025  0.0160  -0.0007 155 PRO B CB  
4065 C CG  . PRO B 185 ? 0.3118 0.3178 0.2888 -0.0029 0.0177  0.0004  155 PRO B CG  
4066 C CD  . PRO B 185 ? 0.3017 0.2982 0.2753 -0.0046 0.0160  0.0042  155 PRO B CD  
4067 N N   . TYR B 186 ? 0.3597 0.3409 0.3136 0.0053  0.0095  0.0071  156 TYR B N   
4068 C CA  . TYR B 186 ? 0.3786 0.3503 0.3253 0.0075  0.0072  0.0101  156 TYR B CA  
4069 C C   . TYR B 186 ? 0.4025 0.3701 0.3398 0.0134  0.0052  0.0082  156 TYR B C   
4070 O O   . TYR B 186 ? 0.4081 0.3724 0.3397 0.0174  0.0045  0.0090  156 TYR B O   
4071 C CB  . TYR B 186 ? 0.3833 0.3453 0.3298 0.0027  0.0056  0.0144  156 TYR B CB  
4072 C CG  . TYR B 186 ? 0.3836 0.3494 0.3381 -0.0022 0.0073  0.0167  156 TYR B CG  
4073 C CD1 . TYR B 186 ? 0.3921 0.3594 0.3485 -0.0026 0.0080  0.0192  156 TYR B CD1 
4074 C CD2 . TYR B 186 ? 0.3842 0.3520 0.3438 -0.0059 0.0083  0.0166  156 TYR B CD2 
4075 C CE1 . TYR B 186 ? 0.4015 0.3727 0.3646 -0.0064 0.0094  0.0213  156 TYR B CE1 
4076 C CE2 . TYR B 186 ? 0.3890 0.3600 0.3549 -0.0095 0.0098  0.0186  156 TYR B CE2 
4077 C CZ  . TYR B 186 ? 0.4029 0.3757 0.3705 -0.0097 0.0102  0.0208  156 TYR B CZ  
4078 O OH  . TYR B 186 ? 0.4142 0.3908 0.3876 -0.0126 0.0116  0.0227  156 TYR B OH  
4079 N N   . ARG B 187 ? 0.4099 0.3771 0.3449 0.0143  0.0043  0.0061  157 ARG B N   
4080 C CA  . ARG B 187 ? 0.4249 0.3890 0.3506 0.0205  0.0023  0.0039  157 ARG B CA  
4081 C C   . ARG B 187 ? 0.4186 0.3937 0.3434 0.0262  0.0037  0.0001  157 ARG B C   
4082 O O   . ARG B 187 ? 0.4270 0.3980 0.3440 0.0318  0.0025  0.0002  157 ARG B O   
4083 C CB  . ARG B 187 ? 0.4680 0.4311 0.3924 0.0202  0.0012  0.0025  157 ARG B CB  
4084 C CG  . ARG B 187 ? 0.5575 0.5219 0.4734 0.0274  -0.0004 -0.0008 157 ARG B CG  
4085 C CD  . ARG B 187 ? 0.6586 0.6190 0.5712 0.0277  -0.0023 -0.0014 157 ARG B CD  
4086 N NE  . ARG B 187 ? 0.7390 0.7045 0.6603 0.0218  -0.0004 -0.0007 157 ARG B NE  
4087 C CZ  . ARG B 187 ? 0.7702 0.7483 0.6973 0.0210  0.0023  -0.0030 157 ARG B CZ  
4088 N NH1 . ARG B 187 ? 0.7750 0.7635 0.7009 0.0255  0.0033  -0.0067 157 ARG B NH1 
4089 N NH2 . ARG B 187 ? 0.7639 0.7444 0.6979 0.0157  0.0041  -0.0018 157 ARG B NH2 
4090 N N   . PRO B 188 ? 0.4058 0.3949 0.3383 0.0249  0.0063  -0.0033 158 PRO B N   
4091 C CA  . PRO B 188 ? 0.3991 0.4001 0.3311 0.0301  0.0075  -0.0074 158 PRO B CA  
4092 C C   . PRO B 188 ? 0.4079 0.4078 0.3390 0.0322  0.0078  -0.0058 158 PRO B C   
4093 O O   . PRO B 188 ? 0.4115 0.4140 0.3362 0.0390  0.0073  -0.0076 158 PRO B O   
4094 C CB  . PRO B 188 ? 0.3945 0.4091 0.3365 0.0259  0.0104  -0.0108 158 PRO B CB  
4095 C CG  . PRO B 188 ? 0.4003 0.4092 0.3480 0.0188  0.0110  -0.0078 158 PRO B CG  
4096 C CD  . PRO B 188 ? 0.3873 0.3820 0.3286 0.0188  0.0083  -0.0039 158 PRO B CD  
4097 N N   . LEU B 189 ? 0.4125 0.4079 0.3487 0.0269  0.0085  -0.0022 159 LEU B N   
4098 C CA  . LEU B 189 ? 0.4285 0.4231 0.3637 0.0290  0.0088  -0.0001 159 LEU B CA  
4099 C C   . LEU B 189 ? 0.4524 0.4354 0.3762 0.0342  0.0067  0.0027  159 LEU B C   
4100 O O   . LEU B 189 ? 0.4543 0.4404 0.3739 0.0401  0.0070  0.0020  159 LEU B O   
4101 C CB  . LEU B 189 ? 0.4254 0.4178 0.3677 0.0226  0.0098  0.0037  159 LEU B CB  
4102 C CG  . LEU B 189 ? 0.4419 0.4327 0.3828 0.0245  0.0101  0.0069  159 LEU B CG  
4103 C CD1 . LEU B 189 ? 0.4397 0.4438 0.3831 0.0290  0.0118  0.0030  159 LEU B CD1 
4104 C CD2 . LEU B 189 ? 0.4520 0.4391 0.3984 0.0183  0.0105  0.0113  159 LEU B CD2 
4105 N N   . LEU B 190 ? 0.4693 0.4388 0.3877 0.0324  0.0044  0.0055  160 LEU B N   
4106 C CA  . LEU B 190 ? 0.4934 0.4493 0.4001 0.0369  0.0022  0.0081  160 LEU B CA  
4107 C C   . LEU B 190 ? 0.5031 0.4628 0.4015 0.0460  0.0016  0.0041  160 LEU B C   
4108 O O   . LEU B 190 ? 0.5148 0.4695 0.4050 0.0519  0.0011  0.0054  160 LEU B O   
4109 C CB  . LEU B 190 ? 0.5137 0.4553 0.4165 0.0332  -0.0004 0.0105  160 LEU B CB  
4110 C CG  . LEU B 190 ? 0.5495 0.4858 0.4585 0.0248  -0.0004 0.0150  160 LEU B CG  
4111 C CD1 . LEU B 190 ? 0.5574 0.4857 0.4658 0.0207  -0.0025 0.0154  160 LEU B CD1 
4112 C CD2 . LEU B 190 ? 0.5683 0.4956 0.4732 0.0244  -0.0006 0.0198  160 LEU B CD2 
4113 N N   . GLN B 191 ? 0.4974 0.4668 0.3978 0.0474  0.0018  -0.0005 161 GLN B N   
4114 C CA  . GLN B 191 ? 0.5005 0.4764 0.3937 0.0562  0.0013  -0.0048 161 GLN B CA  
4115 C C   . GLN B 191 ? 0.4884 0.4776 0.3836 0.0607  0.0033  -0.0072 161 GLN B C   
4116 O O   . GLN B 191 ? 0.4907 0.4798 0.3767 0.0692  0.0027  -0.0083 161 GLN B O   
4117 C CB  . GLN B 191 ? 0.5265 0.5120 0.4231 0.0555  0.0014  -0.0088 161 GLN B CB  
4118 C CG  . GLN B 191 ? 0.5959 0.5689 0.4889 0.0528  -0.0010 -0.0070 161 GLN B CG  
4119 C CD  . GLN B 191 ? 0.6692 0.6521 0.5680 0.0501  -0.0003 -0.0098 161 GLN B CD  
4120 O OE1 . GLN B 191 ? 0.6882 0.6862 0.5959 0.0477  0.0024  -0.0126 161 GLN B OE1 
4121 N NE2 . GLN B 191 ? 0.6832 0.6574 0.5772 0.0502  -0.0026 -0.0092 161 GLN B NE2 
4122 N N   . TYR B 192 ? 0.4745 0.4745 0.3812 0.0554  0.0057  -0.0080 162 TYR B N   
4123 C CA  . TYR B 192 ? 0.4718 0.4850 0.3812 0.0593  0.0076  -0.0106 162 TYR B CA  
4124 C C   . TYR B 192 ? 0.4800 0.4851 0.3831 0.0634  0.0074  -0.0066 162 TYR B C   
4125 O O   . TYR B 192 ? 0.4800 0.4907 0.3770 0.0716  0.0075  -0.0085 162 TYR B O   
4126 C CB  . TYR B 192 ? 0.4616 0.4868 0.3845 0.0525  0.0099  -0.0127 162 TYR B CB  
4127 C CG  . TYR B 192 ? 0.4650 0.5011 0.3942 0.0493  0.0108  -0.0173 162 TYR B CG  
4128 C CD1 . TYR B 192 ? 0.4697 0.5160 0.3950 0.0550  0.0105  -0.0221 162 TYR B CD1 
4129 C CD2 . TYR B 192 ? 0.4726 0.5092 0.4113 0.0407  0.0121  -0.0168 162 TYR B CD2 
4130 C CE1 . TYR B 192 ? 0.4754 0.5328 0.4069 0.0516  0.0116  -0.0260 162 TYR B CE1 
4131 C CE2 . TYR B 192 ? 0.4774 0.5230 0.4214 0.0374  0.0131  -0.0205 162 TYR B CE2 
4132 C CZ  . TYR B 192 ? 0.4856 0.5420 0.4264 0.0425  0.0130  -0.0251 162 TYR B CZ  
4133 O OH  . TYR B 192 ? 0.5030 0.5695 0.4495 0.0389  0.0144  -0.0284 162 TYR B OH  
4134 N N   . VAL B 193 ? 0.4900 0.4827 0.3942 0.0580  0.0071  -0.0008 163 VAL B N   
4135 C CA  . VAL B 193 ? 0.5065 0.4914 0.4047 0.0612  0.0072  0.0038  163 VAL B CA  
4136 C C   . VAL B 193 ? 0.5308 0.5023 0.4143 0.0684  0.0053  0.0055  163 VAL B C   
4137 O O   . VAL B 193 ? 0.5431 0.5123 0.4196 0.0748  0.0058  0.0074  163 VAL B O   
4138 C CB  . VAL B 193 ? 0.5167 0.4938 0.4203 0.0533  0.0076  0.0096  163 VAL B CB  
4139 C CG1 . VAL B 193 ? 0.5118 0.5012 0.4287 0.0471  0.0094  0.0076  163 VAL B CG1 
4140 C CG2 . VAL B 193 ? 0.5349 0.4952 0.4346 0.0483  0.0055  0.0134  163 VAL B CG2 
4141 N N   . GLN B 194 ? 0.5361 0.4990 0.4144 0.0682  0.0031  0.0046  164 GLN B N   
4142 C CA  . GLN B 194 ? 0.5534 0.5031 0.4169 0.0756  0.0010  0.0054  164 GLN B CA  
4143 C C   . GLN B 194 ? 0.5544 0.5174 0.4130 0.0861  0.0016  0.0004  164 GLN B C   
4144 O O   . GLN B 194 ? 0.5658 0.5238 0.4145 0.0938  0.0017  0.0020  164 GLN B O   
4145 C CB  . GLN B 194 ? 0.5818 0.5215 0.4419 0.0732  -0.0017 0.0047  164 GLN B CB  
4146 C CG  . GLN B 194 ? 0.6559 0.5836 0.5000 0.0823  -0.0041 0.0041  164 GLN B CG  
4147 C CD  . GLN B 194 ? 0.7350 0.6589 0.5763 0.0821  -0.0066 0.0014  164 GLN B CD  
4148 O OE1 . GLN B 194 ? 0.7479 0.6864 0.5920 0.0850  -0.0063 -0.0036 164 GLN B OE1 
4149 N NE2 . GLN B 194 ? 0.7528 0.6574 0.5882 0.0788  -0.0092 0.0047  164 GLN B NE2 
4150 N N   . ASP B 195 ? 0.5391 0.5201 0.4053 0.0860  0.0025  -0.0054 165 ASP B N   
4151 C CA  . ASP B 195 ? 0.5427 0.5397 0.4058 0.0952  0.0032  -0.0108 165 ASP B CA  
4152 C C   . ASP B 195 ? 0.5509 0.5549 0.4143 0.0995  0.0051  -0.0101 165 ASP B C   
4153 O O   . ASP B 195 ? 0.5567 0.5633 0.4104 0.1097  0.0050  -0.0115 165 ASP B O   
4154 C CB  . ASP B 195 ? 0.5527 0.5690 0.4265 0.0918  0.0043  -0.0167 165 ASP B CB  
4155 C CG  . ASP B 195 ? 0.6224 0.6568 0.4934 0.1008  0.0049  -0.0227 165 ASP B CG  
4156 O OD1 . ASP B 195 ? 0.6544 0.6883 0.5159 0.1079  0.0033  -0.0247 165 ASP B OD1 
4157 O OD2 . ASP B 195 ? 0.6465 0.6961 0.5245 0.1011  0.0068  -0.0255 165 ASP B OD2 
4158 N N   . MET B 196 ? 0.5571 0.5643 0.4309 0.0924  0.0068  -0.0080 166 MET B N   
4159 C CA  . MET B 196 ? 0.5723 0.5863 0.4474 0.0959  0.0086  -0.0070 166 MET B CA  
4160 C C   . MET B 196 ? 0.5995 0.5972 0.4622 0.1015  0.0082  -0.0010 166 MET B C   
4161 O O   . MET B 196 ? 0.6009 0.6047 0.4609 0.1078  0.0096  -0.0005 166 MET B O   
4162 C CB  . MET B 196 ? 0.5716 0.5892 0.4599 0.0864  0.0101  -0.0051 166 MET B CB  
4163 C CG  . MET B 196 ? 0.5892 0.6266 0.4893 0.0837  0.0116  -0.0112 166 MET B CG  
4164 S SD  . MET B 196 ? 0.6351 0.6764 0.5465 0.0772  0.0134  -0.0086 166 MET B SD  
4165 C CE  . MET B 196 ? 0.5640 0.6275 0.4871 0.0752  0.0147  -0.0171 166 MET B CE  
4166 N N   . GLY B 197 ? 0.6180 0.5954 0.4738 0.0985  0.0064  0.0038  167 GLY B N   
4167 C CA  . GLY B 197 ? 0.6484 0.6074 0.4926 0.1017  0.0061  0.0103  167 GLY B CA  
4168 C C   . GLY B 197 ? 0.6670 0.6254 0.5182 0.0960  0.0080  0.0155  167 GLY B C   
4169 O O   . GLY B 197 ? 0.6807 0.6314 0.5243 0.1003  0.0089  0.0203  167 GLY B O   
4170 N N   . GLN B 198 ? 0.6611 0.6276 0.5264 0.0865  0.0087  0.0149  168 GLN B N   
4171 C CA  . GLN B 198 ? 0.6683 0.6376 0.5415 0.0811  0.0105  0.0191  168 GLN B CA  
4172 C C   . GLN B 198 ? 0.6762 0.6362 0.5561 0.0697  0.0098  0.0231  168 GLN B C   
4173 O O   . GLN B 198 ? 0.6680 0.6357 0.5581 0.0642  0.0111  0.0244  168 GLN B O   
4174 C CB  . GLN B 198 ? 0.6789 0.6704 0.5631 0.0819  0.0122  0.0138  168 GLN B CB  
4175 C CG  . GLN B 198 ? 0.7314 0.7339 0.6104 0.0928  0.0134  0.0110  168 GLN B CG  
4176 C CD  . GLN B 198 ? 0.8080 0.8039 0.6812 0.0961  0.0147  0.0175  168 GLN B CD  
4177 O OE1 . GLN B 198 ? 0.8385 0.8316 0.7177 0.0897  0.0155  0.0224  168 GLN B OE1 
4178 N NE2 . GLN B 198 ? 0.8193 0.8129 0.6806 0.1066  0.0149  0.0180  168 GLN B NE2 
4179 N N   . GLU B 199 ? 0.6891 0.6329 0.5629 0.0668  0.0076  0.0251  169 GLU B N   
