data_8S6L
# 
_entry.id   8S6L 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   8S6L         pdb_00008s6l 10.2210/pdb8s6l/pdb 
WWPDB D_1292136734 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-12 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8S6L 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-27 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 5 
_pdbx_contact_author.email              kira.weissman@univ-lorraine.fr 
_pdbx_contact_author.name_first         Kira 
_pdbx_contact_author.name_last          Weissman 
_pdbx_contact_author.name_mi            J. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3012-2960 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Calderari, A.'  1 0009-0009-2039-7002 
'Gruez, A.'      2 0000-0002-5828-5526 
'Najah, S.'      3 0000-0002-4669-5544 
'Li, Y.'         4 0000-0002-3156-391X 
'Weissman, K.J.' 5 0000-0002-3012-2960 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To be published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'High resolution structure of azetidomonamide dehydratase' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Calderari, A.'  1 0009-0009-2039-7002 
primary 'Gruez, A.'      2 0000-0002-5828-5526 
primary 'Najah, S.'      3 0000-0002-4669-5544 
primary 'Li, Y.'         4 0000-0002-3156-391X 
primary 'Weissman, K.J.' 5 0000-0002-3012-2960 
# 
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 'Phthiocerol/phthiodiolone dimycocerosyl transferase' 51241.734 1   2.3.1.282 ? ? ? 
2 non-polymer syn GLYCEROL                                              92.094    2   ?         ? ? ? 
3 water       nat water                                                 18.015    338 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'Acyltransferase PapA5,Phthiocerol/phthiodiolone O-acyltransferase,Polyketide synthase-associated protein A5' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MGSSHHHHHHSSGLVPRGSHMAEIRRPLSAVERWYWLSDQFSALNVISRVRVHGRLSIDDLRRGLDALQARHPLLRARIE
HDAGLDPRWVPCERPIPLREVRGGGEEQWLREINERELPERIDPDSGPLIRTVAIATDAGAHDLLVVVPHIIADGTTVLT
LAEQWLTLAADPAAQPWTASALPPAEDLRPRRFTGDEGAARLAEQTAQDEALVGRHRPGRIEPSNPVPLEARRTRLLHRE
LDGAQLEQLQRRAREHGTTVHGALTAALAIAAGHDHQRRPSHIAIGSPIDFRDELEPPVRPDEVGTYVATVPVVLDIARP
FWEVARALTDDLGERRRQGHHFNLVTLVASAAPRCMADARPFMAFMEAEGPINLCSSNIGRYPFPERIGALRLSDAQFLT
GISVNGYFVAAINSSHGRLFWNFTYIDEAVPGERAERLAEDCLGTLLSAIHAPQRSALEEQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSSGLVPRGSHMAEIRRPLSAVERWYWLSDQFSALNVISRVRVHGRLSIDDLRRGLDALQARHPLLRARIE
HDAGLDPRWVPCERPIPLREVRGGGEEQWLREINERELPERIDPDSGPLIRTVAIATDAGAHDLLVVVPHIIADGTTVLT
LAEQWLTLAADPAAQPWTASALPPAEDLRPRRFTGDEGAARLAEQTAQDEALVGRHRPGRIEPSNPVPLEARRTRLLHRE
LDGAQLEQLQRRAREHGTTVHGALTAALAIAAGHDHQRRPSHIAIGSPIDFRDELEPPVRPDEVGTYVATVPVVLDIARP
FWEVARALTDDLGERRRQGHHFNLVTLVASAAPRCMADARPFMAFMEAEGPINLCSSNIGRYPFPERIGALRLSDAQFLT
GISVNGYFVAAINSSHGRLFWNFTYIDEAVPGERAERLAEDCLGTLLSAIHAPQRSALEEQ
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 GLYCEROL GOL 
3 water    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  SER n 
1 13  GLY n 
1 14  LEU n 
1 15  VAL n 
1 16  PRO n 
1 17  ARG n 
1 18  GLY n 
1 19  SER n 
1 20  HIS n 
1 21  MET n 
1 22  ALA n 
1 23  GLU n 
1 24  ILE n 
1 25  ARG n 
1 26  ARG n 
1 27  PRO n 
1 28  LEU n 
1 29  SER n 
1 30  ALA n 
1 31  VAL n 
1 32  GLU n 
1 33  ARG n 
1 34  TRP n 
1 35  TYR n 
1 36  TRP n 
1 37  LEU n 
1 38  SER n 
1 39  ASP n 
1 40  GLN n 
1 41  PHE n 
1 42  SER n 
1 43  ALA n 
1 44  LEU n 
1 45  ASN n 
1 46  VAL n 
1 47  ILE n 
1 48  SER n 
1 49  ARG n 
1 50  VAL n 
1 51  ARG n 
1 52  VAL n 
1 53  HIS n 
1 54  GLY n 
1 55  ARG n 
1 56  LEU n 
1 57  SER n 
1 58  ILE n 
1 59  ASP n 
1 60  ASP n 
1 61  LEU n 
1 62  ARG n 
1 63  ARG n 
1 64  GLY n 
1 65  LEU n 
1 66  ASP n 
1 67  ALA n 
1 68  LEU n 
1 69  GLN n 
1 70  ALA n 
1 71  ARG n 
1 72  HIS n 
1 73  PRO n 
1 74  LEU n 
1 75  LEU n 
1 76  ARG n 
1 77  ALA n 
1 78  ARG n 
1 79  ILE n 
1 80  GLU n 
1 81  HIS n 
1 82  ASP n 
1 83  ALA n 
1 84  GLY n 
1 85  LEU n 
1 86  ASP n 
1 87  PRO n 
1 88  ARG n 
1 89  TRP n 
1 90  VAL n 
1 91  PRO n 
1 92  CYS n 
1 93  GLU n 
1 94  ARG n 
1 95  PRO n 
1 96  ILE n 
1 97  PRO n 
1 98  LEU n 
1 99  ARG n 
1 100 GLU n 
1 101 VAL n 
1 102 ARG n 
1 103 GLY n 
1 104 GLY n 
1 105 GLY n 
1 106 GLU n 
1 107 GLU n 
1 108 GLN n 
1 109 TRP n 
1 110 LEU n 
1 111 ARG n 
1 112 GLU n 
1 113 ILE n 
1 114 ASN n 
1 115 GLU n 
1 116 ARG n 
1 117 GLU n 
1 118 LEU n 
1 119 PRO n 
1 120 GLU n 
1 121 ARG n 
1 122 ILE n 
1 123 ASP n 
1 124 PRO n 
1 125 ASP n 
1 126 SER n 
1 127 GLY n 
1 128 PRO n 
1 129 LEU n 
1 130 ILE n 
1 131 ARG n 
1 132 THR n 
1 133 VAL n 
1 134 ALA n 
1 135 ILE n 
1 136 ALA n 
1 137 THR n 
1 138 ASP n 
1 139 ALA n 
1 140 GLY n 
1 141 ALA n 
1 142 HIS n 
1 143 ASP n 
1 144 LEU n 
1 145 LEU n 
1 146 VAL n 
1 147 VAL n 
1 148 VAL n 
1 149 PRO n 
1 150 HIS n 
1 151 ILE n 
1 152 ILE n 
1 153 ALA n 
1 154 ASP n 
1 155 GLY n 
1 156 THR n 
1 157 THR n 
1 158 VAL n 
1 159 LEU n 
1 160 THR n 
1 161 LEU n 
1 162 ALA n 
1 163 GLU n 
1 164 GLN n 
1 165 TRP n 
1 166 LEU n 
1 167 THR n 
1 168 LEU n 
1 169 ALA n 
1 170 ALA n 
1 171 ASP n 
1 172 PRO n 
1 173 ALA n 
1 174 ALA n 
1 175 GLN n 
1 176 PRO n 
1 177 TRP n 
1 178 THR n 
1 179 ALA n 
1 180 SER n 
1 181 ALA n 
1 182 LEU n 
1 183 PRO n 
1 184 PRO n 
1 185 ALA n 
1 186 GLU n 
1 187 ASP n 
1 188 LEU n 
1 189 ARG n 
1 190 PRO n 
1 191 ARG n 
1 192 ARG n 
1 193 PHE n 
1 194 THR n 
1 195 GLY n 
1 196 ASP n 
1 197 GLU n 
1 198 GLY n 
1 199 ALA n 
1 200 ALA n 
1 201 ARG n 
1 202 LEU n 
1 203 ALA n 
1 204 GLU n 
1 205 GLN n 
1 206 THR n 
1 207 ALA n 
1 208 GLN n 
1 209 ASP n 
1 210 GLU n 
1 211 ALA n 
1 212 LEU n 
1 213 VAL n 
1 214 GLY n 
1 215 ARG n 
1 216 HIS n 
1 217 ARG n 
1 218 PRO n 
1 219 GLY n 
1 220 ARG n 
1 221 ILE n 
1 222 GLU n 
1 223 PRO n 
1 224 SER n 
1 225 ASN n 
1 226 PRO n 
1 227 VAL n 
1 228 PRO n 
1 229 LEU n 
1 230 GLU n 
1 231 ALA n 
1 232 ARG n 
1 233 ARG n 
1 234 THR n 
1 235 ARG n 
1 236 LEU n 
1 237 LEU n 
1 238 HIS n 
1 239 ARG n 
1 240 GLU n 
1 241 LEU n 
1 242 ASP n 
1 243 GLY n 
1 244 ALA n 
1 245 GLN n 
1 246 LEU n 
1 247 GLU n 
1 248 GLN n 
1 249 LEU n 
1 250 GLN n 
1 251 ARG n 
1 252 ARG n 
1 253 ALA n 
1 254 ARG n 
1 255 GLU n 
1 256 HIS n 
1 257 GLY n 
1 258 THR n 
1 259 THR n 
1 260 VAL n 
1 261 HIS n 
1 262 GLY n 
1 263 ALA n 
1 264 LEU n 
1 265 THR n 
1 266 ALA n 
1 267 ALA n 
1 268 LEU n 
1 269 ALA n 
1 270 ILE n 
1 271 ALA n 
1 272 ALA n 
1 273 GLY n 
1 274 HIS n 
1 275 ASP n 
1 276 HIS n 
1 277 GLN n 
1 278 ARG n 
1 279 ARG n 
1 280 PRO n 
1 281 SER n 
1 282 HIS n 
1 283 ILE n 
1 284 ALA n 
1 285 ILE n 
1 286 GLY n 
1 287 SER n 
1 288 PRO n 
1 289 ILE n 
1 290 ASP n 
1 291 PHE n 
1 292 ARG n 
1 293 ASP n 
1 294 GLU n 
1 295 LEU n 
1 296 GLU n 
1 297 PRO n 
1 298 PRO n 
1 299 VAL n 
1 300 ARG n 
1 301 PRO n 
1 302 ASP n 
1 303 GLU n 
1 304 VAL n 
1 305 GLY n 
1 306 THR n 
1 307 TYR n 
1 308 VAL n 
1 309 ALA n 
1 310 THR n 
1 311 VAL n 
1 312 PRO n 
1 313 VAL n 
1 314 VAL n 
1 315 LEU n 
1 316 ASP n 
1 317 ILE n 
1 318 ALA n 
1 319 ARG n 
1 320 PRO n 
1 321 PHE n 
1 322 TRP n 
1 323 GLU n 
1 324 VAL n 
1 325 ALA n 
1 326 ARG n 
1 327 ALA n 
1 328 LEU n 
1 329 THR n 
1 330 ASP n 
1 331 ASP n 
1 332 LEU n 
1 333 GLY n 
1 334 GLU n 
1 335 ARG n 
1 336 ARG n 
1 337 ARG n 
1 338 GLN n 
1 339 GLY n 
1 340 HIS n 
1 341 HIS n 
1 342 PHE n 
1 343 ASN n 
1 344 LEU n 
1 345 VAL n 
1 346 THR n 
1 347 LEU n 
1 348 VAL n 
1 349 ALA n 
1 350 SER n 
1 351 ALA n 
1 352 ALA n 
1 353 PRO n 
1 354 ARG n 
1 355 CYS n 
1 356 MET n 
1 357 ALA n 
1 358 ASP n 
1 359 ALA n 
1 360 ARG n 
1 361 PRO n 
1 362 PHE n 
1 363 MET n 
1 364 ALA n 
1 365 PHE n 
1 366 MET n 
1 367 GLU n 
1 368 ALA n 
1 369 GLU n 
1 370 GLY n 
1 371 PRO n 
1 372 ILE n 
1 373 ASN n 
1 374 LEU n 
1 375 CYS n 
1 376 SER n 
1 377 SER n 
1 378 ASN n 
1 379 ILE n 
1 380 GLY n 
1 381 ARG n 
1 382 TYR n 
1 383 PRO n 
1 384 PHE n 
1 385 PRO n 
1 386 GLU n 
1 387 ARG n 
1 388 ILE n 
1 389 GLY n 
1 390 ALA n 
1 391 LEU n 
1 392 ARG n 
1 393 LEU n 
1 394 SER n 
1 395 ASP n 
1 396 ALA n 
1 397 GLN n 
1 398 PHE n 
1 399 LEU n 
1 400 THR n 
1 401 GLY n 
1 402 ILE n 
1 403 SER n 
1 404 VAL n 
1 405 ASN n 
1 406 GLY n 
1 407 TYR n 
1 408 PHE n 
1 409 VAL n 
1 410 ALA n 
1 411 ALA n 
1 412 ILE n 
1 413 ASN n 
1 414 SER n 
1 415 SER n 
1 416 HIS n 
1 417 GLY n 
1 418 ARG n 
1 419 LEU n 
1 420 PHE n 
1 421 TRP n 
1 422 ASN n 
1 423 PHE n 
1 424 THR n 
1 425 TYR n 
1 426 ILE n 
1 427 ASP n 
1 428 GLU n 
1 429 ALA n 
1 430 VAL n 
1 431 PRO n 
1 432 GLY n 
1 433 GLU n 
1 434 ARG n 
1 435 ALA n 
1 436 GLU n 
1 437 ARG n 
1 438 LEU n 
1 439 ALA n 
1 440 GLU n 
1 441 ASP n 
1 442 CYS n 
1 443 LEU n 
1 444 GLY n 
1 445 THR n 
1 446 LEU n 
1 447 LEU n 
1 448 SER n 
1 449 ALA n 
1 450 ILE n 
1 451 HIS n 
1 452 ALA n 
1 453 PRO n 
1 454 GLN n 
1 455 ARG n 
1 456 SER n 
1 457 ALA n 
1 458 LEU n 
1 459 GLU n 
1 460 GLU n 
1 461 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   461 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 PA3329 
_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      'Pseudomonas aeruginosa PAO1' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     208964 
_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      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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          Plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   'His6 tag' 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET28a 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ?                               'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ?                               'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ?                               'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                               'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ?                               'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ?                               'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                               'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ?                               'C2 H5 N O2'     75.067  
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 
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   MET 1   -19 ?   ?   ?   A . n 
A 1 2   GLY 2   -18 ?   ?   ?   A . n 
A 1 3   SER 3   -17 ?   ?   ?   A . n 
A 1 4   SER 4   -16 ?   ?   ?   A . n 
A 1 5   HIS 5   -15 ?   ?   ?   A . n 
A 1 6   HIS 6   -14 ?   ?   ?   A . n 
A 1 7   HIS 7   -13 ?   ?   ?   A . n 
A 1 8   HIS 8   -12 ?   ?   ?   A . n 
A 1 9   HIS 9   -11 ?   ?   ?   A . n 
A 1 10  HIS 10  -10 ?   ?   ?   A . n 
A 1 11  SER 11  -9  ?   ?   ?   A . n 
A 1 12  SER 12  -8  ?   ?   ?   A . n 
A 1 13  GLY 13  -7  ?   ?   ?   A . n 
A 1 14  LEU 14  -6  ?   ?   ?   A . n 
A 1 15  VAL 15  -5  ?   ?   ?   A . n 
A 1 16  PRO 16  -4  ?   ?   ?   A . n 
A 1 17  ARG 17  -3  ?   ?   ?   A . n 
A 1 18  GLY 18  -2  ?   ?   ?   A . n 
A 1 19  SER 19  -1  ?   ?   ?   A . n 
A 1 20  HIS 20  0   ?   ?   ?   A . n 
A 1 21  MET 21  1   ?   ?   ?   A . n 
A 1 22  ALA 22  2   2   ALA ALA A . n 
A 1 23  GLU 23  3   3   GLU GLU A . n 
A 1 24  ILE 24  4   4   ILE ILE A . n 
A 1 25  ARG 25  5   5   ARG ARG A . n 
A 1 26  ARG 26  6   6   ARG ARG A . n 
A 1 27  PRO 27  7   7   PRO PRO A . n 
A 1 28  LEU 28  8   8   LEU LEU A . n 
A 1 29  SER 29  9   9   SER SER A . n 
A 1 30  ALA 30  10  10  ALA ALA A . n 
A 1 31  VAL 31  11  11  VAL VAL A . n 
A 1 32  GLU 32  12  12  GLU GLU A . n 
A 1 33  ARG 33  13  13  ARG ARG A . n 
A 1 34  TRP 34  14  14  TRP TRP A . n 
A 1 35  TYR 35  15  15  TYR TYR A . n 
A 1 36  TRP 36  16  16  TRP TRP A . n 
A 1 37  LEU 37  17  17  LEU LEU A . n 
A 1 38  SER 38  18  18  SER SER A . n 
A 1 39  ASP 39  19  19  ASP ASP A . n 
A 1 40  GLN 40  20  20  GLN GLN A . n 
A 1 41  PHE 41  21  21  PHE PHE A . n 
A 1 42  SER 42  22  22  SER SER A . n 
A 1 43  ALA 43  23  23  ALA ALA A . n 
A 1 44  LEU 44  24  24  LEU LEU A . n 
A 1 45  ASN 45  25  25  ASN ASN A . n 
A 1 46  VAL 46  26  26  VAL VAL A . n 
A 1 47  ILE 47  27  27  ILE ILE A . n 
A 1 48  SER 48  28  28  SER SER A . n 
A 1 49  ARG 49  29  29  ARG ARG A . n 
A 1 50  VAL 50  30  30  VAL VAL A . n 
A 1 51  ARG 51  31  31  ARG ARG A . n 
A 1 52  VAL 52  32  32  VAL VAL A . n 
A 1 53  HIS 53  33  33  HIS HIS A . n 
A 1 54  GLY 54  34  34  GLY GLY A . n 
A 1 55  ARG 55  35  35  ARG ARG A . n 
A 1 56  LEU 56  36  36  LEU LEU A . n 
A 1 57  SER 57  37  37  SER SER A . n 
A 1 58  ILE 58  38  38  ILE ILE A . n 
A 1 59  ASP 59  39  39  ASP ASP A . n 
A 1 60  ASP 60  40  40  ASP ASP A . n 
A 1 61  LEU 61  41  41  LEU LEU A . n 
A 1 62  ARG 62  42  42  ARG ARG A . n 
A 1 63  ARG 63  43  43  ARG ARG A . n 
A 1 64  GLY 64  44  44  GLY GLY A . n 
A 1 65  LEU 65  45  45  LEU LEU A . n 
A 1 66  ASP 66  46  46  ASP ASP A . n 
A 1 67  ALA 67  47  47  ALA ALA A . n 
A 1 68  LEU 68  48  48  LEU LEU A . n 
A 1 69  GLN 69  49  49  GLN GLN A . n 
A 1 70  ALA 70  50  50  ALA ALA A . n 
A 1 71  ARG 71  51  51  ARG ARG A . n 
A 1 72  HIS 72  52  52  HIS HIS A . n 
A 1 73  PRO 73  53  53  PRO PRO A . n 
A 1 74  LEU 74  54  54  LEU LEU A . n 
A 1 75  LEU 75  55  55  LEU LEU A . n 
A 1 76  ARG 76  56  56  ARG ARG A . n 
A 1 77  ALA 77  57  57  ALA ALA A . n 
A 1 78  ARG 78  58  58  ARG ARG A . n 
A 1 79  ILE 79  59  59  ILE ILE A . n 
A 1 80  GLU 80  60  60  GLU GLU A . n 
A 1 81  HIS 81  61  61  HIS HIS A . n 
A 1 82  ASP 82  62  62  ASP ASP A . n 
A 1 83  ALA 83  63  63  ALA ALA A . n 
A 1 84  GLY 84  64  64  GLY GLY A . n 
A 1 85  LEU 85  65  65  LEU LEU A . n 
A 1 86  ASP 86  66  66  ASP ASP A . n 
A 1 87  PRO 87  67  67  PRO PRO A . n 
A 1 88  ARG 88  68  68  ARG ARG A . n 
A 1 89  TRP 89  69  69  TRP TRP A . n 
A 1 90  VAL 90  70  70  VAL VAL A . n 
A 1 91  PRO 91  71  71  PRO PRO A . n 
A 1 92  CYS 92  72  72  CYS CYS A . n 
A 1 93  GLU 93  73  73  GLU GLU A . n 
A 1 94  ARG 94  74  74  ARG ARG A . n 
A 1 95  PRO 95  75  75  PRO PRO A . n 
A 1 96  ILE 96  76  76  ILE ILE A . n 
A 1 97  PRO 97  77  77  PRO PRO A . n 
A 1 98  LEU 98  78  78  LEU LEU A . n 
A 1 99  ARG 99  79  79  ARG ARG A . n 
A 1 100 GLU 100 80  80  GLU GLU A . n 
A 1 101 VAL 101 81  81  VAL VAL A . n 
A 1 102 ARG 102 82  82  ARG ARG A . n 
A 1 103 GLY 103 83  83  GLY GLY A . n 
A 1 104 GLY 104 84  84  GLY GLY A . n 
A 1 105 GLY 105 85  85  GLY GLY A . n 
A 1 106 GLU 106 86  86  GLU GLU A . n 
A 1 107 GLU 107 87  87  GLU GLU A . n 
A 1 108 GLN 108 88  88  GLN GLN A . n 
A 1 109 TRP 109 89  89  TRP TRP A . n 
A 1 110 LEU 110 90  90  LEU LEU A . n 
A 1 111 ARG 111 91  91  ARG ARG A . n 
A 1 112 GLU 112 92  92  GLU GLU A . n 
A 1 113 ILE 113 93  93  ILE ILE A . n 
A 1 114 ASN 114 94  94  ASN ASN A . n 
A 1 115 GLU 115 95  95  GLU GLU A . n 
A 1 116 ARG 116 96  96  ARG ARG A . n 
A 1 117 GLU 117 97  97  GLU GLU A . n 
A 1 118 LEU 118 98  98  LEU LEU A . n 
A 1 119 PRO 119 99  99  PRO PRO A . n 
A 1 120 GLU 120 100 100 GLU GLU A . n 
A 1 121 ARG 121 101 101 ARG ARG A . n 
A 1 122 ILE 122 102 102 ILE ILE A . n 
A 1 123 ASP 123 103 103 ASP ASP A . n 
A 1 124 PRO 124 104 104 PRO PRO A . n 
A 1 125 ASP 125 105 105 ASP ASP A . n 
A 1 126 SER 126 106 106 SER SER A . n 
A 1 127 GLY 127 107 107 GLY GLY A . n 
A 1 128 PRO 128 108 108 PRO PRO A . n 
A 1 129 LEU 129 109 109 LEU LEU A . n 
A 1 130 ILE 130 110 110 ILE ILE A . n 
A 1 131 ARG 131 111 111 ARG ARG A . n 
A 1 132 THR 132 112 112 THR THR A . n 
A 1 133 VAL 133 113 113 VAL VAL A . n 
A 1 134 ALA 134 114 114 ALA ALA A . n 
A 1 135 ILE 135 115 115 ILE ILE A . n 
A 1 136 ALA 136 116 116 ALA ALA A . n 
A 1 137 THR 137 117 117 THR THR A . n 
A 1 138 ASP 138 118 118 ASP ASP A . n 
A 1 139 ALA 139 119 119 ALA ALA A . n 
A 1 140 GLY 140 120 120 GLY GLY A . n 
A 1 141 ALA 141 121 121 ALA ALA A . n 
A 1 142 HIS 142 122 122 HIS HIS A . n 
A 1 143 ASP 143 123 123 ASP ASP A . n 
A 1 144 LEU 144 124 124 LEU LEU A . n 
A 1 145 LEU 145 125 125 LEU LEU A . n 
A 1 146 VAL 146 126 126 VAL VAL A . n 
A 1 147 VAL 147 127 127 VAL VAL A . n 
A 1 148 VAL 148 128 128 VAL VAL A . n 
A 1 149 PRO 149 129 129 PRO PRO A . n 
A 1 150 HIS 150 130 130 HIS HIS A . n 
A 1 151 ILE 151 131 131 ILE ILE A . n 
A 1 152 ILE 152 132 132 ILE ILE A . n 
A 1 153 ALA 153 133 133 ALA ALA A . n 
A 1 154 ASP 154 134 134 ASP ASP A . n 
A 1 155 GLY 155 135 135 GLY GLY A . n 
A 1 156 THR 156 136 136 THR THR A . n 
A 1 157 THR 157 137 137 THR THR A . n 
A 1 158 VAL 158 138 138 VAL VAL A . n 
A 1 159 LEU 159 139 139 LEU LEU A . n 
A 1 160 THR 160 140 140 THR THR A . n 
A 1 161 LEU 161 141 141 LEU LEU A . n 
A 1 162 ALA 162 142 142 ALA ALA A . n 
A 1 163 GLU 163 143 143 GLU GLU A . n 
A 1 164 GLN 164 144 144 GLN GLN A . n 
A 1 165 TRP 165 145 145 TRP TRP A . n 
A 1 166 LEU 166 146 146 LEU LEU A . n 
A 1 167 THR 167 147 147 THR THR A . n 
A 1 168 LEU 168 148 148 LEU LEU A . n 
A 1 169 ALA 169 149 149 ALA ALA A . n 
A 1 170 ALA 170 150 150 ALA ALA A . n 
A 1 171 ASP 171 151 151 ASP ASP A . n 
A 1 172 PRO 172 152 152 PRO PRO A . n 
A 1 173 ALA 173 153 153 ALA ALA A . n 
A 1 174 ALA 174 154 154 ALA ALA A . n 
A 1 175 GLN 175 155 155 GLN GLN A . n 
A 1 176 PRO 176 156 156 PRO PRO A . n 
A 1 177 TRP 177 157 157 TRP TRP A . n 
A 1 178 THR 178 158 158 THR THR A . n 
A 1 179 ALA 179 159 159 ALA ALA A . n 
A 1 180 SER 180 160 160 SER SER A . n 
A 1 181 ALA 181 161 161 ALA ALA A . n 
A 1 182 LEU 182 162 162 LEU LEU A . n 
A 1 183 PRO 183 163 163 PRO PRO A . n 
A 1 184 PRO 184 164 164 PRO PRO A . n 
A 1 185 ALA 185 165 165 ALA ALA A . n 
A 1 186 GLU 186 166 166 GLU GLU A . n 
A 1 187 ASP 187 167 167 ASP ASP A . n 
A 1 188 LEU 188 168 168 LEU LEU A . n 
A 1 189 ARG 189 169 169 ARG ARG A . n 
A 1 190 PRO 190 170 170 PRO PRO A . n 
A 1 191 ARG 191 171 171 ARG ARG A . n 
A 1 192 ARG 192 172 172 ARG ARG A . n 
A 1 193 PHE 193 173 173 PHE PHE A . n 
A 1 194 THR 194 174 174 THR THR A . n 
A 1 195 GLY 195 175 175 GLY GLY A . n 
A 1 196 ASP 196 176 176 ASP ASP A . n 
A 1 197 GLU 197 177 177 GLU GLU A . n 
A 1 198 GLY 198 178 178 GLY GLY A . n 
A 1 199 ALA 199 179 179 ALA ALA A . n 
A 1 200 ALA 200 180 180 ALA ALA A . n 
A 1 201 ARG 201 181 181 ARG ARG A . n 
A 1 202 LEU 202 182 182 LEU LEU A . n 
A 1 203 ALA 203 183 183 ALA ALA A . n 
A 1 204 GLU 204 184 184 GLU GLU A . n 
A 1 205 GLN 205 185 185 GLN GLN A . n 
A 1 206 THR 206 186 186 THR THR A . n 
A 1 207 ALA 207 187 187 ALA ALA A . n 
A 1 208 GLN 208 188 188 GLN GLN A . n 
A 1 209 ASP 209 189 189 ASP ASP A . n 
A 1 210 GLU 210 190 190 GLU GLU A . n 
A 1 211 ALA 211 191 191 ALA ALA A . n 
A 1 212 LEU 212 192 192 LEU LEU A . n 
A 1 213 VAL 213 193 193 VAL VAL A . n 
A 1 214 GLY 214 194 194 GLY GLY A . n 
A 1 215 ARG 215 195 195 ARG ARG A . n 
A 1 216 HIS 216 196 196 HIS HIS A . n 
A 1 217 ARG 217 197 197 ARG ARG A . n 
A 1 218 PRO 218 198 198 PRO PRO A . n 
A 1 219 GLY 219 199 199 GLY GLY A . n 
A 1 220 ARG 220 200 200 ARG ARG A . n 
A 1 221 ILE 221 201 201 ILE ILE A . n 
A 1 222 GLU 222 202 202 GLU GLU A . n 
A 1 223 PRO 223 203 203 PRO PRO A . n 
A 1 224 SER 224 204 204 SER SER A . n 
A 1 225 ASN 225 205 205 ASN ASN A . n 
A 1 226 PRO 226 206 206 PRO PRO A . n 
A 1 227 VAL 227 207 207 VAL VAL A . n 
A 1 228 PRO 228 208 208 PRO PRO A . n 
A 1 229 LEU 229 209 209 LEU LEU A . n 
A 1 230 GLU 230 210 210 GLU GLU A . n 
A 1 231 ALA 231 211 211 ALA ALA A . n 
A 1 232 ARG 232 212 212 ARG ARG A . n 
A 1 233 ARG 233 213 213 ARG ARG A . n 
A 1 234 THR 234 214 214 THR THR A . n 
A 1 235 ARG 235 215 215 ARG ARG A . n 
A 1 236 LEU 236 216 216 LEU LEU A . n 
A 1 237 LEU 237 217 217 LEU LEU A . n 
A 1 238 HIS 238 218 218 HIS HIS A . n 
A 1 239 ARG 239 219 219 ARG ARG A . n 
A 1 240 GLU 240 220 220 GLU GLU A . n 
A 1 241 LEU 241 221 221 LEU LEU A . n 
A 1 242 ASP 242 222 222 ASP ASP A . n 
A 1 243 GLY 243 223 223 GLY GLY A . n 
A 1 244 ALA 244 224 224 ALA ALA A . n 
A 1 245 GLN 245 225 225 GLN GLN A . n 
A 1 246 LEU 246 226 226 LEU LEU A . n 
A 1 247 GLU 247 227 227 GLU GLU A . n 
A 1 248 GLN 248 228 228 GLN GLN A . n 
A 1 249 LEU 249 229 229 LEU LEU A . n 
A 1 250 GLN 250 230 230 GLN GLN A . n 
A 1 251 ARG 251 231 231 ARG ARG A . n 
A 1 252 ARG 252 232 232 ARG ARG A . n 
A 1 253 ALA 253 233 233 ALA ALA A . n 
A 1 254 ARG 254 234 234 ARG ARG A . n 
A 1 255 GLU 255 235 235 GLU GLU A . n 
A 1 256 HIS 256 236 236 HIS HIS A . n 
A 1 257 GLY 257 237 237 GLY GLY A . n 
A 1 258 THR 258 238 238 THR THR A . n 
A 1 259 THR 259 239 239 THR THR A . n 
A 1 260 VAL 260 240 240 VAL VAL A . n 
A 1 261 HIS 261 241 241 HIS HIS A . n 
A 1 262 GLY 262 242 242 GLY GLY A . n 
A 1 263 ALA 263 243 243 ALA ALA A . n 
A 1 264 LEU 264 244 244 LEU LEU A . n 
A 1 265 THR 265 245 245 THR THR A . n 
A 1 266 ALA 266 246 246 ALA ALA A . n 
A 1 267 ALA 267 247 247 ALA ALA A . n 
A 1 268 LEU 268 248 248 LEU LEU A . n 
A 1 269 ALA 269 249 249 ALA ALA A . n 
A 1 270 ILE 270 250 250 ILE ILE A . n 
A 1 271 ALA 271 251 251 ALA ALA A . n 
A 1 272 ALA 272 252 252 ALA ALA A . n 
A 1 273 GLY 273 253 253 GLY GLY A . n 
A 1 274 HIS 274 254 254 HIS HIS A . n 
A 1 275 ASP 275 255 255 ASP ASP A . n 
A 1 276 HIS 276 256 256 HIS HIS A . n 
A 1 277 GLN 277 257 257 GLN GLN A . n 
A 1 278 ARG 278 258 258 ARG ARG A . n 
A 1 279 ARG 279 259 259 ARG ARG A . n 
A 1 280 PRO 280 260 260 PRO PRO A . n 
A 1 281 SER 281 261 261 SER SER A . n 
A 1 282 HIS 282 262 262 HIS HIS A . n 
A 1 283 ILE 283 263 263 ILE ILE A . n 
A 1 284 ALA 284 264 264 ALA ALA A . n 
A 1 285 ILE 285 265 265 ILE ILE A . n 
A 1 286 GLY 286 266 266 GLY GLY A . n 
A 1 287 SER 287 267 267 SER SER A . n 
A 1 288 PRO 288 268 268 PRO PRO A . n 
A 1 289 ILE 289 269 269 ILE ILE A . n 
A 1 290 ASP 290 270 270 ASP ASP A . n 
A 1 291 PHE 291 271 271 PHE PHE A . n 
A 1 292 ARG 292 272 272 ARG ARG A . n 
A 1 293 ASP 293 273 273 ASP ASP A . n 
A 1 294 GLU 294 274 274 GLU GLU A . n 
A 1 295 LEU 295 275 275 LEU LEU A . n 
A 1 296 GLU 296 276 276 GLU GLU A . n 
A 1 297 PRO 297 277 277 PRO PRO A . n 
A 1 298 PRO 298 278 278 PRO PRO A . n 
A 1 299 VAL 299 279 279 VAL VAL A . n 
A 1 300 ARG 300 280 280 ARG ARG A . n 
A 1 301 PRO 301 281 281 PRO PRO A . n 
A 1 302 ASP 302 282 282 ASP ASP A . n 
A 1 303 GLU 303 283 283 GLU GLU A . n 
A 1 304 VAL 304 284 284 VAL VAL A . n 
A 1 305 GLY 305 285 285 GLY GLY A . n 
A 1 306 THR 306 286 286 THR THR A . n 
A 1 307 TYR 307 287 287 TYR TYR A . n 
A 1 308 VAL 308 288 288 VAL VAL A . n 
A 1 309 ALA 309 289 289 ALA ALA A . n 
A 1 310 THR 310 290 290 THR THR A . n 
A 1 311 VAL 311 291 291 VAL VAL A . n 
A 1 312 PRO 312 292 292 PRO PRO A . n 
A 1 313 VAL 313 293 293 VAL VAL A . n 
A 1 314 VAL 314 294 294 VAL VAL A . n 
A 1 315 LEU 315 295 295 LEU LEU A . n 
A 1 316 ASP 316 296 296 ASP ASP A . n 
A 1 317 ILE 317 297 297 ILE ILE A . n 
A 1 318 ALA 318 298 298 ALA ALA A . n 
A 1 319 ARG 319 299 299 ARG ARG A . n 
A 1 320 PRO 320 300 300 PRO PRO A . n 
A 1 321 PHE 321 301 301 PHE PHE A . n 
A 1 322 TRP 322 302 302 TRP TRP A . n 
A 1 323 GLU 323 303 303 GLU GLU A . n 
A 1 324 VAL 324 304 304 VAL VAL A . n 
A 1 325 ALA 325 305 305 ALA ALA A . n 
A 1 326 ARG 326 306 306 ARG ARG A . n 
A 1 327 ALA 327 307 307 ALA ALA A . n 
A 1 328 LEU 328 308 308 LEU LEU A . n 
A 1 329 THR 329 309 309 THR THR A . n 
A 1 330 ASP 330 310 310 ASP ASP A . n 
A 1 331 ASP 331 311 311 ASP ASP A . n 
A 1 332 LEU 332 312 312 LEU LEU A . n 
A 1 333 GLY 333 313 313 GLY GLY A . n 
A 1 334 GLU 334 314 314 GLU GLU A . n 
A 1 335 ARG 335 315 315 ARG ARG A . n 
A 1 336 ARG 336 316 316 ARG ARG A . n 
A 1 337 ARG 337 317 317 ARG ARG A . n 
A 1 338 GLN 338 318 318 GLN GLN A . n 
A 1 339 GLY 339 319 319 GLY GLY A . n 
A 1 340 HIS 340 320 320 HIS HIS A . n 
A 1 341 HIS 341 321 321 HIS HIS A . n 
A 1 342 PHE 342 322 322 PHE PHE A . n 
A 1 343 ASN 343 323 323 ASN ASN A . n 
A 1 344 LEU 344 324 324 LEU LEU A . n 
A 1 345 VAL 345 325 325 VAL VAL A . n 
A 1 346 THR 346 326 326 THR THR A . n 
A 1 347 LEU 347 327 327 LEU LEU A . n 
A 1 348 VAL 348 328 328 VAL VAL A . n 
A 1 349 ALA 349 329 329 ALA ALA A . n 
A 1 350 SER 350 330 330 SER SER A . n 
A 1 351 ALA 351 331 331 ALA ALA A . n 
A 1 352 ALA 352 332 332 ALA ALA A . n 
A 1 353 PRO 353 333 333 PRO PRO A . n 
A 1 354 ARG 354 334 334 ARG ARG A . n 
A 1 355 CYS 355 335 335 CYS CYS A . n 
A 1 356 MET 356 336 336 MET MET A . n 
A 1 357 ALA 357 337 337 ALA ALA A . n 
A 1 358 ASP 358 338 338 ASP ASP A . n 
A 1 359 ALA 359 339 339 ALA ALA A . n 
A 1 360 ARG 360 340 340 ARG ARG A . n 
A 1 361 PRO 361 341 341 PRO PRO A . n 
A 1 362 PHE 362 342 342 PHE PHE A . n 
A 1 363 MET 363 343 343 MET MET A . n 
A 1 364 ALA 364 344 344 ALA ALA A . n 
A 1 365 PHE 365 345 345 PHE PHE A . n 
A 1 366 MET 366 346 346 MET MET A . n 
A 1 367 GLU 367 347 347 GLU GLU A . n 
A 1 368 ALA 368 348 348 ALA ALA A . n 
A 1 369 GLU 369 349 349 GLU GLU A . n 
A 1 370 GLY 370 350 350 GLY GLY A . n 
A 1 371 PRO 371 351 351 PRO PRO A . n 
A 1 372 ILE 372 352 352 ILE ILE A . n 
A 1 373 ASN 373 353 353 ASN ASN A . n 
A 1 374 LEU 374 354 354 LEU LEU A . n 
A 1 375 CYS 375 355 355 CYS CYS A . n 
A 1 376 SER 376 356 356 SER SER A . n 
A 1 377 SER 377 357 357 SER SER A . n 
A 1 378 ASN 378 358 358 ASN ASN A . n 
A 1 379 ILE 379 359 359 ILE ILE A . n 
A 1 380 GLY 380 360 360 GLY GLY A . n 
A 1 381 ARG 381 361 361 ARG ARG A . n 
A 1 382 TYR 382 362 362 TYR TYR A . n 
A 1 383 PRO 383 363 363 PRO PRO A . n 
A 1 384 PHE 384 364 364 PHE PHE A . n 
A 1 385 PRO 385 365 365 PRO PRO A . n 
A 1 386 GLU 386 366 366 GLU GLU A . n 
A 1 387 ARG 387 367 367 ARG ARG A . n 
A 1 388 ILE 388 368 368 ILE ILE A . n 
A 1 389 GLY 389 369 369 GLY GLY A . n 
A 1 390 ALA 390 370 370 ALA ALA A . n 
A 1 391 LEU 391 371 371 LEU LEU A . n 
A 1 392 ARG 392 372 372 ARG ARG A . n 
A 1 393 LEU 393 373 373 LEU LEU A . n 
A 1 394 SER 394 374 374 SER SER A . n 
A 1 395 ASP 395 375 375 ASP ASP A . n 
A 1 396 ALA 396 376 376 ALA ALA A . n 
A 1 397 GLN 397 377 377 GLN GLN A . n 
A 1 398 PHE 398 378 378 PHE PHE A . n 
A 1 399 LEU 399 379 379 LEU LEU A . n 
A 1 400 THR 400 380 380 THR THR A . n 
A 1 401 GLY 401 381 381 GLY GLY A . n 
A 1 402 ILE 402 382 382 ILE ILE A . n 
A 1 403 SER 403 383 383 SER SER A . n 
A 1 404 VAL 404 384 384 VAL VAL A . n 
A 1 405 ASN 405 385 385 ASN ASN A . n 
A 1 406 GLY 406 386 386 GLY GLY A . n 
A 1 407 TYR 407 387 387 TYR TYR A . n 
A 1 408 PHE 408 388 388 PHE PHE A . n 
A 1 409 VAL 409 389 389 VAL VAL A . n 
A 1 410 ALA 410 390 390 ALA ALA A . n 
A 1 411 ALA 411 391 391 ALA ALA A . n 
A 1 412 ILE 412 392 392 ILE ILE A . n 
A 1 413 ASN 413 393 393 ASN ASN A . n 
A 1 414 SER 414 394 394 SER SER A . n 
A 1 415 SER 415 395 395 SER SER A . n 
A 1 416 HIS 416 396 396 HIS HIS A . n 
A 1 417 GLY 417 397 397 GLY GLY A . n 
A 1 418 ARG 418 398 398 ARG ARG A . n 
A 1 419 LEU 419 399 399 LEU LEU A . n 
A 1 420 PHE 420 400 400 PHE PHE A . n 
A 1 421 TRP 421 401 401 TRP TRP A . n 
A 1 422 ASN 422 402 402 ASN ASN A . n 
A 1 423 PHE 423 403 403 PHE PHE A . n 
A 1 424 THR 424 404 404 THR THR A . n 
A 1 425 TYR 425 405 405 TYR TYR A . n 
A 1 426 ILE 426 406 406 ILE ILE A . n 
A 1 427 ASP 427 407 407 ASP ASP A . n 
A 1 428 GLU 428 408 408 GLU GLU A . n 
A 1 429 ALA 429 409 409 ALA ALA A . n 
A 1 430 VAL 430 410 410 VAL VAL A . n 
A 1 431 PRO 431 411 411 PRO PRO A . n 
A 1 432 GLY 432 412 412 GLY GLY A . n 
A 1 433 GLU 433 413 413 GLU GLU A . n 
A 1 434 ARG 434 414 414 ARG ARG A . n 
A 1 435 ALA 435 415 415 ALA ALA A . n 
A 1 436 GLU 436 416 416 GLU GLU A . n 
A 1 437 ARG 437 417 417 ARG ARG A . n 
A 1 438 LEU 438 418 418 LEU LEU A . n 
A 1 439 ALA 439 419 419 ALA ALA A . n 
A 1 440 GLU 440 420 420 GLU GLU A . n 
A 1 441 ASP 441 421 421 ASP ASP A . n 
A 1 442 CYS 442 422 422 CYS CYS A . n 
A 1 443 LEU 443 423 423 LEU LEU A . n 
A 1 444 GLY 444 424 424 GLY GLY A . n 
A 1 445 THR 445 425 425 THR THR A . n 
A 1 446 LEU 446 426 426 LEU LEU A . n 
A 1 447 LEU 447 427 427 LEU LEU A . n 
A 1 448 SER 448 428 428 SER SER A . n 
A 1 449 ALA 449 429 429 ALA ALA A . n 
A 1 450 ILE 450 430 430 ILE ILE A . n 
A 1 451 HIS 451 431 431 HIS HIS A . n 
A 1 452 ALA 452 432 432 ALA ALA A . n 
A 1 453 PRO 453 433 433 PRO PRO A . n 
A 1 454 GLN 454 434 434 GLN GLN A . n 
A 1 455 ARG 455 435 ?   ?   ?   A . n 
A 1 456 SER 456 436 ?   ?   ?   A . n 
A 1 457 ALA 457 437 ?   ?   ?   A . n 
A 1 458 LEU 458 438 ?   ?   ?   A . n 
A 1 459 GLU 459 439 ?   ?   ?   A . n 
A 1 460 GLU 460 440 ?   ?   ?   A . n 
A 1 461 GLN 461 441 ?   ?   ?   A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 GOL 1   501 505 GOL GOL A . 
C 2 GOL 1   502 513 GOL GOL A . 
D 3 HOH 1   601 75  HOH HOH A . 
D 3 HOH 2   602 276 HOH HOH A . 
D 3 HOH 3   603 255 HOH HOH A . 
D 3 HOH 4   604 180 HOH HOH A . 
D 3 HOH 5   605 187 HOH HOH A . 
D 3 HOH 6   606 207 HOH HOH A . 
D 3 HOH 7   607 233 HOH HOH A . 
D 3 HOH 8   608 303 HOH HOH A . 
D 3 HOH 9   609 259 HOH HOH A . 
D 3 HOH 10  610 138 HOH HOH A . 
D 3 HOH 11  611 194 HOH HOH A . 
D 3 HOH 12  612 256 HOH HOH A . 
D 3 HOH 13  613 45  HOH HOH A . 
D 3 HOH 14  614 230 HOH HOH A . 
D 3 HOH 15  615 91  HOH HOH A . 
D 3 HOH 16  616 238 HOH HOH A . 
D 3 HOH 17  617 197 HOH HOH A . 
D 3 HOH 18  618 339 HOH HOH A . 
D 3 HOH 19  619 304 HOH HOH A . 
D 3 HOH 20  620 231 HOH HOH A . 
D 3 HOH 21  621 34  HOH HOH A . 
D 3 HOH 22  622 257 HOH HOH A . 
D 3 HOH 23  623 122 HOH HOH A . 
D 3 HOH 24  624 206 HOH HOH A . 
D 3 HOH 25  625 327 HOH HOH A . 
D 3 HOH 26  626 217 HOH HOH A . 
D 3 HOH 27  627 15  HOH HOH A . 
D 3 HOH 28  628 201 HOH HOH A . 
D 3 HOH 29  629 10  HOH HOH A . 
D 3 HOH 30  630 281 HOH HOH A . 
D 3 HOH 31  631 27  HOH HOH A . 
D 3 HOH 32  632 129 HOH HOH A . 
D 3 HOH 33  633 12  HOH HOH A . 
D 3 HOH 34  634 227 HOH HOH A . 
D 3 HOH 35  635 176 HOH HOH A . 
D 3 HOH 36  636 5   HOH HOH A . 
D 3 HOH 37  637 88  HOH HOH A . 
D 3 HOH 38  638 258 HOH HOH A . 
D 3 HOH 39  639 218 HOH HOH A . 
D 3 HOH 40  640 85  HOH HOH A . 
D 3 HOH 41  641 59  HOH HOH A . 
D 3 HOH 42  642 155 HOH HOH A . 
D 3 HOH 43  643 263 HOH HOH A . 
D 3 HOH 44  644 71  HOH HOH A . 
D 3 HOH 45  645 28  HOH HOH A . 
D 3 HOH 46  646 293 HOH HOH A . 
D 3 HOH 47  647 188 HOH HOH A . 
D 3 HOH 48  648 279 HOH HOH A . 
D 3 HOH 49  649 48  HOH HOH A . 
D 3 HOH 50  650 76  HOH HOH A . 
D 3 HOH 51  651 14  HOH HOH A . 
D 3 HOH 52  652 46  HOH HOH A . 
D 3 HOH 53  653 127 HOH HOH A . 
D 3 HOH 54  654 23  HOH HOH A . 
D 3 HOH 55  655 192 HOH HOH A . 
D 3 HOH 56  656 22  HOH HOH A . 
D 3 HOH 57  657 52  HOH HOH A . 
D 3 HOH 58  658 19  HOH HOH A . 
D 3 HOH 59  659 174 HOH HOH A . 
D 3 HOH 60  660 62  HOH HOH A . 
D 3 HOH 61  661 116 HOH HOH A . 
D 3 HOH 62  662 275 HOH HOH A . 
D 3 HOH 63  663 323 HOH HOH A . 
D 3 HOH 64  664 132 HOH HOH A . 
D 3 HOH 65  665 84  HOH HOH A . 
D 3 HOH 66  666 124 HOH HOH A . 
D 3 HOH 67  667 189 HOH HOH A . 
D 3 HOH 68  668 317 HOH HOH A . 
D 3 HOH 69  669 89  HOH HOH A . 
D 3 HOH 70  670 300 HOH HOH A . 
D 3 HOH 71  671 96  HOH HOH A . 
D 3 HOH 72  672 61  HOH HOH A . 
D 3 HOH 73  673 66  HOH HOH A . 
D 3 HOH 74  674 179 HOH HOH A . 
D 3 HOH 75  675 26  HOH HOH A . 
D 3 HOH 76  676 223 HOH HOH A . 
D 3 HOH 77  677 21  HOH HOH A . 
D 3 HOH 78  678 183 HOH HOH A . 
D 3 HOH 79  679 31  HOH HOH A . 
D 3 HOH 80  680 216 HOH HOH A . 
D 3 HOH 81  681 149 HOH HOH A . 
D 3 HOH 82  682 193 HOH HOH A . 
D 3 HOH 83  683 134 HOH HOH A . 
D 3 HOH 84  684 247 HOH HOH A . 
D 3 HOH 85  685 236 HOH HOH A . 
D 3 HOH 86  686 312 HOH HOH A . 
D 3 HOH 87  687 177 HOH HOH A . 
D 3 HOH 88  688 150 HOH HOH A . 
D 3 HOH 89  689 30  HOH HOH A . 
D 3 HOH 90  690 140 HOH HOH A . 
D 3 HOH 91  691 8   HOH HOH A . 
D 3 HOH 92  692 237 HOH HOH A . 
D 3 HOH 93  693 32  HOH HOH A . 
D 3 HOH 94  694 35  HOH HOH A . 
D 3 HOH 95  695 50  HOH HOH A . 
D 3 HOH 96  696 113 HOH HOH A . 
D 3 HOH 97  697 86  HOH HOH A . 
D 3 HOH 98  698 297 HOH HOH A . 
D 3 HOH 99  699 229 HOH HOH A . 
D 3 HOH 100 700 65  HOH HOH A . 
D 3 HOH 101 701 13  HOH HOH A . 
D 3 HOH 102 702 200 HOH HOH A . 
D 3 HOH 103 703 102 HOH HOH A . 
D 3 HOH 104 704 73  HOH HOH A . 
D 3 HOH 105 705 228 HOH HOH A . 
D 3 HOH 106 706 168 HOH HOH A . 
D 3 HOH 107 707 16  HOH HOH A . 
D 3 HOH 108 708 169 HOH HOH A . 
D 3 HOH 109 709 171 HOH HOH A . 
D 3 HOH 110 710 90  HOH HOH A . 
D 3 HOH 111 711 250 HOH HOH A . 
D 3 HOH 112 712 68  HOH HOH A . 
D 3 HOH 113 713 151 HOH HOH A . 
D 3 HOH 114 714 221 HOH HOH A . 
D 3 HOH 115 715 41  HOH HOH A . 
D 3 HOH 116 716 77  HOH HOH A . 
D 3 HOH 117 717 57  HOH HOH A . 
D 3 HOH 118 718 190 HOH HOH A . 
D 3 HOH 119 719 252 HOH HOH A . 
D 3 HOH 120 720 104 HOH HOH A . 
D 3 HOH 121 721 186 HOH HOH A . 
D 3 HOH 122 722 239 HOH HOH A . 
D 3 HOH 123 723 313 HOH HOH A . 
D 3 HOH 124 724 121 HOH HOH A . 
D 3 HOH 125 725 283 HOH HOH A . 
D 3 HOH 126 726 87  HOH HOH A . 
D 3 HOH 127 727 69  HOH HOH A . 
D 3 HOH 128 728 78  HOH HOH A . 
D 3 HOH 129 729 33  HOH HOH A . 
D 3 HOH 130 730 112 HOH HOH A . 
D 3 HOH 131 731 232 HOH HOH A . 
D 3 HOH 132 732 108 HOH HOH A . 
D 3 HOH 133 733 215 HOH HOH A . 
D 3 HOH 134 734 55  HOH HOH A . 
D 3 HOH 135 735 125 HOH HOH A . 
D 3 HOH 136 736 244 HOH HOH A . 
D 3 HOH 137 737 120 HOH HOH A . 
D 3 HOH 138 738 60  HOH HOH A . 
D 3 HOH 139 739 141 HOH HOH A . 
D 3 HOH 140 740 74  HOH HOH A . 
D 3 HOH 141 741 181 HOH HOH A . 
D 3 HOH 142 742 115 HOH HOH A . 
D 3 HOH 143 743 1   HOH HOH A . 
D 3 HOH 144 744 191 HOH HOH A . 
D 3 HOH 145 745 154 HOH HOH A . 
D 3 HOH 146 746 63  HOH HOH A . 
D 3 HOH 147 747 161 HOH HOH A . 
D 3 HOH 148 748 164 HOH HOH A . 
D 3 HOH 149 749 80  HOH HOH A . 
D 3 HOH 150 750 220 HOH HOH A . 
D 3 HOH 151 751 72  HOH HOH A . 
D 3 HOH 152 752 136 HOH HOH A . 
D 3 HOH 153 753 211 HOH HOH A . 
D 3 HOH 154 754 29  HOH HOH A . 
D 3 HOH 155 755 54  HOH HOH A . 
D 3 HOH 156 756 307 HOH HOH A . 
D 3 HOH 157 757 92  HOH HOH A . 
D 3 HOH 158 758 4   HOH HOH A . 
D 3 HOH 159 759 128 HOH HOH A . 
D 3 HOH 160 760 160 HOH HOH A . 
D 3 HOH 161 761 97  HOH HOH A . 
D 3 HOH 162 762 170 HOH HOH A . 
D 3 HOH 163 763 278 HOH HOH A . 
D 3 HOH 164 764 64  HOH HOH A . 
D 3 HOH 165 765 203 HOH HOH A . 
D 3 HOH 166 766 53  HOH HOH A . 
D 3 HOH 167 767 123 HOH HOH A . 
D 3 HOH 168 768 105 HOH HOH A . 
D 3 HOH 169 769 126 HOH HOH A . 
D 3 HOH 170 770 159 HOH HOH A . 
D 3 HOH 171 771 172 HOH HOH A . 
D 3 HOH 172 772 167 HOH HOH A . 
D 3 HOH 173 773 36  HOH HOH A . 
D 3 HOH 174 774 2   HOH HOH A . 
D 3 HOH 175 775 7   HOH HOH A . 
D 3 HOH 176 776 93  HOH HOH A . 
D 3 HOH 177 777 219 HOH HOH A . 
D 3 HOH 178 778 17  HOH HOH A . 
D 3 HOH 179 779 328 HOH HOH A . 
D 3 HOH 180 780 139 HOH HOH A . 
D 3 HOH 181 781 166 HOH HOH A . 
D 3 HOH 182 782 111 HOH HOH A . 
D 3 HOH 183 783 208 HOH HOH A . 
D 3 HOH 184 784 184 HOH HOH A . 
D 3 HOH 185 785 9   HOH HOH A . 
D 3 HOH 186 786 144 HOH HOH A . 
D 3 HOH 187 787 214 HOH HOH A . 
D 3 HOH 188 788 178 HOH HOH A . 
D 3 HOH 189 789 81  HOH HOH A . 
D 3 HOH 190 790 309 HOH HOH A . 
D 3 HOH 191 791 47  HOH HOH A . 
D 3 HOH 192 792 58  HOH HOH A . 
D 3 HOH 193 793 282 HOH HOH A . 
D 3 HOH 194 794 20  HOH HOH A . 
D 3 HOH 195 795 242 HOH HOH A . 
D 3 HOH 196 796 114 HOH HOH A . 
D 3 HOH 197 797 162 HOH HOH A . 
D 3 HOH 198 798 25  HOH HOH A . 
D 3 HOH 199 799 334 HOH HOH A . 
D 3 HOH 200 800 37  HOH HOH A . 
D 3 HOH 201 801 94  HOH HOH A . 
D 3 HOH 202 802 133 HOH HOH A . 
D 3 HOH 203 803 165 HOH HOH A . 
D 3 HOH 204 804 248 HOH HOH A . 
D 3 HOH 205 805 6   HOH HOH A . 
D 3 HOH 206 806 205 HOH HOH A . 
D 3 HOH 207 807 157 HOH HOH A . 
D 3 HOH 208 808 106 HOH HOH A . 
D 3 HOH 209 809 24  HOH HOH A . 
D 3 HOH 210 810 67  HOH HOH A . 
D 3 HOH 211 811 42  HOH HOH A . 
D 3 HOH 212 812 196 HOH HOH A . 
D 3 HOH 213 813 83  HOH HOH A . 
D 3 HOH 214 814 251 HOH HOH A . 
D 3 HOH 215 815 43  HOH HOH A . 
D 3 HOH 216 816 44  HOH HOH A . 
D 3 HOH 217 817 246 HOH HOH A . 
D 3 HOH 218 818 110 HOH HOH A . 
D 3 HOH 219 819 135 HOH HOH A . 
D 3 HOH 220 820 51  HOH HOH A . 
D 3 HOH 221 821 145 HOH HOH A . 
D 3 HOH 222 822 38  HOH HOH A . 
D 3 HOH 223 823 163 HOH HOH A . 
D 3 HOH 224 824 56  HOH HOH A . 
D 3 HOH 225 825 118 HOH HOH A . 
D 3 HOH 226 826 243 HOH HOH A . 
D 3 HOH 227 827 254 HOH HOH A . 
D 3 HOH 228 828 3   HOH HOH A . 
D 3 HOH 229 829 274 HOH HOH A . 
D 3 HOH 230 830 18  HOH HOH A . 
D 3 HOH 231 831 107 HOH HOH A . 
D 3 HOH 232 832 156 HOH HOH A . 
D 3 HOH 233 833 182 HOH HOH A . 
D 3 HOH 234 834 280 HOH HOH A . 
D 3 HOH 235 835 175 HOH HOH A . 
D 3 HOH 236 836 316 HOH HOH A . 
D 3 HOH 237 837 130 HOH HOH A . 
D 3 HOH 238 838 173 HOH HOH A . 
D 3 HOH 239 839 98  HOH HOH A . 
D 3 HOH 240 840 49  HOH HOH A . 
D 3 HOH 241 841 109 HOH HOH A . 
D 3 HOH 242 842 330 HOH HOH A . 
D 3 HOH 243 843 40  HOH HOH A . 
D 3 HOH 244 844 11  HOH HOH A . 
D 3 HOH 245 845 240 HOH HOH A . 
D 3 HOH 246 846 253 HOH HOH A . 
D 3 HOH 247 847 234 HOH HOH A . 
D 3 HOH 248 848 204 HOH HOH A . 
D 3 HOH 249 849 202 HOH HOH A . 
D 3 HOH 250 850 245 HOH HOH A . 
D 3 HOH 251 851 235 HOH HOH A . 
D 3 HOH 252 852 210 HOH HOH A . 
D 3 HOH 253 853 241 HOH HOH A . 
D 3 HOH 254 854 315 HOH HOH A . 
D 3 HOH 255 855 152 HOH HOH A . 
D 3 HOH 256 856 295 HOH HOH A . 
D 3 HOH 257 857 273 HOH HOH A . 
D 3 HOH 258 858 70  HOH HOH A . 
D 3 HOH 259 859 331 HOH HOH A . 
D 3 HOH 260 860 322 HOH HOH A . 
D 3 HOH 261 861 289 HOH HOH A . 
D 3 HOH 262 862 337 HOH HOH A . 
D 3 HOH 263 863 158 HOH HOH A . 
D 3 HOH 264 864 324 HOH HOH A . 
D 3 HOH 265 865 147 HOH HOH A . 
D 3 HOH 266 866 195 HOH HOH A . 
D 3 HOH 267 867 119 HOH HOH A . 
D 3 HOH 268 868 153 HOH HOH A . 
D 3 HOH 269 869 287 HOH HOH A . 
D 3 HOH 270 870 302 HOH HOH A . 
D 3 HOH 271 871 199 HOH HOH A . 
D 3 HOH 272 872 277 HOH HOH A . 
D 3 HOH 273 873 100 HOH HOH A . 
D 3 HOH 274 874 306 HOH HOH A . 
D 3 HOH 275 875 213 HOH HOH A . 
D 3 HOH 276 876 338 HOH HOH A . 
D 3 HOH 277 877 267 HOH HOH A . 
D 3 HOH 278 878 185 HOH HOH A . 
D 3 HOH 279 879 332 HOH HOH A . 
D 3 HOH 280 880 286 HOH HOH A . 
D 3 HOH 281 881 305 HOH HOH A . 
D 3 HOH 282 882 143 HOH HOH A . 
D 3 HOH 283 883 299 HOH HOH A . 
D 3 HOH 284 884 95  HOH HOH A . 
D 3 HOH 285 885 329 HOH HOH A . 
D 3 HOH 286 886 264 HOH HOH A . 
D 3 HOH 287 887 319 HOH HOH A . 
D 3 HOH 288 888 325 HOH HOH A . 
D 3 HOH 289 889 314 HOH HOH A . 
D 3 HOH 290 890 268 HOH HOH A . 
D 3 HOH 291 891 333 HOH HOH A . 
D 3 HOH 292 892 291 HOH HOH A . 
D 3 HOH 293 893 336 HOH HOH A . 
D 3 HOH 294 894 335 HOH HOH A . 
D 3 HOH 295 895 311 HOH HOH A . 
D 3 HOH 296 896 212 HOH HOH A . 
D 3 HOH 297 897 142 HOH HOH A . 
D 3 HOH 298 898 290 HOH HOH A . 
D 3 HOH 299 899 224 HOH HOH A . 
D 3 HOH 300 900 296 HOH HOH A . 
D 3 HOH 301 901 262 HOH HOH A . 
D 3 HOH 302 902 39  HOH HOH A . 
D 3 HOH 303 903 82  HOH HOH A . 
D 3 HOH 304 904 137 HOH HOH A . 
D 3 HOH 305 905 318 HOH HOH A . 
D 3 HOH 306 906 222 HOH HOH A . 
D 3 HOH 307 907 285 HOH HOH A . 
D 3 HOH 308 908 101 HOH HOH A . 
D 3 HOH 309 909 292 HOH HOH A . 
D 3 HOH 310 910 269 HOH HOH A . 
D 3 HOH 311 911 260 HOH HOH A . 
D 3 HOH 312 912 146 HOH HOH A . 
D 3 HOH 313 913 326 HOH HOH A . 
D 3 HOH 314 914 284 HOH HOH A . 
D 3 HOH 315 915 320 HOH HOH A . 
D 3 HOH 316 916 294 HOH HOH A . 
D 3 HOH 317 917 209 HOH HOH A . 
D 3 HOH 318 918 308 HOH HOH A . 
D 3 HOH 319 919 198 HOH HOH A . 
D 3 HOH 320 920 131 HOH HOH A . 
D 3 HOH 321 921 265 HOH HOH A . 
D 3 HOH 322 922 288 HOH HOH A . 
D 3 HOH 323 923 117 HOH HOH A . 
D 3 HOH 324 924 298 HOH HOH A . 
D 3 HOH 325 925 103 HOH HOH A . 
D 3 HOH 326 926 148 HOH HOH A . 
D 3 HOH 327 927 99  HOH HOH A . 
D 3 HOH 328 928 79  HOH HOH A . 
D 3 HOH 329 929 301 HOH HOH A . 
D 3 HOH 330 930 340 HOH HOH A . 
D 3 HOH 331 931 271 HOH HOH A . 
D 3 HOH 332 932 272 HOH HOH A . 
D 3 HOH 333 933 261 HOH HOH A . 
D 3 HOH 334 934 270 HOH HOH A . 
D 3 HOH 335 935 310 HOH HOH A . 
D 3 HOH 336 936 249 HOH HOH A . 
D 3 HOH 337 937 225 HOH HOH A . 
D 3 HOH 338 938 266 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 0 A ARG 91  ? NH1 ? A ARG 111 NH1 
2  1 Y 0 A ARG 171 ? CG  ? A ARG 191 CG  
3  1 Y 0 A ARG 171 ? CD  ? A ARG 191 CD  
4  1 Y 0 A ARG 171 ? NE  ? A ARG 191 NE  
5  1 Y 0 A ARG 171 ? CZ  ? A ARG 191 CZ  
6  1 Y 0 A ARG 171 ? NH1 ? A ARG 191 NH1 
7  1 Y 0 A ARG 171 ? NH2 ? A ARG 191 NH2 
8  1 Y 0 A ARG 334 ? CD  ? A ARG 354 CD  
9  1 Y 0 A ARG 334 ? NE  ? A ARG 354 NE  
10 1 Y 0 A ARG 334 ? CZ  ? A ARG 354 CZ  
11 1 Y 0 A ARG 334 ? NH1 ? A ARG 354 NH1 
12 1 Y 0 A ARG 334 ? NH2 ? A ARG 354 NH2 
13 1 Y 0 A GLU 349 ? OE2 ? A GLU 369 OE2 
14 1 Y 0 A ARG 367 ? NH2 ? A ARG 387 NH2 
15 1 Y 0 A GLU 413 ? CD  ? A GLU 433 CD  
16 1 Y 0 A GLU 413 ? OE1 ? A GLU 433 OE1 
17 1 Y 0 A GLU 413 ? OE2 ? A GLU 433 OE2 
18 1 Y 0 A GLN 434 ? CG  ? A GLN 454 CG  
19 1 Y 0 A GLN 434 ? CD  ? A GLN 454 CD  
20 1 Y 0 A GLN 434 ? OE1 ? A GLN 454 OE1 
21 1 Y 0 A GLN 434 ? NE2 ? A GLN 454 NE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0405 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .        4 
# 
_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                     8S6L 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     56.460 
_cell.length_a_esd                 ? 
_cell.length_b                     67.590 
_cell.length_b_esd                 ? 
_cell.length_c                     116.680 
_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                         8S6L 
_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                   8S6L 
_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             2.17 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.38 
_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              6.5 
_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    '100 mM bis-Tris methane at pH 6.5 and 25% PEG-3350' 
_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 EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-04-12 
_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                    channel-cut 
_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   0.980112 
_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                        'SOLEIL BEAMLINE PROXIMA 2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.980112 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'PROXIMA 2' 
_diffrn_source.pdbx_synchrotron_site       SOLEIL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8S6L 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.55 
_reflns.d_resolution_low                               44.20 
_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                                     65281 
_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                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          20.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.90 
_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                                0.067 
_reflns.pdbx_Rpim_I_all                                0.019 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.064 
_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                                    1.55 
_reflns_shell.d_res_low                                     1.59 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           63708 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4701 
_reflns_shell.percent_possible_obs                          98.7 
_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                               13.6 
_reflns_shell.pdbx_chi_squared                              0.58 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.9 
_reflns_shell.pdbx_Rrim_I_all                               1.122 
_reflns_shell.pdbx_Rpim_I_all                               0.303 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.769 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.079 
_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]                            -3.22 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            4.01 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.78 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               24.346 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.976 
_refine.correlation_coeff_Fo_to_Fc_free          0.959 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 8S6L 
_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                            1.55 
_refine.ls_d_res_low                             44.20 
_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                     61945 
_refine.ls_number_reflns_R_free                  3261 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.86 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.14808 
_refine.ls_R_factor_R_free                       0.19447 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.14568 
_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                    MASK 
_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                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.085 
_refine.pdbx_overall_ESU_R_Free                  0.076 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             4.079 
_refine.overall_SU_ML                            0.062 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.55 
_refine_hist.d_res_low                        44.20 
_refine_hist.number_atoms_solvent             340 
_refine_hist.number_atoms_total               3745 
_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        3393 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         12 
_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  0.012  3546 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  3347 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.467  1.656  4841 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.523  1.570  7670 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.254  5.000  450  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 8.404  5.000  50   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 12.850 10.000 548  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.077  0.200  532  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  4395 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  869  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.744  2.419  1769 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.744  2.421  1770 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.323  4.358  2223 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.324  4.360  2224 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 1.969  2.784  1777 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.968  2.784  1778 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.649  4.948  2617 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.454  25.09  3849 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 3.279  24.25  3786 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? 3.778  3.000  6893 ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.552 
_refine_ls_shell.d_res_low                        1.593 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             234 
_refine_ls_shell.number_reflns_R_work             4447 
_refine_ls_shell.percent_reflns_obs               98.63 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.348 
_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   20 
_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                  0.408 
# 
_struct.entry_id                     8S6L 
_struct.title                        'AzeD dehydratase of Pseudomonas aeruginosa' 
_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        8S6L 
_struct_keywords.text            
'dehydratase, post-NRPS enzyme, tailoring enzyme, azetidomonamide dehydratase, BIOSYNTHETIC PROTEIN' 
_struct_keywords.pdbx_keywords   'BIOSYNTHETIC PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q9HYR6_PSEAE 
_struct_ref.pdbx_db_accession          Q9HYR6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MAEIRRPLSAVERWYWLSDQFSALNVISRVRVHGRLSIDDLRRGLDALQARHPLLRARIEHDAGLDPRWVPCERPIPLRE
VRGGGEEQWLREINERELPERIDPDSGPLIRTVAIATDAGAHDLLVVVPHIIADGTTVLTLAEQWLTLAADPAAQPWTAS
ALPPAEDLRPRRFTGDEGAARLAEQTAQDEALVGRHRPGRIEPSNPVPLEARRTRLLHRELDGAQLEQLQRRAREHGTTV
HGALTAALAIAAGHDHQRRPSHIAIGSPIDFRDELEPPVRPDEVGTYVATVPVVLDIARPFWEVARALTDDLGERRRQGH
HFNLVTLVASAAPRCMADARPFMAFMEAEGPINLCSSNIGRYPFPERIGALRLSDAQFLTGISVNGYFVAAINSSHGRLF
WNFTYIDEAVPGERAERLAEDCLGTLLSAIHAPQRSALEEQ
;
_struct_ref.pdbx_align_begin           2 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8S6L 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 21 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 461 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9HYR6 
_struct_ref_seq.db_align_beg                  2 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  442 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       441 
# 
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 8S6L MET A 1  ? UNP Q9HYR6 ? ? 'initiating methionine' -19 1  
1 8S6L GLY A 2  ? UNP Q9HYR6 ? ? 'expression tag'        -18 2  
1 8S6L SER A 3  ? UNP Q9HYR6 ? ? 'expression tag'        -17 3  
1 8S6L SER A 4  ? UNP Q9HYR6 ? ? 'expression tag'        -16 4  
1 8S6L HIS A 5  ? UNP Q9HYR6 ? ? 'expression tag'        -15 5  
1 8S6L HIS A 6  ? UNP Q9HYR6 ? ? 'expression tag'        -14 6  
1 8S6L HIS A 7  ? UNP Q9HYR6 ? ? 'expression tag'        -13 7  
1 8S6L HIS A 8  ? UNP Q9HYR6 ? ? 'expression tag'        -12 8  
1 8S6L HIS A 9  ? UNP Q9HYR6 ? ? 'expression tag'        -11 9  
1 8S6L HIS A 10 ? UNP Q9HYR6 ? ? 'expression tag'        -10 10 
1 8S6L SER A 11 ? UNP Q9HYR6 ? ? 'expression tag'        -9  11 
1 8S6L SER A 12 ? UNP Q9HYR6 ? ? 'expression tag'        -8  12 
1 8S6L GLY A 13 ? UNP Q9HYR6 ? ? 'expression tag'        -7  13 
1 8S6L LEU A 14 ? UNP Q9HYR6 ? ? 'expression tag'        -6  14 
1 8S6L VAL A 15 ? UNP Q9HYR6 ? ? 'expression tag'        -5  15 
1 8S6L PRO A 16 ? UNP Q9HYR6 ? ? 'expression tag'        -4  16 
1 8S6L ARG A 17 ? UNP Q9HYR6 ? ? 'expression tag'        -3  17 
1 8S6L GLY A 18 ? UNP Q9HYR6 ? ? 'expression tag'        -2  18 
1 8S6L SER A 19 ? UNP Q9HYR6 ? ? 'expression tag'        -1  19 
1 8S6L HIS A 20 ? UNP Q9HYR6 ? ? 'expression tag'        0   20 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
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)' 560   ? 
1 MORE         -2    ? 
1 'SSA (A^2)'  17670 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   SAXS 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 29  ? SER A 42  ? SER A 9   SER A 22  1 ? 14 
HELX_P HELX_P2  AA2 SER A 57  ? ARG A 71  ? SER A 37  ARG A 51  1 ? 15 
HELX_P HELX_P3  AA3 PRO A 73  ? LEU A 75  ? PRO A 53  LEU A 55  5 ? 3  
HELX_P HELX_P4  AA4 GLU A 107 ? ARG A 116 ? GLU A 87  ARG A 96  1 ? 10 
HELX_P HELX_P5  AA6 GLY A 155 ? ALA A 170 ? GLY A 135 ALA A 150 1 ? 16 
HELX_P HELX_P6  AA7 ALA A 185 ? LEU A 188 ? ALA A 165 LEU A 168 5 ? 4  
HELX_P HELX_P7  AA9 ASP A 196 ? ARG A 217 ? ASP A 176 ARG A 197 1 ? 22 
HELX_P HELX_P8  AB1 PRO A 228 ? ARG A 232 ? PRO A 208 ARG A 212 5 ? 5  
HELX_P HELX_P9  AB2 GLY A 243 ? HIS A 256 ? GLY A 223 HIS A 236 1 ? 14 
HELX_P HELX_P10 AB3 VAL A 260 ? HIS A 276 ? VAL A 240 HIS A 256 1 ? 17 
HELX_P HELX_P11 AB4 ARG A 292 ? LEU A 295 ? ARG A 272 LEU A 275 5 ? 4  
HELX_P HELX_P12 AB5 PHE A 321 ? GLN A 338 ? PHE A 301 GLN A 318 1 ? 18 
HELX_P HELX_P13 AB6 HIS A 340 ? ALA A 352 ? HIS A 320 ALA A 332 1 ? 13 
HELX_P HELX_P14 AB7 CYS A 355 ? ASP A 358 ? CYS A 335 ASP A 338 5 ? 4  
HELX_P HELX_P15 AB8 ALA A 359 ? GLU A 369 ? ALA A 339 GLU A 349 1 ? 11 
HELX_P HELX_P16 AB9 PRO A 431 ? HIS A 451 ? PRO A 411 HIS A 431 1 ? 21 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLY 127 A . ? GLY 107 A PRO 128 A ? PRO 108 A 1 -1.01 
2 GLU 296 A . ? GLU 276 A PRO 297 A ? PRO 277 A 1 -5.05 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 6 ? 
AA3 ? 4 ? 
AA4 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? parallel      
AA4 1 2 ? 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 ARG A 88  ? PRO A 91  ? ARG A 68  PRO A 71  
AA1 2 ALA A 77  ? GLU A 80  ? ALA A 57  GLU A 60  
AA2 1 LEU A 98  ? ARG A 102 ? LEU A 78  ARG A 82  
AA2 2 ARG A 131 ? ALA A 136 ? ARG A 111 ALA A 116 
AA2 3 HIS A 142 ? PRO A 149 ? HIS A 122 PRO A 129 
AA2 4 ASN A 45  ? HIS A 53  ? ASN A 25  HIS A 33  
AA2 5 ARG A 392 ? SER A 394 ? ARG A 372 SER A 374 
AA2 6 GLN A 397 ? THR A 400 ? GLN A 377 THR A 380 
AA3 1 THR A 234 ? LEU A 241 ? THR A 214 LEU A 221 
AA3 2 ARG A 418 ? ILE A 426 ? ARG A 398 ILE A 406 
AA3 3 PHE A 408 ? SER A 415 ? PHE A 388 SER A 395 
AA3 4 LEU A 374 ? ASN A 378 ? LEU A 354 ASN A 358 
AA4 1 HIS A 282 ? ASP A 290 ? HIS A 262 ASP A 270 
AA4 2 VAL A 308 ? ASP A 316 ? VAL A 288 ASP A 296 
# 
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 O LEU A 85  ? O LEU A 65  N ASP A 82  ? N ASP A 62  
AA2 1 2 N VAL A 101 ? N VAL A 81  O ALA A 136 ? O ALA A 116 
AA2 2 3 N ILE A 135 ? N ILE A 115 O ASP A 143 ? O ASP A 123 
AA2 3 4 O HIS A 142 ? O HIS A 122 N VAL A 52  ? N VAL A 32  
AA2 4 5 N HIS A 53  ? N HIS A 33  O ARG A 392 ? O ARG A 372 
AA2 5 6 O LEU A 391 ? O LEU A 371 N ILE A 388 ? N ILE A 368 
AA3 1 2 N LEU A 237 ? N LEU A 217 O PHE A 423 ? O PHE A 403 
AA3 2 3 O THR A 424 ? O THR A 404 N VAL A 409 ? N VAL A 389 
AA3 3 4 O ALA A 410 ? O ALA A 390 N SER A 377 ? N SER A 357 
AA4 1 2 N ILE A 283 ? N ILE A 263 O LEU A 315 ? O LEU A 295 
# 
_pdbx_entry_details.entry_id                   8S6L 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 6   ? ? 179.58  157.87  
2 1 ARG A 96  ? ? -134.20 -44.18  
3 1 ARG A 259 ? ? 39.31   61.09   
4 1 PRO A 281 ? ? -68.14  1.10    
5 1 ALA A 298 ? ? -96.76  50.69   
6 1 SER A 383 ? ? 56.66   -139.40 
7 1 GLU A 408 ? ? 76.89   -54.04  
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 42  ? ? 0.092 'SIDE CHAIN' 
2 1 ARG A 111 ? ? 0.196 'SIDE CHAIN' 
3 1 ARG A 171 ? ? 0.143 'SIDE CHAIN' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -19 ? A MET 1   
2  1 Y 1 A GLY -18 ? A GLY 2   
3  1 Y 1 A SER -17 ? A SER 3   
4  1 Y 1 A SER -16 ? A SER 4   
5  1 Y 1 A HIS -15 ? A HIS 5   
6  1 Y 1 A HIS -14 ? A HIS 6   
7  1 Y 1 A HIS -13 ? A HIS 7   
8  1 Y 1 A HIS -12 ? A HIS 8   
9  1 Y 1 A HIS -11 ? A HIS 9   
10 1 Y 1 A HIS -10 ? A HIS 10  
11 1 Y 1 A SER -9  ? A SER 11  
12 1 Y 1 A SER -8  ? A SER 12  
13 1 Y 1 A GLY -7  ? A GLY 13  
14 1 Y 1 A LEU -6  ? A LEU 14  
15 1 Y 1 A VAL -5  ? A VAL 15  
16 1 Y 1 A PRO -4  ? A PRO 16  
17 1 Y 1 A ARG -3  ? A ARG 17  
18 1 Y 1 A GLY -2  ? A GLY 18  
19 1 Y 1 A SER -1  ? A SER 19  
20 1 Y 1 A HIS 0   ? A HIS 20  
21 1 Y 1 A MET 1   ? A MET 21  
22 1 Y 1 A ARG 435 ? A ARG 455 
23 1 Y 1 A SER 436 ? A SER 456 
24 1 Y 1 A ALA 437 ? A ALA 457 
25 1 Y 1 A LEU 438 ? A LEU 458 
26 1 Y 1 A GLU 439 ? A GLU 459 
27 1 Y 1 A GLU 440 ? A GLU 460 
28 1 Y 1 A GLN 441 ? A GLN 461 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
GOL C1   C N N 137 
GOL O1   O N N 138 
GOL C2   C N N 139 
GOL O2   O N N 140 
GOL C3   C N N 141 
GOL O3   O N N 142 
GOL H11  H N N 143 
GOL H12  H N N 144 
GOL HO1  H N N 145 
GOL H2   H N N 146 
GOL HO2  H N N 147 
GOL H31  H N N 148 
GOL H32  H N N 149 
GOL HO3  H N N 150 
HIS N    N N N 151 
HIS CA   C N S 152 
HIS C    C N N 153 
HIS O    O N N 154 
HIS CB   C N N 155 
HIS CG   C Y N 156 
HIS ND1  N Y N 157 
HIS CD2  C Y N 158 
HIS CE1  C Y N 159 
HIS NE2  N Y N 160 
HIS OXT  O N N 161 
HIS H    H N N 162 
HIS H2   H N N 163 
HIS HA   H N N 164 
HIS HB2  H N N 165 
HIS HB3  H N N 166 
HIS HD1  H N N 167 
HIS HD2  H N N 168 
HIS HE1  H N N 169 
HIS HE2  H N N 170 
HIS HXT  H N N 171 
HOH O    O N N 172 
HOH H1   H N N 173 
HOH H2   H N N 174 
ILE N    N N N 175 
ILE CA   C N S 176 
ILE C    C N N 177 
ILE O    O N N 178 
ILE CB   C N S 179 
ILE CG1  C N N 180 
ILE CG2  C N N 181 
ILE CD1  C N N 182 
ILE OXT  O N N 183 
ILE H    H N N 184 
ILE H2   H N N 185 
ILE HA   H N N 186 
ILE HB   H N N 187 
ILE HG12 H N N 188 
ILE HG13 H N N 189 
ILE HG21 H N N 190 
ILE HG22 H N N 191 
ILE HG23 H N N 192 
ILE HD11 H N N 193 
ILE HD12 H N N 194 
ILE HD13 H N N 195 
ILE HXT  H N N 196 
LEU N    N N N 197 
LEU CA   C N S 198 
LEU C    C N N 199 
LEU O    O N N 200 
LEU CB   C N N 201 
LEU CG   C N N 202 
LEU CD1  C N N 203 
LEU CD2  C N N 204 
LEU OXT  O N N 205 
LEU H    H N N 206 
LEU H2   H N N 207 
LEU HA   H N N 208 
LEU HB2  H N N 209 
LEU HB3  H N N 210 
LEU HG   H N N 211 
LEU HD11 H N N 212 
LEU HD12 H N N 213 
LEU HD13 H N N 214 
LEU HD21 H N N 215 
LEU HD22 H N N 216 
LEU HD23 H N N 217 
LEU HXT  H N N 218 
MET N    N N N 219 
MET CA   C N S 220 
MET C    C N N 221 
MET O    O N N 222 
MET CB   C N N 223 
MET CG   C N N 224 
MET SD   S N N 225 
MET CE   C N N 226 
MET OXT  O N N 227 
MET H    H N N 228 
MET H2   H N N 229 
MET HA   H N N 230 
MET HB2  H N N 231 
MET HB3  H N N 232 
MET HG2  H N N 233 
MET HG3  H N N 234 
MET HE1  H N N 235 
MET HE2  H N N 236 
MET HE3  H N N 237 
MET HXT  H N N 238 
PHE N    N N N 239 
PHE CA   C N S 240 
PHE C    C N N 241 
PHE O    O N N 242 
PHE CB   C N N 243 
PHE CG   C Y N 244 
PHE CD1  C Y N 245 
PHE CD2  C Y N 246 
PHE CE1  C Y N 247 
PHE CE2  C Y N 248 
PHE CZ   C Y N 249 
PHE OXT  O N N 250 
PHE H    H N N 251 
PHE H2   H N N 252 
PHE HA   H N N 253 
PHE HB2  H N N 254 
PHE HB3  H N N 255 
PHE HD1  H N N 256 
PHE HD2  H N N 257 
PHE HE1  H N N 258 
PHE HE2  H N N 259 
PHE HZ   H N N 260 
PHE HXT  H N N 261 
PRO N    N N N 262 
PRO CA   C N S 263 
PRO C    C N N 264 
PRO O    O N N 265 
PRO CB   C N N 266 
PRO CG   C N N 267 
PRO CD   C N N 268 
PRO OXT  O N N 269 
PRO H    H N N 270 
PRO HA   H N N 271 
PRO HB2  H N N 272 
PRO HB3  H N N 273 
PRO HG2  H N N 274 
PRO HG3  H N N 275 
PRO HD2  H N N 276 
PRO HD3  H N N 277 
PRO HXT  H N N 278 
SER N    N N N 279 
SER CA   C N S 280 
SER C    C N N 281 
SER O    O N N 282 
SER CB   C N N 283 
SER OG   O N N 284 
SER OXT  O N N 285 
SER H    H N N 286 
SER H2   H N N 287 
SER HA   H N N 288 
SER HB2  H N N 289 
SER HB3  H N N 290 
SER HG   H N N 291 
SER HXT  H N N 292 
THR N    N N N 293 
THR CA   C N S 294 
THR C    C N N 295 
THR O    O N N 296 
THR CB   C N R 297 
THR OG1  O N N 298 
THR CG2  C N N 299 
THR OXT  O N N 300 
THR H    H N N 301 
THR H2   H N N 302 
THR HA   H N N 303 
THR HB   H N N 304 
THR HG1  H N N 305 
THR HG21 H N N 306 
THR HG22 H N N 307 
THR HG23 H N N 308 
THR HXT  H N N 309 
TRP N    N N N 310 
TRP CA   C N S 311 
TRP C    C N N 312 
TRP O    O N N 313 
TRP CB   C N N 314 
TRP CG   C Y N 315 
TRP CD1  C Y N 316 
TRP CD2  C Y N 317 
TRP NE1  N Y N 318 
TRP CE2  C Y N 319 
TRP CE3  C Y N 320 
TRP CZ2  C Y N 321 
TRP CZ3  C Y N 322 
TRP CH2  C Y N 323 
TRP OXT  O N N 324 
TRP H    H N N 325 
TRP H2   H N N 326 
TRP HA   H N N 327 
TRP HB2  H N N 328 
TRP HB3  H N N 329 
TRP HD1  H N N 330 
TRP HE1  H N N 331 
TRP HE3  H N N 332 
TRP HZ2  H N N 333 
TRP HZ3  H N N 334 
TRP HH2  H N N 335 
TRP HXT  H N N 336 
TYR N    N N N 337 
TYR CA   C N S 338 
TYR C    C N N 339 
TYR O    O N N 340 
TYR CB   C N N 341 
TYR CG   C Y N 342 
TYR CD1  C Y N 343 
TYR CD2  C Y N 344 
TYR CE1  C Y N 345 
TYR CE2  C Y N 346 
TYR CZ   C Y N 347 
TYR OH   O N N 348 
TYR OXT  O N N 349 
TYR H    H N N 350 
TYR H2   H N N 351 
TYR HA   H N N 352 
TYR HB2  H N N 353 
TYR HB3  H N N 354 
TYR HD1  H N N 355 
TYR HD2  H N N 356 
TYR HE1  H N N 357 
TYR HE2  H N N 358 
TYR HH   H N N 359 
TYR HXT  H N N 360 
VAL N    N N N 361 
VAL CA   C N S 362 
VAL C    C N N 363 
VAL O    O N N 364 
VAL CB   C N N 365 
VAL CG1  C N N 366 
VAL CG2  C N N 367 
VAL OXT  O N N 368 
VAL H    H N N 369 
VAL H2   H N N 370 
VAL HA   H N N 371 
VAL HB   H N N 372 
VAL HG11 H N N 373 
VAL HG12 H N N 374 
VAL HG13 H N N 375 
VAL HG21 H N N 376 
VAL HG22 H N N 377 
VAL HG23 H N N 378 
VAL HXT  H N N 379 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
GOL C1  O1   sing N N 129 
GOL C1  C2   sing N N 130 
GOL C1  H11  sing N N 131 
GOL C1  H12  sing N N 132 
GOL O1  HO1  sing N N 133 
GOL C2  O2   sing N N 134 
GOL C2  C3   sing N N 135 
GOL C2  H2   sing N N 136 
GOL O2  HO2  sing N N 137 
GOL C3  O3   sing N N 138 
GOL C3  H31  sing N N 139 
GOL C3  H32  sing N N 140 
GOL O3  HO3  sing N N 141 
HIS N   CA   sing N N 142 
HIS N   H    sing N N 143 
HIS N   H2   sing N N 144 
HIS CA  C    sing N N 145 
HIS CA  CB   sing N N 146 
HIS CA  HA   sing N N 147 
HIS C   O    doub N N 148 
HIS C   OXT  sing N N 149 
HIS CB  CG   sing N N 150 
HIS CB  HB2  sing N N 151 
HIS CB  HB3  sing N N 152 
HIS CG  ND1  sing Y N 153 
HIS CG  CD2  doub Y N 154 
HIS ND1 CE1  doub Y N 155 
HIS ND1 HD1  sing N N 156 
HIS CD2 NE2  sing Y N 157 
HIS CD2 HD2  sing N N 158 
HIS CE1 NE2  sing Y N 159 
HIS CE1 HE1  sing N N 160 
HIS NE2 HE2  sing N N 161 
HIS OXT HXT  sing N N 162 
HOH O   H1   sing N N 163 
HOH O   H2   sing N N 164 
ILE N   CA   sing N N 165 
ILE N   H    sing N N 166 
ILE N   H2   sing N N 167 
ILE CA  C    sing N N 168 
ILE CA  CB   sing N N 169 
ILE CA  HA   sing N N 170 
ILE C   O    doub N N 171 
ILE C   OXT  sing N N 172 
ILE CB  CG1  sing N N 173 
ILE CB  CG2  sing N N 174 
ILE CB  HB   sing N N 175 
ILE CG1 CD1  sing N N 176 
ILE CG1 HG12 sing N N 177 
ILE CG1 HG13 sing N N 178 
ILE CG2 HG21 sing N N 179 
ILE CG2 HG22 sing N N 180 
ILE CG2 HG23 sing N N 181 
ILE CD1 HD11 sing N N 182 
ILE CD1 HD12 sing N N 183 
ILE CD1 HD13 sing N N 184 
ILE OXT HXT  sing N N 185 
LEU N   CA   sing N N 186 
LEU N   H    sing N N 187 
LEU N   H2   sing N N 188 
LEU CA  C    sing N N 189 
LEU CA  CB   sing N N 190 
LEU CA  HA   sing N N 191 
LEU C   O    doub N N 192 
LEU C   OXT  sing N N 193 
LEU CB  CG   sing N N 194 
LEU CB  HB2  sing N N 195 
LEU CB  HB3  sing N N 196 
LEU CG  CD1  sing N N 197 
LEU CG  CD2  sing N N 198 
LEU CG  HG   sing N N 199 
LEU CD1 HD11 sing N N 200 
LEU CD1 HD12 sing N N 201 
LEU CD1 HD13 sing N N 202 
LEU CD2 HD21 sing N N 203 
LEU CD2 HD22 sing N N 204 
LEU CD2 HD23 sing N N 205 
LEU OXT HXT  sing N N 206 
MET N   CA   sing N N 207 
MET N   H    sing N N 208 
MET N   H2   sing N N 209 
MET CA  C    sing N N 210 
MET CA  CB   sing N N 211 
MET CA  HA   sing N N 212 
MET C   O    doub N N 213 
MET C   OXT  sing N N 214 
MET CB  CG   sing N N 215 
MET CB  HB2  sing N N 216 
MET CB  HB3  sing N N 217 
MET CG  SD   sing N N 218 
MET CG  HG2  sing N N 219 
MET CG  HG3  sing N N 220 
MET SD  CE   sing N N 221 
MET CE  HE1  sing N N 222 
MET CE  HE2  sing N N 223 
MET CE  HE3  sing N N 224 
MET OXT HXT  sing N N 225 
PHE N   CA   sing N N 226 
PHE N   H    sing N N 227 
PHE N   H2   sing N N 228 
PHE CA  C    sing N N 229 
PHE CA  CB   sing N N 230 
PHE CA  HA   sing N N 231 
PHE C   O    doub N N 232 
PHE C   OXT  sing N N 233 
PHE CB  CG   sing N N 234 
PHE CB  HB2  sing N N 235 
PHE CB  HB3  sing N N 236 
PHE CG  CD1  doub Y N 237 
PHE CG  CD2  sing Y N 238 
PHE CD1 CE1  sing Y N 239 
PHE CD1 HD1  sing N N 240 
PHE CD2 CE2  doub Y N 241 
PHE CD2 HD2  sing N N 242 
PHE CE1 CZ   doub Y N 243 
PHE CE1 HE1  sing N N 244 
PHE CE2 CZ   sing Y N 245 
PHE CE2 HE2  sing N N 246 
PHE CZ  HZ   sing N N 247 
PHE OXT HXT  sing N N 248 
PRO N   CA   sing N N 249 
PRO N   CD   sing N N 250 
PRO N   H    sing N N 251 
PRO CA  C    sing N N 252 
PRO CA  CB   sing N N 253 
PRO CA  HA   sing N N 254 
PRO C   O    doub N N 255 
PRO C   OXT  sing N N 256 
PRO CB  CG   sing N N 257 
PRO CB  HB2  sing N N 258 
PRO CB  HB3  sing N N 259 
PRO CG  CD   sing N N 260 
PRO CG  HG2  sing N N 261 
PRO CG  HG3  sing N N 262 
PRO CD  HD2  sing N N 263 
PRO CD  HD3  sing N N 264 
PRO OXT HXT  sing N N 265 
SER N   CA   sing N N 266 
SER N   H    sing N N 267 
SER N   H2   sing N N 268 
SER CA  C    sing N N 269 
SER CA  CB   sing N N 270 
SER CA  HA   sing N N 271 
SER C   O    doub N N 272 
SER C   OXT  sing N N 273 
SER CB  OG   sing N N 274 
SER CB  HB2  sing N N 275 
SER CB  HB3  sing N N 276 
SER OG  HG   sing N N 277 
SER OXT HXT  sing N N 278 
THR N   CA   sing N N 279 
THR N   H    sing N N 280 
THR N   H2   sing N N 281 
THR CA  C    sing N N 282 
THR CA  CB   sing N N 283 
THR CA  HA   sing N N 284 
THR C   O    doub N N 285 
THR C   OXT  sing N N 286 
THR CB  OG1  sing N N 287 
THR CB  CG2  sing N N 288 
THR CB  HB   sing N N 289 
THR OG1 HG1  sing N N 290 
THR CG2 HG21 sing N N 291 
THR CG2 HG22 sing N N 292 
THR CG2 HG23 sing N N 293 
THR OXT HXT  sing N N 294 
TRP N   CA   sing N N 295 
TRP N   H    sing N N 296 
TRP N   H2   sing N N 297 
TRP CA  C    sing N N 298 
TRP CA  CB   sing N N 299 
TRP CA  HA   sing N N 300 
TRP C   O    doub N N 301 
TRP C   OXT  sing N N 302 
TRP CB  CG   sing N N 303 
TRP CB  HB2  sing N N 304 
TRP CB  HB3  sing N N 305 
TRP CG  CD1  doub Y N 306 
TRP CG  CD2  sing Y N 307 
TRP CD1 NE1  sing Y N 308 
TRP CD1 HD1  sing N N 309 
TRP CD2 CE2  doub Y N 310 
TRP CD2 CE3  sing Y N 311 
TRP NE1 CE2  sing Y N 312 
TRP NE1 HE1  sing N N 313 
TRP CE2 CZ2  sing Y N 314 
TRP CE3 CZ3  doub Y N 315 
TRP CE3 HE3  sing N N 316 
TRP CZ2 CH2  doub Y N 317 
TRP CZ2 HZ2  sing N N 318 
TRP CZ3 CH2  sing Y N 319 
TRP CZ3 HZ3  sing N N 320 
TRP CH2 HH2  sing N N 321 
TRP OXT HXT  sing N N 322 
TYR N   CA   sing N N 323 
TYR N   H    sing N N 324 
TYR N   H2   sing N N 325 
TYR CA  C    sing N N 326 
TYR CA  CB   sing N N 327 
TYR CA  HA   sing N N 328 
TYR C   O    doub N N 329 
TYR C   OXT  sing N N 330 
TYR CB  CG   sing N N 331 
TYR CB  HB2  sing N N 332 
TYR CB  HB3  sing N N 333 
TYR CG  CD1  doub Y N 334 
TYR CG  CD2  sing Y N 335 
TYR CD1 CE1  sing Y N 336 
TYR CD1 HD1  sing N N 337 
TYR CD2 CE2  doub Y N 338 
TYR CD2 HD2  sing N N 339 
TYR CE1 CZ   doub Y N 340 
TYR CE1 HE1  sing N N 341 
TYR CE2 CZ   sing Y N 342 
TYR CE2 HE2  sing N N 343 
TYR CZ  OH   sing N N 344 
TYR OH  HH   sing N N 345 
TYR OXT HXT  sing N N 346 
VAL N   CA   sing N N 347 
VAL N   H    sing N N 348 
VAL N   H2   sing N N 349 
VAL CA  C    sing N N 350 
VAL CA  CB   sing N N 351 
VAL CA  HA   sing N N 352 
VAL C   O    doub N N 353 
VAL C   OXT  sing N N 354 
VAL CB  CG1  sing N N 355 
VAL CB  CG2  sing N N 356 
VAL CB  HB   sing N N 357 
VAL CG1 HG11 sing N N 358 
VAL CG1 HG12 sing N N 359 
VAL CG1 HG13 sing N N 360 
VAL CG2 HG21 sing N N 361 
VAL CG2 HG22 sing N N 362 
VAL CG2 HG23 sing N N 363 
VAL OXT HXT  sing N N 364 
# 
_pdbx_audit_support.funding_organization   'Agence Nationale de la Recherche (ANR)' 
_pdbx_audit_support.country                France 
_pdbx_audit_support.grant_number           ANR-20-CE92-0038 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8S6L 
_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]   0.017712 
_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]   0.014795 
_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]   0.008570 
_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 
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   . ALA A 1 22  ? 30.055  12.966  14.789  1.00 35.41  ? 2   ALA A N   1 
ATOM   2    C CA  . ALA A 1 22  ? 29.452  11.921  15.643  1.00 32.59  ? 2   ALA A CA  1 
ATOM   3    C C   . ALA A 1 22  ? 29.259  10.671  14.793  1.00 30.54  ? 2   ALA A C   1 
ATOM   4    O O   . ALA A 1 22  ? 28.698  10.776  13.703  1.00 30.39  ? 2   ALA A O   1 
ATOM   5    C CB  . ALA A 1 22  ? 28.124  12.422  16.193  1.00 32.34  ? 2   ALA A CB  1 
ATOM   6    N N   A GLU A 1 23  ? 29.735  9.506   15.272  0.50 30.65  ? 3   GLU A N   1 
ATOM   7    N N   B GLU A 1 23  ? 29.653  9.511   15.359  0.50 30.95  ? 3   GLU A N   1 
ATOM   8    C CA  A GLU A 1 23  ? 29.464  8.251   14.588  0.50 28.74  ? 3   GLU A CA  1 
ATOM   9    C CA  B GLU A 1 23  ? 29.639  8.217   14.692  0.50 28.70  ? 3   GLU A CA  1 
ATOM   10   C C   A GLU A 1 23  ? 29.168  7.121   15.574  0.50 29.54  ? 3   GLU A C   1 
ATOM   11   C C   B GLU A 1 23  ? 29.122  7.126   15.632  0.50 28.56  ? 3   GLU A C   1 
ATOM   12   O O   A GLU A 1 23  ? 29.592  7.136   16.728  0.50 31.87  ? 3   GLU A O   1 
ATOM   13   O O   B GLU A 1 23  ? 29.365  7.162   16.836  0.50 30.64  ? 3   GLU A O   1 
ATOM   14   C CB  A GLU A 1 23  ? 30.610  7.885   13.637  0.50 32.13  ? 3   GLU A CB  1 
ATOM   15   C CB  B GLU A 1 23  ? 31.064  7.869   14.250  0.50 31.17  ? 3   GLU A CB  1 
ATOM   16   C CG  A GLU A 1 23  ? 31.969  7.677   14.291  0.50 32.63  ? 3   GLU A CG  1 
ATOM   17   C CG  B GLU A 1 23  ? 31.632  8.804   13.172  0.50 32.61  ? 3   GLU A CG  1 
ATOM   18   C CD  A GLU A 1 23  ? 33.041  7.266   13.291  0.50 35.29  ? 3   GLU A CD  1 
ATOM   19   C CD  B GLU A 1 23  ? 31.207  8.464   11.750  0.50 34.26  ? 3   GLU A CD  1 
ATOM   20   O OE1 A GLU A 1 23  ? 33.262  8.003   12.298  0.50 34.80  ? 3   GLU A OE1 1 
ATOM   21   O OE1 B GLU A 1 23  ? 30.268  7.672   11.619  0.50 38.09  ? 3   GLU A OE1 1 
ATOM   22   O OE2 A GLU A 1 23  ? 33.619  6.184   13.472  0.50 39.43  ? 3   GLU A OE2 1 
ATOM   23   O OE2 B GLU A 1 23  ? 31.823  8.967   10.773  0.50 34.68  ? 3   GLU A OE2 1 
ATOM   24   N N   . ILE A 1 24  ? 28.416  6.138   15.077  1.00 27.61  ? 4   ILE A N   1 
ATOM   25   C CA  . ILE A 1 24  ? 28.060  4.944   15.836  1.00 27.47  ? 4   ILE A CA  1 
ATOM   26   C C   . ILE A 1 24  ? 29.139  3.900   15.607  1.00 26.13  ? 4   ILE A C   1 
ATOM   27   O O   . ILE A 1 24  ? 29.279  3.383   14.503  1.00 28.17  ? 4   ILE A O   1 
ATOM   28   C CB  . ILE A 1 24  ? 26.670  4.404   15.447  1.00 27.37  ? 4   ILE A CB  1 
ATOM   29   C CG1 . ILE A 1 24  ? 25.603  5.496   15.489  1.00 30.10  ? 4   ILE A CG1 1 
ATOM   30   C CG2 . ILE A 1 24  ? 26.318  3.225   16.336  1.00 30.05  ? 4   ILE A CG2 1 
ATOM   31   C CD1 . ILE A 1 24  ? 25.401  6.134   16.847  1.00 30.92  ? 4   ILE A CD1 1 
ATOM   32   N N   . ARG A 1 25  ? 29.881  3.599   16.671  1.00 27.73  ? 5   ARG A N   1 
ATOM   33   C CA  . ARG A 1 25  ? 30.921  2.548   16.626  1.00 27.38  ? 5   ARG A CA  1 
ATOM   34   C C   . ARG A 1 25  ? 30.910  1.875   17.995  1.00 28.36  ? 5   ARG A C   1 
ATOM   35   O O   . ARG A 1 25  ? 31.426  2.479   18.934  1.00 34.14  ? 5   ARG A O   1 
ATOM   36   C CB  . ARG A 1 25  ? 32.331  3.088   16.369  1.00 29.77  ? 5   ARG A CB  1 
ATOM   37   C CG  . ARG A 1 25  ? 32.766  3.183   14.920  1.00 34.29  ? 5   ARG A CG  1 
ATOM   38   C CD  . ARG A 1 25  ? 34.230  3.567   14.936  1.00 33.96  ? 5   ARG A CD  1 
ATOM   39   N NE  . ARG A 1 25  ? 34.696  3.908   13.593  1.00 36.33  ? 5   ARG A NE  1 
ATOM   40   C CZ  . ARG A 1 25  ? 35.167  3.033   12.729  1.00 34.07  ? 5   ARG A CZ  1 
ATOM   41   N NH1 . ARG A 1 25  ? 35.237  1.764   13.055  1.00 30.78  ? 5   ARG A NH1 1 
ATOM   42   N NH2 . ARG A 1 25  ? 35.573  3.435   11.518  1.00 34.35  ? 5   ARG A NH2 1 
ATOM   43   N N   . ARG A 1 26  ? 30.344  0.676   18.075  1.00 27.35  ? 6   ARG A N   1 
ATOM   44   C CA  . ARG A 1 26  ? 30.156  0.012   19.353  1.00 27.57  ? 6   ARG A CA  1 
ATOM   45   C C   . ARG A 1 26  ? 29.480  -1.318  19.084  1.00 25.43  ? 6   ARG A C   1 
ATOM   46   O O   . ARG A 1 26  ? 28.811  -1.477  18.060  1.00 26.34  ? 6   ARG A O   1 
ATOM   47   C CB  . ARG A 1 26  ? 29.278  0.819   20.321  1.00 27.65  ? 6   ARG A CB  1 
ATOM   48   C CG  . ARG A 1 26  ? 27.895  1.171   19.786  1.00 28.26  ? 6   ARG A CG  1 
ATOM   49   C CD  . ARG A 1 26  ? 27.041  1.807   20.870  1.00 26.26  ? 6   ARG A CD  1 
ATOM   50   N NE  . ARG A 1 26  ? 25.747  2.273   20.421  1.00 24.98  ? 6   ARG A NE  1 
ATOM   51   C CZ  . ARG A 1 26  ? 24.694  1.498   20.179  1.00 25.83  ? 6   ARG A CZ  1 
ATOM   52   N NH1 . ARG A 1 26  ? 24.760  0.186   20.378  1.00 23.26  ? 6   ARG A NH1 1 
ATOM   53   N NH2 . ARG A 1 26  ? 23.570  2.040   19.742  1.00 25.93  ? 6   ARG A NH2 1 
ATOM   54   N N   . PRO A 1 27  ? 29.590  -2.304  19.991  1.00 29.80  ? 7   PRO A N   1 
ATOM   55   C CA  . PRO A 1 27  ? 28.770  -3.500  19.855  1.00 29.44  ? 7   PRO A CA  1 
ATOM   56   C C   . PRO A 1 27  ? 27.275  -3.182  19.846  1.00 25.60  ? 7   PRO A C   1 
ATOM   57   O O   . PRO A 1 27  ? 26.820  -2.201  20.443  1.00 26.07  ? 7   PRO A O   1 
ATOM   58   C CB  . PRO A 1 27  ? 29.138  -4.339  21.090  1.00 31.37  ? 7   PRO A CB  1 
ATOM   59   C CG  . PRO A 1 27  ? 30.495  -3.808  21.535  1.00 33.77  ? 7   PRO A CG  1 
ATOM   60   C CD  . PRO A 1 27  ? 30.466  -2.332  21.180  1.00 31.35  ? 7   PRO A CD  1 
ATOM   61   N N   . LEU A 1 28  ? 26.493  -4.025  19.173  1.00 25.17  ? 8   LEU A N   1 
ATOM   62   C CA  . LEU A 1 28  ? 25.052  -3.937  19.364  1.00 25.06  ? 8   LEU A CA  1 
ATOM   63   C C   . LEU A 1 28  ? 24.749  -4.186  20.839  1.00 23.98  ? 8   LEU A C   1 
ATOM   64   O O   . LEU A 1 28  ? 25.403  -5.035  21.458  1.00 26.05  ? 8   LEU A O   1 
ATOM   65   C CB  . LEU A 1 28  ? 24.313  -4.959  18.501  1.00 24.03  ? 8   LEU A CB  1 
ATOM   66   C CG  . LEU A 1 28  ? 23.801  -4.461  17.160  1.00 24.34  ? 8   LEU A CG  1 
ATOM   67   C CD1 . LEU A 1 28  ? 24.940  -4.000  16.277  1.00 25.96  ? 8   LEU A CD1 1 
ATOM   68   C CD2 . LEU A 1 28  ? 23.001  -5.540  16.456  1.00 25.82  ? 8   LEU A CD2 1 
ATOM   69   N N   . SER A 1 29  ? 23.774  -3.451  21.391  1.00 24.33  ? 9   SER A N   1 
ATOM   70   C CA  . SER A 1 29  ? 23.234  -3.777  22.698  1.00 24.42  ? 9   SER A CA  1 
ATOM   71   C C   . SER A 1 29  ? 22.462  -5.094  22.614  1.00 23.55  ? 9   SER A C   1 
ATOM   72   O O   . SER A 1 29  ? 22.103  -5.553  21.524  1.00 23.25  ? 9   SER A O   1 
ATOM   73   C CB  . SER A 1 29  ? 22.366  -2.679  23.252  1.00 25.63  ? 9   SER A CB  1 
ATOM   74   O OG  . SER A 1 29  ? 21.171  -2.540  22.498  1.00 24.29  ? 9   SER A OG  1 
ATOM   75   N N   . ALA A 1 30  ? 22.174  -5.680  23.780  1.00 24.93  ? 10  ALA A N   1 
ATOM   76   C CA  . ALA A 1 30  ? 21.379  -6.909  23.808  1.00 25.17  ? 10  ALA A CA  1 
ATOM   77   C C   . ALA A 1 30  ? 19.992  -6.713  23.190  1.00 23.67  ? 10  ALA A C   1 
ATOM   78   O O   . ALA A 1 30  ? 19.528  -7.553  22.427  1.00 24.31  ? 10  ALA A O   1 
ATOM   79   C CB  . ALA A 1 30  ? 21.283  -7.425  25.207  1.00 25.40  ? 10  ALA A CB  1 
ATOM   80   N N   . VAL A 1 31  ? 19.323  -5.584  23.479  1.00 24.94  ? 11  VAL A N   1 
ATOM   81   C CA  . VAL A 1 31  ? 18.004  -5.328  22.910  1.00 23.18  ? 11  VAL A CA  1 
ATOM   82   C C   . VAL A 1 31  ? 18.136  -5.142  21.402  1.00 21.30  ? 11  VAL A C   1 
ATOM   83   O O   . VAL A 1 31  ? 17.324  -5.671  20.638  1.00 21.42  ? 11  VAL A O   1 
ATOM   84   C CB  . VAL A 1 31  ? 17.311  -4.139  23.596  1.00 26.21  ? 11  VAL A CB  1 
ATOM   85   C CG1 . VAL A 1 31  ? 16.079  -3.706  22.845  1.00 26.10  ? 11  VAL A CG1 1 
ATOM   86   C CG2 . VAL A 1 31  ? 16.980  -4.464  25.045  1.00 27.90  ? 11  VAL A CG2 1 
ATOM   87   N N   . GLU A 1 32  ? 19.153  -4.374  20.962  1.00 21.40  ? 12  GLU A N   1 
ATOM   88   C CA  . GLU A 1 32  ? 19.386  -4.239  19.525  1.00 20.90  ? 12  GLU A CA  1 
ATOM   89   C C   . GLU A 1 32  ? 19.613  -5.611  18.873  1.00 20.54  ? 12  GLU A C   1 
ATOM   90   O O   . GLU A 1 32  ? 19.079  -5.877  17.802  1.00 22.05  ? 12  GLU A O   1 
ATOM   91   C CB  . GLU A 1 32  ? 20.570  -3.313  19.209  1.00 20.70  ? 12  GLU A CB  1 
ATOM   92   C CG  . GLU A 1 32  ? 20.282  -1.851  19.533  1.00 21.89  ? 12  GLU A CG  1 
ATOM   93   C CD  . GLU A 1 32  ? 21.498  -0.954  19.653  1.00 22.29  ? 12  GLU A CD  1 
ATOM   94   O OE1 . GLU A 1 32  ? 21.289  0.281   19.860  1.00 27.13  ? 12  GLU A OE1 1 
ATOM   95   O OE2 . GLU A 1 32  ? 22.636  -1.439  19.534  1.00 22.30  ? 12  GLU A OE2 1 
ATOM   96   N N   . ARG A 1 33  ? 20.349  -6.506  19.546  1.00 22.34  ? 13  ARG A N   1 
ATOM   97   C CA  . ARG A 1 33  ? 20.622  -7.822  18.982  1.00 23.63  ? 13  ARG A CA  1 
ATOM   98   C C   . ARG A 1 33  ? 19.327  -8.648  18.836  1.00 21.74  ? 13  ARG A C   1 
ATOM   99   O O   . ARG A 1 33  ? 19.129  -9.347  17.846  1.00 22.94  ? 13  ARG A O   1 
ATOM   100  C CB  . ARG A 1 33  ? 21.688  -8.518  19.843  1.00 24.65  ? 13  ARG A CB  1 
ATOM   101  C CG  . ARG A 1 33  ? 22.178  -9.843  19.289  1.00 26.49  ? 13  ARG A CG  1 
ATOM   102  C CD  . ARG A 1 33  ? 23.326  -10.366 20.150  1.00 28.26  ? 13  ARG A CD  1 
ATOM   103  N NE  . ARG A 1 33  ? 22.877  -10.779 21.470  1.00 27.22  ? 13  ARG A NE  1 
ATOM   104  C CZ  . ARG A 1 33  ? 23.223  -10.276 22.653  1.00 28.89  ? 13  ARG A CZ  1 
ATOM   105  N NH1 . ARG A 1 33  ? 23.971  -9.192  22.770  1.00 29.45  ? 13  ARG A NH1 1 
ATOM   106  N NH2 . ARG A 1 33  ? 22.747  -10.858 23.742  1.00 31.26  ? 13  ARG A NH2 1 
ATOM   107  N N   . TRP A 1 34  ? 18.395  -8.509  19.778  1.00 20.73  ? 14  TRP A N   1 
ATOM   108  C CA  . TRP A 1 34  ? 17.072  -9.112  19.685  1.00 21.30  ? 14  TRP A CA  1 
ATOM   109  C C   . TRP A 1 34  ? 16.353  -8.671  18.419  1.00 19.41  ? 14  TRP A C   1 
ATOM   110  O O   . TRP A 1 34  ? 15.856  -9.478  17.657  1.00 22.23  ? 14  TRP A O   1 
ATOM   111  C CB  . TRP A 1 34  ? 16.239  -8.834  20.953  1.00 23.75  ? 14  TRP A CB  1 
ATOM   112  C CG  . TRP A 1 34  ? 14.798  -9.252  20.906  1.00 24.90  ? 14  TRP A CG  1 
ATOM   113  C CD1 . TRP A 1 34  ? 14.306  -10.521 20.778  1.00 26.73  ? 14  TRP A CD1 1 
ATOM   114  C CD2 . TRP A 1 34  ? 13.648  -8.427  21.142  1.00 25.42  ? 14  TRP A CD2 1 
ATOM   115  N NE1 . TRP A 1 34  ? 12.937  -10.515 20.811  1.00 26.12  ? 14  TRP A NE1 1 
ATOM   116  C CE2 . TRP A 1 34  ? 12.503  -9.242  21.048  1.00 27.55  ? 14  TRP A CE2 1 
ATOM   117  C CE3 . TRP A 1 34  ? 13.470  -7.042  21.317  1.00 27.66  ? 14  TRP A CE3 1 
ATOM   118  C CZ2 . TRP A 1 34  ? 11.208  -8.734  21.195  1.00 29.58  ? 14  TRP A CZ2 1 
ATOM   119  C CZ3 . TRP A 1 34  ? 12.192  -6.542  21.477  1.00 30.09  ? 14  TRP A CZ3 1 
ATOM   120  C CH2 . TRP A 1 34  ? 11.078  -7.374  21.414  1.00 30.35  ? 14  TRP A CH2 1 
ATOM   121  N N   . TYR A 1 35  ? 16.330  -7.356  18.132  1.00 19.96  ? 15  TYR A N   1 
ATOM   122  C CA  . TYR A 1 35  ? 15.683  -6.880  16.919  1.00 20.26  ? 15  TYR A CA  1 
ATOM   123  C C   . TYR A 1 35  ? 16.415  -7.347  15.658  1.00 20.28  ? 15  TYR A C   1 
ATOM   124  O O   . TYR A 1 35  ? 15.790  -7.676  14.645  1.00 21.76  ? 15  TYR A O   1 
ATOM   125  C CB  . TYR A 1 35  ? 15.618  -5.346  16.951  1.00 20.30  ? 15  TYR A CB  1 
ATOM   126  C CG  . TYR A 1 35  ? 14.586  -4.741  17.879  1.00 20.42  ? 15  TYR A CG  1 
ATOM   127  C CD1 . TYR A 1 35  ? 13.228  -4.908  17.679  1.00 22.99  ? 15  TYR A CD1 1 
ATOM   128  C CD2 . TYR A 1 35  ? 14.962  -3.962  18.952  1.00 21.15  ? 15  TYR A CD2 1 
ATOM   129  C CE1 . TYR A 1 35  ? 12.277  -4.328  18.520  1.00 24.16  ? 15  TYR A CE1 1 
ATOM   130  C CE2 . TYR A 1 35  ? 14.036  -3.350  19.782  1.00 23.08  ? 15  TYR A CE2 1 
ATOM   131  C CZ  . TYR A 1 35  ? 12.680  -3.543  19.583  1.00 23.33  ? 15  TYR A CZ  1 
ATOM   132  O OH  . TYR A 1 35  ? 11.742  -2.954  20.416  1.00 28.47  ? 15  TYR A OH  1 
ATOM   133  N N   . TRP A 1 36  ? 17.752  -7.378  15.720  1.00 22.29  ? 16  TRP A N   1 
ATOM   134  C CA  . TRP A 1 36  ? 18.581  -7.842  14.616  1.00 21.17  ? 16  TRP A CA  1 
ATOM   135  C C   . TRP A 1 36  ? 18.251  -9.295  14.265  1.00 21.92  ? 16  TRP A C   1 
ATOM   136  O O   . TRP A 1 36  ? 18.132  -9.630  13.098  1.00 22.76  ? 16  TRP A O   1 
ATOM   137  C CB  . TRP A 1 36  ? 20.045  -7.678  15.023  1.00 22.51  ? 16  TRP A CB  1 
ATOM   138  C CG  . TRP A 1 36  ? 21.043  -8.149  14.016  1.00 25.91  ? 16  TRP A CG  1 
ATOM   139  C CD1 . TRP A 1 36  ? 21.278  -7.633  12.772  1.00 27.76  ? 16  TRP A CD1 1 
ATOM   140  C CD2 . TRP A 1 36  ? 22.022  -9.180  14.217  1.00 27.83  ? 16  TRP A CD2 1 
ATOM   141  N NE1 . TRP A 1 36  ? 22.301  -8.308  12.158  1.00 28.48  ? 16  TRP A NE1 1 
ATOM   142  C CE2 . TRP A 1 36  ? 22.804  -9.240  13.039  1.00 28.40  ? 16  TRP A CE2 1 
ATOM   143  C CE3 . TRP A 1 36  ? 22.276  -10.084 15.265  1.00 28.06  ? 16  TRP A CE3 1 
ATOM   144  C CZ2 . TRP A 1 36  ? 23.808  -10.202 12.880  1.00 32.98  ? 16  TRP A CZ2 1 
ATOM   145  C CZ3 . TRP A 1 36  ? 23.292  -10.999 15.113  1.00 30.98  ? 16  TRP A CZ3 1 
ATOM   146  C CH2 . TRP A 1 36  ? 24.031  -11.067 13.930  1.00 30.82  ? 16  TRP A CH2 1 
ATOM   147  N N   . LEU A 1 37  ? 18.109  -10.138 15.286  1.00 23.41  ? 17  LEU A N   1 
ATOM   148  C CA  . LEU A 1 37  ? 17.767  -11.540 15.090  1.00 22.84  ? 17  LEU A CA  1 
ATOM   149  C C   . LEU A 1 37  ? 16.332  -11.694 14.582  1.00 20.97  ? 17  LEU A C   1 
ATOM   150  O O   . LEU A 1 37  ? 16.081  -12.408 13.630  1.00 23.11  ? 17  LEU A O   1 
ATOM   151  C CB  . LEU A 1 37  ? 17.959  -12.293 16.427  1.00 23.04  ? 17  LEU A CB  1 
ATOM   152  C CG  . LEU A 1 37  ? 19.385  -12.386 16.963  1.00 27.89  ? 17  LEU A CG  1 
ATOM   153  C CD1 . LEU A 1 37  ? 19.441  -12.981 18.365  1.00 29.81  ? 17  LEU A CD1 1 
ATOM   154  C CD2 . LEU A 1 37  ? 20.261  -13.218 16.039  1.00 29.72  ? 17  LEU A CD2 1 
ATOM   155  N N   . SER A 1 38  ? 15.353  -11.021 15.206  1.00 22.15  ? 18  SER A N   1 
ATOM   156  C CA  . SER A 1 38  ? 13.972  -11.133 14.769  1.00 21.71  ? 18  SER A CA  1 
ATOM   157  C C   . SER A 1 38  ? 13.872  -10.844 13.271  1.00 22.05  ? 18  SER A C   1 
ATOM   158  O O   . SER A 1 38  ? 13.217  -11.568 12.521  1.00 21.81  ? 18  SER A O   1 
ATOM   159  C CB  . SER A 1 38  ? 13.048  -10.234 15.577  1.00 23.16  ? 18  SER A CB  1 
ATOM   160  O OG  . SER A 1 38  ? 12.996  -10.578 16.960  1.00 24.51  ? 18  SER A OG  1 
ATOM   161  N N   . ASP A 1 39  ? 14.473  -9.721  12.851  1.00 22.72  ? 19  ASP A N   1 
ATOM   162  C CA  . ASP A 1 39  ? 14.433  -9.256  11.480  1.00 22.03  ? 19  ASP A CA  1 
ATOM   163  C C   . ASP A 1 39  ? 15.035  -10.259 10.501  1.00 22.72  ? 19  ASP A C   1 
ATOM   164  O O   . ASP A 1 39  ? 14.585  -10.322 9.351   1.00 23.26  ? 19  ASP A O   1 
ATOM   165  C CB  . ASP A 1 39  ? 15.073  -7.859  11.407  1.00 20.08  ? 19  ASP A CB  1 
ATOM   166  C CG  . ASP A 1 39  ? 15.232  -7.315  9.999   1.00 23.48  ? 19  ASP A CG  1 
ATOM   167  O OD1 . ASP A 1 39  ? 14.210  -6.800  9.453   1.00 23.76  ? 19  ASP A OD1 1 
ATOM   168  O OD2 . ASP A 1 39  ? 16.361  -7.425  9.461   1.00 25.04  ? 19  ASP A OD2 1 
ATOM   169  N N   . GLN A 1 40  ? 16.024  -11.052 10.935  1.00 23.05  ? 20  GLN A N   1 
ATOM   170  C CA  . GLN A 1 40  ? 16.607  -12.075 10.069  1.00 25.65  ? 20  GLN A CA  1 
ATOM   171  C C   . GLN A 1 40  ? 15.628  -13.214 9.809   1.00 26.24  ? 20  GLN A C   1 
ATOM   172  O O   . GLN A 1 40  ? 15.652  -13.804 8.739   1.00 28.11  ? 20  GLN A O   1 
ATOM   173  C CB  . GLN A 1 40  ? 17.910  -12.618 10.661  1.00 25.78  ? 20  GLN A CB  1 
ATOM   174  C CG  . GLN A 1 40  ? 19.031  -11.598 10.606  1.00 26.68  ? 20  GLN A CG  1 
ATOM   175  C CD  . GLN A 1 40  ? 20.295  -12.026 11.309  1.00 29.74  ? 20  GLN A CD  1 
ATOM   176  O OE1 . GLN A 1 40  ? 20.707  -11.487 12.355  1.00 33.31  ? 20  GLN A OE1 1 
ATOM   177  N NE2 . GLN A 1 40  ? 20.914  -13.031 10.729  1.00 28.22  ? 20  GLN A NE2 1 
ATOM   178  N N   . PHE A 1 41  ? 14.774  -13.551 10.776  1.00 24.64  ? 21  PHE A N   1 
ATOM   179  C CA  . PHE A 1 41  ? 13.749  -14.564 10.517  1.00 27.26  ? 21  PHE A CA  1 
ATOM   180  C C   . PHE A 1 41  ? 12.676  -14.019 9.565   1.00 26.53  ? 21  PHE A C   1 
ATOM   181  O O   . PHE A 1 41  ? 12.236  -14.714 8.644   1.00 26.98  ? 21  PHE A O   1 
ATOM   182  C CB  . PHE A 1 41  ? 13.073  -15.028 11.815  1.00 27.50  ? 21  PHE A CB  1 
ATOM   183  C CG  . PHE A 1 41  ? 13.932  -15.898 12.680  1.00 30.05  ? 21  PHE A CG  1 
ATOM   184  C CD1 . PHE A 1 41  ? 14.195  -17.211 12.303  1.00 30.31  ? 21  PHE A CD1 1 
ATOM   185  C CD2 . PHE A 1 41  ? 14.500  -15.409 13.840  1.00 28.80  ? 21  PHE A CD2 1 
ATOM   186  C CE1 . PHE A 1 41  ? 15.014  -18.019 13.082  1.00 32.41  ? 21  PHE A CE1 1 
ATOM   187  C CE2 . PHE A 1 41  ? 15.344  -16.204 14.603  1.00 30.98  ? 21  PHE A CE2 1 
ATOM   188  C CZ  . PHE A 1 41  ? 15.555  -17.524 14.257  1.00 30.60  ? 21  PHE A CZ  1 
ATOM   189  N N   . SER A 1 42  ? 12.252  -12.758 9.811   1.00 25.32  ? 22  SER A N   1 
ATOM   190  C CA  . SER A 1 42  ? 11.131  -12.155 9.116   1.00 24.10  ? 22  SER A CA  1 
ATOM   191  C C   . SER A 1 42  ? 11.264  -10.638 9.262   1.00 22.78  ? 22  SER A C   1 
ATOM   192  O O   . SER A 1 42  ? 11.466  -10.173 10.387  1.00 22.73  ? 22  SER A O   1 
ATOM   193  C CB  . SER A 1 42  ? 9.835   -12.680 9.688   1.00 28.33  ? 22  SER A CB  1 
ATOM   194  O OG  . SER A 1 42  ? 8.679   -12.006 9.179   1.00 32.22  ? 22  SER A OG  1 
ATOM   195  N N   . ALA A 1 43  ? 11.182  -9.901  8.133   1.00 22.71  ? 23  ALA A N   1 
ATOM   196  C CA  . ALA A 1 43  ? 11.489  -8.465  8.116   1.00 21.46  ? 23  ALA A CA  1 
ATOM   197  C C   . ALA A 1 43  ? 10.706  -7.723  9.189   1.00 19.64  ? 23  ALA A C   1 
ATOM   198  O O   . ALA A 1 43  ? 9.497   -7.927  9.337   1.00 21.43  ? 23  ALA A O   1 
ATOM   199  C CB  . ALA A 1 43  ? 11.191  -7.870  6.768   1.00 22.53  ? 23  ALA A CB  1 
ATOM   200  N N   . LEU A 1 44  ? 11.419  -6.841  9.900   1.00 19.69  ? 24  LEU A N   1 
ATOM   201  C CA  . LEU A 1 44  ? 10.806  -6.062  11.004  1.00 17.57  ? 24  LEU A CA  1 
ATOM   202  C C   . LEU A 1 44  ? 10.981  -4.556  10.709  1.00 18.15  ? 24  LEU A C   1 
ATOM   203  O O   . LEU A 1 44  ? 11.821  -3.946  11.343  1.00 21.15  ? 24  LEU A O   1 
ATOM   204  C CB  . LEU A 1 44  ? 11.480  -6.439  12.316  1.00 20.29  ? 24  LEU A CB  1 
ATOM   205  C CG  . LEU A 1 44  ? 10.842  -5.907  13.601  1.00 22.19  ? 24  LEU A CG  1 
ATOM   206  C CD1 . LEU A 1 44  ? 9.338   -6.034  13.583  1.00 23.06  ? 24  LEU A CD1 1 
ATOM   207  C CD2 . LEU A 1 44  ? 11.439  -6.607  14.809  1.00 22.55  ? 24  LEU A CD2 1 
ATOM   208  N N   . ASN A 1 45  ? 10.192  -4.054  9.777   1.00 16.52  ? 25  ASN A N   1 
ATOM   209  C CA  . ASN A 1 45  ? 10.287  -2.668  9.365   1.00 16.63  ? 25  ASN A CA  1 
ATOM   210  C C   . ASN A 1 45  ? 9.169   -1.838  9.984   1.00 17.09  ? 25  ASN A C   1 
ATOM   211  O O   . ASN A 1 45  ? 8.018   -2.220  10.008  1.00 19.28  ? 25  ASN A O   1 
ATOM   212  C CB  . ASN A 1 45  ? 10.218  -2.520  7.845   1.00 17.73  ? 25  ASN A CB  1 
ATOM   213  C CG  . ASN A 1 45  ? 11.415  -3.148  7.173   1.00 18.04  ? 25  ASN A CG  1 
ATOM   214  O OD1 . ASN A 1 45  ? 12.520  -3.102  7.724   1.00 19.33  ? 25  ASN A OD1 1 
ATOM   215  N ND2 . ASN A 1 45  ? 11.190  -3.697  5.987   1.00 20.38  ? 25  ASN A ND2 1 
ATOM   216  N N   . VAL A 1 46  ? 9.541   -0.626  10.385  1.00 17.27  ? 26  VAL A N   1 
ATOM   217  C CA  . VAL A 1 46  ? 8.599   0.393   10.837  1.00 17.52  ? 26  VAL A CA  1 
ATOM   218  C C   . VAL A 1 46  ? 8.486   1.442   9.721   1.00 15.88  ? 26  VAL A C   1 
ATOM   219  O O   . VAL A 1 46  ? 9.482   1.761   9.083   1.00 16.42  ? 26  VAL A O   1 
ATOM   220  C CB  . VAL A 1 46  ? 9.074   1.000   12.177  1.00 18.33  ? 26  VAL A CB  1 
ATOM   221  C CG1 . VAL A 1 46  ? 8.038   1.943   12.769  1.00 18.06  ? 26  VAL A CG1 1 
ATOM   222  C CG2 . VAL A 1 46  ? 9.457   -0.041  13.209  1.00 18.63  ? 26  VAL A CG2 1 
ATOM   223  N N   . ILE A 1 47  ? 7.246   1.861   9.449   1.00 16.51  ? 27  ILE A N   1 
ATOM   224  C CA  . ILE A 1 47  ? 7.002   2.684   8.262   1.00 15.36  ? 27  ILE A CA  1 
ATOM   225  C C   . ILE A 1 47  ? 6.156   3.889   8.622   1.00 15.53  ? 27  ILE A C   1 
ATOM   226  O O   . ILE A 1 47  ? 5.118   3.762   9.255   1.00 15.82  ? 27  ILE A O   1 
ATOM   227  C CB  . ILE A 1 47  ? 6.319   1.842   7.168   1.00 18.14  ? 27  ILE A CB  1 
ATOM   228  C CG1 . ILE A 1 47  ? 7.217   0.669   6.804   1.00 18.71  ? 27  ILE A CG1 1 
ATOM   229  C CG2 . ILE A 1 47  ? 5.970   2.702   5.969   1.00 18.09  ? 27  ILE A CG2 1 
ATOM   230  C CD1 . ILE A 1 47  ? 6.537   -0.310  5.869   1.00 20.01  ? 27  ILE A CD1 1 
ATOM   231  N N   . SER A 1 48  ? 6.596   5.051   8.127   1.00 16.74  ? 28  SER A N   1 
ATOM   232  C CA  . SER A 1 48  ? 5.725   6.226   8.145   1.00 15.95  ? 28  SER A CA  1 
ATOM   233  C C   . SER A 1 48  ? 5.256   6.554   6.728   1.00 16.22  ? 28  SER A C   1 
ATOM   234  O O   . SER A 1 48  ? 5.976   6.288   5.759   1.00 16.54  ? 28  SER A O   1 
ATOM   235  C CB  . SER A 1 48  ? 6.362   7.413   8.804   1.00 16.77  ? 28  SER A CB  1 
ATOM   236  O OG  . SER A 1 48  ? 7.490   7.857   8.058   1.00 17.69  ? 28  SER A OG  1 
ATOM   237  N N   . ARG A 1 49  ? 4.084   7.191   6.642   1.00 16.83  ? 29  ARG A N   1 
ATOM   238  C CA  . ARG A 1 49  ? 3.560   7.708   5.395   1.00 16.69  ? 29  ARG A CA  1 
ATOM   239  C C   . ARG A 1 49  ? 3.060   9.140   5.635   1.00 17.47  ? 29  ARG A C   1 
ATOM   240  O O   . ARG A 1 49  ? 2.455   9.434   6.656   1.00 16.80  ? 29  ARG A O   1 
ATOM   241  C CB  . ARG A 1 49  ? 2.449   6.808   4.862   1.00 19.03  ? 29  ARG A CB  1 
ATOM   242  C CG  . ARG A 1 49  ? 1.736   7.294   3.603   1.00 19.37  ? 29  ARG A CG  1 
ATOM   243  C CD  . ARG A 1 49  ? 0.419   7.950   3.934   1.00 19.73  ? 29  ARG A CD  1 
ATOM   244  N NE  . ARG A 1 49  ? -0.296  8.433   2.755   1.00 20.60  ? 29  ARG A NE  1 
ATOM   245  C CZ  . ARG A 1 49  ? -1.603  8.419   2.577   1.00 20.99  ? 29  ARG A CZ  1 
ATOM   246  N NH1 . ARG A 1 49  ? -2.438  7.989   3.519   1.00 20.26  ? 29  ARG A NH1 1 
ATOM   247  N NH2 . ARG A 1 49  ? -2.089  8.898   1.446   1.00 22.09  ? 29  ARG A NH2 1 
ATOM   248  N N   . VAL A 1 50  ? 3.259   9.987   4.627   1.00 17.16  ? 30  VAL A N   1 
ATOM   249  C CA  . VAL A 1 50  ? 2.660   11.313  4.655   1.00 18.05  ? 30  VAL A CA  1 
ATOM   250  C C   . VAL A 1 50  ? 2.328   11.705  3.215   1.00 17.17  ? 30  VAL A C   1 
ATOM   251  O O   . VAL A 1 50  ? 3.055   11.346  2.292   1.00 17.86  ? 30  VAL A O   1 
ATOM   252  C CB  . VAL A 1 50  ? 3.578   12.340  5.349   1.00 17.68  ? 30  VAL A CB  1 
ATOM   253  C CG1 . VAL A 1 50  ? 4.891   12.525  4.641   1.00 18.56  ? 30  VAL A CG1 1 
ATOM   254  C CG2 . VAL A 1 50  ? 2.851   13.665  5.501   1.00 18.82  ? 30  VAL A CG2 1 
ATOM   255  N N   . ARG A 1 51  ? 1.243   12.461  3.041   1.00 17.74  ? 31  ARG A N   1 
ATOM   256  C CA  . ARG A 1 51  ? 0.895   13.006  1.734   1.00 17.27  ? 31  ARG A CA  1 
ATOM   257  C C   . ARG A 1 51  ? 1.282   14.484  1.630   1.00 17.08  ? 31  ARG A C   1 
ATOM   258  O O   . ARG A 1 51  ? 1.090   15.255  2.563   1.00 19.73  ? 31  ARG A O   1 
ATOM   259  C CB  . ARG A 1 51  ? -0.592  12.819  1.409   1.00 19.61  ? 31  ARG A CB  1 
ATOM   260  C CG  . ARG A 1 51  ? -0.982  13.340  0.039   1.00 21.25  ? 31  ARG A CG  1 
ATOM   261  C CD  . ARG A 1 51  ? -2.281  12.785  -0.447  1.00 21.77  ? 31  ARG A CD  1 
ATOM   262  N NE  . ARG A 1 51  ? -2.164  11.389  -0.822  1.00 21.73  ? 31  ARG A NE  1 
ATOM   263  C CZ  . ARG A 1 51  ? -3.167  10.651  -1.272  1.00 23.95  ? 31  ARG A CZ  1 
ATOM   264  N NH1 . ARG A 1 51  ? -4.391  11.153  -1.340  1.00 24.62  ? 31  ARG A NH1 1 
ATOM   265  N NH2 . ARG A 1 51  ? -2.937  9.381   -1.599  1.00 22.11  ? 31  ARG A NH2 1 
ATOM   266  N N   . VAL A 1 52  ? 1.866   14.772  0.473   1.00 17.74  ? 32  VAL A N   1 
