data_8Y9Q
# 
_entry.id   8Y9Q 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8Y9Q         pdb_00008y9q 10.2210/pdb8y9q/pdb 
WWPDB D_1300044001 ?            ?                   
# 
_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       2025-02-12 
# 
_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                        8Y9Q 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-07 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              chnji@fudan.edu.cn 
_pdbx_contact_author.name_first         Chaoneng 
_pdbx_contact_author.name_last          Ji 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5457-5067 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Guo, Y.'  1 0000-0002-4146-5168 
'Chen, A.' 2 ?                   
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Biochem.Biophys.Res.Commun. 
_citation.journal_id_ASTM           BBRCA9 
_citation.journal_id_CSD            0146 
_citation.journal_id_ISSN           1090-2104 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            732 
_citation.language                  ? 
_citation.page_first                150405 
_citation.page_last                 150405 
_citation.title                     
'Structural insights and functional characterization of a novel beta-glucosidase derived from Thermotoga profunda.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bbrc.2024.150405 
_citation.pdbx_database_id_PubMed   39033552 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Guo, Y.'  1 ? 
primary 'Chen, A.' 2 ? 
primary 'Liu, K.'  3 ? 
primary 'Ji, C.'   4 ? 
# 
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 b-glucosidase 52117.895 2    3.2.1.21 ? ? WP_041081105 
2 non-polymer syn GLYCEROL      92.094    2    ?        ? ? ?            
3 water       nat water         18.015    1078 ?        ? ? ?            
# 
_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       
;MFPQDFLFGVAMSGFQFEMGKENSKDENTDWYIWTHDLQNQANGVVSRDLVEEGADYWNSYARVHELCSRIGMNVIRIGI
EWSRIFPNPTHGIKDPSQIADMKVVEHYKQIIEDAKSRGLKVIVNLNHFTLPLWLHDPIRVSRFNDFSRSGWLDDRSVHE
FTKFATFCAKSFDDVDAFTTMNEPNVVAKLGYFGRLSGFPPSLLNIDLYEKALDNQILAHNKAYETMKQFTNKPVGIIYA
TSWCEGDDARNDAMELENWYFLDRVIDRIDFLGVNYYTRAIVKRTPSVLSSSSGRIKINWSFVPGFGGSCQRNSKSLDGR
PSTDNGWEIYPEGLGYVLRSCRDRYKKPLYVTENGVADDRDIYRPYSLLAHLKIVEDCLKENMDLRGYMHWSIIDNFEWP
MGYSMRFGLVRVDFKQKLFTPRPSYYLFGQIINSRTTEPFLNLLKAWE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MFPQDFLFGVAMSGFQFEMGKENSKDENTDWYIWTHDLQNQANGVVSRDLVEEGADYWNSYARVHELCSRIGMNVIRIGI
EWSRIFPNPTHGIKDPSQIADMKVVEHYKQIIEDAKSRGLKVIVNLNHFTLPLWLHDPIRVSRFNDFSRSGWLDDRSVHE
FTKFATFCAKSFDDVDAFTTMNEPNVVAKLGYFGRLSGFPPSLLNIDLYEKALDNQILAHNKAYETMKQFTNKPVGIIYA
TSWCEGDDARNDAMELENWYFLDRVIDRIDFLGVNYYTRAIVKRTPSVLSSSSGRIKINWSFVPGFGGSCQRNSKSLDGR
PSTDNGWEIYPEGLGYVLRSCRDRYKKPLYVTENGVADDRDIYRPYSLLAHLKIVEDCLKENMDLRGYMHWSIIDNFEWP
MGYSMRFGLVRVDFKQKLFTPRPSYYLFGQIINSRTTEPFLNLLKAWE
;
_entity_poly.pdbx_strand_id                 A,B 
_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   PHE n 
1 3   PRO n 
1 4   GLN n 
1 5   ASP n 
1 6   PHE n 
1 7   LEU n 
1 8   PHE n 
1 9   GLY n 
1 10  VAL n 
1 11  ALA n 
1 12  MET n 
1 13  SER n 
1 14  GLY n 
1 15  PHE n 
1 16  GLN n 
1 17  PHE n 
1 18  GLU n 
1 19  MET n 
1 20  GLY n 
1 21  LYS n 
1 22  GLU n 
1 23  ASN n 
1 24  SER n 
1 25  LYS n 
1 26  ASP n 
1 27  GLU n 
1 28  ASN n 
1 29  THR n 
1 30  ASP n 
1 31  TRP n 
1 32  TYR n 
1 33  ILE n 
1 34  TRP n 
1 35  THR n 
1 36  HIS n 
1 37  ASP n 
1 38  LEU n 
1 39  GLN n 
1 40  ASN n 
1 41  GLN n 
1 42  ALA n 
1 43  ASN n 
1 44  GLY n 
1 45  VAL n 
1 46  VAL n 
1 47  SER n 
1 48  ARG n 
1 49  ASP n 
1 50  LEU n 
1 51  VAL n 
1 52  GLU n 
1 53  GLU n 
1 54  GLY n 
1 55  ALA n 
1 56  ASP n 
1 57  TYR n 
1 58  TRP n 
1 59  ASN n 
1 60  SER n 
1 61  TYR n 
1 62  ALA n 
1 63  ARG n 
1 64  VAL n 
1 65  HIS n 
1 66  GLU n 
1 67  LEU n 
1 68  CYS n 
1 69  SER n 
1 70  ARG n 
1 71  ILE n 
1 72  GLY n 
1 73  MET n 
1 74  ASN n 
1 75  VAL n 
1 76  ILE n 
1 77  ARG n 
1 78  ILE n 
1 79  GLY n 
1 80  ILE n 
1 81  GLU n 
1 82  TRP n 
1 83  SER n 
1 84  ARG n 
1 85  ILE n 
1 86  PHE n 
1 87  PRO n 
1 88  ASN n 
1 89  PRO n 
1 90  THR n 
1 91  HIS n 
1 92  GLY n 
1 93  ILE n 
1 94  LYS n 
1 95  ASP n 
1 96  PRO n 
1 97  SER n 
1 98  GLN n 
1 99  ILE n 
1 100 ALA n 
1 101 ASP n 
1 102 MET n 
1 103 LYS n 
1 104 VAL n 
1 105 VAL n 
1 106 GLU n 
1 107 HIS n 
1 108 TYR n 
1 109 LYS n 
1 110 GLN n 
1 111 ILE n 
1 112 ILE n 
1 113 GLU n 
1 114 ASP n 
1 115 ALA n 
1 116 LYS n 
1 117 SER n 
1 118 ARG n 
1 119 GLY n 
1 120 LEU n 
1 121 LYS n 
1 122 VAL n 
1 123 ILE n 
1 124 VAL n 
1 125 ASN n 
1 126 LEU n 
1 127 ASN n 
1 128 HIS n 
1 129 PHE n 
1 130 THR n 
1 131 LEU n 
1 132 PRO n 
1 133 LEU n 
1 134 TRP n 
1 135 LEU n 
1 136 HIS n 
1 137 ASP n 
1 138 PRO n 
1 139 ILE n 
1 140 ARG n 
1 141 VAL n 
1 142 SER n 
1 143 ARG n 
1 144 PHE n 
1 145 ASN n 
1 146 ASP n 
1 147 PHE n 
1 148 SER n 
1 149 ARG n 
1 150 SER n 
1 151 GLY n 
1 152 TRP n 
1 153 LEU n 
1 154 ASP n 
1 155 ASP n 
1 156 ARG n 
1 157 SER n 
1 158 VAL n 
1 159 HIS n 
1 160 GLU n 
1 161 PHE n 
1 162 THR n 
1 163 LYS n 
1 164 PHE n 
1 165 ALA n 
1 166 THR n 
1 167 PHE n 
1 168 CYS n 
1 169 ALA n 
1 170 LYS n 
1 171 SER n 
1 172 PHE n 
1 173 ASP n 
1 174 ASP n 
1 175 VAL n 
1 176 ASP n 
1 177 ALA n 
1 178 PHE n 
1 179 THR n 
1 180 THR n 
1 181 MET n 
1 182 ASN n 
1 183 GLU n 
1 184 PRO n 
1 185 ASN n 
1 186 VAL n 
1 187 VAL n 
1 188 ALA n 
1 189 LYS n 
1 190 LEU n 
1 191 GLY n 
1 192 TYR n 
1 193 PHE n 
1 194 GLY n 
1 195 ARG n 
1 196 LEU n 
1 197 SER n 
1 198 GLY n 
1 199 PHE n 
1 200 PRO n 
1 201 PRO n 
1 202 SER n 
1 203 LEU n 
1 204 LEU n 
1 205 ASN n 
1 206 ILE n 
1 207 ASP n 
1 208 LEU n 
1 209 TYR n 
1 210 GLU n 
1 211 LYS n 
1 212 ALA n 
1 213 LEU n 
1 214 ASP n 
1 215 ASN n 
1 216 GLN n 
1 217 ILE n 
1 218 LEU n 
1 219 ALA n 
1 220 HIS n 
1 221 ASN n 
1 222 LYS n 
1 223 ALA n 
1 224 TYR n 
1 225 GLU n 
1 226 THR n 
1 227 MET n 
1 228 LYS n 
1 229 GLN n 
1 230 PHE n 
1 231 THR n 
1 232 ASN n 
1 233 LYS n 
1 234 PRO n 
1 235 VAL n 
1 236 GLY n 
1 237 ILE n 
1 238 ILE n 
1 239 TYR n 
1 240 ALA n 
1 241 THR n 
1 242 SER n 
1 243 TRP n 
1 244 CYS n 
1 245 GLU n 
1 246 GLY n 
1 247 ASP n 
1 248 ASP n 
1 249 ALA n 
1 250 ARG n 
1 251 ASN n 
1 252 ASP n 
1 253 ALA n 
1 254 MET n 
1 255 GLU n 
1 256 LEU n 
1 257 GLU n 
1 258 ASN n 
1 259 TRP n 
1 260 TYR n 
1 261 PHE n 
1 262 LEU n 
1 263 ASP n 
1 264 ARG n 
1 265 VAL n 
1 266 ILE n 
1 267 ASP n 
1 268 ARG n 
1 269 ILE n 
1 270 ASP n 
1 271 PHE n 
1 272 LEU n 
1 273 GLY n 
1 274 VAL n 
1 275 ASN n 
1 276 TYR n 
1 277 TYR n 
1 278 THR n 
1 279 ARG n 
1 280 ALA n 
1 281 ILE n 
1 282 VAL n 
1 283 LYS n 
1 284 ARG n 
1 285 THR n 
1 286 PRO n 
1 287 SER n 
1 288 VAL n 
1 289 LEU n 
1 290 SER n 
1 291 SER n 
1 292 SER n 
1 293 SER n 
1 294 GLY n 
1 295 ARG n 
1 296 ILE n 
1 297 LYS n 
1 298 ILE n 
1 299 ASN n 
1 300 TRP n 
1 301 SER n 
1 302 PHE n 
1 303 VAL n 
1 304 PRO n 
1 305 GLY n 
1 306 PHE n 
1 307 GLY n 
1 308 GLY n 
1 309 SER n 
1 310 CYS n 
1 311 GLN n 
1 312 ARG n 
1 313 ASN n 
1 314 SER n 
1 315 LYS n 
1 316 SER n 
1 317 LEU n 
1 318 ASP n 
1 319 GLY n 
1 320 ARG n 
1 321 PRO n 
1 322 SER n 
1 323 THR n 
1 324 ASP n 
1 325 ASN n 
1 326 GLY n 
1 327 TRP n 
1 328 GLU n 
1 329 ILE n 
1 330 TYR n 
1 331 PRO n 
1 332 GLU n 
1 333 GLY n 
1 334 LEU n 
1 335 GLY n 
1 336 TYR n 
1 337 VAL n 
1 338 LEU n 
1 339 ARG n 
1 340 SER n 
1 341 CYS n 
1 342 ARG n 
1 343 ASP n 
1 344 ARG n 
1 345 TYR n 
1 346 LYS n 
1 347 LYS n 
1 348 PRO n 
1 349 LEU n 
1 350 TYR n 
1 351 VAL n 
1 352 THR n 
1 353 GLU n 
1 354 ASN n 
1 355 GLY n 
1 356 VAL n 
1 357 ALA n 
1 358 ASP n 
1 359 ASP n 
1 360 ARG n 
1 361 ASP n 
1 362 ILE n 
1 363 TYR n 
1 364 ARG n 
1 365 PRO n 
1 366 TYR n 
1 367 SER n 
1 368 LEU n 
1 369 LEU n 
1 370 ALA n 
1 371 HIS n 
1 372 LEU n 
1 373 LYS n 
1 374 ILE n 
1 375 VAL n 
1 376 GLU n 
1 377 ASP n 
1 378 CYS n 
1 379 LEU n 
1 380 LYS n 
1 381 GLU n 
1 382 ASN n 
1 383 MET n 
1 384 ASP n 
1 385 LEU n 
1 386 ARG n 
1 387 GLY n 
1 388 TYR n 
1 389 MET n 
1 390 HIS n 
1 391 TRP n 
1 392 SER n 
1 393 ILE n 
1 394 ILE n 
1 395 ASP n 
1 396 ASN n 
1 397 PHE n 
1 398 GLU n 
1 399 TRP n 
1 400 PRO n 
1 401 MET n 
1 402 GLY n 
1 403 TYR n 
1 404 SER n 
1 405 MET n 
1 406 ARG n 
1 407 PHE n 
1 408 GLY n 
1 409 LEU n 
1 410 VAL n 
1 411 ARG n 
1 412 VAL n 
1 413 ASP n 
1 414 PHE n 
1 415 LYS n 
1 416 GLN n 
1 417 LYS n 
1 418 LEU n 
1 419 PHE n 
1 420 THR n 
1 421 PRO n 
1 422 ARG n 
1 423 PRO n 
1 424 SER n 
1 425 TYR n 
1 426 TYR n 
1 427 LEU n 
1 428 PHE n 
1 429 GLY n 
1 430 GLN n 
1 431 ILE n 
1 432 ILE n 
1 433 ASN n 
1 434 SER n 
1 435 ARG n 
1 436 THR n 
1 437 THR n 
1 438 GLU n 
1 439 PRO n 
1 440 PHE n 
1 441 LEU n 
1 442 ASN n 
1 443 LEU n 
1 444 LEU n 
1 445 LYS n 
1 446 ALA n 
1 447 TRP n 
1 448 GLU 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                   448 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Thermotoga profunda' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1508420 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
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 
LYS 'L-peptide linking' y LYSINE          ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ?                               'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ?                               'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ?                               'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ?                               'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ?                               'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ?                               'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ?                               'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   PHE 2   2   2   PHE PHE A . n 
A 1 3   PRO 3   3   3   PRO PRO A . n 
A 1 4   GLN 4   4   4   GLN GLN A . n 
A 1 5   ASP 5   5   5   ASP ASP A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   LEU 7   7   7   LEU LEU A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   GLY 9   9   9   GLY GLY A . n 
A 1 10  VAL 10  10  10  VAL VAL A . n 
A 1 11  ALA 11  11  11  ALA ALA A . n 
A 1 12  MET 12  12  12  MET MET A . n 
A 1 13  SER 13  13  13  SER SER A . n 
A 1 14  GLY 14  14  14  GLY GLY A . n 
A 1 15  PHE 15  15  15  PHE PHE A . n 
A 1 16  GLN 16  16  16  GLN GLN A . n 
A 1 17  PHE 17  17  17  PHE PHE A . n 
A 1 18  GLU 18  18  18  GLU GLU A . n 
A 1 19  MET 19  19  19  MET MET A . n 
A 1 20  GLY 20  20  20  GLY GLY A . n 
A 1 21  LYS 21  21  21  LYS LYS A . n 
A 1 22  GLU 22  22  22  GLU GLU A . n 
A 1 23  ASN 23  23  23  ASN ASN A . n 
A 1 24  SER 24  24  24  SER SER A . n 
A 1 25  LYS 25  25  25  LYS LYS A . n 
A 1 26  ASP 26  26  26  ASP ASP A . n 
A 1 27  GLU 27  27  27  GLU GLU A . n 
A 1 28  ASN 28  28  28  ASN ASN A . n 
A 1 29  THR 29  29  29  THR THR A . n 
A 1 30  ASP 30  30  30  ASP ASP A . n 
A 1 31  TRP 31  31  31  TRP TRP A . n 
A 1 32  TYR 32  32  32  TYR TYR A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  TRP 34  34  34  TRP TRP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  ASP 37  37  37  ASP ASP A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  GLN 39  39  39  GLN GLN A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  GLN 41  41  41  GLN GLN A . n 
A 1 42  ALA 42  42  42  ALA ALA A . n 
A 1 43  ASN 43  43  43  ASN ASN A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  VAL 45  45  45  VAL VAL A . n 
A 1 46  VAL 46  46  46  VAL VAL A . n 
A 1 47  SER 47  47  47  SER SER A . n 
A 1 48  ARG 48  48  48  ARG ARG A . n 
A 1 49  ASP 49  49  49  ASP ASP A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  VAL 51  51  51  VAL VAL A . n 
A 1 52  GLU 52  52  52  GLU GLU A . n 
A 1 53  GLU 53  53  53  GLU GLU A . n 
A 1 54  GLY 54  54  54  GLY GLY A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  TYR 57  57  57  TYR TYR A . n 
A 1 58  TRP 58  58  58  TRP TRP A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  SER 60  60  60  SER SER A . n 
A 1 61  TYR 61  61  61  TYR TYR A . n 
A 1 62  ALA 62  62  62  ALA ALA A . n 
A 1 63  ARG 63  63  63  ARG ARG A . n 
A 1 64  VAL 64  64  64  VAL VAL A . n 
A 1 65  HIS 65  65  65  HIS HIS A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  CYS 68  68  68  CYS CYS A . n 
A 1 69  SER 69  69  69  SER SER A . n 
A 1 70  ARG 70  70  70  ARG ARG A . n 
A 1 71  ILE 71  71  71  ILE ILE A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  MET 73  73  73  MET MET A . n 
A 1 74  ASN 74  74  74  ASN ASN A . n 
A 1 75  VAL 75  75  75  VAL VAL A . n 
A 1 76  ILE 76  76  76  ILE ILE A . n 
A 1 77  ARG 77  77  77  ARG ARG A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  ILE 80  80  80  ILE ILE A . n 
A 1 81  GLU 81  81  81  GLU GLU A . n 
A 1 82  TRP 82  82  82  TRP TRP A . n 
A 1 83  SER 83  83  83  SER SER A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  ILE 85  85  85  ILE ILE A . n 
A 1 86  PHE 86  86  86  PHE PHE A . n 
A 1 87  PRO 87  87  87  PRO PRO A . n 
A 1 88  ASN 88  88  88  ASN ASN A . n 
A 1 89  PRO 89  89  89  PRO PRO A . n 
A 1 90  THR 90  90  90  THR THR A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  GLY 92  92  92  GLY GLY A . n 
A 1 93  ILE 93  93  93  ILE ILE A . n 
A 1 94  LYS 94  94  94  LYS LYS A . n 
A 1 95  ASP 95  95  95  ASP ASP A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  SER 97  97  97  SER SER A . n 
A 1 98  GLN 98  98  98  GLN GLN A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 ALA 100 100 100 ALA ALA A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 MET 102 102 102 MET MET A . n 
A 1 103 LYS 103 103 103 LYS LYS A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 VAL 105 105 105 VAL VAL A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 TYR 108 108 108 TYR TYR A . n 
A 1 109 LYS 109 109 109 LYS LYS A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 ILE 111 111 111 ILE ILE A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 GLU 113 113 113 GLU GLU A . n 
A 1 114 ASP 114 114 114 ASP ASP A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 LYS 116 116 116 LYS LYS A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 ARG 118 118 118 ARG ARG A . n 
A 1 119 GLY 119 119 119 GLY GLY A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 LYS 121 121 121 LYS LYS A . n 
A 1 122 VAL 122 122 122 VAL VAL A . n 
A 1 123 ILE 123 123 123 ILE ILE A . n 
A 1 124 VAL 124 124 124 VAL VAL A . n 
A 1 125 ASN 125 125 125 ASN ASN A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 ASN 127 127 127 ASN ASN A . n 
A 1 128 HIS 128 128 128 HIS HIS A . n 
A 1 129 PHE 129 129 129 PHE PHE A . n 
A 1 130 THR 130 130 130 THR THR A . n 
A 1 131 LEU 131 131 131 LEU LEU A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 TRP 134 134 134 TRP TRP A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 HIS 136 136 136 HIS HIS A . n 
A 1 137 ASP 137 137 137 ASP ASP A . n 
A 1 138 PRO 138 138 138 PRO PRO A . n 
A 1 139 ILE 139 139 139 ILE ILE A . n 
A 1 140 ARG 140 140 140 ARG ARG A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 PHE 144 144 144 PHE PHE A . n 
A 1 145 ASN 145 145 145 ASN ASN A . n 
A 1 146 ASP 146 146 146 ASP ASP A . n 
A 1 147 PHE 147 147 147 PHE PHE A . n 
A 1 148 SER 148 148 148 SER SER A . n 
A 1 149 ARG 149 149 149 ARG ARG A . n 
A 1 150 SER 150 150 150 SER SER A . n 
A 1 151 GLY 151 151 151 GLY GLY A . n 
A 1 152 TRP 152 152 152 TRP TRP A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ASP 154 154 154 ASP ASP A . n 
A 1 155 ASP 155 155 155 ASP ASP A . n 
A 1 156 ARG 156 156 156 ARG ARG A . n 
A 1 157 SER 157 157 157 SER SER A . n 
A 1 158 VAL 158 158 158 VAL VAL A . n 
A 1 159 HIS 159 159 159 HIS HIS A . n 
A 1 160 GLU 160 160 160 GLU GLU A . n 
A 1 161 PHE 161 161 161 PHE PHE A . n 
A 1 162 THR 162 162 162 THR THR A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 PHE 164 164 164 PHE PHE A . n 
A 1 165 ALA 165 165 165 ALA ALA A . n 
A 1 166 THR 166 166 166 THR THR A . n 
A 1 167 PHE 167 167 167 PHE PHE A . n 
A 1 168 CYS 168 168 168 CYS CYS A . n 
A 1 169 ALA 169 169 169 ALA ALA A . n 
A 1 170 LYS 170 170 170 LYS LYS A . n 
A 1 171 SER 171 171 171 SER SER A . n 
A 1 172 PHE 172 172 172 PHE PHE A . n 
A 1 173 ASP 173 173 173 ASP ASP A . n 
A 1 174 ASP 174 174 174 ASP ASP A . n 
A 1 175 VAL 175 175 175 VAL VAL A . n 
A 1 176 ASP 176 176 176 ASP ASP A . n 
A 1 177 ALA 177 177 177 ALA ALA A . n 
A 1 178 PHE 178 178 178 PHE PHE A . n 
A 1 179 THR 179 179 179 THR THR A . n 
A 1 180 THR 180 180 180 THR THR A . n 
A 1 181 MET 181 181 181 MET MET A . n 
A 1 182 ASN 182 182 182 ASN ASN A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 ASN 185 185 185 ASN ASN A . n 
A 1 186 VAL 186 186 186 VAL VAL A . n 
A 1 187 VAL 187 187 187 VAL VAL A . n 
A 1 188 ALA 188 188 188 ALA ALA A . n 
A 1 189 LYS 189 189 189 LYS LYS A . n 
A 1 190 LEU 190 190 190 LEU LEU A . n 
A 1 191 GLY 191 191 191 GLY GLY A . n 
A 1 192 TYR 192 192 192 TYR TYR A . n 
A 1 193 PHE 193 193 193 PHE PHE A . n 
A 1 194 GLY 194 194 194 GLY GLY A . n 
A 1 195 ARG 195 195 195 ARG ARG A . n 
A 1 196 LEU 196 196 196 LEU LEU A . n 
A 1 197 SER 197 197 197 SER SER A . n 
A 1 198 GLY 198 198 198 GLY GLY A . n 
A 1 199 PHE 199 199 199 PHE PHE A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 PRO 201 201 201 PRO PRO A . n 
A 1 202 SER 202 202 202 SER SER A . n 
A 1 203 LEU 203 203 203 LEU LEU A . n 
A 1 204 LEU 204 204 204 LEU LEU A . n 
A 1 205 ASN 205 205 205 ASN ASN A . n 
A 1 206 ILE 206 206 206 ILE ILE A . n 
A 1 207 ASP 207 207 207 ASP ASP A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 TYR 209 209 209 TYR TYR A . n 
A 1 210 GLU 210 210 210 GLU GLU A . n 
A 1 211 LYS 211 211 211 LYS LYS A . n 
A 1 212 ALA 212 212 212 ALA ALA A . n 
A 1 213 LEU 213 213 213 LEU LEU A . n 
A 1 214 ASP 214 214 214 ASP ASP A . n 
A 1 215 ASN 215 215 215 ASN ASN A . n 
A 1 216 GLN 216 216 216 GLN GLN A . n 
A 1 217 ILE 217 217 217 ILE ILE A . n 
A 1 218 LEU 218 218 218 LEU LEU A . n 
A 1 219 ALA 219 219 219 ALA ALA A . n 
A 1 220 HIS 220 220 220 HIS HIS A . n 
A 1 221 ASN 221 221 221 ASN ASN A . n 
A 1 222 LYS 222 222 222 LYS LYS A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 TYR 224 224 224 TYR TYR A . n 
A 1 225 GLU 225 225 225 GLU GLU A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 MET 227 227 227 MET MET A . n 
A 1 228 LYS 228 228 228 LYS LYS A . n 
A 1 229 GLN 229 229 229 GLN GLN A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 THR 231 231 231 THR THR A . n 
A 1 232 ASN 232 232 232 ASN ASN A . n 
A 1 233 LYS 233 233 233 LYS LYS A . n 
A 1 234 PRO 234 234 234 PRO PRO A . n 
A 1 235 VAL 235 235 235 VAL VAL A . n 
A 1 236 GLY 236 236 236 GLY GLY A . n 
A 1 237 ILE 237 237 237 ILE ILE A . n 
A 1 238 ILE 238 238 238 ILE ILE A . n 
A 1 239 TYR 239 239 239 TYR TYR A . n 
A 1 240 ALA 240 240 240 ALA ALA A . n 
A 1 241 THR 241 241 241 THR THR A . n 
A 1 242 SER 242 242 242 SER SER A . n 
A 1 243 TRP 243 243 243 TRP TRP A . n 
A 1 244 CYS 244 244 244 CYS CYS A . n 
A 1 245 GLU 245 245 245 GLU GLU A . n 
A 1 246 GLY 246 246 246 GLY GLY A . n 
A 1 247 ASP 247 247 247 ASP ASP A . n 
A 1 248 ASP 248 248 248 ASP ASP A . n 
A 1 249 ALA 249 249 249 ALA ALA A . n 
A 1 250 ARG 250 250 250 ARG ARG A . n 
A 1 251 ASN 251 251 251 ASN ASN A . n 
A 1 252 ASP 252 252 252 ASP ASP A . n 
A 1 253 ALA 253 253 253 ALA ALA A . n 
A 1 254 MET 254 254 254 MET MET A . n 
A 1 255 GLU 255 255 255 GLU GLU A . n 
A 1 256 LEU 256 256 256 LEU LEU A . n 
A 1 257 GLU 257 257 257 GLU GLU A . n 
A 1 258 ASN 258 258 258 ASN ASN A . n 
A 1 259 TRP 259 259 259 TRP TRP A . n 
A 1 260 TYR 260 260 260 TYR TYR A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ASP 263 263 263 ASP ASP A . n 
A 1 264 ARG 264 264 264 ARG ARG A . n 
A 1 265 VAL 265 265 265 VAL VAL A . n 
A 1 266 ILE 266 266 266 ILE ILE A . n 
A 1 267 ASP 267 267 267 ASP ASP A . n 
A 1 268 ARG 268 268 268 ARG ARG A . n 
A 1 269 ILE 269 269 269 ILE ILE A . n 
A 1 270 ASP 270 270 270 ASP ASP A . n 
A 1 271 PHE 271 271 271 PHE PHE A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 GLY 273 273 273 GLY GLY A . n 
A 1 274 VAL 274 274 274 VAL VAL A . n 
A 1 275 ASN 275 275 275 ASN ASN A . n 
A 1 276 TYR 276 276 276 TYR TYR A . n 
A 1 277 TYR 277 277 277 TYR TYR A . n 
A 1 278 THR 278 278 278 THR THR A . n 
A 1 279 ARG 279 279 279 ARG ARG A . n 
A 1 280 ALA 280 280 280 ALA ALA A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 VAL 282 282 282 VAL VAL A . n 
A 1 283 LYS 283 283 283 LYS LYS A . n 
A 1 284 ARG 284 284 284 ARG ARG A . n 
A 1 285 THR 285 285 285 THR THR A . n 
A 1 286 PRO 286 286 286 PRO PRO A . n 
A 1 287 SER 287 287 287 SER SER A . n 
A 1 288 VAL 288 288 288 VAL VAL A . n 
A 1 289 LEU 289 289 289 LEU LEU A . n 
A 1 290 SER 290 290 290 SER SER A . n 
A 1 291 SER 291 291 291 SER SER A . n 
A 1 292 SER 292 292 292 SER SER A . n 
A 1 293 SER 293 293 293 SER SER A . n 
A 1 294 GLY 294 294 294 GLY GLY A . n 
A 1 295 ARG 295 295 295 ARG ARG A . n 
A 1 296 ILE 296 296 296 ILE ILE A . n 
A 1 297 LYS 297 297 297 LYS LYS A . n 
A 1 298 ILE 298 298 298 ILE ILE A . n 
A 1 299 ASN 299 299 299 ASN ASN A . n 
A 1 300 TRP 300 300 300 TRP TRP A . n 
A 1 301 SER 301 301 301 SER SER A . n 
A 1 302 PHE 302 302 302 PHE PHE A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 PRO 304 304 304 PRO PRO A . n 
A 1 305 GLY 305 305 305 GLY GLY A . n 
A 1 306 PHE 306 306 306 PHE PHE A . n 
A 1 307 GLY 307 307 307 GLY GLY A . n 
A 1 308 GLY 308 308 308 GLY GLY A . n 
A 1 309 SER 309 309 309 SER SER A . n 
A 1 310 CYS 310 310 310 CYS CYS A . n 
A 1 311 GLN 311 311 311 GLN GLN A . n 
A 1 312 ARG 312 312 312 ARG ARG A . n 
A 1 313 ASN 313 313 313 ASN ASN A . n 
A 1 314 SER 314 314 314 SER SER A . n 
A 1 315 LYS 315 315 315 LYS LYS A . n 
A 1 316 SER 316 316 316 SER SER A . n 
A 1 317 LEU 317 317 317 LEU LEU A . n 
A 1 318 ASP 318 318 318 ASP ASP A . n 
A 1 319 GLY 319 319 319 GLY GLY A . n 
A 1 320 ARG 320 320 320 ARG ARG A . n 
A 1 321 PRO 321 321 321 PRO PRO A . n 
A 1 322 SER 322 322 322 SER SER A . n 
A 1 323 THR 323 323 323 THR THR A . n 
A 1 324 ASP 324 324 324 ASP ASP A . n 
A 1 325 ASN 325 325 325 ASN ASN A . n 
A 1 326 GLY 326 326 326 GLY GLY A . n 
A 1 327 TRP 327 327 327 TRP TRP A . n 
A 1 328 GLU 328 328 328 GLU GLU A . n 
A 1 329 ILE 329 329 329 ILE ILE A . n 
A 1 330 TYR 330 330 330 TYR TYR A . n 
A 1 331 PRO 331 331 331 PRO PRO A . n 
A 1 332 GLU 332 332 332 GLU GLU A . n 
A 1 333 GLY 333 333 333 GLY GLY A . n 
A 1 334 LEU 334 334 334 LEU LEU A . n 
A 1 335 GLY 335 335 335 GLY GLY A . n 
A 1 336 TYR 336 336 336 TYR TYR A . n 
A 1 337 VAL 337 337 337 VAL VAL A . n 
A 1 338 LEU 338 338 338 LEU LEU A . n 
A 1 339 ARG 339 339 339 ARG ARG A . n 
A 1 340 SER 340 340 340 SER SER A . n 
A 1 341 CYS 341 341 341 CYS CYS A . n 
A 1 342 ARG 342 342 342 ARG ARG A . n 
A 1 343 ASP 343 343 343 ASP ASP A . n 
A 1 344 ARG 344 344 344 ARG ARG A . n 
A 1 345 TYR 345 345 345 TYR TYR A . n 
A 1 346 LYS 346 346 346 LYS LYS A . n 
A 1 347 LYS 347 347 347 LYS LYS A . n 
A 1 348 PRO 348 348 348 PRO PRO A . n 
A 1 349 LEU 349 349 349 LEU LEU A . n 
A 1 350 TYR 350 350 350 TYR TYR A . n 
A 1 351 VAL 351 351 351 VAL VAL A . n 
A 1 352 THR 352 352 352 THR THR A . n 
A 1 353 GLU 353 353 353 GLU GLU A . n 
A 1 354 ASN 354 354 354 ASN ASN A . n 
A 1 355 GLY 355 355 355 GLY GLY A . n 
A 1 356 VAL 356 356 356 VAL VAL A . n 
A 1 357 ALA 357 357 357 ALA ALA A . n 
A 1 358 ASP 358 358 358 ASP ASP A . n 
A 1 359 ASP 359 359 359 ASP ASP A . n 
A 1 360 ARG 360 360 360 ARG ARG A . n 
A 1 361 ASP 361 361 361 ASP ASP A . n 
A 1 362 ILE 362 362 362 ILE ILE A . n 
A 1 363 TYR 363 363 363 TYR TYR A . n 
A 1 364 ARG 364 364 364 ARG ARG A . n 
A 1 365 PRO 365 365 365 PRO PRO A . n 
A 1 366 TYR 366 366 366 TYR TYR A . n 
A 1 367 SER 367 367 367 SER SER A . n 
A 1 368 LEU 368 368 368 LEU LEU A . n 
A 1 369 LEU 369 369 369 LEU LEU A . n 
A 1 370 ALA 370 370 370 ALA ALA A . n 
A 1 371 HIS 371 371 371 HIS HIS A . n 
A 1 372 LEU 372 372 372 LEU LEU A . n 
A 1 373 LYS 373 373 373 LYS LYS A . n 
A 1 374 ILE 374 374 374 ILE ILE A . n 
A 1 375 VAL 375 375 375 VAL VAL A . n 
A 1 376 GLU 376 376 376 GLU GLU A . n 
A 1 377 ASP 377 377 377 ASP ASP A . n 
A 1 378 CYS 378 378 378 CYS CYS A . n 
A 1 379 LEU 379 379 379 LEU LEU A . n 
A 1 380 LYS 380 380 380 LYS LYS A . n 
A 1 381 GLU 381 381 381 GLU GLU A . n 
A 1 382 ASN 382 382 382 ASN ASN A . n 
A 1 383 MET 383 383 383 MET MET A . n 
A 1 384 ASP 384 384 384 ASP ASP A . n 
A 1 385 LEU 385 385 385 LEU LEU A . n 
A 1 386 ARG 386 386 386 ARG ARG A . n 
A 1 387 GLY 387 387 387 GLY GLY A . n 
A 1 388 TYR 388 388 388 TYR TYR A . n 
A 1 389 MET 389 389 389 MET MET A . n 
A 1 390 HIS 390 390 390 HIS HIS A . n 
A 1 391 TRP 391 391 391 TRP TRP A . n 
A 1 392 SER 392 392 392 SER SER A . n 
A 1 393 ILE 393 393 393 ILE ILE A . n 
A 1 394 ILE 394 394 394 ILE ILE A . n 
A 1 395 ASP 395 395 395 ASP ASP A . n 
A 1 396 ASN 396 396 396 ASN ASN A . n 
A 1 397 PHE 397 397 397 PHE PHE A . n 
A 1 398 GLU 398 398 398 GLU GLU A . n 
A 1 399 TRP 399 399 399 TRP TRP A . n 
A 1 400 PRO 400 400 400 PRO PRO A . n 
A 1 401 MET 401 401 401 MET MET A . n 
A 1 402 GLY 402 402 402 GLY GLY A . n 
A 1 403 TYR 403 403 403 TYR TYR A . n 
A 1 404 SER 404 404 404 SER SER A . n 
A 1 405 MET 405 405 405 MET MET A . n 
A 1 406 ARG 406 406 406 ARG ARG A . n 
A 1 407 PHE 407 407 407 PHE PHE A . n 
A 1 408 GLY 408 408 408 GLY GLY A . n 
A 1 409 LEU 409 409 409 LEU LEU A . n 
A 1 410 VAL 410 410 410 VAL VAL A . n 
A 1 411 ARG 411 411 411 ARG ARG A . n 
A 1 412 VAL 412 412 412 VAL VAL A . n 
A 1 413 ASP 413 413 413 ASP ASP A . n 
A 1 414 PHE 414 414 414 PHE PHE A . n 
A 1 415 LYS 415 415 415 LYS LYS A . n 
A 1 416 GLN 416 416 416 GLN GLN A . n 
A 1 417 LYS 417 417 417 LYS LYS A . n 
A 1 418 LEU 418 418 418 LEU LEU A . n 
A 1 419 PHE 419 419 419 PHE PHE A . n 
A 1 420 THR 420 420 420 THR THR A . n 
A 1 421 PRO 421 421 421 PRO PRO A . n 
A 1 422 ARG 422 422 422 ARG ARG A . n 
A 1 423 PRO 423 423 423 PRO PRO A . n 
A 1 424 SER 424 424 424 SER SER A . n 
A 1 425 TYR 425 425 425 TYR TYR A . n 
A 1 426 TYR 426 426 426 TYR TYR A . n 
A 1 427 LEU 427 427 427 LEU LEU A . n 
A 1 428 PHE 428 428 428 PHE PHE A . n 
A 1 429 GLY 429 429 429 GLY GLY A . n 
A 1 430 GLN 430 430 430 GLN GLN A . n 
A 1 431 ILE 431 431 431 ILE ILE A . n 
A 1 432 ILE 432 432 432 ILE ILE A . n 
A 1 433 ASN 433 433 433 ASN ASN A . n 
A 1 434 SER 434 434 434 SER SER A . n 
A 1 435 ARG 435 435 435 ARG ARG A . n 
A 1 436 THR 436 436 436 THR THR A . n 
A 1 437 THR 437 437 437 THR THR A . n 
A 1 438 GLU 438 438 438 GLU GLU A . n 
A 1 439 PRO 439 439 439 PRO PRO A . n 
A 1 440 PHE 440 440 440 PHE PHE A . n 
A 1 441 LEU 441 441 441 LEU LEU A . n 
A 1 442 ASN 442 442 442 ASN ASN A . n 
A 1 443 LEU 443 443 443 LEU LEU A . n 
A 1 444 LEU 444 444 444 LEU LEU A . n 
A 1 445 LYS 445 445 445 LYS LYS A . n 
A 1 446 ALA 446 446 446 ALA ALA A . n 
A 1 447 TRP 447 447 447 TRP TRP A . n 
A 1 448 GLU 448 448 448 GLU GLU A . n 
B 1 1   MET 1   1   1   MET MET B . n 
B 1 2   PHE 2   2   2   PHE PHE B . n 
B 1 3   PRO 3   3   3   PRO PRO B . n 
B 1 4   GLN 4   4   4   GLN GLN B . n 
B 1 5   ASP 5   5   5   ASP ASP B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   LEU 7   7   7   LEU LEU B . n 
B 1 8   PHE 8   8   8   PHE PHE B . n 
B 1 9   GLY 9   9   9   GLY GLY B . n 
B 1 10  VAL 10  10  10  VAL VAL B . n 
B 1 11  ALA 11  11  11  ALA ALA B . n 
B 1 12  MET 12  12  12  MET MET B . n 
B 1 13  SER 13  13  13  SER SER B . n 
B 1 14  GLY 14  14  14  GLY GLY B . n 
B 1 15  PHE 15  15  15  PHE PHE B . n 
B 1 16  GLN 16  16  16  GLN GLN B . n 
B 1 17  PHE 17  17  17  PHE PHE B . n 
B 1 18  GLU 18  18  18  GLU GLU B . n 
B 1 19  MET 19  19  19  MET MET B . n 
B 1 20  GLY 20  20  20  GLY GLY B . n 
B 1 21  LYS 21  21  21  LYS LYS B . n 
B 1 22  GLU 22  22  22  GLU GLU B . n 
B 1 23  ASN 23  23  23  ASN ASN B . n 
B 1 24  SER 24  24  24  SER SER B . n 
B 1 25  LYS 25  25  25  LYS LYS B . n 
B 1 26  ASP 26  26  26  ASP ASP B . n 
B 1 27  GLU 27  27  27  GLU GLU B . n 
B 1 28  ASN 28  28  28  ASN ASN B . n 
B 1 29  THR 29  29  29  THR THR B . n 
B 1 30  ASP 30  30  30  ASP ASP B . n 
B 1 31  TRP 31  31  31  TRP TRP B . n 
B 1 32  TYR 32  32  32  TYR TYR B . n 
B 1 33  ILE 33  33  33  ILE ILE B . n 
B 1 34  TRP 34  34  34  TRP TRP B . n 
B 1 35  THR 35  35  35  THR THR B . n 
B 1 36  HIS 36  36  36  HIS HIS B . n 
B 1 37  ASP 37  37  37  ASP ASP B . n 
B 1 38  LEU 38  38  38  LEU LEU B . n 
B 1 39  GLN 39  39  39  GLN GLN B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  GLN 41  41  41  GLN GLN B . n 
B 1 42  ALA 42  42  42  ALA ALA B . n 
B 1 43  ASN 43  43  43  ASN ASN B . n 
B 1 44  GLY 44  44  44  GLY GLY B . n 
B 1 45  VAL 45  45  45  VAL VAL B . n 
B 1 46  VAL 46  46  46  VAL VAL B . n 
B 1 47  SER 47  47  47  SER SER B . n 
B 1 48  ARG 48  48  48  ARG ARG B . n 
B 1 49  ASP 49  49  49  ASP ASP B . n 
B 1 50  LEU 50  50  50  LEU LEU B . n 
B 1 51  VAL 51  51  51  VAL VAL B . n 
B 1 52  GLU 52  52  52  GLU GLU B . n 
B 1 53  GLU 53  53  53  GLU GLU B . n 
B 1 54  GLY 54  54  54  GLY GLY B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  ASP 56  56  56  ASP ASP B . n 
B 1 57  TYR 57  57  57  TYR TYR B . n 
B 1 58  TRP 58  58  58  TRP TRP B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  SER 60  60  60  SER SER B . n 
B 1 61  TYR 61  61  61  TYR TYR B . n 
B 1 62  ALA 62  62  62  ALA ALA B . n 
B 1 63  ARG 63  63  63  ARG ARG B . n 
B 1 64  VAL 64  64  64  VAL VAL B . n 
B 1 65  HIS 65  65  65  HIS HIS B . n 
B 1 66  GLU 66  66  66  GLU GLU B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  CYS 68  68  68  CYS CYS B . n 
B 1 69  SER 69  69  69  SER SER B . n 
B 1 70  ARG 70  70  70  ARG ARG B . n 
B 1 71  ILE 71  71  71  ILE ILE B . n 
B 1 72  GLY 72  72  72  GLY GLY B . n 
B 1 73  MET 73  73  73  MET MET B . n 
B 1 74  ASN 74  74  74  ASN ASN B . n 
B 1 75  VAL 75  75  75  VAL VAL B . n 
B 1 76  ILE 76  76  76  ILE ILE B . n 
B 1 77  ARG 77  77  77  ARG ARG B . n 
B 1 78  ILE 78  78  78  ILE ILE B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  ILE 80  80  80  ILE ILE B . n 
B 1 81  GLU 81  81  81  GLU GLU B . n 
B 1 82  TRP 82  82  82  TRP TRP B . n 
B 1 83  SER 83  83  83  SER SER B . n 
B 1 84  ARG 84  84  84  ARG ARG B . n 
B 1 85  ILE 85  85  85  ILE ILE B . n 
B 1 86  PHE 86  86  86  PHE PHE B . n 
B 1 87  PRO 87  87  87  PRO PRO B . n 
B 1 88  ASN 88  88  88  ASN ASN B . n 
B 1 89  PRO 89  89  89  PRO PRO B . n 
B 1 90  THR 90  90  90  THR THR B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  GLY 92  92  92  GLY GLY B . n 
B 1 93  ILE 93  93  93  ILE ILE B . n 
B 1 94  LYS 94  94  94  LYS LYS B . n 
B 1 95  ASP 95  95  95  ASP ASP B . n 
B 1 96  PRO 96  96  96  PRO PRO B . n 
B 1 97  SER 97  97  97  SER SER B . n 
B 1 98  GLN 98  98  98  GLN GLN B . n 
B 1 99  ILE 99  99  99  ILE ILE B . n 
B 1 100 ALA 100 100 100 ALA ALA B . n 
B 1 101 ASP 101 101 101 ASP ASP B . n 
B 1 102 MET 102 102 102 MET MET B . n 
B 1 103 LYS 103 103 103 LYS LYS B . n 
B 1 104 VAL 104 104 104 VAL VAL B . n 
B 1 105 VAL 105 105 105 VAL VAL B . n 
B 1 106 GLU 106 106 106 GLU GLU B . n 
B 1 107 HIS 107 107 107 HIS HIS B . n 
B 1 108 TYR 108 108 108 TYR TYR B . n 
B 1 109 LYS 109 109 109 LYS LYS B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 ILE 111 111 111 ILE ILE B . n 
B 1 112 ILE 112 112 112 ILE ILE B . n 
B 1 113 GLU 113 113 113 GLU GLU B . n 
B 1 114 ASP 114 114 114 ASP ASP B . n 
B 1 115 ALA 115 115 115 ALA ALA B . n 
B 1 116 LYS 116 116 116 LYS LYS B . n 
B 1 117 SER 117 117 117 SER SER B . n 
B 1 118 ARG 118 118 118 ARG ARG B . n 
B 1 119 GLY 119 119 119 GLY GLY B . n 
B 1 120 LEU 120 120 120 LEU LEU B . n 
B 1 121 LYS 121 121 121 LYS LYS B . n 
B 1 122 VAL 122 122 122 VAL VAL B . n 
B 1 123 ILE 123 123 123 ILE ILE B . n 
B 1 124 VAL 124 124 124 VAL VAL B . n 
B 1 125 ASN 125 125 125 ASN ASN B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 ASN 127 127 127 ASN ASN B . n 
B 1 128 HIS 128 128 128 HIS HIS B . n 
B 1 129 PHE 129 129 129 PHE PHE B . n 
B 1 130 THR 130 130 130 THR THR B . n 
B 1 131 LEU 131 131 131 LEU LEU B . n 
B 1 132 PRO 132 132 132 PRO PRO B . n 
B 1 133 LEU 133 133 133 LEU LEU B . n 
B 1 134 TRP 134 134 134 TRP TRP B . n 
B 1 135 LEU 135 135 135 LEU LEU B . n 
B 1 136 HIS 136 136 136 HIS HIS B . n 
B 1 137 ASP 137 137 137 ASP ASP B . n 
B 1 138 PRO 138 138 138 PRO PRO B . n 
B 1 139 ILE 139 139 139 ILE ILE B . n 
B 1 140 ARG 140 140 140 ARG ARG B . n 
B 1 141 VAL 141 141 141 VAL VAL B . n 
B 1 142 SER 142 142 142 SER SER B . n 
B 1 143 ARG 143 143 143 ARG ARG B . n 
B 1 144 PHE 144 144 144 PHE PHE B . n 
B 1 145 ASN 145 145 145 ASN ASN B . n 
B 1 146 ASP 146 146 146 ASP ASP B . n 
B 1 147 PHE 147 147 147 PHE PHE B . n 
B 1 148 SER 148 148 148 SER SER B . n 
B 1 149 ARG 149 149 149 ARG ARG B . n 
B 1 150 SER 150 150 150 SER SER B . n 
B 1 151 GLY 151 151 151 GLY GLY B . n 
B 1 152 TRP 152 152 152 TRP TRP B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ASP 154 154 154 ASP ASP B . n 
B 1 155 ASP 155 155 155 ASP ASP B . n 
B 1 156 ARG 156 156 156 ARG ARG B . n 
B 1 157 SER 157 157 157 SER SER B . n 
B 1 158 VAL 158 158 158 VAL VAL B . n 
B 1 159 HIS 159 159 159 HIS HIS B . n 
B 1 160 GLU 160 160 160 GLU GLU B . n 
B 1 161 PHE 161 161 161 PHE PHE B . n 
B 1 162 THR 162 162 162 THR THR B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 PHE 164 164 164 PHE PHE B . n 
B 1 165 ALA 165 165 165 ALA ALA B . n 
B 1 166 THR 166 166 166 THR THR B . n 
B 1 167 PHE 167 167 167 PHE PHE B . n 
B 1 168 CYS 168 168 168 CYS CYS B . n 
B 1 169 ALA 169 169 169 ALA ALA B . n 
B 1 170 LYS 170 170 170 LYS LYS B . n 
B 1 171 SER 171 171 171 SER SER B . n 
B 1 172 PHE 172 172 172 PHE PHE B . n 
B 1 173 ASP 173 173 173 ASP ASP B . n 
B 1 174 ASP 174 174 174 ASP ASP B . n 
B 1 175 VAL 175 175 175 VAL VAL B . n 
B 1 176 ASP 176 176 176 ASP ASP B . n 
B 1 177 ALA 177 177 177 ALA ALA B . n 
B 1 178 PHE 178 178 178 PHE PHE B . n 
B 1 179 THR 179 179 179 THR THR B . n 
B 1 180 THR 180 180 180 THR THR B . n 
B 1 181 MET 181 181 181 MET MET B . n 
B 1 182 ASN 182 182 182 ASN ASN B . n 
B 1 183 GLU 183 183 183 GLU GLU B . n 
B 1 184 PRO 184 184 184 PRO PRO B . n 
B 1 185 ASN 185 185 185 ASN ASN B . n 
B 1 186 VAL 186 186 186 VAL VAL B . n 
B 1 187 VAL 187 187 187 VAL VAL B . n 
B 1 188 ALA 188 188 188 ALA ALA B . n 
B 1 189 LYS 189 189 189 LYS LYS B . n 
B 1 190 LEU 190 190 190 LEU LEU B . n 
B 1 191 GLY 191 191 191 GLY GLY B . n 
B 1 192 TYR 192 192 192 TYR TYR B . n 
B 1 193 PHE 193 193 193 PHE PHE B . n 
B 1 194 GLY 194 194 194 GLY GLY B . n 
B 1 195 ARG 195 195 195 ARG ARG B . n 
B 1 196 LEU 196 196 196 LEU LEU B . n 
B 1 197 SER 197 197 197 SER SER B . n 
B 1 198 GLY 198 198 198 GLY GLY B . n 
B 1 199 PHE 199 199 199 PHE PHE B . n 
B 1 200 PRO 200 200 200 PRO PRO B . n 
B 1 201 PRO 201 201 201 PRO PRO B . n 
B 1 202 SER 202 202 202 SER SER B . n 
B 1 203 LEU 203 203 203 LEU LEU B . n 
B 1 204 LEU 204 204 204 LEU LEU B . n 
B 1 205 ASN 205 205 205 ASN ASN B . n 
B 1 206 ILE 206 206 206 ILE ILE B . n 
B 1 207 ASP 207 207 207 ASP ASP B . n 
B 1 208 LEU 208 208 208 LEU LEU B . n 
B 1 209 TYR 209 209 209 TYR TYR B . n 
B 1 210 GLU 210 210 210 GLU GLU B . n 
B 1 211 LYS 211 211 211 LYS LYS B . n 
B 1 212 ALA 212 212 212 ALA ALA B . n 
B 1 213 LEU 213 213 213 LEU LEU B . n 
B 1 214 ASP 214 214 214 ASP ASP B . n 
B 1 215 ASN 215 215 215 ASN ASN B . n 
B 1 216 GLN 216 216 216 GLN GLN B . n 
B 1 217 ILE 217 217 217 ILE ILE B . n 
B 1 218 LEU 218 218 218 LEU LEU B . n 
B 1 219 ALA 219 219 219 ALA ALA B . n 
B 1 220 HIS 220 220 220 HIS HIS B . n 
B 1 221 ASN 221 221 221 ASN ASN B . n 
B 1 222 LYS 222 222 222 LYS LYS B . n 
B 1 223 ALA 223 223 223 ALA ALA B . n 
B 1 224 TYR 224 224 224 TYR TYR B . n 
B 1 225 GLU 225 225 225 GLU GLU B . n 
B 1 226 THR 226 226 226 THR THR B . n 
B 1 227 MET 227 227 227 MET MET B . n 
B 1 228 LYS 228 228 228 LYS LYS B . n 
B 1 229 GLN 229 229 229 GLN GLN B . n 
B 1 230 PHE 230 230 230 PHE PHE B . n 
B 1 231 THR 231 231 231 THR THR B . n 
B 1 232 ASN 232 232 232 ASN ASN B . n 
B 1 233 LYS 233 233 233 LYS LYS B . n 
B 1 234 PRO 234 234 234 PRO PRO B . n 
B 1 235 VAL 235 235 235 VAL VAL B . n 
B 1 236 GLY 236 236 236 GLY GLY B . n 
B 1 237 ILE 237 237 237 ILE ILE B . n 
B 1 238 ILE 238 238 238 ILE ILE B . n 
B 1 239 TYR 239 239 239 TYR TYR B . n 
B 1 240 ALA 240 240 240 ALA ALA B . n 
B 1 241 THR 241 241 241 THR THR B . n 
B 1 242 SER 242 242 242 SER SER B . n 
B 1 243 TRP 243 243 243 TRP TRP B . n 
B 1 244 CYS 244 244 244 CYS CYS B . n 
B 1 245 GLU 245 245 245 GLU GLU B . n 
B 1 246 GLY 246 246 246 GLY GLY B . n 
B 1 247 ASP 247 247 247 ASP ASP B . n 
B 1 248 ASP 248 248 248 ASP ASP B . n 
B 1 249 ALA 249 249 249 ALA ALA B . n 
B 1 250 ARG 250 250 250 ARG ARG B . n 
B 1 251 ASN 251 251 251 ASN ASN B . n 
B 1 252 ASP 252 252 252 ASP ASP B . n 
B 1 253 ALA 253 253 253 ALA ALA B . n 
B 1 254 MET 254 254 254 MET MET B . n 
B 1 255 GLU 255 255 255 GLU GLU B . n 
B 1 256 LEU 256 256 256 LEU LEU B . n 
B 1 257 GLU 257 257 257 GLU GLU B . n 
B 1 258 ASN 258 258 258 ASN ASN B . n 
B 1 259 TRP 259 259 259 TRP TRP B . n 
B 1 260 TYR 260 260 260 TYR TYR B . n 
B 1 261 PHE 261 261 261 PHE PHE B . n 
B 1 262 LEU 262 262 262 LEU LEU B . n 
B 1 263 ASP 263 263 263 ASP ASP B . n 
B 1 264 ARG 264 264 264 ARG ARG B . n 
B 1 265 VAL 265 265 265 VAL VAL B . n 
B 1 266 ILE 266 266 266 ILE ILE B . n 
B 1 267 ASP 267 267 267 ASP ASP B . n 
B 1 268 ARG 268 268 268 ARG ARG B . n 
B 1 269 ILE 269 269 269 ILE ILE B . n 
B 1 270 ASP 270 270 270 ASP ASP B . n 
B 1 271 PHE 271 271 271 PHE PHE B . n 
B 1 272 LEU 272 272 272 LEU LEU B . n 
B 1 273 GLY 273 273 273 GLY GLY B . n 
B 1 274 VAL 274 274 274 VAL VAL B . n 
B 1 275 ASN 275 275 275 ASN ASN B . n 
B 1 276 TYR 276 276 276 TYR TYR B . n 
B 1 277 TYR 277 277 277 TYR TYR B . n 
B 1 278 THR 278 278 278 THR THR B . n 
B 1 279 ARG 279 279 279 ARG ARG B . n 
B 1 280 ALA 280 280 280 ALA ALA B . n 
B 1 281 ILE 281 281 281 ILE ILE B . n 
B 1 282 VAL 282 282 282 VAL VAL B . n 
B 1 283 LYS 283 283 283 LYS LYS B . n 
B 1 284 ARG 284 284 284 ARG ARG B . n 
B 1 285 THR 285 285 285 THR THR B . n 
B 1 286 PRO 286 286 286 PRO PRO B . n 
B 1 287 SER 287 287 287 SER SER B . n 
B 1 288 VAL 288 288 288 VAL VAL B . n 
B 1 289 LEU 289 289 289 LEU LEU B . n 
B 1 290 SER 290 290 290 SER SER B . n 
B 1 291 SER 291 291 291 SER SER B . n 
B 1 292 SER 292 292 292 SER SER B . n 
B 1 293 SER 293 293 293 SER SER B . n 
B 1 294 GLY 294 294 294 GLY GLY B . n 
B 1 295 ARG 295 295 295 ARG ARG B . n 
B 1 296 ILE 296 296 296 ILE ILE B . n 
B 1 297 LYS 297 297 297 LYS LYS B . n 
B 1 298 ILE 298 298 298 ILE ILE B . n 
B 1 299 ASN 299 299 299 ASN ASN B . n 
B 1 300 TRP 300 300 300 TRP TRP B . n 
B 1 301 SER 301 301 301 SER SER B . n 
B 1 302 PHE 302 302 302 PHE PHE B . n 
B 1 303 VAL 303 303 303 VAL VAL B . n 
B 1 304 PRO 304 304 304 PRO PRO B . n 
B 1 305 GLY 305 305 305 GLY GLY B . n 
B 1 306 PHE 306 306 306 PHE PHE B . n 
B 1 307 GLY 307 307 307 GLY GLY B . n 
B 1 308 GLY 308 308 308 GLY GLY B . n 
B 1 309 SER 309 309 309 SER SER B . n 
B 1 310 CYS 310 310 310 CYS CYS B . n 
B 1 311 GLN 311 311 311 GLN GLN B . n 
B 1 312 ARG 312 312 312 ARG ARG B . n 
B 1 313 ASN 313 313 313 ASN ASN B . n 
B 1 314 SER 314 314 314 SER SER B . n 
B 1 315 LYS 315 315 315 LYS LYS B . n 
B 1 316 SER 316 316 316 SER SER B . n 
B 1 317 LEU 317 317 317 LEU LEU B . n 
B 1 318 ASP 318 318 318 ASP ASP B . n 
B 1 319 GLY 319 319 319 GLY GLY B . n 
B 1 320 ARG 320 320 320 ARG ARG B . n 
B 1 321 PRO 321 321 321 PRO PRO B . n 
B 1 322 SER 322 322 322 SER SER B . n 
B 1 323 THR 323 323 323 THR THR B . n 
B 1 324 ASP 324 324 324 ASP ASP B . n 
B 1 325 ASN 325 325 325 ASN ASN B . n 
B 1 326 GLY 326 326 326 GLY GLY B . n 
B 1 327 TRP 327 327 327 TRP TRP B . n 
B 1 328 GLU 328 328 328 GLU GLU B . n 
B 1 329 ILE 329 329 329 ILE ILE B . n 
B 1 330 TYR 330 330 330 TYR TYR B . n 
B 1 331 PRO 331 331 331 PRO PRO B . n 
B 1 332 GLU 332 332 332 GLU GLU B . n 
B 1 333 GLY 333 333 333 GLY GLY B . n 
B 1 334 LEU 334 334 334 LEU LEU B . n 
B 1 335 GLY 335 335 335 GLY GLY B . n 
B 1 336 TYR 336 336 336 TYR TYR B . n 
B 1 337 VAL 337 337 337 VAL VAL B . n 
B 1 338 LEU 338 338 338 LEU LEU B . n 
B 1 339 ARG 339 339 339 ARG ARG B . n 
B 1 340 SER 340 340 340 SER SER B . n 
B 1 341 CYS 341 341 341 CYS CYS B . n 
B 1 342 ARG 342 342 342 ARG ARG B . n 
B 1 343 ASP 343 343 343 ASP ASP B . n 
B 1 344 ARG 344 344 344 ARG ARG B . n 
B 1 345 TYR 345 345 345 TYR TYR B . n 
B 1 346 LYS 346 346 346 LYS LYS B . n 
B 1 347 LYS 347 347 347 LYS LYS B . n 
B 1 348 PRO 348 348 348 PRO PRO B . n 
B 1 349 LEU 349 349 349 LEU LEU B . n 
B 1 350 TYR 350 350 350 TYR TYR B . n 
B 1 351 VAL 351 351 351 VAL VAL B . n 
B 1 352 THR 352 352 352 THR THR B . n 
B 1 353 GLU 353 353 353 GLU GLU B . n 
B 1 354 ASN 354 354 354 ASN ASN B . n 
B 1 355 GLY 355 355 355 GLY GLY B . n 
B 1 356 VAL 356 356 356 VAL VAL B . n 
B 1 357 ALA 357 357 357 ALA ALA B . n 
B 1 358 ASP 358 358 358 ASP ASP B . n 
B 1 359 ASP 359 359 359 ASP ASP B . n 
B 1 360 ARG 360 360 360 ARG ARG B . n 
B 1 361 ASP 361 361 361 ASP ASP B . n 
B 1 362 ILE 362 362 362 ILE ILE B . n 
B 1 363 TYR 363 363 363 TYR TYR B . n 
B 1 364 ARG 364 364 364 ARG ARG B . n 
B 1 365 PRO 365 365 365 PRO PRO B . n 
B 1 366 TYR 366 366 366 TYR TYR B . n 
B 1 367 SER 367 367 367 SER SER B . n 
B 1 368 LEU 368 368 368 LEU LEU B . n 
B 1 369 LEU 369 369 369 LEU LEU B . n 
B 1 370 ALA 370 370 370 ALA ALA B . n 
B 1 371 HIS 371 371 371 HIS HIS B . n 
B 1 372 LEU 372 372 372 LEU LEU B . n 
B 1 373 LYS 373 373 373 LYS LYS B . n 
B 1 374 ILE 374 374 374 ILE ILE B . n 
B 1 375 VAL 375 375 375 VAL VAL B . n 
B 1 376 GLU 376 376 376 GLU GLU B . n 
B 1 377 ASP 377 377 377 ASP ASP B . n 
B 1 378 CYS 378 378 378 CYS CYS B . n 
B 1 379 LEU 379 379 379 LEU LEU B . n 
B 1 380 LYS 380 380 380 LYS LYS B . n 
B 1 381 GLU 381 381 381 GLU GLU B . n 
B 1 382 ASN 382 382 382 ASN ASN B . n 
B 1 383 MET 383 383 383 MET MET B . n 
B 1 384 ASP 384 384 384 ASP ASP B . n 
B 1 385 LEU 385 385 385 LEU LEU B . n 
B 1 386 ARG 386 386 386 ARG ARG B . n 
B 1 387 GLY 387 387 387 GLY GLY B . n 
B 1 388 TYR 388 388 388 TYR TYR B . n 
B 1 389 MET 389 389 389 MET MET B . n 
B 1 390 HIS 390 390 390 HIS HIS B . n 
B 1 391 TRP 391 391 391 TRP TRP B . n 
B 1 392 SER 392 392 392 SER SER B . n 
B 1 393 ILE 393 393 393 ILE ILE B . n 
B 1 394 ILE 394 394 394 ILE ILE B . n 
B 1 395 ASP 395 395 395 ASP ASP B . n 
B 1 396 ASN 396 396 396 ASN ASN B . n 
B 1 397 PHE 397 397 397 PHE PHE B . n 
B 1 398 GLU 398 398 398 GLU GLU B . n 
B 1 399 TRP 399 399 399 TRP TRP B . n 
B 1 400 PRO 400 400 400 PRO PRO B . n 
B 1 401 MET 401 401 401 MET MET B . n 
B 1 402 GLY 402 402 402 GLY GLY B . n 
B 1 403 TYR 403 403 403 TYR TYR B . n 
B 1 404 SER 404 404 404 SER SER B . n 
B 1 405 MET 405 405 405 MET MET B . n 
B 1 406 ARG 406 406 406 ARG ARG B . n 
B 1 407 PHE 407 407 407 PHE PHE B . n 
B 1 408 GLY 408 408 408 GLY GLY B . n 
B 1 409 LEU 409 409 409 LEU LEU B . n 
B 1 410 VAL 410 410 410 VAL VAL B . n 
B 1 411 ARG 411 411 411 ARG ARG B . n 
B 1 412 VAL 412 412 412 VAL VAL B . n 
B 1 413 ASP 413 413 413 ASP ASP B . n 
B 1 414 PHE 414 414 414 PHE PHE B . n 
B 1 415 LYS 415 415 415 LYS LYS B . n 
B 1 416 GLN 416 416 416 GLN GLN B . n 
B 1 417 LYS 417 417 417 LYS LYS B . n 
B 1 418 LEU 418 418 418 LEU LEU B . n 
B 1 419 PHE 419 419 419 PHE PHE B . n 
B 1 420 THR 420 420 420 THR THR B . n 
B 1 421 PRO 421 421 421 PRO PRO B . n 
B 1 422 ARG 422 422 422 ARG ARG B . n 
B 1 423 PRO 423 423 423 PRO PRO B . n 
B 1 424 SER 424 424 424 SER SER B . n 
B 1 425 TYR 425 425 425 TYR TYR B . n 
B 1 426 TYR 426 426 426 TYR TYR B . n 
B 1 427 LEU 427 427 427 LEU LEU B . n 
B 1 428 PHE 428 428 428 PHE PHE B . n 
B 1 429 GLY 429 429 429 GLY GLY B . n 
B 1 430 GLN 430 430 430 GLN GLN B . n 
B 1 431 ILE 431 431 431 ILE ILE B . n 
B 1 432 ILE 432 432 432 ILE ILE B . n 
B 1 433 ASN 433 433 433 ASN ASN B . n 
B 1 434 SER 434 434 434 SER SER B . n 
B 1 435 ARG 435 435 435 ARG ARG B . n 
B 1 436 THR 436 436 436 THR THR B . n 
B 1 437 THR 437 437 437 THR THR B . n 
B 1 438 GLU 438 438 438 GLU GLU B . n 
B 1 439 PRO 439 439 439 PRO PRO B . n 
B 1 440 PHE 440 440 440 PHE PHE B . n 
B 1 441 LEU 441 441 441 LEU LEU B . n 
B 1 442 ASN 442 442 442 ASN ASN B . n 
B 1 443 LEU 443 443 443 LEU LEU B . n 
B 1 444 LEU 444 444 444 LEU LEU B . n 
B 1 445 LYS 445 445 445 LYS LYS B . n 
B 1 446 ALA 446 446 446 ALA ALA B . n 
B 1 447 TRP 447 447 447 TRP TRP B . n 
B 1 448 GLU 448 448 448 GLU GLU B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        GOL 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   GOL 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 GOL 1   501  501  GOL LIG A . 
D 2 GOL 1   501  501  GOL LIG B . 
E 3 HOH 1   601  867  HOH HOH A . 
E 3 HOH 2   602  931  HOH HOH A . 
E 3 HOH 3   603  996  HOH HOH A . 
E 3 HOH 4   604  1047 HOH HOH A . 
E 3 HOH 5   605  434  HOH HOH A . 
E 3 HOH 6   606  830  HOH HOH A . 
E 3 HOH 7   607  648  HOH HOH A . 
E 3 HOH 8   608  629  HOH HOH A . 
E 3 HOH 9   609  965  HOH HOH A . 
E 3 HOH 10  610  607  HOH HOH A . 
E 3 HOH 11  611  1092 HOH HOH A . 
E 3 HOH 12  612  595  HOH HOH A . 
E 3 HOH 13  613  483  HOH HOH A . 
E 3 HOH 14  614  592  HOH HOH A . 
E 3 HOH 15  615  429  HOH HOH A . 
E 3 HOH 16  616  836  HOH HOH A . 
E 3 HOH 17  617  538  HOH HOH A . 
E 3 HOH 18  618  451  HOH HOH A . 
E 3 HOH 19  619  149  HOH HOH A . 
E 3 HOH 20  620  886  HOH HOH A . 
E 3 HOH 21  621  984  HOH HOH A . 
E 3 HOH 22  622  182  HOH HOH A . 
E 3 HOH 23  623  319  HOH HOH A . 
E 3 HOH 24  624  500  HOH HOH A . 
E 3 HOH 25  625  878  HOH HOH A . 
E 3 HOH 26  626  15   HOH HOH A . 
E 3 HOH 27  627  543  HOH HOH A . 
E 3 HOH 28  628  349  HOH HOH A . 
E 3 HOH 29  629  221  HOH HOH A . 
E 3 HOH 30  630  750  HOH HOH A . 
E 3 HOH 31  631  137  HOH HOH A . 
E 3 HOH 32  632  354  HOH HOH A . 
E 3 HOH 33  633  377  HOH HOH A . 
E 3 HOH 34  634  309  HOH HOH A . 
E 3 HOH 35  635  605  HOH HOH A . 
E 3 HOH 36  636  321  HOH HOH A . 
E 3 HOH 37  637  343  HOH HOH A . 
E 3 HOH 38  638  174  HOH HOH A . 
E 3 HOH 39  639  1    HOH HOH A . 
E 3 HOH 40  640  667  HOH HOH A . 
E 3 HOH 41  641  689  HOH HOH A . 
E 3 HOH 42  642  115  HOH HOH A . 
E 3 HOH 43  643  190  HOH HOH A . 
E 3 HOH 44  644  102  HOH HOH A . 
E 3 HOH 45  645  348  HOH HOH A . 
E 3 HOH 46  646  269  HOH HOH A . 
E 3 HOH 47  647  18   HOH HOH A . 
E 3 HOH 48  648  266  HOH HOH A . 
E 3 HOH 49  649  200  HOH HOH A . 
E 3 HOH 50  650  20   HOH HOH A . 
E 3 HOH 51  651  334  HOH HOH A . 
E 3 HOH 52  652  166  HOH HOH A . 
E 3 HOH 53  653  8    HOH HOH A . 
E 3 HOH 54  654  742  HOH HOH A . 
E 3 HOH 55  655  417  HOH HOH A . 
E 3 HOH 56  656  797  HOH HOH A . 
E 3 HOH 57  657  655  HOH HOH A . 
E 3 HOH 58  658  465  HOH HOH A . 
E 3 HOH 59  659  147  HOH HOH A . 
E 3 HOH 60  660  813  HOH HOH A . 
E 3 HOH 61  661  313  HOH HOH A . 
E 3 HOH 62  662  154  HOH HOH A . 
E 3 HOH 63  663  603  HOH HOH A . 
E 3 HOH 64  664  467  HOH HOH A . 
E 3 HOH 65  665  393  HOH HOH A . 
E 3 HOH 66  666  732  HOH HOH A . 
E 3 HOH 67  667  185  HOH HOH A . 
E 3 HOH 68  668  56   HOH HOH A . 
E 3 HOH 69  669  445  HOH HOH A . 
E 3 HOH 70  670  247  HOH HOH A . 
E 3 HOH 71  671  637  HOH HOH A . 
E 3 HOH 72  672  521  HOH HOH A . 
E 3 HOH 73  673  111  HOH HOH A . 
E 3 HOH 74  674  307  HOH HOH A . 
E 3 HOH 75  675  96   HOH HOH A . 
E 3 HOH 76  676  116  HOH HOH A . 
E 3 HOH 77  677  584  HOH HOH A . 
E 3 HOH 78  678  423  HOH HOH A . 
E 3 HOH 79  679  228  HOH HOH A . 
E 3 HOH 80  680  179  HOH HOH A . 
E 3 HOH 81  681  39   HOH HOH A . 
E 3 HOH 82  682  90   HOH HOH A . 
E 3 HOH 83  683  370  HOH HOH A . 
E 3 HOH 84  684  93   HOH HOH A . 
E 3 HOH 85  685  509  HOH HOH A . 
E 3 HOH 86  686  787  HOH HOH A . 
E 3 HOH 87  687  485  HOH HOH A . 
E 3 HOH 88  688  345  HOH HOH A . 
E 3 HOH 89  689  29   HOH HOH A . 
E 3 HOH 90  690  203  HOH HOH A . 
E 3 HOH 91  691  85   HOH HOH A . 
E 3 HOH 92  692  76   HOH HOH A . 
E 3 HOH 93  693  234  HOH HOH A . 
E 3 HOH 94  694  494  HOH HOH A . 
E 3 HOH 95  695  400  HOH HOH A . 
E 3 HOH 96  696  781  HOH HOH A . 
E 3 HOH 97  697  37   HOH HOH A . 
E 3 HOH 98  698  134  HOH HOH A . 
E 3 HOH 99  699  531  HOH HOH A . 
E 3 HOH 100 700  402  HOH HOH A . 
E 3 HOH 101 701  237  HOH HOH A . 
E 3 HOH 102 702  481  HOH HOH A . 
E 3 HOH 103 703  103  HOH HOH A . 
E 3 HOH 104 704  69   HOH HOH A . 
E 3 HOH 105 705  596  HOH HOH A . 
E 3 HOH 106 706  227  HOH HOH A . 
E 3 HOH 107 707  549  HOH HOH A . 
E 3 HOH 108 708  900  HOH HOH A . 
E 3 HOH 109 709  48   HOH HOH A . 
E 3 HOH 110 710  34   HOH HOH A . 
E 3 HOH 111 711  114  HOH HOH A . 
E 3 HOH 112 712  501  HOH HOH A . 
E 3 HOH 113 713  929  HOH HOH A . 
E 3 HOH 114 714  219  HOH HOH A . 
E 3 HOH 115 715  405  HOH HOH A . 
E 3 HOH 116 716  35   HOH HOH A . 
E 3 HOH 117 717  222  HOH HOH A . 
E 3 HOH 118 718  492  HOH HOH A . 
E 3 HOH 119 719  12   HOH HOH A . 
E 3 HOH 120 720  807  HOH HOH A . 
E 3 HOH 121 721  721  HOH HOH A . 
E 3 HOH 122 722  61   HOH HOH A . 
E 3 HOH 123 723  64   HOH HOH A . 
E 3 HOH 124 724  868  HOH HOH A . 
E 3 HOH 125 725  117  HOH HOH A . 
E 3 HOH 126 726  455  HOH HOH A . 
E 3 HOH 127 727  74   HOH HOH A . 
E 3 HOH 128 728  919  HOH HOH A . 
E 3 HOH 129 729  551  HOH HOH A . 
E 3 HOH 130 730  217  HOH HOH A . 
E 3 HOH 131 731  594  HOH HOH A . 
E 3 HOH 132 732  21   HOH HOH A . 
E 3 HOH 133 733  110  HOH HOH A . 
E 3 HOH 134 734  387  HOH HOH A . 
E 3 HOH 135 735  597  HOH HOH A . 
E 3 HOH 136 736  784  HOH HOH A . 
E 3 HOH 137 737  384  HOH HOH A . 
E 3 HOH 138 738  497  HOH HOH A . 
E 3 HOH 139 739  518  HOH HOH A . 
E 3 HOH 140 740  45   HOH HOH A . 
E 3 HOH 141 741  727  HOH HOH A . 
E 3 HOH 142 742  236  HOH HOH A . 
E 3 HOH 143 743  146  HOH HOH A . 
E 3 HOH 144 744  356  HOH HOH A . 
E 3 HOH 145 745  1110 HOH HOH A . 
E 3 HOH 146 746  523  HOH HOH A . 
E 3 HOH 147 747  496  HOH HOH A . 
E 3 HOH 148 748  578  HOH HOH A . 
E 3 HOH 149 749  482  HOH HOH A . 
E 3 HOH 150 750  940  HOH HOH A . 
E 3 HOH 151 751  36   HOH HOH A . 
E 3 HOH 152 752  285  HOH HOH A . 
E 3 HOH 153 753  456  HOH HOH A . 
E 3 HOH 154 754  1120 HOH HOH A . 
E 3 HOH 155 755  986  HOH HOH A . 
E 3 HOH 156 756  113  HOH HOH A . 
E 3 HOH 157 757  280  HOH HOH A . 
E 3 HOH 158 758  441  HOH HOH A . 
E 3 HOH 159 759  431  HOH HOH A . 
E 3 HOH 160 760  737  HOH HOH A . 
E 3 HOH 161 761  87   HOH HOH A . 
E 3 HOH 162 762  173  HOH HOH A . 
E 3 HOH 163 763  279  HOH HOH A . 
E 3 HOH 164 764  775  HOH HOH A . 
E 3 HOH 165 765  295  HOH HOH A . 
E 3 HOH 166 766  106  HOH HOH A . 
E 3 HOH 167 767  100  HOH HOH A . 
E 3 HOH 168 768  363  HOH HOH A . 
E 3 HOH 169 769  359  HOH HOH A . 
E 3 HOH 170 770  1051 HOH HOH A . 
E 3 HOH 171 771  42   HOH HOH A . 
E 3 HOH 172 772  516  HOH HOH A . 
E 3 HOH 173 773  286  HOH HOH A . 
E 3 HOH 174 774  1038 HOH HOH A . 
E 3 HOH 175 775  169  HOH HOH A . 
E 3 HOH 176 776  659  HOH HOH A . 
E 3 HOH 177 777  508  HOH HOH A . 
E 3 HOH 178 778  884  HOH HOH A . 
E 3 HOH 179 779  1005 HOH HOH A . 
E 3 HOH 180 780  242  HOH HOH A . 
E 3 HOH 181 781  449  HOH HOH A . 
E 3 HOH 182 782  1003 HOH HOH A . 
E 3 HOH 183 783  379  HOH HOH A . 
E 3 HOH 184 784  197  HOH HOH A . 
E 3 HOH 185 785  1009 HOH HOH A . 
E 3 HOH 186 786  526  HOH HOH A . 
E 3 HOH 187 787  245  HOH HOH A . 
E 3 HOH 188 788  259  HOH HOH A . 
E 3 HOH 189 789  14   HOH HOH A . 
E 3 HOH 190 790  6    HOH HOH A . 
E 3 HOH 191 791  108  HOH HOH A . 
E 3 HOH 192 792  976  HOH HOH A . 
E 3 HOH 193 793  43   HOH HOH A . 
E 3 HOH 194 794  956  HOH HOH A . 
E 3 HOH 195 795  91   HOH HOH A . 
E 3 HOH 196 796  928  HOH HOH A . 
E 3 HOH 197 797  308  HOH HOH A . 
E 3 HOH 198 798  411  HOH HOH A . 
E 3 HOH 199 799  972  HOH HOH A . 
E 3 HOH 200 800  780  HOH HOH A . 
E 3 HOH 201 801  183  HOH HOH A . 
E 3 HOH 202 802  232  HOH HOH A . 
E 3 HOH 203 803  365  HOH HOH A . 
E 3 HOH 204 804  214  HOH HOH A . 
E 3 HOH 205 805  505  HOH HOH A . 
E 3 HOH 206 806  22   HOH HOH A . 
E 3 HOH 207 807  82   HOH HOH A . 
E 3 HOH 208 808  675  HOH HOH A . 
E 3 HOH 209 809  55   HOH HOH A . 
E 3 HOH 210 810  895  HOH HOH A . 
E 3 HOH 211 811  130  HOH HOH A . 
E 3 HOH 212 812  660  HOH HOH A . 
E 3 HOH 213 813  563  HOH HOH A . 
E 3 HOH 214 814  1030 HOH HOH A . 
E 3 HOH 215 815  437  HOH HOH A . 
E 3 HOH 216 816  503  HOH HOH A . 
E 3 HOH 217 817  609  HOH HOH A . 
E 3 HOH 218 818  1107 HOH HOH A . 
E 3 HOH 219 819  487  HOH HOH A . 
E 3 HOH 220 820  618  HOH HOH A . 
E 3 HOH 221 821  582  HOH HOH A . 
E 3 HOH 222 822  118  HOH HOH A . 
E 3 HOH 223 823  1079 HOH HOH A . 
E 3 HOH 224 824  347  HOH HOH A . 
E 3 HOH 225 825  628  HOH HOH A . 
E 3 HOH 226 826  548  HOH HOH A . 
E 3 HOH 227 827  760  HOH HOH A . 
E 3 HOH 228 828  475  HOH HOH A . 
E 3 HOH 229 829  168  HOH HOH A . 
E 3 HOH 230 830  443  HOH HOH A . 
E 3 HOH 231 831  210  HOH HOH A . 
E 3 HOH 232 832  88   HOH HOH A . 
E 3 HOH 233 833  340  HOH HOH A . 
E 3 HOH 234 834  3    HOH HOH A . 
E 3 HOH 235 835  350  HOH HOH A . 
E 3 HOH 236 836  615  HOH HOH A . 
E 3 HOH 237 837  635  HOH HOH A . 
E 3 HOH 238 838  138  HOH HOH A . 
E 3 HOH 239 839  28   HOH HOH A . 
E 3 HOH 240 840  530  HOH HOH A . 
E 3 HOH 241 841  1022 HOH HOH A . 
E 3 HOH 242 842  854  HOH HOH A . 
E 3 HOH 243 843  412  HOH HOH A . 
E 3 HOH 244 844  621  HOH HOH A . 
E 3 HOH 245 845  818  HOH HOH A . 
E 3 HOH 246 846  389  HOH HOH A . 
E 3 HOH 247 847  212  HOH HOH A . 
E 3 HOH 248 848  155  HOH HOH A . 
E 3 HOH 249 849  952  HOH HOH A . 
E 3 HOH 250 850  946  HOH HOH A . 
E 3 HOH 251 851  403  HOH HOH A . 
E 3 HOH 252 852  939  HOH HOH A . 
E 3 HOH 253 853  999  HOH HOH A . 
E 3 HOH 254 854  701  HOH HOH A . 
E 3 HOH 255 855  1028 HOH HOH A . 
E 3 HOH 256 856  490  HOH HOH A . 
E 3 HOH 257 857  223  HOH HOH A . 
E 3 HOH 258 858  535  HOH HOH A . 
E 3 HOH 259 859  47   HOH HOH A . 
E 3 HOH 260 860  270  HOH HOH A . 
E 3 HOH 261 861  163  HOH HOH A . 
E 3 HOH 262 862  601  HOH HOH A . 
E 3 HOH 263 863  63   HOH HOH A . 
E 3 HOH 264 864  7    HOH HOH A . 
E 3 HOH 265 865  438  HOH HOH A . 
E 3 HOH 266 866  1071 HOH HOH A . 
E 3 HOH 267 867  714  HOH HOH A . 
E 3 HOH 268 868  60   HOH HOH A . 
E 3 HOH 269 869  477  HOH HOH A . 
E 3 HOH 270 870  845  HOH HOH A . 
E 3 HOH 271 871  498  HOH HOH A . 
E 3 HOH 272 872  51   HOH HOH A . 
E 3 HOH 273 873  1095 HOH HOH A . 
E 3 HOH 274 874  306  HOH HOH A . 
E 3 HOH 275 875  574  HOH HOH A . 
E 3 HOH 276 876  702  HOH HOH A . 
E 3 HOH 277 877  814  HOH HOH A . 
E 3 HOH 278 878  733  HOH HOH A . 
E 3 HOH 279 879  690  HOH HOH A . 
E 3 HOH 280 880  506  HOH HOH A . 
E 3 HOH 281 881  98   HOH HOH A . 
E 3 HOH 282 882  979  HOH HOH A . 
E 3 HOH 283 883  944  HOH HOH A . 
E 3 HOH 284 884  692  HOH HOH A . 
E 3 HOH 285 885  480  HOH HOH A . 
E 3 HOH 286 886  1054 HOH HOH A . 
E 3 HOH 287 887  78   HOH HOH A . 
E 3 HOH 288 888  181  HOH HOH A . 
E 3 HOH 289 889  382  HOH HOH A . 
E 3 HOH 290 890  1082 HOH HOH A . 
E 3 HOH 291 891  361  HOH HOH A . 
E 3 HOH 292 892  608  HOH HOH A . 
E 3 HOH 293 893  825  HOH HOH A . 
E 3 HOH 294 894  598  HOH HOH A . 
E 3 HOH 295 895  515  HOH HOH A . 
E 3 HOH 296 896  404  HOH HOH A . 
E 3 HOH 297 897  906  HOH HOH A . 
E 3 HOH 298 898  162  HOH HOH A . 
E 3 HOH 299 899  1084 HOH HOH A . 
E 3 HOH 300 900  1059 HOH HOH A . 
E 3 HOH 301 901  1008 HOH HOH A . 
E 3 HOH 302 902  678  HOH HOH A . 
E 3 HOH 303 903  479  HOH HOH A . 
E 3 HOH 304 904  864  HOH HOH A . 
E 3 HOH 305 905  302  HOH HOH A . 
E 3 HOH 306 906  981  HOH HOH A . 
E 3 HOH 307 907  300  HOH HOH A . 
E 3 HOH 308 908  86   HOH HOH A . 
E 3 HOH 309 909  774  HOH HOH A . 
E 3 HOH 310 910  453  HOH HOH A . 
E 3 HOH 311 911  962  HOH HOH A . 
E 3 HOH 312 912  673  HOH HOH A . 
E 3 HOH 313 913  1115 HOH HOH A . 
E 3 HOH 314 914  394  HOH HOH A . 
E 3 HOH 315 915  573  HOH HOH A . 
E 3 HOH 316 916  38   HOH HOH A . 
E 3 HOH 317 917  193  HOH HOH A . 
E 3 HOH 318 918  152  HOH HOH A . 
E 3 HOH 319 919  504  HOH HOH A . 
E 3 HOH 320 920  532  HOH HOH A . 
E 3 HOH 321 921  829  HOH HOH A . 
E 3 HOH 322 922  524  HOH HOH A . 
E 3 HOH 323 923  546  HOH HOH A . 
E 3 HOH 324 924  196  HOH HOH A . 
E 3 HOH 325 925  547  HOH HOH A . 
E 3 HOH 326 926  751  HOH HOH A . 
E 3 HOH 327 927  413  HOH HOH A . 
E 3 HOH 328 928  694  HOH HOH A . 
E 3 HOH 329 929  647  HOH HOH A . 
E 3 HOH 330 930  320  HOH HOH A . 
E 3 HOH 331 931  576  HOH HOH A . 
E 3 HOH 332 932  969  HOH HOH A . 
E 3 HOH 333 933  1061 HOH HOH A . 
E 3 HOH 334 934  463  HOH HOH A . 
E 3 HOH 335 935  493  HOH HOH A . 
E 3 HOH 336 936  470  HOH HOH A . 
E 3 HOH 337 937  730  HOH HOH A . 
E 3 HOH 338 938  324  HOH HOH A . 
E 3 HOH 339 939  297  HOH HOH A . 
E 3 HOH 340 940  911  HOH HOH A . 
E 3 HOH 341 941  876  HOH HOH A . 
E 3 HOH 342 942  58   HOH HOH A . 
E 3 HOH 343 943  557  HOH HOH A . 
E 3 HOH 344 944  452  HOH HOH A . 
E 3 HOH 345 945  658  HOH HOH A . 
E 3 HOH 346 946  859  HOH HOH A . 
E 3 HOH 347 947  653  HOH HOH A . 
E 3 HOH 348 948  230  HOH HOH A . 
E 3 HOH 349 949  650  HOH HOH A . 
E 3 HOH 350 950  593  HOH HOH A . 
E 3 HOH 351 951  891  HOH HOH A . 
E 3 HOH 352 952  755  HOH HOH A . 
E 3 HOH 353 953  901  HOH HOH A . 
E 3 HOH 354 954  178  HOH HOH A . 
E 3 HOH 355 955  982  HOH HOH A . 
E 3 HOH 356 956  682  HOH HOH A . 
E 3 HOH 357 957  330  HOH HOH A . 
E 3 HOH 358 958  1042 HOH HOH A . 
E 3 HOH 359 959  1126 HOH HOH A . 
E 3 HOH 360 960  710  HOH HOH A . 
E 3 HOH 361 961  1064 HOH HOH A . 
E 3 HOH 362 962  951  HOH HOH A . 
E 3 HOH 363 963  1023 HOH HOH A . 
E 3 HOH 364 964  580  HOH HOH A . 
E 3 HOH 365 965  1037 HOH HOH A . 
E 3 HOH 366 966  846  HOH HOH A . 
E 3 HOH 367 967  418  HOH HOH A . 
E 3 HOH 368 968  344  HOH HOH A . 
E 3 HOH 369 969  335  HOH HOH A . 
E 3 HOH 370 970  353  HOH HOH A . 
E 3 HOH 371 971  882  HOH HOH A . 
E 3 HOH 372 972  826  HOH HOH A . 
E 3 HOH 373 973  422  HOH HOH A . 
E 3 HOH 374 974  955  HOH HOH A . 
E 3 HOH 375 975  1058 HOH HOH A . 
E 3 HOH 376 976  700  HOH HOH A . 
E 3 HOH 377 977  966  HOH HOH A . 
E 3 HOH 378 978  176  HOH HOH A . 
E 3 HOH 379 979  865  HOH HOH A . 
E 3 HOH 380 980  704  HOH HOH A . 
E 3 HOH 381 981  1049 HOH HOH A . 
E 3 HOH 382 982  1076 HOH HOH A . 
E 3 HOH 383 983  960  HOH HOH A . 
E 3 HOH 384 984  462  HOH HOH A . 
E 3 HOH 385 985  863  HOH HOH A . 
E 3 HOH 386 986  927  HOH HOH A . 
E 3 HOH 387 987  789  HOH HOH A . 
E 3 HOH 388 988  949  HOH HOH A . 
E 3 HOH 389 989  1083 HOH HOH A . 
E 3 HOH 390 990  676  HOH HOH A . 
E 3 HOH 391 991  293  HOH HOH A . 
E 3 HOH 392 992  1032 HOH HOH A . 
E 3 HOH 393 993  743  HOH HOH A . 
E 3 HOH 394 994  435  HOH HOH A . 
E 3 HOH 395 995  1127 HOH HOH A . 
E 3 HOH 396 996  914  HOH HOH A . 
E 3 HOH 397 997  1128 HOH HOH A . 
E 3 HOH 398 998  941  HOH HOH A . 
E 3 HOH 399 999  819  HOH HOH A . 
E 3 HOH 400 1000 782  HOH HOH A . 
E 3 HOH 401 1001 885  HOH HOH A . 
E 3 HOH 402 1002 824  HOH HOH A . 
E 3 HOH 403 1003 741  HOH HOH A . 
E 3 HOH 404 1004 883  HOH HOH A . 
E 3 HOH 405 1005 759  HOH HOH A . 
E 3 HOH 406 1006 331  HOH HOH A . 
E 3 HOH 407 1007 722  HOH HOH A . 
E 3 HOH 408 1008 1119 HOH HOH A . 
E 3 HOH 409 1009 550  HOH HOH A . 
E 3 HOH 410 1010 1004 HOH HOH A . 
E 3 HOH 411 1011 853  HOH HOH A . 
E 3 HOH 412 1012 195  HOH HOH A . 
E 3 HOH 413 1013 401  HOH HOH A . 
E 3 HOH 414 1014 758  HOH HOH A . 
E 3 HOH 415 1015 476  HOH HOH A . 
E 3 HOH 416 1016 766  HOH HOH A . 
E 3 HOH 417 1017 669  HOH HOH A . 
E 3 HOH 418 1018 729  HOH HOH A . 
E 3 HOH 419 1019 135  HOH HOH A . 
E 3 HOH 420 1020 1091 HOH HOH A . 
E 3 HOH 421 1021 699  HOH HOH A . 
E 3 HOH 422 1022 662  HOH HOH A . 
E 3 HOH 423 1023 785  HOH HOH A . 
E 3 HOH 424 1024 1014 HOH HOH A . 
E 3 HOH 425 1025 918  HOH HOH A . 
E 3 HOH 426 1026 1088 HOH HOH A . 
E 3 HOH 427 1027 208  HOH HOH A . 
E 3 HOH 428 1028 1020 HOH HOH A . 
E 3 HOH 429 1029 804  HOH HOH A . 
E 3 HOH 430 1030 1106 HOH HOH A . 
E 3 HOH 431 1031 974  HOH HOH A . 
E 3 HOH 432 1032 469  HOH HOH A . 
E 3 HOH 433 1033 838  HOH HOH A . 
E 3 HOH 434 1034 457  HOH HOH A . 
E 3 HOH 435 1035 696  HOH HOH A . 
E 3 HOH 436 1036 961  HOH HOH A . 
E 3 HOH 437 1037 935  HOH HOH A . 
E 3 HOH 438 1038 990  HOH HOH A . 
E 3 HOH 439 1039 736  HOH HOH A . 
E 3 HOH 440 1040 273  HOH HOH A . 
E 3 HOH 441 1041 198  HOH HOH A . 
E 3 HOH 442 1042 644  HOH HOH A . 
E 3 HOH 443 1043 312  HOH HOH A . 
E 3 HOH 444 1044 1108 HOH HOH A . 
E 3 HOH 445 1045 238  HOH HOH A . 
E 3 HOH 446 1046 1118 HOH HOH A . 
E 3 HOH 447 1047 790  HOH HOH A . 
E 3 HOH 448 1048 1109 HOH HOH A . 
E 3 HOH 449 1049 613  HOH HOH A . 
E 3 HOH 450 1050 1073 HOH HOH A . 
E 3 HOH 451 1051 424  HOH HOH A . 
E 3 HOH 452 1052 847  HOH HOH A . 
E 3 HOH 453 1053 711  HOH HOH A . 
E 3 HOH 454 1054 522  HOH HOH A . 
E 3 HOH 455 1055 478  HOH HOH A . 
E 3 HOH 456 1056 1101 HOH HOH A . 
E 3 HOH 457 1057 1105 HOH HOH A . 
E 3 HOH 458 1058 430  HOH HOH A . 
E 3 HOH 459 1059 568  HOH HOH A . 
E 3 HOH 460 1060 619  HOH HOH A . 
E 3 HOH 461 1061 1093 HOH HOH A . 
E 3 HOH 462 1062 1063 HOH HOH A . 
E 3 HOH 463 1063 572  HOH HOH A . 
E 3 HOH 464 1064 897  HOH HOH A . 
E 3 HOH 465 1065 762  HOH HOH A . 
E 3 HOH 466 1066 1113 HOH HOH A . 
E 3 HOH 467 1067 471  HOH HOH A . 
E 3 HOH 468 1068 905  HOH HOH A . 
E 3 HOH 469 1069 612  HOH HOH A . 
E 3 HOH 470 1070 241  HOH HOH A . 
E 3 HOH 471 1071 301  HOH HOH A . 
E 3 HOH 472 1072 851  HOH HOH A . 
E 3 HOH 473 1073 707  HOH HOH A . 
E 3 HOH 474 1074 575  HOH HOH A . 
E 3 HOH 475 1075 244  HOH HOH A . 
E 3 HOH 476 1076 680  HOH HOH A . 
E 3 HOH 477 1077 663  HOH HOH A . 
E 3 HOH 478 1078 1122 HOH HOH A . 
E 3 HOH 479 1079 893  HOH HOH A . 
E 3 HOH 480 1080 1043 HOH HOH A . 
E 3 HOH 481 1081 698  HOH HOH A . 
E 3 HOH 482 1082 772  HOH HOH A . 
E 3 HOH 483 1083 706  HOH HOH A . 
E 3 HOH 484 1084 264  HOH HOH A . 
E 3 HOH 485 1085 1116 HOH HOH A . 
E 3 HOH 486 1086 674  HOH HOH A . 
E 3 HOH 487 1087 645  HOH HOH A . 
E 3 HOH 488 1088 1100 HOH HOH A . 
E 3 HOH 489 1089 725  HOH HOH A . 
E 3 HOH 490 1090 686  HOH HOH A . 
E 3 HOH 491 1091 399  HOH HOH A . 
E 3 HOH 492 1092 835  HOH HOH A . 
E 3 HOH 493 1093 1125 HOH HOH A . 
E 3 HOH 494 1094 908  HOH HOH A . 
E 3 HOH 495 1095 317  HOH HOH A . 
E 3 HOH 496 1096 1017 HOH HOH A . 
E 3 HOH 497 1097 610  HOH HOH A . 
E 3 HOH 498 1098 107  HOH HOH A . 
E 3 HOH 499 1099 734  HOH HOH A . 
E 3 HOH 500 1100 858  HOH HOH A . 
E 3 HOH 501 1101 1103 HOH HOH A . 
E 3 HOH 502 1102 632  HOH HOH A . 
E 3 HOH 503 1103 943  HOH HOH A . 
E 3 HOH 504 1104 529  HOH HOH A . 
E 3 HOH 505 1105 715  HOH HOH A . 
E 3 HOH 506 1106 428  HOH HOH A . 
E 3 HOH 507 1107 1034 HOH HOH A . 
E 3 HOH 508 1108 661  HOH HOH A . 
E 3 HOH 509 1109 1089 HOH HOH A . 
E 3 HOH 510 1110 1039 HOH HOH A . 
E 3 HOH 511 1111 229  HOH HOH A . 
E 3 HOH 512 1112 513  HOH HOH A . 
E 3 HOH 513 1113 560  HOH HOH A . 
E 3 HOH 514 1114 420  HOH HOH A . 
E 3 HOH 515 1115 998  HOH HOH A . 
E 3 HOH 516 1116 636  HOH HOH A . 
E 3 HOH 517 1117 915  HOH HOH A . 
E 3 HOH 518 1118 793  HOH HOH A . 
E 3 HOH 519 1119 590  HOH HOH A . 
E 3 HOH 520 1120 337  HOH HOH A . 
E 3 HOH 521 1121 921  HOH HOH A . 
E 3 HOH 522 1122 808  HOH HOH A . 
E 3 HOH 523 1123 739  HOH HOH A . 
E 3 HOH 524 1124 252  HOH HOH A . 
E 3 HOH 525 1125 101  HOH HOH A . 
E 3 HOH 526 1126 614  HOH HOH A . 
E 3 HOH 527 1127 837  HOH HOH A . 
E 3 HOH 528 1128 1053 HOH HOH A . 
E 3 HOH 529 1129 831  HOH HOH A . 
E 3 HOH 530 1130 1055 HOH HOH A . 
E 3 HOH 531 1131 1036 HOH HOH A . 
E 3 HOH 532 1132 458  HOH HOH A . 
E 3 HOH 533 1133 672  HOH HOH A . 
E 3 HOH 534 1134 341  HOH HOH A . 
E 3 HOH 535 1135 569  HOH HOH A . 
E 3 HOH 536 1136 889  HOH HOH A . 
E 3 HOH 537 1137 1104 HOH HOH A . 
E 3 HOH 538 1138 1068 HOH HOH A . 
E 3 HOH 539 1139 677  HOH HOH A . 
E 3 HOH 540 1140 855  HOH HOH A . 
E 3 HOH 541 1141 856  HOH HOH A . 
E 3 HOH 542 1142 767  HOH HOH A . 
E 3 HOH 543 1143 1057 HOH HOH A . 
E 3 HOH 544 1144 968  HOH HOH A . 
E 3 HOH 545 1145 719  HOH HOH A . 
E 3 HOH 546 1146 687  HOH HOH A . 
E 3 HOH 547 1147 799  HOH HOH A . 
F 3 HOH 1   601  519  HOH HOH B . 
F 3 HOH 2   602  599  HOH HOH B . 
F 3 HOH 3   603  157  HOH HOH B . 
F 3 HOH 4   604  670  HOH HOH B . 
F 3 HOH 5   605  591  HOH HOH B . 
F 3 HOH 6   606  486  HOH HOH B . 
F 3 HOH 7   607  77   HOH HOH B . 
F 3 HOH 8   608  355  HOH HOH B . 
F 3 HOH 9   609  274  HOH HOH B . 
F 3 HOH 10  610  957  HOH HOH B . 
F 3 HOH 11  611  913  HOH HOH B . 
F 3 HOH 12  612  255  HOH HOH B . 
F 3 HOH 13  613  249  HOH HOH B . 
F 3 HOH 14  614  602  HOH HOH B . 
F 3 HOH 15  615  811  HOH HOH B . 
F 3 HOH 16  616  27   HOH HOH B . 
F 3 HOH 17  617  641  HOH HOH B . 
F 3 HOH 18  618  583  HOH HOH B . 
F 3 HOH 19  619  1006 HOH HOH B . 
F 3 HOH 20  620  311  HOH HOH B . 
F 3 HOH 21  621  937  HOH HOH B . 
F 3 HOH 22  622  50   HOH HOH B . 
F 3 HOH 23  623  810  HOH HOH B . 
F 3 HOH 24  624  398  HOH HOH B . 
F 3 HOH 25  625  545  HOH HOH B . 
F 3 HOH 26  626  161  HOH HOH B . 
F 3 HOH 27  627  454  HOH HOH B . 
F 3 HOH 28  628  184  HOH HOH B . 
F 3 HOH 29  629  2    HOH HOH B . 
F 3 HOH 30  630  1070 HOH HOH B . 
F 3 HOH 31  631  409  HOH HOH B . 
F 3 HOH 32  632  386  HOH HOH B . 
F 3 HOH 33  633  322  HOH HOH B . 
F 3 HOH 34  634  357  HOH HOH B . 
F 3 HOH 35  635  4    HOH HOH B . 
F 3 HOH 36  636  233  HOH HOH B . 
F 3 HOH 37  637  1002 HOH HOH B . 
F 3 HOH 38  638  756  HOH HOH B . 
F 3 HOH 39  639  71   HOH HOH B . 
F 3 HOH 40  640  40   HOH HOH B . 
F 3 HOH 41  641  126  HOH HOH B . 
F 3 HOH 42  642  296  HOH HOH B . 
F 3 HOH 43  643  735  HOH HOH B . 
F 3 HOH 44  644  468  HOH HOH B . 
F 3 HOH 45  645  364  HOH HOH B . 
F 3 HOH 46  646  375  HOH HOH B . 
F 3 HOH 47  647  685  HOH HOH B . 
F 3 HOH 48  648  261  HOH HOH B . 
F 3 HOH 49  649  289  HOH HOH B . 
F 3 HOH 50  650  199  HOH HOH B . 
F 3 HOH 51  651  132  HOH HOH B . 
F 3 HOH 52  652  109  HOH HOH B . 
F 3 HOH 53  653  11   HOH HOH B . 
F 3 HOH 54  654  127  HOH HOH B . 
F 3 HOH 55  655  192  HOH HOH B . 
F 3 HOH 56  656  1045 HOH HOH B . 
F 3 HOH 57  657  213  HOH HOH B . 
F 3 HOH 58  658  373  HOH HOH B . 
F 3 HOH 59  659  26   HOH HOH B . 
F 3 HOH 60  660  124  HOH HOH B . 
F 3 HOH 61  661  987  HOH HOH B . 
F 3 HOH 62  662  224  HOH HOH B . 
F 3 HOH 63  663  278  HOH HOH B . 
F 3 HOH 64  664  466  HOH HOH B . 
F 3 HOH 65  665  66   HOH HOH B . 
F 3 HOH 66  666  209  HOH HOH B . 
F 3 HOH 67  667  148  HOH HOH B . 
F 3 HOH 68  668  291  HOH HOH B . 
F 3 HOH 69  669  170  HOH HOH B . 
F 3 HOH 70  670  128  HOH HOH B . 
F 3 HOH 71  671  510  HOH HOH B . 
F 3 HOH 72  672  1085 HOH HOH B . 
F 3 HOH 73  673  272  HOH HOH B . 
F 3 HOH 74  674  95   HOH HOH B . 
F 3 HOH 75  675  46   HOH HOH B . 
F 3 HOH 76  676  1062 HOH HOH B . 
F 3 HOH 77  677  256  HOH HOH B . 
F 3 HOH 78  678  561  HOH HOH B . 
F 3 HOH 79  679  932  HOH HOH B . 
F 3 HOH 80  680  342  HOH HOH B . 
F 3 HOH 81  681  215  HOH HOH B . 
F 3 HOH 82  682  495  HOH HOH B . 
F 3 HOH 83  683  880  HOH HOH B . 
F 3 HOH 84  684  541  HOH HOH B . 
F 3 HOH 85  685  325  HOH HOH B . 
F 3 HOH 86  686  362  HOH HOH B . 
F 3 HOH 87  687  194  HOH HOH B . 
F 3 HOH 88  688  145  HOH HOH B . 
F 3 HOH 89  689  691  HOH HOH B . 
F 3 HOH 90  690  565  HOH HOH B . 
F 3 HOH 91  691  697  HOH HOH B . 
F 3 HOH 92  692  346  HOH HOH B . 
F 3 HOH 93  693  1029 HOH HOH B . 
F 3 HOH 94  694  165  HOH HOH B . 
F 3 HOH 95  695  332  HOH HOH B . 
F 3 HOH 96  696  180  HOH HOH B . 
F 3 HOH 97  697  446  HOH HOH B . 
F 3 HOH 98  698  333  HOH HOH B . 
F 3 HOH 99  699  33   HOH HOH B . 
F 3 HOH 100 700  23   HOH HOH B . 
F 3 HOH 101 701  189  HOH HOH B . 
F 3 HOH 102 702  514  HOH HOH B . 
F 3 HOH 103 703  372  HOH HOH B . 
F 3 HOH 104 704  540  HOH HOH B . 
F 3 HOH 105 705  89   HOH HOH B . 
F 3 HOH 106 706  639  HOH HOH B . 
F 3 HOH 107 707  436  HOH HOH B . 
F 3 HOH 108 708  129  HOH HOH B . 
F 3 HOH 109 709  13   HOH HOH B . 
F 3 HOH 110 710  25   HOH HOH B . 
F 3 HOH 111 711  649  HOH HOH B . 
F 3 HOH 112 712  511  HOH HOH B . 
F 3 HOH 113 713  376  HOH HOH B . 
F 3 HOH 114 714  577  HOH HOH B . 
F 3 HOH 115 715  765  HOH HOH B . 
F 3 HOH 116 716  288  HOH HOH B . 
F 3 HOH 117 717  175  HOH HOH B . 
F 3 HOH 118 718  75   HOH HOH B . 
F 3 HOH 119 719  104  HOH HOH B . 
F 3 HOH 120 720  53   HOH HOH B . 
F 3 HOH 121 721  351  HOH HOH B . 
F 3 HOH 122 722  79   HOH HOH B . 
F 3 HOH 123 723  257  HOH HOH B . 
F 3 HOH 124 724  899  HOH HOH B . 
F 3 HOH 125 725  624  HOH HOH B . 
F 3 HOH 126 726  105  HOH HOH B . 
F 3 HOH 127 727  206  HOH HOH B . 
F 3 HOH 128 728  316  HOH HOH B . 
F 3 HOH 129 729  753  HOH HOH B . 
F 3 HOH 130 730  912  HOH HOH B . 
F 3 HOH 131 731  447  HOH HOH B . 
F 3 HOH 132 732  267  HOH HOH B . 
F 3 HOH 133 733  484  HOH HOH B . 
F 3 HOH 134 734  144  HOH HOH B . 
F 3 HOH 135 735  65   HOH HOH B . 
F 3 HOH 136 736  119  HOH HOH B . 
F 3 HOH 137 737  366  HOH HOH B . 
F 3 HOH 138 738  887  HOH HOH B . 
F 3 HOH 139 739  1024 HOH HOH B . 
F 3 HOH 140 740  303  HOH HOH B . 
F 3 HOH 141 741  17   HOH HOH B . 
F 3 HOH 142 742  432  HOH HOH B . 
F 3 HOH 143 743  121  HOH HOH B . 
F 3 HOH 144 744  211  HOH HOH B . 
F 3 HOH 145 745  299  HOH HOH B . 
F 3 HOH 146 746  139  HOH HOH B . 
F 3 HOH 147 747  684  HOH HOH B . 
F 3 HOH 148 748  439  HOH HOH B . 
F 3 HOH 149 749  634  HOH HOH B . 
F 3 HOH 150 750  207  HOH HOH B . 
F 3 HOH 151 751  769  HOH HOH B . 
F 3 HOH 152 752  188  HOH HOH B . 
F 3 HOH 153 753  805  HOH HOH B . 
F 3 HOH 154 754  41   HOH HOH B . 
F 3 HOH 155 755  380  HOH HOH B . 
F 3 HOH 156 756  282  HOH HOH B . 
F 3 HOH 157 757  24   HOH HOH B . 
F 3 HOH 158 758  218  HOH HOH B . 
F 3 HOH 159 759  172  HOH HOH B . 
F 3 HOH 160 760  397  HOH HOH B . 
F 3 HOH 161 761  821  HOH HOH B . 
F 3 HOH 162 762  381  HOH HOH B . 
F 3 HOH 163 763  205  HOH HOH B . 
F 3 HOH 164 764  5    HOH HOH B . 
F 3 HOH 165 765  275  HOH HOH B . 
F 3 HOH 166 766  626  HOH HOH B . 
F 3 HOH 167 767  80   HOH HOH B . 
F 3 HOH 168 768  771  HOH HOH B . 
F 3 HOH 169 769  554  HOH HOH B . 
F 3 HOH 170 770  32   HOH HOH B . 
F 3 HOH 171 771  59   HOH HOH B . 
F 3 HOH 172 772  143  HOH HOH B . 
F 3 HOH 173 773  489  HOH HOH B . 
F 3 HOH 174 774  896  HOH HOH B . 
F 3 HOH 175 775  120  HOH HOH B . 
F 3 HOH 176 776  555  HOH HOH B . 
F 3 HOH 177 777  720  HOH HOH B . 
F 3 HOH 178 778  326  HOH HOH B . 
F 3 HOH 179 779  54   HOH HOH B . 
F 3 HOH 180 780  97   HOH HOH B . 
F 3 HOH 181 781  226  HOH HOH B . 
F 3 HOH 182 782  410  HOH HOH B . 
F 3 HOH 183 783  159  HOH HOH B . 
F 3 HOH 184 784  566  HOH HOH B . 
F 3 HOH 185 785  81   HOH HOH B . 
F 3 HOH 186 786  558  HOH HOH B . 
F 3 HOH 187 787  231  HOH HOH B . 
F 3 HOH 188 788  754  HOH HOH B . 
F 3 HOH 189 789  544  HOH HOH B . 
F 3 HOH 190 790  44   HOH HOH B . 
F 3 HOH 191 791  534  HOH HOH B . 
F 3 HOH 192 792  136  HOH HOH B . 
F 3 HOH 193 793  186  HOH HOH B . 
F 3 HOH 194 794  537  HOH HOH B . 
F 3 HOH 195 795  160  HOH HOH B . 
F 3 HOH 196 796  73   HOH HOH B . 
F 3 HOH 197 797  315  HOH HOH B . 
F 3 HOH 198 798  260  HOH HOH B . 
F 3 HOH 199 799  151  HOH HOH B . 
F 3 HOH 200 800  991  HOH HOH B . 
F 3 HOH 201 801  141  HOH HOH B . 
F 3 HOH 202 802  834  HOH HOH B . 
F 3 HOH 203 803  820  HOH HOH B . 
F 3 HOH 204 804  304  HOH HOH B . 
F 3 HOH 205 805  9    HOH HOH B . 
F 3 HOH 206 806  67   HOH HOH B . 
F 3 HOH 207 807  651  HOH HOH B . 
F 3 HOH 208 808  1026 HOH HOH B . 
F 3 HOH 209 809  444  HOH HOH B . 
F 3 HOH 210 810  585  HOH HOH B . 
F 3 HOH 211 811  553  HOH HOH B . 
F 3 HOH 212 812  360  HOH HOH B . 
F 3 HOH 213 813  123  HOH HOH B . 
F 3 HOH 214 814  204  HOH HOH B . 
F 3 HOH 215 815  216  HOH HOH B . 
F 3 HOH 216 816  947  HOH HOH B . 
F 3 HOH 217 817  220  HOH HOH B . 
F 3 HOH 218 818  122  HOH HOH B . 
F 3 HOH 219 819  881  HOH HOH B . 
F 3 HOH 220 820  1074 HOH HOH B . 
F 3 HOH 221 821  671  HOH HOH B . 
F 3 HOH 222 822  62   HOH HOH B . 
F 3 HOH 223 823  801  HOH HOH B . 
F 3 HOH 224 824  488  HOH HOH B . 
F 3 HOH 225 825  94   HOH HOH B . 
F 3 HOH 226 826  177  HOH HOH B . 
F 3 HOH 227 827  358  HOH HOH B . 
F 3 HOH 228 828  542  HOH HOH B . 
F 3 HOH 229 829  16   HOH HOH B . 
F 3 HOH 230 830  31   HOH HOH B . 
F 3 HOH 231 831  879  HOH HOH B . 
F 3 HOH 232 832  254  HOH HOH B . 
F 3 HOH 233 833  131  HOH HOH B . 
F 3 HOH 234 834  84   HOH HOH B . 
F 3 HOH 235 835  1069 HOH HOH B . 
F 3 HOH 236 836  738  HOH HOH B . 
F 3 HOH 237 837  611  HOH HOH B . 
F 3 HOH 238 838  70   HOH HOH B . 
F 3 HOH 239 839  92   HOH HOH B . 
F 3 HOH 240 840  10   HOH HOH B . 
F 3 HOH 241 841  873  HOH HOH B . 
F 3 HOH 242 842  262  HOH HOH B . 
F 3 HOH 243 843  903  HOH HOH B . 
F 3 HOH 244 844  314  HOH HOH B . 
F 3 HOH 245 845  1124 HOH HOH B . 
F 3 HOH 246 846  248  HOH HOH B . 
F 3 HOH 247 847  133  HOH HOH B . 
F 3 HOH 248 848  586  HOH HOH B . 
F 3 HOH 249 849  201  HOH HOH B . 
F 3 HOH 250 850  327  HOH HOH B . 
F 3 HOH 251 851  512  HOH HOH B . 
F 3 HOH 252 852  383  HOH HOH B . 
F 3 HOH 253 853  371  HOH HOH B . 
F 3 HOH 254 854  890  HOH HOH B . 
F 3 HOH 255 855  623  HOH HOH B . 
F 3 HOH 256 856  502  HOH HOH B . 
F 3 HOH 257 857  507  HOH HOH B . 
F 3 HOH 258 858  1060 HOH HOH B . 
F 3 HOH 259 859  336  HOH HOH B . 
F 3 HOH 260 860  922  HOH HOH B . 
F 3 HOH 261 861  948  HOH HOH B . 
F 3 HOH 262 862  491  HOH HOH B . 
F 3 HOH 263 863  125  HOH HOH B . 
F 3 HOH 264 864  744  HOH HOH B . 
F 3 HOH 265 865  562  HOH HOH B . 
F 3 HOH 266 866  728  HOH HOH B . 
F 3 HOH 267 867  140  HOH HOH B . 
F 3 HOH 268 868  499  HOH HOH B . 
F 3 HOH 269 869  898  HOH HOH B . 
F 3 HOH 270 870  187  HOH HOH B . 
F 3 HOH 271 871  778  HOH HOH B . 
F 3 HOH 272 872  49   HOH HOH B . 
F 3 HOH 273 873  440  HOH HOH B . 
F 3 HOH 274 874  525  HOH HOH B . 
F 3 HOH 275 875  581  HOH HOH B . 
F 3 HOH 276 876  142  HOH HOH B . 
F 3 HOH 277 877  683  HOH HOH B . 
F 3 HOH 278 878  933  HOH HOH B . 
F 3 HOH 279 879  763  HOH HOH B . 
F 3 HOH 280 880  284  HOH HOH B . 
F 3 HOH 281 881  19   HOH HOH B . 
F 3 HOH 282 882  464  HOH HOH B . 
F 3 HOH 283 883  1012 HOH HOH B . 
F 3 HOH 284 884  796  HOH HOH B . 
F 3 HOH 285 885  587  HOH HOH B . 
F 3 HOH 286 886  30   HOH HOH B . 
F 3 HOH 287 887  391  HOH HOH B . 
F 3 HOH 288 888  1072 HOH HOH B . 
F 3 HOH 289 889  600  HOH HOH B . 
F 3 HOH 290 890  448  HOH HOH B . 
F 3 HOH 291 891  638  HOH HOH B . 
F 3 HOH 292 892  374  HOH HOH B . 
F 3 HOH 293 893  1035 HOH HOH B . 
F 3 HOH 294 894  290  HOH HOH B . 
F 3 HOH 295 895  167  HOH HOH B . 
F 3 HOH 296 896  378  HOH HOH B . 
F 3 HOH 297 897  985  HOH HOH B . 
F 3 HOH 298 898  786  HOH HOH B . 
F 3 HOH 299 899  791  HOH HOH B . 
F 3 HOH 300 900  323  HOH HOH B . 
F 3 HOH 301 901  533  HOH HOH B . 
F 3 HOH 302 902  246  HOH HOH B . 
F 3 HOH 303 903  171  HOH HOH B . 
F 3 HOH 304 904  958  HOH HOH B . 
F 3 HOH 305 905  369  HOH HOH B . 
F 3 HOH 306 906  705  HOH HOH B . 
F 3 HOH 307 907  392  HOH HOH B . 
F 3 HOH 308 908  552  HOH HOH B . 
F 3 HOH 309 909  352  HOH HOH B . 
F 3 HOH 310 910  869  HOH HOH B . 
F 3 HOH 311 911  622  HOH HOH B . 
F 3 HOH 312 912  527  HOH HOH B . 
F 3 HOH 313 913  757  HOH HOH B . 
F 3 HOH 314 914  112  HOH HOH B . 
F 3 HOH 315 915  367  HOH HOH B . 
F 3 HOH 316 916  909  HOH HOH B . 
F 3 HOH 317 917  625  HOH HOH B . 
F 3 HOH 318 918  1117 HOH HOH B . 
F 3 HOH 319 919  472  HOH HOH B . 
F 3 HOH 320 920  871  HOH HOH B . 
F 3 HOH 321 921  872  HOH HOH B . 
F 3 HOH 322 922  718  HOH HOH B . 
F 3 HOH 323 923  1027 HOH HOH B . 
F 3 HOH 324 924  421  HOH HOH B . 
F 3 HOH 325 925  643  HOH HOH B . 
F 3 HOH 326 926  1031 HOH HOH B . 
F 3 HOH 327 927  419  HOH HOH B . 
F 3 HOH 328 928  892  HOH HOH B . 
F 3 HOH 329 929  427  HOH HOH B . 
F 3 HOH 330 930  679  HOH HOH B . 
F 3 HOH 331 931  657  HOH HOH B . 
F 3 HOH 332 932  202  HOH HOH B . 
F 3 HOH 333 933  225  HOH HOH B . 
F 3 HOH 334 934  292  HOH HOH B . 
F 3 HOH 335 935  250  HOH HOH B . 
F 3 HOH 336 936  902  HOH HOH B . 
F 3 HOH 337 937  627  HOH HOH B . 
F 3 HOH 338 938  849  HOH HOH B . 
F 3 HOH 339 939  768  HOH HOH B . 
F 3 HOH 340 940  390  HOH HOH B . 
F 3 HOH 341 941  385  HOH HOH B . 
F 3 HOH 342 942  866  HOH HOH B . 
F 3 HOH 343 943  474  HOH HOH B . 
F 3 HOH 344 944  528  HOH HOH B . 
F 3 HOH 345 945  416  HOH HOH B . 
F 3 HOH 346 946  1007 HOH HOH B . 
F 3 HOH 347 947  1077 HOH HOH B . 
F 3 HOH 348 948  806  HOH HOH B . 
F 3 HOH 349 949  954  HOH HOH B . 
F 3 HOH 350 950  83   HOH HOH B . 
F 3 HOH 351 951  251  HOH HOH B . 
F 3 HOH 352 952  426  HOH HOH B . 
F 3 HOH 353 953  268  HOH HOH B . 
F 3 HOH 354 954  294  HOH HOH B . 
F 3 HOH 355 955  1086 HOH HOH B . 
F 3 HOH 356 956  717  HOH HOH B . 
F 3 HOH 357 957  823  HOH HOH B . 
F 3 HOH 358 958  652  HOH HOH B . 
F 3 HOH 359 959  338  HOH HOH B . 
F 3 HOH 360 960  99   HOH HOH B . 
F 3 HOH 361 961  844  HOH HOH B . 
F 3 HOH 362 962  318  HOH HOH B . 
F 3 HOH 363 963  1050 HOH HOH B . 
F 3 HOH 364 964  1090 HOH HOH B . 
F 3 HOH 365 965  396  HOH HOH B . 
F 3 HOH 366 966  668  HOH HOH B . 
F 3 HOH 367 967  664  HOH HOH B . 
F 3 HOH 368 968  654  HOH HOH B . 
F 3 HOH 369 969  567  HOH HOH B . 
F 3 HOH 370 970  930  HOH HOH B . 
F 3 HOH 371 971  1065 HOH HOH B . 
F 3 HOH 372 972  745  HOH HOH B . 
F 3 HOH 373 973  983  HOH HOH B . 
F 3 HOH 374 974  1075 HOH HOH B . 
F 3 HOH 375 975  997  HOH HOH B . 
F 3 HOH 376 976  559  HOH HOH B . 
F 3 HOH 377 977  841  HOH HOH B . 
F 3 HOH 378 978  425  HOH HOH B . 
F 3 HOH 379 979  310  HOH HOH B . 
F 3 HOH 380 980  517  HOH HOH B . 
F 3 HOH 381 981  640  HOH HOH B . 
F 3 HOH 382 982  695  HOH HOH B . 
F 3 HOH 383 983  746  HOH HOH B . 
F 3 HOH 384 984  1094 HOH HOH B . 
F 3 HOH 385 985  761  HOH HOH B . 
F 3 HOH 386 986  150  HOH HOH B . 
F 3 HOH 387 987  1016 HOH HOH B . 
F 3 HOH 388 988  1010 HOH HOH B . 
F 3 HOH 389 989  258  HOH HOH B . 
F 3 HOH 390 990  920  HOH HOH B . 
F 3 HOH 391 991  724  HOH HOH B . 
F 3 HOH 392 992  1066 HOH HOH B . 
F 3 HOH 393 993  191  HOH HOH B . 
F 3 HOH 394 994  1000 HOH HOH B . 
F 3 HOH 395 995  894  HOH HOH B . 
F 3 HOH 396 996  917  HOH HOH B . 
F 3 HOH 397 997  945  HOH HOH B . 
F 3 HOH 398 998  1078 HOH HOH B . 
F 3 HOH 399 999  795  HOH HOH B . 
F 3 HOH 400 1000 415  HOH HOH B . 
F 3 HOH 401 1001 712  HOH HOH B . 
F 3 HOH 402 1002 802  HOH HOH B . 
F 3 HOH 403 1003 839  HOH HOH B . 
F 3 HOH 404 1004 843  HOH HOH B . 
F 3 HOH 405 1005 938  HOH HOH B . 
F 3 HOH 406 1006 414  HOH HOH B . 
F 3 HOH 407 1007 850  HOH HOH B . 
F 3 HOH 408 1008 287  HOH HOH B . 
F 3 HOH 409 1009 408  HOH HOH B . 
F 3 HOH 410 1010 539  HOH HOH B . 
F 3 HOH 411 1011 1044 HOH HOH B . 
F 3 HOH 412 1012 1013 HOH HOH B . 
F 3 HOH 413 1013 923  HOH HOH B . 
F 3 HOH 414 1014 631  HOH HOH B . 
F 3 HOH 415 1015 713  HOH HOH B . 
F 3 HOH 416 1016 617  HOH HOH B . 
F 3 HOH 417 1017 460  HOH HOH B . 
F 3 HOH 418 1018 726  HOH HOH B . 
F 3 HOH 419 1019 809  HOH HOH B . 
F 3 HOH 420 1020 52   HOH HOH B . 
F 3 HOH 421 1021 977  HOH HOH B . 
F 3 HOH 422 1022 666  HOH HOH B . 
F 3 HOH 423 1023 803  HOH HOH B . 
F 3 HOH 424 1024 832  HOH HOH B . 
F 3 HOH 425 1025 72   HOH HOH B . 
F 3 HOH 426 1026 277  HOH HOH B . 
F 3 HOH 427 1027 681  HOH HOH B . 
F 3 HOH 428 1028 283  HOH HOH B . 
F 3 HOH 429 1029 1041 HOH HOH B . 
F 3 HOH 430 1030 579  HOH HOH B . 
F 3 HOH 431 1031 1056 HOH HOH B . 
F 3 HOH 432 1032 904  HOH HOH B . 
F 3 HOH 433 1033 1123 HOH HOH B . 
F 3 HOH 434 1034 973  HOH HOH B . 
F 3 HOH 435 1035 770  HOH HOH B . 
F 3 HOH 436 1036 406  HOH HOH B . 
F 3 HOH 437 1037 748  HOH HOH B . 
F 3 HOH 438 1038 852  HOH HOH B . 
F 3 HOH 439 1039 980  HOH HOH B . 
F 3 HOH 440 1040 281  HOH HOH B . 
F 3 HOH 441 1041 800  HOH HOH B . 
F 3 HOH 442 1042 589  HOH HOH B . 
F 3 HOH 443 1043 459  HOH HOH B . 
F 3 HOH 444 1044 749  HOH HOH B . 
F 3 HOH 445 1045 588  HOH HOH B . 
F 3 HOH 446 1046 827  HOH HOH B . 
F 3 HOH 447 1047 461  HOH HOH B . 
F 3 HOH 448 1048 239  HOH HOH B . 
F 3 HOH 449 1049 1112 HOH HOH B . 
F 3 HOH 450 1050 910  HOH HOH B . 
F 3 HOH 451 1051 656  HOH HOH B . 
F 3 HOH 452 1052 877  HOH HOH B . 
F 3 HOH 453 1053 339  HOH HOH B . 
F 3 HOH 454 1054 1001 HOH HOH B . 
F 3 HOH 455 1055 556  HOH HOH B . 
F 3 HOH 456 1056 1040 HOH HOH B . 
F 3 HOH 457 1057 329  HOH HOH B . 
F 3 HOH 458 1058 665  HOH HOH B . 
F 3 HOH 459 1059 633  HOH HOH B . 
F 3 HOH 460 1060 907  HOH HOH B . 
F 3 HOH 461 1061 776  HOH HOH B . 
F 3 HOH 462 1062 606  HOH HOH B . 
F 3 HOH 463 1063 963  HOH HOH B . 
F 3 HOH 464 1064 57   HOH HOH B . 
F 3 HOH 465 1065 158  HOH HOH B . 
F 3 HOH 466 1066 764  HOH HOH B . 
F 3 HOH 467 1067 1011 HOH HOH B . 
F 3 HOH 468 1068 305  HOH HOH B . 
F 3 HOH 469 1069 570  HOH HOH B . 
F 3 HOH 470 1070 388  HOH HOH B . 
F 3 HOH 471 1071 994  HOH HOH B . 
F 3 HOH 472 1072 708  HOH HOH B . 
F 3 HOH 473 1073 1130 HOH HOH B . 
F 3 HOH 474 1074 298  HOH HOH B . 
F 3 HOH 475 1075 164  HOH HOH B . 
F 3 HOH 476 1076 630  HOH HOH B . 
F 3 HOH 477 1077 788  HOH HOH B . 
F 3 HOH 478 1078 693  HOH HOH B . 
F 3 HOH 479 1079 989  HOH HOH B . 
F 3 HOH 480 1080 604  HOH HOH B . 
F 3 HOH 481 1081 564  HOH HOH B . 
F 3 HOH 482 1082 253  HOH HOH B . 
F 3 HOH 483 1083 828  HOH HOH B . 
F 3 HOH 484 1084 874  HOH HOH B . 
F 3 HOH 485 1085 395  HOH HOH B . 
F 3 HOH 486 1086 368  HOH HOH B . 
F 3 HOH 487 1087 875  HOH HOH B . 
F 3 HOH 488 1088 263  HOH HOH B . 
F 3 HOH 489 1089 442  HOH HOH B . 
F 3 HOH 490 1090 328  HOH HOH B . 
F 3 HOH 491 1091 276  HOH HOH B . 
F 3 HOH 492 1092 571  HOH HOH B . 
F 3 HOH 493 1093 620  HOH HOH B . 
F 3 HOH 494 1094 473  HOH HOH B . 
F 3 HOH 495 1095 520  HOH HOH B . 
F 3 HOH 496 1096 916  HOH HOH B . 
F 3 HOH 497 1097 975  HOH HOH B . 
F 3 HOH 498 1098 243  HOH HOH B . 
F 3 HOH 499 1099 235  HOH HOH B . 
F 3 HOH 500 1100 792  HOH HOH B . 
F 3 HOH 501 1101 407  HOH HOH B . 
F 3 HOH 502 1102 153  HOH HOH B . 
F 3 HOH 503 1103 536  HOH HOH B . 
F 3 HOH 504 1104 688  HOH HOH B . 
F 3 HOH 505 1105 703  HOH HOH B . 
F 3 HOH 506 1106 978  HOH HOH B . 
F 3 HOH 507 1107 1033 HOH HOH B . 
F 3 HOH 508 1108 860  HOH HOH B . 
F 3 HOH 509 1109 794  HOH HOH B . 
F 3 HOH 510 1110 642  HOH HOH B . 
F 3 HOH 511 1111 1019 HOH HOH B . 
F 3 HOH 512 1112 450  HOH HOH B . 
F 3 HOH 513 1113 709  HOH HOH B . 
F 3 HOH 514 1114 1080 HOH HOH B . 
F 3 HOH 515 1115 1098 HOH HOH B . 
F 3 HOH 516 1116 716  HOH HOH B . 
F 3 HOH 517 1117 822  HOH HOH B . 
F 3 HOH 518 1118 992  HOH HOH B . 
F 3 HOH 519 1119 833  HOH HOH B . 
F 3 HOH 520 1120 433  HOH HOH B . 
F 3 HOH 521 1121 783  HOH HOH B . 
F 3 HOH 522 1122 936  HOH HOH B . 
F 3 HOH 523 1123 265  HOH HOH B . 
F 3 HOH 524 1124 861  HOH HOH B . 
F 3 HOH 525 1125 1021 HOH HOH B . 
F 3 HOH 526 1126 240  HOH HOH B . 
F 3 HOH 527 1127 1018 HOH HOH B . 
F 3 HOH 528 1128 995  HOH HOH B . 
F 3 HOH 529 1129 1025 HOH HOH B . 
F 3 HOH 530 1130 1015 HOH HOH B . 
F 3 HOH 531 1131 1129 HOH HOH B . 
# 
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 1 A GLU 66  ? CG  ? A GLU 66  CG  
2  1 Y 1 A GLU 66  ? CD  ? A GLU 66  CD  
3  1 Y 1 A GLU 66  ? OE1 ? A GLU 66  OE1 
4  1 Y 1 A GLU 66  ? OE2 ? A GLU 66  OE2 
5  1 Y 1 A ARG 70  ? CG  ? A ARG 70  CG  
6  1 Y 1 A ARG 70  ? CD  ? A ARG 70  CD  
7  1 Y 1 A ARG 70  ? NE  ? A ARG 70  NE  
8  1 Y 1 A ARG 70  ? CZ  ? A ARG 70  CZ  
9  1 Y 1 A ARG 70  ? NH1 ? A ARG 70  NH1 
10 1 Y 1 A ARG 70  ? NH2 ? A ARG 70  NH2 
11 1 Y 1 A GLU 225 ? CG  ? A GLU 225 CG  
12 1 Y 1 A GLU 225 ? CD  ? A GLU 225 CD  
13 1 Y 1 A GLU 225 ? OE1 ? A GLU 225 OE1 
14 1 Y 1 A GLU 225 ? OE2 ? A GLU 225 OE2 
15 1 Y 1 A ARG 435 ? CG  ? A ARG 435 CG  
16 1 Y 1 A ARG 435 ? CD  ? A ARG 435 CD  
17 1 Y 1 A ARG 435 ? NE  ? A ARG 435 NE  
18 1 Y 1 A ARG 435 ? CZ  ? A ARG 435 CZ  
19 1 Y 1 A ARG 435 ? NH1 ? A ARG 435 NH1 
20 1 Y 1 A ARG 435 ? NH2 ? A ARG 435 NH2 
21 1 Y 1 B LYS 94  ? CG  ? B LYS 94  CG  
22 1 Y 1 B LYS 94  ? CD  ? B LYS 94  CD  
23 1 Y 1 B LYS 94  ? CE  ? B LYS 94  CE  
24 1 Y 1 B LYS 94  ? NZ  ? B LYS 94  NZ  
25 1 Y 1 B ASP 248 ? CG  ? B ASP 248 CG  
26 1 Y 1 B ASP 248 ? OD1 ? B ASP 248 OD1 
27 1 Y 1 B ASP 248 ? OD2 ? B ASP 248 OD2 
28 1 Y 1 B ARG 295 ? CG  ? B ARG 295 CG  
29 1 Y 1 B ARG 295 ? CD  ? B ARG 295 CD  
30 1 Y 1 B ARG 295 ? NE  ? B ARG 295 NE  
31 1 Y 1 B ARG 295 ? CZ  ? B ARG 295 CZ  
32 1 Y 1 B ARG 295 ? NH1 ? B ARG 295 NH1 
33 1 Y 1 B ARG 295 ? NH2 ? B ARG 295 NH2 
34 1 Y 1 B LYS 346 ? CG  ? B LYS 346 CG  
35 1 Y 1 B LYS 346 ? CD  ? B LYS 346 CD  
36 1 Y 1 B LYS 346 ? CE  ? B LYS 346 CE  
37 1 Y 1 B LYS 346 ? NZ  ? B LYS 346 NZ  
38 1 Y 1 B LYS 415 ? CG  ? B LYS 415 CG  
39 1 Y 1 B LYS 415 ? CD  ? B LYS 415 CD  
40 1 Y 1 B LYS 415 ? CE  ? B LYS 415 CE  
41 1 Y 1 B LYS 415 ? NZ  ? B LYS 415 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.19.2_4158: ???)' 1 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                    3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                    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                     8Y9Q 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     179.709 
_cell.length_a_esd                 ? 
_cell.length_b                     179.709 
_cell.length_b_esd                 ? 
_cell.length_c                     89.033 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         8Y9Q 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                92 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 41 21 2' 
_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                   8Y9Q 
_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             3.45 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          64.33 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'0.5 M Ammonium sulfate, 0.1 M Sodium citrate tribasic dihydrate pH 5.6, 1.0 M Lithium sulfate monohydrate' 
_exptl_crystal_grow.pdbx_pH_range   5.5-6.0 
_exptl_crystal_grow.temp            289.15 
# 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'MAR CCD 165 mm' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-11-04 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979183 
_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                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979183 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8Y9Q 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.95 
_reflns.d_resolution_low                               89.85 
_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                                     99543 
_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                           92.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                15.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          20.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.094 
_reflns.pdbx_Rpim_I_all                                0.021 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.091 
_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                                    1.95 
_reflns_shell.d_res_low                                     2.03 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.9 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4797 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               1.5 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.444 
_reflns_shell.pdbx_Rpim_I_all                               0.297 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.774 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          47.6 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.327 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8Y9Q 
_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                            1.96 
_refine.ls_d_res_low                             51.72 
_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                     96988 
_refine.ls_number_reflns_R_free                  4818 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    92.91 
_refine.ls_percent_reflns_R_free                 4.97 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1537 
_refine.ls_R_factor_R_free                       0.1719 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1527 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_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                      6KDC 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 15.64 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.13 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.96 
_refine_hist.d_res_low                        51.72 
_refine_hist.number_atoms_solvent             1078 
_refine_hist.number_atoms_total               8401 
_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        7311 
_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 ? 7556  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.958 ? 10238 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 6.865 ? 998   ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.056 ? 1056  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.012 ? 1326  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.96 1.98  . . 76  1517 47.00  . . . . 0.2629 . . . . . . . . . . . 0.2770 
'X-RAY DIFFRACTION' 1.98 2.01  . . 84  1849 56.00  . . . . 0.2284 . . . . . . . . . . . 0.2824 
'X-RAY DIFFRACTION' 2.01 2.03  . . 126 2112 65.00  . . . . 0.2077 . . . . . . . . . . . 0.2269 
'X-RAY DIFFRACTION' 2.03 2.06  . . 112 2417 74.00  . . . . 0.1942 . . . . . . . . . . . 0.2237 
'X-RAY DIFFRACTION' 2.06 2.08  . . 147 2591 79.00  . . . . 0.1773 . . . . . . . . . . . 0.2099 
'X-RAY DIFFRACTION' 2.08 2.11  . . 146 2756 84.00  . . . . 0.1665 . . . . . . . . . . . 0.1896 
'X-RAY DIFFRACTION' 2.11 2.14  . . 154 2909 90.00  . . . . 0.1691 . . . . . . . . . . . 0.1752 
'X-RAY DIFFRACTION' 2.14 2.17  . . 181 3074 94.00  . . . . 0.1598 . . . . . . . . . . . 0.1882 
'X-RAY DIFFRACTION' 2.17 2.21  . . 192 3143 97.00  . . . . 0.1558 . . . . . . . . . . . 0.1905 
'X-RAY DIFFRACTION' 2.21 2.24  . . 158 3253 99.00  . . . . 0.1562 . . . . . . . . . . . 0.1911 
'X-RAY DIFFRACTION' 2.24 2.28  . . 176 3304 100.00 . . . . 0.1523 . . . . . . . . . . . 0.2050 
'X-RAY DIFFRACTION' 2.28 2.32  . . 163 3240 100.00 . . . . 0.1484 . . . . . . . . . . . 0.1737 
'X-RAY DIFFRACTION' 2.32 2.37  . . 178 3286 100.00 . . . . 0.1488 . . . . . . . . . . . 0.1643 
'X-RAY DIFFRACTION' 2.37 2.42  . . 168 3284 100.00 . . . . 0.1542 . . . . . . . . . . . 0.1883 
'X-RAY DIFFRACTION' 2.42 2.47  . . 177 3282 100.00 . . . . 0.1596 . . . . . . . . . . . 0.1741 
'X-RAY DIFFRACTION' 2.47 2.53  . . 174 3272 100.00 . . . . 0.1553 . . . . . . . . . . . 0.1776 
'X-RAY DIFFRACTION' 2.53 2.59  . . 142 3306 100.00 . . . . 0.1529 . . . . . . . . . . . 0.1835 
'X-RAY DIFFRACTION' 2.59 2.66  . . 179 3298 100.00 . . . . 0.1554 . . . . . . . . . . . 0.1630 
'X-RAY DIFFRACTION' 2.66 2.74  . . 160 3296 100.00 . . . . 0.1508 . . . . . . . . . . . 0.1674 
'X-RAY DIFFRACTION' 2.74 2.83  . . 154 3325 100.00 . . . . 0.1582 . . . . . . . . . . . 0.1925 
'X-RAY DIFFRACTION' 2.83 2.93  . . 187 3291 100.00 . . . . 0.1636 . . . . . . . . . . . 0.1881 
'X-RAY DIFFRACTION' 2.93 3.04  . . 172 3320 100.00 . . . . 0.1582 . . . . . . . . . . . 0.1806 
'X-RAY DIFFRACTION' 3.04 3.18  . . 146 3350 100.00 . . . . 0.1573 . . . . . . . . . . . 0.1644 
'X-RAY DIFFRACTION' 3.18 3.35  . . 186 3294 100.00 . . . . 0.1489 . . . . . . . . . . . 0.1721 
'X-RAY DIFFRACTION' 3.35 3.56  . . 187 3325 100.00 . . . . 0.1354 . . . . . . . . . . . 0.1493 
'X-RAY DIFFRACTION' 3.56 3.84  . . 175 3348 100.00 . . . . 0.1320 . . . . . . . . . . . 0.1408 
'X-RAY DIFFRACTION' 3.84 4.22  . . 169 3353 100.00 . . . . 0.1207 . . . . . . . . . . . 0.1489 
'X-RAY DIFFRACTION' 4.22 4.83  . . 179 3378 100.00 . . . . 0.1198 . . . . . . . . . . . 0.1180 
'X-RAY DIFFRACTION' 4.83 6.09  . . 171 3434 100.00 . . . . 0.1581 . . . . . . . . . . . 0.1760 
'X-RAY DIFFRACTION' 6.09 51.72 . . 199 3563 100.00 . . . . 0.1738 . . . . . . . . . . . 0.1804 
# 
_struct.entry_id                     8Y9Q 
_struct.title                        'b-glucosidase from Thermotoga profunda Tp-BGL' 
_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        8Y9Q 
_struct_keywords.text            'glycoside hydrolase, cellulase, glucosidase, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    8Y9Q 
_struct_ref.pdbx_db_accession          8Y9Q 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8Y9Q A 1 ? 448 ? 8Y9Q 1 ? 448 ? 1 448 
2 1 8Y9Q B 1 ? 448 ? 8Y9Q 1 ? 448 ? 1 448 
# 
_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   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2680  ? 
1 MORE         -11   ? 
1 'SSA (A^2)'  32490 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,E 
1 2 B,D,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z    1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000   
2 'crystal symmetry operation' 7_554 y,x,-z-1 0.0000000000 1.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 -89.0330000000 
# 
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 LYS A 21  ? LYS A 25  ? LYS A 21  LYS A 25  5 ? 5  
HELX_P HELX_P2  AA2 THR A 29  ? ASP A 37  ? THR A 29  ASP A 37  1 ? 9  
HELX_P HELX_P3  AA3 ASP A 37  ? ASN A 43  ? ASP A 37  ASN A 43  1 ? 7  
HELX_P HELX_P4  AA4 LEU A 50  ? GLY A 54  ? LEU A 50  GLY A 54  5 ? 5  
HELX_P HELX_P5  AA5 ASP A 56  ? ILE A 71  ? ASP A 56  ILE A 71  1 ? 16 
HELX_P HELX_P6  AA6 GLU A 81  ? PHE A 86  ? GLU A 81  PHE A 86  1 ? 6  
HELX_P HELX_P7  AA7 ASP A 95  ? ALA A 100 ? ASP A 95  ALA A 100 5 ? 6  
HELX_P HELX_P8  AA8 ASP A 101 ? ARG A 118 ? ASP A 101 ARG A 118 1 ? 18 
HELX_P HELX_P9  AA9 ASP A 137 ? ASN A 145 ? ASP A 137 ASN A 145 1 ? 9  
HELX_P HELX_P10 AB1 SER A 150 ? ASP A 154 ? SER A 150 ASP A 154 5 ? 5  
HELX_P HELX_P11 AB2 ARG A 156 ? PHE A 172 ? ARG A 156 PHE A 172 1 ? 17 
HELX_P HELX_P12 AB3 GLU A 183 ? GLY A 194 ? GLU A 183 GLY A 194 1 ? 12 
HELX_P HELX_P13 AB4 ARG A 195 ? GLY A 198 ? ARG A 195 GLY A 198 5 ? 4  
HELX_P HELX_P14 AB5 ASN A 205 ? LYS A 228 ? ASN A 205 LYS A 228 1 ? 24 
HELX_P HELX_P15 AB6 ALA A 249 ? ASN A 258 ? ALA A 249 ASN A 258 1 ? 10 
HELX_P HELX_P16 AB7 ASN A 258 ? ILE A 266 ? ASN A 258 ILE A 266 1 ? 9  
HELX_P HELX_P17 AB8 ASP A 267 ? ILE A 269 ? ASP A 267 ILE A 269 5 ? 3  
HELX_P HELX_P18 AB9 PHE A 306 ? CYS A 310 ? PHE A 306 CYS A 310 5 ? 5  
HELX_P HELX_P19 AC1 PRO A 331 ? TYR A 345 ? PRO A 331 TYR A 345 1 ? 15 
HELX_P HELX_P20 AC2 TYR A 363 ? GLU A 381 ? TYR A 363 GLU A 381 1 ? 19 
HELX_P HELX_P21 AC3 GLU A 398 ? MET A 405 ? GLU A 398 MET A 405 5 ? 8  
HELX_P HELX_P22 AC4 ARG A 422 ? ARG A 435 ? ARG A 422 ARG A 435 1 ? 14 
HELX_P HELX_P23 AC5 THR A 437 ? GLU A 448 ? THR A 437 GLU A 448 5 ? 12 
HELX_P HELX_P24 AC6 LYS B 21  ? LYS B 25  ? LYS B 21  LYS B 25  5 ? 5  
HELX_P HELX_P25 AC7 THR B 29  ? ASP B 37  ? THR B 29  ASP B 37  1 ? 9  
HELX_P HELX_P26 AC8 ASP B 37  ? ASN B 43  ? ASP B 37  ASN B 43  1 ? 7  
HELX_P HELX_P27 AC9 LEU B 50  ? GLY B 54  ? LEU B 50  GLY B 54  5 ? 5  
HELX_P HELX_P28 AD1 ASP B 56  ? ILE B 71  ? ASP B 56  ILE B 71  1 ? 16 
HELX_P HELX_P29 AD2 GLU B 81  ? PHE B 86  ? GLU B 81  PHE B 86  1 ? 6  
HELX_P HELX_P30 AD3 ASP B 95  ? ALA B 100 ? ASP B 95  ALA B 100 5 ? 6  
HELX_P HELX_P31 AD4 ASP B 101 ? ARG B 118 ? ASP B 101 ARG B 118 1 ? 18 
HELX_P HELX_P32 AD5 ASP B 137 ? ASN B 145 ? ASP B 137 ASN B 145 1 ? 9  
HELX_P HELX_P33 AD6 SER B 150 ? ASP B 154 ? SER B 150 ASP B 154 5 ? 5  
HELX_P HELX_P34 AD7 ARG B 156 ? PHE B 172 ? ARG B 156 PHE B 172 1 ? 17 
HELX_P HELX_P35 AD8 GLU B 183 ? GLY B 194 ? GLU B 183 GLY B 194 1 ? 12 
HELX_P HELX_P36 AD9 ARG B 195 ? GLY B 198 ? ARG B 195 GLY B 198 5 ? 4  
HELX_P HELX_P37 AE1 ASN B 205 ? THR B 231 ? ASN B 205 THR B 231 1 ? 27 
HELX_P HELX_P38 AE2 ALA B 249 ? ASN B 258 ? ALA B 249 ASN B 258 1 ? 10 
HELX_P HELX_P39 AE3 ASN B 258 ? ARG B 264 ? ASN B 258 ARG B 264 1 ? 7  
HELX_P HELX_P40 AE4 VAL B 265 ? ILE B 269 ? VAL B 265 ILE B 269 5 ? 5  
HELX_P HELX_P41 AE5 PHE B 306 ? CYS B 310 ? PHE B 306 CYS B 310 5 ? 5  
HELX_P HELX_P42 AE6 PRO B 331 ? TYR B 345 ? PRO B 331 TYR B 345 1 ? 15 
HELX_P HELX_P43 AE7 TYR B 363 ? GLU B 381 ? TYR B 363 GLU B 381 1 ? 19 
HELX_P HELX_P44 AE8 GLU B 398 ? MET B 405 ? GLU B 398 MET B 405 5 ? 8  
HELX_P HELX_P45 AE9 ARG B 422 ? ARG B 435 ? ARG B 422 ARG B 435 1 ? 14 
HELX_P HELX_P46 AF1 THR B 437 ? GLU B 448 ? THR B 437 GLU B 448 5 ? 12 
# 
_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 PRO 200 A . ? PRO 200 A PRO 201 A ? PRO 201 A 1 -6.14 
2 TRP 391 A . ? TRP 391 A SER 392 A ? SER 392 A 1 -6.09 
3 PRO 200 B . ? PRO 200 B PRO 201 B ? PRO 201 B 1 -2.29 
4 TRP 391 B . ? TRP 391 B SER 392 B ? SER 392 B 1 4.32  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 9 ? 
AA5 ? 3 ? 
AA6 ? 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 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA1 7 8 ? parallel      
AA1 8 9 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA4 5 6 ? parallel      
AA4 6 7 ? parallel      
AA4 7 8 ? parallel      
AA4 8 9 ? parallel      
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA6 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 LEU A 7   ? ALA A 11  ? LEU A 7   ALA A 11  
AA1 2 VAL A 75  ? GLY A 79  ? VAL A 75  GLY A 79  
AA1 3 LYS A 121 ? ASN A 125 ? LYS A 121 ASN A 125 
AA1 4 ALA A 177 ? ASN A 182 ? ALA A 177 ASN A 182 
AA1 5 VAL A 235 ? ALA A 240 ? VAL A 235 ALA A 240 
AA1 6 LEU A 272 ? ASN A 275 ? LEU A 272 ASN A 275 
AA1 7 LEU A 349 ? GLU A 353 ? LEU A 349 GLU A 353 
AA1 8 LEU A 385 ? HIS A 390 ? LEU A 385 HIS A 390 
AA1 9 LEU A 7   ? ALA A 11  ? LEU A 7   ALA A 11  
AA2 1 CYS A 244 ? GLY A 246 ? CYS A 244 GLY A 246 
AA2 2 ALA A 280 ? SER A 290 ? ALA A 280 SER A 290 
AA2 3 LYS A 297 ? PHE A 302 ? LYS A 297 PHE A 302 
AA3 1 VAL A 410 ? ASP A 413 ? VAL A 410 ASP A 413 
AA3 2 LEU A 418 ? PRO A 421 ? LEU A 418 PRO A 421 
AA4 1 LEU B 7   ? ALA B 11  ? LEU B 7   ALA B 11  
AA4 2 VAL B 75  ? GLY B 79  ? VAL B 75  GLY B 79  
AA4 3 LYS B 121 ? ASN B 125 ? LYS B 121 ASN B 125 
AA4 4 ALA B 177 ? ASN B 182 ? ALA B 177 ASN B 182 
AA4 5 VAL B 235 ? ALA B 240 ? VAL B 235 ALA B 240 
AA4 6 LEU B 272 ? ASN B 275 ? LEU B 272 ASN B 275 
AA4 7 LEU B 349 ? GLU B 353 ? LEU B 349 GLU B 353 
AA4 8 LEU B 385 ? HIS B 390 ? LEU B 385 HIS B 390 
AA4 9 LEU B 7   ? ALA B 11  ? LEU B 7   ALA B 11  
AA5 1 CYS B 244 ? GLY B 246 ? CYS B 244 GLY B 246 
AA5 2 ALA B 280 ? SER B 290 ? ALA B 280 SER B 290 
AA5 3 LYS B 297 ? PHE B 302 ? LYS B 297 PHE B 302 
AA6 1 VAL B 410 ? ASP B 413 ? VAL B 410 ASP B 413 
AA6 2 LEU B 418 ? PRO B 421 ? LEU B 418 PRO B 421 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 10  ? N VAL A 10  O ARG A 77  ? O ARG A 77  
AA1 2 3 N ILE A 78  ? N ILE A 78  O ASN A 125 ? O ASN A 125 
AA1 3 4 N VAL A 124 ? N VAL A 124 O ALA A 177 ? O ALA A 177 
AA1 4 5 N PHE A 178 ? N PHE A 178 O GLY A 236 ? O GLY A 236 
AA1 5 6 N ILE A 237 ? N ILE A 237 O GLY A 273 ? O GLY A 273 
AA1 6 7 N VAL A 274 ? N VAL A 274 O TYR A 350 ? O TYR A 350 
AA1 7 8 N LEU A 349 ? N LEU A 349 O ARG A 386 ? O ARG A 386 
AA1 8 9 O HIS A 390 ? O HIS A 390 N GLY A 9   ? N GLY A 9   
AA2 1 2 N GLU A 245 ? N GLU A 245 O VAL A 282 ? O VAL A 282 
AA2 2 3 N LEU A 289 ? N LEU A 289 O ILE A 298 ? O ILE A 298 
AA3 1 2 N ARG A 411 ? N ARG A 411 O THR A 420 ? O THR A 420 
AA4 1 2 N VAL B 10  ? N VAL B 10  O ARG B 77  ? O ARG B 77  
AA4 2 3 N ILE B 78  ? N ILE B 78  O ASN B 125 ? O ASN B 125 
AA4 3 4 N VAL B 124 ? N VAL B 124 O ALA B 177 ? O ALA B 177 
AA4 4 5 N PHE B 178 ? N PHE B 178 O GLY B 236 ? O GLY B 236 
AA4 5 6 N TYR B 239 ? N TYR B 239 O GLY B 273 ? O GLY B 273 
AA4 6 7 N VAL B 274 ? N VAL B 274 O TYR B 350 ? O TYR B 350 
AA4 7 8 N LEU B 349 ? N LEU B 349 O ARG B 386 ? O ARG B 386 
AA4 8 9 O TYR B 388 ? O TYR B 388 N LEU B 7   ? N LEU B 7   
AA5 1 2 N GLU B 245 ? N GLU B 245 O ALA B 280 ? O ALA B 280 
AA5 2 3 N LEU B 289 ? N LEU B 289 O ILE B 298 ? O ILE B 298 
AA6 1 2 N ARG B 411 ? N ARG B 411 O THR B 420 ? O THR B 420 
# 
_pdbx_entry_details.entry_id                   8Y9Q 
_pdbx_entry_details.has_ligand_of_interest     Y 
_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 ASN A 28  ? ? -98.37  35.75   
2  1 PHE A 129 ? ? 71.57   -59.43  
3  1 PHE A 193 ? ? -156.08 38.20   
4  1 ASN A 205 ? ? -161.30 106.57  
5  1 ASP A 247 ? ? -78.04  -169.57 
6  1 ASN A 258 ? ? -124.51 -60.20  
7  1 SER A 314 ? ? -143.27 -145.85 
8  1 ASP A 358 ? ? -171.00 86.56   
9  1 TRP A 399 ? ? 45.83   -121.46 
10 1 ASN B 28  ? ? -93.44  38.21   
11 1 ASP B 95  ? ? 61.42   83.05   
12 1 PHE B 129 ? ? 74.05   -58.97  
13 1 ARG B 156 ? ? 142.85  -43.79  
14 1 PHE B 193 ? ? -156.97 37.47   
15 1 ASN B 205 ? ? -161.97 108.37  
16 1 SER B 314 ? ? -139.14 -144.06 
17 1 ASP B 358 ? ? -171.75 88.65   
18 1 TRP B 399 ? ? 43.96   -120.21 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 1144 ? 6.00 . 
2 1 O ? A HOH 1145 ? 6.23 . 
3 1 O ? A HOH 1146 ? 6.28 . 
4 1 O ? A HOH 1147 ? 6.85 . 
5 1 O ? B HOH 1129 ? 5.90 . 
6 1 O ? B HOH 1130 ? 7.30 . 
7 1 O ? B HOH 1131 ? 7.62 . 