4180 C CA  . GLU B 199 ? 0.6991 0.6341 0.5784 0.0564  0.0066  0.0285  169 GLU B CA  
4181 C C   . GLU B 199 ? 0.7065 0.6378 0.5892 0.0509  0.0079  0.0352  169 GLU B C   
4182 O O   . GLU B 199 ? 0.7058 0.6432 0.5990 0.0436  0.0084  0.0360  169 GLU B O   
4183 C CB  . GLU B 199 ? 0.7375 0.6549 0.6076 0.0555  0.0038  0.0293  169 GLU B CB  
4184 C CG  . GLU B 199 ? 0.8070 0.7291 0.6744 0.0604  0.0024  0.0228  169 GLU B CG  
4185 C CD  . GLU B 199 ? 0.9089 0.8139 0.7660 0.0611  -0.0006 0.0231  169 GLU B CD  
4186 O OE1 . GLU B 199 ? 0.9281 0.8218 0.7720 0.0683  -0.0016 0.0242  169 GLU B OE1 
4187 O OE2 . GLU B 199 ? 0.9524 0.8550 0.8141 0.0548  -0.0021 0.0221  169 GLU B OE2 
4188 N N   . ASP B 200 ? 0.7129 0.6344 0.5864 0.0547  0.0084  0.0402  170 ASP B N   
4189 C CA  . ASP B 200 ? 0.7179 0.6359 0.5941 0.0493  0.0097  0.0472  170 ASP B CA  
4190 C C   . ASP B 200 ? 0.6949 0.6314 0.5823 0.0486  0.0121  0.0468  170 ASP B C   
4191 O O   . ASP B 200 ? 0.6917 0.6300 0.5865 0.0414  0.0127  0.0506  170 ASP B O   
4192 C CB  . ASP B 200 ? 0.7619 0.6662 0.6254 0.0542  0.0102  0.0528  170 ASP B CB  
4193 C CG  . ASP B 200 ? 0.8650 0.7472 0.7172 0.0528  0.0077  0.0548  170 ASP B CG  
4194 O OD1 . ASP B 200 ? 0.8794 0.7566 0.7349 0.0463  0.0055  0.0529  170 ASP B OD1 
4195 O OD2 . ASP B 200 ? 0.9188 0.7880 0.7585 0.0583  0.0080  0.0583  170 ASP B OD2 
4196 N N   . MET B 201 ? 0.6782 0.6288 0.5668 0.0563  0.0133  0.0418  171 MET B N   
4197 C CA  . MET B 201 ? 0.6624 0.6303 0.5605 0.0569  0.0153  0.0407  171 MET B CA  
4198 C C   . MET B 201 ? 0.6280 0.6076 0.5382 0.0517  0.0151  0.0354  171 MET B C   
4199 O O   . MET B 201 ? 0.6268 0.6135 0.5456 0.0471  0.0161  0.0371  171 MET B O   
4200 C CB  . MET B 201 ? 0.6813 0.6595 0.5748 0.0678  0.0166  0.0375  171 MET B CB  
4201 C CG  . MET B 201 ? 0.7332 0.7288 0.6351 0.0696  0.0186  0.0364  171 MET B CG  
4202 S SD  . MET B 201 ? 0.8890 0.9017 0.7889 0.0814  0.0194  0.0287  171 MET B SD  
4203 C CE  . MET B 201 ? 0.8726 0.9017 0.7814 0.0824  0.0214  0.0293  171 MET B CE  
4204 N N   . LEU B 202 ? 0.5959 0.5776 0.5064 0.0526  0.0140  0.0293  172 LEU B N   
4205 C CA  . LEU B 202 ? 0.5656 0.5585 0.4868 0.0484  0.0142  0.0241  172 LEU B CA  
4206 C C   . LEU B 202 ? 0.5370 0.5225 0.4622 0.0400  0.0129  0.0248  172 LEU B C   
4207 O O   . LEU B 202 ? 0.5265 0.5199 0.4611 0.0354  0.0136  0.0228  172 LEU B O   
4208 C CB  . LEU B 202 ? 0.5683 0.5717 0.4888 0.0543  0.0142  0.0166  172 LEU B CB  
4209 C CG  . LEU B 202 ? 0.5823 0.5980 0.5012 0.0627  0.0156  0.0141  172 LEU B CG  
4210 C CD1 . LEU B 202 ? 0.5841 0.6094 0.5010 0.0686  0.0153  0.0068  172 LEU B CD1 
4211 C CD2 . LEU B 202 ? 0.5786 0.6068 0.5077 0.0605  0.0171  0.0133  172 LEU B CD2 
4212 N N   . LEU B 203 ? 0.5206 0.4914 0.4385 0.0384  0.0110  0.0272  173 LEU B N   
4213 C CA  . LEU B 203 ? 0.5062 0.4710 0.4277 0.0311  0.0096  0.0273  173 LEU B CA  
4214 C C   . LEU B 203 ? 0.4815 0.4472 0.4112 0.0233  0.0102  0.0313  173 LEU B C   
4215 O O   . LEU B 203 ? 0.4726 0.4441 0.4099 0.0193  0.0105  0.0288  173 LEU B O   
4216 C CB  . LEU B 203 ? 0.5175 0.4662 0.4294 0.0311  0.0072  0.0289  173 LEU B CB  
4217 C CG  . LEU B 203 ? 0.5416 0.4851 0.4565 0.0247  0.0056  0.0281  173 LEU B CG  
4218 C CD1 . LEU B 203 ? 0.5351 0.4897 0.4556 0.0255  0.0061  0.0219  173 LEU B CD1 
4219 C CD2 . LEU B 203 ? 0.5603 0.4868 0.4650 0.0249  0.0028  0.0299  173 LEU B CD2 
4220 N N   . PRO B 204 ? 0.4699 0.4311 0.3984 0.0212  0.0106  0.0374  174 PRO B N   
4221 C CA  . PRO B 204 ? 0.4499 0.4143 0.3865 0.0142  0.0111  0.0408  174 PRO B CA  
4222 C C   . PRO B 204 ? 0.4263 0.4056 0.3727 0.0141  0.0128  0.0372  174 PRO B C   
4223 O O   . PRO B 204 ? 0.4263 0.4073 0.3788 0.0090  0.0126  0.0366  174 PRO B O   
4224 C CB  . PRO B 204 ? 0.4577 0.4181 0.3910 0.0139  0.0118  0.0475  174 PRO B CB  
4225 C CG  . PRO B 204 ? 0.4787 0.4256 0.4003 0.0178  0.0106  0.0486  174 PRO B CG  
4226 C CD  . PRO B 204 ? 0.4637 0.4163 0.3831 0.0250  0.0106  0.0419  174 PRO B CD  
4227 N N   . LEU B 205 ? 0.4054 0.3949 0.3527 0.0200  0.0143  0.0347  175 LEU B N   
4228 C CA  . LEU B 205 ? 0.3944 0.3972 0.3502 0.0203  0.0156  0.0307  175 LEU B CA  
4229 C C   . LEU B 205 ? 0.3834 0.3891 0.3426 0.0192  0.0155  0.0244  175 LEU B C   
4230 O O   . LEU B 205 ? 0.3758 0.3851 0.3418 0.0150  0.0159  0.0232  175 LEU B O   
4231 C CB  . LEU B 205 ? 0.4011 0.4141 0.3565 0.0272  0.0170  0.0291  175 LEU B CB  
4232 C CG  . LEU B 205 ? 0.4238 0.4502 0.3872 0.0280  0.0182  0.0245  175 LEU B CG  
4233 C CD1 . LEU B 205 ? 0.4310 0.4592 0.4008 0.0228  0.0186  0.0277  175 LEU B CD1 
4234 C CD2 . LEU B 205 ? 0.4329 0.4691 0.3951 0.0352  0.0193  0.0231  175 LEU B CD2 
4235 N N   . ALA B 206 ? 0.3789 0.3830 0.3331 0.0229  0.0148  0.0207  176 ALA B N   
4236 C CA  . ALA B 206 ? 0.3657 0.3735 0.3232 0.0217  0.0148  0.0150  176 ALA B CA  
4237 C C   . ALA B 206 ? 0.3623 0.3625 0.3219 0.0151  0.0140  0.0168  176 ALA B C   
4238 O O   . ALA B 206 ? 0.3567 0.3612 0.3222 0.0121  0.0148  0.0139  176 ALA B O   
4239 C CB  . ALA B 206 ? 0.3613 0.3690 0.3121 0.0272  0.0141  0.0114  176 ALA B CB  
4240 N N   . TRP B 207 ? 0.3662 0.3549 0.3209 0.0129  0.0124  0.0217  177 TRP B N   
4241 C CA  . TRP B 207 ? 0.3730 0.3547 0.3292 0.0070  0.0113  0.0235  177 TRP B CA  
4242 C C   . TRP B 207 ? 0.3508 0.3375 0.3149 0.0025  0.0125  0.0252  177 TRP B C   
4243 O O   . TRP B 207 ? 0.3514 0.3386 0.3195 -0.0009 0.0127  0.0238  177 TRP B O   
4244 C CB  . TRP B 207 ? 0.3867 0.3554 0.3358 0.0055  0.0093  0.0283  177 TRP B CB  
4245 C CG  . TRP B 207 ? 0.4062 0.3678 0.3561 0.0000  0.0077  0.0297  177 TRP B CG  
4246 C CD1 . TRP B 207 ? 0.4134 0.3755 0.3685 -0.0056 0.0078  0.0328  177 TRP B CD1 
4247 C CD2 . TRP B 207 ? 0.4165 0.3698 0.3610 0.0002  0.0057  0.0281  177 TRP B CD2 
4248 N NE1 . TRP B 207 ? 0.4198 0.3746 0.3734 -0.0090 0.0059  0.0331  177 TRP B NE1 
4249 C CE2 . TRP B 207 ? 0.4238 0.3729 0.3709 -0.0055 0.0046  0.0302  177 TRP B CE2 
4250 C CE3 . TRP B 207 ? 0.4271 0.3767 0.3645 0.0053  0.0046  0.0250  177 TRP B CE3 
4251 C CZ2 . TRP B 207 ? 0.4409 0.3823 0.3840 -0.0064 0.0024  0.0291  177 TRP B CZ2 
4252 C CZ3 . TRP B 207 ? 0.4434 0.3851 0.3765 0.0045  0.0024  0.0240  177 TRP B CZ3 
4253 C CH2 . TRP B 207 ? 0.4458 0.3834 0.3819 -0.0013 0.0013  0.0260  177 TRP B CH2 
4254 N N   . ARG B 208 ? 0.3389 0.3296 0.3049 0.0030  0.0133  0.0283  178 ARG B N   
4255 C CA  . ARG B 208 ? 0.3296 0.3260 0.3024 -0.0002 0.0144  0.0300  178 ARG B CA  
4256 C C   . ARG B 208 ? 0.3385 0.3435 0.3169 0.0009  0.0159  0.0246  178 ARG B C   
4257 O O   . ARG B 208 ? 0.3438 0.3500 0.3268 -0.0023 0.0165  0.0245  178 ARG B O   
4258 C CB  . ARG B 208 ? 0.3299 0.3299 0.3026 0.0011  0.0149  0.0344  178 ARG B CB  
4259 C CG  . ARG B 208 ? 0.3381 0.3470 0.3175 0.0002  0.0162  0.0351  178 ARG B CG  
4260 C CD  . ARG B 208 ? 0.3508 0.3697 0.3324 0.0055  0.0176  0.0311  178 ARG B CD  
4261 N NE  . ARG B 208 ? 0.3550 0.3809 0.3428 0.0046  0.0186  0.0297  178 ARG B NE  
4262 C CZ  . ARG B 208 ? 0.3515 0.3840 0.3418 0.0057  0.0192  0.0324  178 ARG B CZ  
4263 N NH1 . ARG B 208 ? 0.3364 0.3740 0.3314 0.0054  0.0198  0.0307  178 ARG B NH1 
4264 N NH2 . ARG B 208 ? 0.3193 0.3532 0.3069 0.0075  0.0191  0.0371  178 ARG B NH2 
4265 N N   . ILE B 209 ? 0.3348 0.3455 0.3126 0.0054  0.0166  0.0200  179 ILE B N   
4266 C CA  . ILE B 209 ? 0.3323 0.3507 0.3153 0.0058  0.0180  0.0144  179 ILE B CA  
4267 C C   . ILE B 209 ? 0.3350 0.3496 0.3191 0.0023  0.0181  0.0121  179 ILE B C   
4268 O O   . ILE B 209 ? 0.3399 0.3565 0.3289 -0.0005 0.0192  0.0105  179 ILE B O   
4269 C CB  . ILE B 209 ? 0.3322 0.3592 0.3145 0.0113  0.0186  0.0097  179 ILE B CB  
4270 C CG1 . ILE B 209 ? 0.3408 0.3727 0.3227 0.0150  0.0189  0.0124  179 ILE B CG1 
4271 C CG2 . ILE B 209 ? 0.3265 0.3609 0.3146 0.0103  0.0200  0.0035  179 ILE B CG2 
4272 C CD1 . ILE B 209 ? 0.3477 0.3884 0.3282 0.0213  0.0194  0.0084  179 ILE B CD1 
4273 N N   . VAL B 210 ? 0.3321 0.3402 0.3111 0.0023  0.0168  0.0126  180 VAL B N   
4274 C CA  . VAL B 210 ? 0.3432 0.3476 0.3228 -0.0008 0.0167  0.0112  180 VAL B CA  
4275 C C   . VAL B 210 ? 0.3555 0.3556 0.3381 -0.0055 0.0168  0.0148  180 VAL B C   
4276 O O   . VAL B 210 ? 0.3571 0.3579 0.3432 -0.0080 0.0180  0.0131  180 VAL B O   
4277 C CB  . VAL B 210 ? 0.3510 0.3489 0.3238 0.0008  0.0149  0.0114  180 VAL B CB  
4278 C CG1 . VAL B 210 ? 0.3494 0.3435 0.3228 -0.0025 0.0148  0.0108  180 VAL B CG1 
4279 C CG2 . VAL B 210 ? 0.3466 0.3500 0.3162 0.0060  0.0150  0.0072  180 VAL B CG2 
4280 N N   . ASN B 211 ? 0.3596 0.3559 0.3409 -0.0066 0.0157  0.0198  181 ASN B N   
4281 C CA  . ASN B 211 ? 0.3651 0.3594 0.3493 -0.0105 0.0157  0.0232  181 ASN B CA  
4282 C C   . ASN B 211 ? 0.3618 0.3624 0.3516 -0.0108 0.0177  0.0214  181 ASN B C   
4283 O O   . ASN B 211 ? 0.3784 0.3775 0.3704 -0.0132 0.0185  0.0214  181 ASN B O   
4284 C CB  . ASN B 211 ? 0.3685 0.3606 0.3512 -0.0117 0.0145  0.0286  181 ASN B CB  
4285 C CG  . ASN B 211 ? 0.3887 0.3722 0.3656 -0.0127 0.0123  0.0309  181 ASN B CG  
4286 O OD1 . ASN B 211 ? 0.3988 0.3774 0.3728 -0.0128 0.0114  0.0288  181 ASN B OD1 
4287 N ND2 . ASN B 211 ? 0.3879 0.3692 0.3628 -0.0136 0.0114  0.0352  181 ASN B ND2 
4288 N N   . ASP B 212 ? 0.3421 0.3493 0.3337 -0.0079 0.0186  0.0196  182 ASP B N   
4289 C CA  . ASP B 212 ? 0.3234 0.3364 0.3196 -0.0073 0.0203  0.0171  182 ASP B CA  
4290 C C   . ASP B 212 ? 0.3175 0.3307 0.3161 -0.0086 0.0218  0.0122  182 ASP B C   
4291 O O   . ASP B 212 ? 0.3184 0.3317 0.3200 -0.0099 0.0230  0.0113  182 ASP B O   
4292 C CB  . ASP B 212 ? 0.3146 0.3350 0.3114 -0.0033 0.0205  0.0157  182 ASP B CB  
4293 C CG  . ASP B 212 ? 0.3441 0.3656 0.3394 -0.0021 0.0197  0.0210  182 ASP B CG  
4294 O OD1 . ASP B 212 ? 0.3491 0.3670 0.3441 -0.0050 0.0190  0.0256  182 ASP B OD1 