ATOM   267  C CA  . VAL A 1 52  ? 2.419   16.058  0.146   1.00 18.45  ? 32  VAL A CA  1 
ATOM   268  C C   . VAL A 1 52  ? 1.625   16.728  -0.989  1.00 16.91  ? 32  VAL A C   1 
ATOM   269  O O   . VAL A 1 52  ? 1.479   16.202  -2.084  1.00 19.33  ? 32  VAL A O   1 
ATOM   270  C CB  . VAL A 1 52  ? 3.907   15.975  -0.283  1.00 17.83  ? 32  VAL A CB  1 
ATOM   271  C CG1 . VAL A 1 52  ? 4.383   17.424  -0.616  1.00 19.57  ? 32  VAL A CG1 1 
ATOM   272  C CG2 . VAL A 1 52  ? 4.740   15.279  0.792   1.00 19.69  ? 32  VAL A CG2 1 
ATOM   273  N N   . HIS A 1 53  ? 1.152   17.962  -0.708  1.00 19.32  ? 33  HIS A N   1 
ATOM   274  C CA  . HIS A 1 53  ? 0.394   18.762  -1.656  1.00 20.35  ? 33  HIS A CA  1 
ATOM   275  C C   . HIS A 1 53  ? 1.193   20.016  -2.012  1.00 20.91  ? 33  HIS A C   1 
ATOM   276  O O   . HIS A 1 53  ? 1.698   20.728  -1.148  1.00 22.78  ? 33  HIS A O   1 
ATOM   277  C CB  . HIS A 1 53  ? -0.941  19.164  -1.035  1.00 21.00  ? 33  HIS A CB  1 
ATOM   278  C CG  . HIS A 1 53  ? -1.742  18.019  -0.504  1.00 21.00  ? 33  HIS A CG  1 
ATOM   279  N ND1 . HIS A 1 53  ? -2.554  17.235  -1.296  1.00 21.36  ? 33  HIS A ND1 1 
ATOM   280  C CD2 . HIS A 1 53  ? -1.822  17.544  0.750   1.00 22.06  ? 33  HIS A CD2 1 
ATOM   281  C CE1 . HIS A 1 53  ? -3.058  16.271  -0.541  1.00 20.57  ? 33  HIS A CE1 1 
ATOM   282  N NE2 . HIS A 1 53  ? -2.670  16.467  0.713   1.00 20.83  ? 33  HIS A NE2 1 
ATOM   283  N N   . GLY A 1 54  ? 1.388   20.165  -3.304  1.00 22.21  ? 34  GLY A N   1 
ATOM   284  C CA  . GLY A 1 54  ? 2.137   21.256  -3.862  1.00 23.84  ? 34  GLY A CA  1 
ATOM   285  C C   . GLY A 1 54  ? 3.247   20.763  -4.782  1.00 24.38  ? 34  GLY A C   1 
ATOM   286  O O   . GLY A 1 54  ? 3.429   19.554  -4.988  1.00 27.71  ? 34  GLY A O   1 
ATOM   287  N N   . ARG A 1 55  ? 3.953   21.744  -5.373  1.00 25.61  ? 35  ARG A N   1 
ATOM   288  C CA  . ARG A 1 55  ? 5.064   21.441  -6.248  1.00 27.24  ? 35  ARG A CA  1 
ATOM   289  C C   . ARG A 1 55  ? 6.220   20.878  -5.416  1.00 27.54  ? 35  ARG A C   1 
ATOM   290  O O   . ARG A 1 55  ? 6.730   21.554  -4.533  1.00 31.54  ? 35  ARG A O   1 
ATOM   291  C CB  . ARG A 1 55  ? 5.548   22.663  -7.016  1.00 29.43  ? 35  ARG A CB  1 
ATOM   292  C CG  . ARG A 1 55  ? 6.599   22.274  -8.050  0.70 32.12  ? 35  ARG A CG  1 
ATOM   293  C CD  . ARG A 1 55  ? 7.118   23.375  -8.940  0.70 34.29  ? 35  ARG A CD  1 
ATOM   294  N NE  . ARG A 1 55  ? 7.934   22.759  -9.970  1.00 35.43  ? 35  ARG A NE  1 
ATOM   295  C CZ  . ARG A 1 55  ? 9.187   22.363  -9.800  1.00 38.04  ? 35  ARG A CZ  1 
ATOM   296  N NH1 . ARG A 1 55  ? 9.868   22.781  -8.747  1.00 35.86  ? 35  ARG A NH1 1 
ATOM   297  N NH2 . ARG A 1 55  ? 9.762   21.585  -10.705 1.00 43.39  ? 35  ARG A NH2 1 
ATOM   298  N N   . LEU A 1 56  ? 6.642   19.653  -5.744  1.00 27.49  ? 36  LEU A N   1 
ATOM   299  C CA  . LEU A 1 56  ? 7.704   18.959  -5.039  1.00 26.41  ? 36  LEU A CA  1 
ATOM   300  C C   . LEU A 1 56  ? 8.703   18.387  -6.040  1.00 27.46  ? 36  LEU A C   1 
ATOM   301  O O   . LEU A 1 56  ? 8.348   17.525  -6.839  1.00 33.44  ? 36  LEU A O   1 
ATOM   302  C CB  . LEU A 1 56  ? 7.088   17.812  -4.227  1.00 28.16  ? 36  LEU A CB  1 
ATOM   303  C CG  . LEU A 1 56  ? 8.061   17.022  -3.361  1.00 28.16  ? 36  LEU A CG  1 
ATOM   304  C CD1 . LEU A 1 56  ? 8.645   17.879  -2.259  1.00 27.25  ? 36  LEU A CD1 1 
ATOM   305  C CD2 . LEU A 1 56  ? 7.385   15.784  -2.794  1.00 29.31  ? 36  LEU A CD2 1 
ATOM   306  N N   . SER A 1 57  ? 9.945   18.843  -5.939  1.00 26.26  ? 37  SER A N   1 
ATOM   307  C CA  . SER A 1 57  ? 11.072  18.386  -6.735  1.00 27.63  ? 37  SER A CA  1 
ATOM   308  C C   . SER A 1 57  ? 11.733  17.178  -6.093  1.00 24.09  ? 37  SER A C   1 
ATOM   309  O O   . SER A 1 57  ? 12.115  17.236  -4.914  1.00 25.71  ? 37  SER A O   1 
ATOM   310  C CB  . SER A 1 57  ? 12.119  19.478  -6.815  1.00 29.30  ? 37  SER A CB  1 
ATOM   311  O OG  . SER A 1 57  ? 13.308  19.045  -7.451  1.00 29.16  ? 37  SER A OG  1 
ATOM   312  N N   . ILE A 1 58  ? 11.939  16.131  -6.889  1.00 27.43  ? 38  ILE A N   1 
ATOM   313  C CA  . ILE A 1 58  ? 12.703  14.980  -6.433  1.00 28.63  ? 38  ILE A CA  1 
ATOM   314  C C   . ILE A 1 58  ? 14.130  15.389  -6.057  1.00 25.44  ? 38  ILE A C   1 
ATOM   315  O O   . ILE A 1 58  ? 14.707  14.852  -5.111  1.00 23.63  ? 38  ILE A O   1 
ATOM   316  C CB  . ILE A 1 58  ? 12.669  13.819  -7.449  1.00 29.11  ? 38  ILE A CB  1 
ATOM   317  C CG1 . ILE A 1 58  ? 11.234  13.406  -7.783  1.00 35.23  ? 38  ILE A CG1 1 
ATOM   318  C CG2 . ILE A 1 58  ? 13.483  12.628  -6.944  1.00 32.52  ? 38  ILE A CG2 1 
ATOM   319  C CD1 . ILE A 1 58  ? 10.386  12.994  -6.595  1.00 36.47  ? 38  ILE A CD1 1 
ATOM   320  N N   . ASP A 1 59  ? 14.701  16.380  -6.750  1.00 24.62  ? 39  ASP A N   1 
ATOM   321  C CA  . ASP A 1 59  ? 16.022  16.875  -6.395  1.00 25.28  ? 39  ASP A CA  1 
ATOM   322  C C   . ASP A 1 59  ? 16.045  17.467  -4.981  1.00 24.03  ? 39  ASP A C   1 
ATOM   323  O O   . ASP A 1 59  ? 17.034  17.320  -4.261  1.00 22.96  ? 39  ASP A O   1 
ATOM   324  C CB  . ASP A 1 59  ? 16.464  17.947  -7.381  1.00 28.29  ? 39  ASP A CB  1 
ATOM   325  C CG  . ASP A 1 59  ? 16.599  17.439  -8.797  1.00 32.37  ? 39  ASP A CG  1 
ATOM   326  O OD1 . ASP A 1 59  ? 17.179  16.346  -8.971  1.00 38.70  ? 39  ASP A OD1 1 
ATOM   327  O OD2 . ASP A 1 59  ? 16.233  18.167  -9.687  1.00 37.11  ? 39  ASP A OD2 1 
ATOM   328  N N   . ASP A 1 60  ? 14.969  18.163  -4.594  1.00 23.43  ? 40  ASP A N   1 
ATOM   329  C CA  . ASP A 1 60  ? 14.886  18.705  -3.254  1.00 23.04  ? 40  ASP A CA  1 
ATOM   330  C C   . ASP A 1 60  ? 14.735  17.581  -2.230  1.00 20.90  ? 40  ASP A C   1 
ATOM   331  O O   . ASP A 1 60  ? 15.320  17.669  -1.155  1.00 20.44  ? 40  ASP A O   1 
ATOM   332  C CB  . ASP A 1 60  ? 13.793  19.768  -3.135  1.00 25.67  ? 40  ASP A CB  1 
ATOM   333  C CG  . ASP A 1 60  ? 14.116  21.004  -3.955  1.00 28.98  ? 40  ASP A CG  1 
ATOM   334  O OD1 . ASP A 1 60  ? 15.313  21.242  -4.233  1.00 32.31  ? 40  ASP A OD1 1 
ATOM   335  O OD2 . ASP A 1 60  ? 13.177  21.683  -4.311  1.00 31.11  ? 40  ASP A OD2 1 
ATOM   336  N N   . LEU A 1 61  ? 13.998  16.506  -2.571  1.00 20.17  ? 41  LEU A N   1 
ATOM   337  C CA  . LEU A 1 61  ? 13.946  15.376  -1.663  1.00 20.67  ? 41  LEU A CA  1 
ATOM   338  C C   . LEU A 1 61  ? 15.325  14.743  -1.457  1.00 21.49  ? 41  LEU A C   1 
ATOM   339  O O   . LEU A 1 61  ? 15.631  14.308  -0.345  1.00 21.19  ? 41  LEU A O   1 
ATOM   340  C CB  . LEU A 1 61  ? 12.960  14.334  -2.184  1.00 20.39  ? 41  LEU A CB  1 
ATOM   341  C CG  . LEU A 1 61  ? 11.491  14.723  -2.137  1.00 21.05  ? 41  LEU A CG  1 
ATOM   342  C CD1 . LEU A 1 61  ? 10.632  13.586  -2.693  1.00 23.85  ? 41  LEU A CD1 1 
ATOM   343  C CD2 . LEU A 1 61  ? 11.043  15.041  -0.710  1.00 21.37  ? 41  LEU A CD2 1 
ATOM   344  N N   . ARG A 1 62  ? 16.127  14.656  -2.513  1.00 20.54  ? 42  ARG A N   1 
ATOM   345  C CA  . ARG A 1 62  ? 17.503  14.105  -2.399  1.00 21.38  ? 42  ARG A CA  1 
ATOM   346  C C   . ARG A 1 62  ? 18.355  15.010  -1.507  1.00 21.82  ? 42  ARG A C   1 
ATOM   347  O O   . ARG A 1 62  ? 19.108  14.493  -0.692  1.00 23.54  ? 42  ARG A O   1 
ATOM   348  C CB  . ARG A 1 62  ? 18.147  13.945  -3.778  1.00 24.97  ? 42  ARG A CB  1 
ATOM   349  C CG  . ARG A 1 62  ? 19.597  13.492  -3.824  1.00 30.23  ? 42  ARG A CG  1 
ATOM   350  C CD  . ARG A 1 62  ? 19.677  11.979  -3.721  1.00 34.31  ? 42  ARG A CD  1 
ATOM   351  N NE  . ARG A 1 62  ? 19.822  11.599  -2.316  1.00 35.85  ? 42  ARG A NE  1 
ATOM   352  C CZ  . ARG A 1 62  ? 19.657  10.379  -1.839  1.00 34.26  ? 42  ARG A CZ  1 
ATOM   353  N NH1 . ARG A 1 62  ? 18.984  9.478   -2.529  1.00 32.38  ? 42  ARG A NH1 1 
ATOM   354  N NH2 . ARG A 1 62  ? 20.172  10.055  -0.631  1.00 34.01  ? 42  ARG A NH2 1 
ATOM   355  N N   . ARG A 1 63  ? 18.269  16.329  -1.718  1.00 24.13  ? 43  ARG A N   1 
ATOM   356  C CA  . ARG A 1 63  ? 18.956  17.297  -0.894  1.00 26.38  ? 43  ARG A CA  1 
ATOM   357  C C   . ARG A 1 63  ? 18.584  17.106  0.581   1.00 24.87  ? 43  ARG A C   1 
ATOM   358  O O   . ARG A 1 63  ? 19.432  17.151  1.467   1.00 24.65  ? 43  ARG A O   1 
ATOM   359  C CB  . ARG A 1 63  ? 18.550  18.656  -1.477  1.00 28.80  ? 43  ARG A CB  1 
ATOM   360  C CG  . ARG A 1 63  ? 19.303  19.867  -0.986  1.00 33.61  ? 43  ARG A CG  1 
ATOM   361  C CD  . ARG A 1 63  ? 18.803  21.067  -1.790  1.00 31.06  ? 43  ARG A CD  1 
ATOM   362  N NE  . ARG A 1 63  ? 19.698  21.519  -2.855  1.00 33.64  ? 43  ARG A NE  1 
ATOM   363  C CZ  . ARG A 1 63  ? 19.466  22.563  -3.677  1.00 33.67  ? 43  ARG A CZ  1 
ATOM   364  N NH1 . ARG A 1 63  ? 18.271  23.123  -3.724  1.00 32.95  ? 43  ARG A NH1 1 
ATOM   365  N NH2 . ARG A 1 63  ? 20.416  23.012  -4.493  1.00 29.67  ? 43  ARG A NH2 1 
ATOM   366  N N   . GLY A 1 64  ? 17.293  16.852  0.819   1.00 23.86  ? 44  GLY A N   1 
ATOM   367  C CA  . GLY A 1 64  ? 16.786  16.627  2.152   1.00 22.10  ? 44  GLY A CA  1 
ATOM   368  C C   . GLY A 1 64  ? 17.345  15.342  2.765   1.00 20.85  ? 44  GLY A C   1 
ATOM   369  O O   . GLY A 1 64  ? 17.710  15.336  3.927   1.00 20.47  ? 44  GLY A O   1 
ATOM   370  N N   . LEU A 1 65  ? 17.448  14.281  1.963   1.00 20.62  ? 45  LEU A N   1 
ATOM   371  C CA  . LEU A 1 65  ? 17.953  13.002  2.481   1.00 20.18  ? 45  LEU A CA  1 
ATOM   372  C C   . LEU A 1 65  ? 19.445  13.083  2.817   1.00 21.46  ? 45  LEU A C   1 
ATOM   373  O O   . LEU A 1 65  ? 19.916  12.457  3.764   1.00 21.06  ? 45  LEU A O   1 
ATOM   374  C CB  . LEU A 1 65  ? 17.733  11.886  1.462   1.00 21.79  ? 45  LEU A CB  1 
ATOM   375  C CG  . LEU A 1 65  ? 16.305  11.352  1.297   1.00 22.71  ? 45  LEU A CG  1 
ATOM   376  C CD1 . LEU A 1 65  ? 16.266  10.218  0.286   1.00 21.84  ? 45  LEU A CD1 1 
ATOM   377  C CD2 . LEU A 1 65  ? 15.735  10.890  2.623   1.00 23.02  ? 45  LEU A CD2 1 
ATOM   378  N N   . ASP A 1 66  ? 20.209  13.837  2.021   1.00 20.29  ? 46  ASP A N   1 
ATOM   379  C CA  . ASP A 1 66  ? 21.628  14.033  2.282   1.00 21.64  ? 46  ASP A CA  1 
ATOM   380  C C   . ASP A 1 66  ? 21.826  14.690  3.649   1.00 20.17  ? 46  ASP A C   1 
ATOM   381  O O   . ASP A 1 66  ? 22.644  14.283  4.470   1.00 21.79  ? 46  ASP A O   1 
ATOM   382  C CB  . ASP A 1 66  ? 22.248  14.861  1.155   1.00 24.48  ? 46  ASP A CB  1 
ATOM   383  C CG  . ASP A 1 66  ? 22.355  14.088  -0.144  1.00 30.54  ? 46  ASP A CG  1 
ATOM   384  O OD1 . ASP A 1 66  ? 22.215  12.814  -0.110  1.00 35.35  ? 46  ASP A OD1 1 
ATOM   385  O OD2 . ASP A 1 66  ? 22.578  14.734  -1.160  1.00 36.06  ? 46  ASP A OD2 1 
ATOM   386  N N   . ALA A 1 67  ? 21.021  15.728  3.899   1.00 19.27  ? 47  ALA A N   1 
ATOM   387  C CA  . ALA A 1 67  ? 21.115  16.446  5.151   1.00 19.89  ? 47  ALA A CA  1 
ATOM   388  C C   . ALA A 1 67  ? 20.601  15.610  6.311   1.00 19.03  ? 47  ALA A C   1 
ATOM   389  O O   . ALA A 1 67  ? 21.153  15.695  7.413   1.00 19.59  ? 47  ALA A O   1 
ATOM   390  C CB  . ALA A 1 67  ? 20.401  17.762  5.056   1.00 22.42  ? 47  ALA A CB  1 
ATOM   391  N N   . LEU A 1 68  ? 19.554  14.808  6.069   1.00 18.95  ? 48  LEU A N   1 
ATOM   392  C CA  . LEU A 1 68  ? 18.986  13.967  7.119   1.00 18.01  ? 48  LEU A CA  1 
ATOM   393  C C   . LEU A 1 68  ? 20.028  12.934  7.560   1.00 16.93  ? 48  LEU A C   1 
ATOM   394  O O   . LEU A 1 68  ? 20.208  12.696  8.758   1.00 18.25  ? 48  LEU A O   1 
ATOM   395  C CB  . LEU A 1 68  ? 17.735  13.281  6.583   1.00 18.39  ? 48  LEU A CB  1 
ATOM   396  C CG  . LEU A 1 68  ? 16.890  12.555  7.633   1.00 19.67  ? 48  LEU A CG  1 
ATOM   397  C CD1 . LEU A 1 68  ? 16.130  13.521  8.533   1.00 19.72  ? 48  LEU A CD1 1 
ATOM   398  C CD2 . LEU A 1 68  ? 15.916  11.644  6.937   1.00 20.32  ? 48  LEU A CD2 1 
ATOM   399  N N   . GLN A 1 69  ? 20.771  12.396  6.594   1.00 18.80  ? 49  GLN A N   1 
ATOM   400  C CA  . GLN A 1 69  ? 21.757  11.374  6.900   1.00 18.23  ? 49  GLN A CA  1 
ATOM   401  C C   . GLN A 1 69  ? 22.955  11.960  7.658   1.00 18.17  ? 49  GLN A C   1 
ATOM   402  O O   . GLN A 1 69  ? 23.477  11.384  8.605   1.00 20.11  ? 49  GLN A O   1 
ATOM   403  C CB  . GLN A 1 69  ? 22.192  10.686  5.615   1.00 18.72  ? 49  GLN A CB  1 
ATOM   404  C CG  . GLN A 1 69  ? 23.086  9.496   5.879   1.00 20.60  ? 49  GLN A CG  1 
ATOM   405  C CD  . GLN A 1 69  ? 23.435  8.718   4.634   1.00 21.46  ? 49  GLN A CD  1 
ATOM   406  O OE1 . GLN A 1 69  ? 23.763  9.259   3.586   1.00 22.18  ? 49  GLN A OE1 1 
ATOM   407  N NE2 . GLN A 1 69  ? 23.392  7.394   4.746   1.00 19.64  ? 49  GLN A NE2 1 
ATOM   408  N N   . ALA A 1 70  ? 23.386  13.180  7.273   1.00 18.20  ? 50  ALA A N   1 
ATOM   409  C CA  . ALA A 1 70  ? 24.453  13.817  8.012   1.00 19.50  ? 50  ALA A CA  1 
ATOM   410  C C   . ALA A 1 70  ? 24.038  14.101  9.463   1.00 19.08  ? 50  ALA A C   1 
ATOM   411  O O   . ALA A 1 70  ? 24.858  14.046  10.379  1.00 20.45  ? 50  ALA A O   1 
ATOM   412  C CB  . ALA A 1 70  ? 24.784  15.104  7.309   1.00 21.00  ? 50  ALA A CB  1 
ATOM   413  N N   . ARG A 1 71  ? 22.775  14.501  9.647   1.00 18.26  ? 51  ARG A N   1 
ATOM   414  C CA  . ARG A 1 71  ? 22.245  14.841  10.954  1.00 17.73  ? 51  ARG A CA  1 
ATOM   415  C C   . ARG A 1 71  ? 22.312  13.662  11.925  1.00 18.82  ? 51  ARG A C   1 
ATOM   416  O O   . ARG A 1 71  ? 22.648  13.861  13.086  1.00 19.00  ? 51  ARG A O   1 
ATOM   417  C CB  . ARG A 1 71  ? 20.832  15.406  10.825  1.00 18.93  ? 51  ARG A CB  1 
ATOM   418  C CG  . ARG A 1 71  ? 20.096  15.604  12.138  1.00 18.92  ? 51  ARG A CG  1 
ATOM   419  C CD  . ARG A 1 71  ? 18.731  16.231  11.907  1.00 18.56  ? 51  ARG A CD  1 
ATOM   420  N NE  . ARG A 1 71  ? 18.856  17.615  11.426  1.00 19.37  ? 51  ARG A NE  1 
ATOM   421  C CZ  . ARG A 1 71  ? 17.818  18.328  10.983  1.00 21.36  ? 51  ARG A CZ  1 
ATOM   422  N NH1 . ARG A 1 71  ? 16.603  17.806  10.991  1.00 20.42  ? 51  ARG A NH1 1 
ATOM   423  N NH2 . ARG A 1 71  ? 18.005  19.555  10.504  1.00 20.36  ? 51  ARG A NH2 1 
ATOM   424  N N   . HIS A 1 72  ? 21.932  12.456  11.457  1.00 19.17  ? 52  HIS A N   1 
ATOM   425  C CA  . HIS A 1 72  ? 21.614  11.358  12.367  1.00 19.57  ? 52  HIS A CA  1 
ATOM   426  C C   . HIS A 1 72  ? 22.614  10.205  12.228  1.00 18.11  ? 52  HIS A C   1 
ATOM   427  O O   . HIS A 1 72  ? 22.607  9.507   11.232  1.00 19.10  ? 52  HIS A O   1 
ATOM   428  C CB  . HIS A 1 72  ? 20.197  10.853  12.106  1.00 18.36  ? 52  HIS A CB  1 
ATOM   429  C CG  . HIS A 1 72  ? 19.161  11.813  12.479  1.00 18.11  ? 52  HIS A CG  1 
ATOM   430  N ND1 . HIS A 1 72  ? 18.944  12.169  13.779  1.00 18.85  ? 52  HIS A ND1 1 
ATOM   431  C CD2 . HIS A 1 72  ? 18.289  12.500  11.706  1.00 17.04  ? 52  HIS A CD2 1 
ATOM   432  C CE1 . HIS A 1 72  ? 17.954  13.059  13.784  1.00 18.20  ? 52  HIS A CE1 1 
ATOM   433  N NE2 . HIS A 1 72  ? 17.530  13.238  12.550  1.00 18.86  ? 52  HIS A NE2 1 
ATOM   434  N N   . PRO A 1 73  ? 23.519  10.020  13.199  1.00 18.87  ? 53  PRO A N   1 
ATOM   435  C CA  . PRO A 1 73  ? 24.544  8.981   13.083  1.00 19.15  ? 53  PRO A CA  1 
ATOM   436  C C   . PRO A 1 73  ? 24.010  7.568   12.824  1.00 18.03  ? 53  PRO A C   1 
ATOM   437  O O   . PRO A 1 73  ? 24.607  6.817   12.048  1.00 19.76  ? 53  PRO A O   1 
ATOM   438  C CB  . PRO A 1 73  ? 25.246  9.057   14.438  1.00 19.86  ? 53  PRO A CB  1 
ATOM   439  C CG  . PRO A 1 73  ? 25.073  10.487  14.890  1.00 22.00  ? 53  PRO A CG  1 
ATOM   440  C CD  . PRO A 1 73  ? 23.700  10.864  14.393  1.00 19.65  ? 53  PRO A CD  1 
ATOM   441  N N   . LEU A 1 74  ? 22.854  7.231   13.390  1.00 17.22  ? 54  LEU A N   1 
ATOM   442  C CA  . LEU A 1 74  ? 22.329  5.886   13.143  1.00 16.80  ? 54  LEU A CA  1 
ATOM   443  C C   . LEU A 1 74  ? 21.850  5.666   11.701  1.00 18.02  ? 54  LEU A C   1 
ATOM   444  O O   . LEU A 1 74  ? 21.620  4.521   11.300  1.00 19.70  ? 54  LEU A O   1 
ATOM   445  C CB  . LEU A 1 74  ? 21.192  5.562   14.105  1.00 18.53  ? 54  LEU A CB  1 
ATOM   446  C CG  . LEU A 1 74  ? 21.643  5.195   15.519  1.00 20.61  ? 54  LEU A CG  1 
ATOM   447  C CD1 . LEU A 1 74  ? 20.476  5.272   16.499  1.00 19.71  ? 54  LEU A CD1 1 
ATOM   448  C CD2 . LEU A 1 74  ? 22.268  3.828   15.499  1.00 21.58  ? 54  LEU A CD2 1 
ATOM   449  N N   . LEU A 1 75  ? 21.681  6.737   10.893  1.00 17.28  ? 55  LEU A N   1 
ATOM   450  C CA  . LEU A 1 75  ? 21.313  6.603   9.496   1.00 16.13  ? 55  LEU A CA  1 
ATOM   451  C C   . LEU A 1 75  ? 22.534  6.505   8.576   1.00 17.26  ? 55  LEU A C   1 
ATOM   452  O O   . LEU A 1 75  ? 22.379  6.445   7.344   1.00 19.47  ? 55  LEU A O   1 
ATOM   453  C CB  . LEU A 1 75  ? 20.466  7.813   9.135   1.00 17.14  ? 55  LEU A CB  1 
ATOM   454  C CG  . LEU A 1 75  ? 19.153  7.932   9.883   1.00 18.11  ? 55  LEU A CG  1 
ATOM   455  C CD1 . LEU A 1 75  ? 18.359  9.073   9.289   1.00 20.19  ? 55  LEU A CD1 1 
ATOM   456  C CD2 . LEU A 1 75  ? 18.360  6.651   9.887   1.00 19.65  ? 55  LEU A CD2 1 
ATOM   457  N N   . ARG A 1 76  ? 23.732  6.476   9.157   1.00 19.48  ? 56  ARG A N   1 
ATOM   458  C CA  . ARG A 1 76  ? 24.958  6.255   8.403   1.00 20.29  ? 56  ARG A CA  1 
ATOM   459  C C   . ARG A 1 76  ? 25.836  5.258   9.150   1.00 20.40  ? 56  ARG A C   1 
ATOM   460  O O   . ARG A 1 76  ? 27.044  5.408   9.251   1.00 21.52  ? 56  ARG A O   1 
ATOM   461  C CB  . ARG A 1 76  ? 25.664  7.567   8.082   1.00 22.06  ? 56  ARG A CB  1 
ATOM   462  C CG  . ARG A 1 76  ? 25.611  8.585   9.198   1.00 21.94  ? 56  ARG A CG  1 
ATOM   463  C CD  . ARG A 1 76  ? 26.315  9.844   8.728   1.00 22.95  ? 56  ARG A CD  1 
ATOM   464  N NE  . ARG A 1 76  ? 26.129  10.894  9.713   1.00 22.15  ? 56  ARG A NE  1 
ATOM   465  C CZ  . ARG A 1 76  ? 26.814  11.018  10.839  1.00 23.49  ? 56  ARG A CZ  1 
ATOM   466  N NH1 . ARG A 1 76  ? 26.488  11.953  11.711  1.00 26.43  ? 56  ARG A NH1 1 
ATOM   467  N NH2 . ARG A 1 76  ? 27.794  10.184  11.131  1.00 24.57  ? 56  ARG A NH2 1 
ATOM   468  N N   . ALA A 1 77  ? 25.170  4.187   9.586   1.00 20.74  ? 57  ALA A N   1 
ATOM   469  C CA  . ALA A 1 77  ? 25.824  3.092   10.287  1.00 22.40  ? 57  ALA A CA  1 
ATOM   470  C C   . ALA A 1 77  ? 25.399  1.792   9.615   1.00 20.99  ? 57  ALA A C   1 
ATOM   471  O O   . ALA A 1 77  ? 24.322  1.721   9.020   1.00 21.88  ? 57  ALA A O   1 
ATOM   472  C CB  . ALA A 1 77  ? 25.473  3.081   11.759  1.00 22.57  ? 57  ALA A CB  1 
ATOM   473  N N   . ARG A 1 78  ? 26.249  0.774   9.746   1.00 20.17  ? 58  ARG A N   1 
ATOM   474  C CA  . ARG A 1 78  ? 25.902  -0.574  9.303   1.00 20.68  ? 58  ARG A CA  1 
ATOM   475  C C   . ARG A 1 78  ? 26.447  -1.552  10.328  1.00 20.42  ? 58  ARG A C   1 
ATOM   476  O O   . ARG A 1 78  ? 27.153  -1.158  11.256  1.00 20.20  ? 58  ARG A O   1 
ATOM   477  C CB  . ARG A 1 78  ? 26.481  -0.853  7.917   1.00 21.72  ? 58  ARG A CB  1 
ATOM   478  C CG  . ARG A 1 78  ? 27.997  -0.715  7.854   1.00 24.18  ? 58  ARG A CG  1 
ATOM   479  C CD  . ARG A 1 78  ? 28.518  -0.753  6.451   1.00 24.37  ? 58  ARG A CD  1 
ATOM   480  N NE  . ARG A 1 78  ? 29.949  -0.938  6.435   1.00 28.10  ? 58  ARG A NE  1 
ATOM   481  C CZ  . ARG A 1 78  ? 30.586  -2.080  6.730   1.00 30.86  ? 58  ARG A CZ  1 
ATOM   482  N NH1 . ARG A 1 78  ? 29.947  -3.242  6.824   1.00 32.54  ? 58  ARG A NH1 1 
ATOM   483  N NH2 . ARG A 1 78  ? 31.896  -2.067  6.827   1.00 33.55  ? 58  ARG A NH2 1 
ATOM   484  N N   . ILE A 1 79  ? 26.149  -2.837  10.109  1.00 23.13  ? 59  ILE A N   1 
ATOM   485  C CA  . ILE A 1 79  ? 26.477  -3.890  11.056  1.00 23.85  ? 59  ILE A CA  1 
ATOM   486  C C   . ILE A 1 79  ? 27.550  -4.810  10.482  1.00 23.81  ? 59  ILE A C   1 
ATOM   487  O O   . ILE A 1 79  ? 27.436  -5.303  9.376   1.00 27.68  ? 59  ILE A O   1 
ATOM   488  C CB  . ILE A 1 79  ? 25.204  -4.665  11.432  1.00 24.21  ? 59  ILE A CB  1 
ATOM   489  C CG1 . ILE A 1 79  ? 24.185  -3.762  12.136  1.00 25.75  ? 59  ILE A CG1 1 
ATOM   490  C CG2 . ILE A 1 79  ? 25.545  -5.913  12.249  1.00 26.18  ? 59  ILE A CG2 1 
ATOM   491  C CD1 . ILE A 1 79  ? 22.900  -4.469  12.507  1.00 29.65  ? 59  ILE A CD1 1 
ATOM   492  N N   . GLU A 1 80  ? 28.606  -4.980  11.271  1.00 26.67  ? 60  GLU A N   1 
ATOM   493  C CA  . GLU A 1 80  ? 29.706  -5.882  11.012  1.00 29.25  ? 60  GLU A CA  1 
ATOM   494  C C   . GLU A 1 80  ? 29.532  -7.034  11.993  1.00 30.50  ? 60  GLU A C   1 
ATOM   495  O O   . GLU A 1 80  ? 29.139  -6.831  13.151  1.00 30.37  ? 60  GLU A O   1 
ATOM   496  C CB  . GLU A 1 80  ? 30.984  -5.046  11.144  1.00 34.73  ? 60  GLU A CB  1 
ATOM   497  C CG  . GLU A 1 80  ? 32.297  -5.784  11.215  1.00 39.89  ? 60  GLU A CG  1 
ATOM   498  C CD  . GLU A 1 80  ? 33.469  -4.815  11.345  1.00 44.17  ? 60  GLU A CD  1 
ATOM   499  O OE1 . GLU A 1 80  ? 33.833  -4.192  10.302  1.00 48.32  ? 60  GLU A OE1 1 
ATOM   500  O OE2 . GLU A 1 80  ? 33.991  -4.637  12.507  1.00 43.70  ? 60  GLU A OE2 1 
ATOM   501  N N   . HIS A 1 81  ? 29.767  -8.253  11.492  1.00 29.52  ? 61  HIS A N   1 
ATOM   502  C CA  . HIS A 1 81  ? 29.691  -9.430  12.339  1.00 31.21  ? 61  HIS A CA  1 
ATOM   503  C C   . HIS A 1 81  ? 30.685  -10.486 11.873  1.00 33.33  ? 61  HIS A C   1 
ATOM   504  O O   . HIS A 1 81  ? 31.221  -10.387 10.777  1.00 34.33  ? 61  HIS A O   1 
ATOM   505  C CB  . HIS A 1 81  ? 28.262  -9.974  12.410  1.00 29.28  ? 61  HIS A CB  1 
ATOM   506  C CG  . HIS A 1 81  ? 27.679  -10.261 11.084  1.00 31.07  ? 61  HIS A CG  1 
ATOM   507  N ND1 . HIS A 1 81  ? 27.793  -11.491 10.488  1.00 32.88  ? 61  HIS A ND1 1 
ATOM   508  C CD2 . HIS A 1 81  ? 27.021  -9.479  10.214  1.00 31.18  ? 61  HIS A CD2 1 
ATOM   509  C CE1 . HIS A 1 81  ? 27.167  -11.458 9.319   1.00 32.58  ? 61  HIS A CE1 1 
ATOM   510  N NE2 . HIS A 1 81  ? 26.716  -10.244 9.123   1.00 32.94  ? 61  HIS A NE2 1 
ATOM   511  N N   . ASP A 1 82  ? 30.908  -11.496 12.726  1.00 34.13  ? 62  ASP A N   1 
ATOM   512  C CA  . ASP A 1 82  ? 31.779  -12.616 12.385  1.00 38.30  ? 62  ASP A CA  1 
ATOM   513  C C   . ASP A 1 82  ? 30.951  -13.885 12.182  1.00 39.80  ? 62  ASP A C   1 
ATOM   514  O O   . ASP A 1 82  ? 30.701  -14.610 13.147  1.00 39.50  ? 62  ASP A O   1 
ATOM   515  C CB  . ASP A 1 82  ? 32.838  -12.831 13.468  1.00 39.66  ? 62  ASP A CB  1 
ATOM   516  C CG  . ASP A 1 82  ? 33.607  -11.559 13.761  1.00 42.11  ? 62  ASP A CG  1 
ATOM   517  O OD1 . ASP A 1 82  ? 34.070  -10.946 12.793  1.00 43.20  ? 62  ASP A OD1 1 
ATOM   518  O OD2 . ASP A 1 82  ? 33.687  -11.168 14.943  1.00 41.31  ? 62  ASP A OD2 1 
ATOM   519  N N   . ALA A 1 83  ? 30.551  -14.149 10.925  1.00 38.26  ? 63  ALA A N   1 
ATOM   520  C CA  . ALA A 1 83  ? 29.687  -15.279 10.609  1.00 41.70  ? 63  ALA A CA  1 
ATOM   521  C C   . ALA A 1 83  ? 28.491  -15.315 11.561  1.00 36.82  ? 63  ALA A C   1 
ATOM   522  O O   . ALA A 1 83  ? 28.136  -16.357 12.094  1.00 38.19  ? 63  ALA A O   1 
ATOM   523  C CB  . ALA A 1 83  ? 30.458  -16.532 10.740  0.50 30.00  ? 63  ALA A CB  1 
ATOM   524  N N   . GLY A 1 84  ? 27.916  -14.142 11.831  1.00 36.68  ? 64  GLY A N   1 
ATOM   525  C CA  . GLY A 1 84  ? 26.694  -14.031 12.610  1.00 34.46  ? 64  GLY A CA  1 
ATOM   526  C C   . GLY A 1 84  ? 26.940  -13.841 14.107  1.00 35.52  ? 64  GLY A C   1 
ATOM   527  O O   . GLY A 1 84  ? 25.959  -13.726 14.844  1.00 37.52  ? 64  GLY A O   1 
ATOM   528  N N   . LEU A 1 85  ? 28.216  -13.765 14.547  1.00 35.37  ? 65  LEU A N   1 
ATOM   529  C CA  . LEU A 1 85  ? 28.538  -13.538 15.954  1.00 35.43  ? 65  LEU A CA  1 
ATOM   530  C C   . LEU A 1 85  ? 29.046  -12.113 16.179  1.00 36.92  ? 65  LEU A C   1 
ATOM   531  O O   . LEU A 1 85  ? 29.620  -11.515 15.277  1.00 35.05  ? 65  LEU A O   1 
ATOM   532  C CB  . LEU A 1 85  ? 29.591  -14.561 16.390  1.00 38.26  ? 65  LEU A CB  1 
ATOM   533  C CG  . LEU A 1 85  ? 29.247  -16.028 16.130  1.00 37.33  ? 65  LEU A CG  1 
ATOM   534  C CD1 . LEU A 1 85  ? 30.305  -16.947 16.728  0.30 37.61  ? 65  LEU A CD1 1 
ATOM   535  C CD2 . LEU A 1 85  ? 27.874  -16.375 16.674  1.00 36.18  ? 65  LEU A CD2 1 
ATOM   536  N N   . ASP A 1 86  ? 28.822  -11.598 17.405  1.00 38.92  ? 66  ASP A N   1 
ATOM   537  C CA  . ASP A 1 86  ? 29.421  -10.358 17.903  1.00 37.63  ? 66  ASP A CA  1 
ATOM   538  C C   . ASP A 1 86  ? 29.122  -9.205  16.952  1.00 34.40  ? 66  ASP A C   1 
ATOM   539  O O   . ASP A 1 86  ? 30.015  -8.479  16.521  1.00 34.76  ? 66  ASP A O   1 
ATOM   540  C CB  . ASP A 1 86  ? 30.926  -10.521 18.153  1.00 40.41  ? 66  ASP A CB  1 
ATOM   541  C CG  . ASP A 1 86  ? 31.211  -11.591 19.193  1.00 43.50  ? 66  ASP A CG  1 
ATOM   542  O OD1 . ASP A 1 86  ? 30.575  -11.525 20.282  1.00 44.14  ? 66  ASP A OD1 1 
ATOM   543  O OD2 . ASP A 1 86  ? 32.035  -12.496 18.908  1.00 45.47  ? 66  ASP A OD2 1 
ATOM   544  N N   . PRO A 1 87  ? 27.838  -8.962  16.638  1.00 30.67  ? 67  PRO A N   1 
ATOM   545  C CA  . PRO A 1 87  ? 27.481  -7.852  15.758  1.00 29.21  ? 67  PRO A CA  1 
ATOM   546  C C   . PRO A 1 87  ? 27.874  -6.516  16.377  1.00 27.31  ? 67  PRO A C   1 
ATOM   547  O O   . PRO A 1 87  ? 27.713  -6.303  17.575  1.00 26.26  ? 67  PRO A O   1 
ATOM   548  C CB  . PRO A 1 87  ? 25.969  -7.997  15.627  1.00 30.18  ? 67  PRO A CB  1 
ATOM   549  C CG  . PRO A 1 87  ? 25.565  -8.658  16.918  1.00 28.18  ? 67  PRO A CG  1 
ATOM   550  C CD  . PRO A 1 87  ? 26.663  -9.676  17.159  1.00 29.96  ? 67  PRO A CD  1 
ATOM   551  N N   . ARG A 1 88  ? 28.353  -5.599  15.535  1.00 27.74  ? 68  ARG A N   1 
ATOM   552  C CA  . ARG A 1 88  ? 28.762  -4.289  16.009  1.00 27.32  ? 68  ARG A CA  1 
ATOM   553  C C   . ARG A 1 88  ? 28.461  -3.255  14.936  1.00 25.23  ? 68  ARG A C   1 
ATOM   554  O O   . ARG A 1 88  ? 28.452  -3.558  13.761  1.00 25.71  ? 68  ARG A O   1 
ATOM   555  C CB  . ARG A 1 88  ? 30.259  -4.264  16.336  1.00 29.18  ? 68  ARG A CB  1 
ATOM   556  C CG  . ARG A 1 88  ? 31.144  -4.760  15.208  1.00 31.41  ? 68  ARG A CG  1 
ATOM   557  C CD  . ARG A 1 88  ? 32.390  -5.445  15.700  1.00 32.78  ? 68  ARG A CD  1 
ATOM   558  N NE  . ARG A 1 88  ? 32.989  -6.211  14.614  1.00 34.82  ? 68  ARG A NE  1 
ATOM   559  C CZ  . ARG A 1 88  ? 33.024  -7.545  14.538  1.00 36.71  ? 68  ARG A CZ  1 
ATOM   560  N NH1 . ARG A 1 88  ? 32.445  -8.295  15.464  1.00 34.25  ? 68  ARG A NH1 1 
ATOM   561  N NH2 . ARG A 1 88  ? 33.668  -8.124  13.534  1.00 40.38  ? 68  ARG A NH2 1 
ATOM   562  N N   . TRP A 1 89  ? 28.233  -2.021  15.392  1.00 21.75  ? 69  TRP A N   1 
ATOM   563  C CA  . TRP A 1 89  ? 28.023  -0.907  14.485  1.00 22.79  ? 69  TRP A CA  1 
ATOM   564  C C   . TRP A 1 89  ? 29.349  -0.332  13.992  1.00 22.09  ? 69  TRP A C   1 
ATOM   565  O O   . TRP A 1 89  ? 30.263  -0.120  14.779  1.00 22.92  ? 69  TRP A O   1 
ATOM   566  C CB  . TRP A 1 89  ? 27.240  0.174   15.196  1.00 22.74  ? 69  TRP A CB  1 
ATOM   567  C CG  . TRP A 1 89  ? 25.887  -0.209  15.713  1.00 22.68  ? 69  TRP A CG  1 
ATOM   568  C CD1 . TRP A 1 89  ? 25.535  -0.412  17.011  1.00 22.07  ? 69  TRP A CD1 1 
ATOM   569  C CD2 . TRP A 1 89  ? 24.675  -0.313  14.946  1.00 22.58  ? 69  TRP A CD2 1 
ATOM   570  N NE1 . TRP A 1 89  ? 24.193  -0.686  17.100  1.00 23.36  ? 69  TRP A NE1 1 
ATOM   571  C CE2 . TRP A 1 89  ? 23.632  -0.615  15.851  1.00 21.18  ? 69  TRP A CE2 1 
ATOM   572  C CE3 . TRP A 1 89  ? 24.375  -0.206  13.583  1.00 22.30  ? 69  TRP A CE3 1 
ATOM   573  C CZ2 . TRP A 1 89  ? 22.313  -0.786  15.428  1.00 22.83  ? 69  TRP A CZ2 1 
ATOM   574  C CZ3 . TRP A 1 89  ? 23.070  -0.371  13.170  1.00 21.95  ? 69  TRP A CZ3 1 
ATOM   575  C CH2 . TRP A 1 89  ? 22.058  -0.671  14.079  1.00 22.15  ? 69  TRP A CH2 1 
ATOM   576  N N   . VAL A 1 90  ? 29.381  -0.022  12.693  1.00 21.46  ? 70  VAL A N   1 
ATOM   577  C CA  . VAL A 1 90  ? 30.479  0.691   12.060  1.00 23.74  ? 70  VAL A CA  1 
ATOM   578  C C   . VAL A 1 90  ? 29.899  1.729   11.099  1.00 22.68  ? 70  VAL A C   1 
ATOM   579  O O   . VAL A 1 90  ? 28.731  1.674   10.703  1.00 22.48  ? 70  VAL A O   1 
ATOM   580  C CB  . VAL A 1 90  ? 31.450  -0.247  11.331  1.00 25.46  ? 70  VAL A CB  1 
ATOM   581  C CG1 . VAL A 1 90  ? 32.167  -1.202  12.286  1.00 26.16  ? 70  VAL A CG1 1 
ATOM   582  C CG2 . VAL A 1 90  ? 30.758  -1.013  10.225  1.00 26.81  ? 70  VAL A CG2 1 
ATOM   583  N N   . PRO A 1 91  ? 30.692  2.717   10.655  1.00 25.63  ? 71  PRO A N   1 
ATOM   584  C CA  . PRO A 1 91  ? 30.161  3.687   9.702   1.00 23.63  ? 71  PRO A CA  1 
ATOM   585  C C   . PRO A 1 91  ? 29.780  3.046   8.368   1.00 22.75  ? 71  PRO A C   1 
ATOM   586  O O   . PRO A 1 91  ? 30.390  2.068   7.934   1.00 25.13  ? 71  PRO A O   1 
ATOM   587  C CB  . PRO A 1 91  ? 31.311  4.686   9.534   1.00 25.67  ? 71  PRO A CB  1 
ATOM   588  C CG  . PRO A 1 91  ? 32.042  4.580   10.819  1.00 28.65  ? 71  PRO A CG  1 
ATOM   589  C CD  . PRO A 1 91  ? 32.032  3.089   11.118  1.00 28.84  ? 71  PRO A CD  1 
ATOM   590  N N   . CYS A 1 92  ? 28.745  3.622   7.765   1.00 21.91  ? 72  CYS A N   1 
ATOM   591  C CA  . CYS A 1 92  ? 28.235  3.269   6.450   1.00 19.35  ? 72  CYS A CA  1 
ATOM   592  C C   . CYS A 1 92  ? 28.411  4.476   5.538   1.00 22.19  ? 72  CYS A C   1 
ATOM   593  O O   . CYS A 1 92  ? 28.055  5.578   5.942   1.00 23.93  ? 72  CYS A O   1 
ATOM   594  C CB  . CYS A 1 92  ? 26.765  2.880   6.579   1.00 20.90  ? 72  CYS A CB  1 
ATOM   595  S SG  . CYS A 1 92  ? 25.912  2.634   5.015   1.00 24.82  ? 72  CYS A SG  1 
ATOM   596  N N   . GLU A 1 93  ? 28.994  4.261   4.357   1.00 23.79  ? 73  GLU A N   1 
ATOM   597  C CA  . GLU A 1 93  ? 29.292  5.355   3.445   1.00 24.83  ? 73  GLU A CA  1 
ATOM   598  C C   . GLU A 1 93  ? 28.273  5.419   2.308   1.00 25.61  ? 73  GLU A C   1 
ATOM   599  O O   . GLU A 1 93  ? 28.440  6.217   1.384   1.00 29.45  ? 73  GLU A O   1 
ATOM   600  C CB  . GLU A 1 93  ? 30.693  5.189   2.843   1.00 28.87  ? 73  GLU A CB  1 
ATOM   601  C CG  . GLU A 1 93  ? 31.794  5.134   3.893   1.00 32.26  ? 73  GLU A CG  1 
ATOM   602  C CD  . GLU A 1 93  ? 33.192  4.782   3.400   1.00 40.57  ? 73  GLU A CD  1 
ATOM   603  O OE1 . GLU A 1 93  ? 34.152  5.168   4.111   0.70 47.49  ? 73  GLU A OE1 1 
ATOM   604  O OE2 . GLU A 1 93  ? 33.336  4.099   2.328   1.00 47.11  ? 73  GLU A OE2 1 
ATOM   605  N N   . ARG A 1 94  ? 27.231  4.597   2.369   1.00 23.48  ? 74  ARG A N   1 
ATOM   606  C CA  . ARG A 1 94  ? 26.226  4.560   1.327   1.00 23.06  ? 74  ARG A CA  1 
ATOM   607  C C   . ARG A 1 94  ? 25.113  5.556   1.642   1.00 21.10  ? 74  ARG A C   1 
ATOM   608  O O   . ARG A 1 94  ? 24.759  5.759   2.810   1.00 19.99  ? 74  ARG A O   1 
ATOM   609  C CB  . ARG A 1 94  ? 25.631  3.150   1.214   1.00 25.01  ? 74  ARG A CB  1 
ATOM   610  C CG  . ARG A 1 94  ? 26.623  2.108   0.715   1.00 26.94  ? 74  ARG A CG  1 
ATOM   611  C CD  . ARG A 1 94  ? 25.990  0.738   0.735   1.00 30.36  ? 74  ARG A CD  1 
ATOM   612  N NE  . ARG A 1 94  ? 26.978  -0.266  0.328   1.00 36.59  ? 74  ARG A NE  1 
ATOM   613  C CZ  . ARG A 1 94  ? 27.257  -0.607  -0.926  1.00 43.17  ? 74  ARG A CZ  1 
ATOM   614  N NH1 . ARG A 1 94  ? 26.561  -0.097  -1.927  1.00 43.95  ? 74  ARG A NH1 1 
ATOM   615  N NH2 . ARG A 1 94  ? 28.232  -1.470  -1.170  1.00 48.72  ? 74  ARG A NH2 1 
ATOM   616  N N   . PRO A 1 95  ? 24.527  6.196   0.612   1.00 22.40  ? 75  PRO A N   1 
ATOM   617  C CA  . PRO A 1 95  ? 23.454  7.176   0.832   1.00 21.59  ? 75  PRO A CA  1 
ATOM   618  C C   . PRO A 1 95  ? 22.119  6.506   1.141   1.00 20.66  ? 75  PRO A C   1 
ATOM   619  O O   . PRO A 1 95  ? 21.920  5.296   0.905   1.00 21.03  ? 75  PRO A O   1 
ATOM   620  C CB  . PRO A 1 95  ? 23.358  7.886   -0.516  1.00 23.43  ? 75  PRO A CB  1 
ATOM   621  C CG  . PRO A 1 95  ? 23.756  6.820   -1.495  1.00 24.82  ? 75  PRO A CG  1 
ATOM   622  C CD  . PRO A 1 95  ? 24.860  6.040   -0.806  1.00 23.11  ? 75  PRO A CD  1 
ATOM   623  N N   . ILE A 1 96  ? 21.182  7.294   1.649   1.00 20.33  ? 76  ILE A N   1 
ATOM   624  C CA  . ILE A 1 96  ? 19.823  6.814   1.824   1.00 18.85  ? 76  ILE A CA  1 
ATOM   625  C C   . ILE A 1 96  ? 19.168  6.657   0.451   1.00 18.95  ? 76  ILE A C   1 
ATOM   626  O O   . ILE A 1 96  ? 19.014  7.612   -0.306  1.00 20.57  ? 76  ILE A O   1 
ATOM   627  C CB  . ILE A 1 96  ? 18.973  7.725   2.716   1.00 18.98  ? 76  ILE A CB  1 
ATOM   628  C CG1 . ILE A 1 96  ? 19.589  7.936   4.094   1.00 19.12  ? 76  ILE A CG1 1 
ATOM   629  C CG2 . ILE A 1 96  ? 17.538  7.220   2.765   1.00 19.16  ? 76  ILE A CG2 1 
ATOM   630  C CD1 . ILE A 1 96  ? 18.915  9.013   4.907   1.00 20.70  ? 76  ILE A CD1 1 
ATOM   631  N N   . PRO A 1 97  ? 18.683  5.449   0.114   1.00 18.69  ? 77  PRO A N   1 
ATOM   632  C CA  . PRO A 1 97  ? 18.004  5.236   -1.141  1.00 19.43  ? 77  PRO A CA  1 
ATOM   633  C C   . PRO A 1 97  ? 16.626  5.906   -1.235  1.00 19.10  ? 77  PRO A C   1 
ATOM   634  O O   . PRO A 1 97  ? 15.928  5.958   -0.263  1.00 20.24  ? 77  PRO A O   1 
ATOM   635  C CB  . PRO A 1 97  ? 17.822  3.706   -1.215  1.00 22.53  ? 77  PRO A CB  1 
ATOM   636  C CG  . PRO A 1 97  ? 18.728  3.146   -0.161  1.00 24.65  ? 77  PRO A CG  1 
ATOM   637  C CD  . PRO A 1 97  ? 18.745  4.211   0.906   1.00 19.86  ? 77  PRO A CD  1 
ATOM   638  N N   . LEU A 1 98  ? 16.302  6.394   -2.425  1.00 20.13  ? 78  LEU A N   1 
ATOM   639  C CA  . LEU A 1 98  ? 14.980  6.997   -2.693  1.00 19.66  ? 78  LEU A CA  1 
ATOM   640  C C   . LEU A 1 98  ? 14.426  6.307   -3.940  1.00 20.22  ? 78  LEU A C   1 
ATOM   641  O O   . LEU A 1 98  ? 15.022  6.433   -4.997  1.00 24.48  ? 78  LEU A O   1 
ATOM   642  C CB  . LEU A 1 98  ? 15.121  8.514   -2.911  1.00 20.79  ? 78  LEU A CB  1 
ATOM   643  C CG  . LEU A 1 98  ? 13.842  9.253   -3.301  1.00 23.66  ? 78  LEU A CG  1 
ATOM   644  C CD1 . LEU A 1 98  ? 12.708  8.931   -2.341  1.00 24.54  ? 78  LEU A CD1 1 
ATOM   645  C CD2 . LEU A 1 98  ? 14.086  10.754  -3.359  1.00 23.56  ? 78  LEU A CD2 1 
ATOM   646  N N   . ARG A 1 99  ? 13.358  5.553   -3.770  1.00 18.71  ? 79  ARG A N   1 
ATOM   647  C CA  . ARG A 1 99  ? 12.716  4.875   -4.884  1.00 20.13  ? 79  ARG A CA  1 
ATOM   648  C C   . ARG A 1 99  ? 11.532  5.731   -5.341  1.00 21.97  ? 79  ARG A C   1 
ATOM   649  O O   . ARG A 1 99  ? 10.658  6.064   -4.544  1.00 22.62  ? 79  ARG A O   1 
ATOM   650  C CB  . ARG A 1 99  ? 12.304  3.471   -4.446  1.00 20.61  ? 79  ARG A CB  1 
ATOM   651  C CG  . ARG A 1 99  ? 11.597  2.693   -5.539  1.00 21.58  ? 79  ARG A CG  1 
ATOM   652  C CD  . ARG A 1 99  ? 11.471  1.230   -5.189  1.00 23.41  ? 79  ARG A CD  1 
ATOM   653  N NE  . ARG A 1 99  ? 10.569  0.949   -4.082  1.00 23.12  ? 79  ARG A NE  1 
ATOM   654  C CZ  . ARG A 1 99  ? 9.254   0.766   -4.157  1.00 21.79  ? 79  ARG A CZ  1 
ATOM   655  N NH1 . ARG A 1 99  ? 8.636   0.840   -5.315  1.00 23.44  ? 79  ARG A NH1 1 
ATOM   656  N NH2 . ARG A 1 99  ? 8.549   0.491   -3.071  1.00 23.83  ? 79  ARG A NH2 1 
ATOM   657  N N   . GLU A 1 100 ? 11.534  6.084   -6.625  1.00 23.58  ? 80  GLU A N   1 
ATOM   658  C CA  . GLU A 1 100 ? 10.412  6.775   -7.234  1.00 25.22  ? 80  GLU A CA  1 
ATOM   659  C C   . GLU A 1 100 ? 9.415   5.771   -7.820  1.00 26.72  ? 80  GLU A C   1 
ATOM   660  O O   . GLU A 1 100 ? 9.792   4.849   -8.555  1.00 30.54  ? 80  GLU A O   1 
ATOM   661  C CB  . GLU A 1 100 ? 10.880  7.676   -8.360  1.00 28.84  ? 80  GLU A CB  1 
ATOM   662  C CG  . GLU A 1 100 ? 11.678  8.861   -7.910  1.00 32.96  ? 80  GLU A CG  1 
ATOM   663  C CD  . GLU A 1 100 ? 12.077  9.709   -9.115  1.00 38.46  ? 80  GLU A CD  1 
ATOM   664  O OE1 . GLU A 1 100 ? 13.270  9.731   -9.425  1.00 43.41  ? 80  GLU A OE1 1 
ATOM   665  O OE2 . GLU A 1 100 ? 11.180  10.293  -9.775  1.00 44.30  ? 80  GLU A OE2 1 
ATOM   666  N N   . VAL A 1 101 ? 8.140   6.008   -7.520  1.00 25.79  ? 81  VAL A N   1 
ATOM   667  C CA  . VAL A 1 101 ? 7.016   5.330   -8.135  1.00 25.39  ? 81  VAL A CA  1 
ATOM   668  C C   . VAL A 1 101 ? 6.262   6.388   -8.926  1.00 25.45  ? 81  VAL A C   1 
ATOM   669  O O   . VAL A 1 101 ? 5.822   7.383   -8.357  1.00 25.36  ? 81  VAL A O   1 
ATOM   670  C CB  . VAL A 1 101 ? 6.125   4.640   -7.077  1.00 25.68  ? 81  VAL A CB  1 
ATOM   671  C CG1 . VAL A 1 101 ? 4.910   3.956   -7.703  1.00 25.89  ? 81  VAL A CG1 1 
ATOM   672  C CG2 . VAL A 1 101 ? 6.926   3.665   -6.223  1.00 25.42  ? 81  VAL A CG2 1 
ATOM   673  N N   . ARG A 1 102 ? 6.174   6.138   -10.240 1.00 29.32  ? 82  ARG A N   1 
ATOM   674  C CA  . ARG A 1 102 ? 5.779   7.097   -11.249 1.00 31.99  ? 82  ARG A CA  1 
ATOM   675  C C   . ARG A 1 102 ? 4.339   6.733   -11.607 1.00 32.79  ? 82  ARG A C   1 
ATOM   676  O O   . ARG A 1 102 ? 4.063   5.973   -12.525 1.00 38.70  ? 82  ARG A O   1 
ATOM   677  C CB  . ARG A 1 102 ? 6.745   7.035   -12.447 1.00 33.85  ? 82  ARG A CB  1 
ATOM   678  C CG  . ARG A 1 102 ? 8.231   7.158   -12.120 0.70 33.79  ? 82  ARG A CG  1 
ATOM   679  C CD  . ARG A 1 102 ? 9.135   6.799   -13.301 0.70 36.77  ? 82  ARG A CD  1 
ATOM   680  N NE  . ARG A 1 102 ? 10.555  6.715   -12.966 1.00 38.78  ? 82  ARG A NE  1 
ATOM   681  C CZ  . ARG A 1 102 ? 11.323  7.768   -12.737 1.00 40.50  ? 82  ARG A CZ  1 
ATOM   682  N NH1 . ARG A 1 102 ? 12.543  7.611   -12.258 1.00 41.92  ? 82  ARG A NH1 1 
ATOM   683  N NH2 . ARG A 1 102 ? 10.846  8.981   -12.948 0.70 43.75  ? 82  ARG A NH2 1 
ATOM   684  N N   . GLY A 1 103 ? 3.419   7.216   -10.800 1.00 28.60  ? 83  GLY A N   1 
ATOM   685  C CA  . GLY A 1 103 ? 2.007   7.023   -11.040 1.00 29.09  ? 83  GLY A CA  1 
ATOM   686  C C   . GLY A 1 103 ? 1.402   6.212   -9.903  1.00 28.07  ? 83  GLY A C   1 
ATOM   687  O O   . GLY A 1 103 ? 2.100   5.578   -9.116  1.00 31.41  ? 83  GLY A O   1 
ATOM   688  N N   . GLY A 1 104 ? 0.087   6.268   -9.810  1.00 27.11  ? 84  GLY A N   1 
ATOM   689  C CA  . GLY A 1 104 ? -0.602  5.448   -8.839  1.00 25.62  ? 84  GLY A CA  1 
ATOM   690  C C   . GLY A 1 104 ? -1.926  6.064   -8.433  1.00 24.44  ? 84  GLY A C   1 
ATOM   691  O O   . GLY A 1 104 ? -2.093  7.277   -8.417  1.00 24.64  ? 84  GLY A O   1 
ATOM   692  N N   . GLY A 1 105 ? -2.855  5.194   -8.085  1.00 25.20  ? 85  GLY A N   1 
ATOM   693  C CA  . GLY A 1 105 ? -4.121  5.628   -7.549  1.00 24.23  ? 85  GLY A CA  1 
ATOM   694  C C   . GLY A 1 105 ? -4.002  5.943   -6.067  1.00 23.74  ? 85  GLY A C   1 
ATOM   695  O O   . GLY A 1 105 ? -2.898  5.935   -5.492  1.00 24.19  ? 85  GLY A O   1 
ATOM   696  N N   A GLU A 1 106 ? -5.169  6.195   -5.464  0.50 25.84  ? 86  GLU A N   1 
ATOM   697  N N   B GLU A 1 106 ? -5.179  6.203   -5.482  0.50 24.85  ? 86  GLU A N   1 
ATOM   698  C CA  A GLU A 1 106 ? -5.277  6.642   -4.091  0.50 25.97  ? 86  GLU A CA  1 
ATOM   699  C CA  B GLU A 1 106 ? -5.349  6.615   -4.102  0.50 24.18  ? 86  GLU A CA  1 
ATOM   700  C C   A GLU A 1 106 ? -4.716  5.609   -3.118  0.50 25.02  ? 86  GLU A C   1 
ATOM   701  C C   B GLU A 1 106 ? -4.710  5.615   -3.141  0.50 24.21  ? 86  GLU A C   1 
ATOM   702  O O   A GLU A 1 106 ? -4.302  5.989   -2.037  0.50 27.49  ? 86  GLU A O   1 
ATOM   703  O O   B GLU A 1 106 ? -4.223  6.028   -2.103  0.50 26.54  ? 86  GLU A O   1 
ATOM   704  C CB  A GLU A 1 106 ? -6.733  6.991   -3.774  0.50 27.35  ? 86  GLU A CB  1 
ATOM   705  C CB  B GLU A 1 106 ? -6.843  6.809   -3.815  0.50 24.37  ? 86  GLU A CB  1 
ATOM   706  C CG  A GLU A 1 106 ? -7.149  8.339   -4.342  0.50 28.62  ? 86  GLU A CG  1 
ATOM   707  C CG  B GLU A 1 106 ? -7.181  6.921   -2.338  0.50 24.10  ? 86  GLU A CG  1 
ATOM   708  C CD  A GLU A 1 106 ? -6.230  9.482   -3.925  0.50 28.66  ? 86  GLU A CD  1 
ATOM   709  C CD  B GLU A 1 106 ? -6.419  8.018   -1.610  0.50 25.42  ? 86  GLU A CD  1 
ATOM   710  O OE1 A GLU A 1 106 ? -6.149  9.745   -2.712  0.50 34.32  ? 86  GLU A OE1 1 
ATOM   711  O OE1 B GLU A 1 106 ? -5.935  8.915   -2.297  0.50 25.90  ? 86  GLU A OE1 1 
ATOM   712  O OE2 A GLU A 1 106 ? -5.580  10.088  -4.789  0.50 23.52  ? 86  GLU A OE2 1 
ATOM   713  O OE2 B GLU A 1 106 ? -6.275  7.949   -0.363  0.50 26.67  ? 86  GLU A OE2 1 
ATOM   714  N N   . GLU A 1 107 ? -4.725  4.317   -3.480  1.00 24.03  ? 87  GLU A N   1 
ATOM   715  C CA  . GLU A 1 107 ? -4.228  3.271   -2.596  1.00 25.24  ? 87  GLU A CA  1 
ATOM   716  C C   . GLU A 1 107 ? -2.878  2.700   -3.019  1.00 22.14  ? 87  GLU A C   1 
ATOM   717  O O   . GLU A 1 107 ? -2.423  1.702   -2.460  1.00 22.28  ? 87  GLU A O   1 
ATOM   718  C CB  . GLU A 1 107 ? -5.267  2.159   -2.452  1.00 28.27  ? 87  GLU A CB  1 
ATOM   719  C CG  . GLU A 1 107 ? -6.473  2.632   -1.639  1.00 34.15  ? 87  GLU A CG  1 
ATOM   720  C CD  . GLU A 1 107 ? -7.424  1.532   -1.205  1.00 38.37  ? 87  GLU A CD  1 
ATOM   721  O OE1 . GLU A 1 107 ? -7.685  0.660   -2.026  1.00 45.46  ? 87  GLU A OE1 1 
ATOM   722  O OE2 . GLU A 1 107 ? -7.923  1.574   -0.072  1.00 43.18  ? 87  GLU A OE2 1 
ATOM   723  N N   . GLN A 1 108 ? -2.154  3.387   -3.897  1.00 21.55  ? 88  GLN A N   1 
ATOM   724  C CA  . GLN A 1 108 ? -0.840  2.913   -4.299  1.00 20.34  ? 88  GLN A CA  1 
ATOM   725  C C   . GLN A 1 108 ? 0.091   2.801   -3.088  1.00 20.60  ? 88  GLN A C   1 
ATOM   726  O O   . GLN A 1 108 ? 0.948   1.935   -3.030  1.00 21.83  ? 88  GLN A O   1 
ATOM   727  C CB  . GLN A 1 108 ? -0.223  3.791   -5.388  1.00 21.78  ? 88  GLN A CB  1 
ATOM   728  C CG  . GLN A 1 108 ? 1.016   3.166   -6.032  1.00 23.42  ? 88  GLN A CG  1 
ATOM   729  C CD  . GLN A 1 108 ? 0.761   1.817   -6.671  1.00 26.48  ? 88  GLN A CD  1 
ATOM   730  O OE1 . GLN A 1 108 ? -0.311  1.543   -7.200  1.00 29.96  ? 88  GLN A OE1 1 
ATOM   731  N NE2 . GLN A 1 108 ? 1.765   0.960   -6.650  1.00 27.54  ? 88  GLN A NE2 1 
ATOM   732  N N   . TRP A 1 109 ? 0.007   3.731   -2.139  1.00 21.17  ? 89  TRP A N   1 
ATOM   733  C CA  . TRP A 1 109 ? 0.833   3.664   -0.941  1.00 19.52  ? 89  TRP A CA  1 
ATOM   734  C C   . TRP A 1 109 ? 0.641   2.335   -0.200  1.00 19.52  ? 89  TRP A C   1 
ATOM   735  O O   . TRP A 1 109 ? 1.606   1.803   0.332   1.00 19.88  ? 89  TRP A O   1 
ATOM   736  C CB  . TRP A 1 109 ? 0.574   4.892   -0.053  1.00 21.11  ? 89  TRP A CB  1 
ATOM   737  C CG  . TRP A 1 109 ? -0.737  4.943   0.657   1.00 20.76  ? 89  TRP A CG  1 
ATOM   738  C CD1 . TRP A 1 109 ? -1.939  5.292   0.142   1.00 21.41  ? 89  TRP A CD1 1 
ATOM   739  C CD2 . TRP A 1 109 ? -0.965  4.687   2.058   1.00 20.23  ? 89  TRP A CD2 1 
ATOM   740  N NE1 . TRP A 1 109 ? -2.905  5.244   1.109   1.00 22.82  ? 89  TRP A NE1 1 
ATOM   741  C CE2 . TRP A 1 109 ? -2.334  4.897   2.304   1.00 21.58  ? 89  TRP A CE2 1 
ATOM   742  C CE3 . TRP A 1 109 ? -0.132  4.346   3.127   1.00 21.59  ? 89  TRP A CE3 1 
ATOM   743  C CZ2 . TRP A 1 109 ? -2.890  4.768   3.577   1.00 23.56  ? 89  TRP A CZ2 1 
ATOM   744  C CZ3 . TRP A 1 109 ? -0.676  4.210   4.387   1.00 22.49  ? 89  TRP A CZ3 1 
ATOM   745  C CH2 . TRP A 1 109 ? -2.040  4.409   4.601   1.00 23.14  ? 89  TRP A CH2 1 
ATOM   746  N N   . LEU A 1 110 ? -0.600  1.854   -0.144  1.00 20.23  ? 90  LEU A N   1 
ATOM   747  C CA  . LEU A 1 110 ? -0.907  0.571   0.492   1.00 20.32  ? 90  LEU A CA  1 
ATOM   748  C C   . LEU A 1 110 ? -0.285  -0.590  -0.261  1.00 21.18  ? 90  LEU A C   1 
ATOM   749  O O   . LEU A 1 110 ? 0.255   -1.501  0.367   1.00 21.32  ? 90  LEU A O   1 
ATOM   750  C CB  . LEU A 1 110 ? -2.412  0.353   0.646   1.00 21.29  ? 90  LEU A CB  1 
ATOM   751  C CG  . LEU A 1 110 ? -3.128  1.374   1.514   1.00 21.65  ? 90  LEU A CG  1 
ATOM   752  C CD1 . LEU A 1 110 ? -4.636  1.168   1.403   1.00 25.95  ? 90  LEU A CD1 1 
ATOM   753  C CD2 . LEU A 1 110 ? -2.698  1.252   2.965   1.00 22.78  ? 90  LEU A CD2 1 
ATOM   754  N N   . ARG A 1 111 ? -0.363  -0.510  -1.582  1.00 21.37  ? 91  ARG A N   1 
ATOM   755  C CA  . ARG A 1 111 ? 0.244   -1.560  -2.434  1.00 22.07  ? 91  ARG A CA  1 
ATOM   756  C C   . ARG A 1 111 ? 1.766   -1.568  -2.207  1.00 21.42  ? 91  ARG A C   1 
ATOM   757  O O   . ARG A 1 111 ? 2.323   -2.658  -2.083  1.00 21.97  ? 91  ARG A O   1 
ATOM   758  C CB  . ARG A 1 111 ? -0.151  -1.329  -3.895  1.00 24.73  ? 91  ARG A CB  1 
ATOM   759  C CG  . ARG A 1 111 ? -1.635  -1.559  -4.126  1.00 29.34  ? 91  ARG A CG  1 
ATOM   760  C CD  . ARG A 1 111 ? -2.038  -1.314  -5.564  1.00 34.01  ? 91  ARG A CD  1 
ATOM   761  N NE  . ARG A 1 111 ? -3.403  -0.783  -5.613  1.00 38.95  ? 91  ARG A NE  1 
ATOM   762  C CZ  . ARG A 1 111 ? -4.158  -0.757  -6.699  0.70 40.50  ? 91  ARG A CZ  1 
ATOM   763  N NH1 . ARG A 1 111 ? -5.347  -0.186  -6.660  0.00 43.85  ? 91  ARG A NH1 1 
ATOM   764  N NH2 . ARG A 1 111 ? -3.717  -1.291  -7.823  0.30 42.56  ? 91  ARG A NH2 1 
ATOM   765  N N   . GLU A 1 112 ? 2.410   -0.395  -2.152  1.00 20.72  ? 92  GLU A N   1 
ATOM   766  C CA  . GLU A 1 112 ? 3.878   -0.408  -1.984  1.00 20.45  ? 92  GLU A CA  1 
ATOM   767  C C   . GLU A 1 112 ? 4.234   -1.039  -0.633  1.00 20.02  ? 92  GLU A C   1 
ATOM   768  O O   . GLU A 1 112 ? 5.238   -1.732  -0.551  1.00 21.94  ? 92  GLU A O   1 
ATOM   769  C CB  . GLU A 1 112 ? 4.434   1.012   -2.082  1.00 20.84  ? 92  GLU A CB  1 
ATOM   770  C CG  . GLU A 1 112 ? 4.248   1.621   -3.457  1.00 21.52  ? 92  GLU A CG  1 
ATOM   771  C CD  . GLU A 1 112 ? 4.942   0.865   -4.576  1.00 22.25  ? 92  GLU A CD  1 
ATOM   772  O OE1 . GLU A 1 112 ? 6.029   0.330   -4.336  1.00 23.72  ? 92  GLU A OE1 1 
ATOM   773  O OE2 . GLU A 1 112 ? 4.390   0.822   -5.680  1.00 26.90  ? 92  GLU A OE2 1 
ATOM   774  N N   . ILE A 1 113 ? 3.431   -0.760  0.383   1.00 18.13  ? 93  ILE A N   1 
ATOM   775  C CA  . ILE A 1 113 ? 3.737   -1.279  1.741   1.00 18.40  ? 93  ILE A CA  1 
ATOM   776  C C   . ILE A 1 113 ? 3.510   -2.797  1.753   1.00 18.26  ? 93  ILE A C   1 
ATOM   777  O O   . ILE A 1 113 ? 4.383   -3.491  2.229   1.00 19.08  ? 93  ILE A O   1 
ATOM   778  C CB  . ILE A 1 113 ? 2.858   -0.566  2.787   1.00 18.65  ? 93  ILE A CB  1 
ATOM   779  C CG1 . ILE A 1 113 ? 3.300   0.888   2.970   1.00 20.57  ? 93  ILE A CG1 1 
ATOM   780  C CG2 . ILE A 1 113 ? 2.839   -1.318  4.104   1.00 20.98  ? 93  ILE A CG2 1 
ATOM   781  C CD1 . ILE A 1 113 ? 2.293   1.749   3.683   1.00 21.56  ? 93  ILE A CD1 1 
ATOM   782  N N   . ASN A 1 114 ? 2.363   -3.205  1.242   1.00 18.90  ? 94  ASN A N   1 
ATOM   783  C CA  . ASN A 1 114 ? 2.037   -4.627  1.343   1.00 18.78  ? 94  ASN A CA  1 
ATOM   784  C C   . ASN A 1 114 ? 2.918   -5.491  0.442   1.00 21.16  ? 94  ASN A C   1 
ATOM   785  O O   . ASN A 1 114 ? 3.304   -6.606  0.833   1.00 22.18  ? 94  ASN A O   1 
ATOM   786  C CB  . ASN A 1 114 ? 0.547   -4.870  1.081   1.00 19.36  ? 94  ASN A CB  1 
ATOM   787  C CG  . ASN A 1 114 ? -0.267  -4.599  2.324   1.00 21.12  ? 94  ASN A CG  1 
ATOM   788  O OD1 . ASN A 1 114 ? 0.138   -4.976  3.409   1.00 23.43  ? 94  ASN A OD1 1 
ATOM   789  N ND2 . ASN A 1 114 ? -1.376  -3.899  2.209   1.00 24.02  ? 94  ASN A ND2 1 
ATOM   790  N N   . GLU A 1 115 ? 3.260   -5.010  -0.747  1.00 20.00  ? 95  GLU A N   1 
ATOM   791  C CA  . GLU A 1 115 ? 3.943   -5.838  -1.727  1.00 22.17  ? 95  GLU A CA  1 
ATOM   792  C C   . GLU A 1 115 ? 5.463   -5.719  -1.671  1.00 23.23  ? 95  GLU A C   1 
ATOM   793  O O   . GLU A 1 115 ? 6.163   -6.654  -2.085  1.00 25.37  ? 95  GLU A O   1 
ATOM   794  C CB  . GLU A 1 115 ? 3.374   -5.562  -3.124  1.00 24.89  ? 95  GLU A CB  1 
ATOM   795  C CG  . GLU A 1 115 ? 1.894   -5.934  -3.212  1.00 30.06  ? 95  GLU A CG  1 
ATOM   796  C CD  . GLU A 1 115 ? 1.576   -7.374  -2.783  1.00 37.52  ? 95  GLU A CD  1 
ATOM   797  O OE1 . GLU A 1 115 ? 2.284   -8.317  -3.253  1.00 43.72  ? 95  GLU A OE1 1 
ATOM   798  O OE2 . GLU A 1 115 ? 0.666   -7.571  -1.915  1.00 39.09  ? 95  GLU A OE2 1 
ATOM   799  N N   . ARG A 1 116 ? 5.998   -4.634  -1.103  1.00 22.94  ? 96  ARG A N   1 
ATOM   800  C CA  . ARG A 1 116 ? 7.435   -4.398  -1.139  1.00 24.60  ? 96  ARG A CA  1 
ATOM   801  C C   . ARG A 1 116 ? 8.031   -3.972  0.198   1.00 23.36  ? 96  ARG A C   1 
ATOM   802  O O   . ARG A 1 116 ? 9.115   -4.421  0.528   1.00 27.97  ? 96  ARG A O   1 
ATOM   803  C CB  . ARG A 1 116 ? 7.751   -3.385  -2.248  1.00 26.57  ? 96  ARG A CB  1 
ATOM   804  C CG  . ARG A 1 116 ? 7.711   -4.018  -3.641  1.00 29.88  ? 96  ARG A CG  1 
ATOM   805  C CD  . ARG A 1 116 ? 7.742   -3.045  -4.819  1.00 33.35  ? 96  ARG A CD  1 
ATOM   806  N NE  . ARG A 1 116 ? 6.447   -2.403  -5.076  1.00 34.65  ? 96  ARG A NE  1 
ATOM   807  C CZ  . ARG A 1 116 ? 5.381   -2.959  -5.649  1.00 33.88  ? 96  ARG A CZ  1 
ATOM   808  N NH1 . ARG A 1 116 ? 5.426   -4.200  -6.111  1.00 37.79  ? 96  ARG A NH1 1 
ATOM   809  N NH2 . ARG A 1 116 ? 4.260   -2.264  -5.773  1.00 33.32  ? 96  ARG A NH2 1 
ATOM   810  N N   . GLU A 1 117 ? 7.401   -3.050  0.945   1.00 21.57  ? 97  GLU A N   1 
ATOM   811  C CA  . GLU A 1 117 ? 8.169   -2.443  2.019   1.00 19.46  ? 97  GLU A CA  1 
ATOM   812  C C   . GLU A 1 117 ? 8.074   -3.243  3.318   1.00 19.62  ? 97  GLU A C   1 
ATOM   813  O O   . GLU A 1 117 ? 9.070   -3.352  4.028   1.00 20.68  ? 97  GLU A O   1 
ATOM   814  C CB  . GLU A 1 117 ? 7.742   -1.004  2.244   1.00 19.70  ? 97  GLU A CB  1 
ATOM   815  C CG  . GLU A 1 117 ? 8.026   -0.135  1.030   1.00 21.10  ? 97  GLU A CG  1 
ATOM   816  C CD  . GLU A 1 117 ? 9.496   -0.069  0.647   1.00 20.60  ? 97  GLU A CD  1 
ATOM   817  O OE1 . GLU A 1 117 ? 9.777   0.038   -0.561  1.00 22.98  ? 97  GLU A OE1 1 
ATOM   818  O OE2 . GLU A 1 117 ? 10.369  -0.162  1.542   1.00 21.47  ? 97  GLU A OE2 1 
ATOM   819  N N   . LEU A 1 118 ? 6.889   -3.752  3.656   1.00 20.49  ? 98  LEU A N   1 
ATOM   820  C CA  . LEU A 1 118 ? 6.775   -4.666  4.801   1.00 20.45  ? 98  LEU A CA  1 
ATOM   821  C C   . LEU A 1 118 ? 7.549   -5.977  4.614   1.00 20.18  ? 98  LEU A C   1 
ATOM   822  O O   . LEU A 1 118 ? 8.191   -6.424  5.556   1.00 20.63  ? 98  LEU A O   1 
ATOM   823  C CB  . LEU A 1 118 ? 5.314   -4.971  5.145   1.00 19.03  ? 98  LEU A CB  1 
ATOM   824  C CG  . LEU A 1 118 ? 4.627   -3.915  6.013   1.00 19.53  ? 98  LEU A CG  1 
ATOM   825  C CD1 . LEU A 1 118 ? 3.132   -4.189  6.125   1.00 19.83  ? 98  LEU A CD1 1 
ATOM   826  C CD2 . LEU A 1 118 ? 5.277   -3.790  7.397   1.00 19.89  ? 98  LEU A CD2 1 
ATOM   827  N N   . PRO A 1 119 ? 7.504   -6.646  3.456   1.00 20.60  ? 99  PRO A N   1 
ATOM   828  C CA  . PRO A 1 119 ? 8.138   -7.971  3.370   1.00 22.42  ? 99  PRO A CA  1 
ATOM   829  C C   . PRO A 1 119 ? 9.637   -8.016  3.064   1.00 21.87  ? 99  PRO A C   1 
ATOM   830  O O   . PRO A 1 119 ? 10.282  -9.031  3.302   1.00 25.35  ? 99  PRO A O   1 
ATOM   831  C CB  . PRO A 1 119 ? 7.362   -8.645  2.237   1.00 24.55  ? 99  PRO A CB  1 
ATOM   832  C CG  . PRO A 1 119 ? 6.900   -7.513  1.347   1.00 24.81  ? 99  PRO A CG  1 
ATOM   833  C CD  . PRO A 1 119 ? 6.621   -6.369  2.318   1.00 22.97  ? 99  PRO A CD  1 
ATOM   834  N N   . GLU A 1 120 ? 10.203  -6.927  2.538   1.00 23.13  ? 100 GLU A N   1 
ATOM   835  C CA  . GLU A 1 120 ? 11.597  -6.921  2.138   1.00 22.37  ? 100 GLU A CA  1 
ATOM   836  C C   . GLU A 1 120 ? 12.475  -6.367  3.257   1.00 20.76  ? 100 GLU A C   1 
ATOM   837  O O   . GLU A 1 120 ? 12.387  -5.192  3.640   1.00 20.57  ? 100 GLU A O   1 
ATOM   838  C CB  . GLU A 1 120 ? 11.795  -6.117  0.849   1.00 25.08  ? 100 GLU A CB  1 
ATOM   839  C CG  . GLU A 1 120 ? 11.045  -6.650  -0.341  1.00 30.89  ? 100 GLU A CG  1 
ATOM   840  C CD  . GLU A 1 120 ? 11.205  -5.884  -1.650  1.00 37.63  ? 100 GLU A CD  1 
ATOM   841  O OE1 . GLU A 1 120 ? 11.912  -4.828  -1.686  1.00 45.90  ? 100 GLU A OE1 1 
ATOM   842  O OE2 . GLU A 1 120 ? 10.587  -6.321  -2.637  1.00 42.41  ? 100 GLU A OE2 1 
ATOM   843  N N   . ARG A 1 121 ? 13.401  -7.181  3.733   1.00 22.64  ? 101 ARG A N   1 
ATOM   844  C CA  . ARG A 1 121 ? 14.391  -6.763  4.706   1.00 21.86  ? 101 ARG A CA  1 
ATOM   845  C C   . ARG A 1 121 ? 15.258  -5.631  4.120   1.00 20.55  ? 101 ARG A C   1 
ATOM   846  O O   . ARG A 1 121 ? 15.581  -5.594  2.935   1.00 22.06  ? 101 ARG A O   1 
ATOM   847  C CB  . ARG A 1 121 ? 15.194  -7.997  5.122   1.00 25.51  ? 101 ARG A CB  1 
ATOM   848  C CG  . ARG A 1 121 ? 16.278  -7.754  6.152   1.00 29.62  ? 101 ARG A CG  1 
ATOM   849  C CD  . ARG A 1 121 ? 16.862  -9.103  6.590   1.00 30.50  ? 101 ARG A CD  1 
ATOM   850  N NE  . ARG A 1 121 ? 17.826  -8.903  7.662   1.00 32.73  ? 101 ARG A NE  1 
ATOM   851  C CZ  . ARG A 1 121 ? 19.141  -9.088  7.585   1.00 32.80  ? 101 ARG A CZ  1 
ATOM   852  N NH1 . ARG A 1 121 ? 19.697  -9.469  6.447   1.00 32.29  ? 101 ARG A NH1 1 
ATOM   853  N NH2 . ARG A 1 121 ? 19.897  -8.902  8.665   1.00 35.49  ? 101 ARG A NH2 1 
ATOM   854  N N   . ILE A 1 122 ? 15.646  -4.706  4.977   1.00 21.50  ? 102 ILE A N   1 
ATOM   855  C CA  . ILE A 1 122 ? 16.713  -3.768  4.667   1.00 20.66  ? 102 ILE A CA  1 
ATOM   856  C C   . ILE A 1 122 ? 18.017  -4.389  5.156   1.00 21.43  ? 102 ILE A C   1 
ATOM   857  O O   . ILE A 1 122 ? 18.211  -4.608  6.358   1.00 22.81  ? 102 ILE A O   1 
ATOM   858  C CB  . ILE A 1 122 ? 16.434  -2.409  5.342   1.00 21.16  ? 102 ILE A CB  1 
ATOM   859  C CG1 . ILE A 1 122 ? 15.122  -1.815  4.824   1.00 20.88  ? 102 ILE A CG1 1 
ATOM   860  C CG2 . ILE A 1 122 ? 17.603  -1.440  5.197   1.00 23.08  ? 102 ILE A CG2 1 
ATOM   861  C CD1 . ILE A 1 122 ? 14.599  -0.639  5.652   1.00 20.49  ? 102 ILE A CD1 1 
ATOM   862  N N   . ASP A 1 123 ? 18.920  -4.630  4.212   1.00 21.56  ? 103 ASP A N   1 
ATOM   863  C CA  . ASP A 1 123 ? 20.169  -5.303  4.523   1.00 23.59  ? 103 ASP A CA  1 
ATOM   864  C C   . ASP A 1 123 ? 21.024  -4.420  5.414   1.00 22.30  ? 103 ASP A C   1 
ATOM   865  O O   . ASP A 1 123 ? 21.458  -3.347  4.960   1.00 23.82  ? 103 ASP A O   1 
ATOM   866  C CB  . ASP A 1 123 ? 20.958  -5.605  3.257   1.00 26.27  ? 103 ASP A CB  1 
ATOM   867  C CG  . ASP A 1 123 ? 22.236  -6.383  3.504   1.00 29.71  ? 103 ASP A CG  1 
ATOM   868  O OD1 . ASP A 1 123 ? 22.579  -6.641  4.670   1.00 31.37  ? 103 ASP A OD1 1 
ATOM   869  O OD2 . ASP A 1 123 ? 22.895  -6.672  2.521   1.00 37.80  ? 103 ASP A OD2 1 
ATOM   870  N N   . PRO A 1 124 ? 21.217  -4.760  6.710   1.00 22.50  ? 104 PRO A N   1 
ATOM   871  C CA  . PRO A 1 124 ? 21.960  -3.884  7.608   1.00 24.86  ? 104 PRO A CA  1 
ATOM   872  C C   . PRO A 1 124 ? 23.472  -4.041  7.501   1.00 26.29  ? 104 PRO A C   1 
ATOM   873  O O   . PRO A 1 124 ? 24.228  -3.271  8.091   1.00 26.43  ? 104 PRO A O   1 
ATOM   874  C CB  . PRO A 1 124 ? 21.490  -4.314  8.988   1.00 24.46  ? 104 PRO A CB  1 
ATOM   875  C CG  . PRO A 1 124 ? 21.241  -5.803  8.803   1.00 25.49  ? 104 PRO A CG  1 
ATOM   876  C CD  . PRO A 1 124 ? 20.721  -5.968  7.393   1.00 23.43  ? 104 PRO A CD  1 
ATOM   877  N N   . ASP A 1 125 ? 23.911  -5.054  6.753   1.00 25.34  ? 105 ASP A N   1 
ATOM   878  C CA  . ASP A 1 125 ? 25.328  -5.280  6.567   1.00 28.57  ? 105 ASP A CA  1 
ATOM   879  C C   . ASP A 1 125 ? 25.930  -4.257  5.593   1.00 24.86  ? 105 ASP A C   1 
ATOM   880  O O   . ASP A 1 125 ? 27.048  -3.784  5.803   1.00 28.20  ? 105 ASP A O   1 
ATOM   881  C CB  . ASP A 1 125 ? 25.550  -6.709  6.119   1.00 29.80  ? 105 ASP A CB  1 
ATOM   882  C CG  . ASP A 1 125 ? 25.228  -7.736  7.199   1.00 34.50  ? 105 ASP A CG  1 
ATOM   883  O OD1 . ASP A 1 125 ? 24.891  -7.357  8.389   1.00 34.04  ? 105 ASP A OD1 1 
ATOM   884  O OD2 . ASP A 1 125 ? 25.311  -8.900  6.863   1.00 36.40  ? 105 ASP A OD2 1 
ATOM   885  N N   . SER A 1 126 ? 25.211  -3.976  4.502   1.00 24.37  ? 106 SER A N   1 
ATOM   886  C CA  . SER A 1 126 ? 25.618  -2.929  3.577   1.00 24.35  ? 106 SER A CA  1 
ATOM   887  C C   . SER A 1 126 ? 25.151  -1.562  4.085   1.00 23.81  ? 106 SER A C   1 
ATOM   888  O O   . SER A 1 126 ? 25.929  -0.628  4.059   1.00 23.67  ? 106 SER A O   1 
ATOM   889  C CB  . SER A 1 126 ? 25.096  -3.198  2.189   1.00 28.63  ? 106 SER A CB  1 
ATOM   890  O OG  . SER A 1 126 ? 23.707  -3.417  2.226   1.00 30.72  ? 106 SER A OG  1 
ATOM   891  N N   . GLY A 1 127 ? 23.898  -1.487  4.548   1.00 21.47  ? 107 GLY A N   1 
ATOM   892  C CA  . GLY A 1 127 ? 23.323  -0.271  5.052   1.00 22.01  ? 107 GLY A CA  1 
ATOM   893  C C   . GLY A 1 127 ? 23.100  0.734   3.933   1.00 21.10  ? 107 GLY A C   1 
ATOM   894  O O   . GLY A 1 127 ? 23.311  0.482   2.746   1.00 22.95  ? 107 GLY A O   1 
ATOM   895  N N   . PRO A 1 128 ? 22.553  1.901   4.273   1.00 19.56  ? 108 PRO A N   1 
ATOM   896  C CA  . PRO A 1 128 ? 22.153  2.231   5.632   1.00 18.46  ? 108 PRO A CA  1 
ATOM   897  C C   . PRO A 1 128 ? 20.826  1.569   6.005   1.00 18.25  ? 108 PRO A C   1 
ATOM   898  O O   . PRO A 1 128 ? 20.138  0.953   5.164   1.00 19.27  ? 108 PRO A O   1 
ATOM   899  C CB  . PRO A 1 128 ? 22.038  3.765   5.515   1.00 17.95  ? 108 PRO A CB  1 
ATOM   900  C CG  . PRO A 1 128 ? 21.480  3.945   4.141   1.00 19.67  ? 108 PRO A CG  1 
ATOM   901  C CD  . PRO A 1 128 ? 22.203  2.936   3.296   1.00 20.61  ? 108 PRO A CD  1 
ATOM   902  N N   . LEU A 1 129 ? 20.437  1.744   7.269   1.00 18.34  ? 109 LEU A N   1 
ATOM   903  C CA  . LEU A 1 129 ? 19.259  1.079   7.797   1.00 19.59  ? 109 LEU A CA  1 
ATOM   904  C C   . LEU A 1 129 ? 18.053  1.995   7.613   1.00 18.54  ? 109 LEU A C   1 
ATOM   905  O O   . LEU A 1 129 ? 17.379  2.364   8.576   1.00 19.42  ? 109 LEU A O   1 
ATOM   906  C CB  . LEU A 1 129 ? 19.472  0.673   9.254   1.00 20.51  ? 109 LEU A CB  1 
ATOM   907  C CG  . LEU A 1 129 ? 20.245  -0.628  9.448   1.00 20.44  ? 109 LEU A CG  1 
ATOM   908  C CD1 . LEU A 1 129 ? 21.706  -0.443  9.071   1.00 19.63  ? 109 LEU A CD1 1 
ATOM   909  C CD2 . LEU A 1 129 ? 20.117  -1.117  10.885  1.00 22.31  ? 109 LEU A CD2 1 
ATOM   910  N N   . ILE A 1 130 ? 17.803  2.284   6.342   1.00 18.71  ? 110 ILE A N   1 
ATOM   911  C CA  . ILE A 1 130 ? 16.645  3.147   5.994   1.00 18.18  ? 110 ILE A CA  1 
ATOM   912  C C   . ILE A 1 130 ? 16.459  3.093   4.472   1.00 18.93  ? 110 ILE A C   1 
ATOM   913  O O   . ILE A 1 130 ? 17.460  3.007   3.762   1.00 19.65  ? 110 ILE A O   1 
ATOM   914  C CB  . ILE A 1 130 ? 16.854  4.597   6.490   1.00 18.57  ? 110 ILE A CB  1 
ATOM   915  C CG1 . ILE A 1 130 ? 15.728  5.522   6.028   1.00 18.37  ? 110 ILE A CG1 1 
ATOM   916  C CG2 . ILE A 1 130 ? 18.232  5.124   6.093   1.00 20.20  ? 110 ILE A CG2 1 
ATOM   917  C CD1 . ILE A 1 130 ? 15.722  6.881   6.702   1.00 19.08  ? 110 ILE A CD1 1 
ATOM   918  N N   . ARG A 1 131 ? 15.212  3.136   4.024   1.00 18.31  ? 111 ARG A N   1 
ATOM   919  C CA  . ARG A 1 131 ? 14.920  3.229   2.567   1.00 19.56  ? 111 ARG A CA  1 
ATOM   920  C C   . ARG A 1 131 ? 13.639  4.075   2.421   1.00 18.28  ? 111 ARG A C   1 
ATOM   921  O O   . ARG A 1 131 ? 12.714  3.882   3.238   1.00 16.94  ? 111 ARG A O   1 
ATOM   922  C CB  . ARG A 1 131 ? 14.853  1.850   1.896   1.00 24.17  ? 111 ARG A CB  1 
ATOM   923  C CG  . ARG A 1 131 ? 13.718  0.914   2.278   1.00 24.22  ? 111 ARG A CG  1 
ATOM   924  C CD  . ARG A 1 131 ? 13.915  -0.414  1.566   1.00 23.23  ? 111 ARG A CD  1 
ATOM   925  N NE  . ARG A 1 131 ? 12.712  -1.250  1.578   1.00 21.40  ? 111 ARG A NE  1 
ATOM   926  C CZ  . ARG A 1 131 ? 12.629  -2.435  2.165   1.00 22.17  ? 111 ARG A CZ  1 
ATOM   927  N NH1 . ARG A 1 131 ? 13.622  -3.299  2.053   1.00 22.41  ? 111 ARG A NH1 1 
ATOM   928  N NH2 . ARG A 1 131 ? 11.554  -2.750  2.863   1.00 21.83  ? 111 ARG A NH2 1 
ATOM   929  N N   . THR A 1 132 ? 13.597  5.003   1.461   1.00 18.83  ? 112 THR A N   1 
ATOM   930  C CA  . THR A 1 132 ? 12.465  5.888   1.286   1.00 18.67  ? 112 THR A CA  1 
ATOM   931  C C   . THR A 1 132 ? 11.849  5.678   -0.086  1.00 17.83  ? 112 THR A C   1 
ATOM   932  O O   . THR A 1 132 ? 12.504  5.202   -1.008  1.00 19.37  ? 112 THR A O   1 
ATOM   933  C CB  . THR A 1 132 ? 12.857  7.362   1.495   1.00 19.46  ? 112 THR A CB  1 
ATOM   934  O OG1 . THR A 1 132 ? 13.748  7.766   0.448   1.00 20.22  ? 112 THR A OG1 1 
ATOM   935  C CG2 . THR A 1 132 ? 13.451  7.600   2.878   1.00 18.64  ? 112 THR A CG2 1 
ATOM   936  N N   . VAL A 1 133 ? 10.568  6.044   -0.183  1.00 18.20  ? 113 VAL A N   1 
ATOM   937  C CA  . VAL A 1 133 ? 9.805   5.967   -1.413  1.00 19.31  ? 113 VAL A CA  1 
ATOM   938  C C   . VAL A 1 133 ? 9.061   7.284   -1.621  1.00 19.50  ? 113 VAL A C   1 
ATOM   939  O O   . VAL A 1 133 ? 8.526   7.825   -0.670  1.00 18.66  ? 113 VAL A O   1 
ATOM   940  C CB  . VAL A 1 133 ? 8.818   4.799   -1.369  1.00 20.03  ? 113 VAL A CB  1 
ATOM   941  C CG1 . VAL A 1 133 ? 8.187   4.550   -2.710  1.00 21.09  ? 113 VAL A CG1 1 
ATOM   942  C CG2 . VAL A 1 133 ? 9.482   3.524   -0.869  1.00 20.48  ? 113 VAL A CG2 1 
ATOM   943  N N   . ALA A 1 134 ? 8.993   7.738   -2.885  1.00 19.83  ? 114 ALA A N   1 
ATOM   944  C CA  . ALA A 1 134 ? 8.162   8.859   -3.267  1.00 19.78  ? 114 ALA A CA  1 
ATOM   945  C C   . ALA A 1 134 ? 7.246   8.443   -4.406  1.00 19.88  ? 114 ALA A C   1 
ATOM   946  O O   . ALA A 1 134 ? 7.725   8.076   -5.473  1.00 21.04  ? 114 ALA A O   1 
ATOM   947  C CB  . ALA A 1 134 ? 9.013   10.040  -3.646  1.00 20.97  ? 114 ALA A CB  1 
ATOM   948  N N   . ILE A 1 135 ? 5.949   8.384   -4.100  1.00 19.47  ? 115 ILE A N   1 
ATOM   949  C CA  . ILE A 1 135 ? 4.914   8.021   -5.050  1.00 20.00  ? 115 ILE A CA  1 
ATOM   950  C C   . ILE A 1 135 ? 4.332   9.312   -5.618  1.00 21.07  ? 115 ILE A C   1 
ATOM   951  O O   . ILE A 1 135 ? 3.717   10.044  -4.879  1.00 20.37  ? 115 ILE A O   1 
ATOM   952  C CB  . ILE A 1 135 ? 3.825   7.167   -4.382  1.00 21.37  ? 115 ILE A CB  1 
ATOM   953  C CG1 . ILE A 1 135 ? 4.451   5.942   -3.697  1.00 22.23  ? 115 ILE A CG1 1 
ATOM   954  C CG2 . ILE A 1 135 ? 2.766   6.803   -5.407  1.00 22.02  ? 115 ILE A CG2 1 
ATOM   955  C CD1 . ILE A 1 135 ? 3.568   5.276   -2.684  1.00 23.63  ? 115 ILE A CD1 1 
ATOM   956  N N   . ALA A 1 136 ? 4.489   9.520   -6.927  1.00 21.84  ? 116 ALA A N   1 
ATOM   957  C CA  . ALA A 1 136 ? 3.846   10.616  -7.615  1.00 22.90  ? 116 ALA A CA  1 
ATOM   958  C C   . ALA A 1 136 ? 2.471   10.132  -8.077  1.00 21.12  ? 116 ALA A C   1 
ATOM   959  O O   . ALA A 1 136 ? 2.343   9.418   -9.074  1.00 23.73  ? 116 ALA A O   1 
ATOM   960  C CB  . ALA A 1 136 ? 4.723   11.080  -8.758  1.00 24.68  ? 116 ALA A CB  1 
ATOM   961  N N   . THR A 1 137 ? 1.439   10.496  -7.327  1.00 21.80  ? 117 THR A N   1 
ATOM   962  C CA  . THR A 1 137 ? 0.114   9.950   -7.583  1.00 21.82  ? 117 THR A CA  1 
ATOM   963  C C   . THR A 1 137 ? -0.499  10.550  -8.854  1.00 21.79  ? 117 THR A C   1 
ATOM   964  O O   . THR A 1 137 ? -0.188  11.670  -9.254  1.00 21.52  ? 117 THR A O   1 
ATOM   965  C CB  . THR A 1 137 ? -0.855  10.144  -6.415  1.00 22.08  ? 117 THR A CB  1 
ATOM   966  O OG1 . THR A 1 137 ? -1.220  11.526  -6.280  1.00 21.40  ? 117 THR A OG1 1 
ATOM   967  C CG2 . THR A 1 137 ? -0.297  9.680   -5.088  1.00 23.12  ? 117 THR A CG2 1 
ATOM   968  N N   . ASP A 1 138 ? -1.443  9.826   -9.447  1.00 21.45  ? 118 ASP A N   1 
ATOM   969  C CA  . ASP A 1 138 ? -2.155  10.286  -10.628 1.00 23.84  ? 118 ASP A CA  1 
ATOM   970  C C   . ASP A 1 138 ? -2.931  11.576  -10.320 1.00 22.90  ? 118 ASP A C   1 
ATOM   971  O O   . ASP A 1 138 ? -3.226  12.339  -11.235 1.00 25.90  ? 118 ASP A O   1 
ATOM   972  C CB  . ASP A 1 138 ? -3.066  9.173   -11.176 1.00 25.18  ? 118 ASP A CB  1 
ATOM   973  C CG  . ASP A 1 138 ? -2.343  7.924   -11.671 1.00 28.65  ? 118 ASP A CG  1 
ATOM   974  O OD1 . ASP A 1 138 ? -1.148  7.974   -11.927 1.00 29.19  ? 118 ASP A OD1 1 
ATOM   975  O OD2 . ASP A 1 138 ? -3.003  6.872   -11.781 1.00 35.74  ? 118 ASP A OD2 1 
ATOM   976  N N   . ALA A 1 139 ? -3.291  11.812  -9.048  1.00 21.39  ? 119 ALA A N   1 
ATOM   977  C CA  . ALA A 1 139 ? -4.041  13.008  -8.668  1.00 20.57  ? 119 ALA A CA  1 
ATOM   978  C C   . ALA A 1 139 ? -3.127  14.216  -8.470  1.00 19.67  ? 119 ALA A C   1 
ATOM   979  O O   . ALA A 1 139 ? -3.628  15.305  -8.175  1.00 21.67  ? 119 ALA A O   1 
ATOM   980  C CB  . ALA A 1 139 ? -4.869  12.750  -7.431  1.00 20.92  ? 119 ALA A CB  1 
ATOM   981  N N   . GLY A 1 140 ? -1.819  14.038  -8.618  1.00 20.23  ? 120 GLY A N   1 
ATOM   982  C CA  . GLY A 1 140 ? -0.905  15.175  -8.625  1.00 21.11  ? 120 GLY A CA  1 
ATOM   983  C C   . GLY A 1 140 ? -0.306  15.470  -7.250  1.00 22.69  ? 120 GLY A C   1 
ATOM   984  O O   . GLY A 1 140 ? 0.326   16.499  -7.078  1.00 25.73  ? 120 GLY A O   1 
ATOM   985  N N   . ALA A 1 141 ? -0.489  14.589  -6.274  1.00 23.22  ? 121 ALA A N   1 
ATOM   986  C CA  . ALA A 1 141 ? 0.167   14.685  -4.976  1.00 22.53  ? 121 ALA A CA  1 
ATOM   987  C C   . ALA A 1 141 ? 1.361   13.730  -4.913  1.00 21.81  ? 121 ALA A C   1 
ATOM   988  O O   . ALA A 1 141 ? 1.665   13.007  -5.872  1.00 24.82  ? 121 ALA A O   1 
ATOM   989  C CB  . ALA A 1 141 ? -0.826  14.388  -3.868  1.00 23.22  ? 121 ALA A CB  1 
ATOM   990  N N   . HIS A 1 142 ? 2.051   13.738  -3.776  1.00 18.34  ? 122 HIS A N   1 
ATOM   991  C CA  . HIS A 1 142 ? 3.072   12.737  -3.510  1.00 20.60  ? 122 HIS A CA  1 
ATOM   992  C C   . HIS A 1 142 ? 2.765   12.050  -2.189  1.00 20.34  ? 122 HIS A C   1 
ATOM   993  O O   . HIS A 1 142 ? 2.445   12.683  -1.199  1.00 20.80  ? 122 HIS A O   1 
ATOM   994  C CB  . HIS A 1 142 ? 4.482   13.330  -3.480  1.00 21.50  ? 122 HIS A CB  1 
ATOM   995  C CG  . HIS A 1 142 ? 4.953   13.772  -4.815  1.00 22.69  ? 122 HIS A CG  1 
ATOM   996  N ND1 . HIS A 1 142 ? 4.565   14.986  -5.357  1.00 24.44  ? 122 HIS A ND1 1 
ATOM   997  C CD2 . HIS A 1 142 ? 5.773   13.227  -5.701  1.00 24.08  ? 122 HIS A CD2 1 
ATOM   998  C CE1 . HIS A 1 142 ? 5.133   15.123  -6.534  1.00 26.51  ? 122 HIS A CE1 1 
ATOM   999  N NE2 . HIS A 1 142 ? 5.842   14.051  -6.785  1.00 26.61  ? 122 HIS A NE2 1 
ATOM   1000 N N   . ASP A 1 143 ? 2.877   10.722  -2.188  1.00 19.23  ? 123 ASP A N   1 
ATOM   1001 C CA  . ASP A 1 143 ? 2.903   9.962   -0.954  1.00 19.50  ? 123 ASP A CA  1 
ATOM   1002 C C   . ASP A 1 143 ? 4.338   9.541   -0.665  1.00 17.97  ? 123 ASP A C   1 
ATOM   1003 O O   . ASP A 1 143 ? 4.977   8.926   -1.528  1.00 18.74  ? 123 ASP A O   1 
ATOM   1004 C CB  . ASP A 1 143 ? 1.990   8.747   -1.040  1.00 19.37  ? 123 ASP A CB  1 
ATOM   1005 C CG  . ASP A 1 143 ? 0.500   9.046   -0.922  1.00 20.29  ? 123 ASP A CG  1 
ATOM   1006 O OD1 . ASP A 1 143 ? 0.132   9.830   -0.029  1.00 22.01  ? 123 ASP A OD1 1 
ATOM   1007 O OD2 . ASP A 1 143 ? -0.310  8.507   -1.734  1.00 22.62  ? 123 ASP A OD2 1 
ATOM   1008 N N   . LEU A 1 144 ? 4.875   9.973   0.491   1.00 17.31  ? 124 LEU A N   1 
ATOM   1009 C CA  . LEU A 1 144 ? 6.233   9.631   0.892   1.00 18.49  ? 124 LEU A CA  1 
ATOM   1010 C C   . LEU A 1 144 ? 6.166   8.522   1.941   1.00 17.87  ? 124 LEU A C   1 
ATOM   1011 O O   . LEU A 1 144 ? 5.358   8.611   2.873   1.00 17.59  ? 124 LEU A O   1 
ATOM   1012 C CB  . LEU A 1 144 ? 6.937   10.850  1.481   1.00 18.44  ? 124 LEU A CB  1 
ATOM   1013 C CG  . LEU A 1 144 ? 7.020   12.044  0.549   1.00 20.33  ? 124 LEU A CG  1 
ATOM   1014 C CD1 . LEU A 1 144 ? 7.919   13.044  1.186   1.00 19.70  ? 124 LEU A CD1 1 
ATOM   1015 C CD2 . LEU A 1 144 ? 7.545   11.690  -0.815  1.00 21.23  ? 124 LEU A CD2 1 
ATOM   1016 N N   . LEU A 1 145 ? 7.070   7.531   1.806   1.00 17.97  ? 125 LEU A N   1 
ATOM   1017 C CA  . LEU A 1 145 ? 7.246   6.498   2.814   1.00 16.63  ? 125 LEU A CA  1 
ATOM   1018 C C   . LEU A 1 145 ? 8.676   6.579   3.348   1.00 14.43  ? 125 LEU A C   1 
ATOM   1019 O O   . LEU A 1 145 ? 9.648   6.690   2.592   1.00 17.33  ? 125 LEU A O   1 
ATOM   1020 C CB  . LEU A 1 145 ? 7.029   5.113   2.195   1.00 17.19  ? 125 LEU A CB  1 
ATOM   1021 C CG  . LEU A 1 145 ? 5.697   4.852   1.508   1.00 18.58  ? 125 LEU A CG  1 
ATOM   1022 C CD1 . LEU A 1 145 ? 5.666   3.440   0.966   1.00 19.12  ? 125 LEU A CD1 1 
ATOM   1023 C CD2 . LEU A 1 145 ? 4.506   5.082   2.434   1.00 18.74  ? 125 LEU A CD2 1 
ATOM   1024 N N   . VAL A 1 146 ? 8.791   6.442   4.671   1.00 16.92  ? 126 VAL A N   1 
ATOM   1025 C CA  . VAL A 1 146 ? 10.052  6.241   5.366   1.00 16.38  ? 126 VAL A CA  1 
ATOM   1026 C C   . VAL A 1 146 ? 10.000  4.854   6.028   1.00 16.11  ? 126 VAL A C   1 
ATOM   1027 O O   . VAL A 1 146 ? 9.078   4.576   6.792   1.00 16.14  ? 126 VAL A O   1 
ATOM   1028 C CB  . VAL A 1 146 ? 10.308  7.355   6.404   1.00 16.75  ? 126 VAL A CB  1 
ATOM   1029 C CG1 . VAL A 1 146 ? 11.583  7.084   7.197   1.00 17.35  ? 126 VAL A CG1 1 
ATOM   1030 C CG2 . VAL A 1 146 ? 10.367  8.741   5.738   1.00 17.16  ? 126 VAL A CG2 1 
ATOM   1031 N N   . VAL A 1 147 ? 10.986  4.017   5.686   1.00 16.81  ? 127 VAL A N   1 
ATOM   1032 C CA  . VAL A 1 147 ? 11.014  2.595   6.086   1.00 16.27  ? 127 VAL A CA  1 
ATOM   1033 C C   . VAL A 1 147 ? 12.328  2.358   6.836   1.00 16.00  ? 127 VAL A C   1 
ATOM   1034 O O   . VAL A 1 147 ? 13.413  2.555   6.278   1.00 17.39  ? 127 VAL A O   1 
ATOM   1035 C CB  . VAL A 1 147 ? 10.933  1.698   4.840   1.00 16.07  ? 127 VAL A CB  1 
ATOM   1036 C CG1 . VAL A 1 147 ? 10.842  0.214   5.221   1.00 16.57  ? 127 VAL A CG1 1 
ATOM   1037 C CG2 . VAL A 1 147 ? 9.777   2.118   3.940   1.00 18.46  ? 127 VAL A CG2 1 
ATOM   1038 N N   . VAL A 1 148 ? 12.215  2.016   8.114   1.00 16.90  ? 128 VAL A N   1 
ATOM   1039 C CA  . VAL A 1 148 ? 13.371  1.861   8.999   1.00 16.94  ? 128 VAL A CA  1 
ATOM   1040 C C   . VAL A 1 148 ? 13.171  0.585   9.823   1.00 16.35  ? 128 VAL A C   1 
ATOM   1041 O O   . VAL A 1 148 ? 12.142  0.422   10.466  1.00 17.49  ? 128 VAL A O   1 
ATOM   1042 C CB  . VAL A 1 148 ? 13.574  3.084   9.913   1.00 18.42  ? 128 VAL A CB  1 
ATOM   1043 C CG1 . VAL A 1 148 ? 14.810  2.993   10.782  1.00 17.79  ? 128 VAL A CG1 1 
ATOM   1044 C CG2 . VAL A 1 148 ? 13.617  4.359   9.094   1.00 19.73  ? 128 VAL A CG2 1 
ATOM   1045 N N   . PRO A 1 149 ? 14.176  -0.307  9.878   1.00 17.74  ? 129 PRO A N   1 
ATOM   1046 C CA  . PRO A 1 149 ? 14.032  -1.465  10.755  1.00 17.82  ? 129 PRO A CA  1 
ATOM   1047 C C   . PRO A 1 149 ? 13.850  -1.043  12.212  1.00 18.71  ? 129 PRO A C   1 
ATOM   1048 O O   . PRO A 1 149 ? 14.491  -0.095  12.684  1.00 18.02  ? 129 PRO A O   1 
ATOM   1049 C CB  . PRO A 1 149 ? 15.301  -2.280  10.516  1.00 20.40  ? 129 PRO A CB  1 
ATOM   1050 C CG  . PRO A 1 149 ? 16.283  -1.368  9.878   1.00 22.56  ? 129 PRO A CG  1 
ATOM   1051 C CD  . PRO A 1 149 ? 15.508  -0.214  9.272   1.00 20.10  ? 129 PRO A CD  1 
ATOM   1052 N N   . HIS A 1 150 ? 13.066  -1.844  12.958  1.00 18.44  ? 130 HIS A N   1 
ATOM   1053 C CA  . HIS A 1 150 ? 12.699  -1.528  14.333  1.00 17.30  ? 130 HIS A CA  1 
ATOM   1054 C C   . HIS A 1 150 ? 13.909  -1.435  15.277  1.00 16.97  ? 130 HIS A C   1 
ATOM   1055 O O   . HIS A 1 150 ? 13.864  -0.767  16.314  1.00 19.51  ? 130 HIS A O   1 
ATOM   1056 C CB  . HIS A 1 150 ? 11.704  -2.547  14.858  1.00 18.60  ? 130 HIS A CB  1 
ATOM   1057 C CG  . HIS A 1 150 ? 10.863  -2.090  15.997  1.00 19.61  ? 130 HIS A CG  1 
ATOM   1058 N ND1 . HIS A 1 150 ? 11.291  -1.277  17.022  1.00 21.55  ? 130 HIS A ND1 1 
ATOM   1059 C CD2 . HIS A 1 150 ? 9.573   -2.389  16.255  1.00 25.26  ? 130 HIS A CD2 1 
ATOM   1060 C CE1 . HIS A 1 150 ? 10.276  -1.096  17.882  1.00 24.70  ? 130 HIS A CE1 1 
ATOM   1061 N NE2 . HIS A 1 150 ? 9.207   -1.765  17.434  1.00 28.83  ? 130 HIS A NE2 1 
ATOM   1062 N N   . ILE A 1 151 ? 15.037  -2.054  14.917  1.00 17.79  ? 131 ILE A N   1 
ATOM   1063 C CA  . ILE A 1 151 ? 16.278  -1.968  15.681  1.00 17.78  ? 131 ILE A CA  1 
ATOM   1064 C C   . ILE A 1 151 ? 16.642  -0.511  15.968  1.00 17.87  ? 131 ILE A C   1 
ATOM   1065 O O   . ILE A 1 151 ? 17.222  -0.236  17.020  1.00 19.92  ? 131 ILE A O   1 
ATOM   1066 C CB  . ILE A 1 151 ? 17.421  -2.736  14.965  1.00 20.13  ? 131 ILE A CB  1 
ATOM   1067 C CG1 . ILE A 1 151 ? 18.675  -2.856  15.839  1.00 21.14  ? 131 ILE A CG1 1 
ATOM   1068 C CG2 . ILE A 1 151 ? 17.747  -2.146  13.598  1.00 20.53  ? 131 ILE A CG2 1 
ATOM   1069 C CD1 . ILE A 1 151 ? 19.753  -3.738  15.231  1.00 22.73  ? 131 ILE A CD1 1 
ATOM   1070 N N   . ILE A 1 152 ? 16.315  0.414   15.031  1.00 17.31  ? 132 ILE A N   1 
ATOM   1071 C CA  . ILE A 1 152 ? 16.648  1.834   15.256  1.00 17.79  ? 132 ILE A CA  1 
ATOM   1072 C C   . ILE A 1 152 ? 15.431  2.740   15.077  1.00 17.41  ? 132 ILE A C   1 
ATOM   1073 O O   . ILE A 1 152 ? 15.590  3.973   14.908  1.00 19.39  ? 132 ILE A O   1 
ATOM   1074 C CB  . ILE A 1 152 ? 17.821  2.295   14.364  1.00 18.18  ? 132 ILE A CB  1 
ATOM   1075 C CG1 . ILE A 1 152 ? 17.501  2.194   12.865  1.00 18.37  ? 132 ILE A CG1 1 
ATOM   1076 C CG2 . ILE A 1 152 ? 19.099  1.565   14.745  1.00 19.38  ? 132 ILE A CG2 1 
ATOM   1077 C CD1 . ILE A 1 152 ? 18.397  3.031   11.958  1.00 19.03  ? 132 ILE A CD1 1 
ATOM   1078 N N   . ALA A 1 153 ? 14.224  2.219   15.164  1.00 17.42  ? 133 ALA A N   1 
ATOM   1079 C CA  . ALA A 1 153 ? 13.063  3.087   15.008  1.00 17.42  ? 133 ALA A CA  1 
ATOM   1080 C C   . ALA A 1 153 ? 11.833  2.552   15.725  1.00 18.98  ? 133 ALA A C   1 
ATOM   1081 O O   . ALA A 1 153 ? 11.495  1.388   15.609  1.00 20.53  ? 133 ALA A O   1 
ATOM   1082 C CB  . ALA A 1 153 ? 12.735  3.249   13.540  1.00 18.09  ? 133 ALA A CB  1 
ATOM   1083 N N   . ASP A 1 154 ? 11.092  3.469   16.333  1.00 18.05  ? 134 ASP A N   1 
ATOM   1084 C CA  . ASP A 1 154 ? 9.712   3.309   16.735  1.00 18.48  ? 134 ASP A CA  1 
ATOM   1085 C C   . ASP A 1 154 ? 8.832   4.264   15.913  1.00 17.11  ? 134 ASP A C   1 
ATOM   1086 O O   . ASP A 1 154 ? 9.318   4.866   14.978  1.00 17.35  ? 134 ASP A O   1 
ATOM   1087 C CB  . ASP A 1 154 ? 9.589   3.478   18.255  1.00 18.63  ? 134 ASP A CB  1 
ATOM   1088 C CG  . ASP A 1 154 ? 10.082  4.809   18.780  1.00 19.75  ? 134 ASP A CG  1 
ATOM   1089 O OD1 . ASP A 1 154 ? 9.928   5.778   18.025  1.00 20.97  ? 134 ASP A OD1 1 
ATOM   1090 O OD2 . ASP A 1 154 ? 10.582  4.847   19.932  1.00 21.95  ? 134 ASP A OD2 1 
ATOM   1091 N N   . GLY A 1 155 ? 7.544   4.377   16.234  1.00 19.42  ? 135 GLY A N   1 
ATOM   1092 C CA  . GLY A 1 155 ? 6.628   5.179   15.433  1.00 18.38  ? 135 GLY A CA  1 
ATOM   1093 C C   . GLY A 1 155 ? 7.013   6.659   15.471  1.00 18.01  ? 135 GLY A C   1 
ATOM   1094 O O   . GLY A 1 155 ? 6.907   7.336   14.449  1.00 17.70  ? 135 GLY A O   1 
ATOM   1095 N N   . THR A 1 156 ? 7.452   7.133   16.639  1.00 16.88  ? 136 THR A N   1 
ATOM   1096 C CA  . THR A 1 156 ? 7.906   8.525   16.731  1.00 17.08  ? 136 THR A CA  1 
ATOM   1097 C C   . THR A 1 156 ? 9.099   8.717   15.804  1.00 16.47  ? 136 THR A C   1 
ATOM   1098 O O   . THR A 1 156 ? 9.207   9.726   15.126  1.00 17.63  ? 136 THR A O   1 
ATOM   1099 C CB  . THR A 1 156 ? 8.250   8.953   18.160  1.00 18.46  ? 136 THR A CB  1 
ATOM   1100 O OG1 . THR A 1 156 ? 7.017   8.959   18.883  1.00 22.56  ? 136 THR A OG1 1 
ATOM   1101 C CG2 . THR A 1 156 ? 8.942   10.310  18.252  1.00 20.54  ? 136 THR A CG2 1 
ATOM   1102 N N   . THR A 1 157 ? 10.051  7.773   15.779  1.00 16.27  ? 137 THR A N   1 
ATOM   1103 C CA  . THR A 1 157 ? 11.224  7.900   14.930  1.00 15.64  ? 137 THR A CA  1 
ATOM   1104 C C   . THR A 1 157 ? 10.842  8.019   13.453  1.00 15.62  ? 137 THR A C   1 
ATOM   1105 O O   . THR A 1 157 ? 11.338  8.915   12.747  1.00 16.38  ? 137 THR A O   1 
ATOM   1106 C CB  . THR A 1 157 ? 12.206  6.765   15.140  1.00 17.74  ? 137 THR A CB  1 
ATOM   1107 O OG1 . THR A 1 157 ? 12.675  6.890   16.490  1.00 21.68  ? 137 THR A OG1 1 
ATOM   1108 C CG2 . THR A 1 157 ? 13.369  6.842   14.172  1.00 18.45  ? 137 THR A CG2 1 
ATOM   1109 N N   . VAL A 1 158 ? 9.976   7.146   12.931  1.00 15.93  ? 138 VAL A N   1 
ATOM   1110 C CA  . VAL A 1 158 ? 9.696   7.200   11.502  1.00 16.45  ? 138 VAL A CA  1 
ATOM   1111 C C   . VAL A 1 158 ? 8.921   8.469   11.154  1.00 15.27  ? 138 VAL A C   1 
ATOM   1112 O O   . VAL A 1 158 ? 9.087   8.953   10.040  1.00 16.93  ? 138 VAL A O   1 
ATOM   1113 C CB  . VAL A 1 158 ? 9.017   5.918   10.976  1.00 17.30  ? 138 VAL A CB  1 
ATOM   1114 C CG1 . VAL A 1 158 ? 10.003  4.770   10.937  1.00 18.24  ? 138 VAL A CG1 1 
ATOM   1115 C CG2 . VAL A 1 158 ? 7.759   5.547   11.738  1.00 16.97  ? 138 VAL A CG2 1 
ATOM   1116 N N   . LEU A 1 159 ? 8.065   8.978   12.059  1.00 15.68  ? 139 LEU A N   1 
ATOM   1117 C CA  . LEU A 1 159 ? 7.328   10.209  11.764  1.00 16.16  ? 139 LEU A CA  1 
ATOM   1118 C C   . LEU A 1 159 ? 8.254   11.413  11.881  1.00 16.38  ? 139 LEU A C   1 
ATOM   1119 O O   . LEU A 1 159 ? 8.171   12.280  10.985  1.00 15.89  ? 139 LEU A O   1 
ATOM   1120 C CB  . LEU A 1 159 ? 6.072   10.323  12.619  1.00 16.67  ? 139 LEU A CB  1 
ATOM   1121 C CG  . LEU A 1 159 ? 4.919   9.491   12.046  1.00 17.93  ? 139 LEU A CG  1 
ATOM   1122 C CD1 . LEU A 1 159 ? 3.868   9.170   13.072  1.00 17.53  ? 139 LEU A CD1 1 
ATOM   1123 C CD2 . LEU A 1 159 ? 4.282   10.195  10.851  1.00 16.69  ? 139 LEU A CD2 1 
ATOM   1124 N N   . THR A 1 160 ? 9.147   11.467  12.881  1.00 15.39  ? 140 THR A N   1 
ATOM   1125 C CA  . THR A 1 160 ? 10.005  12.655  12.950  1.00 16.48  ? 140 THR A CA  1 
ATOM   1126 C C   . THR A 1 160 ? 10.965  12.664  11.759  1.00 15.64  ? 140 THR A C   1 
ATOM   1127 O O   . THR A 1 160 ? 11.307  13.709  11.219  1.00 17.39  ? 140 THR A O   1 
ATOM   1128 C CB  . THR A 1 160 ? 10.748  12.781  14.279  1.00 17.41  ? 140 THR A CB  1 
ATOM   1129 O OG1 . THR A 1 160 ? 11.328  14.077  14.393  1.00 17.88  ? 140 THR A OG1 1 
ATOM   1130 C CG2 . THR A 1 160 ? 11.806  11.722  14.482  1.00 16.33  ? 140 THR A CG2 1 
ATOM   1131 N N   . LEU A 1 161 ? 11.368  11.489  11.255  1.00 15.67  ? 141 LEU A N   1 
ATOM   1132 C CA  . LEU A 1 161 ? 12.249  11.449  10.097  1.00 15.69  ? 141 LEU A CA  1 
ATOM   1133 C C   . LEU A 1 161 ? 11.522  11.973  8.851   1.00 16.47  ? 141 LEU A C   1 
ATOM   1134 O O   . LEU A 1 161 ? 12.140  12.668  8.052   1.00 17.69  ? 141 LEU A O   1 
ATOM   1135 C CB  . LEU A 1 161 ? 12.825  10.055  9.895   1.00 16.52  ? 141 LEU A CB  1 
ATOM   1136 C CG  . LEU A 1 161 ? 13.877  9.622   10.904  1.00 16.94  ? 141 LEU A CG  1 
ATOM   1137 C CD1 . LEU A 1 161 ? 14.394  8.224   10.600  1.00 18.02  ? 141 LEU A CD1 1 
ATOM   1138 C CD2 . LEU A 1 161 ? 15.045  10.569  11.003  1.00 18.33  ? 141 LEU A CD2 1 
ATOM   1139 N N   . ALA A 1 162 ? 10.255  11.628  8.664   1.00 16.63  ? 142 ALA A N   1 
ATOM   1140 C CA  . ALA A 1 162 ? 9.458   12.123  7.552   1.00 16.92  ? 142 ALA A CA  1 
ATOM   1141 C C   . ALA A 1 162 ? 9.346   13.637  7.666   1.00 17.61  ? 142 ALA A C   1 
ATOM   1142 O O   . ALA A 1 162 ? 9.521   14.332  6.656   1.00 18.30  ? 142 ALA A O   1 
ATOM   1143 C CB  . ALA A 1 162 ? 8.095   11.450  7.533   1.00 15.69  ? 142 ALA A CB  1 
ATOM   1144 N N   . GLU A 1 163 ? 9.032   14.126  8.874   1.00 17.13  ? 143 GLU A N   1 
ATOM   1145 C CA  . GLU A 1 163 ? 8.912   15.574  9.084   1.00 17.94  ? 143 GLU A CA  1 
ATOM   1146 C C   . GLU A 1 163 ? 10.236  16.298  8.774   1.00 18.20  ? 143 GLU A C   1 
ATOM   1147 O O   . GLU A 1 163 ? 10.277  17.342  8.084   1.00 19.03  ? 143 GLU A O   1 
ATOM   1148 C CB  . GLU A 1 163 ? 8.494   15.872  10.527  1.00 16.37  ? 143 GLU A CB  1 
ATOM   1149 C CG  . GLU A 1 163 ? 8.395   17.354  10.822  1.00 18.86  ? 143 GLU A CG  1 
ATOM   1150 C CD  . GLU A 1 163 ? 8.059   17.685  12.269  1.00 22.85  ? 143 GLU A CD  1 
ATOM   1151 O OE1 . GLU A 1 163 ? 8.135   18.874  12.666  1.00 24.85  ? 143 GLU A OE1 1 
ATOM   1152 O OE2 . GLU A 1 163 ? 7.696   16.774  13.001  1.00 26.61  ? 143 GLU A OE2 1 
ATOM   1153 N N   . GLN A 1 164 ? 11.332  15.786  9.312   1.00 17.44  ? 144 GLN A N   1 
ATOM   1154 C CA  . GLN A 1 164 ? 12.652  16.365  9.140   1.00 15.58  ? 144 GLN A CA  1 
ATOM   1155 C C   . GLN A 1 164 ? 13.081  16.331  7.680   1.00 17.64  ? 144 GLN A C   1 
ATOM   1156 O O   . GLN A 1 164 ? 13.655  17.283  7.167   1.00 18.68  ? 144 GLN A O   1 
ATOM   1157 C CB  . GLN A 1 164 ? 13.691  15.709  10.035  1.00 16.71  ? 144 GLN A CB  1 
ATOM   1158 C CG  . GLN A 1 164 ? 13.458  15.988  11.506  1.00 16.79  ? 144 GLN A CG  1 
ATOM   1159 C CD  . GLN A 1 164 ? 14.462  15.235  12.352  1.00 18.10  ? 144 GLN A CD  1 
ATOM   1160 O OE1 . GLN A 1 164 ? 15.668  15.245  12.097  1.00 17.82  ? 144 GLN A OE1 1 
ATOM   1161 N NE2 . GLN A 1 164 ? 13.961  14.558  13.369  1.00 17.82  ? 144 GLN A NE2 1 
ATOM   1162 N N   . TRP A 1 165 ? 12.836  15.216  6.997   1.00 17.80  ? 145 TRP A N   1 
ATOM   1163 C CA  . TRP A 1 165 ? 13.117  15.116  5.569   1.00 17.24  ? 145 TRP A CA  1 
ATOM   1164 C C   . TRP A 1 165 ? 12.448  16.262  4.794   1.00 18.89  ? 145 TRP A C   1 
ATOM   1165 O O   . TRP A 1 165 ? 13.107  16.924  4.006   1.00 18.80  ? 145 TRP A O   1 
ATOM   1166 C CB  . TRP A 1 165 ? 12.624  13.727  5.108   1.00 17.79  ? 145 TRP A CB  1 
ATOM   1167 C CG  . TRP A 1 165 ? 12.821  13.437  3.651   1.00 18.06  ? 145 TRP A CG  1 
ATOM   1168 C CD1 . TRP A 1 165 ? 13.659  14.056  2.756   1.00 17.70  ? 145 TRP A CD1 1 
ATOM   1169 C CD2 . TRP A 1 165 ? 12.190  12.375  2.920   1.00 18.33  ? 145 TRP A CD2 1 
ATOM   1170 N NE1 . TRP A 1 165 ? 13.555  13.483  1.520   1.00 18.77  ? 145 TRP A NE1 1 
ATOM   1171 C CE2 . TRP A 1 165 ? 12.697  12.416  1.602   1.00 18.96  ? 145 TRP A CE2 1 
ATOM   1172 C CE3 . TRP A 1 165 ? 11.287  11.373  3.274   1.00 19.35  ? 145 TRP A CE3 1 
ATOM   1173 C CZ2 . TRP A 1 165 ? 12.263  11.529  0.612   1.00 18.89  ? 145 TRP A CZ2 1 
ATOM   1174 C CZ3 . TRP A 1 165 ? 10.872  10.497  2.294   1.00 18.39  ? 145 TRP A CZ3 1 
ATOM   1175 C CH2 . TRP A 1 165 ? 11.411  10.530  1.016   1.00 19.37  ? 145 TRP A CH2 1 
ATOM   1176 N N   . LEU A 1 166 ? 11.140  16.437  4.996   1.00 17.83  ? 146 LEU A N   1 
ATOM   1177 C CA  . LEU A 1 166 ? 10.386  17.466  4.297   1.00 17.39  ? 146 LEU A CA  1 
ATOM   1178 C C   . LEU A 1 166 ? 10.903  18.853  4.675   1.00 18.58  ? 146 LEU A C   1 
ATOM   1179 O O   . LEU A 1 166 ? 10.990  19.708  3.803   1.00 20.10  ? 146 LEU A O   1 
ATOM   1180 C CB  . LEU A 1 166 ? 8.891   17.348  4.563   1.00 18.56  ? 146 LEU A CB  1 
ATOM   1181 C CG  . LEU A 1 166 ? 8.222   16.240  3.752   1.00 20.10  ? 146 LEU A CG  1 
ATOM   1182 C CD1 . LEU A 1 166 ? 6.891   15.807  4.341   1.00 20.93  ? 146 LEU A CD1 1 
ATOM   1183 C CD2 . LEU A 1 166 ? 8.059   16.681  2.299   1.00 20.10  ? 146 LEU A CD2 1 
ATOM   1184 N N   . THR A 1 167 ? 11.221  19.075  5.953   1.00 18.88  ? 147 THR A N   1 
ATOM   1185 C CA  . THR A 1 167 ? 11.691  20.380  6.393   1.00 19.57  ? 147 THR A CA  1 
ATOM   1186 C C   . THR A 1 167 ? 13.011  20.706  5.694   1.00 19.66  ? 147 THR A C   1 
ATOM   1187 O O   . THR A 1 167 ? 13.231  21.843  5.253   1.00 20.98  ? 147 THR A O   1 
ATOM   1188 C CB  . THR A 1 167 ? 11.786  20.423  7.932   1.00 20.20  ? 147 THR A CB  1 
ATOM   1189 O OG1 . THR A 1 167 ? 10.467  20.210  8.462   1.00 22.65  ? 147 THR A OG1 1 
ATOM   1190 C CG2 . THR A 1 167 ? 12.342  21.741  8.443   1.00 22.20  ? 147 THR A CG2 1 
ATOM   1191 N N   . LEU A 1 168 ? 13.930  19.751  5.636   1.00 20.47  ? 148 LEU A N   1 
ATOM   1192 C CA  . LEU A 1 168 ? 15.224  19.902  4.979   1.00 20.65  ? 148 LEU A CA  1 
ATOM   1193 C C   . LEU A 1 168 ? 15.081  20.087  3.469   1.00 22.25  ? 148 LEU A C   1 
ATOM   1194 O O   . LEU A 1 168 ? 15.816  20.911  2.883   1.00 27.48  ? 148 LEU A O   1 
ATOM   1195 C CB  . LEU A 1 168 ? 16.107  18.701  5.322   1.00 21.76  ? 148 LEU A CB  1 
ATOM   1196 C CG  . LEU A 1 168 ? 16.601  18.669  6.768   1.00 20.63  ? 148 LEU A CG  1 
ATOM   1197 C CD1 . LEU A 1 168 ? 17.102  17.267  7.114   1.00 20.77  ? 148 LEU A CD1 1 
ATOM   1198 C CD2 . LEU A 1 168 ? 17.702  19.710  6.972   1.00 21.34  ? 148 LEU A CD2 1 
ATOM   1199 N N   . ALA A 1 169 ? 14.079  19.432  2.872   1.00 21.02  ? 149 ALA A N   1 
ATOM   1200 C CA  . ALA A 1 169 ? 13.810  19.549  1.455   1.00 23.25  ? 149 ALA A CA  1 
ATOM   1201 C C   . ALA A 1 169 ? 13.179  20.894  1.086   1.00 25.43  ? 149 ALA A C   1 
ATOM   1202 O O   . ALA A 1 169 ? 13.508  21.437  0.014   1.00 27.47  ? 149 ALA A O   1 
ATOM   1203 C CB  . ALA A 1 169 ? 12.946  18.409  0.997   1.00 24.12  ? 149 ALA A CB  1 
ATOM   1204 N N   . ALA A 1 170 ? 12.247  21.390  1.929   1.00 23.50  ? 150 ALA A N   1 
ATOM   1205 C CA  . ALA A 1 170 ? 11.302  22.416  1.484   1.00 25.49  ? 150 ALA A CA  1 
ATOM   1206 C C   . ALA A 1 170 ? 11.327  23.710  2.293   1.00 25.84  ? 150 ALA A C   1 
ATOM   1207 O O   . ALA A 1 170 ? 10.674  24.679  1.871   1.00 28.16  ? 150 ALA A O   1 
ATOM   1208 C CB  . ALA A 1 170 ? 9.896   21.869  1.500   1.00 25.94  ? 150 ALA A CB  1 
ATOM   1209 N N   . ASP A 1 171 ? 12.032  23.735  3.430   1.00 26.58  ? 151 ASP A N   1 
ATOM   1210 C CA  . ASP A 1 171 ? 12.015  24.913  4.282   1.00 29.76  ? 151 ASP A CA  1 
ATOM   1211 C C   . ASP A 1 171 ? 13.407  25.509  4.368   1.00 33.16  ? 151 ASP A C   1 
ATOM   1212 O O   . ASP A 1 171 ? 14.170  25.194  5.280   1.00 28.60  ? 151 ASP A O   1 
ATOM   1213 C CB  . ASP A 1 171 ? 11.421  24.641  5.662   1.00 28.63  ? 151 ASP A CB  1 
ATOM   1214 C CG  . ASP A 1 171 ? 11.316  25.903  6.495   1.00 30.97  ? 151 ASP A CG  1 
ATOM   1215 O OD1 . ASP A 1 171 ? 11.710  26.988  5.970   1.00 33.93  ? 151 ASP A OD1 1 
ATOM   1216 O OD2 . ASP A 1 171 ? 10.800  25.808  7.620   1.00 33.14  ? 151 ASP A OD2 1 
ATOM   1217 N N   . PRO A 1 172 ? 13.695  26.508  3.498   1.00 41.01  ? 152 PRO A N   1 
ATOM   1218 C CA  . PRO A 1 172 ? 14.958  27.250  3.523   1.00 44.23  ? 152 PRO A CA  1 
ATOM   1219 C C   . PRO A 1 172 ? 15.289  27.926  4.850   1.00 40.94  ? 152 PRO A C   1 
ATOM   1220 O O   . PRO A 1 172 ? 16.455  28.095  5.181   1.00 42.56  ? 152 PRO A O   1 
ATOM   1221 C CB  . PRO A 1 172 ? 14.769  28.367  2.484   0.30 47.12  ? 152 PRO A CB  1 
ATOM   1222 C CG  . PRO A 1 172 ? 13.649  27.908  1.591   0.30 48.82  ? 152 PRO A CG  1 
ATOM   1223 C CD  . PRO A 1 172 ? 12.805  26.956  2.415   1.00 43.33  ? 152 PRO A CD  1 
ATOM   1224 N N   . ALA A 1 173 ? 14.251  28.338  5.590   1.00 40.03  ? 153 ALA A N   1 
ATOM   1225 C CA  . ALA A 1 173 ? 14.431  29.103  6.815   1.00 42.34  ? 153 ALA A CA  1 
ATOM   1226 C C   . ALA A 1 173 ? 14.774  28.199  7.998   1.00 38.62  ? 153 ALA A C   1 
ATOM   1227 O O   . ALA A 1 173 ? 15.098  28.686  9.073   1.00 43.61  ? 153 ALA A O   1 
ATOM   1228 C CB  . ALA A 1 173 ? 13.182  29.918  7.105   1.00 45.53  ? 153 ALA A CB  1 
ATOM   1229 N N   . ALA A 1 174 ? 14.697  26.877  7.846   1.00 33.05  ? 154 ALA A N   1 
ATOM   1230 C CA  . ALA A 1 174 ? 14.777  26.040  9.034   1.00 30.22  ? 154 ALA A CA  1 
ATOM   1231 C C   . ALA A 1 174 ? 16.220  25.954  9.539   1.00 25.64  ? 154 ALA A C   1 
ATOM   1232 O O   . ALA A 1 174 ? 17.152  25.791  8.765   1.00 27.03  ? 154 ALA A O   1 
ATOM   1233 C CB  . ALA A 1 174 ? 14.207  24.678  8.748   1.00 28.91  ? 154 ALA A CB  1 
ATOM   1234 N N   . GLN A 1 175 ? 16.363  26.074  10.862  1.00 26.69  ? 155 GLN A N   1 
ATOM   1235 C CA  . GLN A 1 175 ? 17.628  26.029  11.586  1.00 29.58  ? 155 GLN A CA  1 
ATOM   1236 C C   . GLN A 1 175 ? 18.348  24.685  11.413  1.00 25.15  ? 155 GLN A C   1 
ATOM   1237 O O   . GLN A 1 175 ? 17.791  23.655  11.764  1.00 26.89  ? 155 GLN A O   1 
ATOM   1238 C CB  . GLN A 1 175 ? 17.283  26.293  13.057  1.00 35.73  ? 155 GLN A CB  1 
ATOM   1239 C CG  . GLN A 1 175 ? 18.376  25.986  14.076  0.50 40.09  ? 155 GLN A CG  1 
ATOM   1240 C CD  . GLN A 1 175 ? 19.415  27.069  14.203  0.50 44.47  ? 155 GLN A CD  1 
ATOM   1241 O OE1 . GLN A 1 175 ? 19.094  28.250  14.267  0.50 49.17  ? 155 GLN A OE1 1 
ATOM   1242 N NE2 . GLN A 1 175 ? 20.676  26.672  14.224  0.50 48.02  ? 155 GLN A NE2 1 
ATOM   1243 N N   . PRO A 1 176 ? 19.606  24.644  10.904  1.00 23.84  ? 156 PRO A N   1 
ATOM   1244 C CA  . PRO A 1 176 ? 20.362  23.398  10.769  1.00 24.97  ? 156 PRO A CA  1 
ATOM   1245 C C   . PRO A 1 176 ? 20.802  22.882  12.135  1.00 24.28  ? 156 PRO A C   1 
ATOM   1246 O O   . PRO A 1 176 ? 20.992  23.664  13.085  1.00 26.95  ? 156 PRO A O   1 
ATOM   1247 C CB  . PRO A 1 176 ? 21.564  23.808  9.896   1.00 25.93  ? 156 PRO A CB  1 
ATOM   1248 C CG  . PRO A 1 176 ? 21.759  25.276  10.195  1.00 29.46  ? 156 PRO A CG  1 
ATOM   1249 C CD  . PRO A 1 176 ? 20.364  25.800  10.405  1.00 25.86  ? 156 PRO A CD  1 
ATOM   1250 N N   . TRP A 1 177 ? 20.935  21.555  12.237  1.00 23.38  ? 157 TRP A N   1 
ATOM   1251 C CA  . TRP A 1 177 ? 21.506  20.936  13.416  1.00 23.24  ? 157 TRP A CA  1 
ATOM   1252 C C   . TRP A 1 177 ? 21.917  19.509  13.065  1.00 21.94  ? 157 TRP A C   1 
ATOM   1253 O O   . TRP A 1 177 ? 21.400  18.915  12.122  1.00 21.39  ? 157 TRP A O   1 
ATOM   1254 C CB  . TRP A 1 177 ? 20.553  20.929  14.609  1.00 24.59  ? 157 TRP A CB  1 
ATOM   1255 C CG  . TRP A 1 177 ? 19.217  20.272  14.400  1.00 25.01  ? 157 TRP A CG  1 
ATOM   1256 C CD1 . TRP A 1 177 ? 18.124  20.793  13.771  1.00 25.33  ? 157 TRP A CD1 1 
ATOM   1257 C CD2 . TRP A 1 177 ? 18.815  18.963  14.845  1.00 24.89  ? 157 TRP A CD2 1 
ATOM   1258 N NE1 . TRP A 1 177 ? 17.074  19.918  13.797  1.00 26.03  ? 157 TRP A NE1 1 
ATOM   1259 C CE2 . TRP A 1 177 ? 17.473  18.779  14.435  1.00 24.23  ? 157 TRP A CE2 1 
ATOM   1260 C CE3 . TRP A 1 177 ? 19.458  17.935  15.535  1.00 24.98  ? 157 TRP A CE3 1 
ATOM   1261 C CZ2 . TRP A 1 177 ? 16.746  17.623  14.731  1.00 25.41  ? 157 TRP A CZ2 1 
ATOM   1262 C CZ3 . TRP A 1 177 ? 18.740  16.784  15.798  1.00 26.06  ? 157 TRP A CZ3 1 
ATOM   1263 C CH2 . TRP A 1 177 ? 17.412  16.630  15.392  1.00 24.01  ? 157 TRP A CH2 1 
ATOM   1264 N N   . THR A 1 178 ? 22.894  19.016  13.821  1.00 21.90  ? 158 THR A N   1 
ATOM   1265 C CA  . THR A 1 178 ? 23.273  17.614  13.763  1.00 21.07  ? 158 THR A CA  1 
ATOM   1266 C C   . THR A 1 178 ? 23.090  17.014  15.156  1.00 20.49  ? 158 THR A C   1 
ATOM   1267 O O   . THR A 1 178 ? 23.186  17.689  16.164  1.00 22.94  ? 158 THR A O   1 
ATOM   1268 C CB  . THR A 1 178 ? 24.708  17.469  13.220  1.00 24.47  ? 158 THR A CB  1 
ATOM   1269 O OG1 . THR A 1 178 ? 25.596  18.107  14.137  1.00 25.65  ? 158 THR A OG1 1 
ATOM   1270 C CG2 . THR A 1 178 ? 24.872  17.999  11.807  1.00 25.01  ? 158 THR A CG2 1 
ATOM   1271 N N   . ALA A 1 179 ? 22.897  15.689  15.194  1.00 20.73  ? 159 ALA A N   1 
ATOM   1272 C CA  . ALA A 1 179 ? 22.531  14.963  16.401  1.00 21.39  ? 159 ALA A CA  1 
ATOM   1273 C C   . ALA A 1 179 ? 23.760  14.263  16.971  1.00 21.20  ? 159 ALA A C   1 
ATOM   1274 O O   . ALA A 1 179 ? 24.673  13.908  16.240  1.00 23.13  ? 159 ALA A O   1 
ATOM   1275 C CB  . ALA A 1 179 ? 21.443  13.941  16.111  1.00 22.04  ? 159 ALA A CB  1 
ATOM   1276 N N   . SER A 1 180 ? 23.726  13.986  18.275  1.00 24.45  ? 160 SER A N   1 