# 
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 
LYS N    N N N 219 
LYS CA   C N S 220 
LYS C    C N N 221 
LYS O    O N N 222 
LYS CB   C N N 223 
LYS CG   C N N 224 
LYS CD   C N N 225 
LYS CE   C N N 226 
LYS NZ   N N N 227 
LYS OXT  O N N 228 
LYS H    H N N 229 
LYS H2   H N N 230 
LYS HA   H N N 231 
LYS HB2  H N N 232 
LYS HB3  H N N 233 
LYS HG2  H N N 234 
LYS HG3  H N N 235 
LYS HD2  H N N 236 
LYS HD3  H N N 237 
LYS HE2  H N N 238 
LYS HE3  H N N 239 
LYS HZ1  H N N 240 
LYS HZ2  H N N 241 
LYS HZ3  H N N 242 
LYS HXT  H N N 243 
MET N    N N N 244 
MET CA   C N S 245 
MET C    C N N 246 
MET O    O N N 247 
MET CB   C N N 248 
MET CG   C N N 249 
MET SD   S N N 250 
MET CE   C N N 251 
MET OXT  O N N 252 
MET H    H N N 253 
MET H2   H N N 254 
MET HA   H N N 255 
MET HB2  H N N 256 
MET HB3  H N N 257 
MET HG2  H N N 258 
MET HG3  H N N 259 
MET HE1  H N N 260 
MET HE2  H N N 261 
MET HE3  H N N 262 
MET HXT  H N N 263 
PHE N    N N N 264 
PHE CA   C N S 265 
PHE C    C N N 266 
PHE O    O N N 267 
PHE CB   C N N 268 
PHE CG   C Y N 269 
PHE CD1  C Y N 270 
PHE CD2  C Y N 271 
PHE CE1  C Y N 272 
PHE CE2  C Y N 273 
PHE CZ   C Y N 274 
PHE OXT  O N N 275 
PHE H    H N N 276 
PHE H2   H N N 277 
PHE HA   H N N 278 
PHE HB2  H N N 279 
PHE HB3  H N N 280 
PHE HD1  H N N 281 
PHE HD2  H N N 282 
PHE HE1  H N N 283 
PHE HE2  H N N 284 
PHE HZ   H N N 285 
PHE HXT  H N N 286 
PRO N    N N N 287 
PRO CA   C N S 288 
PRO C    C N N 289 
PRO O    O N N 290 
PRO CB   C N N 291 
PRO CG   C N N 292 
PRO CD   C N N 293 
PRO OXT  O N N 294 
PRO H    H N N 295 
PRO HA   H N N 296 
PRO HB2  H N N 297 
PRO HB3  H N N 298 
PRO HG2  H N N 299 
PRO HG3  H N N 300 
PRO HD2  H N N 301 
PRO HD3  H N N 302 
PRO HXT  H N N 303 
SER N    N N N 304 
SER CA   C N S 305 
SER C    C N N 306 
SER O    O N N 307 
SER CB   C N N 308 
SER OG   O N N 309 
SER OXT  O N N 310 
SER H    H N N 311 
SER H2   H N N 312 
SER HA   H N N 313 
SER HB2  H N N 314 
SER HB3  H N N 315 
SER HG   H N N 316 
SER HXT  H N N 317 
THR N    N N N 318 
THR CA   C N S 319 
THR C    C N N 320 
THR O    O N N 321 
THR CB   C N R 322 
THR OG1  O N N 323 
THR CG2  C N N 324 
THR OXT  O N N 325 
THR H    H N N 326 
THR H2   H N N 327 
THR HA   H N N 328 
THR HB   H N N 329 
THR HG1  H N N 330 
THR HG21 H N N 331 
THR HG22 H N N 332 
THR HG23 H N N 333 
THR HXT  H N N 334 
TRP N    N N N 335 
TRP CA   C N S 336 
TRP C    C N N 337 
TRP O    O N N 338 
TRP CB   C N N 339 
TRP CG   C Y N 340 
TRP CD1  C Y N 341 
TRP CD2  C Y N 342 
TRP NE1  N Y N 343 
TRP CE2  C Y N 344 
TRP CE3  C Y N 345 
TRP CZ2  C Y N 346 
TRP CZ3  C Y N 347 
TRP CH2  C Y N 348 
TRP OXT  O N N 349 
TRP H    H N N 350 
TRP H2   H N N 351 
TRP HA   H N N 352 
TRP HB2  H N N 353 
TRP HB3  H N N 354 
TRP HD1  H N N 355 
TRP HE1  H N N 356 
TRP HE3  H N N 357 
TRP HZ2  H N N 358 
TRP HZ3  H N N 359 
TRP HH2  H N N 360 
TRP HXT  H N N 361 
TYR N    N N N 362 
TYR CA   C N S 363 
TYR C    C N N 364 
TYR O    O N N 365 
TYR CB   C N N 366 
TYR CG   C Y N 367 
TYR CD1  C Y N 368 
TYR CD2  C Y N 369 
TYR CE1  C Y N 370 
TYR CE2  C Y N 371 
TYR CZ   C Y N 372 
TYR OH   O N N 373 
TYR OXT  O N N 374 
TYR H    H N N 375 
TYR H2   H N N 376 
TYR HA   H N N 377 
TYR HB2  H N N 378 
TYR HB3  H N N 379 
TYR HD1  H N N 380 
TYR HD2  H N N 381 
TYR HE1  H N N 382 
TYR HE2  H N N 383 
TYR HH   H N N 384 
TYR HXT  H N N 385 
VAL N    N N N 386 
VAL CA   C N S 387 
VAL C    C N N 388 
VAL O    O N N 389 
VAL CB   C N N 390 
VAL CG1  C N N 391 
VAL CG2  C N N 392 
VAL OXT  O N N 393 
VAL H    H N N 394 
VAL H2   H N N 395 
VAL HA   H N N 396 
VAL HB   H N N 397 
VAL HG11 H N N 398 
VAL HG12 H N N 399 
VAL HG13 H N N 400 
VAL HG21 H N N 401 
VAL HG22 H N N 402 
VAL HG23 H N N 403 
VAL HXT  H N N 404 
# 
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 
LYS N   CA   sing N N 207 
LYS N   H    sing N N 208 
LYS N   H2   sing N N 209 
LYS CA  C    sing N N 210 
LYS CA  CB   sing N N 211 
LYS CA  HA   sing N N 212 
LYS C   O    doub N N 213 
LYS C   OXT  sing N N 214 
LYS CB  CG   sing N N 215 
LYS CB  HB2  sing N N 216 
LYS CB  HB3  sing N N 217 
LYS CG  CD   sing N N 218 
LYS CG  HG2  sing N N 219 
LYS CG  HG3  sing N N 220 
LYS CD  CE   sing N N 221 
LYS CD  HD2  sing N N 222 
LYS CD  HD3  sing N N 223 
LYS CE  NZ   sing N N 224 
LYS CE  HE2  sing N N 225 
LYS CE  HE3  sing N N 226 
LYS NZ  HZ1  sing N N 227 
LYS NZ  HZ2  sing N N 228 
LYS NZ  HZ3  sing N N 229 
LYS OXT HXT  sing N N 230 
MET N   CA   sing N N 231 
MET N   H    sing N N 232 
MET N   H2   sing N N 233 
MET CA  C    sing N N 234 
MET CA  CB   sing N N 235 
MET CA  HA   sing N N 236 
MET C   O    doub N N 237 
MET C   OXT  sing N N 238 
MET CB  CG   sing N N 239 
MET CB  HB2  sing N N 240 
MET CB  HB3  sing N N 241 
MET CG  SD   sing N N 242 
MET CG  HG2  sing N N 243 
MET CG  HG3  sing N N 244 
MET SD  CE   sing N N 245 
MET CE  HE1  sing N N 246 
MET CE  HE2  sing N N 247 
MET CE  HE3  sing N N 248 
MET OXT HXT  sing N N 249 
PHE N   CA   sing N N 250 
PHE N   H    sing N N 251 
PHE N   H2   sing N N 252 
PHE CA  C    sing N N 253 
PHE CA  CB   sing N N 254 
PHE CA  HA   sing N N 255 
PHE C   O    doub N N 256 
PHE C   OXT  sing N N 257 
PHE CB  CG   sing N N 258 
PHE CB  HB2  sing N N 259 
PHE CB  HB3  sing N N 260 
PHE CG  CD1  doub Y N 261 
PHE CG  CD2  sing Y N 262 
PHE CD1 CE1  sing Y N 263 
PHE CD1 HD1  sing N N 264 
PHE CD2 CE2  doub Y N 265 
PHE CD2 HD2  sing N N 266 
PHE CE1 CZ   doub Y N 267 
PHE CE1 HE1  sing N N 268 
PHE CE2 CZ   sing Y N 269 
PHE CE2 HE2  sing N N 270 
PHE CZ  HZ   sing N N 271 
PHE OXT HXT  sing N N 272 
PRO N   CA   sing N N 273 
PRO N   CD   sing N N 274 
PRO N   H    sing N N 275 
PRO CA  C    sing N N 276 
PRO CA  CB   sing N N 277 
PRO CA  HA   sing N N 278 
PRO C   O    doub N N 279 
PRO C   OXT  sing N N 280 
PRO CB  CG   sing N N 281 
PRO CB  HB2  sing N N 282 
PRO CB  HB3  sing N N 283 
PRO CG  CD   sing N N 284 
PRO CG  HG2  sing N N 285 
PRO CG  HG3  sing N N 286 
PRO CD  HD2  sing N N 287 
PRO CD  HD3  sing N N 288 
PRO OXT HXT  sing N N 289 
SER N   CA   sing N N 290 
SER N   H    sing N N 291 
SER N   H2   sing N N 292 
SER CA  C    sing N N 293 
SER CA  CB   sing N N 294 
SER CA  HA   sing N N 295 
SER C   O    doub N N 296 
SER C   OXT  sing N N 297 
SER CB  OG   sing N N 298 
SER CB  HB2  sing N N 299 
SER CB  HB3  sing N N 300 
SER OG  HG   sing N N 301 
SER OXT HXT  sing N N 302 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TRP N   CA   sing N N 319 
TRP N   H    sing N N 320 
TRP N   H2   sing N N 321 
TRP CA  C    sing N N 322 
TRP CA  CB   sing N N 323 
TRP CA  HA   sing N N 324 
TRP C   O    doub N N 325 
TRP C   OXT  sing N N 326 
TRP CB  CG   sing N N 327 
TRP CB  HB2  sing N N 328 
TRP CB  HB3  sing N N 329 
TRP CG  CD1  doub Y N 330 
TRP CG  CD2  sing Y N 331 
TRP CD1 NE1  sing Y N 332 
TRP CD1 HD1  sing N N 333 
TRP CD2 CE2  doub Y N 334 
TRP CD2 CE3  sing Y N 335 
TRP NE1 CE2  sing Y N 336 
TRP NE1 HE1  sing N N 337 
TRP CE2 CZ2  sing Y N 338 
TRP CE3 CZ3  doub Y N 339 
TRP CE3 HE3  sing N N 340 
TRP CZ2 CH2  doub Y N 341 
TRP CZ2 HZ2  sing N N 342 
TRP CZ3 CH2  sing Y N 343 
TRP CZ3 HZ3  sing N N 344 
TRP CH2 HH2  sing N N 345 
TRP OXT HXT  sing N N 346 
TYR N   CA   sing N N 347 
TYR N   H    sing N N 348 
TYR N   H2   sing N N 349 
TYR CA  C    sing N N 350 
TYR CA  CB   sing N N 351 
TYR CA  HA   sing N N 352 
TYR C   O    doub N N 353 
TYR C   OXT  sing N N 354 
TYR CB  CG   sing N N 355 
TYR CB  HB2  sing N N 356 
TYR CB  HB3  sing N N 357 
TYR CG  CD1  doub Y N 358 
TYR CG  CD2  sing Y N 359 
TYR CD1 CE1  sing Y N 360 
TYR CD1 HD1  sing N N 361 
TYR CD2 CE2  doub Y N 362 
TYR CD2 HD2  sing N N 363 
TYR CE1 CZ   doub Y N 364 
TYR CE1 HE1  sing N N 365 
TYR CE2 CZ   sing Y N 366 
TYR CE2 HE2  sing N N 367 
TYR CZ  OH   sing N N 368 
TYR OH  HH   sing N N 369 
TYR OXT HXT  sing N N 370 
VAL N   CA   sing N N 371 
VAL N   H    sing N N 372 
VAL N   H2   sing N N 373 
VAL CA  C    sing N N 374 
VAL CA  CB   sing N N 375 
VAL CA  HA   sing N N 376 
VAL C   O    doub N N 377 
VAL C   OXT  sing N N 378 
VAL CB  CG1  sing N N 379 
VAL CB  CG2  sing N N 380 
VAL CB  HB   sing N N 381 
VAL CG1 HG11 sing N N 382 
VAL CG1 HG12 sing N N 383 
VAL CG1 HG13 sing N N 384 
VAL CG2 HG21 sing N N 385 
VAL CG2 HG22 sing N N 386 
VAL CG2 HG23 sing N N 387 
VAL OXT HXT  sing N N 388 
# 
_pdbx_audit_support.funding_organization   'Ministry of Science and Technology (MoST, China)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           2021YFC2301500 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6KDC 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8Y9Q 
_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]   0.005565 
_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]   0.005565 
_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]   0.011232 
_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   . MET A 1 1   ? 28.442 35.050 -9.917  1.00 44.65 ? 1    MET A N   1 
ATOM   2    C CA  . MET A 1 1   ? 29.558 35.655 -9.194  1.00 31.73 ? 1    MET A CA  1 
ATOM   3    C C   . MET A 1 1   ? 30.671 34.616 -8.937  1.00 31.68 ? 1    MET A C   1 
ATOM   4    O O   . MET A 1 1   ? 30.390 33.464 -8.623  1.00 35.14 ? 1    MET A O   1 
ATOM   5    C CB  . MET A 1 1   ? 29.025 36.282 -7.905  1.00 34.38 ? 1    MET A CB  1 
ATOM   6    C CG  . MET A 1 1   ? 28.690 37.776 -8.091  1.00 33.33 ? 1    MET A CG  1 
ATOM   7    S SD  . MET A 1 1   ? 29.042 38.798 -6.646  1.00 57.97 ? 1    MET A SD  1 
ATOM   8    C CE  . MET A 1 1   ? 28.409 37.710 -5.370  1.00 51.13 ? 1    MET A CE  1 
ATOM   9    N N   . PHE A 1 2   ? 31.927 35.016 -9.153  1.00 24.15 ? 2    PHE A N   1 
ATOM   10   C CA  . PHE A 1 2   ? 33.057 34.158 -8.817  1.00 28.28 ? 2    PHE A CA  1 
ATOM   11   C C   . PHE A 1 2   ? 33.011 33.867 -7.320  1.00 34.31 ? 2    PHE A C   1 
ATOM   12   O O   . PHE A 1 2   ? 32.787 34.793 -6.529  1.00 32.72 ? 2    PHE A O   1 
ATOM   13   C CB  . PHE A 1 2   ? 34.389 34.833 -9.154  1.00 20.96 ? 2    PHE A CB  1 
ATOM   14   C CG  . PHE A 1 2   ? 34.714 34.901 -10.629 1.00 21.32 ? 2    PHE A CG  1 
ATOM   15   C CD1 . PHE A 1 2   ? 34.034 35.766 -11.470 1.00 21.98 ? 2    PHE A CD1 1 
ATOM   16   C CD2 . PHE A 1 2   ? 35.743 34.135 -11.160 1.00 18.74 ? 2    PHE A CD2 1 
ATOM   17   C CE1 . PHE A 1 2   ? 34.349 35.842 -12.824 1.00 19.87 ? 2    PHE A CE1 1 
ATOM   18   C CE2 . PHE A 1 2   ? 36.067 34.208 -12.510 1.00 18.54 ? 2    PHE A CE2 1 
ATOM   19   C CZ  . PHE A 1 2   ? 35.372 35.058 -13.343 1.00 16.98 ? 2    PHE A CZ  1 
ATOM   20   N N   . PRO A 1 3   ? 33.200 32.620 -6.892  1.00 33.59 ? 3    PRO A N   1 
ATOM   21   C CA  . PRO A 1 3   ? 33.266 32.342 -5.449  1.00 33.36 ? 3    PRO A CA  1 
ATOM   22   C C   . PRO A 1 3   ? 34.299 33.244 -4.791  1.00 31.44 ? 3    PRO A C   1 
ATOM   23   O O   . PRO A 1 3   ? 35.304 33.606 -5.402  1.00 33.65 ? 3    PRO A O   1 
ATOM   24   C CB  . PRO A 1 3   ? 33.679 30.868 -5.378  1.00 34.14 ? 3    PRO A CB  1 
ATOM   25   C CG  . PRO A 1 3   ? 33.542 30.303 -6.758  1.00 35.83 ? 3    PRO A CG  1 
ATOM   26   C CD  . PRO A 1 3   ? 33.239 31.409 -7.731  1.00 27.97 ? 3    PRO A CD  1 
ATOM   27   N N   . GLN A 1 4   ? 34.045 33.650 -3.543  1.00 42.19 ? 4    GLN A N   1 
ATOM   28   C CA  . GLN A 1 4   ? 35.045 34.525 -2.927  1.00 37.47 ? 4    GLN A CA  1 
ATOM   29   C C   . GLN A 1 4   ? 36.329 33.789 -2.561  1.00 28.04 ? 4    GLN A C   1 
ATOM   30   O O   . GLN A 1 4   ? 37.342 34.449 -2.293  1.00 33.93 ? 4    GLN A O   1 
ATOM   31   C CB  . GLN A 1 4   ? 34.532 35.217 -1.666  1.00 49.64 ? 4    GLN A CB  1 
ATOM   32   C CG  . GLN A 1 4   ? 35.300 36.524 -1.374  1.00 45.87 ? 4    GLN A CG  1 
ATOM   33   C CD  . GLN A 1 4   ? 34.481 37.795 -1.510  1.00 50.27 ? 4    GLN A CD  1 
ATOM   34   O OE1 . GLN A 1 4   ? 33.283 37.753 -1.757  1.00 57.49 ? 4    GLN A OE1 1 
ATOM   35   N NE2 . GLN A 1 4   ? 35.143 38.943 -1.364  1.00 52.45 ? 4    GLN A NE2 1 
ATOM   36   N N   . ASP A 1 5   ? 36.319 32.453 -2.542  1.00 29.79 ? 5    ASP A N   1 
ATOM   37   C CA  . ASP A 1 5   ? 37.565 31.704 -2.409  1.00 29.09 ? 5    ASP A CA  1 
ATOM   38   C C   . ASP A 1 5   ? 38.389 31.697 -3.695  1.00 24.75 ? 5    ASP A C   1 
ATOM   39   O O   . ASP A 1 5   ? 39.546 31.253 -3.667  1.00 16.59 ? 5    ASP A O   1 
ATOM   40   C CB  . ASP A 1 5   ? 37.274 30.259 -1.993  1.00 29.51 ? 5    ASP A CB  1 
ATOM   41   C CG  . ASP A 1 5   ? 36.682 30.155 -0.603  1.00 44.93 ? 5    ASP A CG  1 
ATOM   42   O OD1 . ASP A 1 5   ? 36.904 31.079 0.210   1.00 50.02 ? 5    ASP A OD1 1 
ATOM   43   O OD2 . ASP A 1 5   ? 35.991 29.148 -0.324  1.00 51.74 ? 5    ASP A OD2 1 
ATOM   44   N N   . PHE A 1 6   ? 37.823 32.157 -4.809  1.00 19.32 ? 6    PHE A N   1 
ATOM   45   C CA  . PHE A 1 6   ? 38.502 32.072 -6.100  1.00 18.45 ? 6    PHE A CA  1 
ATOM   46   C C   . PHE A 1 6   ? 39.761 32.928 -6.085  1.00 13.80 ? 6    PHE A C   1 
ATOM   47   O O   . PHE A 1 6   ? 39.782 34.011 -5.502  1.00 13.41 ? 6    PHE A O   1 
ATOM   48   C CB  . PHE A 1 6   ? 37.546 32.512 -7.214  1.00 15.59 ? 6    PHE A CB  1 
ATOM   49   C CG  . PHE A 1 6   ? 38.007 32.165 -8.615  1.00 16.94 ? 6    PHE A CG  1 
ATOM   50   C CD1 . PHE A 1 6   ? 37.688 30.937 -9.183  1.00 15.93 ? 6    PHE A CD1 1 
ATOM   51   C CD2 . PHE A 1 6   ? 38.700 33.101 -9.389  1.00 17.63 ? 6    PHE A CD2 1 
ATOM   52   C CE1 . PHE A 1 6   ? 38.091 30.629 -10.494 1.00 14.95 ? 6    PHE A CE1 1 
ATOM   53   C CE2 . PHE A 1 6   ? 39.100 32.807 -10.704 1.00 10.02 ? 6    PHE A CE2 1 
ATOM   54   C CZ  . PHE A 1 6   ? 38.792 31.571 -11.252 1.00 12.40 ? 6    PHE A CZ  1 
ATOM   55   N N   . LEU A 1 7   ? 40.830 32.421 -6.697  1.00 12.27 ? 7    LEU A N   1 
ATOM   56   C CA  . LEU A 1 7   ? 42.117 33.104 -6.696  1.00 12.50 ? 7    LEU A CA  1 
ATOM   57   C C   . LEU A 1 7   ? 42.248 33.901 -7.991  1.00 12.78 ? 7    LEU A C   1 
ATOM   58   O O   . LEU A 1 7   ? 42.094 33.342 -9.079  1.00 12.79 ? 7    LEU A O   1 
ATOM   59   C CB  . LEU A 1 7   ? 43.263 32.098 -6.552  1.00 11.87 ? 7    LEU A CB  1 
ATOM   60   C CG  . LEU A 1 7   ? 43.237 31.233 -5.283  1.00 15.48 ? 7    LEU A CG  1 
ATOM   61   C CD1 . LEU A 1 7   ? 44.516 30.442 -5.150  1.00 15.75 ? 7    LEU A CD1 1 
ATOM   62   C CD2 . LEU A 1 7   ? 43.014 32.077 -4.036  1.00 16.76 ? 7    LEU A CD2 1 
ATOM   63   N N   . PHE A 1 8   ? 42.467 35.208 -7.874  1.00 12.32 ? 8    PHE A N   1 
ATOM   64   C CA  . PHE A 1 8   ? 42.821 36.058 -9.011  1.00 12.88 ? 8    PHE A CA  1 
ATOM   65   C C   . PHE A 1 8   ? 44.261 36.506 -8.829  1.00 12.63 ? 8    PHE A C   1 
ATOM   66   O O   . PHE A 1 8   ? 44.609 37.046 -7.775  1.00 9.84  ? 8    PHE A O   1 
ATOM   67   C CB  . PHE A 1 8   ? 41.930 37.305 -9.121  1.00 12.12 ? 8    PHE A CB  1 
ATOM   68   C CG  . PHE A 1 8   ? 40.523 37.035 -9.586  1.00 13.77 ? 8    PHE A CG  1 
ATOM   69   C CD1 . PHE A 1 8   ? 40.262 36.717 -10.914 1.00 15.01 ? 8    PHE A CD1 1 
ATOM   70   C CD2 . PHE A 1 8   ? 39.456 37.159 -8.710  1.00 17.61 ? 8    PHE A CD2 1 
ATOM   71   C CE1 . PHE A 1 8   ? 38.956 36.493 -11.350 1.00 18.08 ? 8    PHE A CE1 1 
ATOM   72   C CE2 . PHE A 1 8   ? 38.157 36.940 -9.140  1.00 15.73 ? 8    PHE A CE2 1 
ATOM   73   C CZ  . PHE A 1 8   ? 37.911 36.611 -10.460 1.00 14.60 ? 8    PHE A CZ  1 
ATOM   74   N N   . GLY A 1 9   ? 45.090 36.313 -9.853  1.00 9.39  ? 9    GLY A N   1 
ATOM   75   C CA  . GLY A 1 9   ? 46.459 36.767 -9.718  1.00 9.11  ? 9    GLY A CA  1 
ATOM   76   C C   . GLY A 1 9   ? 47.283 36.762 -10.984 1.00 11.12 ? 9    GLY A C   1 
ATOM   77   O O   . GLY A 1 9   ? 46.748 36.927 -12.092 1.00 9.40  ? 9    GLY A O   1 
ATOM   78   N N   . VAL A 1 10  ? 48.601 36.595 -10.823 1.00 10.40 ? 10   VAL A N   1 
ATOM   79   C CA  . VAL A 1 10  ? 49.544 36.612 -11.937 1.00 10.31 ? 10   VAL A CA  1 
ATOM   80   C C   . VAL A 1 10  ? 50.564 35.498 -11.752 1.00 11.87 ? 10   VAL A C   1 
ATOM   81   O O   . VAL A 1 10  ? 50.692 34.898 -10.675 1.00 9.99  ? 10   VAL A O   1 
ATOM   82   C CB  . VAL A 1 10  ? 50.277 37.964 -12.072 1.00 9.68  ? 10   VAL A CB  1 
ATOM   83   C CG1 . VAL A 1 10  ? 49.297 39.058 -12.410 1.00 7.01  ? 10   VAL A CG1 1 
ATOM   84   C CG2 . VAL A 1 10  ? 51.059 38.286 -10.786 1.00 10.32 ? 10   VAL A CG2 1 
ATOM   85   N N   . ALA A 1 11  ? 51.311 35.254 -12.830 1.00 10.57 ? 11   ALA A N   1 
ATOM   86   C CA  . ALA A 1 11  ? 52.338 34.228 -12.915 1.00 10.45 ? 11   ALA A CA  1 
ATOM   87   C C   . ALA A 1 11  ? 53.644 34.863 -13.368 1.00 11.26 ? 11   ALA A C   1 
ATOM   88   O O   . ALA A 1 11  ? 53.651 35.796 -14.178 1.00 10.65 ? 11   ALA A O   1 
ATOM   89   C CB  . ALA A 1 11  ? 51.941 33.110 -13.909 1.00 9.03  ? 11   ALA A CB  1 
ATOM   90   N N   . MET A 1 12  ? 54.751 34.332 -12.846 1.00 8.20  ? 12   MET A N   1 
ATOM   91   C CA  . MET A 1 12  ? 56.098 34.805 -13.142 1.00 13.49 ? 12   MET A CA  1 
ATOM   92   C C   . MET A 1 12  ? 57.034 33.606 -13.167 1.00 10.65 ? 12   MET A C   1 
ATOM   93   O O   . MET A 1 12  ? 56.698 32.529 -12.680 1.00 10.20 ? 12   MET A O   1 
ATOM   94   C CB  . MET A 1 12  ? 56.568 35.841 -12.101 1.00 9.69  ? 12   MET A CB  1 
ATOM   95   C CG  . MET A 1 12  ? 55.675 37.100 -12.058 1.00 12.58 ? 12   MET A CG  1 
ATOM   96   S SD  . MET A 1 12  ? 56.360 38.349 -10.947 1.00 19.05 ? 12   MET A SD  1 
ATOM   97   C CE  . MET A 1 12  ? 56.532 37.331 -9.511  1.00 17.23 ? 12   MET A CE  1 
ATOM   98   N N   . SER A 1 13  ? 58.200 33.797 -13.769 1.00 8.69  ? 13   SER A N   1 
ATOM   99   C CA  . SER A 1 13  ? 59.304 32.844 -13.705 1.00 9.72  ? 13   SER A CA  1 
ATOM   100  C C   . SER A 1 13  ? 60.525 33.546 -13.125 1.00 13.67 ? 13   SER A C   1 
ATOM   101  O O   . SER A 1 13  ? 60.566 34.776 -13.023 1.00 10.47 ? 13   SER A O   1 
ATOM   102  C CB  . SER A 1 13  ? 59.638 32.293 -15.097 1.00 8.68  ? 13   SER A CB  1 
ATOM   103  O OG  . SER A 1 13  ? 60.210 33.329 -15.877 1.00 9.42  ? 13   SER A OG  1 
ATOM   104  N N   . GLY A 1 14  ? 61.549 32.761 -12.775 1.00 8.94  ? 14   GLY A N   1 
ATOM   105  C CA  . GLY A 1 14  ? 62.783 33.361 -12.299 1.00 9.62  ? 14   GLY A CA  1 
ATOM   106  C C   . GLY A 1 14  ? 63.586 34.025 -13.406 1.00 11.12 ? 14   GLY A C   1 
ATOM   107  O O   . GLY A 1 14  ? 63.908 35.218 -13.334 1.00 10.03 ? 14   GLY A O   1 
ATOM   108  N N   . PHE A 1 15  ? 63.917 33.265 -14.447 1.00 9.59  ? 15   PHE A N   1 
ATOM   109  C CA  . PHE A 1 15  ? 64.823 33.764 -15.477 1.00 9.41  ? 15   PHE A CA  1 
ATOM   110  C C   . PHE A 1 15  ? 64.286 35.015 -16.166 1.00 9.14  ? 15   PHE A C   1 
ATOM   111  O O   . PHE A 1 15  ? 65.060 35.905 -16.535 1.00 7.53  ? 15   PHE A O   1 
ATOM   112  C CB  . PHE A 1 15  ? 65.069 32.681 -16.521 1.00 7.65  ? 15   PHE A CB  1 
ATOM   113  C CG  . PHE A 1 15  ? 66.056 33.072 -17.570 1.00 8.90  ? 15   PHE A CG  1 
ATOM   114  C CD1 . PHE A 1 15  ? 67.416 33.084 -17.290 1.00 8.06  ? 15   PHE A CD1 1 
ATOM   115  C CD2 . PHE A 1 15  ? 65.629 33.436 -18.839 1.00 8.33  ? 15   PHE A CD2 1 
ATOM   116  C CE1 . PHE A 1 15  ? 68.349 33.434 -18.270 1.00 9.67  ? 15   PHE A CE1 1 
ATOM   117  C CE2 . PHE A 1 15  ? 66.550 33.793 -19.830 1.00 7.59  ? 15   PHE A CE2 1 
ATOM   118  C CZ  . PHE A 1 15  ? 67.912 33.797 -19.545 1.00 10.00 ? 15   PHE A CZ  1 
ATOM   119  N N   . GLN A 1 16  ? 62.974 35.095 -16.381 1.00 5.58  ? 16   GLN A N   1 
ATOM   120  C CA  . GLN A 1 16  ? 62.486 36.190 -17.218 1.00 7.85  ? 16   GLN A CA  1 
ATOM   121  C C   . GLN A 1 16  ? 62.319 37.494 -16.463 1.00 9.20  ? 16   GLN A C   1 
ATOM   122  O O   . GLN A 1 16  ? 62.075 38.517 -17.112 1.00 7.57  ? 16   GLN A O   1 
ATOM   123  C CB  . GLN A 1 16  ? 61.148 35.833 -17.873 1.00 6.88  ? 16   GLN A CB  1 
ATOM   124  C CG  . GLN A 1 16  ? 61.186 34.562 -18.705 1.00 7.80  ? 16   GLN A CG  1 
ATOM   125  C CD  . GLN A 1 16  ? 59.784 34.147 -19.129 1.00 7.61  ? 16   GLN A CD  1 
ATOM   126  O OE1 . GLN A 1 16  ? 59.093 33.405 -18.415 1.00 7.57  ? 16   GLN A OE1 1 
ATOM   127  N NE2 . GLN A 1 16  ? 59.345 34.643 -20.283 1.00 7.04  ? 16   GLN A NE2 1 
ATOM   128  N N   . PHE A 1 17  ? 62.459 37.483 -15.132 1.00 6.99  ? 17   PHE A N   1 
ATOM   129  C CA  . PHE A 1 17  ? 62.055 38.595 -14.280 1.00 9.90  ? 17   PHE A CA  1 
ATOM   130  C C   . PHE A 1 17  ? 63.161 39.058 -13.335 1.00 9.45  ? 17   PHE A C   1 
ATOM   131  O O   . PHE A 1 17  ? 63.204 40.244 -12.996 1.00 9.77  ? 17   PHE A O   1 
ATOM   132  C CB  . PHE A 1 17  ? 60.833 38.214 -13.423 1.00 7.56  ? 17   PHE A CB  1 
ATOM   133  C CG  . PHE A 1 17  ? 59.549 38.063 -14.197 1.00 10.34 ? 17   PHE A CG  1 
ATOM   134  C CD1 . PHE A 1 17  ? 59.305 36.913 -14.949 1.00 6.54  ? 17   PHE A CD1 1 
ATOM   135  C CD2 . PHE A 1 17  ? 58.574 39.049 -14.137 1.00 7.18  ? 17   PHE A CD2 1 
ATOM   136  C CE1 . PHE A 1 17  ? 58.115 36.748 -15.659 1.00 8.01  ? 17   PHE A CE1 1 
ATOM   137  C CE2 . PHE A 1 17  ? 57.378 38.908 -14.836 1.00 7.43  ? 17   PHE A CE2 1 
ATOM   138  C CZ  . PHE A 1 17  ? 57.143 37.741 -15.599 1.00 8.74  ? 17   PHE A CZ  1 
ATOM   139  N N   . GLU A 1 18  ? 64.030 38.143 -12.860 1.00 8.23  ? 18   GLU A N   1 
ATOM   140  C CA  . GLU A 1 18  ? 64.818 38.437 -11.653 1.00 10.00 ? 18   GLU A CA  1 
ATOM   141  C C   . GLU A 1 18  ? 65.939 39.427 -11.921 1.00 11.23 ? 18   GLU A C   1 
ATOM   142  O O   . GLU A 1 18  ? 66.229 40.285 -11.087 1.00 9.64  ? 18   GLU A O   1 
ATOM   143  C CB  . GLU A 1 18  ? 65.413 37.147 -11.051 1.00 9.29  ? 18   GLU A CB  1 
ATOM   144  C CG  . GLU A 1 18  ? 64.393 36.282 -10.295 1.00 9.60  ? 18   GLU A CG  1 
ATOM   145  C CD  . GLU A 1 18  ? 64.881 34.862 -9.973  1.00 12.65 ? 18   GLU A CD  1 
ATOM   146  O OE1 . GLU A 1 18  ? 65.852 34.398 -10.599 1.00 12.08 ? 18   GLU A OE1 1 
ATOM   147  O OE2 . GLU A 1 18  ? 64.293 34.204 -9.091  1.00 11.53 ? 18   GLU A OE2 1 
ATOM   148  N N   . MET A 1 19  ? 66.588 39.309 -13.056 1.00 8.74  ? 19   MET A N   1 
ATOM   149  C CA  . MET A 1 19  ? 67.894 39.881 -13.291 1.00 12.54 ? 19   MET A CA  1 
ATOM   150  C C   . MET A 1 19  ? 67.700 41.351 -13.694 1.00 13.84 ? 19   MET A C   1 
ATOM   151  O O   . MET A 1 19  ? 66.587 41.785 -14.047 1.00 10.60 ? 19   MET A O   1 
ATOM   152  C CB  . MET A 1 19  ? 68.524 39.005 -14.369 1.00 11.43 ? 19   MET A CB  1 
ATOM   153  C CG  . MET A 1 19  ? 69.415 37.858 -13.809 1.00 10.23 ? 19   MET A CG  1 
ATOM   154  S SD  . MET A 1 19  ? 70.667 37.252 -14.898 1.00 13.15 ? 19   MET A SD  1 
ATOM   155  C CE  . MET A 1 19  ? 69.799 35.713 -15.325 1.00 10.33 ? 19   MET A CE  1 
ATOM   156  N N   . GLY A 1 20  ? 68.760 42.132 -13.602 1.00 13.17 ? 20   GLY A N   1 
ATOM   157  C CA  . GLY A 1 20  ? 68.619 43.548 -13.915 1.00 10.26 ? 20   GLY A CA  1 
ATOM   158  C C   . GLY A 1 20  ? 69.593 44.435 -13.162 1.00 14.91 ? 20   GLY A C   1 
ATOM   159  O O   . GLY A 1 20  ? 69.963 45.508 -13.646 1.00 14.31 ? 20   GLY A O   1 
ATOM   160  N N   . LYS A 1 21  ? 70.005 44.013 -11.968 1.00 15.61 ? 21   LYS A N   1 
ATOM   161  C CA  . LYS A 1 21  ? 71.145 44.624 -11.297 1.00 17.26 ? 21   LYS A CA  1 
ATOM   162  C C   . LYS A 1 21  ? 72.225 43.586 -11.036 1.00 18.34 ? 21   LYS A C   1 
ATOM   163  O O   . LYS A 1 21  ? 71.955 42.390 -10.907 1.00 15.20 ? 21   LYS A O   1 
ATOM   164  C CB  . LYS A 1 21  ? 70.814 45.289 -9.948  1.00 18.41 ? 21   LYS A CB  1 
ATOM   165  C CG  . LYS A 1 21  ? 69.883 46.485 -9.940  1.00 20.75 ? 21   LYS A CG  1 
ATOM   166  C CD  . LYS A 1 21  ? 69.115 46.459 -8.635  1.00 31.45 ? 21   LYS A CD  1 
ATOM   167  C CE  . LYS A 1 21  ? 68.522 47.812 -8.260  1.00 38.46 ? 21   LYS A CE  1 
ATOM   168  N NZ  . LYS A 1 21  ? 67.249 47.641 -7.431  1.00 27.17 ? 21   LYS A NZ  1 
ATOM   169  N N   . GLU A 1 22  ? 73.455 44.086 -10.891 1.00 18.41 ? 22   GLU A N   1 
ATOM   170  C CA  . GLU A 1 22  ? 74.625 43.219 -10.877 1.00 19.86 ? 22   GLU A CA  1 
ATOM   171  C C   . GLU A 1 22  ? 74.571 42.203 -9.740  1.00 19.92 ? 22   GLU A C   1 
ATOM   172  O O   . GLU A 1 22  ? 75.001 41.062 -9.920  1.00 17.88 ? 22   GLU A O   1 
ATOM   173  C CB  . GLU A 1 22  ? 75.895 44.074 -10.799 1.00 23.51 ? 22   GLU A CB  1 
ATOM   174  C CG  . GLU A 1 22  ? 77.199 43.291 -10.677 1.00 29.36 ? 22   GLU A CG  1 
ATOM   175  C CD  . GLU A 1 22  ? 77.450 42.383 -11.880 1.00 46.76 ? 22   GLU A CD  1 
ATOM   176  O OE1 . GLU A 1 22  ? 77.923 41.238 -11.677 1.00 47.83 ? 22   GLU A OE1 1 
ATOM   177  O OE2 . GLU A 1 22  ? 77.151 42.808 -13.024 1.00 37.96 ? 22   GLU A OE2 1 
ATOM   178  N N   . ASN A 1 23  ? 74.001 42.568 -8.584  1.00 17.44 ? 23   ASN A N   1 
ATOM   179  C CA  . ASN A 1 23  ? 73.970 41.642 -7.453  1.00 18.23 ? 23   ASN A CA  1 
ATOM   180  C C   . ASN A 1 23  ? 73.111 40.405 -7.698  1.00 16.26 ? 23   ASN A C   1 
ATOM   181  O O   . ASN A 1 23  ? 73.231 39.441 -6.940  1.00 19.87 ? 23   ASN A O   1 
ATOM   182  C CB  . ASN A 1 23  ? 73.504 42.360 -6.174  1.00 20.34 ? 23   ASN A CB  1 
ATOM   183  C CG  . ASN A 1 23  ? 71.987 42.555 -6.109  1.00 20.36 ? 23   ASN A CG  1 
ATOM   184  O OD1 . ASN A 1 23  ? 71.335 42.804 -7.122  1.00 19.57 ? 23   ASN A OD1 1 
ATOM   185  N ND2 . ASN A 1 23  ? 71.427 42.458 -4.903  1.00 21.18 ? 23   ASN A ND2 1 
ATOM   186  N N   . SER A 1 24  ? 72.269 40.384 -8.731  1.00 14.98 ? 24   SER A N   1 
ATOM   187  C CA  . SER A 1 24  ? 71.448 39.211 -9.009  1.00 15.18 ? 24   SER A CA  1 
ATOM   188  C C   . SER A 1 24  ? 71.913 38.406 -10.217 1.00 18.19 ? 24   SER A C   1 
ATOM   189  O O   . SER A 1 24  ? 71.280 37.392 -10.552 1.00 17.74 ? 24   SER A O   1 
ATOM   190  C CB  . SER A 1 24  ? 69.992 39.628 -9.225  1.00 16.91 ? 24   SER A CB  1 
ATOM   191  O OG  . SER A 1 24  ? 69.862 40.331 -10.443 1.00 13.21 ? 24   SER A OG  1 
ATOM   192  N N   . LYS A 1 25  ? 72.976 38.828 -10.892 1.00 15.49 ? 25   LYS A N   1 
ATOM   193  C CA  . LYS A 1 25  ? 73.366 38.185 -12.140 1.00 17.48 ? 25   LYS A CA  1 
ATOM   194  C C   . LYS A 1 25  ? 73.571 36.690 -11.926 1.00 16.76 ? 25   LYS A C   1 
ATOM   195  O O   . LYS A 1 25  ? 74.289 36.275 -11.012 1.00 15.32 ? 25   LYS A O   1 
ATOM   196  C CB  . LYS A 1 25  ? 74.646 38.818 -12.684 1.00 18.60 ? 25   LYS A CB  1 
ATOM   197  C CG  . LYS A 1 25  ? 75.073 38.244 -14.030 1.00 23.83 ? 25   LYS A CG  1 
ATOM   198  C CD  . LYS A 1 25  ? 75.402 39.328 -15.043 1.00 32.07 ? 25   LYS A CD  1 
ATOM   199  C CE  . LYS A 1 25  ? 76.821 39.837 -14.837 1.00 39.53 ? 25   LYS A CE  1 
ATOM   200  N NZ  . LYS A 1 25  ? 77.465 40.254 -16.117 1.00 44.77 ? 25   LYS A NZ  1 
ATOM   201  N N   . ASP A 1 26  ? 72.905 35.884 -12.751 1.00 11.87 ? 26   ASP A N   1 
ATOM   202  C CA  . ASP A 1 26  ? 73.014 34.424 -12.702 1.00 14.19 ? 26   ASP A CA  1 
ATOM   203  C C   . ASP A 1 26  ? 73.465 33.961 -14.083 1.00 12.59 ? 26   ASP A C   1 
ATOM   204  O O   . ASP A 1 26  ? 72.643 33.802 -14.991 1.00 14.05 ? 26   ASP A O   1 
ATOM   205  C CB  . ASP A 1 26  ? 71.681 33.777 -12.290 1.00 11.91 ? 26   ASP A CB  1 
ATOM   206  C CG  . ASP A 1 26  ? 71.726 32.241 -12.306 1.00 11.95 ? 26   ASP A CG  1 
ATOM   207  O OD1 . ASP A 1 26  ? 72.837 31.670 -12.310 1.00 12.42 ? 26   ASP A OD1 1 
ATOM   208  O OD2 . ASP A 1 26  ? 70.645 31.591 -12.309 1.00 13.18 ? 26   ASP A OD2 1 
ATOM   209  N N   . GLU A 1 27  ? 74.768 33.738 -14.249 1.00 12.09 ? 27   GLU A N   1 
ATOM   210  C CA  . GLU A 1 27  ? 75.290 33.236 -15.517 1.00 15.39 ? 27   GLU A CA  1 
ATOM   211  C C   . GLU A 1 27  ? 75.202 31.720 -15.625 1.00 17.39 ? 27   GLU A C   1 
ATOM   212  O O   . GLU A 1 27  ? 75.655 31.159 -16.624 1.00 15.25 ? 27   GLU A O   1 
ATOM   213  C CB  . GLU A 1 27  ? 76.752 33.678 -15.701 1.00 16.59 ? 27   GLU A CB  1 
ATOM   214  C CG  . GLU A 1 27  ? 77.006 35.153 -15.405 1.00 21.09 ? 27   GLU A CG  1 
ATOM   215  C CD  . GLU A 1 27  ? 78.357 35.651 -15.926 1.00 29.73 ? 27   GLU A CD  1 
ATOM   216  O OE1 . GLU A 1 27  ? 79.179 34.837 -16.389 1.00 32.83 ? 27   GLU A OE1 1 
ATOM   217  O OE2 . GLU A 1 27  ? 78.602 36.866 -15.855 1.00 32.79 ? 27   GLU A OE2 1 
ATOM   218  N N   . ASN A 1 28  ? 74.617 31.050 -14.636 1.00 13.09 ? 28   ASN A N   1 
ATOM   219  C CA  . ASN A 1 28  ? 74.766 29.607 -14.448 1.00 11.89 ? 28   ASN A CA  1 
ATOM   220  C C   . ASN A 1 28  ? 73.587 28.811 -15.017 1.00 10.49 ? 28   ASN A C   1 
ATOM   221  O O   . ASN A 1 28  ? 73.198 27.802 -14.427 1.00 9.59  ? 28   ASN A O   1 
ATOM   222  C CB  . ASN A 1 28  ? 74.942 29.322 -12.949 1.00 13.66 ? 28   ASN A CB  1 
ATOM   223  C CG  . ASN A 1 28  ? 75.421 27.894 -12.651 1.00 17.97 ? 28   ASN A CG  1 
ATOM   224  O OD1 . ASN A 1 28  ? 76.264 27.346 -13.362 1.00 16.54 ? 28   ASN A OD1 1 
ATOM   225  N ND2 . ASN A 1 28  ? 74.868 27.288 -11.599 1.00 14.68 ? 28   ASN A ND2 1 
ATOM   226  N N   . THR A 1 29  ? 72.978 29.217 -16.142 1.00 11.00 ? 29   THR A N   1 
ATOM   227  C CA  . THR A 1 29  ? 71.918 28.424 -16.756 1.00 11.38 ? 29   THR A CA  1 
ATOM   228  C C   . THR A 1 29  ? 72.216 28.137 -18.218 1.00 7.75  ? 29   THR A C   1 
ATOM   229  O O   . THR A 1 29  ? 72.968 28.858 -18.880 1.00 8.58  ? 29   THR A O   1 
ATOM   230  C CB  . THR A 1 29  ? 70.536 29.094 -16.720 1.00 10.25 ? 29   THR A CB  1 
ATOM   231  O OG1 . THR A 1 29  ? 70.575 30.310 -17.482 1.00 7.66  ? 29   THR A OG1 1 
ATOM   232  C CG2 . THR A 1 29  ? 70.108 29.393 -15.297 1.00 12.20 ? 29   THR A CG2 1 
ATOM   233  N N   . ASP A 1 30  ? 71.556 27.092 -18.730 1.00 7.54  ? 30   ASP A N   1 
ATOM   234  C CA  . ASP A 1 30  ? 71.572 26.854 -20.170 1.00 8.58  ? 30   ASP A CA  1 
ATOM   235  C C   . ASP A 1 30  ? 71.059 28.069 -20.944 1.00 10.63 ? 30   ASP A C   1 
ATOM   236  O O   . ASP A 1 30  ? 71.656 28.469 -21.955 1.00 8.17  ? 30   ASP A O   1 
ATOM   237  C CB  . ASP A 1 30  ? 70.773 25.591 -20.534 1.00 5.54  ? 30   ASP A CB  1 
ATOM   238  C CG  . ASP A 1 30  ? 69.360 25.543 -19.950 1.00 10.30 ? 30   ASP A CG  1 
ATOM   239  O OD1 . ASP A 1 30  ? 68.877 26.502 -19.312 1.00 10.91 ? 30   ASP A OD1 1 
ATOM   240  O OD2 . ASP A 1 30  ? 68.705 24.497 -20.162 1.00 10.26 ? 30   ASP A OD2 1 
ATOM   241  N N   . TRP A 1 31  ? 69.981 28.698 -20.461 1.00 8.65  ? 31   TRP A N   1 
ATOM   242  C CA  . TRP A 1 31  ? 69.381 29.807 -21.202 1.00 9.43  ? 31   TRP A CA  1 
ATOM   243  C C   . TRP A 1 31  ? 70.279 31.040 -21.216 1.00 8.36  ? 31   TRP A C   1 
ATOM   244  O O   . TRP A 1 31  ? 70.294 31.779 -22.209 1.00 7.38  ? 31   TRP A O   1 
ATOM   245  C CB  . TRP A 1 31  ? 67.999 30.134 -20.619 1.00 8.29  ? 31   TRP A CB  1 
ATOM   246  C CG  . TRP A 1 31  ? 66.910 29.537 -21.462 1.00 7.33  ? 31   TRP A CG  1 
ATOM   247  C CD1 . TRP A 1 31  ? 66.298 28.323 -21.283 1.00 9.31  ? 31   TRP A CD1 1 
ATOM   248  C CD2 . TRP A 1 31  ? 66.340 30.105 -22.644 1.00 6.86  ? 31   TRP A CD2 1 
ATOM   249  N NE1 . TRP A 1 31  ? 65.360 28.119 -22.272 1.00 8.47  ? 31   TRP A NE1 1 
ATOM   250  C CE2 . TRP A 1 31  ? 65.371 29.201 -23.119 1.00 8.45  ? 31   TRP A CE2 1 
ATOM   251  C CE3 . TRP A 1 31  ? 66.555 31.298 -23.349 1.00 8.64  ? 31   TRP A CE3 1 
ATOM   252  C CZ2 . TRP A 1 31  ? 64.616 29.450 -24.274 1.00 7.91  ? 31   TRP A CZ2 1 
ATOM   253  C CZ3 . TRP A 1 31  ? 65.801 31.543 -24.490 1.00 7.49  ? 31   TRP A CZ3 1 
ATOM   254  C CH2 . TRP A 1 31  ? 64.854 30.618 -24.946 1.00 7.30  ? 31   TRP A CH2 1 
ATOM   255  N N   . TYR A 1 32  ? 71.039 31.279 -20.142 1.00 8.54  ? 32   TYR A N   1 
ATOM   256  C CA  . TYR A 1 32  ? 71.955 32.419 -20.134 1.00 8.60  ? 32   TYR A CA  1 
ATOM   257  C C   . TYR A 1 32  ? 73.004 32.280 -21.234 1.00 7.91  ? 32   TYR A C   1 
ATOM   258  O O   . TYR A 1 32  ? 73.208 33.197 -22.040 1.00 8.13  ? 32   TYR A O   1 
ATOM   259  C CB  . TYR A 1 32  ? 72.626 32.558 -18.763 1.00 9.84  ? 32   TYR A CB  1 
ATOM   260  C CG  . TYR A 1 32  ? 73.410 33.855 -18.627 1.00 13.37 ? 32   TYR A CG  1 
ATOM   261  C CD1 . TYR A 1 32  ? 74.732 33.950 -19.068 1.00 14.30 ? 32   TYR A CD1 1 
ATOM   262  C CD2 . TYR A 1 32  ? 72.813 34.993 -18.095 1.00 14.00 ? 32   TYR A CD2 1 
ATOM   263  C CE1 . TYR A 1 32  ? 75.441 35.144 -18.961 1.00 14.92 ? 32   TYR A CE1 1 
ATOM   264  C CE2 . TYR A 1 32  ? 73.506 36.183 -17.983 1.00 14.15 ? 32   TYR A CE2 1 
ATOM   265  C CZ  . TYR A 1 32  ? 74.821 36.250 -18.411 1.00 17.91 ? 32   TYR A CZ  1 
ATOM   266  O OH  . TYR A 1 32  ? 75.498 37.440 -18.294 1.00 25.99 ? 32   TYR A OH  1 
ATOM   267  N N   . ILE A 1 33  ? 73.675 31.126 -21.293 1.00 8.42  ? 33   ILE A N   1 
ATOM   268  C CA  . ILE A 1 33  ? 74.690 30.958 -22.323 1.00 10.05 ? 33   ILE A CA  1 
ATOM   269  C C   . ILE A 1 33  ? 74.056 30.846 -23.712 1.00 8.39  ? 33   ILE A C   1 
ATOM   270  O O   . ILE A 1 33  ? 74.625 31.345 -24.694 1.00 9.55  ? 33   ILE A O   1 
ATOM   271  C CB  . ILE A 1 33  ? 75.631 29.792 -21.934 1.00 11.84 ? 33   ILE A CB  1 
ATOM   272  C CG1 . ILE A 1 33  ? 75.013 28.420 -22.159 1.00 16.53 ? 33   ILE A CG1 1 
ATOM   273  C CG2 . ILE A 1 33  ? 76.162 29.952 -20.499 1.00 17.27 ? 33   ILE A CG2 1 
ATOM   274  C CD1 . ILE A 1 33  ? 75.215 27.920 -23.518 1.00 23.80 ? 33   ILE A CD1 1 
ATOM   275  N N   . TRP A 1 34  ? 72.844 30.286 -23.808 1.00 8.90  ? 34   TRP A N   1 
ATOM   276  C CA  . TRP A 1 34  ? 72.136 30.202 -25.087 1.00 9.86  ? 34   TRP A CA  1 
ATOM   277  C C   . TRP A 1 34  ? 71.870 31.588 -25.680 1.00 8.80  ? 34   TRP A C   1 
ATOM   278  O O   . TRP A 1 34  ? 72.085 31.817 -26.876 1.00 7.32  ? 34   TRP A O   1 
ATOM   279  C CB  . TRP A 1 34  ? 70.821 29.444 -24.882 1.00 8.37  ? 34   TRP A CB  1 
ATOM   280  C CG  . TRP A 1 34  ? 70.023 29.147 -26.128 1.00 10.72 ? 34   TRP A CG  1 
ATOM   281  C CD1 . TRP A 1 34  ? 68.807 29.668 -26.465 1.00 7.97  ? 34   TRP A CD1 1 
ATOM   282  C CD2 . TRP A 1 34  ? 70.363 28.215 -27.168 1.00 10.63 ? 34   TRP A CD2 1 
ATOM   283  N NE1 . TRP A 1 34  ? 68.375 29.128 -27.659 1.00 7.70  ? 34   TRP A NE1 1 
ATOM   284  C CE2 . TRP A 1 34  ? 69.314 28.238 -28.110 1.00 10.30 ? 34   TRP A CE2 1 
ATOM   285  C CE3 . TRP A 1 34  ? 71.460 27.370 -27.398 1.00 9.12  ? 34   TRP A CE3 1 
ATOM   286  C CZ2 . TRP A 1 34  ? 69.324 27.448 -29.262 1.00 11.72 ? 34   TRP A CZ2 1 
ATOM   287  C CZ3 . TRP A 1 34  ? 71.468 26.590 -28.545 1.00 10.58 ? 34   TRP A CZ3 1 
ATOM   288  C CH2 . TRP A 1 34  ? 70.407 26.637 -29.463 1.00 12.08 ? 34   TRP A CH2 1 
ATOM   289  N N   . THR A 1 35  ? 71.414 32.534 -24.856 1.00 7.95  ? 35   THR A N   1 
ATOM   290  C CA  . THR A 1 35  ? 71.090 33.866 -25.365 1.00 6.81  ? 35   THR A CA  1 
ATOM   291  C C   . THR A 1 35  ? 72.306 34.782 -25.509 1.00 8.75  ? 35   THR A C   1 
ATOM   292  O O   . THR A 1 35  ? 72.220 35.794 -26.217 1.00 11.19 ? 35   THR A O   1 
ATOM   293  C CB  . THR A 1 35  ? 70.045 34.546 -24.476 1.00 9.02  ? 35   THR A CB  1 
ATOM   294  O OG1 . THR A 1 35  ? 70.508 34.581 -23.117 1.00 8.85  ? 35   THR A OG1 1 
ATOM   295  C CG2 . THR A 1 35  ? 68.733 33.792 -24.546 1.00 9.62  ? 35   THR A CG2 1 
ATOM   296  N N   . HIS A 1 36  ? 73.435 34.461 -24.886 1.00 7.34  ? 36   HIS A N   1 
ATOM   297  C CA  . HIS A 1 36  ? 74.640 35.257 -25.074 1.00 10.83 ? 36   HIS A CA  1 
ATOM   298  C C   . HIS A 1 36  ? 75.498 34.757 -26.226 1.00 11.51 ? 36   HIS A C   1 
ATOM   299  O O   . HIS A 1 36  ? 76.517 35.382 -26.532 1.00 14.44 ? 36   HIS A O   1 
ATOM   300  C CB  . HIS A 1 36  ? 75.454 35.296 -23.772 1.00 13.74 ? 36   HIS A CB  1 
ATOM   301  C CG  . HIS A 1 36  ? 74.885 36.252 -22.767 1.00 13.91 ? 36   HIS A CG  1 
ATOM   302  N ND1 . HIS A 1 36  ? 73.730 35.983 -22.065 1.00 12.01 ? 36   HIS A ND1 1 
ATOM   303  C CD2 . HIS A 1 36  ? 75.259 37.503 -22.409 1.00 15.80 ? 36   HIS A CD2 1 
ATOM   304  C CE1 . HIS A 1 36  ? 73.437 37.010 -21.285 1.00 12.27 ? 36   HIS A CE1 1 
ATOM   305  N NE2 . HIS A 1 36  ? 74.351 37.944 -21.472 1.00 13.69 ? 36   HIS A NE2 1 
ATOM   306  N N   . ASP A 1 37  ? 75.092 33.676 -26.892 1.00 9.79  ? 37   ASP A N   1 
ATOM   307  C CA  . ASP A 1 37  ? 75.900 33.087 -27.951 1.00 9.55  ? 37   ASP A CA  1 
ATOM   308  C C   . ASP A 1 37  ? 75.797 33.951 -29.207 1.00 9.02  ? 37   ASP A C   1 
ATOM   309  O O   . ASP A 1 37  ? 74.700 34.148 -29.749 1.00 9.01  ? 37   ASP A O   1 
ATOM   310  C CB  . ASP A 1 37  ? 75.447 31.654 -28.218 1.00 9.63  ? 37   ASP A CB  1 
ATOM   311  C CG  . ASP A 1 37  ? 76.263 30.981 -29.300 1.00 13.45 ? 37   ASP A CG  1 
ATOM   312  O OD1 . ASP A 1 37  ? 77.373 30.497 -28.983 1.00 14.02 ? 37   ASP A OD1 1 
ATOM   313  O OD2 . ASP A 1 37  ? 75.793 30.945 -30.462 1.00 12.79 ? 37   ASP A OD2 1 
ATOM   314  N N   . LEU A 1 38  ? 76.939 34.469 -29.667 1.00 10.12 ? 38   LEU A N   1 
ATOM   315  C CA  . LEU A 1 38  ? 76.936 35.411 -30.790 1.00 11.07 ? 38   LEU A CA  1 
ATOM   316  C C   . LEU A 1 38  ? 76.519 34.748 -32.098 1.00 11.11 ? 38   LEU A C   1 
ATOM   317  O O   . LEU A 1 38  ? 75.938 35.408 -32.971 1.00 9.83  ? 38   LEU A O   1 
ATOM   318  C CB  . LEU A 1 38  ? 78.319 36.040 -30.957 1.00 10.31 ? 38   LEU A CB  1 
ATOM   319  C CG  . LEU A 1 38  ? 78.771 36.954 -29.815 1.00 19.69 ? 38   LEU A CG  1 
ATOM   320  C CD1 . LEU A 1 38  ? 80.169 37.502 -30.073 1.00 19.13 ? 38   LEU A CD1 1 
ATOM   321  C CD2 . LEU A 1 38  ? 77.757 38.072 -29.583 1.00 18.04 ? 38   LEU A CD2 1 
ATOM   322  N N   . GLN A 1 39  ? 76.834 33.464 -32.278 1.00 9.27  ? 39   GLN A N   1 
ATOM   323  C CA  . GLN A 1 39  ? 76.422 32.802 -33.509 1.00 10.28 ? 39   GLN A CA  1 
ATOM   324  C C   . GLN A 1 39  ? 74.906 32.643 -33.556 1.00 9.15  ? 39   GLN A C   1 
ATOM   325  O O   . GLN A 1 39  ? 74.290 32.897 -34.595 1.00 8.07  ? 39   GLN A O   1 
ATOM   326  C CB  . GLN A 1 39  ? 77.146 31.464 -33.653 1.00 9.60  ? 39   GLN A CB  1 
ATOM   327  C CG  . GLN A 1 39  ? 78.665 31.636 -33.758 1.00 11.39 ? 39   GLN A CG  1 
ATOM   328  C CD  . GLN A 1 39  ? 79.390 30.377 -34.163 1.00 12.02 ? 39   GLN A CD  1 
ATOM   329  O OE1 . GLN A 1 39  ? 79.045 29.742 -35.156 1.00 10.42 ? 39   GLN A OE1 1 
ATOM   330  N NE2 . GLN A 1 39  ? 80.421 30.014 -33.400 1.00 11.38 ? 39   GLN A NE2 1 
ATOM   331  N N   . ASN A 1 40  ? 74.288 32.254 -32.431 1.00 8.55  ? 40   ASN A N   1 
ATOM   332  C CA  . ASN A 1 40  ? 72.826 32.242 -32.346 1.00 10.07 ? 40   ASN A CA  1 
ATOM   333  C C   . ASN A 1 40  ? 72.251 33.608 -32.692 1.00 11.29 ? 40   ASN A C   1 
ATOM   334  O O   . ASN A 1 40  ? 71.281 33.711 -33.457 1.00 8.92  ? 40   ASN A O   1 
ATOM   335  C CB  . ASN A 1 40  ? 72.370 31.837 -30.941 1.00 8.97  ? 40   ASN A CB  1 
ATOM   336  C CG  . ASN A 1 40  ? 72.378 30.337 -30.722 1.00 12.79 ? 40   ASN A CG  1 
ATOM   337  O OD1 . ASN A 1 40  ? 72.482 29.559 -31.672 1.00 10.79 ? 40   ASN A OD1 1 
ATOM   338  N ND2 . ASN A 1 40  ? 72.234 29.917 -29.452 1.00 9.97  ? 40   ASN A ND2 1 
ATOM   339  N N   . GLN A 1 41  ? 72.852 34.675 -32.150 1.00 8.75  ? 41   GLN A N   1 
ATOM   340  C CA  . GLN A 1 41  ? 72.339 36.022 -32.405 1.00 9.43  ? 41   GLN A CA  1 
ATOM   341  C C   . GLN A 1 41  ? 72.456 36.388 -33.877 1.00 11.63 ? 41   GLN A C   1 
ATOM   342  O O   . GLN A 1 41  ? 71.517 36.945 -34.460 1.00 9.21  ? 41   GLN A O   1 
ATOM   343  C CB  . GLN A 1 41  ? 73.087 37.039 -31.536 1.00 9.61  ? 41   GLN A CB  1 
ATOM   344  C CG  . GLN A 1 41  ? 72.746 36.915 -30.042 1.00 9.99  ? 41   GLN A CG  1 
ATOM   345  C CD  . GLN A 1 41  ? 73.566 37.853 -29.177 1.00 14.75 ? 41   GLN A CD  1 
ATOM   346  O OE1 . GLN A 1 41  ? 74.254 38.736 -29.687 1.00 13.72 ? 41   GLN A OE1 1 
ATOM   347  N NE2 . GLN A 1 41  ? 73.506 37.659 -27.865 1.00 9.77  ? 41   GLN A NE2 1 
ATOM   348  N N   . ALA A 1 42  ? 73.601 36.073 -34.496 1.00 10.02 ? 42   ALA A N   1 
ATOM   349  C CA  . ALA A 1 42  ? 73.801 36.412 -35.901 1.00 12.89 ? 42   ALA A CA  1 
ATOM   350  C C   . ALA A 1 42  ? 72.840 35.655 -36.808 1.00 14.63 ? 42   ALA A C   1 
ATOM   351  O O   . ALA A 1 42  ? 72.499 36.143 -37.894 1.00 13.65 ? 42   ALA A O   1 
ATOM   352  C CB  . ALA A 1 42  ? 75.249 36.135 -36.305 1.00 11.27 ? 42   ALA A CB  1 
ATOM   353  N N   . ASN A 1 43  ? 72.370 34.488 -36.380 1.00 12.09 ? 43   ASN A N   1 
ATOM   354  C CA  . ASN A 1 43  ? 71.413 33.716 -37.158 1.00 11.36 ? 43   ASN A CA  1 
ATOM   355  C C   . ASN A 1 43  ? 69.968 34.072 -36.827 1.00 12.90 ? 43   ASN A C   1 
ATOM   356  O O   . ASN A 1 43  ? 69.047 33.470 -37.393 1.00 12.40 ? 43   ASN A O   1 
ATOM   357  C CB  . ASN A 1 43  ? 71.647 32.214 -36.922 1.00 8.95  ? 43   ASN A CB  1 
ATOM   358  C CG  . ASN A 1 43  ? 72.725 31.649 -37.836 1.00 15.56 ? 43   ASN A CG  1 
ATOM   359  O OD1 . ASN A 1 43  ? 72.455 30.804 -38.690 1.00 11.09 ? 43   ASN A OD1 1 
ATOM   360  N ND2 . ASN A 1 43  ? 73.962 32.114 -37.650 1.00 11.95 ? 43   ASN A ND2 1 
ATOM   361  N N   . GLY A 1 44  ? 69.743 35.036 -35.937 1.00 12.09 ? 44   GLY A N   1 
ATOM   362  C CA  . GLY A 1 44  ? 68.389 35.364 -35.538 1.00 12.10 ? 44   GLY A CA  1 
ATOM   363  C C   . GLY A 1 44  ? 67.721 34.296 -34.707 1.00 11.40 ? 44   GLY A C   1 
ATOM   364  O O   . GLY A 1 44  ? 66.496 34.303 -34.567 1.00 11.77 ? 44   GLY A O   1 
ATOM   365  N N   . VAL A 1 45  ? 68.494 33.359 -34.161 1.00 10.63 ? 45   VAL A N   1 
ATOM   366  C CA  . VAL A 1 45  ? 67.921 32.306 -33.328 1.00 12.18 ? 45   VAL A CA  1 
ATOM   367  C C   . VAL A 1 45  ? 67.447 32.874 -31.992 1.00 9.81  ? 45   VAL A C   1 
ATOM   368  O O   . VAL A 1 45  ? 66.387 32.493 -31.485 1.00 10.87 ? 45   VAL A O   1 
ATOM   369  C CB  . VAL A 1 45  ? 68.953 31.179 -33.131 1.00 12.62 ? 45   VAL A CB  1 
ATOM   370  C CG1 . VAL A 1 45  ? 68.489 30.208 -32.058 1.00 11.03 ? 45   VAL A CG1 1 
ATOM   371  C CG2 . VAL A 1 45  ? 69.215 30.459 -34.463 1.00 11.43 ? 45   VAL A CG2 1 
ATOM   372  N N   . VAL A 1 46  ? 68.232 33.773 -31.392 1.00 10.53 ? 46   VAL A N   1 
ATOM   373  C CA  . VAL A 1 46  ? 67.845 34.519 -30.197 1.00 10.10 ? 46   VAL A CA  1 
ATOM   374  C C   . VAL A 1 46  ? 68.064 35.995 -30.498 1.00 10.88 ? 46   VAL A C   1 
ATOM   375  O O   . VAL A 1 46  ? 68.795 36.363 -31.420 1.00 10.11 ? 46   VAL A O   1 
ATOM   376  C CB  . VAL A 1 46  ? 68.647 34.123 -28.932 1.00 11.36 ? 46   VAL A CB  1 
ATOM   377  C CG1 . VAL A 1 46  ? 68.495 32.650 -28.626 1.00 8.91  ? 46   VAL A CG1 1 
ATOM   378  C CG2 . VAL A 1 46  ? 70.122 34.521 -29.071 1.00 6.80  ? 46   VAL A CG2 1 
ATOM   379  N N   . SER A 1 47  ? 67.414 36.845 -29.704 1.00 12.22 ? 47   SER A N   1 
ATOM   380  C CA  . SER A 1 47  ? 67.594 38.277 -29.846 1.00 12.15 ? 47   SER A CA  1 
ATOM   381  C C   . SER A 1 47  ? 68.920 38.710 -29.219 1.00 11.79 ? 47   SER A C   1 
ATOM   382  O O   . SER A 1 47  ? 69.613 37.940 -28.551 1.00 11.38 ? 47   SER A O   1 
ATOM   383  C CB  . SER A 1 47  ? 66.434 39.032 -29.195 1.00 11.69 ? 47   SER A CB  1 
ATOM   384  O OG  . SER A 1 47  ? 66.679 39.202 -27.819 1.00 12.54 ? 47   SER A OG  1 
ATOM   385  N N   . ARG A 1 48  ? 69.255 39.980 -29.412 1.00 9.48  ? 48   ARG A N   1 
ATOM   386  C CA  . ARG A 1 48  ? 70.446 40.553 -28.806 1.00 11.79 ? 48   ARG A CA  1 
ATOM   387  C C   . ARG A 1 48  ? 70.177 41.179 -27.446 1.00 12.99 ? 48   ARG A C   1 
ATOM   388  O O   . ARG A 1 48  ? 71.112 41.722 -26.847 1.00 12.43 ? 48   ARG A O   1 
ATOM   389  C CB  . ARG A 1 48  ? 71.060 41.599 -29.745 1.00 13.23 ? 48   ARG A CB  1 
ATOM   390  C CG  . ARG A 1 48  ? 71.519 40.970 -31.038 1.00 16.76 ? 48   ARG A CG  1 
ATOM   391  C CD  . ARG A 1 48  ? 72.361 41.901 -31.879 1.00 23.04 ? 48   ARG A CD  1 
ATOM   392  N NE  . ARG A 1 48  ? 72.907 41.153 -33.004 1.00 27.05 ? 48   ARG A NE  1 
ATOM   393  C CZ  . ARG A 1 48  ? 72.208 40.841 -34.085 1.00 24.35 ? 48   ARG A CZ  1 
ATOM   394  N NH1 . ARG A 1 48  ? 70.950 41.240 -34.237 1.00 23.41 ? 48   ARG A NH1 1 
ATOM   395  N NH2 . ARG A 1 48  ? 72.786 40.120 -35.041 1.00 26.90 ? 48   ARG A NH2 1 
ATOM   396  N N   . ASP A 1 49  ? 68.940 41.113 -26.945 1.00 10.01 ? 49   ASP A N   1 
ATOM   397  C CA  . ASP A 1 49  ? 68.632 41.684 -25.635 1.00 11.31 ? 49   ASP A CA  1 
ATOM   398  C C   . ASP A 1 49  ? 69.337 40.902 -24.531 1.00 11.28 ? 49   ASP A C   1 
ATOM   399  O O   . ASP A 1 49  ? 69.569 39.696 -24.644 1.00 11.62 ? 49   ASP A O   1 
ATOM   400  C CB  . ASP A 1 49  ? 67.126 41.676 -25.366 1.00 10.91 ? 49   ASP A CB  1 
ATOM   401  C CG  . ASP A 1 49  ? 66.366 42.606 -26.276 1.00 14.52 ? 49   ASP A CG  1 
ATOM   402  O OD1 . ASP A 1 49  ? 67.003 43.477 -26.898 1.00 13.41 ? 49   ASP A OD1 1 
ATOM   403  O OD2 . ASP A 1 49  ? 65.127 42.451 -26.375 1.00 11.00 ? 49   ASP A OD2 1 
ATOM   404  N N   . LEU A 1 50  ? 69.658 41.606 -23.449 1.00 9.55  ? 50   LEU A N   1 
ATOM   405  C CA  . LEU A 1 50  ? 70.373 41.039 -22.313 1.00 10.21 ? 50   LEU A CA  1 
ATOM   406  C C   . LEU A 1 50  ? 69.393 40.785 -21.173 1.00 10.95 ? 50   LEU A C   1 
ATOM   407  O O   . LEU A 1 50  ? 68.776 41.728 -20.664 1.00 10.49 ? 50   LEU A O   1 
ATOM   408  C CB  . LEU A 1 50  ? 71.474 41.995 -21.850 1.00 13.26 ? 50   LEU A CB  1 
ATOM   409  C CG  . LEU A 1 50  ? 72.533 42.351 -22.899 1.00 17.61 ? 50   LEU A CG  1 
ATOM   410  C CD1 . LEU A 1 50  ? 73.495 43.406 -22.357 1.00 21.91 ? 50   LEU A CD1 1 
ATOM   411  C CD2 . LEU A 1 50  ? 73.286 41.100 -23.289 1.00 16.34 ? 50   LEU A CD2 1 
ATOM   412  N N   . VAL A 1 51  ? 69.284 39.525 -20.745 1.00 9.32  ? 51   VAL A N   1 
ATOM   413  C CA  . VAL A 1 51  ? 68.427 39.205 -19.605 1.00 10.03 ? 51   VAL A CA  1 
ATOM   414  C C   . VAL A 1 51  ? 68.912 39.924 -18.353 1.00 11.25 ? 51   VAL A C   1 
ATOM   415  O O   . VAL A 1 51  ? 68.109 40.299 -17.489 1.00 10.87 ? 51   VAL A O   1 
ATOM   416  C CB  . VAL A 1 51  ? 68.345 37.676 -19.401 1.00 10.06 ? 51   VAL A CB  1 
ATOM   417  C CG1 . VAL A 1 51  ? 69.692 37.100 -18.969 1.00 8.75  ? 51   VAL A CG1 1 
ATOM   418  C CG2 . VAL A 1 51  ? 67.233 37.326 -18.394 1.00 8.89  ? 51   VAL A CG2 1 
ATOM   419  N N   . GLU A 1 52  ? 70.215 40.167 -18.248 1.00 9.83  ? 52   GLU A N   1 
ATOM   420  C CA  . GLU A 1 52  ? 70.752 40.858 -17.085 1.00 13.09 ? 52   GLU A CA  1 
ATOM   421  C C   . GLU A 1 52  ? 70.486 42.363 -17.100 1.00 14.92 ? 52   GLU A C   1 
ATOM   422  O O   . GLU A 1 52  ? 70.912 43.054 -16.173 1.00 14.89 ? 52   GLU A O   1 
ATOM   423  C CB  . GLU A 1 52  ? 72.262 40.578 -16.959 1.00 13.88 ? 52   GLU A CB  1 
ATOM   424  C CG  . GLU A 1 52  ? 73.131 41.130 -18.090 1.00 16.86 ? 52   GLU A CG  1 
ATOM   425  C CD  . GLU A 1 52  ? 73.318 40.149 -19.243 1.00 16.72 ? 52   GLU A CD  1 
ATOM   426  O OE1 . GLU A 1 52  ? 72.410 39.331 -19.497 1.00 14.87 ? 52   GLU A OE1 1 
ATOM   427  O OE2 . GLU A 1 52  ? 74.377 40.206 -19.901 1.00 13.97 ? 52   GLU A OE2 1 
ATOM   428  N N   . GLU A 1 53  ? 69.791 42.895 -18.109 1.00 9.77  ? 53   GLU A N   1 
ATOM   429  C CA  . GLU A 1 53  ? 69.317 44.276 -18.073 1.00 13.82 ? 53   GLU A CA  1 
ATOM   430  C C   . GLU A 1 53  ? 67.805 44.361 -17.884 1.00 15.31 ? 53   GLU A C   1 
ATOM   431  O O   . GLU A 1 53  ? 67.172 45.332 -18.315 1.00 15.66 ? 53   GLU A O   1 
ATOM   432  C CB  . GLU A 1 53  ? 69.731 45.013 -19.344 1.00 13.76 ? 53   GLU A CB  1 
ATOM   433  C CG  . GLU A 1 53  ? 71.230 45.083 -19.508 1.00 16.61 ? 53   GLU A CG  1 
ATOM   434  C CD  . GLU A 1 53  ? 71.637 45.937 -20.696 1.00 29.83 ? 53   GLU A CD  1 
ATOM   435  O OE1 . GLU A 1 53  ? 70.855 46.017 -21.685 1.00 28.54 ? 53   GLU A OE1 1 
ATOM   436  O OE2 . GLU A 1 53  ? 72.750 46.505 -20.642 1.00 28.25 ? 53   GLU A OE2 1 
ATOM   437  N N   . GLY A 1 54  ? 67.214 43.362 -17.239 1.00 11.91 ? 54   GLY A N   1 
ATOM   438  C CA  . GLY A 1 54  ? 65.769 43.231 -17.147 1.00 11.23 ? 54   GLY A CA  1 
ATOM   439  C C   . GLY A 1 54  ? 65.139 43.922 -15.954 1.00 13.34 ? 54   GLY A C   1 
ATOM   440  O O   . GLY A 1 54  ? 65.672 44.894 -15.403 1.00 9.61  ? 54   GLY A O   1 
ATOM   441  N N   . ALA A 1 55  ? 64.000 43.375 -15.528 1.00 10.48 ? 55   ALA A N   1 
ATOM   442  C CA  . ALA A 1 55  ? 63.054 44.054 -14.647 1.00 10.95 ? 55   ALA A CA  1 
ATOM   443  C C   . ALA A 1 55  ? 63.481 44.129 -13.183 1.00 13.69 ? 55   ALA A C   1 
ATOM   444  O O   . ALA A 1 55  ? 62.835 44.866 -12.421 1.00 10.71 ? 55   ALA A O   1 
ATOM   445  C CB  . ALA A 1 55  ? 61.690 43.361 -14.742 1.00 9.75  ? 55   ALA A CB  1 
ATOM   446  N N   . ASP A 1 56  ? 64.516 43.382 -12.759 1.00 11.71 ? 56   ASP A N   1 
ATOM   447  C CA  . ASP A 1 56  ? 65.047 43.467 -11.392 1.00 10.39 ? 56   ASP A CA  1 
ATOM   448  C C   . ASP A 1 56  ? 64.026 43.036 -10.334 1.00 13.44 ? 56   ASP A C   1 
ATOM   449  O O   . ASP A 1 56  ? 63.936 43.634 -9.255  1.00 12.02 ? 56   ASP A O   1 
ATOM   450  C CB  . ASP A 1 56  ? 65.552 44.888 -11.090 1.00 12.92 ? 56   ASP A CB  1 
ATOM   451  C CG  . ASP A 1 56  ? 66.279 44.995 -9.744  1.00 22.64 ? 56   ASP A CG  1 
ATOM   452  O OD1 . ASP A 1 56  ? 66.904 43.999 -9.274  1.00 15.60 ? 56   ASP A OD1 1 
ATOM   453  O OD2 . ASP A 1 56  ? 66.093 46.054 -9.088  1.00 16.67 ? 56   ASP A OD2 1 
ATOM   454  N N   . TYR A 1 57  ? 63.266 41.973 -10.614 1.00 9.03  ? 57   TYR A N   1 
ATOM   455  C CA  . TYR A 1 57  ? 62.399 41.419 -9.570  1.00 11.14 ? 57   TYR A CA  1 
ATOM   456  C C   . TYR A 1 57  ? 63.206 40.942 -8.364  1.00 11.39 ? 57   TYR A C   1 
ATOM   457  O O   . TYR A 1 57  ? 62.692 40.922 -7.243  1.00 11.65 ? 57   TYR A O   1 
ATOM   458  C CB  . TYR A 1 57  ? 61.562 40.263 -10.129 1.00 8.97  ? 57   TYR A CB  1 
ATOM   459  C CG  . TYR A 1 57  ? 60.650 39.557 -9.130  1.00 10.65 ? 57   TYR A CG  1 
ATOM   460  C CD1 . TYR A 1 57  ? 59.539 40.206 -8.591  1.00 10.09 ? 57   TYR A CD1 1 
ATOM   461  C CD2 . TYR A 1 57  ? 60.885 38.232 -8.749  1.00 11.23 ? 57   TYR A CD2 1 
ATOM   462  C CE1 . TYR A 1 57  ? 58.688 39.558 -7.684  1.00 11.29 ? 57   TYR A CE1 1 
ATOM   463  C CE2 . TYR A 1 57  ? 60.043 37.569 -7.843  1.00 11.50 ? 57   TYR A CE2 1 
ATOM   464  C CZ  . TYR A 1 57  ? 58.950 38.237 -7.315  1.00 10.94 ? 57   TYR A CZ  1 
ATOM   465  O OH  . TYR A 1 57  ? 58.116 37.592 -6.416  1.00 11.00 ? 57   TYR A OH  1 
ATOM   466  N N   . TRP A 1 58  ? 64.466 40.540 -8.568  1.00 9.78  ? 58   TRP A N   1 
ATOM   467  C CA  . TRP A 1 58  ? 65.277 40.077 -7.441  1.00 8.68  ? 58   TRP A CA  1 
ATOM   468  C C   . TRP A 1 58  ? 65.334 41.119 -6.322  1.00 13.65 ? 58   TRP A C   1 
ATOM   469  O O   . TRP A 1 58  ? 65.266 40.772 -5.139  1.00 10.99 ? 58   TRP A O   1 
ATOM   470  C CB  . TRP A 1 58  ? 66.686 39.744 -7.918  1.00 11.57 ? 58   TRP A CB  1 
ATOM   471  C CG  . TRP A 1 58  ? 67.554 39.058 -6.912  1.00 11.20 ? 58   TRP A CG  1 
ATOM   472  C CD1 . TRP A 1 58  ? 68.545 39.629 -6.146  1.00 12.31 ? 58   TRP A CD1 1 
ATOM   473  C CD2 . TRP A 1 58  ? 67.542 37.665 -6.583  1.00 10.93 ? 58   TRP A CD2 1 
ATOM   474  N NE1 . TRP A 1 58  ? 69.145 38.670 -5.367  1.00 13.70 ? 58   TRP A NE1 1 
ATOM   475  C CE2 . TRP A 1 58  ? 68.541 37.459 -5.606  1.00 14.48 ? 58   TRP A CE2 1 
ATOM   476  C CE3 . TRP A 1 58  ? 66.774 36.571 -7.014  1.00 11.67 ? 58   TRP A CE3 1 
ATOM   477  C CZ2 . TRP A 1 58  ? 68.804 36.205 -5.060  1.00 11.98 ? 58   TRP A CZ2 1 
ATOM   478  C CZ3 . TRP A 1 58  ? 67.028 35.325 -6.463  1.00 14.18 ? 58   TRP A CZ3 1 
ATOM   479  C CH2 . TRP A 1 58  ? 68.038 35.155 -5.493  1.00 13.22 ? 58   TRP A CH2 1 
ATOM   480  N N   . ASN A 1 59  ? 65.471 42.398 -6.672  1.00 10.06 ? 59   ASN A N   1 
ATOM   481  C CA  . ASN A 1 59  ? 65.499 43.450 -5.661  1.00 13.56 ? 59   ASN A CA  1 
ATOM   482  C C   . ASN A 1 59  ? 64.201 44.245 -5.559  1.00 13.45 ? 59   ASN A C   1 
ATOM   483  O O   . ASN A 1 59  ? 63.942 44.840 -4.506  1.00 15.11 ? 59   ASN A O   1 
ATOM   484  C CB  . ASN A 1 59  ? 66.651 44.430 -5.931  1.00 13.04 ? 59   ASN A CB  1 
ATOM   485  C CG  . ASN A 1 59  ? 68.010 43.752 -5.934  1.00 16.94 ? 59   ASN A CG  1 
ATOM   486  O OD1 . ASN A 1 59  ? 68.507 43.328 -4.890  1.00 14.12 ? 59   ASN A OD1 1 
ATOM   487  N ND2 . ASN A 1 59  ? 68.626 43.655 -7.111  1.00 13.88 ? 59   ASN A ND2 1 
ATOM   488  N N   . SER A 1 60  ? 63.378 44.266 -6.606  1.00 12.31 ? 60   SER A N   1 
ATOM   489  C CA  . SER A 1 60  ? 62.184 45.101 -6.637  1.00 14.82 ? 60   SER A CA  1 
ATOM   490  C C   . SER A 1 60  ? 60.912 44.309 -6.375  1.00 11.36 ? 60   SER A C   1 
ATOM   491  O O   . SER A 1 60  ? 59.821 44.774 -6.721  1.00 11.19 ? 60   SER A O   1 
ATOM   492  C CB  . SER A 1 60  ? 62.074 45.827 -7.981  1.00 15.92 ? 60   SER A CB  1 
ATOM   493  O OG  . SER A 1 60  ? 63.175 46.691 -8.186  1.00 21.76 ? 60   SER A OG  1 
ATOM   494  N N   . TYR A 1 61  ? 61.025 43.130 -5.760  1.00 11.58 ? 61   TYR A N   1 
ATOM   495  C CA  . TYR A 1 61  ? 59.847 42.279 -5.594  1.00 11.77 ? 61   TYR A CA  1 
ATOM   496  C C   . TYR A 1 61  ? 58.740 42.981 -4.808  1.00 12.18 ? 61   TYR A C   1 
ATOM   497  O O   . TYR A 1 61  ? 57.551 42.785 -5.096  1.00 11.11 ? 61   TYR A O   1 
ATOM   498  C CB  . TYR A 1 61  ? 60.234 40.966 -4.920  1.00 11.25 ? 61   TYR A CB  1 
ATOM   499  C CG  . TYR A 1 61  ? 60.981 41.122 -3.603  1.00 11.40 ? 61   TYR A CG  1 
ATOM   500  C CD1 . TYR A 1 61  ? 62.368 41.186 -3.566  1.00 11.72 ? 61   TYR A CD1 1 
ATOM   501  C CD2 . TYR A 1 61  ? 60.285 41.167 -2.390  1.00 12.46 ? 61   TYR A CD2 1 
ATOM   502  C CE1 . TYR A 1 61  ? 63.052 41.314 -2.346  1.00 11.94 ? 61   TYR A CE1 1 
ATOM   503  C CE2 . TYR A 1 61  ? 60.953 41.292 -1.177  1.00 11.91 ? 61   TYR A CE2 1 
ATOM   504  C CZ  . TYR A 1 61  ? 62.332 41.355 -1.159  1.00 13.60 ? 61   TYR A CZ  1 
ATOM   505  O OH  . TYR A 1 61  ? 62.989 41.475 0.051   1.00 15.70 ? 61   TYR A OH  1 
ATOM   506  N N   . ALA A 1 62  ? 59.100 43.815 -3.825  1.00 9.97  ? 62   ALA A N   1 
ATOM   507  C CA  . ALA A 1 62  ? 58.070 44.487 -3.032  1.00 12.25 ? 62   ALA A CA  1 
ATOM   508  C C   . ALA A 1 62  ? 57.220 45.418 -3.892  1.00 11.33 ? 62   ALA A C   1 
ATOM   509  O O   . ALA A 1 62  ? 55.997 45.489 -3.712  1.00 12.18 ? 62   ALA A O   1 
ATOM   510  C CB  . ALA A 1 62  ? 58.701 45.265 -1.870  1.00 13.19 ? 62   ALA A CB  1 
ATOM   511  N N   . ARG A 1 63  ? 57.844 46.135 -4.835  1.00 11.94 ? 63   ARG A N   1 
ATOM   512  C CA  . ARG A 1 63  ? 57.072 46.958 -5.769  1.00 13.83 ? 63   ARG A CA  1 
ATOM   513  C C   . ARG A 1 63  ? 56.146 46.106 -6.626  1.00 14.70 ? 63   ARG A C   1 
ATOM   514  O O   . ARG A 1 63  ? 55.005 46.504 -6.906  1.00 10.52 ? 63   ARG A O   1 
ATOM   515  C CB  . ARG A 1 63  ? 57.990 47.770 -6.691  1.00 13.47 ? 63   ARG A CB  1 
ATOM   516  C CG  . ARG A 1 63  ? 58.659 48.988 -6.112  1.00 24.56 ? 63   ARG A CG  1 
ATOM   517  C CD  . ARG A 1 63  ? 59.236 49.833 -7.267  1.00 24.67 ? 63   ARG A CD  1 
ATOM   518  N NE  . ARG A 1 63  ? 60.390 49.225 -7.921  1.00 26.32 ? 63   ARG A NE  1 
ATOM   519  C CZ  . ARG A 1 63  ? 60.816 49.536 -9.142  1.00 31.37 ? 63   ARG A CZ  1 
ATOM   520  N NH1 . ARG A 1 63  ? 60.135 50.358 -9.929  1.00 28.01 ? 63   ARG A NH1 1 
ATOM   521  N NH2 . ARG A 1 63  ? 61.952 49.003 -9.590  1.00 28.88 ? 63   ARG A NH2 1 
ATOM   522  N N   . VAL A 1 64  ? 56.640 44.955 -7.099  1.00 10.69 ? 64   VAL A N   1 
ATOM   523  C CA  . VAL A 1 64  ? 55.825 44.091 -7.949  1.00 10.96 ? 64   VAL A CA  1 
ATOM   524  C C   . VAL A 1 64  ? 54.652 43.522 -7.158  1.00 11.44 ? 64   VAL A C   1 
ATOM   525  O O   . VAL A 1 64  ? 53.505 43.518 -7.629  1.00 10.56 ? 64   VAL A O   1 
ATOM   526  C CB  . VAL A 1 64  ? 56.685 42.971 -8.572  1.00 10.69 ? 64   VAL A CB  1 
ATOM   527  C CG1 . VAL A 1 64  ? 55.796 41.984 -9.331  1.00 12.85 ? 64   VAL A CG1 1 
ATOM   528  C CG2 . VAL A 1 64  ? 57.733 43.557 -9.512  1.00 11.17 ? 64   VAL A CG2 1 
ATOM   529  N N   . HIS A 1 65  ? 54.918 43.029 -5.942  1.00 9.31  ? 65   HIS A N   1 
ATOM   530  C CA  . HIS A 1 65  ? 53.841 42.487 -5.119  1.00 11.07 ? 65   HIS A CA  1 
ATOM   531  C C   . HIS A 1 65  ? 52.816 43.556 -4.760  1.00 9.24  ? 65   HIS A C   1 
ATOM   532  O O   . HIS A 1 65  ? 51.621 43.256 -4.651  1.00 8.93  ? 65   HIS A O   1 
ATOM   533  C CB  . HIS A 1 65  ? 54.413 41.862 -3.836  1.00 11.77 ? 65   HIS A CB  1 
ATOM   534  C CG  . HIS A 1 65  ? 55.374 40.736 -4.082  1.00 9.88  ? 65   HIS A CG  1 
ATOM   535  N ND1 . HIS A 1 65  ? 56.284 40.317 -3.132  1.00 8.92  ? 65   HIS A ND1 1 
ATOM   536  C CD2 . HIS A 1 65  ? 55.578 39.953 -5.171  1.00 9.13  ? 65   HIS A CD2 1 
ATOM   537  C CE1 . HIS A 1 65  ? 57.005 39.321 -3.624  1.00 10.27 ? 65   HIS A CE1 1 
ATOM   538  N NE2 . HIS A 1 65  ? 56.598 39.080 -4.861  1.00 8.42  ? 65   HIS A NE2 1 
ATOM   539  N N   . GLU A 1 66  ? 53.260 44.805 -4.568  1.00 10.29 ? 66   GLU A N   1 
ATOM   540  C CA  . GLU A 1 66  ? 52.311 45.871 -4.239  1.00 14.79 ? 66   GLU A CA  1 
ATOM   541  C C   . GLU A 1 66  ? 51.420 46.200 -5.436  1.00 13.92 ? 66   GLU A C   1 
ATOM   542  O O   . GLU A 1 66  ? 50.237 46.510 -5.261  1.00 14.26 ? 66   GLU A O   1 
ATOM   543  C CB  . GLU A 1 66  ? 53.064 47.115 -3.746  1.00 17.82 ? 66   GLU A CB  1 
ATOM   544  N N   . LEU A 1 67  ? 51.956 46.119 -6.658  1.00 13.16 ? 67   LEU A N   1 
ATOM   545  C CA  . LEU A 1 67  ? 51.100 46.277 -7.827  1.00 13.05 ? 67   LEU A CA  1 
ATOM   546  C C   . LEU A 1 67  ? 49.970 45.255 -7.815  1.00 13.76 ? 67   LEU A C   1 
ATOM   547  O O   . LEU A 1 67  ? 48.834 45.568 -8.198  1.00 11.46 ? 67   LEU A O   1 
ATOM   548  C CB  . LEU A 1 67  ? 51.923 46.152 -9.110  1.00 11.99 ? 67   LEU A CB  1 
ATOM   549  C CG  . LEU A 1 67  ? 52.844 47.325 -9.428  1.00 15.09 ? 67   LEU A CG  1 
ATOM   550  C CD1 . LEU A 1 67  ? 53.802 46.934 -10.544 1.00 17.13 ? 67   LEU A CD1 1 
ATOM   551  C CD2 . LEU A 1 67  ? 52.020 48.535 -9.831  1.00 19.63 ? 67   LEU A CD2 1 
ATOM   552  N N   . CYS A 1 68  ? 50.261 44.026 -7.365  1.00 9.61  ? 68   CYS A N   1 
ATOM   553  C CA  . CYS A 1 68  ? 49.247 42.975 -7.351  1.00 10.31 ? 68   CYS A CA  1 
ATOM   554  C C   . CYS A 1 68  ? 48.214 43.221 -6.266  1.00 14.17 ? 68   CYS A C   1 
ATOM   555  O O   . CYS A 1 68  ? 47.003 43.130 -6.511  1.00 11.90 ? 68   CYS A O   1 
ATOM   556  C CB  . CYS A 1 68  ? 49.898 41.608 -7.142  1.00 10.22 ? 68   CYS A CB  1 
ATOM   557  S SG  . CYS A 1 68  ? 51.040 41.137 -8.467  1.00 13.16 ? 68   CYS A SG  1 
ATOM   558  N N   . SER A 1 69  ? 48.674 43.496 -5.044  1.00 11.76 ? 69   SER A N   1 
ATOM   559  C CA  . SER A 1 69  ? 47.727 43.653 -3.953  1.00 16.39 ? 69   SER A CA  1 
ATOM   560  C C   . SER A 1 69  ? 46.894 44.922 -4.106  1.00 11.69 ? 69   SER A C   1 
ATOM   561  O O   . SER A 1 69  ? 45.742 44.946 -3.664  1.00 14.29 ? 69   SER A O   1 
ATOM   562  C CB  . SER A 1 69  ? 48.454 43.631 -2.608  1.00 14.83 ? 69   SER A CB  1 
ATOM   563  O OG  . SER A 1 69  ? 49.293 44.749 -2.485  1.00 21.27 ? 69   SER A OG  1 
ATOM   564  N N   . ARG A 1 70  ? 47.425 45.960 -4.765  1.00 12.76 ? 70   ARG A N   1 
ATOM   565  C CA  . ARG A 1 70  ? 46.676 47.215 -4.873  1.00 17.25 ? 70   ARG A CA  1 
ATOM   566  C C   . ARG A 1 70  ? 45.376 47.046 -5.662  1.00 16.01 ? 70   ARG A C   1 
ATOM   567  O O   . ARG A 1 70  ? 44.400 47.759 -5.404  1.00 20.59 ? 70   ARG A O   1 
ATOM   568  C CB  . ARG A 1 70  ? 47.560 48.305 -5.494  1.00 19.16 ? 70   ARG A CB  1 
ATOM   569  N N   . ILE A 1 71  ? 45.318 46.121 -6.615  1.00 11.98 ? 71   ILE A N   1 
ATOM   570  C CA  . ILE A 1 71  ? 44.064 45.868 -7.316  1.00 14.01 ? 71   ILE A CA  1 
ATOM   571  C C   . ILE A 1 71  ? 43.376 44.614 -6.780  1.00 14.97 ? 71   ILE A C   1 
ATOM   572  O O   . ILE A 1 71  ? 42.516 44.042 -7.450  1.00 13.42 ? 71   ILE A O   1 
ATOM   573  C CB  . ILE A 1 71  ? 44.249 45.808 -8.842  1.00 13.08 ? 71   ILE A CB  1 
ATOM   574  C CG1 . ILE A 1 71  ? 45.332 44.811 -9.246  1.00 11.96 ? 71   ILE A CG1 1 
ATOM   575  C CG2 . ILE A 1 71  ? 44.551 47.206 -9.400  1.00 12.91 ? 71   ILE A CG2 1 
ATOM   576  C CD1 . ILE A 1 71  ? 45.255 44.406 -10.742 1.00 11.92 ? 71   ILE A CD1 1 
ATOM   577  N N   . GLY A 1 72  ? 43.750 44.177 -5.582  1.00 12.86 ? 72   GLY A N   1 
ATOM   578  C CA  . GLY A 1 72  ? 43.031 43.111 -4.921  1.00 14.36 ? 72   GLY A CA  1 
ATOM   579  C C   . GLY A 1 72  ? 43.331 41.706 -5.382  1.00 13.50 ? 72   GLY A C   1 
ATOM   580  O O   . GLY A 1 72  ? 42.507 40.808 -5.144  1.00 9.63  ? 72   GLY A O   1 
ATOM   581  N N   . MET A 1 73  ? 44.469 41.457 -6.032  1.00 11.17 ? 73   MET A N   1 
ATOM   582  C CA  . MET A 1 73  ? 44.653 40.048 -6.320  1.00 12.46 ? 73   MET A CA  1 
ATOM   583  C C   . MET A 1 73  ? 45.100 39.341 -5.038  1.00 13.02 ? 73   MET A C   1 
ATOM   584  O O   . MET A 1 73  ? 45.562 39.967 -4.079  1.00 11.84 ? 73   MET A O   1 
ATOM   585  C CB  . MET A 1 73  ? 45.629 39.783 -7.480  1.00 15.18 ? 73   MET A CB  1 
ATOM   586  C CG  . MET A 1 73  ? 45.857 40.915 -8.457  1.00 11.25 ? 73   MET A CG  1 
ATOM   587  S SD  . MET A 1 73  ? 47.256 40.639 -9.581  1.00 13.61 ? 73   MET A SD  1 
ATOM   588  C CE  . MET A 1 73  ? 46.318 39.897 -10.909 1.00 26.52 ? 73   MET A CE  1 
ATOM   589  N N   . ASN A 1 74  ? 44.898 38.023 -5.009  1.00 9.45  ? 74   ASN A N   1 
ATOM   590  C CA  . ASN A 1 74  ? 45.129 37.251 -3.796  1.00 12.53 ? 74   ASN A CA  1 
ATOM   591  C C   . ASN A 1 74  ? 45.991 36.014 -4.052  1.00 12.86 ? 74   ASN A C   1 
ATOM   592  O O   . ASN A 1 74  ? 46.043 35.120 -3.201  1.00 10.40 ? 74   ASN A O   1 
ATOM   593  C CB  . ASN A 1 74  ? 43.785 36.876 -3.151  1.00 11.65 ? 74   ASN A CB  1 
ATOM   594  C CG  . ASN A 1 74  ? 42.897 36.037 -4.062  1.00 15.11 ? 74   ASN A CG  1 
ATOM   595  O OD1 . ASN A 1 74  ? 43.202 35.825 -5.235  1.00 16.15 ? 74   ASN A OD1 1 
ATOM   596  N ND2 . ASN A 1 74  ? 41.792 35.547 -3.515  1.00 15.50 ? 74   ASN A ND2 1 
ATOM   597  N N   . VAL A 1 75  ? 46.676 35.946 -5.196  1.00 10.82 ? 75   VAL A N   1 
ATOM   598  C CA  . VAL A 1 75  ? 47.611 34.857 -5.454  1.00 13.65 ? 75   VAL A CA  1 
ATOM   599  C C   . VAL A 1 75  ? 48.698 35.347 -6.402  1.00 12.67 ? 75   VAL A C   1 
ATOM   600  O O   . VAL A 1 75  ? 48.467 36.207 -7.260  1.00 10.38 ? 75   VAL A O   1 
ATOM   601  C CB  . VAL A 1 75  ? 46.893 33.600 -6.017  1.00 12.50 ? 75   VAL A CB  1 
ATOM   602  C CG1 . VAL A 1 75  ? 46.340 33.853 -7.448  1.00 8.90  ? 75   VAL A CG1 1 
ATOM   603  C CG2 . VAL A 1 75  ? 47.830 32.373 -5.999  1.00 10.75 ? 75   VAL A CG2 1 
ATOM   604  N N   . ILE A 1 76  ? 49.897 34.791 -6.238  1.00 9.95  ? 76   ILE A N   1 
ATOM   605  C CA  . ILE A 1 76  ? 50.974 34.960 -7.199  1.00 11.12 ? 76   ILE A CA  1 
ATOM   606  C C   . ILE A 1 76  ? 51.747 33.648 -7.304  1.00 15.63 ? 76   ILE A C   1 
ATOM   607  O O   . ILE A 1 76  ? 51.960 32.950 -6.305  1.00 12.03 ? 76   ILE A O   1 
ATOM   608  C CB  . ILE A 1 76  ? 51.882 36.140 -6.795  1.00 11.30 ? 76   ILE A CB  1 
ATOM   609  C CG1 . ILE A 1 76  ? 52.829 36.515 -7.927  1.00 15.66 ? 76   ILE A CG1 1 
ATOM   610  C CG2 . ILE A 1 76  ? 52.634 35.843 -5.476  1.00 9.53  ? 76   ILE A CG2 1 
ATOM   611  C CD1 . ILE A 1 76  ? 53.593 37.824 -7.646  1.00 14.68 ? 76   ILE A CD1 1 
ATOM   612  N N   . ARG A 1 77  ? 52.144 33.297 -8.525  1.00 10.57 ? 77   ARG A N   1 
ATOM   613  C CA  . ARG A 1 77  ? 52.981 32.128 -8.767  1.00 9.35  ? 77   ARG A CA  1 
ATOM   614  C C   . ARG A 1 77  ? 54.346 32.617 -9.218  1.00 8.56  ? 77   ARG A C   1 
ATOM   615  O O   . ARG A 1 77  ? 54.440 33.378 -10.188 1.00 9.44  ? 77   ARG A O   1 
ATOM   616  C CB  . ARG A 1 77  ? 52.367 31.203 -9.815  1.00 7.95  ? 77   ARG A CB  1 
ATOM   617  C CG  . ARG A 1 77  ? 53.176 29.923 -10.059 1.00 7.77  ? 77   ARG A CG  1 
ATOM   618  C CD  . ARG A 1 77  ? 54.009 30.013 -11.347 1.00 7.21  ? 77   ARG A CD  1 
ATOM   619  N NE  . ARG A 1 77  ? 53.171 30.092 -12.546 1.00 8.40  ? 77   ARG A NE  1 
ATOM   620  C CZ  . ARG A 1 77  ? 53.570 29.756 -13.767 1.00 12.07 ? 77   ARG A CZ  1 
ATOM   621  N NH1 . ARG A 1 77  ? 54.830 29.414 -14.019 1.00 8.03  ? 77   ARG A NH1 1 
ATOM   622  N NH2 . ARG A 1 77  ? 52.678 29.749 -14.762 1.00 8.08  ? 77   ARG A NH2 1 
ATOM   623  N N   . ILE A 1 78  ? 55.396 32.191 -8.515  1.00 9.35  ? 78   ILE A N   1 
ATOM   624  C CA  . ILE A 1 78  ? 56.758 32.602 -8.826  1.00 10.77 ? 78   ILE A CA  1 
ATOM   625  C C   . ILE A 1 78  ? 57.579 31.352 -9.094  1.00 10.28 ? 78   ILE A C   1 
ATOM   626  O O   . ILE A 1 78  ? 57.247 30.253 -8.643  1.00 10.70 ? 78   ILE A O   1 
ATOM   627  C CB  . ILE A 1 78  ? 57.394 33.422 -7.685  1.00 12.84 ? 78   ILE A CB  1 
ATOM   628  C CG1 . ILE A 1 78  ? 57.542 32.559 -6.446  1.00 15.77 ? 78   ILE A CG1 1 
ATOM   629  C CG2 . ILE A 1 78  ? 56.506 34.607 -7.281  1.00 13.52 ? 78   ILE A CG2 1 
ATOM   630  C CD1 . ILE A 1 78  ? 58.614 33.082 -5.522  1.00 21.25 ? 78   ILE A CD1 1 
ATOM   631  N N   . GLY A 1 79  ? 58.664 31.529 -9.837  1.00 11.07 ? 79   GLY A N   1 
ATOM   632  C CA  . GLY A 1 79  ? 59.611 30.457 -10.078 1.00 11.50 ? 79   GLY A CA  1 
ATOM   633  C C   . GLY A 1 79  ? 60.858 30.653 -9.233  1.00 11.22 ? 79   GLY A C   1 
ATOM   634  O O   . GLY A 1 79  ? 61.307 31.783 -9.018  1.00 14.27 ? 79   GLY A O   1 
ATOM   635  N N   . ILE A 1 80  ? 61.406 29.550 -8.747  1.00 10.84 ? 80   ILE A N   1 
ATOM   636  C CA  . ILE A 1 80  ? 62.724 29.578 -8.133  1.00 9.48  ? 80   ILE A CA  1 
ATOM   637  C C   . ILE A 1 80  ? 63.693 28.862 -9.060  1.00 10.96 ? 80   ILE A C   1 
ATOM   638  O O   . ILE A 1 80  ? 63.340 27.898 -9.750  1.00 13.23 ? 80   ILE A O   1 
ATOM   639  C CB  . ILE A 1 80  ? 62.731 28.962 -6.717  1.00 10.97 ? 80   ILE A CB  1 
ATOM   640  C CG1 . ILE A 1 80  ? 62.237 27.513 -6.744  1.00 12.86 ? 80   ILE A CG1 1 
ATOM   641  C CG2 . ILE A 1 80  ? 61.888 29.822 -5.744  1.00 10.81 ? 80   ILE A CG2 1 
ATOM   642  C CD1 . ILE A 1 80  ? 62.566 26.772 -5.442  1.00 14.87 ? 80   ILE A CD1 1 
ATOM   643  N N   . GLU A 1 81  ? 64.933 29.329 -9.056  1.00 13.66 ? 81   GLU A N   1 
ATOM   644  C CA  . GLU A 1 81  ? 65.934 28.957 -10.048 1.00 11.37 ? 81   GLU A CA  1 
ATOM   645  C C   . GLU A 1 81  ? 66.824 27.898 -9.400  1.00 13.40 ? 81   GLU A C   1 
ATOM   646  O O   . GLU A 1 81  ? 67.611 28.209 -8.491  1.00 10.40 ? 81   GLU A O   1 
ATOM   647  C CB  . GLU A 1 81  ? 66.734 30.205 -10.416 1.00 11.75 ? 81   GLU A CB  1 
ATOM   648  C CG  . GLU A 1 81  ? 66.246 31.074 -11.595 1.00 10.57 ? 81   GLU A CG  1 
ATOM   649  C CD  . GLU A 1 81  ? 65.817 30.339 -12.876 1.00 14.56 ? 81   GLU A CD  1 
ATOM   650  O OE1 . GLU A 1 81  ? 64.682 29.794 -12.984 1.00 12.07 ? 81   GLU A OE1 1 
ATOM   651  O OE2 . GLU A 1 81  ? 66.633 30.397 -13.819 1.00 11.94 ? 81   GLU A OE2 1 
ATOM   652  N N   . TRP A 1 82  ? 66.674 26.650 -9.836  1.00 10.44 ? 82   TRP A N   1 
ATOM   653  C CA  . TRP A 1 82  ? 67.584 25.554 -9.494  1.00 11.14 ? 82   TRP A CA  1 
ATOM   654  C C   . TRP A 1 82  ? 69.050 25.992 -9.605  1.00 10.98 ? 82   TRP A C   1 
ATOM   655  O O   . TRP A 1 82  ? 69.874 25.704 -8.726  1.00 8.92  ? 82   TRP A O   1 
ATOM   656  C CB  . TRP A 1 82  ? 67.272 24.381 -10.428 1.00 10.56 ? 82   TRP A CB  1 
ATOM   657  C CG  . TRP A 1 82  ? 67.907 23.037 -10.152 1.00 11.06 ? 82   TRP A CG  1 
ATOM   658  C CD1 . TRP A 1 82  ? 68.748 22.699 -9.135  1.00 9.78  ? 82   TRP A CD1 1 
ATOM   659  C CD2 . TRP A 1 82  ? 67.700 21.847 -10.920 1.00 11.16 ? 82   TRP A CD2 1 
ATOM   660  N NE1 . TRP A 1 82  ? 69.083 21.359 -9.227  1.00 12.74 ? 82   TRP A NE1 1 
ATOM   661  C CE2 . TRP A 1 82  ? 68.453 20.819 -10.317 1.00 10.74 ? 82   TRP A CE2 1 
ATOM   662  C CE3 . TRP A 1 82  ? 66.951 21.553 -12.068 1.00 11.69 ? 82   TRP A CE3 1 
ATOM   663  C CZ2 . TRP A 1 82  ? 68.476 19.518 -10.821 1.00 11.85 ? 82   TRP A CZ2 1 
ATOM   664  C CZ3 . TRP A 1 82  ? 66.970 20.251 -12.567 1.00 11.64 ? 82   TRP A CZ3 1 
ATOM   665  C CH2 . TRP A 1 82  ? 67.733 19.261 -11.951 1.00 11.23 ? 82   TRP A CH2 1 
ATOM   666  N N   . SER A 1 83  ? 69.367 26.762 -10.649 1.00 9.37  ? 83   SER A N   1 
ATOM   667  C CA  . SER A 1 83  ? 70.737 27.211 -10.897 1.00 10.24 ? 83   SER A CA  1 
ATOM   668  C C   . SER A 1 83  ? 71.272 28.149 -9.822  1.00 12.35 ? 83   SER A C   1 
ATOM   669  O O   . SER A 1 83  ? 72.499 28.250 -9.662  1.00 10.52 ? 83   SER A O   1 
ATOM   670  C CB  . SER A 1 83  ? 70.796 27.912 -12.239 1.00 11.49 ? 83   SER A CB  1 
ATOM   671  O OG  . SER A 1 83  ? 69.882 29.005 -12.221 1.00 12.96 ? 83   SER A OG  1 
ATOM   672  N N   . ARG A 1 84  ? 70.394 28.857 -9.104  1.00 9.28  ? 84   ARG A N   1 
ATOM   673  C CA  . ARG A 1 84  ? 70.819 29.688 -7.977  1.00 9.61  ? 84   ARG A CA  1 
ATOM   674  C C   . ARG A 1 84  ? 70.894 28.905 -6.667  1.00 11.71 ? 84   ARG A C   1 
ATOM   675  O O   . ARG A 1 84  ? 71.832 29.107 -5.886  1.00 9.71  ? 84   ARG A O   1 
ATOM   676  C CB  . ARG A 1 84  ? 69.858 30.864 -7.772  1.00 10.10 ? 84   ARG A CB  1 
ATOM   677  C CG  . ARG A 1 84  ? 69.733 31.873 -8.910  1.00 9.77  ? 84   ARG A CG  1 
ATOM   678  C CD  . ARG A 1 84  ? 68.754 32.981 -8.457  1.00 12.55 ? 84   ARG A CD  1 
ATOM   679  N NE  . ARG A 1 84  ? 68.477 33.960 -9.505  1.00 12.64 ? 84   ARG A NE  1 
ATOM   680  C CZ  . ARG A 1 84  ? 69.250 35.003 -9.772  1.00 14.93 ? 84   ARG A CZ  1 
ATOM   681  N NH1 . ARG A 1 84  ? 70.373 35.214 -9.097  1.00 9.63  ? 84   ARG A NH1 1 
ATOM   682  N NH2 . ARG A 1 84  ? 68.883 35.859 -10.732 1.00 9.54  ? 84   ARG A NH2 1 
ATOM   683  N N   . ILE A 1 85  ? 69.904 28.033 -6.413  1.00 11.06 ? 85   ILE A N   1 
ATOM   684  C CA  . ILE A 1 85  ? 69.862 27.251 -5.173  1.00 13.01 ? 85   ILE A CA  1 
ATOM   685  C C   . ILE A 1 85  ? 71.043 26.291 -5.100  1.00 13.44 ? 85   ILE A C   1 
ATOM   686  O O   . ILE A 1 85  ? 71.676 26.139 -4.046  1.00 12.14 ? 85   ILE A O   1 
ATOM   687  C CB  . ILE A 1 85  ? 68.536 26.466 -5.046  1.00 11.80 ? 85   ILE A CB  1 
ATOM   688  C CG1 . ILE A 1 85  ? 67.254 27.314 -5.070  1.00 17.01 ? 85   ILE A CG1 1 
ATOM   689  C CG2 . ILE A 1 85  ? 68.522 25.674 -3.769  1.00 12.45 ? 85   ILE A CG2 1 
ATOM   690  C CD1 . ILE A 1 85  ? 67.401 28.603 -4.577  1.00 20.25 ? 85   ILE A CD1 1 
ATOM   691  N N   . PHE A 1 86  ? 71.339 25.598 -6.205  1.00 11.51 ? 86   PHE A N   1 
ATOM   692  C CA  . PHE A 1 86  ? 72.435 24.626 -6.273  1.00 12.01 ? 86   PHE A CA  1 
ATOM   693  C C   . PHE A 1 86  ? 73.375 25.054 -7.391  1.00 13.91 ? 86   PHE A C   1 
ATOM   694  O O   . PHE A 1 86  ? 73.301 24.534 -8.515  1.00 12.51 ? 86   PHE A O   1 
ATOM   695  C CB  . PHE A 1 86  ? 71.913 23.204 -6.484  1.00 12.21 ? 86   PHE A CB  1 
ATOM   696  C CG  . PHE A 1 86  ? 71.286 22.612 -5.252  1.00 15.67 ? 86   PHE A CG  1 
ATOM   697  C CD1 . PHE A 1 86  ? 72.059 22.349 -4.132  1.00 19.42 ? 86   PHE A CD1 1 
ATOM   698  C CD2 . PHE A 1 86  ? 69.931 22.351 -5.195  1.00 18.95 ? 86   PHE A CD2 1 
ATOM   699  C CE1 . PHE A 1 86  ? 71.498 21.831 -2.989  1.00 16.63 ? 86   PHE A CE1 1 
ATOM   700  C CE2 . PHE A 1 86  ? 69.353 21.823 -4.037  1.00 16.84 ? 86   PHE A CE2 1 
ATOM   701  C CZ  . PHE A 1 86  ? 70.136 21.566 -2.943  1.00 19.41 ? 86   PHE A CZ  1 
ATOM   702  N N   . PRO A 1 87  ? 74.263 26.018 -7.128  1.00 13.05 ? 87   PRO A N   1 
ATOM   703  C CA  . PRO A 1 87  ? 75.142 26.513 -8.201  1.00 14.38 ? 87   PRO A CA  1 
ATOM   704  C C   . PRO A 1 87  ? 76.147 25.485 -8.682  1.00 16.45 ? 87   PRO A C   1 
ATOM   705  O O   . PRO A 1 87  ? 76.692 25.649 -9.782  1.00 15.19 ? 87   PRO A O   1 
ATOM   706  C CB  . PRO A 1 87  ? 75.849 27.716 -7.559  1.00 14.38 ? 87   PRO A CB  1 
ATOM   707  C CG  . PRO A 1 87  ? 75.796 27.438 -6.082  1.00 15.51 ? 87   PRO A CG  1 
ATOM   708  C CD  . PRO A 1 87  ? 74.512 26.691 -5.839  1.00 15.36 ? 87   PRO A CD  1 
ATOM   709  N N   . ASN A 1 88  ? 76.402 24.435 -7.900  1.00 14.29 ? 88   ASN A N   1 
ATOM   710  C CA  . ASN A 1 88  ? 77.377 23.396 -8.194  1.00 14.98 ? 88   ASN A CA  1 
ATOM   711  C C   . ASN A 1 88  ? 76.718 22.024 -8.248  1.00 15.15 ? 88   ASN A C   1 
ATOM   712  O O   . ASN A 1 88  ? 75.716 21.786 -7.563  1.00 15.03 ? 88   ASN A O   1 
ATOM   713  C CB  . ASN A 1 88  ? 78.486 23.402 -7.140  1.00 17.56 ? 88   ASN A CB  1 
ATOM   714  C CG  . ASN A 1 88  ? 79.263 24.687 -7.164  1.00 20.89 ? 88   ASN A CG  1 
ATOM   715  O OD1 . ASN A 1 88  ? 79.755 25.092 -8.216  1.00 21.25 ? 88   ASN A OD1 1 
ATOM   716  N ND2 . ASN A 1 88  ? 79.328 25.370 -6.028  1.00 20.66 ? 88   ASN A ND2 1 
ATOM   717  N N   . PRO A 1 89  ? 77.246 21.112 -9.068  1.00 16.62 ? 89   PRO A N   1 
ATOM   718  C CA  . PRO A 1 89  ? 76.566 19.827 -9.276  1.00 17.09 ? 89   PRO A CA  1 
ATOM   719  C C   . PRO A 1 89  ? 76.389 19.062 -7.975  1.00 20.24 ? 89   PRO A C   1 
ATOM   720  O O   . PRO A 1 89  ? 77.252 19.082 -7.095  1.00 17.54 ? 89   PRO A O   1 
ATOM   721  C CB  . PRO A 1 89  ? 77.491 19.071 -10.238 1.00 15.56 ? 89   PRO A CB  1 
ATOM   722  C CG  . PRO A 1 89  ? 78.745 19.861 -10.330 1.00 19.10 ? 89   PRO A CG  1 
ATOM   723  C CD  . PRO A 1 89  ? 78.473 21.249 -9.878  1.00 16.73 ? 89   PRO A CD  1 
ATOM   724  N N   . THR A 1 90  ? 75.261 18.365 -7.877  1.00 17.41 ? 90   THR A N   1 
ATOM   725  C CA  . THR A 1 90  ? 74.915 17.578 -6.702  1.00 19.47 ? 90   THR A CA  1 
ATOM   726  C C   . THR A 1 90  ? 75.124 16.083 -6.899  1.00 22.15 ? 90   THR A C   1 
ATOM   727  O O   . THR A 1 90  ? 74.887 15.317 -5.961  1.00 22.35 ? 90   THR A O   1 
ATOM   728  C CB  . THR A 1 90  ? 73.457 17.841 -6.300  1.00 22.46 ? 90   THR A CB  1 
ATOM   729  O OG1 . THR A 1 90  ? 72.602 17.688 -7.447  1.00 19.94 ? 90   THR A OG1 1 
ATOM   730  C CG2 . THR A 1 90  ? 73.304 19.252 -5.748  1.00 18.87 ? 90   THR A CG2 1 
ATOM   731  N N   . HIS A 1 91  ? 75.563 15.648 -8.083  1.00 24.18 ? 91   HIS A N   1 
ATOM   732  C CA  . HIS A 1 91  ? 75.725 14.220 -8.324  1.00 28.63 ? 91   HIS A CA  1 
ATOM   733  C C   . HIS A 1 91  ? 76.702 13.616 -7.316  1.00 25.72 ? 91   HIS A C   1 
ATOM   734  O O   . HIS A 1 91  ? 77.737 14.207 -6.998  1.00 23.52 ? 91   HIS A O   1 
ATOM   735  C CB  . HIS A 1 91  ? 76.222 13.953 -9.745  1.00 30.72 ? 91   HIS A CB  1 
ATOM   736  C CG  . HIS A 1 91  ? 76.626 12.528 -9.966  1.00 36.38 ? 91   HIS A CG  1 
ATOM   737  N ND1 . HIS A 1 91  ? 75.711 11.530 -10.235 1.00 40.63 ? 91   HIS A ND1 1 
ATOM   738  C CD2 . HIS A 1 91  ? 77.838 11.923 -9.916  1.00 38.96 ? 91   HIS A CD2 1 
ATOM   739  C CE1 . HIS A 1 91  ? 76.345 10.376 -10.359 1.00 38.04 ? 91   HIS A CE1 1 
ATOM   740  N NE2 . HIS A 1 91  ? 77.635 10.586 -10.166 1.00 40.16 ? 91   HIS A NE2 1 
ATOM   741  N N   . GLY A 1 92  ? 76.351 12.439 -6.801  1.00 25.25 ? 92   GLY A N   1 
ATOM   742  C CA  . GLY A 1 92  ? 77.165 11.758 -5.818  1.00 28.26 ? 92   GLY A CA  1 
ATOM   743  C C   . GLY A 1 92  ? 77.069 12.300 -4.410  1.00 31.17 ? 92   GLY A C   1 
ATOM   744  O O   . GLY A 1 92  ? 77.747 11.778 -3.517  1.00 35.40 ? 92   GLY A O   1 
ATOM   745  N N   . ILE A 1 93  ? 76.263 13.328 -4.173  1.00 29.72 ? 93   ILE A N   1 
ATOM   746  C CA  . ILE A 1 93  ? 76.059 13.875 -2.835  1.00 28.01 ? 93   ILE A CA  1 
ATOM   747  C C   . ILE A 1 93  ? 74.640 13.530 -2.412  1.00 30.71 ? 93   ILE A C   1 
ATOM   748  O O   . ILE A 1 93  ? 73.670 14.088 -2.941  1.00 29.59 ? 93   ILE A O   1 
ATOM   749  C CB  . ILE A 1 93  ? 76.317 15.386 -2.786  1.00 31.02 ? 93   ILE A CB  1 
ATOM   750  C CG1 . ILE A 1 93  ? 77.757 15.676 -3.233  1.00 30.26 ? 93   ILE A CG1 1 
ATOM   751  C CG2 . ILE A 1 93  ? 76.012 15.939 -1.386  1.00 27.86 ? 93   ILE A CG2 1 
ATOM   752  C CD1 . ILE A 1 93  ? 77.990 17.088 -3.683  1.00 31.33 ? 93   ILE A CD1 1 
ATOM   753  N N   . LYS A 1 94  ? 74.519 12.600 -1.462  1.00 32.51 ? 94   LYS A N   1 
ATOM   754  C CA  . LYS A 1 94  ? 73.206 12.077 -1.093  1.00 35.04 ? 94   LYS A CA  1 
ATOM   755  C C   . LYS A 1 94  ? 72.327 13.176 -0.502  1.00 33.05 ? 94   LYS A C   1 
ATOM   756  O O   . LYS A 1 94  ? 71.183 13.369 -0.931  1.00 36.58 ? 94   LYS A O   1 
ATOM   757  C CB  . LYS A 1 94  ? 73.372 10.914 -0.112  1.00 36.20 ? 94   LYS A CB  1 
ATOM   758  C CG  . LYS A 1 94  ? 72.215 9.918  -0.096  1.00 47.36 ? 94   LYS A CG  1 
ATOM   759  C CD  . LYS A 1 94  ? 71.039 10.391 0.761   1.00 50.01 ? 94   LYS A CD  1 
ATOM   760  C CE  . LYS A 1 94  ? 71.289 10.143 2.248   1.00 55.83 ? 94   LYS A CE  1 
ATOM   761  N NZ  . LYS A 1 94  ? 70.547 11.114 3.111   1.00 48.83 ? 94   LYS A NZ  1 
ATOM   762  N N   . ASP A 1 95  ? 72.850 13.901 0.493   1.00 35.17 ? 95   ASP A N   1 
ATOM   763  C CA  . ASP A 1 95  ? 72.190 15.065 1.084   1.00 33.81 ? 95   ASP A CA  1 
ATOM   764  C C   . ASP A 1 95  ? 72.926 16.334 0.674   1.00 28.09 ? 95   ASP A C   1 
ATOM   765  O O   . ASP A 1 95  ? 73.975 16.656 1.252   1.00 29.21 ? 95   ASP A O   1 
ATOM   766  C CB  . ASP A 1 95  ? 72.134 14.961 2.612   1.00 37.70 ? 95   ASP A CB  1 
ATOM   767  C CG  . ASP A 1 95  ? 70.976 15.760 3.207   1.00 45.67 ? 95   ASP A CG  1 
ATOM   768  O OD1 . ASP A 1 95  ? 70.594 16.787 2.600   1.00 47.05 ? 95   ASP A OD1 1 
ATOM   769  O OD2 . ASP A 1 95  ? 70.475 15.384 4.293   1.00 50.63 ? 95   ASP A OD2 1 
ATOM   770  N N   . PRO A 1 96  ? 72.415 17.094 -0.292  1.00 28.88 ? 96   PRO A N   1 
ATOM   771  C CA  . PRO A 1 96  ? 73.138 18.270 -0.799  1.00 27.90 ? 96   PRO A CA  1 
ATOM   772  C C   . PRO A 1 96  ? 72.877 19.557 -0.031  1.00 25.23 ? 96   PRO A C   1 
ATOM   773  O O   . PRO A 1 96  ? 73.276 20.624 -0.506  1.00 24.80 ? 96   PRO A O   1 
ATOM   774  C CB  . PRO A 1 96  ? 72.590 18.386 -2.228  1.00 28.41 ? 96   PRO A CB  1 
ATOM   775  C CG  . PRO A 1 96  ? 71.127 17.984 -2.054  1.00 27.15 ? 96   PRO A CG  1 
ATOM   776  C CD  . PRO A 1 96  ? 71.149 16.867 -1.018  1.00 30.56 ? 96   PRO A CD  1 
ATOM   777  N N   . SER A 1 97  ? 72.221 19.485 1.127   1.00 27.42 ? 97   SER A N   1 
ATOM   778  C CA  . SER A 1 97  ? 71.840 20.705 1.831   1.00 29.97 ? 97   SER A CA  1 
ATOM   779  C C   . SER A 1 97  ? 73.054 21.546 2.218   1.00 29.93 ? 97   SER A C   1 
ATOM   780  O O   . SER A 1 97  ? 72.957 22.780 2.270   1.00 29.60 ? 97   SER A O   1 
ATOM   781  C CB  . SER A 1 97  ? 70.993 20.347 3.053   1.00 35.78 ? 97   SER A CB  1 
ATOM   782  O OG  . SER A 1 97  ? 71.814 20.053 4.162   1.00 41.78 ? 97   SER A OG  1 
ATOM   783  N N   . GLN A 1 98  ? 74.212 20.917 2.442   1.00 23.60 ? 98   GLN A N   1 
ATOM   784  C CA  . GLN A 1 98  ? 75.407 21.676 2.802   1.00 29.05 ? 98   GLN A CA  1 
ATOM   785  C C   . GLN A 1 98  ? 76.060 22.377 1.615   1.00 27.07 ? 98   GLN A C   1 
ATOM   786  O O   . GLN A 1 98  ? 76.964 23.191 1.822   1.00 26.74 ? 98   GLN A O   1 
ATOM   787  C CB  . GLN A 1 98  ? 76.423 20.754 3.488   1.00 32.95 ? 98   GLN A CB  1 
ATOM   788  C CG  . GLN A 1 98  ? 76.677 21.087 4.948   1.00 42.29 ? 98   GLN A CG  1 
ATOM   789  C CD  . GLN A 1 98  ? 77.506 20.026 5.656   1.00 49.49 ? 98   GLN A CD  1 
ATOM   790  O OE1 . GLN A 1 98  ? 78.510 19.542 5.122   1.00 53.21 ? 98   GLN A OE1 1 
ATOM   791  N NE2 . GLN A 1 98  ? 77.096 19.669 6.870   1.00 42.28 ? 98   GLN A NE2 1 
ATOM   792  N N   . ILE A 1 99  ? 75.645 22.094 0.381   1.00 22.02 ? 99   ILE A N   1 
ATOM   793  C CA  . ILE A 1 99  ? 76.179 22.820 -0.763  1.00 20.86 ? 99   ILE A CA  1 
ATOM   794  C C   . ILE A 1 99  ? 75.113 23.680 -1.445  1.00 20.86 ? 99   ILE A C   1 
ATOM   795  O O   . ILE A 1 99  ? 75.372 24.255 -2.508  1.00 18.23 ? 99   ILE A O   1 
ATOM   796  C CB  . ILE A 1 99  ? 76.853 21.873 -1.765  1.00 23.53 ? 99   ILE A CB  1 
ATOM   797  C CG1 . ILE A 1 99  ? 75.839 20.896 -2.356  1.00 22.47 ? 99   ILE A CG1 1 
ATOM   798  C CG2 . ILE A 1 99  ? 78.000 21.113 -1.091  1.00 27.13 ? 99   ILE A CG2 1 
ATOM   799  C CD1 . ILE A 1 99  ? 76.281 20.358 -3.697  1.00 26.18 ? 99   ILE A CD1 1 
ATOM   800  N N   . ALA A 1 100 ? 73.918 23.777 -0.867  1.00 16.36 ? 100  ALA A N   1 
ATOM   801  C CA  . ALA A 1 100 ? 72.944 24.760 -1.323  1.00 19.84 ? 100  ALA A CA  1 
ATOM   802  C C   . ALA A 1 100 ? 73.436 26.161 -0.984  1.00 18.05 ? 100  ALA A C   1 
ATOM   803  O O   . ALA A 1 100 ? 74.134 26.366 0.005   1.00 17.54 ? 100  ALA A O   1 
ATOM   804  C CB  . ALA A 1 100 ? 71.585 24.507 -0.671  1.00 15.82 ? 100  ALA A CB  1 
ATOM   805  N N   . ASP A 1 101 ? 73.096 27.132 -1.824  1.00 14.62 ? 101  ASP A N   1 
ATOM   806  C CA  . ASP A 1 101 ? 73.420 28.528 -1.522  1.00 13.21 ? 101  ASP A CA  1 
ATOM   807  C C   . ASP A 1 101 ? 72.323 29.068 -0.601  1.00 14.78 ? 101  ASP A C   1 
ATOM   808  O O   . ASP A 1 101 ? 71.259 29.491 -1.059  1.00 11.39 ? 101  ASP A O   1 
ATOM   809  C CB  . ASP A 1 101 ? 73.544 29.339 -2.810  1.00 13.91 ? 101  ASP A CB  1 
ATOM   810  C CG  . ASP A 1 101 ? 74.039 30.766 -2.578  1.00 17.24 ? 101  ASP A CG  1 
ATOM   811  O OD1 . ASP A 1 101 ? 73.918 31.275 -1.448  1.00 14.09 ? 101  ASP A OD1 1 
ATOM   812  O OD2 . ASP A 1 101 ? 74.548 31.386 -3.536  1.00 16.53 ? 101  ASP A OD2 1 
ATOM   813  N N   . MET A 1 102 ? 72.576 29.052 0.716   1.00 12.65 ? 102  MET A N   1 
ATOM   814  C CA  . MET A 1 102 ? 71.591 29.531 1.694   1.00 13.11 ? 102  MET A CA  1 
ATOM   815  C C   . MET A 1 102 ? 71.315 31.031 1.617   1.00 14.88 ? 102  MET A C   1 
ATOM   816  O O   . MET A 1 102 ? 70.213 31.457 1.985   1.00 14.26 ? 102  MET A O   1 
ATOM   817  C CB  . MET A 1 102 ? 72.010 29.112 3.112   1.00 16.50 ? 102  MET A CB  1 
ATOM   818  C CG  . MET A 1 102 ? 71.994 27.598 3.313   1.00 13.36 ? 102  MET A CG  1 
ATOM   819  S SD  . MET A 1 102 ? 70.347 26.945 2.869   1.00 17.90 ? 102  MET A SD  1 
ATOM   820  C CE  . MET A 1 102 ? 69.287 28.016 3.850   1.00 16.10 ? 102  MET A CE  1 
ATOM   821  N N   . LYS A 1 103 ? 72.265 31.854 1.163   1.00 12.49 ? 103  LYS A N   1 
ATOM   822  C CA  . LYS A 1 103 ? 71.921 33.253 0.900   1.00 13.97 ? 103  LYS A CA  1 
ATOM   823  C C   . LYS A 1 103 ? 70.797 33.343 -0.135  1.00 15.53 ? 103  LYS A C   1 
ATOM   824  O O   . LYS A 1 103 ? 69.885 34.171 -0.010  1.00 12.67 ? 103  LYS A O   1 
ATOM   825  C CB  . LYS A 1 103 ? 73.151 34.022 0.416   1.00 17.41 ? 103  LYS A CB  1 
ATOM   826  C CG  . LYS A 1 103 ? 74.126 34.490 1.498   1.00 22.63 ? 103  LYS A CG  1 
ATOM   827  C CD  . LYS A 1 103 ? 73.482 34.502 2.872   1.00 34.97 ? 103  LYS A CD  1 
ATOM   828  C CE  . LYS A 1 103 ? 74.204 35.445 3.829   1.00 40.39 ? 103  LYS A CE  1 
ATOM   829  N NZ  . LYS A 1 103 ? 73.325 35.802 4.988   1.00 41.68 ? 103  LYS A NZ  1 
ATOM   830  N N   . VAL A 1 104 ? 70.848 32.490 -1.163  1.00 10.69 ? 104  VAL A N   1 
ATOM   831  C CA  . VAL A 1 104 ? 69.785 32.464 -2.164  1.00 10.16 ? 104  VAL A CA  1 
ATOM   832  C C   . VAL A 1 104 ? 68.480 31.942 -1.563  1.00 11.40 ? 104  VAL A C   1 
ATOM   833  O O   . VAL A 1 104 ? 67.405 32.494 -1.817  1.00 10.16 ? 104  VAL A O   1 
ATOM   834  C CB  . VAL A 1 104 ? 70.230 31.631 -3.382  1.00 11.00 ? 104  VAL A CB  1 
ATOM   835  C CG1 . VAL A 1 104 ? 69.052 31.375 -4.281  1.00 10.04 ? 104  VAL A CG1 1 
ATOM   836  C CG2 . VAL A 1 104 ? 71.329 32.368 -4.146  1.00 10.12 ? 104  VAL A CG2 1 
ATOM   837  N N   . VAL A 1 105 ? 68.543 30.875 -0.762  1.00 10.29 ? 105  VAL A N   1 
ATOM   838  C CA  . VAL A 1 105 ? 67.324 30.336 -0.155  1.00 11.75 ? 105  VAL A CA  1 
ATOM   839  C C   . VAL A 1 105 ? 66.689 31.365 0.778   1.00 11.31 ? 105  VAL A C   1 
ATOM   840  O O   . VAL A 1 105 ? 65.473 31.592 0.740   1.00 10.86 ? 105  VAL A O   1 
ATOM   841  C CB  . VAL A 1 105 ? 67.623 29.019 0.584   1.00 11.49 ? 105  VAL A CB  1 
ATOM   842  C CG1 . VAL A 1 105 ? 66.391 28.581 1.406   1.00 11.04 ? 105  VAL A CG1 1 
ATOM   843  C CG2 . VAL A 1 105 ? 68.049 27.925 -0.417  1.00 10.27 ? 105  VAL A CG2 1 
ATOM   844  N N   . GLU A 1 106 ? 67.502 32.006 1.624   1.00 10.64 ? 106  GLU A N   1 
ATOM   845  C CA  . GLU A 1 106 ? 66.988 33.088 2.466   1.00 11.34 ? 106  GLU A CA  1 
ATOM   846  C C   . GLU A 1 106 ? 66.340 34.194 1.640   1.00 11.87 ? 106  GLU A C   1 
ATOM   847  O O   . GLU A 1 106 ? 65.303 34.739 2.034   1.00 11.00 ? 106  GLU A O   1 
ATOM   848  C CB  . GLU A 1 106 ? 68.099 33.665 3.351   1.00 13.34 ? 106  GLU A CB  1 
ATOM   849  C CG  . GLU A 1 106 ? 68.707 32.657 4.315   1.00 17.98 ? 106  GLU A CG  1 
ATOM   850  C CD  . GLU A 1 106 ? 70.142 32.974 4.731   1.00 24.86 ? 106  GLU A CD  1 
ATOM   851  O OE1 . GLU A 1 106 ? 70.572 34.149 4.635   1.00 24.73 ? 106  GLU A OE1 1 
ATOM   852  O OE2 . GLU A 1 106 ? 70.822 32.028 5.191   1.00 26.07 ? 106  GLU A OE2 1 
ATOM   853  N N   . HIS A 1 107 ? 66.942 34.560 0.510   1.00 12.80 ? 107  HIS A N   1 
ATOM   854  C CA  . HIS A 1 107 ? 66.354 35.621 -0.300  1.00 10.68 ? 107  HIS A CA  1 
ATOM   855  C C   . HIS A 1 107 ? 64.978 35.216 -0.818  1.00 12.44 ? 107  HIS A C   1 
ATOM   856  O O   . HIS A 1 107 ? 64.032 36.001 -0.749  1.00 9.83  ? 107  HIS A O   1 
ATOM   857  C CB  . HIS A 1 107 ? 67.279 35.984 -1.460  1.00 13.57 ? 107  HIS A CB  1 
ATOM   858  C CG  . HIS A 1 107 ? 66.884 37.243 -2.163  1.00 14.52 ? 107  HIS A CG  1 
ATOM   859  N ND1 . HIS A 1 107 ? 67.183 38.495 -1.668  1.00 14.63 ? 107  HIS A ND1 1 
ATOM   860  C CD2 . HIS A 1 107 ? 66.187 37.446 -3.308  1.00 14.99 ? 107  HIS A CD2 1 
ATOM   861  C CE1 . HIS A 1 107 ? 66.706 39.417 -2.489  1.00 19.49 ? 107  HIS A CE1 1 
ATOM   862  N NE2 . HIS A 1 107 ? 66.100 38.807 -3.494  1.00 18.77 ? 107  HIS A NE2 1 
ATOM   863  N N   . TYR A 1 108 ? 64.846 33.986 -1.330  1.00 11.92 ? 108  TYR A N   1 
ATOM   864  C CA  . TYR A 1 108 ? 63.542 33.534 -1.811  1.00 10.58 ? 108  TYR A CA  1 
ATOM   865  C C   . TYR A 1 108 ? 62.521 33.489 -0.679  1.00 10.99 ? 108  TYR A C   1 
ATOM   866  O O   . TYR A 1 108 ? 61.351 33.843 -0.875  1.00 10.39 ? 108  TYR A O   1 
ATOM   867  C CB  . TYR A 1 108 ? 63.671 32.161 -2.478  1.00 8.81  ? 108  TYR A CB  1 
ATOM   868  C CG  . TYR A 1 108 ? 64.123 32.195 -3.938  1.00 10.09 ? 108  TYR A CG  1 
ATOM   869  C CD1 . TYR A 1 108 ? 63.504 33.027 -4.867  1.00 8.88  ? 108  TYR A CD1 1 
ATOM   870  C CD2 . TYR A 1 108 ? 65.172 31.389 -4.377  1.00 10.43 ? 108  TYR A CD2 1 
ATOM   871  C CE1 . TYR A 1 108 ? 63.906 33.041 -6.208  1.00 8.90  ? 108  TYR A CE1 1 
ATOM   872  C CE2 . TYR A 1 108 ? 65.588 31.398 -5.720  1.00 10.42 ? 108  TYR A CE2 1 
ATOM   873  C CZ  . TYR A 1 108 ? 64.947 32.224 -6.624  1.00 9.13  ? 108  TYR A CZ  1 
ATOM   874  O OH  . TYR A 1 108 ? 65.362 32.233 -7.942  1.00 9.60  ? 108  TYR A OH  1 
ATOM   875  N N   . LYS A 1 109 ? 62.939 33.067 0.521   1.00 8.50  ? 109  LYS A N   1 
ATOM   876  C CA  . LYS A 1 109 ? 62.011 33.090 1.653   1.00 9.52  ? 109  LYS A CA  1 
ATOM   877  C C   . LYS A 1 109 ? 61.574 34.516 1.986   1.00 10.94 ? 109  LYS A C   1 
ATOM   878  O O   . LYS A 1 109 ? 60.423 34.735 2.379   1.00 10.90 ? 109  LYS A O   1 
ATOM   879  C CB  . LYS A 1 109 ? 62.648 32.409 2.867   1.00 11.03 ? 109  LYS A CB  1 
ATOM   880  C CG  . LYS A 1 109 ? 62.750 30.877 2.761   1.00 10.68 ? 109  LYS A CG  1 
ATOM   881  C CD  . LYS A 1 109 ? 63.608 30.315 3.907   1.00 15.86 ? 109  LYS A CD  1 
ATOM   882  C CE  . LYS A 1 109 ? 62.860 29.701 5.108   1.00 15.97 ? 109  LYS A CE  1 
ATOM   883  N NZ  . LYS A 1 109 ? 61.633 28.896 4.835   1.00 19.12 ? 109  LYS A NZ  1 
ATOM   884  N N   . GLN A 1 110 ? 62.463 35.497 1.804   1.00 9.24  ? 110  GLN A N   1 
ATOM   885  C CA  . GLN A 1 110 ? 62.079 36.893 2.005   1.00 11.18 ? 110  GLN A CA  1 
ATOM   886  C C   . GLN A 1 110 ? 61.079 37.357 0.947   1.00 13.71 ? 110  GLN A C   1 
ATOM   887  O O   . GLN A 1 110 ? 60.150 38.111 1.257   1.00 11.47 ? 110  GLN A O   1 
ATOM   888  C CB  . GLN A 1 110 ? 63.326 37.782 1.999   1.00 11.88 ? 110  GLN A CB  1 
ATOM   889  C CG  . GLN A 1 110 ? 64.157 37.653 3.288   1.00 12.83 ? 110  GLN A CG  1 
ATOM   890  C CD  . GLN A 1 110 ? 65.631 37.996 3.107   1.00 20.50 ? 110  GLN A CD  1 
ATOM   891  O OE1 . GLN A 1 110 ? 66.035 38.594 2.101   1.00 14.12 ? 110  GLN A OE1 1 
ATOM   892  N NE2 . GLN A 1 110 ? 66.447 37.621 4.095   1.00 16.47 ? 110  GLN A NE2 1 
ATOM   893  N N   . ILE A 1 111 ? 61.262 36.932 -0.306  1.00 11.69 ? 111  ILE A N   1 
ATOM   894  C CA  . ILE A 1 111 ? 60.298 37.253 -1.359  1.00 10.45 ? 111  ILE A CA  1 
ATOM   895  C C   . ILE A 1 111 ? 58.939 36.634 -1.043  1.00 11.07 ? 111  ILE A C   1 
ATOM   896  O O   . ILE A 1 111 ? 57.897 37.296 -1.141  1.00 9.34  ? 111  ILE A O   1 
ATOM   897  C CB  . ILE A 1 111 ? 60.826 36.783 -2.731  1.00 9.97  ? 111  ILE A CB  1 
ATOM   898  C CG1 . ILE A 1 111 ? 62.011 37.642 -3.179  1.00 10.88 ? 111  ILE A CG1 1 
ATOM   899  C CG2 . ILE A 1 111 ? 59.711 36.841 -3.784  1.00 10.34 ? 111  ILE A CG2 1 
ATOM   900  C CD1 . ILE A 1 111 ? 62.621 37.208 -4.524  1.00 9.73  ? 111  ILE A CD1 1 
ATOM   901  N N   . ILE A 1 112 ? 58.931 35.353 -0.650  1.00 8.11  ? 112  ILE A N   1 
ATOM   902  C CA  . ILE A 1 112 ? 57.682 34.665 -0.313  1.00 8.87  ? 112  ILE A CA  1 
ATOM   903  C C   . ILE A 1 112 ? 56.954 35.370 0.835   1.00 10.42 ? 112  ILE A C   1 
ATOM   904  O O   . ILE A 1 112 ? 55.745 35.627 0.760   1.00 9.49  ? 112  ILE A O   1 
ATOM   905  C CB  . ILE A 1 112 ? 57.958 33.188 0.025   1.00 9.86  ? 112  ILE A CB  1 
ATOM   906  C CG1 . ILE A 1 112 ? 58.450 32.435 -1.223  1.00 10.30 ? 112  ILE A CG1 1 
ATOM   907  C CG2 . ILE A 1 112 ? 56.710 32.535 0.611   1.00 10.83 ? 112  ILE A CG2 1 
ATOM   908  C CD1 . ILE A 1 112 ? 59.282 31.209 -0.898  1.00 11.90 ? 112  ILE A CD1 1 
ATOM   909  N N   . GLU A 1 113 ? 57.668 35.682 1.920   1.00 10.67 ? 113  GLU A N   1 
ATOM   910  C CA  . GLU A 1 113 ? 57.010 36.321 3.064   1.00 14.60 ? 113  GLU A CA  1 
ATOM   911  C C   . GLU A 1 113 ? 56.495 37.713 2.709   1.00 12.54 ? 113  GLU A C   1 
ATOM   912  O O   . GLU A 1 113 ? 55.449 38.144 3.213   1.00 11.74 ? 113  GLU A O   1 
ATOM   913  C CB  . GLU A 1 113 ? 57.960 36.410 4.265   1.00 15.26 ? 113  GLU A CB  1 
ATOM   914  C CG  . GLU A 1 113 ? 58.382 35.054 4.871   1.00 14.09 ? 113  GLU A CG  1 
ATOM   915  C CD  . GLU A 1 113 ? 57.214 34.219 5.384   1.00 20.12 ? 113  GLU A CD  1 
ATOM   916  O OE1 . GLU A 1 113 ? 56.103 34.771 5.566   1.00 19.38 ? 113  GLU A OE1 1 
ATOM   917  O OE2 . GLU A 1 113 ? 57.411 33.001 5.599   1.00 18.91 ? 113  GLU A OE2 1 
ATOM   918  N N   . ASP A 1 114 ? 57.218 38.442 1.862   1.00 10.44 ? 114  ASP A N   1 
ATOM   919  C CA  . ASP A 1 114 ? 56.727 39.754 1.457   1.00 12.45 ? 114  ASP A CA  1 
ATOM   920  C C   . ASP A 1 114 ? 55.396 39.629 0.727   1.00 12.14 ? 114  ASP A C   1 
ATOM   921  O O   . ASP A 1 114 ? 54.435 40.339 1.046   1.00 12.27 ? 114  ASP A O   1 
ATOM   922  C CB  . ASP A 1 114 ? 57.743 40.482 0.574   1.00 10.58 ? 114  ASP A CB  1 
ATOM   923  C CG  . ASP A 1 114 ? 57.247 41.857 0.157   1.00 13.75 ? 114  ASP A CG  1 
ATOM   924  O OD1 . ASP A 1 114 ? 56.515 41.956 -0.863  1.00 12.20 ? 114  ASP A OD1 1 
ATOM   925  O OD2 . ASP A 1 114 ? 57.559 42.844 0.866   1.00 15.33 ? 114  ASP A OD2 1 
ATOM   926  N N   . ALA A 1 115 ? 55.319 38.723 -0.257  1.00 9.35  ? 115  ALA A N   1 
ATOM   927  C CA  . ALA A 1 115 ? 54.056 38.521 -0.968  1.00 11.47 ? 115  ALA A CA  1 
ATOM   928  C C   . ALA A 1 115 ? 52.936 38.132 -0.005  1.00 11.21 ? 115  ALA A C   1 
ATOM   929  O O   . ALA A 1 115 ? 51.834 38.701 -0.051  1.00 10.71 ? 115  ALA A O   1 
ATOM   930  C CB  . ALA A 1 115 ? 54.227 37.462 -2.066  1.00 7.96  ? 115  ALA A CB  1 
ATOM   931  N N   . LYS A 1 116 ? 53.203 37.170 0.887   1.00 10.04 ? 116  LYS A N   1 
ATOM   932  C CA  . LYS A 1 116 ? 52.190 36.745 1.855   1.00 13.91 ? 116  LYS A CA  1 
ATOM   933  C C   . LYS A 1 116 ? 51.730 37.889 2.753   1.00 14.95 ? 116  LYS A C   1 
ATOM   934  O O   . LYS A 1 116 ? 50.555 37.942 3.135   1.00 13.93 ? 116  LYS A O   1 
ATOM   935  C CB  . LYS A 1 116 ? 52.722 35.599 2.718   1.00 16.31 ? 116  LYS A CB  1 
ATOM   936  C CG  . LYS A 1 116 ? 52.911 34.267 1.981   1.00 14.86 ? 116  LYS A CG  1 
ATOM   937  C CD  . LYS A 1 116 ? 53.500 33.198 2.914   1.00 18.03 ? 116  LYS A CD  1 
ATOM   938  C CE  . LYS A 1 116 ? 52.457 32.603 3.851   1.00 24.94 ? 116  LYS A CE  1 
ATOM   939  N NZ  . LYS A 1 116 ? 51.805 31.408 3.223   1.00 26.58 ? 116  LYS A NZ  1 
ATOM   940  N N   . SER A 1 117 ? 52.632 38.804 3.110   1.00 12.35 ? 117  SER A N   1 
ATOM   941  C CA  . SER A 1 117 ? 52.247 39.909 3.982   1.00 17.01 ? 117  SER A CA  1 
ATOM   942  C C   . SER A 1 117 ? 51.315 40.891 3.287   1.00 18.19 ? 117  SER A C   1 
ATOM   943  O O   . SER A 1 117 ? 50.674 41.700 3.966   1.00 17.24 ? 117  SER A O   1 
ATOM   944  C CB  . SER A 1 117 ? 53.484 40.649 4.483   1.00 17.57 ? 117  SER A CB  1 
ATOM   945  O OG  . SER A 1 117 ? 53.997 41.521 3.484   1.00 15.92 ? 117  SER A OG  1 
ATOM   946  N N   . ARG A 1 118 ? 51.220 40.833 1.959   1.00 16.66 ? 118  ARG A N   1 
ATOM   947  C CA  . ARG A 1 118 ? 50.317 41.682 1.202   1.00 16.01 ? 118  ARG A CA  1 
ATOM   948  C C   . ARG A 1 118 ? 49.035 40.953 0.808   1.00 16.36 ? 118  ARG A C   1 
ATOM   949  O O   . ARG A 1 118 ? 48.287 41.445 -0.040  1.00 18.81 ? 118  ARG A O   1 
ATOM   950  C CB  . ARG A 1 118 ? 51.042 42.233 -0.033  1.00 15.69 ? 118  ARG A CB  1 
ATOM   951  C CG  . ARG A 1 118 ? 52.315 43.012 0.335   1.00 16.49 ? 118  ARG A CG  1 
ATOM   952  C CD  . ARG A 1 118 ? 53.116 43.538 -0.874  1.00 17.78 ? 118  ARG A CD  1 
ATOM   953  N NE  . ARG A 1 118 ? 54.452 43.967 -0.461  1.00 15.38 ? 118  ARG A NE  1 
ATOM   954  C CZ  . ARG A 1 118 ? 54.731 45.141 0.099   1.00 23.07 ? 118  ARG A CZ  1 
ATOM   955  N NH1 . ARG A 1 118 ? 53.812 46.094 0.213   1.00 17.30 ? 118  ARG A NH1 1 
ATOM   956  N NH2 . ARG A 1 118 ? 55.954 45.357 0.577   1.00 19.90 ? 118  ARG A NH2 1 
ATOM   957  N N   . GLY A 1 119 ? 48.759 39.799 1.411   1.00 15.61 ? 119  GLY A N   1 
ATOM   958  C CA  . GLY A 1 119 ? 47.542 39.066 1.135   1.00 15.06 ? 119  GLY A CA  1 
ATOM   959  C C   . GLY A 1 119 ? 47.577 38.190 -0.101  1.00 17.30 ? 119  GLY A C   1 
ATOM   960  O O   . GLY A 1 119 ? 46.518 37.774 -0.577  1.00 15.65 ? 119  GLY A O   1 
ATOM   961  N N   . LEU A 1 120 ? 48.751 37.908 -0.650  1.00 11.44 ? 120  LEU A N   1 
ATOM   962  C CA  . LEU A 1 120 ? 48.878 37.013 -1.791  1.00 13.33 ? 120  LEU A CA  1 
ATOM   963  C C   . LEU A 1 120 ? 49.244 35.622 -1.281  1.00 12.19 ? 120  LEU A C   1 
ATOM   964  O O   . LEU A 1 120 ? 50.240 35.470 -0.568  1.00 13.03 ? 120  LEU A O   1 
ATOM   965  C CB  . LEU A 1 120 ? 49.945 37.524 -2.762  1.00 12.20 ? 120  LEU A CB  1 
ATOM   966  C CG  . LEU A 1 120 ? 49.788 38.978 -3.245  1.00 13.44 ? 120  LEU A CG  1 
ATOM   967  C CD1 . LEU A 1 120 ? 51.047 39.443 -3.973  1.00 11.92 ? 120  LEU A CD1 1 
ATOM   968  C CD2 . LEU A 1 120 ? 48.573 39.136 -4.132  1.00 10.91 ? 120  LEU A CD2 1 
ATOM   969  N N   . LYS A 1 121 ? 48.432 34.620 -1.620  1.00 9.95  ? 121  LYS A N   1 
ATOM   970  C CA  . LYS A 1 121 ? 48.891 33.239 -1.520  1.00 14.74 ? 121  LYS A CA  1 
ATOM   971  C C   . LYS A 1 121 ? 50.033 33.025 -2.505  1.00 17.47 ? 121  LYS A C   1 
ATOM   972  O O   . LYS A 1 121 ? 50.071 33.644 -3.569  1.00 14.10 ? 121  LYS A O   1 
ATOM   973  C CB  . LYS A 1 121 ? 47.753 32.271 -1.830  1.00 14.29 ? 121  LYS A CB  1 
ATOM   974  C CG  . LYS A 1 121 ? 46.683 32.223 -0.766  1.00 20.97 ? 121  LYS A CG  1 
ATOM   975  C CD  . LYS A 1 121 ? 45.658 31.164 -1.105  1.00 24.85 ? 121  LYS A CD  1 
ATOM   976  C CE  . LYS A 1 121 ? 44.422 31.321 -0.231  1.00 36.05 ? 121  LYS A CE  1 
ATOM   977  N NZ  . LYS A 1 121 ? 44.795 31.093 1.189   1.00 36.68 ? 121  LYS A NZ  1 
ATOM   978  N N   . VAL A 1 122 ? 50.987 32.163 -2.159  1.00 10.90 ? 122  VAL A N   1 
ATOM   979  C CA  . VAL A 1 122 ? 52.185 32.032 -2.980  1.00 11.03 ? 122  VAL A CA  1 
ATOM   980  C C   . VAL A 1 122 ? 52.307 30.592 -3.455  1.00 13.05 ? 122  VAL A C   1 
ATOM   981  O O   . VAL A 1 122 ? 52.400 29.663 -2.640  1.00 11.91 ? 122  VAL A O   1 
ATOM   982  C CB  . VAL A 1 122 ? 53.454 32.485 -2.240  1.00 14.30 ? 122  VAL A CB  1 
ATOM   983  C CG1 . VAL A 1 122 ? 54.688 32.281 -3.118  1.00 11.75 ? 122  VAL A CG1 1 
ATOM   984  C CG2 . VAL A 1 122 ? 53.335 33.959 -1.838  1.00 12.89 ? 122  VAL A CG2 1 
ATOM   985  N N   . ILE A 1 123 ? 52.299 30.417 -4.771  1.00 10.39 ? 123  ILE A N   1 
ATOM   986  C CA  . ILE A 1 123 ? 52.599 29.147 -5.418  1.00 10.57 ? 123  ILE A CA  1 
ATOM   987  C C   . ILE A 1 123 ? 54.038 29.234 -5.900  1.00 8.88  ? 123  ILE A C   1 
ATOM   988  O O   . ILE A 1 123 ? 54.401 30.176 -6.615  1.00 11.60 ? 123  ILE A O   1 
ATOM   989  C CB  . ILE A 1 123 ? 51.636 28.868 -6.584  1.00 12.44 ? 123  ILE A CB  1 
ATOM   990  C CG1 . ILE A 1 123 ? 50.178 28.848 -6.094  1.00 10.62 ? 123  ILE A CG1 1 
ATOM   991  C CG2 . ILE A 1 123 ? 52.005 27.564 -7.299  1.00 11.04 ? 123  ILE A CG2 1 
ATOM   992  C CD1 . ILE A 1 123 ? 49.169 28.720 -7.244  1.00 10.61 ? 123  ILE A CD1 1 
ATOM   993  N N   . VAL A 1 124 ? 54.875 28.296 -5.470  1.00 7.17  ? 124  VAL A N   1 
ATOM   994  C CA  . VAL A 1 124 ? 56.281 28.270 -5.859  1.00 9.51  ? 124  VAL A CA  1 
ATOM   995  C C   . VAL A 1 124 ? 56.477 27.134 -6.851  1.00 10.44 ? 124  VAL A C   1 
ATOM   996  O O   . VAL A 1 124 ? 56.193 25.967 -6.543  1.00 9.19  ? 124  VAL A O   1 
ATOM   997  C CB  . VAL A 1 124 ? 57.207 28.126 -4.645  1.00 11.38 ? 124  VAL A CB  1 
ATOM   998  C CG1 . VAL A 1 124 ? 58.606 27.707 -5.099  1.00 8.90  ? 124  VAL A CG1 1 
ATOM   999  C CG2 . VAL A 1 124 ? 57.281 29.475 -3.924  1.00 9.23  ? 124  VAL A CG2 1 
ATOM   1000 N N   . ASN A 1 125 ? 56.940 27.485 -8.045  1.00 8.49  ? 125  ASN A N   1 
ATOM   1001 C CA  . ASN A 1 125 ? 57.187 26.530 -9.117  1.00 10.07 ? 125  ASN A CA  1 
ATOM   1002 C C   . ASN A 1 125 ? 58.676 26.218 -9.167  1.00 8.31  ? 125  ASN A C   1 
ATOM   1003 O O   . ASN A 1 125 ? 59.502 27.131 -9.246  1.00 8.91  ? 125  ASN A O   1 
ATOM   1004 C CB  . ASN A 1 125 ? 56.724 27.090 -10.459 1.00 9.89  ? 125  ASN A CB  1 
ATOM   1005 C CG  . ASN A 1 125 ? 57.116 26.198 -11.613 1.00 10.37 ? 125  ASN A CG  1 
ATOM   1006 O OD1 . ASN A 1 125 ? 56.774 25.014 -11.621 1.00 8.19  ? 125  ASN A OD1 1 
ATOM   1007 N ND2 . ASN A 1 125 ? 57.850 26.748 -12.591 1.00 8.33  ? 125  ASN A ND2 1 
ATOM   1008 N N   . LEU A 1 126 ? 59.014 24.929 -9.121  1.00 7.96  ? 126  LEU A N   1 
ATOM   1009 C CA  . LEU A 1 126 ? 60.407 24.541 -8.941  1.00 8.70  ? 126  LEU A CA  1 
ATOM   1010 C C   . LEU A 1 126 ? 61.229 24.685 -10.210 1.00 7.69  ? 126  LEU A C   1 
ATOM   1011 O O   . LEU A 1 126 ? 62.442 24.911 -10.129 1.00 10.65 ? 126  LEU A O   1 
ATOM   1012 C CB  . LEU A 1 126 ? 60.507 23.091 -8.458  1.00 10.51 ? 126  LEU A CB  1 
ATOM   1013 C CG  . LEU A 1 126 ? 59.839 22.687 -7.134  1.00 14.33 ? 126  LEU A CG  1 
ATOM   1014 C CD1 . LEU A 1 126 ? 60.294 21.289 -6.714  1.00 12.23 ? 126  LEU A CD1 1 
ATOM   1015 C CD2 . LEU A 1 126 ? 60.103 23.670 -6.041  1.00 11.00 ? 126  LEU A CD2 1 
ATOM   1016 N N   . ASN A 1 127 ? 60.619 24.538 -11.381 1.00 7.67  ? 127  ASN A N   1 
ATOM   1017 C CA  . ASN A 1 127 ? 61.396 24.584 -12.614 1.00 9.07  ? 127  ASN A CA  1 
ATOM   1018 C C   . ASN A 1 127 ? 60.589 25.252 -13.718 1.00 8.07  ? 127  ASN A C   1 
ATOM   1019 O O   . ASN A 1 127 ? 59.419 24.917 -13.940 1.00 8.94  ? 127  ASN A O   1 
ATOM   1020 C CB  . ASN A 1 127 ? 61.834 23.173 -13.034 1.00 9.64  ? 127  ASN A CB  1 
ATOM   1021 C CG  . ASN A 1 127 ? 62.862 23.192 -14.144 1.00 11.58 ? 127  ASN A CG  1 
ATOM   1022 O OD1 . ASN A 1 127 ? 63.980 23.719 -13.977 1.00 12.64 ? 127  ASN A OD1 1 
ATOM   1023 N ND2 . ASN A 1 127 ? 62.509 22.607 -15.279 1.00 6.96  ? 127  ASN A ND2 1 
ATOM   1024 N N   . HIS A 1 128 ? 61.216 26.201 -14.405 1.00 7.85  ? 128  HIS A N   1 
ATOM   1025 C CA  . HIS A 1 128 ? 60.553 26.968 -15.458 1.00 7.71  ? 128  HIS A CA  1 
ATOM   1026 C C   . HIS A 1 128 ? 61.575 27.119 -16.586 1.00 9.00  ? 128  HIS A C   1 
ATOM   1027 O O   . HIS A 1 128 ? 62.249 28.144 -16.695 1.00 8.50  ? 128  HIS A O   1 
ATOM   1028 C CB  . HIS A 1 128 ? 60.046 28.320 -14.939 1.00 6.79  ? 128  HIS A CB  1 
ATOM   1029 C CG  . HIS A 1 128 ? 59.068 28.990 -15.851 1.00 9.67  ? 128  HIS A CG  1 
ATOM   1030 N ND1 . HIS A 1 128 ? 57.834 29.431 -15.426 1.00 8.27  ? 128  HIS A ND1 1 
ATOM   1031 C CD2 . HIS A 1 128 ? 59.143 29.293 -17.171 1.00 8.51  ? 128  HIS A CD2 1 
ATOM   1032 C CE1 . HIS A 1 128 ? 57.197 29.997 -16.441 1.00 10.03 ? 128  HIS A CE1 1 
ATOM   1033 N NE2 . HIS A 1 128 ? 57.967 29.916 -17.514 1.00 9.42  ? 128  HIS A NE2 1 
ATOM   1034 N N   . PHE A 1 129 ? 61.703 26.053 -17.387 1.00 9.10  ? 129  PHE A N   1 
ATOM   1035 C CA  . PHE A 1 129 ? 62.578 25.957 -18.557 1.00 8.52  ? 129  PHE A CA  1 
ATOM   1036 C C   . PHE A 1 129 ? 64.055 25.871 -18.185 1.00 10.60 ? 129  PHE A C   1 
ATOM   1037 O O   . PHE A 1 129 ? 64.719 24.900 -18.562 1.00 13.18 ? 129  PHE A O   1 
ATOM   1038 C CB  . PHE A 1 129 ? 62.367 27.123 -19.546 1.00 9.08  ? 129  PHE A CB  1 
ATOM   1039 C CG  . PHE A 1 129 ? 60.959 27.226 -20.117 1.00 9.65  ? 129  PHE A CG  1 
ATOM   1040 C CD1 . PHE A 1 129 ? 59.988 26.274 -19.834 1.00 8.96  ? 129  PHE A CD1 1 
ATOM   1041 C CD2 . PHE A 1 129 ? 60.617 28.288 -20.947 1.00 9.88  ? 129  PHE A CD2 1 
ATOM   1042 C CE1 . PHE A 1 129 ? 58.689 26.382 -20.360 1.00 11.85 ? 129  PHE A CE1 1 
ATOM   1043 C CE2 . PHE A 1 129 ? 59.322 28.408 -21.477 1.00 8.42  ? 129  PHE A CE2 1 
ATOM   1044 C CZ  . PHE A 1 129 ? 58.359 27.449 -21.190 1.00 10.28 ? 129  PHE A CZ  1 
ATOM   1045 N N   . THR A 1 130 ? 64.602 26.867 -17.484 1.00 8.81  ? 130  THR A N   1 
ATOM   1046 C CA  . THR A 1 130 ? 66.053 26.919 -17.346 1.00 8.69  ? 130  THR A CA  1 
ATOM   1047 C C   . THR A 1 130 ? 66.571 25.796 -16.453 1.00 10.85 ? 130  THR A C   1 
ATOM   1048 O O   . THR A 1 130 ? 65.921 25.376 -15.488 1.00 10.80 ? 130  THR A O   1 
ATOM   1049 C CB  . THR A 1 130 ? 66.508 28.254 -16.773 1.00 11.07 ? 130  THR A CB  1 
ATOM   1050 O OG1 . THR A 1 130 ? 66.048 28.354 -15.418 1.00 9.51  ? 130  THR A OG1 1 
ATOM   1051 C CG2 . THR A 1 130 ? 65.963 29.440 -17.605 1.00 8.28  ? 130  THR A CG2 1 
ATOM   1052 N N   . LEU A 1 131 ? 67.775 25.341 -16.768 1.00 8.31  ? 131  LEU A N   1 
ATOM   1053 C CA  . LEU A 1 131 ? 68.495 24.302 -16.052 1.00 9.37  ? 131  LEU A CA  1 
ATOM   1054 C C   . LEU A 1 131 ? 69.872 24.813 -15.639 1.00 8.07  ? 131  LEU A C   1 
ATOM   1055 O O   . LEU A 1 131 ? 70.467 25.640 -16.343 1.00 9.59  ? 131  LEU A O   1 
ATOM   1056 C CB  . LEU A 1 131 ? 68.654 23.054 -16.941 1.00 7.74  ? 131  LEU A CB  1 
ATOM   1057 C CG  . LEU A 1 131 ? 67.337 22.364 -17.321 1.00 11.73 ? 131  LEU A CG  1 
ATOM   1058 C CD1 . LEU A 1 131 ? 67.561 21.290 -18.392 1.00 8.27  ? 131  LEU A CD1 1 
ATOM   1059 C CD2 . LEU A 1 131 ? 66.677 21.760 -16.076 1.00 7.77  ? 131  LEU A CD2 1 
ATOM   1060 N N   . PRO A 1 132 ? 70.404 24.342 -14.510 1.00 9.25  ? 132  PRO A N   1 
ATOM   1061 C CA  . PRO A 1 132 ? 71.791 24.665 -14.158 1.00 9.08  ? 132  PRO A CA  1 
ATOM   1062 C C   . PRO A 1 132 ? 72.738 24.323 -15.300 1.00 8.77  ? 132  PRO A C   1 
ATOM   1063 O O   . PRO A 1 132 ? 72.597 23.299 -15.962 1.00 7.75  ? 132  PRO A O   1 
ATOM   1064 C CB  . PRO A 1 132 ? 72.060 23.787 -12.930 1.00 10.34 ? 132  PRO A CB  1 
ATOM   1065 C CG  . PRO A 1 132 ? 70.706 23.568 -12.331 1.00 10.61 ? 132  PRO A CG  1 
ATOM   1066 C CD  . PRO A 1 132 ? 69.773 23.457 -13.515 1.00 10.25 ? 132  PRO A CD  1 
ATOM   1067 N N   . LEU A 1 133 ? 73.710 25.202 -15.522 1.00 8.43  ? 133  LEU A N   1 
ATOM   1068 C CA  . LEU A 1 133 ? 74.705 24.971 -16.561 1.00 12.27 ? 133  LEU A CA  1 
ATOM   1069 C C   . LEU A 1 133 ? 75.497 23.692 -16.319 1.00 12.22 ? 133  LEU A C   1 
ATOM   1070 O O   . LEU A 1 133 ? 75.940 23.058 -17.281 1.00 10.87 ? 133  LEU A O   1 
ATOM   1071 C CB  . LEU A 1 133 ? 75.640 26.180 -16.645 1.00 12.44 ? 133  LEU A CB  1 
ATOM   1072 C CG  . LEU A 1 133 ? 76.648 26.247 -17.792 1.00 20.50 ? 133  LEU A CG  1 
ATOM   1073 C CD1 . LEU A 1 133 ? 75.943 26.169 -19.141 1.00 12.74 ? 133  LEU A CD1 1 
ATOM   1074 C CD2 . LEU A 1 133 ? 77.462 27.557 -17.666 1.00 17.56 ? 133  LEU A CD2 1 
ATOM   1075 N N   . TRP A 1 134 ? 75.684 23.282 -15.053 1.00 10.17 ? 134  TRP A N   1 
ATOM   1076 C CA  . TRP A 1 134 ? 76.366 22.013 -14.814 1.00 11.01 ? 134  TRP A CA  1 
ATOM   1077 C C   . TRP A 1 134 ? 75.533 20.818 -15.260 1.00 13.60 ? 134  TRP A C   1 
ATOM   1078 O O   . TRP A 1 134 ? 76.069 19.714 -15.378 1.00 14.40 ? 134  TRP A O   1 
ATOM   1079 C CB  . TRP A 1 134 ? 76.760 21.847 -13.334 1.00 13.77 ? 134  TRP A CB  1 
ATOM   1080 C CG  . TRP A 1 134 ? 75.659 22.052 -12.271 1.00 11.70 ? 134  TRP A CG  1 
ATOM   1081 C CD1 . TRP A 1 134 ? 75.466 23.172 -11.506 1.00 13.87 ? 134  TRP A CD1 1 
ATOM   1082 C CD2 . TRP A 1 134 ? 74.678 21.092 -11.821 1.00 11.86 ? 134  TRP A CD2 1 
ATOM   1083 N NE1 . TRP A 1 134 ? 74.412 22.983 -10.631 1.00 11.60 ? 134  TRP A NE1 1 
ATOM   1084 C CE2 . TRP A 1 134 ? 73.915 21.715 -10.803 1.00 12.34 ? 134  TRP A CE2 1 
ATOM   1085 C CE3 . TRP A 1 134 ? 74.366 19.774 -12.185 1.00 13.27 ? 134  TRP A CE3 1 
ATOM   1086 C CZ2 . TRP A 1 134 ? 72.851 21.065 -10.148 1.00 10.85 ? 134  TRP A CZ2 1 
ATOM   1087 C CZ3 . TRP A 1 134 ? 73.305 19.128 -11.528 1.00 15.36 ? 134  TRP A CZ3 1 
ATOM   1088 C CH2 . TRP A 1 134 ? 72.570 19.777 -10.518 1.00 13.30 ? 134  TRP A CH2 1 
ATOM   1089 N N   . LEU A 1 135 ? 74.242 21.008 -15.503 1.00 9.91  ? 135  LEU A N   1 
ATOM   1090 C CA  . LEU A 1 135 ? 73.385 19.934 -15.986 1.00 12.96 ? 135  LEU A CA  1 
ATOM   1091 C C   . LEU A 1 135 ? 73.131 20.010 -17.489 1.00 13.61 ? 135  LEU A C   1 
ATOM   1092 O O   . LEU A 1 135 ? 72.945 18.970 -18.132 1.00 12.63 ? 135  LEU A O   1 
ATOM   1093 C CB  . LEU A 1 135 ? 72.045 19.961 -15.241 1.00 11.72 ? 135  LEU A CB  1 
ATOM   1094 C CG  . LEU A 1 135 ? 71.064 18.855 -15.629 1.00 15.49 ? 135  LEU A CG  1 
ATOM   1095 C CD1 . LEU A 1 135 ? 71.636 17.497 -15.231 1.00 20.94 ? 135  LEU A CD1 1 
ATOM   1096 C CD2 . LEU A 1 135 ? 69.689 19.073 -15.031 1.00 14.44 ? 135  LEU A CD2 1 
ATOM   1097 N N   . HIS A 1 136 ? 73.141 21.211 -18.064 1.00 10.21 ? 136  HIS A N   1 
ATOM   1098 C CA  . HIS A 1 136 ? 72.838 21.402 -19.482 1.00 9.86  ? 136  HIS A CA  1 
ATOM   1099 C C   . HIS A 1 136 ? 73.701 22.531 -20.027 1.00 10.20 ? 136  HIS A C   1 
ATOM   1100 O O   . HIS A 1 136 ? 73.521 23.691 -19.642 1.00 10.91 ? 136  HIS A O   1 
ATOM   1101 C CB  . HIS A 1 136 ? 71.358 21.725 -19.696 1.00 9.53  ? 136  HIS A CB  1 
ATOM   1102 C CG  . HIS A 1 136 ? 70.935 21.686 -21.136 1.00 11.43 ? 136  HIS A CG  1 
ATOM   1103 N ND1 . HIS A 1 136 ? 69.873 22.419 -21.622 1.00 9.68  ? 136  HIS A ND1 1 
ATOM   1104 C CD2 . HIS A 1 136 ? 71.417 20.983 -22.186 1.00 9.38  ? 136  HIS A CD2 1 
ATOM   1105 C CE1 . HIS A 1 136 ? 69.721 22.170 -22.912 1.00 10.52 ? 136  HIS A CE1 1 
ATOM   1106 N NE2 . HIS A 1 136 ? 70.647 21.302 -23.279 1.00 11.28 ? 136  HIS A NE2 1 
ATOM   1107 N N   . ASP A 1 137 ? 74.621 22.200 -20.935 1.00 11.03 ? 137  ASP A N   1 
ATOM   1108 C CA  . ASP A 1 137 ? 75.277 23.213 -21.757 1.00 9.91  ? 137  ASP A CA  1 
ATOM   1109 C C   . ASP A 1 137 ? 74.773 23.048 -23.181 1.00 10.75 ? 137  ASP A C   1 
ATOM   1110 O O   . ASP A 1 137 ? 75.269 22.183 -23.914 1.00 10.91 ? 137  ASP A O   1 
ATOM   1111 C CB  . ASP A 1 137 ? 76.803 23.081 -21.712 1.00 12.59 ? 137  ASP A CB  1 
ATOM   1112 C CG  . ASP A 1 137 ? 77.513 24.203 -22.491 1.00 15.94 ? 137  ASP A CG  1 