4295 O OD2 . ASP B 212 ? 0.3637 0.3904 0.3582 0.0016  0.0198  0.0205  182 ASP B OD2 
4296 N N   . THR B 213 ? 0.3133 0.3264 0.3102 -0.0082 0.0217  0.0090  183 THR B N   
4297 C CA  . THR B 213 ? 0.3226 0.3367 0.3220 -0.0101 0.0233  0.0046  183 THR B CA  
4298 C C   . THR B 213 ? 0.3371 0.3448 0.3371 -0.0137 0.0241  0.0067  183 THR B C   
4299 O O   . THR B 213 ? 0.3440 0.3517 0.3465 -0.0158 0.0260  0.0040  183 THR B O   
4300 C CB  . THR B 213 ? 0.3331 0.3498 0.3303 -0.0087 0.0230  0.0011  183 THR B CB  
4301 O OG1 . THR B 213 ? 0.3316 0.3422 0.3242 -0.0088 0.0214  0.0042  183 THR B OG1 
4302 C CG2 . THR B 213 ? 0.3365 0.3606 0.3331 -0.0044 0.0226  -0.0016 183 THR B CG2 
4303 N N   . TYR B 214 ? 0.3493 0.3518 0.3469 -0.0146 0.0227  0.0116  184 TYR B N   
4304 C CA  . TYR B 214 ? 0.3698 0.3671 0.3676 -0.0173 0.0234  0.0138  184 TYR B CA  
4305 C C   . TYR B 214 ? 0.3977 0.3955 0.3983 -0.0177 0.0248  0.0146  184 TYR B C   
4306 O O   . TYR B 214 ? 0.4115 0.4054 0.4123 -0.0192 0.0259  0.0157  184 TYR B O   
4307 C CB  . TYR B 214 ? 0.3670 0.3594 0.3614 -0.0181 0.0213  0.0180  184 TYR B CB  
4308 C CG  . TYR B 214 ? 0.3685 0.3587 0.3594 -0.0176 0.0201  0.0166  184 TYR B CG  
4309 C CD1 . TYR B 214 ? 0.3767 0.3646 0.3670 -0.0188 0.0208  0.0156  184 TYR B CD1 
4310 C CD2 . TYR B 214 ? 0.3711 0.3618 0.3589 -0.0153 0.0184  0.0163  184 TYR B CD2 
4311 C CE1 . TYR B 214 ? 0.3887 0.3754 0.3754 -0.0176 0.0196  0.0141  184 TYR B CE1 
4312 C CE2 . TYR B 214 ? 0.3856 0.3741 0.3693 -0.0139 0.0172  0.0148  184 TYR B CE2 
4313 C CZ  . TYR B 214 ? 0.3998 0.3867 0.3830 -0.0150 0.0177  0.0136  184 TYR B CZ  
4314 O OH  . TYR B 214 ? 0.4111 0.3966 0.3899 -0.0130 0.0164  0.0120  184 TYR B OH  
4315 N N   . ARG B 215 ? 0.4050 0.4074 0.4072 -0.0156 0.0248  0.0140  185 ARG B N   
4316 C CA  . ARG B 215 ? 0.4137 0.4167 0.4179 -0.0151 0.0260  0.0140  185 ARG B CA  
4317 C C   . ARG B 215 ? 0.4212 0.4238 0.4277 -0.0160 0.0282  0.0089  185 ARG B C   
4318 O O   . ARG B 215 ? 0.4421 0.4437 0.4497 -0.0154 0.0293  0.0081  185 ARG B O   
4319 C CB  . ARG B 215 ? 0.4273 0.4362 0.4322 -0.0122 0.0250  0.0155  185 ARG B CB  
4320 C CG  . ARG B 215 ? 0.4758 0.4847 0.4792 -0.0124 0.0235  0.0213  185 ARG B CG  
4321 C CD  . ARG B 215 ? 0.5315 0.5389 0.5324 -0.0135 0.0217  0.0239  185 ARG B CD  
4322 N NE  . ARG B 215 ? 0.5781 0.5844 0.5779 -0.0152 0.0203  0.0291  185 ARG B NE  
4323 C CZ  . ARG B 215 ? 0.6097 0.6124 0.6069 -0.0171 0.0186  0.0315  185 ARG B CZ  
4324 N NH1 . ARG B 215 ? 0.5987 0.5981 0.5935 -0.0168 0.0179  0.0295  185 ARG B NH1 
4325 N NH2 . ARG B 215 ? 0.6044 0.6070 0.6012 -0.0192 0.0173  0.0358  185 ARG B NH2 
4326 N N   . THR B 216 ? 0.3980 0.4014 0.4050 -0.0174 0.0288  0.0053  186 THR B N   
4327 C CA  . THR B 216 ? 0.3845 0.3886 0.3941 -0.0193 0.0308  0.0001  186 THR B CA  
4328 C C   . THR B 216 ? 0.3734 0.3736 0.3824 -0.0226 0.0322  0.0000  186 THR B C   
4329 O O   . THR B 216 ? 0.3751 0.3726 0.3815 -0.0226 0.0312  0.0035  186 THR B O   
4330 C CB  . THR B 216 ? 0.3968 0.4094 0.4081 -0.0174 0.0302  -0.0047 186 THR B CB  
4331 O OG1 . THR B 216 ? 0.4116 0.4263 0.4212 -0.0173 0.0293  -0.0049 186 THR B OG1 
4332 C CG2 . THR B 216 ? 0.3994 0.4169 0.4106 -0.0134 0.0286  -0.0038 186 THR B CG2 
4333 N N   . ASP B 217 ? 0.3601 0.3606 0.3715 -0.0254 0.0343  -0.0042 187 ASP B N   
4334 C CA  . ASP B 217 ? 0.3599 0.3580 0.3711 -0.0286 0.0360  -0.0044 187 ASP B CA  
4335 C C   . ASP B 217 ? 0.3533 0.3586 0.3645 -0.0284 0.0352  -0.0069 187 ASP B C   
4336 O O   . ASP B 217 ? 0.3558 0.3610 0.3670 -0.0309 0.0367  -0.0074 187 ASP B O   
4337 C CB  . ASP B 217 ? 0.3871 0.3826 0.4010 -0.0324 0.0390  -0.0077 187 ASP B CB  
4338 C CG  . ASP B 217 ? 0.4764 0.4627 0.4889 -0.0327 0.0403  -0.0051 187 ASP B CG  
4339 O OD1 . ASP B 217 ? 0.4974 0.4794 0.5069 -0.0308 0.0396  0.0000  187 ASP B OD1 
4340 O OD2 . ASP B 217 ? 0.5146 0.4981 0.5287 -0.0346 0.0420  -0.0083 187 ASP B OD2 
4341 N N   . LEU B 218 ? 0.3415 0.3532 0.3523 -0.0251 0.0331  -0.0085 188 LEU B N   
4342 C CA  . LEU B 218 ? 0.3398 0.3588 0.3498 -0.0237 0.0323  -0.0113 188 LEU B CA  
4343 C C   . LEU B 218 ? 0.3529 0.3698 0.3597 -0.0239 0.0319  -0.0090 188 LEU B C   
4344 O O   . LEU B 218 ? 0.3581 0.3808 0.3656 -0.0248 0.0328  -0.0121 188 LEU B O   
4345 C CB  . LEU B 218 ? 0.3365 0.3601 0.3447 -0.0190 0.0299  -0.0116 188 LEU B CB  
4346 C CG  . LEU B 218 ? 0.3473 0.3771 0.3588 -0.0179 0.0302  -0.0157 188 LEU B CG  
4347 C CD1 . LEU B 218 ? 0.3548 0.3879 0.3639 -0.0128 0.0281  -0.0144 188 LEU B CD1 
4348 C CD2 . LEU B 218 ? 0.3338 0.3720 0.3488 -0.0197 0.0316  -0.0221 188 LEU B CD2 
4349 N N   . CYS B 219 ? 0.3524 0.3623 0.3557 -0.0229 0.0305  -0.0041 189 CYS B N   
4350 C CA  . CYS B 219 ? 0.3617 0.3694 0.3616 -0.0227 0.0299  -0.0022 189 CYS B CA  
4351 C C   . CYS B 219 ? 0.3828 0.3902 0.3845 -0.0262 0.0327  -0.0028 189 CYS B C   
4352 O O   . CYS B 219 ? 0.4022 0.4107 0.4016 -0.0258 0.0325  -0.0024 189 CYS B O   
4353 C CB  . CYS B 219 ? 0.3593 0.3596 0.3556 -0.0214 0.0278  0.0028  189 CYS B CB  
4354 S SG  . CYS B 219 ? 0.3838 0.3771 0.3816 -0.0241 0.0294  0.0066  189 CYS B SG  
4355 N N   . LEU B 220 ? 0.3793 0.3847 0.3847 -0.0296 0.0353  -0.0035 190 LEU B N   
4356 C CA  . LEU B 220 ? 0.3803 0.3846 0.3873 -0.0335 0.0384  -0.0038 190 LEU B CA  
4357 C C   . LEU B 220 ? 0.3849 0.3979 0.3957 -0.0362 0.0401  -0.0092 190 LEU B C   
4358 O O   . LEU B 220 ? 0.3973 0.4110 0.4097 -0.0399 0.0428  -0.0096 190 LEU B O   
4359 C CB  . LEU B 220 ? 0.3800 0.3760 0.3880 -0.0359 0.0406  -0.0016 190 LEU B CB  
4360 C CG  . LEU B 220 ? 0.3986 0.3872 0.4034 -0.0335 0.0392  0.0035  190 LEU B CG  
4361 C CD1 . LEU B 220 ? 0.4079 0.3894 0.4133 -0.0350 0.0414  0.0048  190 LEU B CD1 
4362 C CD2 . LEU B 220 ? 0.4031 0.3894 0.4045 -0.0326 0.0387  0.0070  190 LEU B CD2 
4363 N N   . LEU B 221 ? 0.3786 0.3988 0.3910 -0.0344 0.0388  -0.0132 191 LEU B N   
4364 C CA  . LEU B 221 ? 0.3733 0.4029 0.3899 -0.0371 0.0403  -0.0189 191 LEU B CA  
4365 C C   . LEU B 221 ? 0.3738 0.4148 0.3895 -0.0338 0.0387  -0.0222 191 LEU B C   
4366 O O   . LEU B 221 ? 0.3785 0.4291 0.3975 -0.0363 0.0401  -0.0267 191 LEU B O   
4367 C CB  . LEU B 221 ? 0.3724 0.4018 0.3923 -0.0379 0.0405  -0.0220 191 LEU B CB  
4368 C CG  . LEU B 221 ? 0.3853 0.4037 0.4059 -0.0406 0.0422  -0.0197 191 LEU B CG  
4369 C CD1 . LEU B 221 ? 0.3827 0.4019 0.4056 -0.0399 0.0416  -0.0230 191 LEU B CD1 
4370 C CD2 . LEU B 221 ? 0.3827 0.3976 0.4052 -0.0467 0.0458  -0.0199 191 LEU B CD2 
4371 N N   . TYR B 222 ? 0.3745 0.4150 0.3857 -0.0283 0.0357  -0.0204 192 TYR B N   
4372 C CA  . TYR B 222 ? 0.3711 0.4214 0.3800 -0.0240 0.0340  -0.0234 192 TYR B CA  
4373 C C   . TYR B 222 ? 0.3836 0.4304 0.3860 -0.0196 0.0317  -0.0201 192 TYR B C   
4374 O O   . TYR B 222 ? 0.3940 0.4308 0.3933 -0.0184 0.0302  -0.0155 192 TYR B O   
4375 C CB  . TYR B 222 ? 0.3601 0.4140 0.3692 -0.0203 0.0324  -0.0257 192 TYR B CB  
4376 C CG  . TYR B 222 ? 0.3604 0.4193 0.3755 -0.0237 0.0341  -0.0303 192 TYR B CG  
4377 C CD1 . TYR B 222 ? 0.3649 0.4367 0.3835 -0.0248 0.0350  -0.0365 192 TYR B CD1 
4378 C CD2 . TYR B 222 ? 0.3661 0.4175 0.3834 -0.0256 0.0346  -0.0289 192 TYR B CD2 
4379 C CE1 . TYR B 222 ? 0.3727 0.4491 0.3969 -0.0282 0.0363  -0.0413 192 TYR B CE1 
4380 C CE2 . TYR B 222 ? 0.3713 0.4266 0.3936 -0.0283 0.0358  -0.0335 192 TYR B CE2 
4381 C CZ  . TYR B 222 ? 0.3847 0.4521 0.4105 -0.0299 0.0366  -0.0399 192 TYR B CZ  
4382 O OH  . TYR B 222 ? 0.4101 0.4810 0.4408 -0.0329 0.0376  -0.0450 192 TYR B OH  
4383 N N   . PRO B 223 ? 0.3791 0.4347 0.3789 -0.0164 0.0309  -0.0227 193 PRO B N   
4384 C CA  . PRO B 223 ? 0.3854 0.4371 0.3778 -0.0112 0.0282  -0.0201 193 PRO B CA  
4385 C C   . PRO B 223 ? 0.3955 0.4406 0.3836 -0.0068 0.0255  -0.0180 193 PRO B C   
4386 O O   . PRO B 223 ? 0.3986 0.4478 0.3886 -0.0056 0.0255  -0.0202 193 PRO B O   
4387 C CB  . PRO B 223 ? 0.3856 0.4502 0.3763 -0.0078 0.0281  -0.0244 193 PRO B CB  
4388 C CG  . PRO B 223 ? 0.3865 0.4610 0.3848 -0.0137 0.0314  -0.0282 193 PRO B CG  
4389 C CD  . PRO B 223 ? 0.3645 0.4343 0.3678 -0.0175 0.0325  -0.0283 193 PRO B CD  
4390 N N   . PRO B 224 ? 0.3934 0.4284 0.3760 -0.0048 0.0233  -0.0138 194 PRO B N   
4391 C CA  . PRO B 224 ? 0.3902 0.4177 0.3687 -0.0018 0.0210  -0.0111 194 PRO B CA  
4392 C C   . PRO B 224 ? 0.3840 0.4168 0.3589 0.0039  0.0196  -0.0136 194 PRO B C   
4393 O O   . PRO B 224 ? 0.3861 0.4162 0.3606 0.0051  0.0190  -0.0122 194 PRO B O   
4394 C CB  . PRO B 224 ? 0.4026 0.4199 0.3752 -0.0007 0.0187  -0.0072 194 PRO B CB  
4395 C CG  . PRO B 224 ? 0.4165 0.4343 0.3919 -0.0043 0.0203  -0.0068 194 PRO B CG  
4396 C CD  . PRO B 224 ? 0.3919 0.4217 0.3717 -0.0055 0.0229  -0.0112 194 PRO B CD  
4397 N N   . PHE B 225 ? 0.3767 0.4171 0.3482 0.0079  0.0192  -0.0170 195 PHE B N   
4398 C CA  . PHE B 225 ? 0.3848 0.4307 0.3518 0.0143  0.0181  -0.0194 195 PHE B CA  
4399 C C   . PHE B 225 ? 0.3794 0.4350 0.3526 0.0134  0.0198  -0.0228 195 PHE B C   
4400 O O   . PHE B 225 ? 0.3866 0.4431 0.3568 0.0180  0.0188  -0.0230 195 PHE B O   
4401 C CB  . PHE B 225 ? 0.3884 0.4417 0.3500 0.0195  0.0172  -0.0226 195 PHE B CB  
4402 C CG  . PHE B 225 ? 0.3952 0.4644 0.3629 0.0174  0.0196  -0.0278 195 PHE B CG  
4403 C CD1 . PHE B 225 ? 0.4044 0.4759 0.3764 0.0123  0.0213  -0.0278 195 PHE B CD1 
4404 C CD2 . PHE B 225 ? 0.4038 0.4861 0.3731 0.0205  0.0202  -0.0326 195 PHE B CD2 
4405 C CE1 . PHE B 225 ? 0.4064 0.4925 0.3842 0.0095  0.0237  -0.0323 195 PHE B CE1 
4406 C CE2 . PHE B 225 ? 0.4036 0.5012 0.3792 0.0176  0.0223  -0.0376 195 PHE B CE2 
4407 C CZ  . PHE B 225 ? 0.3958 0.4949 0.3756 0.0118  0.0241  -0.0374 195 PHE B CZ  
4408 N N   . MET B 226 ? 0.3704 0.4320 0.3519 0.0075  0.0222  -0.0252 196 MET B N   
4409 C CA  . MET B 226 ? 0.3713 0.4415 0.3590 0.0060  0.0237  -0.0289 196 MET B CA  