ATOM   1277 C CA  . SER A 1 180 ? 24.779  13.231  18.942  1.00 25.53  ? 160 SER A CA  1 
ATOM   1278 C C   . SER A 1 180 ? 24.629  11.727  18.701  1.00 23.11  ? 160 SER A C   1 
ATOM   1279 O O   . SER A 1 180 ? 23.520  11.251  18.462  1.00 22.07  ? 160 SER A O   1 
ATOM   1280 C CB  . SER A 1 180 ? 24.737  13.453  20.424  1.00 26.67  ? 160 SER A CB  1 
ATOM   1281 O OG  . SER A 1 180 ? 24.790  14.832  20.689  1.00 35.05  ? 160 SER A OG  1 
ATOM   1282 N N   . ALA A 1 181 ? 25.759  11.017  18.790  1.00 23.02  ? 161 ALA A N   1 
ATOM   1283 C CA  . ALA A 1 181 ? 25.738  9.561   18.902  1.00 22.32  ? 161 ALA A CA  1 
ATOM   1284 C C   . ALA A 1 181 ? 25.412  9.194   20.343  1.00 22.35  ? 161 ALA A C   1 
ATOM   1285 O O   . ALA A 1 181 ? 26.184  9.510   21.260  1.00 25.15  ? 161 ALA A O   1 
ATOM   1286 C CB  . ALA A 1 181 ? 27.057  8.946   18.480  1.00 24.15  ? 161 ALA A CB  1 
ATOM   1287 N N   . LEU A 1 182 ? 24.309  8.473   20.530  1.00 21.36  ? 162 LEU A N   1 
ATOM   1288 C CA  . LEU A 1 182 ? 23.852  8.171   21.873  1.00 21.99  ? 162 LEU A CA  1 
ATOM   1289 C C   . LEU A 1 182 ? 24.286  6.765   22.269  1.00 22.05  ? 162 LEU A C   1 
ATOM   1290 O O   . LEU A 1 182 ? 24.450  5.870   21.425  1.00 23.08  ? 162 LEU A O   1 
ATOM   1291 C CB  . LEU A 1 182 ? 22.329  8.255   21.923  1.00 22.83  ? 162 LEU A CB  1 
ATOM   1292 C CG  . LEU A 1 182 ? 21.700  9.621   21.651  1.00 25.56  ? 162 LEU A CG  1 
ATOM   1293 C CD1 . LEU A 1 182 ? 20.189  9.544   21.831  1.00 26.48  ? 162 LEU A CD1 1 
ATOM   1294 C CD2 . LEU A 1 182 ? 22.298  10.670  22.566  1.00 28.22  ? 162 LEU A CD2 1 
ATOM   1295 N N   . PRO A 1 183 ? 24.415  6.515   23.579  1.00 23.51  ? 163 PRO A N   1 
ATOM   1296 C CA  . PRO A 1 183 ? 24.452  5.138   24.066  1.00 24.09  ? 163 PRO A CA  1 
ATOM   1297 C C   . PRO A 1 183 ? 23.183  4.415   23.631  1.00 24.05  ? 163 PRO A C   1 
ATOM   1298 O O   . PRO A 1 183 ? 22.158  5.018   23.387  1.00 23.00  ? 163 PRO A O   1 
ATOM   1299 C CB  . PRO A 1 183 ? 24.517  5.283   25.594  1.00 26.15  ? 163 PRO A CB  1 
ATOM   1300 C CG  . PRO A 1 183 ? 24.978  6.704   25.809  1.00 26.88  ? 163 PRO A CG  1 
ATOM   1301 C CD  . PRO A 1 183 ? 24.361  7.487   24.675  1.00 25.46  ? 163 PRO A CD  1 
ATOM   1302 N N   . PRO A 1 184 ? 23.190  3.070   23.578  1.00 24.69  ? 164 PRO A N   1 
ATOM   1303 C CA  . PRO A 1 184 ? 21.952  2.328   23.396  1.00 25.13  ? 164 PRO A CA  1 
ATOM   1304 C C   . PRO A 1 184 ? 20.966  2.589   24.537  1.00 25.85  ? 164 PRO A C   1 
ATOM   1305 O O   . PRO A 1 184 ? 21.358  2.933   25.655  1.00 26.55  ? 164 PRO A O   1 
ATOM   1306 C CB  . PRO A 1 184 ? 22.404  0.859   23.373  1.00 26.51  ? 164 PRO A CB  1 
ATOM   1307 C CG  . PRO A 1 184 ? 23.673  0.875   24.177  1.00 26.66  ? 164 PRO A CG  1 
ATOM   1308 C CD  . PRO A 1 184 ? 24.338  2.206   23.876  1.00 27.52  ? 164 PRO A CD  1 
ATOM   1309 N N   . ALA A 1 185 ? 19.677  2.452   24.216  1.00 25.36  ? 165 ALA A N   1 
ATOM   1310 C CA  . ALA A 1 185 ? 18.594  2.740   25.138  1.00 26.15  ? 165 ALA A CA  1 
ATOM   1311 C C   . ALA A 1 185 ? 18.802  2.063   26.493  1.00 27.83  ? 165 ALA A C   1 
ATOM   1312 O O   . ALA A 1 185 ? 18.687  2.717   27.523  1.00 29.42  ? 165 ALA A O   1 
ATOM   1313 C CB  . ALA A 1 185 ? 17.281  2.348   24.515  1.00 27.20  ? 165 ALA A CB  1 
ATOM   1314 N N   . GLU A 1 186 ? 19.133  0.763   26.517  1.00 28.37  ? 166 GLU A N   1 
ATOM   1315 C CA  . GLU A 1 186 ? 19.237  0.047   27.784  1.00 32.06  ? 166 GLU A CA  1 
ATOM   1316 C C   . GLU A 1 186 ? 20.280  0.682   28.707  1.00 32.00  ? 166 GLU A C   1 
ATOM   1317 O O   . GLU A 1 186 ? 20.111  0.659   29.930  1.00 35.32  ? 166 GLU A O   1 
ATOM   1318 C CB  . GLU A 1 186 ? 19.436  -1.465  27.570  1.00 34.55  ? 166 GLU A CB  1 
ATOM   1319 C CG  . GLU A 1 186 ? 20.725  -1.869  26.873  1.00 37.82  ? 166 GLU A CG  1 
ATOM   1320 C CD  . GLU A 1 186 ? 20.758  -3.277  26.270  1.00 39.71  ? 166 GLU A CD  1 
ATOM   1321 O OE1 . GLU A 1 186 ? 21.609  -4.126  26.696  1.00 46.47  ? 166 GLU A OE1 1 
ATOM   1322 O OE2 . GLU A 1 186 ? 19.979  -3.519  25.342  1.00 33.97  ? 166 GLU A OE2 1 
ATOM   1323 N N   . ASP A 1 187 ? 21.331  1.279   28.140  1.00 29.86  ? 167 ASP A N   1 
ATOM   1324 C CA  . ASP A 1 187 ? 22.392  1.881   28.926  1.00 31.46  ? 167 ASP A CA  1 
ATOM   1325 C C   . ASP A 1 187 ? 21.945  3.203   29.552  1.00 33.03  ? 167 ASP A C   1 
ATOM   1326 O O   . ASP A 1 187 ? 22.613  3.638   30.483  1.00 36.15  ? 167 ASP A O   1 
ATOM   1327 C CB  . ASP A 1 187 ? 23.679  2.065   28.118  1.00 32.64  ? 167 ASP A CB  1 
ATOM   1328 C CG  . ASP A 1 187 ? 24.435  0.780   27.796  1.00 35.16  ? 167 ASP A CG  1 
ATOM   1329 O OD1 . ASP A 1 187 ? 23.955  -0.318  28.158  1.00 36.52  ? 167 ASP A OD1 1 
ATOM   1330 O OD2 . ASP A 1 187 ? 25.488  0.883   27.155  1.00 38.66  ? 167 ASP A OD2 1 
ATOM   1331 N N   . LEU A 1 188 ? 20.835  3.809   29.070  1.00 28.34  ? 168 LEU A N   1 
ATOM   1332 C CA  . LEU A 1 188 ? 20.349  5.092   29.567  1.00 30.03  ? 168 LEU A CA  1 
ATOM   1333 C C   . LEU A 1 188 ? 19.261  4.954   30.639  1.00 31.65  ? 168 LEU A C   1 
ATOM   1334 O O   . LEU A 1 188 ? 18.714  5.966   31.125  1.00 33.03  ? 168 LEU A O   1 
ATOM   1335 C CB  . LEU A 1 188 ? 19.823  5.881   28.365  1.00 30.22  ? 168 LEU A CB  1 
ATOM   1336 C CG  . LEU A 1 188 ? 20.865  6.258   27.315  1.00 30.58  ? 168 LEU A CG  1 
ATOM   1337 C CD1 . LEU A 1 188 ? 20.192  6.801   26.057  1.00 30.47  ? 168 LEU A CD1 1 
ATOM   1338 C CD2 . LEU A 1 188 ? 21.875  7.244   27.886  1.00 33.01  ? 168 LEU A CD2 1 
ATOM   1339 N N   . ARG A 1 189 ? 18.959  3.709   30.978  1.00 30.57  ? 169 ARG A N   1 
ATOM   1340 C CA  . ARG A 1 189 ? 17.876  3.411   31.937  1.00 35.36  ? 169 ARG A CA  1 
ATOM   1341 C C   . ARG A 1 189 ? 18.202  3.920   33.334  1.00 36.73  ? 169 ARG A C   1 
ATOM   1342 O O   . ARG A 1 189 ? 19.386  3.945   33.696  1.00 37.78  ? 169 ARG A O   1 
ATOM   1343 C CB  . ARG A 1 189 ? 17.712  1.896   32.091  1.00 36.26  ? 169 ARG A CB  1 
ATOM   1344 C CG  . ARG A 1 189 ? 16.828  1.113   31.138  1.00 39.17  ? 169 ARG A CG  1 
ATOM   1345 C CD  . ARG A 1 189 ? 16.916  -0.351  31.521  1.00 38.43  ? 169 ARG A CD  1 
ATOM   1346 N NE  . ARG A 1 189 ? 18.275  -0.859  31.313  1.00 41.50  ? 169 ARG A NE  1 
ATOM   1347 C CZ  . ARG A 1 189 ? 18.683  -2.087  31.579  1.00 36.37  ? 169 ARG A CZ  1 
ATOM   1348 N NH1 . ARG A 1 189 ? 17.899  -2.919  32.232  1.00 40.41  ? 169 ARG A NH1 1 
ATOM   1349 N NH2 . ARG A 1 189 ? 19.881  -2.481  31.195  1.00 40.58  ? 169 ARG A NH2 1 
ATOM   1350 N N   . PRO A 1 190 ? 17.188  4.360   34.105  1.00 39.16  ? 170 PRO A N   1 
ATOM   1351 C CA  . PRO A 1 190 ? 17.415  4.687   35.503  1.00 38.80  ? 170 PRO A CA  1 
ATOM   1352 C C   . PRO A 1 190 ? 18.067  3.506   36.193  1.00 37.00  ? 170 PRO A C   1 
ATOM   1353 O O   . PRO A 1 190 ? 17.774  2.345   35.907  1.00 36.59  ? 170 PRO A O   1 
ATOM   1354 C CB  . PRO A 1 190 ? 16.018  5.007   36.017  1.00 38.82  ? 170 PRO A CB  1 
ATOM   1355 C CG  . PRO A 1 190 ? 15.300  5.499   34.785  1.00 37.70  ? 170 PRO A CG  1 
ATOM   1356 C CD  . PRO A 1 190 ? 15.835  4.621   33.664  1.00 38.36  ? 170 PRO A CD  1 
ATOM   1357 N N   . ARG A 1 191 ? 19.004  3.804   37.103  1.00 39.23  ? 171 ARG A N   1 
ATOM   1358 C CA  . ARG A 1 191 ? 19.807  2.752   37.783  1.00 38.51  ? 171 ARG A CA  1 
ATOM   1359 C C   . ARG A 1 191 ? 18.944  1.746   38.541  1.00 38.98  ? 171 ARG A C   1 
ATOM   1360 O O   . ARG A 1 191 ? 19.314  0.579   38.666  1.00 37.58  ? 171 ARG A O   1 
ATOM   1361 C CB  . ARG A 1 191 ? 20.733  3.391   38.814  1.00 41.39  ? 171 ARG A CB  1 
ATOM   1362 C CG  . ARG A 1 191 ? 21.786  4.288   38.180  0.00 85.94  ? 171 ARG A CG  1 
ATOM   1363 C CD  . ARG A 1 191 ? 22.730  4.856   39.223  0.00 104.74 ? 171 ARG A CD  1 
ATOM   1364 N NE  . ARG A 1 191 ? 23.911  5.463   38.602  0.00 125.41 ? 171 ARG A NE  1 
ATOM   1365 C CZ  . ARG A 1 191 ? 24.784  6.227   39.242  0.00 143.84 ? 171 ARG A CZ  1 
ATOM   1366 N NH1 . ARG A 1 191 ? 24.391  6.959   40.269  0.00 155.57 ? 171 ARG A NH1 1 
ATOM   1367 N NH2 . ARG A 1 191 ? 26.046  6.255   38.855  0.00 140.77 ? 171 ARG A NH2 1 
ATOM   1368 N N   . ARG A 1 192 ? 17.847  2.229   39.107  1.00 30.00  ? 172 ARG A N   1 
ATOM   1369 C CA  . ARG A 1 192 ? 16.937  1.330   39.858  1.00 30.00  ? 172 ARG A CA  1 
ATOM   1370 C C   . ARG A 1 192 ? 16.438  0.186   38.958  1.00 30.00  ? 172 ARG A C   1 
ATOM   1371 O O   . ARG A 1 192 ? 16.014  -0.833  39.491  1.00 30.00  ? 172 ARG A O   1 
ATOM   1372 C CB  . ARG A 1 192 ? 15.786  2.129   40.474  1.00 30.00  ? 172 ARG A CB  1 
ATOM   1373 C CG  . ARG A 1 192 ? 14.914  2.938   39.529  1.00 30.00  ? 172 ARG A CG  1 
ATOM   1374 C CD  . ARG A 1 192 ? 13.879  3.690   40.339  1.00 30.00  ? 172 ARG A CD  1 
ATOM   1375 N NE  . ARG A 1 192 ? 12.924  4.427   39.507  1.00 30.00  ? 172 ARG A NE  1 
ATOM   1376 C CZ  . ARG A 1 192 ? 13.187  5.561   38.879  1.00 30.00  ? 172 ARG A CZ  1 
ATOM   1377 N NH1 . ARG A 1 192 ? 14.356  6.152   39.035  1.00 30.00  ? 172 ARG A NH1 1 
ATOM   1378 N NH2 . ARG A 1 192 ? 12.276  6.104   38.095  1.00 30.00  ? 172 ARG A NH2 1 
ATOM   1379 N N   . PHE A 1 193 ? 16.530  0.349   37.637  1.00 38.48  ? 173 PHE A N   1 
ATOM   1380 C CA  . PHE A 1 193 ? 16.047  -0.703  36.713  1.00 39.19  ? 173 PHE A CA  1 
ATOM   1381 C C   . PHE A 1 193 ? 17.217  -1.469  36.102  1.00 38.63  ? 173 PHE A C   1 
ATOM   1382 O O   . PHE A 1 193 ? 17.028  -2.097  35.056  1.00 39.12  ? 173 PHE A O   1 
ATOM   1383 C CB  . PHE A 1 193 ? 15.159  -0.070  35.639  1.00 40.23  ? 173 PHE A CB  1 
ATOM   1384 C CG  . PHE A 1 193 ? 13.953  0.707   36.137  1.00 41.62  ? 173 PHE A CG  1 
ATOM   1385 C CD1 . PHE A 1 193 ? 12.852  0.047   36.665  1.00 44.92  ? 173 PHE A CD1 1 
ATOM   1386 C CD2 . PHE A 1 193 ? 13.915  2.090   36.052  1.00 45.24  ? 173 PHE A CD2 1 
ATOM   1387 C CE1 . PHE A 1 193 ? 11.754  0.759   37.111  1.00 45.63  ? 173 PHE A CE1 1 
ATOM   1388 C CE2 . PHE A 1 193 ? 12.812  2.794   36.497  1.00 46.45  ? 173 PHE A CE2 1 
ATOM   1389 C CZ  . PHE A 1 193 ? 11.737  2.127   37.025  1.00 43.59  ? 173 PHE A CZ  1 
ATOM   1390 N N   . THR A 1 194 ? 18.382  -1.455  36.757  1.00 39.66  ? 174 THR A N   1 
ATOM   1391 C CA  . THR A 1 194 ? 19.531  -2.207  36.278  1.00 37.40  ? 174 THR A CA  1 
ATOM   1392 C C   . THR A 1 194 ? 20.109  -3.057  37.401  1.00 37.60  ? 174 THR A C   1 
ATOM   1393 O O   . THR A 1 194 ? 19.788  -2.840  38.575  1.00 37.51  ? 174 THR A O   1 
ATOM   1394 C CB  . THR A 1 194 ? 20.631  -1.281  35.748  1.00 38.37  ? 174 THR A CB  1 
ATOM   1395 O OG1 . THR A 1 194 ? 21.179  -0.598  36.875  1.00 37.86  ? 174 THR A OG1 1 
ATOM   1396 C CG2 . THR A 1 194 ? 20.118  -0.292  34.729  1.00 41.31  ? 174 THR A CG2 1 
ATOM   1397 N N   . GLY A 1 195 ? 20.988  -3.991  37.001  1.00 36.92  ? 175 GLY A N   1 
ATOM   1398 C CA  . GLY A 1 195 ? 21.693  -4.862  37.927  1.00 39.21  ? 175 GLY A CA  1 
ATOM   1399 C C   . GLY A 1 195 ? 20.733  -5.680  38.783  1.00 39.41  ? 175 GLY A C   1 
ATOM   1400 O O   . GLY A 1 195 ? 19.652  -6.044  38.321  1.00 38.78  ? 175 GLY A O   1 
ATOM   1401 N N   . ASP A 1 196 ? 21.141  -5.937  40.037  1.00 43.80  ? 176 ASP A N   1 
ATOM   1402 C CA  . ASP A 1 196 ? 20.388  -6.786  40.950  1.00 47.14  ? 176 ASP A CA  1 
ATOM   1403 C C   . ASP A 1 196 ? 18.991  -6.204  41.218  1.00 46.64  ? 176 ASP A C   1 
ATOM   1404 O O   . ASP A 1 196 ? 18.007  -6.954  41.222  1.00 46.39  ? 176 ASP A O   1 
ATOM   1405 C CB  . ASP A 1 196 ? 21.152  -7.028  42.259  1.00 51.83  ? 176 ASP A CB  1 
ATOM   1406 C CG  . ASP A 1 196 ? 22.495  -7.732  42.112  1.00 56.91  ? 176 ASP A CG  1 
ATOM   1407 O OD1 . ASP A 1 196 ? 22.607  -8.631  41.241  1.00 59.91  ? 176 ASP A OD1 1 
ATOM   1408 O OD2 . ASP A 1 196 ? 23.414  -7.399  42.892  0.30 61.54  ? 176 ASP A OD2 1 
ATOM   1409 N N   . GLU A 1 197 ? 18.876  -4.879  41.420  1.00 44.69  ? 177 GLU A N   1 
ATOM   1410 C CA  . GLU A 1 197 ? 17.577  -4.281  41.695  1.00 45.98  ? 177 GLU A CA  1 
ATOM   1411 C C   . GLU A 1 197 ? 16.638  -4.399  40.486  1.00 43.41  ? 177 GLU A C   1 
ATOM   1412 O O   . GLU A 1 197 ? 15.452  -4.717  40.639  1.00 43.85  ? 177 GLU A O   1 
ATOM   1413 C CB  . GLU A 1 197 ? 17.690  -2.813  42.088  1.00 49.10  ? 177 GLU A CB  1 
ATOM   1414 C CG  . GLU A 1 197 ? 16.348  -2.249  42.512  1.00 51.39  ? 177 GLU A CG  1 
ATOM   1415 C CD  . GLU A 1 197 ? 16.347  -0.810  42.988  1.00 59.89  ? 177 GLU A CD  1 
ATOM   1416 O OE1 . GLU A 1 197 ? 15.236  -0.284  43.220  1.00 64.14  ? 177 GLU A OE1 1 
ATOM   1417 O OE2 . GLU A 1 197 ? 17.446  -0.224  43.127  0.50 65.42  ? 177 GLU A OE2 1 
ATOM   1418 N N   . GLY A 1 198 ? 17.148  -4.093  39.292  1.00 38.91  ? 178 GLY A N   1 
ATOM   1419 C CA  . GLY A 1 198 ? 16.371  -4.275  38.081  1.00 39.12  ? 178 GLY A CA  1 
ATOM   1420 C C   . GLY A 1 198 ? 15.866  -5.712  37.940  1.00 35.14  ? 178 GLY A C   1 
ATOM   1421 O O   . GLY A 1 198 ? 14.725  -5.950  37.536  1.00 34.81  ? 178 GLY A O   1 
ATOM   1422 N N   . ALA A 1 199 ? 16.732  -6.676  38.277  1.00 34.67  ? 179 ALA A N   1 
ATOM   1423 C CA  . ALA A 1 199 ? 16.340  -8.075  38.224  1.00 34.33  ? 179 ALA A CA  1 
ATOM   1424 C C   . ALA A 1 199 ? 15.237  -8.348  39.248  1.00 35.62  ? 179 ALA A C   1 
ATOM   1425 O O   . ALA A 1 199 ? 14.305  -9.102  38.951  1.00 34.70  ? 179 ALA A O   1 
ATOM   1426 C CB  . ALA A 1 199 ? 17.531  -8.981  38.418  1.00 36.00  ? 179 ALA A CB  1 
ATOM   1427 N N   . ALA A 1 200 ? 15.275  -7.675  40.410  1.00 36.53  ? 180 ALA A N   1 
ATOM   1428 C CA  . ALA A 1 200 ? 14.257  -7.911  41.433  1.00 41.35  ? 180 ALA A CA  1 
ATOM   1429 C C   . ALA A 1 200 ? 12.902  -7.348  40.990  1.00 39.13  ? 180 ALA A C   1 
ATOM   1430 O O   . ALA A 1 200 ? 11.844  -7.957  41.240  1.00 39.65  ? 180 ALA A O   1 
ATOM   1431 C CB  . ALA A 1 200 ? 14.692  -7.343  42.770  1.00 42.26  ? 180 ALA A CB  1 
ATOM   1432 N N   . ARG A 1 201 ? 12.951  -6.175  40.343  1.00 36.52  ? 181 ARG A N   1 
ATOM   1433 C CA  . ARG A 1 201 ? 11.770  -5.505  39.833  1.00 35.20  ? 181 ARG A CA  1 
ATOM   1434 C C   . ARG A 1 201 ? 11.085  -6.392  38.796  1.00 31.81  ? 181 ARG A C   1 
ATOM   1435 O O   . ARG A 1 201 ? 9.852   -6.538  38.813  1.00 32.66  ? 181 ARG A O   1 
ATOM   1436 C CB  . ARG A 1 201 ? 12.155  -4.128  39.281  1.00 37.93  ? 181 ARG A CB  1 
ATOM   1437 C CG  . ARG A 1 201 ? 12.507  -3.142  40.383  1.00 39.72  ? 181 ARG A CG  1 
ATOM   1438 C CD  . ARG A 1 201 ? 13.180  -1.893  39.864  1.00 42.44  ? 181 ARG A CD  1 
ATOM   1439 N NE  . ARG A 1 201 ? 13.210  -0.794  40.823  1.00 47.72  ? 181 ARG A NE  1 
ATOM   1440 C CZ  . ARG A 1 201 ? 12.158  -0.068  41.185  1.00 51.91  ? 181 ARG A CZ  1 
ATOM   1441 N NH1 . ARG A 1 201 ? 10.940  -0.387  40.785  0.70 57.09  ? 181 ARG A NH1 1 
ATOM   1442 N NH2 . ARG A 1 201 ? 12.333  0.985   41.964  0.70 55.88  ? 181 ARG A NH2 1 
ATOM   1443 N N   . LEU A 1 202 ? 11.898  -7.014  37.932  1.00 32.63  ? 182 LEU A N   1 
ATOM   1444 C CA  . LEU A 1 202 ? 11.374  -7.875  36.883  1.00 30.59  ? 182 LEU A CA  1 
ATOM   1445 C C   . LEU A 1 202 ? 10.750  -9.122  37.499  1.00 32.35  ? 182 LEU A C   1 
ATOM   1446 O O   . LEU A 1 202 ? 9.693   -9.559  37.044  1.00 30.95  ? 182 LEU A O   1 
ATOM   1447 C CB  . LEU A 1 202 ? 12.479  -8.241  35.893  1.00 29.32  ? 182 LEU A CB  1 
ATOM   1448 C CG  . LEU A 1 202 ? 12.132  -9.349  34.897  1.00 30.43  ? 182 LEU A CG  1 
ATOM   1449 C CD1 . LEU A 1 202 ? 10.936  -8.989  34.024  1.00 29.16  ? 182 LEU A CD1 1 
ATOM   1450 C CD2 . LEU A 1 202 ? 13.330  -9.699  34.033  1.00 30.17  ? 182 LEU A CD2 1 
ATOM   1451 N N   . ALA A 1 203 ? 11.404  -9.675  38.526  1.00 32.74  ? 183 ALA A N   1 
ATOM   1452 C CA  . ALA A 1 203 ? 10.875  -10.851 39.205  1.00 34.15  ? 183 ALA A CA  1 
ATOM   1453 C C   . ALA A 1 203 ? 9.497   -10.546 39.805  1.00 30.67  ? 183 ALA A C   1 
ATOM   1454 O O   . ALA A 1 203 ? 8.584   -11.366 39.719  1.00 32.86  ? 183 ALA A O   1 
ATOM   1455 C CB  . ALA A 1 203 ? 11.848  -11.339 40.263  1.00 33.88  ? 183 ALA A CB  1 
ATOM   1456 N N   . GLU A 1 204 ? 9.352   -9.389  40.429  1.00 34.84  ? 184 GLU A N   1 
ATOM   1457 C CA  . GLU A 1 204 ? 8.065   -9.041  41.079  1.00 36.99  ? 184 GLU A CA  1 
ATOM   1458 C C   . GLU A 1 204 ? 6.955   -8.929  40.013  1.00 33.84  ? 184 GLU A C   1 
ATOM   1459 O O   . GLU A 1 204 ? 5.885   -9.497  40.206  1.00 35.12  ? 184 GLU A O   1 
ATOM   1460 C CB  . GLU A 1 204 ? 8.217   -7.768  41.903  1.00 42.20  ? 184 GLU A CB  1 
ATOM   1461 C CG  . GLU A 1 204 ? 6.956   -7.410  42.681  0.70 47.62  ? 184 GLU A CG  1 
ATOM   1462 C CD  . GLU A 1 204 ? 7.209   -6.423  43.802  1.00 53.54  ? 184 GLU A CD  1 
ATOM   1463 O OE1 . GLU A 1 204 ? 6.278   -6.169  44.594  0.50 52.50  ? 184 GLU A OE1 1 
ATOM   1464 O OE2 . GLU A 1 204 ? 8.344   -5.914  43.882  0.70 63.10  ? 184 GLU A OE2 1 
ATOM   1465 N N   . GLN A 1 205 ? 7.222   -8.213  38.918  1.00 30.68  ? 185 GLN A N   1 
ATOM   1466 C CA  . GLN A 1 205 ? 6.208   -8.085  37.885  1.00 28.68  ? 185 GLN A CA  1 
ATOM   1467 C C   . GLN A 1 205 ? 5.860   -9.455  37.316  1.00 26.37  ? 185 GLN A C   1 
ATOM   1468 O O   . GLN A 1 205 ? 4.690   -9.737  37.048  1.00 29.22  ? 185 GLN A O   1 
ATOM   1469 C CB  . GLN A 1 205 ? 6.649   -7.173  36.740  1.00 29.46  ? 185 GLN A CB  1 
ATOM   1470 C CG  . GLN A 1 205 ? 5.596   -7.067  35.649  1.00 29.20  ? 185 GLN A CG  1 
ATOM   1471 C CD  . GLN A 1 205 ? 6.051   -6.401  34.373  1.00 27.07  ? 185 GLN A CD  1 
ATOM   1472 O OE1 . GLN A 1 205 ? 7.075   -5.708  34.318  1.00 28.71  ? 185 GLN A OE1 1 
ATOM   1473 N NE2 . GLN A 1 205 ? 5.254   -6.590  33.332  1.00 27.21  ? 185 GLN A NE2 1 
ATOM   1474 N N   . THR A 1 206 ? 6.877   -10.297 37.119  1.00 29.00  ? 186 THR A N   1 
ATOM   1475 C CA  . THR A 1 206 ? 6.657   -11.576 36.471  1.00 29.58  ? 186 THR A CA  1 
ATOM   1476 C C   . THR A 1 206 ? 5.734   -12.456 37.324  1.00 30.56  ? 186 THR A C   1 
ATOM   1477 O O   . THR A 1 206 ? 4.829   -13.109 36.785  1.00 26.92  ? 186 THR A O   1 
ATOM   1478 C CB  . THR A 1 206 ? 7.995   -12.273 36.194  1.00 31.76  ? 186 THR A CB  1 
ATOM   1479 O OG1 . THR A 1 206 ? 8.757   -11.509 35.252  1.00 32.87  ? 186 THR A OG1 1 
ATOM   1480 C CG2 . THR A 1 206 ? 7.829   -13.676 35.659  1.00 32.84  ? 186 THR A CG2 1 
ATOM   1481 N N   . ALA A 1 207 ? 5.954   -12.507 38.648  1.00 31.40  ? 187 ALA A N   1 
ATOM   1482 C CA  . ALA A 1 207 ? 5.103   -13.331 39.512  1.00 32.75  ? 187 ALA A CA  1 
ATOM   1483 C C   . ALA A 1 207 ? 3.656   -12.819 39.506  1.00 32.32  ? 187 ALA A C   1 
ATOM   1484 O O   . ALA A 1 207 ? 2.707   -13.593 39.431  1.00 31.34  ? 187 ALA A O   1 
ATOM   1485 C CB  . ALA A 1 207 ? 5.654   -13.347 40.912  1.00 34.69  ? 187 ALA A CB  1 
ATOM   1486 N N   . GLN A 1 208 ? 3.485   -11.497 39.590  1.00 28.99  ? 188 GLN A N   1 
ATOM   1487 C CA  . GLN A 1 208 ? 2.179   -10.865 39.536  1.00 29.35  ? 188 GLN A CA  1 
ATOM   1488 C C   . GLN A 1 208 ? 1.450   -11.180 38.227  1.00 25.56  ? 188 GLN A C   1 
ATOM   1489 O O   . GLN A 1 208 ? 0.247   -11.412 38.249  1.00 25.87  ? 188 GLN A O   1 
ATOM   1490 C CB  . GLN A 1 208 ? 2.309   -9.343  39.653  1.00 29.56  ? 188 GLN A CB  1 
ATOM   1491 C CG  . GLN A 1 208 ? 2.877   -8.841  40.962  1.00 34.26  ? 188 GLN A CG  1 
ATOM   1492 C CD  . GLN A 1 208 ? 3.188   -7.361  40.954  1.00 37.55  ? 188 GLN A CD  1 
ATOM   1493 O OE1 . GLN A 1 208 ? 3.519   -6.747  39.931  1.00 38.58  ? 188 GLN A OE1 1 
ATOM   1494 N NE2 . GLN A 1 208 ? 3.110   -6.772  42.138  1.00 43.24  ? 188 GLN A NE2 1 
ATOM   1495 N N   . ASP A 1 209 ? 2.144   -11.104 37.084  1.00 25.00  ? 189 ASP A N   1 
ATOM   1496 C CA  . ASP A 1 209 ? 1.522   -11.338 35.790  1.00 26.06  ? 189 ASP A CA  1 
ATOM   1497 C C   . ASP A 1 209 ? 1.135   -12.818 35.641  1.00 26.55  ? 189 ASP A C   1 
ATOM   1498 O O   . ASP A 1 209 ? 0.068   -13.114 35.108  1.00 26.71  ? 189 ASP A O   1 
ATOM   1499 C CB  . ASP A 1 209 ? 2.385   -10.833 34.625  1.00 26.80  ? 189 ASP A CB  1 
ATOM   1500 C CG  . ASP A 1 209 ? 2.514   -9.316  34.566  1.00 29.95  ? 189 ASP A CG  1 
ATOM   1501 O OD1 . ASP A 1 209 ? 1.797   -8.627  35.341  1.00 32.87  ? 189 ASP A OD1 1 
ATOM   1502 O OD2 . ASP A 1 209 ? 3.343   -8.825  33.744  1.00 31.93  ? 189 ASP A OD2 1 
ATOM   1503 N N   . GLU A 1 210 ? 1.980   -13.739 36.129  1.00 27.07  ? 190 GLU A N   1 
ATOM   1504 C CA  . GLU A 1 210 ? 1.640   -15.160 36.121  1.00 27.94  ? 190 GLU A CA  1 
ATOM   1505 C C   . GLU A 1 210 ? 0.374   -15.411 36.959  1.00 26.47  ? 190 GLU A C   1 
ATOM   1506 O O   . GLU A 1 210 ? -0.497  -16.233 36.593  1.00 27.07  ? 190 GLU A O   1 
ATOM   1507 C CB  . GLU A 1 210 ? 2.800   -15.965 36.694  1.00 30.84  ? 190 GLU A CB  1 
ATOM   1508 C CG  . GLU A 1 210 ? 4.001   -16.152 35.770  1.00 34.42  ? 190 GLU A CG  1 
ATOM   1509 C CD  . GLU A 1 210 ? 5.147   -16.893 36.454  1.00 38.05  ? 190 GLU A CD  1 
ATOM   1510 O OE1 . GLU A 1 210 ? 6.246   -16.988 35.865  1.00 40.53  ? 190 GLU A OE1 1 
ATOM   1511 O OE2 . GLU A 1 210 ? 4.933   -17.384 37.595  1.00 40.92  ? 190 GLU A OE2 1 
ATOM   1512 N N   . ALA A 1 211 ? 0.277   -14.707 38.110  1.00 24.84  ? 191 ALA A N   1 
ATOM   1513 C CA  . ALA A 1 211 ? -0.894  -14.815 38.970  1.00 24.34  ? 191 ALA A CA  1 
ATOM   1514 C C   . ALA A 1 211 ? -2.155  -14.331 38.244  1.00 23.11  ? 191 ALA A C   1 
ATOM   1515 O O   . ALA A 1 211 ? -3.209  -14.964 38.298  1.00 23.09  ? 191 ALA A O   1 
ATOM   1516 C CB  . ALA A 1 211 ? -0.656  -14.093 40.259  1.00 24.93  ? 191 ALA A CB  1 
ATOM   1517 N N   . LEU A 1 212 ? -2.066  -13.198 37.532  1.00 23.50  ? 192 LEU A N   1 
ATOM   1518 C CA  . LEU A 1 212 ? -3.209  -12.711 36.768  1.00 23.25  ? 192 LEU A CA  1 
ATOM   1519 C C   . LEU A 1 212 ? -3.657  -13.696 35.683  1.00 23.67  ? 192 LEU A C   1 
ATOM   1520 O O   . LEU A 1 212 ? -4.856  -13.849 35.424  1.00 24.14  ? 192 LEU A O   1 
ATOM   1521 C CB  . LEU A 1 212 ? -2.860  -11.351 36.178  1.00 24.58  ? 192 LEU A CB  1 
ATOM   1522 C CG  . LEU A 1 212 ? -2.791  -10.225 37.206  1.00 26.33  ? 192 LEU A CG  1 
ATOM   1523 C CD1 . LEU A 1 212 ? -2.153  -8.998  36.594  1.00 27.98  ? 192 LEU A CD1 1 
ATOM   1524 C CD2 . LEU A 1 212 ? -4.152  -9.856  37.770  1.00 25.57  ? 192 LEU A CD2 1 
ATOM   1525 N N   . VAL A 1 213 ? -2.696  -14.350 35.029  1.00 26.13  ? 193 VAL A N   1 
ATOM   1526 C CA  . VAL A 1 213 ? -3.027  -15.351 34.022  1.00 26.84  ? 193 VAL A CA  1 
ATOM   1527 C C   . VAL A 1 213 ? -3.775  -16.509 34.674  1.00 26.90  ? 193 VAL A C   1 
ATOM   1528 O O   . VAL A 1 213 ? -4.792  -16.964 34.147  1.00 26.45  ? 193 VAL A O   1 
ATOM   1529 C CB  . VAL A 1 213 ? -1.767  -15.824 33.269  1.00 28.35  ? 193 VAL A CB  1 
ATOM   1530 C CG1 . VAL A 1 213 ? -2.019  -17.086 32.468  1.00 31.09  ? 193 VAL A CG1 1 
ATOM   1531 C CG2 . VAL A 1 213 ? -1.236  -14.730 32.364  1.00 27.26  ? 193 VAL A CG2 1 
ATOM   1532 N N   . GLY A 1 214 ? -3.268  -16.986 35.816  1.00 27.35  ? 194 GLY A N   1 
ATOM   1533 C CA  . GLY A 1 214 ? -3.922  -18.087 36.501  1.00 27.25  ? 194 GLY A CA  1 
ATOM   1534 C C   . GLY A 1 214 ? -5.303  -17.734 37.051  1.00 23.05  ? 194 GLY A C   1 
ATOM   1535 O O   . GLY A 1 214 ? -6.219  -18.543 37.021  1.00 25.28  ? 194 GLY A O   1 
ATOM   1536 N N   . ARG A 1 215 ? -5.474  -16.473 37.483  1.00 20.87  ? 195 ARG A N   1 
ATOM   1537 C CA  . ARG A 1 215 ? -6.721  -15.986 38.031  1.00 22.09  ? 195 ARG A CA  1 
ATOM   1538 C C   . ARG A 1 215 ? -7.778  -15.797 36.937  1.00 23.97  ? 195 ARG A C   1 
ATOM   1539 O O   . ARG A 1 215 ? -8.948  -16.133 37.131  1.00 25.22  ? 195 ARG A O   1 
ATOM   1540 C CB  . ARG A 1 215 ? -6.526  -14.640 38.730  1.00 22.82  ? 195 ARG A CB  1 
ATOM   1541 C CG  . ARG A 1 215 ? -7.792  -14.154 39.423  1.00 23.69  ? 195 ARG A CG  1 
ATOM   1542 C CD  . ARG A 1 215 ? -7.536  -12.936 40.296  1.00 25.52  ? 195 ARG A CD  1 
ATOM   1543 N NE  . ARG A 1 215 ? -6.795  -13.268 41.492  1.00 24.91  ? 195 ARG A NE  1 
ATOM   1544 C CZ  . ARG A 1 215 ? -7.311  -13.802 42.590  1.00 27.45  ? 195 ARG A CZ  1 
ATOM   1545 N NH1 . ARG A 1 215 ? -8.593  -14.110 42.649  1.00 27.32  ? 195 ARG A NH1 1 
ATOM   1546 N NH2 . ARG A 1 215 ? -6.527  -14.024 43.640  1.00 30.00  ? 195 ARG A NH2 1 
ATOM   1547 N N   . HIS A 1 216 ? -7.371  -15.219 35.802  1.00 25.14  ? 196 HIS A N   1 
ATOM   1548 C CA  . HIS A 1 216 ? -8.333  -14.714 34.838  1.00 24.79  ? 196 HIS A CA  1 
ATOM   1549 C C   . HIS A 1 216 ? -8.373  -15.472 33.509  1.00 25.59  ? 196 HIS A C   1 
ATOM   1550 O O   . HIS A 1 216 ? -9.314  -15.288 32.733  1.00 28.74  ? 196 HIS A O   1 
ATOM   1551 C CB  . HIS A 1 216 ? -8.053  -13.249 34.533  1.00 24.66  ? 196 HIS A CB  1 
ATOM   1552 C CG  . HIS A 1 216 ? -8.239  -12.370 35.716  1.00 24.64  ? 196 HIS A CG  1 
ATOM   1553 N ND1 . HIS A 1 216 ? -9.414  -12.325 36.434  1.00 24.51  ? 196 HIS A ND1 1 
ATOM   1554 C CD2 . HIS A 1 216 ? -7.395  -11.493 36.297  1.00 25.68  ? 196 HIS A CD2 1 
ATOM   1555 C CE1 . HIS A 1 216 ? -9.275  -11.444 37.430  1.00 26.57  ? 196 HIS A CE1 1 
ATOM   1556 N NE2 . HIS A 1 216 ? -8.055  -10.945 37.376  1.00 27.65  ? 196 HIS A NE2 1 
ATOM   1557 N N   . ARG A 1 217 ? -7.348  -16.274 33.259  1.00 24.79  ? 197 ARG A N   1 
ATOM   1558 C CA  . ARG A 1 217 ? -7.295  -17.133 32.049  1.00 27.52  ? 197 ARG A CA  1 
ATOM   1559 C C   . ARG A 1 217 ? -7.474  -16.321 30.766  1.00 27.40  ? 197 ARG A C   1 
ATOM   1560 O O   . ARG A 1 217 ? -8.322  -16.681 29.955  1.00 27.61  ? 197 ARG A O   1 
ATOM   1561 C CB  . ARG A 1 217 ? -8.392  -18.193 32.125  1.00 28.88  ? 197 ARG A CB  1 
ATOM   1562 C CG  . ARG A 1 217 ? -8.421  -18.952 33.445  1.00 29.24  ? 197 ARG A CG  1 
ATOM   1563 C CD  . ARG A 1 217 ? -7.165  -19.763 33.690  1.00 25.71  ? 197 ARG A CD  1 
ATOM   1564 N NE  . ARG A 1 217 ? -7.243  -20.501 34.955  1.00 26.87  ? 197 ARG A NE  1 
ATOM   1565 C CZ  . ARG A 1 217 ? -7.607  -21.772 35.063  1.00 25.40  ? 197 ARG A CZ  1 
ATOM   1566 N NH1 . ARG A 1 217 ? -8.198  -22.378 34.054  1.00 25.82  ? 197 ARG A NH1 1 
ATOM   1567 N NH2 . ARG A 1 217 ? -7.377  -22.430 36.182  1.00 27.11  ? 197 ARG A NH2 1 
ATOM   1568 N N   . PRO A 1 218 ? -6.682  -15.254 30.543  1.00 25.80  ? 198 PRO A N   1 
ATOM   1569 C CA  . PRO A 1 218 ? -6.941  -14.406 29.377  1.00 26.08  ? 198 PRO A CA  1 
ATOM   1570 C C   . PRO A 1 218 ? -6.625  -15.105 28.060  1.00 25.49  ? 198 PRO A C   1 
ATOM   1571 O O   . PRO A 1 218 ? -5.668  -15.875 27.973  1.00 25.48  ? 198 PRO A O   1 
ATOM   1572 C CB  . PRO A 1 218 ? -5.976  -13.234 29.561  1.00 26.01  ? 198 PRO A CB  1 
ATOM   1573 C CG  . PRO A 1 218 ? -4.850  -13.821 30.387  1.00 26.79  ? 198 PRO A CG  1 
ATOM   1574 C CD  . PRO A 1 218 ? -5.502  -14.840 31.310  1.00 26.20  ? 198 PRO A CD  1 
ATOM   1575 N N   . GLY A 1 219 ? -7.394  -14.793 27.025  1.00 24.95  ? 199 GLY A N   1 
ATOM   1576 C CA  . GLY A 1 219 ? -7.061  -15.255 25.701  1.00 24.33  ? 199 GLY A CA  1 
ATOM   1577 C C   . GLY A 1 219 ? -5.984  -14.381 25.064  1.00 23.24  ? 199 GLY A C   1 
ATOM   1578 O O   . GLY A 1 219 ? -5.780  -13.215 25.439  1.00 23.42  ? 199 GLY A O   1 
ATOM   1579 N N   . ARG A 1 220 ? -5.323  -14.969 24.069  1.00 22.92  ? 200 ARG A N   1 
ATOM   1580 C CA  . ARG A 1 220 ? -4.346  -14.331 23.203  1.00 24.33  ? 200 ARG A CA  1 
ATOM   1581 C C   . ARG A 1 220 ? -4.788  -14.580 21.763  1.00 25.05  ? 200 ARG A C   1 
ATOM   1582 O O   . ARG A 1 220 ? -5.717  -15.353 21.516  1.00 25.75  ? 200 ARG A O   1 
ATOM   1583 C CB  . ARG A 1 220 ? -2.942  -14.883 23.502  1.00 28.04  ? 200 ARG A CB  1 
ATOM   1584 C CG  . ARG A 1 220 ? -2.434  -14.642 24.926  1.00 29.36  ? 200 ARG A CG  1 
ATOM   1585 C CD  . ARG A 1 220 ? -1.212  -15.452 25.359  1.00 31.52  ? 200 ARG A CD  1 
ATOM   1586 N NE  . ARG A 1 220 ? 0.020   -15.212 24.587  1.00 33.03  ? 200 ARG A NE  1 
ATOM   1587 C CZ  . ARG A 1 220 ? 0.876   -14.196 24.774  1.00 33.32  ? 200 ARG A CZ  1 
ATOM   1588 N NH1 . ARG A 1 220 ? 1.988   -14.130 24.055  1.00 32.04  ? 200 ARG A NH1 1 
ATOM   1589 N NH2 . ARG A 1 220 ? 0.619   -13.249 25.668  1.00 32.27  ? 200 ARG A NH2 1 
ATOM   1590 N N   . ILE A 1 221 ? -4.162  -13.900 20.795  1.00 23.80  ? 201 ILE A N   1 
ATOM   1591 C CA  . ILE A 1 221 ? -4.403  -14.240 19.404  1.00 24.22  ? 201 ILE A CA  1 
ATOM   1592 C C   . ILE A 1 221 ? -3.741  -15.582 19.136  1.00 24.93  ? 201 ILE A C   1 
ATOM   1593 O O   . ILE A 1 221 ? -2.523  -15.709 19.340  1.00 25.30  ? 201 ILE A O   1 
ATOM   1594 C CB  . ILE A 1 221 ? -3.840  -13.174 18.441  1.00 25.54  ? 201 ILE A CB  1 
ATOM   1595 C CG1 . ILE A 1 221 ? -4.452  -11.783 18.641  1.00 25.20  ? 201 ILE A CG1 1 
ATOM   1596 C CG2 . ILE A 1 221 ? -3.976  -13.650 17.004  1.00 27.15  ? 201 ILE A CG2 1 
ATOM   1597 C CD1 . ILE A 1 221 ? -5.844  -11.680 18.158  1.00 27.02  ? 201 ILE A CD1 1 
ATOM   1598 N N   . GLU A 1 222 ? -4.543  -16.531 18.639  1.00 25.09  ? 202 GLU A N   1 
ATOM   1599 C CA  . GLU A 1 222 ? -4.074  -17.879 18.316  1.00 27.20  ? 202 GLU A CA  1 
ATOM   1600 C C   . GLU A 1 222 ? -4.077  -18.014 16.798  1.00 27.12  ? 202 GLU A C   1 
ATOM   1601 O O   . GLU A 1 222 ? -5.049  -17.620 16.154  1.00 27.99  ? 202 GLU A O   1 
ATOM   1602 C CB  . GLU A 1 222 ? -4.974  -18.959 18.935  1.00 30.28  ? 202 GLU A CB  1 
ATOM   1603 C CG  . GLU A 1 222 ? -5.015  -18.933 20.456  1.00 31.83  ? 202 GLU A CG  1 
ATOM   1604 C CD  . GLU A 1 222 ? -3.677  -19.177 21.149  1.00 33.62  ? 202 GLU A CD  1 
ATOM   1605 O OE1 . GLU A 1 222 ? -2.773  -19.770 20.513  1.00 39.57  ? 202 GLU A OE1 1 
ATOM   1606 O OE2 . GLU A 1 222 ? -3.511  -18.742 22.301  1.00 37.53  ? 202 GLU A OE2 1 
ATOM   1607 N N   . PRO A 1 223 ? -2.999  -18.537 16.172  1.00 28.58  ? 203 PRO A N   1 
ATOM   1608 C CA  . PRO A 1 223 ? -2.959  -18.683 14.714  1.00 29.30  ? 203 PRO A CA  1 
ATOM   1609 C C   . PRO A 1 223 ? -4.003  -19.623 14.132  1.00 26.14  ? 203 PRO A C   1 
ATOM   1610 O O   . PRO A 1 223 ? -4.236  -20.709 14.657  1.00 30.06  ? 203 PRO A O   1 
ATOM   1611 C CB  . PRO A 1 223 ? -1.548  -19.207 14.410  1.00 31.23  ? 203 PRO A CB  1 
ATOM   1612 C CG  . PRO A 1 223 ? -1.079  -19.774 15.724  1.00 35.17  ? 203 PRO A CG  1 
ATOM   1613 C CD  . PRO A 1 223 ? -1.732  -18.925 16.800  1.00 33.69  ? 203 PRO A CD  1 
ATOM   1614 N N   . SER A 1 224 ? -4.553  -19.232 12.990  1.00 27.58  ? 204 SER A N   1 
ATOM   1615 C CA  . SER A 1 224 ? -5.483  -20.047 12.218  1.00 28.59  ? 204 SER A CA  1 
ATOM   1616 C C   . SER A 1 224 ? -4.762  -21.243 11.593  1.00 29.54  ? 204 SER A C   1 
ATOM   1617 O O   . SER A 1 224 ? -5.349  -22.301 11.392  1.00 34.54  ? 204 SER A O   1 
ATOM   1618 C CB  . SER A 1 224 ? -6.140  -19.243 11.122  1.00 28.44  ? 204 SER A CB  1 
ATOM   1619 O OG  . SER A 1 224 ? -6.957  -18.222 11.658  1.00 29.81  ? 204 SER A OG  1 
ATOM   1620 N N   . ASN A 1 225 ? -3.505  -21.003 11.222  1.00 29.75  ? 205 ASN A N   1 
ATOM   1621 C CA  . ASN A 1 225 ? -2.648  -21.967 10.563  1.00 31.09  ? 205 ASN A CA  1 
ATOM   1622 C C   . ASN A 1 225 ? -1.247  -21.775 11.114  1.00 31.40  ? 205 ASN A C   1 
ATOM   1623 O O   . ASN A 1 225 ? -0.831  -20.639 11.374  1.00 30.05  ? 205 ASN A O   1 
ATOM   1624 C CB  . ASN A 1 225 ? -2.580  -21.746 9.046   1.00 33.82  ? 205 ASN A CB  1 
ATOM   1625 C CG  . ASN A 1 225 ? -3.939  -21.737 8.387   1.00 34.57  ? 205 ASN A CG  1 
ATOM   1626 O OD1 . ASN A 1 225 ? -4.557  -22.794 8.229   1.00 37.82  ? 205 ASN A OD1 1 
ATOM   1627 N ND2 . ASN A 1 225 ? -4.409  -20.556 8.012   1.00 38.45  ? 205 ASN A ND2 1 
ATOM   1628 N N   . PRO A 1 226 ? -0.458  -22.840 11.261  1.00 35.71  ? 206 PRO A N   1 
ATOM   1629 C CA  . PRO A 1 226 ? 0.909   -22.702 11.750  1.00 37.95  ? 206 PRO A CA  1 
ATOM   1630 C C   . PRO A 1 226 ? 1.768   -22.093 10.649  1.00 36.46  ? 206 PRO A C   1 
ATOM   1631 O O   . PRO A 1 226 ? 1.662   -22.480 9.491   1.00 40.32  ? 206 PRO A O   1 
ATOM   1632 C CB  . PRO A 1 226 ? 1.312   -24.154 12.091  0.80 40.03  ? 206 PRO A CB  1 
ATOM   1633 C CG  . PRO A 1 226 ? 0.470   -25.018 11.163  1.00 38.48  ? 206 PRO A CG  1 
ATOM   1634 C CD  . PRO A 1 226 ? -0.817  -24.239 10.953  1.00 37.77  ? 206 PRO A CD  1 
ATOM   1635 N N   . VAL A 1 227 ? 2.570   -21.090 11.004  1.00 34.86  ? 207 VAL A N   1 
ATOM   1636 C CA  . VAL A 1 227 ? 3.516   -20.519 10.065  1.00 33.15  ? 207 VAL A CA  1 
ATOM   1637 C C   . VAL A 1 227 ? 4.881   -20.549 10.744  1.00 34.64  ? 207 VAL A C   1 
ATOM   1638 O O   . VAL A 1 227 ? 5.029   -20.026 11.846  1.00 35.08  ? 207 VAL A O   1 
ATOM   1639 C CB  . VAL A 1 227 ? 3.119   -19.091 9.649   1.00 33.98  ? 207 VAL A CB  1 
ATOM   1640 C CG1 . VAL A 1 227 ? 4.017   -18.537 8.551   1.00 37.42  ? 207 VAL A CG1 1 
ATOM   1641 C CG2 . VAL A 1 227 ? 1.666   -18.998 9.214   1.00 38.27  ? 207 VAL A CG2 1 
ATOM   1642 N N   . PRO A 1 228 ? 5.902   -21.190 10.135  1.00 35.48  ? 208 PRO A N   1 
ATOM   1643 C CA  . PRO A 1 228 ? 7.243   -21.197 10.724  1.00 33.44  ? 208 PRO A CA  1 
ATOM   1644 C C   . PRO A 1 228 ? 7.807   -19.776 10.743  1.00 34.66  ? 208 PRO A C   1 
ATOM   1645 O O   . PRO A 1 228 ? 7.334   -18.907 10.010  1.00 35.32  ? 208 PRO A O   1 
ATOM   1646 C CB  . PRO A 1 228 ? 8.047   -22.158 9.853   1.00 39.42  ? 208 PRO A CB  1 
ATOM   1647 C CG  . PRO A 1 228 ? 7.252   -22.294 8.552   1.00 39.77  ? 208 PRO A CG  1 
ATOM   1648 C CD  . PRO A 1 228 ? 5.824   -21.894 8.846   1.00 36.30  ? 208 PRO A CD  1 
ATOM   1649 N N   . LEU A 1 229 ? 8.787   -19.574 11.610  1.00 32.76  ? 209 LEU A N   1 
ATOM   1650 C CA  . LEU A 1 229 ? 9.377   -18.225 11.800  1.00 31.73  ? 209 LEU A CA  1 
ATOM   1651 C C   . LEU A 1 229 ? 9.841   -17.595 10.488  1.00 31.85  ? 209 LEU A C   1 
ATOM   1652 O O   . LEU A 1 229 ? 9.629   -16.386 10.347  1.00 33.46  ? 209 LEU A O   1 
ATOM   1653 C CB  . LEU A 1 229 ? 10.553  -18.398 12.752  1.00 33.81  ? 209 LEU A CB  1 
ATOM   1654 C CG  . LEU A 1 229 ? 10.250  -18.952 14.146  1.00 38.37  ? 209 LEU A CG  1 
ATOM   1655 C CD1 . LEU A 1 229 ? 11.546  -19.089 14.924  0.80 37.62  ? 209 LEU A CD1 1 
ATOM   1656 C CD2 . LEU A 1 229 ? 9.266   -18.089 14.905  1.00 36.75  ? 209 LEU A CD2 1 
ATOM   1657 N N   . GLU A 1 230 ? 10.429  -18.350 9.572   1.00 32.97  ? 210 GLU A N   1 
ATOM   1658 C CA  . GLU A 1 230 ? 11.047  -17.784 8.373   1.00 33.70  ? 210 GLU A CA  1 
ATOM   1659 C C   . GLU A 1 230 ? 10.022  -17.415 7.303   1.00 35.81  ? 210 GLU A C   1 
ATOM   1660 O O   . GLU A 1 230 ? 10.360  -16.744 6.323   1.00 35.43  ? 210 GLU A O   1 
ATOM   1661 C CB  . GLU A 1 230 ? 12.024  -18.768 7.726   1.00 36.66  ? 210 GLU A CB  1 
ATOM   1662 C CG  . GLU A 1 230 ? 13.183  -19.124 8.619   1.00 40.87  ? 210 GLU A CG  1 
ATOM   1663 C CD  . GLU A 1 230 ? 12.920  -20.152 9.708   1.00 45.22  ? 210 GLU A CD  1 
ATOM   1664 O OE1 . GLU A 1 230 ? 13.860  -20.371 10.512  1.00 49.10  ? 210 GLU A OE1 1 
ATOM   1665 O OE2 . GLU A 1 230 ? 11.794  -20.755 9.750   1.00 42.35  ? 210 GLU A OE2 1 
ATOM   1666 N N   . ALA A 1 231 ? 8.777   -17.852 7.502   1.00 36.64  ? 211 ALA A N   1 
ATOM   1667 C CA  . ALA A 1 231 ? 7.727   -17.654 6.518   1.00 39.05  ? 211 ALA A CA  1 
ATOM   1668 C C   . ALA A 1 231 ? 6.809   -16.499 6.916   1.00 35.71  ? 211 ALA A C   1 
ATOM   1669 O O   . ALA A 1 231 ? 5.963   -16.102 6.117   1.00 38.75  ? 211 ALA A O   1 
ATOM   1670 C CB  . ALA A 1 231 ? 6.940   -18.920 6.344   1.00 40.85  ? 211 ALA A CB  1 
ATOM   1671 N N   . ARG A 1 232 ? 6.981   -15.977 8.135   1.00 33.72  ? 212 ARG A N   1 
ATOM   1672 C CA  . ARG A 1 232 ? 6.132   -14.911 8.638   1.00 33.04  ? 212 ARG A CA  1 
ATOM   1673 C C   . ARG A 1 232 ? 6.261   -13.673 7.745   1.00 33.43  ? 212 ARG A C   1 
ATOM   1674 O O   . ARG A 1 232 ? 7.361   -13.225 7.398   1.00 38.16  ? 212 ARG A O   1 
ATOM   1675 C CB  . ARG A 1 232 ? 6.400   -14.599 10.116  1.00 33.30  ? 212 ARG A CB  1 
ATOM   1676 C CG  . ARG A 1 232 ? 6.328   -15.829 10.997  1.00 35.83  ? 212 ARG A CG  1 
ATOM   1677 C CD  . ARG A 1 232 ? 5.593   -15.756 12.307  1.00 38.66  ? 212 ARG A CD  1 
ATOM   1678 N NE  . ARG A 1 232 ? 5.527   -17.101 12.878  1.00 41.56  ? 212 ARG A NE  1 
ATOM   1679 C CZ  . ARG A 1 232 ? 5.730   -17.402 14.159  1.00 43.10  ? 212 ARG A CZ  1 
ATOM   1680 N NH1 . ARG A 1 232 ? 5.876   -16.432 15.045  1.00 46.11  ? 212 ARG A NH1 1 
ATOM   1681 N NH2 . ARG A 1 232 ? 5.737   -18.670 14.557  1.00 42.04  ? 212 ARG A NH2 1 
ATOM   1682 N N   . ARG A 1 233 ? 5.097   -13.153 7.362   1.00 24.68  ? 213 ARG A N   1 
ATOM   1683 C CA  . ARG A 1 233 ? 5.003   -11.957 6.555   1.00 24.20  ? 213 ARG A CA  1 
ATOM   1684 C C   . ARG A 1 233 ? 3.929   -11.064 7.149   1.00 22.60  ? 213 ARG A C   1 
ATOM   1685 O O   . ARG A 1 233 ? 2.820   -11.505 7.384   1.00 23.67  ? 213 ARG A O   1 
ATOM   1686 C CB  . ARG A 1 233 ? 4.630   -12.324 5.121   1.00 25.67  ? 213 ARG A CB  1 
ATOM   1687 C CG  . ARG A 1 233 ? 4.418   -11.132 4.216   1.00 27.82  ? 213 ARG A CG  1 
ATOM   1688 C CD  . ARG A 1 233 ? 4.384   -11.545 2.763   1.00 30.05  ? 213 ARG A CD  1 
ATOM   1689 N NE  . ARG A 1 233 ? 3.988   -10.459 1.877   1.00 30.39  ? 213 ARG A NE  1 
ATOM   1690 C CZ  . ARG A 1 233 ? 4.079   -10.507 0.552   1.00 29.35  ? 213 ARG A CZ  1 
ATOM   1691 N NH1 . ARG A 1 233 ? 4.347   -11.651 -0.045  1.00 30.32  ? 213 ARG A NH1 1 
ATOM   1692 N NH2 . ARG A 1 233 ? 3.855   -9.424  -0.174  1.00 29.61  ? 213 ARG A NH2 1 
ATOM   1693 N N   . THR A 1 234 ? 4.250   -9.775  7.328   1.00 21.74  ? 214 THR A N   1 
ATOM   1694 C CA  . THR A 1 234 ? 3.290   -8.799  7.823   1.00 20.70  ? 214 THR A CA  1 
ATOM   1695 C C   . THR A 1 234 ? 2.576   -8.088  6.664   1.00 19.15  ? 214 THR A C   1 
ATOM   1696 O O   . THR A 1 234 ? 3.223   -7.692  5.697   1.00 21.19  ? 214 THR A O   1 
ATOM   1697 C CB  . THR A 1 234 ? 3.997   -7.772  8.707   1.00 20.88  ? 214 THR A CB  1 
ATOM   1698 O OG1 . THR A 1 234 ? 4.816   -8.353  9.733   1.00 20.15  ? 214 THR A OG1 1 
ATOM   1699 C CG2 . THR A 1 234 ? 2.989   -6.826  9.320   1.00 20.20  ? 214 THR A CG2 1 
ATOM   1700 N N   . ARG A 1 235 ? 1.256   -7.931  6.808   1.00 19.50  ? 215 ARG A N   1 
ATOM   1701 C CA  . ARG A 1 235 ? 0.433   -7.137  5.913   1.00 20.76  ? 215 ARG A CA  1 
ATOM   1702 C C   . ARG A 1 235 ? -0.340  -6.085  6.711   1.00 20.96  ? 215 ARG A C   1 
ATOM   1703 O O   . ARG A 1 235 ? -0.406  -6.154  7.942   1.00 18.34  ? 215 ARG A O   1 
ATOM   1704 C CB  . ARG A 1 235 ? -0.533  -8.014  5.122   1.00 24.25  ? 215 ARG A CB  1 
ATOM   1705 C CG  . ARG A 1 235 ? 0.164   -8.968  4.158   1.00 24.91  ? 215 ARG A CG  1 
ATOM   1706 C CD  . ARG A 1 235 ? -0.843  -9.793  3.378   1.00 28.20  ? 215 ARG A CD  1 
ATOM   1707 N NE  . ARG A 1 235 ? -0.201  -10.696 2.417   1.00 29.83  ? 215 ARG A NE  1 
ATOM   1708 C CZ  . ARG A 1 235 ? 0.286   -10.350 1.217   1.00 31.85  ? 215 ARG A CZ  1 
ATOM   1709 N NH1 . ARG A 1 235 ? 0.147   -9.123  0.739   1.00 31.45  ? 215 ARG A NH1 1 
ATOM   1710 N NH2 . ARG A 1 235 ? 0.907   -11.250 0.479   1.00 32.49  ? 215 ARG A NH2 1 
ATOM   1711 N N   . LEU A 1 236 ? -0.908  -5.120  5.977   1.00 20.03  ? 216 LEU A N   1 
ATOM   1712 C CA  . LEU A 1 236 ? -1.538  -3.928  6.550   1.00 18.53  ? 216 LEU A CA  1 
ATOM   1713 C C   . LEU A 1 236 ? -2.968  -3.752  6.059   1.00 18.63  ? 216 LEU A C   1 
ATOM   1714 O O   . LEU A 1 236 ? -3.216  -3.908  4.863   1.00 21.45  ? 216 LEU A O   1 
ATOM   1715 C CB  . LEU A 1 236 ? -0.744  -2.692  6.129   1.00 18.18  ? 216 LEU A CB  1 
ATOM   1716 C CG  . LEU A 1 236 ? -1.461  -1.357  6.303   1.00 19.64  ? 216 LEU A CG  1 
ATOM   1717 C CD1 . LEU A 1 236 ? -1.609  -0.987  7.775   1.00 18.89  ? 216 LEU A CD1 1 
ATOM   1718 C CD2 . LEU A 1 236 ? -0.705  -0.262  5.573   1.00 21.17  ? 216 LEU A CD2 1 
ATOM   1719 N N   . LEU A 1 237 ? -3.869  -3.417  7.000   1.00 18.13  ? 217 LEU A N   1 
ATOM   1720 C CA  . LEU A 1 237 ? -5.205  -2.893  6.731   1.00 20.02  ? 217 LEU A CA  1 
ATOM   1721 C C   . LEU A 1 237 ? -5.297  -1.520  7.375   1.00 19.43  ? 217 LEU A C   1 
ATOM   1722 O O   . LEU A 1 237 ? -5.036  -1.373  8.564   1.00 21.16  ? 217 LEU A O   1 
ATOM   1723 C CB  . LEU A 1 237 ? -6.313  -3.767  7.336   1.00 23.27  ? 217 LEU A CB  1 
ATOM   1724 C CG  . LEU A 1 237 ? -6.376  -5.224  6.925   1.00 26.50  ? 217 LEU A CG  1 
ATOM   1725 C CD1 . LEU A 1 237 ? -7.572  -5.861  7.626   1.00 24.59  ? 217 LEU A CD1 1 
ATOM   1726 C CD2 . LEU A 1 237 ? -6.477  -5.347  5.410   1.00 30.80  ? 217 LEU A CD2 1 
ATOM   1727 N N   . HIS A 1 238 ? -5.727  -0.547  6.584   1.00 19.88  ? 218 HIS A N   1 
ATOM   1728 C CA  . HIS A 1 238 ? -5.795  0.825   7.050   1.00 18.86  ? 218 HIS A CA  1 
ATOM   1729 C C   . HIS A 1 238 ? -7.231  1.192   7.424   1.00 18.59  ? 218 HIS A C   1 
ATOM   1730 O O   . HIS A 1 238 ? -8.175  0.930   6.661   1.00 19.69  ? 218 HIS A O   1 
ATOM   1731 C CB  . HIS A 1 238 ? -5.321  1.713   5.901   1.00 18.55  ? 218 HIS A CB  1 
ATOM   1732 C CG  . HIS A 1 238 ? -5.535  3.167   6.145   1.00 19.72  ? 218 HIS A CG  1 
ATOM   1733 N ND1 . HIS A 1 238 ? -4.856  3.896   7.077   1.00 20.28  ? 218 HIS A ND1 1 
ATOM   1734 C CD2 . HIS A 1 238 ? -6.463  3.960   5.607   1.00 19.95  ? 218 HIS A CD2 1 
ATOM   1735 C CE1 . HIS A 1 238 ? -5.359  5.140   7.048   1.00 19.29  ? 218 HIS A CE1 1 
ATOM   1736 N NE2 . HIS A 1 238 ? -6.337  5.189   6.172   1.00 20.78  ? 218 HIS A NE2 1 
ATOM   1737 N N   . ARG A 1 239 ? -7.354  1.910   8.553   1.00 20.16  ? 219 ARG A N   1 
ATOM   1738 C CA  . ARG A 1 239 ? -8.595  2.544   8.969   1.00 19.28  ? 219 ARG A CA  1 
ATOM   1739 C C   . ARG A 1 239 ? -8.267  3.942   9.509   1.00 18.89  ? 219 ARG A C   1 
ATOM   1740 O O   . ARG A 1 239 ? -7.109  4.232   9.796   1.00 18.41  ? 219 ARG A O   1 
ATOM   1741 C CB  . ARG A 1 239 ? -9.305  1.697   10.023  1.00 21.09  ? 219 ARG A CB  1 
ATOM   1742 C CG  . ARG A 1 239 ? -9.770  0.337   9.523   1.00 20.39  ? 219 ARG A CG  1 
ATOM   1743 C CD  . ARG A 1 239 ? -10.897 0.417   8.513   1.00 22.11  ? 219 ARG A CD  1 
ATOM   1744 N NE  . ARG A 1 239 ? -11.453 -0.879  8.165   1.00 24.75  ? 219 ARG A NE  1 
ATOM   1745 C CZ  . ARG A 1 239 ? -10.955 -1.707  7.268   1.00 25.87  ? 219 ARG A CZ  1 
ATOM   1746 N NH1 . ARG A 1 239 ? -9.821  -1.460  6.640   1.00 26.51  ? 219 ARG A NH1 1 
ATOM   1747 N NH2 . ARG A 1 239 ? -11.593 -2.836  7.040   1.00 27.18  ? 219 ARG A NH2 1 
ATOM   1748 N N   . GLU A 1 240 ? -9.315  4.761   9.657   1.00 19.57  ? 220 GLU A N   1 
ATOM   1749 C CA  . GLU A 1 240 ? -9.145  6.101   10.210  1.00 20.08  ? 220 GLU A CA  1 
ATOM   1750 C C   . GLU A 1 240 ? -10.478 6.637   10.738  1.00 21.05  ? 220 GLU A C   1 
ATOM   1751 O O   . GLU A 1 240 ? -11.549 6.191   10.347  1.00 22.47  ? 220 GLU A O   1 
ATOM   1752 C CB  . GLU A 1 240 ? -8.511  7.035   9.179   1.00 25.04  ? 220 GLU A CB  1 
ATOM   1753 C CG  . GLU A 1 240 ? -9.224  7.143   7.857   1.00 25.70  ? 220 GLU A CG  1 
ATOM   1754 C CD  . GLU A 1 240 ? -8.483  8.013   6.842   1.00 27.21  ? 220 GLU A CD  1 
ATOM   1755 O OE1 . GLU A 1 240 ? -7.512  7.557   6.209   1.00 29.11  ? 220 GLU A OE1 1 
ATOM   1756 O OE2 . GLU A 1 240 ? -8.845  9.169   6.722   1.00 31.17  ? 220 GLU A OE2 1 
ATOM   1757 N N   . LEU A 1 241 ? -10.377 7.663   11.604  1.00 20.86  ? 221 LEU A N   1 
ATOM   1758 C CA  . LEU A 1 241 ? -11.508 8.455   12.085  1.00 21.70  ? 221 LEU A CA  1 
ATOM   1759 C C   . LEU A 1 241 ? -11.291 9.879   11.593  1.00 20.86  ? 221 LEU A C   1 
ATOM   1760 O O   . LEU A 1 241 ? -10.153 10.305  11.549  1.00 20.54  ? 221 LEU A O   1 
ATOM   1761 C CB  . LEU A 1 241 ? -11.544 8.511   13.616  1.00 23.29  ? 221 LEU A CB  1 
ATOM   1762 C CG  . LEU A 1 241 ? -11.622 7.189   14.367  1.00 27.91  ? 221 LEU A CG  1 
ATOM   1763 C CD1 . LEU A 1 241 ? -11.651 7.438   15.877  1.00 31.14  ? 221 LEU A CD1 1 
ATOM   1764 C CD2 . LEU A 1 241 ? -12.848 6.419   13.932  1.00 31.19  ? 221 LEU A CD2 1 
ATOM   1765 N N   . ASP A 1 242 ? -12.396 10.566  11.350  1.00 21.14  ? 222 ASP A N   1 
ATOM   1766 C CA  . ASP A 1 242 ? -12.288 11.990  10.969  1.00 21.88  ? 222 ASP A CA  1 
ATOM   1767 C C   . ASP A 1 242 ? -12.215 12.838  12.235  1.00 21.59  ? 222 ASP A C   1 
ATOM   1768 O O   . ASP A 1 242 ? -12.352 12.299  13.331  1.00 21.50  ? 222 ASP A O   1 
ATOM   1769 C CB  . ASP A 1 242 ? -13.401 12.436  10.020  1.00 25.71  ? 222 ASP A CB  1 
ATOM   1770 C CG  . ASP A 1 242 ? -14.804 12.435  10.596  1.00 28.36  ? 222 ASP A CG  1 
ATOM   1771 O OD1 . ASP A 1 242 ? -14.949 12.577  11.812  1.00 28.42  ? 222 ASP A OD1 1 
ATOM   1772 O OD2 . ASP A 1 242 ? -15.743 12.307  9.800   1.00 38.42  ? 222 ASP A OD2 1 
ATOM   1773 N N   . GLY A 1 243 ? -12.057 14.148  12.040  1.00 22.08  ? 223 GLY A N   1 
ATOM   1774 C CA  . GLY A 1 243 ? -11.869 15.051  13.155  1.00 22.10  ? 223 GLY A CA  1 
ATOM   1775 C C   . GLY A 1 243 ? -13.082 15.101  14.079  1.00 22.20  ? 223 GLY A C   1 
ATOM   1776 O O   . GLY A 1 243 ? -12.923 15.187  15.297  1.00 22.76  ? 223 GLY A O   1 
ATOM   1777 N N   . ALA A 1 244 ? -14.283 15.030  13.504  1.00 23.78  ? 224 ALA A N   1 
ATOM   1778 C CA  . ALA A 1 244 ? -15.498 15.109  14.301  1.00 22.80  ? 224 ALA A CA  1 
ATOM   1779 C C   . ALA A 1 244 ? -15.659 13.848  15.147  1.00 22.55  ? 224 ALA A C   1 
ATOM   1780 O O   . ALA A 1 244 ? -16.032 13.923  16.302  1.00 23.21  ? 224 ALA A O   1 
ATOM   1781 C CB  . ALA A 1 244 ? -16.696 15.343  13.417  1.00 25.98  ? 224 ALA A CB  1 
ATOM   1782 N N   . GLN A 1 245 ? -15.346 12.689  14.561  1.00 22.18  ? 225 GLN A N   1 
ATOM   1783 C CA  . GLN A 1 245 ? -15.402 11.446  15.315  1.00 22.33  ? 225 GLN A CA  1 
ATOM   1784 C C   . GLN A 1 245 ? -14.362 11.458  16.437  1.00 20.58  ? 225 GLN A C   1 
ATOM   1785 O O   . GLN A 1 245 ? -14.647 11.043  17.565  1.00 20.70  ? 225 GLN A O   1 
ATOM   1786 C CB  . GLN A 1 245 ? -15.128 10.249  14.401  1.00 22.54  ? 225 GLN A CB  1 
ATOM   1787 C CG  . GLN A 1 245 ? -16.238 9.958   13.411  1.00 25.04  ? 225 GLN A CG  1 
ATOM   1788 C CD  . GLN A 1 245 ? -15.863 9.016   12.295  1.00 25.54  ? 225 GLN A CD  1 
ATOM   1789 O OE1 . GLN A 1 245 ? -14.720 8.982   11.814  1.00 26.19  ? 225 GLN A OE1 1 
ATOM   1790 N NE2 . GLN A 1 245 ? -16.857 8.266   11.853  1.00 29.03  ? 225 GLN A NE2 1 
ATOM   1791 N N   . LEU A 1 246 ? -13.141 11.921  16.134  1.00 20.27  ? 226 LEU A N   1 
ATOM   1792 C CA  . LEU A 1 246 ? -12.111 12.030  17.159  1.00 20.02  ? 226 LEU A CA  1 
ATOM   1793 C C   . LEU A 1 246 ? -12.536 12.972  18.292  1.00 19.91  ? 226 LEU A C   1 
ATOM   1794 O O   . LEU A 1 246 ? -12.286 12.720  19.466  1.00 19.84  ? 226 LEU A O   1 
ATOM   1795 C CB  . LEU A 1 246 ? -10.796 12.508  16.531  1.00 21.21  ? 226 LEU A CB  1 
ATOM   1796 C CG  . LEU A 1 246 ? -9.630  12.654  17.502  1.00 20.67  ? 226 LEU A CG  1 
ATOM   1797 C CD1 . LEU A 1 246 ? -9.359  11.361  18.271  1.00 22.80  ? 226 LEU A CD1 1 
ATOM   1798 C CD2 . LEU A 1 246 ? -8.368  13.112  16.782  1.00 21.49  ? 226 LEU A CD2 1 
ATOM   1799 N N   . GLU A 1 247 ? -13.068 14.139  17.939  1.00 22.27  ? 227 GLU A N   1 
ATOM   1800 C CA  . GLU A 1 247 ? -13.489 15.072  18.965  1.00 24.93  ? 227 GLU A CA  1 
ATOM   1801 C C   . GLU A 1 247 ? -14.516 14.428  19.899  1.00 23.60  ? 227 GLU A C   1 
ATOM   1802 O O   . GLU A 1 247 ? -14.435 14.567  21.121  1.00 23.68  ? 227 GLU A O   1 
ATOM   1803 C CB  . GLU A 1 247 ? -14.035 16.347  18.317  1.00 26.92  ? 227 GLU A CB  1 
ATOM   1804 C CG  . GLU A 1 247 ? -14.443 17.418  19.314  1.00 33.05  ? 227 GLU A CG  1 
ATOM   1805 C CD  . GLU A 1 247 ? -14.850 18.710  18.621  1.00 40.68  ? 227 GLU A CD  1 
ATOM   1806 O OE1 . GLU A 1 247 ? -13.941 19.467  18.157  0.70 49.27  ? 227 GLU A OE1 1 
ATOM   1807 O OE2 . GLU A 1 247 ? -16.066 18.963  18.512  0.30 43.67  ? 227 GLU A OE2 1 
ATOM   1808 N N   . GLN A 1 248 ? -15.485 13.720  19.332  1.00 21.85  ? 228 GLN A N   1 
ATOM   1809 C CA  . GLN A 1 248 ? -16.550 13.109  20.165  1.00 23.50  ? 228 GLN A CA  1 
ATOM   1810 C C   . GLN A 1 248 ? -15.947 11.975  21.011  1.00 24.23  ? 228 GLN A C   1 
ATOM   1811 O O   . GLN A 1 248 ? -16.336 11.823  22.169  1.00 22.98  ? 228 GLN A O   1 
ATOM   1812 C CB  . GLN A 1 248 ? -17.685 12.631  19.271  1.00 26.55  ? 228 GLN A CB  1 
ATOM   1813 C CG  . GLN A 1 248 ? -18.814 11.973  20.058  0.70 30.44  ? 228 GLN A CG  1 
ATOM   1814 C CD  . GLN A 1 248 ? -20.196 12.402  19.621  0.70 36.81  ? 228 GLN A CD  1 
ATOM   1815 O OE1 . GLN A 1 248 ? -20.438 13.571  19.300  0.50 45.86  ? 228 GLN A OE1 1 
ATOM   1816 N NE2 . GLN A 1 248 ? -21.121 11.454  19.612  0.70 35.68  ? 228 GLN A NE2 1 
ATOM   1817 N N   . LEU A 1 249 ? -15.014 11.234  20.423  1.00 21.33  ? 229 LEU A N   1 
ATOM   1818 C CA  . LEU A 1 249 ? -14.347 10.194  21.184  1.00 22.36  ? 229 LEU A CA  1 
ATOM   1819 C C   . LEU A 1 249 ? -13.623 10.783  22.390  1.00 21.19  ? 229 LEU A C   1 
ATOM   1820 O O   . LEU A 1 249 ? -13.715 10.265  23.494  1.00 21.67  ? 229 LEU A O   1 
ATOM   1821 C CB  . LEU A 1 249 ? -13.392 9.415   20.280  1.00 21.29  ? 229 LEU A CB  1 
ATOM   1822 C CG  . LEU A 1 249 ? -12.560 8.338   20.954  1.00 23.66  ? 229 LEU A CG  1 
ATOM   1823 C CD1 . LEU A 1 249 ? -13.461 7.257   21.531  1.00 26.17  ? 229 LEU A CD1 1 
ATOM   1824 C CD2 . LEU A 1 249 ? -11.580 7.774   19.945  1.00 23.52  ? 229 LEU A CD2 1 
ATOM   1825 N N   . GLN A 1 250 ? -12.863 11.846  22.159  1.00 21.83  ? 230 GLN A N   1 
ATOM   1826 C CA  . GLN A 1 250 ? -12.123 12.465  23.232  1.00 23.11  ? 230 GLN A CA  1 
ATOM   1827 C C   . GLN A 1 250 ? -13.077 12.938  24.327  1.00 22.75  ? 230 GLN A C   1 
ATOM   1828 O O   . GLN A 1 250 ? -12.779 12.764  25.510  1.00 22.76  ? 230 GLN A O   1 
ATOM   1829 C CB  . GLN A 1 250 ? -11.345 13.670  22.714  1.00 24.28  ? 230 GLN A CB  1 
ATOM   1830 C CG  . GLN A 1 250 ? -10.183 13.308  21.819  1.00 29.57  ? 230 GLN A CG  1 
ATOM   1831 C CD  . GLN A 1 250 ? -9.490  14.548  21.307  1.00 37.75  ? 230 GLN A CD  1 
ATOM   1832 O OE1 . GLN A 1 250 ? -10.062 15.364  20.585  1.00 43.34  ? 230 GLN A OE1 1 
ATOM   1833 N NE2 . GLN A 1 250 ? -8.246  14.712  21.713  1.00 47.31  ? 230 GLN A NE2 1 
ATOM   1834 N N   . ARG A 1 251 ? -14.189 13.564  23.930  1.00 22.49  ? 231 ARG A N   1 
ATOM   1835 C CA  . ARG A 1 251 ? -15.165 14.058  24.891  1.00 23.73  ? 231 ARG A CA  1 
ATOM   1836 C C   . ARG A 1 251 ? -15.719 12.906  25.732  1.00 23.46  ? 231 ARG A C   1 
ATOM   1837 O O   . ARG A 1 251 ? -15.718 12.956  26.960  1.00 24.31  ? 231 ARG A O   1 
ATOM   1838 C CB  . ARG A 1 251 ? -16.300 14.856  24.230  1.00 26.35  ? 231 ARG A CB  1 
ATOM   1839 C CG  . ARG A 1 251 ? -17.335 15.361  25.235  1.00 32.18  ? 231 ARG A CG  1 
ATOM   1840 C CD  . ARG A 1 251 ? -18.384 16.332  24.705  1.00 39.27  ? 231 ARG A CD  1 
ATOM   1841 N NE  . ARG A 1 251 ? -19.075 15.793  23.538  1.00 44.13  ? 231 ARG A NE  1 
ATOM   1842 C CZ  . ARG A 1 251 ? -18.767 16.090  22.273  1.00 52.73  ? 231 ARG A CZ  1 
ATOM   1843 N NH1 . ARG A 1 251 ? -17.822 16.981  21.994  1.00 55.87  ? 231 ARG A NH1 1 
ATOM   1844 N NH2 . ARG A 1 251 ? -19.407 15.483  21.285  0.70 52.11  ? 231 ARG A NH2 1 
ATOM   1845 N N   . ARG A 1 252 ? -16.163 11.851  25.069  1.00 23.14  ? 232 ARG A N   1 
ATOM   1846 C CA  . ARG A 1 252 ? -16.767 10.736  25.786  1.00 24.75  ? 232 ARG A CA  1 
ATOM   1847 C C   . ARG A 1 252 ? -15.734 10.042  26.676  1.00 22.63  ? 232 ARG A C   1 
ATOM   1848 O O   . ARG A 1 252 ? -16.064 9.585   27.763  1.00 23.37  ? 232 ARG A O   1 
ATOM   1849 C CB  . ARG A 1 252 ? -17.370 9.737   24.794  1.00 26.86  ? 232 ARG A CB  1 
ATOM   1850 C CG  . ARG A 1 252 ? -18.656 10.205  24.120  1.00 33.23  ? 232 ARG A CG  1 
ATOM   1851 C CD  . ARG A 1 252 ? -19.861 9.625   24.852  1.00 42.07  ? 232 ARG A CD  1 
ATOM   1852 N NE  . ARG A 1 252 ? -21.111 9.945   24.201  1.00 47.48  ? 232 ARG A NE  1 
ATOM   1853 C CZ  . ARG A 1 252 ? -21.935 9.080   23.614  1.00 44.75  ? 232 ARG A CZ  1 
ATOM   1854 N NH1 . ARG A 1 252 ? -22.960 9.548   22.934  1.00 52.44  ? 232 ARG A NH1 1 
ATOM   1855 N NH2 . ARG A 1 252 ? -21.744 7.771   23.679  0.60 37.79  ? 232 ARG A NH2 1 
ATOM   1856 N N   . ALA A 1 253 ? -14.488 9.943   26.201  1.00 20.78  ? 233 ALA A N   1 
ATOM   1857 C CA  . ALA A 1 253 ? -13.446 9.304   26.991  1.00 21.35  ? 233 ALA A CA  1 
ATOM   1858 C C   . ALA A 1 253 ? -13.237 10.070  28.290  1.00 21.64  ? 233 ALA A C   1 
ATOM   1859 O O   . ALA A 1 253 ? -13.202 9.499   29.379  1.00 21.79  ? 233 ALA A O   1 
ATOM   1860 C CB  . ALA A 1 253 ? -12.182 9.170   26.218  1.00 22.52  ? 233 ALA A CB  1 
ATOM   1861 N N   . ARG A 1 254 ? -13.122 11.392  28.214  1.00 23.50  ? 234 ARG A N   1 
ATOM   1862 C CA  . ARG A 1 254 ? -12.862 12.100  29.453  1.00 26.44  ? 234 ARG A CA  1 
ATOM   1863 C C   . ARG A 1 254 ? -14.097 12.071  30.363  1.00 25.12  ? 234 ARG A C   1 
ATOM   1864 O O   . ARG A 1 254 ? -13.939 12.083  31.580  1.00 25.73  ? 234 ARG A O   1 
ATOM   1865 C CB  . ARG A 1 254 ? -12.327 13.517  29.216  1.00 28.94  ? 234 ARG A CB  1 
ATOM   1866 C CG  . ARG A 1 254 ? -13.319 14.516  28.666  1.00 33.19  ? 234 ARG A CG  1 
ATOM   1867 C CD  . ARG A 1 254 ? -12.787 15.921  28.885  1.00 36.95  ? 234 ARG A CD  1 
ATOM   1868 N NE  . ARG A 1 254 ? -13.550 16.860  28.086  1.00 37.84  ? 234 ARG A NE  1 
ATOM   1869 C CZ  . ARG A 1 254 ? -14.823 17.171  28.279  1.00 35.01  ? 234 ARG A CZ  1 
ATOM   1870 N NH1 . ARG A 1 254 ? -15.452 16.769  29.372  1.00 38.70  ? 234 ARG A NH1 1 
ATOM   1871 N NH2 . ARG A 1 254 ? -15.440 17.933  27.388  1.00 38.63  ? 234 ARG A NH2 1 
ATOM   1872 N N   . GLU A 1 255 ? -15.313 12.039  29.797  1.00 23.40  ? 235 GLU A N   1 
ATOM   1873 C CA  . GLU A 1 255 ? -16.520 11.958  30.605  1.00 24.80  ? 235 GLU A CA  1 
ATOM   1874 C C   . GLU A 1 255 ? -16.562 10.632  31.373  1.00 24.32  ? 235 GLU A C   1 
ATOM   1875 O O   . GLU A 1 255 ? -17.175 10.560  32.437  1.00 27.09  ? 235 GLU A O   1 
ATOM   1876 C CB  . GLU A 1 255 ? -17.749 12.137  29.713  1.00 24.32  ? 235 GLU A CB  1 
ATOM   1877 C CG  . GLU A 1 255 ? -17.891 13.571  29.220  1.00 25.76  ? 235 GLU A CG  1 
ATOM   1878 C CD  . GLU A 1 255 ? -18.993 13.802  28.203  1.00 29.16  ? 235 GLU A CD  1 
ATOM   1879 O OE1 . GLU A 1 255 ? -19.542 12.814  27.702  1.00 31.03  ? 235 GLU A OE1 1 
ATOM   1880 O OE2 . GLU A 1 255 ? -19.346 14.984  27.966  1.00 32.62  ? 235 GLU A OE2 1 
ATOM   1881 N N   . HIS A 1 256 ? -15.917 9.593   30.831  1.00 23.28  ? 236 HIS A N   1 
ATOM   1882 C CA  . HIS A 1 256 ? -15.855 8.285   31.485  1.00 24.67  ? 236 HIS A CA  1 
ATOM   1883 C C   . HIS A 1 256 ? -14.522 8.018   32.194  1.00 25.25  ? 236 HIS A C   1 
ATOM   1884 O O   . HIS A 1 256 ? -14.177 6.867   32.526  1.00 26.68  ? 236 HIS A O   1 
ATOM   1885 C CB  . HIS A 1 256 ? -16.119 7.183   30.461  1.00 25.41  ? 236 HIS A CB  1 
ATOM   1886 C CG  . HIS A 1 256 ? -17.543 7.124   30.024  1.00 25.60  ? 236 HIS A CG  1 
ATOM   1887 N ND1 . HIS A 1 256 ? -17.997 7.808   28.917  1.00 27.99  ? 236 HIS A ND1 1 
ATOM   1888 C CD2 . HIS A 1 256 ? -18.590 6.424   30.499  1.00 26.24  ? 236 HIS A CD2 1 
ATOM   1889 C CE1 . HIS A 1 256 ? -19.302 7.554   28.759  1.00 29.26  ? 236 HIS A CE1 1 
ATOM   1890 N NE2 . HIS A 1 256 ? -19.686 6.723   29.723  1.00 29.10  ? 236 HIS A NE2 1 
ATOM   1891 N N   . GLY A 1 257 ? -13.743 9.072   32.436  1.00 23.30  ? 237 GLY A N   1 
ATOM   1892 C CA  . GLY A 1 257 ? -12.536 8.929   33.227  1.00 27.95  ? 237 GLY A CA  1 
ATOM   1893 C C   . GLY A 1 257 ? -11.431 8.137   32.534  1.00 25.92  ? 237 GLY A C   1 
ATOM   1894 O O   . GLY A 1 257 ? -10.594 7.541   33.191  1.00 27.29  ? 237 GLY A O   1 
ATOM   1895 N N   . THR A 1 258 ? -11.391 8.203   31.201  1.00 26.02  ? 238 THR A N   1 
ATOM   1896 C CA  . THR A 1 258 ? -10.377 7.494   30.450  1.00 23.74  ? 238 THR A CA  1 
ATOM   1897 C C   . THR A 1 258 ? -9.918  8.350   29.287  1.00 25.04  ? 238 THR A C   1 
ATOM   1898 O O   . THR A 1 258 ? -10.141 9.576   29.250  1.00 24.94  ? 238 THR A O   1 
ATOM   1899 C CB  . THR A 1 258 ? -10.865 6.085   30.077  1.00 25.07  ? 238 THR A CB  1 
ATOM   1900 O OG1 . THR A 1 258 ? -9.796  5.353   29.457  1.00 25.42  ? 238 THR A OG1 1 
ATOM   1901 C CG2 . THR A 1 258 ? -12.080 6.101   29.163  1.00 24.94  ? 238 THR A CG2 1 
ATOM   1902 N N   . THR A 1 259 ? -9.241  7.697   28.357  1.00 23.21  ? 239 THR A N   1 
ATOM   1903 C CA  . THR A 1 259 ? -8.574  8.406   27.272  1.00 24.42  ? 239 THR A CA  1 
ATOM   1904 C C   . THR A 1 259 ? -8.895  7.739   25.940  1.00 22.94  ? 239 THR A C   1 
ATOM   1905 O O   . THR A 1 259 ? -9.416  6.635   25.910  1.00 23.80  ? 239 THR A O   1 
ATOM   1906 C CB  . THR A 1 259 ? -7.065  8.412   27.477  1.00 25.43  ? 239 THR A CB  1 
ATOM   1907 O OG1 . THR A 1 259 ? -6.615  7.045   27.420  1.00 24.51  ? 239 THR A OG1 1 
ATOM   1908 C CG2 . THR A 1 259 ? -6.662  9.059   28.780  1.00 27.55  ? 239 THR A CG2 1 
ATOM   1909 N N   . VAL A 1 260 ? -8.475  8.374   24.854  1.00 23.40  ? 240 VAL A N   1 
ATOM   1910 C CA  . VAL A 1 260 ? -8.534  7.783   23.530  1.00 21.20  ? 240 VAL A CA  1 
ATOM   1911 C C   . VAL A 1 260 ? -7.805  6.447   23.539  1.00 20.73  ? 240 VAL A C   1 
ATOM   1912 O O   . VAL A 1 260 ? -8.342  5.495   22.991  1.00 21.60  ? 240 VAL A O   1 
ATOM   1913 C CB  . VAL A 1 260 ? -7.994  8.723   22.435  1.00 22.86  ? 240 VAL A CB  1 
ATOM   1914 C CG1 . VAL A 1 260 ? -7.822  8.020   21.101  1.00 24.13  ? 240 VAL A CG1 1 
ATOM   1915 C CG2 . VAL A 1 260 ? -8.903  9.939   22.286  1.00 25.03  ? 240 VAL A CG2 1 
ATOM   1916 N N   . HIS A 1 261 ? -6.639  6.371   24.184  1.00 19.99  ? 241 HIS A N   1 
ATOM   1917 C CA  . HIS A 1 261 ? -5.913  5.098   24.219  1.00 18.88  ? 241 HIS A CA  1 
ATOM   1918 C C   . HIS A 1 261 ? -6.771  4.018   24.871  1.00 18.83  ? 241 HIS A C   1 
ATOM   1919 O O   . HIS A 1 261 ? -6.811  2.839   24.429  1.00 19.11  ? 241 HIS A O   1 
ATOM   1920 C CB  . HIS A 1 261 ? -4.576  5.194   24.958  1.00 20.75  ? 241 HIS A CB  1 
ATOM   1921 C CG  . HIS A 1 261 ? -3.807  3.901   24.845  1.00 18.88  ? 241 HIS A CG  1 
ATOM   1922 N ND1 . HIS A 1 261 ? -3.433  3.392   23.626  1.00 20.88  ? 241 HIS A ND1 1 
ATOM   1923 C CD2 . HIS A 1 261 ? -3.409  3.007   25.785  1.00 21.29  ? 241 HIS A CD2 1 
ATOM   1924 C CE1 . HIS A 1 261 ? -2.768  2.258   23.838  1.00 21.22  ? 241 HIS A CE1 1 
ATOM   1925 N NE2 . HIS A 1 261 ? -2.728  2.020   25.147  1.00 21.36  ? 241 HIS A NE2 1 
ATOM   1926 N N   . GLY A 1 262 ? -7.442  4.377   25.952  1.00 18.85  ? 242 GLY A N   1 
ATOM   1927 C CA  . GLY A 1 262 ? -8.286  3.373   26.585  1.00 20.46  ? 242 GLY A CA  1 
ATOM   1928 C C   . GLY A 1 262 ? -9.361  2.836   25.639  1.00 19.66  ? 242 GLY A C   1 
ATOM   1929 O O   . GLY A 1 262 ? -9.635  1.628   25.592  1.00 20.33  ? 242 GLY A O   1 
ATOM   1930 N N   . ALA A 1 263 ? -10.013 3.759   24.918  1.00 19.50  ? 243 ALA A N   1 
ATOM   1931 C CA  . ALA A 1 263 ? -11.094 3.420   24.004  1.00 19.90  ? 243 ALA A CA  1 
ATOM   1932 C C   . ALA A 1 263 ? -10.581 2.504   22.892  1.00 19.45  ? 243 ALA A C   1 
ATOM   1933 O O   . ALA A 1 263 ? -11.210 1.469   22.578  1.00 19.81  ? 243 ALA A O   1 
ATOM   1934 C CB  . ALA A 1 263 ? -11.752 4.685   23.472  1.00 21.17  ? 243 ALA A CB  1 
ATOM   1935 N N   . LEU A 1 264 ? -9.472  2.885   22.267  1.00 19.38  ? 244 LEU A N   1 
ATOM   1936 C CA  . LEU A 1 264 ? -8.992  2.153   21.104  1.00 19.53  ? 244 LEU A CA  1 
ATOM   1937 C C   . LEU A 1 264 ? -8.508  0.765   21.529  1.00 19.02  ? 244 LEU A C   1 
ATOM   1938 O O   . LEU A 1 264 ? -8.619  -0.193  20.775  1.00 18.12  ? 244 LEU A O   1 
ATOM   1939 C CB  . LEU A 1 264 ? -7.893  2.956   20.405  1.00 22.15  ? 244 LEU A CB  1 
ATOM   1940 C CG  . LEU A 1 264 ? -8.277  4.354   19.923  1.00 26.60  ? 244 LEU A CG  1 
ATOM   1941 C CD1 . LEU A 1 264 ? -7.078  5.048   19.307  1.00 29.45  ? 244 LEU A CD1 1 
ATOM   1942 C CD2 . LEU A 1 264 ? -9.420  4.296   18.964  1.00 25.85  ? 244 LEU A CD2 1 
ATOM   1943 N N   . THR A 1 265 ? -7.920  0.712   22.702  1.00 17.45  ? 245 THR A N   1 
ATOM   1944 C CA  . THR A 1 265 ? -7.330  -0.518  23.193  1.00 18.20  ? 245 THR A CA  1 
ATOM   1945 C C   . THR A 1 265 ? -8.457  -1.455  23.641  1.00 18.66  ? 245 THR A C   1 
ATOM   1946 O O   . THR A 1 265 ? -8.416  -2.687  23.373  1.00 18.84  ? 245 THR A O   1 
ATOM   1947 C CB  . THR A 1 265 ? -6.289  -0.214  24.270  1.00 19.27  ? 245 THR A CB  1 
ATOM   1948 O OG1 . THR A 1 265 ? -5.272  0.671   23.758  1.00 19.16  ? 245 THR A OG1 1 
ATOM   1949 C CG2 . THR A 1 265 ? -5.585  -1.485  24.728  1.00 20.43  ? 245 THR A CG2 1 
ATOM   1950 N N   . ALA A 1 266 ? -9.432  -0.922  24.370  1.00 19.37  ? 246 ALA A N   1 
ATOM   1951 C CA  . ALA A 1 266 ? -10.633 -1.693  24.711  1.00 18.50  ? 246 ALA A CA  1 
ATOM   1952 C C   . ALA A 1 266 ? -11.275 -2.275  23.447  1.00 18.80  ? 246 ALA A C   1 
ATOM   1953 O O   . ALA A 1 266 ? -11.662 -3.456  23.391  1.00 20.80  ? 246 ALA A O   1 
ATOM   1954 C CB  . ALA A 1 266 ? -11.634 -0.831  25.447  1.00 20.69  ? 246 ALA A CB  1 
ATOM   1955 N N   . ALA A 1 267 ? -11.438 -1.441  22.425  1.00 19.02  ? 247 ALA A N   1 
ATOM   1956 C CA  . ALA A 1 267 ? -12.089 -1.878  21.195  1.00 17.86  ? 247 ALA A CA  1 
ATOM   1957 C C   . ALA A 1 267 ? -11.354 -3.089  20.596  1.00 19.82  ? 247 ALA A C   1 
ATOM   1958 O O   . ALA A 1 267 ? -11.988 -4.060  20.145  1.00 20.50  ? 247 ALA A O   1 
ATOM   1959 C CB  . ALA A 1 267 ? -12.182 -0.719  20.209  1.00 19.06  ? 247 ALA A CB  1 
ATOM   1960 N N   . LEU A 1 268 ? -10.020 -3.021  20.571  1.00 18.30  ? 248 LEU A N   1 
ATOM   1961 C CA  . LEU A 1 268 ? -9.221  -4.100  19.992  1.00 18.36  ? 248 LEU A CA  1 
ATOM   1962 C C   . LEU A 1 268 ? -9.336  -5.356  20.860  1.00 19.97  ? 248 LEU A C   1 
ATOM   1963 O O   . LEU A 1 268 ? -9.425  -6.456  20.298  1.00 20.92  ? 248 LEU A O   1 
ATOM   1964 C CB  . LEU A 1 268 ? -7.765  -3.649  19.832  1.00 18.90  ? 248 LEU A CB  1 
ATOM   1965 C CG  . LEU A 1 268 ? -6.782  -4.692  19.307  1.00 21.64  ? 248 LEU A CG  1 
ATOM   1966 C CD1 . LEU A 1 268 ? -7.244  -5.274  17.973  1.00 22.73  ? 248 LEU A CD1 1 
ATOM   1967 C CD2 . LEU A 1 268 ? -5.387  -4.099  19.168  1.00 21.78  ? 248 LEU A CD2 1 
ATOM   1968 N N   . ALA A 1 269 ? -9.269  -5.219  22.192  1.00 19.78  ? 249 ALA A N   1 
ATOM   1969 C CA  . ALA A 1 269 ? -9.393  -6.394  23.063  1.00 20.51  ? 249 ALA A CA  1 
ATOM   1970 C C   . ALA A 1 269 ? -10.758 -7.051  22.878  1.00 20.19  ? 249 ALA A C   1 
ATOM   1971 O O   . ALA A 1 269 ? -10.877 -8.301  22.834  1.00 20.95  ? 249 ALA A O   1 
ATOM   1972 C CB  . ALA A 1 269 ? -9.174  -5.990  24.501  1.00 21.90  ? 249 ALA A CB  1 
ATOM   1973 N N   . ILE A 1 270 ? -11.803 -6.222  22.771  1.00 20.20  ? 250 ILE A N   1 
ATOM   1974 C CA  . ILE A 1 270 ? -13.160 -6.715  22.598  1.00 20.30  ? 250 ILE A CA  1 
ATOM   1975 C C   . ILE A 1 270 ? -13.269 -7.471  21.278  1.00 20.04  ? 250 ILE A C   1 
ATOM   1976 O O   . ILE A 1 270 ? -13.861 -8.567  21.231  1.00 22.10  ? 250 ILE A O   1 
ATOM   1977 C CB  . ILE A 1 270 ? -14.181 -5.577  22.740  1.00 21.73  ? 250 ILE A CB  1 
ATOM   1978 C CG1 . ILE A 1 270 ? -14.297 -5.126  24.196  1.00 21.94  ? 250 ILE A CG1 1 
ATOM   1979 C CG2 . ILE A 1 270 ? -15.536 -5.974  22.178  1.00 23.11  ? 250 ILE A CG2 1 
ATOM   1980 C CD1 . ILE A 1 270 ? -14.880 -3.727  24.355  1.00 23.08  ? 250 ILE A CD1 1 
ATOM   1981 N N   . ALA A 1 271 ? -12.694 -6.905  20.219  1.00 20.56  ? 251 ALA A N   1 
ATOM   1982 C CA  . ALA A 1 271 ? -12.655 -7.542  18.901  1.00 21.00  ? 251 ALA A CA  1 
ATOM   1983 C C   . ALA A 1 271 ? -11.923 -8.888  18.981  1.00 22.44  ? 251 ALA A C   1 
ATOM   1984 O O   . ALA A 1 271 ? -12.387 -9.859  18.390  1.00 22.35  ? 251 ALA A O   1 
ATOM   1985 C CB  . ALA A 1 271 ? -12.023 -6.602  17.898  1.00 23.40  ? 251 ALA A CB  1 
ATOM   1986 N N   . ALA A 1 272 ? -10.803 -8.938  19.696  1.00 20.97  ? 252 ALA A N   1 
ATOM   1987 C CA  . ALA A 1 272 ? -10.043 -10.177 19.829  1.00 21.79  ? 252 ALA A CA  1 
ATOM   1988 C C   . ALA A 1 272 ? -10.885 -11.202 20.582  1.00 23.00  ? 252 ALA A C   1 
ATOM   1989 O O   . ALA A 1 272 ? -10.843 -12.401 20.281  1.00 23.56  ? 252 ALA A O   1 
ATOM   1990 C CB  . ALA A 1 272 ? -8.724  -9.934  20.540  1.00 22.44  ? 252 ALA A CB  1 
ATOM   1991 N N   . GLY A 1 273 ? -11.636 -10.754 21.590  1.00 22.13  ? 253 GLY A N   1 
ATOM   1992 C CA  . GLY A 1 273 ? -12.500 -11.675 22.320  1.00 23.43  ? 253 GLY A CA  1 
ATOM   1993 C C   . GLY A 1 273 ? -13.568 -12.316 21.428  1.00 22.47  ? 253 GLY A C   1 
ATOM   1994 O O   . GLY A 1 273 ? -13.814 -13.537 21.484  1.00 25.90  ? 253 GLY A O   1 
ATOM   1995 N N   . HIS A 1 274 ? -14.200 -11.503 20.587  1.00 23.26  ? 254 HIS A N   1 
ATOM   1996 C CA  . HIS A 1 274 ? -15.240 -11.973 19.680  1.00 23.94  ? 254 HIS A CA  1 
ATOM   1997 C C   . HIS A 1 274 ? -14.684 -12.970 18.664  1.00 24.65  ? 254 HIS A C   1 
ATOM   1998 O O   . HIS A 1 274 ? -15.384 -13.920 18.299  1.00 27.39  ? 254 HIS A O   1 
ATOM   1999 C CB  . HIS A 1 274 ? -15.871 -10.803 18.915  1.00 25.48  ? 254 HIS A CB  1 
ATOM   2000 C CG  . HIS A 1 274 ? -16.736 -9.903  19.725  1.00 27.01  ? 254 HIS A CG  1 
ATOM   2001 N ND1 . HIS A 1 274 ? -17.013 -8.634  19.253  1.00 28.45  ? 254 HIS A ND1 1 
ATOM   2002 C CD2 . HIS A 1 274 ? -17.344 -10.008 20.918  1.00 28.19  ? 254 HIS A CD2 1 
ATOM   2003 C CE1 . HIS A 1 274 ? -17.773 -8.003  20.145  1.00 30.44  ? 254 HIS A CE1 1 
ATOM   2004 N NE2 . HIS A 1 274 ? -17.996 -8.818  21.169  1.00 29.38  ? 254 HIS A NE2 1 
ATOM   2005 N N   . ASP A 1 275 ? -13.420 -12.781 18.265  1.00 23.58  ? 255 ASP A N   1 
ATOM   2006 C CA  . ASP A 1 275 ? -12.756 -13.588 17.246  1.00 23.72  ? 255 ASP A CA  1 
ATOM   2007 C C   . ASP A 1 275 ? -12.240 -14.910 17.843  1.00 24.17  ? 255 ASP A C   1 
ATOM   2008 O O   . ASP A 1 275 ? -12.006 -15.890 17.116  1.00 27.07  ? 255 ASP A O   1 
ATOM   2009 C CB  . ASP A 1 275 ? -11.626 -12.762 16.612  1.00 27.16  ? 255 ASP A CB  1 
ATOM   2010 C CG  . ASP A 1 275 ? -10.658 -13.592 15.789  1.00 28.31  ? 255 ASP A CG  1 
ATOM   2011 O OD1 . ASP A 1 275 ? -11.047 -13.993 14.672  1.00 32.44  ? 255 ASP A OD1 1 
ATOM   2012 O OD2 . ASP A 1 275 ? -9.540  -13.853 16.283  1.00 31.39  ? 255 ASP A OD2 1 
ATOM   2013 N N   . HIS A 1 276 ? -12.037 -14.939 19.165  1.00 24.90  ? 256 HIS A N   1 
ATOM   2014 C CA  . HIS A 1 276 ? -11.371 -16.058 19.824  1.00 24.74  ? 256 HIS A CA  1 
ATOM   2015 C C   . HIS A 1 276 ? -12.277 -17.291 19.795  1.00 28.51  ? 256 HIS A C   1 
ATOM   2016 O O   . HIS A 1 276 ? -13.470 -17.179 20.064  1.00 30.50  ? 256 HIS A O   1 
ATOM   2017 C CB  . HIS A 1 276 ? -11.037 -15.702 21.281  1.00 24.17  ? 256 HIS A CB  1 
ATOM   2018 C CG  . HIS A 1 276 ? -9.995  -16.570 21.892  1.00 24.69  ? 256 HIS A CG  1 
ATOM   2019 N ND1 . HIS A 1 276 ? -10.255 -17.877 22.252  1.00 25.08  ? 256 HIS A ND1 1 
ATOM   2020 C CD2 . HIS A 1 276 ? -8.716  -16.344 22.233  1.00 26.47  ? 256 HIS A CD2 1 
ATOM   2021 C CE1 . HIS A 1 276 ? -9.154  -18.411 22.750  1.00 28.63  ? 256 HIS A CE1 1 
ATOM   2022 N NE2 . HIS A 1 276 ? -8.202  -17.514 22.742  1.00 27.30  ? 256 HIS A NE2 1 
ATOM   2023 N N   . GLN A 1 277 ? -11.702 -18.461 19.482  1.00 29.48  ? 257 GLN A N   1 
ATOM   2024 C CA  . GLN A 1 277 ? -12.450 -19.713 19.368  1.00 33.90  ? 257 GLN A CA  1 
ATOM   2025 C C   . GLN A 1 277 ? -13.180 -20.056 20.673  1.00 34.97  ? 257 GLN A C   1 
ATOM   2026 O O   . GLN A 1 277 ? -14.221 -20.713 20.634  1.00 34.70  ? 257 GLN A O   1 
ATOM   2027 C CB  . GLN A 1 277 ? -11.496 -20.848 18.977  1.00 36.00  ? 257 GLN A CB  1 
ATOM   2028 C CG  . GLN A 1 277 ? -12.093 -22.249 19.074  0.50 38.53  ? 257 GLN A CG  1 
ATOM   2029 C CD  . GLN A 1 277 ? -11.051 -23.334 19.229  0.30 41.90  ? 257 GLN A CD  1 
ATOM   2030 O OE1 . GLN A 1 277 ? -9.869  -23.153 18.930  0.30 45.28  ? 257 GLN A OE1 1 
ATOM   2031 N NE2 . GLN A 1 277 ? -11.492 -24.492 19.690  0.30 41.11  ? 257 GLN A NE2 1 
ATOM   2032 N N   . ARG A 1 278 ? -12.629 -19.651 21.827  1.00 32.84  ? 258 ARG A N   1 
ATOM   2033 C CA  . ARG A 1 278 ? -13.154 -20.079 23.119  1.00 33.42  ? 258 ARG A CA  1 
ATOM   2034 C C   . ARG A 1 278 ? -13.869 -18.948 23.858  1.00 33.44  ? 258 ARG A C   1 
ATOM   2035 O O   . ARG A 1 278 ? -14.200 -19.085 25.033  1.00 34.68  ? 258 ARG A O   1 
ATOM   2036 C CB  . ARG A 1 278 ? -12.035 -20.633 24.005  1.00 35.51  ? 258 ARG A CB  1 
ATOM   2037 C CG  . ARG A 1 278 ? -11.408 -21.907 23.450  1.00 40.55  ? 258 ARG A CG  1 
ATOM   2038 C CD  . ARG A 1 278 ? -10.364 -22.500 24.371  1.00 47.57  ? 258 ARG A CD  1 
ATOM   2039 N NE  . ARG A 1 278 ? -9.115  -21.752 24.507  1.00 52.98  ? 258 ARG A NE  1 
ATOM   2040 C CZ  . ARG A 1 278 ? -8.153  -21.689 23.588  1.00 57.94  ? 258 ARG A CZ  1 
ATOM   2041 N NH1 . ARG A 1 278 ? -7.004  -21.094 23.863  1.00 55.87  ? 258 ARG A NH1 1 
ATOM   2042 N NH2 . ARG A 1 278 ? -8.334  -22.226 22.394  0.30 64.76  ? 258 ARG A NH2 1 
ATOM   2043 N N   . ARG A 1 279 ? -14.112 -17.834 23.172  1.00 34.12  ? 259 ARG A N   1 
ATOM   2044 C CA  . ARG A 1 279 ? -14.878 -16.746 23.763  1.00 39.82  ? 259 ARG A CA  1 
ATOM   2045 C C   . ARG A 1 279 ? -14.547 -16.517 25.246  1.00 37.11  ? 259 ARG A C   1 
ATOM   2046 O O   . ARG A 1 279 ? -15.416 -16.535 26.114  1.00 39.89  ? 259 ARG A O   1 
ATOM   2047 C CB  . ARG A 1 279 ? -16.353 -17.053 23.505  0.70 45.12  ? 259 ARG A CB  1 
ATOM   2048 C CG  . ARG A 1 279 ? -16.725 -17.020 22.027  0.70 47.66  ? 259 ARG A CG  1 
ATOM   2049 C CD  . ARG A 1 279 ? -16.281 -15.738 21.339  1.00 48.31  ? 259 ARG A CD  1 
ATOM   2050 N NE  . ARG A 1 279 ? -17.212 -15.332 20.288  1.00 56.44  ? 259 ARG A NE  1 
ATOM   2051 C CZ  . ARG A 1 279 ? -18.092 -14.339 20.403  0.70 61.01  ? 259 ARG A CZ  1 
ATOM   2052 N NH1 . ARG A 1 279 ? -18.373 -13.835 21.596  1.00 60.41  ? 259 ARG A NH1 1 
ATOM   2053 N NH2 . ARG A 1 279 ? -18.711 -13.871 19.329  0.70 62.98  ? 259 ARG A NH2 1 
ATOM   2054 N N   . PRO A 1 280 ? -13.281 -16.179 25.574  1.00 32.03  ? 260 PRO A N   1 
ATOM   2055 C CA  . PRO A 1 280 ? -12.882 -15.878 26.955  1.00 26.69  ? 260 PRO A CA  1 
ATOM   2056 C C   . PRO A 1 280 ? -13.437 -14.542 27.444  1.00 26.30  ? 260 PRO A C   1 
ATOM   2057 O O   . PRO A 1 280 ? -13.736 -13.662 26.636  1.00 30.26  ? 260 PRO A O   1 
ATOM   2058 C CB  . PRO A 1 280 ? -11.351 -15.779 26.841  1.00 29.05  ? 260 PRO A CB  1 
ATOM   2059 C CG  . PRO A 1 280 ? -11.111 -15.291 25.434  1.00 29.97  ? 260 PRO A CG  1 
ATOM   2060 C CD  . PRO A 1 280 ? -12.197 -15.945 24.603  1.00 31.44  ? 260 PRO A CD  1 
ATOM   2061 N N   . SER A 1 281 ? -13.498 -14.378 28.773  1.00 27.18  ? 261 SER A N   1 
ATOM   2062 C CA  . SER A 1 281 ? -13.972 -13.142 29.383  1.00 28.38  ? 261 SER A CA  1 
ATOM   2063 C C   . SER A 1 281 ? -12.848 -12.113 29.513  1.00 26.74  ? 261 SER A C   1 
ATOM   2064 O O   . SER A 1 281 ? -13.115 -10.932 29.809  1.00 25.81  ? 261 SER A O   1 
ATOM   2065 C CB  . SER A 1 281 ? -14.578 -13.439 30.735  1.00 32.10  ? 261 SER A CB  1 
ATOM   2066 O OG  . SER A 1 281 ? -13.603 -13.945 31.639  1.00 33.53  ? 261 SER A OG  1 
ATOM   2067 N N   . HIS A 1 282 ? -11.596 -12.576 29.391  1.00 25.32  ? 262 HIS A N   1 
ATOM   2068 C CA  . HIS A 1 282 ? -10.424 -11.732 29.565  1.00 23.73  ? 262 HIS A CA  1 
ATOM   2069 C C   . HIS A 1 282 ? -9.519  -11.909 28.352  1.00 24.12  ? 262 HIS A C   1 
ATOM   2070 O O   . HIS A 1 282 ? -9.445  -12.996 27.756  1.00 24.24  ? 262 HIS A O   1 
ATOM   2071 C CB  . HIS A 1 282 ? -9.666  -12.042 30.860  1.00 24.89  ? 262 HIS A CB  1 
ATOM   2072 C CG  . HIS A 1 282 ? -10.355 -11.629 32.104  1.00 28.81  ? 262 HIS A CG  1 
ATOM   2073 N ND1 . HIS A 1 282 ? -11.517 -12.219 32.555  1.00 28.24  ? 262 HIS A ND1 1 
ATOM   2074 C CD2 . HIS A 1 282 ? -10.026 -10.677 33.007  1.00 29.70  ? 262 HIS A CD2 1 
ATOM   2075 C CE1 . HIS A 1 282 ? -11.884 -11.620 33.684  1.00 31.15  ? 262 HIS A CE1 1 
ATOM   2076 N NE2 . HIS A 1 282 ? -10.984 -10.696 33.987  1.00 31.53  ? 262 HIS A NE2 1 
ATOM   2077 N N   . ILE A 1 283 ? -8.850  -10.808 27.975  1.00 23.10  ? 263 ILE A N   1 
ATOM   2078 C CA  . ILE A 1 283 ? -7.915  -10.787 26.861  1.00 22.96  ? 263 ILE A CA  1 
ATOM   2079 C C   . ILE A 1 283 ? -6.630  -10.125 27.356  1.00 23.55  ? 263 ILE A C   1 
ATOM   2080 O O   . ILE A 1 283 ? -6.679  -9.106  28.056  1.00 25.47  ? 263 ILE A O   1 
ATOM   2081 C CB  . ILE A 1 283 ? -8.495  -10.020 25.653  1.00 22.82  ? 263 ILE A CB  1 
ATOM   2082 C CG1 . ILE A 1 283 ? -9.651  -10.775 24.983  1.00 24.61  ? 263 ILE A CG1 1 
ATOM   2083 C CG2 . ILE A 1 283 ? -7.390  -9.632  24.651  1.00 22.71  ? 263 ILE A CG2 1 
ATOM   2084 C CD1 . ILE A 1 283 ? -9.230  -12.029 24.217  1.00 25.72  ? 263 ILE A CD1 1 
ATOM   2085 N N   . ALA A 1 284 ? -5.487  -10.698 26.984  1.00 23.03  ? 264 ALA A N   1 
ATOM   2086 C CA  . ALA A 1 284 ? -4.189  -10.095 27.265  1.00 23.50  ? 264 ALA A CA  1 
ATOM   2087 C C   . ALA A 1 284 ? -3.849  -9.176  26.105  1.00 21.16  ? 264 ALA A C   1 
ATOM   2088 O O   . ALA A 1 284 ? -3.895  -9.613  24.953  1.00 23.04  ? 264 ALA A O   1 
ATOM   2089 C CB  . ALA A 1 284 ? -3.113  -11.155 27.432  1.00 24.89  ? 264 ALA A CB  1 
ATOM   2090 N N   . ILE A 1 285 ? -3.534  -7.904  26.397  1.00 22.16  ? 265 ILE A N   1 
ATOM   2091 C CA  . ILE A 1 285 ? -3.247  -6.946  25.341  1.00 21.51  ? 265 ILE A CA  1 
ATOM   2092 C C   . ILE A 1 285 ? -2.069  -6.072  25.775  1.00 19.85  ? 265 ILE A C   1 
ATOM   2093 O O   . ILE A 1 285 ? -2.024  -5.638  26.917  1.00 22.74  ? 265 ILE A O   1 
ATOM   2094 C CB  . ILE A 1 285 ? -4.500  -6.129  24.950  1.00 21.62  ? 265 ILE A CB  1 
ATOM   2095 C CG1 . ILE A 1 285 ? -4.224  -5.230  23.738  1.00 22.26  ? 265 ILE A CG1 1 
ATOM   2096 C CG2 . ILE A 1 285 ? -5.045  -5.348  26.128  1.00 22.95  ? 265 ILE A CG2 1 
ATOM   2097 C CD1 . ILE A 1 285 ? -5.465  -4.846  22.969  1.00 21.37  ? 265 ILE A CD1 1 
ATOM   2098 N N   . GLY A 1 286 ? -1.108  -5.875  24.867  1.00 20.65  ? 266 GLY A N   1 
ATOM   2099 C CA  . GLY A 1 286 ? 0.093   -5.096  25.124  1.00 20.51  ? 266 GLY A CA  1 
ATOM   2100 C C   . GLY A 1 286 ? -0.055  -3.668  24.616  1.00 20.46  ? 266 GLY A C   1 
ATOM   2101 O O   . GLY A 1 286 ? -0.715  -3.432  23.599  1.00 21.68  ? 266 GLY A O   1 
ATOM   2102 N N   . SER A 1 287 ? 0.547   -2.745  25.373  1.00 19.28  ? 267 SER A N   1 
ATOM   2103 C CA  . SER A 1 287 ? 0.658   -1.341  24.997  1.00 19.40  ? 267 SER A CA  1 
ATOM   2104 C C   . SER A 1 287 ? 2.133   -0.934  25.036  1.00 20.25  ? 267 SER A C   1 
ATOM   2105 O O   . SER A 1 287 ? 2.712   -0.808  26.116  1.00 20.78  ? 267 SER A O   1 
ATOM   2106 C CB  . SER A 1 287 ? -0.096  -0.452  25.947  1.00 20.84  ? 267 SER A CB  1 
ATOM   2107 O OG  . SER A 1 287 ? -1.483  -0.595  25.911  1.00 23.25  ? 267 SER A OG  1 
ATOM   2108 N N   . PRO A 1 288 ? 2.786   -0.707  23.874  1.00 21.17  ? 268 PRO A N   1 
ATOM   2109 C CA  . PRO A 1 288 ? 4.125   -0.103  23.831  1.00 23.07  ? 268 PRO A CA  1 
ATOM   2110 C C   . PRO A 1 288 ? 4.122   1.289   24.451  1.00 23.84  ? 268 PRO A C   1 
ATOM   2111 O O   . PRO A 1 288 ? 3.271   2.098   24.123  1.00 26.19  ? 268 PRO A O   1 
ATOM   2112 C CB  . PRO A 1 288 ? 4.436   -0.043  22.338  1.00 25.80  ? 268 PRO A CB  1 
ATOM   2113 C CG  . PRO A 1 288 ? 3.605   -1.193  21.767  1.00 26.20  ? 268 PRO A CG  1 
ATOM   2114 C CD  . PRO A 1 288 ? 2.308   -1.119  22.543  1.00 23.13  ? 268 PRO A CD  1 
ATOM   2115 N N   . ILE A 1 289 ? 4.991   1.472   25.444  1.00 22.83  ? 269 ILE A N   1 
ATOM   2116 C CA  . ILE A 1 289 ? 5.146   2.698   26.200  1.00 24.28  ? 269 ILE A CA  1 
ATOM   2117 C C   . ILE A 1 289 ? 6.440   3.363   25.761  1.00 22.72  ? 269 ILE A C   1 
ATOM   2118 O O   . ILE A 1 289 ? 7.510   2.785   25.850  1.00 21.38  ? 269 ILE A O   1 
ATOM   2119 C CB  . ILE A 1 289 ? 5.149   2.401   27.712  1.00 24.79  ? 269 ILE A CB  1 
ATOM   2120 C CG1 . ILE A 1 289 ? 3.855   1.727   28.154  1.00 27.43  ? 269 ILE A CG1 1 
ATOM   2121 C CG2 . ILE A 1 289 ? 5.428   3.670   28.507  1.00 28.32  ? 269 ILE A CG2 1 
ATOM   2122 C CD1 . ILE A 1 289 ? 2.614   2.390   27.627  0.80 27.54  ? 269 ILE A CD1 1 
ATOM   2123 N N   . ASP A 1 290 ? 6.320   4.642   25.365  1.00 22.22  ? 270 ASP A N   1 
ATOM   2124 C CA  . ASP A 1 290 ? 7.455   5.483   25.047  1.00 24.48  ? 270 ASP A CA  1 
ATOM   2125 C C   . ASP A 1 290 ? 8.165   5.891   26.339  1.00 22.16  ? 270 ASP A C   1 
ATOM   2126 O O   . ASP A 1 290 ? 7.544   6.502   27.233  1.00 27.64  ? 270 ASP A O   1 
ATOM   2127 C CB  . ASP A 1 290 ? 6.938   6.692   24.271  1.00 25.35  ? 270 ASP A CB  1 
ATOM   2128 C CG  . ASP A 1 290 ? 7.982   7.706   23.842  1.00 30.81  ? 270 ASP A CG  1 
ATOM   2129 O OD1 . ASP A 1 290 ? 9.147   7.521   24.173  1.00 30.15  ? 270 ASP A OD1 1 
ATOM   2130 O OD2 . ASP A 1 290 ? 7.615   8.678   23.137  1.00 38.44  ? 270 ASP A OD2 1 
ATOM   2131 N N   . PHE A 1 291 ? 9.459   5.605   26.410  1.00 19.18  ? 271 PHE A N   1 
ATOM   2132 C CA  . PHE A 1 291 ? 10.230  5.940   27.633  1.00 21.46  ? 271 PHE A CA  1 
ATOM   2133 C C   . PHE A 1 291 ? 11.356  6.953   27.362  1.00 22.49  ? 271 PHE A C   1 
ATOM   2134 O O   . PHE A 1 291 ? 12.210  7.119   28.226  1.00 22.44  ? 271 PHE A O   1 
ATOM   2135 C CB  . PHE A 1 291 ? 10.749  4.668   28.314  1.00 22.28  ? 271 PHE A CB  1 
ATOM   2136 C CG  . PHE A 1 291 ? 11.574  3.731   27.469  1.00 21.65  ? 271 PHE A CG  1 
ATOM   2137 C CD1 . PHE A 1 291 ? 12.874  4.047   27.117  1.00 23.23  ? 271 PHE A CD1 1 
ATOM   2138 C CD2 . PHE A 1 291 ? 11.061  2.513   27.061  1.00 21.87  ? 271 PHE A CD2 1 
ATOM   2139 C CE1 . PHE A 1 291 ? 13.637  3.178   26.354  1.00 22.78  ? 271 PHE A CE1 1 
ATOM   2140 C CE2 . PHE A 1 291 ? 11.824  1.644   26.299  1.00 23.45  ? 271 PHE A CE2 1 
ATOM   2141 C CZ  . PHE A 1 291 ? 13.108  1.978   25.945  1.00 22.39  ? 271 PHE A CZ  1 
ATOM   2142 N N   . ARG A 1 292 ? 11.320  7.621   26.205  1.00 21.11  ? 272 ARG A N   1 
ATOM   2143 C CA  . ARG A 1 292 ? 12.344  8.616   25.903  1.00 22.16  ? 272 ARG A CA  1 
ATOM   2144 C C   . ARG A 1 292 ? 12.578  9.582   27.069  1.00 23.68  ? 272 ARG A C   1 
ATOM   2145 O O   . ARG A 1 292 ? 13.724  9.902   27.378  1.00 23.85  ? 272 ARG A O   1 
ATOM   2146 C CB  . ARG A 1 292 ? 11.927  9.439   24.689  1.00 21.93  ? 272 ARG A CB  1 
ATOM   2147 C CG  . ARG A 1 292 ? 12.043  8.727   23.352  1.00 22.18  ? 272 ARG A CG  1 
ATOM   2148 C CD  . ARG A 1 292 ? 11.625  9.628   22.206  1.00 22.27  ? 272 ARG A CD  1 
ATOM   2149 N NE  . ARG A 1 292 ? 11.397  8.840   20.985  1.00 24.75  ? 272 ARG A NE  1 
ATOM   2150 C CZ  . ARG A 1 292 ? 12.147  8.838   19.906  1.00 25.28  ? 272 ARG A CZ  1 
ATOM   2151 N NH1 . ARG A 1 292 ? 13.132  9.718   19.756  1.00 25.04  ? 272 ARG A NH1 1 
ATOM   2152 N NH2 . ARG A 1 292 ? 11.875  7.956   18.955  1.00 22.67  ? 272 ARG A NH2 1 
ATOM   2153 N N   . ASP A 1 293 ? 11.486  10.035  27.695  1.00 23.27  ? 273 ASP A N   1 
ATOM   2154 C CA  . ASP A 1 293 ? 11.550  11.125  28.658  1.00 24.64  ? 273 ASP A CA  1 
ATOM   2155 C C   . ASP A 1 293 ? 12.094  10.620  30.001  1.00 25.15  ? 273 ASP A C   1 
ATOM   2156 O O   . ASP A 1 293 ? 12.439  11.422  30.872  1.00 26.44  ? 273 ASP A O   1 
ATOM   2157 C CB  . ASP A 1 293 ? 10.164  11.761  28.799  1.00 27.17  ? 273 ASP A CB  1 
ATOM   2158 C CG  . ASP A 1 293 ? 9.707   12.453  27.518  1.00 29.74  ? 273 ASP A CG  1 
ATOM   2159 O OD1 . ASP A 1 293 ? 10.431  13.352  27.057  0.60 32.43  ? 273 ASP A OD1 1 
ATOM   2160 O OD2 . ASP A 1 293 ? 8.638   12.136  27.020  0.40 27.10  ? 273 ASP A OD2 1 
ATOM   2161 N N   . GLU A 1 294 ? 12.120  9.279   30.185  1.00 22.95  ? 274 GLU A N   1 
ATOM   2162 C CA  . GLU A 1 294 ? 12.543  8.702   31.457  1.00 26.09  ? 274 GLU A CA  1 
ATOM   2163 C C   . GLU A 1 294 ? 14.003  8.263   31.430  1.00 26.70  ? 274 GLU A C   1 
ATOM   2164 O O   . GLU A 1 294 ? 14.527  7.834   32.450  1.00 28.49  ? 274 GLU A O   1 
ATOM   2165 C CB  . GLU A 1 294 ? 11.690  7.513   31.878  1.00 27.15  ? 274 GLU A CB  1 
ATOM   2166 C CG  . GLU A 1 294 ? 10.238  7.868   32.122  1.00 29.69  ? 274 GLU A CG  1 
ATOM   2167 C CD  . GLU A 1 294 ? 9.328   6.664   32.296  1.00 34.14  ? 274 GLU A CD  1 
ATOM   2168 O OE1 . GLU A 1 294 ? 8.360   6.544   31.523  1.00 40.83  ? 274 GLU A OE1 1 
ATOM   2169 O OE2 . GLU A 1 294 ? 9.593   5.849   33.194  1.00 39.19  ? 274 GLU A OE2 1 
ATOM   2170 N N   . LEU A 1 295 ? 14.668  8.375   30.281  1.00 26.99  ? 275 LEU A N   1 
ATOM   2171 C CA  . LEU A 1 295 ? 16.065  7.983   30.171  1.00 25.28  ? 275 LEU A CA  1 
ATOM   2172 C C   . LEU A 1 295 ? 16.942  9.089   30.755  1.00 27.65  ? 275 LEU A C   1 
ATOM   2173 O O   . LEU A 1 295 ? 16.477  10.216  30.897  1.00 28.90  ? 275 LEU A O   1 
ATOM   2174 C CB  . LEU A 1 295 ? 16.358  7.708   28.689  1.00 24.26  ? 275 LEU A CB  1 
ATOM   2175 C CG  . LEU A 1 295 ? 15.606  6.531   28.057  1.00 23.62  ? 275 LEU A CG  1 
ATOM   2176 C CD1 . LEU A 1 295 ? 15.893  6.427   26.572  1.00 21.07  ? 275 LEU A CD1 1 
ATOM   2177 C CD2 . LEU A 1 295 ? 15.979  5.233   28.750  1.00 25.40  ? 275 LEU A CD2 1 
ATOM   2178 N N   . GLU A 1 296 ? 18.181  8.735   31.151  1.00 31.85  ? 276 GLU A N   1 
ATOM   2179 C CA  . GLU A 1 296 ? 19.099  9.652   31.809  1.00 31.59  ? 276 GLU A CA  1 
ATOM   2180 C C   . GLU A 1 296 ? 20.383  9.713   30.989  1.00 33.07  ? 276 GLU A C   1 
ATOM   2181 O O   . GLU A 1 296 ? 21.177  8.779   31.012  1.00 35.64  ? 276 GLU A O   1 
ATOM   2182 C CB  . GLU A 1 296 ? 19.359  9.205   33.249  1.00 33.85  ? 276 GLU A CB  1 
ATOM   2183 C CG  . GLU A 1 296 ? 18.104  9.249   34.095  1.00 37.83  ? 276 GLU A CG  1 
ATOM   2184 C CD  . GLU A 1 296 ? 18.180  8.713   35.514  1.00 44.46  ? 276 GLU A CD  1 
ATOM   2185 O OE1 . GLU A 1 296 ? 17.214  8.935   36.264  1.00 51.82  ? 276 GLU A OE1 1 
ATOM   2186 O OE2 . GLU A 1 296 ? 19.178  8.062   35.866  1.00 49.04  ? 276 GLU A OE2 1 
ATOM   2187 N N   . PRO A 1 297 ? 20.648  10.799  30.229  1.00 34.77  ? 277 PRO A N   1 
ATOM   2188 C CA  . PRO A 1 297 ? 19.700  11.894  30.067  1.00 35.03  ? 277 PRO A CA  1 
ATOM   2189 C C   . PRO A 1 297 ? 18.564  11.541  29.104  1.00 31.72  ? 277 PRO A C   1 
ATOM   2190 O O   . PRO A 1 297 ? 18.653  10.590  28.329  1.00 31.15  ? 277 PRO A O   1 
ATOM   2191 C CB  . PRO A 1 297 ? 20.571  13.008  29.473  1.00 36.22  ? 277 PRO A CB  1 
ATOM   2192 C CG  . PRO A 1 297 ? 21.588  12.248  28.658  1.00 38.33  ? 277 PRO A CG  1 
ATOM   2193 C CD  . PRO A 1 297 ? 21.897  11.015  29.484  1.00 38.08  ? 277 PRO A CD  1 
ATOM   2194 N N   . PRO A 1 298 ? 17.461  12.317  29.106  1.00 32.35  ? 278 PRO A N   1 
ATOM   2195 C CA  . PRO A 1 298 ? 16.318  12.029  28.245  1.00 30.40  ? 278 PRO A CA  1 
ATOM   2196 C C   . PRO A 1 298 ? 16.681  12.119  26.762  1.00 26.90  ? 278 PRO A C   1 
ATOM   2197 O O   . PRO A 1 298 ? 17.536  12.886  26.344  1.00 27.18  ? 278 PRO A O   1 
ATOM   2198 C CB  . PRO A 1 298 ? 15.283  13.116  28.576  1.00 31.34  ? 278 PRO A CB  1 
ATOM   2199 C CG  . PRO A 1 298 ? 15.755  13.742  29.870  1.00 32.56  ? 278 PRO A CG  1 
ATOM   2200 C CD  . PRO A 1 298 ? 17.242  13.497  29.951  1.00 33.38  ? 278 PRO A CD  1 
ATOM   2201 N N   . VAL A 1 299 ? 16.021  11.293  25.973  1.00 25.50  ? 279 VAL A N   1 
ATOM   2202 C CA  . VAL A 1 299 ? 16.152  11.310  24.531  1.00 23.70  ? 279 VAL A CA  1 
ATOM   2203 C C   . VAL A 1 299 ? 15.035  12.195  23.976  1.00 22.82  ? 279 VAL A C   1 
ATOM   2204 O O   . VAL A 1 299 ? 13.878  12.120  24.401  1.00 23.47  ? 279 VAL A O   1 
ATOM   2205 C CB  . VAL A 1 299 ? 16.103  9.856   24.021  1.00 23.64  ? 279 VAL A CB  1 
ATOM   2206 C CG1 . VAL A 1 299 ? 15.987  9.748   22.503  1.00 23.17  ? 279 VAL A CG1 1 
ATOM   2207 C CG2 . VAL A 1 299 ? 17.289  9.061   24.539  1.00 24.57  ? 279 VAL A CG2 1 
ATOM   2208 N N   . ARG A 1 300 ? 15.382  13.071  23.035  1.00 22.94  ? 280 ARG A N   1 
ATOM   2209 C CA  . ARG A 1 300 ? 14.376  13.961  22.489  1.00 23.56  ? 280 ARG A CA  1 
ATOM   2210 C C   . ARG A 1 300 ? 13.558  13.233  21.428  1.00 20.99  ? 280 ARG A C   1 
ATOM   2211 O O   . ARG A 1 300 ? 14.019  12.275  20.798  1.00 20.60  ? 280 ARG A O   1 
ATOM   2212 C CB  . ARG A 1 300 ? 15.003  15.267  21.983  1.00 25.69  ? 280 ARG A CB  1 
ATOM   2213 C CG  . ARG A 1 300 ? 15.704  16.056  23.073  1.00 30.23  ? 280 ARG A CG  1 
ATOM   2214 C CD  . ARG A 1 300 ? 14.791  16.430  24.247  1.00 36.64  ? 280 ARG A CD  1 
ATOM   2215 N NE  . ARG A 1 300 ? 13.748  17.408  23.883  1.00 38.41  ? 280 ARG A NE  1 
ATOM   2216 C CZ  . ARG A 1 300 ? 12.624  17.645  24.554  1.00 37.41  ? 280 ARG A CZ  1 
ATOM   2217 N NH1 . ARG A 1 300 ? 12.323  16.975  25.654  1.00 41.36  ? 280 ARG A NH1 1 
ATOM   2218 N NH2 . ARG A 1 300 ? 11.785  18.547  24.092  1.00 38.93  ? 280 ARG A NH2 1 
ATOM   2219 N N   . PRO A 1 301 ? 12.310  13.682  21.188  1.00 22.13  ? 281 PRO A N   1 
ATOM   2220 C CA  . PRO A 1 301 ? 11.449  13.069  20.174  1.00 21.00  ? 281 PRO A CA  1 
ATOM   2221 C C   . PRO A 1 301 ? 11.880  13.257  18.715  1.00 20.19  ? 281 PRO A C   1 
ATOM   2222 O O   . PRO A 1 301 ? 11.209  12.739  17.812  1.00 22.62  ? 281 PRO A O   1 
ATOM   2223 C CB  . PRO A 1 301 ? 10.077  13.735  20.377  1.00 24.46  ? 281 PRO A CB  1 
ATOM   2224 C CG  . PRO A 1 301 ? 10.157  14.436  21.695  1.00 25.97  ? 281 PRO A CG  1 
ATOM   2225 C CD  . PRO A 1 301 ? 11.619  14.745  21.930  1.00 25.16  ? 281 PRO A CD  1 
ATOM   2226 N N   . ASP A 1 302 ? 13.012  13.941  18.480  1.00 19.39  ? 282 ASP A N   1 
ATOM   2227 C CA  . ASP A 1 302 ? 13.525  14.151  17.132  1.00 18.12  ? 282 ASP A CA  1 
ATOM   2228 C C   . ASP A 1 302 ? 14.805  13.346  16.873  1.00 19.19  ? 282 ASP A C   1 
ATOM   2229 O O   . ASP A 1 302 ? 15.436  13.526  15.819  1.00 18.21  ? 282 ASP A O   1 
ATOM   2230 C CB  . ASP A 1 302 ? 13.697  15.648  16.808  1.00 19.99  ? 282 ASP A CB  1 
ATOM   2231 C CG  . ASP A 1 302 ? 14.611  16.409  17.758  1.00 21.30  ? 282 ASP A CG  1 
ATOM   2232 O OD1 . ASP A 1 302 ? 15.219  15.789  18.633  1.00 23.17  ? 282 ASP A OD1 1 
ATOM   2233 O OD2 . ASP A 1 302 ? 14.650  17.666  17.651  1.00 24.10  ? 282 ASP A OD2 1 
ATOM   2234 N N   . GLU A 1 303 ? 15.160  12.422  17.791  1.00 20.78  ? 283 GLU A N   1 
ATOM   2235 C CA  . GLU A 1 303 ? 16.367  11.607  17.673  1.00 20.53  ? 283 GLU A CA  1 
ATOM   2236 C C   . GLU A 1 303 ? 15.992  10.189  17.227  1.00 19.42  ? 283 GLU A C   1 
ATOM   2237 O O   . GLU A 1 303 ? 14.900  9.726   17.531  1.00 20.56  ? 283 GLU A O   1 
ATOM   2238 C CB  . GLU A 1 303 ? 17.126  11.599  19.004  1.00 21.64  ? 283 GLU A CB  1 
ATOM   2239 C CG  . GLU A 1 303 ? 17.600  12.994  19.415  1.00 23.39  ? 283 GLU A CG  1 
ATOM   2240 C CD  . GLU A 1 303 ? 18.477  12.948  20.660  1.00 25.58  ? 283 GLU A CD  1 
ATOM   2241 O OE1 . GLU A 1 303 ? 17.918  12.977  21.787  1.00 28.21  ? 283 GLU A OE1 1 
ATOM   2242 O OE2 . GLU A 1 303 ? 19.707  12.859  20.507  1.00 29.27  ? 283 GLU A OE2 1 
ATOM   2243 N N   . VAL A 1 304 ? 16.936  9.564   16.506  1.00 17.84  ? 284 VAL A N   1 
ATOM   2244 C CA  . VAL A 1 304 ? 16.759  8.220   15.971  1.00 18.04  ? 284 VAL A CA  1 
ATOM   2245 C C   . VAL A 1 304 ? 17.011  7.178   17.049  1.00 19.37  ? 284 VAL A C   1 
ATOM   2246 O O   . VAL A 1 304 ? 17.742  7.375   17.990  1.00 20.00  ? 284 VAL A O   1 
ATOM   2247 C CB  . VAL A 1 304 ? 17.612  8.018   14.705  1.00 18.80  ? 284 VAL A CB  1 
ATOM   2248 C CG1 . VAL A 1 304 ? 17.564  6.604   14.120  1.00 18.45  ? 284 VAL A CG1 1 
ATOM   2249 C CG2 . VAL A 1 304 ? 17.207  9.018   13.643  1.00 20.39  ? 284 VAL A CG2 1 
ATOM   2250 N N   . GLY A 1 305 ? 16.317  6.058   16.869  1.00 19.69  ? 285 GLY A N   1 
ATOM   2251 C CA  . GLY A 1 305 ? 16.413  4.881   17.722  1.00 19.47  ? 285 GLY A CA  1 
ATOM   2252 C C   . GLY A 1 305 ? 15.027  4.361   18.086  1.00 19.28  ? 285 GLY A C   1 
ATOM   2253 O O   . GLY A 1 305 ? 14.015  4.875   17.649  1.00 20.69  ? 285 GLY A O   1 
ATOM   2254 N N   . THR A 1 306 ? 15.004  3.283   18.875  1.00 20.38  ? 286 THR A N   1 
ATOM   2255 C CA  . THR A 1 306 ? 13.758  2.695   19.364  1.00 21.41  ? 286 THR A CA  1 
ATOM   2256 C C   . THR A 1 306 ? 13.721  2.848   20.884  1.00 19.58  ? 286 THR A C   1 
ATOM   2257 O O   . THR A 1 306 ? 14.663  2.498   21.582  1.00 21.38  ? 286 THR A O   1 
ATOM   2258 C CB  . THR A 1 306 ? 13.539  1.252   18.838  1.00 23.99  ? 286 THR A CB  1 
ATOM   2259 O OG1 . THR A 1 306 ? 12.291  0.779   19.338  1.00 24.08  ? 286 THR A OG1 1 
ATOM   2260 C CG2 . THR A 1 306 ? 14.599  0.241   19.212  1.00 25.08  ? 286 THR A CG2 1 
ATOM   2261 N N   . TYR A 1 307 ? 12.626  3.409   21.379  1.00 18.60  ? 287 TYR A N   1 
ATOM   2262 C CA  . TYR A 1 307 ? 12.516  3.775   22.779  1.00 18.88  ? 287 TYR A CA  1 
ATOM   2263 C C   . TYR A 1 307 ? 11.132  3.422   23.319  1.00 21.04  ? 287 TYR A C   1 
ATOM   2264 O O   . TYR A 1 307 ? 10.567  4.162   24.103  1.00 21.51  ? 287 TYR A O   1 
ATOM   2265 C CB  . TYR A 1 307 ? 12.819  5.271   22.921  1.00 19.92  ? 287 TYR A CB  1 
ATOM   2266 C CG  . TYR A 1 307 ? 14.141  5.687   22.338  1.00 20.26  ? 287 TYR A CG  1 
ATOM   2267 C CD1 . TYR A 1 307 ? 15.326  5.450   23.007  1.00 20.07  ? 287 TYR A CD1 1 
ATOM   2268 C CD2 . TYR A 1 307 ? 14.212  6.296   21.083  1.00 18.27  ? 287 TYR A CD2 1 
ATOM   2269 C CE1 . TYR A 1 307 ? 16.558  5.777   22.466  1.00 20.33  ? 287 TYR A CE1 1 
ATOM   2270 C CE2 . TYR A 1 307 ? 15.438  6.627   20.534  1.00 20.49  ? 287 TYR A CE2 1 
ATOM   2271 C CZ  . TYR A 1 307 ? 16.625  6.384   21.225  1.00 20.14  ? 287 TYR A CZ  1 
ATOM   2272 O OH  . TYR A 1 307 ? 17.879  6.716   20.735  1.00 20.63  ? 287 TYR A OH  1 
ATOM   2273 N N   . VAL A 1 308 ? 10.625  2.233   22.983  1.00 20.51  ? 288 VAL A N   1 
ATOM   2274 C CA  . VAL A 1 308 ? 9.330   1.760   23.450  1.00 21.09  ? 288 VAL A CA  1 
ATOM   2275 C C   . VAL A 1 308 ? 9.517   0.350   24.000  1.00 20.89  ? 288 VAL A C   1 
ATOM   2276 O O   . VAL A 1 308 ? 10.373  -0.408  23.560  1.00 22.73  ? 288 VAL A O   1 
ATOM   2277 C CB  . VAL A 1 308 ? 8.235   1.772   22.355  1.00 21.79  ? 288 VAL A CB  1 
ATOM   2278 C CG1 . VAL A 1 308 ? 7.909   3.182   21.944  1.00 22.10  ? 288 VAL A CG1 1 
ATOM   2279 C CG2 . VAL A 1 308 ? 8.627   0.988   21.135  1.00 24.38  ? 288 VAL A CG2 1 
ATOM   2280 N N   . ALA A 1 309 ? 8.674   0.039   24.977  1.00 21.01  ? 289 ALA A N   1 
ATOM   2281 C CA  . ALA A 1 309 ? 8.589   -1.295  25.526  1.00 21.41  ? 289 ALA A CA  1 
ATOM   2282 C C   . ALA A 1 309 ? 7.130   -1.600  25.833  1.00 21.58  ? 289 ALA A C   1 
ATOM   2283 O O   . ALA A 1 309 ? 6.432   -0.801  26.448  1.00 21.12  ? 289 ALA A O   1 
ATOM   2284 C CB  . ALA A 1 309 ? 9.467   -1.362  26.748  1.00 23.10  ? 289 ALA A CB  1 
ATOM   2285 N N   . THR A 1 310 ? 6.703   -2.800  25.445  1.00 22.46  ? 290 THR A N   1 
ATOM   2286 C CA  . THR A 1 310 ? 5.331   -3.257  25.609  1.00 23.52  ? 290 THR A CA  1 