ATOM   1113 O OD1 . ASP A 1 137 ? 77.001 24.661 -23.545 1.00 10.69 ? 137  ASP A OD1 1 
ATOM   1114 O OD2 . ASP A 1 137 ? 78.604 24.624 -22.059 1.00 16.41 ? 137  ASP A OD2 1 
ATOM   1115 N N   . PRO A 1 138 ? 73.818 23.866 -23.630 1.00 9.22  ? 138  PRO A N   1 
ATOM   1116 C CA  . PRO A 1 138 ? 73.195 23.624 -24.934 1.00 12.35 ? 138  PRO A CA  1 
ATOM   1117 C C   . PRO A 1 138 ? 74.063 24.000 -26.112 1.00 10.38 ? 138  PRO A C   1 
ATOM   1118 O O   . PRO A 1 138 ? 73.765 23.560 -27.226 1.00 12.52 ? 138  PRO A O   1 
ATOM   1119 C CB  . PRO A 1 138 ? 71.933 24.504 -24.885 1.00 9.53  ? 138  PRO A CB  1 
ATOM   1120 C CG  . PRO A 1 138 ? 72.335 25.645 -24.029 1.00 9.06  ? 138  PRO A CG  1 
ATOM   1121 C CD  . PRO A 1 138 ? 73.261 25.060 -22.971 1.00 11.15 ? 138  PRO A CD  1 
ATOM   1122 N N   . ILE A 1 139 ? 75.115 24.791 -25.916 1.00 10.02 ? 139  ILE A N   1 
ATOM   1123 C CA  . ILE A 1 139 ? 76.024 25.073 -27.020 1.00 11.55 ? 139  ILE A CA  1 
ATOM   1124 C C   . ILE A 1 139 ? 76.953 23.889 -27.259 1.00 11.83 ? 139  ILE A C   1 
ATOM   1125 O O   . ILE A 1 139 ? 77.233 23.541 -28.408 1.00 11.13 ? 139  ILE A O   1 
ATOM   1126 C CB  . ILE A 1 139 ? 76.794 26.388 -26.762 1.00 13.86 ? 139  ILE A CB  1 
ATOM   1127 C CG1 . ILE A 1 139 ? 75.824 27.585 -26.709 1.00 10.51 ? 139  ILE A CG1 1 
ATOM   1128 C CG2 . ILE A 1 139 ? 77.873 26.629 -27.839 1.00 11.23 ? 139  ILE A CG2 1 
ATOM   1129 C CD1 . ILE A 1 139 ? 75.199 27.909 -28.062 1.00 13.87 ? 139  ILE A CD1 1 
ATOM   1130 N N   . ARG A 1 140 ? 77.434 23.240 -26.189 1.00 10.20 ? 140  ARG A N   1 
ATOM   1131 C CA  . ARG A 1 140 ? 78.193 21.999 -26.362 1.00 10.66 ? 140  ARG A CA  1 
ATOM   1132 C C   . ARG A 1 140 ? 77.347 20.928 -27.036 1.00 11.87 ? 140  ARG A C   1 
ATOM   1133 O O   . ARG A 1 140 ? 77.839 20.191 -27.902 1.00 11.86 ? 140  ARG A O   1 
ATOM   1134 C CB  . ARG A 1 140 ? 78.716 21.488 -25.013 1.00 12.74 ? 140  ARG A CB  1 
ATOM   1135 C CG  . ARG A 1 140 ? 79.706 22.415 -24.314 1.00 14.94 ? 140  ARG A CG  1 
ATOM   1136 C CD  . ARG A 1 140 ? 81.007 22.581 -25.115 1.00 18.80 ? 140  ARG A CD  1 
ATOM   1137 N NE  . ARG A 1 140 ? 81.622 21.299 -25.451 1.00 20.09 ? 140  ARG A NE  1 
ATOM   1138 C CZ  . ARG A 1 140 ? 82.658 21.157 -26.267 1.00 23.56 ? 140  ARG A CZ  1 
ATOM   1139 N NH1 . ARG A 1 140 ? 83.225 22.203 -26.852 1.00 23.12 ? 140  ARG A NH1 1 
ATOM   1140 N NH2 . ARG A 1 140 ? 83.133 19.938 -26.506 1.00 20.26 ? 140  ARG A NH2 1 
ATOM   1141 N N   . VAL A 1 141 ? 76.067 20.828 -26.655 1.00 10.16 ? 141  VAL A N   1 
ATOM   1142 C CA  . VAL A 1 141 ? 75.165 19.873 -27.295 1.00 9.94  ? 141  VAL A CA  1 
ATOM   1143 C C   . VAL A 1 141 ? 74.957 20.246 -28.759 1.00 15.08 ? 141  VAL A C   1 
ATOM   1144 O O   . VAL A 1 141 ? 75.151 19.425 -29.663 1.00 11.00 ? 141  VAL A O   1 
ATOM   1145 C CB  . VAL A 1 141 ? 73.818 19.805 -26.548 1.00 11.25 ? 141  VAL A CB  1 
ATOM   1146 C CG1 . VAL A 1 141 ? 72.827 18.984 -27.354 1.00 7.54  ? 141  VAL A CG1 1 
ATOM   1147 C CG2 . VAL A 1 141 ? 73.980 19.196 -25.137 1.00 10.21 ? 141  VAL A CG2 1 
ATOM   1148 N N   . SER A 1 142 ? 74.589 21.505 -29.004 1.00 11.60 ? 142  SER A N   1 
ATOM   1149 C CA  . SER A 1 142 ? 74.151 21.960 -30.320 1.00 15.62 ? 142  SER A CA  1 
ATOM   1150 C C   . SER A 1 142 ? 75.293 21.988 -31.330 1.00 16.49 ? 142  SER A C   1 
ATOM   1151 O O   . SER A 1 142 ? 75.147 21.525 -32.470 1.00 17.03 ? 142  SER A O   1 
ATOM   1152 C CB  . SER A 1 142 ? 73.537 23.361 -30.183 1.00 11.80 ? 142  SER A CB  1 
ATOM   1153 O OG  . SER A 1 142 ? 73.325 23.951 -31.447 1.00 28.01 ? 142  SER A OG  1 
ATOM   1154 N N   . ARG A 1 143 ? 76.427 22.556 -30.943 1.00 11.94 ? 143  ARG A N   1 
ATOM   1155 C CA  . ARG A 1 143 ? 77.471 22.876 -31.905 1.00 17.37 ? 143  ARG A CA  1 
ATOM   1156 C C   . ARG A 1 143 ? 78.635 21.889 -31.898 1.00 17.89 ? 143  ARG A C   1 
ATOM   1157 O O   . ARG A 1 143 ? 79.374 21.823 -32.887 1.00 16.66 ? 143  ARG A O   1 
ATOM   1158 C CB  . ARG A 1 143 ? 77.997 24.296 -31.642 1.00 11.80 ? 143  ARG A CB  1 
ATOM   1159 C CG  . ARG A 1 143 ? 78.883 24.865 -32.760 1.00 13.38 ? 143  ARG A CG  1 
ATOM   1160 C CD  . ARG A 1 143 ? 79.078 26.364 -32.596 1.00 12.22 ? 143  ARG A CD  1 
ATOM   1161 N NE  . ARG A 1 143 ? 77.790 27.051 -32.622 1.00 12.72 ? 143  ARG A NE  1 
ATOM   1162 C CZ  . ARG A 1 143 ? 77.457 28.061 -31.825 1.00 12.73 ? 143  ARG A CZ  1 
ATOM   1163 N NH1 . ARG A 1 143 ? 78.340 28.617 -31.007 1.00 10.47 ? 143  ARG A NH1 1 
ATOM   1164 N NH2 . ARG A 1 143 ? 76.207 28.521 -31.848 1.00 11.88 ? 143  ARG A NH2 1 
ATOM   1165 N N   . PHE A 1 144 ? 78.825 21.125 -30.824 1.00 13.92 ? 144  PHE A N   1 
ATOM   1166 C CA  . PHE A 1 144 ? 79.989 20.249 -30.723 1.00 16.07 ? 144  PHE A CA  1 
ATOM   1167 C C   . PHE A 1 144 ? 79.615 18.799 -30.476 1.00 15.92 ? 144  PHE A C   1 
ATOM   1168 O O   . PHE A 1 144 ? 80.502 17.987 -30.199 1.00 17.37 ? 144  PHE A O   1 
ATOM   1169 C CB  . PHE A 1 144 ? 80.927 20.755 -29.627 1.00 18.02 ? 144  PHE A CB  1 
ATOM   1170 C CG  . PHE A 1 144 ? 81.387 22.161 -29.864 1.00 20.36 ? 144  PHE A CG  1 
ATOM   1171 C CD1 . PHE A 1 144 ? 82.361 22.430 -30.815 1.00 27.95 ? 144  PHE A CD1 1 
ATOM   1172 C CD2 . PHE A 1 144 ? 80.811 23.216 -29.176 1.00 17.61 ? 144  PHE A CD2 1 
ATOM   1173 C CE1 . PHE A 1 144 ? 82.769 23.731 -31.063 1.00 28.94 ? 144  PHE A CE1 1 
ATOM   1174 C CE2 . PHE A 1 144 ? 81.216 24.518 -29.413 1.00 20.18 ? 144  PHE A CE2 1 
ATOM   1175 C CZ  . PHE A 1 144 ? 82.195 24.778 -30.360 1.00 27.01 ? 144  PHE A CZ  1 
ATOM   1176 N N   . ASN A 1 145 ? 78.329 18.459 -30.584 1.00 11.77 ? 145  ASN A N   1 
ATOM   1177 C CA  . ASN A 1 145 ? 77.835 17.093 -30.418 1.00 17.85 ? 145  ASN A CA  1 
ATOM   1178 C C   . ASN A 1 145 ? 78.350 16.496 -29.109 1.00 19.28 ? 145  ASN A C   1 
ATOM   1179 O O   . ASN A 1 145 ? 78.719 15.323 -29.033 1.00 15.59 ? 145  ASN A O   1 
ATOM   1180 C CB  . ASN A 1 145 ? 78.215 16.230 -31.627 1.00 19.34 ? 145  ASN A CB  1 
ATOM   1181 C CG  . ASN A 1 145 ? 77.537 14.868 -31.614 1.00 26.00 ? 145  ASN A CG  1 
ATOM   1182 O OD1 . ASN A 1 145 ? 78.192 13.822 -31.583 1.00 33.28 ? 145  ASN A OD1 1 
ATOM   1183 N ND2 . ASN A 1 145 ? 76.212 14.878 -31.637 1.00 26.59 ? 145  ASN A ND2 1 
ATOM   1184 N N   . ASP A 1 146 ? 78.379 17.332 -28.070 1.00 15.87 ? 146  ASP A N   1 
ATOM   1185 C CA  . ASP A 1 146 ? 78.900 16.987 -26.748 1.00 16.44 ? 146  ASP A CA  1 
ATOM   1186 C C   . ASP A 1 146 ? 77.720 16.884 -25.785 1.00 15.84 ? 146  ASP A C   1 
ATOM   1187 O O   . ASP A 1 146 ? 77.142 17.904 -25.396 1.00 14.20 ? 146  ASP A O   1 
ATOM   1188 C CB  . ASP A 1 146 ? 79.907 18.045 -26.303 1.00 17.79 ? 146  ASP A CB  1 
ATOM   1189 C CG  . ASP A 1 146 ? 80.419 17.838 -24.876 1.00 21.01 ? 146  ASP A CG  1 
ATOM   1190 O OD1 . ASP A 1 146 ? 80.070 16.839 -24.214 1.00 18.50 ? 146  ASP A OD1 1 
ATOM   1191 O OD2 . ASP A 1 146 ? 81.202 18.697 -24.429 1.00 22.35 ? 146  ASP A OD2 1 
ATOM   1192 N N   . PHE A 1 147 ? 77.368 15.653 -25.402 1.00 13.51 ? 147  PHE A N   1 
ATOM   1193 C CA  . PHE A 1 147 ? 76.213 15.381 -24.555 1.00 14.02 ? 147  PHE A CA  1 
ATOM   1194 C C   . PHE A 1 147 ? 76.599 15.106 -23.108 1.00 15.17 ? 147  PHE A C   1 
ATOM   1195 O O   . PHE A 1 147 ? 75.797 14.547 -22.352 1.00 16.64 ? 147  PHE A O   1 
ATOM   1196 C CB  . PHE A 1 147 ? 75.403 14.214 -25.127 1.00 15.15 ? 147  PHE A CB  1 
ATOM   1197 C CG  . PHE A 1 147 ? 74.641 14.575 -26.378 1.00 16.05 ? 147  PHE A CG  1 
ATOM   1198 C CD1 . PHE A 1 147 ? 75.301 14.704 -27.588 1.00 19.98 ? 147  PHE A CD1 1 
ATOM   1199 C CD2 . PHE A 1 147 ? 73.276 14.812 -26.334 1.00 12.50 ? 147  PHE A CD2 1 
ATOM   1200 C CE1 . PHE A 1 147 ? 74.618 15.053 -28.737 1.00 17.70 ? 147  PHE A CE1 1 
ATOM   1201 C CE2 . PHE A 1 147 ? 72.586 15.150 -27.482 1.00 14.74 ? 147  PHE A CE2 1 
ATOM   1202 C CZ  . PHE A 1 147 ? 73.260 15.268 -28.683 1.00 17.41 ? 147  PHE A CZ  1 
ATOM   1203 N N   . SER A 1 148 ? 77.809 15.498 -22.703 1.00 13.16 ? 148  SER A N   1 
ATOM   1204 C CA  . SER A 1 148 ? 78.228 15.286 -21.323 1.00 19.66 ? 148  SER A CA  1 
ATOM   1205 C C   . SER A 1 148 ? 77.360 16.058 -20.321 1.00 21.57 ? 148  SER A C   1 
ATOM   1206 O O   . SER A 1 148 ? 77.208 15.616 -19.176 1.00 18.51 ? 148  SER A O   1 
ATOM   1207 C CB  . SER A 1 148 ? 79.709 15.640 -21.194 1.00 20.03 ? 148  SER A CB  1 
ATOM   1208 O OG  . SER A 1 148 ? 79.910 17.027 -21.394 1.00 23.77 ? 148  SER A OG  1 
ATOM   1209 N N   . ARG A 1 149 ? 76.767 17.184 -20.735 1.00 15.84 ? 149  ARG A N   1 
ATOM   1210 C CA  . ARG A 1 149 ? 75.800 17.950 -19.931 1.00 12.94 ? 149  ARG A CA  1 
ATOM   1211 C C   . ARG A 1 149 ? 74.592 18.225 -20.829 1.00 12.33 ? 149  ARG A C   1 
ATOM   1212 O O   . ARG A 1 149 ? 74.521 19.268 -21.491 1.00 10.51 ? 149  ARG A O   1 
ATOM   1213 C CB  . ARG A 1 149 ? 76.424 19.245 -19.399 1.00 13.66 ? 149  ARG A CB  1 
ATOM   1214 C CG  . ARG A 1 149 ? 77.508 19.005 -18.328 1.00 19.75 ? 149  ARG A CG  1 
ATOM   1215 C CD  . ARG A 1 149 ? 78.314 20.271 -17.985 1.00 20.80 ? 149  ARG A CD  1 
ATOM   1216 N NE  . ARG A 1 149 ? 79.053 20.822 -19.115 1.00 29.38 ? 149  ARG A NE  1 
ATOM   1217 C CZ  . ARG A 1 149 ? 79.346 22.111 -19.274 1.00 35.30 ? 149  ARG A CZ  1 
ATOM   1218 N NH1 . ARG A 1 149 ? 78.897 23.038 -18.431 1.00 23.50 ? 149  ARG A NH1 1 
ATOM   1219 N NH2 . ARG A 1 149 ? 80.116 22.480 -20.301 1.00 23.19 ? 149  ARG A NH2 1 
ATOM   1220 N N   . SER A 1 150 ? 73.650 17.279 -20.872 1.00 11.50 ? 150  SER A N   1 
ATOM   1221 C CA  . SER A 1 150 ? 72.637 17.254 -21.919 1.00 10.95 ? 150  SER A CA  1 
ATOM   1222 C C   . SER A 1 150 ? 71.230 17.509 -21.388 1.00 10.51 ? 150  SER A C   1 
ATOM   1223 O O   . SER A 1 150 ? 70.254 17.232 -22.090 1.00 10.67 ? 150  SER A O   1 
ATOM   1224 C CB  . SER A 1 150 ? 72.680 15.924 -22.679 1.00 11.83 ? 150  SER A CB  1 
ATOM   1225 O OG  . SER A 1 150 ? 72.512 14.828 -21.795 1.00 12.79 ? 150  SER A OG  1 
ATOM   1226 N N   . GLY A 1 151 ? 71.103 18.039 -20.173 1.00 12.56 ? 151  GLY A N   1 
ATOM   1227 C CA  . GLY A 1 151 ? 69.788 18.484 -19.709 1.00 9.94  ? 151  GLY A CA  1 
ATOM   1228 C C   . GLY A 1 151 ? 68.833 17.326 -19.472 1.00 10.26 ? 151  GLY A C   1 
ATOM   1229 O O   . GLY A 1 151 ? 69.194 16.318 -18.860 1.00 10.18 ? 151  GLY A O   1 
ATOM   1230 N N   . TRP A 1 152 ? 67.593 17.457 -19.959 1.00 9.68  ? 152  TRP A N   1 
ATOM   1231 C CA  . TRP A 1 152 ? 66.619 16.388 -19.756 1.00 9.93  ? 152  TRP A CA  1 
ATOM   1232 C C   . TRP A 1 152 ? 66.940 15.137 -20.559 1.00 10.87 ? 152  TRP A C   1 
ATOM   1233 O O   . TRP A 1 152 ? 66.289 14.113 -20.345 1.00 10.82 ? 152  TRP A O   1 
ATOM   1234 C CB  . TRP A 1 152 ? 65.198 16.875 -20.077 1.00 8.51  ? 152  TRP A CB  1 
ATOM   1235 C CG  . TRP A 1 152 ? 64.705 17.880 -19.059 1.00 7.66  ? 152  TRP A CG  1 
ATOM   1236 C CD1 . TRP A 1 152 ? 64.400 19.191 -19.283 1.00 9.08  ? 152  TRP A CD1 1 
ATOM   1237 C CD2 . TRP A 1 152 ? 64.500 17.651 -17.660 1.00 8.96  ? 152  TRP A CD2 1 
ATOM   1238 N NE1 . TRP A 1 152 ? 64.004 19.793 -18.106 1.00 9.12  ? 152  TRP A NE1 1 
ATOM   1239 C CE2 . TRP A 1 152 ? 64.049 18.865 -17.099 1.00 9.41  ? 152  TRP A CE2 1 
ATOM   1240 C CE3 . TRP A 1 152 ? 64.624 16.526 -16.832 1.00 9.68  ? 152  TRP A CE3 1 
ATOM   1241 C CZ2 . TRP A 1 152 ? 63.740 18.998 -15.741 1.00 9.62  ? 152  TRP A CZ2 1 
ATOM   1242 C CZ3 . TRP A 1 152 ? 64.314 16.649 -15.483 1.00 11.11 ? 152  TRP A CZ3 1 
ATOM   1243 C CH2 . TRP A 1 152 ? 63.882 17.882 -14.946 1.00 11.58 ? 152  TRP A CH2 1 
ATOM   1244 N N   . LEU A 1 153 ? 67.921 15.186 -21.465 1.00 10.27 ? 153  LEU A N   1 
ATOM   1245 C CA  . LEU A 1 153 ? 68.435 13.954 -22.059 1.00 12.75 ? 153  LEU A CA  1 
ATOM   1246 C C   . LEU A 1 153 ? 69.384 13.213 -21.116 1.00 18.58 ? 153  LEU A C   1 
ATOM   1247 O O   . LEU A 1 153 ? 69.646 12.020 -21.323 1.00 14.52 ? 153  LEU A O   1 
ATOM   1248 C CB  . LEU A 1 153 ? 69.168 14.267 -23.363 1.00 9.85  ? 153  LEU A CB  1 
ATOM   1249 C CG  . LEU A 1 153 ? 68.423 15.010 -24.476 1.00 11.39 ? 153  LEU A CG  1 
ATOM   1250 C CD1 . LEU A 1 153 ? 69.324 15.082 -25.677 1.00 10.22 ? 153  LEU A CD1 1 
ATOM   1251 C CD2 . LEU A 1 153 ? 67.090 14.330 -24.822 1.00 10.21 ? 153  LEU A CD2 1 
ATOM   1252 N N   . ASP A 1 154 ? 69.879 13.898 -20.082 1.00 15.70 ? 154  ASP A N   1 
ATOM   1253 C CA  . ASP A 1 154 ? 71.001 13.421 -19.278 1.00 19.44 ? 154  ASP A CA  1 
ATOM   1254 C C   . ASP A 1 154 ? 70.525 12.375 -18.289 1.00 21.45 ? 154  ASP A C   1 
ATOM   1255 O O   . ASP A 1 154 ? 69.467 12.521 -17.664 1.00 15.37 ? 154  ASP A O   1 
ATOM   1256 C CB  . ASP A 1 154 ? 71.649 14.583 -18.514 1.00 21.33 ? 154  ASP A CB  1 
ATOM   1257 C CG  . ASP A 1 154 ? 73.107 14.312 -18.124 1.00 31.11 ? 154  ASP A CG  1 
ATOM   1258 O OD1 . ASP A 1 154 ? 73.335 13.443 -17.252 1.00 31.43 ? 154  ASP A OD1 1 
ATOM   1259 O OD2 . ASP A 1 154 ? 74.021 14.951 -18.723 1.00 27.59 ? 154  ASP A OD2 1 
ATOM   1260 N N   . ASP A 1 155 ? 71.326 11.322 -18.126 1.00 27.35 ? 155  ASP A N   1 
ATOM   1261 C CA  . ASP A 1 155 ? 70.909 10.253 -17.233 1.00 33.68 ? 155  ASP A CA  1 
ATOM   1262 C C   . ASP A 1 155 ? 70.990 10.645 -15.756 1.00 29.13 ? 155  ASP A C   1 
ATOM   1263 O O   . ASP A 1 155 ? 70.490 9.906  -14.904 1.00 33.12 ? 155  ASP A O   1 
ATOM   1264 C CB  . ASP A 1 155 ? 71.707 8.976  -17.560 1.00 36.80 ? 155  ASP A CB  1 
ATOM   1265 C CG  . ASP A 1 155 ? 73.194 9.098  -17.262 1.00 43.24 ? 155  ASP A CG  1 
ATOM   1266 O OD1 . ASP A 1 155 ? 73.632 10.086 -16.631 1.00 54.06 ? 155  ASP A OD1 1 
ATOM   1267 O OD2 . ASP A 1 155 ? 73.938 8.180  -17.670 1.00 50.83 ? 155  ASP A OD2 1 
ATOM   1268 N N   . ARG A 1 156 ? 71.555 11.798 -15.433 1.00 25.12 ? 156  ARG A N   1 
ATOM   1269 C CA  . ARG A 1 156 ? 71.525 12.284 -14.062 1.00 27.16 ? 156  ARG A CA  1 
ATOM   1270 C C   . ARG A 1 156 ? 70.339 13.203 -13.776 1.00 20.54 ? 156  ARG A C   1 
ATOM   1271 O O   . ARG A 1 156 ? 70.078 13.497 -12.603 1.00 21.59 ? 156  ARG A O   1 
ATOM   1272 C CB  . ARG A 1 156 ? 72.836 13.015 -13.748 1.00 28.91 ? 156  ARG A CB  1 
ATOM   1273 C CG  . ARG A 1 156 ? 74.073 12.348 -14.366 1.00 37.32 ? 156  ARG A CG  1 
ATOM   1274 C CD  . ARG A 1 156 ? 75.390 12.982 -13.899 1.00 40.01 ? 156  ARG A CD  1 
ATOM   1275 N NE  . ARG A 1 156 ? 76.467 11.997 -13.875 1.00 43.99 ? 156  ARG A NE  1 
ATOM   1276 C CZ  . ARG A 1 156 ? 77.691 12.214 -13.410 1.00 41.91 ? 156  ARG A CZ  1 
ATOM   1277 N NH1 . ARG A 1 156 ? 78.059 13.401 -12.949 1.00 36.25 ? 156  ARG A NH1 1 
ATOM   1278 N NH2 . ARG A 1 156 ? 78.568 11.212 -13.403 1.00 44.09 ? 156  ARG A NH2 1 
ATOM   1279 N N   . SER A 1 157 ? 69.601 13.648 -14.804 1.00 12.93 ? 157  SER A N   1 
ATOM   1280 C CA  . SER A 1 157 ? 68.677 14.758 -14.593 1.00 15.43 ? 157  SER A CA  1 
ATOM   1281 C C   . SER A 1 157 ? 67.532 14.362 -13.667 1.00 12.98 ? 157  SER A C   1 
ATOM   1282 O O   . SER A 1 157 ? 67.172 15.124 -12.762 1.00 10.69 ? 157  SER A O   1 
ATOM   1283 C CB  . SER A 1 157 ? 68.138 15.289 -15.928 1.00 14.87 ? 157  SER A CB  1 
ATOM   1284 O OG  . SER A 1 157 ? 67.393 14.301 -16.634 1.00 16.90 ? 157  SER A OG  1 
ATOM   1285 N N   . VAL A 1 158 ? 66.954 13.176 -13.864 1.00 9.05  ? 158  VAL A N   1 
ATOM   1286 C CA  . VAL A 1 158 ? 65.813 12.767 -13.048 1.00 12.56 ? 158  VAL A CA  1 
ATOM   1287 C C   . VAL A 1 158 ? 66.219 12.714 -11.577 1.00 13.96 ? 158  VAL A C   1 
ATOM   1288 O O   . VAL A 1 158 ? 65.549 13.285 -10.709 1.00 11.89 ? 158  VAL A O   1 
ATOM   1289 C CB  . VAL A 1 158 ? 65.257 11.413 -13.530 1.00 12.47 ? 158  VAL A CB  1 
ATOM   1290 C CG1 . VAL A 1 158 ? 64.206 10.887 -12.566 1.00 14.64 ? 158  VAL A CG1 1 
ATOM   1291 C CG2 . VAL A 1 158 ? 64.688 11.516 -14.964 1.00 11.79 ? 158  VAL A CG2 1 
ATOM   1292 N N   . HIS A 1 159 ? 67.349 12.065 -11.290 1.00 13.33 ? 159  HIS A N   1 
ATOM   1293 C CA  . HIS A 1 159 ? 67.805 11.905 -9.911  1.00 16.77 ? 159  HIS A CA  1 
ATOM   1294 C C   . HIS A 1 159 ? 68.144 13.252 -9.291  1.00 15.74 ? 159  HIS A C   1 
ATOM   1295 O O   . HIS A 1 159 ? 67.751 13.549 -8.156  1.00 11.97 ? 159  HIS A O   1 
ATOM   1296 C CB  . HIS A 1 159 ? 69.030 10.986 -9.868  1.00 21.22 ? 159  HIS A CB  1 
ATOM   1297 C CG  . HIS A 1 159 ? 69.411 10.548 -8.487  1.00 29.22 ? 159  HIS A CG  1 
ATOM   1298 N ND1 . HIS A 1 159 ? 68.496 10.071 -7.573  1.00 38.51 ? 159  HIS A ND1 1 
ATOM   1299 C CD2 . HIS A 1 159 ? 70.605 10.565 -7.847  1.00 35.63 ? 159  HIS A CD2 1 
ATOM   1300 C CE1 . HIS A 1 159 ? 69.116 9.780  -6.442  1.00 33.34 ? 159  HIS A CE1 1 
ATOM   1301 N NE2 . HIS A 1 159 ? 70.394 10.076 -6.580  1.00 34.70 ? 159  HIS A NE2 1 
ATOM   1302 N N   . GLU A 1 160 ? 68.875 14.084 -10.027 1.00 11.47 ? 160  GLU A N   1 
ATOM   1303 C CA  . GLU A 1 160 ? 69.268 15.371 -9.471  1.00 13.86 ? 160  GLU A CA  1 
ATOM   1304 C C   . GLU A 1 160 ? 68.067 16.298 -9.284  1.00 11.76 ? 160  GLU A C   1 
ATOM   1305 O O   . GLU A 1 160 ? 68.038 17.074 -8.323  1.00 13.05 ? 160  GLU A O   1 
ATOM   1306 C CB  . GLU A 1 160 ? 70.338 16.020 -10.344 1.00 17.03 ? 160  GLU A CB  1 
ATOM   1307 C CG  . GLU A 1 160 ? 71.742 15.370 -10.244 1.00 18.21 ? 160  GLU A CG  1 
ATOM   1308 C CD  . GLU A 1 160 ? 71.982 14.617 -8.919  1.00 25.76 ? 160  GLU A CD  1 
ATOM   1309 O OE1 . GLU A 1 160 ? 72.294 15.282 -7.911  1.00 23.29 ? 160  GLU A OE1 1 
ATOM   1310 O OE2 . GLU A 1 160 ? 71.981 13.359 -8.904  1.00 21.79 ? 160  GLU A OE2 1 
ATOM   1311 N N   . PHE A 1 161 ? 67.051 16.209 -10.145 1.00 11.00 ? 161  PHE A N   1 
ATOM   1312 C CA  . PHE A 1 161 ? 65.843 17.010 -9.921  1.00 11.34 ? 161  PHE A CA  1 
ATOM   1313 C C   . PHE A 1 161 ? 65.084 16.546 -8.675  1.00 14.01 ? 161  PHE A C   1 
ATOM   1314 O O   . PHE A 1 161 ? 64.551 17.373 -7.918  1.00 11.85 ? 161  PHE A O   1 
ATOM   1315 C CB  . PHE A 1 161 ? 64.918 16.963 -11.138 1.00 9.94  ? 161  PHE A CB  1 
ATOM   1316 C CG  . PHE A 1 161 ? 63.675 17.806 -10.972 1.00 10.08 ? 161  PHE A CG  1 
ATOM   1317 C CD1 . PHE A 1 161 ? 63.755 19.189 -10.993 1.00 11.80 ? 161  PHE A CD1 1 
ATOM   1318 C CD2 . PHE A 1 161 ? 62.444 17.217 -10.757 1.00 10.58 ? 161  PHE A CD2 1 
ATOM   1319 C CE1 . PHE A 1 161 ? 62.616 19.972 -10.821 1.00 12.13 ? 161  PHE A CE1 1 
ATOM   1320 C CE2 . PHE A 1 161 ? 61.310 17.984 -10.583 1.00 12.41 ? 161  PHE A CE2 1 
ATOM   1321 C CZ  . PHE A 1 161 ? 61.399 19.370 -10.611 1.00 11.75 ? 161  PHE A CZ  1 
ATOM   1322 N N   . THR A 1 162 ? 65.013 15.230 -8.459  1.00 10.69 ? 162  THR A N   1 
ATOM   1323 C CA  . THR A 1 162 ? 64.347 14.693 -7.273  1.00 13.99 ? 162  THR A CA  1 
ATOM   1324 C C   . THR A 1 162 ? 65.005 15.213 -6.001  1.00 12.97 ? 162  THR A C   1 
ATOM   1325 O O   . THR A 1 162 ? 64.323 15.595 -5.039  1.00 14.63 ? 162  THR A O   1 
ATOM   1326 C CB  . THR A 1 162 ? 64.395 13.160 -7.302  1.00 14.29 ? 162  THR A CB  1 
ATOM   1327 O OG1 . THR A 1 162 ? 63.734 12.689 -8.483  1.00 18.30 ? 162  THR A OG1 1 
ATOM   1328 C CG2 . THR A 1 162 ? 63.697 12.577 -6.067  1.00 18.55 ? 162  THR A CG2 1 
ATOM   1329 N N   . LYS A 1 163 ? 66.336 15.238 -5.991  1.00 11.68 ? 163  LYS A N   1 
ATOM   1330 C CA  . LYS A 1 163 ? 67.087 15.758 -4.854  1.00 13.88 ? 163  LYS A CA  1 
ATOM   1331 C C   . LYS A 1 163 ? 66.780 17.238 -4.628  1.00 14.50 ? 163  LYS A C   1 
ATOM   1332 O O   . LYS A 1 163 ? 66.570 17.681 -3.487  1.00 10.41 ? 163  LYS A O   1 
ATOM   1333 C CB  . LYS A 1 163 ? 68.571 15.507 -5.136  1.00 15.96 ? 163  LYS A CB  1 
ATOM   1334 C CG  . LYS A 1 163 ? 69.454 15.249 -3.956  1.00 30.66 ? 163  LYS A CG  1 
ATOM   1335 C CD  . LYS A 1 163 ? 70.937 15.203 -4.366  1.00 27.79 ? 163  LYS A CD  1 
ATOM   1336 C CE  . LYS A 1 163 ? 71.261 13.930 -5.151  1.00 28.86 ? 163  LYS A CE  1 
ATOM   1337 N NZ  . LYS A 1 163 ? 72.723 13.806 -5.502  1.00 26.57 ? 163  LYS A NZ  1 
ATOM   1338 N N   . PHE A 1 164 ? 66.727 18.013 -5.713  1.00 9.57  ? 164  PHE A N   1 
ATOM   1339 C CA  . PHE A 1 164 ? 66.363 19.426 -5.636  1.00 10.29 ? 164  PHE A CA  1 
ATOM   1340 C C   . PHE A 1 164 ? 64.956 19.602 -5.072  1.00 10.52 ? 164  PHE A C   1 
ATOM   1341 O O   . PHE A 1 164 ? 64.723 20.444 -4.198  1.00 11.65 ? 164  PHE A O   1 
ATOM   1342 C CB  . PHE A 1 164 ? 66.489 20.039 -7.038  1.00 10.06 ? 164  PHE A CB  1 
ATOM   1343 C CG  . PHE A 1 164 ? 65.962 21.449 -7.158  1.00 11.70 ? 164  PHE A CG  1 
ATOM   1344 C CD1 . PHE A 1 164 ? 66.432 22.464 -6.336  1.00 11.99 ? 164  PHE A CD1 1 
ATOM   1345 C CD2 . PHE A 1 164 ? 65.006 21.755 -8.119  1.00 10.78 ? 164  PHE A CD2 1 
ATOM   1346 C CE1 . PHE A 1 164 ? 65.955 23.770 -6.471  1.00 10.15 ? 164  PHE A CE1 1 
ATOM   1347 C CE2 . PHE A 1 164 ? 64.509 23.050 -8.254  1.00 10.88 ? 164  PHE A CE2 1 
ATOM   1348 C CZ  . PHE A 1 164 ? 64.988 24.060 -7.432  1.00 11.01 ? 164  PHE A CZ  1 
ATOM   1349 N N   . ALA A 1 165 ? 64.007 18.793 -5.553  1.00 12.19 ? 165  ALA A N   1 
ATOM   1350 C CA  . ALA A 1 165 ? 62.628 18.862 -5.084  1.00 11.85 ? 165  ALA A CA  1 
ATOM   1351 C C   . ALA A 1 165 ? 62.521 18.521 -3.600  1.00 12.70 ? 165  ALA A C   1 
ATOM   1352 O O   . ALA A 1 165 ? 61.785 19.177 -2.854  1.00 10.86 ? 165  ALA A O   1 
ATOM   1353 C CB  . ALA A 1 165 ? 61.759 17.911 -5.912  1.00 11.07 ? 165  ALA A CB  1 
ATOM   1354 N N   . THR A 1 166 ? 63.234 17.485 -3.161  1.00 11.29 ? 166  THR A N   1 
ATOM   1355 C CA  . THR A 1 166 ? 63.241 17.131 -1.743  1.00 14.43 ? 166  THR A CA  1 
ATOM   1356 C C   . THR A 1 166 ? 63.699 18.304 -0.888  1.00 11.75 ? 166  THR A C   1 
ATOM   1357 O O   . THR A 1 166 ? 63.087 18.618 0.141   1.00 13.93 ? 166  THR A O   1 
ATOM   1358 C CB  . THR A 1 166 ? 64.160 15.930 -1.508  1.00 14.31 ? 166  THR A CB  1 
ATOM   1359 O OG1 . THR A 1 166 ? 63.731 14.831 -2.310  1.00 13.91 ? 166  THR A OG1 1 
ATOM   1360 C CG2 . THR A 1 166 ? 64.137 15.519 -0.049  1.00 18.92 ? 166  THR A CG2 1 
ATOM   1361 N N   . PHE A 1 167 ? 64.799 18.940 -1.291  1.00 11.88 ? 167  PHE A N   1 
ATOM   1362 C CA  . PHE A 1 167 ? 65.326 20.086 -0.567  1.00 15.11 ? 167  PHE A CA  1 
ATOM   1363 C C   . PHE A 1 167 ? 64.302 21.214 -0.489  1.00 15.89 ? 167  PHE A C   1 
ATOM   1364 O O   . PHE A 1 167 ? 64.146 21.846 0.563   1.00 12.59 ? 167  PHE A O   1 
ATOM   1365 C CB  . PHE A 1 167 ? 66.609 20.578 -1.245  1.00 12.04 ? 167  PHE A CB  1 
ATOM   1366 C CG  . PHE A 1 167 ? 67.198 21.794 -0.601  1.00 14.83 ? 167  PHE A CG  1 
ATOM   1367 C CD1 . PHE A 1 167 ? 68.015 21.676 0.514   1.00 17.59 ? 167  PHE A CD1 1 
ATOM   1368 C CD2 . PHE A 1 167 ? 66.902 23.062 -1.084  1.00 16.21 ? 167  PHE A CD2 1 
ATOM   1369 C CE1 . PHE A 1 167 ? 68.549 22.804 1.127   1.00 21.65 ? 167  PHE A CE1 1 
ATOM   1370 C CE2 . PHE A 1 167 ? 67.430 24.202 -0.473  1.00 16.60 ? 167  PHE A CE2 1 
ATOM   1371 C CZ  . PHE A 1 167 ? 68.254 24.070 0.633   1.00 17.33 ? 167  PHE A CZ  1 
ATOM   1372 N N   . CYS A 1 168 ? 63.611 21.497 -1.599  1.00 11.40 ? 168  CYS A N   1 
ATOM   1373 C CA  . CYS A 1 168 ? 62.651 22.600 -1.615  1.00 11.33 ? 168  CYS A CA  1 
ATOM   1374 C C   . CYS A 1 168 ? 61.445 22.309 -0.731  1.00 12.17 ? 168  CYS A C   1 
ATOM   1375 O O   . CYS A 1 168 ? 60.948 23.205 -0.037  1.00 10.92 ? 168  CYS A O   1 
ATOM   1376 C CB  . CYS A 1 168 ? 62.200 22.895 -3.049  1.00 10.87 ? 168  CYS A CB  1 
ATOM   1377 S SG  . CYS A 1 168 ? 63.536 23.553 -4.053  1.00 14.59 ? 168  CYS A SG  1 
ATOM   1378 N N   . ALA A 1 169 ? 60.946 21.072 -0.747  1.00 10.75 ? 169  ALA A N   1 
ATOM   1379 C CA  . ALA A 1 169 ? 59.798 20.755 0.097   1.00 11.72 ? 169  ALA A CA  1 
ATOM   1380 C C   . ALA A 1 169 ? 60.155 20.890 1.575   1.00 14.11 ? 169  ALA A C   1 
ATOM   1381 O O   . ALA A 1 169 ? 59.337 21.353 2.381   1.00 12.72 ? 169  ALA A O   1 
ATOM   1382 C CB  . ALA A 1 169 ? 59.278 19.350 -0.222  1.00 10.86 ? 169  ALA A CB  1 
ATOM   1383 N N   . LYS A 1 170 ? 61.385 20.528 1.943   1.00 12.57 ? 170  LYS A N   1 
ATOM   1384 C CA  . LYS A 1 170 ? 61.831 20.692 3.328   1.00 19.18 ? 170  LYS A CA  1 
ATOM   1385 C C   . LYS A 1 170 ? 62.016 22.160 3.688   1.00 16.87 ? 170  LYS A C   1 
ATOM   1386 O O   . LYS A 1 170 ? 61.556 22.612 4.745   1.00 17.79 ? 170  LYS A O   1 
ATOM   1387 C CB  . LYS A 1 170 ? 63.144 19.954 3.558   1.00 13.34 ? 170  LYS A CB  1 
ATOM   1388 C CG  . LYS A 1 170 ? 63.062 18.433 3.601   1.00 19.15 ? 170  LYS A CG  1 
ATOM   1389 C CD  . LYS A 1 170 ? 64.488 17.917 3.688   1.00 22.47 ? 170  LYS A CD  1 
ATOM   1390 C CE  . LYS A 1 170 ? 64.543 16.432 3.942   1.00 29.49 ? 170  LYS A CE  1 
ATOM   1391 N NZ  . LYS A 1 170 ? 63.724 15.748 2.954   1.00 31.49 ? 170  LYS A NZ  1 
ATOM   1392 N N   . SER A 1 171 ? 62.722 22.912 2.842   1.00 9.83  ? 171  SER A N   1 
ATOM   1393 C CA  . SER A 1 171 ? 63.197 24.238 3.240   1.00 16.10 ? 171  SER A CA  1 
ATOM   1394 C C   . SER A 1 171 ? 62.129 25.314 3.084   1.00 14.88 ? 171  SER A C   1 
ATOM   1395 O O   . SER A 1 171 ? 62.054 26.234 3.907   1.00 15.68 ? 171  SER A O   1 
ATOM   1396 C CB  . SER A 1 171 ? 64.436 24.635 2.433   1.00 14.24 ? 171  SER A CB  1 
ATOM   1397 O OG  . SER A 1 171 ? 65.548 23.823 2.773   1.00 26.23 ? 171  SER A OG  1 
ATOM   1398 N N   . PHE A 1 172 ? 61.309 25.235 2.036   1.00 13.46 ? 172  PHE A N   1 
ATOM   1399 C CA  . PHE A 1 172 ? 60.324 26.288 1.759   1.00 12.75 ? 172  PHE A CA  1 
ATOM   1400 C C   . PHE A 1 172 ? 59.006 25.927 2.446   1.00 13.34 ? 172  PHE A C   1 
ATOM   1401 O O   . PHE A 1 172 ? 58.002 25.572 1.826   1.00 13.01 ? 172  PHE A O   1 
ATOM   1402 C CB  . PHE A 1 172 ? 60.172 26.490 0.253   1.00 8.82  ? 172  PHE A CB  1 
ATOM   1403 C CG  . PHE A 1 172 ? 61.387 27.111 -0.387  1.00 8.23  ? 172  PHE A CG  1 
ATOM   1404 C CD1 . PHE A 1 172 ? 61.748 28.423 -0.095  1.00 9.87  ? 172  PHE A CD1 1 
ATOM   1405 C CD2 . PHE A 1 172 ? 62.187 26.376 -1.242  1.00 8.92  ? 172  PHE A CD2 1 
ATOM   1406 C CE1 . PHE A 1 172 ? 62.876 28.992 -0.666  1.00 10.52 ? 172  PHE A CE1 1 
ATOM   1407 C CE2 . PHE A 1 172 ? 63.309 26.934 -1.817  1.00 13.24 ? 172  PHE A CE2 1 
ATOM   1408 C CZ  . PHE A 1 172 ? 63.657 28.251 -1.527  1.00 12.98 ? 172  PHE A CZ  1 
ATOM   1409 N N   . ASP A 1 173 ? 59.043 26.022 3.775   1.00 12.47 ? 173  ASP A N   1 
ATOM   1410 C CA  . ASP A 1 173 ? 57.954 25.542 4.608   1.00 14.28 ? 173  ASP A CA  1 
ATOM   1411 C C   . ASP A 1 173 ? 56.728 26.442 4.580   1.00 14.88 ? 173  ASP A C   1 
ATOM   1412 O O   . ASP A 1 173 ? 55.663 26.006 5.019   1.00 14.01 ? 173  ASP A O   1 
ATOM   1413 C CB  . ASP A 1 173 ? 58.430 25.399 6.065   1.00 15.17 ? 173  ASP A CB  1 
ATOM   1414 C CG  . ASP A 1 173 ? 59.059 26.690 6.609   1.00 17.06 ? 173  ASP A CG  1 
ATOM   1415 O OD1 . ASP A 1 173 ? 58.302 27.593 7.025   1.00 15.43 ? 173  ASP A OD1 1 
ATOM   1416 O OD2 . ASP A 1 173 ? 60.306 26.798 6.643   1.00 17.17 ? 173  ASP A OD2 1 
ATOM   1417 N N   . ASP A 1 174 ? 56.838 27.682 4.092   1.00 12.68 ? 174  ASP A N   1 
ATOM   1418 C CA  . ASP A 1 174 ? 55.753 28.642 4.264   1.00 15.89 ? 174  ASP A CA  1 
ATOM   1419 C C   . ASP A 1 174 ? 55.083 29.061 2.954   1.00 18.47 ? 174  ASP A C   1 
ATOM   1420 O O   . ASP A 1 174 ? 54.316 30.029 2.943   1.00 15.89 ? 174  ASP A O   1 
ATOM   1421 C CB  . ASP A 1 174 ? 56.258 29.848 5.054   1.00 13.97 ? 174  ASP A CB  1 
ATOM   1422 C CG  . ASP A 1 174 ? 55.159 30.494 5.903   1.00 21.88 ? 174  ASP A CG  1 
ATOM   1423 O OD1 . ASP A 1 174 ? 54.230 29.761 6.329   1.00 21.36 ? 174  ASP A OD1 1 
ATOM   1424 O OD2 . ASP A 1 174 ? 55.134 31.733 6.035   1.00 19.27 ? 174  ASP A OD2 1 
ATOM   1425 N N   . VAL A 1 175 ? 55.286 28.308 1.872   1.00 11.61 ? 175  VAL A N   1 
ATOM   1426 C CA  . VAL A 1 175 ? 54.551 28.567 0.635   1.00 12.16 ? 175  VAL A CA  1 
ATOM   1427 C C   . VAL A 1 175 ? 53.117 28.099 0.817   1.00 13.88 ? 175  VAL A C   1 
ATOM   1428 O O   . VAL A 1 175 ? 52.806 27.372 1.768   1.00 14.07 ? 175  VAL A O   1 
ATOM   1429 C CB  . VAL A 1 175 ? 55.195 27.858 -0.562  1.00 12.61 ? 175  VAL A CB  1 
ATOM   1430 C CG1 . VAL A 1 175 ? 56.663 28.266 -0.688  1.00 12.66 ? 175  VAL A CG1 1 
ATOM   1431 C CG2 . VAL A 1 175 ? 55.042 26.351 -0.429  1.00 12.65 ? 175  VAL A CG2 1 
ATOM   1432 N N   . ASP A 1 176 ? 52.234 28.482 -0.102  1.00 11.44 ? 176  ASP A N   1 
ATOM   1433 C CA  . ASP A 1 176 ? 50.882 27.960 -0.040  1.00 11.23 ? 176  ASP A CA  1 
ATOM   1434 C C   . ASP A 1 176 ? 50.703 26.725 -0.898  1.00 13.29 ? 176  ASP A C   1 
ATOM   1435 O O   . ASP A 1 176 ? 49.816 25.915 -0.613  1.00 11.14 ? 176  ASP A O   1 
ATOM   1436 C CB  . ASP A 1 176 ? 49.889 29.053 -0.440  1.00 15.51 ? 176  ASP A CB  1 
ATOM   1437 C CG  . ASP A 1 176 ? 49.851 30.177 0.586   1.00 17.16 ? 176  ASP A CG  1 
ATOM   1438 O OD1 . ASP A 1 176 ? 49.229 29.982 1.652   1.00 19.16 ? 176  ASP A OD1 1 
ATOM   1439 O OD2 . ASP A 1 176 ? 50.520 31.216 0.359   1.00 15.13 ? 176  ASP A OD2 1 
ATOM   1440 N N   . ALA A 1 177 ? 51.539 26.553 -1.920  1.00 12.72 ? 177  ALA A N   1 
ATOM   1441 C CA  . ALA A 1 177 ? 51.476 25.401 -2.807  1.00 10.69 ? 177  ALA A CA  1 
ATOM   1442 C C   . ALA A 1 177 ? 52.758 25.360 -3.619  1.00 10.03 ? 177  ALA A C   1 
ATOM   1443 O O   . ALA A 1 177 ? 53.448 26.374 -3.763  1.00 12.98 ? 177  ALA A O   1 
ATOM   1444 C CB  . ALA A 1 177 ? 50.263 25.461 -3.740  1.00 13.67 ? 177  ALA A CB  1 
ATOM   1445 N N   . PHE A 1 178 ? 53.072 24.170 -4.140  1.00 11.15 ? 178  PHE A N   1 
ATOM   1446 C CA  . PHE A 1 178 ? 54.169 23.970 -5.080  1.00 9.31  ? 178  PHE A CA  1 
ATOM   1447 C C   . PHE A 1 178 ? 53.636 23.473 -6.415  1.00 10.90 ? 178  PHE A C   1 
ATOM   1448 O O   . PHE A 1 178 ? 52.612 22.784 -6.471  1.00 10.38 ? 178  PHE A O   1 
ATOM   1449 C CB  . PHE A 1 178 ? 55.154 22.900 -4.617  1.00 9.34  ? 178  PHE A CB  1 
ATOM   1450 C CG  . PHE A 1 178 ? 55.925 23.239 -3.384  1.00 11.70 ? 178  PHE A CG  1 
ATOM   1451 C CD1 . PHE A 1 178 ? 57.048 24.052 -3.453  1.00 12.12 ? 178  PHE A CD1 1 
ATOM   1452 C CD2 . PHE A 1 178 ? 55.582 22.670 -2.169  1.00 11.07 ? 178  PHE A CD2 1 
ATOM   1453 C CE1 . PHE A 1 178 ? 57.791 24.323 -2.321  1.00 12.07 ? 178  PHE A CE1 1 
ATOM   1454 C CE2 . PHE A 1 178 ? 56.325 22.939 -1.023  1.00 11.90 ? 178  PHE A CE2 1 
ATOM   1455 C CZ  . PHE A 1 178 ? 57.429 23.760 -1.107  1.00 11.71 ? 178  PHE A CZ  1 
ATOM   1456 N N   . THR A 1 179 ? 54.399 23.743 -7.478  1.00 10.89 ? 179  THR A N   1 
ATOM   1457 C CA  . THR A 1 179 ? 54.334 22.969 -8.711  1.00 10.75 ? 179  THR A CA  1 
ATOM   1458 C C   . THR A 1 179 ? 55.749 22.517 -9.056  1.00 8.63  ? 179  THR A C   1 
ATOM   1459 O O   . THR A 1 179 ? 56.718 23.233 -8.796  1.00 9.19  ? 179  THR A O   1 
ATOM   1460 C CB  . THR A 1 179 ? 53.721 23.764 -9.888  1.00 10.76 ? 179  THR A CB  1 
ATOM   1461 O OG1 . THR A 1 179 ? 54.528 24.913 -10.152 1.00 8.99  ? 179  THR A OG1 1 
ATOM   1462 C CG2 . THR A 1 179 ? 52.296 24.207 -9.577  1.00 11.00 ? 179  THR A CG2 1 
ATOM   1463 N N   . THR A 1 180 ? 55.869 21.313 -9.617  1.00 9.54  ? 180  THR A N   1 
ATOM   1464 C CA  . THR A 1 180 ? 57.199 20.787 -9.931  1.00 8.04  ? 180  THR A CA  1 
ATOM   1465 C C   . THR A 1 180 ? 57.812 21.505 -11.132 1.00 11.13 ? 180  THR A C   1 
ATOM   1466 O O   . THR A 1 180 ? 59.006 21.833 -11.127 1.00 8.78  ? 180  THR A O   1 
ATOM   1467 C CB  . THR A 1 180 ? 57.105 19.280 -10.193 1.00 9.81  ? 180  THR A CB  1 
ATOM   1468 O OG1 . THR A 1 180 ? 56.112 19.052 -11.205 1.00 8.65  ? 180  THR A OG1 1 
ATOM   1469 C CG2 . THR A 1 180 ? 56.684 18.520 -8.913  1.00 9.38  ? 180  THR A CG2 1 
ATOM   1470 N N   . MET A 1 181 ? 57.023 21.735 -12.180 1.00 8.03  ? 181  MET A N   1 
ATOM   1471 C CA  . MET A 1 181 ? 57.577 22.236 -13.425 1.00 8.52  ? 181  MET A CA  1 
ATOM   1472 C C   . MET A 1 181 ? 56.500 22.961 -14.217 1.00 10.23 ? 181  MET A C   1 
ATOM   1473 O O   . MET A 1 181 ? 55.297 22.794 -13.987 1.00 8.15  ? 181  MET A O   1 
ATOM   1474 C CB  . MET A 1 181 ? 58.193 21.111 -14.274 1.00 11.89 ? 181  MET A CB  1 
ATOM   1475 C CG  . MET A 1 181 ? 57.412 19.823 -14.262 1.00 12.20 ? 181  MET A CG  1 
ATOM   1476 S SD  . MET A 1 181 ? 58.228 18.405 -15.071 1.00 14.78 ? 181  MET A SD  1 
ATOM   1477 C CE  . MET A 1 181 ? 59.545 17.914 -13.977 1.00 12.97 ? 181  MET A CE  1 
ATOM   1478 N N   . ASN A 1 182 ? 56.968 23.767 -15.169 1.00 9.07  ? 182  ASN A N   1 
ATOM   1479 C CA  . ASN A 1 182 ? 56.145 24.652 -15.984 1.00 8.62  ? 182  ASN A CA  1 
ATOM   1480 C C   . ASN A 1 182 ? 56.323 24.266 -17.445 1.00 7.16  ? 182  ASN A C   1 
ATOM   1481 O O   . ASN A 1 182 ? 57.433 24.363 -17.980 1.00 8.12  ? 182  ASN A O   1 
ATOM   1482 C CB  . ASN A 1 182 ? 56.546 26.120 -15.767 1.00 7.88  ? 182  ASN A CB  1 
ATOM   1483 C CG  . ASN A 1 182 ? 55.855 27.068 -16.748 1.00 10.44 ? 182  ASN A CG  1 
ATOM   1484 O OD1 . ASN A 1 182 ? 54.818 27.652 -16.432 1.00 11.42 ? 182  ASN A OD1 1 
ATOM   1485 N ND2 . ASN A 1 182 ? 56.432 27.223 -17.942 1.00 10.40 ? 182  ASN A ND2 1 
ATOM   1486 N N   . GLU A 1 183 ? 55.232 23.834 -18.075 1.00 8.58  ? 183  GLU A N   1 
ATOM   1487 C CA  . GLU A 1 183 ? 55.162 23.450 -19.486 1.00 6.71  ? 183  GLU A CA  1 
ATOM   1488 C C   . GLU A 1 183 ? 56.336 22.533 -19.876 1.00 8.99  ? 183  GLU A C   1 
ATOM   1489 O O   . GLU A 1 183 ? 57.083 22.841 -20.817 1.00 8.15  ? 183  GLU A O   1 
ATOM   1490 C CB  . GLU A 1 183 ? 55.102 24.675 -20.393 1.00 8.28  ? 183  GLU A CB  1 
ATOM   1491 C CG  . GLU A 1 183 ? 54.236 25.822 -19.862 1.00 9.70  ? 183  GLU A CG  1 
ATOM   1492 C CD  . GLU A 1 183 ? 54.094 26.964 -20.869 1.00 16.88 ? 183  GLU A CD  1 
ATOM   1493 O OE1 . GLU A 1 183 ? 52.967 27.443 -21.109 1.00 12.74 ? 183  GLU A OE1 1 
ATOM   1494 O OE2 . GLU A 1 183 ? 55.067 27.217 -21.617 1.00 12.65 ? 183  GLU A OE2 1 
ATOM   1495 N N   . PRO A 1 184 ? 56.502 21.393 -19.201 1.00 8.97  ? 184  PRO A N   1 
ATOM   1496 C CA  . PRO A 1 184 ? 57.568 20.463 -19.612 1.00 9.71  ? 184  PRO A CA  1 
ATOM   1497 C C   . PRO A 1 184 ? 57.432 20.009 -21.054 1.00 8.25  ? 184  PRO A C   1 
ATOM   1498 O O   . PRO A 1 184 ? 58.449 19.701 -21.689 1.00 9.13  ? 184  PRO A O   1 
ATOM   1499 C CB  . PRO A 1 184 ? 57.408 19.286 -18.629 1.00 9.38  ? 184  PRO A CB  1 
ATOM   1500 C CG  . PRO A 1 184 ? 55.975 19.390 -18.122 1.00 9.13  ? 184  PRO A CG  1 
ATOM   1501 C CD  . PRO A 1 184 ? 55.729 20.873 -18.052 1.00 8.61  ? 184  PRO A CD  1 
ATOM   1502 N N   . ASN A 1 185 ? 56.204 19.955 -21.589 1.00 8.24  ? 185  ASN A N   1 
ATOM   1503 C CA  . ASN A 1 185 ? 56.010 19.558 -22.982 1.00 8.85  ? 185  ASN A CA  1 
ATOM   1504 C C   . ASN A 1 185 ? 56.608 20.575 -23.952 1.00 11.18 ? 185  ASN A C   1 
ATOM   1505 O O   . ASN A 1 185 ? 57.039 20.205 -25.050 1.00 8.79  ? 185  ASN A O   1 
ATOM   1506 C CB  . ASN A 1 185 ? 54.521 19.367 -23.275 1.00 7.39  ? 185  ASN A CB  1 
ATOM   1507 C CG  . ASN A 1 185 ? 53.667 20.596 -22.909 1.00 11.60 ? 185  ASN A CG  1 
ATOM   1508 O OD1 . ASN A 1 185 ? 53.816 21.185 -21.837 1.00 10.40 ? 185  ASN A OD1 1 
ATOM   1509 N ND2 . ASN A 1 185 ? 52.742 20.956 -23.795 1.00 9.29  ? 185  ASN A ND2 1 
ATOM   1510 N N   . VAL A 1 186 ? 56.626 21.855 -23.574 1.00 10.11 ? 186  VAL A N   1 
ATOM   1511 C CA  . VAL A 1 186 ? 57.240 22.885 -24.411 1.00 8.99  ? 186  VAL A CA  1 
ATOM   1512 C C   . VAL A 1 186 ? 58.761 22.768 -24.376 1.00 8.12  ? 186  VAL A C   1 
ATOM   1513 O O   . VAL A 1 186 ? 59.434 22.912 -25.404 1.00 8.48  ? 186  VAL A O   1 
ATOM   1514 C CB  . VAL A 1 186 ? 56.774 24.279 -23.946 1.00 10.73 ? 186  VAL A CB  1 
ATOM   1515 C CG1 . VAL A 1 186 ? 57.616 25.391 -24.620 1.00 10.09 ? 186  VAL A CG1 1 
ATOM   1516 C CG2 . VAL A 1 186 ? 55.285 24.457 -24.195 1.00 9.12  ? 186  VAL A CG2 1 
ATOM   1517 N N   . VAL A 1 187 ? 59.330 22.548 -23.188 1.00 7.84  ? 187  VAL A N   1 
ATOM   1518 C CA  . VAL A 1 187 ? 60.769 22.305 -23.081 1.00 8.07  ? 187  VAL A CA  1 
ATOM   1519 C C   . VAL A 1 187 ? 61.186 21.195 -24.035 1.00 8.83  ? 187  VAL A C   1 
ATOM   1520 O O   . VAL A 1 187 ? 62.188 21.304 -24.755 1.00 9.06  ? 187  VAL A O   1 
ATOM   1521 C CB  . VAL A 1 187 ? 61.146 21.940 -21.634 1.00 8.55  ? 187  VAL A CB  1 
ATOM   1522 C CG1 . VAL A 1 187 ? 62.623 21.541 -21.555 1.00 7.56  ? 187  VAL A CG1 1 
ATOM   1523 C CG2 . VAL A 1 187 ? 60.793 23.078 -20.659 1.00 8.82  ? 187  VAL A CG2 1 
ATOM   1524 N N   . ALA A 1 188 ? 60.442 20.085 -24.016 1.00 7.58  ? 188  ALA A N   1 
ATOM   1525 C CA  . ALA A 1 188 ? 60.815 18.928 -24.822 1.00 7.63  ? 188  ALA A CA  1 
ATOM   1526 C C   . ALA A 1 188 ? 60.559 19.185 -26.303 1.00 8.73  ? 188  ALA A C   1 
ATOM   1527 O O   . ALA A 1 188 ? 61.443 18.967 -27.144 1.00 7.04  ? 188  ALA A O   1 
ATOM   1528 C CB  . ALA A 1 188 ? 60.054 17.682 -24.349 1.00 8.07  ? 188  ALA A CB  1 
ATOM   1529 N N   . LYS A 1 189 ? 59.361 19.662 -26.646 1.00 8.61  ? 189  LYS A N   1 
ATOM   1530 C CA  . LYS A 1 189 ? 59.031 19.808 -28.063 1.00 7.76  ? 189  LYS A CA  1 
ATOM   1531 C C   . LYS A 1 189 ? 59.862 20.905 -28.720 1.00 9.12  ? 189  LYS A C   1 
ATOM   1532 O O   . LYS A 1 189 ? 60.402 20.709 -29.817 1.00 7.15  ? 189  LYS A O   1 
ATOM   1533 C CB  . LYS A 1 189 ? 57.540 20.088 -28.247 1.00 9.37  ? 189  LYS A CB  1 
ATOM   1534 C CG  . LYS A 1 189 ? 57.100 20.133 -29.735 1.00 14.20 ? 189  LYS A CG  1 
ATOM   1535 C CD  . LYS A 1 189 ? 55.731 20.789 -29.877 1.00 19.00 ? 189  LYS A CD  1 
ATOM   1536 C CE  . LYS A 1 189 ? 55.291 20.874 -31.329 1.00 31.99 ? 189  LYS A CE  1 
ATOM   1537 N NZ  . LYS A 1 189 ? 53.929 21.466 -31.444 1.00 31.66 ? 189  LYS A NZ  1 
ATOM   1538 N N   . LEU A 1 190 ? 59.986 22.070 -28.065 1.00 6.41  ? 190  LEU A N   1 
ATOM   1539 C CA  . LEU A 1 190 ? 60.728 23.162 -28.696 1.00 9.72  ? 190  LEU A CA  1 
ATOM   1540 C C   . LEU A 1 190 ? 62.233 22.923 -28.657 1.00 8.26  ? 190  LEU A C   1 
ATOM   1541 O O   . LEU A 1 190 ? 62.956 23.377 -29.553 1.00 8.04  ? 190  LEU A O   1 
ATOM   1542 C CB  . LEU A 1 190 ? 60.390 24.508 -28.038 1.00 6.62  ? 190  LEU A CB  1 
ATOM   1543 C CG  . LEU A 1 190 ? 58.916 24.934 -28.169 1.00 11.72 ? 190  LEU A CG  1 
ATOM   1544 C CD1 . LEU A 1 190 ? 58.747 26.410 -27.826 1.00 9.40  ? 190  LEU A CD1 1 
ATOM   1545 C CD2 . LEU A 1 190 ? 58.345 24.641 -29.573 1.00 10.91 ? 190  LEU A CD2 1 
ATOM   1546 N N   . GLY A 1 191 ? 62.725 22.219 -27.636 1.00 7.74  ? 191  GLY A N   1 
ATOM   1547 C CA  . GLY A 1 191 ? 64.157 21.968 -27.546 1.00 7.99  ? 191  GLY A CA  1 
ATOM   1548 C C   . GLY A 1 191 ? 64.672 20.969 -28.568 1.00 9.48  ? 191  GLY A C   1 
ATOM   1549 O O   . GLY A 1 191 ? 65.786 21.121 -29.075 1.00 8.67  ? 191  GLY A O   1 
ATOM   1550 N N   . TYR A 1 192 ? 63.864 19.961 -28.908 1.00 8.50  ? 192  TYR A N   1 
ATOM   1551 C CA  . TYR A 1 192 ? 64.301 18.812 -29.702 1.00 8.10  ? 192  TYR A CA  1 
ATOM   1552 C C   . TYR A 1 192 ? 63.459 18.577 -30.948 1.00 9.83  ? 192  TYR A C   1 
ATOM   1553 O O   . TYR A 1 192 ? 63.768 17.667 -31.732 1.00 8.90  ? 192  TYR A O   1 
ATOM   1554 C CB  . TYR A 1 192 ? 64.292 17.545 -28.819 1.00 7.99  ? 192  TYR A CB  1 
ATOM   1555 C CG  . TYR A 1 192 ? 65.167 17.773 -27.613 1.00 8.09  ? 192  TYR A CG  1 
ATOM   1556 C CD1 . TYR A 1 192 ? 66.553 17.654 -27.708 1.00 8.41  ? 192  TYR A CD1 1 
ATOM   1557 C CD2 . TYR A 1 192 ? 64.625 18.233 -26.415 1.00 7.68  ? 192  TYR A CD2 1 
ATOM   1558 C CE1 . TYR A 1 192 ? 67.377 17.935 -26.620 1.00 7.06  ? 192  TYR A CE1 1 
ATOM   1559 C CE2 . TYR A 1 192 ? 65.431 18.513 -25.327 1.00 8.25  ? 192  TYR A CE2 1 
ATOM   1560 C CZ  . TYR A 1 192 ? 66.801 18.354 -25.430 1.00 9.68  ? 192  TYR A CZ  1 
ATOM   1561 O OH  . TYR A 1 192 ? 67.606 18.638 -24.351 1.00 9.20  ? 192  TYR A OH  1 
ATOM   1562 N N   . PHE A 1 193 ? 62.402 19.353 -31.157 1.00 9.63  ? 193  PHE A N   1 
ATOM   1563 C CA  . PHE A 1 193 ? 61.557 19.125 -32.323 1.00 8.47  ? 193  PHE A CA  1 
ATOM   1564 C C   . PHE A 1 193 ? 60.832 20.416 -32.666 1.00 10.77 ? 193  PHE A C   1 
ATOM   1565 O O   . PHE A 1 193 ? 59.648 20.393 -33.011 1.00 10.24 ? 193  PHE A O   1 
ATOM   1566 C CB  . PHE A 1 193 ? 60.562 17.982 -32.061 1.00 9.08  ? 193  PHE A CB  1 
ATOM   1567 C CG  . PHE A 1 193 ? 60.096 17.272 -33.314 1.00 8.48  ? 193  PHE A CG  1 
ATOM   1568 C CD1 . PHE A 1 193 ? 60.981 16.487 -34.046 1.00 10.46 ? 193  PHE A CD1 1 
ATOM   1569 C CD2 . PHE A 1 193 ? 58.770 17.377 -33.746 1.00 10.11 ? 193  PHE A CD2 1 
ATOM   1570 C CE1 . PHE A 1 193 ? 60.562 15.817 -35.203 1.00 8.77  ? 193  PHE A CE1 1 
ATOM   1571 C CE2 . PHE A 1 193 ? 58.332 16.721 -34.910 1.00 11.37 ? 193  PHE A CE2 1 
ATOM   1572 C CZ  . PHE A 1 193 ? 59.240 15.932 -35.639 1.00 10.13 ? 193  PHE A CZ  1 
ATOM   1573 N N   . GLY A 1 194 ? 61.528 21.547 -32.522 1.00 11.73 ? 194  GLY A N   1 
ATOM   1574 C CA  . GLY A 1 194 ? 60.963 22.841 -32.857 1.00 10.21 ? 194  GLY A CA  1 
ATOM   1575 C C   . GLY A 1 194 ? 62.066 23.754 -33.343 1.00 12.92 ? 194  GLY A C   1 
ATOM   1576 O O   . GLY A 1 194 ? 62.344 24.792 -32.734 1.00 10.73 ? 194  GLY A O   1 
ATOM   1577 N N   . ARG A 1 195 ? 62.710 23.368 -34.450 1.00 9.58  ? 195  ARG A N   1 
ATOM   1578 C CA  . ARG A 1 195 ? 63.941 24.041 -34.851 1.00 11.25 ? 195  ARG A CA  1 
ATOM   1579 C C   . ARG A 1 195 ? 63.731 25.532 -35.094 1.00 14.31 ? 195  ARG A C   1 
ATOM   1580 O O   . ARG A 1 195 ? 64.645 26.328 -34.852 1.00 14.77 ? 195  ARG A O   1 
ATOM   1581 C CB  . ARG A 1 195 ? 64.525 23.395 -36.109 1.00 16.60 ? 195  ARG A CB  1 
ATOM   1582 C CG  . ARG A 1 195 ? 65.842 24.052 -36.554 1.00 20.27 ? 195  ARG A CG  1 
ATOM   1583 C CD  . ARG A 1 195 ? 67.028 23.370 -35.891 1.00 20.78 ? 195  ARG A CD  1 
ATOM   1584 N NE  . ARG A 1 195 ? 67.653 22.538 -36.902 1.00 26.78 ? 195  ARG A NE  1 
ATOM   1585 C CZ  . ARG A 1 195 ? 68.554 21.603 -36.673 1.00 27.04 ? 195  ARG A CZ  1 
ATOM   1586 N NH1 . ARG A 1 195 ? 68.986 21.338 -35.447 1.00 17.04 ? 195  ARG A NH1 1 
ATOM   1587 N NH2 . ARG A 1 195 ? 69.030 20.912 -37.705 1.00 33.87 ? 195  ARG A NH2 1 
ATOM   1588 N N   . LEU A 1 196 ? 62.553 25.939 -35.572 1.00 9.94  ? 196  LEU A N   1 
ATOM   1589 C CA  . LEU A 1 196 ? 62.333 27.360 -35.840 1.00 13.91 ? 196  LEU A CA  1 
ATOM   1590 C C   . LEU A 1 196 ? 61.908 28.148 -34.603 1.00 14.94 ? 196  LEU A C   1 
ATOM   1591 O O   . LEU A 1 196 ? 61.718 29.367 -34.692 1.00 15.65 ? 196  LEU A O   1 
ATOM   1592 C CB  . LEU A 1 196 ? 61.293 27.531 -36.953 1.00 12.16 ? 196  LEU A CB  1 
ATOM   1593 C CG  . LEU A 1 196 ? 61.703 26.813 -38.240 1.00 14.69 ? 196  LEU A CG  1 
ATOM   1594 C CD1 . LEU A 1 196 ? 60.635 26.963 -39.327 1.00 17.09 ? 196  LEU A CD1 1 
ATOM   1595 C CD2 . LEU A 1 196 ? 63.057 27.329 -38.711 1.00 15.55 ? 196  LEU A CD2 1 
ATOM   1596 N N   . SER A 1 197 ? 61.797 27.508 -33.449 1.00 11.38 ? 197  SER A N   1 
ATOM   1597 C CA  . SER A 1 197 ? 61.336 28.195 -32.251 1.00 12.31 ? 197  SER A CA  1 
ATOM   1598 C C   . SER A 1 197 ? 62.451 28.882 -31.464 1.00 11.84 ? 197  SER A C   1 
ATOM   1599 O O   . SER A 1 197 ? 62.157 29.756 -30.646 1.00 14.89 ? 197  SER A O   1 
ATOM   1600 C CB  . SER A 1 197 ? 60.624 27.207 -31.332 1.00 12.51 ? 197  SER A CB  1 
ATOM   1601 O OG  . SER A 1 197 ? 61.594 26.451 -30.610 1.00 12.89 ? 197  SER A OG  1 
ATOM   1602 N N   . GLY A 1 198 ? 63.705 28.485 -31.658 1.00 11.42 ? 198  GLY A N   1 
ATOM   1603 C CA  . GLY A 1 198 ? 64.845 29.093 -30.956 1.00 10.14 ? 198  GLY A CA  1 
ATOM   1604 C C   . GLY A 1 198 ? 65.049 28.632 -29.510 1.00 12.55 ? 198  GLY A C   1 
ATOM   1605 O O   . GLY A 1 198 ? 65.815 29.294 -28.807 1.00 13.79 ? 198  GLY A O   1 
ATOM   1606 N N   . PHE A 1 199 ? 64.399 27.550 -29.097 1.00 9.12  ? 199  PHE A N   1 
ATOM   1607 C CA  . PHE A 1 199 ? 64.627 27.009 -27.737 1.00 9.19  ? 199  PHE A CA  1 
ATOM   1608 C C   . PHE A 1 199 ? 65.855 26.092 -27.735 1.00 9.85  ? 199  PHE A C   1 
ATOM   1609 O O   . PHE A 1 199 ? 66.047 25.348 -28.687 1.00 9.71  ? 199  PHE A O   1 
ATOM   1610 C CB  . PHE A 1 199 ? 63.390 26.293 -27.191 1.00 9.60  ? 199  PHE A CB  1 
ATOM   1611 C CG  . PHE A 1 199 ? 62.400 27.175 -26.480 1.00 10.73 ? 199  PHE A CG  1 
ATOM   1612 C CD1 . PHE A 1 199 ? 61.927 28.331 -27.074 1.00 9.72  ? 199  PHE A CD1 1 
ATOM   1613 C CD2 . PHE A 1 199 ? 61.938 26.845 -25.219 1.00 9.17  ? 199  PHE A CD2 1 
ATOM   1614 C CE1 . PHE A 1 199 ? 61.019 29.143 -26.419 1.00 9.90  ? 199  PHE A CE1 1 
ATOM   1615 C CE2 . PHE A 1 199 ? 61.028 27.658 -24.564 1.00 11.95 ? 199  PHE A CE2 1 
ATOM   1616 C CZ  . PHE A 1 199 ? 60.571 28.803 -25.166 1.00 10.86 ? 199  PHE A CZ  1 
ATOM   1617 N N   . PRO A 1 200 ? 66.673 26.122 -26.657 1.00 10.14 ? 200  PRO A N   1 
ATOM   1618 C CA  . PRO A 1 200 ? 67.858 25.257 -26.549 1.00 10.19 ? 200  PRO A CA  1 
ATOM   1619 C C   . PRO A 1 200 ? 67.492 23.777 -26.351 1.00 10.64 ? 200  PRO A C   1 
ATOM   1620 O O   . PRO A 1 200 ? 66.479 23.528 -25.752 1.00 9.24  ? 200  PRO A O   1 
ATOM   1621 C CB  . PRO A 1 200 ? 68.573 25.747 -25.284 1.00 7.94  ? 200  PRO A CB  1 
ATOM   1622 C CG  . PRO A 1 200 ? 67.460 26.323 -24.438 1.00 9.66  ? 200  PRO A CG  1 
ATOM   1623 C CD  . PRO A 1 200 ? 66.528 26.954 -25.448 1.00 9.17  ? 200  PRO A CD  1 
ATOM   1624 N N   . PRO A 1 201 ? 68.312 22.800 -26.815 1.00 10.16 ? 201  PRO A N   1 
ATOM   1625 C CA  . PRO A 1 201 ? 69.512 23.026 -27.634 1.00 9.20  ? 201  PRO A CA  1 
ATOM   1626 C C   . PRO A 1 201 ? 69.237 23.129 -29.152 1.00 9.16  ? 201  PRO A C   1 
ATOM   1627 O O   . PRO A 1 201 ? 70.159 23.054 -29.906 1.00 10.26 ? 201  PRO A O   1 
ATOM   1628 C CB  . PRO A 1 201 ? 70.325 21.760 -27.337 1.00 10.14 ? 201  PRO A CB  1 
ATOM   1629 C CG  . PRO A 1 201 ? 69.295 20.681 -27.233 1.00 9.07  ? 201  PRO A CG  1 
ATOM   1630 C CD  . PRO A 1 201 ? 68.115 21.363 -26.582 1.00 10.55 ? 201  PRO A CD  1 
ATOM   1631 N N   . SER A 1 202 ? 67.969 23.302 -29.524 1.00 9.51  ? 202  SER A N   1 
ATOM   1632 C CA  . SER A 1 202 ? 67.540 23.378 -30.949 1.00 9.63  ? 202  SER A CA  1 
ATOM   1633 C C   . SER A 1 202 ? 67.981 22.143 -31.762 1.00 13.09 ? 202  SER A C   1 
ATOM   1634 O O   . SER A 1 202 ? 68.455 22.325 -32.877 1.00 8.84  ? 202  SER A O   1 
ATOM   1635 C CB  . SER A 1 202 ? 67.902 24.690 -31.641 1.00 11.21 ? 202  SER A CB  1 
ATOM   1636 O OG  . SER A 1 202 ? 67.065 24.921 -32.757 1.00 14.57 ? 202  SER A OG  1 
ATOM   1637 N N   . LEU A 1 203 ? 67.867 20.944 -31.189 1.00 9.89  ? 203  LEU A N   1 
ATOM   1638 C CA  . LEU A 1 203 ? 68.057 19.746 -31.994 1.00 11.49 ? 203  LEU A CA  1 
ATOM   1639 C C   . LEU A 1 203 ? 66.786 19.465 -32.785 1.00 12.69 ? 203  LEU A C   1 
ATOM   1640 O O   . LEU A 1 203 ? 65.728 20.042 -32.525 1.00 9.86  ? 203  LEU A O   1 
ATOM   1641 C CB  . LEU A 1 203 ? 68.409 18.549 -31.113 1.00 7.43  ? 203  LEU A CB  1 
ATOM   1642 C CG  . LEU A 1 203 ? 69.698 18.712 -30.301 1.00 9.73  ? 203  LEU A CG  1 
ATOM   1643 C CD1 . LEU A 1 203 ? 70.012 17.472 -29.488 1.00 10.60 ? 203  LEU A CD1 1 
ATOM   1644 C CD2 . LEU A 1 203 ? 70.870 19.087 -31.192 1.00 17.64 ? 203  LEU A CD2 1 
ATOM   1645 N N   . LEU A 1 204 ? 66.886 18.558 -33.758 1.00 10.14 ? 204  LEU A N   1 
ATOM   1646 C CA  . LEU A 1 204 ? 65.728 18.174 -34.570 1.00 10.55 ? 204  LEU A CA  1 
ATOM   1647 C C   . LEU A 1 204 ? 65.744 16.648 -34.665 1.00 10.20 ? 204  LEU A C   1 
ATOM   1648 O O   . LEU A 1 204 ? 66.319 16.081 -35.594 1.00 9.91  ? 204  LEU A O   1 
ATOM   1649 C CB  . LEU A 1 204 ? 65.770 18.854 -35.942 1.00 10.74 ? 204  LEU A CB  1 
ATOM   1650 C CG  . LEU A 1 204 ? 64.405 19.047 -36.607 1.00 14.39 ? 204  LEU A CG  1 
ATOM   1651 C CD1 . LEU A 1 204 ? 64.496 19.891 -37.880 1.00 16.23 ? 204  LEU A CD1 1 
ATOM   1652 C CD2 . LEU A 1 204 ? 63.782 17.720 -36.918 1.00 11.19 ? 204  LEU A CD2 1 
ATOM   1653 N N   . ASN A 1 205 ? 65.092 15.987 -33.710 1.00 6.84  ? 205  ASN A N   1 
ATOM   1654 C CA  . ASN A 1 205 ? 65.178 14.529 -33.593 1.00 10.22 ? 205  ASN A CA  1 
ATOM   1655 C C   . ASN A 1 205 ? 64.004 14.050 -32.751 1.00 9.56  ? 205  ASN A C   1 
ATOM   1656 O O   . ASN A 1 205 ? 64.001 14.237 -31.526 1.00 7.27  ? 205  ASN A O   1 
ATOM   1657 C CB  . ASN A 1 205 ? 66.513 14.111 -32.971 1.00 11.11 ? 205  ASN A CB  1 
ATOM   1658 C CG  . ASN A 1 205 ? 66.741 12.604 -33.021 1.00 12.76 ? 205  ASN A CG  1 
ATOM   1659 O OD1 . ASN A 1 205 ? 65.796 11.815 -32.965 1.00 14.17 ? 205  ASN A OD1 1 
ATOM   1660 N ND2 . ASN A 1 205 ? 68.002 12.200 -33.131 1.00 15.19 ? 205  ASN A ND2 1 
ATOM   1661 N N   . ILE A 1 206 ? 63.022 13.429 -33.403 1.00 7.11  ? 206  ILE A N   1 
ATOM   1662 C CA  . ILE A 1 206 ? 61.822 12.987 -32.690 1.00 9.67  ? 206  ILE A CA  1 
ATOM   1663 C C   . ILE A 1 206 ? 62.171 12.061 -31.524 1.00 10.38 ? 206  ILE A C   1 
ATOM   1664 O O   . ILE A 1 206 ? 61.473 12.052 -30.501 1.00 9.50  ? 206  ILE A O   1 
ATOM   1665 C CB  . ILE A 1 206 ? 60.838 12.317 -33.681 1.00 10.53 ? 206  ILE A CB  1 
ATOM   1666 C CG1 . ILE A 1 206 ? 59.477 12.096 -33.012 1.00 12.75 ? 206  ILE A CG1 1 
ATOM   1667 C CG2 . ILE A 1 206 ? 61.431 11.012 -34.253 1.00 9.38  ? 206  ILE A CG2 1 
ATOM   1668 C CD1 . ILE A 1 206 ? 58.378 11.644 -33.960 1.00 14.41 ? 206  ILE A CD1 1 
ATOM   1669 N N   . ASP A 1 207 ? 63.247 11.273 -31.649 1.00 11.88 ? 207  ASP A N   1 
ATOM   1670 C CA  . ASP A 1 207 ? 63.622 10.362 -30.569 1.00 9.85  ? 207  ASP A CA  1 
ATOM   1671 C C   . ASP A 1 207 ? 64.108 11.117 -29.334 1.00 11.61 ? 207  ASP A C   1 
ATOM   1672 O O   . ASP A 1 207 ? 63.901 10.655 -28.209 1.00 8.88  ? 207  ASP A O   1 
ATOM   1673 C CB  . ASP A 1 207 ? 64.699 9.378  -31.043 1.00 11.40 ? 207  ASP A CB  1 
ATOM   1674 C CG  . ASP A 1 207 ? 64.195 8.427  -32.122 1.00 13.70 ? 207  ASP A CG  1 
ATOM   1675 O OD1 . ASP A 1 207 ? 62.983 8.133  -32.164 1.00 12.13 ? 207  ASP A OD1 1 
ATOM   1676 O OD2 . ASP A 1 207 ? 65.016 7.975  -32.937 1.00 15.69 ? 207  ASP A OD2 1 
ATOM   1677 N N   . LEU A 1 208 ? 64.750 12.273 -29.516 1.00 9.03  ? 208  LEU A N   1 
ATOM   1678 C CA  . LEU A 1 208 ? 65.197 13.053 -28.363 1.00 11.96 ? 208  LEU A CA  1 
ATOM   1679 C C   . LEU A 1 208 ? 64.038 13.822 -27.746 1.00 9.88  ? 208  LEU A C   1 
ATOM   1680 O O   . LEU A 1 208 ? 63.979 13.988 -26.529 1.00 10.14 ? 208  LEU A O   1 
ATOM   1681 C CB  . LEU A 1 208 ? 66.319 14.003 -28.778 1.00 8.44  ? 208  LEU A CB  1 
ATOM   1682 C CG  . LEU A 1 208 ? 67.497 13.246 -29.381 1.00 12.01 ? 208  LEU A CG  1 
ATOM   1683 C CD1 . LEU A 1 208 ? 68.647 14.176 -29.745 1.00 12.57 ? 208  LEU A CD1 1 
ATOM   1684 C CD2 . LEU A 1 208 ? 67.974 12.149 -28.424 1.00 14.38 ? 208  LEU A CD2 1 
ATOM   1685 N N   . TYR A 1 209 ? 63.122 14.308 -28.583 1.00 11.67 ? 209  TYR A N   1 
ATOM   1686 C CA  . TYR A 1 209 ? 61.850 14.836 -28.104 1.00 9.46  ? 209  TYR A CA  1 
ATOM   1687 C C   . TYR A 1 209 ? 61.166 13.820 -27.190 1.00 9.46  ? 209  TYR A C   1 
ATOM   1688 O O   . TYR A 1 209 ? 60.761 14.143 -26.067 1.00 8.30  ? 209  TYR A O   1 
ATOM   1689 C CB  . TYR A 1 209 ? 61.007 15.190 -29.338 1.00 8.51  ? 209  TYR A CB  1 
ATOM   1690 C CG  . TYR A 1 209 ? 59.561 15.632 -29.163 1.00 12.46 ? 209  TYR A CG  1 
ATOM   1691 C CD1 . TYR A 1 209 ? 59.078 16.160 -27.967 1.00 9.33  ? 209  TYR A CD1 1 
ATOM   1692 C CD2 . TYR A 1 209 ? 58.685 15.558 -30.247 1.00 13.07 ? 209  TYR A CD2 1 
ATOM   1693 C CE1 . TYR A 1 209 ? 57.741 16.574 -27.859 1.00 8.88  ? 209  TYR A CE1 1 
ATOM   1694 C CE2 . TYR A 1 209 ? 57.373 15.966 -30.152 1.00 14.39 ? 209  TYR A CE2 1 
ATOM   1695 C CZ  . TYR A 1 209 ? 56.902 16.476 -28.968 1.00 11.78 ? 209  TYR A CZ  1 
ATOM   1696 O OH  . TYR A 1 209 ? 55.572 16.863 -28.938 1.00 11.92 ? 209  TYR A OH  1 
ATOM   1697 N N   . GLU A 1 210 ? 61.091 12.563 -27.635 1.00 9.21  ? 210  GLU A N   1 
ATOM   1698 C CA  . GLU A 1 210 ? 60.467 11.524 -26.820 1.00 10.96 ? 210  GLU A CA  1 
ATOM   1699 C C   . GLU A 1 210 ? 61.240 11.304 -25.525 1.00 8.28  ? 210  GLU A C   1 
ATOM   1700 O O   . GLU A 1 210 ? 60.645 11.137 -24.456 1.00 10.29 ? 210  GLU A O   1 
ATOM   1701 C CB  . GLU A 1 210 ? 60.376 10.221 -27.620 1.00 9.70  ? 210  GLU A CB  1 
ATOM   1702 C CG  . GLU A 1 210 ? 59.846 9.010  -26.863 1.00 12.99 ? 210  GLU A CG  1 
ATOM   1703 C CD  . GLU A 1 210 ? 59.839 7.759  -27.749 1.00 17.90 ? 210  GLU A CD  1 
ATOM   1704 O OE1 . GLU A 1 210 ? 59.814 6.623  -27.226 1.00 14.62 ? 210  GLU A OE1 1 
ATOM   1705 O OE2 . GLU A 1 210 ? 59.886 7.921  -28.983 1.00 18.38 ? 210  GLU A OE2 1 
ATOM   1706 N N   . LYS A 1 211 ? 62.570 11.298 -25.601 1.00 10.62 ? 211  LYS A N   1 
ATOM   1707 C CA  . LYS A 1 211 ? 63.367 11.070 -24.401 1.00 10.42 ? 211  LYS A CA  1 
ATOM   1708 C C   . LYS A 1 211 ? 63.189 12.190 -23.381 1.00 10.99 ? 211  LYS A C   1 
ATOM   1709 O O   . LYS A 1 211 ? 63.105 11.929 -22.174 1.00 9.86  ? 211  LYS A O   1 
ATOM   1710 C CB  . LYS A 1 211 ? 64.844 10.916 -24.765 1.00 9.85  ? 211  LYS A CB  1 
ATOM   1711 C CG  . LYS A 1 211 ? 65.698 10.604 -23.546 1.00 18.73 ? 211  LYS A CG  1 
ATOM   1712 C CD  . LYS A 1 211 ? 67.164 10.885 -23.811 1.00 24.50 ? 211  LYS A CD  1 
ATOM   1713 C CE  . LYS A 1 211 ? 67.936 9.584  -23.953 1.00 38.23 ? 211  LYS A CE  1 
ATOM   1714 N NZ  . LYS A 1 211 ? 67.569 8.658  -22.835 1.00 42.16 ? 211  LYS A NZ  1 
ATOM   1715 N N   . ALA A 1 212 ? 63.145 13.443 -23.841 1.00 8.08  ? 212  ALA A N   1 
ATOM   1716 C CA  . ALA A 1 212 ? 63.016 14.576 -22.919 1.00 8.37  ? 212  ALA A CA  1 
ATOM   1717 C C   . ALA A 1 212 ? 61.632 14.620 -22.272 1.00 9.50  ? 212  ALA A C   1 
ATOM   1718 O O   . ALA A 1 212 ? 61.500 14.974 -21.093 1.00 8.49  ? 212  ALA A O   1 
ATOM   1719 C CB  . ALA A 1 212 ? 63.298 15.884 -23.658 1.00 7.30  ? 212  ALA A CB  1 
ATOM   1720 N N   . LEU A 1 213 ? 60.584 14.313 -23.041 1.00 8.24  ? 213  LEU A N   1 
ATOM   1721 C CA  . LEU A 1 213 ? 59.254 14.145 -22.461 1.00 10.79 ? 213  LEU A CA  1 
ATOM   1722 C C   . LEU A 1 213 ? 59.267 13.102 -21.349 1.00 13.57 ? 213  LEU A C   1 
ATOM   1723 O O   . LEU A 1 213 ? 58.729 13.325 -20.255 1.00 11.34 ? 213  LEU A O   1 
ATOM   1724 C CB  . LEU A 1 213 ? 58.259 13.715 -23.547 1.00 12.31 ? 213  LEU A CB  1 
ATOM   1725 C CG  . LEU A 1 213 ? 57.604 14.712 -24.513 1.00 16.78 ? 213  LEU A CG  1 
ATOM   1726 C CD1 . LEU A 1 213 ? 56.685 13.936 -25.452 1.00 12.76 ? 213  LEU A CD1 1 
ATOM   1727 C CD2 . LEU A 1 213 ? 56.829 15.847 -23.799 1.00 9.93  ? 213  LEU A CD2 1 
ATOM   1728 N N   . ASP A 1 214 ? 59.870 11.941 -21.623 1.00 10.16 ? 214  ASP A N   1 
ATOM   1729 C CA  . ASP A 1 214 ? 59.753 10.823 -20.695 1.00 13.72 ? 214  ASP A CA  1 
ATOM   1730 C C   . ASP A 1 214 ? 60.600 11.039 -19.446 1.00 11.87 ? 214  ASP A C   1 
ATOM   1731 O O   . ASP A 1 214 ? 60.180 10.665 -18.347 1.00 11.64 ? 214  ASP A O   1 
ATOM   1732 C CB  . ASP A 1 214 ? 60.125 9.518  -21.397 1.00 12.36 ? 214  ASP A CB  1 
ATOM   1733 C CG  . ASP A 1 214 ? 59.054 9.074  -22.379 1.00 18.59 ? 214  ASP A CG  1 
ATOM   1734 O OD1 . ASP A 1 214 ? 57.949 9.652  -22.337 1.00 16.35 ? 214  ASP A OD1 1 
ATOM   1735 O OD2 . ASP A 1 214 ? 59.318 8.163  -23.191 1.00 14.14 ? 214  ASP A OD2 1 
ATOM   1736 N N   . ASN A 1 215 ? 61.788 11.640 -19.587 1.00 9.76  ? 215  ASN A N   1 
ATOM   1737 C CA  . ASN A 1 215 ? 62.571 11.987 -18.398 1.00 11.49 ? 215  ASN A CA  1 
ATOM   1738 C C   . ASN A 1 215 ? 61.881 13.046 -17.537 1.00 12.24 ? 215  ASN A C   1 
ATOM   1739 O O   . ASN A 1 215 ? 61.983 13.006 -16.304 1.00 10.83 ? 215  ASN A O   1 
ATOM   1740 C CB  . ASN A 1 215 ? 63.969 12.454 -18.802 1.00 9.35  ? 215  ASN A CB  1 
ATOM   1741 C CG  . ASN A 1 215 ? 64.923 11.284 -18.985 1.00 19.28 ? 215  ASN A CG  1 
ATOM   1742 O OD1 . ASN A 1 215 ? 64.593 10.164 -18.607 1.00 12.08 ? 215  ASN A OD1 1 
ATOM   1743 N ND2 . ASN A 1 215 ? 66.093 11.531 -19.565 1.00 14.21 ? 215  ASN A ND2 1 
ATOM   1744 N N   . GLN A 1 216 ? 61.172 13.996 -18.151 1.00 10.04 ? 216  GLN A N   1 
ATOM   1745 C CA  . GLN A 1 216 ? 60.431 14.948 -17.328 1.00 9.33  ? 216  GLN A CA  1 
ATOM   1746 C C   . GLN A 1 216 ? 59.230 14.291 -16.642 1.00 9.53  ? 216  GLN A C   1 
ATOM   1747 O O   . GLN A 1 216 ? 58.892 14.662 -15.512 1.00 9.73  ? 216  GLN A O   1 
ATOM   1748 C CB  . GLN A 1 216 ? 60.003 16.152 -18.163 1.00 9.35  ? 216  GLN A CB  1 
ATOM   1749 C CG  . GLN A 1 216 ? 61.177 17.084 -18.500 1.00 9.46  ? 216  GLN A CG  1 
ATOM   1750 C CD  . GLN A 1 216 ? 60.763 18.268 -19.357 1.00 11.06 ? 216  GLN A CD  1 
ATOM   1751 O OE1 . GLN A 1 216 ? 60.615 19.386 -18.864 1.00 11.10 ? 216  GLN A OE1 1 
ATOM   1752 N NE2 . GLN A 1 216 ? 60.569 18.024 -20.648 1.00 9.43  ? 216  GLN A NE2 1 
ATOM   1753 N N   . ILE A 1 217 ? 58.578 13.324 -17.291 1.00 9.45  ? 217  ILE A N   1 
ATOM   1754 C CA  . ILE A 1 217 ? 57.504 12.582 -16.627 1.00 10.05 ? 217  ILE A CA  1 
ATOM   1755 C C   . ILE A 1 217 ? 58.051 11.867 -15.395 1.00 11.31 ? 217  ILE A C   1 
ATOM   1756 O O   . ILE A 1 217 ? 57.487 11.955 -14.294 1.00 11.12 ? 217  ILE A O   1 
ATOM   1757 C CB  . ILE A 1 217 ? 56.850 11.590 -17.609 1.00 12.91 ? 217  ILE A CB  1 
ATOM   1758 C CG1 . ILE A 1 217 ? 56.010 12.321 -18.652 1.00 9.89  ? 217  ILE A CG1 1 
ATOM   1759 C CG2 . ILE A 1 217 ? 56.017 10.527 -16.859 1.00 10.22 ? 217  ILE A CG2 1 
ATOM   1760 C CD1 . ILE A 1 217 ? 55.642 11.445 -19.867 1.00 12.53 ? 217  ILE A CD1 1 
ATOM   1761 N N   . LEU A 1 218 ? 59.178 11.164 -15.560 1.00 11.18 ? 218  LEU A N   1 
ATOM   1762 C CA  . LEU A 1 218 ? 59.818 10.465 -14.447 1.00 12.62 ? 218  LEU A CA  1 
ATOM   1763 C C   . LEU A 1 218 ? 60.223 11.435 -13.348 1.00 14.57 ? 218  LEU A C   1 
ATOM   1764 O O   . LEU A 1 218 ? 60.020 11.170 -12.160 1.00 12.03 ? 218  LEU A O   1 
ATOM   1765 C CB  . LEU A 1 218 ? 61.064 9.733  -14.945 1.00 13.59 ? 218  LEU A CB  1 
ATOM   1766 C CG  . LEU A 1 218 ? 60.937 8.368  -15.610 1.00 18.08 ? 218  LEU A CG  1 
ATOM   1767 C CD1 . LEU A 1 218 ? 62.278 8.016  -16.262 1.00 19.44 ? 218  LEU A CD1 1 
ATOM   1768 C CD2 . LEU A 1 218 ? 60.500 7.310  -14.606 1.00 20.00 ? 218  LEU A CD2 1 
ATOM   1769 N N   . ALA A 1 219 ? 60.868 12.540 -13.731 1.00 11.13 ? 219  ALA A N   1 
ATOM   1770 C CA  . ALA A 1 219 ? 61.285 13.531 -12.750 1.00 12.83 ? 219  ALA A CA  1 
ATOM   1771 C C   . ALA A 1 219 ? 60.091 14.069 -11.963 1.00 12.10 ? 219  ALA A C   1 
ATOM   1772 O O   . ALA A 1 219 ? 60.148 14.179 -10.731 1.00 10.33 ? 219  ALA A O   1 
ATOM   1773 C CB  . ALA A 1 219 ? 62.039 14.661 -13.455 1.00 9.85  ? 219  ALA A CB  1 
ATOM   1774 N N   . HIS A 1 220 ? 58.989 14.389 -12.649 1.00 10.83 ? 220  HIS A N   1 
ATOM   1775 C CA  . HIS A 1 220 ? 57.822 14.887 -11.930 1.00 8.45  ? 220  HIS A CA  1 
ATOM   1776 C C   . HIS A 1 220 ? 57.297 13.860 -10.936 1.00 11.75 ? 220  HIS A C   1 
ATOM   1777 O O   . HIS A 1 220 ? 56.998 14.196 -9.784  1.00 10.52 ? 220  HIS A O   1 
ATOM   1778 C CB  . HIS A 1 220 ? 56.672 15.256 -12.857 1.00 7.21  ? 220  HIS A CB  1 
ATOM   1779 C CG  . HIS A 1 220 ? 55.403 15.443 -12.092 1.00 10.30 ? 220  HIS A CG  1 
ATOM   1780 N ND1 . HIS A 1 220 ? 55.118 16.616 -11.425 1.00 8.92  ? 220  HIS A ND1 1 
ATOM   1781 C CD2 . HIS A 1 220 ? 54.423 14.568 -11.758 1.00 9.27  ? 220  HIS A CD2 1 
ATOM   1782 C CE1 . HIS A 1 220 ? 53.995 16.466 -10.743 1.00 10.46 ? 220  HIS A CE1 1 
ATOM   1783 N NE2 . HIS A 1 220 ? 53.553 15.234 -10.928 1.00 9.85  ? 220  HIS A NE2 1 
ATOM   1784 N N   . ASN A 1 221 ? 57.081 12.628 -11.386 1.00 8.15  ? 221  ASN A N   1 
ATOM   1785 C CA  . ASN A 1 221 ? 56.479 11.581 -10.522 1.00 12.05 ? 221  ASN A CA  1 
ATOM   1786 C C   . ASN A 1 221 ? 57.325 11.348 -9.259  1.00 11.71 ? 221  ASN A C   1 
ATOM   1787 O O   . ASN A 1 221 ? 56.771 11.247 -8.175  1.00 11.33 ? 221  ASN A O   1 
ATOM   1788 C CB  . ASN A 1 221 ? 56.211 10.317 -11.340 1.00 11.36 ? 221  ASN A CB  1 
ATOM   1789 C CG  . ASN A 1 221 ? 54.995 10.464 -12.235 1.00 12.04 ? 221  ASN A CG  1 
ATOM   1790 O OD1 . ASN A 1 221 ? 54.058 11.182 -11.904 1.00 11.74 ? 221  ASN A OD1 1 
ATOM   1791 N ND2 . ASN A 1 221 ? 54.999 9.794  -13.372 1.00 9.80  ? 221  ASN A ND2 1 
ATOM   1792 N N   . LYS A 1 222 ? 58.626 11.231 -9.439  1.00 12.04 ? 222  LYS A N   1 
ATOM   1793 C CA  . LYS A 1 222 ? 59.528 10.980 -8.292  1.00 12.57 ? 222  LYS A CA  1 
ATOM   1794 C C   . LYS A 1 222 ? 59.557 12.215 -7.373  1.00 13.88 ? 222  LYS A C   1 
ATOM   1795 O O   . LYS A 1 222 ? 59.635 12.050 -6.159  1.00 10.64 ? 222  LYS A O   1 
ATOM   1796 C CB  . LYS A 1 222 ? 60.895 10.585 -8.847  1.00 16.12 ? 222  LYS A CB  1 
ATOM   1797 C CG  . LYS A 1 222 ? 60.907 9.287  -9.634  1.00 20.75 ? 222  LYS A CG  1 
ATOM   1798 C CD  . LYS A 1 222 ? 62.265 8.928  -10.172 1.00 31.21 ? 222  LYS A CD  1 
ATOM   1799 C CE  . LYS A 1 222 ? 62.330 7.486  -10.625 1.00 41.14 ? 222  LYS A CE  1 
ATOM   1800 N NZ  . LYS A 1 222 ? 61.732 6.576  -9.621  1.00 43.29 ? 222  LYS A NZ  1 
ATOM   1801 N N   . ALA A 1 223 ? 59.530 13.399 -7.976  1.00 10.44 ? 223  ALA A N   1 
ATOM   1802 C CA  . ALA A 1 223 ? 59.569 14.637 -7.175  1.00 12.07 ? 223  ALA A CA  1 
ATOM   1803 C C   . ALA A 1 223 ? 58.299 14.714 -6.308  1.00 10.77 ? 223  ALA A C   1 
ATOM   1804 O O   . ALA A 1 223 ? 58.407 14.981 -5.130  1.00 12.59 ? 223  ALA A O   1 
ATOM   1805 C CB  . ALA A 1 223 ? 59.755 15.835 -8.070  1.00 10.37 ? 223  ALA A CB  1 
ATOM   1806 N N   . TYR A 1 224 ? 57.145 14.452 -6.914  1.00 10.71 ? 224  TYR A N   1 
ATOM   1807 C CA  . TYR A 1 224 ? 55.878 14.492 -6.133  1.00 13.34 ? 224  TYR A CA  1 
ATOM   1808 C C   . TYR A 1 224 ? 55.956 13.543 -4.921  1.00 14.18 ? 224  TYR A C   1 
ATOM   1809 O O   . TYR A 1 224 ? 55.635 13.952 -3.816  1.00 12.99 ? 224  TYR A O   1 
ATOM   1810 C CB  . TYR A 1 224 ? 54.677 14.167 -7.015  1.00 12.20 ? 224  TYR A CB  1 
ATOM   1811 C CG  . TYR A 1 224 ? 53.354 14.124 -6.299  1.00 15.24 ? 224  TYR A CG  1 
ATOM   1812 C CD1 . TYR A 1 224 ? 52.611 15.275 -6.097  1.00 11.45 ? 224  TYR A CD1 1 
ATOM   1813 C CD2 . TYR A 1 224 ? 52.837 12.928 -5.836  1.00 15.57 ? 224  TYR A CD2 1 
ATOM   1814 C CE1 . TYR A 1 224 ? 51.388 15.239 -5.451  1.00 12.88 ? 224  TYR A CE1 1 
ATOM   1815 C CE2 . TYR A 1 224 ? 51.618 12.874 -5.185  1.00 15.66 ? 224  TYR A CE2 1 
ATOM   1816 C CZ  . TYR A 1 224 ? 50.893 14.033 -4.989  1.00 13.96 ? 224  TYR A CZ  1 
ATOM   1817 O OH  . TYR A 1 224 ? 49.695 13.973 -4.351  1.00 15.48 ? 224  TYR A OH  1 
ATOM   1818 N N   . GLU A 1 225 ? 56.421 12.328 -5.151  1.00 14.16 ? 225  GLU A N   1 
ATOM   1819 C CA  . GLU A 1 225 ? 56.475 11.290 -4.090  1.00 17.34 ? 225  GLU A CA  1 
ATOM   1820 C C   . GLU A 1 225 ? 57.416 11.705 -2.946  1.00 16.07 ? 225  GLU A C   1 
ATOM   1821 O O   . GLU A 1 225 ? 57.038 11.531 -1.803  1.00 18.94 ? 225  GLU A O   1 
ATOM   1822 C CB  . GLU A 1 225 ? 56.876 9.953  -4.720  1.00 21.41 ? 225  GLU A CB  1 
ATOM   1823 N N   . THR A 1 226 ? 58.577 12.253 -3.271  1.00 13.45 ? 226  THR A N   1 
ATOM   1824 C CA  . THR A 1 226 ? 59.501 12.721 -2.215  1.00 16.75 ? 226  THR A CA  1 
ATOM   1825 C C   . THR A 1 226 ? 58.935 13.972 -1.526  1.00 19.26 ? 226  THR A C   1 
ATOM   1826 O O   . THR A 1 226 ? 58.956 14.011 -0.298  1.00 16.63 ? 226  THR A O   1 
ATOM   1827 C CB  . THR A 1 226 ? 60.925 12.960 -2.730  1.00 17.17 ? 226  THR A CB  1 
ATOM   1828 O OG1 . THR A 1 226 ? 61.739 13.235 -1.593  1.00 18.76 ? 226  THR A OG1 1 
ATOM   1829 C CG2 . THR A 1 226 ? 61.021 14.087 -3.734  1.00 13.36 ? 226  THR A CG2 1 
ATOM   1830 N N   . MET A 1 227 ? 58.436 14.934 -2.306  1.00 13.33 ? 227  MET A N   1 
ATOM   1831 C CA  . MET A 1 227 ? 57.996 16.166 -1.649  1.00 13.71 ? 227  MET A CA  1 
ATOM   1832 C C   . MET A 1 227 ? 56.820 15.913 -0.717  1.00 14.45 ? 227  MET A C   1 
ATOM   1833 O O   . MET A 1 227 ? 56.736 16.521 0.357   1.00 14.19 ? 227  MET A O   1 
ATOM   1834 C CB  . MET A 1 227 ? 57.628 17.258 -2.658  1.00 10.77 ? 227  MET A CB  1 
ATOM   1835 C CG  . MET A 1 227 ? 58.678 17.572 -3.717  1.00 11.48 ? 227  MET A CG  1 
ATOM   1836 S SD  . MET A 1 227 ? 58.009 18.704 -4.979  1.00 14.70 ? 227  MET A SD  1 
ATOM   1837 C CE  . MET A 1 227 ? 57.576 20.134 -4.007  1.00 10.79 ? 227  MET A CE  1 
ATOM   1838 N N   . LYS A 1 228 ? 55.894 15.031 -1.108  1.00 11.51 ? 228  LYS A N   1 
ATOM   1839 C CA  . LYS A 1 228 ? 54.747 14.754 -0.248  1.00 15.53 ? 228  LYS A CA  1 
ATOM   1840 C C   . LYS A 1 228 ? 55.165 14.116 1.072   1.00 19.57 ? 228  LYS A C   1 
ATOM   1841 O O   . LYS A 1 228 ? 54.368 14.098 2.013   1.00 21.45 ? 228  LYS A O   1 
ATOM   1842 C CB  . LYS A 1 228 ? 53.734 13.847 -0.955  1.00 15.00 ? 228  LYS A CB  1 
ATOM   1843 C CG  . LYS A 1 228 ? 53.005 14.502 -2.116  1.00 16.23 ? 228  LYS A CG  1 
ATOM   1844 C CD  . LYS A 1 228 ? 52.222 15.733 -1.674  1.00 22.34 ? 228  LYS A CD  1 
ATOM   1845 C CE  . LYS A 1 228 ? 50.766 15.371 -1.426  1.00 22.34 ? 228  LYS A CE  1 
ATOM   1846 N NZ  . LYS A 1 228 ? 49.961 16.550 -1.013  1.00 21.35 ? 228  LYS A NZ  1 
ATOM   1847 N N   . GLN A 1 229 ? 56.379 13.574 1.156   1.00 15.79 ? 229  GLN A N   1 
ATOM   1848 C CA  . GLN A 1 229 ? 56.856 13.038 2.424   1.00 21.83 ? 229  GLN A CA  1 
ATOM   1849 C C   . GLN A 1 229 ? 57.255 14.131 3.399   1.00 21.87 ? 229  GLN A C   1 
ATOM   1850 O O   . GLN A 1 229 ? 57.342 13.870 4.605   1.00 20.70 ? 229  GLN A O   1 
ATOM   1851 C CB  . GLN A 1 229 ? 58.056 12.118 2.208   1.00 18.62 ? 229  GLN A CB  1 
ATOM   1852 C CG  . GLN A 1 229 ? 57.684 10.699 1.839   1.00 24.39 ? 229  GLN A CG  1 
ATOM   1853 C CD  . GLN A 1 229 ? 58.875 9.902  1.354   1.00 33.80 ? 229  GLN A CD  1 
ATOM   1854 O OE1 . GLN A 1 229 ? 59.979 10.031 1.885   1.00 39.87 ? 229  GLN A OE1 1 
ATOM   1855 N NE2 . GLN A 1 229 ? 58.668 9.099  0.311   1.00 39.26 ? 229  GLN A NE2 1 
ATOM   1856 N N   . PHE A 1 230 ? 57.488 15.346 2.908   1.00 16.21 ? 230  PHE A N   1 
ATOM   1857 C CA  . PHE A 1 230 ? 58.063 16.403 3.719   1.00 19.85 ? 230  PHE A CA  1 
ATOM   1858 C C   . PHE A 1 230 ? 57.234 17.671 3.755   1.00 20.92 ? 230  PHE A C   1 
ATOM   1859 O O   . PHE A 1 230 ? 57.584 18.593 4.496   1.00 25.83 ? 230  PHE A O   1 
ATOM   1860 C CB  . PHE A 1 230 ? 59.479 16.729 3.218   1.00 18.30 ? 230  PHE A CB  1 
ATOM   1861 C CG  . PHE A 1 230 ? 60.400 15.553 3.286   1.00 21.40 ? 230  PHE A CG  1 
ATOM   1862 C CD1 . PHE A 1 230 ? 60.846 15.078 4.513   1.00 26.20 ? 230  PHE A CD1 1 
ATOM   1863 C CD2 . PHE A 1 230 ? 60.749 14.865 2.137   1.00 19.26 ? 230  PHE A CD2 1 
ATOM   1864 C CE1 . PHE A 1 230 ? 61.677 13.957 4.592   1.00 23.54 ? 230  PHE A CE1 1 
ATOM   1865 C CE2 . PHE A 1 230 ? 61.575 13.745 2.199   1.00 23.17 ? 230  PHE A CE2 1 
ATOM   1866 C CZ  . PHE A 1 230 ? 62.041 13.288 3.427   1.00 27.39 ? 230  PHE A CZ  1 
ATOM   1867 N N   . THR A 1 231 ? 56.152 17.752 2.992   1.00 17.68 ? 231  THR A N   1 
ATOM   1868 C CA  . THR A 1 231 ? 55.290 18.915 3.059   1.00 19.66 ? 231  THR A CA  1 
ATOM   1869 C C   . THR A 1 231 ? 53.846 18.458 3.074   1.00 20.04 ? 231  THR A C   1 
ATOM   1870 O O   . THR A 1 231 ? 53.496 17.425 2.499   1.00 22.24 ? 231  THR A O   1 
ATOM   1871 C CB  . THR A 1 231 ? 55.522 19.900 1.893   1.00 21.44 ? 231  THR A CB  1 
ATOM   1872 O OG1 . THR A 1 231 ? 54.623 21.005 2.028   1.00 24.83 ? 231  THR A OG1 1 
ATOM   1873 C CG2 . THR A 1 231 ? 55.281 19.241 0.533   1.00 14.02 ? 231  THR A CG2 1 
ATOM   1874 N N   . ASN A 1 232 ? 53.018 19.237 3.760   1.00 23.28 ? 232  ASN A N   1 
ATOM   1875 C CA  . ASN A 1 232 ? 51.571 19.105 3.733   1.00 25.84 ? 232  ASN A CA  1 
ATOM   1876 C C   . ASN A 1 232 ? 50.920 19.966 2.655   1.00 26.51 ? 232  ASN A C   1 
ATOM   1877 O O   . ASN A 1 232 ? 49.719 19.827 2.407   1.00 25.77 ? 232  ASN A O   1 
ATOM   1878 C CB  . ASN A 1 232 ? 51.004 19.439 5.132   1.00 32.98 ? 232  ASN A CB  1 
ATOM   1879 C CG  . ASN A 1 232 ? 51.291 20.898 5.583   1.00 43.03 ? 232  ASN A CG  1 
ATOM   1880 O OD1 . ASN A 1 232 ? 52.232 21.544 5.113   1.00 35.54 ? 232  ASN A OD1 1 
ATOM   1881 N ND2 . ASN A 1 232 ? 50.485 21.396 6.521   1.00 45.56 ? 232  ASN A ND2 1 
ATOM   1882 N N   . LYS A 1 233 ? 51.678 20.808 1.982   1.00 23.77 ? 233  LYS A N   1 
ATOM   1883 C CA  . LYS A 1 233 ? 51.063 21.702 1.012   1.00 21.45 ? 233  LYS A CA  1 
ATOM   1884 C C   . LYS A 1 233 ? 50.790 20.989 -0.316  1.00 18.35 ? 233  LYS A C   1 
ATOM   1885 O O   . LYS A 1 233 ? 51.493 20.044 -0.678  1.00 15.65 ? 233  LYS A O   1 
ATOM   1886 C CB  . LYS A 1 233 ? 51.958 22.913 0.799   1.00 20.74 ? 233  LYS A CB  1 
ATOM   1887 C CG  . LYS A 1 233 ? 51.888 23.854 2.004   1.00 23.61 ? 233  LYS A CG  1 
ATOM   1888 C CD  . LYS A 1 233 ? 53.248 24.270 2.467   1.00 28.34 ? 233  LYS A CD  1 
ATOM   1889 C CE  . LYS A 1 233 ? 53.146 24.848 3.884   1.00 28.21 ? 233  LYS A CE  1 
ATOM   1890 N NZ  . LYS A 1 233 ? 51.922 25.660 4.029   1.00 31.25 ? 233  LYS A NZ  1 
ATOM   1891 N N   . PRO A 1 234 ? 49.759 21.421 -1.045  1.00 16.33 ? 234  PRO A N   1 
ATOM   1892 C CA  . PRO A 1 234 ? 49.455 20.806 -2.344  1.00 18.10 ? 234  PRO A CA  1 
ATOM   1893 C C   . PRO A 1 234 ? 50.630 20.926 -3.306  1.00 14.29 ? 234  PRO A C   1 
ATOM   1894 O O   . PRO A 1 234 ? 51.326 21.945 -3.343  1.00 11.93 ? 234  PRO A O   1 
ATOM   1895 C CB  . PRO A 1 234 ? 48.250 21.608 -2.851  1.00 14.90 ? 234  PRO A CB  1 
ATOM   1896 C CG  . PRO A 1 234 ? 47.717 22.336 -1.672  1.00 23.01 ? 234  PRO A CG  1 
ATOM   1897 C CD  . PRO A 1 234 ? 48.866 22.553 -0.741  1.00 19.17 ? 234  PRO A CD  1 
ATOM   1898 N N   . VAL A 1 235 ? 50.841 19.872 -4.089  1.00 13.65 ? 235  VAL A N   1 
ATOM   1899 C CA  . VAL A 1 235 ? 51.902 19.832 -5.088  1.00 11.09 ? 235  VAL A CA  1 
ATOM   1900 C C   . VAL A 1 235 ? 51.272 19.501 -6.435  1.00 11.13 ? 235  VAL A C   1 
ATOM   1901 O O   . VAL A 1 235 ? 50.718 18.412 -6.610  1.00 10.94 ? 235  VAL A O   1 
ATOM   1902 C CB  . VAL A 1 235 ? 52.991 18.804 -4.743  1.00 10.91 ? 235  VAL A CB  1 
ATOM   1903 C CG1 . VAL A 1 235 ? 54.037 18.774 -5.854  1.00 9.28  ? 235  VAL A CG1 1 
ATOM   1904 C CG2 . VAL A 1 235 ? 53.652 19.125 -3.381  1.00 10.74 ? 235  VAL A CG2 1 
ATOM   1905 N N   . GLY A 1 236 ? 51.386 20.419 -7.394  1.00 10.05 ? 236  GLY A N   1 
ATOM   1906 C CA  . GLY A 1 236 ? 50.795 20.179 -8.702  1.00 9.96  ? 236  GLY A CA  1 
ATOM   1907 C C   . GLY A 1 236 ? 51.790 20.263 -9.843  1.00 12.05 ? 236  GLY A C   1 
ATOM   1908 O O   . GLY A 1 236 ? 53.004 20.140 -9.639  1.00 9.46  ? 236  GLY A O   1 
ATOM   1909 N N   . ILE A 1 237 ? 51.285 20.492 -11.055 1.00 9.23  ? 237  ILE A N   1 
ATOM   1910 C CA  . ILE A 1 237 ? 52.121 20.679 -12.233 1.00 9.21  ? 237  ILE A CA  1 
ATOM   1911 C C   . ILE A 1 237 ? 51.428 21.723 -13.103 1.00 10.31 ? 237  ILE A C   1 
ATOM   1912 O O   . ILE A 1 237 ? 50.217 21.935 -13.009 1.00 9.90  ? 237  ILE A O   1 
ATOM   1913 C CB  . ILE A 1 237 ? 52.354 19.350 -13.015 1.00 8.08  ? 237  ILE A CB  1 
ATOM   1914 C CG1 . ILE A 1 237 ? 53.602 19.437 -13.914 1.00 8.47  ? 237  ILE A CG1 1 
ATOM   1915 C CG2 . ILE A 1 237 ? 51.104 18.936 -13.831 1.00 5.90  ? 237  ILE A CG2 1 
ATOM   1916 C CD1 . ILE A 1 237 ? 53.975 18.113 -14.564 1.00 8.70  ? 237  ILE A CD1 1 
ATOM   1917 N N   . ILE A 1 238 ? 52.214 22.402 -13.932 1.00 7.41  ? 238  ILE A N   1 
ATOM   1918 C CA  . ILE A 1 238 ? 51.710 23.420 -14.852 1.00 10.63 ? 238  ILE A CA  1 
ATOM   1919 C C   . ILE A 1 238 ? 52.006 22.964 -16.272 1.00 9.20  ? 238  ILE A C   1 
ATOM   1920 O O   . ILE A 1 238 ? 53.156 22.647 -16.596 1.00 10.05 ? 238  ILE A O   1 
ATOM   1921 C CB  . ILE A 1 238 ? 52.341 24.796 -14.569 1.00 10.25 ? 238  ILE A CB  1 
ATOM   1922 C CG1 . ILE A 1 238 ? 51.823 25.347 -13.241 1.00 10.30 ? 238  ILE A CG1 1 
ATOM   1923 C CG2 . ILE A 1 238 ? 52.026 25.783 -15.676 1.00 7.49  ? 238  ILE A CG2 1 
ATOM   1924 C CD1 . ILE A 1 238 ? 52.710 26.456 -12.685 1.00 11.90 ? 238  ILE A CD1 1 
ATOM   1925 N N   . TYR A 1 239 ? 50.978 22.943 -17.118 1.00 10.99 ? 239  TYR A N   1 
ATOM   1926 C CA  . TYR A 1 239 ? 51.061 22.298 -18.422 1.00 8.57  ? 239  TYR A CA  1 
ATOM   1927 C C   . TYR A 1 239 ? 50.570 23.235 -19.518 1.00 10.17 ? 239  TYR A C   1 
ATOM   1928 O O   . TYR A 1 239 ? 49.571 23.940 -19.344 1.00 11.48 ? 239  TYR A O   1 
ATOM   1929 C CB  . TYR A 1 239 ? 50.243 20.991 -18.444 1.00 9.90  ? 239  TYR A CB  1 
ATOM   1930 C CG  . TYR A 1 239 ? 50.607 20.118 -19.626 1.00 9.85  ? 239  TYR A CG  1 
ATOM   1931 C CD1 . TYR A 1 239 ? 51.659 19.214 -19.544 1.00 7.78  ? 239  TYR A CD1 1 
ATOM   1932 C CD2 . TYR A 1 239 ? 49.916 20.224 -20.834 1.00 8.37  ? 239  TYR A CD2 1 
ATOM   1933 C CE1 . TYR A 1 239 ? 52.019 18.422 -20.631 1.00 10.23 ? 239  TYR A CE1 1 
ATOM   1934 C CE2 . TYR A 1 239 ? 50.272 19.436 -21.937 1.00 8.80  ? 239  TYR A CE2 1 
ATOM   1935 C CZ  . TYR A 1 239 ? 51.323 18.530 -21.824 1.00 9.04  ? 239  TYR A CZ  1 
ATOM   1936 O OH  . TYR A 1 239 ? 51.691 17.751 -22.916 1.00 9.77  ? 239  TYR A OH  1 
ATOM   1937 N N   . ALA A 1 240 ? 51.277 23.250 -20.650 1.00 7.31  ? 240  ALA A N   1 
ATOM   1938 C CA  . ALA A 1 240 ? 50.844 24.057 -21.796 1.00 9.98  ? 240  ALA A CA  1 
ATOM   1939 C C   . ALA A 1 240 ? 49.834 23.247 -22.594 1.00 10.60 ? 240  ALA A C   1 
ATOM   1940 O O   . ALA A 1 240 ? 50.204 22.408 -23.416 1.00 10.92 ? 240  ALA A O   1 
ATOM   1941 C CB  . ALA A 1 240 ? 52.029 24.458 -22.665 1.00 9.75  ? 240  ALA A CB  1 
ATOM   1942 N N   . THR A 1 241 ? 48.554 23.493 -22.352 1.00 10.09 ? 241  THR A N   1 
ATOM   1943 C CA  . THR A 1 241 ? 47.480 22.749 -22.998 1.00 13.06 ? 241  THR A CA  1 
ATOM   1944 C C   . THR A 1 241 ? 47.173 23.380 -24.347 1.00 14.80 ? 241  THR A C   1 
ATOM   1945 O O   . THR A 1 241 ? 46.789 24.550 -24.410 1.00 14.56 ? 241  THR A O   1 
ATOM   1946 C CB  . THR A 1 241 ? 46.219 22.755 -22.133 1.00 14.95 ? 241  THR A CB  1 
ATOM   1947 O OG1 . THR A 1 241 ? 45.877 24.114 -21.812 1.00 16.24 ? 241  THR A OG1 1 
ATOM   1948 C CG2 . THR A 1 241 ? 46.453 21.992 -20.842 1.00 12.58 ? 241  THR A CG2 1 
ATOM   1949 N N   . SER A 1 242 ? 47.351 22.618 -25.419 1.00 11.83 ? 242  SER A N   1 
ATOM   1950 C CA  . SER A 1 242 ? 46.870 23.075 -26.714 1.00 14.56 ? 242  SER A CA  1 
ATOM   1951 C C   . SER A 1 242 ? 45.386 22.782 -26.881 1.00 15.42 ? 242  SER A C   1 
ATOM   1952 O O   . SER A 1 242 ? 44.824 21.889 -26.243 1.00 14.62 ? 242  SER A O   1 
ATOM   1953 C CB  . SER A 1 242 ? 47.642 22.432 -27.873 1.00 16.95 ? 242  SER A CB  1 
ATOM   1954 O OG  . SER A 1 242 ? 49.012 22.314 -27.599 1.00 19.42 ? 242  SER A OG  1 
ATOM   1955 N N   . TRP A 1 243 ? 44.753 23.555 -27.764 1.00 12.89 ? 243  TRP A N   1 
ATOM   1956 C CA  . TRP A 1 243 ? 43.398 23.274 -28.222 1.00 11.85 ? 243  TRP A CA  1 
ATOM   1957 C C   . TRP A 1 243 ? 43.444 23.184 -29.746 1.00 12.45 ? 243  TRP A C   1 
ATOM   1958 O O   . TRP A 1 243 ? 43.529 24.208 -30.438 1.00 12.02 ? 243  TRP A O   1 
ATOM   1959 C CB  . TRP A 1 243 ? 42.392 24.328 -27.758 1.00 11.95 ? 243  TRP A CB  1 
ATOM   1960 C CG  . TRP A 1 243 ? 41.051 23.957 -28.298 1.00 15.64 ? 243  TRP A CG  1 
ATOM   1961 C CD1 . TRP A 1 243 ? 40.378 24.562 -29.326 1.00 14.12 ? 243  TRP A CD1 1 
ATOM   1962 C CD2 . TRP A 1 243 ? 40.264 22.824 -27.915 1.00 14.25 ? 243  TRP A CD2 1 
ATOM   1963 N NE1 . TRP A 1 243 ? 39.200 23.903 -29.565 1.00 13.54 ? 243  TRP A NE1 1 
ATOM   1964 C CE2 . TRP A 1 243 ? 39.108 22.828 -28.723 1.00 13.97 ? 243  TRP A CE2 1 
ATOM   1965 C CE3 . TRP A 1 243 ? 40.410 21.818 -26.941 1.00 15.64 ? 243  TRP A CE3 1 
ATOM   1966 C CZ2 . TRP A 1 243 ? 38.105 21.868 -28.595 1.00 16.37 ? 243  TRP A CZ2 1 
ATOM   1967 C CZ3 . TRP A 1 243 ? 39.419 20.867 -26.818 1.00 16.92 ? 243  TRP A CZ3 1 
ATOM   1968 C CH2 . TRP A 1 243 ? 38.277 20.896 -27.641 1.00 17.19 ? 243  TRP A CH2 1 
ATOM   1969 N N   . CYS A 1 244 ? 43.378 21.958 -30.265 1.00 11.72 ? 244  CYS A N   1 
ATOM   1970 C CA  . CYS A 1 244 ? 43.507 21.678 -31.692 1.00 13.80 ? 244  CYS A CA  1 
ATOM   1971 C C   . CYS A 1 244 ? 42.133 21.499 -32.316 1.00 18.28 ? 244  CYS A C   1 
ATOM   1972 O O   . CYS A 1 244 ? 41.301 20.743 -31.800 1.00 19.44 ? 244  CYS A O   1 
ATOM   1973 C CB  . CYS A 1 244 ? 44.343 20.418 -31.929 1.00 14.16 ? 244  CYS A CB  1 
ATOM   1974 S SG  . CYS A 1 244 ? 46.047 20.549 -31.325 1.00 18.46 ? 244  CYS A SG  1 
ATOM   1975 N N   . GLU A 1 245 ? 41.900 22.187 -33.425 1.00 14.55 ? 245  GLU A N   1 
ATOM   1976 C CA  . GLU A 1 245 ? 40.709 21.993 -34.230 1.00 17.62 ? 245  GLU A CA  1 
ATOM   1977 C C   . GLU A 1 245 ? 41.141 21.580 -35.635 1.00 20.74 ? 245  GLU A C   1 
ATOM   1978 O O   . GLU A 1 245 ? 42.320 21.662 -35.982 1.00 17.60 ? 245  GLU A O   1 
ATOM   1979 C CB  . GLU A 1 245 ? 39.847 23.269 -34.244 1.00 19.26 ? 245  GLU A CB  1 
ATOM   1980 C CG  . GLU A 1 245 ? 39.351 23.660 -32.846 1.00 20.84 ? 245  GLU A CG  1 
ATOM   1981 C CD  . GLU A 1 245 ? 38.676 25.031 -32.793 1.00 18.11 ? 245  GLU A CD  1 
ATOM   1982 O OE1 . GLU A 1 245 ? 38.788 25.806 -33.768 1.00 14.63 ? 245  GLU A OE1 1 
ATOM   1983 O OE2 . GLU A 1 245 ? 38.013 25.316 -31.767 1.00 14.17 ? 245  GLU A OE2 1 
ATOM   1984 N N   . GLY A 1 246 ? 40.192 21.102 -36.436 1.00 23.08 ? 246  GLY A N   1 
ATOM   1985 C CA  . GLY A 1 246 ? 40.527 20.677 -37.788 1.00 23.89 ? 246  GLY A CA  1 
ATOM   1986 C C   . GLY A 1 246 ? 39.834 19.392 -38.194 1.00 26.35 ? 246  GLY A C   1 
ATOM   1987 O O   . GLY A 1 246 ? 38.733 19.103 -37.725 1.00 25.98 ? 246  GLY A O   1 
ATOM   1988 N N   . ASP A 1 247 ? 40.474 18.605 -39.064 1.00 28.04 ? 247  ASP A N   1 
ATOM   1989 C CA  . ASP A 1 247 ? 39.880 17.357 -39.524 1.00 28.47 ? 247  ASP A CA  1 
ATOM   1990 C C   . ASP A 1 247 ? 40.054 16.302 -38.433 1.00 27.65 ? 247  ASP A C   1 
ATOM   1991 O O   . ASP A 1 247 ? 40.494 16.597 -37.324 1.00 30.47 ? 247  ASP A O   1 
ATOM   1992 C CB  . ASP A 1 247 ? 40.484 16.938 -40.869 1.00 25.16 ? 247  ASP A CB  1 
ATOM   1993 C CG  . ASP A 1 247 ? 41.985 16.634 -40.792 1.00 28.75 ? 247  ASP A CG  1 
ATOM   1994 O OD1 . ASP A 1 247 ? 42.535 16.478 -39.672 1.00 26.33 ? 247  ASP A OD1 1 
ATOM   1995 O OD2 . ASP A 1 247 ? 42.624 16.565 -41.871 1.00 22.66 ? 247  ASP A OD2 1 
ATOM   1996 N N   . ASP A 1 248 ? 39.766 15.044 -38.751 1.00 24.93 ? 248  ASP A N   1 
ATOM   1997 C CA  . ASP A 1 248 ? 39.841 13.975 -37.761 1.00 29.73 ? 248  ASP A CA  1 
ATOM   1998 C C   . ASP A 1 248 ? 41.217 13.829 -37.111 1.00 31.04 ? 248  ASP A C   1 
ATOM   1999 O O   . ASP A 1 248 ? 41.319 13.195 -36.052 1.00 33.53 ? 248  ASP A O   1 
ATOM   2000 C CB  . ASP A 1 248 ? 39.410 12.656 -38.409 1.00 39.70 ? 248  ASP A CB  1 
ATOM   2001 C CG  . ASP A 1 248 ? 39.984 12.472 -39.816 1.00 48.23 ? 248  ASP A CG  1 
ATOM   2002 O OD1 . ASP A 1 248 ? 41.185 12.754 -40.026 1.00 49.00 ? 248  ASP A OD1 1 
ATOM   2003 O OD2 . ASP A 1 248 ? 39.232 12.020 -40.713 1.00 57.07 ? 248  ASP A OD2 1 
ATOM   2004 N N   . ALA A 1 249 ? 42.271 14.405 -37.686 1.00 24.83 ? 249  ALA A N   1 
ATOM   2005 C CA  . ALA A 1 249 ? 43.573 14.318 -37.035 1.00 24.82 ? 249  ALA A CA  1 
ATOM   2006 C C   . ALA A 1 249 ? 43.677 15.117 -35.730 1.00 19.26 ? 249  ALA A C   1 
ATOM   2007 O O   . ALA A 1 249 ? 44.724 15.016 -35.081 1.00 18.93 ? 249  ALA A O   1 
ATOM   2008 C CB  . ALA A 1 249 ? 44.676 14.767 -37.996 1.00 22.00 ? 249  ALA A CB  1 
ATOM   2009 N N   . ARG A 1 250 ? 42.654 15.907 -35.341 1.00 20.24 ? 250  ARG A N   1 
ATOM   2010 C CA  . ARG A 1 250 ? 42.685 16.627 -34.060 1.00 23.48 ? 250  ARG A CA  1 
ATOM   2011 C C   . ARG A 1 250 ? 43.013 15.697 -32.910 1.00 21.44 ? 250  ARG A C   1 
ATOM   2012 O O   . ARG A 1 250 ? 43.743 16.064 -31.984 1.00 20.61 ? 250  ARG A O   1 
ATOM   2013 C CB  . ARG A 1 250 ? 41.339 17.249 -33.690 1.00 25.40 ? 250  ARG A CB  1 
ATOM   2014 C CG  . ARG A 1 250 ? 40.378 17.635 -34.712 1.00 34.64 ? 250  ARG A CG  1 
ATOM   2015 C CD  . ARG A 1 250 ? 39.194 18.304 -34.023 1.00 33.30 ? 250  ARG A CD  1 
ATOM   2016 N NE  . ARG A 1 250 ? 38.456 19.234 -34.870 1.00 42.92 ? 250  ARG A NE  1 
ATOM   2017 C CZ  . ARG A 1 250 ? 37.806 20.309 -34.434 1.00 36.64 ? 250  ARG A CZ  1 
ATOM   2018 N NH1 . ARG A 1 250 ? 37.705 20.582 -33.140 1.00 40.83 ? 250  ARG A NH1 1 
ATOM   2019 N NH2 . ARG A 1 250 ? 37.231 21.122 -35.316 1.00 34.29 ? 250  ARG A NH2 1 
ATOM   2020 N N   . ASN A 1 251 ? 42.359 14.532 -32.892 1.00 21.11 ? 251  ASN A N   1 
ATOM   2021 C CA  . ASN A 1 251 ? 42.485 13.624 -31.758 1.00 24.53 ? 251  ASN A CA  1 
ATOM   2022 C C   . ASN A 1 251 ? 43.919 13.160 -31.585 1.00 21.03 ? 251  ASN A C   1 
ATOM   2023 O O   . ASN A 1 251 ? 44.434 13.132 -30.464 1.00 19.62 ? 251  ASN A O   1 
ATOM   2024 C CB  . ASN A 1 251 ? 41.557 12.424 -31.932 1.00 29.03 ? 251  ASN A CB  1 
ATOM   2025 C CG  . ASN A 1 251 ? 40.099 12.786 -31.779 1.00 36.18 ? 251  ASN A CG  1 
ATOM   2026 O OD1 . ASN A 1 251 ? 39.755 13.938 -31.509 1.00 34.00 ? 251  ASN A OD1 1 
ATOM   2027 N ND2 . ASN A 1 251 ? 39.226 11.803 -31.970 1.00 45.61 ? 251  ASN A ND2 1 
ATOM   2028 N N   . ASP A 1 252 ? 44.584 12.799 -32.682 1.00 14.97 ? 252  ASP A N   1 
ATOM   2029 C CA  . ASP A 1 252 ? 45.976 12.388 -32.574 1.00 18.92 ? 252  ASP A CA  1 
ATOM   2030 C C   . ASP A 1 252 ? 46.863 13.549 -32.151 1.00 18.47 ? 252  ASP A C   1 
ATOM   2031 O O   . ASP A 1 252 ? 47.811 13.362 -31.382 1.00 15.48 ? 252  ASP A O   1 
ATOM   2032 C CB  . ASP A 1 252 ? 46.458 11.809 -33.898 1.00 21.33 ? 252  ASP A CB  1 
ATOM   2033 C CG  . ASP A 1 252 ? 45.671 10.575 -34.304 1.00 35.25 ? 252  ASP A CG  1 
ATOM   2034 O OD1 . ASP A 1 252 ? 45.504 9.670  -33.455 1.00 40.63 ? 252  ASP A OD1 1 
ATOM   2035 O OD2 . ASP A 1 252 ? 45.211 10.518 -35.463 1.00 35.92 ? 252  ASP A OD2 1 
ATOM   2036 N N   . ALA A 1 253 ? 46.585 14.750 -32.658 1.00 14.61 ? 253  ALA A N   1 
ATOM   2037 C CA  . ALA A 1 253 ? 47.374 15.910 -32.258 1.00 14.76 ? 253  ALA A CA  1 
ATOM   2038 C C   . ALA A 1 253 ? 47.227 16.169 -30.761 1.00 12.25 ? 253  ALA A C   1 
ATOM   2039 O O   . ALA A 1 253 ? 48.220 16.370 -30.054 1.00 11.51 ? 253  ALA A O   1 
ATOM   2040 C CB  . ALA A 1 253 ? 46.953 17.137 -33.071 1.00 12.76 ? 253  ALA A CB  1 
ATOM   2041 N N   . MET A 1 254 ? 45.987 16.155 -30.261 1.00 11.45 ? 254  MET A N   1 
ATOM   2042 C CA  . MET A 1 254 ? 45.741 16.379 -28.834 1.00 11.77 ? 254  MET A CA  1 
ATOM   2043 C C   . MET A 1 254 ? 46.393 15.307 -27.970 1.00 14.11 ? 254  MET A C   1 
ATOM   2044 O O   . MET A 1 254 ? 46.781 15.578 -26.824 1.00 11.95 ? 254  MET A O   1 
ATOM   2045 C CB  . MET A 1 254 ? 44.236 16.407 -28.557 1.00 12.69 ? 254  MET A CB  1 
ATOM   2046 C CG  . MET A 1 254 ? 43.453 17.665 -29.028 1.00 14.94 ? 254  MET A CG  1 
ATOM   2047 S SD  . MET A 1 254 ? 44.056 19.183 -28.261 1.00 15.43 ? 254  MET A SD  1 
ATOM   2048 C CE  . MET A 1 254 ? 43.053 19.124 -26.779 1.00 13.16 ? 254  MET A CE  1 
ATOM   2049 N N   . GLU A 1 255 ? 46.476 14.076 -28.477 1.00 13.78 ? 255  GLU A N   1 
ATOM   2050 C CA  . GLU A 1 255 ? 47.115 13.015 -27.711 1.00 14.28 ? 255  GLU A CA  1 
ATOM   2051 C C   . GLU A 1 255 ? 48.590 13.318 -27.489 1.00 15.18 ? 255  GLU A C   1 
ATOM   2052 O O   . GLU A 1 255 ? 49.100 13.160 -26.377 1.00 12.34 ? 255  GLU A O   1 
ATOM   2053 C CB  . GLU A 1 255 ? 46.939 11.672 -28.420 1.00 15.52 ? 255  GLU A CB  1 
ATOM   2054 C CG  . GLU A 1 255 ? 47.803 10.551 -27.832 1.00 16.96 ? 255  GLU A CG  1 
ATOM   2055 C CD  . GLU A 1 255 ? 47.400 10.182 -26.402 1.00 17.78 ? 255  GLU A CD  1 
ATOM   2056 O OE1 . GLU A 1 255 ? 46.239 10.441 -26.012 1.00 20.27 ? 255  GLU A OE1 1 
ATOM   2057 O OE2 . GLU A 1 255 ? 48.244 9.623  -25.668 1.00 21.24 ? 255  GLU A OE2 1 
ATOM   2058 N N   . LEU A 1 256 ? 49.297 13.769 -28.530 1.00 12.30 ? 256  LEU A N   1 
ATOM   2059 C CA  . LEU A 1 256 ? 50.716 14.045 -28.340 1.00 13.36 ? 256  LEU A CA  1 
ATOM   2060 C C   . LEU A 1 256 ? 50.930 15.384 -27.642 1.00 13.79 ? 256  LEU A C   1 
ATOM   2061 O O   . LEU A 1 256 ? 51.828 15.516 -26.804 1.00 13.38 ? 256  LEU A O   1 
ATOM   2062 C CB  . LEU A 1 256 ? 51.450 14.021 -29.680 1.00 11.01 ? 256  LEU A CB  1 
ATOM   2063 C CG  . LEU A 1 256 ? 52.957 14.255 -29.557 1.00 16.14 ? 256  LEU A CG  1 
ATOM   2064 C CD1 . LEU A 1 256 ? 53.565 13.253 -28.574 1.00 14.01 ? 256  LEU A CD1 1 
ATOM   2065 C CD2 . LEU A 1 256 ? 53.641 14.147 -30.899 1.00 11.35 ? 256  LEU A CD2 1 
ATOM   2066 N N   . GLU A 1 257 ? 50.093 16.375 -27.945 1.00 9.98  ? 257  GLU A N   1 
ATOM   2067 C CA  . GLU A 1 257 ? 50.311 17.707 -27.389 1.00 11.57 ? 257  GLU A CA  1 
ATOM   2068 C C   . GLU A 1 257 ? 49.967 17.754 -25.901 1.00 12.99 ? 257  GLU A C   1 
ATOM   2069 O O   . GLU A 1 257 ? 50.629 18.457 -25.124 1.00 14.47 ? 257  GLU A O   1 
ATOM   2070 C CB  . GLU A 1 257 ? 49.472 18.731 -28.152 1.00 13.14 ? 257  GLU A CB  1 
ATOM   2071 C CG  . GLU A 1 257 ? 49.932 18.986 -29.580 1.00 16.44 ? 257  GLU A CG  1 
ATOM   2072 C CD  . GLU A 1 257 ? 51.101 19.960 -29.647 1.00 26.89 ? 257  GLU A CD  1 
ATOM   2073 O OE1 . GLU A 1 257 ? 52.160 19.594 -30.196 1.00 21.13 ? 257  GLU A OE1 1 
ATOM   2074 O OE2 . GLU A 1 257 ? 50.969 21.083 -29.110 1.00 30.60 ? 257  GLU A OE2 1 
ATOM   2075 N N   . ASN A 1 258 ? 48.936 17.015 -25.484 1.00 10.16 ? 258  ASN A N   1 
ATOM   2076 C CA  . ASN A 1 258 ? 48.374 17.142 -24.140 1.00 11.30 ? 258  ASN A CA  1 
ATOM   2077 C C   . ASN A 1 258 ? 48.346 15.822 -23.380 1.00 10.99 ? 258  ASN A C   1 
ATOM   2078 O O   . ASN A 1 258 ? 48.933 15.722 -22.295 1.00 11.54 ? 258  ASN A O   1 
ATOM   2079 C CB  . ASN A 1 258 ? 46.938 17.687 -24.207 1.00 11.74 ? 258  ASN A CB  1 
ATOM   2080 C CG  . ASN A 1 258 ? 46.864 19.151 -24.612 1.00 15.11 ? 258  ASN A CG  1 
ATOM   2081 O OD1 . ASN A 1 258 ? 47.877 19.807 -24.863 1.00 12.20 ? 258  ASN A OD1 1 
ATOM   2082 N ND2 . ASN A 1 258 ? 45.645 19.669 -24.668 1.00 13.45 ? 258  ASN A ND2 1 
ATOM   2083 N N   . TRP A 1 259 ? 47.642 14.814 -23.899 1.00 10.79 ? 259  TRP A N   1 
ATOM   2084 C CA  . TRP A 1 259 ? 47.192 13.730 -23.034 1.00 14.06 ? 259  TRP A CA  1 
ATOM   2085 C C   . TRP A 1 259 ? 48.274 12.698 -22.779 1.00 13.52 ? 259  TRP A C   1 
ATOM   2086 O O   . TRP A 1 259 ? 48.246 12.042 -21.730 1.00 13.13 ? 259  TRP A O   1 
ATOM   2087 C CB  . TRP A 1 259 ? 45.947 13.058 -23.620 1.00 13.47 ? 259  TRP A CB  1 
ATOM   2088 C CG  . TRP A 1 259 ? 44.876 14.038 -24.044 1.00 15.48 ? 259  TRP A CG  1 
ATOM   2089 C CD1 . TRP A 1 259 ? 44.154 14.012 -25.211 1.00 16.41 ? 259  TRP A CD1 1 
ATOM   2090 C CD2 . TRP A 1 259 ? 44.413 15.185 -23.313 1.00 12.90 ? 259  TRP A CD2 1 
ATOM   2091 N NE1 . TRP A 1 259 ? 43.271 15.070 -25.245 1.00 15.22 ? 259  TRP A NE1 1 
ATOM   2092 C CE2 . TRP A 1 259 ? 43.412 15.804 -24.096 1.00 15.60 ? 259  TRP A CE2 1 
ATOM   2093 C CE3 . TRP A 1 259 ? 44.743 15.748 -22.072 1.00 12.16 ? 259  TRP A CE3 1 
ATOM   2094 C CZ2 . TRP A 1 259 ? 42.740 16.952 -23.676 1.00 14.60 ? 259  TRP A CZ2 1 
ATOM   2095 C CZ3 . TRP A 1 259 ? 44.080 16.892 -21.663 1.00 14.68 ? 259  TRP A CZ3 1 
ATOM   2096 C CH2 . TRP A 1 259 ? 43.088 17.480 -22.460 1.00 14.84 ? 259  TRP A CH2 1 
ATOM   2097 N N   . TYR A 1 260 ? 49.225 12.534 -23.701 1.00 10.93 ? 260  TYR A N   1 
ATOM   2098 C CA  . TYR A 1 260 ? 50.315 11.592 -23.445 1.00 14.81 ? 260  TYR A CA  1 
ATOM   2099 C C   . TYR A 1 260 ? 51.010 11.916 -22.128 1.00 13.70 ? 260  TYR A C   1 
ATOM   2100 O O   . TYR A 1 260 ? 51.146 11.052 -21.255 1.00 11.06 ? 260  TYR A O   1 
ATOM   2101 C CB  . TYR A 1 260 ? 51.322 11.608 -24.595 1.00 15.98 ? 260  TYR A CB  1 
ATOM   2102 C CG  . TYR A 1 260 ? 52.566 10.802 -24.307 1.00 15.11 ? 260  TYR A CG  1 
ATOM   2103 C CD1 . TYR A 1 260 ? 52.600 9.439  -24.573 1.00 15.61 ? 260  TYR A CD1 1 
ATOM   2104 C CD2 . TYR A 1 260 ? 53.708 11.399 -23.775 1.00 14.25 ? 260  TYR A CD2 1 
ATOM   2105 C CE1 . TYR A 1 260 ? 53.737 8.687  -24.320 1.00 17.47 ? 260  TYR A CE1 1 
ATOM   2106 C CE2 . TYR A 1 260 ? 54.858 10.649 -23.511 1.00 14.98 ? 260  TYR A CE2 1 
ATOM   2107 C CZ  . TYR A 1 260 ? 54.861 9.295  -23.787 1.00 19.26 ? 260  TYR A CZ  1 
ATOM   2108 O OH  . TYR A 1 260 ? 55.985 8.536  -23.530 1.00 16.25 ? 260  TYR A OH  1 
ATOM   2109 N N   . PHE A 1 261 ? 51.442 13.168 -21.964 1.00 9.76  ? 261  PHE A N   1 
ATOM   2110 C CA  . PHE A 1 261 ? 52.158 13.561 -20.755 1.00 11.37 ? 261  PHE A CA  1 
ATOM   2111 C C   . PHE A 1 261 ? 51.221 13.582 -19.554 1.00 10.54 ? 261  PHE A C   1 
ATOM   2112 O O   . PHE A 1 261 ? 51.534 13.022 -18.496 1.00 11.39 ? 261  PHE A O   1 
ATOM   2113 C CB  . PHE A 1 261 ? 52.807 14.939 -20.967 1.00 10.29 ? 261  PHE A CB  1 
ATOM   2114 C CG  . PHE A 1 261 ? 53.840 15.310 -19.924 1.00 10.78 ? 261  PHE A CG  1 
ATOM   2115 C CD1 . PHE A 1 261 ? 53.461 15.659 -18.630 1.00 8.89  ? 261  PHE A CD1 1 
ATOM   2116 C CD2 . PHE A 1 261 ? 55.185 15.351 -20.256 1.00 9.33  ? 261  PHE A CD2 1 
ATOM   2117 C CE1 . PHE A 1 261 ? 54.406 16.021 -17.679 1.00 9.31  ? 261  PHE A CE1 1 
ATOM   2118 C CE2 . PHE A 1 261 ? 56.138 15.702 -19.312 1.00 11.14 ? 261  PHE A CE2 1 
ATOM   2119 C CZ  . PHE A 1 261 ? 55.743 16.039 -18.013 1.00 9.60  ? 261  PHE A CZ  1 
ATOM   2120 N N   . LEU A 1 262 ? 50.055 14.209 -19.709 1.00 8.29  ? 262  LEU A N   1 
ATOM   2121 C CA  . LEU A 1 262 ? 49.156 14.404 -18.575 1.00 11.02 ? 262  LEU A CA  1 
ATOM   2122 C C   . LEU A 1 262 ? 48.604 13.073 -18.057 1.00 14.08 ? 262  LEU A C   1 
ATOM   2123 O O   . LEU A 1 262 ? 48.475 12.893 -16.840 1.00 11.36 ? 262  LEU A O   1 
ATOM   2124 C CB  . LEU A 1 262 ? 48.038 15.367 -18.977 1.00 9.65  ? 262  LEU A CB  1 
ATOM   2125 C CG  . LEU A 1 262 ? 48.449 16.852 -19.045 1.00 9.92  ? 262  LEU A CG  1 
ATOM   2126 C CD1 . LEU A 1 262 ? 47.281 17.723 -19.460 1.00 9.17  ? 262  LEU A CD1 1 
ATOM   2127 C CD2 . LEU A 1 262 ? 49.013 17.328 -17.696 1.00 9.88  ? 262  LEU A CD2 1 
ATOM   2128 N N   . ASP A 1 263 ? 48.293 12.121 -18.953 1.00 11.48 ? 263  ASP A N   1 
ATOM   2129 C CA  . ASP A 1 263 ? 47.891 10.785 -18.498 1.00 14.55 ? 263  ASP A CA  1 
ATOM   2130 C C   . ASP A 1 263 ? 48.933 10.189 -17.556 1.00 13.27 ? 263  ASP A C   1 
ATOM   2131 O O   . ASP A 1 263 ? 48.586 9.511  -16.586 1.00 13.18 ? 263  ASP A O   1 
ATOM   2132 C CB  . ASP A 1 263 ? 47.688 9.809  -19.675 1.00 13.88 ? 263  ASP A CB  1 
ATOM   2133 C CG  . ASP A 1 263 ? 46.424 10.076 -20.496 1.00 16.54 ? 263  ASP A CG  1 
ATOM   2134 O OD1 . ASP A 1 263 ? 45.589 10.910 -20.096 1.00 15.29 ? 263  ASP A OD1 1 
ATOM   2135 O OD2 . ASP A 1 263 ? 46.263 9.410  -21.555 1.00 17.44 ? 263  ASP A OD2 1 
ATOM   2136 N N   . ARG A 1 264 ? 50.217 10.430 -17.827 1.00 11.34 ? 264  ARG A N   1 
ATOM   2137 C CA  . ARG A 1 264 ? 51.304 9.780  -17.105 1.00 13.91 ? 264  ARG A CA  1 
ATOM   2138 C C   . ARG A 1 264 ? 51.761 10.534 -15.847 1.00 13.96 ? 264  ARG A C   1 
ATOM   2139 O O   . ARG A 1 264 ? 52.608 10.013 -15.105 1.00 12.99 ? 264  ARG A O   1 
ATOM   2140 C CB  . ARG A 1 264 ? 52.485 9.553  -18.064 1.00 12.41 ? 264  ARG A CB  1 
ATOM   2141 C CG  . ARG A 1 264 ? 52.219 8.407  -19.043 1.00 13.00 ? 264  ARG A CG  1 
ATOM   2142 C CD  . ARG A 1 264 ? 53.099 8.460  -20.283 1.00 15.20 ? 264  ARG A CD  1 
ATOM   2143 N NE  . ARG A 1 264 ? 52.765 7.377  -21.202 1.00 14.85 ? 264  ARG A NE  1 
ATOM   2144 C CZ  . ARG A 1 264 ? 51.658 7.315  -21.931 1.00 19.26 ? 264  ARG A CZ  1 
ATOM   2145 N NH1 . ARG A 1 264 ? 50.792 8.321  -21.970 1.00 15.59 ? 264  ARG A NH1 1 
ATOM   2146 N NH2 . ARG A 1 264 ? 51.411 6.215  -22.641 1.00 20.03 ? 264  ARG A NH2 1 
ATOM   2147 N N   . VAL A 1 265 ? 51.152 11.680 -15.547 1.00 11.91 ? 265  VAL A N   1 
ATOM   2148 C CA  . VAL A 1 265 ? 51.473 12.387 -14.269 1.00 8.19  ? 265  VAL A CA  1 
ATOM   2149 C C   . VAL A 1 265 ? 50.210 12.633 -13.424 1.00 12.96 ? 265  VAL A C   1 
ATOM   2150 O O   . VAL A 1 265 ? 50.376 12.990 -12.256 1.00 10.98 ? 265  VAL A O   1 
ATOM   2151 C CB  . VAL A 1 265 ? 52.216 13.703 -14.564 1.00 12.97 ? 265  VAL A CB  1 
ATOM   2152 C CG1 . VAL A 1 265 ? 53.548 13.468 -15.255 1.00 10.25 ? 265  VAL A CG1 1 
ATOM   2153 C CG2 . VAL A 1 265 ? 51.357 14.688 -15.334 1.00 7.88  ? 265  VAL A CG2 1 
ATOM   2154 N N   . ILE A 1 266 ? 49.011 12.436 -13.984 1.00 11.11 ? 266  ILE A N   1 
ATOM   2155 C CA  . ILE A 1 266 ? 47.734 12.808 -13.296 1.00 12.78 ? 266  ILE A CA  1 
ATOM   2156 C C   . ILE A 1 266 ? 47.586 12.150 -11.910 1.00 16.20 ? 266  ILE A C   1 
ATOM   2157 O O   . ILE A 1 266 ? 47.045 12.787 -11.029 1.00 13.98 ? 266  ILE A O   1 
ATOM   2158 C CB  . ILE A 1 266 ? 46.507 12.536 -14.193 1.00 15.77 ? 266  ILE A CB  1 
ATOM   2159 C CG1 . ILE A 1 266 ? 45.326 13.422 -13.796 1.00 15.34 ? 266  ILE A CG1 1 
ATOM   2160 C CG2 . ILE A 1 266 ? 46.150 11.061 -14.209 1.00 15.08 ? 266  ILE A CG2 1 
ATOM   2161 C CD1 . ILE A 1 266 ? 45.511 14.872 -14.158 1.00 15.31 ? 266  ILE A CD1 1 
ATOM   2162 N N   . ASP A 1 267 ? 48.075 10.928 -11.758 1.00 14.75 ? 267  ASP A N   1 
ATOM   2163 C CA  . ASP A 1 267 ? 47.978 10.202 -10.461 1.00 17.38 ? 267  ASP A CA  1 
ATOM   2164 C C   . ASP A 1 267 ? 48.909 10.837 -9.417  1.00 16.87 ? 267  ASP A C   1 
ATOM   2165 O O   . ASP A 1 267 ? 48.780 10.484 -8.246  1.00 19.13 ? 267  ASP A O   1 
ATOM   2166 C CB  . ASP A 1 267 ? 48.254 8.711  -10.667 1.00 16.29 ? 267  ASP A CB  1 
ATOM   2167 C CG  . ASP A 1 267 ? 47.210 8.026  -11.531 1.00 26.59 ? 267  ASP A CG  1 
ATOM   2168 O OD1 . ASP A 1 267 ? 46.069 8.512  -11.568 1.00 28.30 ? 267  ASP A OD1 1 
ATOM   2169 O OD2 . ASP A 1 267 ? 47.547 7.015  -12.155 1.00 39.83 ? 267  ASP A OD2 1 
ATOM   2170 N N   . ARG A 1 268 ? 49.817 11.707 -9.844  1.00 12.04 ? 268  ARG A N   1 
ATOM   2171 C CA  . ARG A 1 268 ? 50.826 12.275 -8.923  1.00 11.57 ? 268  ARG A CA  1 
ATOM   2172 C C   . ARG A 1 268 ? 50.770 13.817 -8.953  1.00 11.22 ? 268  ARG A C   1 
ATOM   2173 O O   . ARG A 1 268 ? 51.824 14.441 -8.961  1.00 10.93 ? 268  ARG A O   1 
ATOM   2174 C CB  . ARG A 1 268 ? 52.181 11.617 -9.194  1.00 12.80 ? 268  ARG A CB  1 
ATOM   2175 C CG  . ARG A 1 268 ? 52.216 10.130 -8.874  1.00 18.56 ? 268  ARG A CG  1 
ATOM   2176 C CD  . ARG A 1 268 ? 53.618 9.556  -8.810  1.00 24.03 ? 268  ARG A CD  1 
ATOM   2177 N NE  . ARG A 1 268 ? 53.637 8.258  -8.148  1.00 30.63 ? 268  ARG A NE  1 
ATOM   2178 C CZ  . ARG A 1 268 ? 54.718 7.691  -7.623  1.00 42.84 ? 268  ARG A CZ  1 
ATOM   2179 N NH1 . ARG A 1 268 ? 55.887 8.303  -7.677  1.00 37.25 ? 268  ARG A NH1 1 
ATOM   2180 N NH2 . ARG A 1 268 ? 54.629 6.511  -7.037  1.00 49.15 ? 268  ARG A NH2 1 
ATOM   2181 N N   . ILE A 1 269 ? 49.560 14.368 -8.931  1.00 11.95 ? 269  ILE A N   1 
ATOM   2182 C CA  . ILE A 1 269 ? 49.384 15.839 -8.781  1.00 9.89  ? 269  ILE A CA  1 
ATOM   2183 C C   . ILE A 1 269 ? 48.163 16.104 -7.900  1.00 13.55 ? 269  ILE A C   1 
ATOM   2184 O O   . ILE A 1 269 ? 47.217 15.329 -7.946  1.00 13.44 ? 269  ILE A O   1 
ATOM   2185 C CB  . ILE A 1 269 ? 49.259 16.559 -10.142 1.00 10.60 ? 269  ILE A CB  1 
ATOM   2186 C CG1 . ILE A 1 269 ? 47.974 16.181 -10.885 1.00 12.63 ? 269  ILE A CG1 1 
ATOM   2187 C CG2 . ILE A 1 269 ? 50.494 16.357 -11.004 1.00 8.62  ? 269  ILE A CG2 1 
ATOM   2188 C CD1 . ILE A 1 269 ? 47.693 17.047 -12.088 1.00 11.25 ? 269  ILE A CD1 1 
ATOM   2189 N N   . ASP A 1 270 ? 48.222 17.170 -7.128  1.00 11.33 ? 270  ASP A N   1 
ATOM   2190 C CA  . ASP A 1 270 ? 47.078 17.585 -6.322  1.00 13.28 ? 270  ASP A CA  1 
ATOM   2191 C C   . ASP A 1 270 ? 46.189 18.581 -7.053  1.00 13.75 ? 270  ASP A C   1 
ATOM   2192 O O   . ASP A 1 270 ? 45.038 18.787 -6.653  1.00 11.51 ? 270  ASP A O   1 
ATOM   2193 C CB  . ASP A 1 270 ? 47.564 18.189 -4.995  1.00 11.68 ? 270  ASP A CB  1 
ATOM   2194 C CG  . ASP A 1 270 ? 48.370 17.193 -4.155  1.00 17.96 ? 270  ASP A CG  1 
ATOM   2195 O OD1 . ASP A 1 270 ? 48.074 15.976 -4.252  1.00 12.24 ? 270  ASP A OD1 1 
ATOM   2196 O OD2 . ASP A 1 270 ? 49.305 17.616 -3.420  1.00 11.94 ? 270  ASP A OD2 1 
ATOM   2197 N N   . PHE A 1 271 ? 46.697 19.196 -8.116  1.00 10.58 ? 271  PHE A N   1 
ATOM   2198 C CA  . PHE A 1 271 ? 45.917 20.099 -8.948  1.00 12.53 ? 271  PHE A CA  1 
ATOM   2199 C C   . PHE A 1 271 ? 46.652 20.234 -10.265 1.00 10.00 ? 271  PHE A C   1 
ATOM   2200 O O   . PHE A 1 271 ? 47.856 19.968 -10.353 1.00 9.47  ? 271  PHE A O   1 
ATOM   2201 C CB  . PHE A 1 271 ? 45.731 21.483 -8.308  1.00 9.91  ? 271  PHE A CB  1 
ATOM   2202 C CG  . PHE A 1 271 ? 47.025 22.204 -8.019  1.00 10.41 ? 271  PHE A CG  1 
ATOM   2203 C CD1 . PHE A 1 271 ? 47.676 22.038 -6.795  1.00 11.96 ? 271  PHE A CD1 1 
ATOM   2204 C CD2 . PHE A 1 271 ? 47.588 23.053 -8.961  1.00 12.68 ? 271  PHE A CD2 1 
ATOM   2205 C CE1 . PHE A 1 271 ? 48.865 22.704 -6.518  1.00 13.54 ? 271  PHE A CE1 1 
ATOM   2206 C CE2 . PHE A 1 271 ? 48.778 23.728 -8.697  1.00 9.00  ? 271  PHE A CE2 1 
ATOM   2207 C CZ  . PHE A 1 271 ? 49.422 23.554 -7.471  1.00 14.34 ? 271  PHE A CZ  1 
ATOM   2208 N N   . LEU A 1 272 ? 45.924 20.669 -11.285 1.00 9.47  ? 272  LEU A N   1 
ATOM   2209 C CA  . LEU A 1 272 ? 46.490 20.858 -12.614 1.00 10.27 ? 272  LEU A CA  1 
ATOM   2210 C C   . LEU A 1 272 ? 46.413 22.334 -12.967 1.00 11.90 ? 272  LEU A C   1 
ATOM   2211 O O   . LEU A 1 272 ? 45.326 22.920 -12.946 1.00 11.17 ? 272  LEU A O   1 
ATOM   2212 C CB  . LEU A 1 272 ? 45.744 20.021 -13.653 1.00 10.39 ? 272  LEU A CB  1 
ATOM   2213 C CG  . LEU A 1 272 ? 46.169 20.274 -15.098 1.00 12.95 ? 272  LEU A CG  1 
ATOM   2214 C CD1 . LEU A 1 272 ? 47.664 19.983 -15.305 1.00 7.56  ? 272  LEU A CD1 1 
ATOM   2215 C CD2 . LEU A 1 272 ? 45.299 19.472 -16.069 1.00 11.04 ? 272  LEU A CD2 1 
ATOM   2216 N N   . GLY A 1 273 ? 47.563 22.930 -13.280 1.00 10.61 ? 273  GLY A N   1 
ATOM   2217 C CA  . GLY A 1 273 ? 47.602 24.278 -13.811 1.00 8.52  ? 273  GLY A CA  1 
ATOM   2218 C C   . GLY A 1 273 ? 47.597 24.240 -15.328 1.00 9.79  ? 273  GLY A C   1 
ATOM   2219 O O   . GLY A 1 273 ? 48.435 23.582 -15.947 1.00 10.03 ? 273  GLY A O   1 
ATOM   2220 N N   . VAL A 1 274 ? 46.646 24.950 -15.919 1.00 8.91  ? 274  VAL A N   1 
ATOM   2221 C CA  . VAL A 1 274 ? 46.448 24.998 -17.358 1.00 9.78  ? 274  VAL A CA  1 
ATOM   2222 C C   . VAL A 1 274 ? 46.967 26.341 -17.869 1.00 9.77  ? 274  VAL A C   1 
ATOM   2223 O O   . VAL A 1 274 ? 46.520 27.407 -17.415 1.00 10.17 ? 274  VAL A O   1 
ATOM   2224 C CB  . VAL A 1 274 ? 44.963 24.786 -17.700 1.00 13.17 ? 274  VAL A CB  1 
ATOM   2225 C CG1 . VAL A 1 274 ? 44.618 25.359 -19.039 1.00 16.89 ? 274  VAL A CG1 1 
ATOM   2226 C CG2 . VAL A 1 274 ? 44.616 23.298 -17.609 1.00 11.17 ? 274  VAL A CG2 1 
ATOM   2227 N N   . ASN A 1 275 ? 47.929 26.293 -18.797 1.00 11.17 ? 275  ASN A N   1 
ATOM   2228 C CA  . ASN A 1 275 ? 48.436 27.478 -19.487 1.00 9.15  ? 275  ASN A CA  1 
ATOM   2229 C C   . ASN A 1 275 ? 47.849 27.481 -20.892 1.00 10.45 ? 275  ASN A C   1 
ATOM   2230 O O   . ASN A 1 275 ? 48.095 26.547 -21.662 1.00 10.63 ? 275  ASN A O   1 
ATOM   2231 C CB  . ASN A 1 275 ? 49.967 27.478 -19.583 1.00 9.66  ? 275  ASN A CB  1 
ATOM   2232 C CG  . ASN A 1 275 ? 50.649 27.674 -18.254 1.00 10.41 ? 275  ASN A CG  1 
ATOM   2233 O OD1 . ASN A 1 275 ? 49.999 27.783 -17.207 1.00 8.02  ? 275  ASN A OD1 1 
ATOM   2234 N ND2 . ASN A 1 275 ? 51.980 27.741 -18.289 1.00 6.10  ? 275  ASN A ND2 1 
ATOM   2235 N N   . TYR A 1 276 ? 47.095 28.531 -21.233 1.00 9.15  ? 276  TYR A N   1 
ATOM   2236 C CA  . TYR A 1 276 ? 46.427 28.611 -22.528 1.00 10.08 ? 276  TYR A CA  1 
ATOM   2237 C C   . TYR A 1 276 ? 46.597 30.003 -23.119 1.00 10.83 ? 276  TYR A C   1 
ATOM   2238 O O   . TYR A 1 276 ? 46.322 31.004 -22.444 1.00 8.90  ? 276  TYR A O   1 
ATOM   2239 C CB  . TYR A 1 276 ? 44.929 28.278 -22.411 1.00 9.49  ? 276  TYR A CB  1 
ATOM   2240 C CG  . TYR A 1 276 ? 44.191 28.535 -23.707 1.00 9.83  ? 276  TYR A CG  1 
ATOM   2241 C CD1 . TYR A 1 276 ? 44.124 27.557 -24.696 1.00 10.34 ? 276  TYR A CD1 1 
ATOM   2242 C CD2 . TYR A 1 276 ? 43.592 29.765 -23.966 1.00 8.42  ? 276  TYR A CD2 1 
ATOM   2243 C CE1 . TYR A 1 276 ? 43.475 27.791 -25.901 1.00 10.53 ? 276  TYR A CE1 1 
ATOM   2244 C CE2 . TYR A 1 276 ? 42.930 30.009 -25.179 1.00 8.04  ? 276  TYR A CE2 1 
ATOM   2245 C CZ  . TYR A 1 276 ? 42.880 29.019 -26.138 1.00 10.29 ? 276  TYR A CZ  1 
ATOM   2246 O OH  . TYR A 1 276 ? 42.235 29.227 -27.346 1.00 9.58  ? 276  TYR A OH  1 
ATOM   2247 N N   . TYR A 1 277 ? 47.032 30.067 -24.384 1.00 8.12  ? 277  TYR A N   1 
ATOM   2248 C CA  . TYR A 1 277 ? 47.150 31.329 -25.112 1.00 7.65  ? 277  TYR A CA  1 
ATOM   2249 C C   . TYR A 1 277 ? 46.315 31.370 -26.384 1.00 11.26 ? 277  TYR A C   1 
ATOM   2250 O O   . TYR A 1 277 ? 45.674 32.393 -26.654 1.00 11.80 ? 277  TYR A O   1 
ATOM   2251 C CB  . TYR A 1 277 ? 48.622 31.627 -25.455 1.00 8.68  ? 277  TYR A CB  1 
ATOM   2252 C CG  . TYR A 1 277 ? 49.464 31.913 -24.221 1.00 12.13 ? 277  TYR A CG  1 
ATOM   2253 C CD1 . TYR A 1 277 ? 50.070 30.877 -23.503 1.00 11.86 ? 277  TYR A CD1 1 
ATOM   2254 C CD2 . TYR A 1 277 ? 49.611 33.212 -23.751 1.00 8.15  ? 277  TYR A CD2 1 
ATOM   2255 C CE1 . TYR A 1 277 ? 50.819 31.144 -22.344 1.00 9.61  ? 277  TYR A CE1 1 
ATOM   2256 C CE2 . TYR A 1 277 ? 50.346 33.488 -22.603 1.00 10.75 ? 277  TYR A CE2 1 
ATOM   2257 C CZ  . TYR A 1 277 ? 50.943 32.458 -21.912 1.00 12.09 ? 277  TYR A CZ  1 
ATOM   2258 O OH  . TYR A 1 277 ? 51.674 32.773 -20.798 1.00 11.38 ? 277  TYR A OH  1 
ATOM   2259 N N   . THR A 1 278 ? 46.281 30.296 -27.169 1.00 7.36  ? 278  THR A N   1 
ATOM   2260 C CA  . THR A 1 278 ? 45.540 30.323 -28.428 1.00 9.39  ? 278  THR A CA  1 
ATOM   2261 C C   . THR A 1 278 ? 45.313 28.887 -28.890 1.00 11.80 ? 278  THR A C   1 
ATOM   2262 O O   . THR A 1 278 ? 45.758 27.930 -28.250 1.00 9.25  ? 278  THR A O   1 
ATOM   2263 C CB  . THR A 1 278 ? 46.273 31.161 -29.489 1.00 12.61 ? 278  THR A CB  1 
ATOM   2264 O OG1 . THR A 1 278 ? 45.416 31.373 -30.622 1.00 11.25 ? 278  THR A OG1 1 
ATOM   2265 C CG2 . THR A 1 278 ? 47.546 30.470 -29.946 1.00 10.42 ? 278  THR A CG2 1 
ATOM   2266 N N   . ARG A 1 279 ? 44.580 28.749 -29.995 1.00 9.20  ? 279  ARG A N   1 
ATOM   2267 C CA  . ARG A 1 279 ? 44.228 27.456 -30.558 1.00 9.98  ? 279  ARG A CA  1 
ATOM   2268 C C   . ARG A 1 279 ? 45.238 27.053 -31.634 1.00 10.33 ? 279  ARG A C   1 
ATOM   2269 O O   . ARG A 1 279 ? 46.199 27.765 -31.923 1.00 12.09 ? 279  ARG A O   1 
ATOM   2270 C CB  . ARG A 1 279 ? 42.818 27.490 -31.151 1.00 10.17 ? 279  ARG A CB  1 
ATOM   2271 C CG  . ARG A 1 279 ? 42.673 28.455 -32.326 1.00 11.60 ? 279  ARG A CG  1 
ATOM   2272 C CD  . ARG A 1 279 ? 41.394 28.179 -33.135 1.00 12.77 ? 279  ARG A CD  1 
ATOM   2273 N NE  . ARG A 1 279 ? 41.116 29.243 -34.095 1.00 11.02 ? 279  ARG A NE  1 
ATOM   2274 C CZ  . ARG A 1 279 ? 40.017 29.319 -34.833 1.00 15.73 ? 279  ARG A CZ  1 
ATOM   2275 N NH1 . ARG A 1 279 ? 39.093 28.370 -34.796 1.00 13.65 ? 279  ARG A NH1 1 
ATOM   2276 N NH2 . ARG A 1 279 ? 39.835 30.378 -35.623 1.00 13.54 ? 279  ARG A NH2 1 
ATOM   2277 N N   . ALA A 1 280 ? 45.009 25.898 -32.247 1.00 10.54 ? 280  ALA A N   1 
ATOM   2278 C CA  . ALA A 1 280 ? 45.841 25.434 -33.346 1.00 11.80 ? 280  ALA A CA  1 
ATOM   2279 C C   . ALA A 1 280 ? 44.933 24.689 -34.308 1.00 13.65 ? 280  ALA A C   1 
ATOM   2280 O O   . ALA A 1 280 ? 44.045 23.954 -33.870 1.00 12.78 ? 280  ALA A O   1 
ATOM   2281 C CB  . ALA A 1 280 ? 46.974 24.524 -32.840 1.00 12.19 ? 280  ALA A CB  1 
ATOM   2282 N N   . ILE A 1 281 ? 45.127 24.893 -35.608 1.00 12.33 ? 281  ILE A N   1 
ATOM   2283 C CA  . ILE A 1 281 ? 44.346 24.194 -36.629 1.00 17.56 ? 281  ILE A CA  1 
ATOM   2284 C C   . ILE A 1 281 ? 45.239 23.128 -37.244 1.00 14.77 ? 281  ILE A C   1 
ATOM   2285 O O   . ILE A 1 281 ? 46.384 23.411 -37.623 1.00 14.57 ? 281  ILE A O   1 
ATOM   2286 C CB  . ILE A 1 281 ? 43.804 25.154 -37.704 1.00 15.42 ? 281  ILE A CB  1 
ATOM   2287 C CG1 . ILE A 1 281 ? 42.943 26.241 -37.061 1.00 16.51 ? 281  ILE A CG1 1 
ATOM   2288 C CG2 . ILE A 1 281 ? 42.982 24.392 -38.751 1.00 14.42 ? 281  ILE A CG2 1 
ATOM   2289 C CD1 . ILE A 1 281 ? 41.693 25.735 -36.383 1.00 18.74 ? 281  ILE A CD1 1 
ATOM   2290 N N   . VAL A 1 282 ? 44.736 21.900 -37.320 1.00 11.54 ? 282  VAL A N   1 
ATOM   2291 C CA  . VAL A 1 282 ? 45.548 20.808 -37.835 1.00 14.00 ? 282  VAL A CA  1 
ATOM   2292 C C   . VAL A 1 282 ? 44.852 20.175 -39.028 1.00 16.33 ? 282  VAL A C   1 
ATOM   2293 O O   . VAL A 1 282 ? 43.632 20.249 -39.197 1.00 15.47 ? 282  VAL A O   1 
ATOM   2294 C CB  . VAL A 1 282 ? 45.853 19.730 -36.771 1.00 16.39 ? 282  VAL A CB  1 
ATOM   2295 C CG1 . VAL A 1 282 ? 46.487 20.356 -35.524 1.00 19.48 ? 282  VAL A CG1 1 
ATOM   2296 C CG2 . VAL A 1 282 ? 44.600 18.955 -36.419 1.00 18.15 ? 282  VAL A CG2 1 
ATOM   2297 N N   . LYS A 1 283 ? 45.652 19.522 -39.856 1.00 17.20 ? 283  LYS A N   1 
ATOM   2298 C CA  . LYS A 1 283 ? 45.106 18.672 -40.896 1.00 20.55 ? 283  LYS A CA  1 
ATOM   2299 C C   . LYS A 1 283 ? 46.023 17.473 -41.087 1.00 18.22 ? 283  LYS A C   1 
ATOM   2300 O O   . LYS A 1 283 ? 47.241 17.557 -40.893 1.00 16.67 ? 283  LYS A O   1 
ATOM   2301 C CB  . LYS A 1 283 ? 44.906 19.430 -42.211 1.00 24.97 ? 283  LYS A CB  1 
ATOM   2302 C CG  . LYS A 1 283 ? 46.122 19.485 -43.087 1.00 31.16 ? 283  LYS A CG  1 
ATOM   2303 C CD  . LYS A 1 283 ? 45.787 20.009 -44.479 1.00 33.55 ? 283  LYS A CD  1 
ATOM   2304 C CE  . LYS A 1 283 ? 47.026 20.635 -45.101 1.00 42.48 ? 283  LYS A CE  1 
ATOM   2305 N NZ  . LYS A 1 283 ? 46.932 20.802 -46.585 1.00 48.14 ? 283  LYS A NZ  1 
ATOM   2306 N N   . ARG A 1 284 ? 45.409 16.357 -41.460 1.00 18.99 ? 284  ARG A N   1 
ATOM   2307 C CA  . ARG A 1 284 ? 46.124 15.106 -41.658 1.00 21.25 ? 284  ARG A CA  1 
ATOM   2308 C C   . ARG A 1 284 ? 47.199 15.254 -42.729 1.00 23.64 ? 284  ARG A C   1 
ATOM   2309 O O   . ARG A 1 284 ? 47.002 15.933 -43.738 1.00 22.45 ? 284  ARG A O   1 
ATOM   2310 C CB  . ARG A 1 284 ? 45.129 14.017 -42.058 1.00 21.54 ? 284  ARG A CB  1 
ATOM   2311 C CG  . ARG A 1 284 ? 45.736 12.639 -42.152 1.00 28.44 ? 284  ARG A CG  1 
ATOM   2312 C CD  . ARG A 1 284 ? 45.501 11.869 -40.885 1.00 37.01 ? 284  ARG A CD  1 
ATOM   2313 N NE  . ARG A 1 284 ? 44.180 11.258 -40.873 1.00 41.73 ? 284  ARG A NE  1 
ATOM   2314 C CZ  . ARG A 1 284 ? 43.467 11.034 -39.779 1.00 42.05 ? 284  ARG A CZ  1 
ATOM   2315 N NH1 . ARG A 1 284 ? 43.910 11.378 -38.578 1.00 43.58 ? 284  ARG A NH1 1 
ATOM   2316 N NH2 . ARG A 1 284 ? 42.280 10.445 -39.890 1.00 48.23 ? 284  ARG A NH2 1 
ATOM   2317 N N   . THR A 1 285 ? 48.357 14.617 -42.496 1.00 19.58 ? 285  THR A N   1 
ATOM   2318 C CA  . THR A 1 285 ? 49.427 14.545 -43.482 1.00 19.41 ? 285  THR A CA  1 
ATOM   2319 C C   . THR A 1 285 ? 49.337 13.246 -44.279 1.00 20.31 ? 285  THR A C   1 
ATOM   2320 O O   . THR A 1 285 ? 48.804 12.246 -43.798 1.00 21.40 ? 285  THR A O   1 
ATOM   2321 C CB  . THR A 1 285 ? 50.789 14.620 -42.794 1.00 22.69 ? 285  THR A CB  1 
ATOM   2322 O OG1 . THR A 1 285 ? 50.893 13.554 -41.841 1.00 20.56 ? 285  THR A OG1 1 
ATOM   2323 C CG2 . THR A 1 285 ? 50.998 15.962 -42.098 1.00 21.57 ? 285  THR A CG2 1 
ATOM   2324 N N   . PRO A 1 286 ? 49.891 13.214 -45.495 1.00 28.63 ? 286  PRO A N   1 
ATOM   2325 C CA  . PRO A 1 286 ? 49.844 11.965 -46.270 1.00 31.28 ? 286  PRO A CA  1 
ATOM   2326 C C   . PRO A 1 286 ? 50.654 10.834 -45.651 1.00 28.31 ? 286  PRO A C   1 
ATOM   2327 O O   . PRO A 1 286 ? 50.275 9.667  -45.796 1.00 33.64 ? 286  PRO A O   1 