4410 C C   . MET B 226 ? 0.3638 0.4259 0.3529 0.0050  0.0234  -0.0255 196 MET B C   
4411 O O   . MET B 226 ? 0.3597 0.4269 0.3497 0.0077  0.0233  -0.0274 196 MET B O   
4412 C CB  . MET B 226 ? 0.3868 0.4642 0.3821 -0.0004 0.0264  -0.0325 196 MET B CB  
4413 C CG  . MET B 226 ? 0.4325 0.5228 0.4278 0.0007  0.0270  -0.0371 196 MET B CG  
4414 S SD  . MET B 226 ? 0.5784 0.6760 0.5834 -0.0085 0.0305  -0.0408 196 MET B SD  
4415 C CE  . MET B 226 ? 0.5530 0.6636 0.5566 -0.0073 0.0310  -0.0437 196 MET B CE  
4416 N N   . ILE B 227 ? 0.3576 0.4077 0.3464 0.0015  0.0232  -0.0204 197 ILE B N   
4417 C CA  . ILE B 227 ? 0.3603 0.4033 0.3500 0.0008  0.0228  -0.0166 197 ILE B CA  
4418 C C   . ILE B 227 ? 0.3654 0.4051 0.3486 0.0064  0.0206  -0.0139 197 ILE B C   
4419 O O   . ILE B 227 ? 0.3733 0.4140 0.3573 0.0081  0.0205  -0.0130 197 ILE B O   
4420 C CB  . ILE B 227 ? 0.3658 0.3984 0.3566 -0.0040 0.0231  -0.0120 197 ILE B CB  
4421 C CG1 . ILE B 227 ? 0.3645 0.3992 0.3605 -0.0091 0.0256  -0.0142 197 ILE B CG1 
4422 C CG2 . ILE B 227 ? 0.3655 0.3928 0.3576 -0.0047 0.0228  -0.0083 197 ILE B CG2 
4423 C CD1 . ILE B 227 ? 0.3744 0.3996 0.3702 -0.0126 0.0259  -0.0098 197 ILE B CD1 
4424 N N   . ALA B 228 ? 0.3620 0.3978 0.3382 0.0097  0.0190  -0.0128 198 ALA B N   
4425 C CA  . ALA B 228 ? 0.3650 0.3958 0.3338 0.0152  0.0170  -0.0102 198 ALA B CA  
4426 C C   . ALA B 228 ? 0.3674 0.4087 0.3356 0.0206  0.0174  -0.0139 198 ALA B C   
4427 O O   . ALA B 228 ? 0.3686 0.4078 0.3344 0.0236  0.0169  -0.0115 198 ALA B O   
4428 C CB  . ALA B 228 ? 0.3647 0.3893 0.3257 0.0180  0.0151  -0.0093 198 ALA B CB  
4429 N N   . LEU B 229 ? 0.3607 0.4141 0.3314 0.0218  0.0184  -0.0198 199 LEU B N   
4430 C CA  . LEU B 229 ? 0.3599 0.4253 0.3304 0.0271  0.0188  -0.0241 199 LEU B CA  
4431 C C   . LEU B 229 ? 0.3532 0.4228 0.3301 0.0253  0.0199  -0.0248 199 LEU B C   
4432 O O   . LEU B 229 ? 0.3543 0.4282 0.3289 0.0306  0.0196  -0.0252 199 LEU B O   
4433 C CB  . LEU B 229 ? 0.3567 0.4357 0.3294 0.0278  0.0196  -0.0305 199 LEU B CB  
4434 C CG  . LEU B 229 ? 0.3736 0.4510 0.3381 0.0325  0.0181  -0.0304 199 LEU B CG  
4435 C CD1 . LEU B 229 ? 0.3724 0.4630 0.3400 0.0316  0.0192  -0.0358 199 LEU B CD1 
4436 C CD2 . LEU B 229 ? 0.3922 0.4688 0.3477 0.0414  0.0166  -0.0296 199 LEU B CD2 
4437 N N   . ALA B 230 ? 0.3478 0.4159 0.3319 0.0185  0.0212  -0.0249 200 ALA B N   
4438 C CA  . ALA B 230 ? 0.3488 0.4203 0.3385 0.0171  0.0220  -0.0258 200 ALA B CA  
4439 C C   . ALA B 230 ? 0.3547 0.4183 0.3412 0.0193  0.0211  -0.0198 200 ALA B C   
4440 O O   . ALA B 230 ? 0.3597 0.4289 0.3468 0.0229  0.0212  -0.0206 200 ALA B O   
4441 C CB  . ALA B 230 ? 0.3454 0.4148 0.3421 0.0098  0.0235  -0.0267 200 ALA B CB  
4442 N N   . CYS B 231 ? 0.3522 0.4035 0.3349 0.0173  0.0202  -0.0140 201 CYS B N   
4443 C CA  . CYS B 231 ? 0.3574 0.4010 0.3370 0.0184  0.0193  -0.0078 201 CYS B CA  
4444 C C   . CYS B 231 ? 0.3704 0.4148 0.3432 0.0251  0.0184  -0.0066 201 CYS B C   
4445 O O   . CYS B 231 ? 0.3702 0.4148 0.3425 0.0272  0.0185  -0.0036 201 CYS B O   
4446 C CB  . CYS B 231 ? 0.3580 0.3893 0.3354 0.0141  0.0184  -0.0027 201 CYS B CB  
4447 S SG  . CYS B 231 ? 0.3509 0.3804 0.3355 0.0069  0.0197  -0.0031 201 CYS B SG  
4448 N N   . LEU B 232 ? 0.3829 0.4278 0.3500 0.0289  0.0176  -0.0087 202 LEU B N   
4449 C CA  . LEU B 232 ? 0.4010 0.4464 0.3603 0.0364  0.0169  -0.0081 202 LEU B CA  
4450 C C   . LEU B 232 ? 0.4180 0.4773 0.3801 0.0411  0.0179  -0.0123 202 LEU B C   
4451 O O   . LEU B 232 ? 0.4237 0.4832 0.3815 0.0463  0.0179  -0.0098 202 LEU B O   
4452 C CB  . LEU B 232 ? 0.3988 0.4428 0.3513 0.0400  0.0158  -0.0103 202 LEU B CB  
4453 C CG  . LEU B 232 ? 0.4199 0.4620 0.3623 0.0485  0.0149  -0.0093 202 LEU B CG  
4454 C CD1 . LEU B 232 ? 0.4310 0.4599 0.3680 0.0488  0.0142  -0.0019 202 LEU B CD1 
4455 C CD2 . LEU B 232 ? 0.4256 0.4653 0.3608 0.0520  0.0136  -0.0113 202 LEU B CD2 
4456 N N   . HIS B 233 ? 0.4184 0.4893 0.3877 0.0391  0.0190  -0.0187 203 HIS B N   
4457 C CA  . HIS B 233 ? 0.4248 0.5097 0.3975 0.0429  0.0197  -0.0237 203 HIS B CA  
4458 C C   . HIS B 233 ? 0.4206 0.5046 0.3965 0.0423  0.0202  -0.0205 203 HIS B C   
4459 O O   . HIS B 233 ? 0.4177 0.5076 0.3912 0.0485  0.0202  -0.0205 203 HIS B O   
4460 C CB  . HIS B 233 ? 0.4449 0.5412 0.4252 0.0392  0.0207  -0.0312 203 HIS B CB  
4461 C CG  . HIS B 233 ? 0.4905 0.6018 0.4748 0.0427  0.0212  -0.0373 203 HIS B CG  
4462 N ND1 . HIS B 233 ? 0.5130 0.6369 0.4945 0.0490  0.0210  -0.0425 203 HIS B ND1 
4463 C CD2 . HIS B 233 ? 0.5062 0.6219 0.4966 0.0411  0.0217  -0.0391 203 HIS B CD2 
4464 C CE1 . HIS B 233 ? 0.5164 0.6522 0.5027 0.0509  0.0214  -0.0474 203 HIS B CE1 
4465 N NE2 . HIS B 233 ? 0.5155 0.6465 0.5071 0.0463  0.0218  -0.0456 203 HIS B NE2 
4466 N N   . VAL B 234 ? 0.4158 0.4928 0.3966 0.0355  0.0205  -0.0177 204 VAL B N   
4467 C CA  . VAL B 234 ? 0.4138 0.4904 0.3976 0.0350  0.0209  -0.0144 204 VAL B CA  
4468 C C   . VAL B 234 ? 0.4218 0.4921 0.3990 0.0388  0.0203  -0.0074 204 VAL B C   
4469 O O   . VAL B 234 ? 0.4199 0.4955 0.3973 0.0426  0.0207  -0.0061 204 VAL B O   
4470 C CB  . VAL B 234 ? 0.4184 0.4890 0.4079 0.0277  0.0213  -0.0127 204 VAL B CB  
4471 C CG1 . VAL B 234 ? 0.4205 0.4912 0.4118 0.0283  0.0215  -0.0087 204 VAL B CG1 
4472 C CG2 . VAL B 234 ? 0.4128 0.4892 0.4087 0.0239  0.0222  -0.0195 204 VAL B CG2 
4473 N N   . ALA B 235 ? 0.4267 0.4859 0.3976 0.0381  0.0194  -0.0031 205 ALA B N   
4474 C CA  . ALA B 235 ? 0.4357 0.4871 0.3997 0.0409  0.0190  0.0037  205 ALA B CA  
4475 C C   . ALA B 235 ? 0.4410 0.4997 0.3998 0.0497  0.0193  0.0022  205 ALA B C   
4476 O O   . ALA B 235 ? 0.4360 0.4953 0.3928 0.0528  0.0198  0.0065  205 ALA B O   
4477 C CB  . ALA B 235 ? 0.4358 0.4732 0.3937 0.0384  0.0177  0.0074  205 ALA B CB  
4478 N N   . CYS B 236 ? 0.4439 0.5099 0.4010 0.0539  0.0192  -0.0039 206 CYS B N   
4479 C CA  . CYS B 236 ? 0.4553 0.5303 0.4073 0.0631  0.0195  -0.0064 206 CYS B CA  
4480 C C   . CYS B 236 ? 0.4626 0.5504 0.4203 0.0657  0.0205  -0.0086 206 CYS B C   
4481 O O   . CYS B 236 ? 0.4662 0.5575 0.4193 0.0725  0.0209  -0.0065 206 CYS B O   
4482 C CB  . CYS B 236 ? 0.4550 0.5380 0.4056 0.0664  0.0191  -0.0134 206 CYS B CB  
4483 S SG  . CYS B 236 ? 0.4823 0.5519 0.4240 0.0664  0.0177  -0.0112 206 CYS B SG  
4484 N N   . VAL B 237 ? 0.4637 0.5583 0.4307 0.0607  0.0208  -0.0131 207 VAL B N   
4485 C CA  . VAL B 237 ? 0.4648 0.5712 0.4373 0.0630  0.0214  -0.0160 207 VAL B CA  
4486 C C   . VAL B 237 ? 0.4977 0.5990 0.4692 0.0632  0.0218  -0.0085 207 VAL B C   
4487 O O   . VAL B 237 ? 0.5076 0.6167 0.4777 0.0695  0.0223  -0.0077 207 VAL B O   
4488 C CB  . VAL B 237 ? 0.4525 0.5646 0.4343 0.0570  0.0215  -0.0224 207 VAL B CB  
4489 C CG1 . VAL B 237 ? 0.4447 0.5675 0.4317 0.0594  0.0218  -0.0256 207 VAL B CG1 
4490 C CG2 . VAL B 237 ? 0.4489 0.5679 0.4319 0.0566  0.0214  -0.0299 207 VAL B CG2 
4491 N N   . VAL B 238 ? 0.5097 0.5990 0.4820 0.0565  0.0216  -0.0027 208 VAL B N   
4492 C CA  . VAL B 238 ? 0.5197 0.6044 0.4915 0.0554  0.0220  0.0049  208 VAL B CA  
4493 C C   . VAL B 238 ? 0.5476 0.6290 0.5110 0.0612  0.0223  0.0107  208 VAL B C   
4494 O O   . VAL B 238 ? 0.5519 0.6388 0.5149 0.0652  0.0232  0.0139  208 VAL B O   
4495 C CB  . VAL B 238 ? 0.5162 0.5892 0.4902 0.0468  0.0215  0.0092  208 VAL B CB  
4496 C CG1 . VAL B 238 ? 0.5240 0.5918 0.4963 0.0455  0.0218  0.0178  208 VAL B CG1 
4497 C CG2 . VAL B 238 ? 0.5112 0.5880 0.4933 0.0421  0.0216  0.0045  208 VAL B CG2 
4498 N N   . GLN B 239 ? 0.5660 0.6385 0.5222 0.0623  0.0218  0.0118  209 GLN B N   
4499 C CA  . GLN B 239 ? 0.5892 0.6558 0.5359 0.0678  0.0222  0.0174  209 GLN B CA  
4500 C C   . GLN B 239 ? 0.6057 0.6822 0.5475 0.0779  0.0227  0.0133  209 GLN B C   
4501 O O   . GLN B 239 ? 0.6143 0.6847 0.5467 0.0834  0.0230  0.0173  209 GLN B O   
4502 C CB  . GLN B 239 ? 0.6259 0.6757 0.5660 0.0641  0.0212  0.0214  209 GLN B CB  
4503 C CG  . GLN B 239 ? 0.6924 0.7319 0.6331 0.0575  0.0212  0.0295  209 GLN B CG  
4504 C CD  . GLN B 239 ? 0.7841 0.8084 0.7211 0.0518  0.0198  0.0318  209 GLN B CD  
4505 O OE1 . GLN B 239 ? 0.8080 0.8314 0.7474 0.0490  0.0187  0.0270  209 GLN B OE1 
4506 N NE2 . GLN B 239 ? 0.8123 0.8242 0.7433 0.0499  0.0196  0.0391  209 GLN B NE2 
4507 N N   . GLN B 240 ? 0.6097 0.7014 0.5576 0.0805  0.0227  0.0052  210 GLN B N   
4508 C CA  . GLN B 240 ? 0.6222 0.7270 0.5671 0.0900  0.0231  -0.0001 210 GLN B CA  
4509 C C   . GLN B 240 ? 0.6385 0.7381 0.5733 0.0956  0.0227  -0.0002 210 GLN B C   
4510 O O   . GLN B 240 ? 0.6474 0.7497 0.5745 0.1045  0.0234  0.0014  210 GLN B O   
4511 C CB  . GLN B 240 ? 0.6429 0.7558 0.5872 0.0961  0.0243  0.0030  210 GLN B CB  
4512 C CG  . GLN B 240 ? 0.6888 0.8084 0.6431 0.0914  0.0244  0.0019  210 GLN B CG  
4513 C CD  . GLN B 240 ? 0.7520 0.8799 0.7061 0.0972  0.0254  0.0053  210 GLN B CD  
4514 O OE1 . GLN B 240 ? 0.7642 0.8925 0.7106 0.1046  0.0264  0.0094  210 GLN B OE1 
4515 N NE2 . GLN B 240 ? 0.7634 0.8980 0.7254 0.0943  0.0253  0.0038  210 GLN B NE2 
4516 N N   . LYS B 241 ? 0.6387 0.7306 0.5731 0.0907  0.0216  -0.0020 211 LYS B N   
4517 C CA  . LYS B 241 ? 0.6479 0.7342 0.5729 0.0954  0.0209  -0.0028 211 LYS B CA  
4518 C C   . LYS B 241 ? 0.6505 0.7519 0.5791 0.0977  0.0205  -0.0124 211 LYS B C   
4519 O O   . LYS B 241 ? 0.6577 0.7631 0.5951 0.0906  0.0202  -0.0169 211 LYS B O   
4520 C CB  . LYS B 241 ? 0.6766 0.7448 0.5988 0.0883  0.0198  0.0017  211 LYS B CB  
4521 C CG  . LYS B 241 ? 0.7492 0.8107 0.6614 0.0930  0.0188  0.0005  211 LYS B CG  
4522 C CD  . LYS B 241 ? 0.8343 0.8893 0.7338 0.1024  0.0192  0.0052  211 LYS B CD  
4523 C CE  . LYS B 241 ? 0.8959 0.9445 0.7842 0.1087  0.0180  0.0036  211 LYS B CE  
4524 N NZ  . LYS B 241 ? 0.9332 0.9690 0.8078 0.1161  0.0184  0.0100  211 LYS B NZ  