ATOM   2287 C C   . THR A 1 310 ? 5.032   -3.659  27.054  1.00 23.35  ? 290 THR A C   1 
ATOM   2288 O O   . THR A 1 310 ? 5.746   -4.466  27.666  1.00 26.88  ? 290 THR A O   1 
ATOM   2289 C CB  . THR A 1 310 ? 5.017   -4.345  24.582  1.00 27.42  ? 290 THR A CB  1 
ATOM   2290 O OG1 . THR A 1 310 ? 5.342   -3.871  23.283  1.00 29.16  ? 290 THR A OG1 1 
ATOM   2291 C CG2 . THR A 1 310 ? 3.560   -4.738  24.585  1.00 31.38  ? 290 THR A CG2 1 
ATOM   2292 N N   . VAL A 1 311 ? 3.950   -3.059  27.580  1.00 21.32  ? 291 VAL A N   1 
ATOM   2293 C CA  . VAL A 1 311 ? 3.397   -3.370  28.880  1.00 23.64  ? 291 VAL A CA  1 
ATOM   2294 C C   . VAL A 1 311 ? 2.089   -4.129  28.687  1.00 25.18  ? 291 VAL A C   1 
ATOM   2295 O O   . VAL A 1 311 ? 1.139   -3.630  28.064  1.00 23.23  ? 291 VAL A O   1 
ATOM   2296 C CB  . VAL A 1 311 ? 3.193   -2.080  29.683  1.00 24.44  ? 291 VAL A CB  1 
ATOM   2297 C CG1 . VAL A 1 311 ? 2.447   -2.321  30.977  1.00 26.02  ? 291 VAL A CG1 1 
ATOM   2298 C CG2 . VAL A 1 311 ? 4.528   -1.419  29.970  1.00 26.67  ? 291 VAL A CG2 1 
ATOM   2299 N N   . PRO A 1 312 ? 1.971   -5.345  29.260  1.00 24.94  ? 292 PRO A N   1 
ATOM   2300 C CA  . PRO A 1 312 ? 0.734   -6.117  29.175  1.00 26.99  ? 292 PRO A CA  1 
ATOM   2301 C C   . PRO A 1 312 ? -0.310  -5.697  30.208  1.00 22.53  ? 292 PRO A C   1 
ATOM   2302 O O   . PRO A 1 312 ? 0.034   -5.291  31.311  1.00 24.25  ? 292 PRO A O   1 
ATOM   2303 C CB  . PRO A 1 312 ? 1.230   -7.533  29.463  1.00 28.02  ? 292 PRO A CB  1 
ATOM   2304 C CG  . PRO A 1 312 ? 2.311   -7.316  30.473  1.00 27.42  ? 292 PRO A CG  1 
ATOM   2305 C CD  . PRO A 1 312 ? 3.001   -6.026  30.068  1.00 26.45  ? 292 PRO A CD  1 
ATOM   2306 N N   . VAL A 1 313 ? -1.570  -5.827  29.812  1.00 22.45  ? 293 VAL A N   1 
ATOM   2307 C CA  . VAL A 1 313 ? -2.706  -5.734  30.702  1.00 22.56  ? 293 VAL A CA  1 
ATOM   2308 C C   . VAL A 1 313 ? -3.609  -6.945  30.443  1.00 23.42  ? 293 VAL A C   1 
ATOM   2309 O O   . VAL A 1 313 ? -3.878  -7.322  29.312  1.00 23.51  ? 293 VAL A O   1 
ATOM   2310 C CB  . VAL A 1 313 ? -3.462  -4.406  30.525  1.00 23.53  ? 293 VAL A CB  1 
ATOM   2311 C CG1 . VAL A 1 313 ? -4.755  -4.355  31.322  1.00 23.87  ? 293 VAL A CG1 1 
ATOM   2312 C CG2 . VAL A 1 313 ? -2.594  -3.218  30.875  1.00 24.86  ? 293 VAL A CG2 1 
ATOM   2313 N N   . VAL A 1 314 ? -4.059  -7.555  31.533  1.00 23.80  ? 294 VAL A N   1 
ATOM   2314 C CA  . VAL A 1 314 ? -5.055  -8.599  31.491  1.00 26.08  ? 294 VAL A CA  1 
ATOM   2315 C C   . VAL A 1 314 ? -6.405  -7.940  31.716  1.00 23.70  ? 294 VAL A C   1 
ATOM   2316 O O   . VAL A 1 314 ? -6.720  -7.497  32.817  1.00 28.06  ? 294 VAL A O   1 
ATOM   2317 C CB  . VAL A 1 314 ? -4.703  -9.657  32.545  1.00 26.92  ? 294 VAL A CB  1 
ATOM   2318 C CG1 . VAL A 1 314 ? -5.776  -10.716 32.651  1.00 30.13  ? 294 VAL A CG1 1 
ATOM   2319 C CG2 . VAL A 1 314 ? -3.333  -10.261 32.254  1.00 27.55  ? 294 VAL A CG2 1 
ATOM   2320 N N   . LEU A 1 315 ? -7.158  -7.828  30.628  1.00 22.85  ? 295 LEU A N   1 
ATOM   2321 C CA  . LEU A 1 315 ? -8.312  -6.967  30.590  1.00 23.56  ? 295 LEU A CA  1 
ATOM   2322 C C   . LEU A 1 315 ? -9.602  -7.790  30.575  1.00 24.70  ? 295 LEU A C   1 
ATOM   2323 O O   . LEU A 1 315 ? -9.783  -8.655  29.718  1.00 25.15  ? 295 LEU A O   1 
ATOM   2324 C CB  . LEU A 1 315 ? -8.118  -6.157  29.309  1.00 24.97  ? 295 LEU A CB  1 
ATOM   2325 C CG  . LEU A 1 315 ? -8.986  -4.929  29.152  1.00 25.12  ? 295 LEU A CG  1 
ATOM   2326 C CD1 . LEU A 1 315 ? -8.842  -3.957  30.303  1.00 24.05  ? 295 LEU A CD1 1 
ATOM   2327 C CD2 . LEU A 1 315 ? -8.666  -4.250  27.821  1.00 23.85  ? 295 LEU A CD2 1 
ATOM   2328 N N   . ASP A 1 316 ? -10.498 -7.480  31.512  1.00 23.41  ? 296 ASP A N   1 
ATOM   2329 C CA  . ASP A 1 316 ? -11.846 -8.042  31.530  1.00 24.66  ? 296 ASP A CA  1 
ATOM   2330 C C   . ASP A 1 316 ? -12.669 -7.331  30.453  1.00 24.19  ? 296 ASP A C   1 
ATOM   2331 O O   . ASP A 1 316 ? -12.973 -6.140  30.598  1.00 25.25  ? 296 ASP A O   1 
ATOM   2332 C CB  . ASP A 1 316 ? -12.509 -7.833  32.893  1.00 26.20  ? 296 ASP A CB  1 
ATOM   2333 C CG  . ASP A 1 316 ? -13.876 -8.483  33.085  1.00 28.81  ? 296 ASP A CG  1 
ATOM   2334 O OD1 . ASP A 1 316 ? -14.439 -9.042  32.118  1.00 28.72  ? 296 ASP A OD1 1 
ATOM   2335 O OD2 . ASP A 1 316 ? -14.373 -8.439  34.240  1.00 31.15  ? 296 ASP A OD2 1 
ATOM   2336 N N   . ILE A 1 317 ? -13.019 -8.048  29.395  1.00 25.41  ? 297 ILE A N   1 
ATOM   2337 C CA  . ILE A 1 317 ? -13.777 -7.510  28.281  1.00 24.63  ? 297 ILE A CA  1 
ATOM   2338 C C   . ILE A 1 317 ? -15.274 -7.799  28.386  1.00 25.02  ? 297 ILE A C   1 
ATOM   2339 O O   . ILE A 1 317 ? -16.031 -7.370  27.510  1.00 27.72  ? 297 ILE A O   1 
ATOM   2340 C CB  . ILE A 1 317 ? -13.221 -8.021  26.946  1.00 24.14  ? 297 ILE A CB  1 
ATOM   2341 C CG1 . ILE A 1 317 ? -13.237 -9.559  26.897  1.00 26.30  ? 297 ILE A CG1 1 
ATOM   2342 C CG2 . ILE A 1 317 ? -11.855 -7.401  26.696  1.00 24.42  ? 297 ILE A CG2 1 
ATOM   2343 C CD1 . ILE A 1 317 ? -13.149 -10.124 25.527  1.00 32.21  ? 297 ILE A CD1 1 
ATOM   2344 N N   . ALA A 1 318 ? -15.707 -8.481  29.446  1.00 25.33  ? 298 ALA A N   1 
ATOM   2345 C CA  . ALA A 1 318 ? -17.133 -8.840  29.623  1.00 27.59  ? 298 ALA A CA  1 
ATOM   2346 C C   . ALA A 1 318 ? -17.806 -7.818  30.525  1.00 28.19  ? 298 ALA A C   1 
ATOM   2347 O O   . ALA A 1 318 ? -18.441 -8.187  31.511  1.00 34.30  ? 298 ALA A O   1 
ATOM   2348 C CB  . ALA A 1 318 ? -17.224 -10.224 30.211  1.00 31.36  ? 298 ALA A CB  1 
ATOM   2349 N N   . ARG A 1 319 ? -17.634 -6.550  30.201  1.00 25.57  ? 299 ARG A N   1 
ATOM   2350 C CA  . ARG A 1 319 ? -18.132 -5.446  30.985  1.00 26.83  ? 299 ARG A CA  1 
ATOM   2351 C C   . ARG A 1 319 ? -18.547 -4.403  29.963  1.00 25.44  ? 299 ARG A C   1 
ATOM   2352 O O   . ARG A 1 319 ? -18.090 -4.454  28.815  1.00 25.10  ? 299 ARG A O   1 
ATOM   2353 C CB  . ARG A 1 319 ? -17.056 -4.832  31.894  1.00 29.25  ? 299 ARG A CB  1 
ATOM   2354 C CG  . ARG A 1 319 ? -16.475 -5.758  32.954  1.00 32.76  ? 299 ARG A CG  1 
ATOM   2355 C CD  . ARG A 1 319 ? -17.530 -6.233  33.936  1.00 36.98  ? 299 ARG A CD  1 
ATOM   2356 N NE  . ARG A 1 319 ? -18.176 -5.103  34.604  1.00 44.65  ? 299 ARG A NE  1 
ATOM   2357 C CZ  . ARG A 1 319 ? -19.437 -5.059  35.022  1.00 46.73  ? 299 ARG A CZ  1 
ATOM   2358 N NH1 . ARG A 1 319 ? -20.183 -6.149  35.027  1.00 52.73  ? 299 ARG A NH1 1 
ATOM   2359 N NH2 . ARG A 1 319 ? -19.927 -3.928  35.500  0.70 45.41  ? 299 ARG A NH2 1 
ATOM   2360 N N   . PRO A 1 320 ? -19.308 -3.365  30.386  1.00 24.85  ? 300 PRO A N   1 
ATOM   2361 C CA  . PRO A 1 320 ? -19.595 -2.225  29.512  1.00 25.19  ? 300 PRO A CA  1 
ATOM   2362 C C   . PRO A 1 320 ? -18.322 -1.586  28.961  1.00 23.52  ? 300 PRO A C   1 
ATOM   2363 O O   . PRO A 1 320 ? -17.308 -1.471  29.660  1.00 23.44  ? 300 PRO A O   1 
ATOM   2364 C CB  . PRO A 1 320 ? -20.312 -1.248  30.441  1.00 26.67  ? 300 PRO A CB  1 
ATOM   2365 C CG  . PRO A 1 320 ? -20.981 -2.150  31.453  1.00 28.75  ? 300 PRO A CG  1 
ATOM   2366 C CD  . PRO A 1 320 ? -19.969 -3.251  31.693  1.00 27.33  ? 300 PRO A CD  1 
ATOM   2367 N N   . PHE A 1 321 ? -18.403 -1.183  27.691  1.00 22.28  ? 301 PHE A N   1 
ATOM   2368 C CA  . PHE A 1 321 ? -17.239 -0.708  26.959  1.00 21.61  ? 301 PHE A CA  1 
ATOM   2369 C C   . PHE A 1 321 ? -16.406 0.292   27.764  1.00 20.96  ? 301 PHE A C   1 
ATOM   2370 O O   . PHE A 1 321 ? -15.180 0.197   27.816  1.00 20.27  ? 301 PHE A O   1 
ATOM   2371 C CB  . PHE A 1 321 ? -17.657 -0.044  25.653  1.00 21.73  ? 301 PHE A CB  1 
ATOM   2372 C CG  . PHE A 1 321 ? -16.510 0.561   24.881  1.00 20.40  ? 301 PHE A CG  1 
ATOM   2373 C CD1 . PHE A 1 321 ? -15.782 -0.165  23.945  1.00 20.81  ? 301 PHE A CD1 1 
ATOM   2374 C CD2 . PHE A 1 321 ? -16.142 1.877   25.096  1.00 21.50  ? 301 PHE A CD2 1 
ATOM   2375 C CE1 . PHE A 1 321 ? -14.710 0.403   23.259  1.00 21.53  ? 301 PHE A CE1 1 
ATOM   2376 C CE2 . PHE A 1 321 ? -15.090 2.444   24.399  1.00 22.54  ? 301 PHE A CE2 1 
ATOM   2377 C CZ  . PHE A 1 321 ? -14.370 1.712   23.498  1.00 21.74  ? 301 PHE A CZ  1 
ATOM   2378 N N   . TRP A 1 322 ? -17.055 1.326   28.293  1.00 21.51  ? 302 TRP A N   1 
ATOM   2379 C CA  . TRP A 1 322 ? -16.292 2.367   28.949  1.00 22.05  ? 302 TRP A CA  1 
ATOM   2380 C C   . TRP A 1 322 ? -15.647 1.910   30.249  1.00 23.00  ? 302 TRP A C   1 
ATOM   2381 O O   . TRP A 1 322 ? -14.626 2.483   30.643  1.00 23.72  ? 302 TRP A O   1 
ATOM   2382 C CB  . TRP A 1 322 ? -17.131 3.637   29.133  1.00 22.69  ? 302 TRP A CB  1 
ATOM   2383 C CG  . TRP A 1 322 ? -17.360 4.341   27.837  1.00 22.97  ? 302 TRP A CG  1 
ATOM   2384 C CD1 . TRP A 1 322 ? -18.532 4.497   27.167  1.00 24.32  ? 302 TRP A CD1 1 
ATOM   2385 C CD2 . TRP A 1 322 ? -16.355 5.023   27.063  1.00 23.27  ? 302 TRP A CD2 1 
ATOM   2386 N NE1 . TRP A 1 322 ? -18.332 5.206   26.016  1.00 25.35  ? 302 TRP A NE1 1 
ATOM   2387 C CE2 . TRP A 1 322 ? -17.007 5.552   25.924  1.00 24.20  ? 302 TRP A CE2 1 
ATOM   2388 C CE3 . TRP A 1 322 ? -14.973 5.200   27.206  1.00 21.73  ? 302 TRP A CE3 1 
ATOM   2389 C CZ2 . TRP A 1 322 ? -16.300 6.237   24.929  1.00 22.55  ? 302 TRP A CZ2 1 
ATOM   2390 C CZ3 . TRP A 1 322 ? -14.285 5.891   26.241  1.00 22.26  ? 302 TRP A CZ3 1 
ATOM   2391 C CH2 . TRP A 1 322 ? -14.943 6.419   25.123  1.00 21.92  ? 302 TRP A CH2 1 
ATOM   2392 N N   . GLU A 1 323 ? -16.201 0.870   30.890  1.00 23.67  ? 303 GLU A N   1 
ATOM   2393 C CA  . GLU A 1 323 ? -15.551 0.277   32.052  1.00 25.88  ? 303 GLU A CA  1 
ATOM   2394 C C   . GLU A 1 323 ? -14.281 -0.466  31.619  1.00 23.43  ? 303 GLU A C   1 
ATOM   2395 O O   . GLU A 1 323 ? -13.273 -0.440  32.318  1.00 22.73  ? 303 GLU A O   1 
ATOM   2396 C CB  . GLU A 1 323 ? -16.507 -0.685  32.767  1.00 27.82  ? 303 GLU A CB  1 
ATOM   2397 C CG  . GLU A 1 323 ? -15.976 -1.170  34.089  1.00 31.52  ? 303 GLU A CG  1 
ATOM   2398 C CD  . GLU A 1 323 ? -16.910 -2.141  34.771  1.00 35.66  ? 303 GLU A CD  1 
ATOM   2399 O OE1 . GLU A 1 323 ? -18.149 -1.937  34.639  1.00 38.82  ? 303 GLU A OE1 1 
ATOM   2400 O OE2 . GLU A 1 323 ? -16.387 -3.129  35.390  1.00 42.52  ? 303 GLU A OE2 1 
ATOM   2401 N N   . VAL A 1 324 ? -14.328 -1.127  30.456  1.00 22.98  ? 304 VAL A N   1 
ATOM   2402 C CA  . VAL A 1 324 ? -13.153 -1.814  29.918  1.00 22.69  ? 304 VAL A CA  1 
ATOM   2403 C C   . VAL A 1 324 ? -12.050 -0.782  29.635  1.00 21.38  ? 304 VAL A C   1 
ATOM   2404 O O   . VAL A 1 324 ? -10.896 -0.954  30.009  1.00 22.35  ? 304 VAL A O   1 
ATOM   2405 C CB  . VAL A 1 324 ? -13.500 -2.594  28.639  1.00 23.02  ? 304 VAL A CB  1 
ATOM   2406 C CG1 . VAL A 1 324 ? -12.266 -3.293  28.057  1.00 23.32  ? 304 VAL A CG1 1 
ATOM   2407 C CG2 . VAL A 1 324 ? -14.619 -3.603  28.895  1.00 25.25  ? 304 VAL A CG2 1 
ATOM   2408 N N   . ALA A 1 325 ? -12.421 0.315   28.963  1.00 20.30  ? 305 ALA A N   1 
ATOM   2409 C CA  . ALA A 1 325 ? -11.467 1.363   28.625  1.00 20.27  ? 305 ALA A CA  1 
ATOM   2410 C C   . ALA A 1 325 ? -10.800 1.958   29.872  1.00 20.74  ? 305 ALA A C   1 
ATOM   2411 O O   . ALA A 1 325 ? -9.581  2.152   29.894  1.00 21.33  ? 305 ALA A O   1 
ATOM   2412 C CB  . ALA A 1 325 ? -12.214 2.404   27.847  1.00 20.45  ? 305 ALA A CB  1 
ATOM   2413 N N   . ARG A 1 326 ? -11.616 2.296   30.885  1.00 22.27  ? 306 ARG A N   1 
ATOM   2414 C CA  . ARG A 1 326 ? -11.117 2.865   32.132  1.00 22.43  ? 306 ARG A CA  1 
ATOM   2415 C C   . ARG A 1 326 ? -10.267 1.840   32.884  1.00 22.77  ? 306 ARG A C   1 
ATOM   2416 O O   . ARG A 1 326 ? -9.238  2.166   33.445  1.00 21.88  ? 306 ARG A O   1 
ATOM   2417 C CB  . ARG A 1 326 ? -12.267 3.366   33.014  1.00 22.52  ? 306 ARG A CB  1 
ATOM   2418 C CG  . ARG A 1 326 ? -11.780 4.130   34.239  1.00 26.99  ? 306 ARG A CG  1 
ATOM   2419 C CD  . ARG A 1 326 ? -12.924 4.765   35.023  1.00 31.52  ? 306 ARG A CD  1 
ATOM   2420 N NE  . ARG A 1 326 ? -13.985 3.819   35.354  1.00 35.19  ? 306 ARG A NE  1 
ATOM   2421 C CZ  . ARG A 1 326 ? -15.158 3.701   34.720  1.00 39.03  ? 306 ARG A CZ  1 
ATOM   2422 N NH1 . ARG A 1 326 ? -15.443 4.389   33.615  1.00 37.65  ? 306 ARG A NH1 1 
ATOM   2423 N NH2 . ARG A 1 326 ? -16.035 2.823   35.169  1.00 40.53  ? 306 ARG A NH2 1 
ATOM   2424 N N   . ALA A 1 327 ? -10.656 0.558   32.841  1.00 21.57  ? 307 ALA A N   1 
ATOM   2425 C CA  . ALA A 1 327 ? -9.803  -0.443  33.469  1.00 24.58  ? 307 ALA A CA  1 
ATOM   2426 C C   . ALA A 1 327 ? -8.411  -0.476  32.821  1.00 22.43  ? 307 ALA A C   1 
ATOM   2427 O O   . ALA A 1 327 ? -7.389  -0.613  33.507  1.00 22.40  ? 307 ALA A O   1 
ATOM   2428 C CB  . ALA A 1 327 ? -10.441 -1.811  33.407  1.00 23.94  ? 307 ALA A CB  1 
ATOM   2429 N N   . LEU A 1 328 ? -8.387  -0.395  31.492  1.00 20.60  ? 308 LEU A N   1 
ATOM   2430 C CA  . LEU A 1 328 ? -7.106  -0.413  30.737  1.00 22.41  ? 308 LEU A CA  1 
ATOM   2431 C C   . LEU A 1 328 ? -6.222  0.784   31.153  1.00 21.77  ? 308 LEU A C   1 
ATOM   2432 O O   . LEU A 1 328 ? -5.065  0.566   31.479  1.00 22.06  ? 308 LEU A O   1 
ATOM   2433 C CB  . LEU A 1 328 ? -7.401  -0.430  29.233  1.00 21.99  ? 308 LEU A CB  1 
ATOM   2434 C CG  . LEU A 1 328 ? -6.224  -0.617  28.272  1.00 23.27  ? 308 LEU A CG  1 
ATOM   2435 C CD1 . LEU A 1 328 ? -5.475  0.666   27.951  1.00 23.11  ? 308 LEU A CD1 1 
ATOM   2436 C CD2 . LEU A 1 328 ? -5.277  -1.725  28.674  1.00 24.89  ? 308 LEU A CD2 1 
ATOM   2437 N N   . THR A 1 329 ? -6.771  1.998   31.095  1.00 21.60  ? 309 THR A N   1 
ATOM   2438 C CA  . THR A 1 329 ? -5.941  3.148   31.419  1.00 22.75  ? 309 THR A CA  1 
ATOM   2439 C C   . THR A 1 329 ? -5.527  3.206   32.887  1.00 22.09  ? 309 THR A C   1 
ATOM   2440 O O   . THR A 1 329 ? -4.401  3.607   33.180  1.00 24.02  ? 309 THR A O   1 
ATOM   2441 C CB  . THR A 1 329 ? -6.597  4.449   30.936  1.00 23.21  ? 309 THR A CB  1 
ATOM   2442 O OG1 . THR A 1 329 ? -7.929  4.569   31.410  1.00 23.83  ? 309 THR A OG1 1 
ATOM   2443 C CG2 . THR A 1 329 ? -6.590  4.530   29.432  1.00 25.21  ? 309 THR A CG2 1 
ATOM   2444 N N   . ASP A 1 330 ? -6.402  2.783   33.809  1.00 23.05  ? 310 ASP A N   1 
ATOM   2445 C CA  . ASP A 1 330 ? -6.054  2.715   35.222  1.00 24.53  ? 310 ASP A CA  1 
ATOM   2446 C C   . ASP A 1 330 ? -4.908  1.722   35.460  1.00 24.12  ? 310 ASP A C   1 
ATOM   2447 O O   . ASP A 1 330 ? -3.953  2.010   36.192  1.00 27.17  ? 310 ASP A O   1 
ATOM   2448 C CB  . ASP A 1 330 ? -7.274  2.352   36.065  1.00 25.86  ? 310 ASP A CB  1 
ATOM   2449 C CG  . ASP A 1 330 ? -8.279  3.483   36.267  1.00 28.73  ? 310 ASP A CG  1 
ATOM   2450 O OD1 . ASP A 1 330 ? -7.946  4.645   35.907  1.00 32.55  ? 310 ASP A OD1 1 
ATOM   2451 O OD2 . ASP A 1 330 ? -9.387  3.205   36.786  1.00 31.06  ? 310 ASP A OD2 1 
ATOM   2452 N N   . ASP A 1 331 ? -4.996  0.530   34.852  1.00 24.09  ? 311 ASP A N   1 
ATOM   2453 C CA  . ASP A 1 331 ? -3.972  -0.473  35.068  1.00 26.62  ? 311 ASP A CA  1 
ATOM   2454 C C   . ASP A 1 331 ? -2.655  -0.063  34.406  1.00 25.19  ? 311 ASP A C   1 
ATOM   2455 O O   . ASP A 1 331 ? -1.575  -0.212  34.969  1.00 25.01  ? 311 ASP A O   1 
ATOM   2456 C CB  . ASP A 1 331 ? -4.445  -1.831  34.561  1.00 26.64  ? 311 ASP A CB  1 
ATOM   2457 C CG  . ASP A 1 331 ? -3.548  -2.948  35.072  1.00 30.36  ? 311 ASP A CG  1 
ATOM   2458 O OD1 . ASP A 1 331 ? -3.345  -3.017  36.296  1.00 35.42  ? 311 ASP A OD1 1 
ATOM   2459 O OD2 . ASP A 1 331 ? -3.018  -3.694  34.261  1.00 32.10  ? 311 ASP A OD2 1 
ATOM   2460 N N   . LEU A 1 332 ? -2.744  0.475   33.189  1.00 23.40  ? 312 LEU A N   1 
ATOM   2461 C CA  . LEU A 1 332 ? -1.550  0.839   32.472  1.00 23.32  ? 312 LEU A CA  1 
ATOM   2462 C C   . LEU A 1 332 ? -0.832  1.970   33.212  1.00 23.47  ? 312 LEU A C   1 
ATOM   2463 O O   . LEU A 1 332 ? 0.404   2.001   33.278  1.00 25.82  ? 312 LEU A O   1 
ATOM   2464 C CB  . LEU A 1 332 ? -1.953  1.257   31.066  1.00 25.09  ? 312 LEU A CB  1 
ATOM   2465 C CG  . LEU A 1 332 ? -0.831  1.364   30.052  1.00 28.07  ? 312 LEU A CG  1 
ATOM   2466 C CD1 . LEU A 1 332 ? 0.001   0.079   29.973  1.00 29.78  ? 312 LEU A CD1 1 
ATOM   2467 C CD2 . LEU A 1 332 ? -1.420  1.674   28.682  1.00 28.84  ? 312 LEU A CD2 1 
ATOM   2468 N N   . GLY A 1 333 ? -1.619  2.893   33.775  1.00 23.79  ? 313 GLY A N   1 
ATOM   2469 C CA  . GLY A 1 333 ? -1.047  4.003   34.513  1.00 26.90  ? 313 GLY A CA  1 
ATOM   2470 C C   . GLY A 1 333 ? -0.253  3.527   35.730  1.00 26.77  ? 313 GLY A C   1 
ATOM   2471 O O   . GLY A 1 333 ? 0.843   4.010   36.002  1.00 29.17  ? 313 GLY A O   1 
ATOM   2472 N N   . GLU A 1 334 ? -0.796  2.548   36.458  1.00 25.88  ? 314 GLU A N   1 
ATOM   2473 C CA  . GLU A 1 334 ? -0.099  1.998   37.615  1.00 27.86  ? 314 GLU A CA  1 
ATOM   2474 C C   . GLU A 1 334 ? 1.141   1.216   37.183  1.00 27.13  ? 314 GLU A C   1 
ATOM   2475 O O   . GLU A 1 334 ? 2.198   1.326   37.808  1.00 26.36  ? 314 GLU A O   1 
ATOM   2476 C CB  . GLU A 1 334 ? -1.049  1.123   38.440  1.00 32.50  ? 314 GLU A CB  1 
ATOM   2477 C CG  . GLU A 1 334 ? -0.392  0.523   39.674  1.00 36.88  ? 314 GLU A CG  1 
ATOM   2478 C CD  . GLU A 1 334 ? 0.121   1.506   40.716  1.00 41.46  ? 314 GLU A CD  1 
ATOM   2479 O OE1 . GLU A 1 334 ? 0.984   1.096   41.500  1.00 46.23  ? 314 GLU A OE1 1 
ATOM   2480 O OE2 . GLU A 1 334 ? -0.346  2.672   40.754  1.00 44.80  ? 314 GLU A OE2 1 
ATOM   2481 N N   . ARG A 1 335 ? 1.020   0.425   36.108  1.00 24.32  ? 315 ARG A N   1 
ATOM   2482 C CA  . ARG A 1 335 ? 2.155   -0.310  35.581  1.00 25.55  ? 315 ARG A CA  1 
ATOM   2483 C C   . ARG A 1 335 ? 3.282   0.632   35.151  1.00 24.98  ? 315 ARG A C   1 
ATOM   2484 O O   . ARG A 1 335 ? 4.447   0.361   35.378  1.00 27.09  ? 315 ARG A O   1 
ATOM   2485 C CB  . ARG A 1 335 ? 1.673   -1.236  34.467  1.00 25.08  ? 315 ARG A CB  1 
ATOM   2486 C CG  . ARG A 1 335 ? 0.819   -2.391  34.985  1.00 26.19  ? 315 ARG A CG  1 
ATOM   2487 C CD  . ARG A 1 335 ? 0.442   -3.296  33.829  1.00 23.82  ? 315 ARG A CD  1 
ATOM   2488 N NE  . ARG A 1 335 ? -0.229  -4.505  34.256  1.00 23.70  ? 315 ARG A NE  1 
ATOM   2489 C CZ  . ARG A 1 335 ? 0.384   -5.681  34.329  1.00 26.05  ? 315 ARG A CZ  1 
ATOM   2490 N NH1 . ARG A 1 335 ? 1.697   -5.750  34.302  1.00 26.30  ? 315 ARG A NH1 1 
ATOM   2491 N NH2 . ARG A 1 335 ? -0.322  -6.781  34.490  1.00 26.70  ? 315 ARG A NH2 1 
ATOM   2492 N N   . ARG A 1 336 ? 2.938   1.762   34.534  1.00 24.98  ? 316 ARG A N   1 
ATOM   2493 C CA  . ARG A 1 336 ? 3.943   2.737   34.134  1.00 27.86  ? 316 ARG A CA  1 
ATOM   2494 C C   . ARG A 1 336 ? 4.648   3.320   35.362  1.00 28.75  ? 316 ARG A C   1 
ATOM   2495 O O   . ARG A 1 336 ? 5.867   3.477   35.349  1.00 30.81  ? 316 ARG A O   1 
ATOM   2496 C CB  . ARG A 1 336 ? 3.297   3.828   33.283  1.00 29.85  ? 316 ARG A CB  1 
ATOM   2497 C CG  . ARG A 1 336 ? 2.897   3.341   31.896  1.00 33.57  ? 316 ARG A CG  1 
ATOM   2498 C CD  . ARG A 1 336 ? 2.273   4.452   31.080  0.70 35.04  ? 316 ARG A CD  1 
ATOM   2499 N NE  . ARG A 1 336 ? 3.249   5.525   30.979  1.00 41.17  ? 316 ARG A NE  1 
ATOM   2500 C CZ  . ARG A 1 336 ? 3.429   6.308   29.922  1.00 44.44  ? 316 ARG A CZ  1 
ATOM   2501 N NH1 . ARG A 1 336 ? 2.519   6.386   28.967  1.00 47.18  ? 316 ARG A NH1 1 
ATOM   2502 N NH2 . ARG A 1 336 ? 4.504   7.068   29.865  1.00 46.73  ? 316 ARG A NH2 1 
ATOM   2503 N N   . ARG A 1 337 ? 3.891   3.634   36.424  1.00 31.27  ? 317 ARG A N   1 
ATOM   2504 C CA  . ARG A 1 337 ? 4.484   4.151   37.655  1.00 33.70  ? 317 ARG A CA  1 
ATOM   2505 C C   . ARG A 1 337 ? 5.434   3.124   38.283  1.00 33.60  ? 317 ARG A C   1 
ATOM   2506 O O   . ARG A 1 337 ? 6.376   3.515   38.953  1.00 32.37  ? 317 ARG A O   1 
ATOM   2507 C CB  . ARG A 1 337 ? 3.407   4.560   38.665  1.00 36.80  ? 317 ARG A CB  1 
ATOM   2508 C CG  . ARG A 1 337 ? 2.667   5.841   38.310  1.00 39.88  ? 317 ARG A CG  1 
ATOM   2509 C CD  . ARG A 1 337 ? 1.781   6.283   39.459  1.00 41.29  ? 317 ARG A CD  1 
ATOM   2510 N NE  . ARG A 1 337 ? 0.627   5.411   39.642  1.00 40.31  ? 317 ARG A NE  1 
ATOM   2511 C CZ  . ARG A 1 337 ? -0.500  5.465   38.933  1.00 41.66  ? 317 ARG A CZ  1 
ATOM   2512 N NH1 . ARG A 1 337 ? -0.624  6.308   37.925  1.00 43.12  ? 317 ARG A NH1 1 
ATOM   2513 N NH2 . ARG A 1 337 ? -1.495  4.636   39.207  1.00 44.92  ? 317 ARG A NH2 1 
ATOM   2514 N N   . GLN A 1 338 ? 5.176   1.822   38.071  1.00 32.34  ? 318 GLN A N   1 
ATOM   2515 C CA  . GLN A 1 338 ? 6.015   0.746   38.583  1.00 32.52  ? 318 GLN A CA  1 
ATOM   2516 C C   . GLN A 1 338 ? 7.136   0.364   37.607  1.00 29.99  ? 318 GLN A C   1 
ATOM   2517 O O   . GLN A 1 338 ? 7.902   -0.551  37.904  1.00 34.12  ? 318 GLN A O   1 
ATOM   2518 C CB  . GLN A 1 338 ? 5.151   -0.479  38.898  1.00 31.12  ? 318 GLN A CB  1 
ATOM   2519 C CG  . GLN A 1 338 ? 4.162   -0.254  40.029  1.00 35.53  ? 318 GLN A CG  1 
ATOM   2520 C CD  . GLN A 1 338 ? 4.808   0.059   41.336  1.00 49.21  ? 318 GLN A CD  1 
ATOM   2521 O OE1 . GLN A 1 338 ? 5.847   -0.487  41.702  0.50 58.67  ? 318 GLN A OE1 1 
ATOM   2522 N NE2 . GLN A 1 338 ? 4.199   0.984   42.058  0.50 50.64  ? 318 GLN A NE2 1 
ATOM   2523 N N   . GLY A 1 339 ? 7.229   1.033   36.446  1.00 27.31  ? 319 GLY A N   1 
ATOM   2524 C CA  . GLY A 1 339 ? 8.321   0.862   35.497  1.00 25.52  ? 319 GLY A CA  1 
ATOM   2525 C C   . GLY A 1 339 ? 8.279   -0.474  34.754  1.00 25.42  ? 319 GLY A C   1 
ATOM   2526 O O   . GLY A 1 339 ? 9.325   -0.988  34.369  1.00 25.10  ? 319 GLY A O   1 
ATOM   2527 N N   . HIS A 1 340 ? 7.072   -0.990  34.497  1.00 24.20  ? 320 HIS A N   1 
ATOM   2528 C CA  . HIS A 1 340 ? 6.940   -2.276  33.817  1.00 23.90  ? 320 HIS A CA  1 
ATOM   2529 C C   . HIS A 1 340 ? 7.565   -2.258  32.422  1.00 23.07  ? 320 HIS A C   1 
ATOM   2530 O O   . HIS A 1 340 ? 8.033   -3.285  31.921  1.00 24.26  ? 320 HIS A O   1 
ATOM   2531 C CB  . HIS A 1 340 ? 5.479   -2.724  33.782  1.00 23.99  ? 320 HIS A CB  1 
ATOM   2532 C CG  . HIS A 1 340 ? 4.988   -3.171  35.125  1.00 25.22  ? 320 HIS A CG  1 
ATOM   2533 N ND1 . HIS A 1 340 ? 3.791   -3.817  35.300  1.00 26.21  ? 320 HIS A ND1 1 
ATOM   2534 C CD2 . HIS A 1 340 ? 5.543   -3.101  36.351  1.00 25.86  ? 320 HIS A CD2 1 
ATOM   2535 C CE1 . HIS A 1 340 ? 3.631   -4.100  36.583  1.00 26.94  ? 320 HIS A CE1 1 
ATOM   2536 N NE2 . HIS A 1 340 ? 4.706   -3.706  37.238  1.00 26.39  ? 320 HIS A NE2 1 
ATOM   2537 N N   . HIS A 1 341 ? 7.584   -1.087  31.780  1.00 22.68  ? 321 HIS A N   1 
ATOM   2538 C CA  . HIS A 1 341 ? 8.235   -0.942  30.491  1.00 24.83  ? 321 HIS A CA  1 
ATOM   2539 C C   . HIS A 1 341 ? 9.739   -1.228  30.600  1.00 23.72  ? 321 HIS A C   1 
ATOM   2540 O O   . HIS A 1 341 ? 10.296  -1.945  29.770  1.00 24.92  ? 321 HIS A O   1 
ATOM   2541 C CB  . HIS A 1 341 ? 7.914   0.436   29.903  1.00 24.59  ? 321 HIS A CB  1 
ATOM   2542 C CG  . HIS A 1 341 ? 8.063   1.551   30.858  1.00 26.47  ? 321 HIS A CG  1 
ATOM   2543 N ND1 . HIS A 1 341 ? 7.192   1.814   31.887  1.00 29.90  ? 321 HIS A ND1 1 
ATOM   2544 C CD2 . HIS A 1 341 ? 8.963   2.534   30.870  1.00 29.77  ? 321 HIS A CD2 1 
ATOM   2545 C CE1 . HIS A 1 341 ? 7.590   2.915   32.527  1.00 31.06  ? 321 HIS A CE1 1 
ATOM   2546 N NE2 . HIS A 1 341 ? 8.671   3.360   31.934  1.00 31.79  ? 321 HIS A NE2 1 
ATOM   2547 N N   . PHE A 1 342 ? 10.387  -0.723  31.658  1.00 23.13  ? 322 PHE A N   1 
ATOM   2548 C CA  . PHE A 1 342 ? 11.805  -0.983  31.872  1.00 23.04  ? 322 PHE A CA  1 
ATOM   2549 C C   . PHE A 1 342 ? 12.074  -2.443  32.254  1.00 23.07  ? 322 PHE A C   1 
ATOM   2550 O O   . PHE A 1 342 ? 13.147  -2.958  31.961  1.00 26.06  ? 322 PHE A O   1 
ATOM   2551 C CB  . PHE A 1 342 ? 12.397  -0.018  32.902  1.00 25.63  ? 322 PHE A CB  1 
ATOM   2552 C CG  . PHE A 1 342 ? 12.618  1.374   32.381  1.00 26.55  ? 322 PHE A CG  1 
ATOM   2553 C CD1 . PHE A 1 342 ? 13.283  1.583   31.180  1.00 28.75  ? 322 PHE A CD1 1 
ATOM   2554 C CD2 . PHE A 1 342 ? 12.115  2.472   33.058  1.00 27.93  ? 322 PHE A CD2 1 
ATOM   2555 C CE1 . PHE A 1 342 ? 13.437  2.863   30.672  1.00 28.51  ? 322 PHE A CE1 1 
ATOM   2556 C CE2 . PHE A 1 342 ? 12.320  3.757   32.573  1.00 28.12  ? 322 PHE A CE2 1 
ATOM   2557 C CZ  . PHE A 1 342 ? 12.984  3.950   31.393  1.00 29.11  ? 322 PHE A CZ  1 
ATOM   2558 N N   . ASN A 1 343 ? 11.092  -3.105  32.880  1.00 24.50  ? 323 ASN A N   1 
ATOM   2559 C CA  . ASN A 1 343 ? 11.220  -4.511  33.218  1.00 23.40  ? 323 ASN A CA  1 
ATOM   2560 C C   . ASN A 1 343 ? 11.328  -5.360  31.953  1.00 23.16  ? 323 ASN A C   1 
ATOM   2561 O O   . ASN A 1 343 ? 12.063  -6.341  31.920  1.00 24.45  ? 323 ASN A O   1 
ATOM   2562 C CB  . ASN A 1 343 ? 10.067  -4.970  34.103  1.00 24.33  ? 323 ASN A CB  1 
ATOM   2563 C CG  . ASN A 1 343 ? 10.080  -4.394  35.513  1.00 26.95  ? 323 ASN A CG  1 
ATOM   2564 O OD1 . ASN A 1 343 ? 11.094  -3.908  36.014  1.00 26.47  ? 323 ASN A OD1 1 
ATOM   2565 N ND2 . ASN A 1 343 ? 8.939   -4.459  36.182  1.00 29.99  ? 323 ASN A ND2 1 
ATOM   2566 N N   . LEU A 1 344 ? 10.573  -5.016  30.903  1.00 23.50  ? 324 LEU A N   1 
ATOM   2567 C CA  . LEU A 1 344 ? 10.703  -5.736  29.652  1.00 24.26  ? 324 LEU A CA  1 
ATOM   2568 C C   . LEU A 1 344 ? 12.099  -5.544  29.045  1.00 22.87  ? 324 LEU A C   1 
ATOM   2569 O O   . LEU A 1 344 ? 12.692  -6.460  28.466  1.00 22.56  ? 324 LEU A O   1 
ATOM   2570 C CB  . LEU A 1 344 ? 9.588   -5.346  28.685  1.00 26.30  ? 324 LEU A CB  1 
ATOM   2571 C CG  . LEU A 1 344 ? 9.663   -6.104  27.355  1.00 29.80  ? 324 LEU A CG  1 
ATOM   2572 C CD1 . LEU A 1 344 ? 9.385   -7.593  27.535  1.00 33.11  ? 324 LEU A CD1 1 
ATOM   2573 C CD2 . LEU A 1 344 ? 8.719   -5.523  26.319  1.00 33.01  ? 324 LEU A CD2 1 
ATOM   2574 N N   . VAL A 1 345 ? 12.631  -4.327  29.118  1.00 23.45  ? 325 VAL A N   1 
ATOM   2575 C CA  . VAL A 1 345 ? 13.984  -4.075  28.648  1.00 23.71  ? 325 VAL A CA  1 
ATOM   2576 C C   . VAL A 1 345 ? 14.958  -4.979  29.422  1.00 24.12  ? 325 VAL A C   1 
ATOM   2577 O O   . VAL A 1 345 ? 15.846  -5.609  28.839  1.00 24.90  ? 325 VAL A O   1 
ATOM   2578 C CB  . VAL A 1 345 ? 14.343  -2.584  28.810  1.00 24.02  ? 325 VAL A CB  1 
ATOM   2579 C CG1 . VAL A 1 345 ? 15.800  -2.304  28.515  1.00 24.98  ? 325 VAL A CG1 1 
ATOM   2580 C CG2 . VAL A 1 345 ? 13.444  -1.690  27.961  1.00 25.03  ? 325 VAL A CG2 1 
ATOM   2581 N N   . THR A 1 346 ? 14.768  -5.071  30.746  1.00 25.38  ? 326 THR A N   1 
ATOM   2582 C CA  . THR A 1 346 ? 15.615  -5.923  31.566  1.00 25.73  ? 326 THR A CA  1 
ATOM   2583 C C   . THR A 1 346 ? 15.529  -7.375  31.098  1.00 27.05  ? 326 THR A C   1 
ATOM   2584 O O   . THR A 1 346 ? 16.553  -8.035  30.955  1.00 28.30  ? 326 THR A O   1 
ATOM   2585 C CB  . THR A 1 346 ? 15.228  -5.796  33.036  1.00 27.47  ? 326 THR A CB  1 
ATOM   2586 O OG1 . THR A 1 346 ? 15.501  -4.440  33.416  1.00 28.20  ? 326 THR A OG1 1 
ATOM   2587 C CG2 . THR A 1 346 ? 15.943  -6.801  33.911  1.00 29.58  ? 326 THR A CG2 1 
ATOM   2588 N N   . LEU A 1 347 ? 14.308  -7.860  30.851  1.00 23.80  ? 327 LEU A N   1 
ATOM   2589 C CA  . LEU A 1 347 ? 14.136  -9.237  30.415  1.00 24.89  ? 327 LEU A CA  1 
ATOM   2590 C C   . LEU A 1 347 ? 14.889  -9.482  29.112  1.00 25.59  ? 327 LEU A C   1 
ATOM   2591 O O   . LEU A 1 347 ? 15.655  -10.448 28.976  1.00 26.53  ? 327 LEU A O   1 
ATOM   2592 C CB  . LEU A 1 347 ? 12.646  -9.528  30.250  1.00 24.35  ? 327 LEU A CB  1 
ATOM   2593 C CG  . LEU A 1 347 ? 12.284  -10.870 29.610  1.00 29.32  ? 327 LEU A CG  1 
ATOM   2594 C CD1 . LEU A 1 347 ? 12.863  -12.065 30.366  1.00 31.81  ? 327 LEU A CD1 1 
ATOM   2595 C CD2 . LEU A 1 347 ? 10.765  -10.964 29.521  1.00 33.13  ? 327 LEU A CD2 1 
ATOM   2596 N N   . VAL A 1 348 ? 14.654  -8.624  28.121  1.00 24.57  ? 328 VAL A N   1 
ATOM   2597 C CA  . VAL A 1 348 ? 15.256  -8.844  26.817  1.00 24.60  ? 328 VAL A CA  1 
ATOM   2598 C C   . VAL A 1 348 ? 16.771  -8.682  26.927  1.00 25.44  ? 328 VAL A C   1 
ATOM   2599 O O   . VAL A 1 348 ? 17.517  -9.452  26.316  1.00 28.23  ? 328 VAL A O   1 
ATOM   2600 C CB  . VAL A 1 348 ? 14.675  -7.911  25.750  1.00 24.86  ? 328 VAL A CB  1 
ATOM   2601 C CG1 . VAL A 1 348 ? 15.420  -8.026  24.428  1.00 25.34  ? 328 VAL A CG1 1 
ATOM   2602 C CG2 . VAL A 1 348 ? 13.183  -8.118  25.558  1.00 27.34  ? 328 VAL A CG2 1 
ATOM   2603 N N   . ALA A 1 349 ? 17.239  -7.676  27.675  1.00 25.52  ? 329 ALA A N   1 
ATOM   2604 C CA  . ALA A 1 349 ? 18.676  -7.478  27.794  1.00 27.88  ? 329 ALA A CA  1 
ATOM   2605 C C   . ALA A 1 349 ? 19.351  -8.689  28.446  1.00 30.36  ? 329 ALA A C   1 
ATOM   2606 O O   . ALA A 1 349 ? 20.518  -8.982  28.181  1.00 33.34  ? 329 ALA A O   1 
ATOM   2607 C CB  . ALA A 1 349 ? 18.952  -6.187  28.535  1.00 29.05  ? 329 ALA A CB  1 
ATOM   2608 N N   . SER A 1 350 ? 18.597  -9.412  29.274  1.00 30.28  ? 330 SER A N   1 
ATOM   2609 C CA  . SER A 1 350 ? 19.172  -10.511 30.027  1.00 32.92  ? 330 SER A CA  1 
ATOM   2610 C C   . SER A 1 350 ? 19.125  -11.788 29.208  1.00 33.56  ? 330 SER A C   1 
ATOM   2611 O O   . SER A 1 350 ? 19.993  -12.644 29.390  1.00 37.69  ? 330 SER A O   1 
ATOM   2612 C CB  . SER A 1 350 ? 18.465  -10.684 31.340  1.00 37.37  ? 330 SER A CB  1 
ATOM   2613 O OG  . SER A 1 350 ? 18.487  -9.452  32.059  1.00 45.88  ? 330 SER A OG  1 
ATOM   2614 N N   . ALA A 1 351 ? 18.133  -11.905 28.313  1.00 29.96  ? 331 ALA A N   1 
ATOM   2615 C CA  . ALA A 1 351 ? 17.860  -13.188 27.674  1.00 30.64  ? 331 ALA A CA  1 
ATOM   2616 C C   . ALA A 1 351 ? 18.079  -13.185 26.166  1.00 29.01  ? 331 ALA A C   1 
ATOM   2617 O O   . ALA A 1 351 ? 18.047  -14.235 25.553  1.00 31.34  ? 331 ALA A O   1 
ATOM   2618 C CB  . ALA A 1 351 ? 16.456  -13.646 27.998  1.00 30.80  ? 331 ALA A CB  1 
ATOM   2619 N N   . ALA A 1 352 ? 18.351  -12.040 25.554  1.00 27.99  ? 332 ALA A N   1 
ATOM   2620 C CA  . ALA A 1 352 ? 18.516  -11.981 24.108  1.00 27.88  ? 332 ALA A CA  1 
ATOM   2621 C C   . ALA A 1 352 ? 19.598  -12.966 23.670  1.00 29.28  ? 332 ALA A C   1 
ATOM   2622 O O   . ALA A 1 352 ? 20.714  -12.937 24.163  1.00 30.10  ? 332 ALA A O   1 
ATOM   2623 C CB  . ALA A 1 352 ? 18.832  -10.566 23.697  1.00 29.17  ? 332 ALA A CB  1 
ATOM   2624 N N   . PRO A 1 353 ? 19.288  -13.896 22.750  1.00 29.85  ? 333 PRO A N   1 
ATOM   2625 C CA  . PRO A 1 353 ? 20.273  -14.860 22.245  1.00 30.19  ? 333 PRO A CA  1 
ATOM   2626 C C   . PRO A 1 353 ? 21.469  -14.206 21.557  1.00 30.17  ? 333 PRO A C   1 
ATOM   2627 O O   . PRO A 1 353 ? 21.327  -13.083 21.074  1.00 29.15  ? 333 PRO A O   1 
ATOM   2628 C CB  . PRO A 1 353 ? 19.491  -15.632 21.180  1.00 30.54  ? 333 PRO A CB  1 
ATOM   2629 C CG  . PRO A 1 353 ? 18.070  -15.485 21.586  1.00 31.79  ? 333 PRO A CG  1 
ATOM   2630 C CD  . PRO A 1 353 ? 17.959  -14.102 22.172  1.00 31.74  ? 333 PRO A CD  1 
ATOM   2631 N N   . ARG A 1 354 ? 22.608  -14.908 21.530  1.00 33.30  ? 334 ARG A N   1 
ATOM   2632 C CA  . ARG A 1 354 ? 23.851  -14.415 20.960  1.00 34.15  ? 334 ARG A CA  1 
ATOM   2633 C C   . ARG A 1 354 ? 23.838  -14.495 19.432  1.00 35.03  ? 334 ARG A C   1 
ATOM   2634 O O   . ARG A 1 354 ? 24.575  -13.737 18.795  1.00 35.10  ? 334 ARG A O   1 
ATOM   2635 C CB  . ARG A 1 354 ? 25.042  -15.216 21.511  1.00 39.10  ? 334 ARG A CB  1 
ATOM   2636 C CG  . ARG A 1 354 ? 25.399  -14.872 22.951  1.00 43.30  ? 334 ARG A CG  1 
ATOM   2637 C CD  . ARG A 1 354 ? 26.365  -15.881 23.548  0.00 42.46  ? 334 ARG A CD  1 
ATOM   2638 N NE  . ARG A 1 354 ? 26.440  -15.810 25.000  0.00 42.12  ? 334 ARG A NE  1 
ATOM   2639 C CZ  . ARG A 1 354 ? 26.932  -16.773 25.771  0.00 41.30  ? 334 ARG A CZ  1 
ATOM   2640 N NH1 . ARG A 1 354 ? 27.355  -17.899 25.227  0.00 41.00  ? 334 ARG A NH1 1 
ATOM   2641 N NH2 . ARG A 1 354 ? 26.984  -16.617 27.082  0.00 41.25  ? 334 ARG A NH2 1 
ATOM   2642 N N   . CYS A 1 355 ? 23.066  -15.441 18.858  1.00 31.19  ? 335 CYS A N   1 
ATOM   2643 C CA  . CYS A 1 355 ? 23.095  -15.687 17.420  1.00 32.26  ? 335 CYS A CA  1 
ATOM   2644 C C   . CYS A 1 355 ? 21.853  -16.442 16.943  1.00 30.88  ? 335 CYS A C   1 
ATOM   2645 O O   . CYS A 1 355 ? 21.039  -16.906 17.741  1.00 31.14  ? 335 CYS A O   1 
ATOM   2646 C CB  . CYS A 1 355 ? 24.353  -16.456 17.034  1.00 34.27  ? 335 CYS A CB  1 
ATOM   2647 S SG  . CYS A 1 355 ? 24.387  -18.170 17.619  1.00 39.76  ? 335 CYS A SG  1 
ATOM   2648 N N   . MET A 1 356 ? 21.709  -16.525 15.616  1.00 30.19  ? 336 MET A N   1 
ATOM   2649 C CA  . MET A 1 356 ? 20.530  -17.097 14.990  1.00 30.37  ? 336 MET A CA  1 
ATOM   2650 C C   . MET A 1 356 ? 20.404  -18.578 15.353  1.00 34.31  ? 336 MET A C   1 
ATOM   2651 O O   . MET A 1 356 ? 19.307  -19.054 15.631  1.00 32.17  ? 336 MET A O   1 
ATOM   2652 C CB  . MET A 1 356 ? 20.606  -16.937 13.467  1.00 31.79  ? 336 MET A CB  1 
ATOM   2653 C CG  . MET A 1 356 ? 20.338  -15.497 13.039  1.00 32.34  ? 336 MET A CG  1 
ATOM   2654 S SD  . MET A 1 356 ? 18.627  -15.012 13.373  1.00 32.40  ? 336 MET A SD  1 
ATOM   2655 C CE  . MET A 1 356 ? 17.775  -16.029 12.162  1.00 33.90  ? 336 MET A CE  1 
ATOM   2656 N N   . ALA A 1 357 ? 21.532  -19.292 15.357  1.00 35.31  ? 337 ALA A N   1 
ATOM   2657 C CA  . ALA A 1 357 ? 21.523  -20.713 15.659  1.00 36.34  ? 337 ALA A CA  1 
ATOM   2658 C C   . ALA A 1 357 ? 20.913  -20.979 17.043  1.00 34.74  ? 337 ALA A C   1 
ATOM   2659 O O   . ALA A 1 357 ? 20.313  -22.009 17.264  1.00 37.75  ? 337 ALA A O   1 
ATOM   2660 C CB  . ALA A 1 357 ? 22.928  -21.271 15.559  1.00 37.35  ? 337 ALA A CB  1 
ATOM   2661 N N   . ASP A 1 358 ? 21.076  -20.053 17.987  1.00 33.58  ? 338 ASP A N   1 
ATOM   2662 C CA  . ASP A 1 358 ? 20.655  -20.263 19.360  1.00 31.80  ? 338 ASP A CA  1 
ATOM   2663 C C   . ASP A 1 358 ? 19.344  -19.559 19.696  1.00 34.38  ? 338 ASP A C   1 
ATOM   2664 O O   . ASP A 1 358 ? 18.947  -19.594 20.866  1.00 34.12  ? 338 ASP A O   1 
ATOM   2665 C CB  . ASP A 1 358 ? 21.713  -19.730 20.330  1.00 40.99  ? 338 ASP A CB  1 
ATOM   2666 C CG  . ASP A 1 358 ? 23.029  -20.480 20.257  1.00 46.34  ? 338 ASP A CG  1 
ATOM   2667 O OD1 . ASP A 1 358 ? 23.037  -21.591 19.705  1.00 52.77  ? 338 ASP A OD1 1 
ATOM   2668 O OD2 . ASP A 1 358 ? 24.031  -19.929 20.738  1.00 53.66  ? 338 ASP A OD2 1 
ATOM   2669 N N   . ALA A 1 359 ? 18.705  -18.901 18.707  1.00 31.27  ? 339 ALA A N   1 
ATOM   2670 C CA  . ALA A 1 359 ? 17.646  -17.952 18.997  1.00 30.84  ? 339 ALA A CA  1 
ATOM   2671 C C   . ALA A 1 359 ? 16.266  -18.590 19.182  1.00 30.51  ? 339 ALA A C   1 
ATOM   2672 O O   . ALA A 1 359 ? 15.371  -17.972 19.727  1.00 29.56  ? 339 ALA A O   1 
ATOM   2673 C CB  . ALA A 1 359 ? 17.599  -16.899 17.906  1.00 30.08  ? 339 ALA A CB  1 
ATOM   2674 N N   . ARG A 1 360 ? 16.070  -19.857 18.823  1.00 30.91  ? 340 ARG A N   1 
ATOM   2675 C CA  . ARG A 1 360 ? 14.707  -20.359 18.718  1.00 32.17  ? 340 ARG A CA  1 
ATOM   2676 C C   . ARG A 1 360 ? 14.022  -20.462 20.083  1.00 29.62  ? 340 ARG A C   1 
ATOM   2677 O O   . ARG A 1 360 ? 12.857  -20.074 20.203  1.00 29.65  ? 340 ARG A O   1 
ATOM   2678 C CB  . ARG A 1 360 ? 14.698  -21.650 17.917  1.00 33.34  ? 340 ARG A CB  1 
ATOM   2679 C CG  . ARG A 1 360 ? 14.916  -21.396 16.440  1.00 36.48  ? 340 ARG A CG  1 
ATOM   2680 C CD  . ARG A 1 360 ? 15.045  -22.679 15.663  0.50 36.86  ? 340 ARG A CD  1 
ATOM   2681 N NE  . ARG A 1 360 ? 15.312  -22.365 14.273  0.60 40.72  ? 340 ARG A NE  1 
ATOM   2682 C CZ  . ARG A 1 360 ? 14.389  -22.074 13.361  1.00 42.13  ? 340 ARG A CZ  1 
ATOM   2683 N NH1 . ARG A 1 360 ? 13.104  -22.110 13.663  1.00 46.57  ? 340 ARG A NH1 1 
ATOM   2684 N NH2 . ARG A 1 360 ? 14.760  -21.811 12.122  0.60 40.29  ? 340 ARG A NH2 1 
ATOM   2685 N N   . PRO A 1 361 ? 14.678  -20.983 21.141  1.00 31.24  ? 341 PRO A N   1 
ATOM   2686 C CA  . PRO A 1 361 ? 14.049  -21.061 22.463  1.00 30.79  ? 341 PRO A CA  1 
ATOM   2687 C C   . PRO A 1 361 ? 13.485  -19.730 22.948  1.00 30.23  ? 341 PRO A C   1 
ATOM   2688 O O   . PRO A 1 361 ? 12.343  -19.697 23.408  1.00 29.17  ? 341 PRO A O   1 
ATOM   2689 C CB  . PRO A 1 361 ? 15.166  -21.653 23.358  1.00 32.52  ? 341 PRO A CB  1 
ATOM   2690 C CG  . PRO A 1 361 ? 15.989  -22.489 22.398  0.20 32.26  ? 341 PRO A CG  1 
ATOM   2691 C CD  . PRO A 1 361 ? 15.989  -21.676 21.118  1.00 33.92  ? 341 PRO A CD  1 
ATOM   2692 N N   . PHE A 1 362 ? 14.261  -18.646 22.821  1.00 30.62  ? 342 PHE A N   1 
ATOM   2693 C CA  . PHE A 1 362 ? 13.783  -17.362 23.329  1.00 31.02  ? 342 PHE A CA  1 
ATOM   2694 C C   . PHE A 1 362 ? 12.614  -16.856 22.485  1.00 30.61  ? 342 PHE A C   1 
ATOM   2695 O O   . PHE A 1 362 ? 11.656  -16.304 23.017  1.00 29.39  ? 342 PHE A O   1 
ATOM   2696 C CB  . PHE A 1 362 ? 14.883  -16.302 23.403  1.00 30.84  ? 342 PHE A CB  1 
ATOM   2697 C CG  . PHE A 1 362 ? 14.446  -15.007 24.042  1.00 32.30  ? 342 PHE A CG  1 
ATOM   2698 C CD1 . PHE A 1 362 ? 14.061  -14.954 25.373  1.00 32.10  ? 342 PHE A CD1 1 
ATOM   2699 C CD2 . PHE A 1 362 ? 14.434  -13.827 23.302  1.00 31.06  ? 342 PHE A CD2 1 
ATOM   2700 C CE1 . PHE A 1 362 ? 13.660  -13.754 25.951  1.00 32.48  ? 342 PHE A CE1 1 
ATOM   2701 C CE2 . PHE A 1 362 ? 14.041  -12.627 23.873  1.00 29.41  ? 342 PHE A CE2 1 
ATOM   2702 C CZ  . PHE A 1 362 ? 13.657  -12.589 25.200  1.00 32.36  ? 342 PHE A CZ  1 
ATOM   2703 N N   . MET A 1 363 ? 12.692  -17.038 21.161  1.00 28.47  ? 343 MET A N   1 
ATOM   2704 C CA  . MET A 1 363 ? 11.614  -16.581 20.295  1.00 27.17  ? 343 MET A CA  1 
ATOM   2705 C C   . MET A 1 363 ? 10.340  -17.359 20.635  1.00 27.28  ? 343 MET A C   1 
ATOM   2706 O O   . MET A 1 363 ? 9.261   -16.773 20.667  1.00 28.29  ? 343 MET A O   1 
ATOM   2707 C CB  . MET A 1 363 ? 11.961  -16.719 18.806  1.00 25.51  ? 343 MET A CB  1 
ATOM   2708 C CG  . MET A 1 363 ? 13.123  -15.840 18.371  1.00 24.05  ? 343 MET A CG  1 
ATOM   2709 S SD  . MET A 1 363 ? 12.979  -14.091 18.816  1.00 21.57  ? 343 MET A SD  1 
ATOM   2710 C CE  . MET A 1 363 ? 14.455  -13.471 18.007  0.38 20.27  ? 343 MET A CE  1 
ATOM   2711 N N   . ALA A 1 364 ? 10.469  -18.655 20.982  1.00 27.71  ? 344 ALA A N   1 
ATOM   2712 C CA  . ALA A 1 364 ? 9.281   -19.449 21.264  1.00 29.99  ? 344 ALA A CA  1 
ATOM   2713 C C   . ALA A 1 364 ? 8.661   -19.021 22.594  1.00 27.66  ? 344 ALA A C   1 
ATOM   2714 O O   . ALA A 1 364 ? 7.449   -19.038 22.773  1.00 32.54  ? 344 ALA A O   1 
ATOM   2715 C CB  . ALA A 1 364 ? 9.638   -20.915 21.244  1.00 29.43  ? 344 ALA A CB  1 
ATOM   2716 N N   . PHE A 1 365 ? 9.522   -18.699 23.554  1.00 30.83  ? 345 PHE A N   1 
ATOM   2717 C CA  . PHE A 1 365 ? 9.071   -18.211 24.843  1.00 32.38  ? 345 PHE A CA  1 
ATOM   2718 C C   . PHE A 1 365 ? 8.366   -16.861 24.667  1.00 31.55  ? 345 PHE A C   1 
ATOM   2719 O O   . PHE A 1 365 ? 7.282   -16.657 25.200  1.00 29.74  ? 345 PHE A O   1 
ATOM   2720 C CB  . PHE A 1 365 ? 10.256  -18.095 25.806  1.00 35.81  ? 345 PHE A CB  1 
ATOM   2721 C CG  . PHE A 1 365 ? 9.977   -17.280 27.043  1.00 36.95  ? 345 PHE A CG  1 
ATOM   2722 C CD1 . PHE A 1 365 ? 9.236   -17.816 28.095  1.00 38.07  ? 345 PHE A CD1 1 
ATOM   2723 C CD2 . PHE A 1 365 ? 10.430  -15.968 27.143  1.00 37.49  ? 345 PHE A CD2 1 
ATOM   2724 C CE1 . PHE A 1 365 ? 8.991   -17.066 29.239  1.00 38.92  ? 345 PHE A CE1 1 
ATOM   2725 C CE2 . PHE A 1 365 ? 10.146  -15.208 28.271  0.80 38.66  ? 345 PHE A CE2 1 
ATOM   2726 C CZ  . PHE A 1 365 ? 9.434   -15.759 29.315  0.80 38.56  ? 345 PHE A CZ  1 
ATOM   2727 N N   . MET A 1 366 ? 8.964   -15.939 23.911  1.00 30.20  ? 346 MET A N   1 
ATOM   2728 C CA  . MET A 1 366 ? 8.351   -14.620 23.759  1.00 30.56  ? 346 MET A CA  1 
ATOM   2729 C C   . MET A 1 366 ? 7.031   -14.738 22.991  1.00 31.42  ? 346 MET A C   1 
ATOM   2730 O O   . MET A 1 366 ? 6.058   -14.031 23.280  1.00 32.25  ? 346 MET A O   1 
ATOM   2731 C CB  . MET A 1 366 ? 9.290   -13.641 23.031  1.00 29.95  ? 346 MET A CB  1 
ATOM   2732 C CG  . MET A 1 366 ? 10.474  -13.210 23.898  1.00 32.86  ? 346 MET A CG  1 
ATOM   2733 S SD  . MET A 1 366 ? 9.978   -12.301 25.399  1.00 35.87  ? 346 MET A SD  1 
ATOM   2734 C CE  . MET A 1 366 ? 9.501   -10.718 24.703  0.60 31.54  ? 346 MET A CE  1 
ATOM   2735 N N   . GLU A 1 367 ? 6.992   -15.667 22.024  1.00 30.89  ? 347 GLU A N   1 
ATOM   2736 C CA  . GLU A 1 367 ? 5.777   -15.947 21.266  1.00 33.91  ? 347 GLU A CA  1 
ATOM   2737 C C   . GLU A 1 367 ? 4.649   -16.419 22.188  1.00 33.73  ? 347 GLU A C   1 
ATOM   2738 O O   . GLU A 1 367 ? 3.502   -15.971 22.019  1.00 30.99  ? 347 GLU A O   1 
ATOM   2739 C CB  . GLU A 1 367 ? 6.034   -16.965 20.139  1.00 32.65  ? 347 GLU A CB  1 
ATOM   2740 C CG  . GLU A 1 367 ? 4.770   -17.540 19.545  1.00 34.08  ? 347 GLU A CG  1 
ATOM   2741 C CD  . GLU A 1 367 ? 4.872   -18.094 18.133  1.00 32.96  ? 347 GLU A CD  1 
ATOM   2742 O OE1 . GLU A 1 367 ? 5.967   -18.019 17.531  1.00 33.74  ? 347 GLU A OE1 1 
ATOM   2743 O OE2 . GLU A 1 367 ? 3.841   -18.581 17.622  1.00 34.83  ? 347 GLU A OE2 1 
ATOM   2744 N N   . ALA A 1 368 ? 4.962   -17.354 23.099  1.00 32.49  ? 348 ALA A N   1 
ATOM   2745 C CA  . ALA A 1 368 ? 3.944   -17.968 23.955  1.00 32.37  ? 348 ALA A CA  1 
ATOM   2746 C C   . ALA A 1 368 ? 3.577   -17.095 25.167  1.00 33.93  ? 348 ALA A C   1 
ATOM   2747 O O   . ALA A 1 368 ? 2.461   -17.198 25.664  1.00 36.35  ? 348 ALA A O   1 
ATOM   2748 C CB  . ALA A 1 368 ? 4.347   -19.385 24.395  1.00 33.53  ? 348 ALA A CB  1 
ATOM   2749 N N   . GLU A 1 369 ? 4.484   -16.249 25.664  1.00 30.19  ? 349 GLU A N   1 
ATOM   2750 C CA  . GLU A 1 369 ? 4.301   -15.639 26.981  1.00 33.76  ? 349 GLU A CA  1 
ATOM   2751 C C   . GLU A 1 369 ? 4.487   -14.121 26.960  1.00 35.96  ? 349 GLU A C   1 
ATOM   2752 O O   . GLU A 1 369 ? 4.126   -13.457 27.935  1.00 38.01  ? 349 GLU A O   1 
ATOM   2753 C CB  . GLU A 1 369 ? 5.292   -16.240 27.990  1.00 38.26  ? 349 GLU A CB  1 
ATOM   2754 C CG  . GLU A 1 369 ? 5.072   -17.722 28.268  1.00 40.76  ? 349 GLU A CG  1 
ATOM   2755 C CD  . GLU A 1 369 ? 5.685   -18.236 29.564  0.30 46.54  ? 349 GLU A CD  1 
ATOM   2756 O OE1 . GLU A 1 369 ? 5.634   -17.503 30.576  0.30 49.08  ? 349 GLU A OE1 1 
ATOM   2757 O OE2 . GLU A 1 369 ? 6.181   -19.390 29.573  0.00 48.19  ? 349 GLU A OE2 1 
ATOM   2758 N N   . GLY A 1 370 ? 5.051   -13.568 25.882  1.00 33.89  ? 350 GLY A N   1 
ATOM   2759 C CA  . GLY A 1 370 ? 5.390   -12.155 25.860  1.00 35.47  ? 350 GLY A CA  1 
ATOM   2760 C C   . GLY A 1 370 ? 4.192   -11.260 25.542  1.00 38.75  ? 350 GLY A C   1 
ATOM   2761 O O   . GLY A 1 370 ? 3.158   -11.739 25.057  1.00 41.02  ? 350 GLY A O   1 
ATOM   2762 N N   . PRO A 1 371 ? 4.317   -9.928  25.774  1.00 36.86  ? 351 PRO A N   1 
ATOM   2763 C CA  . PRO A 1 371 ? 3.191   -9.006  25.619  1.00 37.06  ? 351 PRO A CA  1 
ATOM   2764 C C   . PRO A 1 371 ? 2.836   -8.540  24.198  1.00 37.82  ? 351 PRO A C   1 
ATOM   2765 O O   . PRO A 1 371 ? 1.746   -7.997  24.006  1.00 37.02  ? 351 PRO A O   1 
ATOM   2766 C CB  . PRO A 1 371 ? 3.607   -7.821  26.523  0.80 35.90  ? 351 PRO A CB  1 
ATOM   2767 C CG  . PRO A 1 371 ? 5.125   -7.806  26.488  1.00 35.60  ? 351 PRO A CG  1 
ATOM   2768 C CD  . PRO A 1 371 ? 5.524   -9.265  26.296  1.00 36.61  ? 351 PRO A CD  1 
ATOM   2769 N N   . ILE A 1 372 ? 3.697   -8.816  23.198  1.00 33.87  ? 352 ILE A N   1 
ATOM   2770 C CA  . ILE A 1 372 ? 3.581   -8.199  21.879  1.00 34.08  ? 352 ILE A CA  1 
ATOM   2771 C C   . ILE A 1 372 ? 2.612   -8.966  20.959  1.00 31.21  ? 352 ILE A C   1 
ATOM   2772 O O   . ILE A 1 372 ? 2.275   -8.497  19.862  1.00 35.24  ? 352 ILE A O   1 
ATOM   2773 C CB  . ILE A 1 372 ? 4.992   -8.008  21.281  1.00 36.39  ? 352 ILE A CB  1 
ATOM   2774 C CG1 . ILE A 1 372 ? 5.846   -7.135  22.209  1.00 38.14  ? 352 ILE A CG1 1 
ATOM   2775 C CG2 . ILE A 1 372 ? 4.943   -7.459  19.853  1.00 37.70  ? 352 ILE A CG2 1 
ATOM   2776 C CD1 . ILE A 1 372 ? 7.326   -7.048  21.837  1.00 38.68  ? 352 ILE A CD1 1 
ATOM   2777 N N   . ASN A 1 373 ? 2.118   -10.129 21.424  1.00 28.97  ? 353 ASN A N   1 
ATOM   2778 C CA  . ASN A 1 373 ? 1.150   -10.967 20.709  1.00 25.35  ? 353 ASN A CA  1 
ATOM   2779 C C   . ASN A 1 373 ? -0.005  -10.180 20.095  1.00 22.48  ? 353 ASN A C   1 
ATOM   2780 O O   . ASN A 1 373 ? -0.280  -10.333 18.909  1.00 22.83  ? 353 ASN A O   1 
ATOM   2781 C CB  . ASN A 1 373 ? 0.562   -12.009 21.660  1.00 26.08  ? 353 ASN A CB  1 
ATOM   2782 C CG  . ASN A 1 373 ? -0.581  -12.828 21.074  1.00 23.34  ? 353 ASN A CG  1 
ATOM   2783 O OD1 . ASN A 1 373 ? -1.751  -12.513 21.258  1.00 22.99  ? 353 ASN A OD1 1 
ATOM   2784 N ND2 . ASN A 1 373 ? -0.282  -13.847 20.299  1.00 25.41  ? 353 ASN A ND2 1 
ATOM   2785 N N   . LEU A 1 374 ? -0.714  -9.416  20.939  1.00 22.61  ? 354 LEU A N   1 
ATOM   2786 C CA  . LEU A 1 374 ? -1.749  -8.485  20.504  1.00 21.57  ? 354 LEU A CA  1 
ATOM   2787 C C   . LEU A 1 374 ? -1.380  -7.130  21.103  1.00 22.71  ? 354 LEU A C   1 
ATOM   2788 O O   . LEU A 1 374 ? -1.246  -7.028  22.308  1.00 22.27  ? 354 LEU A O   1 
ATOM   2789 C CB  . LEU A 1 374 ? -3.127  -8.961  21.003  1.00 22.88  ? 354 LEU A CB  1 
ATOM   2790 C CG  . LEU A 1 374 ? -4.340  -8.039  20.770  1.00 22.07  ? 354 LEU A CG  1 
ATOM   2791 C CD1 . LEU A 1 374 ? -4.723  -7.947  19.303  1.00 21.93  ? 354 LEU A CD1 1 
ATOM   2792 C CD2 . LEU A 1 374 ? -5.561  -8.496  21.569  1.00 23.62  ? 354 LEU A CD2 1 
ATOM   2793 N N   . CYS A 1 375 ? -1.199  -6.113  20.254  1.00 23.15  ? 355 CYS A N   1 
ATOM   2794 C CA  . CYS A 1 375 ? -0.637  -4.853  20.711  1.00 22.93  ? 355 CYS A CA  1 
ATOM   2795 C C   . CYS A 1 375 ? -1.418  -3.680  20.172  1.00 20.45  ? 355 CYS A C   1 
ATOM   2796 O O   . CYS A 1 375 ? -1.830  -3.675  19.024  1.00 20.57  ? 355 CYS A O   1 
ATOM   2797 C CB  . CYS A 1 375 ? 0.790   -4.627  20.248  1.00 25.41  ? 355 CYS A CB  1 
ATOM   2798 S SG  . CYS A 1 375 ? 1.944   -5.558  21.261  1.00 30.21  ? 355 CYS A SG  1 
ATOM   2799 N N   . SER A 1 376 ? -1.606  -2.699  21.056  1.00 20.63  ? 356 SER A N   1 
ATOM   2800 C CA  . SER A 1 376 ? -2.207  -1.423  20.711  1.00 19.43  ? 356 SER A CA  1 
ATOM   2801 C C   . SER A 1 376 ? -1.113  -0.352  20.876  1.00 19.14  ? 356 SER A C   1 
ATOM   2802 O O   . SER A 1 376 ? -0.766  0.024   21.989  1.00 20.97  ? 356 SER A O   1 
ATOM   2803 C CB  . SER A 1 376 ? -3.420  -1.187  21.568  1.00 21.70  ? 356 SER A CB  1 
ATOM   2804 O OG  . SER A 1 376 ? -4.031  0.055   21.284  1.00 20.36  ? 356 SER A OG  1 
ATOM   2805 N N   . SER A 1 377 ? -0.510  0.032   19.749  1.00 19.59  ? 357 SER A N   1 
ATOM   2806 C CA  . SER A 1 377 ? 0.709   0.814   19.731  1.00 17.87  ? 357 SER A CA  1 
ATOM   2807 C C   . SER A 1 377 ? 0.387   2.265   19.332  1.00 17.99  ? 357 SER A C   1 
ATOM   2808 O O   . SER A 1 377 ? 0.186   2.539   18.164  1.00 19.19  ? 357 SER A O   1 
ATOM   2809 C CB  . SER A 1 377 ? 1.719   0.229   18.768  1.00 21.32  ? 357 SER A CB  1 
ATOM   2810 O OG  . SER A 1 377 ? 2.947   0.944   18.833  1.00 23.75  ? 357 SER A OG  1 
ATOM   2811 N N   . ASN A 1 378 ? 0.326   3.144   20.322  1.00 19.16  ? 358 ASN A N   1 
ATOM   2812 C CA  . ASN A 1 378 ? -0.291  4.458   20.193  1.00 18.96  ? 358 ASN A CA  1 
ATOM   2813 C C   . ASN A 1 378 ? 0.718   5.512   20.591  1.00 18.88  ? 358 ASN A C   1 
ATOM   2814 O O   . ASN A 1 378 ? 1.156   5.520   21.740  1.00 20.56  ? 358 ASN A O   1 
ATOM   2815 C CB  . ASN A 1 378 ? -1.522  4.511   21.085  1.00 19.68  ? 358 ASN A CB  1 
ATOM   2816 C CG  . ASN A 1 378 ? -2.395  5.743   20.962  1.00 20.85  ? 358 ASN A CG  1 
ATOM   2817 O OD1 . ASN A 1 378 ? -2.029  6.729   20.313  1.00 20.81  ? 358 ASN A OD1 1 
ATOM   2818 N ND2 . ASN A 1 378 ? -3.579  5.677   21.554  1.00 21.36  ? 358 ASN A ND2 1 
ATOM   2819 N N   . ILE A 1 379 ? 1.056   6.419   19.658  1.00 18.13  ? 359 ILE A N   1 
ATOM   2820 C CA  . ILE A 1 379 ? 1.997   7.488   19.998  1.00 19.85  ? 359 ILE A CA  1 
ATOM   2821 C C   . ILE A 1 379 ? 1.265   8.786   20.329  1.00 19.83  ? 359 ILE A C   1 
ATOM   2822 O O   . ILE A 1 379 ? 1.942   9.783   20.532  1.00 23.56  ? 359 ILE A O   1 
ATOM   2823 C CB  . ILE A 1 379 ? 3.035   7.687   18.876  1.00 22.21  ? 359 ILE A CB  1 
ATOM   2824 C CG1 . ILE A 1 379 ? 2.402   8.185   17.580  1.00 21.84  ? 359 ILE A CG1 1 
ATOM   2825 C CG2 . ILE A 1 379 ? 3.813   6.395   18.634  1.00 20.70  ? 359 ILE A CG2 1 
ATOM   2826 C CD1 . ILE A 1 379 ? 3.386   8.585   16.532  1.00 20.62  ? 359 ILE A CD1 1 
ATOM   2827 N N   . GLY A 1 380 ? -0.063  8.785   20.434  1.00 19.94  ? 360 GLY A N   1 
ATOM   2828 C CA  . GLY A 1 380 ? -0.798  10.008  20.757  1.00 20.18  ? 360 GLY A CA  1 
ATOM   2829 C C   . GLY A 1 380 ? -0.832  10.963  19.584  1.00 19.26  ? 360 GLY A C   1 
ATOM   2830 O O   . GLY A 1 380 ? -0.888  10.565  18.426  1.00 21.75  ? 360 GLY A O   1 
ATOM   2831 N N   . ARG A 1 381 ? -0.809  12.261  19.899  1.00 18.95  ? 361 ARG A N   1 
ATOM   2832 C CA  . ARG A 1 381 ? -0.764  13.240  18.837  1.00 19.71  ? 361 ARG A CA  1 
ATOM   2833 C C   . ARG A 1 381 ? 0.679   13.407  18.363  1.00 19.22  ? 361 ARG A C   1 
ATOM   2834 O O   . ARG A 1 381 ? 1.559   13.759  19.139  1.00 20.67  ? 361 ARG A O   1 
ATOM   2835 C CB  . ARG A 1 381 ? -1.334  14.583  19.291  1.00 21.64  ? 361 ARG A CB  1 
ATOM   2836 C CG  . ARG A 1 381 ? -1.219  15.605  18.160  1.00 23.44  ? 361 ARG A CG  1 
ATOM   2837 C CD  . ARG A 1 381 ? -2.084  16.816  18.343  1.00 26.61  ? 361 ARG A CD  1 
ATOM   2838 N NE  . ARG A 1 381 ? -3.512  16.534  18.401  1.00 27.28  ? 361 ARG A NE  1 
ATOM   2839 C CZ  . ARG A 1 381 ? -4.287  16.397  17.345  1.00 31.42  ? 361 ARG A CZ  1 
ATOM   2840 N NH1 . ARG A 1 381 ? -3.770  16.485  16.129  1.00 32.64  ? 361 ARG A NH1 1 
ATOM   2841 N NH2 . ARG A 1 381 ? -5.573  16.168  17.513  1.00 35.31  ? 361 ARG A NH2 1 
ATOM   2842 N N   . TYR A 1 382 ? 0.892   13.112  17.077  1.00 18.74  ? 362 TYR A N   1 
ATOM   2843 C CA  . TYR A 1 382 ? 2.211   13.392  16.477  1.00 18.24  ? 362 TYR A CA  1 
ATOM   2844 C C   . TYR A 1 382 ? 2.085   14.787  15.858  1.00 19.38  ? 362 TYR A C   1 
ATOM   2845 O O   . TYR A 1 382 ? 1.182   15.018  15.069  1.00 19.30  ? 362 TYR A O   1 
ATOM   2846 C CB  . TYR A 1 382 ? 2.719   12.332  15.484  1.00 16.88  ? 362 TYR A CB  1 
ATOM   2847 C CG  . TYR A 1 382 ? 4.098   12.744  15.057  1.00 17.97  ? 362 TYR A CG  1 
ATOM   2848 C CD1 . TYR A 1 382 ? 4.273   13.618  14.001  1.00 19.45  ? 362 TYR A CD1 1 
ATOM   2849 C CD2 . TYR A 1 382 ? 5.203   12.420  15.823  1.00 17.99  ? 362 TYR A CD2 1 
ATOM   2850 C CE1 . TYR A 1 382 ? 5.525   14.092  13.661  1.00 20.05  ? 362 TYR A CE1 1 
ATOM   2851 C CE2 . TYR A 1 382 ? 6.464   12.883  15.496  1.00 19.59  ? 362 TYR A CE2 1 
ATOM   2852 C CZ  . TYR A 1 382 ? 6.623   13.727  14.412  1.00 19.73  ? 362 TYR A CZ  1 
ATOM   2853 O OH  . TYR A 1 382 ? 7.851   14.211  14.071  1.00 22.50  ? 362 TYR A OH  1 
ATOM   2854 N N   . PRO A 1 383 ? 2.999   15.705  16.207  1.00 19.62  ? 363 PRO A N   1 
ATOM   2855 C CA  . PRO A 1 383 ? 2.856   17.109  15.802  1.00 19.28  ? 363 PRO A CA  1 
ATOM   2856 C C   . PRO A 1 383 ? 3.348   17.399  14.381  1.00 19.61  ? 363 PRO A C   1 
ATOM   2857 O O   . PRO A 1 383 ? 4.187   18.257  14.132  1.00 23.18  ? 363 PRO A O   1 
ATOM   2858 C CB  . PRO A 1 383 ? 3.734   17.774  16.882  1.00 20.19  ? 363 PRO A CB  1 
ATOM   2859 C CG  . PRO A 1 383 ? 4.906   16.822  17.027  1.00 19.95  ? 363 PRO A CG  1 
ATOM   2860 C CD  . PRO A 1 383 ? 4.179   15.495  17.070  1.00 19.13  ? 363 PRO A CD  1 
ATOM   2861 N N   . PHE A 1 384 ? 2.781   16.710  13.401  1.00 18.17  ? 364 PHE A N   1 
ATOM   2862 C CA  . PHE A 1 384 ? 3.230   16.894  12.040  1.00 18.05  ? 364 PHE A CA  1 
ATOM   2863 C C   . PHE A 1 384 ? 2.727   18.231  11.521  1.00 18.51  ? 364 PHE A C   1 
ATOM   2864 O O   . PHE A 1 384 ? 1.522   18.468  11.557  1.00 20.50  ? 364 PHE A O   1 
ATOM   2865 C CB  . PHE A 1 384 ? 2.778   15.738  11.142  1.00 17.64  ? 364 PHE A CB  1 
ATOM   2866 C CG  . PHE A 1 384 ? 3.773   15.410  10.068  1.00 17.75  ? 364 PHE A CG  1 
ATOM   2867 C CD1 . PHE A 1 384 ? 4.003   16.240  8.983   1.00 18.14  ? 364 PHE A CD1 1 
ATOM   2868 C CD2 . PHE A 1 384 ? 4.488   14.216  10.129  1.00 17.03  ? 364 PHE A CD2 1 
ATOM   2869 C CE1 . PHE A 1 384 ? 4.971   15.933  8.028   1.00 17.92  ? 364 PHE A CE1 1 
ATOM   2870 C CE2 . PHE A 1 384 ? 5.419   13.887  9.158   1.00 17.79  ? 364 PHE A CE2 1 
ATOM   2871 C CZ  . PHE A 1 384 ? 5.676   14.738  8.109   1.00 18.83  ? 364 PHE A CZ  1 
ATOM   2872 N N   . PRO A 1 385 ? 3.615   19.138  11.063  1.00 19.03  ? 365 PRO A N   1 
ATOM   2873 C CA  . PRO A 1 385 ? 3.131   20.427  10.548  1.00 21.33  ? 365 PRO A CA  1 
ATOM   2874 C C   . PRO A 1 385 ? 2.140   20.266  9.397   1.00 20.79  ? 365 PRO A C   1 
ATOM   2875 O O   . PRO A 1 385 ? 2.279   19.364  8.574   1.00 19.29  ? 365 PRO A O   1 
ATOM   2876 C CB  . PRO A 1 385 ? 4.429   21.091  10.070  1.00 22.28  ? 365 PRO A CB  1 
ATOM   2877 C CG  . PRO A 1 385 ? 5.503   20.480  10.956  1.00 20.86  ? 365 PRO A CG  1 
ATOM   2878 C CD  . PRO A 1 385 ? 5.074   19.036  11.082  1.00 18.94  ? 365 PRO A CD  1 
ATOM   2879 N N   . GLU A 1 386 ? 1.163   21.169  9.325   1.00 19.97  ? 366 GLU A N   1 
ATOM   2880 C CA  . GLU A 1 386 ? 0.237   21.274  8.205   1.00 23.50  ? 366 GLU A CA  1 
ATOM   2881 C C   . GLU A 1 386 ? 0.916   21.896  6.986   1.00 22.15  ? 366 GLU A C   1 
ATOM   2882 O O   . GLU A 1 386 ? 0.499   21.624  5.846   1.00 20.63  ? 366 GLU A O   1 
ATOM   2883 C CB  . GLU A 1 386 ? -0.968  22.161  8.574   1.00 25.93  ? 366 GLU A CB  1 
ATOM   2884 C CG  . GLU A 1 386 ? -1.799  21.575  9.696   1.00 32.21  ? 366 GLU A CG  1 
ATOM   2885 C CD  . GLU A 1 386 ? -3.184  22.179  9.855   0.50 34.99  ? 366 GLU A CD  1 
ATOM   2886 O OE1 . GLU A 1 386 ? -3.555  23.044  9.049   1.00 33.43  ? 366 GLU A OE1 1 
ATOM   2887 O OE2 . GLU A 1 386 ? -3.891  21.761  10.787  0.50 46.18  ? 366 GLU A OE2 1 
ATOM   2888 N N   . ARG A 1 387 ? 1.892   22.787  7.238   1.00 21.78  ? 367 ARG A N   1 
ATOM   2889 C CA  . ARG A 1 387 ? 2.607   23.483  6.188   1.00 21.50  ? 367 ARG A CA  1 
ATOM   2890 C C   . ARG A 1 387 ? 4.104   23.445  6.466   1.00 22.68  ? 367 ARG A C   1 
ATOM   2891 O O   . ARG A 1 387 ? 4.516   23.669  7.602   1.00 22.89  ? 367 ARG A O   1 
ATOM   2892 C CB  . ARG A 1 387 ? 2.178   24.955  6.131   1.00 24.23  ? 367 ARG A CB  1 
ATOM   2893 C CG  . ARG A 1 387 ? 0.693   25.186  5.901   1.00 27.88  ? 367 ARG A CG  1 
ATOM   2894 C CD  . ARG A 1 387 ? 0.297   26.621  5.655   0.30 28.71  ? 367 ARG A CD  1 
ATOM   2895 N NE  . ARG A 1 387 ? -1.092  26.724  5.228   0.30 33.42  ? 367 ARG A NE  1 
ATOM   2896 C CZ  . ARG A 1 387 ? -1.696  27.876  4.959   0.30 34.87  ? 367 ARG A CZ  1 
ATOM   2897 N NH1 . ARG A 1 387 ? -2.980  27.907  4.655   0.30 34.67  ? 367 ARG A NH1 1 
ATOM   2898 N NH2 . ARG A 1 387 ? -1.011  29.003  5.042   0.00 37.27  ? 367 ARG A NH2 1 
ATOM   2899 N N   . ILE A 1 388 ? 4.885   23.137  5.418   1.00 21.05  ? 368 ILE A N   1 
ATOM   2900 C CA  . ILE A 1 388 ? 6.346   23.181  5.464   1.00 21.42  ? 368 ILE A CA  1 
ATOM   2901 C C   . ILE A 1 388 ? 6.795   23.911  4.208   1.00 22.42  ? 368 ILE A C   1 
ATOM   2902 O O   . ILE A 1 388 ? 6.594   23.427  3.098   1.00 23.83  ? 368 ILE A O   1 
ATOM   2903 C CB  . ILE A 1 388 ? 6.985   21.778  5.550   1.00 22.16  ? 368 ILE A CB  1 
ATOM   2904 C CG1 . ILE A 1 388 ? 6.618   21.110  6.873   1.00 21.46  ? 368 ILE A CG1 1 
ATOM   2905 C CG2 . ILE A 1 388 ? 8.499   21.817  5.351   1.00 23.75  ? 368 ILE A CG2 1 
ATOM   2906 C CD1 . ILE A 1 388 ? 6.971   19.622  6.936   1.00 22.75  ? 368 ILE A CD1 1 
ATOM   2907 N N   . GLY A 1 389 ? 7.350   25.112  4.369   1.00 24.91  ? 369 GLY A N   1 
ATOM   2908 C CA  . GLY A 1 389 ? 7.608   25.944  3.201   1.00 27.55  ? 369 GLY A CA  1 
ATOM   2909 C C   . GLY A 1 389 ? 6.327   26.158  2.398   1.00 26.86  ? 369 GLY A C   1 
ATOM   2910 O O   . GLY A 1 389 ? 5.292   26.467  2.980   1.00 28.51  ? 369 GLY A O   1 
ATOM   2911 N N   . ALA A 1 390 ? 6.385   25.906  1.079   1.00 26.43  ? 370 ALA A N   1 
ATOM   2912 C CA  . ALA A 1 390 ? 5.230   26.059  0.213   1.00 27.46  ? 370 ALA A CA  1 
ATOM   2913 C C   . ALA A 1 390 ? 4.399   24.781  0.121   1.00 26.07  ? 370 ALA A C   1 
ATOM   2914 O O   . ALA A 1 390 ? 3.427   24.740  -0.622  1.00 28.82  ? 370 ALA A O   1 
ATOM   2915 C CB  . ALA A 1 390 ? 5.690   26.482  -1.158  1.00 30.70  ? 370 ALA A CB  1 
ATOM   2916 N N   . LEU A 1 391 ? 4.763   23.749  0.874   1.00 24.37  ? 371 LEU A N   1 
ATOM   2917 C CA  . LEU A 1 391 ? 4.025   22.487  0.828   1.00 23.14  ? 371 LEU A CA  1 
ATOM   2918 C C   . LEU A 1 391 ? 2.937   22.447  1.894   1.00 22.57  ? 371 LEU A C   1 
ATOM   2919 O O   . LEU A 1 391 ? 3.117   23.005  2.977   1.00 22.94  ? 371 LEU A O   1 
ATOM   2920 C CB  . LEU A 1 391 ? 4.978   21.306  1.058   1.00 21.54  ? 371 LEU A CB  1 
ATOM   2921 C CG  . LEU A 1 391 ? 6.191   21.213  0.139   1.00 23.74  ? 371 LEU A CG  1 
ATOM   2922 C CD1 . LEU A 1 391 ? 7.109   20.106  0.596   1.00 24.63  ? 371 LEU A CD1 1 
ATOM   2923 C CD2 . LEU A 1 391 ? 5.767   21.002  -1.309  1.00 23.42  ? 371 LEU A CD2 1 
ATOM   2924 N N   . ARG A 1 392 ? 1.854   21.706  1.596   1.00 20.76  ? 372 ARG A N   1 
ATOM   2925 C CA  . ARG A 1 392 ? 0.810   21.415  2.562   1.00 20.64  ? 372 ARG A CA  1 
ATOM   2926 C C   . ARG A 1 392 ? 0.820   19.901  2.769   1.00 19.21  ? 372 ARG A C   1 
ATOM   2927 O O   . ARG A 1 392 ? 1.018   19.167  1.814   1.00 21.36  ? 372 ARG A O   1 
ATOM   2928 C CB  . ARG A 1 392 ? -0.561  21.919  2.105   1.00 25.24  ? 372 ARG A CB  1 
ATOM   2929 C CG  . ARG A 1 392 ? -0.641  23.437  2.045   1.00 28.99  ? 372 ARG A CG  1 
ATOM   2930 C CD  . ARG A 1 392 ? -1.959  23.964  1.520   1.00 34.02  ? 372 ARG A CD  1 
ATOM   2931 N NE  . ARG A 1 392 ? -2.583  23.047  0.552   1.00 43.22  ? 372 ARG A NE  1 
ATOM   2932 C CZ  . ARG A 1 392 ? -2.507  23.114  -0.783  1.00 43.68  ? 372 ARG A CZ  1 
ATOM   2933 N NH1 . ARG A 1 392 ? -1.721  23.990  -1.389  1.00 50.88  ? 372 ARG A NH1 1 
ATOM   2934 N NH2 . ARG A 1 392 ? -3.238  22.286  -1.517  1.00 43.26  ? 372 ARG A NH2 1 
ATOM   2935 N N   . LEU A 1 393 ? 0.662   19.488  4.014   1.00 18.56  ? 373 LEU A N   1 
ATOM   2936 C CA  . LEU A 1 393 ? 0.820   18.046  4.338   1.00 16.78  ? 373 LEU A CA  1 
ATOM   2937 C C   . LEU A 1 393 ? -0.468  17.501  4.946   1.00 18.48  ? 373 LEU A C   1 
ATOM   2938 O O   . LEU A 1 393 ? -1.154  18.227  5.655   1.00 18.94  ? 373 LEU A O   1 
ATOM   2939 C CB  . LEU A 1 393 ? 1.984   17.934  5.323   1.00 18.32  ? 373 LEU A CB  1 
ATOM   2940 C CG  . LEU A 1 393 ? 3.396   18.270  4.839   1.00 18.75  ? 373 LEU A CG  1 
ATOM   2941 C CD1 . LEU A 1 393 ? 3.714   17.733  3.467   1.00 21.74  ? 373 LEU A CD1 1 
ATOM   2942 C CD2 . LEU A 1 393 ? 3.685   19.765  4.935   1.00 21.39  ? 373 LEU A CD2 1 
ATOM   2943 N N   . SER A 1 394 ? -0.719  16.198  4.722   1.00 17.72  ? 374 SER A N   1 
ATOM   2944 C CA  . SER A 1 394 ? -1.868  15.545  5.306   1.00 17.73  ? 374 SER A CA  1 
ATOM   2945 C C   . SER A 1 394 ? -1.531  14.061  5.508   1.00 18.27  ? 374 SER A C   1 
ATOM   2946 O O   . SER A 1 394 ? -0.523  13.604  5.004   1.00 18.16  ? 374 SER A O   1 
ATOM   2947 C CB  . SER A 1 394 ? -3.079  15.699  4.442   1.00 19.52  ? 374 SER A CB  1 
ATOM   2948 O OG  . SER A 1 394 ? -2.929  15.002  3.204   1.00 19.70  ? 374 SER A OG  1 
ATOM   2949 N N   . ASP A 1 395 ? -2.416  13.382  6.228   1.00 16.51  ? 375 ASP A N   1 
ATOM   2950 C CA  . ASP A 1 395 ? -2.389  11.934  6.328   1.00 16.27  ? 375 ASP A CA  1 
ATOM   2951 C C   . ASP A 1 395 ? -1.091  11.373  6.928   1.00 16.68  ? 375 ASP A C   1 
ATOM   2952 O O   . ASP A 1 395 ? -0.748  10.197  6.682   1.00 16.39  ? 375 ASP A O   1 
ATOM   2953 C CB  . ASP A 1 395 ? -2.649  11.382  4.936   1.00 16.85  ? 375 ASP A CB  1 
ATOM   2954 C CG  . ASP A 1 395 ? -4.034  11.693  4.427   1.00 19.37  ? 375 ASP A CG  1 
ATOM   2955 O OD1 . ASP A 1 395 ? -4.999  11.012  4.882   1.00 22.82  ? 375 ASP A OD1 1 
ATOM   2956 O OD2 . ASP A 1 395 ? -4.148  12.691  3.623   1.00 22.89  ? 375 ASP A OD2 1 
ATOM   2957 N N   . ALA A 1 396 ? -0.395  12.086  7.805   1.00 15.80  ? 376 ALA A N   1 
ATOM   2958 C CA  . ALA A 1 396 ? 0.804   11.581  8.476   1.00 17.05  ? 376 ALA A CA  1 
ATOM   2959 C C   . ALA A 1 396 ? 0.449   10.462  9.457   1.00 16.61  ? 376 ALA A C   1 
ATOM   2960 O O   . ALA A 1 396 ? -0.399  10.654  10.308  1.00 16.11  ? 376 ALA A O   1 
ATOM   2961 C CB  . ALA A 1 396 ? 1.562   12.684  9.178   1.00 16.45  ? 376 ALA A CB  1 
ATOM   2962 N N   . GLN A 1 397 ? 1.045   9.260   9.280   1.00 16.30  ? 377 GLN A N   1 
ATOM   2963 C CA  . GLN A 1 397 ? 0.660   8.085   10.050  1.00 16.33  ? 377 GLN A CA  1 
ATOM   2964 C C   . GLN A 1 397 ? 1.831   7.097   10.021  1.00 15.69  ? 377 GLN A C   1 
ATOM   2965 O O   . GLN A 1 397 ? 2.833   7.302   9.316   1.00 15.65  ? 377 GLN A O   1 
ATOM   2966 C CB  . GLN A 1 397 ? -0.609  7.442   9.480   1.00 15.90  ? 377 GLN A CB  1 
ATOM   2967 C CG  . GLN A 1 397 ? -0.522  7.038   8.031   1.00 15.40  ? 377 GLN A CG  1 
ATOM   2968 C CD  . GLN A 1 397 ? -1.910  6.840   7.467   1.00 16.82  ? 377 GLN A CD  1 
ATOM   2969 O OE1 . GLN A 1 397 ? -2.624  5.897   7.819   1.00 17.01  ? 377 GLN A OE1 1 
ATOM   2970 N NE2 . GLN A 1 397 ? -2.386  7.790   6.661   1.00 17.72  ? 377 GLN A NE2 1 
ATOM   2971 N N   . PHE A 1 398 ? 1.660   5.979   10.784  1.00 16.78  ? 378 PHE A N   1 
ATOM   2972 C CA  . PHE A 1 398 ? 2.682   4.941   10.825  1.00 15.24  ? 378 PHE A CA  1 
ATOM   2973 C C   . PHE A 1 398 ? 2.034   3.570   10.944  1.00 15.57  ? 378 PHE A C   1 
ATOM   2974 O O   . PHE A 1 398 ? 0.851   3.443   11.221  1.00 17.06  ? 378 PHE A O   1 
ATOM   2975 C CB  . PHE A 1 398 ? 3.740   5.132   11.917  1.00 15.83  ? 378 PHE A CB  1 
ATOM   2976 C CG  . PHE A 1 398 ? 3.369   4.691   13.295  1.00 15.94  ? 378 PHE A CG  1 
ATOM   2977 C CD1 . PHE A 1 398 ? 2.425   5.341   14.066  1.00 17.74  ? 378 PHE A CD1 1 
ATOM   2978 C CD2 . PHE A 1 398 ? 3.959   3.537   13.811  1.00 17.69  ? 378 PHE A CD2 1 
ATOM   2979 C CE1 . PHE A 1 398 ? 2.114   4.902   15.344  1.00 18.64  ? 378 PHE A CE1 1 
ATOM   2980 C CE2 . PHE A 1 398 ? 3.636   3.104   15.077  1.00 19.25  ? 378 PHE A CE2 1 
ATOM   2981 C CZ  . PHE A 1 398 ? 2.709   3.762   15.837  1.00 19.53  ? 378 PHE A CZ  1 
ATOM   2982 N N   . LEU A 1 399 ? 2.872   2.548   10.744  1.00 16.66  ? 379 LEU A N   1 
ATOM   2983 C CA  . LEU A 1 399 ? 2.435   1.137   10.877  1.00 17.65  ? 379 LEU A CA  1 
ATOM   2984 C C   . LEU A 1 399 ? 3.722   0.336   11.130  1.00 19.04  ? 379 LEU A C   1 
ATOM   2985 O O   . LEU A 1 399 ? 4.812   0.858   10.798  1.00 18.47  ? 379 LEU A O   1 
ATOM   2986 C CB  . LEU A 1 399 ? 1.719   0.666   9.615   1.00 18.72  ? 379 LEU A CB  1 
ATOM   2987 C CG  . LEU A 1 399 ? 2.529   0.775   8.321   1.00 22.50  ? 379 LEU A CG  1 
ATOM   2988 C CD1 . LEU A 1 399 ? 2.665   -0.581  7.657   1.00 23.69  ? 379 LEU A CD1 1 
ATOM   2989 C CD2 . LEU A 1 399 ? 1.909   1.789   7.378   1.00 24.42  ? 379 LEU A CD2 1 
ATOM   2990 N N   . THR A 1 400 ? 3.618   -0.865  11.698  1.00 19.72  ? 380 THR A N   1 
ATOM   2991 C CA  . THR A 1 400 ? 4.817   -1.632  12.031  1.00 20.52  ? 380 THR A CA  1 
ATOM   2992 C C   . THR A 1 400 ? 4.731   -3.076  11.579  1.00 18.95  ? 380 THR A C   1 
ATOM   2993 O O   . THR A 1 400 ? 3.690   -3.734  11.743  1.00 20.90  ? 380 THR A O   1 
ATOM   2994 C CB  . THR A 1 400 ? 5.131   -1.612  13.535  1.00 21.79  ? 380 THR A CB  1 
ATOM   2995 O OG1 . THR A 1 400 ? 6.415   -2.185  13.760  1.00 24.24  ? 380 THR A OG1 1 
ATOM   2996 C CG2 . THR A 1 400 ? 4.057   -2.244  14.384  1.00 21.33  ? 380 THR A CG2 1 
ATOM   2997 N N   . GLY A 1 401 ? 5.858   -3.533  11.051  1.00 17.79  ? 381 GLY A N   1 
ATOM   2998 C CA  . GLY A 1 401 ? 6.044   -4.965  10.889  1.00 18.35  ? 381 GLY A CA  1 
ATOM   2999 C C   . GLY A 1 401 ? 6.014   -5.662  12.244  1.00 18.86  ? 381 GLY A C   1 
ATOM   3000 O O   . GLY A 1 401 ? 6.242   -5.097  13.287  1.00 20.85  ? 381 GLY A O   1 
ATOM   3001 N N   . ILE A 1 402 ? 5.742   -6.961  12.192  1.00 18.13  ? 382 ILE A N   1 
ATOM   3002 C CA  . ILE A 1 402 ? 5.558   -7.764  13.388  1.00 21.38  ? 382 ILE A CA  1 
ATOM   3003 C C   . ILE A 1 402 ? 6.641   -8.817  13.517  1.00 20.94  ? 382 ILE A C   1 
ATOM   3004 O O   . ILE A 1 402 ? 7.039   -9.100  14.640  1.00 21.47  ? 382 ILE A O   1 
ATOM   3005 C CB  . ILE A 1 402 ? 4.147   -8.378  13.358  1.00 22.59  ? 382 ILE A CB  1 
ATOM   3006 C CG1 . ILE A 1 402 ? 3.071   -7.284  13.391  1.00 22.50  ? 382 ILE A CG1 1 
ATOM   3007 C CG2 . ILE A 1 402 ? 3.985   -9.418  14.442  1.00 24.25  ? 382 ILE A CG2 1 
ATOM   3008 C CD1 . ILE A 1 402 ? 1.634   -7.767  13.299  1.00 22.57  ? 382 ILE A CD1 1 
ATOM   3009 N N   . SER A 1 403 ? 7.061   -9.383  12.403  1.00 22.63  ? 383 SER A N   1 
ATOM   3010 C CA  . SER A 1 403 ? 8.110   -10.431 12.436  1.00 23.06  ? 383 SER A CA  1 
ATOM   3011 C C   . SER A 1 403 ? 7.665   -11.584 13.349  1.00 23.15  ? 383 SER A C   1 
ATOM   3012 O O   . SER A 1 403 ? 6.488   -11.918 13.343  1.00 23.35  ? 383 SER A O   1 
ATOM   3013 C CB  . SER A 1 403 ? 9.439   -9.874  12.884  1.00 24.24  ? 383 SER A CB  1 
ATOM   3014 O OG  . SER A 1 403 ? 10.510  -10.791 12.726  1.00 25.80  ? 383 SER A OG  1 
ATOM   3015 N N   . VAL A 1 404 ? 8.610   -12.104 14.131  1.00 23.10  ? 384 VAL A N   1 
ATOM   3016 C CA  . VAL A 1 404 ? 8.299   -13.249 14.971  1.00 22.95  ? 384 VAL A CA  1 
ATOM   3017 C C   . VAL A 1 404 ? 7.697   -12.825 16.324  1.00 22.38  ? 384 VAL A C   1 
ATOM   3018 O O   . VAL A 1 404 ? 7.498   -13.642 17.212  1.00 27.38  ? 384 VAL A O   1 
ATOM   3019 C CB  . VAL A 1 404 ? 9.597   -14.057 15.179  1.00 23.65  ? 384 VAL A CB  1 
ATOM   3020 C CG1 . VAL A 1 404 ? 10.136  -14.610 13.870  1.00 25.88  ? 384 VAL A CG1 1 
ATOM   3021 C CG2 . VAL A 1 404 ? 10.631  -13.220 15.918  1.00 26.65  ? 384 VAL A CG2 1 
ATOM   3022 N N   . ASN A 1 405 ? 7.454   -11.527 16.551  1.00 23.06  ? 385 ASN A N   1 
ATOM   3023 C CA  . ASN A 1 405 ? 7.294   -11.014 17.909  1.00 23.29  ? 385 ASN A CA  1 
ATOM   3024 C C   . ASN A 1 405 ? 5.847   -11.079 18.414  1.00 25.58  ? 385 ASN A C   1 
ATOM   3025 O O   . ASN A 1 405 ? 5.624   -11.060 19.643  1.00 28.25  ? 385 ASN A O   1 
ATOM   3026 C CB  . ASN A 1 405 ? 7.834   -9.582  18.028  1.00 26.43  ? 385 ASN A CB  1 
ATOM   3027 C CG  . ASN A 1 405 ? 9.331   -9.481  17.795  1.00 29.94  ? 385 ASN A CG  1 
ATOM   3028 O OD1 . ASN A 1 405 ? 10.074  -10.465 17.807  1.00 31.00  ? 385 ASN A OD1 1 
ATOM   3029 N ND2 . ASN A 1 405 ? 9.799   -8.266  17.600  1.00 29.40  ? 385 ASN A ND2 1 
ATOM   3030 N N   . GLY A 1 406 ? 4.877   -11.163 17.494  1.00 25.55  ? 386 GLY A N   1 
ATOM   3031 C CA  . GLY A 1 406 ? 3.455   -11.290 17.817  1.00 24.34  ? 386 GLY A CA  1 
ATOM   3032 C C   . GLY A 1 406 ? 2.612   -11.621 16.586  1.00 22.18  ? 386 GLY A C   1 
ATOM   3033 O O   . GLY A 1 406 ? 3.153   -12.103 15.594  1.00 25.55  ? 386 GLY A O   1 
ATOM   3034 N N   . TYR A 1 407 ? 1.284   -11.372 16.643  1.00 22.27  ? 387 TYR A N   1 
ATOM   3035 C CA  . TYR A 1 407 ? 0.417   -11.702 15.517  1.00 22.55  ? 387 TYR A CA  1 
ATOM   3036 C C   . TYR A 1 407 ? -0.433  -10.555 15.006  1.00 22.70  ? 387 TYR A C   1 
ATOM   3037 O O   . TYR A 1 407 ? -0.791  -10.599 13.837  1.00 20.36  ? 387 TYR A O   1 
ATOM   3038 C CB  . TYR A 1 407 ? -0.473  -12.917 15.830  1.00 24.74  ? 387 TYR A CB  1 
ATOM   3039 C CG  . TYR A 1 407 ? 0.281   -14.213 15.807  1.00 27.00  ? 387 TYR A CG  1 
ATOM   3040 C CD1 . TYR A 1 407 ? 0.820   -14.690 14.641  1.00 25.09  ? 387 TYR A CD1 1 
ATOM   3041 C CD2 . TYR A 1 407 ? 0.598   -14.871 16.975  1.00 29.03  ? 387 TYR A CD2 1 
ATOM   3042 C CE1 . TYR A 1 407 ? 1.543   -15.862 14.589  1.00 30.19  ? 387 TYR A CE1 1 
ATOM   3043 C CE2 . TYR A 1 407 ? 1.301   -16.065 16.945  1.00 32.80  ? 387 TYR A CE2 1 
ATOM   3044 C CZ  . TYR A 1 407 ? 1.813   -16.538 15.749  1.00 32.62  ? 387 TYR A CZ  1 
ATOM   3045 O OH  . TYR A 1 407 ? 2.542   -17.725 15.649  1.00 36.87  ? 387 TYR A OH  1 
ATOM   3046 N N   . PHE A 1 408 ? -0.775  -9.569  15.850  1.00 20.49  ? 388 PHE A N   1 
ATOM   3047 C CA  . PHE A 1 408 ? -1.706  -8.536  15.421  1.00 19.86  ? 388 PHE A CA  1 
ATOM   3048 C C   . PHE A 1 408 ? -1.406  -7.250  16.172  1.00 19.83  ? 388 PHE A C   1 
ATOM   3049 O O   . PHE A 1 408 ? -1.327  -7.254  17.403  1.00 20.81  ? 388 PHE A O   1 
ATOM   3050 C CB  . PHE A 1 408 ? -3.159  -8.973  15.670  1.00 20.58  ? 388 PHE A CB  1 
ATOM   3051 C CG  . PHE A 1 408 ? -4.205  -8.239  14.886  1.00 20.01  ? 388 PHE A CG  1 
ATOM   3052 C CD1 . PHE A 1 408 ? -4.510  -8.599  13.597  1.00 20.79  ? 388 PHE A CD1 1 
ATOM   3053 C CD2 . PHE A 1 408 ? -4.855  -7.135  15.425  1.00 22.25  ? 388 PHE A CD2 1 
ATOM   3054 C CE1 . PHE A 1 408 ? -5.449  -7.887  12.869  1.00 20.46  ? 388 PHE A CE1 1 
ATOM   3055 C CE2 . PHE A 1 408 ? -5.821  -6.441  14.711  1.00 20.61  ? 388 PHE A CE2 1 
ATOM   3056 C CZ  . PHE A 1 408 ? -6.085  -6.794  13.418  1.00 19.29  ? 388 PHE A CZ  1 
ATOM   3057 N N   . VAL A 1 409 ? -1.203  -6.161  15.418  1.00 19.91  ? 389 VAL A N   1 
ATOM   3058 C CA  . VAL A 1 409 ? -0.836  -4.886  16.019  1.00 20.80  ? 389 VAL A CA  1 
ATOM   3059 C C   . VAL A 1 409 ? -1.687  -3.773  15.428  1.00 18.41  ? 389 VAL A C   1 
ATOM   3060 O O   . VAL A 1 409 ? -1.801  -3.680  14.211  1.00 19.25  ? 389 VAL A O   1 
ATOM   3061 C CB  . VAL A 1 409 ? 0.662   -4.568  15.795  1.00 20.76  ? 389 VAL A CB  1 
ATOM   3062 C CG1 . VAL A 1 409 ? 1.073   -3.188  16.328  1.00 22.88  ? 389 VAL A CG1 1 
ATOM   3063 C CG2 . VAL A 1 409 ? 1.518   -5.639  16.436  1.00 22.68  ? 389 VAL A CG2 1 
ATOM   3064 N N   . ALA A 1 410 ? -2.165  -2.866  16.286  1.00 17.82  ? 390 ALA A N   1 
ATOM   3065 C CA  . ALA A 1 410 ? -2.757  -1.619  15.810  1.00 18.77  ? 390 ALA A CA  1 
ATOM   3066 C C   . ALA A 1 410 ? -1.804  -0.466  16.084  1.00 19.12  ? 390 ALA A C   1 
ATOM   3067 O O   . ALA A 1 410 ? -1.412  -0.265  17.228  1.00 22.75  ? 390 ALA A O   1 
ATOM   3068 C CB  . ALA A 1 410 ? -4.082  -1.364  16.499  1.00 18.61  ? 390 ALA A CB  1 
ATOM   3069 N N   . ALA A 1 411 ? -1.490  0.309   15.036  1.00 18.02  ? 391 ALA A N   1 
ATOM   3070 C CA  . ALA A 1 411 ? -0.650  1.493   15.158  1.00 17.90  ? 391 ALA A CA  1 
ATOM   3071 C C   . ALA A 1 411 ? -1.486  2.762   15.017  1.00 19.13  ? 391 ALA A C   1 
ATOM   3072 O O   . ALA A 1 411 ? -2.193  2.943   14.026  1.00 21.20  ? 391 ALA A O   1 
ATOM   3073 C CB  . ALA A 1 411 ? 0.401   1.477   14.087  1.00 18.15  ? 391 ALA A CB  1 
ATOM   3074 N N   . ILE A 1 412 ? -1.383  3.613   16.032  1.00 16.96  ? 392 ILE A N   1 
ATOM   3075 C CA  . ILE A 1 412 ? -2.286  4.740   16.194  1.00 17.42  ? 392 ILE A CA  1 
ATOM   3076 C C   . ILE A 1 412 ? -1.506  6.048   16.313  1.00 16.76  ? 392 ILE A C   1 
ATOM   3077 O O   . ILE A 1 412 ? -0.570  6.160   17.094  1.00 17.02  ? 392 ILE A O   1 
ATOM   3078 C CB  . ILE A 1 412 ? -3.162  4.571   17.445  1.00 17.76  ? 392 ILE A CB  1 
ATOM   3079 C CG1 . ILE A 1 412 ? -4.000  3.294   17.380  1.00 20.02  ? 392 ILE A CG1 1 
ATOM   3080 C CG2 . ILE A 1 412 ? -4.042  5.803   17.647  1.00 18.60  ? 392 ILE A CG2 1 
ATOM   3081 C CD1 . ILE A 1 412 ? -4.305  2.681   18.732  1.00 20.56  ? 392 ILE A CD1 1 
ATOM   3082 N N   . ASN A 1 413 ? -1.980  7.055   15.585  1.00 16.17  ? 393 ASN A N   1 
ATOM   3083 C CA  . ASN A 1 413 ? -1.572  8.420   15.883  1.00 17.42  ? 393 ASN A CA  1 
ATOM   3084 C C   . ASN A 1 413 ? -2.656  9.378   15.440  1.00 16.99  ? 393 ASN A C   1 
ATOM   3085 O O   . ASN A 1 413 ? -3.447  9.078   14.555  1.00 17.38  ? 393 ASN A O   1 
ATOM   3086 C CB  . ASN A 1 413 ? -0.259  8.835   15.225  1.00 17.01  ? 393 ASN A CB  1 
ATOM   3087 C CG  . ASN A 1 413 ? -0.358  8.951   13.725  1.00 17.83  ? 393 ASN A CG  1 
ATOM   3088 O OD1 . ASN A 1 413 ? -0.517  7.979   13.013  1.00 19.85  ? 393 ASN A OD1 1 
ATOM   3089 N ND2 . ASN A 1 413 ? -0.314  10.161  13.189  1.00 18.09  ? 393 ASN A ND2 1 
ATOM   3090 N N   . SER A 1 414 ? -2.701  10.544  16.095  1.00 19.65  ? 394 SER A N   1 
ATOM   3091 C CA  . SER A 1 414 ? -3.545  11.632  15.624  1.00 20.28  ? 394 SER A CA  1 
ATOM   3092 C C   . SER A 1 414 ? -2.629  12.676  15.004  1.00 20.01  ? 394 SER A C   1 
ATOM   3093 O O   . SER A 1 414 ? -1.650  13.079  15.625  1.00 21.84  ? 394 SER A O   1 
ATOM   3094 C CB  . SER A 1 414 ? -4.418  12.207  16.720  1.00 21.74  ? 394 SER A CB  1 
ATOM   3095 O OG  . SER A 1 414 ? -3.634  12.673  17.789  1.00 23.79  ? 394 SER A OG  1 
ATOM   3096 N N   . SER A 1 415 ? -2.915  13.013  13.752  1.00 16.31  ? 395 SER A N   1 
ATOM   3097 C CA  . SER A 1 415 ? -2.220  14.080  13.037  1.00 17.22  ? 395 SER A CA  1 
ATOM   3098 C C   . SER A 1 415 ? -3.148  14.593  11.948  1.00 18.06  ? 395 SER A C   1 
ATOM   3099 O O   . SER A 1 415 ? -4.035  13.885  11.515  1.00 19.10  ? 395 SER A O   1 
ATOM   3100 C CB  . SER A 1 415 ? -0.935  13.606  12.374  1.00 17.79  ? 395 SER A CB  1 
ATOM   3101 O OG  . SER A 1 415 ? 0.029   13.163  13.303  1.00 21.10  ? 395 SER A OG  1 
ATOM   3102 N N   . HIS A 1 416 ? -2.936  15.854  11.524  1.00 17.76  ? 396 HIS A N   1 
ATOM   3103 C CA  . HIS A 1 416 ? -3.541  16.331  10.304  1.00 18.61  ? 396 HIS A CA  1 
ATOM   3104 C C   . HIS A 1 416 ? -5.065  16.188  10.344  1.00 17.45  ? 396 HIS A C   1 
ATOM   3105 O O   . HIS A 1 416 ? -5.692  15.875  9.334   1.00 20.29  ? 396 HIS A O   1 
ATOM   3106 C CB  . HIS A 1 416 ? -2.903  15.684  9.072   1.00 18.87  ? 396 HIS A CB  1 
ATOM   3107 C CG  . HIS A 1 416 ? -1.503  16.068  8.855   1.00 17.73  ? 396 HIS A CG  1 
ATOM   3108 N ND1 . HIS A 1 416 ? -0.563  15.248  8.291   1.00 16.23  ? 396 HIS A ND1 1 
ATOM   3109 C CD2 . HIS A 1 416 ? -0.891  17.279  8.989   1.00 17.84  ? 396 HIS A CD2 1 
ATOM   3110 C CE1 . HIS A 1 416 ? 0.588   15.886  8.182   1.00 16.30  ? 396 HIS A CE1 1 
ATOM   3111 N NE2 . HIS A 1 416 ? 0.389   17.164  8.590   1.00 15.39  ? 396 HIS A NE2 1 
ATOM   3112 N N   . GLY A 1 417 ? -5.668  16.453  11.511  1.00 19.77  ? 397 GLY A N   1 
ATOM   3113 C CA  . GLY A 1 417 ? -7.113  16.539  11.613  1.00 19.89  ? 397 GLY A CA  1 
ATOM   3114 C C   . GLY A 1 417 ? -7.830  15.205  11.789  1.00 20.70  ? 397 GLY A C   1 
ATOM   3115 O O   . GLY A 1 417 ? -9.053  15.185  11.905  1.00 21.80  ? 397 GLY A O   1 
ATOM   3116 N N   . ARG A 1 418 ? -7.068  14.116  11.816  1.00 19.97  ? 398 ARG A N   1 
ATOM   3117 C CA  . ARG A 1 418 ? -7.688  12.793  11.830  1.00 19.16  ? 398 ARG A CA  1 
ATOM   3118 C C   . ARG A 1 418 ? -7.019  11.892  12.872  1.00 18.50  ? 398 ARG A C   1 
ATOM   3119 O O   . ARG A 1 418 ? -5.980  12.237  13.452  1.00 18.80  ? 398 ARG A O   1 
ATOM   3120 C CB  . ARG A 1 418 ? -7.598  12.144  10.445  1.00 20.83  ? 398 ARG A CB  1 
ATOM   3121 C CG  . ARG A 1 418 ? -8.332  12.898  9.344   1.00 22.83  ? 398 ARG A CG  1 
ATOM   3122 C CD  . ARG A 1 418 ? -8.215  12.271  7.996   1.00 26.20  ? 398 ARG A CD  1 
ATOM   3123 N NE  . ARG A 1 418 ? -8.850  13.025  6.938   1.00 29.23  ? 398 ARG A NE  1 
ATOM   3124 C CZ  . ARG A 1 418 ? -10.077 12.834  6.460   1.00 29.96  ? 398 ARG A CZ  1 
ATOM   3125 N NH1 . ARG A 1 418 ? -10.936 12.029  7.066   1.00 32.42  ? 398 ARG A NH1 1 
ATOM   3126 N NH2 . ARG A 1 418 ? -10.475 13.548  5.418   1.00 32.32  ? 398 ARG A NH2 1 
ATOM   3127 N N   . LEU A 1 419 ? -7.595  10.686  13.067  1.00 19.31  ? 399 LEU A N   1 
ATOM   3128 C CA  . LEU A 1 419 ? -6.896  9.667   13.834  1.00 18.41  ? 399 LEU A CA  1 
ATOM   3129 C C   . LEU A 1 419 ? -6.690  8.473   12.911  1.00 16.92  ? 399 LEU A C   1 
ATOM   3130 O O   . LEU A 1 419 ? -7.633  8.068   12.244  1.00 19.98  ? 399 LEU A O   1 
ATOM   3131 C CB  . LEU A 1 419 ? -7.687  9.228   15.066  1.00 19.37  ? 399 LEU A CB  1 
ATOM   3132 C CG  . LEU A 1 419 ? -6.946  8.143   15.858  1.00 22.53  ? 399 LEU A CG  1 
ATOM   3133 C CD1 . LEU A 1 419 ? -6.882  8.437   17.325  1.00 26.14  ? 399 LEU A CD1 1 
ATOM   3134 C CD2 . LEU A 1 419 ? -7.441  6.743   15.546  1.00 26.11  ? 399 LEU A CD2 1 
ATOM   3135 N N   . PHE A 1 420 ? -5.448  7.999   12.821  1.00 17.39  ? 400 PHE A N   1 
ATOM   3136 C CA  . PHE A 1 420 ? -5.137  6.873   11.948  1.00 16.27  ? 400 PHE A CA  1 
ATOM   3137 C C   . PHE A 1 420 ? -4.954  5.617   12.787  1.00 18.35  ? 400 PHE A C   1 
ATOM   3138 O O   . PHE A 1 420 ? -4.342  5.690   13.849  1.00 18.67  ? 400 PHE A O   1 
ATOM   3139 C CB  . PHE A 1 420 ? -3.881  7.216   11.124  1.00 17.68  ? 400 PHE A CB  1 
ATOM   3140 C CG  . PHE A 1 420 ? -4.044  8.515   10.379  1.00 16.76  ? 400 PHE A CG  1 
ATOM   3141 C CD1 . PHE A 1 420 ? -4.847  8.576   9.251   1.00 18.30  ? 400 PHE A CD1 1 
ATOM   3142 C CD2 . PHE A 1 420 ? -3.467  9.663   10.860  1.00 17.58  ? 400 PHE A CD2 1 
ATOM   3143 C CE1 . PHE A 1 420 ? -5.049  9.755   8.560   1.00 18.61  ? 400 PHE A CE1 1 
ATOM   3144 C CE2 . PHE A 1 420 ? -3.676  10.843  10.175  1.00 18.24  ? 400 PHE A CE2 1 
ATOM   3145 C CZ  . PHE A 1 420 ? -4.463  10.901  9.057   1.00 19.01  ? 400 PHE A CZ  1 
ATOM   3146 N N   . TRP A 1 421 ? -5.502  4.496   12.274  1.00 17.69  ? 401 TRP A N   1 
ATOM   3147 C CA  . TRP A 1 421 ? -5.579  3.228   13.014  1.00 17.27  ? 401 TRP A CA  1 
ATOM   3148 C C   . TRP A 1 421 ? -5.172  2.131   12.034  1.00 15.91  ? 401 TRP A C   1 
ATOM   3149 O O   . TRP A 1 421 ? -6.010  1.659   11.252  1.00 18.56  ? 401 TRP A O   1 
ATOM   3150 C CB  . TRP A 1 421 ? -7.005  3.057   13.575  1.00 18.53  ? 401 TRP A CB  1 
ATOM   3151 C CG  . TRP A 1 421 ? -7.216  2.142   14.746  1.00 18.03  ? 401 TRP A CG  1 
ATOM   3152 C CD1 . TRP A 1 421 ? -6.264  1.515   15.508  1.00 19.43  ? 401 TRP A CD1 1 
ATOM   3153 C CD2 . TRP A 1 421 ? -8.475  1.875   15.385  1.00 19.51  ? 401 TRP A CD2 1 
ATOM   3154 N NE1 . TRP A 1 421 ? -6.851  0.860   16.554  1.00 19.12  ? 401 TRP A NE1 1 
ATOM   3155 C CE2 . TRP A 1 421 ? -8.205  1.065   16.518  1.00 18.73  ? 401 TRP A CE2 1 
ATOM   3156 C CE3 . TRP A 1 421 ? -9.796  2.250   15.112  1.00 21.46  ? 401 TRP A CE3 1 
ATOM   3157 C CZ2 . TRP A 1 421 ? -9.226  0.608   17.357  1.00 20.66  ? 401 TRP A CZ2 1 
ATOM   3158 C CZ3 . TRP A 1 421 ? -10.809 1.789   15.931  1.00 21.16  ? 401 TRP A CZ3 1 
ATOM   3159 C CH2 . TRP A 1 421 ? -10.520 0.983   17.043  1.00 22.38  ? 401 TRP A CH2 1 
ATOM   3160 N N   . ASN A 1 422 ? -3.884  1.831   12.030  1.00 16.64  ? 402 ASN A N   1 
ATOM   3161 C CA  . ASN A 1 422 ? -3.290  0.945   11.045  1.00 17.30  ? 402 ASN A CA  1 
ATOM   3162 C C   . ASN A 1 422 ? -3.027  -0.426  11.655  1.00 18.23  ? 402 ASN A C   1 
ATOM   3163 O O   . ASN A 1 422 ? -2.131  -0.567  12.482  1.00 16.61  ? 402 ASN A O   1 
ATOM   3164 C CB  . ASN A 1 422 ? -2.007  1.556   10.459  1.00 17.54  ? 402 ASN A CB  1 
ATOM   3165 C CG  . ASN A 1 422 ? -2.346  2.656   9.481   1.00 17.93  ? 402 ASN A CG  1 
ATOM   3166 O OD1 . ASN A 1 422 ? -3.219  2.494   8.647   1.00 19.05  ? 402 ASN A OD1 1 
ATOM   3167 N ND2 . ASN A 1 422 ? -1.730  3.812   9.652   1.00 17.37  ? 402 ASN A ND2 1 
ATOM   3168 N N   . PHE A 1 423 ? -3.771  -1.422  11.151  1.00 17.30  ? 403 PHE A N   1 
ATOM   3169 C CA  . PHE A 1 423 ? -3.691  -2.801  11.622  1.00 16.77  ? 403 PHE A CA  1 
ATOM   3170 C C   . PHE A 1 423 ? -2.704  -3.603  10.793  1.00 16.27  ? 403 PHE A C   1 
ATOM   3171 O O   . PHE A 1 423 ? -2.866  -3.761  9.591   1.00 19.94  ? 403 PHE A O   1 
ATOM   3172 C CB  . PHE A 1 423 ? -5.079  -3.425  11.555  1.00 17.55  ? 403 PHE A CB  1 
ATOM   3173 C CG  . PHE A 1 423 ? -6.127  -2.736  12.384  1.00 18.29  ? 403 PHE A CG  1 
ATOM   3174 C CD1 . PHE A 1 423 ? -6.190  -2.928  13.748  1.00 18.87  ? 403 PHE A CD1 1 
ATOM   3175 C CD2 . PHE A 1 423 ? -7.048  -1.878  11.811  1.00 20.46  ? 403 PHE A CD2 1 
ATOM   3176 C CE1 . PHE A 1 423 ? -7.117  -2.249  14.528  1.00 21.61  ? 403 PHE A CE1 1 
ATOM   3177 C CE2 . PHE A 1 423 ? -7.990  -1.211  12.583  1.00 19.74  ? 403 PHE A CE2 1 
ATOM   3178 C CZ  . PHE A 1 423 ? -8.050  -1.435  13.943  1.00 20.30  ? 403 PHE A CZ  1 
ATOM   3179 N N   . THR A 1 424 ? -1.666  -4.110  11.465  1.00 16.49  ? 404 THR A N   1 
ATOM   3180 C CA  . THR A 1 424 ? -0.799  -5.078  10.812  1.00 16.78  ? 404 THR A CA  1 
ATOM   3181 C C   . THR A 1 424 ? -1.023  -6.461  11.409  1.00 17.35  ? 404 THR A C   1 
ATOM   3182 O O   . THR A 1 424 ? -1.415  -6.611  12.563  1.00 17.54  ? 404 THR A O   1 
ATOM   3183 C CB  . THR A 1 424 ? 0.665   -4.644  10.826  1.00 17.62  ? 404 THR A CB  1 
ATOM   3184 O OG1 . THR A 1 424 ? 1.082   -4.300  12.147  1.00 17.50  ? 404 THR A OG1 1 
ATOM   3185 C CG2 . THR A 1 424 ? 0.897   -3.508  9.868   1.00 18.77  ? 404 THR A CG2 1 
ATOM   3186 N N   . TYR A 1 425 ? -0.787  -7.451  10.557  1.00 17.10  ? 405 TYR A N   1 
ATOM   3187 C CA  . TYR A 1 425 ? -1.055  -8.832  10.940  1.00 17.99  ? 405 TYR A CA  1 
ATOM   3188 C C   . TYR A 1 425 ? -0.084  -9.754  10.217  1.00 20.23  ? 405 TYR A C   1 
ATOM   3189 O O   . TYR A 1 425 ? 0.418   -9.424  9.161   1.00 20.27  ? 405 TYR A O   1 
ATOM   3190 C CB  . TYR A 1 425 ? -2.506  -9.183  10.633  1.00 19.02  ? 405 TYR A CB  1 
ATOM   3191 C CG  . TYR A 1 425 ? -2.902  -9.082  9.187   1.00 19.84  ? 405 TYR A CG  1 
ATOM   3192 C CD1 . TYR A 1 425 ? -3.214  -7.879  8.579   1.00 21.77  ? 405 TYR A CD1 1 
ATOM   3193 C CD2 . TYR A 1 425 ? -2.985  -10.230 8.406   1.00 21.66  ? 405 TYR A CD2 1 
ATOM   3194 C CE1 . TYR A 1 425 ? -3.613  -7.828  7.256   1.00 22.99  ? 405 TYR A CE1 1 
ATOM   3195 C CE2 . TYR A 1 425 ? -3.375  -10.192 7.072   1.00 22.31  ? 405 TYR A CE2 1 
ATOM   3196 C CZ  . TYR A 1 425 ? -3.676  -8.973  6.482   1.00 22.69  ? 405 TYR A CZ  1 
ATOM   3197 O OH  . TYR A 1 425 ? -4.052  -8.923  5.150   1.00 25.22  ? 405 TYR A OH  1 
ATOM   3198 N N   . ILE A 1 426 ? 0.146   -10.937 10.806  1.00 21.82  ? 406 ILE A N   1 
ATOM   3199 C CA  . ILE A 1 426 ? 0.924   -11.998 10.182  1.00 21.23  ? 406 ILE A CA  1 
ATOM   3200 C C   . ILE A 1 426 ? -0.016  -12.832 9.322   1.00 21.42  ? 406 ILE A C   1 
ATOM   3201 O O   . ILE A 1 426 ? -0.973  -13.409 9.821   1.00 23.54  ? 406 ILE A O   1 
ATOM   3202 C CB  . ILE A 1 426 ? 1.624   -12.865 11.239  1.00 21.85  ? 406 ILE A CB  1 
ATOM   3203 C CG1 . ILE A 1 426 ? 2.627   -12.099 12.085  1.00 22.35  ? 406 ILE A CG1 1 
ATOM   3204 C CG2 . ILE A 1 426 ? 2.272   -14.032 10.544  1.00 24.08  ? 406 ILE A CG2 1 
ATOM   3205 C CD1 . ILE A 1 426 ? 3.704   -11.428 11.270  1.00 23.14  ? 406 ILE A CD1 1 
ATOM   3206 N N   . ASP A 1 427 ? 0.251   -12.833 8.019   1.00 22.39  ? 407 ASP A N   1 
ATOM   3207 C CA  . ASP A 1 427 ? -0.611  -13.484 7.059   1.00 25.21  ? 407 ASP A CA  1 
ATOM   3208 C C   . ASP A 1 427 ? -0.607  -14.983 7.333   1.00 25.74  ? 407 ASP A C   1 
ATOM   3209 O O   . ASP A 1 427 ? 0.370   -15.521 7.874   1.00 25.97  ? 407 ASP A O   1 
ATOM   3210 C CB  . ASP A 1 427 ? -0.170  -13.163 5.627   1.00 25.98  ? 407 ASP A CB  1 
ATOM   3211 C CG  . ASP A 1 427 ? -1.218  -13.400 4.564   1.00 28.60  ? 407 ASP A CG  1 
ATOM   3212 O OD1 . ASP A 1 427 ? -2.416  -13.582 4.925   1.00 31.54  ? 407 ASP A OD1 1 
ATOM   3213 O OD2 . ASP A 1 427 ? -0.824  -13.398 3.369   1.00 32.51  ? 407 ASP A OD2 1 
ATOM   3214 N N   . GLU A 1 428 ? -1.753  -15.612 7.003   1.00 27.08  ? 408 GLU A N   1 
ATOM   3215 C CA  . GLU A 1 428 ? -1.957  -17.044 7.138   1.00 28.43  ? 408 GLU A CA  1 
ATOM   3216 C C   . GLU A 1 428 ? -2.211  -17.438 8.598   1.00 27.67  ? 408 GLU A C   1 
ATOM   3217 O O   . GLU A 1 428 ? -3.227  -18.080 8.887   1.00 28.54  ? 408 GLU A O   1 
ATOM   3218 C CB  . GLU A 1 428 ? -0.795  -17.805 6.504   1.00 34.18  ? 408 GLU A CB  1 
ATOM   3219 C CG  . GLU A 1 428 ? -0.680  -17.567 5.014   1.00 42.65  ? 408 GLU A CG  1 
ATOM   3220 C CD  . GLU A 1 428 ? -0.095  -18.734 4.237   0.70 50.00  ? 408 GLU A CD  1 
ATOM   3221 O OE1 . GLU A 1 428 ? 0.035   -18.611 2.991   0.50 61.09  ? 408 GLU A OE1 1 
ATOM   3222 O OE2 . GLU A 1 428 ? 0.229   -19.758 4.875   1.00 55.22  ? 408 GLU A OE2 1 
ATOM   3223 N N   . ALA A 1 429 ? -1.314  -17.056 9.522   1.00 24.98  ? 409 ALA A N   1 
ATOM   3224 C CA  . ALA A 1 429 ? -1.643  -17.093 10.941  1.00 25.30  ? 409 ALA A CA  1 
ATOM   3225 C C   . ALA A 1 429 ? -2.923  -16.298 11.202  1.00 25.21  ? 409 ALA A C   1 
ATOM   3226 O O   . ALA A 1 429 ? -3.780  -16.705 11.972  1.00 25.05  ? 409 ALA A O   1 
ATOM   3227 C CB  . ALA A 1 429 ? -0.497  -16.587 11.799  1.00 25.53  ? 409 ALA A CB  1 
ATOM   3228 N N   . VAL A 1 430 ? -2.998  -15.111 10.613  1.00 25.09  ? 410 VAL A N   1 
ATOM   3229 C CA  . VAL A 1 430 ? -4.227  -14.343 10.595  1.00 22.40  ? 410 VAL A CA  1 
ATOM   3230 C C   . VAL A 1 430 ? -4.610  -14.139 9.143   1.00 23.67  ? 410 VAL A C   1 
ATOM   3231 O O   . VAL A 1 430 ? -4.045  -13.274 8.470   1.00 23.92  ? 410 VAL A O   1 
ATOM   3232 C CB  . VAL A 1 430 ? -4.033  -12.994 11.296  1.00 22.95  ? 410 VAL A CB  1 
ATOM   3233 C CG1 . VAL A 1 430 ? -5.332  -12.198 11.299  1.00 24.51  ? 410 VAL A CG1 1 
ATOM   3234 C CG2 . VAL A 1 430 ? -3.512  -13.216 12.704  1.00 23.14  ? 410 VAL A CG2 1 
ATOM   3235 N N   . PRO A 1 431 ? -5.500  -14.977 8.574   1.00 24.08  ? 411 PRO A N   1 
ATOM   3236 C CA  . PRO A 1 431 ? -5.891  -14.785 7.186   1.00 25.27  ? 411 PRO A CA  1 
ATOM   3237 C C   . PRO A 1 431 ? -6.512  -13.407 6.953   1.00 24.32  ? 411 PRO A C   1 
ATOM   3238 O O   . PRO A 1 431 ? -7.068  -12.783 7.883   1.00 24.10  ? 411 PRO A O   1 
ATOM   3239 C CB  . PRO A 1 431 ? -6.873  -15.931 6.934   1.00 28.65  ? 411 PRO A CB  1 
ATOM   3240 C CG  . PRO A 1 431 ? -6.430  -16.989 7.920   1.00 27.53  ? 411 PRO A CG  1 
ATOM   3241 C CD  . PRO A 1 431 ? -6.024  -16.227 9.160   1.00 25.31  ? 411 PRO A CD  1 
ATOM   3242 N N   . GLY A 1 432 ? -6.417  -12.958 5.688   1.00 24.97  ? 412 GLY A N   1 
ATOM   3243 C CA  . GLY A 1 432 ? -6.926  -11.645 5.318   1.00 24.27  ? 412 GLY A CA  1 
ATOM   3244 C C   . GLY A 1 432 ? -8.379  -11.467 5.760   1.00 25.68  ? 412 GLY A C   1 
ATOM   3245 O O   . GLY A 1 432 ? -8.733  -10.431 6.281   1.00 25.06  ? 412 GLY A O   1 
ATOM   3246 N N   . GLU A 1 433 ? -9.232  -12.489 5.574   1.00 26.45  ? 413 GLU A N   1 
ATOM   3247 C CA  . GLU A 1 433 ? -10.642 -12.393 5.944   1.00 27.63  ? 413 GLU A CA  1 
ATOM   3248 C C   . GLU A 1 433 ? -10.798 -12.179 7.457   1.00 26.15  ? 413 GLU A C   1 
ATOM   3249 O O   . GLU A 1 433 ? -11.689 -11.452 7.925   1.00 24.55  ? 413 GLU A O   1 
ATOM   3250 C CB  . GLU A 1 433 ? -11.400 -13.628 5.439   1.00 30.41  ? 413 GLU A CB  1 
ATOM   3251 C CG  . GLU A 1 433 ? -11.590 -13.596 3.943   0.50 39.13  ? 413 GLU A CG  1 
ATOM   3252 C CD  . GLU A 1 433 ? -12.151 -14.882 3.387   0.00 30.00  ? 413 GLU A CD  1 
ATOM   3253 O OE1 . GLU A 1 433 ? -12.439 -15.791 4.190   0.00 30.00  ? 413 GLU A OE1 1 
ATOM   3254 O OE2 . GLU A 1 433 ? -12.395 -14.939 2.165   0.00 30.00  ? 413 GLU A OE2 1 
ATOM   3255 N N   . ARG A 1 434 ? -9.905  -12.786 8.229   1.00 23.28  ? 414 ARG A N   1 
ATOM   3256 C CA  . ARG A 1 434 ? -9.935  -12.681 9.681   1.00 22.61  ? 414 ARG A CA  1 
ATOM   3257 C C   . ARG A 1 434 ? -9.480  -11.290 10.114  1.00 23.30  ? 414 ARG A C   1 
ATOM   3258 O O   . ARG A 1 434 ? -10.124 -10.689 10.976  1.00 23.89  ? 414 ARG A O   1 
ATOM   3259 C CB  . ARG A 1 434 ? -9.085  -13.786 10.309  1.00 23.57  ? 414 ARG A CB  1 
ATOM   3260 C CG  . ARG A 1 434 ? -9.080  -13.793 11.825  1.00 24.19  ? 414 ARG A CG  1 
ATOM   3261 C CD  . ARG A 1 434 ? -8.292  -14.968 12.372  1.00 24.72  ? 414 ARG A CD  1 
ATOM   3262 N NE  . ARG A 1 434 ? -8.192  -14.975 13.825  1.00 25.86  ? 414 ARG A NE  1 
ATOM   3263 C CZ  . ARG A 1 434 ? -7.262  -15.621 14.524  1.00 24.99  ? 414 ARG A CZ  1 
ATOM   3264 N NH1 . ARG A 1 434 ? -6.361  -16.392 13.926  1.00 25.69  ? 414 ARG A NH1 1 
ATOM   3265 N NH2 . ARG A 1 434 ? -7.247  -15.501 15.839  1.00 25.49  ? 414 ARG A NH2 1 
ATOM   3266 N N   . ALA A 1 435 ? -8.397  -10.804 9.492   1.00 22.94  ? 415 ALA A N   1 
ATOM   3267 C CA  . ALA A 1 435 ? -7.878  -9.477  9.764   1.00 23.62  ? 415 ALA A CA  1 
ATOM   3268 C C   . ALA A 1 435 ? -8.965  -8.442  9.507   1.00 21.37  ? 415 ALA A C   1 
ATOM   3269 O O   . ALA A 1 435 ? -9.159  -7.504  10.311  1.00 22.13  ? 415 ALA A O   1 
ATOM   3270 C CB  . ALA A 1 435 ? -6.630  -9.201  8.952   1.00 23.78  ? 415 ALA A CB  1 
ATOM   3271 N N   . GLU A 1 436 ? -9.656  -8.618  8.384   1.00 21.70  ? 416 GLU A N   1 
ATOM   3272 C CA  . GLU A 1 436 ? -10.735 -7.699  8.024   1.00 23.48  ? 416 GLU A CA  1 
ATOM   3273 C C   . GLU A 1 436 ? -11.837 -7.722  9.079   1.00 22.43  ? 416 GLU A C   1 
ATOM   3274 O O   . GLU A 1 436 ? -12.362 -6.677  9.456   1.00 22.01  ? 416 GLU A O   1 
ATOM   3275 C CB  . GLU A 1 436 ? -11.298 -8.020  6.637   1.00 26.01  ? 416 GLU A CB  1 
ATOM   3276 C CG  . GLU A 1 436 ? -10.457 -7.477  5.500   1.00 28.55  ? 416 GLU A CG  1 
ATOM   3277 C CD  . GLU A 1 436 ? -10.511 -5.975  5.210   1.00 29.46  ? 416 GLU A CD  1 
ATOM   3278 O OE1 . GLU A 1 436 ? -11.327 -5.255  5.818   1.00 24.08  ? 416 GLU A OE1 1 
ATOM   3279 O OE2 . GLU A 1 436 ? -9.692  -5.553  4.345   1.00 36.80  ? 416 GLU A OE2 1 
ATOM   3280 N N   . ARG A 1 437 ? -12.244 -8.919  9.537   1.00 22.65  ? 417 ARG A N   1 
ATOM   3281 C CA  . ARG A 1 437 ? -13.273 -9.016  10.567  1.00 23.32  ? 417 ARG A CA  1 
ATOM   3282 C C   . ARG A 1 437 ? -12.836 -8.281  11.833  1.00 21.81  ? 417 ARG A C   1 
ATOM   3283 O O   . ARG A 1 437 ? -13.629 -7.597  12.461  1.00 22.03  ? 417 ARG A O   1 
ATOM   3284 C CB  . ARG A 1 437 ? -13.602 -10.470 10.928  1.00 25.98  ? 417 ARG A CB  1 
ATOM   3285 C CG  . ARG A 1 437 ? -14.435 -11.193 9.883   1.00 29.07  ? 417 ARG A CG  1 
ATOM   3286 C CD  . ARG A 1 437 ? -14.979 -12.525 10.408  1.00 33.80  ? 417 ARG A CD  1 
ATOM   3287 N NE  . ARG A 1 437 ? -13.981 -13.549 10.704  1.00 34.20  ? 417 ARG A NE  1 
ATOM   3288 C CZ  . ARG A 1 437 ? -13.328 -14.303 9.812   1.00 39.35  ? 417 ARG A CZ  1 
ATOM   3289 N NH1 . ARG A 1 437 ? -13.628 -14.296 8.514   1.00 40.86  ? 417 ARG A NH1 1 
ATOM   3290 N NH2 . ARG A 1 437 ? -12.361 -15.096 10.246  1.00 42.50  ? 417 ARG A NH2 1 
ATOM   3291 N N   . LEU A 1 438 ? -11.582 -8.475  12.232  1.00 22.56  ? 418 LEU A N   1 
ATOM   3292 C CA  . LEU A 1 438 ? -11.064 -7.846  13.435  1.00 21.67  ? 418 LEU A CA  1 
ATOM   3293 C C   . LEU A 1 438 ? -11.106 -6.335  13.256  1.00 21.22  ? 418 LEU A C   1 
ATOM   3294 O O   . LEU A 1 438 ? -11.574 -5.626  14.149  1.00 23.57  ? 418 LEU A O   1 
ATOM   3295 C CB  . LEU A 1 438 ? -9.640  -8.346  13.684  1.00 23.48  ? 418 LEU A CB  1 
ATOM   3296 C CG  . LEU A 1 438 ? -9.514  -9.717  14.326  1.00 23.86  ? 418 LEU A CG  1 