ATOM   2328 C CB  . PRO A 1 286 ? 50.408 12.382 -47.631 1.00 29.40 ? 286  PRO A CB  1 
ATOM   2329 C CG  . PRO A 1 286 ? 51.354 13.494 -47.308 1.00 33.93 ? 286  PRO A CG  1 
ATOM   2330 C CD  . PRO A 1 286 ? 50.695 14.251 -46.174 1.00 28.25 ? 286  PRO A CD  1 
ATOM   2331 N N   . SER A 1 287 ? 51.744 11.134 -44.956 1.00 24.87 ? 287  SER A N   1 
ATOM   2332 C CA  . SER A 1 287 ? 52.589 10.103 -44.375 1.00 30.42 ? 287  SER A CA  1 
ATOM   2333 C C   . SER A 1 287 ? 52.534 10.150 -42.853 1.00 25.49 ? 287  SER A C   1 
ATOM   2334 O O   . SER A 1 287 ? 52.188 11.164 -42.243 1.00 23.23 ? 287  SER A O   1 
ATOM   2335 C CB  . SER A 1 287 ? 54.041 10.251 -44.843 1.00 30.06 ? 287  SER A CB  1 
ATOM   2336 O OG  . SER A 1 287 ? 54.151 10.027 -46.237 1.00 41.85 ? 287  SER A OG  1 
ATOM   2337 N N   . VAL A 1 288 ? 52.877 9.025  -42.248 1.00 21.67 ? 288  VAL A N   1 
ATOM   2338 C CA  . VAL A 1 288 ? 52.997 8.917  -40.803 1.00 22.16 ? 288  VAL A CA  1 
ATOM   2339 C C   . VAL A 1 288 ? 54.468 9.025  -40.445 1.00 17.61 ? 288  VAL A C   1 
ATOM   2340 O O   . VAL A 1 288 ? 55.307 8.316  -41.011 1.00 14.80 ? 288  VAL A O   1 
ATOM   2341 C CB  . VAL A 1 288 ? 52.404 7.599  -40.281 1.00 23.65 ? 288  VAL A CB  1 
ATOM   2342 C CG1 . VAL A 1 288 ? 52.611 7.505  -38.779 1.00 18.44 ? 288  VAL A CG1 1 
ATOM   2343 C CG2 . VAL A 1 288 ? 50.926 7.514  -40.623 1.00 28.92 ? 288  VAL A CG2 1 
ATOM   2344 N N   . LEU A 1 289 ? 54.786 9.914  -39.515 1.00 16.72 ? 289  LEU A N   1 
ATOM   2345 C CA  . LEU A 1 289 ? 56.120 10.000 -38.940 1.00 12.91 ? 289  LEU A CA  1 
ATOM   2346 C C   . LEU A 1 289 ? 56.082 9.334  -37.573 1.00 16.47 ? 289  LEU A C   1 
ATOM   2347 O O   . LEU A 1 289 ? 55.277 9.719  -36.717 1.00 13.45 ? 289  LEU A O   1 
ATOM   2348 C CB  . LEU A 1 289 ? 56.570 11.457 -38.823 1.00 12.58 ? 289  LEU A CB  1 
ATOM   2349 C CG  . LEU A 1 289 ? 57.765 11.710 -37.900 1.00 13.48 ? 289  LEU A CG  1 
ATOM   2350 C CD1 . LEU A 1 289 ? 58.997 10.957 -38.392 1.00 13.33 ? 289  LEU A CD1 1 
ATOM   2351 C CD2 . LEU A 1 289 ? 58.038 13.208 -37.773 1.00 12.66 ? 289  LEU A CD2 1 
ATOM   2352 N N   . SER A 1 290 ? 56.933 8.331  -37.368 1.00 12.64 ? 290  SER A N   1 
ATOM   2353 C CA  . SER A 1 290 ? 56.998 7.637  -36.090 1.00 15.65 ? 290  SER A CA  1 
ATOM   2354 C C   . SER A 1 290 ? 58.402 7.694  -35.511 1.00 10.15 ? 290  SER A C   1 
ATOM   2355 O O   . SER A 1 290 ? 59.400 7.656  -36.238 1.00 12.82 ? 290  SER A O   1 
ATOM   2356 C CB  . SER A 1 290 ? 56.568 6.156  -36.206 1.00 16.48 ? 290  SER A CB  1 
ATOM   2357 O OG  . SER A 1 290 ? 55.501 6.006  -37.115 1.00 24.88 ? 290  SER A OG  1 
ATOM   2358 N N   . SER A 1 291 ? 58.468 7.768  -34.191 1.00 9.22  ? 291  SER A N   1 
ATOM   2359 C CA  . SER A 1 291 ? 59.748 7.635  -33.527 1.00 11.54 ? 291  SER A CA  1 
ATOM   2360 C C   . SER A 1 291 ? 60.288 6.220  -33.726 1.00 10.85 ? 291  SER A C   1 
ATOM   2361 O O   . SER A 1 291 ? 59.556 5.290  -34.084 1.00 9.87  ? 291  SER A O   1 
ATOM   2362 C CB  . SER A 1 291 ? 59.605 7.950  -32.043 1.00 11.24 ? 291  SER A CB  1 
ATOM   2363 O OG  . SER A 1 291 ? 58.786 6.981  -31.379 1.00 9.61  ? 291  SER A OG  1 
ATOM   2364 N N   . SER A 1 292 ? 61.573 6.053  -33.438 1.00 9.82  ? 292  SER A N   1 
ATOM   2365 C CA  . SER A 1 292 ? 62.259 4.744  -33.584 1.00 11.48 ? 292  SER A CA  1 
ATOM   2366 C C   . SER A 1 292 ? 61.632 3.690  -32.650 1.00 12.26 ? 292  SER A C   1 
ATOM   2367 O O   . SER A 1 292 ? 61.607 2.533  -33.043 1.00 12.81 ? 292  SER A O   1 
ATOM   2368 C CB  . SER A 1 292 ? 63.737 4.937  -33.387 1.00 12.15 ? 292  SER A CB  1 
ATOM   2369 O OG  . SER A 1 292 ? 64.252 5.904  -34.284 1.00 13.24 ? 292  SER A OG  1 
ATOM   2370 N N   . SER A 1 293 ? 61.135 4.106  -31.488 1.00 10.85 ? 293  SER A N   1 
ATOM   2371 C CA  . SER A 1 293 ? 60.446 3.224  -30.512 1.00 12.20 ? 293  SER A CA  1 
ATOM   2372 C C   . SER A 1 293 ? 59.053 2.843  -31.009 1.00 12.68 ? 293  SER A C   1 
ATOM   2373 O O   . SER A 1 293 ? 58.442 1.983  -30.401 1.00 11.62 ? 293  SER A O   1 
ATOM   2374 C CB  . SER A 1 293 ? 60.280 3.968  -29.214 1.00 12.53 ? 293  SER A CB  1 
ATOM   2375 O OG  . SER A 1 293 ? 59.340 5.011  -29.335 1.00 10.64 ? 293  SER A OG  1 
ATOM   2376 N N   . GLY A 1 294 ? 58.544 3.566  -32.009 1.00 12.26 ? 294  GLY A N   1 
ATOM   2377 C CA  . GLY A 1 294 ? 57.153 3.366  -32.447 1.00 11.67 ? 294  GLY A CA  1 
ATOM   2378 C C   . GLY A 1 294 ? 56.152 3.952  -31.450 1.00 15.44 ? 294  GLY A C   1 
ATOM   2379 O O   . GLY A 1 294 ? 54.967 3.840  -31.692 1.00 14.70 ? 294  GLY A O   1 
ATOM   2380 N N   . ARG A 1 295 ? 56.636 4.589  -30.380 1.00 11.79 ? 295  ARG A N   1 
ATOM   2381 C CA  . ARG A 1 295 ? 55.704 5.057  -29.316 1.00 13.89 ? 295  ARG A CA  1 
ATOM   2382 C C   . ARG A 1 295 ? 55.103 6.442  -29.640 1.00 17.30 ? 295  ARG A C   1 
ATOM   2383 O O   . ARG A 1 295 ? 54.003 6.700  -29.168 1.00 17.69 ? 295  ARG A O   1 
ATOM   2384 C CB  . ARG A 1 295 ? 56.387 5.023  -27.945 1.00 30.00 ? 295  ARG A CB  1 
ATOM   2385 C CG  . ARG A 1 295 ? 57.036 3.696  -27.586 1.00 30.00 ? 295  ARG A CG  1 
ATOM   2386 C CD  . ARG A 1 295 ? 57.816 3.864  -26.299 1.00 30.00 ? 295  ARG A CD  1 
ATOM   2387 N NE  . ARG A 1 295 ? 56.951 4.274  -25.206 1.00 30.00 ? 295  ARG A NE  1 
ATOM   2388 C CZ  . ARG A 1 295 ? 56.979 5.461  -24.612 1.00 30.00 ? 295  ARG A CZ  1 
ATOM   2389 N NH1 . ARG A 1 295 ? 57.841 6.385  -25.001 1.00 30.00 ? 295  ARG A NH1 1 
ATOM   2390 N NH2 . ARG A 1 295 ? 56.141 5.718  -23.625 1.00 30.00 ? 295  ARG A NH2 1 
ATOM   2391 N N   . ILE A 1 296 ? 55.829 7.293  -30.367 1.00 13.11 ? 296  ILE A N   1 
ATOM   2392 C CA  . ILE A 1 296 ? 55.318 8.630  -30.780 1.00 14.78 ? 296  ILE A CA  1 
ATOM   2393 C C   . ILE A 1 296 ? 54.982 8.593  -32.280 1.00 16.31 ? 296  ILE A C   1 
ATOM   2394 O O   . ILE A 1 296 ? 55.813 8.120  -33.049 1.00 13.44 ? 296  ILE A O   1 
ATOM   2395 C CB  . ILE A 1 296 ? 56.292 9.768  -30.398 1.00 16.93 ? 296  ILE A CB  1 
ATOM   2396 C CG1 . ILE A 1 296 ? 56.570 9.804  -28.895 1.00 18.21 ? 296  ILE A CG1 1 
ATOM   2397 C CG2 . ILE A 1 296 ? 55.783 11.101 -30.912 1.00 19.59 ? 296  ILE A CG2 1 
ATOM   2398 C CD1 . ILE A 1 296 ? 55.327 9.834  -28.051 1.00 23.58 ? 296  ILE A CD1 1 
ATOM   2399 N N   . LYS A 1 297 ? 53.806 9.097  -32.641 1.00 15.52 ? 297  LYS A N   1 
ATOM   2400 C CA  . LYS A 1 297 ? 53.346 9.059  -34.024 1.00 17.86 ? 297  LYS A CA  1 
ATOM   2401 C C   . LYS A 1 297 ? 52.781 10.427 -34.391 1.00 20.33 ? 297  LYS A C   1 
ATOM   2402 O O   . LYS A 1 297 ? 51.975 10.985 -33.641 1.00 16.84 ? 297  LYS A O   1 
ATOM   2403 C CB  . LYS A 1 297 ? 52.302 7.946  -34.193 1.00 19.15 ? 297  LYS A CB  1 
ATOM   2404 C CG  . LYS A 1 297 ? 51.265 8.148  -35.275 1.00 29.23 ? 297  LYS A CG  1 
ATOM   2405 C CD  . LYS A 1 297 ? 50.480 6.844  -35.490 1.00 35.92 ? 297  LYS A CD  1 
ATOM   2406 C CE  . LYS A 1 297 ? 49.564 6.902  -36.718 1.00 35.79 ? 297  LYS A CE  1 
ATOM   2407 N NZ  . LYS A 1 297 ? 48.759 5.652  -36.886 1.00 37.08 ? 297  LYS A NZ  1 
ATOM   2408 N N   . ILE A 1 298 ? 53.233 10.986 -35.516 1.00 17.36 ? 298  ILE A N   1 
ATOM   2409 C CA  . ILE A 1 298 ? 52.784 12.296 -35.984 1.00 15.41 ? 298  ILE A CA  1 
ATOM   2410 C C   . ILE A 1 298 ? 52.260 12.150 -37.404 1.00 17.22 ? 298  ILE A C   1 
ATOM   2411 O O   . ILE A 1 298 ? 52.995 11.732 -38.307 1.00 16.13 ? 298  ILE A O   1 
ATOM   2412 C CB  . ILE A 1 298 ? 53.897 13.351 -35.917 1.00 13.95 ? 298  ILE A CB  1 
ATOM   2413 C CG1 . ILE A 1 298 ? 54.315 13.590 -34.462 1.00 14.42 ? 298  ILE A CG1 1 
ATOM   2414 C CG2 . ILE A 1 298 ? 53.423 14.661 -36.559 1.00 16.42 ? 298  ILE A CG2 1 
ATOM   2415 C CD1 . ILE A 1 298 ? 55.618 14.390 -34.319 1.00 15.90 ? 298  ILE A CD1 1 
ATOM   2416 N N   . ASN A 1 299 ? 50.987 12.483 -37.595 1.00 17.45 ? 299  ASN A N   1 
ATOM   2417 C CA  . ASN A 1 299 ? 50.336 12.403 -38.896 1.00 18.46 ? 299  ASN A CA  1 
ATOM   2418 C C   . ASN A 1 299 ? 49.425 13.608 -39.107 1.00 15.45 ? 299  ASN A C   1 
ATOM   2419 O O   . ASN A 1 299 ? 48.348 13.495 -39.692 1.00 18.93 ? 299  ASN A O   1 
ATOM   2420 C CB  . ASN A 1 299 ? 49.550 11.098 -39.040 1.00 18.07 ? 299  ASN A CB  1 
ATOM   2421 C CG  . ASN A 1 299 ? 48.496 10.923 -37.951 1.00 22.90 ? 299  ASN A CG  1 
ATOM   2422 O OD1 . ASN A 1 299 ? 48.399 11.720 -37.014 1.00 26.85 ? 299  ASN A OD1 1 
ATOM   2423 N ND2 . ASN A 1 299 ? 47.708 9.870  -38.067 1.00 31.77 ? 299  ASN A ND2 1 
ATOM   2424 N N   . TRP A 1 300 ? 49.839 14.775 -38.612 1.00 15.06 ? 300  TRP A N   1 
ATOM   2425 C CA  . TRP A 1 300 ? 49.118 16.026 -38.817 1.00 18.24 ? 300  TRP A CA  1 
ATOM   2426 C C   . TRP A 1 300 ? 50.142 17.126 -39.046 1.00 19.49 ? 300  TRP A C   1 
ATOM   2427 O O   . TRP A 1 300 ? 51.325 16.977 -38.726 1.00 15.79 ? 300  TRP A O   1 
ATOM   2428 C CB  . TRP A 1 300 ? 48.220 16.409 -37.620 1.00 14.67 ? 300  TRP A CB  1 
ATOM   2429 C CG  . TRP A 1 300 ? 49.038 16.685 -36.396 1.00 15.69 ? 300  TRP A CG  1 
ATOM   2430 C CD1 . TRP A 1 300 ? 49.576 17.880 -36.011 1.00 18.03 ? 300  TRP A CD1 1 
ATOM   2431 C CD2 . TRP A 1 300 ? 49.477 15.720 -35.442 1.00 15.12 ? 300  TRP A CD2 1 
ATOM   2432 N NE1 . TRP A 1 300 ? 50.312 17.718 -34.859 1.00 17.53 ? 300  TRP A NE1 1 
ATOM   2433 C CE2 . TRP A 1 300 ? 50.262 16.398 -34.490 1.00 16.97 ? 300  TRP A CE2 1 
ATOM   2434 C CE3 . TRP A 1 300 ? 49.268 14.346 -35.292 1.00 18.26 ? 300  TRP A CE3 1 
ATOM   2435 C CZ2 . TRP A 1 300 ? 50.843 15.749 -33.405 1.00 19.26 ? 300  TRP A CZ2 1 
ATOM   2436 C CZ3 . TRP A 1 300 ? 49.849 13.700 -34.210 1.00 17.33 ? 300  TRP A CZ3 1 
ATOM   2437 C CH2 . TRP A 1 300 ? 50.633 14.401 -33.289 1.00 16.99 ? 300  TRP A CH2 1 
ATOM   2438 N N   . SER A 1 301 ? 49.674 18.225 -39.621 1.00 12.61 ? 301  SER A N   1 
ATOM   2439 C CA  . SER A 1 301 ? 50.438 19.455 -39.719 1.00 16.84 ? 301  SER A CA  1 
ATOM   2440 C C   . SER A 1 301 ? 49.586 20.584 -39.168 1.00 17.73 ? 301  SER A C   1 
ATOM   2441 O O   . SER A 1 301 ? 48.359 20.484 -39.114 1.00 17.08 ? 301  SER A O   1 
ATOM   2442 C CB  . SER A 1 301 ? 50.836 19.768 -41.173 1.00 18.90 ? 301  SER A CB  1 
ATOM   2443 O OG  . SER A 1 301 ? 49.674 19.980 -41.961 1.00 21.83 ? 301  SER A OG  1 
ATOM   2444 N N   . PHE A 1 302 ? 50.242 21.665 -38.761 1.00 18.84 ? 302  PHE A N   1 
ATOM   2445 C CA  . PHE A 1 302 ? 49.549 22.856 -38.293 1.00 21.86 ? 302  PHE A CA  1 
ATOM   2446 C C   . PHE A 1 302 ? 49.299 23.800 -39.466 1.00 20.46 ? 302  PHE A C   1 
ATOM   2447 O O   . PHE A 1 302 ? 50.223 24.125 -40.217 1.00 23.88 ? 302  PHE A O   1 
ATOM   2448 C CB  . PHE A 1 302 ? 50.363 23.550 -37.200 1.00 20.59 ? 302  PHE A CB  1 
ATOM   2449 C CG  . PHE A 1 302 ? 50.447 22.759 -35.928 1.00 20.45 ? 302  PHE A CG  1 
ATOM   2450 C CD1 . PHE A 1 302 ? 49.344 22.636 -35.099 1.00 20.84 ? 302  PHE A CD1 1 
ATOM   2451 C CD2 . PHE A 1 302 ? 51.622 22.115 -35.574 1.00 27.80 ? 302  PHE A CD2 1 
ATOM   2452 C CE1 . PHE A 1 302 ? 49.409 21.892 -33.922 1.00 24.10 ? 302  PHE A CE1 1 
ATOM   2453 C CE2 . PHE A 1 302 ? 51.698 21.371 -34.404 1.00 31.57 ? 302  PHE A CE2 1 
ATOM   2454 C CZ  . PHE A 1 302 ? 50.585 21.259 -33.576 1.00 26.65 ? 302  PHE A CZ  1 
ATOM   2455 N N   . VAL A 1 303 ? 48.051 24.239 -39.610 1.00 24.17 ? 303  VAL A N   1 
ATOM   2456 C CA  . VAL A 1 303 ? 47.609 25.080 -40.725 1.00 23.17 ? 303  VAL A CA  1 
ATOM   2457 C C   . VAL A 1 303 ? 47.956 26.543 -40.449 1.00 23.66 ? 303  VAL A C   1 
ATOM   2458 O O   . VAL A 1 303 ? 47.537 27.096 -39.420 1.00 21.04 ? 303  VAL A O   1 
ATOM   2459 C CB  . VAL A 1 303 ? 46.102 24.910 -40.969 1.00 19.37 ? 303  VAL A CB  1 
ATOM   2460 C CG1 . VAL A 1 303 ? 45.635 25.786 -42.130 1.00 23.50 ? 303  VAL A CG1 1 
ATOM   2461 C CG2 . VAL A 1 303 ? 45.770 23.444 -41.226 1.00 20.08 ? 303  VAL A CG2 1 
ATOM   2462 N N   . PRO A 1 304 ? 48.702 27.209 -41.331 1.00 24.91 ? 304  PRO A N   1 
ATOM   2463 C CA  . PRO A 1 304 ? 49.052 28.615 -41.093 1.00 23.78 ? 304  PRO A CA  1 
ATOM   2464 C C   . PRO A 1 304 ? 47.854 29.544 -41.262 1.00 21.46 ? 304  PRO A C   1 
ATOM   2465 O O   . PRO A 1 304 ? 46.857 29.223 -41.913 1.00 19.85 ? 304  PRO A O   1 
ATOM   2466 C CB  . PRO A 1 304 ? 50.138 28.903 -42.137 1.00 26.18 ? 304  PRO A CB  1 
ATOM   2467 C CG  . PRO A 1 304 ? 50.008 27.845 -43.167 1.00 29.06 ? 304  PRO A CG  1 
ATOM   2468 C CD  . PRO A 1 304 ? 49.309 26.665 -42.560 1.00 24.02 ? 304  PRO A CD  1 
ATOM   2469 N N   . GLY A 1 305 ? 47.958 30.712 -40.631 1.00 19.53 ? 305  GLY A N   1 
ATOM   2470 C CA  . GLY A 1 305 ? 46.889 31.691 -40.635 1.00 21.22 ? 305  GLY A CA  1 
ATOM   2471 C C   . GLY A 1 305 ? 45.906 31.578 -39.490 1.00 23.90 ? 305  GLY A C   1 
ATOM   2472 O O   . GLY A 1 305 ? 44.883 32.276 -39.505 1.00 20.07 ? 305  GLY A O   1 
ATOM   2473 N N   . PHE A 1 306 ? 46.169 30.705 -38.513 1.00 18.38 ? 306  PHE A N   1 
ATOM   2474 C CA  . PHE A 1 306 ? 45.307 30.516 -37.354 1.00 19.20 ? 306  PHE A CA  1 
ATOM   2475 C C   . PHE A 1 306 ? 46.170 30.296 -36.118 1.00 19.60 ? 306  PHE A C   1 
ATOM   2476 O O   . PHE A 1 306 ? 47.338 29.911 -36.216 1.00 18.03 ? 306  PHE A O   1 
ATOM   2477 C CB  . PHE A 1 306 ? 44.377 29.299 -37.488 1.00 20.37 ? 306  PHE A CB  1 
ATOM   2478 C CG  . PHE A 1 306 ? 43.492 29.299 -38.708 1.00 22.88 ? 306  PHE A CG  1 
ATOM   2479 C CD1 . PHE A 1 306 ? 42.239 29.918 -38.677 1.00 22.16 ? 306  PHE A CD1 1 
ATOM   2480 C CD2 . PHE A 1 306 ? 43.885 28.636 -39.869 1.00 20.72 ? 306  PHE A CD2 1 
ATOM   2481 C CE1 . PHE A 1 306 ? 41.410 29.898 -39.790 1.00 26.29 ? 306  PHE A CE1 1 
ATOM   2482 C CE2 . PHE A 1 306 ? 43.057 28.606 -40.994 1.00 23.84 ? 306  PHE A CE2 1 
ATOM   2483 C CZ  . PHE A 1 306 ? 41.819 29.237 -40.955 1.00 26.36 ? 306  PHE A CZ  1 
ATOM   2484 N N   . GLY A 1 307 ? 45.557 30.494 -34.944 1.00 15.64 ? 307  GLY A N   1 
ATOM   2485 C CA  . GLY A 1 307 ? 46.215 30.251 -33.674 1.00 13.25 ? 307  GLY A CA  1 
ATOM   2486 C C   . GLY A 1 307 ? 47.559 30.943 -33.540 1.00 16.56 ? 307  GLY A C   1 
ATOM   2487 O O   . GLY A 1 307 ? 47.644 32.164 -33.686 1.00 13.51 ? 307  GLY A O   1 
ATOM   2488 N N   . GLY A 1 308 ? 48.622 30.172 -33.279 1.00 17.20 ? 308  GLY A N   1 
ATOM   2489 C CA  . GLY A 1 308 ? 49.950 30.734 -33.115 1.00 14.75 ? 308  GLY A CA  1 
ATOM   2490 C C   . GLY A 1 308 ? 50.661 31.120 -34.389 1.00 20.52 ? 308  GLY A C   1 
ATOM   2491 O O   . GLY A 1 308 ? 51.796 31.610 -34.334 1.00 18.58 ? 308  GLY A O   1 
ATOM   2492 N N   . SER A 1 309 ? 50.010 30.936 -35.541 1.00 20.75 ? 309  SER A N   1 
ATOM   2493 C CA  . SER A 1 309 ? 50.648 31.020 -36.850 1.00 24.13 ? 309  SER A CA  1 
ATOM   2494 C C   . SER A 1 309 ? 50.082 32.165 -37.684 1.00 20.26 ? 309  SER A C   1 
ATOM   2495 O O   . SER A 1 309 ? 50.020 32.075 -38.911 1.00 22.73 ? 309  SER A O   1 
ATOM   2496 C CB  . SER A 1 309 ? 50.487 29.697 -37.602 1.00 22.58 ? 309  SER A CB  1 
ATOM   2497 O OG  . SER A 1 309 ? 51.332 28.700 -37.052 1.00 35.89 ? 309  SER A OG  1 
ATOM   2498 N N   . CYS A 1 310 ? 49.663 33.245 -37.039 1.00 18.56 ? 310  CYS A N   1 
ATOM   2499 C CA  . CYS A 1 310 ? 49.094 34.372 -37.761 1.00 23.33 ? 310  CYS A CA  1 
ATOM   2500 C C   . CYS A 1 310 ? 50.163 35.414 -38.030 1.00 24.62 ? 310  CYS A C   1 
ATOM   2501 O O   . CYS A 1 310 ? 51.251 35.385 -37.450 1.00 20.79 ? 310  CYS A O   1 
ATOM   2502 C CB  . CYS A 1 310 ? 47.954 35.015 -36.974 1.00 19.18 ? 310  CYS A CB  1 
ATOM   2503 S SG  . CYS A 1 310 ? 46.604 33.900 -36.585 1.00 20.26 ? 310  CYS A SG  1 
ATOM   2504 N N   . GLN A 1 311 ? 49.838 36.342 -38.927 1.00 21.72 ? 311  GLN A N   1 
ATOM   2505 C CA  . GLN A 1 311 ? 50.666 37.526 -39.085 1.00 23.12 ? 311  GLN A CA  1 
ATOM   2506 C C   . GLN A 1 311 ? 50.558 38.407 -37.840 1.00 20.23 ? 311  GLN A C   1 
ATOM   2507 O O   . GLN A 1 311 ? 49.532 38.434 -37.159 1.00 18.87 ? 311  GLN A O   1 
ATOM   2508 C CB  . GLN A 1 311 ? 50.245 38.314 -40.331 1.00 26.65 ? 311  GLN A CB  1 
ATOM   2509 C CG  . GLN A 1 311 ? 50.821 37.743 -41.620 1.00 41.78 ? 311  GLN A CG  1 
ATOM   2510 C CD  . GLN A 1 311 ? 50.773 38.734 -42.773 1.00 51.15 ? 311  GLN A CD  1 
ATOM   2511 O OE1 . GLN A 1 311 ? 49.913 39.623 -42.813 1.00 47.74 ? 311  GLN A OE1 1 
ATOM   2512 N NE2 . GLN A 1 311 ? 51.703 38.589 -43.716 1.00 51.23 ? 311  GLN A NE2 1 
ATOM   2513 N N   . ARG A 1 312 ? 51.628 39.137 -37.554 1.00 17.92 ? 312  ARG A N   1 
ATOM   2514 C CA  . ARG A 1 312 ? 51.644 40.022 -36.399 1.00 19.96 ? 312  ARG A CA  1 
ATOM   2515 C C   . ARG A 1 312 ? 50.666 41.179 -36.594 1.00 22.25 ? 312  ARG A C   1 
ATOM   2516 O O   . ARG A 1 312 ? 50.559 41.738 -37.692 1.00 20.14 ? 312  ARG A O   1 
ATOM   2517 C CB  . ARG A 1 312 ? 53.055 40.566 -36.198 1.00 19.92 ? 312  ARG A CB  1 
ATOM   2518 C CG  . ARG A 1 312 ? 53.942 39.673 -35.373 1.00 25.42 ? 312  ARG A CG  1 
ATOM   2519 C CD  . ARG A 1 312 ? 55.391 39.796 -35.807 1.00 27.32 ? 312  ARG A CD  1 
ATOM   2520 N NE  . ARG A 1 312 ? 56.185 38.680 -35.309 1.00 37.93 ? 312  ARG A NE  1 
ATOM   2521 C CZ  . ARG A 1 312 ? 57.402 38.800 -34.792 1.00 36.18 ? 312  ARG A CZ  1 
ATOM   2522 N NH1 . ARG A 1 312 ? 58.018 39.973 -34.732 1.00 30.62 ? 312  ARG A NH1 1 
ATOM   2523 N NH2 . ARG A 1 312 ? 58.021 37.715 -34.334 1.00 35.23 ? 312  ARG A NH2 1 
ATOM   2524 N N   . ASN A 1 313 ? 49.957 41.549 -35.523 1.00 16.67 ? 313  ASN A N   1 
ATOM   2525 C CA  . ASN A 1 313 ? 49.080 42.732 -35.520 1.00 16.53 ? 313  ASN A CA  1 
ATOM   2526 C C   . ASN A 1 313 ? 48.151 42.737 -36.725 1.00 20.14 ? 313  ASN A C   1 
ATOM   2527 O O   . ASN A 1 313 ? 48.088 43.696 -37.498 1.00 17.89 ? 313  ASN A O   1 
ATOM   2528 C CB  . ASN A 1 313 ? 49.903 44.019 -35.475 1.00 15.58 ? 313  ASN A CB  1 
ATOM   2529 C CG  . ASN A 1 313 ? 50.793 44.079 -34.264 1.00 20.20 ? 313  ASN A CG  1 
ATOM   2530 O OD1 . ASN A 1 313 ? 52.019 44.045 -34.386 1.00 18.34 ? 313  ASN A OD1 1 
ATOM   2531 N ND2 . ASN A 1 313 ? 50.186 44.164 -33.080 1.00 13.00 ? 313  ASN A ND2 1 
ATOM   2532 N N   . SER A 1 314 ? 47.437 41.634 -36.894 1.00 18.82 ? 314  SER A N   1 
ATOM   2533 C CA  . SER A 1 314 ? 46.652 41.435 -38.096 1.00 20.62 ? 314  SER A CA  1 
ATOM   2534 C C   . SER A 1 314 ? 45.365 40.723 -37.715 1.00 20.44 ? 314  SER A C   1 
ATOM   2535 O O   . SER A 1 314 ? 44.811 40.960 -36.635 1.00 17.28 ? 314  SER A O   1 
ATOM   2536 C CB  . SER A 1 314 ? 47.473 40.643 -39.121 1.00 23.57 ? 314  SER A CB  1 
ATOM   2537 O OG  . SER A 1 314 ? 46.797 40.519 -40.361 1.00 25.67 ? 314  SER A OG  1 
ATOM   2538 N N   . LYS A 1 315 ? 44.872 39.867 -38.599 1.00 16.82 ? 315  LYS A N   1 
ATOM   2539 C CA  . LYS A 1 315 ? 43.726 39.021 -38.317 1.00 20.11 ? 315  LYS A CA  1 
ATOM   2540 C C   . LYS A 1 315 ? 44.056 37.605 -38.764 1.00 21.33 ? 315  LYS A C   1 
ATOM   2541 O O   . LYS A 1 315 ? 44.805 37.403 -39.728 1.00 20.65 ? 315  LYS A O   1 
ATOM   2542 C CB  . LYS A 1 315 ? 42.459 39.508 -39.054 1.00 23.17 ? 315  LYS A CB  1 
ATOM   2543 C CG  . LYS A 1 315 ? 41.857 40.792 -38.508 1.00 29.61 ? 315  LYS A CG  1 
ATOM   2544 C CD  . LYS A 1 315 ? 40.481 41.059 -39.120 1.00 38.50 ? 315  LYS A CD  1 
ATOM   2545 C CE  . LYS A 1 315 ? 40.266 42.547 -39.365 1.00 43.99 ? 315  LYS A CE  1 
ATOM   2546 N NZ  . LYS A 1 315 ? 39.302 43.146 -38.389 1.00 53.36 ? 315  LYS A NZ  1 
ATOM   2547 N N   . SER A 1 316 ? 43.502 36.625 -38.061 1.00 16.98 ? 316  SER A N   1 
ATOM   2548 C CA  . SER A 1 316 ? 43.533 35.267 -38.584 1.00 17.60 ? 316  SER A CA  1 
ATOM   2549 C C   . SER A 1 316 ? 42.641 35.159 -39.826 1.00 21.82 ? 316  SER A C   1 
ATOM   2550 O O   . SER A 1 316 ? 41.862 36.061 -40.151 1.00 16.65 ? 316  SER A O   1 
ATOM   2551 C CB  . SER A 1 316 ? 43.055 34.274 -37.533 1.00 17.20 ? 316  SER A CB  1 
ATOM   2552 O OG  . SER A 1 316 ? 41.652 34.419 -37.330 1.00 17.74 ? 316  SER A OG  1 
ATOM   2553 N N   . LEU A 1 317 ? 42.738 34.013 -40.512 1.00 25.17 ? 317  LEU A N   1 
ATOM   2554 C CA  . LEU A 1 317 ? 41.852 33.727 -41.637 1.00 24.51 ? 317  LEU A CA  1 
ATOM   2555 C C   . LEU A 1 317 ? 40.396 33.569 -41.223 1.00 26.96 ? 317  LEU A C   1 
ATOM   2556 O O   . LEU A 1 317 ? 39.529 33.541 -42.100 1.00 27.52 ? 317  LEU A O   1 
ATOM   2557 C CB  . LEU A 1 317 ? 42.311 32.465 -42.374 1.00 23.01 ? 317  LEU A CB  1 
ATOM   2558 C CG  . LEU A 1 317 ? 43.740 32.427 -42.920 1.00 26.26 ? 317  LEU A CG  1 
ATOM   2559 C CD1 . LEU A 1 317 ? 43.891 31.284 -43.915 1.00 30.62 ? 317  LEU A CD1 1 
ATOM   2560 C CD2 . LEU A 1 317 ? 44.082 33.740 -43.600 1.00 31.91 ? 317  LEU A CD2 1 
ATOM   2561 N N   . ASP A 1 318 ? 40.102 33.449 -39.927 1.00 23.10 ? 318  ASP A N   1 
ATOM   2562 C CA  . ASP A 1 318 ? 38.730 33.507 -39.432 1.00 24.75 ? 318  ASP A CA  1 
ATOM   2563 C C   . ASP A 1 318 ? 38.310 34.909 -39.007 1.00 21.53 ? 318  ASP A C   1 
ATOM   2564 O O   . ASP A 1 318 ? 37.251 35.061 -38.388 1.00 24.31 ? 318  ASP A O   1 
ATOM   2565 C CB  . ASP A 1 318 ? 38.542 32.542 -38.255 1.00 22.74 ? 318  ASP A CB  1 
ATOM   2566 C CG  . ASP A 1 318 ? 38.050 31.177 -38.691 1.00 36.76 ? 318  ASP A CG  1 
ATOM   2567 O OD1 . ASP A 1 318 ? 37.846 30.967 -39.911 1.00 37.61 ? 318  ASP A OD1 1 
ATOM   2568 O OD2 . ASP A 1 318 ? 37.885 30.302 -37.808 1.00 43.59 ? 318  ASP A OD2 1 
ATOM   2569 N N   . GLY A 1 319 ? 39.126 35.925 -39.280 1.00 22.97 ? 319  GLY A N   1 
ATOM   2570 C CA  . GLY A 1 319 ? 38.754 37.287 -38.944 1.00 24.71 ? 319  GLY A CA  1 
ATOM   2571 C C   . GLY A 1 319 ? 38.968 37.692 -37.501 1.00 24.06 ? 319  GLY A C   1 
ATOM   2572 O O   . GLY A 1 319 ? 38.485 38.755 -37.097 1.00 23.18 ? 319  GLY A O   1 
ATOM   2573 N N   . ARG A 1 320 ? 39.692 36.884 -36.702 1.00 18.84 ? 320  ARG A N   1 
ATOM   2574 C CA  . ARG A 1 320 ? 39.914 37.236 -35.304 1.00 17.68 ? 320  ARG A CA  1 
ATOM   2575 C C   . ARG A 1 320 ? 41.238 37.975 -35.143 1.00 16.47 ? 320  ARG A C   1 
ATOM   2576 O O   . ARG A 1 320 ? 42.188 37.712 -35.885 1.00 14.80 ? 320  ARG A O   1 
ATOM   2577 C CB  . ARG A 1 320 ? 39.926 35.976 -34.446 1.00 20.27 ? 320  ARG A CB  1 
ATOM   2578 C CG  . ARG A 1 320 ? 38.579 35.303 -34.337 1.00 19.47 ? 320  ARG A CG  1 
ATOM   2579 C CD  . ARG A 1 320 ? 38.710 33.990 -33.586 1.00 22.56 ? 320  ARG A CD  1 
ATOM   2580 N NE  . ARG A 1 320 ? 37.457 33.243 -33.570 1.00 19.56 ? 320  ARG A NE  1 
ATOM   2581 C CZ  . ARG A 1 320 ? 36.612 33.240 -32.551 1.00 24.74 ? 320  ARG A CZ  1 
ATOM   2582 N NH1 . ARG A 1 320 ? 36.845 33.954 -31.456 1.00 22.68 ? 320  ARG A NH1 1 
ATOM   2583 N NH2 . ARG A 1 320 ? 35.512 32.494 -32.624 1.00 24.28 ? 320  ARG A NH2 1 
ATOM   2584 N N   . PRO A 1 321 ? 41.350 38.892 -34.176 1.00 15.98 ? 321  PRO A N   1 
ATOM   2585 C CA  . PRO A 1 321 ? 42.588 39.675 -34.049 1.00 13.20 ? 321  PRO A CA  1 
ATOM   2586 C C   . PRO A 1 321 ? 43.770 38.791 -33.687 1.00 15.71 ? 321  PRO A C   1 
ATOM   2587 O O   . PRO A 1 321 ? 43.632 37.799 -32.961 1.00 14.85 ? 321  PRO A O   1 
ATOM   2588 C CB  . PRO A 1 321 ? 42.276 40.672 -32.918 1.00 19.02 ? 321  PRO A CB  1 
ATOM   2589 C CG  . PRO A 1 321 ? 40.789 40.647 -32.752 1.00 19.18 ? 321  PRO A CG  1 
ATOM   2590 C CD  . PRO A 1 321 ? 40.335 39.287 -33.184 1.00 14.10 ? 321  PRO A CD  1 
ATOM   2591 N N   . SER A 1 322 ? 44.939 39.151 -34.220 1.00 13.77 ? 322  SER A N   1 
ATOM   2592 C CA  . SER A 1 322 ? 46.212 38.578 -33.806 1.00 13.60 ? 322  SER A CA  1 
ATOM   2593 C C   . SER A 1 322 ? 47.097 39.670 -33.214 1.00 13.63 ? 322  SER A C   1 
ATOM   2594 O O   . SER A 1 322 ? 47.070 40.820 -33.661 1.00 14.07 ? 322  SER A O   1 
ATOM   2595 C CB  . SER A 1 322 ? 46.941 37.885 -34.982 1.00 14.59 ? 322  SER A CB  1 
ATOM   2596 O OG  . SER A 1 322 ? 47.170 38.799 -36.049 1.00 16.28 ? 322  SER A OG  1 
ATOM   2597 N N   . THR A 1 323 ? 47.913 39.282 -32.228 1.00 11.29 ? 323  THR A N   1 
ATOM   2598 C CA  . THR A 1 323 ? 48.602 40.198 -31.328 1.00 13.30 ? 323  THR A CA  1 
ATOM   2599 C C   . THR A 1 323 ? 50.008 40.543 -31.832 1.00 13.37 ? 323  THR A C   1 
ATOM   2600 O O   . THR A 1 323 ? 50.365 40.276 -32.981 1.00 13.47 ? 323  THR A O   1 
ATOM   2601 C CB  . THR A 1 323 ? 48.689 39.576 -29.940 1.00 13.35 ? 323  THR A CB  1 
ATOM   2602 O OG1 . THR A 1 323 ? 49.424 38.341 -30.038 1.00 12.22 ? 323  THR A OG1 1 
ATOM   2603 C CG2 . THR A 1 323 ? 47.284 39.317 -29.378 1.00 10.62 ? 323  THR A CG2 1 
ATOM   2604 N N   . ASP A 1 324 ? 50.831 41.118 -30.941 1.00 12.50 ? 324  ASP A N   1 
ATOM   2605 C CA  . ASP A 1 324 ? 52.180 41.552 -31.312 1.00 11.44 ? 324  ASP A CA  1 
ATOM   2606 C C   . ASP A 1 324 ? 53.050 40.386 -31.756 1.00 11.72 ? 324  ASP A C   1 
ATOM   2607 O O   . ASP A 1 324 ? 54.011 40.589 -32.504 1.00 13.14 ? 324  ASP A O   1 
ATOM   2608 C CB  . ASP A 1 324 ? 52.884 42.255 -30.145 1.00 8.91  ? 324  ASP A CB  1 
ATOM   2609 C CG  . ASP A 1 324 ? 52.375 43.678 -29.877 1.00 11.15 ? 324  ASP A CG  1 
ATOM   2610 O OD1 . ASP A 1 324 ? 51.391 44.138 -30.495 1.00 11.40 ? 324  ASP A OD1 1 
ATOM   2611 O OD2 . ASP A 1 324 ? 52.985 44.337 -29.023 1.00 12.55 ? 324  ASP A OD2 1 
ATOM   2612 N N   . ASN A 1 325 ? 52.781 39.173 -31.272 1.00 10.90 ? 325  ASN A N   1 
ATOM   2613 C CA  . ASN A 1 325 ? 53.554 38.014 -31.706 1.00 13.12 ? 325  ASN A CA  1 
ATOM   2614 C C   . ASN A 1 325 ? 52.747 37.115 -32.635 1.00 12.99 ? 325  ASN A C   1 
ATOM   2615 O O   . ASN A 1 325 ? 53.106 35.952 -32.841 1.00 13.10 ? 325  ASN A O   1 
ATOM   2616 C CB  . ASN A 1 325 ? 54.111 37.235 -30.497 1.00 11.55 ? 325  ASN A CB  1 
ATOM   2617 C CG  . ASN A 1 325 ? 53.032 36.595 -29.629 1.00 12.13 ? 325  ASN A CG  1 
ATOM   2618 O OD1 . ASN A 1 325 ? 51.833 36.784 -29.847 1.00 10.63 ? 325  ASN A OD1 1 
ATOM   2619 N ND2 . ASN A 1 325 ? 53.467 35.842 -28.606 1.00 12.36 ? 325  ASN A ND2 1 
ATOM   2620 N N   . GLY A 1 326 ? 51.663 37.633 -33.205 1.00 12.81 ? 326  GLY A N   1 
ATOM   2621 C CA  . GLY A 1 326 ? 50.897 36.873 -34.179 1.00 13.37 ? 326  GLY A CA  1 
ATOM   2622 C C   . GLY A 1 326 ? 50.047 35.743 -33.634 1.00 15.87 ? 326  GLY A C   1 
ATOM   2623 O O   . GLY A 1 326 ? 49.722 34.816 -34.383 1.00 15.02 ? 326  GLY A O   1 
ATOM   2624 N N   . TRP A 1 327 ? 49.661 35.778 -32.361 1.00 10.92 ? 327  TRP A N   1 
ATOM   2625 C CA  . TRP A 1 327 ? 48.802 34.734 -31.812 1.00 9.61  ? 327  TRP A CA  1 
ATOM   2626 C C   . TRP A 1 327 ? 47.352 35.193 -31.835 1.00 13.30 ? 327  TRP A C   1 
ATOM   2627 O O   . TRP A 1 327 ? 47.027 36.287 -31.354 1.00 11.70 ? 327  TRP A O   1 
ATOM   2628 C CB  . TRP A 1 327 ? 49.209 34.349 -30.391 1.00 11.76 ? 327  TRP A CB  1 
ATOM   2629 C CG  . TRP A 1 327 ? 50.585 33.743 -30.297 1.00 11.80 ? 327  TRP A CG  1 
ATOM   2630 C CD1 . TRP A 1 327 ? 51.403 33.380 -31.337 1.00 11.94 ? 327  TRP A CD1 1 
ATOM   2631 C CD2 . TRP A 1 327 ? 51.300 33.432 -29.095 1.00 9.83  ? 327  TRP A CD2 1 
ATOM   2632 N NE1 . TRP A 1 327 ? 52.584 32.874 -30.853 1.00 12.54 ? 327  TRP A NE1 1 
ATOM   2633 C CE2 . TRP A 1 327 ? 52.547 32.890 -29.480 1.00 16.70 ? 327  TRP A CE2 1 
ATOM   2634 C CE3 . TRP A 1 327 ? 51.013 33.570 -27.732 1.00 9.95  ? 327  TRP A CE3 1 
ATOM   2635 C CZ2 . TRP A 1 327 ? 53.506 32.481 -28.548 1.00 14.53 ? 327  TRP A CZ2 1 
ATOM   2636 C CZ3 . TRP A 1 327 ? 51.969 33.162 -26.801 1.00 13.58 ? 327  TRP A CZ3 1 
ATOM   2637 C CH2 . TRP A 1 327 ? 53.203 32.627 -27.216 1.00 13.65 ? 327  TRP A CH2 1 
ATOM   2638 N N   . GLU A 1 328 ? 46.494 34.349 -32.393 1.00 11.98 ? 328  GLU A N   1 
ATOM   2639 C CA  . GLU A 1 328 ? 45.077 34.641 -32.521 1.00 13.91 ? 328  GLU A CA  1 
ATOM   2640 C C   . GLU A 1 328 ? 44.400 34.693 -31.157 1.00 12.75 ? 328  GLU A C   1 
ATOM   2641 O O   . GLU A 1 328 ? 44.672 33.869 -30.279 1.00 12.74 ? 328  GLU A O   1 
ATOM   2642 C CB  . GLU A 1 328 ? 44.423 33.563 -33.391 1.00 11.72 ? 328  GLU A CB  1 
ATOM   2643 C CG  . GLU A 1 328 ? 42.968 33.792 -33.745 1.00 11.79 ? 328  GLU A CG  1 
ATOM   2644 C CD  . GLU A 1 328 ? 42.383 32.592 -34.493 1.00 15.21 ? 328  GLU A CD  1 
ATOM   2645 O OE1 . GLU A 1 328 ? 42.922 31.468 -34.345 1.00 14.51 ? 328  GLU A OE1 1 
ATOM   2646 O OE2 . GLU A 1 328 ? 41.411 32.775 -35.249 1.00 16.89 ? 328  GLU A OE2 1 
ATOM   2647 N N   . ILE A 1 329 ? 43.504 35.659 -30.982 1.00 10.20 ? 329  ILE A N   1 
ATOM   2648 C CA  . ILE A 1 329 ? 42.672 35.711 -29.784 1.00 12.83 ? 329  ILE A CA  1 
ATOM   2649 C C   . ILE A 1 329 ? 41.488 34.771 -29.992 1.00 12.29 ? 329  ILE A C   1 
ATOM   2650 O O   . ILE A 1 329 ? 40.625 35.016 -30.841 1.00 12.02 ? 329  ILE A O   1 
ATOM   2651 C CB  . ILE A 1 329 ? 42.207 37.138 -29.464 1.00 14.18 ? 329  ILE A CB  1 
ATOM   2652 C CG1 . ILE A 1 329 ? 43.404 38.085 -29.335 1.00 13.86 ? 329  ILE A CG1 1 
ATOM   2653 C CG2 . ILE A 1 329 ? 41.414 37.160 -28.139 1.00 9.89  ? 329  ILE A CG2 1 
ATOM   2654 C CD1 . ILE A 1 329 ? 43.001 39.585 -29.233 1.00 11.36 ? 329  ILE A CD1 1 
ATOM   2655 N N   . TYR A 1 330 ? 41.454 33.682 -29.221 1.00 11.09 ? 330  TYR A N   1 
ATOM   2656 C CA  . TYR A 1 330 ? 40.443 32.629 -29.358 1.00 9.08  ? 330  TYR A CA  1 
ATOM   2657 C C   . TYR A 1 330 ? 39.993 32.218 -27.960 1.00 12.53 ? 330  TYR A C   1 
ATOM   2658 O O   . TYR A 1 330 ? 40.348 31.145 -27.454 1.00 10.39 ? 330  TYR A O   1 
ATOM   2659 C CB  . TYR A 1 330 ? 41.002 31.434 -30.136 1.00 11.80 ? 330  TYR A CB  1 
ATOM   2660 C CG  . TYR A 1 330 ? 39.943 30.437 -30.556 1.00 13.48 ? 330  TYR A CG  1 
ATOM   2661 C CD1 . TYR A 1 330 ? 39.023 30.746 -31.563 1.00 12.08 ? 330  TYR A CD1 1 
ATOM   2662 C CD2 . TYR A 1 330 ? 39.847 29.200 -29.934 1.00 9.15  ? 330  TYR A CD2 1 
ATOM   2663 C CE1 . TYR A 1 330 ? 38.039 29.830 -31.942 1.00 15.08 ? 330  TYR A CE1 1 
ATOM   2664 C CE2 . TYR A 1 330 ? 38.881 28.279 -30.303 1.00 12.66 ? 330  TYR A CE2 1 
ATOM   2665 C CZ  . TYR A 1 330 ? 37.977 28.596 -31.308 1.00 16.77 ? 330  TYR A CZ  1 
ATOM   2666 O OH  . TYR A 1 330 ? 37.018 27.674 -31.667 1.00 13.85 ? 330  TYR A OH  1 
ATOM   2667 N N   . PRO A 1 331 ? 39.216 33.069 -27.294 1.00 12.37 ? 331  PRO A N   1 
ATOM   2668 C CA  . PRO A 1 331 ? 38.886 32.798 -25.885 1.00 12.80 ? 331  PRO A CA  1 
ATOM   2669 C C   . PRO A 1 331 ? 38.101 31.505 -25.675 1.00 14.12 ? 331  PRO A C   1 
ATOM   2670 O O   . PRO A 1 331 ? 38.288 30.869 -24.633 1.00 10.42 ? 331  PRO A O   1 
ATOM   2671 C CB  . PRO A 1 331 ? 38.076 34.034 -25.458 1.00 9.96  ? 331  PRO A CB  1 
ATOM   2672 C CG  . PRO A 1 331 ? 38.270 35.057 -26.549 1.00 12.60 ? 331  PRO A CG  1 
ATOM   2673 C CD  . PRO A 1 331 ? 38.609 34.311 -27.800 1.00 13.97 ? 331  PRO A CD  1 
ATOM   2674 N N   . GLU A 1 332 ? 37.257 31.082 -26.627 1.00 11.85 ? 332  GLU A N   1 
ATOM   2675 C CA  . GLU A 1 332 ? 36.464 29.866 -26.427 1.00 14.45 ? 332  GLU A CA  1 
ATOM   2676 C C   . GLU A 1 332 ? 37.349 28.642 -26.217 1.00 13.32 ? 332  GLU A C   1 
ATOM   2677 O O   . GLU A 1 332 ? 36.943 27.690 -25.544 1.00 10.64 ? 332  GLU A O   1 
ATOM   2678 C CB  . GLU A 1 332 ? 35.533 29.614 -27.625 1.00 15.89 ? 332  GLU A CB  1 
ATOM   2679 C CG  . GLU A 1 332 ? 34.603 30.770 -27.881 1.00 25.03 ? 332  GLU A CG  1 
ATOM   2680 C CD  . GLU A 1 332 ? 35.123 31.666 -28.993 1.00 27.42 ? 332  GLU A CD  1 
ATOM   2681 O OE1 . GLU A 1 332 ? 34.475 31.738 -30.057 1.00 31.44 ? 332  GLU A OE1 1 
ATOM   2682 O OE2 . GLU A 1 332 ? 36.232 32.222 -28.835 1.00 16.50 ? 332  GLU A OE2 1 
ATOM   2683 N N   . GLY A 1 333 ? 38.550 28.640 -26.797 1.00 11.33 ? 333  GLY A N   1 
ATOM   2684 C CA  . GLY A 1 333 ? 39.433 27.499 -26.635 1.00 12.29 ? 333  GLY A CA  1 
ATOM   2685 C C   . GLY A 1 333 ? 39.812 27.246 -25.192 1.00 11.86 ? 333  GLY A C   1 
ATOM   2686 O O   . GLY A 1 333 ? 40.053 26.100 -24.799 1.00 10.18 ? 333  GLY A O   1 
ATOM   2687 N N   . LEU A 1 334 ? 39.878 28.302 -24.382 1.00 8.62  ? 334  LEU A N   1 
ATOM   2688 C CA  . LEU A 1 334 ? 40.186 28.091 -22.972 1.00 10.40 ? 334  LEU A CA  1 
ATOM   2689 C C   . LEU A 1 334 ? 39.095 27.257 -22.298 1.00 12.51 ? 334  LEU A C   1 
ATOM   2690 O O   . LEU A 1 334 ? 39.393 26.336 -21.525 1.00 9.97  ? 334  LEU A O   1 
ATOM   2691 C CB  . LEU A 1 334 ? 40.370 29.430 -22.264 1.00 7.97  ? 334  LEU A CB  1 
ATOM   2692 C CG  . LEU A 1 334 ? 40.490 29.389 -20.733 1.00 12.74 ? 334  LEU A CG  1 
ATOM   2693 C CD1 . LEU A 1 334 ? 41.740 28.627 -20.309 1.00 10.90 ? 334  LEU A CD1 1 
ATOM   2694 C CD2 . LEU A 1 334 ? 40.473 30.801 -20.115 1.00 10.49 ? 334  LEU A CD2 1 
ATOM   2695 N N   . GLY A 1 335 ? 37.828 27.546 -22.603 1.00 12.01 ? 335  GLY A N   1 
ATOM   2696 C CA  . GLY A 1 335 ? 36.744 26.741 -22.057 1.00 10.90 ? 335  GLY A CA  1 
ATOM   2697 C C   . GLY A 1 335 ? 36.740 25.318 -22.587 1.00 13.36 ? 335  GLY A C   1 
ATOM   2698 O O   . GLY A 1 335 ? 36.468 24.376 -21.841 1.00 11.83 ? 335  GLY A O   1 
ATOM   2699 N N   . TYR A 1 336 ? 37.037 25.142 -23.880 1.00 10.87 ? 336  TYR A N   1 
ATOM   2700 C CA  . TYR A 1 336 ? 37.111 23.794 -24.444 1.00 13.59 ? 336  TYR A CA  1 
ATOM   2701 C C   . TYR A 1 336 ? 38.211 22.968 -23.787 1.00 14.64 ? 336  TYR A C   1 
ATOM   2702 O O   . TYR A 1 336 ? 37.999 21.797 -23.455 1.00 13.34 ? 336  TYR A O   1 
ATOM   2703 C CB  . TYR A 1 336 ? 37.340 23.857 -25.953 1.00 13.87 ? 336  TYR A CB  1 
ATOM   2704 C CG  . TYR A 1 336 ? 36.305 24.636 -26.724 1.00 14.87 ? 336  TYR A CG  1 
ATOM   2705 C CD1 . TYR A 1 336 ? 34.981 24.677 -26.312 1.00 17.99 ? 336  TYR A CD1 1 
ATOM   2706 C CD2 . TYR A 1 336 ? 36.660 25.333 -27.876 1.00 15.18 ? 336  TYR A CD2 1 
ATOM   2707 C CE1 . TYR A 1 336 ? 34.032 25.394 -27.032 1.00 21.57 ? 336  TYR A CE1 1 
ATOM   2708 C CE2 . TYR A 1 336 ? 35.729 26.036 -28.599 1.00 16.50 ? 336  TYR A CE2 1 
ATOM   2709 C CZ  . TYR A 1 336 ? 34.421 26.072 -28.174 1.00 19.29 ? 336  TYR A CZ  1 
ATOM   2710 O OH  . TYR A 1 336 ? 33.512 26.805 -28.899 1.00 20.34 ? 336  TYR A OH  1 
ATOM   2711 N N   . VAL A 1 337 ? 39.396 23.556 -23.602 1.00 11.05 ? 337  VAL A N   1 
ATOM   2712 C CA  . VAL A 1 337 ? 40.497 22.843 -22.949 1.00 12.98 ? 337  VAL A CA  1 
ATOM   2713 C C   . VAL A 1 337 ? 40.118 22.458 -21.523 1.00 12.66 ? 337  VAL A C   1 
ATOM   2714 O O   . VAL A 1 337 ? 40.356 21.326 -21.083 1.00 11.59 ? 337  VAL A O   1 
ATOM   2715 C CB  . VAL A 1 337 ? 41.776 23.703 -22.959 1.00 15.86 ? 337  VAL A CB  1 
ATOM   2716 C CG1 . VAL A 1 337 ? 42.678 23.320 -21.780 1.00 19.26 ? 337  VAL A CG1 1 
ATOM   2717 C CG2 . VAL A 1 337 ? 42.518 23.517 -24.240 1.00 17.62 ? 337  VAL A CG2 1 
ATOM   2718 N N   . LEU A 1 338 ? 39.553 23.408 -20.767 1.00 10.67 ? 338  LEU A N   1 
ATOM   2719 C CA  . LEU A 1 338 ? 39.218 23.132 -19.371 1.00 12.67 ? 338  LEU A CA  1 
ATOM   2720 C C   . LEU A 1 338 ? 38.152 22.050 -19.265 1.00 14.07 ? 338  LEU A C   1 
ATOM   2721 O O   . LEU A 1 338 ? 38.192 21.222 -18.347 1.00 13.05 ? 338  LEU A O   1 
ATOM   2722 C CB  . LEU A 1 338 ? 38.751 24.407 -18.660 1.00 9.36  ? 338  LEU A CB  1 
ATOM   2723 C CG  . LEU A 1 338 ? 39.808 25.478 -18.353 1.00 13.96 ? 338  LEU A CG  1 
ATOM   2724 C CD1 . LEU A 1 338 ? 39.152 26.793 -17.958 1.00 12.46 ? 338  LEU A CD1 1 
ATOM   2725 C CD2 . LEU A 1 338 ? 40.745 25.005 -17.249 1.00 10.84 ? 338  LEU A CD2 1 
ATOM   2726 N N   . ARG A 1 339 ? 37.172 22.061 -20.175 1.00 12.80 ? 339  ARG A N   1 
ATOM   2727 C CA  . ARG A 1 339 ? 36.144 21.024 -20.153 1.00 14.69 ? 339  ARG A CA  1 
ATOM   2728 C C   . ARG A 1 339 ? 36.726 19.663 -20.530 1.00 17.97 ? 339  ARG A C   1 
ATOM   2729 O O   . ARG A 1 339 ? 36.322 18.634 -19.974 1.00 15.05 ? 339  ARG A O   1 
ATOM   2730 C CB  . ARG A 1 339 ? 34.994 21.407 -21.087 1.00 15.49 ? 339  ARG A CB  1 
ATOM   2731 C CG  . ARG A 1 339 ? 34.069 22.474 -20.512 1.00 16.84 ? 339  ARG A CG  1 
ATOM   2732 C CD  . ARG A 1 339 ? 33.173 23.130 -21.573 1.00 25.00 ? 339  ARG A CD  1 
ATOM   2733 N NE  . ARG A 1 339 ? 32.686 24.415 -21.084 1.00 22.48 ? 339  ARG A NE  1 
ATOM   2734 C CZ  . ARG A 1 339 ? 32.801 25.565 -21.735 1.00 25.60 ? 339  ARG A CZ  1 
ATOM   2735 N NH1 . ARG A 1 339 ? 33.269 25.617 -22.975 1.00 23.90 ? 339  ARG A NH1 1 
ATOM   2736 N NH2 . ARG A 1 339 ? 32.453 26.694 -21.121 1.00 23.99 ? 339  ARG A NH2 1 
ATOM   2737 N N   . SER A 1 340 ? 37.685 19.635 -21.467 1.00 14.51 ? 340  SER A N   1 
ATOM   2738 C CA  . SER A 1 340 ? 38.382 18.382 -21.766 1.00 16.91 ? 340  SER A CA  1 
ATOM   2739 C C   . SER A 1 340 ? 39.142 17.867 -20.553 1.00 16.83 ? 340  SER A C   1 
ATOM   2740 O O   . SER A 1 340 ? 39.130 16.661 -20.271 1.00 15.32 ? 340  SER A O   1 
ATOM   2741 C CB  . SER A 1 340 ? 39.345 18.555 -22.938 1.00 16.44 ? 340  SER A CB  1 
ATOM   2742 O OG  . SER A 1 340 ? 38.646 18.778 -24.140 1.00 22.78 ? 340  SER A OG  1 
ATOM   2743 N N   . CYS A 1 341 ? 39.821 18.761 -19.826 1.00 13.76 ? 341  CYS A N   1 
ATOM   2744 C CA  . CYS A 1 341 ? 40.531 18.322 -18.630 1.00 15.19 ? 341  CYS A CA  1 
ATOM   2745 C C   . CYS A 1 341 ? 39.558 17.813 -17.577 1.00 19.02 ? 341  CYS A C   1 
ATOM   2746 O O   . CYS A 1 341 ? 39.830 16.809 -16.898 1.00 15.81 ? 341  CYS A O   1 
ATOM   2747 C CB  . CYS A 1 341 ? 41.381 19.462 -18.066 1.00 14.93 ? 341  CYS A CB  1 
ATOM   2748 S SG  . CYS A 1 341 ? 42.797 19.874 -19.102 1.00 14.98 ? 341  CYS A SG  1 
ATOM   2749 N N   . ARG A 1 342 ? 38.418 18.494 -17.424 1.00 14.56 ? 342  ARG A N   1 
ATOM   2750 C CA  . ARG A 1 342 ? 37.419 18.036 -16.461 1.00 19.43 ? 342  ARG A CA  1 
ATOM   2751 C C   . ARG A 1 342 ? 36.876 16.664 -16.849 1.00 18.99 ? 342  ARG A C   1 
ATOM   2752 O O   . ARG A 1 342 ? 36.737 15.780 -15.995 1.00 21.85 ? 342  ARG A O   1 
ATOM   2753 C CB  . ARG A 1 342 ? 36.277 19.048 -16.350 1.00 18.40 ? 342  ARG A CB  1 
ATOM   2754 C CG  . ARG A 1 342 ? 35.012 18.480 -15.702 1.00 17.47 ? 342  ARG A CG  1 
ATOM   2755 C CD  . ARG A 1 342 ? 33.902 19.522 -15.577 1.00 21.77 ? 342  ARG A CD  1 
ATOM   2756 N NE  . ARG A 1 342 ? 32.933 19.163 -14.544 1.00 29.18 ? 342  ARG A NE  1 
ATOM   2757 C CZ  . ARG A 1 342 ? 31.861 19.883 -14.229 1.00 29.63 ? 342  ARG A CZ  1 
ATOM   2758 N NH1 . ARG A 1 342 ? 31.575 21.015 -14.854 1.00 22.26 ? 342  ARG A NH1 1 
ATOM   2759 N NH2 . ARG A 1 342 ? 31.051 19.451 -13.268 1.00 29.09 ? 342  ARG A NH2 1 
ATOM   2760 N N   . ASP A 1 343 ? 36.579 16.466 -18.136 1.00 20.11 ? 343  ASP A N   1 
ATOM   2761 C CA  . ASP A 1 343 ? 36.049 15.183 -18.592 1.00 18.84 ? 343  ASP A CA  1 
ATOM   2762 C C   . ASP A 1 343 ? 37.065 14.054 -18.425 1.00 19.67 ? 343  ASP A C   1 
ATOM   2763 O O   . ASP A 1 343 ? 36.692 12.926 -18.079 1.00 17.09 ? 343  ASP A O   1 
ATOM   2764 C CB  . ASP A 1 343 ? 35.608 15.284 -20.052 1.00 20.54 ? 343  ASP A CB  1 
ATOM   2765 C CG  . ASP A 1 343 ? 34.419 16.216 -20.256 1.00 32.79 ? 343  ASP A CG  1 
ATOM   2766 O OD1 . ASP A 1 343 ? 33.898 16.787 -19.263 1.00 36.79 ? 343  ASP A OD1 1 
ATOM   2767 O OD2 . ASP A 1 343 ? 34.012 16.385 -21.429 1.00 42.30 ? 343  ASP A OD2 1 
ATOM   2768 N N   . ARG A 1 344 ? 38.351 14.324 -18.672 1.00 17.29 ? 344  ARG A N   1 
ATOM   2769 C CA  . ARG A 1 344 ? 39.340 13.249 -18.626 1.00 14.17 ? 344  ARG A CA  1 
ATOM   2770 C C   . ARG A 1 344 ? 39.834 12.942 -17.221 1.00 20.03 ? 344  ARG A C   1 
ATOM   2771 O O   . ARG A 1 344 ? 40.208 11.797 -16.938 1.00 15.66 ? 344  ARG A O   1 
ATOM   2772 C CB  . ARG A 1 344 ? 40.547 13.585 -19.499 1.00 17.68 ? 344  ARG A CB  1 
ATOM   2773 C CG  . ARG A 1 344 ? 40.283 13.412 -20.959 1.00 19.80 ? 344  ARG A CG  1 
ATOM   2774 C CD  . ARG A 1 344 ? 41.392 13.994 -21.827 1.00 22.72 ? 344  ARG A CD  1 
ATOM   2775 N NE  . ARG A 1 344 ? 41.549 13.168 -23.019 1.00 31.84 ? 344  ARG A NE  1 
ATOM   2776 C CZ  . ARG A 1 344 ? 42.210 12.016 -23.031 1.00 24.60 ? 344  ARG A CZ  1 
ATOM   2777 N NH1 . ARG A 1 344 ? 42.873 11.586 -21.964 1.00 31.17 ? 344  ARG A NH1 1 
ATOM   2778 N NH2 . ARG A 1 344 ? 42.210 11.282 -24.134 1.00 31.09 ? 344  ARG A NH2 1 
ATOM   2779 N N   . TYR A 1 345 ? 39.888 13.938 -16.348 1.00 16.40 ? 345  TYR A N   1 
ATOM   2780 C CA  . TYR A 1 345 ? 40.597 13.822 -15.088 1.00 18.06 ? 345  TYR A CA  1 
ATOM   2781 C C   . TYR A 1 345 ? 39.707 14.328 -13.966 1.00 22.23 ? 345  TYR A C   1 
ATOM   2782 O O   . TYR A 1 345 ? 38.926 15.265 -14.154 1.00 24.05 ? 345  TYR A O   1 
ATOM   2783 C CB  . TYR A 1 345 ? 41.917 14.620 -15.128 1.00 16.96 ? 345  TYR A CB  1 
ATOM   2784 C CG  . TYR A 1 345 ? 42.810 14.314 -16.323 1.00 15.36 ? 345  TYR A CG  1 
ATOM   2785 C CD1 . TYR A 1 345 ? 43.285 13.028 -16.561 1.00 15.61 ? 345  TYR A CD1 1 
ATOM   2786 C CD2 . TYR A 1 345 ? 43.177 15.321 -17.215 1.00 17.32 ? 345  TYR A CD2 1 
ATOM   2787 C CE1 . TYR A 1 345 ? 44.115 12.753 -17.655 1.00 16.64 ? 345  TYR A CE1 1 
ATOM   2788 C CE2 . TYR A 1 345 ? 44.001 15.060 -18.304 1.00 13.49 ? 345  TYR A CE2 1 
ATOM   2789 C CZ  . TYR A 1 345 ? 44.459 13.778 -18.522 1.00 15.77 ? 345  TYR A CZ  1 
ATOM   2790 O OH  . TYR A 1 345 ? 45.270 13.520 -19.597 1.00 14.37 ? 345  TYR A OH  1 
ATOM   2791 N N   . LYS A 1 346 ? 39.804 13.695 -12.808 1.00 21.22 ? 346  LYS A N   1 
ATOM   2792 C CA  . LYS A 1 346 ? 39.079 14.147 -11.621 1.00 27.83 ? 346  LYS A CA  1 
ATOM   2793 C C   . LYS A 1 346 ? 40.102 14.915 -10.788 1.00 23.00 ? 346  LYS A C   1 
ATOM   2794 O O   . LYS A 1 346 ? 40.775 14.356 -9.926  1.00 29.79 ? 346  LYS A O   1 
ATOM   2795 C CB  . LYS A 1 346 ? 38.460 12.961 -10.879 1.00 28.10 ? 346  LYS A CB  1 
ATOM   2796 C CG  . LYS A 1 346 ? 37.776 13.312 -9.550  1.00 36.62 ? 346  LYS A CG  1 
ATOM   2797 C CD  . LYS A 1 346 ? 36.489 14.115 -9.758  1.00 39.10 ? 346  LYS A CD  1 
ATOM   2798 C CE  . LYS A 1 346 ? 36.085 14.859 -8.483  1.00 42.28 ? 346  LYS A CE  1 
ATOM   2799 N NZ  . LYS A 1 346 ? 35.516 16.221 -8.773  1.00 46.90 ? 346  LYS A NZ  1 
ATOM   2800 N N   . LYS A 1 347 ? 40.256 16.200 -11.086 1.00 21.72 ? 347  LYS A N   1 
ATOM   2801 C CA  . LYS A 1 347 ? 41.366 16.943 -10.500 1.00 18.62 ? 347  LYS A CA  1 
ATOM   2802 C C   . LYS A 1 347 ? 41.065 18.437 -10.467 1.00 15.36 ? 347  LYS A C   1 
ATOM   2803 O O   . LYS A 1 347 ? 40.585 18.989 -11.460 1.00 14.13 ? 347  LYS A O   1 
ATOM   2804 C CB  . LYS A 1 347 ? 42.645 16.655 -11.293 1.00 19.12 ? 347  LYS A CB  1 
ATOM   2805 C CG  . LYS A 1 347 ? 43.923 17.020 -10.576 1.00 17.56 ? 347  LYS A CG  1 
ATOM   2806 C CD  . LYS A 1 347 ? 44.176 16.114 -9.358  1.00 21.29 ? 347  LYS A CD  1 
ATOM   2807 C CE  . LYS A 1 347 ? 44.336 14.647 -9.740  1.00 23.56 ? 347  LYS A CE  1 
ATOM   2808 N NZ  . LYS A 1 347 ? 44.967 13.890 -8.605  1.00 25.55 ? 347  LYS A NZ  1 
ATOM   2809 N N   . PRO A 1 348 ? 41.317 19.122 -9.355  1.00 14.59 ? 348  PRO A N   1 
ATOM   2810 C CA  . PRO A 1 348 ? 41.120 20.577 -9.331  1.00 16.23 ? 348  PRO A CA  1 
ATOM   2811 C C   . PRO A 1 348 ? 41.984 21.269 -10.380 1.00 14.83 ? 348  PRO A C   1 
ATOM   2812 O O   . PRO A 1 348 ? 43.131 20.879 -10.628 1.00 10.38 ? 348  PRO A O   1 
ATOM   2813 C CB  . PRO A 1 348 ? 41.525 20.976 -7.904  1.00 15.56 ? 348  PRO A CB  1 
ATOM   2814 C CG  . PRO A 1 348 ? 41.461 19.692 -7.103  1.00 17.05 ? 348  PRO A CG  1 
ATOM   2815 C CD  . PRO A 1 348 ? 41.802 18.595 -8.063  1.00 18.81 ? 348  PRO A CD  1 
ATOM   2816 N N   . LEU A 1 349 ? 41.397 22.280 -11.020 1.00 11.63 ? 349  LEU A N   1 
ATOM   2817 C CA  . LEU A 1 349 ? 42.002 23.031 -12.111 1.00 12.02 ? 349  LEU A CA  1 
ATOM   2818 C C   . LEU A 1 349 ? 42.227 24.485 -11.709 1.00 12.87 ? 349  LEU A C   1 
ATOM   2819 O O   . LEU A 1 349 ? 41.433 25.071 -10.962 1.00 12.25 ? 349  LEU A O   1 
ATOM   2820 C CB  . LEU A 1 349 ? 41.101 22.997 -13.351 1.00 11.63 ? 349  LEU A CB  1 
ATOM   2821 C CG  . LEU A 1 349 ? 40.734 21.606 -13.862 1.00 13.18 ? 349  LEU A CG  1 
ATOM   2822 C CD1 . LEU A 1 349 ? 39.679 21.691 -14.959 1.00 12.48 ? 349  LEU A CD1 1 
ATOM   2823 C CD2 . LEU A 1 349 ? 41.997 20.947 -14.382 1.00 14.50 ? 349  LEU A CD2 1 
ATOM   2824 N N   . TYR A 1 350 ? 43.327 25.054 -12.211 1.00 12.64 ? 350  TYR A N   1 
ATOM   2825 C CA  . TYR A 1 350 ? 43.621 26.484 -12.172 1.00 10.70 ? 350  TYR A CA  1 
ATOM   2826 C C   . TYR A 1 350 ? 44.030 26.900 -13.579 1.00 10.38 ? 350  TYR A C   1 
ATOM   2827 O O   . TYR A 1 350 ? 44.714 26.141 -14.271 1.00 11.63 ? 350  TYR A O   1 
ATOM   2828 C CB  . TYR A 1 350 ? 44.788 26.830 -11.220 1.00 10.43 ? 350  TYR A CB  1 
ATOM   2829 C CG  . TYR A 1 350 ? 44.518 26.565 -9.757  1.00 12.63 ? 350  TYR A CG  1 
ATOM   2830 C CD1 . TYR A 1 350 ? 44.616 25.276 -9.233  1.00 12.57 ? 350  TYR A CD1 1 
ATOM   2831 C CD2 . TYR A 1 350 ? 44.162 27.600 -8.901  1.00 11.06 ? 350  TYR A CD2 1 
ATOM   2832 C CE1 . TYR A 1 350 ? 44.354 25.025 -7.884  1.00 16.46 ? 350  TYR A CE1 1 
ATOM   2833 C CE2 . TYR A 1 350 ? 43.912 27.362 -7.544  1.00 18.86 ? 350  TYR A CE2 1 
ATOM   2834 C CZ  . TYR A 1 350 ? 44.007 26.073 -7.050  1.00 19.32 ? 350  TYR A CZ  1 
ATOM   2835 O OH  . TYR A 1 350 ? 43.757 25.826 -5.719  1.00 16.61 ? 350  TYR A OH  1 
ATOM   2836 N N   . VAL A 1 351 ? 43.648 28.102 -13.999 1.00 8.45  ? 351  VAL A N   1 
ATOM   2837 C CA  . VAL A 1 351 ? 44.305 28.706 -15.154 1.00 10.84 ? 351  VAL A CA  1 
ATOM   2838 C C   . VAL A 1 351 ? 45.567 29.370 -14.615 1.00 8.16  ? 351  VAL A C   1 
ATOM   2839 O O   . VAL A 1 351 ? 45.483 30.349 -13.876 1.00 9.32  ? 351  VAL A O   1 
ATOM   2840 C CB  . VAL A 1 351 ? 43.402 29.711 -15.879 1.00 12.07 ? 351  VAL A CB  1 
ATOM   2841 C CG1 . VAL A 1 351 ? 44.162 30.332 -17.069 1.00 8.38  ? 351  VAL A CG1 1 
ATOM   2842 C CG2 . VAL A 1 351 ? 42.123 29.039 -16.364 1.00 9.35  ? 351  VAL A CG2 1 
ATOM   2843 N N   . THR A 1 352 ? 46.735 28.809 -14.930 1.00 9.03  ? 352  THR A N   1 
ATOM   2844 C CA  . THR A 1 352 ? 47.976 29.312 -14.363 1.00 9.31  ? 352  THR A CA  1 
ATOM   2845 C C   . THR A 1 352 ? 48.699 30.309 -15.273 1.00 9.43  ? 352  THR A C   1 
ATOM   2846 O O   . THR A 1 352 ? 49.592 31.016 -14.796 1.00 9.76  ? 352  THR A O   1 
ATOM   2847 C CB  . THR A 1 352 ? 48.892 28.130 -14.002 1.00 9.68  ? 352  THR A CB  1 
ATOM   2848 O OG1 . THR A 1 352 ? 48.799 27.125 -15.015 1.00 10.08 ? 352  THR A OG1 1 
ATOM   2849 C CG2 . THR A 1 352 ? 48.440 27.540 -12.671 1.00 7.06  ? 352  THR A CG2 1 
ATOM   2850 N N   . GLU A 1 353 ? 48.310 30.389 -16.549 1.00 7.35  ? 353  GLU A N   1 
ATOM   2851 C CA  . GLU A 1 353 ? 48.773 31.386 -17.518 1.00 9.94  ? 353  GLU A CA  1 
ATOM   2852 C C   . GLU A 1 353 ? 47.731 31.642 -18.591 1.00 8.70  ? 353  GLU A C   1 
ATOM   2853 O O   . GLU A 1 353 ? 47.119 30.711 -19.119 1.00 8.71  ? 353  GLU A O   1 
ATOM   2854 C CB  . GLU A 1 353 ? 50.090 31.010 -18.224 1.00 9.37  ? 353  GLU A CB  1 
ATOM   2855 C CG  . GLU A 1 353 ? 51.279 30.813 -17.330 1.00 7.79  ? 353  GLU A CG  1 
ATOM   2856 C CD  . GLU A 1 353 ? 52.577 30.690 -18.105 1.00 11.73 ? 353  GLU A CD  1 
ATOM   2857 O OE1 . GLU A 1 353 ? 52.632 31.101 -19.287 1.00 10.91 ? 353  GLU A OE1 1 
ATOM   2858 O OE2 . GLU A 1 353 ? 53.582 30.283 -17.486 1.00 13.37 ? 353  GLU A OE2 1 
ATOM   2859 N N   . ASN A 1 354 ? 47.584 32.927 -18.930 1.00 10.16 ? 354  ASN A N   1 
ATOM   2860 C CA  . ASN A 1 354 ? 46.806 33.395 -20.066 1.00 10.68 ? 354  ASN A CA  1 
ATOM   2861 C C   . ASN A 1 354 ? 47.163 34.862 -20.263 1.00 10.59 ? 354  ASN A C   1 
ATOM   2862 O O   . ASN A 1 354 ? 47.229 35.613 -19.281 1.00 8.99  ? 354  ASN A O   1 
ATOM   2863 C CB  . ASN A 1 354 ? 45.309 33.210 -19.815 1.00 8.61  ? 354  ASN A CB  1 
ATOM   2864 C CG  . ASN A 1 354 ? 44.465 33.829 -20.899 1.00 11.14 ? 354  ASN A CG  1 
ATOM   2865 O OD1 . ASN A 1 354 ? 44.508 33.402 -22.071 1.00 11.74 ? 354  ASN A OD1 1 
ATOM   2866 N ND2 . ASN A 1 354 ? 43.707 34.844 -20.537 1.00 7.09  ? 354  ASN A ND2 1 
ATOM   2867 N N   . GLY A 1 355 ? 47.462 35.267 -21.490 1.00 8.94  ? 355  GLY A N   1 
ATOM   2868 C CA  . GLY A 1 355 ? 47.820 36.653 -21.734 1.00 9.98  ? 355  GLY A CA  1 
ATOM   2869 C C   . GLY A 1 355 ? 48.106 36.893 -23.201 1.00 8.78  ? 355  GLY A C   1 
ATOM   2870 O O   . GLY A 1 355 ? 47.850 36.033 -24.047 1.00 8.31  ? 355  GLY A O   1 
ATOM   2871 N N   . VAL A 1 356 ? 48.624 38.094 -23.495 1.00 7.03  ? 356  VAL A N   1 
ATOM   2872 C CA  . VAL A 1 356 ? 48.868 38.555 -24.860 1.00 7.38  ? 356  VAL A CA  1 
ATOM   2873 C C   . VAL A 1 356 ? 50.126 39.415 -24.885 1.00 7.86  ? 356  VAL A C   1 
ATOM   2874 O O   . VAL A 1 356 ? 50.413 40.174 -23.946 1.00 8.17  ? 356  VAL A O   1 
ATOM   2875 C CB  . VAL A 1 356 ? 47.690 39.387 -25.444 1.00 9.52  ? 356  VAL A CB  1 
ATOM   2876 C CG1 . VAL A 1 356 ? 46.448 38.528 -25.686 1.00 10.88 ? 356  VAL A CG1 1 
ATOM   2877 C CG2 . VAL A 1 356 ? 47.363 40.590 -24.541 1.00 7.23  ? 356  VAL A CG2 1 
ATOM   2878 N N   . ALA A 1 357 ? 50.870 39.300 -25.987 1.00 8.56  ? 357  ALA A N   1 
ATOM   2879 C CA  . ALA A 1 357 ? 51.940 40.232 -26.319 1.00 8.76  ? 357  ALA A CA  1 
ATOM   2880 C C   . ALA A 1 357 ? 51.317 41.485 -26.921 1.00 9.88  ? 357  ALA A C   1 
ATOM   2881 O O   . ALA A 1 357 ? 50.686 41.422 -27.986 1.00 10.25 ? 357  ALA A O   1 
ATOM   2882 C CB  . ALA A 1 357 ? 52.921 39.598 -27.304 1.00 9.03  ? 357  ALA A CB  1 
ATOM   2883 N N   . ASP A 1 358 ? 51.503 42.620 -26.258 1.00 8.06  ? 358  ASP A N   1 
ATOM   2884 C CA  . ASP A 1 358 ? 50.684 43.789 -26.567 1.00 9.45  ? 358  ASP A CA  1 
ATOM   2885 C C   . ASP A 1 358 ? 51.212 45.027 -25.851 1.00 10.74 ? 358  ASP A C   1 
ATOM   2886 O O   . ASP A 1 358 ? 50.756 45.361 -24.751 1.00 10.05 ? 358  ASP A O   1 
ATOM   2887 C CB  . ASP A 1 358 ? 49.228 43.501 -26.172 1.00 9.22  ? 358  ASP A CB  1 
ATOM   2888 C CG  . ASP A 1 358 ? 48.288 44.677 -26.418 1.00 11.49 ? 358  ASP A CG  1 
ATOM   2889 O OD1 . ASP A 1 358 ? 48.613 45.582 -27.221 1.00 9.60  ? 358  ASP A OD1 1 
ATOM   2890 O OD2 . ASP A 1 358 ? 47.186 44.659 -25.824 1.00 9.70  ? 358  ASP A OD2 1 
ATOM   2891 N N   . ASP A 1 359 ? 52.170 45.721 -26.469 1.00 8.56  ? 359  ASP A N   1 
ATOM   2892 C CA  . ASP A 1 359 ? 52.773 46.882 -25.817 1.00 10.31 ? 359  ASP A CA  1 
ATOM   2893 C C   . ASP A 1 359 ? 51.780 48.043 -25.714 1.00 13.74 ? 359  ASP A C   1 
ATOM   2894 O O   . ASP A 1 359 ? 51.742 48.756 -24.699 1.00 9.64  ? 359  ASP A O   1 
ATOM   2895 C CB  . ASP A 1 359 ? 54.021 47.305 -26.590 1.00 9.95  ? 359  ASP A CB  1 
ATOM   2896 C CG  . ASP A 1 359 ? 54.852 48.346 -25.857 1.00 10.52 ? 359  ASP A CG  1 
ATOM   2897 O OD1 . ASP A 1 359 ? 54.607 48.621 -24.655 1.00 13.56 ? 359  ASP A OD1 1 
ATOM   2898 O OD2 . ASP A 1 359 ? 55.761 48.899 -26.501 1.00 10.25 ? 359  ASP A OD2 1 
ATOM   2899 N N   . ARG A 1 360 ? 50.969 48.245 -26.749 1.00 10.21 ? 360  ARG A N   1 
ATOM   2900 C CA  . ARG A 1 360 ? 50.047 49.373 -26.783 1.00 9.83  ? 360  ARG A CA  1 
ATOM   2901 C C   . ARG A 1 360 ? 48.768 49.142 -25.988 1.00 11.88 ? 360  ARG A C   1 
ATOM   2902 O O   . ARG A 1 360 ? 48.009 50.101 -25.807 1.00 11.34 ? 360  ARG A O   1 
ATOM   2903 C CB  . ARG A 1 360 ? 49.675 49.735 -28.233 1.00 10.36 ? 360  ARG A CB  1 
ATOM   2904 C CG  . ARG A 1 360 ? 50.831 50.341 -29.058 1.00 17.22 ? 360  ARG A CG  1 
ATOM   2905 C CD  . ARG A 1 360 ? 50.529 50.242 -30.550 1.00 18.92 ? 360  ARG A CD  1 
ATOM   2906 N NE  . ARG A 1 360 ? 50.388 48.851 -30.962 1.00 26.27 ? 360  ARG A NE  1 
ATOM   2907 C CZ  . ARG A 1 360 ? 50.317 48.433 -32.220 1.00 37.34 ? 360  ARG A CZ  1 
ATOM   2908 N NH1 . ARG A 1 360 ? 50.292 49.286 -33.235 1.00 35.13 ? 360  ARG A NH1 1 
ATOM   2909 N NH2 . ARG A 1 360 ? 50.256 47.127 -32.466 1.00 30.69 ? 360  ARG A NH2 1 
ATOM   2910 N N   . ASP A 1 361 ? 48.519 47.920 -25.501 1.00 9.81  ? 361  ASP A N   1 
ATOM   2911 C CA  . ASP A 1 361 ? 47.320 47.585 -24.725 1.00 9.72  ? 361  ASP A CA  1 
ATOM   2912 C C   . ASP A 1 361 ? 46.049 47.654 -25.568 1.00 12.79 ? 361  ASP A C   1 
ATOM   2913 O O   . ASP A 1 361 ? 44.977 47.970 -25.054 1.00 14.45 ? 361  ASP A O   1 
ATOM   2914 C CB  . ASP A 1 361 ? 47.175 48.463 -23.465 1.00 9.65  ? 361  ASP A CB  1 
ATOM   2915 C CG  . ASP A 1 361 ? 46.479 47.731 -22.303 1.00 13.63 ? 361  ASP A CG  1 
ATOM   2916 O OD1 . ASP A 1 361 ? 46.925 46.616 -21.940 1.00 9.86  ? 361  ASP A OD1 1 
ATOM   2917 O OD2 . ASP A 1 361 ? 45.525 48.295 -21.708 1.00 11.82 ? 361  ASP A OD2 1 
ATOM   2918 N N   . ILE A 1 362 ? 46.156 47.356 -26.864 1.00 11.42 ? 362  ILE A N   1 
ATOM   2919 C CA  . ILE A 1 362 ? 44.989 47.392 -27.743 1.00 13.80 ? 362  ILE A CA  1 
ATOM   2920 C C   . ILE A 1 362 ? 44.304 46.040 -27.862 1.00 12.45 ? 362  ILE A C   1 
ATOM   2921 O O   . ILE A 1 362 ? 43.194 45.970 -28.410 1.00 14.18 ? 362  ILE A O   1 
ATOM   2922 C CB  . ILE A 1 362 ? 45.376 47.911 -29.144 1.00 12.13 ? 362  ILE A CB  1 
ATOM   2923 C CG1 . ILE A 1 362 ? 46.447 47.029 -29.783 1.00 14.51 ? 362  ILE A CG1 1 
ATOM   2924 C CG2 . ILE A 1 362 ? 45.855 49.362 -29.076 1.00 11.48 ? 362  ILE A CG2 1 
ATOM   2925 C CD1 . ILE A 1 362 ? 46.552 47.249 -31.295 1.00 22.05 ? 362  ILE A CD1 1 
ATOM   2926 N N   . TYR A 1 363 ? 44.923 44.969 -27.362 1.00 9.31  ? 363  TYR A N   1 
ATOM   2927 C CA  . TYR A 1 363 ? 44.365 43.622 -27.342 1.00 10.49 ? 363  TYR A CA  1 
ATOM   2928 C C   . TYR A 1 363 ? 44.053 43.117 -25.946 1.00 10.05 ? 363  TYR A C   1 
ATOM   2929 O O   . TYR A 1 363 ? 43.104 42.347 -25.774 1.00 11.33 ? 363  TYR A O   1 
ATOM   2930 C CB  . TYR A 1 363 ? 45.347 42.628 -27.980 1.00 10.13 ? 363  TYR A CB  1 
ATOM   2931 C CG  . TYR A 1 363 ? 45.830 43.010 -29.357 1.00 12.50 ? 363  TYR A CG  1 
ATOM   2932 C CD1 . TYR A 1 363 ? 44.958 43.059 -30.434 1.00 12.46 ? 363  TYR A CD1 1 
ATOM   2933 C CD2 . TYR A 1 363 ? 47.158 43.372 -29.563 1.00 15.87 ? 363  TYR A CD2 1 
ATOM   2934 C CE1 . TYR A 1 363 ? 45.412 43.419 -31.706 1.00 14.73 ? 363  TYR A CE1 1 
ATOM   2935 C CE2 . TYR A 1 363 ? 47.615 43.741 -30.814 1.00 12.99 ? 363  TYR A CE2 1 
ATOM   2936 C CZ  . TYR A 1 363 ? 46.741 43.759 -31.877 1.00 13.35 ? 363  TYR A CZ  1 
ATOM   2937 O OH  . TYR A 1 363 ? 47.203 44.126 -33.110 1.00 15.83 ? 363  TYR A OH  1 
ATOM   2938 N N   . ARG A 1 364 ? 44.835 43.526 -24.951 1.00 9.85  ? 364  ARG A N   1 
ATOM   2939 C CA  . ARG A 1 364 ? 44.761 42.952 -23.609 1.00 8.21  ? 364  ARG A CA  1 
ATOM   2940 C C   . ARG A 1 364 ? 43.435 43.232 -22.898 1.00 9.25  ? 364  ARG A C   1 
ATOM   2941 O O   . ARG A 1 364 ? 42.890 42.309 -22.286 1.00 9.47  ? 364  ARG A O   1 
ATOM   2942 C CB  . ARG A 1 364 ? 45.937 43.440 -22.755 1.00 9.04  ? 364  ARG A CB  1 
ATOM   2943 C CG  . ARG A 1 364 ? 46.111 42.666 -21.446 1.00 8.29  ? 364  ARG A CG  1 
ATOM   2944 C CD  . ARG A 1 364 ? 47.428 43.062 -20.754 1.00 7.33  ? 364  ARG A CD  1 
ATOM   2945 N NE  . ARG A 1 364 ? 48.595 42.599 -21.502 1.00 8.10  ? 364  ARG A NE  1 
ATOM   2946 C CZ  . ARG A 1 364 ? 49.369 43.371 -22.258 1.00 9.24  ? 364  ARG A CZ  1 
ATOM   2947 N NH1 . ARG A 1 364 ? 49.105 44.662 -22.442 1.00 8.13  ? 364  ARG A NH1 1 
ATOM   2948 N NH2 . ARG A 1 364 ? 50.429 42.835 -22.850 1.00 6.88  ? 364  ARG A NH2 1 
ATOM   2949 N N   . PRO A 1 365 ? 42.873 44.457 -22.918 1.00 11.31 ? 365  PRO A N   1 
ATOM   2950 C CA  . PRO A 1 365 ? 41.544 44.626 -22.288 1.00 11.29 ? 365  PRO A CA  1 
ATOM   2951 C C   . PRO A 1 365 ? 40.506 43.660 -22.837 1.00 11.11 ? 365  PRO A C   1 
ATOM   2952 O O   . PRO A 1 365 ? 39.794 43.013 -22.067 1.00 11.53 ? 365  PRO A O   1 
ATOM   2953 C CB  . PRO A 1 365 ? 41.184 46.089 -22.589 1.00 12.52 ? 365  PRO A CB  1 
ATOM   2954 C CG  . PRO A 1 365 ? 42.511 46.779 -22.759 1.00 11.42 ? 365  PRO A CG  1 
ATOM   2955 C CD  . PRO A 1 365 ? 43.451 45.749 -23.342 1.00 9.24  ? 365  PRO A CD  1 
ATOM   2956 N N   . TYR A 1 366 ? 40.407 43.549 -24.162 1.00 10.54 ? 366  TYR A N   1 
ATOM   2957 C CA  . TYR A 1 366 ? 39.449 42.637 -24.777 1.00 11.97 ? 366  TYR A CA  1 
ATOM   2958 C C   . TYR A 1 366 ? 39.771 41.186 -24.426 1.00 10.21 ? 366  TYR A C   1 
ATOM   2959 O O   . TYR A 1 366 ? 38.893 40.424 -24.006 1.00 9.42  ? 366  TYR A O   1 
ATOM   2960 C CB  . TYR A 1 366 ? 39.459 42.852 -26.301 1.00 12.23 ? 366  TYR A CB  1 
ATOM   2961 C CG  . TYR A 1 366 ? 38.804 41.745 -27.078 1.00 15.32 ? 366  TYR A CG  1 
ATOM   2962 C CD1 . TYR A 1 366 ? 37.465 41.423 -26.881 1.00 14.61 ? 366  TYR A CD1 1 
ATOM   2963 C CD2 . TYR A 1 366 ? 39.522 41.024 -28.027 1.00 17.21 ? 366  TYR A CD2 1 
ATOM   2964 C CE1 . TYR A 1 366 ? 36.862 40.396 -27.603 1.00 16.18 ? 366  TYR A CE1 1 
ATOM   2965 C CE2 . TYR A 1 366 ? 38.933 40.008 -28.752 1.00 24.10 ? 366  TYR A CE2 1 
ATOM   2966 C CZ  . TYR A 1 366 ? 37.604 39.693 -28.530 1.00 24.97 ? 366  TYR A CZ  1 
ATOM   2967 O OH  . TYR A 1 366 ? 37.021 38.679 -29.249 1.00 28.18 ? 366  TYR A OH  1 
ATOM   2968 N N   . SER A 1 367 ? 41.037 40.792 -24.571 1.00 8.74  ? 367  SER A N   1 
ATOM   2969 C CA  . SER A 1 367 ? 41.405 39.401 -24.338 1.00 10.63 ? 367  SER A CA  1 
ATOM   2970 C C   . SER A 1 367 ? 41.173 39.002 -22.882 1.00 8.77  ? 367  SER A C   1 
ATOM   2971 O O   . SER A 1 367 ? 40.636 37.927 -22.600 1.00 7.95  ? 367  SER A O   1 
ATOM   2972 C CB  . SER A 1 367 ? 42.863 39.179 -24.736 1.00 9.18  ? 367  SER A CB  1 
ATOM   2973 O OG  . SER A 1 367 ? 43.229 37.855 -24.438 1.00 10.07 ? 367  SER A OG  1 
ATOM   2974 N N   . LEU A 1 368 ? 41.583 39.855 -21.939 1.00 9.41  ? 368  LEU A N   1 
ATOM   2975 C CA  . LEU A 1 368 ? 41.363 39.574 -20.519 1.00 9.22  ? 368  LEU A CA  1 
ATOM   2976 C C   . LEU A 1 368 ? 39.878 39.387 -20.204 1.00 8.98  ? 368  LEU A C   1 
ATOM   2977 O O   . LEU A 1 368 ? 39.478 38.414 -19.554 1.00 9.10  ? 368  LEU A O   1 
ATOM   2978 C CB  . LEU A 1 368 ? 41.941 40.712 -19.667 1.00 8.87  ? 368  LEU A CB  1 
ATOM   2979 C CG  . LEU A 1 368 ? 41.676 40.678 -18.145 1.00 12.22 ? 368  LEU A CG  1 
ATOM   2980 C CD1 . LEU A 1 368 ? 42.473 39.571 -17.431 1.00 7.62  ? 368  LEU A CD1 1 
ATOM   2981 C CD2 . LEU A 1 368 ? 41.967 42.024 -17.490 1.00 10.88 ? 368  LEU A CD2 1 
ATOM   2982 N N   . LEU A 1 369 ? 39.047 40.328 -20.635 1.00 9.09  ? 369  LEU A N   1 
ATOM   2983 C CA  . LEU A 1 369 ? 37.624 40.234 -20.330 1.00 11.12 ? 369  LEU A CA  1 
ATOM   2984 C C   . LEU A 1 369 ? 36.998 39.008 -20.985 1.00 10.65 ? 369  LEU A C   1 
ATOM   2985 O O   . LEU A 1 369 ? 36.225 38.280 -20.345 1.00 8.56  ? 369  LEU A O   1 
ATOM   2986 C CB  . LEU A 1 369 ? 36.912 41.511 -20.778 1.00 10.14 ? 369  LEU A CB  1 
ATOM   2987 C CG  . LEU A 1 369 ? 35.394 41.519 -20.680 1.00 11.43 ? 369  LEU A CG  1 
ATOM   2988 C CD1 . LEU A 1 369 ? 34.924 41.176 -19.258 1.00 10.53 ? 369  LEU A CD1 1 
ATOM   2989 C CD2 . LEU A 1 369 ? 34.868 42.888 -21.145 1.00 12.78 ? 369  LEU A CD2 1 
ATOM   2990 N N   . ALA A 1 370 ? 37.330 38.755 -22.252 1.00 7.57  ? 370  ALA A N   1 
ATOM   2991 C CA  . ALA A 1 370 ? 36.710 37.629 -22.952 1.00 13.62 ? 370  ALA A CA  1 
ATOM   2992 C C   . ALA A 1 370 ? 37.117 36.296 -22.338 1.00 10.66 ? 370  ALA A C   1 
ATOM   2993 O O   . ALA A 1 370 ? 36.298 35.372 -22.254 1.00 9.03  ? 370  ALA A O   1 
ATOM   2994 C CB  . ALA A 1 370 ? 37.070 37.652 -24.438 1.00 8.33  ? 370  ALA A CB  1 
ATOM   2995 N N   . HIS A 1 371 ? 38.378 36.163 -21.919 1.00 8.29  ? 371  HIS A N   1 
ATOM   2996 C CA  . HIS A 1 371 ? 38.791 34.898 -21.316 1.00 9.58  ? 371  HIS A CA  1 
ATOM   2997 C C   . HIS A 1 371 ? 38.199 34.726 -19.926 1.00 10.97 ? 371  HIS A C   1 
ATOM   2998 O O   . HIS A 1 371 ? 37.861 33.607 -19.528 1.00 9.47  ? 371  HIS A O   1 
ATOM   2999 C CB  . HIS A 1 371 ? 40.314 34.789 -21.249 1.00 11.63 ? 371  HIS A CB  1 
ATOM   3000 C CG  . HIS A 1 371 ? 40.949 34.442 -22.557 1.00 11.48 ? 371  HIS A CG  1 
ATOM   3001 N ND1 . HIS A 1 371 ? 41.368 35.401 -23.456 1.00 7.06  ? 371  HIS A ND1 1 
ATOM   3002 C CD2 . HIS A 1 371 ? 41.229 33.244 -23.123 1.00 9.50  ? 371  HIS A CD2 1 
ATOM   3003 C CE1 . HIS A 1 371 ? 41.887 34.807 -24.514 1.00 8.84  ? 371  HIS A CE1 1 
ATOM   3004 N NE2 . HIS A 1 371 ? 41.822 33.500 -24.334 1.00 10.26 ? 371  HIS A NE2 1 
ATOM   3005 N N   . LEU A 1 372 ? 38.075 35.817 -19.166 1.00 9.35  ? 372  LEU A N   1 
ATOM   3006 C CA  . LEU A 1 372 ? 37.458 35.708 -17.849 1.00 9.55  ? 372  LEU A CA  1 
ATOM   3007 C C   . LEU A 1 372 ? 35.976 35.383 -17.965 1.00 11.18 ? 372  LEU A C   1 
ATOM   3008 O O   . LEU A 1 372 ? 35.412 34.716 -17.090 1.00 13.00 ? 372  LEU A O   1 
ATOM   3009 C CB  . LEU A 1 372 ? 37.667 37.005 -17.055 1.00 9.87  ? 372  LEU A CB  1 
ATOM   3010 C CG  . LEU A 1 372 ? 39.063 37.147 -16.422 1.00 11.53 ? 372  LEU A CG  1 
ATOM   3011 C CD1 . LEU A 1 372 ? 39.231 38.500 -15.736 1.00 11.27 ? 372  LEU A CD1 1 
ATOM   3012 C CD2 . LEU A 1 372 ? 39.300 36.012 -15.435 1.00 11.43 ? 372  LEU A CD2 1 
ATOM   3013 N N   . LYS A 1 373 ? 35.328 35.848 -19.028 1.00 10.15 ? 373  LYS A N   1 
ATOM   3014 C CA  . LYS A 1 373 ? 33.935 35.476 -19.240 1.00 12.55 ? 373  LYS A CA  1 
ATOM   3015 C C   . LYS A 1 373 ? 33.807 33.970 -19.461 1.00 12.34 ? 373  LYS A C   1 
ATOM   3016 O O   . LYS A 1 373 ? 32.895 33.326 -18.922 1.00 13.62 ? 373  LYS A O   1 
ATOM   3017 C CB  . LYS A 1 373 ? 33.364 36.257 -20.426 1.00 14.65 ? 373  LYS A CB  1 
ATOM   3018 C CG  . LYS A 1 373 ? 31.876 35.983 -20.672 1.00 15.98 ? 373  LYS A CG  1 
ATOM   3019 C CD  . LYS A 1 373 ? 31.670 34.996 -21.799 1.00 24.15 ? 373  LYS A CD  1 
ATOM   3020 C CE  . LYS A 1 373 ? 30.175 34.788 -22.100 1.00 29.15 ? 373  LYS A CE  1 
ATOM   3021 N NZ  . LYS A 1 373 ? 29.945 33.574 -22.957 1.00 31.52 ? 373  LYS A NZ  1 
ATOM   3022 N N   . ILE A 1 374 ? 34.724 33.394 -20.241 1.00 10.20 ? 374  ILE A N   1 
ATOM   3023 C CA  . ILE A 1 374 ? 34.751 31.944 -20.443 1.00 11.12 ? 374  ILE A CA  1 
ATOM   3024 C C   . ILE A 1 374 ? 34.994 31.225 -19.120 1.00 12.63 ? 374  ILE A C   1 
ATOM   3025 O O   . ILE A 1 374 ? 34.366 30.195 -18.828 1.00 11.79 ? 374  ILE A O   1 
ATOM   3026 C CB  . ILE A 1 374 ? 35.824 31.572 -21.486 1.00 12.48 ? 374  ILE A CB  1 
ATOM   3027 C CG1 . ILE A 1 374 ? 35.504 32.179 -22.861 1.00 17.99 ? 374  ILE A CG1 1 
ATOM   3028 C CG2 . ILE A 1 374 ? 35.989 30.054 -21.572 1.00 13.49 ? 374  ILE A CG2 1 
ATOM   3029 C CD1 . ILE A 1 374 ? 34.132 31.799 -23.429 1.00 18.76 ? 374  ILE A CD1 1 
ATOM   3030 N N   . VAL A 1 375 ? 35.924 31.742 -18.304 1.00 10.61 ? 375  VAL A N   1 
ATOM   3031 C CA  . VAL A 1 375 ? 36.152 31.164 -16.978 1.00 12.68 ? 375  VAL A CA  1 
ATOM   3032 C C   . VAL A 1 375 ? 34.865 31.196 -16.158 1.00 16.79 ? 375  VAL A C   1 
ATOM   3033 O O   . VAL A 1 375 ? 34.502 30.209 -15.504 1.00 13.61 ? 375  VAL A O   1 
ATOM   3034 C CB  . VAL A 1 375 ? 37.297 31.896 -16.253 1.00 11.79 ? 375  VAL A CB  1 
ATOM   3035 C CG1 . VAL A 1 375 ? 37.273 31.578 -14.751 1.00 10.85 ? 375  VAL A CG1 1 
ATOM   3036 C CG2 . VAL A 1 375 ? 38.662 31.526 -16.880 1.00 12.03 ? 375  VAL A CG2 1 
ATOM   3037 N N   . GLU A 1 376 ? 34.159 32.334 -16.174 1.00 13.06 ? 376  GLU A N   1 
ATOM   3038 C CA  . GLU A 1 376 ? 32.897 32.431 -15.436 1.00 15.05 ? 376  GLU A CA  1 
ATOM   3039 C C   . GLU A 1 376 ? 31.857 31.442 -15.969 1.00 14.28 ? 376  GLU A C   1 
ATOM   3040 O O   . GLU A 1 376 ? 31.080 30.877 -15.189 1.00 15.49 ? 376  GLU A O   1 
ATOM   3041 C CB  . GLU A 1 376 ? 32.349 33.865 -15.480 1.00 14.57 ? 376  GLU A CB  1 
ATOM   3042 C CG  . GLU A 1 376 ? 31.236 34.140 -14.438 1.00 15.64 ? 376  GLU A CG  1 
ATOM   3043 C CD  . GLU A 1 376 ? 30.961 35.633 -14.224 1.00 20.00 ? 376  GLU A CD  1 
ATOM   3044 O OE1 . GLU A 1 376 ? 31.690 36.475 -14.800 1.00 19.37 ? 376  GLU A OE1 1 
ATOM   3045 O OE2 . GLU A 1 376 ? 30.023 35.969 -13.461 1.00 22.33 ? 376  GLU A OE2 1 
ATOM   3046 N N   . ASP A 1 377 ? 31.827 31.216 -17.290 1.00 13.67 ? 377  ASP A N   1 
ATOM   3047 C CA  . ASP A 1 377 ? 30.946 30.189 -17.860 1.00 14.82 ? 377  ASP A CA  1 
ATOM   3048 C C   . ASP A 1 377 ? 31.240 28.811 -17.275 1.00 17.52 ? 377  ASP A C   1 
ATOM   3049 O O   . ASP A 1 377 ? 30.318 28.034 -17.002 1.00 14.57 ? 377  ASP A O   1 
ATOM   3050 C CB  . ASP A 1 377 ? 31.107 30.116 -19.380 1.00 13.53 ? 377  ASP A CB  1 
ATOM   3051 C CG  . ASP A 1 377 ? 30.448 31.269 -20.117 1.00 22.92 ? 377  ASP A CG  1 
ATOM   3052 O OD1 . ASP A 1 377 ? 29.692 32.044 -19.494 1.00 17.30 ? 377  ASP A OD1 1 
ATOM   3053 O OD2 . ASP A 1 377 ? 30.715 31.403 -21.338 1.00 20.24 ? 377  ASP A OD2 1 
ATOM   3054 N N   . CYS A 1 378 ? 32.526 28.463 -17.141 1.00 14.70 ? 378  CYS A N   1 
ATOM   3055 C CA  . CYS A 1 378 ? 32.896 27.167 -16.572 1.00 17.06 ? 378  CYS A CA  1 
ATOM   3056 C C   . CYS A 1 378 ? 32.465 27.056 -15.109 1.00 17.39 ? 378  CYS A C   1 
ATOM   3057 O O   . CYS A 1 378 ? 31.985 26.001 -14.677 1.00 16.99 ? 378  CYS A O   1 
ATOM   3058 C CB  . CYS A 1 378 ? 34.410 26.942 -16.713 1.00 11.82 ? 378  CYS A CB  1 
ATOM   3059 S SG  . CYS A 1 378 ? 34.968 26.771 -18.428 1.00 17.48 ? 378  CYS A SG  1 
ATOM   3060 N N   . LEU A 1 379 ? 32.633 28.131 -14.329 1.00 14.03 ? 379  LEU A N   1 
ATOM   3061 C CA  . LEU A 1 379 ? 32.157 28.121 -12.948 1.00 16.85 ? 379  LEU A CA  1 
ATOM   3062 C C   . LEU A 1 379 ? 30.650 27.894 -12.876 1.00 19.19 ? 379  LEU A C   1 
ATOM   3063 O O   . LEU A 1 379 ? 30.168 27.157 -12.008 1.00 20.54 ? 379  LEU A O   1 
ATOM   3064 C CB  . LEU A 1 379 ? 32.531 29.429 -12.254 1.00 16.34 ? 379  LEU A CB  1 
ATOM   3065 C CG  . LEU A 1 379 ? 34.027 29.620 -12.014 1.00 17.31 ? 379  LEU A CG  1 
ATOM   3066 C CD1 . LEU A 1 379 ? 34.270 31.043 -11.542 1.00 18.13 ? 379  LEU A CD1 1 
ATOM   3067 C CD2 . LEU A 1 379 ? 34.512 28.613 -10.995 1.00 19.29 ? 379  LEU A CD2 1 
ATOM   3068 N N   . LYS A 1 380 ? 29.887 28.529 -13.771 1.00 19.29 ? 380  LYS A N   1 
ATOM   3069 C CA  . LYS A 1 380 ? 28.450 28.281 -13.827 1.00 22.08 ? 380  LYS A CA  1 
ATOM   3070 C C   . LYS A 1 380 ? 28.137 26.822 -14.126 1.00 21.21 ? 380  LYS A C   1 
ATOM   3071 O O   . LYS A 1 380 ? 27.083 26.328 -13.729 1.00 23.57 ? 380  LYS A O   1 
ATOM   3072 C CB  . LYS A 1 380 ? 27.792 29.175 -14.879 1.00 19.67 ? 380  LYS A CB  1 
ATOM   3073 C CG  . LYS A 1 380 ? 27.640 30.610 -14.441 1.00 28.72 ? 380  LYS A CG  1 
ATOM   3074 C CD  . LYS A 1 380 ? 26.754 31.385 -15.410 1.00 38.76 ? 380  LYS A CD  1 
ATOM   3075 C CE  . LYS A 1 380 ? 27.236 32.815 -15.568 1.00 34.96 ? 380  LYS A CE  1 
ATOM   3076 N NZ  . LYS A 1 380 ? 26.494 33.526 -16.646 1.00 46.23 ? 380  LYS A NZ  1 
ATOM   3077 N N   . GLU A 1 381 ? 29.023 26.119 -14.824 1.00 20.77 ? 381  GLU A N   1 
ATOM   3078 C CA  . GLU A 1 381 ? 28.826 24.688 -15.036 1.00 22.83 ? 381  GLU A CA  1 
ATOM   3079 C C   . GLU A 1 381 ? 29.255 23.855 -13.833 1.00 20.97 ? 381  GLU A C   1 
ATOM   3080 O O   . GLU A 1 381 ? 29.296 22.622 -13.934 1.00 20.95 ? 381  GLU A O   1 
ATOM   3081 C CB  . GLU A 1 381 ? 29.573 24.228 -16.296 1.00 19.18 ? 381  GLU A CB  1 
ATOM   3082 C CG  . GLU A 1 381 ? 29.031 24.857 -17.579 1.00 23.64 ? 381  GLU A CG  1 
ATOM   3083 C CD  . GLU A 1 381 ? 30.021 24.858 -18.745 1.00 26.97 ? 381  GLU A CD  1 
ATOM   3084 O OE1 . GLU A 1 381 ? 29.670 25.389 -19.820 1.00 34.00 ? 381  GLU A OE1 1 
ATOM   3085 O OE2 . GLU A 1 381 ? 31.132 24.301 -18.614 1.00 28.94 ? 381  GLU A OE2 1 
ATOM   3086 N N   . ASN A 1 382 ? 29.597 24.513 -12.719 1.00 20.37 ? 382  ASN A N   1 
ATOM   3087 C CA  . ASN A 1 382 ? 30.060 23.867 -11.484 1.00 23.77 ? 382  ASN A CA  1 
ATOM   3088 C C   . ASN A 1 382 ? 31.383 23.126 -11.669 1.00 24.79 ? 382  ASN A C   1 
ATOM   3089 O O   . ASN A 1 382 ? 31.652 22.148 -10.971 1.00 22.35 ? 382  ASN A O   1 
ATOM   3090 C CB  . ASN A 1 382 ? 29.003 22.919 -10.901 1.00 25.91 ? 382  ASN A CB  1 
ATOM   3091 C CG  . ASN A 1 382 ? 27.708 23.634 -10.544 1.00 36.33 ? 382  ASN A CG  1 
ATOM   3092 O OD1 . ASN A 1 382 ? 26.623 23.057 -10.641 1.00 45.12 ? 382  ASN A OD1 1 
ATOM   3093 N ND2 . ASN A 1 382 ? 27.819 24.883 -10.097 1.00 36.50 ? 382  ASN A ND2 1 
ATOM   3094 N N   . MET A 1 383 ? 32.231 23.589 -12.585 1.00 19.28 ? 383  MET A N   1 
ATOM   3095 C CA  . MET A 1 383 ? 33.543 22.975 -12.737 1.00 21.32 ? 383  MET A CA  1 
ATOM   3096 C C   . MET A 1 383 ? 34.418 23.334 -11.541 1.00 18.63 ? 383  MET A C   1 
ATOM   3097 O O   . MET A 1 383 ? 34.344 24.444 -11.004 1.00 14.74 ? 383  MET A O   1 
ATOM   3098 C CB  . MET A 1 383 ? 34.182 23.423 -14.057 1.00 18.16 ? 383  MET A CB  1 
ATOM   3099 C CG  . MET A 1 383 ? 35.658 23.048 -14.270 1.00 16.17 ? 383  MET A CG  1 
ATOM   3100 S SD  . MET A 1 383 ? 36.381 23.928 -15.698 1.00 16.34 ? 383  MET A SD  1 
ATOM   3101 C CE  . MET A 1 383 ? 35.449 23.215 -17.070 1.00 11.28 ? 383  MET A CE  1 
ATOM   3102 N N   . ASP A 1 384 ? 35.207 22.365 -11.082 1.00 16.82 ? 384  ASP A N   1 
ATOM   3103 C CA  . ASP A 1 384 ? 36.140 22.601 -9.987  1.00 20.98 ? 384  ASP A CA  1 
ATOM   3104 C C   . ASP A 1 384 ? 37.336 23.421 -10.477 1.00 20.38 ? 384  ASP A C   1 
ATOM   3105 O O   . ASP A 1 384 ? 38.456 22.911 -10.612 1.00 17.14 ? 384  ASP A O   1 
ATOM   3106 C CB  . ASP A 1 384 ? 36.584 21.265 -9.379  1.00 20.08 ? 384  ASP A CB  1 
ATOM   3107 C CG  . ASP A 1 384 ? 37.341 21.432 -8.069  1.00 19.42 ? 384  ASP A CG  1 
ATOM   3108 O OD1 . ASP A 1 384 ? 37.411 22.566 -7.552  1.00 20.23 ? 384  ASP A OD1 1 
ATOM   3109 O OD2 . ASP A 1 384 ? 37.875 20.420 -7.554  1.00 20.02 ? 384  ASP A OD2 1 
ATOM   3110 N N   . LEU A 1 385 ? 37.096 24.700 -10.739 1.00 15.13 ? 385  LEU A N   1 
ATOM   3111 C CA  . LEU A 1 385 ? 38.093 25.631 -11.247 1.00 15.25 ? 385  LEU A CA  1 
ATOM   3112 C C   . LEU A 1 385 ? 38.326 26.678 -10.169 1.00 15.38 ? 385  LEU A C   1 
ATOM   3113 O O   . LEU A 1 385 ? 37.382 27.354 -9.753  1.00 17.01 ? 385  LEU A O   1 
ATOM   3114 C CB  . LEU A 1 385 ? 37.600 26.270 -12.544 1.00 15.13 ? 385  LEU A CB  1 
ATOM   3115 C CG  . LEU A 1 385 ? 38.475 27.334 -13.197 1.00 16.54 ? 385  LEU A CG  1 
ATOM   3116 C CD1 . LEU A 1 385 ? 39.817 26.715 -13.574 1.00 14.40 ? 385  LEU A CD1 1 
ATOM   3117 C CD2 . LEU A 1 385 ? 37.751 27.891 -14.426 1.00 20.22 ? 385  LEU A CD2 1 
ATOM   3118 N N   . ARG A 1 386 ? 39.572 26.808 -9.710  1.00 12.39 ? 386  ARG A N   1 
ATOM   3119 C CA  . ARG A 1 386 ? 39.854 27.481 -8.452  1.00 15.23 ? 386  ARG A CA  1 
ATOM   3120 C C   . ARG A 1 386 ? 40.634 28.784 -8.592  1.00 12.59 ? 386  ARG A C   1 
ATOM   3121 O O   . ARG A 1 386 ? 40.850 29.474 -7.585  1.00 11.84 ? 386  ARG A O   1 
ATOM   3122 C CB  . ARG A 1 386 ? 40.600 26.511 -7.530  1.00 15.73 ? 386  ARG A CB  1 
ATOM   3123 C CG  . ARG A 1 386 ? 39.737 25.316 -7.138  1.00 18.59 ? 386  ARG A CG  1 
ATOM   3124 C CD  . ARG A 1 386 ? 40.268 24.545 -5.936  1.00 20.87 ? 386  ARG A CD  1 
ATOM   3125 N NE  . ARG A 1 386 ? 39.516 23.308 -5.748  1.00 22.88 ? 386  ARG A NE  1 
ATOM   3126 C CZ  . ARG A 1 386 ? 39.855 22.329 -4.917  1.00 23.23 ? 386  ARG A CZ  1 
ATOM   3127 N NH1 . ARG A 1 386 ? 40.972 22.375 -4.209  1.00 21.66 ? 386  ARG A NH1 1 
ATOM   3128 N NH2 . ARG A 1 386 ? 39.056 21.271 -4.803  1.00 16.90 ? 386  ARG A NH2 1 
ATOM   3129 N N   . GLY A 1 387 ? 41.056 29.159 -9.791  1.00 10.65 ? 387  GLY A N   1 
ATOM   3130 C CA  . GLY A 1 387 ? 41.745 30.425 -9.907  1.00 11.92 ? 387  GLY A CA  1 
ATOM   3131 C C   . GLY A 1 387 ? 42.120 30.721 -11.341 1.00 11.79 ? 387  GLY A C   1 
ATOM   3132 O O   . GLY A 1 387 ? 42.078 29.850 -12.214 1.00 9.91  ? 387  GLY A O   1 
ATOM   3133 N N   . TYR A 1 388 ? 42.532 31.975 -11.550 1.00 10.57 ? 388  TYR A N   1 
ATOM   3134 C CA  . TYR A 1 388 ? 42.962 32.485 -12.844 1.00 8.93  ? 388  TYR A CA  1 
ATOM   3135 C C   . TYR A 1 388 ? 44.158 33.392 -12.607 1.00 11.92 ? 388  TYR A C   1 
ATOM   3136 O O   . TYR A 1 388 ? 44.078 34.325 -11.805 1.00 8.26  ? 388  TYR A O   1 
ATOM   3137 C CB  . TYR A 1 388 ? 41.830 33.259 -13.559 1.00 9.29  ? 388  TYR A CB  1 
ATOM   3138 C CG  . TYR A 1 388 ? 42.304 34.017 -14.804 1.00 9.29  ? 388  TYR A CG  1 
ATOM   3139 C CD1 . TYR A 1 388 ? 42.829 35.301 -14.711 1.00 10.59 ? 388  TYR A CD1 1 
ATOM   3140 C CD2 . TYR A 1 388 ? 42.233 33.432 -16.054 1.00 8.14  ? 388  TYR A CD2 1 
ATOM   3141 C CE1 . TYR A 1 388 ? 43.263 35.989 -15.839 1.00 9.72  ? 388  TYR A CE1 1 
ATOM   3142 C CE2 . TYR A 1 388 ? 42.664 34.107 -17.201 1.00 10.45 ? 388  TYR A CE2 1 
ATOM   3143 C CZ  . TYR A 1 388 ? 43.183 35.392 -17.081 1.00 10.31 ? 388  TYR A CZ  1 
ATOM   3144 O OH  . TYR A 1 388 ? 43.604 36.084 -18.199 1.00 9.60  ? 388  TYR A OH  1 
ATOM   3145 N N   . MET A 1 389 ? 45.246 33.135 -13.319 1.00 8.80  ? 389  MET A N   1 
ATOM   3146 C CA  . MET A 1 389 ? 46.508 33.811 -13.108 1.00 9.27  ? 389  MET A CA  1 
ATOM   3147 C C   . MET A 1 389 ? 46.948 34.296 -14.487 1.00 9.88  ? 389  MET A C   1 
ATOM   3148 O O   . MET A 1 389 ? 47.053 33.491 -15.423 1.00 8.70  ? 389  MET A O   1 
ATOM   3149 C CB  . MET A 1 389 ? 47.445 32.793 -12.467 1.00 10.84 ? 389  MET A CB  1 
ATOM   3150 C CG  . MET A 1 389 ? 47.394 32.908 -10.932 1.00 9.82  ? 389  MET A CG  1 
ATOM   3151 S SD  . MET A 1 389 ? 48.209 31.549 -10.091 1.00 13.74 ? 389  MET A SD  1 
ATOM   3152 C CE  . MET A 1 389 ? 46.886 30.352 -10.279 1.00 13.92 ? 389  MET A CE  1 
ATOM   3153 N N   . HIS A 1 390 ? 47.089 35.603 -14.631 1.00 7.82  ? 390  HIS A N   1 
ATOM   3154 C CA  . HIS A 1 390 ? 47.457 36.214 -15.927 1.00 8.23  ? 390  HIS A CA  1 
ATOM   3155 C C   . HIS A 1 390 ? 48.972 36.265 -16.147 1.00 8.07  ? 390  HIS A C   1 
ATOM   3156 O O   . HIS A 1 390 ? 49.696 36.454 -15.180 1.00 7.36  ? 390  HIS A O   1 
ATOM   3157 C CB  . HIS A 1 390 ? 46.897 37.637 -15.995 1.00 9.69  ? 390  HIS A CB  1 
ATOM   3158 C CG  . HIS A 1 390 ? 46.826 38.249 -17.351 1.00 8.66  ? 390  HIS A CG  1 
ATOM   3159 N ND1 . HIS A 1 390 ? 45.808 37.972 -18.227 1.00 8.17  ? 390  HIS A ND1 1 
ATOM   3160 C CD2 . HIS A 1 390 ? 47.609 39.166 -17.956 1.00 7.01  ? 390  HIS A CD2 1 
ATOM   3161 C CE1 . HIS A 1 390 ? 45.981 38.665 -19.328 1.00 8.50  ? 390  HIS A CE1 1 
ATOM   3162 N NE2 . HIS A 1 390 ? 47.071 39.411 -19.182 1.00 7.96  ? 390  HIS A NE2 1 
ATOM   3163 N N   . TRP A 1 391 ? 49.397 36.096 -17.388 1.00 5.52  ? 391  TRP A N   1 
ATOM   3164 C CA  . TRP A 1 391 ? 50.814 36.277 -17.773 1.00 7.04  ? 391  TRP A CA  1 
ATOM   3165 C C   . TRP A 1 391 ? 50.911 37.598 -18.551 1.00 5.82  ? 391  TRP A C   1 
ATOM   3166 O O   . TRP A 1 391 ? 50.470 37.639 -19.689 1.00 7.20  ? 391  TRP A O   1 
ATOM   3167 C CB  . TRP A 1 391 ? 51.377 35.122 -18.610 1.00 6.98  ? 391  TRP A CB  1 
ATOM   3168 C CG  . TRP A 1 391 ? 52.840 35.278 -18.860 1.00 8.24  ? 391  TRP A CG  1 
ATOM   3169 C CD1 . TRP A 1 391 ? 53.443 36.023 -19.829 1.00 9.30  ? 391  TRP A CD1 1 
ATOM   3170 C CD2 . TRP A 1 391 ? 53.895 34.709 -18.072 1.00 7.96  ? 391  TRP A CD2 1 
ATOM   3171 N NE1 . TRP A 1 391 ? 54.802 35.942 -19.708 1.00 8.27  ? 391  TRP A NE1 1 
ATOM   3172 C CE2 . TRP A 1 391 ? 55.109 35.141 -18.643 1.00 8.35  ? 391  TRP A CE2 1 
ATOM   3173 C CE3 . TRP A 1 391 ? 53.928 33.874 -16.951 1.00 7.40  ? 391  TRP A CE3 1 
ATOM   3174 C CZ2 . TRP A 1 391 ? 56.344 34.760 -18.124 1.00 7.66  ? 391  TRP A CZ2 1 
ATOM   3175 C CZ3 . TRP A 1 391 ? 55.149 33.497 -16.444 1.00 7.75  ? 391  TRP A CZ3 1 
ATOM   3176 C CH2 . TRP A 1 391 ? 56.338 33.941 -17.022 1.00 7.69  ? 391  TRP A CH2 1 
ATOM   3177 N N   . SER A 1 392 ? 51.463 38.616 -17.903 1.00 5.51  ? 392  SER A N   1 
ATOM   3178 C CA  . SER A 1 392 ? 51.878 38.651 -16.481 1.00 6.90  ? 392  SER A CA  1 
ATOM   3179 C C   . SER A 1 392 ? 51.591 40.039 -15.866 1.00 9.39  ? 392  SER A C   1 
ATOM   3180 O O   . SER A 1 392 ? 50.946 40.871 -16.516 1.00 6.68  ? 392  SER A O   1 
ATOM   3181 C CB  . SER A 1 392 ? 53.355 38.264 -16.289 1.00 6.30  ? 392  SER A CB  1 
ATOM   3182 O OG  . SER A 1 392 ? 53.789 38.300 -14.945 1.00 9.95  ? 392  SER A OG  1 
ATOM   3183 N N   . ILE A 1 393 ? 52.080 40.258 -14.650 1.00 8.71  ? 393  ILE A N   1 
ATOM   3184 C CA  . ILE A 1 393 ? 51.924 41.583 -13.976 1.00 7.89  ? 393  ILE A CA  1 
ATOM   3185 C C   . ILE A 1 393 ? 52.764 42.606 -14.744 1.00 9.06  ? 393  ILE A C   1 
ATOM   3186 O O   . ILE A 1 393 ? 52.281 43.695 -14.991 1.00 8.29  ? 393  ILE A O   1 
ATOM   3187 C CB  . ILE A 1 393 ? 52.326 41.508 -12.487 1.00 6.94  ? 393  ILE A CB  1 
ATOM   3188 C CG1 . ILE A 1 393 ? 52.068 42.834 -11.767 1.00 10.50 ? 393  ILE A CG1 1 
ATOM   3189 C CG2 . ILE A 1 393 ? 53.755 41.016 -12.297 1.00 7.25  ? 393  ILE A CG2 1 
ATOM   3190 C CD1 . ILE A 1 393 ? 50.688 43.386 -11.990 1.00 9.68  ? 393  ILE A CD1 1 
ATOM   3191 N N   . ILE A 1 394 ? 53.977 42.214 -15.122 1.00 7.50  ? 394  ILE A N   1 
ATOM   3192 C CA  . ILE A 1 394 ? 54.901 43.148 -15.813 1.00 8.72  ? 394  ILE A CA  1 
ATOM   3193 C C   . ILE A 1 394 ? 55.543 42.551 -17.074 1.00 9.75  ? 394  ILE A C   1 
ATOM   3194 O O   . ILE A 1 394 ? 55.692 41.343 -17.159 1.00 7.70  ? 394  ILE A O   1 
ATOM   3195 C CB  . ILE A 1 394 ? 55.987 43.680 -14.847 1.00 5.58  ? 394  ILE A CB  1 
ATOM   3196 C CG1 . ILE A 1 394 ? 56.925 42.558 -14.391 1.00 7.97  ? 394  ILE A CG1 1 
ATOM   3197 C CG2 . ILE A 1 394 ? 55.380 44.435 -13.675 1.00 8.28  ? 394  ILE A CG2 1 
ATOM   3198 C CD1 . ILE A 1 394 ? 58.126 43.034 -13.613 1.00 7.11  ? 394  ILE A CD1 1 
ATOM   3199 N N   . ASP A 1 395 ? 55.929 43.433 -17.994 1.00 7.40  ? 395  ASP A N   1 
ATOM   3200 C CA  . ASP A 1 395 ? 56.722 43.026 -19.150 1.00 7.83  ? 395  ASP A CA  1 
ATOM   3201 C C   . ASP A 1 395 ? 57.998 42.331 -18.683 1.00 9.76  ? 395  ASP A C   1 
ATOM   3202 O O   . ASP A 1 395 ? 58.535 42.638 -17.621 1.00 8.42  ? 395  ASP A O   1 
ATOM   3203 C CB  . ASP A 1 395 ? 57.125 44.238 -19.997 1.00 9.39  ? 395  ASP A CB  1 
ATOM   3204 C CG  . ASP A 1 395 ? 55.943 45.008 -20.548 1.00 7.92  ? 395  ASP A CG  1 
ATOM   3205 O OD1 . ASP A 1 395 ? 54.830 44.437 -20.659 1.00 8.69  ? 395  ASP A OD1 1 
ATOM   3206 O OD2 . ASP A 1 395 ? 56.153 46.191 -20.904 1.00 8.46  ? 395  ASP A OD2 1 
ATOM   3207 N N   . ASN A 1 396 ? 58.520 41.425 -19.508 1.00 8.69  ? 396  ASN A N   1 
ATOM   3208 C CA  . ASN A 1 396 ? 59.647 40.612 -19.069 1.00 7.81  ? 396  ASN A CA  1 
ATOM   3209 C C   . ASN A 1 396 ? 60.373 40.048 -20.292 1.00 9.38  ? 396  ASN A C   1 
ATOM   3210 O O   . ASN A 1 396 ? 60.037 40.358 -21.438 1.00 7.66  ? 396  ASN A O   1 
ATOM   3211 C CB  . ASN A 1 396 ? 59.155 39.509 -18.125 1.00 7.38  ? 396  ASN A CB  1 
ATOM   3212 C CG  . ASN A 1 396 ? 58.096 38.623 -18.768 1.00 8.92  ? 396  ASN A CG  1 
ATOM   3213 O OD1 . ASN A 1 396 ? 58.422 37.659 -19.457 1.00 10.08 ? 396  ASN A OD1 1 
ATOM   3214 N ND2 . ASN A 1 396 ? 56.819 38.949 -18.551 1.00 8.50  ? 396  ASN A ND2 1 
ATOM   3215 N N   . PHE A 1 397 ? 61.381 39.207 -20.037 1.00 7.20  ? 397  PHE A N   1 
ATOM   3216 C CA  . PHE A 1 397 ? 62.242 38.667 -21.097 1.00 8.25  ? 397  PHE A CA  1 
ATOM   3217 C C   . PHE A 1 397 ? 61.550 37.481 -21.762 1.00 9.03  ? 397  PHE A C   1 
ATOM   3218 O O   . PHE A 1 397 ? 61.472 36.402 -21.171 1.00 8.68  ? 397  PHE A O   1 
ATOM   3219 C CB  . PHE A 1 397 ? 63.579 38.248 -20.489 1.00 9.43  ? 397  PHE A CB  1 
ATOM   3220 C CG  . PHE A 1 397 ? 64.642 37.878 -21.494 1.00 10.77 ? 397  PHE A CG  1 
ATOM   3221 C CD1 . PHE A 1 397 ? 65.513 38.843 -21.986 1.00 9.69  ? 397  PHE A CD1 1 
ATOM   3222 C CD2 . PHE A 1 397 ? 64.810 36.555 -21.897 1.00 8.60  ? 397  PHE A CD2 1 
ATOM   3223 C CE1 . PHE A 1 397 ? 66.520 38.495 -22.887 1.00 9.80  ? 397  PHE A CE1 1 
ATOM   3224 C CE2 . PHE A 1 397 ? 65.815 36.208 -22.788 1.00 10.26 ? 397  PHE A CE2 1 
ATOM   3225 C CZ  . PHE A 1 397 ? 66.665 37.186 -23.288 1.00 9.99  ? 397  PHE A CZ  1 
ATOM   3226 N N   . GLU A 1 398 ? 61.082 37.647 -23.003 1.00 8.10  ? 398  GLU A N   1 
ATOM   3227 C CA  . GLU A 1 398 ? 60.246 36.617 -23.648 1.00 9.28  ? 398  GLU A CA  1 
ATOM   3228 C C   . GLU A 1 398 ? 61.111 35.646 -24.467 1.00 10.28 ? 398  GLU A C   1 
ATOM   3229 O O   . GLU A 1 398 ? 61.079 35.602 -25.701 1.00 8.77  ? 398  GLU A O   1 
ATOM   3230 C CB  . GLU A 1 398 ? 59.167 37.281 -24.500 1.00 10.49 ? 398  GLU A CB  1 
ATOM   3231 C CG  . GLU A 1 398 ? 58.205 36.347 -25.283 1.00 12.42 ? 398  GLU A CG  1 
ATOM   3232 C CD  . GLU A 1 398 ? 57.457 35.331 -24.419 1.00 15.99 ? 398  GLU A CD  1 
ATOM   3233 O OE1 . GLU A 1 398 ? 57.393 35.489 -23.177 1.00 12.95 ? 398  GLU A OE1 1 
ATOM   3234 O OE2 . GLU A 1 398 ? 56.896 34.373 -25.001 1.00 20.72 ? 398  GLU A OE2 1 
ATOM   3235 N N   . TRP A 1 399 ? 61.908 34.853 -23.738 1.00 9.22  ? 399  TRP A N   1 
ATOM   3236 C CA  . TRP A 1 399 ? 62.723 33.749 -24.270 1.00 10.56 ? 399  TRP A CA  1 
ATOM   3237 C C   . TRP A 1 399 ? 63.474 34.193 -25.545 1.00 9.92  ? 399  TRP A C   1 
ATOM   3238 O O   . TRP A 1 399 ? 64.252 35.156 -25.424 1.00 10.57 ? 399  TRP A O   1 
ATOM   3239 C CB  . TRP A 1 399 ? 61.817 32.510 -24.366 1.00 8.73  ? 399  TRP A CB  1 
ATOM   3240 C CG  . TRP A 1 399 ? 61.199 32.161 -23.031 1.00 8.35  ? 399  TRP A CG  1 
ATOM   3241 C CD1 . TRP A 1 399 ? 59.866 32.199 -22.703 1.00 7.94  ? 399  TRP A CD1 1 
ATOM   3242 C CD2 . TRP A 1 399 ? 61.893 31.745 -21.842 1.00 6.09  ? 399  TRP A CD2 1 
ATOM   3243 N NE1 . TRP A 1 399 ? 59.694 31.825 -21.389 1.00 9.78  ? 399  TRP A NE1 1 
ATOM   3244 C CE2 . TRP A 1 399 ? 60.920 31.551 -20.835 1.00 8.41  ? 399  TRP A CE2 1 
ATOM   3245 C CE3 . TRP A 1 399 ? 63.240 31.513 -21.534 1.00 6.44  ? 399  TRP A CE3 1 
ATOM   3246 C CZ2 . TRP A 1 399 ? 61.253 31.133 -19.540 1.00 8.56  ? 399  TRP A CZ2 1 
ATOM   3247 C CZ3 . TRP A 1 399 ? 63.575 31.102 -20.240 1.00 8.84  ? 399  TRP A CZ3 1 
ATOM   3248 C CH2 . TRP A 1 399 ? 62.587 30.915 -19.266 1.00 9.12  ? 399  TRP A CH2 1 
ATOM   3249 N N   . PRO A 1 400 ? 63.351 33.600 -26.753 1.00 8.21  ? 400  PRO A N   1 
ATOM   3250 C CA  . PRO A 1 400 ? 64.247 34.055 -27.837 1.00 9.24  ? 400  PRO A CA  1 
ATOM   3251 C C   . PRO A 1 400 ? 63.847 35.396 -28.437 1.00 10.73 ? 400  PRO A C   1 
ATOM   3252 O O   . PRO A 1 400 ? 64.579 35.924 -29.287 1.00 10.35 ? 400  PRO A O   1 
ATOM   3253 C CB  . PRO A 1 400 ? 64.125 32.939 -28.882 1.00 9.06  ? 400  PRO A CB  1 
ATOM   3254 C CG  . PRO A 1 400 ? 62.709 32.584 -28.810 1.00 11.03 ? 400  PRO A CG  1 
ATOM   3255 C CD  . PRO A 1 400 ? 62.387 32.620 -27.318 1.00 8.86  ? 400  PRO A CD  1 
ATOM   3256 N N   . MET A 1 401 ? 62.712 35.951 -28.023 1.00 9.63  ? 401  MET A N   1 
ATOM   3257 C CA  . MET A 1 401 ? 62.235 37.238 -28.497 1.00 10.68 ? 401  MET A CA  1 
ATOM   3258 C C   . MET A 1 401 ? 62.783 38.402 -27.677 1.00 12.73 ? 401  MET A C   1 
ATOM   3259 O O   . MET A 1 401 ? 62.615 39.560 -28.081 1.00 11.44 ? 401  MET A O   1 
ATOM   3260 C CB  . MET A 1 401 ? 60.701 37.271 -28.443 1.00 9.18  ? 401  MET A CB  1 
ATOM   3261 C CG  . MET A 1 401 ? 60.013 36.160 -29.235 1.00 14.75 ? 401  MET A CG  1 
ATOM   3262 S SD  . MET A 1 401 ? 60.721 35.888 -30.887 1.00 23.41 ? 401  MET A SD  1 
ATOM   3263 C CE  . MET A 1 401 ? 59.981 37.265 -31.755 1.00 23.28 ? 401  MET A CE  1 
ATOM   3264 N N   . GLY A 1 402 ? 63.408 38.129 -26.525 1.00 8.99  ? 402  GLY A N   1 
ATOM   3265 C CA  . GLY A 1 402 ? 63.903 39.218 -25.702 1.00 10.83 ? 402  GLY A CA  1 
ATOM   3266 C C   . GLY A 1 402 ? 62.746 40.052 -25.176 1.00 10.96 ? 402  GLY A C   1 
ATOM   3267 O O   . GLY A 1 402 ? 61.643 39.547 -24.942 1.00 7.90  ? 402  GLY A O   1 
ATOM   3268 N N   . TYR A 1 403 ? 62.994 41.358 -25.026 1.00 10.04 ? 403  TYR A N   1 
ATOM   3269 C CA  . TYR A 1 403 ? 61.989 42.282 -24.505 1.00 12.53 ? 403  TYR A CA  1 
ATOM   3270 C C   . TYR A 1 403 ? 61.001 42.751 -25.563 1.00 12.80 ? 403  TYR A C   1 
ATOM   3271 O O   . TYR A 1 403 ? 60.067 43.486 -25.228 1.00 12.75 ? 403  TYR A O   1 
ATOM   3272 C CB  . TYR A 1 403 ? 62.664 43.510 -23.858 1.00 11.41 ? 403  TYR A CB  1 
ATOM   3273 C CG  . TYR A 1 403 ? 63.613 43.114 -22.755 1.00 12.15 ? 403  TYR A CG  1 
ATOM   3274 C CD1 . TYR A 1 403 ? 63.138 42.523 -21.585 1.00 11.17 ? 403  TYR A CD1 1 
ATOM   3275 C CD2 . TYR A 1 403 ? 64.988 43.277 -22.905 1.00 11.30 ? 403  TYR A CD2 1 
ATOM   3276 C CE1 . TYR A 1 403 ? 64.016 42.112 -20.574 1.00 10.48 ? 403  TYR A CE1 1 
ATOM   3277 C CE2 . TYR A 1 403 ? 65.873 42.880 -21.904 1.00 11.20 ? 403  TYR A CE2 1 
ATOM   3278 C CZ  . TYR A 1 403 ? 65.380 42.302 -20.742 1.00 9.88  ? 403  TYR A CZ  1 
ATOM   3279 O OH  . TYR A 1 403 ? 66.262 41.892 -19.765 1.00 9.93  ? 403  TYR A OH  1 
ATOM   3280 N N   . SER A 1 404 ? 61.158 42.338 -26.821 1.00 11.14 ? 404  SER A N   1 
ATOM   3281 C CA  . SER A 1 404 ? 60.297 42.882 -27.872 1.00 16.06 ? 404  SER A CA  1 
ATOM   3282 C C   . SER A 1 404 ? 58.819 42.519 -27.687 1.00 13.06 ? 404  SER A C   1 
ATOM   3283 O O   . SER A 1 404 ? 57.952 43.225 -28.215 1.00 13.05 ? 404  SER A O   1 
ATOM   3284 C CB  . SER A 1 404 ? 60.792 42.413 -29.247 1.00 14.60 ? 404  SER A CB  1 
ATOM   3285 O OG  . SER A 1 404 ? 60.696 41.006 -29.394 1.00 15.48 ? 404  SER A OG  1 
ATOM   3286 N N   . MET A 1 405 ? 58.508 41.464 -26.935 1.00 8.63  ? 405  MET A N   1 
ATOM   3287 C CA  . MET A 1 405 ? 57.168 40.924 -26.863 1.00 8.51  ? 405  MET A CA  1 
ATOM   3288 C C   . MET A 1 405 ? 56.716 41.226 -25.435 1.00 9.75  ? 405  MET A C   1 
ATOM   3289 O O   . MET A 1 405 ? 57.270 40.662 -24.483 1.00 10.09 ? 405  MET A O   1 
ATOM   3290 C CB  . MET A 1 405 ? 57.249 39.425 -27.134 1.00 13.55 ? 405  MET A CB  1 
ATOM   3291 C CG  . MET A 1 405 ? 57.228 39.075 -28.629 1.00 12.39 ? 405  MET A CG  1 
ATOM   3292 S SD  . MET A 1 405 ? 56.252 40.034 -29.769 1.00 12.95 ? 405  MET A SD  1 
ATOM   3293 C CE  . MET A 1 405 ? 57.080 39.618 -31.318 1.00 19.31 ? 405  MET A CE  1 
ATOM   3294 N N   . ARG A 1 406 ? 55.785 42.169 -25.261 1.00 7.12  ? 406  ARG A N   1 
ATOM   3295 C CA  . ARG A 1 406 ? 55.491 42.716 -23.938 1.00 8.21  ? 406  ARG A CA  1 
ATOM   3296 C C   . ARG A 1 406 ? 54.143 42.203 -23.428 1.00 8.66  ? 406  ARG A C   1 
ATOM   3297 O O   . ARG A 1 406 ? 53.085 42.630 -23.915 1.00 8.94  ? 406  ARG A O   1 
ATOM   3298 C CB  . ARG A 1 406 ? 55.531 44.250 -23.970 1.00 9.93  ? 406  ARG A CB  1 
ATOM   3299 C CG  . ARG A 1 406 ? 56.974 44.800 -24.001 1.00 8.86  ? 406  ARG A CG  1 
ATOM   3300 C CD  . ARG A 1 406 ? 57.037 46.259 -24.453 1.00 14.06 ? 406  ARG A CD  1 
ATOM   3301 N NE  . ARG A 1 406 ? 58.391 46.815 -24.444 1.00 13.64 ? 406  ARG A NE  1 
ATOM   3302 C CZ  . ARG A 1 406 ? 58.995 47.336 -23.383 1.00 13.47 ? 406  ARG A CZ  1 
ATOM   3303 N NH1 . ARG A 1 406 ? 58.410 47.363 -22.192 1.00 10.28 ? 406  ARG A NH1 1 
ATOM   3304 N NH2 . ARG A 1 406 ? 60.210 47.861 -23.523 1.00 13.05 ? 406  ARG A NH2 1 
ATOM   3305 N N   . PHE A 1 407 ? 54.177 41.325 -22.412 1.00 7.39  ? 407  PHE A N   1 
ATOM   3306 C CA  . PHE A 1 407 ? 52.985 40.632 -21.903 1.00 8.49  ? 407  PHE A CA  1 
ATOM   3307 C C   . PHE A 1 407 ? 52.386 41.261 -20.646 1.00 9.40  ? 407  PHE A C   1 
ATOM   3308 O O   . PHE A 1 407 ? 51.393 40.738 -20.125 1.00 10.28 ? 407  PHE A O   1 
ATOM   3309 C CB  . PHE A 1 407 ? 53.302 39.157 -21.581 1.00 6.95  ? 407  PHE A CB  1 
ATOM   3310 C CG  . PHE A 1 407 ? 53.238 38.244 -22.769 1.00 8.28  ? 407  PHE A CG  1 
ATOM   3311 C CD1 . PHE A 1 407 ? 54.298 38.174 -23.666 1.00 9.41  ? 407  PHE A CD1 1 
ATOM   3312 C CD2 . PHE A 1 407 ? 52.119 37.455 -22.992 1.00 7.18  ? 407  PHE A CD2 1 
ATOM   3313 C CE1 . PHE A 1 407 ? 54.242 37.325 -24.774 1.00 10.46 ? 407  PHE A CE1 1 
ATOM   3314 C CE2 . PHE A 1 407 ? 52.047 36.611 -24.105 1.00 9.60  ? 407  PHE A CE2 1 
ATOM   3315 C CZ  . PHE A 1 407 ? 53.118 36.543 -24.990 1.00 10.20 ? 407  PHE A CZ  1 
ATOM   3316 N N   . GLY A 1 408 ? 52.955 42.346 -20.130 1.00 8.07  ? 408  GLY A N   1 
ATOM   3317 C CA  . GLY A 1 408 ? 52.552 42.822 -18.806 1.00 8.19  ? 408  GLY A CA  1 
ATOM   3318 C C   . GLY A 1 408 ? 51.215 43.562 -18.802 1.00 9.39  ? 408  GLY A C   1 
ATOM   3319 O O   . GLY A 1 408 ? 50.856 44.263 -19.748 1.00 8.11  ? 408  GLY A O   1 
ATOM   3320 N N   . LEU A 1 409 ? 50.470 43.391 -17.708 1.00 8.70  ? 409  LEU A N   1 
ATOM   3321 C CA  . LEU A 1 409 ? 49.456 44.377 -17.347 1.00 8.15  ? 409  LEU A CA  1 
ATOM   3322 C C   . LEU A 1 409 ? 50.091 45.731 -17.062 1.00 8.76  ? 409  LEU A C   1 
ATOM   3323 O O   . LEU A 1 409 ? 49.409 46.762 -17.113 1.00 8.43  ? 409  LEU A O   1 
ATOM   3324 C CB  . LEU A 1 409 ? 48.690 43.899 -16.112 1.00 7.25  ? 409  LEU A CB  1 
ATOM   3325 C CG  . LEU A 1 409 ? 47.851 42.646 -16.354 1.00 7.41  ? 409  LEU A CG  1 
ATOM   3326 C CD1 . LEU A 1 409 ? 47.664 41.815 -15.059 1.00 7.99  ? 409  LEU A CD1 1 
ATOM   3327 C CD2 . LEU A 1 409 ? 46.526 43.042 -16.960 1.00 8.73  ? 409  LEU A CD2 1 
ATOM   3328 N N   . VAL A 1 410 ? 51.388 45.734 -16.761 1.00 7.13  ? 410  VAL A N   1 
ATOM   3329 C CA  . VAL A 1 410 ? 52.146 46.915 -16.382 1.00 7.50  ? 410  VAL A CA  1 
ATOM   3330 C C   . VAL A 1 410 ? 53.359 46.997 -17.297 1.00 9.09  ? 410  VAL A C   1 
ATOM   3331 O O   . VAL A 1 410 ? 54.086 46.010 -17.461 1.00 8.37  ? 410  VAL A O   1 
ATOM   3332 C CB  . VAL A 1 410 ? 52.564 46.842 -14.899 1.00 8.19  ? 410  VAL A CB  1 
ATOM   3333 C CG1 . VAL A 1 410 ? 53.413 48.047 -14.486 1.00 7.90  ? 410  VAL A CG1 1 
ATOM   3334 C CG2 . VAL A 1 410 ? 51.316 46.708 -14.015 1.00 7.40  ? 410  VAL A CG2 1 
ATOM   3335 N N   . ARG A 1 411 ? 53.568 48.164 -17.907 1.00 8.56  ? 411  ARG A N   1 
ATOM   3336 C CA  . ARG A 1 411 ? 54.713 48.370 -18.784 1.00 8.34  ? 411  ARG A CA  1 
ATOM   3337 C C   . ARG A 1 411 ? 55.985 48.580 -17.972 1.00 11.41 ? 411  ARG A C   1 
ATOM   3338 O O   . ARG A 1 411 ? 55.970 49.225 -16.917 1.00 10.30 ? 411  ARG A O   1 
ATOM   3339 C CB  . ARG A 1 411 ? 54.471 49.575 -19.693 1.00 9.16  ? 411  ARG A CB  1 
ATOM   3340 C CG  . ARG A 1 411 ? 55.590 49.824 -20.698 1.00 8.52  ? 411  ARG A CG  1 
ATOM   3341 C CD  . ARG A 1 411 ? 55.164 50.830 -21.782 1.00 8.89  ? 411  ARG A CD  1 
ATOM   3342 N NE  . ARG A 1 411 ? 55.798 50.533 -23.062 1.00 10.48 ? 411  ARG A NE  1 
ATOM   3343 C CZ  . ARG A 1 411 ? 57.066 50.784 -23.361 1.00 11.76 ? 411  ARG A CZ  1 
ATOM   3344 N NH1 . ARG A 1 411 ? 57.867 51.410 -22.515 1.00 11.68 ? 411  ARG A NH1 1 
ATOM   3345 N NH2 . ARG A 1 411 ? 57.540 50.403 -24.546 1.00 13.65 ? 411  ARG A NH2 1 
ATOM   3346 N N   . VAL A 1 412 ? 57.094 48.028 -18.458 1.00 7.82  ? 412  VAL A N   1 
ATOM   3347 C CA  . VAL A 1 412 ? 58.392 48.229 -17.832 1.00 10.26 ? 412  VAL A CA  1 
ATOM   3348 C C   . VAL A 1 412 ? 59.246 49.035 -18.788 1.00 13.57 ? 412  VAL A C   1 
ATOM   3349 O O   . VAL A 1 412 ? 59.407 48.656 -19.953 1.00 12.70 ? 412  VAL A O   1 
ATOM   3350 C CB  . VAL A 1 412 ? 59.091 46.902 -17.487 1.00 10.12 ? 412  VAL A CB  1 
ATOM   3351 C CG1 . VAL A 1 412 ? 60.457 47.199 -16.826 1.00 9.52  ? 412  VAL A CG1 1 
ATOM   3352 C CG2 . VAL A 1 412 ? 58.217 46.060 -16.566 1.00 8.00  ? 412  VAL A CG2 1 
ATOM   3353 N N   . ASP A 1 413 ? 59.794 50.144 -18.305 1.00 12.53 ? 413  ASP A N   1 
ATOM   3354 C CA  . ASP A 1 413 ? 60.923 50.762 -18.987 1.00 14.19 ? 413  ASP A CA  1 
ATOM   3355 C C   . ASP A 1 413 ? 62.177 50.140 -18.390 1.00 11.81 ? 413  ASP A C   1 
ATOM   3356 O O   . ASP A 1 413 ? 62.538 50.434 -17.246 1.00 12.92 ? 413  ASP A O   1 
ATOM   3357 C CB  . ASP A 1 413 ? 60.925 52.277 -18.838 1.00 16.10 ? 413  ASP A CB  1 
ATOM   3358 C CG  . ASP A 1 413 ? 61.899 52.929 -19.789 1.00 25.24 ? 413  ASP A CG  1 
ATOM   3359 O OD1 . ASP A 1 413 ? 63.118 52.741 -19.589 1.00 18.89 ? 413  ASP A OD1 1 
ATOM   3360 O OD2 . ASP A 1 413 ? 61.442 53.554 -20.779 1.00 23.80 ? 413  ASP A OD2 1 
ATOM   3361 N N   . PHE A 1 414 ? 62.824 49.258 -19.153 1.00 10.20 ? 414  PHE A N   1 
ATOM   3362 C CA  . PHE A 1 414 ? 63.877 48.434 -18.566 1.00 16.88 ? 414  PHE A CA  1 
ATOM   3363 C C   . PHE A 1 414 ? 65.117 49.256 -18.247 1.00 17.09 ? 414  PHE A C   1 
ATOM   3364 O O   . PHE A 1 414 ? 65.762 49.020 -17.224 1.00 19.12 ? 414  PHE A O   1 
ATOM   3365 C CB  . PHE A 1 414 ? 64.199 47.259 -19.493 1.00 14.14 ? 414  PHE A CB  1 
ATOM   3366 C CG  . PHE A 1 414 ? 63.095 46.236 -19.550 1.00 13.04 ? 414  PHE A CG  1 
ATOM   3367 C CD1 . PHE A 1 414 ? 62.927 45.328 -18.512 1.00 11.19 ? 414  PHE A CD1 1 
ATOM   3368 C CD2 . PHE A 1 414 ? 62.223 46.192 -20.633 1.00 12.27 ? 414  PHE A CD2 1 
ATOM   3369 C CE1 . PHE A 1 414 ? 61.892 44.393 -18.543 1.00 10.49 ? 414  PHE A CE1 1 
ATOM   3370 C CE2 . PHE A 1 414 ? 61.187 45.259 -20.687 1.00 10.87 ? 414  PHE A CE2 1 
ATOM   3371 C CZ  . PHE A 1 414 ? 61.018 44.361 -19.629 1.00 8.25  ? 414  PHE A CZ  1 
ATOM   3372 N N   . LYS A 1 415 ? 65.423 50.257 -19.068 1.00 13.68 ? 415  LYS A N   1 
ATOM   3373 C CA  . LYS A 1 415 ? 66.569 51.120 -18.801 1.00 18.17 ? 415  LYS A CA  1 
ATOM   3374 C C   . LYS A 1 415 ? 66.346 51.961 -17.545 1.00 25.96 ? 415  LYS A C   1 
ATOM   3375 O O   . LYS A 1 415 ? 67.223 52.040 -16.677 1.00 19.46 ? 415  LYS A O   1 
ATOM   3376 C CB  . LYS A 1 415 ? 66.833 52.003 -20.023 1.00 25.19 ? 415  LYS A CB  1 
ATOM   3377 C CG  . LYS A 1 415 ? 68.067 52.894 -19.920 1.00 38.51 ? 415  LYS A CG  1 
ATOM   3378 C CD  . LYS A 1 415 ? 68.214 53.783 -21.165 1.00 37.05 ? 415  LYS A CD  1 
ATOM   3379 C CE  . LYS A 1 415 ? 69.387 54.754 -21.024 1.00 43.93 ? 415  LYS A CE  1 
ATOM   3380 N NZ  . LYS A 1 415 ? 70.364 54.276 -19.996 1.00 43.04 ? 415  LYS A NZ  1 
ATOM   3381 N N   . GLN A 1 416 ? 65.171 52.577 -17.409 1.00 21.70 ? 416  GLN A N   1 
ATOM   3382 C CA  . GLN A 1 416 ? 64.933 53.438 -16.255 1.00 25.97 ? 416  GLN A CA  1 
ATOM   3383 C C   . GLN A 1 416 ? 64.372 52.688 -15.058 1.00 24.10 ? 416  GLN A C   1 
ATOM   3384 O O   . GLN A 1 416 ? 64.195 53.300 -14.001 1.00 24.90 ? 416  GLN A O   1 
ATOM   3385 C CB  . GLN A 1 416 ? 64.005 54.606 -16.615 1.00 24.89 ? 416  GLN A CB  1 
ATOM   3386 C CG  . GLN A 1 416 ? 64.250 55.222 -17.988 1.00 30.50 ? 416  GLN A CG  1 
ATOM   3387 C CD  . GLN A 1 416 ? 65.579 55.971 -18.063 1.00 45.12 ? 416  GLN A CD  1 
ATOM   3388 O OE1 . GLN A 1 416 ? 66.089 56.469 -17.049 1.00 46.14 ? 416  GLN A OE1 1 
ATOM   3389 N NE2 . GLN A 1 416 ? 66.150 56.048 -19.269 1.00 41.89 ? 416  GLN A NE2 1 
ATOM   3390 N N   . LYS A 1 417 ? 64.115 51.384 -15.198 1.00 20.58 ? 417  LYS A N   1 
ATOM   3391 C CA  . LYS A 1 417 ? 63.568 50.538 -14.134 1.00 17.97 ? 417  LYS A CA  1 
ATOM   3392 C C   . LYS A 1 417 ? 62.250 51.109 -13.590 1.00 23.59 ? 417  LYS A C   1 
ATOM   3393 O O   . LYS A 1 417 ? 62.024 51.189 -12.382 1.00 23.72 ? 417  LYS A O   1 
ATOM   3394 C CB  . LYS A 1 417 ? 64.594 50.323 -13.016 1.00 24.57 ? 417  LYS A CB  1 
ATOM   3395 C CG  . LYS A 1 417 ? 65.958 49.805 -13.502 1.00 26.77 ? 417  LYS A CG  1 
ATOM   3396 C CD  . LYS A 1 417 ? 65.871 48.387 -14.103 1.00 29.02 ? 417  LYS A CD  1 
ATOM   3397 C CE  . LYS A 1 417 ? 67.267 47.842 -14.445 1.00 23.31 ? 417  LYS A CE  1 
ATOM   3398 N NZ  . LYS A 1 417 ? 67.349 47.102 -15.753 1.00 16.74 ? 417  LYS A NZ  1 
ATOM   3399 N N   . LEU A 1 418 ? 61.367 51.482 -14.510 1.00 20.15 ? 418  LEU A N   1 
ATOM   3400 C CA  . LEU A 1 418 ? 60.107 52.152 -14.211 1.00 19.60 ? 418  LEU A CA  1 
ATOM   3401 C C   . LEU A 1 418 ? 58.932 51.242 -14.546 1.00 13.29 ? 418  LEU A C   1 
ATOM   3402 O O   . LEU A 1 418 ? 58.900 50.633 -15.617 1.00 12.22 ? 418  LEU A O   1 
ATOM   3403 C CB  . LEU A 1 418 ? 60.005 53.442 -15.028 1.00 19.96 ? 418  LEU A CB  1 
ATOM   3404 C CG  . LEU A 1 418 ? 58.734 54.289 -14.984 1.00 20.46 ? 418  LEU A CG  1 
ATOM   3405 C CD1 . LEU A 1 418 ? 58.449 54.810 -13.569 1.00 20.57 ? 418  LEU A CD1 1 
ATOM   3406 C CD2 . LEU A 1 418 ? 58.826 55.433 -16.013 1.00 21.30 ? 418  LEU A CD2 1 
ATOM   3407 N N   . PHE A 1 419 ? 57.953 51.171 -13.645 1.00 12.42 ? 419  PHE A N   1 
ATOM   3408 C CA  . PHE A 1 419 ? 56.729 50.391 -13.830 1.00 13.96 ? 419  PHE A CA  1 
ATOM   3409 C C   . PHE A 1 419 ? 55.552 51.336 -14.058 1.00 13.88 ? 419  PHE A C   1 
ATOM   3410 O O   . PHE A 1 419 ? 55.295 52.210 -13.223 1.00 10.63 ? 419  PHE A O   1 
ATOM   3411 C CB  . PHE A 1 419 ? 56.432 49.540 -12.590 1.00 10.70 ? 419  PHE A CB  1 
ATOM   3412 C CG  . PHE A 1 419 ? 57.463 48.474 -12.291 1.00 13.90 ? 419  PHE A CG  1 
ATOM   3413 C CD1 . PHE A 1 419 ? 58.336 48.022 -13.265 1.00 15.46 ? 419  PHE A CD1 1 
ATOM   3414 C CD2 . PHE A 1 419 ? 57.606 47.989 -10.996 1.00 16.40 ? 419  PHE A CD2 1 
ATOM   3415 C CE1 . PHE A 1 419 ? 59.290 47.050 -12.970 1.00 19.25 ? 419  PHE A CE1 1 
ATOM   3416 C CE2 . PHE A 1 419 ? 58.564 47.016 -10.696 1.00 17.96 ? 419  PHE A CE2 1 
ATOM   3417 C CZ  . PHE A 1 419 ? 59.403 46.551 -11.680 1.00 14.68 ? 419  PHE A CZ  1 
ATOM   3418 N N   . THR A 1 420 ? 54.821 51.147 -15.151 1.00 9.60  ? 420  THR A N   1 
ATOM   3419 C CA  . THR A 1 420 ? 53.657 51.986 -15.463 1.00 10.32 ? 420  THR A CA  1 
ATOM   3420 C C   . THR A 1 420 ? 52.453 51.135 -15.854 1.00 8.26  ? 420  THR A C   1 
ATOM   3421 O O   . THR A 1 420 ? 52.431 50.577 -16.970 1.00 7.95  ? 420  THR A O   1 
ATOM   3422 C CB  . THR A 1 420 ? 53.969 52.968 -16.593 1.00 11.12 ? 420  THR A CB  1 
ATOM   3423 O OG1 . THR A 1 420 ? 55.166 53.710 -16.302 1.00 10.20 ? 420  THR A OG1 1 
ATOM   3424 C CG2 . THR A 1 420 ? 52.801 53.934 -16.789 1.00 9.91  ? 420  THR A CG2 1 
ATOM   3425 N N   . PRO A 1 421 ? 51.424 51.035 -15.018 1.00 8.43  ? 421  PRO A N   1 
ATOM   3426 C CA  . PRO A 1 421 ? 50.263 50.205 -15.380 1.00 8.78  ? 421  PRO A CA  1 
ATOM   3427 C C   . PRO A 1 421 ? 49.583 50.660 -16.669 1.00 10.36 ? 421  PRO A C   1 
ATOM   3428 O O   . PRO A 1 421 ? 49.400 51.854 -16.915 1.00 9.22  ? 421  PRO A O   1 
ATOM   3429 C CB  . PRO A 1 421 ? 49.333 50.356 -14.172 1.00 9.77  ? 421  PRO A CB  1 
ATOM   3430 C CG  . PRO A 1 421 ? 50.295 50.680 -13.013 1.00 12.64 ? 421  PRO A CG  1 
ATOM   3431 C CD  . PRO A 1 421 ? 51.359 51.527 -13.629 1.00 9.24  ? 421  PRO A CD  1 
ATOM   3432 N N   . ARG A 1 422 ? 49.221 49.684 -17.498 1.00 7.58  ? 422  ARG A N   1 
ATOM   3433 C CA  . ARG A 1 422 ? 48.406 49.934 -18.681 1.00 8.65  ? 422  ARG A CA  1 
ATOM   3434 C C   . ARG A 1 422 ? 46.940 49.958 -18.272 1.00 8.11  ? 422  ARG A C   1 
ATOM   3435 O O   . ARG A 1 422 ? 46.598 49.524 -17.172 1.00 9.45  ? 422  ARG A O   1 
ATOM   3436 C CB  . ARG A 1 422 ? 48.636 48.851 -19.732 1.00 7.50  ? 422  ARG A CB  1 
ATOM   3437 C CG  . ARG A 1 422 ? 50.080 48.741 -20.220 1.00 7.94  ? 422  ARG A CG  1 
ATOM   3438 C CD  . ARG A 1 422 ? 50.237 47.590 -21.232 1.00 7.75  ? 422  ARG A CD  1 
ATOM   3439 N NE  . ARG A 1 422 ? 51.513 47.653 -21.951 1.00 8.28  ? 422  ARG A NE  1 
ATOM   3440 C CZ  . ARG A 1 422 ? 52.622 47.020 -21.576 1.00 11.60 ? 422  ARG A CZ  1 
ATOM   3441 N NH1 . ARG A 1 422 ? 52.640 46.213 -20.522 1.00 8.23  ? 422  ARG A NH1 1 
ATOM   3442 N NH2 . ARG A 1 422 ? 53.747 47.218 -22.262 1.00 7.44  ? 422  ARG A NH2 1 
ATOM   3443 N N   . PRO A 1 423 ? 46.048 50.471 -19.126 1.00 8.78  ? 423  PRO A N   1 
ATOM   3444 C CA  . PRO A 1 423 ? 44.633 50.531 -18.725 1.00 10.16 ? 423  PRO A CA  1 
ATOM   3445 C C   . PRO A 1 423 ? 44.044 49.169 -18.408 1.00 9.72  ? 423  PRO A C   1 
ATOM   3446 O O   . PRO A 1 423 ? 43.159 49.080 -17.552 1.00 8.74  ? 423  PRO A O   1 
ATOM   3447 C CB  . PRO A 1 423 ? 43.953 51.184 -19.937 1.00 8.55  ? 423  PRO A CB  1 
ATOM   3448 C CG  . PRO A 1 423 ? 45.014 52.045 -20.516 1.00 10.34 ? 423  PRO A CG  1 
ATOM   3449 C CD  . PRO A 1 423 ? 46.298 51.250 -20.355 1.00 9.87  ? 423  PRO A CD  1 
ATOM   3450 N N   . SER A 1 424 ? 44.526 48.100 -19.051 1.00 8.90  ? 424  SER A N   1 
ATOM   3451 C CA  . SER A 1 424 ? 44.038 46.758 -18.724 1.00 10.03 ? 424  SER A CA  1 
ATOM   3452 C C   . SER A 1 424 ? 44.280 46.399 -17.256 1.00 7.59  ? 424  SER A C   1 
ATOM   3453 O O   . SER A 1 424 ? 43.546 45.580 -16.688 1.00 9.52  ? 424  SER A O   1 
ATOM   3454 C CB  . SER A 1 424 ? 44.698 45.716 -19.644 1.00 8.68  ? 424  SER A CB  1 
ATOM   3455 O OG  . SER A 1 424 ? 46.121 45.833 -19.614 1.00 7.34  ? 424  SER A OG  1 
ATOM   3456 N N   . TYR A 1 425 ? 45.319 46.968 -16.634 1.00 7.52  ? 425  TYR A N   1 
ATOM   3457 C CA  . TYR A 1 425 ? 45.555 46.743 -15.207 1.00 7.59  ? 425  TYR A CA  1 
ATOM   3458 C C   . TYR A 1 425 ? 44.390 47.269 -14.378 1.00 9.25  ? 425  TYR A C   1 
ATOM   3459 O O   . TYR A 1 425 ? 43.887 46.586 -13.480 1.00 7.84  ? 425  TYR A O   1 
ATOM   3460 C CB  . TYR A 1 425 ? 46.867 47.414 -14.792 1.00 6.77  ? 425  TYR A CB  1 
ATOM   3461 C CG  . TYR A 1 425 ? 47.158 47.491 -13.293 1.00 8.69  ? 425  TYR A CG  1 
ATOM   3462 C CD1 . TYR A 1 425 ? 47.841 46.460 -12.640 1.00 8.39  ? 425  TYR A CD1 1 
ATOM   3463 C CD2 . TYR A 1 425 ? 46.812 48.623 -12.553 1.00 9.36  ? 425  TYR A CD2 1 
ATOM   3464 C CE1 . TYR A 1 425 ? 48.143 46.541 -11.275 1.00 10.40 ? 425  TYR A CE1 1 
ATOM   3465 C CE2 . TYR A 1 425 ? 47.111 48.723 -11.189 1.00 10.88 ? 425  TYR A CE2 1 
ATOM   3466 C CZ  . TYR A 1 425 ? 47.770 47.678 -10.557 1.00 11.34 ? 425  TYR A CZ  1 
ATOM   3467 O OH  . TYR A 1 425 ? 48.054 47.784 -9.214  1.00 11.43 ? 425  TYR A OH  1 
ATOM   3468 N N   . TYR A 1 426 ? 43.932 48.489 -14.680 1.00 9.52  ? 426  TYR A N   1 
ATOM   3469 C CA  . TYR A 1 426 ? 42.793 49.045 -13.951 1.00 9.62  ? 426  TYR A CA  1 
ATOM   3470 C C   . TYR A 1 426 ? 41.507 48.284 -14.258 1.00 11.21 ? 426  TYR A C   1 
ATOM   3471 O O   . TYR A 1 426 ? 40.658 48.132 -13.375 1.00 10.21 ? 426  TYR A O   1 
ATOM   3472 C CB  . TYR A 1 426 ? 42.649 50.535 -14.275 1.00 8.57  ? 426  TYR A CB  1 
ATOM   3473 C CG  . TYR A 1 426 ? 43.916 51.310 -13.961 1.00 10.52 ? 426  TYR A CG  1 
ATOM   3474 C CD1 . TYR A 1 426 ? 44.379 51.421 -12.653 1.00 10.70 ? 426  TYR A CD1 1 
ATOM   3475 C CD2 . TYR A 1 426 ? 44.670 51.890 -14.974 1.00 12.54 ? 426  TYR A CD2 1 
ATOM   3476 C CE1 . TYR A 1 426 ? 45.556 52.108 -12.361 1.00 11.46 ? 426  TYR A CE1 1 
ATOM   3477 C CE2 . TYR A 1 426 ? 45.847 52.578 -14.692 1.00 14.21 ? 426  TYR A CE2 1 
ATOM   3478 C CZ  . TYR A 1 426 ? 46.279 52.680 -13.385 1.00 15.77 ? 426  TYR A CZ  1 
ATOM   3479 O OH  . TYR A 1 426 ? 47.443 53.357 -13.108 1.00 16.49 ? 426  TYR A OH  1 
ATOM   3480 N N   . LEU A 1 427 ? 41.349 47.782 -15.488 1.00 7.75  ? 427  LEU A N   1 
ATOM   3481 C CA  . LEU A 1 427 ? 40.161 46.993 -15.801 1.00 10.13 ? 427  LEU A CA  1 
ATOM   3482 C C   . LEU A 1 427 ? 40.146 45.686 -15.007 1.00 10.46 ? 427  LEU A C   1 
ATOM   3483 O O   . LEU A 1 427 ? 39.106 45.296 -14.459 1.00 10.86 ? 427  LEU A O   1 
ATOM   3484 C CB  . LEU A 1 427 ? 40.082 46.724 -17.313 1.00 8.17  ? 427  LEU A CB  1 
ATOM   3485 C CG  . LEU A 1 427 ? 38.928 45.802 -17.733 1.00 10.81 ? 427  LEU A CG  1 
ATOM   3486 C CD1 . LEU A 1 427 ? 37.584 46.461 -17.475 1.00 11.54 ? 427  LEU A CD1 1 
ATOM   3487 C CD2 . LEU A 1 427 ? 39.048 45.378 -19.207 1.00 11.17 ? 427  LEU A CD2 1 
ATOM   3488 N N   . PHE A 1 428 ? 41.292 45.001 -14.925 1.00 9.08  ? 428  PHE A N   1 
ATOM   3489 C CA  . PHE A 1 428 ? 41.384 43.784 -14.117 1.00 9.61  ? 428  PHE A CA  1 
ATOM   3490 C C   . PHE A 1 428 ? 40.968 44.061 -12.673 1.00 9.13  ? 428  PHE A C   1 
ATOM   3491 O O   . PHE A 1 428 ? 40.178 43.310 -12.084 1.00 10.20 ? 428  PHE A O   1 
ATOM   3492 C CB  . PHE A 1 428 ? 42.814 43.228 -14.187 1.00 8.02  ? 428  PHE A CB  1 
ATOM   3493 C CG  . PHE A 1 428 ? 42.939 41.750 -13.828 1.00 13.87 ? 428  PHE A CG  1 
ATOM   3494 C CD1 . PHE A 1 428 ? 41.829 40.968 -13.555 1.00 11.24 ? 428  PHE A CD1 1 
ATOM   3495 C CD2 . PHE A 1 428 ? 44.184 41.155 -13.755 1.00 16.96 ? 428  PHE A CD2 1 
ATOM   3496 C CE1 . PHE A 1 428 ? 41.960 39.609 -13.218 1.00 11.27 ? 428  PHE A CE1 1 
ATOM   3497 C CE2 . PHE A 1 428 ? 44.316 39.799 -13.437 1.00 17.98 ? 428  PHE A CE2 1 
ATOM   3498 C CZ  . PHE A 1 428 ? 43.203 39.033 -13.157 1.00 10.89 ? 428  PHE A CZ  1 
ATOM   3499 N N   . GLY A 1 429 ? 41.468 45.156 -12.092 1.00 10.25 ? 429  GLY A N   1 
ATOM   3500 C CA  . GLY A 1 429 ? 41.040 45.527 -10.746 1.00 10.65 ? 429  GLY A CA  1 
ATOM   3501 C C   . GLY A 1 429 ? 39.531 45.681 -10.616 1.00 11.87 ? 429  GLY A C   1 
ATOM   3502 O O   . GLY A 1 429 ? 38.938 45.262 -9.619  1.00 10.50 ? 429  GLY A O   1 
ATOM   3503 N N   . GLN A 1 430 ? 38.890 46.290 -11.620 1.00 10.51 ? 430  GLN A N   1 
ATOM   3504 C CA  . GLN A 1 430 ? 37.441 46.481 -11.564 1.00 12.93 ? 430  GLN A CA  1 
ATOM   3505 C C   . GLN A 1 430 ? 36.705 45.150 -11.657 1.00 14.71 ? 430  GLN A C   1 
ATOM   3506 O O   . GLN A 1 430 ? 35.695 44.947 -10.971 1.00 12.11 ? 430  GLN A O   1 
ATOM   3507 C CB  . GLN A 1 430 ? 36.981 47.417 -12.686 1.00 10.51 ? 430  GLN A CB  1 
ATOM   3508 C CG  . GLN A 1 430 ? 37.469 48.855 -12.563 1.00 11.75 ? 430  GLN A CG  1 
ATOM   3509 C CD  . GLN A 1 430 ? 36.901 49.572 -11.334 1.00 18.10 ? 430  GLN A CD  1 
ATOM   3510 O OE1 . GLN A 1 430 ? 35.803 49.269 -10.863 1.00 17.74 ? 430  GLN A OE1 1 
ATOM   3511 N NE2 . GLN A 1 430 ? 37.655 50.524 -10.815 1.00 19.56 ? 430  GLN A NE2 1 
ATOM   3512 N N   . ILE A 1 431 ? 37.190 44.230 -12.501 1.00 10.56 ? 431  ILE A N   1 
ATOM   3513 C CA  . ILE A 1 431 ? 36.546 42.921 -12.590 1.00 11.41 ? 431  ILE A CA  1 
ATOM   3514 C C   . ILE A 1 431 ? 36.707 42.164 -11.278 1.00 11.41 ? 431  ILE A C   1 
ATOM   3515 O O   . ILE A 1 431 ? 35.753 41.564 -10.773 1.00 11.78 ? 431  ILE A O   1 
ATOM   3516 C CB  . ILE A 1 431 ? 37.094 42.108 -13.779 1.00 10.81 ? 431  ILE A CB  1 
ATOM   3517 C CG1 . ILE A 1 431 ? 36.790 42.813 -15.103 1.00 10.36 ? 431  ILE A CG1 1 
ATOM   3518 C CG2 . ILE A 1 431 ? 36.486 40.696 -13.784 1.00 11.91 ? 431  ILE A CG2 1 
ATOM   3519 C CD1 . ILE A 1 431 ? 37.640 42.289 -16.245 1.00 11.92 ? 431  ILE A CD1 1 
ATOM   3520 N N   . ILE A 1 432 ? 37.909 42.191 -10.703 1.00 9.49  ? 432  ILE A N   1 
ATOM   3521 C CA  . ILE A 1 432 ? 38.139 41.539 -9.416  1.00 12.80 ? 432  ILE A CA  1 
ATOM   3522 C C   . ILE A 1 432 ? 37.226 42.130 -8.344  1.00 13.62 ? 432  ILE A C   1 
ATOM   3523 O O   . ILE A 1 432 ? 36.633 41.400 -7.537  1.00 15.42 ? 432  ILE A O   1 
ATOM   3524 C CB  . ILE A 1 432 ? 39.625 41.664 -9.021  1.00 9.07  ? 432  ILE A CB  1 
ATOM   3525 C CG1 . ILE A 1 432 ? 40.509 40.827 -9.949  1.00 10.06 ? 432  ILE A CG1 1 
ATOM   3526 C CG2 . ILE A 1 432 ? 39.828 41.261 -7.566  1.00 15.35 ? 432  ILE A CG2 1 
ATOM   3527 C CD1 . ILE A 1 432 ? 41.984 41.069 -9.759  1.00 10.63 ? 432  ILE A CD1 1 
ATOM   3528 N N   . ASN A 1 433 ? 37.096 43.445 -8.327  1.00 13.33 ? 433  ASN A N   1 
ATOM   3529 C CA  . ASN A 1 433 ? 36.253 44.122 -7.314  1.00 16.47 ? 433  ASN A CA  1 
ATOM   3530 C C   . ASN A 1 433 ? 34.793 43.659 -7.427  1.00 19.99 ? 433  ASN A C   1 
ATOM   3531 O O   . ASN A 1 433 ? 34.162 43.455 -6.403  1.00 16.59 ? 433  ASN A O   1 
ATOM   3532 C CB  . ASN A 1 433 ? 36.314 45.633 -7.483  1.00 17.63 ? 433  ASN A CB  1 
ATOM   3533 C CG  . ASN A 1 433 ? 35.425 46.356 -6.496  1.00 24.03 ? 433  ASN A CG  1 
ATOM   3534 O OD1 . ASN A 1 433 ? 35.719 46.389 -5.308  1.00 26.91 ? 433  ASN A OD1 1 
ATOM   3535 N ND2 . ASN A 1 433 ? 34.331 46.917 -6.977  1.00 22.49 ? 433  ASN A ND2 1 
ATOM   3536 N N   . SER A 1 434 ? 34.292 43.541 -8.653  1.00 16.30 ? 434  SER A N   1 
ATOM   3537 C CA  . SER A 1 434 ? 32.878 43.165 -8.894  1.00 16.05 ? 434  SER A CA  1 
ATOM   3538 C C   . SER A 1 434 ? 32.670 41.646 -8.706  1.00 14.15 ? 434  SER A C   1 
ATOM   3539 O O   . SER A 1 434 ? 31.537 41.224 -8.544  1.00 14.18 ? 434  SER A O   1 
ATOM   3540 C CB  . SER A 1 434 ? 32.443 43.663 -10.266 1.00 16.41 ? 434  SER A CB  1 
ATOM   3541 O OG  . SER A 1 434 ? 32.571 45.060 -10.411 1.00 21.68 ? 434  SER A OG  1 
ATOM   3542 N N   . ARG A 1 435 ? 33.746 40.867 -8.783  1.00 11.47 ? 435  ARG A N   1 