4525 N N   . ASP B 242 ? 0.6457 0.7561 0.5677 0.1078  0.0207  -0.0157 212 ASP B N   
4526 C CA  . ASP B 242 ? 0.6361 0.7629 0.5612 0.1105  0.0203  -0.0251 212 ASP B CA  
4527 C C   . ASP B 242 ? 0.6278 0.7471 0.5492 0.1081  0.0192  -0.0261 212 ASP B C   
4528 O O   . ASP B 242 ? 0.6411 0.7498 0.5512 0.1134  0.0186  -0.0223 212 ASP B O   
4529 C CB  . ASP B 242 ? 0.6629 0.8024 0.5811 0.1230  0.0207  -0.0279 212 ASP B CB  
4530 C CG  . ASP B 242 ? 0.7320 0.8928 0.6550 0.1261  0.0204  -0.0384 212 ASP B CG  
4531 O OD1 . ASP B 242 ? 0.7343 0.8993 0.6656 0.1181  0.0199  -0.0434 212 ASP B OD1 
4532 O OD2 . ASP B 242 ? 0.7710 0.9447 0.6893 0.1364  0.0207  -0.0416 212 ASP B OD2 
4533 N N   . ALA B 243 ? 0.6095 0.7338 0.5398 0.1002  0.0189  -0.0309 213 ALA B N   
4534 C CA  . ALA B 243 ? 0.6080 0.7275 0.5358 0.0977  0.0179  -0.0324 213 ALA B CA  
4535 C C   . ALA B 243 ? 0.5956 0.7326 0.5316 0.0950  0.0181  -0.0413 213 ALA B C   
4536 O O   . ALA B 243 ? 0.5905 0.7245 0.5287 0.0894  0.0177  -0.0425 213 ALA B O   
4537 C CB  . ALA B 243 ? 0.6137 0.7153 0.5432 0.0885  0.0174  -0.0265 213 ALA B CB  
4538 N N   . ARG B 244 ? 0.5867 0.7423 0.5269 0.0991  0.0186  -0.0477 214 ARG B N   
4539 C CA  . ARG B 244 ? 0.5797 0.7535 0.5281 0.0963  0.0189  -0.0567 214 ARG B CA  
4540 C C   . ARG B 244 ? 0.5694 0.7491 0.5122 0.1003  0.0182  -0.0600 214 ARG B C   
4541 O O   . ARG B 244 ? 0.5663 0.7519 0.5153 0.0938  0.0184  -0.0640 214 ARG B O   
4542 C CB  . ARG B 244 ? 0.5958 0.7882 0.5487 0.1008  0.0193  -0.0629 214 ARG B CB  
4543 C CG  . ARG B 244 ? 0.6573 0.8465 0.6177 0.0959  0.0198  -0.0612 214 ARG B CG  
4544 C CD  . ARG B 244 ? 0.7141 0.9184 0.6754 0.1033  0.0200  -0.0653 214 ARG B CD  
4545 N NE  . ARG B 244 ? 0.7737 0.9786 0.7233 0.1155  0.0199  -0.0622 214 ARG B NE  
4546 C CZ  . ARG B 244 ? 0.8042 1.0248 0.7518 0.1249  0.0200  -0.0664 214 ARG B CZ  
4547 N NH1 . ARG B 244 ? 0.8020 1.0212 0.7378 0.1361  0.0201  -0.0630 214 ARG B NH1 
4548 N NH2 . ARG B 244 ? 0.7984 1.0359 0.7553 0.1234  0.0199  -0.0742 214 ARG B NH2 
4549 N N   . GLN B 245 ? 0.5632 0.7411 0.4938 0.1112  0.0176  -0.0580 215 GLN B N   
4550 C CA  . GLN B 245 ? 0.5592 0.7428 0.4826 0.1169  0.0168  -0.0609 215 GLN B CA  
4551 C C   . GLN B 245 ? 0.5453 0.7131 0.4664 0.1111  0.0161  -0.0567 215 GLN B C   
4552 O O   . GLN B 245 ? 0.5468 0.7229 0.4697 0.1092  0.0158  -0.0609 215 GLN B O   
4553 C CB  . GLN B 245 ? 0.6039 0.7871 0.5133 0.1309  0.0163  -0.0591 215 GLN B CB  
4554 C CG  . GLN B 245 ? 0.6803 0.8733 0.5819 0.1387  0.0155  -0.0634 215 GLN B CG  
4555 C CD  . GLN B 245 ? 0.7817 0.9653 0.6667 0.1517  0.0148  -0.0592 215 GLN B CD  
4556 O OE1 . GLN B 245 ? 0.8019 0.9899 0.6821 0.1603  0.0154  -0.0588 215 GLN B OE1 
4557 N NE2 . GLN B 245 ? 0.8105 0.9805 0.6858 0.1539  0.0135  -0.0561 215 GLN B NE2 
4558 N N   . TRP B 246 ? 0.5317 0.6776 0.4493 0.1078  0.0157  -0.0487 216 TRP B N   
4559 C CA  . TRP B 246 ? 0.5235 0.6541 0.4393 0.1020  0.0148  -0.0449 216 TRP B CA  
4560 C C   . TRP B 246 ? 0.5149 0.6519 0.4435 0.0908  0.0156  -0.0483 216 TRP B C   
4561 O O   . TRP B 246 ? 0.5125 0.6513 0.4411 0.0887  0.0152  -0.0500 216 TRP B O   
4562 C CB  . TRP B 246 ? 0.5211 0.6283 0.4317 0.0998  0.0143  -0.0360 216 TRP B CB  
4563 C CG  . TRP B 246 ? 0.5241 0.6155 0.4317 0.0950  0.0130  -0.0323 216 TRP B CG  
4564 C CD1 . TRP B 246 ? 0.5387 0.6185 0.4340 0.1007  0.0113  -0.0299 216 TRP B CD1 
4565 C CD2 . TRP B 246 ? 0.5210 0.6065 0.4374 0.0838  0.0132  -0.0309 216 TRP B CD2 
4566 N NE1 . TRP B 246 ? 0.5442 0.6121 0.4407 0.0937  0.0103  -0.0274 216 TRP B NE1 
4567 C CE2 . TRP B 246 ? 0.5370 0.6087 0.4464 0.0835  0.0116  -0.0279 216 TRP B CE2 
4568 C CE3 . TRP B 246 ? 0.5186 0.6095 0.4479 0.0747  0.0146  -0.0322 216 TRP B CE3 
4569 C CZ2 . TRP B 246 ? 0.5422 0.6060 0.4572 0.0744  0.0114  -0.0260 216 TRP B CZ2 
4570 C CZ3 . TRP B 246 ? 0.5332 0.6153 0.4673 0.0659  0.0145  -0.0299 216 TRP B CZ3 
4571 C CH2 . TRP B 246 ? 0.5379 0.6073 0.4652 0.0659  0.0130  -0.0269 216 TRP B CH2 
4572 N N   . PHE B 247 ? 0.5087 0.6501 0.4479 0.0843  0.0169  -0.0494 217 PHE B N   
4573 C CA  . PHE B 247 ? 0.5108 0.6573 0.4619 0.0737  0.0179  -0.0526 217 PHE B CA  
4574 C C   . PHE B 247 ? 0.5243 0.6916 0.4803 0.0735  0.0185  -0.0609 217 PHE B C   
4575 O O   . PHE B 247 ? 0.5213 0.6903 0.4830 0.0662  0.0191  -0.0625 217 PHE B O   
4576 C CB  . PHE B 247 ? 0.4946 0.6396 0.4544 0.0678  0.0189  -0.0518 217 PHE B CB  
4577 C CG  . PHE B 247 ? 0.4910 0.6164 0.4508 0.0620  0.0187  -0.0442 217 PHE B CG  
4578 C CD1 . PHE B 247 ? 0.4915 0.6098 0.4562 0.0534  0.0191  -0.0429 217 PHE B CD1 
4579 C CD2 . PHE B 247 ? 0.4938 0.6088 0.4487 0.0654  0.0183  -0.0382 217 PHE B CD2 
4580 C CE1 . PHE B 247 ? 0.4980 0.5998 0.4624 0.0486  0.0188  -0.0362 217 PHE B CE1 
4581 C CE2 . PHE B 247 ? 0.5015 0.6002 0.4565 0.0599  0.0180  -0.0315 217 PHE B CE2 
4582 C CZ  . PHE B 247 ? 0.4981 0.5906 0.4579 0.0517  0.0182  -0.0307 217 PHE B CZ  
4583 N N   . ALA B 248 ? 0.5336 0.7171 0.4873 0.0816  0.0184  -0.0661 218 ALA B N   
4584 C CA  . ALA B 248 ? 0.5379 0.7434 0.4960 0.0820  0.0189  -0.0744 218 ALA B CA  
4585 C C   . ALA B 248 ? 0.5548 0.7618 0.5058 0.0857  0.0181  -0.0744 218 ALA B C   
4586 O O   . ALA B 248 ? 0.5554 0.7751 0.5121 0.0811  0.0188  -0.0791 218 ALA B O   
4587 C CB  . ALA B 248 ? 0.5330 0.7556 0.4897 0.0907  0.0187  -0.0797 218 ALA B CB  
4588 N N   . GLU B 249 ? 0.5662 0.7596 0.5046 0.0937  0.0167  -0.0691 219 GLU B N   
4589 C CA  . GLU B 249 ? 0.5834 0.7765 0.5137 0.0981  0.0157  -0.0689 219 GLU B CA  
4590 C C   . GLU B 249 ? 0.5897 0.7727 0.5240 0.0888  0.0158  -0.0661 219 GLU B C   
4591 O O   . GLU B 249 ? 0.5912 0.7754 0.5200 0.0918  0.0150  -0.0664 219 GLU B O   
4592 C CB  . GLU B 249 ? 0.6361 0.8159 0.5508 0.1096  0.0140  -0.0643 219 GLU B CB  
4593 C CG  . GLU B 249 ? 0.7058 0.8999 0.6139 0.1216  0.0138  -0.0682 219 GLU B CG  
4594 C CD  . GLU B 249 ? 0.8044 0.9827 0.6976 0.1323  0.0126  -0.0626 219 GLU B CD  
4595 O OE1 . GLU B 249 ? 0.8308 0.9863 0.7182 0.1302  0.0117  -0.0559 219 GLU B OE1 
4596 O OE2 . GLU B 249 ? 0.8316 1.0202 0.7189 0.1426  0.0127  -0.0651 219 GLU B OE2 
4597 N N   . LEU B 250 ? 0.5909 0.7646 0.5343 0.0783  0.0168  -0.0634 220 LEU B N   
4598 C CA  . LEU B 250 ? 0.6022 0.7662 0.5498 0.0694  0.0172  -0.0604 220 LEU B CA  
4599 C C   . LEU B 250 ? 0.6022 0.7837 0.5591 0.0631  0.0189  -0.0662 220 LEU B C   
4600 O O   . LEU B 250 ? 0.5972 0.7929 0.5624 0.0598  0.0202  -0.0714 220 LEU B O   
4601 C CB  . LEU B 250 ? 0.6045 0.7540 0.5584 0.0611  0.0180  -0.0559 220 LEU B CB  
4602 C CG  . LEU B 250 ? 0.6237 0.7528 0.5700 0.0637  0.0166  -0.0487 220 LEU B CG  
4603 C CD1 . LEU B 250 ? 0.6288 0.7491 0.5827 0.0560  0.0175  -0.0456 220 LEU B CD1 
4604 C CD2 . LEU B 250 ? 0.6348 0.7504 0.5738 0.0643  0.0151  -0.0446 220 LEU B CD2 
4605 N N   . SER B 251 ? 0.6074 0.7873 0.5632 0.0606  0.0189  -0.0650 221 SER B N   
4606 C CA  . SER B 251 ? 0.6159 0.8110 0.5807 0.0534  0.0208  -0.0694 221 SER B CA  
4607 C C   . SER B 251 ? 0.6246 0.8078 0.5980 0.0418  0.0225  -0.0661 221 SER B C   
4608 O O   . SER B 251 ? 0.6265 0.8026 0.5999 0.0378  0.0228  -0.0628 221 SER B O   
4609 C CB  . SER B 251 ? 0.6401 0.8414 0.5991 0.0575  0.0202  -0.0698 221 SER B CB  
4610 O OG  . SER B 251 ? 0.6879 0.8694 0.6399 0.0583  0.0187  -0.0635 221 SER B OG  
4611 N N   . VAL B 252 ? 0.6255 0.8056 0.6053 0.0374  0.0233  -0.0665 222 VAL B N   
4612 C CA  . VAL B 252 ? 0.6308 0.7992 0.6180 0.0275  0.0248  -0.0634 222 VAL B CA  
4613 C C   . VAL B 252 ? 0.6237 0.8029 0.6214 0.0209  0.0266  -0.0688 222 VAL B C   
4614 O O   . VAL B 252 ? 0.6188 0.8113 0.6175 0.0249  0.0263  -0.0740 222 VAL B O   
4615 C CB  . VAL B 252 ? 0.6473 0.7953 0.6303 0.0287  0.0235  -0.0568 222 VAL B CB  
4616 C CG1 . VAL B 252 ? 0.6639 0.7998 0.6363 0.0346  0.0214  -0.0517 222 VAL B CG1 
4617 C CG2 . VAL B 252 ? 0.6508 0.8008 0.6334 0.0331  0.0228  -0.0581 222 VAL B CG2 
4618 N N   . ASP B 253 ? 0.6200 0.7928 0.6251 0.0111  0.0286  -0.0676 223 ASP B N   
4619 C CA  . ASP B 253 ? 0.6124 0.7916 0.6269 0.0040  0.0303  -0.0724 223 ASP B CA  
4620 C C   . ASP B 253 ? 0.6105 0.7796 0.6247 0.0059  0.0293  -0.0704 223 ASP B C   
4621 O O   . ASP B 253 ? 0.6200 0.7728 0.6341 0.0026  0.0295  -0.0650 223 ASP B O   
4622 C CB  . ASP B 253 ? 0.6330 0.8059 0.6538 -0.0066 0.0328  -0.0707 223 ASP B CB  
4623 C CG  . ASP B 253 ? 0.6815 0.8612 0.7119 -0.0149 0.0348  -0.0762 223 ASP B CG  
4624 O OD1 . ASP B 253 ? 0.6818 0.8704 0.7146 -0.0128 0.0340  -0.0814 223 ASP B OD1 
4625 O OD2 . ASP B 253 ? 0.7094 0.8851 0.7446 -0.0236 0.0371  -0.0753 223 ASP B OD2 
4626 N N   . MET B 254 ? 0.5970 0.7763 0.6106 0.0118  0.0282  -0.0745 224 MET B N   
4627 C CA  . MET B 254 ? 0.5942 0.7659 0.6072 0.0145  0.0273  -0.0728 224 MET B CA  
4628 C C   . MET B 254 ? 0.5838 0.7514 0.6050 0.0065  0.0286  -0.0744 224 MET B C   
4629 O O   . MET B 254 ? 0.5879 0.7472 0.6085 0.0081  0.0280  -0.0719 224 MET B O   
4630 C CB  . MET B 254 ? 0.5998 0.7844 0.6096 0.0237  0.0259  -0.0768 224 MET B CB  
4631 C CG  . MET B 254 ? 0.6413 0.8233 0.6404 0.0333  0.0243  -0.0730 224 MET B CG  
4632 S SD  . MET B 254 ? 0.7215 0.8799 0.7132 0.0358  0.0232  -0.0629 224 MET B SD  
4633 C CE  . MET B 254 ? 0.7081 0.8664 0.7042 0.0360  0.0232  -0.0635 224 MET B CE  
4634 N N   . GLU B 255 ? 0.5694 0.7424 0.5976 -0.0019 0.0305  -0.0786 225 GLU B N   
4635 C CA  . GLU B 255 ? 0.5648 0.7314 0.5998 -0.0096 0.0318  -0.0800 225 GLU B CA  
4636 C C   . GLU B 255 ? 0.5477 0.6944 0.5806 -0.0128 0.0323  -0.0721 225 GLU B C   
4637 O O   . GLU B 255 ? 0.5537 0.6907 0.5874 -0.0135 0.0321  -0.0702 225 GLU B O   
4638 C CB  . GLU B 255 ? 0.6013 0.7783 0.6441 -0.0181 0.0337  -0.0867 225 GLU B CB  
4639 C CG  . GLU B 255 ? 0.6907 0.8597 0.7396 -0.0258 0.0350  -0.0886 225 GLU B CG  