ATOM   3297 C CD1 . LEU A 1 438 ? -8.076  -10.208 14.208  1.00 26.13  ? 418 LEU A CD1 1 
ATOM   3298 C CD2 . LEU A 1 438 ? -9.934  -9.658  15.787  1.00 24.97  ? 418 LEU A CD2 1 
ATOM   3299 N N   . ALA A 1 439 ? -10.614 -5.850  12.121  1.00 21.65  ? 419 ALA A N   1 
ATOM   3300 C CA  . ALA A 1 439 ? -10.592 -4.389  11.972  1.00 21.80  ? 419 ALA A CA  1 
ATOM   3301 C C   . ALA A 1 439 ? -12.003 -3.801  11.977  1.00 23.39  ? 419 ALA A C   1 
ATOM   3302 O O   . ALA A 1 439 ? -12.239 -2.734  12.542  1.00 22.17  ? 419 ALA A O   1 
ATOM   3303 C CB  . ALA A 1 439 ? -9.881  -3.994  10.707  1.00 24.30  ? 419 ALA A CB  1 
ATOM   3304 N N   . GLU A 1 440 ? -12.931 -4.437  11.264  1.00 23.44  ? 420 GLU A N   1 
ATOM   3305 C CA  . GLU A 1 440 ? -14.305 -3.956  11.182  1.00 23.86  ? 420 GLU A CA  1 
ATOM   3306 C C   . GLU A 1 440 ? -14.967 -3.947  12.564  1.00 23.33  ? 420 GLU A C   1 
ATOM   3307 O O   . GLU A 1 440 ? -15.758 -3.053  12.871  1.00 23.75  ? 420 GLU A O   1 
ATOM   3308 C CB  . GLU A 1 440 ? -15.089 -4.821  10.188  1.00 25.86  ? 420 GLU A CB  1 
ATOM   3309 C CG  . GLU A 1 440 ? -14.744 -4.511  8.736   1.00 28.94  ? 420 GLU A CG  1 
ATOM   3310 C CD  . GLU A 1 440 ? -15.027 -3.059  8.368   1.00 32.63  ? 420 GLU A CD  1 
ATOM   3311 O OE1 . GLU A 1 440 ? -14.074 -2.314  8.043   1.00 34.31  ? 420 GLU A OE1 1 
ATOM   3312 O OE2 . GLU A 1 440 ? -16.194 -2.658  8.475   1.00 38.57  ? 420 GLU A OE2 1 
ATOM   3313 N N   . ASP A 1 441 ? -14.691 -4.993  13.372  1.00 22.76  ? 421 ASP A N   1 
ATOM   3314 C CA  . ASP A 1 441 ? -15.226 -5.090  14.724  1.00 22.57  ? 421 ASP A CA  1 
ATOM   3315 C C   . ASP A 1 441 ? -14.636 -3.998  15.630  1.00 21.91  ? 421 ASP A C   1 
ATOM   3316 O O   . ASP A 1 441 ? -15.347 -3.427  16.452  1.00 24.45  ? 421 ASP A O   1 
ATOM   3317 C CB  . ASP A 1 441 ? -15.012 -6.488  15.305  1.00 23.89  ? 421 ASP A CB  1 
ATOM   3318 C CG  . ASP A 1 441 ? -15.919 -6.848  16.453  1.00 26.20  ? 421 ASP A CG  1 
ATOM   3319 O OD1 . ASP A 1 441 ? -16.817 -6.074  16.752  1.00 29.73  ? 421 ASP A OD1 1 
ATOM   3320 O OD2 . ASP A 1 441 ? -15.747 -7.971  17.005  1.00 27.57  ? 421 ASP A OD2 1 
ATOM   3321 N N   . CYS A 1 442 ? -13.350 -3.739  15.475  1.00 22.70  ? 422 CYS A N   1 
ATOM   3322 C CA  . CYS A 1 442 ? -12.736 -2.645  16.262  1.00 23.03  ? 422 CYS A CA  1 
ATOM   3323 C C   . CYS A 1 442 ? -13.485 -1.344  15.973  1.00 22.63  ? 422 CYS A C   1 
ATOM   3324 O O   . CYS A 1 442 ? -13.879 -0.672  16.919  1.00 22.45  ? 422 CYS A O   1 
ATOM   3325 C CB  . CYS A 1 442 ? -11.295 -2.439  15.832  1.00 24.36  ? 422 CYS A CB  1 
ATOM   3326 S SG  . CYS A 1 442 ? -10.145 -3.666  16.499  1.00 28.61  ? 422 CYS A SG  1 
ATOM   3327 N N   . LEU A 1 443 ? -13.685 -1.058  14.690  1.00 21.87  ? 423 LEU A N   1 
ATOM   3328 C CA  . LEU A 1 443 ? -14.272 0.224   14.306  1.00 22.72  ? 423 LEU A CA  1 
ATOM   3329 C C   . LEU A 1 443 ? -15.737 0.250   14.719  1.00 21.50  ? 423 LEU A C   1 
ATOM   3330 O O   . LEU A 1 443 ? -16.202 1.238   15.266  1.00 24.21  ? 423 LEU A O   1 
ATOM   3331 C CB  . LEU A 1 443 ? -14.101 0.464   12.803  1.00 26.34  ? 423 LEU A CB  1 
ATOM   3332 C CG  . LEU A 1 443 ? -14.096 1.918   12.340  1.00 33.87  ? 423 LEU A CG  1 
ATOM   3333 C CD1 . LEU A 1 443 ? -13.095 2.768   13.098  1.00 29.08  ? 423 LEU A CD1 1 
ATOM   3334 C CD2 . LEU A 1 443 ? -13.803 1.965   10.843  0.50 38.21  ? 423 LEU A CD2 1 
ATOM   3335 N N   . GLY A 1 444 ? -16.459 -0.874  14.548  1.00 22.18  ? 424 GLY A N   1 
ATOM   3336 C CA  . GLY A 1 444 ? -17.870 -0.899  14.921  1.00 23.61  ? 424 GLY A CA  1 
ATOM   3337 C C   . GLY A 1 444 ? -18.057 -0.734  16.426  1.00 21.70  ? 424 GLY A C   1 
ATOM   3338 O O   . GLY A 1 444 ? -18.991 -0.082  16.885  1.00 23.05  ? 424 GLY A O   1 
ATOM   3339 N N   . THR A 1 445 ? -17.163 -1.387  17.183  1.00 22.31  ? 425 THR A N   1 
ATOM   3340 C CA  . THR A 1 445 ? -17.203 -1.348  18.632  1.00 20.32  ? 425 THR A CA  1 
ATOM   3341 C C   . THR A 1 445 ? -16.927 0.076   19.087  1.00 20.39  ? 425 THR A C   1 
ATOM   3342 O O   . THR A 1 445 ? -17.648 0.583   19.938  1.00 21.47  ? 425 THR A O   1 
ATOM   3343 C CB  . THR A 1 445 ? -16.213 -2.353  19.223  1.00 21.72  ? 425 THR A CB  1 
ATOM   3344 O OG1 . THR A 1 445 ? -16.633 -3.673  18.821  1.00 23.29  ? 425 THR A OG1 1 
ATOM   3345 C CG2 . THR A 1 445 ? -16.091 -2.233  20.723  1.00 22.15  ? 425 THR A CG2 1 
ATOM   3346 N N   . LEU A 1 446 ? -15.924 0.698   18.479  1.00 21.79  ? 426 LEU A N   1 
ATOM   3347 C CA  . LEU A 1 446 ? -15.547 2.045   18.874  1.00 21.80  ? 426 LEU A CA  1 
ATOM   3348 C C   . LEU A 1 446 ? -16.680 3.009   18.528  1.00 22.16  ? 426 LEU A C   1 
ATOM   3349 O O   . LEU A 1 446 ? -17.044 3.870   19.350  1.00 22.28  ? 426 LEU A O   1 
ATOM   3350 C CB  . LEU A 1 446 ? -14.246 2.442   18.168  1.00 22.80  ? 426 LEU A CB  1 
ATOM   3351 C CG  . LEU A 1 446 ? -13.735 3.813   18.550  1.00 24.24  ? 426 LEU A CG  1 
ATOM   3352 C CD1 . LEU A 1 446 ? -13.244 3.783   19.973  1.00 24.52  ? 426 LEU A CD1 1 
ATOM   3353 C CD2 . LEU A 1 446 ? -12.650 4.238   17.613  1.00 28.27  ? 426 LEU A CD2 1 
ATOM   3354 N N   . LEU A 1 447 ? -17.208 2.890   17.297  1.00 21.37  ? 427 LEU A N   1 
ATOM   3355 C CA  . LEU A 1 447 ? -18.238 3.829   16.857  1.00 22.65  ? 427 LEU A CA  1 
ATOM   3356 C C   . LEU A 1 447 ? -19.519 3.685   17.688  1.00 22.93  ? 427 LEU A C   1 
ATOM   3357 O O   . LEU A 1 447 ? -20.186 4.689   17.958  1.00 23.86  ? 427 LEU A O   1 
ATOM   3358 C CB  . LEU A 1 447 ? -18.494 3.733   15.349  1.00 23.38  ? 427 LEU A CB  1 
ATOM   3359 C CG  . LEU A 1 447 ? -17.378 4.279   14.454  1.00 23.54  ? 427 LEU A CG  1 
ATOM   3360 C CD1 . LEU A 1 447 ? -17.560 3.896   13.014  1.00 24.90  ? 427 LEU A CD1 1 
ATOM   3361 C CD2 . LEU A 1 447 ? -17.303 5.806   14.552  1.00 26.99  ? 427 LEU A CD2 1 
ATOM   3362 N N   . SER A 1 448 ? -19.831 2.469   18.136  1.00 23.23  ? 428 SER A N   1 
ATOM   3363 C CA  . SER A 1 448 ? -20.990 2.270   19.046  1.00 24.25  ? 428 SER A CA  1 
ATOM   3364 C C   . SER A 1 448 ? -20.722 3.009   20.360  1.00 25.53  ? 428 SER A C   1 
ATOM   3365 O O   . SER A 1 448 ? -21.662 3.603   20.888  1.00 28.86  ? 428 SER A O   1 
ATOM   3366 C CB  . SER A 1 448 ? -21.283 0.807   19.333  1.00 25.44  ? 428 SER A CB  1 
ATOM   3367 O OG  . SER A 1 448 ? -21.402 0.047   18.143  1.00 26.28  ? 428 SER A OG  1 
ATOM   3368 N N   . ALA A 1 449 ? -19.481 2.946   20.847  1.00 23.71  ? 429 ALA A N   1 
ATOM   3369 C CA  . ALA A 1 449 ? -19.166 3.623   22.090  1.00 25.90  ? 429 ALA A CA  1 
ATOM   3370 C C   . ALA A 1 449 ? -19.311 5.137   21.908  1.00 26.33  ? 429 ALA A C   1 
ATOM   3371 O O   . ALA A 1 449 ? -19.791 5.794   22.831  1.00 33.39  ? 429 ALA A O   1 
ATOM   3372 C CB  . ALA A 1 449 ? -17.782 3.265   22.551  1.00 28.17  ? 429 ALA A CB  1 
ATOM   3373 N N   . ILE A 1 450 ? -18.899 5.668   20.760  1.00 25.08  ? 430 ILE A N   1 
ATOM   3374 C CA  . ILE A 1 450 ? -18.936 7.143   20.501  1.00 28.79  ? 430 ILE A CA  1 
ATOM   3375 C C   . ILE A 1 450 ? -20.380 7.623   20.323  1.00 30.03  ? 430 ILE A C   1 
ATOM   3376 O O   . ILE A 1 450 ? -20.690 8.720   20.797  1.00 32.00  ? 430 ILE A O   1 
ATOM   3377 C CB  . ILE A 1 450 ? -18.139 7.459   19.216  1.00 31.09  ? 430 ILE A CB  1 
ATOM   3378 C CG1 . ILE A 1 450 ? -16.638 7.352   19.423  1.00 35.60  ? 430 ILE A CG1 1 
ATOM   3379 C CG2 . ILE A 1 450 ? -18.511 8.812   18.608  1.00 35.97  ? 430 ILE A CG2 1 
ATOM   3380 C CD1 . ILE A 1 450 ? -15.851 7.436   18.128  1.00 37.17  ? 430 ILE A CD1 1 
ATOM   3381 N N   . HIS A 1 451 ? -21.231 6.812   19.710  1.00 29.17  ? 431 HIS A N   1 
ATOM   3382 C CA  . HIS A 1 451 ? -22.560 7.245   19.313  1.00 31.44  ? 431 HIS A CA  1 
ATOM   3383 C C   . HIS A 1 451 ? -23.666 6.741   20.227  1.00 35.15  ? 431 HIS A C   1 
ATOM   3384 O O   . HIS A 1 451 ? -24.811 7.157   20.046  1.00 36.58  ? 431 HIS A O   1 
ATOM   3385 C CB  . HIS A 1 451 ? -22.871 6.839   17.870  1.00 29.80  ? 431 HIS A CB  1 
ATOM   3386 C CG  . HIS A 1 451 ? -22.128 7.667   16.872  1.00 32.10  ? 431 HIS A CG  1 
ATOM   3387 N ND1 . HIS A 1 451 ? -22.477 8.974   16.611  1.00 35.21  ? 431 HIS A ND1 1 
ATOM   3388 C CD2 . HIS A 1 451 ? -21.114 7.368   16.047  1.00 32.98  ? 431 HIS A CD2 1 
ATOM   3389 C CE1 . HIS A 1 451 ? -21.646 9.454   15.688  1.00 39.25  ? 431 HIS A CE1 1 
ATOM   3390 N NE2 . HIS A 1 451 ? -20.819 8.480   15.319  1.00 37.95  ? 431 HIS A NE2 1 
ATOM   3391 N N   . ALA A 1 452 ? -23.348 5.859   21.186  1.00 40.38  ? 432 ALA A N   1 
ATOM   3392 C CA  . ALA A 1 452 ? -24.345 5.349   22.126  1.00 44.34  ? 432 ALA A CA  1 
ATOM   3393 C C   . ALA A 1 452 ? -25.118 6.513   22.723  1.00 43.80  ? 432 ALA A C   1 
ATOM   3394 O O   . ALA A 1 452 ? -24.509 7.499   23.113  1.00 44.56  ? 432 ALA A O   1 
ATOM   3395 C CB  . ALA A 1 452 ? -23.699 4.559   23.248  1.00 46.80  ? 432 ALA A CB  1 
ATOM   3396 N N   . PRO A 1 453 ? -26.460 6.423   22.859  1.00 45.14  ? 433 PRO A N   1 
ATOM   3397 C CA  . PRO A 1 453 ? -27.230 7.531   23.416  1.00 48.30  ? 433 PRO A CA  1 
ATOM   3398 C C   . PRO A 1 453 ? -26.851 7.655   24.889  1.00 54.88  ? 433 PRO A C   1 
ATOM   3399 O O   . PRO A 1 453 ? -26.685 6.643   25.574  1.00 56.59  ? 433 PRO A O   1 
ATOM   3400 C CB  . PRO A 1 453 ? -28.691 7.123   23.165  1.00 46.75  ? 433 PRO A CB  1 
ATOM   3401 C CG  . PRO A 1 453 ? -28.634 5.602   23.156  0.50 49.25  ? 433 PRO A CG  1 
ATOM   3402 C CD  . PRO A 1 453 ? -27.293 5.250   22.535  1.00 44.97  ? 433 PRO A CD  1 
ATOM   3403 N N   . GLN A 1 454 ? -26.650 8.892   25.342  1.00 61.13  ? 434 GLN A N   1 
ATOM   3404 C CA  . GLN A 1 454 ? -26.270 9.129   26.761  1.00 66.54  ? 434 GLN A CA  1 
ATOM   3405 C C   . GLN A 1 454 ? -27.543 9.336   27.606  1.00 66.66  ? 434 GLN A C   1 
ATOM   3406 O O   . GLN A 1 454 ? -27.814 8.488   28.473  1.00 69.01  ? 434 GLN A O   1 
ATOM   3407 C CB  . GLN A 1 454 ? -25.303 10.310  26.856  0.30 70.45  ? 434 GLN A CB  1 
ATOM   3408 C CG  . GLN A 1 454 ? -23.836 9.903   26.778  0.00 68.93  ? 434 GLN A CG  1 
ATOM   3409 C CD  . GLN A 1 454 ? -22.887 11.076  26.673  0.00 67.65  ? 434 GLN A CD  1 
ATOM   3410 O OE1 . GLN A 1 454 ? -23.026 11.943  25.804  0.00 67.89  ? 434 GLN A OE1 1 
ATOM   3411 N NE2 . GLN A 1 454 ? -21.900 11.107  27.557  0.00 68.61  ? 434 GLN A NE2 1 
HETATM 3412 C C1  . GOL B 2 .   ? -0.343  6.845   24.165  1.00 43.05  ? 501 GOL A C1  1 
HETATM 3413 O O1  . GOL B 2 .   ? -1.544  7.579   23.952  1.00 45.26  ? 501 GOL A O1  1 
HETATM 3414 C C2  . GOL B 2 .   ? -0.559  5.651   25.070  1.00 44.10  ? 501 GOL A C2  1 
HETATM 3415 O O2  . GOL B 2 .   ? 0.439   4.661   24.832  1.00 43.07  ? 501 GOL A O2  1 
HETATM 3416 C C3  . GOL B 2 .   ? -0.588  6.008   26.540  0.70 47.66  ? 501 GOL A C3  1 
HETATM 3417 O O3  . GOL B 2 .   ? -0.320  4.874   27.361  0.70 48.08  ? 501 GOL A O3  1 
HETATM 3418 C C1  . GOL C 2 .   ? 18.819  2.093   19.035  1.00 27.80  ? 502 GOL A C1  1 
HETATM 3419 O O1  . GOL C 2 .   ? 17.456  1.771   18.788  1.00 24.71  ? 502 GOL A O1  1 
HETATM 3420 C C2  . GOL C 2 .   ? 19.028  2.619   20.439  0.70 30.69  ? 502 GOL A C2  1 
HETATM 3421 O O2  . GOL C 2 .   ? 19.167  1.521   21.344  1.00 24.14  ? 502 GOL A O2  1 
HETATM 3422 C C3  . GOL C 2 .   ? 20.239  3.522   20.546  0.70 30.00  ? 502 GOL A C3  1 
HETATM 3423 O O3  . GOL C 2 .   ? 19.940  4.802   21.096  1.00 25.30  ? 502 GOL A O3  1 
HETATM 3424 O O   . HOH D 3 .   ? 28.953  7.756   9.830   1.00 32.75  ? 601 HOH A O   1 
HETATM 3425 O O   . HOH D 3 .   ? -15.739 21.265  18.399  1.00 52.32  ? 602 HOH A O   1 
HETATM 3426 O O   . HOH D 3 .   ? 6.269   23.851  -3.637  1.00 39.29  ? 603 HOH A O   1 
HETATM 3427 O O   . HOH D 3 .   ? 14.644  -11.099 37.437  1.00 45.24  ? 604 HOH A O   1 
HETATM 3428 O O   . HOH D 3 .   ? 17.959  -22.062 18.205  1.00 45.00  ? 605 HOH A O   1 
HETATM 3429 O O   . HOH D 3 .   ? -13.352 -13.596 13.165  1.00 40.19  ? 606 HOH A O   1 
HETATM 3430 O O   . HOH D 3 .   ? -5.000  9.135   1.497   1.00 34.94  ? 607 HOH A O   1 
HETATM 3431 O O   . HOH D 3 .   ? -13.848 -5.605  5.666   1.00 46.30  ? 608 HOH A O   1 
HETATM 3432 O O   . HOH D 3 .   ? 18.761  15.008  27.108  1.00 44.85  ? 609 HOH A O   1 
HETATM 3433 O O   . HOH D 3 .   ? 32.292  -16.382 14.141  1.00 54.75  ? 610 HOH A O   1 
HETATM 3434 O O   . HOH D 3 .   ? 17.138  -18.767 22.511  1.00 31.74  ? 611 HOH A O   1 
HETATM 3435 O O   . HOH D 3 .   ? -2.155  12.869  -13.551 1.00 40.67  ? 612 HOH A O   1 
HETATM 3436 O O   . HOH D 3 .   ? -8.296  5.919   33.609  1.00 31.07  ? 613 HOH A O   1 
HETATM 3437 O O   . HOH D 3 .   ? 9.499   6.837   21.235  1.00 25.80  ? 614 HOH A O   1 
HETATM 3438 O O   . HOH D 3 .   ? -5.780  12.085  1.673   1.00 31.03  ? 615 HOH A O   1 
HETATM 3439 O O   . HOH D 3 .   ? 19.464  -1.201  24.242  1.00 34.80  ? 616 HOH A O   1 
HETATM 3440 O O   . HOH D 3 .   ? 2.014   -14.519 29.066  1.00 41.05  ? 617 HOH A O   1 
HETATM 3441 O O   . HOH D 3 .   ? -4.530  -24.915 9.768   1.00 30.00  ? 618 HOH A O   1 
HETATM 3442 O O   . HOH D 3 .   ? -17.247 -1.731  11.166  1.00 45.88  ? 619 HOH A O   1 
HETATM 3443 O O   . HOH D 3 .   ? 4.883   -13.766 14.537  1.00 24.99  ? 620 HOH A O   1 
HETATM 3444 O O   . HOH D 3 .   ? 12.111  0.609   -1.611  1.00 24.11  ? 621 HOH A O   1 
HETATM 3445 O O   . HOH D 3 .   ? -4.104  19.574  9.353   1.00 39.09  ? 622 HOH A O   1 
HETATM 3446 O O   . HOH D 3 .   ? 16.032  23.341  5.417   1.00 41.74  ? 623 HOH A O   1 
HETATM 3447 O O   . HOH D 3 .   ? 32.834  1.098   8.024   1.00 41.14  ? 624 HOH A O   1 
HETATM 3448 O O   . HOH D 3 .   ? 16.187  -19.533 9.613   1.00 46.61  ? 625 HOH A O   1 
HETATM 3449 O O   . HOH D 3 .   ? 27.014  3.026   27.082  1.00 50.33  ? 626 HOH A O   1 
HETATM 3450 O O   . HOH D 3 .   ? -0.976  5.467   12.368  1.00 21.71  ? 627 HOH A O   1 
HETATM 3451 O O   . HOH D 3 .   ? -10.966 1.105   36.577  1.00 42.03  ? 628 HOH A O   1 
HETATM 3452 O O   . HOH D 3 .   ? -2.721  2.346   -7.915  1.00 35.07  ? 629 HOH A O   1 
HETATM 3453 O O   . HOH D 3 .   ? -13.641 -6.609  35.999  1.00 41.50  ? 630 HOH A O   1 
HETATM 3454 O O   . HOH D 3 .   ? 22.490  3.304   -0.734  1.00 27.65  ? 631 HOH A O   1 
HETATM 3455 O O   . HOH D 3 .   ? 19.136  -6.486  35.768  1.00 42.66  ? 632 HOH A O   1 
HETATM 3456 O O   . HOH D 3 .   ? 22.197  3.288   8.921   1.00 17.84  ? 633 HOH A O   1 
HETATM 3457 O O   . HOH D 3 .   ? -2.741  19.708  11.990  1.00 38.49  ? 634 HOH A O   1 
HETATM 3458 O O   . HOH D 3 .   ? 15.096  11.469  32.772  1.00 36.18  ? 635 HOH A O   1 
HETATM 3459 O O   . HOH D 3 .   ? -0.971  6.356   -3.123  1.00 21.65  ? 636 HOH A O   1 
HETATM 3460 O O   . HOH D 3 .   ? 15.237  22.969  11.858  1.00 32.38  ? 637 HOH A O   1 
HETATM 3461 O O   . HOH D 3 .   ? 18.206  -16.635 26.662  1.00 42.99  ? 638 HOH A O   1 
HETATM 3462 O O   . HOH D 3 .   ? 19.142  6.559   38.048  1.00 51.36  ? 639 HOH A O   1 
HETATM 3463 O O   . HOH D 3 .   ? 2.885   -15.109 7.146   1.00 26.97  ? 640 HOH A O   1 
HETATM 3464 O O   . HOH D 3 .   ? 24.963  13.159  3.838   1.00 28.46  ? 641 HOH A O   1 
HETATM 3465 O O   . HOH D 3 .   ? 18.526  -7.952  10.908  1.00 24.45  ? 642 HOH A O   1 
HETATM 3466 O O   . HOH D 3 .   ? 24.374  -2.424  26.593  1.00 43.93  ? 643 HOH A O   1 
HETATM 3467 O O   . HOH D 3 .   ? 13.173  19.131  15.995  1.00 27.86  ? 644 HOH A O   1 
HETATM 3468 O O   . HOH D 3 .   ? 3.542   -8.059  3.048   1.00 25.39  ? 645 HOH A O   1 
HETATM 3469 O O   . HOH D 3 .   ? -4.611  22.307  2.110   1.00 48.31  ? 646 HOH A O   1 
HETATM 3470 O O   . HOH D 3 .   ? 20.779  -1.709  2.974   1.00 34.82  ? 647 HOH A O   1 
HETATM 3471 O O   . HOH D 3 .   ? -0.194  -9.213  25.365  1.00 44.18  ? 648 HOH A O   1 
HETATM 3472 O O   . HOH D 3 .   ? 3.091   17.032  -4.201  1.00 24.95  ? 649 HOH A O   1 
HETATM 3473 O O   . HOH D 3 .   ? 12.353  -0.587  21.786  1.00 26.46  ? 650 HOH A O   1 
HETATM 3474 O O   . HOH D 3 .   ? 28.347  -0.570  2.940   1.00 27.17  ? 651 HOH A O   1 
HETATM 3475 O O   . HOH D 3 .   ? -9.321  -2.913  4.269   1.00 30.66  ? 652 HOH A O   1 
HETATM 3476 O O   . HOH D 3 .   ? -3.791  4.266   37.617  1.00 38.76  ? 653 HOH A O   1 
HETATM 3477 O O   . HOH D 3 .   ? -5.602  -17.929 23.755  1.00 26.16  ? 654 HOH A O   1 
HETATM 3478 O O   . HOH D 3 .   ? 23.224  -14.173 11.443  1.00 39.08  ? 655 HOH A O   1 
HETATM 3479 O O   . HOH D 3 .   ? -18.775 -4.791  19.971  1.00 30.17  ? 656 HOH A O   1 
HETATM 3480 O O   . HOH D 3 .   ? -5.016  8.383   5.384   1.00 22.32  ? 657 HOH A O   1 
HETATM 3481 O O   . HOH D 3 .   ? 14.547  -4.882  7.616   1.00 23.82  ? 658 HOH A O   1 
HETATM 3482 O O   . HOH D 3 .   ? 21.380  14.781  19.682  1.00 34.77  ? 659 HOH A O   1 
HETATM 3483 O O   . HOH D 3 .   ? 17.450  -4.499  8.925   1.00 25.50  ? 660 HOH A O   1 
HETATM 3484 O O   . HOH D 3 .   ? -4.023  -11.242 3.797   1.00 34.03  ? 661 HOH A O   1 
HETATM 3485 O O   . HOH D 3 .   ? 1.322   -10.583 -2.179  1.00 46.07  ? 662 HOH A O   1 
HETATM 3486 O O   . HOH D 3 .   ? 5.054   7.668   27.300  1.00 39.12  ? 663 HOH A O   1 
HETATM 3487 O O   . HOH D 3 .   ? -19.163 -7.884  23.412  1.00 45.72  ? 664 HOH A O   1 
HETATM 3488 O O   . HOH D 3 .   ? 8.302   -5.731  8.327   1.00 20.35  ? 665 HOH A O   1 
HETATM 3489 O O   . HOH D 3 .   ? -10.222 17.580  11.493  1.00 28.94  ? 666 HOH A O   1 
HETATM 3490 O O   . HOH D 3 .   ? 3.432   11.853  19.655  1.00 32.39  ? 667 HOH A O   1 
HETATM 3491 O O   . HOH D 3 .   ? 1.500   6.425   34.988  1.00 40.05  ? 668 HOH A O   1 
HETATM 3492 O O   . HOH D 3 .   ? 22.826  -1.642  30.231  1.00 40.17  ? 669 HOH A O   1 
HETATM 3493 O O   . HOH D 3 .   ? -9.490  -18.465 10.736  1.00 51.75  ? 670 HOH A O   1 
HETATM 3494 O O   . HOH D 3 .   ? 9.791   20.744  11.622  1.00 33.36  ? 671 HOH A O   1 
HETATM 3495 O O   . HOH D 3 .   ? -11.848 -9.354  36.176  1.00 57.50  ? 672 HOH A O   1 
HETATM 3496 O O   . HOH D 3 .   ? 32.540  -1.193  15.782  1.00 30.27  ? 673 HOH A O   1 
HETATM 3497 O O   . HOH D 3 .   ? 27.120  -12.890 19.180  1.00 40.02  ? 674 HOH A O   1 
HETATM 3498 O O   . HOH D 3 .   ? -2.013  -11.220 23.845  1.00 28.48  ? 675 HOH A O   1 
HETATM 3499 O O   . HOH D 3 .   ? 1.873   -6.964  37.484  1.00 41.75  ? 676 HOH A O   1 
HETATM 3500 O O   . HOH D 3 .   ? 22.772  4.837   19.559  1.00 27.81  ? 677 HOH A O   1 
HETATM 3501 O O   . HOH D 3 .   ? 21.025  -1.937  40.817  1.00 44.13  ? 678 HOH A O   1 
HETATM 3502 O O   . HOH D 3 .   ? -13.676 -9.628  16.008  1.00 24.35  ? 679 HOH A O   1 
HETATM 3503 O O   . HOH D 3 .   ? 26.647  7.465   4.578   1.00 36.85  ? 680 HOH A O   1 
HETATM 3504 O O   . HOH D 3 .   ? 20.774  11.349  18.507  1.00 22.79  ? 681 HOH A O   1 
HETATM 3505 O O   . HOH D 3 .   ? 8.974   22.217  9.543   1.00 33.54  ? 682 HOH A O   1 
HETATM 3506 O O   . HOH D 3 .   ? -4.603  -2.626  2.896   1.00 35.34  ? 683 HOH A O   1 
HETATM 3507 O O   . HOH D 3 .   ? -18.682 12.698  33.210  1.00 38.86  ? 684 HOH A O   1 
HETATM 3508 O O   . HOH D 3 .   ? 11.599  -21.530 25.289  1.00 32.56  ? 685 HOH A O   1 
HETATM 3509 O O   . HOH D 3 .   ? -17.498 -5.188  26.253  1.00 39.11  ? 686 HOH A O   1 
HETATM 3510 O O   . HOH D 3 .   ? 4.407   -12.209 21.801  1.00 35.73  ? 687 HOH A O   1 
HETATM 3511 O O   . HOH D 3 .   ? 0.739   2.143   23.100  1.00 20.71  ? 688 HOH A O   1 
HETATM 3512 O O   . HOH D 3 .   ? 19.082  1.155   2.572   1.00 23.74  ? 689 HOH A O   1 
HETATM 3513 O O   . HOH D 3 .   ? -19.502 8.500   12.922  1.00 37.41  ? 690 HOH A O   1 
HETATM 3514 O O   . HOH D 3 .   ? -2.572  17.878  -3.955  1.00 22.31  ? 691 HOH A O   1 
HETATM 3515 O O   . HOH D 3 .   ? -13.811 -3.909  34.881  1.00 41.06  ? 692 HOH A O   1 
HETATM 3516 O O   . HOH D 3 .   ? 7.255   -9.540  9.351   1.00 23.29  ? 693 HOH A O   1 
HETATM 3517 O O   . HOH D 3 .   ? -16.314 -7.900  11.977  1.00 30.62  ? 694 HOH A O   1 
HETATM 3518 O O   . HOH D 3 .   ? 17.281  17.035  19.950  1.00 38.77  ? 695 HOH A O   1 
HETATM 3519 O O   . HOH D 3 .   ? 5.749   0.134   -7.965  1.00 33.64  ? 696 HOH A O   1 
HETATM 3520 O O   . HOH D 3 .   ? -1.273  -10.535 40.362  1.00 37.26  ? 697 HOH A O   1 
HETATM 3521 O O   . HOH D 3 .   ? -8.165  -7.263  2.831   1.00 52.07  ? 698 HOH A O   1 
HETATM 3522 O O   . HOH D 3 .   ? -0.883  17.594  12.561  1.00 22.21  ? 699 HOH A O   1 
HETATM 3523 O O   . HOH D 3 .   ? 29.310  5.455   18.990  1.00 33.41  ? 700 HOH A O   1 
HETATM 3524 O O   . HOH D 3 .   ? -3.314  -6.427  34.197  1.00 25.41  ? 701 HOH A O   1 
HETATM 3525 O O   . HOH D 3 .   ? 5.122   -9.133  -2.675  1.00 43.86  ? 702 HOH A O   1 
HETATM 3526 O O   . HOH D 3 .   ? 13.852  -4.082  35.711  1.00 30.38  ? 703 HOH A O   1 
HETATM 3527 O O   . HOH D 3 .   ? 9.878   16.394  14.732  1.00 26.57  ? 704 HOH A O   1 
HETATM 3528 O O   . HOH D 3 .   ? 12.623  -8.086  18.078  1.00 30.33  ? 705 HOH A O   1 
HETATM 3529 O O   . HOH D 3 .   ? 0.375   -18.343 35.048  1.00 37.98  ? 706 HOH A O   1 
HETATM 3530 O O   . HOH D 3 .   ? -3.202  11.686  -4.369  1.00 25.37  ? 707 HOH A O   1 
HETATM 3531 O O   . HOH D 3 .   ? 3.524   4.269   22.400  1.00 30.42  ? 708 HOH A O   1 
HETATM 3532 O O   . HOH D 3 .   ? 9.014   -14.246 19.436  1.00 32.75  ? 709 HOH A O   1 
HETATM 3533 O O   . HOH D 3 .   ? 29.786  1.701   3.700   1.00 27.56  ? 710 HOH A O   1 
HETATM 3534 O O   . HOH D 3 .   ? 35.012  0.363   15.424  1.00 40.46  ? 711 HOH A O   1 
HETATM 3535 O O   . HOH D 3 .   ? -7.806  -1.513  36.086  1.00 38.50  ? 712 HOH A O   1 
HETATM 3536 O O   . HOH D 3 .   ? -6.314  15.750  -8.651  1.00 19.33  ? 713 HOH A O   1 
HETATM 3537 O O   . HOH D 3 .   ? 1.461   -19.264 18.851  1.00 42.14  ? 714 HOH A O   1 
HETATM 3538 O O   . HOH D 3 .   ? -8.780  -13.789 18.940  1.00 27.62  ? 715 HOH A O   1 
HETATM 3539 O O   . HOH D 3 .   ? 6.745   23.850  9.231   1.00 29.57  ? 716 HOH A O   1 
HETATM 3540 O O   . HOH D 3 .   ? -3.970  6.775   28.192  1.00 34.88  ? 717 HOH A O   1 
HETATM 3541 O O   . HOH D 3 .   ? 12.531  14.186  31.015  1.00 34.13  ? 718 HOH A O   1 
HETATM 3542 O O   . HOH D 3 .   ? 26.805  -1.132  22.999  1.00 44.52  ? 719 HOH A O   1 
HETATM 3543 O O   . HOH D 3 .   ? -4.721  -14.660 3.828   1.00 45.49  ? 720 HOH A O   1 
HETATM 3544 O O   . HOH D 3 .   ? 7.902   -10.742 21.196  1.00 32.49  ? 721 HOH A O   1 
HETATM 3545 O O   . HOH D 3 .   ? 22.882  -9.021  9.338   1.00 36.05  ? 722 HOH A O   1 
HETATM 3546 O O   . HOH D 3 .   ? -7.305  -9.160  39.367  1.00 35.75  ? 723 HOH A O   1 
HETATM 3547 O O   . HOH D 3 .   ? -13.866 -10.561 6.448   1.00 31.74  ? 724 HOH A O   1 
HETATM 3548 O O   . HOH D 3 .   ? -15.377 -9.570  23.332  1.00 42.58  ? 725 HOH A O   1 
HETATM 3549 O O   . HOH D 3 .   ? -3.003  5.274   31.452  1.00 37.03  ? 726 HOH A O   1 
HETATM 3550 O O   . HOH D 3 .   ? -1.704  -2.782  27.612  1.00 25.07  ? 727 HOH A O   1 
HETATM 3551 O O   . HOH D 3 .   ? 25.607  13.971  13.622  1.00 29.03  ? 728 HOH A O   1 
HETATM 3552 O O   . HOH D 3 .   ? 14.838  0.178   23.105  1.00 25.20  ? 729 HOH A O   1 
HETATM 3553 O O   . HOH D 3 .   ? -10.916 -15.696 30.144  1.00 33.97  ? 730 HOH A O   1 
HETATM 3554 O O   . HOH D 3 .   ? -10.493 -16.577 39.401  1.00 32.53  ? 731 HOH A O   1 
HETATM 3555 O O   . HOH D 3 .   ? 7.884   26.151  6.894   1.00 37.04  ? 732 HOH A O   1 
HETATM 3556 O O   . HOH D 3 .   ? 22.064  -4.193  34.438  1.00 43.13  ? 733 HOH A O   1 
HETATM 3557 O O   . HOH D 3 .   ? 0.754   -1.567  12.586  1.00 17.98  ? 734 HOH A O   1 
HETATM 3558 O O   . HOH D 3 .   ? -10.717 7.652   35.975  1.00 52.26  ? 735 HOH A O   1 
HETATM 3559 O O   . HOH D 3 .   ? -4.245  -17.523 29.717  1.00 38.63  ? 736 HOH A O   1 
HETATM 3560 O O   . HOH D 3 .   ? -5.832  5.570   1.025   1.00 38.40  ? 737 HOH A O   1 
HETATM 3561 O O   . HOH D 3 .   ? 14.170  26.609  12.503  1.00 48.12  ? 738 HOH A O   1 
HETATM 3562 O O   . HOH D 3 .   ? 5.257   -4.533  39.846  1.00 37.76  ? 739 HOH A O   1 
HETATM 3563 O O   . HOH D 3 .   ? 6.287   -5.061  30.660  1.00 28.01  ? 740 HOH A O   1 
HETATM 3564 O O   . HOH D 3 .   ? 10.940  -20.287 18.183  1.00 39.31  ? 741 HOH A O   1 
HETATM 3565 O O   . HOH D 3 .   ? 7.062   3.695   -11.269 1.00 40.20  ? 742 HOH A O   1 
HETATM 3566 O O   . HOH D 3 .   ? 19.574  10.699  16.072  1.00 18.06  ? 743 HOH A O   1 
HETATM 3567 O O   . HOH D 3 .   ? 23.693  -15.086 13.930  1.00 37.63  ? 744 HOH A O   1 
HETATM 3568 O O   . HOH D 3 .   ? -0.140  18.485  -5.162  1.00 24.93  ? 745 HOH A O   1 
HETATM 3569 O O   . HOH D 3 .   ? 26.653  4.854   19.824  1.00 33.21  ? 746 HOH A O   1 
HETATM 3570 O O   . HOH D 3 .   ? 8.744   9.347   27.243  1.00 31.10  ? 747 HOH A O   1 
HETATM 3571 O O   . HOH D 3 .   ? 26.505  -5.617  23.968  1.00 38.39  ? 748 HOH A O   1 
HETATM 3572 O O   . HOH D 3 .   ? 25.378  -7.757  20.773  1.00 32.17  ? 749 HOH A O   1 
HETATM 3573 O O   . HOH D 3 .   ? 22.662  -17.359 22.905  1.00 42.99  ? 750 HOH A O   1 
HETATM 3574 O O   . HOH D 3 .   ? -6.850  -19.687 39.510  1.00 24.46  ? 751 HOH A O   1 
HETATM 3575 O O   . HOH D 3 .   ? 27.949  -8.045  19.769  1.00 33.40  ? 752 HOH A O   1 
HETATM 3576 O O   . HOH D 3 .   ? 10.386  -11.942 20.179  1.00 31.55  ? 753 HOH A O   1 
HETATM 3577 O O   . HOH D 3 .   ? 20.223  8.596   18.509  1.00 25.53  ? 754 HOH A O   1 
HETATM 3578 O O   . HOH D 3 .   ? 7.095   6.314   19.839  1.00 32.68  ? 755 HOH A O   1 
HETATM 3579 O O   . HOH D 3 .   ? -10.362 -17.400 15.402  1.00 52.62  ? 756 HOH A O   1 
HETATM 3580 O O   . HOH D 3 .   ? -7.408  5.928   -7.183  1.00 36.25  ? 757 HOH A O   1 
HETATM 3581 O O   . HOH D 3 .   ? 13.831  2.728   -1.285  1.00 24.39  ? 758 HOH A O   1 
HETATM 3582 O O   . HOH D 3 .   ? 19.439  12.826  24.166  1.00 36.35  ? 759 HOH A O   1 
HETATM 3583 O O   . HOH D 3 .   ? 11.843  20.247  21.833  1.00 35.88  ? 760 HOH A O   1 
HETATM 3584 O O   . HOH D 3 .   ? -5.256  2.914   -5.886  1.00 41.47  ? 761 HOH A O   1 
HETATM 3585 O O   . HOH D 3 .   ? -10.516 16.367  16.223  1.00 29.92  ? 762 HOH A O   1 
HETATM 3586 O O   . HOH D 3 .   ? -10.389 5.814   37.294  1.00 44.37  ? 763 HOH A O   1 
HETATM 3587 O O   . HOH D 3 .   ? -0.978  16.860  15.262  1.00 26.60  ? 764 HOH A O   1 
HETATM 3588 O O   . HOH D 3 .   ? -18.846 -4.336  15.766  1.00 43.23  ? 765 HOH A O   1 
HETATM 3589 O O   . HOH D 3 .   ? 9.089   14.572  17.299  1.00 35.18  ? 766 HOH A O   1 
HETATM 3590 O O   . HOH D 3 .   ? 2.231   -19.863 13.789  1.00 43.44  ? 767 HOH A O   1 
HETATM 3591 O O   . HOH D 3 .   ? 17.430  23.106  7.847   1.00 33.35  ? 768 HOH A O   1 
HETATM 3592 O O   . HOH D 3 .   ? 16.265  21.704  -0.664  1.00 54.67  ? 769 HOH A O   1 
HETATM 3593 O O   . HOH D 3 .   ? 2.048   13.564  -8.643  1.00 26.80  ? 770 HOH A O   1 
HETATM 3594 O O   . HOH D 3 .   ? -3.623  18.415  7.071   1.00 28.91  ? 771 HOH A O   1 
HETATM 3595 O O   . HOH D 3 .   ? -18.164 4.017   32.842  1.00 48.16  ? 772 HOH A O   1 
HETATM 3596 O O   . HOH D 3 .   ? 18.268  6.327   -4.492  1.00 32.69  ? 773 HOH A O   1 
HETATM 3597 O O   . HOH D 3 .   ? -5.043  14.057  7.231   1.00 20.04  ? 774 HOH A O   1 
HETATM 3598 O O   . HOH D 3 .   ? 21.627  10.203  1.941   1.00 22.21  ? 775 HOH A O   1 
HETATM 3599 O O   . HOH D 3 .   ? 27.497  6.662   12.419  1.00 26.91  ? 776 HOH A O   1 
HETATM 3600 O O   . HOH D 3 .   ? 5.640   -20.523 21.113  1.00 37.34  ? 777 HOH A O   1 
HETATM 3601 O O   . HOH D 3 .   ? -3.934  15.799  -5.365  1.00 21.59  ? 778 HOH A O   1 
HETATM 3602 O O   . HOH D 3 .   ? 20.186  -14.163 8.193   1.00 40.82  ? 779 HOH A O   1 
HETATM 3603 O O   . HOH D 3 .   ? -9.213  12.073  28.172  1.00 42.21  ? 780 HOH A O   1 
HETATM 3604 O O   . HOH D 3 .   ? 18.606  -3.618  1.539   1.00 41.07  ? 781 HOH A O   1 
HETATM 3605 O O   . HOH D 3 .   ? -3.646  -6.539  3.592   1.00 30.88  ? 782 HOH A O   1 
HETATM 3606 O O   . HOH D 3 .   ? 21.880  2.504   33.024  1.00 47.03  ? 783 HOH A O   1 
HETATM 3607 O O   . HOH D 3 .   ? 3.115   -10.852 28.625  1.00 35.65  ? 784 HOH A O   1 
HETATM 3608 O O   . HOH D 3 .   ? 3.701   5.831   25.518  1.00 31.33  ? 785 HOH A O   1 
HETATM 3609 O O   . HOH D 3 .   ? 20.340  10.620  25.994  1.00 31.40  ? 786 HOH A O   1 
HETATM 3610 O O   . HOH D 3 .   ? 2.634   -14.198 19.917  1.00 35.20  ? 787 HOH A O   1 
HETATM 3611 O O   . HOH D 3 .   ? 29.583  7.464   7.502   1.00 35.01  ? 788 HOH A O   1 
HETATM 3612 O O   . HOH D 3 .   ? 28.134  12.483  19.524  1.00 36.65  ? 789 HOH A O   1 
HETATM 3613 O O   . HOH D 3 .   ? -23.971 1.919   21.316  1.00 42.35  ? 790 HOH A O   1 
HETATM 3614 O O   . HOH D 3 .   ? -20.788 -1.690  26.140  1.00 36.56  ? 791 HOH A O   1 
HETATM 3615 O O   . HOH D 3 .   ? -19.095 -0.601  22.142  1.00 26.51  ? 792 HOH A O   1 
HETATM 3616 O O   . HOH D 3 .   ? -16.896 -8.410  24.954  1.00 46.31  ? 793 HOH A O   1 
HETATM 3617 O O   . HOH D 3 .   ? -6.660  -1.302  3.952   1.00 26.72  ? 794 HOH A O   1 
HETATM 3618 O O   . HOH D 3 .   ? -7.348  12.378  -4.740  1.00 35.25  ? 795 HOH A O   1 
HETATM 3619 O O   . HOH D 3 .   ? 13.743  -9.839  2.636   1.00 33.83  ? 796 HOH A O   1 
HETATM 3620 O O   . HOH D 3 .   ? -5.780  14.895  14.586  1.00 26.57  ? 797 HOH A O   1 
HETATM 3621 O O   . HOH D 3 .   ? 6.932   -9.018  6.523   1.00 23.87  ? 798 HOH A O   1 
HETATM 3622 O O   . HOH D 3 .   ? 23.922  -5.489  40.734  1.00 30.00  ? 799 HOH A O   1 
HETATM 3623 O O   . HOH D 3 .   ? -7.379  -16.185 19.151  1.00 28.61  ? 800 HOH A O   1 
HETATM 3624 O O   . HOH D 3 .   ? -2.883  4.759   28.719  1.00 34.78  ? 801 HOH A O   1 
HETATM 3625 O O   . HOH D 3 .   ? -6.494  13.841  4.890   1.00 34.13  ? 802 HOH A O   1 
HETATM 3626 O O   . HOH D 3 .   ? 8.320   10.794  -9.634  1.00 40.61  ? 803 HOH A O   1 
HETATM 3627 O O   . HOH D 3 .   ? 14.353  -11.447 6.680   1.00 44.91  ? 804 HOH A O   1 
HETATM 3628 O O   . HOH D 3 .   ? 20.600  20.368  9.472   1.00 20.98  ? 805 HOH A O   1 
HETATM 3629 O O   . HOH D 3 .   ? -13.316 16.772  22.657  1.00 39.49  ? 806 HOH A O   1 
HETATM 3630 O O   . HOH D 3 .   ? -13.265 0.436   35.094  1.00 32.62  ? 807 HOH A O   1 
HETATM 3631 O O   . HOH D 3 .   ? -17.639 16.176  17.221  1.00 43.31  ? 808 HOH A O   1 
HETATM 3632 O O   . HOH D 3 .   ? -11.489 3.838   7.946   1.00 29.12  ? 809 HOH A O   1 
HETATM 3633 O O   . HOH D 3 .   ? -7.644  11.135  25.293  1.00 29.56  ? 810 HOH A O   1 
HETATM 3634 O O   . HOH D 3 .   ? 14.355  19.265  9.836   1.00 26.09  ? 811 HOH A O   1 
HETATM 3635 O O   . HOH D 3 .   ? 5.052   18.270  -7.763  1.00 42.14  ? 812 HOH A O   1 
HETATM 3636 O O   . HOH D 3 .   ? 0.742   22.853  11.673  1.00 44.04  ? 813 HOH A O   1 
HETATM 3637 O O   . HOH D 3 .   ? -5.583  -7.479  35.508  1.00 47.07  ? 814 HOH A O   1 
HETATM 3638 O O   . HOH D 3 .   ? 22.644  7.474   18.344  1.00 23.11  ? 815 HOH A O   1 
HETATM 3639 O O   . HOH D 3 .   ? 6.052   11.651  19.512  1.00 28.73  ? 816 HOH A O   1 
HETATM 3640 O O   . HOH D 3 .   ? -8.653  -14.795 3.860   1.00 37.52  ? 817 HOH A O   1 
HETATM 3641 O O   . HOH D 3 .   ? -4.044  9.275   -7.516  1.00 24.91  ? 818 HOH A O   1 
HETATM 3642 O O   . HOH D 3 .   ? 14.250  20.670  13.508  1.00 40.91  ? 819 HOH A O   1 
HETATM 3643 O O   . HOH D 3 .   ? -6.138  -0.357  19.208  1.00 19.60  ? 820 HOH A O   1 
HETATM 3644 O O   . HOH D 3 .   ? -2.050  -7.248  1.284   1.00 32.81  ? 821 HOH A O   1 
HETATM 3645 O O   . HOH D 3 .   ? 21.433  8.699   15.505  1.00 20.34  ? 822 HOH A O   1 
HETATM 3646 O O   . HOH D 3 .   ? -8.794  -18.551 19.037  1.00 29.39  ? 823 HOH A O   1 
HETATM 3647 O O   . HOH D 3 .   ? -19.989 1.615   28.290  1.00 30.01  ? 824 HOH A O   1 
HETATM 3648 O O   . HOH D 3 .   ? 7.873   10.532  -7.121  1.00 38.08  ? 825 HOH A O   1 
HETATM 3649 O O   . HOH D 3 .   ? 31.107  9.757   17.929  1.00 40.31  ? 826 HOH A O   1 
HETATM 3650 O O   . HOH D 3 .   ? 10.650  -11.141 5.495   1.00 41.73  ? 827 HOH A O   1 
HETATM 3651 O O   . HOH D 3 .   ? 15.952  21.459  9.515   1.00 25.77  ? 828 HOH A O   1 
HETATM 3652 O O   . HOH D 3 .   ? -2.739  -23.072 13.655  1.00 46.26  ? 829 HOH A O   1 
HETATM 3653 O O   . HOH D 3 .   ? 13.697  5.089   -8.403  1.00 33.72  ? 830 HOH A O   1 
HETATM 3654 O O   . HOH D 3 .   ? 17.406  -0.697  22.262  1.00 36.41  ? 831 HOH A O   1 
HETATM 3655 O O   . HOH D 3 .   ? -4.928  8.725   24.846  1.00 28.53  ? 832 HOH A O   1 
HETATM 3656 O O   . HOH D 3 .   ? -0.527  13.062  22.763  1.00 35.21  ? 833 HOH A O   1 
HETATM 3657 O O   . HOH D 3 .   ? 6.186   -10.478 23.203  1.00 44.78  ? 834 HOH A O   1 
HETATM 3658 O O   . HOH D 3 .   ? 23.889  21.094  15.763  1.00 35.06  ? 835 HOH A O   1 
HETATM 3659 O O   . HOH D 3 .   ? -3.877  -12.642 43.256  1.00 35.78  ? 836 HOH A O   1 
HETATM 3660 O O   . HOH D 3 .   ? 11.459  16.412  -9.853  1.00 34.35  ? 837 HOH A O   1 
HETATM 3661 O O   . HOH D 3 .   ? 7.589   13.424  -9.164  1.00 42.24  ? 838 HOH A O   1 
HETATM 3662 O O   . HOH D 3 .   ? 9.524   1.670   -8.077  1.00 28.78  ? 839 HOH A O   1 
HETATM 3663 O O   . HOH D 3 .   ? -4.659  18.318  13.661  1.00 31.83  ? 840 HOH A O   1 
HETATM 3664 O O   . HOH D 3 .   ? 8.306   -11.196 5.369   1.00 41.34  ? 841 HOH A O   1 
HETATM 3665 O O   . HOH D 3 .   ? 30.837  -13.192 8.072   1.00 44.38  ? 842 HOH A O   1 
HETATM 3666 O O   . HOH D 3 .   ? -23.839 -1.744  18.450  1.00 32.75  ? 843 HOH A O   1 
HETATM 3667 O O   . HOH D 3 .   ? 2.176   24.201  9.916   1.00 37.69  ? 844 HOH A O   1 
HETATM 3668 O O   . HOH D 3 .   ? 22.486  17.779  -1.294  1.00 44.34  ? 845 HOH A O   1 
HETATM 3669 O O   . HOH D 3 .   ? -6.271  19.909  10.315  1.00 49.02  ? 846 HOH A O   1 
HETATM 3670 O O   . HOH D 3 .   ? 15.105  -4.615  13.222  1.00 32.75  ? 847 HOH A O   1 
HETATM 3671 O O   . HOH D 3 .   ? 24.398  -9.315  25.852  1.00 56.97  ? 848 HOH A O   1 
HETATM 3672 O O   . HOH D 3 .   ? -7.915  1.007   2.968   1.00 44.69  ? 849 HOH A O   1 
HETATM 3673 O O   . HOH D 3 .   ? 3.603   24.360  -3.709  1.00 41.53  ? 850 HOH A O   1 
HETATM 3674 O O   . HOH D 3 .   ? -14.912 15.019  31.975  1.00 38.14  ? 851 HOH A O   1 
HETATM 3675 O O   . HOH D 3 .   ? 12.099  15.301  28.835  1.00 44.03  ? 852 HOH A O   1 
HETATM 3676 O O   . HOH D 3 .   ? 17.714  9.397   -5.380  1.00 49.44  ? 853 HOH A O   1 
HETATM 3677 O O   . HOH D 3 .   ? -4.018  -11.882 41.034  1.00 33.06  ? 854 HOH A O   1 
HETATM 3678 O O   . HOH D 3 .   ? -2.618  -3.488  -0.643  1.00 40.27  ? 855 HOH A O   1 
HETATM 3679 O O   . HOH D 3 .   ? 9.079   -22.049 13.525  1.00 52.91  ? 856 HOH A O   1 
HETATM 3680 O O   . HOH D 3 .   ? 18.956  29.190  11.265  1.00 47.80  ? 857 HOH A O   1 
HETATM 3681 O O   . HOH D 3 .   ? 21.272  0.849   0.361   1.00 31.50  ? 858 HOH A O   1 
HETATM 3682 O O   . HOH D 3 .   ? -22.327 4.977   29.675  1.00 45.26  ? 859 HOH A O   1 
HETATM 3683 O O   . HOH D 3 .   ? -2.910  8.529   26.657  1.00 42.34  ? 860 HOH A O   1 
HETATM 3684 O O   . HOH D 3 .   ? 24.179  -18.105 14.037  1.00 47.80  ? 861 HOH A O   1 
HETATM 3685 O O   . HOH D 3 .   ? -14.538 -16.966 30.319  1.00 30.00  ? 862 HOH A O   1 
HETATM 3686 O O   . HOH D 3 .   ? -7.349  -4.514  33.837  1.00 40.86  ? 863 HOH A O   1 
HETATM 3687 O O   . HOH D 3 .   ? 4.465   9.002   22.472  1.00 41.40  ? 864 HOH A O   1 
HETATM 3688 O O   . HOH D 3 .   ? -12.447 -3.518  3.325   1.00 58.24  ? 865 HOH A O   1 
HETATM 3689 O O   . HOH D 3 .   ? -7.763  16.683  15.170  1.00 33.85  ? 866 HOH A O   1 
HETATM 3690 O O   . HOH D 3 .   ? 4.446   -14.610 17.847  1.00 41.78  ? 867 HOH A O   1 
HETATM 3691 O O   . HOH D 3 .   ? 2.444   10.629  -12.105 1.00 45.98  ? 868 HOH A O   1 
HETATM 3692 O O   . HOH D 3 .   ? 17.960  -14.506 31.160  1.00 45.80  ? 869 HOH A O   1 
HETATM 3693 O O   . HOH D 3 .   ? -15.704 -12.478 6.722   1.00 42.02  ? 870 HOH A O   1 
HETATM 3694 O O   . HOH D 3 .   ? 0.662   -10.543 27.547  1.00 41.11  ? 871 HOH A O   1 
HETATM 3695 O O   . HOH D 3 .   ? -7.683  17.759  19.545  1.00 43.56  ? 872 HOH A O   1 
HETATM 3696 O O   . HOH D 3 .   ? -12.679 6.120   7.200   1.00 53.97  ? 873 HOH A O   1 
HETATM 3697 O O   . HOH D 3 .   ? -20.501 -3.068  16.921  1.00 48.77  ? 874 HOH A O   1 
HETATM 3698 O O   . HOH D 3 .   ? -10.190 -16.776 8.280   1.00 44.82  ? 875 HOH A O   1 
HETATM 3699 O O   . HOH D 3 .   ? -4.559  -25.320 12.742  1.00 30.00  ? 876 HOH A O   1 
HETATM 3700 O O   . HOH D 3 .   ? 29.747  -3.021  3.428   1.00 37.84  ? 877 HOH A O   1 
HETATM 3701 O O   . HOH D 3 .   ? -21.864 7.244   27.071  1.00 49.25  ? 878 HOH A O   1 
HETATM 3702 O O   . HOH D 3 .   ? -20.883 9.547   31.451  1.00 45.98  ? 879 HOH A O   1 
HETATM 3703 O O   . HOH D 3 .   ? 8.309   -7.713  31.669  1.00 45.88  ? 880 HOH A O   1 
HETATM 3704 O O   . HOH D 3 .   ? -18.086 -5.961  12.714  1.00 47.67  ? 881 HOH A O   1 
HETATM 3705 O O   . HOH D 3 .   ? 12.212  19.452  11.579  1.00 33.51  ? 882 HOH A O   1 
HETATM 3706 O O   . HOH D 3 .   ? -14.965 -8.255  7.191   1.00 39.01  ? 883 HOH A O   1 
HETATM 3707 O O   . HOH D 3 .   ? 18.023  -5.004  11.652  1.00 32.68  ? 884 HOH A O   1 
HETATM 3708 O O   . HOH D 3 .   ? 26.746  -15.068 8.475   1.00 46.23  ? 885 HOH A O   1 
HETATM 3709 O O   . HOH D 3 .   ? -4.725  13.968  -3.711  1.00 29.70  ? 886 HOH A O   1 
HETATM 3710 O O   . HOH D 3 .   ? -6.601  7.867   32.470  1.00 40.98  ? 887 HOH A O   1 
HETATM 3711 O O   . HOH D 3 .   ? 4.822   6.440   21.991  1.00 39.19  ? 888 HOH A O   1 
HETATM 3712 O O   . HOH D 3 .   ? -5.623  -9.664  41.313  1.00 38.97  ? 889 HOH A O   1 
HETATM 3713 O O   . HOH D 3 .   ? 12.075  17.831  13.929  1.00 35.55  ? 890 HOH A O   1 
HETATM 3714 O O   . HOH D 3 .   ? -16.118 5.160   9.733   1.00 44.73  ? 891 HOH A O   1 
HETATM 3715 O O   . HOH D 3 .   ? 12.381  -24.074 21.210  1.00 41.74  ? 892 HOH A O   1 
HETATM 3716 O O   . HOH D 3 .   ? -9.168  12.142  31.963  1.00 30.00  ? 893 HOH A O   1 
HETATM 3717 O O   . HOH D 3 .   ? -7.713  10.013  32.471  1.00 30.00  ? 894 HOH A O   1 
HETATM 3718 O O   . HOH D 3 .   ? -21.103 2.506   25.416  1.00 40.94  ? 895 HOH A O   1 
HETATM 3719 O O   . HOH D 3 .   ? 25.875  -3.042  24.796  1.00 51.08  ? 896 HOH A O   1 
HETATM 3720 O O   . HOH D 3 .   ? -8.151  11.683  -7.334  1.00 25.31  ? 897 HOH A O   1 
HETATM 3721 O O   . HOH D 3 .   ? 6.966   -21.447 19.315  1.00 48.53  ? 898 HOH A O   1 
HETATM 3722 O O   . HOH D 3 .   ? 17.256  -18.724 25.482  1.00 37.41  ? 899 HOH A O   1 
HETATM 3723 O O   . HOH D 3 .   ? -3.875  -10.830 0.798   1.00 56.43  ? 900 HOH A O   1 
HETATM 3724 O O   . HOH D 3 .   ? 33.210  -4.087  19.406  1.00 39.83  ? 901 HOH A O   1 
HETATM 3725 O O   . HOH D 3 .   ? -14.832 -11.657 14.567  1.00 36.08  ? 902 HOH A O   1 
HETATM 3726 O O   . HOH D 3 .   ? -7.148  19.309  14.098  1.00 38.17  ? 903 HOH A O   1 
HETATM 3727 O O   . HOH D 3 .   ? -20.919 0.429   23.820  1.00 33.89  ? 904 HOH A O   1 
HETATM 3728 O O   . HOH D 3 .   ? -3.982  7.204   35.293  1.00 50.47  ? 905 HOH A O   1 
HETATM 3729 O O   . HOH D 3 .   ? -19.960 2.637   31.523  1.00 62.40  ? 906 HOH A O   1 
HETATM 3730 O O   . HOH D 3 .   ? -0.015  7.236   33.106  1.00 51.67  ? 907 HOH A O   1 
HETATM 3731 O O   . HOH D 3 .   ? 7.351   1.505   -9.614  1.00 36.49  ? 908 HOH A O   1 
HETATM 3732 O O   . HOH D 3 .   ? -6.672  16.716  4.355   1.00 39.28  ? 909 HOH A O   1 
HETATM 3733 O O   . HOH D 3 .   ? 10.790  19.569  17.411  1.00 37.31  ? 910 HOH A O   1 
HETATM 3734 O O   . HOH D 3 .   ? -8.356  19.824  11.545  1.00 38.49  ? 911 HOH A O   1 
HETATM 3735 O O   . HOH D 3 .   ? -5.641  -6.000  1.971   1.00 42.13  ? 912 HOH A O   1 
HETATM 3736 O O   . HOH D 3 .   ? 12.599  24.151  11.736  1.00 41.99  ? 913 HOH A O   1 
HETATM 3737 O O   . HOH D 3 .   ? -6.210  3.049   39.725  1.00 61.45  ? 914 HOH A O   1 
HETATM 3738 O O   . HOH D 3 .   ? -4.352  7.591   31.360  1.00 39.25  ? 915 HOH A O   1 
HETATM 3739 O O   . HOH D 3 .   ? -5.763  24.625  3.835   1.00 49.83  ? 916 HOH A O   1 
HETATM 3740 O O   . HOH D 3 .   ? 28.475  0.680   23.951  1.00 49.51  ? 917 HOH A O   1 
HETATM 3741 O O   . HOH D 3 .   ? 1.544   -22.038 15.165  1.00 52.07  ? 918 HOH A O   1 
HETATM 3742 O O   . HOH D 3 .   ? 17.654  -0.679  1.307   1.00 39.03  ? 919 HOH A O   1 
HETATM 3743 O O   . HOH D 3 .   ? -17.038 -10.423 13.049  1.00 40.16  ? 920 HOH A O   1 
HETATM 3744 O O   . HOH D 3 .   ? 0.535   16.888  -11.539 1.00 46.59  ? 921 HOH A O   1 
HETATM 3745 O O   . HOH D 3 .   ? 18.197  -16.756 29.374  1.00 40.64  ? 922 HOH A O   1 
HETATM 3746 O O   . HOH D 3 .   ? 15.533  1.679   -3.074  1.00 30.59  ? 923 HOH A O   1 
HETATM 3747 O O   . HOH D 3 .   ? -13.072 -10.254 3.800   1.00 41.50  ? 924 HOH A O   1 
HETATM 3748 O O   . HOH D 3 .   ? -19.597 -3.260  22.201  1.00 40.09  ? 925 HOH A O   1 
HETATM 3749 O O   . HOH D 3 .   ? -23.081 -0.405  22.522  1.00 40.18  ? 926 HOH A O   1 
HETATM 3750 O O   . HOH D 3 .   ? 11.828  0.578   -8.685  1.00 43.56  ? 927 HOH A O   1 
HETATM 3751 O O   . HOH D 3 .   ? -16.841 -7.943  9.115   1.00 40.27  ? 928 HOH A O   1 
HETATM 3752 O O   . HOH D 3 .   ? -18.207 -11.595 11.148  1.00 47.64  ? 929 HOH A O   1 
HETATM 3753 O O   . HOH D 3 .   ? -1.899  -25.343 5.223   1.00 30.00  ? 930 HOH A O   1 
HETATM 3754 O O   . HOH D 3 .   ? 23.142  10.595  26.155  1.00 41.33  ? 931 HOH A O   1 
HETATM 3755 O O   . HOH D 3 .   ? 21.407  29.081  9.684   1.00 39.25  ? 932 HOH A O   1 
HETATM 3756 O O   . HOH D 3 .   ? 34.116  -3.026  21.897  1.00 37.59  ? 933 HOH A O   1 
HETATM 3757 O O   . HOH D 3 .   ? 7.411   23.643  14.626  1.00 50.01  ? 934 HOH A O   1 
HETATM 3758 O O   . HOH D 3 .   ? -24.332 1.971   26.006  1.00 48.60  ? 935 HOH A O   1 
HETATM 3759 O O   . HOH D 3 .   ? -1.271  -13.907 44.007  1.00 41.24  ? 936 HOH A O   1 
HETATM 3760 O O   . HOH D 3 .   ? 16.963  -0.002  -1.367  1.00 42.09  ? 937 HOH A O   1 
HETATM 3761 O O   . HOH D 3 .   ? 8.712   20.441  -15.843 1.00 55.23  ? 938 HOH A 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   . ALA A 22  ? 0.5447 0.3408 0.4596 -0.0903 -0.0052 -0.0225 2   ALA A N   
2    C CA  . ALA A 22  ? 0.4566 0.3325 0.4491 -0.0379 -0.0034 0.0041  2   ALA A CA  
3    C C   . ALA A 22  ? 0.4346 0.3259 0.3996 -0.0233 -0.0102 0.0311  2   ALA A C   
4    O O   . ALA A 22  ? 0.4504 0.3249 0.3793 -0.0361 -0.0031 0.0645  2   ALA A O   
5    C CB  . ALA A 22  ? 0.5144 0.2850 0.4292 -0.0061 -0.0006 -0.0239 2   ALA A CB  
6    N N   A GLU A 23  ? 0.3806 0.3754 0.4084 0.0209  -0.0244 0.0132  3   GLU A N   
7    N N   B GLU A 23  ? 0.4097 0.3630 0.4031 -0.0041 -0.0054 0.0503  3   GLU A N   
8    C CA  A GLU A 23  ? 0.3578 0.3671 0.3669 0.0149  -0.0039 0.0162  3   GLU A CA  
9    C CA  B GLU A 23  ? 0.4010 0.3303 0.3592 -0.0180 0.0299  0.0767  3   GLU A CA  
10   C C   A GLU A 23  ? 0.3850 0.3624 0.3749 0.0173  -0.0144 0.0342  3   GLU A C   
11   C C   B GLU A 23  ? 0.4026 0.3235 0.3590 0.0007  0.0046  0.0780  3   GLU A C   
12   O O   A GLU A 23  ? 0.4371 0.4245 0.3493 0.0057  0.0297  0.0292  3   GLU A O   
13   O O   B GLU A 23  ? 0.4426 0.3744 0.3469 0.0032  0.0480  0.0583  3   GLU A O   
14   C CB  A GLU A 23  ? 0.3429 0.4263 0.4516 0.0214  -0.0152 -0.0269 3   GLU A CB  
15   C CB  B GLU A 23  ? 0.4132 0.3473 0.4236 -0.0303 0.0417  0.0873  3   GLU A CB  
16   C CG  A GLU A 23  ? 0.3534 0.4377 0.4484 0.0329  -0.0341 -0.0461 3   GLU A CG  
17   C CG  B GLU A 23  ? 0.4209 0.3451 0.4727 -0.0284 0.0570  0.1328  3   GLU A CG  
18   C CD  A GLU A 23  ? 0.3420 0.4935 0.5053 0.0187  -0.0154 -0.0612 3   GLU A CD  
19   C CD  B GLU A 23  ? 0.4422 0.3476 0.5118 -0.0411 0.0692  0.1243  3   GLU A CD  
20   O OE1 A GLU A 23  ? 0.3168 0.5452 0.4602 0.0034  0.0197  -0.1092 3   GLU A OE1 
21   O OE1 B GLU A 23  ? 0.4745 0.4195 0.5530 -0.0634 0.1017  0.1269  3   GLU A OE1 
22   O OE2 A GLU A 23  ? 0.3935 0.5606 0.5437 0.0506  0.0079  -0.0722 3   GLU A OE2 
23   O OE2 B GLU A 23  ? 0.4156 0.2903 0.6116 -0.0488 0.1019  0.1618  3   GLU A OE2 
24   N N   . ILE A 24  ? 0.4041 0.3148 0.3299 0.0036  0.0029  0.0991  4   ILE A N   
25   C CA  . ILE A 24  ? 0.3899 0.2809 0.3730 -0.0125 -0.0004 0.0804  4   ILE A CA  
26   C C   . ILE A 24  ? 0.3581 0.3175 0.3169 -0.0163 -0.0073 0.0679  4   ILE A C   
27   O O   . ILE A 24  ? 0.4155 0.3244 0.3304 0.0295  -0.0086 0.0643  4   ILE A O   
28   C CB  . ILE A 24  ? 0.3855 0.2733 0.3811 -0.0123 0.0051  0.1157  4   ILE A CB  
29   C CG1 . ILE A 24  ? 0.4379 0.2936 0.4122 -0.0172 0.0083  0.0937  4   ILE A CG1 
30   C CG2 . ILE A 24  ? 0.4112 0.3189 0.4117 -0.0396 0.0264  0.1234  4   ILE A CG2 
31   C CD1 . ILE A 24  ? 0.4817 0.2478 0.4450 -0.0143 -0.0069 0.0725  4   ILE A CD1 
32   N N   . ARG A 25  ? 0.3532 0.3834 0.3170 -0.0084 -0.0083 0.0475  5   ARG A N   
33   C CA  . ARG A 25  ? 0.3593 0.3617 0.3190 -0.0113 -0.0321 0.0689  5   ARG A CA  
34   C C   . ARG A 25  ? 0.3956 0.3666 0.3152 -0.0767 -0.0127 0.0818  5   ARG A C   
35   O O   . ARG A 25  ? 0.4244 0.4856 0.3869 -0.1143 -0.0717 0.0772  5   ARG A O   
36   C CB  . ARG A 25  ? 0.3708 0.3792 0.3811 -0.0374 -0.0296 0.0605  5   ARG A CB  
37   C CG  . ARG A 25  ? 0.3876 0.4929 0.4222 -0.0643 -0.0363 0.0105  5   ARG A CG  
38   C CD  . ARG A 25  ? 0.3695 0.5065 0.4141 -0.0722 -0.0128 -0.0094 5   ARG A CD  
39   N NE  . ARG A 25  ? 0.4092 0.5528 0.4183 -0.0352 -0.0160 -0.0525 5   ARG A NE  
40   C CZ  . ARG A 25  ? 0.4296 0.4939 0.3707 -0.0306 -0.0140 -0.0512 5   ARG A CZ  
41   N NH1 . ARG A 25  ? 0.3759 0.4564 0.3371 -0.0189 -0.0149 -0.0134 5   ARG A NH1 
42   N NH2 . ARG A 25  ? 0.4363 0.5194 0.3494 -0.0292 -0.0222 -0.0359 5   ARG A NH2 
43   N N   . ARG A 26  ? 0.3934 0.3311 0.3146 -0.0367 -0.0435 0.0717  6   ARG A N   
44   C CA  . ARG A 26  ? 0.3664 0.3560 0.3250 -0.0360 -0.0412 0.0725  6   ARG A CA  
45   C C   . ARG A 26  ? 0.3239 0.3044 0.3377 -0.0099 -0.0542 0.1089  6   ARG A C   
46   O O   . ARG A 26  ? 0.3646 0.3316 0.3045 -0.0364 -0.0042 0.1214  6   ARG A O   
47   C CB  . ARG A 26  ? 0.3643 0.3399 0.3461 -0.0730 -0.0151 0.0651  6   ARG A CB  
48   C CG  . ARG A 26  ? 0.3710 0.3445 0.3582 -0.0588 0.0047  0.0595  6   ARG A CG  
49   C CD  . ARG A 26  ? 0.3618 0.2931 0.3426 -0.0919 -0.0033 0.0324  6   ARG A CD  
50   N NE  . ARG A 26  ? 0.3881 0.2314 0.3293 -0.0515 -0.0060 0.0508  6   ARG A NE  
51   C CZ  . ARG A 26  ? 0.3724 0.2745 0.3343 -0.0464 -0.0158 0.0524  6   ARG A CZ  
52   N NH1 . ARG A 26  ? 0.3458 0.2295 0.3083 -0.0381 -0.0114 0.0558  6   ARG A NH1 
53   N NH2 . ARG A 26  ? 0.3444 0.2957 0.3448 -0.0657 -0.0101 0.0572  6   ARG A NH2 
54   N N   . PRO A 27  ? 0.3742 0.4179 0.3400 -0.0244 -0.0402 0.1347  7   PRO A N   
55   C CA  . PRO A 27  ? 0.3577 0.4004 0.3605 -0.0093 -0.0406 0.1307  7   PRO A CA  
56   C C   . PRO A 27  ? 0.3337 0.3244 0.3143 -0.0049 -0.0101 0.1302  7   PRO A C   
57   O O   . PRO A 27  ? 0.3267 0.3104 0.3531 -0.0221 -0.0227 0.1243  7   PRO A O   
58   C CB  . PRO A 27  ? 0.3804 0.4410 0.3705 0.0112  -0.0353 0.1465  7   PRO A CB  
59   C CG  . PRO A 27  ? 0.4210 0.4763 0.3856 -0.0094 -0.0383 0.1373  7   PRO A CG  
60   C CD  . PRO A 27  ? 0.3895 0.4327 0.3687 -0.0013 -0.0395 0.1263  7   PRO A CD  
61   N N   . LEU A 28  ? 0.3537 0.2744 0.3281 -0.0025 -0.0210 0.1213  8   LEU A N   
62   C CA  . LEU A 28  ? 0.3701 0.2404 0.3416 -0.0086 -0.0154 0.1063  8   LEU A CA  
63   C C   . LEU A 28  ? 0.3352 0.2648 0.3110 -0.0127 -0.0160 0.1022  8   LEU A C   
64   O O   . LEU A 28  ? 0.3768 0.2848 0.3279 -0.0059 -0.0023 0.1418  8   LEU A O   
65   C CB  . LEU A 28  ? 0.3677 0.2441 0.3010 0.0109  -0.0068 0.0792  8   LEU A CB  
66   C CG  . LEU A 28  ? 0.3685 0.2310 0.3253 0.0380  -0.0099 0.0861  8   LEU A CG  
67   C CD1 . LEU A 28  ? 0.3988 0.2456 0.3420 0.0404  -0.0016 0.0831  8   LEU A CD1 
68   C CD2 . LEU A 28  ? 0.3923 0.2403 0.3484 0.0281  0.0058  0.0889  8   LEU A CD2 
69   N N   . SER A 29  ? 0.3920 0.2274 0.3048 -0.0267 -0.0198 0.0871  9   SER A N   
70   C CA  . SER A 29  ? 0.3624 0.2404 0.3250 -0.0235 -0.0054 0.0810  9   SER A CA  
71   C C   . SER A 29  ? 0.3547 0.2257 0.3142 -0.0315 -0.0061 0.0953  9   SER A C   
72   O O   . SER A 29  ? 0.3837 0.1847 0.3148 0.0139  0.0211  0.0878  9   SER A O   
73   C CB  . SER A 29  ? 0.3935 0.2369 0.3433 -0.0348 -0.0023 0.0645  9   SER A CB  
74   O OG  . SER A 29  ? 0.4061 0.1863 0.3305 -0.0161 -0.0050 0.0402  9   SER A OG  
75   N N   . ALA A 30  ? 0.3555 0.2810 0.3107 -0.0208 -0.0284 0.0919  10  ALA A N   
76   C CA  . ALA A 30  ? 0.3729 0.2609 0.3222 -0.0279 -0.0034 0.0931  10  ALA A CA  
77   C C   . ALA A 30  ? 0.3577 0.2370 0.3045 -0.0075 0.0064  0.0873  10  ALA A C   
78   O O   . ALA A 30  ? 0.3970 0.1888 0.3377 -0.0331 -0.0012 0.1157  10  ALA A O   
79   C CB  . ALA A 30  ? 0.3542 0.2935 0.3172 -0.0001 -0.0165 0.0993  10  ALA A CB  
80   N N   . VAL A 31  ? 0.3387 0.2661 0.3427 -0.0054 -0.0029 0.0805  11  VAL A N   
81   C CA  . VAL A 31  ? 0.3385 0.2206 0.3214 0.0025  0.0040  0.0554  11  VAL A CA  
82   C C   . VAL A 31  ? 0.3156 0.1727 0.3208 0.0118  -0.0158 0.0856  11  VAL A C   
83   O O   . VAL A 31  ? 0.3419 0.1602 0.3118 -0.0180 0.0021  0.0859  11  VAL A O   
84   C CB  . VAL A 31  ? 0.3653 0.2950 0.3354 0.0076  -0.0044 0.0226  11  VAL A CB  
85   C CG1 . VAL A 31  ? 0.3586 0.3009 0.3320 0.0222  -0.0036 0.0049  11  VAL A CG1 
86   C CG2 . VAL A 31  ? 0.3560 0.3622 0.3418 -0.0025 -0.0012 0.0341  11  VAL A CG2 
87   N N   . GLU A 32  ? 0.3306 0.1637 0.3186 -0.0154 0.0150  0.0707  12  GLU A N   
88   C CA  . GLU A 32  ? 0.3418 0.1614 0.2907 -0.0026 0.0053  0.0661  12  GLU A CA  
89   C C   . GLU A 32  ? 0.3341 0.1796 0.2665 0.0048  -0.0003 0.0591  12  GLU A C   
90   O O   . GLU A 32  ? 0.3622 0.1849 0.2908 -0.0003 -0.0136 0.0842  12  GLU A O   
91   C CB  . GLU A 32  ? 0.3255 0.1730 0.2878 0.0113  0.0100  0.0621  12  GLU A CB  
92   C CG  . GLU A 32  ? 0.3353 0.1822 0.3143 0.0219  0.0150  0.0729  12  GLU A CG  
93   C CD  . GLU A 32  ? 0.3362 0.1649 0.3455 0.0065  0.0047  0.0506  12  GLU A CD  
94   O OE1 . GLU A 32  ? 0.4001 0.1873 0.4430 -0.0077 -0.0049 0.0455  12  GLU A OE1 
95   O OE2 . GLU A 32  ? 0.3061 0.1840 0.3569 -0.0333 -0.0197 0.0697  12  GLU A OE2 
96   N N   . ARG A 33  ? 0.3722 0.1804 0.2960 0.0030  -0.0062 0.0824  13  ARG A N   
97   C CA  . ARG A 33  ? 0.3852 0.1961 0.3162 0.0215  -0.0157 0.0669  13  ARG A CA  
98   C C   . ARG A 33  ? 0.3677 0.1812 0.2771 0.0335  -0.0195 0.0855  13  ARG A C   
99   O O   . ARG A 33  ? 0.4068 0.1551 0.3096 0.0425  0.0033  0.0685  13  ARG A O   
100  C CB  . ARG A 33  ? 0.4029 0.1829 0.3505 0.0190  -0.0264 0.0718  13  ARG A CB  
101  C CG  . ARG A 33  ? 0.4407 0.1773 0.3884 0.0231  -0.0229 0.1023  13  ARG A CG  
102  C CD  . ARG A 33  ? 0.4249 0.2115 0.4371 0.0416  -0.0108 0.1196  13  ARG A CD  
103  N NE  . ARG A 33  ? 0.4716 0.1590 0.4036 0.0663  -0.0138 0.1025  13  ARG A NE  
104  C CZ  . ARG A 33  ? 0.4621 0.2267 0.4088 0.0261  -0.0023 0.1393  13  ARG A CZ  
105  N NH1 . ARG A 33  ? 0.4358 0.2441 0.4390 0.0306  -0.0155 0.0996  13  ARG A NH1 
106  N NH2 . ARG A 33  ? 0.4847 0.2677 0.4352 0.0054  0.0144  0.1859  13  ARG A NH2 
107  N N   . TRP A 34  ? 0.3511 0.1430 0.2933 0.0273  -0.0137 0.0965  14  TRP A N   
108  C CA  . TRP A 34  ? 0.3520 0.1288 0.3282 0.0122  0.0008  0.0631  14  TRP A CA  
109  C C   . TRP A 34  ? 0.3361 0.0925 0.3086 -0.0084 -0.0043 0.0775  14  TRP A C   
110  O O   . TRP A 34  ? 0.3623 0.1673 0.3150 -0.0229 -0.0005 0.0631  14  TRP A O   
111  C CB  . TRP A 34  ? 0.3986 0.1587 0.3449 -0.0027 0.0011  0.0853  14  TRP A CB  
112  C CG  . TRP A 34  ? 0.4215 0.1543 0.3703 -0.0183 0.0299  0.1081  14  TRP A CG  
113  C CD1 . TRP A 34  ? 0.4207 0.1761 0.4186 -0.0237 0.0351  0.0500  14  TRP A CD1 
114  C CD2 . TRP A 34  ? 0.4326 0.1154 0.4177 -0.0186 0.0313  0.0762  14  TRP A CD2 
115  N NE1 . TRP A 34  ? 0.4306 0.1844 0.3772 -0.0201 0.0400  0.0616  14  TRP A NE1 
116  C CE2 . TRP A 34  ? 0.4422 0.1813 0.4233 -0.0044 0.0193  0.0803  14  TRP A CE2 
117  C CE3 . TRP A 34  ? 0.4690 0.1131 0.4687 0.0250  0.0088  0.0958  14  TRP A CE3 
118  C CZ2 . TRP A 34  ? 0.4672 0.2061 0.4506 0.0036  0.0263  0.0638  14  TRP A CZ2 
119  C CZ3 . TRP A 34  ? 0.4618 0.2069 0.4743 -0.0077 -0.0075 0.1064  14  TRP A CZ3 
120  C CH2 . TRP A 34  ? 0.4585 0.1967 0.4977 -0.0146 -0.0044 0.0750  14  TRP A CH2 
121  N N   . TYR A 35  ? 0.3590 0.0771 0.3222 0.0039  -0.0171 0.0463  15  TYR A N   
122  C CA  . TYR A 35  ? 0.3424 0.1156 0.3115 -0.0004 -0.0108 0.0403  15  TYR A CA  
123  C C   . TYR A 35  ? 0.3358 0.1072 0.3276 0.0093  -0.0082 0.0636  15  TYR A C   
124  O O   . TYR A 35  ? 0.3493 0.1374 0.3401 -0.0115 -0.0110 0.0612  15  TYR A O   
125  C CB  . TYR A 35  ? 0.3361 0.1104 0.3246 -0.0270 0.0049  0.0673  15  TYR A CB  
126  C CG  . TYR A 35  ? 0.3224 0.1225 0.3308 -0.0027 0.0065  0.0689  15  TYR A CG  
127  C CD1 . TYR A 35  ? 0.3385 0.1620 0.3728 0.0192  0.0035  0.0500  15  TYR A CD1 
128  C CD2 . TYR A 35  ? 0.2987 0.1724 0.3322 -0.0087 0.0104  0.0504  15  TYR A CD2 
129  C CE1 . TYR A 35  ? 0.3575 0.1812 0.3791 -0.0009 0.0061  0.0512  15  TYR A CE1 
130  C CE2 . TYR A 35  ? 0.3404 0.1843 0.3519 -0.0006 0.0414  0.0590  15  TYR A CE2 
131  C CZ  . TYR A 35  ? 0.3440 0.2105 0.3316 0.0129  0.0326  0.0607  15  TYR A CZ  
132  O OH  . TYR A 35  ? 0.3698 0.2819 0.4300 -0.0070 0.0781  0.0295  15  TYR A OH  
133  N N   . TRP A 36  ? 0.3573 0.1534 0.3363 0.0274  0.0010  0.0644  16  TRP A N   
134  C CA  . TRP A 36  ? 0.3452 0.0987 0.3602 0.0339  0.0099  0.0485  16  TRP A CA  
135  C C   . TRP A 36  ? 0.3556 0.1274 0.3498 0.0097  -0.0117 0.0218  16  TRP A C   
136  O O   . TRP A 36  ? 0.4012 0.0966 0.3667 0.0229  -0.0085 -0.0113 16  TRP A O   
137  C CB  . TRP A 36  ? 0.3518 0.1146 0.3886 0.0075  0.0140  0.0524  16  TRP A CB  
138  C CG  . TRP A 36  ? 0.3646 0.2228 0.3969 0.0210  0.0318  0.0486  16  TRP A CG  
139  C CD1 . TRP A 36  ? 0.3885 0.2704 0.3955 0.0174  0.0128  0.0461  16  TRP A CD1 
140  C CD2 . TRP A 36  ? 0.4242 0.2301 0.4031 0.0395  0.0061  0.0616  16  TRP A CD2 
141  N NE1 . TRP A 36  ? 0.3727 0.2939 0.4155 0.0153  0.0284  0.0309  16  TRP A NE1 
142  C CE2 . TRP A 36  ? 0.3771 0.2369 0.4648 0.0545  0.0225  0.0422  16  TRP A CE2 
143  C CE3 . TRP A 36  ? 0.4124 0.2017 0.4520 0.0660  0.0083  0.0734  16  TRP A CE3 
144  C CZ2 . TRP A 36  ? 0.3912 0.3745 0.4873 0.0844  -0.0078 0.0371  16  TRP A CZ2 
145  C CZ3 . TRP A 36  ? 0.4217 0.2533 0.5021 0.0657  0.0271  0.0758  16  TRP A CZ3 
146  C CH2 . TRP A 36  ? 0.3864 0.2487 0.5358 0.0836  0.0344  0.0442  16  TRP A CH2 
147  N N   . LEU A 37  ? 0.3416 0.1789 0.3688 0.0134  -0.0184 0.0273  17  LEU A N   
148  C CA  . LEU A 37  ? 0.3770 0.1124 0.3782 0.0467  -0.0078 0.0579  17  LEU A CA  
149  C C   . LEU A 37  ? 0.3794 0.1075 0.3099 0.0443  -0.0032 0.0527  17  LEU A C   
150  O O   . LEU A 37  ? 0.4218 0.1007 0.3557 0.0705  -0.0203 0.0388  17  LEU A O   
151  C CB  . LEU A 37  ? 0.3961 0.0638 0.4156 0.0371  -0.0353 0.0838  17  LEU A CB  
152  C CG  . LEU A 37  ? 0.4331 0.1583 0.4680 0.0279  -0.0486 0.0851  17  LEU A CG  
153  C CD1 . LEU A 37  ? 0.4828 0.1486 0.5011 0.0600  -0.0593 0.0922  17  LEU A CD1 
154  C CD2 . LEU A 37  ? 0.4188 0.1941 0.5160 0.0622  -0.0642 0.0631  17  LEU A CD2 
155  N N   . SER A 38  ? 0.3716 0.0991 0.3708 0.0291  0.0253  0.0630  18  SER A N   
156  C CA  . SER A 38  ? 0.3679 0.1119 0.3450 0.0237  0.0264  0.0667  18  SER A CA  
157  C C   . SER A 38  ? 0.3555 0.1195 0.3626 0.0205  -0.0008 0.0379  18  SER A C   
158  O O   . SER A 38  ? 0.3777 0.0823 0.3685 0.0354  -0.0103 0.0416  18  SER A O   
159  C CB  . SER A 38  ? 0.4157 0.1163 0.3477 0.0211  0.0264  0.0640  18  SER A CB  
160  O OG  . SER A 38  ? 0.4047 0.1759 0.3505 0.0359  0.0146  0.0932  18  SER A OG  
161  N N   . ASP A 39  ? 0.3735 0.1331 0.3565 0.0130  0.0119  0.0391  19  ASP A N   
162  C CA  . ASP A 39  ? 0.3648 0.1278 0.3445 0.0009  -0.0198 0.0396  19  ASP A CA  
163  C C   . ASP A 39  ? 0.3604 0.1429 0.3599 0.0116  -0.0055 0.0469  19  ASP A C   
164  O O   . ASP A 39  ? 0.4145 0.0777 0.3916 0.0332  -0.0088 0.0238  19  ASP A O   
165  C CB  . ASP A 39  ? 0.3715 0.0717 0.3196 0.0341  -0.0273 0.0523  19  ASP A CB  
166  C CG  . ASP A 39  ? 0.3719 0.1776 0.3423 0.0162  -0.0016 0.0446  19  ASP A CG  
167  O OD1 . ASP A 39  ? 0.3524 0.1717 0.3784 0.0012  -0.0113 0.0170  19  ASP A OD1 
168  O OD2 . ASP A 39  ? 0.3869 0.1709 0.3934 0.0212  0.0165  0.0624  19  ASP A OD2 
169  N N   . GLN A 40  ? 0.3773 0.1298 0.3687 0.0133  0.0052  0.0428  20  GLN A N   
170  C CA  . GLN A 40  ? 0.3889 0.1748 0.4107 0.0223  0.0266  0.0280  20  GLN A CA  
171  C C   . GLN A 40  ? 0.4085 0.1679 0.4204 0.0451  0.0153  0.0142  20  GLN A C   
172  O O   . GLN A 40  ? 0.5120 0.1305 0.4253 0.0400  0.0315  -0.0023 20  GLN A O   
173  C CB  . GLN A 40  ? 0.3750 0.1748 0.4298 0.0169  0.0002  0.0145  20  GLN A CB  
174  C CG  . GLN A 40  ? 0.3813 0.1940 0.4384 0.0190  0.0114  0.0239  20  GLN A CG  
175  C CD  . GLN A 40  ? 0.4276 0.2465 0.4557 0.0404  0.0051  0.0297  20  GLN A CD  
176  O OE1 . GLN A 40  ? 0.4960 0.2673 0.5022 0.0364  -0.0221 0.0198  20  GLN A OE1 
177  N NE2 . GLN A 40  ? 0.4183 0.2535 0.4003 0.0779  0.0117  0.0027  20  GLN A NE2 
178  N N   . PHE A 41  ? 0.4342 0.0686 0.4334 0.0521  0.0099  0.0593  21  PHE A N   
179  C CA  . PHE A 41  ? 0.4581 0.1180 0.4595 0.0266  0.0089  0.0109  21  PHE A CA  
180  C C   . PHE A 41  ? 0.4664 0.1009 0.4404 0.0251  0.0044  0.0166  21  PHE A C   
181  O O   . PHE A 41  ? 0.4660 0.1000 0.4590 0.0608  0.0083  0.0099  21  PHE A O   
182  C CB  . PHE A 41  ? 0.4907 0.0894 0.4646 0.0651  0.0131  0.0389  21  PHE A CB  
183  C CG  . PHE A 41  ? 0.5224 0.1524 0.4669 0.0351  -0.0186 0.0457  21  PHE A CG  
184  C CD1 . PHE A 41  ? 0.5293 0.1436 0.4784 0.0153  -0.0175 0.0109  21  PHE A CD1 
185  C CD2 . PHE A 41  ? 0.4904 0.1157 0.4880 0.0204  -0.0147 0.0465  21  PHE A CD2 
186  C CE1 . PHE A 41  ? 0.5616 0.1768 0.4927 0.0059  -0.0261 0.0426  21  PHE A CE1 
187  C CE2 . PHE A 41  ? 0.5690 0.1066 0.5016 0.0408  -0.0513 0.0538  21  PHE A CE2 
188  C CZ  . PHE A 41  ? 0.5638 0.0830 0.5157 0.0116  -0.0293 0.0596  21  PHE A CZ  
189  N N   . SER A 42  ? 0.4384 0.0977 0.4259 0.0174  0.0024  -0.0032 22  SER A N   
190  C CA  . SER A 42  ? 0.4298 0.0849 0.4009 0.0064  -0.0221 -0.0136 22  SER A CA  
191  C C   . SER A 42  ? 0.4037 0.0831 0.3785 0.0060  -0.0254 0.0043  22  SER A C   
192  O O   . SER A 42  ? 0.3645 0.1151 0.3840 -0.0008 -0.0285 0.0227  22  SER A O   
193  C CB  . SER A 42  ? 0.4950 0.1498 0.4314 -0.0045 -0.0262 0.0299  22  SER A CB  
194  O OG  . SER A 42  ? 0.5625 0.1423 0.5191 0.0168  -0.0171 -0.0063 22  SER A OG  
195  N N   . ALA A 43  ? 0.4105 0.0987 0.3534 0.0198  -0.0271 -0.0083 23  ALA A N   
196  C CA  . ALA A 43  ? 0.3824 0.1126 0.3202 0.0178  -0.0250 -0.0033 23  ALA A CA  
197  C C   . ALA A 43  ? 0.3359 0.0836 0.3266 0.0414  -0.0177 0.0326  23  ALA A C   
198  O O   . ALA A 43  ? 0.3650 0.1185 0.3306 0.0432  0.0084  0.0143  23  ALA A O   
199  C CB  . ALA A 43  ? 0.4014 0.1076 0.3468 0.0083  -0.0392 0.0074  23  ALA A CB  
200  N N   . LEU A 44  ? 0.3349 0.1106 0.3026 0.0112  0.0022  0.0213  24  LEU A N   
201  C CA  . LEU A 44  ? 0.3541 0.0235 0.2899 -0.0233 0.0096  0.0275  24  LEU A CA  
202  C C   . LEU A 44  ? 0.3552 0.0282 0.3062 -0.0236 -0.0154 0.0439  24  LEU A C   
203  O O   . LEU A 44  ? 0.3836 0.1000 0.3199 0.0175  -0.0265 0.0333  24  LEU A O   
204  C CB  . LEU A 44  ? 0.3826 0.0856 0.3027 0.0011  -0.0097 0.0232  24  LEU A CB  
205  C CG  . LEU A 44  ? 0.3900 0.1373 0.3157 0.0150  -0.0088 0.0478  24  LEU A CG  
206  C CD1 . LEU A 44  ? 0.3981 0.1596 0.3185 0.0406  -0.0014 0.0149  24  LEU A CD1 
207  C CD2 . LEU A 44  ? 0.3962 0.1357 0.3248 -0.0230 -0.0068 0.0683  24  LEU A CD2 
208  N N   . ASN A 45  ? 0.3232 0.0092 0.2951 -0.0147 -0.0013 0.0123  25  ASN A N   
209  C CA  . ASN A 45  ? 0.3203 0.0273 0.2839 -0.0294 0.0109  0.0348  25  ASN A CA  
210  C C   . ASN A 45  ? 0.2962 0.0640 0.2891 -0.0185 -0.0041 0.0362  25  ASN A C   
211  O O   . ASN A 45  ? 0.3245 0.0772 0.3308 0.0048  0.0338  0.0115  25  ASN A O   
212  C CB  . ASN A 45  ? 0.3266 0.0598 0.2872 -0.0096 0.0102  0.0428  25  ASN A CB  
213  C CG  . ASN A 45  ? 0.3491 0.0583 0.2780 0.0010  0.0069  0.0440  25  ASN A CG  
214  O OD1 . ASN A 45  ? 0.3536 0.0646 0.3163 0.0251  0.0086  0.0147  25  ASN A OD1 
215  N ND2 . ASN A 45  ? 0.3594 0.1394 0.2755 0.0048  0.0004  0.0162  25  ASN A ND2 
216  N N   . VAL A 46  ? 0.3108 0.0549 0.2904 -0.0144 0.0037  -0.0030 26  VAL A N   
217  C CA  . VAL A 46  ? 0.3260 0.0733 0.2661 0.0127  -0.0088 0.0599  26  VAL A CA  
218  C C   . VAL A 46  ? 0.3030 0.0618 0.2385 0.0083  0.0087  0.0315  26  VAL A C   
219  O O   . VAL A 46  ? 0.2739 0.0839 0.2659 0.0173  0.0080  0.0235  26  VAL A O   
220  C CB  . VAL A 46  ? 0.3621 0.0828 0.2515 0.0083  0.0025  0.0528  26  VAL A CB  
221  C CG1 . VAL A 46  ? 0.3621 0.0787 0.2451 0.0210  -0.0171 0.0395  26  VAL A CG1 
222  C CG2 . VAL A 46  ? 0.3645 0.0826 0.2604 0.0055  0.0053  0.0553  26  VAL A CG2 
223  N N   . ILE A 47  ? 0.2963 0.0817 0.2493 0.0077  0.0078  0.0585  27  ILE A N   
224  C CA  . ILE A 47  ? 0.2859 0.0760 0.2214 0.0040  -0.0005 0.0333  27  ILE A CA  
225  C C   . ILE A 47  ? 0.2715 0.1058 0.2126 -0.0076 0.0236  0.0029  27  ILE A C   
226  O O   . ILE A 47  ? 0.2949 0.0621 0.2439 -0.0150 0.0266  0.0196  27  ILE A O   
227  C CB  . ILE A 47  ? 0.3246 0.1411 0.2235 0.0016  -0.0006 0.0150  27  ILE A CB  
228  C CG1 . ILE A 47  ? 0.3354 0.1241 0.2512 -0.0058 0.0065  0.0126  27  ILE A CG1 
229  C CG2 . ILE A 47  ? 0.3558 0.0912 0.2403 -0.0111 -0.0040 0.0031  27  ILE A CG2 
230  C CD1 . ILE A 47  ? 0.3581 0.1338 0.2683 0.0033  0.0059  -0.0005 27  ILE A CD1 
231  N N   . SER A 48  ? 0.2832 0.1187 0.2340 -0.0105 0.0227  0.0276  28  SER A N   
232  C CA  . SER A 48  ? 0.2932 0.0802 0.2326 -0.0137 0.0002  -0.0047 28  SER A CA  
233  C C   . SER A 48  ? 0.3045 0.0691 0.2425 -0.0209 0.0170  0.0214  28  SER A C   
234  O O   . SER A 48  ? 0.3311 0.0545 0.2426 0.0132  0.0097  0.0247  28  SER A O   
235  C CB  . SER A 48  ? 0.3276 0.0482 0.2612 0.0013  -0.0089 -0.0042 28  SER A CB  
236  O OG  . SER A 48  ? 0.3451 0.0436 0.2834 0.0155  0.0059  0.0004  28  SER A OG  
237  N N   . ARG A 49  ? 0.3070 0.1062 0.2261 -0.0112 0.0033  0.0157  29  ARG A N   
238  C CA  . ARG A 49  ? 0.3051 0.0992 0.2298 0.0147  -0.0060 0.0176  29  ARG A CA  
239  C C   . ARG A 49  ? 0.3050 0.1080 0.2505 0.0126  0.0136  0.0207  29  ARG A C   
240  O O   . ARG A 49  ? 0.3334 0.0736 0.2310 -0.0117 -0.0126 0.0394  29  ARG A O   
241  C CB  . ARG A 49  ? 0.3500 0.1303 0.2427 0.0092  -0.0138 0.0046  29  ARG A CB  
242  C CG  . ARG A 49  ? 0.3328 0.1476 0.2552 -0.0082 -0.0248 -0.0014 29  ARG A CG  
243  C CD  . ARG A 49  ? 0.3403 0.1369 0.2724 0.0144  -0.0262 0.0276  29  ARG A CD  
244  N NE  . ARG A 49  ? 0.3375 0.1730 0.2720 0.0095  -0.0338 0.0133  29  ARG A NE  
245  C CZ  . ARG A 49  ? 0.3477 0.1583 0.2916 -0.0162 -0.0243 0.0065  29  ARG A CZ  
246  N NH1 . ARG A 49  ? 0.3103 0.1390 0.3202 -0.0265 -0.0256 0.0213  29  ARG A NH1 
247  N NH2 . ARG A 49  ? 0.3348 0.2055 0.2987 -0.0324 -0.0272 0.0415  29  ARG A NH2 
248  N N   . VAL A 50  ? 0.2844 0.1273 0.2403 0.0275  0.0206  0.0288  30  VAL A N   
249  C CA  . VAL A 50  ? 0.3007 0.1261 0.2587 0.0267  -0.0047 0.0091  30  VAL A CA  
250  C C   . VAL A 50  ? 0.3027 0.0973 0.2523 -0.0153 0.0113  0.0329  30  VAL A C   
251  O O   . VAL A 50  ? 0.3347 0.0934 0.2503 0.0241  0.0054  0.0284  30  VAL A O   
252  C CB  . VAL A 50  ? 0.2728 0.1430 0.2560 0.0502  -0.0111 0.0046  30  VAL A CB  
253  C CG1 . VAL A 50  ? 0.2976 0.1451 0.2624 0.0359  -0.0217 0.0049  30  VAL A CG1 
254  C CG2 . VAL A 50  ? 0.3004 0.1451 0.2693 0.0557  -0.0006 0.0251  30  VAL A CG2 
255  N N   . ARG A 51  ? 0.3071 0.1203 0.2465 0.0020  -0.0040 0.0198  31  ARG A N   
256  C CA  . ARG A 51  ? 0.3223 0.0748 0.2589 0.0087  -0.0150 0.0307  31  ARG A CA  
257  C C   . ARG A 51  ? 0.3219 0.0877 0.2392 0.0114  -0.0137 0.0588  31  ARG A C   
258  O O   . ARG A 51  ? 0.3417 0.1736 0.2342 -0.0067 0.0240  0.0528  31  ARG A O   
259  C CB  . ARG A 51  ? 0.3325 0.1269 0.2855 -0.0038 -0.0189 0.0584  31  ARG A CB  
260  C CG  . ARG A 51  ? 0.3515 0.1684 0.2871 0.0162  -0.0154 0.0421  31  ARG A CG  
261  C CD  . ARG A 51  ? 0.3819 0.1511 0.2939 0.0181  -0.0142 0.0272  31  ARG A CD  
262  N NE  . ARG A 51  ? 0.3685 0.1543 0.3028 0.0243  -0.0106 0.0042  31  ARG A NE  
263  C CZ  . ARG A 51  ? 0.3785 0.1905 0.3408 0.0179  -0.0247 0.0187  31  ARG A CZ  
264  N NH1 . ARG A 51  ? 0.3767 0.2142 0.3443 -0.0059 -0.0386 0.0440  31  ARG A NH1 
265  N NH2 . ARG A 51  ? 0.3556 0.1410 0.3433 0.0116  -0.0250 0.0160  31  ARG A NH2 
266  N N   . VAL A 52  ? 0.3366 0.0833 0.2541 -0.0201 -0.0014 0.0466  32  VAL A N   
267  C CA  . VAL A 52  ? 0.3501 0.0738 0.2769 0.0038  -0.0092 0.0967  32  VAL A CA  
268  C C   . VAL A 52  ? 0.3855 0.1054 0.1516 0.0066  -0.0060 0.0778  32  VAL A C   
269  O O   . VAL A 52  ? 0.3467 0.1337 0.2538 0.0218  -0.0118 0.0772  32  VAL A O   
270  C CB  . VAL A 52  ? 0.3404 0.0162 0.3207 0.0020  -0.0227 0.0372  32  VAL A CB  
271  C CG1 . VAL A 52  ? 0.3528 0.0670 0.3236 -0.0214 0.0105  0.1009  32  VAL A CG1 
272  C CG2 . VAL A 52  ? 0.3365 0.0857 0.3257 0.0231  -0.0174 0.0242  32  VAL A CG2 
273  N N   . HIS A 53  ? 0.3666 0.1219 0.2453 0.0242  -0.0220 0.0786  33  HIS A N   
274  C CA  . HIS A 53  ? 0.3862 0.0965 0.2903 -0.0165 -0.0151 0.1124  33  HIS A CA  
275  C C   . HIS A 53  ? 0.3794 0.1062 0.3086 -0.0113 -0.0143 0.0891  33  HIS A C   
276  O O   . HIS A 53  ? 0.3748 0.1754 0.3153 -0.0250 -0.0169 0.0518  33  HIS A O   
277  C CB  . HIS A 53  ? 0.3765 0.0936 0.3276 -0.0099 -0.0216 0.0835  33  HIS A CB  
278  C CG  . HIS A 53  ? 0.3593 0.1040 0.3346 -0.0167 -0.0090 0.0601  33  HIS A CG  
279  N ND1 . HIS A 53  ? 0.3423 0.1525 0.3166 -0.0086 -0.0246 0.0555  33  HIS A ND1 
280  C CD2 . HIS A 53  ? 0.3581 0.1431 0.3367 -0.0286 -0.0042 0.0428  33  HIS A CD2 
281  C CE1 . HIS A 53  ? 0.3464 0.1121 0.3231 -0.0173 -0.0166 0.0331  33  HIS A CE1 
282  N NE2 . HIS A 53  ? 0.3516 0.1216 0.3179 -0.0082 -0.0152 0.0602  33  HIS A NE2 
283  N N   . GLY A 54  ? 0.3718 0.1582 0.3138 -0.0217 -0.0224 0.1019  34  GLY A N   
284  C CA  . GLY A 54  ? 0.4094 0.1580 0.3382 -0.0139 -0.0334 0.1605  34  GLY A CA  
285  C C   . GLY A 54  ? 0.4115 0.1796 0.3351 -0.0186 -0.0135 0.1702  34  GLY A C   
286  O O   . GLY A 54  ? 0.4168 0.2437 0.3922 -0.0027 -0.0146 0.0893  34  GLY A O   
287  N N   . ARG A 55  ? 0.4158 0.1232 0.4337 -0.0248 -0.0081 0.1552  35  ARG A N   
288  C CA  . ARG A 55  ? 0.3953 0.2337 0.4059 -0.0167 -0.0106 0.1328  35  ARG A CA  
289  C C   . ARG A 55  ? 0.3542 0.2977 0.3945 -0.0089 -0.0149 0.1020  35  ARG A C   
290  O O   . ARG A 55  ? 0.4387 0.3672 0.3925 0.0124  -0.0331 0.1095  35  ARG A O   
291  C CB  . ARG A 55  ? 0.4305 0.2633 0.4243 -0.0341 -0.0022 0.1343  35  ARG A CB  
292  C CG  . ARG A 55  ? 0.4606 0.3259 0.4339 -0.0408 -0.0077 0.1181  35  ARG A CG  
293  C CD  . ARG A 55  ? 0.4986 0.3475 0.4565 -0.0628 0.0106  0.1073  35  ARG A CD  
294  N NE  . ARG A 55  ? 0.4949 0.3742 0.4769 -0.0454 0.0066  0.0853  35  ARG A NE  
295  C CZ  . ARG A 55  ? 0.5196 0.4240 0.5014 -0.0496 0.0068  0.0672  35  ARG A CZ  
296  N NH1 . ARG A 55  ? 0.5154 0.3731 0.4741 -0.0491 0.0176  0.0560  35  ARG A NH1 
297  N NH2 . ARG A 55  ? 0.5862 0.4850 0.5771 -0.0671 -0.0029 0.0118  35  ARG A NH2 
298  N N   . LEU A 56  ? 0.3649 0.2942 0.3854 0.0027  0.0087  0.0808  36  LEU A N   
299  C CA  . LEU A 56  ? 0.3339 0.3072 0.3621 -0.0110 0.0134  0.0960  36  LEU A CA  
300  C C   . LEU A 56  ? 0.3862 0.3029 0.3540 0.0074  -0.0040 0.0842  36  LEU A C   
301  O O   . LEU A 56  ? 0.4666 0.4024 0.4014 -0.0182 -0.0142 0.0277  36  LEU A O   
302  C CB  . LEU A 56  ? 0.3772 0.2909 0.4018 -0.0066 0.0144  0.0978  36  LEU A CB  
303  C CG  . LEU A 56  ? 0.4103 0.2727 0.3869 -0.0106 0.0132  0.0933  36  LEU A CG  
304  C CD1 . LEU A 56  ? 0.4387 0.2544 0.3420 0.0300  -0.0174 0.1052  36  LEU A CD1 
305  C CD2 . LEU A 56  ? 0.4694 0.2224 0.4215 -0.0007 0.0107  0.0786  36  LEU A CD2 
306  N N   . SER A 57  ? 0.3857 0.2625 0.3494 0.0103  -0.0177 0.0877  37  SER A N   
307  C CA  . SER A 57  ? 0.3843 0.2806 0.3847 -0.0014 -0.0048 0.1060  37  SER A CA  
308  C C   . SER A 57  ? 0.3340 0.2527 0.3286 0.0010  -0.0066 0.0781  37  SER A C   
309  O O   . SER A 57  ? 0.3367 0.3232 0.3169 0.0043  -0.0102 0.0925  37  SER A O   
310  C CB  . SER A 57  ? 0.4484 0.2122 0.4527 0.0139  0.0212  0.1552  37  SER A CB  
311  O OG  . SER A 57  ? 0.4674 0.1675 0.4731 0.0170  0.0281  0.1003  37  SER A OG  
312  N N   . ILE A 58  ? 0.3672 0.3357 0.3390 -0.0255 -0.0270 0.0437  38  ILE A N   
313  C CA  . ILE A 58  ? 0.4328 0.3222 0.3325 -0.0187 -0.0473 0.0763  38  ILE A CA  
314  C C   . ILE A 58  ? 0.4013 0.2427 0.3223 -0.0115 -0.0086 0.0889  38  ILE A C   
315  O O   . ILE A 58  ? 0.4277 0.1526 0.3173 -0.0054 -0.0335 0.0702  38  ILE A O   
316  C CB  . ILE A 58  ? 0.4501 0.3333 0.3223 -0.0328 -0.0724 0.0679  38  ILE A CB  
317  C CG1 . ILE A 58  ? 0.5072 0.4543 0.3770 -0.0713 -0.0490 0.0844  38  ILE A CG1 
318  C CG2 . ILE A 58  ? 0.5263 0.3420 0.3673 -0.0257 -0.0729 0.0475  38  ILE A CG2 
319  C CD1 . ILE A 58  ? 0.5266 0.5133 0.3456 -0.0885 -0.0722 0.1086  38  ILE A CD1 
320  N N   . ASP A 59  ? 0.3940 0.2267 0.3147 0.0274  -0.0141 0.1188  39  ASP A N   
321  C CA  . ASP A 59  ? 0.3925 0.2371 0.3309 -0.0010 0.0077  0.1200  39  ASP A CA  
322  C C   . ASP A 59  ? 0.3656 0.2203 0.3270 -0.0178 0.0034  0.1386  39  ASP A C   
323  O O   . ASP A 59  ? 0.3490 0.2078 0.3155 -0.0072 -0.0018 0.1306  39  ASP A O   
324  C CB  . ASP A 59  ? 0.4404 0.2798 0.3546 0.0252  0.0344  0.1306  39  ASP A CB  
325  C CG  . ASP A 59  ? 0.4900 0.3610 0.3787 0.0801  0.0336  0.1072  39  ASP A CG  
326  O OD1 . ASP A 59  ? 0.6043 0.3823 0.4835 0.1093  0.0045  0.0846  39  ASP A OD1 
327  O OD2 . ASP A 59  ? 0.5035 0.4858 0.4204 0.1453  0.0172  0.1392  39  ASP A OD2 
328  N N   . ASP A 60  ? 0.3598 0.2333 0.2970 -0.0067 -0.0071 0.1133  40  ASP A N   
329  C CA  . ASP A 60  ? 0.3729 0.1976 0.3049 -0.0111 -0.0102 0.0917  40  ASP A CA  
330  C C   . ASP A 60  ? 0.3460 0.1783 0.2696 -0.0084 -0.0100 0.0663  40  ASP A C   
331  O O   . ASP A 60  ? 0.3628 0.1270 0.2868 -0.0155 -0.0072 0.0838  40  ASP A O   
332  C CB  . ASP A 60  ? 0.4073 0.2078 0.3600 -0.0065 -0.0022 0.0968  40  ASP A CB  
333  C CG  . ASP A 60  ? 0.4255 0.2394 0.4361 -0.0032 0.0138  0.1300  40  ASP A CG  
334  O OD1 . ASP A 60  ? 0.4516 0.2505 0.5253 -0.0195 0.0407  0.1340  40  ASP A OD1 
335  O OD2 . ASP A 60  ? 0.4530 0.2212 0.5077 0.0190  0.0143  0.1522  40  ASP A OD2 
336  N N   . LEU A 61  ? 0.3375 0.1531 0.2756 0.0175  -0.0273 0.0814  41  LEU A N   
337  C CA  . LEU A 61  ? 0.3267 0.1989 0.2595 -0.0160 -0.0041 0.0929  41  LEU A CA  
338  C C   . LEU A 61  ? 0.3282 0.2189 0.2694 -0.0195 0.0067  0.0823  41  LEU A C   
339  O O   . LEU A 61  ? 0.3632 0.1525 0.2893 0.0014  0.0015  0.1172  41  LEU A O   
340  C CB  . LEU A 61  ? 0.3327 0.1574 0.2847 -0.0195 0.0028  0.0986  41  LEU A CB  
341  C CG  . LEU A 61  ? 0.3262 0.1614 0.3120 -0.0234 -0.0074 0.0780  41  LEU A CG  
342  C CD1 . LEU A 61  ? 0.3601 0.2080 0.3380 -0.0428 -0.0039 0.0614  41  LEU A CD1 
343  C CD2 . LEU A 61  ? 0.3400 0.1624 0.3093 0.0000  -0.0156 0.0990  41  LEU A CD2 
344  N N   . ARG A 62  ? 0.3403 0.1821 0.2579 0.0093  0.0207  0.0743  42  ARG A N   
345  C CA  . ARG A 62  ? 0.3538 0.1671 0.2912 0.0174  0.0219  0.1139  42  ARG A CA  
346  C C   . ARG A 62  ? 0.3378 0.2119 0.2793 0.0300  0.0244  0.0792  42  ARG A C   
347  O O   . ARG A 62  ? 0.3813 0.2031 0.3100 -0.0042 0.0124  0.1004  42  ARG A O   
348  C CB  . ARG A 62  ? 0.4173 0.2251 0.3064 0.0344  0.0240  0.1125  42  ARG A CB  
349  C CG  . ARG A 62  ? 0.4751 0.2847 0.3886 0.0529  0.0319  0.1345  42  ARG A CG  
350  C CD  . ARG A 62  ? 0.4888 0.3200 0.4948 0.0905  0.0499  0.0812  42  ARG A CD  
351  N NE  . ARG A 62  ? 0.4908 0.3769 0.4941 0.0906  0.0640  0.1135  42  ARG A NE  
352  C CZ  . ARG A 62  ? 0.4845 0.3597 0.4573 0.0589  0.0766  0.1305  42  ARG A CZ  
353  N NH1 . ARG A 62  ? 0.4906 0.3408 0.3989 0.0637  0.0673  0.1713  42  ARG A NH1 
354  N NH2 . ARG A 62  ? 0.4443 0.4310 0.4167 0.0972  0.0574  0.1122  42  ARG A NH2 
355  N N   . ARG A 63  ? 0.3809 0.2267 0.3092 0.0102  0.0052  0.0923  43  ARG A N   
356  C CA  . ARG A 63  ? 0.3795 0.2522 0.3706 0.0136  0.0016  0.0840  43  ARG A CA  
357  C C   . ARG A 63  ? 0.3653 0.1974 0.3819 -0.0218 0.0101  0.0515  43  ARG A C   
358  O O   . ARG A 63  ? 0.3627 0.2035 0.3701 -0.0350 0.0064  0.0518  43  ARG A O   
359  C CB  . ARG A 63  ? 0.4273 0.2365 0.4302 0.0331  -0.0517 0.0739  43  ARG A CB  
360  C CG  . ARG A 63  ? 0.4542 0.3117 0.5110 0.0334  -0.0510 0.0696  43  ARG A CG  
361  C CD  . ARG A 63  ? 0.4644 0.2466 0.4690 0.0200  -0.0007 0.0851  43  ARG A CD  
362  N NE  . ARG A 63  ? 0.4392 0.3126 0.5261 0.0942  -0.0123 0.0939  43  ARG A NE  
363  C CZ  . ARG A 63  ? 0.4131 0.3171 0.5489 0.0448  0.0120  0.0883  43  ARG A CZ  
364  N NH1 . ARG A 63  ? 0.3983 0.3265 0.5271 0.0527  0.0201  0.0678  43  ARG A NH1 
365  N NH2 . ARG A 63  ? 0.4135 0.2060 0.5076 0.0550  0.0070  0.1210  43  ARG A NH2 
366  N N   . GLY A 64  ? 0.3528 0.2073 0.3464 -0.0086 -0.0082 0.0535  44  GLY A N   
367  C CA  . GLY A 64  ? 0.3401 0.1549 0.3447 -0.0288 -0.0102 0.0689  44  GLY A CA  
368  C C   . GLY A 64  ? 0.3412 0.1495 0.3015 -0.0059 -0.0115 0.0714  44  GLY A C   
369  O O   . GLY A 64  ? 0.3714 0.0976 0.3086 -0.0203 -0.0146 0.0594  44  GLY A O   
370  N N   . LEU A 65  ? 0.3427 0.2019 0.2386 0.0008  -0.0096 0.0757  45  LEU A N   
371  C CA  . LEU A 65  ? 0.3300 0.1651 0.2717 -0.0016 -0.0021 0.0713  45  LEU A CA  
372  C C   . LEU A 65  ? 0.3444 0.1827 0.2880 0.0115  -0.0083 0.0572  45  LEU A C   
373  O O   . LEU A 65  ? 0.3672 0.1534 0.2796 -0.0380 -0.0355 0.0659  45  LEU A O   
374  C CB  . LEU A 65  ? 0.3490 0.2116 0.2671 -0.0028 0.0073  0.0540  45  LEU A CB  
375  C CG  . LEU A 65  ? 0.3617 0.2141 0.2867 -0.0132 0.0202  0.0251  45  LEU A CG  
376  C CD1 . LEU A 65  ? 0.3725 0.1673 0.2900 0.0054  0.0194  0.0244  45  LEU A CD1 
377  C CD2 . LEU A 65  ? 0.3685 0.1950 0.3110 -0.0395 0.0263  0.0437  45  LEU A CD2 
378  N N   . ASP A 66  ? 0.3107 0.1518 0.3084 0.0282  0.0037  0.0860  46  ASP A N   
379  C CA  . ASP A 66  ? 0.3289 0.1743 0.3190 0.0140  0.0246  0.0729  46  ASP A CA  
380  C C   . ASP A 66  ? 0.2903 0.1707 0.3051 0.0137  0.0120  0.0646  46  ASP A C   
381  O O   . ASP A 66  ? 0.3728 0.1423 0.3128 0.0077  -0.0068 0.0692  46  ASP A O   
382  C CB  . ASP A 66  ? 0.3674 0.2241 0.3385 0.0066  0.0280  0.0745  46  ASP A CB  
383  C CG  . ASP A 66  ? 0.4350 0.3768 0.3486 0.0120  0.0579  0.0609  46  ASP A CG  
384  O OD1 . ASP A 66  ? 0.5031 0.4110 0.4290 0.0632  0.0643  0.0287  46  ASP A OD1 
385  O OD2 . ASP A 66  ? 0.4717 0.5453 0.3528 0.0076  0.1009  0.0727  46  ASP A OD2 
386  N N   . ALA A 67  ? 0.3203 0.1098 0.3019 0.0204  -0.0099 0.1052  47  ALA A N   
387  C CA  . ALA A 67  ? 0.3240 0.1412 0.2902 0.0118  -0.0061 0.0630  47  ALA A CA  
388  C C   . ALA A 67  ? 0.3138 0.1178 0.2913 0.0037  0.0038  0.0399  47  ALA A C   
389  O O   . ALA A 67  ? 0.3654 0.1118 0.2670 -0.0116 0.0001  0.0671  47  ALA A O   
390  C CB  . ALA A 67  ? 0.3308 0.1679 0.3531 0.0173  -0.0176 0.0664  47  ALA A CB  
391  N N   . LEU A 68  ? 0.3289 0.1389 0.2522 -0.0112 0.0163  0.0340  48  LEU A N   
392  C CA  . LEU A 68  ? 0.2845 0.1355 0.2643 0.0027  0.0234  0.0447  48  LEU A CA  
393  C C   . LEU A 68  ? 0.2846 0.1087 0.2496 -0.0037 0.0173  0.0432  48  LEU A C   
394  O O   . LEU A 68  ? 0.3388 0.1072 0.2474 0.0064  0.0204  0.0250  48  LEU A O   
395  C CB  . LEU A 68  ? 0.2974 0.1422 0.2591 -0.0027 0.0141  0.0307  48  LEU A CB  
396  C CG  . LEU A 68  ? 0.3130 0.1544 0.2799 -0.0161 0.0039  0.0461  48  LEU A CG  
397  C CD1 . LEU A 68  ? 0.3171 0.1423 0.2897 -0.0039 0.0110  0.0558  48  LEU A CD1 
398  C CD2 . LEU A 68  ? 0.3105 0.1709 0.2906 -0.0320 0.0009  0.0588  48  LEU A CD2 
399  N N   . GLN A 69  ? 0.3192 0.1459 0.2492 -0.0087 0.0035  0.0515  49  GLN A N   
400  C CA  . GLN A 69  ? 0.3212 0.1142 0.2572 0.0007  0.0246  0.0628  49  GLN A CA  
401  C C   . GLN A 69  ? 0.3183 0.1050 0.2668 -0.0041 0.0117  0.0621  49  GLN A C   
402  O O   . GLN A 69  ? 0.3529 0.1757 0.2353 0.0022  -0.0024 0.0472  49  GLN A O   
403  C CB  . GLN A 69  ? 0.3558 0.1080 0.2474 0.0109  0.0119  0.0602  49  GLN A CB  
404  C CG  . GLN A 69  ? 0.3690 0.1285 0.2850 0.0284  0.0134  0.0566  49  GLN A CG  
405  C CD  . GLN A 69  ? 0.3818 0.1650 0.2686 0.0009  0.0183  0.0449  49  GLN A CD  
406  O OE1 . GLN A 69  ? 0.3942 0.1584 0.2902 0.0026  0.0471  0.0540  49  GLN A OE1 
407  N NE2 . GLN A 69  ? 0.3429 0.1454 0.2580 0.0208  0.0184  0.0569  49  GLN A NE2 
408  N N   . ALA A 70  ? 0.3370 0.0843 0.2701 -0.0105 -0.0129 0.0567  50  ALA A N   
409  C CA  . ALA A 70  ? 0.3318 0.1248 0.2843 -0.0055 -0.0102 0.0668  50  ALA A CA  
410  C C   . ALA A 70  ? 0.3146 0.1200 0.2901 -0.0221 -0.0025 0.0652  50  ALA A C   
411  O O   . ALA A 70  ? 0.3112 0.1596 0.3062 -0.0074 -0.0140 0.0393  50  ALA A O   
412  C CB  . ALA A 70  ? 0.3690 0.1310 0.2978 -0.0147 -0.0001 0.0589  50  ALA A CB  
413  N N   . ARG A 71  ? 0.3253 0.1118 0.2564 -0.0150 -0.0033 0.0509  51  ARG A N   
414  C CA  . ARG A 71  ? 0.3246 0.0838 0.2651 -0.0230 0.0091  0.0316  51  ARG A CA  
415  C C   . ARG A 71  ? 0.3261 0.1441 0.2446 -0.0124 0.0015  0.0447  51  ARG A C   
416  O O   . ARG A 71  ? 0.3269 0.1235 0.2715 -0.0111 -0.0207 0.0258  51  ARG A O   
417  C CB  . ARG A 71  ? 0.3066 0.1335 0.2792 -0.0408 0.0020  0.0348  51  ARG A CB  
418  C CG  . ARG A 71  ? 0.3073 0.1258 0.2855 -0.0320 -0.0093 0.0250  51  ARG A CG  
419  C CD  . ARG A 71  ? 0.3111 0.0885 0.3055 -0.0379 0.0151  0.0461  51  ARG A CD  
420  N NE  . ARG A 71  ? 0.3373 0.0694 0.3291 -0.0454 0.0026  0.0285  51  ARG A NE  
421  C CZ  . ARG A 71  ? 0.3576 0.1182 0.3356 -0.0130 0.0066  0.0372  51  ARG A CZ  
422  N NH1 . ARG A 71  ? 0.3456 0.0921 0.3380 0.0262  -0.0053 0.0114  51  ARG A NH1 
423  N NH2 . ARG A 71  ? 0.3416 0.0870 0.3450 -0.0307 0.0069  0.0218  51  ARG A NH2 
424  N N   . HIS A 72  ? 0.3377 0.1675 0.2228 -0.0291 0.0066  0.0285  52  HIS A N   
425  C CA  . HIS A 72  ? 0.3274 0.1488 0.2674 0.0055  0.0064  0.0384  52  HIS A CA  
426  C C   . HIS A 72  ? 0.3003 0.1310 0.2566 -0.0153 0.0101  0.0411  52  HIS A C   
427  O O   . HIS A 72  ? 0.3410 0.1404 0.2443 0.0069  0.0337  0.0436  52  HIS A O   
428  C CB  . HIS A 72  ? 0.3007 0.1176 0.2793 0.0064  0.0134  0.0584  52  HIS A CB  
429  C CG  . HIS A 72  ? 0.2897 0.1200 0.2783 -0.0167 0.0017  0.0253  52  HIS A CG  
430  N ND1 . HIS A 72  ? 0.3205 0.1089 0.2868 -0.0112 0.0130  0.0326  52  HIS A ND1 
431  C CD2 . HIS A 72  ? 0.3177 0.0886 0.2411 -0.0247 0.0012  0.0328  52  HIS A CD2 
432  C CE1 . HIS A 72  ? 0.2970 0.1228 0.2717 -0.0206 0.0090  0.0317  52  HIS A CE1 
433  N NE2 . HIS A 72  ? 0.3101 0.1199 0.2863 -0.0353 0.0119  0.0498  52  HIS A NE2 
434  N N   . PRO A 73  ? 0.3204 0.1354 0.2611 0.0026  -0.0049 0.0318  53  PRO A N   
435  C CA  . PRO A 73  ? 0.3209 0.1120 0.2947 -0.0160 -0.0098 0.0415  53  PRO A CA  
436  C C   . PRO A 73  ? 0.3190 0.1203 0.2457 -0.0204 -0.0033 0.0233  53  PRO A C   
437  O O   . PRO A 73  ? 0.3290 0.1576 0.2642 -0.0047 0.0073  0.0538  53  PRO A O   
438  C CB  . PRO A 73  ? 0.3363 0.1194 0.2986 -0.0251 -0.0323 0.0334  53  PRO A CB  
439  C CG  . PRO A 73  ? 0.3708 0.1621 0.3027 -0.0084 -0.0193 0.0196  53  PRO A CG  
440  C CD  . PRO A 73  ? 0.3410 0.1281 0.2774 -0.0091 -0.0148 0.0343  53  PRO A CD  
441  N N   . LEU A 74  ? 0.3253 0.1040 0.2250 -0.0045 0.0103  0.0013  54  LEU A N   
442  C CA  . LEU A 74  ? 0.3287 0.0834 0.2259 0.0042  0.0090  0.0095  54  LEU A CA  
443  C C   . LEU A 74  ? 0.3301 0.1241 0.2302 0.0167  0.0091  0.0130  54  LEU A C   
444  O O   . LEU A 74  ? 0.3446 0.1343 0.2695 -0.0079 0.0196  0.0027  54  LEU A O   
445  C CB  . LEU A 74  ? 0.3452 0.1350 0.2236 -0.0205 0.0043  -0.0033 54  LEU A CB  
446  C CG  . LEU A 74  ? 0.3372 0.1776 0.2682 -0.0151 -0.0041 0.0380  54  LEU A CG  
447  C CD1 . LEU A 74  ? 0.3493 0.1420 0.2575 -0.0283 0.0005  0.0375  54  LEU A CD1 
448  C CD2 . LEU A 74  ? 0.3601 0.1811 0.2786 0.0024  -0.0134 0.0299  54  LEU A CD2 
449  N N   . LEU A 75  ? 0.3078 0.1156 0.2330 0.0333  -0.0003 0.0214  55  LEU A N   
450  C CA  . LEU A 75  ? 0.3044 0.0588 0.2495 0.0277  0.0067  0.0227  55  LEU A CA  
451  C C   . LEU A 75  ? 0.3311 0.0710 0.2535 0.0055  0.0152  0.0294  55  LEU A C   
452  O O   . LEU A 75  ? 0.3664 0.1060 0.2670 0.0071  0.0180  0.0321  55  LEU A O   
453  C CB  . LEU A 75  ? 0.3193 0.0849 0.2469 0.0372  0.0011  0.0273  55  LEU A CB  
454  C CG  . LEU A 75  ? 0.3111 0.1138 0.2630 0.0200  -0.0058 0.0087  55  LEU A CG  
455  C CD1 . LEU A 75  ? 0.3261 0.1448 0.2963 0.0305  -0.0037 0.0256  55  LEU A CD1 
456  C CD2 . LEU A 75  ? 0.3236 0.1504 0.2724 -0.0056 0.0248  0.0050  55  LEU A CD2 
457  N N   . ARG A 76  ? 0.3402 0.1467 0.2531 0.0001  0.0128  0.0400  56  ARG A N   
458  C CA  . ARG A 76  ? 0.3220 0.1671 0.2817 0.0106  0.0153  0.0532  56  ARG A CA  
459  C C   . ARG A 76  ? 0.2999 0.1950 0.2800 0.0106  0.0177  0.0630  56  ARG A C   
460  O O   . ARG A 76  ? 0.3355 0.1665 0.3156 0.0026  0.0100  0.0590  56  ARG A O   
461  C CB  . ARG A 76  ? 0.3372 0.2127 0.2881 -0.0193 0.0433  0.0683  56  ARG A CB  
462  C CG  . ARG A 76  ? 0.3305 0.1891 0.3138 -0.0263 0.0120  0.0722  56  ARG A CG  
463  C CD  . ARG A 76  ? 0.3589 0.2098 0.3032 -0.0402 0.0371  0.0737  56  ARG A CD  
464  N NE  . ARG A 76  ? 0.3706 0.1620 0.3090 -0.0167 0.0172  0.0818  56  ARG A NE  
465  C CZ  . ARG A 76  ? 0.3975 0.1861 0.3086 -0.0236 0.0072  0.0588  56  ARG A CZ  
466  N NH1 . ARG A 76  ? 0.4630 0.2186 0.3224 -0.0180 0.0032  0.0421  56  ARG A NH1 
467  N NH2 . ARG A 76  ? 0.4019 0.2044 0.3272 -0.0294 0.0128  0.0483  56  ARG A NH2 
468  N N   . ALA A 77  ? 0.3210 0.1519 0.3150 0.0135  0.0237  0.0469  57  ALA A N   
469  C CA  . ALA A 77  ? 0.3370 0.1865 0.3276 0.0223  -0.0094 0.0514  57  ALA A CA  
470  C C   . ALA A 77  ? 0.3175 0.1897 0.2901 0.0127  0.0065  0.0487  57  ALA A C   
471  O O   . ALA A 77  ? 0.3149 0.2050 0.3112 0.0388  0.0107  0.0687  57  ALA A O   
472  C CB  . ALA A 77  ? 0.3998 0.1192 0.3384 0.0287  0.0000  0.0557  57  ALA A CB  
473  N N   . ARG A 78  ? 0.2914 0.1845 0.2903 0.0101  0.0045  0.0293  58  ARG A N   
474  C CA  . ARG A 78  ? 0.3018 0.1872 0.2966 0.0067  -0.0070 0.0427  58  ARG A CA  
475  C C   . ARG A 78  ? 0.3039 0.1845 0.2872 0.0251  -0.0145 0.0308  58  ARG A C   
476  O O   . ARG A 78  ? 0.3223 0.1540 0.2913 0.0077  -0.0117 0.0675  58  ARG A O   
477  C CB  . ARG A 78  ? 0.3303 0.1705 0.3244 0.0405  -0.0057 0.0405  58  ARG A CB  
478  C CG  . ARG A 78  ? 0.3433 0.2109 0.3644 0.0367  0.0179  0.0344  58  ARG A CG  
479  C CD  . ARG A 78  ? 0.3798 0.1857 0.3601 0.0042  0.0261  0.0490  58  ARG A CD  
480  N NE  . ARG A 78  ? 0.4167 0.2620 0.3887 0.0344  0.0241  0.0628  58  ARG A NE  
481  C CZ  . ARG A 78  ? 0.4319 0.3209 0.4197 0.0738  0.0178  0.0254  58  ARG A CZ  
482  N NH1 . ARG A 78  ? 0.4439 0.3339 0.4585 0.0889  -0.0083 -0.0136 58  ARG A NH1 
483  N NH2 . ARG A 78  ? 0.4440 0.3768 0.4540 0.0910  -0.0142 0.0231  58  ARG A NH2 
484  N N   . ILE A 79  ? 0.3595 0.1962 0.3230 0.0139  0.0046  0.0657  59  ILE A N   
485  C CA  . ILE A 79  ? 0.3414 0.2274 0.3372 0.0679  -0.0023 0.0687  59  ILE A CA  
486  C C   . ILE A 79  ? 0.3828 0.1724 0.3495 0.0385  0.0079  0.0605  59  ILE A C   
487  O O   . ILE A 79  ? 0.4304 0.2514 0.3699 0.0963  0.0000  0.0459  59  ILE A O   
488  C CB  . ILE A 79  ? 0.3545 0.2271 0.3379 0.0465  0.0034  0.1090  59  ILE A CB  
489  C CG1 . ILE A 79  ? 0.3346 0.2751 0.3685 0.0219  0.0099  0.1050  59  ILE A CG1 
490  C CG2 . ILE A 79  ? 0.3657 0.2374 0.3914 0.0520  0.0165  0.1358  59  ILE A CG2 
491  C CD1 . ILE A 79  ? 0.3755 0.3351 0.4159 0.0250  0.0240  0.1087  59  ILE A CD1 
492  N N   . GLU A 80  ? 0.3988 0.2043 0.4099 0.0548  0.0121  0.0873  60  GLU A N   
493  C CA  . GLU A 80  ? 0.4140 0.2587 0.4385 0.0801  0.0285  0.0908  60  GLU A CA  
494  C C   . GLU A 80  ? 0.4300 0.2774 0.4514 0.0713  0.0333  0.0940  60  GLU A C   
495  O O   . GLU A 80  ? 0.4492 0.2785 0.4261 0.0862  0.0020  0.1385  60  GLU A O   
496  C CB  . GLU A 80  ? 0.4394 0.3619 0.5180 0.0602  0.0141  0.0792  60  GLU A CB  
497  C CG  . GLU A 80  ? 0.5164 0.4258 0.5734 0.0703  0.0250  0.0671  60  GLU A CG  
498  C CD  . GLU A 80  ? 0.5428 0.5003 0.6351 0.0238  0.0296  0.1009  60  GLU A CD  
499  O OE1 . GLU A 80  ? 0.6495 0.4774 0.7090 0.0278  0.1376  0.1439  60  GLU A OE1 
500  O OE2 . GLU A 80  ? 0.5245 0.5094 0.6262 -0.0276 -0.0235 0.0643  60  GLU A OE2 
501  N N   . HIS A 81  ? 0.4507 0.2360 0.4347 0.0935  0.0341  0.1127  61  HIS A N   
502  C CA  . HIS A 81  ? 0.4593 0.2619 0.4644 0.1176  0.0215  0.1456  61  HIS A CA  
503  C C   . HIS A 81  ? 0.4779 0.2973 0.4911 0.1326  0.0822  0.1179  61  HIS A C   
504  O O   . HIS A 81  ? 0.4309 0.3299 0.5436 0.1274  0.1216  0.1348  61  HIS A O   
505  C CB  . HIS A 81  ? 0.4394 0.2095 0.4636 0.1562  0.0071  0.1547  61  HIS A CB  
506  C CG  . HIS A 81  ? 0.4945 0.2029 0.4828 0.0998  0.0342  0.0951  61  HIS A CG  
507  N ND1 . HIS A 81  ? 0.5386 0.1810 0.5295 0.1128  0.0352  0.0769  61  HIS A ND1 
508  C CD2 . HIS A 81  ? 0.4917 0.2369 0.4558 0.0773  0.0212  0.1226  61  HIS A CD2 
509  C CE1 . HIS A 81  ? 0.5226 0.2141 0.5010 0.0844  0.0120  0.1037  61  HIS A CE1 
510  N NE2 . HIS A 81  ? 0.4927 0.2484 0.5104 0.1096  0.0177  0.0994  61  HIS A NE2 
511  N N   . ASP A 82  ? 0.4717 0.2934 0.5316 0.1435  0.0769  0.1365  62  ASP A N   
512  C CA  . ASP A 82  ? 0.5299 0.3228 0.6022 0.1425  0.0679  0.0934  62  ASP A CA  
513  C C   . ASP A 82  ? 0.5177 0.3536 0.6406 0.1205  0.1003  0.0897  62  ASP A C   
514  O O   . ASP A 82  ? 0.5120 0.3262 0.6626 0.1434  0.1442  0.1230  62  ASP A O   
515  C CB  . ASP A 82  ? 0.5378 0.3363 0.6327 0.1530  0.0407  0.1412  62  ASP A CB  
516  C CG  . ASP A 82  ? 0.5481 0.4151 0.6365 0.1434  0.0213  0.1469  62  ASP A CG  
517  O OD1 . ASP A 82  ? 0.4872 0.4467 0.7075 0.1522  0.0304  0.2059  62  ASP A OD1 
518  O OD2 . ASP A 82  ? 0.5980 0.3599 0.6116 0.1808  -0.0091 0.1590  62  ASP A OD2 
519  N N   . ALA A 83  ? 0.5211 0.2820 0.6504 0.1315  0.0791  0.0501  63  ALA A N   
520  C CA  . ALA A 83  ? 0.5458 0.3860 0.6525 0.0696  0.0863  0.0300  63  ALA A CA  
521  C C   . ALA A 83  ? 0.5369 0.2171 0.6448 0.1120  0.0776  0.0780  63  ALA A C   
522  O O   . ALA A 83  ? 0.5181 0.1696 0.7630 0.0961  0.0756  0.0665  63  ALA A O   
523  C CB  . ALA A 83  ? 0.3799 0.3799 0.3799 0.0000  0.0000  0.0000  63  ALA A CB  
524  N N   . GLY A 84  ? 0.4945 0.2642 0.6347 0.1494  0.0523  0.0736  64  GLY A N   
525  C CA  . GLY A 84  ? 0.5164 0.2131 0.5798 0.1080  0.0633  0.1408  64  GLY A CA  
526  C C   . GLY A 84  ? 0.5179 0.2401 0.5914 0.1021  0.0491  0.1489  64  GLY A C   
527  O O   . GLY A 84  ? 0.4932 0.3258 0.6064 0.0975  0.0352  0.2215  64  GLY A O   
528  N N   . LEU A 85  ? 0.4803 0.2789 0.5847 0.1152  0.0516  0.1822  65  LEU A N   
529  C CA  . LEU A 85  ? 0.4484 0.3116 0.5860 0.0948  0.0353  0.1903  65  LEU A CA  
530  C C   . LEU A 85  ? 0.4588 0.3876 0.5562 0.1145  0.0093  0.1731  65  LEU A C   
531  O O   . LEU A 85  ? 0.4309 0.3714 0.5294 0.1209  0.0413  0.2005  65  LEU A O   
532  C CB  . LEU A 85  ? 0.4775 0.3612 0.6149 0.1362  0.0436  0.1869  65  LEU A CB  
533  C CG  . LEU A 85  ? 0.4765 0.2961 0.6456 0.1576  0.0521  0.1833  65  LEU A CG  
534  C CD1 . LEU A 85  ? 0.4808 0.2605 0.6876 0.1737  0.0682  0.1501  65  LEU A CD1 
535  C CD2 . LEU A 85  ? 0.4418 0.2496 0.6832 0.2150  0.0554  0.1735  65  LEU A CD2 
536  N N   . ASP A 86  ? 0.4777 0.4349 0.5659 0.1125  0.0076  0.1626  66  ASP A N   
537  C CA  . ASP A 86  ? 0.4745 0.3655 0.5897 0.1091  -0.0180 0.1930  66  ASP A CA  
538  C C   . ASP A 86  ? 0.4020 0.3562 0.5488 0.0900  0.0047  0.1709  66  ASP A C   
539  O O   . ASP A 86  ? 0.3604 0.3311 0.6291 0.0861  0.0111  0.1842  66  ASP A O   
540  C CB  . ASP A 86  ? 0.4991 0.4194 0.6168 0.0948  -0.0063 0.2090  66  ASP A CB  
541  C CG  . ASP A 86  ? 0.5446 0.4745 0.6337 0.1607  -0.0370 0.2217  66  ASP A CG  
542  O OD1 . ASP A 86  ? 0.6215 0.4442 0.6111 0.1515  -0.0224 0.2080  66  ASP A OD1 
543  O OD2 . ASP A 86  ? 0.5860 0.4507 0.6910 0.1714  -0.0532 0.2172  66  ASP A OD2 
544  N N   . PRO A 87  ? 0.3837 0.3172 0.4642 0.0605  0.0000  0.1772  67  PRO A N   
545  C CA  . PRO A 87  ? 0.4093 0.2762 0.4240 0.0543  -0.0003 0.1492  67  PRO A CA  
546  C C   . PRO A 87  ? 0.3875 0.2862 0.3637 0.0605  -0.0061 0.1397  67  PRO A C   
547  O O   . PRO A 87  ? 0.4582 0.1655 0.3740 0.0416  -0.0245 0.1332  67  PRO A O   
548  C CB  . PRO A 87  ? 0.4172 0.2835 0.4460 0.0528  -0.0017 0.1639  67  PRO A CB  
549  C CG  . PRO A 87  ? 0.3834 0.2287 0.4586 0.0385  0.0268  0.1658  67  PRO A CG  
550  C CD  . PRO A 87  ? 0.3921 0.2846 0.4615 0.0534  0.0207  0.1629  67  PRO A CD  
551  N N   . ARG A 88  ? 0.4055 0.2610 0.3873 0.0264  -0.0088 0.1113  68  ARG A N   
552  C CA  . ARG A 88  ? 0.3884 0.3151 0.3343 0.0101  -0.0107 0.0815  68  ARG A CA  
553  C C   . ARG A 88  ? 0.3516 0.2450 0.3619 0.0145  -0.0085 0.0646  68  ARG A C   
554  O O   . ARG A 88  ? 0.3888 0.2241 0.3638 0.0166  -0.0126 0.0814  68  ARG A O   
555  C CB  . ARG A 88  ? 0.4157 0.3468 0.3461 0.0405  -0.0269 0.0925  68  ARG A CB  
556  C CG  . ARG A 88  ? 0.4257 0.3805 0.3871 0.0536  -0.0101 0.0553  68  ARG A CG  
557  C CD  . ARG A 88  ? 0.5090 0.3396 0.3965 0.0845  -0.0007 0.0823  68  ARG A CD  
558  N NE  . ARG A 88  ? 0.5619 0.3466 0.4143 0.0926  0.0223  0.0887  68  ARG A NE  
559  C CZ  . ARG A 88  ? 0.5649 0.3792 0.4504 0.0644  0.0431  0.0569  68  ARG A CZ  
560  N NH1 . ARG A 88  ? 0.4673 0.4030 0.4309 0.0633  0.0130  0.1105  68  ARG A NH1 
561  N NH2 . ARG A 88  ? 0.5934 0.4462 0.4945 0.1039  0.0496  0.0708  68  ARG A NH2 
562  N N   . TRP A 89  ? 0.3519 0.1829 0.2913 -0.0064 0.0020  0.1045  69  TRP A N   
563  C CA  . TRP A 89  ? 0.3511 0.2356 0.2792 0.0062  -0.0043 0.1100  69  TRP A CA  
564  C C   . TRP A 89  ? 0.3066 0.2248 0.3076 0.0159  -0.0210 0.0711  69  TRP A C   
565  O O   . TRP A 89  ? 0.3209 0.2202 0.3295 0.0103  -0.0313 0.0780  69  TRP A O   
566  C CB  . TRP A 89  ? 0.3362 0.2349 0.2927 0.0192  -0.0066 0.0895  69  TRP A CB  
567  C CG  . TRP A 89  ? 0.3503 0.2239 0.2874 0.0071  0.0022  0.0939  69  TRP A CG  
568  C CD1 . TRP A 89  ? 0.3786 0.1721 0.2877 -0.0043 0.0053  0.1050  69  TRP A CD1 
569  C CD2 . TRP A 89  ? 0.3347 0.2266 0.2964 -0.0047 0.0075  0.0640  69  TRP A CD2 
570  N NE1 . TRP A 89  ? 0.3763 0.2296 0.2815 -0.0055 -0.0161 0.0719  69  TRP A NE1 