ATOM   3543 C CA  . ARG A 1 435 ? 33.646 39.387 -8.675  1.00 14.97 ? 435  ARG A CA  1 
ATOM   3544 C C   . ARG A 1 435 ? 32.746 38.801 -9.781  1.00 17.61 ? 435  ARG A C   1 
ATOM   3545 O O   . ARG A 1 435 ? 32.201 37.726 -9.570  1.00 14.50 ? 435  ARG A O   1 
ATOM   3546 C CB  . ARG A 1 435 ? 33.239 38.977 -7.252  1.00 20.91 ? 435  ARG A CB  1 
ATOM   3547 N N   . THR A 1 436 ? 32.644 39.480 -10.929 1.00 12.48 ? 436  THR A N   1 
ATOM   3548 C CA  . THR A 1 436 ? 31.901 38.953 -12.100 1.00 12.21 ? 436  THR A CA  1 
ATOM   3549 C C   . THR A 1 436 ? 32.213 39.818 -13.318 1.00 14.47 ? 436  THR A C   1 
ATOM   3550 O O   . THR A 1 436 ? 32.470 41.000 -13.150 1.00 12.18 ? 436  THR A O   1 
ATOM   3551 C CB  . THR A 1 436 ? 30.372 38.930 -11.928 1.00 17.09 ? 436  THR A CB  1 
ATOM   3552 O OG1 . THR A 1 436 ? 29.741 38.565 -13.154 1.00 15.60 ? 436  THR A OG1 1 
ATOM   3553 C CG2 . THR A 1 436 ? 29.827 40.253 -11.433 1.00 14.67 ? 436  THR A CG2 1 
ATOM   3554 N N   . THR A 1 437 ? 32.164 39.213 -14.490 1.00 11.99 ? 437  THR A N   1 
ATOM   3555 C CA  . THR A 1 437 ? 32.340 39.964 -15.725 1.00 13.06 ? 437  THR A CA  1 
ATOM   3556 C C   . THR A 1 437 ? 31.036 40.567 -16.236 1.00 14.22 ? 437  THR A C   1 
ATOM   3557 O O   . THR A 1 437 ? 31.070 41.369 -17.173 1.00 11.56 ? 437  THR A O   1 
ATOM   3558 C CB  . THR A 1 437 ? 32.940 39.069 -16.813 1.00 12.44 ? 437  THR A CB  1 
ATOM   3559 O OG1 . THR A 1 437 ? 32.042 37.986 -17.071 1.00 13.33 ? 437  THR A OG1 1 
ATOM   3560 C CG2 . THR A 1 437 ? 34.304 38.504 -16.373 1.00 9.52  ? 437  THR A CG2 1 
ATOM   3561 N N   . GLU A 1 438 ? 29.901 40.215 -15.631 1.00 16.56 ? 438  GLU A N   1 
ATOM   3562 C CA  . GLU A 1 438 ? 28.596 40.628 -16.149 1.00 17.06 ? 438  GLU A CA  1 
ATOM   3563 C C   . GLU A 1 438 ? 28.466 42.135 -16.393 1.00 14.53 ? 438  GLU A C   1 
ATOM   3564 O O   . GLU A 1 438 ? 27.934 42.507 -17.451 1.00 17.18 ? 438  GLU A O   1 
ATOM   3565 C CB  . GLU A 1 438 ? 27.500 40.105 -15.196 1.00 17.46 ? 438  GLU A CB  1 
ATOM   3566 C CG  . GLU A 1 438 ? 26.039 40.290 -15.683 1.00 28.44 ? 438  GLU A CG  1 
ATOM   3567 C CD  . GLU A 1 438 ? 25.491 41.719 -15.540 1.00 35.87 ? 438  GLU A CD  1 
ATOM   3568 O OE1 . GLU A 1 438 ? 26.077 42.538 -14.794 1.00 36.24 ? 438  GLU A OE1 1 
ATOM   3569 O OE2 . GLU A 1 438 ? 24.466 42.027 -16.199 1.00 46.51 ? 438  GLU A OE2 1 
ATOM   3570 N N   . PRO A 1 439 ? 28.904 43.038 -15.503 1.00 14.51 ? 439  PRO A N   1 
ATOM   3571 C CA  . PRO A 1 439 ? 28.776 44.478 -15.797 1.00 14.78 ? 439  PRO A CA  1 
ATOM   3572 C C   . PRO A 1 439 ? 29.709 44.995 -16.888 1.00 15.93 ? 439  PRO A C   1 
ATOM   3573 O O   . PRO A 1 439 ? 29.687 46.202 -17.165 1.00 13.82 ? 439  PRO A O   1 
ATOM   3574 C CB  . PRO A 1 439 ? 29.132 45.156 -14.460 1.00 17.18 ? 439  PRO A CB  1 
ATOM   3575 C CG  . PRO A 1 439 ? 29.328 44.081 -13.464 1.00 18.41 ? 439  PRO A CG  1 
ATOM   3576 C CD  . PRO A 1 439 ? 29.514 42.796 -14.181 1.00 14.20 ? 439  PRO A CD  1 
ATOM   3577 N N   . PHE A 1 440 ? 30.560 44.150 -17.477 1.00 12.39 ? 440  PHE A N   1 
ATOM   3578 C CA  . PHE A 1 440 ? 31.561 44.584 -18.445 1.00 10.81 ? 440  PHE A CA  1 
ATOM   3579 C C   . PHE A 1 440 ? 31.318 44.018 -19.837 1.00 12.36 ? 440  PHE A C   1 
ATOM   3580 O O   . PHE A 1 440 ? 31.953 44.475 -20.797 1.00 11.95 ? 440  PHE A O   1 
ATOM   3581 C CB  . PHE A 1 440 ? 32.972 44.172 -17.971 1.00 13.06 ? 440  PHE A CB  1 
ATOM   3582 C CG  . PHE A 1 440 ? 33.300 44.615 -16.555 1.00 13.59 ? 440  PHE A CG  1 
ATOM   3583 C CD1 . PHE A 1 440 ? 33.892 45.848 -16.314 1.00 12.35 ? 440  PHE A CD1 1 
ATOM   3584 C CD2 . PHE A 1 440 ? 32.992 43.802 -15.469 1.00 12.90 ? 440  PHE A CD2 1 
ATOM   3585 C CE1 . PHE A 1 440 ? 34.189 46.257 -15.013 1.00 12.64 ? 440  PHE A CE1 1 
ATOM   3586 C CE2 . PHE A 1 440 ? 33.273 44.205 -14.162 1.00 10.82 ? 440  PHE A CE2 1 
ATOM   3587 C CZ  . PHE A 1 440 ? 33.878 45.436 -13.932 1.00 12.47 ? 440  PHE A CZ  1 
ATOM   3588 N N   . LEU A 1 441 ? 30.396 43.067 -19.971 1.00 12.35 ? 441  LEU A N   1 
ATOM   3589 C CA  . LEU A 1 441 ? 30.262 42.277 -21.190 1.00 14.22 ? 441  LEU A CA  1 
ATOM   3590 C C   . LEU A 1 441 ? 29.965 43.125 -22.420 1.00 12.71 ? 441  LEU A C   1 
ATOM   3591 O O   . LEU A 1 441 ? 30.306 42.720 -23.534 1.00 11.56 ? 441  LEU A O   1 
ATOM   3592 C CB  . LEU A 1 441 ? 29.153 41.240 -20.998 1.00 14.66 ? 441  LEU A CB  1 
ATOM   3593 C CG  . LEU A 1 441 ? 29.449 40.147 -19.968 1.00 17.90 ? 441  LEU A CG  1 
ATOM   3594 C CD1 . LEU A 1 441 ? 28.383 39.073 -20.026 1.00 18.68 ? 441  LEU A CD1 1 
ATOM   3595 C CD2 . LEU A 1 441 ? 30.825 39.541 -20.218 1.00 15.52 ? 441  LEU A CD2 1 
ATOM   3596 N N   . ASN A 1 442 ? 29.303 44.276 -22.258 1.00 11.46 ? 442  ASN A N   1 
ATOM   3597 C CA  . ASN A 1 442 ? 28.932 45.054 -23.441 1.00 12.05 ? 442  ASN A CA  1 
ATOM   3598 C C   . ASN A 1 442 ? 30.152 45.538 -24.216 1.00 9.69  ? 442  ASN A C   1 
ATOM   3599 O O   . ASN A 1 442 ? 30.055 45.782 -25.427 1.00 10.77 ? 442  ASN A O   1 
ATOM   3600 C CB  . ASN A 1 442 ? 28.079 46.268 -23.069 1.00 12.03 ? 442  ASN A CB  1 
ATOM   3601 C CG  . ASN A 1 442 ? 27.313 46.819 -24.275 1.00 16.37 ? 442  ASN A CG  1 
ATOM   3602 O OD1 . ASN A 1 442 ? 27.447 47.994 -24.628 1.00 13.28 ? 442  ASN A OD1 1 
ATOM   3603 N ND2 . ASN A 1 442 ? 26.469 45.982 -24.875 1.00 12.55 ? 442  ASN A ND2 1 
ATOM   3604 N N   . LEU A 1 443 ? 31.298 45.709 -23.539 1.00 8.21  ? 443  LEU A N   1 
ATOM   3605 C CA  . LEU A 1 443 ? 32.526 46.111 -24.231 1.00 10.31 ? 443  LEU A CA  1 
ATOM   3606 C C   . LEU A 1 443 ? 32.897 45.126 -25.331 1.00 14.76 ? 443  LEU A C   1 
ATOM   3607 O O   . LEU A 1 443 ? 33.514 45.513 -26.335 1.00 12.55 ? 443  LEU A O   1 
ATOM   3608 C CB  . LEU A 1 443 ? 33.694 46.233 -23.244 1.00 10.90 ? 443  LEU A CB  1 
ATOM   3609 C CG  . LEU A 1 443 ? 33.572 47.300 -22.148 1.00 13.19 ? 443  LEU A CG  1 
ATOM   3610 C CD1 . LEU A 1 443 ? 34.832 47.360 -21.294 1.00 13.45 ? 443  LEU A CD1 1 
ATOM   3611 C CD2 . LEU A 1 443 ? 33.239 48.680 -22.754 1.00 9.96  ? 443  LEU A CD2 1 
ATOM   3612 N N   . LEU A 1 444 ? 32.543 43.852 -25.148 1.00 10.95 ? 444  LEU A N   1 
ATOM   3613 C CA  . LEU A 1 444 ? 32.894 42.818 -26.109 1.00 15.38 ? 444  LEU A CA  1 
ATOM   3614 C C   . LEU A 1 444 ? 32.194 43.049 -27.437 1.00 16.64 ? 444  LEU A C   1 
ATOM   3615 O O   . LEU A 1 444 ? 32.672 42.589 -28.478 1.00 15.54 ? 444  LEU A O   1 
ATOM   3616 C CB  . LEU A 1 444 ? 32.508 41.455 -25.535 1.00 13.89 ? 444  LEU A CB  1 
ATOM   3617 C CG  . LEU A 1 444 ? 33.335 41.039 -24.315 1.00 16.14 ? 444  LEU A CG  1 
ATOM   3618 C CD1 . LEU A 1 444 ? 33.051 39.601 -23.968 1.00 17.15 ? 444  LEU A CD1 1 
ATOM   3619 C CD2 . LEU A 1 444 ? 34.829 41.233 -24.578 1.00 13.20 ? 444  LEU A CD2 1 
ATOM   3620 N N   . LYS A 1 445 ? 31.059 43.757 -27.421 1.00 12.54 ? 445  LYS A N   1 
ATOM   3621 C CA  . LYS A 1 445 ? 30.316 43.976 -28.653 1.00 13.00 ? 445  LYS A CA  1 
ATOM   3622 C C   . LYS A 1 445 ? 31.102 44.808 -29.658 1.00 18.11 ? 445  LYS A C   1 
ATOM   3623 O O   . LYS A 1 445 ? 30.854 44.693 -30.865 1.00 17.16 ? 445  LYS A O   1 
ATOM   3624 C CB  . LYS A 1 445 ? 28.975 44.650 -28.352 1.00 16.60 ? 445  LYS A CB  1 
ATOM   3625 C CG  . LYS A 1 445 ? 27.880 43.695 -27.852 1.00 19.36 ? 445  LYS A CG  1 
ATOM   3626 C CD  . LYS A 1 445 ? 26.513 44.358 -28.019 1.00 27.16 ? 445  LYS A CD  1 
ATOM   3627 C CE  . LYS A 1 445 ? 25.364 43.478 -27.556 1.00 31.76 ? 445  LYS A CE  1 
ATOM   3628 N NZ  . LYS A 1 445 ? 24.056 44.190 -27.733 1.00 35.04 ? 445  LYS A NZ  1 
ATOM   3629 N N   . ALA A 1 446 ? 32.055 45.629 -29.199 1.00 14.16 ? 446  ALA A N   1 
ATOM   3630 C CA  . ALA A 1 446 ? 32.844 46.429 -30.130 1.00 13.83 ? 446  ALA A CA  1 
ATOM   3631 C C   . ALA A 1 446 ? 33.727 45.571 -31.029 1.00 18.23 ? 446  ALA A C   1 
ATOM   3632 O O   . ALA A 1 446 ? 34.182 46.050 -32.071 1.00 17.61 ? 446  ALA A O   1 
ATOM   3633 C CB  . ALA A 1 446 ? 33.703 47.432 -29.359 1.00 11.04 ? 446  ALA A CB  1 
ATOM   3634 N N   . TRP A 1 447 ? 33.971 44.322 -30.648 1.00 17.31 ? 447  TRP A N   1 
ATOM   3635 C CA  . TRP A 1 447 ? 34.845 43.424 -31.382 1.00 23.86 ? 447  TRP A CA  1 
ATOM   3636 C C   . TRP A 1 447 ? 34.080 42.414 -32.228 1.00 32.56 ? 447  TRP A C   1 
ATOM   3637 O O   . TRP A 1 447 ? 34.706 41.653 -32.971 1.00 30.61 ? 447  TRP A O   1 
ATOM   3638 C CB  . TRP A 1 447 ? 35.788 42.710 -30.404 1.00 17.72 ? 447  TRP A CB  1 
ATOM   3639 C CG  . TRP A 1 447 ? 36.693 43.680 -29.659 1.00 18.60 ? 447  TRP A CG  1 
ATOM   3640 C CD1 . TRP A 1 447 ? 36.386 44.420 -28.544 1.00 18.58 ? 447  TRP A CD1 1 
ATOM   3641 C CD2 . TRP A 1 447 ? 38.038 44.025 -30.010 1.00 19.23 ? 447  TRP A CD2 1 
ATOM   3642 N NE1 . TRP A 1 447 ? 37.470 45.196 -28.180 1.00 19.24 ? 447  TRP A NE1 1 
ATOM   3643 C CE2 . TRP A 1 447 ? 38.494 44.964 -29.062 1.00 13.71 ? 447  TRP A CE2 1 
ATOM   3644 C CE3 . TRP A 1 447 ? 38.905 43.617 -31.029 1.00 17.95 ? 447  TRP A CE3 1 
ATOM   3645 C CZ2 . TRP A 1 447 ? 39.777 45.508 -29.109 1.00 18.17 ? 447  TRP A CZ2 1 
ATOM   3646 C CZ3 . TRP A 1 447 ? 40.184 44.154 -31.073 1.00 19.11 ? 447  TRP A CZ3 1 
ATOM   3647 C CH2 . TRP A 1 447 ? 40.606 45.093 -30.123 1.00 17.94 ? 447  TRP A CH2 1 
ATOM   3648 N N   . GLU A 1 448 ? 32.749 42.403 -32.158 1.00 34.29 ? 448  GLU A N   1 
ATOM   3649 C CA  . GLU A 1 448 ? 31.953 41.608 -33.098 1.00 48.96 ? 448  GLU A CA  1 
ATOM   3650 C C   . GLU A 1 448 ? 31.105 42.481 -34.026 1.00 47.04 ? 448  GLU A C   1 
ATOM   3651 O O   . GLU A 1 448 ? 31.400 42.603 -35.219 1.00 53.69 ? 448  GLU A O   1 
ATOM   3652 C CB  . GLU A 1 448 ? 31.055 40.618 -32.356 1.00 52.56 ? 448  GLU A CB  1 
ATOM   3653 C CG  . GLU A 1 448 ? 30.509 39.522 -33.272 1.00 60.30 ? 448  GLU A CG  1 
ATOM   3654 C CD  . GLU A 1 448 ? 31.609 38.684 -33.914 1.00 66.08 ? 448  GLU A CD  1 
ATOM   3655 O OE1 . GLU A 1 448 ? 32.441 38.115 -33.171 1.00 66.40 ? 448  GLU A OE1 1 
ATOM   3656 O OE2 . GLU A 1 448 ? 31.638 38.598 -35.165 1.00 69.43 ? 448  GLU A OE2 1 
ATOM   3657 N N   . MET B 1 1   ? 69.887 52.217 -78.365 1.00 35.40 ? 1    MET B N   1 
ATOM   3658 C CA  . MET B 1 1   ? 69.329 50.866 -78.141 1.00 26.22 ? 1    MET B CA  1 
ATOM   3659 C C   . MET B 1 1   ? 70.353 49.903 -77.537 1.00 29.13 ? 1    MET B C   1 
ATOM   3660 O O   . MET B 1 1   ? 71.547 50.155 -77.715 1.00 28.94 ? 1    MET B O   1 
ATOM   3661 C CB  . MET B 1 1   ? 68.867 50.285 -79.478 1.00 26.91 ? 1    MET B CB  1 
ATOM   3662 C CG  . MET B 1 1   ? 67.581 50.858 -80.033 1.00 27.57 ? 1    MET B CG  1 
ATOM   3663 S SD  . MET B 1 1   ? 67.131 50.027 -81.583 1.00 43.80 ? 1    MET B SD  1 
ATOM   3664 C CE  . MET B 1 1   ? 68.626 50.269 -82.539 1.00 39.19 ? 1    MET B CE  1 
ATOM   3665 N N   . PHE B 1 2   ? 69.905 48.875 -76.814 1.00 24.04 ? 2    PHE B N   1 
ATOM   3666 C CA  . PHE B 1 2   ? 70.763 47.785 -76.372 1.00 19.40 ? 2    PHE B CA  1 
ATOM   3667 C C   . PHE B 1 2   ? 71.615 47.329 -77.559 1.00 23.39 ? 2    PHE B C   1 
ATOM   3668 O O   . PHE B 1 2   ? 71.111 47.287 -78.689 1.00 21.89 ? 2    PHE B O   1 
ATOM   3669 C CB  . PHE B 1 2   ? 69.906 46.612 -75.884 1.00 19.77 ? 2    PHE B CB  1 
ATOM   3670 C CG  . PHE B 1 2   ? 69.389 46.753 -74.481 1.00 20.35 ? 2    PHE B CG  1 
ATOM   3671 C CD1 . PHE B 1 2   ? 68.377 47.651 -74.190 1.00 25.39 ? 2    PHE B CD1 1 
ATOM   3672 C CD2 . PHE B 1 2   ? 69.871 45.952 -73.467 1.00 18.08 ? 2    PHE B CD2 1 
ATOM   3673 C CE1 . PHE B 1 2   ? 67.872 47.773 -72.889 1.00 19.69 ? 2    PHE B CE1 1 
ATOM   3674 C CE2 . PHE B 1 2   ? 69.376 46.066 -72.176 1.00 18.05 ? 2    PHE B CE2 1 
ATOM   3675 C CZ  . PHE B 1 2   ? 68.377 46.978 -71.888 1.00 17.24 ? 2    PHE B CZ  1 
ATOM   3676 N N   . PRO B 1 3   ? 72.898 47.011 -77.366 1.00 21.72 ? 3    PRO B N   1 
ATOM   3677 C CA  . PRO B 1 3   ? 73.711 46.555 -78.505 1.00 24.95 ? 3    PRO B CA  1 
ATOM   3678 C C   . PRO B 1 3   ? 73.076 45.352 -79.185 1.00 23.14 ? 3    PRO B C   1 
ATOM   3679 O O   . PRO B 1 3   ? 72.292 44.605 -78.592 1.00 16.97 ? 3    PRO B O   1 
ATOM   3680 C CB  . PRO B 1 3   ? 75.059 46.200 -77.871 1.00 22.91 ? 3    PRO B CB  1 
ATOM   3681 C CG  . PRO B 1 3   ? 75.102 46.999 -76.606 1.00 25.11 ? 3    PRO B CG  1 
ATOM   3682 C CD  . PRO B 1 3   ? 73.685 47.105 -76.124 1.00 19.91 ? 3    PRO B CD  1 
ATOM   3683 N N   . GLN B 1 4   ? 73.397 45.184 -80.464 1.00 24.46 ? 4    GLN B N   1 
ATOM   3684 C CA  . GLN B 1 4   ? 72.728 44.151 -81.244 1.00 24.80 ? 4    GLN B CA  1 
ATOM   3685 C C   . GLN B 1 4   ? 73.078 42.741 -80.759 1.00 18.32 ? 4    GLN B C   1 
ATOM   3686 O O   . GLN B 1 4   ? 72.241 41.834 -80.836 1.00 21.10 ? 4    GLN B O   1 
ATOM   3687 C CB  . GLN B 1 4   ? 73.078 44.329 -82.724 1.00 32.06 ? 4    GLN B CB  1 
ATOM   3688 C CG  . GLN B 1 4   ? 72.324 43.404 -83.643 1.00 34.57 ? 4    GLN B CG  1 
ATOM   3689 C CD  . GLN B 1 4   ? 72.522 43.753 -85.111 1.00 58.40 ? 4    GLN B CD  1 
ATOM   3690 O OE1 . GLN B 1 4   ? 71.568 44.103 -85.807 1.00 57.86 ? 4    GLN B OE1 1 
ATOM   3691 N NE2 . GLN B 1 4   ? 73.764 43.639 -85.593 1.00 50.56 ? 4    GLN B NE2 1 
ATOM   3692 N N   . ASP B 1 5   ? 74.283 42.534 -80.240 1.00 16.60 ? 5    ASP B N   1 
ATOM   3693 C CA  . ASP B 1 5   ? 74.678 41.230 -79.714 1.00 22.48 ? 5    ASP B CA  1 
ATOM   3694 C C   . ASP B 1 5   ? 74.359 41.048 -78.224 1.00 19.22 ? 5    ASP B C   1 
ATOM   3695 O O   . ASP B 1 5   ? 74.799 40.055 -77.635 1.00 15.77 ? 5    ASP B O   1 
ATOM   3696 C CB  . ASP B 1 5   ? 76.175 40.997 -79.935 1.00 24.56 ? 5    ASP B CB  1 
ATOM   3697 C CG  . ASP B 1 5   ? 77.035 42.080 -79.308 1.00 34.39 ? 5    ASP B CG  1 
ATOM   3698 O OD1 . ASP B 1 5   ? 76.465 43.090 -78.836 1.00 38.98 ? 5    ASP B OD1 1 
ATOM   3699 O OD2 . ASP B 1 5   ? 78.281 41.931 -79.281 1.00 45.23 ? 5    ASP B OD2 1 
ATOM   3700 N N   . PHE B 1 6   ? 73.629 41.980 -77.606 1.00 17.27 ? 6    PHE B N   1 
ATOM   3701 C CA  . PHE B 1 6   ? 73.230 41.828 -76.207 1.00 13.66 ? 6    PHE B CA  1 
ATOM   3702 C C   . PHE B 1 6   ? 72.321 40.616 -76.044 1.00 12.51 ? 6    PHE B C   1 
ATOM   3703 O O   . PHE B 1 6   ? 71.435 40.374 -76.863 1.00 11.48 ? 6    PHE B O   1 
ATOM   3704 C CB  . PHE B 1 6   ? 72.509 43.094 -75.724 1.00 12.59 ? 6    PHE B CB  1 
ATOM   3705 C CG  . PHE B 1 6   ? 72.321 43.166 -74.221 1.00 11.95 ? 6    PHE B CG  1 
ATOM   3706 C CD1 . PHE B 1 6   ? 73.321 43.689 -73.409 1.00 11.30 ? 6    PHE B CD1 1 
ATOM   3707 C CD2 . PHE B 1 6   ? 71.136 42.740 -73.628 1.00 13.76 ? 6    PHE B CD2 1 
ATOM   3708 C CE1 . PHE B 1 6   ? 73.146 43.773 -72.021 1.00 14.57 ? 6    PHE B CE1 1 
ATOM   3709 C CE2 . PHE B 1 6   ? 70.944 42.828 -72.237 1.00 13.73 ? 6    PHE B CE2 1 
ATOM   3710 C CZ  . PHE B 1 6   ? 71.947 43.343 -71.439 1.00 11.70 ? 6    PHE B CZ  1 
ATOM   3711 N N   . LEU B 1 7   ? 72.522 39.852 -74.973 1.00 12.77 ? 7    LEU B N   1 
ATOM   3712 C CA  . LEU B 1 7   ? 71.750 38.633 -74.758 1.00 13.19 ? 7    LEU B CA  1 
ATOM   3713 C C   . LEU B 1 7   ? 70.568 38.911 -73.827 1.00 12.20 ? 7    LEU B C   1 
ATOM   3714 O O   . LEU B 1 7   ? 70.751 39.453 -72.732 1.00 12.47 ? 7    LEU B O   1 
ATOM   3715 C CB  . LEU B 1 7   ? 72.640 37.521 -74.190 1.00 13.31 ? 7    LEU B CB  1 
ATOM   3716 C CG  . LEU B 1 7   ? 73.837 37.108 -75.067 1.00 16.69 ? 7    LEU B CG  1 
ATOM   3717 C CD1 . LEU B 1 7   ? 74.569 35.924 -74.439 1.00 17.87 ? 7    LEU B CD1 1 
ATOM   3718 C CD2 . LEU B 1 7   ? 73.419 36.781 -76.522 1.00 13.88 ? 7    LEU B CD2 1 
ATOM   3719 N N   . PHE B 1 8   ? 69.360 38.556 -74.275 1.00 10.02 ? 8    PHE B N   1 
ATOM   3720 C CA  . PHE B 1 8   ? 68.154 38.567 -73.448 1.00 10.39 ? 8    PHE B CA  1 
ATOM   3721 C C   . PHE B 1 8   ? 67.688 37.129 -73.297 1.00 11.61 ? 8    PHE B C   1 
ATOM   3722 O O   . PHE B 1 8   ? 67.474 36.442 -74.301 1.00 10.67 ? 8    PHE B O   1 
ATOM   3723 C CB  . PHE B 1 8   ? 67.002 39.375 -74.077 1.00 9.10  ? 8    PHE B CB  1 
ATOM   3724 C CG  . PHE B 1 8   ? 67.250 40.868 -74.201 1.00 11.52 ? 8    PHE B CG  1 
ATOM   3725 C CD1 . PHE B 1 8   ? 67.129 41.707 -73.098 1.00 15.03 ? 8    PHE B CD1 1 
ATOM   3726 C CD2 . PHE B 1 8   ? 67.522 41.436 -75.447 1.00 13.69 ? 8    PHE B CD2 1 
ATOM   3727 C CE1 . PHE B 1 8   ? 67.313 43.085 -73.221 1.00 20.52 ? 8    PHE B CE1 1 
ATOM   3728 C CE2 . PHE B 1 8   ? 67.704 42.808 -75.582 1.00 16.37 ? 8    PHE B CE2 1 
ATOM   3729 C CZ  . PHE B 1 8   ? 67.596 43.635 -74.468 1.00 15.48 ? 8    PHE B CZ  1 
ATOM   3730 N N   . GLY B 1 9   ? 67.500 36.678 -72.061 1.00 10.42 ? 9    GLY B N   1 
ATOM   3731 C CA  . GLY B 1 9   ? 67.035 35.316 -71.879 1.00 8.28  ? 9    GLY B CA  1 
ATOM   3732 C C   . GLY B 1 9   ? 66.617 34.999 -70.459 1.00 11.17 ? 9    GLY B C   1 
ATOM   3733 O O   . GLY B 1 9   ? 66.176 35.889 -69.723 1.00 9.51  ? 9    GLY B O   1 
ATOM   3734 N N   . VAL B 1 10  ? 66.765 33.730 -70.058 1.00 6.55  ? 10   VAL B N   1 
ATOM   3735 C CA  . VAL B 1 10  ? 66.314 33.254 -68.756 1.00 9.54  ? 10   VAL B CA  1 
ATOM   3736 C C   . VAL B 1 10  ? 67.353 32.288 -68.211 1.00 10.00 ? 10   VAL B C   1 
ATOM   3737 O O   . VAL B 1 10  ? 68.240 31.820 -68.931 1.00 8.00  ? 10   VAL B O   1 
ATOM   3738 C CB  . VAL B 1 10  ? 64.940 32.550 -68.817 1.00 12.03 ? 10   VAL B CB  1 
ATOM   3739 C CG1 . VAL B 1 10  ? 63.843 33.520 -69.323 1.00 7.88  ? 10   VAL B CG1 1 
ATOM   3740 C CG2 . VAL B 1 10  ? 65.031 31.275 -69.673 1.00 8.97  ? 10   VAL B CG2 1 
ATOM   3741 N N   . ALA B 1 11  ? 67.209 31.987 -66.920 1.00 8.01  ? 11   ALA B N   1 
ATOM   3742 C CA  . ALA B 1 11  ? 68.073 31.095 -66.167 1.00 8.65  ? 11   ALA B CA  1 
ATOM   3743 C C   . ALA B 1 11  ? 67.230 29.992 -65.546 1.00 11.53 ? 11   ALA B C   1 
ATOM   3744 O O   . ALA B 1 11  ? 66.112 30.238 -65.079 1.00 7.43  ? 11   ALA B O   1 
ATOM   3745 C CB  . ALA B 1 11  ? 68.809 31.850 -65.055 1.00 9.97  ? 11   ALA B CB  1 
ATOM   3746 N N   . MET B 1 12  ? 67.783 28.784 -65.536 1.00 9.48  ? 12   MET B N   1 
ATOM   3747 C CA  . MET B 1 12  ? 67.186 27.616 -64.903 1.00 8.04  ? 12   MET B CA  1 
ATOM   3748 C C   . MET B 1 12  ? 68.263 26.803 -64.200 1.00 10.17 ? 12   MET B C   1 
ATOM   3749 O O   . MET B 1 12  ? 69.469 27.015 -64.388 1.00 9.18  ? 12   MET B O   1 
ATOM   3750 C CB  . MET B 1 12  ? 66.429 26.744 -65.924 1.00 9.50  ? 12   MET B CB  1 
ATOM   3751 C CG  . MET B 1 12  ? 65.569 27.533 -66.894 1.00 14.25 ? 12   MET B CG  1 
ATOM   3752 S SD  . MET B 1 12  ? 64.656 26.450 -67.997 1.00 16.79 ? 12   MET B SD  1 
ATOM   3753 C CE  . MET B 1 12  ? 66.032 25.541 -68.640 1.00 14.08 ? 12   MET B CE  1 
ATOM   3754 N N   . SER B 1 13  ? 67.797 25.868 -63.375 1.00 9.17  ? 13   SER B N   1 
ATOM   3755 C CA  . SER B 1 13  ? 68.619 24.875 -62.699 1.00 8.75  ? 13   SER B CA  1 
ATOM   3756 C C   . SER B 1 13  ? 68.067 23.496 -63.018 1.00 9.80  ? 13   SER B C   1 
ATOM   3757 O O   . SER B 1 13  ? 66.926 23.351 -63.472 1.00 8.75  ? 13   SER B O   1 
ATOM   3758 C CB  . SER B 1 13  ? 68.631 25.078 -61.177 1.00 9.21  ? 13   SER B CB  1 
ATOM   3759 O OG  . SER B 1 13  ? 67.366 24.725 -60.611 1.00 9.37  ? 13   SER B OG  1 
ATOM   3760 N N   . GLY B 1 14  ? 68.881 22.476 -62.751 1.00 8.70  ? 14   GLY B N   1 
ATOM   3761 C CA  . GLY B 1 14  ? 68.420 21.112 -62.950 1.00 9.23  ? 14   GLY B CA  1 
ATOM   3762 C C   . GLY B 1 14  ? 67.375 20.702 -61.931 1.00 11.49 ? 14   GLY B C   1 
ATOM   3763 O O   . GLY B 1 14  ? 66.277 20.265 -62.290 1.00 8.31  ? 14   GLY B O   1 
ATOM   3764 N N   . PHE B 1 15  ? 67.689 20.869 -60.641 1.00 8.64  ? 15   PHE B N   1 
ATOM   3765 C CA  . PHE B 1 15  ? 66.831 20.301 -59.606 1.00 9.54  ? 15   PHE B CA  1 
ATOM   3766 C C   . PHE B 1 15  ? 65.464 20.971 -59.574 1.00 8.21  ? 15   PHE B C   1 
ATOM   3767 O O   . PHE B 1 15  ? 64.460 20.306 -59.313 1.00 8.29  ? 15   PHE B O   1 
ATOM   3768 C CB  . PHE B 1 15  ? 67.509 20.415 -58.244 1.00 7.59  ? 15   PHE B CB  1 
ATOM   3769 C CG  . PHE B 1 15  ? 66.724 19.812 -57.105 1.00 10.11 ? 15   PHE B CG  1 
ATOM   3770 C CD1 . PHE B 1 15  ? 66.782 18.450 -56.843 1.00 10.13 ? 15   PHE B CD1 1 
ATOM   3771 C CD2 . PHE B 1 15  ? 65.970 20.617 -56.262 1.00 10.09 ? 15   PHE B CD2 1 
ATOM   3772 C CE1 . PHE B 1 15  ? 66.084 17.901 -55.762 1.00 10.34 ? 15   PHE B CE1 1 
ATOM   3773 C CE2 . PHE B 1 15  ? 65.260 20.079 -55.185 1.00 8.96  ? 15   PHE B CE2 1 
ATOM   3774 C CZ  . PHE B 1 15  ? 65.309 18.720 -54.940 1.00 6.63  ? 15   PHE B CZ  1 
ATOM   3775 N N   . GLN B 1 16  ? 65.390 22.266 -59.861 1.00 7.84  ? 16   GLN B N   1 
ATOM   3776 C CA  . GLN B 1 16  ? 64.119 22.945 -59.673 1.00 7.77  ? 16   GLN B CA  1 
ATOM   3777 C C   . GLN B 1 16  ? 63.155 22.747 -60.837 1.00 8.39  ? 16   GLN B C   1 
ATOM   3778 O O   . GLN B 1 16  ? 61.981 23.121 -60.708 1.00 8.36  ? 16   GLN B O   1 
ATOM   3779 C CB  . GLN B 1 16  ? 64.362 24.428 -59.453 1.00 6.32  ? 16   GLN B CB  1 
ATOM   3780 C CG  . GLN B 1 16  ? 65.201 24.727 -58.207 1.00 7.62  ? 16   GLN B CG  1 
ATOM   3781 C CD  . GLN B 1 16  ? 65.588 26.192 -58.163 1.00 9.36  ? 16   GLN B CD  1 
ATOM   3782 O OE1 . GLN B 1 16  ? 66.581 26.606 -58.784 1.00 7.63  ? 16   GLN B OE1 1 
ATOM   3783 N NE2 . GLN B 1 16  ? 64.774 26.999 -57.473 1.00 8.64  ? 16   GLN B NE2 1 
ATOM   3784 N N   . PHE B 1 17  ? 63.606 22.150 -61.944 1.00 7.36  ? 17   PHE B N   1 
ATOM   3785 C CA  . PHE B 1 17  ? 62.860 22.170 -63.200 1.00 7.53  ? 17   PHE B CA  1 
ATOM   3786 C C   . PHE B 1 17  ? 62.665 20.787 -63.822 1.00 9.45  ? 17   PHE B C   1 
ATOM   3787 O O   . PHE B 1 17  ? 61.654 20.552 -64.492 1.00 9.47  ? 17   PHE B O   1 
ATOM   3788 C CB  . PHE B 1 17  ? 63.573 23.063 -64.228 1.00 7.05  ? 17   PHE B CB  1 
ATOM   3789 C CG  . PHE B 1 17  ? 63.569 24.530 -63.887 1.00 10.08 ? 17   PHE B CG  1 
ATOM   3790 C CD1 . PHE B 1 17  ? 64.415 25.030 -62.913 1.00 7.90  ? 17   PHE B CD1 1 
ATOM   3791 C CD2 . PHE B 1 17  ? 62.749 25.413 -64.570 1.00 9.67  ? 17   PHE B CD2 1 
ATOM   3792 C CE1 . PHE B 1 17  ? 64.436 26.380 -62.605 1.00 8.98  ? 17   PHE B CE1 1 
ATOM   3793 C CE2 . PHE B 1 17  ? 62.761 26.777 -64.272 1.00 9.35  ? 17   PHE B CE2 1 
ATOM   3794 C CZ  . PHE B 1 17  ? 63.610 27.259 -63.289 1.00 8.37  ? 17   PHE B CZ  1 
ATOM   3795 N N   . GLU B 1 18  ? 63.638 19.884 -63.643 1.00 8.09  ? 18   GLU B N   1 
ATOM   3796 C CA  . GLU B 1 18  ? 63.741 18.711 -64.514 1.00 10.11 ? 18   GLU B CA  1 
ATOM   3797 C C   . GLU B 1 18  ? 62.647 17.688 -64.238 1.00 9.70  ? 18   GLU B C   1 
ATOM   3798 O O   . GLU B 1 18  ? 62.056 17.127 -65.174 1.00 8.38  ? 18   GLU B O   1 
ATOM   3799 C CB  . GLU B 1 18  ? 65.118 18.053 -64.353 1.00 11.46 ? 18   GLU B CB  1 
ATOM   3800 C CG  . GLU B 1 18  ? 66.235 18.787 -65.111 1.00 10.12 ? 18   GLU B CG  1 
ATOM   3801 C CD  . GLU B 1 18  ? 67.634 18.269 -64.811 1.00 13.36 ? 18   GLU B CD  1 
ATOM   3802 O OE1 . GLU B 1 18  ? 67.822 17.534 -63.809 1.00 11.43 ? 18   GLU B OE1 1 
ATOM   3803 O OE2 . GLU B 1 18  ? 68.552 18.612 -65.585 1.00 10.76 ? 18   GLU B OE2 1 
ATOM   3804 N N   . MET B 1 19  ? 62.393 17.396 -62.967 1.00 5.90  ? 19   MET B N   1 
ATOM   3805 C CA  . MET B 1 19  ? 61.616 16.224 -62.613 1.00 10.18 ? 19   MET B CA  1 
ATOM   3806 C C   . MET B 1 19  ? 60.117 16.518 -62.782 1.00 11.26 ? 19   MET B C   1 
ATOM   3807 O O   . MET B 1 19  ? 59.690 17.669 -62.943 1.00 11.03 ? 19   MET B O   1 
ATOM   3808 C CB  . MET B 1 19  ? 61.927 15.837 -61.166 1.00 8.60  ? 19   MET B CB  1 
ATOM   3809 C CG  . MET B 1 19  ? 63.140 14.912 -61.029 1.00 11.66 ? 19   MET B CG  1 
ATOM   3810 S SD  . MET B 1 19  ? 63.439 14.411 -59.312 1.00 13.89 ? 19   MET B SD  1 
ATOM   3811 C CE  . MET B 1 19  ? 64.708 15.550 -58.747 1.00 9.73  ? 19   MET B CE  1 
ATOM   3812 N N   . GLY B 1 20  ? 59.307 15.471 -62.717 1.00 11.10 ? 20   GLY B N   1 
ATOM   3813 C CA  . GLY B 1 20  ? 57.884 15.596 -62.972 1.00 11.98 ? 20   GLY B CA  1 
ATOM   3814 C C   . GLY B 1 20  ? 57.295 14.344 -63.596 1.00 16.38 ? 20   GLY B C   1 
ATOM   3815 O O   . GLY B 1 20  ? 56.098 14.076 -63.465 1.00 17.68 ? 20   GLY B O   1 
ATOM   3816 N N   . LYS B 1 21  ? 58.138 13.562 -64.263 1.00 14.50 ? 21   LYS B N   1 
ATOM   3817 C CA  . LYS B 1 21  ? 57.758 12.287 -64.856 1.00 18.24 ? 21   LYS B CA  1 
ATOM   3818 C C   . LYS B 1 21  ? 58.650 11.207 -64.272 1.00 17.51 ? 21   LYS B C   1 
ATOM   3819 O O   . LYS B 1 21  ? 59.822 11.457 -63.981 1.00 16.81 ? 21   LYS B O   1 
ATOM   3820 C CB  . LYS B 1 21  ? 57.932 12.287 -66.382 1.00 18.21 ? 21   LYS B CB  1 
ATOM   3821 C CG  . LYS B 1 21  ? 56.859 12.973 -67.181 1.00 22.80 ? 21   LYS B CG  1 
ATOM   3822 C CD  . LYS B 1 21  ? 55.486 12.418 -66.912 1.00 32.43 ? 21   LYS B CD  1 
ATOM   3823 C CE  . LYS B 1 21  ? 54.529 13.545 -66.551 1.00 40.34 ? 21   LYS B CE  1 
ATOM   3824 N NZ  . LYS B 1 21  ? 54.175 14.369 -67.752 1.00 42.56 ? 21   LYS B NZ  1 
ATOM   3825 N N   . GLU B 1 22  ? 58.107 9.991  -64.148 1.00 17.85 ? 22   GLU B N   1 
ATOM   3826 C CA  . GLU B 1 22  ? 58.853 8.913  -63.501 1.00 20.68 ? 22   GLU B CA  1 
ATOM   3827 C C   . GLU B 1 22  ? 60.201 8.647  -64.171 1.00 18.26 ? 22   GLU B C   1 
ATOM   3828 O O   . GLU B 1 22  ? 61.181 8.350  -63.481 1.00 16.93 ? 22   GLU B O   1 
ATOM   3829 C CB  . GLU B 1 22  ? 58.006 7.640  -63.464 1.00 21.94 ? 22   GLU B CB  1 
ATOM   3830 C CG  . GLU B 1 22  ? 58.737 6.464  -62.844 1.00 31.33 ? 22   GLU B CG  1 
ATOM   3831 C CD  . GLU B 1 22  ? 58.807 6.558  -61.325 1.00 41.09 ? 22   GLU B CD  1 
ATOM   3832 O OE1 . GLU B 1 22  ? 59.642 5.838  -60.728 1.00 44.05 ? 22   GLU B OE1 1 
ATOM   3833 O OE2 . GLU B 1 22  ? 58.036 7.355  -60.733 1.00 39.35 ? 22   GLU B OE2 1 
ATOM   3834 N N   . ASN B 1 23  ? 60.290 8.786  -65.496 1.00 15.95 ? 23   ASN B N   1 
ATOM   3835 C CA  . ASN B 1 23  ? 61.538 8.475  -66.185 1.00 17.45 ? 23   ASN B CA  1 
ATOM   3836 C C   . ASN B 1 23  ? 62.666 9.445  -65.842 1.00 21.24 ? 23   ASN B C   1 
ATOM   3837 O O   . ASN B 1 23  ? 63.825 9.131  -66.121 1.00 17.57 ? 23   ASN B O   1 
ATOM   3838 C CB  . ASN B 1 23  ? 61.324 8.438  -67.712 1.00 19.52 ? 23   ASN B CB  1 
ATOM   3839 C CG  . ASN B 1 23  ? 61.243 9.834  -68.343 1.00 21.45 ? 23   ASN B CG  1 
ATOM   3840 O OD1 . ASN B 1 23  ? 60.711 10.769 -67.745 1.00 17.02 ? 23   ASN B OD1 1 
ATOM   3841 N ND2 . ASN B 1 23  ? 61.773 9.972  -69.562 1.00 24.03 ? 23   ASN B ND2 1 
ATOM   3842 N N   . SER B 1 24  ? 62.376 10.603 -65.239 1.00 14.13 ? 24   SER B N   1 
ATOM   3843 C CA  . SER B 1 24  ? 63.435 11.550 -64.896 1.00 17.56 ? 24   SER B CA  1 
ATOM   3844 C C   . SER B 1 24  ? 63.796 11.548 -63.419 1.00 18.48 ? 24   SER B C   1 
ATOM   3845 O O   . SER B 1 24  ? 64.686 12.307 -63.015 1.00 18.99 ? 24   SER B O   1 
ATOM   3846 C CB  . SER B 1 24  ? 63.028 12.970 -65.270 1.00 15.72 ? 24   SER B CB  1 
ATOM   3847 O OG  . SER B 1 24  ? 61.972 13.388 -64.419 1.00 16.22 ? 24   SER B OG  1 
ATOM   3848 N N   . LYS B 1 25  ? 63.104 10.763 -62.599 1.00 15.80 ? 25   LYS B N   1 
ATOM   3849 C CA  . LYS B 1 25  ? 63.247 10.884 -61.152 1.00 15.29 ? 25   LYS B CA  1 
ATOM   3850 C C   . LYS B 1 25  ? 64.706 10.670 -60.743 1.00 15.97 ? 25   LYS B C   1 
ATOM   3851 O O   . LYS B 1 25  ? 65.343 9.700  -61.157 1.00 19.50 ? 25   LYS B O   1 
ATOM   3852 C CB  . LYS B 1 25  ? 62.333 9.869  -60.472 1.00 17.62 ? 25   LYS B CB  1 
ATOM   3853 C CG  . LYS B 1 25  ? 62.436 9.769  -58.966 1.00 24.92 ? 25   LYS B CG  1 
ATOM   3854 C CD  . LYS B 1 25  ? 61.040 9.706  -58.402 1.00 25.26 ? 25   LYS B CD  1 
ATOM   3855 C CE  . LYS B 1 25  ? 60.990 8.910  -57.133 1.00 32.65 ? 25   LYS B CE  1 
ATOM   3856 N NZ  . LYS B 1 25  ? 59.578 8.567  -56.761 1.00 44.78 ? 25   LYS B NZ  1 
ATOM   3857 N N   . ASP B 1 26  ? 65.247 11.602 -59.965 1.00 11.01 ? 26   ASP B N   1 
ATOM   3858 C CA  . ASP B 1 26  ? 66.634 11.552 -59.501 1.00 13.39 ? 26   ASP B CA  1 
ATOM   3859 C C   . ASP B 1 26  ? 66.603 11.646 -57.977 1.00 15.25 ? 26   ASP B C   1 
ATOM   3860 O O   . ASP B 1 26  ? 66.509 12.749 -57.423 1.00 14.87 ? 26   ASP B O   1 
ATOM   3861 C CB  . ASP B 1 26  ? 67.477 12.683 -60.120 1.00 11.00 ? 26   ASP B CB  1 
ATOM   3862 C CG  . ASP B 1 26  ? 68.911 12.732 -59.570 1.00 12.96 ? 26   ASP B CG  1 
ATOM   3863 O OD1 . ASP B 1 26  ? 69.345 11.745 -58.920 1.00 13.79 ? 26   ASP B OD1 1 
ATOM   3864 O OD2 . ASP B 1 26  ? 69.610 13.752 -59.778 1.00 11.54 ? 26   ASP B OD2 1 
ATOM   3865 N N   . GLU B 1 27  ? 66.688 10.500 -57.300 1.00 11.87 ? 27   GLU B N   1 
ATOM   3866 C CA  . GLU B 1 27  ? 66.757 10.484 -55.841 1.00 16.80 ? 27   GLU B CA  1 
ATOM   3867 C C   . GLU B 1 27  ? 68.173 10.649 -55.304 1.00 14.12 ? 27   GLU B C   1 
ATOM   3868 O O   . GLU B 1 27  ? 68.360 10.622 -54.087 1.00 14.95 ? 27   GLU B O   1 
ATOM   3869 C CB  . GLU B 1 27  ? 66.151 9.189  -55.283 1.00 13.74 ? 27   GLU B CB  1 
ATOM   3870 C CG  . GLU B 1 27  ? 64.910 8.726  -56.009 1.00 17.69 ? 27   GLU B CG  1 
ATOM   3871 C CD  . GLU B 1 27  ? 64.277 7.515  -55.341 1.00 28.98 ? 27   GLU B CD  1 
ATOM   3872 O OE1 . GLU B 1 27  ? 64.986 6.797  -54.612 1.00 34.90 ? 27   GLU B OE1 1 
ATOM   3873 O OE2 . GLU B 1 27  ? 63.071 7.287  -55.531 1.00 31.09 ? 27   GLU B OE2 1 
ATOM   3874 N N   . ASN B 1 28  ? 69.161 10.851 -56.169 1.00 11.10 ? 28   ASN B N   1 
ATOM   3875 C CA  . ASN B 1 28  ? 70.570 10.802 -55.782 1.00 13.51 ? 28   ASN B CA  1 
ATOM   3876 C C   . ASN B 1 28  ? 71.159 12.164 -55.413 1.00 10.50 ? 28   ASN B C   1 
ATOM   3877 O O   . ASN B 1 28  ? 72.305 12.435 -55.758 1.00 10.73 ? 28   ASN B O   1 
ATOM   3878 C CB  . ASN B 1 28  ? 71.348 10.143 -56.925 1.00 14.87 ? 28   ASN B CB  1 
ATOM   3879 C CG  . ASN B 1 28  ? 72.761 9.745  -56.542 1.00 20.63 ? 28   ASN B CG  1 
ATOM   3880 O OD1 . ASN B 1 28  ? 72.990 9.175  -55.476 1.00 20.18 ? 28   ASN B OD1 1 
ATOM   3881 N ND2 . ASN B 1 28  ? 73.707 9.966  -57.457 1.00 13.41 ? 28   ASN B ND2 1 
ATOM   3882 N N   . THR B 1 29  ? 70.432 13.059 -54.735 1.00 10.91 ? 29   THR B N   1 
ATOM   3883 C CA  . THR B 1 29  ? 71.015 14.322 -54.290 1.00 9.10  ? 29   THR B CA  1 
ATOM   3884 C C   . THR B 1 29  ? 70.767 14.535 -52.807 1.00 9.13  ? 29   THR B C   1 
ATOM   3885 O O   . THR B 1 29  ? 69.833 13.984 -52.216 1.00 6.75  ? 29   THR B O   1 
ATOM   3886 C CB  . THR B 1 29  ? 70.465 15.555 -55.020 1.00 8.56  ? 29   THR B CB  1 
ATOM   3887 O OG1 . THR B 1 29  ? 69.058 15.657 -54.784 1.00 9.49  ? 29   THR B OG1 1 
ATOM   3888 C CG2 . THR B 1 29  ? 70.754 15.495 -56.533 1.00 11.55 ? 29   THR B CG2 1 
ATOM   3889 N N   . ASP B 1 30  ? 71.610 15.393 -52.230 1.00 8.70  ? 30   ASP B N   1 
ATOM   3890 C CA  . ASP B 1 30  ? 71.375 15.844 -50.868 1.00 7.87  ? 30   ASP B CA  1 
ATOM   3891 C C   . ASP B 1 30  ? 70.019 16.542 -50.749 1.00 8.48  ? 30   ASP B C   1 
ATOM   3892 O O   . ASP B 1 30  ? 69.279 16.311 -49.785 1.00 7.59  ? 30   ASP B O   1 
ATOM   3893 C CB  . ASP B 1 30  ? 72.525 16.752 -50.402 1.00 6.98  ? 30   ASP B CB  1 
ATOM   3894 C CG  . ASP B 1 30  ? 72.843 17.903 -51.376 1.00 12.28 ? 30   ASP B CG  1 
ATOM   3895 O OD1 . ASP B 1 30  ? 72.165 18.065 -52.423 1.00 10.04 ? 30   ASP B OD1 1 
ATOM   3896 O OD2 . ASP B 1 30  ? 73.769 18.694 -51.052 1.00 10.71 ? 30   ASP B OD2 1 
ATOM   3897 N N   . TRP B 1 31  ? 69.642 17.331 -51.757 1.00 7.13  ? 31   TRP B N   1 
ATOM   3898 C CA  . TRP B 1 31  ? 68.400 18.094 -51.702 1.00 9.01  ? 31   TRP B CA  1 
ATOM   3899 C C   . TRP B 1 31  ? 67.171 17.205 -51.836 1.00 8.20  ? 31   TRP B C   1 
ATOM   3900 O O   . TRP B 1 31  ? 66.122 17.509 -51.248 1.00 8.96  ? 31   TRP B O   1 
ATOM   3901 C CB  . TRP B 1 31  ? 68.398 19.184 -52.789 1.00 7.60  ? 31   TRP B CB  1 
ATOM   3902 C CG  . TRP B 1 31  ? 68.747 20.528 -52.228 1.00 9.54  ? 31   TRP B CG  1 
ATOM   3903 C CD1 . TRP B 1 31  ? 69.979 21.126 -52.218 1.00 8.66  ? 31   TRP B CD1 1 
ATOM   3904 C CD2 . TRP B 1 31  ? 67.859 21.419 -51.539 1.00 8.80  ? 31   TRP B CD2 1 
ATOM   3905 N NE1 . TRP B 1 31  ? 69.901 22.345 -51.577 1.00 10.67 ? 31   TRP B NE1 1 
ATOM   3906 C CE2 . TRP B 1 31  ? 68.609 22.550 -51.163 1.00 10.13 ? 31   TRP B CE2 1 
ATOM   3907 C CE3 . TRP B 1 31  ? 66.488 21.388 -51.247 1.00 9.46  ? 31   TRP B CE3 1 
ATOM   3908 C CZ2 . TRP B 1 31  ? 68.040 23.632 -50.492 1.00 10.38 ? 31   TRP B CZ2 1 
ATOM   3909 C CZ3 . TRP B 1 31  ? 65.924 22.460 -50.571 1.00 10.40 ? 31   TRP B CZ3 1 
ATOM   3910 C CH2 . TRP B 1 31  ? 66.699 23.562 -50.199 1.00 10.23 ? 31   TRP B CH2 1 
ATOM   3911 N N   . TYR B 1 32  ? 67.256 16.131 -52.620 1.00 8.54  ? 32   TYR B N   1 
ATOM   3912 C CA  . TYR B 1 32  ? 66.141 15.191 -52.661 1.00 7.85  ? 32   TYR B CA  1 
ATOM   3913 C C   . TYR B 1 32  ? 65.871 14.608 -51.279 1.00 8.27  ? 32   TYR B C   1 
ATOM   3914 O O   . TYR B 1 32  ? 64.726 14.592 -50.820 1.00 10.26 ? 32   TYR B O   1 
ATOM   3915 C CB  . TYR B 1 32  ? 66.405 14.069 -53.663 1.00 10.03 ? 32   TYR B CB  1 
ATOM   3916 C CG  . TYR B 1 32  ? 65.155 13.243 -53.964 1.00 14.76 ? 32   TYR B CG  1 
ATOM   3917 C CD1 . TYR B 1 32  ? 64.825 12.122 -53.198 1.00 12.88 ? 32   TYR B CD1 1 
ATOM   3918 C CD2 . TYR B 1 32  ? 64.308 13.600 -55.003 1.00 10.67 ? 32   TYR B CD2 1 
ATOM   3919 C CE1 . TYR B 1 32  ? 63.672 11.376 -53.476 1.00 16.97 ? 32   TYR B CE1 1 
ATOM   3920 C CE2 . TYR B 1 32  ? 63.162 12.863 -55.292 1.00 15.27 ? 32   TYR B CE2 1 
ATOM   3921 C CZ  . TYR B 1 32  ? 62.854 11.759 -54.527 1.00 18.34 ? 32   TYR B CZ  1 
ATOM   3922 O OH  . TYR B 1 32  ? 61.725 11.049 -54.832 1.00 23.46 ? 32   TYR B OH  1 
ATOM   3923 N N   . ILE B 1 33  ? 66.907 14.105 -50.597 1.00 7.46  ? 33   ILE B N   1 
ATOM   3924 C CA  . ILE B 1 33  ? 66.603 13.468 -49.317 1.00 9.92  ? 33   ILE B CA  1 
ATOM   3925 C C   . ILE B 1 33  ? 66.279 14.520 -48.257 1.00 9.97  ? 33   ILE B C   1 
ATOM   3926 O O   . ILE B 1 33  ? 65.495 14.258 -47.339 1.00 9.93  ? 33   ILE B O   1 
ATOM   3927 C CB  . ILE B 1 33  ? 67.736 12.536 -48.858 1.00 13.87 ? 33   ILE B CB  1 
ATOM   3928 C CG1 . ILE B 1 33  ? 68.987 13.316 -48.517 1.00 14.83 ? 33   ILE B CG1 1 
ATOM   3929 C CG2 . ILE B 1 33  ? 68.061 11.508 -49.929 1.00 20.81 ? 33   ILE B CG2 1 
ATOM   3930 C CD1 . ILE B 1 33  ? 69.523 12.890 -47.197 1.00 24.03 ? 33   ILE B CD1 1 
ATOM   3931 N N   . TRP B 1 34  ? 66.845 15.726 -48.389 1.00 9.19  ? 34   TRP B N   1 
ATOM   3932 C CA  . TRP B 1 34  ? 66.558 16.820 -47.462 1.00 9.55  ? 34   TRP B CA  1 
ATOM   3933 C C   . TRP B 1 34  ? 65.090 17.218 -47.502 1.00 9.68  ? 34   TRP B C   1 
ATOM   3934 O O   . TRP B 1 34  ? 64.482 17.469 -46.451 1.00 8.18  ? 34   TRP B O   1 
ATOM   3935 C CB  . TRP B 1 34  ? 67.441 18.024 -47.809 1.00 7.26  ? 34   TRP B CB  1 
ATOM   3936 C CG  . TRP B 1 34  ? 67.334 19.208 -46.877 1.00 10.70 ? 34   TRP B CG  1 
ATOM   3937 C CD1 . TRP B 1 34  ? 66.762 20.415 -47.152 1.00 9.28  ? 34   TRP B CD1 1 
ATOM   3938 C CD2 . TRP B 1 34  ? 67.862 19.309 -45.546 1.00 9.55  ? 34   TRP B CD2 1 
ATOM   3939 N NE1 . TRP B 1 34  ? 66.890 21.263 -46.071 1.00 8.02  ? 34   TRP B NE1 1 
ATOM   3940 C CE2 . TRP B 1 34  ? 67.556 20.606 -45.072 1.00 9.74  ? 34   TRP B CE2 1 
ATOM   3941 C CE3 . TRP B 1 34  ? 68.562 18.431 -44.708 1.00 9.05  ? 34   TRP B CE3 1 
ATOM   3942 C CZ2 . TRP B 1 34  ? 67.919 21.042 -43.795 1.00 9.22  ? 34   TRP B CZ2 1 
ATOM   3943 C CZ3 . TRP B 1 34  ? 68.925 18.863 -43.443 1.00 9.82  ? 34   TRP B CZ3 1 
ATOM   3944 C CH2 . TRP B 1 34  ? 68.601 20.156 -43.000 1.00 11.46 ? 34   TRP B CH2 1 
ATOM   3945 N N   . THR B 1 35  ? 64.502 17.288 -48.704 1.00 8.33  ? 35   THR B N   1 
ATOM   3946 C CA  . THR B 1 35  ? 63.111 17.709 -48.845 1.00 8.72  ? 35   THR B CA  1 
ATOM   3947 C C   . THR B 1 35  ? 62.126 16.578 -48.598 1.00 8.60  ? 35   THR B C   1 
ATOM   3948 O O   . THR B 1 35  ? 60.941 16.848 -48.373 1.00 8.82  ? 35   THR B O   1 
ATOM   3949 C CB  . THR B 1 35  ? 62.846 18.311 -50.239 1.00 7.66  ? 35   THR B CB  1 
ATOM   3950 O OG1 . THR B 1 35  ? 63.281 17.411 -51.262 1.00 8.98  ? 35   THR B OG1 1 
ATOM   3951 C CG2 . THR B 1 35  ? 63.571 19.637 -50.418 1.00 8.76  ? 35   THR B CG2 1 
ATOM   3952 N N   . HIS B 1 36  ? 62.572 15.328 -48.638 1.00 8.54  ? 36   HIS B N   1 
ATOM   3953 C CA  . HIS B 1 36  ? 61.698 14.201 -48.343 1.00 8.86  ? 36   HIS B CA  1 
ATOM   3954 C C   . HIS B 1 36  ? 61.734 13.808 -46.866 1.00 10.52 ? 36   HIS B C   1 
ATOM   3955 O O   . HIS B 1 36  ? 60.989 12.915 -46.459 1.00 10.77 ? 36   HIS B O   1 
ATOM   3956 C CB  . HIS B 1 36  ? 62.070 13.002 -49.236 1.00 9.56  ? 36   HIS B CB  1 
ATOM   3957 C CG  . HIS B 1 36  ? 61.543 13.136 -50.634 1.00 9.85  ? 36   HIS B CG  1 
ATOM   3958 N ND1 . HIS B 1 36  ? 62.078 14.024 -51.541 1.00 9.81  ? 36   HIS B ND1 1 
ATOM   3959 C CD2 . HIS B 1 36  ? 60.487 12.559 -51.251 1.00 11.42 ? 36   HIS B CD2 1 
ATOM   3960 C CE1 . HIS B 1 36  ? 61.394 13.965 -52.671 1.00 10.59 ? 36   HIS B CE1 1 
ATOM   3961 N NE2 . HIS B 1 36  ? 60.422 13.085 -52.521 1.00 12.47 ? 36   HIS B NE2 1 
ATOM   3962 N N   . ASP B 1 37  ? 62.554 14.472 -46.061 1.00 8.54  ? 37   ASP B N   1 
ATOM   3963 C CA  . ASP B 1 37  ? 62.692 14.114 -44.655 1.00 8.60  ? 37   ASP B CA  1 
ATOM   3964 C C   . ASP B 1 37  ? 61.457 14.561 -43.884 1.00 10.50 ? 37   ASP B C   1 
ATOM   3965 O O   . ASP B 1 37  ? 61.144 15.756 -43.828 1.00 8.82  ? 37   ASP B O   1 
ATOM   3966 C CB  . ASP B 1 37  ? 63.962 14.740 -44.081 1.00 10.48 ? 37   ASP B CB  1 
ATOM   3967 C CG  . ASP B 1 37  ? 64.217 14.326 -42.641 1.00 11.16 ? 37   ASP B CG  1 
ATOM   3968 O OD1 . ASP B 1 37  ? 64.705 13.199 -42.422 1.00 10.22 ? 37   ASP B OD1 1 
ATOM   3969 O OD2 . ASP B 1 37  ? 63.961 15.139 -41.731 1.00 11.11 ? 37   ASP B OD2 1 
ATOM   3970 N N   . LEU B 1 38  ? 60.743 13.593 -43.308 1.00 8.48  ? 38   LEU B N   1 
ATOM   3971 C CA  . LEU B 1 38  ? 59.488 13.894 -42.626 1.00 10.00 ? 38   LEU B CA  1 
ATOM   3972 C C   . LEU B 1 38  ? 59.692 14.774 -41.398 1.00 10.75 ? 38   LEU B C   1 
ATOM   3973 O O   . LEU B 1 38  ? 58.808 15.563 -41.051 1.00 10.37 ? 38   LEU B O   1 
ATOM   3974 C CB  . LEU B 1 38  ? 58.804 12.597 -42.212 1.00 12.42 ? 38   LEU B CB  1 
ATOM   3975 C CG  . LEU B 1 38  ? 58.315 11.668 -43.325 1.00 16.26 ? 38   LEU B CG  1 
ATOM   3976 C CD1 . LEU B 1 38  ? 57.446 10.564 -42.711 1.00 14.95 ? 38   LEU B CD1 1 
ATOM   3977 C CD2 . LEU B 1 38  ? 57.552 12.439 -44.373 1.00 15.99 ? 38   LEU B CD2 1 
ATOM   3978 N N   . GLN B 1 39  ? 60.821 14.633 -40.698 1.00 9.03  ? 39   GLN B N   1 
ATOM   3979 C CA  . GLN B 1 39  ? 61.029 15.474 -39.520 1.00 9.93  ? 39   GLN B CA  1 
ATOM   3980 C C   . GLN B 1 39  ? 61.273 16.926 -39.923 1.00 9.93  ? 39   GLN B C   1 
ATOM   3981 O O   . GLN B 1 39  ? 60.729 17.838 -39.293 1.00 8.82  ? 39   GLN B O   1 
ATOM   3982 C CB  . GLN B 1 39  ? 62.170 14.925 -38.655 1.00 9.81  ? 39   GLN B CB  1 
ATOM   3983 C CG  . GLN B 1 39  ? 61.902 13.489 -38.157 1.00 9.98  ? 39   GLN B CG  1 
ATOM   3984 C CD  . GLN B 1 39  ? 62.904 13.008 -37.110 1.00 12.37 ? 39   GLN B CD  1 
ATOM   3985 O OE1 . GLN B 1 39  ? 63.190 13.696 -36.134 1.00 10.26 ? 39   GLN B OE1 1 
ATOM   3986 N NE2 . GLN B 1 39  ? 63.434 11.810 -37.315 1.00 10.80 ? 39   GLN B NE2 1 
ATOM   3987 N N   . ASN B 1 40  ? 62.066 17.158 -40.979 1.00 9.62  ? 40   ASN B N   1 
ATOM   3988 C CA  . ASN B 1 40  ? 62.198 18.507 -41.537 1.00 9.78  ? 40   ASN B CA  1 
ATOM   3989 C C   . ASN B 1 40  ? 60.835 19.097 -41.876 1.00 12.12 ? 40   ASN B C   1 
ATOM   3990 O O   . ASN B 1 40  ? 60.565 20.276 -41.605 1.00 9.61  ? 40   ASN B O   1 
ATOM   3991 C CB  . ASN B 1 40  ? 63.072 18.484 -42.798 1.00 7.95  ? 40   ASN B CB  1 
ATOM   3992 C CG  . ASN B 1 40  ? 64.564 18.470 -42.489 1.00 14.19 ? 40   ASN B CG  1 
ATOM   3993 O OD1 . ASN B 1 40  ? 64.979 18.649 -41.341 1.00 12.47 ? 40   ASN B OD1 1 
ATOM   3994 N ND2 . ASN B 1 40  ? 65.379 18.227 -43.517 1.00 10.67 ? 40   ASN B ND2 1 
ATOM   3995 N N   . GLN B 1 41  ? 59.968 18.292 -42.489 1.00 10.03 ? 41   GLN B N   1 
ATOM   3996 C CA  . GLN B 1 41  ? 58.651 18.772 -42.896 1.00 10.99 ? 41   GLN B CA  1 
ATOM   3997 C C   . GLN B 1 41  ? 57.786 19.121 -41.685 1.00 14.02 ? 41   GLN B C   1 
ATOM   3998 O O   . GLN B 1 41  ? 57.126 20.169 -41.661 1.00 11.60 ? 41   GLN B O   1 
ATOM   3999 C CB  . GLN B 1 41  ? 57.967 17.711 -43.762 1.00 12.35 ? 41   GLN B CB  1 
ATOM   4000 C CG  . GLN B 1 41  ? 58.591 17.543 -45.154 1.00 11.15 ? 41   GLN B CG  1 
ATOM   4001 C CD  . GLN B 1 41  ? 57.957 16.391 -45.932 1.00 12.92 ? 41   GLN B CD  1 
ATOM   4002 O OE1 . GLN B 1 41  ? 56.924 15.863 -45.529 1.00 13.63 ? 41   GLN B OE1 1 
ATOM   4003 N NE2 . GLN B 1 41  ? 58.558 16.020 -47.055 1.00 11.39 ? 41   GLN B NE2 1 
ATOM   4004 N N   . ALA B 1 42  ? 57.770 18.242 -40.674 1.00 10.77 ? 42   ALA B N   1 
ATOM   4005 C CA  . ALA B 1 42  ? 57.029 18.507 -39.441 1.00 13.09 ? 42   ALA B CA  1 
ATOM   4006 C C   . ALA B 1 42  ? 57.504 19.779 -38.739 1.00 16.96 ? 42   ALA B C   1 
ATOM   4007 O O   . ALA B 1 42  ? 56.717 20.441 -38.049 1.00 14.73 ? 42   ALA B O   1 
ATOM   4008 C CB  . ALA B 1 42  ? 57.161 17.321 -38.481 1.00 8.42  ? 42   ALA B CB  1 
ATOM   4009 N N   . ASN B 1 43  ? 58.778 20.127 -38.882 1.00 10.59 ? 43   ASN B N   1 
ATOM   4010 C CA  . ASN B 1 43  ? 59.318 21.331 -38.262 1.00 10.78 ? 43   ASN B CA  1 
ATOM   4011 C C   . ASN B 1 43  ? 59.162 22.571 -39.133 1.00 15.10 ? 43   ASN B C   1 
ATOM   4012 O O   . ASN B 1 43  ? 59.583 23.656 -38.717 1.00 14.05 ? 43   ASN B O   1 
ATOM   4013 C CB  . ASN B 1 43  ? 60.794 21.115 -37.922 1.00 12.29 ? 43   ASN B CB  1 
ATOM   4014 C CG  . ASN B 1 43  ? 60.989 20.447 -36.574 1.00 14.90 ? 43   ASN B CG  1 
ATOM   4015 O OD1 . ASN B 1 43  ? 61.490 21.057 -35.626 1.00 11.75 ? 43   ASN B OD1 1 
ATOM   4016 N ND2 . ASN B 1 43  ? 60.521 19.202 -36.464 1.00 12.30 ? 43   ASN B ND2 1 
ATOM   4017 N N   . GLY B 1 44  ? 58.585 22.438 -40.327 1.00 13.54 ? 44   GLY B N   1 
ATOM   4018 C CA  . GLY B 1 44  ? 58.494 23.579 -41.225 1.00 15.01 ? 44   GLY B CA  1 
ATOM   4019 C C   . GLY B 1 44  ? 59.813 23.986 -41.839 1.00 13.64 ? 44   GLY B C   1 
ATOM   4020 O O   . GLY B 1 44  ? 59.923 25.089 -42.371 1.00 14.55 ? 44   GLY B O   1 
ATOM   4021 N N   . VAL B 1 45  ? 60.832 23.122 -41.764 1.00 12.34 ? 45   VAL B N   1 
ATOM   4022 C CA  . VAL B 1 45  ? 62.139 23.443 -42.326 1.00 9.63  ? 45   VAL B CA  1 
ATOM   4023 C C   . VAL B 1 45  ? 62.083 23.422 -43.852 1.00 13.71 ? 45   VAL B C   1 
ATOM   4024 O O   . VAL B 1 45  ? 62.660 24.288 -44.523 1.00 10.23 ? 45   VAL B O   1 
ATOM   4025 C CB  . VAL B 1 45  ? 63.195 22.468 -41.771 1.00 11.36 ? 45   VAL B CB  1 
ATOM   4026 C CG1 . VAL B 1 45  ? 64.526 22.624 -42.506 1.00 11.08 ? 45   VAL B CG1 1 
ATOM   4027 C CG2 . VAL B 1 45  ? 63.379 22.691 -40.277 1.00 14.51 ? 45   VAL B CG2 1 
ATOM   4028 N N   . VAL B 1 46  ? 61.373 22.446 -44.419 1.00 10.19 ? 46   VAL B N   1 
ATOM   4029 C CA  . VAL B 1 46  ? 61.116 22.362 -45.848 1.00 11.90 ? 46   VAL B CA  1 
ATOM   4030 C C   . VAL B 1 46  ? 59.619 22.143 -46.009 1.00 13.57 ? 46   VAL B C   1 
ATOM   4031 O O   . VAL B 1 46  ? 58.923 21.736 -45.074 1.00 11.36 ? 46   VAL B O   1 
ATOM   4032 C CB  . VAL B 1 46  ? 61.901 21.217 -46.531 1.00 10.28 ? 46   VAL B CB  1 
ATOM   4033 C CG1 . VAL B 1 46  ? 63.390 21.354 -46.263 1.00 9.69  ? 46   VAL B CG1 1 
ATOM   4034 C CG2 . VAL B 1 46  ? 61.401 19.863 -46.019 1.00 9.32  ? 46   VAL B CG2 1 
ATOM   4035 N N   . SER B 1 47  ? 59.125 22.406 -47.214 1.00 11.96 ? 47   SER B N   1 
ATOM   4036 C CA  . SER B 1 47  ? 57.715 22.191 -47.480 1.00 12.49 ? 47   SER B CA  1 
ATOM   4037 C C   . SER B 1 47  ? 57.446 20.713 -47.754 1.00 13.81 ? 47   SER B C   1 
ATOM   4038 O O   . SER B 1 47  ? 58.362 19.891 -47.884 1.00 10.59 ? 47   SER B O   1 
ATOM   4039 C CB  . SER B 1 47  ? 57.252 23.037 -48.668 1.00 14.64 ? 47   SER B CB  1 
ATOM   4040 O OG  . SER B 1 47  ? 57.561 22.391 -49.894 1.00 12.99 ? 47   SER B OG  1 
ATOM   4041 N N   . ARG B 1 48  ? 56.162 20.381 -47.861 1.00 11.97 ? 48   ARG B N   1 
ATOM   4042 C CA  . ARG B 1 48  ? 55.722 19.034 -48.200 1.00 15.99 ? 48   ARG B CA  1 
ATOM   4043 C C   . ARG B 1 48  ? 55.557 18.829 -49.702 1.00 14.63 ? 48   ARG B C   1 
ATOM   4044 O O   . ARG B 1 48  ? 55.092 17.763 -50.119 1.00 13.41 ? 48   ARG B O   1 
ATOM   4045 C CB  . ARG B 1 48  ? 54.407 18.728 -47.479 1.00 13.74 ? 48   ARG B CB  1 
ATOM   4046 C CG  . ARG B 1 48  ? 54.590 18.695 -45.966 1.00 14.09 ? 48   ARG B CG  1 
ATOM   4047 C CD  . ARG B 1 48  ? 53.348 18.224 -45.224 1.00 18.06 ? 48   ARG B CD  1 
ATOM   4048 N NE  . ARG B 1 48  ? 53.614 18.196 -43.787 1.00 22.34 ? 48   ARG B NE  1 
ATOM   4049 C CZ  . ARG B 1 48  ? 53.623 19.263 -43.001 1.00 21.57 ? 48   ARG B CZ  1 
ATOM   4050 N NH1 . ARG B 1 48  ? 53.294 20.466 -43.459 1.00 20.93 ? 48   ARG B NH1 1 
ATOM   4051 N NH2 . ARG B 1 48  ? 53.971 19.121 -41.725 1.00 26.24 ? 48   ARG B NH2 1 
ATOM   4052 N N   . ASP B 1 49  ? 55.930 19.813 -50.521 1.00 12.08 ? 49   ASP B N   1 
ATOM   4053 C CA  . ASP B 1 49  ? 55.874 19.645 -51.970 1.00 13.37 ? 49   ASP B CA  1 
ATOM   4054 C C   . ASP B 1 49  ? 56.918 18.633 -52.439 1.00 11.00 ? 49   ASP B C   1 
ATOM   4055 O O   . ASP B 1 49  ? 57.993 18.506 -51.853 1.00 9.75  ? 49   ASP B O   1 
ATOM   4056 C CB  . ASP B 1 49  ? 56.102 20.987 -52.670 1.00 10.37 ? 49   ASP B CB  1 
ATOM   4057 C CG  . ASP B 1 49  ? 54.938 21.944 -52.485 1.00 12.78 ? 49   ASP B CG  1 
ATOM   4058 O OD1 . ASP B 1 49  ? 53.864 21.499 -52.027 1.00 14.30 ? 49   ASP B OD1 1 
ATOM   4059 O OD2 . ASP B 1 49  ? 55.099 23.141 -52.796 1.00 12.25 ? 49   ASP B OD2 1 
ATOM   4060 N N   . LEU B 1 50  ? 56.593 17.924 -53.517 1.00 10.58 ? 50   LEU B N   1 
ATOM   4061 C CA  . LEU B 1 50  ? 57.456 16.905 -54.106 1.00 12.20 ? 50   LEU B CA  1 
ATOM   4062 C C   . LEU B 1 50  ? 58.122 17.471 -55.358 1.00 10.99 ? 50   LEU B C   1 
ATOM   4063 O O   . LEU B 1 50  ? 57.436 17.829 -56.326 1.00 12.67 ? 50   LEU B O   1 
ATOM   4064 C CB  . LEU B 1 50  ? 56.651 15.652 -54.461 1.00 10.51 ? 50   LEU B CB  1 
ATOM   4065 C CG  . LEU B 1 50  ? 55.803 15.036 -53.337 1.00 15.86 ? 50   LEU B CG  1 
ATOM   4066 C CD1 . LEU B 1 50  ? 55.023 13.829 -53.835 1.00 19.80 ? 50   LEU B CD1 1 
ATOM   4067 C CD2 . LEU B 1 50  ? 56.713 14.631 -52.220 1.00 16.46 ? 50   LEU B CD2 1 
ATOM   4068 N N   . VAL B 1 51  ? 59.455 17.533 -55.349 1.00 10.08 ? 51   VAL B N   1 
ATOM   4069 C CA  . VAL B 1 51  ? 60.165 17.968 -56.549 1.00 9.78  ? 51   VAL B CA  1 
ATOM   4070 C C   . VAL B 1 51  ? 59.862 17.033 -57.720 1.00 13.73 ? 51   VAL B C   1 
ATOM   4071 O O   . VAL B 1 51  ? 59.868 17.462 -58.878 1.00 11.90 ? 51   VAL B O   1 
ATOM   4072 C CB  . VAL B 1 51  ? 61.686 18.068 -56.283 1.00 11.02 ? 51   VAL B CB  1 
ATOM   4073 C CG1 . VAL B 1 51  ? 62.299 16.682 -56.031 1.00 10.79 ? 51   VAL B CG1 1 
ATOM   4074 C CG2 . VAL B 1 51  ? 62.388 18.781 -57.436 1.00 11.23 ? 51   VAL B CG2 1 
ATOM   4075 N N   . GLU B 1 52  ? 59.557 15.755 -57.445 1.00 11.36 ? 52   GLU B N   1 
ATOM   4076 C CA  . GLU B 1 52  ? 59.288 14.797 -58.512 1.00 10.46 ? 52   GLU B CA  1 
ATOM   4077 C C   . GLU B 1 52  ? 57.896 14.952 -59.118 1.00 12.95 ? 52   GLU B C   1 
ATOM   4078 O O   . GLU B 1 52  ? 57.557 14.193 -60.034 1.00 13.68 ? 52   GLU B O   1 
ATOM   4079 C CB  . GLU B 1 52  ? 59.480 13.354 -58.013 1.00 10.76 ? 52   GLU B CB  1 
ATOM   4080 C CG  . GLU B 1 52  ? 58.520 12.897 -56.914 1.00 11.24 ? 52   GLU B CG  1 
ATOM   4081 C CD  . GLU B 1 52  ? 59.057 13.200 -55.514 1.00 15.97 ? 52   GLU B CD  1 
ATOM   4082 O OE1 . GLU B 1 52  ? 59.730 14.241 -55.325 1.00 12.71 ? 52   GLU B OE1 1 
ATOM   4083 O OE2 . GLU B 1 52  ? 58.831 12.382 -54.606 1.00 13.71 ? 52   GLU B OE2 1 
ATOM   4084 N N   . GLU B 1 53  ? 57.091 15.911 -58.648 1.00 12.74 ? 53   GLU B N   1 
ATOM   4085 C CA  . GLU B 1 53  ? 55.841 16.294 -59.300 1.00 13.75 ? 53   GLU B CA  1 
ATOM   4086 C C   . GLU B 1 53  ? 55.935 17.659 -59.985 1.00 12.56 ? 53   GLU B C   1 
ATOM   4087 O O   . GLU B 1 53  ? 54.921 18.339 -60.152 1.00 13.60 ? 53   GLU B O   1 
ATOM   4088 C CB  . GLU B 1 53  ? 54.691 16.295 -58.290 1.00 16.87 ? 53   GLU B CB  1 
ATOM   4089 C CG  . GLU B 1 53  ? 54.589 15.011 -57.468 1.00 20.51 ? 53   GLU B CG  1 
ATOM   4090 C CD  . GLU B 1 53  ? 53.246 14.874 -56.753 1.00 29.84 ? 53   GLU B CD  1 
ATOM   4091 O OE1 . GLU B 1 53  ? 52.842 15.840 -56.052 1.00 27.71 ? 53   GLU B OE1 1 
ATOM   4092 O OE2 . GLU B 1 53  ? 52.624 13.797 -56.857 1.00 32.68 ? 53   GLU B OE2 1 
ATOM   4093 N N   . GLY B 1 54  ? 57.125 18.054 -60.425 1.00 11.14 ? 54   GLY B N   1 
ATOM   4094 C CA  . GLY B 1 54  ? 57.370 19.392 -60.951 1.00 8.60  ? 54   GLY B CA  1 
ATOM   4095 C C   . GLY B 1 54  ? 57.107 19.561 -62.435 1.00 11.19 ? 54   GLY B C   1 
ATOM   4096 O O   . GLY B 1 54  ? 56.286 18.858 -63.031 1.00 9.44  ? 54   GLY B O   1 
ATOM   4097 N N   . ALA B 1 55  ? 57.844 20.504 -63.045 1.00 10.65 ? 55   ALA B N   1 
ATOM   4098 C CA  . ALA B 1 55  ? 57.539 21.044 -64.368 1.00 12.63 ? 55   ALA B CA  1 
ATOM   4099 C C   . ALA B 1 55  ? 57.931 20.129 -65.524 1.00 11.15 ? 55   ALA B C   1 
ATOM   4100 O O   . ALA B 1 55  ? 57.534 20.404 -66.662 1.00 10.99 ? 55   ALA B O   1 
ATOM   4101 C CB  . ALA B 1 55  ? 58.236 22.393 -64.553 1.00 8.94  ? 55   ALA B CB  1 
ATOM   4102 N N   . ASP B 1 56  ? 58.724 19.087 -65.274 1.00 8.56  ? 56   ASP B N   1 
ATOM   4103 C CA  . ASP B 1 56  ? 59.064 18.079 -66.286 1.00 12.91 ? 56   ASP B CA  1 
ATOM   4104 C C   . ASP B 1 56  ? 59.894 18.687 -67.430 1.00 11.03 ? 56   ASP B C   1 
ATOM   4105 O O   . ASP B 1 56  ? 59.666 18.407 -68.607 1.00 11.78 ? 56   ASP B O   1 
ATOM   4106 C CB  . ASP B 1 56  ? 57.796 17.391 -66.824 1.00 11.99 ? 56   ASP B CB  1 
ATOM   4107 C CG  . ASP B 1 56  ? 58.098 16.325 -67.883 1.00 21.25 ? 56   ASP B CG  1 
ATOM   4108 O OD1 . ASP B 1 56  ? 59.063 15.541 -67.691 1.00 18.86 ? 56   ASP B OD1 1 
ATOM   4109 O OD2 . ASP B 1 56  ? 57.358 16.258 -68.890 1.00 18.73 ? 56   ASP B OD2 1 
ATOM   4110 N N   . TYR B 1 57  ? 60.875 19.524 -67.092 1.00 9.89  ? 57   TYR B N   1 
ATOM   4111 C CA  . TYR B 1 57  ? 61.774 20.042 -68.125 1.00 10.40 ? 57   TYR B CA  1 
ATOM   4112 C C   . TYR B 1 57  ? 62.562 18.919 -68.796 1.00 10.38 ? 57   TYR B C   1 
ATOM   4113 O O   . TYR B 1 57  ? 62.946 19.038 -69.965 1.00 8.14  ? 57   TYR B O   1 
ATOM   4114 C CB  . TYR B 1 57  ? 62.730 21.066 -67.517 1.00 7.31  ? 57   TYR B CB  1 
ATOM   4115 C CG  . TYR B 1 57  ? 63.754 21.653 -68.467 1.00 9.30  ? 57   TYR B CG  1 
ATOM   4116 C CD1 . TYR B 1 57  ? 63.371 22.464 -69.534 1.00 7.17  ? 57   TYR B CD1 1 
ATOM   4117 C CD2 . TYR B 1 57  ? 65.104 21.389 -68.297 1.00 11.27 ? 57   TYR B CD2 1 
ATOM   4118 C CE1 . TYR B 1 57  ? 64.319 23.018 -70.385 1.00 11.41 ? 57   TYR B CE1 1 
ATOM   4119 C CE2 . TYR B 1 57  ? 66.054 21.917 -69.150 1.00 9.36  ? 57   TYR B CE2 1 
ATOM   4120 C CZ  . TYR B 1 57  ? 65.661 22.726 -70.192 1.00 11.71 ? 57   TYR B CZ  1 
ATOM   4121 O OH  . TYR B 1 57  ? 66.630 23.263 -71.015 1.00 9.86  ? 57   TYR B OH  1 
ATOM   4122 N N   . TRP B 1 58  ? 62.806 17.827 -68.074 1.00 11.06 ? 58   TRP B N   1 
ATOM   4123 C CA  . TRP B 1 58  ? 63.565 16.705 -68.626 1.00 12.56 ? 58   TRP B CA  1 
ATOM   4124 C C   . TRP B 1 58  ? 62.990 16.214 -69.952 1.00 14.01 ? 58   TRP B C   1 
ATOM   4125 O O   . TRP B 1 58  ? 63.739 15.857 -70.864 1.00 13.57 ? 58   TRP B O   1 
ATOM   4126 C CB  . TRP B 1 58  ? 63.586 15.564 -67.615 1.00 12.49 ? 58   TRP B CB  1 
ATOM   4127 C CG  . TRP B 1 58  ? 64.528 14.443 -67.959 1.00 13.68 ? 58   TRP B CG  1 
ATOM   4128 C CD1 . TRP B 1 58  ? 64.190 13.198 -68.415 1.00 14.97 ? 58   TRP B CD1 1 
ATOM   4129 C CD2 . TRP B 1 58  ? 65.959 14.454 -67.846 1.00 13.21 ? 58   TRP B CD2 1 
ATOM   4130 N NE1 . TRP B 1 58  ? 65.321 12.435 -68.590 1.00 13.63 ? 58   TRP B NE1 1 
ATOM   4131 C CE2 . TRP B 1 58  ? 66.418 13.180 -68.248 1.00 14.61 ? 58   TRP B CE2 1 
ATOM   4132 C CE3 . TRP B 1 58  ? 66.893 15.409 -67.432 1.00 13.36 ? 58   TRP B CE3 1 
ATOM   4133 C CZ2 . TRP B 1 58  ? 67.774 12.842 -68.265 1.00 17.15 ? 58   TRP B CZ2 1 
ATOM   4134 C CZ3 . TRP B 1 58  ? 68.244 15.069 -67.447 1.00 14.09 ? 58   TRP B CZ3 1 
ATOM   4135 C CH2 . TRP B 1 58  ? 68.666 13.797 -67.862 1.00 13.60 ? 58   TRP B CH2 1 
ATOM   4136 N N   . ASN B 1 59  ? 61.663 16.156 -70.061 1.00 13.68 ? 59   ASN B N   1 
ATOM   4137 C CA  . ASN B 1 59  ? 60.966 15.694 -71.256 1.00 14.93 ? 59   ASN B CA  1 
ATOM   4138 C C   . ASN B 1 59  ? 60.309 16.812 -72.045 1.00 13.76 ? 59   ASN B C   1 
ATOM   4139 O O   . ASN B 1 59  ? 60.113 16.660 -73.251 1.00 13.09 ? 59   ASN B O   1 
ATOM   4140 C CB  . ASN B 1 59  ? 59.875 14.678 -70.886 1.00 13.54 ? 59   ASN B CB  1 
ATOM   4141 C CG  . ASN B 1 59  ? 60.440 13.409 -70.271 1.00 18.08 ? 59   ASN B CG  1 
ATOM   4142 O OD1 . ASN B 1 59  ? 61.165 12.659 -70.925 1.00 14.60 ? 59   ASN B OD1 1 
ATOM   4143 N ND2 . ASN B 1 59  ? 60.130 13.180 -68.998 1.00 13.59 ? 59   ASN B ND2 1 
ATOM   4144 N N   . SER B 1 60  ? 59.959 17.921 -71.395 1.00 8.98  ? 60   SER B N   1 
ATOM   4145 C CA  . SER B 1 60  ? 59.232 19.003 -72.041 1.00 14.54 ? 60   SER B CA  1 
ATOM   4146 C C   . SER B 1 60  ? 60.134 20.163 -72.438 1.00 11.42 ? 60   SER B C   1 
ATOM   4147 O O   . SER B 1 60  ? 59.635 21.270 -72.669 1.00 12.96 ? 60   SER B O   1 
ATOM   4148 C CB  . SER B 1 60  ? 58.110 19.500 -71.123 1.00 16.44 ? 60   SER B CB  1 
ATOM   4149 O OG  . SER B 1 60  ? 57.198 18.452 -70.831 1.00 18.19 ? 60   SER B OG  1 
ATOM   4150 N N   . TYR B 1 61  ? 61.451 19.936 -72.539 1.00 10.14 ? 61   TYR B N   1 
ATOM   4151 C CA  . TYR B 1 61  ? 62.365 21.051 -72.797 1.00 11.23 ? 61   TYR B CA  1 
ATOM   4152 C C   . TYR B 1 61  ? 62.045 21.789 -74.094 1.00 11.13 ? 61   TYR B C   1 
ATOM   4153 O O   . TYR B 1 61  ? 62.231 23.010 -74.161 1.00 9.58  ? 61   TYR B O   1 
ATOM   4154 C CB  . TYR B 1 61  ? 63.820 20.567 -72.822 1.00 9.81  ? 61   TYR B CB  1 
ATOM   4155 C CG  . TYR B 1 61  ? 64.059 19.396 -73.749 1.00 9.08  ? 61   TYR B CG  1 
ATOM   4156 C CD1 . TYR B 1 61  ? 63.911 18.093 -73.297 1.00 12.01 ? 61   TYR B CD1 1 
ATOM   4157 C CD2 . TYR B 1 61  ? 64.451 19.599 -75.071 1.00 12.10 ? 61   TYR B CD2 1 
ATOM   4158 C CE1 . TYR B 1 61  ? 64.133 17.016 -74.135 1.00 13.60 ? 61   TYR B CE1 1 
ATOM   4159 C CE2 . TYR B 1 61  ? 64.676 18.519 -75.925 1.00 14.86 ? 61   TYR B CE2 1 
ATOM   4160 C CZ  . TYR B 1 61  ? 64.516 17.229 -75.442 1.00 14.07 ? 61   TYR B CZ  1 
ATOM   4161 O OH  . TYR B 1 61  ? 64.732 16.146 -76.266 1.00 14.85 ? 61   TYR B OH  1 
ATOM   4162 N N   . ALA B 1 62  ? 61.556 21.091 -75.130 1.00 11.91 ? 62   ALA B N   1 
ATOM   4163 C CA  . ALA B 1 62  ? 61.227 21.782 -76.380 1.00 12.29 ? 62   ALA B CA  1 
ATOM   4164 C C   . ALA B 1 62  ? 60.153 22.842 -76.153 1.00 11.48 ? 62   ALA B C   1 
ATOM   4165 O O   . ALA B 1 62  ? 60.280 23.976 -76.635 1.00 10.31 ? 62   ALA B O   1 
ATOM   4166 C CB  . ALA B 1 62  ? 60.790 20.787 -77.470 1.00 13.44 ? 62   ALA B CB  1 
ATOM   4167 N N   . ARG B 1 63  ? 59.105 22.505 -75.390 1.00 10.65 ? 63   ARG B N   1 
ATOM   4168 C CA  . ARG B 1 63  ? 58.064 23.486 -75.080 1.00 13.83 ? 63   ARG B CA  1 
ATOM   4169 C C   . ARG B 1 63  ? 58.645 24.693 -74.355 1.00 12.57 ? 63   ARG B C   1 
ATOM   4170 O O   . ARG B 1 63  ? 58.283 25.836 -74.653 1.00 11.91 ? 63   ARG B O   1 
ATOM   4171 C CB  . ARG B 1 63  ? 56.944 22.858 -74.231 1.00 12.91 ? 63   ARG B CB  1 
ATOM   4172 C CG  . ARG B 1 63  ? 55.869 22.098 -75.002 1.00 23.48 ? 63   ARG B CG  1 
ATOM   4173 C CD  . ARG B 1 63  ? 54.630 21.788 -74.103 1.00 28.17 ? 63   ARG B CD  1 
ATOM   4174 N NE  . ARG B 1 63  ? 54.938 20.941 -72.953 1.00 30.14 ? 63   ARG B NE  1 
ATOM   4175 C CZ  . ARG B 1 63  ? 54.299 20.963 -71.785 1.00 33.95 ? 63   ARG B CZ  1 
ATOM   4176 N NH1 . ARG B 1 63  ? 53.324 21.826 -71.539 1.00 28.62 ? 63   ARG B NH1 1 
ATOM   4177 N NH2 . ARG B 1 63  ? 54.649 20.095 -70.838 1.00 27.81 ? 63   ARG B NH2 1 
ATOM   4178 N N   . VAL B 1 64  ? 59.550 24.453 -73.403 1.00 11.95 ? 64   VAL B N   1 
ATOM   4179 C CA  . VAL B 1 64  ? 60.156 25.540 -72.637 1.00 8.65  ? 64   VAL B CA  1 
ATOM   4180 C C   . VAL B 1 64  ? 61.034 26.403 -73.530 1.00 11.88 ? 64   VAL B C   1 
ATOM   4181 O O   . VAL B 1 64  ? 60.976 27.637 -73.474 1.00 9.41  ? 64   VAL B O   1 
ATOM   4182 C CB  . VAL B 1 64  ? 60.953 24.976 -71.449 1.00 8.93  ? 64   VAL B CB  1 
ATOM   4183 C CG1 . VAL B 1 64  ? 61.735 26.109 -70.726 1.00 8.93  ? 64   VAL B CG1 1 
ATOM   4184 C CG2 . VAL B 1 64  ? 60.010 24.233 -70.492 1.00 11.18 ? 64   VAL B CG2 1 
ATOM   4185 N N   . HIS B 1 65  ? 61.869 25.767 -74.361 1.00 10.83 ? 65   HIS B N   1 
ATOM   4186 C CA  . HIS B 1 65  ? 62.703 26.531 -75.288 1.00 13.04 ? 65   HIS B CA  1 
ATOM   4187 C C   . HIS B 1 65  ? 61.856 27.351 -76.253 1.00 11.39 ? 65   HIS B C   1 
ATOM   4188 O O   . HIS B 1 65  ? 62.238 28.469 -76.618 1.00 12.98 ? 65   HIS B O   1 
ATOM   4189 C CB  . HIS B 1 65  ? 63.637 25.597 -76.060 1.00 11.08 ? 65   HIS B CB  1 
ATOM   4190 C CG  . HIS B 1 65  ? 64.588 24.836 -75.182 1.00 9.58  ? 65   HIS B CG  1 
ATOM   4191 N ND1 . HIS B 1 65  ? 65.210 23.674 -75.590 1.00 8.32  ? 65   HIS B ND1 1 
ATOM   4192 C CD2 . HIS B 1 65  ? 65.021 25.073 -73.918 1.00 9.01  ? 65   HIS B CD2 1 
ATOM   4193 C CE1 . HIS B 1 65  ? 65.993 23.230 -74.619 1.00 9.58  ? 65   HIS B CE1 1 
ATOM   4194 N NE2 . HIS B 1 65  ? 65.890 24.057 -73.588 1.00 11.58 ? 65   HIS B NE2 1 
ATOM   4195 N N   . GLU B 1 66  ? 60.706 26.816 -76.682 1.00 10.19 ? 66   GLU B N   1 
ATOM   4196 C CA  . GLU B 1 66  ? 59.891 27.557 -77.638 1.00 13.60 ? 66   GLU B CA  1 
ATOM   4197 C C   . GLU B 1 66  ? 59.253 28.774 -76.983 1.00 11.91 ? 66   GLU B C   1 
ATOM   4198 O O   . GLU B 1 66  ? 59.095 29.817 -77.631 1.00 12.37 ? 66   GLU B O   1 
ATOM   4199 C CB  . GLU B 1 66  ? 58.827 26.656 -78.276 1.00 12.73 ? 66   GLU B CB  1 
ATOM   4200 C CG  . GLU B 1 66  ? 59.449 25.590 -79.177 1.00 16.26 ? 66   GLU B CG  1 
ATOM   4201 C CD  . GLU B 1 66  ? 58.561 24.390 -79.424 1.00 19.96 ? 66   GLU B CD  1 
ATOM   4202 O OE1 . GLU B 1 66  ? 59.005 23.477 -80.151 1.00 25.32 ? 66   GLU B OE1 1 
ATOM   4203 O OE2 . GLU B 1 66  ? 57.407 24.381 -78.945 1.00 22.35 ? 66   GLU B OE2 1 
ATOM   4204 N N   . LEU B 1 67  ? 58.889 28.668 -75.699 1.00 9.38  ? 67   LEU B N   1 
ATOM   4205 C CA  . LEU B 1 67  ? 58.425 29.850 -74.978 1.00 12.37 ? 67   LEU B CA  1 
ATOM   4206 C C   . LEU B 1 67  ? 59.453 30.969 -75.067 1.00 10.98 ? 67   LEU B C   1 
ATOM   4207 O O   . LEU B 1 67  ? 59.100 32.144 -75.235 1.00 10.17 ? 67   LEU B O   1 
ATOM   4208 C CB  . LEU B 1 67  ? 58.157 29.515 -73.505 1.00 10.46 ? 67   LEU B CB  1 
ATOM   4209 C CG  . LEU B 1 67  ? 56.943 28.648 -73.173 1.00 13.83 ? 67   LEU B CG  1 
ATOM   4210 C CD1 . LEU B 1 67  ? 57.038 28.179 -71.719 1.00 15.50 ? 67   LEU B CD1 1 
ATOM   4211 C CD2 . LEU B 1 67  ? 55.664 29.410 -73.423 1.00 12.55 ? 67   LEU B CD2 1 
ATOM   4212 N N   . CYS B 1 68  ? 60.741 30.618 -74.962 1.00 9.65  ? 68   CYS B N   1 
ATOM   4213 C CA  . CYS B 1 68  ? 61.793 31.630 -75.006 1.00 9.55  ? 68   CYS B CA  1 
ATOM   4214 C C   . CYS B 1 68  ? 61.960 32.195 -76.414 1.00 10.78 ? 68   CYS B C   1 
ATOM   4215 O O   . CYS B 1 68  ? 62.025 33.416 -76.601 1.00 10.50 ? 68   CYS B O   1 
ATOM   4216 C CB  . CYS B 1 68  ? 63.118 31.032 -74.521 1.00 10.41 ? 68   CYS B CB  1 
ATOM   4217 S SG  . CYS B 1 68  ? 63.075 30.465 -72.810 1.00 13.31 ? 68   CYS B SG  1 
ATOM   4218 N N   . SER B 1 69  ? 62.058 31.320 -77.417 1.00 10.30 ? 69   SER B N   1 
ATOM   4219 C CA  . SER B 1 69  ? 62.382 31.796 -78.762 1.00 14.74 ? 69   SER B CA  1 
ATOM   4220 C C   . SER B 1 69  ? 61.212 32.530 -79.407 1.00 12.39 ? 69   SER B C   1 
ATOM   4221 O O   . SER B 1 69  ? 61.429 33.417 -80.238 1.00 13.20 ? 69   SER B O   1 
ATOM   4222 C CB  . SER B 1 69  ? 62.839 30.633 -79.647 1.00 10.37 ? 69   SER B CB  1 
ATOM   4223 O OG  . SER B 1 69  ? 61.865 29.611 -79.703 1.00 12.07 ? 69   SER B OG  1 
ATOM   4224 N N   . ARG B 1 70  ? 59.973 32.204 -79.035 1.00 12.29 ? 70   ARG B N   1 
ATOM   4225 C CA  . ARG B 1 70  ? 58.835 32.903 -79.641 1.00 13.43 ? 70   ARG B CA  1 
ATOM   4226 C C   . ARG B 1 70  ? 58.791 34.378 -79.255 1.00 16.00 ? 70   ARG B C   1 
ATOM   4227 O O   . ARG B 1 70  ? 58.275 35.196 -80.025 1.00 16.50 ? 70   ARG B O   1 
ATOM   4228 C CB  . ARG B 1 70  ? 57.543 32.176 -79.272 1.00 14.80 ? 70   ARG B CB  1 
ATOM   4229 C CG  . ARG B 1 70  ? 57.421 30.845 -80.012 1.00 17.52 ? 70   ARG B CG  1 
ATOM   4230 C CD  . ARG B 1 70  ? 56.164 30.055 -79.662 1.00 20.98 ? 70   ARG B CD  1 
ATOM   4231 N NE  . ARG B 1 70  ? 56.147 28.795 -80.399 1.00 18.69 ? 70   ARG B NE  1 
ATOM   4232 C CZ  . ARG B 1 70  ? 55.199 27.870 -80.300 1.00 25.27 ? 70   ARG B CZ  1 
ATOM   4233 N NH1 . ARG B 1 70  ? 54.199 27.995 -79.442 1.00 25.09 ? 70   ARG B NH1 1 
ATOM   4234 N NH2 . ARG B 1 70  ? 55.251 26.796 -81.088 1.00 18.09 ? 70   ARG B NH2 1 
ATOM   4235 N N   . ILE B 1 71  ? 59.341 34.723 -78.079 1.00 11.13 ? 71   ILE B N   1 
ATOM   4236 C CA  . ILE B 1 71  ? 59.593 36.102 -77.624 1.00 16.03 ? 71   ILE B CA  1 
ATOM   4237 C C   . ILE B 1 71  ? 60.900 36.713 -78.107 1.00 13.75 ? 71   ILE B C   1 
ATOM   4238 O O   . ILE B 1 71  ? 61.175 37.878 -77.791 1.00 12.17 ? 71   ILE B O   1 
ATOM   4239 C CB  . ILE B 1 71  ? 59.431 36.027 -76.084 1.00 17.08 ? 71   ILE B CB  1 
ATOM   4240 C CG1 . ILE B 1 71  ? 58.010 35.639 -75.810 1.00 25.33 ? 71   ILE B CG1 1 
ATOM   4241 C CG2 . ILE B 1 71  ? 59.840 37.235 -75.319 1.00 31.70 ? 71   ILE B CG2 1 
ATOM   4242 C CD1 . ILE B 1 71  ? 57.035 36.538 -76.509 1.00 18.72 ? 71   ILE B CD1 1 
ATOM   4243 N N   . GLY B 1 72  ? 61.693 35.998 -78.893 1.00 14.07 ? 72   GLY B N   1 
ATOM   4244 C CA  . GLY B 1 72  ? 62.933 36.593 -79.361 1.00 13.00 ? 72   GLY B CA  1 
ATOM   4245 C C   . GLY B 1 72  ? 64.064 36.563 -78.360 1.00 14.02 ? 72   GLY B C   1 
ATOM   4246 O O   . GLY B 1 72  ? 65.071 37.252 -78.565 1.00 12.70 ? 72   GLY B O   1 
ATOM   4247 N N   . MET B 1 73  ? 63.947 35.785 -77.282 1.00 11.54 ? 73   MET B N   1 
ATOM   4248 C CA  . MET B 1 73  ? 65.126 35.575 -76.450 1.00 11.16 ? 73   MET B CA  1 
ATOM   4249 C C   . MET B 1 73  ? 66.204 34.893 -77.270 1.00 14.31 ? 73   MET B C   1 
ATOM   4250 O O   . MET B 1 73  ? 65.921 34.170 -78.229 1.00 9.63  ? 73   MET B O   1 
ATOM   4251 C CB  . MET B 1 73  ? 64.802 34.751 -75.199 1.00 10.41 ? 73   MET B CB  1 
ATOM   4252 C CG  . MET B 1 73  ? 63.770 35.393 -74.291 1.00 12.00 ? 73   MET B CG  1 
ATOM   4253 S SD  . MET B 1 73  ? 63.368 34.352 -72.887 1.00 14.31 ? 73   MET B SD  1 
ATOM   4254 C CE  . MET B 1 73  ? 62.338 35.466 -71.951 1.00 23.91 ? 73   MET B CE  1 
ATOM   4255 N N   . ASN B 1 74  ? 67.460 35.142 -76.893 1.00 10.41 ? 74   ASN B N   1 
ATOM   4256 C CA  . ASN B 1 74  ? 68.577 34.568 -77.627 1.00 11.58 ? 74   ASN B CA  1 
ATOM   4257 C C   . ASN B 1 74  ? 69.609 33.917 -76.712 1.00 13.39 ? 74   ASN B C   1 
ATOM   4258 O O   . ASN B 1 74  ? 70.724 33.631 -77.168 1.00 10.35 ? 74   ASN B O   1 
ATOM   4259 C CB  . ASN B 1 74  ? 69.236 35.627 -78.531 1.00 10.58 ? 74   ASN B CB  1 
ATOM   4260 C CG  . ASN B 1 74  ? 69.716 36.857 -77.763 1.00 14.22 ? 74   ASN B CG  1 
ATOM   4261 O OD1 . ASN B 1 74  ? 69.632 36.916 -76.542 1.00 14.31 ? 74   ASN B OD1 1 
ATOM   4262 N ND2 . ASN B 1 74  ? 70.199 37.852 -78.486 1.00 16.79 ? 74   ASN B ND2 1 
ATOM   4263 N N   . VAL B 1 75  ? 69.280 33.682 -75.435 1.00 10.08 ? 75   VAL B N   1 
ATOM   4264 C CA  . VAL B 1 75  ? 70.173 32.950 -74.536 1.00 9.35  ? 75   VAL B CA  1 
ATOM   4265 C C   . VAL B 1 75  ? 69.321 32.203 -73.522 1.00 14.50 ? 75   VAL B C   1 
ATOM   4266 O O   . VAL B 1 75  ? 68.224 32.643 -73.150 1.00 7.57  ? 75   VAL B O   1 
ATOM   4267 C CB  . VAL B 1 75  ? 71.203 33.879 -73.830 1.00 11.20 ? 75   VAL B CB  1 
ATOM   4268 C CG1 . VAL B 1 75  ? 70.514 34.846 -72.870 1.00 8.16  ? 75   VAL B CG1 1 
ATOM   4269 C CG2 . VAL B 1 75  ? 72.286 33.059 -73.069 1.00 11.37 ? 75   VAL B CG2 1 
ATOM   4270 N N   . ILE B 1 76  ? 69.833 31.059 -73.078 1.00 8.19  ? 76   ILE B N   1 
ATOM   4271 C CA  . ILE B 1 76  ? 69.285 30.359 -71.928 1.00 8.86  ? 76   ILE B CA  1 
ATOM   4272 C C   . ILE B 1 76  ? 70.450 29.756 -71.150 1.00 13.10 ? 76   ILE B C   1 
ATOM   4273 O O   . ILE B 1 76  ? 71.432 29.286 -71.739 1.00 10.92 ? 76   ILE B O   1 
ATOM   4274 C CB  . ILE B 1 76  ? 68.261 29.282 -72.346 1.00 8.96  ? 76   ILE B CB  1 
ATOM   4275 C CG1 . ILE B 1 76  ? 67.584 28.682 -71.114 1.00 13.11 ? 76   ILE B CG1 1 
ATOM   4276 C CG2 . ILE B 1 76  ? 68.921 28.192 -73.172 1.00 9.97  ? 76   ILE B CG2 1 
ATOM   4277 C CD1 . ILE B 1 76  ? 66.324 27.900 -71.427 1.00 15.20 ? 76   ILE B CD1 1 
ATOM   4278 N N   . ARG B 1 77  ? 70.359 29.806 -69.828 1.00 8.79  ? 77   ARG B N   1 
ATOM   4279 C CA  . ARG B 1 77  ? 71.337 29.171 -68.955 1.00 10.43 ? 77   ARG B CA  1 
ATOM   4280 C C   . ARG B 1 77  ? 70.660 27.990 -68.286 1.00 11.61 ? 77   ARG B C   1 
ATOM   4281 O O   . ARG B 1 77  ? 69.599 28.143 -67.670 1.00 9.39  ? 77   ARG B O   1 
ATOM   4282 C CB  . ARG B 1 77  ? 71.879 30.152 -67.914 1.00 9.18  ? 77   ARG B CB  1 
ATOM   4283 C CG  . ARG B 1 77  ? 72.977 29.561 -67.012 1.00 10.09 ? 77   ARG B CG  1 
ATOM   4284 C CD  . ARG B 1 77  ? 72.429 29.242 -65.622 1.00 10.22 ? 77   ARG B CD  1 
ATOM   4285 N NE  . ARG B 1 77  ? 72.060 30.448 -64.885 1.00 9.72  ? 77   ARG B NE  1 
ATOM   4286 C CZ  . ARG B 1 77  ? 71.909 30.482 -63.565 1.00 12.44 ? 77   ARG B CZ  1 
ATOM   4287 N NH1 . ARG B 1 77  ? 72.014 29.386 -62.832 1.00 7.72  ? 77   ARG B NH1 1 
ATOM   4288 N NH2 . ARG B 1 77  ? 71.661 31.644 -62.968 1.00 8.37  ? 77   ARG B NH2 1 
ATOM   4289 N N   . ILE B 1 78  ? 71.258 26.810 -68.418 1.00 11.16 ? 78   ILE B N   1 
ATOM   4290 C CA  . ILE B 1 78  ? 70.679 25.598 -67.857 1.00 9.75  ? 78   ILE B CA  1 
ATOM   4291 C C   . ILE B 1 78  ? 71.705 24.964 -66.929 1.00 13.52 ? 78   ILE B C   1 
ATOM   4292 O O   . ILE B 1 78  ? 72.917 25.158 -67.081 1.00 14.89 ? 78   ILE B O   1 
ATOM   4293 C CB  . ILE B 1 78  ? 70.230 24.609 -68.960 1.00 13.80 ? 78   ILE B CB  1 
ATOM   4294 C CG1 . ILE B 1 78  ? 71.428 23.900 -69.565 1.00 19.65 ? 78   ILE B CG1 1 
ATOM   4295 C CG2 . ILE B 1 78  ? 69.460 25.323 -70.081 1.00 10.69 ? 78   ILE B CG2 1 
ATOM   4296 C CD1 . ILE B 1 78  ? 71.031 22.786 -70.491 1.00 25.84 ? 78   ILE B CD1 1 
ATOM   4297 N N   . GLY B 1 79  ? 71.210 24.230 -65.940 1.00 10.39 ? 79   GLY B N   1 
ATOM   4298 C CA  . GLY B 1 79  ? 72.064 23.487 -65.029 1.00 10.44 ? 79   GLY B CA  1 
ATOM   4299 C C   . GLY B 1 79  ? 72.135 22.031 -65.457 1.00 14.50 ? 79   GLY B C   1 
ATOM   4300 O O   . GLY B 1 79  ? 71.156 21.472 -65.958 1.00 14.14 ? 79   GLY B O   1 
ATOM   4301 N N   . ILE B 1 80  ? 73.324 21.436 -65.279 1.00 10.09 ? 80   ILE B N   1 
ATOM   4302 C CA  . ILE B 1 80  ? 73.556 19.999 -65.422 1.00 15.07 ? 80   ILE B CA  1 
ATOM   4303 C C   . ILE B 1 80  ? 73.701 19.428 -64.021 1.00 9.19  ? 80   ILE B C   1 
ATOM   4304 O O   . ILE B 1 80  ? 74.387 20.024 -63.187 1.00 11.11 ? 80   ILE B O   1 
ATOM   4305 C CB  . ILE B 1 80  ? 74.830 19.699 -66.242 1.00 16.58 ? 80   ILE B CB  1 
ATOM   4306 C CG1 . ILE B 1 80  ? 74.706 20.136 -67.695 1.00 21.90 ? 80   ILE B CG1 1 
ATOM   4307 C CG2 . ILE B 1 80  ? 75.140 18.219 -66.204 1.00 26.99 ? 80   ILE B CG2 1 
ATOM   4308 C CD1 . ILE B 1 80  ? 73.384 20.119 -68.214 1.00 21.46 ? 80   ILE B CD1 1 
ATOM   4309 N N   . GLU B 1 81  ? 73.075 18.280 -63.759 1.00 10.01 ? 81   GLU B N   1 
ATOM   4310 C CA  . GLU B 1 81  ? 73.135 17.648 -62.440 1.00 12.09 ? 81   GLU B CA  1 
ATOM   4311 C C   . GLU B 1 81  ? 74.307 16.671 -62.390 1.00 12.41 ? 81   GLU B C   1 
ATOM   4312 O O   . GLU B 1 81  ? 74.314 15.651 -63.088 1.00 12.09 ? 81   GLU B O   1 
ATOM   4313 C CB  . GLU B 1 81  ? 71.819 16.942 -62.103 1.00 9.01  ? 81   GLU B CB  1 
ATOM   4314 C CG  . GLU B 1 81  ? 70.668 17.913 -61.776 1.00 11.24 ? 81   GLU B CG  1 
ATOM   4315 C CD  . GLU B 1 81  ? 70.884 18.656 -60.449 1.00 12.39 ? 81   GLU B CD  1 
ATOM   4316 O OE1 . GLU B 1 81  ? 70.455 18.148 -59.389 1.00 12.38 ? 81   GLU B OE1 1 
ATOM   4317 O OE2 . GLU B 1 81  ? 71.511 19.741 -60.467 1.00 12.56 ? 81   GLU B OE2 1 
ATOM   4318 N N   . TRP B 1 82  ? 75.297 17.001 -61.560 1.00 12.22 ? 82   TRP B N   1 
ATOM   4319 C CA  . TRP B 1 82  ? 76.386 16.088 -61.227 1.00 10.64 ? 82   TRP B CA  1 
ATOM   4320 C C   . TRP B 1 82  ? 75.848 14.719 -60.812 1.00 9.75  ? 82   TRP B C   1 
ATOM   4321 O O   . TRP B 1 82  ? 76.352 13.682 -61.259 1.00 11.14 ? 82   TRP B O   1 
ATOM   4322 C CB  . TRP B 1 82  ? 77.208 16.752 -60.117 1.00 9.22  ? 82   TRP B CB  1 
ATOM   4323 C CG  . TRP B 1 82  ? 78.514 16.140 -59.679 1.00 9.53  ? 82   TRP B CG  1 
ATOM   4324 C CD1 . TRP B 1 82  ? 79.149 15.026 -60.186 1.00 10.45 ? 82   TRP B CD1 1 
ATOM   4325 C CD2 . TRP B 1 82  ? 79.374 16.670 -58.667 1.00 8.47  ? 82   TRP B CD2 1 
ATOM   4326 N NE1 . TRP B 1 82  ? 80.347 14.825 -59.518 1.00 8.44  ? 82   TRP B NE1 1 
ATOM   4327 C CE2 . TRP B 1 82  ? 80.506 15.824 -58.586 1.00 10.16 ? 82   TRP B CE2 1 
ATOM   4328 C CE3 . TRP B 1 82  ? 79.294 17.783 -57.811 1.00 9.65  ? 82   TRP B CE3 1 
ATOM   4329 C CZ2 . TRP B 1 82  ? 81.553 16.055 -57.682 1.00 8.03  ? 82   TRP B CZ2 1 
ATOM   4330 C CZ3 . TRP B 1 82  ? 80.339 18.012 -56.902 1.00 7.94  ? 82   TRP B CZ3 1 
ATOM   4331 C CH2 . TRP B 1 82  ? 81.453 17.148 -56.854 1.00 7.05  ? 82   TRP B CH2 1 
ATOM   4332 N N   . SER B 1 83  ? 74.768 14.706 -60.024 1.00 9.42  ? 83   SER B N   1 
ATOM   4333 C CA  . SER B 1 83  ? 74.192 13.473 -59.494 1.00 9.70  ? 83   SER B CA  1 
ATOM   4334 C C   . SER B 1 83  ? 73.616 12.564 -60.583 1.00 13.40 ? 83   SER B C   1 
ATOM   4335 O O   . SER B 1 83  ? 73.455 11.355 -60.357 1.00 13.11 ? 83   SER B O   1 
ATOM   4336 C CB  . SER B 1 83  ? 73.081 13.816 -58.500 1.00 10.66 ? 83   SER B CB  1 
ATOM   4337 O OG  . SER B 1 83  ? 72.071 14.587 -59.163 1.00 10.17 ? 83   SER B OG  1 
ATOM   4338 N N   . ARG B 1 84  ? 73.215 13.129 -61.726 1.00 11.80 ? 84   ARG B N   1 
ATOM   4339 C CA  . ARG B 1 84  ? 72.765 12.314 -62.855 1.00 9.39  ? 84   ARG B CA  1 
ATOM   4340 C C   . ARG B 1 84  ? 73.942 11.817 -63.695 1.00 11.86 ? 84   ARG B C   1 
ATOM   4341 O O   . ARG B 1 84  ? 73.949 10.662 -64.146 1.00 10.05 ? 84   ARG B O   1 
ATOM   4342 C CB  . ARG B 1 84  ? 71.823 13.116 -63.757 1.00 10.68 ? 84   ARG B CB  1 
ATOM   4343 C CG  . ARG B 1 84  ? 70.494 13.554 -63.167 1.00 10.64 ? 84   ARG B CG  1 
ATOM   4344 C CD  . ARG B 1 84  ? 69.654 14.276 -64.256 1.00 10.55 ? 84   ARG B CD  1 
ATOM   4345 N NE  . ARG B 1 84  ? 68.383 14.784 -63.740 1.00 10.72 ? 84   ARG B NE  1 
ATOM   4346 C CZ  . ARG B 1 84  ? 67.280 14.057 -63.628 1.00 14.05 ? 84   ARG B CZ  1 
ATOM   4347 N NH1 . ARG B 1 84  ? 67.249 12.784 -64.005 1.00 12.12 ? 84   ARG B NH1 1 
ATOM   4348 N NH2 . ARG B 1 84  ? 66.180 14.619 -63.131 1.00 11.41 ? 84   ARG B NH2 1 
ATOM   4349 N N   . ILE B 1 85  ? 74.918 12.691 -63.947 1.00 10.77 ? 85   ILE B N   1 
ATOM   4350 C CA  . ILE B 1 85  ? 76.028 12.360 -64.838 1.00 11.97 ? 85   ILE B CA  1 
ATOM   4351 C C   . ILE B 1 85  ? 76.925 11.303 -64.204 1.00 13.01 ? 85   ILE B C   1 
ATOM   4352 O O   . ILE B 1 85  ? 77.400 10.385 -64.884 1.00 13.04 ? 85   ILE B O   1 
ATOM   4353 C CB  . ILE B 1 85  ? 76.833 13.627 -65.184 1.00 13.60 ? 85   ILE B CB  1 
ATOM   4354 C CG1 . ILE B 1 85  ? 75.979 14.697 -65.887 1.00 13.48 ? 85   ILE B CG1 1 
ATOM   4355 C CG2 . ILE B 1 85  ? 78.039 13.270 -66.048 1.00 10.76 ? 85   ILE B CG2 1 
ATOM   4356 C CD1 . ILE B 1 85  ? 75.689 14.404 -67.290 1.00 23.18 ? 85   ILE B CD1 1 
ATOM   4357 N N   . PHE B 1 86  ? 77.183 11.426 -62.895 1.00 12.69 ? 86   PHE B N   1 
ATOM   4358 C CA  . PHE B 1 86  ? 77.985 10.482 -62.117 1.00 13.62 ? 86   PHE B CA  1 
ATOM   4359 C C   . PHE B 1 86  ? 77.111 9.967  -60.978 1.00 13.33 ? 86   PHE B C   1 
ATOM   4360 O O   . PHE B 1 86  ? 77.189 10.461 -59.845 1.00 14.30 ? 86   PHE B O   1 
ATOM   4361 C CB  . PHE B 1 86  ? 79.263 11.146 -61.607 1.00 13.98 ? 86   PHE B CB  1 
ATOM   4362 C CG  . PHE B 1 86  ? 80.289 11.345 -62.689 1.00 16.40 ? 86   PHE B CG  1 
ATOM   4363 C CD1 . PHE B 1 86  ? 80.857 10.251 -63.329 1.00 17.83 ? 86   PHE B CD1 1 
ATOM   4364 C CD2 . PHE B 1 86  ? 80.610 12.618 -63.132 1.00 16.95 ? 86   PHE B CD2 1 
ATOM   4365 C CE1 . PHE B 1 86  ? 81.774 10.424 -64.345 1.00 17.38 ? 86   PHE B CE1 1 
ATOM   4366 C CE2 . PHE B 1 86  ? 81.528 12.807 -64.169 1.00 16.46 ? 86   PHE B CE2 1 
ATOM   4367 C CZ  . PHE B 1 86  ? 82.109 11.712 -64.773 1.00 17.46 ? 86   PHE B CZ  1 
ATOM   4368 N N   . PRO B 1 87  ? 76.235 8.998  -61.252 1.00 13.41 ? 87   PRO B N   1 
ATOM   4369 C CA  . PRO B 1 87  ? 75.371 8.469  -60.185 1.00 11.97 ? 87   PRO B CA  1 
ATOM   4370 C C   . PRO B 1 87  ? 76.141 7.725  -59.115 1.00 17.47 ? 87   PRO B C   1 
ATOM   4371 O O   . PRO B 1 87  ? 75.610 7.544  -58.016 1.00 13.86 ? 87   PRO B O   1 
ATOM   4372 C CB  . PRO B 1 87  ? 74.407 7.535  -60.926 1.00 15.20 ? 87   PRO B CB  1 
ATOM   4373 C CG  . PRO B 1 87  ? 75.110 7.183  -62.210 1.00 12.92 ? 87   PRO B CG  1 
ATOM   4374 C CD  . PRO B 1 87  ? 76.009 8.343  -62.552 1.00 13.19 ? 87   PRO B CD  1 
ATOM   4375 N N   . ASN B 1 88  ? 77.380 7.314  -59.390 1.00 14.15 ? 88   ASN B N   1 
ATOM   4376 C CA  . ASN B 1 88  ? 78.187 6.567  -58.444 1.00 14.69 ? 88   ASN B CA  1 
ATOM   4377 C C   . ASN B 1 88  ? 79.490 7.299  -58.160 1.00 14.80 ? 88   ASN B C   1 
ATOM   4378 O O   . ASN B 1 88  ? 80.002 8.026  -59.018 1.00 14.28 ? 88   ASN B O   1 
ATOM   4379 C CB  . ASN B 1 88  ? 78.472 5.153  -58.975 1.00 15.10 ? 88   ASN B CB  1 
ATOM   4380 C CG  . ASN B 1 88  ? 77.208 4.336  -59.116 1.00 20.78 ? 88   ASN B CG  1 
ATOM   4381 O OD1 . ASN B 1 88  ? 76.410 4.254  -58.179 1.00 21.44 ? 88   ASN B OD1 1 
ATOM   4382 N ND2 . ASN B 1 88  ? 76.991 3.763  -60.297 1.00 23.28 ? 88   ASN B ND2 1 
ATOM   4383 N N   . PRO B 1 89  ? 80.034 7.144  -56.953 1.00 14.81 ? 89   PRO B N   1 
ATOM   4384 C CA  . PRO B 1 89  ? 81.193 7.947  -56.550 1.00 15.60 ? 89   PRO B CA  1 
ATOM   4385 C C   . PRO B 1 89  ? 82.406 7.703  -57.441 1.00 16.89 ? 89   PRO B C   1 
ATOM   4386 O O   . PRO B 1 89  ? 82.664 6.581  -57.882 1.00 15.92 ? 89   PRO B O   1 
ATOM   4387 C CB  . PRO B 1 89  ? 81.458 7.493  -55.107 1.00 16.15 ? 89   PRO B CB  1 
ATOM   4388 C CG  . PRO B 1 89  ? 80.763 6.193  -54.954 1.00 21.24 ? 89   PRO B CG  1 
ATOM   4389 C CD  . PRO B 1 89  ? 79.598 6.206  -55.904 1.00 16.51 ? 89   PRO B CD  1 
ATOM   4390 N N   . THR B 1 90  ? 83.155 8.777  -57.687 1.00 16.61 ? 90   THR B N   1 
ATOM   4391 C CA  . THR B 1 90  ? 84.298 8.769  -58.582 1.00 18.15 ? 90   THR B CA  1 
ATOM   4392 C C   . THR B 1 90  ? 85.630 8.706  -57.842 1.00 19.62 ? 90   THR B C   1 
ATOM   4393 O O   . THR B 1 90  ? 86.677 8.676  -58.495 1.00 19.24 ? 90   THR B O   1 
ATOM   4394 C CB  . THR B 1 90  ? 84.281 10.014 -59.478 1.00 18.38 ? 90   THR B CB  1 
ATOM   4395 O OG1 . THR B 1 90  ? 84.107 11.182 -58.671 1.00 16.22 ? 90   THR B OG1 1 
ATOM   4396 C CG2 . THR B 1 90  ? 83.143 9.949  -60.491 1.00 16.70 ? 90   THR B CG2 1 
ATOM   4397 N N   . HIS B 1 91  ? 85.621 8.690  -56.510 1.00 18.82 ? 91   HIS B N   1 
ATOM   4398 C CA  . HIS B 1 91  ? 86.879 8.694  -55.770 1.00 26.93 ? 91   HIS B CA  1 
ATOM   4399 C C   . HIS B 1 91  ? 87.726 7.475  -56.114 1.00 25.00 ? 91   HIS B C   1 
ATOM   4400 O O   . HIS B 1 91  ? 87.216 6.359  -56.237 1.00 18.35 ? 91   HIS B O   1 
ATOM   4401 C CB  . HIS B 1 91  ? 86.645 8.713  -54.260 1.00 30.23 ? 91   HIS B CB  1 
ATOM   4402 C CG  . HIS B 1 91  ? 87.910 8.535  -53.475 1.00 34.42 ? 91   HIS B CG  1 
ATOM   4403 N ND1 . HIS B 1 91  ? 88.852 9.536  -53.342 1.00 32.89 ? 91   HIS B ND1 1 
ATOM   4404 C CD2 . HIS B 1 91  ? 88.417 7.454  -52.834 1.00 35.54 ? 91   HIS B CD2 1 
ATOM   4405 C CE1 . HIS B 1 91  ? 89.868 9.089  -52.624 1.00 35.44 ? 91   HIS B CE1 1 
ATOM   4406 N NE2 . HIS B 1 91  ? 89.629 7.829  -52.303 1.00 41.15 ? 91   HIS B NE2 1 
ATOM   4407 N N   . GLY B 1 92  ? 89.030 7.697  -56.256 1.00 23.90 ? 92   GLY B N   1 
ATOM   4408 C CA  . GLY B 1 92  ? 89.947 6.634  -56.594 1.00 24.72 ? 92   GLY B CA  1 
ATOM   4409 C C   . GLY B 1 92  ? 89.916 6.189  -58.038 1.00 29.17 ? 92   GLY B C   1 
ATOM   4410 O O   . GLY B 1 92  ? 90.648 5.259  -58.394 1.00 29.38 ? 92   GLY B O   1 
ATOM   4411 N N   . ILE B 1 93  ? 89.098 6.810  -58.884 1.00 27.02 ? 93   ILE B N   1 
ATOM   4412 C CA  . ILE B 1 93  ? 89.035 6.467  -60.302 1.00 23.61 ? 93   ILE B CA  1 
ATOM   4413 C C   . ILE B 1 93  ? 89.658 7.614  -61.085 1.00 31.87 ? 93   ILE B C   1 
ATOM   4414 O O   . ILE B 1 93  ? 89.047 8.674  -61.266 1.00 33.08 ? 93   ILE B O   1 
ATOM   4415 C CB  . ILE B 1 93  ? 87.606 6.174  -60.773 1.00 25.70 ? 93   ILE B CB  1 
ATOM   4416 C CG1 . ILE B 1 93  ? 87.020 4.990  -60.006 1.00 28.46 ? 93   ILE B CG1 1 
ATOM   4417 C CG2 . ILE B 1 93  ? 87.589 5.908  -62.275 1.00 29.08 ? 93   ILE B CG2 1 
ATOM   4418 C CD1 . ILE B 1 93  ? 85.606 5.221  -59.531 1.00 27.65 ? 93   ILE B CD1 1 
ATOM   4419 N N   . LYS B 1 94  ? 90.888 7.410  -61.545 1.00 33.84 ? 94   LYS B N   1 
ATOM   4420 C CA  . LYS B 1 94  ? 91.479 8.313  -62.519 1.00 38.40 ? 94   LYS B CA  1 
ATOM   4421 C C   . LYS B 1 94  ? 90.771 8.099  -63.852 1.00 46.37 ? 94   LYS B C   1 
ATOM   4422 O O   . LYS B 1 94  ? 90.685 6.965  -64.345 1.00 47.09 ? 94   LYS B O   1 
ATOM   4423 C CB  . LYS B 1 94  ? 92.981 8.065  -62.646 1.00 37.42 ? 94   LYS B CB  1 
ATOM   4424 N N   . ASP B 1 95  ? 90.248 9.184  -64.416 1.00 35.13 ? 95   ASP B N   1 
ATOM   4425 C CA  . ASP B 1 95  ? 89.357 9.155  -65.575 1.00 40.50 ? 95   ASP B CA  1 
ATOM   4426 C C   . ASP B 1 95  ? 88.070 8.388  -65.285 1.00 31.89 ? 95   ASP B C   1 
ATOM   4427 O O   . ASP B 1 95  ? 87.946 7.207  -65.637 1.00 29.09 ? 95   ASP B O   1 
ATOM   4428 C CB  . ASP B 1 95  ? 90.045 8.549  -66.800 1.00 44.68 ? 95   ASP B CB  1 
ATOM   4429 C CG  . ASP B 1 95  ? 89.210 8.704  -68.054 1.00 49.53 ? 95   ASP B CG  1 
ATOM   4430 O OD1 . ASP B 1 95  ? 88.766 9.845  -68.319 1.00 48.60 ? 95   ASP B OD1 1 
ATOM   4431 O OD2 . ASP B 1 95  ? 88.985 7.688  -68.756 1.00 52.61 ? 95   ASP B OD2 1 
ATOM   4432 N N   . PRO B 1 96  ? 87.077 9.030  -64.669 1.00 30.30 ? 96   PRO B N   1 
ATOM   4433 C CA  . PRO B 1 96  ? 85.792 8.367  -64.433 1.00 26.43 ? 96   PRO B CA  1 
ATOM   4434 C C   . PRO B 1 96  ? 84.858 8.339  -65.634 1.00 25.02 ? 96   PRO B C   1 
ATOM   4435 O O   . PRO B 1 96  ? 83.687 7.989  -65.473 1.00 22.85 ? 96   PRO B O   1 
ATOM   4436 C CB  . PRO B 1 96  ? 85.193 9.207  -63.296 1.00 30.81 ? 96   PRO B CB  1 
ATOM   4437 C CG  . PRO B 1 96  ? 85.746 10.566 -63.530 1.00 28.19 ? 96   PRO B CG  1 
ATOM   4438 C CD  . PRO B 1 96  ? 87.157 10.340 -63.999 1.00 30.90 ? 96   PRO B CD  1 
ATOM   4439 N N   . SER B 1 97  ? 85.329 8.681  -66.834 1.00 23.27 ? 97   SER B N   1 
ATOM   4440 C CA  . SER B 1 97  ? 84.442 8.671  -67.989 1.00 25.24 ? 97   SER B CA  1 
ATOM   4441 C C   . SER B 1 97  ? 83.829 7.294  -68.240 1.00 27.41 ? 97   SER B C   1 
ATOM   4442 O O   . SER B 1 97  ? 82.745 7.208  -68.829 1.00 25.19 ? 97   SER B O   1 
ATOM   4443 C CB  . SER B 1 97  ? 85.198 9.172  -69.221 1.00 27.57 ? 97   SER B CB  1 
ATOM   4444 O OG  . SER B 1 97  ? 86.086 8.184  -69.696 1.00 35.83 ? 97   SER B OG  1 
ATOM   4445 N N   . GLN B 1 98  ? 84.469 6.220  -67.772 1.00 25.61 ? 98   GLN B N   1 
ATOM   4446 C CA  . GLN B 1 98  ? 83.929 4.876  -67.937 1.00 27.46 ? 98   GLN B CA  1 
ATOM   4447 C C   . GLN B 1 98  ? 82.787 4.563  -66.980 1.00 27.23 ? 98   GLN B C   1 
ATOM   4448 O O   . GLN B 1 98  ? 82.114 3.545  -67.162 1.00 20.43 ? 98   GLN B O   1 
ATOM   4449 C CB  . GLN B 1 98  ? 85.039 3.833  -67.759 1.00 35.64 ? 98   GLN B CB  1 
ATOM   4450 C CG  . GLN B 1 98  ? 86.103 3.888  -68.843 1.00 40.88 ? 98   GLN B CG  1 
ATOM   4451 C CD  . GLN B 1 98  ? 85.544 3.500  -70.199 1.00 51.76 ? 98   GLN B CD  1 
ATOM   4452 O OE1 . GLN B 1 98  ? 85.304 2.319  -70.468 1.00 59.33 ? 98   GLN B OE1 1 
ATOM   4453 N NE2 . GLN B 1 98  ? 85.323 4.494  -71.061 1.00 52.46 ? 98   GLN B NE2 1 
ATOM   4454 N N   . ILE B 1 99  ? 82.542 5.398  -65.969 1.00 21.51 ? 99   ILE B N   1 
ATOM   4455 C CA  . ILE B 1 99  ? 81.397 5.189  -65.098 1.00 19.97 ? 99   ILE B CA  1 
ATOM   4456 C C   . ILE B 1 99  ? 80.395 6.338  -65.172 1.00 20.63 ? 99   ILE B C   1 
ATOM   4457 O O   . ILE B 1 99  ? 79.457 6.381  -64.380 1.00 18.12 ? 99   ILE B O   1 
ATOM   4458 C CB  . ILE B 1 99  ? 81.835 4.941  -63.643 1.00 18.97 ? 99   ILE B CB  1 
ATOM   4459 C CG1 . ILE B 1 99  ? 82.582 6.159  -63.105 1.00 19.67 ? 99   ILE B CG1 1 
ATOM   4460 C CG2 . ILE B 1 99  ? 82.700 3.683  -63.553 1.00 26.45 ? 99   ILE B CG2 1 
ATOM   4461 C CD1 . ILE B 1 99  ? 82.657 6.179  -61.600 1.00 20.67 ? 99   ILE B CD1 1 
ATOM   4462 N N   . ALA B 1 100 ? 80.578 7.272  -66.099 1.00 17.74 ? 100  ALA B N   1 
ATOM   4463 C CA  . ALA B 1 100 ? 79.559 8.282  -66.349 1.00 16.57 ? 100  ALA B CA  1 
ATOM   4464 C C   . ALA B 1 100 ? 78.325 7.638  -66.975 1.00 18.76 ? 100  ALA B C   1 
ATOM   4465 O O   . ALA B 1 100 ? 78.413 6.626  -67.674 1.00 16.63 ? 100  ALA B O   1 
ATOM   4466 C CB  . ALA B 1 100 ? 80.104 9.372  -67.269 1.00 15.30 ? 100  ALA B CB  1 
ATOM   4467 N N   . ASP B 1 101 ? 77.158 8.218  -66.705 1.00 13.94 ? 101  ASP B N   1 
ATOM   4468 C CA  . ASP B 1 101 ? 75.920 7.731  -67.307 1.00 14.75 ? 101  ASP B CA  1 
ATOM   4469 C C   . ASP B 1 101 ? 75.784 8.389  -68.678 1.00 17.77 ? 101  ASP B C   1 
ATOM   4470 O O   . ASP B 1 101 ? 75.331 9.532  -68.791 1.00 12.68 ? 101  ASP B O   1 
ATOM   4471 C CB  . ASP B 1 101 ? 74.720 8.026  -66.409 1.00 15.45 ? 101  ASP B CB  1 
ATOM   4472 C CG  . ASP B 1 101 ? 73.430 7.380  -66.921 1.00 15.67 ? 101  ASP B CG  1 
ATOM   4473 O OD1 . ASP B 1 101 ? 73.318 7.147  -68.146 1.00 17.26 ? 101  ASP B OD1 1 
ATOM   4474 O OD2 . ASP B 1 101 ? 72.514 7.125  -66.114 1.00 13.16 ? 101  ASP B OD2 1 
ATOM   4475 N N   . MET B 1 102 ? 76.161 7.648  -69.732 1.00 17.49 ? 102  MET B N   1 
ATOM   4476 C CA  . MET B 1 102 ? 76.198 8.207  -71.085 1.00 17.14 ? 102  MET B CA  1 
ATOM   4477 C C   . MET B 1 102 ? 74.799 8.448  -71.643 1.00 16.31 ? 102  MET B C   1 
ATOM   4478 O O   . MET B 1 102 ? 74.625 9.282  -72.541 1.00 15.15 ? 102  MET B O   1 
ATOM   4479 C CB  . MET B 1 102 ? 76.985 7.272  -72.015 1.00 17.98 ? 102  MET B CB  1 
ATOM   4480 C CG  . MET B 1 102 ? 78.513 7.343  -71.887 1.00 20.80 ? 102  MET B CG  1 
ATOM   4481 S SD  . MET B 1 102 ? 79.256 8.923  -71.436 1.00 23.65 ? 102  MET B SD  1 
ATOM   4482 C CE  . MET B 1 102 ? 79.064 9.789  -72.985 1.00 22.87 ? 102  MET B CE  1 
ATOM   4483 N N   . LYS B 1 103 ? 73.795 7.718  -71.161 1.00 15.25 ? 103  LYS B N   1 
ATOM   4484 C CA  . LYS B 1 103 ? 72.424 8.025  -71.566 1.00 14.93 ? 103  LYS B CA  1 
ATOM   4485 C C   . LYS B 1 103 ? 72.004 9.400  -71.045 1.00 17.53 ? 103  LYS B C   1 
ATOM   4486 O O   . LYS B 1 103 ? 71.310 10.155 -71.740 1.00 11.84 ? 103  LYS B O   1 
ATOM   4487 C CB  . LYS B 1 103 ? 71.480 6.935  -71.063 1.00 20.84 ? 103  LYS B CB  1 
ATOM   4488 C CG  . LYS B 1 103 ? 71.431 5.686  -71.964 1.00 34.81 ? 103  LYS B CG  1 
ATOM   4489 C CD  . LYS B 1 103 ? 70.260 4.777  -71.601 1.00 44.41 ? 103  LYS B CD  1 
ATOM   4490 C CE  . LYS B 1 103 ? 69.491 4.303  -72.843 1.00 52.18 ? 103  LYS B CE  1 
ATOM   4491 N NZ  . LYS B 1 103 ? 69.058 2.865  -72.757 1.00 50.86 ? 103  LYS B NZ  1 
ATOM   4492 N N   . VAL B 1 104 ? 72.424 9.740  -69.825 1.00 12.71 ? 104  VAL B N   1 
ATOM   4493 C CA  . VAL B 1 104 ? 72.191 11.079 -69.287 1.00 13.71 ? 104  VAL B CA  1 
ATOM   4494 C C   . VAL B 1 104 ? 72.962 12.123 -70.089 1.00 10.95 ? 104  VAL B C   1 
ATOM   4495 O O   . VAL B 1 104 ? 72.422 13.179 -70.447 1.00 10.43 ? 104  VAL B O   1 
ATOM   4496 C CB  . VAL B 1 104 ? 72.568 11.112 -67.796 1.00 10.95 ? 104  VAL B CB  1 
ATOM   4497 C CG1 . VAL B 1 104 ? 72.718 12.543 -67.317 1.00 9.71  ? 104  VAL B CG1 1 
ATOM   4498 C CG2 . VAL B 1 104 ? 71.527 10.375 -66.989 1.00 9.99  ? 104  VAL B CG2 1 
ATOM   4499 N N   . VAL B 1 105 ? 74.235 11.848 -70.387 1.00 9.44  ? 105  VAL B N   1 
ATOM   4500 C CA  . VAL B 1 105 ? 75.029 12.807 -71.150 1.00 12.47 ? 105  VAL B CA  1 
ATOM   4501 C C   . VAL B 1 105 ? 74.390 13.056 -72.514 1.00 16.74 ? 105  VAL B C   1 
ATOM   4502 O O   . VAL B 1 105 ? 74.280 14.202 -72.973 1.00 12.67 ? 105  VAL B O   1 
ATOM   4503 C CB  . VAL B 1 105 ? 76.482 12.307 -71.286 1.00 16.22 ? 105  VAL B CB  1 
ATOM   4504 C CG1 . VAL B 1 105 ? 77.238 13.127 -72.338 1.00 17.36 ? 105  VAL B CG1 1 
ATOM   4505 C CG2 . VAL B 1 105 ? 77.200 12.341 -69.929 1.00 11.64 ? 105  VAL B CG2 1 
ATOM   4506 N N   . GLU B 1 106 ? 73.956 11.987 -73.180 1.00 13.71 ? 106  GLU B N   1 
ATOM   4507 C CA  . GLU B 1 106 ? 73.317 12.139 -74.483 1.00 19.26 ? 106  GLU B CA  1 
ATOM   4508 C C   . GLU B 1 106 ? 72.016 12.917 -74.365 1.00 13.57 ? 106  GLU B C   1 
ATOM   4509 O O   . GLU B 1 106 ? 71.685 13.719 -75.239 1.00 11.76 ? 106  GLU B O   1 
ATOM   4510 C CB  . GLU B 1 106 ? 73.070 10.766 -75.107 1.00 17.01 ? 106  GLU B CB  1 
ATOM   4511 C CG  . GLU B 1 106 ? 72.834 10.738 -76.632 1.00 36.94 ? 106  GLU B CG  1 
ATOM   4512 C CD  . GLU B 1 106 ? 73.514 11.869 -77.424 1.00 43.30 ? 106  GLU B CD  1 
ATOM   4513 O OE1 . GLU B 1 106 ? 72.787 12.794 -77.875 1.00 36.84 ? 106  GLU B OE1 1 
ATOM   4514 O OE2 . GLU B 1 106 ? 74.763 11.820 -77.614 1.00 37.62 ? 106  GLU B OE2 1 
ATOM   4515 N N   . HIS B 1 107 ? 71.265 12.695 -73.287 1.00 11.61 ? 107  HIS B N   1 
ATOM   4516 C CA  . HIS B 1 107 ? 70.024 13.438 -73.107 1.00 13.58 ? 107  HIS B CA  1 
ATOM   4517 C C   . HIS B 1 107 ? 70.289 14.931 -72.913 1.00 12.80 ? 107  HIS B C   1 
ATOM   4518 O O   . HIS B 1 107 ? 69.555 15.765 -73.455 1.00 10.89 ? 107  HIS B O   1 
ATOM   4519 C CB  . HIS B 1 107 ? 69.232 12.871 -71.929 1.00 11.45 ? 107  HIS B CB  1 
ATOM   4520 C CG  . HIS B 1 107 ? 67.852 13.427 -71.826 1.00 16.36 ? 107  HIS B CG  1 
ATOM   4521 N ND1 . HIS B 1 107 ? 66.789 12.907 -72.530 1.00 16.91 ? 107  HIS B ND1 1 
ATOM   4522 C CD2 . HIS B 1 107 ? 67.365 14.482 -71.130 1.00 14.17 ? 107  HIS B CD2 1 
ATOM   4523 C CE1 . HIS B 1 107 ? 65.700 13.605 -72.259 1.00 17.11 ? 107  HIS B CE1 1 
ATOM   4524 N NE2 . HIS B 1 107 ? 66.022 14.566 -71.413 1.00 14.18 ? 107  HIS B NE2 1 
ATOM   4525 N N   . TYR B 1 108 ? 71.323 15.295 -72.143 1.00 10.14 ? 108  TYR B N   1 
ATOM   4526 C CA  . TYR B 1 108 ? 71.641 16.717 -71.988 1.00 12.35 ? 108  TYR B CA  1 
ATOM   4527 C C   . TYR B 1 108 ? 72.090 17.325 -73.311 1.00 12.46 ? 108  TYR B C   1 
ATOM   4528 O O   . TYR B 1 108 ? 71.774 18.487 -73.609 1.00 11.62 ? 108  TYR B O   1 
ATOM   4529 C CB  . TYR B 1 108 ? 72.718 16.934 -70.913 1.00 11.01 ? 108  TYR B CB  1 
ATOM   4530 C CG  . TYR B 1 108 ? 72.194 17.020 -69.480 1.00 11.51 ? 108  TYR B CG  1 
ATOM   4531 C CD1 . TYR B 1 108 ? 71.198 17.925 -69.136 1.00 13.25 ? 108  TYR B CD1 1 
ATOM   4532 C CD2 . TYR B 1 108 ? 72.715 16.212 -68.477 1.00 12.64 ? 108  TYR B CD2 1 
ATOM   4533 C CE1 . TYR B 1 108 ? 70.725 18.019 -67.824 1.00 13.84 ? 108  TYR B CE1 1 
ATOM   4534 C CE2 . TYR B 1 108 ? 72.254 16.296 -67.165 1.00 11.85 ? 108  TYR B CE2 1 
ATOM   4535 C CZ  . TYR B 1 108 ? 71.254 17.202 -66.850 1.00 12.68 ? 108  TYR B CZ  1 
ATOM   4536 O OH  . TYR B 1 108 ? 70.785 17.289 -65.559 1.00 10.85 ? 108  TYR B OH  1 
ATOM   4537 N N   . LYS B 1 109 ? 72.832 16.562 -74.119 1.00 11.07 ? 109  LYS B N   1 
ATOM   4538 C CA  . LYS B 1 109 ? 73.231 17.067 -75.437 1.00 12.68 ? 109  LYS B CA  1 
ATOM   4539 C C   . LYS B 1 109 ? 72.019 17.327 -76.326 1.00 11.77 ? 109  LYS B C   1 
ATOM   4540 O O   . LYS B 1 109 ? 72.011 18.283 -77.116 1.00 14.28 ? 109  LYS B O   1 
ATOM   4541 C CB  . LYS B 1 109 ? 74.181 16.079 -76.110 1.00 12.80 ? 109  LYS B CB  1 
ATOM   4542 C CG  . LYS B 1 109 ? 75.575 16.046 -75.507 1.00 18.72 ? 109  LYS B CG  1 
ATOM   4543 C CD  . LYS B 1 109 ? 76.491 15.171 -76.362 1.00 23.19 ? 109  LYS B CD  1 
ATOM   4544 C CE  . LYS B 1 109 ? 77.900 15.137 -75.800 1.00 27.67 ? 109  LYS B CE  1 
ATOM   4545 N NZ  . LYS B 1 109 ? 78.952 15.080 -76.869 1.00 43.63 ? 109  LYS B NZ  1 
ATOM   4546 N N   . GLN B 1 110 ? 70.998 16.469 -76.236 1.00 11.13 ? 110  GLN B N   1 
ATOM   4547 C CA  . GLN B 1 110 ? 69.742 16.710 -76.948 1.00 9.93  ? 110  GLN B CA  1 
ATOM   4548 C C   . GLN B 1 110 ? 69.042 17.970 -76.459 1.00 12.02 ? 110  GLN B C   1 
ATOM   4549 O O   . GLN B 1 110 ? 68.519 18.744 -77.271 1.00 12.76 ? 110  GLN B O   1 
ATOM   4550 C CB  . GLN B 1 110 ? 68.829 15.494 -76.819 1.00 15.50 ? 110  GLN B CB  1 
ATOM   4551 C CG  . GLN B 1 110 ? 69.473 14.250 -77.443 1.00 20.23 ? 110  GLN B CG  1 
ATOM   4552 C CD  . GLN B 1 110 ? 68.664 12.989 -77.249 1.00 29.05 ? 110  GLN B CD  1 
ATOM   4553 O OE1 . GLN B 1 110 ? 67.741 12.936 -76.430 1.00 21.77 ? 110  GLN B OE1 1 
ATOM   4554 N NE2 . GLN B 1 110 ? 68.995 11.961 -78.026 1.00 33.28 ? 110  GLN B NE2 1 
ATOM   4555 N N   . ILE B 1 111 ? 69.002 18.187 -75.140 1.00 9.99  ? 111  ILE B N   1 
ATOM   4556 C CA  . ILE B 1 111 ? 68.418 19.418 -74.614 1.00 11.65 ? 111  ILE B CA  1 
ATOM   4557 C C   . ILE B 1 111 ? 69.168 20.627 -75.153 1.00 10.42 ? 111  ILE B C   1 
ATOM   4558 O O   . ILE B 1 111 ? 68.565 21.588 -75.653 1.00 10.84 ? 111  ILE B O   1 
ATOM   4559 C CB  . ILE B 1 111 ? 68.425 19.399 -73.074 1.00 11.10 ? 111  ILE B CB  1 
ATOM   4560 C CG1 . ILE B 1 111 ? 67.414 18.371 -72.558 1.00 8.65  ? 111  ILE B CG1 1 
ATOM   4561 C CG2 . ILE B 1 111 ? 68.125 20.797 -72.525 1.00 11.40 ? 111  ILE B CG2 1 
ATOM   4562 C CD1 . ILE B 1 111 ? 67.457 18.163 -71.039 1.00 10.65 ? 111  ILE B CD1 1 
ATOM   4563 N N   . ILE B 1 112 ? 70.499 20.590 -75.064 1.00 9.71  ? 112  ILE B N   1 
ATOM   4564 C CA  . ILE B 1 112 ? 71.327 21.700 -75.530 1.00 11.35 ? 112  ILE B CA  1 
ATOM   4565 C C   . ILE B 1 112 ? 71.096 21.948 -77.018 1.00 11.33 ? 112  ILE B C   1 
ATOM   4566 O O   . ILE B 1 112 ? 70.903 23.091 -77.455 1.00 11.64 ? 112  ILE B O   1 
ATOM   4567 C CB  . ILE B 1 112 ? 72.811 21.411 -75.224 1.00 9.96  ? 112  ILE B CB  1 
ATOM   4568 C CG1 . ILE B 1 112 ? 73.071 21.448 -73.713 1.00 10.25 ? 112  ILE B CG1 1 
ATOM   4569 C CG2 . ILE B 1 112 ? 73.740 22.394 -75.960 1.00 10.92 ? 112  ILE B CG2 1 
ATOM   4570 C CD1 . ILE B 1 112 ? 74.385 20.766 -73.308 1.00 10.23 ? 112  ILE B CD1 1 
ATOM   4571 N N   . GLU B 1 113 ? 71.107 20.878 -77.820 1.00 12.36 ? 113  GLU B N   1 
ATOM   4572 C CA  . GLU B 1 113 ? 70.944 21.040 -79.264 1.00 14.63 ? 113  GLU B CA  1 
ATOM   4573 C C   . GLU B 1 113 ? 69.559 21.579 -79.615 1.00 13.22 ? 113  GLU B C   1 
ATOM   4574 O O   . GLU B 1 113 ? 69.416 22.357 -80.570 1.00 11.58 ? 113  GLU B O   1 
ATOM   4575 C CB  . GLU B 1 113 ? 71.210 19.710 -79.980 1.00 15.78 ? 113  GLU B CB  1 
ATOM   4576 C CG  . GLU B 1 113 ? 70.949 19.761 -81.497 1.00 30.56 ? 113  GLU B CG  1 
ATOM   4577 C CD  . GLU B 1 113 ? 70.966 18.386 -82.177 1.00 39.78 ? 113  GLU B CD  1 
ATOM   4578 O OE1 . GLU B 1 113 ? 71.894 17.594 -81.906 1.00 48.47 ? 113  GLU B OE1 1 
ATOM   4579 O OE2 . GLU B 1 113 ? 70.060 18.099 -82.995 1.00 40.76 ? 113  GLU B OE2 1 
ATOM   4580 N N   . ASP B 1 114 ? 68.527 21.192 -78.862 1.00 11.78 ? 114  ASP B N   1 
ATOM   4581 C CA  . ASP B 1 114 ? 67.205 21.753 -79.128 1.00 11.65 ? 114  ASP B CA  1 
ATOM   4582 C C   . ASP B 1 114 ? 67.198 23.264 -78.910 1.00 11.08 ? 114  ASP B C   1 
ATOM   4583 O O   . ASP B 1 114 ? 66.695 24.020 -79.749 1.00 11.33 ? 114  ASP B O   1 
ATOM   4584 C CB  . ASP B 1 114 ? 66.149 21.068 -78.260 1.00 9.70  ? 114  ASP B CB  1 
ATOM   4585 C CG  . ASP B 1 114 ? 64.755 21.593 -78.526 1.00 14.17 ? 114  ASP B CG  1 
ATOM   4586 O OD1 . ASP B 1 114 ? 64.404 22.660 -77.979 1.00 12.92 ? 114  ASP B OD1 1 
ATOM   4587 O OD2 . ASP B 1 114 ? 64.014 20.962 -79.308 1.00 12.74 ? 114  ASP B OD2 1 
ATOM   4588 N N   . ALA B 1 115 ? 67.762 23.728 -77.791 1.00 10.22 ? 115  ALA B N   1 
ATOM   4589 C CA  . ALA B 1 115 ? 67.812 25.168 -77.542 1.00 12.08 ? 115  ALA B CA  1 
ATOM   4590 C C   . ALA B 1 115 ? 68.578 25.890 -78.647 1.00 11.94 ? 115  ALA B C   1 
ATOM   4591 O O   . ALA B 1 115 ? 68.122 26.919 -79.163 1.00 10.14 ? 115  ALA B O   1 
ATOM   4592 C CB  . ALA B 1 115 ? 68.448 25.452 -76.180 1.00 8.36  ? 115  ALA B CB  1 
ATOM   4593 N N   . LYS B 1 116 ? 69.749 25.360 -79.024 1.00 9.80  ? 116  LYS B N   1 
ATOM   4594 C CA  . LYS B 1 116 ? 70.546 25.975 -80.088 1.00 14.30 ? 116  LYS B CA  1 
ATOM   4595 C C   . LYS B 1 116 ? 69.763 26.076 -81.391 1.00 14.37 ? 116  LYS B C   1 
ATOM   4596 O O   . LYS B 1 116 ? 69.875 27.073 -82.113 1.00 13.03 ? 116  LYS B O   1 
ATOM   4597 C CB  . LYS B 1 116 ? 71.831 25.182 -80.329 1.00 15.09 ? 116  LYS B CB  1 
ATOM   4598 C CG  . LYS B 1 116 ? 72.648 24.937 -79.078 1.00 22.02 ? 116  LYS B CG  1 
ATOM   4599 C CD  . LYS B 1 116 ? 73.623 26.036 -78.851 1.00 20.07 ? 116  LYS B CD  1 
ATOM   4600 C CE  . LYS B 1 116 ? 74.798 25.921 -79.813 1.00 27.72 ? 116  LYS B CE  1 
ATOM   4601 N NZ  . LYS B 1 116 ? 75.188 27.270 -80.248 1.00 25.25 ? 116  LYS B NZ  1 
ATOM   4602 N N   . SER B 1 117 ? 68.969 25.048 -81.710 1.00 12.62 ? 117  SER B N   1 
ATOM   4603 C CA  . SER B 1 117 ? 68.259 24.993 -82.981 1.00 14.31 ? 117  SER B CA  1 
ATOM   4604 C C   . SER B 1 117 ? 67.119 25.996 -83.061 1.00 16.06 ? 117  SER B C   1 
ATOM   4605 O O   . SER B 1 117 ? 66.558 26.192 -84.144 1.00 14.64 ? 117  SER B O   1 
ATOM   4606 C CB  . SER B 1 117 ? 67.709 23.587 -83.206 1.00 13.89 ? 117  SER B CB  1 
ATOM   4607 O OG  . SER B 1 117 ? 66.548 23.373 -82.418 1.00 17.89 ? 117  SER B OG  1 
ATOM   4608 N N   . ARG B 1 118 ? 66.756 26.617 -81.945 1.00 11.86 ? 118  ARG B N   1 
ATOM   4609 C CA  . ARG B 1 118 ? 65.716 27.628 -81.914 1.00 16.85 ? 118  ARG B CA  1 
ATOM   4610 C C   . ARG B 1 118 ? 66.301 29.027 -81.797 1.00 17.66 ? 118  ARG B C   1 
ATOM   4611 O O   . ARG B 1 118 ? 65.548 30.000 -81.675 1.00 15.97 ? 118  ARG B O   1 
ATOM   4612 C CB  . ARG B 1 118 ? 64.751 27.329 -80.762 1.00 15.00 ? 118  ARG B CB  1 
ATOM   4613 C CG  . ARG B 1 118 ? 64.117 25.946 -80.937 1.00 13.44 ? 118  ARG B CG  1 
ATOM   4614 C CD  . ARG B 1 118 ? 62.979 25.645 -79.981 1.00 13.63 ? 118  ARG B CD  1 
ATOM   4615 N NE  . ARG B 1 118 ? 62.728 24.209 -79.971 1.00 15.46 ? 118  ARG B NE  1 
ATOM   4616 C CZ  . ARG B 1 118 ? 62.157 23.556 -80.974 1.00 17.96 ? 118  ARG B CZ  1 
ATOM   4617 N NH1 . ARG B 1 118 ? 61.634 24.199 -82.006 1.00 14.83 ? 118  ARG B NH1 1 
ATOM   4618 N NH2 . ARG B 1 118 ? 62.127 22.224 -80.951 1.00 18.05 ? 118  ARG B NH2 1 
ATOM   4619 N N   . GLY B 1 119 ? 67.627 29.146 -81.853 1.00 12.83 ? 119  GLY B N   1 
ATOM   4620 C CA  . GLY B 1 119 ? 68.285 30.431 -81.824 1.00 14.20 ? 119  GLY B CA  1 
ATOM   4621 C C   . GLY B 1 119 ? 68.740 30.896 -80.459 1.00 17.44 ? 119  GLY B C   1 
ATOM   4622 O O   . GLY B 1 119 ? 69.025 32.085 -80.300 1.00 16.41 ? 119  GLY B O   1 
ATOM   4623 N N   . LEU B 1 120 ? 68.796 30.012 -79.467 1.00 11.48 ? 120  LEU B N   1 
ATOM   4624 C CA  . LEU B 1 120 ? 69.236 30.367 -78.120 1.00 13.43 ? 120  LEU B CA  1 
ATOM   4625 C C   . LEU B 1 120 ? 70.702 29.975 -77.959 1.00 13.04 ? 120  LEU B C   1 
ATOM   4626 O O   . LEU B 1 120 ? 71.059 28.805 -78.148 1.00 14.38 ? 120  LEU B O   1 
ATOM   4627 C CB  . LEU B 1 120 ? 68.385 29.656 -77.060 1.00 13.97 ? 120  LEU B CB  1 
ATOM   4628 C CG  . LEU B 1 120 ? 66.860 29.799 -77.131 1.00 12.08 ? 120  LEU B CG  1 
ATOM   4629 C CD1 . LEU B 1 120 ? 66.169 28.839 -76.187 1.00 10.25 ? 120  LEU B CD1 1 
ATOM   4630 C CD2 . LEU B 1 120 ? 66.464 31.240 -76.795 1.00 12.39 ? 120  LEU B CD2 1 
ATOM   4631 N N   . LYS B 1 121 ? 71.550 30.934 -77.612 1.00 10.74 ? 121  LYS B N   1 
ATOM   4632 C CA  . LYS B 1 121 ? 72.854 30.551 -77.090 1.00 12.43 ? 121  LYS B CA  1 
ATOM   4633 C C   . LYS B 1 121 ? 72.665 29.846 -75.749 1.00 15.42 ? 121  LYS B C   1 
ATOM   4634 O O   . LYS B 1 121 ? 71.711 30.117 -75.020 1.00 11.99 ? 121  LYS B O   1 
ATOM   4635 C CB  . LYS B 1 121 ? 73.755 31.774 -76.949 1.00 15.47 ? 121  LYS B CB  1 
ATOM   4636 C CG  . LYS B 1 121 ? 74.325 32.176 -78.298 1.00 22.37 ? 121  LYS B CG  1 
ATOM   4637 C CD  . LYS B 1 121 ? 74.886 33.560 -78.319 1.00 30.73 ? 121  LYS B CD  1 
ATOM   4638 C CE  . LYS B 1 121 ? 75.466 33.848 -79.700 1.00 37.74 ? 121  LYS B CE  1 
ATOM   4639 N NZ  . LYS B 1 121 ? 76.498 34.912 -79.628 1.00 46.08 ? 121  LYS B NZ  1 
ATOM   4640 N N   . VAL B 1 122 ? 73.557 28.912 -75.429 1.00 9.64  ? 122  VAL B N   1 
ATOM   4641 C CA  . VAL B 1 122 ? 73.383 28.065 -74.245 1.00 12.75 ? 122  VAL B CA  1 
ATOM   4642 C C   . VAL B 1 122 ? 74.592 28.232 -73.331 1.00 12.92 ? 122  VAL B C   1 
ATOM   4643 O O   . VAL B 1 122 ? 75.733 27.982 -73.743 1.00 12.51 ? 122  VAL B O   1 
ATOM   4644 C CB  . VAL B 1 122 ? 73.174 26.587 -74.615 1.00 13.07 ? 122  VAL B CB  1 
ATOM   4645 C CG1 . VAL B 1 122 ? 73.121 25.720 -73.350 1.00 13.86 ? 122  VAL B CG1 1 
ATOM   4646 C CG2 . VAL B 1 122 ? 71.901 26.416 -75.419 1.00 13.23 ? 122  VAL B CG2 1 
ATOM   4647 N N   . ILE B 1 123 ? 74.339 28.685 -72.107 1.00 9.19  ? 123  ILE B N   1 
ATOM   4648 C CA  . ILE B 1 123 ? 75.314 28.648 -71.024 1.00 9.34  ? 123  ILE B CA  1 
ATOM   4649 C C   . ILE B 1 123 ? 74.979 27.445 -70.154 1.00 10.93 ? 123  ILE B C   1 
ATOM   4650 O O   . ILE B 1 123 ? 73.848 27.317 -69.670 1.00 10.65 ? 123  ILE B O   1 
ATOM   4651 C CB  . ILE B 1 123 ? 75.292 29.944 -70.198 1.00 7.21  ? 123  ILE B CB  1 
ATOM   4652 C CG1 . ILE B 1 123 ? 75.452 31.168 -71.108 1.00 9.10  ? 123  ILE B CG1 1 
ATOM   4653 C CG2 . ILE B 1 123 ? 76.379 29.893 -69.107 1.00 11.16 ? 123  ILE B CG2 1 
ATOM   4654 C CD1 . ILE B 1 123 ? 75.240 32.504 -70.398 1.00 10.76 ? 123  ILE B CD1 1 
ATOM   4655 N N   . VAL B 1 124 ? 75.942 26.553 -69.957 1.00 8.64  ? 124  VAL B N   1 
ATOM   4656 C CA  . VAL B 1 124 ? 75.739 25.387 -69.107 1.00 9.61  ? 124  VAL B CA  1 
ATOM   4657 C C   . VAL B 1 124 ? 76.454 25.622 -67.786 1.00 10.98 ? 124  VAL B C   1 
ATOM   4658 O O   . VAL B 1 124 ? 77.662 25.892 -67.753 1.00 10.14 ? 124  VAL B O   1 
ATOM   4659 C CB  . VAL B 1 124 ? 76.213 24.093 -69.790 1.00 12.45 ? 124  VAL B CB  1 
ATOM   4660 C CG1 . VAL B 1 124 ? 76.400 22.981 -68.757 1.00 14.38 ? 124  VAL B CG1 1 
ATOM   4661 C CG2 . VAL B 1 124 ? 75.196 23.668 -70.831 1.00 13.24 ? 124  VAL B CG2 1 
ATOM   4662 N N   . ASN B 1 125 ? 75.703 25.541 -66.699 1.00 9.90  ? 125  ASN B N   1 
ATOM   4663 C CA  . ASN B 1 125 ? 76.227 25.734 -65.355 1.00 9.73  ? 125  ASN B CA  1 
ATOM   4664 C C   . ASN B 1 125 ? 76.409 24.365 -64.709 1.00 7.79  ? 125  ASN B C   1 
ATOM   4665 O O   . ASN B 1 125 ? 75.458 23.584 -64.653 1.00 10.09 ? 125  ASN B O   1 
ATOM   4666 C CB  . ASN B 1 125 ? 75.269 26.599 -64.536 1.00 10.32 ? 125  ASN B CB  1 
ATOM   4667 C CG  . ASN B 1 125 ? 75.673 26.683 -63.076 1.00 10.91 ? 125  ASN B CG  1 
ATOM   4668 O OD1 . ASN B 1 125 ? 76.779 27.124 -62.760 1.00 11.42 ? 125  ASN B OD1 1 
ATOM   4669 N ND2 . ASN B 1 125 ? 74.795 26.239 -62.185 1.00 8.70  ? 125  ASN B ND2 1 
ATOM   4670 N N   . LEU B 1 126 ? 77.630 24.074 -64.226 1.00 9.35  ? 126  LEU B N   1 
ATOM   4671 C CA  . LEU B 1 126 ? 77.955 22.709 -63.791 1.00 10.93 ? 126  LEU B CA  1 
ATOM   4672 C C   . LEU B 1 126 ? 77.387 22.337 -62.421 1.00 8.77  ? 126  LEU B C   1 
ATOM   4673 O O   . LEU B 1 126 ? 77.173 21.145 -62.153 1.00 10.92 ? 126  LEU B O   1 
ATOM   4674 C CB  . LEU B 1 126 ? 79.476 22.490 -63.761 1.00 7.43  ? 126  LEU B CB  1 
ATOM   4675 C CG  . LEU B 1 126 ? 80.276 22.679 -65.065 1.00 12.78 ? 126  LEU B CG  1 
ATOM   4676 C CD1 . LEU B 1 126 ? 81.686 22.103 -64.927 1.00 17.39 ? 126  LEU B CD1 1 
ATOM   4677 C CD2 . LEU B 1 126 ? 79.572 22.092 -66.255 1.00 13.38 ? 126  LEU B CD2 1 
ATOM   4678 N N   . ASN B 1 127 ? 77.167 23.295 -61.523 1.00 7.48  ? 127  ASN B N   1 
ATOM   4679 C CA  . ASN B 1 127 ? 76.674 22.944 -60.190 1.00 8.42  ? 127  ASN B CA  1 
ATOM   4680 C C   . ASN B 1 127 ? 75.714 24.018 -59.713 1.00 7.91  ? 127  ASN B C   1 
ATOM   4681 O O   . ASN B 1 127 ? 76.024 25.209 -59.799 1.00 9.30  ? 127  ASN B O   1 
ATOM   4682 C CB  . ASN B 1 127 ? 77.826 22.785 -59.190 1.00 7.68  ? 127  ASN B CB  1 
ATOM   4683 C CG  . ASN B 1 127 ? 77.385 22.156 -57.872 1.00 9.71  ? 127  ASN B CG  1 
ATOM   4684 O OD1 . ASN B 1 127 ? 76.873 21.035 -57.836 1.00 11.45 ? 127  ASN B OD1 1 
ATOM   4685 N ND2 . ASN B 1 127 ? 77.583 22.880 -56.786 1.00 6.58  ? 127  ASN B ND2 1 
ATOM   4686 N N   . HIS B 1 128 ? 74.536 23.598 -59.216 1.00 8.41  ? 128  HIS B N   1 
ATOM   4687 C CA  . HIS B 1 128 ? 73.513 24.548 -58.767 1.00 9.31  ? 128  HIS B CA  1 
ATOM   4688 C C   . HIS B 1 128 ? 72.929 23.989 -57.469 1.00 8.69  ? 128  HIS B C   1 
ATOM   4689 O O   . HIS B 1 128 ? 71.847 23.397 -57.472 1.00 8.23  ? 128  HIS B O   1 
ATOM   4690 C CB  . HIS B 1 128 ? 72.444 24.791 -59.844 1.00 7.40  ? 128  HIS B CB  1 
ATOM   4691 C CG  . HIS B 1 128 ? 71.567 25.976 -59.575 1.00 9.35  ? 128  HIS B CG  1 
ATOM   4692 N ND1 . HIS B 1 128 ? 71.291 26.934 -60.530 1.00 8.69  ? 128  HIS B ND1 1 
ATOM   4693 C CD2 . HIS B 1 128 ? 70.874 26.340 -58.465 1.00 8.45  ? 128  HIS B CD2 1 
ATOM   4694 C CE1 . HIS B 1 128 ? 70.476 27.845 -60.018 1.00 10.62 ? 128  HIS B CE1 1 
ATOM   4695 N NE2 . HIS B 1 128 ? 70.211 27.511 -58.766 1.00 9.12  ? 128  HIS B NE2 1 
ATOM   4696 N N   . PHE B 1 129 ? 73.683 24.176 -56.377 1.00 7.54  ? 129  PHE B N   1 
ATOM   4697 C CA  . PHE B 1 129 ? 73.321 23.805 -55.011 1.00 9.07  ? 129  PHE B CA  1 
ATOM   4698 C C   . PHE B 1 129 ? 73.412 22.293 -54.804 1.00 10.62 ? 129  PHE B C   1 
ATOM   4699 O O   . PHE B 1 129 ? 74.154 21.830 -53.933 1.00 12.94 ? 129  PHE B O   1 
ATOM   4700 C CB  . PHE B 1 129 ? 71.910 24.300 -54.625 1.00 10.29 ? 129  PHE B CB  1 
ATOM   4701 C CG  . PHE B 1 129 ? 71.739 25.814 -54.619 1.00 7.71  ? 129  PHE B CG  1 
ATOM   4702 C CD1 . PHE B 1 129 ? 72.797 26.673 -54.881 1.00 8.55  ? 129  PHE B CD1 1 
ATOM   4703 C CD2 . PHE B 1 129 ? 70.491 26.373 -54.358 1.00 8.69  ? 129  PHE B CD2 1 
ATOM   4704 C CE1 . PHE B 1 129 ? 72.618 28.047 -54.865 1.00 8.30  ? 129  PHE B CE1 1 
ATOM   4705 C CE2 . PHE B 1 129 ? 70.296 27.747 -54.358 1.00 7.71  ? 129  PHE B CE2 1 
ATOM   4706 C CZ  . PHE B 1 129 ? 71.360 28.588 -54.617 1.00 10.54 ? 129  PHE B CZ  1 
ATOM   4707 N N   . THR B 1 130 ? 72.664 21.504 -55.574 1.00 9.67  ? 130  THR B N   1 
ATOM   4708 C CA  . THR B 1 130 ? 72.583 20.082 -55.256 1.00 9.18  ? 130  THR B CA  1 
ATOM   4709 C C   . THR B 1 130 ? 73.911 19.380 -55.502 1.00 9.65  ? 130  THR B C   1 
ATOM   4710 O O   . THR B 1 130 ? 74.669 19.715 -56.421 1.00 11.00 ? 130  THR B O   1 
ATOM   4711 C CB  . THR B 1 130 ? 71.486 19.383 -56.059 1.00 11.73 ? 130  THR B CB  1 
ATOM   4712 O OG1 . THR B 1 130 ? 71.915 19.210 -57.418 1.00 10.19 ? 130  THR B OG1 1 
ATOM   4713 C CG2 . THR B 1 130 ? 70.182 20.175 -56.000 1.00 9.69  ? 130  THR B CG2 1 
ATOM   4714 N N   . LEU B 1 131 ? 74.180 18.393 -54.661 1.00 8.48  ? 131  LEU B N   1 
ATOM   4715 C CA  . LEU B 1 131 ? 75.355 17.544 -54.718 1.00 9.96  ? 131  LEU B CA  1 
ATOM   4716 C C   . LEU B 1 131 ? 74.907 16.094 -54.761 1.00 8.51  ? 131  LEU B C   1 
ATOM   4717 O O   . LEU B 1 131 ? 73.868 15.749 -54.193 1.00 8.61  ? 131  LEU B O   1 
ATOM   4718 C CB  . LEU B 1 131 ? 76.247 17.767 -53.486 1.00 7.99  ? 131  LEU B CB  1 
ATOM   4719 C CG  . LEU B 1 131 ? 76.869 19.165 -53.345 1.00 9.86  ? 131  LEU B CG  1 
ATOM   4720 C CD1 . LEU B 1 131 ? 77.599 19.322 -51.995 1.00 9.46  ? 131  LEU B CD1 1 
ATOM   4721 C CD2 . LEU B 1 131 ? 77.825 19.410 -54.492 1.00 10.15 ? 131  LEU B CD2 1 
ATOM   4722 N N   . PRO B 1 132 ? 75.679 15.219 -55.401 1.00 10.40 ? 132  PRO B N   1 
ATOM   4723 C CA  . PRO B 1 132 ? 75.383 13.783 -55.317 1.00 10.97 ? 132  PRO B CA  1 
ATOM   4724 C C   . PRO B 1 132 ? 75.303 13.315 -53.870 1.00 7.63  ? 132  PRO B C   1 
ATOM   4725 O O   . PRO B 1 132 ? 76.074 13.741 -53.008 1.00 8.51  ? 132  PRO B O   1 
ATOM   4726 C CB  . PRO B 1 132 ? 76.563 13.132 -56.051 1.00 10.12 ? 132  PRO B CB  1 
ATOM   4727 C CG  . PRO B 1 132 ? 77.097 14.241 -56.955 1.00 9.27  ? 132  PRO B CG  1 
ATOM   4728 C CD  . PRO B 1 132 ? 76.921 15.485 -56.149 1.00 9.99  ? 132  PRO B CD  1 
ATOM   4729 N N   . LEU B 1 133 ? 74.354 12.419 -53.626 1.00 8.08  ? 133  LEU B N   1 
ATOM   4730 C CA  . LEU B 1 133 ? 74.172 11.821 -52.311 1.00 9.10  ? 133  LEU B CA  1 
ATOM   4731 C C   . LEU B 1 133 ? 75.412 11.069 -51.844 1.00 12.14 ? 133  LEU B C   1 
ATOM   4732 O O   . LEU B 1 133 ? 75.673 11.000 -50.636 1.00 10.54 ? 133  LEU B O   1 
ATOM   4733 C CB  . LEU B 1 133 ? 72.973 10.875 -52.362 1.00 12.97 ? 133  LEU B CB  1 
ATOM   4734 C CG  . LEU B 1 133 ? 72.360 10.369 -51.057 1.00 11.46 ? 133  LEU B CG  1 
ATOM   4735 C CD1 . LEU B 1 133 ? 72.147 11.488 -50.023 1.00 10.05 ? 133  LEU B CD1 1 
ATOM   4736 C CD2 . LEU B 1 133 ? 71.073 9.569  -51.351 1.00 19.40 ? 133  LEU B CD2 1 
ATOM   4737 N N   . TRP B 1 134 ? 76.182 10.485 -52.773 1.00 10.32 ? 134  TRP B N   1 
ATOM   4738 C CA  . TRP B 1 134 ? 77.424 9.820  -52.385 1.00 11.17 ? 134  TRP B CA  1 
ATOM   4739 C C   . TRP B 1 134 ? 78.475 10.814 -51.915 1.00 14.41 ? 134  TRP B C   1 
ATOM   4740 O O   . TRP B 1 134 ? 79.451 10.423 -51.262 1.00 12.46 ? 134  TRP B O   1 
ATOM   4741 C CB  . TRP B 1 134 ? 77.977 8.952  -53.537 1.00 14.30 ? 134  TRP B CB  1 
ATOM   4742 C CG  . TRP B 1 134 ? 78.195 9.611  -54.912 1.00 12.12 ? 134  TRP B CG  1 
ATOM   4743 C CD1 . TRP B 1 134 ? 77.424 9.433  -56.031 1.00 11.74 ? 134  TRP B CD1 1 
ATOM   4744 C CD2 . TRP B 1 134 ? 79.289 10.462 -55.320 1.00 11.86 ? 134  TRP B CD2 1 
ATOM   4745 N NE1 . TRP B 1 134 ? 77.943 10.145 -57.089 1.00 11.98 ? 134  TRP B NE1 1 
ATOM   4746 C CE2 . TRP B 1 134 ? 79.087 10.778 -56.685 1.00 11.22 ? 134  TRP B CE2 1 
ATOM   4747 C CE3 . TRP B 1 134 ? 80.411 10.991 -54.664 1.00 12.67 ? 134  TRP B CE3 1 
ATOM   4748 C CZ2 . TRP B 1 134 ? 79.958 11.607 -57.403 1.00 11.40 ? 134  TRP B CZ2 1 
ATOM   4749 C CZ3 . TRP B 1 134 ? 81.278 11.815 -55.380 1.00 12.93 ? 134  TRP B CZ3 1 
ATOM   4750 C CH2 . TRP B 1 134 ? 81.044 12.114 -56.737 1.00 10.69 ? 134  TRP B CH2 1 
ATOM   4751 N N   . LEU B 1 135 ? 78.285 12.093 -52.209 1.00 9.93  ? 135  LEU B N   1 
ATOM   4752 C CA  . LEU B 1 135 ? 79.173 13.127 -51.716 1.00 9.16  ? 135  LEU B CA  1 
ATOM   4753 C C   . LEU B 1 135 ? 78.633 13.826 -50.478 1.00 11.19 ? 135  LEU B C   1 
ATOM   4754 O O   . LEU B 1 135 ? 79.421 14.240 -49.617 1.00 12.72 ? 135  LEU B O   1 
ATOM   4755 C CB  . LEU B 1 135 ? 79.413 14.164 -52.824 1.00 11.55 ? 135  LEU B CB  1 
ATOM   4756 C CG  . LEU B 1 135 ? 80.392 15.270 -52.435 1.00 16.19 ? 135  LEU B CG  1 
ATOM   4757 C CD1 . LEU B 1 135 ? 81.776 14.684 -52.196 1.00 20.70 ? 135  LEU B CD1 1 