4640 C CD  . GLU B 255 ? 0.8082 0.9731 0.8570 -0.0220 0.0335  -0.0896 225 GLU B CD  
4641 O OE1 . GLU B 255 ? 0.8412 1.0187 0.8895 -0.0156 0.0319  -0.0940 225 GLU B OE1 
4642 O OE2 . GLU B 255 ? 0.8327 0.9825 0.8818 -0.0251 0.0340  -0.0860 225 GLU B OE2 
4643 N N   . LYS B 256 ? 0.5277 0.6689 0.5572 -0.0137 0.0328  -0.0676 226 LYS B N   
4644 C CA  . LYS B 256 ? 0.5185 0.6420 0.5455 -0.0159 0.0331  -0.0601 226 LYS B CA  
4645 C C   . LYS B 256 ? 0.4969 0.6112 0.5181 -0.0093 0.0310  -0.0549 226 LYS B C   
4646 O O   . LYS B 256 ? 0.5045 0.6061 0.5255 -0.0113 0.0311  -0.0504 226 LYS B O   
4647 C CB  . LYS B 256 ? 0.5440 0.6653 0.5688 -0.0180 0.0340  -0.0571 226 LYS B CB  
4648 C CG  . LYS B 256 ? 0.6029 0.7298 0.6341 -0.0264 0.0367  -0.0606 226 LYS B CG  
4649 C CD  . LYS B 256 ? 0.6800 0.8058 0.7094 -0.0285 0.0379  -0.0574 226 LYS B CD  
4650 C CE  . LYS B 256 ? 0.7389 0.8708 0.7751 -0.0374 0.0410  -0.0608 226 LYS B CE  
4651 N NZ  . LYS B 256 ? 0.7743 0.8969 0.8153 -0.0438 0.0425  -0.0615 226 LYS B NZ  
4652 N N   . ILE B 257 ? 0.4717 0.5928 0.4881 -0.0015 0.0292  -0.0556 227 ILE B N   
4653 C CA  . ILE B 257 ? 0.4639 0.5774 0.4746 0.0046  0.0274  -0.0508 227 ILE B CA  
4654 C C   . ILE B 257 ? 0.4608 0.5736 0.4751 0.0044  0.0274  -0.0519 227 ILE B C   
4655 O O   . ILE B 257 ? 0.4701 0.5720 0.4827 0.0049  0.0269  -0.0466 227 ILE B O   
4656 C CB  . ILE B 257 ? 0.4631 0.5842 0.4671 0.0133  0.0257  -0.0517 227 ILE B CB  
4657 C CG1 . ILE B 257 ? 0.4698 0.5907 0.4694 0.0140  0.0255  -0.0506 227 ILE B CG1 
4658 C CG2 . ILE B 257 ? 0.4663 0.5796 0.4642 0.0195  0.0241  -0.0467 227 ILE B CG2 
4659 C CD1 . ILE B 257 ? 0.4888 0.5937 0.4850 0.0116  0.0251  -0.0438 227 ILE B CD1 
4660 N N   . LEU B 258 ? 0.4467 0.5717 0.4663 0.0035  0.0280  -0.0591 228 LEU B N   
4661 C CA  . LEU B 258 ? 0.4454 0.5711 0.4687 0.0036  0.0278  -0.0611 228 LEU B CA  
4662 C C   . LEU B 258 ? 0.4353 0.5490 0.4623 -0.0035 0.0291  -0.0590 228 LEU B C   
4663 O O   . LEU B 258 ? 0.4447 0.5526 0.4717 -0.0022 0.0286  -0.0568 228 LEU B O   
4664 C CB  . LEU B 258 ? 0.4502 0.5923 0.4781 0.0042  0.0279  -0.0701 228 LEU B CB  
4665 C CG  . LEU B 258 ? 0.4687 0.6239 0.4926 0.0130  0.0266  -0.0726 228 LEU B CG  
4666 C CD1 . LEU B 258 ? 0.4725 0.6454 0.5018 0.0123  0.0267  -0.0821 228 LEU B CD1 
4667 C CD2 . LEU B 258 ? 0.4808 0.6324 0.5006 0.0200  0.0253  -0.0688 228 LEU B CD2 
4668 N N   . GLU B 259 ? 0.4142 0.5239 0.4435 -0.0104 0.0307  -0.0590 229 GLU B N   
4669 C CA  . GLU B 259 ? 0.4066 0.5036 0.4382 -0.0165 0.0321  -0.0562 229 GLU B CA  
4670 C C   . GLU B 259 ? 0.3967 0.4808 0.4233 -0.0139 0.0313  -0.0480 229 GLU B C   
4671 O O   . GLU B 259 ? 0.4008 0.4769 0.4280 -0.0148 0.0314  -0.0457 229 GLU B O   
4672 C CB  . GLU B 259 ? 0.4307 0.5257 0.4645 -0.0236 0.0343  -0.0567 229 GLU B CB  
4673 C CG  . GLU B 259 ? 0.4797 0.5862 0.5194 -0.0284 0.0356  -0.0646 229 GLU B CG  
4674 C CD  . GLU B 259 ? 0.5696 0.6761 0.6115 -0.0354 0.0380  -0.0647 229 GLU B CD  
4675 O OE1 . GLU B 259 ? 0.5709 0.6682 0.6094 -0.0360 0.0385  -0.0585 229 GLU B OE1 
4676 O OE2 . GLU B 259 ? 0.5990 0.7154 0.6460 -0.0403 0.0393  -0.0710 229 GLU B OE2 
4677 N N   . ILE B 260 ? 0.3808 0.4636 0.4024 -0.0105 0.0302  -0.0438 230 ILE B N   
4678 C CA  . ILE B 260 ? 0.3777 0.4492 0.3948 -0.0086 0.0292  -0.0364 230 ILE B CA  
4679 C C   . ILE B 260 ? 0.3772 0.4494 0.3926 -0.0034 0.0278  -0.0348 230 ILE B C   
4680 O O   . ILE B 260 ? 0.3828 0.4470 0.3979 -0.0040 0.0276  -0.0304 230 ILE B O   
4681 C CB  . ILE B 260 ? 0.3799 0.4491 0.3917 -0.0066 0.0283  -0.0331 230 ILE B CB  
4682 C CG1 . ILE B 260 ? 0.3825 0.4528 0.3960 -0.0114 0.0299  -0.0348 230 ILE B CG1 
4683 C CG2 . ILE B 260 ? 0.3906 0.4480 0.3982 -0.0056 0.0271  -0.0258 230 ILE B CG2 
4684 C CD1 . ILE B 260 ? 0.3920 0.4634 0.4003 -0.0083 0.0288  -0.0332 230 ILE B CD1 
4685 N N   . ILE B 261 ? 0.3714 0.4542 0.3862 0.0017  0.0269  -0.0385 231 ILE B N   
4686 C CA  . ILE B 261 ? 0.3811 0.4661 0.3943 0.0071  0.0258  -0.0370 231 ILE B CA  
4687 C C   . ILE B 261 ? 0.3942 0.4778 0.4118 0.0051  0.0263  -0.0383 231 ILE B C   
4688 O O   . ILE B 261 ? 0.4067 0.4852 0.4227 0.0070  0.0258  -0.0334 231 ILE B O   
4689 C CB  . ILE B 261 ? 0.3813 0.4792 0.3929 0.0134  0.0250  -0.0414 231 ILE B CB  
4690 C CG1 . ILE B 261 ? 0.4015 0.4978 0.4063 0.0174  0.0241  -0.0384 231 ILE B CG1 
4691 C CG2 . ILE B 261 ? 0.3791 0.4817 0.3905 0.0188  0.0243  -0.0415 231 ILE B CG2 
4692 C CD1 . ILE B 261 ? 0.4172 0.5272 0.4203 0.0228  0.0238  -0.0440 231 ILE B CD1 
4693 N N   . ARG B 262 ? 0.3883 0.4756 0.4111 0.0009  0.0275  -0.0444 232 ARG B N   
4694 C CA  . ARG B 262 ? 0.3887 0.4734 0.4150 -0.0010 0.0279  -0.0464 232 ARG B CA  
4695 C C   . ARG B 262 ? 0.3780 0.4492 0.4030 -0.0040 0.0284  -0.0402 232 ARG B C   
4696 O O   . ARG B 262 ? 0.3799 0.4483 0.4050 -0.0023 0.0280  -0.0385 232 ARG B O   
4697 C CB  . ARG B 262 ? 0.4148 0.5052 0.4464 -0.0055 0.0289  -0.0547 232 ARG B CB  
4698 C CG  . ARG B 262 ? 0.4662 0.5723 0.4993 -0.0016 0.0281  -0.0615 232 ARG B CG  
4699 C CD  . ARG B 262 ? 0.5202 0.6333 0.5591 -0.0062 0.0288  -0.0703 232 ARG B CD  
4700 N NE  . ARG B 262 ? 0.5788 0.6925 0.6199 -0.0128 0.0304  -0.0722 232 ARG B NE  
4701 C CZ  . ARG B 262 ? 0.6099 0.7368 0.6527 -0.0128 0.0305  -0.0773 232 ARG B CZ  
4702 N NH1 . ARG B 262 ? 0.6036 0.7441 0.6458 -0.0062 0.0290  -0.0812 232 ARG B NH1 
4703 N NH2 . ARG B 262 ? 0.6031 0.7306 0.6480 -0.0192 0.0321  -0.0785 232 ARG B NH2 
4704 N N   . VAL B 263 ? 0.3662 0.4301 0.3899 -0.0078 0.0292  -0.0366 233 VAL B N   
4705 C CA  . VAL B 263 ? 0.3660 0.4180 0.3880 -0.0101 0.0297  -0.0305 233 VAL B CA  
4706 C C   . VAL B 263 ? 0.3638 0.4140 0.3821 -0.0055 0.0281  -0.0243 233 VAL B C   
4707 O O   . VAL B 263 ? 0.3651 0.4108 0.3832 -0.0051 0.0280  -0.0211 233 VAL B O   
4708 C CB  . VAL B 263 ? 0.3689 0.4143 0.3900 -0.0148 0.0309  -0.0283 233 VAL B CB  
4709 C CG1 . VAL B 263 ? 0.3810 0.4154 0.4001 -0.0161 0.0311  -0.0220 233 VAL B CG1 
4710 C CG2 . VAL B 263 ? 0.3660 0.4128 0.3911 -0.0201 0.0329  -0.0338 233 VAL B CG2 
4711 N N   . ILE B 264 ? 0.3591 0.4132 0.3742 -0.0020 0.0269  -0.0227 234 ILE B N   
4712 C CA  . ILE B 264 ? 0.3713 0.4237 0.3829 0.0017  0.0255  -0.0167 234 ILE B CA  
4713 C C   . ILE B 264 ? 0.3878 0.4459 0.4007 0.0057  0.0251  -0.0173 234 ILE B C   
4714 O O   . ILE B 264 ? 0.3898 0.4445 0.4020 0.0062  0.0248  -0.0125 234 ILE B O   
4715 C CB  . ILE B 264 ? 0.3686 0.4224 0.3757 0.0047  0.0244  -0.0149 234 ILE B CB  
4716 C CG1 . ILE B 264 ? 0.3709 0.4187 0.3761 0.0013  0.0245  -0.0140 234 ILE B CG1 
4717 C CG2 . ILE B 264 ? 0.3701 0.4210 0.3734 0.0077  0.0232  -0.0085 234 ILE B CG2 
4718 C CD1 . ILE B 264 ? 0.3751 0.4247 0.3754 0.0048  0.0234  -0.0139 234 ILE B CD1 
4719 N N   . LEU B 265 ? 0.3974 0.4650 0.4125 0.0084  0.0251  -0.0235 235 LEU B N   
4720 C CA  . LEU B 265 ? 0.4142 0.4883 0.4305 0.0128  0.0247  -0.0248 235 LEU B CA  
4721 C C   . LEU B 265 ? 0.4275 0.4966 0.4462 0.0105  0.0252  -0.0247 235 LEU B C   
4722 O O   . LEU B 265 ? 0.4343 0.5045 0.4524 0.0137  0.0246  -0.0216 235 LEU B O   
4723 C CB  . LEU B 265 ? 0.4144 0.5000 0.4328 0.0158  0.0245  -0.0325 235 LEU B CB  
4724 C CG  . LEU B 265 ? 0.4344 0.5264 0.4497 0.0197  0.0240  -0.0330 235 LEU B CG  
4725 C CD1 . LEU B 265 ? 0.4367 0.5418 0.4546 0.0228  0.0239  -0.0413 235 LEU B CD1 
4726 C CD2 . LEU B 265 ? 0.4434 0.5352 0.4541 0.0249  0.0233  -0.0265 235 LEU B CD2 
4727 N N   . LYS B 266 ? 0.4278 0.4911 0.4487 0.0052  0.0263  -0.0277 236 LYS B N   
4728 C CA  . LYS B 266 ? 0.4325 0.4890 0.4545 0.0031  0.0269  -0.0277 236 LYS B CA  
4729 C C   . LYS B 266 ? 0.4262 0.4753 0.4455 0.0029  0.0268  -0.0198 236 LYS B C   
4730 O O   . LYS B 266 ? 0.4437 0.4912 0.4626 0.0048  0.0267  -0.0182 236 LYS B O   
4731 C CB  . LYS B 266 ? 0.4660 0.5168 0.4903 -0.0029 0.0285  -0.0321 236 LYS B CB  
4732 C CG  . LYS B 266 ? 0.5462 0.5887 0.5707 -0.0047 0.0294  -0.0326 236 LYS B CG  
4733 C CD  . LYS B 266 ? 0.6370 0.6726 0.6632 -0.0111 0.0313  -0.0363 236 LYS B CD  
4734 C CE  . LYS B 266 ? 0.7136 0.7403 0.7392 -0.0119 0.0320  -0.0376 236 LYS B CE  
4735 N NZ  . LYS B 266 ? 0.7593 0.7821 0.7874 -0.0176 0.0337  -0.0438 236 LYS B NZ  
4736 N N   . LEU B 267 ? 0.4039 0.4492 0.4211 0.0010  0.0267  -0.0152 237 LEU B N   
4737 C CA  . LEU B 267 ? 0.3927 0.4322 0.4075 0.0005  0.0264  -0.0080 237 LEU B CA  
4738 C C   . LEU B 267 ? 0.3696 0.4149 0.3834 0.0051  0.0252  -0.0042 237 LEU B C   
4739 O O   . LEU B 267 ? 0.3680 0.4113 0.3811 0.0055  0.0251  -0.0001 237 LEU B O   
4740 C CB  . LEU B 267 ? 0.4006 0.4354 0.4131 -0.0023 0.0261  -0.0045 237 LEU B CB  
4741 C CG  . LEU B 267 ? 0.4235 0.4551 0.4333 -0.0022 0.0251  0.0029  237 LEU B CG  
4742 C CD1 . LEU B 267 ? 0.4264 0.4520 0.4363 -0.0043 0.0257  0.0060  237 LEU B CD1 
4743 C CD2 . LEU B 267 ? 0.4384 0.4676 0.4456 -0.0032 0.0242  0.0050  237 LEU B CD2 
4744 N N   . TYR B 268 ? 0.3608 0.4138 0.3742 0.0088  0.0245  -0.0054 238 TYR B N   
4745 C CA  . TYR B 268 ? 0.3600 0.4191 0.3722 0.0132  0.0237  -0.0013 238 TYR B CA  
4746 C C   . TYR B 268 ? 0.3649 0.4285 0.3788 0.0165  0.0237  -0.0033 238 TYR B C   
4747 O O   . TYR B 268 ? 0.3719 0.4381 0.3850 0.0187  0.0234  0.0016  238 TYR B O   
4748 C CB  . TYR B 268 ? 0.3475 0.4130 0.3580 0.0169  0.0232  -0.0018 238 TYR B CB  
4749 C CG  . TYR B 268 ? 0.3503 0.4099 0.3576 0.0146  0.0229  0.0021  238 TYR B CG  
4750 C CD1 . TYR B 268 ? 0.3663 0.4187 0.3719 0.0112  0.0225  0.0084  238 TYR B CD1 
4751 C CD2 . TYR B 268 ? 0.3482 0.4092 0.3536 0.0158  0.0227  -0.0009 238 TYR B CD2 
4752 C CE1 . TYR B 268 ? 0.3773 0.4232 0.3796 0.0089  0.0219  0.0114  238 TYR B CE1 
4753 C CE2 . TYR B 268 ? 0.3635 0.4182 0.3650 0.0142  0.0222  0.0024  238 TYR B CE2 
4754 C CZ  . TYR B 268 ? 0.3867 0.4333 0.3868 0.0106  0.0217  0.0084  238 TYR B CZ  