571  C CE2 . TRP A 89  ? 0.3707 0.1345 0.2993 -0.0266 -0.0118 0.0732  69  TRP A CE2 
572  C CE3 . TRP A 89  ? 0.3340 0.2092 0.3041 0.0032  -0.0233 0.0724  69  TRP A CE3 
573  C CZ2 . TRP A 89  ? 0.3687 0.1869 0.3115 0.0053  -0.0130 0.0721  69  TRP A CZ2 
574  C CZ3 . TRP A 89  ? 0.3365 0.2009 0.2964 0.0079  -0.0193 0.0541  69  TRP A CZ3 
575  C CH2 . TRP A 89  ? 0.3365 0.2028 0.3023 0.0004  -0.0155 0.0437  69  TRP A CH2 
576  N N   . VAL A 90  ? 0.2912 0.2222 0.3019 0.0097  -0.0331 0.0604  70  VAL A N   
577  C CA  . VAL A 90  ? 0.3359 0.2463 0.3199 0.0246  -0.0216 0.0984  70  VAL A CA  
578  C C   . VAL A 90  ? 0.3347 0.1919 0.3348 0.0142  -0.0252 0.0927  70  VAL A C   
579  O O   . VAL A 90  ? 0.3414 0.2108 0.3018 -0.0245 -0.0036 0.0930  70  VAL A O   
580  C CB  . VAL A 90  ? 0.3506 0.2788 0.3379 0.0017  0.0061  0.0901  70  VAL A CB  
581  C CG1 . VAL A 90  ? 0.3763 0.2545 0.3629 0.0140  0.0096  0.0792  70  VAL A CG1 
582  C CG2 . VAL A 90  ? 0.3745 0.2713 0.3728 -0.0086 -0.0122 0.0893  70  VAL A CG2 
583  N N   . PRO A 91  ? 0.3553 0.2607 0.3575 -0.0052 -0.0203 0.0978  71  PRO A N   
584  C CA  . PRO A 91  ? 0.3445 0.2322 0.3209 -0.0017 -0.0336 0.0921  71  PRO A CA  
585  C C   . PRO A 91  ? 0.3531 0.2049 0.3062 0.0084  0.0077  0.0680  71  PRO A C   
586  O O   . PRO A 91  ? 0.3439 0.2534 0.3573 0.0424  0.0372  0.0854  71  PRO A O   
587  C CB  . PRO A 91  ? 0.3468 0.2404 0.3881 -0.0097 -0.0500 0.1083  71  PRO A CB  
588  C CG  . PRO A 91  ? 0.4015 0.2777 0.4091 -0.0539 -0.0464 0.1207  71  PRO A CG  
589  C CD  . PRO A 91  ? 0.3978 0.2801 0.4176 -0.0013 -0.0354 0.1160  71  PRO A CD  
590  N N   . CYS A 92  ? 0.3489 0.1680 0.3154 0.0142  -0.0117 0.0286  72  CYS A N   
591  C CA  . CYS A 92  ? 0.3240 0.1152 0.2961 0.0343  -0.0063 0.0454  72  CYS A CA  
592  C C   . CYS A 92  ? 0.3593 0.1809 0.3028 0.0224  0.0017  0.0681  72  CYS A C   
593  O O   . CYS A 92  ? 0.3847 0.1992 0.3253 0.0284  0.0312  0.0406  72  CYS A O   
594  C CB  . CYS A 92  ? 0.3657 0.0905 0.3378 0.0191  0.0061  0.0115  72  CYS A CB  
595  S SG  . CYS A 92  ? 0.3936 0.2183 0.3308 0.0055  0.0041  0.0424  72  CYS A SG  
596  N N   . GLU A 93  ? 0.3569 0.2215 0.3254 0.0246  0.0108  0.1074  73  GLU A N   
597  C CA  . GLU A 93  ? 0.3585 0.2307 0.3542 -0.0142 -0.0011 0.1130  73  GLU A CA  
598  C C   . GLU A 93  ? 0.3857 0.2508 0.3363 -0.0120 -0.0026 0.1030  73  GLU A C   
599  O O   . GLU A 93  ? 0.4762 0.2983 0.3443 -0.0383 -0.0163 0.1404  73  GLU A O   
600  C CB  . GLU A 93  ? 0.3750 0.2924 0.4296 -0.0170 0.0355  0.1153  73  GLU A CB  
601  C CG  . GLU A 93  ? 0.3529 0.3849 0.4878 -0.0355 0.0366  0.1502  73  GLU A CG  
602  C CD  . GLU A 93  ? 0.4496 0.4817 0.6099 -0.0083 0.0097  0.1253  73  GLU A CD  
603  O OE1 . GLU A 93  ? 0.5119 0.5626 0.7299 -0.0326 -0.0473 0.1113  73  GLU A OE1 
604  O OE2 . GLU A 93  ? 0.5468 0.4819 0.7611 0.0119  0.0550  0.0187  73  GLU A OE2 
605  N N   . ARG A 94  ? 0.3499 0.2567 0.2855 0.0008  0.0232  0.0712  74  ARG A N   
606  C CA  . ARG A 94  ? 0.3388 0.2396 0.2977 0.0071  0.0283  0.0464  74  ARG A CA  
607  C C   . ARG A 94  ? 0.3343 0.1949 0.2722 0.0140  0.0401  0.0351  74  ARG A C   
608  O O   . ARG A 94  ? 0.3656 0.1243 0.2695 0.0447  0.0416  0.0276  74  ARG A O   
609  C CB  . ARG A 94  ? 0.3979 0.2484 0.3037 -0.0108 0.0270  0.0308  74  ARG A CB  
610  C CG  . ARG A 94  ? 0.4123 0.2851 0.3261 0.0198  0.0335  0.0149  74  ARG A CG  
611  C CD  . ARG A 94  ? 0.4672 0.2863 0.3998 0.0312  0.0498  0.0014  74  ARG A CD  
612  N NE  . ARG A 94  ? 0.5526 0.4141 0.4235 0.0539  0.0420  -0.0055 74  ARG A NE  
613  C CZ  . ARG A 94  ? 0.6529 0.5344 0.4529 0.0803  0.0291  -0.0434 74  ARG A CZ  
614  N NH1 . ARG A 94  ? 0.7167 0.5382 0.4149 0.0120  -0.0294 -0.0592 74  ARG A NH1 
615  N NH2 . ARG A 94  ? 0.7136 0.5848 0.5525 0.1029  0.0234  -0.0547 74  ARG A NH2 
616  N N   . PRO A 95  ? 0.3199 0.2555 0.2757 0.0190  0.0445  0.0407  75  PRO A N   
617  C CA  . PRO A 95  ? 0.3176 0.2337 0.2688 0.0248  0.0265  0.0406  75  PRO A CA  
618  C C   . PRO A 95  ? 0.2936 0.2175 0.2737 0.0210  0.0299  0.0236  75  PRO A C   
619  O O   . PRO A 95  ? 0.3145 0.1961 0.2882 0.0044  -0.0027 0.0317  75  PRO A O   
620  C CB  . PRO A 95  ? 0.3419 0.2597 0.2884 0.0052  0.0258  0.0640  75  PRO A CB  
621  C CG  . PRO A 95  ? 0.3524 0.2959 0.2946 0.0036  0.0256  0.0578  75  PRO A CG  
622  C CD  . PRO A 95  ? 0.3411 0.2436 0.2933 0.0096  0.0384  0.0412  75  PRO A CD  
623  N N   . ILE A 96  ? 0.2984 0.2122 0.2618 0.0229  0.0116  0.0358  76  ILE A N   
624  C CA  . ILE A 96  ? 0.2917 0.1766 0.2478 0.0372  0.0015  0.0447  76  ILE A CA  
625  C C   . ILE A 96  ? 0.3079 0.1831 0.2288 0.0352  -0.0081 0.0523  76  ILE A C   
626  O O   . ILE A 96  ? 0.3523 0.1981 0.2310 0.0510  0.0118  0.0844  76  ILE A O   
627  C CB  . ILE A 96  ? 0.3010 0.1760 0.2441 0.0429  0.0086  0.0373  76  ILE A CB  
628  C CG1 . ILE A 96  ? 0.3097 0.1747 0.2421 0.0350  0.0152  0.0363  76  ILE A CG1 
629  C CG2 . ILE A 96  ? 0.2966 0.1813 0.2501 0.0719  0.0046  0.0204  76  ILE A CG2 
630  C CD1 . ILE A 96  ? 0.3176 0.1741 0.2948 0.0161  0.0235  0.0239  76  ILE A CD1 
631  N N   . PRO A 97  ? 0.2991 0.1709 0.2401 0.0367  -0.0036 0.0474  77  PRO A N   
632  C CA  . PRO A 97  ? 0.3195 0.1702 0.2484 0.0019  0.0113  0.0427  77  PRO A CA  
633  C C   . PRO A 97  ? 0.3102 0.1601 0.2554 -0.0227 0.0005  0.0252  77  PRO A C   
634  O O   . PRO A 97  ? 0.3212 0.1768 0.2709 0.0063  -0.0036 0.0263  77  PRO A O   
635  C CB  . PRO A 97  ? 0.3757 0.1919 0.2882 -0.0023 -0.0007 0.0188  77  PRO A CB  
636  C CG  . PRO A 97  ? 0.4121 0.2292 0.2953 -0.0065 -0.0063 0.0415  77  PRO A CG  
637  C CD  . PRO A 97  ? 0.3640 0.1742 0.2161 0.0212  0.0176  0.0562  77  PRO A CD  
638  N N   . LEU A 98  ? 0.3390 0.1938 0.2320 -0.0141 -0.0006 0.0229  78  LEU A N   
639  C CA  . LEU A 98  ? 0.3341 0.1673 0.2456 -0.0120 0.0020  0.0366  78  LEU A CA  
640  C C   . LEU A 98  ? 0.3417 0.1912 0.2353 0.0106  0.0209  0.0243  78  LEU A C   
641  O O   . LEU A 98  ? 0.3792 0.3149 0.2360 -0.0255 0.0232  0.0344  78  LEU A O   
642  C CB  . LEU A 98  ? 0.3437 0.1617 0.2843 -0.0078 0.0185  0.0316  78  LEU A CB  
643  C CG  . LEU A 98  ? 0.3945 0.1809 0.3235 0.0103  0.0076  0.0367  78  LEU A CG  
644  C CD1 . LEU A 98  ? 0.3851 0.1893 0.3578 0.0573  0.0115  0.0113  78  LEU A CD1 
645  C CD2 . LEU A 98  ? 0.4063 0.1605 0.3282 0.0340  -0.0065 0.0238  78  LEU A CD2 
646  N N   . ARG A 99  ? 0.3252 0.1756 0.2099 0.0142  0.0026  0.0543  79  ARG A N   
647  C CA  . ARG A 99  ? 0.3372 0.2113 0.2163 0.0065  0.0087  0.0598  79  ARG A CA  
648  C C   . ARG A 99  ? 0.3276 0.2591 0.2479 0.0345  0.0201  0.0311  79  ARG A C   
649  O O   . ARG A 99  ? 0.3318 0.2252 0.3024 0.0453  0.0075  0.0541  79  ARG A O   
650  C CB  . ARG A 99  ? 0.3303 0.2084 0.2442 0.0058  0.0180  0.0426  79  ARG A CB  
651  C CG  . ARG A 99  ? 0.3570 0.2315 0.2311 0.0094  0.0010  0.0382  79  ARG A CG  
652  C CD  . ARG A 99  ? 0.3736 0.2289 0.2869 0.0055  0.0005  0.0318  79  ARG A CD  
653  N NE  . ARG A 99  ? 0.3639 0.2470 0.2675 0.0111  -0.0115 0.0156  79  ARG A NE  
654  C CZ  . ARG A 99  ? 0.3490 0.1995 0.2794 0.0353  0.0008  0.0145  79  ARG A CZ  
655  N NH1 . ARG A 99  ? 0.3672 0.2371 0.2860 0.0404  0.0066  0.0350  79  ARG A NH1 
656  N NH2 . ARG A 99  ? 0.3775 0.2202 0.3075 0.0087  0.0072  0.0233  79  ARG A NH2 
657  N N   . GLU A 100 ? 0.3598 0.2836 0.2525 0.0555  0.0353  0.0313  80  GLU A N   
658  C CA  . GLU A 100 ? 0.3813 0.3108 0.2658 0.0401  0.0295  0.0271  80  GLU A CA  
659  C C   . GLU A 100 ? 0.3893 0.3738 0.2519 0.0711  -0.0053 -0.0132 80  GLU A C   
660  O O   . GLU A 100 ? 0.3951 0.4341 0.3309 0.0822  -0.0291 -0.0927 80  GLU A O   
661  C CB  . GLU A 100 ? 0.4622 0.3540 0.2795 0.0278  0.0702  0.0260  80  GLU A CB  
662  C CG  . GLU A 100 ? 0.5312 0.4127 0.3084 -0.0250 0.0704  0.0226  80  GLU A CG  
663  C CD  . GLU A 100 ? 0.6202 0.4307 0.4102 -0.0761 0.0961  0.0555  80  GLU A CD  
664  O OE1 . GLU A 100 ? 0.6652 0.4890 0.4950 -0.1159 0.1852  0.0052  80  GLU A OE1 
665  O OE2 . GLU A 100 ? 0.7237 0.5254 0.4341 -0.0923 0.0183  0.0410  80  GLU A OE2 
666  N N   . VAL A 101 ? 0.4001 0.3394 0.2403 0.0555  0.0113  -0.0067 81  VAL A N   
667  C CA  . VAL A 101 ? 0.3780 0.3143 0.2721 0.0718  0.0084  0.0106  81  VAL A CA  
668  C C   . VAL A 101 ? 0.3910 0.3323 0.2435 0.0517  0.0229  0.0384  81  VAL A C   
669  O O   . VAL A 101 ? 0.3713 0.3286 0.2635 0.0630  -0.0225 0.0496  81  VAL A O   
670  C CB  . VAL A 101 ? 0.3976 0.2841 0.2938 0.0932  0.0109  0.0061  81  VAL A CB  
671  C CG1 . VAL A 101 ? 0.4325 0.2353 0.3158 0.0855  -0.0159 0.0081  81  VAL A CG1 
672  C CG2 . VAL A 101 ? 0.4313 0.2140 0.3203 0.0940  0.0110  -0.0121 81  VAL A CG2 
673  N N   . ARG A 102 ? 0.4392 0.4129 0.2617 0.0619  -0.0221 0.0628  82  ARG A N   
674  C CA  . ARG A 102 ? 0.4634 0.4503 0.3017 0.0479  -0.0317 0.0709  82  ARG A CA  
675  C C   . ARG A 102 ? 0.4985 0.4246 0.3226 0.0589  -0.0654 0.0379  82  ARG A C   
676  O O   . ARG A 102 ? 0.5588 0.4540 0.4575 0.0338  -0.1203 -0.0358 82  ARG A O   
677  C CB  . ARG A 102 ? 0.5285 0.4887 0.2690 0.0341  -0.0118 0.0777  82  ARG A CB  
678  C CG  . ARG A 102 ? 0.4964 0.5443 0.2429 0.0196  0.0232  0.0609  82  ARG A CG  
679  C CD  . ARG A 102 ? 0.5115 0.6050 0.2805 0.0189  0.0298  0.0396  82  ARG A CD  
680  N NE  . ARG A 102 ? 0.5164 0.6803 0.2764 0.0099  0.0765  0.0155  82  ARG A NE  
681  C CZ  . ARG A 102 ? 0.5136 0.7191 0.3062 0.0227  0.0542  0.0131  82  ARG A CZ  
682  N NH1 . ARG A 102 ? 0.5353 0.7675 0.2897 0.0713  0.0694  0.0108  82  ARG A NH1 
683  N NH2 . ARG A 102 ? 0.5498 0.7608 0.3515 0.0432  0.0269  0.0029  82  ARG A NH2 
684  N N   . GLY A 103 ? 0.4962 0.3108 0.2795 0.0103  -0.0444 0.0192  83  GLY A N   
685  C CA  . GLY A 103 ? 0.4702 0.3285 0.3063 0.0108  -0.0349 0.0426  83  GLY A CA  
686  C C   . GLY A 103 ? 0.4237 0.3115 0.3312 0.0067  -0.0428 0.0420  83  GLY A C   
687  O O   . GLY A 103 ? 0.4156 0.4024 0.3753 0.0238  -0.0450 0.0915  83  GLY A O   
688  N N   . GLY A 104 ? 0.4259 0.2553 0.3486 0.0273  -0.0224 0.0330  84  GLY A N   
689  C CA  . GLY A 104 ? 0.4404 0.2111 0.3217 0.0196  -0.0327 0.0128  84  GLY A CA  
690  C C   . GLY A 104 ? 0.3973 0.2237 0.3075 -0.0139 -0.0301 0.0111  84  GLY A C   
691  O O   . GLY A 104 ? 0.3986 0.1921 0.3452 0.0141  -0.0281 -0.0025 84  GLY A O   
692  N N   . GLY A 105 ? 0.4221 0.1909 0.3444 -0.0088 -0.0368 0.0306  85  GLY A N   
693  C CA  . GLY A 105 ? 0.4157 0.1323 0.3725 -0.0140 -0.0236 0.0443  85  GLY A CA  
694  C C   . GLY A 105 ? 0.3898 0.1256 0.3866 -0.0141 -0.0495 0.0446  85  GLY A C   
695  O O   . GLY A 105 ? 0.3990 0.1494 0.3706 0.0122  -0.0520 0.0273  85  GLY A O   
696  N N   A GLU A 106 ? 0.4008 0.1795 0.4013 -0.0044 -0.0587 0.0285  86  GLU A N   
697  N N   B GLU A 106 ? 0.3961 0.1647 0.3833 -0.0050 -0.0472 0.0304  86  GLU A N   
698  C CA  A GLU A 106 ? 0.4043 0.2022 0.3801 -0.0050 -0.0590 0.0287  86  GLU A CA  
699  C CA  B GLU A 106 ? 0.3879 0.1765 0.3544 -0.0039 -0.0342 0.0352  86  GLU A CA  
700  C C   A GLU A 106 ? 0.3686 0.2356 0.3465 0.0097  -0.0568 0.0157  86  GLU A C   
701  C C   B GLU A 106 ? 0.3628 0.2261 0.3308 0.0116  -0.0423 0.0230  86  GLU A C   
702  O O   A GLU A 106 ? 0.3962 0.2710 0.3772 0.0313  -0.0645 -0.0140 86  GLU A O   
703  O O   B GLU A 106 ? 0.3877 0.2634 0.3570 0.0326  -0.0456 -0.0022 86  GLU A O   
704  C CB  A GLU A 106 ? 0.4179 0.2109 0.4104 0.0035  -0.0874 0.0448  86  GLU A CB  
705  C CB  B GLU A 106 ? 0.3968 0.1662 0.3627 0.0053  -0.0470 0.0523  86  GLU A CB  
706  C CG  A GLU A 106 ? 0.4444 0.2194 0.4236 0.0075  -0.0915 0.0473  86  GLU A CG  
707  C CG  B GLU A 106 ? 0.4027 0.1530 0.3599 0.0033  -0.0230 0.0543  86  GLU A CG  
708  C CD  A GLU A 106 ? 0.4364 0.2417 0.4106 -0.0227 -0.0883 0.0451  86  GLU A CD  
709  C CD  B GLU A 106 ? 0.4434 0.1556 0.3668 -0.0215 -0.0178 0.0705  86  GLU A CD  
710  O OE1 A GLU A 106 ? 0.4841 0.3557 0.4641 -0.0048 -0.1173 -0.0129 86  GLU A OE1 
711  O OE1 B GLU A 106 ? 0.4573 0.1524 0.3742 -0.0030 -0.0323 0.1072  86  GLU A OE1 
712  O OE2 A GLU A 106 ? 0.4745 0.0702 0.3489 -0.0813 -0.1147 0.0499  86  GLU A OE2 
713  O OE2 B GLU A 106 ? 0.4850 0.1598 0.3684 -0.0294 -0.0165 0.0720  86  GLU A OE2 
714  N N   . GLU A 107 ? 0.3594 0.2304 0.3230 0.0002  -0.0431 0.0316  87  GLU A N   
715  C CA  . GLU A 107 ? 0.3522 0.2738 0.3331 -0.0203 -0.0356 0.0602  87  GLU A CA  
716  C C   . GLU A 107 ? 0.3502 0.2177 0.2734 -0.0133 -0.0439 0.0305  87  GLU A C   
717  O O   . GLU A 107 ? 0.3472 0.1743 0.3247 -0.0110 -0.0420 0.0385  87  GLU A O   
718  C CB  . GLU A 107 ? 0.3623 0.3067 0.4051 -0.0216 -0.0368 0.0808  87  GLU A CB  
719  C CG  . GLU A 107 ? 0.4319 0.3878 0.4776 -0.0160 0.0106  0.0852  87  GLU A CG  
720  C CD  . GLU A 107 ? 0.5109 0.4200 0.5268 -0.0602 0.0222  0.0537  87  GLU A CD  
721  O OE1 . GLU A 107 ? 0.6173 0.4555 0.6542 -0.0809 -0.0024 0.0099  87  GLU A OE1 
722  O OE2 . GLU A 107 ? 0.5733 0.5127 0.5546 -0.0687 0.0630  0.0615  87  GLU A OE2 
723  N N   . GLN A 108 ? 0.3490 0.1942 0.2756 -0.0110 -0.0404 0.0347  88  GLN A N   
724  C CA  . GLN A 108 ? 0.3462 0.1567 0.2699 -0.0104 -0.0108 0.0225  88  GLN A CA  
725  C C   . GLN A 108 ? 0.3285 0.1754 0.2788 -0.0031 -0.0119 0.0160  88  GLN A C   
726  O O   . GLN A 108 ? 0.3786 0.1515 0.2993 0.0074  -0.0177 0.0021  88  GLN A O   
727  C CB  . GLN A 108 ? 0.3726 0.1836 0.2711 -0.0018 -0.0224 0.0494  88  GLN A CB  
728  C CG  . GLN A 108 ? 0.3980 0.1878 0.3041 0.0000  -0.0300 0.0427  88  GLN A CG  
729  C CD  . GLN A 108 ? 0.4065 0.2666 0.3327 0.0052  -0.0388 -0.0349 88  GLN A CD  
730  O OE1 . GLN A 108 ? 0.4331 0.3348 0.3702 0.0423  -0.0458 -0.0732 88  GLN A OE1 
731  N NE2 . GLN A 108 ? 0.4329 0.2840 0.3292 0.0302  -0.0280 -0.0278 88  GLN A NE2 
732  N N   . TRP A 109 ? 0.3560 0.1744 0.2736 0.0138  -0.0198 0.0088  89  TRP A N   
733  C CA  . TRP A 109 ? 0.3463 0.1259 0.2694 -0.0020 -0.0039 0.0132  89  TRP A CA  
734  C C   . TRP A 109 ? 0.3344 0.1429 0.2643 0.0000  -0.0129 0.0169  89  TRP A C   
735  O O   . TRP A 109 ? 0.3404 0.1168 0.2981 -0.0177 -0.0081 0.0251  89  TRP A O   
736  C CB  . TRP A 109 ? 0.3748 0.1552 0.2720 0.0070  -0.0041 0.0114  89  TRP A CB  
737  C CG  . TRP A 109 ? 0.3629 0.1416 0.2840 -0.0071 -0.0097 0.0144  89  TRP A CG  
738  C CD1 . TRP A 109 ? 0.3550 0.1589 0.2994 0.0039  0.0094  0.0009  89  TRP A CD1 
739  C CD2 . TRP A 109 ? 0.3723 0.0859 0.3105 -0.0248 0.0129  -0.0065 89  TRP A CD2 
740  N NE1 . TRP A 109 ? 0.3814 0.1609 0.3246 0.0170  0.0140  -0.0021 89  TRP A NE1 
741  C CE2 . TRP A 109 ? 0.3997 0.0884 0.3318 -0.0193 0.0112  -0.0035 89  TRP A CE2 
742  C CE3 . TRP A 109 ? 0.3786 0.1271 0.3144 -0.0314 0.0106  0.0171  89  TRP A CE3 
743  C CZ2 . TRP A 109 ? 0.4059 0.1387 0.3503 0.0059  0.0223  -0.0040 89  TRP A CZ2 
744  C CZ3 . TRP A 109 ? 0.4197 0.0940 0.3406 -0.0425 0.0184  0.0123  89  TRP A CZ3 
745  C CH2 . TRP A 109 ? 0.4424 0.0921 0.3445 -0.0280 0.0325  0.0061  89  TRP A CH2 
746  N N   . LEU A 110 ? 0.3369 0.1495 0.2820 0.0041  -0.0236 0.0479  90  LEU A N   
747  C CA  . LEU A 110 ? 0.3513 0.1385 0.2822 0.0084  -0.0113 0.0372  90  LEU A CA  
748  C C   . LEU A 110 ? 0.3411 0.1838 0.2797 0.0022  -0.0195 0.0056  90  LEU A C   
749  O O   . LEU A 110 ? 0.3977 0.1222 0.2900 -0.0080 -0.0048 0.0354  90  LEU A O   
750  C CB  . LEU A 110 ? 0.3594 0.1476 0.3017 0.0236  -0.0129 0.0336  90  LEU A CB  
751  C CG  . LEU A 110 ? 0.3656 0.1403 0.3165 -0.0020 -0.0082 -0.0001 90  LEU A CG  
752  C CD1 . LEU A 110 ? 0.4051 0.2299 0.3506 0.0060  0.0156  0.0262  90  LEU A CD1 
753  C CD2 . LEU A 110 ? 0.3893 0.1453 0.3309 -0.0206 -0.0051 -0.0453 90  LEU A CD2 
754  N N   . ARG A 111 ? 0.3484 0.1856 0.2777 -0.0019 -0.0058 0.0071  91  ARG A N   
755  C CA  . ARG A 111 ? 0.3728 0.1696 0.2960 -0.0005 -0.0080 -0.0143 91  ARG A CA  
756  C C   . ARG A 111 ? 0.3654 0.1671 0.2813 -0.0049 -0.0073 -0.0138 91  ARG A C   
757  O O   . ARG A 111 ? 0.3735 0.1618 0.2994 0.0061  -0.0088 -0.0200 91  ARG A O   
758  C CB  . ARG A 111 ? 0.4002 0.2151 0.3243 -0.0001 -0.0154 -0.0087 91  ARG A CB  
759  C CG  . ARG A 111 ? 0.4346 0.2933 0.3867 0.0159  -0.0158 -0.0026 91  ARG A CG  
760  C CD  . ARG A 111 ? 0.4843 0.3911 0.4167 0.0014  -0.0176 0.0073  91  ARG A CD  
761  N NE  . ARG A 111 ? 0.5296 0.4339 0.5164 -0.0031 -0.0155 0.0160  91  ARG A NE  
762  C CZ  . ARG A 111 ? 0.5135 0.4396 0.5856 0.0159  0.0138  0.0016  91  ARG A CZ  
763  N NH1 . ARG A 111 ? 0.5698 0.4318 0.6645 0.0097  0.0267  0.0470  91  ARG A NH1 
764  N NH2 . ARG A 111 ? 0.5567 0.4703 0.5897 -0.0026 0.0072  -0.0328 91  ARG A NH2 
765  N N   . GLU A 112 ? 0.3573 0.1625 0.2673 -0.0047 0.0018  0.0016  92  GLU A N   
766  C CA  . GLU A 112 ? 0.3497 0.1674 0.2599 -0.0093 -0.0010 -0.0121 92  GLU A CA  
767  C C   . GLU A 112 ? 0.3261 0.1720 0.2625 -0.0073 -0.0030 -0.0022 92  GLU A C   
768  O O   . GLU A 112 ? 0.3618 0.1762 0.2953 0.0006  0.0066  0.0444  92  GLU A O   
769  C CB  . GLU A 112 ? 0.3624 0.1764 0.2528 -0.0139 -0.0019 -0.0302 92  GLU A CB  
770  C CG  . GLU A 112 ? 0.3597 0.1741 0.2837 -0.0051 -0.0095 0.0043  92  GLU A CG  
771  C CD  . GLU A 112 ? 0.3498 0.2187 0.2768 -0.0072 -0.0205 0.0007  92  GLU A CD  
772  O OE1 . GLU A 112 ? 0.3463 0.2540 0.3008 0.0217  0.0071  0.0216  92  GLU A OE1 
773  O OE2 . GLU A 112 ? 0.4333 0.3059 0.2829 0.0302  -0.0380 -0.0067 92  GLU A OE2 
774  N N   . ILE A 113 ? 0.3125 0.1239 0.2521 0.0143  0.0029  0.0223  93  ILE A N   
775  C CA  . ILE A 113 ? 0.3614 0.0827 0.2550 0.0028  -0.0150 0.0039  93  ILE A CA  
776  C C   . ILE A 113 ? 0.3355 0.0815 0.2765 0.0152  -0.0063 -0.0091 93  ILE A C   
777  O O   . ILE A 113 ? 0.3311 0.1013 0.2925 0.0213  -0.0182 0.0024  93  ILE A O   
778  C CB  . ILE A 113 ? 0.3321 0.1419 0.2346 -0.0027 -0.0158 0.0052  93  ILE A CB  
779  C CG1 . ILE A 113 ? 0.3383 0.1676 0.2756 -0.0280 -0.0099 0.0142  93  ILE A CG1 
780  C CG2 . ILE A 113 ? 0.3774 0.1681 0.2515 -0.0129 0.0009  -0.0023 93  ILE A CG2 
781  C CD1 . ILE A 113 ? 0.3702 0.1464 0.3026 -0.0110 -0.0168 0.0281  93  ILE A CD1 
782  N N   . ASN A 114 ? 0.3725 0.0469 0.2987 0.0267  -0.0208 -0.0141 94  ASN A N   
783  C CA  . ASN A 114 ? 0.3818 0.0493 0.2822 0.0170  -0.0030 0.0169  94  ASN A CA  
784  C C   . ASN A 114 ? 0.3779 0.1313 0.2945 0.0266  -0.0123 0.0143  94  ASN A C   
785  O O   . ASN A 114 ? 0.4325 0.0799 0.3303 0.0116  -0.0191 -0.0022 94  ASN A O   
786  C CB  . ASN A 114 ? 0.3927 0.0547 0.2881 -0.0020 0.0150  0.0100  94  ASN A CB  
787  C CG  . ASN A 114 ? 0.3695 0.1419 0.2909 -0.0125 -0.0029 -0.0026 94  ASN A CG  
788  O OD1 . ASN A 114 ? 0.4301 0.1577 0.3024 0.0320  0.0198  0.0242  94  ASN A OD1 
789  N ND2 . ASN A 114 ? 0.4064 0.2087 0.2974 0.0062  -0.0144 0.0213  94  ASN A ND2 
790  N N   . GLU A 115 ? 0.3742 0.0955 0.2899 -0.0022 0.0045  -0.0101 95  GLU A N   
791  C CA  . GLU A 115 ? 0.4256 0.0988 0.3178 0.0490  -0.0119 -0.0168 95  GLU A CA  
792  C C   . GLU A 115 ? 0.4006 0.1766 0.3053 0.0452  -0.0208 -0.0311 95  GLU A C   
793  O O   . GLU A 115 ? 0.4086 0.2187 0.3367 0.0460  -0.0078 -0.0539 95  GLU A O   
794  C CB  . GLU A 115 ? 0.4697 0.1561 0.3196 0.0271  -0.0073 -0.0571 95  GLU A CB  
795  C CG  . GLU A 115 ? 0.5087 0.2493 0.3841 0.0040  -0.0269 -0.0850 95  GLU A CG  
796  C CD  . GLU A 115 ? 0.5677 0.3350 0.5227 -0.0691 0.0304  -0.0710 95  GLU A CD  
797  O OE1 . GLU A 115 ? 0.6404 0.4046 0.6161 -0.0485 0.0339  -0.1225 95  GLU A OE1 
798  O OE2 . GLU A 115 ? 0.5706 0.4173 0.4970 -0.0974 0.0610  -0.0602 95  GLU A OE2 
799  N N   . ARG A 116 ? 0.3891 0.2015 0.2811 0.0286  0.0001  -0.0518 96  ARG A N   
800  C CA  . ARG A 116 ? 0.4232 0.2105 0.3010 0.0204  0.0058  -0.0507 96  ARG A CA  
801  C C   . ARG A 116 ? 0.3381 0.2081 0.3412 0.0004  0.0051  -0.0749 96  ARG A C   
802  O O   . ARG A 116 ? 0.4211 0.2341 0.4075 0.0518  -0.0379 -0.0763 96  ARG A O   
803  C CB  . ARG A 116 ? 0.4433 0.2317 0.3343 0.0155  0.0012  -0.0250 96  ARG A CB  
804  C CG  . ARG A 116 ? 0.5011 0.2670 0.3672 0.0169  -0.0308 -0.0262 96  ARG A CG  
805  C CD  . ARG A 116 ? 0.5498 0.3057 0.4115 0.0471  -0.0078 -0.0485 96  ARG A CD  
806  N NE  . ARG A 116 ? 0.5713 0.2453 0.4998 0.0516  -0.0615 -0.0686 96  ARG A NE  
807  C CZ  . ARG A 116 ? 0.5749 0.2253 0.4871 0.0630  -0.0569 -0.0958 96  ARG A CZ  
808  N NH1 . ARG A 116 ? 0.6880 0.2418 0.5059 0.0086  -0.0628 -0.1235 96  ARG A NH1 
809  N NH2 . ARG A 116 ? 0.5448 0.2543 0.4666 0.0256  -0.0458 -0.0362 96  ARG A NH2 
810  N N   . GLU A 117 ? 0.3387 0.1781 0.3028 0.0395  -0.0015 0.0028  97  GLU A N   
811  C CA  . GLU A 117 ? 0.3244 0.1160 0.2988 0.0167  0.0055  -0.0194 97  GLU A CA  
812  C C   . GLU A 117 ? 0.3382 0.1094 0.2977 0.0245  -0.0088 -0.0150 97  GLU A C   
813  O O   . GLU A 117 ? 0.3740 0.1083 0.3032 -0.0140 -0.0253 0.0541  97  GLU A O   
814  C CB  . GLU A 117 ? 0.3213 0.1320 0.2951 0.0105  -0.0007 -0.0337 97  GLU A CB  
815  C CG  . GLU A 117 ? 0.3816 0.1252 0.2949 0.0019  -0.0129 -0.0210 97  GLU A CG  
816  C CD  . GLU A 117 ? 0.3930 0.0957 0.2939 0.0080  -0.0128 -0.0189 97  GLU A CD  
817  O OE1 . GLU A 117 ? 0.4352 0.1456 0.2922 0.0185  -0.0039 0.0239  97  GLU A OE1 
818  O OE2 . GLU A 117 ? 0.3587 0.1569 0.3000 0.0044  -0.0142 -0.0010 97  GLU A OE2 
819  N N   . LEU A 118 ? 0.3679 0.1175 0.2929 -0.0040 0.0045  0.0214  98  LEU A N   
820  C CA  . LEU A 118 ? 0.3621 0.1291 0.2856 0.0446  0.0010  0.0300  98  LEU A CA  
821  C C   . LEU A 118 ? 0.3521 0.1074 0.3071 0.0179  0.0000  0.0244  98  LEU A C   
822  O O   . LEU A 118 ? 0.3744 0.0830 0.3262 0.0376  -0.0072 0.0331  98  LEU A O   
823  C CB  . LEU A 118 ? 0.3574 0.0963 0.2691 0.0362  -0.0016 0.0339  98  LEU A CB  
824  C CG  . LEU A 118 ? 0.3658 0.0961 0.2801 0.0423  -0.0042 0.0261  98  LEU A CG  
825  C CD1 . LEU A 118 ? 0.3779 0.0923 0.2829 0.0052  0.0003  0.0335  98  LEU A CD1 
826  C CD2 . LEU A 118 ? 0.3933 0.0720 0.2901 0.0585  0.0140  0.0432  98  LEU A CD2 
827  N N   . PRO A 119 ? 0.3607 0.0913 0.3307 0.0196  -0.0044 0.0007  99  PRO A N   
828  C CA  . PRO A 119 ? 0.3879 0.1253 0.3384 0.0510  -0.0172 0.0222  99  PRO A CA  
829  C C   . PRO A 119 ? 0.3629 0.1227 0.3451 0.0628  -0.0206 0.0205  99  PRO A C   
830  O O   . PRO A 119 ? 0.4322 0.1312 0.3995 0.0898  -0.0635 0.0436  99  PRO A O   
831  C CB  . PRO A 119 ? 0.4019 0.1662 0.3644 0.0198  -0.0062 -0.0061 99  PRO A CB  
832  C CG  . PRO A 119 ? 0.4212 0.1713 0.3501 0.0187  0.0013  -0.0018 99  PRO A CG  
833  C CD  . PRO A 119 ? 0.4042 0.1279 0.3403 0.0041  -0.0065 -0.0041 99  PRO A CD  
834  N N   . GLU A 120 ? 0.3805 0.1578 0.3402 0.0138  0.0159  0.0019  100 GLU A N   
835  C CA  . GLU A 120 ? 0.3867 0.0988 0.3644 0.0331  -0.0036 -0.0182 100 GLU A CA  
836  C C   . GLU A 120 ? 0.3608 0.1224 0.3056 0.0431  0.0101  -0.0323 100 GLU A C   
837  O O   . GLU A 120 ? 0.3699 0.1131 0.2985 0.0233  0.0162  -0.0349 100 GLU A O   
838  C CB  . GLU A 120 ? 0.4159 0.1624 0.3746 -0.0031 -0.0059 -0.0136 100 GLU A CB  
839  C CG  . GLU A 120 ? 0.4741 0.2664 0.4331 0.0160  -0.0181 -0.0183 100 GLU A CG  
840  C CD  . GLU A 120 ? 0.5888 0.3832 0.4575 -0.0461 -0.0161 0.0076  100 GLU A CD  
841  O OE1 . GLU A 120 ? 0.6395 0.5625 0.5419 -0.1397 0.0299  0.0085  100 GLU A OE1 
842  O OE2 . GLU A 120 ? 0.6127 0.4774 0.5210 -0.0605 -0.0552 -0.0211 100 GLU A OE2 
843  N N   . ARG A 121 ? 0.4045 0.1324 0.3234 0.0288  0.0071  -0.0146 101 ARG A N   
844  C CA  . ARG A 121 ? 0.3822 0.1519 0.2964 0.0334  0.0108  0.0112  101 ARG A CA  
845  C C   . ARG A 121 ? 0.3609 0.1445 0.2751 0.0288  0.0077  0.0110  101 ARG A C   
846  O O   . ARG A 121 ? 0.3974 0.1344 0.3060 0.0069  0.0430  -0.0010 101 ARG A O   
847  C CB  . ARG A 121 ? 0.4031 0.2286 0.3376 0.0974  0.0152  0.0210  101 ARG A CB  
848  C CG  . ARG A 121 ? 0.4865 0.2404 0.3983 0.0888  0.0198  0.0735  101 ARG A CG  
849  C CD  . ARG A 121 ? 0.4928 0.2588 0.4070 0.1404  0.0078  0.0865  101 ARG A CD  
850  N NE  . ARG A 121 ? 0.5396 0.2650 0.4387 0.0929  0.0146  0.1034  101 ARG A NE  
851  C CZ  . ARG A 121 ? 0.5434 0.2532 0.4496 0.0861  0.0605  0.1049  101 ARG A CZ  
852  N NH1 . ARG A 121 ? 0.5416 0.2448 0.4404 0.0727  0.0684  0.0671  101 ARG A NH1 
853  N NH2 . ARG A 121 ? 0.5687 0.3009 0.4787 0.0698  0.0594  0.1422  101 ARG A NH2 
854  N N   . ILE A 122 ? 0.3613 0.1796 0.2758 0.0386  0.0178  -0.0036 102 ILE A N   
855  C CA  . ILE A 122 ? 0.3410 0.1495 0.2945 0.0319  0.0225  -0.0074 102 ILE A CA  
856  C C   . ILE A 122 ? 0.3480 0.1518 0.3143 0.0180  0.0106  -0.0131 102 ILE A C   
857  O O   . ILE A 122 ? 0.3634 0.1984 0.3050 0.0453  0.0134  0.0169  102 ILE A O   
858  C CB  . ILE A 122 ? 0.3543 0.1344 0.3152 0.0272  0.0055  -0.0082 102 ILE A CB  
859  C CG1 . ILE A 122 ? 0.3611 0.1238 0.3084 0.0221  0.0121  -0.0053 102 ILE A CG1 
860  C CG2 . ILE A 122 ? 0.3440 0.1866 0.3462 0.0318  -0.0098 0.0065  102 ILE A CG2 
861  C CD1 . ILE A 122 ? 0.3757 0.0805 0.3220 0.0439  -0.0137 0.0106  102 ILE A CD1 
862  N N   . ASP A 123 ? 0.3776 0.1312 0.3103 0.0348  0.0248  -0.0105 103 ASP A N   
863  C CA  . ASP A 123 ? 0.3774 0.1713 0.3475 0.0488  0.0207  0.0094  103 ASP A CA  
864  C C   . ASP A 123 ? 0.3424 0.1760 0.3289 0.0122  0.0262  0.0339  103 ASP A C   
865  O O   . ASP A 123 ? 0.3971 0.1301 0.3777 0.0136  0.0147  0.0248  103 ASP A O   
866  C CB  . ASP A 123 ? 0.4016 0.2199 0.3767 0.0540  0.0350  0.0024  103 ASP A CB  
867  C CG  . ASP A 123 ? 0.4171 0.2910 0.4205 0.0819  0.0427  -0.0250 103 ASP A CG  
868  O OD1 . ASP A 123 ? 0.4778 0.2472 0.4668 0.0938  0.0096  -0.0183 103 ASP A OD1 
869  O OD2 . ASP A 123 ? 0.4685 0.4641 0.5034 0.1360  0.0694  -0.0876 103 ASP A OD2 
870  N N   . PRO A 124 ? 0.3435 0.1624 0.3489 0.0198  0.0119  0.0414  104 PRO A N   
871  C CA  . PRO A 124 ? 0.3784 0.2095 0.3564 0.0209  -0.0067 0.0420  104 PRO A CA  
872  C C   . PRO A 124 ? 0.3748 0.2514 0.3726 0.0181  -0.0102 0.0510  104 PRO A C   
873  O O   . PRO A 124 ? 0.3637 0.2571 0.3831 -0.0173 -0.0403 0.0950  104 PRO A O   
874  C CB  . PRO A 124 ? 0.3753 0.2039 0.3498 0.0141  0.0160  0.0461  104 PRO A CB  
875  C CG  . PRO A 124 ? 0.3977 0.2023 0.3685 0.0131  0.0102  0.0554  104 PRO A CG  
876  C CD  . PRO A 124 ? 0.3685 0.1641 0.3575 0.0103  -0.0007 0.0355  104 PRO A CD  
877  N N   . ASP A 125 ? 0.3658 0.2054 0.3913 0.0272  0.0144  0.0533  105 ASP A N   
878  C CA  . ASP A 125 ? 0.3881 0.2546 0.4426 0.0206  0.0186  0.0696  105 ASP A CA  
879  C C   . ASP A 125 ? 0.3447 0.1913 0.4083 0.0492  0.0318  0.0359  105 ASP A C   
880  O O   . ASP A 125 ? 0.3727 0.2641 0.4345 0.0626  -0.0047 0.0390  105 ASP A O   
881  C CB  . ASP A 125 ? 0.4010 0.2589 0.4722 0.0266  0.0210  0.0393  105 ASP A CB  
882  C CG  . ASP A 125 ? 0.4940 0.2748 0.5420 0.0381  0.0170  0.0539  105 ASP A CG  
883  O OD1 . ASP A 125 ? 0.4662 0.2155 0.6116 0.0765  -0.0036 0.1012  105 ASP A OD1 
884  O OD2 . ASP A 125 ? 0.5360 0.2350 0.6118 0.0412  -0.0100 0.0351  105 ASP A OD2 
885  N N   . SER A 126 ? 0.3856 0.1699 0.3702 0.0264  0.0272  0.0157  106 SER A N   
886  C CA  . SER A 126 ? 0.3738 0.1886 0.3627 0.0556  0.0444  0.0315  106 SER A CA  
887  C C   . SER A 126 ? 0.3498 0.1856 0.3692 0.0175  0.0241  0.0100  106 SER A C   
888  O O   . SER A 126 ? 0.3537 0.1680 0.3776 0.0594  0.0349  0.0617  106 SER A O   
889  C CB  . SER A 126 ? 0.4207 0.2489 0.4182 0.0402  0.0220  -0.0111 106 SER A CB  
890  O OG  . SER A 126 ? 0.4579 0.2897 0.4196 0.0194  0.0008  -0.0252 106 SER A OG  
891  N N   . GLY A 127 ? 0.3634 0.1299 0.3223 0.0484  0.0413  0.0113  107 GLY A N   
892  C CA  . GLY A 127 ? 0.3646 0.1790 0.2925 0.0227  0.0527  0.0163  107 GLY A CA  
893  C C   . GLY A 127 ? 0.3605 0.1644 0.2766 0.0336  0.0489  0.0199  107 GLY A C   
894  O O   . GLY A 127 ? 0.3882 0.1960 0.2877 0.0465  0.0128  0.0220  107 GLY A O   
895  N N   . PRO A 128 ? 0.3633 0.1289 0.2509 0.0254  0.0275  0.0533  108 PRO A N   
896  C CA  . PRO A 128 ? 0.3452 0.1054 0.2507 0.0182  0.0068  0.0685  108 PRO A CA  
897  C C   . PRO A 128 ? 0.3027 0.1252 0.2654 0.0393  -0.0115 0.0496  108 PRO A C   
898  O O   . PRO A 128 ? 0.3419 0.1115 0.2786 -0.0084 0.0120  0.0448  108 PRO A O   
899  C CB  . PRO A 128 ? 0.3281 0.0996 0.2541 0.0125  0.0103  0.0441  108 PRO A CB  
900  C CG  . PRO A 128 ? 0.3485 0.1372 0.2615 0.0065  0.0141  0.0426  108 PRO A CG  
901  C CD  . PRO A 128 ? 0.3811 0.1407 0.2611 0.0172  0.0211  0.0640  108 PRO A CD  
902  N N   . LEU A 129 ? 0.2983 0.1395 0.2590 0.0321  -0.0249 0.0376  109 LEU A N   
903  C CA  . LEU A 129 ? 0.3046 0.1666 0.2729 0.0388  -0.0037 0.0218  109 LEU A CA  
904  C C   . LEU A 129 ? 0.3058 0.1321 0.2664 0.0224  -0.0029 0.0199  109 LEU A C   
905  O O   . LEU A 129 ? 0.3386 0.1237 0.2753 0.0176  0.0228  0.0415  109 LEU A O   
906  C CB  . LEU A 129 ? 0.3118 0.1795 0.2879 0.0471  -0.0129 0.0263  109 LEU A CB  
907  C CG  . LEU A 129 ? 0.3207 0.1669 0.2887 0.0466  0.0125  0.0464  109 LEU A CG  
908  C CD1 . LEU A 129 ? 0.3255 0.1299 0.2903 0.0530  -0.0075 0.0307  109 LEU A CD1 
909  C CD2 . LEU A 129 ? 0.3315 0.2150 0.3012 0.0438  0.0267  0.0413  109 LEU A CD2 
910  N N   . ILE A 130 ? 0.3056 0.1551 0.2501 0.0399  -0.0038 0.0276  110 ILE A N   
911  C CA  . ILE A 130 ? 0.3156 0.1345 0.2407 0.0173  -0.0024 0.0282  110 ILE A CA  
912  C C   . ILE A 130 ? 0.3284 0.1239 0.2667 0.0500  -0.0010 0.0319  110 ILE A C   
913  O O   . ILE A 130 ? 0.3298 0.1282 0.2885 0.0447  -0.0005 0.0337  110 ILE A O   
914  C CB  . ILE A 130 ? 0.3228 0.1357 0.2470 0.0066  -0.0138 0.0362  110 ILE A CB  
915  C CG1 . ILE A 130 ? 0.3151 0.1190 0.2639 0.0018  0.0187  0.0293  110 ILE A CG1 
916  C CG2 . ILE A 130 ? 0.3322 0.1667 0.2686 0.0218  -0.0091 0.0541  110 ILE A CG2 
917  C CD1 . ILE A 130 ? 0.3316 0.1185 0.2747 0.0119  0.0192  0.0383  110 ILE A CD1 
918  N N   . ARG A 131 ? 0.2936 0.1630 0.2391 0.0425  0.0258  0.0443  111 ARG A N   
919  C CA  . ARG A 131 ? 0.3290 0.1831 0.2309 0.0155  -0.0097 0.0202  111 ARG A CA  
920  C C   . ARG A 131 ? 0.2971 0.1747 0.2228 0.0024  0.0133  0.0264  111 ARG A C   
921  O O   . ARG A 131 ? 0.3067 0.1098 0.2272 0.0229  0.0082  0.0470  111 ARG A O   
922  C CB  . ARG A 131 ? 0.4142 0.2587 0.2453 0.0452  -0.0235 -0.0055 111 ARG A CB  
923  C CG  . ARG A 131 ? 0.4061 0.2458 0.2683 0.0456  0.0026  -0.0119 111 ARG A CG  
924  C CD  . ARG A 131 ? 0.4072 0.2137 0.2618 0.0634  0.0065  -0.0072 111 ARG A CD  
925  N NE  . ARG A 131 ? 0.3695 0.1615 0.2821 0.0563  0.0000  0.0074  111 ARG A NE  
926  C CZ  . ARG A 131 ? 0.3699 0.1655 0.3067 0.0319  0.0102  0.0160  111 ARG A CZ  
927  N NH1 . ARG A 131 ? 0.3649 0.1947 0.2918 0.0046  0.0095  -0.0011 111 ARG A NH1 
928  N NH2 . ARG A 131 ? 0.3598 0.1277 0.3419 0.0301  0.0186  -0.0047 111 ARG A NH2 
929  N N   . THR A 132 ? 0.3162 0.1775 0.2217 0.0116  0.0108  0.0213  112 THR A N   
930  C CA  . THR A 132 ? 0.3187 0.1444 0.2462 -0.0020 0.0027  0.0230  112 THR A CA  
931  C C   . THR A 132 ? 0.3066 0.1357 0.2348 0.0166  0.0165  0.0378  112 THR A C   
932  O O   . THR A 132 ? 0.3041 0.2129 0.2188 0.0554  0.0096  0.0224  112 THR A O   
933  C CB  . THR A 132 ? 0.3326 0.1511 0.2555 -0.0118 0.0154  0.0132  112 THR A CB  
934  O OG1 . THR A 132 ? 0.3787 0.1442 0.2454 -0.0089 0.0174  0.0259  112 THR A OG1 
935  C CG2 . THR A 132 ? 0.3242 0.1364 0.2474 -0.0046 0.0143  0.0317  112 THR A CG2 
936  N N   . VAL A 133 ? 0.3150 0.1360 0.2404 0.0418  0.0152  0.0219  113 VAL A N   
937  C CA  . VAL A 133 ? 0.3040 0.1815 0.2480 0.0342  -0.0078 0.0150  113 VAL A CA  
938  C C   . VAL A 133 ? 0.3255 0.1864 0.2288 0.0371  0.0112  0.0261  113 VAL A C   
939  O O   . VAL A 133 ? 0.3279 0.1417 0.2392 0.0407  0.0165  0.0585  113 VAL A O   
940  C CB  . VAL A 133 ? 0.3301 0.1868 0.2441 0.0174  -0.0336 0.0471  113 VAL A CB  
941  C CG1 . VAL A 133 ? 0.3443 0.1869 0.2701 -0.0051 -0.0272 0.0215  113 VAL A CG1 
942  C CG2 . VAL A 133 ? 0.3512 0.1783 0.2484 0.0275  -0.0353 0.0216  113 VAL A CG2 
943  N N   . ALA A 134 ? 0.3155 0.1997 0.2381 0.0368  0.0018  0.0215  114 ALA A N   
944  C CA  . ALA A 134 ? 0.3139 0.1851 0.2524 0.0193  0.0024  0.0185  114 ALA A CA  
945  C C   . ALA A 134 ? 0.3306 0.1800 0.2444 0.0306  0.0018  0.0288  114 ALA A C   
946  O O   . ALA A 134 ? 0.3463 0.2092 0.2439 0.0173  0.0207  0.0357  114 ALA A O   
947  C CB  . ALA A 134 ? 0.3353 0.1822 0.2792 0.0054  0.0004  0.0336  114 ALA A CB  
948  N N   . ILE A 135 ? 0.3350 0.1753 0.2294 0.0330  -0.0091 0.0406  115 ILE A N   
949  C CA  . ILE A 135 ? 0.3318 0.1725 0.2554 0.0332  -0.0023 0.0265  115 ILE A CA  
950  C C   . ILE A 135 ? 0.3457 0.1889 0.2657 0.0405  -0.0025 0.0437  115 ILE A C   
951  O O   . ILE A 135 ? 0.3605 0.1275 0.2857 0.0158  -0.0041 0.0686  115 ILE A O   
952  C CB  . ILE A 135 ? 0.3221 0.1981 0.2914 0.0295  -0.0035 -0.0016 115 ILE A CB  
953  C CG1 . ILE A 135 ? 0.3357 0.2014 0.3075 0.0388  0.0024  0.0044  115 ILE A CG1 
954  C CG2 . ILE A 135 ? 0.3473 0.1975 0.2919 0.0238  -0.0048 -0.0084 115 ILE A CG2 
955  C CD1 . ILE A 135 ? 0.3538 0.2284 0.3157 0.0320  -0.0109 0.0151  115 ILE A CD1 
956  N N   . ALA A 136 ? 0.3407 0.2056 0.2832 0.0409  -0.0153 0.0542  116 ALA A N   
957  C CA  . ALA A 136 ? 0.3368 0.2325 0.3005 0.0435  -0.0139 0.0570  116 ALA A CA  
958  C C   . ALA A 136 ? 0.3106 0.2260 0.2657 0.0347  -0.0188 0.0527  116 ALA A C   
959  O O   . ALA A 136 ? 0.3661 0.2409 0.2944 -0.0157 -0.0178 0.0280  116 ALA A O   
960  C CB  . ALA A 136 ? 0.3663 0.2566 0.3148 0.0409  -0.0070 0.0789  116 ALA A CB  
961  N N   . THR A 137 ? 0.3330 0.2302 0.2650 0.0437  -0.0116 0.0425  117 THR A N   
962  C CA  . THR A 137 ? 0.3326 0.2142 0.2821 0.0363  -0.0287 0.0230  117 THR A CA  
963  C C   . THR A 137 ? 0.3333 0.2160 0.2785 0.0132  -0.0253 0.0434  117 THR A C   
964  O O   . THR A 137 ? 0.3416 0.1921 0.2839 -0.0003 -0.0369 0.0424  117 THR A O   
965  C CB  . THR A 137 ? 0.3458 0.2125 0.2804 0.0291  -0.0066 0.0351  117 THR A CB  
966  O OG1 . THR A 137 ? 0.3444 0.1938 0.2748 0.0438  0.0163  0.0422  117 THR A OG1 
967  C CG2 . THR A 137 ? 0.3588 0.2448 0.2748 0.0176  0.0028  0.0524  117 THR A CG2 
968  N N   . ASP A 138 ? 0.3805 0.1827 0.2516 0.0163  -0.0496 0.0033  118 ASP A N   
969  C CA  . ASP A 138 ? 0.3690 0.2459 0.2906 0.0262  -0.0400 0.0149  118 ASP A CA  
970  C C   . ASP A 138 ? 0.3652 0.2359 0.2687 0.0206  -0.0462 0.0224  118 ASP A C   
971  O O   . ASP A 138 ? 0.4469 0.2395 0.2973 0.0489  -0.0309 0.0405  118 ASP A O   
972  C CB  . ASP A 138 ? 0.4069 0.2327 0.3168 0.0061  -0.0448 -0.0060 118 ASP A CB  
973  C CG  . ASP A 138 ? 0.4278 0.3036 0.3570 0.0000  -0.0179 -0.0350 118 ASP A CG  
974  O OD1 . ASP A 138 ? 0.4475 0.3079 0.3536 0.0234  0.0123  -0.0358 118 ASP A OD1 
975  O OD2 . ASP A 138 ? 0.5527 0.3023 0.5027 0.0050  -0.0185 -0.0643 118 ASP A OD2 
976  N N   . ALA A 139 ? 0.3333 0.2106 0.2686 0.0626  -0.0232 0.0417  119 ALA A N   
977  C CA  . ALA A 139 ? 0.3291 0.1649 0.2875 0.0232  -0.0416 0.0286  119 ALA A CA  
978  C C   . ALA A 139 ? 0.3303 0.1494 0.2673 0.0167  -0.0203 0.0525  119 ALA A C   
979  O O   . ALA A 139 ? 0.3215 0.1441 0.3577 0.0437  -0.0192 0.0419  119 ALA A O   
980  C CB  . ALA A 139 ? 0.3762 0.1359 0.2825 0.0322  -0.0248 0.0119  119 ALA A CB  
981  N N   . GLY A 140 ? 0.3587 0.1203 0.2897 -0.0117 -0.0261 0.0439  120 GLY A N   
982  C CA  . GLY A 140 ? 0.3437 0.1317 0.3265 0.0113  -0.0149 0.0520  120 GLY A CA  
983  C C   . GLY A 140 ? 0.3501 0.1970 0.3147 -0.0037 -0.0230 0.0262  120 GLY A C   
984  O O   . GLY A 140 ? 0.4356 0.2266 0.3152 -0.0324 -0.0266 0.0527  120 GLY A O   
985  N N   . ALA A 141 ? 0.3742 0.1842 0.3236 -0.0147 -0.0538 0.0462  121 ALA A N   
986  C CA  . ALA A 141 ? 0.3676 0.1558 0.3324 0.0052  -0.0347 0.0103  121 ALA A CA  
987  C C   . ALA A 141 ? 0.3433 0.1844 0.3006 0.0219  -0.0289 0.0314  121 ALA A C   
988  O O   . ALA A 141 ? 0.4077 0.1882 0.3471 0.0762  -0.0503 0.0510  121 ALA A O   
989  C CB  . ALA A 141 ? 0.3666 0.1733 0.3421 0.0460  -0.0347 -0.0028 121 ALA A CB  
990  N N   . HIS A 142 ? 0.2999 0.1295 0.2674 0.0104  -0.0015 0.0479  122 HIS A N   
991  C CA  . HIS A 142 ? 0.3287 0.1827 0.2711 0.0298  0.0014  0.0491  122 HIS A CA  
992  C C   . HIS A 142 ? 0.3553 0.1467 0.2706 0.0170  -0.0016 0.0493  122 HIS A C   
993  O O   . HIS A 142 ? 0.4189 0.0978 0.2736 0.0023  -0.0086 0.0617  122 HIS A O   
994  C CB  . HIS A 142 ? 0.3388 0.1906 0.2874 0.0244  -0.0104 0.0717  122 HIS A CB  
995  C CG  . HIS A 142 ? 0.3583 0.1786 0.3250 0.0073  0.0084  0.0866  122 HIS A CG  
996  N ND1 . HIS A 142 ? 0.4201 0.1767 0.3317 -0.0092 0.0106  0.1359  122 HIS A ND1 
997  C CD2 . HIS A 142 ? 0.4055 0.1382 0.3709 -0.0155 -0.0066 0.0831  122 HIS A CD2 
998  C CE1 . HIS A 142 ? 0.4232 0.2244 0.3596 -0.0025 0.0297  0.1113  122 HIS A CE1 
999  N NE2 . HIS A 142 ? 0.4278 0.2313 0.3519 -0.0341 0.0149  0.1084  122 HIS A NE2 
1000 N N   . ASP A 143 ? 0.3484 0.1339 0.2482 0.0058  -0.0310 0.0242  123 ASP A N   
1001 C CA  . ASP A 143 ? 0.3102 0.1797 0.2507 -0.0159 0.0032  0.0373  123 ASP A CA  
1002 C C   . ASP A 143 ? 0.3212 0.1231 0.2382 0.0040  -0.0042 0.0503  123 ASP A C   
1003 O O   . ASP A 143 ? 0.3357 0.1346 0.2414 0.0297  0.0043  0.0535  123 ASP A O   
1004 C CB  . ASP A 143 ? 0.3177 0.1327 0.2855 -0.0006 -0.0154 0.0445  123 ASP A CB  
1005 C CG  . ASP A 143 ? 0.3248 0.1780 0.2680 0.0041  0.0067  0.0400  123 ASP A CG  
1006 O OD1 . ASP A 143 ? 0.3439 0.1895 0.3027 0.0071  0.0164  -0.0128 123 ASP A OD1 
1007 O OD2 . ASP A 143 ? 0.3692 0.1635 0.3266 0.0100  -0.0250 0.0522  123 ASP A OD2 
1008 N N   . LEU A 144 ? 0.3284 0.0972 0.2318 0.0143  0.0028  0.0382  124 LEU A N   
1009 C CA  . LEU A 144 ? 0.3313 0.1175 0.2534 0.0016  0.0066  0.0390  124 LEU A CA  
1010 C C   . LEU A 144 ? 0.3114 0.1104 0.2570 0.0047  0.0237  0.0422  124 LEU A C   
1011 O O   . LEU A 144 ? 0.3452 0.0749 0.2482 0.0271  0.0116  0.0495  124 LEU A O   
1012 C CB  . LEU A 144 ? 0.3284 0.1242 0.2479 0.0065  -0.0007 0.0332  124 LEU A CB  
1013 C CG  . LEU A 144 ? 0.3718 0.1083 0.2922 -0.0082 -0.0061 0.0359  124 LEU A CG  
1014 C CD1 . LEU A 144 ? 0.3862 0.0423 0.3199 -0.0095 -0.0140 0.0533  124 LEU A CD1 
1015 C CD2 . LEU A 144 ? 0.4038 0.0870 0.3157 -0.0224 -0.0063 0.0165  124 LEU A CD2 
1016 N N   . LEU A 145 ? 0.3109 0.1443 0.2274 0.0231  0.0169  0.0384  125 LEU A N   
1017 C CA  . LEU A 145 ? 0.3044 0.0930 0.2342 0.0064  0.0238  0.0126  125 LEU A CA  
1018 C C   . LEU A 145 ? 0.2916 0.0311 0.2255 0.0063  0.0161  0.0060  125 LEU A C   
1019 O O   . LEU A 145 ? 0.3046 0.1223 0.2315 0.0215  0.0234  0.0275  125 LEU A O   
1020 C CB  . LEU A 145 ? 0.3014 0.0846 0.2668 0.0093  0.0180  0.0091  125 LEU A CB  
1021 C CG  . LEU A 145 ? 0.3434 0.0779 0.2844 0.0175  0.0073  0.0124  125 LEU A CG  
1022 C CD1 . LEU A 145 ? 0.3523 0.0878 0.2861 -0.0156 0.0241  0.0036  125 LEU A CD1 
1023 C CD2 . LEU A 145 ? 0.3573 0.0592 0.2954 0.0165  0.0010  0.0198  125 LEU A CD2 
1024 N N   . VAL A 146 ? 0.3096 0.1053 0.2277 -0.0085 0.0108  0.0111  126 VAL A N   
1025 C CA  . VAL A 146 ? 0.2989 0.0910 0.2322 -0.0165 0.0050  0.0310  126 VAL A CA  
1026 C C   . VAL A 146 ? 0.2854 0.0879 0.2386 -0.0037 0.0070  0.0275  126 VAL A C   
1027 O O   . VAL A 146 ? 0.3131 0.0617 0.2382 0.0190  0.0085  0.0138  126 VAL A O   
1028 C CB  . VAL A 146 ? 0.3028 0.0824 0.2512 -0.0130 0.0014  0.0284  126 VAL A CB  
1029 C CG1 . VAL A 146 ? 0.3265 0.0852 0.2474 -0.0037 0.0015  -0.0099 126 VAL A CG1 
1030 C CG2 . VAL A 146 ? 0.3201 0.0700 0.2617 -0.0139 0.0154  0.0247  126 VAL A CG2 
1031 N N   . VAL A 147 ? 0.2974 0.0841 0.2569 -0.0037 0.0266  0.0421  127 VAL A N   
1032 C CA  . VAL A 147 ? 0.2941 0.0772 0.2466 -0.0144 0.0048  0.0263  127 VAL A CA  
1033 C C   . VAL A 147 ? 0.3099 0.0587 0.2390 0.0219  0.0041  -0.0037 127 VAL A C   
1034 O O   . VAL A 147 ? 0.2844 0.1273 0.2490 0.0287  -0.0030 0.0154  127 VAL A O   
1035 C CB  . VAL A 147 ? 0.3020 0.0742 0.2343 -0.0343 0.0074  0.0400  127 VAL A CB  
1036 C CG1 . VAL A 147 ? 0.3172 0.0683 0.2441 -0.0216 0.0007  0.0391  127 VAL A CG1 
1037 C CG2 . VAL A 147 ? 0.3362 0.1236 0.2415 -0.0162 0.0003  0.0190  127 VAL A CG2 
1038 N N   . VAL A 148 ? 0.3271 0.0853 0.2294 0.0062  0.0206  0.0171  128 VAL A N   
1039 C CA  . VAL A 148 ? 0.3216 0.0948 0.2271 -0.0072 0.0030  0.0248  128 VAL A CA  
1040 C C   . VAL A 148 ? 0.2686 0.1246 0.2279 -0.0131 -0.0095 0.0379  128 VAL A C   
1041 O O   . VAL A 148 ? 0.3058 0.0943 0.2643 -0.0121 -0.0017 0.0259  128 VAL A O   
1042 C CB  . VAL A 148 ? 0.3354 0.1311 0.2333 0.0016  0.0058  0.0158  128 VAL A CB  
1043 C CG1 . VAL A 148 ? 0.3672 0.0942 0.2143 0.0075  0.0023  0.0361  128 VAL A CG1 
1044 C CG2 . VAL A 148 ? 0.3425 0.1746 0.2324 -0.0138 -0.0045 0.0363  128 VAL A CG2 
1045 N N   . PRO A 149 ? 0.2846 0.1185 0.2709 -0.0056 0.0088  0.0421  129 PRO A N   
1046 C CA  . PRO A 149 ? 0.2805 0.1302 0.2660 -0.0044 0.0050  0.0612  129 PRO A CA  
1047 C C   . PRO A 149 ? 0.2886 0.1632 0.2589 -0.0052 -0.0129 0.0585  129 PRO A C   
1048 O O   . PRO A 149 ? 0.3160 0.1304 0.2382 0.0035  -0.0039 0.0436  129 PRO A O   
1049 C CB  . PRO A 149 ? 0.3447 0.1356 0.2945 0.0265  0.0027  0.0300  129 PRO A CB  
1050 C CG  . PRO A 149 ? 0.3314 0.1788 0.3468 0.0365  0.0186  0.0539  129 PRO A CG  
1051 C CD  . PRO A 149 ? 0.2923 0.1879 0.2833 0.0252  -0.0153 0.0489  129 PRO A CD  
1052 N N   . HIS A 150 ? 0.3149 0.1267 0.2588 -0.0227 -0.0006 0.0467  130 HIS A N   
1053 C CA  . HIS A 150 ? 0.2990 0.1131 0.2449 -0.0162 0.0340  0.0597  130 HIS A CA  
1054 C C   . HIS A 150 ? 0.2886 0.1166 0.2393 -0.0174 0.0371  0.0651  130 HIS A C   
1055 O O   . HIS A 150 ? 0.3166 0.1681 0.2566 -0.0013 -0.0014 0.0245  130 HIS A O   
1056 C CB  . HIS A 150 ? 0.3263 0.1231 0.2572 -0.0268 0.0140  0.0719  130 HIS A CB  
1057 C CG  . HIS A 150 ? 0.3345 0.1324 0.2780 -0.0188 0.0365  0.0519  130 HIS A CG  
1058 N ND1 . HIS A 150 ? 0.3205 0.1908 0.3073 -0.0489 0.0192  0.0243  130 HIS A ND1 
1059 C CD2 . HIS A 150 ? 0.3702 0.2458 0.3437 -0.0315 0.0267  -0.0036 130 HIS A CD2 
1060 C CE1 . HIS A 150 ? 0.3725 0.2270 0.3390 -0.0433 0.0230  -0.0012 130 HIS A CE1 
1061 N NE2 . HIS A 150 ? 0.4004 0.3221 0.3728 -0.0635 0.0597  -0.0370 130 HIS A NE2 
1062 N N   . ILE A 151 ? 0.2843 0.1320 0.2593 0.0042  0.0277  0.0578  131 ILE A N   
1063 C CA  . ILE A 151 ? 0.2886 0.1044 0.2826 0.0205  0.0110  0.0446  131 ILE A CA  
1064 C C   . ILE A 151 ? 0.2897 0.1228 0.2663 -0.0035 -0.0261 0.0395  131 ILE A C   
1065 O O   . ILE A 151 ? 0.3887 0.1024 0.2658 0.0164  -0.0278 0.0510  131 ILE A O   
1066 C CB  . ILE A 151 ? 0.3029 0.1563 0.3055 0.0271  0.0231  0.0564  131 ILE A CB  
1067 C CG1 . ILE A 151 ? 0.3380 0.1417 0.3233 0.0124  0.0288  0.0724  131 ILE A CG1 
1068 C CG2 . ILE A 151 ? 0.3076 0.1792 0.2932 0.0287  0.0275  0.0448  131 ILE A CG2 
1069 C CD1 . ILE A 151 ? 0.3562 0.1701 0.3371 0.0265  0.0276  0.0539  131 ILE A CD1 
1070 N N   . ILE A 152 ? 0.3152 0.0870 0.2555 0.0040  -0.0209 0.0280  132 ILE A N   
1071 C CA  . ILE A 152 ? 0.3195 0.1011 0.2554 0.0027  -0.0196 -0.0016 132 ILE A CA  
1072 C C   . ILE A 152 ? 0.2971 0.1152 0.2490 0.0024  0.0156  0.0321  132 ILE A C   
1073 O O   . ILE A 152 ? 0.3320 0.1195 0.2852 -0.0208 0.0188  0.0550  132 ILE A O   
1074 C CB  . ILE A 152 ? 0.3206 0.1137 0.2565 0.0109  -0.0157 0.0059  132 ILE A CB  
1075 C CG1 . ILE A 152 ? 0.3333 0.1108 0.2535 0.0224  -0.0117 0.0092  132 ILE A CG1 
1076 C CG2 . ILE A 152 ? 0.3173 0.1244 0.2943 0.0035  -0.0001 0.0397  132 ILE A CG2 
1077 C CD1 . ILE A 152 ? 0.3541 0.1400 0.2288 0.0201  -0.0017 0.0165  132 ILE A CD1 
1078 N N   . ALA A 153 ? 0.3047 0.0957 0.2614 0.0013  0.0184  0.0362  133 ALA A N   
1079 C CA  . ALA A 153 ? 0.2939 0.1207 0.2472 0.0003  0.0225  0.0344  133 ALA A CA  
1080 C C   . ALA A 153 ? 0.3009 0.1549 0.2651 -0.0060 0.0050  0.0219  133 ALA A C   
1081 O O   . ALA A 153 ? 0.3327 0.1274 0.3197 -0.0134 0.0037  0.0143  133 ALA A O   
1082 C CB  . ALA A 153 ? 0.3317 0.0978 0.2579 0.0250  0.0134  0.0372  133 ALA A CB  
1083 N N   . ASP A 154 ? 0.3283 0.0927 0.2648 -0.0209 0.0269  0.0203  134 ASP A N   
1084 C CA  . ASP A 154 ? 0.3103 0.1228 0.2688 0.0039  0.0044  0.0298  134 ASP A CA  
1085 C C   . ASP A 154 ? 0.2914 0.1193 0.2390 -0.0187 0.0047  0.0233  134 ASP A C   
1086 O O   . ASP A 154 ? 0.2938 0.1242 0.2411 -0.0026 0.0253  0.0283  134 ASP A O   
1087 C CB  . ASP A 154 ? 0.3481 0.1135 0.2460 0.0031  -0.0208 0.0368  134 ASP A CB  
1088 C CG  . ASP A 154 ? 0.3604 0.1498 0.2401 -0.0052 -0.0267 0.0208  134 ASP A CG  
1089 O OD1 . ASP A 154 ? 0.3801 0.1712 0.2455 -0.0001 -0.0162 0.0420  134 ASP A OD1 
1090 O OD2 . ASP A 154 ? 0.4125 0.1430 0.2783 -0.0233 -0.0447 0.0508  134 ASP A OD2 
1091 N N   . GLY A 155 ? 0.3205 0.1405 0.2768 0.0085  -0.0101 0.0159  135 GLY A N   
1092 C CA  . GLY A 155 ? 0.2720 0.1363 0.2898 -0.0043 -0.0029 0.0079  135 GLY A CA  
1093 C C   . GLY A 155 ? 0.2924 0.1347 0.2569 -0.0124 -0.0008 0.0079  135 GLY A C   
1094 O O   . GLY A 155 ? 0.3177 0.1140 0.2407 -0.0032 -0.0052 -0.0085 135 GLY A O   
1095 N N   . THR A 156 ? 0.2865 0.1071 0.2476 -0.0353 0.0171  0.0292  136 THR A N   
1096 C CA  . THR A 156 ? 0.3194 0.0880 0.2414 -0.0237 0.0074  0.0042  136 THR A CA  
1097 C C   . THR A 156 ? 0.2997 0.0992 0.2266 -0.0112 -0.0065 0.0086  136 THR A C   
1098 O O   . THR A 156 ? 0.3280 0.1068 0.2348 -0.0079 0.0316  0.0242  136 THR A O   
1099 C CB  . THR A 156 ? 0.3479 0.1182 0.2351 -0.0258 0.0338  0.0022  136 THR A CB  
1100 O OG1 . THR A 156 ? 0.3906 0.2075 0.2588 -0.0432 0.0379  -0.0213 136 THR A OG1 
1101 C CG2 . THR A 156 ? 0.3549 0.1715 0.2539 -0.0466 0.0153  -0.0055 136 THR A CG2 
1102 N N   . THR A 157 ? 0.2951 0.0839 0.2392 0.0071  0.0171  -0.0036 137 THR A N   
1103 C CA  . THR A 157 ? 0.2983 0.0494 0.2464 0.0151  0.0023  0.0101  137 THR A CA  
1104 C C   . THR A 157 ? 0.2652 0.0971 0.2310 -0.0063 -0.0060 0.0128  137 THR A C   
1105 O O   . THR A 157 ? 0.3207 0.0582 0.2433 -0.0274 -0.0091 0.0163  137 THR A O   
1106 C CB  . THR A 157 ? 0.3488 0.0680 0.2572 0.0415  -0.0067 0.0091  137 THR A CB  
1107 O OG1 . THR A 157 ? 0.3778 0.1806 0.2651 0.0501  -0.0275 0.0126  137 THR A OG1 
1108 C CG2 . THR A 157 ? 0.3437 0.0631 0.2940 0.0152  -0.0137 0.0054  137 THR A CG2 
1109 N N   . VAL A 158 ? 0.3027 0.0582 0.2442 0.0013  -0.0101 0.0125  138 VAL A N   
1110 C CA  . VAL A 158 ? 0.2962 0.0824 0.2462 -0.0031 -0.0032 0.0283  138 VAL A CA  
1111 C C   . VAL A 158 ? 0.2773 0.0907 0.2123 0.0033  -0.0041 0.0065  138 VAL A C   
1112 O O   . VAL A 158 ? 0.3378 0.0576 0.2478 -0.0049 0.0111  0.0024  138 VAL A O   
1113 C CB  . VAL A 158 ? 0.2991 0.1254 0.2326 -0.0023 -0.0192 0.0032  138 VAL A CB  
1114 C CG1 . VAL A 158 ? 0.3043 0.1354 0.2534 -0.0212 -0.0037 0.0236  138 VAL A CG1 
1115 C CG2 . VAL A 158 ? 0.3118 0.0720 0.2609 0.0246  -0.0128 0.0160  138 VAL A CG2 
1116 N N   . LEU A 159 ? 0.2812 0.0835 0.2311 0.0309  0.0048  0.0340  139 LEU A N   
1117 C CA  . LEU A 159 ? 0.2755 0.0903 0.2480 0.0229  -0.0182 0.0288  139 LEU A CA  
1118 C C   . LEU A 159 ? 0.2832 0.1068 0.2323 0.0107  -0.0010 0.0212  139 LEU A C   
1119 O O   . LEU A 159 ? 0.3207 0.0284 0.2546 0.0009  -0.0089 0.0128  139 LEU A O   
1120 C CB  . LEU A 159 ? 0.2840 0.0834 0.2659 0.0179  -0.0186 0.0349  139 LEU A CB  
1121 C CG  . LEU A 159 ? 0.2828 0.1101 0.2884 0.0032  -0.0056 0.0106  139 LEU A CG  
1122 C CD1 . LEU A 159 ? 0.2869 0.0852 0.2940 -0.0116 -0.0016 0.0166  139 LEU A CD1 
1123 C CD2 . LEU A 159 ? 0.2868 0.0583 0.2888 0.0016  -0.0070 -0.0064 139 LEU A CD2 
1124 N N   . THR A 160 ? 0.2810 0.0800 0.2234 -0.0109 0.0012  0.0187  140 THR A N   
1125 C CA  . THR A 160 ? 0.2942 0.0874 0.2445 -0.0132 -0.0117 0.0233  140 THR A CA  
1126 C C   . THR A 160 ? 0.2980 0.0868 0.2093 -0.0127 0.0035  0.0279  140 THR A C   
1127 O O   . THR A 160 ? 0.3140 0.0862 0.2604 -0.0021 0.0146  0.0544  140 THR A O   
1128 C CB  . THR A 160 ? 0.2980 0.1180 0.2455 -0.0346 -0.0206 0.0130  140 THR A CB  
1129 O OG1 . THR A 160 ? 0.3078 0.1244 0.2469 -0.0458 -0.0173 0.0030  140 THR A OG1 
1130 C CG2 . THR A 160 ? 0.3105 0.0788 0.2311 -0.0296 -0.0327 0.0012  140 THR A CG2 
1131 N N   . LEU A 161 ? 0.2890 0.0834 0.2230 -0.0034 0.0035  0.0179  141 LEU A N   
1132 C CA  . LEU A 161 ? 0.2876 0.0759 0.2325 -0.0140 -0.0039 0.0066  141 LEU A CA  
1133 C C   . LEU A 161 ? 0.2989 0.0923 0.2344 0.0206  0.0035  -0.0009 141 LEU A C   
1134 O O   . LEU A 161 ? 0.3135 0.0994 0.2591 -0.0084 0.0047  0.0156  141 LEU A O   
1135 C CB  . LEU A 161 ? 0.3155 0.0771 0.2348 -0.0091 -0.0069 0.0038  141 LEU A CB  
1136 C CG  . LEU A 161 ? 0.3106 0.0988 0.2341 0.0114  0.0074  0.0148  141 LEU A CG  
1137 C CD1 . LEU A 161 ? 0.3523 0.0901 0.2421 0.0188  0.0086  0.0230  141 LEU A CD1 
1138 C CD2 . LEU A 161 ? 0.3337 0.1109 0.2516 0.0048  0.0026  0.0500  141 LEU A CD2 
1139 N N   . ALA A 162 ? 0.3145 0.0904 0.2268 -0.0017 -0.0055 0.0417  142 ALA A N   
1140 C CA  . ALA A 162 ? 0.3095 0.0843 0.2491 0.0095  -0.0170 0.0091  142 ALA A CA  
1141 C C   . ALA A 162 ? 0.3211 0.0885 0.2593 0.0166  -0.0136 0.0326  142 ALA A C   
1142 O O   . ALA A 162 ? 0.3608 0.0630 0.2713 -0.0202 -0.0167 0.0430  142 ALA A O   
1143 C CB  . ALA A 162 ? 0.3399 0.0078 0.2485 0.0067  -0.0196 0.0177  142 ALA A CB  
1144 N N   . GLU A 163 ? 0.3278 0.0729 0.2499 -0.0258 -0.0184 0.0390  143 GLU A N   
1145 C CA  . GLU A 163 ? 0.3230 0.0761 0.2823 0.0219  -0.0013 0.0312  143 GLU A CA  
1146 C C   . GLU A 163 ? 0.3151 0.1099 0.2665 0.0033  -0.0160 0.0295  143 GLU A C   
1147 O O   . GLU A 163 ? 0.3325 0.1027 0.2876 0.0030  -0.0100 0.0386  143 GLU A O   
1148 C CB  . GLU A 163 ? 0.2992 0.0084 0.3141 -0.0022 0.0055  0.0133  143 GLU A CB  
1149 C CG  . GLU A 163 ? 0.3576 0.0074 0.3513 -0.0045 0.0274  0.0135  143 GLU A CG  
1150 C CD  . GLU A 163 ? 0.3990 0.0976 0.3715 -0.0035 0.0454  -0.0227 143 GLU A CD  
1151 O OE1 . GLU A 163 ? 0.4285 0.0897 0.4259 0.0174  0.0108  -0.0515 143 GLU A OE1 
1152 O OE2 . GLU A 163 ? 0.4541 0.1607 0.3962 -0.0254 0.0555  -0.0049 143 GLU A OE2 
1153 N N   . GLN A 164 ? 0.2698 0.1186 0.2743 -0.0176 -0.0194 -0.0073 144 GLN A N   
1154 C CA  . GLN A 164 ? 0.2870 0.0507 0.2541 -0.0094 -0.0075 0.0172  144 GLN A CA  
1155 C C   . GLN A 164 ? 0.2953 0.1200 0.2547 -0.0100 0.0070  0.0100  144 GLN A C   
1156 O O   . GLN A 164 ? 0.3425 0.0840 0.2833 -0.0090 0.0052  0.0360  144 GLN A O   
1157 C CB  . GLN A 164 ? 0.2985 0.0801 0.2563 0.0076  -0.0173 0.0182  144 GLN A CB  
1158 C CG  . GLN A 164 ? 0.2906 0.0833 0.2637 -0.0068 -0.0076 0.0207  144 GLN A CG  
1159 C CD  . GLN A 164 ? 0.3115 0.1018 0.2743 -0.0040 -0.0005 0.0088  144 GLN A CD  
1160 O OE1 . GLN A 164 ? 0.2983 0.0707 0.3078 -0.0071 -0.0068 0.0316  144 GLN A OE1 
1161 N NE2 . GLN A 164 ? 0.3208 0.0816 0.2743 -0.0063 0.0191  0.0128  144 GLN A NE2 
1162 N N   . TRP A 165 ? 0.3290 0.0970 0.2501 0.0092  -0.0046 0.0241  145 TRP A N   
1163 C CA  . TRP A 165 ? 0.3148 0.0869 0.2533 0.0136  -0.0042 0.0228  145 TRP A CA  
1164 C C   . TRP A 165 ? 0.3194 0.1505 0.2476 0.0136  -0.0016 0.0364  145 TRP A C   
1165 O O   . TRP A 165 ? 0.3010 0.1065 0.3067 -0.0084 0.0056  0.0440  145 TRP A O   
1166 C CB  . TRP A 165 ? 0.3332 0.0722 0.2703 0.0000  0.0009  0.0539  145 TRP A CB  
1167 C CG  . TRP A 165 ? 0.3296 0.1111 0.2455 -0.0038 -0.0127 0.0483  145 TRP A CG  
1168 C CD1 . TRP A 165 ? 0.3386 0.1015 0.2321 -0.0129 -0.0131 0.0659  145 TRP A CD1 
1169 C CD2 . TRP A 165 ? 0.3468 0.0954 0.2542 0.0048  -0.0018 0.0428  145 TRP A CD2 
1170 N NE1 . TRP A 165 ? 0.3314 0.1328 0.2488 -0.0057 0.0150  0.0778  145 TRP A NE1 
1171 C CE2 . TRP A 165 ? 0.3515 0.1110 0.2579 -0.0016 0.0028  0.0517  145 TRP A CE2 
1172 C CE3 . TRP A 165 ? 0.3479 0.1410 0.2464 -0.0113 0.0022  0.0385  145 TRP A CE3 
1173 C CZ2 . TRP A 165 ? 0.3325 0.1459 0.2390 0.0069  0.0154  0.0438  145 TRP A CZ2 
1174 C CZ3 . TRP A 165 ? 0.3691 0.0887 0.2407 0.0092  0.0007  0.0595  145 TRP A CZ3 
1175 C CH2 . TRP A 165 ? 0.3516 0.1267 0.2576 0.0235  -0.0028 0.0448  145 TRP A CH2 
1176 N N   . LEU A 166 ? 0.2927 0.1140 0.2708 0.0394  -0.0229 0.0530  146 LEU A N   
1177 C CA  . LEU A 166 ? 0.2908 0.0862 0.2837 0.0220  -0.0267 0.0511  146 LEU A CA  
1178 C C   . LEU A 166 ? 0.3092 0.0992 0.2973 -0.0063 -0.0071 0.0529  146 LEU A C   
1179 O O   . LEU A 166 ? 0.3551 0.1043 0.3041 0.0223  -0.0455 0.0816  146 LEU A O   
1180 C CB  . LEU A 166 ? 0.3282 0.0948 0.2820 0.0160  -0.0221 0.0617  146 LEU A CB  
1181 C CG  . LEU A 166 ? 0.3310 0.1291 0.3032 0.0138  -0.0332 0.0283  146 LEU A CG  
1182 C CD1 . LEU A 166 ? 0.3651 0.1404 0.2896 -0.0079 -0.0302 0.0428  146 LEU A CD1 
1183 C CD2 . LEU A 166 ? 0.3553 0.1011 0.3073 0.0183  -0.0286 0.0139  146 LEU A CD2 
1184 N N   . THR A 167 ? 0.3164 0.0561 0.3446 -0.0444 -0.0176 0.0453  147 THR A N   
1185 C CA  . THR A 167 ? 0.3513 0.0341 0.3580 -0.0125 0.0036  0.0247  147 THR A CA  
1186 C C   . THR A 167 ? 0.3500 0.0504 0.3464 -0.0370 -0.0027 0.0539  147 THR A C   
1187 O O   . THR A 167 ? 0.3790 0.0479 0.3700 -0.0476 -0.0140 0.0643  147 THR A O   
1188 C CB  . THR A 167 ? 0.3393 0.0789 0.3492 -0.0167 -0.0107 0.0051  147 THR A CB  
1189 O OG1 . THR A 167 ? 0.3349 0.1937 0.3316 -0.0350 -0.0100 0.0286  147 THR A OG1 
1190 C CG2 . THR A 167 ? 0.3710 0.1090 0.3632 -0.0317 -0.0287 0.0011  147 THR A CG2 
1191 N N   . LEU A 168 ? 0.3360 0.1071 0.3345 -0.0145 -0.0082 0.0440  148 LEU A N   
1192 C CA  . LEU A 168 ? 0.3508 0.0841 0.3495 -0.0259 -0.0171 0.0580  148 LEU A CA  
1193 C C   . LEU A 168 ? 0.3521 0.1537 0.3393 -0.0354 -0.0087 0.0935  148 LEU A C   
1194 O O   . LEU A 168 ? 0.4054 0.2423 0.3963 -0.1109 -0.0282 0.1132  148 LEU A O   
1195 C CB  . LEU A 168 ? 0.3668 0.1124 0.3476 -0.0062 -0.0213 0.0608  148 LEU A CB  
1196 C CG  . LEU A 168 ? 0.3305 0.1061 0.3470 0.0049  -0.0146 0.0579  148 LEU A CG  
1197 C CD1 . LEU A 168 ? 0.3470 0.1072 0.3347 0.0158  -0.0058 0.0487  148 LEU A CD1 
1198 C CD2 . LEU A 168 ? 0.3427 0.1001 0.3679 0.0071  -0.0195 0.0768  148 LEU A CD2 
1199 N N   . ALA A 169 ? 0.3490 0.1348 0.3146 0.0003  -0.0004 0.0713  149 ALA A N   
1200 C CA  . ALA A 169 ? 0.3748 0.1837 0.3248 -0.0035 -0.0134 0.0683  149 ALA A CA  
1201 C C   . ALA A 169 ? 0.4007 0.2019 0.3636 -0.0034 -0.0273 0.0870  149 ALA A C   
1202 O O   . ALA A 169 ? 0.4802 0.1990 0.3644 -0.0106 -0.0130 0.0636  149 ALA A O   
1203 C CB  . ALA A 169 ? 0.3753 0.2428 0.2982 -0.0241 -0.0347 0.0880  149 ALA A CB  
1204 N N   . ALA A 170 ? 0.4077 0.1367 0.3483 0.0155  -0.0309 0.1087  150 ALA A N   
1205 C CA  . ALA A 170 ? 0.4181 0.1610 0.3892 0.0248  -0.0434 0.1133  150 ALA A CA  
1206 C C   . ALA A 170 ? 0.4144 0.1484 0.4190 0.0185  -0.0767 0.1297  150 ALA A C   
1207 O O   . ALA A 170 ? 0.4410 0.1730 0.4560 0.0354  -0.1169 0.1515  150 ALA A O   
1208 C CB  . ALA A 170 ? 0.4181 0.1569 0.4105 0.0248  -0.0453 0.1326  150 ALA A CB  
1209 N N   . ASP A 171 ? 0.4278 0.1188 0.4632 -0.0116 -0.0717 0.1042  151 ASP A N   
1210 C CA  . ASP A 171 ? 0.4636 0.1636 0.5036 -0.0003 -0.1041 0.0623  151 ASP A CA  
1211 C C   . ASP A 171 ? 0.5107 0.1909 0.5581 -0.0703 -0.0767 0.1118  151 ASP A C   
1212 O O   . ASP A 171 ? 0.4274 0.1265 0.5328 -0.0658 -0.0661 0.0468  151 ASP A O   
1213 C CB  . ASP A 171 ? 0.4347 0.1530 0.5000 0.0326  -0.0756 0.0275  151 ASP A CB  
1214 C CG  . ASP A 171 ? 0.5039 0.1747 0.4978 -0.0082 -0.0668 0.0246  151 ASP A CG  
1215 O OD1 . ASP A 171 ? 0.5427 0.1304 0.6162 -0.0124 -0.1053 0.0221  151 ASP A OD1 
1216 O OD2 . ASP A 171 ? 0.5618 0.2266 0.4706 0.0283  -0.0407 -0.0416 151 ASP A OD2 
1217 N N   . PRO A 172 ? 0.6455 0.2602 0.6523 -0.1683 -0.0772 0.1419  152 PRO A N   
1218 C CA  . PRO A 172 ? 0.6412 0.3201 0.7190 -0.1675 -0.0490 0.0725  152 PRO A CA  
1219 C C   . PRO A 172 ? 0.6059 0.2730 0.6763 -0.1121 -0.0399 0.0897  152 PRO A C   
1220 O O   . PRO A 172 ? 0.6154 0.2603 0.7414 -0.0750 -0.0412 0.0761  152 PRO A O   
1221 C CB  . PRO A 172 ? 0.6825 0.3648 0.7428 -0.1788 -0.0662 0.0831  152 PRO A CB  
1222 C CG  . PRO A 172 ? 0.6810 0.4190 0.7548 -0.1855 -0.0528 0.1287  152 PRO A CG  
1223 C CD  . PRO A 172 ? 0.6851 0.2386 0.7224 -0.1759 -0.0980 0.1326  152 PRO A CD  
1224 N N   . ALA A 173 ? 0.6473 0.1538 0.7196 -0.0712 -0.0509 0.0641  153 ALA A N   
1225 C CA  . ALA A 173 ? 0.6567 0.2658 0.6862 -0.0336 -0.0872 0.0293  153 ALA A CA  
1226 C C   . ALA A 173 ? 0.6431 0.1716 0.6525 -0.0227 -0.0946 0.0085  153 ALA A C   
1227 O O   . ALA A 173 ? 0.7416 0.1917 0.7233 -0.0107 -0.1924 0.0476  153 ALA A O   
1228 C CB  . ALA A 173 ? 0.6888 0.3169 0.7240 -0.0306 -0.0635 0.0257  153 ALA A CB  
1229 N N   . ALA A 174 ? 0.5169 0.1748 0.5639 -0.0243 -0.0726 0.0413  154 ALA A N   
1230 C CA  . ALA A 174 ? 0.4405 0.2061 0.5014 -0.0035 -0.0547 0.0167  154 ALA A CA  
1231 C C   . ALA A 174 ? 0.3924 0.1274 0.4543 0.0152  -0.0168 0.0028  154 ALA A C   
1232 O O   . ALA A 174 ? 0.4102 0.2103 0.4064 0.0125  0.0275  0.0272  154 ALA A O   
1233 C CB  . ALA A 174 ? 0.4113 0.1938 0.4933 -0.0058 -0.0725 0.0113  154 ALA A CB  
1234 N N   . GLN A 175 ? 0.4225 0.1331 0.4583 0.0399  -0.0367 -0.0099 155 GLN A N   
1235 C CA  . GLN A 175 ? 0.4199 0.2112 0.4926 0.0358  -0.0137 -0.0192 155 GLN A CA  
1236 C C   . GLN A 175 ? 0.3926 0.1503 0.4124 -0.0155 -0.0042 0.0078  155 GLN A C   
1237 O O   . GLN A 175 ? 0.4318 0.1498 0.4400 -0.0245 0.0144  0.0249  155 GLN A O   
1238 C CB  . GLN A 175 ? 0.4896 0.3361 0.5317 0.0605  -0.0162 -0.0365 155 GLN A CB  
1239 C CG  . GLN A 175 ? 0.5379 0.3796 0.6055 0.0634  -0.0239 -0.0171 155 GLN A CG  
1240 C CD  . GLN A 175 ? 0.5463 0.4637 0.6795 0.0517  -0.0323 -0.0649 155 GLN A CD  
1241 O OE1 . GLN A 175 ? 0.6658 0.4924 0.7098 0.0425  0.0144  -0.2127 155 GLN A OE1 
1242 N NE2 . GLN A 175 ? 0.5612 0.5635 0.6998 0.0636  -0.0157 -0.0175 155 GLN A NE2 
1243 N N   . PRO A 176 ? 0.4061 0.0818 0.4177 -0.0193 -0.0096 0.0080  156 PRO A N   
1244 C CA  . PRO A 176 ? 0.3819 0.1492 0.4177 0.0158  -0.0083 0.0137  156 PRO A CA  
1245 C C   . PRO A 176 ? 0.4068 0.1451 0.3705 -0.0287 -0.0003 -0.0074 156 PRO A C   
1246 O O   . PRO A 176 ? 0.4567 0.1335 0.4339 -0.0095 -0.0436 -0.0571 156 PRO A O   
1247 C CB  . PRO A 176 ? 0.4202 0.0968 0.4682 -0.0087 0.0024  0.0321  156 PRO A CB  
1248 C CG  . PRO A 176 ? 0.4716 0.1242 0.5233 -0.0209 0.0201  0.0422  156 PRO A CG  
1249 C CD  . PRO A 176 ? 0.4112 0.1004 0.4708 -0.0116 0.0096  0.0567  156 PRO A CD  
1250 N N   . TRP A 177 ? 0.3687 0.1517 0.3679 -0.0244 -0.0031 0.0039  157 TRP A N   
1251 C CA  . TRP A 177 ? 0.3666 0.1329 0.3835 -0.0479 -0.0182 -0.0091 157 TRP A CA  
1252 C C   . TRP A 177 ? 0.3542 0.1314 0.3476 -0.0319 -0.0239 0.0212  157 TRP A C   
1253 O O   . TRP A 177 ? 0.3622 0.1389 0.3114 -0.0256 -0.0126 0.0412  157 TRP A O   
1254 C CB  . TRP A 177 ? 0.3820 0.1724 0.3796 -0.0483 -0.0202 -0.0146 157 TRP A CB  
1255 C CG  . TRP A 177 ? 0.3753 0.1885 0.3864 -0.0614 0.0066  0.0084  157 TRP A CG  
1256 C CD1 . TRP A 177 ? 0.3724 0.2048 0.3852 -0.0380 -0.0124 -0.0142 157 TRP A CD1 
1257 C CD2 . TRP A 177 ? 0.3726 0.1738 0.3990 -0.0398 0.0216  0.0070  157 TRP A CD2 
1258 N NE1 . TRP A 177 ? 0.3695 0.2494 0.3698 -0.0444 -0.0200 -0.0108 157 TRP A NE1 
1259 C CE2 . TRP A 177 ? 0.3582 0.1888 0.3734 -0.0420 0.0097  -0.0249 157 TRP A CE2 
1260 C CE3 . TRP A 177 ? 0.3504 0.2175 0.3810 -0.0210 0.0144  -0.0058 157 TRP A CE3 
1261 C CZ2 . TRP A 177 ? 0.3430 0.2555 0.3670 -0.0559 -0.0103 -0.0107 157 TRP A CZ2 
1262 C CZ3 . TRP A 177 ? 0.3530 0.2218 0.4152 -0.0265 0.0414  -0.0110 157 TRP A CZ3 
1263 C CH2 . TRP A 177 ? 0.3723 0.1780 0.3617 -0.0459 0.0216  -0.0183 157 TRP A CH2 
1264 N N   . THR A 178 ? 0.3778 0.1171 0.3370 -0.0222 -0.0275 0.0260  158 THR A N   
1265 C CA  . THR A 178 ? 0.3640 0.1135 0.3230 -0.0176 0.0006  0.0222  158 THR A CA  
1266 C C   . THR A 178 ? 0.3503 0.1274 0.3006 -0.0444 0.0095  -0.0060 158 THR A C   
1267 O O   . THR A 178 ? 0.4095 0.1537 0.3081 -0.0197 -0.0035 -0.0098 158 THR A O   
1268 C CB  . THR A 178 ? 0.3729 0.2372 0.3195 -0.0505 0.0044  0.0518  158 THR A CB  
1269 O OG1 . THR A 178 ? 0.3157 0.3124 0.3464 -0.0380 -0.0121 0.0319  158 THR A OG1 
1270 C CG2 . THR A 178 ? 0.3819 0.2516 0.3167 -0.0410 0.0033  0.0705  158 THR A CG2 
1271 N N   . ALA A 179 ? 0.3586 0.0992 0.3298 -0.0044 0.0059  0.0051  159 ALA A N   
1272 C CA  . ALA A 179 ? 0.3473 0.1735 0.2917 -0.0309 -0.0005 0.0012  159 ALA A CA  
1273 C C   . ALA A 179 ? 0.3625 0.1404 0.3024 -0.0362 0.0078  0.0361  159 ALA A C   
1274 O O   . ALA A 179 ? 0.3648 0.1795 0.3344 -0.0240 0.0122  0.0514  159 ALA A O   
1275 C CB  . ALA A 179 ? 0.3581 0.1693 0.3097 -0.0167 -0.0055 0.0056  159 ALA A CB  
1276 N N   . SER A 180 ? 0.4182 0.2151 0.2957 -0.0204 0.0164  0.0123  160 SER A N   
1277 C CA  . SER A 180 ? 0.4386 0.1819 0.3493 -0.0175 0.0010  0.0358  160 SER A CA  
1278 C C   . SER A 180 ? 0.3809 0.1898 0.3071 -0.0240 0.0064  0.0240  160 SER A C   
1279 O O   . SER A 180 ? 0.3334 0.2057 0.2994 -0.0062 -0.0095 0.0517  160 SER A O   
1280 C CB  . SER A 180 ? 0.4901 0.1583 0.3650 0.0013  -0.0435 -0.0202 160 SER A CB  
1281 O OG  . SER A 180 ? 0.6359 0.1957 0.5001 0.0101  -0.1016 -0.0317 160 SER A OG  
1282 N N   . ALA A 181 ? 0.3541 0.1990 0.3215 -0.0419 0.0059  0.0648  161 ALA A N   
1283 C CA  . ALA A 181 ? 0.3599 0.2011 0.2869 -0.0166 -0.0007 0.0151  161 ALA A CA  
1284 C C   . ALA A 181 ? 0.3322 0.2068 0.3102 -0.0288 -0.0102 0.0236  161 ALA A C   
1285 O O   . ALA A 181 ? 0.3657 0.2498 0.3400 -0.0978 -0.0296 0.0299  161 ALA A O   
1286 C CB  . ALA A 181 ? 0.3852 0.2111 0.3211 -0.0039 -0.0005 0.0206  161 ALA A CB  
1287 N N   . LEU A 182 ? 0.3344 0.1893 0.2876 -0.0456 0.0064  0.0148  162 LEU A N   
1288 C CA  . LEU A 182 ? 0.3509 0.1849 0.2996 -0.0331 0.0239  0.0178  162 LEU A CA  
1289 C C   . LEU A 182 ? 0.3487 0.1982 0.2907 -0.0415 0.0262  0.0228  162 LEU A C   
1290 O O   . LEU A 182 ? 0.3481 0.2410 0.2878 -0.0231 0.0171  0.0103  162 LEU A O   
1291 C CB  . LEU A 182 ? 0.3551 0.2107 0.3014 -0.0041 0.0318  0.0161  162 LEU A CB  
1292 C CG  . LEU A 182 ? 0.3825 0.2568 0.3317 0.0156  0.0263  0.0251  162 LEU A CG  
1293 C CD1 . LEU A 182 ? 0.3956 0.2984 0.3118 0.0024  0.0300  0.0528  162 LEU A CD1 
1294 C CD2 . LEU A 182 ? 0.4195 0.2802 0.3725 -0.0028 -0.0079 0.0223  162 LEU A CD2 
1295 N N   . PRO A 183 ? 0.3922 0.1940 0.3069 -0.0332 0.0067  0.0299  163 PRO A N   
1296 C CA  . PRO A 183 ? 0.3705 0.2310 0.3135 -0.0002 -0.0026 0.0561  163 PRO A CA  
1297 C C   . PRO A 183 ? 0.3457 0.2311 0.3368 0.0043  0.0036  0.0616  163 PRO A C   
1298 O O   . PRO A 183 ? 0.3163 0.2216 0.3360 -0.0281 -0.0189 0.0576  163 PRO A O   
1299 C CB  . PRO A 183 ? 0.3933 0.2888 0.3114 0.0002  -0.0110 0.0360  163 PRO A CB  
1300 C CG  . PRO A 183 ? 0.4031 0.3172 0.3010 -0.0118 0.0047  0.0274  163 PRO A CG  
1301 C CD  . PRO A 183 ? 0.3836 0.2784 0.3052 -0.0171 -0.0022 0.0163  163 PRO A CD  
1302 N N   . PRO A 184 ? 0.3989 0.2144 0.3248 0.0042  0.0000  0.0552  164 PRO A N   
1303 C CA  . PRO A 184 ? 0.3830 0.2592 0.3123 0.0102  0.0025  0.0673  164 PRO A CA  
1304 C C   . PRO A 184 ? 0.3949 0.2547 0.3325 -0.0156 0.0111  0.0617  164 PRO A C   
1305 O O   . PRO A 184 ? 0.3880 0.2841 0.3365 -0.0210 0.0247  0.0880  164 PRO A O   
1306 C CB  . PRO A 184 ? 0.4082 0.2626 0.3361 0.0265  0.0013  0.0540  164 PRO A CB  
1307 C CG  . PRO A 184 ? 0.4201 0.2325 0.3603 0.0174  -0.0091 0.0968  164 PRO A CG  
1308 C CD  . PRO A 184 ? 0.3820 0.2867 0.3769 -0.0181 -0.0082 0.0603  164 PRO A CD  
1309 N N   . ALA A 185 ? 0.3822 0.2430 0.3381 0.0150  0.0085  0.0660  165 ALA A N   
1310 C CA  . ALA A 185 ? 0.3609 0.2570 0.3757 0.0000  0.0149  0.0524  165 ALA A CA  
1311 C C   . ALA A 185 ? 0.3712 0.3189 0.3670 0.0105  0.0218  0.0568  165 ALA A C   
1312 O O   . ALA A 185 ? 0.4070 0.3137 0.3970 -0.0071 0.0037  0.0232  165 ALA A O   
1313 C CB  . ALA A 185 ? 0.3685 0.2664 0.3986 -0.0181 0.0134  0.0438  165 ALA A CB  
1314 N N   . GLU A 186 ? 0.3914 0.2983 0.3882 0.0017  0.0369  0.0466  166 GLU A N   
1315 C CA  . GLU A 186 ? 0.4479 0.3871 0.3829 0.0236  0.0269  0.0709  166 GLU A CA  
1316 C C   . GLU A 186 ? 0.4574 0.4074 0.3510 0.0470  0.0225  0.0934  166 GLU A C   
1317 O O   . GLU A 186 ? 0.4939 0.4906 0.3571 0.0129  0.0381  0.0872  166 GLU A O   
1318 C CB  . GLU A 186 ? 0.5063 0.3659 0.4403 0.0274  -0.0197 0.0904  166 GLU A CB  
1319 C CG  . GLU A 186 ? 0.5658 0.3970 0.4739 -0.0108 -0.0236 0.0816  166 GLU A CG  
1320 C CD  . GLU A 186 ? 0.6212 0.3684 0.5190 -0.0653 -0.0642 0.1053  166 GLU A CD  
1321 O OE1 . GLU A 186 ? 0.8280 0.3428 0.5946 -0.0802 -0.1121 0.1541  166 GLU A OE1 
1322 O OE2 . GLU A 186 ? 0.4736 0.3313 0.4856 -0.0517 -0.0248 0.1036  166 GLU A OE2 
1323 N N   . ASP A 187 ? 0.3968 0.4228 0.3148 0.0534  -0.0124 0.0742  167 ASP A N   
1324 C CA  . ASP A 187 ? 0.4121 0.4566 0.3265 0.0461  -0.0209 0.0394  167 ASP A CA  
1325 C C   . ASP A 187 ? 0.4102 0.4945 0.3502 0.0429  -0.0371 -0.0127 167 ASP A C   
1326 O O   . ASP A 187 ? 0.3901 0.5993 0.3841 0.0737  -0.0524 -0.0223 167 ASP A O   
1327 C CB  . ASP A 187 ? 0.4215 0.4809 0.3377 0.0145  -0.0381 0.0381  167 ASP A CB  
1328 C CG  . ASP A 187 ? 0.4193 0.5042 0.4121 0.0024  -0.0173 0.0720  167 ASP A CG  
1329 O OD1 . ASP A 187 ? 0.4445 0.4701 0.4727 -0.0041 -0.0074 0.1116  167 ASP A OD1 
1330 O OD2 . ASP A 187 ? 0.4185 0.5744 0.4758 0.0410  -0.0095 0.0994  167 ASP A OD2 
1331 N N   . LEU A 188 ? 0.3871 0.3987 0.2907 0.0317  -0.0128 -0.0087 168 LEU A N   
1332 C CA  . LEU A 188 ? 0.3915 0.4351 0.3145 0.0377  -0.0093 -0.0044 168 LEU A CA  
1333 C C   . LEU A 188 ? 0.4374 0.4627 0.3023 0.0274  -0.0143 -0.0004 168 LEU A C   
1334 O O   . LEU A 188 ? 0.4517 0.4798 0.3233 0.0236  -0.0297 0.0069  168 LEU A O   
1335 C CB  . LEU A 188 ? 0.4250 0.4094 0.3138 0.0187  0.0064  -0.0068 168 LEU A CB  
1336 C CG  . LEU A 188 ? 0.4278 0.4088 0.3251 -0.0100 0.0172  -0.0125 168 LEU A CG  
1337 C CD1 . LEU A 188 ? 0.4365 0.3814 0.3396 -0.0074 0.0356  0.0220  168 LEU A CD1 
1338 C CD2 . LEU A 188 ? 0.4623 0.4315 0.3603 -0.0188 0.0467  -0.0399 168 LEU A CD2 
1339 N N   . ARG A 189 ? 0.4356 0.4362 0.2898 0.0557  -0.0091 0.0456  169 ARG A N   
1340 C CA  . ARG A 189 ? 0.4863 0.5644 0.2926 0.0491  0.0109  0.0156  169 ARG A CA  
1341 C C   . ARG A 189 ? 0.4894 0.6125 0.2936 0.0164  -0.0119 0.0254  169 ARG A C   
1342 O O   . ARG A 189 ? 0.5037 0.5748 0.3568 0.0350  -0.0429 0.0504  169 ARG A O   
1343 C CB  . ARG A 189 ? 0.4706 0.5928 0.3140 0.0553  0.0080  0.0128  169 ARG A CB  
1344 C CG  . ARG A 189 ? 0.4548 0.6473 0.3860 0.0330  -0.0114 0.0060  169 ARG A CG  
1345 C CD  . ARG A 189 ? 0.4367 0.6458 0.3777 0.0044  -0.0034 -0.0024 169 ARG A CD  
1346 N NE  . ARG A 189 ? 0.5126 0.6600 0.4041 -0.0121 -0.0079 -0.0054 169 ARG A NE  
1347 C CZ  . ARG A 189 ? 0.5261 0.5445 0.3113 -0.0807 0.0198  0.0494  169 ARG A CZ  
1348 N NH1 . ARG A 189 ? 0.5333 0.6518 0.3501 -0.1525 0.0707  0.0121  169 ARG A NH1 
1349 N NH2 . ARG A 189 ? 0.6167 0.5190 0.4062 -0.0701 0.0107  0.1177  169 ARG A NH2 
1350 N N   . PRO A 190 ? 0.5196 0.6642 0.3038 0.0552  -0.0037 -0.0030 170 PRO A N   
1351 C CA  . PRO A 190 ? 0.5121 0.6512 0.3109 0.0323  -0.0146 -0.0079 170 PRO A CA  
1352 C C   . PRO A 190 ? 0.4651 0.6421 0.2984 0.0182  -0.0066 0.0095  170 PRO A C   
1353 O O   . PRO A 190 ? 0.4332 0.6764 0.2804 -0.0128 -0.0215 0.0390  170 PRO A O   
1354 C CB  . PRO A 190 ? 0.4940 0.6398 0.3409 0.0109  -0.0009 -0.0032 170 PRO A CB  
1355 C CG  . PRO A 190 ? 0.4912 0.6245 0.3168 0.0274  0.0034  -0.0073 170 PRO A CG  
1356 C CD  . PRO A 190 ? 0.5228 0.6601 0.2743 0.0396  -0.0102 0.0320  170 PRO A CD  
1357 N N   . ARG A 191 ? 0.4819 0.6522 0.3564 0.0055  -0.0333 0.0098  171 ARG A N   
1358 C CA  . ARG A 191 ? 0.4687 0.6495 0.3448 -0.0112 -0.0715 0.0291  171 ARG A CA  
1359 C C   . ARG A 191 ? 0.4655 0.6970 0.3183 0.0005  -0.0822 0.0417  171 ARG A C   
1360 O O   . ARG A 191 ? 0.4569 0.6378 0.3329 0.0012  -0.0502 0.0477  171 ARG A O   
1361 C CB  . ARG A 191 ? 0.5369 0.6258 0.4097 -0.0061 -0.1011 -0.0071 171 ARG A CB  
1362 C CG  . ARG A 191 ? 1.0884 1.0884 1.0884 0.0000  0.0000  0.0000  171 ARG A CG  
1363 C CD  . ARG A 191 ? 1.3265 1.3265 1.3265 0.0000  0.0000  0.0000  171 ARG A CD  
1364 N NE  . ARG A 191 ? 1.5883 1.5883 1.5883 0.0000  0.0000  0.0000  171 ARG A NE  
1365 C CZ  . ARG A 191 ? 1.8218 1.8218 1.8218 0.0000  0.0000  0.0000  171 ARG A CZ  
1366 N NH1 . ARG A 191 ? 1.9703 1.9703 1.9703 0.0000  0.0000  0.0000  171 ARG A NH1 
1367 N NH2 . ARG A 191 ? 1.7829 1.7829 1.7829 0.0000  0.0000  0.0000  171 ARG A NH2 
1379 N N   . PHE A 193 ? 0.4400 0.7523 0.2698 -0.0978 -0.0325 0.0702  173 PHE A N   
1380 C CA  . PHE A 193 ? 0.4413 0.7622 0.2856 -0.0658 -0.0318 0.0760  173 PHE A CA  
1381 C C   . PHE A 193 ? 0.4461 0.7455 0.2761 -0.0695 -0.0306 0.0817  173 PHE A C   
1382 O O   . PHE A 193 ? 0.4540 0.7443 0.2879 -0.0760 -0.0525 0.0613  173 PHE A O   
1383 C CB  . PHE A 193 ? 0.4062 0.8332 0.2891 -0.0510 -0.0386 0.0628  173 PHE A CB  
1384 C CG  . PHE A 193 ? 0.4430 0.8549 0.2834 -0.0332 -0.0241 0.0169  173 PHE A CG  
1385 C CD1 . PHE A 193 ? 0.4473 0.9229 0.3365 -0.0231 -0.0397 0.0382  173 PHE A CD1 
1386 C CD2 . PHE A 193 ? 0.4713 0.8802 0.3673 -0.0231 -0.0181 -0.0130 173 PHE A CD2 
1387 C CE1 . PHE A 193 ? 0.4424 0.9154 0.3758 0.0074  -0.0397 0.0141  173 PHE A CE1 
1388 C CE2 . PHE A 193 ? 0.4266 0.8952 0.4429 -0.0259 -0.0401 -0.0003 173 PHE A CE2 
1389 C CZ  . PHE A 193 ? 0.4384 0.8757 0.3421 -0.0194 -0.0136 0.0153  173 PHE A CZ  
1390 N N   . THR A 194 ? 0.4316 0.7309 0.3442 -0.0815 -0.0107 0.0891  174 THR A N   
1391 C CA  . THR A 194 ? 0.4039 0.7044 0.3126 -0.0674 -0.0202 0.0984  174 THR A CA  
1392 C C   . THR A 194 ? 0.3894 0.6797 0.3595 -0.0588 -0.0150 0.1156  174 THR A C   
1393 O O   . THR A 194 ? 0.4117 0.6924 0.3209 -0.0818 -0.0413 0.1427  174 THR A O   
1394 C CB  . THR A 194 ? 0.4303 0.6692 0.3583 -0.0841 -0.0136 0.0708  174 THR A CB  
1395 O OG1 . THR A 194 ? 0.4004 0.6505 0.3873 -0.0845 -0.0481 0.0498  174 THR A OG1 
1396 C CG2 . THR A 194 ? 0.4882 0.7230 0.3582 -0.0615 0.0110  0.0713  174 THR A CG2 
1397 N N   . GLY A 195 ? 0.3960 0.6607 0.3460 -0.0439 -0.0123 0.1188  175 GLY A N   
1398 C CA  . GLY A 195 ? 0.4143 0.7062 0.3691 -0.0532 -0.0301 0.1512  175 GLY A CA  
1399 C C   . GLY A 195 ? 0.4208 0.7353 0.3410 -0.0472 -0.0216 0.1624  175 GLY A C   
1400 O O   . GLY A 195 ? 0.4020 0.6817 0.3896 -0.0288 -0.0051 0.1717  175 GLY A O   
1401 N N   . ASP A 196 ? 0.4023 0.8721 0.3898 -0.0584 -0.0652 0.1946  176 ASP A N   
1402 C CA  . ASP A 196 ? 0.4972 0.9207 0.3731 -0.0911 -0.0647 0.2171  176 ASP A CA  
1403 C C   . ASP A 196 ? 0.4964 0.9052 0.3702 -0.1167 -0.0654 0.2160  176 ASP A C   
1404 O O   . ASP A 196 ? 0.4706 0.9316 0.3603 -0.1072 -0.0613 0.2397  176 ASP A O   
1405 C CB  . ASP A 196 ? 0.5660 1.0190 0.3842 -0.0760 -0.0643 0.2337  176 ASP A CB  
1406 C CG  . ASP A 196 ? 0.6470 1.0483 0.4667 -0.0654 -0.0434 0.2131  176 ASP A CG  
1407 O OD1 . ASP A 196 ? 0.7674 0.9457 0.5630 -0.1248 -0.0384 0.1923  176 ASP A OD1 
1408 O OD2 . ASP A 196 ? 0.7685 1.1830 0.3867 -0.0483 -0.0616 0.2514  176 ASP A OD2 
1409 N N   . GLU A 197 ? 0.4415 0.8950 0.3612 -0.1498 -0.0928 0.1290  177 GLU A N   
1410 C CA  . GLU A 197 ? 0.4878 0.9111 0.3479 -0.1181 -0.0703 0.1269  177 GLU A CA  
1411 C C   . GLU A 197 ? 0.4541 0.8530 0.3420 -0.1118 -0.0483 0.1354  177 GLU A C   
1412 O O   . GLU A 197 ? 0.4298 0.9267 0.3096 -0.1113 -0.0324 0.0930  177 GLU A O   
1413 C CB  . GLU A 197 ? 0.5312 0.9745 0.3595 -0.1210 -0.0730 0.0817  177 GLU A CB  
1414 C CG  . GLU A 197 ? 0.5764 1.0459 0.3303 -0.0891 -0.0727 0.1042  177 GLU A CG  
1415 C CD  . GLU A 197 ? 0.6820 1.1210 0.4722 -0.0772 -0.0309 0.0205  177 GLU A CD  
1416 O OE1 . GLU A 197 ? 0.7169 1.1871 0.5330 -0.0560 0.0914  0.0335  177 GLU A OE1 
1417 O OE2 . GLU A 197 ? 0.7142 1.3219 0.4495 -0.0875 -0.1381 -0.0246 177 GLU A OE2 
1418 N N   . GLY A 198 ? 0.3954 0.7596 0.3232 -0.1074 -0.0267 0.0973  178 GLY A N   
1419 C CA  . GLY A 198 ? 0.4604 0.6942 0.3318 -0.0702 -0.0463 0.1354  178 GLY A CA  
1420 C C   . GLY A 198 ? 0.4199 0.6234 0.2918 -0.0505 -0.0286 0.1499  178 GLY A C   
1421 O O   . GLY A 198 ? 0.4402 0.6001 0.2822 -0.0379 -0.0178 0.1704  178 GLY A O   
1422 N N   . ALA A 199 ? 0.3822 0.6265 0.3084 -0.0384 -0.0157 0.1445  179 ALA A N   
1423 C CA  . ALA A 199 ? 0.3717 0.6190 0.3135 -0.0591 -0.0315 0.1328  179 ALA A CA  
1424 C C   . ALA A 199 ? 0.3823 0.6463 0.3247 -0.0523 -0.0367 0.1540  179 ALA A C   
1425 O O   . ALA A 199 ? 0.3836 0.6005 0.3342 -0.0636 -0.0303 0.2019  179 ALA A O   
1426 C CB  . ALA A 199 ? 0.3781 0.6441 0.3454 -0.0688 0.0026  0.1382  179 ALA A CB  
1427 N N   . ALA A 200 ? 0.3833 0.6875 0.3172 -0.0362 -0.0222 0.1648  180 ALA A N   
1428 C CA  . ALA A 200 ? 0.4198 0.7471 0.4043 -0.0473 -0.0010 0.1329  180 ALA A CA  
1429 C C   . ALA A 200 ? 0.3973 0.6917 0.3976 -0.0774 -0.0161 0.1554  180 ALA A C   
1430 O O   . ALA A 200 ? 0.4205 0.7481 0.3378 -0.1046 -0.0379 0.1856  180 ALA A O   
1431 C CB  . ALA A 200 ? 0.4737 0.7698 0.3622 -0.0410 -0.0056 0.1204  180 ALA A CB  
1432 N N   . ARG A 201 ? 0.3944 0.6511 0.3420 -0.0583 -0.0099 0.1229  181 ARG A N   
1433 C CA  . ARG A 201 ? 0.3645 0.6002 0.3726 -0.0634 -0.0279 0.1030  181 ARG A CA  
1434 C C   . ARG A 201 ? 0.3733 0.5200 0.3151 -0.0344 -0.0073 0.1240  181 ARG A C   
1435 O O   . ARG A 201 ? 0.3773 0.5270 0.3364 -0.0242 -0.0098 0.1300  181 ARG A O   
1436 C CB  . ARG A 201 ? 0.4105 0.6292 0.4014 -0.0783 -0.0092 0.0683  181 ARG A CB  
1437 C CG  . ARG A 201 ? 0.4152 0.6512 0.4428 -0.0702 -0.0265 0.0253  181 ARG A CG  
1438 C CD  . ARG A 201 ? 0.4213 0.7048 0.4861 -0.0562 -0.0273 -0.0250 181 ARG A CD  
1439 N NE  . ARG A 201 ? 0.5097 0.7426 0.5605 -0.0610 0.0309  -0.1081 181 ARG A NE  
1440 C CZ  . ARG A 201 ? 0.5318 0.8185 0.6219 -0.1071 0.0543  -0.1997 181 ARG A CZ  
1441 N NH1 . ARG A 201 ? 0.5494 0.9038 0.7159 -0.1688 0.0661  -0.2360 181 ARG A NH1 
1442 N NH2 . ARG A 201 ? 0.6266 0.8128 0.6835 -0.1489 0.0956  -0.2067 181 ARG A NH2 
1443 N N   . LEU A 202 ? 0.3557 0.5334 0.3506 -0.0367 -0.0336 0.1341  182 LEU A N   
1444 C CA  . LEU A 202 ? 0.3804 0.4300 0.3516 -0.0397 0.0001  0.1611  182 LEU A CA  
1445 C C   . LEU A 202 ? 0.4072 0.4374 0.3845 -0.0158 -0.0082 0.1916  182 LEU A C   
1446 O O   . LEU A 202 ? 0.3994 0.4057 0.3706 0.0108  -0.0162 0.2177  182 LEU A O   
1447 C CB  . LEU A 202 ? 0.3498 0.4051 0.3592 -0.0387 -0.0067 0.1529  182 LEU A CB  
1448 C CG  . LEU A 202 ? 0.3742 0.3950 0.3870 -0.0394 0.0217  0.1688  182 LEU A CG  
1449 C CD1 . LEU A 202 ? 0.3741 0.3931 0.3408 -0.0456 0.0346  0.1535  182 LEU A CD1 
1450 C CD2 . LEU A 202 ? 0.4084 0.3599 0.3781 -0.0120 0.0432  0.2097  182 LEU A CD2 
1451 N N   . ALA A 203 ? 0.3634 0.5260 0.3546 -0.0085 -0.0064 0.1690  183 ALA A N   
1452 C CA  . ALA A 203 ? 0.4026 0.5187 0.3761 -0.0245 -0.0305 0.1798  183 ALA A CA  
1453 C C   . ALA A 203 ? 0.3610 0.4666 0.3377 -0.0211 -0.0488 0.1883  183 ALA A C   
1454 O O   . ALA A 203 ? 0.3604 0.4339 0.4542 -0.0194 -0.0119 0.2294  183 ALA A O   
1455 C CB  . ALA A 203 ? 0.3745 0.4998 0.4128 -0.0099 -0.0174 0.1817  183 ALA A CB  
1456 N N   . GLU A 204 ? 0.4006 0.5379 0.3851 -0.0331 -0.0343 0.1915  184 GLU A N   
1457 C CA  . GLU A 204 ? 0.4399 0.5755 0.3898 -0.0492 -0.0010 0.1611  184 GLU A CA  
1458 C C   . GLU A 204 ? 0.4153 0.4893 0.3812 -0.0678 -0.0054 0.1793  184 GLU A C   
1459 O O   . GLU A 204 ? 0.4061 0.5433 0.3848 -0.0565 -0.0249 0.1991  184 GLU A O   
1460 C CB  . GLU A 204 ? 0.4963 0.6640 0.4431 -0.0961 0.0148  0.1026  184 GLU A CB  
1461 C CG  . GLU A 204 ? 0.5586 0.7275 0.5230 -0.0881 0.0237  0.0448  184 GLU A CG  
1462 C CD  . GLU A 204 ? 0.6400 0.7938 0.6004 -0.1340 -0.0095 -0.0288 184 GLU A CD  
1463 O OE1 . GLU A 204 ? 0.5794 0.7887 0.6263 -0.1445 -0.0054 -0.0224 184 GLU A OE1 
1464 O OE2 . GLU A 204 ? 0.7591 0.8629 0.7754 -0.1884 0.0405  -0.0685 184 GLU A OE2 
1465 N N   . GLN A 205 ? 0.3673 0.4398 0.3586 -0.0595 -0.0079 0.1627  185 GLN A N   
1466 C CA  . GLN A 205 ? 0.3792 0.3676 0.3429 -0.0389 -0.0026 0.1223  185 GLN A CA  
1467 C C   . GLN A 205 ? 0.3537 0.3406 0.3074 0.0002  0.0062  0.1407  185 GLN A C   
1468 O O   . GLN A 205 ? 0.3696 0.3473 0.3932 0.0072  0.0044  0.1151  185 GLN A O   
1469 C CB  . GLN A 205 ? 0.4031 0.3635 0.3527 -0.0253 0.0189  0.1043  185 GLN A CB  
1470 C CG  . GLN A 205 ? 0.4195 0.3318 0.3582 -0.0050 0.0122  0.0826  185 GLN A CG  
1471 C CD  . GLN A 205 ? 0.3747 0.3212 0.3326 -0.0027 0.0232  0.0598  185 GLN A CD  
1472 O OE1 . GLN A 205 ? 0.3781 0.3747 0.3379 -0.0166 0.0173  0.1044  185 GLN A OE1 
1473 N NE2 . GLN A 205 ? 0.4035 0.2970 0.3332 -0.0232 0.0088  0.0822  185 GLN A NE2 
1474 N N   . THR A 206 ? 0.3531 0.3810 0.3678 -0.0001 0.0112  0.1458  186 THR A N   
1475 C CA  . THR A 206 ? 0.3704 0.3793 0.3740 -0.0049 0.0137  0.1434  186 THR A CA  
1476 C C   . THR A 206 ? 0.3493 0.4134 0.3984 -0.0081 0.0106  0.1425  186 THR A C   
1477 O O   . THR A 206 ? 0.3903 0.2045 0.4279 -0.0007 0.0316  0.1529  186 THR A O   
1478 C CB  . THR A 206 ? 0.3715 0.4264 0.4087 -0.0238 0.0661  0.1184  186 THR A CB  
1479 O OG1 . THR A 206 ? 0.3955 0.3933 0.4601 -0.0067 0.0682  0.1635  186 THR A OG1 
1480 C CG2 . THR A 206 ? 0.4221 0.3731 0.4523 0.0050  0.0519  0.0991  186 THR A CG2 
1481 N N   . ALA A 207 ? 0.3158 0.4794 0.3976 0.0004  0.0319  0.1688  187 ALA A N   
1482 C CA  . ALA A 207 ? 0.3693 0.4767 0.3982 0.0000  0.0343  0.1784  187 ALA A CA  
1483 C C   . ALA A 207 ? 0.3595 0.4304 0.4379 -0.0271 -0.0090 0.1571  187 ALA A C   
1484 O O   . ALA A 207 ? 0.4146 0.3447 0.4311 -0.0004 -0.0300 0.1864  187 ALA A O   
1485 C CB  . ALA A 207 ? 0.3875 0.5283 0.4023 0.0215  0.0271  0.1873  187 ALA A CB  
1486 N N   . GLN A 208 ? 0.3581 0.3978 0.3456 -0.0195 0.0191  0.0997  188 GLN A N   
1487 C CA  . GLN A 208 ? 0.3831 0.3801 0.3519 -0.0116 0.0153  0.0840  188 GLN A CA  
1488 C C   . GLN A 208 ? 0.3391 0.2759 0.3561 0.0084  0.0184  0.0876  188 GLN A C   
1489 O O   . GLN A 208 ? 0.3714 0.2573 0.3542 -0.0101 -0.0009 0.0929  188 GLN A O   
1490 C CB  . GLN A 208 ? 0.4323 0.3696 0.3212 -0.0439 0.0184  0.0970  188 GLN A CB  
1491 C CG  . GLN A 208 ? 0.4807 0.4567 0.3642 -0.0314 0.0220  0.0640  188 GLN A CG  
1492 C CD  . GLN A 208 ? 0.5756 0.4985 0.3526 -0.0472 0.0156  0.0335  188 GLN A CD  
1493 O OE1 . GLN A 208 ? 0.5821 0.5503 0.3335 0.0029  0.0172  0.0276  188 GLN A OE1 
1494 N NE2 . GLN A 208 ? 0.6649 0.5968 0.3810 -0.0813 -0.0123 -0.0107 188 GLN A NE2 
1495 N N   . ASP A 209 ? 0.3185 0.2676 0.3637 0.0285  0.0167  0.0846  189 ASP A N   
1496 C CA  . ASP A 209 ? 0.3598 0.2576 0.3726 -0.0038 0.0074  0.0901  189 ASP A CA  
1497 C C   . ASP A 209 ? 0.3811 0.2392 0.3885 0.0160  0.0097  0.1015  189 ASP A C   
1498 O O   . ASP A 209 ? 0.4029 0.2139 0.3978 -0.0081 0.0255  0.1049  189 ASP A O   
1499 C CB  . ASP A 209 ? 0.3903 0.2721 0.3556 0.0000  -0.0086 0.0988  189 ASP A CB  
1500 C CG  . ASP A 209 ? 0.4366 0.3100 0.3914 -0.0191 -0.0071 0.0939  189 ASP A CG  
1501 O OD1 . ASP A 209 ? 0.4453 0.3990 0.4046 -0.0143 -0.0210 0.0802  189 ASP A OD1 
1502 O OD2 . ASP A 209 ? 0.4869 0.3284 0.3978 -0.0407 -0.0291 0.1103  189 ASP A OD2 
1503 N N   . GLU A 210 ? 0.3595 0.2808 0.3879 -0.0026 0.0326  0.1443  190 GLU A N   
1504 C CA  . GLU A 210 ? 0.3816 0.2516 0.4283 0.0354  0.0408  0.1264  190 GLU A CA  
1505 C C   . GLU A 210 ? 0.3827 0.2385 0.3843 0.0083  0.0254  0.1168  190 GLU A C   
1506 O O   . GLU A 210 ? 0.4292 0.1655 0.4336 -0.0081 0.0456  0.0963  190 GLU A O   
1507 C CB  . GLU A 210 ? 0.4114 0.2787 0.4816 0.0803  0.0726  0.1663  190 GLU A CB  
1508 C CG  . GLU A 210 ? 0.4402 0.3418 0.5255 0.1049  0.0911  0.1537  190 GLU A CG  
1509 C CD  . GLU A 210 ? 0.4543 0.4526 0.5385 0.1322  0.1011  0.1673  190 GLU A CD  
1510 O OE1 . GLU A 210 ? 0.5035 0.4233 0.6130 0.1188  0.1700  0.1559  190 GLU A OE1 
1511 O OE2 . GLU A 210 ? 0.4981 0.5934 0.4630 0.1750  0.0597  0.1292  190 GLU A OE2 
1512 N N   . ALA A 211 ? 0.3713 0.2033 0.3690 0.0042  0.0179  0.1352  191 ALA A N   
1513 C CA  . ALA A 211 ? 0.3851 0.2172 0.3223 0.0191  0.0126  0.1064  191 ALA A CA  
1514 C C   . ALA A 211 ? 0.3488 0.2006 0.3285 0.0072  0.0109  0.0896  191 ALA A C   
1515 O O   . ALA A 211 ? 0.4009 0.1593 0.3170 0.0067  0.0028  0.0690  191 ALA A O   
1516 C CB  . ALA A 211 ? 0.3535 0.2622 0.3313 0.0114  -0.0207 0.1154  191 ALA A CB  
1517 N N   . LEU A 212 ? 0.3332 0.2232 0.3364 -0.0339 0.0117  0.1033  192 LEU A N   
1518 C CA  . LEU A 212 ? 0.3457 0.2178 0.3197 -0.0259 0.0007  0.0922  192 LEU A CA  
1519 C C   . LEU A 212 ? 0.3534 0.2234 0.3226 0.0174  0.0139  0.0847  192 LEU A C   
1520 O O   . LEU A 212 ? 0.3654 0.2098 0.3418 -0.0287 0.0268  0.0953  192 LEU A O   
1521 C CB  . LEU A 212 ? 0.3608 0.2108 0.3624 0.0020  -0.0160 0.1073  192 LEU A CB  
1522 C CG  . LEU A 212 ? 0.3662 0.2693 0.3649 -0.0417 -0.0158 0.0673  192 LEU A CG  
1523 C CD1 . LEU A 212 ? 0.3935 0.2279 0.4414 -0.0329 -0.0157 0.0763  192 LEU A CD1 
1524 C CD2 . LEU A 212 ? 0.3787 0.2100 0.3826 -0.0478 -0.0165 0.0752  192 LEU A CD2 
1525 N N   . VAL A 213 ? 0.3549 0.3041 0.3337 0.0176  0.0228  0.0487  193 VAL A N   
1526 C CA  . VAL A 213 ? 0.4069 0.2831 0.3298 -0.0084 0.0396  0.0531  193 VAL A CA  
1527 C C   . VAL A 213 ? 0.4148 0.2658 0.3415 -0.0039 0.0418  0.0420  193 VAL A C   
1528 O O   . VAL A 213 ? 0.4585 0.2152 0.3310 0.0195  0.0078  0.0127  193 VAL A O   
1529 C CB  . VAL A 213 ? 0.4332 0.2996 0.3443 -0.0014 0.0430  0.0470  193 VAL A CB  
1530 C CG1 . VAL A 213 ? 0.4708 0.3281 0.3824 -0.0041 0.0540  0.0056  193 VAL A CG1 
1531 C CG2 . VAL A 213 ? 0.3841 0.3413 0.3103 -0.0526 0.0543  0.0524  193 VAL A CG2 
1532 N N   . GLY A 214 ? 0.4100 0.2551 0.3738 0.0124  0.0434  0.0282  194 GLY A N   
1533 C CA  . GLY A 214 ? 0.4283 0.2227 0.3841 0.0053  0.0379  0.0471  194 GLY A CA  
1534 C C   . GLY A 214 ? 0.3990 0.1418 0.3349 -0.0107 0.0404  0.0234  194 GLY A C   
1535 O O   . GLY A 214 ? 0.4473 0.1628 0.3500 -0.0183 0.0576  0.0305  194 GLY A O   
1536 N N   . ARG A 215 ? 0.3871 0.0989 0.3070 -0.0295 0.0154  0.0593  195 ARG A N   
1537 C CA  . ARG A 215 ? 0.3841 0.1558 0.2994 -0.0331 0.0120  0.0588  195 ARG A CA  
1538 C C   . ARG A 215 ? 0.3863 0.2052 0.3191 -0.0096 0.0115  0.0700  195 ARG A C   
1539 O O   . ARG A 215 ? 0.4321 0.2239 0.3023 -0.0308 0.0095  0.0774  195 ARG A O   
1540 C CB  . ARG A 215 ? 0.3896 0.1567 0.3206 -0.0234 -0.0019 0.0472  195 ARG A CB  
1541 C CG  . ARG A 215 ? 0.3967 0.1617 0.3417 0.0050  -0.0219 0.0276  195 ARG A CG  
1542 C CD  . ARG A 215 ? 0.4112 0.2051 0.3533 0.0005  -0.0398 0.0061  195 ARG A CD  
1543 N NE  . ARG A 215 ? 0.4077 0.1836 0.3551 0.0168  -0.0238 0.0321  195 ARG A NE  
1544 C CZ  . ARG A 215 ? 0.4015 0.2850 0.3564 0.0182  -0.0134 0.0177  195 ARG A CZ  
1545 N NH1 . ARG A 215 ? 0.4225 0.2391 0.3762 0.0244  -0.0248 0.0273  195 ARG A NH1 
1546 N NH2 . ARG A 215 ? 0.4344 0.3415 0.3638 0.0184  -0.0013 0.0228  195 ARG A NH2 
1547 N N   . HIS A 216 ? 0.4134 0.2224 0.3194 -0.0417 0.0156  0.0845  196 HIS A N   
1548 C CA  . HIS A 216 ? 0.4001 0.2042 0.3375 -0.0362 0.0230  0.0936  196 HIS A CA  
1549 C C   . HIS A 216 ? 0.4158 0.2365 0.3197 -0.0505 0.0213  0.0817  196 HIS A C   
1550 O O   . HIS A 216 ? 0.4703 0.3068 0.3145 -0.0280 0.0021  0.0868  196 HIS A O   
1551 C CB  . HIS A 216 ? 0.4259 0.1822 0.3286 -0.0215 0.0333  0.0947  196 HIS A CB  
1552 C CG  . HIS A 216 ? 0.4281 0.2102 0.2979 0.0079  0.0038  0.0799  196 HIS A CG  
1553 N ND1 . HIS A 216 ? 0.4130 0.1957 0.3225 0.0462  -0.0001 0.0632  196 HIS A ND1 
1554 C CD2 . HIS A 216 ? 0.4295 0.1804 0.3657 0.0202  0.0068  0.0638  196 HIS A CD2 
1555 C CE1 . HIS A 216 ? 0.4021 0.2426 0.3648 0.0343  0.0127  0.0423  196 HIS A CE1 
1556 N NE2 . HIS A 216 ? 0.4549 0.2138 0.3818 0.0149  0.0010  0.0409  196 HIS A NE2 
1557 N N   . ARG A 217 ? 0.4193 0.2357 0.2866 -0.0270 0.0184  0.0719  197 ARG A N   
1558 C CA  . ARG A 217 ? 0.5031 0.2444 0.2978 -0.0272 0.0052  0.0582  197 ARG A CA  
1559 C C   . ARG A 217 ? 0.4988 0.2442 0.2978 -0.0371 0.0026  0.0531  197 ARG A C   
1560 O O   . ARG A 217 ? 0.5465 0.1725 0.3299 -0.0097 0.0042  0.0401  197 ARG A O   
1561 C CB  . ARG A 217 ? 0.4991 0.3158 0.2822 -0.0472 0.0134  0.0472  197 ARG A CB  
1562 C CG  . ARG A 217 ? 0.5074 0.2710 0.3323 -0.0391 -0.0030 0.0654  197 ARG A CG  
1563 C CD  . ARG A 217 ? 0.4412 0.2016 0.3340 -0.0249 -0.0041 0.0437  197 ARG A CD  
1564 N NE  . ARG A 217 ? 0.4549 0.2210 0.3450 -0.0314 0.0067  0.0375  197 ARG A NE  
1565 C CZ  . ARG A 217 ? 0.4061 0.2205 0.3383 0.0103  -0.0021 0.0546  197 ARG A CZ  
1566 N NH1 . ARG A 217 ? 0.4495 0.1971 0.3343 0.0461  -0.0389 0.0701  197 ARG A NH1 
1567 N NH2 . ARG A 217 ? 0.4328 0.2320 0.3650 0.0035  0.0098  0.0662  197 ARG A NH2 
1568 N N   . PRO A 218 ? 0.4741 0.1997 0.3064 -0.0154 0.0047  0.0778  198 PRO A N   
1569 C CA  . PRO A 218 ? 0.4509 0.2375 0.3023 -0.0025 0.0259  0.0747  198 PRO A CA  
1570 C C   . PRO A 218 ? 0.4053 0.2392 0.3237 0.0089  -0.0030 0.0614  198 PRO A C   
1571 O O   . PRO A 218 ? 0.4269 0.1978 0.3432 0.0291  -0.0011 0.0440  198 PRO A O   
1572 C CB  . PRO A 218 ? 0.4711 0.2181 0.2989 -0.0153 0.0186  0.0856  198 PRO A CB  
1573 C CG  . PRO A 218 ? 0.4600 0.2452 0.3126 -0.0129 0.0172  0.0886  198 PRO A CG  
1574 C CD  . PRO A 218 ? 0.4707 0.2040 0.3209 0.0043  0.0069  0.0981  198 PRO A CD  
1575 N N   . GLY A 219 ? 0.4047 0.2069 0.3363 -0.0085 0.0010  0.0601  199 GLY A N   
1576 C CA  . GLY A 219 ? 0.3949 0.1785 0.3509 0.0202  0.0103  0.0653  199 GLY A CA  
1577 C C   . GLY A 219 ? 0.4090 0.1314 0.3423 -0.0146 0.0152  0.0574  199 GLY A C   
1578 O O   . GLY A 219 ? 0.4465 0.0998 0.3436 0.0110  0.0274  0.0475  199 GLY A O   
1579 N N   . ARG A 220 ? 0.4227 0.1071 0.3409 -0.0135 0.0142  0.0674  200 ARG A N   
1580 C CA  . ARG A 220 ? 0.4286 0.1497 0.3458 -0.0318 0.0222  0.0533  200 ARG A CA  
1581 C C   . ARG A 220 ? 0.4189 0.1936 0.3392 -0.0279 0.0320  0.0610  200 ARG A C   
1582 O O   . ARG A 220 ? 0.4423 0.1889 0.3470 -0.0169 0.0290  0.0424  200 ARG A O   
1583 C CB  . ARG A 220 ? 0.4455 0.2116 0.4080 -0.0150 0.0224  0.0518  200 ARG A CB  
1584 C CG  . ARG A 220 ? 0.4440 0.2389 0.4326 -0.0151 0.0262  0.0466  200 ARG A CG  
1585 C CD  . ARG A 220 ? 0.4663 0.2573 0.4739 -0.0141 0.0158  0.0548  200 ARG A CD  
1586 N NE  . ARG A 220 ? 0.4736 0.2695 0.5116 0.0248  0.0167  0.0175  200 ARG A NE  
1587 C CZ  . ARG A 220 ? 0.5050 0.3042 0.4568 0.0153  -0.0091 -0.0033 200 ARG A CZ  
1588 N NH1 . ARG A 220 ? 0.4858 0.2702 0.4613 0.0278  -0.0075 0.0430  200 ARG A NH1 
1589 N NH2 . ARG A 220 ? 0.5714 0.2184 0.4360 0.0571  -0.0323 -0.0202 200 ARG A NH2 
1590 N N   . ILE A 221 ? 0.4542 0.1471 0.3028 -0.0017 0.0108  0.0672  201 ILE A N   
1591 C CA  . ILE A 221 ? 0.4425 0.1724 0.3050 0.0297  0.0149  0.0528  201 ILE A CA  
1592 C C   . ILE A 221 ? 0.4217 0.1766 0.3489 0.0352  0.0124  0.0586  201 ILE A C   
1593 O O   . ILE A 221 ? 0.4468 0.1207 0.3936 0.0265  -0.0054 0.0312  201 ILE A O   
1594 C CB  . ILE A 221 ? 0.4481 0.1976 0.3245 0.0264  0.0279  0.0606  201 ILE A CB  
1595 C CG1 . ILE A 221 ? 0.4508 0.1676 0.3391 0.0071  0.0294  0.0502  201 ILE A CG1 
1596 C CG2 . ILE A 221 ? 0.4762 0.2307 0.3247 0.0344  0.0334  0.0791  201 ILE A CG2 
1597 C CD1 . ILE A 221 ? 0.4741 0.1943 0.3582 -0.0080 0.0253  0.0767  201 ILE A CD1 
1598 N N   . GLU A 222 ? 0.4233 0.1653 0.3647 0.0565  0.0319  0.0277  202 GLU A N   
1599 C CA  . GLU A 222 ? 0.4771 0.1709 0.3854 0.0456  0.0573  0.0301  202 GLU A CA  
1600 C C   . GLU A 222 ? 0.4678 0.1768 0.3857 -0.0107 0.0173  0.0293  202 GLU A C   
1601 O O   . GLU A 222 ? 0.4761 0.1981 0.3890 -0.0033 -0.0043 0.0504  202 GLU A O   
1602 C CB  . GLU A 222 ? 0.5569 0.1632 0.4304 0.0428  0.0424  0.0376  202 GLU A CB  
1603 C CG  . GLU A 222 ? 0.5727 0.1969 0.4397 0.0647  0.0705  0.0308  202 GLU A CG  
1604 C CD  . GLU A 222 ? 0.5902 0.2069 0.4802 0.1018  0.0628  0.0293  202 GLU A CD  
1605 O OE1 . GLU A 222 ? 0.6207 0.3153 0.5674 0.1624  0.0490  0.0012  202 GLU A OE1 
1606 O OE2 . GLU A 222 ? 0.6105 0.2958 0.5196 0.1065  0.0148  0.0230  202 GLU A OE2 
1607 N N   . PRO A 223 ? 0.5111 0.1634 0.4114 0.0282  0.0403  0.0775  203 PRO A N   
1608 C CA  . PRO A 223 ? 0.5339 0.1504 0.4289 0.0139  0.0386  0.0688  203 PRO A CA  
1609 C C   . PRO A 223 ? 0.5215 0.0613 0.4101 0.0123  0.0490  0.0969  203 PRO A C   
1610 O O   . PRO A 223 ? 0.6038 0.0817 0.4566 -0.0035 0.0489  0.1313  203 PRO A O   
1611 C CB  . PRO A 223 ? 0.5531 0.1957 0.4376 0.0373  0.0367  0.0479  203 PRO A CB  
1612 C CG  . PRO A 223 ? 0.5909 0.2877 0.4576 0.0619  0.0407  0.0435  203 PRO A CG  
1613 C CD  . PRO A 223 ? 0.5625 0.2921 0.4255 0.0601  0.0412  0.0416  203 PRO A CD  
1614 N N   . SER A 224 ? 0.5134 0.0940 0.4402 0.0082  0.0304  0.0536  204 SER A N   
1615 C CA  . SER A 224 ? 0.5170 0.1060 0.4633 -0.0130 0.0463  -0.0142 204 SER A CA  
1616 C C   . SER A 224 ? 0.5186 0.0867 0.5169 0.0169  0.0350  0.0027  204 SER A C   
1617 O O   . SER A 224 ? 0.5765 0.1545 0.5811 -0.0365 -0.0127 0.0173  204 SER A O   
1618 C CB  . SER A 224 ? 0.4898 0.1155 0.4750 -0.0084 0.0485  -0.0250 204 SER A CB  
1619 O OG  . SER A 224 ? 0.4943 0.1763 0.4618 -0.0082 0.0545  -0.0123 204 SER A OG  
1620 N N   . ASN A 225 ? 0.4950 0.1256 0.5095 -0.0011 0.0149  -0.0373 205 ASN A N   
1621 C CA  . ASN A 225 ? 0.5235 0.1301 0.5274 -0.0573 0.0306  -0.0653 205 ASN A CA  
1622 C C   . ASN A 225 ? 0.5333 0.1311 0.5284 -0.0652 0.0050  -0.0531 205 ASN A C   
1623 O O   . ASN A 225 ? 0.5450 0.0691 0.5277 -0.0229 0.0255  -0.0220 205 ASN A O   
1624 C CB  . ASN A 225 ? 0.5500 0.1778 0.5571 -0.0820 0.0149  -0.0479 205 ASN A CB  
1625 C CG  . ASN A 225 ? 0.5774 0.1502 0.5857 -0.1368 0.0113  -0.0354 205 ASN A CG  
1626 O OD1 . ASN A 225 ? 0.6220 0.1364 0.6785 -0.1317 0.0121  -0.0894 205 ASN A OD1 
1627 N ND2 . ASN A 225 ? 0.6043 0.2323 0.6242 -0.1041 -0.0261 -0.0470 205 ASN A ND2 
1628 N N   . PRO A 226 ? 0.5534 0.1602 0.6429 -0.0629 -0.0180 -0.0044 206 PRO A N   
1629 C CA  . PRO A 226 ? 0.5839 0.1825 0.6753 -0.0723 -0.0076 0.0053  206 PRO A CA  
1630 C C   . PRO A 226 ? 0.5928 0.1351 0.6572 -0.0560 0.0210  -0.0180 206 PRO A C   
1631 O O   . PRO A 226 ? 0.6823 0.2305 0.6190 -0.0777 0.0651  -0.0226 206 PRO A O   
1632 C CB  . PRO A 226 ? 0.5914 0.2003 0.7292 -0.0369 -0.0192 -0.0104 206 PRO A CB  
1633 C CG  . PRO A 226 ? 0.5879 0.1465 0.7276 -0.0305 -0.0380 0.0007  206 PRO A CG  
1634 C CD  . PRO A 226 ? 0.5774 0.1534 0.7042 -0.0379 -0.0150 -0.0224 206 PRO A CD  
1635 N N   . VAL A 227 ? 0.5351 0.1284 0.6610 0.0039  0.0120  -0.0404 207 VAL A N   
1636 C CA  . VAL A 227 ? 0.5079 0.0750 0.6766 0.0734  0.0495  -0.0492 207 VAL A CA  
1637 C C   . VAL A 227 ? 0.5208 0.1575 0.6377 0.0271  0.0158  -0.0176 207 VAL A C   
1638 O O   . VAL A 227 ? 0.5415 0.1508 0.6403 0.0000  0.0019  0.0102  207 VAL A O   
1639 C CB  . VAL A 227 ? 0.4928 0.0715 0.7268 0.0300  0.0578  0.0085  207 VAL A CB  