ATOM   4758 C CD2 . LEU B 1 135 ? 80.428 16.365 -53.492 1.00 10.71 ? 135  LEU B CD2 1 
ATOM   4759 N N   . HIS B 1 136 ? 77.309 13.969 -50.363 1.00 9.86  ? 136  HIS B N   1 
ATOM   4760 C CA  . HIS B 1 136 ? 76.702 14.721 -49.262 1.00 9.51  ? 136  HIS B CA  1 
ATOM   4761 C C   . HIS B 1 136 ? 75.390 14.063 -48.857 1.00 9.64  ? 136  HIS B C   1 
ATOM   4762 O O   . HIS B 1 136 ? 74.425 14.077 -49.631 1.00 9.66  ? 136  HIS B O   1 
ATOM   4763 C CB  . HIS B 1 136 ? 76.448 16.175 -49.655 1.00 7.30  ? 136  HIS B CB  1 
ATOM   4764 C CG  . HIS B 1 136 ? 76.040 17.042 -48.507 1.00 10.05 ? 136  HIS B CG  1 
ATOM   4765 N ND1 . HIS B 1 136 ? 75.291 18.190 -48.667 1.00 8.95  ? 136  HIS B ND1 1 
ATOM   4766 C CD2 . HIS B 1 136 ? 76.293 16.938 -47.178 1.00 10.26 ? 136  HIS B CD2 1 
ATOM   4767 C CE1 . HIS B 1 136 ? 75.097 18.753 -47.486 1.00 9.99  ? 136  HIS B CE1 1 
ATOM   4768 N NE2 . HIS B 1 136 ? 75.695 18.014 -46.566 1.00 9.53  ? 136  HIS B NE2 1 
ATOM   4769 N N   . ASP B 1 137 ? 75.335 13.517 -47.644 1.00 8.76  ? 137  ASP B N   1 
ATOM   4770 C CA  . ASP B 1 137 ? 74.047 13.153 -47.061 1.00 11.79 ? 137  ASP B CA  1 
ATOM   4771 C C   . ASP B 1 137 ? 73.768 14.120 -45.919 1.00 11.26 ? 137  ASP B C   1 
ATOM   4772 O O   . ASP B 1 137 ? 74.322 13.959 -44.823 1.00 9.31  ? 137  ASP B O   1 
ATOM   4773 C CB  . ASP B 1 137 ? 74.023 11.698 -46.568 1.00 14.06 ? 137  ASP B CB  1 
ATOM   4774 C CG  . ASP B 1 137 ? 72.658 11.293 -45.991 1.00 17.13 ? 137  ASP B CG  1 
ATOM   4775 O OD1 . ASP B 1 137 ? 71.993 12.116 -45.318 1.00 12.81 ? 137  ASP B OD1 1 
ATOM   4776 O OD2 . ASP B 1 137 ? 72.239 10.146 -46.221 1.00 16.51 ? 137  ASP B OD2 1 
ATOM   4777 N N   . PRO B 1 138 ? 72.912 15.129 -46.119 1.00 9.96  ? 138  PRO B N   1 
ATOM   4778 C CA  . PRO B 1 138 ? 72.756 16.168 -45.093 1.00 10.66 ? 138  PRO B CA  1 
ATOM   4779 C C   . PRO B 1 138 ? 71.966 15.717 -43.879 1.00 9.59  ? 138  PRO B C   1 
ATOM   4780 O O   . PRO B 1 138 ? 72.050 16.382 -42.842 1.00 11.59 ? 138  PRO B O   1 
ATOM   4781 C CB  . PRO B 1 138 ? 72.030 17.291 -45.849 1.00 8.68  ? 138  PRO B CB  1 
ATOM   4782 C CG  . PRO B 1 138 ? 71.155 16.541 -46.813 1.00 9.26  ? 138  PRO B CG  1 
ATOM   4783 C CD  . PRO B 1 138 ? 72.010 15.352 -47.261 1.00 10.83 ? 138  PRO B CD  1 
ATOM   4784 N N   . ILE B 1 139 ? 71.208 14.620 -43.966 1.00 9.05  ? 139  ILE B N   1 
ATOM   4785 C CA  . ILE B 1 139 ? 70.524 14.095 -42.789 1.00 10.56 ? 139  ILE B CA  1 
ATOM   4786 C C   . ILE B 1 139 ? 71.510 13.378 -41.870 1.00 12.40 ? 139  ILE B C   1 
ATOM   4787 O O   . ILE B 1 139 ? 71.450 13.534 -40.643 1.00 9.40  ? 139  ILE B O   1 
ATOM   4788 C CB  . ILE B 1 139 ? 69.355 13.178 -43.197 1.00 9.65  ? 139  ILE B CB  1 
ATOM   4789 C CG1 . ILE B 1 139 ? 68.316 13.950 -44.015 1.00 10.25 ? 139  ILE B CG1 1 
ATOM   4790 C CG2 . ILE B 1 139 ? 68.675 12.589 -41.961 1.00 11.60 ? 139  ILE B CG2 1 
ATOM   4791 C CD1 . ILE B 1 139 ? 67.588 15.034 -43.206 1.00 10.67 ? 139  ILE B CD1 1 
ATOM   4792 N N   . ARG B 1 140 ? 72.439 12.598 -42.442 1.00 12.40 ? 140  ARG B N   1 
ATOM   4793 C CA  . ARG B 1 140 ? 73.503 12.011 -41.632 1.00 13.49 ? 140  ARG B CA  1 
ATOM   4794 C C   . ARG B 1 140 ? 74.326 13.102 -40.946 1.00 12.56 ? 140  ARG B C   1 
ATOM   4795 O O   . ARG B 1 140 ? 74.651 12.988 -39.756 1.00 10.59 ? 140  ARG B O   1 
ATOM   4796 C CB  . ARG B 1 140 ? 74.399 11.109 -42.491 1.00 11.96 ? 140  ARG B CB  1 
ATOM   4797 C CG  . ARG B 1 140 ? 73.717 9.847  -43.069 1.00 16.19 ? 140  ARG B CG  1 
ATOM   4798 C CD  . ARG B 1 140 ? 73.187 8.913  -41.957 1.00 18.11 ? 140  ARG B CD  1 
ATOM   4799 N NE  . ARG B 1 140 ? 74.231 8.540  -41.002 1.00 21.28 ? 140  ARG B NE  1 
ATOM   4800 C CZ  . ARG B 1 140 ? 74.028 7.841  -39.892 1.00 23.64 ? 140  ARG B CZ  1 
ATOM   4801 N NH1 . ARG B 1 140 ? 72.822 7.406  -39.557 1.00 25.47 ? 140  ARG B NH1 1 
ATOM   4802 N NH2 . ARG B 1 140 ? 75.060 7.580  -39.092 1.00 22.12 ? 140  ARG B NH2 1 
ATOM   4803 N N   . VAL B 1 141 ? 74.651 14.176 -41.679 1.00 11.19 ? 141  VAL B N   1 
ATOM   4804 C CA  . VAL B 1 141 ? 75.409 15.293 -41.107 1.00 10.68 ? 141  VAL B CA  1 
ATOM   4805 C C   . VAL B 1 141 ? 74.626 15.957 -39.979 1.00 14.14 ? 141  VAL B C   1 
ATOM   4806 O O   . VAL B 1 141 ? 75.139 16.149 -38.874 1.00 12.80 ? 141  VAL B O   1 
ATOM   4807 C CB  . VAL B 1 141 ? 75.773 16.322 -42.198 1.00 9.82  ? 141  VAL B CB  1 
ATOM   4808 C CG1 . VAL B 1 141 ? 76.352 17.598 -41.561 1.00 8.03  ? 141  VAL B CG1 1 
ATOM   4809 C CG2 . VAL B 1 141 ? 76.767 15.727 -43.210 1.00 10.00 ? 141  VAL B CG2 1 
ATOM   4810 N N   . SER B 1 142 ? 73.375 16.339 -40.248 1.00 14.12 ? 142  SER B N   1 
ATOM   4811 C CA  . SER B 1 142 ? 72.672 17.212 -39.309 1.00 17.79 ? 142  SER B CA  1 
ATOM   4812 C C   . SER B 1 142 ? 72.122 16.456 -38.104 1.00 13.92 ? 142  SER B C   1 
ATOM   4813 O O   . SER B 1 142 ? 72.210 16.949 -36.977 1.00 14.34 ? 142  SER B O   1 
ATOM   4814 C CB  . SER B 1 142 ? 71.537 17.954 -40.015 1.00 17.78 ? 142  SER B CB  1 
ATOM   4815 O OG  . SER B 1 142 ? 70.472 17.083 -40.318 1.00 25.88 ? 142  SER B OG  1 
ATOM   4816 N N   . ARG B 1 143 ? 71.542 15.274 -38.311 1.00 12.95 ? 143  ARG B N   1 
ATOM   4817 C CA  . ARG B 1 143 ? 70.862 14.570 -37.229 1.00 11.85 ? 143  ARG B CA  1 
ATOM   4818 C C   . ARG B 1 143 ? 71.751 13.547 -36.527 1.00 18.62 ? 143  ARG B C   1 
ATOM   4819 O O   . ARG B 1 143 ? 71.499 13.234 -35.359 1.00 14.53 ? 143  ARG B O   1 
ATOM   4820 C CB  . ARG B 1 143 ? 69.597 13.874 -37.763 1.00 12.37 ? 143  ARG B CB  1 
ATOM   4821 C CG  . ARG B 1 143 ? 68.619 13.373 -36.678 1.00 14.67 ? 143  ARG B CG  1 
ATOM   4822 C CD  . ARG B 1 143 ? 67.253 13.028 -37.302 1.00 15.24 ? 143  ARG B CD  1 
ATOM   4823 N NE  . ARG B 1 143 ? 66.660 14.217 -37.903 1.00 11.81 ? 143  ARG B NE  1 
ATOM   4824 C CZ  . ARG B 1 143 ? 66.021 14.243 -39.065 1.00 13.36 ? 143  ARG B CZ  1 
ATOM   4825 N NH1 . ARG B 1 143 ? 65.766 13.132 -39.745 1.00 11.92 ? 143  ARG B NH1 1 
ATOM   4826 N NH2 . ARG B 1 143 ? 65.636 15.416 -39.561 1.00 13.09 ? 143  ARG B NH2 1 
ATOM   4827 N N   . PHE B 1 144 ? 72.792 13.030 -37.187 1.00 15.55 ? 144  PHE B N   1 
ATOM   4828 C CA  . PHE B 1 144 ? 73.584 11.949 -36.608 1.00 15.83 ? 144  PHE B CA  1 
ATOM   4829 C C   . PHE B 1 144 ? 75.063 12.278 -36.492 1.00 16.38 ? 144  PHE B C   1 
ATOM   4830 O O   . PHE B 1 144 ? 75.864 11.371 -36.253 1.00 19.59 ? 144  PHE B O   1 
ATOM   4831 C CB  . PHE B 1 144 ? 73.378 10.663 -37.413 1.00 17.21 ? 144  PHE B CB  1 
ATOM   4832 C CG  . PHE B 1 144 ? 71.946 10.241 -37.464 1.00 21.76 ? 144  PHE B CG  1 
ATOM   4833 C CD1 . PHE B 1 144 ? 71.360 9.623  -36.363 1.00 27.92 ? 144  PHE B CD1 1 
ATOM   4834 C CD2 . PHE B 1 144 ? 71.166 10.495 -38.583 1.00 18.86 ? 144  PHE B CD2 1 
ATOM   4835 C CE1 . PHE B 1 144 ? 70.020 9.256  -36.379 1.00 27.36 ? 144  PHE B CE1 1 
ATOM   4836 C CE2 . PHE B 1 144 ? 69.826 10.126 -38.611 1.00 19.75 ? 144  PHE B CE2 1 
ATOM   4837 C CZ  . PHE B 1 144 ? 69.251 9.507  -37.507 1.00 25.19 ? 144  PHE B CZ  1 
ATOM   4838 N N   . ASN B 1 145 ? 75.439 13.549 -36.635 1.00 14.18 ? 145  ASN B N   1 
ATOM   4839 C CA  . ASN B 1 145 ? 76.832 13.995 -36.517 1.00 17.08 ? 145  ASN B CA  1 
ATOM   4840 C C   . ASN B 1 145 ? 77.775 13.130 -37.350 1.00 18.38 ? 145  ASN B C   1 
ATOM   4841 O O   . ASN B 1 145 ? 78.914 12.866 -36.958 1.00 21.61 ? 145  ASN B O   1 
ATOM   4842 C CB  . ASN B 1 145 ? 77.282 14.022 -35.051 1.00 20.83 ? 145  ASN B CB  1 
ATOM   4843 C CG  . ASN B 1 145 ? 78.526 14.866 -34.841 1.00 24.95 ? 145  ASN B CG  1 
ATOM   4844 O OD1 . ASN B 1 145 ? 78.571 16.027 -35.245 1.00 24.58 ? 145  ASN B OD1 1 
ATOM   4845 N ND2 . ASN B 1 145 ? 79.547 14.282 -34.223 1.00 28.57 ? 145  ASN B ND2 1 
ATOM   4846 N N   . ASP B 1 146 ? 77.306 12.665 -38.501 1.00 14.97 ? 146  ASP B N   1 
ATOM   4847 C CA  . ASP B 1 146 ? 78.069 11.744 -39.338 1.00 14.27 ? 146  ASP B CA  1 
ATOM   4848 C C   . ASP B 1 146 ? 78.561 12.529 -40.548 1.00 16.56 ? 146  ASP B C   1 
ATOM   4849 O O   . ASP B 1 146 ? 77.773 12.879 -41.434 1.00 12.67 ? 146  ASP B O   1 
ATOM   4850 C CB  . ASP B 1 146 ? 77.206 10.540 -39.715 1.00 19.41 ? 146  ASP B CB  1 
ATOM   4851 C CG  . ASP B 1 146 ? 77.819 9.673  -40.810 1.00 21.28 ? 146  ASP B CG  1 
ATOM   4852 O OD1 . ASP B 1 146 ? 79.007 9.847  -41.164 1.00 18.40 ? 146  ASP B OD1 1 
ATOM   4853 O OD2 . ASP B 1 146 ? 77.086 8.791  -41.307 1.00 22.45 ? 146  ASP B OD2 1 
ATOM   4854 N N   . PHE B 1 147 ? 79.867 12.802 -40.585 1.00 12.91 ? 147  PHE B N   1 
ATOM   4855 C CA  . PHE B 1 147 ? 80.460 13.630 -41.623 1.00 16.40 ? 147  PHE B CA  1 
ATOM   4856 C C   . PHE B 1 147 ? 81.180 12.806 -42.691 1.00 17.85 ? 147  PHE B C   1 
ATOM   4857 O O   . PHE B 1 147 ? 82.040 13.340 -43.392 1.00 15.35 ? 147  PHE B O   1 
ATOM   4858 C CB  . PHE B 1 147 ? 81.415 14.648 -40.995 1.00 17.69 ? 147  PHE B CB  1 
ATOM   4859 C CG  . PHE B 1 147 ? 80.713 15.770 -40.266 1.00 17.63 ? 147  PHE B CG  1 
ATOM   4860 C CD1 . PHE B 1 147 ? 80.209 15.576 -38.987 1.00 21.18 ? 147  PHE B CD1 1 
ATOM   4861 C CD2 . PHE B 1 147 ? 80.569 17.021 -40.850 1.00 14.44 ? 147  PHE B CD2 1 
ATOM   4862 C CE1 . PHE B 1 147 ? 79.560 16.604 -38.310 1.00 17.90 ? 147  PHE B CE1 1 
ATOM   4863 C CE2 . PHE B 1 147 ? 79.934 18.056 -40.174 1.00 13.11 ? 147  PHE B CE2 1 
ATOM   4864 C CZ  . PHE B 1 147 ? 79.424 17.845 -38.905 1.00 16.00 ? 147  PHE B CZ  1 
ATOM   4865 N N   . SER B 1 148 ? 80.843 11.518 -42.835 1.00 16.96 ? 148  SER B N   1 
ATOM   4866 C CA  . SER B 1 148 ? 81.550 10.704 -43.820 1.00 20.81 ? 148  SER B CA  1 
ATOM   4867 C C   . SER B 1 148 ? 81.229 11.147 -45.242 1.00 23.08 ? 148  SER B C   1 
ATOM   4868 O O   . SER B 1 148 ? 82.060 10.974 -46.141 1.00 20.29 ? 148  SER B O   1 
ATOM   4869 C CB  . SER B 1 148 ? 81.221 9.224  -43.638 1.00 20.21 ? 148  SER B CB  1 
ATOM   4870 O OG  . SER B 1 148 ? 79.830 8.993  -43.706 1.00 22.07 ? 148  SER B OG  1 
ATOM   4871 N N   . ARG B 1 149 ? 80.044 11.731 -45.464 1.00 15.70 ? 149  ARG B N   1 
ATOM   4872 C CA  . ARG B 1 149 ? 79.653 12.317 -46.753 1.00 13.21 ? 149  ARG B CA  1 
ATOM   4873 C C   . ARG B 1 149 ? 79.169 13.729 -46.438 1.00 10.53 ? 149  ARG B C   1 
ATOM   4874 O O   . ARG B 1 149 ? 77.975 13.947 -46.229 1.00 9.49  ? 149  ARG B O   1 
ATOM   4875 C CB  . ARG B 1 149 ? 78.572 11.488 -47.461 1.00 14.78 ? 149  ARG B CB  1 
ATOM   4876 C CG  . ARG B 1 149 ? 79.002 10.070 -47.839 1.00 18.53 ? 149  ARG B CG  1 
ATOM   4877 C CD  . ARG B 1 149 ? 77.846 9.257  -48.422 1.00 18.09 ? 149  ARG B CD  1 
ATOM   4878 N NE  . ARG B 1 149 ? 76.956 8.791  -47.363 1.00 22.41 ? 149  ARG B NE  1 
ATOM   4879 C CZ  . ARG B 1 149 ? 75.664 8.529  -47.517 1.00 27.11 ? 149  ARG B CZ  1 
ATOM   4880 N NH1 . ARG B 1 149 ? 75.076 8.600  -48.705 1.00 21.43 ? 149  ARG B NH1 1 
ATOM   4881 N NH2 . ARG B 1 149 ? 74.943 8.189  -46.451 1.00 21.03 ? 149  ARG B NH2 1 
ATOM   4882 N N   . SER B 1 150 ? 80.093 14.688 -46.399 1.00 11.44 ? 150  SER B N   1 
ATOM   4883 C CA  . SER B 1 150 ? 79.799 15.993 -45.816 1.00 12.69 ? 150  SER B CA  1 
ATOM   4884 C C   . SER B 1 150 ? 79.796 17.125 -46.840 1.00 9.71  ? 150  SER B C   1 
ATOM   4885 O O   . SER B 1 150 ? 79.879 18.294 -46.454 1.00 11.05 ? 150  SER B O   1 
ATOM   4886 C CB  . SER B 1 150 ? 80.795 16.311 -44.696 1.00 12.34 ? 150  SER B CB  1 
ATOM   4887 O OG  . SER B 1 150 ? 82.122 16.179 -45.157 1.00 14.65 ? 150  SER B OG  1 
ATOM   4888 N N   . GLY B 1 151 ? 79.692 16.815 -48.129 1.00 11.01 ? 151  GLY B N   1 
ATOM   4889 C CA  . GLY B 1 151 ? 79.536 17.882 -49.112 1.00 10.53 ? 151  GLY B CA  1 
ATOM   4890 C C   . GLY B 1 151 ? 80.796 18.722 -49.251 1.00 11.67 ? 151  GLY B C   1 
ATOM   4891 O O   . GLY B 1 151 ? 81.909 18.202 -49.328 1.00 13.59 ? 151  GLY B O   1 
ATOM   4892 N N   . TRP B 1 152 ? 80.621 20.048 -49.278 1.00 8.92  ? 152  TRP B N   1 
ATOM   4893 C CA  . TRP B 1 152 ? 81.764 20.938 -49.449 1.00 11.97 ? 152  TRP B CA  1 
ATOM   4894 C C   . TRP B 1 152 ? 82.656 20.995 -48.215 1.00 12.07 ? 152  TRP B C   1 
ATOM   4895 O O   . TRP B 1 152 ? 83.726 21.601 -48.281 1.00 11.47 ? 152  TRP B O   1 
ATOM   4896 C CB  . TRP B 1 152 ? 81.293 22.353 -49.814 1.00 9.17  ? 152  TRP B CB  1 
ATOM   4897 C CG  . TRP B 1 152 ? 80.669 22.421 -51.196 1.00 9.93  ? 152  TRP B CG  1 
ATOM   4898 C CD1 . TRP B 1 152 ? 79.378 22.761 -51.499 1.00 9.61  ? 152  TRP B CD1 1 
ATOM   4899 C CD2 . TRP B 1 152 ? 81.310 22.139 -52.442 1.00 9.00  ? 152  TRP B CD2 1 
ATOM   4900 N NE1 . TRP B 1 152 ? 79.175 22.704 -52.858 1.00 9.80  ? 152  TRP B NE1 1 
ATOM   4901 C CE2 . TRP B 1 152 ? 80.347 22.329 -53.461 1.00 9.90  ? 152  TRP B CE2 1 
ATOM   4902 C CE3 . TRP B 1 152 ? 82.615 21.761 -52.801 1.00 10.83 ? 152  TRP B CE3 1 
ATOM   4903 C CZ2 . TRP B 1 152 ? 80.640 22.150 -54.811 1.00 8.51  ? 152  TRP B CZ2 1 
ATOM   4904 C CZ3 . TRP B 1 152 ? 82.903 21.574 -54.137 1.00 11.83 ? 152  TRP B CZ3 1 
ATOM   4905 C CH2 . TRP B 1 152 ? 81.916 21.767 -55.131 1.00 9.84  ? 152  TRP B CH2 1 
ATOM   4906 N N   . LEU B 1 153 ? 82.250 20.383 -47.100 1.00 10.39 ? 153  LEU B N   1 
ATOM   4907 C CA  . LEU B 1 153 ? 83.161 20.203 -45.976 1.00 13.72 ? 153  LEU B CA  1 
ATOM   4908 C C   . LEU B 1 153 ? 84.153 19.076 -46.225 1.00 16.55 ? 153  LEU B C   1 
ATOM   4909 O O   . LEU B 1 153 ? 85.196 19.025 -45.570 1.00 16.53 ? 153  LEU B O   1 
ATOM   4910 C CB  . LEU B 1 153 ? 82.381 19.890 -44.696 1.00 9.91  ? 153  LEU B CB  1 
ATOM   4911 C CG  . LEU B 1 153 ? 81.354 20.923 -44.205 1.00 13.51 ? 153  LEU B CG  1 
ATOM   4912 C CD1 . LEU B 1 153 ? 80.763 20.491 -42.844 1.00 9.28  ? 153  LEU B CD1 1 
ATOM   4913 C CD2 . LEU B 1 153 ? 81.969 22.336 -44.124 1.00 10.85 ? 153  LEU B CD2 1 
ATOM   4914 N N   . ASP B 1 154 ? 83.819 18.168 -47.134 1.00 12.25 ? 154  ASP B N   1 
ATOM   4915 C CA  . ASP B 1 154 ? 84.583 16.955 -47.385 1.00 18.90 ? 154  ASP B CA  1 
ATOM   4916 C C   . ASP B 1 154 ? 85.832 17.347 -48.152 1.00 24.19 ? 154  ASP B C   1 
ATOM   4917 O O   . ASP B 1 154 ? 85.737 17.883 -49.261 1.00 16.32 ? 154  ASP B O   1 
ATOM   4918 C CB  . ASP B 1 154 ? 83.730 15.997 -48.221 1.00 22.09 ? 154  ASP B CB  1 
ATOM   4919 C CG  . ASP B 1 154 ? 83.940 14.536 -47.878 1.00 37.44 ? 154  ASP B CG  1 
ATOM   4920 O OD1 . ASP B 1 154 ? 85.038 14.019 -48.185 1.00 29.11 ? 154  ASP B OD1 1 
ATOM   4921 O OD2 . ASP B 1 154 ? 82.960 13.888 -47.402 1.00 32.60 ? 154  ASP B OD2 1 
ATOM   4922 N N   . ASP B 1 155 ? 86.999 17.139 -47.565 1.00 33.29 ? 155  ASP B N   1 
ATOM   4923 C CA  . ASP B 1 155 ? 88.190 17.176 -48.398 1.00 35.96 ? 155  ASP B CA  1 
ATOM   4924 C C   . ASP B 1 155 ? 88.236 15.859 -49.167 1.00 36.50 ? 155  ASP B C   1 
ATOM   4925 O O   . ASP B 1 155 ? 88.543 14.803 -48.605 1.00 54.60 ? 155  ASP B O   1 
ATOM   4926 C CB  . ASP B 1 155 ? 89.465 17.476 -47.603 1.00 43.15 ? 155  ASP B CB  1 
ATOM   4927 C CG  . ASP B 1 155 ? 89.476 18.909 -47.001 1.00 45.67 ? 155  ASP B CG  1 
ATOM   4928 O OD1 . ASP B 1 155 ? 88.399 19.545 -46.845 1.00 36.09 ? 155  ASP B OD1 1 
ATOM   4929 O OD2 . ASP B 1 155 ? 90.582 19.431 -46.734 1.00 42.80 ? 155  ASP B OD2 1 
ATOM   4930 N N   . ARG B 1 156 ? 88.007 15.977 -50.475 1.00 28.49 ? 156  ARG B N   1 
ATOM   4931 C CA  . ARG B 1 156 ? 87.510 14.978 -51.424 1.00 30.86 ? 156  ARG B CA  1 
ATOM   4932 C C   . ARG B 1 156 ? 86.589 15.681 -52.421 1.00 21.63 ? 156  ARG B C   1 
ATOM   4933 O O   . ARG B 1 156 ? 86.652 15.438 -53.632 1.00 19.37 ? 156  ARG B O   1 
ATOM   4934 C CB  . ARG B 1 156 ? 86.762 13.841 -50.729 1.00 34.92 ? 156  ARG B CB  1 
ATOM   4935 C CG  . ARG B 1 156 ? 86.925 12.501 -51.430 1.00 34.63 ? 156  ARG B CG  1 
ATOM   4936 C CD  . ARG B 1 156 ? 86.264 11.293 -50.737 1.00 41.54 ? 156  ARG B CD  1 
ATOM   4937 N NE  . ARG B 1 156 ? 87.260 10.413 -50.127 1.00 42.74 ? 156  ARG B NE  1 
ATOM   4938 C CZ  . ARG B 1 156 ? 87.129 9.097  -50.000 1.00 45.96 ? 156  ARG B CZ  1 
ATOM   4939 N NH1 . ARG B 1 156 ? 86.038 8.467  -50.407 1.00 44.60 ? 156  ARG B NH1 1 
ATOM   4940 N NH2 . ARG B 1 156 ? 88.127 8.392  -49.474 1.00 46.32 ? 156  ARG B NH2 1 
ATOM   4941 N N   . SER B 1 157 ? 85.721 16.558 -51.908 1.00 14.84 ? 157  SER B N   1 
ATOM   4942 C CA  . SER B 1 157 ? 84.783 17.270 -52.774 1.00 15.38 ? 157  SER B CA  1 
ATOM   4943 C C   . SER B 1 157 ? 85.502 18.093 -53.844 1.00 9.78  ? 157  SER B C   1 
ATOM   4944 O O   . SER B 1 157 ? 85.086 18.098 -55.006 1.00 10.25 ? 157  SER B O   1 
ATOM   4945 C CB  . SER B 1 157 ? 83.848 18.125 -51.914 1.00 13.19 ? 157  SER B CB  1 
ATOM   4946 O OG  . SER B 1 157 ? 84.516 19.287 -51.429 1.00 19.52 ? 157  SER B OG  1 
ATOM   4947 N N   . VAL B 1 158 ? 86.604 18.751 -53.489 1.00 10.82 ? 158  VAL B N   1 
ATOM   4948 C CA  . VAL B 1 158 ? 87.334 19.569 -54.460 1.00 12.24 ? 158  VAL B CA  1 
ATOM   4949 C C   . VAL B 1 158 ? 87.852 18.702 -55.603 1.00 12.77 ? 158  VAL B C   1 
ATOM   4950 O O   . VAL B 1 158 ? 87.700 19.036 -56.785 1.00 12.26 ? 158  VAL B O   1 
ATOM   4951 C CB  . VAL B 1 158 ? 88.487 20.322 -53.769 1.00 14.41 ? 158  VAL B CB  1 
ATOM   4952 C CG1 . VAL B 1 158 ? 89.356 21.036 -54.792 1.00 10.65 ? 158  VAL B CG1 1 
ATOM   4953 C CG2 . VAL B 1 158 ? 87.951 21.313 -52.727 1.00 13.70 ? 158  VAL B CG2 1 
ATOM   4954 N N   . HIS B 1 159 ? 88.487 17.581 -55.265 1.00 13.33 ? 159  HIS B N   1 
ATOM   4955 C CA  . HIS B 1 159 ? 89.056 16.724 -56.299 1.00 17.64 ? 159  HIS B CA  1 
ATOM   4956 C C   . HIS B 1 159 ? 87.970 16.116 -57.183 1.00 15.81 ? 159  HIS B C   1 
ATOM   4957 O O   . HIS B 1 159 ? 88.127 16.050 -58.405 1.00 13.72 ? 159  HIS B O   1 
ATOM   4958 C CB  . HIS B 1 159 ? 89.911 15.626 -55.662 1.00 19.54 ? 159  HIS B CB  1 
ATOM   4959 C CG  . HIS B 1 159 ? 90.806 14.924 -56.638 1.00 29.03 ? 159  HIS B CG  1 
ATOM   4960 N ND1 . HIS B 1 159 ? 91.256 15.520 -57.798 1.00 37.74 ? 159  HIS B ND1 1 
ATOM   4961 C CD2 . HIS B 1 159 ? 91.274 13.654 -56.665 1.00 28.33 ? 159  HIS B CD2 1 
ATOM   4962 C CE1 . HIS B 1 159 ? 91.997 14.661 -58.475 1.00 37.43 ? 159  HIS B CE1 1 
ATOM   4963 N NE2 . HIS B 1 159 ? 92.018 13.519 -57.814 1.00 28.79 ? 159  HIS B NE2 1 
ATOM   4964 N N   . GLU B 1 160 ? 86.865 15.650 -56.594 1.00 9.60  ? 160  GLU B N   1 
ATOM   4965 C CA  . GLU B 1 160 ? 85.847 15.018 -57.428 1.00 11.73 ? 160  GLU B CA  1 
ATOM   4966 C C   . GLU B 1 160 ? 85.115 16.043 -58.303 1.00 11.52 ? 160  GLU B C   1 
ATOM   4967 O O   . GLU B 1 160 ? 84.712 15.720 -59.426 1.00 10.39 ? 160  GLU B O   1 
ATOM   4968 C CB  . GLU B 1 160 ? 84.868 14.230 -56.553 1.00 13.11 ? 160  GLU B CB  1 
ATOM   4969 C CG  . GLU B 1 160 ? 85.531 13.073 -55.763 1.00 19.41 ? 160  GLU B CG  1 
ATOM   4970 C CD  . GLU B 1 160 ? 86.608 12.326 -56.570 1.00 24.32 ? 160  GLU B CD  1 
ATOM   4971 O OE1 . GLU B 1 160 ? 86.287 11.813 -57.659 1.00 18.65 ? 160  GLU B OE1 1 
ATOM   4972 O OE2 . GLU B 1 160 ? 87.775 12.250 -56.119 1.00 21.54 ? 160  GLU B OE2 1 
ATOM   4973 N N   . PHE B 1 161 ? 84.937 17.275 -57.819 1.00 9.44  ? 161  PHE B N   1 
ATOM   4974 C CA  . PHE B 1 161 ? 84.359 18.311 -58.678 1.00 9.30  ? 161  PHE B CA  1 
ATOM   4975 C C   . PHE B 1 161 ? 85.286 18.635 -59.851 1.00 11.91 ? 161  PHE B C   1 
ATOM   4976 O O   . PHE B 1 161 ? 84.823 18.840 -60.980 1.00 10.19 ? 161  PHE B O   1 
ATOM   4977 C CB  . PHE B 1 161 ? 84.048 19.583 -57.872 1.00 8.10  ? 161  PHE B CB  1 
ATOM   4978 C CG  . PHE B 1 161 ? 83.376 20.660 -58.700 1.00 10.75 ? 161  PHE B CG  1 
ATOM   4979 C CD1 . PHE B 1 161 ? 82.034 20.547 -59.044 1.00 9.43  ? 161  PHE B CD1 1 
ATOM   4980 C CD2 . PHE B 1 161 ? 84.104 21.738 -59.191 1.00 9.52  ? 161  PHE B CD2 1 
ATOM   4981 C CE1 . PHE B 1 161 ? 81.414 21.518 -59.840 1.00 10.76 ? 161  PHE B CE1 1 
ATOM   4982 C CE2 . PHE B 1 161 ? 83.491 22.716 -59.982 1.00 9.95  ? 161  PHE B CE2 1 
ATOM   4983 C CZ  . PHE B 1 161 ? 82.147 22.603 -60.305 1.00 10.24 ? 161  PHE B CZ  1 
ATOM   4984 N N   . THR B 1 162 ? 86.597 18.682 -59.606 1.00 9.25  ? 162  THR B N   1 
ATOM   4985 C CA  . THR B 1 162 ? 87.542 18.895 -60.698 1.00 11.80 ? 162  THR B CA  1 
ATOM   4986 C C   . THR B 1 162 ? 87.383 17.832 -61.783 1.00 10.92 ? 162  THR B C   1 
ATOM   4987 O O   . THR B 1 162 ? 87.367 18.154 -62.974 1.00 12.57 ? 162  THR B O   1 
ATOM   4988 C CB  . THR B 1 162 ? 88.970 18.912 -60.144 1.00 17.75 ? 162  THR B CB  1 
ATOM   4989 O OG1 . THR B 1 162 ? 89.054 19.916 -59.132 1.00 16.55 ? 162  THR B OG1 1 
ATOM   4990 C CG2 . THR B 1 162 ? 89.966 19.264 -61.225 1.00 15.80 ? 162  THR B CG2 1 
ATOM   4991 N N   . LYS B 1 163 ? 87.223 16.567 -61.388 1.00 13.57 ? 163  LYS B N   1 
ATOM   4992 C CA  . LYS B 1 163 ? 87.041 15.484 -62.355 1.00 13.56 ? 163  LYS B CA  1 
ATOM   4993 C C   . LYS B 1 163 ? 85.752 15.648 -63.140 1.00 12.98 ? 163  LYS B C   1 
ATOM   4994 O O   . LYS B 1 163 ? 85.699 15.365 -64.346 1.00 10.54 ? 163  LYS B O   1 
ATOM   4995 C CB  . LYS B 1 163 ? 87.000 14.137 -61.635 1.00 12.54 ? 163  LYS B CB  1 
ATOM   4996 C CG  . LYS B 1 163 ? 88.332 13.567 -61.206 1.00 22.63 ? 163  LYS B CG  1 
ATOM   4997 C CD  . LYS B 1 163 ? 88.069 12.601 -60.075 1.00 25.18 ? 163  LYS B CD  1 
ATOM   4998 C CE  . LYS B 1 163 ? 89.182 11.621 -59.832 1.00 29.44 ? 163  LYS B CE  1 
ATOM   4999 N NZ  . LYS B 1 163 ? 88.705 10.629 -58.831 1.00 21.84 ? 163  LYS B NZ  1 
ATOM   5000 N N   . PHE B 1 164 ? 84.680 16.018 -62.444 1.00 9.79  ? 164  PHE B N   1 
ATOM   5001 C CA  . PHE B 1 164 ? 83.402 16.285 -63.091 1.00 10.08 ? 164  PHE B CA  1 
ATOM   5002 C C   . PHE B 1 164 ? 83.528 17.439 -64.081 1.00 10.09 ? 164  PHE B C   1 
ATOM   5003 O O   . PHE B 1 164 ? 83.059 17.343 -65.222 1.00 10.50 ? 164  PHE B O   1 
ATOM   5004 C CB  . PHE B 1 164 ? 82.360 16.552 -61.991 1.00 10.79 ? 164  PHE B CB  1 
ATOM   5005 C CG  . PHE B 1 164 ? 81.033 17.060 -62.485 1.00 10.76 ? 164  PHE B CG  1 
ATOM   5006 C CD1 . PHE B 1 164 ? 80.262 16.321 -63.363 1.00 8.81  ? 164  PHE B CD1 1 
ATOM   5007 C CD2 . PHE B 1 164 ? 80.547 18.277 -62.033 1.00 12.94 ? 164  PHE B CD2 1 
ATOM   5008 C CE1 . PHE B 1 164 ? 79.024 16.795 -63.798 1.00 13.28 ? 164  PHE B CE1 1 
ATOM   5009 C CE2 . PHE B 1 164 ? 79.318 18.758 -62.468 1.00 10.60 ? 164  PHE B CE2 1 
ATOM   5010 C CZ  . PHE B 1 164 ? 78.556 18.018 -63.342 1.00 10.06 ? 164  PHE B CZ  1 
ATOM   5011 N N   . ALA B 1 165 ? 84.214 18.514 -63.685 1.00 9.57  ? 165  ALA B N   1 
ATOM   5012 C CA  . ALA B 1 165 ? 84.395 19.658 -64.581 1.00 11.90 ? 165  ALA B CA  1 
ATOM   5013 C C   . ALA B 1 165 ? 85.195 19.276 -65.822 1.00 11.73 ? 165  ALA B C   1 
ATOM   5014 O O   . ALA B 1 165 ? 84.886 19.728 -66.931 1.00 12.49 ? 165  ALA B O   1 
ATOM   5015 C CB  . ALA B 1 165 ? 85.097 20.809 -63.843 1.00 11.53 ? 165  ALA B CB  1 
ATOM   5016 N N   . THR B 1 166 ? 86.262 18.494 -65.639 1.00 11.17 ? 166  THR B N   1 
ATOM   5017 C CA  . THR B 1 166 ? 87.046 18.004 -66.769 1.00 14.51 ? 166  THR B CA  1 
ATOM   5018 C C   . THR B 1 166 ? 86.170 17.222 -67.736 1.00 13.92 ? 166  THR B C   1 
ATOM   5019 O O   . THR B 1 166 ? 86.228 17.424 -68.955 1.00 15.29 ? 166  THR B O   1 
ATOM   5020 C CB  . THR B 1 166 ? 88.194 17.108 -66.279 1.00 17.15 ? 166  THR B CB  1 
ATOM   5021 O OG1 . THR B 1 166 ? 89.044 17.826 -65.382 1.00 21.05 ? 166  THR B OG1 1 
ATOM   5022 C CG2 . THR B 1 166 ? 89.032 16.614 -67.466 1.00 24.18 ? 166  THR B CG2 1 
ATOM   5023 N N   . PHE B 1 167 ? 85.360 16.307 -67.207 1.00 13.16 ? 167  PHE B N   1 
ATOM   5024 C CA  . PHE B 1 167 ? 84.518 15.485 -68.064 1.00 14.18 ? 167  PHE B CA  1 
ATOM   5025 C C   . PHE B 1 167 ? 83.511 16.334 -68.832 1.00 17.05 ? 167  PHE B C   1 
ATOM   5026 O O   . PHE B 1 167 ? 83.246 16.083 -70.019 1.00 13.26 ? 167  PHE B O   1 
ATOM   5027 C CB  . PHE B 1 167 ? 83.803 14.429 -67.224 1.00 13.28 ? 167  PHE B CB  1 
ATOM   5028 C CG  . PHE B 1 167 ? 82.838 13.586 -68.007 1.00 13.71 ? 167  PHE B CG  1 
ATOM   5029 C CD1 . PHE B 1 167 ? 83.284 12.485 -68.726 1.00 17.49 ? 167  PHE B CD1 1 
ATOM   5030 C CD2 . PHE B 1 167 ? 81.490 13.900 -68.039 1.00 15.64 ? 167  PHE B CD2 1 
ATOM   5031 C CE1 . PHE B 1 167 ? 82.395 11.712 -69.458 1.00 20.40 ? 167  PHE B CE1 1 
ATOM   5032 C CE2 . PHE B 1 167 ? 80.597 13.130 -68.762 1.00 13.66 ? 167  PHE B CE2 1 
ATOM   5033 C CZ  . PHE B 1 167 ? 81.050 12.037 -69.474 1.00 19.00 ? 167  PHE B CZ  1 
ATOM   5034 N N   . CYS B 1 168 ? 82.939 17.346 -68.174 1.00 10.21 ? 168  CYS B N   1 
ATOM   5035 C CA  . CYS B 1 168 ? 81.947 18.181 -68.851 1.00 12.89 ? 168  CYS B CA  1 
ATOM   5036 C C   . CYS B 1 168 ? 82.578 19.011 -69.965 1.00 12.77 ? 168  CYS B C   1 
ATOM   5037 O O   . CYS B 1 168 ? 81.987 19.160 -71.042 1.00 13.09 ? 168  CYS B O   1 
ATOM   5038 C CB  . CYS B 1 168 ? 81.244 19.088 -67.840 1.00 12.35 ? 168  CYS B CB  1 
ATOM   5039 S SG  . CYS B 1 168 ? 80.165 18.196 -66.693 1.00 14.10 ? 168  CYS B SG  1 
ATOM   5040 N N   . ALA B 1 169 ? 83.763 19.580 -69.719 1.00 13.52 ? 169  ALA B N   1 
ATOM   5041 C CA  . ALA B 1 169 ? 84.421 20.389 -70.737 1.00 13.52 ? 169  ALA B CA  1 
ATOM   5042 C C   . ALA B 1 169 ? 84.743 19.558 -71.971 1.00 19.32 ? 169  ALA B C   1 
ATOM   5043 O O   . ALA B 1 169 ? 84.642 20.050 -73.102 1.00 18.77 ? 169  ALA B O   1 
ATOM   5044 C CB  . ALA B 1 169 ? 85.695 21.028 -70.175 1.00 12.79 ? 169  ALA B CB  1 
ATOM   5045 N N   . LYS B 1 170 ? 85.121 18.294 -71.775 1.00 16.42 ? 170  LYS B N   1 
ATOM   5046 C CA  . LYS B 1 170 ? 85.394 17.429 -72.914 1.00 19.08 ? 170  LYS B CA  1 
ATOM   5047 C C   . LYS B 1 170 ? 84.111 16.980 -73.592 1.00 19.24 ? 170  LYS B C   1 
ATOM   5048 O O   . LYS B 1 170 ? 84.085 16.827 -74.819 1.00 20.04 ? 170  LYS B O   1 
ATOM   5049 C CB  . LYS B 1 170 ? 86.197 16.203 -72.478 1.00 17.86 ? 170  LYS B CB  1 
ATOM   5050 C CG  . LYS B 1 170 ? 87.598 16.491 -71.969 1.00 21.95 ? 170  LYS B CG  1 
ATOM   5051 C CD  . LYS B 1 170 ? 88.375 15.190 -71.883 1.00 28.01 ? 170  LYS B CD  1 
ATOM   5052 C CE  . LYS B 1 170 ? 89.279 15.158 -70.672 1.00 30.87 ? 170  LYS B CE  1 
ATOM   5053 N NZ  . LYS B 1 170 ? 90.332 14.105 -70.776 1.00 36.78 ? 170  LYS B NZ  1 
ATOM   5054 N N   . SER B 1 171 ? 83.040 16.770 -72.822 1.00 12.76 ? 171  SER B N   1 
ATOM   5055 C CA  . SER B 1 171 ? 81.857 16.112 -73.366 1.00 15.62 ? 171  SER B CA  1 
ATOM   5056 C C   . SER B 1 171 ? 80.932 17.084 -74.090 1.00 20.70 ? 171  SER B C   1 
ATOM   5057 O O   . SER B 1 171 ? 80.420 16.759 -75.168 1.00 17.64 ? 171  SER B O   1 
ATOM   5058 C CB  . SER B 1 171 ? 81.089 15.400 -72.251 1.00 16.84 ? 171  SER B CB  1 
ATOM   5059 O OG  . SER B 1 171 ? 81.892 14.390 -71.677 1.00 20.79 ? 171  SER B OG  1 
ATOM   5060 N N   . PHE B 1 172 ? 80.701 18.271 -73.519 1.00 13.35 ? 172  PHE B N   1 
ATOM   5061 C CA  . PHE B 1 172 ? 79.676 19.190 -74.018 1.00 15.12 ? 172  PHE B CA  1 
ATOM   5062 C C   . PHE B 1 172 ? 80.346 20.234 -74.906 1.00 20.57 ? 172  PHE B C   1 
ATOM   5063 O O   . PHE B 1 172 ? 80.576 21.376 -74.517 1.00 17.72 ? 172  PHE B O   1 
ATOM   5064 C CB  . PHE B 1 172 ? 78.907 19.820 -72.852 1.00 15.86 ? 172  PHE B CB  1 
ATOM   5065 C CG  . PHE B 1 172 ? 78.176 18.818 -72.013 1.00 12.80 ? 172  PHE B CG  1 
ATOM   5066 C CD1 . PHE B 1 172 ? 77.097 18.130 -72.535 1.00 12.64 ? 172  PHE B CD1 1 
ATOM   5067 C CD2 . PHE B 1 172 ? 78.583 18.540 -70.713 1.00 16.20 ? 172  PHE B CD2 1 
ATOM   5068 C CE1 . PHE B 1 172 ? 76.429 17.175 -71.787 1.00 14.69 ? 172  PHE B CE1 1 
ATOM   5069 C CE2 . PHE B 1 172 ? 77.913 17.593 -69.942 1.00 13.32 ? 172  PHE B CE2 1 
ATOM   5070 C CZ  . PHE B 1 172 ? 76.832 16.908 -70.479 1.00 13.97 ? 172  PHE B CZ  1 
ATOM   5071 N N   . ASP B 1 173 ? 80.642 19.828 -76.134 1.00 21.01 ? 173  ASP B N   1 
ATOM   5072 C CA  . ASP B 1 173 ? 81.402 20.665 -77.047 1.00 24.21 ? 173  ASP B CA  1 
ATOM   5073 C C   . ASP B 1 173 ? 80.528 21.561 -77.911 1.00 28.59 ? 173  ASP B C   1 
ATOM   5074 O O   . ASP B 1 173 ? 81.064 22.295 -78.745 1.00 32.30 ? 173  ASP B O   1 
ATOM   5075 C CB  . ASP B 1 173 ? 82.299 19.795 -77.939 1.00 31.12 ? 173  ASP B CB  1 
ATOM   5076 C CG  . ASP B 1 173 ? 81.507 18.769 -78.731 1.00 34.98 ? 173  ASP B CG  1 
ATOM   5077 O OD1 . ASP B 1 173 ? 80.838 19.150 -79.718 1.00 44.06 ? 173  ASP B OD1 1 
ATOM   5078 O OD2 . ASP B 1 173 ? 81.526 17.585 -78.343 1.00 44.37 ? 173  ASP B OD2 1 
ATOM   5079 N N   . ASP B 1 174 ? 79.208 21.542 -77.741 1.00 20.41 ? 174  ASP B N   1 
ATOM   5080 C CA  . ASP B 1 174 ? 78.367 22.468 -78.487 1.00 24.82 ? 174  ASP B CA  1 
ATOM   5081 C C   . ASP B 1 174 ? 77.754 23.566 -77.621 1.00 24.40 ? 174  ASP B C   1 
ATOM   5082 O O   . ASP B 1 174 ? 76.858 24.267 -78.085 1.00 22.08 ? 174  ASP B O   1 
ATOM   5083 C CB  . ASP B 1 174 ? 77.268 21.713 -79.241 1.00 34.69 ? 174  ASP B CB  1 
ATOM   5084 C CG  . ASP B 1 174 ? 76.749 22.498 -80.449 1.00 40.62 ? 174  ASP B CG  1 
ATOM   5085 O OD1 . ASP B 1 174 ? 77.569 23.155 -81.133 1.00 44.01 ? 174  ASP B OD1 1 
ATOM   5086 O OD2 . ASP B 1 174 ? 75.518 22.496 -80.683 1.00 45.78 ? 174  ASP B OD2 1 
ATOM   5087 N N   . VAL B 1 175 ? 78.220 23.762 -76.390 1.00 16.79 ? 175  VAL B N   1 
ATOM   5088 C CA  . VAL B 1 175 ? 77.704 24.882 -75.609 1.00 16.51 ? 175  VAL B CA  1 
ATOM   5089 C C   . VAL B 1 175 ? 78.394 26.169 -76.046 1.00 14.91 ? 175  VAL B C   1 
ATOM   5090 O O   . VAL B 1 175 ? 79.453 26.158 -76.676 1.00 13.50 ? 175  VAL B O   1 
ATOM   5091 C CB  . VAL B 1 175 ? 77.894 24.639 -74.106 1.00 15.10 ? 175  VAL B CB  1 
ATOM   5092 C CG1 . VAL B 1 175 ? 77.340 23.293 -73.738 1.00 14.66 ? 175  VAL B CG1 1 
ATOM   5093 C CG2 . VAL B 1 175 ? 79.369 24.752 -73.762 1.00 15.37 ? 175  VAL B CG2 1 
ATOM   5094 N N   . ASP B 1 176 ? 77.804 27.300 -75.668 1.00 12.19 ? 176  ASP B N   1 
ATOM   5095 C CA  . ASP B 1 176 ? 78.412 28.592 -75.949 1.00 14.53 ? 176  ASP B CA  1 
ATOM   5096 C C   . ASP B 1 176 ? 79.274 29.102 -74.809 1.00 14.43 ? 176  ASP B C   1 
ATOM   5097 O O   . ASP B 1 176 ? 80.156 29.936 -75.041 1.00 14.06 ? 176  ASP B O   1 
ATOM   5098 C CB  . ASP B 1 176 ? 77.323 29.617 -76.279 1.00 14.42 ? 176  ASP B CB  1 
ATOM   5099 C CG  . ASP B 1 176 ? 76.574 29.249 -77.539 1.00 21.55 ? 176  ASP B CG  1 
ATOM   5100 O OD1 . ASP B 1 176 ? 77.116 29.500 -78.633 1.00 25.05 ? 176  ASP B OD1 1 
ATOM   5101 O OD2 . ASP B 1 176 ? 75.485 28.658 -77.438 1.00 15.27 ? 176  ASP B OD2 1 
ATOM   5102 N N   . ALA B 1 177 ? 79.034 28.636 -73.589 1.00 10.65 ? 177  ALA B N   1 
ATOM   5103 C CA  . ALA B 1 177 ? 79.810 29.066 -72.434 1.00 10.24 ? 177  ALA B CA  1 
ATOM   5104 C C   . ALA B 1 177 ? 79.495 28.136 -71.279 1.00 11.22 ? 177  ALA B C   1 
ATOM   5105 O O   . ALA B 1 177 ? 78.455 27.473 -71.258 1.00 11.48 ? 177  ALA B O   1 
ATOM   5106 C CB  . ALA B 1 177 ? 79.508 30.522 -72.034 1.00 11.22 ? 177  ALA B CB  1 
ATOM   5107 N N   . PHE B 1 178 ? 80.394 28.120 -70.304 1.00 11.45 ? 178  PHE B N   1 
ATOM   5108 C CA  . PHE B 1 178 ? 80.226 27.351 -69.081 1.00 11.49 ? 178  PHE B CA  1 
ATOM   5109 C C   . PHE B 1 178 ? 80.282 28.285 -67.878 1.00 9.33  ? 178  PHE B C   1 
ATOM   5110 O O   . PHE B 1 178 ? 81.004 29.283 -67.889 1.00 9.45  ? 178  PHE B O   1 
ATOM   5111 C CB  . PHE B 1 178 ? 81.345 26.325 -68.896 1.00 9.50  ? 178  PHE B CB  1 
ATOM   5112 C CG  . PHE B 1 178 ? 81.282 25.133 -69.808 1.00 15.20 ? 178  PHE B CG  1 
ATOM   5113 C CD1 . PHE B 1 178 ? 80.430 24.062 -69.534 1.00 12.82 ? 178  PHE B CD1 1 
ATOM   5114 C CD2 . PHE B 1 178 ? 82.127 25.055 -70.911 1.00 13.41 ? 178  PHE B CD2 1 
ATOM   5115 C CE1 . PHE B 1 178 ? 80.415 22.931 -70.349 1.00 12.42 ? 178  PHE B CE1 1 
ATOM   5116 C CE2 . PHE B 1 178 ? 82.110 23.935 -71.750 1.00 16.07 ? 178  PHE B CE2 1 
ATOM   5117 C CZ  . PHE B 1 178 ? 81.254 22.877 -71.472 1.00 16.81 ? 178  PHE B CZ  1 
ATOM   5118 N N   . THR B 1 179 ? 79.556 27.937 -66.819 1.00 9.31  ? 179  THR B N   1 
ATOM   5119 C CA  . THR B 1 179 ? 79.907 28.419 -65.489 1.00 8.83  ? 179  THR B CA  1 
ATOM   5120 C C   . THR B 1 179 ? 80.153 27.219 -64.589 1.00 7.35  ? 179  THR B C   1 
ATOM   5121 O O   . THR B 1 179 ? 79.555 26.152 -64.770 1.00 7.40  ? 179  THR B O   1 
ATOM   5122 C CB  . THR B 1 179 ? 78.829 29.337 -64.883 1.00 9.36  ? 179  THR B CB  1 
ATOM   5123 O OG1 . THR B 1 179 ? 77.576 28.652 -64.849 1.00 10.62 ? 179  THR B OG1 1 
ATOM   5124 C CG2 . THR B 1 179 ? 78.668 30.609 -65.724 1.00 9.84  ? 179  THR B CG2 1 
ATOM   5125 N N   . THR B 1 180 ? 81.069 27.387 -63.635 1.00 8.23  ? 180  THR B N   1 
ATOM   5126 C CA  . THR B 1 180 ? 81.393 26.287 -62.727 1.00 9.88  ? 180  THR B CA  1 
ATOM   5127 C C   . THR B 1 180 ? 80.277 26.059 -61.713 1.00 11.10 ? 180  THR B C   1 
ATOM   5128 O O   . THR B 1 180 ? 79.891 24.912 -61.443 1.00 8.56  ? 180  THR B O   1 
ATOM   5129 C CB  . THR B 1 180 ? 82.701 26.571 -61.987 1.00 7.63  ? 180  THR B CB  1 
ATOM   5130 O OG1 . THR B 1 180 ? 82.595 27.828 -61.304 1.00 9.14  ? 180  THR B OG1 1 
ATOM   5131 C CG2 . THR B 1 180 ? 83.881 26.604 -62.957 1.00 7.63  ? 180  THR B CG2 1 
ATOM   5132 N N   . MET B 1 181 ? 79.770 27.136 -61.116 1.00 7.32  ? 181  MET B N   1 
ATOM   5133 C CA  . MET B 1 181 ? 78.829 26.995 -60.014 1.00 8.53  ? 181  MET B CA  1 
ATOM   5134 C C   . MET B 1 181 ? 77.964 28.242 -59.914 1.00 9.72  ? 181  MET B C   1 
ATOM   5135 O O   . MET B 1 181 ? 78.291 29.298 -60.463 1.00 8.67  ? 181  MET B O   1 
ATOM   5136 C CB  . MET B 1 181 ? 79.546 26.740 -58.675 1.00 10.07 ? 181  MET B CB  1 
ATOM   5137 C CG  . MET B 1 181 ? 80.756 27.627 -58.423 1.00 11.05 ? 181  MET B CG  1 
ATOM   5138 S SD  . MET B 1 181 ? 81.772 27.097 -57.005 1.00 13.91 ? 181  MET B SD  1 
ATOM   5139 C CE  . MET B 1 181 ? 82.391 25.509 -57.505 1.00 18.44 ? 181  MET B CE  1 
ATOM   5140 N N   . ASN B 1 182 ? 76.870 28.101 -59.163 1.00 9.07  ? 182  ASN B N   1 
ATOM   5141 C CA  . ASN B 1 182 ? 75.828 29.112 -59.018 1.00 8.25  ? 182  ASN B CA  1 
ATOM   5142 C C   . ASN B 1 182 ? 75.695 29.467 -57.542 1.00 7.47  ? 182  ASN B C   1 
ATOM   5143 O O   . ASN B 1 182 ? 75.361 28.602 -56.721 1.00 8.53  ? 182  ASN B O   1 
ATOM   5144 C CB  . ASN B 1 182 ? 74.495 28.584 -59.584 1.00 8.52  ? 182  ASN B CB  1 
ATOM   5145 C CG  . ASN B 1 182 ? 73.308 29.511 -59.292 1.00 10.91 ? 182  ASN B CG  1 
ATOM   5146 O OD1 . ASN B 1 182 ? 72.937 30.319 -60.134 1.00 11.72 ? 182  ASN B OD1 1 
ATOM   5147 N ND2 . ASN B 1 182 ? 72.688 29.360 -58.119 1.00 7.52  ? 182  ASN B ND2 1 
ATOM   5148 N N   . GLU B 1 183 ? 75.943 30.732 -57.207 1.00 8.71  ? 183  GLU B N   1 
ATOM   5149 C CA  . GLU B 1 183 ? 75.863 31.256 -55.838 1.00 8.83  ? 183  GLU B CA  1 
ATOM   5150 C C   . GLU B 1 183 ? 76.517 30.340 -54.806 1.00 9.52  ? 183  GLU B C   1 
ATOM   5151 O O   . GLU B 1 183 ? 75.870 29.958 -53.819 1.00 9.29  ? 183  GLU B O   1 
ATOM   5152 C CB  . GLU B 1 183 ? 74.399 31.497 -55.444 1.00 6.93  ? 183  GLU B CB  1 
ATOM   5153 C CG  . GLU B 1 183 ? 73.570 32.209 -56.519 1.00 10.44 ? 183  GLU B CG  1 
ATOM   5154 C CD  . GLU B 1 183 ? 72.148 32.541 -56.047 1.00 14.64 ? 183  GLU B CD  1 
ATOM   5155 O OE1 . GLU B 1 183 ? 71.666 31.923 -55.064 1.00 12.36 ? 183  GLU B OE1 1 
ATOM   5156 O OE2 . GLU B 1 183 ? 71.530 33.452 -56.644 1.00 13.80 ? 183  GLU B OE2 1 
ATOM   5157 N N   . PRO B 1 184 ? 77.796 29.991 -54.973 1.00 9.19  ? 184  PRO B N   1 
ATOM   5158 C CA  . PRO B 1 184 ? 78.463 29.196 -53.934 1.00 10.65 ? 184  PRO B CA  1 
ATOM   5159 C C   . PRO B 1 184 ? 78.409 29.857 -52.567 1.00 10.47 ? 184  PRO B C   1 
ATOM   5160 O O   . PRO B 1 184 ? 78.390 29.156 -51.551 1.00 8.74  ? 184  PRO B O   1 
ATOM   5161 C CB  . PRO B 1 184 ? 79.911 29.071 -54.455 1.00 7.92  ? 184  PRO B CB  1 
ATOM   5162 C CG  . PRO B 1 184 ? 80.077 30.280 -55.360 1.00 9.67  ? 184  PRO B CG  1 
ATOM   5163 C CD  . PRO B 1 184 ? 78.733 30.425 -56.027 1.00 9.76  ? 184  PRO B CD  1 
ATOM   5164 N N   . ASN B 1 185 ? 78.349 31.191 -52.520 1.00 8.88  ? 185  ASN B N   1 
ATOM   5165 C CA  . ASN B 1 185 ? 78.264 31.878 -51.243 1.00 8.48  ? 185  ASN B CA  1 
ATOM   5166 C C   . ASN B 1 185 ? 76.949 31.575 -50.541 1.00 9.81  ? 185  ASN B C   1 
ATOM   5167 O O   . ASN B 1 185 ? 76.909 31.514 -49.308 1.00 9.38  ? 185  ASN B O   1 
ATOM   5168 C CB  . ASN B 1 185 ? 78.452 33.384 -51.443 1.00 9.15  ? 185  ASN B CB  1 
ATOM   5169 C CG  . ASN B 1 185 ? 77.462 33.989 -52.437 1.00 9.11  ? 185  ASN B CG  1 
ATOM   5170 O OD1 . ASN B 1 185 ? 77.227 33.452 -53.523 1.00 8.91  ? 185  ASN B OD1 1 
ATOM   5171 N ND2 . ASN B 1 185 ? 76.887 35.126 -52.067 1.00 10.11 ? 185  ASN B ND2 1 
ATOM   5172 N N   . VAL B 1 186 ? 75.880 31.331 -51.300 1.00 8.20  ? 186  VAL B N   1 
ATOM   5173 C CA  . VAL B 1 186 ? 74.605 30.973 -50.681 1.00 8.75  ? 186  VAL B CA  1 
ATOM   5174 C C   . VAL B 1 186 ? 74.640 29.539 -50.152 1.00 8.98  ? 186  VAL B C   1 
ATOM   5175 O O   . VAL B 1 186 ? 74.135 29.255 -49.055 1.00 8.82  ? 186  VAL B O   1 
ATOM   5176 C CB  . VAL B 1 186 ? 73.460 31.197 -51.687 1.00 7.97  ? 186  VAL B CB  1 
ATOM   5177 C CG1 . VAL B 1 186 ? 72.157 30.608 -51.174 1.00 7.78  ? 186  VAL B CG1 1 
ATOM   5178 C CG2 . VAL B 1 186 ? 73.298 32.691 -51.965 1.00 6.16  ? 186  VAL B CG2 1 
ATOM   5179 N N   . VAL B 1 187 ? 75.229 28.610 -50.911 1.00 7.23  ? 187  VAL B N   1 
ATOM   5180 C CA  . VAL B 1 187 ? 75.375 27.236 -50.418 1.00 9.56  ? 187  VAL B CA  1 
ATOM   5181 C C   . VAL B 1 187 ? 76.078 27.227 -49.060 1.00 9.69  ? 187  VAL B C   1 
ATOM   5182 O O   . VAL B 1 187 ? 75.649 26.544 -48.118 1.00 10.01 ? 187  VAL B O   1 
ATOM   5183 C CB  . VAL B 1 187 ? 76.142 26.374 -51.442 1.00 10.70 ? 187  VAL B CB  1 
ATOM   5184 C CG1 . VAL B 1 187 ? 76.381 24.968 -50.887 1.00 9.06  ? 187  VAL B CG1 1 
ATOM   5185 C CG2 . VAL B 1 187 ? 75.394 26.320 -52.764 1.00 11.41 ? 187  VAL B CG2 1 
ATOM   5186 N N   . ALA B 1 188 ? 77.169 27.992 -48.942 1.00 7.92  ? 188  ALA B N   1 
ATOM   5187 C CA  . ALA B 1 188 ? 77.963 27.991 -47.712 1.00 9.88  ? 188  ALA B CA  1 
ATOM   5188 C C   . ALA B 1 188 ? 77.235 28.708 -46.580 1.00 9.84  ? 188  ALA B C   1 
ATOM   5189 O O   . ALA B 1 188 ? 77.140 28.189 -45.460 1.00 9.04  ? 188  ALA B O   1 
ATOM   5190 C CB  . ALA B 1 188 ? 79.328 28.649 -47.961 1.00 6.97  ? 188  ALA B CB  1 
ATOM   5191 N N   . LYS B 1 189 ? 76.732 29.915 -46.846 1.00 8.58  ? 189  LYS B N   1 
ATOM   5192 C CA  . LYS B 1 189 ? 76.133 30.714 -45.780 1.00 8.91  ? 189  LYS B CA  1 
ATOM   5193 C C   . LYS B 1 189 ? 74.847 30.074 -45.274 1.00 9.22  ? 189  LYS B C   1 
ATOM   5194 O O   . LYS B 1 189 ? 74.656 29.905 -44.068 1.00 8.48  ? 189  LYS B O   1 
ATOM   5195 C CB  . LYS B 1 189 ? 75.851 32.136 -46.268 1.00 8.98  ? 189  LYS B CB  1 
ATOM   5196 C CG  . LYS B 1 189 ? 75.253 33.010 -45.157 1.00 18.83 ? 189  LYS B CG  1 
ATOM   5197 C CD  . LYS B 1 189 ? 75.244 34.489 -45.523 1.00 28.50 ? 189  LYS B CD  1 
ATOM   5198 C CE  . LYS B 1 189 ? 74.412 35.308 -44.530 1.00 32.56 ? 189  LYS B CE  1 
ATOM   5199 N NZ  . LYS B 1 189 ? 73.802 36.533 -45.151 1.00 41.74 ? 189  LYS B NZ  1 
ATOM   5200 N N   . LEU B 1 190 ? 73.949 29.695 -46.183 1.00 7.93  ? 190  LEU B N   1 
ATOM   5201 C CA  . LEU B 1 190 ? 72.683 29.154 -45.717 1.00 8.52  ? 190  LEU B CA  1 
ATOM   5202 C C   . LEU B 1 190 ? 72.836 27.722 -45.211 1.00 9.09  ? 190  LEU B C   1 
ATOM   5203 O O   . LEU B 1 190 ? 72.093 27.309 -44.315 1.00 9.87  ? 190  LEU B O   1 
ATOM   5204 C CB  . LEU B 1 190 ? 71.631 29.239 -46.829 1.00 7.85  ? 190  LEU B CB  1 
ATOM   5205 C CG  . LEU B 1 190 ? 71.297 30.630 -47.382 1.00 9.78  ? 190  LEU B CG  1 
ATOM   5206 C CD1 . LEU B 1 190 ? 70.070 30.558 -48.296 1.00 9.36  ? 190  LEU B CD1 1 
ATOM   5207 C CD2 . LEU B 1 190 ? 71.076 31.639 -46.256 1.00 11.51 ? 190  LEU B CD2 1 
ATOM   5208 N N   . GLY B 1 191 ? 73.807 26.967 -45.733 1.00 7.34  ? 191  GLY B N   1 
ATOM   5209 C CA  . GLY B 1 191 ? 74.008 25.608 -45.258 1.00 6.11  ? 191  GLY B CA  1 
ATOM   5210 C C   . GLY B 1 191 ? 74.573 25.522 -43.851 1.00 8.79  ? 191  GLY B C   1 
ATOM   5211 O O   . GLY B 1 191 ? 74.224 24.605 -43.096 1.00 8.02  ? 191  GLY B O   1 
ATOM   5212 N N   . TYR B 1 192 ? 75.445 26.469 -43.473 1.00 8.28  ? 192  TYR B N   1 
ATOM   5213 C CA  . TYR B 1 192 ? 76.220 26.357 -42.240 1.00 8.12  ? 192  TYR B CA  1 
ATOM   5214 C C   . TYR B 1 192 ? 76.112 27.571 -41.325 1.00 9.53  ? 192  TYR B C   1 
ATOM   5215 O O   . TYR B 1 192 ? 76.704 27.556 -40.240 1.00 9.74  ? 192  TYR B O   1 
ATOM   5216 C CB  . TYR B 1 192 ? 77.708 26.088 -42.566 1.00 7.41  ? 192  TYR B CB  1 
ATOM   5217 C CG  . TYR B 1 192 ? 77.843 24.867 -43.448 1.00 10.24 ? 192  TYR B CG  1 
ATOM   5218 C CD1 . TYR B 1 192 ? 77.878 23.591 -42.893 1.00 8.86  ? 192  TYR B CD1 1 
ATOM   5219 C CD2 . TYR B 1 192 ? 77.854 24.983 -44.833 1.00 8.58  ? 192  TYR B CD2 1 
ATOM   5220 C CE1 . TYR B 1 192 ? 77.950 22.461 -43.693 1.00 9.29  ? 192  TYR B CE1 1 
ATOM   5221 C CE2 . TYR B 1 192 ? 77.926 23.856 -45.646 1.00 9.66  ? 192  TYR B CE2 1 
ATOM   5222 C CZ  . TYR B 1 192 ? 77.971 22.595 -45.063 1.00 9.01  ? 192  TYR B CZ  1 
ATOM   5223 O OH  . TYR B 1 192 ? 78.040 21.455 -45.851 1.00 10.82 ? 192  TYR B OH  1 
ATOM   5224 N N   . PHE B 1 193 ? 75.378 28.611 -41.723 1.00 7.61  ? 193  PHE B N   1 
ATOM   5225 C CA  . PHE B 1 193 ? 75.262 29.827 -40.935 1.00 8.77  ? 193  PHE B CA  1 
ATOM   5226 C C   . PHE B 1 193 ? 73.980 30.550 -41.321 1.00 8.77  ? 193  PHE B C   1 
ATOM   5227 O O   . PHE B 1 193 ? 73.954 31.780 -41.398 1.00 9.76  ? 193  PHE B O   1 
ATOM   5228 C CB  . PHE B 1 193 ? 76.473 30.744 -41.146 1.00 7.89  ? 193  PHE B CB  1 
ATOM   5229 C CG  . PHE B 1 193 ? 76.796 31.597 -39.950 1.00 10.65 ? 193  PHE B CG  1 
ATOM   5230 C CD1 . PHE B 1 193 ? 77.279 31.017 -38.784 1.00 8.52  ? 193  PHE B CD1 1 
ATOM   5231 C CD2 . PHE B 1 193 ? 76.595 32.976 -39.977 1.00 9.88  ? 193  PHE B CD2 1 
ATOM   5232 C CE1 . PHE B 1 193 ? 77.580 31.799 -37.662 1.00 10.04 ? 193  PHE B CE1 1 
ATOM   5233 C CE2 . PHE B 1 193 ? 76.876 33.763 -38.853 1.00 11.04 ? 193  PHE B CE2 1 
ATOM   5234 C CZ  . PHE B 1 193 ? 77.364 33.167 -37.693 1.00 9.83  ? 193  PHE B CZ  1 
ATOM   5235 N N   . GLY B 1 194 ? 72.926 29.786 -41.585 1.00 9.79  ? 194  GLY B N   1 
ATOM   5236 C CA  . GLY B 1 194 ? 71.628 30.324 -41.950 1.00 10.02 ? 194  GLY B CA  1 
ATOM   5237 C C   . GLY B 1 194 ? 70.553 29.382 -41.462 1.00 11.34 ? 194  GLY B C   1 
ATOM   5238 O O   . GLY B 1 194 ? 69.775 28.837 -42.252 1.00 10.92 ? 194  GLY B O   1 
ATOM   5239 N N   . ARG B 1 195 ? 70.519 29.191 -40.141 1.00 10.83 ? 195  ARG B N   1 
ATOM   5240 C CA  . ARG B 1 195 ? 69.684 28.166 -39.518 1.00 13.57 ? 195  ARG B CA  1 
ATOM   5241 C C   . ARG B 1 195 ? 68.205 28.342 -39.841 1.00 14.55 ? 195  ARG B C   1 
ATOM   5242 O O   . ARG B 1 195 ? 67.486 27.349 -39.984 1.00 13.72 ? 195  ARG B O   1 
ATOM   5243 C CB  . ARG B 1 195 ? 69.936 28.187 -38.006 1.00 14.08 ? 195  ARG B CB  1 
ATOM   5244 C CG  . ARG B 1 195 ? 69.008 27.372 -37.126 1.00 19.37 ? 195  ARG B CG  1 
ATOM   5245 C CD  . ARG B 1 195 ? 68.974 25.889 -37.496 1.00 24.10 ? 195  ARG B CD  1 
ATOM   5246 N NE  . ARG B 1 195 ? 70.238 25.165 -37.368 1.00 20.02 ? 195  ARG B NE  1 
ATOM   5247 C CZ  . ARG B 1 195 ? 70.767 24.712 -36.239 1.00 22.03 ? 195  ARG B CZ  1 
ATOM   5248 N NH1 . ARG B 1 195 ? 70.283 25.054 -35.056 1.00 25.81 ? 195  ARG B NH1 1 
ATOM   5249 N NH2 . ARG B 1 195 ? 71.802 23.878 -36.299 1.00 15.83 ? 195  ARG B NH2 1 
ATOM   5250 N N   . LEU B 1 196 ? 67.728 29.578 -39.975 1.00 10.60 ? 196  LEU B N   1 
ATOM   5251 C CA  . LEU B 1 196 ? 66.319 29.776 -40.301 1.00 12.01 ? 196  LEU B CA  1 
ATOM   5252 C C   . LEU B 1 196 ? 66.018 29.672 -41.798 1.00 14.10 ? 196  LEU B C   1 
ATOM   5253 O O   . LEU B 1 196 ? 64.856 29.803 -42.186 1.00 12.25 ? 196  LEU B O   1 
ATOM   5254 C CB  . LEU B 1 196 ? 65.853 31.137 -39.774 1.00 13.69 ? 196  LEU B CB  1 
ATOM   5255 C CG  . LEU B 1 196 ? 66.055 31.316 -38.253 1.00 13.78 ? 196  LEU B CG  1 
ATOM   5256 C CD1 . LEU B 1 196 ? 65.526 32.678 -37.806 1.00 14.91 ? 196  LEU B CD1 1 
ATOM   5257 C CD2 . LEU B 1 196 ? 65.362 30.198 -37.496 1.00 14.30 ? 196  LEU B CD2 1 
ATOM   5258 N N   . SER B 1 197 ? 67.016 29.436 -42.651 1.00 9.94  ? 197  SER B N   1 
ATOM   5259 C CA  . SER B 1 197 ? 66.786 29.468 -44.090 1.00 11.12 ? 197  SER B CA  1 
ATOM   5260 C C   . SER B 1 197 ? 66.292 28.143 -44.661 1.00 12.55 ? 197  SER B C   1 
ATOM   5261 O O   . SER B 1 197 ? 65.778 28.123 -45.788 1.00 12.44 ? 197  SER B O   1 
ATOM   5262 C CB  . SER B 1 197 ? 68.077 29.869 -44.815 1.00 11.35 ? 197  SER B CB  1 
ATOM   5263 O OG  . SER B 1 197 ? 68.988 28.771 -44.871 1.00 12.07 ? 197  SER B OG  1 
ATOM   5264 N N   . GLY B 1 198 ? 66.482 27.030 -43.955 1.00 10.36 ? 198  GLY B N   1 
ATOM   5265 C CA  . GLY B 1 198 ? 66.032 25.744 -44.465 1.00 11.72 ? 198  GLY B CA  1 
ATOM   5266 C C   . GLY B 1 198 ? 66.953 25.064 -45.464 1.00 11.67 ? 198  GLY B C   1 
ATOM   5267 O O   . GLY B 1 198 ? 66.549 24.068 -46.078 1.00 11.45 ? 198  GLY B O   1 
ATOM   5268 N N   . PHE B 1 199 ? 68.161 25.552 -45.645 1.00 8.75  ? 199  PHE B N   1 
ATOM   5269 C CA  . PHE B 1 199 ? 69.097 24.940 -46.582 1.00 8.68  ? 199  PHE B CA  1 
ATOM   5270 C C   . PHE B 1 199 ? 69.920 23.852 -45.887 1.00 11.00 ? 199  PHE B C   1 
ATOM   5271 O O   . PHE B 1 199 ? 70.271 23.999 -44.710 1.00 8.92  ? 199  PHE B O   1 
ATOM   5272 C CB  . PHE B 1 199 ? 70.031 25.995 -47.166 1.00 7.88  ? 199  PHE B CB  1 
ATOM   5273 C CG  . PHE B 1 199 ? 69.527 26.599 -48.463 1.00 11.01 ? 199  PHE B CG  1 
ATOM   5274 C CD1 . PHE B 1 199 ? 68.263 27.172 -48.539 1.00 9.42  ? 199  PHE B CD1 1 
ATOM   5275 C CD2 . PHE B 1 199 ? 70.323 26.599 -49.600 1.00 8.07  ? 199  PHE B CD2 1 
ATOM   5276 C CE1 . PHE B 1 199 ? 67.807 27.727 -49.730 1.00 10.28 ? 199  PHE B CE1 1 
ATOM   5277 C CE2 . PHE B 1 199 ? 69.871 27.159 -50.785 1.00 10.53 ? 199  PHE B CE2 1 
ATOM   5278 C CZ  . PHE B 1 199 ? 68.610 27.716 -50.849 1.00 9.43  ? 199  PHE B CZ  1 
ATOM   5279 N N   . PRO B 1 200 ? 70.251 22.764 -46.581 1.00 9.17  ? 200  PRO B N   1 
ATOM   5280 C CA  . PRO B 1 200 ? 70.997 21.659 -45.947 1.00 10.27 ? 200  PRO B CA  1 
ATOM   5281 C C   . PRO B 1 200 ? 72.473 21.995 -45.807 1.00 8.79  ? 200  PRO B C   1 
ATOM   5282 O O   . PRO B 1 200 ? 73.036 22.746 -46.625 1.00 8.75  ? 200  PRO B O   1 
ATOM   5283 C CB  . PRO B 1 200 ? 70.784 20.495 -46.931 1.00 9.23  ? 200  PRO B CB  1 
ATOM   5284 C CG  . PRO B 1 200 ? 70.705 21.205 -48.282 1.00 10.17 ? 200  PRO B CG  1 
ATOM   5285 C CD  . PRO B 1 200 ? 70.005 22.518 -48.014 1.00 8.73  ? 200  PRO B CD  1 
ATOM   5286 N N   . PRO B 1 201 ? 73.153 21.451 -44.777 1.00 9.45  ? 201  PRO B N   1 
ATOM   5287 C CA  . PRO B 1 201 ? 72.581 20.588 -43.735 1.00 9.89  ? 201  PRO B CA  1 
ATOM   5288 C C   . PRO B 1 201 ? 72.040 21.357 -42.528 1.00 9.11  ? 201  PRO B C   1 
ATOM   5289 O O   . PRO B 1 201 ? 71.740 20.739 -41.516 1.00 9.31  ? 201  PRO B O   1 
ATOM   5290 C CB  . PRO B 1 201 ? 73.767 19.707 -43.336 1.00 11.22 ? 201  PRO B CB  1 
ATOM   5291 C CG  . PRO B 1 201 ? 74.942 20.625 -43.472 1.00 7.55  ? 201  PRO B CG  1 
ATOM   5292 C CD  . PRO B 1 201 ? 74.623 21.508 -44.678 1.00 7.62  ? 201  PRO B CD  1 
ATOM   5293 N N   . SER B 1 202 ? 71.909 22.678 -42.646 1.00 8.26  ? 202  SER B N   1 
ATOM   5294 C CA  . SER B 1 202 ? 71.398 23.525 -41.564 1.00 10.66 ? 202  SER B CA  1 
ATOM   5295 C C   . SER B 1 202 ? 72.212 23.361 -40.278 1.00 10.63 ? 202  SER B C   1 
ATOM   5296 O O   . SER B 1 202 ? 71.670 23.221 -39.174 1.00 12.26 ? 202  SER B O   1 
ATOM   5297 C CB  . SER B 1 202 ? 69.916 23.262 -41.297 1.00 15.51 ? 202  SER B CB  1 
ATOM   5298 O OG  . SER B 1 202 ? 69.312 24.419 -40.741 1.00 17.08 ? 202  SER B OG  1 
ATOM   5299 N N   . LEU B 1 203 ? 73.529 23.393 -40.423 1.00 10.00 ? 203  LEU B N   1 
ATOM   5300 C CA  . LEU B 1 203 ? 74.362 23.553 -39.251 1.00 9.84  ? 203  LEU B CA  1 
ATOM   5301 C C   . LEU B 1 203 ? 74.445 25.034 -38.898 1.00 13.27 ? 203  LEU B C   1 
ATOM   5302 O O   . LEU B 1 203 ? 74.022 25.915 -39.664 1.00 8.16  ? 203  LEU B O   1 
ATOM   5303 C CB  . LEU B 1 203 ? 75.758 22.961 -39.489 1.00 11.63 ? 203  LEU B CB  1 
ATOM   5304 C CG  . LEU B 1 203 ? 75.772 21.463 -39.852 1.00 15.30 ? 203  LEU B CG  1 
ATOM   5305 C CD1 . LEU B 1 203 ? 77.196 20.907 -39.915 1.00 11.65 ? 203  LEU B CD1 1 
ATOM   5306 C CD2 . LEU B 1 203 ? 74.924 20.646 -38.891 1.00 17.99 ? 203  LEU B CD2 1 
ATOM   5307 N N   . LEU B 1 204 ? 74.989 25.309 -37.716 1.00 10.32 ? 204  LEU B N   1 
ATOM   5308 C CA  . LEU B 1 204 ? 75.182 26.687 -37.262 1.00 11.07 ? 204  LEU B CA  1 
ATOM   5309 C C   . LEU B 1 204 ? 76.582 26.735 -36.656 1.00 13.12 ? 204  LEU B C   1 
ATOM   5310 O O   . LEU B 1 204 ? 76.766 26.477 -35.460 1.00 9.75  ? 204  LEU B O   1 
ATOM   5311 C CB  . LEU B 1 204 ? 74.107 27.102 -36.269 1.00 10.39 ? 204  LEU B CB  1 
ATOM   5312 C CG  . LEU B 1 204 ? 73.851 28.599 -36.105 1.00 12.93 ? 204  LEU B CG  1 
ATOM   5313 C CD1 . LEU B 1 204 ? 72.634 28.833 -35.209 1.00 14.42 ? 204  LEU B CD1 1 
ATOM   5314 C CD2 . LEU B 1 204 ? 75.059 29.344 -35.555 1.00 11.15 ? 204  LEU B CD2 1 
ATOM   5315 N N   . ASN B 1 205 ? 77.561 27.070 -37.494 1.00 9.51  ? 205  ASN B N   1 
ATOM   5316 C CA  . ASN B 1 205 ? 78.963 26.992 -37.095 1.00 11.00 ? 205  ASN B CA  1 
ATOM   5317 C C   . ASN B 1 205 ? 79.760 27.845 -38.073 1.00 10.29 ? 205  ASN B C   1 
ATOM   5318 O O   . ASN B 1 205 ? 79.929 27.465 -39.240 1.00 7.60  ? 205  ASN B O   1 
ATOM   5319 C CB  . ASN B 1 205 ? 79.440 25.541 -37.094 1.00 12.51 ? 205  ASN B CB  1 
ATOM   5320 C CG  . ASN B 1 205 ? 80.819 25.383 -36.493 1.00 14.65 ? 205  ASN B CG  1 
ATOM   5321 O OD1 . ASN B 1 205 ? 81.688 26.251 -36.647 1.00 15.43 ? 205  ASN B OD1 1 
ATOM   5322 N ND2 . ASN B 1 205 ? 81.023 24.283 -35.785 1.00 14.78 ? 205  ASN B ND2 1 
ATOM   5323 N N   . ILE B 1 206 ? 80.243 28.987 -37.597 1.00 8.19  ? 206  ILE B N   1 
ATOM   5324 C CA  . ILE B 1 206 ? 80.929 29.931 -38.478 1.00 9.73  ? 206  ILE B CA  1 
ATOM   5325 C C   . ILE B 1 206 ? 82.181 29.308 -39.089 1.00 9.84  ? 206  ILE B C   1 
ATOM   5326 O O   . ILE B 1 206 ? 82.595 29.688 -40.194 1.00 9.76  ? 206  ILE B O   1 
ATOM   5327 C CB  . ILE B 1 206 ? 81.266 31.224 -37.708 1.00 8.27  ? 206  ILE B CB  1 
ATOM   5328 C CG1 . ILE B 1 206 ? 81.755 32.311 -38.673 1.00 12.68 ? 206  ILE B CG1 1 
ATOM   5329 C CG2 . ILE B 1 206 ? 82.319 30.962 -36.631 1.00 12.48 ? 206  ILE B CG2 1 
ATOM   5330 C CD1 . ILE B 1 206 ? 81.794 33.701 -38.055 1.00 14.44 ? 206  ILE B CD1 1 
ATOM   5331 N N   . ASP B 1 207 ? 82.804 28.347 -38.393 1.00 9.13  ? 207  ASP B N   1 
ATOM   5332 C CA  . ASP B 1 207 ? 84.007 27.713 -38.933 1.00 12.02 ? 207  ASP B CA  1 
ATOM   5333 C C   . ASP B 1 207 ? 83.680 26.791 -40.104 1.00 9.84  ? 207  ASP B C   1 
ATOM   5334 O O   . ASP B 1 207 ? 84.519 26.597 -40.989 1.00 11.37 ? 207  ASP B O   1 
ATOM   5335 C CB  . ASP B 1 207 ? 84.732 26.915 -37.846 1.00 12.16 ? 207  ASP B CB  1 
ATOM   5336 C CG  . ASP B 1 207 ? 85.346 27.798 -36.765 1.00 18.29 ? 207  ASP B CG  1 
ATOM   5337 O OD1 . ASP B 1 207 ? 85.588 28.993 -37.009 1.00 16.04 ? 207  ASP B OD1 1 
ATOM   5338 O OD2 . ASP B 1 207 ? 85.566 27.296 -35.652 1.00 23.17 ? 207  ASP B OD2 1 
ATOM   5339 N N   . LEU B 1 208 ? 82.490 26.183 -40.112 1.00 10.62 ? 208  LEU B N   1 
ATOM   5340 C CA  . LEU B 1 208 ? 82.103 25.340 -41.241 1.00 10.59 ? 208  LEU B CA  1 
ATOM   5341 C C   . LEU B 1 208 ? 81.592 26.176 -42.403 1.00 11.64 ? 208  LEU B C   1 
ATOM   5342 O O   . LEU B 1 208 ? 81.783 25.798 -43.561 1.00 9.81  ? 208  LEU B O   1 
ATOM   5343 C CB  . LEU B 1 208 ? 81.049 24.307 -40.805 1.00 11.16 ? 208  LEU B CB  1 
ATOM   5344 C CG  . LEU B 1 208 ? 81.458 23.426 -39.609 1.00 10.64 ? 208  LEU B CG  1 
ATOM   5345 C CD1 . LEU B 1 208 ? 80.417 22.362 -39.302 1.00 13.34 ? 208  LEU B CD1 1 
ATOM   5346 C CD2 . LEU B 1 208 ? 82.835 22.783 -39.824 1.00 15.26 ? 208  LEU B CD2 1 
ATOM   5347 N N   . TYR B 1 209 ? 80.941 27.305 -42.108 1.00 9.61  ? 209  TYR B N   1 
ATOM   5348 C CA  . TYR B 1 209 ? 80.685 28.327 -43.116 1.00 9.97  ? 209  TYR B CA  1 
ATOM   5349 C C   . TYR B 1 209 ? 81.981 28.709 -43.835 1.00 12.27 ? 209  TYR B C   1 
ATOM   5350 O O   . TYR B 1 209 ? 82.064 28.676 -45.072 1.00 11.63 ? 209  TYR B O   1 
ATOM   5351 C CB  . TYR B 1 209 ? 80.052 29.533 -42.411 1.00 8.05  ? 209  TYR B CB  1 
ATOM   5352 C CG  . TYR B 1 209 ? 79.727 30.771 -43.230 1.00 12.91 ? 209  TYR B CG  1 
ATOM   5353 C CD1 . TYR B 1 209 ? 79.749 30.787 -44.629 1.00 11.47 ? 209  TYR B CD1 1 
ATOM   5354 C CD2 . TYR B 1 209 ? 79.463 31.958 -42.574 1.00 13.73 ? 209  TYR B CD2 1 
ATOM   5355 C CE1 . TYR B 1 209 ? 79.470 31.968 -45.332 1.00 12.12 ? 209  TYR B CE1 1 
ATOM   5356 C CE2 . TYR B 1 209 ? 79.177 33.118 -43.253 1.00 18.51 ? 209  TYR B CE2 1 
ATOM   5357 C CZ  . TYR B 1 209 ? 79.185 33.129 -44.624 1.00 15.84 ? 209  TYR B CZ  1 
ATOM   5358 O OH  . TYR B 1 209 ? 78.894 34.325 -45.242 1.00 17.39 ? 209  TYR B OH  1 
ATOM   5359 N N   . GLU B 1 210 ? 83.015 29.057 -43.064 1.00 11.06 ? 210  GLU B N   1 
ATOM   5360 C CA  . GLU B 1 210 ? 84.308 29.419 -43.645 1.00 10.85 ? 210  GLU B CA  1 
ATOM   5361 C C   . GLU B 1 210 ? 84.876 28.283 -44.491 1.00 10.46 ? 210  GLU B C   1 
ATOM   5362 O O   . GLU B 1 210 ? 85.381 28.502 -45.598 1.00 11.58 ? 210  GLU B O   1 
ATOM   5363 C CB  . GLU B 1 210 ? 85.288 29.758 -42.526 1.00 10.42 ? 210  GLU B CB  1 
ATOM   5364 C CG  . GLU B 1 210 ? 86.654 30.209 -43.010 1.00 15.85 ? 210  GLU B CG  1 
ATOM   5365 C CD  . GLU B 1 210 ? 87.523 30.664 -41.855 1.00 23.93 ? 210  GLU B CD  1 
ATOM   5366 O OE1 . GLU B 1 210 ? 88.507 29.970 -41.547 1.00 24.18 ? 210  GLU B OE1 1 
ATOM   5367 O OE2 . GLU B 1 210 ? 87.184 31.681 -41.212 1.00 27.02 ? 210  GLU B OE2 1 
ATOM   5368 N N   . LYS B 1 211 ? 84.822 27.059 -43.965 1.00 10.32 ? 211  LYS B N   1 
ATOM   5369 C CA  . LYS B 1 211 ? 85.375 25.911 -44.677 1.00 11.85 ? 211  LYS B CA  1 
ATOM   5370 C C   . LYS B 1 211 ? 84.629 25.641 -45.989 1.00 13.26 ? 211  LYS B C   1 
ATOM   5371 O O   . LYS B 1 211 ? 85.248 25.306 -47.007 1.00 8.28  ? 211  LYS B O   1 
ATOM   5372 C CB  . LYS B 1 211 ? 85.333 24.689 -43.751 1.00 11.08 ? 211  LYS B CB  1 
ATOM   5373 C CG  . LYS B 1 211 ? 85.640 23.336 -44.412 1.00 18.22 ? 211  LYS B CG  1 
ATOM   5374 C CD  . LYS B 1 211 ? 87.048 23.276 -44.973 1.00 24.26 ? 211  LYS B CD  1 
ATOM   5375 C CE  . LYS B 1 211 ? 87.787 22.036 -44.442 1.00 40.10 ? 211  LYS B CE  1 
ATOM   5376 N NZ  . LYS B 1 211 ? 89.288 22.147 -44.475 1.00 42.66 ? 211  LYS B NZ  1 
ATOM   5377 N N   . ALA B 1 212 ? 83.299 25.764 -45.982 1.00 10.46 ? 212  ALA B N   1 
ATOM   5378 C CA  . ALA B 1 212 ? 82.520 25.546 -47.203 1.00 12.12 ? 212  ALA B CA  1 
ATOM   5379 C C   . ALA B 1 212 ? 82.803 26.619 -48.249 1.00 9.86  ? 212  ALA B C   1 
ATOM   5380 O O   . ALA B 1 212 ? 82.835 26.323 -49.449 1.00 10.91 ? 212  ALA B O   1 
ATOM   5381 C CB  . ALA B 1 212 ? 81.024 25.502 -46.877 1.00 9.46  ? 212  ALA B CB  1 
ATOM   5382 N N   . LEU B 1 213 ? 83.001 27.870 -47.823 1.00 9.49  ? 213  LEU B N   1 
ATOM   5383 C CA  . LEU B 1 213 ? 83.415 28.912 -48.764 1.00 11.24 ? 213  LEU B CA  1 
ATOM   5384 C C   . LEU B 1 213 ? 84.758 28.566 -49.398 1.00 9.27  ? 213  LEU B C   1 
ATOM   5385 O O   . LEU B 1 213 ? 84.913 28.607 -50.625 1.00 10.43 ? 213  LEU B O   1 
ATOM   5386 C CB  . LEU B 1 213 ? 83.534 30.257 -48.052 1.00 11.44 ? 213  LEU B CB  1 
ATOM   5387 C CG  . LEU B 1 213 ? 82.290 31.044 -47.657 1.00 12.82 ? 213  LEU B CG  1 
ATOM   5388 C CD1 . LEU B 1 213 ? 82.730 32.238 -46.805 1.00 12.64 ? 213  LEU B CD1 1 
ATOM   5389 C CD2 . LEU B 1 213 ? 81.516 31.491 -48.882 1.00 11.17 ? 213  LEU B CD2 1 
ATOM   5390 N N   . ASP B 1 214 ? 85.745 28.243 -48.561 1.00 9.68  ? 214  ASP B N   1 
ATOM   5391 C CA  . ASP B 1 214 ? 87.105 28.001 -49.036 1.00 10.88 ? 214  ASP B CA  1 
ATOM   5392 C C   . ASP B 1 214 ? 87.172 26.803 -49.970 1.00 10.25 ? 214  ASP B C   1 
ATOM   5393 O O   . ASP B 1 214 ? 87.906 26.827 -50.963 1.00 10.85 ? 214  ASP B O   1 
ATOM   5394 C CB  . ASP B 1 214 ? 88.044 27.780 -47.847 1.00 11.66 ? 214  ASP B CB  1 
ATOM   5395 C CG  . ASP B 1 214 ? 88.306 29.052 -47.057 1.00 18.10 ? 214  ASP B CG  1 
ATOM   5396 O OD1 . ASP B 1 214 ? 87.851 30.143 -47.475 1.00 14.33 ? 214  ASP B OD1 1 
ATOM   5397 O OD2 . ASP B 1 214 ? 88.943 28.949 -45.992 1.00 19.88 ? 214  ASP B OD2 1 
ATOM   5398 N N   . ASN B 1 215 ? 86.436 25.731 -49.658 1.00 9.36  ? 215  ASN B N   1 
ATOM   5399 C CA  . ASN B 1 215 ? 86.489 24.554 -50.520 1.00 10.85 ? 215  ASN B CA  1 
ATOM   5400 C C   . ASN B 1 215 ? 85.809 24.814 -51.860 1.00 9.27  ? 215  ASN B C   1 
ATOM   5401 O O   . ASN B 1 215 ? 86.264 24.317 -52.896 1.00 10.55 ? 215  ASN B O   1 
ATOM   5402 C CB  . ASN B 1 215 ? 85.878 23.338 -49.817 1.00 9.32  ? 215  ASN B CB  1 
ATOM   5403 C CG  . ASN B 1 215 ? 86.913 22.558 -49.007 1.00 15.27 ? 215  ASN B CG  1 
ATOM   5404 O OD1 . ASN B 1 215 ? 88.102 22.840 -49.098 1.00 13.81 ? 215  ASN B OD1 1 
ATOM   5405 N ND2 . ASN B 1 215 ? 86.463 21.556 -48.240 1.00 11.13 ? 215  ASN B ND2 1 
ATOM   5406 N N   . GLN B 1 216 ? 84.736 25.606 -51.874 1.00 7.85  ? 216  GLN B N   1 
ATOM   5407 C CA  . GLN B 1 216 ? 84.133 25.964 -53.153 1.00 8.56  ? 216  GLN B CA  1 
ATOM   5408 C C   . GLN B 1 216 ? 85.043 26.882 -53.966 1.00 9.45  ? 216  GLN B C   1 
ATOM   5409 O O   . GLN B 1 216 ? 85.040 26.821 -55.200 1.00 8.60  ? 216  GLN B O   1 
ATOM   5410 C CB  . GLN B 1 216 ? 82.766 26.607 -52.927 1.00 9.43  ? 216  GLN B CB  1 
ATOM   5411 C CG  . GLN B 1 216 ? 81.693 25.579 -52.604 1.00 9.22  ? 216  GLN B CG  1 
ATOM   5412 C CD  . GLN B 1 216 ? 80.345 26.204 -52.330 1.00 10.64 ? 216  GLN B CD  1 
ATOM   5413 O OE1 . GLN B 1 216 ? 79.438 26.112 -53.154 1.00 9.58  ? 216  GLN B OE1 1 
ATOM   5414 N NE2 . GLN B 1 216 ? 80.200 26.831 -51.170 1.00 10.28 ? 216  GLN B NE2 1 
ATOM   5415 N N   . ILE B 1 217 ? 85.830 27.726 -53.299 1.00 9.61  ? 217  ILE B N   1 
ATOM   5416 C CA  . ILE B 1 217 ? 86.818 28.548 -54.003 1.00 9.97  ? 217  ILE B CA  1 
ATOM   5417 C C   . ILE B 1 217 ? 87.868 27.660 -54.659 1.00 10.88 ? 217  ILE B C   1 
ATOM   5418 O O   . ILE B 1 217 ? 88.161 27.787 -55.860 1.00 8.42  ? 217  ILE B O   1 
ATOM   5419 C CB  . ILE B 1 217 ? 87.464 29.547 -53.027 1.00 11.13 ? 217  ILE B CB  1 
ATOM   5420 C CG1 . ILE B 1 217 ? 86.457 30.627 -52.618 1.00 9.94  ? 217  ILE B CG1 1 
ATOM   5421 C CG2 . ILE B 1 217 ? 88.738 30.176 -53.633 1.00 8.91  ? 217  ILE B CG2 1 
ATOM   5422 C CD1 . ILE B 1 217 ? 86.918 31.498 -51.458 1.00 12.71 ? 217  ILE B CD1 1 
ATOM   5423 N N   . LEU B 1 218 ? 88.458 26.755 -53.868 1.00 10.58 ? 218  LEU B N   1 
ATOM   5424 C CA  . LEU B 1 218 ? 89.399 25.773 -54.398 1.00 11.61 ? 218  LEU B CA  1 
ATOM   5425 C C   . LEU B 1 218 ? 88.786 25.003 -55.558 1.00 12.68 ? 218  LEU B C   1 
ATOM   5426 O O   . LEU B 1 218 ? 89.419 24.828 -56.606 1.00 10.34 ? 218  LEU B O   1 
ATOM   5427 C CB  . LEU B 1 218 ? 89.826 24.803 -53.289 1.00 9.56  ? 218  LEU B CB  1 
ATOM   5428 C CG  . LEU B 1 218 ? 90.882 25.302 -52.295 1.00 18.94 ? 218  LEU B CG  1 
ATOM   5429 C CD1 . LEU B 1 218 ? 91.015 24.333 -51.109 1.00 18.52 ? 218  LEU B CD1 1 
ATOM   5430 C CD2 . LEU B 1 218 ? 92.232 25.514 -52.992 1.00 16.36 ? 218  LEU B CD2 1 
ATOM   5431 N N   . ALA B 1 219 ? 87.536 24.549 -55.394 1.00 7.82  ? 219  ALA B N   1 
ATOM   5432 C CA  . ALA B 1 219 ? 86.892 23.762 -56.444 1.00 10.10 ? 219  ALA B CA  1 
ATOM   5433 C C   . ALA B 1 219 ? 86.711 24.578 -57.714 1.00 10.07 ? 219  ALA B C   1 
ATOM   5434 O O   . ALA B 1 219 ? 86.926 24.071 -58.823 1.00 10.11 ? 219  ALA B O   1 
ATOM   5435 C CB  . ALA B 1 219 ? 85.540 23.232 -55.968 1.00 9.57  ? 219  ALA B CB  1 
ATOM   5436 N N   . HIS B 1 220 ? 86.313 25.845 -57.581 1.00 8.40  ? 220  HIS B N   1 
ATOM   5437 C CA  . HIS B 1 220 ? 86.159 26.658 -58.778 1.00 10.54 ? 220  HIS B CA  1 
ATOM   5438 C C   . HIS B 1 220 ? 87.494 26.868 -59.482 1.00 10.94 ? 220  HIS B C   1 
ATOM   5439 O O   . HIS B 1 220 ? 87.588 26.736 -60.708 1.00 10.06 ? 220  HIS B O   1 
ATOM   5440 C CB  . HIS B 1 220 ? 85.571 28.034 -58.481 1.00 8.52  ? 220  HIS B CB  1 
ATOM   5441 C CG  . HIS B 1 220 ? 85.756 28.953 -59.639 1.00 9.26  ? 220  HIS B CG  1 
ATOM   5442 N ND1 . HIS B 1 220 ? 84.912 28.939 -60.729 1.00 8.44  ? 220  HIS B ND1 1 
ATOM   5443 C CD2 . HIS B 1 220 ? 86.757 29.811 -59.947 1.00 9.12  ? 220  HIS B CD2 1 
ATOM   5444 C CE1 . HIS B 1 220 ? 85.363 29.785 -61.639 1.00 9.91  ? 220  HIS B CE1 1 
ATOM   5445 N NE2 . HIS B 1 220 ? 86.488 30.318 -61.193 1.00 9.32  ? 220  HIS B NE2 1 
ATOM   5446 N N   . ASN B 1 221 ? 88.514 27.293 -58.733 1.00 9.29  ? 221  ASN B N   1 
ATOM   5447 C CA  . ASN B 1 221 ? 89.793 27.640 -59.346 1.00 11.43 ? 221  ASN B CA  1 
ATOM   5448 C C   . ASN B 1 221 ? 90.415 26.430 -60.038 1.00 13.45 ? 221  ASN B C   1 
ATOM   5449 O O   . ASN B 1 221 ? 90.934 26.539 -61.161 1.00 11.06 ? 221  ASN B O   1 
ATOM   5450 C CB  . ASN B 1 221 ? 90.752 28.205 -58.289 1.00 10.62 ? 221  ASN B CB  1 
ATOM   5451 C CG  . ASN B 1 221 ? 90.398 29.609 -57.865 1.00 9.15  ? 221  ASN B CG  1 
ATOM   5452 O OD1 . ASN B 1 221 ? 89.786 30.359 -58.617 1.00 13.20 ? 221  ASN B OD1 1 
ATOM   5453 N ND2 . ASN B 1 221 ? 90.793 29.980 -56.650 1.00 10.08 ? 221  ASN B ND2 1 
ATOM   5454 N N   . LYS B 1 222 ? 90.356 25.265 -59.385 1.00 10.57 ? 222  LYS B N   1 
ATOM   5455 C CA  . LYS B 1 222 ? 90.841 24.024 -59.994 1.00 14.94 ? 222  LYS B CA  1 
ATOM   5456 C C   . LYS B 1 222 ? 90.023 23.651 -61.221 1.00 12.79 ? 222  LYS B C   1 
ATOM   5457 O O   . LYS B 1 222 ? 90.569 23.171 -62.220 1.00 12.42 ? 222  LYS B O   1 
ATOM   5458 C CB  . LYS B 1 222 ? 90.749 22.873 -58.998 1.00 17.87 ? 222  LYS B CB  1 
ATOM   5459 C CG  . LYS B 1 222 ? 91.994 22.445 -58.265 1.00 28.66 ? 222  LYS B CG  1 
ATOM   5460 C CD  . LYS B 1 222 ? 92.627 23.521 -57.491 1.00 25.11 ? 222  LYS B CD  1 
ATOM   5461 C CE  . LYS B 1 222 ? 93.864 22.954 -56.785 1.00 34.80 ? 222  LYS B CE  1 
ATOM   5462 N NZ  . LYS B 1 222 ? 93.508 22.140 -55.588 1.00 30.95 ? 222  LYS B NZ  1 
ATOM   5463 N N   . ALA B 1 223 ? 88.700 23.777 -61.128 1.00 12.87 ? 223  ALA B N   1 
ATOM   5464 C CA  . ALA B 1 223 ? 87.850 23.407 -62.255 1.00 11.22 ? 223  ALA B CA  1 
ATOM   5465 C C   . ALA B 1 223 ? 88.144 24.293 -63.455 1.00 13.64 ? 223  ALA B C   1 
ATOM   5466 O O   . ALA B 1 223 ? 88.238 23.811 -64.586 1.00 12.92 ? 223  ALA B O   1 
ATOM   5467 C CB  . ALA B 1 223 ? 86.371 23.503 -61.868 1.00 9.93  ? 223  ALA B CB  1 
ATOM   5468 N N   . TYR B 1 224 ? 88.298 25.593 -63.225 1.00 11.11 ? 224  TYR B N   1 
ATOM   5469 C CA  . TYR B 1 224 ? 88.599 26.499 -64.326 1.00 12.69 ? 224  TYR B CA  1 
ATOM   5470 C C   . TYR B 1 224 ? 89.878 26.081 -65.048 1.00 14.74 ? 224  TYR B C   1 
ATOM   5471 O O   . TYR B 1 224 ? 89.901 25.970 -66.277 1.00 11.32 ? 224  TYR B O   1 
ATOM   5472 C CB  . TYR B 1 224 ? 88.712 27.927 -63.798 1.00 10.87 ? 224  TYR B CB  1 
ATOM   5473 C CG  . TYR B 1 224 ? 89.118 28.942 -64.854 1.00 13.46 ? 224  TYR B CG  1 
ATOM   5474 C CD1 . TYR B 1 224 ? 88.155 29.569 -65.648 1.00 13.21 ? 224  TYR B CD1 1 
ATOM   5475 C CD2 . TYR B 1 224 ? 90.459 29.283 -65.048 1.00 12.05 ? 224  TYR B CD2 1 
ATOM   5476 C CE1 . TYR B 1 224 ? 88.512 30.505 -66.608 1.00 14.09 ? 224  TYR B CE1 1 
ATOM   5477 C CE2 . TYR B 1 224 ? 90.830 30.220 -66.005 1.00 14.63 ? 224  TYR B CE2 1 
ATOM   5478 C CZ  . TYR B 1 224 ? 89.849 30.825 -66.782 1.00 17.28 ? 224  TYR B CZ  1 
ATOM   5479 O OH  . TYR B 1 224 ? 90.203 31.747 -67.732 1.00 13.23 ? 224  TYR B OH  1 
ATOM   5480 N N   . GLU B 1 225 ? 90.950 25.837 -64.291 1.00 13.11 ? 225  GLU B N   1 
ATOM   5481 C CA  . GLU B 1 225 ? 92.227 25.443 -64.880 1.00 17.97 ? 225  GLU B CA  1 
ATOM   5482 C C   . GLU B 1 225 ? 92.097 24.172 -65.713 1.00 17.42 ? 225  GLU B C   1 
ATOM   5483 O O   . GLU B 1 225 ? 92.622 24.095 -66.829 1.00 19.28 ? 225  GLU B O   1 
ATOM   5484 C CB  . GLU B 1 225 ? 93.260 25.262 -63.767 1.00 19.95 ? 225  GLU B CB  1 
ATOM   5485 C CG  . GLU B 1 225 ? 93.567 26.561 -63.042 1.00 25.78 ? 225  GLU B CG  1 
ATOM   5486 C CD  . GLU B 1 225 ? 95.030 26.716 -62.686 1.00 35.65 ? 225  GLU B CD  1 
ATOM   5487 O OE1 . GLU B 1 225 ? 95.716 25.680 -62.536 1.00 38.19 ? 225  GLU B OE1 1 
ATOM   5488 O OE2 . GLU B 1 225 ? 95.489 27.872 -62.555 1.00 43.20 ? 225  GLU B OE2 1 
ATOM   5489 N N   . THR B 1 226 ? 91.415 23.152 -65.190 1.00 14.85 ? 226  THR B N   1 
ATOM   5490 C CA  . THR B 1 226 ? 91.302 21.928 -65.978 1.00 18.43 ? 226  THR B CA  1 
ATOM   5491 C C   . THR B 1 226 ? 90.394 22.131 -67.187 1.00 20.77 ? 226  THR B C   1 
ATOM   5492 O O   . THR B 1 226 ? 90.703 21.650 -68.285 1.00 17.04 ? 226  THR B O   1 
ATOM   5493 C CB  . THR B 1 226 ? 90.823 20.757 -65.119 1.00 19.39 ? 226  THR B CB  1 
ATOM   5494 O OG1 . THR B 1 226 ? 90.825 19.569 -65.919 1.00 20.02 ? 226  THR B OG1 1 
ATOM   5495 C CG2 . THR B 1 226 ? 89.403 20.980 -64.578 1.00 15.15 ? 226  THR B CG2 1 
ATOM   5496 N N   . MET B 1 227 ? 89.297 22.877 -67.017 1.00 15.15 ? 227  MET B N   1 
ATOM   5497 C CA  . MET B 1 227 ? 88.347 23.044 -68.109 1.00 14.01 ? 227  MET B CA  1 
ATOM   5498 C C   . MET B 1 227 ? 88.984 23.775 -69.280 1.00 16.62 ? 227  MET B C   1 
ATOM   5499 O O   . MET B 1 227 ? 88.748 23.420 -70.441 1.00 17.97 ? 227  MET B O   1 
ATOM   5500 C CB  . MET B 1 227 ? 87.113 23.801 -67.619 1.00 11.20 ? 227  MET B CB  1 
ATOM   5501 C CG  . MET B 1 227 ? 86.217 22.977 -66.719 1.00 14.81 ? 227  MET B CG  1 
ATOM   5502 S SD  . MET B 1 227 ? 84.861 23.962 -66.066 1.00 16.48 ? 227  MET B SD  1 
ATOM   5503 C CE  . MET B 1 227 ? 83.795 23.988 -67.486 1.00 15.08 ? 227  MET B CE  1 
ATOM   5504 N N   . LYS B 1 228 ? 89.798 24.799 -68.997 1.00 16.29 ? 228  LYS B N   1 
ATOM   5505 C CA  . LYS B 1 228 ? 90.386 25.594 -70.072 1.00 16.62 ? 228  LYS B CA  1 
ATOM   5506 C C   . LYS B 1 228 ? 91.397 24.811 -70.900 1.00 22.46 ? 228  LYS B C   1 
ATOM   5507 O O   . LYS B 1 228 ? 91.744 25.255 -71.999 1.00 17.46 ? 228  LYS B O   1 
ATOM   5508 C CB  . LYS B 1 228 ? 91.055 26.856 -69.519 1.00 18.98 ? 228  LYS B CB  1 
ATOM   5509 C CG  . LYS B 1 228 ? 90.102 27.838 -68.873 1.00 16.92 ? 228  LYS B CG  1 
ATOM   5510 C CD  . LYS B 1 228 ? 89.120 28.456 -69.876 1.00 17.64 ? 228  LYS B CD  1 
ATOM   5511 C CE  . LYS B 1 228 ? 89.673 29.748 -70.463 1.00 25.23 ? 228  LYS B CE  1 
ATOM   5512 N NZ  . LYS B 1 228 ? 88.778 30.299 -71.529 1.00 20.13 ? 228  LYS B NZ  1 
ATOM   5513 N N   . GLN B 1 229 ? 91.890 23.669 -70.404 1.00 19.92 ? 229  GLN B N   1 
ATOM   5514 C CA  . GLN B 1 229 ? 92.705 22.804 -71.252 1.00 20.87 ? 229  GLN B CA  1 
ATOM   5515 C C   . GLN B 1 229 ? 91.894 22.138 -72.353 1.00 23.31 ? 229  GLN B C   1 
ATOM   5516 O O   . GLN B 1 229 ? 92.465 21.753 -73.374 1.00 21.86 ? 229  GLN B O   1 
ATOM   5517 C CB  . GLN B 1 229 ? 93.407 21.725 -70.419 1.00 18.50 ? 229  GLN B CB  1 
ATOM   5518 C CG  . GLN B 1 229 ? 94.114 22.272 -69.190 1.00 24.05 ? 229  GLN B CG  1 
ATOM   5519 C CD  . GLN B 1 229 ? 94.809 21.200 -68.352 1.00 36.77 ? 229  GLN B CD  1 
ATOM   5520 O OE1 . GLN B 1 229 ? 94.864 20.024 -68.725 1.00 37.56 ? 229  GLN B OE1 1 
ATOM   5521 N NE2 . GLN B 1 229 ? 95.358 21.615 -67.214 1.00 38.11 ? 229  GLN B NE2 1 
ATOM   5522 N N   . PHE B 1 230 ? 90.585 21.997 -72.187 1.00 18.65 ? 230  PHE B N   1 
ATOM   5523 C CA  . PHE B 1 230 ? 89.806 21.181 -73.101 1.00 21.40 ? 230  PHE B CA  1 
ATOM   5524 C C   . PHE B 1 230 ? 88.725 21.956 -73.832 1.00 22.70 ? 230  PHE B C   1 
ATOM   5525 O O   . PHE B 1 230 ? 88.061 21.388 -74.705 1.00 25.35 ? 230  PHE B O   1 
ATOM   5526 C CB  . PHE B 1 230 ? 89.198 19.997 -72.337 1.00 18.77 ? 230  PHE B CB  1 
ATOM   5527 C CG  . PHE B 1 230 ? 90.234 19.137 -71.676 1.00 22.53 ? 230  PHE B CG  1 
ATOM   5528 C CD1 . PHE B 1 230 ? 91.105 18.374 -72.437 1.00 25.59 ? 230  PHE B CD1 1 
ATOM   5529 C CD2 . PHE B 1 230 ? 90.381 19.135 -70.299 1.00 21.10 ? 230  PHE B CD2 1 
ATOM   5530 C CE1 . PHE B 1 230 ? 92.087 17.596 -71.835 1.00 24.70 ? 230  PHE B CE1 1 
ATOM   5531 C CE2 . PHE B 1 230 ? 91.356 18.362 -69.692 1.00 26.52 ? 230  PHE B CE2 1 
ATOM   5532 C CZ  . PHE B 1 230 ? 92.213 17.592 -70.462 1.00 26.64 ? 230  PHE B CZ  1 
ATOM   5533 N N   . THR B 1 231 ? 88.530 23.233 -73.520 1.00 17.96 ? 231  THR B N   1 
ATOM   5534 C CA  . THR B 1 231 ? 87.543 24.019 -74.238 1.00 19.12 ? 231  THR B CA  1 
ATOM   5535 C C   . THR B 1 231 ? 88.085 25.419 -74.457 1.00 22.15 ? 231  THR B C   1 
ATOM   5536 O O   . THR B 1 231 ? 88.858 25.937 -73.649 1.00 22.86 ? 231  THR B O   1 
ATOM   5537 C CB  . THR B 1 231 ? 86.180 24.074 -73.508 1.00 20.83 ? 231  THR B CB  1 
ATOM   5538 O OG1 . THR B 1 231 ? 85.286 24.918 -74.240 1.00 23.33 ? 231  THR B OG1 1 
ATOM   5539 C CG2 . THR B 1 231 ? 86.311 24.623 -72.093 1.00 19.89 ? 231  THR B CG2 1 
ATOM   5540 N N   . ASN B 1 232 ? 87.693 26.011 -75.583 1.00 23.82 ? 232  ASN B N   1 
ATOM   5541 C CA  . ASN B 1 232 ? 87.963 27.411 -75.880 1.00 28.24 ? 232  ASN B CA  1 
ATOM   5542 C C   . ASN B 1 232 ? 86.797 28.320 -75.516 1.00 25.31 ? 232  ASN B C   1 
ATOM   5543 O O   . ASN B 1 232 ? 86.918 29.540 -75.635 1.00 28.73 ? 232  ASN B O   1 
ATOM   5544 C CB  . ASN B 1 232 ? 88.301 27.585 -77.368 1.00 33.68 ? 232  ASN B CB  1 
ATOM   5545 C CG  . ASN B 1 232 ? 89.765 27.311 -77.676 1.00 46.71 ? 232  ASN B CG  1 
ATOM   5546 O OD1 . ASN B 1 232 ? 90.527 26.855 -76.816 1.00 40.96 ? 232  ASN B OD1 1 
ATOM   5547 N ND2 . ASN B 1 232 ? 90.161 27.570 -78.921 1.00 57.61 ? 232  ASN B ND2 1 
ATOM   5548 N N   . LYS B 1 233 ? 85.677 27.760 -75.080 1.00 21.39 ? 233  LYS B N   1 
ATOM   5549 C CA  . LYS B 1 233 ? 84.537 28.584 -74.719 1.00 21.68 ? 233  LYS B CA  1 
ATOM   5550 C C   . LYS B 1 233 ? 84.789 29.307 -73.392 1.00 18.18 ? 233  LYS B C   1 
ATOM   5551 O O   . LYS B 1 233 ? 85.579 28.849 -72.561 1.00 16.11 ? 233  LYS B O   1 
ATOM   5552 C CB  . LYS B 1 233 ? 83.282 27.720 -74.629 1.00 21.87 ? 233  LYS B CB  1 
ATOM   5553 C CG  . LYS B 1 233 ? 83.080 26.852 -75.867 1.00 23.41 ? 233  LYS B CG  1 
ATOM   5554 C CD  . LYS B 1 233 ? 82.426 27.649 -77.007 1.00 27.85 ? 233  LYS B CD  1 
ATOM   5555 C CE  . LYS B 1 233 ? 82.404 26.835 -78.314 1.00 30.67 ? 233  LYS B CE  1 
ATOM   5556 N NZ  . LYS B 1 233 ? 82.008 25.409 -78.036 1.00 31.72 ? 233  LYS B NZ  1 
ATOM   5557 N N   . PRO B 1 234 ? 84.133 30.444 -73.173 1.00 17.13 ? 234  PRO B N   1 
ATOM   5558 C CA  . PRO B 1 234 ? 84.306 31.156 -71.903 1.00 15.42 ? 234  PRO B CA  1 
ATOM   5559 C C   . PRO B 1 234 ? 83.836 30.300 -70.742 1.00 12.97 ? 234  PRO B C   1 
ATOM   5560 O O   . PRO B 1 234 ? 82.834 29.588 -70.841 1.00 12.91 ? 234  PRO B O   1 
ATOM   5561 C CB  . PRO B 1 234 ? 83.426 32.401 -72.071 1.00 14.61 ? 234  PRO B CB  1 
ATOM   5562 C CG  . PRO B 1 234 ? 83.268 32.559 -73.562 1.00 22.39 ? 234  PRO B CG  1 
ATOM   5563 C CD  . PRO B 1 234 ? 83.234 31.164 -74.092 1.00 18.85 ? 234  PRO B CD  1 
ATOM   5564 N N   . VAL B 1 235 ? 84.576 30.365 -69.638 1.00 10.78 ? 235  VAL B N   1 
ATOM   5565 C CA  . VAL B 1 235 ? 84.205 29.705 -68.389 1.00 11.28 ? 235  VAL B CA  1 
ATOM   5566 C C   . VAL B 1 235 ? 84.135 30.784 -67.315 1.00 14.48 ? 235  VAL B C   1 
ATOM   5567 O O   . VAL B 1 235 ? 85.141 31.450 -67.032 1.00 12.01 ? 235  VAL B O   1 
ATOM   5568 C CB  . VAL B 1 235 ? 85.200 28.601 -67.986 1.00 12.95 ? 235  VAL B CB  1 
ATOM   5569 C CG1 . VAL B 1 235 ? 84.780 27.972 -66.655 1.00 10.91 ? 235  VAL B CG1 1 
ATOM   5570 C CG2 . VAL B 1 235 ? 85.306 27.522 -69.068 1.00 11.80 ? 235  VAL B CG2 1 
ATOM   5571 N N   . GLY B 1 236 ? 82.952 30.959 -66.722 1.00 9.90  ? 236  GLY B N   1 
ATOM   5572 C CA  . GLY B 1 236 ? 82.778 31.959 -65.686 1.00 10.96 ? 236  GLY B CA  1 
ATOM   5573 C C   . GLY B 1 236 ? 82.230 31.384 -64.393 1.00 10.24 ? 236  GLY B C   1 
ATOM   5574 O O   . GLY B 1 236 ? 82.286 30.172 -64.161 1.00 8.68  ? 236  GLY B O   1 
ATOM   5575 N N   . ILE B 1 237 ? 81.708 32.252 -63.534 1.00 8.93  ? 237  ILE B N   1 
ATOM   5576 C CA  . ILE B 1 237 ? 81.039 31.851 -62.305 1.00 8.81  ? 237  ILE B CA  1 
ATOM   5577 C C   . ILE B 1 237 ? 79.811 32.740 -62.146 1.00 9.38  ? 237  ILE B C   1 
ATOM   5578 O O   . ILE B 1 237 ? 79.737 33.842 -62.695 1.00 10.60 ? 237  ILE B O   1 
ATOM   5579 C CB  . ILE B 1 237 ? 81.970 31.958 -61.068 1.00 7.56  ? 237  ILE B CB  1 
ATOM   5580 C CG1 . ILE B 1 237 ? 81.498 31.027 -59.943 1.00 8.27  ? 237  ILE B CG1 1 
ATOM   5581 C CG2 . ILE B 1 237 ? 82.081 33.407 -60.591 1.00 6.60  ? 237  ILE B CG2 1 
ATOM   5582 C CD1 . ILE B 1 237 ? 82.453 30.971 -58.742 1.00 6.81  ? 237  ILE B CD1 1 
ATOM   5583 N N   . ILE B 1 238 ? 78.833 32.240 -61.394 1.00 11.58 ? 238  ILE B N   1 
ATOM   5584 C CA  . ILE B 1 238 ? 77.598 32.962 -61.110 1.00 10.41 ? 238  ILE B CA  1 
ATOM   5585 C C   . ILE B 1 238 ? 77.532 33.183 -59.603 1.00 9.82  ? 238  ILE B C   1 
ATOM   5586 O O   . ILE B 1 238 ? 77.645 32.225 -58.825 1.00 7.70  ? 238  ILE B O   1 
ATOM   5587 C CB  . ILE B 1 238 ? 76.362 32.191 -61.616 1.00 10.17 ? 238  ILE B CB  1 
ATOM   5588 C CG1 . ILE B 1 238 ? 76.322 32.202 -63.151 1.00 9.78  ? 238  ILE B CG1 1 
ATOM   5589 C CG2 . ILE B 1 238 ? 75.099 32.798 -61.030 1.00 7.99  ? 238  ILE B CG2 1 
ATOM   5590 C CD1 . ILE B 1 238 ? 75.355 31.168 -63.770 1.00 9.46  ? 238  ILE B CD1 1 
ATOM   5591 N N   . TYR B 1 239 ? 77.346 34.439 -59.190 1.00 10.01 ? 239  TYR B N   1 
ATOM   5592 C CA  . TYR B 1 239 ? 77.512 34.810 -57.793 1.00 9.22  ? 239  TYR B CA  1 
ATOM   5593 C C   . TYR B 1 239 ? 76.298 35.594 -57.302 1.00 11.67 ? 239  TYR B C   1 
ATOM   5594 O O   . TYR B 1 239 ? 75.779 36.458 -58.015 1.00 9.75  ? 239  TYR B O   1 
ATOM   5595 C CB  . TYR B 1 239 ? 78.804 35.641 -57.605 1.00 9.84  ? 239  TYR B CB  1 
ATOM   5596 C CG  . TYR B 1 239 ? 79.215 35.724 -56.157 1.00 9.95  ? 239  TYR B CG  1 
ATOM   5597 C CD1 . TYR B 1 239 ? 80.008 34.730 -55.573 1.00 7.08  ? 239  TYR B CD1 1 
ATOM   5598 C CD2 . TYR B 1 239 ? 78.779 36.772 -55.359 1.00 8.39  ? 239  TYR B CD2 1 
ATOM   5599 C CE1 . TYR B 1 239 ? 80.356 34.787 -54.242 1.00 8.61  ? 239  TYR B CE1 1 
ATOM   5600 C CE2 . TYR B 1 239 ? 79.128 36.839 -54.007 1.00 8.96  ? 239  TYR B CE2 1 
ATOM   5601 C CZ  . TYR B 1 239 ? 79.918 35.847 -53.460 1.00 9.32  ? 239  TYR B CZ  1 
ATOM   5602 O OH  . TYR B 1 239 ? 80.252 35.917 -52.120 1.00 9.62  ? 239  TYR B OH  1 
ATOM   5603 N N   . ALA B 1 240 ? 75.843 35.284 -56.082 1.00 8.66  ? 240  ALA B N   1 
ATOM   5604 C CA  . ALA B 1 240 ? 74.762 36.040 -55.440 1.00 11.98 ? 240  ALA B CA  1 
ATOM   5605 C C   . ALA B 1 240 ? 75.347 37.316 -54.842 1.00 12.29 ? 240  ALA B C   1 
ATOM   5606 O O   . ALA B 1 240 ? 75.841 37.321 -53.710 1.00 10.88 ? 240  ALA B O   1 
ATOM   5607 C CB  . ALA B 1 240 ? 74.067 35.205 -54.373 1.00 9.73  ? 240  ALA B CB  1 
ATOM   5608 N N   . THR B 1 241 ? 75.281 38.409 -55.598 1.00 10.78 ? 241  THR B N   1 
ATOM   5609 C CA  . THR B 1 241 ? 75.874 39.678 -55.180 1.00 14.33 ? 241  THR B CA  1 
ATOM   5610 C C   . THR B 1 241 ? 74.886 40.439 -54.308 1.00 14.83 ? 241  THR B C   1 
ATOM   5611 O O   . THR B 1 241 ? 73.831 40.865 -54.789 1.00 16.51 ? 241  THR B O   1 
ATOM   5612 C CB  . THR B 1 241 ? 76.241 40.536 -56.386 1.00 16.12 ? 241  THR B CB  1 
ATOM   5613 O OG1 . THR B 1 241 ? 75.057 40.730 -57.173 1.00 17.82 ? 241  THR B OG1 1 
ATOM   5614 C CG2 . THR B 1 241 ? 77.283 39.844 -57.235 1.00 13.91 ? 241  THR B CG2 1 
ATOM   5615 N N   . SER B 1 242 ? 75.243 40.645 -53.047 1.00 13.75 ? 242  SER B N   1 
ATOM   5616 C CA  . SER B 1 242 ? 74.452 41.484 -52.165 1.00 16.19 ? 242  SER B CA  1 
ATOM   5617 C C   . SER B 1 242 ? 74.729 42.959 -52.449 1.00 14.09 ? 242  SER B C   1 
ATOM   5618 O O   . SER B 1 242 ? 75.815 43.333 -52.906 1.00 12.33 ? 242  SER B O   1 
ATOM   5619 C CB  . SER B 1 242 ? 74.778 41.161 -50.704 1.00 13.25 ? 242  SER B CB  1 
ATOM   5620 O OG  . SER B 1 242 ? 74.401 39.829 -50.397 1.00 17.18 ? 242  SER B OG  1 
ATOM   5621 N N   . TRP B 1 243 ? 73.731 43.801 -52.180 1.00 12.52 ? 243  TRP B N   1 
ATOM   5622 C CA  . TRP B 1 243 ? 73.917 45.251 -52.161 1.00 11.81 ? 243  TRP B CA  1 
ATOM   5623 C C   . TRP B 1 243 ? 73.537 45.730 -50.765 1.00 15.83 ? 243  TRP B C   1 
ATOM   5624 O O   . TRP B 1 243 ? 72.351 45.805 -50.427 1.00 11.16 ? 243  TRP B O   1 
ATOM   5625 C CB  . TRP B 1 243 ? 73.099 45.980 -53.231 1.00 12.72 ? 243  TRP B CB  1 
ATOM   5626 C CG  . TRP B 1 243 ? 73.327 47.452 -53.071 1.00 11.96 ? 243  TRP B CG  1 
ATOM   5627 C CD1 . TRP B 1 243 ? 72.437 48.373 -52.609 1.00 13.32 ? 243  TRP B CD1 1 
ATOM   5628 C CD2 . TRP B 1 243 ? 74.561 48.144 -53.262 1.00 12.20 ? 243  TRP B CD2 1 
ATOM   5629 N NE1 . TRP B 1 243 ? 73.031 49.607 -52.533 1.00 14.15 ? 243  TRP B NE1 1 
ATOM   5630 C CE2 . TRP B 1 243 ? 74.337 49.496 -52.931 1.00 15.41 ? 243  TRP B CE2 1 
ATOM   5631 C CE3 . TRP B 1 243 ? 75.831 47.759 -53.711 1.00 14.57 ? 243  TRP B CE3 1 
ATOM   5632 C CZ2 . TRP B 1 243 ? 75.336 50.466 -53.025 1.00 13.96 ? 243  TRP B CZ2 1 
ATOM   5633 C CZ3 . TRP B 1 243 ? 76.828 48.725 -53.800 1.00 15.46 ? 243  TRP B CZ3 1 
ATOM   5634 C CH2 . TRP B 1 243 ? 76.573 50.060 -53.459 1.00 14.70 ? 243  TRP B CH2 1 
ATOM   5635 N N   . CYS B 1 244 ? 74.533 46.060 -49.951 1.00 12.46 ? 244  CYS B N   1 
ATOM   5636 C CA  . CYS B 1 244 ? 74.294 46.418 -48.561 1.00 13.83 ? 244  CYS B CA  1 
ATOM   5637 C C   . CYS B 1 244 ? 74.333 47.931 -48.402 1.00 19.04 ? 244  CYS B C   1 
ATOM   5638 O O   . CYS B 1 244 ? 75.284 48.582 -48.846 1.00 18.35 ? 244  CYS B O   1 
ATOM   5639 C CB  . CYS B 1 244 ? 75.335 45.784 -47.640 1.00 15.99 ? 244  CYS B CB  1 
ATOM   5640 S SG  . CYS B 1 244 ? 75.341 43.991 -47.605 1.00 19.77 ? 244  CYS B SG  1 
ATOM   5641 N N   . GLU B 1 245 ? 73.303 48.478 -47.767 1.00 16.41 ? 245  GLU B N   1 
ATOM   5642 C CA  . GLU B 1 245 ? 73.256 49.870 -47.352 1.00 22.29 ? 245  GLU B CA  1 
ATOM   5643 C C   . GLU B 1 245 ? 73.112 49.914 -45.833 1.00 20.28 ? 245  GLU B C   1 
ATOM   5644 O O   . GLU B 1 245 ? 72.895 48.895 -45.179 1.00 19.02 ? 245  GLU B O   1 
ATOM   5645 C CB  . GLU B 1 245 ? 72.101 50.614 -48.050 1.00 17.59 ? 245  GLU B CB  1 
ATOM   5646 C CG  . GLU B 1 245 ? 72.148 50.491 -49.571 1.00 15.98 ? 245  GLU B CG  1 
ATOM   5647 C CD  . GLU B 1 245 ? 70.949 51.108 -50.277 1.00 16.67 ? 245  GLU B CD  1 
ATOM   5648 O OE1 . GLU B 1 245 ? 69.920 51.365 -49.612 1.00 17.61 ? 245  GLU B OE1 1 
ATOM   5649 O OE2 . GLU B 1 245 ? 71.044 51.348 -51.502 1.00 16.61 ? 245  GLU B OE2 1 
ATOM   5650 N N   . GLY B 1 246 ? 73.235 51.109 -45.266 1.00 27.91 ? 246  GLY B N   1 
ATOM   5651 C CA  . GLY B 1 246 ? 73.111 51.269 -43.830 1.00 24.88 ? 246  GLY B CA  1 
ATOM   5652 C C   . GLY B 1 246 ? 74.218 52.123 -43.248 1.00 26.71 ? 246  GLY B C   1 
ATOM   5653 O O   . GLY B 1 246 ? 74.690 53.057 -43.900 1.00 24.75 ? 246  GLY B O   1 
ATOM   5654 N N   . ASP B 1 247 ? 74.652 51.821 -42.027 1.00 23.83 ? 247  ASP B N   1 
ATOM   5655 C CA  . ASP B 1 247 ? 75.731 52.597 -41.435 1.00 26.27 ? 247  ASP B CA  1 
ATOM   5656 C C   . ASP B 1 247 ? 77.069 52.141 -42.026 1.00 29.23 ? 247  ASP B C   1 
ATOM   5657 O O   . ASP B 1 247 ? 77.135 51.354 -42.975 1.00 28.04 ? 247  ASP B O   1 
ATOM   5658 C CB  . ASP B 1 247 ? 75.669 52.508 -39.910 1.00 29.08 ? 247  ASP B CB  1 
ATOM   5659 C CG  . ASP B 1 247 ? 75.908 51.097 -39.376 1.00 27.05 ? 247  ASP B CG  1 
ATOM   5660 O OD1 . ASP B 1 247 ? 76.313 50.197 -40.148 1.00 26.39 ? 247  ASP B OD1 1 
ATOM   5661 O OD2 . ASP B 1 247 ? 75.679 50.889 -38.166 1.00 21.49 ? 247  ASP B OD2 1 
ATOM   5662 N N   . ASP B 1 248 ? 78.157 52.629 -41.447 1.00 28.45 ? 248  ASP B N   1 
ATOM   5663 C CA  . ASP B 1 248 ? 79.497 52.330 -41.924 1.00 32.43 ? 248  ASP B CA  1 
ATOM   5664 C C   . ASP B 1 248 ? 79.867 50.846 -41.852 1.00 32.88 ? 248  ASP B C   1 
ATOM   5665 O O   . ASP B 1 248 ? 80.878 50.452 -42.448 1.00 35.14 ? 248  ASP B O   1 
ATOM   5666 C CB  . ASP B 1 248 ? 80.468 53.213 -41.140 1.00 36.64 ? 248  ASP B CB  1 
ATOM   5667 N N   . ALA B 1 249 ? 79.079 50.007 -41.179 1.00 24.80 ? 249  ALA B N   1 
ATOM   5668 C CA  . ALA B 1 249 ? 79.343 48.570 -41.256 1.00 22.73 ? 249  ALA B CA  1 
ATOM   5669 C C   . ALA B 1 249 ? 78.985 47.966 -42.618 1.00 22.42 ? 249  ALA B C   1 
ATOM   5670 O O   . ALA B 1 249 ? 79.229 46.769 -42.821 1.00 20.46 ? 249  ALA B O   1 
ATOM   5671 C CB  . ALA B 1 249 ? 78.590 47.828 -40.148 1.00 21.94 ? 249  ALA B CB  1 
ATOM   5672 N N   . ARG B 1 250 ? 78.427 48.749 -43.552 1.00 23.03 ? 250  ARG B N   1 
ATOM   5673 C CA  . ARG B 1 250 ? 78.050 48.181 -44.841 1.00 22.27 ? 250  ARG B CA  1 
ATOM   5674 C C   . ARG B 1 250 ? 79.277 47.684 -45.607 1.00 23.03 ? 250  ARG B C   1 
ATOM   5675 O O   . ARG B 1 250 ? 79.179 46.715 -46.369 1.00 19.80 ? 250  ARG B O   1 
ATOM   5676 C CB  . ARG B 1 250 ? 77.268 49.199 -45.690 1.00 22.71 ? 250  ARG B CB  1 
ATOM   5677 C CG  . ARG B 1 250 ? 78.067 50.443 -46.096 1.00 30.84 ? 250  ARG B CG  1 
ATOM   5678 C CD  . ARG B 1 250 ? 77.353 51.304 -47.163 1.00 33.33 ? 250  ARG B CD  1 
ATOM   5679 N NE  . ARG B 1 250 ? 76.102 51.917 -46.729 1.00 42.02 ? 250  ARG B NE  1 
ATOM   5680 C CZ  . ARG B 1 250 ? 75.328 52.677 -47.502 1.00 43.19 ? 250  ARG B CZ  1 
ATOM   5681 N NH1 . ARG B 1 250 ? 75.568 52.823 -48.803 1.00 40.51 ? 250  ARG B NH1 1 
ATOM   5682 N NH2 . ARG B 1 250 ? 74.272 53.291 -46.964 1.00 26.50 ? 250  ARG B NH2 1 
ATOM   5683 N N   . ASN B 1 251 ? 80.438 48.315 -45.405 1.00 20.17 ? 251  ASN B N   1 
ATOM   5684 C CA  . ASN B 1 251 ? 81.644 47.899 -46.115 1.00 21.83 ? 251  ASN B CA  1 
ATOM   5685 C C   . ASN B 1 251 ? 82.143 46.551 -45.614 1.00 20.89 ? 251  ASN B C   1 
ATOM   5686 O O   . ASN B 1 251 ? 82.594 45.716 -46.408 1.00 17.10 ? 251  ASN B O   1 
ATOM   5687 C CB  . ASN B 1 251 ? 82.734 48.960 -45.961 1.00 23.66 ? 251  ASN B CB  1 
ATOM   5688 C CG  . ASN B 1 251 ? 82.349 50.289 -46.582 1.00 34.41 ? 251  ASN B CG  1 
ATOM   5689 O OD1 . ASN B 1 251 ? 81.947 50.358 -47.741 1.00 27.03 ? 251  ASN B OD1 1 
ATOM   5690 N ND2 . ASN B 1 251 ? 82.420 51.350 -45.785 1.00 42.18 ? 251  ASN B ND2 1 
ATOM   5691 N N   . ASP B 1 252 ? 82.095 46.328 -44.296 1.00 15.61 ? 252  ASP B N   1 
ATOM   5692 C CA  . ASP B 1 252 ? 82.435 45.013 -43.758 1.00 17.54 ? 252  ASP B CA  1 
ATOM   5693 C C   . ASP B 1 252 ? 81.463 43.948 -44.243 1.00 18.84 ? 252  ASP B C   1 
ATOM   5694 O O   . ASP B 1 252 ? 81.863 42.811 -44.525 1.00 14.25 ? 252  ASP B O   1 
ATOM   5695 C CB  . ASP B 1 252 ? 82.435 45.041 -42.231 1.00 20.36 ? 252  ASP B CB  1 
ATOM   5696 C CG  . ASP B 1 252 ? 83.451 46.006 -41.673 1.00 26.77 ? 252  ASP B CG  1 
ATOM   5697 O OD1 . ASP B 1 252 ? 84.599 45.991 -42.160 1.00 27.41 ? 252  ASP B OD1 1 
ATOM   5698 O OD2 . ASP B 1 252 ? 83.093 46.784 -40.766 1.00 36.15 ? 252  ASP B OD2 1 
ATOM   5699 N N   . ALA B 1 253 ? 80.171 44.276 -44.283 1.00 16.33 ? 253  ALA B N   1 
ATOM   5700 C CA  . ALA B 1 253 ? 79.196 43.301 -44.754 1.00 15.54 ? 253  ALA B CA  1 
ATOM   5701 C C   . ALA B 1 253 ? 79.451 42.947 -46.218 1.00 14.56 ? 253  ALA B C   1 
ATOM   5702 O O   . ALA B 1 253 ? 79.426 41.767 -46.595 1.00 13.79 ? 253  ALA B O   1 
ATOM   5703 C CB  . ALA B 1 253 ? 77.779 43.841 -44.550 1.00 14.76 ? 253  ALA B CB  1 
ATOM   5704 N N   . MET B 1 254 ? 79.724 43.955 -47.053 1.00 12.88 ? 254  MET B N   1 
ATOM   5705 C CA  . MET B 1 254 ? 79.983 43.693 -48.469 1.00 17.02 ? 254  MET B CA  1 
ATOM   5706 C C   . MET B 1 254 ? 81.221 42.817 -48.651 1.00 16.36 ? 254  MET B C   1 
ATOM   5707 O O   . MET B 1 254 ? 81.259 41.950 -49.536 1.00 13.74 ? 254  MET B O   1 
ATOM   5708 C CB  . MET B 1 254 ? 80.142 45.016 -49.225 1.00 12.64 ? 254  MET B CB  1 
ATOM   5709 C CG  . MET B 1 254 ? 78.847 45.821 -49.363 1.00 13.99 ? 254  MET B CG  1 
ATOM   5710 S SD  . MET B 1 254 ? 77.715 45.034 -50.535 1.00 17.26 ? 254  MET B SD  1 
ATOM   5711 C CE  . MET B 1 254 ? 78.424 45.524 -52.106 1.00 14.48 ? 254  MET B CE  1 
ATOM   5712 N N   . GLU B 1 255 ? 82.239 43.022 -47.807 1.00 17.27 ? 255  GLU B N   1 
ATOM   5713 C CA  . GLU B 1 255 ? 83.455 42.210 -47.874 1.00 17.15 ? 255  GLU B CA  1 
ATOM   5714 C C   . GLU B 1 255 ? 83.150 40.727 -47.666 1.00 15.13 ? 255  GLU B C   1 
ATOM   5715 O O   . GLU B 1 255 ? 83.615 39.873 -48.429 1.00 16.63 ? 255  GLU B O   1 
ATOM   5716 C CB  . GLU B 1 255 ? 84.462 42.723 -46.837 1.00 18.35 ? 255  GLU B CB  1 
ATOM   5717 C CG  . GLU B 1 255 ? 85.716 41.875 -46.650 1.00 23.73 ? 255  GLU B CG  1 
ATOM   5718 C CD  . GLU B 1 255 ? 86.465 41.650 -47.957 1.00 24.46 ? 255  GLU B CD  1 
ATOM   5719 O OE1 . GLU B 1 255 ? 86.697 42.639 -48.685 1.00 26.86 ? 255  GLU B OE1 1 
ATOM   5720 O OE2 . GLU B 1 255 ? 86.869 40.502 -48.229 1.00 27.69 ? 255  GLU B OE2 1 
ATOM   5721 N N   . LEU B 1 256 ? 82.354 40.398 -46.647 1.00 12.35 ? 256  LEU B N   1 
ATOM   5722 C CA  . LEU B 1 256 ? 82.034 38.992 -46.406 1.00 15.48 ? 256  LEU B CA  1 
ATOM   5723 C C   . LEU B 1 256 ? 81.000 38.474 -47.402 1.00 16.28 ? 256  LEU B C   1 
ATOM   5724 O O   . LEU B 1 256 ? 81.096 37.331 -47.867 1.00 13.59 ? 256  LEU B O   1 
ATOM   5725 C CB  . LEU B 1 256 ? 81.539 38.787 -44.968 1.00 13.07 ? 256  LEU B CB  1 
ATOM   5726 C CG  . LEU B 1 256 ? 81.173 37.331 -44.618 1.00 17.60 ? 256  LEU B CG  1 
ATOM   5727 C CD1 . LEU B 1 256 ? 82.310 36.361 -44.955 1.00 16.11 ? 256  LEU B CD1 1 
ATOM   5728 C CD2 . LEU B 1 256 ? 80.743 37.169 -43.142 1.00 16.54 ? 256  LEU B CD2 1 
ATOM   5729 N N   . GLU B 1 257 ? 79.999 39.290 -47.741 1.00 12.61 ? 257  GLU B N   1 
ATOM   5730 C CA  . GLU B 1 257 ? 78.952 38.809 -48.641 1.00 15.55 ? 257  GLU B CA  1 
ATOM   5731 C C   . GLU B 1 257 ? 79.471 38.613 -50.065 1.00 12.93 ? 257  GLU B C   1 
ATOM   5732 O O   . GLU B 1 257 ? 79.091 37.641 -50.732 1.00 13.51 ? 257  GLU B O   1 
ATOM   5733 C CB  . GLU B 1 257 ? 77.765 39.768 -48.642 1.00 12.11 ? 257  GLU B CB  1 
ATOM   5734 C CG  . GLU B 1 257 ? 77.028 39.793 -47.333 1.00 16.84 ? 257  GLU B CG  1 
ATOM   5735 C CD  . GLU B 1 257 ? 75.947 38.740 -47.272 1.00 31.30 ? 257  GLU B CD  1 
ATOM   5736 O OE1 . GLU B 1 257 ? 75.003 38.779 -48.100 1.00 34.93 ? 257  GLU B OE1 1 
ATOM   5737 O OE2 . GLU B 1 257 ? 76.050 37.866 -46.390 1.00 26.51 ? 257  GLU B OE2 1 
ATOM   5738 N N   . ASN B 1 258 ? 80.330 39.519 -50.551 1.00 8.99  ? 258  ASN B N   1 
ATOM   5739 C CA  . ASN B 1 258 ? 80.721 39.545 -51.967 1.00 11.11 ? 258  ASN B CA  1 
ATOM   5740 C C   . ASN B 1 258 ? 82.213 39.326 -52.199 1.00 15.10 ? 258  ASN B C   1 
ATOM   5741 O O   . ASN B 1 258 ? 82.592 38.410 -52.939 1.00 12.44 ? 258  ASN B O   1 
ATOM   5742 C CB  . ASN B 1 258 ? 80.319 40.876 -52.618 1.00 11.87 ? 258  ASN B CB  1 
ATOM   5743 C CG  . ASN B 1 258 ? 78.825 41.050 -52.718 1.00 14.49 ? 258  ASN B CG  1 
ATOM   5744 O OD1 . ASN B 1 258 ? 78.063 40.121 -52.460 1.00 14.53 ? 258  ASN B OD1 1 
ATOM   5745 N ND2 . ASN B 1 258 ? 78.396 42.237 -53.118 1.00 16.46 ? 258  ASN B ND2 1 
ATOM   5746 N N   . TRP B 1 259 ? 83.077 40.164 -51.627 1.00 11.80 ? 259  TRP B N   1 
ATOM   5747 C CA  . TRP B 1 259 ? 84.437 40.264 -52.143 1.00 13.55 ? 259  TRP B CA  1 
ATOM   5748 C C   . TRP B 1 259 ? 85.374 39.208 -51.567 1.00 13.49 ? 259  TRP B C   1 
ATOM   5749 O O   . TRP B 1 259 ? 86.367 38.870 -52.215 1.00 13.58 ? 259  TRP B O   1 
ATOM   5750 C CB  . TRP B 1 259 ? 84.994 41.667 -51.876 1.00 14.67 ? 259  TRP B CB  1 
ATOM   5751 C CG  . TRP B 1 259 ? 84.028 42.793 -52.133 1.00 16.22 ? 259  TRP B CG  1 
ATOM   5752 C CD1 . TRP B 1 259 ? 83.776 43.855 -51.306 1.00 16.56 ? 259  TRP B CD1 1 
ATOM   5753 C CD2 . TRP B 1 259 ? 83.210 42.997 -53.307 1.00 16.34 ? 259  TRP B CD2 1 
ATOM   5754 N NE1 . TRP B 1 259 ? 82.844 44.693 -51.881 1.00 18.96 ? 259  TRP B NE1 1 
ATOM   5755 C CE2 . TRP B 1 259 ? 82.481 44.190 -53.105 1.00 16.91 ? 259  TRP B CE2 1 
ATOM   5756 C CE3 . TRP B 1 259 ? 83.018 42.284 -54.499 1.00 13.57 ? 259  TRP B CE3 1 
ATOM   5757 C CZ2 . TRP B 1 259 ? 81.574 44.689 -54.050 1.00 17.63 ? 259  TRP B CZ2 1 
ATOM   5758 C CZ3 . TRP B 1 259 ? 82.107 42.778 -55.436 1.00 16.93 ? 259  TRP B CZ3 1 
ATOM   5759 C CH2 . TRP B 1 259 ? 81.402 43.974 -55.203 1.00 17.02 ? 259  TRP B CH2 1 
ATOM   5760 N N   . TYR B 1 260 ? 85.101 38.700 -50.361 1.00 13.09 ? 260  TYR B N   1 
ATOM   5761 C CA  . TYR B 1 260 ? 85.904 37.613 -49.805 1.00 13.54 ? 260  TYR B CA  1 
ATOM   5762 C C   . TYR B 1 260 ? 86.036 36.485 -50.820 1.00 15.49 ? 260  TYR B C   1 
ATOM   5763 O O   . TYR B 1 260 ? 87.145 36.069 -51.174 1.00 15.19 ? 260  TYR B O   1 
ATOM   5764 C CB  . TYR B 1 260 ? 85.266 37.124 -48.494 1.00 13.19 ? 260  TYR B CB  1 
ATOM   5765 C CG  . TYR B 1 260 ? 85.877 35.883 -47.846 1.00 17.08 ? 260  TYR B CG  1 
ATOM   5766 C CD1 . TYR B 1 260 ? 85.674 34.612 -48.373 1.00 16.67 ? 260  TYR B CD1 1 
ATOM   5767 C CD2 . TYR B 1 260 ? 86.651 35.987 -46.698 1.00 25.33 ? 260  TYR B CD2 1 
ATOM   5768 C CE1 . TYR B 1 260 ? 86.217 33.483 -47.778 1.00 16.46 ? 260  TYR B CE1 1 
ATOM   5769 C CE2 . TYR B 1 260 ? 87.204 34.860 -46.096 1.00 26.64 ? 260  TYR B CE2 1 
ATOM   5770 C CZ  . TYR B 1 260 ? 86.978 33.615 -46.634 1.00 23.21 ? 260  TYR B CZ  1 
ATOM   5771 O OH  . TYR B 1 260 ? 87.521 32.490 -46.048 1.00 26.54 ? 260  TYR B OH  1 
ATOM   5772 N N   . PHE B 1 261 ? 84.904 36.022 -51.342 1.00 13.87 ? 261  PHE B N   1 
ATOM   5773 C CA  . PHE B 1 261 ? 84.915 34.954 -52.333 1.00 10.10 ? 261  PHE B CA  1 
ATOM   5774 C C   . PHE B 1 261 ? 85.396 35.466 -53.691 1.00 12.77 ? 261  PHE B C   1 
ATOM   5775 O O   . PHE B 1 261 ? 86.285 34.869 -54.312 1.00 11.60 ? 261  PHE B O   1 
ATOM   5776 C CB  . PHE B 1 261 ? 83.506 34.355 -52.422 1.00 9.26  ? 261  PHE B CB  1 
ATOM   5777 C CG  . PHE B 1 261 ? 83.433 33.038 -53.148 1.00 10.25 ? 261  PHE B CG  1 
ATOM   5778 C CD1 . PHE B 1 261 ? 83.608 32.974 -54.525 1.00 9.62  ? 261  PHE B CD1 1 
ATOM   5779 C CD2 . PHE B 1 261 ? 83.176 31.871 -52.451 1.00 8.06  ? 261  PHE B CD2 1 
ATOM   5780 C CE1 . PHE B 1 261 ? 83.527 31.769 -55.201 1.00 10.20 ? 261  PHE B CE1 1 
ATOM   5781 C CE2 . PHE B 1 261 ? 83.098 30.647 -53.119 1.00 8.71  ? 261  PHE B CE2 1 
ATOM   5782 C CZ  . PHE B 1 261 ? 83.275 30.599 -54.493 1.00 11.26 ? 261  PHE B CZ  1 
ATOM   5783 N N   . LEU B 1 262 ? 84.819 36.570 -54.177 1.00 10.94 ? 262  LEU B N   1 
ATOM   5784 C CA  . LEU B 1 262 ? 85.082 36.972 -55.561 1.00 13.55 ? 262  LEU B CA  1 
ATOM   5785 C C   . LEU B 1 262 ? 86.543 37.382 -55.770 1.00 14.42 ? 262  LEU B C   1 
ATOM   5786 O O   . LEU B 1 262 ? 87.126 37.086 -56.822 1.00 10.79 ? 262  LEU B O   1 
ATOM   5787 C CB  . LEU B 1 262 ? 84.125 38.092 -55.980 1.00 10.30 ? 262  LEU B CB  1 
ATOM   5788 C CG  . LEU B 1 262 ? 82.678 37.633 -56.279 1.00 13.85 ? 262  LEU B CG  1 
ATOM   5789 C CD1 . LEU B 1 262 ? 81.783 38.827 -56.597 1.00 8.31  ? 262  LEU B CD1 1 
ATOM   5790 C CD2 . LEU B 1 262 ? 82.612 36.606 -57.417 1.00 10.33 ? 262  LEU B CD2 1 
ATOM   5791 N N   . ASP B 1 263 ? 87.157 38.057 -54.788 1.00 9.90  ? 263  ASP B N   1 
ATOM   5792 C CA  . ASP B 1 263 ? 88.587 38.360 -54.874 1.00 12.72 ? 263  ASP B CA  1 
ATOM   5793 C C   . ASP B 1 263 ? 89.405 37.101 -55.127 1.00 12.71 ? 263  ASP B C   1 
ATOM   5794 O O   . ASP B 1 263 ? 90.406 37.137 -55.845 1.00 14.49 ? 263  ASP B O   1 
ATOM   5795 C CB  . ASP B 1 263 ? 89.079 39.029 -53.583 1.00 12.98 ? 263  ASP B CB  1 
ATOM   5796 C CG  . ASP B 1 263 ? 88.660 40.502 -53.467 1.00 19.75 ? 263  ASP B CG  1 
ATOM   5797 O OD1 . ASP B 1 263 ? 87.978 41.042 -54.384 1.00 14.31 ? 263  ASP B OD1 1 
ATOM   5798 O OD2 . ASP B 1 263 ? 88.969 41.096 -52.412 1.00 16.83 ? 263  ASP B OD2 1 
ATOM   5799 N N   . ARG B 1 264 ? 88.973 35.969 -54.600 1.00 9.65  ? 264  ARG B N   1 
ATOM   5800 C CA  . ARG B 1 264 ? 89.810 34.749 -54.695 1.00 11.59 ? 264  ARG B CA  1 
ATOM   5801 C C   . ARG B 1 264 ? 89.515 33.912 -55.954 1.00 12.32 ? 264  ARG B C   1 
ATOM   5802 O O   . ARG B 1 264 ? 90.191 32.899 -56.124 1.00 11.99 ? 264  ARG B O   1 
ATOM   5803 C CB  . ARG B 1 264 ? 89.674 33.972 -53.383 1.00 10.32 ? 264  ARG B CB  1 
ATOM   5804 C CG  . ARG B 1 264 ? 90.215 34.724 -52.177 1.00 11.05 ? 264  ARG B CG  1 
ATOM   5805 C CD  . ARG B 1 264 ? 89.830 34.099 -50.853 1.00 12.02 ? 264  ARG B CD  1 
ATOM   5806 N NE  . ARG B 1 264 ? 90.241 32.710 -50.735 1.00 15.17 ? 264  ARG B NE  1 
ATOM   5807 C CZ  . ARG B 1 264 ? 90.051 31.961 -49.658 1.00 16.15 ? 264  ARG B CZ  1 
ATOM   5808 N NH1 . ARG B 1 264 ? 89.458 32.470 -48.593 1.00 19.97 ? 264  ARG B NH1 1 
ATOM   5809 N NH2 . ARG B 1 264 ? 90.456 30.708 -49.644 1.00 15.16 ? 264  ARG B NH2 1 
ATOM   5810 N N   . VAL B 1 265 ? 88.568 34.328 -56.795 1.00 10.26 ? 265  VAL B N   1 
ATOM   5811 C CA  . VAL B 1 265 ? 88.294 33.583 -58.065 1.00 9.77  ? 265  VAL B CA  1 
ATOM   5812 C C   . VAL B 1 265 ? 88.366 34.501 -59.302 1.00 13.61 ? 265  VAL B C   1 
ATOM   5813 O O   . VAL B 1 265 ? 88.359 33.966 -60.405 1.00 10.04 ? 265  VAL B O   1 
ATOM   5814 C CB  . VAL B 1 265 ? 86.938 32.859 -57.977 1.00 12.14 ? 265  VAL B CB  1 
ATOM   5815 C CG1 . VAL B 1 265 ? 86.924 31.781 -56.908 1.00 10.07 ? 265  VAL B CG1 1 
ATOM   5816 C CG2 . VAL B 1 265 ? 85.782 33.829 -57.796 1.00 9.16  ? 265  VAL B CG2 1 
ATOM   5817 N N   . ILE B 1 266 ? 88.428 35.815 -59.107 1.00 9.98  ? 266  ILE B N   1 
ATOM   5818 C CA  . ILE B 1 266 ? 88.416 36.798 -60.229 1.00 12.82 ? 266  ILE B CA  1 
ATOM   5819 C C   . ILE B 1 266 ? 89.470 36.453 -61.299 1.00 13.87 ? 266  ILE B C   1 
ATOM   5820 O O   . ILE B 1 266 ? 89.168 36.605 -62.467 1.00 13.44 ? 266  ILE B O   1 
ATOM   5821 C CB  . ILE B 1 266 ? 88.561 38.232 -59.685 1.00 13.44 ? 266  ILE B CB  1 
ATOM   5822 C CG1 . ILE B 1 266 ? 88.120 39.266 -60.724 1.00 13.70 ? 266  ILE B CG1 1 
ATOM   5823 C CG2 . ILE B 1 266 ? 89.964 38.491 -59.163 1.00 15.10 ? 266  ILE B CG2 1 
ATOM   5824 C CD1 . ILE B 1 266 ? 86.662 39.149 -61.100 1.00 15.30 ? 266  ILE B CD1 1 
ATOM   5825 N N   . ASP B 1 267 ? 90.655 35.996 -60.891 1.00 14.69 ? 267  ASP B N   1 
ATOM   5826 C CA  . ASP B 1 267 ? 91.723 35.747 -61.901 1.00 17.91 ? 267  ASP B CA  1 
ATOM   5827 C C   . ASP B 1 267 ? 91.468 34.424 -62.629 1.00 17.18 ? 267  ASP B C   1 
ATOM   5828 O O   . ASP B 1 267 ? 92.244 34.113 -63.527 1.00 20.52 ? 267  ASP B O   1 
ATOM   5829 C CB  . ASP B 1 267 ? 93.103 35.801 -61.257 1.00 21.94 ? 267  ASP B CB  1 
ATOM   5830 C CG  . ASP B 1 267 ? 93.422 37.204 -60.770 1.00 27.76 ? 267  ASP B CG  1 
ATOM   5831 O OD1 . ASP B 1 267 ? 93.295 38.140 -61.572 1.00 29.51 ? 267  ASP B OD1 1 
ATOM   5832 O OD2 . ASP B 1 267 ? 93.774 37.345 -59.596 1.00 31.46 ? 267  ASP B OD2 1 
ATOM   5833 N N   . ARG B 1 268 ? 90.434 33.686 -62.224 1.00 11.91 ? 268  ARG B N   1 
ATOM   5834 C CA  . ARG B 1 268 ? 90.085 32.407 -62.886 1.00 12.01 ? 268  ARG B CA  1 
ATOM   5835 C C   . ARG B 1 268 ? 88.628 32.399 -63.388 1.00 11.85 ? 268  ARG B C   1 
ATOM   5836 O O   . ARG B 1 268 ? 87.978 31.377 -63.250 1.00 9.38  ? 268  ARG B O   1 
ATOM   5837 C CB  . ARG B 1 268 ? 90.451 31.225 -61.995 1.00 10.90 ? 268  ARG B CB  1 
ATOM   5838 C CG  . ARG B 1 268 ? 91.944 30.998 -61.830 1.00 15.74 ? 268  ARG B CG  1 
ATOM   5839 C CD  . ARG B 1 268 ? 92.152 29.623 -61.238 1.00 12.85 ? 268  ARG B CD  1 
ATOM   5840 N NE  . ARG B 1 268 ? 93.540 29.256 -61.033 1.00 14.98 ? 268  ARG B NE  1 
ATOM   5841 C CZ  . ARG B 1 268 ? 94.261 29.600 -59.977 1.00 19.73 ? 268  ARG B CZ  1 
ATOM   5842 N NH1 . ARG B 1 268 ? 93.738 30.362 -59.031 1.00 13.23 ? 268  ARG B NH1 1 
ATOM   5843 N NH2 . ARG B 1 268 ? 95.509 29.189 -59.878 1.00 17.21 ? 268  ARG B NH2 1 
ATOM   5844 N N   . ILE B 1 269 ? 88.161 33.514 -63.949 1.00 11.35 ? 269  ILE B N   1 
ATOM   5845 C CA  . ILE B 1 269 ? 86.871 33.522 -64.634 1.00 10.85 ? 269  ILE B CA  1 
ATOM   5846 C C   . ILE B 1 269 ? 86.993 34.359 -65.898 1.00 12.64 ? 269  ILE B C   1 
ATOM   5847 O O   . ILE B 1 269 ? 87.735 35.344 -65.949 1.00 11.48 ? 269  ILE B O   1 
ATOM   5848 C CB  . ILE B 1 269 ? 85.711 34.064 -63.758 1.00 10.89 ? 269  ILE B CB  1 
ATOM   5849 C CG1 . ILE B 1 269 ? 85.997 35.487 -63.286 1.00 12.33 ? 269  ILE B CG1 1 
ATOM   5850 C CG2 . ILE B 1 269 ? 85.402 33.139 -62.579 1.00 9.64  ? 269  ILE B CG2 1 
ATOM   5851 C CD1 . ILE B 1 269 ? 84.784 36.125 -62.608 1.00 15.00 ? 269  ILE B CD1 1 
ATOM   5852 N N   . ASP B 1 270 ? 86.245 33.968 -66.921 1.00 12.14 ? 270  ASP B N   1 
ATOM   5853 C CA  . ASP B 1 270 ? 86.201 34.753 -68.146 1.00 15.35 ? 270  ASP B CA  1 
ATOM   5854 C C   . ASP B 1 270 ? 85.081 35.788 -68.137 1.00 13.89 ? 270  ASP B C   1 
ATOM   5855 O O   . ASP B 1 270 ? 85.087 36.702 -68.972 1.00 14.11 ? 270  ASP B O   1 
ATOM   5856 C CB  . ASP B 1 270 ? 86.060 33.813 -69.343 1.00 12.51 ? 270  ASP B CB  1 
ATOM   5857 C CG  . ASP B 1 270 ? 87.245 32.870 -69.471 1.00 17.37 ? 270  ASP B CG  1 
ATOM   5858 O OD1 . ASP B 1 270 ? 88.360 33.279 -69.058 1.00 13.06 ? 270  ASP B OD1 1 
ATOM   5859 O OD2 . ASP B 1 270 ? 87.060 31.723 -69.955 1.00 13.45 ? 270  ASP B OD2 1 
ATOM   5860 N N   . PHE B 1 271 ? 84.132 35.665 -67.212 1.00 10.49 ? 271  PHE B N   1 
ATOM   5861 C CA  . PHE B 1 271 ? 83.033 36.607 -67.050 1.00 12.12 ? 271  PHE B CA  1 
ATOM   5862 C C   . PHE B 1 271 ? 82.432 36.350 -65.680 1.00 11.82 ? 271  PHE B C   1 
ATOM   5863 O O   . PHE B 1 271 ? 82.583 35.263 -65.114 1.00 11.24 ? 271  PHE B O   1 
ATOM   5864 C CB  . PHE B 1 271 ? 81.964 36.465 -68.156 1.00 10.49 ? 271  PHE B CB  1 
ATOM   5865 C CG  . PHE B 1 271 ? 81.316 35.092 -68.231 1.00 9.78  ? 271  PHE B CG  1 
ATOM   5866 C CD1 . PHE B 1 271 ? 80.203 34.786 -67.465 1.00 13.06 ? 271  PHE B CD1 1 
ATOM   5867 C CD2 . PHE B 1 271 ? 81.827 34.113 -69.072 1.00 12.28 ? 271  PHE B CD2 1 
ATOM   5868 C CE1 . PHE B 1 271 ? 79.603 33.518 -67.528 1.00 10.74 ? 271  PHE B CE1 1 
ATOM   5869 C CE2 . PHE B 1 271 ? 81.238 32.845 -69.145 1.00 11.51 ? 271  PHE B CE2 1 
ATOM   5870 C CZ  . PHE B 1 271 ? 80.118 32.550 -68.365 1.00 12.57 ? 271  PHE B CZ  1 
ATOM   5871 N N   . LEU B 1 272 ? 81.756 37.361 -65.149 1.00 10.36 ? 272  LEU B N   1 
ATOM   5872 C CA  . LEU B 1 272 ? 81.091 37.268 -63.856 1.00 11.46 ? 272  LEU B CA  1 
ATOM   5873 C C   . LEU B 1 272 ? 79.584 37.376 -64.064 1.00 11.60 ? 272  LEU B C   1 
ATOM   5874 O O   . LEU B 1 272 ? 79.100 38.361 -64.636 1.00 11.81 ? 272  LEU B O   1 
ATOM   5875 C CB  . LEU B 1 272 ? 81.590 38.365 -62.910 1.00 9.89  ? 272  LEU B CB  1 
ATOM   5876 C CG  . LEU B 1 272 ? 80.823 38.448 -61.577 1.00 11.57 ? 272  LEU B CG  1 
ATOM   5877 C CD1 . LEU B 1 272 ? 80.898 37.142 -60.790 1.00 9.42  ? 272  LEU B CD1 1 
ATOM   5878 C CD2 . LEU B 1 272 ? 81.308 39.616 -60.733 1.00 12.68 ? 272  LEU B CD2 1 
ATOM   5879 N N   . GLY B 1 273 ? 78.854 36.354 -63.626 1.00 10.36 ? 273  GLY B N   1 
ATOM   5880 C CA  . GLY B 1 273 ? 77.409 36.393 -63.624 1.00 10.77 ? 273  GLY B CA  1 
ATOM   5881 C C   . GLY B 1 273 ? 76.901 36.929 -62.302 1.00 12.93 ? 273  GLY B C   1 
ATOM   5882 O O   . GLY B 1 273 ? 77.179 36.357 -61.237 1.00 10.64 ? 273  GLY B O   1 
ATOM   5883 N N   . VAL B 1 274 ? 76.178 38.042 -62.368 1.00 8.31  ? 274  VAL B N   1 
ATOM   5884 C CA  . VAL B 1 274 ? 75.636 38.737 -61.203 1.00 9.87  ? 274  VAL B CA  1 
ATOM   5885 C C   . VAL B 1 274 ? 74.186 38.312 -61.013 1.00 9.74  ? 274  VAL B C   1 
ATOM   5886 O O   . VAL B 1 274 ? 73.349 38.544 -61.894 1.00 9.30  ? 274  VAL B O   1 
ATOM   5887 C CB  . VAL B 1 274 ? 75.741 40.258 -61.395 1.00 14.82 ? 274  VAL B CB  1 
ATOM   5888 C CG1 . VAL B 1 274 ? 74.880 41.007 -60.383 1.00 14.88 ? 274  VAL B CG1 1 
ATOM   5889 C CG2 . VAL B 1 274 ? 77.203 40.699 -61.318 1.00 13.64 ? 274  VAL B CG2 1 
ATOM   5890 N N   . ASN B 1 275 ? 73.887 37.674 -59.880 1.00 8.58  ? 275  ASN B N   1 
ATOM   5891 C CA  . ASN B 1 275 ? 72.518 37.351 -59.472 1.00 11.78 ? 275  ASN B CA  1 
ATOM   5892 C C   . ASN B 1 275 ? 72.062 38.392 -58.457 1.00 13.32 ? 275  ASN B C   1 
ATOM   5893 O O   . ASN B 1 275 ? 72.675 38.526 -57.390 1.00 11.78 ? 275  ASN B O   1 
ATOM   5894 C CB  . ASN B 1 275 ? 72.429 35.963 -58.838 1.00 10.73 ? 275  ASN B CB  1 
ATOM   5895 C CG  . ASN B 1 275 ? 72.549 34.842 -59.845 1.00 10.81 ? 275  ASN B CG  1 
ATOM   5896 O OD1 . ASN B 1 275 ? 72.756 35.069 -61.046 1.00 8.03  ? 275  ASN B OD1 1 
ATOM   5897 N ND2 . ASN B 1 275 ? 72.380 33.613 -59.365 1.00 8.68  ? 275  ASN B ND2 1 
ATOM   5898 N N   . TYR B 1 276 ? 70.989 39.118 -58.776 1.00 11.27 ? 276  TYR B N   1 
ATOM   5899 C CA  . TYR B 1 276 ? 70.526 40.198 -57.914 1.00 11.51 ? 276  TYR B CA  1 
ATOM   5900 C C   . TYR B 1 276 ? 69.009 40.175 -57.796 1.00 10.76 ? 276  TYR B C   1 
ATOM   5901 O O   . TYR B 1 276 ? 68.309 40.138 -58.814 1.00 7.67  ? 276  TYR B O   1 
ATOM   5902 C CB  . TYR B 1 276 ? 70.974 41.564 -58.446 1.00 11.61 ? 276  TYR B CB  1 
ATOM   5903 C CG  . TYR B 1 276 ? 70.368 42.691 -57.653 1.00 11.18 ? 276  TYR B CG  1 
ATOM   5904 C CD1 . TYR B 1 276 ? 70.939 43.097 -56.464 1.00 10.55 ? 276  TYR B CD1 1 
ATOM   5905 C CD2 . TYR B 1 276 ? 69.195 43.313 -58.073 1.00 11.58 ? 276  TYR B CD2 1 
ATOM   5906 C CE1 . TYR B 1 276 ? 70.382 44.112 -55.714 1.00 11.66 ? 276  TYR B CE1 1 
ATOM   5907 C CE2 . TYR B 1 276 ? 68.627 44.324 -57.338 1.00 11.29 ? 276  TYR B CE2 1 
ATOM   5908 C CZ  . TYR B 1 276 ? 69.227 44.716 -56.154 1.00 12.05 ? 276  TYR B CZ  1 
ATOM   5909 O OH  . TYR B 1 276 ? 68.673 45.710 -55.396 1.00 10.36 ? 276  TYR B OH  1 
ATOM   5910 N N   . TYR B 1 277 ? 68.507 40.231 -56.558 1.00 10.05 ? 277  TYR B N   1 
ATOM   5911 C CA  . TYR B 1 277 ? 67.069 40.278 -56.289 1.00 11.36 ? 277  TYR B CA  1 
ATOM   5912 C C   . TYR B 1 277 ? 66.621 41.497 -55.497 1.00 11.58 ? 277  TYR B C   1 
ATOM   5913 O O   . TYR B 1 277 ? 65.593 42.089 -55.830 1.00 10.45 ? 277  TYR B O   1 
ATOM   5914 C CB  . TYR B 1 277 ? 66.629 39.010 -55.546 1.00 9.34  ? 277  TYR B CB  1 
ATOM   5915 C CG  . TYR B 1 277 ? 66.675 37.807 -56.450 1.00 12.17 ? 277  TYR B CG  1 
ATOM   5916 C CD1 . TYR B 1 277 ? 65.570 37.455 -57.226 1.00 10.44 ? 277  TYR B CD1 1 
ATOM   5917 C CD2 . TYR B 1 277 ? 67.836 37.043 -56.561 1.00 12.92 ? 277  TYR B CD2 1 
ATOM   5918 C CE1 . TYR B 1 277 ? 65.611 36.354 -58.077 1.00 10.30 ? 277  TYR B CE1 1 
ATOM   5919 C CE2 . TYR B 1 277 ? 67.891 35.935 -57.413 1.00 9.96  ? 277  TYR B CE2 1 
ATOM   5920 C CZ  . TYR B 1 277 ? 66.777 35.596 -58.159 1.00 11.62 ? 277  TYR B CZ  1 
ATOM   5921 O OH  . TYR B 1 277 ? 66.823 34.504 -58.996 1.00 9.51  ? 277  TYR B OH  1 
ATOM   5922 N N   . THR B 1 278 ? 67.356 41.894 -54.463 1.00 9.66  ? 278  THR B N   1 
ATOM   5923 C CA  . THR B 1 278 ? 66.940 43.003 -53.606 1.00 10.18 ? 278  THR B CA  1 
ATOM   5924 C C   . THR B 1 278 ? 68.158 43.460 -52.811 1.00 12.52 ? 278  THR B C   1 
ATOM   5925 O O   . THR B 1 278 ? 69.231 42.855 -52.887 1.00 12.51 ? 278  THR B O   1 
ATOM   5926 C CB  . THR B 1 278 ? 65.770 42.593 -52.690 1.00 11.02 ? 278  THR B CB  1 
ATOM   5927 O OG1 . THR B 1 278 ? 65.227 43.754 -52.056 1.00 14.68 ? 278  THR B OG1 1 
ATOM   5928 C CG2 . THR B 1 278 ? 66.212 41.614 -51.619 1.00 12.48 ? 278  THR B CG2 1 
ATOM   5929 N N   . ARG B 1 279 ? 67.985 44.532 -52.035 1.00 11.42 ? 279  ARG B N   1 
ATOM   5930 C CA  . ARG B 1 279 ? 69.058 45.070 -51.215 1.00 8.78  ? 279  ARG B CA  1 
ATOM   5931 C C   . ARG B 1 279 ? 69.033 44.465 -49.806 1.00 14.66 ? 279  ARG B C   1 
ATOM   5932 O O   . ARG B 1 279 ? 68.201 43.619 -49.472 1.00 13.14 ? 279  ARG B O   1 
ATOM   5933 C CB  . ARG B 1 279 ? 68.947 46.596 -51.126 1.00 9.86  ? 279  ARG B CB  1 
ATOM   5934 C CG  . ARG B 1 279 ? 67.612 47.081 -50.534 1.00 9.86  ? 279  ARG B CG  1 
ATOM   5935 C CD  . ARG B 1 279 ? 67.698 48.544 -50.056 1.00 13.63 ? 279  ARG B CD  1 
ATOM   5936 N NE  . ARG B 1 279 ? 66.389 49.060 -49.677 1.00 12.86 ? 279  ARG B NE  1 
ATOM   5937 C CZ  . ARG B 1 279 ? 66.121 50.340 -49.450 1.00 19.05 ? 279  ARG B CZ  1 
ATOM   5938 N NH1 . ARG B 1 279 ? 67.066 51.268 -49.510 1.00 10.85 ? 279  ARG B NH1 1 
ATOM   5939 N NH2 . ARG B 1 279 ? 64.873 50.697 -49.151 1.00 15.03 ? 279  ARG B NH2 1 
ATOM   5940 N N   . ALA B 1 280 ? 69.953 44.930 -48.959 1.00 12.34 ? 280  ALA B N   1 
ATOM   5941 C CA  . ALA B 1 280 ? 69.964 44.596 -47.540 1.00 13.44 ? 280  ALA B CA  1 
ATOM   5942 C C   . ALA B 1 280 ? 70.423 45.815 -46.758 1.00 14.10 ? 280  ALA B C   1 
ATOM   5943 O O   . ALA B 1 280 ? 71.281 46.570 -47.222 1.00 16.02 ? 280  ALA B O   1 
ATOM   5944 C CB  . ALA B 1 280 ? 70.887 43.399 -47.246 1.00 16.32 ? 280  ALA B CB  1 
ATOM   5945 N N   . ILE B 1 281 ? 69.852 46.007 -45.574 1.00 14.81 ? 281  ILE B N   1 
ATOM   5946 C CA  . ILE B 1 281 ? 70.184 47.128 -44.701 1.00 15.05 ? 281  ILE B CA  1 
ATOM   5947 C C   . ILE B 1 281 ? 70.884 46.565 -43.474 1.00 16.83 ? 281  ILE B C   1 
ATOM   5948 O O   . ILE B 1 281 ? 70.380 45.625 -42.849 1.00 18.30 ? 281  ILE B O   1 
ATOM   5949 C CB  . ILE B 1 281 ? 68.928 47.921 -44.300 1.00 15.95 ? 281  ILE B CB  1 
ATOM   5950 C CG1 . ILE B 1 281 ? 68.179 48.419 -45.540 1.00 15.46 ? 281  ILE B CG1 1 
ATOM   5951 C CG2 . ILE B 1 281 ? 69.302 49.090 -43.396 1.00 16.91 ? 281  ILE B CG2 1 
ATOM   5952 C CD1 . ILE B 1 281 ? 68.945 49.411 -46.376 1.00 16.16 ? 281  ILE B CD1 1 
ATOM   5953 N N   . VAL B 1 282 ? 72.050 47.113 -43.139 1.00 16.48 ? 282  VAL B N   1 
ATOM   5954 C CA  . VAL B 1 282 ? 72.826 46.582 -42.026 1.00 19.39 ? 282  VAL B CA  1 
ATOM   5955 C C   . VAL B 1 282 ? 73.074 47.686 -41.006 1.00 16.60 ? 282  VAL B C   1 
ATOM   5956 O O   . VAL B 1 282 ? 73.042 48.882 -41.314 1.00 17.37 ? 282  VAL B O   1 
ATOM   5957 C CB  . VAL B 1 282 ? 74.174 45.963 -42.467 1.00 21.03 ? 282  VAL B CB  1 
ATOM   5958 C CG1 . VAL B 1 282 ? 73.975 44.924 -43.566 1.00 19.49 ? 282  VAL B CG1 1 
ATOM   5959 C CG2 . VAL B 1 282 ? 75.159 47.040 -42.882 1.00 19.04 ? 282  VAL B CG2 1 
ATOM   5960 N N   . LYS B 1 283 ? 73.359 47.239 -39.789 1.00 16.53 ? 283  LYS B N   1 
ATOM   5961 C CA  . LYS B 1 283 ? 73.732 48.175 -38.704 1.00 22.85 ? 283  LYS B CA  1 
ATOM   5962 C C   . LYS B 1 283 ? 74.826 47.505 -37.873 1.00 19.85 ? 283  LYS B C   1 
ATOM   5963 O O   . LYS B 1 283 ? 74.757 46.287 -37.670 1.00 16.88 ? 283  LYS B O   1 
ATOM   5964 C CB  . LYS B 1 283 ? 72.541 48.545 -37.821 1.00 24.30 ? 283  LYS B CB  1 
ATOM   5965 C CG  . LYS B 1 283 ? 71.800 47.396 -37.165 1.00 29.71 ? 283  LYS B CG  1 
ATOM   5966 C CD  . LYS B 1 283 ? 70.573 47.885 -36.434 1.00 34.31 ? 283  LYS B CD  1 
ATOM   5967 C CE  . LYS B 1 283 ? 70.751 47.919 -34.933 1.00 44.65 ? 283  LYS B CE  1 
ATOM   5968 N NZ  . LYS B 1 283 ? 71.718 48.960 -34.517 1.00 52.44 ? 283  LYS B NZ  1 
ATOM   5969 N N   . ARG B 1 284 ? 75.773 48.298 -37.413 1.00 18.37 ? 284  ARG B N   1 
ATOM   5970 C CA  . ARG B 1 284 ? 76.872 47.775 -36.582 1.00 22.71 ? 284  ARG B CA  1 
ATOM   5971 C C   . ARG B 1 284 ? 76.305 47.092 -35.333 1.00 21.44 ? 284  ARG B C   1 