4755 O OH  . TYR B 268 ? 0.4093 0.4488 0.4054 0.0088  0.0210  0.0110  238 TYR B OH  
4756 N N   . GLU B 269 ? 0.3606 0.4252 0.3768 0.0166  0.0241  -0.0104 239 GLU B N   
4757 C CA  . GLU B 269 ? 0.3685 0.4358 0.3858 0.0197  0.0239  -0.0133 239 GLU B CA  
4758 C C   . GLU B 269 ? 0.3788 0.4377 0.3951 0.0175  0.0244  -0.0102 239 GLU B C   
4759 O O   . GLU B 269 ? 0.3800 0.4417 0.3955 0.0211  0.0240  -0.0079 239 GLU B O   
4760 C CB  . GLU B 269 ? 0.3950 0.4646 0.4148 0.0195  0.0241  -0.0223 239 GLU B CB  
4761 C CG  . GLU B 269 ? 0.4486 0.5288 0.4692 0.0230  0.0235  -0.0257 239 GLU B CG  
4762 C CD  . GLU B 269 ? 0.5386 0.6281 0.5579 0.0299  0.0226  -0.0227 239 GLU B CD  
4763 O OE1 . GLU B 269 ? 0.5517 0.6433 0.5711 0.0332  0.0221  -0.0231 239 GLU B OE1 
4764 O OE2 . GLU B 269 ? 0.5502 0.6443 0.5678 0.0321  0.0224  -0.0194 239 GLU B OE2 
4765 N N   . GLN B 270 ? 0.3791 0.4286 0.3952 0.0120  0.0254  -0.0098 240 GLN B N   
4766 C CA  . GLN B 270 ? 0.3953 0.4366 0.4098 0.0103  0.0260  -0.0065 240 GLN B CA  
4767 C C   . GLN B 270 ? 0.3908 0.4345 0.4035 0.0116  0.0253  0.0013  240 GLN B C   
4768 O O   . GLN B 270 ? 0.3995 0.4433 0.4110 0.0139  0.0252  0.0037  240 GLN B O   
4769 C CB  . GLN B 270 ? 0.4397 0.4713 0.4541 0.0045  0.0274  -0.0070 240 GLN B CB  
4770 C CG  . GLN B 270 ? 0.5214 0.5444 0.5334 0.0031  0.0282  -0.0031 240 GLN B CG  
4771 C CD  . GLN B 270 ? 0.6096 0.6282 0.6205 0.0053  0.0288  -0.0060 240 GLN B CD  
4772 O OE1 . GLN B 270 ? 0.6403 0.6502 0.6508 0.0022  0.0303  -0.0094 240 GLN B OE1 
4773 N NE2 . GLN B 270 ? 0.6139 0.6379 0.6237 0.0106  0.0277  -0.0047 240 GLN B NE2 
4774 N N   . TRP B 271 ? 0.3832 0.4290 0.3956 0.0102  0.0248  0.0050  241 TRP B N   
4775 C CA  . TRP B 271 ? 0.3733 0.4213 0.3844 0.0102  0.0241  0.0123  241 TRP B CA  
4776 C C   . TRP B 271 ? 0.3774 0.4347 0.3886 0.0154  0.0235  0.0143  241 TRP B C   
4777 O O   . TRP B 271 ? 0.3853 0.4440 0.3957 0.0161  0.0233  0.0186  241 TRP B O   
4778 C CB  . TRP B 271 ? 0.3559 0.4046 0.3663 0.0087  0.0235  0.0139  241 TRP B CB  
4779 C CG  . TRP B 271 ? 0.3409 0.3897 0.3497 0.0072  0.0227  0.0209  241 TRP B CG  
4780 C CD1 . TRP B 271 ? 0.3415 0.3962 0.3501 0.0089  0.0223  0.0260  241 TRP B CD1 
4781 C CD2 . TRP B 271 ? 0.3387 0.3822 0.3455 0.0038  0.0222  0.0233  241 TRP B CD2 
4782 N NE1 . TRP B 271 ? 0.3437 0.3966 0.3509 0.0058  0.0216  0.0315  241 TRP B NE1 
4783 C CE2 . TRP B 271 ? 0.3458 0.3912 0.3516 0.0029  0.0214  0.0298  241 TRP B CE2 
4784 C CE3 . TRP B 271 ? 0.3464 0.3841 0.3522 0.0016  0.0222  0.0205  241 TRP B CE3 
4785 C CZ2 . TRP B 271 ? 0.3578 0.3977 0.3611 -0.0005 0.0205  0.0333  241 TRP B CZ2 
4786 C CZ3 . TRP B 271 ? 0.3634 0.3963 0.3665 -0.0009 0.0213  0.0240  241 TRP B CZ3 
4787 C CH2 . TRP B 271 ? 0.3641 0.3973 0.3659 -0.0021 0.0204  0.0302  241 TRP B CH2 
4788 N N   . LYS B 272 ? 0.3728 0.4371 0.3849 0.0193  0.0232  0.0108  242 LYS B N   
4789 C CA  . LYS B 272 ? 0.3820 0.4562 0.3942 0.0250  0.0227  0.0118  242 LYS B CA  
4790 C C   . LYS B 272 ? 0.4045 0.4781 0.4162 0.0275  0.0228  0.0106  242 LYS B C   
4791 O O   . LYS B 272 ? 0.4209 0.5005 0.4318 0.0304  0.0224  0.0151  242 LYS B O   
4792 C CB  . LYS B 272 ? 0.3907 0.4715 0.4039 0.0289  0.0225  0.0064  242 LYS B CB  
4793 C CG  . LYS B 272 ? 0.4172 0.5080 0.4306 0.0357  0.0220  0.0048  242 LYS B CG  
4794 C CD  . LYS B 272 ? 0.4487 0.5437 0.4634 0.0387  0.0217  -0.0028 242 LYS B CD  
4795 C CE  . LYS B 272 ? 0.4884 0.5925 0.5032 0.0456  0.0209  -0.0054 242 LYS B CE  
4796 N NZ  . LYS B 272 ? 0.5158 0.6226 0.5323 0.0476  0.0204  -0.0146 242 LYS B NZ  
4797 N N   . ASN B 273 ? 0.4020 0.4683 0.4138 0.0265  0.0232  0.0045  243 ASN B N   
4798 C CA  . ASN B 273 ? 0.4034 0.4672 0.4137 0.0295  0.0232  0.0026  243 ASN B CA  
4799 C C   . ASN B 273 ? 0.4209 0.4775 0.4291 0.0272  0.0238  0.0068  243 ASN B C   
4800 O O   . ASN B 273 ? 0.4367 0.4919 0.4426 0.0307  0.0238  0.0065  243 ASN B O   
4801 C CB  . ASN B 273 ? 0.4077 0.4661 0.4187 0.0293  0.0235  -0.0058 243 ASN B CB  
4802 C CG  . ASN B 273 ? 0.4454 0.5130 0.4583 0.0329  0.0227  -0.0107 243 ASN B CG  
4803 O OD1 . ASN B 273 ? 0.4656 0.5316 0.4804 0.0305  0.0229  -0.0165 243 ASN B OD1 
4804 N ND2 . ASN B 273 ? 0.4415 0.5200 0.4540 0.0390  0.0217  -0.0084 243 ASN B ND2 
4805 N N   . PHE B 274 ? 0.4138 0.4659 0.4222 0.0220  0.0243  0.0105  244 PHE B N   
4806 C CA  . PHE B 274 ? 0.4138 0.4595 0.4203 0.0198  0.0248  0.0143  244 PHE B CA  
4807 C C   . PHE B 274 ? 0.4247 0.4783 0.4309 0.0206  0.0240  0.0214  244 PHE B C   
4808 O O   . PHE B 274 ? 0.4292 0.4876 0.4368 0.0186  0.0235  0.0245  244 PHE B O   
4809 C CB  . PHE B 274 ? 0.4033 0.4403 0.4104 0.0135  0.0256  0.0138  244 PHE B CB  
4810 C CG  . PHE B 274 ? 0.4051 0.4356 0.4104 0.0106  0.0261  0.0177  244 PHE B CG  
4811 C CD1 . PHE B 274 ? 0.4120 0.4392 0.4145 0.0131  0.0267  0.0186  244 PHE B CD1 
4812 C CD2 . PHE B 274 ? 0.4140 0.4411 0.4198 0.0058  0.0261  0.0198  244 PHE B CD2 
4813 C CE1 . PHE B 274 ? 0.4235 0.4454 0.4241 0.0110  0.0273  0.0220  244 PHE B CE1 
4814 C CE2 . PHE B 274 ? 0.4267 0.4485 0.4309 0.0035  0.0265  0.0230  244 PHE B CE2 
4815 C CZ  . PHE B 274 ? 0.4226 0.4420 0.4242 0.0061  0.0272  0.0240  244 PHE B CZ  
4816 N N   . ASP B 275 ? 0.4254 0.4803 0.4294 0.0233  0.0240  0.0240  245 ASP B N   
4817 C CA  . ASP B 275 ? 0.4341 0.4966 0.4380 0.0229  0.0234  0.0308  245 ASP B CA  
4818 C C   . ASP B 275 ? 0.4348 0.4899 0.4368 0.0202  0.0239  0.0326  245 ASP B C   
4819 O O   . ASP B 275 ? 0.4430 0.4969 0.4421 0.0238  0.0243  0.0327  245 ASP B O   
4820 C CB  . ASP B 275 ? 0.4690 0.5437 0.4722 0.0288  0.0227  0.0333  245 ASP B CB  
4821 C CG  . ASP B 275 ? 0.5439 0.6284 0.5484 0.0268  0.0221  0.0405  245 ASP B CG  
4822 O OD1 . ASP B 275 ? 0.5426 0.6228 0.5474 0.0214  0.0221  0.0432  245 ASP B OD1 
4823 O OD2 . ASP B 275 ? 0.5994 0.6963 0.6046 0.0303  0.0216  0.0434  245 ASP B OD2 
4824 N N   . GLU B 276 ? 0.4242 0.4749 0.4273 0.0145  0.0239  0.0342  246 GLU B N   
4825 C CA  . GLU B 276 ? 0.4228 0.4668 0.4244 0.0114  0.0243  0.0360  246 GLU B CA  
4826 C C   . GLU B 276 ? 0.4017 0.4524 0.4019 0.0133  0.0238  0.0406  246 GLU B C   
4827 O O   . GLU B 276 ? 0.4036 0.4491 0.4011 0.0142  0.0245  0.0407  246 GLU B O   
4828 C CB  . GLU B 276 ? 0.4660 0.5071 0.4694 0.0055  0.0237  0.0372  246 GLU B CB  
4829 C CG  . GLU B 276 ? 0.5446 0.5815 0.5470 0.0017  0.0235  0.0399  246 GLU B CG  
4830 C CD  . GLU B 276 ? 0.6325 0.6670 0.6362 -0.0032 0.0225  0.0407  246 GLU B CD  
4831 O OE1 . GLU B 276 ? 0.6615 0.7014 0.6666 -0.0036 0.0217  0.0420  246 GLU B OE1 
4832 O OE2 . GLU B 276 ? 0.6570 0.6841 0.6599 -0.0063 0.0226  0.0400  246 GLU B OE2 
4833 N N   A ARG B 277 ? 0.3892 0.4520 0.3910 0.0141  0.0227  0.0445  247 ARG B N   
4834 N N   B ARG B 277 ? 0.3903 0.4530 0.3921 0.0141  0.0227  0.0445  247 ARG B N   
4835 C CA  A ARG B 277 ? 0.3836 0.4554 0.3845 0.0157  0.0222  0.0489  247 ARG B CA  
4836 C CA  B ARG B 277 ? 0.3857 0.4576 0.3866 0.0157  0.0222  0.0489  247 ARG B CA  
4837 C C   A ARG B 277 ? 0.3861 0.4607 0.3837 0.0231  0.0227  0.0477  247 ARG B C   
4838 C C   B ARG B 277 ? 0.3873 0.4616 0.3849 0.0231  0.0227  0.0476  247 ARG B C   
4839 O O   A ARG B 277 ? 0.3845 0.4610 0.3795 0.0252  0.0228  0.0496  247 ARG B O   
4840 O O   B ARG B 277 ? 0.3855 0.4616 0.3805 0.0251  0.0228  0.0495  247 ARG B O   
4841 C CB  A ARG B 277 ? 0.3818 0.4660 0.3858 0.0133  0.0211  0.0538  247 ARG B CB  
4842 C CB  B ARG B 277 ? 0.3863 0.4709 0.3902 0.0137  0.0211  0.0537  247 ARG B CB  
4843 C CG  A ARG B 277 ? 0.3966 0.4757 0.4025 0.0062  0.0204  0.0551  247 ARG B CG  
4844 C CG  B ARG B 277 ? 0.4042 0.4855 0.4102 0.0063  0.0203  0.0559  247 ARG B CG  
4845 C CD  A ARG B 277 ? 0.4080 0.4972 0.4164 0.0027  0.0194  0.0603  247 ARG B CD  
4846 C CD  B ARG B 277 ? 0.4233 0.5117 0.4318 0.0041  0.0197  0.0589  247 ARG B CD  
4847 N NE  A ARG B 277 ? 0.4161 0.4984 0.4252 -0.0042 0.0186  0.0614  247 ARG B NE  
4848 N NE  B ARG B 277 ? 0.4438 0.5312 0.4524 0.0075  0.0203  0.0558  247 ARG B NE  
4849 C CZ  A ARG B 277 ? 0.4089 0.4946 0.4188 -0.0090 0.0175  0.0652  247 ARG B CZ  
4850 C CZ  B ARG B 277 ? 0.4773 0.5553 0.4859 0.0059  0.0206  0.0522  247 ARG B CZ  
4851 N NH1 A ARG B 277 ? 0.3886 0.4860 0.3993 -0.0080 0.0172  0.0684  247 ARG B NH1 
4852 N NH1 B ARG B 277 ? 0.4679 0.5360 0.4759 0.0012  0.0204  0.0513  247 ARG B NH1 
4853 N NH2 A ARG B 277 ? 0.4007 0.4786 0.4106 -0.0148 0.0166  0.0655  247 ARG B NH2 
4854 N NH2 B ARG B 277 ? 0.4796 0.5589 0.4885 0.0095  0.0210  0.0491  247 ARG B NH2 
4855 N N   . LYS B 278 ? 0.3872 0.4611 0.3842 0.0275  0.0230  0.0439  248 LYS B N   
4856 C CA  . LYS B 278 ? 0.3917 0.4664 0.3848 0.0350  0.0233  0.0420  248 LYS B CA  
4857 C C   . LYS B 278 ? 0.4006 0.4596 0.3897 0.0358  0.0246  0.0379  248 LYS B C   
4858 O O   . LYS B 278 ? 0.4030 0.4601 0.3873 0.0410  0.0250  0.0379  248 LYS B O   
4859 C CB  . LYS B 278 ? 0.4095 0.4906 0.4032 0.0397  0.0228  0.0396  248 LYS B CB  
4860 C CG  . LYS B 278 ? 0.4593 0.5573 0.4561 0.0402  0.0218  0.0446  248 LYS B CG  
4861 C CD  . LYS B 278 ? 0.5169 0.6210 0.5149 0.0444  0.0214  0.0421  248 LYS B CD  
4862 C CE  . LYS B 278 ? 0.5730 0.6949 0.5728 0.0467  0.0208  0.0475  248 LYS B CE  
4863 N NZ  . LYS B 278 ? 0.6078 0.7350 0.6103 0.0471  0.0206  0.0468  248 LYS B NZ  
4864 N N   . GLU B 279 ? 0.3976 0.4453 0.3883 0.0306  0.0254  0.0347  249 GLU B N   
4865 C CA  . GLU B 279 ? 0.3998 0.4326 0.3870 0.0307  0.0270  0.0308  249 GLU B CA  
4866 C C   . GLU B 279 ? 0.4063 0.4303 0.3918 0.0271  0.0281  0.0326  249 GLU B C   
4867 O O   . GLU B 279 ? 0.4166 0.4291 0.3979 0.0288  0.0297  0.0304  249 GLU B O   
4868 C CB  . GLU B 279 ? 0.4127 0.4388 0.4025 0.0278  0.0274  0.0253  249 GLU B CB  
4869 C CG  . GLU B 279 ? 0.4732 0.5066 0.4643 0.0318  0.0264  0.0224  249 GLU B CG  