1640 C CG1 . VAL A 227 ? 0.5655 0.1384 0.7179 0.0766  0.0443  0.0416  207 VAL A CG1 
1641 C CG2 . VAL A 227 ? 0.5341 0.2001 0.7199 0.0564  0.0371  0.0010  207 VAL A CG2 
1642 N N   . PRO A 228 ? 0.5332 0.1726 0.6422 0.0281  0.0102  0.0136  208 PRO A N   
1643 C CA  . PRO A 228 ? 0.5273 0.0881 0.6548 0.0460  0.0148  0.0167  208 PRO A CA  
1644 C C   . PRO A 228 ? 0.4782 0.1453 0.6933 -0.0098 0.0133  0.0401  208 PRO A C   
1645 O O   . PRO A 228 ? 0.4556 0.2067 0.6795 0.0239  0.0783  0.0892  208 PRO A O   
1646 C CB  . PRO A 228 ? 0.5605 0.2485 0.6886 0.1162  0.0270  -0.0054 208 PRO A CB  
1647 C CG  . PRO A 228 ? 0.5689 0.2663 0.6756 0.1136  0.0133  0.0150  208 PRO A CG  
1648 C CD  . PRO A 228 ? 0.5671 0.2048 0.6073 0.0521  0.0480  0.0047  208 PRO A CD  
1649 N N   . LEU A 229 ? 0.5206 0.0505 0.6733 0.0135  0.0183  0.0013  209 LEU A N   
1650 C CA  . LEU A 229 ? 0.5063 0.0371 0.6618 0.0079  0.0361  0.0420  209 LEU A CA  
1651 C C   . LEU A 229 ? 0.5214 0.0448 0.6436 0.0720  0.0353  0.0338  209 LEU A C   
1652 O O   . LEU A 229 ? 0.5502 0.0338 0.6870 0.0724  0.0586  0.0041  209 LEU A O   
1653 C CB  . LEU A 229 ? 0.5343 0.0790 0.6712 0.0405  0.0454  0.0610  209 LEU A CB  
1654 C CG  . LEU A 229 ? 0.5314 0.2261 0.7001 0.0151  0.0791  0.0735  209 LEU A CG  
1655 C CD1 . LEU A 229 ? 0.5202 0.2072 0.7017 0.0646  0.0687  0.0430  209 LEU A CD1 
1656 C CD2 . LEU A 229 ? 0.4576 0.2035 0.7351 0.0379  0.0710  0.0985  209 LEU A CD2 
1657 N N   . GLU A 230 ? 0.4844 0.1786 0.5894 0.0083  0.0195  -0.0255 210 GLU A N   
1658 C CA  . GLU A 230 ? 0.5133 0.1799 0.5871 0.0353  0.0162  0.0004  210 GLU A CA  
1659 C C   . GLU A 230 ? 0.5476 0.2220 0.5910 0.0117  0.0358  0.0304  210 GLU A C   
1660 O O   . GLU A 230 ? 0.6124 0.2052 0.5283 0.0000  0.0628  0.0092  210 GLU A O   
1661 C CB  . GLU A 230 ? 0.5633 0.2347 0.5946 0.0628  0.0089  -0.0092 210 GLU A CB  
1662 C CG  . GLU A 230 ? 0.5851 0.3011 0.6664 0.0282  -0.0271 -0.0477 210 GLU A CG  
1663 C CD  . GLU A 230 ? 0.6376 0.3332 0.7473 -0.0016 -0.0548 -0.0236 210 GLU A CD  
1664 O OE1 . GLU A 230 ? 0.7323 0.3535 0.7798 0.0358  -0.0994 -0.0089 210 GLU A OE1 
1665 O OE2 . GLU A 230 ? 0.6224 0.1713 0.8152 0.0528  -0.0557 -0.1099 210 GLU A OE2 
1666 N N   . ALA A 231 ? 0.5439 0.1641 0.6838 0.0069  -0.0173 0.0768  211 ALA A N   
1667 C CA  . ALA A 231 ? 0.6023 0.1699 0.7114 0.0248  -0.0204 0.0762  211 ALA A CA  
1668 C C   . ALA A 231 ? 0.5130 0.1509 0.6926 0.0370  -0.0292 0.0786  211 ALA A C   
1669 O O   . ALA A 231 ? 0.5797 0.1463 0.7460 0.0576  -0.0685 -0.0329 211 ALA A O   
1670 C CB  . ALA A 231 ? 0.6250 0.1528 0.7742 0.0207  -0.0348 0.0858  211 ALA A CB  
1671 N N   . ARG A 232 ? 0.4796 0.1908 0.6108 0.0265  -0.0223 0.1242  212 ARG A N   
1672 C CA  . ARG A 232 ? 0.4569 0.1432 0.6551 -0.0123 0.0042  0.1280  212 ARG A CA  
1673 C C   . ARG A 232 ? 0.4658 0.2117 0.5926 -0.0105 0.0080  0.1326  212 ARG A C   
1674 O O   . ARG A 232 ? 0.5176 0.2731 0.6591 -0.0275 -0.0158 0.1668  212 ARG A O   
1675 C CB  . ARG A 232 ? 0.4703 0.1299 0.6650 0.0003  0.0017  0.1430  212 ARG A CB  
1676 C CG  . ARG A 232 ? 0.5651 0.0756 0.7204 0.0620  0.0394  0.1279  212 ARG A CG  
1677 C CD  . ARG A 232 ? 0.5875 0.1256 0.7557 0.0646  0.0372  0.1105  212 ARG A CD  
1678 N NE  . ARG A 232 ? 0.6124 0.2235 0.7431 0.0432  0.0390  0.1336  212 ARG A NE  
1679 C CZ  . ARG A 232 ? 0.6513 0.2294 0.7567 0.0570  0.0294  0.1798  212 ARG A CZ  
1680 N NH1 . ARG A 232 ? 0.6847 0.3536 0.7135 0.0705  0.0786  0.1004  212 ARG A NH1 
1681 N NH2 . ARG A 232 ? 0.6355 0.1141 0.8474 0.1159  -0.0113 0.0212  212 ARG A NH2 
1682 N N   . ARG A 233 ? 0.4285 0.0207 0.4881 0.0082  0.0429  0.0626  213 ARG A N   
1683 C CA  . ARG A 233 ? 0.4284 0.0836 0.4075 0.0117  0.0181  0.0625  213 ARG A CA  
1684 C C   . ARG A 233 ? 0.4233 0.0709 0.3643 0.0056  0.0153  0.0374  213 ARG A C   
1685 O O   . ARG A 233 ? 0.4529 0.0711 0.3752 0.0298  0.0097  0.0156  213 ARG A O   
1686 C CB  . ARG A 233 ? 0.4721 0.0901 0.4129 0.0054  0.0377  -0.0061 213 ARG A CB  
1687 C CG  . ARG A 233 ? 0.4957 0.1550 0.4063 0.0426  0.0051  0.0012  213 ARG A CG  
1688 C CD  . ARG A 233 ? 0.5367 0.1746 0.4301 0.0292  0.0071  -0.0240 213 ARG A CD  
1689 N NE  . ARG A 233 ? 0.5279 0.2122 0.4144 0.0189  0.0040  0.0081  213 ARG A NE  
1690 C CZ  . ARG A 233 ? 0.5345 0.1768 0.4037 0.0071  0.0062  -0.0413 213 ARG A CZ  
1691 N NH1 . ARG A 233 ? 0.5475 0.1283 0.4761 -0.0245 0.0402  -0.0322 213 ARG A NH1 
1692 N NH2 . ARG A 233 ? 0.5467 0.1565 0.4216 -0.0320 -0.0018 -0.0319 213 ARG A NH2 
1693 N N   . THR A 234 ? 0.3949 0.0679 0.3630 -0.0063 0.0291  0.0424  214 THR A N   
1694 C CA  . THR A 234 ? 0.3653 0.1046 0.3164 0.0127  -0.0042 0.0502  214 THR A CA  
1695 C C   . THR A 234 ? 0.3632 0.0444 0.3197 0.0164  0.0009  0.0032  214 THR A C   
1696 O O   . THR A 234 ? 0.4013 0.1093 0.2943 0.0404  0.0117  -0.0128 214 THR A O   
1697 C CB  . THR A 234 ? 0.3704 0.1047 0.3181 0.0145  -0.0238 0.0316  214 THR A CB  
1698 O OG1 . THR A 234 ? 0.3786 0.0660 0.3209 0.0069  -0.0111 0.0039  214 THR A OG1 
1699 C CG2 . THR A 234 ? 0.3863 0.0594 0.3216 0.0092  -0.0056 0.0233  214 THR A CG2 
1700 N N   . ARG A 235 ? 0.3575 0.0706 0.3126 -0.0078 -0.0010 0.0064  215 ARG A N   
1701 C CA  . ARG A 235 ? 0.3673 0.1224 0.2991 0.0334  -0.0112 0.0007  215 ARG A CA  
1702 C C   . ARG A 235 ? 0.4056 0.1169 0.2736 0.0204  -0.0156 -0.0164 215 ARG A C   
1703 O O   . ARG A 235 ? 0.3929 0.0288 0.2752 0.0105  -0.0055 0.0260  215 ARG A O   
1704 C CB  . ARG A 235 ? 0.4182 0.1580 0.3452 0.0125  -0.0129 0.0093  215 ARG A CB  
1705 C CG  . ARG A 235 ? 0.4187 0.1575 0.3702 0.0231  -0.0066 -0.0139 215 ARG A CG  
1706 C CD  . ARG A 235 ? 0.4682 0.2082 0.3949 0.0129  -0.0100 -0.0213 215 ARG A CD  
1707 N NE  . ARG A 235 ? 0.5231 0.1980 0.4123 0.0554  0.0107  -0.0107 215 ARG A NE  
1708 C CZ  . ARG A 235 ? 0.5452 0.2630 0.4019 0.0304  0.0234  -0.0452 215 ARG A CZ  
1709 N NH1 . ARG A 235 ? 0.5908 0.2541 0.3498 -0.0753 0.0013  -0.0466 215 ARG A NH1 
1710 N NH2 . ARG A 235 ? 0.5526 0.2538 0.4277 -0.0021 -0.0060 -0.0873 215 ARG A NH2 
1711 N N   . LEU A 236 ? 0.3608 0.1378 0.2622 0.0387  -0.0233 -0.0133 216 LEU A N   
1712 C CA  . LEU A 236 ? 0.3355 0.1195 0.2490 -0.0028 -0.0063 -0.0130 216 LEU A CA  
1713 C C   . LEU A 236 ? 0.3525 0.0755 0.2797 0.0100  -0.0166 0.0025  216 LEU A C   
1714 O O   . LEU A 236 ? 0.3652 0.1707 0.2788 -0.0016 -0.0401 0.0098  216 LEU A O   
1715 C CB  . LEU A 236 ? 0.3301 0.0917 0.2687 0.0004  0.0017  -0.0150 216 LEU A CB  
1716 C CG  . LEU A 236 ? 0.3556 0.0968 0.2938 0.0088  0.0019  0.0134  216 LEU A CG  
1717 C CD1 . LEU A 236 ? 0.3740 0.0390 0.3047 0.0294  -0.0284 0.0124  216 LEU A CD1 
1718 C CD2 . LEU A 236 ? 0.3768 0.1256 0.3017 -0.0129 0.0193  0.0109  216 LEU A CD2 
1719 N N   . LEU A 237 ? 0.3489 0.1001 0.2397 -0.0278 -0.0202 -0.0060 217 LEU A N   
1720 C CA  . LEU A 237 ? 0.3604 0.1260 0.2743 -0.0016 -0.0046 -0.0288 217 LEU A CA  
1721 C C   . LEU A 237 ? 0.3698 0.1190 0.2491 0.0086  -0.0154 -0.0174 217 LEU A C   
1722 O O   . LEU A 237 ? 0.4260 0.1029 0.2749 0.0019  -0.0418 0.0188  217 LEU A O   
1723 C CB  . LEU A 237 ? 0.3882 0.1823 0.3134 0.0027  -0.0128 -0.0244 217 LEU A CB  
1724 C CG  . LEU A 237 ? 0.4214 0.1906 0.3947 -0.0289 0.0136  -0.0140 217 LEU A CG  
1725 C CD1 . LEU A 237 ? 0.4422 0.0761 0.4158 -0.0527 0.0152  0.0201  217 LEU A CD1 
1726 C CD2 . LEU A 237 ? 0.4825 0.2669 0.4208 -0.0703 0.0082  -0.0608 217 LEU A CD2 
1727 N N   . HIS A 238 ? 0.3670 0.1278 0.2603 0.0062  -0.0218 -0.0290 218 HIS A N   
1728 C CA  . HIS A 238 ? 0.3357 0.1095 0.2715 -0.0176 -0.0113 -0.0074 218 HIS A CA  
1729 C C   . HIS A 238 ? 0.3298 0.1170 0.2594 -0.0214 -0.0170 0.0305  218 HIS A C   
1730 O O   . HIS A 238 ? 0.3426 0.1042 0.3011 0.0018  -0.0389 0.0253  218 HIS A O   
1731 C CB  . HIS A 238 ? 0.3425 0.0941 0.2681 -0.0151 -0.0083 -0.0064 218 HIS A CB  
1732 C CG  . HIS A 238 ? 0.3469 0.0922 0.3101 -0.0298 -0.0286 -0.0192 218 HIS A CG  
1733 N ND1 . HIS A 238 ? 0.3408 0.1263 0.3034 -0.0087 -0.0188 -0.0076 218 HIS A ND1 
1734 C CD2 . HIS A 238 ? 0.3503 0.0923 0.3152 -0.0519 -0.0447 -0.0110 218 HIS A CD2 
1735 C CE1 . HIS A 238 ? 0.3224 0.0930 0.3174 -0.0278 -0.0378 -0.0132 218 HIS A CE1 
1736 N NE2 . HIS A 238 ? 0.3516 0.1057 0.3320 -0.0537 -0.0270 -0.0198 218 HIS A NE2 
1737 N N   . ARG A 239 ? 0.3447 0.1543 0.2669 -0.0298 -0.0311 0.0358  219 ARG A N   
1738 C CA  . ARG A 239 ? 0.3465 0.1198 0.2660 -0.0382 -0.0263 -0.0005 219 ARG A CA  
1739 C C   . ARG A 239 ? 0.3305 0.1150 0.2722 -0.0153 -0.0422 0.0065  219 ARG A C   
1740 O O   . ARG A 239 ? 0.3296 0.0953 0.2744 0.0102  -0.0192 0.0266  219 ARG A O   
1741 C CB  . ARG A 239 ? 0.3628 0.1500 0.2885 -0.0421 -0.0211 -0.0226 219 ARG A CB  
1742 C CG  . ARG A 239 ? 0.3602 0.1248 0.2898 -0.0520 -0.0212 -0.0135 219 ARG A CG  
1743 C CD  . ARG A 239 ? 0.3646 0.1082 0.3673 -0.0443 -0.0165 0.0046  219 ARG A CD  
1744 N NE  . ARG A 239 ? 0.3963 0.1609 0.3830 -0.0595 -0.0323 -0.0221 219 ARG A NE  
1745 C CZ  . ARG A 239 ? 0.4369 0.1344 0.4114 -0.0480 -0.0289 -0.0239 219 ARG A CZ  
1746 N NH1 . ARG A 239 ? 0.4454 0.1299 0.4319 -0.0420 -0.0694 -0.0295 219 ARG A NH1 
1747 N NH2 . ARG A 239 ? 0.4483 0.1396 0.4446 -0.0451 -0.0300 -0.0201 219 ARG A NH2 
1748 N N   . GLU A 240 ? 0.3184 0.1289 0.2961 -0.0186 -0.0263 -0.0240 220 GLU A N   
1749 C CA  . GLU A 240 ? 0.3502 0.1263 0.2862 -0.0120 -0.0337 -0.0111 220 GLU A CA  
1750 C C   . GLU A 240 ? 0.3242 0.1633 0.3121 0.0015  -0.0293 0.0058  220 GLU A C   
1751 O O   . GLU A 240 ? 0.3354 0.1440 0.3742 0.0120  -0.0339 -0.0120 220 GLU A O   
1752 C CB  . GLU A 240 ? 0.3979 0.2074 0.3458 -0.0230 -0.0076 -0.0057 220 GLU A CB  
1753 C CG  . GLU A 240 ? 0.4288 0.1616 0.3859 -0.0216 -0.0081 0.0217  220 GLU A CG  
1754 C CD  . GLU A 240 ? 0.4447 0.2035 0.3855 -0.0121 0.0134  0.0329  220 GLU A CD  
1755 O OE1 . GLU A 240 ? 0.4610 0.2170 0.4281 -0.0441 0.0167  0.0586  220 GLU A OE1 
1756 O OE2 . GLU A 240 ? 0.4842 0.2150 0.4851 0.0365  0.0375  0.0302  220 GLU A OE2 
1757 N N   . LEU A 241 ? 0.2986 0.1724 0.3213 -0.0181 -0.0095 -0.0025 221 LEU A N   
1758 C CA  . LEU A 241 ? 0.3453 0.1348 0.3444 -0.0166 0.0142  0.0141  221 LEU A CA  
1759 C C   . LEU A 241 ? 0.3162 0.1530 0.3230 0.0004  0.0105  0.0231  221 LEU A C   
1760 O O   . LEU A 241 ? 0.3021 0.1516 0.3267 0.0282  0.0015  0.0268  221 LEU A O   
1761 C CB  . LEU A 241 ? 0.3832 0.1529 0.3489 -0.0189 0.0175  0.0302  221 LEU A CB  
1762 C CG  . LEU A 241 ? 0.4649 0.2107 0.3846 -0.0080 0.0039  0.0495  221 LEU A CG  
1763 C CD1 . LEU A 241 ? 0.5043 0.2783 0.4006 -0.0267 -0.0024 0.0459  221 LEU A CD1 
1764 C CD2 . LEU A 241 ? 0.5000 0.2476 0.4373 -0.0714 -0.0024 0.0040  221 LEU A CD2 
1765 N N   . ASP A 242 ? 0.3136 0.1681 0.3212 0.0104  -0.0162 0.0155  222 ASP A N   
1766 C CA  . ASP A 242 ? 0.3251 0.1786 0.3275 -0.0014 -0.0265 0.0078  222 ASP A CA  
1767 C C   . ASP A 242 ? 0.3332 0.1868 0.3004 0.0159  -0.0189 0.0158  222 ASP A C   
1768 O O   . ASP A 242 ? 0.3741 0.1162 0.3265 0.0191  -0.0153 0.0087  222 ASP A O   
1769 C CB  . ASP A 242 ? 0.3733 0.2266 0.3769 0.0072  -0.0588 -0.0192 222 ASP A CB  
1770 C CG  . ASP A 242 ? 0.3677 0.3038 0.4059 0.0440  -0.0509 -0.0250 222 ASP A CG  
1771 O OD1 . ASP A 242 ? 0.4201 0.2625 0.3969 0.0374  -0.0562 0.0099  222 ASP A OD1 
1772 O OD2 . ASP A 242 ? 0.4293 0.5171 0.5131 0.0661  -0.0536 -0.0204 222 ASP A OD2 
1773 N N   . GLY A 243 ? 0.3617 0.1855 0.2916 0.0147  -0.0105 0.0047  223 GLY A N   
1774 C CA  . GLY A 243 ? 0.3464 0.2052 0.2880 0.0152  -0.0094 0.0048  223 GLY A CA  
1775 C C   . GLY A 243 ? 0.3624 0.1710 0.3100 0.0111  0.0025  0.0110  223 GLY A C   
1776 O O   . GLY A 243 ? 0.3935 0.1736 0.2975 0.0193  0.0086  0.0133  223 GLY A O   
1777 N N   . ALA A 244 ? 0.3630 0.2021 0.3382 0.0307  0.0147  0.0192  224 ALA A N   
1778 C CA  . ALA A 244 ? 0.3496 0.1884 0.3282 0.0121  0.0116  0.0016  224 ALA A CA  
1779 C C   . ALA A 244 ? 0.3579 0.2159 0.2828 0.0308  0.0082  0.0094  224 ALA A C   
1780 O O   . ALA A 244 ? 0.3745 0.2228 0.2844 0.0400  0.0076  0.0354  224 ALA A O   
1781 C CB  . ALA A 244 ? 0.3947 0.2437 0.3484 0.0102  0.0004  0.0303  224 ALA A CB  
1782 N N   . GLN A 245 ? 0.3256 0.2121 0.3048 0.0077  -0.0414 0.0004  225 GLN A N   
1783 C CA  . GLN A 245 ? 0.3358 0.1877 0.3249 0.0114  -0.0042 0.0000  225 GLN A CA  
1784 C C   . GLN A 245 ? 0.3391 0.1449 0.2980 0.0303  0.0127  -0.0092 225 GLN A C   
1785 O O   . GLN A 245 ? 0.3582 0.1417 0.2866 0.0068  0.0066  0.0228  225 GLN A O   
1786 C CB  . GLN A 245 ? 0.3420 0.1832 0.3311 0.0038  -0.0037 -0.0078 225 GLN A CB  
1787 C CG  . GLN A 245 ? 0.3657 0.2202 0.3654 0.0097  -0.0028 0.0016  225 GLN A CG  
1788 C CD  . GLN A 245 ? 0.3761 0.2330 0.3613 -0.0155 -0.0085 -0.0110 225 GLN A CD  
1789 O OE1 . GLN A 245 ? 0.3718 0.2035 0.4198 -0.0073 -0.0165 -0.0445 225 GLN A OE1 
1790 N NE2 . GLN A 245 ? 0.3798 0.3500 0.3731 -0.0300 -0.0129 -0.0384 225 GLN A NE2 
1791 N N   . LEU A 246 ? 0.3226 0.1238 0.3235 0.0284  -0.0146 0.0246  226 LEU A N   
1792 C CA  . LEU A 246 ? 0.3051 0.1397 0.3155 0.0282  0.0061  -0.0014 226 LEU A CA  
1793 C C   . LEU A 246 ? 0.3139 0.1635 0.2789 0.0092  0.0269  0.0062  226 LEU A C   
1794 O O   . LEU A 246 ? 0.3530 0.1123 0.2882 -0.0050 0.0126  0.0081  226 LEU A O   
1795 C CB  . LEU A 246 ? 0.3455 0.1449 0.3153 0.0043  0.0215  0.0086  226 LEU A CB  
1796 C CG  . LEU A 246 ? 0.3212 0.1518 0.3123 0.0337  0.0120  -0.0068 226 LEU A CG  
1797 C CD1 . LEU A 246 ? 0.3558 0.1786 0.3318 0.0293  -0.0090 -0.0012 226 LEU A CD1 
1798 C CD2 . LEU A 246 ? 0.3367 0.1550 0.3245 0.0378  0.0041  -0.0135 226 LEU A CD2 
1799 N N   . GLU A 247 ? 0.3677 0.1792 0.2993 -0.0052 0.0275  0.0422  227 GLU A N   
1800 C CA  . GLU A 247 ? 0.4042 0.2077 0.3353 0.0183  0.0191  0.0041  227 GLU A CA  
1801 C C   . GLU A 247 ? 0.3700 0.1959 0.3307 0.0182  0.0210  -0.0098 227 GLU A C   
1802 O O   . GLU A 247 ? 0.3770 0.1830 0.3394 -0.0151 0.0367  -0.0256 227 GLU A O   
1803 C CB  . GLU A 247 ? 0.4628 0.1680 0.3917 0.0274  0.0173  0.0173  227 GLU A CB  
1804 C CG  . GLU A 247 ? 0.5355 0.2562 0.4639 0.0669  0.0264  0.0207  227 GLU A CG  
1805 C CD  . GLU A 247 ? 0.5826 0.3181 0.6448 0.0666  0.0300  0.1092  227 GLU A CD  
1806 O OE1 . GLU A 247 ? 0.6556 0.4173 0.7990 0.1067  0.0703  0.1331  227 GLU A OE1 
1807 O OE2 . GLU A 247 ? 0.5445 0.4042 0.7106 0.0295  0.0073  0.1960  227 GLU A OE2 
1808 N N   . GLN A 248 ? 0.3206 0.1977 0.3117 0.0120  0.0490  -0.0191 228 GLN A N   
1809 C CA  . GLN A 248 ? 0.3327 0.2051 0.3550 0.0186  0.0260  0.0072  228 GLN A CA  
1810 C C   . GLN A 248 ? 0.3374 0.2467 0.3364 -0.0045 0.0177  0.0165  228 GLN A C   
1811 O O   . GLN A 248 ? 0.3138 0.2608 0.2986 0.0231  0.0218  -0.0029 228 GLN A O   
1812 C CB  . GLN A 248 ? 0.3812 0.2341 0.3933 -0.0220 0.0006  -0.0041 228 GLN A CB  
1813 C CG  . GLN A 248 ? 0.3829 0.3491 0.4243 -0.0303 0.0030  0.0330  228 GLN A CG  
1814 C CD  . GLN A 248 ? 0.4152 0.4770 0.5061 -0.0558 0.0030  0.0458  228 GLN A CD  
1815 O OE1 . GLN A 248 ? 0.5285 0.6202 0.5934 -0.0245 -0.0416 0.0780  228 GLN A OE1 
1816 N NE2 . GLN A 248 ? 0.3782 0.4341 0.5432 -0.0355 0.0332  0.0433  228 GLN A NE2 
1817 N N   . LEU A 249 ? 0.3557 0.1635 0.2910 -0.0214 0.0077  -0.0009 229 LEU A N   
1818 C CA  . LEU A 249 ? 0.3520 0.2209 0.2764 -0.0101 0.0024  0.0225  229 LEU A CA  
1819 C C   . LEU A 249 ? 0.3341 0.1862 0.2849 -0.0109 0.0159  -0.0009 229 LEU A C   
1820 O O   . LEU A 249 ? 0.3610 0.2095 0.2526 0.0066  -0.0054 -0.0022 229 LEU A O   
1821 C CB  . LEU A 249 ? 0.3643 0.1641 0.2803 -0.0079 0.0035  0.0240  229 LEU A CB  
1822 C CG  . LEU A 249 ? 0.3904 0.2190 0.2896 0.0082  -0.0173 0.0136  229 LEU A CG  
1823 C CD1 . LEU A 249 ? 0.4376 0.2361 0.3205 0.0112  0.0199  0.0300  229 LEU A CD1 
1824 C CD2 . LEU A 249 ? 0.3877 0.2164 0.2894 0.0044  -0.0012 0.0360  229 LEU A CD2 
1825 N N   . GLN A 250 ? 0.3448 0.1954 0.2891 -0.0133 0.0178  0.0054  230 GLN A N   
1826 C CA  . GLN A 250 ? 0.3584 0.2129 0.3066 -0.0285 -0.0020 -0.0086 230 GLN A CA  
1827 C C   . GLN A 250 ? 0.3398 0.2105 0.3138 -0.0254 0.0127  -0.0138 230 GLN A C   
1828 O O   . GLN A 250 ? 0.3798 0.1723 0.3124 -0.0190 0.0068  -0.0394 230 GLN A O   
1829 C CB  . GLN A 250 ? 0.3764 0.1942 0.3519 -0.0325 0.0079  -0.0039 230 GLN A CB  
1830 C CG  . GLN A 250 ? 0.4138 0.2702 0.4394 -0.0231 -0.0032 -0.0122 230 GLN A CG  
1831 C CD  . GLN A 250 ? 0.4929 0.3567 0.5846 -0.0805 -0.0185 -0.0028 230 GLN A CD  
1832 O OE1 . GLN A 250 ? 0.6244 0.3956 0.6267 -0.0724 -0.0596 -0.0271 230 GLN A OE1 
1833 N NE2 . GLN A 250 ? 0.5066 0.5134 0.7775 -0.0590 -0.0363 0.0046  230 GLN A NE2 
1834 N N   . ARG A 251 ? 0.3417 0.1958 0.3170 -0.0289 0.0268  -0.0105 231 ARG A N   
1835 C CA  . ARG A 251 ? 0.3746 0.2114 0.3155 0.0027  0.0227  -0.0430 231 ARG A CA  
1836 C C   . ARG A 251 ? 0.3513 0.2341 0.3059 0.0144  0.0303  -0.0237 231 ARG A C   
1837 O O   . ARG A 251 ? 0.4078 0.2044 0.3112 0.0268  0.0435  -0.0162 231 ARG A O   
1838 C CB  . ARG A 251 ? 0.4040 0.2605 0.3365 0.0333  -0.0066 -0.0520 231 ARG A CB  
1839 C CG  . ARG A 251 ? 0.4944 0.3473 0.3809 0.0690  0.0022  -0.0448 231 ARG A CG  
1840 C CD  . ARG A 251 ? 0.6007 0.4403 0.4508 0.1139  -0.0489 -0.0007 231 ARG A CD  
1841 N NE  . ARG A 251 ? 0.6724 0.4688 0.5353 0.1129  -0.0702 0.0100  231 ARG A NE  
1842 C CZ  . ARG A 251 ? 0.7406 0.6559 0.6069 0.1032  -0.1001 0.0194  231 ARG A CZ  
1843 N NH1 . ARG A 251 ? 0.7186 0.7057 0.6982 0.0558  -0.0828 0.0443  231 ARG A NH1 
1844 N NH2 . ARG A 251 ? 0.6331 0.6657 0.6808 0.1409  -0.1760 0.0084  231 ARG A NH2 
1845 N N   . ARG A 252 ? 0.3560 0.2422 0.2808 -0.0081 -0.0036 -0.0142 232 ARG A N   
1846 C CA  . ARG A 252 ? 0.3534 0.2777 0.3090 -0.0268 -0.0046 -0.0034 232 ARG A CA  
1847 C C   . ARG A 252 ? 0.3552 0.2035 0.3008 -0.0078 0.0125  -0.0266 232 ARG A C   
1848 O O   . ARG A 252 ? 0.3542 0.2300 0.3034 -0.0079 0.0406  -0.0285 232 ARG A O   
1849 C CB  . ARG A 252 ? 0.3985 0.2957 0.3261 -0.0459 -0.0262 -0.0025 232 ARG A CB  
1850 C CG  . ARG A 252 ? 0.4556 0.4042 0.4028 -0.0604 -0.0259 0.0671  232 ARG A CG  
1851 C CD  . ARG A 252 ? 0.4956 0.5864 0.5163 -0.0683 -0.0244 0.0627  232 ARG A CD  
1852 N NE  . ARG A 252 ? 0.5722 0.5856 0.6460 0.0057  -0.0460 0.0600  232 ARG A NE  
1853 C CZ  . ARG A 252 ? 0.5205 0.5823 0.5971 -0.0455 -0.0574 0.0719  232 ARG A CZ  
1854 N NH1 . ARG A 252 ? 0.6879 0.6371 0.6673 -0.0469 -0.0716 0.0911  232 ARG A NH1 
1855 N NH2 . ARG A 252 ? 0.4389 0.5697 0.4270 -0.0621 -0.0253 0.1204  232 ARG A NH2 
1856 N N   . ALA A 253 ? 0.3482 0.1404 0.3008 0.0072  0.0095  -0.0079 233 ALA A N   
1857 C CA  . ALA A 253 ? 0.3459 0.1839 0.2814 -0.0085 -0.0034 0.0045  233 ALA A CA  
1858 C C   . ALA A 253 ? 0.3549 0.1930 0.2740 -0.0017 0.0088  -0.0042 233 ALA A C   
1859 O O   . ALA A 253 ? 0.3803 0.1890 0.2585 0.0026  0.0234  0.0020  233 ALA A O   
1860 C CB  . ALA A 253 ? 0.3778 0.1796 0.2982 0.0025  0.0014  0.0165  233 ALA A CB  
1861 N N   . ARG A 254 ? 0.3884 0.1852 0.3193 0.0000  0.0284  -0.0193 234 ARG A N   
1862 C CA  . ARG A 254 ? 0.4152 0.2652 0.3239 -0.0404 0.0260  -0.0243 234 ARG A CA  
1863 C C   . ARG A 254 ? 0.4008 0.2091 0.3443 0.0000  0.0298  -0.0310 234 ARG A C   
1864 O O   . ARG A 254 ? 0.4148 0.2420 0.3205 0.0312  0.0190  -0.0590 234 ARG A O   
1865 C CB  . ARG A 254 ? 0.4427 0.2590 0.3976 -0.0708 0.0323  -0.0178 234 ARG A CB  
1866 C CG  . ARG A 254 ? 0.4483 0.3480 0.4647 -0.0815 0.0297  -0.0230 234 ARG A CG  
1867 C CD  . ARG A 254 ? 0.4905 0.3513 0.5621 -0.0593 0.0165  -0.0320 234 ARG A CD  
1868 N NE  . ARG A 254 ? 0.5426 0.3029 0.5920 -0.0856 -0.0048 -0.0335 234 ARG A NE  
1869 C CZ  . ARG A 254 ? 0.5347 0.2422 0.5532 -0.0378 -0.0123 -0.0776 234 ARG A CZ  
1870 N NH1 . ARG A 254 ? 0.5728 0.3060 0.5914 -0.0361 -0.0308 -0.0678 234 ARG A NH1 
1871 N NH2 . ARG A 254 ? 0.6295 0.2699 0.5682 -0.0755 -0.0355 -0.0247 234 ARG A NH2 
1872 N N   . GLU A 255 ? 0.3599 0.1861 0.3431 0.0050  0.0437  -0.0490 235 GLU A N   
1873 C CA  . GLU A 255 ? 0.3936 0.1881 0.3603 -0.0016 0.0459  -0.0163 235 GLU A CA  
1874 C C   . GLU A 255 ? 0.3913 0.2096 0.3231 0.0016  0.0505  0.0011  235 GLU A C   
1875 O O   . GLU A 255 ? 0.4396 0.2247 0.3650 0.0136  0.0663  -0.0157 235 GLU A O   
1876 C CB  . GLU A 255 ? 0.3915 0.1717 0.3607 0.0281  0.0436  -0.0128 235 GLU A CB  
1877 C CG  . GLU A 255 ? 0.4016 0.1743 0.4026 0.0373  0.0512  -0.0264 235 GLU A CG  
1878 C CD  . GLU A 255 ? 0.4310 0.2343 0.4425 0.0557  0.0278  -0.0187 235 GLU A CD  
1879 O OE1 . GLU A 255 ? 0.4244 0.2685 0.4859 0.0361  -0.0126 -0.0492 235 GLU A OE1 
1880 O OE2 . GLU A 255 ? 0.5028 0.2519 0.4844 0.1072  -0.0003 -0.0052 235 GLU A OE2 
1881 N N   . HIS A 256 ? 0.3639 0.2315 0.2888 0.0260  0.0409  0.0055  236 HIS A N   
1882 C CA  . HIS A 256 ? 0.3905 0.2323 0.3145 0.0022  0.0140  0.0094  236 HIS A CA  
1883 C C   . HIS A 256 ? 0.3944 0.2332 0.3315 -0.0043 0.0020  -0.0064 236 HIS A C   
1884 O O   . HIS A 256 ? 0.4511 0.2248 0.3375 0.0259  -0.0112 0.0200  236 HIS A O   
1885 C CB  . HIS A 256 ? 0.3890 0.2453 0.3308 0.0087  0.0053  -0.0154 236 HIS A CB  
1886 C CG  . HIS A 256 ? 0.3721 0.2451 0.3554 0.0151  0.0115  -0.0358 236 HIS A CG  
1887 N ND1 . HIS A 256 ? 0.3902 0.2747 0.3985 -0.0136 -0.0087 -0.0120 236 HIS A ND1 
1888 C CD2 . HIS A 256 ? 0.3596 0.2940 0.3433 0.0042  0.0197  -0.0127 236 HIS A CD2 
1889 C CE1 . HIS A 256 ? 0.4024 0.2974 0.4117 0.0180  0.0111  0.0074  236 HIS A CE1 
1890 N NE2 . HIS A 256 ? 0.3992 0.2867 0.4196 -0.0204 0.0206  -0.0276 236 HIS A NE2 
1891 N N   . GLY A 257 ? 0.3914 0.2030 0.2908 0.0011  0.0217  -0.0312 237 GLY A N   
1892 C CA  . GLY A 257 ? 0.4361 0.2521 0.3737 -0.0157 -0.0124 -0.0315 237 GLY A CA  
1893 C C   . GLY A 257 ? 0.3704 0.2707 0.3437 -0.0083 -0.0295 -0.0164 237 GLY A C   
1894 O O   . GLY A 257 ? 0.4322 0.2687 0.3359 0.0058  -0.0280 -0.0125 237 GLY A O   
1895 N N   . THR A 258 ? 0.3611 0.2667 0.3608 0.0123  -0.0296 0.0253  238 THR A N   
1896 C CA  . THR A 258 ? 0.3524 0.1795 0.3700 -0.0153 -0.0179 0.0090  238 THR A CA  
1897 C C   . THR A 258 ? 0.3703 0.2257 0.3550 0.0298  0.0003  -0.0044 238 THR A C   
1898 O O   . THR A 258 ? 0.3873 0.1650 0.3949 -0.0057 0.0272  -0.0310 238 THR A O   
1899 C CB  . THR A 258 ? 0.3805 0.1431 0.4287 -0.0078 -0.0135 0.0201  238 THR A CB  
1900 O OG1 . THR A 258 ? 0.3420 0.2363 0.3873 -0.0110 0.0096  0.0079  238 THR A OG1 
1901 C CG2 . THR A 258 ? 0.3863 0.0803 0.4807 0.0157  -0.0424 -0.0155 238 THR A CG2 
1902 N N   . THR A 259 ? 0.3749 0.1682 0.3388 0.0151  0.0164  -0.0049 239 THR A N   
1903 C CA  . THR A 259 ? 0.3987 0.1884 0.3406 0.0046  0.0127  0.0008  239 THR A CA  
1904 C C   . THR A 259 ? 0.3378 0.2266 0.3070 -0.0107 0.0022  0.0111  239 THR A C   
1905 O O   . THR A 259 ? 0.3511 0.2243 0.3286 -0.0155 -0.0131 0.0285  239 THR A O   
1906 C CB  . THR A 259 ? 0.4074 0.1973 0.3613 0.0058  -0.0181 -0.0064 239 THR A CB  
1907 O OG1 . THR A 259 ? 0.3742 0.1802 0.3767 0.0216  -0.0427 -0.0294 239 THR A OG1 
1908 C CG2 . THR A 259 ? 0.4338 0.2484 0.3644 0.0017  -0.0063 -0.0158 239 THR A CG2 
1909 N N   . VAL A 260 ? 0.3737 0.1956 0.3196 -0.0224 -0.0061 0.0275  240 VAL A N   
1910 C CA  . VAL A 260 ? 0.3530 0.1413 0.3109 -0.0086 -0.0128 0.0238  240 VAL A CA  
1911 C C   . VAL A 260 ? 0.3160 0.1758 0.2956 0.0169  -0.0125 0.0204  240 VAL A C   
1912 O O   . VAL A 260 ? 0.3210 0.2007 0.2987 -0.0234 -0.0285 0.0238  240 VAL A O   
1913 C CB  . VAL A 260 ? 0.3684 0.1870 0.3130 -0.0183 -0.0082 0.0266  240 VAL A CB  
1914 C CG1 . VAL A 260 ? 0.4249 0.1552 0.3366 -0.0340 -0.0064 0.0422  240 VAL A CG1 
1915 C CG2 . VAL A 260 ? 0.3871 0.2069 0.3568 -0.0135 -0.0294 0.0379  240 VAL A CG2 
1916 N N   . HIS A 261 ? 0.3150 0.1251 0.3194 0.0183  -0.0043 -0.0152 241 HIS A N   
1917 C CA  . HIS A 261 ? 0.2896 0.1282 0.2996 0.0256  0.0061  0.0215  241 HIS A CA  
1918 C C   . HIS A 261 ? 0.2933 0.1362 0.2859 -0.0147 -0.0039 -0.0041 241 HIS A C   
1919 O O   . HIS A 261 ? 0.3445 0.0853 0.2961 0.0067  -0.0138 0.0169  241 HIS A O   
1920 C CB  . HIS A 261 ? 0.3180 0.1474 0.3230 0.0155  0.0005  0.0143  241 HIS A CB  
1921 C CG  . HIS A 261 ? 0.3131 0.1370 0.2671 0.0098  0.0056  0.0177  241 HIS A CG  
1922 N ND1 . HIS A 261 ? 0.3556 0.1330 0.3047 -0.0065 0.0130  0.0146  241 HIS A ND1 
1923 C CD2 . HIS A 261 ? 0.3406 0.1763 0.2917 -0.0068 0.0060  0.0119  241 HIS A CD2 
1924 C CE1 . HIS A 261 ? 0.3649 0.1570 0.2842 -0.0064 -0.0003 0.0211  241 HIS A CE1 
1925 N NE2 . HIS A 261 ? 0.3529 0.1829 0.2758 -0.0204 -0.0045 0.0037  241 HIS A NE2 
1926 N N   . GLY A 262 ? 0.3041 0.1400 0.2719 -0.0361 -0.0216 0.0110  242 GLY A N   
1927 C CA  . GLY A 262 ? 0.3127 0.1747 0.2897 -0.0365 -0.0097 0.0233  242 GLY A CA  
1928 C C   . GLY A 262 ? 0.3008 0.1657 0.2804 -0.0235 -0.0065 0.0190  242 GLY A C   
1929 O O   . GLY A 262 ? 0.3434 0.1310 0.2979 -0.0138 -0.0114 0.0346  242 GLY A O   
1930 N N   . ALA A 263 ? 0.3005 0.1597 0.2808 -0.0160 -0.0122 0.0431  243 ALA A N   
1931 C CA  . ALA A 263 ? 0.3138 0.1527 0.2893 -0.0187 -0.0149 0.0494  243 ALA A CA  
1932 C C   . ALA A 263 ? 0.2755 0.2035 0.2601 -0.0314 -0.0205 0.0348  243 ALA A C   
1933 O O   . ALA A 263 ? 0.3039 0.1677 0.2810 -0.0441 -0.0036 0.0611  243 ALA A O   
1934 C CB  . ALA A 263 ? 0.3470 0.1524 0.3047 -0.0159 -0.0165 0.0335  243 ALA A CB  
1935 N N   . LEU A 264 ? 0.3042 0.1698 0.2623 -0.0421 -0.0087 0.0338  244 LEU A N   
1936 C CA  . LEU A 264 ? 0.3037 0.1762 0.2619 0.0089  0.0032  0.0567  244 LEU A CA  
1937 C C   . LEU A 264 ? 0.3239 0.1432 0.2554 -0.0104 -0.0063 0.0385  244 LEU A C   
1938 O O   . LEU A 264 ? 0.3166 0.1236 0.2480 -0.0135 -0.0097 0.0250  244 LEU A O   
1939 C CB  . LEU A 264 ? 0.3300 0.1984 0.3131 0.0090  0.0237  0.0655  244 LEU A CB  
1940 C CG  . LEU A 264 ? 0.4022 0.2490 0.3594 -0.0065 0.0111  0.1050  244 LEU A CG  
1941 C CD1 . LEU A 264 ? 0.4380 0.2807 0.4002 -0.0002 0.0176  0.1240  244 LEU A CD1 
1942 C CD2 . LEU A 264 ? 0.3997 0.2059 0.3764 -0.0675 -0.0084 0.0997  244 LEU A CD2 
1943 N N   . THR A 265 ? 0.3095 0.0929 0.2605 -0.0100 -0.0097 0.0511  245 THR A N   
1944 C CA  . THR A 265 ? 0.2876 0.1272 0.2765 0.0122  -0.0196 0.0452  245 THR A CA  
1945 C C   . THR A 265 ? 0.2887 0.1335 0.2867 0.0063  -0.0047 0.0385  245 THR A C   
1946 O O   . THR A 265 ? 0.3449 0.0829 0.2877 0.0012  -0.0025 0.0550  245 THR A O   
1947 C CB  . THR A 265 ? 0.2578 0.1820 0.2923 0.0006  -0.0142 0.0330  245 THR A CB  
1948 O OG1 . THR A 265 ? 0.2430 0.1948 0.2899 -0.0248 -0.0254 0.0330  245 THR A OG1 
1949 C CG2 . THR A 265 ? 0.2856 0.1905 0.2999 0.0276  -0.0243 0.0301  245 THR A CG2 
1950 N N   . ALA A 266 ? 0.2846 0.1728 0.2784 -0.0223 -0.0082 0.0377  246 ALA A N   
1951 C CA  . ALA A 266 ? 0.2874 0.1413 0.2740 -0.0243 -0.0044 0.0596  246 ALA A CA  
1952 C C   . ALA A 266 ? 0.2883 0.1652 0.2606 -0.0293 -0.0009 0.0518  246 ALA A C   
1953 O O   . ALA A 266 ? 0.3392 0.1538 0.2970 -0.0325 -0.0070 0.0626  246 ALA A O   
1954 C CB  . ALA A 266 ? 0.3105 0.1565 0.3189 -0.0447 0.0059  0.0364  246 ALA A CB  
1955 N N   . ALA A 267 ? 0.3144 0.1617 0.2464 -0.0027 -0.0165 0.0525  247 ALA A N   
1956 C CA  . ALA A 267 ? 0.3092 0.1100 0.2593 -0.0183 -0.0106 0.0632  247 ALA A CA  
1957 C C   . ALA A 267 ? 0.3193 0.1600 0.2737 -0.0012 0.0000  0.0405  247 ALA A C   
1958 O O   . ALA A 267 ? 0.3360 0.1454 0.2972 -0.0136 -0.0233 0.0472  247 ALA A O   
1959 C CB  . ALA A 267 ? 0.3728 0.0758 0.2755 0.0018  -0.0168 0.0459  247 ALA A CB  
1960 N N   . LEU A 268 ? 0.3028 0.1329 0.2593 0.0049  0.0232  0.0235  248 LEU A N   
1961 C CA  . LEU A 268 ? 0.2962 0.1331 0.2683 0.0181  0.0319  0.0255  248 LEU A CA  
1962 C C   . LEU A 268 ? 0.3152 0.1689 0.2746 -0.0099 0.0307  0.0478  248 LEU A C   
1963 O O   . LEU A 268 ? 0.3632 0.1762 0.2553 -0.0103 0.0130  0.0416  248 LEU A O   
1964 C CB  . LEU A 268 ? 0.3202 0.1166 0.2813 0.0000  0.0434  0.0420  248 LEU A CB  
1965 C CG  . LEU A 268 ? 0.3387 0.1664 0.3168 0.0168  0.0264  0.0348  248 LEU A CG  
1966 C CD1 . LEU A 268 ? 0.3568 0.1771 0.3298 0.0156  0.0197  0.0087  248 LEU A CD1 
1967 C CD2 . LEU A 268 ? 0.3505 0.1160 0.3608 0.0353  0.0617  0.0258  248 LEU A CD2 
1968 N N   . ALA A 269 ? 0.3378 0.1236 0.2900 -0.0303 0.0217  0.0687  249 ALA A N   
1969 C CA  . ALA A 269 ? 0.3617 0.1648 0.2525 -0.0247 0.0118  0.0748  249 ALA A CA  
1970 C C   . ALA A 269 ? 0.3372 0.1639 0.2660 -0.0155 0.0009  0.0605  249 ALA A C   
1971 O O   . ALA A 269 ? 0.3732 0.1364 0.2862 -0.0270 -0.0033 0.0610  249 ALA A O   
1972 C CB  . ALA A 269 ? 0.3528 0.1882 0.2911 -0.0374 -0.0052 0.0649  249 ALA A CB  
1973 N N   . ILE A 270 ? 0.3115 0.1646 0.2910 -0.0324 0.0110  0.0721  250 ILE A N   
1974 C CA  . ILE A 270 ? 0.3291 0.1470 0.2949 -0.0246 -0.0026 0.0623  250 ILE A CA  
1975 C C   . ILE A 270 ? 0.3065 0.1711 0.2836 -0.0444 -0.0033 0.0467  250 ILE A C   
1976 O O   . ILE A 270 ? 0.3738 0.1245 0.3413 -0.0455 0.0074  0.0348  250 ILE A O   
1977 C CB  . ILE A 270 ? 0.3561 0.1632 0.3062 -0.0001 -0.0175 0.0525  250 ILE A CB  
1978 C CG1 . ILE A 270 ? 0.3684 0.1449 0.3202 -0.0109 -0.0042 0.0572  250 ILE A CG1 
1979 C CG2 . ILE A 270 ? 0.3661 0.1578 0.3541 -0.0137 0.0000  0.0682  250 ILE A CG2 
1980 C CD1 . ILE A 270 ? 0.3859 0.1382 0.3525 0.0100  -0.0182 0.0523  250 ILE A CD1 
1981 N N   . ALA A 271 ? 0.3476 0.1399 0.2937 -0.0386 0.0083  0.0442  251 ALA A N   
1982 C CA  . ALA A 271 ? 0.3723 0.1218 0.3038 -0.0312 0.0024  0.0442  251 ALA A CA  
1983 C C   . ALA A 271 ? 0.3561 0.1663 0.3301 -0.0019 -0.0055 0.0364  251 ALA A C   
1984 O O   . ALA A 271 ? 0.3555 0.1466 0.3467 0.0004  -0.0137 0.0109  251 ALA A O   
1985 C CB  . ALA A 271 ? 0.4093 0.1690 0.3105 -0.0467 -0.0001 0.0414  251 ALA A CB  
1986 N N   . ALA A 272 ? 0.3535 0.1118 0.3315 0.0080  0.0003  0.0504  252 ALA A N   
1987 C CA  . ALA A 272 ? 0.3542 0.1225 0.3512 0.0120  0.0008  0.0557  252 ALA A CA  
1988 C C   . ALA A 272 ? 0.3681 0.1566 0.3489 -0.0108 0.0125  0.0541  252 ALA A C   
1989 O O   . ALA A 272 ? 0.4108 0.1180 0.3661 -0.0104 -0.0116 0.0499  252 ALA A O   
1990 C CB  . ALA A 272 ? 0.3718 0.1204 0.3601 -0.0048 0.0182  0.0615  252 ALA A CB  
1991 N N   . GLY A 273 ? 0.3494 0.1595 0.3319 -0.0296 0.0061  0.0714  253 GLY A N   
1992 C CA  . GLY A 273 ? 0.4052 0.1422 0.3426 -0.0435 0.0038  0.0924  253 GLY A CA  
1993 C C   . GLY A 273 ? 0.3861 0.1177 0.3498 -0.0599 0.0150  0.0787  253 GLY A C   
1994 O O   . GLY A 273 ? 0.4681 0.0920 0.4239 -0.0357 0.0204  0.0953  253 GLY A O   
1995 N N   . HIS A 274 ? 0.3623 0.1874 0.3339 -0.0216 -0.0026 0.0592  254 HIS A N   
1996 C CA  . HIS A 274 ? 0.3942 0.1522 0.3630 -0.0305 0.0124  0.0693  254 HIS A CA  
1997 C C   . HIS A 274 ? 0.3888 0.1692 0.3782 -0.0268 -0.0112 0.0393  254 HIS A C   
1998 O O   . HIS A 274 ? 0.4273 0.1827 0.4307 -0.0751 -0.0291 0.0490  254 HIS A O   
1999 C CB  . HIS A 274 ? 0.4200 0.1858 0.3622 -0.0075 0.0253  0.0803  254 HIS A CB  
2000 C CG  . HIS A 274 ? 0.3984 0.2205 0.4074 -0.0122 0.0217  0.0500  254 HIS A CG  
2001 N ND1 . HIS A 274 ? 0.4015 0.2440 0.4354 0.0123  0.0044  0.0205  254 HIS A ND1 
2002 C CD2 . HIS A 274 ? 0.4368 0.2175 0.4168 0.0125  0.0277  0.0567  254 HIS A CD2 
2003 C CE1 . HIS A 274 ? 0.4220 0.2717 0.4628 0.0162  0.0308  0.0166  254 HIS A CE1 
2004 N NE2 . HIS A 274 ? 0.4156 0.2523 0.4482 0.0057  0.0159  0.0443  254 HIS A NE2 
2005 N N   . ASP A 275 ? 0.4124 0.1272 0.3560 -0.0189 -0.0089 0.0381  255 ASP A N   
2006 C CA  . ASP A 275 ? 0.3941 0.1428 0.3642 -0.0150 -0.0005 0.0234  255 ASP A CA  
2007 C C   . ASP A 275 ? 0.4599 0.1035 0.3549 -0.0352 -0.0016 0.0260  255 ASP A C   
2008 O O   . ASP A 275 ? 0.4646 0.1752 0.3884 -0.0115 0.0008  -0.0096 255 ASP A O   
2009 C CB  . ASP A 275 ? 0.4580 0.1836 0.3903 -0.0193 0.0312  0.0377  255 ASP A CB  
2010 C CG  . ASP A 275 ? 0.4510 0.1963 0.4283 -0.0186 0.0386  0.0536  255 ASP A CG  
2011 O OD1 . ASP A 275 ? 0.5456 0.2595 0.4272 0.0296  0.0309  0.0135  255 ASP A OD1 
2012 O OD2 . ASP A 275 ? 0.4435 0.2377 0.5112 0.0213  0.0539  0.0104  255 ASP A OD2 
2013 N N   . HIS A 276 ? 0.4872 0.0817 0.3769 -0.0052 -0.0061 0.0509  256 HIS A N   
2014 C CA  . HIS A 276 ? 0.4709 0.0875 0.3816 -0.0205 0.0081  0.0570  256 HIS A CA  
2015 C C   . HIS A 276 ? 0.4697 0.1566 0.4569 -0.0580 0.0266  0.0419  256 HIS A C   
2016 O O   . HIS A 276 ? 0.4768 0.1468 0.5352 -0.0726 0.0333  0.0413  256 HIS A O   
2017 C CB  . HIS A 276 ? 0.4563 0.0897 0.3722 -0.0471 0.0078  0.0806  256 HIS A CB  
2018 C CG  . HIS A 276 ? 0.4482 0.1011 0.3887 -0.0330 0.0367  0.0894  256 HIS A CG  
2019 N ND1 . HIS A 276 ? 0.4799 0.0810 0.3920 -0.0236 0.0402  0.0663  256 HIS A ND1 
2020 C CD2 . HIS A 276 ? 0.4723 0.1049 0.4282 -0.0130 0.0118  0.1024  256 HIS A CD2 
2021 C CE1 . HIS A 276 ? 0.4881 0.1704 0.4291 -0.0186 0.0221  0.0794  256 HIS A CE1 
2022 N NE2 . HIS A 276 ? 0.4953 0.1403 0.4016 0.0090  0.0177  0.1188  256 HIS A NE2 
2023 N N   . GLN A 277 ? 0.5057 0.1831 0.4313 -0.0390 0.0552  0.0554  257 GLN A N   
2024 C CA  . GLN A 277 ? 0.5279 0.2507 0.5092 -0.0766 0.0371  0.0334  257 GLN A CA  
2025 C C   . GLN A 277 ? 0.5308 0.2635 0.5343 -0.0659 0.0442  0.0729  257 GLN A C   
2026 O O   . GLN A 277 ? 0.5325 0.1869 0.5989 -0.0354 0.0212  0.0908  257 GLN A O   
2027 C CB  . GLN A 277 ? 0.5850 0.2500 0.5327 -0.0792 0.0558  -0.0089 257 GLN A CB  
2028 C CG  . GLN A 277 ? 0.6087 0.2606 0.5944 -0.0812 0.0647  -0.0007 257 GLN A CG  
2029 C CD  . GLN A 277 ? 0.6572 0.2990 0.6357 -0.0667 0.0607  0.0454  257 GLN A CD  
2030 O OE1 . GLN A 277 ? 0.6852 0.3207 0.7143 -0.0486 0.0759  0.0332  257 GLN A OE1 
2031 N NE2 . GLN A 277 ? 0.6714 0.3171 0.5734 -0.0357 0.0593  0.0994  257 GLN A NE2 
2032 N N   . ARG A 278 ? 0.5336 0.2114 0.5028 -0.0511 0.0693  0.0435  258 ARG A N   
2033 C CA  . ARG A 278 ? 0.5377 0.2129 0.5191 -0.0399 0.0958  0.0412  258 ARG A CA  
2034 C C   . ARG A 278 ? 0.5466 0.2443 0.4794 -0.0405 0.0884  0.0046  258 ARG A C   
2035 O O   . ARG A 278 ? 0.4971 0.3538 0.4667 -0.0757 0.0656  0.0176  258 ARG A O   
2036 C CB  . ARG A 278 ? 0.5665 0.2278 0.5549 -0.0338 0.0922  0.0870  258 ARG A CB  
2037 C CG  . ARG A 278 ? 0.6052 0.3440 0.5913 0.0250  0.0818  0.0940  258 ARG A CG  
2038 C CD  . ARG A 278 ? 0.7302 0.4376 0.6396 0.0208  0.0447  0.1898  258 ARG A CD  
2039 N NE  . ARG A 278 ? 0.7400 0.5875 0.6854 0.0294  0.0132  0.1819  258 ARG A NE  
2040 C CZ  . ARG A 278 ? 0.7488 0.7186 0.7339 0.1490  0.0192  0.0616  258 ARG A CZ  
2041 N NH1 . ARG A 278 ? 0.6377 0.7169 0.7680 0.1891  -0.0535 0.1166  258 ARG A NH1 
2042 N NH2 . ARG A 278 ? 0.8437 0.8585 0.7581 0.2140  0.0879  -0.0308 258 ARG A NH2 
2043 N N   . ARG A 279 ? 0.4960 0.3313 0.4690 -0.0026 0.0734  0.0185  259 ARG A N   
2044 C CA  . ARG A 279 ? 0.5400 0.4363 0.5367 0.0265  0.0454  -0.0091 259 ARG A CA  
2045 C C   . ARG A 279 ? 0.4751 0.4044 0.5304 -0.0384 0.0634  -0.0188 259 ARG A C   
2046 O O   . ARG A 279 ? 0.4983 0.3893 0.6280 -0.1145 0.0915  -0.0709 259 ARG A O   
2047 C CB  . ARG A 279 ? 0.5655 0.5365 0.6123 0.0093  0.0451  0.0010  259 ARG A CB  
2048 C CG  . ARG A 279 ? 0.6414 0.5492 0.6202 -0.0086 0.0368  0.0627  259 ARG A CG  
2049 C CD  . ARG A 279 ? 0.6662 0.5011 0.6682 -0.0139 0.0035  0.1206  259 ARG A CD  
2050 N NE  . ARG A 279 ? 0.7257 0.6320 0.7865 -0.0171 0.0108  0.1095  259 ARG A NE  
2051 C CZ  . ARG A 279 ? 0.7731 0.7478 0.7968 0.0129  -0.0155 0.1086  259 ARG A CZ  
2052 N NH1 . ARG A 279 ? 0.8019 0.7532 0.7400 -0.0307 0.0923  0.1354  259 ARG A NH1 
2053 N NH2 . ARG A 279 ? 0.7897 0.8341 0.7691 -0.0017 -0.0876 0.1122  259 ARG A NH2 
2054 N N   . PRO A 280 ? 0.4801 0.2590 0.4778 -0.0359 0.0214  -0.0050 260 PRO A N   
2055 C CA  . PRO A 280 ? 0.4390 0.1701 0.4047 -0.0234 0.0307  0.0365  260 PRO A CA  
2056 C C   . PRO A 280 ? 0.4094 0.2175 0.3723 -0.0272 0.0261  0.0079  260 PRO A C   
2057 O O   . PRO A 280 ? 0.4557 0.2983 0.3954 -0.0351 -0.0326 0.0363  260 PRO A O   
2058 C CB  . PRO A 280 ? 0.4906 0.1905 0.4225 0.0000  0.0238  0.0231  260 PRO A CB  
2059 C CG  . PRO A 280 ? 0.5084 0.1879 0.4424 -0.0385 0.0386  0.0207  260 PRO A CG  
2060 C CD  . PRO A 280 ? 0.4925 0.2478 0.4540 -0.0215 0.0383  0.0111  260 PRO A CD  
2061 N N   . SER A 281 ? 0.4405 0.2005 0.3914 -0.0172 0.0667  0.0219  261 SER A N   
2062 C CA  . SER A 281 ? 0.4565 0.2152 0.4067 0.0171  0.0683  0.0293  261 SER A CA  
2063 C C   . SER A 281 ? 0.4278 0.2339 0.3543 0.0222  0.0562  0.0564  261 SER A C   
2064 O O   . SER A 281 ? 0.4137 0.2008 0.3660 0.0134  0.0640  0.0387  261 SER A O   
2065 C CB  . SER A 281 ? 0.5053 0.3061 0.4080 0.0314  0.0661  0.0337  261 SER A CB  
2066 O OG  . SER A 281 ? 0.5729 0.3009 0.3999 -0.0217 0.0568  0.0850  261 SER A OG  
2067 N N   . HIS A 282 ? 0.4139 0.1709 0.3770 0.0097  0.0442  0.0604  262 HIS A N   
2068 C CA  . HIS A 282 ? 0.3847 0.1668 0.3501 0.0296  0.0111  0.0680  262 HIS A CA  
2069 C C   . HIS A 282 ? 0.4003 0.1920 0.3241 -0.0078 0.0164  0.0842  262 HIS A C   
2070 O O   . HIS A 282 ? 0.4296 0.1716 0.3196 -0.0106 0.0028  0.0878  262 HIS A O   
2071 C CB  . HIS A 282 ? 0.4176 0.1854 0.3428 0.0178  0.0242  0.0638  262 HIS A CB  
2072 C CG  . HIS A 282 ? 0.4599 0.2856 0.3490 0.0507  0.0212  0.0908  262 HIS A CG  
2073 N ND1 . HIS A 282 ? 0.4557 0.2869 0.3302 0.0338  0.0228  0.1040  262 HIS A ND1 
2074 C CD2 . HIS A 282 ? 0.4607 0.2995 0.3682 0.0560  0.0112  0.1042  262 HIS A CD2 
2075 C CE1 . HIS A 282 ? 0.4910 0.3476 0.3448 0.0464  0.0524  0.1008  262 HIS A CE1 
2076 N NE2 . HIS A 282 ? 0.4942 0.3665 0.3372 0.0575  0.0289  0.1060  262 HIS A NE2 
2077 N N   . ILE A 283 ? 0.3998 0.1585 0.3195 -0.0073 0.0192  0.0727  263 ILE A N   
2078 C CA  . ILE A 283 ? 0.3867 0.1825 0.3031 -0.0008 0.0088  0.0951  263 ILE A CA  
2079 C C   . ILE A 283 ? 0.3799 0.2235 0.2911 -0.0097 -0.0018 0.0848  263 ILE A C   
2080 O O   . ILE A 283 ? 0.4051 0.2624 0.2999 -0.0359 -0.0122 0.0297  263 ILE A O   
2081 C CB  . ILE A 283 ? 0.3743 0.1649 0.3277 0.0229  -0.0057 0.0961  263 ILE A CB  
2082 C CG1 . ILE A 283 ? 0.3819 0.2160 0.3371 0.0227  -0.0009 0.0984  263 ILE A CG1 
2083 C CG2 . ILE A 283 ? 0.4148 0.1384 0.3096 0.0471  -0.0118 0.0957  263 ILE A CG2 
2084 C CD1 . ILE A 283 ? 0.3945 0.2190 0.3635 0.0155  0.0029  0.0922  263 ILE A CD1 
2085 N N   . ALA A 284 ? 0.3850 0.1705 0.3193 -0.0190 -0.0001 0.1087  264 ALA A N   
2086 C CA  . ALA A 284 ? 0.3759 0.2185 0.2983 -0.0183 0.0032  0.1050  264 ALA A CA  
2087 C C   . ALA A 284 ? 0.3769 0.1474 0.2796 -0.0325 -0.0067 0.0814  264 ALA A C   
2088 O O   . ALA A 284 ? 0.4102 0.1734 0.2916 -0.0279 0.0302  0.0889  264 ALA A O   
2089 C CB  . ALA A 284 ? 0.4111 0.1867 0.3475 -0.0203 0.0175  0.0831  264 ALA A CB  
2090 N N   . ILE A 285 ? 0.3882 0.1821 0.2714 -0.0238 0.0013  0.0553  265 ILE A N   
2091 C CA  . ILE A 285 ? 0.3610 0.1984 0.2579 -0.0298 0.0002  0.0657  265 ILE A CA  
2092 C C   . ILE A 285 ? 0.3455 0.1516 0.2571 0.0025  -0.0097 0.0606  265 ILE A C   
2093 O O   . ILE A 285 ? 0.4043 0.1994 0.2603 -0.0282 -0.0074 0.0684  265 ILE A O   
2094 C CB  . ILE A 285 ? 0.3492 0.2004 0.2718 -0.0377 0.0078  0.0498  265 ILE A CB  
2095 C CG1 . ILE A 285 ? 0.3860 0.1920 0.2677 -0.0341 -0.0011 0.0327  265 ILE A CG1 
2096 C CG2 . ILE A 285 ? 0.3453 0.2597 0.2667 -0.0139 0.0082  0.0551  265 ILE A CG2 
2097 C CD1 . ILE A 285 ? 0.3926 0.1537 0.2655 -0.0418 -0.0049 0.0294  265 ILE A CD1 
2098 N N   . GLY A 286 ? 0.3641 0.1666 0.2536 0.0066  -0.0090 0.0524  266 GLY A N   
2099 C CA  . GLY A 286 ? 0.3381 0.1851 0.2558 0.0247  -0.0004 0.0551  266 GLY A CA  
2100 C C   . GLY A 286 ? 0.3575 0.1754 0.2441 -0.0090 -0.0198 0.0482  266 GLY A C   
2101 O O   . GLY A 286 ? 0.3853 0.1785 0.2599 -0.0334 -0.0331 0.0604  266 GLY A O   
2102 N N   . SER A 287 ? 0.3297 0.1526 0.2501 -0.0259 -0.0223 0.0690  267 SER A N   
2103 C CA  . SER A 287 ? 0.3331 0.1469 0.2571 -0.0186 -0.0012 0.0772  267 SER A CA  
2104 C C   . SER A 287 ? 0.3451 0.1495 0.2748 -0.0072 -0.0245 0.0524  267 SER A C   
2105 O O   . SER A 287 ? 0.3530 0.1498 0.2867 -0.0102 -0.0277 0.0560  267 SER A O   
2106 C CB  . SER A 287 ? 0.3260 0.1783 0.2876 -0.0160 -0.0088 0.0616  267 SER A CB  
2107 O OG  . SER A 287 ? 0.3506 0.1880 0.3445 0.0073  -0.0380 0.0525  267 SER A OG  
2108 N N   . PRO A 288 ? 0.3421 0.1856 0.2764 -0.0101 -0.0088 0.0606  268 PRO A N   
2109 C CA  . PRO A 288 ? 0.3681 0.2063 0.3021 -0.0155 -0.0133 0.0553  268 PRO A CA  
2110 C C   . PRO A 288 ? 0.3542 0.2209 0.3304 -0.0173 -0.0224 0.0659  268 PRO A C   
2111 O O   . PRO A 288 ? 0.3548 0.2269 0.4131 -0.0163 -0.0607 0.0722  268 PRO A O   
2112 C CB  . PRO A 288 ? 0.4076 0.2326 0.3398 -0.0461 0.0401  0.0521  268 PRO A CB  
2113 C CG  . PRO A 288 ? 0.4131 0.2650 0.3171 -0.0201 0.0046  0.0490  268 PRO A CG  
2114 C CD  . PRO A 288 ? 0.3876 0.1943 0.2968 -0.0153 -0.0013 0.0872  268 PRO A CD  
2115 N N   . ILE A 289 ? 0.3520 0.1876 0.3277 -0.0250 -0.0218 0.0703  269 ILE A N   
2116 C CA  . ILE A 289 ? 0.3435 0.2522 0.3268 0.0053  -0.0074 0.0195  269 ILE A CA  
2117 C C   . ILE A 289 ? 0.3627 0.1814 0.3189 -0.0110 -0.0071 0.0153  269 ILE A C   
2118 O O   . ILE A 289 ? 0.3305 0.1741 0.3077 -0.0428 0.0085  0.0093  269 ILE A O   
2119 C CB  . ILE A 289 ? 0.3308 0.2819 0.3290 0.0187  0.0227  0.0249  269 ILE A CB  
2120 C CG1 . ILE A 289 ? 0.3700 0.3218 0.3502 0.0083  0.0460  0.0405  269 ILE A CG1 
2121 C CG2 . ILE A 289 ? 0.3998 0.3329 0.3431 0.0023  0.0160  0.0241  269 ILE A CG2 
2122 C CD1 . ILE A 289 ? 0.3398 0.3455 0.3611 -0.0045 0.0514  0.0522  269 ILE A CD1 
2123 N N   . ASP A 290 ? 0.3405 0.1899 0.3138 0.0160  -0.0174 0.0473  270 ASP A N   
2124 C CA  . ASP A 290 ? 0.3762 0.2376 0.3161 -0.0324 -0.0188 0.0066  270 ASP A CA  
2125 C C   . ASP A 290 ? 0.3509 0.1802 0.3106 -0.0356 0.0023  -0.0027 270 ASP A C   
2126 O O   . ASP A 290 ? 0.4115 0.3086 0.3299 -0.0036 0.0011  -0.0712 270 ASP A O   
2127 C CB  . ASP A 290 ? 0.3682 0.2240 0.3707 -0.0275 -0.0369 0.0102  270 ASP A CB  
2128 C CG  . ASP A 290 ? 0.3921 0.3220 0.4563 -0.0500 -0.0290 0.0566  270 ASP A CG  
2129 O OD1 . ASP A 290 ? 0.4330 0.2734 0.4391 -0.0743 -0.0440 0.1229  270 ASP A OD1 
2130 O OD2 . ASP A 290 ? 0.4826 0.3649 0.6129 -0.0169 -0.0394 0.0415  270 ASP A OD2 
2131 N N   . PHE A 291 ? 0.3475 0.1015 0.2796 -0.0146 0.0227  0.0024  271 PHE A N   
2132 C CA  . PHE A 291 ? 0.3344 0.2032 0.2778 0.0056  0.0112  0.0070  271 PHE A CA  
2133 C C   . PHE A 291 ? 0.3497 0.2280 0.2765 -0.0010 -0.0045 0.0208  271 PHE A C   
2134 O O   . PHE A 291 ? 0.3594 0.2052 0.2878 0.0004  -0.0112 0.0017  271 PHE A O   
2135 C CB  . PHE A 291 ? 0.3433 0.2226 0.2806 -0.0040 0.0030  0.0290  271 PHE A CB  
2136 C CG  . PHE A 291 ? 0.3310 0.2111 0.2805 0.0033  -0.0090 0.0048  271 PHE A CG  
2137 C CD1 . PHE A 291 ? 0.3474 0.2246 0.3104 0.0008  0.0175  -0.0003 271 PHE A CD1 
2138 C CD2 . PHE A 291 ? 0.3299 0.2032 0.2976 -0.0368 0.0197  0.0533  271 PHE A CD2 
2139 C CE1 . PHE A 291 ? 0.3325 0.2078 0.3250 -0.0131 0.0054  0.0105  271 PHE A CE1 
2140 C CE2 . PHE A 291 ? 0.3291 0.2460 0.3155 0.0324  -0.0246 0.0304  271 PHE A CE2 
2141 C CZ  . PHE A 291 ? 0.3487 0.2193 0.2826 0.0000  -0.0112 0.0072  271 PHE A CZ  
2142 N N   . ARG A 292 ? 0.3304 0.2176 0.2539 -0.0218 -0.0198 0.0092  272 ARG A N   
2143 C CA  . ARG A 292 ? 0.3622 0.2109 0.2686 -0.0132 -0.0093 -0.0121 272 ARG A CA  
2144 C C   . ARG A 292 ? 0.3779 0.2363 0.2854 -0.0259 -0.0286 -0.0255 272 ARG A C   
2145 O O   . ARG A 292 ? 0.3880 0.2340 0.2839 -0.0248 -0.0292 -0.0346 272 ARG A O   
2146 C CB  . ARG A 292 ? 0.3590 0.2184 0.2557 -0.0249 -0.0099 0.0100  272 ARG A CB  
2147 C CG  . ARG A 292 ? 0.3615 0.2197 0.2614 -0.0233 -0.0068 0.0056  272 ARG A CG  
2148 C CD  . ARG A 292 ? 0.3576 0.2309 0.2576 -0.0157 -0.0255 0.0240  272 ARG A CD  
2149 N NE  . ARG A 292 ? 0.3843 0.2767 0.2792 0.0198  -0.0148 0.0395  272 ARG A NE  
2150 C CZ  . ARG A 292 ? 0.4071 0.2529 0.3002 0.0006  -0.0170 -0.0008 272 ARG A CZ  
2151 N NH1 . ARG A 292 ? 0.4118 0.2163 0.3233 0.0084  0.0154  -0.0135 272 ARG A NH1 
2152 N NH2 . ARG A 292 ? 0.3946 0.1700 0.2967 -0.0230 -0.0369 0.0177  272 ARG A NH2 
2153 N N   . ASP A 293 ? 0.4047 0.2044 0.2748 -0.0402 -0.0137 -0.0462 273 ASP A N   
2154 C CA  . ASP A 293 ? 0.4314 0.2042 0.3004 -0.0090 -0.0247 -0.0541 273 ASP A CA  
2155 C C   . ASP A 293 ? 0.3886 0.2720 0.2947 -0.0215 -0.0249 -0.0496 273 ASP A C   
2156 O O   . ASP A 293 ? 0.3883 0.3269 0.2892 -0.0422 -0.0465 -0.0415 273 ASP A O   
2157 C CB  . ASP A 293 ? 0.4683 0.2156 0.3481 0.0114  -0.0514 -0.0544 273 ASP A CB  
2158 C CG  . ASP A 293 ? 0.5061 0.1890 0.4346 0.0308  -0.0377 -0.0180 273 ASP A CG  
2159 O OD1 . ASP A 293 ? 0.5513 0.2025 0.4783 0.0797  -0.0050 0.0638  273 ASP A OD1 
2160 O OD2 . ASP A 293 ? 0.5856 0.0496 0.3945 0.0020  -0.0957 -0.1137 273 ASP A OD2 
2161 N N   . GLU A 294 ? 0.3603 0.2364 0.2749 -0.0199 -0.0088 -0.0613 274 GLU A N   
2162 C CA  . GLU A 294 ? 0.3896 0.3005 0.3011 -0.0402 -0.0156 -0.0333 274 GLU A CA  
2163 C C   . GLU A 294 ? 0.4081 0.3274 0.2787 -0.0239 -0.0002 -0.0167 274 GLU A C   
2164 O O   . GLU A 294 ? 0.4405 0.3781 0.2638 0.0074  0.0148  0.0275  274 GLU A O   
2165 C CB  . GLU A 294 ? 0.4049 0.2898 0.3367 -0.0324 -0.0188 -0.0439 274 GLU A CB  
2166 C CG  . GLU A 294 ? 0.4275 0.3211 0.3794 -0.0481 -0.0112 -0.0214 274 GLU A CG  
2167 C CD  . GLU A 294 ? 0.4512 0.3664 0.4795 -0.0599 0.0054  0.0154  274 GLU A CD  
2168 O OE1 . GLU A 294 ? 0.5351 0.3733 0.6429 -0.0861 -0.0260 0.0421  274 GLU A OE1 
2169 O OE2 . GLU A 294 ? 0.4748 0.4429 0.5712 0.0168  0.0062  0.0490  274 GLU A OE2 
2170 N N   . LEU A 295 ? 0.3840 0.3596 0.2819 -0.0250 0.0065  -0.0220 275 LEU A N   
2171 C CA  . LEU A 295 ? 0.3557 0.3263 0.2785 -0.0215 0.0202  -0.0226 275 LEU A CA  
2172 C C   . LEU A 295 ? 0.3583 0.3903 0.3019 -0.0033 0.0083  -0.0374 275 LEU A C   
2173 O O   . LEU A 295 ? 0.4115 0.3688 0.3176 -0.0137 -0.0214 -0.0529 275 LEU A O   
2174 C CB  . LEU A 295 ? 0.3408 0.3027 0.2781 -0.0167 0.0194  -0.0203 275 LEU A CB  
2175 C CG  . LEU A 295 ? 0.3488 0.2682 0.2803 -0.0167 0.0256  0.0020  275 LEU A CG  
2176 C CD1 . LEU A 295 ? 0.3254 0.2026 0.2725 -0.0422 0.0216  0.0109  275 LEU A CD1 
2177 C CD2 . LEU A 295 ? 0.3614 0.3105 0.2932 -0.0184 0.0053  0.0057  275 LEU A CD2 
2178 N N   . GLU A 296 ? 0.3995 0.4740 0.3365 -0.0267 -0.0248 -0.0579 276 GLU A N   
2179 C CA  . GLU A 296 ? 0.3829 0.4921 0.3250 -0.0153 -0.0572 -0.0476 276 GLU A CA  
2180 C C   . GLU A 296 ? 0.4126 0.5021 0.3417 -0.0409 -0.0438 -0.0174 276 GLU A C   
2181 O O   . GLU A 296 ? 0.4146 0.5534 0.3860 0.0142  -0.0690 -0.0662 276 GLU A O   
2182 C CB  . GLU A 296 ? 0.4383 0.5067 0.3409 -0.0269 -0.0417 -0.0383 276 GLU A CB  
2183 C CG  . GLU A 296 ? 0.4714 0.6002 0.3656 -0.0045 -0.0406 -0.0255 276 GLU A CG  
2184 C CD  . GLU A 296 ? 0.5282 0.7516 0.4092 0.0414  -0.0580 -0.0039 276 GLU A CD  
2185 O OE1 . GLU A 296 ? 0.6359 0.9128 0.4203 0.0250  -0.0130 0.0044  276 GLU A OE1 
2186 O OE2 . GLU A 296 ? 0.6088 0.8100 0.4442 0.1202  -0.1142 0.0111  276 GLU A OE2 
2187 N N   . PRO A 297 ? 0.4643 0.5217 0.3350 -0.0774 -0.0456 -0.0218 277 PRO A N   
2188 C CA  . PRO A 297 ? 0.4655 0.5226 0.3426 -0.1064 -0.0483 0.0042  277 PRO A CA  
2189 C C   . PRO A 297 ? 0.4389 0.4530 0.3131 -0.1052 -0.0320 -0.0314 277 PRO A C   
2190 O O   . PRO A 297 ? 0.4382 0.4143 0.3310 -0.0923 -0.0487 -0.0187 277 PRO A O   
2191 C CB  . PRO A 297 ? 0.4668 0.5353 0.3738 -0.1321 -0.0567 -0.0079 277 PRO A CB  
2192 C CG  . PRO A 297 ? 0.4985 0.5704 0.3872 -0.1158 -0.0104 0.0070  277 PRO A CG  
2193 C CD  . PRO A 297 ? 0.5129 0.5279 0.4059 -0.0969 -0.0022 -0.0036 277 PRO A CD  
2194 N N   . PRO A 298 ? 0.4718 0.4050 0.3521 -0.0967 -0.0429 -0.0623 278 PRO A N   
2195 C CA  . PRO A 298 ? 0.4688 0.3639 0.3220 -0.0770 -0.0314 -0.0311 278 PRO A CA  
2196 C C   . PRO A 298 ? 0.4135 0.3068 0.3016 -0.0880 -0.0182 -0.0378 278 PRO A C   
2197 O O   . PRO A 298 ? 0.4371 0.2684 0.3271 -0.0925 -0.0177 0.0138  278 PRO A O   
2198 C CB  . PRO A 298 ? 0.4759 0.3504 0.3641 -0.0845 -0.0177 -0.0527 278 PRO A CB  
2199 C CG  . PRO A 298 ? 0.5183 0.2942 0.4245 -0.0993 -0.0537 -0.0592 278 PRO A CG  
2200 C CD  . PRO A 298 ? 0.4897 0.3402 0.4381 -0.1027 -0.0385 -0.0781 278 PRO A CD  
2201 N N   . VAL A 299 ? 0.3884 0.2728 0.3075 -0.0480 -0.0257 -0.0294 279 VAL A N   
2202 C CA  . VAL A 299 ? 0.3772 0.2254 0.2978 -0.0273 -0.0164 -0.0200 279 VAL A CA  
2203 C C   . VAL A 299 ? 0.3496 0.2434 0.2740 -0.0225 -0.0003 -0.0444 279 VAL A C   
2204 O O   . VAL A 299 ? 0.3901 0.1936 0.3080 -0.0235 0.0140  -0.0111 279 VAL A O   
2205 C CB  . VAL A 299 ? 0.3594 0.2305 0.3082 -0.0325 -0.0160 -0.0122 279 VAL A CB  
2206 C CG1 . VAL A 299 ? 0.3776 0.2049 0.2976 -0.0098 -0.0151 0.0174  279 VAL A CG1 
2207 C CG2 . VAL A 299 ? 0.4026 0.2336 0.2973 -0.0362 -0.0302 0.0246  279 VAL A CG2 
2208 N N   . ARG A 300 ? 0.3435 0.2314 0.2965 -0.0003 0.0065  -0.0426 280 ARG A N   
2209 C CA  . ARG A 300 ? 0.3670 0.2492 0.2787 -0.0117 -0.0091 -0.0152 280 ARG A CA  
2210 C C   . ARG A 300 ? 0.3454 0.2130 0.2390 0.0044  0.0147  -0.0111 280 ARG A C   
2211 O O   . ARG A 300 ? 0.3273 0.1667 0.2885 0.0299  -0.0032 -0.0303 280 ARG A O   
2212 C CB  . ARG A 300 ? 0.4139 0.2292 0.3329 0.0132  -0.0273 0.0062  280 ARG A CB  
2213 C CG  . ARG A 300 ? 0.4385 0.3281 0.3818 0.0221  -0.0478 -0.0340 280 ARG A CG  
2214 C CD  . ARG A 300 ? 0.4920 0.4262 0.4736 0.0586  -0.0215 -0.0264 280 ARG A CD  
2215 N NE  . ARG A 300 ? 0.5523 0.3600 0.5469 0.0239  0.0060  -0.0420 280 ARG A NE  
2216 C CZ  . ARG A 300 ? 0.5550 0.4061 0.4600 0.0545  0.0255  -0.0662 280 ARG A CZ  
2217 N NH1 . ARG A 300 ? 0.5743 0.4814 0.5156 -0.0085 0.0443  -0.0342 280 ARG A NH1 
2218 N NH2 . ARG A 300 ? 0.5686 0.4263 0.4842 0.0699  0.0285  -0.0846 280 ARG A NH2 
2219 N N   . PRO A 301 ? 0.3468 0.2141 0.2798 0.0051  0.0085  -0.0220 281 PRO A N   
2220 C CA  . PRO A 301 ? 0.3333 0.1841 0.2804 -0.0223 -0.0013 -0.0004 281 PRO A CA  
2221 C C   . PRO A 301 ? 0.3314 0.1656 0.2700 -0.0151 -0.0209 0.0073  281 PRO A C   
2222 O O   . PRO A 301 ? 0.3729 0.1736 0.3128 -0.0712 -0.0156 0.0092  281 PRO A O   
2223 C CB  . PRO A 301 ? 0.3657 0.2564 0.3070 -0.0113 0.0192  -0.0123 281 PRO A CB  
2224 C CG  . PRO A 301 ? 0.4089 0.2388 0.3387 0.0225  0.0104  -0.0321 281 PRO A CG  
2225 C CD  . PRO A 301 ? 0.3883 0.2335 0.3340 0.0207  0.0169  -0.0315 281 PRO A CD  
2226 N N   . ASP A 302 ? 0.3209 0.1453 0.2705 -0.0139 -0.0133 0.0046  282 ASP A N   
2227 C CA  . ASP A 302 ? 0.3350 0.0847 0.2687 -0.0327 -0.0123 -0.0073 282 ASP A CA  
2228 C C   . ASP A 302 ? 0.3329 0.1531 0.2429 -0.0257 -0.0152 -0.0050 282 ASP A C   
2229 O O   . ASP A 302 ? 0.3079 0.1254 0.2585 -0.0146 -0.0098 0.0063  282 ASP A O   
2230 C CB  . ASP A 302 ? 0.3680 0.0852 0.3063 -0.0140 0.0049  0.0055  282 ASP A CB  
2231 C CG  . ASP A 302 ? 0.3853 0.0813 0.3425 -0.0038 -0.0061 -0.0038 282 ASP A CG  
2232 O OD1 . ASP A 302 ? 0.3806 0.1611 0.3384 -0.0336 -0.0206 -0.0094 282 ASP A OD1 
2233 O OD2 . ASP A 302 ? 0.4387 0.0716 0.4052 -0.0084 0.0309  -0.0263 282 ASP A OD2 
2234 N N   . GLU A 303 ? 0.3406 0.1756 0.2733 -0.0120 0.0035  0.0197  283 GLU A N   
2235 C CA  . GLU A 303 ? 0.3230 0.1609 0.2960 -0.0500 -0.0165 0.0026  283 GLU A CA  
2236 C C   . GLU A 303 ? 0.3193 0.1381 0.2802 -0.0213 -0.0047 0.0321  283 GLU A C   
2237 O O   . GLU A 303 ? 0.3066 0.1894 0.2850 -0.0040 0.0017  0.0011  283 GLU A O   
2238 C CB  . GLU A 303 ? 0.3092 0.1908 0.3219 -0.0546 -0.0162 0.0207  283 GLU A CB  
2239 C CG  . GLU A 303 ? 0.3295 0.2270 0.3323 -0.0698 -0.0186 -0.0012 283 GLU A CG  
2240 C CD  . GLU A 303 ? 0.3395 0.2980 0.3344 -0.0422 -0.0131 0.0155  283 GLU A CD  
2241 O OE1 . GLU A 303 ? 0.4007 0.3264 0.3447 -0.0239 0.0033  0.0074  283 GLU A OE1 
2242 O OE2 . GLU A 303 ? 0.3683 0.3716 0.3722 -0.0005 -0.0097 0.0081  283 GLU A OE2 
2243 N N   . VAL A 304 ? 0.2914 0.1216 0.2649 -0.0393 0.0060  0.0155  284 VAL A N   
2244 C CA  . VAL A 304 ? 0.3065 0.1221 0.2568 -0.0155 -0.0072 0.0111  284 VAL A CA  
2245 C C   . VAL A 304 ? 0.3093 0.1812 0.2452 -0.0017 -0.0136 0.0048  284 VAL A C   
2246 O O   . VAL A 304 ? 0.3263 0.1470 0.2865 -0.0266 -0.0404 0.0313  284 VAL A O   
2247 C CB  . VAL A 304 ? 0.3149 0.1329 0.2665 0.0042  -0.0011 0.0174  284 VAL A CB  
2248 C CG1 . VAL A 304 ? 0.3082 0.1215 0.2713 -0.0016 0.0117  0.0234  284 VAL A CG1 
2249 C CG2 . VAL A 304 ? 0.2995 0.2008 0.2745 0.0348  -0.0008 0.0266  284 VAL A CG2 
2250 N N   . GLY A 305 ? 0.3452 0.1651 0.2378 -0.0172 -0.0141 0.0393  285 GLY A N   
2251 C CA  . GLY A 305 ? 0.3543 0.1498 0.2356 0.0138  0.0107  0.0408  285 GLY A CA  
2252 C C   . GLY A 305 ? 0.3605 0.1387 0.2331 0.0059  -0.0016 0.0220  285 GLY A C   
2253 O O   . GLY A 305 ? 0.3636 0.1436 0.2788 -0.0252 0.0025  0.0270  285 GLY A O   
2254 N N   . THR A 306 ? 0.3844 0.1213 0.2683 0.0093  0.0139  0.0496  286 THR A N   
2255 C CA  . THR A 306 ? 0.3823 0.1581 0.2731 -0.0078 0.0036  0.0230  286 THR A CA  
2256 C C   . THR A 306 ? 0.3539 0.1048 0.2850 -0.0299 0.0036  0.0091  286 THR A C   
2257 O O   . THR A 306 ? 0.3729 0.1337 0.3058 0.0092  0.0299  -0.0090 286 THR A O   
2258 C CB  . THR A 306 ? 0.4350 0.1784 0.2980 -0.0056 0.0046  0.0096  286 THR A CB  
2259 O OG1 . THR A 306 ? 0.4744 0.1245 0.3157 -0.0660 0.0027  0.0200  286 THR A OG1 
2260 C CG2 . THR A 306 ? 0.4433 0.2010 0.3085 -0.0034 0.0158  0.0379  286 THR A CG2 
2261 N N   . TYR A 307 ? 0.3334 0.1062 0.2671 -0.0313 0.0004  0.0232  287 TYR A N   
2262 C CA  . TYR A 307 ? 0.3545 0.1047 0.2580 -0.0154 0.0181  0.0251  287 TYR A CA  
2263 C C   . TYR A 307 ? 0.3598 0.1602 0.2791 -0.0169 0.0106  0.0210  287 TYR A C   
2264 O O   . TYR A 307 ? 0.3846 0.1325 0.2999 -0.0153 0.0237  0.0211  287 TYR A O   
2265 C CB  . TYR A 307 ? 0.3670 0.1169 0.2728 -0.0259 0.0189  0.0350  287 TYR A CB  
2266 C CG  . TYR A 307 ? 0.3478 0.1705 0.2514 -0.0068 0.0084  0.0274  287 TYR A CG  
2267 C CD1 . TYR A 307 ? 0.3621 0.1559 0.2446 0.0024  -0.0058 0.0472  287 TYR A CD1 
2268 C CD2 . TYR A 307 ? 0.3521 0.0900 0.2520 -0.0030 -0.0090 0.0252  287 TYR A CD2 
2269 C CE1 . TYR A 307 ? 0.3519 0.1479 0.2724 -0.0077 -0.0258 0.0275  287 TYR A CE1 
2270 C CE2 . TYR A 307 ? 0.3497 0.1488 0.2798 0.0125  -0.0086 0.0159  287 TYR A CE2 
2271 C CZ  . TYR A 307 ? 0.3351 0.1599 0.2702 -0.0020 -0.0246 0.0322  287 TYR A CZ  
2272 O OH  . TYR A 307 ? 0.3572 0.1272 0.2994 -0.0208 0.0012  0.0254  287 TYR A OH  
2273 N N   . VAL A 308 ? 0.3624 0.1448 0.2718 -0.0272 0.0103  0.0150  288 VAL A N   
2274 C CA  . VAL A 308 ? 0.3560 0.1559 0.2891 -0.0007 0.0103  0.0391  288 VAL A CA  
2275 C C   . VAL A 308 ? 0.3348 0.1786 0.2802 -0.0084 0.0241  0.0439  288 VAL A C   
2276 O O   . VAL A 308 ? 0.3246 0.2524 0.2865 -0.0025 0.0401  0.0453  288 VAL A O   
2277 C CB  . VAL A 308 ? 0.3761 0.1619 0.2897 -0.0466 0.0034  0.0536  288 VAL A CB  
2278 C CG1 . VAL A 308 ? 0.3734 0.1844 0.2817 -0.0147 -0.0278 0.0461  288 VAL A CG1 
2279 C CG2 . VAL A 308 ? 0.4088 0.2070 0.3102 -0.0649 -0.0371 0.0522  288 VAL A CG2 
2280 N N   . ALA A 309 ? 0.3454 0.1851 0.2675 -0.0205 0.0073  0.0610  289 ALA A N   
2281 C CA  . ALA A 309 ? 0.3497 0.1851 0.2784 0.0082  0.0001  0.0622  289 ALA A CA  
2282 C C   . ALA A 309 ? 0.3287 0.2193 0.2719 0.0140  -0.0008 0.0406  289 ALA A C   
2283 O O   . ALA A 309 ? 0.3591 0.1402 0.3031 -0.0088 0.0158  0.0523  289 ALA A O   
2284 C CB  . ALA A 309 ? 0.3499 0.2223 0.3056 0.0129  -0.0189 0.0468  289 ALA A CB  
2285 N N   . THR A 310 ? 0.3322 0.2266 0.2946 -0.0130 -0.0098 0.0519  290 THR A N   
2286 C CA  . THR A 310 ? 0.3430 0.2302 0.3204 -0.0013 -0.0175 0.0510  290 THR A CA  
2287 C C   . THR A 310 ? 0.3247 0.2329 0.3297 -0.0053 -0.0138 0.0708  290 THR A C   
2288 O O   . THR A 310 ? 0.3625 0.2839 0.3747 0.0239  0.0005  0.1285  290 THR A O   
2289 C CB  . THR A 310 ? 0.4249 0.2594 0.3573 -0.0296 -0.0109 0.0177  290 THR A CB  
2290 O OG1 . THR A 310 ? 0.4526 0.3045 0.3505 -0.0710 -0.0216 -0.0310 290 THR A OG1 
2291 C CG2 . THR A 310 ? 0.4525 0.3188 0.4209 -0.0363 -0.0112 -0.0193 290 THR A CG2 
2292 N N   . VAL A 311 ? 0.2993 0.2195 0.2910 -0.0503 -0.0193 0.0729  291 VAL A N   
2293 C CA  . VAL A 311 ? 0.3268 0.2889 0.2824 -0.0118 -0.0166 0.0560  291 VAL A CA  
2294 C C   . VAL A 311 ? 0.3606 0.2920 0.3042 -0.0289 -0.0181 0.0900  291 VAL A C   
2295 O O   . VAL A 311 ? 0.3302 0.2406 0.3115 -0.0622 -0.0283 0.1001  291 VAL A O   
2296 C CB  . VAL A 311 ? 0.3693 0.2903 0.2689 -0.0415 -0.0352 0.0545  291 VAL A CB  
2297 C CG1 . VAL A 311 ? 0.3711 0.2974 0.3200 -0.0552 -0.0244 0.0534  291 VAL A CG1 
2298 C CG2 . VAL A 311 ? 0.3993 0.3339 0.2801 -0.0565 -0.0248 0.0706  291 VAL A CG2 
2299 N N   . PRO A 312 ? 0.3516 0.2556 0.3401 -0.0140 -0.0005 0.0643  292 PRO A N   
2300 C CA  . PRO A 312 ? 0.3856 0.2858 0.3538 -0.0025 -0.0061 0.0346  292 PRO A CA  
2301 C C   . PRO A 312 ? 0.3589 0.2039 0.2930 -0.0391 -0.0008 0.0791  292 PRO A C   
2302 O O   . PRO A 312 ? 0.3648 0.2677 0.2888 -0.0235 -0.0038 0.0568  292 PRO A O   
2303 C CB  . PRO A 312 ? 0.4278 0.2602 0.3764 -0.0090 -0.0019 0.0493  292 PRO A CB  
2304 C CG  . PRO A 312 ? 0.3876 0.2492 0.4050 0.0051  0.0025  0.0847  292 PRO A CG  
2305 C CD  . PRO A 312 ? 0.3779 0.2618 0.3650 -0.0192 -0.0054 0.0830  292 PRO A CD  
2306 N N   . VAL A 313 ? 0.3618 0.2033 0.2879 -0.0338 -0.0129 0.0621  293 VAL A N   
2307 C CA  . VAL A 313 ? 0.3426 0.2199 0.2945 -0.0281 -0.0269 0.0645  293 VAL A CA  
2308 C C   . VAL A 313 ? 0.3788 0.2227 0.2883 -0.0553 -0.0225 0.0741  293 VAL A C   
2309 O O   . VAL A 313 ? 0.4189 0.1685 0.3055 -0.0839 0.0129  0.0640  293 VAL A O   
2310 C CB  . VAL A 313 ? 0.3851 0.2191 0.2896 -0.0062 -0.0317 0.0880  293 VAL A CB  
2311 C CG1 . VAL A 313 ? 0.3848 0.2126 0.3093 0.0046  -0.0465 0.0768  293 VAL A CG1 
2312 C CG2 . VAL A 313 ? 0.3663 0.2597 0.3185 -0.0068 -0.0379 0.0529  293 VAL A CG2 
2313 N N   . VAL A 314 ? 0.3700 0.2363 0.2977 -0.0551 -0.0248 0.0631  294 VAL A N   
2314 C CA  . VAL A 314 ? 0.4026 0.2668 0.3213 -0.0600 -0.0179 0.0784  294 VAL A CA  
2315 C C   . VAL A 314 ? 0.3989 0.2116 0.2898 -0.0618 -0.0145 0.0415  294 VAL A C   
2316 O O   . VAL A 314 ? 0.4287 0.3481 0.2892 -0.0189 0.0240  0.0378  294 VAL A O   
2317 C CB  . VAL A 314 ? 0.4337 0.2403 0.3486 -0.0599 0.0174  0.0963  294 VAL A CB  
2318 C CG1 . VAL A 314 ? 0.4847 0.2770 0.3829 -0.1046 0.0168  0.0751  294 VAL A CG1 
2319 C CG2 . VAL A 314 ? 0.4384 0.2463 0.3618 -0.0339 0.0316  0.0982  294 VAL A CG2 
2320 N N   . LEU A 315 ? 0.3838 0.1663 0.3181 -0.0348 -0.0196 0.0592  295 LEU A N   
2321 C CA  . LEU A 315 ? 0.3840 0.2150 0.2962 -0.0287 -0.0267 0.0445  295 LEU A CA  
2322 C C   . LEU A 315 ? 0.3871 0.2333 0.3179 -0.0069 -0.0068 0.0519  295 LEU A C   
2323 O O   . LEU A 315 ? 0.3954 0.2107 0.3493 -0.0035 -0.0063 0.0508  295 LEU A O   
2324 C CB  . LEU A 315 ? 0.4216 0.2369 0.2901 -0.0127 -0.0256 0.0453  295 LEU A CB  
2325 C CG  . LEU A 315 ? 0.4433 0.2355 0.2755 -0.0129 -0.0233 0.0428  295 LEU A CG  
2326 C CD1 . LEU A 315 ? 0.4099 0.2450 0.2586 -0.0143 -0.0182 0.0381  295 LEU A CD1 
2327 C CD2 . LEU A 315 ? 0.4298 0.2173 0.2591 -0.0456 0.0206  0.0226  295 LEU A CD2 
2328 N N   . ASP A 316 ? 0.3875 0.1948 0.3070 0.0360  -0.0034 0.0403  296 ASP A N   
2329 C CA  . ASP A 316 ? 0.3940 0.1919 0.3511 0.0355  -0.0011 0.0426  296 ASP A CA  
2330 C C   . ASP A 316 ? 0.4029 0.1853 0.3306 0.0421  -0.0073 0.0354  296 ASP A C   
2331 O O   . ASP A 316 ? 0.4771 0.1423 0.3397 0.0222  -0.0150 0.0339  296 ASP A O   
2332 C CB  . ASP A 316 ? 0.4332 0.2348 0.3274 0.0278  0.0011  0.0634  296 ASP A CB  
2333 C CG  . ASP A 316 ? 0.4410 0.3004 0.3531 0.0432  0.0090  0.0538  296 ASP A CG  
2334 O OD1 . ASP A 316 ? 0.4741 0.2536 0.3633 -0.0022 -0.0006 0.0627  296 ASP A OD1 
2335 O OD2 . ASP A 316 ? 0.4794 0.2998 0.4043 0.0330  0.0274  0.0868  296 ASP A OD2 
2336 N N   . ILE A 317 ? 0.3899 0.2048 0.3706 0.0064  0.0100  0.0556  297 ILE A N   
2337 C CA  . ILE A 317 ? 0.3970 0.1892 0.3496 0.0139  -0.0155 0.0528  297 ILE A CA  
2338 C C   . ILE A 317 ? 0.4077 0.2010 0.3417 -0.0173 -0.0145 0.0369  297 ILE A C   
2339 O O   . ILE A 317 ? 0.4243 0.2758 0.3529 -0.0358 -0.0534 0.0228  297 ILE A O   
2340 C CB  . ILE A 317 ? 0.4201 0.1590 0.3378 0.0054  -0.0198 0.0627  297 ILE A CB  
2341 C CG1 . ILE A 317 ? 0.5022 0.1675 0.3296 0.0204  -0.0311 0.0926  297 ILE A CG1 
2342 C CG2 . ILE A 317 ? 0.4205 0.1810 0.3264 0.0065  -0.0337 0.0340  297 ILE A CG2 
2343 C CD1 . ILE A 317 ? 0.5378 0.2574 0.4285 -0.0090 -0.0476 0.0600  297 ILE A CD1 
2344 N N   . ALA A 318 ? 0.4088 0.1943 0.3592 -0.0152 0.0236  0.0319  298 ALA A N   
2345 C CA  . ALA A 318 ? 0.4358 0.2171 0.3952 -0.0508 0.0415  0.0478  298 ALA A CA  
2346 C C   . ALA A 318 ? 0.4404 0.2199 0.4109 -0.0677 0.0595  0.0703  298 ALA A C   
2347 O O   . ALA A 318 ? 0.4468 0.3443 0.5120 -0.0994 0.0905  0.0522  298 ALA A O   
2348 C CB  . ALA A 318 ? 0.4871 0.2289 0.4754 -0.0741 0.0469  0.0638  298 ALA A CB  
2349 N N   . ARG A 319 ? 0.4026 0.1894 0.3794 0.0069  0.0602  0.0769  299 ARG A N   
2350 C CA  . ARG A 319 ? 0.3942 0.2444 0.3807 -0.0016 0.0577  0.0453  299 ARG A CA  
2351 C C   . ARG A 319 ? 0.3812 0.2437 0.3415 -0.0003 0.0449  0.0470  299 ARG A C   
2352 O O   . ARG A 319 ? 0.3845 0.2238 0.3452 -0.0191 0.0245  0.0393  299 ARG A O   
2353 C CB  . ARG A 319 ? 0.4574 0.2576 0.3962 0.0354  0.0217  0.0665  299 ARG A CB  
2354 C CG  . ARG A 319 ? 0.4872 0.3330 0.4244 0.0767  0.0431  0.0844  299 ARG A CG  
2355 C CD  . ARG A 319 ? 0.5614 0.3698 0.4739 0.0675  0.0865  0.0864  299 ARG A CD  
2356 N NE  . ARG A 319 ? 0.6381 0.4622 0.5958 0.0806  0.1200  0.0488  299 ARG A NE  
2357 C CZ  . ARG A 319 ? 0.6718 0.4645 0.6392 0.0386  0.1858  0.0244  299 ARG A CZ  
2358 N NH1 . ARG A 319 ? 0.7225 0.5508 0.7302 -0.0421 0.2125  -0.0140 299 ARG A NH1 
2359 N NH2 . ARG A 319 ? 0.6883 0.4181 0.6189 0.0347  0.1983  0.0340  299 ARG A NH2 
2360 N N   . PRO A 320 ? 0.3611 0.2342 0.3487 -0.0033 0.0495  0.0706  300 PRO A N   
2361 C CA  . PRO A 320 ? 0.3586 0.2334 0.3648 -0.0156 0.0379  0.0665  300 PRO A CA  
2362 C C   . PRO A 320 ? 0.3425 0.2438 0.3070 -0.0114 0.0270  0.0438  300 PRO A C   
2363 O O   . PRO A 320 ? 0.3606 0.2100 0.3199 -0.0130 -0.0146 0.0652  300 PRO A O   
2364 C CB  . PRO A 320 ? 0.3608 0.2620 0.3903 -0.0168 0.0627  0.0492  300 PRO A CB  
2365 C CG  . PRO A 320 ? 0.4143 0.2817 0.3960 0.0165  0.0457  0.0730  300 PRO A CG  
2366 C CD  . PRO A 320 ? 0.4000 0.2509 0.3872 0.0250  0.0412  0.0580  300 PRO A CD  
2367 N N   . PHE A 321 ? 0.3638 0.1782 0.3046 -0.0142 0.0074  0.0445  301 PHE A N   
2368 C CA  . PHE A 321 ? 0.3425 0.2077 0.2709 -0.0189 -0.0025 0.0252  301 PHE A CA  
2369 C C   . PHE A 321 ? 0.3278 0.1987 0.2698 -0.0041 -0.0052 0.0217  301 PHE A C   
2370 O O   . PHE A 321 ? 0.3353 0.1554 0.2792 -0.0311 -0.0056 0.0251  301 PHE A O   
2371 C CB  . PHE A 321 ? 0.3402 0.2210 0.2642 -0.0112 -0.0045 0.0079  301 PHE A CB  
2372 C CG  . PHE A 321 ? 0.3228 0.1991 0.2529 -0.0140 0.0111  0.0131  301 PHE A CG  
2373 C CD1 . PHE A 321 ? 0.3421 0.1642 0.2842 0.0042  0.0168  0.0289  301 PHE A CD1 
2374 C CD2 . PHE A 321 ? 0.3507 0.1907 0.2755 -0.0068 0.0155  -0.0095 301 PHE A CD2 
2375 C CE1 . PHE A 321 ? 0.3581 0.1885 0.2711 -0.0110 0.0079  0.0091  301 PHE A CE1 
2376 C CE2 . PHE A 321 ? 0.3409 0.2245 0.2911 -0.0075 0.0210  -0.0131 301 PHE A CE2 
2377 C CZ  . PHE A 321 ? 0.3531 0.1860 0.2869 -0.0152 0.0291  0.0048  301 PHE A CZ  
2378 N N   . TRP A 322 ? 0.2955 0.2425 0.2793 0.0068  -0.0045 0.0286  302 TRP A N   
2379 C CA  . TRP A 322 ? 0.3374 0.2097 0.2906 -0.0016 -0.0020 0.0179  302 TRP A CA  
2380 C C   . TRP A 322 ? 0.3380 0.2494 0.2865 -0.0025 0.0092  0.0299  302 TRP A C   
2381 O O   . TRP A 322 ? 0.3696 0.2407 0.2908 -0.0080 -0.0252 0.0329  302 TRP A O   
2382 C CB  . TRP A 322 ? 0.3258 0.2212 0.3149 0.0169  -0.0046 0.0282  302 TRP A CB  
2383 C CG  . TRP A 322 ? 0.3604 0.2042 0.3078 -0.0144 0.0016  0.0175  302 TRP A CG  
2384 C CD1 . TRP A 322 ? 0.3634 0.2258 0.3348 0.0045  0.0156  0.0315  302 TRP A CD1 
2385 C CD2 . TRP A 322 ? 0.3733 0.2032 0.3074 0.0077  0.0016  0.0311  302 TRP A CD2 
2386 N NE1 . TRP A 322 ? 0.3833 0.2504 0.3294 0.0357  0.0021  0.0482  302 TRP A NE1 
2387 C CE2 . TRP A 322 ? 0.3635 0.2307 0.3252 0.0066  -0.0130 0.0480  302 TRP A CE2 
2388 C CE3 . TRP A 322 ? 0.3610 0.1688 0.2957 0.0043  -0.0092 0.0304  302 TRP A CE3 
2389 C CZ2 . TRP A 322 ? 0.3680 0.1728 0.3157 0.0269  -0.0112 0.0599  302 TRP A CZ2 
2390 C CZ3 . TRP A 322 ? 0.3347 0.2078 0.3031 -0.0171 -0.0052 0.0121  302 TRP A CZ3 
2391 C CH2 . TRP A 322 ? 0.3731 0.1661 0.2937 -0.0054 -0.0245 0.0196  302 TRP A CH2 
2392 N N   . GLU A 323 ? 0.3539 0.2346 0.3106 0.0000  0.0041  0.0382  303 GLU A N   
2393 C CA  . GLU A 323 ? 0.3699 0.2946 0.3185 -0.0126 0.0028  0.0503  303 GLU A CA  
2394 C C   . GLU A 323 ? 0.3391 0.2500 0.3011 -0.0054 0.0038  0.0579  303 GLU A C   
2395 O O   . GLU A 323 ? 0.3642 0.2027 0.2966 -0.0003 -0.0032 0.0300  303 GLU A O   
2396 C CB  . GLU A 323 ? 0.4053 0.3122 0.3392 -0.0378 -0.0093 0.0597  303 GLU A CB  
2397 C CG  . GLU A 323 ? 0.4299 0.3367 0.4307 -0.0203 -0.0152 0.0856  303 GLU A CG  
2398 C CD  . GLU A 323 ? 0.4696 0.4420 0.4432 -0.0128 0.0226  0.1199  303 GLU A CD  
2399 O OE1 . GLU A 323 ? 0.4276 0.5230 0.5241 -0.0521 0.0956  0.0707  303 GLU A OE1 
2400 O OE2 . GLU A 323 ? 0.5888 0.4327 0.5938 0.0497  -0.0044 0.1636  303 GLU A OE2 
2401 N N   . VAL A 324 ? 0.3328 0.2685 0.2716 -0.0136 0.0078  0.0726  304 VAL A N   
2402 C CA  . VAL A 324 ? 0.3418 0.2356 0.2845 -0.0133 0.0012  0.0512  304 VAL A CA  
2403 C C   . VAL A 324 ? 0.3237 0.2043 0.2843 -0.0021 -0.0096 0.0442  304 VAL A C   
2404 O O   . VAL A 324 ? 0.3545 0.2033 0.2911 0.0020  -0.0105 0.0161  304 VAL A O   
2405 C CB  . VAL A 324 ? 0.3381 0.2308 0.3054 -0.0130 0.0067  0.0622  304 VAL A CB  
2406 C CG1 . VAL A 324 ? 0.3449 0.2378 0.3031 -0.0205 0.0312  0.0730  304 VAL A CG1 
2407 C CG2 . VAL A 324 ? 0.3360 0.2824 0.3408 -0.0092 0.0293  0.0629  304 VAL A CG2 
2408 N N   . ALA A 325 ? 0.3045 0.1816 0.2849 -0.0003 -0.0222 0.0402  305 ALA A N   
2409 C CA  . ALA A 325 ? 0.3267 0.1699 0.2735 -0.0077 -0.0165 0.0108  305 ALA A CA  
2410 C C   . ALA A 325 ? 0.3219 0.2031 0.2630 0.0081  -0.0198 0.0318  305 ALA A C   
2411 O O   . ALA A 325 ? 0.3385 0.1923 0.2793 0.0019  -0.0138 0.0241  305 ALA A O   
2412 C CB  . ALA A 325 ? 0.3538 0.1416 0.2814 -0.0244 -0.0150 0.0176  305 ALA A CB  
2413 N N   . ARG A 326 ? 0.3369 0.2328 0.2764 -0.0184 -0.0066 0.0220  306 ARG A N   
2414 C CA  . ARG A 326 ? 0.3835 0.1962 0.2724 -0.0201 -0.0108 0.0087  306 ARG A CA  
2415 C C   . ARG A 326 ? 0.3514 0.2293 0.2844 -0.0239 -0.0314 -0.0049 306 ARG A C   
2416 O O   . ARG A 326 ? 0.3639 0.1816 0.2855 -0.0314 -0.0170 0.0016  306 ARG A O   
2417 C CB  . ARG A 326 ? 0.3800 0.2101 0.2655 -0.0070 -0.0179 0.0052  306 ARG A CB  
2418 C CG  . ARG A 326 ? 0.4355 0.2937 0.2962 0.0080  0.0063  -0.0327 306 ARG A CG  
2419 C CD  . ARG A 326 ? 0.4682 0.3545 0.3746 0.0221  0.0287  -0.0145 306 ARG A CD  
2420 N NE  . ARG A 326 ? 0.5394 0.3823 0.4151 -0.0278 0.0289  -0.0139 306 ARG A NE  
2421 C CZ  . ARG A 326 ? 0.5317 0.3951 0.5560 -0.0148 0.0502  0.0509  306 ARG A CZ  
2422 N NH1 . ARG A 326 ? 0.5745 0.2307 0.6252 -0.0270 0.0707  0.0835  306 ARG A NH1 
2423 N NH2 . ARG A 326 ? 0.5283 0.4361 0.5754 -0.0348 0.0722  0.0694  306 ARG A NH2 
2424 N N   . ALA A 327 ? 0.3416 0.1962 0.2817 -0.0172 -0.0124 -0.0177 307 ALA A N   
2425 C CA  . ALA A 327 ? 0.3697 0.2540 0.3102 -0.0026 -0.0284 0.0019  307 ALA A CA  
2426 C C   . ALA A 327 ? 0.3461 0.2063 0.2998 -0.0293 -0.0245 0.0316  307 ALA A C   
2427 O O   . ALA A 327 ? 0.3637 0.2149 0.2722 -0.0112 -0.0062 0.0384  307 ALA A O   
2428 C CB  . ALA A 327 ? 0.3519 0.2514 0.3061 -0.0193 -0.0144 0.0096  307 ALA A CB  
2429 N N   . LEU A 328 ? 0.3379 0.1644 0.2801 0.0094  -0.0358 0.0266  308 LEU A N   
2430 C CA  . LEU A 328 ? 0.3680 0.1855 0.2978 0.0047  -0.0328 0.0404  308 LEU A CA  
2431 C C   . LEU A 328 ? 0.3414 0.2097 0.2761 -0.0127 -0.0346 0.0300  308 LEU A C   
2432 O O   . LEU A 328 ? 0.3573 0.1855 0.2954 -0.0287 -0.0408 0.0110  308 LEU A O   
2433 C CB  . LEU A 328 ? 0.3697 0.1627 0.3030 0.0039  -0.0400 0.0207  308 LEU A CB  
2434 C CG  . LEU A 328 ? 0.3866 0.1668 0.3304 -0.0063 -0.0354 0.0377  308 LEU A CG  
2435 C CD1 . LEU A 328 ? 0.4137 0.1439 0.3205 -0.0069 -0.0293 -0.0062 308 LEU A CD1 
2436 C CD2 . LEU A 328 ? 0.4108 0.2069 0.3280 0.0405  -0.0113 0.0216  308 LEU A CD2 
2437 N N   . THR A 329 ? 0.3211 0.2361 0.2634 -0.0030 -0.0281 0.0198  309 THR A N   
2438 C CA  . THR A 329 ? 0.3674 0.1977 0.2990 -0.0031 -0.0324 0.0203  309 THR A CA  
2439 C C   . THR A 329 ? 0.3581 0.1598 0.3213 0.0042  -0.0269 0.0066  309 THR A C   
2440 O O   . THR A 329 ? 0.3629 0.2048 0.3448 0.0029  -0.0628 0.0285  309 THR A O   
2441 C CB  . THR A 329 ? 0.3810 0.1824 0.3181 -0.0247 -0.0376 0.0150  309 THR A CB  
2442 O OG1 . THR A 329 ? 0.3880 0.1704 0.3469 -0.0175 -0.0158 -0.0080 309 THR A OG1 
2443 C CG2 . THR A 329 ? 0.3974 0.2403 0.3200 -0.0377 -0.0376 0.0197  309 THR A CG2 
2444 N N   . ASP A 330 ? 0.3671 0.2091 0.2994 -0.0305 -0.0392 -0.0123 310 ASP A N   
2445 C CA  . ASP A 330 ? 0.3820 0.2655 0.2845 -0.0094 -0.0363 -0.0207 310 ASP A CA  
2446 C C   . ASP A 330 ? 0.3752 0.2381 0.3029 -0.0126 -0.0230 -0.0164 310 ASP A C   
2447 O O   . ASP A 330 ? 0.3830 0.2954 0.3539 0.0327  -0.0210 0.0197  310 ASP A O   
2448 C CB  . ASP A 330 ? 0.3722 0.3030 0.3073 -0.0054 -0.0337 -0.0283 310 ASP A CB  
2449 C CG  . ASP A 330 ? 0.4153 0.3220 0.3540 0.0144  -0.0339 -0.0178 310 ASP A CG  
2450 O OD1 . ASP A 330 ? 0.5067 0.3640 0.3659 0.0226  -0.0365 -0.0185 310 ASP A OD1 
2451 O OD2 . ASP A 330 ? 0.4217 0.3706 0.3877 0.0445  -0.0197 0.0395  310 ASP A OD2 
2452 N N   . ASP A 331 ? 0.3682 0.2610 0.2859 -0.0173 -0.0353 -0.0023 311 ASP A N   
2453 C CA  . ASP A 331 ? 0.4082 0.2705 0.3324 0.0013  -0.0212 0.0009  311 ASP A CA  
2454 C C   . ASP A 331 ? 0.3834 0.2600 0.3137 0.0225  -0.0286 0.0022  311 ASP A C   
2455 O O   . ASP A 331 ? 0.3735 0.2373 0.3391 0.0046  -0.0078 0.0098  311 ASP A O   
2456 C CB  . ASP A 331 ? 0.4354 0.2437 0.3330 0.0058  -0.0171 0.0156  311 ASP A CB  
2457 C CG  . ASP A 331 ? 0.4960 0.3102 0.3473 0.0515  -0.0083 0.0696  311 ASP A CG  
2458 O OD1 . ASP A 331 ? 0.5289 0.3982 0.4185 0.0581  -0.0253 0.0391  311 ASP A OD1 
2459 O OD2 . ASP A 331 ? 0.5208 0.3089 0.3896 0.0579  -0.0102 0.0680  311 ASP A OD2 
2460 N N   . LEU A 332 ? 0.3477 0.2268 0.3144 0.0317  -0.0408 -0.0042 312 LEU A N   
2461 C CA  . LEU A 332 ? 0.3635 0.2271 0.2953 0.0167  -0.0292 -0.0014 312 LEU A CA  
2462 C C   . LEU A 332 ? 0.3544 0.2608 0.2765 -0.0013 -0.0281 0.0152  312 LEU A C   
2463 O O   . LEU A 332 ? 0.3718 0.3031 0.3059 0.0152  -0.0232 0.0265  312 LEU A O   
2464 C CB  . LEU A 332 ? 0.3766 0.2598 0.3167 0.0340  -0.0453 -0.0058 312 LEU A CB  
2465 C CG  . LEU A 332 ? 0.4188 0.3144 0.3332 0.0632  -0.0196 0.0488  312 LEU A CG  
2466 C CD1 . LEU A 332 ? 0.4520 0.3456 0.3336 0.0908  -0.0253 -0.0007 312 LEU A CD1 
2467 C CD2 . LEU A 332 ? 0.4651 0.3481 0.2823 0.0562  -0.0154 0.0404  312 LEU A CD2 
2468 N N   . GLY A 333 ? 0.3439 0.2631 0.2968 -0.0018 -0.0247 -0.0009 313 GLY A N   
2469 C CA  . GLY A 333 ? 0.4000 0.2821 0.3396 -0.0226 -0.0294 -0.0202 313 GLY A CA  
2470 C C   . GLY A 333 ? 0.3947 0.3029 0.3195 -0.0324 -0.0177 -0.0221 313 GLY A C   
2471 O O   . GLY A 333 ? 0.4319 0.2788 0.3976 -0.0099 -0.0522 -0.0457 313 GLY A O   
2472 N N   . GLU A 334 ? 0.3925 0.2811 0.3095 -0.0504 -0.0202 -0.0251 314 GLU A N   
2473 C CA  . GLU A 334 ? 0.4142 0.3337 0.3104 -0.0308 -0.0126 -0.0162 314 GLU A CA  
2474 C C   . GLU A 334 ? 0.3821 0.3284 0.3200 -0.0322 -0.0326 0.0094  314 GLU A C   
2475 O O   . GLU A 334 ? 0.4047 0.2711 0.3258 -0.0026 -0.0409 -0.0135 314 GLU A O   
2476 C CB  . GLU A 334 ? 0.4616 0.4317 0.3413 -0.0361 0.0001  0.0112  314 GLU A CB  
2477 C CG  . GLU A 334 ? 0.4996 0.5218 0.3796 -0.0295 0.0024  0.0269  314 GLU A CG  
2478 C CD  . GLU A 334 ? 0.5408 0.6245 0.4096 -0.0197 -0.0273 0.0178  314 GLU A CD  
2479 O OE1 . GLU A 334 ? 0.5482 0.7476 0.4607 0.0187  -0.0413 -0.0005 314 GLU A OE1 
2480 O OE2 . GLU A 334 ? 0.5297 0.6958 0.4767 0.0424  -0.0390 -0.0332 314 GLU A OE2 
2481 N N   . ARG A 335 ? 0.3476 0.2922 0.2843 -0.0115 -0.0387 0.0309  315 ARG A N   
2482 C CA  . ARG A 335 ? 0.3924 0.2626 0.3156 -0.0056 -0.0365 0.0368  315 ARG A CA  
2483 C C   . ARG A 335 ? 0.3740 0.2722 0.3029 0.0018  -0.0190 0.0116  315 ARG A C   
2484 O O   . ARG A 335 ? 0.3959 0.2454 0.3878 -0.0197 -0.0331 0.0201  315 ARG A O   
2485 C CB  . ARG A 335 ? 0.4046 0.2382 0.3101 -0.0108 -0.0303 0.0610  315 ARG A CB  
2486 C CG  . ARG A 335 ? 0.4068 0.2505 0.3375 -0.0316 -0.0330 0.0387  315 ARG A CG  
2487 C CD  . ARG A 335 ? 0.4098 0.1830 0.3120 -0.0280 -0.0255 0.0565  315 ARG A CD  
2488 N NE  . ARG A 335 ? 0.3894 0.1865 0.3245 -0.0193 -0.0346 0.0739  315 ARG A NE  
2489 C CZ  . ARG A 335 ? 0.3858 0.2409 0.3631 0.0037  -0.0148 0.0618  315 ARG A CZ  
2490 N NH1 . ARG A 335 ? 0.4029 0.2411 0.3552 0.0037  -0.0075 0.0701  315 ARG A NH1 
2491 N NH2 . ARG A 335 ? 0.3634 0.2744 0.3765 -0.0143 -0.0203 0.0723  315 ARG A NH2 
2492 N N   . ARG A 336 ? 0.3697 0.2586 0.3205 0.0208  -0.0275 -0.0118 316 ARG A N   
2493 C CA  . ARG A 336 ? 0.3980 0.3038 0.3565 -0.0040 -0.0333 0.0040  316 ARG A CA  
2494 C C   . ARG A 336 ? 0.3711 0.3581 0.3630 0.0034  -0.0237 -0.0160 316 ARG A C   
2495 O O   . ARG A 336 ? 0.3621 0.3976 0.4108 -0.0164 0.0071  -0.0492 316 ARG A O   
2496 C CB  . ARG A 336 ? 0.4529 0.2881 0.3931 -0.0039 -0.0342 -0.0001 316 ARG A CB  
2497 C CG  . ARG A 336 ? 0.5380 0.3231 0.4141 0.0042  -0.0045 0.0335  316 ARG A CG  
2498 C CD  . ARG A 336 ? 0.6179 0.3044 0.4090 0.0057  0.0139  0.0409  316 ARG A CD  
2499 N NE  . ARG A 336 ? 0.6716 0.3785 0.5140 -0.0464 0.0251  0.0667  316 ARG A NE  
2500 C CZ  . ARG A 336 ? 0.7629 0.3653 0.5603 -0.0464 0.0146  0.0745  316 ARG A CZ  
2501 N NH1 . ARG A 336 ? 0.8181 0.3147 0.6597 -0.0245 -0.0216 0.0774  316 ARG A NH1 
2502 N NH2 . ARG A 336 ? 0.8030 0.3587 0.6137 -0.0555 0.0087  0.0322  316 ARG A NH2 
2503 N N   . ARG A 337 ? 0.4044 0.4216 0.3619 -0.0128 -0.0057 -0.0364 317 ARG A N   
2504 C CA  . ARG A 337 ? 0.4020 0.4809 0.3973 -0.0083 -0.0247 -0.0726 317 ARG A CA  
2505 C C   . ARG A 337 ? 0.4418 0.4767 0.3579 -0.0221 -0.0551 -0.0674 317 ARG A C   
2506 O O   . ARG A 337 ? 0.4116 0.4238 0.3945 -0.0257 -0.0651 -0.0899 317 ARG A O   
2507 C CB  . ARG A 337 ? 0.4390 0.5166 0.4423 0.0015  -0.0300 -0.0892 317 ARG A CB  
2508 C CG  . ARG A 337 ? 0.4736 0.5348 0.5067 0.0168  -0.0092 -0.1079 317 ARG A CG  
2509 C CD  . ARG A 337 ? 0.4904 0.5363 0.5420 -0.0120 0.0017  -0.1119 317 ARG A CD  
2510 N NE  . ARG A 337 ? 0.5415 0.4563 0.5335 -0.0182 0.0116  -0.1081 317 ARG A NE  
2511 C CZ  . ARG A 337 ? 0.5462 0.4839 0.5527 0.0054  0.0188  -0.1040 317 ARG A CZ  
2512 N NH1 . ARG A 337 ? 0.5533 0.4838 0.6011 0.0232  -0.0105 -0.0868 317 ARG A NH1 
2513 N NH2 . ARG A 337 ? 0.5163 0.6269 0.5636 -0.0007 0.0379  -0.0980 317 ARG A NH2 
2514 N N   . GLN A 338 ? 0.4473 0.4507 0.3306 -0.0101 -0.0214 -0.0465 318 GLN A N   
2515 C CA  . GLN A 338 ? 0.4288 0.4636 0.3429 0.0006  -0.0333 -0.0200 318 GLN A CA  
2516 C C   . GLN A 338 ? 0.4075 0.4298 0.3021 0.0089  -0.0305 0.0231  318 GLN A C   
2517 O O   . GLN A 338 ? 0.4346 0.5111 0.3506 0.0400  -0.0021 0.0155  318 GLN A O   
2518 C CB  . GLN A 338 ? 0.4029 0.4443 0.3352 -0.0109 -0.0288 -0.0251 318 GLN A CB  
2519 C CG  . GLN A 338 ? 0.4244 0.4793 0.4463 -0.0109 0.0020  0.0226  318 GLN A CG  
2520 C CD  . GLN A 338 ? 0.6232 0.6232 0.6232 0.0000  0.0000  0.0000  318 GLN A CD  
2521 O OE1 . GLN A 338 ? 0.7431 0.7431 0.7431 0.0000  0.0000  0.0000  318 GLN A OE1 
2522 N NE2 . GLN A 338 ? 0.6414 0.6414 0.6414 0.0000  0.0000  0.0000  318 GLN A NE2 
2523 N N   . GLY A 339 ? 0.3632 0.3291 0.3452 -0.0144 -0.0159 0.0185  319 GLY A N   
2524 C CA  . GLY A 339 ? 0.3903 0.2639 0.3153 -0.0251 -0.0034 0.0390  319 GLY A CA  
2525 C C   . GLY A 339 ? 0.3723 0.2940 0.2995 -0.0141 -0.0012 0.0348  319 GLY A C   
2526 O O   . GLY A 339 ? 0.3864 0.2576 0.3095 0.0017  -0.0180 0.0575  319 GLY A O   
2527 N N   . HIS A 340 ? 0.3704 0.2615 0.2872 -0.0175 0.0041  0.0389  320 HIS A N   
2528 C CA  . HIS A 340 ? 0.3671 0.2527 0.2883 0.0034  0.0037  0.0354  320 HIS A CA  
2529 C C   . HIS A 340 ? 0.3397 0.2465 0.2902 0.0038  0.0215  0.0672  320 HIS A C   
2530 O O   . HIS A 340 ? 0.3935 0.2574 0.2706 -0.0227 0.0149  0.0040  320 HIS A O   
2531 C CB  . HIS A 340 ? 0.3660 0.2581 0.2874 -0.0082 0.0022  0.0590  320 HIS A CB  
2532 C CG  . HIS A 340 ? 0.3599 0.3203 0.2780 -0.0063 0.0075  0.0449  320 HIS A CG  
2533 N ND1 . HIS A 340 ? 0.4031 0.3097 0.2829 -0.0189 0.0133  0.0692  320 HIS A ND1 
2534 C CD2 . HIS A 340 ? 0.3477 0.3549 0.2800 -0.0277 0.0068  0.0579  320 HIS A CD2 
2535 C CE1 . HIS A 340 ? 0.4177 0.3221 0.2837 -0.0200 0.0002  0.0629  320 HIS A CE1 
2536 N NE2 . HIS A 340 ? 0.3639 0.3224 0.3164 -0.0275 0.0150  0.0652  320 HIS A NE2 
2537 N N   . HIS A 341 ? 0.3293 0.2428 0.2894 0.0088  0.0236  0.0629  321 HIS A N   
2538 C CA  . HIS A 341 ? 0.3885 0.2637 0.2909 0.0030  0.0158  0.0712  321 HIS A CA  
2539 C C   . HIS A 341 ? 0.3629 0.2864 0.2520 -0.0241 0.0094  0.0694  321 HIS A C   
2540 O O   . HIS A 341 ? 0.3868 0.2896 0.2703 -0.0020 -0.0187 0.0667  321 HIS A O   
2541 C CB  . HIS A 341 ? 0.3997 0.2457 0.2887 -0.0235 0.0260  0.0733  321 HIS A CB  
2542 C CG  . HIS A 341 ? 0.4319 0.2818 0.2918 -0.0135 0.0280  0.0529  321 HIS A CG  
2543 N ND1 . HIS A 341 ? 0.4579 0.3279 0.3501 -0.0435 0.0415  0.0224  321 HIS A ND1 
2544 C CD2 . HIS A 341 ? 0.4738 0.3152 0.3419 -0.0328 0.0594  0.0323  321 HIS A CD2 
2545 C CE1 . HIS A 341 ? 0.4734 0.3128 0.3937 -0.0396 0.0412  0.0236  321 HIS A CE1 
2546 N NE2 . HIS A 341 ? 0.5014 0.3137 0.3926 -0.0126 0.1005  0.0067  321 HIS A NE2 
2547 N N   . PHE A 342 ? 0.3667 0.2434 0.2687 -0.0604 -0.0023 0.0343  322 PHE A N   
2548 C CA  . PHE A 342 ? 0.3721 0.2416 0.2618 -0.0464 -0.0063 0.0575  322 PHE A CA  
2549 C C   . PHE A 342 ? 0.3444 0.2479 0.2843 -0.0110 -0.0095 0.0662  322 PHE A C   
2550 O O   . PHE A 342 ? 0.3801 0.2667 0.3433 -0.0487 -0.0055 0.0966  322 PHE A O   
2551 C CB  . PHE A 342 ? 0.3938 0.3019 0.2782 -0.0430 -0.0045 0.0406  322 PHE A CB  
2552 C CG  . PHE A 342 ? 0.3992 0.3056 0.3037 -0.0168 0.0030  0.0563  322 PHE A CG  
2553 C CD1 . PHE A 342 ? 0.3925 0.3391 0.3606 -0.0288 0.0053  0.0445  322 PHE A CD1 
2554 C CD2 . PHE A 342 ? 0.4290 0.3472 0.2848 -0.0298 0.0056  0.0378  322 PHE A CD2 
2555 C CE1 . PHE A 342 ? 0.3822 0.3324 0.3685 -0.0474 0.0111  0.0574  322 PHE A CE1 
2556 C CE2 . PHE A 342 ? 0.4219 0.3165 0.3297 -0.0031 -0.0046 0.0436  322 PHE A CE2 
2557 C CZ  . PHE A 342 ? 0.3937 0.3582 0.3540 -0.0231 0.0061  0.0376  322 PHE A CZ  
2558 N N   . ASN A 343 ? 0.3448 0.2558 0.3302 0.0185  0.0165  0.0614  323 ASN A N   
2559 C CA  . ASN A 343 ? 0.3489 0.2589 0.2810 0.0093  -0.0129 0.0875  323 ASN A CA  
2560 C C   . ASN A 343 ? 0.3230 0.2653 0.2916 0.0067  0.0191  0.1011  323 ASN A C   
2561 O O   . ASN A 343 ? 0.3607 0.2444 0.3237 0.0110  0.0035  0.1133  323 ASN A O   
2562 C CB  . ASN A 343 ? 0.3638 0.2700 0.2905 0.0071  0.0067  0.0882  323 ASN A CB  
2563 C CG  . ASN A 343 ? 0.3840 0.3522 0.2875 -0.0035 -0.0069 0.0919  323 ASN A CG  
2564 O OD1 . ASN A 343 ? 0.3738 0.3341 0.2976 -0.0281 0.0033  0.0860  323 ASN A OD1 
2565 N ND2 . ASN A 343 ? 0.4376 0.4271 0.2747 0.0110  0.0072  0.0965  323 ASN A ND2 
2566 N N   . LEU A 344 ? 0.3348 0.2276 0.3305 0.0197  0.0049  0.0782  324 LEU A N   
2567 C CA  . LEU A 344 ? 0.3710 0.2616 0.2890 -0.0036 0.0010  0.0801  324 LEU A CA  
2568 C C   . LEU A 344 ? 0.3361 0.2350 0.2975 -0.0039 -0.0061 0.0506  324 LEU A C   
2569 O O   . LEU A 344 ? 0.3733 0.1922 0.2917 0.0170  -0.0064 0.0678  324 LEU A O   
2570 C CB  . LEU A 344 ? 0.3893 0.2900 0.3197 0.0119  -0.0209 0.0725  324 LEU A CB  
2571 C CG  . LEU A 344 ? 0.4249 0.3561 0.3513 0.0491  -0.0247 0.0340  324 LEU A CG  
2572 C CD1 . LEU A 344 ? 0.4707 0.3672 0.4200 0.0178  -0.0353 0.0320  324 LEU A CD1 
2573 C CD2 . LEU A 344 ? 0.4586 0.3985 0.3971 0.0687  -0.0482 0.0165  324 LEU A CD2 
2574 N N   . VAL A 345 ? 0.3550 0.2257 0.3101 -0.0115 -0.0228 0.0501  325 VAL A N   
2575 C CA  . VAL A 345 ? 0.3656 0.2464 0.2888 0.0027  0.0075  0.0395  325 VAL A CA  
2576 C C   . VAL A 345 ? 0.3621 0.2620 0.2920 -0.0058 0.0167  0.0564  325 VAL A C   
2577 O O   . VAL A 345 ? 0.4235 0.2115 0.3109 -0.0031 0.0248  0.0423  325 VAL A O   
2578 C CB  . VAL A 345 ? 0.3914 0.2378 0.2833 0.0014  0.0084  0.0513  325 VAL A CB  
2579 C CG1 . VAL A 345 ? 0.3983 0.2202 0.3305 0.0117  -0.0037 0.0357  325 VAL A CG1 
2580 C CG2 . VAL A 345 ? 0.3875 0.2634 0.2999 -0.0125 -0.0037 0.0597  325 VAL A CG2 
2581 N N   . THR A 346 ? 0.3850 0.2957 0.2834 0.0074  -0.0154 0.0474  326 THR A N   
2582 C CA  . THR A 346 ? 0.3946 0.2831 0.2997 -0.0132 -0.0096 0.0595  326 THR A CA  
2583 C C   . THR A 346 ? 0.3931 0.3133 0.3213 0.0052  -0.0047 0.0672  326 THR A C   
2584 O O   . THR A 346 ? 0.3755 0.3543 0.3454 0.0062  -0.0069 0.0909  326 THR A O   
2585 C CB  . THR A 346 ? 0.4017 0.3335 0.3084 -0.0103 -0.0151 0.0711  326 THR A CB  
2586 O OG1 . THR A 346 ? 0.3933 0.3726 0.3055 -0.0625 -0.0368 0.0527  326 THR A OG1 
2587 C CG2 . THR A 346 ? 0.4381 0.3693 0.3165 -0.0050 0.0017  0.0990  326 THR A CG2 
2588 N N   . LEU A 347 ? 0.3737 0.2407 0.2897 0.0248  -0.0105 0.0770  327 LEU A N   
2589 C CA  . LEU A 347 ? 0.4125 0.2340 0.2990 0.0177  -0.0119 0.0708  327 LEU A CA  
2590 C C   . LEU A 347 ? 0.4041 0.2479 0.3200 0.0287  0.0138  0.1057  327 LEU A C   
2591 O O   . LEU A 347 ? 0.4488 0.2332 0.3257 0.0508  0.0102  0.0909  327 LEU A O   
2592 C CB  . LEU A 347 ? 0.4128 0.2144 0.2977 -0.0002 -0.0165 0.0813  327 LEU A CB  
2593 C CG  . LEU A 347 ? 0.4571 0.2596 0.3971 -0.0241 -0.0281 0.0883  327 LEU A CG  
2594 C CD1 . LEU A 347 ? 0.4977 0.3191 0.3915 -0.0389 -0.0317 0.1170  327 LEU A CD1 
2595 C CD2 . LEU A 347 ? 0.4872 0.2929 0.4785 -0.0485 -0.0153 0.0930  327 LEU A CD2 
2596 N N   . VAL A 348 ? 0.4068 0.2248 0.3018 0.0245  0.0088  0.0857  328 VAL A N   
2597 C CA  . VAL A 348 ? 0.4114 0.2064 0.3169 0.0285  0.0218  0.0822  328 VAL A CA  
2598 C C   . VAL A 348 ? 0.4071 0.2463 0.3133 0.0120  -0.0047 0.0847  328 VAL A C   
2599 O O   . VAL A 348 ? 0.4167 0.2428 0.4129 0.0102  0.0387  0.0960  328 VAL A O   
2600 C CB  . VAL A 348 ? 0.4085 0.2290 0.3070 0.0352  0.0051  0.0748  328 VAL A CB  
2601 C CG1 . VAL A 348 ? 0.4017 0.2492 0.3118 0.0448  0.0253  0.0815  328 VAL A CG1 
2602 C CG2 . VAL A 348 ? 0.4272 0.2796 0.3320 0.0204  -0.0163 0.0517  328 VAL A CG2 
2603 N N   . ALA A 349 ? 0.4041 0.2268 0.3388 -0.0085 -0.0022 0.0728  329 ALA A N   
2604 C CA  . ALA A 349 ? 0.4186 0.2867 0.3537 0.0103  -0.0219 0.0718  329 ALA A CA  
2605 C C   . ALA A 349 ? 0.3809 0.3893 0.3833 0.0580  -0.0208 0.0948  329 ALA A C   
2606 O O   . ALA A 349 ? 0.3914 0.4459 0.4293 0.0674  0.0204  0.1098  329 ALA A O   
2607 C CB  . ALA A 349 ? 0.4097 0.3453 0.3485 -0.0055 -0.0311 0.0192  329 ALA A CB  
2608 N N   . SER A 350 ? 0.4236 0.3274 0.3992 0.0663  -0.0223 0.1116  330 SER A N   
2609 C CA  . SER A 350 ? 0.4577 0.3798 0.4131 0.0896  -0.0051 0.1192  330 SER A CA  
2610 C C   . SER A 350 ? 0.4574 0.3447 0.4731 0.1275  0.0107  0.0979  330 SER A C   
2611 O O   . SER A 350 ? 0.5250 0.3403 0.5668 0.1562  -0.0628 0.1172  330 SER A O   
2612 C CB  . SER A 350 ? 0.5053 0.5091 0.4054 0.1246  0.0048  0.1020  330 SER A CB  
2613 O OG  . SER A 350 ? 0.5914 0.6661 0.4854 0.1063  -0.0506 0.0675  330 SER A OG  
2614 N N   . ALA A 351 ? 0.4564 0.2345 0.4473 0.0622  0.0387  0.1181  331 ALA A N   
2615 C CA  . ALA A 351 ? 0.4924 0.1862 0.4856 0.0808  0.0558  0.0694  331 ALA A CA  
2616 C C   . ALA A 351 ? 0.5020 0.1391 0.4609 0.0320  0.0172  0.1136  331 ALA A C   
2617 O O   . ALA A 351 ? 0.4893 0.2406 0.4606 0.0299  0.0155  0.0523  331 ALA A O   
2618 C CB  . ALA A 351 ? 0.4853 0.1494 0.5353 0.0969  0.0487  0.0646  331 ALA A CB  
2619 N N   . ALA A 352 ? 0.5039 0.1221 0.4374 0.0258  0.0085  0.0959  332 ALA A N   
2620 C CA  . ALA A 352 ? 0.4795 0.1435 0.4360 0.0313  0.0203  0.0850  332 ALA A CA  
2621 C C   . ALA A 352 ? 0.4375 0.2414 0.4336 0.0420  0.0099  0.0699  332 ALA A C   
2622 O O   . ALA A 352 ? 0.4449 0.2835 0.4152 0.0566  -0.0317 0.0896  332 ALA A O   
2623 C CB  . ALA A 352 ? 0.5248 0.1624 0.4210 -0.0031 0.0068  0.0905  332 ALA A CB  
2624 N N   . PRO A 353 ? 0.4311 0.2339 0.4691 0.0537  0.0246  0.0676  333 PRO A N   
2625 C CA  . PRO A 353 ? 0.4421 0.2250 0.4798 0.0634  0.0175  0.0933  333 PRO A CA  
2626 C C   . PRO A 353 ? 0.4599 0.2060 0.4802 0.0472  0.0079  0.1472  333 PRO A C   
2627 O O   . PRO A 353 ? 0.4597 0.2055 0.4423 0.0844  -0.0053 0.1526  333 PRO A O   
2628 C CB  . PRO A 353 ? 0.4639 0.2010 0.4953 0.0352  0.0304  0.0621  333 PRO A CB  
2629 C CG  . PRO A 353 ? 0.4861 0.2344 0.4873 0.0351  0.0354  0.0472  333 PRO A CG  
2630 C CD  . PRO A 353 ? 0.4837 0.2352 0.4869 0.0402  0.0207  0.0589  333 PRO A CD  
2631 N N   . ARG A 354 ? 0.4416 0.3230 0.5006 0.0505  0.0261  0.1273  334 ARG A N   
2632 C CA  . ARG A 354 ? 0.4692 0.3544 0.4738 0.0966  0.0232  0.1343  334 ARG A CA  
2633 C C   . ARG A 354 ? 0.4899 0.3553 0.4854 0.0820  0.0246  0.1331  334 ARG A C   
2634 O O   . ARG A 354 ? 0.5408 0.2472 0.5453 0.0943  0.0473  0.1421  334 ARG A O   
2635 C CB  . ARG A 354 ? 0.5054 0.5016 0.4785 0.1052  -0.0117 0.1442  334 ARG A CB  
2636 C CG  . ARG A 354 ? 0.5729 0.5635 0.5086 0.1045  0.0084  0.1109  334 ARG A CG  
2637 C CD  . ARG A 354 ? 0.5473 0.5521 0.5137 0.1088  0.0037  0.1033  334 ARG A CD  
2638 N NE  . ARG A 354 ? 0.5332 0.5450 0.5220 0.1210  0.0019  0.0955  334 ARG A NE  
2639 C CZ  . ARG A 354 ? 0.5147 0.5269 0.5273 0.1228  0.0001  0.0871  334 ARG A CZ  
2640 N NH1 . ARG A 354 ? 0.4959 0.5277 0.5341 0.1305  -0.0073 0.0830  334 ARG A NH1 
2641 N NH2 . ARG A 354 ? 0.5157 0.5210 0.5305 0.1190  0.0065  0.0931  334 ARG A NH2 
2642 N N   . CYS A 355 ? 0.4357 0.3295 0.4198 0.0787  0.0088  0.1372  335 CYS A N   
2643 C CA  . CYS A 355 ? 0.4356 0.3030 0.4870 0.0993  0.0461  0.0973  335 CYS A CA  
2644 C C   . CYS A 355 ? 0.4442 0.2789 0.4502 0.1123  0.0303  0.0839  335 CYS A C   
2645 O O   . CYS A 355 ? 0.4741 0.2062 0.5026 0.0605  0.0069  0.1217  335 CYS A O   
2646 C CB  . CYS A 355 ? 0.4799 0.3046 0.5175 0.1502  0.0344  0.1169  335 CYS A CB  
2647 S SG  . CYS A 355 ? 0.5504 0.3154 0.6445 0.1556  0.0356  0.1474  335 CYS A SG  
2648 N N   . MET A 356 ? 0.4572 0.2286 0.4613 0.1034  0.0428  0.0883  336 MET A N   
2649 C CA  . MET A 356 ? 0.4993 0.1725 0.4820 0.0889  0.0258  0.0830  336 MET A CA  
2650 C C   . MET A 356 ? 0.5732 0.1989 0.5315 0.0600  0.0725  0.0910  336 MET A C   
2651 O O   . MET A 356 ? 0.5259 0.1482 0.5482 0.0365  0.0402  0.0272  336 MET A O   
2652 C CB  . MET A 356 ? 0.4951 0.2093 0.5033 0.0426  0.0266  0.0825  336 MET A CB  
2653 C CG  . MET A 356 ? 0.5098 0.2008 0.5180 0.0618  0.0100  0.0517  336 MET A CG  
2654 S SD  . MET A 356 ? 0.5100 0.1686 0.5522 0.0587  -0.0201 0.0780  336 MET A SD  
2655 C CE  . MET A 356 ? 0.5021 0.2400 0.5459 0.0373  -0.0377 0.0254  336 MET A CE  
2656 N N   . ALA A 357 ? 0.5883 0.2679 0.4852 0.0885  0.1167  0.1088  337 ALA A N   
2657 C CA  . ALA A 357 ? 0.6231 0.2578 0.4995 0.1350  0.1103  0.0907  337 ALA A CA  
2658 C C   . ALA A 357 ? 0.6177 0.2098 0.4924 0.0758  0.1052  0.0744  337 ALA A C   
2659 O O   . ALA A 357 ? 0.7130 0.1546 0.5666 0.0703  0.0365  0.0667  337 ALA A O   
2660 C CB  . ALA A 357 ? 0.6500 0.2159 0.5530 0.1837  0.1274  0.0628  337 ALA A CB  
2661 N N   . ASP A 358 ? 0.5906 0.2212 0.4641 0.1271  0.0666  0.0940  338 ASP A N   
2662 C CA  . ASP A 358 ? 0.5563 0.1860 0.4658 0.0854  0.0791  0.1272  338 ASP A CA  
2663 C C   . ASP A 358 ? 0.5554 0.2892 0.4614 0.0776  0.0822  0.1313  338 ASP A C   
2664 O O   . ASP A 358 ? 0.6402 0.2313 0.4246 0.0881  0.0972  0.1045  338 ASP A O   
2665 C CB  . ASP A 358 ? 0.5939 0.4094 0.5540 0.0808  0.0516  0.1192  338 ASP A CB  
2666 C CG  . ASP A 358 ? 0.6074 0.5298 0.6234 0.0936  -0.0009 0.1098  338 ASP A CG  
2667 O OD1 . ASP A 358 ? 0.7093 0.6062 0.6894 0.2124  -0.0034 0.0449  338 ASP A OD1 
2668 O OD2 . ASP A 358 ? 0.5606 0.8117 0.6664 0.0471  -0.0482 0.1443  338 ASP A OD2 
2669 N N   . ALA A 359 ? 0.4598 0.2629 0.4653 0.1089  0.0520  0.0947  339 ALA A N   
2670 C CA  . ALA A 359 ? 0.4930 0.1782 0.5004 0.0805  0.0539  0.0967  339 ALA A CA  
2671 C C   . ALA A 359 ? 0.4990 0.1720 0.4882 0.0689  0.0343  0.0729  339 ALA A C   
2672 O O   . ALA A 359 ? 0.4809 0.1699 0.4721 0.0643  0.0505  0.0901  339 ALA A O   
2673 C CB  . ALA A 359 ? 0.4625 0.1846 0.4958 0.0778  0.0390  0.0993  339 ALA A CB  
2674 N N   . ARG A 360 ? 0.5054 0.2051 0.4636 0.0299  0.0389  0.0418  340 ARG A N   
2675 C CA  . ARG A 360 ? 0.4944 0.2518 0.4760 0.0232  0.0548  0.0414  340 ARG A CA  
2676 C C   . ARG A 360 ? 0.4527 0.2452 0.4273 0.0203  0.0316  0.0560  340 ARG A C   
2677 O O   . ARG A 360 ? 0.4548 0.2115 0.4601 -0.0277 0.0806  0.0329  340 ARG A O   
2678 C CB  . ARG A 360 ? 0.5329 0.2388 0.4949 -0.0355 0.0505  -0.0002 340 ARG A CB  
2679 C CG  . ARG A 360 ? 0.5735 0.2894 0.5229 -0.0197 0.0195  -0.0018 340 ARG A CG  
2680 C CD  . ARG A 360 ? 0.5797 0.2969 0.5238 0.0169  0.0429  -0.0202 340 ARG A CD  
2681 N NE  . ARG A 360 ? 0.6430 0.3695 0.5346 0.0370  0.0240  -0.0126 340 ARG A NE  
2682 C CZ  . ARG A 360 ? 0.6725 0.3481 0.5802 0.0786  0.0438  -0.0191 340 ARG A CZ  
2683 N NH1 . ARG A 360 ? 0.7627 0.3594 0.6473 0.0570  0.0504  -0.0839 340 ARG A NH1 
2684 N NH2 . ARG A 360 ? 0.7135 0.3102 0.5068 0.0669  0.0133  -0.0117 340 ARG A NH2 
2685 N N   . PRO A 361 ? 0.4717 0.2532 0.4619 0.0639  0.0414  0.1054  341 PRO A N   
2686 C CA  . PRO A 361 ? 0.4660 0.2582 0.4457 0.1080  0.0339  0.0665  341 PRO A CA  
2687 C C   . PRO A 361 ? 0.4439 0.2478 0.4569 0.1063  0.0325  0.0849  341 PRO A C   
2688 O O   . PRO A 361 ? 0.4678 0.2410 0.3992 0.0768  0.0427  0.0778  341 PRO A O   
2689 C CB  . PRO A 361 ? 0.5297 0.3319 0.3738 0.0493  0.0007  0.1556  341 PRO A CB  
2690 C CG  . PRO A 361 ? 0.4685 0.3060 0.4512 0.0655  0.0223  0.1080  341 PRO A CG  
2691 C CD  . PRO A 361 ? 0.4611 0.3685 0.4590 0.0613  0.0480  0.0681  341 PRO A CD  
2692 N N   . PHE A 362 ? 0.4224 0.2967 0.4443 0.0879  0.0511  0.0696  342 PHE A N   
2693 C CA  . PHE A 362 ? 0.4652 0.2586 0.4548 0.0667  0.0352  0.0680  342 PHE A CA  
2694 C C   . PHE A 362 ? 0.4708 0.2919 0.4004 0.0566  0.0462  0.0780  342 PHE A C   
2695 O O   . PHE A 362 ? 0.4891 0.2595 0.3681 0.0676  0.0291  0.0484  342 PHE A O   
2696 C CB  . PHE A 362 ? 0.4735 0.2702 0.4280 0.0642  0.0432  0.0361  342 PHE A CB  