ATOM   5972 O O   . ARG B 1 284 ? 75.291 47.538 -34.827 1.00 22.25 ? 284  ARG B O   1 
ATOM   5973 C CB  . ARG B 1 284 ? 77.844 48.909 -36.237 1.00 24.08 ? 284  ARG B CB  1 
ATOM   5974 C CG  . ARG B 1 284 ? 79.093 48.450 -35.501 1.00 27.96 ? 284  ARG B CG  1 
ATOM   5975 C CD  . ARG B 1 284 ? 80.279 49.336 -35.813 1.00 30.88 ? 284  ARG B CD  1 
ATOM   5976 N NE  . ARG B 1 284 ? 80.978 48.871 -36.998 1.00 37.85 ? 284  ARG B NE  1 
ATOM   5977 C CZ  . ARG B 1 284 ? 81.314 49.640 -38.022 1.00 42.49 ? 284  ARG B CZ  1 
ATOM   5978 N NH1 . ARG B 1 284 ? 81.022 50.929 -38.000 1.00 44.97 ? 284  ARG B NH1 1 
ATOM   5979 N NH2 . ARG B 1 284 ? 81.941 49.122 -39.062 1.00 38.29 ? 284  ARG B NH2 1 
ATOM   5980 N N   . THR B 1 285 ? 76.932 46.004 -34.915 1.00 22.75 ? 285  THR B N   1 
ATOM   5981 C CA  . THR B 1 285 ? 76.543 45.299 -33.673 1.00 24.21 ? 285  THR B CA  1 
ATOM   5982 C C   . THR B 1 285 ? 77.522 45.728 -32.570 1.00 23.42 ? 285  THR B C   1 
ATOM   5983 O O   . THR B 1 285 ? 78.624 46.141 -32.908 1.00 22.81 ? 285  THR B O   1 
ATOM   5984 C CB  . THR B 1 285 ? 76.594 43.783 -33.905 1.00 23.39 ? 285  THR B CB  1 
ATOM   5985 O OG1 . THR B 1 285 ? 77.901 43.432 -34.353 1.00 22.53 ? 285  THR B OG1 1 
ATOM   5986 C CG2 . THR B 1 285 ? 75.556 43.309 -34.897 1.00 24.42 ? 285  THR B CG2 1 
ATOM   5987 N N   . PRO B 1 286 ? 77.202 45.589 -31.266 1.00 31.81 ? 286  PRO B N   1 
ATOM   5988 C CA  . PRO B 1 286 ? 78.178 45.953 -30.227 1.00 32.87 ? 286  PRO B CA  1 
ATOM   5989 C C   . PRO B 1 286 ? 79.388 45.030 -30.188 1.00 32.18 ? 286  PRO B C   1 
ATOM   5990 O O   . PRO B 1 286 ? 80.487 45.485 -29.854 1.00 36.45 ? 286  PRO B O   1 
ATOM   5991 C CB  . PRO B 1 286 ? 77.355 45.870 -28.933 1.00 36.02 ? 286  PRO B CB  1 
ATOM   5992 C CG  . PRO B 1 286 ? 76.265 44.877 -29.243 1.00 36.04 ? 286  PRO B CG  1 
ATOM   5993 C CD  . PRO B 1 286 ? 75.928 45.107 -30.693 1.00 34.39 ? 286  PRO B CD  1 
ATOM   5994 N N   . SER B 1 287 ? 79.229 43.759 -30.546 1.00 29.47 ? 287  SER B N   1 
ATOM   5995 C CA  . SER B 1 287 ? 80.279 42.760 -30.427 1.00 28.60 ? 287  SER B CA  1 
ATOM   5996 C C   . SER B 1 287 ? 80.785 42.348 -31.806 1.00 27.63 ? 287  SER B C   1 
ATOM   5997 O O   . SER B 1 287 ? 80.109 42.530 -32.822 1.00 27.01 ? 287  SER B O   1 
ATOM   5998 C CB  . SER B 1 287 ? 79.758 41.530 -29.674 1.00 33.24 ? 287  SER B CB  1 
ATOM   5999 O OG  . SER B 1 287 ? 79.562 41.820 -28.296 1.00 43.23 ? 287  SER B OG  1 
ATOM   6000 N N   . VAL B 1 288 ? 81.995 41.796 -31.834 1.00 22.28 ? 288  VAL B N   1 
ATOM   6001 C CA  . VAL B 1 288 ? 82.582 41.233 -33.043 1.00 21.57 ? 288  VAL B CA  1 
ATOM   6002 C C   . VAL B 1 288 ? 82.592 39.717 -32.895 1.00 20.03 ? 288  VAL B C   1 
ATOM   6003 O O   . VAL B 1 288 ? 83.086 39.187 -31.894 1.00 20.21 ? 288  VAL B O   1 
ATOM   6004 C CB  . VAL B 1 288 ? 84.001 41.776 -33.299 1.00 23.38 ? 288  VAL B CB  1 
ATOM   6005 C CG1 . VAL B 1 288 ? 84.600 41.146 -34.549 1.00 22.58 ? 288  VAL B CG1 1 
ATOM   6006 C CG2 . VAL B 1 288 ? 83.982 43.297 -33.430 1.00 23.18 ? 288  VAL B CG2 1 
ATOM   6007 N N   . LEU B 1 289 ? 82.025 39.023 -33.874 1.00 15.21 ? 289  LEU B N   1 
ATOM   6008 C CA  . LEU B 1 289 ? 82.085 37.570 -33.948 1.00 12.47 ? 289  LEU B CA  1 
ATOM   6009 C C   . LEU B 1 289 ? 83.211 37.171 -34.895 1.00 15.98 ? 289  LEU B C   1 
ATOM   6010 O O   . LEU B 1 289 ? 83.215 37.580 -36.061 1.00 15.27 ? 289  LEU B O   1 
ATOM   6011 C CB  . LEU B 1 289 ? 80.759 37.011 -34.451 1.00 15.41 ? 289  LEU B CB  1 
ATOM   6012 C CG  . LEU B 1 289 ? 80.727 35.515 -34.739 1.00 13.47 ? 289  LEU B CG  1 
ATOM   6013 C CD1 . LEU B 1 289 ? 81.227 34.689 -33.541 1.00 14.43 ? 289  LEU B CD1 1 
ATOM   6014 C CD2 . LEU B 1 289 ? 79.324 35.127 -35.182 1.00 14.55 ? 289  LEU B CD2 1 
ATOM   6015 N N   . SER B 1 290 ? 84.140 36.353 -34.414 1.00 17.07 ? 290  SER B N   1 
ATOM   6016 C CA  . SER B 1 290 ? 85.272 35.903 -35.217 1.00 22.50 ? 290  SER B CA  1 
ATOM   6017 C C   . SER B 1 290 ? 85.237 34.392 -35.385 1.00 17.21 ? 290  SER B C   1 
ATOM   6018 O O   . SER B 1 290 ? 84.947 33.665 -34.431 1.00 18.15 ? 290  SER B O   1 
ATOM   6019 C CB  . SER B 1 290 ? 86.602 36.290 -34.559 1.00 23.57 ? 290  SER B CB  1 
ATOM   6020 O OG  . SER B 1 290 ? 86.879 37.658 -34.761 1.00 33.15 ? 290  SER B OG  1 
ATOM   6021 N N   . SER B 1 291 ? 85.558 33.918 -36.586 1.00 15.11 ? 291  SER B N   1 
ATOM   6022 C CA  . SER B 1 291 ? 85.837 32.497 -36.735 1.00 16.83 ? 291  SER B CA  1 
ATOM   6023 C C   . SER B 1 291 ? 87.119 32.142 -35.977 1.00 18.54 ? 291  SER B C   1 
ATOM   6024 O O   . SER B 1 291 ? 87.898 33.015 -35.583 1.00 15.43 ? 291  SER B O   1 
ATOM   6025 C CB  . SER B 1 291 ? 85.972 32.119 -38.214 1.00 15.88 ? 291  SER B CB  1 
ATOM   6026 O OG  . SER B 1 291 ? 87.125 32.716 -38.791 1.00 17.36 ? 291  SER B OG  1 
ATOM   6027 N N   . SER B 1 292 ? 87.329 30.839 -35.766 1.00 16.34 ? 292  SER B N   1 
ATOM   6028 C CA  . SER B 1 292 ? 88.524 30.383 -35.056 1.00 21.73 ? 292  SER B CA  1 
ATOM   6029 C C   . SER B 1 292 ? 89.798 30.806 -35.776 1.00 20.85 ? 292  SER B C   1 
ATOM   6030 O O   . SER B 1 292 ? 90.776 31.203 -35.136 1.00 21.59 ? 292  SER B O   1 
ATOM   6031 C CB  . SER B 1 292 ? 88.500 28.861 -34.891 1.00 21.88 ? 292  SER B CB  1 
ATOM   6032 O OG  . SER B 1 292 ? 87.364 28.457 -34.156 1.00 22.24 ? 292  SER B OG  1 
ATOM   6033 N N   . SER B 1 293 ? 89.808 30.731 -37.102 1.00 16.25 ? 293  SER B N   1 
ATOM   6034 C CA  . SER B 1 293 ? 90.955 31.170 -37.943 1.00 21.09 ? 293  SER B CA  1 
ATOM   6035 C C   . SER B 1 293 ? 91.168 32.683 -37.865 1.00 23.98 ? 293  SER B C   1 
ATOM   6036 O O   . SER B 1 293 ? 92.299 33.121 -38.035 1.00 22.35 ? 293  SER B O   1 
ATOM   6037 C CB  . SER B 1 293 ? 90.686 30.835 -39.373 1.00 22.36 ? 293  SER B CB  1 
ATOM   6038 O OG  . SER B 1 293 ? 89.793 31.757 -39.962 1.00 19.20 ? 293  SER B OG  1 
ATOM   6039 N N   . GLY B 1 294 ? 90.089 33.440 -37.681 1.00 23.83 ? 294  GLY B N   1 
ATOM   6040 C CA  . GLY B 1 294 ? 90.162 34.910 -37.704 1.00 20.90 ? 294  GLY B CA  1 
ATOM   6041 C C   . GLY B 1 294 ? 89.877 35.453 -39.087 1.00 23.64 ? 294  GLY B C   1 
ATOM   6042 O O   . GLY B 1 294 ? 89.806 36.668 -39.223 1.00 28.01 ? 294  GLY B O   1 
ATOM   6043 N N   . ARG B 1 295 ? 89.703 34.577 -40.070 1.00 22.68 ? 295  ARG B N   1 
ATOM   6044 C CA  . ARG B 1 295 ? 89.539 35.031 -41.475 1.00 23.34 ? 295  ARG B CA  1 
ATOM   6045 C C   . ARG B 1 295 ? 88.135 35.607 -41.712 1.00 22.57 ? 295  ARG B C   1 
ATOM   6046 O O   . ARG B 1 295 ? 87.984 36.412 -42.617 1.00 21.42 ? 295  ARG B O   1 
ATOM   6047 C CB  . ARG B 1 295 ? 89.873 33.868 -42.408 1.00 25.60 ? 295  ARG B CB  1 
ATOM   6048 N N   . ILE B 1 296 ? 87.163 35.171 -40.921 1.00 19.29 ? 296  ILE B N   1 
ATOM   6049 C CA  . ILE B 1 296 ? 85.785 35.713 -41.024 1.00 22.47 ? 296  ILE B CA  1 
ATOM   6050 C C   . ILE B 1 296 ? 85.469 36.497 -39.753 1.00 22.38 ? 296  ILE B C   1 
ATOM   6051 O O   . ILE B 1 296 ? 85.600 35.930 -38.671 1.00 23.38 ? 296  ILE B O   1 
ATOM   6052 C CB  . ILE B 1 296 ? 84.748 34.602 -41.283 1.00 22.95 ? 296  ILE B CB  1 
ATOM   6053 C CG1 . ILE B 1 296 ? 84.967 33.913 -42.628 1.00 26.36 ? 296  ILE B CG1 1 
ATOM   6054 C CG2 . ILE B 1 296 ? 83.339 35.155 -41.145 1.00 18.79 ? 296  ILE B CG2 1 
ATOM   6055 C CD1 . ILE B 1 296 ? 85.117 34.874 -43.766 1.00 28.31 ? 296  ILE B CD1 1 
ATOM   6056 N N   . LYS B 1 297 ? 85.079 37.751 -39.916 1.00 18.70 ? 297  LYS B N   1 
ATOM   6057 C CA  . LYS B 1 297 ? 84.706 38.610 -38.804 1.00 22.06 ? 297  LYS B CA  1 
ATOM   6058 C C   . LYS B 1 297 ? 83.361 39.239 -39.123 1.00 22.09 ? 297  LYS B C   1 
ATOM   6059 O O   . LYS B 1 297 ? 83.172 39.786 -40.214 1.00 23.01 ? 297  LYS B O   1 
ATOM   6060 C CB  . LYS B 1 297 ? 85.772 39.680 -38.545 1.00 24.61 ? 297  LYS B CB  1 
ATOM   6061 C CG  . LYS B 1 297 ? 87.113 39.099 -38.078 1.00 30.71 ? 297  LYS B CG  1 
ATOM   6062 C CD  . LYS B 1 297 ? 87.716 39.934 -36.946 1.00 35.05 ? 297  LYS B CD  1 
ATOM   6063 C CE  . LYS B 1 297 ? 89.209 39.666 -36.759 1.00 41.02 ? 297  LYS B CE  1 
ATOM   6064 N NZ  . LYS B 1 297 ? 89.447 38.377 -36.035 1.00 31.71 ? 297  LYS B NZ  1 
ATOM   6065 N N   . ILE B 1 298 ? 82.420 39.131 -38.190 1.00 18.35 ? 298  ILE B N   1 
ATOM   6066 C CA  . ILE B 1 298 ? 81.070 39.645 -38.382 1.00 16.56 ? 298  ILE B CA  1 
ATOM   6067 C C   . ILE B 1 298 ? 80.783 40.646 -37.276 1.00 17.67 ? 298  ILE B C   1 
ATOM   6068 O O   . ILE B 1 298 ? 80.845 40.306 -36.088 1.00 16.12 ? 298  ILE B O   1 
ATOM   6069 C CB  . ILE B 1 298 ? 80.021 38.523 -38.399 1.00 17.29 ? 298  ILE B CB  1 
ATOM   6070 C CG1 . ILE B 1 298 ? 80.256 37.600 -39.603 1.00 18.14 ? 298  ILE B CG1 1 
ATOM   6071 C CG2 . ILE B 1 298 ? 78.603 39.119 -38.415 1.00 18.30 ? 298  ILE B CG2 1 
ATOM   6072 C CD1 . ILE B 1 298 ? 79.532 36.271 -39.519 1.00 18.99 ? 298  ILE B CD1 1 
ATOM   6073 N N   . ASN B 1 299 ? 80.469 41.878 -37.668 1.00 17.23 ? 299  ASN B N   1 
ATOM   6074 C CA  . ASN B 1 299 ? 80.169 42.931 -36.711 1.00 19.44 ? 299  ASN B CA  1 
ATOM   6075 C C   . ASN B 1 299 ? 78.971 43.764 -37.172 1.00 20.03 ? 299  ASN B C   1 
ATOM   6076 O O   . ASN B 1 299 ? 78.895 44.966 -36.895 1.00 17.64 ? 299  ASN B O   1 
ATOM   6077 C CB  . ASN B 1 299 ? 81.404 43.813 -36.470 1.00 22.30 ? 299  ASN B CB  1 
ATOM   6078 C CG  . ASN B 1 299 ? 81.843 44.554 -37.717 1.00 24.17 ? 299  ASN B CG  1 
ATOM   6079 O OD1 . ASN B 1 299 ? 81.659 44.079 -38.838 1.00 28.99 ? 299  ASN B OD1 1 
ATOM   6080 N ND2 . ASN B 1 299 ? 82.439 45.725 -37.527 1.00 38.19 ? 299  ASN B ND2 1 
ATOM   6081 N N   . TRP B 1 300 ? 78.026 43.137 -37.865 1.00 16.92 ? 300  TRP B N   1 
ATOM   6082 C CA  . TRP B 1 300 ? 76.823 43.810 -38.325 1.00 16.64 ? 300  TRP B CA  1 
ATOM   6083 C C   . TRP B 1 300 ? 75.650 42.857 -38.168 1.00 18.76 ? 300  TRP B C   1 
ATOM   6084 O O   . TRP B 1 300 ? 75.826 41.640 -38.061 1.00 15.78 ? 300  TRP B O   1 
ATOM   6085 C CB  . TRP B 1 300 ? 76.938 44.243 -39.798 1.00 17.37 ? 300  TRP B CB  1 
ATOM   6086 C CG  . TRP B 1 300 ? 77.072 43.050 -40.698 1.00 17.13 ? 300  TRP B CG  1 
ATOM   6087 C CD1 . TRP B 1 300 ? 76.062 42.322 -41.266 1.00 19.34 ? 300  TRP B CD1 1 
ATOM   6088 C CD2 . TRP B 1 300 ? 78.290 42.413 -41.082 1.00 16.87 ? 300  TRP B CD2 1 
ATOM   6089 N NE1 . TRP B 1 300 ? 76.580 41.277 -41.992 1.00 17.96 ? 300  TRP B NE1 1 
ATOM   6090 C CE2 . TRP B 1 300 ? 77.948 41.312 -41.898 1.00 20.13 ? 300  TRP B CE2 1 
ATOM   6091 C CE3 . TRP B 1 300 ? 79.641 42.673 -40.830 1.00 18.54 ? 300  TRP B CE3 1 
ATOM   6092 C CZ2 . TRP B 1 300 ? 78.906 40.475 -42.456 1.00 20.73 ? 300  TRP B CZ2 1 
ATOM   6093 C CZ3 . TRP B 1 300 ? 80.595 41.836 -41.387 1.00 18.37 ? 300  TRP B CZ3 1 
ATOM   6094 C CH2 . TRP B 1 300 ? 80.222 40.751 -42.182 1.00 19.92 ? 300  TRP B CH2 1 
ATOM   6095 N N   . SER B 1 301 ? 74.449 43.428 -38.174 1.00 16.54 ? 301  SER B N   1 
ATOM   6096 C CA  . SER B 1 301 ? 73.212 42.670 -38.281 1.00 22.42 ? 301  SER B CA  1 
ATOM   6097 C C   . SER B 1 301 ? 72.399 43.222 -39.445 1.00 23.19 ? 301  SER B C   1 
ATOM   6098 O O   . SER B 1 301 ? 72.612 44.351 -39.891 1.00 18.47 ? 301  SER B O   1 
ATOM   6099 C CB  . SER B 1 301 ? 72.387 42.746 -36.990 1.00 21.98 ? 301  SER B CB  1 
ATOM   6100 O OG  . SER B 1 301 ? 71.927 44.072 -36.786 1.00 25.61 ? 301  SER B OG  1 
ATOM   6101 N N   . PHE B 1 302 ? 71.452 42.419 -39.930 1.00 23.25 ? 302  PHE B N   1 
ATOM   6102 C CA  . PHE B 1 302 ? 70.546 42.848 -40.988 1.00 21.82 ? 302  PHE B CA  1 
ATOM   6103 C C   . PHE B 1 302 ? 69.268 43.427 -40.383 1.00 24.70 ? 302  PHE B C   1 
ATOM   6104 O O   . PHE B 1 302 ? 68.651 42.805 -39.515 1.00 29.83 ? 302  PHE B O   1 
ATOM   6105 C CB  . PHE B 1 302 ? 70.219 41.680 -41.919 1.00 22.18 ? 302  PHE B CB  1 
ATOM   6106 C CG  . PHE B 1 302 ? 71.385 41.237 -42.758 1.00 22.37 ? 302  PHE B CG  1 
ATOM   6107 C CD1 . PHE B 1 302 ? 71.787 41.984 -43.852 1.00 22.97 ? 302  PHE B CD1 1 
ATOM   6108 C CD2 . PHE B 1 302 ? 72.086 40.085 -42.443 1.00 29.85 ? 302  PHE B CD2 1 
ATOM   6109 C CE1 . PHE B 1 302 ? 72.870 41.592 -44.625 1.00 28.44 ? 302  PHE B CE1 1 
ATOM   6110 C CE2 . PHE B 1 302 ? 73.166 39.682 -43.206 1.00 27.08 ? 302  PHE B CE2 1 
ATOM   6111 C CZ  . PHE B 1 302 ? 73.556 40.435 -44.302 1.00 29.25 ? 302  PHE B CZ  1 
ATOM   6112 N N   . VAL B 1 303 ? 68.868 44.605 -40.857 1.00 21.88 ? 303  VAL B N   1 
ATOM   6113 C CA  . VAL B 1 303 ? 67.719 45.333 -40.314 1.00 22.98 ? 303  VAL B CA  1 
ATOM   6114 C C   . VAL B 1 303 ? 66.421 44.833 -40.942 1.00 20.51 ? 303  VAL B C   1 
ATOM   6115 O O   . VAL B 1 303 ? 66.280 44.866 -42.174 1.00 20.25 ? 303  VAL B O   1 
ATOM   6116 C CB  . VAL B 1 303 ? 67.871 46.846 -40.534 1.00 23.87 ? 303  VAL B CB  1 
ATOM   6117 C CG1 . VAL B 1 303 ? 66.707 47.598 -39.871 1.00 24.67 ? 303  VAL B CG1 1 
ATOM   6118 C CG2 . VAL B 1 303 ? 69.230 47.341 -40.013 1.00 22.29 ? 303  VAL B CG2 1 
ATOM   6119 N N   . PRO B 1 304 ? 65.451 44.376 -40.146 1.00 24.40 ? 304  PRO B N   1 
ATOM   6120 C CA  . PRO B 1 304 ? 64.183 43.898 -40.718 1.00 23.44 ? 304  PRO B CA  1 
ATOM   6121 C C   . PRO B 1 304 ? 63.334 45.040 -41.261 1.00 23.70 ? 304  PRO B C   1 
ATOM   6122 O O   . PRO B 1 304 ? 63.449 46.193 -40.836 1.00 21.79 ? 304  PRO B O   1 
ATOM   6123 C CB  . PRO B 1 304 ? 63.490 43.204 -39.536 1.00 26.36 ? 304  PRO B CB  1 
ATOM   6124 C CG  . PRO B 1 304 ? 64.149 43.759 -38.308 1.00 32.02 ? 304  PRO B CG  1 
ATOM   6125 C CD  . PRO B 1 304 ? 65.542 44.152 -38.688 1.00 26.60 ? 304  PRO B CD  1 
ATOM   6126 N N   . GLY B 1 305 ? 62.467 44.705 -42.222 1.00 26.01 ? 305  GLY B N   1 
ATOM   6127 C CA  . GLY B 1 305 ? 61.606 45.685 -42.860 1.00 19.38 ? 305  GLY B CA  1 
ATOM   6128 C C   . GLY B 1 305 ? 62.124 46.242 -44.173 1.00 27.25 ? 305  GLY B C   1 
ATOM   6129 O O   . GLY B 1 305 ? 61.468 47.122 -44.756 1.00 20.60 ? 305  GLY B O   1 
ATOM   6130 N N   . PHE B 1 306 ? 63.287 45.783 -44.640 1.00 22.13 ? 306  PHE B N   1 
ATOM   6131 C CA  . PHE B 1 306 ? 63.865 46.197 -45.915 1.00 20.32 ? 306  PHE B CA  1 
ATOM   6132 C C   . PHE B 1 306 ? 64.423 44.970 -46.626 1.00 18.89 ? 306  PHE B C   1 
ATOM   6133 O O   . PHE B 1 306 ? 64.684 43.938 -46.004 1.00 20.57 ? 306  PHE B O   1 
ATOM   6134 C CB  . PHE B 1 306 ? 65.015 47.204 -45.762 1.00 20.87 ? 306  PHE B CB  1 
ATOM   6135 C CG  . PHE B 1 306 ? 64.709 48.393 -44.887 1.00 22.16 ? 306  PHE B CG  1 
ATOM   6136 C CD1 . PHE B 1 306 ? 64.900 48.326 -43.510 1.00 20.58 ? 306  PHE B CD1 1 
ATOM   6137 C CD2 . PHE B 1 306 ? 64.302 49.600 -45.450 1.00 23.59 ? 306  PHE B CD2 1 
ATOM   6138 C CE1 . PHE B 1 306 ? 64.645 49.434 -42.708 1.00 24.32 ? 306  PHE B CE1 1 
ATOM   6139 C CE2 . PHE B 1 306 ? 64.049 50.713 -44.657 1.00 25.34 ? 306  PHE B CE2 1 
ATOM   6140 C CZ  . PHE B 1 306 ? 64.219 50.630 -43.289 1.00 28.26 ? 306  PHE B CZ  1 
ATOM   6141 N N   . GLY B 1 307 ? 64.648 45.115 -47.932 1.00 19.20 ? 307  GLY B N   1 
ATOM   6142 C CA  . GLY B 1 307 ? 65.307 44.066 -48.694 1.00 16.02 ? 307  GLY B CA  1 
ATOM   6143 C C   . GLY B 1 307 ? 64.599 42.730 -48.563 1.00 19.13 ? 307  GLY B C   1 
ATOM   6144 O O   . GLY B 1 307 ? 63.386 42.613 -48.794 1.00 16.38 ? 307  GLY B O   1 
ATOM   6145 N N   . GLY B 1 308 ? 65.364 41.699 -48.186 1.00 16.87 ? 308  GLY B N   1 
ATOM   6146 C CA  . GLY B 1 308 ? 64.832 40.351 -48.083 1.00 16.69 ? 308  GLY B CA  1 
ATOM   6147 C C   . GLY B 1 308 ? 63.981 40.086 -46.862 1.00 19.35 ? 308  GLY B C   1 
ATOM   6148 O O   . GLY B 1 308 ? 63.449 38.979 -46.725 1.00 22.27 ? 308  GLY B O   1 
ATOM   6149 N N   . SER B 1 309 ? 63.821 41.071 -45.979 1.00 20.04 ? 309  SER B N   1 
ATOM   6150 C CA  . SER B 1 309 ? 63.191 40.877 -44.675 1.00 23.34 ? 309  SER B CA  1 
ATOM   6151 C C   . SER B 1 309 ? 61.937 41.732 -44.524 1.00 23.52 ? 309  SER B C   1 
ATOM   6152 O O   . SER B 1 309 ? 61.705 42.331 -43.474 1.00 24.14 ? 309  SER B O   1 
ATOM   6153 C CB  . SER B 1 309 ? 64.178 41.189 -43.549 1.00 22.30 ? 309  SER B CB  1 
ATOM   6154 O OG  . SER B 1 309 ? 65.481 40.722 -43.876 1.00 31.35 ? 309  SER B OG  1 
ATOM   6155 N N   . CYS B 1 310 ? 61.112 41.814 -45.563 1.00 22.24 ? 310  CYS B N   1 
ATOM   6156 C CA  . CYS B 1 310 ? 59.835 42.505 -45.455 1.00 22.14 ? 310  CYS B CA  1 
ATOM   6157 C C   . CYS B 1 310 ? 58.710 41.500 -45.232 1.00 24.24 ? 310  CYS B C   1 
ATOM   6158 O O   . CYS B 1 310 ? 58.870 40.287 -45.402 1.00 21.81 ? 310  CYS B O   1 
ATOM   6159 C CB  . CYS B 1 310 ? 59.545 43.338 -46.709 1.00 21.10 ? 310  CYS B CB  1 
ATOM   6160 S SG  . CYS B 1 310 ? 60.870 44.433 -47.218 1.00 22.28 ? 310  CYS B SG  1 
ATOM   6161 N N   . GLN B 1 311 ? 57.555 42.025 -44.839 1.00 22.05 ? 311  GLN B N   1 
ATOM   6162 C CA  . GLN B 1 311 ? 56.350 41.213 -44.853 1.00 26.74 ? 311  GLN B CA  1 
ATOM   6163 C C   . GLN B 1 311 ? 55.939 40.926 -46.295 1.00 21.40 ? 311  GLN B C   1 
ATOM   6164 O O   . GLN B 1 311 ? 56.211 41.708 -47.211 1.00 19.55 ? 311  GLN B O   1 
ATOM   6165 C CB  . GLN B 1 311 ? 55.224 41.920 -44.095 1.00 28.30 ? 311  GLN B CB  1 
ATOM   6166 C CG  . GLN B 1 311 ? 55.594 42.257 -42.648 1.00 35.58 ? 311  GLN B CG  1 
ATOM   6167 C CD  . GLN B 1 311 ? 54.559 43.128 -41.960 1.00 46.10 ? 311  GLN B CD  1 
ATOM   6168 O OE1 . GLN B 1 311 ? 53.672 42.623 -41.271 1.00 54.87 ? 311  GLN B OE1 1 
ATOM   6169 N NE2 . GLN B 1 311 ? 54.669 44.444 -42.142 1.00 49.45 ? 311  GLN B NE2 1 
ATOM   6170 N N   . ARG B 1 312 ? 55.287 39.783 -46.488 1.00 18.48 ? 312  ARG B N   1 
ATOM   6171 C CA  . ARG B 1 312 ? 54.848 39.373 -47.817 1.00 20.19 ? 312  ARG B CA  1 
ATOM   6172 C C   . ARG B 1 312 ? 53.740 40.287 -48.335 1.00 21.72 ? 312  ARG B C   1 
ATOM   6173 O O   . ARG B 1 312 ? 52.851 40.694 -47.583 1.00 20.83 ? 312  ARG B O   1 
ATOM   6174 C CB  . ARG B 1 312 ? 54.349 37.930 -47.773 1.00 19.17 ? 312  ARG B CB  1 
ATOM   6175 C CG  . ARG B 1 312 ? 55.376 36.953 -47.200 1.00 22.08 ? 312  ARG B CG  1 
ATOM   6176 C CD  . ARG B 1 312 ? 54.893 35.504 -47.282 1.00 24.04 ? 312  ARG B CD  1 
ATOM   6177 N NE  . ARG B 1 312 ? 55.999 34.573 -47.096 1.00 31.39 ? 312  ARG B NE  1 
ATOM   6178 C CZ  . ARG B 1 312 ? 55.868 33.261 -46.945 1.00 35.83 ? 312  ARG B CZ  1 
ATOM   6179 N NH1 . ARG B 1 312 ? 54.686 32.670 -47.010 1.00 36.76 ? 312  ARG B NH1 1 
ATOM   6180 N NH2 . ARG B 1 312 ? 56.955 32.521 -46.739 1.00 33.66 ? 312  ARG B NH2 1 
ATOM   6181 N N   . ASN B 1 313 ? 53.801 40.609 -49.631 1.00 17.14 ? 313  ASN B N   1 
ATOM   6182 C CA  . ASN B 1 313 ? 52.721 41.310 -50.327 1.00 16.53 ? 313  ASN B CA  1 
ATOM   6183 C C   . ASN B 1 313 ? 52.380 42.617 -49.621 1.00 21.31 ? 313  ASN B C   1 
ATOM   6184 O O   . ASN B 1 313 ? 51.220 42.936 -49.361 1.00 18.28 ? 313  ASN B O   1 
ATOM   6185 C CB  . ASN B 1 313 ? 51.491 40.413 -50.431 1.00 19.93 ? 313  ASN B CB  1 
ATOM   6186 C CG  . ASN B 1 313 ? 51.760 39.173 -51.246 1.00 22.90 ? 313  ASN B CG  1 
ATOM   6187 O OD1 . ASN B 1 313 ? 51.559 38.054 -50.773 1.00 23.01 ? 313  ASN B OD1 1 
ATOM   6188 N ND2 . ASN B 1 313 ? 52.229 39.362 -52.474 1.00 16.63 ? 313  ASN B ND2 1 
ATOM   6189 N N   . SER B 1 314 ? 53.417 43.361 -49.269 1.00 16.07 ? 314  SER B N   1 
ATOM   6190 C CA  . SER B 1 314 ? 53.230 44.534 -48.431 1.00 19.82 ? 314  SER B CA  1 
ATOM   6191 C C   . SER B 1 314 ? 54.118 45.653 -48.950 1.00 23.32 ? 314  SER B C   1 
ATOM   6192 O O   . SER B 1 314 ? 54.322 45.782 -50.164 1.00 16.99 ? 314  SER B O   1 
ATOM   6193 C CB  . SER B 1 314 ? 53.550 44.184 -46.972 1.00 25.19 ? 314  SER B CB  1 
ATOM   6194 O OG  . SER B 1 314 ? 53.143 45.198 -46.069 1.00 28.86 ? 314  SER B OG  1 
ATOM   6195 N N   . LYS B 1 315 ? 54.658 46.453 -48.035 1.00 21.44 ? 315  LYS B N   1 
ATOM   6196 C CA  . LYS B 1 315 ? 55.605 47.504 -48.363 1.00 19.52 ? 315  LYS B CA  1 
ATOM   6197 C C   . LYS B 1 315 ? 56.744 47.441 -47.358 1.00 22.20 ? 315  LYS B C   1 
ATOM   6198 O O   . LYS B 1 315 ? 56.554 47.031 -46.207 1.00 18.48 ? 315  LYS B O   1 
ATOM   6199 C CB  . LYS B 1 315 ? 54.934 48.885 -48.334 1.00 22.14 ? 315  LYS B CB  1 
ATOM   6200 C CG  . LYS B 1 315 ? 53.752 49.003 -49.287 1.00 28.81 ? 315  LYS B CG  1 
ATOM   6201 C CD  . LYS B 1 315 ? 53.568 50.421 -49.793 1.00 38.87 ? 315  LYS B CD  1 
ATOM   6202 C CE  . LYS B 1 315 ? 53.231 51.357 -48.637 1.00 41.38 ? 315  LYS B CE  1 
ATOM   6203 N NZ  . LYS B 1 315 ? 52.140 52.317 -48.983 1.00 42.07 ? 315  LYS B NZ  1 
ATOM   6204 N N   . SER B 1 316 ? 57.937 47.818 -47.810 1.00 20.29 ? 316  SER B N   1 
ATOM   6205 C CA  . SER B 1 316 ? 59.060 47.992 -46.904 1.00 23.39 ? 316  SER B CA  1 
ATOM   6206 C C   . SER B 1 316 ? 58.847 49.238 -46.042 1.00 21.90 ? 316  SER B C   1 
ATOM   6207 O O   . SER B 1 316 ? 57.935 50.038 -46.270 1.00 19.46 ? 316  SER B O   1 
ATOM   6208 C CB  . SER B 1 316 ? 60.360 48.130 -47.686 1.00 20.59 ? 316  SER B CB  1 
ATOM   6209 O OG  . SER B 1 316 ? 60.385 49.370 -48.390 1.00 20.18 ? 316  SER B OG  1 
ATOM   6210 N N   . LEU B 1 317 ? 59.731 49.421 -45.061 1.00 23.86 ? 317  LEU B N   1 
ATOM   6211 C CA  . LEU B 1 317 ? 59.710 50.646 -44.272 1.00 24.49 ? 317  LEU B CA  1 
ATOM   6212 C C   . LEU B 1 317 ? 60.081 51.877 -45.092 1.00 27.37 ? 317  LEU B C   1 
ATOM   6213 O O   . LEU B 1 317 ? 59.896 52.997 -44.610 1.00 32.16 ? 317  LEU B O   1 
ATOM   6214 C CB  . LEU B 1 317 ? 60.642 50.511 -43.062 1.00 23.93 ? 317  LEU B CB  1 
ATOM   6215 C CG  . LEU B 1 317 ? 60.250 49.415 -42.065 1.00 26.71 ? 317  LEU B CG  1 
ATOM   6216 C CD1 . LEU B 1 317 ? 61.247 49.337 -40.907 1.00 29.38 ? 317  LEU B CD1 1 
ATOM   6217 C CD2 . LEU B 1 317 ? 58.817 49.598 -41.557 1.00 29.08 ? 317  LEU B CD2 1 
ATOM   6218 N N   . ASP B 1 318 ? 60.590 51.704 -46.311 1.00 22.68 ? 318  ASP B N   1 
ATOM   6219 C CA  . ASP B 1 318 ? 60.800 52.804 -47.244 1.00 25.51 ? 318  ASP B CA  1 
ATOM   6220 C C   . ASP B 1 318 ? 59.637 53.004 -48.208 1.00 23.74 ? 318  ASP B C   1 
ATOM   6221 O O   . ASP B 1 318 ? 59.767 53.789 -49.152 1.00 29.96 ? 318  ASP B O   1 
ATOM   6222 C CB  . ASP B 1 318 ? 62.086 52.589 -48.051 1.00 25.44 ? 318  ASP B CB  1 
ATOM   6223 C CG  . ASP B 1 318 ? 63.293 53.232 -47.407 1.00 36.33 ? 318  ASP B CG  1 
ATOM   6224 O OD1 . ASP B 1 318 ? 63.161 53.759 -46.275 1.00 36.12 ? 318  ASP B OD1 1 
ATOM   6225 O OD2 . ASP B 1 318 ? 64.370 53.228 -48.044 1.00 40.58 ? 318  ASP B OD2 1 
ATOM   6226 N N   . GLY B 1 319 ? 58.520 52.307 -48.008 1.00 23.56 ? 319  GLY B N   1 
ATOM   6227 C CA  . GLY B 1 319 ? 57.371 52.450 -48.884 1.00 20.59 ? 319  GLY B CA  1 
ATOM   6228 C C   . GLY B 1 319 ? 57.468 51.728 -50.210 1.00 22.33 ? 319  GLY B C   1 
ATOM   6229 O O   . GLY B 1 319 ? 56.613 51.943 -51.076 1.00 23.37 ? 319  GLY B O   1 
ATOM   6230 N N   . ARG B 1 320 ? 58.503 50.867 -50.413 1.00 20.57 ? 320  ARG B N   1 
ATOM   6231 C CA  . ARG B 1 320 ? 58.557 50.201 -51.708 1.00 19.66 ? 320  ARG B CA  1 
ATOM   6232 C C   . ARG B 1 320 ? 57.839 48.855 -51.640 1.00 17.15 ? 320  ARG B C   1 
ATOM   6233 O O   . ARG B 1 320 ? 57.797 48.223 -50.580 1.00 16.98 ? 320  ARG B O   1 
ATOM   6234 C CB  . ARG B 1 320 ? 60.009 49.997 -52.136 1.00 17.05 ? 320  ARG B CB  1 
ATOM   6235 C CG  . ARG B 1 320 ? 60.755 51.302 -52.457 1.00 20.93 ? 320  ARG B CG  1 
ATOM   6236 C CD  . ARG B 1 320 ? 62.267 51.049 -52.459 1.00 21.01 ? 320  ARG B CD  1 
ATOM   6237 N NE  . ARG B 1 320 ? 63.078 52.210 -52.810 1.00 23.27 ? 320  ARG B NE  1 
ATOM   6238 C CZ  . ARG B 1 320 ? 63.486 52.507 -54.037 1.00 26.56 ? 320  ARG B CZ  1 
ATOM   6239 N NH1 . ARG B 1 320 ? 63.111 51.788 -55.088 1.00 25.19 ? 320  ARG B NH1 1 
ATOM   6240 N NH2 . ARG B 1 320 ? 64.301 53.545 -54.215 1.00 30.42 ? 320  ARG B NH2 1 
ATOM   6241 N N   . PRO B 1 321 ? 57.267 48.373 -52.745 1.00 15.55 ? 321  PRO B N   1 
ATOM   6242 C CA  . PRO B 1 321 ? 56.508 47.116 -52.685 1.00 18.16 ? 321  PRO B CA  1 
ATOM   6243 C C   . PRO B 1 321 ? 57.396 45.921 -52.360 1.00 18.58 ? 321  PRO B C   1 
ATOM   6244 O O   . PRO B 1 321 ? 58.582 45.879 -52.709 1.00 13.39 ? 321  PRO B O   1 
ATOM   6245 C CB  . PRO B 1 321 ? 55.905 46.985 -54.094 1.00 16.38 ? 321  PRO B CB  1 
ATOM   6246 C CG  . PRO B 1 321 ? 56.156 48.318 -54.775 1.00 18.13 ? 321  PRO B CG  1 
ATOM   6247 C CD  . PRO B 1 321 ? 57.331 48.927 -54.111 1.00 14.37 ? 321  PRO B CD  1 
ATOM   6248 N N   . SER B 1 322 ? 56.799 44.946 -51.674 1.00 14.04 ? 322  SER B N   1 
ATOM   6249 C CA  . SER B 1 322 ? 57.409 43.656 -51.394 1.00 18.25 ? 322  SER B CA  1 
ATOM   6250 C C   . SER B 1 322 ? 56.519 42.558 -51.973 1.00 16.81 ? 322  SER B C   1 
ATOM   6251 O O   . SER B 1 322 ? 55.288 42.691 -52.015 1.00 17.10 ? 322  SER B O   1 
ATOM   6252 C CB  . SER B 1 322 ? 57.639 43.477 -49.873 1.00 16.42 ? 322  SER B CB  1 
ATOM   6253 O OG  . SER B 1 322 ? 56.411 43.425 -49.155 1.00 22.09 ? 322  SER B OG  1 
ATOM   6254 N N   . THR B 1 323 ? 57.148 41.471 -52.426 1.00 12.09 ? 323  THR B N   1 
ATOM   6255 C CA  . THR B 1 323 ? 56.511 40.498 -53.310 1.00 10.94 ? 323  THR B CA  1 
ATOM   6256 C C   . THR B 1 323 ? 55.932 39.323 -52.512 1.00 15.19 ? 323  THR B C   1 
ATOM   6257 O O   . THR B 1 323 ? 55.773 39.406 -51.292 1.00 12.65 ? 323  THR B O   1 
ATOM   6258 C CB  . THR B 1 323 ? 57.529 40.019 -54.341 1.00 12.95 ? 323  THR B CB  1 
ATOM   6259 O OG1 . THR B 1 323 ? 58.609 39.391 -53.636 1.00 10.09 ? 323  THR B OG1 1 
ATOM   6260 C CG2 . THR B 1 323 ? 58.060 41.187 -55.163 1.00 11.62 ? 323  THR B CG2 1 
ATOM   6261 N N   . ASP B 1 324 ? 55.628 38.205 -53.197 1.00 11.65 ? 324  ASP B N   1 
ATOM   6262 C CA  . ASP B 1 324 ? 55.029 37.050 -52.523 1.00 13.99 ? 324  ASP B CA  1 
ATOM   6263 C C   . ASP B 1 324 ? 55.950 36.455 -51.458 1.00 14.69 ? 324  ASP B C   1 
ATOM   6264 O O   . ASP B 1 324 ? 55.462 35.822 -50.520 1.00 13.36 ? 324  ASP B O   1 
ATOM   6265 C CB  . ASP B 1 324 ? 54.658 35.934 -53.512 1.00 13.52 ? 324  ASP B CB  1 
ATOM   6266 C CG  . ASP B 1 324 ? 53.474 36.284 -54.425 1.00 16.58 ? 324  ASP B CG  1 
ATOM   6267 O OD1 . ASP B 1 324 ? 52.908 37.401 -54.327 1.00 13.97 ? 324  ASP B OD1 1 
ATOM   6268 O OD2 . ASP B 1 324 ? 53.087 35.397 -55.232 1.00 12.04 ? 324  ASP B OD2 1 
ATOM   6269 N N   . ASN B 1 325 ? 57.276 36.602 -51.588 1.00 12.49 ? 325  ASN B N   1 
ATOM   6270 C CA  . ASN B 1 325 ? 58.178 36.102 -50.553 1.00 12.77 ? 325  ASN B CA  1 
ATOM   6271 C C   . ASN B 1 325 ? 58.771 37.220 -49.697 1.00 14.49 ? 325  ASN B C   1 
ATOM   6272 O O   . ASN B 1 325 ? 59.757 36.996 -48.989 1.00 12.00 ? 325  ASN B O   1 
ATOM   6273 C CB  . ASN B 1 325 ? 59.290 35.229 -51.154 1.00 14.87 ? 325  ASN B CB  1 
ATOM   6274 C CG  . ASN B 1 325 ? 60.209 35.990 -52.109 1.00 14.03 ? 325  ASN B CG  1 
ATOM   6275 O OD1 . ASN B 1 325 ? 60.034 37.182 -52.358 1.00 11.05 ? 325  ASN B OD1 1 
ATOM   6276 N ND2 . ASN B 1 325 ? 61.200 35.292 -52.650 1.00 13.44 ? 325  ASN B ND2 1 
ATOM   6277 N N   . GLY B 1 326 ? 58.182 38.413 -49.725 1.00 12.81 ? 326  GLY B N   1 
ATOM   6278 C CA  . GLY B 1 326 ? 58.635 39.473 -48.842 1.00 13.37 ? 326  GLY B CA  1 
ATOM   6279 C C   . GLY B 1 326 ? 59.908 40.178 -49.259 1.00 16.37 ? 326  GLY B C   1 
ATOM   6280 O O   . GLY B 1 326 ? 60.561 40.800 -48.415 1.00 16.34 ? 326  GLY B O   1 
ATOM   6281 N N   . TRP B 1 327 ? 60.286 40.123 -50.533 1.00 11.93 ? 327  TRP B N   1 
ATOM   6282 C CA  . TRP B 1 327 ? 61.504 40.776 -50.999 1.00 11.72 ? 327  TRP B CA  1 
ATOM   6283 C C   . TRP B 1 327 ? 61.159 42.135 -51.598 1.00 13.28 ? 327  TRP B C   1 
ATOM   6284 O O   . TRP B 1 327 ? 60.300 42.234 -52.483 1.00 10.44 ? 327  TRP B O   1 
ATOM   6285 C CB  . TRP B 1 327 ? 62.243 39.904 -52.020 1.00 13.20 ? 327  TRP B CB  1 
ATOM   6286 C CG  . TRP B 1 327 ? 62.809 38.627 -51.430 1.00 11.49 ? 327  TRP B CG  1 
ATOM   6287 C CD1 . TRP B 1 327 ? 62.791 38.251 -50.110 1.00 13.97 ? 327  TRP B CD1 1 
ATOM   6288 C CD2 . TRP B 1 327 ? 63.493 37.576 -52.139 1.00 11.00 ? 327  TRP B CD2 1 
ATOM   6289 N NE1 . TRP B 1 327 ? 63.406 37.020 -49.960 1.00 13.48 ? 327  TRP B NE1 1 
ATOM   6290 C CE2 . TRP B 1 327 ? 63.843 36.587 -51.188 1.00 13.72 ? 327  TRP B CE2 1 
ATOM   6291 C CE3 . TRP B 1 327 ? 63.831 37.369 -53.490 1.00 11.96 ? 327  TRP B CE3 1 
ATOM   6292 C CZ2 . TRP B 1 327 ? 64.517 35.410 -51.542 1.00 14.93 ? 327  TRP B CZ2 1 
ATOM   6293 C CZ3 . TRP B 1 327 ? 64.499 36.198 -53.842 1.00 10.08 ? 327  TRP B CZ3 1 
ATOM   6294 C CH2 . TRP B 1 327 ? 64.827 35.231 -52.871 1.00 11.49 ? 327  TRP B CH2 1 
ATOM   6295 N N   . GLU B 1 328 ? 61.823 43.175 -51.099 1.00 12.00 ? 328  GLU B N   1 
ATOM   6296 C CA  . GLU B 1 328 ? 61.617 44.536 -51.583 1.00 12.91 ? 328  GLU B CA  1 
ATOM   6297 C C   . GLU B 1 328 ? 62.044 44.702 -53.039 1.00 13.44 ? 328  GLU B C   1 
ATOM   6298 O O   . GLU B 1 328 ? 63.101 44.215 -53.458 1.00 11.28 ? 328  GLU B O   1 
ATOM   6299 C CB  . GLU B 1 328 ? 62.423 45.499 -50.708 1.00 12.19 ? 328  GLU B CB  1 
ATOM   6300 C CG  . GLU B 1 328 ? 62.169 46.963 -50.930 1.00 11.96 ? 328  GLU B CG  1 
ATOM   6301 C CD  . GLU B 1 328 ? 63.102 47.816 -50.061 1.00 17.16 ? 328  GLU B CD  1 
ATOM   6302 O OE1 . GLU B 1 328 ? 64.196 47.331 -49.695 1.00 16.75 ? 328  GLU B OE1 1 
ATOM   6303 O OE2 . GLU B 1 328 ? 62.740 48.956 -49.723 1.00 17.21 ? 328  GLU B OE2 1 
ATOM   6304 N N   . ILE B 1 329 ? 61.249 45.444 -53.803 1.00 12.15 ? 329  ILE B N   1 
ATOM   6305 C CA  . ILE B 1 329 ? 61.639 45.826 -55.160 1.00 12.54 ? 329  ILE B CA  1 
ATOM   6306 C C   . ILE B 1 329 ? 62.545 47.056 -55.072 1.00 16.16 ? 329  ILE B C   1 
ATOM   6307 O O   . ILE B 1 329 ? 62.103 48.146 -54.696 1.00 13.54 ? 329  ILE B O   1 
ATOM   6308 C CB  . ILE B 1 329 ? 60.417 46.087 -56.046 1.00 13.90 ? 329  ILE B CB  1 
ATOM   6309 C CG1 . ILE B 1 329 ? 59.507 44.844 -56.052 1.00 11.22 ? 329  ILE B CG1 1 
ATOM   6310 C CG2 . ILE B 1 329 ? 60.877 46.474 -57.478 1.00 11.70 ? 329  ILE B CG2 1 
ATOM   6311 C CD1 . ILE B 1 329 ? 58.131 45.063 -56.682 1.00 13.24 ? 329  ILE B CD1 1 
ATOM   6312 N N   . TYR B 1 330 ? 63.825 46.881 -55.409 1.00 13.84 ? 330  TYR B N   1 
ATOM   6313 C CA  . TYR B 1 330 ? 64.837 47.928 -55.247 1.00 12.60 ? 330  TYR B CA  1 
ATOM   6314 C C   . TYR B 1 330 ? 65.755 47.921 -56.463 1.00 12.77 ? 330  TYR B C   1 
ATOM   6315 O O   . TYR B 1 330 ? 66.911 47.484 -56.394 1.00 9.90  ? 330  TYR B O   1 
ATOM   6316 C CB  . TYR B 1 330 ? 65.628 47.719 -53.952 1.00 11.61 ? 330  TYR B CB  1 
ATOM   6317 C CG  . TYR B 1 330 ? 66.513 48.894 -53.611 1.00 13.55 ? 330  TYR B CG  1 
ATOM   6318 C CD1 . TYR B 1 330 ? 65.962 50.085 -53.159 1.00 13.88 ? 330  TYR B CD1 1 
ATOM   6319 C CD2 . TYR B 1 330 ? 67.899 48.820 -53.761 1.00 11.50 ? 330  TYR B CD2 1 
ATOM   6320 C CE1 . TYR B 1 330 ? 66.768 51.177 -52.859 1.00 16.43 ? 330  TYR B CE1 1 
ATOM   6321 C CE2 . TYR B 1 330 ? 68.710 49.903 -53.467 1.00 12.30 ? 330  TYR B CE2 1 
ATOM   6322 C CZ  . TYR B 1 330 ? 68.137 51.075 -53.013 1.00 16.64 ? 330  TYR B CZ  1 
ATOM   6323 O OH  . TYR B 1 330 ? 68.943 52.151 -52.723 1.00 14.62 ? 330  TYR B OH  1 
ATOM   6324 N N   . PRO B 1 331 ? 65.260 48.389 -57.612 1.00 13.43 ? 331  PRO B N   1 
ATOM   6325 C CA  . PRO B 1 331 ? 66.017 48.170 -58.857 1.00 14.48 ? 331  PRO B CA  1 
ATOM   6326 C C   . PRO B 1 331 ? 67.312 48.960 -58.919 1.00 13.25 ? 331  PRO B C   1 
ATOM   6327 O O   . PRO B 1 331 ? 68.271 48.486 -59.531 1.00 12.55 ? 331  PRO B O   1 
ATOM   6328 C CB  . PRO B 1 331 ? 65.034 48.581 -59.970 1.00 13.39 ? 331  PRO B CB  1 
ATOM   6329 C CG  . PRO B 1 331 ? 63.837 49.134 -59.305 1.00 17.11 ? 331  PRO B CG  1 
ATOM   6330 C CD  . PRO B 1 331 ? 63.908 48.933 -57.830 1.00 10.41 ? 331  PRO B CD  1 
ATOM   6331 N N   . GLU B 1 332 ? 67.388 50.126 -58.279 1.00 11.95 ? 332  GLU B N   1 
ATOM   6332 C CA  . GLU B 1 332 ? 68.642 50.875 -58.236 1.00 17.20 ? 332  GLU B CA  1 
ATOM   6333 C C   . GLU B 1 332 ? 69.796 50.028 -57.713 1.00 14.83 ? 332  GLU B C   1 
ATOM   6334 O O   . GLU B 1 332 ? 70.945 50.218 -58.132 1.00 12.52 ? 332  GLU B O   1 
ATOM   6335 C CB  . GLU B 1 332 ? 68.460 52.123 -57.362 1.00 21.66 ? 332  GLU B CB  1 
ATOM   6336 C CG  . GLU B 1 332 ? 67.366 53.036 -57.874 1.00 30.37 ? 332  GLU B CG  1 
ATOM   6337 C CD  . GLU B 1 332 ? 66.105 52.959 -57.027 1.00 33.43 ? 332  GLU B CD  1 
ATOM   6338 O OE1 . GLU B 1 332 ? 65.617 54.027 -56.587 1.00 32.96 ? 332  GLU B OE1 1 
ATOM   6339 O OE2 . GLU B 1 332 ? 65.599 51.827 -56.824 1.00 23.19 ? 332  GLU B OE2 1 
ATOM   6340 N N   . GLY B 1 333 ? 69.509 49.089 -56.804 1.00 12.71 ? 333  GLY B N   1 
ATOM   6341 C CA  . GLY B 1 333 ? 70.558 48.235 -56.272 1.00 13.88 ? 333  GLY B CA  1 
ATOM   6342 C C   . GLY B 1 333 ? 71.265 47.409 -57.333 1.00 13.76 ? 333  GLY B C   1 
ATOM   6343 O O   . GLY B 1 333 ? 72.455 47.106 -57.196 1.00 10.87 ? 333  GLY B O   1 
ATOM   6344 N N   . LEU B 1 334 ? 70.559 47.041 -58.406 1.00 10.11 ? 334  LEU B N   1 
ATOM   6345 C CA  . LEU B 1 334 ? 71.221 46.301 -59.476 1.00 13.20 ? 334  LEU B CA  1 
ATOM   6346 C C   . LEU B 1 334 ? 72.304 47.150 -60.129 1.00 12.64 ? 334  LEU B C   1 
ATOM   6347 O O   . LEU B 1 334 ? 73.409 46.664 -60.410 1.00 10.37 ? 334  LEU B O   1 
ATOM   6348 C CB  . LEU B 1 334 ? 70.204 45.839 -60.520 1.00 10.99 ? 334  LEU B CB  1 
ATOM   6349 C CG  . LEU B 1 334 ? 70.756 45.122 -61.766 1.00 11.53 ? 334  LEU B CG  1 
ATOM   6350 C CD1 . LEU B 1 334 ? 71.579 43.884 -61.385 1.00 10.28 ? 334  LEU B CD1 1 
ATOM   6351 C CD2 . LEU B 1 334 ? 69.630 44.755 -62.733 1.00 12.63 ? 334  LEU B CD2 1 
ATOM   6352 N N   . GLY B 1 335 ? 72.008 48.428 -60.365 1.00 12.59 ? 335  GLY B N   1 
ATOM   6353 C CA  . GLY B 1 335 ? 73.015 49.313 -60.922 1.00 14.09 ? 335  GLY B CA  1 
ATOM   6354 C C   . GLY B 1 335 ? 74.159 49.553 -59.957 1.00 13.24 ? 335  GLY B C   1 
ATOM   6355 O O   . GLY B 1 335 ? 75.322 49.591 -60.365 1.00 14.67 ? 335  GLY B O   1 
ATOM   6356 N N   . TYR B 1 336 ? 73.848 49.706 -58.666 1.00 10.92 ? 336  TYR B N   1 
ATOM   6357 C CA  . TYR B 1 336 ? 74.908 49.892 -57.677 1.00 13.28 ? 336  TYR B CA  1 
ATOM   6358 C C   . TYR B 1 336 ? 75.827 48.676 -57.620 1.00 14.08 ? 336  TYR B C   1 
ATOM   6359 O O   . TYR B 1 336 ? 77.051 48.820 -57.566 1.00 12.44 ? 336  TYR B O   1 
ATOM   6360 C CB  . TYR B 1 336 ? 74.314 50.169 -56.297 1.00 12.83 ? 336  TYR B CB  1 
ATOM   6361 C CG  . TYR B 1 336 ? 73.391 51.371 -56.241 1.00 17.67 ? 336  TYR B CG  1 
ATOM   6362 C CD1 . TYR B 1 336 ? 73.504 52.414 -57.164 1.00 20.07 ? 336  TYR B CD1 1 
ATOM   6363 C CD2 . TYR B 1 336 ? 72.424 51.475 -55.254 1.00 17.52 ? 336  TYR B CD2 1 
ATOM   6364 C CE1 . TYR B 1 336 ? 72.658 53.514 -57.111 1.00 20.26 ? 336  TYR B CE1 1 
ATOM   6365 C CE2 . TYR B 1 336 ? 71.574 52.575 -55.192 1.00 14.44 ? 336  TYR B CE2 1 
ATOM   6366 C CZ  . TYR B 1 336 ? 71.700 53.588 -56.119 1.00 22.74 ? 336  TYR B CZ  1 
ATOM   6367 O OH  . TYR B 1 336 ? 70.853 54.670 -56.061 1.00 21.19 ? 336  TYR B OH  1 
ATOM   6368 N N   . VAL B 1 337 ? 75.254 47.471 -57.646 1.00 13.22 ? 337  VAL B N   1 
ATOM   6369 C CA  . VAL B 1 337 ? 76.062 46.250 -57.612 1.00 13.90 ? 337  VAL B CA  1 
ATOM   6370 C C   . VAL B 1 337 ? 76.944 46.153 -58.845 1.00 14.22 ? 337  VAL B C   1 
ATOM   6371 O O   . VAL B 1 337 ? 78.144 45.853 -58.754 1.00 11.85 ? 337  VAL B O   1 
ATOM   6372 C CB  . VAL B 1 337 ? 75.158 45.013 -57.486 1.00 18.16 ? 337  VAL B CB  1 
ATOM   6373 C CG1 . VAL B 1 337 ? 75.875 43.784 -58.024 1.00 21.59 ? 337  VAL B CG1 1 
ATOM   6374 C CG2 . VAL B 1 337 ? 74.795 44.799 -56.059 1.00 19.20 ? 337  VAL B CG2 1 
ATOM   6375 N N   . LEU B 1 338 ? 76.359 46.387 -60.025 1.00 11.67 ? 338  LEU B N   1 
ATOM   6376 C CA  . LEU B 1 338 ? 77.124 46.232 -61.253 1.00 12.02 ? 338  LEU B CA  1 
ATOM   6377 C C   . LEU B 1 338 ? 78.257 47.250 -61.306 1.00 15.54 ? 338  LEU B C   1 
ATOM   6378 O O   . LEU B 1 338 ? 79.388 46.914 -61.679 1.00 13.59 ? 338  LEU B O   1 
ATOM   6379 C CB  . LEU B 1 338 ? 76.203 46.362 -62.474 1.00 12.01 ? 338  LEU B CB  1 
ATOM   6380 C CG  . LEU B 1 338 ? 75.234 45.202 -62.744 1.00 12.01 ? 338  LEU B CG  1 
ATOM   6381 C CD1 . LEU B 1 338 ? 74.230 45.581 -63.819 1.00 11.39 ? 338  LEU B CD1 1 
ATOM   6382 C CD2 . LEU B 1 338 ? 75.984 43.940 -63.161 1.00 8.87  ? 338  LEU B CD2 1 
ATOM   6383 N N   . ARG B 1 339 ? 77.978 48.491 -60.904 1.00 13.53 ? 339  ARG B N   1 
ATOM   6384 C CA  . ARG B 1 339 ? 79.012 49.518 -60.924 1.00 14.99 ? 339  ARG B CA  1 
ATOM   6385 C C   . ARG B 1 339 ? 80.122 49.203 -59.931 1.00 16.90 ? 339  ARG B C   1 
ATOM   6386 O O   . ARG B 1 339 ? 81.301 49.464 -60.208 1.00 16.37 ? 339  ARG B O   1 
ATOM   6387 C CB  . ARG B 1 339 ? 78.395 50.889 -60.643 1.00 16.36 ? 339  ARG B CB  1 
ATOM   6388 C CG  . ARG B 1 339 ? 77.546 51.383 -61.818 1.00 18.39 ? 339  ARG B CG  1 
ATOM   6389 C CD  . ARG B 1 339 ? 76.867 52.734 -61.557 1.00 25.26 ? 339  ARG B CD  1 
ATOM   6390 N NE  . ARG B 1 339 ? 75.759 52.928 -62.491 1.00 25.23 ? 339  ARG B NE  1 
ATOM   6391 C CZ  . ARG B 1 339 ? 74.477 52.945 -62.152 1.00 23.15 ? 339  ARG B CZ  1 
ATOM   6392 N NH1 . ARG B 1 339 ? 74.096 52.934 -60.882 1.00 22.05 ? 339  ARG B NH1 1 
ATOM   6393 N NH2 . ARG B 1 339 ? 73.553 52.999 -63.109 1.00 25.38 ? 339  ARG B NH2 1 
ATOM   6394 N N   . SER B 1 340 ? 79.781 48.622 -58.780 1.00 13.43 ? 340  SER B N   1 
ATOM   6395 C CA  . SER B 1 340 ? 80.845 48.267 -57.851 1.00 16.08 ? 340  SER B CA  1 
ATOM   6396 C C   . SER B 1 340 ? 81.677 47.090 -58.369 1.00 17.73 ? 340  SER B C   1 
ATOM   6397 O O   . SER B 1 340 ? 82.904 47.087 -58.201 1.00 18.11 ? 340  SER B O   1 
ATOM   6398 C CB  . SER B 1 340 ? 80.260 48.018 -56.455 1.00 21.29 ? 340  SER B CB  1 
ATOM   6399 O OG  . SER B 1 340 ? 80.022 46.649 -56.228 1.00 35.92 ? 340  SER B OG  1 
ATOM   6400 N N   . CYS B 1 341 ? 81.063 46.118 -59.059 1.00 15.25 ? 341  CYS B N   1 
ATOM   6401 C CA  . CYS B 1 341 ? 81.860 45.082 -59.721 1.00 17.19 ? 341  CYS B CA  1 
ATOM   6402 C C   . CYS B 1 341 ? 82.730 45.676 -60.825 1.00 17.40 ? 341  CYS B C   1 
ATOM   6403 O O   . CYS B 1 341 ? 83.908 45.315 -60.961 1.00 16.26 ? 341  CYS B O   1 
ATOM   6404 C CB  . CYS B 1 341 ? 80.961 43.992 -60.303 1.00 14.67 ? 341  CYS B CB  1 
ATOM   6405 S SG  . CYS B 1 341 ? 80.109 43.028 -59.050 1.00 15.45 ? 341  CYS B SG  1 
ATOM   6406 N N   . ARG B 1 342 ? 82.164 46.582 -61.627 1.00 13.16 ? 342  ARG B N   1 
ATOM   6407 C CA  . ARG B 1 342 ? 82.964 47.260 -62.645 1.00 18.56 ? 342  ARG B CA  1 
ATOM   6408 C C   . ARG B 1 342 ? 84.163 47.960 -62.021 1.00 17.41 ? 342  ARG B C   1 
ATOM   6409 O O   . ARG B 1 342 ? 85.284 47.865 -62.532 1.00 19.03 ? 342  ARG B O   1 
ATOM   6410 C CB  . ARG B 1 342 ? 82.113 48.271 -63.424 1.00 19.31 ? 342  ARG B CB  1 
ATOM   6411 C CG  . ARG B 1 342 ? 82.903 49.039 -64.489 1.00 19.46 ? 342  ARG B CG  1 
ATOM   6412 C CD  . ARG B 1 342 ? 82.092 50.154 -65.160 1.00 21.44 ? 342  ARG B CD  1 
ATOM   6413 N NE  . ARG B 1 342 ? 82.872 50.816 -66.205 1.00 28.34 ? 342  ARG B NE  1 
ATOM   6414 C CZ  . ARG B 1 342 ? 82.399 51.693 -67.085 1.00 28.79 ? 342  ARG B CZ  1 
ATOM   6415 N NH1 . ARG B 1 342 ? 81.132 52.080 -67.072 1.00 20.96 ? 342  ARG B NH1 1 
ATOM   6416 N NH2 . ARG B 1 342 ? 83.220 52.195 -68.006 1.00 24.68 ? 342  ARG B NH2 1 
ATOM   6417 N N   . ASP B 1 343 ? 83.949 48.651 -60.902 1.00 17.23 ? 343  ASP B N   1 
ATOM   6418 C CA  . ASP B 1 343 ? 85.035 49.404 -60.282 1.00 22.39 ? 343  ASP B CA  1 
ATOM   6419 C C   . ASP B 1 343 ? 86.088 48.480 -59.689 1.00 24.77 ? 343  ASP B C   1 
ATOM   6420 O O   . ASP B 1 343 ? 87.290 48.762 -59.776 1.00 18.46 ? 343  ASP B O   1 
ATOM   6421 C CB  . ASP B 1 343 ? 84.471 50.332 -59.206 1.00 22.27 ? 343  ASP B CB  1 
ATOM   6422 C CG  . ASP B 1 343 ? 83.722 51.529 -59.800 1.00 34.16 ? 343  ASP B CG  1 
ATOM   6423 O OD1 . ASP B 1 343 ? 83.855 51.772 -61.030 1.00 38.36 ? 343  ASP B OD1 1 
ATOM   6424 O OD2 . ASP B 1 343 ? 82.992 52.216 -59.042 1.00 39.21 ? 343  ASP B OD2 1 
ATOM   6425 N N   . ARG B 1 344 ? 85.660 47.370 -59.088 1.00 15.47 ? 344  ARG B N   1 
ATOM   6426 C CA  . ARG B 1 344 ? 86.596 46.510 -58.384 1.00 16.98 ? 344  ARG B CA  1 
ATOM   6427 C C   . ARG B 1 344 ? 87.358 45.595 -59.332 1.00 19.54 ? 344  ARG B C   1 
ATOM   6428 O O   . ARG B 1 344 ? 88.535 45.308 -59.098 1.00 17.39 ? 344  ARG B O   1 
ATOM   6429 C CB  . ARG B 1 344 ? 85.843 45.703 -57.325 1.00 16.85 ? 344  ARG B CB  1 
ATOM   6430 C CG  . ARG B 1 344 ? 86.711 45.109 -56.257 1.00 20.78 ? 344  ARG B CG  1 
ATOM   6431 C CD  . ARG B 1 344 ? 85.867 44.437 -55.172 1.00 20.10 ? 344  ARG B CD  1 
ATOM   6432 N NE  . ARG B 1 344 ? 86.720 43.808 -54.171 1.00 23.30 ? 344  ARG B NE  1 
ATOM   6433 C CZ  . ARG B 1 344 ? 87.059 44.384 -53.028 1.00 22.44 ? 344  ARG B CZ  1 
ATOM   6434 N NH1 . ARG B 1 344 ? 86.629 45.596 -52.715 1.00 15.70 ? 344  ARG B NH1 1 
ATOM   6435 N NH2 . ARG B 1 344 ? 87.845 43.727 -52.177 1.00 23.74 ? 344  ARG B NH2 1 
ATOM   6436 N N   . TYR B 1 345 ? 86.731 45.160 -60.417 1.00 14.97 ? 345  TYR B N   1 
ATOM   6437 C CA  . TYR B 1 345 ? 87.292 44.123 -61.265 1.00 17.10 ? 345  TYR B CA  1 
ATOM   6438 C C   . TYR B 1 345 ? 87.258 44.574 -62.718 1.00 20.17 ? 345  TYR B C   1 
ATOM   6439 O O   . TYR B 1 345 ? 86.423 45.389 -63.119 1.00 22.77 ? 345  TYR B O   1 
ATOM   6440 C CB  . TYR B 1 345 ? 86.513 42.816 -61.123 1.00 14.99 ? 345  TYR B CB  1 
ATOM   6441 C CG  . TYR B 1 345 ? 86.323 42.324 -59.693 1.00 15.34 ? 345  TYR B CG  1 
ATOM   6442 C CD1 . TYR B 1 345 ? 87.421 42.049 -58.880 1.00 15.97 ? 345  TYR B CD1 1 
ATOM   6443 C CD2 . TYR B 1 345 ? 85.055 42.097 -59.176 1.00 13.06 ? 345  TYR B CD2 1 
ATOM   6444 C CE1 . TYR B 1 345 ? 87.264 41.573 -57.593 1.00 14.30 ? 345  TYR B CE1 1 
ATOM   6445 C CE2 . TYR B 1 345 ? 84.881 41.617 -57.867 1.00 11.48 ? 345  TYR B CE2 1 
ATOM   6446 C CZ  . TYR B 1 345 ? 85.994 41.352 -57.089 1.00 13.42 ? 345  TYR B CZ  1 
ATOM   6447 O OH  . TYR B 1 345 ? 85.859 40.874 -55.800 1.00 13.33 ? 345  TYR B OH  1 
ATOM   6448 N N   . LYS B 1 346 ? 88.155 44.016 -63.514 1.00 19.49 ? 346  LYS B N   1 
ATOM   6449 C CA  . LYS B 1 346 ? 88.185 44.289 -64.951 1.00 28.59 ? 346  LYS B CA  1 
ATOM   6450 C C   . LYS B 1 346 ? 87.667 43.018 -65.609 1.00 25.25 ? 346  LYS B C   1 
ATOM   6451 O O   . LYS B 1 346 ? 88.435 42.111 -65.934 1.00 25.83 ? 346  LYS B O   1 
ATOM   6452 C CB  . LYS B 1 346 ? 89.589 44.663 -65.436 1.00 26.70 ? 346  LYS B CB  1 
ATOM   6453 N N   . LYS B 1 347 ? 86.350 42.942 -65.779 1.00 20.50 ? 347  LYS B N   1 
ATOM   6454 C CA  . LYS B 1 347 ? 85.765 41.654 -66.107 1.00 17.72 ? 347  LYS B CA  1 
ATOM   6455 C C   . LYS B 1 347 ? 84.412 41.845 -66.782 1.00 14.69 ? 347  LYS B C   1 
ATOM   6456 O O   . LYS B 1 347 ? 83.578 42.617 -66.287 1.00 15.41 ? 347  LYS B O   1 
ATOM   6457 C CB  . LYS B 1 347 ? 85.644 40.813 -64.826 1.00 17.33 ? 347  LYS B CB  1 
ATOM   6458 C CG  . LYS B 1 347 ? 85.466 39.341 -65.057 1.00 18.82 ? 347  LYS B CG  1 
ATOM   6459 C CD  . LYS B 1 347 ? 86.693 38.744 -65.730 1.00 20.72 ? 347  LYS B CD  1 
ATOM   6460 C CE  . LYS B 1 347 ? 87.930 38.781 -64.850 1.00 18.67 ? 347  LYS B CE  1 
ATOM   6461 N NZ  . LYS B 1 347 ? 88.981 37.875 -65.458 1.00 19.48 ? 347  LYS B NZ  1 
ATOM   6462 N N   . PRO B 1 348 ? 84.164 41.174 -67.908 1.00 13.98 ? 348  PRO B N   1 
ATOM   6463 C CA  . PRO B 1 348 ? 82.841 41.261 -68.541 1.00 13.02 ? 348  PRO B CA  1 
ATOM   6464 C C   . PRO B 1 348 ? 81.751 40.789 -67.582 1.00 16.37 ? 348  PRO B C   1 
ATOM   6465 O O   . PRO B 1 348 ? 81.944 39.845 -66.809 1.00 14.30 ? 348  PRO B O   1 
ATOM   6466 C CB  . PRO B 1 348 ? 82.965 40.333 -69.757 1.00 14.66 ? 348  PRO B CB  1 
ATOM   6467 C CG  . PRO B 1 348 ? 84.464 40.181 -69.989 1.00 17.62 ? 348  PRO B CG  1 
ATOM   6468 C CD  . PRO B 1 348 ? 85.072 40.257 -68.616 1.00 13.52 ? 348  PRO B CD  1 
ATOM   6469 N N   . LEU B 1 349 ? 80.603 41.466 -67.625 1.00 11.95 ? 349  LEU B N   1 
ATOM   6470 C CA  . LEU B 1 349 ? 79.515 41.210 -66.692 1.00 14.79 ? 349  LEU B CA  1 
ATOM   6471 C C   . LEU B 1 349 ? 78.276 40.725 -67.432 1.00 12.60 ? 349  LEU B C   1 
ATOM   6472 O O   . LEU B 1 349 ? 77.997 41.161 -68.556 1.00 13.03 ? 349  LEU B O   1 
ATOM   6473 C CB  . LEU B 1 349 ? 79.168 42.478 -65.885 1.00 12.30 ? 349  LEU B CB  1 
ATOM   6474 C CG  . LEU B 1 349 ? 80.293 43.075 -65.029 1.00 13.97 ? 349  LEU B CG  1 
ATOM   6475 C CD1 . LEU B 1 349 ? 79.829 44.359 -64.355 1.00 16.41 ? 349  LEU B CD1 1 
ATOM   6476 C CD2 . LEU B 1 349 ? 80.771 42.081 -63.995 1.00 12.22 ? 349  LEU B CD2 1 
ATOM   6477 N N   . TYR B 1 350 ? 77.538 39.822 -66.785 1.00 10.91 ? 350  TYR B N   1 
ATOM   6478 C CA  . TYR B 1 350 ? 76.183 39.456 -67.172 1.00 11.30 ? 350  TYR B CA  1 
ATOM   6479 C C   . TYR B 1 350 ? 75.293 39.537 -65.944 1.00 13.96 ? 350  TYR B C   1 
ATOM   6480 O O   . TYR B 1 350 ? 75.715 39.167 -64.841 1.00 9.98  ? 350  TYR B O   1 
ATOM   6481 C CB  . TYR B 1 350 ? 76.087 38.023 -67.744 1.00 10.47 ? 350  TYR B CB  1 
ATOM   6482 C CG  . TYR B 1 350 ? 76.856 37.772 -69.021 1.00 15.15 ? 350  TYR B CG  1 
ATOM   6483 C CD1 . TYR B 1 350 ? 78.243 37.626 -69.008 1.00 17.35 ? 350  TYR B CD1 1 
ATOM   6484 C CD2 . TYR B 1 350 ? 76.190 37.656 -70.245 1.00 12.78 ? 350  TYR B CD2 1 
ATOM   6485 C CE1 . TYR B 1 350 ? 78.952 37.393 -70.185 1.00 17.01 ? 350  TYR B CE1 1 
ATOM   6486 C CE2 . TYR B 1 350 ? 76.883 37.421 -71.419 1.00 15.21 ? 350  TYR B CE2 1 
ATOM   6487 C CZ  . TYR B 1 350 ? 78.266 37.291 -71.382 1.00 21.29 ? 350  TYR B CZ  1 
ATOM   6488 O OH  . TYR B 1 350 ? 78.974 37.058 -72.539 1.00 21.93 ? 350  TYR B OH  1 
ATOM   6489 N N   . VAL B 1 351 ? 74.057 39.995 -66.126 1.00 10.44 ? 351  VAL B N   1 
ATOM   6490 C CA  . VAL B 1 351 ? 73.031 39.733 -65.118 1.00 8.49  ? 351  VAL B CA  1 
ATOM   6491 C C   . VAL B 1 351 ? 72.505 38.329 -65.386 1.00 9.38  ? 351  VAL B C   1 
ATOM   6492 O O   . VAL B 1 351 ? 71.813 38.096 -66.384 1.00 10.32 ? 351  VAL B O   1 
ATOM   6493 C CB  . VAL B 1 351 ? 71.900 40.761 -65.159 1.00 9.29  ? 351  VAL B CB  1 
ATOM   6494 C CG1 . VAL B 1 351 ? 70.820 40.383 -64.131 1.00 9.30  ? 351  VAL B CG1 1 
ATOM   6495 C CG2 . VAL B 1 351 ? 72.451 42.175 -64.914 1.00 8.45  ? 351  VAL B CG2 1 
ATOM   6496 N N   . THR B 1 352 ? 72.846 37.380 -64.513 1.00 8.84  ? 352  THR B N   1 
ATOM   6497 C CA  . THR B 1 352 ? 72.460 36.000 -64.759 1.00 8.15  ? 352  THR B CA  1 
ATOM   6498 C C   . THR B 1 352 ? 71.189 35.595 -64.031 1.00 7.64  ? 352  THR B C   1 
ATOM   6499 O O   . THR B 1 352 ? 70.595 34.580 -64.403 1.00 7.81  ? 352  THR B O   1 
ATOM   6500 C CB  . THR B 1 352 ? 73.609 35.037 -64.404 1.00 8.71  ? 352  THR B CB  1 
ATOM   6501 O OG1 . THR B 1 352 ? 74.284 35.499 -63.230 1.00 8.43  ? 352  THR B OG1 1 
ATOM   6502 C CG2 . THR B 1 352 ? 74.619 34.948 -65.572 1.00 5.78  ? 352  THR B CG2 1 
ATOM   6503 N N   . GLU B 1 353 ? 70.735 36.364 -63.033 1.00 10.74 ? 353  GLU B N   1 
ATOM   6504 C CA  . GLU B 1 353 ? 69.406 36.172 -62.456 1.00 11.27 ? 353  GLU B CA  1 
ATOM   6505 C C   . GLU B 1 353 ? 68.863 37.498 -61.940 1.00 10.05 ? 353  GLU B C   1 
ATOM   6506 O O   . GLU B 1 353 ? 69.597 38.313 -61.372 1.00 9.67  ? 353  GLU B O   1 
ATOM   6507 C CB  . GLU B 1 353 ? 69.363 35.187 -61.277 1.00 9.67  ? 353  GLU B CB  1 
ATOM   6508 C CG  . GLU B 1 353 ? 69.958 33.835 -61.499 1.00 11.45 ? 353  GLU B CG  1 
ATOM   6509 C CD  . GLU B 1 353 ? 69.567 32.818 -60.435 1.00 13.79 ? 353  GLU B CD  1 
ATOM   6510 O OE1 . GLU B 1 353 ? 68.948 33.196 -59.399 1.00 10.84 ? 353  GLU B OE1 1 
ATOM   6511 O OE2 . GLU B 1 353 ? 70.047 31.664 -60.557 1.00 11.80 ? 353  GLU B OE2 1 
ATOM   6512 N N   . ASN B 1 354 ? 67.559 37.673 -62.118 1.00 9.61  ? 354  ASN B N   1 
ATOM   6513 C CA  . ASN B 1 354 ? 66.789 38.774 -61.561 1.00 10.48 ? 354  ASN B CA  1 
ATOM   6514 C C   . ASN B 1 354 ? 65.330 38.383 -61.739 1.00 9.40  ? 354  ASN B C   1 
ATOM   6515 O O   . ASN B 1 354 ? 64.959 37.906 -62.818 1.00 9.90  ? 354  ASN B O   1 
ATOM   6516 C CB  . ASN B 1 354 ? 67.118 40.095 -62.265 1.00 6.88  ? 354  ASN B CB  1 
ATOM   6517 C CG  . ASN B 1 354 ? 66.222 41.241 -61.813 1.00 10.32 ? 354  ASN B CG  1 
ATOM   6518 O OD1 . ASN B 1 354 ? 65.442 41.783 -62.602 1.00 11.07 ? 354  ASN B OD1 1 
ATOM   6519 N ND2 . ASN B 1 354 ? 66.329 41.619 -60.538 1.00 9.86  ? 354  ASN B ND2 1 
ATOM   6520 N N   . GLY B 1 355 ? 64.510 38.529 -60.703 1.00 7.84  ? 355  GLY B N   1 
ATOM   6521 C CA  . GLY B 1 355 ? 63.109 38.173 -60.835 1.00 9.54  ? 355  GLY B CA  1 
ATOM   6522 C C   . GLY B 1 355 ? 62.373 38.384 -59.534 1.00 9.14  ? 355  GLY B C   1 
ATOM   6523 O O   . GLY B 1 355 ? 62.925 38.916 -58.568 1.00 9.76  ? 355  GLY B O   1 
ATOM   6524 N N   . VAL B 1 356 ? 61.113 37.946 -59.514 1.00 7.04  ? 356  VAL B N   1 
ATOM   6525 C CA  . VAL B 1 356 ? 60.252 38.128 -58.351 1.00 7.37  ? 356  VAL B CA  1 
ATOM   6526 C C   . VAL B 1 356 ? 59.350 36.917 -58.160 1.00 9.13  ? 356  VAL B C   1 
ATOM   6527 O O   . VAL B 1 356 ? 58.931 36.262 -59.125 1.00 7.44  ? 356  VAL B O   1 
ATOM   6528 C CB  . VAL B 1 356 ? 59.381 39.401 -58.478 1.00 13.05 ? 356  VAL B CB  1 
ATOM   6529 C CG1 . VAL B 1 356 ? 60.236 40.669 -58.350 1.00 9.91  ? 356  VAL B CG1 1 
ATOM   6530 C CG2 . VAL B 1 356 ? 58.602 39.384 -59.818 1.00 6.92  ? 356  VAL B CG2 1 
ATOM   6531 N N   . ALA B 1 357 ? 59.027 36.645 -56.898 1.00 7.72  ? 357  ALA B N   1 
ATOM   6532 C CA  . ALA B 1 357 ? 57.981 35.685 -56.558 1.00 9.87  ? 357  ALA B CA  1 
ATOM   6533 C C   . ALA B 1 357 ? 56.628 36.385 -56.637 1.00 9.18  ? 357  ALA B C   1 
ATOM   6534 O O   . ALA B 1 357 ? 56.369 37.329 -55.881 1.00 8.97  ? 357  ALA B O   1 
ATOM   6535 C CB  . ALA B 1 357 ? 58.207 35.116 -55.156 1.00 8.11  ? 357  ALA B CB  1 
ATOM   6536 N N   . ASP B 1 358 ? 55.757 35.918 -57.529 1.00 8.78  ? 358  ASP B N   1 
ATOM   6537 C CA  . ASP B 1 358 ? 54.614 36.742 -57.921 1.00 10.24 ? 358  ASP B CA  1 
ATOM   6538 C C   . ASP B 1 358 ? 53.655 35.931 -58.786 1.00 9.53  ? 358  ASP B C   1 
ATOM   6539 O O   . ASP B 1 358 ? 53.789 35.920 -60.007 1.00 9.87  ? 358  ASP B O   1 
ATOM   6540 C CB  . ASP B 1 358 ? 55.118 37.977 -58.679 1.00 7.61  ? 358  ASP B CB  1 
ATOM   6541 C CG  . ASP B 1 358 ? 53.987 38.899 -59.173 1.00 11.71 ? 358  ASP B CG  1 
ATOM   6542 O OD1 . ASP B 1 358 ? 52.832 38.801 -58.705 1.00 9.90  ? 358  ASP B OD1 1 
ATOM   6543 O OD2 . ASP B 1 358 ? 54.264 39.704 -60.081 1.00 10.00 ? 358  ASP B OD2 1 
ATOM   6544 N N   . ASP B 1 359 ? 52.699 35.232 -58.171 1.00 11.84 ? 359  ASP B N   1 
ATOM   6545 C CA  . ASP B 1 359 ? 51.806 34.365 -58.944 1.00 11.94 ? 359  ASP B CA  1 
ATOM   6546 C C   . ASP B 1 359 ? 50.813 35.183 -59.772 1.00 11.15 ? 359  ASP B C   1 
ATOM   6547 O O   . ASP B 1 359 ? 50.502 34.834 -60.920 1.00 10.70 ? 359  ASP B O   1 
ATOM   6548 C CB  . ASP B 1 359 ? 51.072 33.417 -57.990 1.00 9.18  ? 359  ASP B CB  1 
ATOM   6549 C CG  . ASP B 1 359 ? 50.331 32.299 -58.710 1.00 12.93 ? 359  ASP B CG  1 
ATOM   6550 O OD1 . ASP B 1 359 ? 50.553 32.085 -59.918 1.00 11.47 ? 359  ASP B OD1 1 
ATOM   6551 O OD2 . ASP B 1 359 ? 49.495 31.636 -58.065 1.00 10.25 ? 359  ASP B OD2 1 
ATOM   6552 N N   . ARG B 1 360 ? 50.311 36.282 -59.211 1.00 7.57  ? 360  ARG B N   1 
ATOM   6553 C CA  . ARG B 1 360 ? 49.289 37.083 -59.882 1.00 12.31 ? 360  ARG B CA  1 
ATOM   6554 C C   . ARG B 1 360 ? 49.850 37.993 -60.963 1.00 11.26 ? 360  ARG B C   1 
ATOM   6555 O O   . ARG B 1 360 ? 49.056 38.595 -61.695 1.00 12.13 ? 360  ARG B O   1 
ATOM   6556 C CB  . ARG B 1 360 ? 48.540 37.923 -58.842 1.00 11.07 ? 360  ARG B CB  1 
ATOM   6557 C CG  . ARG B 1 360 ? 47.909 37.072 -57.741 1.00 14.52 ? 360  ARG B CG  1 
ATOM   6558 C CD  . ARG B 1 360 ? 46.968 37.870 -56.845 1.00 19.24 ? 360  ARG B CD  1 
ATOM   6559 N NE  . ARG B 1 360 ? 46.160 36.977 -56.021 1.00 30.08 ? 360  ARG B NE  1 
ATOM   6560 C CZ  . ARG B 1 360 ? 45.388 37.365 -55.013 1.00 37.52 ? 360  ARG B CZ  1 
ATOM   6561 N NH1 . ARG B 1 360 ? 45.281 38.643 -54.674 1.00 34.67 ? 360  ARG B NH1 1 
ATOM   6562 N NH2 . ARG B 1 360 ? 44.714 36.446 -54.320 1.00 34.74 ? 360  ARG B NH2 1 
ATOM   6563 N N   . ASP B 1 361 ? 51.182 38.127 -61.057 1.00 7.81  ? 361  ASP B N   1 
ATOM   6564 C CA  . ASP B 1 361 ? 51.855 39.008 -62.020 1.00 10.09 ? 361  ASP B CA  1 
ATOM   6565 C C   . ASP B 1 361 ? 51.594 40.483 -61.710 1.00 10.21 ? 361  ASP B C   1 
ATOM   6566 O O   . ASP B 1 361 ? 51.559 41.328 -62.610 1.00 9.44  ? 361  ASP B O   1 
ATOM   6567 C CB  . ASP B 1 361 ? 51.464 38.679 -63.474 1.00 9.53  ? 361  ASP B CB  1 
ATOM   6568 C CG  . ASP B 1 361 ? 52.597 38.970 -64.472 1.00 10.12 ? 361  ASP B CG  1 
ATOM   6569 O OD1 . ASP B 1 361 ? 53.755 38.568 -64.202 1.00 9.79  ? 361  ASP B OD1 1 
ATOM   6570 O OD2 . ASP B 1 361 ? 52.333 39.571 -65.536 1.00 8.62  ? 361  ASP B OD2 1 
ATOM   6571 N N   . ILE B 1 362 ? 51.411 40.819 -60.430 1.00 9.48  ? 362  ILE B N   1 
ATOM   6572 C CA  . ILE B 1 362 ? 51.164 42.214 -60.075 1.00 10.22 ? 362  ILE B CA  1 
ATOM   6573 C C   . ILE B 1 362 ? 52.449 42.991 -59.817 1.00 12.80 ? 362  ILE B C   1 
ATOM   6574 O O   . ILE B 1 362 ? 52.403 44.228 -59.761 1.00 12.70 ? 362  ILE B O   1 
ATOM   6575 C CB  . ILE B 1 362 ? 50.203 42.306 -58.871 1.00 9.07  ? 362  ILE B CB  1 
ATOM   6576 C CG1 . ILE B 1 362 ? 50.792 41.642 -57.626 1.00 13.31 ? 362  ILE B CG1 1 
ATOM   6577 C CG2 . ILE B 1 362 ? 48.867 41.646 -59.206 1.00 10.26 ? 362  ILE B CG2 1 
ATOM   6578 C CD1 . ILE B 1 362 ? 49.825 41.722 -56.430 1.00 14.37 ? 362  ILE B CD1 1 
ATOM   6579 N N   . TYR B 1 363 ? 53.592 42.312 -59.683 1.00 7.21  ? 363  TYR B N   1 
ATOM   6580 C CA  . TYR B 1 363 ? 54.879 42.956 -59.448 1.00 10.31 ? 363  TYR B CA  1 
ATOM   6581 C C   . TYR B 1 363 ? 55.861 42.787 -60.591 1.00 12.26 ? 363  TYR B C   1 
ATOM   6582 O O   . TYR B 1 363 ? 56.698 43.663 -60.799 1.00 9.47  ? 363  TYR B O   1 
ATOM   6583 C CB  . TYR B 1 363 ? 55.552 42.395 -58.187 1.00 10.93 ? 363  TYR B CB  1 
ATOM   6584 C CG  . TYR B 1 363 ? 54.687 42.337 -56.959 1.00 10.28 ? 363  TYR B CG  1 
ATOM   6585 C CD1 . TYR B 1 363 ? 54.326 43.502 -56.287 1.00 14.38 ? 363  TYR B CD1 1 
ATOM   6586 C CD2 . TYR B 1 363 ? 54.272 41.118 -56.437 1.00 10.50 ? 363  TYR B CD2 1 
ATOM   6587 C CE1 . TYR B 1 363 ? 53.545 43.454 -55.137 1.00 15.15 ? 363  TYR B CE1 1 
ATOM   6588 C CE2 . TYR B 1 363 ? 53.487 41.062 -55.294 1.00 16.80 ? 363  TYR B CE2 1 
ATOM   6589 C CZ  . TYR B 1 363 ? 53.129 42.237 -54.649 1.00 13.73 ? 363  TYR B CZ  1 
ATOM   6590 O OH  . TYR B 1 363 ? 52.362 42.186 -53.507 1.00 17.80 ? 363  TYR B OH  1 
ATOM   6591 N N   . ARG B 1 364 ? 55.778 41.672 -61.319 1.00 8.66  ? 364  ARG B N   1 
ATOM   6592 C CA  . ARG B 1 364 ? 56.798 41.354 -62.314 1.00 10.06 ? 364  ARG B CA  1 
ATOM   6593 C C   . ARG B 1 364 ? 56.855 42.352 -63.470 1.00 9.16  ? 364  ARG B C   1 
ATOM   6594 O O   . ARG B 1 364 ? 57.974 42.727 -63.860 1.00 8.19  ? 364  ARG B O   1 
ATOM   6595 C CB  . ARG B 1 364 ? 56.571 39.920 -62.821 1.00 8.80  ? 364  ARG B CB  1 
ATOM   6596 C CG  . ARG B 1 364 ? 57.708 39.358 -63.687 1.00 7.47  ? 364  ARG B CG  1 
ATOM   6597 C CD  . ARG B 1 364 ? 57.517 37.844 -63.957 1.00 8.08  ? 364  ARG B CD  1 
ATOM   6598 N NE  . ARG B 1 364 ? 57.612 37.033 -62.745 1.00 8.70  ? 364  ARG B NE  1 
ATOM   6599 C CZ  . ARG B 1 364 ? 56.574 36.577 -62.052 1.00 11.08 ? 364  ARG B CZ  1 
ATOM   6600 N NH1 . ARG B 1 364 ? 55.323 36.842 -62.412 1.00 7.13  ? 364  ARG B NH1 1 
ATOM   6601 N NH2 . ARG B 1 364 ? 56.793 35.823 -60.978 1.00 9.46  ? 364  ARG B NH2 1 
ATOM   6602 N N   . PRO B 1 365 ? 55.742 42.805 -64.066 1.00 10.31 ? 365  PRO B N   1 
ATOM   6603 C CA  . PRO B 1 365 ? 55.874 43.816 -65.135 1.00 11.45 ? 365  PRO B CA  1 
ATOM   6604 C C   . PRO B 1 365 ? 56.648 45.039 -64.685 1.00 9.10  ? 365  PRO B C   1 
ATOM   6605 O O   . PRO B 1 365 ? 57.576 45.487 -65.369 1.00 9.66  ? 365  PRO B O   1 
ATOM   6606 C CB  . PRO B 1 365 ? 54.416 44.157 -65.478 1.00 11.75 ? 365  PRO B CB  1 
ATOM   6607 C CG  . PRO B 1 365 ? 53.645 42.938 -65.092 1.00 12.02 ? 365  PRO B CG  1 
ATOM   6608 C CD  . PRO B 1 365 ? 54.339 42.379 -63.877 1.00 8.41  ? 365  PRO B CD  1 
ATOM   6609 N N   . TYR B 1 366 ? 56.296 45.576 -63.525 1.00 9.67  ? 366  TYR B N   1 
ATOM   6610 C CA  . TYR B 1 366 ? 57.001 46.733 -62.988 1.00 12.03 ? 366  TYR B CA  1 
ATOM   6611 C C   . TYR B 1 366 ? 58.467 46.405 -62.719 1.00 11.87 ? 366  TYR B C   1 
ATOM   6612 O O   . TYR B 1 366 ? 59.374 47.143 -63.128 1.00 9.27  ? 366  TYR B O   1 
ATOM   6613 C CB  . TYR B 1 366 ? 56.294 47.202 -61.713 1.00 13.95 ? 366  TYR B CB  1 
ATOM   6614 C CG  . TYR B 1 366 ? 57.097 48.171 -60.875 1.00 17.11 ? 366  TYR B CG  1 
ATOM   6615 C CD1 . TYR B 1 366 ? 57.509 49.395 -61.383 1.00 17.24 ? 366  TYR B CD1 1 
ATOM   6616 C CD2 . TYR B 1 366 ? 57.445 47.851 -59.571 1.00 17.27 ? 366  TYR B CD2 1 
ATOM   6617 C CE1 . TYR B 1 366 ? 58.250 50.280 -60.607 1.00 20.64 ? 366  TYR B CE1 1 
ATOM   6618 C CE2 . TYR B 1 366 ? 58.186 48.717 -58.794 1.00 21.46 ? 366  TYR B CE2 1 
ATOM   6619 C CZ  . TYR B 1 366 ? 58.587 49.930 -59.314 1.00 21.29 ? 366  TYR B CZ  1 
ATOM   6620 O OH  . TYR B 1 366 ? 59.325 50.776 -58.524 1.00 31.32 ? 366  TYR B OH  1 
ATOM   6621 N N   . SER B 1 367 ? 58.718 45.283 -62.048 1.00 10.25 ? 367  SER B N   1 
ATOM   6622 C CA  . SER B 1 367 ? 60.085 44.941 -61.674 1.00 9.02  ? 367  SER B CA  1 
ATOM   6623 C C   . SER B 1 367 ? 60.946 44.636 -62.895 1.00 8.02  ? 367  SER B C   1 
ATOM   6624 O O   . SER B 1 367 ? 62.098 45.077 -62.972 1.00 9.60  ? 367  SER B O   1 
ATOM   6625 C CB  . SER B 1 367 ? 60.062 43.751 -60.715 1.00 10.21 ? 367  SER B CB  1 
ATOM   6626 O OG  . SER B 1 367 ? 61.373 43.305 -60.466 1.00 9.65  ? 367  SER B OG  1 
ATOM   6627 N N   . LEU B 1 368 ? 60.416 43.877 -63.855 1.00 8.52  ? 368  LEU B N   1 
ATOM   6628 C CA  . LEU B 1 368 ? 61.163 43.617 -65.085 1.00 8.60  ? 368  LEU B CA  1 
ATOM   6629 C C   . LEU B 1 368 ? 61.551 44.918 -65.791 1.00 10.95 ? 368  LEU B C   1 
ATOM   6630 O O   . LEU B 1 368 ? 62.718 45.127 -66.154 1.00 9.83  ? 368  LEU B O   1 
ATOM   6631 C CB  . LEU B 1 368 ? 60.327 42.744 -66.018 1.00 10.11 ? 368  LEU B CB  1 
ATOM   6632 C CG  . LEU B 1 368 ? 60.910 42.500 -67.418 1.00 10.99 ? 368  LEU B CG  1 
ATOM   6633 C CD1 . LEU B 1 368 ? 62.085 41.505 -67.375 1.00 8.53  ? 368  LEU B CD1 1 
ATOM   6634 C CD2 . LEU B 1 368 ? 59.818 42.010 -68.339 1.00 10.08 ? 368  LEU B CD2 1 
ATOM   6635 N N   . LEU B 1 369 ? 60.572 45.800 -66.019 1.00 9.69  ? 369  LEU B N   1 
ATOM   6636 C CA  . LEU B 1 369 ? 60.860 47.037 -66.741 1.00 10.16 ? 369  LEU B CA  1 
ATOM   6637 C C   . LEU B 1 369 ? 61.843 47.914 -65.972 1.00 9.04  ? 369  LEU B C   1 
ATOM   6638 O O   . LEU B 1 369 ? 62.786 48.461 -66.555 1.00 8.53  ? 369  LEU B O   1 
ATOM   6639 C CB  . LEU B 1 369 ? 59.563 47.800 -67.020 1.00 7.71  ? 369  LEU B CB  1 
ATOM   6640 C CG  . LEU B 1 369 ? 59.751 49.160 -67.688 1.00 13.13 ? 369  LEU B CG  1 
ATOM   6641 C CD1 . LEU B 1 369 ? 60.558 49.020 -68.983 1.00 9.00  ? 369  LEU B CD1 1 
ATOM   6642 C CD2 . LEU B 1 369 ? 58.397 49.801 -67.948 1.00 11.72 ? 369  LEU B CD2 1 
ATOM   6643 N N   . ALA B 1 370 ? 61.643 48.054 -64.658 1.00 9.08  ? 370  ALA B N   1 
ATOM   6644 C CA  . ALA B 1 370 ? 62.508 48.927 -63.871 1.00 10.68 ? 370  ALA B CA  1 
ATOM   6645 C C   . ALA B 1 370 ? 63.946 48.418 -63.847 1.00 10.68 ? 370  ALA B C   1 
ATOM   6646 O O   . ALA B 1 370 ? 64.896 49.213 -63.926 1.00 10.65 ? 370  ALA B O   1 
ATOM   6647 C CB  . ALA B 1 370 ? 61.961 49.055 -62.447 1.00 9.37  ? 370  ALA B CB  1 
ATOM   6648 N N   . HIS B 1 371 ? 64.137 47.095 -63.742 1.00 9.06  ? 371  HIS B N   1 
ATOM   6649 C CA  . HIS B 1 371 ? 65.510 46.590 -63.700 1.00 10.22 ? 371  HIS B CA  1 
ATOM   6650 C C   . HIS B 1 371 ? 66.162 46.687 -65.076 1.00 10.77 ? 371  HIS B C   1 
ATOM   6651 O O   . HIS B 1 371 ? 67.354 47.004 -65.181 1.00 11.08 ? 371  HIS B O   1 
ATOM   6652 C CB  . HIS B 1 371 ? 65.553 45.151 -63.159 1.00 10.15 ? 371  HIS B CB  1 
ATOM   6653 C CG  . HIS B 1 371 ? 65.374 45.048 -61.665 1.00 9.71  ? 371  HIS B CG  1 
ATOM   6654 N ND1 . HIS B 1 371 ? 64.132 44.965 -61.063 1.00 10.01 ? 371  HIS B ND1 1 
ATOM   6655 C CD2 . HIS B 1 371 ? 66.280 45.010 -60.656 1.00 13.02 ? 371  HIS B CD2 1 
ATOM   6656 C CE1 . HIS B 1 371 ? 64.281 44.887 -59.752 1.00 11.03 ? 371  HIS B CE1 1 
ATOM   6657 N NE2 . HIS B 1 371 ? 65.574 44.910 -59.477 1.00 10.78 ? 371  HIS B NE2 1 
ATOM   6658 N N   . LEU B 1 372 ? 65.391 46.453 -66.147 1.00 8.29  ? 372  LEU B N   1 
ATOM   6659 C CA  . LEU B 1 372 ? 65.938 46.617 -67.497 1.00 9.59  ? 372  LEU B CA  1 
ATOM   6660 C C   . LEU B 1 372 ? 66.270 48.072 -67.796 1.00 10.82 ? 372  LEU B C   1 
ATOM   6661 O O   . LEU B 1 372 ? 67.201 48.347 -68.562 1.00 11.23 ? 372  LEU B O   1 
ATOM   6662 C CB  . LEU B 1 372 ? 64.964 46.079 -68.550 1.00 10.66 ? 372  LEU B CB  1 
ATOM   6663 C CG  . LEU B 1 372 ? 64.936 44.553 -68.639 1.00 12.23 ? 372  LEU B CG  1 
ATOM   6664 C CD1 . LEU B 1 372 ? 63.904 44.091 -69.684 1.00 12.71 ? 372  LEU B CD1 1 
ATOM   6665 C CD2 . LEU B 1 372 ? 66.340 44.044 -68.959 1.00 11.94 ? 372  LEU B CD2 1 
ATOM   6666 N N   . LYS B 1 373 ? 65.524 49.014 -67.220 1.00 8.90  ? 373  LYS B N   1 
ATOM   6667 C CA  . LYS B 1 373 ? 65.914 50.414 -67.355 1.00 9.75  ? 373  LYS B CA  1 
ATOM   6668 C C   . LYS B 1 373 ? 67.266 50.666 -66.689 1.00 13.03 ? 373  LYS B C   1 
ATOM   6669 O O   . LYS B 1 373 ? 68.106 51.400 -67.230 1.00 10.09 ? 373  LYS B O   1 
ATOM   6670 C CB  . LYS B 1 373 ? 64.825 51.326 -66.778 1.00 12.55 ? 373  LYS B CB  1 
ATOM   6671 C CG  . LYS B 1 373 ? 65.089 52.825 -66.934 1.00 18.12 ? 373  LYS B CG  1 
ATOM   6672 C CD  . LYS B 1 373 ? 65.860 53.385 -65.747 1.00 25.03 ? 373  LYS B CD  1 
ATOM   6673 C CE  . LYS B 1 373 ? 66.115 54.890 -65.873 1.00 34.89 ? 373  LYS B CE  1 
ATOM   6674 N NZ  . LYS B 1 373 ? 66.726 55.430 -64.612 1.00 31.00 ? 373  LYS B NZ  1 
ATOM   6675 N N   . ILE B 1 374 ? 67.497 50.064 -65.517 1.00 11.25 ? 374  ILE B N   1 
ATOM   6676 C CA  . ILE B 1 374 ? 68.792 50.200 -64.846 1.00 11.80 ? 374  ILE B CA  1 
ATOM   6677 C C   . ILE B 1 374 ? 69.910 49.603 -65.693 1.00 11.86 ? 374  ILE B C   1 
ATOM   6678 O O   . ILE B 1 374 ? 70.997 50.188 -65.817 1.00 11.70 ? 374  ILE B O   1 
ATOM   6679 C CB  . ILE B 1 374 ? 68.751 49.554 -63.448 1.00 12.92 ? 374  ILE B CB  1 
ATOM   6680 C CG1 . ILE B 1 374 ? 67.757 50.287 -62.541 1.00 12.20 ? 374  ILE B CG1 1 
ATOM   6681 C CG2 . ILE B 1 374 ? 70.155 49.518 -62.835 1.00 13.70 ? 374  ILE B CG2 1 
ATOM   6682 C CD1 . ILE B 1 374 ? 68.095 51.754 -62.316 1.00 15.75 ? 374  ILE B CD1 1 
ATOM   6683 N N   . VAL B 1 375 ? 69.678 48.414 -66.261 1.00 10.87 ? 375  VAL B N   1 
ATOM   6684 C CA  . VAL B 1 375 ? 70.648 47.808 -67.176 1.00 12.67 ? 375  VAL B CA  1 
ATOM   6685 C C   . VAL B 1 375 ? 70.963 48.760 -68.328 1.00 16.24 ? 375  VAL B C   1 
ATOM   6686 O O   . VAL B 1 375 ? 72.131 48.949 -68.708 1.00 15.25 ? 375  VAL B O   1 
ATOM   6687 C CB  . VAL B 1 375 ? 70.117 46.457 -67.693 1.00 11.63 ? 375  VAL B CB  1 
ATOM   6688 C CG1 . VAL B 1 375 ? 70.933 45.976 -68.886 1.00 11.68 ? 375  VAL B CG1 1 
ATOM   6689 C CG2 . VAL B 1 375 ? 70.139 45.411 -66.570 1.00 9.62  ? 375  VAL B CG2 1 
ATOM   6690 N N   . GLU B 1 376 ? 69.921 49.361 -68.915 1.00 12.99 ? 376  GLU B N   1 
ATOM   6691 C CA  . GLU B 1 376 ? 70.139 50.285 -70.025 1.00 15.07 ? 376  GLU B CA  1 
ATOM   6692 C C   . GLU B 1 376 ? 70.935 51.506 -69.573 1.00 14.62 ? 376  GLU B C   1 
ATOM   6693 O O   . GLU B 1 376 ? 71.772 52.012 -70.328 1.00 16.46 ? 376  GLU B O   1 
ATOM   6694 C CB  . GLU B 1 376 ? 68.804 50.707 -70.656 1.00 12.46 ? 376  GLU B CB  1 
ATOM   6695 C CG  . GLU B 1 376 ? 68.950 51.384 -72.029 1.00 16.22 ? 376  GLU B CG  1 
ATOM   6696 C CD  . GLU B 1 376 ? 67.637 51.466 -72.820 1.00 19.72 ? 376  GLU B CD  1 
ATOM   6697 O OE1 . GLU B 1 376 ? 66.591 50.992 -72.333 1.00 18.78 ? 376  GLU B OE1 1 
ATOM   6698 O OE2 . GLU B 1 376 ? 67.653 51.989 -73.953 1.00 18.97 ? 376  GLU B OE2 1 
ATOM   6699 N N   . ASP B 1 377 ? 70.707 51.983 -68.338 1.00 13.82 ? 377  ASP B N   1 
ATOM   6700 C CA  . ASP B 1 377 ? 71.528 53.073 -67.805 1.00 17.59 ? 377  ASP B CA  1 
ATOM   6701 C C   . ASP B 1 377 ? 72.999 52.674 -67.763 1.00 19.61 ? 377  ASP B C   1 
ATOM   6702 O O   . ASP B 1 377 ? 73.879 53.485 -68.077 1.00 15.30 ? 377  ASP B O   1 
ATOM   6703 C CB  . ASP B 1 377 ? 71.102 53.469 -66.389 1.00 18.58 ? 377  ASP B CB  1 
ATOM   6704 C CG  . ASP B 1 377 ? 69.753 54.165 -66.322 1.00 24.76 ? 377  ASP B CG  1 
ATOM   6705 O OD1 . ASP B 1 377 ? 69.257 54.646 -67.361 1.00 23.00 ? 377  ASP B OD1 1 
ATOM   6706 O OD2 . ASP B 1 377 ? 69.183 54.197 -65.202 1.00 23.24 ? 377  ASP B OD2 1 
ATOM   6707 N N   . CYS B 1 378 ? 73.284 51.439 -67.325 1.00 16.42 ? 378  CYS B N   1 
ATOM   6708 C CA  . CYS B 1 378 ? 74.663 50.962 -67.247 1.00 18.57 ? 378  CYS B CA  1 
ATOM   6709 C C   . CYS B 1 378 ? 75.287 50.863 -68.632 1.00 17.33 ? 378  CYS B C   1 
ATOM   6710 O O   . CYS B 1 378 ? 76.468 51.185 -68.813 1.00 13.16 ? 378  CYS B O   1 
ATOM   6711 C CB  . CYS B 1 378 ? 74.718 49.604 -66.539 1.00 15.23 ? 378  CYS B CB  1 
ATOM   6712 S SG  . CYS B 1 378 ? 74.314 49.705 -64.771 1.00 16.18 ? 378  CYS B SG  1 
ATOM   6713 N N   . LEU B 1 379 ? 74.500 50.450 -69.625 1.00 15.51 ? 379  LEU B N   1 
ATOM   6714 C CA  . LEU B 1 379 ? 75.007 50.378 -70.990 1.00 17.23 ? 379  LEU B CA  1 
ATOM   6715 C C   . LEU B 1 379 ? 75.372 51.769 -71.517 1.00 20.62 ? 379  LEU B C   1 
ATOM   6716 O O   . LEU B 1 379 ? 76.363 51.929 -72.240 1.00 19.28 ? 379  LEU B O   1 
ATOM   6717 C CB  . LEU B 1 379 ? 73.958 49.701 -71.869 1.00 15.26 ? 379  LEU B CB  1 
ATOM   6718 C CG  . LEU B 1 379 ? 73.826 48.184 -71.687 1.00 17.34 ? 379  LEU B CG  1 
ATOM   6719 C CD1 . LEU B 1 379 ? 72.678 47.669 -72.519 1.00 18.27 ? 379  LEU B CD1 1 
ATOM   6720 C CD2 . LEU B 1 379 ? 75.120 47.455 -72.081 1.00 19.53 ? 379  LEU B CD2 1 
ATOM   6721 N N   . LYS B 1 380 ? 74.592 52.794 -71.144 1.00 19.75 ? 380  LYS B N   1 
ATOM   6722 C CA  . LYS B 1 380 ? 74.903 54.163 -71.560 1.00 24.33 ? 380  LYS B CA  1 
ATOM   6723 C C   . LYS B 1 380 ? 76.173 54.682 -70.896 1.00 21.65 ? 380  LYS B C   1 
ATOM   6724 O O   . LYS B 1 380 ? 76.815 55.599 -71.417 1.00 24.56 ? 380  LYS B O   1 
ATOM   6725 C CB  . LYS B 1 380 ? 73.744 55.107 -71.236 1.00 24.26 ? 380  LYS B CB  1 
ATOM   6726 C CG  . LYS B 1 380 ? 72.512 54.938 -72.110 1.00 30.70 ? 380  LYS B CG  1 
ATOM   6727 C CD  . LYS B 1 380 ? 71.275 55.504 -71.412 1.00 29.60 ? 380  LYS B CD  1 
ATOM   6728 C CE  . LYS B 1 380 ? 70.300 56.125 -72.405 1.00 38.10 ? 380  LYS B CE  1 
ATOM   6729 N NZ  . LYS B 1 380 ? 68.894 55.687 -72.161 1.00 40.01 ? 380  LYS B NZ  1 
ATOM   6730 N N   . GLU B 1 381 ? 76.527 54.143 -69.738 1.00 18.70 ? 381  GLU B N   1 
ATOM   6731 C CA  . GLU B 1 381 ? 77.797 54.454 -69.095 1.00 21.13 ? 381  GLU B CA  1 
ATOM   6732 C C   . GLU B 1 381 ? 78.953 53.668 -69.706 1.00 19.51 ? 381  GLU B C   1 
ATOM   6733 O O   . GLU B 1 381 ? 80.075 53.739 -69.190 1.00 21.93 ? 381  GLU B O   1 
ATOM   6734 C CB  . GLU B 1 381 ? 77.693 54.180 -67.591 1.00 21.55 ? 381  GLU B CB  1 
ATOM   6735 C CG  . GLU B 1 381 ? 76.760 55.128 -66.849 1.00 24.81 ? 381  GLU B CG  1 
ATOM   6736 C CD  . GLU B 1 381 ? 76.345 54.598 -65.474 1.00 33.84 ? 381  GLU B CD  1 
ATOM   6737 O OE1 . GLU B 1 381 ? 76.996 53.659 -64.964 1.00 34.33 ? 381  GLU B OE1 1 
ATOM   6738 O OE2 . GLU B 1 381 ? 75.386 55.140 -64.881 1.00 37.38 ? 381  GLU B OE2 1 
ATOM   6739 N N   . ASN B 1 382 ? 78.689 52.939 -70.796 1.00 19.10 ? 382  ASN B N   1 
ATOM   6740 C CA  . ASN B 1 382 ? 79.675 52.115 -71.507 1.00 20.81 ? 382  ASN B CA  1 
ATOM   6741 C C   . ASN B 1 382 ? 80.197 50.963 -70.653 1.00 23.00 ? 382  ASN B C   1 
ATOM   6742 O O   . ASN B 1 382 ? 81.345 50.536 -70.807 1.00 19.35 ? 382  ASN B O   1 
ATOM   6743 C CB  . ASN B 1 382 ? 80.855 52.944 -72.035 1.00 25.84 ? 382  ASN B CB  1 
ATOM   6744 C CG  . ASN B 1 382 ? 80.408 54.199 -72.757 1.00 39.82 ? 382  ASN B CG  1 
ATOM   6745 O OD1 . ASN B 1 382 ? 79.662 54.126 -73.741 1.00 36.90 ? 382  ASN B OD1 1 
ATOM   6746 N ND2 . ASN B 1 382 ? 80.835 55.362 -72.261 1.00 41.27 ? 382  ASN B ND2 1 
ATOM   6747 N N   . MET B 1 383 ? 79.383 50.411 -69.760 1.00 19.31 ? 383  MET B N   1 
ATOM   6748 C CA  . MET B 1 383 ? 79.930 49.309 -68.989 1.00 18.66 ? 383  MET B CA  1 
ATOM   6749 C C   . MET B 1 383 ? 79.852 48.036 -69.821 1.00 18.52 ? 383  MET B C   1 
ATOM   6750 O O   . MET B 1 383 ? 78.981 47.874 -70.683 1.00 13.73 ? 383  MET B O   1 
ATOM   6751 C CB  . MET B 1 383 ? 79.249 49.197 -67.610 1.00 21.86 ? 383  MET B CB  1 
ATOM   6752 C CG  . MET B 1 383 ? 79.237 47.843 -66.845 1.00 16.97 ? 383  MET B CG  1 
ATOM   6753 S SD  . MET B 1 383 ? 77.785 47.518 -65.790 1.00 17.72 ? 383  MET B SD  1 
ATOM   6754 C CE  . MET B 1 383 ? 78.113 48.759 -64.521 1.00 13.28 ? 383  MET B CE  1 
ATOM   6755 N N   . ASP B 1 384 ? 80.858 47.178 -69.636 1.00 18.55 ? 384  ASP B N   1 
ATOM   6756 C CA  . ASP B 1 384 ? 80.961 45.919 -70.371 1.00 18.45 ? 384  ASP B CA  1 
ATOM   6757 C C   . ASP B 1 384 ? 79.965 44.920 -69.775 1.00 17.65 ? 384  ASP B C   1 
ATOM   6758 O O   . ASP B 1 384 ? 80.316 43.972 -69.068 1.00 16.65 ? 384  ASP B O   1 
ATOM   6759 C CB  . ASP B 1 384 ? 82.393 45.402 -70.318 1.00 19.44 ? 384  ASP B CB  1 
ATOM   6760 C CG  . ASP B 1 384 ? 82.620 44.226 -71.236 1.00 20.03 ? 384  ASP B CG  1 
ATOM   6761 O OD1 . ASP B 1 384 ? 81.709 43.916 -72.032 1.00 20.97 ? 384  ASP B OD1 1 
ATOM   6762 O OD2 . ASP B 1 384 ? 83.706 43.604 -71.152 1.00 19.39 ? 384  ASP B OD2 1 
ATOM   6763 N N   . LEU B 1 385 ? 78.691 45.187 -70.045 1.00 13.95 ? 385  LEU B N   1 
ATOM   6764 C CA  . LEU B 1 385 ? 77.560 44.370 -69.611 1.00 14.43 ? 385  LEU B CA  1 
ATOM   6765 C C   . LEU B 1 385 ? 76.962 43.706 -70.844 1.00 13.16 ? 385  LEU B C   1 
ATOM   6766 O O   . LEU B 1 385 ? 76.519 44.398 -71.765 1.00 15.91 ? 385  LEU B O   1 
ATOM   6767 C CB  . LEU B 1 385 ? 76.510 45.239 -68.916 1.00 12.56 ? 385  LEU B CB  1 
ATOM   6768 C CG  . LEU B 1 385 ? 75.252 44.603 -68.310 1.00 12.76 ? 385  LEU B CG  1 
ATOM   6769 C CD1 . LEU B 1 385 ? 75.551 43.394 -67.392 1.00 11.73 ? 385  LEU B CD1 1 
ATOM   6770 C CD2 . LEU B 1 385 ? 74.404 45.672 -67.606 1.00 15.11 ? 385  LEU B CD2 1 
ATOM   6771 N N   . ARG B 1 386 ? 76.921 42.377 -70.855 1.00 13.00 ? 386  ARG B N   1 
ATOM   6772 C CA  . ARG B 1 386 ? 76.702 41.638 -72.089 1.00 14.37 ? 386  ARG B CA  1 
ATOM   6773 C C   . ARG B 1 386 ? 75.379 40.878 -72.148 1.00 13.00 ? 386  ARG B C   1 
ATOM   6774 O O   . ARG B 1 386 ? 75.069 40.295 -73.192 1.00 11.64 ? 386  ARG B O   1 
ATOM   6775 C CB  . ARG B 1 386 ? 77.882 40.675 -72.310 1.00 17.21 ? 386  ARG B CB  1 
ATOM   6776 C CG  . ARG B 1 386 ? 79.219 41.414 -72.398 1.00 16.06 ? 386  ARG B CG  1 
ATOM   6777 C CD  . ARG B 1 386 ? 80.357 40.553 -72.961 1.00 17.77 ? 386  ARG B CD  1 
ATOM   6778 N NE  . ARG B 1 386 ? 81.617 41.289 -72.950 1.00 18.55 ? 386  ARG B NE  1 
ATOM   6779 C CZ  . ARG B 1 386 ? 82.786 40.789 -73.327 1.00 21.89 ? 386  ARG B CZ  1 
ATOM   6780 N NH1 . ARG B 1 386 ? 82.903 39.536 -73.735 1.00 20.89 ? 386  ARG B NH1 1 
ATOM   6781 N NH2 . ARG B 1 386 ? 83.865 41.569 -73.296 1.00 16.86 ? 386  ARG B NH2 1 
ATOM   6782 N N   . GLY B 1 387 ? 74.576 40.884 -71.091 1.00 11.73 ? 387  GLY B N   1 
ATOM   6783 C CA  . GLY B 1 387 ? 73.310 40.184 -71.160 1.00 10.63 ? 387  GLY B CA  1 
ATOM   6784 C C   . GLY B 1 387 ? 72.527 40.315 -69.872 1.00 12.80 ? 387  GLY B C   1 
ATOM   6785 O O   . GLY B 1 387 ? 73.050 40.738 -68.832 1.00 9.69  ? 387  GLY B O   1 
ATOM   6786 N N   . TYR B 1 388 ? 71.252 39.946 -69.970 1.00 9.29  ? 388  TYR B N   1 
ATOM   6787 C CA  . TYR B 1 388 ? 70.326 39.954 -68.847 1.00 9.89  ? 388  TYR B CA  1 
ATOM   6788 C C   . TYR B 1 388 ? 69.489 38.689 -68.946 1.00 9.60  ? 388  TYR B C   1 
ATOM   6789 O O   . TYR B 1 388 ? 68.829 38.454 -69.967 1.00 9.48  ? 388  TYR B O   1 
ATOM   6790 C CB  . TYR B 1 388 ? 69.431 41.208 -68.862 1.00 8.96  ? 388  TYR B CB  1 
ATOM   6791 C CG  . TYR B 1 388 ? 68.278 41.161 -67.856 1.00 10.76 ? 388  TYR B CG  1 
ATOM   6792 C CD1 . TYR B 1 388 ? 67.066 40.559 -68.182 1.00 11.47 ? 388  TYR B CD1 1 
ATOM   6793 C CD2 . TYR B 1 388 ? 68.422 41.697 -66.577 1.00 8.21  ? 388  TYR B CD2 1 
ATOM   6794 C CE1 . TYR B 1 388 ? 66.011 40.510 -67.273 1.00 9.24  ? 388  TYR B CE1 1 
ATOM   6795 C CE2 . TYR B 1 388 ? 67.372 41.657 -65.655 1.00 11.16 ? 388  TYR B CE2 1 
ATOM   6796 C CZ  . TYR B 1 388 ? 66.165 41.059 -66.018 1.00 12.55 ? 388  TYR B CZ  1 
ATOM   6797 O OH  . TYR B 1 388 ? 65.114 40.999 -65.118 1.00 11.39 ? 388  TYR B OH  1 
ATOM   6798 N N   . MET B 1 389 ? 69.515 37.879 -67.897 1.00 7.62  ? 389  MET B N   1 
ATOM   6799 C CA  . MET B 1 389 ? 68.715 36.664 -67.828 1.00 8.53  ? 389  MET B CA  1 
ATOM   6800 C C   . MET B 1 389 ? 67.784 36.749 -66.631 1.00 11.20 ? 389  MET B C   1 
ATOM   6801 O O   . MET B 1 389 ? 68.230 36.986 -65.504 1.00 9.31  ? 389  MET B O   1 
ATOM   6802 C CB  . MET B 1 389 ? 69.592 35.408 -67.767 1.00 7.99  ? 389  MET B CB  1 
ATOM   6803 C CG  . MET B 1 389 ? 70.189 35.084 -69.128 1.00 11.68 ? 389  MET B CG  1 
ATOM   6804 S SD  . MET B 1 389 ? 71.796 34.264 -69.150 1.00 12.94 ? 389  MET B SD  1 
ATOM   6805 C CE  . MET B 1 389 ? 72.909 35.667 -69.146 1.00 10.67 ? 389  MET B CE  1 
ATOM   6806 N N   . HIS B 1 390 ? 66.492 36.592 -66.899 1.00 7.83  ? 390  HIS B N   1 
ATOM   6807 C CA  . HIS B 1 390 ? 65.453 36.665 -65.887 1.00 10.18 ? 390  HIS B CA  1 
ATOM   6808 C C   . HIS B 1 390 ? 65.289 35.314 -65.196 1.00 8.17  ? 390  HIS B C   1 
ATOM   6809 O O   . HIS B 1 390 ? 65.381 34.266 -65.842 1.00 8.65  ? 390  HIS B O   1 
ATOM   6810 C CB  . HIS B 1 390 ? 64.131 37.081 -66.555 1.00 8.94  ? 390  HIS B CB  1 
ATOM   6811 C CG  . HIS B 1 390 ? 63.065 37.505 -65.588 1.00 9.22  ? 390  HIS B CG  1 
ATOM   6812 N ND1 . HIS B 1 390 ? 63.054 38.750 -64.996 1.00 8.87  ? 390  HIS B ND1 1 
ATOM   6813 C CD2 . HIS B 1 390 ? 61.983 36.849 -65.107 1.00 8.99  ? 390  HIS B CD2 1 
ATOM   6814 C CE1 . HIS B 1 390 ? 62.003 38.846 -64.197 1.00 9.81  ? 390  HIS B CE1 1 
ATOM   6815 N NE2 . HIS B 1 390 ? 61.338 37.705 -64.243 1.00 9.33  ? 390  HIS B NE2 1 
ATOM   6816 N N   . TRP B 1 391 ? 65.051 35.337 -63.882 1.00 7.20  ? 391  TRP B N   1 
ATOM   6817 C CA  . TRP B 1 391 ? 64.681 34.134 -63.133 1.00 8.59  ? 391  TRP B CA  1 
ATOM   6818 C C   . TRP B 1 391 ? 63.176 34.201 -62.867 1.00 7.99  ? 391  TRP B C   1 
ATOM   6819 O O   . TRP B 1 391 ? 62.738 34.913 -61.958 1.00 9.50  ? 391  TRP B O   1 
ATOM   6820 C CB  . TRP B 1 391 ? 65.453 34.009 -61.813 1.00 7.06  ? 391  TRP B CB  1 
ATOM   6821 C CG  . TRP B 1 391 ? 65.111 32.676 -61.164 1.00 9.47  ? 391  TRP B CG  1 
ATOM   6822 C CD1 . TRP B 1 391 ? 64.005 32.390 -60.392 1.00 7.29  ? 391  TRP B CD1 1 
ATOM   6823 C CD2 . TRP B 1 391 ? 65.823 31.440 -61.314 1.00 8.94  ? 391  TRP B CD2 1 
ATOM   6824 N NE1 . TRP B 1 391 ? 64.000 31.056 -60.049 1.00 9.81  ? 391  TRP B NE1 1 
ATOM   6825 C CE2 . TRP B 1 391 ? 65.107 30.451 -60.590 1.00 8.86  ? 391  TRP B CE2 1 
ATOM   6826 C CE3 . TRP B 1 391 ? 67.006 31.075 -61.975 1.00 8.43  ? 391  TRP B CE3 1 
ATOM   6827 C CZ2 . TRP B 1 391 ? 65.533 29.115 -60.514 1.00 7.73  ? 391  TRP B CZ2 1 
ATOM   6828 C CZ3 . TRP B 1 391 ? 67.436 29.748 -61.895 1.00 9.42  ? 391  TRP B CZ3 1 
ATOM   6829 C CH2 . TRP B 1 391 ? 66.697 28.782 -61.164 1.00 9.36  ? 391  TRP B CH2 1 
ATOM   6830 N N   . SER B 1 392 ? 62.372 33.447 -63.626 1.00 6.83  ? 392  SER B N   1 
ATOM   6831 C CA  . SER B 1 392 ? 62.804 32.484 -64.643 1.00 5.54  ? 392  SER B CA  1 
ATOM   6832 C C   . SER B 1 392 ? 61.747 32.440 -65.747 1.00 7.08  ? 392  SER B C   1 
ATOM   6833 O O   . SER B 1 392 ? 60.773 33.213 -65.713 1.00 8.07  ? 392  SER B O   1 
ATOM   6834 C CB  . SER B 1 392 ? 62.986 31.090 -64.020 1.00 8.62  ? 392  SER B CB  1 
ATOM   6835 O OG  . SER B 1 392 ? 63.378 30.140 -65.004 1.00 8.55  ? 392  SER B OG  1 
ATOM   6836 N N   . ILE B 1 393 ? 61.899 31.537 -66.719 1.00 6.58  ? 393  ILE B N   1 
ATOM   6837 C CA  . ILE B 1 393 ? 60.869 31.413 -67.751 1.00 7.49  ? 393  ILE B CA  1 
ATOM   6838 C C   . ILE B 1 393 ? 59.591 30.808 -67.167 1.00 7.64  ? 393  ILE B C   1 
ATOM   6839 O O   . ILE B 1 393 ? 58.482 31.255 -67.486 1.00 7.56  ? 393  ILE B O   1 
ATOM   6840 C CB  . ILE B 1 393 ? 61.394 30.613 -68.970 1.00 10.04 ? 393  ILE B CB  1 
ATOM   6841 C CG1 . ILE B 1 393 ? 60.333 30.515 -70.084 1.00 10.48 ? 393  ILE B CG1 1 
ATOM   6842 C CG2 . ILE B 1 393 ? 61.897 29.218 -68.562 1.00 9.29  ? 393  ILE B CG2 1 
ATOM   6843 C CD1 . ILE B 1 393 ? 59.962 31.868 -70.741 1.00 10.21 ? 393  ILE B CD1 1 
ATOM   6844 N N   . ILE B 1 394 ? 59.710 29.806 -66.289 1.00 7.14  ? 394  ILE B N   1 
ATOM   6845 C CA  . ILE B 1 394 ? 58.534 29.129 -65.750 1.00 6.94  ? 394  ILE B CA  1 
ATOM   6846 C C   . ILE B 1 394 ? 58.645 29.021 -64.235 1.00 7.77  ? 394  ILE B C   1 
ATOM   6847 O O   . ILE B 1 394 ? 59.744 29.000 -63.678 1.00 7.49  ? 394  ILE B O   1 
ATOM   6848 C CB  . ILE B 1 394 ? 58.323 27.725 -66.374 1.00 7.44  ? 394  ILE B CB  1 
ATOM   6849 C CG1 . ILE B 1 394 ? 59.555 26.825 -66.180 1.00 8.80  ? 394  ILE B CG1 1 
ATOM   6850 C CG2 . ILE B 1 394 ? 57.933 27.819 -67.871 1.00 6.15  ? 394  ILE B CG2 1 
ATOM   6851 C CD1 . ILE B 1 394 ? 59.255 25.369 -66.457 1.00 8.77  ? 394  ILE B CD1 1 
ATOM   6852 N N   . ASP B 1 395 ? 57.488 28.943 -63.569 1.00 6.37  ? 395  ASP B N   1 
ATOM   6853 C CA  . ASP B 1 395 ? 57.423 28.563 -62.160 1.00 8.62  ? 395  ASP B CA  1 
ATOM   6854 C C   . ASP B 1 395 ? 58.162 27.250 -61.929 1.00 7.60  ? 395  ASP B C   1 
ATOM   6855 O O   . ASP B 1 395 ? 58.154 26.357 -62.781 1.00 5.41  ? 395  ASP B O   1 
ATOM   6856 C CB  . ASP B 1 395 ? 55.959 28.388 -61.710 1.00 7.57  ? 395  ASP B CB  1 
ATOM   6857 C CG  . ASP B 1 395 ? 55.138 29.662 -61.835 1.00 10.59 ? 395  ASP B CG  1 
ATOM   6858 O OD1 . ASP B 1 395 ? 55.745 30.757 -61.894 1.00 8.44  ? 395  ASP B OD1 1 
ATOM   6859 O OD2 . ASP B 1 395 ? 53.880 29.550 -61.876 1.00 9.23  ? 395  ASP B OD2 1 
ATOM   6860 N N   . ASN B 1 396 ? 58.766 27.113 -60.746 1.00 6.76  ? 396  ASN B N   1 
ATOM   6861 C CA  . ASN B 1 396 ? 59.615 25.955 -60.463 1.00 5.64  ? 396  ASN B CA  1 
ATOM   6862 C C   . ASN B 1 396 ? 59.648 25.702 -58.949 1.00 6.91  ? 396  ASN B C   1 
ATOM   6863 O O   . ASN B 1 396 ? 58.932 26.347 -58.171 1.00 8.83  ? 396  ASN B O   1 
ATOM   6864 C CB  . ASN B 1 396 ? 61.004 26.193 -61.078 1.00 5.13  ? 396  ASN B CB  1 
ATOM   6865 C CG  . ASN B 1 396 ? 61.662 27.463 -60.556 1.00 7.85  ? 396  ASN B CG  1 
ATOM   6866 O OD1 . ASN B 1 396 ? 62.336 27.438 -59.515 1.00 8.55  ? 396  ASN B OD1 1 
ATOM   6867 N ND2 . ASN B 1 396 ? 61.453 28.592 -61.261 1.00 6.07  ? 396  ASN B ND2 1 
ATOM   6868 N N   . PHE B 1 397 ? 60.478 24.744 -58.529 1.00 8.42  ? 397  PHE B N   1 
ATOM   6869 C CA  . PHE B 1 397 ? 60.561 24.315 -57.130 1.00 8.91  ? 397  PHE B CA  1 
ATOM   6870 C C   . PHE B 1 397 ? 61.505 25.257 -56.386 1.00 8.33  ? 397  PHE B C   1 
ATOM   6871 O O   . PHE B 1 397 ? 62.722 25.231 -56.602 1.00 8.67  ? 397  PHE B O   1 
ATOM   6872 C CB  . PHE B 1 397 ? 61.040 22.863 -57.073 1.00 9.24  ? 397  PHE B CB  1 
ATOM   6873 C CG  . PHE B 1 397 ? 60.955 22.213 -55.705 1.00 8.39  ? 397  PHE B CG  1 
ATOM   6874 C CD1 . PHE B 1 397 ? 62.049 22.219 -54.849 1.00 6.17  ? 397  PHE B CD1 1 
ATOM   6875 C CD2 . PHE B 1 397 ? 59.807 21.531 -55.312 1.00 9.25  ? 397  PHE B CD2 1 
ATOM   6876 C CE1 . PHE B 1 397 ? 61.988 21.594 -53.609 1.00 10.37 ? 397  PHE B CE1 1 
ATOM   6877 C CE2 . PHE B 1 397 ? 59.740 20.904 -54.069 1.00 11.36 ? 397  PHE B CE2 1 
ATOM   6878 C CZ  . PHE B 1 397 ? 60.830 20.940 -53.218 1.00 8.75  ? 397  PHE B CZ  1 
ATOM   6879 N N   . GLU B 1 398 ? 60.959 26.107 -55.516 1.00 9.32  ? 398  GLU B N   1 
ATOM   6880 C CA  . GLU B 1 398 ? 61.770 27.174 -54.909 1.00 9.69  ? 398  GLU B CA  1 
ATOM   6881 C C   . GLU B 1 398 ? 62.359 26.686 -53.574 1.00 9.57  ? 398  GLU B C   1 
ATOM   6882 O O   . GLU B 1 398 ? 61.992 27.121 -52.486 1.00 9.38  ? 398  GLU B O   1 
ATOM   6883 C CB  . GLU B 1 398 ? 60.933 28.447 -54.759 1.00 8.64  ? 398  GLU B CB  1 
ATOM   6884 C CG  . GLU B 1 398 ? 61.595 29.627 -53.989 1.00 10.56 ? 398  GLU B CG  1 
ATOM   6885 C CD  . GLU B 1 398 ? 62.854 30.158 -54.656 1.00 15.44 ? 398  GLU B CD  1 
ATOM   6886 O OE1 . GLU B 1 398 ? 63.576 30.955 -54.005 1.00 19.55 ? 398  GLU B OE1 1 
ATOM   6887 O OE2 . GLU B 1 398 ? 63.111 29.809 -55.836 1.00 13.22 ? 398  GLU B OE2 1 
ATOM   6888 N N   . TRP B 1 399 ? 63.300 25.741 -53.687 1.00 10.12 ? 399  TRP B N   1 
ATOM   6889 C CA  . TRP B 1 399 ? 64.099 25.205 -52.576 1.00 7.87  ? 399  TRP B CA  1 
ATOM   6890 C C   . TRP B 1 399 ? 63.214 24.925 -51.339 1.00 8.26  ? 399  TRP B C   1 
ATOM   6891 O O   . TRP B 1 399 ? 62.291 24.112 -51.498 1.00 7.90  ? 399  TRP B O   1 
ATOM   6892 C CB  . TRP B 1 399 ? 65.303 26.137 -52.383 1.00 8.26  ? 399  TRP B CB  1 
ATOM   6893 C CG  . TRP B 1 399 ? 66.110 26.255 -53.661 1.00 9.70  ? 399  TRP B CG  1 
ATOM   6894 C CD1 . TRP B 1 399 ? 66.280 27.381 -54.422 1.00 8.43  ? 399  TRP B CD1 1 
ATOM   6895 C CD2 . TRP B 1 399 ? 66.826 25.204 -54.329 1.00 7.83  ? 399  TRP B CD2 1 
ATOM   6896 N NE1 . TRP B 1 399 ? 67.064 27.095 -55.514 1.00 8.20  ? 399  TRP B NE1 1 
ATOM   6897 C CE2 . TRP B 1 399 ? 67.409 25.766 -55.483 1.00 8.84  ? 399  TRP B CE2 1 
ATOM   6898 C CE3 . TRP B 1 399 ? 67.038 23.842 -54.057 1.00 10.34 ? 399  TRP B CE3 1 
ATOM   6899 C CZ2 . TRP B 1 399 ? 68.197 25.013 -56.374 1.00 7.77  ? 399  TRP B CZ2 1 
ATOM   6900 C CZ3 . TRP B 1 399 ? 67.830 23.092 -54.944 1.00 9.63  ? 399  TRP B CZ3 1 
ATOM   6901 C CH2 . TRP B 1 399 ? 68.391 23.684 -56.089 1.00 6.57  ? 399  TRP B CH2 1 
ATOM   6902 N N   . PRO B 1 400 ? 63.382 25.499 -50.126 1.00 9.44  ? 400  PRO B N   1 
ATOM   6903 C CA  . PRO B 1 400 ? 62.541 25.012 -49.014 1.00 10.90 ? 400  PRO B CA  1 
ATOM   6904 C C   . PRO B 1 400 ? 61.095 25.502 -49.051 1.00 11.81 ? 400  PRO B C   1 
ATOM   6905 O O   . PRO B 1 400 ? 60.283 25.009 -48.260 1.00 10.67 ? 400  PRO B O   1 
ATOM   6906 C CB  . PRO B 1 400 ? 63.253 25.550 -47.766 1.00 10.16 ? 400  PRO B CB  1 
ATOM   6907 C CG  . PRO B 1 400 ? 63.708 26.895 -48.209 1.00 10.80 ? 400  PRO B CG  1 
ATOM   6908 C CD  . PRO B 1 400 ? 64.147 26.688 -49.658 1.00 8.66  ? 400  PRO B CD  1 
ATOM   6909 N N   . MET B 1 401 ? 60.750 26.456 -49.919 1.00 11.71 ? 401  MET B N   1 
ATOM   6910 C CA  . MET B 1 401 ? 59.364 26.893 -50.110 1.00 10.05 ? 401  MET B CA  1 
ATOM   6911 C C   . MET B 1 401 ? 58.554 26.014 -51.060 1.00 12.62 ? 401  MET B C   1 
ATOM   6912 O O   . MET B 1 401 ? 57.336 26.194 -51.137 1.00 10.47 ? 401  MET B O   1 
ATOM   6913 C CB  . MET B 1 401 ? 59.335 28.346 -50.613 1.00 10.04 ? 401  MET B CB  1 
ATOM   6914 C CG  . MET B 1 401 ? 60.384 29.260 -49.991 1.00 16.87 ? 401  MET B CG  1 
ATOM   6915 S SD  . MET B 1 401 ? 60.149 29.253 -48.190 1.00 24.88 ? 401  MET B SD  1 
ATOM   6916 C CE  . MET B 1 401 ? 58.443 29.720 -48.073 1.00 23.33 ? 401  MET B CE  1 
ATOM   6917 N N   . GLY B 1 402 ? 59.182 25.090 -51.781 1.00 11.90 ? 402  GLY B N   1 
ATOM   6918 C CA  . GLY B 1 402 ? 58.431 24.286 -52.742 1.00 9.07  ? 402  GLY B CA  1 
ATOM   6919 C C   . GLY B 1 402 ? 57.852 25.140 -53.856 1.00 10.46 ? 402  GLY B C   1 
ATOM   6920 O O   . GLY B 1 402 ? 58.460 26.126 -54.305 1.00 7.78  ? 402  GLY B O   1 
ATOM   6921 N N   . TYR B 1 403 ? 56.647 24.779 -54.303 1.00 10.58 ? 403  TYR B N   1 
ATOM   6922 C CA  . TYR B 1 403 ? 56.041 25.475 -55.439 1.00 11.48 ? 403  TYR B CA  1 
ATOM   6923 C C   . TYR B 1 403 ? 55.312 26.758 -55.044 1.00 11.75 ? 403  TYR B C   1 
ATOM   6924 O O   . TYR B 1 403 ? 54.792 27.443 -55.929 1.00 12.54 ? 403  TYR B O   1 
ATOM   6925 C CB  . TYR B 1 403 ? 55.072 24.541 -56.172 1.00 8.26  ? 403  TYR B CB  1 
ATOM   6926 C CG  . TYR B 1 403 ? 55.770 23.294 -56.696 1.00 12.14 ? 403  TYR B CG  1 
ATOM   6927 C CD1 . TYR B 1 403 ? 56.760 23.382 -57.669 1.00 10.58 ? 403  TYR B CD1 1 
ATOM   6928 C CD2 . TYR B 1 403 ? 55.473 22.038 -56.175 1.00 11.76 ? 403  TYR B CD2 1 
ATOM   6929 C CE1 . TYR B 1 403 ? 57.423 22.241 -58.134 1.00 11.60 ? 403  TYR B CE1 1 
ATOM   6930 C CE2 . TYR B 1 403 ? 56.133 20.896 -56.630 1.00 10.40 ? 403  TYR B CE2 1 
ATOM   6931 C CZ  . TYR B 1 403 ? 57.104 21.012 -57.607 1.00 10.74 ? 403  TYR B CZ  1 
ATOM   6932 O OH  . TYR B 1 403 ? 57.765 19.892 -58.057 1.00 10.75 ? 403  TYR B OH  1 
ATOM   6933 N N   . SER B 1 404 ? 55.289 27.109 -53.755 1.00 10.38 ? 404  SER B N   1 
ATOM   6934 C CA  . SER B 1 404 ? 54.453 28.214 -53.282 1.00 13.47 ? 404  SER B CA  1 
ATOM   6935 C C   . SER B 1 404 ? 54.953 29.564 -53.775 1.00 10.41 ? 404  SER B C   1 
ATOM   6936 O O   . SER B 1 404 ? 54.162 30.504 -53.886 1.00 11.95 ? 404  SER B O   1 
ATOM   6937 C CB  . SER B 1 404 ? 54.391 28.199 -51.752 1.00 16.67 ? 404  SER B CB  1 
ATOM   6938 O OG  . SER B 1 404 ? 55.667 28.508 -51.212 1.00 16.02 ? 404  SER B OG  1 
ATOM   6939 N N   . MET B 1 405 ? 56.244 29.681 -54.097 1.00 9.43  ? 405  MET B N   1 
ATOM   6940 C CA  . MET B 1 405 ? 56.824 30.918 -54.637 1.00 8.51  ? 405  MET B CA  1 
ATOM   6941 C C   . MET B 1 405 ? 57.061 30.733 -56.131 1.00 11.00 ? 405  MET B C   1 
ATOM   6942 O O   . MET B 1 405 ? 57.918 29.940 -56.541 1.00 9.01  ? 405  MET B O   1 
ATOM   6943 C CB  . MET B 1 405 ? 58.115 31.322 -53.907 1.00 11.05 ? 405  MET B CB  1 
ATOM   6944 C CG  . MET B 1 405 ? 57.975 31.413 -52.382 1.00 10.52 ? 405  MET B CG  1 
ATOM   6945 S SD  . MET B 1 405 ? 56.711 32.688 -52.033 1.00 14.16 ? 405  MET B SD  1 
ATOM   6946 C CE  . MET B 1 405 ? 56.717 32.700 -50.240 1.00 21.36 ? 405  MET B CE  1 
ATOM   6947 N N   . ARG B 1 406 ? 56.322 31.502 -56.934 1.00 7.09  ? 406  ARG B N   1 
ATOM   6948 C CA  . ARG B 1 406 ? 56.236 31.326 -58.385 1.00 10.00 ? 406  ARG B CA  1 
ATOM   6949 C C   . ARG B 1 406 ? 56.981 32.464 -59.071 1.00 8.75  ? 406  ARG B C   1 
ATOM   6950 O O   . ARG B 1 406 ? 56.493 33.596 -59.104 1.00 8.51  ? 406  ARG B O   1 
ATOM   6951 C CB  . ARG B 1 406 ? 54.763 31.267 -58.800 1.00 8.18  ? 406  ARG B CB  1 
ATOM   6952 C CG  . ARG B 1 406 ? 54.093 29.957 -58.323 1.00 10.08 ? 406  ARG B CG  1 
ATOM   6953 C CD  . ARG B 1 406 ? 52.587 29.912 -58.522 1.00 12.09 ? 406  ARG B CD  1 
ATOM   6954 N NE  . ARG B 1 406 ? 52.004 28.611 -58.189 1.00 10.78 ? 406  ARG B NE  1 
ATOM   6955 C CZ  . ARG B 1 406 ? 51.800 27.632 -59.063 1.00 13.33 ? 406  ARG B CZ  1 
ATOM   6956 N NH1 . ARG B 1 406 ? 52.179 27.744 -60.330 1.00 9.18  ? 406  ARG B NH1 1 
ATOM   6957 N NH2 . ARG B 1 406 ? 51.181 26.520 -58.661 1.00 10.84 ? 406  ARG B NH2 1 
ATOM   6958 N N   . PHE B 1 407 ? 58.167 32.166 -59.615 1.00 8.11  ? 407  PHE B N   1 
ATOM   6959 C CA  . PHE B 1 407 ? 59.036 33.178 -60.219 1.00 8.36  ? 407  PHE B CA  1 
ATOM   6960 C C   . PHE B 1 407 ? 58.916 33.272 -61.741 1.00 6.96  ? 407  PHE B C   1 
ATOM   6961 O O   . PHE B 1 407 ? 59.683 34.020 -62.355 1.00 8.40  ? 407  PHE B O   1 
ATOM   6962 C CB  . PHE B 1 407 ? 60.515 32.895 -59.882 1.00 6.93  ? 407  PHE B CB  1 
ATOM   6963 C CG  . PHE B 1 407 ? 60.955 33.381 -58.512 1.00 9.53  ? 407  PHE B CG  1 
ATOM   6964 C CD1 . PHE B 1 407 ? 60.680 32.635 -57.380 1.00 8.78  ? 407  PHE B CD1 1 
ATOM   6965 C CD2 . PHE B 1 407 ? 61.651 34.579 -58.372 1.00 9.65  ? 407  PHE B CD2 1 
ATOM   6966 C CE1 . PHE B 1 407 ? 61.107 33.062 -56.122 1.00 9.75  ? 407  PHE B CE1 1 
ATOM   6967 C CE2 . PHE B 1 407 ? 62.080 35.015 -57.119 1.00 8.17  ? 407  PHE B CE2 1 
ATOM   6968 C CZ  . PHE B 1 407 ? 61.811 34.249 -55.995 1.00 9.54  ? 407  PHE B CZ  1 
ATOM   6969 N N   . GLY B 1 408 ? 58.010 32.529 -62.368 1.00 8.14  ? 408  GLY B N   1 
ATOM   6970 C CA  . GLY B 1 408 ? 58.017 32.431 -63.831 1.00 6.54  ? 408  GLY B CA  1 
ATOM   6971 C C   . GLY B 1 408 ? 57.382 33.633 -64.522 1.00 8.66  ? 408  GLY B C   1 
ATOM   6972 O O   . GLY B 1 408 ? 56.414 34.224 -64.036 1.00 8.97  ? 408  GLY B O   1 
ATOM   6973 N N   . LEU B 1 409 ? 57.955 33.997 -65.674 1.00 7.34  ? 409  LEU B N   1 
ATOM   6974 C CA  . LEU B 1 409 ? 57.204 34.764 -66.669 1.00 8.03  ? 409  LEU B CA  1 
ATOM   6975 C C   . LEU B 1 409 ? 55.994 33.981 -67.173 1.00 7.81  ? 409  LEU B C   1 
ATOM   6976 O O   . LEU B 1 409 ? 55.051 34.573 -67.721 1.00 6.33  ? 409  LEU B O   1 
ATOM   6977 C CB  . LEU B 1 409 ? 58.117 35.102 -67.850 1.00 8.61  ? 409  LEU B CB  1 
ATOM   6978 C CG  . LEU B 1 409 ? 59.253 36.055 -67.482 1.00 8.40  ? 409  LEU B CG  1 
ATOM   6979 C CD1 . LEU B 1 409 ? 60.403 35.821 -68.462 1.00 8.45  ? 409  LEU B CD1 1 
ATOM   6980 C CD2 . LEU B 1 409 ? 58.741 37.507 -67.545 1.00 5.30  ? 409  LEU B CD2 1 
ATOM   6981 N N   . VAL B 1 410 ? 56.017 32.657 -67.000 1.00 7.01  ? 410  VAL B N   1 
ATOM   6982 C CA  . VAL B 1 410 ? 54.991 31.738 -67.482 1.00 8.14  ? 410  VAL B CA  1 
ATOM   6983 C C   . VAL B 1 410 ? 54.515 30.905 -66.300 1.00 10.57 ? 410  VAL B C   1 
ATOM   6984 O O   . VAL B 1 410 ? 55.336 30.301 -65.598 1.00 7.37  ? 410  VAL B O   1 
ATOM   6985 C CB  . VAL B 1 410 ? 55.546 30.834 -68.601 1.00 8.35  ? 410  VAL B CB  1 
ATOM   6986 C CG1 . VAL B 1 410 ? 54.501 29.808 -69.067 1.00 9.26  ? 410  VAL B CG1 1 
ATOM   6987 C CG2 . VAL B 1 410 ? 56.043 31.687 -69.764 1.00 8.34  ? 410  VAL B CG2 1 
ATOM   6988 N N   . ARG B 1 411 ? 53.198 30.880 -66.073 1.00 8.54  ? 411  ARG B N   1 
ATOM   6989 C CA  . ARG B 1 411 ? 52.640 30.078 -64.993 1.00 9.96  ? 411  ARG B CA  1 
ATOM   6990 C C   . ARG B 1 411 ? 52.684 28.601 -65.341 1.00 10.73 ? 411  ARG B C   1 
ATOM   6991 O O   . ARG B 1 411 ? 52.437 28.211 -66.486 1.00 12.48 ? 411  ARG B O   1 
ATOM   6992 C CB  . ARG B 1 411 ? 51.184 30.477 -64.705 1.00 8.07  ? 411  ARG B CB  1 
ATOM   6993 C CG  . ARG B 1 411 ? 50.629 29.832 -63.413 1.00 11.11 ? 411  ARG B CG  1 
ATOM   6994 C CD  . ARG B 1 411 ? 49.325 30.498 -62.940 1.00 8.89  ? 411  ARG B CD  1 
ATOM   6995 N NE  . ARG B 1 411 ? 49.146 30.330 -61.502 1.00 11.91 ? 411  ARG B NE  1 
ATOM   6996 C CZ  . ARG B 1 411 ? 48.693 29.227 -60.922 1.00 10.52 ? 411  ARG B CZ  1 
ATOM   6997 N NH1 . ARG B 1 411 ? 48.296 28.179 -61.636 1.00 10.18 ? 411  ARG B NH1 1 
ATOM   6998 N NH2 . ARG B 1 411 ? 48.659 29.163 -59.591 1.00 10.69 ? 411  ARG B NH2 1 
ATOM   6999 N N   . VAL B 1 412 ? 52.964 27.767 -64.342 1.00 7.31  ? 412  VAL B N   1 
ATOM   7000 C CA  . VAL B 1 412 ? 52.896 26.318 -64.505 1.00 10.49 ? 412  VAL B CA  1 
ATOM   7001 C C   . VAL B 1 412 ? 51.758 25.782 -63.659 1.00 10.22 ? 412  VAL B C   1 
ATOM   7002 O O   . VAL B 1 412 ? 51.699 26.043 -62.450 1.00 9.83  ? 412  VAL B O   1 
ATOM   7003 C CB  . VAL B 1 412 ? 54.206 25.622 -64.108 1.00 10.74 ? 412  VAL B CB  1 
ATOM   7004 C CG1 . VAL B 1 412 ? 54.047 24.106 -64.307 1.00 11.04 ? 412  VAL B CG1 1 
ATOM   7005 C CG2 . VAL B 1 412 ? 55.369 26.167 -64.911 1.00 8.06  ? 412  VAL B CG2 1 
ATOM   7006 N N   . ASP B 1 413 ? 50.892 24.985 -64.259 1.00 9.38  ? 413  ASP B N   1 
ATOM   7007 C CA  . ASP B 1 413 ? 49.987 24.189 -63.451 1.00 11.51 ? 413  ASP B CA  1 
ATOM   7008 C C   . ASP B 1 413 ? 50.643 22.820 -63.344 1.00 13.11 ? 413  ASP B C   1 
ATOM   7009 O O   . ASP B 1 413 ? 50.698 22.064 -64.327 1.00 13.72 ? 413  ASP B O   1 
ATOM   7010 C CB  . ASP B 1 413 ? 48.587 24.109 -64.044 1.00 14.23 ? 413  ASP B CB  1 
ATOM   7011 C CG  . ASP B 1 413 ? 47.633 23.386 -63.119 1.00 25.47 ? 413  ASP B CG  1 
ATOM   7012 O OD1 . ASP B 1 413 ? 47.829 22.187 -62.833 1.00 20.08 ? 413  ASP B OD1 1 
ATOM   7013 O OD2 . ASP B 1 413 ? 46.745 24.092 -62.567 1.00 26.47 ? 413  ASP B OD2 1 
ATOM   7014 N N   . PHE B 1 414 ? 51.189 22.532 -62.168 1.00 9.67  ? 414  PHE B N   1 
ATOM   7015 C CA  . PHE B 1 414 ? 52.052 21.369 -62.033 1.00 14.80 ? 414  PHE B CA  1 
ATOM   7016 C C   . PHE B 1 414 ? 51.257 20.072 -62.157 1.00 15.48 ? 414  PHE B C   1 
ATOM   7017 O O   . PHE B 1 414 ? 51.747 19.104 -62.745 1.00 19.06 ? 414  PHE B O   1 
ATOM   7018 C CB  . PHE B 1 414 ? 52.825 21.458 -60.712 1.00 12.36 ? 414  PHE B CB  1 
ATOM   7019 C CG  . PHE B 1 414 ? 53.855 22.570 -60.694 1.00 11.21 ? 414  PHE B CG  1 
ATOM   7020 C CD1 . PHE B 1 414 ? 55.063 22.421 -61.368 1.00 11.51 ? 414  PHE B CD1 1 
ATOM   7021 C CD2 . PHE B 1 414 ? 53.603 23.773 -60.033 1.00 12.88 ? 414  PHE B CD2 1 
ATOM   7022 C CE1 . PHE B 1 414 ? 56.015 23.443 -61.383 1.00 11.31 ? 414  PHE B CE1 1 
ATOM   7023 C CE2 . PHE B 1 414 ? 54.550 24.810 -60.044 1.00 12.81 ? 414  PHE B CE2 1 
ATOM   7024 C CZ  . PHE B 1 414 ? 55.760 24.638 -60.715 1.00 8.93  ? 414  PHE B CZ  1 
ATOM   7025 N N   . LYS B 1 415 ? 50.020 20.044 -61.662 1.00 14.84 ? 415  LYS B N   1 
ATOM   7026 C CA  . LYS B 1 415 ? 49.192 18.847 -61.812 1.00 18.46 ? 415  LYS B CA  1 
ATOM   7027 C C   . LYS B 1 415 ? 48.885 18.556 -63.280 1.00 19.11 ? 415  LYS B C   1 
ATOM   7028 O O   . LYS B 1 415 ? 49.053 17.422 -63.743 1.00 20.70 ? 415  LYS B O   1 
ATOM   7029 C CB  . LYS B 1 415 ? 47.897 19.001 -61.019 1.00 22.98 ? 415  LYS B CB  1 
ATOM   7030 N N   . GLN B 1 416 ? 48.431 19.559 -64.032 1.00 21.24 ? 416  GLN B N   1 
ATOM   7031 C CA  . GLN B 1 416 ? 48.068 19.339 -65.426 1.00 21.79 ? 416  GLN B CA  1 
ATOM   7032 C C   . GLN B 1 416 ? 49.235 19.473 -66.390 1.00 22.04 ? 416  GLN B C   1 
ATOM   7033 O O   . GLN B 1 416 ? 49.053 19.215 -67.583 1.00 26.23 ? 416  GLN B O   1 
ATOM   7034 C CB  . GLN B 1 416 ? 46.930 20.275 -65.857 1.00 26.74 ? 416  GLN B CB  1 
ATOM   7035 C CG  . GLN B 1 416 ? 45.868 20.554 -64.797 1.00 30.14 ? 416  GLN B CG  1 
ATOM   7036 C CD  . GLN B 1 416 ? 44.986 21.752 -65.147 1.00 44.93 ? 416  GLN B CD  1 
ATOM   7037 O OE1 . GLN B 1 416 ? 45.002 22.784 -64.466 1.00 44.79 ? 416  GLN B OE1 1 
ATOM   7038 N NE2 . GLN B 1 416 ? 44.235 21.627 -66.242 1.00 45.00 ? 416  GLN B NE2 1 
ATOM   7039 N N   . LYS B 1 417 ? 50.418 19.852 -65.909 1.00 18.65 ? 417  LYS B N   1 
ATOM   7040 C CA  . LYS B 1 417 ? 51.610 20.002 -66.751 1.00 19.29 ? 417  LYS B CA  1 
ATOM   7041 C C   . LYS B 1 417 ? 51.354 21.018 -67.870 1.00 20.88 ? 417  LYS B C   1 
ATOM   7042 O O   . LYS B 1 417 ? 51.648 20.781 -69.043 1.00 21.42 ? 417  LYS B O   1 
ATOM   7043 C CB  . LYS B 1 417 ? 52.057 18.645 -67.306 1.00 24.27 ? 417  LYS B CB  1 
ATOM   7044 C CG  . LYS B 1 417 ? 52.328 17.618 -66.197 1.00 22.72 ? 417  LYS B CG  1 
ATOM   7045 C CD  . LYS B 1 417 ? 53.524 18.008 -65.298 1.00 24.25 ? 417  LYS B CD  1 
ATOM   7046 C CE  . LYS B 1 417 ? 53.927 16.856 -64.353 1.00 28.73 ? 417  LYS B CE  1 
ATOM   7047 N NZ  . LYS B 1 417 ? 53.993 17.265 -62.900 1.00 14.74 ? 417  LYS B NZ  1 
ATOM   7048 N N   . LEU B 1 418 ? 50.801 22.168 -67.481 1.00 20.43 ? 418  LEU B N   1 
ATOM   7049 C CA  . LEU B 1 418 ? 50.316 23.203 -68.383 1.00 16.49 ? 418  LEU B CA  1 
ATOM   7050 C C   . LEU B 1 418 ? 51.139 24.470 -68.195 1.00 13.30 ? 418  LEU B C   1 
ATOM   7051 O O   . LEU B 1 418 ? 51.389 24.880 -67.059 1.00 14.02 ? 418  LEU B O   1 
ATOM   7052 C CB  . LEU B 1 418 ? 48.841 23.510 -68.088 1.00 17.03 ? 418  LEU B CB  1 
ATOM   7053 C CG  . LEU B 1 418 ? 48.067 24.538 -68.929 1.00 23.33 ? 418  LEU B CG  1 
ATOM   7054 C CD1 . LEU B 1 418 ? 48.282 24.363 -70.439 1.00 20.77 ? 418  LEU B CD1 1 
ATOM   7055 C CD2 . LEU B 1 418 ? 46.573 24.592 -68.537 1.00 24.78 ? 418  LEU B CD2 1 
ATOM   7056 N N   . PHE B 1 419 ? 51.531 25.100 -69.303 1.00 11.35 ? 419  PHE B N   1 
ATOM   7057 C CA  . PHE B 1 419 ? 52.289 26.350 -69.305 1.00 11.63 ? 419  PHE B CA  1 
ATOM   7058 C C   . PHE B 1 419 ? 51.387 27.470 -69.824 1.00 12.66 ? 419  PHE B C   1 
ATOM   7059 O O   . PHE B 1 419 ? 50.803 27.343 -70.904 1.00 13.97 ? 419  PHE B O   1 
ATOM   7060 C CB  . PHE B 1 419 ? 53.525 26.240 -70.210 1.00 12.25 ? 419  PHE B CB  1 
ATOM   7061 C CG  . PHE B 1 419 ? 54.565 25.220 -69.764 1.00 12.15 ? 419  PHE B CG  1 
ATOM   7062 C CD1 . PHE B 1 419 ? 54.656 24.790 -68.455 1.00 14.35 ? 419  PHE B CD1 1 
ATOM   7063 C CD2 . PHE B 1 419 ? 55.421 24.654 -70.706 1.00 18.75 ? 419  PHE B CD2 1 
ATOM   7064 C CE1 . PHE B 1 419 ? 55.618 23.840 -68.078 1.00 19.44 ? 419  PHE B CE1 1 
ATOM   7065 C CE2 . PHE B 1 419 ? 56.373 23.700 -70.345 1.00 15.30 ? 419  PHE B CE2 1 
ATOM   7066 C CZ  . PHE B 1 419 ? 56.474 23.291 -69.035 1.00 15.64 ? 419  PHE B CZ  1 
ATOM   7067 N N   . THR B 1 420 ? 51.272 28.560 -69.074 1.00 9.09  ? 420  THR B N   1 
ATOM   7068 C CA  . THR B 1 420 ? 50.429 29.691 -69.467 1.00 10.82 ? 420  THR B CA  1 
ATOM   7069 C C   . THR B 1 420 ? 51.185 30.992 -69.238 1.00 8.08  ? 420  THR B C   1 
ATOM   7070 O O   . THR B 1 420 ? 51.338 31.407 -68.072 1.00 10.40 ? 420  THR B O   1 
ATOM   7071 C CB  . THR B 1 420 ? 49.118 29.716 -68.682 1.00 12.31 ? 420  THR B CB  1 
ATOM   7072 O OG1 . THR B 1 420 ? 48.427 28.462 -68.835 1.00 10.96 ? 420  THR B OG1 1 
ATOM   7073 C CG2 . THR B 1 420 ? 48.226 30.871 -69.178 1.00 9.69  ? 420  THR B CG2 1 
ATOM   7074 N N   . PRO B 1 421 ? 51.663 31.665 -70.288 1.00 11.50 ? 421  PRO B N   1 
ATOM   7075 C CA  . PRO B 1 421 ? 52.378 32.938 -70.097 1.00 12.13 ? 421  PRO B CA  1 
ATOM   7076 C C   . PRO B 1 421 ? 51.559 33.986 -69.343 1.00 10.78 ? 421  PRO B C   1 
ATOM   7077 O O   . PRO B 1 421 ? 50.363 34.170 -69.589 1.00 9.72  ? 421  PRO B O   1 
ATOM   7078 C CB  . PRO B 1 421 ? 52.660 33.390 -71.537 1.00 10.24 ? 421  PRO B CB  1 
ATOM   7079 C CG  . PRO B 1 421 ? 52.792 32.092 -72.293 1.00 12.57 ? 421  PRO B CG  1 
ATOM   7080 C CD  . PRO B 1 421 ? 51.715 31.208 -71.690 1.00 12.07 ? 421  PRO B CD  1 
ATOM   7081 N N   . ARG B 1 422 ? 52.229 34.689 -68.427 1.00 10.35 ? 422  ARG B N   1 
ATOM   7082 C CA  . ARG B 1 422 ? 51.654 35.842 -67.747 1.00 8.11  ? 422  ARG B CA  1 
ATOM   7083 C C   . ARG B 1 422 ? 51.864 37.084 -68.605 1.00 5.88  ? 422  ARG B C   1 
ATOM   7084 O O   . ARG B 1 422 ? 52.684 37.073 -69.522 1.00 7.77  ? 422  ARG B O   1 
ATOM   7085 C CB  . ARG B 1 422 ? 52.321 36.025 -66.378 1.00 6.35  ? 422  ARG B CB  1 
ATOM   7086 C CG  . ARG B 1 422 ? 52.055 34.873 -65.385 1.00 9.03  ? 422  ARG B CG  1 
ATOM   7087 C CD  . ARG B 1 422 ? 52.823 35.109 -64.062 1.00 8.43  ? 422  ARG B CD  1 
ATOM   7088 N NE  . ARG B 1 422 ? 52.434 34.163 -63.019 1.00 8.30  ? 422  ARG B NE  1 
ATOM   7089 C CZ  . ARG B 1 422 ? 53.100 33.053 -62.722 1.00 10.84 ? 422  ARG B CZ  1 
ATOM   7090 N NH1 . ARG B 1 422 ? 54.226 32.729 -63.348 1.00 7.15  ? 422  ARG B NH1 1 
ATOM   7091 N NH2 . ARG B 1 422 ? 52.619 32.240 -61.785 1.00 10.31 ? 422  ARG B NH2 1 
ATOM   7092 N N   . PRO B 1 423 ? 51.147 38.179 -68.337 1.00 8.30  ? 423  PRO B N   1 
ATOM   7093 C CA  . PRO B 1 423 ? 51.308 39.363 -69.209 1.00 9.66  ? 423  PRO B CA  1 
ATOM   7094 C C   . PRO B 1 423 ? 52.732 39.931 -69.246 1.00 9.16  ? 423  PRO B C   1 
ATOM   7095 O O   . PRO B 1 423 ? 53.150 40.461 -70.287 1.00 9.22  ? 423  PRO B O   1 
ATOM   7096 C CB  . PRO B 1 423 ? 50.297 40.363 -68.631 1.00 10.91 ? 423  PRO B CB  1 
ATOM   7097 C CG  . PRO B 1 423 ? 49.214 39.471 -68.023 1.00 12.64 ? 423  PRO B CG  1 
ATOM   7098 C CD  . PRO B 1 423 ? 49.990 38.301 -67.425 1.00 9.20  ? 423  PRO B CD  1 
ATOM   7099 N N   . SER B 1 424 ? 53.491 39.815 -68.151 1.00 7.08  ? 424  SER B N   1 
ATOM   7100 C CA  . SER B 1 424 ? 54.894 40.238 -68.134 1.00 10.82 ? 424  SER B CA  1 
ATOM   7101 C C   . SER B 1 424 ? 55.714 39.522 -69.205 1.00 8.23  ? 424  SER B C   1 
ATOM   7102 O O   . SER B 1 424 ? 56.705 40.067 -69.707 1.00 9.03  ? 424  SER B O   1 
ATOM   7103 C CB  . SER B 1 424 ? 55.492 39.960 -66.751 1.00 7.10  ? 424  SER B CB  1 
ATOM   7104 O OG  . SER B 1 424 ? 55.339 38.579 -66.419 1.00 9.00  ? 424  SER B OG  1 
ATOM   7105 N N   . TYR B 1 425 ? 55.323 38.298 -69.558 1.00 9.50  ? 425  TYR B N   1 
ATOM   7106 C CA  . TYR B 1 425 ? 55.972 37.599 -70.664 1.00 8.04  ? 425  TYR B CA  1 
ATOM   7107 C C   . TYR B 1 425 ? 55.827 38.376 -71.969 1.00 11.62 ? 425  TYR B C   1 
ATOM   7108 O O   . TYR B 1 425 ? 56.802 38.552 -72.717 1.00 9.50  ? 425  TYR B O   1 
ATOM   7109 C CB  . TYR B 1 425 ? 55.373 36.203 -70.780 1.00 8.11  ? 425  TYR B CB  1 
ATOM   7110 C CG  . TYR B 1 425 ? 55.764 35.368 -71.983 1.00 9.77  ? 425  TYR B CG  1 
ATOM   7111 C CD1 . TYR B 1 425 ? 56.881 34.525 -71.946 1.00 8.98  ? 425  TYR B CD1 1 
ATOM   7112 C CD2 . TYR B 1 425 ? 54.975 35.363 -73.124 1.00 9.59  ? 425  TYR B CD2 1 
ATOM   7113 C CE1 . TYR B 1 425 ? 57.213 33.729 -73.049 1.00 9.60  ? 425  TYR B CE1 1 
ATOM   7114 C CE2 . TYR B 1 425 ? 55.272 34.567 -74.209 1.00 11.91 ? 425  TYR B CE2 1 
ATOM   7115 C CZ  . TYR B 1 425 ? 56.384 33.740 -74.168 1.00 14.51 ? 425  TYR B CZ  1 
ATOM   7116 O OH  . TYR B 1 425 ? 56.683 32.973 -75.284 1.00 10.09 ? 425  TYR B OH  1 
ATOM   7117 N N   . TYR B 1 426 ? 54.610 38.845 -72.272 1.00 9.16  ? 426  TYR B N   1 
ATOM   7118 C CA  . TYR B 1 426 ? 54.424 39.587 -73.517 1.00 12.07 ? 426  TYR B CA  1 
ATOM   7119 C C   . TYR B 1 426 ? 55.105 40.944 -73.454 1.00 11.73 ? 426  TYR B C   1 
ATOM   7120 O O   . TYR B 1 426 ? 55.615 41.427 -74.472 1.00 11.34 ? 426  TYR B O   1 
ATOM   7121 C CB  . TYR B 1 426 ? 52.928 39.729 -73.842 1.00 10.13 ? 426  TYR B CB  1 
ATOM   7122 C CG  . TYR B 1 426 ? 52.227 38.388 -73.910 1.00 10.32 ? 426  TYR B CG  1 
ATOM   7123 C CD1 . TYR B 1 426 ? 52.462 37.505 -74.960 1.00 9.28  ? 426  TYR B CD1 1 
ATOM   7124 C CD2 . TYR B 1 426 ? 51.364 37.990 -72.903 1.00 11.28 ? 426  TYR B CD2 1 
ATOM   7125 C CE1 . TYR B 1 426 ? 51.851 36.259 -75.000 1.00 10.84 ? 426  TYR B CE1 1 
ATOM   7126 C CE2 . TYR B 1 426 ? 50.739 36.752 -72.937 1.00 12.44 ? 426  TYR B CE2 1 
ATOM   7127 C CZ  . TYR B 1 426 ? 50.988 35.891 -73.990 1.00 14.19 ? 426  TYR B CZ  1 
ATOM   7128 O OH  . TYR B 1 426 ? 50.378 34.655 -74.013 1.00 16.40 ? 426  TYR B OH  1 
ATOM   7129 N N   . LEU B 1 427 ? 55.136 41.569 -72.277 1.00 11.01 ? 427  LEU B N   1 
ATOM   7130 C CA  . LEU B 1 427 ? 55.864 42.826 -72.135 1.00 10.59 ? 427  LEU B CA  1 
ATOM   7131 C C   . LEU B 1 427 ? 57.351 42.636 -72.409 1.00 10.54 ? 427  LEU B C   1 
ATOM   7132 O O   . LEU B 1 427 ? 57.979 43.472 -73.073 1.00 11.16 ? 427  LEU B O   1 
ATOM   7133 C CB  . LEU B 1 427 ? 55.657 43.399 -70.732 1.00 9.50  ? 427  LEU B CB  1 
ATOM   7134 C CG  . LEU B 1 427 ? 56.480 44.647 -70.382 1.00 11.72 ? 427  LEU B CG  1 
ATOM   7135 C CD1 . LEU B 1 427 ? 56.117 45.807 -71.315 1.00 11.38 ? 427  LEU B CD1 1 
ATOM   7136 C CD2 . LEU B 1 427 ? 56.260 45.039 -68.919 1.00 8.97  ? 427  LEU B CD2 1 
ATOM   7137 N N   . PHE B 1 428 ? 57.935 41.552 -71.880 1.00 10.50 ? 428  PHE B N   1 
ATOM   7138 C CA  . PHE B 1 428 ? 59.345 41.251 -72.128 1.00 10.88 ? 428  PHE B CA  1 
ATOM   7139 C C   . PHE B 1 428 ? 59.616 41.126 -73.623 1.00 11.01 ? 428  PHE B C   1 
ATOM   7140 O O   . PHE B 1 428 ? 60.601 41.681 -74.132 1.00 10.27 ? 428  PHE B O   1 
ATOM   7141 C CB  . PHE B 1 428 ? 59.738 39.965 -71.380 1.00 12.47 ? 428  PHE B CB  1 
ATOM   7142 C CG  . PHE B 1 428 ? 61.233 39.811 -71.133 1.00 13.74 ? 428  PHE B CG  1 
ATOM   7143 C CD1 . PHE B 1 428 ? 62.137 40.789 -71.524 1.00 12.45 ? 428  PHE B CD1 1 
ATOM   7144 C CD2 . PHE B 1 428 ? 61.723 38.687 -70.502 1.00 14.45 ? 428  PHE B CD2 1 
ATOM   7145 C CE1 . PHE B 1 428 ? 63.501 40.642 -71.286 1.00 12.93 ? 428  PHE B CE1 1 
ATOM   7146 C CE2 . PHE B 1 428 ? 63.087 38.537 -70.259 1.00 18.32 ? 428  PHE B CE2 1 
ATOM   7147 C CZ  . PHE B 1 428 ? 63.974 39.514 -70.660 1.00 12.90 ? 428  PHE B CZ  1 
ATOM   7148 N N   . GLY B 1 429 ? 58.721 40.446 -74.349 1.00 9.46  ? 429  GLY B N   1 
ATOM   7149 C CA  . GLY B 1 429 ? 58.873 40.339 -75.798 1.00 13.77 ? 429  GLY B CA  1 
ATOM   7150 C C   . GLY B 1 429 ? 58.853 41.681 -76.502 1.00 15.24 ? 429  GLY B C   1 
ATOM   7151 O O   . GLY B 1 429 ? 59.603 41.904 -77.458 1.00 12.75 ? 429  GLY B O   1 
ATOM   7152 N N   . GLN B 1 430 ? 57.982 42.588 -76.051 1.00 11.45 ? 430  GLN B N   1 
ATOM   7153 C CA  . GLN B 1 430 ? 57.923 43.911 -76.659 1.00 10.56 ? 430  GLN B CA  1 
ATOM   7154 C C   . GLN B 1 430 ? 59.201 44.695 -76.403 1.00 13.13 ? 430  GLN B C   1 
ATOM   7155 O O   . GLN B 1 430 ? 59.694 45.395 -77.299 1.00 13.05 ? 430  GLN B O   1 
ATOM   7156 C CB  . GLN B 1 430 ? 56.699 44.675 -76.131 1.00 12.70 ? 430  GLN B CB  1 
ATOM   7157 C CG  . GLN B 1 430 ? 55.373 44.036 -76.545 1.00 12.63 ? 430  GLN B CG  1 
ATOM   7158 C CD  . GLN B 1 430 ? 55.166 44.157 -78.040 1.00 16.00 ? 430  GLN B CD  1 
ATOM   7159 O OE1 . GLN B 1 430 ? 55.650 45.102 -78.667 1.00 17.36 ? 430  GLN B OE1 1 
ATOM   7160 N NE2 . GLN B 1 430 ? 54.477 43.193 -78.623 1.00 16.01 ? 430  GLN B NE2 1 
ATOM   7161 N N   . ILE B 1 431 ? 59.753 44.596 -75.188 1.00 8.88  ? 431  ILE B N   1 
ATOM   7162 C CA  . ILE B 1 431 ? 61.004 45.289 -74.874 1.00 9.76  ? 431  ILE B CA  1 
ATOM   7163 C C   . ILE B 1 431 ? 62.158 44.729 -75.707 1.00 10.29 ? 431  ILE B C   1 
ATOM   7164 O O   . ILE B 1 431 ? 62.984 45.484 -76.233 1.00 11.68 ? 431  ILE B O   1 
ATOM   7165 C CB  . ILE B 1 431 ? 61.311 45.195 -73.364 1.00 9.13  ? 431  ILE B CB  1 
ATOM   7166 C CG1 . ILE B 1 431 ? 60.225 45.881 -72.541 1.00 9.57  ? 431  ILE B CG1 1 
ATOM   7167 C CG2 . ILE B 1 431 ? 62.686 45.813 -73.051 1.00 13.42 ? 431  ILE B CG2 1 
ATOM   7168 C CD1 . ILE B 1 431 ? 60.293 45.541 -71.021 1.00 10.25 ? 431  ILE B CD1 1 
ATOM   7169 N N   . ILE B 1 432 ? 62.252 43.400 -75.813 1.00 12.02 ? 432  ILE B N   1 
ATOM   7170 C CA  . ILE B 1 432 ? 63.274 42.786 -76.661 1.00 12.84 ? 432  ILE B CA  1 
ATOM   7171 C C   . ILE B 1 432 ? 63.127 43.268 -78.098 1.00 14.45 ? 432  ILE B C   1 
ATOM   7172 O O   . ILE B 1 432 ? 64.111 43.632 -78.750 1.00 14.22 ? 432  ILE B O   1 
ATOM   7173 C CB  . ILE B 1 432 ? 63.196 41.249 -76.569 1.00 13.90 ? 432  ILE B CB  1 
ATOM   7174 C CG1 . ILE B 1 432 ? 63.569 40.784 -75.159 1.00 10.46 ? 432  ILE B CG1 1 
ATOM   7175 C CG2 . ILE B 1 432 ? 64.114 40.600 -77.617 1.00 10.91 ? 432  ILE B CG2 1 
ATOM   7176 C CD1 . ILE B 1 432 ? 63.290 39.293 -74.877 1.00 12.41 ? 432  ILE B CD1 1 
ATOM   7177 N N   . ASN B 1 433 ? 61.893 43.324 -78.601 1.00 13.29 ? 433  ASN B N   1 
ATOM   7178 C CA  . ASN B 1 433 ? 61.718 43.700 -79.998 1.00 18.41 ? 433  ASN B CA  1 
ATOM   7179 C C   . ASN B 1 433 ? 62.087 45.165 -80.216 1.00 20.67 ? 433  ASN B C   1 
ATOM   7180 O O   . ASN B 1 433 ? 62.651 45.520 -81.257 1.00 15.53 ? 433  ASN B O   1 
ATOM   7181 C CB  . ASN B 1 433 ? 60.286 43.429 -80.453 1.00 17.04 ? 433  ASN B CB  1 
ATOM   7182 C CG  . ASN B 1 433 ? 60.091 43.733 -81.922 1.00 25.72 ? 433  ASN B CG  1 
ATOM   7183 O OD1 . ASN B 1 433 ? 60.518 42.954 -82.783 1.00 30.51 ? 433  ASN B OD1 1 
ATOM   7184 N ND2 . ASN B 1 433 ? 59.467 44.862 -82.225 1.00 22.95 ? 433  ASN B ND2 1 
ATOM   7185 N N   . SER B 1 434 ? 61.807 46.022 -79.227 1.00 13.02 ? 434  SER B N   1 
ATOM   7186 C CA  . SER B 1 434 ? 62.171 47.432 -79.320 1.00 16.25 ? 434  SER B CA  1 