4870 C CD  . GLU B 279 ? 0.5360 0.5646 0.5300 0.0287  0.0267  0.0168  249 GLU B CD  
4871 O OE1 . GLU B 279 ? 0.5389 0.5555 0.5321 0.0253  0.0281  0.0136  249 GLU B OE1 
4872 O OE2 . GLU B 279 ? 0.5598 0.5972 0.5568 0.0296  0.0256  0.0158  249 GLU B OE2 
4873 N N   . MET B 280 ? 0.4002 0.4282 0.3885 0.0222  0.0275  0.0361  250 MET B N   
4874 C CA  . MET B 280 ? 0.4069 0.4263 0.3938 0.0187  0.0285  0.0370  250 MET B CA  
4875 C C   . MET B 280 ? 0.4166 0.4339 0.3984 0.0228  0.0293  0.0393  250 MET B C   
4876 O O   . MET B 280 ? 0.4183 0.4247 0.3975 0.0215  0.0309  0.0386  250 MET B O   
4877 C CB  . MET B 280 ? 0.4108 0.4339 0.4014 0.0127  0.0273  0.0395  250 MET B CB  
4878 C CG  . MET B 280 ? 0.4209 0.4412 0.4151 0.0083  0.0271  0.0367  250 MET B CG  
4879 S SD  . MET B 280 ? 0.4596 0.4667 0.4531 0.0072  0.0292  0.0309  250 MET B SD  
4880 C CE  . MET B 280 ? 0.3510 0.3484 0.3409 0.0060  0.0309  0.0325  250 MET B CE  
4881 N N   . ALA B 281 ? 0.4233 0.4510 0.4033 0.0278  0.0284  0.0421  251 ALA B N   
4882 C CA  . ALA B 281 ? 0.4342 0.4604 0.4085 0.0326  0.0292  0.0442  251 ALA B CA  
4883 C C   . ALA B 281 ? 0.4534 0.4655 0.4216 0.0372  0.0313  0.0409  251 ALA B C   
4884 O O   . ALA B 281 ? 0.4670 0.4704 0.4305 0.0387  0.0329  0.0417  251 ALA B O   
4885 C CB  . ALA B 281 ? 0.4269 0.4687 0.4004 0.0375  0.0278  0.0476  251 ALA B CB  
4886 N N   . THR B 282 ? 0.4547 0.4635 0.4231 0.0389  0.0313  0.0370  252 THR B N   
4887 C CA  . THR B 282 ? 0.4686 0.4628 0.4315 0.0423  0.0330  0.0332  252 THR B CA  
4888 C C   . THR B 282 ? 0.4740 0.4540 0.4380 0.0360  0.0350  0.0307  252 THR B C   
4889 O O   . THR B 282 ? 0.4967 0.4635 0.4552 0.0374  0.0371  0.0302  252 THR B O   
4890 C CB  . THR B 282 ? 0.4911 0.4876 0.4545 0.0458  0.0320  0.0293  252 THR B CB  
4891 O OG1 . THR B 282 ? 0.5077 0.5199 0.4710 0.0512  0.0302  0.0321  252 THR B OG1 
4892 C CG2 . THR B 282 ? 0.4994 0.4804 0.4561 0.0498  0.0335  0.0252  252 THR B CG2 
4893 N N   . ILE B 283 ? 0.4549 0.4376 0.4255 0.0292  0.0344  0.0294  253 ILE B N   
4894 C CA  . ILE B 283 ? 0.4461 0.4178 0.4184 0.0230  0.0361  0.0271  253 ILE B CA  
4895 C C   . ILE B 283 ? 0.4486 0.4156 0.4187 0.0213  0.0374  0.0306  253 ILE B C   
4896 O O   . ILE B 283 ? 0.4565 0.4108 0.4237 0.0197  0.0399  0.0295  253 ILE B O   
4897 C CB  . ILE B 283 ? 0.4363 0.4140 0.4156 0.0175  0.0348  0.0250  253 ILE B CB  
4898 C CG1 . ILE B 283 ? 0.4380 0.4200 0.4191 0.0199  0.0337  0.0210  253 ILE B CG1 
4899 C CG2 . ILE B 283 ? 0.4362 0.4050 0.4174 0.0112  0.0365  0.0230  253 ILE B CG2 
4900 C CD1 . ILE B 283 ? 0.4395 0.4278 0.4267 0.0157  0.0326  0.0186  253 ILE B CD1 
4901 N N   . LEU B 284 ? 0.4407 0.4179 0.4117 0.0218  0.0360  0.0349  254 LEU B N   
4902 C CA  . LEU B 284 ? 0.4531 0.4274 0.4219 0.0208  0.0369  0.0380  254 LEU B CA  
4903 C C   . LEU B 284 ? 0.4792 0.4449 0.4401 0.0269  0.0390  0.0392  254 LEU B C   
4904 O O   . LEU B 284 ? 0.4873 0.4446 0.4452 0.0259  0.0410  0.0404  254 LEU B O   
4905 C CB  . LEU B 284 ? 0.4463 0.4341 0.4180 0.0198  0.0345  0.0418  254 LEU B CB  
4906 C CG  . LEU B 284 ? 0.4554 0.4484 0.4335 0.0132  0.0328  0.0414  254 LEU B CG  
4907 C CD1 . LEU B 284 ? 0.4550 0.4619 0.4357 0.0128  0.0302  0.0448  254 LEU B CD1 
4908 C CD2 . LEU B 284 ? 0.4610 0.4464 0.4394 0.0088  0.0338  0.0412  254 LEU B CD2 
4909 N N   . SER B 285 ? 0.4935 0.4609 0.4502 0.0336  0.0387  0.0389  255 SER B N   
4910 C CA  . SER B 285 ? 0.5158 0.4739 0.4637 0.0404  0.0407  0.0398  255 SER B CA  
4911 C C   . SER B 285 ? 0.5391 0.4784 0.4835 0.0388  0.0435  0.0366  255 SER B C   
4912 O O   . SER B 285 ? 0.5604 0.4883 0.4979 0.0417  0.0460  0.0382  255 SER B O   
4913 C CB  . SER B 285 ? 0.5394 0.5049 0.4834 0.0485  0.0393  0.0402  255 SER B CB  
4914 O OG  . SER B 285 ? 0.5898 0.5521 0.5347 0.0491  0.0388  0.0360  255 SER B OG  
4915 N N   . LYS B 286 ? 0.5361 0.4723 0.4851 0.0342  0.0433  0.0323  256 LYS B N   
4916 C CA  . LYS B 286 ? 0.5547 0.4741 0.5015 0.0313  0.0459  0.0288  256 LYS B CA  
4917 C C   . LYS B 286 ? 0.5740 0.4869 0.5229 0.0244  0.0481  0.0298  256 LYS B C   
4918 O O   . LYS B 286 ? 0.5887 0.4871 0.5344 0.0223  0.0509  0.0284  256 LYS B O   
4919 C CB  . LYS B 286 ? 0.5728 0.4928 0.5242 0.0285  0.0448  0.0233  256 LYS B CB  
4920 C CG  . LYS B 286 ? 0.6185 0.5432 0.5672 0.0355  0.0428  0.0216  256 LYS B CG  
4921 C CD  . LYS B 286 ? 0.6658 0.5900 0.6187 0.0327  0.0419  0.0156  256 LYS B CD  
4922 C CE  . LYS B 286 ? 0.7129 0.6411 0.6625 0.0403  0.0400  0.0135  256 LYS B CE  
4923 N NZ  . LYS B 286 ? 0.7406 0.6683 0.6939 0.0382  0.0390  0.0072  256 LYS B NZ  
4924 N N   . MET B 287 ? 0.5748 0.4985 0.5292 0.0208  0.0467  0.0319  257 MET B N   
4925 C CA  . MET B 287 ? 0.5876 0.5083 0.5448 0.0148  0.0481  0.0328  257 MET B CA  
4926 C C   . MET B 287 ? 0.6122 0.5229 0.5626 0.0171  0.0510  0.0362  257 MET B C   
4927 O O   . MET B 287 ? 0.6194 0.5331 0.5649 0.0233  0.0507  0.0396  257 MET B O   
4928 C CB  . MET B 287 ? 0.5825 0.5177 0.5456 0.0122  0.0452  0.0345  257 MET B CB  
4929 C CG  . MET B 287 ? 0.6018 0.5362 0.5672 0.0073  0.0460  0.0357  257 MET B CG  
4930 S SD  . MET B 287 ? 0.5822 0.5320 0.5532 0.0050  0.0422  0.0376  257 MET B SD  
4931 C CE  . MET B 287 ? 0.5864 0.5427 0.5530 0.0113  0.0412  0.0419  257 MET B CE  
4932 N N   . PRO B 288 ? 0.6211 0.5205 0.5709 0.0126  0.0540  0.0356  258 PRO B N   
4933 C CA  . PRO B 288 ? 0.6394 0.5292 0.5825 0.0149  0.0572  0.0394  258 PRO B CA  
4934 C C   . PRO B 288 ? 0.6599 0.5597 0.6032 0.0170  0.0559  0.0436  258 PRO B C   
4935 O O   . PRO B 288 ? 0.6552 0.5647 0.6047 0.0127  0.0539  0.0432  258 PRO B O   
4936 C CB  . PRO B 288 ? 0.6424 0.5224 0.5875 0.0078  0.0602  0.0378  258 PRO B CB  
4937 C CG  . PRO B 288 ? 0.6355 0.5244 0.5893 0.0018  0.0580  0.0338  258 PRO B CG  
4938 C CD  . PRO B 288 ? 0.6120 0.5084 0.5674 0.0051  0.0548  0.0316  258 PRO B CD  
4939 N N   . LYS B 289 ? 0.6803 0.5781 0.6162 0.0239  0.0569  0.0472  259 LYS B N   
4940 C CA  . LYS B 289 ? 0.7009 0.6090 0.6365 0.0264  0.0555  0.0508  259 LYS B CA  
4941 C C   . LYS B 289 ? 0.7311 0.6314 0.6626 0.0266  0.0588  0.0538  259 LYS B C   
4942 O O   . LYS B 289 ? 0.7399 0.6255 0.6657 0.0275  0.0625  0.0545  259 LYS B O   
4943 C CB  . LYS B 289 ? 0.7134 0.6289 0.6444 0.0346  0.0539  0.0528  259 LYS B CB  
4944 C CG  . LYS B 289 ? 0.7429 0.6673 0.6776 0.0353  0.0509  0.0504  259 LYS B CG  
4945 C CD  . LYS B 289 ? 0.7694 0.7067 0.7136 0.0290  0.0476  0.0489  259 LYS B CD  
4946 C CE  . LYS B 289 ? 0.7849 0.7331 0.7318 0.0309  0.0447  0.0477  259 LYS B CE  
4947 N NZ  . LYS B 289 ? 0.8027 0.7424 0.7465 0.0337  0.0458  0.0450  259 LYS B NZ  
4948 N N   . PRO B 290 ? 0.7473 0.6568 0.6814 0.0255  0.0574  0.0557  260 PRO B N   
4949 C CA  . PRO B 290 ? 0.7663 0.6697 0.6964 0.0262  0.0604  0.0587  260 PRO B CA  
4950 C C   . PRO B 290 ? 0.7949 0.6901 0.7148 0.0344  0.0633  0.0621  260 PRO B C   
4951 O O   . PRO B 290 ? 0.8012 0.7033 0.7178 0.0408  0.0616  0.0632  260 PRO B O   
4952 C CB  . PRO B 290 ? 0.7645 0.6820 0.6986 0.0255  0.0572  0.0596  260 PRO B CB  
4953 C CG  . PRO B 290 ? 0.7578 0.6856 0.6997 0.0211  0.0531  0.0565  260 PRO B CG  
4954 C CD  . PRO B 290 ? 0.7378 0.6633 0.6782 0.0236  0.0530  0.0551  260 PRO B CD  
4955 N N   . LYS B 291 ? 0.8101 0.6908 0.7248 0.0342  0.0678  0.0639  261 LYS B N   
4956 C CA  . LYS B 291 ? 0.8328 0.7030 0.7366 0.0421  0.0713  0.0677  261 LYS B CA  
4957 C C   . LYS B 291 ? 0.8463 0.7251 0.7472 0.0471  0.0711  0.0714  261 LYS B C   
4958 O O   . LYS B 291 ? 0.8421 0.7244 0.7466 0.0433  0.0713  0.0721  261 LYS B O   
4959 C CB  . LYS B 291 ? 0.8626 0.7135 0.7621 0.0389  0.0764  0.0685  261 LYS B CB  
4960 C CG  . LYS B 291 ? 0.9221 0.7598 0.8095 0.0467  0.0807  0.0731  261 LYS B CG  
4961 C CD  . LYS B 291 ? 0.9829 0.8030 0.8672 0.0419  0.0861  0.0747  261 LYS B CD  
4962 C CE  . LYS B 291 ? 1.0366 0.8415 0.9195 0.0383  0.0876  0.0717  261 LYS B CE  
4963 N NZ  . LYS B 291 ? 1.0707 0.8574 0.9496 0.0336  0.0932  0.0737  261 LYS B NZ  
4964 N N   . PRO B 292 ? 0.8617 0.7447 0.7558 0.0563  0.0705  0.0735  262 PRO B N   
4965 C CA  . PRO B 292 ? 0.8664 0.7586 0.7573 0.0617  0.0702  0.0767  262 PRO B CA  
4966 C C   . PRO B 292 ? 0.8769 0.7562 0.7600 0.0647  0.0753  0.0808  262 PRO B C   
4967 O O   . PRO B 292 ? 0.8836 0.7454 0.7612 0.0645  0.0795  0.0818  262 PRO B O   
4968 C CB  . PRO B 292 ? 0.8763 0.7763 0.7619 0.0708  0.0684  0.0774  262 PRO B CB  
4969 C CG  . PRO B 292 ? 0.8894 0.7750 0.7695 0.0730  0.0705  0.0767  262 PRO B CG  
4970 C CD  . PRO B 292 ? 0.8656 0.7459 0.7541 0.0626  0.0701  0.0730  262 PRO B CD  
4971 N N   . PRO B 293 ? 0.8770 0.7649 0.7595 0.0673  0.0751  0.0831  263 PRO B N   
4972 C CA  . PRO B 293 ? 0.8907 0.7673 0.7654 0.0707  0.0802  0.0874  263 PRO B CA  
4973 C C   . PRO B 293 ? 0.9119 0.7780 0.7737 0.0812  0.0837  0.0911  263 PRO B C   
4974 O O   . PRO B 293 ? 0.9150 0.7881 0.7738 0.0876  0.0813  0.0904  263 PRO B O   
4975 C CB  . PRO B 293 ? 0.8909 0.7825 0.7685 0.0719  0.0780  0.0883  263 PRO B CB  
4976 C CG  . PRO B 293 ? 0.8846 0.7941 0.7676 0.0728  0.0723  0.0853  263 PRO B CG  
4977 C CD  . PRO B 293 ? 0.8598 0.7675 0.7483 0.0672  0.0703  0.0817  263 PRO B CD  
4978 N N   . PRO B 294 ? 0.9267 0.7760 0.7802 0.0834  0.0894  0.0951  264 PRO B N   
4979 C CA  . PRO B 294 ? 0.9431 0.7804 0.7828 0.0940  0.0928  0.0988  264 PRO B CA  
4980 C C   . PRO B 294 ? 0.9498 0.8001 0.7830 0.1056  0.0915  0.1011  264 PRO B C   
4981 O O   . PRO B 294 ? 0.9484 0.8153 0.7866 0.1057  0.0889  0.1009  264 PRO B O   
4982 C CB  . PRO B 294 ? 0.9588 0.7762 0.7922 0.0923  0.0993  0.1029  264 PRO B CB  
4983 C CG  . PRO B 294 ? 0.9556 0.7807 0.7983 0.0838  0.0989  0.1025  264 PRO B CG  
4984 C CD  . PRO B 294 ? 0.9245 0.7645 0.7801 0.0763  0.0931  0.0967  264 PRO B CD  
# 