2697 C CG  . PHE A 362 ? 0.5206 0.2647 0.4419 0.0715  0.0472  0.0535  342 PHE A CG  
2698 C CD1 . PHE A 362 ? 0.5192 0.2393 0.4608 0.0753  0.0398  0.0602  342 PHE A CD1 
2699 C CD2 . PHE A 362 ? 0.5252 0.2581 0.3965 0.0821  0.0200  0.0382  342 PHE A CD2 
2700 C CE1 . PHE A 362 ? 0.5385 0.2525 0.4430 0.0538  0.0319  0.0261  342 PHE A CE1 
2701 C CE2 . PHE A 362 ? 0.4729 0.2012 0.4430 0.0246  0.0390  0.0277  342 PHE A CE2 
2702 C CZ  . PHE A 362 ? 0.5336 0.2538 0.4420 0.0384  -0.0048 0.0426  342 PHE A CZ  
2703 N N   . MET A 363 ? 0.4636 0.2320 0.3860 0.0700  0.0368  0.0653  343 MET A N   
2704 C CA  . MET A 363 ? 0.4658 0.1933 0.3733 0.0752  0.0371  0.0681  343 MET A CA  
2705 C C   . MET A 363 ? 0.4741 0.1695 0.3928 0.0687  0.0190  0.0777  343 MET A C   
2706 O O   . MET A 363 ? 0.4622 0.2047 0.4078 0.0753  0.0194  0.0636  343 MET A O   
2707 C CB  . MET A 363 ? 0.4482 0.1613 0.3596 0.0796  0.0400  0.0786  343 MET A CB  
2708 C CG  . MET A 363 ? 0.4402 0.1385 0.3347 0.1031  0.0482  0.0686  343 MET A CG  
2709 S SD  . MET A 363 ? 0.4235 0.1022 0.2935 0.0757  0.0494  0.1056  343 MET A SD  
2710 C CE  . MET A 363 ? 0.4339 0.0797 0.2564 0.0750  0.0230  0.1264  343 MET A CE  
2711 N N   . ALA A 364 ? 0.4879 0.1576 0.4071 0.0649  0.0209  0.0591  344 ALA A N   
2712 C CA  . ALA A 364 ? 0.4975 0.2051 0.4367 0.0517  0.0031  0.0723  344 ALA A CA  
2713 C C   . ALA A 364 ? 0.4421 0.1674 0.4412 0.0612  -0.0147 0.0779  344 ALA A C   
2714 O O   . ALA A 364 ? 0.4424 0.2944 0.4994 0.0825  -0.0027 0.0481  344 ALA A O   
2715 C CB  . ALA A 364 ? 0.4656 0.1870 0.4653 0.0407  -0.0071 0.0543  344 ALA A CB  
2716 N N   . PHE A 365 ? 0.4997 0.1961 0.4754 0.0243  0.0008  -0.0081 345 PHE A N   
2717 C CA  . PHE A 365 ? 0.4887 0.2944 0.4471 0.0534  0.0278  0.0118  345 PHE A CA  
2718 C C   . PHE A 365 ? 0.4741 0.2545 0.4699 0.0299  0.0470  0.0286  345 PHE A C   
2719 O O   . PHE A 365 ? 0.4462 0.2337 0.4499 0.0058  0.0488  0.0335  345 PHE A O   
2720 C CB  . PHE A 365 ? 0.5237 0.3778 0.4588 0.0519  0.0184  0.0175  345 PHE A CB  
2721 C CG  . PHE A 365 ? 0.5538 0.4043 0.4455 0.0736  0.0130  -0.0103 345 PHE A CG  
2722 C CD1 . PHE A 365 ? 0.5293 0.4370 0.4800 0.0481  0.0328  -0.0385 345 PHE A CD1 
2723 C CD2 . PHE A 365 ? 0.5284 0.4579 0.4378 0.0318  -0.0216 -0.0232 345 PHE A CD2 
2724 C CE1 . PHE A 365 ? 0.5406 0.4629 0.4752 0.0741  0.0435  -0.0332 345 PHE A CE1 
2725 C CE2 . PHE A 365 ? 0.5549 0.4295 0.4844 0.0739  -0.0033 -0.0300 345 PHE A CE2 
2726 C CZ  . PHE A 365 ? 0.5323 0.4784 0.4541 0.0706  0.0284  -0.0734 345 PHE A CZ  
2727 N N   . MET A 366 ? 0.4401 0.2245 0.4829 0.0207  0.0411  0.0321  346 MET A N   
2728 C CA  . MET A 366 ? 0.4491 0.2125 0.4994 0.0280  0.0287  0.0328  346 MET A CA  
2729 C C   . MET A 366 ? 0.4729 0.2361 0.4848 0.0367  0.0361  0.0130  346 MET A C   
2730 O O   . MET A 366 ? 0.4527 0.2605 0.5122 0.0701  0.0235  0.0177  346 MET A O   
2731 C CB  . MET A 366 ? 0.4426 0.1691 0.5261 0.0345  0.0072  0.0433  346 MET A CB  
2732 C CG  . MET A 366 ? 0.5120 0.2015 0.5350 0.0658  -0.0033 0.0052  346 MET A CG  
2733 S SD  . MET A 366 ? 0.5581 0.2967 0.5077 0.0515  0.0085  0.0132  346 MET A SD  
2734 C CE  . MET A 366 ? 0.5022 0.2566 0.4395 0.0659  -0.0397 0.0189  346 MET A CE  
2735 N N   . GLU A 367 ? 0.4879 0.2449 0.4408 0.0329  0.0304  -0.0153 347 GLU A N   
2736 C CA  . GLU A 367 ? 0.4736 0.3415 0.4732 0.0225  0.0330  -0.0004 347 GLU A CA  
2737 C C   . GLU A 367 ? 0.4698 0.3266 0.4851 0.0006  0.0414  0.0501  347 GLU A C   
2738 O O   . GLU A 367 ? 0.4539 0.2324 0.4909 -0.0049 0.0622  -0.0226 347 GLU A O   
2739 C CB  . GLU A 367 ? 0.4599 0.3479 0.4327 0.0136  0.0382  -0.0215 347 GLU A CB  
2740 C CG  . GLU A 367 ? 0.4956 0.3449 0.4543 -0.0038 0.0259  -0.0002 347 GLU A CG  
2741 C CD  . GLU A 367 ? 0.5049 0.2719 0.4753 0.0151  0.0319  0.0160  347 GLU A CD  
2742 O OE1 . GLU A 367 ? 0.5259 0.2940 0.4618 0.0259  0.0056  0.0353  347 GLU A OE1 
2743 O OE2 . GLU A 367 ? 0.5640 0.2182 0.5411 0.0063  -0.0195 0.0467  347 GLU A OE2 
2744 N N   . ALA A 368 ? 0.4627 0.2579 0.5138 0.0299  -0.0103 0.0570  348 ALA A N   
2745 C CA  . ALA A 368 ? 0.4753 0.2269 0.5274 0.0353  0.0327  0.0490  348 ALA A CA  
2746 C C   . ALA A 368 ? 0.4985 0.3164 0.4740 0.0095  0.0541  0.0307  348 ALA A C   
2747 O O   . ALA A 368 ? 0.5191 0.3112 0.5506 0.0067  0.0998  -0.0446 348 ALA A O   
2748 C CB  . ALA A 368 ? 0.4852 0.2810 0.5077 0.0515  -0.0460 0.1040  348 ALA A CB  
2749 N N   . GLU A 369 ? 0.4808 0.2493 0.4168 0.0246  0.0562  0.0595  349 GLU A N   
2750 C CA  . GLU A 369 ? 0.5687 0.2557 0.4584 0.0110  0.0347  0.0392  349 GLU A CA  
2751 C C   . GLU A 369 ? 0.6198 0.2660 0.4803 0.0200  0.0459  0.0189  349 GLU A C   
2752 O O   . GLU A 369 ? 0.6414 0.3356 0.4669 0.0094  0.0365  0.0153  349 GLU A O   
2753 C CB  . GLU A 369 ? 0.6577 0.3591 0.4369 -0.0081 0.0387  0.0786  349 GLU A CB  
2754 C CG  . GLU A 369 ? 0.7106 0.3222 0.5156 0.0497  -0.0061 0.0697  349 GLU A CG  
2755 C CD  . GLU A 369 ? 0.7936 0.4358 0.5386 0.0521  -0.0162 0.0445  349 GLU A CD  
2756 O OE1 . GLU A 369 ? 0.8373 0.4772 0.5502 0.0366  0.0054  0.0189  349 GLU A OE1 
2757 O OE2 . GLU A 369 ? 0.7790 0.4572 0.5945 0.0515  -0.0314 0.0323  349 GLU A OE2 
2758 N N   . GLY A 370 ? 0.5905 0.1928 0.5043 -0.0093 0.0606  -0.0243 350 GLY A N   
2759 C CA  . GLY A 370 ? 0.5781 0.2091 0.5605 -0.0091 0.0514  0.0618  350 GLY A CA  
2760 C C   . GLY A 370 ? 0.5768 0.2739 0.6215 0.0174  0.0696  -0.0397 350 GLY A C   
2761 O O   . GLY A 370 ? 0.6175 0.3405 0.6004 0.0149  0.1054  -0.1171 350 GLY A O   
2762 N N   . PRO A 371 ? 0.5452 0.2433 0.6118 -0.0097 0.0003  0.0214  351 PRO A N   
2763 C CA  . PRO A 371 ? 0.5526 0.2862 0.5693 -0.0012 0.0051  0.0185  351 PRO A CA  
2764 C C   . PRO A 371 ? 0.5694 0.3333 0.5342 0.0297  0.0278  0.0226  351 PRO A C   
2765 O O   . PRO A 371 ? 0.5994 0.3305 0.4764 0.1103  0.0893  0.0353  351 PRO A O   
2766 C CB  . PRO A 371 ? 0.5364 0.2556 0.5719 0.0277  0.0125  -0.0002 351 PRO A CB  
2767 C CG  . PRO A 371 ? 0.5279 0.1973 0.6275 0.0006  -0.0205 0.0133  351 PRO A CG  
2768 C CD  . PRO A 371 ? 0.5245 0.2144 0.6519 0.0011  -0.0177 -0.0040 351 PRO A CD  
2769 N N   . ILE A 372 ? 0.5494 0.2431 0.4942 0.0160  0.0277  0.0351  352 ILE A N   
2770 C CA  . ILE A 372 ? 0.5293 0.2595 0.5061 0.0134  0.0256  0.0269  352 ILE A CA  
2771 C C   . ILE A 372 ? 0.5190 0.1455 0.5212 -0.0097 0.0125  0.0471  352 ILE A C   
2772 O O   . ILE A 372 ? 0.5896 0.2092 0.5400 0.0360  0.0422  -0.0532 352 ILE A O   
2773 C CB  . ILE A 372 ? 0.5388 0.2859 0.5580 -0.0030 0.0280  0.0275  352 ILE A CB  
2774 C CG1 . ILE A 372 ? 0.5416 0.2654 0.6420 -0.0104 0.0430  -0.0461 352 ILE A CG1 
2775 C CG2 . ILE A 372 ? 0.6035 0.2403 0.5887 0.0194  0.0406  0.0796  352 ILE A CG2 
2776 C CD1 . ILE A 372 ? 0.5028 0.2943 0.6724 -0.0324 0.0571  -0.0570 352 ILE A CD1 
2777 N N   . ASN A 373 ? 0.4600 0.1881 0.4524 -0.0126 -0.0031 0.0791  353 ASN A N   
2778 C CA  . ASN A 373 ? 0.4088 0.1561 0.3980 0.0213  -0.0079 0.0497  353 ASN A CA  
2779 C C   . ASN A 373 ? 0.4043 0.1284 0.3214 -0.0059 -0.0115 0.0796  353 ASN A C   
2780 O O   . ASN A 373 ? 0.4431 0.0922 0.3321 0.0080  -0.0049 0.0642  353 ASN A O   
2781 C CB  . ASN A 373 ? 0.3569 0.2312 0.4027 -0.0209 -0.0119 0.0890  353 ASN A CB  
2782 C CG  . ASN A 373 ? 0.3300 0.1937 0.3629 -0.0078 0.0189  0.0328  353 ASN A CG  
2783 O OD1 . ASN A 373 ? 0.3320 0.1443 0.3971 -0.0404 0.0106  0.0437  353 ASN A OD1 
2784 N ND2 . ASN A 373 ? 0.3802 0.2420 0.3431 0.0294  0.0131  0.0045  353 ASN A ND2 
2785 N N   . LEU A 374 ? 0.3757 0.1703 0.3128 0.0064  0.0122  0.0813  354 LEU A N   
2786 C CA  . LEU A 374 ? 0.3788 0.1579 0.2828 0.0116  -0.0222 0.0440  354 LEU A CA  
2787 C C   . LEU A 374 ? 0.4027 0.1835 0.2763 -0.0084 -0.0190 0.0525  354 LEU A C   
2788 O O   . LEU A 374 ? 0.3929 0.1748 0.2785 0.0114  -0.0059 0.0480  354 LEU A O   
2789 C CB  . LEU A 374 ? 0.4009 0.1633 0.3051 0.0178  0.0013  0.0503  354 LEU A CB  
2790 C CG  . LEU A 374 ? 0.3813 0.1325 0.3246 0.0017  0.0096  0.0281  354 LEU A CG  
2791 C CD1 . LEU A 374 ? 0.4200 0.0714 0.3417 0.0042  -0.0090 0.0085  354 LEU A CD1 
2792 C CD2 . LEU A 374 ? 0.4306 0.1140 0.3525 -0.0453 0.0042  0.0260  354 LEU A CD2 
2793 N N   . CYS A 375 ? 0.4086 0.1857 0.2852 -0.0203 -0.0357 0.0627  355 CYS A N   
2794 C CA  . CYS A 375 ? 0.3888 0.2009 0.2813 0.0057  -0.0384 0.0420  355 CYS A CA  
2795 C C   . CYS A 375 ? 0.3526 0.1541 0.2703 -0.0086 -0.0127 0.0358  355 CYS A C   
2796 O O   . CYS A 375 ? 0.3774 0.1359 0.2681 0.0084  -0.0145 0.0554  355 CYS A O   
2797 C CB  . CYS A 375 ? 0.4024 0.2346 0.3283 -0.0132 -0.0416 0.0088  355 CYS A CB  
2798 S SG  . CYS A 375 ? 0.4135 0.2999 0.4343 0.0656  -0.0532 -0.0364 355 CYS A SG  
2799 N N   . SER A 376 ? 0.3732 0.1379 0.2727 0.0275  -0.0169 0.0434  356 SER A N   
2800 C CA  . SER A 376 ? 0.3233 0.1262 0.2888 -0.0004 -0.0236 0.0639  356 SER A CA  
2801 C C   . SER A 376 ? 0.3096 0.1398 0.2776 0.0017  -0.0105 0.0373  356 SER A C   
2802 O O   . SER A 376 ? 0.3206 0.1845 0.2914 -0.0221 -0.0257 0.0618  356 SER A O   
2803 C CB  . SER A 376 ? 0.3639 0.1235 0.3370 0.0213  -0.0124 0.0414  356 SER A CB  
2804 O OG  . SER A 376 ? 0.3564 0.1012 0.3158 0.0023  -0.0171 0.0376  356 SER A OG  
2805 N N   . SER A 377 ? 0.3226 0.1482 0.2735 -0.0056 -0.0150 0.0468  357 SER A N   
2806 C CA  . SER A 377 ? 0.3062 0.1041 0.2686 -0.0003 -0.0061 0.0539  357 SER A CA  
2807 C C   . SER A 377 ? 0.3322 0.1061 0.2452 0.0082  -0.0232 0.0515  357 SER A C   
2808 O O   . SER A 377 ? 0.3749 0.1119 0.2423 -0.0018 -0.0145 0.0399  357 SER A O   
2809 C CB  . SER A 377 ? 0.3227 0.1913 0.2961 -0.0022 0.0060  0.0457  357 SER A CB  
2810 O OG  . SER A 377 ? 0.3374 0.2075 0.3575 -0.0097 0.0305  0.0356  357 SER A OG  
2811 N N   . ASN A 378 ? 0.3487 0.1538 0.2253 0.0013  -0.0165 0.0565  358 ASN A N   
2812 C CA  . ASN A 378 ? 0.3232 0.1656 0.2313 0.0049  -0.0440 0.0360  358 ASN A CA  
2813 C C   . ASN A 378 ? 0.3222 0.1487 0.2462 0.0102  -0.0136 0.0342  358 ASN A C   
2814 O O   . ASN A 378 ? 0.3751 0.1215 0.2844 0.0072  -0.0280 0.0364  358 ASN A O   
2815 C CB  . ASN A 378 ? 0.3214 0.1684 0.2580 -0.0091 -0.0121 0.0202  358 ASN A CB  
2816 C CG  . ASN A 378 ? 0.3309 0.1912 0.2700 0.0033  0.0104  0.0530  358 ASN A CG  
2817 O OD1 . ASN A 378 ? 0.3818 0.1565 0.2523 -0.0119 0.0028  0.0241  358 ASN A OD1 
2818 N ND2 . ASN A 378 ? 0.3444 0.1655 0.3015 -0.0052 0.0174  0.0520  358 ASN A ND2 
2819 N N   . ILE A 379 ? 0.3181 0.1389 0.2319 -0.0254 -0.0122 0.0262  359 ILE A N   
2820 C CA  . ILE A 379 ? 0.3218 0.1546 0.2776 -0.0221 -0.0059 -0.0001 359 ILE A CA  
2821 C C   . ILE A 379 ? 0.3286 0.1486 0.2763 -0.0278 -0.0042 0.0228  359 ILE A C   
2822 O O   . ILE A 379 ? 0.3709 0.1836 0.3403 -0.0599 -0.0084 -0.0280 359 ILE A O   
2823 C CB  . ILE A 379 ? 0.3414 0.2025 0.2997 -0.0075 -0.0023 0.0050  359 ILE A CB  
2824 C CG1 . ILE A 379 ? 0.3537 0.1732 0.3027 0.0120  0.0036  0.0186  359 ILE A CG1 
2825 C CG2 . ILE A 379 ? 0.3304 0.1813 0.2747 -0.0155 0.0074  0.0059  359 ILE A CG2 
2826 C CD1 . ILE A 379 ? 0.3358 0.1307 0.3166 0.0260  0.0140  0.0140  359 ILE A CD1 
2827 N N   . GLY A 380 ? 0.3640 0.1093 0.2842 -0.0233 -0.0072 0.0010  360 GLY A N   
2828 C CA  . GLY A 380 ? 0.3365 0.1560 0.2742 -0.0141 -0.0084 -0.0027 360 GLY A CA  
2829 C C   . GLY A 380 ? 0.3393 0.1218 0.2707 -0.0367 -0.0063 -0.0123 360 GLY A C   
2830 O O   . GLY A 380 ? 0.3759 0.1724 0.2780 -0.0339 -0.0054 0.0120  360 GLY A O   
2831 N N   . ARG A 381 ? 0.3381 0.1301 0.2517 -0.0171 0.0082  -0.0234 361 ARG A N   
2832 C CA  . ARG A 381 ? 0.3353 0.1488 0.2646 0.0085  -0.0034 -0.0008 361 ARG A CA  
2833 C C   . ARG A 381 ? 0.3423 0.1214 0.2665 0.0023  -0.0086 -0.0005 361 ARG A C   
2834 O O   . ARG A 381 ? 0.3560 0.1522 0.2771 -0.0047 -0.0201 -0.0165 361 ARG A O   
2835 C CB  . ARG A 381 ? 0.3266 0.2051 0.2902 0.0091  0.0379  -0.0325 361 ARG A CB  
2836 C CG  . ARG A 381 ? 0.3650 0.1889 0.3366 0.0171  0.0318  -0.0141 361 ARG A CG  
2837 C CD  . ARG A 381 ? 0.3851 0.2547 0.3712 0.0491  0.0162  -0.0098 361 ARG A CD  
2838 N NE  . ARG A 381 ? 0.3782 0.3034 0.3547 0.0388  0.0221  -0.0484 361 ARG A NE  
2839 C CZ  . ARG A 381 ? 0.3840 0.4256 0.3841 -0.0073 0.0072  -0.0815 361 ARG A CZ  
2840 N NH1 . ARG A 381 ? 0.3821 0.4360 0.4220 -0.0283 0.0002  -0.0633 361 ARG A NH1 
2841 N NH2 . ARG A 381 ? 0.3820 0.5554 0.4039 0.0012  -0.0031 -0.0909 361 ARG A NH2 
2842 N N   . TYR A 382 ? 0.3230 0.1110 0.2779 0.0040  0.0003  -0.0321 362 TYR A N   
2843 C CA  . TYR A 382 ? 0.3264 0.1058 0.2608 0.0307  0.0080  -0.0237 362 TYR A CA  
2844 C C   . TYR A 382 ? 0.3279 0.1169 0.2914 0.0182  -0.0042 -0.0140 362 TYR A C   
2845 O O   . TYR A 382 ? 0.3294 0.0956 0.3080 0.0119  0.0020  -0.0067 362 TYR A O   
2846 C CB  . TYR A 382 ? 0.3211 0.0806 0.2395 0.0135  -0.0223 -0.0331 362 TYR A CB  
2847 C CG  . TYR A 382 ? 0.3223 0.1159 0.2442 0.0053  -0.0141 -0.0265 362 TYR A CG  
2848 C CD1 . TYR A 382 ? 0.3415 0.1403 0.2570 0.0280  -0.0029 0.0081  362 TYR A CD1 
2849 C CD2 . TYR A 382 ? 0.3314 0.1031 0.2490 0.0149  -0.0081 -0.0117 362 TYR A CD2 
2850 C CE1 . TYR A 382 ? 0.3347 0.1363 0.2906 0.0329  0.0090  -0.0328 362 TYR A CE1 
2851 C CE2 . TYR A 382 ? 0.3095 0.1740 0.2607 0.0115  0.0010  -0.0279 362 TYR A CE2 
2852 C CZ  . TYR A 382 ? 0.3163 0.1508 0.2822 0.0203  0.0043  -0.0187 362 TYR A CZ  
2853 O OH  . TYR A 382 ? 0.3139 0.1731 0.3677 0.0050  0.0312  -0.0420 362 TYR A OH  
2854 N N   . PRO A 383 ? 0.3801 0.0952 0.2699 0.0189  -0.0008 -0.0189 363 PRO A N   
2855 C CA  . PRO A 383 ? 0.3853 0.0844 0.2628 0.0174  -0.0154 -0.0118 363 PRO A CA  
2856 C C   . PRO A 383 ? 0.3403 0.1368 0.2678 -0.0008 -0.0046 -0.0449 363 PRO A C   
2857 O O   . PRO A 383 ? 0.3836 0.2207 0.2762 -0.0506 0.0179  -0.0187 363 PRO A O   
2858 C CB  . PRO A 383 ? 0.3894 0.1360 0.2417 0.0030  -0.0013 -0.0051 363 PRO A CB  
2859 C CG  . PRO A 383 ? 0.3819 0.1275 0.2485 -0.0162 -0.0207 -0.0261 363 PRO A CG  
2860 C CD  . PRO A 383 ? 0.3517 0.1082 0.2668 -0.0009 -0.0015 -0.0408 363 PRO A CD  
2861 N N   . PHE A 384 ? 0.3494 0.0831 0.2579 -0.0142 0.0018  -0.0293 364 PHE A N   
2862 C CA  . PHE A 384 ? 0.3381 0.0731 0.2745 0.0138  0.0080  -0.0113 364 PHE A CA  
2863 C C   . PHE A 384 ? 0.3359 0.0606 0.3065 -0.0039 0.0113  0.0085  364 PHE A C   
2864 O O   . PHE A 384 ? 0.3566 0.0509 0.3714 -0.0048 0.0131  0.0539  364 PHE A O   
2865 C CB  . PHE A 384 ? 0.3255 0.0759 0.2688 -0.0119 0.0018  -0.0133 364 PHE A CB  
2866 C CG  . PHE A 384 ? 0.3330 0.0639 0.2772 -0.0059 0.0137  -0.0188 364 PHE A CG  
2867 C CD1 . PHE A 384 ? 0.3153 0.1084 0.2655 0.0078  0.0038  -0.0073 364 PHE A CD1 
2868 C CD2 . PHE A 384 ? 0.3088 0.0668 0.2715 -0.0078 -0.0052 0.0087  364 PHE A CD2 
2869 C CE1 . PHE A 384 ? 0.3274 0.0968 0.2565 0.0147  0.0206  0.0019  364 PHE A CE1 
2870 C CE2 . PHE A 384 ? 0.3359 0.0598 0.2800 -0.0310 0.0096  -0.0063 364 PHE A CE2 
2871 C CZ  . PHE A 384 ? 0.3505 0.0968 0.2681 0.0011  0.0231  0.0123  364 PHE A CZ  
2872 N N   . PRO A 385 ? 0.3314 0.0925 0.2989 -0.0114 -0.0133 0.0003  365 PRO A N   
2873 C CA  . PRO A 385 ? 0.3442 0.1095 0.3565 0.0219  0.0016  0.0084  365 PRO A CA  
2874 C C   . PRO A 385 ? 0.3502 0.1102 0.3295 0.0201  -0.0069 0.0224  365 PRO A C   
2875 O O   . PRO A 385 ? 0.3516 0.0665 0.3147 -0.0040 -0.0166 0.0330  365 PRO A O   
2876 C CB  . PRO A 385 ? 0.3689 0.1033 0.3741 -0.0280 -0.0125 0.0383  365 PRO A CB  
2877 C CG  . PRO A 385 ? 0.3531 0.0775 0.3617 -0.0364 -0.0097 0.0059  365 PRO A CG  
2878 C CD  . PRO A 385 ? 0.3447 0.0653 0.3094 -0.0281 0.0105  -0.0048 365 PRO A CD  
2879 N N   . GLU A 386 ? 0.3465 0.0679 0.3442 0.0082  -0.0043 0.0189  366 GLU A N   
2880 C CA  . GLU A 386 ? 0.3760 0.1404 0.3763 0.0211  -0.0019 0.0358  366 GLU A CA  
2881 C C   . GLU A 386 ? 0.3776 0.1139 0.3499 0.0131  -0.0201 0.0298  366 GLU A C   
2882 O O   . GLU A 386 ? 0.3932 0.0095 0.3810 -0.0016 -0.0262 0.0348  366 GLU A O   
2883 C CB  . GLU A 386 ? 0.3799 0.2181 0.3869 0.0407  0.0413  0.0311  366 GLU A CB  
2884 C CG  . GLU A 386 ? 0.4471 0.3177 0.4589 0.0561  0.0364  0.0102  366 GLU A CG  
2885 C CD  . GLU A 386 ? 0.4531 0.3404 0.5358 0.0546  0.0469  0.0164  366 GLU A CD  
2886 O OE1 . GLU A 386 ? 0.4155 0.3083 0.5462 0.0433  0.0580  0.0372  366 GLU A OE1 
2887 O OE2 . GLU A 386 ? 0.6330 0.4182 0.7034 -0.0095 0.0905  0.0309  366 GLU A OE2 
2888 N N   . ARG A 387 ? 0.3861 0.0786 0.3626 0.0016  -0.0175 0.0367  367 ARG A N   
2889 C CA  . ARG A 387 ? 0.3806 0.0572 0.3789 0.0002  -0.0122 0.0222  367 ARG A CA  
2890 C C   . ARG A 387 ? 0.4044 0.0761 0.3812 -0.0249 -0.0067 0.0496  367 ARG A C   
2891 O O   . ARG A 387 ? 0.4016 0.1101 0.3580 -0.0242 -0.0170 0.0399  367 ARG A O   
2892 C CB  . ARG A 387 ? 0.4134 0.0716 0.4356 -0.0034 -0.0156 0.0325  367 ARG A CB  
2893 C CG  . ARG A 387 ? 0.4373 0.1264 0.4954 -0.0108 -0.0071 0.0287  367 ARG A CG  
2894 C CD  . ARG A 387 ? 0.4623 0.1206 0.5079 -0.0026 -0.0215 0.0332  367 ARG A CD  
2895 N NE  . ARG A 387 ? 0.4970 0.2032 0.5694 -0.0059 -0.0311 0.0243  367 ARG A NE  
2896 C CZ  . ARG A 387 ? 0.5230 0.2371 0.5648 0.0054  -0.0512 0.0567  367 ARG A CZ  
2897 N NH1 . ARG A 387 ? 0.5261 0.2469 0.5442 -0.0199 -0.0604 0.0309  367 ARG A NH1 
2898 N NH2 . ARG A 387 ? 0.5459 0.2903 0.5796 -0.0138 -0.0345 0.0682  367 ARG A NH2 
2899 N N   . ILE A 388 ? 0.3824 0.0364 0.3810 -0.0101 0.0214  0.0443  368 ILE A N   
2900 C CA  . ILE A 388 ? 0.3586 0.0961 0.3589 -0.0190 -0.0021 0.0238  368 ILE A CA  
2901 C C   . ILE A 388 ? 0.3821 0.1092 0.3606 -0.0398 -0.0033 0.0361  368 ILE A C   
2902 O O   . ILE A 388 ? 0.4173 0.1559 0.3321 0.0021  0.0014  0.0671  368 ILE A O   
2903 C CB  . ILE A 388 ? 0.3515 0.1147 0.3755 -0.0127 0.0006  0.0145  368 ILE A CB  
2904 C CG1 . ILE A 388 ? 0.3546 0.0949 0.3658 -0.0175 0.0151  0.0213  368 ILE A CG1 
2905 C CG2 . ILE A 388 ? 0.3661 0.1631 0.3730 -0.0080 -0.0066 0.0345  368 ILE A CG2 
2906 C CD1 . ILE A 388 ? 0.3818 0.0982 0.3842 0.0001  0.0212  0.0175  368 ILE A CD1 
2907 N N   . GLY A 389 ? 0.4327 0.1269 0.3868 -0.0695 -0.0112 0.0328  369 GLY A N   
2908 C CA  . GLY A 389 ? 0.4492 0.1847 0.4127 -0.0758 -0.0202 0.0573  369 GLY A CA  
2909 C C   . GLY A 389 ? 0.4250 0.1457 0.4498 -0.0502 -0.0034 0.0689  369 GLY A C   
2910 O O   . GLY A 389 ? 0.4385 0.0818 0.5628 -0.0173 0.0255  0.0890  369 GLY A O   
2911 N N   . ALA A 390 ? 0.4420 0.1130 0.4491 -0.0482 -0.0110 0.1280  370 ALA A N   
2912 C CA  . ALA A 390 ? 0.4341 0.1663 0.4426 -0.0509 -0.0355 0.1072  370 ALA A CA  
2913 C C   . ALA A 390 ? 0.3938 0.1716 0.4252 -0.0362 -0.0742 0.1089  370 ALA A C   
2914 O O   . ALA A 390 ? 0.4344 0.1526 0.5078 -0.0431 -0.0854 0.1468  370 ALA A O   
2915 C CB  . ALA A 390 ? 0.4701 0.2226 0.4737 -0.0605 -0.0444 0.1222  370 ALA A CB  
2916 N N   . LEU A 391 ? 0.3999 0.1619 0.3642 -0.0369 -0.0394 0.1052  371 LEU A N   
2917 C CA  . LEU A 391 ? 0.3468 0.1618 0.3704 -0.0155 -0.0296 0.0608  371 LEU A CA  
2918 C C   . LEU A 391 ? 0.3705 0.1473 0.3396 0.0147  -0.0362 0.0664  371 LEU A C   
2919 O O   . LEU A 391 ? 0.4036 0.1101 0.3578 -0.0156 -0.0100 0.0536  371 LEU A O   
2920 C CB  . LEU A 391 ? 0.3513 0.1107 0.3563 -0.0118 -0.0002 0.0500  371 LEU A CB  
2921 C CG  . LEU A 391 ? 0.3865 0.1479 0.3674 0.0016  -0.0017 0.0478  371 LEU A CG  
2922 C CD1 . LEU A 391 ? 0.4114 0.1257 0.3985 0.0069  0.0027  0.0508  371 LEU A CD1 
2923 C CD2 . LEU A 391 ? 0.3792 0.1685 0.3422 0.0039  0.0165  0.0452  371 LEU A CD2 
2924 N N   . ARG A 392 ? 0.3556 0.1108 0.3221 0.0232  -0.0339 0.0490  372 ARG A N   
2925 C CA  . ARG A 392 ? 0.3638 0.0637 0.3566 0.0150  -0.0241 0.0446  372 ARG A CA  
2926 C C   . ARG A 392 ? 0.3479 0.0665 0.3155 0.0162  -0.0096 0.0555  372 ARG A C   
2927 O O   . ARG A 392 ? 0.4079 0.1140 0.2896 0.0049  -0.0103 0.0500  372 ARG A O   
2928 C CB  . ARG A 392 ? 0.4324 0.1360 0.3905 0.0093  -0.0386 0.0545  372 ARG A CB  
2929 C CG  . ARG A 392 ? 0.4975 0.1412 0.4624 -0.0078 -0.0526 0.0303  372 ARG A CG  
2930 C CD  . ARG A 392 ? 0.5483 0.1659 0.5782 0.0530  -0.0862 0.0096  372 ARG A CD  
2931 N NE  . ARG A 392 ? 0.6935 0.2901 0.6584 0.0828  -0.1177 -0.0207 372 ARG A NE  
2932 C CZ  . ARG A 392 ? 0.7355 0.2510 0.6729 0.0834  -0.1383 0.0721  372 ARG A CZ  
2933 N NH1 . ARG A 392 ? 0.7217 0.4674 0.7440 -0.0480 -0.0913 0.0754  372 ARG A NH1 
2934 N NH2 . ARG A 392 ? 0.6999 0.2983 0.6452 0.1031  -0.1554 0.0338  372 ARG A NH2 
2935 N N   . LEU A 393 ? 0.3499 0.0259 0.3293 0.0189  -0.0162 0.0397  373 LEU A N   
2936 C CA  . LEU A 393 ? 0.3014 0.0263 0.3096 0.0250  -0.0141 0.0366  373 LEU A CA  
2937 C C   . LEU A 393 ? 0.3043 0.0949 0.3028 0.0260  -0.0086 0.0125  373 LEU A C   
2938 O O   . LEU A 393 ? 0.3182 0.0918 0.3095 0.0226  0.0313  0.0425  373 LEU A O   
2939 C CB  . LEU A 393 ? 0.3115 0.0571 0.3272 0.0096  -0.0180 0.0386  373 LEU A CB  
2940 C CG  . LEU A 393 ? 0.3084 0.0600 0.3439 0.0132  -0.0344 0.0422  373 LEU A CG  
2941 C CD1 . LEU A 393 ? 0.3170 0.1498 0.3593 0.0138  -0.0216 0.0436  373 LEU A CD1 
2942 C CD2 . LEU A 393 ? 0.3372 0.0684 0.4071 0.0067  -0.0247 0.0349  373 LEU A CD2 
2943 N N   . SER A 394 ? 0.2983 0.0947 0.2802 0.0027  -0.0231 0.0110  374 SER A N   
2944 C CA  . SER A 394 ? 0.3162 0.1000 0.2573 0.0176  -0.0109 0.0157  374 SER A CA  
2945 C C   . SER A 394 ? 0.3163 0.1166 0.2610 0.0197  -0.0078 0.0443  374 SER A C   
2946 O O   . SER A 394 ? 0.3256 0.1187 0.2456 -0.0057 0.0033  0.0406  374 SER A O   
2947 C CB  . SER A 394 ? 0.3193 0.1361 0.2860 -0.0136 -0.0066 0.0380  374 SER A CB  
2948 O OG  . SER A 394 ? 0.3359 0.1325 0.2798 0.0085  -0.0372 0.0346  374 SER A OG  
2949 N N   . ASP A 395 ? 0.2953 0.0587 0.2730 0.0072  -0.0165 0.0295  375 ASP A N   
2950 C CA  . ASP A 395 ? 0.2933 0.0526 0.2721 -0.0040 -0.0216 0.0387  375 ASP A CA  
2951 C C   . ASP A 395 ? 0.2887 0.0990 0.2460 0.0044  -0.0094 0.0153  375 ASP A C   
2952 O O   . ASP A 395 ? 0.3070 0.0732 0.2424 0.0105  -0.0014 0.0350  375 ASP A O   
2953 C CB  . ASP A 395 ? 0.3117 0.0369 0.2915 -0.0227 -0.0430 0.0661  375 ASP A CB  
2954 C CG  . ASP A 395 ? 0.3341 0.0978 0.3039 -0.0071 -0.0552 0.0575  375 ASP A CG  
2955 O OD1 . ASP A 395 ? 0.3246 0.1655 0.3767 0.0048  -0.0360 0.0251  375 ASP A OD1 
2956 O OD2 . ASP A 395 ? 0.3989 0.1197 0.3510 -0.0410 -0.0563 0.1026  375 ASP A OD2 
2957 N N   . ALA A 396 ? 0.2741 0.0866 0.2396 -0.0138 -0.0086 0.0240  376 ALA A N   
2958 C CA  . ALA A 396 ? 0.2973 0.0952 0.2553 -0.0043 0.0026  0.0205  376 ALA A CA  
2959 C C   . ALA A 396 ? 0.2989 0.0748 0.2575 0.0035  0.0147  0.0195  376 ALA A C   
2960 O O   . ALA A 396 ? 0.3048 0.0362 0.2709 0.0010  0.0204  0.0518  376 ALA A O   
2961 C CB  . ALA A 396 ? 0.3058 0.0683 0.2508 0.0139  -0.0160 0.0326  376 ALA A CB  
2962 N N   . GLN A 397 ? 0.2879 0.0798 0.2517 -0.0065 0.0043  0.0206  377 GLN A N   
2963 C CA  . GLN A 397 ? 0.2908 0.0942 0.2353 -0.0249 -0.0056 0.0208  377 GLN A CA  
2964 C C   . GLN A 397 ? 0.2903 0.0828 0.2230 -0.0139 0.0076  0.0143  377 GLN A C   
2965 O O   . GLN A 397 ? 0.3171 0.0323 0.2452 -0.0010 0.0006  0.0226  377 GLN A O   
2966 C CB  . GLN A 397 ? 0.3118 0.0541 0.2380 -0.0095 -0.0176 0.0402  377 GLN A CB  
2967 C CG  . GLN A 397 ? 0.3171 0.0171 0.2506 -0.0061 -0.0027 0.0512  377 GLN A CG  
2968 C CD  . GLN A 397 ? 0.3063 0.0737 0.2589 -0.0198 -0.0197 0.0377  377 GLN A CD  
2969 O OE1 . GLN A 397 ? 0.3090 0.0524 0.2849 -0.0329 -0.0224 0.0375  377 GLN A OE1 
2970 N NE2 . GLN A 397 ? 0.2927 0.1032 0.2771 -0.0050 -0.0631 0.0240  377 GLN A NE2 
2971 N N   . PHE A 398 ? 0.3024 0.0868 0.2482 0.0099  0.0040  0.0347  378 PHE A N   
2972 C CA  . PHE A 398 ? 0.2728 0.0680 0.2381 -0.0254 0.0087  0.0141  378 PHE A CA  
2973 C C   . PHE A 398 ? 0.2599 0.0809 0.2507 -0.0300 -0.0141 0.0241  378 PHE A C   
2974 O O   . PHE A 398 ? 0.2923 0.0936 0.2622 0.0067  0.0120  0.0274  378 PHE A O   
2975 C CB  . PHE A 398 ? 0.3076 0.0441 0.2496 -0.0059 0.0013  0.0200  378 PHE A CB  
2976 C CG  . PHE A 398 ? 0.3096 0.0664 0.2297 0.0079  0.0040  0.0129  378 PHE A CG  
2977 C CD1 . PHE A 398 ? 0.3581 0.0640 0.2519 -0.0162 -0.0022 -0.0194 378 PHE A CD1 
2978 C CD2 . PHE A 398 ? 0.3331 0.0891 0.2498 0.0221  0.0015  0.0226  378 PHE A CD2 
2979 C CE1 . PHE A 398 ? 0.3664 0.0990 0.2429 -0.0080 -0.0073 -0.0116 378 PHE A CE1 
2980 C CE2 . PHE A 398 ? 0.3526 0.1229 0.2556 0.0123  -0.0061 0.0350  378 PHE A CE2 
2981 C CZ  . PHE A 398 ? 0.3674 0.1214 0.2530 -0.0049 0.0078  0.0181  378 PHE A CZ  
2982 N N   . LEU A 399 ? 0.2733 0.1012 0.2584 -0.0157 0.0313  0.0300  379 LEU A N   
2983 C CA  . LEU A 399 ? 0.3193 0.0809 0.2704 -0.0082 0.0111  0.0421  379 LEU A CA  
2984 C C   . LEU A 399 ? 0.3203 0.1467 0.2564 -0.0200 0.0182  0.0543  379 LEU A C   
2985 O O   . LEU A 399 ? 0.3394 0.0644 0.2977 -0.0089 0.0159  0.0436  379 LEU A O   
2986 C CB  . LEU A 399 ? 0.3401 0.0882 0.2831 0.0003  -0.0144 0.0334  379 LEU A CB  
2987 C CG  . LEU A 399 ? 0.3591 0.1762 0.3195 -0.0198 0.0050  0.0075  379 LEU A CG  
2988 C CD1 . LEU A 399 ? 0.3900 0.1469 0.3632 -0.0110 -0.0121 0.0173  379 LEU A CD1 
2989 C CD2 . LEU A 399 ? 0.4332 0.1350 0.3596 -0.0479 0.0078  0.0529  379 LEU A CD2 
2990 N N   . THR A 400 ? 0.3341 0.1321 0.2830 -0.0096 -0.0113 0.0637  380 THR A N   
2991 C CA  . THR A 400 ? 0.3575 0.0953 0.3269 -0.0122 -0.0030 0.0120  380 THR A CA  
2992 C C   . THR A 400 ? 0.3385 0.0911 0.2901 -0.0091 0.0045  0.0357  380 THR A C   
2993 O O   . THR A 400 ? 0.3196 0.1199 0.3544 0.0016  0.0231  0.0265  380 THR A O   
2994 C CB  . THR A 400 ? 0.3754 0.0893 0.3631 0.0062  -0.0307 0.0213  380 THR A CB  
2995 O OG1 . THR A 400 ? 0.4040 0.1192 0.3977 0.0155  -0.0410 0.0345  380 THR A OG1 
2996 C CG2 . THR A 400 ? 0.4093 0.0375 0.3637 -0.0067 -0.0098 0.0330  380 THR A CG2 
2997 N N   . GLY A 401 ? 0.3323 0.0284 0.3152 -0.0386 0.0151  0.0364  381 GLY A N   
2998 C CA  . GLY A 401 ? 0.3493 0.0356 0.3123 -0.0227 0.0130  0.0089  381 GLY A CA  
2999 C C   . GLY A 401 ? 0.3580 0.0389 0.3197 -0.0201 0.0019  0.0016  381 GLY A C   
3000 O O   . GLY A 401 ? 0.3708 0.1060 0.3152 0.0052  -0.0174 0.0255  381 GLY A O   
3001 N N   . ILE A 402 ? 0.3746 0.0188 0.2953 -0.0002 0.0161  0.0205  382 ILE A N   
3002 C CA  . ILE A 402 ? 0.3716 0.1433 0.2973 0.0172  0.0092  0.0212  382 ILE A CA  
3003 C C   . ILE A 402 ? 0.3440 0.1301 0.3213 -0.0187 0.0058  0.0202  382 ILE A C   
3004 O O   . ILE A 402 ? 0.3684 0.0944 0.3528 -0.0006 -0.0013 0.0236  382 ILE A O   
3005 C CB  . ILE A 402 ? 0.3425 0.1808 0.3348 0.0291  0.0068  0.0461  382 ILE A CB  
3006 C CG1 . ILE A 402 ? 0.3539 0.1747 0.3261 0.0405  0.0008  0.0632  382 ILE A CG1 
3007 C CG2 . ILE A 402 ? 0.3180 0.2529 0.3504 0.0111  0.0113  0.0508  382 ILE A CG2 
3008 C CD1 . ILE A 402 ? 0.3698 0.1318 0.3559 0.0383  -0.0017 0.0698  382 ILE A CD1 
3009 N N   . SER A 403 ? 0.3619 0.1741 0.3238 0.0298  0.0049  0.0131  383 SER A N   
3010 C CA  . SER A 403 ? 0.3690 0.1501 0.3568 0.0427  -0.0009 0.0486  383 SER A CA  
3011 C C   . SER A 403 ? 0.3647 0.1688 0.3458 0.0299  -0.0058 0.0453  383 SER A C   
3012 O O   . SER A 403 ? 0.4002 0.0862 0.4007 0.0611  -0.0581 0.0399  383 SER A O   
3013 C CB  . SER A 403 ? 0.3275 0.1931 0.4001 0.0683  0.0203  0.0586  383 SER A CB  
3014 O OG  . SER A 403 ? 0.3322 0.2037 0.4444 0.0671  0.0230  0.1113  383 SER A OG  
3015 N N   . VAL A 404 ? 0.3903 0.1271 0.3602 0.0109  0.0139  0.0772  384 VAL A N   
3016 C CA  . VAL A 404 ? 0.3914 0.1249 0.3556 0.0113  -0.0083 0.0827  384 VAL A CA  
3017 C C   . VAL A 404 ? 0.3623 0.1365 0.3513 0.0150  0.0221  0.0810  384 VAL A C   
3018 O O   . VAL A 404 ? 0.4276 0.2147 0.3979 0.0126  0.0520  0.1210  384 VAL A O   
3019 C CB  . VAL A 404 ? 0.3956 0.1559 0.3470 0.0338  0.0216  0.0795  384 VAL A CB  
3020 C CG1 . VAL A 404 ? 0.4065 0.1843 0.3924 0.0552  0.0284  0.0674  384 VAL A CG1 
3021 C CG2 . VAL A 404 ? 0.3794 0.2412 0.3918 0.0294  -0.0032 0.1439  384 VAL A CG2 
3022 N N   . ASN A 405 ? 0.3789 0.1439 0.3532 0.0305  0.0081  0.0613  385 ASN A N   
3023 C CA  . ASN A 405 ? 0.4065 0.1107 0.3675 0.0029  0.0258  0.0800  385 ASN A CA  
3024 C C   . ASN A 405 ? 0.4301 0.1654 0.3764 0.0269  0.0088  0.0326  385 ASN A C   
3025 O O   . ASN A 405 ? 0.5127 0.1716 0.3889 0.0109  0.0158  0.0386  385 ASN A O   
3026 C CB  . ASN A 405 ? 0.4177 0.1356 0.4507 -0.0177 0.0195  0.0729  385 ASN A CB  
3027 C CG  . ASN A 405 ? 0.4445 0.2023 0.4908 -0.0082 0.0386  0.0543  385 ASN A CG  
3028 O OD1 . ASN A 405 ? 0.4389 0.2683 0.4705 0.0446  0.0411  0.0242  385 ASN A OD1 
3029 N ND2 . ASN A 405 ? 0.4844 0.1902 0.4424 -0.0151 0.0650  0.0344  385 ASN A ND2 
3030 N N   . GLY A 406 ? 0.4331 0.2386 0.2988 0.0488  0.0132  0.0431  386 GLY A N   
3031 C CA  . GLY A 406 ? 0.4495 0.1403 0.3347 0.0246  0.0116  0.0502  386 GLY A CA  
3032 C C   . GLY A 406 ? 0.4165 0.0879 0.3382 0.0140  0.0183  0.0839  386 GLY A C   
3033 O O   . GLY A 406 ? 0.4181 0.1637 0.3886 0.0761  0.0043  0.0369  386 GLY A O   
3034 N N   . TYR A 407 ? 0.4271 0.0772 0.3418 0.0319  0.0294  0.0513  387 TYR A N   
3035 C CA  . TYR A 407 ? 0.4367 0.0888 0.3312 0.0003  0.0099  0.0249  387 TYR A CA  
3036 C C   . TYR A 407 ? 0.4185 0.1425 0.3015 -0.0003 -0.0040 0.0287  387 TYR A C   
3037 O O   . TYR A 407 ? 0.4318 0.0163 0.3254 -0.0281 -0.0008 0.0511  387 TYR A O   
3038 C CB  . TYR A 407 ? 0.4892 0.0965 0.3543 -0.0027 0.0203  0.0336  387 TYR A CB  
3039 C CG  . TYR A 407 ? 0.5207 0.1131 0.3921 0.0096  0.0007  0.0412  387 TYR A CG  
3040 C CD1 . TYR A 407 ? 0.4961 0.0865 0.3707 0.0168  -0.0017 0.0257  387 TYR A CD1 
3041 C CD2 . TYR A 407 ? 0.6099 0.0180 0.4749 0.0653  0.0017  0.0354  387 TYR A CD2 
3042 C CE1 . TYR A 407 ? 0.5571 0.1433 0.4466 0.0647  -0.0054 0.0287  387 TYR A CE1 
3043 C CE2 . TYR A 407 ? 0.7166 0.0300 0.4996 0.0927  -0.0172 0.0731  387 TYR A CE2 
3044 C CZ  . TYR A 407 ? 0.6292 0.1229 0.4870 0.0750  -0.0113 0.0598  387 TYR A CZ  
3045 O OH  . TYR A 407 ? 0.6620 0.1659 0.5728 0.0973  -0.0834 -0.0030 387 TYR A OH  
3046 N N   . PHE A 408 ? 0.3719 0.1267 0.2799 0.0040  -0.0279 0.0303  388 PHE A N   
3047 C CA  . PHE A 408 ? 0.3546 0.1125 0.2872 0.0131  -0.0069 0.0223  388 PHE A CA  
3048 C C   . PHE A 408 ? 0.3407 0.1362 0.2765 -0.0113 0.0016  0.0240  388 PHE A C   
3049 O O   . PHE A 408 ? 0.4079 0.0794 0.3031 0.0193  0.0094  0.0442  388 PHE A O   
3050 C CB  . PHE A 408 ? 0.3826 0.0950 0.3040 0.0170  0.0077  0.0139  388 PHE A CB  
3051 C CG  . PHE A 408 ? 0.3782 0.1076 0.2743 -0.0076 -0.0057 0.0236  388 PHE A CG  
3052 C CD1 . PHE A 408 ? 0.3748 0.1240 0.2908 0.0016  -0.0156 0.0346  388 PHE A CD1 
3053 C CD2 . PHE A 408 ? 0.4067 0.1658 0.2727 0.0316  0.0042  0.0314  388 PHE A CD2 
3054 C CE1 . PHE A 408 ? 0.3358 0.1253 0.3161 -0.0133 -0.0279 0.0092  388 PHE A CE1 
3055 C CE2 . PHE A 408 ? 0.4046 0.1019 0.2766 0.0007  -0.0183 0.0395  388 PHE A CE2 
3056 C CZ  . PHE A 408 ? 0.3586 0.0884 0.2856 -0.0134 -0.0132 0.0245  388 PHE A CZ  
3057 N N   . VAL A 409 ? 0.3273 0.1660 0.2632 -0.0124 -0.0047 0.0405  389 VAL A N   
3058 C CA  . VAL A 409 ? 0.3443 0.1664 0.2795 0.0033  -0.0189 0.0089  389 VAL A CA  
3059 C C   . VAL A 409 ? 0.3387 0.1141 0.2466 -0.0153 -0.0007 0.0261  389 VAL A C   
3060 O O   . VAL A 409 ? 0.4231 0.0440 0.2643 0.0039  -0.0076 0.0297  389 VAL A O   
3061 C CB  . VAL A 409 ? 0.3360 0.1504 0.3022 0.0040  -0.0227 0.0021  389 VAL A CB  
3062 C CG1 . VAL A 409 ? 0.3618 0.1454 0.3620 -0.0273 -0.0122 0.0262  389 VAL A CG1 
3063 C CG2 . VAL A 409 ? 0.3167 0.2071 0.3377 0.0299  -0.0354 0.0060  389 VAL A CG2 
3064 N N   . ALA A 410 ? 0.3543 0.1015 0.2212 0.0055  0.0073  0.0412  390 ALA A N   
3065 C CA  . ALA A 410 ? 0.3563 0.0959 0.2607 -0.0028 -0.0155 0.0441  390 ALA A CA  
3066 C C   . ALA A 410 ? 0.3765 0.1040 0.2456 -0.0017 -0.0158 0.0207  390 ALA A C   
3067 O O   . ALA A 410 ? 0.4664 0.1261 0.2719 -0.0568 -0.0578 0.0630  390 ALA A O   
3068 C CB  . ALA A 410 ? 0.3629 0.0400 0.3039 0.0036  -0.0017 0.0487  390 ALA A CB  
3069 N N   . ALA A 411 ? 0.3498 0.1078 0.2267 -0.0310 -0.0062 0.0143  391 ALA A N   
3070 C CA  . ALA A 411 ? 0.3401 0.0930 0.2471 -0.0163 -0.0292 0.0040  391 ALA A CA  
3071 C C   . ALA A 411 ? 0.3324 0.1423 0.2520 0.0085  -0.0271 0.0089  391 ALA A C   
3072 O O   . ALA A 411 ? 0.3754 0.1456 0.2842 0.0208  -0.0487 -0.0021 391 ALA A O   
3073 C CB  . ALA A 411 ? 0.3481 0.0742 0.2671 -0.0124 -0.0216 -0.0037 391 ALA A CB  
3074 N N   . ILE A 412 ? 0.3234 0.1041 0.2168 0.0000  -0.0136 0.0377  392 ILE A N   
3075 C CA  . ILE A 412 ? 0.2846 0.1269 0.2501 0.0014  -0.0098 0.0167  392 ILE A CA  
3076 C C   . ILE A 412 ? 0.2630 0.1376 0.2360 -0.0152 -0.0057 0.0305  392 ILE A C   
3077 O O   . ILE A 412 ? 0.3092 0.1020 0.2354 -0.0256 -0.0090 0.0217  392 ILE A O   
3078 C CB  . ILE A 412 ? 0.2862 0.1132 0.2751 0.0092  0.0142  0.0336  392 ILE A CB  
3079 C CG1 . ILE A 412 ? 0.3060 0.1524 0.3023 -0.0252 0.0134  0.0485  392 ILE A CG1 
3080 C CG2 . ILE A 412 ? 0.3094 0.1148 0.2823 0.0182  0.0267  0.0472  392 ILE A CG2 
3081 C CD1 . ILE A 412 ? 0.3401 0.1114 0.3296 -0.0248 0.0102  0.0772  392 ILE A CD1 
3082 N N   . ASN A 413 ? 0.3043 0.0912 0.2188 -0.0162 -0.0281 -0.0019 393 ASN A N   
3083 C CA  . ASN A 413 ? 0.3190 0.0986 0.2442 -0.0298 -0.0248 0.0019  393 ASN A CA  
3084 C C   . ASN A 413 ? 0.3048 0.0966 0.2441 -0.0243 -0.0165 0.0184  393 ASN A C   
3085 O O   . ASN A 413 ? 0.3338 0.0529 0.2736 -0.0144 -0.0220 0.0137  393 ASN A O   
3086 C CB  . ASN A 413 ? 0.3188 0.0664 0.2611 -0.0074 -0.0012 0.0194  393 ASN A CB  
3087 C CG  . ASN A 413 ? 0.3513 0.0645 0.2616 -0.0156 -0.0077 0.0436  393 ASN A CG  
3088 O OD1 . ASN A 413 ? 0.4129 0.0665 0.2746 -0.0180 0.0123  0.0146  393 ASN A OD1 
3089 N ND2 . ASN A 413 ? 0.3629 0.0515 0.2726 0.0155  -0.0080 0.0473  393 ASN A ND2 
3090 N N   . SER A 414 ? 0.3541 0.1175 0.2749 0.0136  -0.0146 0.0034  394 SER A N   
3091 C CA  . SER A 414 ? 0.3418 0.1376 0.2910 0.0052  -0.0044 0.0261  394 SER A CA  
3092 C C   . SER A 414 ? 0.3575 0.1029 0.2998 0.0061  0.0025  0.0110  394 SER A C   
3093 O O   . SER A 414 ? 0.3717 0.1375 0.3206 0.0068  -0.0153 0.0480  394 SER A O   
3094 C CB  . SER A 414 ? 0.3504 0.1403 0.3350 0.0315  0.0238  0.0325  394 SER A CB  
3095 O OG  . SER A 414 ? 0.3801 0.1848 0.3390 0.0161  0.0523  0.0012  394 SER A OG  
3096 N N   . SER A 415 ? 0.3064 0.0387 0.2742 -0.0210 0.0052  0.0169  395 SER A N   
3097 C CA  . SER A 415 ? 0.3071 0.0711 0.2760 -0.0302 -0.0088 0.0232  395 SER A CA  
3098 C C   . SER A 415 ? 0.3092 0.0850 0.2920 -0.0030 -0.0176 0.0258  395 SER A C   
3099 O O   . SER A 415 ? 0.3017 0.1403 0.2837 0.0146  -0.0383 0.0012  395 SER A O   
3100 C CB  . SER A 415 ? 0.2885 0.0901 0.2971 -0.0232 0.0061  0.0335  395 SER A CB  
3101 O OG  . SER A 415 ? 0.2876 0.2067 0.3073 -0.0156 -0.0092 0.0210  395 SER A OG  
3102 N N   . HIS A 416 ? 0.3076 0.0761 0.2912 -0.0134 -0.0155 0.0118  396 HIS A N   
3103 C CA  . HIS A 416 ? 0.3349 0.0792 0.2928 0.0013  0.0094  0.0192  396 HIS A CA  
3104 C C   . HIS A 416 ? 0.3058 0.0689 0.2880 0.0081  0.0016  0.0330  396 HIS A C   
3105 O O   . HIS A 416 ? 0.3080 0.1613 0.3015 0.0146  -0.0028 0.0223  396 HIS A O   
3106 C CB  . HIS A 416 ? 0.3292 0.0867 0.3011 0.0223  0.0045  0.0225  396 HIS A CB  
3107 C CG  . HIS A 416 ? 0.3224 0.0779 0.2731 0.0108  0.0159  0.0240  396 HIS A CG  
3108 N ND1 . HIS A 416 ? 0.3012 0.0454 0.2701 0.0251  -0.0005 0.0440  396 HIS A ND1 
3109 C CD2 . HIS A 416 ? 0.3333 0.0673 0.2770 0.0114  0.0081  0.0290  396 HIS A CD2 
3110 C CE1 . HIS A 416 ? 0.2961 0.0386 0.2843 0.0462  0.0066  0.0139  396 HIS A CE1 
3111 N NE2 . HIS A 416 ? 0.3114 0.0224 0.2507 0.0280  0.0214  0.0258  396 HIS A NE2 
3112 N N   . GLY A 417 ? 0.3293 0.0980 0.3238 0.0229  0.0040  -0.0010 397 GLY A N   
3113 C CA  . GLY A 417 ? 0.3334 0.0809 0.3414 0.0046  0.0177  -0.0082 397 GLY A CA  
3114 C C   . GLY A 417 ? 0.3129 0.1376 0.3359 -0.0309 0.0087  0.0012  397 GLY A C   
3115 O O   . GLY A 417 ? 0.3679 0.1111 0.3492 -0.0427 0.0268  0.0128  397 GLY A O   
3116 N N   . ARG A 418 ? 0.2689 0.1628 0.3270 -0.0166 -0.0018 0.0063  398 ARG A N   
3117 C CA  . ARG A 418 ? 0.3052 0.1265 0.2961 -0.0157 -0.0090 0.0064  398 ARG A CA  
3118 C C   . ARG A 418 ? 0.3000 0.1262 0.2766 -0.0055 -0.0050 -0.0005 398 ARG A C   
3119 O O   . ARG A 418 ? 0.2988 0.1333 0.2822 0.0068  -0.0095 0.0359  398 ARG A O   
3120 C CB  . ARG A 418 ? 0.3596 0.1515 0.2802 -0.0213 -0.0150 0.0325  398 ARG A CB  
3121 C CG  . ARG A 418 ? 0.4024 0.1474 0.3175 -0.0072 -0.0257 0.0255  398 ARG A CG  
3122 C CD  . ARG A 418 ? 0.4618 0.1934 0.3403 0.0393  -0.0198 0.0373  398 ARG A CD  
3123 N NE  . ARG A 418 ? 0.4625 0.2655 0.3824 0.0306  -0.0264 0.0610  398 ARG A NE  
3124 C CZ  . ARG A 418 ? 0.4453 0.2730 0.4198 0.0105  -0.0415 0.0514  398 ARG A CZ  
3125 N NH1 . ARG A 418 ? 0.4651 0.2432 0.5234 -0.0391 -0.1059 0.0492  398 ARG A NH1 
3126 N NH2 . ARG A 418 ? 0.4707 0.2872 0.4699 0.0030  -0.0347 0.0526  398 ARG A NH2 
3127 N N   . LEU A 419 ? 0.2920 0.1522 0.2894 -0.0249 0.0031  0.0113  399 LEU A N   
3128 C CA  . LEU A 419 ? 0.3021 0.1063 0.2910 0.0172  0.0110  -0.0190 399 LEU A CA  
3129 C C   . LEU A 419 ? 0.3015 0.0518 0.2896 -0.0115 -0.0085 0.0079  399 LEU A C   
3130 O O   . LEU A 419 ? 0.2884 0.1830 0.2876 0.0144  -0.0154 -0.0048 399 LEU A O   
3131 C CB  . LEU A 419 ? 0.3220 0.1292 0.2845 0.0417  0.0122  0.0156  399 LEU A CB  
3132 C CG  . LEU A 419 ? 0.4127 0.1151 0.3282 0.0368  0.0314  0.0646  399 LEU A CG  
3133 C CD1 . LEU A 419 ? 0.4500 0.1754 0.3678 0.0642  0.0194  0.0346  399 LEU A CD1 
3134 C CD2 . LEU A 419 ? 0.4172 0.2082 0.3664 -0.0495 0.0061  0.0639  399 LEU A CD2 
3135 N N   . PHE A 420 ? 0.3010 0.1040 0.2557 -0.0251 -0.0069 -0.0065 400 PHE A N   
3136 C CA  . PHE A 420 ? 0.2965 0.0820 0.2396 0.0242  -0.0122 0.0090  400 PHE A CA  
3137 C C   . PHE A 420 ? 0.3088 0.1158 0.2723 -0.0070 -0.0275 0.0302  400 PHE A C   
3138 O O   . PHE A 420 ? 0.3747 0.0535 0.2809 -0.0031 -0.0300 0.0287  400 PHE A O   
3139 C CB  . PHE A 420 ? 0.3248 0.0969 0.2501 0.0124  -0.0127 0.0330  400 PHE A CB  
3140 C CG  . PHE A 420 ? 0.3073 0.0795 0.2500 0.0121  -0.0134 0.0112  400 PHE A CG  
3141 C CD1 . PHE A 420 ? 0.3222 0.1010 0.2721 -0.0022 -0.0196 0.0168  400 PHE A CD1 
3142 C CD2 . PHE A 420 ? 0.3017 0.1113 0.2550 0.0104  -0.0087 0.0086  400 PHE A CD2 
3143 C CE1 . PHE A 420 ? 0.3396 0.1188 0.2487 -0.0026 -0.0179 0.0009  400 PHE A CE1 
3144 C CE2 . PHE A 420 ? 0.3363 0.0700 0.2865 -0.0026 -0.0151 -0.0033 400 PHE A CE2 
3145 C CZ  . PHE A 420 ? 0.3382 0.0920 0.2918 -0.0054 -0.0082 -0.0018 400 PHE A CZ  
3146 N N   . TRP A 421 ? 0.3279 0.1022 0.2417 -0.0177 -0.0237 0.0349  401 TRP A N   
3147 C CA  . TRP A 421 ? 0.3141 0.0816 0.2604 -0.0001 -0.0074 0.0283  401 TRP A CA  
3148 C C   . TRP A 421 ? 0.2827 0.0596 0.2621 -0.0061 -0.0113 0.0456  401 TRP A C   
3149 O O   . TRP A 421 ? 0.3311 0.0766 0.2972 0.0100  -0.0264 0.0209  401 TRP A O   
3150 C CB  . TRP A 421 ? 0.3360 0.1197 0.2482 0.0045  0.0085  0.0339  401 TRP A CB  
3151 C CG  . TRP A 421 ? 0.2940 0.1188 0.2721 -0.0105 -0.0004 0.0388  401 TRP A CG  
3152 C CD1 . TRP A 421 ? 0.3137 0.1423 0.2822 -0.0281 0.0016  0.0386  401 TRP A CD1 
3153 C CD2 . TRP A 421 ? 0.3181 0.1532 0.2698 -0.0173 -0.0054 0.0353  401 TRP A CD2 
3154 N NE1 . TRP A 421 ? 0.3347 0.0998 0.2919 -0.0444 0.0144  0.0325  401 TRP A NE1 
3155 C CE2 . TRP A 421 ? 0.3133 0.1165 0.2818 -0.0349 -0.0074 0.0338  401 TRP A CE2 
3156 C CE3 . TRP A 421 ? 0.3084 0.2149 0.2920 -0.0257 -0.0111 0.0392  401 TRP A CE3 
3157 C CZ2 . TRP A 421 ? 0.3301 0.1604 0.2943 -0.0291 -0.0034 0.0268  401 TRP A CZ2 
3158 C CZ3 . TRP A 421 ? 0.2934 0.2182 0.2921 -0.0055 -0.0048 0.0356  401 TRP A CZ3 
3159 C CH2 . TRP A 421 ? 0.3423 0.2016 0.3061 -0.0264 -0.0007 0.0364  401 TRP A CH2 
3160 N N   . ASN A 422 ? 0.2976 0.0719 0.2627 -0.0152 -0.0188 0.0264  402 ASN A N   
3161 C CA  . ASN A 422 ? 0.2916 0.0935 0.2720 0.0187  -0.0188 0.0186  402 ASN A CA  
3162 C C   . ASN A 422 ? 0.3102 0.1036 0.2785 -0.0018 -0.0304 0.0318  402 ASN A C   
3163 O O   . ASN A 422 ? 0.3185 0.0178 0.2948 -0.0034 -0.0255 0.0299  402 ASN A O   
3164 C CB  . ASN A 422 ? 0.3269 0.0835 0.2561 0.0088  -0.0218 0.0182  402 ASN A CB  
3165 C CG  . ASN A 422 ? 0.3265 0.0767 0.2780 -0.0205 -0.0318 0.0285  402 ASN A CG  
3166 O OD1 . ASN A 422 ? 0.3709 0.0512 0.3016 -0.0171 -0.0436 0.0705  402 ASN A OD1 
3167 N ND2 . ASN A 422 ? 0.3430 0.0497 0.2671 -0.0334 -0.0384 0.0481  402 ASN A ND2 
3168 N N   . PHE A 423 ? 0.3153 0.0736 0.2684 0.0175  -0.0364 0.0262  403 PHE A N   
3169 C CA  . PHE A 423 ? 0.2979 0.0821 0.2570 0.0226  -0.0216 0.0280  403 PHE A CA  
3170 C C   . PHE A 423 ? 0.3043 0.0615 0.2521 -0.0216 -0.0264 0.0103  403 PHE A C   
3171 O O   . PHE A 423 ? 0.3602 0.1289 0.2682 0.0007  -0.0251 0.0250  403 PHE A O   
3172 C CB  . PHE A 423 ? 0.3113 0.0906 0.2646 0.0034  -0.0033 0.0175  403 PHE A CB  
3173 C CG  . PHE A 423 ? 0.3107 0.1169 0.2671 -0.0109 0.0019  0.0134  403 PHE A CG  
3174 C CD1 . PHE A 423 ? 0.3459 0.1002 0.2708 0.0195  -0.0009 0.0535  403 PHE A CD1 
3175 C CD2 . PHE A 423 ? 0.3530 0.1518 0.2725 -0.0104 -0.0012 0.0467  403 PHE A CD2 
3176 C CE1 . PHE A 423 ? 0.3722 0.1527 0.2959 0.0029  0.0009  0.0376  403 PHE A CE1 
3177 C CE2 . PHE A 423 ? 0.3429 0.1342 0.2730 -0.0031 0.0050  0.0375  403 PHE A CE2 
3178 C CZ  . PHE A 423 ? 0.3677 0.1125 0.2912 -0.0088 -0.0163 0.0049  403 PHE A CZ  
3179 N N   . THR A 424 ? 0.3028 0.0721 0.2517 -0.0023 -0.0192 0.0016  404 THR A N   
3180 C CA  . THR A 424 ? 0.3170 0.0732 0.2472 0.0223  0.0005  0.0349  404 THR A CA  
3181 C C   . THR A 424 ? 0.3327 0.0898 0.2365 -0.0249 -0.0123 0.0297  404 THR A C   
3182 O O   . THR A 424 ? 0.3187 0.0869 0.2605 -0.0346 0.0086  -0.0006 404 THR A O   
3183 C CB  . THR A 424 ? 0.3399 0.0639 0.2655 0.0236  -0.0178 0.0393  404 THR A CB  
3184 O OG1 . THR A 424 ? 0.3263 0.0825 0.2559 0.0047  -0.0154 0.0556  404 THR A OG1 
3185 C CG2 . THR A 424 ? 0.3651 0.0915 0.2566 -0.0018 -0.0108 0.0395  404 THR A CG2 
3186 N N   . TYR A 425 ? 0.3501 0.0350 0.2646 -0.0316 -0.0115 0.0507  405 TYR A N   
3187 C CA  . TYR A 425 ? 0.3521 0.0240 0.3073 -0.0311 -0.0141 0.0376  405 TYR A CA  
3188 C C   . TYR A 425 ? 0.3703 0.0909 0.3072 -0.0311 0.0026  0.0190  405 TYR A C   
3189 O O   . TYR A 425 ? 0.4076 0.0338 0.3284 0.0005  0.0288  0.0230  405 TYR A O   
3190 C CB  . TYR A 425 ? 0.3779 0.0236 0.3211 -0.0113 -0.0037 -0.0141 405 TYR A CB  
3191 C CG  . TYR A 425 ? 0.3462 0.0805 0.3268 -0.0066 -0.0285 0.0023  405 TYR A CG  
3192 C CD1 . TYR A 425 ? 0.3367 0.1325 0.3579 0.0071  -0.0124 0.0312  405 TYR A CD1 
3193 C CD2 . TYR A 425 ? 0.3926 0.0644 0.3658 -0.0378 -0.0218 -0.0038 405 TYR A CD2 
3194 C CE1 . TYR A 425 ? 0.3669 0.1593 0.3473 0.0100  -0.0122 0.0039  405 TYR A CE1 
3195 C CE2 . TYR A 425 ? 0.3928 0.0696 0.3853 -0.0451 -0.0306 0.0209  405 TYR A CE2 
3196 C CZ  . TYR A 425 ? 0.3970 0.1175 0.3475 -0.0409 -0.0254 0.0490  405 TYR A CZ  
3197 O OH  . TYR A 425 ? 0.4460 0.1642 0.3480 -0.0284 -0.0696 0.0102  405 TYR A OH  
3198 N N   . ILE A 426 ? 0.3995 0.1004 0.3289 -0.0047 0.0220  0.0324  406 ILE A N   
3199 C CA  . ILE A 426 ? 0.3698 0.1199 0.3167 -0.0085 0.0000  0.0118  406 ILE A CA  
3200 C C   . ILE A 426 ? 0.3731 0.1056 0.3352 0.0171  0.0079  0.0092  406 ILE A C   
3201 O O   . ILE A 426 ? 0.4112 0.1102 0.3730 -0.0121 -0.0015 0.0258  406 ILE A O   
3202 C CB  . ILE A 426 ? 0.3563 0.1278 0.3460 0.0222  -0.0108 -0.0131 406 ILE A CB  
3203 C CG1 . ILE A 426 ? 0.3485 0.1653 0.3354 0.0390  -0.0026 0.0046  406 ILE A CG1 
3204 C CG2 . ILE A 426 ? 0.3994 0.1127 0.4028 0.0559  -0.0070 -0.0019 406 ILE A CG2 
3205 C CD1 . ILE A 426 ? 0.3576 0.1757 0.3458 0.0251  0.0016  0.0104  406 ILE A CD1 
3206 N N   . ASP A 427 ? 0.4245 0.0868 0.3391 0.0027  0.0009  -0.0031 407 ASP A N   
3207 C CA  . ASP A 427 ? 0.4316 0.1523 0.3738 -0.0087 -0.0110 -0.0203 407 ASP A CA  
3208 C C   . ASP A 427 ? 0.4241 0.1623 0.3915 -0.0086 -0.0130 -0.0149 407 ASP A C   
3209 O O   . ASP A 427 ? 0.3870 0.2146 0.3850 0.0173  0.0019  -0.0181 407 ASP A O   
3210 C CB  . ASP A 427 ? 0.4668 0.1067 0.4136 -0.0358 0.0000  -0.0121 407 ASP A CB  
3211 C CG  . ASP A 427 ? 0.4991 0.1682 0.4192 -0.0156 -0.0030 -0.0323 407 ASP A CG  
3212 O OD1 . ASP A 427 ? 0.4706 0.3100 0.4177 -0.0171 -0.0510 -0.0601 407 ASP A OD1 
3213 O OD2 . ASP A 427 ? 0.5479 0.2371 0.4501 -0.0179 0.0250  -0.0528 407 ASP A OD2 
3214 N N   . GLU A 428 ? 0.4785 0.0911 0.4591 -0.0496 -0.0013 -0.0265 408 GLU A N   
3215 C CA  . GLU A 428 ? 0.5161 0.0850 0.4790 -0.0319 -0.0004 -0.0038 408 GLU A CA  
3216 C C   . GLU A 428 ? 0.4768 0.1083 0.4662 -0.0189 -0.0029 -0.0205 408 GLU A C   
3217 O O   . GLU A 428 ? 0.5033 0.1286 0.4522 -0.0359 0.0204  -0.0104 408 GLU A O   
3218 C CB  . GLU A 428 ? 0.5787 0.1893 0.5306 0.0042  0.0047  0.0146  408 GLU A CB  
3219 C CG  . GLU A 428 ? 0.7188 0.3036 0.5981 0.0293  0.0136  0.0427  408 GLU A CG  
3220 C CD  . GLU A 428 ? 0.8960 0.3454 0.6582 0.0986  0.0147  0.0883  408 GLU A CD  
3221 O OE1 . GLU A 428 ? 1.0531 0.5847 0.6831 0.0838  0.0609  0.0763  408 GLU A OE1 
3222 O OE2 . GLU A 428 ? 0.9346 0.3818 0.7817 0.1417  -0.0075 0.1378  408 GLU A OE2 
3223 N N   . ALA A 429 ? 0.4411 0.0731 0.4346 -0.0315 0.0127  0.0047  409 ALA A N   
3224 C CA  . ALA A 429 ? 0.4483 0.0819 0.4309 -0.0335 0.0067  0.0294  409 ALA A CA  
3225 C C   . ALA A 429 ? 0.4294 0.1053 0.4230 -0.0279 0.0331  0.0240  409 ALA A C   
3226 O O   . ALA A 429 ? 0.4276 0.1053 0.4188 -0.0277 0.0108  0.0251  409 ALA A O   
3227 C CB  . ALA A 429 ? 0.4499 0.1130 0.4071 -0.0355 0.0068  0.0431  409 ALA A CB  
3228 N N   . VAL A 430 ? 0.4338 0.1205 0.3990 -0.0240 0.0045  0.0240  410 VAL A N   
3229 C CA  . VAL A 430 ? 0.4117 0.0627 0.3764 -0.0606 0.0070  0.0049  410 VAL A CA  
3230 C C   . VAL A 430 ? 0.4158 0.1189 0.3644 -0.0403 -0.0025 -0.0018 410 VAL A C   
3231 O O   . VAL A 430 ? 0.4388 0.1080 0.3620 -0.0315 -0.0126 0.0132  410 VAL A O   
3232 C CB  . VAL A 430 ? 0.4207 0.0762 0.3751 -0.0365 -0.0104 -0.0111 410 VAL A CB  
3233 C CG1 . VAL A 430 ? 0.4504 0.0947 0.3862 -0.0187 -0.0163 0.0401  410 VAL A CG1 
3234 C CG2 . VAL A 430 ? 0.4352 0.0784 0.3654 -0.0285 -0.0270 0.0011  410 VAL A CG2 
3235 N N   . PRO A 431 ? 0.4460 0.0824 0.3863 -0.0391 0.0014  0.0070  411 PRO A N   
3236 C CA  . PRO A 431 ? 0.4736 0.1188 0.3676 -0.0193 0.0077  0.0019  411 PRO A CA  
3237 C C   . PRO A 431 ? 0.4504 0.1214 0.3521 -0.0391 0.0110  0.0014  411 PRO A C   
3238 O O   . PRO A 431 ? 0.4278 0.1283 0.3594 -0.0458 0.0189  -0.0110 411 PRO A O   
3239 C CB  . PRO A 431 ? 0.4901 0.2036 0.3948 -0.0354 0.0123  -0.0088 411 PRO A CB  
3240 C CG  . PRO A 431 ? 0.4756 0.1511 0.4190 -0.0114 0.0190  -0.0007 411 PRO A CG  
3241 C CD  . PRO A 431 ? 0.4552 0.0885 0.4179 -0.0305 0.0068  0.0096  411 PRO A CD  
3242 N N   . GLY A 432 ? 0.4422 0.1541 0.3523 -0.0107 0.0058  -0.0096 412 GLY A N   
3243 C CA  . GLY A 432 ? 0.4353 0.1423 0.3444 -0.0231 -0.0067 0.0045  412 GLY A CA  
3244 C C   . GLY A 432 ? 0.4342 0.1977 0.3437 -0.0156 0.0048  -0.0250 412 GLY A C   
3245 O O   . GLY A 432 ? 0.4272 0.1518 0.3729 -0.0050 -0.0180 -0.0067 412 GLY A O   
3246 N N   . GLU A 433 ? 0.4151 0.2156 0.3742 -0.0278 -0.0023 -0.0179 413 GLU A N   
3247 C CA  . GLU A 433 ? 0.4480 0.2241 0.3777 -0.0451 0.0016  -0.0335 413 GLU A CA  
3248 C C   . GLU A 433 ? 0.4220 0.2046 0.3668 -0.0311 0.0025  -0.0058 413 GLU A C   
3249 O O   . GLU A 433 ? 0.4340 0.1186 0.3802 -0.0752 -0.0055 0.0052  413 GLU A O   
3250 C CB  . GLU A 433 ? 0.4944 0.2885 0.3726 -0.0557 -0.0109 -0.0962 413 GLU A CB  
3251 C CG  . GLU A 433 ? 0.5766 0.4298 0.4802 -0.0060 -0.0209 -0.0350 413 GLU A CG  
3252 C CD  . GLU A 433 ? 0.3799 0.3799 0.3799 0.0000  0.0000  0.0000  413 GLU A CD  
3253 O OE1 . GLU A 433 ? 0.3799 0.3799 0.3799 0.0000  0.0000  0.0000  413 GLU A OE1 
3254 O OE2 . GLU A 433 ? 0.3799 0.3799 0.3799 0.0000  0.0000  0.0000  413 GLU A OE2 
3255 N N   . ARG A 434 ? 0.3984 0.1377 0.3484 -0.0234 0.0027  0.0018  414 ARG A N   
3256 C CA  . ARG A 434 ? 0.3907 0.1241 0.3440 -0.0048 -0.0016 -0.0013 414 ARG A CA  
3257 C C   . ARG A 434 ? 0.3752 0.1923 0.3176 -0.0280 -0.0124 -0.0234 414 ARG A C   
3258 O O   . ARG A 434 ? 0.3795 0.1938 0.3345 -0.0228 -0.0039 0.0017  414 ARG A O   
3259 C CB  . ARG A 434 ? 0.3967 0.1430 0.3556 0.0000  0.0061  0.0030  414 ARG A CB  
3260 C CG  . ARG A 434 ? 0.4131 0.1544 0.3512 0.0065  0.0046  0.0021  414 ARG A CG  
3261 C CD  . ARG A 434 ? 0.4194 0.1503 0.3692 0.0033  0.0106  0.0041  414 ARG A CD  
3262 N NE  . ARG A 434 ? 0.4210 0.1800 0.3814 -0.0030 0.0023  0.0305  414 ARG A NE  
3263 C CZ  . ARG A 434 ? 0.4189 0.1547 0.3756 0.0221  0.0187  0.0365  414 ARG A CZ  
3264 N NH1 . ARG A 434 ? 0.4111 0.1521 0.4128 0.0334  0.0205  0.0661  414 ARG A NH1 
3265 N NH2 . ARG A 434 ? 0.4522 0.1264 0.3899 0.0291  0.0042  0.0477  414 ARG A NH2 
3266 N N   . ALA A 435 ? 0.3922 0.1675 0.3117 -0.0215 -0.0077 -0.0059 415 ALA A N   
3267 C CA  . ALA A 435 ? 0.3776 0.2080 0.3116 -0.0307 -0.0137 -0.0038 415 ALA A CA  
3268 C C   . ALA A 435 ? 0.3551 0.1723 0.2842 -0.0358 -0.0089 0.0233  415 ALA A C   
3269 O O   . ALA A 435 ? 0.3606 0.1830 0.2971 -0.0304 0.0093  0.0025  415 ALA A O   
3270 C CB  . ALA A 435 ? 0.4091 0.2030 0.2913 0.0061  0.0014  0.0133  415 ALA A CB  
3271 N N   . GLU A 436 ? 0.3770 0.1436 0.3036 -0.0414 -0.0180 0.0266  416 GLU A N   
3272 C CA  . GLU A 436 ? 0.3909 0.1660 0.3352 -0.0392 -0.0237 0.0178  416 GLU A CA  
3273 C C   . GLU A 436 ? 0.3785 0.1349 0.3385 -0.0456 0.0051  0.0097  416 GLU A C   
3274 O O   . GLU A 436 ? 0.3536 0.1496 0.3329 -0.0327 0.0043  0.0127  416 GLU A O   
3275 C CB  . GLU A 436 ? 0.4450 0.1864 0.3568 -0.0644 -0.0178 0.0425  416 GLU A CB  
3276 C CG  . GLU A 436 ? 0.4969 0.2012 0.3865 -0.1000 -0.0167 0.0821  416 GLU A CG  
3277 C CD  . GLU A 436 ? 0.5017 0.2365 0.3811 -0.1609 -0.0429 0.1980  416 GLU A CD  
3278 O OE1 . GLU A 436 ? 0.4588 0.1472 0.3088 -0.1645 -0.0469 0.1723  416 GLU A OE1 
3279 O OE2 . GLU A 436 ? 0.5371 0.4119 0.4491 -0.1006 0.0240  0.1364  416 GLU A OE2 
3280 N N   . ARG A 437 ? 0.3780 0.1328 0.3498 -0.0437 0.0093  0.0111  417 ARG A N   
3281 C CA  . ARG A 437 ? 0.3837 0.1417 0.3606 -0.0444 0.0006  0.0097  417 ARG A CA  
3282 C C   . ARG A 437 ? 0.3577 0.1331 0.3376 -0.0442 0.0002  0.0325  417 ARG A C   
3283 O O   . ARG A 437 ? 0.3338 0.1355 0.3676 -0.0459 -0.0002 0.0150  417 ARG A O   
3284 C CB  . ARG A 437 ? 0.4281 0.1363 0.4226 -0.0223 -0.0177 0.0105  417 ARG A CB  
3285 C CG  . ARG A 437 ? 0.4426 0.2052 0.4565 -0.0338 -0.0381 0.0001  417 ARG A CG  
3286 C CD  . ARG A 437 ? 0.5075 0.2117 0.5648 -0.0770 -0.0555 -0.0009 417 ARG A CD  
3287 N NE  . ARG A 437 ? 0.5198 0.2027 0.5766 -0.0894 -0.0639 -0.0263 417 ARG A NE  
3288 C CZ  . ARG A 437 ? 0.5676 0.2262 0.7013 -0.0779 -0.0720 0.0448  417 ARG A CZ  
3289 N NH1 . ARG A 437 ? 0.6734 0.1548 0.7240 -0.1304 -0.1162 -0.0202 417 ARG A NH1 
3290 N NH2 . ARG A 437 ? 0.5613 0.2672 0.7861 -0.0371 -0.0684 0.1235  417 ARG A NH2 
3291 N N   . LEU A 438 ? 0.3845 0.1250 0.3477 -0.0377 -0.0190 0.0227  418 LEU A N   
3292 C CA  . LEU A 438 ? 0.3881 0.0831 0.3519 -0.0409 -0.0323 0.0587  418 LEU A CA  
3293 C C   . LEU A 438 ? 0.3735 0.0760 0.3566 -0.0149 -0.0093 0.0246  418 LEU A C   
3294 O O   . LEU A 438 ? 0.3819 0.1834 0.3303 0.0049  -0.0300 0.0024  418 LEU A O   
3295 C CB  . LEU A 438 ? 0.3884 0.1160 0.3877 -0.0554 -0.0035 0.0611  418 LEU A CB  
3296 C CG  . LEU A 438 ? 0.3806 0.1190 0.4069 -0.0439 -0.0018 0.0680  418 LEU A CG  
3297 C CD1 . LEU A 438 ? 0.3949 0.1393 0.4584 -0.0427 -0.0059 0.0745  418 LEU A CD1 
3298 C CD2 . LEU A 438 ? 0.3938 0.1474 0.4075 -0.0464 -0.0049 0.0448  418 LEU A CD2 
3299 N N   . ALA A 439 ? 0.3887 0.1054 0.3283 0.0187  -0.0147 -0.0154 419 ALA A N   
3300 C CA  . ALA A 439 ? 0.4085 0.1000 0.3198 -0.0206 -0.0266 -0.0326 419 ALA A CA  
3301 C C   . ALA A 439 ? 0.3962 0.1886 0.3036 -0.0391 -0.0152 -0.0400 419 ALA A C   
3302 O O   . ALA A 439 ? 0.4083 0.1165 0.3173 -0.0366 -0.0050 0.0075  419 ALA A O   
3303 C CB  . ALA A 439 ? 0.4075 0.1555 0.3603 -0.0398 -0.0114 -0.0037 419 ALA A CB  
3304 N N   . GLU A 440 ? 0.3920 0.2010 0.2976 -0.0534 -0.0280 0.0031  420 GLU A N   
3305 C CA  . GLU A 440 ? 0.4025 0.1823 0.3218 -0.0318 -0.0256 0.0138  420 GLU A CA  
3306 C C   . GLU A 440 ? 0.3784 0.1958 0.3121 -0.0117 -0.0245 0.0142  420 GLU A C   
3307 O O   . GLU A 440 ? 0.4143 0.1439 0.3440 -0.0492 -0.0134 0.0061  420 GLU A O   
3308 C CB  . GLU A 440 ? 0.4281 0.2101 0.3440 -0.0318 -0.0352 0.0148  420 GLU A CB  
3309 C CG  . GLU A 440 ? 0.4529 0.2658 0.3806 -0.0012 -0.0345 0.0260  420 GLU A CG  
3310 C CD  . GLU A 440 ? 0.4478 0.3199 0.4719 0.0242  -0.0331 0.1096  420 GLU A CD  
3311 O OE1 . GLU A 440 ? 0.4669 0.3063 0.5304 0.0207  -0.0076 0.1130  420 GLU A OE1 
3312 O OE2 . GLU A 440 ? 0.4466 0.4550 0.5637 0.0246  -0.0343 0.1487  420 GLU A OE2 
3313 N N   . ASP A 441 ? 0.3886 0.1538 0.3224 0.0009  0.0054  0.0166  421 ASP A N   
3314 C CA  . ASP A 441 ? 0.3854 0.1426 0.3294 -0.0013 -0.0235 0.0409  421 ASP A CA  
3315 C C   . ASP A 441 ? 0.3607 0.1719 0.2998 -0.0159 -0.0275 0.0314  421 ASP A C   
3316 O O   . ASP A 441 ? 0.3683 0.2463 0.3142 -0.0184 0.0012  0.0240  421 ASP A O   
3317 C CB  . ASP A 441 ? 0.4105 0.1326 0.3644 0.0074  -0.0030 0.0352  421 ASP A CB  
3318 C CG  . ASP A 441 ? 0.4360 0.1763 0.3831 0.0125  0.0027  0.0518  421 ASP A CG  
3319 O OD1 . ASP A 441 ? 0.5000 0.1643 0.4653 0.0205  0.0454  0.0557  421 ASP A OD1 
3320 O OD2 . ASP A 441 ? 0.4432 0.1890 0.4150 0.0367  -0.0008 0.0827  421 ASP A OD2 
3321 N N   . CYS A 442 ? 0.3852 0.1654 0.3117 -0.0265 -0.0174 0.0231  422 CYS A N   
3322 C CA  . CYS A 442 ? 0.3859 0.1729 0.3159 -0.0321 -0.0233 0.0211  422 CYS A CA  
3323 C C   . CYS A 442 ? 0.3641 0.1908 0.3049 -0.0197 -0.0089 0.0302  422 CYS A C   
3324 O O   . CYS A 442 ? 0.3842 0.1712 0.2976 -0.0161 -0.0189 0.0299  422 CYS A O   
3325 C CB  . CYS A 442 ? 0.4046 0.1732 0.3476 -0.0170 0.0000  0.0130  422 CYS A CB  
3326 S SG  . CYS A 442 ? 0.4687 0.2081 0.4103 -0.0251 -0.0112 0.0442  422 CYS A SG  
3327 N N   . LEU A 443 ? 0.3214 0.2206 0.2888 -0.0100 -0.0115 0.0150  423 LEU A N   
3328 C CA  . LEU A 443 ? 0.3838 0.1806 0.2987 -0.0136 -0.0158 0.0179  423 LEU A CA  
3329 C C   . LEU A 443 ? 0.3610 0.1659 0.2898 -0.0463 -0.0176 0.0195  423 LEU A C   
3330 O O   . LEU A 443 ? 0.3984 0.1977 0.3237 -0.0073 0.0037  0.0187  423 LEU A O   
3331 C CB  . LEU A 443 ? 0.4472 0.2147 0.3387 -0.0234 -0.0234 0.0229  423 LEU A CB  
3332 C CG  . LEU A 443 ? 0.6083 0.3025 0.3761 -0.0256 -0.0075 0.0737  423 LEU A CG  
3333 C CD1 . LEU A 443 ? 0.5710 0.1498 0.3841 -0.0693 0.0067  0.0675  423 LEU A CD1 
3334 C CD2 . LEU A 443 ? 0.6812 0.3443 0.4261 -0.0232 0.0320  0.0219  423 LEU A CD2 
3335 N N   . GLY A 444 ? 0.3716 0.1500 0.3210 -0.0508 -0.0096 -0.0112 424 GLY A N   
3336 C CA  . GLY A 444 ? 0.3838 0.1798 0.3334 -0.0289 -0.0130 0.0039  424 GLY A CA  
3337 C C   . GLY A 444 ? 0.3174 0.1988 0.3082 -0.0401 -0.0174 0.0132  424 GLY A C   
3338 O O   . GLY A 444 ? 0.3559 0.2130 0.3069 -0.0128 -0.0510 0.0035  424 GLY A O   
3339 N N   . THR A 445 ? 0.3393 0.1867 0.3215 -0.0469 -0.0187 0.0069  425 THR A N   
3340 C CA  . THR A 445 ? 0.3208 0.1517 0.2995 -0.0382 -0.0234 0.0090  425 THR A CA  
3341 C C   . THR A 445 ? 0.3244 0.1698 0.2805 -0.0211 -0.0061 -0.0031 425 THR A C   
3342 O O   . THR A 445 ? 0.3481 0.1647 0.3028 -0.0305 0.0126  0.0041  425 THR A O   
3343 C CB  . THR A 445 ? 0.3099 0.1961 0.3190 -0.0315 -0.0323 0.0127  425 THR A CB  
3344 O OG1 . THR A 445 ? 0.3635 0.1686 0.3526 -0.0533 -0.0258 0.0248  425 THR A OG1 
3345 C CG2 . THR A 445 ? 0.3547 0.1834 0.3035 -0.0172 -0.0152 0.0115  425 THR A CG2 
3346 N N   . LEU A 446 ? 0.3552 0.1893 0.2832 -0.0201 -0.0062 -0.0175 426 LEU A N   
3347 C CA  . LEU A 446 ? 0.3307 0.2082 0.2893 -0.0207 -0.0265 -0.0072 426 LEU A CA  
3348 C C   . LEU A 446 ? 0.3289 0.2238 0.2891 -0.0058 -0.0069 0.0001  426 LEU A C   
3349 O O   . LEU A 446 ? 0.3394 0.2187 0.2884 -0.0152 0.0079  -0.0090 426 LEU A O   
3350 C CB  . LEU A 446 ? 0.3451 0.2229 0.2982 -0.0251 -0.0255 0.0062  426 LEU A CB  
3351 C CG  . LEU A 446 ? 0.3427 0.2541 0.3242 -0.0575 -0.0097 -0.0224 426 LEU A CG  
3352 C CD1 . LEU A 446 ? 0.3721 0.1990 0.3605 -0.0704 -0.0327 -0.0312 426 LEU A CD1 
3353 C CD2 . LEU A 446 ? 0.4124 0.2879 0.3739 -0.0579 0.0119  -0.0100 426 LEU A CD2 
3354 N N   . LEU A 447 ? 0.3153 0.2066 0.2899 -0.0139 -0.0131 -0.0052 427 LEU A N   
3355 C CA  . LEU A 447 ? 0.3241 0.2245 0.3116 -0.0016 -0.0191 -0.0109 427 LEU A CA  
3356 C C   . LEU A 447 ? 0.3207 0.2436 0.3067 -0.0071 -0.0161 0.0042  427 LEU A C   
3357 O O   . LEU A 447 ? 0.3479 0.2415 0.3168 0.0212  -0.0062 -0.0093 427 LEU A O   
3358 C CB  . LEU A 447 ? 0.3696 0.2150 0.3034 -0.0058 -0.0154 0.0249  427 LEU A CB  
3359 C CG  . LEU A 447 ? 0.3619 0.1970 0.3353 -0.0214 -0.0198 0.0101  427 LEU A CG  
3360 C CD1 . LEU A 447 ? 0.4126 0.2029 0.3304 0.0081  -0.0016 0.0408  427 LEU A CD1 
3361 C CD2 . LEU A 447 ? 0.4384 0.2018 0.3853 -0.0665 0.0155  0.0145  427 LEU A CD2 
3362 N N   . SER A 448 ? 0.3303 0.2298 0.3223 -0.0260 -0.0155 -0.0067 428 SER A N   
3363 C CA  . SER A 448 ? 0.3519 0.2480 0.3215 -0.0287 -0.0088 -0.0014 428 SER A CA  
3364 C C   . SER A 448 ? 0.3545 0.3008 0.3147 -0.0349 0.0104  -0.0108 428 SER A C   
3365 O O   . SER A 448 ? 0.3724 0.3822 0.3417 -0.0218 0.0074  -0.0577 428 SER A O   
3366 C CB  . SER A 448 ? 0.3841 0.2709 0.3115 -0.0460 -0.0161 0.0426  428 SER A CB  
3367 O OG  . SER A 448 ? 0.3961 0.2893 0.3132 -0.0304 -0.0308 0.0766  428 SER A OG  
3368 N N   . ALA A 449 ? 0.3421 0.2618 0.2970 -0.0336 0.0180  -0.0199 429 ALA A N   
3369 C CA  . ALA A 449 ? 0.3772 0.2439 0.3627 -0.0552 -0.0040 -0.0376 429 ALA A CA  
3370 C C   . ALA A 449 ? 0.3709 0.2164 0.4129 -0.0309 0.0189  -0.0804 429 ALA A C   
3371 O O   . ALA A 449 ? 0.4183 0.3449 0.5054 -0.0480 0.0528  -0.1269 429 ALA A O   
3372 C CB  . ALA A 449 ? 0.4208 0.2556 0.3937 -0.0334 0.0001  -0.0157 429 ALA A CB  
3373 N N   . ILE A 450 ? 0.3224 0.2205 0.4098 0.0034  -0.0092 -0.0786 430 ILE A N   
3374 C CA  . ILE A 450 ? 0.3660 0.2171 0.5107 0.0270  0.0067  -0.0876 430 ILE A CA  
3375 C C   . ILE A 450 ? 0.3736 0.2726 0.4948 0.0386  0.0112  -0.1102 430 ILE A C   
3376 O O   . ILE A 450 ? 0.4145 0.2432 0.5579 0.0571  -0.0146 -0.1201 430 ILE A O   
3377 C CB  . ILE A 450 ? 0.3853 0.2089 0.5869 0.0110  0.0176  -0.0423 430 ILE A CB  
3378 C CG1 . ILE A 450 ? 0.4299 0.2725 0.6500 -0.0718 0.0363  -0.0723 430 ILE A CG1 
3379 C CG2 . ILE A 450 ? 0.4263 0.2953 0.6449 -0.0061 -0.0018 -0.0121 430 ILE A CG2 
3380 C CD1 . ILE A 450 ? 0.5109 0.3106 0.5906 -0.1258 0.0235  -0.0637 430 ILE A CD1 
3381 N N   . HIS A 451 ? 0.3505 0.2945 0.4633 0.0171  -0.0067 -0.0661 431 HIS A N   
3382 C CA  . HIS A 451 ? 0.3780 0.3578 0.4587 0.0422  0.0061  -0.0570 431 HIS A CA  
3383 C C   . HIS A 451 ? 0.3632 0.5157 0.4565 0.0652  0.0497  -0.0300 431 HIS A C   
3384 O O   . HIS A 451 ? 0.3762 0.5343 0.4793 0.0711  0.0059  -0.0496 431 HIS A O   
3385 C CB  . HIS A 451 ? 0.3850 0.3055 0.4417 0.0309  0.0050  -0.0433 431 HIS A CB  
3386 C CG  . HIS A 451 ? 0.4416 0.2954 0.4825 0.0478  0.0105  -0.0096 431 HIS A CG  
3387 N ND1 . HIS A 451 ? 0.5484 0.2777 0.5117 0.0220  0.0344  0.0015  431 HIS A ND1 
3388 C CD2 . HIS A 451 ? 0.4368 0.3183 0.4979 0.0186  0.0296  0.0227  431 HIS A CD2 
3389 C CE1 . HIS A 451 ? 0.5699 0.3372 0.5842 0.0154  0.0844  0.0181  431 HIS A CE1 
3390 N NE2 . HIS A 451 ? 0.5407 0.3314 0.5696 0.0256  0.0369  0.0551  431 HIS A NE2 
3391 N N   . ALA A 452 ? 0.3987 0.6443 0.4912 0.0638  0.0422  -0.0082 432 ALA A N   
3392 C CA  . ALA A 452 ? 0.3912 0.7580 0.5353 0.0123  0.0650  0.0017  432 ALA A CA  
3393 C C   . ALA A 452 ? 0.3825 0.7604 0.5211 -0.0396 0.0583  -0.0352 432 ALA A C   
3394 O O   . ALA A 452 ? 0.3243 0.8133 0.5552 -0.0926 0.0619  -0.1049 432 ALA A O   
3395 C CB  . ALA A 452 ? 0.4337 0.8239 0.5204 0.0264  0.0984  0.0302  432 ALA A CB  
3396 N N   . PRO A 453 ? 0.3843 0.8161 0.5148 -0.0161 0.0728  -0.0467 433 PRO A N   
3397 C CA  . PRO A 453 ? 0.4766 0.8227 0.5355 -0.0133 0.0801  -0.0455 433 PRO A CA  
3398 C C   . PRO A 453 ? 0.6031 0.9394 0.5427 0.0162  0.1120  -0.0852 433 PRO A C   
3399 O O   . PRO A 453 ? 0.5321 0.9924 0.6255 0.0620  0.1387  0.0188  433 PRO A O   
3400 C CB  . PRO A 453 ? 0.4273 0.7463 0.6027 -0.0070 0.0778  -0.0453 433 PRO A CB  
3401 C CG  . PRO A 453 ? 0.4227 0.8418 0.6067 -0.0480 0.0584  -0.0644 433 PRO A CG  
3402 C CD  . PRO A 453 ? 0.3699 0.7957 0.5429 -0.0343 0.0598  -0.0446 433 PRO A CD  
3403 N N   . GLN A 454 ? 0.7627 1.0174 0.5424 -0.0046 0.0990  -0.2138 434 GLN A N   
3404 C CA  . GLN A 454 ? 0.8354 1.1090 0.5837 -0.0260 0.0715  -0.2191 434 GLN A CA  
3405 C C   . GLN A 454 ? 0.8395 1.1005 0.5925 0.0018  0.1311  -0.2794 434 GLN A C   
3406 O O   . GLN A 454 ? 0.8205 1.1089 0.6924 0.0472  0.1394  -0.2833 434 GLN A O   
3407 C CB  . GLN A 454 ? 0.8761 1.1616 0.6391 -0.0351 0.0511  -0.2150 434 GLN A CB  
3408 C CG  . GLN A 454 ? 0.8414 1.1350 0.6425 -0.0308 0.0406  -0.2246 434 GLN A CG  
3409 C CD  . GLN A 454 ? 0.7875 1.1360 0.6466 -0.0277 0.0279  -0.2411 434 GLN A CD  
3410 O OE1 . GLN A 454 ? 0.7855 1.1391 0.6549 -0.0194 0.0217  -0.2293 434 GLN A OE1 
3411 N NE2 . GLN A 454 ? 0.8159 1.1485 0.6422 -0.0149 0.0272  -0.2401 434 GLN A NE2 
3412 C C1  . GOL B .   ? 0.4964 0.5825 0.5566 -0.1643 0.1604  -0.2450 501 GOL A C1  
3413 O O1  . GOL B .   ? 0.5314 0.6284 0.5599 -0.2096 0.1255  -0.2295 501 GOL A O1  
3414 C C2  . GOL B .   ? 0.4878 0.5614 0.6262 -0.1707 0.1379  -0.2235 501 GOL A C2  
3415 O O2  . GOL B .   ? 0.5552 0.4669 0.6143 -0.1455 0.0861  -0.2255 501 GOL A O2  
3416 C C3  . GOL B .   ? 0.5493 0.5867 0.6748 -0.1193 0.1385  -0.2126 501 GOL A C3  
3417 O O3  . GOL B .   ? 0.5645 0.5094 0.7527 -0.1010 0.1573  -0.1921 501 GOL A O3  
3418 C C1  . GOL C .   ? 0.4137 0.1687 0.4737 0.0254  -0.0657 0.1182  502 GOL A C1  
3419 O O1  . GOL C .   ? 0.3979 0.1082 0.4325 0.0168  -0.0408 0.0801  502 GOL A O1  
3420 C C2  . GOL C .   ? 0.4473 0.2656 0.4529 0.0230  -0.0418 0.1166  502 GOL A C2  
3421 O O2  . GOL C .   ? 0.4020 0.1586 0.3565 0.0490  -0.0512 0.0459  502 GOL A O2  
3422 C C3  . GOL C .   ? 0.4058 0.2649 0.4688 0.0480  -0.0303 0.1335  502 GOL A C3  
3423 O O3  . GOL C .   ? 0.2839 0.2181 0.4590 0.0811  -0.0315 0.1588  502 GOL A O3  
3424 O O   . HOH D .   ? 0.4143 0.3378 0.4921 -0.0615 -0.0309 0.1230  601 HOH A O   
3425 O O   . HOH D .   ? 0.6776 0.4624 0.8480 -0.0474 -0.0324 -0.0229 602 HOH A O   
3426 O O   . HOH D .   ? 0.6512 0.2052 0.6361 -0.0624 -0.0282 0.0852  603 HOH A O   
3427 O O   . HOH D .   ? 0.4841 0.7087 0.5259 0.0241  -0.0079 0.2938  604 HOH A O   
3428 O O   . HOH D .   ? 0.7371 0.3658 0.6067 0.1455  0.1831  -0.0627 605 HOH A O   
3429 O O   . HOH D .   ? 0.5769 0.2205 0.7297 -0.1192 -0.0473 0.0647  606 HOH A O   
3430 O O   . HOH D .   ? 0.4314 0.4513 0.4448 0.0266  0.0407  0.0338  607 HOH A O   
3431 O O   . HOH D .   ? 0.7189 0.5379 0.5023 0.1682  -0.0360 -0.0802 608 HOH A O   
3432 O O   . HOH D .   ? 0.5642 0.5373 0.6025 -0.1056 0.0248  -0.2194 609 HOH A O   
3433 O O   . HOH D .   ? 0.8616 0.1971 1.0213 0.1597  0.0922  0.0766  610 HOH A O   
3434 O O   . HOH D .   ? 0.4636 0.2582 0.4842 0.0393  0.0191  0.1431  611 HOH A O   
3435 O O   . HOH D .   ? 0.6588 0.3782 0.5083 0.1494  0.0927  0.0806  612 HOH A O   
3436 O O   . HOH D .   ? 0.5728 0.2303 0.3770 -0.0088 0.0304  -0.0486 613 HOH A O   
3437 O O   . HOH D .   ? 0.4310 0.2342 0.3151 0.0077  0.0005  -0.0008 614 HOH A O   
3438 O O   . HOH D .   ? 0.4541 0.3400 0.3849 -0.0194 -0.0360 0.0606  615 HOH A O   
3439 O O   . HOH D .   ? 0.3825 0.2998 0.6397 -0.0188 0.0805  -0.0548 616 HOH A O   
3440 O O   . HOH D .   ? 0.5955 0.2655 0.6984 0.0094  -0.0966 0.0468  617 HOH A O   
3442 O O   . HOH D .   ? 0.6946 0.6015 0.4471 0.1616  -0.0887 0.0266  619 HOH A O   
3443 O O   . HOH D .   ? 0.4330 0.1007 0.4156 0.0265  0.0112  0.0606  620 HOH A O   
3444 O O   . HOH D .   ? 0.4241 0.1979 0.2940 0.0570  -0.0088 0.0175  621 HOH A O   
3445 O O   . HOH D .   ? 0.7104 0.2597 0.5149 0.0876  0.0174  0.1288  622 HOH A O   
3446 O O   . HOH D .   ? 0.4491 0.2992 0.8374 0.0039  -0.0564 -0.0608 623 HOH A O   
3447 O O   . HOH D .   ? 0.3804 0.5283 0.6541 0.1050  0.0438  0.0950  624 HOH A O   
3448 O O   . HOH D .   ? 0.5602 0.6863 0.5246 -0.0258 0.0302  -0.0305 625 HOH A O   
3449 O O   . HOH D .   ? 0.4575 0.5392 0.9153 0.0093  0.0524  0.1290  626 HOH A O   
3450 O O   . HOH D .   ? 0.3613 0.1943 0.2691 0.0082  0.0008  0.0479  627 HOH A O   
3451 O O   . HOH D .   ? 0.7223 0.4469 0.4275 -0.0194 0.1365  -0.0669 628 HOH A O   
3452 O O   . HOH D .   ? 0.5237 0.2822 0.5264 -0.0094 -0.1790 0.0186  629 HOH A O   
3453 O O   . HOH D .   ? 0.6169 0.4329 0.5267 -0.0111 0.0213  0.0712  630 HOH A O   
3454 O O   . HOH D .   ? 0.4258 0.3145 0.3101 0.0396  0.0145  -0.0477 631 HOH A O   
3455 O O   . HOH D .   ? 0.4630 0.7850 0.3728 0.0725  -0.0199 0.1622  632 HOH A O   
3456 O O   . HOH D .   ? 0.3608 0.0470 0.2698 0.0220  -0.0090 0.0443  633 HOH A O   
3457 O O   . HOH D .   ? 0.4435 0.2524 0.7665 0.0373  0.0224  -0.0128 634 HOH A O   
3458 O O   . HOH D .   ? 0.4628 0.4437 0.4680 0.0992  0.0492  0.0178  635 HOH A O   
3459 O O   . HOH D .   ? 0.4014 0.1098 0.3113 0.0019  -0.0528 0.0391  636 HOH A O   
3460 O O   . HOH D .   ? 0.4893 0.3098 0.4310 -0.0091 0.0199  0.0385  637 HOH A O   
3461 O O   . HOH D .   ? 0.7421 0.2032 0.6878 0.0280  -0.0653 0.0652  638 HOH A O   
3462 O O   . HOH D .   ? 0.7302 0.8394 0.3818 -0.0532 -0.1313 -0.0295 639 HOH A O   
3463 O O   . HOH D .   ? 0.4748 0.0789 0.4711 -0.0057 -0.0073 0.0092  640 HOH A O   
3464 O O   . HOH D .   ? 0.4061 0.3006 0.3746 0.0609  0.0496  0.1267  641 HOH A O   
3465 O O   . HOH D .   ? 0.3848 0.1561 0.3878 0.0453  0.0162  0.0585  642 HOH A O   
3466 O O   . HOH D .   ? 0.5929 0.4559 0.6202 -0.0059 0.0589  0.0970  643 HOH A O   
3467 O O   . HOH D .   ? 0.4765 0.1327 0.4493 -0.0228 0.0103  0.0099  644 HOH A O   
3468 O O   . HOH D .   ? 0.4711 0.1506 0.3429 0.0143  -0.0066 -0.0040 645 HOH A O   
3469 O O   . HOH D .   ? 0.7071 0.4942 0.6340 -0.2051 -0.1748 -0.0280 646 HOH A O   
3470 O O   . HOH D .   ? 0.4254 0.2845 0.6131 -0.0207 -0.0033 0.1792  647 HOH A O   
3471 O O   . HOH D .   ? 0.5688 0.1382 0.9714 0.0667  0.0887  0.0487  648 HOH A O   
3472 O O   . HOH D .   ? 0.4312 0.1176 0.3991 0.0057  0.0156  0.0933  649 HOH A O   
3473 O O   . HOH D .   ? 0.4318 0.2292 0.3444 -0.0015 0.0099  0.0729  650 HOH A O   
3474 O O   . HOH D .   ? 0.4318 0.2428 0.3576 0.0431  0.0557  -0.0025 651 HOH A O   
3475 O O   . HOH D .   ? 0.4723 0.2801 0.4126 0.0010  0.0102  -0.0559 652 HOH A O   
3476 O O   . HOH D .   ? 0.4472 0.4549 0.5703 0.1092  -0.1072 -0.1333 653 HOH A O   
3477 O O   . HOH D .   ? 0.4840 0.1321 0.3777 0.0182  -0.0038 0.0617  654 HOH A O   
3478 O O   . HOH D .   ? 0.6191 0.3897 0.4760 0.2305  0.0609  0.1327  655 HOH A O   
3479 O O   . HOH D .   ? 0.3792 0.2859 0.4813 -0.0622 0.0376  0.0402  656 HOH A O   
3480 O O   . HOH D .   ? 0.3600 0.1750 0.3130 -0.0403 -0.0532 0.0281  657 HOH A O   
3481 O O   . HOH D .   ? 0.4100 0.1159 0.3790 0.0596  0.0155  -0.0129 658 HOH A O   
3482 O O   . HOH D .   ? 0.5603 0.2900 0.4705 -0.0710 0.0551  -0.0865 659 HOH A O   
3483 O O   . HOH D .   ? 0.4531 0.1809 0.3347 -0.0094 0.0454  0.0012  660 HOH A O   
3484 O O   . HOH D .   ? 0.4689 0.2991 0.5249 0.0073  -0.0073 -0.0748 661 HOH A O   
3485 O O   . HOH D .   ? 0.6585 0.5221 0.5698 -0.0561 -0.0421 -0.0782 662 HOH A O   
3486 O O   . HOH D .   ? 0.5505 0.3764 0.5594 -0.0352 0.0551  0.0309  663 HOH A O   
3487 O O   . HOH D .   ? 0.4849 0.5917 0.6605 -0.0624 0.0647  -0.1587 664 HOH A O   
3488 O O   . HOH D .   ? 0.3572 0.1003 0.3156 0.0076  -0.0087 -0.0115 665 HOH A O   
3489 O O   . HOH D .   ? 0.4103 0.2366 0.4527 0.0105  0.0121  0.1118  666 HOH A O   
3490 O O   . HOH D .   ? 0.3967 0.2688 0.5652 0.0258  -0.0140 0.1342  667 HOH A O   
3491 O O   . HOH D .   ? 0.5720 0.3703 0.5794 0.0115  0.0306  -0.0259 668 HOH A O   
3492 O O   . HOH D .   ? 0.4878 0.5005 0.5378 0.0023  0.0072  0.1652  669 HOH A O   
3493 O O   . HOH D .   ? 0.6191 0.4868 0.8604 0.0560  -0.0502 -0.1399 670 HOH A O   
3494 O O   . HOH D .   ? 0.5320 0.1257 0.6097 -0.0859 -0.0361 0.0270  671 HOH A O   
3495 O O   . HOH D .   ? 1.0655 0.6445 0.4744 0.3494  -0.1269 0.0818  672 HOH A O   
3496 O O   . HOH D .   ? 0.3262 0.4012 0.4225 0.0555  -0.0371 0.0642  673 HOH A O   
3497 O O   . HOH D .   ? 0.5734 0.4175 0.5294 0.0081  -0.0372 0.2181  674 HOH A O   
3498 O O   . HOH D .   ? 0.4584 0.2177 0.4060 0.0023  0.0325  0.0857  675 HOH A O   
3499 O O   . HOH D .   ? 0.5367 0.4571 0.5922 -0.0481 -0.0028 0.2758  676 HOH A O   
3500 O O   . HOH D .   ? 0.4231 0.2446 0.3887 -0.0637 -0.0164 0.0355  677 HOH A O   
3501 O O   . HOH D .   ? 0.4492 0.7104 0.5170 -0.0174 -0.0261 -0.0590 678 HOH A O   
3502 O O   . HOH D .   ? 0.4030 0.1832 0.3386 0.0101  -0.0083 0.0309  679 HOH A O   
3503 O O   . HOH D .   ? 0.5140 0.4014 0.4845 0.1067  -0.0797 -0.0029 680 HOH A O   
3504 O O   . HOH D .   ? 0.3336 0.2565 0.2755 -0.0075 -0.0393 0.0400  681 HOH A O   
3505 O O   . HOH D .   ? 0.5247 0.2447 0.5049 0.0154  0.0485  -0.0090 682 HOH A O   
3506 O O   . HOH D .   ? 0.5631 0.3599 0.4198 0.1287  0.0074  -0.0021 683 HOH A O   
3507 O O   . HOH D .   ? 0.6786 0.2767 0.5212 0.0895  0.1407  0.0481  684 HOH A O   
3508 O O   . HOH D .   ? 0.4986 0.2708 0.4674 0.0755  0.0476  0.0902  685 HOH A O   
3509 O O   . HOH D .   ? 0.5632 0.4574 0.4652 0.0333  0.0373  -0.0110 686 HOH A O   
3510 O O   . HOH D .   ? 0.5652 0.3434 0.4486 0.0127  0.0456  0.0681  687 HOH A O   
3511 O O   . HOH D .   ? 0.3836 0.1064 0.2968 -0.0232 -0.0267 0.0579  688 HOH A O   
3512 O O   . HOH D .   ? 0.4668 0.1210 0.3140 0.0209  0.0114  0.0030  689 HOH A O   
3513 O O   . HOH D .   ? 0.4384 0.4276 0.5553 -0.0660 -0.0110 -0.0522 690 HOH A O   
3514 O O   . HOH D .   ? 0.3845 0.1760 0.2870 -0.0164 -0.0583 0.0616  691 HOH A O   
3515 O O   . HOH D .   ? 0.6140 0.5240 0.4219 -0.0238 0.0984  0.0201  692 HOH A O   
3516 O O   . HOH D .   ? 0.4276 0.0750 0.3822 0.0321  0.0017  0.0448  693 HOH A O   
3517 O O   . HOH D .   ? 0.3748 0.3604 0.4280 -0.0518 -0.0147 0.0095  694 HOH A O   
3518 O O   . HOH D .   ? 0.6400 0.2278 0.6053 -0.1741 -0.1900 0.0342  695 HOH A O   
3519 O O   . HOH D .   ? 0.6283 0.3026 0.3472 0.1227  0.0594  0.0064  696 HOH A O   
3520 O O   . HOH D .   ? 0.5343 0.4654 0.4159 0.0559  0.0628  -0.0023 697 HOH A O   
3521 O O   . HOH D .   ? 0.8386 0.5861 0.5537 0.1379  -0.2220 -0.1542 698 HOH A O   
3522 O O   . HOH D .   ? 0.3447 0.1759 0.3232 -0.0572 0.0126  -0.0316 699 HOH A O   
3523 O O   . HOH D .   ? 0.3642 0.5004 0.4047 -0.0474 -0.0183 -0.0119 700 HOH A O   
3524 O O   . HOH D .   ? 0.4034 0.2484 0.3134 0.0259  -0.0277 0.0655  701 HOH A O   
3525 O O   . HOH D .   ? 0.7602 0.2968 0.6094 -0.0181 0.1032  -0.0719 702 HOH A O   
3526 O O   . HOH D .   ? 0.4146 0.4615 0.2782 -0.0227 0.0363  0.0794  703 HOH A O   
3527 O O   . HOH D .   ? 0.5009 0.0678 0.4405 0.0445  -0.0263 -0.0493 704 HOH A O   
3528 O O   . HOH D .   ? 0.5247 0.1797 0.4477 -0.0093 -0.0180 0.0560  705 HOH A O   
3529 O O   . HOH D .   ? 0.6784 0.3210 0.4433 0.1192  0.1403  0.0660  706 HOH A O   
3530 O O   . HOH D .   ? 0.3931 0.2732 0.2974 0.0121  -0.0024 0.0449  707 HOH A O   
3531 O O   . HOH D .   ? 0.4571 0.2131 0.4853 0.0389  0.0087  0.1107  708 HOH A O   
3532 O O   . HOH D .   ? 0.4881 0.3019 0.4542 0.0495  -0.0174 0.1023  709 HOH A O   
3533 O O   . HOH D .   ? 0.3811 0.2101 0.4559 0.0423  0.0571  0.0251  710 HOH A O   
3534 O O   . HOH D .   ? 0.3553 0.7587 0.4230 0.0029  -0.0548 0.0103  711 HOH A O   
3535 O O   . HOH D .   ? 0.5068 0.5387 0.4170 0.0174  -0.0185 0.1544  712 HOH A O   
3536 O O   . HOH D .   ? 0.3328 0.0832 0.3183 0.0280  -0.0546 0.0408  713 HOH A O   
3537 O O   . HOH D .   ? 0.6509 0.2254 0.7249 0.1280  0.1746  0.2479  714 HOH A O   
3538 O O   . HOH D .   ? 0.4627 0.1005 0.4859 0.0053  0.0163  0.0462  715 HOH A O   
3539 O O   . HOH D .   ? 0.3895 0.2032 0.5308 -0.0253 -0.0307 -0.0218 716 HOH A O   
3540 O O   . HOH D .   ? 0.4333 0.3932 0.4986 -0.0176 -0.0969 -0.1206 717 HOH A O   
3541 O O   . HOH D .   ? 0.5495 0.2601 0.4869 -0.0339 0.0009  -0.1179 718 HOH A O   
3542 O O   . HOH D .   ? 0.5818 0.7154 0.3942 0.1372  0.0250  0.0983  719 HOH A O   
3543 O O   . HOH D .   ? 0.7318 0.4173 0.5792 -0.0725 0.0545  -0.1479 720 HOH A O   
3544 O O   . HOH D .   ? 0.4923 0.2307 0.5115 0.0107  0.0110  0.0332  721 HOH A O   
3545 O O   . HOH D .   ? 0.5264 0.3633 0.4798 0.0739  0.0773  0.0892  722 HOH A O   
3546 O O   . HOH D .   ? 0.5421 0.3770 0.4393 0.0197  0.0380  -0.0051 723 HOH A O   
3547 O O   . HOH D .   ? 0.4300 0.2849 0.4910 -0.0376 -0.0249 -0.0777 724 HOH A O   
3548 O O   . HOH D .   ? 0.5995 0.4984 0.5198 -0.0800 0.0552  0.0228  725 HOH A O   
3549 O O   . HOH D .   ? 0.5057 0.2961 0.6051 -0.0201 -0.0476 0.1620  726 HOH A O   
3550 O O   . HOH D .   ? 0.4008 0.2041 0.3473 -0.0480 0.0265  0.0399  727 HOH A O   
3551 O O   . HOH D .   ? 0.3937 0.2405 0.4685 -0.0059 -0.0390 0.0018  728 HOH A O   
3552 O O   . HOH D .   ? 0.4300 0.2400 0.2872 0.0047  -0.0344 0.0822  729 HOH A O   
3553 O O   . HOH D .   ? 0.5663 0.2150 0.5092 0.0165  -0.0601 0.1108  730 HOH A O   
3554 O O   . HOH D .   ? 0.5221 0.3085 0.4051 -0.0267 0.0641  -0.0072 731 HOH A O   
3555 O O   . HOH D .   ? 0.6323 0.3018 0.4729 -0.1455 0.0078  -0.0492 732 HOH A O   
3556 O O   . HOH D .   ? 0.6281 0.6006 0.4099 -0.0691 0.0275  0.1037  733 HOH A O   
3557 O O   . HOH D .   ? 0.3242 0.0747 0.2841 -0.0230 -0.0054 -0.0025 734 HOH A O   
3558 O O   . HOH D .   ? 0.8478 0.7788 0.3588 0.3348  -0.0695 -0.0641 735 HOH A O   
3559 O O   . HOH D .   ? 0.7131 0.2251 0.5296 0.0083  -0.0402 0.0561  736 HOH A O   
3560 O O   . HOH D .   ? 0.4099 0.4404 0.6084 0.0146  -0.0306 -0.0186 737 HOH A O   
3561 O O   . HOH D .   ? 0.5383 0.5748 0.7150 0.0991  0.1205  0.0444  738 HOH A O   
3562 O O   . HOH D .   ? 0.5586 0.5253 0.3505 -0.0767 0.0486  0.0456  739 HOH A O   
3563 O O   . HOH D .   ? 0.4392 0.2405 0.3843 -0.0246 -0.0082 0.0823  740 HOH A O   
3564 O O   . HOH D .   ? 0.7292 0.2894 0.4750 0.0416  -0.0078 0.0945  741 HOH A O   
3565 O O   . HOH D .   ? 0.6220 0.5652 0.3400 0.1679  0.0055  -0.0917 742 HOH A O   
3566 O O   . HOH D .   ? 0.3295 0.1068 0.2496 -0.0446 -0.0138 0.0232  743 HOH A O   
3567 O O   . HOH D .   ? 0.5520 0.4827 0.3949 -0.0553 0.0007  0.0891  744 HOH A O   
3568 O O   . HOH D .   ? 0.4376 0.1697 0.3396 -0.0381 -0.0510 0.0536  745 HOH A O   
3569 O O   . HOH D .   ? 0.4602 0.3518 0.4496 -0.0214 0.0304  0.0441  746 HOH A O   
3570 O O   . HOH D .   ? 0.3963 0.3116 0.4735 0.0534  -0.0262 -0.0525 747 HOH A O   
3571 O O   . HOH D .   ? 0.5380 0.5242 0.3962 0.0368  -0.0264 0.1859  748 HOH A O   
3572 O O   . HOH D .   ? 0.5156 0.3282 0.3782 0.0082  0.0046  0.1452  749 HOH A O   
3573 O O   . HOH D .   ? 0.7011 0.2812 0.6509 0.1883  0.0858  0.1153  750 HOH A O   
3574 O O   . HOH D .   ? 0.3607 0.2094 0.3591 -0.0409 0.0145  0.0475  751 HOH A O   
3575 O O   . HOH D .   ? 0.5312 0.3711 0.3665 0.0057  -0.0376 0.1783  752 HOH A O   
3576 O O   . HOH D .   ? 0.5014 0.2867 0.4105 -0.0416 0.0684  0.0132  753 HOH A O   
3577 O O   . HOH D .   ? 0.3886 0.1862 0.3949 -0.0300 -0.0557 0.0181  754 HOH A O   
3578 O O   . HOH D .   ? 0.3791 0.3343 0.5280 -0.0954 -0.0326 0.1753  755 HOH A O   
3579 O O   . HOH D .   ? 0.7371 0.4905 0.7717 -0.2662 0.1021  -0.0830 756 HOH A O   
3580 O O   . HOH D .   ? 0.3943 0.4994 0.4836 -0.0497 -0.1453 0.1001  757 HOH A O   
3581 O O   . HOH D .   ? 0.4104 0.2577 0.2586 0.0459  -0.0056 0.0031  758 HOH A O   
3582 O O   . HOH D .   ? 0.4798 0.3434 0.5578 -0.0489 -0.0287 -0.1066 759 HOH A O   
3583 O O   . HOH D .   ? 0.4453 0.4374 0.4805 0.0089  -0.0426 -0.1057 760 HOH A O   
3584 O O   . HOH D .   ? 0.8054 0.3738 0.3963 -0.1937 -0.0933 0.0273  761 HOH A O   
3585 O O   . HOH D .   ? 0.4962 0.2249 0.4157 -0.0394 -0.0128 -0.0236 762 HOH A O   
3586 O O   . HOH D .   ? 0.8050 0.3528 0.5279 0.1071  -0.0562 0.0122  763 HOH A O   
3587 O O   . HOH D .   ? 0.3799 0.2272 0.4033 0.0514  -0.0275 -0.0414 764 HOH A O   
3588 O O   . HOH D .   ? 0.4695 0.4287 0.7442 -0.0071 -0.0467 0.1266  765 HOH A O   
3589 O O   . HOH D .   ? 0.3808 0.6077 0.3479 -0.0002 -0.0354 -0.0227 766 HOH A O   
3590 O O   . HOH D .   ? 0.6386 0.3789 0.6326 -0.0994 0.1097  -0.0008 767 HOH A O   
3591 O O   . HOH D .   ? 0.4695 0.2702 0.5272 0.0369  0.0303  0.0242  768 HOH A O   
3592 O O   . HOH D .   ? 0.7644 0.4554 0.8571 -0.0048 0.0798  -0.0420 769 HOH A O   
3593 O O   . HOH D .   ? 0.3801 0.2660 0.3722 -0.0036 -0.0349 0.1008  770 HOH A O   
3594 O O   . HOH D .   ? 0.4390 0.1999 0.4596 0.0921  0.0204  0.0435  771 HOH A O   
3595 O O   . HOH D .   ? 0.5036 0.9079 0.4182 -0.0460 0.0239  -0.2012 772 HOH A O   
3596 O O   . HOH D .   ? 0.4421 0.4832 0.3167 0.0764  0.0461  0.1057  773 HOH A O   
3597 O O   . HOH D .   ? 0.3149 0.1397 0.3068 -0.0012 -0.0009 0.0292  774 HOH A O   
3598 O O   . HOH D .   ? 0.3360 0.1903 0.3172 0.0252  -0.0001 0.0355  775 HOH A O   
3599 O O   . HOH D .   ? 0.4222 0.2711 0.3289 0.0146  0.0044  0.0447  776 HOH A O   
3600 O O   . HOH D .   ? 0.6251 0.2518 0.5417 -0.0314 0.0719  -0.0213 777 HOH A O   
3601 O O   . HOH D .   ? 0.3924 0.1186 0.3092 0.0229  -0.0526 0.0352  778 HOH A O   
3602 O O   . HOH D .   ? 0.5008 0.5437 0.5062 0.0215  0.0404  -0.0382 779 HOH A O   
3603 O O   . HOH D .   ? 0.6020 0.2886 0.7131 -0.0267 -0.0486 0.0623  780 HOH A O   
3604 O O   . HOH D .   ? 0.4366 0.7856 0.3379 0.0657  0.0356  0.0586  781 HOH A O   
3605 O O   . HOH D .   ? 0.4930 0.2120 0.4681 -0.0333 -0.0234 -0.0527 782 HOH A O   
3606 O O   . HOH D .   ? 0.4903 0.7706 0.5260 -0.0382 0.0024  0.1436  783 HOH A O   
3607 O O   . HOH D .   ? 0.5556 0.3249 0.4739 0.0931  -0.0040 0.0158  784 HOH A O   
3608 O O   . HOH D .   ? 0.3635 0.3365 0.4903 0.0349  -0.0203 0.0785  785 HOH A O   
3609 O O   . HOH D .   ? 0.4641 0.3769 0.3520 -0.0465 -0.0286 -0.0098 786 HOH A O   
3610 O O   . HOH D .   ? 0.5080 0.3495 0.4799 0.1521  -0.0474 0.0493  787 HOH A O   
3611 O O   . HOH D .   ? 0.5077 0.3173 0.5051 -0.0297 0.1060  -0.0525 788 HOH A O   
3612 O O   . HOH D .   ? 0.4326 0.3997 0.5602 -0.0673 -0.0803 0.0200  789 HOH A O   
3613 O O   . HOH D .   ? 0.5532 0.4908 0.5648 -0.1499 -0.0536 0.2216  790 HOH A O   
3614 O O   . HOH D .   ? 0.4228 0.5314 0.4345 -0.0598 -0.0603 0.1087  791 HOH A O   
3615 O O   . HOH D .   ? 0.3708 0.2469 0.3893 -0.0171 0.0091  0.0993  792 HOH A O   
3616 O O   . HOH D .   ? 0.5168 0.7304 0.5124 0.1052  0.0218  0.0361  793 HOH A O   
3617 O O   . HOH D .   ? 0.4877 0.1694 0.3579 0.0115  -0.0800 -0.0534 794 HOH A O   
3618 O O   . HOH D .   ? 0.4964 0.3197 0.5230 0.0262  0.0285  0.0152  795 HOH A O   
3619 O O   . HOH D .   ? 0.5729 0.1576 0.5548 0.1366  -0.0375 -0.0555 796 HOH A O   
3620 O O   . HOH D .   ? 0.4877 0.1371 0.3846 -0.0620 -0.0076 0.0016  797 HOH A O   
3621 O O   . HOH D .   ? 0.3680 0.1735 0.3651 -0.0036 0.0381  0.0443  798 HOH A O   
3623 O O   . HOH D .   ? 0.4678 0.1881 0.4310 0.0175  0.0594  0.0389  800 HOH A O   
3624 O O   . HOH D .   ? 0.4877 0.3451 0.4887 0.0009  -0.0038 -0.0245 801 HOH A O   
3625 O O   . HOH D .   ? 0.3924 0.4190 0.4851 0.0038  -0.0328 -0.0576 802 HOH A O   
3626 O O   . HOH D .   ? 0.5594 0.5695 0.4139 -0.0349 0.0423  0.0894  803 HOH A O   
3627 O O   . HOH D .   ? 0.5729 0.6094 0.5241 0.0599  0.0658  0.0757  804 HOH A O   
3628 O O   . HOH D .   ? 0.3409 0.0827 0.3733 -0.0572 0.0136  0.0545  805 HOH A O   
3629 O O   . HOH D .   ? 0.5351 0.3918 0.5735 -0.0901 0.0095  -0.0383 806 HOH A O   
3630 O O   . HOH D .   ? 0.5077 0.4116 0.3199 0.0163  0.0435  0.0634  807 HOH A O   
3631 O O   . HOH D .   ? 0.6216 0.3678 0.6561 0.1390  0.0593  0.1051  808 HOH A O   
3632 O O   . HOH D .   ? 0.4682 0.1563 0.4816 -0.0130 -0.1111 -0.0255 809 HOH A O   
3633 O O   . HOH D .   ? 0.5205 0.2462 0.3563 -0.0402 -0.0417 0.0062  810 HOH A O   
3634 O O   . HOH D .   ? 0.3825 0.0709 0.5378 -0.0152 -0.0648 0.0877  811 HOH A O   
3635 O O   . HOH D .   ? 0.6832 0.3659 0.5520 0.0954  -0.1894 0.0539  812 HOH A O   
3636 O O   . HOH D .   ? 0.7378 0.4801 0.4553 0.2448  -0.0417 -0.1316 813 HOH A O   
3637 O O   . HOH D .   ? 0.6623 0.6035 0.5225 0.0976  -0.0382 0.1988  814 HOH A O   
3638 O O   . HOH D .   ? 0.3983 0.1770 0.3028 -0.0372 0.0116  0.0190  815 HOH A O   
3639 O O   . HOH D .   ? 0.4326 0.2975 0.3614 -0.0027 0.0264  0.0030  816 HOH A O   
3640 O O   . HOH D .   ? 0.6352 0.2800 0.5103 -0.0230 -0.0105 -0.1110 817 HOH A O   
3641 O O   . HOH D .   ? 0.3991 0.1647 0.3825 0.0155  -0.0412 0.0234  818 HOH A O   
3642 O O   . HOH D .   ? 0.4201 0.5428 0.5912 -0.1351 -0.0224 0.1124  819 HOH A O   
3643 O O   . HOH D .   ? 0.3481 0.1004 0.2962 -0.0380 0.0042  0.0424  820 HOH A O   
3644 O O   . HOH D .   ? 0.5305 0.2583 0.4577 -0.0754 -0.0456 -0.0059 821 HOH A O   
3645 O O   . HOH D .   ? 0.3526 0.1449 0.2751 -0.0317 0.0272  -0.0054 822 HOH A O   
3646 O O   . HOH D .   ? 0.5064 0.1610 0.4490 0.0188  0.0066  0.0094  823 HOH A O   
3647 O O   . HOH D .   ? 0.3432 0.2872 0.5095 -0.0013 0.0398  0.0616  824 HOH A O   
3648 O O   . HOH D .   ? 0.4932 0.3906 0.5631 -0.0424 -0.0638 0.2497  825 HOH A O   
3649 O O   . HOH D .   ? 0.5310 0.4624 0.5379 -0.0719 -0.0898 0.0591  826 HOH A O   
3650 O O   . HOH D .   ? 0.6668 0.4350 0.4835 -0.0779 0.0642  -0.1049 827 HOH A O   
3651 O O   . HOH D .   ? 0.3615 0.1241 0.4933 0.0355  0.0332  0.0608  828 HOH A O   
3652 O O   . HOH D .   ? 0.8123 0.1693 0.7758 0.0135  -0.0616 0.1483  829 HOH A O   
3653 O O   . HOH D .   ? 0.3675 0.5210 0.3926 0.1027  0.0724  0.1100  830 HOH A O   
3654 O O   . HOH D .   ? 0.4426 0.3117 0.6289 -0.0697 0.1292  -0.0590 831 HOH A O   
3655 O O   . HOH D .   ? 0.4590 0.1281 0.4966 -0.0329 -0.0085 -0.0012 832 HOH A O   
3656 O O   . HOH D .   ? 0.8761 0.1262 0.3354 -0.0427 0.0751  0.0269  833 HOH A O   
3657 O O   . HOH D .   ? 0.6051 0.5203 0.5758 0.0708  0.0867  -0.0022 834 HOH A O   
3658 O O   . HOH D .   ? 0.5209 0.2089 0.6024 0.0065  -0.0300 -0.0007 835 HOH A O   
3659 O O   . HOH D .   ? 0.5345 0.2418 0.5829 0.0332  0.0836  0.0787  836 HOH A O   
3660 O O   . HOH D .   ? 0.5593 0.3090 0.4368 -0.0712 -0.0094 0.0580  837 HOH A O   
3661 O O   . HOH D .   ? 0.5520 0.5662 0.4867 -0.1618 0.0469  0.0998  838 HOH A O   
3662 O O   . HOH D .   ? 0.4298 0.3645 0.2990 -0.0294 -0.0050 0.0171  839 HOH A O   
3663 O O   . HOH D .   ? 0.4361 0.3511 0.4219 0.0034  0.0279  0.0170  840 HOH A O   
3664 O O   . HOH D .   ? 0.6428 0.3600 0.5679 0.1410  0.0903  0.0052  841 HOH A O   
3665 O O   . HOH D .   ? 0.5405 0.5396 0.6059 0.0434  0.0308  0.0506  842 HOH A O   
3666 O O   . HOH D .   ? 0.3811 0.4531 0.4099 -0.0776 -0.0281 0.1388  843 HOH A O   
3667 O O   . HOH D .   ? 0.6103 0.1782 0.6435 0.0036  0.0170  -0.0571 844 HOH A O   
3668 O O   . HOH D .   ? 0.4066 0.8006 0.4774 0.1011  0.0280  0.3000  845 HOH A O   
3669 O O   . HOH D .   ? 0.6273 0.3510 0.8842 0.0223  0.1624  -0.0708 846 HOH A O   
3670 O O   . HOH D .   ? 0.7905 0.1541 0.2997 -0.1326 0.0722  0.0469  847 HOH A O   
3671 O O   . HOH D .   ? 0.7984 0.8405 0.5256 0.1508  -0.1944 -0.1865 848 HOH A O   
3672 O O   . HOH D .   ? 0.5370 0.4321 0.7288 0.0725  -0.0038 0.1917  849 HOH A O   
3673 O O   . HOH D .   ? 0.6169 0.2018 0.7591 -0.0948 -0.0065 0.1049  850 HOH A O   
3674 O O   . HOH D .   ? 0.5963 0.2774 0.5752 -0.0418 0.0495  -0.1743 851 HOH A O   
3675 O O   . HOH D .   ? 0.6876 0.5320 0.4534 -0.0028 0.0063  -0.0612 852 HOH A O   
3676 O O   . HOH D .   ? 0.6224 0.6958 0.5603 0.0209  0.0674  -0.0843 853 HOH A O   
3677 O O   . HOH D .   ? 0.5188 0.2818 0.4554 -0.0656 -0.0238 0.0107  854 HOH A O   
3678 O O   . HOH D .   ? 0.5519 0.5394 0.4387 -0.1593 -0.0896 0.1073  855 HOH A O   
3679 O O   . HOH D .   ? 0.6605 0.3207 1.0291 0.0246  -0.0544 0.0910  856 HOH A O   
3680 O O   . HOH D .   ? 0.9167 0.2565 0.6428 0.0676  0.1592  -0.0654 857 HOH A O   
3681 O O   . HOH D .   ? 0.5972 0.2558 0.3437 0.0152  -0.0504 0.0402  858 HOH A O   
3682 O O   . HOH D .   ? 0.6150 0.5103 0.5943 -0.0499 -0.0027 -0.0222 859 HOH A O   
3683 O O   . HOH D .   ? 0.5515 0.5064 0.5506 -0.0946 0.0092  0.0041  860 HOH A O   
3684 O O   . HOH D .   ? 0.6718 0.4658 0.6784 0.1297  0.1864  0.1275  861 HOH A O   
3686 O O   . HOH D .   ? 0.5009 0.5221 0.5294 0.0114  0.0281  0.0961  863 HOH A O   
3687 O O   . HOH D .   ? 0.5248 0.5444 0.5035 -0.0026 0.0133  0.0717  864 HOH A O   
3688 O O   . HOH D .   ? 0.8638 0.6125 0.7365 0.0355  0.0545  0.0292  865 HOH A O   
3689 O O   . HOH D .   ? 0.6358 0.1850 0.4653 0.0508  0.0518  -0.0887 866 HOH A O   
3690 O O   . HOH D .   ? 0.8831 0.0887 0.6155 0.1266  0.1970  0.0601  867 HOH A O   
3691 O O   . HOH D .   ? 0.5560 0.5474 0.6435 0.1427  0.0000  0.0285  868 HOH A O   
3692 O O   . HOH D .   ? 0.8904 0.2445 0.6051 -0.0098 0.0717  0.0634  869 HOH A O   
3693 O O   . HOH D .   ? 0.7094 0.3190 0.5682 -0.1762 -0.0507 0.0207  870 HOH A O   
3694 O O   . HOH D .   ? 0.5278 0.4956 0.5385 -0.0380 0.0206  -0.1309 871 HOH A O   
3695 O O   . HOH D .   ? 0.6175 0.4133 0.6241 -0.0788 0.0304  -0.1315 872 HOH A O   
3696 O O   . HOH D .   ? 0.7255 0.5334 0.7914 -0.1771 0.0275  0.1720  873 HOH A O   
3697 O O   . HOH D .   ? 0.4627 0.5199 0.8704 0.0016  -0.1694 0.1174  874 HOH A O   
3698 O O   . HOH D .   ? 0.5741 0.5511 0.5778 -0.1361 0.0153  -0.1072 875 HOH A O   
3700 O O   . HOH D .   ? 0.5223 0.4386 0.4768 0.0982  0.0320  0.0587  877 HOH A O   
3701 O O   . HOH D .   ? 0.5953 0.7926 0.4834 -0.0052 -0.0533 0.1058  878 HOH A O   
3702 O O   . HOH D .   ? 0.6372 0.4782 0.6312 -0.0192 -0.0344 -0.0252 879 HOH A O   
3703 O O   . HOH D .   ? 0.5746 0.4138 0.7547 -0.0130 0.0546  0.0119  880 HOH A O   
3704 O O   . HOH D .   ? 0.6112 0.5864 0.6134 -0.0236 -0.1037 -0.0226 881 HOH A O   
3705 O O   . HOH D .   ? 0.5176 0.1662 0.5892 0.0222  0.0651  0.1246  882 HOH A O   
3706 O O   . HOH D .   ? 0.6456 0.3488 0.4878 -0.1075 -0.0733 0.0375  883 HOH A O   
3707 O O   . HOH D .   ? 0.5615 0.1630 0.5170 0.0529  -0.1171 -0.0071 884 HOH A O   
3708 O O   . HOH D .   ? 0.6069 0.5144 0.6352 0.0081  -0.0085 0.0509  885 HOH A O   
3709 O O   . HOH D .   ? 0.4812 0.1870 0.4600 0.1011  0.0992  0.0956  886 HOH A O   
3710 O O   . HOH D .   ? 0.5927 0.3343 0.6297 0.0504  -0.0089 -0.0152 887 HOH A O   
3711 O O   . HOH D .   ? 0.5816 0.4782 0.4292 -0.0136 -0.0512 -0.0009 888 HOH A O   
3712 O O   . HOH D .   ? 0.5571 0.3871 0.5363 -0.0270 -0.0017 0.0009  889 HOH A O   
3713 O O   . HOH D .   ? 0.6702 0.1986 0.4817 0.0519  0.0729  -0.0001 890 HOH A O   
3714 O O   . HOH D .   ? 0.5464 0.6221 0.5308 -0.0831 -0.0048 0.0260  891 HOH A O   
3715 O O   . HOH D .   ? 0.7142 0.2894 0.5821 -0.0467 -0.1097 -0.0003 892 HOH A O   
3718 O O   . HOH D .   ? 0.5202 0.4845 0.5509 0.0788  -0.0127 -0.0116 895 HOH A O   
3719 O O   . HOH D .   ? 0.6468 0.6676 0.6263 -0.1458 -0.1115 0.3027  896 HOH A O   
3720 O O   . HOH D .   ? 0.3473 0.1960 0.4182 0.0387  0.0300  0.0716  897 HOH A O   
3721 O O   . HOH D .   ? 0.7146 0.5510 0.5781 0.1059  0.0791  0.2091  898 HOH A O   
3722 O O   . HOH D .   ? 0.5860 0.2784 0.5569 -0.0178 0.0059  0.1035  899 HOH A O   
3723 O O   . HOH D .   ? 0.6412 0.7992 0.7035 -0.2061 -0.0593 0.0066  900 HOH A O   
3724 O O   . HOH D .   ? 0.4677 0.4326 0.6129 0.0502  0.0506  0.1910  901 HOH A O   
3725 O O   . HOH D .   ? 0.7183 0.1514 0.5011 -0.0280 -0.0152 -0.0727 902 HOH A O   
3726 O O   . HOH D .   ? 0.5150 0.3400 0.5950 0.0611  0.0159  -0.2032 903 HOH A O   
3727 O O   . HOH D .   ? 0.4458 0.2594 0.5824 0.0203  0.0529  -0.0559 904 HOH A O   
3728 O O   . HOH D .   ? 0.6773 0.6343 0.6057 -0.0444 0.0155  -0.0118 905 HOH A O   
3729 O O   . HOH D .   ? 0.9291 0.5507 0.8911 -0.0610 0.4900  -0.0278 906 HOH A O   
3730 O O   . HOH D .   ? 0.8082 0.4288 0.7259 -0.0069 -0.0225 0.1943  907 HOH A O   
3731 O O   . HOH D .   ? 0.5342 0.4873 0.3647 0.0515  0.0049  -0.0941 908 HOH A O   
3732 O O   . HOH D .   ? 0.6154 0.2913 0.5855 -0.0564 -0.0188 -0.0020 909 HOH A O   
3733 O O   . HOH D .   ? 0.4429 0.5405 0.4340 0.0316  0.0349  0.0818  910 HOH A O   
3734 O O   . HOH D .   ? 0.6226 0.2769 0.5627 0.1548  -0.0839 0.0362  911 HOH A O   
3735 O O   . HOH D .   ? 0.5154 0.5598 0.5253 -0.0020 0.0522  -0.0237 912 HOH A O   
3736 O O   . HOH D .   ? 0.5984 0.4807 0.5162 0.0247  -0.0095 0.0546  913 HOH A O   
3737 O O   . HOH D .   ? 0.7645 1.0115 0.5587 0.2694  -0.0980 -0.0888 914 HOH A O   
3738 O O   . HOH D .   ? 0.4854 0.4213 0.5844 -0.0689 -0.0154 0.0168  915 HOH A O   
3739 O O   . HOH D .   ? 0.6576 0.6508 0.5848 -0.2028 -0.0272 0.2489  916 HOH A O   
3740 O O   . HOH D .   ? 0.5164 0.9889 0.3757 0.0216  0.0490  -0.0264 917 HOH A O   
3741 O O   . HOH D .   ? 0.9064 0.4351 0.6369 0.0233  -0.0130 0.1983  918 HOH A O   
3742 O O   . HOH D .   ? 0.6252 0.2999 0.5576 0.0428  -0.0668 -0.0727 919 HOH A O   
3743 O O   . HOH D .   ? 0.5665 0.4068 0.5523 -0.1122 0.0647  0.0035  920 HOH A O   
3744 O O   . HOH D .   ? 0.6206 0.5304 0.6192 0.0018  0.0749  0.0946  921 HOH A O   
3745 O O   . HOH D .   ? 0.5345 0.3678 0.6417 -0.0238 0.0091  -0.0196 922 HOH A O   
3746 O O   . HOH D .   ? 0.3998 0.3428 0.4195 0.0119  0.0458  -0.1271 923 HOH A O   
3747 O O   . HOH D .   ? 0.6507 0.3795 0.5465 0.0563  -0.0640 -0.0558 924 HOH A O   
3748 O O   . HOH D .   ? 0.5729 0.4160 0.5341 0.0708  -0.0594 0.0302  925 HOH A O   
3749 O O   . HOH D .   ? 0.6463 0.4503 0.4300 -0.0022 -0.1290 0.0244  926 HOH A O   
3750 O O   . HOH D .   ? 0.6095 0.5305 0.5150 0.0744  0.0232  -0.0434 927 HOH A O   
3751 O O   . HOH D .   ? 0.4708 0.5154 0.5437 -0.0903 -0.1143 0.0089  928 HOH A O   
3752 O O   . HOH D .   ? 0.5650 0.5900 0.6550 0.0724  0.0431  -0.1271 929 HOH A O   
3754 O O   . HOH D .   ? 0.4685 0.7166 0.3850 -0.0815 0.0113  -0.0262 931 HOH A O   
3755 O O   . HOH D .   ? 0.7733 0.1469 0.5708 -0.1254 0.1759  0.0403  932 HOH A O   
3756 O O   . HOH D .   ? 0.5027 0.4584 0.4669 0.0405  -0.0275 -0.0264 933 HOH A O   
3757 O O   . HOH D .   ? 0.7426 0.4209 0.7366 -0.1426 0.0775  0.0726  934 HOH A O   
3758 O O   . HOH D .   ? 0.6799 0.6671 0.4993 -0.0171 -0.0462 -0.1644 935 HOH A O   
3759 O O   . HOH D .   ? 0.6081 0.5435 0.4152 -0.0224 0.0015  0.0712  936 HOH A O   
3760 O O   . HOH D .   ? 0.6363 0.2520 0.7107 -0.0113 -0.0517 -0.1225 937 HOH A O   
3761 O O   . HOH D .   ? 0.6922 0.7515 0.6546 0.2748  -0.0403 -0.0987 938 HOH A O   
# 