ATOM   7187 C C   . SER B 1 434 ? 63.667 47.659 -79.119 1.00 16.23 ? 434  SER B C   1 
ATOM   7188 O O   . SER B 1 434 ? 64.206 48.662 -79.604 1.00 17.04 ? 434  SER B O   1 
ATOM   7189 C CB  . SER B 1 434 ? 61.382 48.244 -78.289 1.00 15.02 ? 434  SER B CB  1 
ATOM   7190 O OG  . SER B 1 434 ? 60.000 48.200 -78.599 1.00 18.13 ? 434  SER B OG  1 
ATOM   7191 N N   . ARG B 1 435 ? 64.336 46.768 -78.383 1.00 12.27 ? 435  ARG B N   1 
ATOM   7192 C CA  . ARG B 1 435 ? 65.751 46.904 -78.030 1.00 17.62 ? 435  ARG B CA  1 
ATOM   7193 C C   . ARG B 1 435 ? 66.017 48.152 -77.184 1.00 18.87 ? 435  ARG B C   1 
ATOM   7194 O O   . ARG B 1 435 ? 67.116 48.717 -77.210 1.00 15.21 ? 435  ARG B O   1 
ATOM   7195 C CB  . ARG B 1 435 ? 66.637 46.885 -79.282 1.00 21.24 ? 435  ARG B CB  1 
ATOM   7196 C CG  . ARG B 1 435 ? 66.654 45.520 -79.998 1.00 23.80 ? 435  ARG B CG  1 
ATOM   7197 C CD  . ARG B 1 435 ? 67.424 45.584 -81.321 1.00 30.82 ? 435  ARG B CD  1 
ATOM   7198 N NE  . ARG B 1 435 ? 68.775 46.083 -81.101 1.00 27.10 ? 435  ARG B NE  1 
ATOM   7199 C CZ  . ARG B 1 435 ? 69.467 46.802 -81.974 1.00 31.41 ? 435  ARG B CZ  1 
ATOM   7200 N NH1 . ARG B 1 435 ? 69.005 47.050 -83.189 1.00 31.19 ? 435  ARG B NH1 1 
ATOM   7201 N NH2 . ARG B 1 435 ? 70.652 47.288 -81.618 1.00 25.39 ? 435  ARG B NH2 1 
ATOM   7202 N N   . THR B 1 436 ? 65.018 48.588 -76.419 1.00 13.53 ? 436  THR B N   1 
ATOM   7203 C CA  . THR B 1 436 ? 65.183 49.701 -75.495 1.00 13.64 ? 436  THR B CA  1 
ATOM   7204 C C   . THR B 1 436 ? 63.945 49.770 -74.611 1.00 14.40 ? 436  THR B C   1 
ATOM   7205 O O   . THR B 1 436 ? 62.851 49.384 -75.034 1.00 11.21 ? 436  THR B O   1 
ATOM   7206 C CB  . THR B 1 436 ? 65.399 51.036 -76.236 1.00 14.88 ? 436  THR B CB  1 
ATOM   7207 O OG1 . THR B 1 436 ? 65.449 52.127 -75.294 1.00 13.58 ? 436  THR B OG1 1 
ATOM   7208 C CG2 . THR B 1 436 ? 64.303 51.272 -77.271 1.00 15.48 ? 436  THR B CG2 1 
ATOM   7209 N N   . THR B 1 437 ? 64.131 50.253 -73.381 1.00 12.21 ? 437  THR B N   1 
ATOM   7210 C CA  . THR B 1 437 ? 63.007 50.479 -72.475 1.00 13.27 ? 437  THR B CA  1 
ATOM   7211 C C   . THR B 1 437 ? 62.334 51.826 -72.696 1.00 15.81 ? 437  THR B C   1 
ATOM   7212 O O   . THR B 1 437 ? 61.279 52.079 -72.097 1.00 12.82 ? 437  THR B O   1 
ATOM   7213 C CB  . THR B 1 437 ? 63.458 50.401 -71.016 1.00 12.06 ? 437  THR B CB  1 
ATOM   7214 O OG1 . THR B 1 437 ? 64.475 51.386 -70.769 1.00 14.48 ? 437  THR B OG1 1 
ATOM   7215 C CG2 . THR B 1 437 ? 63.991 49.003 -70.670 1.00 12.09 ? 437  THR B CG2 1 
ATOM   7216 N N   . GLU B 1 438 ? 62.916 52.689 -73.529 1.00 12.54 ? 438  GLU B N   1 
ATOM   7217 C CA  . GLU B 1 438 ? 62.438 54.066 -73.614 1.00 16.61 ? 438  GLU B CA  1 
ATOM   7218 C C   . GLU B 1 438 ? 60.949 54.171 -73.961 1.00 15.52 ? 438  GLU B C   1 
ATOM   7219 O O   . GLU B 1 438 ? 60.261 54.984 -73.319 1.00 13.39 ? 438  GLU B O   1 
ATOM   7220 C CB  . GLU B 1 438 ? 63.316 54.852 -74.604 1.00 18.84 ? 438  GLU B CB  1 
ATOM   7221 C CG  . GLU B 1 438 ? 62.998 56.350 -74.666 1.00 24.73 ? 438  GLU B CG  1 
ATOM   7222 C CD  . GLU B 1 438 ? 61.818 56.689 -75.580 1.00 33.51 ? 438  GLU B CD  1 
ATOM   7223 O OE1 . GLU B 1 438 ? 61.348 55.807 -76.337 1.00 33.82 ? 438  GLU B OE1 1 
ATOM   7224 O OE2 . GLU B 1 438 ? 61.335 57.844 -75.507 1.00 42.38 ? 438  GLU B OE2 1 
ATOM   7225 N N   . PRO B 1 439 ? 60.389 53.403 -74.908 1.00 14.18 ? 439  PRO B N   1 
ATOM   7226 C CA  . PRO B 1 439 ? 58.946 53.513 -75.200 1.00 15.82 ? 439  PRO B CA  1 
ATOM   7227 C C   . PRO B 1 439 ? 58.034 53.012 -74.086 1.00 12.64 ? 439  PRO B C   1 
ATOM   7228 O O   . PRO B 1 439 ? 56.805 53.087 -74.235 1.00 12.07 ? 439  PRO B O   1 
ATOM   7229 C CB  . PRO B 1 439 ? 58.763 52.620 -76.442 1.00 16.96 ? 439  PRO B CB  1 
ATOM   7230 C CG  . PRO B 1 439 ? 60.125 52.352 -76.960 1.00 18.52 ? 439  PRO B CG  1 
ATOM   7231 C CD  . PRO B 1 439 ? 61.045 52.424 -75.798 1.00 15.53 ? 439  PRO B CD  1 
ATOM   7232 N N   . PHE B 1 440 ? 58.576 52.446 -73.008 1.00 12.09 ? 440  PHE B N   1 
ATOM   7233 C CA  . PHE B 1 440 ? 57.754 51.847 -71.963 1.00 11.89 ? 440  PHE B CA  1 
ATOM   7234 C C   . PHE B 1 440 ? 57.841 52.581 -70.641 1.00 10.47 ? 440  PHE B C   1 
ATOM   7235 O O   . PHE B 1 440 ? 57.071 52.263 -69.724 1.00 11.45 ? 440  PHE B O   1 
ATOM   7236 C CB  . PHE B 1 440 ? 58.157 50.379 -71.745 1.00 11.05 ? 440  PHE B CB  1 
ATOM   7237 C CG  . PHE B 1 440 ? 58.186 49.581 -73.007 1.00 11.20 ? 440  PHE B CG  1 
ATOM   7238 C CD1 . PHE B 1 440 ? 59.337 49.547 -73.800 1.00 9.50  ? 440  PHE B CD1 1 
ATOM   7239 C CD2 . PHE B 1 440 ? 57.056 48.887 -73.425 1.00 8.05  ? 440  PHE B CD2 1 
ATOM   7240 C CE1 . PHE B 1 440 ? 59.364 48.824 -74.985 1.00 11.91 ? 440  PHE B CE1 1 
ATOM   7241 C CE2 . PHE B 1 440 ? 57.077 48.160 -74.616 1.00 14.83 ? 440  PHE B CE2 1 
ATOM   7242 C CZ  . PHE B 1 440 ? 58.233 48.126 -75.393 1.00 10.45 ? 440  PHE B CZ  1 
ATOM   7243 N N   . LEU B 1 441 ? 58.747 53.554 -70.526 1.00 9.77  ? 441  LEU B N   1 
ATOM   7244 C CA  . LEU B 1 441 ? 59.099 54.111 -69.225 1.00 11.64 ? 441  LEU B CA  1 
ATOM   7245 C C   . LEU B 1 441 ? 57.917 54.771 -68.528 1.00 14.29 ? 441  LEU B C   1 
ATOM   7246 O O   . LEU B 1 441 ? 57.879 54.817 -67.294 1.00 11.58 ? 441  LEU B O   1 
ATOM   7247 C CB  . LEU B 1 441 ? 60.233 55.127 -69.385 1.00 14.14 ? 441  LEU B CB  1 
ATOM   7248 C CG  . LEU B 1 441 ? 61.568 54.526 -69.825 1.00 16.84 ? 441  LEU B CG  1 
ATOM   7249 C CD1 . LEU B 1 441 ? 62.589 55.641 -69.940 1.00 18.24 ? 441  LEU B CD1 1 
ATOM   7250 C CD2 . LEU B 1 441 ? 62.017 53.436 -68.838 1.00 15.54 ? 441  LEU B CD2 1 
ATOM   7251 N N   . ASN B 1 442 ? 56.952 55.299 -69.285 1.00 13.55 ? 442  ASN B N   1 
ATOM   7252 C CA  . ASN B 1 442 ? 55.848 56.001 -68.632 1.00 15.66 ? 442  ASN B CA  1 
ATOM   7253 C C   . ASN B 1 442 ? 55.022 55.076 -67.746 1.00 13.35 ? 442  ASN B C   1 
ATOM   7254 O O   . ASN B 1 442 ? 54.352 55.554 -66.818 1.00 9.99  ? 442  ASN B O   1 
ATOM   7255 C CB  . ASN B 1 442 ? 54.951 56.674 -69.675 1.00 11.86 ? 442  ASN B CB  1 
ATOM   7256 C CG  . ASN B 1 442 ? 54.086 57.759 -69.072 1.00 16.28 ? 442  ASN B CG  1 
ATOM   7257 O OD1 . ASN B 1 442 ? 54.587 58.797 -68.635 1.00 19.43 ? 442  ASN B OD1 1 
ATOM   7258 N ND2 . ASN B 1 442 ? 52.789 57.522 -69.029 1.00 8.47  ? 442  ASN B ND2 1 
ATOM   7259 N N   . LEU B 1 443 ? 55.052 53.765 -68.005 1.00 9.26  ? 443  LEU B N   1 
ATOM   7260 C CA  . LEU B 1 443 ? 54.370 52.825 -67.122 1.00 11.96 ? 443  LEU B CA  1 
ATOM   7261 C C   . LEU B 1 443 ? 54.884 52.943 -65.690 1.00 15.64 ? 443  LEU B C   1 
ATOM   7262 O O   . LEU B 1 443 ? 54.119 52.754 -64.736 1.00 14.09 ? 443  LEU B O   1 
ATOM   7263 C CB  . LEU B 1 443 ? 54.567 51.397 -67.633 1.00 12.09 ? 443  LEU B CB  1 
ATOM   7264 C CG  . LEU B 1 443 ? 53.960 51.106 -69.017 1.00 11.43 ? 443  LEU B CG  1 
ATOM   7265 C CD1 . LEU B 1 443 ? 54.172 49.643 -69.413 1.00 13.61 ? 443  LEU B CD1 1 
ATOM   7266 C CD2 . LEU B 1 443 ? 52.475 51.467 -69.057 1.00 10.72 ? 443  LEU B CD2 1 
ATOM   7267 N N   . LEU B 1 444 ? 56.165 53.277 -65.515 1.00 13.15 ? 444  LEU B N   1 
ATOM   7268 C CA  . LEU B 1 444 ? 56.726 53.358 -64.171 1.00 14.71 ? 444  LEU B CA  1 
ATOM   7269 C C   . LEU B 1 444 ? 56.119 54.484 -63.338 1.00 15.98 ? 444  LEU B C   1 
ATOM   7270 O O   . LEU B 1 444 ? 56.189 54.427 -62.109 1.00 15.86 ? 444  LEU B O   1 
ATOM   7271 C CB  . LEU B 1 444 ? 58.245 53.536 -64.250 1.00 13.81 ? 444  LEU B CB  1 
ATOM   7272 C CG  . LEU B 1 444 ? 58.998 52.424 -64.985 1.00 16.06 ? 444  LEU B CG  1 
ATOM   7273 C CD1 . LEU B 1 444 ? 60.492 52.751 -65.081 1.00 19.47 ? 444  LEU B CD1 1 
ATOM   7274 C CD2 . LEU B 1 444 ? 58.779 51.072 -64.316 1.00 13.89 ? 444  LEU B CD2 1 
ATOM   7275 N N   . LYS B 1 445 ? 55.520 55.505 -63.960 1.00 12.88 ? 445  LYS B N   1 
ATOM   7276 C CA  . LYS B 1 445 ? 54.959 56.588 -63.157 1.00 14.39 ? 445  LYS B CA  1 
ATOM   7277 C C   . LYS B 1 445 ? 53.795 56.123 -62.288 1.00 15.38 ? 445  LYS B C   1 
ATOM   7278 O O   . LYS B 1 445 ? 53.518 56.739 -61.250 1.00 18.23 ? 445  LYS B O   1 
ATOM   7279 C CB  . LYS B 1 445 ? 54.530 57.751 -64.041 1.00 16.35 ? 445  LYS B CB  1 
ATOM   7280 C CG  . LYS B 1 445 ? 55.668 58.343 -64.842 1.00 22.06 ? 445  LYS B CG  1 
ATOM   7281 C CD  . LYS B 1 445 ? 55.186 59.515 -65.688 1.00 25.90 ? 445  LYS B CD  1 
ATOM   7282 C CE  . LYS B 1 445 ? 56.064 60.754 -65.525 1.00 37.58 ? 445  LYS B CE  1 
ATOM   7283 N NZ  . LYS B 1 445 ? 55.422 61.953 -66.171 1.00 36.09 ? 445  LYS B NZ  1 
ATOM   7284 N N   . ALA B 1 446 ? 53.103 55.051 -62.682 1.00 14.65 ? 446  ALA B N   1 
ATOM   7285 C CA  . ALA B 1 446 ? 52.002 54.544 -61.863 1.00 15.37 ? 446  ALA B CA  1 
ATOM   7286 C C   . ALA B 1 446 ? 52.475 54.082 -60.492 1.00 19.69 ? 446  ALA B C   1 
ATOM   7287 O O   . ALA B 1 446 ? 51.676 54.024 -59.549 1.00 18.68 ? 446  ALA B O   1 
ATOM   7288 C CB  . ALA B 1 446 ? 51.296 53.386 -62.571 1.00 11.13 ? 446  ALA B CB  1 
ATOM   7289 N N   . TRP B 1 447 ? 53.746 53.730 -60.369 1.00 18.56 ? 447  TRP B N   1 
ATOM   7290 C CA  . TRP B 1 447 ? 54.322 53.290 -59.110 1.00 22.71 ? 447  TRP B CA  1 
ATOM   7291 C C   . TRP B 1 447 ? 55.088 54.406 -58.416 1.00 34.91 ? 447  TRP B C   1 
ATOM   7292 O O   . TRP B 1 447 ? 55.652 54.178 -57.342 1.00 36.97 ? 447  TRP B O   1 
ATOM   7293 C CB  . TRP B 1 447 ? 55.229 52.080 -59.354 1.00 19.13 ? 447  TRP B CB  1 
ATOM   7294 C CG  . TRP B 1 447 ? 54.512 50.915 -60.052 1.00 18.49 ? 447  TRP B CG  1 
ATOM   7295 C CD1 . TRP B 1 447 ? 54.212 50.797 -61.395 1.00 17.55 ? 447  TRP B CD1 1 
ATOM   7296 C CD2 . TRP B 1 447 ? 54.025 49.718 -59.431 1.00 18.38 ? 447  TRP B CD2 1 
ATOM   7297 N NE1 . TRP B 1 447 ? 53.570 49.597 -61.633 1.00 18.79 ? 447  TRP B NE1 1 
ATOM   7298 C CE2 . TRP B 1 447 ? 53.449 48.919 -60.444 1.00 18.03 ? 447  TRP B CE2 1 
ATOM   7299 C CE3 . TRP B 1 447 ? 54.033 49.239 -58.119 1.00 20.06 ? 447  TRP B CE3 1 
ATOM   7300 C CZ2 . TRP B 1 447 ? 52.878 47.675 -60.177 1.00 21.50 ? 447  TRP B CZ2 1 
ATOM   7301 C CZ3 . TRP B 1 447 ? 53.467 48.000 -57.856 1.00 26.48 ? 447  TRP B CZ3 1 
ATOM   7302 C CH2 . TRP B 1 447 ? 52.900 47.233 -58.879 1.00 22.37 ? 447  TRP B CH2 1 
ATOM   7303 N N   . GLU B 1 448 ? 55.088 55.606 -59.002 1.00 34.08 ? 448  GLU B N   1 
ATOM   7304 C CA  . GLU B 1 448 ? 55.762 56.801 -58.486 1.00 43.24 ? 448  GLU B CA  1 
ATOM   7305 C C   . GLU B 1 448 ? 57.275 56.608 -58.507 1.00 43.44 ? 448  GLU B C   1 
ATOM   7306 O O   . GLU B 1 448 ? 57.790 55.736 -59.218 1.00 47.56 ? 448  GLU B O   1 
ATOM   7307 C CB  . GLU B 1 448 ? 55.274 57.141 -57.071 1.00 47.29 ? 448  GLU B CB  1 
ATOM   7308 C CG  . GLU B 1 448 ? 53.762 57.323 -56.954 1.00 44.14 ? 448  GLU B CG  1 
ATOM   7309 C CD  . GLU B 1 448 ? 53.321 57.635 -55.528 1.00 62.12 ? 448  GLU B CD  1 
ATOM   7310 O OE1 . GLU B 1 448 ? 54.127 57.413 -54.596 1.00 61.71 ? 448  GLU B OE1 1 
ATOM   7311 O OE2 . GLU B 1 448 ? 52.174 58.103 -55.339 1.00 62.83 ? 448  GLU B OE2 1 
HETATM 7312 C C1  . GOL C 2 .   ? 55.638 30.193 -20.343 1.00 18.22 ? 501  GOL A C1  1 
HETATM 7313 O O1  . GOL C 2 .   ? 55.260 29.597 -19.128 1.00 12.66 ? 501  GOL A O1  1 
HETATM 7314 C C2  . GOL C 2 .   ? 56.006 31.671 -20.142 1.00 14.90 ? 501  GOL A C2  1 
HETATM 7315 O O2  . GOL C 2 .   ? 57.345 31.736 -19.682 1.00 11.13 ? 501  GOL A O2  1 
HETATM 7316 C C3  . GOL C 2 .   ? 55.870 32.415 -21.490 1.00 15.15 ? 501  GOL A C3  1 
HETATM 7317 O O3  . GOL C 2 .   ? 56.590 33.615 -21.459 1.00 19.58 ? 501  GOL A O3  1 
HETATM 7318 C C1  . GOL D 2 .   ? 69.153 30.943 -57.186 1.00 16.03 ? 501  GOL B C1  1 
HETATM 7319 O O1  . GOL D 2 .   ? 70.091 30.557 -58.157 1.00 14.89 ? 501  GOL B O1  1 
HETATM 7320 C C2  . GOL D 2 .   ? 67.876 30.090 -57.225 1.00 13.08 ? 501  GOL B C2  1 
HETATM 7321 O O2  . GOL D 2 .   ? 67.938 28.835 -57.858 1.00 10.12 ? 501  GOL B O2  1 
HETATM 7322 C C3  . GOL D 2 .   ? 66.549 30.835 -57.373 1.00 15.77 ? 501  GOL B C3  1 
HETATM 7323 O O3  . GOL D 2 .   ? 65.478 30.000 -57.004 1.00 16.64 ? 501  GOL B O3  1 
HETATM 7324 O O   . HOH E 3 .   ? 42.784 11.985 -34.947 1.00 32.70 ? 601  HOH A O   1 
HETATM 7325 O O   . HOH E 3 .   ? 29.044 34.040 -11.824 1.00 41.59 ? 602  HOH A O   1 
HETATM 7326 O O   . HOH E 3 .   ? 32.970 16.115 -17.309 1.00 41.36 ? 603  HOH A O   1 
HETATM 7327 O O   . HOH E 3 .   ? 65.249 47.802 -6.330  1.00 50.57 ? 604  HOH A O   1 
HETATM 7328 O O   . HOH E 3 .   ? 50.346 21.477 -25.938 1.00 27.32 ? 605  HOH A O   1 
HETATM 7329 O O   . HOH E 3 .   ? 48.991 22.364 5.080   1.00 45.75 ? 606  HOH A O   1 
HETATM 7330 O O   . HOH E 3 .   ? 25.359 44.563 -13.935 1.00 36.18 ? 607  HOH A O   1 
HETATM 7331 O O   . HOH E 3 .   ? 55.376 11.479 -47.571 1.00 35.21 ? 608  HOH A O   1 
HETATM 7332 O O   . HOH E 3 .   ? 29.214 33.452 -17.615 1.00 28.27 ? 609  HOH A O   1 
HETATM 7333 O O   . HOH E 3 .   ? 70.120 7.512  -14.928 1.00 37.38 ? 610  HOH A O   1 
HETATM 7334 O O   . HOH E 3 .   ? 50.381 47.333 -34.889 1.00 30.00 ? 611  HOH A O   1 
HETATM 7335 O O   . HOH E 3 .   ? 75.282 13.300 -20.026 1.00 28.60 ? 612  HOH A O   1 
HETATM 7336 O O   . HOH E 3 .   ? 68.289 42.230 -10.521 1.00 14.09 ? 613  HOH A O   1 
HETATM 7337 O O   . HOH E 3 .   ? 34.960 35.981 -6.148  1.00 38.40 ? 614  HOH A O   1 
HETATM 7338 O O   . HOH E 3 .   ? 51.198 17.765 0.815   1.00 35.06 ? 615  HOH A O   1 
HETATM 7339 O O   . HOH E 3 .   ? 41.667 9.124  -25.325 1.00 34.57 ? 616  HOH A O   1 
HETATM 7340 O O   . HOH E 3 .   ? 44.799 9.695  -23.615 1.00 25.03 ? 617  HOH A O   1 
HETATM 7341 O O   . HOH E 3 .   ? 29.430 42.626 -8.195  1.00 32.57 ? 618  HOH A O   1 
HETATM 7342 O O   . HOH E 3 .   ? 78.556 30.623 -26.722 1.00 18.48 ? 619  HOH A O   1 
HETATM 7343 O O   . HOH E 3 .   ? 55.034 28.827 -23.606 1.00 22.37 ? 620  HOH A O   1 
HETATM 7344 O O   . HOH E 3 .   ? 32.970 19.163 -19.047 1.00 36.43 ? 621  HOH A O   1 
HETATM 7345 O O   . HOH E 3 .   ? 66.212 24.434 -20.758 1.00 13.58 ? 622  HOH A O   1 
HETATM 7346 O O   . HOH E 3 .   ? 59.581 31.686 5.225   1.00 17.29 ? 623  HOH A O   1 
HETATM 7347 O O   . HOH E 3 .   ? 68.738 10.266 -13.065 1.00 22.04 ? 624  HOH A O   1 
HETATM 7348 O O   . HOH E 3 .   ? 29.521 24.149 -22.066 1.00 40.11 ? 625  HOH A O   1 
HETATM 7349 O O   . HOH E 3 .   ? 50.144 37.106 -27.900 1.00 8.41  ? 626  HOH A O   1 
HETATM 7350 O O   . HOH E 3 .   ? 49.920 3.426  -36.326 1.00 32.86 ? 627  HOH A O   1 
HETATM 7351 O O   . HOH E 3 .   ? 69.905 46.940 -15.996 1.00 23.35 ? 628  HOH A O   1 
HETATM 7352 O O   . HOH E 3 .   ? 75.021 39.942 -32.165 1.00 22.11 ? 629  HOH A O   1 
HETATM 7353 O O   . HOH E 3 .   ? 57.809 7.772  -9.319  1.00 38.14 ? 630  HOH A O   1 
HETATM 7354 O O   . HOH E 3 .   ? 48.059 8.535  -23.195 1.00 18.62 ? 631  HOH A O   1 
HETATM 7355 O O   . HOH E 3 .   ? 65.234 48.230 -10.191 1.00 25.42 ? 632  HOH A O   1 
HETATM 7356 O O   . HOH E 3 .   ? 34.033 47.141 -9.939  1.00 20.40 ? 633  HOH A O   1 
HETATM 7357 O O   . HOH E 3 .   ? 37.851 18.140 -8.781  1.00 29.29 ? 634  HOH A O   1 
HETATM 7358 O O   . HOH E 3 .   ? 33.191 44.467 -35.068 1.00 38.98 ? 635  HOH A O   1 
HETATM 7359 O O   . HOH E 3 .   ? 53.645 17.582 -30.910 1.00 21.35 ? 636  HOH A O   1 
HETATM 7360 O O   . HOH E 3 .   ? 42.448 27.389 -4.096  1.00 25.81 ? 637  HOH A O   1 
HETATM 7361 O O   . HOH E 3 .   ? 74.813 33.981 -3.500  1.00 21.07 ? 638  HOH A O   1 
HETATM 7362 O O   . HOH E 3 .   ? 70.214 18.678 -24.428 1.00 7.80  ? 639  HOH A O   1 
HETATM 7363 O O   . HOH E 3 .   ? 41.520 17.507 -44.042 1.00 34.43 ? 640  HOH A O   1 
HETATM 7364 O O   . HOH E 3 .   ? 73.358 32.268 5.768   1.00 36.04 ? 641  HOH A O   1 
HETATM 7365 O O   . HOH E 3 .   ? 56.632 37.312 -21.333 1.00 9.10  ? 642  HOH A O   1 
HETATM 7366 O O   . HOH E 3 .   ? 74.100 30.693 -6.033  1.00 15.68 ? 643  HOH A O   1 
HETATM 7367 O O   . HOH E 3 .   ? 51.636 27.896 -23.339 1.00 18.93 ? 644  HOH A O   1 
HETATM 7368 O O   . HOH E 3 .   ? 59.668 30.495 -30.187 1.00 20.04 ? 645  HOH A O   1 
HETATM 7369 O O   . HOH E 3 .   ? 73.745 41.845 -26.932 1.00 19.69 ? 646  HOH A O   1 
HETATM 7370 O O   . HOH E 3 .   ? 50.321 30.508 -12.307 1.00 9.43  ? 647  HOH A O   1 
HETATM 7371 O O   . HOH E 3 .   ? 73.758 30.684 -10.034 1.00 18.54 ? 648  HOH A O   1 
HETATM 7372 O O   . HOH E 3 .   ? 68.332 38.630 0.788   1.00 20.22 ? 649  HOH A O   1 
HETATM 7373 O O   . HOH E 3 .   ? 59.868 23.944 -17.030 1.00 8.54  ? 650  HOH A O   1 
HETATM 7374 O O   . HOH E 3 .   ? 54.974 10.177 -0.844  1.00 22.10 ? 651  HOH A O   1 
HETATM 7375 O O   . HOH E 3 .   ? 75.537 40.808 -28.640 1.00 21.66 ? 652  HOH A O   1 
HETATM 7376 O O   . HOH E 3 .   ? 61.790 44.776 -2.952  1.00 12.43 ? 653  HOH A O   1 
HETATM 7377 O O   . HOH E 3 .   ? 43.512 50.096 -25.676 1.00 35.15 ? 654  HOH A O   1 
HETATM 7378 O O   . HOH E 3 .   ? 78.832 16.546 -7.620  1.00 27.68 ? 655  HOH A O   1 
HETATM 7379 O O   . HOH E 3 .   ? 74.380 46.863 -22.710 1.00 38.74 ? 656  HOH A O   1 
HETATM 7380 O O   . HOH E 3 .   ? 37.216 40.935 -33.474 1.00 34.54 ? 657  HOH A O   1 
HETATM 7381 O O   . HOH E 3 .   ? 55.309 42.854 -33.010 1.00 27.06 ? 658  HOH A O   1 
HETATM 7382 O O   . HOH E 3 .   ? 72.932 11.699 -10.752 1.00 33.88 ? 659  HOH A O   1 
HETATM 7383 O O   . HOH E 3 .   ? 69.735 11.431 -2.037  1.00 41.75 ? 660  HOH A O   1 
HETATM 7384 O O   . HOH E 3 .   ? 77.117 32.274 -24.820 1.00 12.58 ? 661  HOH A O   1 
HETATM 7385 O O   . HOH E 3 .   ? 68.528 32.283 -13.769 1.00 8.82  ? 662  HOH A O   1 
HETATM 7386 O O   . HOH E 3 .   ? 69.578 50.794 -16.683 1.00 34.67 ? 663  HOH A O   1 
HETATM 7387 O O   . HOH E 3 .   ? 37.876 25.594 -36.266 1.00 28.41 ? 664  HOH A O   1 
HETATM 7388 O O   . HOH E 3 .   ? 65.166 10.360 -35.116 1.00 18.46 ? 665  HOH A O   1 
HETATM 7389 O O   . HOH E 3 .   ? 33.387 48.256 -33.353 1.00 28.46 ? 666  HOH A O   1 
HETATM 7390 O O   . HOH E 3 .   ? 54.238 17.258 -26.651 1.00 11.41 ? 667  HOH A O   1 
HETATM 7391 O O   . HOH E 3 .   ? 77.770 25.142 -13.153 1.00 19.40 ? 668  HOH A O   1 
HETATM 7392 O O   . HOH E 3 .   ? 48.753 32.216 3.051   1.00 29.67 ? 669  HOH A O   1 
HETATM 7393 O O   . HOH E 3 .   ? 45.975 41.189 -1.731  1.00 21.71 ? 670  HOH A O   1 
HETATM 7394 O O   . HOH E 3 .   ? 50.657 51.943 -33.240 1.00 32.44 ? 671  HOH A O   1 
HETATM 7395 O O   . HOH E 3 .   ? 79.790 26.304 -23.781 1.00 24.55 ? 672  HOH A O   1 
HETATM 7396 O O   . HOH E 3 .   ? 38.353 36.435 -30.995 1.00 21.06 ? 673  HOH A O   1 
HETATM 7397 O O   . HOH E 3 .   ? 48.147 25.684 1.476   1.00 29.02 ? 674  HOH A O   1 
HETATM 7398 O O   . HOH E 3 .   ? 63.406 22.666 -17.862 1.00 9.79  ? 675  HOH A O   1 
HETATM 7399 O O   . HOH E 3 .   ? 46.523 25.482 -29.043 1.00 11.01 ? 676  HOH A O   1 
HETATM 7400 O O   . HOH E 3 .   ? 77.646 37.491 -25.311 1.00 32.19 ? 677  HOH A O   1 
HETATM 7401 O O   . HOH E 3 .   ? 48.755 27.326 -32.628 1.00 21.98 ? 678  HOH A O   1 
HETATM 7402 O O   . HOH E 3 .   ? 79.682 20.027 -6.442  1.00 26.34 ? 679  HOH A O   1 
HETATM 7403 O O   . HOH E 3 .   ? 44.142 23.416 -4.592  1.00 27.57 ? 680  HOH A O   1 
HETATM 7404 O O   . HOH E 3 .   ? 47.143 26.753 -36.783 1.00 19.22 ? 681  HOH A O   1 
HETATM 7405 O O   . HOH E 3 .   ? 62.117 6.512  -30.202 1.00 9.06  ? 682  HOH A O   1 
HETATM 7406 O O   . HOH E 3 .   ? 60.794 9.761  -5.354  1.00 22.71 ? 683  HOH A O   1 
HETATM 7407 O O   . HOH E 3 .   ? 61.565 34.454 -8.835  1.00 8.26  ? 684  HOH A O   1 
HETATM 7408 O O   . HOH E 3 .   ? 54.370 49.106 -6.626  1.00 18.72 ? 685  HOH A O   1 
HETATM 7409 O O   . HOH E 3 .   ? 44.947 7.890  -13.937 1.00 37.49 ? 686  HOH A O   1 
HETATM 7410 O O   . HOH E 3 .   ? 77.060 19.056 -22.962 1.00 12.65 ? 687  HOH A O   1 
HETATM 7411 O O   . HOH E 3 .   ? 42.973 12.697 -28.241 1.00 23.05 ? 688  HOH A O   1 
HETATM 7412 O O   . HOH E 3 .   ? 43.053 32.946 -26.971 1.00 8.61  ? 689  HOH A O   1 
HETATM 7413 O O   . HOH E 3 .   ? 55.094 43.665 -27.481 1.00 9.58  ? 690  HOH A O   1 
HETATM 7414 O O   . HOH E 3 .   ? 69.513 38.355 -33.092 1.00 18.11 ? 691  HOH A O   1 
HETATM 7415 O O   . HOH E 3 .   ? 40.140 28.922 -5.041  1.00 16.17 ? 692  HOH A O   1 
HETATM 7416 O O   . HOH E 3 .   ? 43.738 10.314 -27.019 1.00 30.33 ? 693  HOH A O   1 
HETATM 7417 O O   . HOH E 3 .   ? 68.021 10.858 -15.436 1.00 21.91 ? 694  HOH A O   1 
HETATM 7418 O O   . HOH E 3 .   ? 60.809 51.876 -22.797 1.00 19.59 ? 695  HOH A O   1 
HETATM 7419 O O   . HOH E 3 .   ? 64.167 41.934 -28.845 1.00 31.57 ? 696  HOH A O   1 
HETATM 7420 O O   . HOH E 3 .   ? 49.065 18.244 -43.938 1.00 31.64 ? 697  HOH A O   1 
HETATM 7421 O O   . HOH E 3 .   ? 62.142 30.193 -12.154 1.00 11.68 ? 698  HOH A O   1 
HETATM 7422 O O   . HOH E 3 .   ? 32.259 22.097 -17.234 1.00 28.43 ? 699  HOH A O   1 
HETATM 7423 O O   . HOH E 3 .   ? 75.306 39.622 -35.888 1.00 29.52 ? 700  HOH A O   1 
HETATM 7424 O O   . HOH E 3 .   ? 43.612 17.048 -5.150  1.00 23.53 ? 701  HOH A O   1 
HETATM 7425 O O   . HOH E 3 .   ? 64.304 22.233 -31.821 1.00 8.37  ? 702  HOH A O   1 
HETATM 7426 O O   . HOH E 3 .   ? 77.731 25.060 -3.565  1.00 29.25 ? 703  HOH A O   1 
HETATM 7427 O O   . HOH E 3 .   ? 64.540 25.728 -11.635 1.00 7.89  ? 704  HOH A O   1 
HETATM 7428 O O   . HOH E 3 .   ? 46.995 28.454 1.790   1.00 36.41 ? 705  HOH A O   1 
HETATM 7429 O O   . HOH E 3 .   ? 66.468 36.957 -14.472 1.00 13.82 ? 706  HOH A O   1 
HETATM 7430 O O   . HOH E 3 .   ? 52.489 31.094 7.922   1.00 29.21 ? 707  HOH A O   1 
HETATM 7431 O O   . HOH E 3 .   ? 49.185 22.432 -43.010 1.00 32.50 ? 708  HOH A O   1 
HETATM 7432 O O   . HOH E 3 .   ? 31.539 29.133 -22.572 1.00 23.86 ? 709  HOH A O   1 
HETATM 7433 O O   . HOH E 3 .   ? 57.010 52.039 -17.388 1.00 9.66  ? 710  HOH A O   1 
HETATM 7434 O O   . HOH E 3 .   ? 72.783 12.385 -22.952 1.00 23.64 ? 711  HOH A O   1 
HETATM 7435 O O   . HOH E 3 .   ? 40.028 45.068 -7.068  1.00 19.71 ? 712  HOH A O   1 
HETATM 7436 O O   . HOH E 3 .   ? 47.083 9.239  -40.637 1.00 35.97 ? 713  HOH A O   1 
HETATM 7437 O O   . HOH E 3 .   ? 60.197 39.511 3.588   1.00 15.62 ? 714  HOH A O   1 
HETATM 7438 O O   . HOH E 3 .   ? 68.209 27.053 -33.999 1.00 25.91 ? 715  HOH A O   1 
HETATM 7439 O O   . HOH E 3 .   ? 63.380 40.902 -17.025 1.00 9.30  ? 716  HOH A O   1 
HETATM 7440 O O   . HOH E 3 .   ? 44.246 36.270 -26.403 1.00 13.20 ? 717  HOH A O   1 
HETATM 7441 O O   . HOH E 3 .   ? 57.099 22.907 2.413   1.00 17.86 ? 718  HOH A O   1 
HETATM 7442 O O   . HOH E 3 .   ? 58.684 8.388  -18.429 1.00 10.77 ? 719  HOH A O   1 
HETATM 7443 O O   . HOH E 3 .   ? 58.447 21.211 4.957   1.00 25.58 ? 720  HOH A O   1 
HETATM 7444 O O   . HOH E 3 .   ? 29.987 45.698 -9.803  1.00 36.04 ? 721  HOH A O   1 
HETATM 7445 O O   . HOH E 3 .   ? 68.940 37.297 -25.983 1.00 10.22 ? 722  HOH A O   1 
HETATM 7446 O O   . HOH E 3 .   ? 70.388 32.476 -15.781 1.00 9.47  ? 723  HOH A O   1 
HETATM 7447 O O   . HOH E 3 .   ? 36.543 28.881 -35.898 1.00 40.62 ? 724  HOH A O   1 
HETATM 7448 O O   . HOH E 3 .   ? 61.265 27.647 -11.511 1.00 10.13 ? 725  HOH A O   1 
HETATM 7449 O O   . HOH E 3 .   ? 64.361 53.770 -21.795 1.00 33.36 ? 726  HOH A O   1 
HETATM 7450 O O   . HOH E 3 .   ? 49.242 53.909 -15.118 1.00 12.47 ? 727  HOH A O   1 
HETATM 7451 O O   . HOH E 3 .   ? 56.545 11.758 6.156   1.00 42.33 ? 728  HOH A O   1 
HETATM 7452 O O   . HOH E 3 .   ? 78.094 27.933 -10.350 1.00 30.43 ? 729  HOH A O   1 
HETATM 7453 O O   . HOH E 3 .   ? 61.874 41.517 2.553   1.00 19.84 ? 730  HOH A O   1 
HETATM 7454 O O   . HOH E 3 .   ? 66.345 21.251 3.278   1.00 28.29 ? 731  HOH A O   1 
HETATM 7455 O O   . HOH E 3 .   ? 67.242 34.748 -12.934 1.00 12.08 ? 732  HOH A O   1 
HETATM 7456 O O   . HOH E 3 .   ? 49.372 26.407 -24.083 1.00 16.99 ? 733  HOH A O   1 
HETATM 7457 O O   . HOH E 3 .   ? 65.795 13.027 -2.321  1.00 26.04 ? 734  HOH A O   1 
HETATM 7458 O O   . HOH E 3 .   ? 61.519 5.369  -25.483 1.00 31.70 ? 735  HOH A O   1 
HETATM 7459 O O   . HOH E 3 .   ? 56.961 47.669 -28.638 1.00 39.88 ? 736  HOH A O   1 
HETATM 7460 O O   . HOH E 3 .   ? 65.751 40.640 0.297   1.00 21.04 ? 737  HOH A O   1 
HETATM 7461 O O   . HOH E 3 .   ? 35.376 19.907 -12.290 1.00 20.03 ? 738  HOH A O   1 
HETATM 7462 O O   . HOH E 3 .   ? 42.072 21.256 -41.221 1.00 23.07 ? 739  HOH A O   1 
HETATM 7463 O O   . HOH E 3 .   ? 64.811 25.560 -31.323 1.00 10.19 ? 740  HOH A O   1 
HETATM 7464 O O   . HOH E 3 .   ? 57.302 29.850 -12.756 1.00 7.47  ? 741  HOH A O   1 
HETATM 7465 O O   . HOH E 3 .   ? 28.920 40.813 -24.948 1.00 21.45 ? 742  HOH A O   1 
HETATM 7466 O O   . HOH E 3 .   ? 52.511 27.619 6.196   1.00 28.77 ? 743  HOH A O   1 
HETATM 7467 O O   . HOH E 3 .   ? 66.050 8.871  -16.664 1.00 26.51 ? 744  HOH A O   1 
HETATM 7468 O O   . HOH E 3 .   ? 33.982 51.331 -10.779 1.00 30.00 ? 745  HOH A O   1 
HETATM 7469 O O   . HOH E 3 .   ? 61.955 7.538  -23.678 1.00 22.00 ? 746  HOH A O   1 
HETATM 7470 O O   . HOH E 3 .   ? 78.675 22.471 -35.471 1.00 18.14 ? 747  HOH A O   1 
HETATM 7471 O O   . HOH E 3 .   ? 31.275 27.635 -27.523 1.00 33.40 ? 748  HOH A O   1 
HETATM 7472 O O   . HOH E 3 .   ? 48.985 39.852 -21.127 1.00 7.13  ? 749  HOH A O   1 
HETATM 7473 O O   . HOH E 3 .   ? 45.779 32.739 3.169   1.00 42.55 ? 750  HOH A O   1 
HETATM 7474 O O   . HOH E 3 .   ? 69.357 32.048 -39.736 1.00 12.66 ? 751  HOH A O   1 
HETATM 7475 O O   . HOH E 3 .   ? 34.332 28.239 -31.394 1.00 35.10 ? 752  HOH A O   1 
HETATM 7476 O O   . HOH E 3 .   ? 46.193 8.155  -16.358 1.00 24.27 ? 753  HOH A O   1 
HETATM 7477 O O   . HOH E 3 .   ? 71.749 46.964 -24.119 1.00 30.00 ? 754  HOH A O   1 
HETATM 7478 O O   . HOH E 3 .   ? 54.036 46.517 -30.352 1.00 32.58 ? 755  HOH A O   1 
HETATM 7479 O O   . HOH E 3 .   ? 27.077 49.518 -22.355 1.00 11.14 ? 756  HOH A O   1 
HETATM 7480 O O   . HOH E 3 .   ? 73.888 26.573 -32.107 1.00 22.32 ? 757  HOH A O   1 
HETATM 7481 O O   . HOH E 3 .   ? 78.616 18.931 -14.628 1.00 24.64 ? 758  HOH A O   1 
HETATM 7482 O O   . HOH E 3 .   ? 61.267 31.203 -36.715 1.00 32.37 ? 759  HOH A O   1 
HETATM 7483 O O   . HOH E 3 .   ? 66.878 11.647 -5.971  1.00 41.17 ? 760  HOH A O   1 
HETATM 7484 O O   . HOH E 3 .   ? 59.444 46.085 -26.899 1.00 28.36 ? 761  HOH A O   1 
HETATM 7485 O O   . HOH E 3 .   ? 47.640 46.781 -1.584  1.00 31.12 ? 762  HOH A O   1 
HETATM 7486 O O   . HOH E 3 .   ? 41.027 49.444 -10.957 1.00 19.09 ? 763  HOH A O   1 
HETATM 7487 O O   . HOH E 3 .   ? 37.223 40.517 -4.971  1.00 33.49 ? 764  HOH A O   1 
HETATM 7488 O O   . HOH E 3 .   ? 69.261 43.120 -33.084 1.00 34.00 ? 765  HOH A O   1 
HETATM 7489 O O   . HOH E 3 .   ? 66.349 36.490 -26.666 1.00 11.07 ? 766  HOH A O   1 
HETATM 7490 O O   . HOH E 3 .   ? 67.866 16.899 -1.157  1.00 15.42 ? 767  HOH A O   1 
HETATM 7491 O O   . HOH E 3 .   ? 65.891 28.695 -34.098 1.00 18.04 ? 768  HOH A O   1 
HETATM 7492 O O   . HOH E 3 .   ? 60.648 40.791 -32.165 1.00 36.05 ? 769  HOH A O   1 
HETATM 7493 O O   . HOH E 3 .   ? 48.353 53.876 -10.533 1.00 42.29 ? 770  HOH A O   1 
HETATM 7494 O O   . HOH E 3 .   ? 51.618 15.190 -24.051 1.00 10.53 ? 771  HOH A O   1 
HETATM 7495 O O   . HOH E 3 .   ? 34.288 35.474 -24.175 1.00 21.32 ? 772  HOH A O   1 
HETATM 7496 O O   . HOH E 3 .   ? 54.702 37.171 5.714   1.00 17.80 ? 773  HOH A O   1 
HETATM 7497 O O   . HOH E 3 .   ? 71.308 22.739 -32.934 1.00 31.93 ? 774  HOH A O   1 
HETATM 7498 O O   . HOH E 3 .   ? 64.010 23.393 -24.472 1.00 14.63 ? 775  HOH A O   1 
HETATM 7499 O O   . HOH E 3 .   ? 52.737 4.174  -33.326 1.00 37.73 ? 776  HOH A O   1 
HETATM 7500 O O   . HOH E 3 .   ? 26.228 44.272 -18.767 1.00 23.94 ? 777  HOH A O   1 
HETATM 7501 O O   . HOH E 3 .   ? 45.701 51.473 -25.065 1.00 21.58 ? 778  HOH A O   1 
HETATM 7502 O O   . HOH E 3 .   ? 75.475 43.085 -15.233 1.00 51.38 ? 779  HOH A O   1 
HETATM 7503 O O   . HOH E 3 .   ? 45.605 34.534 -24.741 1.00 12.44 ? 780  HOH A O   1 
HETATM 7504 O O   . HOH E 3 .   ? 63.475 52.146 -10.200 1.00 31.13 ? 781  HOH A O   1 
HETATM 7505 O O   . HOH E 3 .   ? 75.781 11.807 -17.096 1.00 44.41 ? 782  HOH A O   1 
HETATM 7506 O O   . HOH E 3 .   ? 72.077 38.043 -24.568 1.00 13.21 ? 783  HOH A O   1 
HETATM 7507 O O   . HOH E 3 .   ? 70.168 36.522 1.477   1.00 19.26 ? 784  HOH A O   1 
HETATM 7508 O O   . HOH E 3 .   ? 47.701 50.316 -32.995 1.00 43.79 ? 785  HOH A O   1 
HETATM 7509 O O   . HOH E 3 .   ? 78.795 13.316 -25.980 1.00 23.18 ? 786  HOH A O   1 
HETATM 7510 O O   . HOH E 3 .   ? 68.963 46.982 -5.317  1.00 31.73 ? 787  HOH A O   1 
HETATM 7511 O O   . HOH E 3 .   ? 76.405 32.228 -0.582  1.00 28.56 ? 788  HOH A O   1 
HETATM 7512 O O   . HOH E 3 .   ? 50.381 46.549 -29.167 1.00 13.68 ? 789  HOH A O   1 
HETATM 7513 O O   . HOH E 3 .   ? 44.385 37.417 -21.923 1.00 10.96 ? 790  HOH A O   1 
HETATM 7514 O O   . HOH E 3 .   ? 52.913 7.235  -15.319 1.00 18.52 ? 791  HOH A O   1 
HETATM 7515 O O   . HOH E 3 .   ? 40.012 41.152 -3.914  1.00 31.80 ? 792  HOH A O   1 
HETATM 7516 O O   . HOH E 3 .   ? 60.559 21.214 -16.734 1.00 10.85 ? 793  HOH A O   1 
HETATM 7517 O O   . HOH E 3 .   ? 60.101 43.780 1.600   1.00 20.24 ? 794  HOH A O   1 
HETATM 7518 O O   . HOH E 3 .   ? 48.211 35.328 -26.740 1.00 7.83  ? 795  HOH A O   1 
HETATM 7519 O O   . HOH E 3 .   ? 48.837 35.798 3.711   1.00 33.02 ? 796  HOH A O   1 
HETATM 7520 O O   . HOH E 3 .   ? 70.115 18.942 -7.797  1.00 10.92 ? 797  HOH A O   1 
HETATM 7521 O O   . HOH E 3 .   ? 67.250 42.617 -2.482  1.00 21.99 ? 798  HOH A O   1 
HETATM 7522 O O   . HOH E 3 .   ? 37.624 16.790 -35.977 1.00 40.09 ? 799  HOH A O   1 
HETATM 7523 O O   . HOH E 3 .   ? 57.786 21.836 -34.543 1.00 32.17 ? 800  HOH A O   1 
HETATM 7524 O O   . HOH E 3 .   ? 40.049 17.867 -13.980 1.00 25.11 ? 801  HOH A O   1 
HETATM 7525 O O   . HOH E 3 .   ? 54.429 33.712 -23.827 1.00 23.42 ? 802  HOH A O   1 
HETATM 7526 O O   . HOH E 3 .   ? 46.089 28.303 -44.457 1.00 26.61 ? 803  HOH A O   1 
HETATM 7527 O O   . HOH E 3 .   ? 45.297 43.213 -34.967 1.00 23.67 ? 804  HOH A O   1 
HETATM 7528 O O   . HOH E 3 .   ? 58.364 52.299 -10.939 1.00 20.44 ? 805  HOH A O   1 
HETATM 7529 O O   . HOH E 3 .   ? 44.169 50.333 -23.102 1.00 12.40 ? 806  HOH A O   1 
HETATM 7530 O O   . HOH E 3 .   ? 53.175 22.055 -27.652 1.00 33.51 ? 807  HOH A O   1 
HETATM 7531 O O   . HOH E 3 .   ? 64.747 35.844 -36.150 1.00 26.92 ? 808  HOH A O   1 
HETATM 7532 O O   . HOH E 3 .   ? 67.073 19.588 -21.750 1.00 10.32 ? 809  HOH A O   1 
HETATM 7533 O O   . HOH E 3 .   ? 51.245 28.791 4.113   1.00 39.63 ? 810  HOH A O   1 
HETATM 7534 O O   . HOH E 3 .   ? 63.152 30.586 -15.217 1.00 8.19  ? 811  HOH A O   1 
HETATM 7535 O O   . HOH E 3 .   ? 78.199 30.948 -17.825 1.00 29.00 ? 812  HOH A O   1 
HETATM 7536 O O   . HOH E 3 .   ? 51.672 14.860 2.363   1.00 29.65 ? 813  HOH A O   1 
HETATM 7537 O O   . HOH E 3 .   ? 74.391 17.930 -31.938 1.00 36.43 ? 814  HOH A O   1 
HETATM 7538 O O   . HOH E 3 .   ? 56.233 35.483 -28.134 1.00 22.54 ? 815  HOH A O   1 
HETATM 7539 O O   . HOH E 3 .   ? 67.754 41.729 -31.053 1.00 19.07 ? 816  HOH A O   1 
HETATM 7540 O O   . HOH E 3 .   ? 53.736 34.103 6.970   1.00 44.21 ? 817  HOH A O   1 
HETATM 7541 O O   . HOH E 3 .   ? 82.373 19.270 -21.914 1.00 30.00 ? 818  HOH A O   1 
HETATM 7542 O O   . HOH E 3 .   ? 55.326 56.473 -16.920 1.00 13.31 ? 819  HOH A O   1 
HETATM 7543 O O   . HOH E 3 .   ? 35.974 24.765 -6.482  1.00 41.99 ? 820  HOH A O   1 
HETATM 7544 O O   . HOH E 3 .   ? 44.782 34.928 -0.667  1.00 30.26 ? 821  HOH A O   1 
HETATM 7545 O O   . HOH E 3 .   ? 71.394 40.968 -13.299 1.00 12.82 ? 822  HOH A O   1 
HETATM 7546 O O   . HOH E 3 .   ? 42.953 14.140 -6.619  1.00 53.48 ? 823  HOH A O   1 
HETATM 7547 O O   . HOH E 3 .   ? 35.622 27.354 -7.520  1.00 31.10 ? 824  HOH A O   1 
HETATM 7548 O O   . HOH E 3 .   ? 50.600 30.343 5.568   1.00 35.20 ? 825  HOH A O   1 
HETATM 7549 O O   . HOH E 3 .   ? 74.547 25.121 2.550   1.00 29.06 ? 826  HOH A O   1 
HETATM 7550 O O   . HOH E 3 .   ? 37.152 46.863 -25.898 1.00 31.57 ? 827  HOH A O   1 
HETATM 7551 O O   . HOH E 3 .   ? 76.849 11.317 -0.446  1.00 38.42 ? 828  HOH A O   1 
HETATM 7552 O O   . HOH E 3 .   ? 65.721 39.810 -16.016 1.00 12.92 ? 829  HOH A O   1 
HETATM 7553 O O   . HOH E 3 .   ? 79.537 20.112 -21.831 1.00 23.23 ? 830  HOH A O   1 
HETATM 7554 O O   . HOH E 3 .   ? 34.381 27.928 -24.216 1.00 17.17 ? 831  HOH A O   1 
HETATM 7555 O O   . HOH E 3 .   ? 64.015 27.114 -13.853 1.00 8.80  ? 832  HOH A O   1 
HETATM 7556 O O   . HOH E 3 .   ? 69.481 35.866 6.631   1.00 33.13 ? 833  HOH A O   1 
HETATM 7557 O O   . HOH E 3 .   ? 56.810 40.219 -21.705 1.00 6.72  ? 834  HOH A O   1 
HETATM 7558 O O   . HOH E 3 .   ? 52.957 34.004 -35.630 1.00 24.29 ? 835  HOH A O   1 
HETATM 7559 O O   . HOH E 3 .   ? 62.922 47.717 -12.401 1.00 30.46 ? 836  HOH A O   1 
HETATM 7560 O O   . HOH E 3 .   ? 52.080 26.681 -38.923 1.00 32.33 ? 837  HOH A O   1 
HETATM 7561 O O   . HOH E 3 .   ? 64.171 25.531 -22.472 1.00 8.90  ? 838  HOH A O   1 
HETATM 7562 O O   . HOH E 3 .   ? 67.621 27.426 -12.965 1.00 9.51  ? 839  HOH A O   1 
HETATM 7563 O O   . HOH E 3 .   ? 47.287 36.007 -40.177 1.00 28.71 ? 840  HOH A O   1 
HETATM 7564 O O   . HOH E 3 .   ? 45.268 5.333  -11.749 1.00 47.61 ? 841  HOH A O   1 
HETATM 7565 O O   . HOH E 3 .   ? 65.387 45.830 -26.689 1.00 44.12 ? 842  HOH A O   1 
HETATM 7566 O O   . HOH E 3 .   ? 36.078 20.195 -24.848 1.00 24.57 ? 843  HOH A O   1 
HETATM 7567 O O   . HOH E 3 .   ? 73.614 36.500 -8.236  1.00 28.26 ? 844  HOH A O   1 
HETATM 7568 O O   . HOH E 3 .   ? 65.414 44.663 -2.050  1.00 36.05 ? 845  HOH A O   1 
HETATM 7569 O O   . HOH E 3 .   ? 45.664 14.504 -4.764  1.00 25.47 ? 846  HOH A O   1 
HETATM 7570 O O   . HOH E 3 .   ? 79.094 32.180 -30.546 1.00 19.24 ? 847  HOH A O   1 
HETATM 7571 O O   . HOH E 3 .   ? 75.355 23.495 -5.277  1.00 15.37 ? 848  HOH A O   1 
HETATM 7572 O O   . HOH E 3 .   ? 49.351 45.817 -38.966 1.00 45.02 ? 849  HOH A O   1 
HETATM 7573 O O   . HOH E 3 .   ? 77.421 39.534 -9.418  1.00 44.83 ? 850  HOH A O   1 
HETATM 7574 O O   . HOH E 3 .   ? 64.766 37.088 -31.908 1.00 27.49 ? 851  HOH A O   1 
HETATM 7575 O O   . HOH E 3 .   ? 54.294 31.061 -33.020 1.00 36.75 ? 852  HOH A O   1 
HETATM 7576 O O   . HOH E 3 .   ? 32.400 19.971 -9.247  1.00 39.95 ? 853  HOH A O   1 
HETATM 7577 O O   . HOH E 3 .   ? 76.012 18.687 1.296   1.00 33.94 ? 854  HOH A O   1 
HETATM 7578 O O   . HOH E 3 .   ? 64.977 8.104  -27.425 1.00 24.69 ? 855  HOH A O   1 
HETATM 7579 O O   . HOH E 3 .   ? 56.957 7.715  -13.733 1.00 17.78 ? 856  HOH A O   1 
HETATM 7580 O O   . HOH E 3 .   ? 40.934 30.845 -1.178  1.00 31.69 ? 857  HOH A O   1 
HETATM 7581 O O   . HOH E 3 .   ? 77.076 19.491 -33.126 1.00 22.59 ? 858  HOH A O   1 
HETATM 7582 O O   . HOH E 3 .   ? 70.462 37.310 -22.158 1.00 13.91 ? 859  HOH A O   1 
HETATM 7583 O O   . HOH E 3 .   ? 72.055 34.261 -6.963  1.00 21.77 ? 860  HOH A O   1 
HETATM 7584 O O   . HOH E 3 .   ? 31.119 48.444 -16.059 1.00 14.77 ? 861  HOH A O   1 
HETATM 7585 O O   . HOH E 3 .   ? 32.126 26.003 -10.014 1.00 30.95 ? 862  HOH A O   1 
HETATM 7586 O O   . HOH E 3 .   ? 49.591 9.108  -13.909 1.00 16.47 ? 863  HOH A O   1 
HETATM 7587 O O   . HOH E 3 .   ? 46.123 35.654 -28.533 1.00 9.88  ? 864  HOH A O   1 
HETATM 7588 O O   . HOH E 3 .   ? 69.011 44.421 -23.486 1.00 14.81 ? 865  HOH A O   1 
HETATM 7589 O O   . HOH E 3 .   ? 50.826 43.073 -40.240 1.00 43.20 ? 866  HOH A O   1 
HETATM 7590 O O   . HOH E 3 .   ? 49.308 9.148  -5.738  1.00 39.47 ? 867  HOH A O   1 
HETATM 7591 O O   . HOH E 3 .   ? 57.567 43.139 3.742   1.00 31.91 ? 868  HOH A O   1 
HETATM 7592 O O   . HOH E 3 .   ? 34.788 34.803 -29.608 1.00 36.26 ? 869  HOH A O   1 
HETATM 7593 O O   . HOH E 3 .   ? 24.114 44.757 -17.103 1.00 38.51 ? 870  HOH A O   1 
HETATM 7594 O O   . HOH E 3 .   ? 51.638 51.396 -23.506 1.00 17.82 ? 871  HOH A O   1 
HETATM 7595 O O   . HOH E 3 .   ? 81.161 28.433 -30.363 1.00 19.93 ? 872  HOH A O   1 
HETATM 7596 O O   . HOH E 3 .   ? 47.908 9.075  -31.947 1.00 30.00 ? 873  HOH A O   1 
HETATM 7597 O O   . HOH E 3 .   ? 64.936 10.047 -8.457  1.00 30.15 ? 874  HOH A O   1 
HETATM 7598 O O   . HOH E 3 .   ? 68.033 9.401  -19.952 1.00 29.77 ? 875  HOH A O   1 
HETATM 7599 O O   . HOH E 3 .   ? 70.919 24.063 3.899   1.00 41.97 ? 876  HOH A O   1 
HETATM 7600 O O   . HOH E 3 .   ? 37.791 18.316 -11.916 1.00 34.91 ? 877  HOH A O   1 
HETATM 7601 O O   . HOH E 3 .   ? 40.264 19.142 -29.602 1.00 30.67 ? 878  HOH A O   1 
HETATM 7602 O O   . HOH E 3 .   ? 54.826 24.169 -30.838 1.00 38.75 ? 879  HOH A O   1 
HETATM 7603 O O   . HOH E 3 .   ? 25.770 43.425 -23.666 1.00 23.11 ? 880  HOH A O   1 
HETATM 7604 O O   . HOH E 3 .   ? 59.090 42.917 -22.469 1.00 7.67  ? 881  HOH A O   1 
HETATM 7605 O O   . HOH E 3 .   ? 58.080 32.073 -26.351 1.00 35.61 ? 882  HOH A O   1 
HETATM 7606 O O   . HOH E 3 .   ? 62.010 54.706 -12.664 1.00 42.29 ? 883  HOH A O   1 
HETATM 7607 O O   . HOH E 3 .   ? 41.715 9.807  -18.460 1.00 32.42 ? 884  HOH A O   1 
HETATM 7608 O O   . HOH E 3 .   ? 81.134 18.770 -19.230 1.00 35.75 ? 885  HOH A O   1 
HETATM 7609 O O   . HOH E 3 .   ? 76.096 14.694 -16.630 1.00 45.54 ? 886  HOH A O   1 
HETATM 7610 O O   . HOH E 3 .   ? 41.539 45.518 -26.011 1.00 13.01 ? 887  HOH A O   1 
HETATM 7611 O O   . HOH E 3 .   ? 81.612 31.489 -31.163 1.00 25.65 ? 888  HOH A O   1 
HETATM 7612 O O   . HOH E 3 .   ? 74.564 39.165 -25.582 1.00 14.94 ? 889  HOH A O   1 
HETATM 7613 O O   . HOH E 3 .   ? 37.389 15.671 -31.552 1.00 51.25 ? 890  HOH A O   1 
HETATM 7614 O O   . HOH E 3 .   ? 47.399 6.545  -39.327 1.00 42.20 ? 891  HOH A O   1 
HETATM 7615 O O   . HOH E 3 .   ? 53.506 44.888 -36.774 1.00 29.71 ? 892  HOH A O   1 
HETATM 7616 O O   . HOH E 3 .   ? 72.859 20.100 -33.636 1.00 33.32 ? 893  HOH A O   1 
HETATM 7617 O O   . HOH E 3 .   ? 53.743 13.268 -40.700 1.00 29.06 ? 894  HOH A O   1 
HETATM 7618 O O   . HOH E 3 .   ? 72.964 43.151 -14.068 1.00 22.51 ? 895  HOH A O   1 
HETATM 7619 O O   . HOH E 3 .   ? 76.985 16.053 -12.261 1.00 33.62 ? 896  HOH A O   1 
HETATM 7620 O O   . HOH E 3 .   ? 35.598 27.533 -34.242 1.00 44.71 ? 897  HOH A O   1 
HETATM 7621 O O   . HOH E 3 .   ? 75.610 34.681 -8.916  1.00 46.02 ? 898  HOH A O   1 
HETATM 7622 O O   . HOH E 3 .   ? 51.066 46.722 -0.660  1.00 30.00 ? 899  HOH A O   1 
HETATM 7623 O O   . HOH E 3 .   ? 27.055 33.976 -23.389 1.00 44.32 ? 900  HOH A O   1 
HETATM 7624 O O   . HOH E 3 .   ? 48.576 39.237 4.901   1.00 38.61 ? 901  HOH A O   1 
HETATM 7625 O O   . HOH E 3 .   ? 62.414 10.682 -0.274  1.00 38.38 ? 902  HOH A O   1 
HETATM 7626 O O   . HOH E 3 .   ? 68.344 14.177 -0.909  1.00 32.88 ? 903  HOH A O   1 
HETATM 7627 O O   . HOH E 3 .   ? 53.603 13.377 -44.476 1.00 29.05 ? 904  HOH A O   1 
HETATM 7628 O O   . HOH E 3 .   ? 76.508 33.994 -11.874 1.00 26.61 ? 905  HOH A O   1 
HETATM 7629 O O   . HOH E 3 .   ? 72.366 38.938 -38.848 1.00 45.13 ? 906  HOH A O   1 
HETATM 7630 O O   . HOH E 3 .   ? 68.769 16.958 -37.000 1.00 24.12 ? 907  HOH A O   1 
HETATM 7631 O O   . HOH E 3 .   ? 59.204 34.400 -10.300 1.00 12.77 ? 908  HOH A O   1 
HETATM 7632 O O   . HOH E 3 .   ? 35.917 23.288 -31.262 1.00 29.58 ? 909  HOH A O   1 
HETATM 7633 O O   . HOH E 3 .   ? 76.434 38.228 -33.724 1.00 22.11 ? 910  HOH A O   1 
HETATM 7634 O O   . HOH E 3 .   ? 44.640 43.498 -1.328  1.00 35.69 ? 911  HOH A O   1 
HETATM 7635 O O   . HOH E 3 .   ? 68.221 52.831 -14.003 1.00 36.58 ? 912  HOH A O   1 
HETATM 7636 O O   . HOH E 3 .   ? 77.227 40.550 -19.167 1.00 30.00 ? 913  HOH A O   1 
HETATM 7637 O O   . HOH E 3 .   ? 44.718 20.849 -4.537  1.00 23.22 ? 914  HOH A O   1 
HETATM 7638 O O   . HOH E 3 .   ? 78.727 28.907 -13.963 1.00 34.35 ? 915  HOH A O   1 
HETATM 7639 O O   . HOH E 3 .   ? 51.482 9.691  -12.038 1.00 11.02 ? 916  HOH A O   1 
HETATM 7640 O O   . HOH E 3 .   ? 62.310 49.496 -22.172 1.00 13.92 ? 917  HOH A O   1 
HETATM 7641 O O   . HOH E 3 .   ? 37.009 38.542 -32.231 1.00 36.44 ? 918  HOH A O   1 
HETATM 7642 O O   . HOH E 3 .   ? 51.858 9.806  -30.487 1.00 22.72 ? 919  HOH A O   1 
HETATM 7643 O O   . HOH E 3 .   ? 26.857 38.303 -12.404 1.00 25.99 ? 920  HOH A O   1 
HETATM 7644 O O   . HOH E 3 .   ? 71.079 19.259 -34.950 1.00 36.31 ? 921  HOH A O   1 
HETATM 7645 O O   . HOH E 3 .   ? 73.773 45.439 -7.773  1.00 23.62 ? 922  HOH A O   1 
HETATM 7646 O O   . HOH E 3 .   ? 62.361 48.561 -5.768  1.00 28.07 ? 923  HOH A O   1 
HETATM 7647 O O   . HOH E 3 .   ? 53.330 19.693 -26.446 1.00 20.16 ? 924  HOH A O   1 
HETATM 7648 O O   . HOH E 3 .   ? 49.670 11.021 -31.632 1.00 26.20 ? 925  HOH A O   1 
HETATM 7649 O O   . HOH E 3 .   ? 45.778 6.521  -20.892 1.00 39.33 ? 926  HOH A O   1 
HETATM 7650 O O   . HOH E 3 .   ? 54.031 39.063 -39.357 1.00 29.77 ? 927  HOH A O   1 
HETATM 7651 O O   . HOH E 3 .   ? 49.079 7.504  -44.085 1.00 41.22 ? 928  HOH A O   1 
HETATM 7652 O O   . HOH E 3 .   ? 38.651 41.387 -35.652 1.00 34.47 ? 929  HOH A O   1 
HETATM 7653 O O   . HOH E 3 .   ? 64.574 31.251 -33.541 1.00 18.07 ? 930  HOH A O   1 
HETATM 7654 O O   . HOH E 3 .   ? 52.351 7.203  -10.662 1.00 30.38 ? 931  HOH A O   1 
HETATM 7655 O O   . HOH E 3 .   ? 73.585 11.254 -7.020  1.00 38.81 ? 932  HOH A O   1 
HETATM 7656 O O   . HOH E 3 .   ? 75.573 11.928 -31.641 1.00 47.65 ? 933  HOH A O   1 
HETATM 7657 O O   . HOH E 3 .   ? 56.650 7.839  -20.299 1.00 24.46 ? 934  HOH A O   1 
HETATM 7658 O O   . HOH E 3 .   ? 69.466 17.063 -34.261 1.00 15.22 ? 935  HOH A O   1 
HETATM 7659 O O   . HOH E 3 .   ? 75.157 16.802 -10.853 1.00 27.04 ? 936  HOH A O   1 
HETATM 7660 O O   . HOH E 3 .   ? 71.002 39.041 -3.003  1.00 30.51 ? 937  HOH A O   1 
HETATM 7661 O O   . HOH E 3 .   ? 29.282 36.754 -17.289 1.00 26.16 ? 938  HOH A O   1 
HETATM 7662 O O   . HOH E 3 .   ? 42.064 11.677 -12.662 1.00 26.90 ? 939  HOH A O   1 
HETATM 7663 O O   . HOH E 3 .   ? 27.507 20.999 -15.770 1.00 40.69 ? 940  HOH A O   1 
HETATM 7664 O O   . HOH E 3 .   ? 48.002 18.814 0.113   1.00 38.95 ? 941  HOH A O   1 
HETATM 7665 O O   . HOH E 3 .   ? 79.373 24.717 -11.208 1.00 21.64 ? 942  HOH A O   1 
HETATM 7666 O O   . HOH E 3 .   ? 36.136 16.243 -13.049 1.00 25.96 ? 943  HOH A O   1 
HETATM 7667 O O   . HOH E 3 .   ? 49.161 34.286 2.021   1.00 26.70 ? 944  HOH A O   1 
HETATM 7668 O O   . HOH E 3 .   ? 67.692 48.171 -19.421 1.00 43.58 ? 945  HOH A O   1 
HETATM 7669 O O   . HOH E 3 .   ? 37.350 40.285 -39.475 1.00 46.11 ? 946  HOH A O   1 
HETATM 7670 O O   . HOH E 3 .   ? 36.061 13.439 -14.165 1.00 30.26 ? 947  HOH A O   1 
HETATM 7671 O O   . HOH E 3 .   ? 70.875 27.135 -32.584 1.00 23.95 ? 948  HOH A O   1 
HETATM 7672 O O   . HOH E 3 .   ? 82.102 21.266 -34.165 1.00 31.81 ? 949  HOH A O   1 
HETATM 7673 O O   . HOH E 3 .   ? 73.611 11.115 -20.167 1.00 29.04 ? 950  HOH A O   1 
HETATM 7674 O O   . HOH E 3 .   ? 49.001 50.584 -8.381  1.00 31.67 ? 951  HOH A O   1 
HETATM 7675 O O   . HOH E 3 .   ? 70.959 44.763 -26.400 1.00 32.94 ? 952  HOH A O   1 
HETATM 7676 O O   . HOH E 3 .   ? 47.329 23.448 -45.059 1.00 43.73 ? 953  HOH A O   1 
HETATM 7677 O O   . HOH E 3 .   ? 79.598 33.860 -28.233 1.00 21.68 ? 954  HOH A O   1 
HETATM 7678 O O   . HOH E 3 .   ? 50.853 7.145  -7.432  1.00 38.48 ? 955  HOH A O   1 
HETATM 7679 O O   . HOH E 3 .   ? 55.337 22.625 4.552   1.00 36.40 ? 956  HOH A O   1 
HETATM 7680 O O   . HOH E 3 .   ? 75.412 28.884 1.928   1.00 22.75 ? 957  HOH A O   1 
HETATM 7681 O O   . HOH E 3 .   ? 61.069 49.091 -26.224 1.00 45.94 ? 958  HOH A O   1 
HETATM 7682 O O   . HOH E 3 .   ? 50.318 7.901  -27.187 1.00 30.00 ? 959  HOH A O   1 
HETATM 7683 O O   . HOH E 3 .   ? 76.142 37.551 -8.880  1.00 37.54 ? 960  HOH A O   1 
HETATM 7684 O O   . HOH E 3 .   ? 53.709 51.607 -10.629 1.00 41.59 ? 961  HOH A O   1 
HETATM 7685 O O   . HOH E 3 .   ? 45.821 10.957 -7.445  1.00 46.65 ? 962  HOH A O   1 
HETATM 7686 O O   . HOH E 3 .   ? 59.276 29.512 2.904   1.00 5.27  ? 963  HOH A O   1 
HETATM 7687 O O   . HOH E 3 .   ? 75.750 13.893 1.628   1.00 36.80 ? 964  HOH A O   1 
HETATM 7688 O O   . HOH E 3 .   ? 32.469 49.138 -5.830  1.00 39.14 ? 965  HOH A O   1 
HETATM 7689 O O   . HOH E 3 .   ? 57.307 43.143 -31.266 1.00 36.69 ? 966  HOH A O   1 
HETATM 7690 O O   . HOH E 3 .   ? 48.247 9.364  -42.740 1.00 36.89 ? 967  HOH A O   1 
HETATM 7691 O O   . HOH E 3 .   ? 41.234 25.064 -2.648  1.00 33.24 ? 968  HOH A O   1 
HETATM 7692 O O   . HOH E 3 .   ? 69.520 37.024 4.031   1.00 29.91 ? 969  HOH A O   1 
HETATM 7693 O O   . HOH E 3 .   ? 31.967 23.521 -24.889 1.00 32.10 ? 970  HOH A O   1 
HETATM 7694 O O   . HOH E 3 .   ? 31.408 44.379 -5.256  1.00 41.29 ? 971  HOH A O   1 
HETATM 7695 O O   . HOH E 3 .   ? 36.835 17.754 -26.476 1.00 39.88 ? 972  HOH A O   1 
HETATM 7696 O O   . HOH E 3 .   ? 58.883 5.445  -21.703 1.00 31.83 ? 973  HOH A O   1 
HETATM 7697 O O   . HOH E 3 .   ? 75.439 16.646 -15.309 1.00 29.09 ? 974  HOH A O   1 
HETATM 7698 O O   . HOH E 3 .   ? 81.124 13.280 -30.617 1.00 51.18 ? 975  HOH A O   1 
HETATM 7699 O O   . HOH E 3 .   ? 81.584 14.194 -24.992 1.00 35.08 ? 976  HOH A O   1 
HETATM 7700 O O   . HOH E 3 .   ? 35.307 30.624 -35.154 1.00 35.44 ? 977  HOH A O   1 
HETATM 7701 O O   . HOH E 3 .   ? 60.721 47.137 -4.023  1.00 21.50 ? 978  HOH A O   1 
HETATM 7702 O O   . HOH E 3 .   ? 44.261 11.369 -10.362 1.00 39.33 ? 979  HOH A O   1 
HETATM 7703 O O   . HOH E 3 .   ? 27.938 19.578 -12.708 1.00 39.93 ? 980  HOH A O   1 
HETATM 7704 O O   . HOH E 3 .   ? 33.061 39.637 -29.568 1.00 41.68 ? 981  HOH A O   1 
HETATM 7705 O O   . HOH E 3 .   ? 52.259 3.206  -30.151 1.00 42.26 ? 982  HOH A O   1 
HETATM 7706 O O   . HOH E 3 .   ? 60.354 51.311 -25.716 1.00 33.63 ? 983  HOH A O   1 
HETATM 7707 O O   . HOH E 3 .   ? 37.477 45.015 -22.926 1.00 31.05 ? 984  HOH A O   1 
HETATM 7708 O O   . HOH E 3 .   ? 50.671 33.504 -41.701 1.00 43.39 ? 985  HOH A O   1 
HETATM 7709 O O   . HOH E 3 .   ? 55.024 5.367  -20.134 1.00 32.48 ? 986  HOH A O   1 
HETATM 7710 O O   . HOH E 3 .   ? 40.079 16.580 -29.715 1.00 39.09 ? 987  HOH A O   1 
HETATM 7711 O O   . HOH E 3 .   ? 47.659 11.775 -5.504  1.00 40.61 ? 988  HOH A O   1 
HETATM 7712 O O   . HOH E 3 .   ? 38.208 27.147 -38.315 1.00 30.00 ? 989  HOH A O   1 
HETATM 7713 O O   . HOH E 3 .   ? 56.864 5.660  -40.057 1.00 39.39 ? 990  HOH A O   1 
HETATM 7714 O O   . HOH E 3 .   ? 50.265 25.132 -26.628 1.00 30.08 ? 991  HOH A O   1 
HETATM 7715 O O   . HOH E 3 .   ? 53.120 18.460 -33.425 1.00 33.02 ? 992  HOH A O   1 
HETATM 7716 O O   . HOH E 3 .   ? 64.855 40.828 4.130   1.00 31.47 ? 993  HOH A O   1 
HETATM 7717 O O   . HOH E 3 .   ? 79.205 23.993 -15.344 1.00 25.21 ? 994  HOH A O   1 
HETATM 7718 O O   . HOH E 3 .   ? 52.957 5.151  -26.504 1.00 30.00 ? 995  HOH A O   1 
HETATM 7719 O O   . HOH E 3 .   ? 46.825 44.069 1.216   1.00 39.54 ? 996  HOH A O   1 
HETATM 7720 O O   . HOH E 3 .   ? 85.474 20.958 -28.853 1.00 30.00 ? 997  HOH A O   1 
HETATM 7721 O O   . HOH E 3 .   ? 73.736 43.851 -3.040  1.00 44.26 ? 998  HOH A O   1 
HETATM 7722 O O   . HOH E 3 .   ? 71.262 9.101  -11.808 1.00 38.08 ? 999  HOH A O   1 
HETATM 7723 O O   . HOH E 3 .   ? 53.778 15.352 5.057   1.00 37.40 ? 1000 HOH A O   1 
HETATM 7724 O O   . HOH E 3 .   ? 58.859 7.406  -39.914 1.00 22.02 ? 1001 HOH A O   1 
HETATM 7725 O O   . HOH E 3 .   ? 41.802 36.235 -0.257  1.00 42.58 ? 1002 HOH A O   1 
HETATM 7726 O O   . HOH E 3 .   ? 56.113 48.479 -2.209  1.00 32.86 ? 1003 HOH A O   1 
HETATM 7727 O O   . HOH E 3 .   ? 63.388 39.863 -31.326 1.00 43.16 ? 1004 HOH A O   1 
HETATM 7728 O O   . HOH E 3 .   ? 77.460 30.052 -4.517  1.00 40.81 ? 1005 HOH A O   1 
HETATM 7729 O O   . HOH E 3 .   ? 53.635 10.821 1.619   1.00 33.14 ? 1006 HOH A O   1 
HETATM 7730 O O   . HOH E 3 .   ? 45.900 35.369 1.725   1.00 38.50 ? 1007 HOH A O   1 
HETATM 7731 O O   . HOH E 3 .   ? 67.507 46.221 -22.149 1.00 30.00 ? 1008 HOH A O   1 
HETATM 7732 O O   . HOH E 3 .   ? 49.524 26.730 -34.958 1.00 28.90 ? 1009 HOH A O   1 
HETATM 7733 O O   . HOH E 3 .   ? 69.431 40.994 -1.110  1.00 44.36 ? 1010 HOH A O   1 
HETATM 7734 O O   . HOH E 3 .   ? 34.615 34.155 -26.507 1.00 39.04 ? 1011 HOH A O   1 
HETATM 7735 O O   . HOH E 3 .   ? 40.613 52.179 -11.408 1.00 14.90 ? 1012 HOH A O   1 
HETATM 7736 O O   . HOH E 3 .   ? 64.594 44.477 0.710   1.00 36.09 ? 1013 HOH A O   1 
HETATM 7737 O O   . HOH E 3 .   ? 65.544 9.253  -5.934  1.00 41.24 ? 1014 HOH A O   1 
HETATM 7738 O O   . HOH E 3 .   ? 65.066 50.500 -9.220  1.00 37.36 ? 1015 HOH A O   1 
HETATM 7739 O O   . HOH E 3 .   ? 77.602 12.048 -28.614 1.00 41.46 ? 1016 HOH A O   1 
HETATM 7740 O O   . HOH E 3 .   ? 59.983 3.698  -23.578 1.00 37.68 ? 1017 HOH A O   1 
HETATM 7741 O O   . HOH E 3 .   ? 41.173 19.246 -2.664  1.00 33.10 ? 1018 HOH A O   1 
HETATM 7742 O O   . HOH E 3 .   ? 66.336 22.229 -22.485 1.00 11.87 ? 1019 HOH A O   1 
HETATM 7743 O O   . HOH E 3 .   ? 51.297 49.309 -36.616 1.00 30.00 ? 1020 HOH A O   1 
HETATM 7744 O O   . HOH E 3 .   ? 41.928 33.947 -0.374  1.00 40.57 ? 1021 HOH A O   1 
HETATM 7745 O O   . HOH E 3 .   ? 78.229 36.360 -12.378 1.00 35.95 ? 1022 HOH A O   1 
HETATM 7746 O O   . HOH E 3 .   ? 45.114 23.605 -45.400 1.00 38.62 ? 1023 HOH A O   1 
HETATM 7747 O O   . HOH E 3 .   ? 78.086 12.096 -23.690 1.00 43.04 ? 1024 HOH A O   1 
HETATM 7748 O O   . HOH E 3 .   ? 79.355 16.450 -16.465 1.00 44.40 ? 1025 HOH A O   1 
HETATM 7749 O O   . HOH E 3 .   ? 58.260 5.650  -7.598  1.00 30.00 ? 1026 HOH A O   1 
HETATM 7750 O O   . HOH E 3 .   ? 61.879 44.857 -0.094  1.00 24.97 ? 1027 HOH A O   1 
HETATM 7751 O O   . HOH E 3 .   ? 36.794 24.708 -3.898  1.00 43.93 ? 1028 HOH A O   1 
HETATM 7752 O O   . HOH E 3 .   ? 37.493 36.941 -42.304 1.00 40.65 ? 1029 HOH A O   1 
HETATM 7753 O O   . HOH E 3 .   ? 83.229 22.343 -22.084 1.00 30.00 ? 1030 HOH A O   1 
HETATM 7754 O O   . HOH E 3 .   ? 33.324 22.048 -7.786  1.00 38.28 ? 1031 HOH A O   1 
HETATM 7755 O O   . HOH E 3 .   ? 39.180 16.204 -7.270  1.00 31.28 ? 1032 HOH A O   1 
HETATM 7756 O O   . HOH E 3 .   ? 63.100 33.559 -33.556 1.00 40.14 ? 1033 HOH A O   1 
HETATM 7757 O O   . HOH E 3 .   ? 75.004 36.802 -40.448 1.00 33.26 ? 1034 HOH A O   1 
HETATM 7758 O O   . HOH E 3 .   ? 36.857 28.785 -5.806  1.00 34.32 ? 1035 HOH A O   1 
HETATM 7759 O O   . HOH E 3 .   ? 73.770 10.449 -4.532  1.00 35.53 ? 1036 HOH A O   1 
HETATM 7760 O O   . HOH E 3 .   ? 28.910 27.671 -22.593 1.00 41.41 ? 1037 HOH A O   1 
HETATM 7761 O O   . HOH E 3 .   ? 38.745 44.428 -4.572  1.00 47.01 ? 1038 HOH A O   1 
HETATM 7762 O O   . HOH E 3 .   ? 66.523 8.044  -9.939  1.00 35.08 ? 1039 HOH A O   1 
HETATM 7763 O O   . HOH E 3 .   ? 57.861 40.799 4.641   1.00 20.69 ? 1040 HOH A O   1 
HETATM 7764 O O   . HOH E 3 .   ? 62.296 35.851 5.489   1.00 17.23 ? 1041 HOH A O   1 
HETATM 7765 O O   . HOH E 3 .   ? 60.681 54.147 -10.592 1.00 30.00 ? 1042 HOH A O   1 
HETATM 7766 O O   . HOH E 3 .   ? 49.164 25.654 -29.221 1.00 30.67 ? 1043 HOH A O   1 
HETATM 7767 O O   . HOH E 3 .   ? 83.480 16.002 -21.600 1.00 30.00 ? 1044 HOH A O   1 
HETATM 7768 O O   . HOH E 3 .   ? 67.157 17.616 1.391   1.00 25.05 ? 1045 HOH A O   1 
HETATM 7769 O O   . HOH E 3 .   ? 24.891 45.941 -30.952 1.00 30.00 ? 1046 HOH A O   1 
HETATM 7770 O O   . HOH E 3 .   ? 55.545 16.662 7.007   1.00 43.79 ? 1047 HOH A O   1 
HETATM 7771 O O   . HOH E 3 .   ? 37.609 54.274 -10.453 1.00 30.00 ? 1048 HOH A O   1 
HETATM 7772 O O   . HOH E 3 .   ? 42.194 9.721  -14.495 1.00 30.80 ? 1049 HOH A O   1 
HETATM 7773 O O   . HOH E 3 .   ? 34.872 50.586 -6.057  1.00 51.07 ? 1050 HOH A O   1 
HETATM 7774 O O   . HOH E 3 .   ? 40.806 48.381 -8.416  1.00 25.91 ? 1051 HOH A O   1 
HETATM 7775 O O   . HOH E 3 .   ? 44.655 41.884 1.265   1.00 37.07 ? 1052 HOH A O   1 
HETATM 7776 O O   . HOH E 3 .   ? 31.779 48.803 -9.234  1.00 38.90 ? 1053 HOH A O   1 
HETATM 7777 O O   . HOH E 3 .   ? 51.866 9.005  -4.735  1.00 36.90 ? 1054 HOH A O   1 
HETATM 7778 O O   . HOH E 3 .   ? 47.575 5.646  -23.195 1.00 38.26 ? 1055 HOH A O   1 
HETATM 7779 O O   . HOH E 3 .   ? 46.598 6.555  -18.268 1.00 30.00 ? 1056 HOH A O   1 
HETATM 7780 O O   . HOH E 3 .   ? 81.050 25.442 -26.143 1.00 30.00 ? 1057 HOH A O   1 
HETATM 7781 O O   . HOH E 3 .   ? 54.030 5.949  -13.204 1.00 32.20 ? 1058 HOH A O   1 
HETATM 7782 O O   . HOH E 3 .   ? 31.650 32.022 -26.201 1.00 31.84 ? 1059 HOH A O   1 
HETATM 7783 O O   . HOH E 3 .   ? 58.528 25.225 -33.796 1.00 30.00 ? 1060 HOH A O   1 
HETATM 7784 O O   . HOH E 3 .   ? 48.053 47.449 -36.140 1.00 30.00 ? 1061 HOH A O   1 
HETATM 7785 O O   . HOH E 3 .   ? 63.199 8.264  -6.293  1.00 55.16 ? 1062 HOH A O   1 
HETATM 7786 O O   . HOH E 3 .   ? 29.736 39.961 -27.523 1.00 30.57 ? 1063 HOH A O   1 
HETATM 7787 O O   . HOH E 3 .   ? 47.503 53.043 -23.111 1.00 28.84 ? 1064 HOH A O   1 
HETATM 7788 O O   . HOH E 3 .   ? 40.689 17.628 -4.181  1.00 43.89 ? 1065 HOH A O   1 
HETATM 7789 O O   . HOH E 3 .   ? 25.717 46.427 -15.899 1.00 30.00 ? 1066 HOH A O   1 
HETATM 7790 O O   . HOH E 3 .   ? 67.272 42.396 1.327   1.00 38.80 ? 1067 HOH A O   1 
HETATM 7791 O O   . HOH E 3 .   ? 79.132 29.438 -6.348  1.00 40.58 ? 1068 HOH A O   1 
HETATM 7792 O O   . HOH E 3 .   ? 67.011 8.100  -12.283 1.00 26.66 ? 1069 HOH A O   1 
HETATM 7793 O O   . HOH E 3 .   ? 76.748 30.556 -9.978  1.00 25.27 ? 1070 HOH A O   1 
HETATM 7794 O O   . HOH E 3 .   ? 56.756 39.367 6.915   1.00 28.23 ? 1071 HOH A O   1 
HETATM 7795 O O   . HOH E 3 .   ? 79.495 19.979 -36.590 1.00 32.68 ? 1072 HOH A O   1 
HETATM 7796 O O   . HOH E 3 .   ? 50.206 5.726  -16.025 1.00 37.89 ? 1073 HOH A O   1 
HETATM 7797 O O   . HOH E 3 .   ? 76.854 30.915 -6.980  1.00 31.53 ? 1074 HOH A O   1 
HETATM 7798 O O   . HOH E 3 .   ? 53.557 30.919 -24.043 1.00 27.23 ? 1075 HOH A O   1 
HETATM 7799 O O   . HOH E 3 .   ? 69.968 49.109 -18.895 1.00 35.53 ? 1076 HOH A O   1 
HETATM 7800 O O   . HOH E 3 .   ? 67.400 11.612 -3.829  1.00 40.32 ? 1077 HOH A O   1 
HETATM 7801 O O   . HOH E 3 .   ? 66.688 50.995 -23.039 1.00 30.00 ? 1078 HOH A O   1 
HETATM 7802 O O   . HOH E 3 .   ? 50.213 55.680 -10.890 1.00 33.70 ? 1079 HOH A O   1 
HETATM 7803 O O   . HOH E 3 .   ? 62.789 6.862  -21.124 1.00 37.68 ? 1080 HOH A O   1 
HETATM 7804 O O   . HOH E 3 .   ? 31.827 36.612 -25.251 1.00 41.32 ? 1081 HOH A O   1 
HETATM 7805 O O   . HOH E 3 .   ? 51.188 29.908 -28.147 1.00 31.15 ? 1082 HOH A O   1 
HETATM 7806 O O   . HOH E 3 .   ? 78.601 17.986 1.148   1.00 42.80 ? 1083 HOH A O   1 
HETATM 7807 O O   . HOH E 3 .   ? 57.129 34.275 -30.147 1.00 24.46 ? 1084 HOH A O   1 
HETATM 7808 O O   . HOH E 3 .   ? 78.820 36.323 -23.055 1.00 30.00 ? 1085 HOH A O   1 
HETATM 7809 O O   . HOH E 3 .   ? 47.662 1.586  -37.659 1.00 36.79 ? 1086 HOH A O   1 
HETATM 7810 O O   . HOH E 3 .   ? 59.643 49.047 -2.257  1.00 33.79 ? 1087 HOH A O   1 
HETATM 7811 O O   . HOH E 3 .   ? 46.866 6.228  -7.985  1.00 30.00 ? 1088 HOH A O   1 
HETATM 7812 O O   . HOH E 3 .   ? 64.074 7.166  -24.880 1.00 38.64 ? 1089 HOH A O   1 
HETATM 7813 O O   . HOH E 3 .   ? 27.238 36.934 -22.817 1.00 36.66 ? 1090 HOH A O   1 
HETATM 7814 O O   . HOH E 3 .   ? 60.787 6.464  -19.175 1.00 23.12 ? 1091 HOH A O   1 
HETATM 7815 O O   . HOH E 3 .   ? 43.616 8.898  -16.810 1.00 36.04 ? 1092 HOH A O   1 
HETATM 7816 O O   . HOH E 3 .   ? 67.507 52.064 -11.502 1.00 30.00 ? 1093 HOH A O   1 
HETATM 7817 O O   . HOH E 3 .   ? 48.750 5.691  -18.682 1.00 42.10 ? 1094 HOH A O   1 
HETATM 7818 O O   . HOH E 3 .   ? 73.737 32.695 -7.895  1.00 23.24 ? 1095 HOH A O   1 
HETATM 7819 O O   . HOH E 3 .   ? 75.560 31.418 4.022   1.00 48.10 ? 1096 HOH A O   1 
HETATM 7820 O O   . HOH E 3 .   ? 76.937 39.860 -24.466 1.00 35.28 ? 1097 HOH A O   1 
HETATM 7821 O O   . HOH E 3 .   ? 64.407 5.727  -28.771 1.00 24.70 ? 1098 HOH A O   1 
HETATM 7822 O O   . HOH E 3 .   ? 25.343 42.640 -21.020 1.00 34.49 ? 1099 HOH A O   1 
HETATM 7823 O O   . HOH E 3 .   ? 47.932 34.596 -42.759 1.00 43.66 ? 1100 HOH A O   1 
HETATM 7824 O O   . HOH E 3 .   ? 82.478 26.445 -31.767 1.00 30.00 ? 1101 HOH A O   1 
HETATM 7825 O O   . HOH E 3 .   ? 80.107 16.441 -10.441 1.00 42.81 ? 1102 HOH A O   1 
HETATM 7826 O O   . HOH E 3 .   ? 81.480 20.554 -7.835  1.00 36.75 ? 1103 HOH A O   1 
HETATM 7827 O O   . HOH E 3 .   ? 32.180 29.221 -25.349 1.00 24.62 ? 1104 HOH A O   1 
HETATM 7828 O O   . HOH E 3 .   ? 52.783 24.625 -27.045 1.00 35.71 ? 1105 HOH A O   1 
HETATM 7829 O O   . HOH E 3 .   ? 64.290 40.190 7.058   1.00 28.14 ? 1106 HOH A O   1 
HETATM 7830 O O   . HOH E 3 .   ? 31.960 38.205 -27.736 1.00 35.98 ? 1107 HOH A O   1 
HETATM 7831 O O   . HOH E 3 .   ? 67.866 8.601  -27.552 1.00 34.88 ? 1108 HOH A O   1 
HETATM 7832 O O   . HOH E 3 .   ? 74.925 41.349 -2.275  1.00 30.00 ? 1109 HOH A O   1 
HETATM 7833 O O   . HOH E 3 .   ? 47.202 52.136 -34.882 1.00 41.01 ? 1110 HOH A O   1 
HETATM 7834 O O   . HOH E 3 .   ? 54.753 6.512  -17.234 1.00 27.15 ? 1111 HOH A O   1 
HETATM 7835 O O   . HOH E 3 .   ? 55.568 50.590 -8.827  1.00 21.95 ? 1112 HOH A O   1 
HETATM 7836 O O   . HOH E 3 .   ? 59.050 33.000 -28.855 1.00 26.94 ? 1113 HOH A O   1 
HETATM 7837 O O   . HOH E 3 .   ? 26.232 40.807 -24.338 1.00 34.93 ? 1114 HOH A O   1 
HETATM 7838 O O   . HOH E 3 .   ? 45.099 19.437 -2.119  1.00 36.28 ? 1115 HOH A O   1 
HETATM 7839 O O   . HOH E 3 .   ? 72.632 35.565 -4.054  1.00 32.17 ? 1116 HOH A O   1 
HETATM 7840 O O   . HOH E 3 .   ? 47.573 26.093 -45.632 1.00 36.72 ? 1117 HOH A O   1 
HETATM 7841 O O   . HOH E 3 .   ? 53.693 33.312 10.124  1.00 45.19 ? 1118 HOH A O   1 
HETATM 7842 O O   . HOH E 3 .   ? 29.471 38.056 -23.948 1.00 29.57 ? 1119 HOH A O   1 
HETATM 7843 O O   . HOH E 3 .   ? 43.639 27.627 -44.812 1.00 34.08 ? 1120 HOH A O   1 
HETATM 7844 O O   . HOH E 3 .   ? 78.296 31.788 -11.947 1.00 42.60 ? 1121 HOH A O   1 
HETATM 7845 O O   . HOH E 3 .   ? 69.671 45.243 -32.320 1.00 40.72 ? 1122 HOH A O   1 
HETATM 7846 O O   . HOH E 3 .   ? 55.436 50.347 -4.273  1.00 33.36 ? 1123 HOH A O   1 
HETATM 7847 O O   . HOH E 3 .   ? 60.921 38.050 5.923   1.00 19.74 ? 1124 HOH A O   1 
HETATM 7848 O O   . HOH E 3 .   ? 63.910 4.283  -26.679 1.00 28.31 ? 1125 HOH A O   1 
HETATM 7849 O O   . HOH E 3 .   ? 78.406 33.419 -22.625 1.00 34.36 ? 1126 HOH A O   1 
HETATM 7850 O O   . HOH E 3 .   ? 68.424 7.005  -18.443 1.00 39.06 ? 1127 HOH A O   1 
HETATM 7851 O O   . HOH E 3 .   ? 34.022 22.119 -29.658 1.00 45.03 ? 1128 HOH A O   1 
HETATM 7852 O O   . HOH E 3 .   ? 36.968 39.504 -41.647 1.00 42.14 ? 1129 HOH A O   1 
HETATM 7853 O O   . HOH E 3 .   ? 46.656 23.553 2.192   1.00 41.43 ? 1130 HOH A O   1 
HETATM 7854 O O   . HOH E 3 .   ? 51.651 52.425 -10.048 1.00 35.64 ? 1131 HOH A O   1 
HETATM 7855 O O   . HOH E 3 .   ? 61.313 31.437 -39.076 1.00 34.15 ? 1132 HOH A O   1 
HETATM 7856 O O   . HOH E 3 .   ? 79.749 28.243 -25.380 1.00 33.42 ? 1133 HOH A O   1 
HETATM 7857 O O   . HOH E 3 .   ? 52.496 29.302 -25.599 1.00 31.24 ? 1134 HOH A O   1 
HETATM 7858 O O   . HOH E 3 .   ? 65.586 7.733  -14.384 1.00 34.97 ? 1135 HOH A O   1 
HETATM 7859 O O   . HOH E 3 .   ? 80.975 22.211 -12.179 1.00 36.71 ? 1136 HOH A O   1 
HETATM 7860 O O   . HOH E 3 .   ? 81.585 27.608 -27.326 1.00 30.00 ? 1137 HOH A O   1 
HETATM 7861 O O   . HOH E 3 .   ? 60.480 47.630 0.479   1.00 46.22 ? 1138 HOH A O   1 
HETATM 7862 O O   . HOH E 3 .   ? 42.844 23.089 -43.358 1.00 38.44 ? 1139 HOH A O   1 
HETATM 7863 O O   . HOH E 3 .   ? 44.786 22.260 -0.170  1.00 43.27 ? 1140 HOH A O   1 
HETATM 7864 O O   . HOH E 3 .   ? 44.741 24.860 -0.774  1.00 45.54 ? 1141 HOH A O   1 
HETATM 7865 O O   . HOH E 3 .   ? 79.836 29.615 -19.369 1.00 38.90 ? 1142 HOH A O   1 
HETATM 7866 O O   . HOH E 3 .   ? 35.990 17.658 -28.527 1.00 45.06 ? 1143 HOH A O   1 
HETATM 7867 O O   . HOH E 3 .   ? 54.569 26.283 -27.927 1.00 32.37 ? 1144 HOH A O   1 
HETATM 7868 O O   . HOH E 3 .   ? 80.179 31.183 -21.885 1.00 41.28 ? 1145 HOH A O   1 
HETATM 7869 O O   . HOH E 3 .   ? 81.701 29.864 -23.600 1.00 45.95 ? 1146 HOH A O   1 
HETATM 7870 O O   . HOH E 3 .   ? 53.362 52.393 -3.685  1.00 48.80 ? 1147 HOH A O   1 
HETATM 7871 O O   . HOH F 3 .   ? 90.651 10.858 -63.009 1.00 35.16 ? 601  HOH B O   1 
HETATM 7872 O O   . HOH F 3 .   ? 86.291 5.652  -65.626 1.00 34.49 ? 602  HOH B O   1 
HETATM 7873 O O   . HOH F 3 .   ? 74.129 20.672 -80.309 1.00 36.59 ? 603  HOH B O   1 
HETATM 7874 O O   . HOH F 3 .   ? 76.533 44.434 -80.798 1.00 34.83 ? 604  HOH B O   1 
HETATM 7875 O O   . HOH F 3 .   ? 89.027 26.861 -44.835 1.00 27.90 ? 605  HOH B O   1 
HETATM 7876 O O   . HOH F 3 .   ? 88.387 18.284 -50.967 1.00 24.95 ? 606  HOH B O   1 
HETATM 7877 O O   . HOH F 3 .   ? 88.131 28.595 -73.074 1.00 40.74 ? 607  HOH B O   1 
HETATM 7878 O O   . HOH F 3 .   ? 77.840 40.790 -26.921 1.00 34.05 ? 608  HOH B O   1 
HETATM 7879 O O   . HOH F 3 .   ? 47.603 25.374 -60.681 1.00 18.79 ? 609  HOH B O   1 
HETATM 7880 O O   . HOH F 3 .   ? 69.557 32.601 -54.032 1.00 22.43 ? 610  HOH B O   1 
HETATM 7881 O O   . HOH F 3 .   ? 57.822 21.335 -80.371 1.00 44.54 ? 611  HOH B O   1 
HETATM 7882 O O   . HOH F 3 .   ? 55.049 17.137 -68.863 1.00 28.80 ? 612  HOH B O   1 
HETATM 7883 O O   . HOH F 3 .   ? 68.459 54.393 -69.686 1.00 35.66 ? 613  HOH B O   1 
HETATM 7884 O O   . HOH F 3 .   ? 74.305 52.290 -36.628 1.00 36.04 ? 614  HOH B O   1 
HETATM 7885 O O   . HOH F 3 .   ? 61.386 8.920  -53.572 1.00 38.76 ? 615  HOH B O   1 
HETATM 7886 O O   . HOH F 3 .   ? 60.298 14.827 -65.603 1.00 10.61 ? 616  HOH B O   1 
HETATM 7887 O O   . HOH F 3 .   ? 75.960 37.963 -51.004 1.00 31.74 ? 617  HOH B O   1 
HETATM 7888 O O   . HOH F 3 .   ? 49.273 54.765 -59.438 1.00 28.94 ? 618  HOH B O   1 
HETATM 7889 O O   . HOH F 3 .   ? 54.199 11.932 -57.500 1.00 40.44 ? 619  HOH B O   1 
HETATM 7890 O O   . HOH F 3 .   ? 86.447 45.151 -48.839 1.00 29.58 ? 620  HOH B O   1 
HETATM 7891 O O   . HOH F 3 .   ? 79.028 17.584 -77.928 1.00 43.80 ? 621  HOH B O   1 
HETATM 7892 O O   . HOH F 3 .   ? 60.497 38.108 -54.741 1.00 7.72  ? 622  HOH B O   1 
HETATM 7893 O O   . HOH F 3 .   ? 72.216 8.396  -48.058 1.00 27.56 ? 623  HOH B O   1 
HETATM 7894 O O   . HOH F 3 .   ? 79.365 34.776 -47.698 1.00 19.09 ? 624  HOH B O   1 
HETATM 7895 O O   . HOH F 3 .   ? 63.318 50.593 -81.021 1.00 32.07 ? 625  HOH B O   1 
HETATM 7896 O O   . HOH F 3 .   ? 53.916 15.032 -61.659 1.00 23.47 ? 626  HOH B O   1 
HETATM 7897 O O   . HOH F 3 .   ? 54.954 15.356 -49.249 1.00 24.64 ? 627  HOH B O   1 
HETATM 7898 O O   . HOH F 3 .   ? 62.059 29.672 -58.285 1.00 8.81  ? 628  HOH B O   1 
HETATM 7899 O O   . HOH F 3 .   ? 77.772 19.109 -44.821 1.00 9.35  ? 629  HOH B O   1 
HETATM 7900 O O   . HOH F 3 .   ? 78.151 44.914 -78.136 1.00 50.17 ? 630  HOH B O   1 
HETATM 7901 O O   . HOH F 3 .   ? 65.853 38.209 -80.835 1.00 24.81 ? 631  HOH B O   1 
HETATM 7902 O O   . HOH F 3 .   ? 70.271 9.376  -44.732 1.00 26.02 ? 632  HOH B O   1 
HETATM 7903 O O   . HOH F 3 .   ? 74.905 7.751  -54.478 1.00 20.41 ? 633  HOH B O   1 
HETATM 7904 O O   . HOH F 3 .   ? 65.442 13.657 -75.477 1.00 27.05 ? 634  HOH B O   1 
HETATM 7905 O O   . HOH F 3 .   ? 59.737 19.597 -50.067 1.00 9.86  ? 635  HOH B O   1 
HETATM 7906 O O   . HOH F 3 .   ? 81.020 31.021 -77.237 1.00 29.10 ? 636  HOH B O   1 
HETATM 7907 O O   . HOH F 3 .   ? 75.734 45.283 -85.126 1.00 48.14 ? 637  HOH B O   1 
HETATM 7908 O O   . HOH F 3 .   ? 54.522 63.248 -64.090 1.00 41.13 ? 638  HOH B O   1 
HETATM 7909 O O   . HOH F 3 .   ? 49.087 33.685 -71.960 1.00 10.40 ? 639  HOH B O   1 
HETATM 7910 O O   . HOH F 3 .   ? 69.468 25.952 -42.854 1.00 8.69  ? 640  HOH B O   1 
HETATM 7911 O O   . HOH F 3 .   ? 88.926 40.073 -50.002 1.00 19.14 ? 641  HOH B O   1 
HETATM 7912 O O   . HOH F 3 .   ? 60.803 50.141 -55.792 1.00 21.59 ? 642  HOH B O   1 
HETATM 7913 O O   . HOH F 3 .   ? 72.756 50.531 -75.418 1.00 37.26 ? 643  HOH B O   1 
HETATM 7914 O O   . HOH F 3 .   ? 88.811 12.505 -53.722 1.00 31.49 ? 644  HOH B O   1 
HETATM 7915 O O   . HOH F 3 .   ? 72.501 39.396 -47.582 1.00 43.60 ? 645  HOH B O   1 
HETATM 7916 O O   . HOH F 3 .   ? 49.963 15.269 -62.533 1.00 33.71 ? 646  HOH B O   1 
HETATM 7917 O O   . HOH F 3 .   ? 81.538 12.195 -73.090 1.00 34.01 ? 647  HOH B O   1 
HETATM 7918 O O   . HOH F 3 .   ? 48.157 40.148 -63.626 1.00 19.47 ? 648  HOH B O   1 
HETATM 7919 O O   . HOH F 3 .   ? 69.545 44.636 -79.032 1.00 28.48 ? 649  HOH B O   1 
HETATM 7920 O O   . HOH F 3 .   ? 70.898 54.134 -63.196 1.00 23.00 ? 650  HOH B O   1 
HETATM 7921 O O   . HOH F 3 .   ? 68.616 16.253 -59.378 1.00 12.08 ? 651  HOH B O   1 
HETATM 7922 O O   . HOH F 3 .   ? 80.498 44.951 -74.139 1.00 27.05 ? 652  HOH B O   1 
HETATM 7923 O O   . HOH F 3 .   ? 72.391 26.889 -41.500 1.00 8.00  ? 653  HOH B O   1 
HETATM 7924 O O   . HOH F 3 .   ? 76.362 40.098 -75.489 1.00 17.19 ? 654  HOH B O   1 
HETATM 7925 O O   . HOH F 3 .   ? 72.317 8.581  -63.915 1.00 17.71 ? 655  HOH B O   1 
HETATM 7926 O O   . HOH F 3 .   ? 83.856 23.583 -76.023 1.00 48.94 ? 656  HOH B O   1 
HETATM 7927 O O   . HOH F 3 .   ? 85.590 44.341 -69.445 1.00 24.18 ? 657  HOH B O   1 
HETATM 7928 O O   . HOH F 3 .   ? 91.400 29.358 -46.896 1.00 33.24 ? 658  HOH B O   1 
HETATM 7929 O O   . HOH F 3 .   ? 59.725 21.807 -61.169 1.00 9.90  ? 659  HOH B O   1 
HETATM 7930 O O   . HOH F 3 .   ? 71.290 42.437 -51.267 1.00 12.96 ? 660  HOH B O   1 
HETATM 7931 O O   . HOH F 3 .   ? 68.748 20.176 -84.001 1.00 41.78 ? 661  HOH B O   1 
HETATM 7932 O O   . HOH F 3 .   ? 80.162 7.877  -51.000 1.00 24.59 ? 662  HOH B O   1 
HETATM 7933 O O   . HOH F 3 .   ? 77.401 45.104 -74.173 1.00 26.76 ? 663  HOH B O   1 
HETATM 7934 O O   . HOH F 3 .   ? 92.180 39.059 -56.334 1.00 29.90 ? 664  HOH B O   1 
HETATM 7935 O O   . HOH F 3 .   ? 70.008 6.741  -66.924 1.00 22.04 ? 665  HOH B O   1 
HETATM 7936 O O   . HOH F 3 .   ? 90.439 28.296 -50.769 1.00 16.50 ? 666  HOH B O   1 
HETATM 7937 O O   . HOH F 3 .   ? 81.587 36.543 -72.600 1.00 25.58 ? 667  HOH B O   1 
HETATM 7938 O O   . HOH F 3 .   ? 77.368 48.849 -50.486 1.00 27.74 ? 668  HOH B O   1 
HETATM 7939 O O   . HOH F 3 .   ? 67.605 15.207 -56.974 1.00 10.19 ? 669  HOH B O   1 
HETATM 7940 O O   . HOH F 3 .   ? 73.657 24.640 -48.397 1.00 12.11 ? 670  HOH B O   1 
HETATM 7941 O O   . HOH F 3 .   ? 60.405 39.991 -79.227 1.00 21.14 ? 671  HOH B O   1 
HETATM 7942 O O   . HOH F 3 .   ? 80.892 48.184 -48.874 1.00 30.00 ? 672  HOH B O   1 
HETATM 7943 O O   . HOH F 3 .   ? 54.911 15.877 -43.534 1.00 21.92 ? 673  HOH B O   1 
HETATM 7944 O O   . HOH F 3 .   ? 66.734 17.057 -61.415 1.00 7.45  ? 674  HOH B O   1 
HETATM 7945 O O   . HOH F 3 .   ? 73.948 21.381 -51.306 1.00 10.20 ? 675  HOH B O   1 
HETATM 7946 O O   . HOH F 3 .   ? 85.660 18.131 -76.541 1.00 42.26 ? 676  HOH B O   1 
HETATM 7947 O O   . HOH F 3 .   ? 70.314 41.936 -78.723 1.00 26.27 ? 677  HOH B O   1 
HETATM 7948 O O   . HOH F 3 .   ? 73.819 15.460 -35.443 1.00 28.39 ? 678  HOH B O   1 
HETATM 7949 O O   . HOH F 3 .   ? 67.989 41.372 -47.783 1.00 29.20 ? 679  HOH B O   1 
HETATM 7950 O O   . HOH F 3 .   ? 73.035 45.445 -34.774 1.00 34.07 ? 680  HOH B O   1 
HETATM 7951 O O   . HOH F 3 .   ? 81.622 4.131  -58.154 1.00 19.47 ? 681  HOH B O   1 
HETATM 7952 O O   . HOH F 3 .   ? 69.957 14.522 -33.590 1.00 19.22 ? 682  HOH B O   1 
HETATM 7953 O O   . HOH F 3 .   ? 54.992 51.394 -53.135 1.00 32.29 ? 683  HOH B O   1 
HETATM 7954 O O   . HOH F 3 .   ? 71.858 28.862 -81.898 1.00 26.24 ? 684  HOH B O   1 
HETATM 7955 O O   . HOH F 3 .   ? 94.401 25.845 -67.809 1.00 19.82 ? 685  HOH B O   1 
HETATM 7956 O O   . HOH F 3 .   ? 54.619 31.860 -76.584 1.00 25.94 ? 686  HOH B O   1 
HETATM 7957 O O   . HOH F 3 .   ? 62.040 43.230 -57.870 1.00 14.52 ? 687  HOH B O   1 
HETATM 7958 O O   . HOH F 3 .   ? 50.551 34.942 -54.489 1.00 28.29 ? 688  HOH B O   1 
HETATM 7959 O O   . HOH F 3 .   ? 76.794 11.232 -75.963 1.00 36.14 ? 689  HOH B O   1 
HETATM 7960 O O   . HOH F 3 .   ? 54.962 25.023 -78.043 1.00 27.36 ? 690  HOH B O   1 
HETATM 7961 O O   . HOH F 3 .   ? 74.575 50.013 -34.072 1.00 36.00 ? 691  HOH B O   1 
HETATM 7962 O O   . HOH F 3 .   ? 66.959 23.610 -39.731 1.00 21.98 ? 692  HOH B O   1 
HETATM 7963 O O   . HOH F 3 .   ? 77.520 36.886 -44.366 1.00 22.49 ? 693  HOH B O   1 
HETATM 7964 O O   . HOH F 3 .   ? 54.215 32.979 -55.596 1.00 12.50 ? 694  HOH B O   1 
HETATM 7965 O O   . HOH F 3 .   ? 79.330 52.313 -65.004 1.00 28.40 ? 695  HOH B O   1 
HETATM 7966 O O   . HOH F 3 .   ? 87.202 13.461 -65.520 1.00 18.24 ? 696  HOH B O   1 
HETATM 7967 O O   . HOH F 3 .   ? 84.730 5.337  -56.047 1.00 26.97 ? 697  HOH B O   1 
HETATM 7968 O O   . HOH F 3 .   ? 86.107 19.125 -43.035 1.00 35.69 ? 698  HOH B O   1 
HETATM 7969 O O   . HOH F 3 .   ? 76.587 23.064 -54.284 1.00 10.91 ? 699  HOH B O   1 
HETATM 7970 O O   . HOH F 3 .   ? 71.889 33.083 -66.244 1.00 9.25  ? 700  HOH B O   1 
HETATM 7971 O O   . HOH F 3 .   ? 67.782 17.800 -79.694 1.00 17.58 ? 701  HOH B O   1 
HETATM 7972 O O   . HOH F 3 .   ? 57.930 11.783 -61.200 1.00 21.08 ? 702  HOH B O   1 
HETATM 7973 O O   . HOH F 3 .   ? 51.900 21.332 -45.610 1.00 36.84 ? 703  HOH B O   1 
HETATM 7974 O O   . HOH F 3 .   ? 56.328 14.634 -70.798 1.00 28.45 ? 704  HOH B O   1 
HETATM 7975 O O   . HOH F 3 .   ? 56.460 21.605 -43.949 1.00 15.96 ? 705  HOH B O   1 
HETATM 7976 O O   . HOH F 3 .   ? 58.106 27.066 -41.979 1.00 33.07 ? 706  HOH B O   1 
HETATM 7977 O O   . HOH F 3 .   ? 61.668 33.215 -82.934 1.00 16.68 ? 707  HOH B O   1 
HETATM 7978 O O   . HOH F 3 .   ? 64.390 11.857 -46.717 1.00 11.61 ? 708  HOH B O   1 
HETATM 7979 O O   . HOH F 3 .   ? 74.198 22.583 -62.298 1.00 8.31  ? 709  HOH B O   1 
HETATM 7980 O O   . HOH F 3 .   ? 71.891 26.555 -63.249 1.00 8.26  ? 710  HOH B O   1 
HETATM 7981 O O   . HOH F 3 .   ? 82.840 15.552 -77.105 1.00 34.26 ? 711  HOH B O   1 
HETATM 7982 O O   . HOH F 3 .   ? 51.544 23.831 -71.992 1.00 24.45 ? 712  HOH B O   1 
HETATM 7983 O O   . HOH F 3 .   ? 60.275 36.665 -61.966 1.00 7.20  ? 713  HOH B O   1 
HETATM 7984 O O   . HOH F 3 .   ? 80.476 5.563  -69.093 1.00 27.67 ? 714  HOH B O   1 
HETATM 7985 O O   . HOH F 3 .   ? 51.835 28.841 -55.483 1.00 33.28 ? 715  HOH B O   1 
HETATM 7986 O O   . HOH F 3 .   ? 52.895 34.923 -50.603 1.00 25.74 ? 716  HOH B O   1 
HETATM 7987 O O   . HOH F 3 .   ? 65.300 11.179 -44.151 1.00 18.24 ? 717  HOH B O   1 
HETATM 7988 O O   . HOH F 3 .   ? 64.053 18.111 -60.876 1.00 11.12 ? 718  HOH B O   1 
HETATM 7989 O O   . HOH F 3 .   ? 69.639 9.303  -73.718 1.00 24.50 ? 719  HOH B O   1 
HETATM 7990 O O   . HOH F 3 .   ? 60.830 18.343 -75.277 1.00 9.69  ? 720  HOH B O   1 
HETATM 7991 O O   . HOH F 3 .   ? 58.626 37.596 -81.283 1.00 21.47 ? 721  HOH B O   1 
HETATM 7992 O O   . HOH F 3 .   ? 75.947 25.935 -56.616 1.00 6.48  ? 722  HOH B O   1 
HETATM 7993 O O   . HOH F 3 .   ? 92.939 21.819 -62.054 1.00 23.08 ? 723  HOH B O   1 
HETATM 7994 O O   . HOH F 3 .   ? 79.485 30.738 -79.219 1.00 38.08 ? 724  HOH B O   1 
HETATM 7995 O O   . HOH F 3 .   ? 85.874 43.787 -43.172 1.00 37.67 ? 725  HOH B O   1 
HETATM 7996 O O   . HOH F 3 .   ? 67.525 10.989 -74.511 1.00 27.93 ? 726  HOH B O   1 
HETATM 7997 O O   . HOH F 3 .   ? 59.258 16.415 -50.496 1.00 13.08 ? 727  HOH B O   1 
HETATM 7998 O O   . HOH F 3 .   ? 89.821 35.597 -68.877 1.00 27.60 ? 728  HOH B O   1 
HETATM 7999 O O   . HOH F 3 .   ? 49.539 31.515 -55.321 1.00 33.07 ? 729  HOH B O   1 
HETATM 8000 O O   . HOH F 3 .   ? 76.096 30.394 -81.024 1.00 40.60 ? 730  HOH B O   1 
HETATM 8001 O O   . HOH F 3 .   ? 88.447 18.784 -75.497 1.00 31.40 ? 731  HOH B O   1 
HETATM 8002 O O   . HOH F 3 .   ? 54.796 40.476 -76.918 1.00 18.77 ? 732  HOH B O   1 
HETATM 8003 O O   . HOH F 3 .   ? 77.470 12.102 -44.055 1.00 12.13 ? 733  HOH B O   1 
HETATM 8004 O O   . HOH F 3 .   ? 51.376 37.872 -56.563 1.00 10.19 ? 734  HOH B O   1 
HETATM 8005 O O   . HOH F 3 .   ? 75.694 19.604 -60.417 1.00 8.08  ? 735  HOH B O   1 
HETATM 8006 O O   . HOH F 3 .   ? 60.460 12.929 -61.744 1.00 12.84 ? 736  HOH B O   1 
HETATM 8007 O O   . HOH F 3 .   ? 83.779 46.364 -48.808 1.00 25.68 ? 737  HOH B O   1 
HETATM 8008 O O   . HOH F 3 .   ? 94.439 31.392 -38.214 1.00 25.17 ? 738  HOH B O   1 
HETATM 8009 O O   . HOH F 3 .   ? 71.890 37.990 -54.801 1.00 17.49 ? 739  HOH B O   1 
HETATM 8010 O O   . HOH F 3 .   ? 52.648 44.545 -52.107 1.00 25.24 ? 740  HOH B O   1 
HETATM 8011 O O   . HOH F 3 .   ? 65.095 44.723 -56.567 1.00 11.00 ? 741  HOH B O   1 
HETATM 8012 O O   . HOH F 3 .   ? 78.234 4.472  -62.805 1.00 31.58 ? 742  HOH B O   1 
HETATM 8013 O O   . HOH F 3 .   ? 82.234 36.422 -50.266 1.00 13.57 ? 743  HOH B O   1 
HETATM 8014 O O   . HOH F 3 .   ? 62.547 12.195 -41.021 1.00 19.90 ? 744  HOH B O   1 
HETATM 8015 O O   . HOH F 3 .   ? 90.396 15.833 -64.023 1.00 30.26 ? 745  HOH B O   1 
HETATM 8016 O O   . HOH F 3 .   ? 67.621 44.334 -44.534 1.00 20.09 ? 746  HOH B O   1 
HETATM 8017 O O   . HOH F 3 .   ? 68.703 54.549 -54.320 1.00 35.59 ? 747  HOH B O   1 
HETATM 8018 O O   . HOH F 3 .   ? 82.686 47.708 -67.624 1.00 21.11 ? 748  HOH B O   1 
HETATM 8019 O O   . HOH F 3 .   ? 59.880 50.196 -80.516 1.00 36.76 ? 749  HOH B O   1 
HETATM 8020 O O   . HOH F 3 .   ? 89.450 17.015 -52.730 1.00 26.55 ? 750  HOH B O   1 
HETATM 8021 O O   . HOH F 3 .   ? 68.785 10.667 -64.923 1.00 18.49 ? 751  HOH B O   1 
HETATM 8022 O O   . HOH F 3 .   ? 65.559 16.435 -78.896 1.00 19.52 ? 752  HOH B O   1 
HETATM 8023 O O   . HOH F 3 .   ? 64.879 32.736 -55.683 1.00 23.28 ? 753  HOH B O   1 
HETATM 8024 O O   . HOH F 3 .   ? 59.217 29.532 -58.956 1.00 6.86  ? 754  HOH B O   1 
HETATM 8025 O O   . HOH F 3 .   ? 83.915 41.494 -43.204 1.00 27.46 ? 755  HOH B O   1 
HETATM 8026 O O   . HOH F 3 .   ? 55.084 14.203 -46.774 1.00 19.68 ? 756  HOH B O   1 
HETATM 8027 O O   . HOH F 3 .   ? 68.569 21.048 -66.915 1.00 11.25 ? 757  HOH B O   1 
HETATM 8028 O O   . HOH F 3 .   ? 78.384 25.527 -55.655 1.00 13.76 ? 758  HOH B O   1 
HETATM 8029 O O   . HOH F 3 .   ? 60.169 24.293 -36.079 1.00 16.54 ? 759  HOH B O   1 
HETATM 8030 O O   . HOH F 3 .   ? 84.366 31.455 -32.854 1.00 32.12 ? 760  HOH B O   1 
HETATM 8031 O O   . HOH F 3 .   ? 52.761 49.409 -64.283 1.00 39.06 ? 761  HOH B O   1 
HETATM 8032 O O   . HOH F 3 .   ? 55.731 26.419 -75.583 1.00 17.77 ? 762  HOH B O   1 
HETATM 8033 O O   . HOH F 3 .   ? 63.404 18.258 -79.513 1.00 22.74 ? 763  HOH B O   1 
HETATM 8034 O O   . HOH F 3 .   ? 83.003 13.488 -59.764 1.00 7.46  ? 764  HOH B O   1 
HETATM 8035 O O   . HOH F 3 .   ? 78.117 37.445 -75.156 1.00 26.21 ? 765  HOH B O   1 
HETATM 8036 O O   . HOH F 3 .   ? 70.752 56.214 -58.372 1.00 34.83 ? 766  HOH B O   1 
HETATM 8037 O O   . HOH F 3 .   ? 78.039 21.087 -48.610 1.00 8.38  ? 767  HOH B O   1 
HETATM 8038 O O   . HOH F 3 .   ? 67.642 34.194 -81.479 1.00 26.13 ? 768  HOH B O   1 
HETATM 8039 O O   . HOH F 3 .   ? 59.097 11.244 -47.635 1.00 28.67 ? 769  HOH B O   1 
HETATM 8040 O O   . HOH F 3 .   ? 56.418 27.504 -58.485 1.00 6.90  ? 770  HOH B O   1 
HETATM 8041 O O   . HOH F 3 .   ? 73.630 20.872 -59.054 1.00 8.02  ? 771  HOH B O   1 
HETATM 8042 O O   . HOH F 3 .   ? 89.936 20.827 -49.690 1.00 27.37 ? 772  HOH B O   1 
HETATM 8043 O O   . HOH F 3 .   ? 45.667 28.347 -69.212 1.00 14.90 ? 773  HOH B O   1 
HETATM 8044 O O   . HOH F 3 .   ? 69.758 16.129 -80.874 1.00 35.32 ? 774  HOH B O   1 
HETATM 8045 O O   . HOH F 3 .   ? 71.578 21.994 -62.230 1.00 11.62 ? 775  HOH B O   1 
HETATM 8046 O O   . HOH F 3 .   ? 83.361 22.196 -74.341 1.00 26.64 ? 776  HOH B O   1 
HETATM 8047 O O   . HOH F 3 .   ? 79.157 7.246  -45.776 1.00 40.71 ? 777  HOH B O   1 
HETATM 8048 O O   . HOH F 3 .   ? 60.148 29.706 -81.903 1.00 17.62 ? 778  HOH B O   1 
HETATM 8049 O O   . HOH F 3 .   ? 71.036 9.959  -60.391 1.00 16.01 ? 779  HOH B O   1 
HETATM 8050 O O   . HOH F 3 .   ? 72.309 23.634 -50.985 1.00 8.88  ? 780  HOH B O   1 
HETATM 8051 O O   . HOH F 3 .   ? 58.317 56.992 -73.302 1.00 22.50 ? 781  HOH B O   1 
HETATM 8052 O O   . HOH F 3 .   ? 63.577 48.010 -38.714 1.00 28.07 ? 782  HOH B O   1 
HETATM 8053 O O   . HOH F 3 .   ? 87.495 37.683 -70.008 1.00 24.24 ? 783  HOH B O   1 
HETATM 8054 O O   . HOH F 3 .   ? 57.921 46.544 -79.481 1.00 23.07 ? 784  HOH B O   1 
HETATM 8055 O O   . HOH F 3 .   ? 60.907 19.281 -60.738 1.00 11.66 ? 785  HOH B O   1 
HETATM 8056 O O   . HOH F 3 .   ? 60.833 14.484 -74.863 1.00 26.79 ? 786  HOH B O   1 
HETATM 8057 O O   . HOH F 3 .   ? 69.455 53.241 -47.582 1.00 29.78 ? 787  HOH B O   1 
HETATM 8058 O O   . HOH F 3 .   ? 90.342 46.432 -57.272 1.00 38.56 ? 788  HOH B O   1 
HETATM 8059 O O   . HOH F 3 .   ? 65.055 30.476 -47.134 1.00 23.67 ? 789  HOH B O   1 
HETATM 8060 O O   . HOH F 3 .   ? 58.327 25.691 -46.365 1.00 26.29 ? 790  HOH B O   1 
HETATM 8061 O O   . HOH F 3 .   ? 75.792 17.811 -36.704 1.00 25.70 ? 791  HOH B O   1 
HETATM 8062 O O   . HOH F 3 .   ? 67.790 41.602 -45.215 1.00 26.74 ? 792  HOH B O   1 
HETATM 8063 O O   . HOH F 3 .   ? 79.129 7.521  -61.644 1.00 14.04 ? 793  HOH B O   1 
HETATM 8064 O O   . HOH F 3 .   ? 66.192 54.445 -76.704 1.00 23.59 ? 794  HOH B O   1 
HETATM 8065 O O   . HOH F 3 .   ? 83.565 44.174 -63.944 1.00 28.45 ? 795  HOH B O   1 
HETATM 8066 O O   . HOH F 3 .   ? 48.182 27.627 -71.888 1.00 18.84 ? 796  HOH B O   1 
HETATM 8067 O O   . HOH F 3 .   ? 60.748 38.270 -45.972 1.00 24.20 ? 797  HOH B O   1 
HETATM 8068 O O   . HOH F 3 .   ? 89.405 37.254 -49.987 1.00 17.04 ? 798  HOH B O   1 
HETATM 8069 O O   . HOH F 3 .   ? 78.164 51.255 -56.686 1.00 20.76 ? 799  HOH B O   1 
HETATM 8070 O O   . HOH F 3 .   ? 83.766 40.063 -29.303 1.00 42.19 ? 800  HOH B O   1 
HETATM 8071 O O   . HOH F 3 .   ? 65.327 25.861 -41.019 1.00 19.80 ? 801  HOH B O   1 
HETATM 8072 O O   . HOH F 3 .   ? 70.183 52.017 -75.202 1.00 40.68 ? 802  HOH B O   1 
HETATM 8073 O O   . HOH F 3 .   ? 80.361 52.465 -58.050 1.00 38.90 ? 803  HOH B O   1 
HETATM 8074 O O   . HOH F 3 .   ? 70.359 7.226  -40.936 1.00 36.90 ? 804  HOH B O   1 
HETATM 8075 O O   . HOH F 3 .   ? 62.625 41.442 -62.198 1.00 9.29  ? 805  HOH B O   1 
HETATM 8076 O O   . HOH F 3 .   ? 91.508 32.564 -59.077 1.00 13.68 ? 806  HOH B O   1 
HETATM 8077 O O   . HOH F 3 .   ? 54.337 53.546 -50.526 1.00 37.91 ? 807  HOH B O   1 
HETATM 8078 O O   . HOH F 3 .   ? 70.111 55.047 -78.371 1.00 33.34 ? 808  HOH B O   1 
HETATM 8079 O O   . HOH F 3 .   ? 62.719 13.027 -73.275 1.00 25.54 ? 809  HOH B O   1 
HETATM 8080 O O   . HOH F 3 .   ? 54.460 25.212 -50.956 1.00 36.23 ? 810  HOH B O   1 
HETATM 8081 O O   . HOH F 3 .   ? 86.135 38.522 -32.155 1.00 28.93 ? 811  HOH B O   1 
HETATM 8082 O O   . HOH F 3 .   ? 73.628 3.786  -58.563 1.00 40.76 ? 812  HOH B O   1 
HETATM 8083 O O   . HOH F 3 .   ? 62.759 39.570 -55.802 1.00 11.55 ? 813  HOH B O   1 
HETATM 8084 O O   . HOH F 3 .   ? 71.421 52.134 -60.186 1.00 15.42 ? 814  HOH B O   1 
HETATM 8085 O O   . HOH F 3 .   ? 55.148 54.952 -75.611 1.00 20.76 ? 815  HOH B O   1 
HETATM 8086 O O   . HOH F 3 .   ? 62.910 54.743 -78.472 1.00 38.33 ? 816  HOH B O   1 
HETATM 8087 O O   . HOH F 3 .   ? 83.792 36.329 -71.487 1.00 20.46 ? 817  HOH B O   1 
HETATM 8088 O O   . HOH F 3 .   ? 60.805 17.034 -52.882 1.00 9.15  ? 818  HOH B O   1 
HETATM 8089 O O   . HOH F 3 .   ? 77.148 55.977 -74.231 1.00 43.79 ? 819  HOH B O   1 
HETATM 8090 O O   . HOH F 3 .   ? 93.340 18.245 -66.227 1.00 50.15 ? 820  HOH B O   1 
HETATM 8091 O O   . HOH F 3 .   ? 81.435 46.120 -33.430 1.00 31.26 ? 821  HOH B O   1 
HETATM 8092 O O   . HOH F 3 .   ? 55.091 51.117 -75.403 1.00 15.17 ? 822  HOH B O   1 
HETATM 8093 O O   . HOH F 3 .   ? 67.024 8.065  -58.766 1.00 20.97 ? 823  HOH B O   1 
HETATM 8094 O O   . HOH F 3 .   ? 53.758 45.083 -62.135 1.00 14.94 ? 824  HOH B O   1 
HETATM 8095 O O   . HOH F 3 .   ? 65.686 42.371 -80.785 1.00 25.94 ? 825  HOH B O   1 
HETATM 8096 O O   . HOH F 3 .   ? 70.571 35.628 -55.043 1.00 20.26 ? 826  HOH B O   1 
HETATM 8097 O O   . HOH F 3 .   ? 94.168 32.440 -64.839 1.00 31.43 ? 827  HOH B O   1 
HETATM 8098 O O   . HOH F 3 .   ? 71.468 51.094 -40.381 1.00 26.85 ? 828  HOH B O   1 
HETATM 8099 O O   . HOH F 3 .   ? 50.092 41.356 -65.336 1.00 12.87 ? 829  HOH B O   1 
HETATM 8100 O O   . HOH F 3 .   ? 64.155 41.541 -58.256 1.00 9.80  ? 830  HOH B O   1 
HETATM 8101 O O   . HOH F 3 .   ? 52.284 19.688 -50.452 1.00 33.50 ? 831  HOH B O   1 
HETATM 8102 O O   . HOH F 3 .   ? 54.006 16.946 -39.843 1.00 25.63 ? 832  HOH B O   1 
HETATM 8103 O O   . HOH F 3 .   ? 70.047 21.952 -59.351 1.00 7.56  ? 833  HOH B O   1 
HETATM 8104 O O   . HOH F 3 .   ? 74.555 19.401 -77.863 1.00 21.44 ? 834  HOH B O   1 
HETATM 8105 O O   . HOH F 3 .   ? 84.107 49.738 -70.938 1.00 45.37 ? 835  HOH B O   1 
HETATM 8106 O O   . HOH F 3 .   ? 83.637 23.139 -35.403 1.00 33.47 ? 836  HOH B O   1 
HETATM 8107 O O   . HOH F 3 .   ? 84.377 12.873 -45.011 1.00 34.15 ? 837  HOH B O   1 
HETATM 8108 O O   . HOH F 3 .   ? 61.913 42.164 -55.100 1.00 11.74 ? 838  HOH B O   1 
HETATM 8109 O O   . HOH F 3 .   ? 75.968 23.262 -35.934 1.00 15.63 ? 839  HOH B O   1 
HETATM 8110 O O   . HOH F 3 .   ? 60.582 22.359 -49.971 1.00 10.37 ? 840  HOH B O   1 
HETATM 8111 O O   . HOH F 3 .   ? 54.831 19.993 -67.586 1.00 34.54 ? 841  HOH B O   1 
HETATM 8112 O O   . HOH F 3 .   ? 51.054 18.707 -70.962 1.00 33.20 ? 842  HOH B O   1 
HETATM 8113 O O   . HOH F 3 .   ? 90.224 30.899 -44.284 1.00 39.41 ? 843  HOH B O   1 
HETATM 8114 O O   . HOH F 3 .   ? 87.915 29.248 -38.708 1.00 16.91 ? 844  HOH B O   1 
HETATM 8115 O O   . HOH F 3 .   ? 90.167 39.106 -40.739 1.00 30.00 ? 845  HOH B O   1 
HETATM 8116 O O   . HOH F 3 .   ? 91.530 27.821 -73.321 1.00 28.85 ? 846  HOH B O   1 
HETATM 8117 O O   . HOH F 3 .   ? 82.236 27.831 -34.283 1.00 21.64 ? 847  HOH B O   1 
HETATM 8118 O O   . HOH F 3 .   ? 78.174 49.578 -72.887 1.00 29.28 ? 848  HOH B O   1 
HETATM 8119 O O   . HOH F 3 .   ? 64.453 51.840 -62.775 1.00 18.91 ? 849  HOH B O   1 
HETATM 8120 O O   . HOH F 3 .   ? 54.560 28.831 -76.686 1.00 28.11 ? 850  HOH B O   1 
HETATM 8121 O O   . HOH F 3 .   ? 84.249 35.613 -31.609 1.00 27.93 ? 851  HOH B O   1 
HETATM 8122 O O   . HOH F 3 .   ? 57.779 14.332 -49.285 1.00 14.35 ? 852  HOH B O   1 
HETATM 8123 O O   . HOH F 3 .   ? 57.617 44.905 -44.469 1.00 28.34 ? 853  HOH B O   1 
HETATM 8124 O O   . HOH F 3 .   ? 64.792 32.528 -82.889 1.00 23.80 ? 854  HOH B O   1 
HETATM 8125 O O   . HOH F 3 .   ? 82.147 7.870  -71.594 1.00 37.16 ? 855  HOH B O   1 
HETATM 8126 O O   . HOH F 3 .   ? 48.427 34.227 -62.861 1.00 16.83 ? 856  HOH B O   1 
HETATM 8127 O O   . HOH F 3 .   ? 61.729 32.536 -51.896 1.00 19.80 ? 857  HOH B O   1 
HETATM 8128 O O   . HOH F 3 .   ? 66.434 56.689 -57.420 1.00 50.14 ? 858  HOH B O   1 
HETATM 8129 O O   . HOH F 3 .   ? 64.619 43.925 -82.685 1.00 33.81 ? 859  HOH B O   1 
HETATM 8130 O O   . HOH F 3 .   ? 59.308 56.912 -65.869 1.00 22.10 ? 860  HOH B O   1 
HETATM 8131 O O   . HOH F 3 .   ? 84.423 9.401  -45.505 1.00 44.50 ? 861  HOH B O   1 
HETATM 8132 O O   . HOH F 3 .   ? 71.187 22.688 -82.854 1.00 28.42 ? 862  HOH B O   1 
HETATM 8133 O O   . HOH F 3 .   ? 68.341 23.750 -66.046 1.00 10.87 ? 863  HOH B O   1 
HETATM 8134 O O   . HOH F 3 .   ? 52.116 18.128 -59.401 1.00 34.80 ? 864  HOH B O   1 
HETATM 8135 O O   . HOH F 3 .   ? 87.912 46.599 -50.301 1.00 40.11 ? 865  HOH B O   1 
HETATM 8136 O O   . HOH F 3 .   ? 56.153 18.426 -73.784 1.00 25.68 ? 866  HOH B O   1 
HETATM 8137 O O   . HOH F 3 .   ? 89.536 38.835 -68.155 1.00 38.07 ? 867  HOH B O   1 
HETATM 8138 O O   . HOH F 3 .   ? 81.872 11.507 -38.909 1.00 24.69 ? 868  HOH B O   1 
HETATM 8139 O O   . HOH F 3 .   ? 73.382 29.529 -79.864 1.00 39.11 ? 869  HOH B O   1 
HETATM 8140 O O   . HOH F 3 .   ? 53.918 18.313 -54.620 1.00 17.01 ? 870  HOH B O   1 
HETATM 8141 O O   . HOH F 3 .   ? 75.530 54.656 -59.004 1.00 31.82 ? 871  HOH B O   1 
HETATM 8142 O O   . HOH F 3 .   ? 54.881 29.423 -48.546 1.00 31.49 ? 872  HOH B O   1 
HETATM 8143 O O   . HOH F 3 .   ? 55.906 15.176 -41.125 1.00 22.12 ? 873  HOH B O   1 
HETATM 8144 O O   . HOH F 3 .   ? 57.463 59.158 -69.060 1.00 26.16 ? 874  HOH B O   1 
HETATM 8145 O O   . HOH F 3 .   ? 52.125 27.737 -73.492 1.00 28.31 ? 875  HOH B O   1 
HETATM 8146 O O   . HOH F 3 .   ? 66.108 10.270 -39.188 1.00 18.24 ? 876  HOH B O   1 
HETATM 8147 O O   . HOH F 3 .   ? 96.529 23.601 -64.444 1.00 35.92 ? 877  HOH B O   1 
HETATM 8148 O O   . HOH F 3 .   ? 72.164 34.055 -40.876 1.00 38.18 ? 878  HOH B O   1 
HETATM 8149 O O   . HOH F 3 .   ? 73.087 4.742  -64.484 1.00 39.94 ? 879  HOH B O   1 
HETATM 8150 O O   . HOH F 3 .   ? 74.394 35.999 -48.860 1.00 28.87 ? 880  HOH B O   1 
HETATM 8151 O O   . HOH F 3 .   ? 70.020 40.167 -54.027 1.00 17.26 ? 881  HOH B O   1 
HETATM 8152 O O   . HOH F 3 .   ? 75.401 37.654 -79.245 1.00 31.01 ? 882  HOH B O   1 
HETATM 8153 O O   . HOH F 3 .   ? 52.252 22.641 -49.831 1.00 44.18 ? 883  HOH B O   1 
HETATM 8154 O O   . HOH F 3 .   ? 55.958 51.679 -44.809 1.00 36.98 ? 884  HOH B O   1 
HETATM 8155 O O   . HOH F 3 .   ? 72.279 4.414  -68.583 1.00 30.21 ? 885  HOH B O   1 
HETATM 8156 O O   . HOH F 3 .   ? 73.631 17.094 -58.702 1.00 10.47 ? 886  HOH B O   1 
HETATM 8157 O O   . HOH F 3 .   ? 67.465 17.741 -39.466 1.00 23.98 ? 887  HOH B O   1 
HETATM 8158 O O   . HOH F 3 .   ? 83.449 11.305 -48.762 1.00 58.73 ? 888  HOH B O   1 
HETATM 8159 O O   . HOH F 3 .   ? 86.195 24.699 -77.773 1.00 34.75 ? 889  HOH B O   1 
HETATM 8160 O O   . HOH F 3 .   ? 81.833 12.834 -36.466 1.00 31.65 ? 890  HOH B O   1 
HETATM 8161 O O   . HOH F 3 .   ? 71.997 52.047 -73.282 1.00 38.32 ? 891  HOH B O   1 
HETATM 8162 O O   . HOH F 3 .   ? 58.391 58.076 -75.761 1.00 34.31 ? 892  HOH B O   1 
HETATM 8163 O O   . HOH F 3 .   ? 63.912 54.290 -50.869 1.00 46.23 ? 893  HOH B O   1 
HETATM 8164 O O   . HOH F 3 .   ? 76.522 4.705  -69.697 1.00 20.03 ? 894  HOH B O   1 
HETATM 8165 O O   . HOH F 3 .   ? 84.179 16.588 -43.056 1.00 24.50 ? 895  HOH B O   1 
HETATM 8166 O O   . HOH F 3 .   ? 50.008 24.026 -59.771 1.00 13.14 ? 896  HOH B O   1 
HETATM 8167 O O   . HOH F 3 .   ? 50.197 37.327 -48.232 1.00 34.52 ? 897  HOH B O   1 
HETATM 8168 O O   . HOH F 3 .   ? 93.130 32.985 -34.778 1.00 37.63 ? 898  HOH B O   1 
HETATM 8169 O O   . HOH F 3 .   ? 67.585 54.534 -51.574 1.00 39.40 ? 899  HOH B O   1 
HETATM 8170 O O   . HOH F 3 .   ? 91.644 18.884 -58.092 1.00 24.08 ? 900  HOH B O   1 
HETATM 8171 O O   . HOH F 3 .   ? 49.325 21.779 -59.346 1.00 29.11 ? 901  HOH B O   1 
HETATM 8172 O O   . HOH F 3 .   ? 76.762 43.191 -75.876 1.00 25.87 ? 902  HOH B O   1 
HETATM 8173 O O   . HOH F 3 .   ? 75.254 24.639 -33.672 1.00 23.26 ? 903  HOH B O   1 
HETATM 8174 O O   . HOH F 3 .   ? 64.764 30.163 -51.392 1.00 27.88 ? 904  HOH B O   1 
HETATM 8175 O O   . HOH F 3 .   ? 83.627 48.497 -55.677 1.00 29.32 ? 905  HOH B O   1 
HETATM 8176 O O   . HOH F 3 .   ? 77.353 26.955 -82.274 1.00 42.55 ? 906  HOH B O   1 
HETATM 8177 O O   . HOH F 3 .   ? 54.007 22.365 -47.302 1.00 25.90 ? 907  HOH B O   1 
HETATM 8178 O O   . HOH F 3 .   ? 85.310 38.890 -42.663 1.00 30.73 ? 908  HOH B O   1 
HETATM 8179 O O   . HOH F 3 .   ? 73.242 53.349 -51.751 1.00 32.15 ? 909  HOH B O   1 
HETATM 8180 O O   . HOH F 3 .   ? 87.321 25.685 -40.511 1.00 28.27 ? 910  HOH B O   1 
HETATM 8181 O O   . HOH F 3 .   ? 62.216 30.753 -41.159 1.00 34.27 ? 911  HOH B O   1 
HETATM 8182 O O   . HOH F 3 .   ? 57.897 8.453  -67.263 1.00 23.27 ? 912  HOH B O   1 
HETATM 8183 O O   . HOH F 3 .   ? 89.923 36.913 -44.843 1.00 33.42 ? 913  HOH B O   1 
HETATM 8184 O O   . HOH F 3 .   ? 54.780 38.198 -43.997 1.00 29.48 ? 914  HOH B O   1 
HETATM 8185 O O   . HOH F 3 .   ? 82.371 10.942 -50.834 1.00 31.45 ? 915  HOH B O   1 
HETATM 8186 O O   . HOH F 3 .   ? 62.793 53.797 -57.568 1.00 39.89 ? 916  HOH B O   1 
HETATM 8187 O O   . HOH F 3 .   ? 71.117 7.001  -54.604 1.00 28.77 ? 917  HOH B O   1 
HETATM 8188 O O   . HOH F 3 .   ? 49.379 26.073 -56.302 1.00 30.00 ? 918  HOH B O   1 
HETATM 8189 O O   . HOH F 3 .   ? 82.115 47.583 -51.482 1.00 31.54 ? 919  HOH B O   1 
HETATM 8190 O O   . HOH F 3 .   ? 71.575 33.679 -80.257 1.00 28.87 ? 920  HOH B O   1 
HETATM 8191 O O   . HOH F 3 .   ? 96.370 19.289 -71.226 1.00 42.32 ? 921  HOH B O   1 
HETATM 8192 O O   . HOH F 3 .   ? 52.425 17.407 -51.471 1.00 45.92 ? 922  HOH B O   1 
HETATM 8193 O O   . HOH F 3 .   ? 62.771 9.970  -39.605 1.00 29.65 ? 923  HOH B O   1 
HETATM 8194 O O   . HOH F 3 .   ? 72.803 6.507  -57.666 1.00 24.72 ? 924  HOH B O   1 
HETATM 8195 O O   . HOH F 3 .   ? 93.353 35.649 -39.292 1.00 35.28 ? 925  HOH B O   1 
HETATM 8196 O O   . HOH F 3 .   ? 47.434 27.125 -57.732 1.00 32.00 ? 926  HOH B O   1 
HETATM 8197 O O   . HOH F 3 .   ? 66.560 41.106 -41.083 1.00 29.92 ? 927  HOH B O   1 
HETATM 8198 O O   . HOH F 3 .   ? 90.421 10.377 -56.359 1.00 37.07 ? 928  HOH B O   1 
HETATM 8199 O O   . HOH F 3 .   ? 68.698 38.321 -81.065 1.00 31.10 ? 929  HOH B O   1 
HETATM 8200 O O   . HOH F 3 .   ? 85.414 44.990 -73.225 1.00 37.71 ? 930  HOH B O   1 
HETATM 8201 O O   . HOH F 3 .   ? 83.901 43.013 -29.826 1.00 37.79 ? 931  HOH B O   1 
HETATM 8202 O O   . HOH F 3 .   ? 75.942 5.636  -55.529 1.00 24.14 ? 932  HOH B O   1 
HETATM 8203 O O   . HOH F 3 .   ? 91.458 35.341 -58.044 1.00 18.78 ? 933  HOH B O   1 
HETATM 8204 O O   . HOH F 3 .   ? 65.675 54.158 -70.991 1.00 24.34 ? 934  HOH B O   1 
HETATM 8205 O O   . HOH F 3 .   ? 63.177 26.833 -42.964 1.00 22.50 ? 935  HOH B O   1 
HETATM 8206 O O   . HOH F 3 .   ? 83.495 54.753 -69.606 1.00 35.48 ? 936  HOH B O   1 
HETATM 8207 O O   . HOH F 3 .   ? 77.489 53.808 -44.788 1.00 39.41 ? 937  HOH B O   1 
HETATM 8208 O O   . HOH F 3 .   ? 53.386 12.800 -63.922 1.00 38.49 ? 938  HOH B O   1 
HETATM 8209 O O   . HOH F 3 .   ? 88.337 27.245 -31.552 1.00 42.85 ? 939  HOH B O   1 
HETATM 8210 O O   . HOH F 3 .   ? 58.253 19.594 -75.464 1.00 19.47 ? 940  HOH B O   1 
HETATM 8211 O O   . HOH F 3 .   ? 76.803 9.354  -44.356 1.00 23.24 ? 941  HOH B O   1 
HETATM 8212 O O   . HOH F 3 .   ? 72.398 38.273 -52.065 1.00 27.87 ? 942  HOH B O   1 
HETATM 8213 O O   . HOH F 3 .   ? 92.949 33.047 -67.719 1.00 42.82 ? 943  HOH B O   1 
HETATM 8214 O O   . HOH F 3 .   ? 83.599 9.731  -54.494 1.00 40.89 ? 944  HOH B O   1 
HETATM 8215 O O   . HOH F 3 .   ? 61.799 10.743 -43.369 1.00 21.91 ? 945  HOH B O   1 
HETATM 8216 O O   . HOH F 3 .   ? 48.406 41.787 -49.157 1.00 40.14 ? 946  HOH B O   1 
HETATM 8217 O O   . HOH F 3 .   ? 64.350 7.266  -62.699 1.00 46.99 ? 947  HOH B O   1 
HETATM 8218 O O   . HOH F 3 .   ? 84.646 45.387 -66.982 1.00 28.94 ? 948  HOH B O   1 
HETATM 8219 O O   . HOH F 3 .   ? 89.799 30.905 -74.340 1.00 45.38 ? 949  HOH B O   1 
HETATM 8220 O O   . HOH F 3 .   ? 77.064 19.863 -76.361 1.00 14.69 ? 950  HOH B O   1 
HETATM 8221 O O   . HOH F 3 .   ? 66.894 20.743 -40.188 1.00 24.19 ? 951  HOH B O   1 
HETATM 8222 O O   . HOH F 3 .   ? 51.308 32.741 -76.216 1.00 32.90 ? 952  HOH B O   1 
HETATM 8223 O O   . HOH F 3 .   ? 67.214 18.914 -82.189 1.00 24.97 ? 953  HOH B O   1 
HETATM 8224 O O   . HOH F 3 .   ? 58.616 51.870 -55.732 1.00 31.59 ? 954  HOH B O   1 
HETATM 8225 O O   . HOH F 3 .   ? 52.232 24.011 -53.520 1.00 30.00 ? 955  HOH B O   1 
HETATM 8226 O O   . HOH F 3 .   ? 81.022 8.411  -39.325 1.00 38.57 ? 956  HOH B O   1 
HETATM 8227 O O   . HOH F 3 .   ? 60.445 19.930 -82.140 1.00 33.71 ? 957  HOH B O   1 
HETATM 8228 O O   . HOH F 3 .   ? 90.829 39.372 -63.493 1.00 33.89 ? 958  HOH B O   1 
HETATM 8229 O O   . HOH F 3 .   ? 84.430 29.356 -33.651 1.00 29.78 ? 959  HOH B O   1 
HETATM 8230 O O   . HOH F 3 .   ? 84.619 42.463 -40.759 1.00 35.25 ? 960  HOH B O   1 
HETATM 8231 O O   . HOH F 3 .   ? 66.276 9.427  -64.257 1.00 32.65 ? 961  HOH B O   1 
HETATM 8232 O O   . HOH F 3 .   ? 85.822 47.202 -65.553 1.00 26.66 ? 962  HOH B O   1 
HETATM 8233 O O   . HOH F 3 .   ? 65.315 9.774  -70.179 1.00 42.84 ? 963  HOH B O   1 
HETATM 8234 O O   . HOH F 3 .   ? 55.653 51.733 -55.430 1.00 30.00 ? 964  HOH B O   1 
HETATM 8235 O O   . HOH F 3 .   ? 74.727 38.819 -38.768 1.00 33.83 ? 965  HOH B O   1 
HETATM 8236 O O   . HOH F 3 .   ? 55.919 48.062 -65.931 1.00 32.96 ? 966  HOH B O   1 
HETATM 8237 O O   . HOH F 3 .   ? 90.050 41.921 -62.204 1.00 28.41 ? 967  HOH B O   1 
HETATM 8238 O O   . HOH F 3 .   ? 94.721 21.735 -64.168 1.00 34.87 ? 968  HOH B O   1 
HETATM 8239 O O   . HOH F 3 .   ? 65.099 20.617 -82.287 1.00 28.84 ? 969  HOH B O   1 
HETATM 8240 O O   . HOH F 3 .   ? 71.333 39.973 -49.852 1.00 32.69 ? 970  HOH B O   1 
HETATM 8241 O O   . HOH F 3 .   ? 78.980 6.311  -41.284 1.00 46.50 ? 971  HOH B O   1 
HETATM 8242 O O   . HOH F 3 .   ? 66.778 52.992 -46.070 1.00 36.41 ? 972  HOH B O   1 
HETATM 8243 O O   . HOH F 3 .   ? 86.022 32.516 -75.984 1.00 43.80 ? 973  HOH B O   1 
HETATM 8244 O O   . HOH F 3 .   ? 80.648 55.999 -67.094 1.00 51.86 ? 974  HOH B O   1 
HETATM 8245 O O   . HOH F 3 .   ? 75.972 5.986  -36.550 1.00 49.31 ? 975  HOH B O   1 
HETATM 8246 O O   . HOH F 3 .   ? 77.060 35.824 -49.013 1.00 24.52 ? 976  HOH B O   1 
HETATM 8247 O O   . HOH F 3 .   ? 88.122 39.558 -45.505 1.00 39.13 ? 977  HOH B O   1 
HETATM 8248 O O   . HOH F 3 .   ? 83.694 8.718  -52.493 1.00 33.31 ? 978  HOH B O   1 
HETATM 8249 O O   . HOH F 3 .   ? 94.341 29.815 -64.762 1.00 32.00 ? 979  HOH B O   1 
HETATM 8250 O O   . HOH F 3 .   ? 61.803 40.298 -81.629 1.00 18.60 ? 980  HOH B O   1 
HETATM 8251 O O   . HOH F 3 .   ? 77.896 35.854 -76.936 1.00 39.40 ? 981  HOH B O   1 
HETATM 8252 O O   . HOH F 3 .   ? 72.200 15.607 -79.440 1.00 33.42 ? 982  HOH B O   1 
HETATM 8253 O O   . HOH F 3 .   ? 43.253 40.934 -53.788 1.00 39.39 ? 983  HOH B O   1 
HETATM 8254 O O   . HOH F 3 .   ? 88.410 47.791 -63.798 1.00 30.00 ? 984  HOH B O   1 
HETATM 8255 O O   . HOH F 3 .   ? 56.026 26.815 -48.279 1.00 37.55 ? 985  HOH B O   1 
HETATM 8256 O O   . HOH F 3 .   ? 94.848 23.050 -60.919 1.00 34.22 ? 986  HOH B O   1 
HETATM 8257 O O   . HOH F 3 .   ? 77.162 34.605 -82.755 1.00 48.54 ? 987  HOH B O   1 
HETATM 8258 O O   . HOH F 3 .   ? 90.431 42.841 -55.455 1.00 37.21 ? 988  HOH B O   1 
HETATM 8259 O O   . HOH F 3 .   ? 89.943 35.557 -47.757 1.00 26.46 ? 989  HOH B O   1 
HETATM 8260 O O   . HOH F 3 .   ? 75.234 6.738  -43.503 1.00 40.17 ? 990  HOH B O   1 
HETATM 8261 O O   . HOH F 3 .   ? 84.955 13.844 -42.026 1.00 43.01 ? 991  HOH B O   1 
HETATM 8262 O O   . HOH F 3 .   ? 66.275 58.273 -66.139 1.00 54.31 ? 992  HOH B O   1 
HETATM 8263 O O   . HOH F 3 .   ? 75.278 7.389  -51.737 1.00 21.98 ? 993  HOH B O   1 
HETATM 8264 O O   . HOH F 3 .   ? 77.867 52.777 -36.605 1.00 39.33 ? 994  HOH B O   1 
HETATM 8265 O O   . HOH F 3 .   ? 91.981 10.372 -58.788 1.00 37.13 ? 995  HOH B O   1 
HETATM 8266 O O   . HOH F 3 .   ? 91.423 27.934 -36.470 1.00 40.49 ? 996  HOH B O   1 
HETATM 8267 O O   . HOH F 3 .   ? 73.778 21.277 -35.758 1.00 34.41 ? 997  HOH B O   1 
HETATM 8268 O O   . HOH F 3 .   ? 84.716 43.763 -75.635 1.00 47.22 ? 998  HOH B O   1 
HETATM 8269 O O   . HOH F 3 .   ? 70.525 53.019 -45.131 1.00 38.52 ? 999  HOH B O   1 
HETATM 8270 O O   . HOH F 3 .   ? 92.680 18.927 -55.537 1.00 32.84 ? 1000 HOH B O   1 
HETATM 8271 O O   . HOH F 3 .   ? 83.676 37.146 -29.335 1.00 36.63 ? 1001 HOH B O   1 
HETATM 8272 O O   . HOH F 3 .   ? 87.251 33.428 -72.810 1.00 32.56 ? 1002 HOH B O   1 
HETATM 8273 O O   . HOH F 3 .   ? 81.009 52.585 -62.598 1.00 36.37 ? 1003 HOH B O   1 
HETATM 8274 O O   . HOH F 3 .   ? 76.430 5.004  -64.941 1.00 33.34 ? 1004 HOH B O   1 
HETATM 8275 O O   . HOH F 3 .   ? 79.796 49.583 -50.223 1.00 38.67 ? 1005 HOH B O   1 
HETATM 8276 O O   . HOH F 3 .   ? 76.196 37.940 -42.388 1.00 31.30 ? 1006 HOH B O   1 
HETATM 8277 O O   . HOH F 3 .   ? 51.727 13.695 -65.510 1.00 44.11 ? 1007 HOH B O   1 
HETATM 8278 O O   . HOH F 3 .   ? 55.435 41.622 -81.479 1.00 38.24 ? 1008 HOH B O   1 
HETATM 8279 O O   . HOH F 3 .   ? 80.549 38.326 -75.881 1.00 32.88 ? 1009 HOH B O   1 
HETATM 8280 O O   . HOH F 3 .   ? 78.298 7.925  -38.076 1.00 40.96 ? 1010 HOH B O   1 
HETATM 8281 O O   . HOH F 3 .   ? 80.496 9.849  -36.649 1.00 47.52 ? 1011 HOH B O   1 
HETATM 8282 O O   . HOH F 3 .   ? 79.404 2.403  -62.323 1.00 38.72 ? 1012 HOH B O   1 
HETATM 8283 O O   . HOH F 3 .   ? 58.540 56.960 -63.078 1.00 28.46 ? 1013 HOH B O   1 
HETATM 8284 O O   . HOH F 3 .   ? 49.982 21.202 -72.255 1.00 31.49 ? 1014 HOH B O   1 
HETATM 8285 O O   . HOH F 3 .   ? 80.075 12.160 -75.340 1.00 39.44 ? 1015 HOH B O   1 
HETATM 8286 O O   . HOH F 3 .   ? 95.420 23.051 -52.796 1.00 31.84 ? 1016 HOH B O   1 
HETATM 8287 O O   . HOH F 3 .   ? 73.633 3.680  -61.366 1.00 40.41 ? 1017 HOH B O   1 
HETATM 8288 O O   . HOH F 3 .   ? 57.911 45.852 -41.870 1.00 44.59 ? 1018 HOH B O   1 
HETATM 8289 O O   . HOH F 3 .   ? 61.100 27.734 -44.420 1.00 34.29 ? 1019 HOH B O   1 
HETATM 8290 O O   . HOH F 3 .   ? 87.170 13.018 -68.339 1.00 22.10 ? 1020 HOH B O   1 
HETATM 8291 O O   . HOH F 3 .   ? 74.214 53.124 -74.819 1.00 40.96 ? 1021 HOH B O   1 
HETATM 8292 O O   . HOH F 3 .   ? 94.249 30.394 -35.267 1.00 34.85 ? 1022 HOH B O   1 
HETATM 8293 O O   . HOH F 3 .   ? 64.816 6.384  -58.523 1.00 34.21 ? 1023 HOH B O   1 
HETATM 8294 O O   . HOH F 3 .   ? 76.209 50.523 -75.547 1.00 46.78 ? 1024 HOH B O   1 
HETATM 8295 O O   . HOH F 3 .   ? 75.460 21.787 -49.109 1.00 11.51 ? 1025 HOH B O   1 
HETATM 8296 O O   . HOH F 3 .   ? 54.939 23.495 -44.564 1.00 37.25 ? 1026 HOH B O   1 
HETATM 8297 O O   . HOH F 3 .   ? 91.474 15.577 -61.431 1.00 39.16 ? 1027 HOH B O   1 
HETATM 8298 O O   . HOH F 3 .   ? 83.994 32.804 -31.019 1.00 42.25 ? 1028 HOH B O   1 
HETATM 8299 O O   . HOH F 3 .   ? 73.509 5.722  -36.364 1.00 45.48 ? 1029 HOH B O   1 
HETATM 8300 O O   . HOH F 3 .   ? 68.000 9.602  -70.309 1.00 32.43 ? 1030 HOH B O   1 
HETATM 8301 O O   . HOH F 3 .   ? 51.115 15.591 -59.667 1.00 48.51 ? 1031 HOH B O   1 
HETATM 8302 O O   . HOH F 3 .   ? 82.795 50.799 -55.665 1.00 41.47 ? 1032 HOH B O   1 
HETATM 8303 O O   . HOH F 3 .   ? 86.259 33.975 -31.011 1.00 30.00 ? 1033 HOH B O   1 
HETATM 8304 O O   . HOH F 3 .   ? 53.178 19.534 -57.122 1.00 33.74 ? 1034 HOH B O   1 
HETATM 8305 O O   . HOH F 3 .   ? 49.081 38.886 -54.725 1.00 32.66 ? 1035 HOH B O   1 
HETATM 8306 O O   . HOH F 3 .   ? 95.154 25.798 -70.593 1.00 33.89 ? 1036 HOH B O   1 
HETATM 8307 O O   . HOH F 3 .   ? 47.572 38.016 -65.116 1.00 35.58 ? 1037 HOH B O   1 
HETATM 8308 O O   . HOH F 3 .   ? 49.846 28.987 -74.171 1.00 43.76 ? 1038 HOH B O   1 
HETATM 8309 O O   . HOH F 3 .   ? 92.172 12.763 -61.530 1.00 41.95 ? 1039 HOH B O   1 
HETATM 8310 O O   . HOH F 3 .   ? 61.416 17.244 -77.917 1.00 22.73 ? 1040 HOH B O   1 
HETATM 8311 O O   . HOH F 3 .   ? 52.597 40.500 -80.667 1.00 25.35 ? 1041 HOH B O   1 
HETATM 8312 O O   . HOH F 3 .   ? 89.933 13.032 -64.814 1.00 32.88 ? 1042 HOH B O   1 
HETATM 8313 O O   . HOH F 3 .   ? 60.124 54.186 -55.728 1.00 42.98 ? 1043 HOH B O   1 
HETATM 8314 O O   . HOH F 3 .   ? 82.351 36.013 -75.306 1.00 42.59 ? 1044 HOH B O   1 
HETATM 8315 O O   . HOH F 3 .   ? 66.859 55.149 -60.701 1.00 35.89 ? 1045 HOH B O   1 
HETATM 8316 O O   . HOH F 3 .   ? 48.279 36.809 -52.541 1.00 48.80 ? 1046 HOH B O   1 
HETATM 8317 O O   . HOH F 3 .   ? 61.498 14.249 -77.604 1.00 32.75 ? 1047 HOH B O   1 
HETATM 8318 O O   . HOH F 3 .   ? 87.671 42.443 -69.832 1.00 28.30 ? 1048 HOH B O   1 
HETATM 8319 O O   . HOH F 3 .   ? 48.868 31.139 -75.162 1.00 30.00 ? 1049 HOH B O   1 
HETATM 8320 O O   . HOH F 3 .   ? 66.487 16.304 -82.958 1.00 42.91 ? 1050 HOH B O   1 
HETATM 8321 O O   . HOH F 3 .   ? 93.524 28.835 -71.916 1.00 38.43 ? 1051 HOH B O   1 
HETATM 8322 O O   . HOH F 3 .   ? 72.082 14.917 -31.743 1.00 34.21 ? 1052 HOH B O   1 
HETATM 8323 O O   . HOH F 3 .   ? 70.095 40.884 -87.767 1.00 40.32 ? 1053 HOH B O   1 
HETATM 8324 O O   . HOH F 3 .   ? 84.090 11.517 -40.416 1.00 41.17 ? 1054 HOH B O   1 
HETATM 8325 O O   . HOH F 3 .   ? 67.149 34.071 -54.981 1.00 27.08 ? 1055 HOH B O   1 
HETATM 8326 O O   . HOH F 3 .   ? 54.693 18.416 -35.154 1.00 34.85 ? 1056 HOH B O   1 
HETATM 8327 O O   . HOH F 3 .   ? 91.795 26.925 -48.798 1.00 28.60 ? 1057 HOH B O   1 
HETATM 8328 O O   . HOH F 3 .   ? 44.237 42.608 -54.923 1.00 35.03 ? 1058 HOH B O   1 
HETATM 8329 O O   . HOH F 3 .   ? 89.439 26.912 -38.570 1.00 41.57 ? 1059 HOH B O   1 
HETATM 8330 O O   . HOH F 3 .   ? 96.885 25.829 -66.490 1.00 36.33 ? 1060 HOH B O   1 
HETATM 8331 O O   . HOH F 3 .   ? 91.132 14.393 -52.673 1.00 32.09 ? 1061 HOH B O   1 
HETATM 8332 O O   . HOH F 3 .   ? 62.047 32.696 -49.537 1.00 29.88 ? 1062 HOH B O   1 
HETATM 8333 O O   . HOH F 3 .   ? 62.408 18.067 -81.853 1.00 37.55 ? 1063 HOH B O   1 
HETATM 8334 O O   . HOH F 3 .   ? 67.550 40.991 -79.341 1.00 33.98 ? 1064 HOH B O   1 
HETATM 8335 O O   . HOH F 3 .   ? 70.993 7.426  -59.403 1.00 22.07 ? 1065 HOH B O   1 
HETATM 8336 O O   . HOH F 3 .   ? 86.002 12.194 -71.122 1.00 35.38 ? 1066 HOH B O   1 
HETATM 8337 O O   . HOH F 3 .   ? 92.043 13.547 -66.902 1.00 44.99 ? 1067 HOH B O   1 
HETATM 8338 O O   . HOH F 3 .   ? 93.598 29.698 -69.329 1.00 36.99 ? 1068 HOH B O   1 
HETATM 8339 O O   . HOH F 3 .   ? 99.543 22.293 -66.586 1.00 30.91 ? 1069 HOH B O   1 
HETATM 8340 O O   . HOH F 3 .   ? 84.061 5.128  -53.548 1.00 36.62 ? 1070 HOH B O   1 
HETATM 8341 O O   . HOH F 3 .   ? 90.984 41.595 -57.450 1.00 40.00 ? 1071 HOH B O   1 
HETATM 8342 O O   . HOH F 3 .   ? 71.414 6.146  -62.029 1.00 37.72 ? 1072 HOH B O   1 
HETATM 8343 O O   . HOH F 3 .   ? 93.019 40.061 -53.610 1.00 30.00 ? 1073 HOH B O   1 
HETATM 8344 O O   . HOH F 3 .   ? 77.723 6.284  -51.285 1.00 24.58 ? 1074 HOH B O   1 
HETATM 8345 O O   . HOH F 3 .   ? 69.948 9.383  -62.968 1.00 18.56 ? 1075 HOH B O   1 
HETATM 8346 O O   . HOH F 3 .   ? 58.894 58.699 -71.295 1.00 30.13 ? 1076 HOH B O   1 
HETATM 8347 O O   . HOH F 3 .   ? 97.249 21.398 -72.179 1.00 37.74 ? 1077 HOH B O   1 
HETATM 8348 O O   . HOH F 3 .   ? 63.709 57.856 -66.783 1.00 34.80 ? 1078 HOH B O   1 
HETATM 8349 O O   . HOH F 3 .   ? 87.688 40.198 -71.475 1.00 45.35 ? 1079 HOH B O   1 
HETATM 8350 O O   . HOH F 3 .   ? 80.669 2.784  -56.277 1.00 34.47 ? 1080 HOH B O   1 
HETATM 8351 O O   . HOH F 3 .   ? 62.364 55.909 -65.523 1.00 30.12 ? 1081 HOH B O   1 
HETATM 8352 O O   . HOH F 3 .   ? 83.683 31.704 -77.880 1.00 38.42 ? 1082 HOH B O   1 
HETATM 8353 O O   . HOH F 3 .   ? 83.342 14.851 -36.569 1.00 45.13 ? 1083 HOH B O   1 
HETATM 8354 O O   . HOH F 3 .   ? 85.047 22.877 -37.233 1.00 42.94 ? 1084 HOH B O   1 
HETATM 8355 O O   . HOH F 3 .   ? 57.392 11.516 -49.582 1.00 34.19 ? 1085 HOH B O   1 
HETATM 8356 O O   . HOH F 3 .   ? 77.550 47.844 -74.960 1.00 38.01 ? 1086 HOH B O   1 
HETATM 8357 O O   . HOH F 3 .   ? 74.888 53.937 -54.176 1.00 34.62 ? 1087 HOH B O   1 
HETATM 8358 O O   . HOH F 3 .   ? 59.510 59.028 -67.419 1.00 31.01 ? 1088 HOH B O   1 
HETATM 8359 O O   . HOH F 3 .   ? 57.179 19.404 -78.053 1.00 33.66 ? 1089 HOH B O   1 
HETATM 8360 O O   . HOH F 3 .   ? 68.190 9.034  -67.323 1.00 29.38 ? 1090 HOH B O   1 
HETATM 8361 O O   . HOH F 3 .   ? 98.730 22.469 -63.604 1.00 26.91 ? 1091 HOH B O   1 
HETATM 8362 O O   . HOH F 3 .   ? 56.856 56.427 -77.337 1.00 33.68 ? 1092 HOH B O   1 
HETATM 8363 O O   . HOH F 3 .   ? 84.235 19.578 -41.142 1.00 31.31 ? 1093 HOH B O   1 
HETATM 8364 O O   . HOH F 3 .   ? 53.686 25.592 -74.106 1.00 25.14 ? 1094 HOH B O   1 
HETATM 8365 O O   . HOH F 3 .   ? 69.655 54.448 -60.469 1.00 23.68 ? 1095 HOH B O   1 
HETATM 8366 O O   . HOH F 3 .   ? 80.475 34.374 -76.263 1.00 48.43 ? 1096 HOH B O   1 
HETATM 8367 O O   . HOH F 3 .   ? 85.678 35.695 -73.438 1.00 40.23 ? 1097 HOH B O   1 
HETATM 8368 O O   . HOH F 3 .   ? 93.771 28.565 -67.163 1.00 26.88 ? 1098 HOH B O   1 
HETATM 8369 O O   . HOH F 3 .   ? 96.864 32.587 -38.582 1.00 16.03 ? 1099 HOH B O   1 
HETATM 8370 O O   . HOH F 3 .   ? 64.260 50.325 -38.894 1.00 41.44 ? 1100 HOH B O   1 
HETATM 8371 O O   . HOH F 3 .   ? 63.673 30.210 -49.417 1.00 25.09 ? 1101 HOH B O   1 
HETATM 8372 O O   . HOH F 3 .   ? 71.043 8.118  -75.940 1.00 40.52 ? 1102 HOH B O   1 
HETATM 8373 O O   . HOH F 3 .   ? 64.113 9.872  -48.200 1.00 24.87 ? 1103 HOH B O   1 
HETATM 8374 O O   . HOH F 3 .   ? 61.895 52.738 -79.928 1.00 37.12 ? 1104 HOH B O   1 
HETATM 8375 O O   . HOH F 3 .   ? 93.689 19.871 -59.931 1.00 40.45 ? 1105 HOH B O   1 
HETATM 8376 O O   . HOH F 3 .   ? 67.844 46.336 -36.105 1.00 39.61 ? 1106 HOH B O   1 
HETATM 8377 O O   . HOH F 3 .   ? 56.910 51.612 -79.682 1.00 38.20 ? 1107 HOH B O   1 
HETATM 8378 O O   . HOH F 3 .   ? 58.073 54.607 -79.564 1.00 40.81 ? 1108 HOH B O   1 
HETATM 8379 O O   . HOH F 3 .   ? 67.745 49.708 -37.025 1.00 42.40 ? 1109 HOH B O   1 
HETATM 8380 O O   . HOH F 3 .   ? 56.813 27.453 -39.524 1.00 45.53 ? 1110 HOH B O   1 
HETATM 8381 O O   . HOH F 3 .   ? 79.091 36.004 -83.480 1.00 46.13 ? 1111 HOH B O   1 
HETATM 8382 O O   . HOH F 3 .   ? 94.197 29.086 -39.767 1.00 27.90 ? 1112 HOH B O   1 
HETATM 8383 O O   . HOH F 3 .   ? 64.918 47.399 -36.407 1.00 32.94 ? 1113 HOH B O   1 
HETATM 8384 O O   . HOH F 3 .   ? 59.215 18.499 -79.834 1.00 52.63 ? 1114 HOH B O   1 
HETATM 8385 O O   . HOH F 3 .   ? 75.133 55.671 -37.435 1.00 30.00 ? 1115 HOH B O   1 
HETATM 8386 O O   . HOH F 3 .   ? 91.706 20.275 -51.460 1.00 38.55 ? 1116 HOH B O   1 
HETATM 8387 O O   . HOH F 3 .   ? 52.130 30.129 -74.909 1.00 37.04 ? 1117 HOH B O   1 
HETATM 8388 O O   . HOH F 3 .   ? 76.455 53.494 -56.157 1.00 38.61 ? 1118 HOH B O   1 
HETATM 8389 O O   . HOH F 3 .   ? 62.667 33.848 -40.371 1.00 42.83 ? 1119 HOH B O   1 
HETATM 8390 O O   . HOH F 3 .   ? 68.441 35.433 -53.320 1.00 37.62 ? 1120 HOH B O   1 
HETATM 8391 O O   . HOH F 3 .   ? 68.892 50.822 -39.430 1.00 37.57 ? 1121 HOH B O   1 
HETATM 8392 O O   . HOH F 3 .   ? 67.431 53.114 -43.757 1.00 42.06 ? 1122 HOH B O   1 
HETATM 8393 O O   . HOH F 3 .   ? 77.850 4.530  -53.261 1.00 34.26 ? 1123 HOH B O   1 
HETATM 8394 O O   . HOH F 3 .   ? 51.418 21.601 -56.518 1.00 39.45 ? 1124 HOH B O   1 
HETATM 8395 O O   . HOH F 3 .   ? 85.300 1.924  -63.374 1.00 49.60 ? 1125 HOH B O   1 
HETATM 8396 O O   . HOH F 3 .   ? 81.999 35.270 -28.686 1.00 38.83 ? 1126 HOH B O   1 
HETATM 8397 O O   . HOH F 3 .   ? 44.934 16.335 -60.497 1.00 45.69 ? 1127 HOH B O   1 
HETATM 8398 O O   . HOH F 3 .   ? 94.017 21.944 -50.217 1.00 40.34 ? 1128 HOH B O   1 
HETATM 8399 O O   . HOH F 3 .   ? 82.382 8.311  -35.511 1.00 45.29 ? 1129 HOH B O   1 
HETATM 8400 O O   . HOH F 3 .   ? 44.345 17.169 -58.090 1.00 45.42 ? 1130 HOH B O   1 
HETATM 8401 O O   . HOH F 3 .   ? 89.483 26.768 -27.037 1.00 30.00 ? 1131 HOH B O   1 
# 
